LOCUS       NP_001307511             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307511
VERSION     NP_001307511.1
DBSOURCE    REFSEQ: accession NM_001320582.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA238657.1, DB062061.1, BC000978.2 and BC110855.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3229777.1,
                                           SRR14038193.2620743.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320582.2:397..2727"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001307509             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307509 XP_005265305
VERSION     NP_001307509.1
DBSOURCE    REFSEQ: accession NM_001320580.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA238657.1, AK292536.1, BC000978.2 and BC110855.1.
            
            On Mar 1, 2016 this sequence version replaced XP_005265305.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4481813.1, AK292536.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320580.2:438..2768"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001307513             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307513
VERSION     NP_001307513.1
DBSOURCE    REFSEQ: accession NM_001320584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135506.3, DA388875.1, BC000978.2 and BC110855.1.
            
            Transcript Variant: This variant (7) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.19363.1,
                                           SRR1660809.209188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320584.1:59..2389"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_942581                776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_942581
VERSION     NP_942581.1
DBSOURCE    REFSEQ: accession NM_198880.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA241522.1, AW673597.1, AK074313.1, BC000978.2, AK025013.1 and
            BC110855.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110855.1, SRR1803617.155379.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395443.7/ ENSP00000378830.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_198880.3:182..2512"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_060200                776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_060200
VERSION     NP_060200.2
DBSOURCE    REFSEQ: accession NM_017730.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA241522.1, AK074313.1, BC000978.2, AK025013.1 and BC110855.1.
            
            On Dec 1, 2003 this sequence version replaced NP_060200.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.4325054.1, AK074313.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_017730.4:242..2572"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001307512             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307512 XP_006713275
VERSION     NP_001307512.1
DBSOURCE    REFSEQ: accession NM_001320583.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA238657.1, DB062828.1, BC000978.2 and BC110855.1.
            
            On Mar 1, 2016 this sequence version replaced XP_006713275.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1540139.1,
                                           SRR11853563.22770.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320583.2:378..2708"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001307514             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307514
VERSION     NP_001307514.1
DBSOURCE    REFSEQ: accession NM_001320585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135506.3, HY006215.1, BC000978.2 and BC110855.1.
            
            Transcript Variant: This variant (8) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC110855.1, SRR1803614.161816.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320585.1:259..2589"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001307510             776 aa            linear   PRI 19-NOV-2025
DEFINITION  transcriptional regulator QRICH1 [Homo sapiens].
ACCESSION   NP_001307510 XP_011532164
VERSION     NP_001307510.1
DBSOURCE    REFSEQ: accession NM_001320581.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Zhao,J., Kang,M., Li,H., Rong,L., Wang,Y., Xue,Y., Yao,Y. and
            Fang,Y.
  TITLE     QRICH1 suppresses pediatric T-cell acute lymphoblastic leukemia by
            inhibiting GRP78
  JOURNAL   Cell Death Dis 15 (9), 646 (2024)
   PUBMED   39227586
  REMARK    GeneRIF: QRICH1 suppresses pediatric T-cell acute lymphoblastic
            leukemia by inhibiting GRP78.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Baruch,Y., Horn-Saban,S., Plotsky,Y., Bercovich,D. and
            Gershoni-Baruch,R.
  TITLE     A case of Ververi-Brady syndrome due to QRICH1 loss of function and
            the literature review
  JOURNAL   Am J Med Genet A 185 (6), 1913-1917 (2021)
   PUBMED   33738978
  REMARK    GeneRIF: A case of Ververi-Brady syndrome due to QRICH1 loss of
            function and the literature review.
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 776)
  AUTHORS   You,K., Wang,L., Chou,C.H., Liu,K., Nakata,T., Jaiswal,A., Yao,J.,
            Lefkovith,A., Omar,A., Perrigoue,J.G., Towne,J.E., Regev,A.,
            Graham,D.B. and Xavier,R.J.
  TITLE     QRICH1 dictates the outcome of ER stress through transcriptional
            control of proteostasis
  JOURNAL   Science 371 (6524) (2021)
   PUBMED   33384352
  REMARK    GeneRIF: QRICH1 dictates the outcome of ER stress through
            transcriptional control of proteostasis.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Fohrenbach,M., Jamra,R.A., Borkhardt,A., Brozou,T., Muschke,P.,
            Popp,B., Rey,L.K., Schaper,J., Surowy,H., Zenker,M., Zweier,C.,
            Wieczorek,D. and Redler,S.
  TITLE     QRICH1 variants in Ververi-Brady syndrome-delineation of the
            genotypic and phenotypic spectrum
  JOURNAL   Clin Genet 99 (1), 199-207 (2021)
   PUBMED   33009816
  REMARK    GeneRIF: QRICH1 variants in Ververi-Brady syndrome-delineation of
            the genotypic and phenotypic spectrum.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Ververi,A., Splitt,M., Dean,J.C.S. and Brady,A.F.
  CONSRTM   DDD Study
  TITLE     Phenotypic spectrum associated with de novo mutations in QRICH1
            gene
  JOURNAL   Clin Genet 93 (2), 286-292 (2018)
   PUBMED   28692176
  REMARK    GeneRIF: Despite their small number, the patients had a relatively
            consistent pattern of clinical features suggesting the presence of
            a QRICH1-associated phenotype. LoF mutations in QRICH1 are
            suggested as a novel cause of developmental delay.
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lakshmana,M.K., Araki,W. and Tabira,T.
  TITLE     Amyloid beta peptide binds a novel death-inducing protein, AB-DIP
  JOURNAL   FASEB J 19 (10), 1362-1364 (2005)
   PUBMED   15923395
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA238657.1, DB062422.1, BC000978.2 and BC110855.1.
            
            On Mar 1, 2016 this sequence version replaced XP_011532164.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-8 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2081656.1,
                                           SRR11853564.19209.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..776
                     /product="transcriptional regulator QRICH1"
                     /note="glutamine-rich protein 1"
                     /calculated_mol_wt=86305
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          <6..>45
                     /region_name="CARD"
                     /note="Caspase activation and recruitment domain: a
                     protein-protein interaction domain; cd01671"
                     /db_xref="CDD:260018"
     Region          139..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          218..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          419..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q2TAL8.1)"
     Region          599..759
                     /region_name="DUF3504"
                     /note="Domain of unknown function (DUF3504); pfam12012"
                     /db_xref="CDD:463430"
     CDS             1..776
                     /gene="QRICH1"
                     /gene_synonym="AB-DIP; VERBRAS; VERBRAS1"
                     /coded_by="NM_001320581.2:457..2787"
                     /db_xref="CCDS:CCDS2787.1"
                     /db_xref="GeneID:54870"
                     /db_xref="HGNC:HGNC:24713"
                     /db_xref="MIM:617387"
ORIGIN      
        1 mnnslentis feeyirvkar svpqhrmkef ldslaskgpe alqefqqtat ttmvyqqggn
       61 ciytdsteva gsllelacpv ttsvqpqtqq eqqiqvqqpq qvqvqvqvqq spqqvsaqls
      121 pqltvhqpte qpiqvqvqiq gqapqsaaps iqtpslqsps psqlqaaqiq vqhvqaaqqi
      181 qaaeipeehi phqqiqaqlv agqslaggqq iqiqtvgals pppsqqgspr egerrvgtas
      241 vlqpvkkrkv dmpitvsyai sgqpvatvla ipqgqqqsyv slrpdlltvd sahlysatgt
      301 itsptgetwt ipvysaqprg dpqqqsithi aipqeaynav hvsgsptala avkleddkek
      361 mvgttsvvkn sheevvqtla nslfpaqfmn gnihipvavq avagtyqnta qtvhiwdpqq
      421 qpqqqtpqeq tpppqqqqqq lqvtcsaqtv qvaevepqsq pqpspelllp nslkpeegle
      481 vwknwaqtkn aelekdaqnr lapigrrqll rfqedlissa vaelnyglcl mtrearngeg
      541 epydpdvlyy iflciqkylf engrvddifs dlyyvrftew lhevlkdvqp rvtplgyvlp
      601 shvteemlwe ckqlgahsps tllttlmffn tkyfllktvd qhmklafskv lrqtkknpsn
      661 pkdkstsiry lkalgihqtg qkvtddmyae qtenpenplr cpiklydfyl fkcpqsvkgr
      721 ndtfyltpep vvapnspiwy svqpisreqm gqmltrilvi reiqeaiava nastmh
//
LOCUS       NP_001266280             329 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA exonuclease 4 isoform 4 [Homo sapiens].
ACCESSION   NP_001266280
VERSION     NP_001266280.1
DBSOURCE    REFSEQ: accession NM_001279351.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Krishnamurthy,N., Ngam,C.R., Berdis,A.J. and Montano,M.M.
  TITLE     The exonuclease activity of hPMC2 is required for transcriptional
            regulation of the QR gene and repair of estrogen-induced abasic
            sites
  JOURNAL   Oncogene 30 (47), 4731-4739 (2011)
   PUBMED   21602889
  REMARK    GeneRIF: determined that the catalytic activity of hPMC2 is
            required for repair of abasic sites that result from
            estrogen-induced DNA damage
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Montano,M.M., Wittmann,B.M. and Bianco,N.R.
  TITLE     Identification and characterization of a novel factor that
            regulates quinone reductase gene transcriptional activity
  JOURNAL   J Biol Chem 275 (44), 34306-34313 (2000)
   PUBMED   10908561
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Kwiatkowska,J., Slomski,R., Jozwiak,S., Short,M.P. and
            Kwiatkowski,D.J.
  TITLE     Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and
            evaluation as TSC1
  JOURNAL   Genomics 44 (3), 350-354 (1997)
   PUBMED   9325058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK295982.1, BC009274.2, AL136894.1 and BM984937.1.
            
            Transcript Variant: This variant (4) differs in the 5' exon and
            initiates translation at a downstream in-frame start codon,
            compared to variant 1. The encoded isoform (4) has a shorter
            N-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295982.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..329
                     /product="RNA exonuclease 4 isoform 4"
                     /note="Xenopus prevents mitotic catastrophe 2 homolog;
                     REX4 homolog, 3'-5' exonuclease; exonuclease XPMC2; XPMC2
                     prevents mitotic catastrophe 2 homolog; REX4, RNA
                     exonuclease 4 homolog"
                     /calculated_mol_wt=36249
     Region          151..301
                     /region_name="REX4_like"
                     /note="DEDDh 3'-5' exonuclease domain of RNA exonuclease
                     4, XPMC2, Interferon Stimulated Gene product of 20 kDa,
                     and similar proteins; cd06144"
                     /db_xref="CDD:99847"
     Site            order(154..157,159,197,201,233..234,236..238,288,293)
                     /site_type="active"
                     /db_xref="CDD:99847"
     Site            order(154..157,159,197,201,233..234,236..237,288,293)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99847"
     Site            order(154,156,238,288,293)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99847"
     CDS             1..329
                     /gene="REXO4"
                     /gene_synonym="REX4; XPMC2; XPMC2H"
                     /coded_by="NM_001279351.1:215..1204"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:57109"
                     /db_xref="HGNC:HGNC:12820"
                     /db_xref="MIM:602930"
ORIGIN      
        1 mgskkkpkii qqnkketspq vkgeempagk dqeasrgsvp sgskmdrrap vprtkasgte
       61 hnkkgtkert ngdivpergd iehkkrkake aapappteed iwfddvdpad ieaaigpeaa
      121 kiarkqlgqs egsvslslvk eqafggltra laldcemvgv gpkgeesmaa rvsivnqygk
      181 cvydkyvkpt epvtdyrtav sgirpenlkq geelevvqke vaemlkgril vghalhndlk
      241 vlfldhpkkk irdtqkykpf ksqvksgrps lrllsekilg lqvqqaehcs iqdaqaamrl
      301 yvmvkkewes mardrrpllt apdhcsdda
//
LOCUS       NP_001394023             160 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform a [Homo sapiens].
ACCESSION   NP_001394023
VERSION     NP_001394023.1
DBSOURCE    REFSEQ: accession NM_001407094.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.1390310.1,
                                           SRR14038196.2284387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..160
                     /product="protein max isoform a"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=18144
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Region          81..102
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          103..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Region          152..156
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            153
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     CDS             1..160
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407094.1:34..516"
                     /note="isoform a is encoded by transcript variant 12"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqvr alekarssaq lqtnypssdn
      121 slytnakgst isafdggsds ssesepeepq srkklrmeas
//
LOCUS       NP_005300                496 aa            linear   PRI 20-NOV-2025
DEFINITION  alanine aminotransferase 1 [Homo sapiens].
ACCESSION   NP_005300
VERSION     NP_005300.1
DBSOURCE    REFSEQ: accession NM_005309.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Fan,X., Rong,H., Wang,Y., Li,M., Song,W., Su,A. and Yu,T.
  TITLE     The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism
  JOURNAL   BMC Pregnancy Childbirth 24 (1), 26 (2024)
   PUBMED   38172739
  REMARK    GeneRIF: The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhang,C., Xu,Q., Xu,C., Yang,K., Xia,T., Hasi,W., Hao,M. and
            Kuang,H.
  TITLE     Sex Differences in the Association Between AST/ALT and Incidence of
            Type 2 Diabetes in Japanese Patients with Nonalcoholic Fatty Liver
            Disease: A Retrospective Cohort Study
  JOURNAL   Endocr Res 49 (1), 1-11 (2024)
   PUBMED   37752709
  REMARK    GeneRIF: Sex Differences in the Association Between AST/ALT and
            Incidence of Type 2 Diabetes in Japanese Patients with Nonalcoholic
            Fatty Liver Disease: A Retrospective Cohort Study.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Qin,Y.J., Wang,Z.G., Gong,J.H., Gong,J.P. and Li,J.H.
  TITLE     Role of alanine aminotransferase in the effects of urinary caffeine
            concentration and its primary metabolite concentration on cognitive
            function in older adults: Bayesian Kernel Machine regression
            analysis and mediation analysis
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (2), 721-733 (2024)
   PUBMED   38305614
  REMARK    GeneRIF: Role of alanine aminotransferase in the effects of urinary
            caffeine concentration and its primary metabolite concentration on
            cognitive function in older adults: Bayesian Kernel Machine
            regression analysis and mediation analysis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   He,S., Yu,C., Kuang,M., Qiu,J., Yang,R., Zhang,S., Sheng,G. and
            Zou,Y.
  TITLE     Alanine aminotransferase to high- density lipoprotein cholesterol
            ratio is positively correlated with the occurrence of diabetes in
            the Chinese population: a population-based cohort study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1266692 (2023)
   PUBMED   38089616
  REMARK    GeneRIF: Alanine aminotransferase to high- density lipoprotein
            cholesterol ratio is positively correlated with the occurrence of
            diabetes in the Chinese population: a population-based cohort
            study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Asgari,S., Molavizadeh,D., Tohidi,M., Momenan,A.A., Azizi,F. and
            Hadaegh,F.
  TITLE     Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022
  JOURNAL   J Clin Lab Anal 37 (11-12), e24937 (2023)
   PUBMED   37403787
  REMARK    GeneRIF: Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Ishiguro,M., Takio,K., Suzuki,M., Oyama,R., Matsuzawa,T. and
            Titani,K.
  TITLE     Complete amino acid sequence of human liver cytosolic alanine
            aminotransferase (GPT) determined by a combination of conventional
            and mass spectral methods
  JOURNAL   Biochemistry 30 (43), 10451-10457 (1991)
   PUBMED   1931970
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Rocha,J., Amorim,A., Almeida,V.M., Oliveira,J.P., Leao,M.,
            Tavares,M.C., Pereira,M.S. and Vidal-Pinheiro,L.
  TITLE     Gene dosage evidence for the regional assignment of GPT
            (glutamate-pyruvate transaminase; E.C. 2.6.1.2) locus to
            8q24.2----8qter
  JOURNAL   Hum Genet 80 (3), 299-300 (1988)
   PUBMED   3192219
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Astrin,K.H., Arredondo-Vega,F.X., Desnick,R.J. and Smith,M.
  TITLE     Assignment of the gene for cytosolic alanine aminotransferase
            (AAT1) to human chromosome 8
  JOURNAL   Ann Hum Genet 46 (2), 125-133 (1982)
   PUBMED   7114790
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Olaisen,B.
  TITLE     Genetics of the GPT system. Family, mother/child and association
            studies
  JOURNAL   Clin Genet 7 (3), 245-254 (1975)
   PUBMED   49232
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Chen,S.H. and Giblett,E.R.
  TITLE     Polymorphism of soluble glutamic-pyruvic transaminase: a new
            genetic marker in man
  JOURNAL   Science 173 (3992), 148-149 (1971)
   PUBMED   5581908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP275218.1, BT006992.1 and
            AI283141.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes cytosolic alanine aminotransaminase 1
            (ALT1); also known as glutamate-pyruvate transaminase 1. This
            enzyme catalyzes the reversible transamination between alanine and
            2-oxoglutarate to generate pyruvate and glutamate and, therefore,
            plays a key role in the intermediary metabolism of glucose and
            amino acids. Serum activity levels of this enzyme are routinely
            used as a biomarker of liver injury caused by drug toxicity,
            infection, alcohol, and steatosis. A related gene on chromosome 16
            encodes a putative mitochondrial alanine
            aminotransaminase.[provided by RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.911110.1,
                                           SRR1660807.79276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: relevant for disease process
            MANE Ensembl match     :: ENST00000394955.3/ ENSP00000378408.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..496
                     /product="alanine aminotransferase 1"
                     /EC_number="2.6.1.2"
                     /note="glutamic-alanine transaminase 1; glutamic--pyruvic
                     transaminase 1; alanine aminotransferase; glutamate
                     pyruvate transaminase 1; glutamic-pyruvate transaminase
                     (alanine aminotransferase); serum glutamic-pyruvic
                     transaminase; serum glutamate-pyruvate transaminase"
                     /calculated_mol_wt=54506
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1931970; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     Region          17..496
                     /region_name="PTZ00377"
                     /note="alanine aminotransferase; Provisional"
                     /db_xref="CDD:240391"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     CDS             1..496
                     /gene="GPT"
                     /gene_synonym="AAT1; ALT; ALT1; GPT1; SGPT"
                     /coded_by="NM_005309.3:166..1656"
                     /db_xref="CCDS:CCDS6430.1"
                     /db_xref="GeneID:2875"
                     /db_xref="HGNC:HGNC:4552"
                     /db_xref="MIM:138200"
ORIGIN      
        1 masstgdrsq avrhglrakv ltldgmnprv rrveyavrgp ivqraleleq elrqgvkkpf
       61 teviranigd aqamgqrpit flrqvlalcv npdllsspnf pddakkraer ilqacgghsl
      121 gaysvssgiq liredvaryi errdggipad pnnvflstga sdaivtvlkl lvageghtrt
      181 gvlipipqyp lysatlaelg avqvdyylde erawaldvae lhralgqard hcrpralcvi
      241 npgnptgqvq trecieavir fafeerlfll adevyqdnvy aagsqfhsfk kvlmemgppy
      301 agqqelasfh stskgymgec gfrggyvevv nmdaavqqqm lklmsvrlcp pvpgqalldl
      361 vvsppaptdp sfaqfqaekq avlaelaaka klteqvfnea pgiscnpvqg amysfprvql
      421 ppraveraqe lglapdmffc lrlleetgic vvpgsgfgqr egtyhfrmti lppleklrll
      481 leklsrfhak ftleys
//
LOCUS       NP_001341646             451 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-fetoprotein isoform 2 [Homo sapiens].
ACCESSION   NP_001341646
VERSION     NP_001341646.2
DBSOURCE    REFSEQ: accession NM_001354717.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Zhang,Y.F., Lin,S., Zhen,X. and Ho,M.
  TITLE     A proteomic atlas of glypican-3 interacting partners:
            Identification of alpha-fetoprotein and other extracellular
            proteins as potential immunotherapy targets in liver cancer
  JOURNAL   Proteoglycan Res 2 (4) (2024)
   PUBMED   39822733
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Liu,K., Wu,C., Zhu,M., Xu,J., Lin,B., Lin,H., Liu,Z. and Li,M.
  TITLE     Structural characteristics of alpha-fetoprotein, including
            N-glycosylation, metal ion and fatty acid binding sites
  JOURNAL   Commun Biol 7 (1), 505 (2024)
   PUBMED   38678117
  REMARK    GeneRIF: Structural characteristics of alpha-fetoprotein, including
            N-glycosylation, metal ion and fatty acid binding sites.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Yeo,Y.H., Lee,Y.T., Tseng,H.R., Zhu,Y., You,S., Agopian,V.G. and
            Yang,J.D.
  TITLE     Alpha-fetoprotein: Past, present, and future
  JOURNAL   Hepatol Commun 8 (5), e0422 (2024)
   PUBMED   38619448
  REMARK    GeneRIF: Alpha-fetoprotein: Past, present, and future.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Song,H., Wang,J., Zhang,H., Wu,Y., Wang,K., Wang,X. and Xu,X.
  TITLE     Combination of serum alpha-fetoprotein, PIVKA- and glypican-3 in
            diagnosis of hepatocellular carcinoma: a meta-analysis
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 53 (1), 131-139 (2024)
   PUBMED   38310085
  REMARK    GeneRIF: Combination of serum alpha-fetoprotein, PIVKA- and
            glypican-3 in diagnosis of hepatocellular carcinoma: a
            meta-analysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Chaudhuri,A.G., Samanta,S., Dey,M., Raviraja,N.S. and Dey,S.
  TITLE     Role of Alpha-Fetoprotein in the Pathogenesis of Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 43 (2), 57-76 (2024)
   PUBMED   38505913
  REMARK    GeneRIF: Role of Alpha-Fetoprotein in the Pathogenesis of Cancer.
            Review article
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Pucci,P., Siciliano,R., Malorni,A., Marino,G., Tecce,M.F.,
            Ceccarini,C. and Terrana,B.
  TITLE     Human alpha-fetoprotein primary structure: a mass spectrometric
            study
  JOURNAL   Biochemistry 30 (20), 5061-5066 (1991)
   PUBMED   1709810
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     alpha-Fetoprotein as a carrier protein in plasma and its
            bilirubin-binding ability
  JOURNAL   Cancer Res 39 (9), 3571-3574 (1979)
   PUBMED   89900
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     Copper(II)-binding ability of human alpha-fetoprotein
  JOURNAL   Cancer Res 38 (10), 3483-3486 (1978)
   PUBMED   80265
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     Comparative chemical structures of human alpha-fetoproteins from
            fetal serum and from ascites fluid of a patient with hepatoma
  JOURNAL   Cancer Res 37 (10), 3663-3667 (1977)
   PUBMED   71198
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Yachnin,S., Hsu,R., Heinrikson,R.L. and Miller,J.B.
  TITLE     Studies on human alpha-fetoprotein. Isolation and characterization
            of monomeric and polymeric forms and amino-terminal sequence
            analysis
  JOURNAL   Biochim Biophys Acta 493 (2), 418-428 (1977)
   PUBMED   70228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108157.3.
            
            On May 31, 2019 this sequence version replaced NP_001341646.1.
            
            Summary: This gene encodes alpha-fetoprotein, a major plasma
            protein produced by the yolk sac and the liver during fetal life.
            Alpha-fetoprotein expression in adults is often associated with
            hepatocarcinoma and with teratoma, and has prognostic value for
            managing advanced gastric cancer. However, hereditary persistance
            of alpha-fetoprotein may also be found in individuals with no
            obvious pathology. The protein is thought to be the fetal
            counterpart of serum albumin, and the alpha-fetoprotein and albumin
            genes are present in tandem in the same transcriptional orientation
            on chromosome 4. Alpha-fetoprotein is found in monomeric as well as
            dimeric and trimeric forms, and binds copper, nickel, fatty acids
            and bilirubin. The level of alpha-fetoprotein in amniotic fluid is
            used to measure renal loss of protein to screen for spina bifida
            and anencephaly. [provided by RefSeq, Oct 2019].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297674.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267750,
                                           SAMN03267752 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..451
                     /product="alpha-fetoprotein isoform 2"
                     /note="alpha-fetoglobulin; alpha-1-fetoprotein"
                     /calculated_mol_wt=50597
     Region          <1..50
                     /region_name="ALBUMIN"
                     /note="Albumin domain, contains five or six internal
                     disulphide bonds; albuminoid superfamily includes
                     alpha-fetoprotein which binds various cations, fatty acids
                     and bilirubin; vitamin D-binding protein which binds to
                     vitamin D, its metabolites, and fatty acids; cl00031"
                     /db_xref="CDD:469585"
     Site            order(1,4..5,8,24,27)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Region          54..238
                     /region_name="ALBUMIN"
                     /note="serum albumin; smart00103"
                     /db_xref="CDD:214517"
     Site            order(85,89,104,123,127,130,153,156..157)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Site            order(193,196..197,200,216,219)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Region          246..436
                     /region_name="ALBUMIN"
                     /note="serum albumin; smart00103"
                     /db_xref="CDD:214517"
     Site            order(277,281,296,319,323,326,351,354..355)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Site            order(391,394..395,398,414,417)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     CDS             1..451
                     /gene="AFP"
                     /gene_synonym="AFPD; FETA; HPAFP"
                     /coded_by="NM_001354717.2:375..1730"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:174"
                     /db_xref="HGNC:HGNC:317"
                     /db_xref="MIM:104150"
ORIGIN      
        1 mnkfiyeiar rhpflyapti llwaarydki ipscckaena vecfqtkaat vtkelressl
       61 lnqhacavmk nfgtrtfqai tvtklsqkft kvnfteiqkl vldvahvheh ccrgdvldcl
      121 qdgekimsyi csqqdtlsnk iteccklttl ergqciihae ndekpeglsp nlnrflgdrd
      181 fnqfssgekn iflasfvhey srrhpqlavs vilrvakgyq ellekcfqte nplecqdkge
      241 eelqkyiqes qalakrscgl fqklgeyylq naflvaytkk apqltsselm aitrkmaata
      301 atccqlsedk llacgegaad iiighlcirh emtpvnpgvg qcctssyanr rpcfsslvvd
      361 etyvppafsd dkfifhkdlc qaqgvalqtm kqeflinlvk qkpqiteeql eaviadfsgl
      421 lekccqgqeq evcfaeegqk lisktraalg v
//
LOCUS       NP_001316667             150 aa            linear   PRI 20-NOV-2025
DEFINITION  telomerase RNA component interacting RNase isoform 2 [Homo
            sapiens].
ACCESSION   NP_001316667
VERSION     NP_001316667.1
DBSOURCE    REFSEQ: accession NM_001329738.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Xie,J., Chen,Z., Zhang,X., Chen,H. and Guan,W.
  TITLE     Identification of an RNase that preferentially cleaves A/G
            nucleotides
  JOURNAL   Sci Rep 7, 45207 (2017)
   PUBMED   28322335
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ668685.1, BU599327.1 and BC000216.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU599327.1, ERR3218368.947155.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..150
                     /product="telomerase RNA component interacting RNase
                     isoform 2"
                     /note="uncharacterized protein C19orf43; My029 protein;
                     exoribonuclease TRIR"
                     /calculated_mol_wt=15481
     CDS             1..150
                     /gene="TRIR"
                     /gene_synonym="C19orf43; fSAP18; TERCIR"
                     /coded_by="NM_001329738.2:28..480"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86709.1"
                     /db_xref="GeneID:79002"
                     /db_xref="HGNC:HGNC:28424"
                     /db_xref="MIM:621422"
ORIGIN      
        1 maargrraep qgreapgpag gggggsrwae sgsgtspesg deevsgagss pvsggvnlfa
       61 ndgsflelfk rkmeeeqrqr qeepppgpqr pdqsaaaagp gdpkrkggpg stlsfvltsk
      121 gdawakymae vkkykahqcg dddktrplvk
//
LOCUS       NP_001275763             625 aa            linear   PRI 20-NOV-2025
DEFINITION  uncharacterized protein C19orf44 isoform 2 [Homo sapiens].
ACCESSION   NP_001275763
VERSION     NP_001275763.1
DBSOURCE    REFSEQ: accession NM_001288834.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Sroka,T.J., Sanwald,L.K., Prasai,A., Hoeren,J., Trivigno,V.,
            Chaumet,V., Krauss,L.M., Weber,D., Yildiz,D., von der Malsburg,K.,
            Walentek,P., Haberkant,P., Schrul,B., Feistel,K. and Mick,D.U.
  TITLE     An enzymatic cascade enables sensitive and specific proximity
            labeling proteomics in challenging biological systems
  JOURNAL   Nat Commun 16 (1), 9691 (2025)
   PUBMED   41184298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Hussain,H.M.J., Meng,W., Li,Y., Firasat,S., Pennesi,M.E.,
            Gorin,M.B., Guan,B., Clark,R.L., Fale-Olsen,E., Al Rawi,R.,
            Agather,A., Huryn,L.A., Yang,P., Matynia,A. and Chen,R.
  TITLE     Biallelic loss-of-function variants in C19orf44 lead to retinal
            degeneration
  JOURNAL   J Med Genet 62 (11), 693-699 (2025)
   PUBMED   40744518
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Ehrenberg,M., Avraham,M., Asodu,S.S., Moye,A.R., Sangermano,R.,
            Rizel,L., Ali-Nasser,T., Sher,I., Gurwitz,D., Chao,K.R., Rivera,A.,
            Webster,A.R., Rivolta,C., Newman,H., Pras,E., Rotenstreich,Y.,
            Banin,E., Pierce,E.A., Zur,D., Arno,G., Bujakowska,K.M., Lin,S.,
            Sharon,D. and Ben-Yosef,T.
  TITLE     Biallelic null variants in C19orf44 cause a unique late-onset
            retinal dystrophy phenotype characterized by patchy perifoveal
            chorioretinal atrophy
  JOURNAL   Genet Med 27 (6), 101401 (2025)
   PUBMED   40079362
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008764.9.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and has
            multiple coding region differences, compared to variant 1. The
            resulting isoform (2) has a shorter C-terminus, compared to isoform
            1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..625
                     /product="uncharacterized protein C19orf44 isoform 2"
                     /note="uncharacterized protein C19orf44"
                     /calculated_mol_wt=68120
     Region          <139..515
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          474..609
                     /region_name="DUF4614"
                     /note="Domain of unknown function (DUF4614); pfam15391"
                     /db_xref="CDD:464698"
     CDS             1..625
                     /gene="C19orf44"
                     /gene_synonym="FCAP71"
                     /coded_by="NM_001288834.2:74..1951"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74306.1"
                     /db_xref="GeneID:84167"
                     /db_xref="HGNC:HGNC:26141"
                     /db_xref="MIM:621208"
ORIGIN      
        1 masarkasrp mrdvfgdfsd vsledstmee irnfqisrnl tkiapghsrf lkrnqtldek
       61 hlllkenpvl gsgprlascr ppttasrira naalmklaql etrimnrklq rnlsdtesds
      121 mtadaglpkr adrilsggal elasqntdkt sqnqarelpv tennaqnakv srflkkkqap
      181 venispeapa gkertlqtpk qkepartfds pdsdeeemkv llgslmdssr ekntnqgfss
      241 anvseeeerk lfsvpsqlra ftvpsvelss akpsqtshlp tslaadrtlh strsradypq
      301 shvssdtash tpsvsitgaf snsvslkmgh vklvsspgrs eaetvdepvs egaddsldef
      361 rinilsldgl apavsensdl eqeeesaqrq ktagkifrae astgqdaprq aqarswasqg
      421 kaasaegdes evsehlsass asaiqqdsts smqppseapm vntvssayse dfenspslta
      481 septahskes ldrtldalse ssssvktdlp qtaesrkksg rhvtrvlvkd tavqtpdpaf
      541 tyewtkalta yspavlalhd vlkqqlsltq qfiqasrhlh asllrsldad sfhyhtleea
      601 keyirchrpa pltmedalee vnkel
//
LOCUS       NP_071881                651 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 5 [Homo sapiens].
ACCESSION   NP_071881
VERSION     NP_071881.1
DBSOURCE    REFSEQ: accession NM_022436.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Zhang,L., Zhang,S., Zou,W., Hu,Y., Gao,Y., Zhang,J. and Zheng,J.
  TITLE     Maternal high-fat diet regulates offspring hepatic ABCG5 expression
            and cholesterol metabolism via the gut microbiota and its derived
            butyrate
  JOURNAL   Clin Sci (Lond) 138 (17), 1039-1054 (2024)
   PUBMED   39136693
  REMARK    GeneRIF: Maternal high-fat diet regulates offspring hepatic ABCG5
            expression and cholesterol metabolism via the gut microbiota and
            its derived butyrate.
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Khabou,B., Kallabi,F., Abdelaziz,R.B., Maaloul,I., Aloulou,H.,
            Chehida,A.B., Kammoun,T., Barbu,V., Boudawara,T.S., Fakhfakh,F.,
            Khemakhem,B. and Sahnoun,O.S.
  TITLE     Molecular and computational characterization of ABCB11 and ABCG5
            variants in Tunisian patients with neonatal/infantile low-GGT
            intrahepatic cholestasis: Genetic diagnosis and genotype-phenotype
            correlation assessment
  JOURNAL   Ann Hum Genet 88 (3), 194-211 (2024)
   PUBMED   38108658
  REMARK    GeneRIF: Molecular and computational characterization of ABCB11 and
            ABCG5 variants in Tunisian patients with neonatal/infantile low-GGT
            intrahepatic cholestasis: Genetic diagnosis and genotype-phenotype
            correlation assessment.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Mi,J., Jiang,Q., Qi,Z., Liu,Z., Bai,X., Zheng,X., Wu,J., Fang,Y.,
            Yang,A. and Chen,H.
  TITLE     Plasma campesterol and ABCG5/ABCG8 gene loci on the risk of
            cholelithiasis and cholecystitis: evidence from Mendelian
            randomization and colocalization analyses
  JOURNAL   Hum Genomics 18 (1), 19 (2024)
   PUBMED   38347599
  REMARK    GeneRIF: Plasma campesterol and ABCG5/ABCG8 gene loci on the risk
            of cholelithiasis and cholecystitis: evidence from Mendelian
            randomization and colocalization analyses.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Tada,H., Okada,H., Nomura,A., Takamura,M. and Kawashiri,M.A.
  TITLE     Children with Severe Hypercholesterolemia Caused by a Pathogenic
            Mutation in ABCG5
  JOURNAL   Intern Med 62 (2), 251-259 (2023)
   PUBMED   35705271
  REMARK    GeneRIF: Children with Severe Hypercholesterolemia Caused by a
            Pathogenic Mutation in ABCG5.
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Farhat,D., Rezaei,F., Ristovski,M., Yang,Y., Stancescu,A.,
            Dzimkova,L., Samnani,S., Couture,J.F. and Lee,J.Y.
  TITLE     Structural Analysis of Cholesterol Binding and Sterol Selectivity
            by ABCG5/G8
  JOURNAL   J Mol Biol 434 (20), 167795 (2022)
   PUBMED   35988751
  REMARK    GeneRIF: Structural Analysis of Cholesterol Binding and Sterol
            Selectivity by ABCG5/G8.
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Lee,M.H., Lu,K., Hazard,S., Yu,H., Shulenin,S., Hidaka,H.,
            Kojima,H., Allikmets,R., Sakuma,N., Pegoraro,R., Srivastava,A.K.,
            Salen,G., Dean,M. and Patel,S.B.
  TITLE     Identification of a gene, ABCG5, important in the regulation of
            dietary cholesterol absorption
  JOURNAL   Nat Genet 27 (1), 79-83 (2001)
   PUBMED   11138003
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Shulenin,S., Schriml,L.M., Remaley,A.T., Fojo,S., Brewer,B.,
            Allikmets,R. and Dean,M.
  TITLE     An ATP-binding cassette gene (ABCG5) from the ABCG (White) gene
            subfamily maps to human chromosome 2p21 in the region of the
            Sitosterolemia locus
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 204-208 (2001)
   PUBMED   11435688
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Berge,K.E., Tian,H., Graf,G.A., Yu,L., Grishin,N.V., Schultz,J.,
            Kwiterovich,P., Shan,B., Barnes,R. and Hobbs,H.H.
  TITLE     Accumulation of dietary cholesterol in sitosterolemia caused by
            mutations in adjacent ABC transporters
  JOURNAL   Science 290 (5497), 1771-1775 (2000)
   PUBMED   11099417
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Patel,S.B., Salen,G., Hidaka,H., Kwiterovich,P.O., Stalenhoef,A.F.,
            Miettinen,T.A., Grundy,S.M., Lee,M.H., Rubenstein,J.S.,
            Polymeropoulos,M.H. and Brownstein,M.J.
  TITLE     Mapping a gene involved in regulating dietary cholesterol
            absorption. The sitosterolemia locus is found at chromosome 2p21
  JOURNAL   J Clin Invest 102 (5), 1041-1044 (1998)
   PUBMED   9727073
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Myrie,S.B., Steiner,R.D. and Mymin,D.
  TITLE     Sitosterolemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556150
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Karyn Megy. The reference sequence was derived
            from AC108476.5 and AF312715.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. The protein encoded by
            this gene functions as a half-transporter to limit intestinal
            absorption and promote biliary excretion of sterols. It is
            expressed in a tissue-specific manner in the liver, colon, and
            intestine. This gene is tandemly arrayed on chromosome 2, in a
            head-to-head orientation with family member ABCG8. Mutations in
            this gene may contribute to sterol accumulation and
            atheroschlerosis, and have been observed in patients with
            sitosterolemia. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF312715.2, AF320293.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000405322.8/ ENSP00000384513.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..651
                     /product="ATP-binding cassette sub-family G member 5"
                     /EC_number="7.6.2.-"
                     /note="sterolin 1; ATP-binding cassette, sub-family G
                     (WHITE), member 5"
                     /calculated_mol_wt=72373
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Region          50..275
                     /region_name="ABCG_White"
                     /note="White pigment protein homolog of ABCG transporter
                     subfamily; cd03234"
                     /db_xref="CDD:213201"
     Region          60..645
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            86..93
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213201"
     Site            order(89..90,92..94,134,217..218,250)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:213201"
     Site            131..134
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213201"
     Site            193..202
                     /site_type="other"
                     /note="ABC transporter signature motif"
                     /db_xref="CDD:213201"
     Site            213..218
                     /site_type="other"
                     /note="Walker B"
                     /db_xref="CDD:213201"
     Site            221..224
                     /site_type="other"
                     /note="D-loop"
                     /db_xref="CDD:213201"
     Site            246..252
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213201"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            422..442
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            468..489
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            501..521
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            529..549
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            584
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            591
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H222.1)"
     Site            624..644
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H222.1)"
     CDS             1..651
                     /gene="ABCG5"
                     /gene_synonym="STSL; STSL2"
                     /coded_by="NM_022436.3:161..2116"
                     /db_xref="CCDS:CCDS1814.1"
                     /db_xref="GeneID:64240"
                     /db_xref="HGNC:HGNC:13886"
                     /db_xref="MIM:605459"
ORIGIN      
        1 mgdlssltpg gsmglqvnrg sqsslegapa tapephslgi lhasysvshr vrpwwditsc
       61 rqqwtrqilk dvslyvesgq imcilgssgs gkttlldams grlgragtfl gevyvngral
      121 rreqfqdcfs yvlqsdtlls sltvretlhy tallairrgn pgsfqkkvea vmaelslshv
      181 adrlignysl ggistgerrr vsiaaqllqd pkvmlfdept tgldcmtanq ivvllvelar
      241 rnrivvltih qprselfqlf dkiailsfge lifcgtpaem ldffndcgyp cpehsnpfdf
      301 ymdltsvdtq skereietsk rvqmiesayk ksaichktlk niermkhlkt lpmvpfktkd
      361 spgvfsklgv llrrvtrnlv rnklavitrl lqnlimglfl lffvlrvrsn vlkgaiqdrv
      421 gllyqfvgat pytgmlnavn lfpvlravsd qesqdglyqk wqmmlayalh vlpfsvvatm
      481 ifssvcywtl glhpevarfg yfsaallaph ligefltlvl lgivqnpniv nsvvallsia
      541 gvlvgsgflr niqempipfk iisyftfqky cseilvvnef yglnftcgss nvsvttnpmc
      601 aftqgiqfie ktcpgatsrf tmnflilysf ipalvilgiv vfkirdhlis r
//
LOCUS       NP_997511                644 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_997511
VERSION     NP_997511.1
DBSOURCE    REFSEQ: accession NM_207628.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF323661.1, BC029158.1 and
            X91249.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (6) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF323661.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMN03267761,
                                           SAMN03465406 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..644
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 6"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=71829
     Region          38..644
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     CDS             1..644
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_207628.1:251..2185"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 mtepksvcvs vdevvssnme atetdllngh lkkvdnnlte aqrfsslprr aavniefrdl
       61 sysvpegpww rkkgyktllk gisgkfnsge lvaimgpsga gkstlmnila gyretgmkga
      121 vlinglprdl rcfrkvscyi mqddmllphl tvqeammvsa hlklqekdeg rremvkeilt
      181 algllscant rtgslsggqr krlaialelv nnppvmffde ptsgldsasc fqvvslmkgl
      241 aqggrsiict ihqpsaklfe lfdqlyvlsq gqcvyrgkvc nlvpylrdlg lncptyhnpa
      301 dfvmevasge ygdqnsrlvr avregmcdsd hkrdlggdae vnpflwhrps eedsssmegc
      361 hsfsascltq fcilfkrtfl simrdsvlth lritshigig lligllylgi gneakkvlsn
      421 sgflffsmlf lmfaalmptv ltfplemgvf lrehlnywys lkayylaktm advpfqimfp
      481 vaycsivywm tsqpsdavrf vlfaalgtmt slvaqslgll igaastslqv atfvgpvtai
      541 pvllfsgffv sfdtiptylq wmsyisyvry gfegvilsiy gldredlhcd idetchfqks
      601 eailreldve naklyldfiv lgiffislrl iayfvlryki raer
//
LOCUS       NP_001369594             496 aa            linear   PRI 20-NOV-2025
DEFINITION  alanine aminotransferase 1 [Homo sapiens].
ACCESSION   NP_001369594
VERSION     NP_001369594.1
DBSOURCE    REFSEQ: accession NM_001382665.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Fan,X., Rong,H., Wang,Y., Li,M., Song,W., Su,A. and Yu,T.
  TITLE     The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism
  JOURNAL   BMC Pregnancy Childbirth 24 (1), 26 (2024)
   PUBMED   38172739
  REMARK    GeneRIF: The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhang,C., Xu,Q., Xu,C., Yang,K., Xia,T., Hasi,W., Hao,M. and
            Kuang,H.
  TITLE     Sex Differences in the Association Between AST/ALT and Incidence of
            Type 2 Diabetes in Japanese Patients with Nonalcoholic Fatty Liver
            Disease: A Retrospective Cohort Study
  JOURNAL   Endocr Res 49 (1), 1-11 (2024)
   PUBMED   37752709
  REMARK    GeneRIF: Sex Differences in the Association Between AST/ALT and
            Incidence of Type 2 Diabetes in Japanese Patients with Nonalcoholic
            Fatty Liver Disease: A Retrospective Cohort Study.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Qin,Y.J., Wang,Z.G., Gong,J.H., Gong,J.P. and Li,J.H.
  TITLE     Role of alanine aminotransferase in the effects of urinary caffeine
            concentration and its primary metabolite concentration on cognitive
            function in older adults: Bayesian Kernel Machine regression
            analysis and mediation analysis
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (2), 721-733 (2024)
   PUBMED   38305614
  REMARK    GeneRIF: Role of alanine aminotransferase in the effects of urinary
            caffeine concentration and its primary metabolite concentration on
            cognitive function in older adults: Bayesian Kernel Machine
            regression analysis and mediation analysis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   He,S., Yu,C., Kuang,M., Qiu,J., Yang,R., Zhang,S., Sheng,G. and
            Zou,Y.
  TITLE     Alanine aminotransferase to high- density lipoprotein cholesterol
            ratio is positively correlated with the occurrence of diabetes in
            the Chinese population: a population-based cohort study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1266692 (2023)
   PUBMED   38089616
  REMARK    GeneRIF: Alanine aminotransferase to high- density lipoprotein
            cholesterol ratio is positively correlated with the occurrence of
            diabetes in the Chinese population: a population-based cohort
            study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Asgari,S., Molavizadeh,D., Tohidi,M., Momenan,A.A., Azizi,F. and
            Hadaegh,F.
  TITLE     Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022
  JOURNAL   J Clin Lab Anal 37 (11-12), e24937 (2023)
   PUBMED   37403787
  REMARK    GeneRIF: Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Ishiguro,M., Takio,K., Suzuki,M., Oyama,R., Matsuzawa,T. and
            Titani,K.
  TITLE     Complete amino acid sequence of human liver cytosolic alanine
            aminotransferase (GPT) determined by a combination of conventional
            and mass spectral methods
  JOURNAL   Biochemistry 30 (43), 10451-10457 (1991)
   PUBMED   1931970
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Rocha,J., Amorim,A., Almeida,V.M., Oliveira,J.P., Leao,M.,
            Tavares,M.C., Pereira,M.S. and Vidal-Pinheiro,L.
  TITLE     Gene dosage evidence for the regional assignment of GPT
            (glutamate-pyruvate transaminase; E.C. 2.6.1.2) locus to
            8q24.2----8qter
  JOURNAL   Hum Genet 80 (3), 299-300 (1988)
   PUBMED   3192219
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Astrin,K.H., Arredondo-Vega,F.X., Desnick,R.J. and Smith,M.
  TITLE     Assignment of the gene for cytosolic alanine aminotransferase
            (AAT1) to human chromosome 8
  JOURNAL   Ann Hum Genet 46 (2), 125-133 (1982)
   PUBMED   7114790
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Olaisen,B.
  TITLE     Genetics of the GPT system. Family, mother/child and association
            studies
  JOURNAL   Clin Genet 7 (3), 245-254 (1975)
   PUBMED   49232
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Chen,S.H. and Giblett,E.R.
  TITLE     Polymorphism of soluble glutamic-pyruvic transaminase: a new
            genetic marker in man
  JOURNAL   Science 173 (3992), 148-149 (1971)
   PUBMED   5581908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084125.9.
            
            Summary: This gene encodes cytosolic alanine aminotransaminase 1
            (ALT1); also known as glutamate-pyruvate transaminase 1. This
            enzyme catalyzes the reversible transamination between alanine and
            2-oxoglutarate to generate pyruvate and glutamate and, therefore,
            plays a key role in the intermediary metabolism of glucose and
            amino acids. Serum activity levels of this enzyme are routinely
            used as a biomarker of liver injury caused by drug toxicity,
            infection, alcohol, and steatosis. A related gene on chromosome 16
            encodes a putative mitochondrial alanine
            aminotransaminase.[provided by RefSeq, Nov 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9304715.613116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2151405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: relevant for disease process
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..496
                     /product="alanine aminotransferase 1"
                     /EC_number="2.6.1.2"
                     /note="glutamic-alanine transaminase 1; glutamic--pyruvic
                     transaminase 1; alanine aminotransferase; glutamate
                     pyruvate transaminase 1; glutamic-pyruvate transaminase
                     (alanine aminotransferase); serum glutamic-pyruvic
                     transaminase; serum glutamate-pyruvate transaminase"
                     /calculated_mol_wt=54506
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1931970; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     Region          17..496
                     /region_name="PTZ00377"
                     /note="alanine aminotransferase; Provisional"
                     /db_xref="CDD:240391"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     CDS             1..496
                     /gene="GPT"
                     /gene_synonym="AAT1; ALT; ALT1; GPT1; SGPT"
                     /coded_by="NM_001382665.1:222..1712"
                     /db_xref="CCDS:CCDS6430.1"
                     /db_xref="GeneID:2875"
                     /db_xref="HGNC:HGNC:4552"
                     /db_xref="MIM:138200"
ORIGIN      
        1 masstgdrsq avrhglrakv ltldgmnprv rrveyavrgp ivqraleleq elrqgvkkpf
       61 teviranigd aqamgqrpit flrqvlalcv npdllsspnf pddakkraer ilqacgghsl
      121 gaysvssgiq liredvaryi errdggipad pnnvflstga sdaivtvlkl lvageghtrt
      181 gvlipipqyp lysatlaelg avqvdyylde erawaldvae lhralgqard hcrpralcvi
      241 npgnptgqvq trecieavir fafeerlfll adevyqdnvy aagsqfhsfk kvlmemgppy
      301 agqqelasfh stskgymgec gfrggyvevv nmdaavqqqm lklmsvrlcp pvpgqalldl
      361 vvsppaptdp sfaqfqaekq avlaelaaka klteqvfnea pgiscnpvqg amysfprvql
      421 ppraveraqe lglapdmffc lrlleetgic vvpgsgfgqr egtyhfrmti lppleklrll
      481 leklsrfhak ftleys
//
LOCUS       NP_001394038              94 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform m [Homo sapiens].
ACCESSION   NP_001394038
VERSION     NP_001394038.1
DBSOURCE    REFSEQ: accession NM_001407109.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 94)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 94)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 94)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 94)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.855128.1,
                                           SRR14038191.3330473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..94
                     /product="protein max isoform m"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10895
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..94
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407109.1:179..463"
                     /note="isoform m is encoded by transcript variant 27"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg eses
//
LOCUS       NP_001316668             132 aa            linear   PRI 20-NOV-2025
DEFINITION  telomerase RNA component interacting RNase isoform 3 [Homo
            sapiens].
ACCESSION   NP_001316668
VERSION     NP_001316668.1
DBSOURCE    REFSEQ: accession NM_001329739.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Xie,J., Chen,Z., Zhang,X., Chen,H. and Guan,W.
  TITLE     Identification of an RNase that preferentially cleaves A/G
            nucleotides
  JOURNAL   Sci Rep 7, 45207 (2017)
   PUBMED   28322335
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018761.6.
            
            Transcript Variant: This variant (3) uses an alternate splice site,
            which results in a frameshift, compared to variant 1. The encoded
            protein (isoform 3) has a distinct, shorter C-terminus compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.293743.1, BX376854.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155751, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..132
                     /product="telomerase RNA component interacting RNase
                     isoform 3"
                     /note="uncharacterized protein C19orf43; My029 protein;
                     exoribonuclease TRIR"
                     /calculated_mol_wt=13372
     CDS             1..132
                     /gene="TRIR"
                     /gene_synonym="C19orf43; fSAP18; TERCIR"
                     /coded_by="NM_001329739.2:28..426"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86710.1"
                     /db_xref="GeneID:79002"
                     /db_xref="HGNC:HGNC:28424"
                     /db_xref="MIM:621422"
ORIGIN      
        1 maargrraep qgreapgpag gggggsrwae sgsgtspesg deevsgagss pvsggvnlfa
       61 ndgsflelfk rkmeeeqrqr qeepppgpqr pdqsaaaagp gdpkrkgggq tqrreqtspq
      121 dgnssqeaed gg
//
LOCUS       NP_001123481             908 aa            linear   PRI 20-NOV-2025
DEFINITION  flap endonuclease GEN homolog 1 [Homo sapiens].
ACCESSION   NP_001123481
VERSION     NP_001123481.3
DBSOURCE    REFSEQ: accession NM_001130009.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Du,X., Wang,C., Liu,J., Yu,M., Ju,H., Xue,S., Li,Y., Liu,J.,
            Dai,R., Chen,J., Zhai,Y., Rao,J., Wang,X., Sun,Y., Sun,L., Wu,X.,
            Xu,H. and Shen,Q.
  TITLE     GEN1 as a risk factor for human congenital anomalies of the kidney
            and urinary tract
  JOURNAL   Hum Genomics 18 (1), 41 (2024)
   PUBMED   38654324
  REMARK    GeneRIF: GEN1 as a risk factor for human congenital anomalies of
            the kidney and urinary tract.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Kim,J., Yu,J., Lee,S., Kim,S., Lee,I.S., Lee,W. and Chun,S.
  TITLE     Reverse Transcription-PCR-based Sanger Sequencing-confirmed
            Exon-skipping Effect of a Novel GEN1 Intronic Variant (c.1408+4A>G)
  JOURNAL   Ann Lab Med 44 (2), 188-191 (2024)
   PUBMED   37840312
  REMARK    GeneRIF: Reverse Transcription-PCR-based Sanger
            Sequencing-confirmed Exon-skipping Effect of a Novel GEN1 Intronic
            Variant (c.1408+4A>G).
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Benitez,A., Sebald,M., Kanagaraj,R., Rodrigo-Brenni,M.C.,
            Chan,Y.W., Liang,C.C. and West,S.C.
  TITLE     GEN1 promotes common fragile site expression
  JOURNAL   Cell Rep 42 (2), 112062 (2023)
   PUBMED   36729836
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Chan,Y.W. and West,S.
  TITLE     GEN1 promotes Holliday junction resolution by a coordinated nick
            and counter-nick mechanism
  JOURNAL   Nucleic Acids Res 43 (22), 10882-10892 (2015)
   PUBMED   26578604
  REMARK    GeneRIF: human GEN1 protein promotes Holliday junction resolution
            by a mechanism that is analogous to that exhibited by the
            prototypic HJ resolvase E. coli RuvC.
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Chan,Y.W. and West,S.C.
  TITLE     Spatial control of the GEN1 Holliday junction resolvase ensures
            genome stability
  JOURNAL   Nat Commun 5, 4844 (2014)
   PUBMED   25209024
  REMARK    GeneRIF: GEN1 is controlled by nuclear exclusion, driven by a
            nuclear export signal that restricts GEN1 actions to mitosis.
            Spatial control of GEN1 contributes to genome stability by avoiding
            competition with non-crossover promoting repair pathways.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Garner,E., Kim,Y., Lach,F.P., Kottemann,M.C. and Smogorzewska,A.
  TITLE     Human GEN1 and the SLX4-associated nucleases MUS81 and SLX1 are
            essential for the resolution of replication-induced Holliday
            junctions
  JOURNAL   Cell Rep 5 (1), 207-215 (2013)
   PUBMED   24080495
  REMARK    GeneRIF: GEN1 activity cannot be substituted for the
            SLX4-associated nucleases, and one of the HJ resolvase activities,
            either of those associated with SLX4 or with GEN1, is required for
            cell viability, even in the presence of BLM.
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Gao,M., Rendtlew Danielsen,J., Wei,L.Z., Zhou,D.P., Xu,Q., Li,M.M.,
            Wang,Z.Q., Tong,W.M. and Yang,Y.G.
  TITLE     A novel role of human holliday junction resolvase GEN1 in the
            maintenance of centrosome integrity
  JOURNAL   PLoS One 7 (11), e49687 (2012)
   PUBMED   23166748
  REMARK    GeneRIF: Our findings provide novel insight into the biological
            functions of GEN1 by uncovering an important role of GEN1 in the
            regulation of centrosome integrity.
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Lorenz,A., West,S.C. and Whitby,M.C.
  TITLE     The human Holliday junction resolvase GEN1 rescues the meiotic
            phenotype of a Schizosaccharomyces pombe mus81 mutant
  JOURNAL   Nucleic Acids Res 38 (6), 1866-1873 (2010)
   PUBMED   20040574
  REMARK    GeneRIF: ectopic expression of GEN1 in fission yeast mus81Delta
            strains results in Holliday junction resolution and crossover
            formation during meiosis.
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Ip,S.C., Rass,U., Blanco,M.G., Flynn,H.R., Skehel,J.M. and
            West,S.C.
  TITLE     Identification of Holliday junction resolvases from humans and
            yeast
  JOURNAL   Nature 456 (7220), 357-361 (2008)
   PUBMED   19020614
  REMARK    GeneRIF: Recombinant GEN1 and Yen1 resolve Holliday junctions by
            the introduction of symmetrically related cuts across the junction
            point, to produce nicked duplex products in which the nicks can be
            readily ligated
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Ishikawa,G., Kanai,Y., Takata,K., Takeuchi,R., Shimanouchi,K.,
            Ruike,T., Furukawa,T., Kimura,S. and Sakaguchi,K.
  TITLE     DmGEN, a novel RAD2 family endo-exonuclease from Drosophila
            melanogaster
  JOURNAL   Nucleic Acids Res 32 (21), 6251-6259 (2004)
   PUBMED   15576351
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097377.3 and AC093731.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NP_001123481.2.
            
            Summary: This gene encodes a member of the Rad2/xeroderma
            pigmentosum group G nuclease family, whose members are
            characterized by N-terminal and internal xeroderma pigmentosum
            group G nuclease domains followed by helix-hairpin-helix domains
            and disordered C-terminal domains. The protein encoded by this gene
            is involved in resolution of Holliday junctions, which are
            intermediate four-way structures that covalently link DNA during
            homologous recombination and double-strand break repair. The
            protein resolves Holliday junctions by creating dual incisions
            across the junction to produce nicked duplex products that can be
            ligated. In addition, this protein has been found to localize to
            centrosomes where it has been implicated in regulation of
            centrosome integrity. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence data consistent
            with the reference genome assembly was not available for all
            regions of the RefSeq transcript. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.308.1,
                                           SRR1660807.163351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381254.7/ ENSP00000370653.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.2"
     Protein         1..908
                     /product="flap endonuclease GEN homolog 1"
                     /note="Gen endonuclease homolog 1; Holliday junction
                     resolvase; GEN1 Holliday junction 5' flap endonuclease;
                     structure-selective endonuclease GEN1; replication fork
                     endonuclease"
                     /calculated_mol_wt=102754
     Region          2..206
                     /region_name="PIN_GEN1"
                     /note="FEN-like PIN domains of Gap Endonuclease 1, a
                     structure-specific, divalent-metal-ion dependent, 5'
                     nuclease and homologs; cd09869"
                     /db_xref="CDD:350217"
     Region          2..96
                     /region_name="XPG-N domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            order(16,30,37,54..55,58..59,75,134,136,155,157,170..171)
                     /site_type="active"
                     /db_xref="CDD:350217"
     Site            order(81..92,104..111)
                     /site_type="other"
                     /note="helical arch"
                     /db_xref="CDD:350217"
     Region          122..208
                     /region_name="XPG-I domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Region          195..338
                     /region_name="H3TH_GEN1"
                     /note="H3TH domain of Gap Endonuclease 1, a
                     structure-specific, divalent-metal-ion dependent, 5'
                     nuclease; cd09905"
                     /db_xref="CDD:188625"
     Site            order(205..210,213..218,220..223)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:188625"
     Region          208..384
                     /region_name="5'-3' exonuclease domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            208
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:188625"
     Region          390..464
                     /region_name="Chromodomain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Region          398..458
                     /region_name="Chromo_2"
                     /note="Chromatin organization modifier domain 2;
                     pfam18704"
                     /db_xref="CDD:465841"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMI4; propagated from
                     UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMI4; propagated from
                     UniProtKB/Swiss-Prot (Q17RS7.2)"
     CDS             1..908
                     /gene="GEN1"
                     /gene_synonym="Gen"
                     /coded_by="NM_001130009.3:224..2950"
                     /db_xref="CCDS:CCDS1691.1"
                     /db_xref="GeneID:348654"
                     /db_xref="HGNC:HGNC:26881"
                     /db_xref="MIM:612449"
ORIGIN      
        1 mgvndlwqil epvkqhiplr nlggktiavd lslwvceaqt vkkmmgsvmk phlrnlffri
       61 syltqmdvkl vfvmegeppk lkadviskrn qsrygssgks wsqktgrshf ksvlreclhm
      121 leclgipwvq aageaeamca ylnagghvdg cltndgdtfl ygaqtvyrnf tmntkdphvd
      181 cytmssiksk lgldrdalvg laillgcdyl pkgvpgvgke qalkliqilk gqsllqrfnr
      241 wnetscnssp qllvtkklah csvcshpgsp kdherngcrl cksdkyceph dyeyccpcew
      301 hrtehdrqls evennikkka cccegfpfhe viqefllnkd klvkviryqr pdlllfqrft
      361 lekmewpnhy acekllvllt hydmierklg srnsnqlqpi rivktrirng vhcfeiewek
      421 pehyamedkq hgefalltie eeslfeaayp eivavyqkqk leikgkkqkr ikpkennlpe
      481 pdevmsfqsh mtlkptceif hkqnsklnsg ispdptlpqe sisaslnsll lpkntpclna
      541 qeqfmsslrp laiqqikavs kslisessqp ntsshnisvi adlhlstidw egtsfsnspa
      601 iqrntfshdl kseveselsa ipdgfenipe qlsceseryt anikkvlded sdgispeehl
      661 lsgitdlclq dlplkerift klsypqdnlq pdvnlktlsi lsvkescian sgsdctshls
      721 kdlpgiplqn esrdskilkg dqllqedykv ntsvpysvsn tvvktcnvrp pntaldhsrk
      781 vdmqttrkil mkksvcldrh ssdeqsapvf gkakyttqrm khssqkhnss hfkesghnkl
      841 sspkihiket eqcvrsyeta eneescfpds tksslsslqc hkkennsgtc ldsplplrqr
      901 lklrfqst
//
LOCUS       NP_001035809             599 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family E member 1 [Homo sapiens].
ACCESSION   NP_001035809
VERSION     NP_001035809.1
DBSOURCE    REFSEQ: accession NM_001040876.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Tong,S., Zhu,Y., Leng,Y., Wu,Y., Xiao,X., Zhao,W. and Tan,S.
  TITLE     Restoration of miR-299-3p promotes macrophage phagocytosis and
            suppresses malignant phenotypes in breast cancer carcinogenesis via
            dual-targeting CD47 and ABCE1
  JOURNAL   Int Immunopharmacol 130, 111708 (2024)
   PUBMED   38394889
  REMARK    GeneRIF: Restoration of miR-299-3p promotes macrophage phagocytosis
            and suppresses malignant phenotypes in breast cancer carcinogenesis
            via dual-targeting CD47 and ABCE1.
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   3  (residues 1 to 599)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Sun,L., Ding,X. and Kang,Y.J.
  TITLE     ABCE1 selectively promotes HIF-1alpha transactivation of angiogenic
            gene expression
  JOURNAL   J Trace Elem Med Biol 80, 127307 (2023)
   PUBMED   37738929
  REMARK    GeneRIF: ABCE1 selectively promotes HIF-1alpha transactivation of
            angiogenic gene expression.
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Martinand,C., Montavon,C., Salehzada,T., Silhol,M., Lebleu,B. and
            Bisbal,C.
  TITLE     RNase L inhibitor is induced during human immunodeficiency virus
            type 1 infection and down regulates the 2-5A/RNase L pathway in
            human T cells
  JOURNAL   J Virol 73 (1), 290-296 (1999)
   PUBMED   9847332
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Martinand,C., Salehzada,T., Silhol,M., Lebleu,B. and Bisbal,C.
  TITLE     RNase L inhibitor (RLI) antisense constructions block partially the
            down regulation of the 2-5A/RNase L pathway in
            encephalomyocarditis-virus-(EMCV)-infected cells
  JOURNAL   Eur J Biochem 254 (2), 248-255 (1998)
   PUBMED   9660177
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Diriong,S., Salehzada,T., Bisbal,C., Martinand,C. and Taviaux,S.
  TITLE     Localization of the ribonuclease L inhibitor gene (RNS4I), a new
            member of the interferon-regulated 2-5A pathway, to 4q31 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 32 (3), 488-490 (1996)
   PUBMED   8838820
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Aubry,F., Mattei,M.G., Barque,J.P. and Galibert,F.
  TITLE     Chromosomal localization and expression pattern of the RNase L
            inhibitor gene
  JOURNAL   FEBS Lett 381 (1-2), 135-139 (1996)
   PUBMED   8641422
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Bisbal,C., Martinand,C., Silhol,M., Lebleu,B. and Salehzada,T.
  TITLE     Cloning and characterization of a RNAse L inhibitor. A new
            component of the interferon-regulated 2-5A pathway
  JOURNAL   J Biol Chem 270 (22), 13308-13317 (1995)
   PUBMED   7539425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA218189.1, BC016283.1 and
            AC096757.3.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the OABP subfamily. Alternatively referred
            to as the RNase L inhibitor, this protein functions to block the
            activity of ribonuclease L. Activation of ribonuclease L leads to
            inhibition of protein synthesis in the 2-5A/RNase L system, the
            central pathway for viral interferon action. Two transcript
            variants encoding the same protein have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.18985.1,
                                           SRR1660805.162230.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..599
                     /product="ATP-binding cassette sub-family E member 1"
                     /EC_number="3.6.5.-"
                     /note="ribonuclease L (2',5'-oligoisoadenylate
                     synthetase-dependent) inhibitor; huHP68; ribonuclease 4
                     inhibitor; 2'-5'-oligoadenylate-binding protein;
                     ATP-binding cassette, sub-family E (OABP), member 1; RNase
                     L inhibitor 1"
                     /calculated_mol_wt=67184
     Region          6..598
                     /region_name="Rli1"
                     /note="Translation initiation factor RLI1, contains Fe-S
                     and AAA+ ATPase domains [Translation, ribosomal structure
                     and biogenesis]; COG1245"
                     /db_xref="CDD:440858"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61221.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61221.1)"
     CDS             1..599
                     /gene="ABCE1"
                     /gene_synonym="ABC38; OABP; RLI; RLI1; RNASEL1; RNASELI;
                     RNS4I"
                     /coded_by="NM_001040876.2:134..1933"
                     /db_xref="CCDS:CCDS34071.1"
                     /db_xref="GeneID:6059"
                     /db_xref="HGNC:HGNC:69"
                     /db_xref="MIM:601213"
ORIGIN      
        1 madkltriai vnhdkckpkk crqeckkscp vvrmgklcie vtpqskiawi setlcigcgi
       61 cikkcpfgal sivnlpsnle ketthrycan afklhrlpip rpgevlglvg tngigkstal
      121 kilagkqkpn lgkyddppdw qeiltyfrgs elqnyftkil eddlkaiikp qyvdqipkaa
      181 kgtvgsildr kdetktqaiv cqqldlthlk ernvedlsgg elqrfacavv ciqkadifmf
      241 depssyldvk qrlkaaitir slinpdryii vvehdlsvld ylsdficcly gvpsaygvvt
      301 mpfsvregin ifldgyvpte nlrfrdaslv fkvaetanee evkkmcmyky pgmkkkmgef
      361 elaivageft dseimvmlge ngtgkttfir mlagrlkpde ggevpvlnvs ykpqkispks
      421 tgsvrqllhe kirdaythpq fvtdvmkplq ieniidqevq tlsggelqrv alalclgkpa
      481 dvylidepsa yldseqrlma arvvkrfilh akktafvveh dfimatylad rvivfdgvps
      541 kntvanspqt llagmnkfls qleitfrrdp nnyrprinkl nsikdveqkk sgnyffldd
//
LOCUS       NP_001337667             688 aa            linear   PRI 20-NOV-2025
DEFINITION  SRSF protein kinase 2 isoform b [Homo sapiens].
ACCESSION   NP_001337667 XP_016868055
VERSION     NP_001337667.1
DBSOURCE    REFSEQ: accession NM_001350738.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Yip,R.P.H., Kwok,D.C.Y., Lai,L.T.F., Ho,S.M., Wong,I.C.K.,
            Chan,C.P., Lau,W.C.Y. and Ngo,J.C.K.
  TITLE     SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly
            via Docking Interaction
  JOURNAL   PLoS Pathog 20 (2), e1011978 (2024)
   PUBMED   38324561
  REMARK    GeneRIF: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid
            Assembly via Docking Interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Yang,Z. and Ding,W.X.
  TITLE     The pre-mRNA alternative splicing regulated by SRPK2: A new player
            in alcohol-associated liver disease?
  JOURNAL   Hepatology 78 (5), 1329-1331 (2023)
   PUBMED   37183907
  REMARK    GeneRIF: The pre-mRNA alternative splicing regulated by SRPK2: A
            new player in alcohol-associated liver disease?
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Koizumi,J., Okamoto,Y., Onogi,H., Mayeda,A., Krainer,A.R. and
            Hagiwara,M.
  TITLE     The subcellular localization of SF2/ASF is regulated by direct
            interaction with SR protein kinases (SRPKs)
  JOURNAL   J Biol Chem 274 (16), 11125-11131 (1999)
   PUBMED   10196197
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Kuroyanagi,N., Onogi,H., Wakabayashi,T. and Hagiwara,M.
  TITLE     Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
            speckles
  JOURNAL   Biochem Biophys Res Commun 242 (2), 357-364 (1998)
   PUBMED   9446799
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Bedford,M.T., Chan,D.C. and Leder,P.
  TITLE     FBP WW domains and the Abl SH3 domain bind to a specific class of
            proline-rich ligands
  JOURNAL   EMBO J 16 (9), 2376-2383 (1997)
   PUBMED   9171351
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073138.3, AC004884.1 and AC005070.1.
            
            On Apr 22, 2017 this sequence version replaced XP_016868055.1.
            
            Transcript Variant: This variant (4), as well as variants 2 and 3,
            encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2183805.1,
                                           SRR14038197.2415672.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..688
                     /product="SRSF protein kinase 2 isoform b"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 2; serine/arginine-rich
                     splicing factor kinase 2; SR protein kinase 2;
                     serine/threonine-protein kinase SRPK2; serine kinase
                     SRPK2; SR-protein-specific kinase 2; serine/arginine-rich
                     protein-specific kinase 2"
                     /calculated_mol_wt=77396
     Region          1..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Region          68..>256
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(87..90,93,95,108,110,146,166..169,214,218..219,221)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271119"
     Site            139..140
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:21056976; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Region          239..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          329..444
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          <341..383
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            403..404
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000269|PubMed:21056976; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Region          469..501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54781; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:19592491; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78362.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     Region          <504..686
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P78362.3)"
     CDS             1..688
                     /gene="SRPK2"
                     /gene_synonym="SFRSK2"
                     /coded_by="NM_001350738.2:213..2279"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS5735.1"
                     /db_xref="GeneID:6733"
                     /db_xref="HGNC:HGNC:11306"
                     /db_xref="MIM:602980"
ORIGIN      
        1 msvnseksss serpepqqka plvppppppp pppppplpdp tppepeeeil gsddeeqedp
       61 adyckggyhp vkigdlfngr yhvirklgwg hfstvwlcwd mqgkrfvamk vvksaqhyte
      121 taldeikllk cvresdpsdp nkdmvvqlid dfkisgmngi hvcmvfevlg hhllkwiiks
      181 nyqglpvrcv ksiirqvlqg ldylhskcki ihtdikpeni lmcvddayvr rmaaeatewq
      241 kagapppsgs avstapqqkp igkisknkkk klkkkqkrqa ellekrlqei eelereaerk
      301 iieenitsaa psndqdgeyc pevklkttgl eeaaeaetak dngeaedqee kedaekenie
      361 kdeddvdqel anidptwies pktnghieng pfsleqqldd edddeedcpn peeynldepn
      421 aesdytysss yeqfngelpn grhkipesqf pefstslfsg slepvacgsv lsegsplteq
      481 eesspshdrs rtvsasstgd lpkaktraad llvnpldprn adkirvkiad lgnacwvhkh
      541 ftediqtrqy rsievligag ystpadiwst acmafelatg dylfephsge dysrdedhia
      601 hiiellgsip rhfalsgkys reffnrrgel rhitklkpws lfdvlvekyg wphedaaqft
      661 dflipmlemv pekrasagec lrhpwlns
//
LOCUS       NP_001364250            1543 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family A member 10 [Homo sapiens].
ACCESSION   NP_001364250
VERSION     NP_001364250.1
DBSOURCE    REFSEQ: accession NM_001377321.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1543)
  AUTHORS   Chen,H., Li,L., Qin,P., Xiong,H., Chen,R., Zhang,M. and Jiang,Q.
  TITLE     A 4-gene signature predicts prognosis of uterine serous carcinoma
  JOURNAL   BMC Cancer 21 (1), 154 (2021)
   PUBMED   33579221
  REMARK    GeneRIF: A 4-gene signature predicts prognosis of uterine serous
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1543)
  AUTHORS   Baecklund,F., Foo,J.N., Bracci,P., Darabi,H., Karlsson,R.,
            Hjalgrim,H., Rosenquist,R., Adami,H.O., Glimelius,B., Melbye,M.,
            Conde,L., Liu,J., Humphreys,K., Skibola,C.F. and Smedby,K.E.
  TITLE     A comprehensive evaluation of the role of genetic variation in
            follicular lymphoma survival
  JOURNAL   BMC Med Genet 15, 113 (2014)
   PUBMED   25294155
  REMARK    GeneRIF: Results suggest a possible role for multidrug resistance
            genes ABCA10 and ABCA6 in follicular lymphoma survival and add to
            the evidence that genetic variation in CD46 and IL8 may have
            prognostic implications follicular lymphoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1543)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   4  (residues 1 to 1543)
  AUTHORS   Wenzel,J.J., Kaminski,W.E., Piehler,A., Heimerl,S., Langmann,T. and
            Schmitz,G.
  TITLE     ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter
  JOURNAL   Biochem Biophys Res Commun 306 (4), 1089-1098 (2003)
   PUBMED   12821155
  REMARK    GeneRIF: ABCA10 is a novel member of the group of ABCA6-like
            transporters involved in macrophage lipid homeostasis
REFERENCE   5  (residues 1 to 1543)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   6  (residues 1 to 1543)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005495.2.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            and White). This encoded protein is a member of the ABC1 subfamily.
            Members of the ABC1 subfamily comprise the only major ABC subfamily
            found exclusively in multicellular eukaryotes. This gene is
            clustered among 4 other ABC1 family members on 17q24, but neither
            the substrate nor the function of this gene is known. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY247065.1, AY028900.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000690296.1/ ENSP00000509702.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.3"
     Protein         1..1543
                     /product="ATP-binding cassette sub-family A member 10"
                     /EC_number="7.6.2.-"
                     /note="ATP-binding cassette A10; ATP-binding cassette,
                     sub-family A (ABC1), member 10"
                     /calculated_mol_wt=175660
     Region          <37..1520
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            210..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            774..794
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            890..910
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            926..946
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            985..1005
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1014..1034
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1046..1066
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1073..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1113..1133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Region          1153..1177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     CDS             1..1543
                     /gene="ABCA10"
                     /gene_synonym="EST698739"
                     /coded_by="NM_001377321.1:557..5188"
                     /db_xref="CCDS:CCDS11684.1"
                     /db_xref="GeneID:10349"
                     /db_xref="HGNC:HGNC:30"
                     /db_xref="MIM:612508"
ORIGIN      
        1 mnkmalasfm kgrtvigtpd eetmdielpk kyhemvgvif sdtfsyrlkf nwgyripvik
       61 ehseytehcw amhgeifcyl akywlkgfva fqaainaaii evttnhsvme eltsviginm
      121 kippfiskge imnewfhftc lvsfssfiyf aslnvarerg kfkklmtvmg lresafwlsw
      181 gltyicfifi msifmalvit sipivfhtgf mviftlysly glslialafl msvlirkpml
      241 aglagflftv fwgclgftvl yrqlplslgw vlsllspfaf tagmaqithl dnylsgvifp
      301 dpsgdsykmi atffilafdt lfyliftlyf ervlpdkdgh gdsplfflks sfwskhqnth
      361 heifeneinp ehssddsfep vspefhgkea irirnvikey ngktgkveal qgiffdiyeg
      421 qitailghng agkstllnil sglsvstegs atiyntqlse itdmeeirkn igfcpqfnfq
      481 fdfltvrenl rvfakikgiq pkeveqevkr iimeldmqsi qdiiakklsg gqkrkltlgi
      541 ailgdpqvll ldeptagldp fsrhrvwsll kehkvdrlil fstqfmdead iladrkvfls
      601 ngklkcagss lflkrkwgig yhlslhrnem cdtekitsli kqhipdaklt teseeklvys
      661 lplektnkfp dlysdldkcs dqgirnyavs vtslnevfln legksaidep dfdigkqeki
      721 hvtrntgdes emeqvlcslp etrkavssaa lwrrqiyava tlrflklrre rrallclllv
      781 lgiafipiil ekimykvtre thcwefspsm yflsleqipk tpltsllivn ntgsniedlv
      841 hslkcqdivl eiddfrnrng sddpsyngai ivsgdqkdyr fsvacntkkl ncfpvlmgiv
      901 snalmgifnf teliqmests fsrddivldl gfidgsifll litncvspfi gmssisdykk
      961 nvqsqlwisg lwpsaywcgq alvdiplyfl ilfsihliyy fiflgfqlsw elmfvlvvci
     1021 igcavslifl tyvlsfifrk wrknngfwsf gffiilicvs timvstqyek lnlilcmifi
     1081 psftllgyvm lliqldfmrn ldsldnrine vnktillttl ipylqsvifl fvirclemky
     1141 gneimnkdpv frisprsret hpnpeepeee dedvqaervq aanaltapnl eeepvitasc
     1201 lhkeyyetkk scfstrkkki airnvsfcvk kgevlgllgh ngagkstsik mitgctkpta
     1261 gvvvlqgsra svrqqhdnsl kflgycpqen slwpkltmke hlelyaavkg lgkedaalsi
     1321 srlvealklq eqlkapvktl segikrklcf vlsilgnpsv vlldepftgm dpegqqqmwq
     1381 ilqatvknke rgtlltthym seaeavcdrm ammvsgtlrc igsiqhlknk fgrdylleik
     1441 mkeptqveal hteilklfpq aawqeryssl mayklpvedv hplsraffkl eamkqtfnle
     1501 eyslsqatle qvflelckeq elgnvddkid ttvewkllpq edp
//
LOCUS       NP_001399717             725 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001399717
VERSION     NP_001399717.1
DBSOURCE    REFSEQ: accession NM_001412788.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125491.1 and AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.3852546.1,
                                           SRR18074968.4318657.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..725
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 2"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=81764
     Region          1..218
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:10777694"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Region          74..681
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     CDS             1..725
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412788.1:189..2366"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvemkqlq ksykaladqm nlilskrlwy imieqflmky vwsssglimv
      361 aipiitatgf adgedgqkqv mvserteaft tarnllasga daierimssy kevtelagyt
      421 arvynmfwvf devkrgiykr taviqesesh skngakvelp lsdtlaikgk vidvdhgiic
      481 envpiitpag evvasrlnfk veegmhllit gpngcgkssl frilsglwpv yegvlykppp
      541 qhmfyipqrp ymslgslrdq viypdsvddm hdkgytdqdl erilhnvhly hivqreggwd
      601 avmdwkdvls ggekqrmgma rmfyhkpkya lldectsavs idvegkifqa akgagislls
      661 ithrpslwyi lfkphnnpve frksnlpilq mkklrtrkvr yfhdhilctt ahgshykelk
      721 vylmh
//
LOCUS       NP_006036               1047 aa            linear   PRI 20-NOV-2025
DEFINITION  probable phospholipid-transporting ATPase IIA [Homo sapiens].
ACCESSION   NP_006036 XP_030577
VERSION     NP_006036.1
DBSOURCE    REFSEQ: accession NM_006045.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Abe,K., Marimuthu,P., Qian,Y., Gopalasingam,C.C., Gerle,C.,
            Shigematsu,H., Tanaka,K. and Khandelia,H.
  TITLE     A unique gating mechanism revealed by the cryo-EM structure of
            monomeric ATP9A flippase
  JOURNAL   J Biol Chem 301 (10), 110631 (2025)
   PUBMED   40876594
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Yagi,T., Nakabuchi,R., Muranaka,Y., Tanaka,G., Katoh,Y.,
            Nakayama,K., Takatsu,H. and Shin,H.W.
  TITLE     Lipid flippases ATP9A and ATP9B form a complex and contribute to
            the exocytic pathway from the Golgi
  JOURNAL   Life Sci Alliance 8 (7), e202403163 (2025)
   PUBMED   40234049
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Yao,Y., Chen,C., Wang,J., Xuan,H., Chen,X., Li,Z., Yang,F.,
            Wang,B., Lin,S., Li,S., Tang,D., Gong,L. and Gao,W.
  TITLE     Circular RNA circATP9A promotes non-small cell lung cancer
            progression by interacting with HuR and by promoting extracellular
            vesicles-mediated macrophage M2 polarization
  JOURNAL   J Exp Clin Cancer Res 42 (1), 330 (2023)
   PUBMED   38049814
  REMARK    GeneRIF: Circular RNA circATP9A promotes non-small cell lung cancer
            progression by interacting with HuR and by promoting extracellular
            vesicles-mediated macrophage M2 polarization.
            Erratum:[J Exp Clin Cancer Res. 2023 Dec 19;42(1):345. doi:
            10.1186/s13046-023-02924-6. PMID: 38111017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Wang,X., Li,Y., Xiao,Y., Huang,X., Wu,X., Zhao,Z., Yang,M.,
            Kong,L., Shi,D., Chen,X., Ouyang,Y., Chen,X., Lin,C., Li,J.,
            Song,L., Lin,Y. and Guan,J.
  TITLE     The phospholipid flippase ATP9A enhances macropinocytosis to
            promote nutrient starvation tolerance in hepatocellular carcinoma
  JOURNAL   J Pathol 260 (1), 17-31 (2023)
   PUBMED   36715683
  REMARK    GeneRIF: The phospholipid flippase ATP9A enhances macropinocytosis
            to promote nutrient starvation tolerance in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Meng,T., Chen,X., He,Z., Huang,H., Lin,S., Liu,K., Bai,G., Liu,H.,
            Xu,M., Zhuang,H., Zhang,Y., Waqas,A., Liu,Q., Zhang,C., Sun,X.D.,
            Huang,H., Umair,M., Yan,Y. and Feng,D.
  TITLE     ATP9A deficiency causes ADHD and aberrant endosomal recycling via
            modulating RAB5 and RAB11 activity
  JOURNAL   Mol Psychiatry 28 (3), 1219-1231 (2023)
   PUBMED   36604604
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Yu,D., Mathews,C.A., Scharf,J.M., Neale,B.M., Davis,L.K.,
            Gamazon,E.R., Derks,E.M., Evans,P., Edlund,C.K., Crane,J.,
            Fagerness,J.A., Osiecki,L., Gallagher,P., Gerber,G., Haddad,S.,
            Illmann,C., McGrath,L.M., Mayerfeld,C., Arepalli,S., Barlassina,C.,
            Barr,C.L., Bellodi,L., Benarroch,F., Berrio,G.B., Bienvenu,O.J.,
            Black,D.W., Bloch,M.H., Brentani,H., Bruun,R.D., Budman,C.L.,
            Camarena,B., Campbell,D.D., Cappi,C., Silgado,J.C., Cavallini,M.C.,
            Chavira,D.A., Chouinard,S., Cook,E.H., Cookson,M.R., Coric,V.,
            Cullen,B., Cusi,D., Delorme,R., Denys,D., Dion,Y., Eapen,V.,
            Egberts,K., Falkai,P., Fernandez,T., Fournier,E., Garrido,H.,
            Geller,D., Gilbert,D.L., Girard,S.L., Grabe,H.J., Grados,M.A.,
            Greenberg,B.D., Gross-Tsur,V., Grunblatt,E., Hardy,J., Heiman,G.A.,
            Hemmings,S.M., Herrera,L.D., Hezel,D.M., Hoekstra,P.J.,
            Jankovic,J., Kennedy,J.L., King,R.A., Konkashbaev,A.I.,
            Kremeyer,B., Kurlan,R., Lanzagorta,N., Leboyer,M., Leckman,J.F.,
            Lennertz,L., Liu,C., Lochner,C., Lowe,T.L., Lupoli,S.,
            Macciardi,F., Maier,W., Manunta,P., Marconi,M., McCracken,J.T.,
            Mesa Restrepo,S.C., Moessner,R., Moorjani,P., Morgan,J., Muller,H.,
            Murphy,D.L., Naarden,A.L., Nurmi,E., Ochoa,W.C., Ophoff,R.A.,
            Pakstis,A.J., Pato,M.T., Pato,C.N., Piacentini,J., Pittenger,C.,
            Pollak,Y., Rauch,S.L., Renner,T., Reus,V.I., Richter,M.A.,
            Riddle,M.A., Robertson,M.M., Romero,R., Rosario,M.C., Rosenberg,D.,
            Ruhrmann,S., Sabatti,C., Salvi,E., Sampaio,A.S., Samuels,J.,
            Sandor,P., Service,S.K., Sheppard,B., Singer,H.S., Smit,J.H.,
            Stein,D.J., Strengman,E., Tischfield,J.A., Turiel,M., Valencia
            Duarte,A.V., Vallada,H., Veenstra-VanderWeele,J., Walitza,S.,
            Wang,Y., Weale,M., Weiss,R., Wendland,J.R., Westenberg,H.G.,
            Shugart,Y.Y., Hounie,A.G., Miguel,E.C., Nicolini,H., Wagner,M.,
            Ruiz-Linares,A., Cath,D.C., McMahon,W., Posthuma,D., Oostra,B.A.,
            Nestadt,G., Rouleau,G.A., Purcell,S., Jenike,M.A., Heutink,P.,
            Hanna,G.L., Conti,D.V., Arnold,P.D., Freimer,N.B., Stewart,S.E.,
            Knowles,J.A., Cox,N.J. and Pauls,D.L.
  TITLE     Cross-disorder genome-wide analyses suggest a complex genetic
            relationship between Tourette's syndrome and OCD
  JOURNAL   Am J Psychiatry 172 (1), 82-93 (2015)
   PUBMED   25158072
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY147052.1, AK299064.1, BC110592.1, BF089115.1 and AL035684.25.
            
            On May 15, 2005 this sequence version replaced XP_030577.9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.196180.1,
                                           SRR1803614.38645.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338821.6/ ENSP00000342481.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2"
     Protein         1..1047
                     /product="probable phospholipid-transporting ATPase IIA"
                     /EC_number="7.6.2.1"
                     /note="ATPase type IV, phospholipid-transporting
                     (P-type),(putative); phospholipid-transporting ATPase IIA;
                     ATPase, class II, type 9A; ATPase phospholipid
                     transporting 9A (putative)"
                     /calculated_mol_wt=118452
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75110.3)"
     Region          55..967
                     /region_name="P-type_ATPase_APLT_Neo1-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Neo1p and human putative APLT,
                     ATP9B; cd07541"
                     /db_xref="CDD:319841"
     Site            70..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            97..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            304..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            333..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            order(391..393,544,568..570,630,677..679,759,762,765,785,
                     788)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319841"
     Region          464..571
                     /region_name="Cation_ATPase"
                     /note="Cation transport ATPase (P-type); pfam13246"
                     /db_xref="CDD:463817"
     Site            842..862
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            875..893
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            924..942
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            950..972
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            979..999
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     Site            1007..1030
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75110.3)"
     CDS             1..1047
                     /gene="ATP9A"
                     /gene_synonym="ATPIIA; NEDGBA"
                     /coded_by="NM_006045.3:22..3165"
                     /db_xref="CCDS:CCDS33489.1"
                     /db_xref="GeneID:10079"
                     /db_xref="HGNC:HGNC:13540"
                     /db_xref="MIM:609126"
ORIGIN      
        1 mtdniplqpv rqkkrmdsrp ragccewlrc cgggearprt vwlghpekrd qryprnvinn
       61 qkynfftflp gvlfnqfkyf fnlyflllac sqfvpemrlg alytywvplg fvlavtvire
      121 aveeircyvr dkevnsqvys rltargtvkv kssniqvgdl iiveknqrvp admiflrtse
      181 kngscflrtd qldgetdwkl rlpvactqrl ptaadllqir syvyaeepni dihnfvgtft
      241 redsdppise slsientlwa gtvvasgtvv gvvlytgrel rsvmntsnpr skiglfdlev
      301 ncltkilfga lvvvslvmva lqhfagrwyl qiirflllfs niipislrvn ldmgkivysw
      361 virrdskipg tvvrsstipe qlgrisyllt dktgtltqne mifkrlhlgt vaygldsmde
      421 vqshifsiyt qqsqdppaqk gptlttkvrr tmssrvheav kaialchnvt pvyesngvtd
      481 qaeaekqyed scrvyqassp devalvqwte svgltlvgrd qssmqlrtpg dqilnftilq
      541 ifpftyeskr mgiivrdest geitfymkga dvvmagivqy ndwleeecgn mareglrvlv
      601 vakkslaeeq yqdfearyvq aklsvhdrsl kvatviesle memellcltg vedqlqadvr
      661 ptletlrnag ikvwmltgdk letatctakn ahlvtrnqdi hvfrlvtnrg eahlelnafr
      721 rkhdcalvis gdslevclky yeyefmelac qcpavvccrc aptqkaqivr llqertgklt
      781 cavgdggndv smiqesdcgv gvegkegkqa slaadfsitq fkhlgrllmv hgrnsykrsa
      841 alsqfvihrs lcistmqavf ssvfyfasvp lyqgfliigy stiytmfpvf slvldkdvks
      901 evamlypely kdllkgrpls yktfliwvli siyqgstimy galllfesef vhivaisfts
      961 liltellmva ltiqtwhwlm tvaellslac yiaslvflhe fidvyfiatl sflwkvsvit
     1021 lvsclplyvl kylrrrfspp sysklts
//
LOCUS       NP_001273355             574 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-capping enzyme isoform b [Homo sapiens].
ACCESSION   NP_001273355 XP_005248824
VERSION     NP_001273355.1
DBSOURCE    REFSEQ: accession NM_001286426.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Lombardi,O., Varshney,D., Phillips,N.M. and Cowling,V.H.
  TITLE     c-Myc deregulation induces mRNA capping enzyme dependency
  JOURNAL   Oncotarget 7 (50), 82273-82288 (2016)
   PUBMED   27756891
  REMARK    GeneRIF: c-Myc deregulation induces mRNA capping enzyme dependency
            in tumor cells.
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Mukherjee,C., Bakthavachalu,B. and Schoenberg,D.R.
  TITLE     The cytoplasmic capping complex assembles on adapter protein nck1
            bound to the proline-rich C-terminus of Mammalian capping enzyme
  JOURNAL   PLoS Biol 12 (8), e1001933 (2014)
   PUBMED   25137142
  REMARK    GeneRIF: These results identify a new domain of CE that is specific
            to its function in cytoplasmic capping, and a new role for Nck1 in
            regulating gene expression through its role as the scaffold for
            assembly of the cytoplasmic capping complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Niikura,Y. and Mizumoto,K.
  TITLE     Cloning and characterization of three human cDNAs encoding mRNA
            (guanine-7-)-methyltransferase, an mRNA cap methylase
  JOURNAL   Biochem Biophys Res Commun 251 (1), 27-34 (1998)
   PUBMED   9790902
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Pillutla,R.C., Yue,Z., Maldonado,E. and Shatkin,A.J.
  TITLE     Recombinant human mRNA cap methyltransferase binds capping
            enzyme/RNA polymerase IIo complexes
  JOURNAL   J Biol Chem 273 (34), 21443-21446 (1998)
   PUBMED   9705270
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Yamada-Okabe,T., Doi,R., Shimmi,O., Arisawa,M. and Yamada-Okabe,H.
  TITLE     Isolation and characterization of a human cDNA for mRNA 5'-capping
            enzyme
  JOURNAL   Nucleic Acids Res 26 (7), 1700-1706 (1998)
   PUBMED   9512541
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Murakoshi,T., Suzuki,M., Nakamura,A.,
            Gotoh,H. and Mizumoto,K.
  TITLE     Cloning and characterization of two human cDNAs encoding the mRNA
            capping enzyme
  JOURNAL   Biochem Biophys Res Commun 243 (1), 101-108 (1998)
   PUBMED   9473487
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Yue,Z., Maldonado,E., Pillutla,R., Cho,H., Reinberg,D. and
            Shatkin,A.J.
  TITLE     Mammalian capping enzyme complements mutant Saccharomyces
            cerevisiae lacking mRNA guanylyltransferase and selectively binds
            the elongating form of RNA polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12898-12903 (1997)
   PUBMED   9371772
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP256840.1, AB009023.1, BX537450.1, BC019954.1, AI193199.1 and
            BP396964.1.
            
            On Nov 5, 2013 this sequence version replaced XP_005248824.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1, resulting in
            an isoform (b) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.46989.1,
                                           SRR1660809.238709.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..574
                     /product="mRNA-capping enzyme isoform b"
                     /EC_number="2.7.7.50"
                     /EC_number="3.6.1.74"
                     /note="mRNA-capping enzyme; HCAP1; mRNA
                     guanylyltransferase; mRNA 5'-triphosphate monophosphatase"
                     /calculated_mol_wt=65911
     Region          9..175
                     /region_name="Mce1_N"
                     /note="N-terminal triphosphatase domain of mRNA capping
                     enzyme; cd17664"
                     /db_xref="CDD:350502"
     Region          248..438
                     /region_name="Adenylation_mRNA_capping"
                     /note="Adenylation domain of GTP-dependent mRNA capping
                     enzymes; cd07895"
                     /db_xref="CDD:185706"
     Site            order(271..273,292,294,299,345,362,413,433,435,437)
                     /site_type="active"
                     /db_xref="CDD:185706"
     Site            order(290,358,378..379,381..383,385,409,412,415..416)
                     /site_type="active"
                     /note="CTD docking site [active]"
                     /db_xref="CDD:185706"
     Region          442..535
                     /region_name="mRNA_cap_C"
                     /note="mRNA capping enzyme, C-terminal domain; pfam03919"
                     /db_xref="CDD:461093"
     CDS             1..574
                     /gene="RNGTT"
                     /gene_synonym="CAP1A; hCAP; HCE; HCE1"
                     /coded_by="NM_001286426.2:210..1934"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS69153.1"
                     /db_xref="GeneID:8732"
                     /db_xref="HGNC:HGNC:10073"
                     /db_xref="MIM:603512"
ORIGIN      
        1 mahnkipprw lncprrgqpv agrflplktm lgprydsqva eenrfhpsml snylkslkvk
       61 mgllvdltnt srfydrndie kegikyiklq ckghgecptt entetfirlc erfnernppe
      121 ligvhcthgf nrtgflicaf lvekmdwsie aavatfaqar ppgiykgdyl kelfrrygdi
      181 eeappppllp dwcfeddede dededgkkes epgssasfgk rrkerlklga iflegvtvkg
      241 vtqvttqpkl gevqqkchqf cgwegsgfpg aqpvsmdkqn iklldlkpyk vswkadgtry
      301 mmlidgtnev fmidrdnsvf hvsnlefpfr kdlrmhlsnt lldgemiidr vngqavpryl
      361 iydiikfnsq pvgdcdfnvr lqciereiis prhekmktgl idktqepfsv rnkpffdict
      421 srkkykpgrc ddilkwkpps lnsvdfrlki trmggegllp qnvgllyvgg yerpfaqikv
      481 tkelkqydnk iieckfenns wvfmrqrtdk sfpnayntam avcnsisnpv tkemlfefid
      541 rctaasqgqk rkhhldpdte lmpppppkrp rplt
//
LOCUS       NP_001394028             121 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform l [Homo sapiens].
ACCESSION   NP_001394028
VERSION     NP_001394028.1
DBSOURCE    REFSEQ: accession NM_001407099.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.226441.1,
                                           SRR14038197.1306224.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..121
                     /product="protein max isoform l"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=13911
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..121
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407099.1:179..544"
                     /note="isoform l is encoded by transcript variant 17"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg alpavgitpg irclkralrs lewnvlwese
      121 s
//
LOCUS       NP_997510                668 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_997510
VERSION     NP_997510.1
DBSOURCE    REFSEQ: accession NM_207627.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF323660.1, BC029158.1 and
            X91249.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (5) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF323660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..668
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 5"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=74480
     Region          62..668
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     CDS             1..668
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_207627.2:261..2267"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS42937.1"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 mlgtqgwtkq rkpcpqnass ysaemtepks vcvsvdevvs snmeatetdl lnghlkkvdn
       61 nlteaqrfss lprraavnie frdlsysvpe gpwwrkkgyk tllkgisgkf nsgelvaimg
      121 psgagkstlm nilagyretg mkgavlingl prdlrcfrkv scyimqddml lphltvqeam
      181 mvsahlklqe kdegrremvk eiltalglls cantrtgsls ggqrkrlaia lelvnnppvm
      241 ffdeptsgld sascfqvvsl mkglaqggrs iictihqpsa klfelfdqly vlsqgqcvyr
      301 gkvcnlvpyl rdlglncpty hnpadfvmev asgeygdqns rlvravregm cdsdhkrdlg
      361 gdaevnpflw hrpseedsss megchsfsas cltqfcilfk rtflsimrds vlthlritsh
      421 igiglligll ylgigneakk vlsnsgflff smlflmfaal mptvltfple mgvflrehln
      481 ywyslkayyl aktmadvpfq imfpvaycsi vywmtsqpsd avrfvlfaal gtmtslvaqs
      541 lglligaast slqvatfvgp vtaipvllfs gffvsfdtip tylqwmsyis yvrygfegvi
      601 lsiygldred lhcdidetch fqkseailre ldvenaklyl dfivlgiffi slrliayfvl
      661 rykiraer
//
LOCUS       NP_001394036              97 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform i [Homo sapiens].
ACCESSION   NP_001394036
VERSION     NP_001394036.1
DBSOURCE    REFSEQ: accession NM_001407107.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2392639.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..97
                     /product="protein max isoform i"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10571
     CDS             1..97
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407107.1:281..574"
                     /note="isoform i is encoded by transcript variant 25"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mlfwsskgka radqvlcswg ihfssslmed askrkfrale karssaqlqt nypssdnsly
       61 tnakgstisa fdggsdssse sepeepqsrk klrmeas
//
LOCUS       NP_665894                893 aa            linear   PRI 20-NOV-2025
DEFINITION  p53-induced death domain-containing protein 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_665894
VERSION     NP_665894.2
DBSOURCE    REFSEQ: accession NM_145887.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Comtois,F., Jacques,J.F., Metayer,L., Ouedraogo,W.Y.D.,
            Ouangraoua,A., Denault,J.B. and Roucou,X.
  TITLE     Noncanonical altPIDD1 protein: unveiling the true major
            translational output of the PIDD1 gene
  JOURNAL   Life Sci Alliance 8 (2), e202402910 (2024)
   PUBMED   39532532
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Garcia-Carpio,I., Braun,V.Z., Weiler,E.S., Leone,M., Ninerola,S.,
            Barco,A., Fava,L.L. and Villunger,A.
  TITLE     Extra centrosomes induce PIDD1-mediated inflammation and
            immunosurveillance
  JOURNAL   EMBO J 42 (20), e113510 (2023)
   PUBMED   37530438
  REMARK    GeneRIF: Extra centrosomes induce PIDD1-mediated inflammation and
            immunosurveillance.
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Ha,H.J. and Park,H.H.
  TITLE     Molecular basis of neurodevelopmental disorders caused by
            pathogenic variants of PIDD
  JOURNAL   Biochem Biophys Res Commun 645, 147-153 (2023)
   PUBMED   36689811
  REMARK    GeneRIF: Molecular basis of neurodevelopmental disorders caused by
            pathogenic variants of PIDD.
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Zaki,M.S., Accogli,A., Mirzaa,G., Rahman,F., Mohammed,H.,
            Porras-Hurtado,G.L., Efthymiou,S., Maqbool,S., Shukla,A.,
            Vincent,J.B., Hussain,A., Mir,A., Beetz,C., Leubauer,A.,
            Houlden,H., Gleeson,J.G. and Maroofian,R.
  TITLE     Pathogenic variants in PIDD1 lead to an autosomal recessive
            neurodevelopmental disorder with pachygyria and psychiatric
            features
  JOURNAL   Eur J Hum Genet 29 (8), 1226-1234 (2021)
   PUBMED   34163010
  REMARK    GeneRIF: Pathogenic variants in PIDD1 lead to an autosomal
            recessive neurodevelopmental disorder with pachygyria and
            psychiatric features.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Sheikh,T.I., Vasli,N., Pastore,S., Kharizi,K., Harripaul,R.,
            Fattahi,Z., Pande,S., Naeem,F., Hussain,A., Mir,A., Islam,O.,
            Girisha,K.M., Irfan,M., Ayub,M., Schwarzer,C., Najmabadi,H.,
            Shukla,A., Sladky,V.C., Braun,V.Z., Garcia-Carpio,I., Villunger,A.
            and Vincent,J.B.
  TITLE     Biallelic mutations in the death domain of PIDD1 impair caspase-2
            activation and are associated with intellectual disability
  JOURNAL   Transl Psychiatry 11 (1), 1 (2021)
   PUBMED   33414379
  REMARK    GeneRIF: Biallelic mutations in the death domain of PIDD1 impair
            caspase-2 activation and are associated with intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Vakifahmetoglu,H., Olsson,M., Orrenius,S. and Zhivotovsky,B.
  TITLE     Functional connection between p53 and caspase-2 is essential for
            apoptosis induced by DNA damage
  JOURNAL   Oncogene 25 (41), 5683-5692 (2006)
   PUBMED   16652156
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Janssens,S., Tinel,A., Lippens,S. and Tschopp,J.
  TITLE     PIDD mediates NF-kappaB activation in response to DNA damage
  JOURNAL   Cell 123 (6), 1079-1092 (2005)
   PUBMED   16360037
  REMARK    GeneRIF: PIDD plays a critical role in DNA-damage-induced NF-kappaB
            activation, controlling the balance between life and death upon DNA
            damage.
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Tinel,A. and Tschopp,J.
  TITLE     The PIDDosome, a protein complex implicated in activation of
            caspase-2 in response to genotoxic stress
  JOURNAL   Science 304 (5672), 843-846 (2004)
   PUBMED   15073321
  REMARK    GeneRIF: activation of caspase-2 occurs in a complex that contains
            PIDD, whose expression is induced by p53, and RAIDD; increased PIDD
            expression resulted in spontaneous activation of caspase-2 and
            sensitization to apoptosis by genotoxic stimuli
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Lin,Y., Ma,W. and Benchimol,S.
  TITLE     Pidd, a new death-domain-containing protein, is induced by p53 and
            promotes apoptosis
  JOURNAL   Nat Genet 26 (1), 122-127 (2000)
   PUBMED   10973264
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Telliez,J.B., Bean,K.M. and Lin,L.L.
  TITLE     LRDD, a novel leucine rich repeat and death domain containing
            protein
  JOURNAL   Biochim Biophys Acta 1478 (2), 280-288 (2000)
   PUBMED   10825539
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ059356.1, CN427946.1,
            BC014904.1 and BX349115.2.
            
            On Mar 24, 2005 this sequence version replaced NP_665894.1.
            
            Summary: The protein encoded by this gene contains a leucine-rich
            repeat and a death domain. This protein has been shown to interact
            with other death domain proteins, such as Fas (TNFRSF6)-associated
            via death domain (FADD) and MAP-kinase activating death
            domain-containing protein (MADD), and thus may function as an
            adaptor protein in cell death-related signaling processes. The
            expression of the mouse counterpart of this gene has been found to
            be positively regulated by the tumor suppressor p53 and to induce
            cell apoptosis in response to DNA damage, which suggests a role for
            this gene as an effector of p53-dependent apoptosis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1,
            resulting in an isoform (3) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1910231.1,
                                           SRR14038194.3022793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..893
                     /product="p53-induced death domain-containing protein 1
                     isoform 3"
                     /note="leucine-rich repeats and death domain containing;
                     leucine-rich repeat and death domain-containing protein;
                     p53-induced protein with a death domain; p53-induced death
                     domain-containing protein 1"
                     /calculated_mol_wt=97692
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          39..63
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          64..91
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <87..>296
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          126..147
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          127..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          149..171
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          153..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..194
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          173..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          195..216
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          196..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          218..240
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          219..241
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          241..263
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          242..264
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          264..285
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          265..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          325..416
                     /region_name="ZU5"
                     /note="ZU5 domain; cl02517"
                     /db_xref="CDD:470600"
     Region          421..453
                     /region_name="Peptidase_S68"
                     /note="Peptidase S68; pfam10461"
                     /db_xref="CDD:463098"
     Region          423..452
                     /region_name="Peptidase S68.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            445..446
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:17159900; propagated from
                     UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          465..537
                     /region_name="ZU5"
                     /note="ZU5 domain; cl02517"
                     /db_xref="CDD:470600"
     Region          566..594
                     /region_name="Peptidase S68.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            587..588
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:17159900; propagated from
                     UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          771..856
                     /region_name="Death_PIDD"
                     /note="Death Domain of p53-induced protein with a death
                     domain; cd08779"
                     /db_xref="CDD:260049"
     Site            order(779..780,782,784,809..812,815)
                     /site_type="other"
                     /note="Type III interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(784,788,791..793,796..797,804,842,844..847,850)
                     /site_type="other"
                     /note="PIDD-RAIDD interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(784,788,791..792,796..797,804,842..843)
                     /site_type="other"
                     /note="Type I interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(844..847,850)
                     /site_type="other"
                     /note="Type II interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Region          867..893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     CDS             1..893
                     /gene="PIDD1"
                     /gene_synonym="altPIDD1; LRDD; MRT75; PIDD"
                     /coded_by="NM_145887.4:129..2810"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS44508.1"
                     /db_xref="GeneID:55367"
                     /db_xref="HGNC:HGNC:16491"
                     /db_xref="MIM:605247"
ORIGIN      
        1 maatvegpel eaaaaagdas edsdagsral pflggnrlsl dlypggcqql lhlcvqqplq
       61 llqveflrls thedpqllea tlaqlpqsls clrslvlkgg qrrdtlgacl rgaltnlpag
      121 lsglahlahl dlsfnsletl pacvlqmrgl galllshncl selpealgal paltfltvth
      181 nrlqtlppal galstlqrld lsqnlldtlp peigglgsll elnlasnrlq slpaslaglr
      241 slrllvlhsn llasvpadla rlplltrldl rdnqlrdlpp elldapfvrl qgnplgeasp
      301 dapsspvaal ipemprlflt sdldsfpvtp qgcsvtlacg vrlqfpagat atpitiryrl
      361 llpepglvpl gphdallshv lelqphgvaf qqdvglwllf tppqarrcre vvvrtrndns
      421 wgdletylee eapqrlwahc qvphfswflv vsrpvsnacl vppegtllcs sghpgvkvif
      481 ppgateeprr vsmqvvrmag relqallgep eaavspllcl sqsgppsflq pvtvqlplps
      541 gitglsldrs rlhllywapp aatwdditaq vvlelthlya rfqvthfswy wlwyttkncv
      601 gglarkawer lrlhrvnlia lqrrrdpeqv llqclprnkv datlrrller yrgpepsdtv
      661 emfegeeffa afergidvda drpdcvegri cfvfyshlkn vkevsfyrga vpvrvpeeae
      721 aarqrkgada lwmatlpikl prlrgsegpr rgaglslapl nlgdaetgfl tqsnllsvag
      781 rlgldwpava lhlgvsyrev qrirhefrdd ldeqirhmlf swaerqagqp gavgllvqal
      841 eqsdrqdvae evravlelgr rkyqdsirrm glapkdpalp gssapqppep aqa
//
LOCUS       NP_997057                677 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_997057
VERSION     NP_997057.1
DBSOURCE    REFSEQ: accession NM_207174.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF323664.1, BC029158.1 and
            X91249.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (3) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF323664.1, SRR1803612.139619.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..677
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 3"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=75250
     Region          71..677
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     CDS             1..677
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_207174.1:75..2108"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13683.1"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 mrislprape rdggvsassl ldtvtnassy saemtepksv cvsvdevvss nmeatetdll
       61 nghlkkvdnn lteaqrfssl prraavnief rdlsysvpeg pwwrkkgykt llkgisgkfn
      121 sgelvaimgp sgagkstlmn ilagyretgm kgavlinglp rdlrcfrkvs cyimqddmll
      181 phltvqeamm vsahlklqek degrremvke iltalgllsc antrtgslsg gqrkrlaial
      241 elvnnppvmf fdeptsglds ascfqvvslm kglaqggrsi ictihqpsak lfelfdqlyv
      301 lsqgqcvyrg kvcnlvpylr dlglncptyh npadfvmeva sgeygdqnsr lvravregmc
      361 dsdhkrdlgg daevnpflwh rpseedsssm egchsfsasc ltqfcilfkr tflsimrdsv
      421 lthlritshi giglliglly lgigneakkv lsnsgflffs mlflmfaalm ptvltfplem
      481 gvflrehlny wyslkayyla ktmadvpfqi mfpvaycsiv ywmtsqpsda vrfvlfaalg
      541 tmtslvaqsl glligaasts lqvatfvgpv taipvllfsg ffvsfdtipt ylqwmsyisy
      601 vrygfegvil siygldredl hcdidetchf qkseailrel dvenaklyld fivlgiffis
      661 lrliayfvlr ykiraer
//
LOCUS       NP_001394032             103 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform c [Homo sapiens].
ACCESSION   NP_001394032
VERSION     NP_001394032.1
DBSOURCE    REFSEQ: accession NM_001407103.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3234595.1,
                                           SRR14478891.704724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..103
                     /product="protein max isoform c"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=11968
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     CDS             1..103
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407103.1:34..345"
                     /note="isoform c is encoded by transcript variant 21"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqge ses
//
LOCUS       NP_057188                147 aa            linear   PRI 20-NOV-2025
DEFINITION  RWD domain-containing protein 1 isoform b [Homo sapiens].
ACCESSION   NP_057188
VERSION     NP_057188.2
DBSOURCE    REFSEQ: accession NM_016104.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Grotsch,H., Kunert,M., Mooslehner,K.A., Gao,Z., Struve,D.,
            Hughes,I.A., Hiort,O. and Werner,R.
  TITLE     RWDD1 interacts with the ligand binding domain of the androgen
            receptor and acts as a coactivator of androgen-dependent
            transactivation
  JOURNAL   Mol Cell Endocrinol 358 (1), 53-62 (2012)
   PUBMED   22406838
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290727.1, CN363729.1, AK301089.1, CK817864.1 and AL121953.21.
            
            On Nov 22, 2004 this sequence version replaced NP_057188.1.
            
            Transcript Variant: This variant (2) differs in its 5' UTR, and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (b) has a shorter N-terminus,
            compared to isoform a. Variants 2 and 3 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.66366.1,
                                           SRR1803611.197340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..147
                     /product="RWD domain-containing protein 1 isoform b"
                     /note="RWD domain-containing protein 1; DRG
                     family-regulatory protein 2"
                     /calculated_mol_wt=16951
     Region          <1..23
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          <48..>101
                     /region_name="DFRP_C"
                     /note="DRG Family Regulatory Proteins, Tma46; pfam16543"
                     /db_xref="CDD:465167"
     CDS             1..147
                     /gene="RWDD1"
                     /gene_synonym="CGI-24; DFRP2; PTD013"
                     /coded_by="NM_016104.4:610..1053"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43496.1"
                     /db_xref="GeneID:51389"
                     /db_xref="HGNC:HGNC:20993"
                     /db_xref="MIM:620844"
ORIGIN      
        1 mvmiftlvta vqeklneivd qiktrreeek kqkekeaeea ekqlfhgtpv tienflnwka
       61 kfdaelleik kkrmkeeeqa gknklsgkql fetdhnldts diqfledagn nvevdeslfq
      121 emddleledd eddpdynpad pesdsad
//
LOCUS       NP_001316153             703 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 7 [Homo sapiens].
ACCESSION   NP_001316153 XP_016872902
VERSION     NP_001316153.1
DBSOURCE    REFSEQ: accession NM_001329224.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 703)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6 and EU794613.1.
            
            On Jul 8, 2016 this sequence version replaced XP_016872902.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.393220.1,
                                           SRR14478891.703350.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..703
                     /product="neutral alpha-glucosidase AB isoform 7"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=79881
     Region          3..143
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            42
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          143..610
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(188,301,361,374,377,410,435)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          586..654
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..703
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001329224.2:1028..3139"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 msvgldfslp gmehvygipe hadnlrlkvt eggepyrlyn ldvfqyelyn pmalygsvpv
       61 llahnphrdl gifwlnaaet wvdissntag ktlfgkmmdy lqgsgetpqt dvrwmsetgi
      121 idvflllgps isdvfrqyas ltgtqalppl fslgyhqsrw nyrdeadvle vdqgfddhnl
      181 pcdviwldie hadgkryftw dpsrfpqprt mlerlaskrr klvaivdphi kvdsgyrvhe
      241 elrnlglyvk trdgsdyegw cwpgsagypd ftnptmraww anmfsydnye gsapnlfvwn
      301 dmnepsvfng pevtmlkdaq hyggwehrdv hniyglyvhm atadglrqrs ggmerpfvla
      361 raffagsqrf gavwtgdnta ewdhlkisip mclslglvgl sfcgadvggf fknpepellv
      421 rwyqmgayqp ffrahahldt grrepwllps qhndiirdal gqrysllpfw ytllyqahre
      481 gipvmrplwv qypqdvttfn iddqyllgda llvhpvsdsg ahgvqvylpg qgevwydiqs
      541 yqkhhgpqtl ylpvtlssip vfqrggtivp rwmrvrrsse cmkddpitlf valspqgtaq
      601 gelflddght fnyqtrqefl lrrfsfsgnt lvsssadpeg hfetpiwier vviigagkpa
      661 avvlqtkgsp esrlsfqhdp etsvlvlrkp ginvasdwsi hlr
//
LOCUS       NP_001307344              97 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform i [Homo sapiens].
ACCESSION   NP_001307344
VERSION     NP_001307344.1
DBSOURCE    REFSEQ: accession NM_001320415.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833643.1 and BC025685.1.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (11) contains an alternate
            internal exon in its 5' coding region resulting in a frameshift
            compared to variant 1. The encoded isoform (i) has a shorter and
            distinct N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833643.1, SRR3476690.980266.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..97
                     /product="protein max isoform i"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10571
     CDS             1..97
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001320415.2:453..746"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS81813.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mlfwsskgka radqvlcswg ihfssslmed askrkfrale karssaqlqt nypssdnsly
       61 tnakgstisa fdggsdssse sepeepqsrk klrmeas
//
LOCUS       NP_001394026             130 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform j [Homo sapiens].
ACCESSION   NP_001394026
VERSION     NP_001394026.1
DBSOURCE    REFSEQ: accession NM_001407097.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.412305.1,
                                           SRR14038194.1575866.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..130
                     /product="protein max isoform j"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=14984
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..130
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407097.1:179..571"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqga lpavgitpgi rclkralrsl
      121 ewnvlweses
//
LOCUS       NP_665893                910 aa            linear   PRI 20-NOV-2025
DEFINITION  p53-induced death domain-containing protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_665893
VERSION     NP_665893.2
DBSOURCE    REFSEQ: accession NM_145886.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 910)
  AUTHORS   Comtois,F., Jacques,J.F., Metayer,L., Ouedraogo,W.Y.D.,
            Ouangraoua,A., Denault,J.B. and Roucou,X.
  TITLE     Noncanonical altPIDD1 protein: unveiling the true major
            translational output of the PIDD1 gene
  JOURNAL   Life Sci Alliance 8 (2), e202402910 (2024)
   PUBMED   39532532
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 910)
  AUTHORS   Garcia-Carpio,I., Braun,V.Z., Weiler,E.S., Leone,M., Ninerola,S.,
            Barco,A., Fava,L.L. and Villunger,A.
  TITLE     Extra centrosomes induce PIDD1-mediated inflammation and
            immunosurveillance
  JOURNAL   EMBO J 42 (20), e113510 (2023)
   PUBMED   37530438
  REMARK    GeneRIF: Extra centrosomes induce PIDD1-mediated inflammation and
            immunosurveillance.
REFERENCE   3  (residues 1 to 910)
  AUTHORS   Ha,H.J. and Park,H.H.
  TITLE     Molecular basis of neurodevelopmental disorders caused by
            pathogenic variants of PIDD
  JOURNAL   Biochem Biophys Res Commun 645, 147-153 (2023)
   PUBMED   36689811
  REMARK    GeneRIF: Molecular basis of neurodevelopmental disorders caused by
            pathogenic variants of PIDD.
REFERENCE   4  (residues 1 to 910)
  AUTHORS   Zaki,M.S., Accogli,A., Mirzaa,G., Rahman,F., Mohammed,H.,
            Porras-Hurtado,G.L., Efthymiou,S., Maqbool,S., Shukla,A.,
            Vincent,J.B., Hussain,A., Mir,A., Beetz,C., Leubauer,A.,
            Houlden,H., Gleeson,J.G. and Maroofian,R.
  TITLE     Pathogenic variants in PIDD1 lead to an autosomal recessive
            neurodevelopmental disorder with pachygyria and psychiatric
            features
  JOURNAL   Eur J Hum Genet 29 (8), 1226-1234 (2021)
   PUBMED   34163010
  REMARK    GeneRIF: Pathogenic variants in PIDD1 lead to an autosomal
            recessive neurodevelopmental disorder with pachygyria and
            psychiatric features.
REFERENCE   5  (residues 1 to 910)
  AUTHORS   Sheikh,T.I., Vasli,N., Pastore,S., Kharizi,K., Harripaul,R.,
            Fattahi,Z., Pande,S., Naeem,F., Hussain,A., Mir,A., Islam,O.,
            Girisha,K.M., Irfan,M., Ayub,M., Schwarzer,C., Najmabadi,H.,
            Shukla,A., Sladky,V.C., Braun,V.Z., Garcia-Carpio,I., Villunger,A.
            and Vincent,J.B.
  TITLE     Biallelic mutations in the death domain of PIDD1 impair caspase-2
            activation and are associated with intellectual disability
  JOURNAL   Transl Psychiatry 11 (1), 1 (2021)
   PUBMED   33414379
  REMARK    GeneRIF: Biallelic mutations in the death domain of PIDD1 impair
            caspase-2 activation and are associated with intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 910)
  AUTHORS   Vakifahmetoglu,H., Olsson,M., Orrenius,S. and Zhivotovsky,B.
  TITLE     Functional connection between p53 and caspase-2 is essential for
            apoptosis induced by DNA damage
  JOURNAL   Oncogene 25 (41), 5683-5692 (2006)
   PUBMED   16652156
REFERENCE   7  (residues 1 to 910)
  AUTHORS   Janssens,S., Tinel,A., Lippens,S. and Tschopp,J.
  TITLE     PIDD mediates NF-kappaB activation in response to DNA damage
  JOURNAL   Cell 123 (6), 1079-1092 (2005)
   PUBMED   16360037
  REMARK    GeneRIF: PIDD plays a critical role in DNA-damage-induced NF-kappaB
            activation, controlling the balance between life and death upon DNA
            damage.
REFERENCE   8  (residues 1 to 910)
  AUTHORS   Tinel,A. and Tschopp,J.
  TITLE     The PIDDosome, a protein complex implicated in activation of
            caspase-2 in response to genotoxic stress
  JOURNAL   Science 304 (5672), 843-846 (2004)
   PUBMED   15073321
  REMARK    GeneRIF: activation of caspase-2 occurs in a complex that contains
            PIDD, whose expression is induced by p53, and RAIDD; increased PIDD
            expression resulted in spontaneous activation of caspase-2 and
            sensitization to apoptosis by genotoxic stimuli
REFERENCE   9  (residues 1 to 910)
  AUTHORS   Lin,Y., Ma,W. and Benchimol,S.
  TITLE     Pidd, a new death-domain-containing protein, is induced by p53 and
            promotes apoptosis
  JOURNAL   Nat Genet 26 (1), 122-127 (2000)
   PUBMED   10973264
REFERENCE   10 (residues 1 to 910)
  AUTHORS   Telliez,J.B., Bean,K.M. and Lin,L.L.
  TITLE     LRDD, a novel leucine rich repeat and death domain containing
            protein
  JOURNAL   Biochim Biophys Acta 1478 (2), 280-288 (2000)
   PUBMED   10825539
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF274972.1, CN427946.1,
            BX349115.2 and BQ214414.1.
            
            On Mar 24, 2005 this sequence version replaced NP_665893.1.
            
            Summary: The protein encoded by this gene contains a leucine-rich
            repeat and a death domain. This protein has been shown to interact
            with other death domain proteins, such as Fas (TNFRSF6)-associated
            via death domain (FADD) and MAP-kinase activating death
            domain-containing protein (MADD), and thus may function as an
            adaptor protein in cell death-related signaling processes. The
            expression of the mouse counterpart of this gene has been found to
            be positively regulated by the tumor suppressor p53 and to induce
            cell apoptosis in response to DNA damage, which suggests a role for
            this gene as an effector of p53-dependent apoptosis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Aug 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF274972.1, SRR14038195.694096.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000347755.10/ ENSP00000337797.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..910
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..910
                     /product="p53-induced death domain-containing protein 1
                     isoform 1"
                     /note="leucine-rich repeats and death domain containing;
                     leucine-rich repeat and death domain-containing protein;
                     p53-induced protein with a death domain; p53-induced death
                     domain-containing protein 1"
                     /calculated_mol_wt=99581
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          39..63
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          64..91
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <87..>296
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          126..147
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          127..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          149..171
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          153..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..194
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          173..195
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          195..216
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          196..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          218..240
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          219..241
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          241..263
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          242..264
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          264..285
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          265..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            305
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          325..416
                     /region_name="ZU5"
                     /note="ZU5 domain; cl02517"
                     /db_xref="CDD:470600"
     Region          421..453
                     /region_name="Peptidase_S68"
                     /note="Peptidase S68; pfam10461"
                     /db_xref="CDD:463098"
     Region          423..452
                     /region_name="Peptidase S68.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            445..446
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:17159900; propagated from
                     UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          465..537
                     /region_name="ZU5"
                     /note="ZU5 domain; cl02517"
                     /db_xref="CDD:470600"
     Region          566..594
                     /region_name="Peptidase S68.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          580..716
                     /region_name="UPA domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     Site            587..588
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:17159900; propagated from
                     UniProtKB/Swiss-Prot (Q9HB75.2)"
     Region          788..873
                     /region_name="Death_PIDD"
                     /note="Death Domain of p53-induced protein with a death
                     domain; cd08779"
                     /db_xref="CDD:260049"
     Site            order(796..797,799,801,826..829,832)
                     /site_type="other"
                     /note="Type III interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(801,805,808..810,813..814,821,859,861..864,867)
                     /site_type="other"
                     /note="PIDD-RAIDD interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(801,805,808..809,813..814,821,859..860)
                     /site_type="other"
                     /note="Type I interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Site            order(861..864,867)
                     /site_type="other"
                     /note="Type II interaction site [polypeptide binding]"
                     /db_xref="CDD:260049"
     Region          884..910
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB75.2)"
     CDS             1..910
                     /gene="PIDD1"
                     /gene_synonym="altPIDD1; LRDD; MRT75; PIDD"
                     /coded_by="NM_145886.4:129..2861"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7716.1"
                     /db_xref="GeneID:55367"
                     /db_xref="HGNC:HGNC:16491"
                     /db_xref="MIM:605247"
ORIGIN      
        1 maatvegpel eaaaaagdas edsdagsral pflggnrlsl dlypggcqql lhlcvqqplq
       61 llqveflrls thedpqllea tlaqlpqsls clrslvlkgg qrrdtlgacl rgaltnlpag
      121 lsglahlahl dlsfnsletl pacvlqmrgl galllshncl selpealgal paltfltvth
      181 nrlqtlppal galstlqrld lsqnlldtlp peigglgsll elnlasnrlq slpaslaglr
      241 slrllvlhsn llasvpadla rlplltrldl rdnqlrdlpp elldapfvrl qgnplgeasp
      301 dapsspvaal ipemprlflt sdldsfpvtp qgcsvtlacg vrlqfpagat atpitiryrl
      361 llpepglvpl gphdallshv lelqphgvaf qqdvglwllf tppqarrcre vvvrtrndns
      421 wgdletylee eapqrlwahc qvphfswflv vsrpvsnacl vppegtllcs sghpgvkvif
      481 ppgateeprr vsmqvvrmag relqallgep eaavspllcl sqsgppsflq pvtvqlplps
      541 gitglsldrs rlhllywapp aatwdditaq vvlelthlya rfqvthfswy wlwyttkncv
      601 gglarkawer lrlhrvnlia lqrrrdpeqv llqclprnkv datlrrller yrgpepsdtv
      661 emfegeeffa afergidvda drpdcvegri cfvfyshlkn vkevyvtttl dreaqavrgq
      721 vsfyrgavpv rvpeeaeaar qrkgadalwm atlpiklprl rgsegprrga glslaplnlg
      781 daetgfltqs nllsvagrlg ldwpavalhl gvsyrevqri rhefrddlde qirhmlfswa
      841 erqagqpgav gllvqaleqs drqdvaeevr avlelgrrky qdsirrmgla pkdpalpgss
      901 apqppepaqa
//
LOCUS       NP_848697                143 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptide peptidase isoform 4 [Homo sapiens].
ACCESSION   NP_848697
VERSION     NP_848697.1
DBSOURCE    REFSEQ: accession NM_178582.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Mentrup,T., Leinung,N., Patel,M., Fluhrer,R. and Schroder,B.
  TITLE     The role of SPP/SPPL intramembrane proteases in membrane protein
            homeostasis
  JOURNAL   FEBS J 291 (1), 25-44 (2024)
   PUBMED   37625440
  REMARK    GeneRIF: The role of SPP/SPPL intramembrane proteases in membrane
            protein homeostasis.
            Review article
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Yang,H., Li,Z., Wang,Z., Zhang,X., Dai,X., Zhou,G. and Ding,Q.
  TITLE     Histocompatibility Minor 13 (HM13), targeted by miR-760, exerts
            oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway
  JOURNAL   Cell Death Dis 13 (8), 728 (2022)
   PUBMED   36153332
  REMARK    GeneRIF: Histocompatibility Minor 13 (HM13), targeted by miR-760,
            exerts oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Hsu,F.F., Chou,Y.T., Chiang,M.T., Li,F.A., Yeh,C.T., Lee,W.H. and
            Chau,L.Y.
  TITLE     Signal peptide peptidase promotes tumor progression via
            facilitating FKBP8 degradation
  JOURNAL   Oncogene 38 (10), 1688-1701 (2019)
   PUBMED   30348988
  REMARK    GeneRIF: Study demonstrates that SPP is highly induced in lung and
            breast cancers and promotes tumor progression, at least in part, by
            facilitating the degradation of mTOR inhibitor FKBP8.
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Kronenberg-Versteeg,D., Eichmann,M., Russell,M.A., de Ru,A.,
            Hehn,B., Yusuf,N., van Veelen,P.A., Richardson,S.J., Morgan,N.G.,
            Lemberg,M.K. and Peakman,M.
  TITLE     Molecular Pathways for Immune Recognition of Preproinsulin Signal
            Peptide in Type 1 Diabetes
  JOURNAL   Diabetes 67 (4), 687-696 (2018)
   PUBMED   29343547
  REMARK    GeneRIF: Preproinsulin signal peptide epitopes are processed by SPP
            and loaded for HLA-guided immune recognition via pathways that are
            enhanced during type 1 diabetes pathogenesis.
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Wood,A.J., Roberts,R.G., Monk,D., Moore,G.E., Schulz,R. and
            Oakey,R.J.
  TITLE     A screen for retrotransposed imprinted genes reveals an association
            between X chromosome homology and maternal germ-line methylation
  JOURNAL   PLoS Genet 3 (2), e20 (2007)
   PUBMED   17291163
REFERENCE   7  (residues 1 to 143)
  AUTHORS   McLauchlan,J., Lemberg,M.K., Hope,G. and Martoglio,B.
  TITLE     Intramembrane proteolysis promotes trafficking of hepatitis C virus
            core protein to lipid droplets
  JOURNAL   EMBO J 21 (15), 3980-3988 (2002)
   PUBMED   12145199
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Grigorenko,A.P., Moliaka,Y.K., Korovaitseva,G.I. and Rogaev,E.I.
  TITLE     Novel class of polytopic proteins with domains associated with
            putative protease activity
  JOURNAL   Biochemistry (Mosc) 67 (7), 826-835 (2002)
   PUBMED   12139484
  REMARK    GeneRIF: identification and molecular cloning; expression analysis
            of the hIMP1 gene (located on chromosome 20) was performed in human
            cell tissues and transfected cell cultures [IMP1]
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Weihofen,A., Binns,K., Lemberg,M.K., Ashman,K. and Martoglio,B.
  TITLE     Identification of signal peptide peptidase, a presenilin-type
            aspartic protease
  JOURNAL   Science 296 (5576), 2215-2218 (2002)
   PUBMED   12077416
  REMARK    GeneRIF: identified human signal peptide peptidase as a polytopic
            membrane protein with sequence motifs characteristic of the
            presenilin-type aspartic proteases [SPP]
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Lemberg,M.K., Bland,F.A., Weihofen,A., Braud,V.M. and Martoglio,B.
  TITLE     Intramembrane proteolysis of signal peptides: an essential step in
            the generation of HLA-E epitopes
  JOURNAL   J Immunol 167 (11), 6441-6446 (2001)
   PUBMED   11714810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552780.1, AK074686.1,
            BU155406.1, BQ707066.1, BQ890506.1, AL110115.38 and KF456879.1.
            
            Summary: The protein encoded by this gene, which localizes to the
            endoplasmic reticulum, catalyzes intramembrane proteolysis of some
            signal peptides after they have been cleaved from a preprotein.
            This activity is required to generate signal sequence-derived human
            lymphocyte antigen-E epitopes that are recognized by the immune
            system, and to process hepatitis C virus core protein. The encoded
            protein is an integral membrane protein with sequence motifs
            characteristic of the presenilin-type aspartic proteases. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) contains an alternate segment
            compared to variant 1, that causes a frameshift. The resulting
            isoform (4) is shorter and has a distinct C-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.188317.1,
                                           SRR7346977.1997302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 17291163
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..143
                     /product="signal peptide peptidase isoform 4"
                     /EC_number="3.4.23.-"
                     /note="minor histocompatibility antigen 13; minor
                     histocompatibility antigen H13; presenilin-like protein 3;
                     signal peptide peptidase beta; intramembrane protease 1;
                     signal peptide peptidase like 1; HM13 intronic transcript
                     1"
                     /calculated_mol_wt=15301
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            20
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Region          63..>123
                     /region_name="Peptidase_A22B"
                     /note="Signal peptide peptidase; cl01342"
                     /db_xref="CDD:470165"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     CDS             1..143
                     /gene="HM13"
                     /gene_synonym="H13; HM13-IT1; IMP1; IMPAS; IMPAS-1;
                     MSTP086; PSENL3; PSL3; SPP; SPPL1"
                     /coded_by="NM_178582.3:111..542"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:81502"
                     /db_xref="HGNC:HGNC:16435"
                     /db_xref="MIM:607106"
ORIGIN      
        1 mdsalsdphn gsaeaggptn sttrppstpe gialaygsll lmallpiffg alrsvrcarg
       61 knasdmpeti tsrdaarfpi iasctllgly lffkifsqey inlllsmyff vlgilalsht
      121 irsegislqh lkqlsrepvq glg
//
LOCUS       NP_076943                176 aa            linear   PRI 20-NOV-2025
DEFINITION  telomerase RNA component interacting RNase isoform 1 [Homo
            sapiens].
ACCESSION   NP_076943
VERSION     NP_076943.1
DBSOURCE    REFSEQ: accession NM_024038.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Xie,J., Chen,Z., Zhang,X., Chen,H. and Guan,W.
  TITLE     Identification of an RNase that preferentially cleaves A/G
            nucleotides
  JOURNAL   Sci Rep 7, 45207 (2017)
   PUBMED   28322335
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000216.2.
            
            Transcript Variant: This variant (1) encodes the longest protein
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000216.2, BM925747.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242784.5/ ENSP00000242784.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..176
                     /product="telomerase RNA component interacting RNase
                     isoform 1"
                     /note="uncharacterized protein C19orf43; My029 protein;
                     exoribonuclease TRIR"
                     /calculated_mol_wt=18288
     Region          1..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ61.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ61.1)"
     CDS             1..176
                     /gene="TRIR"
                     /gene_synonym="C19orf43; fSAP18; TERCIR"
                     /coded_by="NM_024038.4:28..558"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12279.1"
                     /db_xref="GeneID:79002"
                     /db_xref="HGNC:HGNC:28424"
                     /db_xref="MIM:621422"
ORIGIN      
        1 maargrraep qgreapgpag gggggsrwae sgsgtspesg deevsgagss pvsggvnlfa
       61 ndgsflelfk rkmeeeqrqr qeepppgpqr pdqsaaaagp gdpkrkggpg stlsfvgkrr
      121 ggnklalktg ivakkqkted evltskgdaw akymaevkky kahqcgdddk trplvk
//
LOCUS       NP_065118                422 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA exonuclease 4 isoform 1 [Homo sapiens].
ACCESSION   NP_065118
VERSION     NP_065118.2
DBSOURCE    REFSEQ: accession NM_020385.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Krishnamurthy,N., Ngam,C.R., Berdis,A.J. and Montano,M.M.
  TITLE     The exonuclease activity of hPMC2 is required for transcriptional
            regulation of the QR gene and repair of estrogen-induced abasic
            sites
  JOURNAL   Oncogene 30 (47), 4731-4739 (2011)
   PUBMED   21602889
  REMARK    GeneRIF: determined that the catalytic activity of hPMC2 is
            required for repair of abasic sites that result from
            estrogen-induced DNA damage
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Montano,M.M., Wittmann,B.M. and Bianco,N.R.
  TITLE     Identification and characterization of a novel factor that
            regulates quinone reductase gene transcriptional activity
  JOURNAL   J Biol Chem 275 (44), 34306-34313 (2000)
   PUBMED   10908561
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Kwiatkowska,J., Slomski,R., Jozwiak,S., Short,M.P. and
            Kwiatkowski,D.J.
  TITLE     Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and
            evaluation as TSC1
  JOURNAL   Genomics 44 (3), 350-354 (1997)
   PUBMED   9325058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC387839.1, AL136894.1 and BC009274.2.
            
            On Oct 3, 2005 this sequence version replaced NP_065118.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF273304.1, AF295774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371942.8/ ENSP00000361010.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..422
                     /product="RNA exonuclease 4 isoform 1"
                     /note="Xenopus prevents mitotic catastrophe 2 homolog;
                     REX4 homolog, 3'-5' exonuclease; exonuclease XPMC2; XPMC2
                     prevents mitotic catastrophe 2 homolog; REX4, RNA
                     exonuclease 4 homolog"
                     /calculated_mol_wt=46541
     Region          1..194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZR2.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR2.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR2.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZR2.2)"
     Region          244..394
                     /region_name="REX4_like"
                     /note="DEDDh 3'-5' exonuclease domain of RNA exonuclease
                     4, XPMC2, Interferon Stimulated Gene product of 20 kDa,
                     and similar proteins; cd06144"
                     /db_xref="CDD:99847"
     Site            order(247..250,252,290,294,326..327,329..331,381,386)
                     /site_type="active"
                     /db_xref="CDD:99847"
     Site            order(247..250,252,290,294,326..327,329..330,381,386)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99847"
     Site            order(247,249,331,381,386)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99847"
     CDS             1..422
                     /gene="REXO4"
                     /gene_synonym="REX4; XPMC2; XPMC2H"
                     /coded_by="NM_020385.4:167..1435"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6969.1"
                     /db_xref="GeneID:57109"
                     /db_xref="HGNC:HGNC:12820"
                     /db_xref="MIM:602930"
ORIGIN      
        1 mgkakvpask rapsspvakp gpvktltrkk nkkkkrfwks karevskkpa sgpgavvrpp
       61 kapedfsqnw kalqewllkq ksqapekplv isqmgskkkp kiiqqnkket spqvkgeemp
      121 agkdqeasrg svpsgskmdr rapvprtkas gtehnkkgtk ertngdivpe rgdiehkkrk
      181 akeaapappt eediwfddvd padieaaigp eaakiarkql gqsegsvsls lvkeqafggl
      241 tralaldcem vgvgpkgees maarvsivnq ygkcvydkyv kptepvtdyr tavsgirpen
      301 lkqgeelevv qkevaemlkg rilvghalhn dlkvlfldhp kkkirdtqky kpfksqvksg
      361 rpslrllsek ilglqvqqae hcsiqdaqaa mrlyvmvkke wesmardrrp lltapdhcsd
      421 da
//
LOCUS       NP_001369593             496 aa            linear   PRI 20-NOV-2025
DEFINITION  alanine aminotransferase 1 [Homo sapiens].
ACCESSION   NP_001369593 XP_011515295
VERSION     NP_001369593.1
DBSOURCE    REFSEQ: accession NM_001382664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Fan,X., Rong,H., Wang,Y., Li,M., Song,W., Su,A. and Yu,T.
  TITLE     The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism
  JOURNAL   BMC Pregnancy Childbirth 24 (1), 26 (2024)
   PUBMED   38172739
  REMARK    GeneRIF: The correlation between serum total bile acid and alanine
            aminotransferase of pregnant women and the disorders of neonatal
            hyperbilirubinemia-related amino acid metabolism.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Zhang,C., Xu,Q., Xu,C., Yang,K., Xia,T., Hasi,W., Hao,M. and
            Kuang,H.
  TITLE     Sex Differences in the Association Between AST/ALT and Incidence of
            Type 2 Diabetes in Japanese Patients with Nonalcoholic Fatty Liver
            Disease: A Retrospective Cohort Study
  JOURNAL   Endocr Res 49 (1), 1-11 (2024)
   PUBMED   37752709
  REMARK    GeneRIF: Sex Differences in the Association Between AST/ALT and
            Incidence of Type 2 Diabetes in Japanese Patients with Nonalcoholic
            Fatty Liver Disease: A Retrospective Cohort Study.
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Qin,Y.J., Wang,Z.G., Gong,J.H., Gong,J.P. and Li,J.H.
  TITLE     Role of alanine aminotransferase in the effects of urinary caffeine
            concentration and its primary metabolite concentration on cognitive
            function in older adults: Bayesian Kernel Machine regression
            analysis and mediation analysis
  JOURNAL   Eur Rev Med Pharmacol Sci 28 (2), 721-733 (2024)
   PUBMED   38305614
  REMARK    GeneRIF: Role of alanine aminotransferase in the effects of urinary
            caffeine concentration and its primary metabolite concentration on
            cognitive function in older adults: Bayesian Kernel Machine
            regression analysis and mediation analysis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   He,S., Yu,C., Kuang,M., Qiu,J., Yang,R., Zhang,S., Sheng,G. and
            Zou,Y.
  TITLE     Alanine aminotransferase to high- density lipoprotein cholesterol
            ratio is positively correlated with the occurrence of diabetes in
            the Chinese population: a population-based cohort study
  JOURNAL   Front Endocrinol (Lausanne) 14, 1266692 (2023)
   PUBMED   38089616
  REMARK    GeneRIF: Alanine aminotransferase to high- density lipoprotein
            cholesterol ratio is positively correlated with the occurrence of
            diabetes in the Chinese population: a population-based cohort
            study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Asgari,S., Molavizadeh,D., Tohidi,M., Momenan,A.A., Azizi,F. and
            Hadaegh,F.
  TITLE     Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022
  JOURNAL   J Clin Lab Anal 37 (11-12), e24937 (2023)
   PUBMED   37403787
  REMARK    GeneRIF: Prevalence and metabolic determinants of abnormal alanine
            aminotransferase: A cross-sectional study of Iranian adults,
            2018-2022.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Ishiguro,M., Takio,K., Suzuki,M., Oyama,R., Matsuzawa,T. and
            Titani,K.
  TITLE     Complete amino acid sequence of human liver cytosolic alanine
            aminotransferase (GPT) determined by a combination of conventional
            and mass spectral methods
  JOURNAL   Biochemistry 30 (43), 10451-10457 (1991)
   PUBMED   1931970
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Rocha,J., Amorim,A., Almeida,V.M., Oliveira,J.P., Leao,M.,
            Tavares,M.C., Pereira,M.S. and Vidal-Pinheiro,L.
  TITLE     Gene dosage evidence for the regional assignment of GPT
            (glutamate-pyruvate transaminase; E.C. 2.6.1.2) locus to
            8q24.2----8qter
  JOURNAL   Hum Genet 80 (3), 299-300 (1988)
   PUBMED   3192219
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Astrin,K.H., Arredondo-Vega,F.X., Desnick,R.J. and Smith,M.
  TITLE     Assignment of the gene for cytosolic alanine aminotransferase
            (AAT1) to human chromosome 8
  JOURNAL   Ann Hum Genet 46 (2), 125-133 (1982)
   PUBMED   7114790
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Olaisen,B.
  TITLE     Genetics of the GPT system. Family, mother/child and association
            studies
  JOURNAL   Clin Genet 7 (3), 245-254 (1975)
   PUBMED   49232
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Chen,S.H. and Giblett,E.R.
  TITLE     Polymorphism of soluble glutamic-pyruvic transaminase: a new
            genetic marker in man
  JOURNAL   Science 173 (3992), 148-149 (1971)
   PUBMED   5581908
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084125.9.
            
            On May 18, 2020 this sequence version replaced XP_011515295.1.
            
            Summary: This gene encodes cytosolic alanine aminotransaminase 1
            (ALT1); also known as glutamate-pyruvate transaminase 1. This
            enzyme catalyzes the reversible transamination between alanine and
            2-oxoglutarate to generate pyruvate and glutamate and, therefore,
            plays a key role in the intermediary metabolism of glucose and
            amino acids. Serum activity levels of this enzyme are routinely
            used as a biomarker of liver injury caused by drug toxicity,
            infection, alcohol, and steatosis. A related gene on chromosome 16
            encodes a putative mitochondrial alanine
            aminotransaminase.[provided by RefSeq, Nov 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018207.1, DRR138515.31887.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: relevant for disease process
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..496
                     /product="alanine aminotransferase 1"
                     /EC_number="2.6.1.2"
                     /note="glutamic-alanine transaminase 1; glutamic--pyruvic
                     transaminase 1; alanine aminotransferase; glutamate
                     pyruvate transaminase 1; glutamic-pyruvate transaminase
                     (alanine aminotransferase); serum glutamic-pyruvic
                     transaminase; serum glutamate-pyruvate transaminase"
                     /calculated_mol_wt=54506
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:1931970; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     Region          17..496
                     /region_name="PTZ00377"
                     /note="alanine aminotransferase; Provisional"
                     /db_xref="CDD:240391"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24298.3)"
     CDS             1..496
                     /gene="GPT"
                     /gene_synonym="AAT1; ALT; ALT1; GPT1; SGPT"
                     /coded_by="NM_001382664.1:63..1553"
                     /db_xref="CCDS:CCDS6430.1"
                     /db_xref="GeneID:2875"
                     /db_xref="HGNC:HGNC:4552"
                     /db_xref="MIM:138200"
ORIGIN      
        1 masstgdrsq avrhglrakv ltldgmnprv rrveyavrgp ivqraleleq elrqgvkkpf
       61 teviranigd aqamgqrpit flrqvlalcv npdllsspnf pddakkraer ilqacgghsl
      121 gaysvssgiq liredvaryi errdggipad pnnvflstga sdaivtvlkl lvageghtrt
      181 gvlipipqyp lysatlaelg avqvdyylde erawaldvae lhralgqard hcrpralcvi
      241 npgnptgqvq trecieavir fafeerlfll adevyqdnvy aagsqfhsfk kvlmemgppy
      301 agqqelasfh stskgymgec gfrggyvevv nmdaavqqqm lklmsvrlcp pvpgqalldl
      361 vvsppaptdp sfaqfqaekq avlaelaaka klteqvfnea pgiscnpvqg amysfprvql
      421 ppraveraqe lglapdmffc lrlleetgic vvpgsgfgqr egtyhfrmti lppleklrll
      481 leklsrfhak ftleys
//
LOCUS       NP_001273357             514 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-capping enzyme isoform c [Homo sapiens].
ACCESSION   NP_001273357
VERSION     NP_001273357.1
DBSOURCE    REFSEQ: accession NM_001286428.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Lombardi,O., Varshney,D., Phillips,N.M. and Cowling,V.H.
  TITLE     c-Myc deregulation induces mRNA capping enzyme dependency
  JOURNAL   Oncotarget 7 (50), 82273-82288 (2016)
   PUBMED   27756891
  REMARK    GeneRIF: c-Myc deregulation induces mRNA capping enzyme dependency
            in tumor cells.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Mukherjee,C., Bakthavachalu,B. and Schoenberg,D.R.
  TITLE     The cytoplasmic capping complex assembles on adapter protein nck1
            bound to the proline-rich C-terminus of Mammalian capping enzyme
  JOURNAL   PLoS Biol 12 (8), e1001933 (2014)
   PUBMED   25137142
  REMARK    GeneRIF: These results identify a new domain of CE that is specific
            to its function in cytoplasmic capping, and a new role for Nck1 in
            regulating gene expression through its role as the scaffold for
            assembly of the cytoplasmic capping complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Niikura,Y. and Mizumoto,K.
  TITLE     Cloning and characterization of three human cDNAs encoding mRNA
            (guanine-7-)-methyltransferase, an mRNA cap methylase
  JOURNAL   Biochem Biophys Res Commun 251 (1), 27-34 (1998)
   PUBMED   9790902
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Pillutla,R.C., Yue,Z., Maldonado,E. and Shatkin,A.J.
  TITLE     Recombinant human mRNA cap methyltransferase binds capping
            enzyme/RNA polymerase IIo complexes
  JOURNAL   J Biol Chem 273 (34), 21443-21446 (1998)
   PUBMED   9705270
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Yamada-Okabe,T., Doi,R., Shimmi,O., Arisawa,M. and Yamada-Okabe,H.
  TITLE     Isolation and characterization of a human cDNA for mRNA 5'-capping
            enzyme
  JOURNAL   Nucleic Acids Res 26 (7), 1700-1706 (1998)
   PUBMED   9512541
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Murakoshi,T., Suzuki,M., Nakamura,A.,
            Gotoh,H. and Mizumoto,K.
  TITLE     Cloning and characterization of two human cDNAs encoding the mRNA
            capping enzyme
  JOURNAL   Biochem Biophys Res Commun 243 (1), 101-108 (1998)
   PUBMED   9473487
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Yue,Z., Maldonado,E., Pillutla,R., Cho,H., Reinberg,D. and
            Shatkin,A.J.
  TITLE     Mammalian capping enzyme complements mutant Saccharomyces
            cerevisiae lacking mRNA guanylyltransferase and selectively binds
            the elongating form of RNA polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12898-12903 (1997)
   PUBMED   9371772
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK299777.1, BX537450.1, BC019954.1, AI193199.1 and BP396964.1.
            
            Transcript Variant: This variant (3) differs in its 5' UTR, lacks a
            portion of the 5' coding region, initiates translation at a
            downstream in-frame start codon, and lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (c) is shorter at the N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299777.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..514
                     /product="mRNA-capping enzyme isoform c"
                     /EC_number="2.7.7.50"
                     /EC_number="3.6.1.74"
                     /note="mRNA-capping enzyme; HCAP1; mRNA
                     guanylyltransferase; mRNA 5'-triphosphate monophosphatase"
                     /calculated_mol_wt=58953
     Region          <1..115
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          188..378
                     /region_name="Adenylation_mRNA_capping"
                     /note="Adenylation domain of GTP-dependent mRNA capping
                     enzymes; cd07895"
                     /db_xref="CDD:185706"
     Site            order(211..213,232,234,239,285,302,353,373,375,377)
                     /site_type="active"
                     /db_xref="CDD:185706"
     Site            order(230,298,318..319,321..323,325,349,352,355..356)
                     /site_type="active"
                     /note="CTD docking site [active]"
                     /db_xref="CDD:185706"
     Region          382..475
                     /region_name="mRNA_cap_C"
                     /note="mRNA capping enzyme, C-terminal domain; pfam03919"
                     /db_xref="CDD:461093"
     CDS             1..514
                     /gene="RNGTT"
                     /gene_synonym="CAP1A; hCAP; HCE; HCE1"
                     /coded_by="NM_001286428.2:280..1824"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:8732"
                     /db_xref="HGNC:HGNC:10073"
                     /db_xref="MIM:603512"
ORIGIN      
        1 mgllvdltnt srfydrndie kegikyiklq ckghgecptt entetfirlc erfnernppe
       61 ligvhcthgf nrtgflicaf lvekmdwsie aavatfaqar ppgiykgdyl kelfrrygdi
      121 eeappppllp dwcfeddede dededgkkes epgssasfgk rrkerlklga iflegvtvkg
      181 vtqvttqpkl gevqqkchqf cgwegsgfpg aqpvsmdkqn iklldlkpyk vswkadgtry
      241 mmlidgtnev fmidrdnsvf hvsnlefpfr kdlrmhlsnt lldgemiidr vngqavpryl
      301 iydiikfnsq pvgdcdfnvr lqciereiis prhekmktgl idktqepfsv rnkpffdict
      361 srkkykpgrc ddilkwkpps lnsvdfrlki trmggegllp qnvgllyvgg yerpfaqikv
      421 tkelkqydnk iieckfenns wvfmrqrtdk sfpnayntam avcnsisnpv tkemlfefid
      481 rctaasqgqk rkhhldpdte lmpppppkrp rplt
//
LOCUS       NP_001139754             455 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle subunit SRP54 isoform 2 [Homo sapiens].
ACCESSION   NP_001139754
VERSION     NP_001139754.1
DBSOURCE    REFSEQ: accession NM_001146282.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   McCarthy,P., Cotter,M. and Smith,O.P.
  TITLE     Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features
  JOURNAL   Br J Haematol 196 (3), e39-e42 (2022)
   PUBMED   34549814
  REMARK    GeneRIF: Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Schurch,C., Schaefer,T., Muller,J.S., Hanns,P., Arnone,M.,
            Dumlin,A., Scharer,J., Sinning,I., Wild,K., Skokowa,J., Welte,K.,
            Carapito,R., Bahram,S., Konantz,M. and Lengerke,C.
  TITLE     SRP54 mutations induce congenital neutropenia via dominant-negative
            effects on XBP1 splicing
  JOURNAL   Blood 137 (10), 1340-1352 (2021)
   PUBMED   33227812
  REMARK    GeneRIF: SRP54 mutations induce congenital neutropenia via
            dominant-negative effects on XBP1 splicing.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Juaire,K.D., Lapouge,K., Becker,M.M.M., Kotova,I., Michelhans,M.,
            Carapito,R., Wild,K., Bahram,S. and Sinning,I.
  TITLE     Structural and Functional Impact of SRP54 Mutations Causing Severe
            Congenital Neutropenia
  JOURNAL   Structure 29 (1), 15-28 (2021)
   PUBMED   33053321
  REMARK    GeneRIF: Structural and Functional Impact of SRP54 Mutations
            Causing Severe Congenital Neutropenia.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Goldberg,L., Simon,A.J., Rechavi,G., Lev,A., Barel,O., Kunik,V.,
            Toren,A., Schiby,G., Tamary,H., Steinberg-Shemer,O. and Somech,R.
  TITLE     Congenital neutropenia with variable clinical presentation in novel
            mutation of the SRP54 gene
  JOURNAL   Pediatr Blood Cancer 67 (6), e28237 (2020)
   PUBMED   32277798
  REMARK    GeneRIF: Congenital neutropenia with variable clinical presentation
            in novel mutation of the SRP54 gene.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Bacher,G., Lutcke,H., Jungnickel,B., Rapoport,T.A. and
            Dobberstein,B.
  TITLE     Regulation by the ribosome of the GTPase of the signal-recognition
            particle during protein targeting
  JOURNAL   Nature 381 (6579), 248-251 (1996)
   PUBMED   8622769
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Patel,S. and Austen,B.
  TITLE     Sequence of the highly conserved gene encoding the human 54kDa
            subunit of signal recognition particle
  JOURNAL   DNA Seq 6 (3), 167-170 (1996)
   PUBMED   8722571
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Miller,J.D., Wilhelm,H., Gierasch,L., Gilmore,R. and Walter,P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle
            during initiation of protein translocation
  JOURNAL   Nature 366 (6453), 351-354 (1993)
   PUBMED   8247130
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA495064.1, AK300824.1 and BC000652.2.
            
            Transcript Variant: This variant (2) lacks a portion of the 5'
            coding region and uses a distinct translational start codon,
            compared to variant 1. The resulting isoform (2) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300824.1, SRR7346977.936925.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..455
                     /product="signal recognition particle subunit SRP54
                     isoform 2"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 54 kDa protein; signal
                     recognition particle 54kD; signal recognition particle
                     54kDa; signal recognition particle subunit SRP54; SRP54
                     GTPase"
                     /calculated_mol_wt=50239
     Region          8..381
                     /region_name="SRP54_euk"
                     /note="signal recognition particle protein SRP54;
                     TIGR01425"
                     /db_xref="CDD:273615"
     CDS             1..455
                     /gene="SRP54"
                     /gene_synonym="SCN8"
                     /coded_by="NM_001146282.2:313..1680"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6729"
                     /db_xref="HGNC:HGNC:11301"
                     /db_xref="MIM:604857"
ORIGIN      
        1 mpplsmkrsa idleemasgl nkrkmiqhav fkelvklvdp gvkawtptkg kqnvimfvgl
       61 qgsgktttcs klayyyqrkg wktclicadt fragafdqlk qnatkaripf ygsytemdpv
      121 iiasegvekf knenfeiiiv dtsgrhkqed slfeemlqva naiqpdnivy vmdasigqac
      181 eaqakafkdk vdvasvivtk ldghakggga lsavaatksp iifigtgehi ddfepfktqp
      241 fiskllgmgd ieglidkvne lklddneali eklkhgqftl rdmyeqfqni mkmgpfsqil
      301 gmipgfgtdf mskgneqesm arlkklmtim dsmndqelds tdgakvfskq pgriqrvarg
      361 sgvstrdvqe lltqytkfaq mvkkmggikg lfkggdmskn vsqsqmakln qqmakmmdpr
      421 vlhhmggmag lqsmmrqfqq gaagnmkgmm gfnnm
//
LOCUS       NP_001394039              94 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform m [Homo sapiens].
ACCESSION   NP_001394039
VERSION     NP_001394039.1
DBSOURCE    REFSEQ: accession NM_001407110.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 94)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 94)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 94)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 94)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803617.243322.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2144333 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 1566084
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..94
                     /product="protein max isoform m"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10895
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..94
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407110.1:34..318"
                     /note="isoform m is encoded by transcript variant 28"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg eses
//
LOCUS       NP_001394029             121 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform l [Homo sapiens].
ACCESSION   NP_001394029
VERSION     NP_001394029.1
DBSOURCE    REFSEQ: accession NM_001407100.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2099317.1,
                                           SRR7346977.993410.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..121
                     /product="protein max isoform l"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=13911
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..121
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407100.1:179..544"
                     /note="isoform l is encoded by transcript variant 18"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg alpavgitpg irclkralrs lewnvlwese
      121 s
//
LOCUS       NP_001399721             557 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001399721
VERSION     NP_001399721.1
DBSOURCE    REFSEQ: accession NM_001412792.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125491.1 and AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3762551.1,
                                           SRR18074968.441875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150585 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..557
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 6"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=62228
     Region          1..218
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:10777694"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Region          74..>554
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     CDS             1..557
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412792.1:189..1862"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvemkqlq ksykaladqm nlilskrlwy imieqflmky vwsssglimv
      361 aipiitatgf adgedgqkqv mvserteaft tarnllasga daierimssy kevtelagyt
      421 arvynmfwvf devkrgiykr taviqesesh skngakvelp lsdtlaikgk vidvdhgiic
      481 envpiitpag evvasrlnfk veegmhllit gpngcgkssl frilsglwpv yegvlykppp
      541 qhmfyipqrm hyglkrs
//
LOCUS       NP_001265122             830 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 5 [Homo sapiens].
ACCESSION   NP_001265122
VERSION     NP_001265122.1
DBSOURCE    REFSEQ: accession NM_001278193.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 830)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 830)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 830)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 830)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 830)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 830)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 830)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 830)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 830)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 830)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295806.1, AK314370.1 and
            D42041.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (5) has multiple differences in
            the coding region but maintains the reading frame, compared to
            variant 3. The resulting isoform (5) lacks two internal segments,
            compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295806.1, SRR1803613.80525.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..830
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..830
                     /product="neutral alpha-glucosidase AB isoform 5"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=93849
     Region          130..270
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            169
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          270..737
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(315,428,488,501,504,537,562)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          713..781
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..830
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001278193.2:15..2507"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 maavaavaar rrrlsvsgrd ensveltmae gpykiiltar pfrldlledr slllsvnarg
       61 llefehqrap rvsqgskdpa egdgaqpeet prdgdkpeet qgkaekdepg aweetfkths
      121 dskpygpmsv gldfslpgme hvygipehad nlrlkvtegg epyrlynldv fqyelynpma
      181 lygsvpvlla hnphrdlgif wlnaaetwvd issntagktl fgkmmdylqg sgetpqtdvr
      241 wmsetgiidv flllgpsisd vfrqyasltg tqalpplfsl gyhqsrwnyr deadvlevdq
      301 gfddhnlpcd viwldiehad gkryftwdps rfpqprtmle rlaskrrklv aivdphikvd
      361 sgyrvheelr nlglyvktrd gsdyegwcwp gsagypdftn ptmrawwanm fsydnyegsa
      421 pnlfvwndmn epsvfngpev tmlkdaqhyg gwehrdvhni yglyvhmata dglrqrsggm
      481 erpfvlaraf fagsqrfgav wtgdntaewd hlkisipmcl slglvglsfc gadvggffkn
      541 pepellvrwy qmgayqpffr ahahldtgrr epwllpsqhn diirdalgqr ysllpfwytl
      601 lyqahregip vmrplwvqyp qdvttfnidd qyllgdallv hpvsdsgahg vqvylpgqge
      661 vwydiqsyqk hhgpqtlylp vtlssipvfq rggtivprwm rvrrssecmk ddpitlfval
      721 spqgtaqgel flddghtfny qtrqefllrr fsfsgntlvs ssadpeghfe tpiwiervvi
      781 igagkpaavv lqtkgspesr lsfqhdpets vlvlrkpgin vasdwsihlr
//
LOCUS       NP_001266278             250 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA exonuclease 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001266278
VERSION     NP_001266278.1
DBSOURCE    REFSEQ: accession NM_001279349.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Krishnamurthy,N., Ngam,C.R., Berdis,A.J. and Montano,M.M.
  TITLE     The exonuclease activity of hPMC2 is required for transcriptional
            regulation of the QR gene and repair of estrogen-induced abasic
            sites
  JOURNAL   Oncogene 30 (47), 4731-4739 (2011)
   PUBMED   21602889
  REMARK    GeneRIF: determined that the catalytic activity of hPMC2 is
            required for repair of abasic sites that result from
            estrogen-induced DNA damage
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Montano,M.M., Wittmann,B.M. and Bianco,N.R.
  TITLE     Identification and characterization of a novel factor that
            regulates quinone reductase gene transcriptional activity
  JOURNAL   J Biol Chem 275 (44), 34306-34313 (2000)
   PUBMED   10908561
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Kwiatkowska,J., Slomski,R., Jozwiak,S., Short,M.P. and
            Kwiatkowski,D.J.
  TITLE     Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and
            evaluation as TSC1
  JOURNAL   Genomics 44 (3), 350-354 (1997)
   PUBMED   9325058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304547.1, BX333016.2 and AL136894.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' coding region and lacks two coding exons, which results
            in a region containing a frameshift, compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.227815.1,
                                           SRR3476690.198068.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..250
                     /product="RNA exonuclease 4 isoform 2"
                     /note="Xenopus prevents mitotic catastrophe 2 homolog;
                     REX4 homolog, 3'-5' exonuclease; exonuclease XPMC2; XPMC2
                     prevents mitotic catastrophe 2 homolog; REX4, RNA
                     exonuclease 4 homolog"
                     /calculated_mol_wt=28259
     Region          <114..222
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     CDS             1..250
                     /gene="REXO4"
                     /gene_synonym="REX4; XPMC2; XPMC2H"
                     /coded_by="NM_001279349.2:167..919"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS65179.1"
                     /db_xref="GeneID:57109"
                     /db_xref="HGNC:HGNC:12820"
                     /db_xref="MIM:602930"
ORIGIN      
        1 mgkakvpask rapsspvakp gpvktltrkk nkkkkrfwks karevskkpa sgpgavvrpp
       61 kapedfsqnw kalqevprwt ggrqylaprp veqstirkep rkgqmvilfq negtssirsg
      121 klrrqpqphp preelevvqk evaemlkgri lvghalhndl kvlfldhpkk kirdtqkykp
      181 fksqvksgrp slrllsekil glqvqqaehc siqdaqaamr lyvmvkkewe smardrrpll
      241 tapdhcsdda
//
LOCUS       NP_848696                426 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptide peptidase isoform 3 [Homo sapiens].
ACCESSION   NP_848696
VERSION     NP_848696.1
DBSOURCE    REFSEQ: accession NM_178581.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Mentrup,T., Leinung,N., Patel,M., Fluhrer,R. and Schroder,B.
  TITLE     The role of SPP/SPPL intramembrane proteases in membrane protein
            homeostasis
  JOURNAL   FEBS J 291 (1), 25-44 (2024)
   PUBMED   37625440
  REMARK    GeneRIF: The role of SPP/SPPL intramembrane proteases in membrane
            protein homeostasis.
            Review article
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Yang,H., Li,Z., Wang,Z., Zhang,X., Dai,X., Zhou,G. and Ding,Q.
  TITLE     Histocompatibility Minor 13 (HM13), targeted by miR-760, exerts
            oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway
  JOURNAL   Cell Death Dis 13 (8), 728 (2022)
   PUBMED   36153332
  REMARK    GeneRIF: Histocompatibility Minor 13 (HM13), targeted by miR-760,
            exerts oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Hsu,F.F., Chou,Y.T., Chiang,M.T., Li,F.A., Yeh,C.T., Lee,W.H. and
            Chau,L.Y.
  TITLE     Signal peptide peptidase promotes tumor progression via
            facilitating FKBP8 degradation
  JOURNAL   Oncogene 38 (10), 1688-1701 (2019)
   PUBMED   30348988
  REMARK    GeneRIF: Study demonstrates that SPP is highly induced in lung and
            breast cancers and promotes tumor progression, at least in part, by
            facilitating the degradation of mTOR inhibitor FKBP8.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Kronenberg-Versteeg,D., Eichmann,M., Russell,M.A., de Ru,A.,
            Hehn,B., Yusuf,N., van Veelen,P.A., Richardson,S.J., Morgan,N.G.,
            Lemberg,M.K. and Peakman,M.
  TITLE     Molecular Pathways for Immune Recognition of Preproinsulin Signal
            Peptide in Type 1 Diabetes
  JOURNAL   Diabetes 67 (4), 687-696 (2018)
   PUBMED   29343547
  REMARK    GeneRIF: Preproinsulin signal peptide epitopes are processed by SPP
            and loaded for HLA-guided immune recognition via pathways that are
            enhanced during type 1 diabetes pathogenesis.
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Wood,A.J., Roberts,R.G., Monk,D., Moore,G.E., Schulz,R. and
            Oakey,R.J.
  TITLE     A screen for retrotransposed imprinted genes reveals an association
            between X chromosome homology and maternal germ-line methylation
  JOURNAL   PLoS Genet 3 (2), e20 (2007)
   PUBMED   17291163
REFERENCE   7  (residues 1 to 426)
  AUTHORS   McLauchlan,J., Lemberg,M.K., Hope,G. and Martoglio,B.
  TITLE     Intramembrane proteolysis promotes trafficking of hepatitis C virus
            core protein to lipid droplets
  JOURNAL   EMBO J 21 (15), 3980-3988 (2002)
   PUBMED   12145199
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Grigorenko,A.P., Moliaka,Y.K., Korovaitseva,G.I. and Rogaev,E.I.
  TITLE     Novel class of polytopic proteins with domains associated with
            putative protease activity
  JOURNAL   Biochemistry (Mosc) 67 (7), 826-835 (2002)
   PUBMED   12139484
  REMARK    GeneRIF: identification and molecular cloning; expression analysis
            of the hIMP1 gene (located on chromosome 20) was performed in human
            cell tissues and transfected cell cultures [IMP1]
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Weihofen,A., Binns,K., Lemberg,M.K., Ashman,K. and Martoglio,B.
  TITLE     Identification of signal peptide peptidase, a presenilin-type
            aspartic protease
  JOURNAL   Science 296 (5576), 2215-2218 (2002)
   PUBMED   12077416
  REMARK    GeneRIF: identified human signal peptide peptidase as a polytopic
            membrane protein with sequence motifs characteristic of the
            presenilin-type aspartic proteases [SPP]
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Lemberg,M.K., Bland,F.A., Weihofen,A., Braud,V.M. and Martoglio,B.
  TITLE     Intramembrane proteolysis of signal peptides: an essential step in
            the generation of HLA-E epitopes
  JOURNAL   J Immunol 167 (11), 6441-6446 (2001)
   PUBMED   11714810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552780.1, AY169312.1 and
            AL110115.38.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene, which localizes to the
            endoplasmic reticulum, catalyzes intramembrane proteolysis of some
            signal peptides after they have been cleaved from a preprotein.
            This activity is required to generate signal sequence-derived human
            lymphocyte antigen-E epitopes that are recognized by the immune
            system, and to process hepatitis C virus core protein. The encoded
            protein is an integral membrane protein with sequence motifs
            characteristic of the presenilin-type aspartic proteases. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) contains an alternate in-frame
            exon compared to variant 1, resulting in an isoform (3) which is
            longer compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY169312.1, SRR14038193.2009361.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 17291163
            MANE Ensembl match     :: ENST00000398174.9/ ENSP00000381237.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..426
                     /product="signal peptide peptidase isoform 3"
                     /EC_number="3.4.23.-"
                     /note="minor histocompatibility antigen 13; minor
                     histocompatibility antigen H13; presenilin-like protein 3;
                     signal peptide peptidase beta; intramembrane protease 1;
                     signal peptide peptidase like 1; HM13 intronic transcript
                     1"
                     /calculated_mol_wt=46694
     Region          63..350
                     /region_name="Peptidase_A22B"
                     /note="Signal peptide peptidase; pfam04258"
                     /db_xref="CDD:282158"
     CDS             1..426
                     /gene="HM13"
                     /gene_synonym="H13; HM13-IT1; IMP1; IMPAS; IMPAS-1;
                     MSTP086; PSENL3; PSL3; SPP; SPPL1"
                     /coded_by="NM_178581.3:111..1391"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42861.1"
                     /db_xref="GeneID:81502"
                     /db_xref="HGNC:HGNC:16435"
                     /db_xref="MIM:607106"
ORIGIN      
        1 mdsalsdphn gsaeaggptn sttrppstpe gialaygsll lmallpiffg alrsvrcarg
       61 knasdmpeti tsrdaarfpi iasctllgly lffkifsqey inlllsmyff vlgilalsht
      121 ispfmnkffp asfpnrqyql lftqgsgenk eeiinyefdt kdlvclglss ivgvwyllrk
      181 hwiannlfgl afslngvell hlnnvstgci llgglfiydv fwvfgtnvmv tvaksfeapi
      241 klvfpqdlle kgleannfam lglgdvvipg ifialllrfd islkknthty fytsfaayif
      301 glgltifimh ifkhaqpall ylvpacigfp vlvalakgev temfsyessa eilphtprlt
      361 hfptvsgspa sladsmqqkl agprrrrpqn psaiyeesnp kdpaavtesk egteasaskg
      421 lekkek
//
LOCUS       NP_001394031             121 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform l [Homo sapiens].
ACCESSION   NP_001394031
VERSION     NP_001394031.1
DBSOURCE    REFSEQ: accession NM_001407102.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3236747.1,
                                           SRR1660803.200928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..121
                     /product="protein max isoform l"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=13911
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..121
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407102.1:34..399"
                     /note="isoform l is encoded by transcript variant 20"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg alpavgitpg irclkralrs lewnvlwese
      121 s
//
LOCUS       NP_002373                160 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform a [Homo sapiens].
ACCESSION   NP_002373
VERSION     NP_002373.3
DBSOURCE    REFSEQ: accession NM_002382.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833643.1, BC004516.2 and
            BC025685.1.
            
            On Jul 8, 2002 this sequence version replaced NP_002373.2.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a) which is also known as the long form.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.104760.1,
                                           SRR3476690.1114661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358664.9/ ENSP00000351490.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..160
                     /product="protein max isoform a"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=18144
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Region          81..102
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          103..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Region          152..156
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            153
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     CDS             1..160
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_002382.5:179..661"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9771.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqvr alekarssaq lqtnypssdn
      121 slytnakgst isafdggsds ssesepeepq srkklrmeas
//
LOCUS       NP_001125                609 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-fetoprotein isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001125
VERSION     NP_001125.1
DBSOURCE    REFSEQ: accession NM_001134.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Zhang,Y.F., Lin,S., Zhen,X. and Ho,M.
  TITLE     A proteomic atlas of glypican-3 interacting partners:
            Identification of alpha-fetoprotein and other extracellular
            proteins as potential immunotherapy targets in liver cancer
  JOURNAL   Proteoglycan Res 2 (4) (2024)
   PUBMED   39822733
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Liu,K., Wu,C., Zhu,M., Xu,J., Lin,B., Lin,H., Liu,Z. and Li,M.
  TITLE     Structural characteristics of alpha-fetoprotein, including
            N-glycosylation, metal ion and fatty acid binding sites
  JOURNAL   Commun Biol 7 (1), 505 (2024)
   PUBMED   38678117
  REMARK    GeneRIF: Structural characteristics of alpha-fetoprotein, including
            N-glycosylation, metal ion and fatty acid binding sites.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Yeo,Y.H., Lee,Y.T., Tseng,H.R., Zhu,Y., You,S., Agopian,V.G. and
            Yang,J.D.
  TITLE     Alpha-fetoprotein: Past, present, and future
  JOURNAL   Hepatol Commun 8 (5), e0422 (2024)
   PUBMED   38619448
  REMARK    GeneRIF: Alpha-fetoprotein: Past, present, and future.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Song,H., Wang,J., Zhang,H., Wu,Y., Wang,K., Wang,X. and Xu,X.
  TITLE     Combination of serum alpha-fetoprotein, PIVKA- and glypican-3 in
            diagnosis of hepatocellular carcinoma: a meta-analysis
  JOURNAL   Zhejiang Da Xue Xue Bao Yi Xue Ban 53 (1), 131-139 (2024)
   PUBMED   38310085
  REMARK    GeneRIF: Combination of serum alpha-fetoprotein, PIVKA- and
            glypican-3 in diagnosis of hepatocellular carcinoma: a
            meta-analysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Chaudhuri,A.G., Samanta,S., Dey,M., Raviraja,N.S. and Dey,S.
  TITLE     Role of Alpha-Fetoprotein in the Pathogenesis of Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 43 (2), 57-76 (2024)
   PUBMED   38505913
  REMARK    GeneRIF: Role of Alpha-Fetoprotein in the Pathogenesis of Cancer.
            Review article
REFERENCE   6  (residues 1 to 609)
  AUTHORS   Pucci,P., Siciliano,R., Malorni,A., Marino,G., Tecce,M.F.,
            Ceccarini,C. and Terrana,B.
  TITLE     Human alpha-fetoprotein primary structure: a mass spectrometric
            study
  JOURNAL   Biochemistry 30 (20), 5061-5066 (1991)
   PUBMED   1709810
REFERENCE   7  (residues 1 to 609)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     alpha-Fetoprotein as a carrier protein in plasma and its
            bilirubin-binding ability
  JOURNAL   Cancer Res 39 (9), 3571-3574 (1979)
   PUBMED   89900
REFERENCE   8  (residues 1 to 609)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     Copper(II)-binding ability of human alpha-fetoprotein
  JOURNAL   Cancer Res 38 (10), 3483-3486 (1978)
   PUBMED   80265
REFERENCE   9  (residues 1 to 609)
  AUTHORS   Aoyagi,Y., Ikenaka,T. and Ichida,F.
  TITLE     Comparative chemical structures of human alpha-fetoproteins from
            fetal serum and from ascites fluid of a patient with hepatoma
  JOURNAL   Cancer Res 37 (10), 3663-3667 (1977)
   PUBMED   71198
REFERENCE   10 (residues 1 to 609)
  AUTHORS   Yachnin,S., Hsu,R., Heinrikson,R.L. and Miller,J.B.
  TITLE     Studies on human alpha-fetoprotein. Isolation and characterization
            of monomeric and polymeric forms and amino-terminal sequence
            analysis
  JOURNAL   Biochim Biophys Acta 493 (2), 418-428 (1977)
   PUBMED   70228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108157.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes alpha-fetoprotein, a major plasma
            protein produced by the yolk sac and the liver during fetal life.
            Alpha-fetoprotein expression in adults is often associated with
            hepatocarcinoma and with teratoma, and has prognostic value for
            managing advanced gastric cancer. However, hereditary persistance
            of alpha-fetoprotein may also be found in individuals with no
            obvious pathology. The protein is thought to be the fetal
            counterpart of serum albumin, and the alpha-fetoprotein and albumin
            genes are present in tandem in the same transcriptional orientation
            on chromosome 4. Alpha-fetoprotein is found in monomeric as well as
            dimeric and trimeric forms, and binds copper, nickel, fatty acids
            and bilirubin. The level of alpha-fetoprotein in amniotic fluid is
            used to measure renal loss of protein to screen for spina bifida
            and anencephaly. [provided by RefSeq, Oct 2019].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: V01514.1, BC027881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750, SAMN03267752
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395792.7/ ENSP00000379138.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..609
                     /product="alpha-fetoprotein isoform 1 precursor"
                     /note="alpha-fetoglobulin; alpha-1-fetoprotein"
                     /calculated_mol_wt=66478
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2218
     mat_peptide     19..609
                     /product="Alpha-fetoprotein. /id=PRO_0000001097"
                     /note="propagated from UniProtKB/Swiss-Prot (P02771.1)"
                     /calculated_mol_wt=66478
     Region          20..204
                     /region_name="ALBUMIN"
                     /note="serum albumin; smart00103"
                     /db_xref="CDD:214517"
     Site            order(51,55,70,91,95,98,122,125..126)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            order(159,162..163,166,182,185)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Region          212..396
                     /region_name="ALBUMIN"
                     /note="serum albumin; smart00103"
                     /db_xref="CDD:214517"
     Site            order(243,247,262,281,285,288,311,314..315)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine. /id=CAR_000070;
                     propagated from UniProtKB/Swiss-Prot (P02771.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            order(351,354..355,358,374,377)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Region          404..594
                     /region_name="ALBUMIN"
                     /note="serum albumin; smart00103"
                     /db_xref="CDD:214517"
     Site            order(435,439,454,477,481,484,509,512..513)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P02771.1)"
     Site            order(549,552..553,556,572,575)
                     /site_type="binding"
                     /db_xref="CDD:237982"
     CDS             1..609
                     /gene="AFP"
                     /gene_synonym="AFPD; FETA; HPAFP"
                     /coded_by="NM_001134.3:43..1872"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3556.1"
                     /db_xref="GeneID:174"
                     /db_xref="HGNC:HGNC:317"
                     /db_xref="MIM:104150"
ORIGIN      
        1 mkwvesifli fllnftesrt lhrneygias ildsyqctae isladlatif faqfvqeaty
       61 kevskmvkda ltaiekptgd eqssgclenq lpafleelch ekeilekygh sdccsqseeg
      121 rhncflahkk ptpasiplfq vpepvtscea yeedretfmn kfiyeiarrh pflyaptill
      181 waarydkiip scckaenave cfqtkaatvt kelresslln qhacavmknf gtrtfqaitv
      241 tklsqkftkv nfteiqklvl dvahvhehcc rgdvldclqd gekimsyics qqdtlsnkit
      301 eccklttler gqciihaend ekpeglspnl nrflgdrdfn qfssgeknif lasfvheysr
      361 rhpqlavsvi lrvakgyqel lekcfqtenp lecqdkgeee lqkyiqesqa lakrscglfq
      421 klgeyylqna flvaytkkap qltsselmai trkmaataat ccqlsedkll acgegaadii
      481 ighlcirhem tpvnpgvgqc ctssyanrrp cfsslvvdet yvppafsddk fifhkdlcqa
      541 qgvalqtmkq eflinlvkqk pqiteeqlea viadfsglle kccqgqeqev cfaeegqkli
      601 sktraalgv
//
LOCUS       NP_001394977             274 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger TRAF-type-containing protein 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001394977
VERSION     NP_001394977.1
DBSOURCE    REFSEQ: accession NM_001408048.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Asif,M., Khayyat,A.I.A., Alawbathani,S., Abdullah,U., Sanner,A.,
            Georgomanolis,T., Haasters,J., Becker,K., Budde,B., Becker,C.,
            Thiele,H., Baig,S.M., Isidoro-Garcia,M., Winter,D., Pogoda,H.M.,
            Muhammad,S., Hammerschmidt,M., Kraft,F., Kurth,I., Martin,H.G.,
            Wagner,M., Nurnberg,P. and Hussain,M.S.
  TITLE     Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia
  JOURNAL   Genet Med 26 (7), 101143 (2024)
   PUBMED   38641995
  REMARK    GeneRIF: Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia.
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Desaki,R., Sawada,G., Okumura,H., Ikeda,R., Tanabe,K., Komatsu,H.,
            Mimori,K., Mori,M., Kita,Y., Uchikado,Y., Arigami,T., Uenosono,Y.,
            Owaki,T., Ishigami,S. and Natsugoe,S.
  TITLE     As a Novel Prognostic Marker, Cysteine/histidine-rich 1 (CYHR1) is
            a Therapeutic Target in Patients with Esophageal Squamous Cell
            Carcinoma
  JOURNAL   Ann Surg Oncol 24 (2), 586-593 (2017)
   PUBMED   26676980
  REMARK    GeneRIF: High CYHR1 expression is associated with Esophageal
            Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Menon,R.P., Strom,M. and Hughes,R.C.
  TITLE     Interaction of a novel cysteine and histidine-rich cytoplasmic
            protein with galectin-3 in a carbohydrate-independent manner
  JOURNAL   FEBS Lett 470 (3), 227-231 (2000)
   PUBMED   10745073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084125.9.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.28151.1,
                                           SRR11853563.32963.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..274
                     /product="zinc finger TRAF-type-containing protein 1
                     isoform 3"
                     /note="cysteine and histidine rich protein; cysteine and
                     histidine-rich protein 1; cysteine/histidine-rich 1;
                     cysteine and histidine rich 1; Zinc finger
                     TRAF-type-containing protein 1; zinc finger TRAF-type
                     containing 1"
                     /calculated_mol_wt=31629
     Region          <1..31
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          36..>97
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          119..274
                     /region_name="CYHR1_C"
                     /note="C-terminal domain of cysteine and histidine-rich
                     protein 1 and similar proteins; cd22861"
                     /db_xref="CDD:439370"
     CDS             1..274
                     /gene="ZFTRAF1"
                     /gene_synonym="CHRP; CYHR1"
                     /coded_by="NM_001408048.1:57..881"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:50626"
                     /db_xref="HGNC:HGNC:17806"
                     /db_xref="MIM:616635"
ORIGIN      
        1 mcagcfihll adarlkeeqa tcpncrceis kslccrnlav ekavselpse cgfclrqfpr
       61 sllerhqkee cqdrvtqcky krigcpwhgp fheltvheaa cahptktgse lmeildgmdq
      121 shrkemqlyn sifsllsfek igytevqfrp yrtddfitrl yyetprftvl nqtwvlkarv
      181 ndsernpnls ckrtlsfqll lkskvtaple csflllkgpy ddvrispviy hfvftnesne
      241 tdyvplpiid svecnkllaa kninlrlflf qiqk
//
LOCUS       NP_001121698             928 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex exonuclease RRP44 isoform b [Homo sapiens].
ACCESSION   NP_001121698
VERSION     NP_001121698.1
DBSOURCE    REFSEQ: accession NM_001128226.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Favasuli,V.K., Ronchetti,D., Silvestris,I., Puccio,N., Fabbiano,G.,
            Traini,V., Todoerti,K., Erratico,S., Ciarrocchi,A., Fragliasso,V.,
            Giannandrea,D., Tumiatti,F., Chiaramonte,R., Torrente,Y.,
            Finelli,P., Morelli,E., Munshi,N.C., Bolli,N., Neri,A. and
            Taiana,E.
  TITLE     DIS3 depletion in multiple myeloma causes extensive perturbation in
            cell cycle progression and centrosome amplification
  JOURNAL   Haematologica 109 (1), 231-244 (2024)
   PUBMED   37439377
  REMARK    GeneRIF: DIS3 depletion in multiple myeloma causes extensive
            perturbation in cell cycle progression and centrosome
            amplification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Johnstone,E.B., Gorsi,B., Coelho,E., Moore,B., Farr,A.M.,
            Cooper,A.R., Mardis,E.R., Rajkovic,A., Chow,C.Y., Yandell,M. and
            Welt,C.K.
  TITLE     DIS3 Variants are Associated With Primary Ovarian Insufficiency:
            Importance of Transcription/Translation in Oogenesis
  JOURNAL   J Clin Endocrinol Metab 108 (9), 2330-2335 (2023)
   PUBMED   36869713
  REMARK    GeneRIF: DIS3 Variants are Associated With Primary Ovarian
            Insufficiency: Importance of Transcription/Translation in
            Oogenesis.
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Ohguchi,Y. and Ohguchi,H.
  TITLE     DIS3: The Enigmatic Gene in Multiple Myeloma
  JOURNAL   Int J Mol Sci 24 (4), 4079 (2023)
   PUBMED   36835493
  REMARK    GeneRIF: DIS3: The Enigmatic Gene in Multiple Myeloma.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Gritti,I., Basso,V., Rinchai,D., Corigliano,F., Pivetti,S.,
            Gaviraghi,M., Rosano,D., Mazza,D., Barozzi,S., Roncador,M.,
            Parmigiani,G., Legube,G., Parazzoli,D., Cittaro,D., Bedognetti,D.,
            Mondino,A., Segalla,S. and Tonon,G.
  TITLE     Loss of ribonuclease DIS3 hampers genome integrity in myeloma by
            disrupting DNA:RNA hybrid metabolism
  JOURNAL   EMBO J 41 (22), e108040 (2022)
   PUBMED   36215697
  REMARK    GeneRIF: Loss of ribonuclease DIS3 hampers genome integrity in
            myeloma by disrupting DNA:RNA hybrid metabolism.
REFERENCE   5  (residues 1 to 928)
  AUTHORS   Fujiwara,N., Shigemoto,M., Hirayama,M., Fujita,K.I., Seno,S.,
            Matsuda,H., Nagahama,M. and Masuda,S.
  TITLE     MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of
            MTR4-sensitive substrates in the human nucleus
  JOURNAL   Nucleic Acids Res 50 (15), 8779-8806 (2022)
   PUBMED   35902094
  REMARK    GeneRIF: MPP6 stimulates both RRP6 and DIS3 to degrade a specified
            subset of MTR4-sensitive substrates in the human nucleus.
REFERENCE   6  (residues 1 to 928)
  AUTHORS   Rozenblum,E., Vahteristo,P., Sandberg,T., Bergthorsson,J.T.,
            Syrjakoski,K., Weaver,D., Haraldsson,K., Johannsdottir,H.K.,
            Vehmanen,P., Nigam,S., Golberger,N., Robbins,C., Pak,E., Dutra,A.,
            Gillander,E., Stephan,D.A., Bailey-Wilson,J., Juo,S.H., Kainu,T.,
            Arason,A., Barkardottir,R.B., Nevanlinna,H., Borg,A. and
            Kallioniemi,O.P.
  TITLE     A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
            development: identification and characterization of candidate genes
  JOURNAL   Hum Genet 110 (2), 111-121 (2002)
   PUBMED   11935316
REFERENCE   7  (residues 1 to 928)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   8  (residues 1 to 928)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 928)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 928)
  AUTHORS   Shiomi,T., Fukushima,K., Suzuki,N., Nakashima,N., Noguchi,E. and
            Nishimoto,T.
  TITLE     Human dis3p, which binds to either GTP- or GDP-Ran, complements
            Saccharomyces cerevisiae dis3
  JOURNAL   J Biochem 123 (5), 883-890 (1998)
   PUBMED   9562621
  REMARK    GeneRIF: Dis3p is identical to Rrp44p, which comprises the exosome
            involved in ribosomal RNA processing. Similar to S. cerevisiae
            Dis3p, human Dis3p enhanced RCC1-stimulated nucleotide release from
            Ran, in a dose-dependent manner, and bound to GTP- or GDP-Ran.
            GeneRIF: S. cerevisiae Dis3p is identical to Rrp44p, which
            comprises the exosome involved in ribosomal RNA processing, S.
            cerevisiae Dis3p was found to be localized in the nucleolus.
            Erratum:[J Biochem (Tokyo) 1998 Jul;124(1):250]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB023225.1, AL832266.1, AL080158.1, AL138695.13 and U79246.1.
            
            Transcript Variant: This variant (2) lacks an exon and contains an
            alternate exon in the 5' coding region, but maintains the reading
            frame, compared to variant 1. The encoded isoform (b) is shorter
            than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023225.1, SRR11853565.8313.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q21.33"
     Protein         1..928
                     /product="exosome complex exonuclease RRP44 isoform b"
                     /note="mitotic control protein dis3 homolog; exosome
                     component 11; exosome complex exonuclease RRP44; DIS3
                     exosome endoribonuclease and 3''-5'' exoribonuclease; DIS3
                     mitotic control homolog; ribosomal RNA-processing protein
                     44; DIS3 homolog, exosome endoribonuclease and 3'-5'
                     exoribonuclease"
                     /calculated_mol_wt=104910
     Region          9..167
                     /region_name="PIN_Rrp44-like"
                     /note="VapC-like PIN domain of yeast exosome subunit Rrp44
                     endoribonuclease and other eukaryotic homologs; cd09862"
                     /db_xref="CDD:350211"
     Site            order(31,36,39,129)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:350211"
     Region          176..899
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     CDS             1..928
                     /gene="DIS3"
                     /gene_synonym="2810028N01Rik; dis3p; EXOSC11; KIAA1008;
                     RRP44"
                     /coded_by="NM_001128226.3:69..2855"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45057.1"
                     /db_xref="GeneID:22894"
                     /db_xref="HGNC:HGNC:20604"
                     /db_xref="MIM:607533"
ORIGIN      
        1 mlksktflkk traggvmkiv rehylrddig cgapgcaacg gahegpalep qpqdpassvc
       61 pqphyllpdt nvllhqivsa wrpgtwasva sslrlpgsle tyveqeqgen andrndrair
      121 vaakwynehl kkmsadnqlq vifitndrrn kekaieegip aftceeyvks ltanpelidr
      181 laclseegne iesgkiifse hlplsklqqg iksgtylqgt frasrenyle atvwihgdne
      241 enkeiilqgl khlnravhed ivavellpks qwvapssvvl hdegqneedv ekeeeterml
      301 ktavsekmlk ptgrvvgiik rnwrpycgml sksdikesrr hlftpadkri pririetrqa
      361 stlegrriiv aidgwprnsr ypnghfvrnl gdvgeketet evlllehdvp hqpfsqavls
      421 flpkmpwsit ekdmknredl rhlcicsvdp pgctdiddal hcrelengnl evgvhiadvs
      481 hfirpgnald qesarrgttv ylcekridmv pellssnlcs lkcdvdrlaf sciwemnhna
      541 eilktkftks vinskaslty aeaqlridsa nmnddittsl rglnklakil kkrriekgal
      601 tlsspevrfh mdsethdpid lqtkelretn smveefmlla nisvakkihe efsehallrk
      661 hpapppsnye ilvkaarsrn leiktdtaks laesldqaes ptfpylntll rilatrcmmq
      721 avyfcsgmdn dfhhyglasp iythftspir ryadvivhrl lavaigadct ypeltdkhkl
      781 adicknlnfr hkmaqyaqra svafhtqlff kskgivseea yilfvrknai vvlipkygle
      841 gtvffeekdk pnpqliydde ipslkiedtv fhvfdkvkvk imldssnlqh qkirmslvep
      901 qipgisiptd tsnmdlngpk kkkmklgk
//
LOCUS       NP_110416                377 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptide peptidase isoform 1 [Homo sapiens].
ACCESSION   NP_110416
VERSION     NP_110416.1
DBSOURCE    REFSEQ: accession NM_030789.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Mentrup,T., Leinung,N., Patel,M., Fluhrer,R. and Schroder,B.
  TITLE     The role of SPP/SPPL intramembrane proteases in membrane protein
            homeostasis
  JOURNAL   FEBS J 291 (1), 25-44 (2024)
   PUBMED   37625440
  REMARK    GeneRIF: The role of SPP/SPPL intramembrane proteases in membrane
            protein homeostasis.
            Review article
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Yang,H., Li,Z., Wang,Z., Zhang,X., Dai,X., Zhou,G. and Ding,Q.
  TITLE     Histocompatibility Minor 13 (HM13), targeted by miR-760, exerts
            oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway
  JOURNAL   Cell Death Dis 13 (8), 728 (2022)
   PUBMED   36153332
  REMARK    GeneRIF: Histocompatibility Minor 13 (HM13), targeted by miR-760,
            exerts oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Hsu,F.F., Chou,Y.T., Chiang,M.T., Li,F.A., Yeh,C.T., Lee,W.H. and
            Chau,L.Y.
  TITLE     Signal peptide peptidase promotes tumor progression via
            facilitating FKBP8 degradation
  JOURNAL   Oncogene 38 (10), 1688-1701 (2019)
   PUBMED   30348988
  REMARK    GeneRIF: Study demonstrates that SPP is highly induced in lung and
            breast cancers and promotes tumor progression, at least in part, by
            facilitating the degradation of mTOR inhibitor FKBP8.
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Kronenberg-Versteeg,D., Eichmann,M., Russell,M.A., de Ru,A.,
            Hehn,B., Yusuf,N., van Veelen,P.A., Richardson,S.J., Morgan,N.G.,
            Lemberg,M.K. and Peakman,M.
  TITLE     Molecular Pathways for Immune Recognition of Preproinsulin Signal
            Peptide in Type 1 Diabetes
  JOURNAL   Diabetes 67 (4), 687-696 (2018)
   PUBMED   29343547
  REMARK    GeneRIF: Preproinsulin signal peptide epitopes are processed by SPP
            and loaded for HLA-guided immune recognition via pathways that are
            enhanced during type 1 diabetes pathogenesis.
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Wood,A.J., Roberts,R.G., Monk,D., Moore,G.E., Schulz,R. and
            Oakey,R.J.
  TITLE     A screen for retrotransposed imprinted genes reveals an association
            between X chromosome homology and maternal germ-line methylation
  JOURNAL   PLoS Genet 3 (2), e20 (2007)
   PUBMED   17291163
REFERENCE   7  (residues 1 to 377)
  AUTHORS   McLauchlan,J., Lemberg,M.K., Hope,G. and Martoglio,B.
  TITLE     Intramembrane proteolysis promotes trafficking of hepatitis C virus
            core protein to lipid droplets
  JOURNAL   EMBO J 21 (15), 3980-3988 (2002)
   PUBMED   12145199
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Grigorenko,A.P., Moliaka,Y.K., Korovaitseva,G.I. and Rogaev,E.I.
  TITLE     Novel class of polytopic proteins with domains associated with
            putative protease activity
  JOURNAL   Biochemistry (Mosc) 67 (7), 826-835 (2002)
   PUBMED   12139484
  REMARK    GeneRIF: identification and molecular cloning; expression analysis
            of the hIMP1 gene (located on chromosome 20) was performed in human
            cell tissues and transfected cell cultures [IMP1]
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Weihofen,A., Binns,K., Lemberg,M.K., Ashman,K. and Martoglio,B.
  TITLE     Identification of signal peptide peptidase, a presenilin-type
            aspartic protease
  JOURNAL   Science 296 (5576), 2215-2218 (2002)
   PUBMED   12077416
  REMARK    GeneRIF: identified human signal peptide peptidase as a polytopic
            membrane protein with sequence motifs characteristic of the
            presenilin-type aspartic proteases [SPP]
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Lemberg,M.K., Bland,F.A., Weihofen,A., Braud,V.M. and Martoglio,B.
  TITLE     Intramembrane proteolysis of signal peptides: an essential step in
            the generation of HLA-E epitopes
  JOURNAL   J Immunol 167 (11), 6441-6446 (2001)
   PUBMED   11714810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552780.1 and BC062595.1.
            
            Summary: The protein encoded by this gene, which localizes to the
            endoplasmic reticulum, catalyzes intramembrane proteolysis of some
            signal peptides after they have been cleaved from a preprotein.
            This activity is required to generate signal sequence-derived human
            lymphocyte antigen-E epitopes that are recognized by the immune
            system, and to process hepatitis C virus core protein. The encoded
            protein is an integral membrane protein with sequence motifs
            characteristic of the presenilin-type aspartic proteases. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008938.2, AF172086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 17291163
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..377
                     /product="signal peptide peptidase isoform 1"
                     /EC_number="3.4.23.-"
                     /note="minor histocompatibility antigen 13; minor
                     histocompatibility antigen H13; presenilin-like protein 3;
                     signal peptide peptidase beta; intramembrane protease 1;
                     signal peptide peptidase like 1; HM13 intronic transcript
                     1"
                     /calculated_mol_wt=41357
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            20
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            32..52
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Region          63..350
                     /region_name="Peptidase_A22B"
                     /note="Signal peptide peptidase; pfam04258"
                     /db_xref="CDD:282158"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            182..202
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            210..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            315..335
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Region          317..319
                     /region_name="PAL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Region          345..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TCT9.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TCT9.1)"
     CDS             1..377
                     /gene="HM13"
                     /gene_synonym="H13; HM13-IT1; IMP1; IMPAS; IMPAS-1;
                     MSTP086; PSENL3; PSL3; SPP; SPPL1"
                     /coded_by="NM_030789.4:111..1244"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13182.1"
                     /db_xref="GeneID:81502"
                     /db_xref="HGNC:HGNC:16435"
                     /db_xref="MIM:607106"
ORIGIN      
        1 mdsalsdphn gsaeaggptn sttrppstpe gialaygsll lmallpiffg alrsvrcarg
       61 knasdmpeti tsrdaarfpi iasctllgly lffkifsqey inlllsmyff vlgilalsht
      121 ispfmnkffp asfpnrqyql lftqgsgenk eeiinyefdt kdlvclglss ivgvwyllrk
      181 hwiannlfgl afslngvell hlnnvstgci llgglfiydv fwvfgtnvmv tvaksfeapi
      241 klvfpqdlle kgleannfam lglgdvvipg ifialllrfd islkknthty fytsfaayif
      301 glgltifimh ifkhaqpall ylvpacigfp vlvalakgev temfsyeesn pkdpaavtes
      361 kegteasask glekkek
//
LOCUS       NP_001394030             121 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform l [Homo sapiens].
ACCESSION   NP_001394030
VERSION     NP_001394030.1
DBSOURCE    REFSEQ: accession NM_001407101.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2186281.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..121
                     /product="protein max isoform l"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=13911
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..121
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407101.1:34..399"
                     /note="isoform l is encoded by transcript variant 19"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg alpavgitpg irclkralrs lewnvlwese
      121 s
//
LOCUS       NP_001394035              97 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform i [Homo sapiens].
ACCESSION   NP_001394035
VERSION     NP_001394035.1
DBSOURCE    REFSEQ: accession NM_001407106.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1487640.1, BG177865.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..97
                     /product="protein max isoform i"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10571
     CDS             1..97
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407106.1:248..541"
                     /note="isoform i is encoded by transcript variant 24"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mlfwsskgka radqvlcswg ihfssslmed askrkfrale karssaqlqt nypssdnsly
       61 tnakgstisa fdggsdssse sepeepqsrk klrmeas
//
LOCUS       NP_115583                657 aa            linear   PRI 20-NOV-2025
DEFINITION  uncharacterized protein C19orf44 isoform 1 [Homo sapiens].
ACCESSION   NP_115583
VERSION     NP_115583.1
DBSOURCE    REFSEQ: accession NM_032207.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Sroka,T.J., Sanwald,L.K., Prasai,A., Hoeren,J., Trivigno,V.,
            Chaumet,V., Krauss,L.M., Weber,D., Yildiz,D., von der Malsburg,K.,
            Walentek,P., Haberkant,P., Schrul,B., Feistel,K. and Mick,D.U.
  TITLE     An enzymatic cascade enables sensitive and specific proximity
            labeling proteomics in challenging biological systems
  JOURNAL   Nat Commun 16 (1), 9691 (2025)
   PUBMED   41184298
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Hussain,H.M.J., Meng,W., Li,Y., Firasat,S., Pennesi,M.E.,
            Gorin,M.B., Guan,B., Clark,R.L., Fale-Olsen,E., Al Rawi,R.,
            Agather,A., Huryn,L.A., Yang,P., Matynia,A. and Chen,R.
  TITLE     Biallelic loss-of-function variants in C19orf44 lead to retinal
            degeneration
  JOURNAL   J Med Genet 62 (11), 693-699 (2025)
   PUBMED   40744518
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Ehrenberg,M., Avraham,M., Asodu,S.S., Moye,A.R., Sangermano,R.,
            Rizel,L., Ali-Nasser,T., Sher,I., Gurwitz,D., Chao,K.R., Rivera,A.,
            Webster,A.R., Rivolta,C., Newman,H., Pras,E., Rotenstreich,Y.,
            Banin,E., Pierce,E.A., Zur,D., Arno,G., Bujakowska,K.M., Lin,S.,
            Sharon,D. and Ben-Yosef,T.
  TITLE     Biallelic null variants in C19orf44 cause a unique late-onset
            retinal dystrophy phenotype characterized by patchy perifoveal
            chorioretinal atrophy
  JOURNAL   Genet Med 27 (6), 101401 (2025)
   PUBMED   40079362
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008764.9 and AK025395.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.179031.1,
                                           SRR1660805.222521.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221671.8/ ENSP00000221671.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..657
                     /product="uncharacterized protein C19orf44 isoform 1"
                     /note="uncharacterized protein C19orf44"
                     /calculated_mol_wt=71212
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          <139..515
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          142..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXP1; propagated from
                     UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          228..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          291..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          335..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          399..522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6X5.1)"
     Region          474..641
                     /region_name="DUF4614"
                     /note="Domain of unknown function (DUF4614); pfam15391"
                     /db_xref="CDD:464698"
     CDS             1..657
                     /gene="C19orf44"
                     /gene_synonym="FCAP71"
                     /coded_by="NM_032207.4:74..2047"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12345.1"
                     /db_xref="GeneID:84167"
                     /db_xref="HGNC:HGNC:26141"
                     /db_xref="MIM:621208"
ORIGIN      
        1 masarkasrp mrdvfgdfsd vsledstmee irnfqisrnl tkiapghsrf lkrnqtldek
       61 hlllkenpvl gsgprlascr ppttasrira naalmklaql etrimnrklq rnlsdtesds
      121 mtadaglpkr adrilsggal elasqntdkt sqnqarelpv tennaqnakv srflkkkqap
      181 venispeapa gkertlqtpk qkepartfds pdsdeeemkv llgslmdssr ekntnqgfss
      241 anvseeeerk lfsvpsqlra ftvpsvelss akpsqtshlp tslaadrtlh strsradypq
      301 shvssdtash tpsvsitgaf snsvslkmgh vklvsspgrs eaetvdepvs egaddsldef
      361 rinilsldgl apavsensdl eqeeesaqrq ktagkifrae astgqdaprq aqarswasqg
      421 kaasaegdes evsehlsass asaiqqdsts smqppseapm vntvssayse dfenspslta
      481 septahskes ldrtldalse ssssvktdlp qtaesrkksg rhvtrvlvkd tavqtpdpaf
      541 tyewtkvasm aamgpalgga yvdptpianh visadaieal tayspavlal hdvlkqqlsl
      601 tqqfiqasrh lhasllrsld adsfhyhtle eakeyirchr papltmedal eevnkel
//
LOCUS       NP_001399720             641 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001399720
VERSION     NP_001399720.1
DBSOURCE    REFSEQ: accession NM_001412791.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 641)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 641)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 641)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 641)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125491.1 and AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.111933.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2154125
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..641
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 5"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=71919
     Region          1..218
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:10777694"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Region          74..586
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     CDS             1..641
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412791.1:189..2114"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvtelagy tarvynmfwv fdevkrgiyk rtaviqeses hskngakvel
      361 plsdtlaikg kvidvdhgii cenvpiitpa gevvasrlnf kveegmhlli tgpngcgkss
      421 lfrilsglwp vyegvlykpp pqhmfyipqr pymslgslrd qviypdsvdd mhdkgytdqd
      481 lerilhnvhl yhivqreggw davmdwkdvl sggekqrmgm armfyhkpky alldectsav
      541 sidvegkifq aakgagisll sithrpslwk yhthllqfdg eggwrfeqld tairltlsee
      601 kqklesqlag ipkmqqrlne lckilgedsv lktiknedet s
//
LOCUS       NP_003127                504 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle subunit SRP54 isoform 1 [Homo sapiens].
ACCESSION   NP_003127 XP_945638
VERSION     NP_003127.1
DBSOURCE    REFSEQ: accession NM_003136.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   McCarthy,P., Cotter,M. and Smith,O.P.
  TITLE     Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features
  JOURNAL   Br J Haematol 196 (3), e39-e42 (2022)
   PUBMED   34549814
  REMARK    GeneRIF: Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Schurch,C., Schaefer,T., Muller,J.S., Hanns,P., Arnone,M.,
            Dumlin,A., Scharer,J., Sinning,I., Wild,K., Skokowa,J., Welte,K.,
            Carapito,R., Bahram,S., Konantz,M. and Lengerke,C.
  TITLE     SRP54 mutations induce congenital neutropenia via dominant-negative
            effects on XBP1 splicing
  JOURNAL   Blood 137 (10), 1340-1352 (2021)
   PUBMED   33227812
  REMARK    GeneRIF: SRP54 mutations induce congenital neutropenia via
            dominant-negative effects on XBP1 splicing.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Juaire,K.D., Lapouge,K., Becker,M.M.M., Kotova,I., Michelhans,M.,
            Carapito,R., Wild,K., Bahram,S. and Sinning,I.
  TITLE     Structural and Functional Impact of SRP54 Mutations Causing Severe
            Congenital Neutropenia
  JOURNAL   Structure 29 (1), 15-28 (2021)
   PUBMED   33053321
  REMARK    GeneRIF: Structural and Functional Impact of SRP54 Mutations
            Causing Severe Congenital Neutropenia.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Goldberg,L., Simon,A.J., Rechavi,G., Lev,A., Barel,O., Kunik,V.,
            Toren,A., Schiby,G., Tamary,H., Steinberg-Shemer,O. and Somech,R.
  TITLE     Congenital neutropenia with variable clinical presentation in novel
            mutation of the SRP54 gene
  JOURNAL   Pediatr Blood Cancer 67 (6), e28237 (2020)
   PUBMED   32277798
  REMARK    GeneRIF: Congenital neutropenia with variable clinical presentation
            in novel mutation of the SRP54 gene.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Bacher,G., Lutcke,H., Jungnickel,B., Rapoport,T.A. and
            Dobberstein,B.
  TITLE     Regulation by the ribosome of the GTPase of the signal-recognition
            particle during protein targeting
  JOURNAL   Nature 381 (6579), 248-251 (1996)
   PUBMED   8622769
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Patel,S. and Austen,B.
  TITLE     Sequence of the highly conserved gene encoding the human 54kDa
            subunit of signal recognition particle
  JOURNAL   DNA Seq 6 (3), 167-170 (1996)
   PUBMED   8722571
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Miller,J.D., Wilhelm,H., Gierasch,L., Gilmore,R. and Walter,P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle
            during initiation of protein translocation
  JOURNAL   Nature 366 (6453), 351-354 (1993)
   PUBMED   8247130
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA495064.1 and BC000652.2.
            
            On Mar 4, 2006 this sequence version replaced XP_945638.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.126494.1,
                                           SRR5189658.194175.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216774.11/ ENSP00000216774.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..504
                     /product="signal recognition particle subunit SRP54
                     isoform 1"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 54 kDa protein; signal
                     recognition particle 54kD; signal recognition particle
                     54kDa; signal recognition particle subunit SRP54; SRP54
                     GTPase"
                     /calculated_mol_wt=55574
     Region          1..295
                     /region_name="NG domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     Region          2..430
                     /region_name="SRP54_euk"
                     /note="signal recognition particle protein SRP54;
                     TIGR01425"
                     /db_xref="CDD:273615"
     Region          296..504
                     /region_name="M-domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     CDS             1..504
                     /gene="SRP54"
                     /gene_synonym="SCN8"
                     /coded_by="NM_003136.4:258..1772"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9652.1"
                     /db_xref="GeneID:6729"
                     /db_xref="HGNC:HGNC:11301"
                     /db_xref="MIM:604857"
ORIGIN      
        1 mvladlgrki tsalrslsna tiineevlna mlkevctall eadvniklvk qlrenvksai
       61 dleemasgln krkmiqhavf kelvklvdpg vkawtptkgk qnvimfvglq gsgktttcsk
      121 layyyqrkgw ktclicadtf ragafdqlkq natkaripfy gsytemdpvi iasegvekfk
      181 nenfeiiivd tsgrhkqeds lfeemlqvan aiqpdnivyv mdasigqace aqakafkdkv
      241 dvasvivtkl dghakgggal savaatkspi ifigtgehid dfepfktqpf iskllgmgdi
      301 eglidkvnel klddnealie klkhgqftlr dmyeqfqnim kmgpfsqilg mipgfgtdfm
      361 skgneqesma rlkklmtimd smndqeldst dgakvfskqp griqrvargs gvstrdvqel
      421 ltqytkfaqm vkkmggikgl fkggdmsknv sqsqmaklnq qmakmmdprv lhhmggmagl
      481 qsmmrqfqqg aagnmkgmmg fnnm
//
LOCUS       NP_001309278             796 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex exonuclease RRP44 isoform d [Homo sapiens].
ACCESSION   NP_001309278 XP_005266351
VERSION     NP_001309278.1
DBSOURCE    REFSEQ: accession NM_001322349.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Favasuli,V.K., Ronchetti,D., Silvestris,I., Puccio,N., Fabbiano,G.,
            Traini,V., Todoerti,K., Erratico,S., Ciarrocchi,A., Fragliasso,V.,
            Giannandrea,D., Tumiatti,F., Chiaramonte,R., Torrente,Y.,
            Finelli,P., Morelli,E., Munshi,N.C., Bolli,N., Neri,A. and
            Taiana,E.
  TITLE     DIS3 depletion in multiple myeloma causes extensive perturbation in
            cell cycle progression and centrosome amplification
  JOURNAL   Haematologica 109 (1), 231-244 (2024)
   PUBMED   37439377
  REMARK    GeneRIF: DIS3 depletion in multiple myeloma causes extensive
            perturbation in cell cycle progression and centrosome
            amplification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Johnstone,E.B., Gorsi,B., Coelho,E., Moore,B., Farr,A.M.,
            Cooper,A.R., Mardis,E.R., Rajkovic,A., Chow,C.Y., Yandell,M. and
            Welt,C.K.
  TITLE     DIS3 Variants are Associated With Primary Ovarian Insufficiency:
            Importance of Transcription/Translation in Oogenesis
  JOURNAL   J Clin Endocrinol Metab 108 (9), 2330-2335 (2023)
   PUBMED   36869713
  REMARK    GeneRIF: DIS3 Variants are Associated With Primary Ovarian
            Insufficiency: Importance of Transcription/Translation in
            Oogenesis.
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Ohguchi,Y. and Ohguchi,H.
  TITLE     DIS3: The Enigmatic Gene in Multiple Myeloma
  JOURNAL   Int J Mol Sci 24 (4), 4079 (2023)
   PUBMED   36835493
  REMARK    GeneRIF: DIS3: The Enigmatic Gene in Multiple Myeloma.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Gritti,I., Basso,V., Rinchai,D., Corigliano,F., Pivetti,S.,
            Gaviraghi,M., Rosano,D., Mazza,D., Barozzi,S., Roncador,M.,
            Parmigiani,G., Legube,G., Parazzoli,D., Cittaro,D., Bedognetti,D.,
            Mondino,A., Segalla,S. and Tonon,G.
  TITLE     Loss of ribonuclease DIS3 hampers genome integrity in myeloma by
            disrupting DNA:RNA hybrid metabolism
  JOURNAL   EMBO J 41 (22), e108040 (2022)
   PUBMED   36215697
  REMARK    GeneRIF: Loss of ribonuclease DIS3 hampers genome integrity in
            myeloma by disrupting DNA:RNA hybrid metabolism.
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Fujiwara,N., Shigemoto,M., Hirayama,M., Fujita,K.I., Seno,S.,
            Matsuda,H., Nagahama,M. and Masuda,S.
  TITLE     MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of
            MTR4-sensitive substrates in the human nucleus
  JOURNAL   Nucleic Acids Res 50 (15), 8779-8806 (2022)
   PUBMED   35902094
  REMARK    GeneRIF: MPP6 stimulates both RRP6 and DIS3 to degrade a specified
            subset of MTR4-sensitive substrates in the human nucleus.
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Rozenblum,E., Vahteristo,P., Sandberg,T., Bergthorsson,J.T.,
            Syrjakoski,K., Weaver,D., Haraldsson,K., Johannsdottir,H.K.,
            Vehmanen,P., Nigam,S., Golberger,N., Robbins,C., Pak,E., Dutra,A.,
            Gillander,E., Stephan,D.A., Bailey-Wilson,J., Juo,S.H., Kainu,T.,
            Arason,A., Barkardottir,R.B., Nevanlinna,H., Borg,A. and
            Kallioniemi,O.P.
  TITLE     A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
            development: identification and characterization of candidate genes
  JOURNAL   Hum Genet 110 (2), 111-121 (2002)
   PUBMED   11935316
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Shiomi,T., Fukushima,K., Suzuki,N., Nakashima,N., Noguchi,E. and
            Nishimoto,T.
  TITLE     Human dis3p, which binds to either GTP- or GDP-Ran, complements
            Saccharomyces cerevisiae dis3
  JOURNAL   J Biochem 123 (5), 883-890 (1998)
   PUBMED   9562621
  REMARK    GeneRIF: Dis3p is identical to Rrp44p, which comprises the exosome
            involved in ribosomal RNA processing. Similar to S. cerevisiae
            Dis3p, human Dis3p enhanced RCC1-stimulated nucleotide release from
            Ran, in a dose-dependent manner, and bound to GTP- or GDP-Ran.
            GeneRIF: S. cerevisiae Dis3p is identical to Rrp44p, which
            comprises the exosome involved in ribosomal RNA processing, S.
            cerevisiae Dis3p was found to be localized in the nucleolus.
            Erratum:[J Biochem (Tokyo) 1998 Jul;124(1):250]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL391384.18 and AL138695.13.
            
            On Apr 11, 2016 this sequence version replaced XP_005266351.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.2624916.1,
                                           SRR14038194.4173544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q21.33"
     Protein         1..796
                     /product="exosome complex exonuclease RRP44 isoform d"
                     /note="mitotic control protein dis3 homolog; exosome
                     component 11; exosome complex exonuclease RRP44; DIS3
                     exosome endoribonuclease and 3''-5'' exoribonuclease; DIS3
                     mitotic control homolog; ribosomal RNA-processing protein
                     44; DIS3 homolog, exosome endoribonuclease and 3'-5'
                     exoribonuclease"
                     /calculated_mol_wt=90453
     Region          <3..35
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          44..767
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     CDS             1..796
                     /gene="DIS3"
                     /gene_synonym="2810028N01Rik; dis3p; EXOSC11; KIAA1008;
                     RRP44"
                     /coded_by="NM_001322349.2:623..3013"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81772.1"
                     /db_xref="GeneID:22894"
                     /db_xref="HGNC:HGNC:20604"
                     /db_xref="MIM:607533"
ORIGIN      
        1 msadnqlqvi fitndrrnke kaieegipaf tceeyvkslt anpelidrla clseegneie
       61 sgkiifsehl plsklqqgik sgtylqgtfr asrenyleat vwihgdneen keiilqglkh
      121 lnravhediv avellpksqw vapssvvlhd egqneedvek eeetermlkt avsekmlkpt
      181 grvvgiikrn wrpycgmlsk sdikesrrhl ftpadkripr irietrqast legrriivai
      241 dgwprnsryp nghfvrnlgd vgeketetev lllehdvphq pfsqavlsfl pkmpwsitek
      301 dmknredlrh lcicsvdppg ctdiddalhc relengnlev gvhiadvshf irpgnaldqe
      361 sarrgttvyl cekridmvpe llssnlcslk cdvdrlafsc iwemnhnaei lktkftksvi
      421 nskasltyae aqlridsanm nddittslrg lnklakilkk rriekgaltl sspevrfhmd
      481 sethdpidlq tkelretnsm veefmllani svakkiheef sehallrkhp apppsnyeil
      541 vkaarsrnle iktdtaksla esldqaespt fpylntllri latrcmmqav yfcsgmdndf
      601 hhyglaspiy thftspirry advivhrlla vaigadctyp eltdkhklad icknlnfrhk
      661 maqyaqrasv afhtqlffks kgivseeayi lfvrknaivv lipkyglegt vffeekdkpn
      721 pqliyddeip slkiedtvfh vfdkvkvkim ldssnlqhqk irmslvepqi pgisiptdts
      781 nmdlngpkkk kmklgk
//
LOCUS       NP_001394042              87 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform g [Homo sapiens].
ACCESSION   NP_001394042
VERSION     NP_001394042.1
DBSOURCE    REFSEQ: accession NM_001407113.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 87)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14478891.2279383.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..87
                     /product="protein max isoform g"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10251
     Region          15..>48
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..87
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407113.1:34..297"
                     /note="isoform g is encoded by transcript variant 31"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekly flfwklctpv
       61 lhrqslmqkc htfissyqvh kkkecki
//
LOCUS       NP_001394043              82 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform o [Homo sapiens].
ACCESSION   NP_001394043
VERSION     NP_001394043.1
DBSOURCE    REFSEQ: accession NM_001407114.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 82)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 82)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..82
                     /product="protein max isoform o"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=9093
     CDS             1..82
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407114.1:54..302"
                     /note="isoform o is encoded by transcript variant 32"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mlsvkitsif siffflsysr ksnrgfnlrl tngliimhwn envgttskta ftvcgtqshh
       61 skerssissf gncvllsfiv kv
//
LOCUS       NP_005155                740 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_005155
VERSION     NP_005155.1
DBSOURCE    REFSEQ: accession NM_005164.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314254.1, DB259336.1 and
            AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.255673.1,
                                           SRR1660809.224460.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308666.4/ ENSP00000310688.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..740
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 1"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=83102
     Region          1..218
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:10777694"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Region          74..685
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     CDS             1..740
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_005164.4:189..2411"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8734.1"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvemkqlq ksykaladqm nlilskrlwy imieqflmky vwsssglimv
      361 aipiitatgf adgedgqkqv mvserteaft tarnllasga daierimssy kevtelagyt
      421 arvynmfwvf devkrgiykr taviqesesh skngakvelp lsdtlaikgk vidvdhgiic
      481 envpiitpag evvasrlnfk veegmhllit gpngcgkssl frilsglwpv yegvlykppp
      541 qhmfyipqrp ymslgslrdq viypdsvddm hdkgytdqdl erilhnvhly hivqreggwd
      601 avmdwkdvls ggekqrmgma rmfyhkpkya lldectsavs idvegkifqa akgagislls
      661 ithrpslwky hthllqfdge ggwrfeqldt airltlseek qklesqlagi pkmqqrlnel
      721 ckilgedsvl ktiknedets
//
LOCUS       NP_001399722             315 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001399722
VERSION     NP_001399722.1
DBSOURCE    REFSEQ: accession NM_001412793.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.269348.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..315
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 7"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=35565
     Region          <1..260
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     CDS             1..315
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412793.1:204..1151"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mfwvfdevkr giykrtaviq eseshsknga kvelplsdtl aikgkvidvd hgiicenvpi
       61 itpagevvas rlnfkveegm hllitgpngc gksslfrils glwpvyegvl ykpppqhmfy
      121 ipqrpymslg slrdqviypd svddmhdkgy tdqdlerilh nvhlyhivqr eggwdavmdw
      181 kdvlsggekq rmgmarmfyh kpkyalldec tsavsidveg kifqaakgag isllsithrp
      241 slwkyhthll qfdgeggwrf eqldtairlt lseekqkles qlagipkmqq rlnelckilg
      301 edsvlktikn edets
//
LOCUS       NP_001265121             852 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 4 [Homo sapiens].
ACCESSION   NP_001265121
VERSION     NP_001265121.1
DBSOURCE    REFSEQ: accession NM_001278192.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 852)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 852)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 852)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 852)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302752.1, AF144074.1,
            AK314370.1 and D42041.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (4) lacks three consecutive exons
            in the 5' coding region but maintains the reading frame, compared
            to variant 3. The resulting isoform (4) lacks an internal segment,
            compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302752.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..852
                     /product="neutral alpha-glucosidase AB isoform 4"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=96413
     Region          152..292
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            191
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          292..759
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(337,450,510,523,526,559,584)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          735..803
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..852
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001278192.2:15..2573"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS60818.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 maavaavaar rrrlsvsgrd ensveltmae gpykiiltar pfrldlledr slllsvnarg
       61 llefehqrap rvsfsdkvnl tlgsiwdkik nlfsrqgskd paegdgaqpe etprdgdkpe
      121 etqgkaekde pgaweetfkt hsdskpygpm svgldfslpg mehvygipeh adnlrlkvte
      181 ggepyrlynl dvfqyelynp malygsvpvl lahnphrdlg ifwlnaaetw vdissntagk
      241 tlfgkmmdyl qgsgetpqtd vrwmsetgii dvflllgpsi sdvfrqyasl tgtqalpplf
      301 slgyhqsrwn yrdeadvlev dqgfddhnlp cdviwldieh adgkryftwd psrfpqprtm
      361 lerlaskrrk lvaivdphik vdsgyrvhee lrnlglyvkt rdgsdyegwc wpgsagypdf
      421 tnptmrawwa nmfsydnyeg sapnlfvwnd mnepsvfngp evtmlkdaqh yggwehrdvh
      481 niyglyvhma tadglrqrsg gmerpfvlar affagsqrfg avwtgdntae wdhlkisipm
      541 clslglvgls fcgadvggff knpepellvr wyqmgayqpf frahahldtg rrepwllpsq
      601 hndiirdalg qrysllpfwy tllyqahreg ipvmrplwvq ypqdvttfni ddqyllgdal
      661 lvhpvsdsga hgvqvylpgq gevwydiqsy qkhhgpqtly lpvtlssipv fqrggtivpr
      721 wmrvrrssec mkddpitlfv alspqgtaqg elflddghtf nyqtrqefll rrfsfsgntl
      781 vsssadpegh fetpiwierv viigagkpaa vvlqtkgspe srlsfqhdpe tsvlvlrkpg
      841 invasdwsih lr
//
LOCUS       NP_055768                958 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex exonuclease RRP44 isoform a [Homo sapiens].
ACCESSION   NP_055768
VERSION     NP_055768.3
DBSOURCE    REFSEQ: accession NM_014953.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 958)
  AUTHORS   Favasuli,V.K., Ronchetti,D., Silvestris,I., Puccio,N., Fabbiano,G.,
            Traini,V., Todoerti,K., Erratico,S., Ciarrocchi,A., Fragliasso,V.,
            Giannandrea,D., Tumiatti,F., Chiaramonte,R., Torrente,Y.,
            Finelli,P., Morelli,E., Munshi,N.C., Bolli,N., Neri,A. and
            Taiana,E.
  TITLE     DIS3 depletion in multiple myeloma causes extensive perturbation in
            cell cycle progression and centrosome amplification
  JOURNAL   Haematologica 109 (1), 231-244 (2024)
   PUBMED   37439377
  REMARK    GeneRIF: DIS3 depletion in multiple myeloma causes extensive
            perturbation in cell cycle progression and centrosome
            amplification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 958)
  AUTHORS   Johnstone,E.B., Gorsi,B., Coelho,E., Moore,B., Farr,A.M.,
            Cooper,A.R., Mardis,E.R., Rajkovic,A., Chow,C.Y., Yandell,M. and
            Welt,C.K.
  TITLE     DIS3 Variants are Associated With Primary Ovarian Insufficiency:
            Importance of Transcription/Translation in Oogenesis
  JOURNAL   J Clin Endocrinol Metab 108 (9), 2330-2335 (2023)
   PUBMED   36869713
  REMARK    GeneRIF: DIS3 Variants are Associated With Primary Ovarian
            Insufficiency: Importance of Transcription/Translation in
            Oogenesis.
REFERENCE   3  (residues 1 to 958)
  AUTHORS   Ohguchi,Y. and Ohguchi,H.
  TITLE     DIS3: The Enigmatic Gene in Multiple Myeloma
  JOURNAL   Int J Mol Sci 24 (4), 4079 (2023)
   PUBMED   36835493
  REMARK    GeneRIF: DIS3: The Enigmatic Gene in Multiple Myeloma.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 958)
  AUTHORS   Gritti,I., Basso,V., Rinchai,D., Corigliano,F., Pivetti,S.,
            Gaviraghi,M., Rosano,D., Mazza,D., Barozzi,S., Roncador,M.,
            Parmigiani,G., Legube,G., Parazzoli,D., Cittaro,D., Bedognetti,D.,
            Mondino,A., Segalla,S. and Tonon,G.
  TITLE     Loss of ribonuclease DIS3 hampers genome integrity in myeloma by
            disrupting DNA:RNA hybrid metabolism
  JOURNAL   EMBO J 41 (22), e108040 (2022)
   PUBMED   36215697
  REMARK    GeneRIF: Loss of ribonuclease DIS3 hampers genome integrity in
            myeloma by disrupting DNA:RNA hybrid metabolism.
REFERENCE   5  (residues 1 to 958)
  AUTHORS   Fujiwara,N., Shigemoto,M., Hirayama,M., Fujita,K.I., Seno,S.,
            Matsuda,H., Nagahama,M. and Masuda,S.
  TITLE     MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of
            MTR4-sensitive substrates in the human nucleus
  JOURNAL   Nucleic Acids Res 50 (15), 8779-8806 (2022)
   PUBMED   35902094
  REMARK    GeneRIF: MPP6 stimulates both RRP6 and DIS3 to degrade a specified
            subset of MTR4-sensitive substrates in the human nucleus.
REFERENCE   6  (residues 1 to 958)
  AUTHORS   Rozenblum,E., Vahteristo,P., Sandberg,T., Bergthorsson,J.T.,
            Syrjakoski,K., Weaver,D., Haraldsson,K., Johannsdottir,H.K.,
            Vehmanen,P., Nigam,S., Golberger,N., Robbins,C., Pak,E., Dutra,A.,
            Gillander,E., Stephan,D.A., Bailey-Wilson,J., Juo,S.H., Kainu,T.,
            Arason,A., Barkardottir,R.B., Nevanlinna,H., Borg,A. and
            Kallioniemi,O.P.
  TITLE     A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
            development: identification and characterization of candidate genes
  JOURNAL   Hum Genet 110 (2), 111-121 (2002)
   PUBMED   11935316
REFERENCE   7  (residues 1 to 958)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   8  (residues 1 to 958)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 958)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 958)
  AUTHORS   Shiomi,T., Fukushima,K., Suzuki,N., Nakashima,N., Noguchi,E. and
            Nishimoto,T.
  TITLE     Human dis3p, which binds to either GTP- or GDP-Ran, complements
            Saccharomyces cerevisiae dis3
  JOURNAL   J Biochem 123 (5), 883-890 (1998)
   PUBMED   9562621
  REMARK    GeneRIF: Dis3p is identical to Rrp44p, which comprises the exosome
            involved in ribosomal RNA processing. Similar to S. cerevisiae
            Dis3p, human Dis3p enhanced RCC1-stimulated nucleotide release from
            Ran, in a dose-dependent manner, and bound to GTP- or GDP-Ran.
            GeneRIF: S. cerevisiae Dis3p is identical to Rrp44p, which
            comprises the exosome involved in ribosomal RNA processing, S.
            cerevisiae Dis3p was found to be localized in the nucleolus.
            Erratum:[J Biochem (Tokyo) 1998 Jul;124(1):250]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC056143.1, AL832266.1, AL080158.1, AL138695.13 and U79246.1.
            
            On Jun 11, 2008 this sequence version replaced NP_055768.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF330044.1, BC056143.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377767.9/ ENSP00000366997.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..958
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q21.33"
     Protein         1..958
                     /product="exosome complex exonuclease RRP44 isoform a"
                     /note="mitotic control protein dis3 homolog; exosome
                     component 11; exosome complex exonuclease RRP44; DIS3
                     exosome endoribonuclease and 3''-5'' exoribonuclease; DIS3
                     mitotic control homolog; ribosomal RNA-processing protein
                     44; DIS3 homolog, exosome endoribonuclease and 3'-5'
                     exoribonuclease"
                     /calculated_mol_wt=108872
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L1.2)"
     Region          9..197
                     /region_name="PIN_Rrp44-like"
                     /note="VapC-like PIN domain of yeast exosome subunit Rrp44
                     endoribonuclease and other eukaryotic homologs; cd09862"
                     /db_xref="CDD:350211"
     Site            18
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L1.2)"
     Site            order(20..24,26,28,95,99..100,106,110,124,127)
                     /site_type="other"
                     /note="exosome subunit interface [polypeptide binding]"
                     /db_xref="CDD:350211"
     Site            order(31,36,39,159)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:350211"
     Region          206..929
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y2L1.2)"
     Region          938..958
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y2L1.2)"
     CDS             1..958
                     /gene="DIS3"
                     /gene_synonym="2810028N01Rik; dis3p; EXOSC11; KIAA1008;
                     RRP44"
                     /coded_by="NM_014953.5:69..2945"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9447.1"
                     /db_xref="GeneID:22894"
                     /db_xref="HGNC:HGNC:20604"
                     /db_xref="MIM:607533"
ORIGIN      
        1 mlksktflkk traggvmkiv rehylrddig cgapgcaacg gahegpalep qpqdpassvc
       61 pqphyllpdt nvllhqidvl edpairnviv lqtvlqevrn rsapvykrir dvtnnqekhf
      121 ytftnehhre tyveqeqgen andrndrair vaakwynehl kkmsadnqlq vifitndrrn
      181 kekaieegip aftceeyvks ltanpelidr laclseegne iesgkiifse hlplsklqqg
      241 iksgtylqgt frasrenyle atvwihgdne enkeiilqgl khlnravhed ivavellpks
      301 qwvapssvvl hdegqneedv ekeeeterml ktavsekmlk ptgrvvgiik rnwrpycgml
      361 sksdikesrr hlftpadkri pririetrqa stlegrriiv aidgwprnsr ypnghfvrnl
      421 gdvgeketet evlllehdvp hqpfsqavls flpkmpwsit ekdmknredl rhlcicsvdp
      481 pgctdiddal hcrelengnl evgvhiadvs hfirpgnald qesarrgttv ylcekridmv
      541 pellssnlcs lkcdvdrlaf sciwemnhna eilktkftks vinskaslty aeaqlridsa
      601 nmnddittsl rglnklakil kkrriekgal tlsspevrfh mdsethdpid lqtkelretn
      661 smveefmlla nisvakkihe efsehallrk hpapppsnye ilvkaarsrn leiktdtaks
      721 laesldqaes ptfpylntll rilatrcmmq avyfcsgmdn dfhhyglasp iythftspir
      781 ryadvivhrl lavaigadct ypeltdkhkl adicknlnfr hkmaqyaqra svafhtqlff
      841 kskgivseea yilfvrknai vvlipkygle gtvffeekdk pnpqliydde ipslkiedtv
      901 fhvfdkvkvk imldssnlqh qkirmslvep qipgisiptd tsnmdlngpk kkkmklgk
//
LOCUS       NP_660089                 96 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform d [Homo sapiens].
ACCESSION   NP_660089
VERSION     NP_660089.1
DBSOURCE    REFSEQ: accession NM_145114.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 96)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 96)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 96)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 96)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 96)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 96)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 96)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 96)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 96)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 96)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF038005.1, BC013669.1 and
            HY018878.1.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (4) lacks one alternate in-frame
            exon in the coding region and includes an alternate 3' terminal
            exon compared to variant 1. It encodes isoform d which is shorter
            and has a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013669.1, BM810102.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..96
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..96
                     /product="protein max isoform d"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=11324
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..>57
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..96
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_145114.3:179..469"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS9774.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgeklyf
       61 lfwklctpvl hrqslmqkch tfissyqvhk kkecki
//
LOCUS       NP_001266279             285 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA exonuclease 4 isoform 3 [Homo sapiens].
ACCESSION   NP_001266279
VERSION     NP_001266279.1
DBSOURCE    REFSEQ: accession NM_001279350.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Krishnamurthy,N., Ngam,C.R., Berdis,A.J. and Montano,M.M.
  TITLE     The exonuclease activity of hPMC2 is required for transcriptional
            regulation of the QR gene and repair of estrogen-induced abasic
            sites
  JOURNAL   Oncogene 30 (47), 4731-4739 (2011)
   PUBMED   21602889
  REMARK    GeneRIF: determined that the catalytic activity of hPMC2 is
            required for repair of abasic sites that result from
            estrogen-induced DNA damage
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Montano,M.M., Wittmann,B.M. and Bianco,N.R.
  TITLE     Identification and characterization of a novel factor that
            regulates quinone reductase gene transcriptional activity
  JOURNAL   J Biol Chem 275 (44), 34306-34313 (2000)
   PUBMED   10908561
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Kwiatkowska,J., Slomski,R., Jozwiak,S., Short,M.P. and
            Kwiatkowski,D.J.
  TITLE     Human XPMC2H: cDNA cloning, mapping to 9q34, genomic structure, and
            evaluation as TSC1
  JOURNAL   Genomics 44 (3), 350-354 (1997)
   PUBMED   9325058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304547.1, BC009274.2 and AL136894.1.
            
            Transcript Variant: This variant (3) uses an alternate splice site
            near the 5' end and initiates translation at a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (3) has a
            shorter N-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.178168.1, AK304547.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..285
                     /product="RNA exonuclease 4 isoform 3"
                     /note="Xenopus prevents mitotic catastrophe 2 homolog;
                     REX4 homolog, 3'-5' exonuclease; exonuclease XPMC2; XPMC2
                     prevents mitotic catastrophe 2 homolog; REX4, RNA
                     exonuclease 4 homolog"
                     /calculated_mol_wt=31554
     Region          107..257
                     /region_name="REX4_like"
                     /note="DEDDh 3'-5' exonuclease domain of RNA exonuclease
                     4, XPMC2, Interferon Stimulated Gene product of 20 kDa,
                     and similar proteins; cd06144"
                     /db_xref="CDD:99847"
     Site            order(110..113,115,153,157,189..190,192..194,244,249)
                     /site_type="active"
                     /db_xref="CDD:99847"
     Site            order(110..113,115,153,157,189..190,192..193,244,249)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:99847"
     Site            order(110,112,194,244,249)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:99847"
     CDS             1..285
                     /gene="REXO4"
                     /gene_synonym="REX4; XPMC2; XPMC2H"
                     /coded_by="NM_001279350.2:400..1257"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:57109"
                     /db_xref="HGNC:HGNC:12820"
                     /db_xref="MIM:602930"
ORIGIN      
        1 mdrrapvprt kasgtehnkk gtkertngdi vpergdiehk krkakeaapa ppteediwfd
       61 dvdpadieaa igpeaakiar kqlgqsegsv slslvkeqaf ggltralald cemvgvgpkg
      121 eesmaarvsi vnqygkcvyd kyvkptepvt dyrtavsgir penlkqgeel evvqkevaem
      181 lkgrilvgha lhndlkvlfl dhpkkkirdt qkykpfksqv ksgrpslrll sekilglqvq
      241 qaehcsiqda qaamrlyvmv kkewesmard rrplltapdh csdda
//
LOCUS       NP_660088                103 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform c [Homo sapiens].
ACCESSION   NP_660088
VERSION     NP_660088.1
DBSOURCE    REFSEQ: accession NM_145113.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833643.1, X60287.1,
            AK290929.1, BC025685.1 and BC027924.1.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            exon in the 3' coding region compared to variant 1. The resulting
            protein (isoform c) has a distinct C-terminus and is shorter than
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.621755.1, AK290929.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 1566084
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..103
                     /product="protein max isoform c"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=11968
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     CDS             1..103
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_145113.3:179..490"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS41965.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqge ses
//
LOCUS       NP_001394037              94 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform m [Homo sapiens].
ACCESSION   NP_001394037
VERSION     NP_001394037.1
DBSOURCE    REFSEQ: accession NM_001407108.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 94)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 94)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 94)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 94)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1011561.1,
                                           SRR14038191.2809799.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: PMID: 1566084
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..94
                     /product="protein max isoform m"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10895
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..94
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407108.1:179..463"
                     /note="isoform m is encoded by transcript variant 26"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqg eses
//
LOCUS       NP_001007465             147 aa            linear   PRI 20-NOV-2025
DEFINITION  RWD domain-containing protein 1 isoform b [Homo sapiens].
ACCESSION   NP_001007465
VERSION     NP_001007465.1
DBSOURCE    REFSEQ: accession NM_001007464.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Grotsch,H., Kunert,M., Mooslehner,K.A., Gao,Z., Struve,D.,
            Hughes,I.A., Hiort,O. and Werner,R.
  TITLE     RWDD1 interacts with the ligand binding domain of the androgen
            receptor and acts as a coactivator of androgen-dependent
            transactivation
  JOURNAL   Mol Cell Endocrinol 358 (1), 53-62 (2012)
   PUBMED   22406838
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC012534.1, AK301089.1, CK817864.1 and AL121953.21.
            
            Transcript Variant: This variant (3) differs in its 5' UTR, and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (b) has a shorter N-terminus,
            compared to isoform a. Variants 2 and 3 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.43052.1,
                                           SRR1803616.31213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..147
                     /product="RWD domain-containing protein 1 isoform b"
                     /note="RWD domain-containing protein 1; DRG
                     family-regulatory protein 2"
                     /calculated_mol_wt=16951
     Region          <1..23
                     /region_name="RWD_DRWD_ELF-like"
                     /note="RWD, DRWD, and ELF domain family; cl45901"
                     /db_xref="CDD:480265"
     Region          <48..>101
                     /region_name="DFRP_C"
                     /note="DRG Family Regulatory Proteins, Tma46; pfam16543"
                     /db_xref="CDD:465167"
     CDS             1..147
                     /gene="RWDD1"
                     /gene_synonym="CGI-24; DFRP2; PTD013"
                     /coded_by="NM_001007464.3:482..925"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43496.1"
                     /db_xref="GeneID:51389"
                     /db_xref="HGNC:HGNC:20993"
                     /db_xref="MIM:620844"
ORIGIN      
        1 mvmiftlvta vqeklneivd qiktrreeek kqkekeaeea ekqlfhgtpv tienflnwka
       61 kfdaelleik kkrmkeeeqa gknklsgkql fetdhnldts diqfledagn nvevdeslfq
      121 emddleledd eddpdynpad pesdsad
//
LOCUS       NP_001394976             333 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger TRAF-type-containing protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001394976
VERSION     NP_001394976.1
DBSOURCE    REFSEQ: accession NM_001408047.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Asif,M., Khayyat,A.I.A., Alawbathani,S., Abdullah,U., Sanner,A.,
            Georgomanolis,T., Haasters,J., Becker,K., Budde,B., Becker,C.,
            Thiele,H., Baig,S.M., Isidoro-Garcia,M., Winter,D., Pogoda,H.M.,
            Muhammad,S., Hammerschmidt,M., Kraft,F., Kurth,I., Martin,H.G.,
            Wagner,M., Nurnberg,P. and Hussain,M.S.
  TITLE     Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia
  JOURNAL   Genet Med 26 (7), 101143 (2024)
   PUBMED   38641995
  REMARK    GeneRIF: Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Desaki,R., Sawada,G., Okumura,H., Ikeda,R., Tanabe,K., Komatsu,H.,
            Mimori,K., Mori,M., Kita,Y., Uchikado,Y., Arigami,T., Uenosono,Y.,
            Owaki,T., Ishigami,S. and Natsugoe,S.
  TITLE     As a Novel Prognostic Marker, Cysteine/histidine-rich 1 (CYHR1) is
            a Therapeutic Target in Patients with Esophageal Squamous Cell
            Carcinoma
  JOURNAL   Ann Surg Oncol 24 (2), 586-593 (2017)
   PUBMED   26676980
  REMARK    GeneRIF: High CYHR1 expression is associated with Esophageal
            Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Menon,R.P., Strom,M. and Hughes,R.C.
  TITLE     Interaction of a novel cysteine and histidine-rich cytoplasmic
            protein with galectin-3 in a carbohydrate-independent manner
  JOURNAL   FEBS Lett 470 (3), 227-231 (2000)
   PUBMED   10745073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084125.9.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.208479.1,
                                           SRR14038197.591653.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..333
                     /product="zinc finger TRAF-type-containing protein 1
                     isoform 2"
                     /note="cysteine and histidine rich protein; cysteine and
                     histidine-rich protein 1; cysteine/histidine-rich 1;
                     cysteine and histidine rich 1; Zinc finger
                     TRAF-type-containing protein 1; zinc finger TRAF-type
                     containing 1"
                     /calculated_mol_wt=34689
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DTL6.1)"
     Region          100..161
                     /region_name="RING-HC_CYHR1"
                     /note="RING finger, HC subclass, found in cysteine and
                     histidine-rich protein 1 (CYHR1) and similar proteins;
                     cd16505"
                     /db_xref="CDD:438168"
     Region          166..>227
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          249..>274
                     /region_name="CYHR1_C"
                     /note="C-terminal domain of cysteine and histidine-rich
                     protein 1 and similar proteins; cd22861"
                     /db_xref="CDD:439370"
     CDS             1..333
                     /gene="ZFTRAF1"
                     /gene_synonym="CHRP; CYHR1"
                     /coded_by="NM_001408047.1:218..1219"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:50626"
                     /db_xref="HGNC:HGNC:17806"
                     /db_xref="MIM:616635"
ORIGIN      
        1 msgaeeaggg gpaagpagsv pagvgvgvga gpgaaagqaa aaalgeaagp glpdeaglag
       61 arqlqlqeaa gdpdappkkr lraaeaaeaa aaaaaagsgk leerlysvlc ctvcldlpka
      121 svyqctnghl mcagcfihll adarlkeeqa tcpncrceis kslccrnlav ekavselpse
      181 cgfclrqfpr sllerhqkee cqdrvtqcky krigcpwhgp fheltvheaa cahptktgse
      241 lmeildgmdq shrkemqlyn sifsllsfek igytgeaprr llhatqvwvg glaarslgaa
      301 gsghwaltap dsraldklpv drwtprsrrq agd
//
LOCUS       NP_001257998              74 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform h [Homo sapiens].
ACCESSION   NP_001257998
VERSION     NP_001257998.1
DBSOURCE    REFSEQ: accession NM_001271069.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 74)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 74)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 74)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 74)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 74)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 74)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 74)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 74)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 74)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 74)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833643.1, DB482510.1 and
            AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (8) lacks two alternate in-frame
            exons in the coding region and includes an alternate 3' terminal
            exon, compared to variant 1. It encodes isoform h which is shorter
            and has a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB482510.1, DB498279.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..74
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..74
                     /product="protein max isoform h"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=8394
     Region          15..>48
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..74
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001271069.2:179..403"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekgt kmkltlppvf
       61 pyehlpfptv fchg
//
LOCUS       NP_940933               1147 aa            linear   PRI 20-NOV-2025
DEFINITION  probable phospholipid-transporting ATPase IIB isoform 1 [Homo
            sapiens].
ACCESSION   NP_940933 XP_351169
VERSION     NP_940933.3
DBSOURCE    REFSEQ: accession NM_198531.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1147)
  AUTHORS   Yagi,T., Nakabuchi,R., Muranaka,Y., Tanaka,G., Katoh,Y.,
            Nakayama,K., Takatsu,H. and Shin,H.W.
  TITLE     Lipid flippases ATP9A and ATP9B form a complex and contribute to
            the exocytic pathway from the Golgi
  JOURNAL   Life Sci Alliance 8 (7), e202403163 (2025)
   PUBMED   40234049
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1147)
  AUTHORS   Eeles,R.A., Olama,A.A., Benlloch,S., Saunders,E.J.,
            Leongamornlert,D.A., Tymrakiewicz,M., Ghoussaini,M., Luccarini,C.,
            Dennis,J., Jugurnauth-Little,S., Dadaev,T., Neal,D.E., Hamdy,F.C.,
            Donovan,J.L., Muir,K., Giles,G.G., Severi,G., Wiklund,F.,
            Gronberg,H., Haiman,C.A., Schumacher,F., Henderson,B.E., Le
            Marchand,L., Lindstrom,S., Kraft,P., Hunter,D.J., Gapstur,S.,
            Chanock,S.J., Berndt,S.I., Albanes,D., Andriole,G., Schleutker,J.,
            Weischer,M., Canzian,F., Riboli,E., Key,T.J., Travis,R.C.,
            Campa,D., Ingles,S.A., John,E.M., Hayes,R.B., Pharoah,P.D.,
            Pashayan,N., Khaw,K.T., Stanford,J.L., Ostrander,E.A.,
            Signorello,L.B., Thibodeau,S.N., Schaid,D., Maier,C., Vogel,W.,
            Kibel,A.S., Cybulski,C., Lubinski,J., Cannon-Albright,L.,
            Brenner,H., Park,J.Y., Kaneva,R., Batra,J., Spurdle,A.B.,
            Clements,J.A., Teixeira,M.R., Dicks,E., Lee,A., Dunning,A.M.,
            Baynes,C., Conroy,D., Maranian,M.J., Ahmed,S., Govindasami,K.,
            Guy,M., Wilkinson,R.A., Sawyer,E.J., Morgan,A., Dearnaley,D.P.,
            Horwich,A., Huddart,R.A., Khoo,V.S., Parker,C.C., Van As,N.J.,
            Woodhouse,C.J., Thompson,A., Dudderidge,T., Ogden,C., Cooper,C.S.,
            Lophatananon,A., Cox,A., Southey,M.C., Hopper,J.L., English,D.R.,
            Aly,M., Adolfsson,J., Xu,J., Zheng,S.L., Yeager,M., Kaaks,R.,
            Diver,W.R., Gaudet,M.M., Stern,M.C., Corral,R., Joshi,A.D.,
            Shahabi,A., Wahlfors,T., Tammela,T.L., Auvinen,A., Virtamo,J.,
            Klarskov,P., Nordestgaard,B.G., Roder,M.A., Nielsen,S.F.,
            Bojesen,S.E., Siddiq,A., Fitzgerald,L.M., Kolb,S., Kwon,E.M.,
            Karyadi,D.M., Blot,W.J., Zheng,W., Cai,Q., McDonnell,S.K.,
            Rinckleb,A.E., Drake,B., Colditz,G., Wokolorczyk,D.,
            Stephenson,R.A., Teerlink,C., Muller,H., Rothenbacher,D.,
            Sellers,T.A., Lin,H.Y., Slavov,C., Mitev,V., Lose,F.,
            Srinivasan,S., Maia,S., Paulo,P., Lange,E., Cooney,K.A.,
            Antoniou,A.C., Vincent,D., Bacot,F., Tessier,D.C., Kote-Jarai,Z.
            and Easton,D.F.
  CONSRTM   COGS-Cancer Research UK GWAS-ELLIPSE (part of GAME-ON) Initiative;
            Australian Prostate Cancer Bioresource; UK Genetic Prostate Cancer
            Study Collaborators/British Association of Urological Surgeons'
            Section of Oncology; UK ProtecT (Prostate testing for cancer and
            Treatment) Study Collaborators; PRACTICAL (Prostate Cancer
            Association Group to Investigate Cancer-Associated Alterations in
            the Genome) Consortium
  TITLE     Identification of 23 new prostate cancer susceptibility loci using
            the iCOGS custom genotyping array
  JOURNAL   Nat Genet 45 (4), 385-391 (2013)
   PUBMED   23535732
REFERENCE   3  (residues 1 to 1147)
  AUTHORS   Tashiro-Yamaji,J., Shimizu,T., Hayashi,M., Yamana,H., Tanigawa,N.,
            Uchiyama,K., Kubota,T. and Yoshida,R.
  TITLE     Specific binding of HLA-B44 to human macrophage MHC receptor 1 on
            monocytes
  JOURNAL   Gene 501 (2), 127-134 (2012)
   PUBMED   22525042
  REMARK    GeneRIF: These results revealed that human human macrophage MHC
            receptor 1 on monocytes is a novel receptor specific for HLA-B44.
REFERENCE   4  (residues 1 to 1147)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   5  (residues 1 to 1147)
  AUTHORS   Nusbaum,C., Zody,M.C., Borowsky,M.L., Kamal,M., Kodira,C.D.,
            Taylor,T.D., Whittaker,C.A., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Yang,X., Abouelleil,A., Allen,N.R., Anderson,S.,
            Bloom,T., Bugalter,B., Butler,J., Cook,A., DeCaprio,D., Engels,R.,
            Garber,M., Gnirke,A., Hafez,N., Hall,J.L., Norman,C.H., Itoh,T.,
            Jaffe,D.B., Kuroki,Y., Lehoczky,J., Lui,A., Macdonald,P.,
            Mauceli,E., Mikkelsen,T.S., Naylor,J.W., Nicol,R., Nguyen,C.,
            Noguchi,H., O'Leary,S.B., O'Neill,K., Piqani,B., Smith,C.L.,
            Talamas,J.A., Topham,K., Totoki,Y., Toyoda,A., Wain,H.M.,
            Young,S.K., Zeng,Q., Zimmer,A.R., Fujiyama,A., Hattori,M.,
            Birren,B.W., Sakaki,Y. and Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 18
  JOURNAL   Nature 437 (7058), 551-555 (2005)
   PUBMED   16177791
  REMARK    Erratum:[Nature. 2005 Dec 1;438(7068):696. O'Neill, Keith [added]]
REFERENCE   6  (residues 1 to 1147)
  AUTHORS   Stanchi,F., Bertocco,E., Toppo,S., Dioguardi,R., Simionati,B.,
            Cannata,N., Zimbello,R., Lanfranchi,G. and Valle,G.
  TITLE     Characterization of 16 novel human genes showing high similarity to
            yeast sequences
  JOURNAL   Yeast 18 (1), 69-80 (2001)
   PUBMED   11124703
REFERENCE   7  (residues 1 to 1147)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1147)
  AUTHORS   Halleck,M.S., Pradhan,D., Blackman,C., Berkes,C., Williamson,P. and
            Schlegel,R.A.
  TITLE     Multiple members of a third subfamily of P-type ATPases identified
            by genomic sequences and ESTs
  JOURNAL   Genome Res 8 (4), 354-361 (1998)
   PUBMED   9548971
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY028472.1, BC022535.1, AK093704.1, BX537860.1, BC037546.1,
            AL096735.1 and AW411030.1.
            
            On Jan 26, 2004 this sequence version replaced NP_940933.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This transcript is supported by overlapping EST and
            cDNA clones. The available sequence data suggest that some
            alternate splicing occurs. This record is provided so that the
            longer gene length can be represented. It is possible that this
            exact combination does not occur in vivo. The encoded protein is
            supported by mouse data.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.240124.1,
                                           SRR1803612.156541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000426216.6/ ENSP00000398076.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..1147
                     /product="probable phospholipid-transporting ATPase IIB
                     isoform 1"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IIB;
                     ATPase type IV, phospholipid transporting (P-type);
                     macrophage MHC receptor 1; ATPase, class II, type 9B;
                     ATPase phospholipid transporting 9B (putative)"
                     /calculated_mol_wt=129173
     Region          132..1056
                     /region_name="P-type_ATPase_APLT_Neo1-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Neo1p and human putative APLT,
                     ATP9B; cd07541"
                     /db_xref="CDD:319841"
     Site            147..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            174..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            410..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            order(468..470,633,657..659,719,766..768,848,851,854,874,
                     877)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319841"
     Region          503..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Region          576..660
                     /region_name="Cation_ATPase"
                     /note="Cation transport ATPase (P-type); pfam13246"
                     /db_xref="CDD:463817"
     Site            931..951
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            964..982
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1013..1031
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1039..1061
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1068..1088
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1106..1130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     CDS             1..1147
                     /gene="ATP9B"
                     /gene_synonym="ATPASEP; ATPIIB; hMMR1; HUSSY-20; NEO1L"
                     /coded_by="NM_198531.5:18..3461"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12014.1"
                     /db_xref="GeneID:374868"
                     /db_xref="HGNC:HGNC:13541"
                     /db_xref="MIM:614446"
ORIGIN      
        1 madqiplypv rsaaaaaanr kraayysaag prpgadrhsr yqledesahl demplmmsee
       61 gfeneesdyh tlprarimqr krglewfvcd gwkflctscc gwlinicrrk kelkartvwl
      121 gcpekceekh prnsiknqky nvftfipgvl yeqfkfflnl yflviscsqf vpalkigyly
      181 tywaplgfvl avtmtreaid efrrfqrdke vnsqlysklt vrgkvqvkss diqvgdliiv
      241 eknqripsdm vflrtsekag scfirtdqld getdwklkva vsctqqlpal gdlfsisayv
      301 yaqkpqmdih sfegtftred sdppihesls ientlwasti vasgtvigvv iytgketrsv
      361 mntsnpknkv glldlelnrl tkalflalva lsivmvtlqg fvgpwyrnlf rflllfsyii
      421 pislrvnldm gkavygwmmm kdenipgtvv rtstipeelg rlvylltdkt gtltqnemif
      481 krlhlgtvsy gadtmdeiqs hvrdsysqmq sqaggnntgs tplrkaqssa pkvrksvssr
      541 iheavkaivl chnvtpvyes ragvteetef aeadqdfsde nrtyqasspd evalvqwtes
      601 vgltlvsrdl tsmqlktpsg qvlsfcilql fpftseskrm gvivrdesta eitfymkgad
      661 vamspivqyn dwleeecgnm areglrtlvv akkalteeqy qdfesrytqa klsmhdrslk
      721 vaavvesler emellcltgv edqlqadvrp tlemlrnagi kiwmltgdkl etatciakss
      781 hlvsrtqdih ifrqvtsrge ahlelnafrr khdcalvisg dslevclkyy ehefvelacq
      841 cpavvccrcs ptqkarivtl lqqhtgrrtc aigdggndvs miqaadcgig iegkegkqas
      901 laadfsitqf rhigrllmvh grnsykrsaa lgqfvmhrgl iistmqavfs svfyfasvpl
      961 yqgflmvgya tiytmfpvfs lvldqdvkpe mamlypelyk dltkgrslsf ktfliwvlis
     1021 iyqggilmyg alvlfesefv hvvaisftal iltellmval tvrtwhwlmv vaeflslgcy
     1081 vsslaflney fgigrvsfga fldvafittv tflwkvsait vvsclplyvl kylrrklspp
     1141 sycklas
//
LOCUS       NP_001394040              93 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform n [Homo sapiens].
ACCESSION   NP_001394040
VERSION     NP_001394040.1
DBSOURCE    REFSEQ: accession NM_001407111.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 93)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 93)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803613.18539.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..93
                     /product="protein max isoform n"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10028
     CDS             1..93
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407111.1:510..791"
                     /note="isoform n is encoded by transcript variant 29"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mccgkaradq vlcswgihfs sslmedaskr kfralekars saqlqtnyps sdnslytnak
       61 gstisafdgg sdsssesepe epqsrkklrm eas
//
LOCUS       NP_001399719             667 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001399719
VERSION     NP_001399719.1
DBSOURCE    REFSEQ: accession NM_001412790.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125491.1 and AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.1331.1,
                                           SRR14038197.154821.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..667
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 4"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=74603
     Region          1..218
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:10777694"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Region          74..667
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     Site            107..127
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            227
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBJ2.1)"
     CDS             1..667
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412790.1:189..2192"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvemkqlq ksykaladqm nlilskrlwy imieqflmky vwsssglimv
      361 aipiitatgf adgedgqkqv mvserteaft tarnllasga daierimssy kevtelagyt
      421 arvynmfwvf devkrgiykr taviqesesh skngakvelp lsdtlaikgk vidvdhgiic
      481 envpiitpag evvasrlnfk veegmhllit gpngcgkssl frilsglwpv yegvlykppp
      541 qhmfyipqrp ymslgslrdq viypdsvddm hdkgytdqdl erilhnvhly hivqreggwd
      601 avmdwkdvls ggekqrmgma rmfyhkpkya lldectsavs idvegkifqa akgagislls
      661 ithrpsl
//
LOCUS       NP_872431                908 aa            linear   PRI 20-NOV-2025
DEFINITION  flap endonuclease GEN homolog 1 [Homo sapiens].
ACCESSION   NP_872431
VERSION     NP_872431.5
DBSOURCE    REFSEQ: accession NM_182625.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Du,X., Wang,C., Liu,J., Yu,M., Ju,H., Xue,S., Li,Y., Liu,J.,
            Dai,R., Chen,J., Zhai,Y., Rao,J., Wang,X., Sun,Y., Sun,L., Wu,X.,
            Xu,H. and Shen,Q.
  TITLE     GEN1 as a risk factor for human congenital anomalies of the kidney
            and urinary tract
  JOURNAL   Hum Genomics 18 (1), 41 (2024)
   PUBMED   38654324
  REMARK    GeneRIF: GEN1 as a risk factor for human congenital anomalies of
            the kidney and urinary tract.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Kim,J., Yu,J., Lee,S., Kim,S., Lee,I.S., Lee,W. and Chun,S.
  TITLE     Reverse Transcription-PCR-based Sanger Sequencing-confirmed
            Exon-skipping Effect of a Novel GEN1 Intronic Variant (c.1408+4A>G)
  JOURNAL   Ann Lab Med 44 (2), 188-191 (2024)
   PUBMED   37840312
  REMARK    GeneRIF: Reverse Transcription-PCR-based Sanger
            Sequencing-confirmed Exon-skipping Effect of a Novel GEN1 Intronic
            Variant (c.1408+4A>G).
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Benitez,A., Sebald,M., Kanagaraj,R., Rodrigo-Brenni,M.C.,
            Chan,Y.W., Liang,C.C. and West,S.C.
  TITLE     GEN1 promotes common fragile site expression
  JOURNAL   Cell Rep 42 (2), 112062 (2023)
   PUBMED   36729836
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Chan,Y.W. and West,S.
  TITLE     GEN1 promotes Holliday junction resolution by a coordinated nick
            and counter-nick mechanism
  JOURNAL   Nucleic Acids Res 43 (22), 10882-10892 (2015)
   PUBMED   26578604
  REMARK    GeneRIF: human GEN1 protein promotes Holliday junction resolution
            by a mechanism that is analogous to that exhibited by the
            prototypic HJ resolvase E. coli RuvC.
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Chan,Y.W. and West,S.C.
  TITLE     Spatial control of the GEN1 Holliday junction resolvase ensures
            genome stability
  JOURNAL   Nat Commun 5, 4844 (2014)
   PUBMED   25209024
  REMARK    GeneRIF: GEN1 is controlled by nuclear exclusion, driven by a
            nuclear export signal that restricts GEN1 actions to mitosis.
            Spatial control of GEN1 contributes to genome stability by avoiding
            competition with non-crossover promoting repair pathways.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Garner,E., Kim,Y., Lach,F.P., Kottemann,M.C. and Smogorzewska,A.
  TITLE     Human GEN1 and the SLX4-associated nucleases MUS81 and SLX1 are
            essential for the resolution of replication-induced Holliday
            junctions
  JOURNAL   Cell Rep 5 (1), 207-215 (2013)
   PUBMED   24080495
  REMARK    GeneRIF: GEN1 activity cannot be substituted for the
            SLX4-associated nucleases, and one of the HJ resolvase activities,
            either of those associated with SLX4 or with GEN1, is required for
            cell viability, even in the presence of BLM.
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Gao,M., Rendtlew Danielsen,J., Wei,L.Z., Zhou,D.P., Xu,Q., Li,M.M.,
            Wang,Z.Q., Tong,W.M. and Yang,Y.G.
  TITLE     A novel role of human holliday junction resolvase GEN1 in the
            maintenance of centrosome integrity
  JOURNAL   PLoS One 7 (11), e49687 (2012)
   PUBMED   23166748
  REMARK    GeneRIF: Our findings provide novel insight into the biological
            functions of GEN1 by uncovering an important role of GEN1 in the
            regulation of centrosome integrity.
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Lorenz,A., West,S.C. and Whitby,M.C.
  TITLE     The human Holliday junction resolvase GEN1 rescues the meiotic
            phenotype of a Schizosaccharomyces pombe mus81 mutant
  JOURNAL   Nucleic Acids Res 38 (6), 1866-1873 (2010)
   PUBMED   20040574
  REMARK    GeneRIF: ectopic expression of GEN1 in fission yeast mus81Delta
            strains results in Holliday junction resolution and crossover
            formation during meiosis.
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Ip,S.C., Rass,U., Blanco,M.G., Flynn,H.R., Skehel,J.M. and
            West,S.C.
  TITLE     Identification of Holliday junction resolvases from humans and
            yeast
  JOURNAL   Nature 456 (7220), 357-361 (2008)
   PUBMED   19020614
  REMARK    GeneRIF: Recombinant GEN1 and Yen1 resolve Holliday junctions by
            the introduction of symmetrically related cuts across the junction
            point, to produce nicked duplex products in which the nicks can be
            readily ligated
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Ishikawa,G., Kanai,Y., Takata,K., Takeuchi,R., Shimanouchi,K.,
            Ruike,T., Furukawa,T., Kimura,S. and Sakaguchi,K.
  TITLE     DmGEN, a novel RAD2 family endo-exonuclease from Drosophila
            melanogaster
  JOURNAL   Nucleic Acids Res 32 (21), 6251-6259 (2004)
   PUBMED   15576351
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC097377.3 and AC093731.2.
            
            On May 31, 2019 this sequence version replaced NP_872431.4.
            
            Summary: This gene encodes a member of the Rad2/xeroderma
            pigmentosum group G nuclease family, whose members are
            characterized by N-terminal and internal xeroderma pigmentosum
            group G nuclease domains followed by helix-hairpin-helix domains
            and disordered C-terminal domains. The protein encoded by this gene
            is involved in resolution of Holliday junctions, which are
            intermediate four-way structures that covalently link DNA during
            homologous recombination and double-strand break repair. The
            protein resolves Holliday junctions by creating dual incisions
            across the junction to produce nicked duplex products that can be
            ligated. In addition, this protein has been found to localize to
            centrosomes where it has been implicated in regulation of
            centrosome integrity. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence data consistent
            with the reference genome assembly was not available for all
            regions of the RefSeq transcript. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131387.1, SRR1803611.21782.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.2"
     Protein         1..908
                     /product="flap endonuclease GEN homolog 1"
                     /note="Gen endonuclease homolog 1; Holliday junction
                     resolvase; GEN1 Holliday junction 5' flap endonuclease;
                     structure-selective endonuclease GEN1; replication fork
                     endonuclease"
                     /calculated_mol_wt=102754
     Region          2..206
                     /region_name="PIN_GEN1"
                     /note="FEN-like PIN domains of Gap Endonuclease 1, a
                     structure-specific, divalent-metal-ion dependent, 5'
                     nuclease and homologs; cd09869"
                     /db_xref="CDD:350217"
     Region          2..96
                     /region_name="XPG-N domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            order(16,30,37,54..55,58..59,75,134,136,155,157,170..171)
                     /site_type="active"
                     /db_xref="CDD:350217"
     Site            order(81..92,104..111)
                     /site_type="other"
                     /note="helical arch"
                     /db_xref="CDD:350217"
     Region          122..208
                     /region_name="XPG-I domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Region          195..338
                     /region_name="H3TH_GEN1"
                     /note="H3TH domain of Gap Endonuclease 1, a
                     structure-specific, divalent-metal-ion dependent, 5'
                     nuclease; cd09905"
                     /db_xref="CDD:188625"
     Site            order(205..210,213..218,220..223)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:188625"
     Region          208..384
                     /region_name="5'-3' exonuclease domain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            208
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:188625"
     Region          390..464
                     /region_name="Chromodomain.
                     /evidence=ECO:0000269|PubMed:26682650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17RS7.2)"
     Region          398..458
                     /region_name="Chromo_2"
                     /note="Chromatin organization modifier domain 2;
                     pfam18704"
                     /db_xref="CDD:465841"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMI4; propagated from
                     UniProtKB/Swiss-Prot (Q17RS7.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BMI4; propagated from
                     UniProtKB/Swiss-Prot (Q17RS7.2)"
     CDS             1..908
                     /gene="GEN1"
                     /gene_synonym="Gen"
                     /coded_by="NM_182625.5:115..2841"
                     /db_xref="CCDS:CCDS1691.1"
                     /db_xref="GeneID:348654"
                     /db_xref="HGNC:HGNC:26881"
                     /db_xref="MIM:612449"
ORIGIN      
        1 mgvndlwqil epvkqhiplr nlggktiavd lslwvceaqt vkkmmgsvmk phlrnlffri
       61 syltqmdvkl vfvmegeppk lkadviskrn qsrygssgks wsqktgrshf ksvlreclhm
      121 leclgipwvq aageaeamca ylnagghvdg cltndgdtfl ygaqtvyrnf tmntkdphvd
      181 cytmssiksk lgldrdalvg laillgcdyl pkgvpgvgke qalkliqilk gqsllqrfnr
      241 wnetscnssp qllvtkklah csvcshpgsp kdherngcrl cksdkyceph dyeyccpcew
      301 hrtehdrqls evennikkka cccegfpfhe viqefllnkd klvkviryqr pdlllfqrft
      361 lekmewpnhy acekllvllt hydmierklg srnsnqlqpi rivktrirng vhcfeiewek
      421 pehyamedkq hgefalltie eeslfeaayp eivavyqkqk leikgkkqkr ikpkennlpe
      481 pdevmsfqsh mtlkptceif hkqnsklnsg ispdptlpqe sisaslnsll lpkntpclna
      541 qeqfmsslrp laiqqikavs kslisessqp ntsshnisvi adlhlstidw egtsfsnspa
      601 iqrntfshdl kseveselsa ipdgfenipe qlsceseryt anikkvlded sdgispeehl
      661 lsgitdlclq dlplkerift klsypqdnlq pdvnlktlsi lsvkescian sgsdctshls
      721 kdlpgiplqn esrdskilkg dqllqedykv ntsvpysvsn tvvktcnvrp pntaldhsrk
      781 vdmqttrkil mkksvcldrh ssdeqsapvf gkakyttqrm khssqkhnss hfkesghnkl
      841 sspkihiket eqcvrsyeta eneescfpds tksslsslqc hkkennsgtc ldsplplrqr
      901 lklrfqst
//
LOCUS       NP_001399718             698 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family D member 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001399718
VERSION     NP_001399718.1
DBSOURCE    REFSEQ: accession NM_001412789.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Tawbeh,A., Gondcaille,C., Trompier,D. and Savary,S.
  TITLE     Peroxisomal ABC Transporters: An Update
  JOURNAL   Int J Mol Sci 22 (11), 6093 (2021)
   PUBMED   34198763
  REMARK    GeneRIF: Peroxisomal ABC Transporters: An Update.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Park,S., Oh,J., Kim,Y.I., Choe,S.K., Chun,C.H. and Jin,E.J.
  TITLE     Suppression of ABCD2 dysregulates lipid metabolism via
            dysregulation of miR-141:ACSL4 in human osteoarthritis
  JOURNAL   Cell Biochem Funct 36 (7), 366-376 (2018)
   PUBMED   30264402
  REMARK    GeneRIF: The functional integrity of ABCD2 may play an important
            role in OA pathogenesis via the accumulation of VLCFAs and
            stimulation of apoptotic death through altering profiles of miRNAs
            that target ACSL4.
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Okamoto,T., Kawaguchi,K., Watanabe,S., Agustina,R., Ikejima,T.,
            Ikeda,K., Nakano,M., Morita,M. and Imanaka,T.
  TITLE     Characterization of human ATP-binding cassette protein subfamily D
            reconstituted into proteoliposomes
  JOURNAL   Biochem Biophys Res Commun 496 (4), 1122-1127 (2018)
   PUBMED   29397936
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Kawaguchi,K. and Morita,M.
  TITLE     ABC Transporter Subfamily D: Distinct Differences in Behavior
            between ABCD1-3 and ABCD4 in Subcellular Localization, Function,
            and Human Disease
  JOURNAL   Biomed Res Int 2016, 6786245 (2016)
   PUBMED   27766264
  REMARK    GeneRIF: ABCD1 and ABCD2 are involved in the transport of long and
            very long chain fatty acids (VLCFA) or their CoA-derivatives into
            peroxisomes with different substrate specificities, while ABCD3 is
            involved in the transport of branched chain acyl-CoA into
            peroxisomes.ABCD4 is deduced to take part in the transport of
            vitamin B12 from lysosomes into the cytosol.
            Review article
REFERENCE   5  (residues 1 to 698)
  AUTHORS   Li,Q., Zhu,X., Feng,C., Fang,M. and Liu,X.
  TITLE     Duration of symptom and ABCD2 score as predictors of risk of early
            recurrent events after transient ischemic attack: a hospital-based
            case series study
  JOURNAL   Med Sci Monit 21, 262-267 (2015)
   PUBMED   25604068
  REMARK    GeneRIF: ABCD2 has a role, but not a strong one, in risk of early
            recurrent events after transient ischemic attack
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Holzinger,A., Mayerhofer,P., Berger,J., Lichtner,P., Kammerer,S.
            and Roscher,A.A.
  TITLE     Full length cDNA cloning, promoter sequence, and genomic
            organization of the human adrenoleukodystrophy related (ALDR) gene
            functionally redundant to the gene responsible for X-linked
            adrenoleukodystrophy
  JOURNAL   Biochem Biophys Res Commun 258 (2), 436-442 (1999)
   PUBMED   10329405
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Netik,A., Forss-Petter,S., Holzinger,A., Molzer,B., Unterrainer,G.
            and Berger,J.
  TITLE     Adrenoleukodystrophy-related protein can compensate functionally
            for adrenoleukodystrophy protein deficiency (X-ALD): implications
            for therapy
  JOURNAL   Hum Mol Genet 8 (5), 907-913 (1999)
   PUBMED   10196381
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Holzinger,A., Kammerer,S., Berger,J. and Roscher,A.A.
  TITLE     cDNA cloning and mRNA expression of the human adrenoleukodystrophy
            related protein (ALDRP), a peroxisomal ABC transporter
  JOURNAL   Biochem Biophys Res Commun 239 (1), 261-264 (1997)
   PUBMED   9345306
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Savary,S., Troffer-Charlier,N., Gyapay,G., Mattei,M.G. and
            Chimini,G.
  TITLE     Chromosomal localization of the adrenoleukodystrophy-related gene
            in man and mice
  JOURNAL   Eur J Hum Genet 5 (2), 99-101 (1997)
   PUBMED   9195160
REFERENCE   10 (residues 1 to 698)
  AUTHORS   Lombard-Platet,G., Savary,S., Sarde,C.O., Mandel,J.L. and
            Chimini,G.
  TITLE     A close relative of the adrenoleukodystrophy (ALD) gene codes for a
            peroxisomal protein with a specific expression pattern
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1265-1269 (1996)
   PUBMED   8577752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125491.1 and AC121334.5.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown; however
            this protein is speculated to function as a dimerization partner of
            ABCD1 and/or other peroxisomal ABC transporters. Mutations in this
            gene have been observed in patients with adrenoleukodystrophy, a
            severe demyelinating disease. This gene has been identified as a
            candidate for a modifier gene, accounting for the extreme variation
            among adrenoleukodystrophy phenotypes. This gene is also a
            candidate for a complement group of Zellweger syndrome, a
            genetically heterogeneous disorder of peroxisomal biogenesis.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.43195.1,
                                           SRR1803612.224341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..698
                     /product="ATP-binding cassette sub-family D member 2
                     isoform 3"
                     /EC_number="3.1.2.-"
                     /EC_number="7.6.2.-"
                     /note="adrenoleukodystrophy-like 1; ATP-binding cassette
                     sub-family D member 2; adrenoleukodystrophy-related
                     protein; ATP-binding cassette, sub-family D (ALD), member
                     2"
                     /calculated_mol_wt=78633
     Region          74..643
                     /region_name="3a01203"
                     /note="Peroxysomal Fatty Acyl CoA Transporter (FAT) Family
                     protein; TIGR00954"
                     /db_xref="CDD:273360"
     CDS             1..698
                     /gene="ABCD2"
                     /gene_synonym="ABC39; ALDL1; ALDR; ALDRP; hALDR"
                     /coded_by="NM_001412789.1:189..2285"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:225"
                     /db_xref="HGNC:HGNC:66"
                     /db_xref="MIM:601081"
ORIGIN      
        1 mthmlnaaad rvkwtrssaa kraaclvaaa yalktlypii gkrlkqsghg kkkaaaypaa
       61 enteilhcte ticekpspgv nadffkqlle lrkilfpklv ttetgwlclh svalisrtfl
      121 siyvagldgk ivksivekkp rtfiiklikw lmiaipatfv nsairyleck lalafrtrlv
      181 dhayetyftn qtyykvinmd grlanpdqsl tedimmfsqs vahlysnltk pildvmltsy
      241 tliqtatsrg aspigptlla glvvyatakv lkacspkfgk lvaeeahrkg ylryvhsrii
      301 anveeiafyr ghkvemkqlq ksykaladqm nlilskrlwy imieqflmky vwsssglimv
      361 aipiitatgf adgedgqkqv mvserteaft tarnllasga daierimssy kevtelagyt
      421 arvynmfwvf devkrgiykr taviqesesh skngakvelp lsdtlaikgk vidvdhgiic
      481 envpiitpag evvasrlnfk veegmhllit gpngcgkssl frilsglwpv yegvlykppp
      541 qhmfyipqrp ymslgslrdq viypdsvddm hdkgytdqdl erilhnvhly hivqreggwd
      601 avmdwkdvls ggekqrmgma rmfyhkkyht hllqfdgegg wrfeqldtai rltlseekqk
      661 lesqlagipk mqqrlnelck ilgedsvlkt iknedets
//
LOCUS       NP_001265123             847 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 6 [Homo sapiens].
ACCESSION   NP_001265123
VERSION     NP_001265123.1
DBSOURCE    REFSEQ: accession NM_001278194.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400833.1, AK299819.1,
            AK314370.1 and D42041.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (6) has multiple differences in
            the coding region including translation initiation at a downstream
            start codon, but maintains the reading frame, compared to variant
            3. The resulting isoform (6) has a shorter N-terminus, compared to
            isoform 6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065266.1, SRR14038191.3120398.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..847
                     /product="neutral alpha-glucosidase AB isoform 6"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=96086
     Region          147..287
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            186
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          287..754
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(332,445,505,518,521,554,579)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          730..798
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..847
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001278194.2:197..2740"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS60817.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 mtrfridele prrpryrvpd vlvadppiar lsvsgrdens veltmaegpy kiiltarpfr
       61 ldlledrsll lsvnarglle fehqraprvs qgskdpaegd gaqpeetprd gdkpeetqgk
      121 aekdepgawe etfkthsdsk pygpmsvgld fslpgmehvy gipehadnlr lkvteggepy
      181 rlynldvfqy elynpmalyg svpvllahnp hrdlgifwln aaetwvdiss ntagktlfgk
      241 mmdylqgsge tpqtdvrwms etgiidvfll lgpsisdvfr qyasltgtqa lpplfslgyh
      301 qsrwnyrdea dvlevdqgfd dhnlpcdviw ldiehadgkr yftwdpsrfp qprtmlerla
      361 skrrklvaiv dphikvdsgy rvheelrnlg lyvktrdgsd yegwcwpgsa gypdftnptm
      421 rawwanmfsy dnyegsapnl fvwndmneps vfngpevtml kdaqhyggwe hrdvhniygl
      481 yvhmatadgl rqrsggmerp fvlaraffag sqrfgavwtg dntaewdhlk isipmclslg
      541 lvglsfcgad vggffknpep ellvrwyqmg ayqpffraha hldtgrrepw llpsqhndii
      601 rdalgqrysl lpfwytllyq ahregipvmr plwvqypqdv ttfniddqyl lgdallvhpv
      661 sdsgahgvqv ylpgqgevwy diqsyqkhhg pqtlylpvtl ssipvfqrgg tivprwmrvr
      721 rssecmkddp itlfvalspq gtaqgelfld dghtfnyqtr qefllrrfsf sgntlvsssa
      781 dpeghfetpi wiervviiga gkpaavvlqt kgspesrlsf qhdpetsvlv lrkpginvas
      841 dwsihlr
//
LOCUS       NP_058198                666 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_058198
VERSION     NP_058198.2
DBSOURCE    REFSEQ: accession NM_016818.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 666)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 666)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 666)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 666)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 666)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 666)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 666)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 666)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 666)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 666)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001622.1, BC029158.1 and
            X91249.1.
            
            On Apr 27, 2004 this sequence version replaced NP_058198.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (2) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029158.1, AF323663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398449.8/ ENSP00000381467.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..666
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..666
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 2"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=74024
     Region          60..666
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            415..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            445..465
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            495..513
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            522..543
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            556..574
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            638..657
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     CDS             1..666
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_016818.3:124..2124"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42938.1"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 maclmaafsv gtamnassys aemtepksvc vsvdevvssn meatetdlln ghlkkvdnnl
       61 teaqrfsslp rraavniefr dlsysvpegp wwrkkgyktl lkgisgkfns gelvaimgps
      121 gagkstlmni lagyretgmk gavlinglpr dlrcfrkvsc yimqddmllp hltvqeammv
      181 sahlklqekd egrremvkei ltalgllsca ntrtgslsgg qrkrlaiale lvnnppvmff
      241 deptsgldsa scfqvvslmk glaqggrsii ctihqpsakl felfdqlyvl sqgqcvyrgk
      301 vcnlvpylrd lglncptyhn padfvmevas geygdqnsrl vravregmcd sdhkrdlggd
      361 aevnpflwhr pseedsssme gchsfsascl tqfcilfkrt flsimrdsvl thlritshig
      421 iglligllyl gigneakkvl snsgflffsm lflmfaalmp tvltfplemg vflrehlnyw
      481 yslkayylak tmadvpfqim fpvaycsivy wmtsqpsdav rfvlfaalgt mtslvaqslg
      541 lligaastsl qvatfvgpvt aipvllfsgf fvsfdtipty lqwmsyisyv rygfegvils
      601 iygldredlh cdidetchfq kseailreld venaklyldf ivlgiffisl rliayfvlry
      661 kiraer
//
LOCUS       NP_001394025             130 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform j [Homo sapiens].
ACCESSION   NP_001394025
VERSION     NP_001394025.1
DBSOURCE    REFSEQ: accession NM_001407096.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.878958.1,
                                           SRR14038195.1478123.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..130
                     /product="protein max isoform j"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=14984
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..130
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407096.1:179..571"
                     /note="isoform j is encoded by transcript variant 14"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqga lpavgitpgi rclkralrsl
      121 ewnvlweses
//
LOCUS       NP_001427742             504 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle subunit SRP54 isoform 1 [Homo sapiens].
ACCESSION   NP_001427742 XP_011535408 XP_054232621
VERSION     NP_001427742.1
DBSOURCE    REFSEQ: accession NM_001440813.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   McCarthy,P., Cotter,M. and Smith,O.P.
  TITLE     Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features
  JOURNAL   Br J Haematol 196 (3), e39-e42 (2022)
   PUBMED   34549814
  REMARK    GeneRIF: Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Schurch,C., Schaefer,T., Muller,J.S., Hanns,P., Arnone,M.,
            Dumlin,A., Scharer,J., Sinning,I., Wild,K., Skokowa,J., Welte,K.,
            Carapito,R., Bahram,S., Konantz,M. and Lengerke,C.
  TITLE     SRP54 mutations induce congenital neutropenia via dominant-negative
            effects on XBP1 splicing
  JOURNAL   Blood 137 (10), 1340-1352 (2021)
   PUBMED   33227812
  REMARK    GeneRIF: SRP54 mutations induce congenital neutropenia via
            dominant-negative effects on XBP1 splicing.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Juaire,K.D., Lapouge,K., Becker,M.M.M., Kotova,I., Michelhans,M.,
            Carapito,R., Wild,K., Bahram,S. and Sinning,I.
  TITLE     Structural and Functional Impact of SRP54 Mutations Causing Severe
            Congenital Neutropenia
  JOURNAL   Structure 29 (1), 15-28 (2021)
   PUBMED   33053321
  REMARK    GeneRIF: Structural and Functional Impact of SRP54 Mutations
            Causing Severe Congenital Neutropenia.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Goldberg,L., Simon,A.J., Rechavi,G., Lev,A., Barel,O., Kunik,V.,
            Toren,A., Schiby,G., Tamary,H., Steinberg-Shemer,O. and Somech,R.
  TITLE     Congenital neutropenia with variable clinical presentation in novel
            mutation of the SRP54 gene
  JOURNAL   Pediatr Blood Cancer 67 (6), e28237 (2020)
   PUBMED   32277798
  REMARK    GeneRIF: Congenital neutropenia with variable clinical presentation
            in novel mutation of the SRP54 gene.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Bacher,G., Lutcke,H., Jungnickel,B., Rapoport,T.A. and
            Dobberstein,B.
  TITLE     Regulation by the ribosome of the GTPase of the signal-recognition
            particle during protein targeting
  JOURNAL   Nature 381 (6579), 248-251 (1996)
   PUBMED   8622769
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Patel,S. and Austen,B.
  TITLE     Sequence of the highly conserved gene encoding the human 54kDa
            subunit of signal recognition particle
  JOURNAL   DNA Seq 6 (3), 167-170 (1996)
   PUBMED   8722571
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Miller,J.D., Wilhelm,H., Gierasch,L., Gilmore,R. and Walter,P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle
            during initiation of protein translocation
  JOURNAL   Nature 366 (6453), 351-354 (1993)
   PUBMED   8247130
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049776.3.
            
            On or before May 30, 2025 this sequence version replaced
            XP_011535408.1, XP_054232621.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.165538.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..504
                     /product="signal recognition particle subunit SRP54
                     isoform 1"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 54 kDa protein; signal
                     recognition particle 54kD; signal recognition particle
                     54kDa; signal recognition particle subunit SRP54; SRP54
                     GTPase"
                     /calculated_mol_wt=55574
     Region          1..295
                     /region_name="NG domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     Region          2..430
                     /region_name="SRP54_euk"
                     /note="signal recognition particle protein SRP54;
                     TIGR01425"
                     /db_xref="CDD:273615"
     Region          296..504
                     /region_name="M-domain.
                     /evidence=ECO:0000303|PubMed:34020957"
                     /note="propagated from UniProtKB/Swiss-Prot (P61011.1)"
     CDS             1..504
                     /gene="SRP54"
                     /gene_synonym="SCN8"
                     /coded_by="NM_001440813.1:233..1747"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="GeneID:6729"
                     /db_xref="HGNC:HGNC:11301"
                     /db_xref="MIM:604857"
ORIGIN      
        1 mvladlgrki tsalrslsna tiineevlna mlkevctall eadvniklvk qlrenvksai
       61 dleemasgln krkmiqhavf kelvklvdpg vkawtptkgk qnvimfvglq gsgktttcsk
      121 layyyqrkgw ktclicadtf ragafdqlkq natkaripfy gsytemdpvi iasegvekfk
      181 nenfeiiivd tsgrhkqeds lfeemlqvan aiqpdnivyv mdasigqace aqakafkdkv
      241 dvasvivtkl dghakgggal savaatkspi ifigtgehid dfepfktqpf iskllgmgdi
      301 eglidkvnel klddnealie klkhgqftlr dmyeqfqnim kmgpfsqilg mipgfgtdfm
      361 skgneqesma rlkklmtimd smndqeldst dgakvfskqp griqrvargs gvstrdvqel
      421 ltqytkfaqm vkkmggikgl fkggdmsknv sqsqmaklnq qmakmmdprv lhhmggmagl
      481 qsmmrqfqqg aagnmkgmmg fnnm
//
LOCUS       NP_997512                663 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_997512
VERSION     NP_997512.1
DBSOURCE    REFSEQ: accession NM_207629.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 663)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF323662.1, BC029158.1 and
            X91249.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (7) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF323662.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..663
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 7"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=73901
     Region          57..663
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     CDS             1..663
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_207629.2:80..2071"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS13681.1"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 mimrlpqphg tnassysaem tepksvcvsv devvssnmea tetdllnghl kkvdnnltea
       61 qrfsslprra avniefrdls ysvpegpwwr kkgyktllkg isgkfnsgel vaimgpsgag
      121 kstlmnilag yretgmkgav linglprdlr cfrkvscyim qddmllphlt vqeammvsah
      181 lklqekdegr remvkeilta lgllscantr tgslsggqrk rlaialelvn nppvmffdep
      241 tsgldsascf qvvslmkgla qggrsiicti hqpsaklfel fdqlyvlsqg qcvyrgkvcn
      301 lvpylrdlgl ncptyhnpad fvmevasgey gdqnsrlvra vregmcdsdh krdlggdaev
      361 npflwhrpse edsssmegch sfsascltqf cilfkrtfls imrdsvlthl ritshigigl
      421 ligllylgig neakkvlsns gflffsmlfl mfaalmptvl tfplemgvfl rehlnywysl
      481 kayylaktma dvpfqimfpv aycsivywmt sqpsdavrfv lfaalgtmts lvaqslglli
      541 gaastslqva tfvgpvtaip vllfsgffvs fdtiptylqw msyisyvryg fegvilsiyg
      601 ldredlhcdi detchfqkse ailreldven aklyldfivl giffislrli ayfvlrykir
      661 aer
//
LOCUS       NP_001394033             103 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform c [Homo sapiens].
ACCESSION   NP_001394033
VERSION     NP_001394033.1
DBSOURCE    REFSEQ: accession NM_001407104.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.299691.1,
                                           SRR14038196.3445260.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..103
                     /product="protein max isoform c"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=11968
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     N-acetylserine. /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P61244.1)"
     Region          24..92
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(25,27..29,31..33,35..36,40,59..60)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(39,42..43,45..46,49..51,61,64..65,68,70..72,74..75,
                     77..78,81,84..85,88..89,91..92)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000305|PubMed:17217336; propagated from
                     UniProtKB/Swiss-Prot (P61244.1)"
     CDS             1..103
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407104.1:34..345"
                     /note="isoform c is encoded by transcript variant 22"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekasr
       61 aqildkatey iqymrrknht hqqdiddlkr qnalleqqge ses
//
LOCUS       NP_001394027             124 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform k [Homo sapiens].
ACCESSION   NP_001394027
VERSION     NP_001394027.1
DBSOURCE    REFSEQ: accession NM_001407098.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.355060.1,
                                           SRR14038195.2418980.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968540,
                                           SAMEA2142348 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..124
                     /product="protein max isoform k"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=13926
     Region          <22..56
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..124
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407098.1:179..553"
                     /note="isoform k is encoded by transcript variant 16"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aasraqildk ateyiqymrr knhthqqdid dlkrqnalle
       61 qqvralekar ssaqlqtnyp ssdnslytna kgstisafdg gsdsssesep eepqsrkklr
      121 meas
//
LOCUS       NP_932061                 83 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform f [Homo sapiens].
ACCESSION   NP_932061
VERSION     NP_932061.1
DBSOURCE    REFSEQ: accession NM_197957.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 83)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 83)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 83)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 83)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 83)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 83)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 83)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 83)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 83)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 83)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF038005.1, BC013669.1,
            AI917842.1 and AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon in the coding region and includes an alternate 3' terminal
            exon, compared to variant 1. It encodes isoform f which is shorter
            and has a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI655674.1, CB049360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..83
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..83
                     /product="protein max isoform f"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=9468
     Region          24..>57
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..83
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_197957.4:179..430"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS9770.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdeeqprfqs aadkrahhna lerkrrdhik dsfhslrdsv pslqgekgtk
       61 mkltlppvfp yehlpfptvf chg
//
LOCUS       NP_001394024             151 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform b [Homo sapiens].
ACCESSION   NP_001394024
VERSION     NP_001394024.1
DBSOURCE    REFSEQ: accession NM_001407095.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.949173.1,
                                           SRR18074968.1876564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..151
                     /product="protein max isoform b"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=17071
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..151
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407095.1:34..489"
                     /note="isoform b is encoded by transcript variant 13"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqv ralekarssa qlqtnypssd nslytnakgs
      121 tisafdggsd sssesepeep qsrkklrmea s
//
LOCUS       NP_072054                177 aa            linear   PRI 20-NOV-2025
DEFINITION  somatotropin isoform 3 precursor [Homo sapiens].
ACCESSION   NP_072054
VERSION     NP_072054.1
DBSOURCE    REFSEQ: accession NM_022560.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Huang,X., Chen,H., Shangguan,H., Wu,W., Ai,Z., Chen,Z. and Chen,R.
  TITLE     The clinical and genetic aspects of six individuals with GH1
            variants and isolated growth hormone deficiency type II
  JOURNAL   Front Endocrinol (Lausanne) 15, 1363050 (2024)
   PUBMED   39435354
  REMARK    GeneRIF: The clinical and genetic aspects of six individuals with
            GH1 variants and isolated growth hormone deficiency type II.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Maimaituxun,G., Amano,T., Kenny,G.P., Mundel,T., Kajiki,M.,
            Tagawa,K., Katagiri,A., Tanabe,Y., Watanabe,K., Nishiyasu,T.,
            Kondo,N. and Fujii,N.
  TITLE     GH and IGF-1 in skin interstitial fluid and blood are associated
            with heat loss responses in exercising young adults
  JOURNAL   Eur J Appl Physiol 124 (8), 2285-2301 (2024)
   PUBMED   38446190
  REMARK    GeneRIF: GH and IGF-1 in skin interstitial fluid and blood are
            associated with heat loss responses in exercising young adults.
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Zhou,Z., Luo,Y., Li,K., Zhong,S., Zhu,Y., Yang,H., Wang,L.,
            Chen,S., Duan,L., Gong,F., Gong,G., Zhu,H. and Pan,H.
  TITLE     Brain white matter alterations in young adult male patients with
            childhood-onset growth hormone deficiency: a diffusion tensor
            imaging study
  JOURNAL   Endocrine 83 (3), 724-732 (2024)
   PUBMED   37936007
  REMARK    GeneRIF: Brain white matter alterations in young adult male
            patients with childhood-onset growth hormone deficiency: a
            diffusion tensor imaging study.
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Herman,R., Janez,A., Mikhailidis,D.P., Poredos,P., Blinc,A.,
            Sabovic,M., Studen,K.B., Schernthaner,G.H., Anagnostis,P.,
            Antignani,P.L. and Jensterle,M.
  TITLE     Growth Hormone, Atherosclerosis and Peripheral Arterial Disease:
            Exploring the Spectrum from Acromegaly to Growth Hormone Deficiency
  JOURNAL   Curr Vasc Pharmacol 22 (1), 28-35 (2024)
   PUBMED   37962050
  REMARK    GeneRIF: Growth Hormone, Atherosclerosis and Peripheral Arterial
            Disease: Exploring the Spectrum from Acromegaly to Growth Hormone
            Deficiency.
            Review article
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Fedorczak,A., Lewinski,A. and Stawerska,R.
  TITLE     Involvement of Sirtuin 1 in the Growth Hormone/Insulin-like Growth
            Factor 1 Signal Transduction and Its Impact on Growth Processes in
            Children
  JOURNAL   Int J Mol Sci 24 (20), 15406 (2023)
   PUBMED   37895086
  REMARK    GeneRIF: Involvement of Sirtuin 1 in the Growth
            Hormone/Insulin-like Growth Factor 1 Signal Transduction and Its
            Impact on Growth Processes in Children.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Akinci,A., Kanaka,C., Eble,A., Akar,N., Vidinlisan,S. and
            Mullis,P.E.
  TITLE     Isolated growth hormone (GH) deficiency type IA associated with a
            45-kilobase gene deletion within the human GH gene cluster
  JOURNAL   J Clin Endocrinol Metab 75 (2), 437-441 (1992)
   PUBMED   1322425
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Estes,P.A., Cooke,N.E. and Liebhaber,S.A.
  TITLE     A native RNA secondary structure controls alternative splice-site
            selection and generates two human growth hormone isoforms
  JOURNAL   J Biol Chem 267 (21), 14902-14908 (1992)
   PUBMED   1634529
REFERENCE   8  (residues 1 to 177)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Roskam,W.G. and Rougeon,F.
  TITLE     Molecular cloning and nucleotide sequence of the human growth
            hormone structural gene
  JOURNAL   Nucleic Acids Res 7 (2), 305-320 (1979)
   PUBMED   386281
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Martial,J.A., Hallewell,R.A., Baxter,J.D. and Goodman,H.M.
  TITLE     Human growth hormone: complementary DNA cloning and expression in
            bacteria
  JOURNAL   Science 205 (4406), 602-607 (1979)
   PUBMED   377496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV749353.1 and CD108592.1.
            
            Summary: The protein encoded by this gene is a member of the
            somatotropin/prolactin family of hormones which play an important
            role in growth control. The gene, along with four other related
            genes, is located at the growth hormone locus on chromosome 17
            where they are interspersed in the same transcriptional
            orientation; an arrangement which is thought to have evolved by a
            series of gene duplications. The five genes share a remarkably high
            degree of sequence identity. Alternative splicing generates
            additional isoforms of each of the five growth hormones, leading to
            further diversity and potential for specialization. This particular
            family member is expressed in the pituitary but not in placental
            tissue as is the case for the other four genes in the growth
            hormone locus. Mutations in or deletions of the gene lead to growth
            hormone deficiency and short stature. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) lacks an in-frame exon in the
            central coding region, compared to variant 1. The encoded isoform
            (3) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD106566.1, CD108592.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2151358,
                                           SAMEA2162568 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..177
                     /product="somatotropin isoform 3 precursor"
                     /note="pituitary growth hormone; somatotropin; growth
                     hormone B5"
                     /calculated_mol_wt=17483
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2736
     Region          35..175
                     /region_name="somatotropin_like"
                     /note="Somatotropin or growth hormone (GH), placental
                     lactogen, and related pituitary gland hormones; cd10285"
                     /db_xref="CDD:198435"
     CDS             1..177
                     /gene="GH1"
                     /gene_synonym="GH; GH-N; GHB5; GHN; hGH; hGH-N; IGHD1A;
                     IGHD1B; IGHD2"
                     /coded_by="NM_022560.4:64..597"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS11654.1"
                     /db_xref="GeneID:2688"
                     /db_xref="HGNC:HGNC:4261"
                     /db_xref="MIM:139250"
ORIGIN      
        1 matgsrtsll lafgllclpw lqegsafpti plsrlfdnam lrahrlhqla fdtyqefnle
       61 llrisllliq swlepvqflr svfanslvyg asdsnvydll kdleegiqtl mgrledgspr
      121 tgqifkqtys kfdtnshndd allknyglly cfrkdmdkve tflrivqcrs vegscgf
//
LOCUS       NP_000939                227 aa            linear   PRI 20-NOV-2025
DEFINITION  prolactin precursor [Homo sapiens].
ACCESSION   NP_000939
VERSION     NP_000939.1
DBSOURCE    REFSEQ: accession NM_000948.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wu,T., Duan,Y., Jiang,J., Gu,T., Zhang,P. and Bi,Y.
  TITLE     A Century of Prolactin: Emerging Perspectives as a Metabolic
            Regulator
  JOURNAL   Diabetes Metab Res Rev 40 (6), e3836 (2024)
   PUBMED   39096246
  REMARK    GeneRIF: A Century of Prolactin: Emerging Perspectives as a
            Metabolic Regulator.
            Review article
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Bartos,H.B., Weise,L., Schock,A., Diez,S., Weiss,C.,
            Drommelschmidt,K., Mahnken,A.H., Hummler,H. and Muller,H.
  TITLE     Pronounced neonatal breast enlargement beyond the first week of
            life and its regression correlates with serum prolactin levels - a
            case series
  JOURNAL   J Pediatr Endocrinol Metab 37 (10), 916-923 (2024)
   PUBMED   39135519
  REMARK    GeneRIF: Pronounced neonatal breast enlargement beyond the first
            week of life and its regression correlates with serum prolactin
            levels - a case series.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Lin,W.W., Ou,G.Y., Dai,H.F. and Zhao,W.J.
  TITLE     Neuregulin 4 (Nrg4) cooperates with melatonin to regulate the PRL
            expression via ErbB4/Erk signaling pathway as a potential prolactin
            (PRL) regulator
  JOURNAL   J Cell Biochem 125 (5), e30551 (2024)
   PUBMED   38465779
  REMARK    GeneRIF: Neuregulin 4 (Nrg4) cooperates with melatonin to regulate
            the PRL expression via ErbB4/Erk signaling pathway as a potential
            prolactin (PRL) regulator.
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Miao,X., Fu,Z., Luo,X., Wang,J., Yuan,L., Zhao,S., Feng,Y.,
            Huang,S. and Xiao,S.
  TITLE     A study on the correlations of PRL levels with anxiety, depression,
            sleep, and self-efficacy in patients with prolactinoma
  JOURNAL   Front Endocrinol (Lausanne) 15, 1369729 (2024)
   PUBMED   38572480
  REMARK    GeneRIF: A study on the correlations of PRL levels with anxiety,
            depression, sleep, and self-efficacy in patients with prolactinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Szukiewicz,D.
  TITLE     Current Insights in Prolactin Signaling and Ovulatory Function
  JOURNAL   Int J Mol Sci 25 (4), 1976 (2024)
   PUBMED   38396659
  REMARK    GeneRIF: Current Insights in Prolactin Signaling and Ovulatory
            Function.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Peers,B., Nalda,A.M., Monget,P., Voz,M.L., Belayew,A. and
            Martial,J.A.
  TITLE     Binding of a 100-kDa ubiquitous factor to the human prolactin
            promoter is required for its basal and hormone-regulated activity
  JOURNAL   Eur J Biochem 210 (1), 53-58 (1992)
   PUBMED   1332868
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Maddox,P.R., Jones,D.L. and Mansel,R.E.
  TITLE     Bioactive and immunoactive prolactin levels after TRH-stimulation
            in the sera of normal women
  JOURNAL   Horm Metab Res 24 (4), 181-184 (1992)
   PUBMED   1601394
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Farquhar,M.G., Reid,J.J. and Daniell,L.W.
  TITLE     Intracellular transport and packaging of prolactin: a quantitative
            electron microscope autoradiographic study of mammotrophs
            dissociated from rat pituitaries
  JOURNAL   Endocrinology 102 (1), 296-311 (1978)
   PUBMED   743954
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Shome,B. and Parlow,A.F.
  TITLE     Human pituitary prolactin (hPRL): the entire linear amino acid
            sequence
  JOURNAL   J Clin Endocrinol Metab 45 (5), 1112-1115 (1977)
   PUBMED   925136
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Jacobs,J.W. and Niall,H.D.
  TITLE     High sensitivity automated sequence determination of polypeptides
  JOURNAL   J Biol Chem 250 (10), 3629-3636 (1975)
   PUBMED   1126929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015850.1 and CD106243.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the anterior pituitary hormone
            prolactin. This secreted hormone is a growth regulator for many
            tissues, including cells of the immune system. It may also play a
            role in cell survival by suppressing apoptosis, and it is essential
            for lactation. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Aug
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279860.1893.1, BC015850.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306482.2/ ENSP00000302150.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..227
                     /product="prolactin precursor"
                     /note="decidual prolactin; growth hormone A1; prolactin
                     peptide; luteotropin; luteotropic hormone"
                     /calculated_mol_wt=22898
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2996
     mat_peptide     29..227
                     /product="Prolactin. /id=PRO_0000032916"
                     /note="propagated from UniProtKB/Swiss-Prot (P01236.1)"
                     /calculated_mol_wt=22898
     Region          29..227
                     /region_name="prolactin_like"
                     /note="Prolactin (PRL or PRL1), chorionic
                     somatomammotropin, and related pituitary gland hormones;
                     cd10288"
                     /db_xref="CDD:198438"
     Site            order(29..31,39..41,46,49..50,55,58..59,83..84,94,
                     100..101,150,153,156..157,204..205,208..209,211..213,
                     215..216,219,227)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198438"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial;
                     propagated from UniProtKB/Swiss-Prot (P01236.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15687336; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15687336; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     CDS             1..227
                     /gene="PRL"
                     /gene_synonym="GHA1; pPRL"
                     /coded_by="NM_000948.6:55..738"
                     /db_xref="CCDS:CCDS4548.1"
                     /db_xref="GeneID:5617"
                     /db_xref="HGNC:HGNC:9445"
                     /db_xref="MIM:176760"
ORIGIN      
        1 mnikgspwkg slllllvsnl llcqsvaplp icpggaarcq vtlrdlfdra vvlshyihnl
       61 ssemfsefdk rythgrgfit kainschtss latpedkeqa qqmnqkdfls livsilrswn
      121 eplyhlvtev rgmqeapeai lskaveieeq tkrllegmel ivsqvhpetk eneiypvwsg
      181 lpslqmadee srlsayynll hclrrdshki dnylkllkcr iihnnnc
//
LOCUS       NP_001257997              87 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform g [Homo sapiens].
ACCESSION   NP_001257997
VERSION     NP_001257997.1
DBSOURCE    REFSEQ: accession NM_001271068.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 87)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 87)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 87)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 87)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 87)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 87)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 87)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 87)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 87)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 87)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL833643.1, AI769390.1,
            HY018878.1 and BC013669.1.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (7) lacks two alternate in-frame
            exons in the coding region and includes an alternate 3' terminal
            exon compared to variant 1. It encodes isoform g which is shorter
            and has a distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB528756.1, SRR18074967.102050.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..87
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..87
                     /product="protein max isoform g"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10251
     Region          15..>48
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     CDS             1..87
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001271068.2:179..442"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekly flfwklctpv
       61 lhrqslmqkc htfissyqvh kkkecki
//
LOCUS       NP_525022               1624 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family A member 9 [Homo sapiens].
ACCESSION   NP_525022
VERSION     NP_525022.2
DBSOURCE    REFSEQ: accession NM_080283.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1624)
  AUTHORS   Hwang,H.J., Lee,K.H. and Cho,J.Y.
  TITLE     ABCA9, an ER cholesterol transporter, inhibits breast cancer cell
            proliferation via SREBP-2 signaling
  JOURNAL   Cancer Sci 114 (4), 1451-1463 (2023)
   PUBMED   36576228
  REMARK    GeneRIF: ABCA9, an ER cholesterol transporter, inhibits breast
            cancer cell proliferation via SREBP-2 signaling.
REFERENCE   2  (residues 1 to 1624)
  AUTHORS   Chen,J., Qian,X., He,Y., Han,X. and Pan,Y.
  TITLE     Novel key genes in triple-negative breast cancer identified by
            weighted gene co-expression network analysis
  JOURNAL   J Cell Biochem 120 (10), 16900-16912 (2019)
   PUBMED   31081967
  REMARK    GeneRIF: Novel key genes in triple-negative breast cancer
            identified by weighted gene co-expression network analysis.
REFERENCE   3  (residues 1 to 1624)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1624)
  AUTHORS   Piehler,A., Kaminski,W.E., Wenzel,J.J., Langmann,T. and Schmitz,G.
  TITLE     Molecular structure of a novel cholesterol-responsive A subclass
            ABC transporter, ABCA9
  JOURNAL   Biochem Biophys Res Commun 295 (2), 408-416 (2002)
   PUBMED   12150964
REFERENCE   5  (residues 1 to 1624)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   6  (residues 1 to 1624)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY028899.1, AF423307.1,
            BU072174.1, AW130042.1, BU076154.1, W84726.1 and AC005922.1.
            
            On Jan 3, 2003 this sequence version replaced NP_525022.1.
            
            Summary: This gene is a member of the superfamily of ATP-binding
            cassette (ABC) transporters and the encoded protein contains two
            transmembrane domains and two nucleotide binding folds. ABC
            proteins transport various molecules across extra- and
            intracellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White). This
            gene is a member of the ABC1 subfamily and is clustered with four
            other ABC1 family members on chromosome 17q24. Transcriptional
            expression of this gene is induced during monocyte differentiation
            into macrophages and is suppressed by cholesterol import. [provided
            by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY028899.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340001.9/ ENSP00000342216.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1624
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..1624
                     /product="ATP-binding cassette sub-family A member 9"
                     /EC_number="7.6.2.-"
                     /note="ATP-binding cassette A9; ATP-binding cassette,
                     sub-family A (ABC1), member 9"
                     /calculated_mol_wt=184231
     Site            31..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Region          45..408
                     /region_name="ABC2_membrane_3"
                     /note="ABC-2 family transporter protein; pfam12698"
                     /db_xref="CDD:463674"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            221..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Region          <237..1601
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            329..349
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            354..374
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            398..418
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            864..884
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            949
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1026..1046
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1065..1085
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1108..1128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1136..1156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1163..1183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     Site            1200..1220
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUA7.1)"
     CDS             1..1624
                     /gene="ABCA9"
                     /gene_synonym="EST640918"
                     /coded_by="NM_080283.4:76..4950"
                     /db_xref="CCDS:CCDS11681.1"
                     /db_xref="GeneID:10350"
                     /db_xref="HGNC:HGNC:39"
                     /db_xref="MIM:612507"
ORIGIN      
        1 mskrrmsvgq qtwallcknc lkkwrmkrqt llewlfsfll vlflylffsn lhqvhdtpqm
       61 ssmdlgrvds fndtnyviaf apeskttqei mnkvasapfl kgrtimgwpd eksmdeldln
      121 ysidavrvif tdtfsyhlkf swghripmmk ehrdhsahcq avnekmkceg sefwekgfva
      181 fqaainaaii eiatnhsvme qlmsvtgvhm kilpfvaqgg vatdffiffc iisfstfiyy
      241 vsvnvtqerq yitslmtmmg lresafwlsw glmyagfili matlmalivk saqivvltgf
      301 vmvftlflly glslitlafl msvlikkpfl tglvvflliv fwgilgfpal ytrlpaflew
      361 tlcllspfaf tvgmaqlihl dydvnsnahl dssqnpylii atlfmlvfdt llylvltlyf
      421 dkilpaeygh rcsplfflks cfwfqhgran hvvlenetds dptpndcfep vspefcgkea
      481 iriknlkkey agkcerveal kgvvfdiyeg qitallghsg agkttllnil sglsvptsgs
      541 vtvynhtlsr madieniskf tgfcpqsnvq fgfltvkenl rlfakikgil phevekevqr
      601 vvqelemeni qdilaqnlsg gqnrkltfgi ailgdpqvll ldeptagldp lsrhriwnll
      661 kegksdrvil fstqfidead iladrkvfis ngklkcagss lflkkkwgig yhlslhlner
      721 cdpesitslv kqhisdaklt aqseeklvyi lplertnkfp elyrdldrcs nqgiedygvs
      781 ittlnevflk legkstides digiwgqlqt dgakdigslv eleqvlssfh etrktisgva
      841 lwrqqvcaia kvrflklkke rkslwtilll fgisfipqll ehlfyesyqk sypwelspnt
      901 yflspgqqpq dplthllvin ktgstidnfl hslrrqniai evdafgtrng tddpsyngai
      961 ivsgdekdhr fsiacntkrl ncfpvlldvi sngllgifns sehiqtdrst ffeehmdyey
     1021 gyrsntffwi pmaasftpyi amssigdykk kahsqlrisg lypsaywfgq alvdvslyfl
     1081 illlmqimdy ifspeeiifi iqnlliqilc sigyvsslvf ltyvisfifr ngrknsgiws
     1141 ffflivvifs ivatdlneyg flglffgtml ippftligsl fifseispds mdylgasese
     1201 ivylallipy lhfliflfil rclemncrkk lmrkdpvfri sprsnaifpn peepegeeed
     1261 iqmermrtvn amavrdfdet pviiasclrk eyagkkkncf skrkkkiatr nvsfcvkkge
     1321 vigllghnga gksttikmit gdtkptagqv ilkgsgggep lgflgycpqe nalwpnltvr
     1381 qhlevyaavk glrkgdamia itrlvdalkl qdqlkapvkt lsegikrklc fvlsilgnps
     1441 vvlldepstg mdpegqqqmw qviratfrnt ergalltthy maeaeavcdr vaimvsgrlr
     1501 cigsiqhlks kfgkdyllem klknlaqmep lhaeilrlfp qaaqqerfss lmvyklpved
     1561 vrplsqaffk leivkqsfdl eeyslsqstl eqvflelske qelgdleedf dpsvkwklll
     1621 qeep
//
LOCUS       NP_660087                151 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform b [Homo sapiens].
ACCESSION   NP_660087
VERSION     NP_660087.1
DBSOURCE    REFSEQ: accession NM_145112.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF038005.1, BC025685.1 and
            BC027924.1.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the coding region compared to variant 1. It encodes isoform
            b (also known as the short form) which is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025685.1, SRR3476690.508388.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..151
                     /product="protein max isoform b"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=17071
     Region          15..83
                     /region_name="bHLHzip_Max"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in protein Max and similar proteins; cd11406"
                     /db_xref="CDD:381412"
     Site            order(16,18..20,22..24,26..27,31,50..51)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381412"
     Site            order(30,33..34,36..37,40..42,52,55..56,59,61..63,65..66,
                     68..69,72,75..76,79..80,82..83)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381412"
     CDS             1..151
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_145112.3:179..634"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9772.1"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 msdnddieve sdadkrahhn alerkrrdhi kdsfhslrds vpslqgekas raqildkate
       61 yiqymrrknh thqqdiddlk rqnalleqqv ralekarssa qlqtnypssd nslytnakgs
      121 tisafdggsd sssesepeep qsrkklrmea s
//
LOCUS       NP_001397946             447 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle subunit SRP54 isoform 3 [Homo sapiens].
ACCESSION   NP_001397946 XP_005268081
VERSION     NP_001397946.1
DBSOURCE    REFSEQ: accession NM_001411017.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   McCarthy,P., Cotter,M. and Smith,O.P.
  TITLE     Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features
  JOURNAL   Br J Haematol 196 (3), e39-e42 (2022)
   PUBMED   34549814
  REMARK    GeneRIF: Autosomal dominant Shwachman-Diamond syndrome with a novel
            heterozygous missense variant in the SRP54 gene causing severe
            phenotypic features.
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Schurch,C., Schaefer,T., Muller,J.S., Hanns,P., Arnone,M.,
            Dumlin,A., Scharer,J., Sinning,I., Wild,K., Skokowa,J., Welte,K.,
            Carapito,R., Bahram,S., Konantz,M. and Lengerke,C.
  TITLE     SRP54 mutations induce congenital neutropenia via dominant-negative
            effects on XBP1 splicing
  JOURNAL   Blood 137 (10), 1340-1352 (2021)
   PUBMED   33227812
  REMARK    GeneRIF: SRP54 mutations induce congenital neutropenia via
            dominant-negative effects on XBP1 splicing.
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Juaire,K.D., Lapouge,K., Becker,M.M.M., Kotova,I., Michelhans,M.,
            Carapito,R., Wild,K., Bahram,S. and Sinning,I.
  TITLE     Structural and Functional Impact of SRP54 Mutations Causing Severe
            Congenital Neutropenia
  JOURNAL   Structure 29 (1), 15-28 (2021)
   PUBMED   33053321
  REMARK    GeneRIF: Structural and Functional Impact of SRP54 Mutations
            Causing Severe Congenital Neutropenia.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Goldberg,L., Simon,A.J., Rechavi,G., Lev,A., Barel,O., Kunik,V.,
            Toren,A., Schiby,G., Tamary,H., Steinberg-Shemer,O. and Somech,R.
  TITLE     Congenital neutropenia with variable clinical presentation in novel
            mutation of the SRP54 gene
  JOURNAL   Pediatr Blood Cancer 67 (6), e28237 (2020)
   PUBMED   32277798
  REMARK    GeneRIF: Congenital neutropenia with variable clinical presentation
            in novel mutation of the SRP54 gene.
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Bacher,G., Lutcke,H., Jungnickel,B., Rapoport,T.A. and
            Dobberstein,B.
  TITLE     Regulation by the ribosome of the GTPase of the signal-recognition
            particle during protein targeting
  JOURNAL   Nature 381 (6579), 248-251 (1996)
   PUBMED   8622769
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Patel,S. and Austen,B.
  TITLE     Sequence of the highly conserved gene encoding the human 54kDa
            subunit of signal recognition particle
  JOURNAL   DNA Seq 6 (3), 167-170 (1996)
   PUBMED   8722571
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Miller,J.D., Wilhelm,H., Gierasch,L., Gilmore,R. and Walter,P.
  TITLE     GTP binding and hydrolysis by the signal recognition particle
            during initiation of protein translocation
  JOURNAL   Nature 366 (6453), 351-354 (1993)
   PUBMED   8247130
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Nelson,A. and Myers,K.
  TITLE     Shwachman-Diamond Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301722
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049776.3.
            
            On Aug 20, 2022 this sequence version replaced XP_005268081.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.9673.1,
                                           SRR14038193.3904360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..447
                     /product="signal recognition particle subunit SRP54
                     isoform 3"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 54 kDa protein; signal
                     recognition particle 54kD; signal recognition particle
                     54kDa; signal recognition particle subunit SRP54; SRP54
                     GTPase"
                     /calculated_mol_wt=49304
     Region          2..385
                     /region_name="SRP54_euk"
                     /note="signal recognition particle protein SRP54;
                     TIGR01425"
                     /db_xref="CDD:273615"
     CDS             1..447
                     /gene="SRP54"
                     /gene_synonym="SCN8"
                     /coded_by="NM_001411017.1:258..1601"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91863.1"
                     /db_xref="GeneID:6729"
                     /db_xref="HGNC:HGNC:11301"
                     /db_xref="MIM:604857"
ORIGIN      
        1 mvladlgrki tsalrslsna tiineevlna mlkevctall eadvniklvk qlrenvksai
       61 dleemasgln krkmiqhavf kelvklvdpg vkawtptkgk qnvimfvglq gsgktttcsk
      121 layyyqrkgw ktclicadtf ragafdqlkq natkaripfy gsytemdpvi iasegvekfk
      181 nenfeiiivd tsgrhkqeds lfeemlqvan aiqpdnivyv mdasigqace aqakafkdkv
      241 dvasvivtkl dghakgggal savaatkspi ifigtgehid dfepfktqpf iskllgmgdi
      301 eglidkvnel klddnealie klkhgqftlr dmyeqfqnim kmgpfsqilg mipgfgtdfm
      361 skgneqesma rlkklmtimd smndqggdms knvsqsqmak lnqqmakmmd prvlhhmggm
      421 aglqsmmrqf qqgaagnmkg mmgfnnm
//
LOCUS       NP_001316152             847 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 6 [Homo sapiens].
ACCESSION   NP_001316152
VERSION     NP_001316152.1
DBSOURCE    REFSEQ: accession NM_001329223.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6 and EU794613.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.190849.1,
                                           SRR1803614.163927.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..847
                     /product="neutral alpha-glucosidase AB isoform 6"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=96086
     Region          147..287
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            186
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          287..754
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(332,445,505,518,521,554,579)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          730..798
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..847
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001329223.2:302..2845"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS60817.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 mtrfridele prrpryrvpd vlvadppiar lsvsgrdens veltmaegpy kiiltarpfr
       61 ldlledrsll lsvnarglle fehqraprvs qgskdpaegd gaqpeetprd gdkpeetqgk
      121 aekdepgawe etfkthsdsk pygpmsvgld fslpgmehvy gipehadnlr lkvteggepy
      181 rlynldvfqy elynpmalyg svpvllahnp hrdlgifwln aaetwvdiss ntagktlfgk
      241 mmdylqgsge tpqtdvrwms etgiidvfll lgpsisdvfr qyasltgtqa lpplfslgyh
      301 qsrwnyrdea dvlevdqgfd dhnlpcdviw ldiehadgkr yftwdpsrfp qprtmlerla
      361 skrrklvaiv dphikvdsgy rvheelrnlg lyvktrdgsd yegwcwpgsa gypdftnptm
      421 rawwanmfsy dnyegsapnl fvwndmneps vfngpevtml kdaqhyggwe hrdvhniygl
      481 yvhmatadgl rqrsggmerp fvlaraffag sqrfgavwtg dntaewdhlk isipmclslg
      541 lvglsfcgad vggffknpep ellvrwyqmg ayqpffraha hldtgrrepw llpsqhndii
      601 rdalgqrysl lpfwytllyq ahregipvmr plwvqypqdv ttfniddqyl lgdallvhpv
      661 sdsgahgvqv ylpgqgevwy diqsyqkhhg pqtlylpvtl ssipvfqrgg tivprwmrvr
      721 rssecmkddp itlfvalspq gtaqgelfld dghtfnyqtr qefllrrfsf sgntlvsssa
      781 dpeghfetpi wiervviiga gkpaavvlqt kgspesrlsf qhdpetsvlv lrkpginvas
      841 dwsihlr
//
LOCUS       NP_848695                394 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptide peptidase isoform 2 [Homo sapiens].
ACCESSION   NP_848695
VERSION     NP_848695.1
DBSOURCE    REFSEQ: accession NM_178580.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Avci,D., Heidasch,R., Costa,M., Luchtenborg,C., Kale,D., Brugger,B.
            and Lemberg,M.K.
  TITLE     Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase
  JOURNAL   J Biol Chem 300 (2), 105644 (2024)
   PUBMED   38218226
  REMARK    GeneRIF: Intramembrane protease SPP defines a cholesterol-regulated
            abundance control of the mevalonate pathway enzyme squalene
            synthase.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Mentrup,T., Leinung,N., Patel,M., Fluhrer,R. and Schroder,B.
  TITLE     The role of SPP/SPPL intramembrane proteases in membrane protein
            homeostasis
  JOURNAL   FEBS J 291 (1), 25-44 (2024)
   PUBMED   37625440
  REMARK    GeneRIF: The role of SPP/SPPL intramembrane proteases in membrane
            protein homeostasis.
            Review article
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Yang,H., Li,Z., Wang,Z., Zhang,X., Dai,X., Zhou,G. and Ding,Q.
  TITLE     Histocompatibility Minor 13 (HM13), targeted by miR-760, exerts
            oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway
  JOURNAL   Cell Death Dis 13 (8), 728 (2022)
   PUBMED   36153332
  REMARK    GeneRIF: Histocompatibility Minor 13 (HM13), targeted by miR-760,
            exerts oncogenic role in breast cancer by suppressing autophagy and
            activating PI3K-AKT-mTOR pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Hsu,F.F., Chou,Y.T., Chiang,M.T., Li,F.A., Yeh,C.T., Lee,W.H. and
            Chau,L.Y.
  TITLE     Signal peptide peptidase promotes tumor progression via
            facilitating FKBP8 degradation
  JOURNAL   Oncogene 38 (10), 1688-1701 (2019)
   PUBMED   30348988
  REMARK    GeneRIF: Study demonstrates that SPP is highly induced in lung and
            breast cancers and promotes tumor progression, at least in part, by
            facilitating the degradation of mTOR inhibitor FKBP8.
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Kronenberg-Versteeg,D., Eichmann,M., Russell,M.A., de Ru,A.,
            Hehn,B., Yusuf,N., van Veelen,P.A., Richardson,S.J., Morgan,N.G.,
            Lemberg,M.K. and Peakman,M.
  TITLE     Molecular Pathways for Immune Recognition of Preproinsulin Signal
            Peptide in Type 1 Diabetes
  JOURNAL   Diabetes 67 (4), 687-696 (2018)
   PUBMED   29343547
  REMARK    GeneRIF: Preproinsulin signal peptide epitopes are processed by SPP
            and loaded for HLA-guided immune recognition via pathways that are
            enhanced during type 1 diabetes pathogenesis.
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Wood,A.J., Roberts,R.G., Monk,D., Moore,G.E., Schulz,R. and
            Oakey,R.J.
  TITLE     A screen for retrotransposed imprinted genes reveals an association
            between X chromosome homology and maternal germ-line methylation
  JOURNAL   PLoS Genet 3 (2), e20 (2007)
   PUBMED   17291163
REFERENCE   7  (residues 1 to 394)
  AUTHORS   McLauchlan,J., Lemberg,M.K., Hope,G. and Martoglio,B.
  TITLE     Intramembrane proteolysis promotes trafficking of hepatitis C virus
            core protein to lipid droplets
  JOURNAL   EMBO J 21 (15), 3980-3988 (2002)
   PUBMED   12145199
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Grigorenko,A.P., Moliaka,Y.K., Korovaitseva,G.I. and Rogaev,E.I.
  TITLE     Novel class of polytopic proteins with domains associated with
            putative protease activity
  JOURNAL   Biochemistry (Mosc) 67 (7), 826-835 (2002)
   PUBMED   12139484
  REMARK    GeneRIF: identification and molecular cloning; expression analysis
            of the hIMP1 gene (located on chromosome 20) was performed in human
            cell tissues and transfected cell cultures [IMP1]
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Weihofen,A., Binns,K., Lemberg,M.K., Ashman,K. and Martoglio,B.
  TITLE     Identification of signal peptide peptidase, a presenilin-type
            aspartic protease
  JOURNAL   Science 296 (5576), 2215-2218 (2002)
   PUBMED   12077416
  REMARK    GeneRIF: identified human signal peptide peptidase as a polytopic
            membrane protein with sequence motifs characteristic of the
            presenilin-type aspartic proteases [SPP]
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Lemberg,M.K., Bland,F.A., Weihofen,A., Braud,V.M. and Martoglio,B.
  TITLE     Intramembrane proteolysis of signal peptides: an essential step in
            the generation of HLA-E epitopes
  JOURNAL   J Immunol 167 (11), 6441-6446 (2001)
   PUBMED   11714810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552780.1 and DQ168450.1.
            
            Summary: The protein encoded by this gene, which localizes to the
            endoplasmic reticulum, catalyzes intramembrane proteolysis of some
            signal peptides after they have been cleaved from a preprotein.
            This activity is required to generate signal sequence-derived human
            lymphocyte antigen-E epitopes that are recognized by the immune
            system, and to process hepatitis C virus core protein. The encoded
            protein is an integral membrane protein with sequence motifs
            characteristic of the presenilin-type aspartic proteases. Multiple
            transcript variants encoding several different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an alternate exon
            compared to variant 1, that causes a frameshift. The resulting
            isoform (2) is longer and has a distinct C-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ168450.1, AY169310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 17291163
            NMD candidate  :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..394
                     /product="signal peptide peptidase isoform 2"
                     /EC_number="3.4.23.-"
                     /note="minor histocompatibility antigen 13; minor
                     histocompatibility antigen H13; presenilin-like protein 3;
                     signal peptide peptidase beta; intramembrane protease 1;
                     signal peptide peptidase like 1; HM13 intronic transcript
                     1"
                     /calculated_mol_wt=43292
     Region          63..350
                     /region_name="Peptidase_A22B"
                     /note="Signal peptide peptidase; pfam04258"
                     /db_xref="CDD:282158"
     CDS             1..394
                     /gene="HM13"
                     /gene_synonym="H13; HM13-IT1; IMP1; IMPAS; IMPAS-1;
                     MSTP086; PSENL3; PSL3; SPP; SPPL1"
                     /coded_by="NM_178580.3:111..1295"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13183.1"
                     /db_xref="GeneID:81502"
                     /db_xref="HGNC:HGNC:16435"
                     /db_xref="MIM:607106"
ORIGIN      
        1 mdsalsdphn gsaeaggptn sttrppstpe gialaygsll lmallpiffg alrsvrcarg
       61 knasdmpeti tsrdaarfpi iasctllgly lffkifsqey inlllsmyff vlgilalsht
      121 ispfmnkffp asfpnrqyql lftqgsgenk eeiinyefdt kdlvclglss ivgvwyllrk
      181 hwiannlfgl afslngvell hlnnvstgci llgglfiydv fwvfgtnvmv tvaksfeapi
      241 klvfpqdlle kgleannfam lglgdvvipg ifialllrfd islkknthty fytsfaayif
      301 glgltifimh ifkhaqpall ylvpacigfp vlvalakgev temfsyessa eilphtprlt
      361 hfptvsgspa sladsmqqkl agprrrrpqn psam
//
LOCUS       NP_001342203             334 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA 2'-O-methyltransferase FBLL1 [Homo sapiens].
ACCESSION   NP_001342203 XP_001722581 XP_001725399 XP_293903
VERSION     NP_001342203.1
DBSOURCE    REFSEQ: accession NM_001355274.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Zhang,D., Li,B., Xu,H., Li,J., Ma,C., Ge,W., Lu,C. and Cao,X.
  TITLE     Identification of FBLL1 as a neuron-specific RNA
            2'-O-methyltransferase mediating neuronal differentiation
  JOURNAL   Proc Natl Acad Sci U S A 121 (48), e2406961121 (2024)
   PUBMED   39570315
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020894.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: ERR279832.1192.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338333.5/ ENSP00000473383.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..334
                     /product="RNA 2'-O-methyltransferase FBLL1"
                     /note="protein-glutamine methyltransferase; rRNA/tRNA
                     2'-O-methyltransferase fibrillarin-like protein 1;
                     fibrillarin like 1"
                     /calculated_mol_wt=34672
     mat_peptide     1..333
                     /product="RNA 2'-O-methyltransferase FBLL1.
                     /id=PRO_0000331762"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ2.2)"
                     /calculated_mol_wt=34675
     Region          1..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ2.2)"
     Site            8
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ2.2)"
     Site            15
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q80WS3; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ2.2)"
     Site            27
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ2.2)"
     Region          90..331
                     /region_name="PTZ00146"
                     /note="fibrillarin; Provisional"
                     /db_xref="CDD:240291"
     CDS             1..334
                     /gene="FBLL1"
                     /coded_by="NM_001355274.2:201..1205"
                     /db_xref="CCDS:CCDS87345.1"
                     /db_xref="GeneID:345630"
                     /db_xref="HGNC:HGNC:35458"
ORIGIN      
        1 mksaassrgg ggggrggggw gswgggrggg ggagkggggd gggqggkggf garargfggg
       61 grgrgrgggd gkdrggggqr rggvaksksr rrkgamvvsv ephrhegvfi yrgaedalvt
      121 lnmvpgqsvy gerrvtvteg gvkqeyrtwn pfrsklaaai lggvdqihik pkskvlylga
      181 asgttvshvs diigpdglvy avefshragr dlvnvakkrt niipvledar hplkyrmlig
      241 mvdvifadva qpdqsrival nahtflrngg hflisikanc idstasaeav fasevrklqq
      301 enlkpqeqlt lepyerdhav vvgvyrplpk sssk
//
LOCUS       NP_001634                100 aa            linear   PRI 20-NOV-2025
DEFINITION  apolipoprotein A-II preproprotein [Homo sapiens].
ACCESSION   NP_001634
VERSION     NP_001634.1
DBSOURCE    REFSEQ: accession NM_001643.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 100)
  AUTHORS   Kim,M., Lee,S., Cho,E., Hong,K.W., You,S.J. and Choi,H.J.
  TITLE     CETP and APOA2 polymorphisms are associated with weight loss and
            healthy eating behavior changes in response to digital lifestyle
            modifications
  JOURNAL   Sci Rep 13 (1), 21615 (2023)
   PUBMED   38062157
  REMARK    GeneRIF: CETP and APOA2 polymorphisms are associated with weight
            loss and healthy eating behavior changes in response to digital
            lifestyle modifications.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 100)
  AUTHORS   Futagami,S., Agawa,S., Nakamura,K., Watanabe,Y., Habiro,M.,
            Kawawa,R., Yamawaki,H., Tsushima,R., Kirita,K., Akimoto,T.,
            Ueki,N., Tomohide,T., Itokawa,N., Suzuki,N., Naito,Y., Takeuchi,K.,
            Kashiro,A., Ohta,R., Mizutani,S., Taniai,N., Yoshida,H., Iwakiri,K.
            and Honda,K.
  TITLE     Apolipoprotein A2 isoforms associated with exocrine pancreatic
            insufficiency in early chronic pancreatitis
  JOURNAL   J Gastroenterol Hepatol 38 (11), 1949-1957 (2023)
   PUBMED   37501507
  REMARK    GeneRIF: Apolipoprotein A2 isoforms associated with exocrine
            pancreatic insufficiency in early chronic pancreatitis.
REFERENCE   3  (residues 1 to 100)
  AUTHORS   Wilkins,J.T. and Rohatgi,A.
  TITLE     Resolution of apolipoprotein A1 and A2 proteoforms: their
            cardiometabolic correlates and implications for future research
  JOURNAL   Curr Opin Lipidol 33 (4), 264-269 (2022)
   PUBMED   36082946
  REMARK    GeneRIF: Resolution of apolipoprotein A1 and A2 proteoforms: their
            cardiometabolic correlates and implications for future research.
            Review article
REFERENCE   4  (residues 1 to 100)
  AUTHORS   Abaj,F., Esmaeily,Z., Naeini,Z., Rafiee,M. and Koohdani,F.
  TITLE     Dietary acid load modifies the effects of ApoA2-265 T > C
            polymorphism on lipid profile and serum leptin and ghrelin levels
            among type 2 diabetic patients
  JOURNAL   BMC Endocr Disord 22 (1), 190 (2022)
   PUBMED   35883173
  REMARK    GeneRIF: Dietary acid load modifies the effects of ApoA2-265 T > C
            polymorphism on lipid profile and serum leptin and ghrelin levels
            among type 2 diabetic patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 100)
  AUTHORS   Wilkins,J.T., Seckler,H.S., Rink,J., Compton,P.D., Fornelli,L.,
            Thaxton,C.S., LeDuc,R., Jacobs,D., Doubleday,P.F., Sniderman,A.,
            Lloyd-Jones,D.M. and Kelleher,N.L.
  TITLE     Spectrum of Apolipoprotein AI and Apolipoprotein AII Proteoforms
            and Their Associations With Indices of Cardiometabolic Health: The
            CARDIA Study
  JOURNAL   J Am Heart Assoc 10 (17), e019890 (2021)
   PUBMED   34472376
  REMARK    GeneRIF: Spectrum of Apolipoprotein AI and Apolipoprotein AII
            Proteoforms and Their Associations With Indices of Cardiometabolic
            Health: The CARDIA Study.
REFERENCE   6  (residues 1 to 100)
  AUTHORS   Bekaert,E.D., Alaupovic,P., Knight-Gibson,C., Norum,R.A., Laux,M.J.
            and Ayrault-Jarrier,M.
  TITLE     Isolation and partial characterization of lipoprotein A-II
            (LP-A-II) particles of human plasma
  JOURNAL   Biochim Biophys Acta 1126 (1), 105-113 (1992)
   PUBMED   1606170
  REMARK    Erratum:[Biochim Biophys Acta 1992 Jul 9;1127(1):103]
REFERENCE   7  (residues 1 to 100)
  AUTHORS   Vollmer,E., Brust,J., Roessner,A., Bosse,A., Burwikel,F.,
            Kaesberg,B., Harrach,B., Robenek,H. and Bocker,W.
  TITLE     Distribution patterns of apolipoproteins A1, A2, and B in the wall
            of atherosclerotic vessels
  JOURNAL   Virchows Arch A Pathol Anat Histopathol 419 (2), 79-88 (1991)
   PUBMED   1908160
REFERENCE   8  (residues 1 to 100)
  AUTHORS   Deeb,S.S., Takata,K., Peng,R.L., Kajiyama,G. and Albers,J.J.
  TITLE     A splice-junction mutation responsible for familial apolipoprotein
            A-II deficiency
  JOURNAL   Am J Hum Genet 46 (4), 822-827 (1990)
   PUBMED   2107739
REFERENCE   9  (residues 1 to 100)
  AUTHORS   Ritter,M.C. and Scanu,A.M.
  TITLE     Apolipoprotein A-II and structure of human serum high density
            lipoproteins. An approach by reassembly techniques
  JOURNAL   J Biol Chem 254 (7), 2517-2525 (1979)
   PUBMED   218942
REFERENCE   10 (residues 1 to 100)
  AUTHORS   Weisgraber,K.H. and Mahley,R.W.
  TITLE     Apoprotein (E--A-II) complex of human plasma lipoproteins. I.
            Characterization of this mixed disulfide and its identification in
            a high density lipoprotein subfraction
  JOURNAL   J Biol Chem 253 (17), 6281-6288 (1978)
   PUBMED   210174
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590714.27.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes apolipoprotein (apo-) A-II, which is the
            second most abundant protein of the high density lipoprotein
            particles. The protein is found in plasma as a monomer, homodimer,
            or heterodimer with apolipoprotein D. Defects in this gene may
            result in apolipoprotein A-II deficiency or hypercholesterolemia.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV681656.1, AV682018.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367990.7/ ENSP00000356969.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..100
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..100
                     /product="apolipoprotein A-II preproprotein"
                     /note="apolipoprotein A-II"
                     /calculated_mol_wt=8708
     Region          1..98
                     /region_name="ApoA-II"
                     /note="Apolipoprotein A-II (ApoA-II); pfam04711"
                     /db_xref="CDD:461404"
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2485
     proprotein      19..100
                     /product="apolipoprotein A-II proprotein"
                     /calculated_mol_wt=9304
     mat_peptide     24..100
                     /product="apolipoprotein A-II"
                     /calculated_mol_wt=8708
     CDS             1..100
                     /gene="APOA2"
                     /gene_synonym="Apo-AII; ApoA-II; APOA2D; apoAII"
                     /coded_by="NM_001643.2:59..361"
                     /db_xref="CCDS:CCDS1226.1"
                     /db_xref="GeneID:336"
                     /db_xref="HGNC:HGNC:601"
                     /db_xref="MIM:107670"
ORIGIN      
        1 mkllaatvll lticslegal vrrqakepcv eslvsqyfqt vtdygkdlme kvkspelqae
       61 aksyfekske qltplikkag telvnflsyf velgtqpatq
//
LOCUS       NP_001317145             401 aa            linear   PRI 20-NOV-2025
DEFINITION  2',3'-cyclic-nucleotide 3'-phosphodiesterase isoform 2 [Homo
            sapiens].
ACCESSION   NP_001317145 XP_006721764
VERSION     NP_001317145.1
DBSOURCE    REFSEQ: accession NM_001330216.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Qu,W., Jiang,L. and Hou,G.
  TITLE     Circ-AFF2/miR-650/CNP axis promotes proliferation, inflammatory
            response, migration, and invasion of rheumatoid arthritis synovial
            fibroblasts
  JOURNAL   J Orthop Surg Res 16 (1), 165 (2021)
   PUBMED   33653372
  REMARK    GeneRIF: Circ-AFF2/miR-650/CNP axis promotes proliferation,
            inflammatory response, migration, and invasion of rheumatoid
            arthritis synovial fibroblasts.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Al-Abdi,L., Al Murshedi,F., Elmanzalawy,A., Al Habsi,A., Helaby,R.,
            Ganesh,A., Ibrahim,N., Patel,N. and Alkuraya,F.S.
  TITLE     CNP deficiency causes severe hypomyelinating leukodystrophy in
            humans
  JOURNAL   Hum Genet 139 (5), 615-622 (2020)
   PUBMED   32128616
  REMARK    GeneRIF: CNP deficiency causes severe hypomyelinating
            leukodystrophy.
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Li,Y., Zhao,Y. and Wang,Y.
  TITLE     2',3'-Cyclic-nucleotide 3'-phosphodiesterase contributes to
            epithelial-mesenchymal transition of lens epithelial cells through
            the notch signalling pathway
  JOURNAL   Cell Prolif 52 (6), e12707 (2019)
   PUBMED   31617266
  REMARK    GeneRIF: 2',3'-Cyclic-nucleotide 3'-phosphodiesterase contributes
            to epithelial-mesenchymal transition of lens epithelial cells
            through the notch signalling pathway
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Garcia-Agudo,L.F., Janova,H., Sendler,L.E., Arinrad,S.,
            Steixner,A.A., Hassouna,I., Balmuth,E., Ronnenberg,A., Schopf,N.,
            van der Flier,F.J., Begemann,M., Martens,H., Weber,M.S.,
            Boretius,S., Nave,K.A. and Ehrenreich,H.
  TITLE     Genetically induced brain inflammation by Cnp deletion transiently
            benefits from microglia depletion
  JOURNAL   FASEB J 33 (7), 8634-8647 (2019)
   PUBMED   31090455
  REMARK    GeneRIF: Catatonia-related executive dysfunction and brain atrophy
            of Cnp(-/-) mice fail to improve under PLX5622.
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Thompson,R.J.
  TITLE     2',3'-cyclic nucleotide-3'-phosphohydrolase and signal transduction
            in central nervous system myelin
  JOURNAL   Biochem Soc Trans 20 (3), 621-626 (1992)
   PUBMED   1385234
  REMARK    Review article
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Douglas,A.J., Fox,M.F., Abbott,C.M., Hinks,L.J., Sharpe,G.,
            Povey,S. and Thompson,R.J.
  TITLE     Structure and chromosomal localization of the human 2',3'-cyclic
            nucleotide 3'-phosphodiesterase gene
  JOURNAL   Ann Hum Genet 56 (3), 243-254 (1992)
   PUBMED   1360194
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Sprinkle,T.J., Lanclos,K.D. and Lapp,D.F.
  TITLE     Assignment of the human 2',3'-cyclic nucleotide 3'-phosphohydrolase
            gene to chromosome 17
  JOURNAL   Genomics 13 (3), 877-880 (1992)
   PUBMED   1322358
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Leroy,M.J., Dumler,I., Lugnier,C., Shushakova,N.D. and Ferre,F.
  TITLE     A new peptide (1150Da) selectively activates the calcium-calmodulin
            sensitive isoform of cyclic nucleotide phosphodiesterase from human
            myometrium
  JOURNAL   Biochem Biophys Res Commun 184 (2), 700-705 (1992)
   PUBMED   1315529
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Staugaitis,S.M., Bernier,L., Smith,P.R. and Colman,D.R.
  TITLE     Expression of the oligodendrocyte marker 2'3'-cyclic nucleotide
            3'-phosphodiesterase in non-glial cells
  JOURNAL   J Neurosci Res 25 (4), 556-560 (1990)
   PUBMED   2161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC125257.4 and HY337437.1.
            
            On Aug 20, 2016 this sequence version replaced XP_006721764.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.255924.1,
                                           SRR1803617.112239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..401
                     /product="2',3'-cyclic-nucleotide 3'-phosphodiesterase
                     isoform 2"
                     /EC_number="3.1.4.37"
                     /note="2', 3' cyclic nucleotide 3' phosphohydrolase;
                     CNPase; 2'',3''-cyclic nucleotide 3'' phosphodiesterase"
                     /calculated_mol_wt=44968
     Region          30..>128
                     /region_name="COG4639"
                     /note="Predicted kinase [General function prediction
                     only]"
                     /db_xref="CDD:443677"
     Region          166..379
                     /region_name="CNPase"
                     /note="2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP
                     or CNPase); pfam05881"
                     /db_xref="CDD:461769"
     CDS             1..401
                     /gene="CNP"
                     /gene_synonym="CN37; CNP1; HLD20"
                     /coded_by="NM_001330216.2:215..1420"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82123.1"
                     /db_xref="GeneID:1267"
                     /db_xref="HGNC:HGNC:2158"
                     /db_xref="MIM:123830"
ORIGIN      
        1 msssgakdkp elqfpflqde dtvatlleck tlfilrglpg sgkstlarvi vdkyrdgtkm
       61 vsadaykitp gargafseey krldedlaay crrrdirilv lddtnherer leqlfemadq
      121 yqyqvvlvep ktawrldcaq lkeknqwqls addlkklkpg lekdflplyf gwfltkksse
      181 tlrkagqvfl eelgnhkafk kelrqfvpgd eprekmdlvt yfgkrppgvl hcttkfcdyg
      241 kapgaeeyaq qdvlkksysk aftltisalf vtpkttgarv elseqqlqlw psdvdklspt
      301 dnlprgsrah itlgcaadve avqtgldlle ilrqekggsr geevgelsrg klyslgngrw
      361 mltlaknmev raiftgyygk gkpvptqgsr kggalqscti i
//
LOCUS       NP_002931                599 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family E member 1 [Homo sapiens].
ACCESSION   NP_002931
VERSION     NP_002931.2
DBSOURCE    REFSEQ: accession NM_002940.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Tong,S., Zhu,Y., Leng,Y., Wu,Y., Xiao,X., Zhao,W. and Tan,S.
  TITLE     Restoration of miR-299-3p promotes macrophage phagocytosis and
            suppresses malignant phenotypes in breast cancer carcinogenesis via
            dual-targeting CD47 and ABCE1
  JOURNAL   Int Immunopharmacol 130, 111708 (2024)
   PUBMED   38394889
  REMARK    GeneRIF: Restoration of miR-299-3p promotes macrophage phagocytosis
            and suppresses malignant phenotypes in breast cancer carcinogenesis
            via dual-targeting CD47 and ABCE1.
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   3  (residues 1 to 599)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Sun,L., Ding,X. and Kang,Y.J.
  TITLE     ABCE1 selectively promotes HIF-1alpha transactivation of angiogenic
            gene expression
  JOURNAL   J Trace Elem Med Biol 80, 127307 (2023)
   PUBMED   37738929
  REMARK    GeneRIF: ABCE1 selectively promotes HIF-1alpha transactivation of
            angiogenic gene expression.
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Martinand,C., Montavon,C., Salehzada,T., Silhol,M., Lebleu,B. and
            Bisbal,C.
  TITLE     RNase L inhibitor is induced during human immunodeficiency virus
            type 1 infection and down regulates the 2-5A/RNase L pathway in
            human T cells
  JOURNAL   J Virol 73 (1), 290-296 (1999)
   PUBMED   9847332
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Martinand,C., Salehzada,T., Silhol,M., Lebleu,B. and Bisbal,C.
  TITLE     RNase L inhibitor (RLI) antisense constructions block partially the
            down regulation of the 2-5A/RNase L pathway in
            encephalomyocarditis-virus-(EMCV)-infected cells
  JOURNAL   Eur J Biochem 254 (2), 248-255 (1998)
   PUBMED   9660177
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Diriong,S., Salehzada,T., Bisbal,C., Martinand,C. and Taviaux,S.
  TITLE     Localization of the ribonuclease L inhibitor gene (RNS4I), a new
            member of the interferon-regulated 2-5A pathway, to 4q31 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 32 (3), 488-490 (1996)
   PUBMED   8838820
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Aubry,F., Mattei,M.G., Barque,J.P. and Galibert,F.
  TITLE     Chromosomal localization and expression pattern of the RNase L
            inhibitor gene
  JOURNAL   FEBS Lett 381 (1-2), 135-139 (1996)
   PUBMED   8641422
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Bisbal,C., Martinand,C., Silhol,M., Lebleu,B. and Salehzada,T.
  TITLE     Cloning and characterization of a RNAse L inhibitor. A new
            component of the interferon-regulated 2-5A pathway
  JOURNAL   J Biol Chem 270 (22), 13308-13317 (1995)
   PUBMED   7539425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA218189.1, BC016283.1 and
            AC096757.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2006 this sequence version replaced NP_002931.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the OABP subfamily. Alternatively referred
            to as the RNase L inhibitor, this protein functions to block the
            activity of ribonuclease L. Activation of ribonuclease L leads to
            inhibition of protein synthesis in the 2-5A/RNase L system, the
            central pathway for viral interferon action. Two transcript
            variants encoding the same protein have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.120695.1,
                                           SRR1660807.133363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296577.9/ ENSP00000296577.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21"
     Protein         1..599
                     /product="ATP-binding cassette sub-family E member 1"
                     /EC_number="3.6.5.-"
                     /note="ribonuclease L (2',5'-oligoisoadenylate
                     synthetase-dependent) inhibitor; huHP68; ribonuclease 4
                     inhibitor; 2'-5'-oligoadenylate-binding protein;
                     ATP-binding cassette, sub-family E (OABP), member 1; RNase
                     L inhibitor 1"
                     /calculated_mol_wt=67184
     Region          6..598
                     /region_name="Rli1"
                     /note="Translation initiation factor RLI1, contains Fe-S
                     and AAA+ ATPase domains [Translation, ribosomal structure
                     and biogenesis]; COG1245"
                     /db_xref="CDD:440858"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61221.1)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P61221.1)"
     CDS             1..599
                     /gene="ABCE1"
                     /gene_synonym="ABC38; OABP; RLI; RLI1; RNASEL1; RNASELI;
                     RNS4I"
                     /coded_by="NM_002940.3:137..1936"
                     /db_xref="CCDS:CCDS34071.1"
                     /db_xref="GeneID:6059"
                     /db_xref="HGNC:HGNC:69"
                     /db_xref="MIM:601213"
ORIGIN      
        1 madkltriai vnhdkckpkk crqeckkscp vvrmgklcie vtpqskiawi setlcigcgi
       61 cikkcpfgal sivnlpsnle ketthrycan afklhrlpip rpgevlglvg tngigkstal
      121 kilagkqkpn lgkyddppdw qeiltyfrgs elqnyftkil eddlkaiikp qyvdqipkaa
      181 kgtvgsildr kdetktqaiv cqqldlthlk ernvedlsgg elqrfacavv ciqkadifmf
      241 depssyldvk qrlkaaitir slinpdryii vvehdlsvld ylsdficcly gvpsaygvvt
      301 mpfsvregin ifldgyvpte nlrfrdaslv fkvaetanee evkkmcmyky pgmkkkmgef
      361 elaivageft dseimvmlge ngtgkttfir mlagrlkpde ggevpvlnvs ykpqkispks
      421 tgsvrqllhe kirdaythpq fvtdvmkplq ieniidqevq tlsggelqrv alalclgkpa
      481 dvylidepsa yldseqrlma arvvkrfilh akktafvveh dfimatylad rvivfdgvps
      541 kntvanspqt llagmnkfls qleitfrrdp nnyrprinkl nsikdveqkk sgnyffldd
//
LOCUS       NP_000506                217 aa            linear   PRI 20-NOV-2025
DEFINITION  somatotropin isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000506
VERSION     NP_000506.2
DBSOURCE    REFSEQ: accession NM_000515.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Huang,X., Chen,H., Shangguan,H., Wu,W., Ai,Z., Chen,Z. and Chen,R.
  TITLE     The clinical and genetic aspects of six individuals with GH1
            variants and isolated growth hormone deficiency type II
  JOURNAL   Front Endocrinol (Lausanne) 15, 1363050 (2024)
   PUBMED   39435354
  REMARK    GeneRIF: The clinical and genetic aspects of six individuals with
            GH1 variants and isolated growth hormone deficiency type II.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Maimaituxun,G., Amano,T., Kenny,G.P., Mundel,T., Kajiki,M.,
            Tagawa,K., Katagiri,A., Tanabe,Y., Watanabe,K., Nishiyasu,T.,
            Kondo,N. and Fujii,N.
  TITLE     GH and IGF-1 in skin interstitial fluid and blood are associated
            with heat loss responses in exercising young adults
  JOURNAL   Eur J Appl Physiol 124 (8), 2285-2301 (2024)
   PUBMED   38446190
  REMARK    GeneRIF: GH and IGF-1 in skin interstitial fluid and blood are
            associated with heat loss responses in exercising young adults.
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Zhou,Z., Luo,Y., Li,K., Zhong,S., Zhu,Y., Yang,H., Wang,L.,
            Chen,S., Duan,L., Gong,F., Gong,G., Zhu,H. and Pan,H.
  TITLE     Brain white matter alterations in young adult male patients with
            childhood-onset growth hormone deficiency: a diffusion tensor
            imaging study
  JOURNAL   Endocrine 83 (3), 724-732 (2024)
   PUBMED   37936007
  REMARK    GeneRIF: Brain white matter alterations in young adult male
            patients with childhood-onset growth hormone deficiency: a
            diffusion tensor imaging study.
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Herman,R., Janez,A., Mikhailidis,D.P., Poredos,P., Blinc,A.,
            Sabovic,M., Studen,K.B., Schernthaner,G.H., Anagnostis,P.,
            Antignani,P.L. and Jensterle,M.
  TITLE     Growth Hormone, Atherosclerosis and Peripheral Arterial Disease:
            Exploring the Spectrum from Acromegaly to Growth Hormone Deficiency
  JOURNAL   Curr Vasc Pharmacol 22 (1), 28-35 (2024)
   PUBMED   37962050
  REMARK    GeneRIF: Growth Hormone, Atherosclerosis and Peripheral Arterial
            Disease: Exploring the Spectrum from Acromegaly to Growth Hormone
            Deficiency.
            Review article
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Fedorczak,A., Lewinski,A. and Stawerska,R.
  TITLE     Involvement of Sirtuin 1 in the Growth Hormone/Insulin-like Growth
            Factor 1 Signal Transduction and Its Impact on Growth Processes in
            Children
  JOURNAL   Int J Mol Sci 24 (20), 15406 (2023)
   PUBMED   37895086
  REMARK    GeneRIF: Involvement of Sirtuin 1 in the Growth
            Hormone/Insulin-like Growth Factor 1 Signal Transduction and Its
            Impact on Growth Processes in Children.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Akinci,A., Kanaka,C., Eble,A., Akar,N., Vidinlisan,S. and
            Mullis,P.E.
  TITLE     Isolated growth hormone (GH) deficiency type IA associated with a
            45-kilobase gene deletion within the human GH gene cluster
  JOURNAL   J Clin Endocrinol Metab 75 (2), 437-441 (1992)
   PUBMED   1322425
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Estes,P.A., Cooke,N.E. and Liebhaber,S.A.
  TITLE     A native RNA secondary structure controls alternative splice-site
            selection and generates two human growth hormone isoforms
  JOURNAL   J Biol Chem 267 (21), 14902-14908 (1992)
   PUBMED   1634529
REFERENCE   8  (residues 1 to 217)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Roskam,W.G. and Rougeon,F.
  TITLE     Molecular cloning and nucleotide sequence of the human growth
            hormone structural gene
  JOURNAL   Nucleic Acids Res 7 (2), 305-320 (1979)
   PUBMED   386281
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Martial,J.A., Hallewell,R.A., Baxter,J.D. and Goodman,H.M.
  TITLE     Human growth hormone: complementary DNA cloning and expression in
            bacteria
  JOURNAL   Science 205 (4406), 602-607 (1979)
   PUBMED   377496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV749353.1 and BC090045.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 21, 2001 this sequence version replaced NP_000506.1.
            
            Summary: The protein encoded by this gene is a member of the
            somatotropin/prolactin family of hormones which play an important
            role in growth control. The gene, along with four other related
            genes, is located at the growth hormone locus on chromosome 17
            where they are interspersed in the same transcriptional
            orientation; an arrangement which is thought to have evolved by a
            series of gene duplications. The five genes share a remarkably high
            degree of sequence identity. Alternative splicing generates
            additional isoforms of each of the five growth hormones, leading to
            further diversity and potential for specialization. This particular
            family member is expressed in the pituitary but not in placental
            tissue as is the case for the other four genes in the growth
            hormone locus. Mutations in or deletions of the gene lead to growth
            hormone deficiency and short stature. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY613431.1, SRR5189667.317972.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162568 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323322.10/ ENSP00000312673.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..217
                     /product="somatotropin isoform 1 precursor"
                     /note="pituitary growth hormone; somatotropin; growth
                     hormone B5"
                     /calculated_mol_wt=22129
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2736
     mat_peptide     27..217
                     /product="Somatotropin. /id=PRO_0000032988"
                     /note="propagated from UniProtKB/Swiss-Prot (P01241.2)"
                     /calculated_mol_wt=22129
     Region          35..215
                     /region_name="somatotropin_like"
                     /note="Somatotropin or growth hormone (GH), placental
                     lactogen, and related pituitary gland hormones; cd10285"
                     /db_xref="CDD:198435"
     Site            order(35,38,41..42,44,47..48,51,67..68,71..72,74,87..90,
                     93..94,142,145..146,149,190,193..194,197..198,200..201,
                     204..205,208,215)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198435"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14997482; propagated from
                     UniProtKB/Swiss-Prot (P01241.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14997482; propagated from
                     UniProtKB/Swiss-Prot (P01241.2)"
     CDS             1..217
                     /gene="GH1"
                     /gene_synonym="GH; GH-N; GHB5; GHN; hGH; hGH-N; IGHD1A;
                     IGHD1B; IGHD2"
                     /coded_by="NM_000515.5:64..717"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11653.1"
                     /db_xref="GeneID:2688"
                     /db_xref="HGNC:HGNC:4261"
                     /db_xref="MIM:139250"
ORIGIN      
        1 matgsrtsll lafgllclpw lqegsafpti plsrlfdnam lrahrlhqla fdtyqefeea
       61 yipkeqkysf lqnpqtslcf sesiptpsnr eetqqksnle llrisllliq swlepvqflr
      121 svfanslvyg asdsnvydll kdleegiqtl mgrledgspr tgqifkqtys kfdtnshndd
      181 allknyglly cfrkdmdkve tflrivqcrs vegscgf
//
LOCUS       NP_001316151             847 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 6 [Homo sapiens].
ACCESSION   NP_001316151
VERSION     NP_001316151.1
DBSOURCE    REFSEQ: accession NM_001329222.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6 and EU794613.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.781936.1,
                                           SRR14038194.3763226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..847
                     /product="neutral alpha-glucosidase AB isoform 6"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=96086
     Region          147..287
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            186
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          287..754
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(332,445,505,518,521,554,579)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          730..798
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..847
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001329222.2:543..3086"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS60817.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 mtrfridele prrpryrvpd vlvadppiar lsvsgrdens veltmaegpy kiiltarpfr
       61 ldlledrsll lsvnarglle fehqraprvs qgskdpaegd gaqpeetprd gdkpeetqgk
      121 aekdepgawe etfkthsdsk pygpmsvgld fslpgmehvy gipehadnlr lkvteggepy
      181 rlynldvfqy elynpmalyg svpvllahnp hrdlgifwln aaetwvdiss ntagktlfgk
      241 mmdylqgsge tpqtdvrwms etgiidvfll lgpsisdvfr qyasltgtqa lpplfslgyh
      301 qsrwnyrdea dvlevdqgfd dhnlpcdviw ldiehadgkr yftwdpsrfp qprtmlerla
      361 skrrklvaiv dphikvdsgy rvheelrnlg lyvktrdgsd yegwcwpgsa gypdftnptm
      421 rawwanmfsy dnyegsapnl fvwndmneps vfngpevtml kdaqhyggwe hrdvhniygl
      481 yvhmatadgl rqrsggmerp fvlaraffag sqrfgavwtg dntaewdhlk isipmclslg
      541 lvglsfcgad vggffknpep ellvrwyqmg ayqpffraha hldtgrrepw llpsqhndii
      601 rdalgqrysl lpfwytllyq ahregipvmr plwvqypqdv ttfniddqyl lgdallvhpv
      661 sdsgahgvqv ylpgqgevwy diqsyqkhhg pqtlylpvtl ssipvfqrgg tivprwmrvr
      721 rssecmkddp itlfvalspq gtaqgelfld dghtfnyqtr qefllrrfsf sgntlvsssa
      781 dpeghfetpi wiervviiga gkpaavvlqt kgspesrlsf qhdpetsvlv lrkpginvas
      841 dwsihlr
//
LOCUS       NP_001157030             227 aa            linear   PRI 20-NOV-2025
DEFINITION  prolactin precursor [Homo sapiens].
ACCESSION   NP_001157030
VERSION     NP_001157030.1
DBSOURCE    REFSEQ: accession NM_001163558.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Wu,T., Duan,Y., Jiang,J., Gu,T., Zhang,P. and Bi,Y.
  TITLE     A Century of Prolactin: Emerging Perspectives as a Metabolic
            Regulator
  JOURNAL   Diabetes Metab Res Rev 40 (6), e3836 (2024)
   PUBMED   39096246
  REMARK    GeneRIF: A Century of Prolactin: Emerging Perspectives as a
            Metabolic Regulator.
            Review article
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Bartos,H.B., Weise,L., Schock,A., Diez,S., Weiss,C.,
            Drommelschmidt,K., Mahnken,A.H., Hummler,H. and Muller,H.
  TITLE     Pronounced neonatal breast enlargement beyond the first week of
            life and its regression correlates with serum prolactin levels - a
            case series
  JOURNAL   J Pediatr Endocrinol Metab 37 (10), 916-923 (2024)
   PUBMED   39135519
  REMARK    GeneRIF: Pronounced neonatal breast enlargement beyond the first
            week of life and its regression correlates with serum prolactin
            levels - a case series.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Lin,W.W., Ou,G.Y., Dai,H.F. and Zhao,W.J.
  TITLE     Neuregulin 4 (Nrg4) cooperates with melatonin to regulate the PRL
            expression via ErbB4/Erk signaling pathway as a potential prolactin
            (PRL) regulator
  JOURNAL   J Cell Biochem 125 (5), e30551 (2024)
   PUBMED   38465779
  REMARK    GeneRIF: Neuregulin 4 (Nrg4) cooperates with melatonin to regulate
            the PRL expression via ErbB4/Erk signaling pathway as a potential
            prolactin (PRL) regulator.
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Miao,X., Fu,Z., Luo,X., Wang,J., Yuan,L., Zhao,S., Feng,Y.,
            Huang,S. and Xiao,S.
  TITLE     A study on the correlations of PRL levels with anxiety, depression,
            sleep, and self-efficacy in patients with prolactinoma
  JOURNAL   Front Endocrinol (Lausanne) 15, 1369729 (2024)
   PUBMED   38572480
  REMARK    GeneRIF: A study on the correlations of PRL levels with anxiety,
            depression, sleep, and self-efficacy in patients with prolactinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Szukiewicz,D.
  TITLE     Current Insights in Prolactin Signaling and Ovulatory Function
  JOURNAL   Int J Mol Sci 25 (4), 1976 (2024)
   PUBMED   38396659
  REMARK    GeneRIF: Current Insights in Prolactin Signaling and Ovulatory
            Function.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Peers,B., Nalda,A.M., Monget,P., Voz,M.L., Belayew,A. and
            Martial,J.A.
  TITLE     Binding of a 100-kDa ubiquitous factor to the human prolactin
            promoter is required for its basal and hormone-regulated activity
  JOURNAL   Eur J Biochem 210 (1), 53-58 (1992)
   PUBMED   1332868
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Maddox,P.R., Jones,D.L. and Mansel,R.E.
  TITLE     Bioactive and immunoactive prolactin levels after TRH-stimulation
            in the sera of normal women
  JOURNAL   Horm Metab Res 24 (4), 181-184 (1992)
   PUBMED   1601394
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Farquhar,M.G., Reid,J.J. and Daniell,L.W.
  TITLE     Intracellular transport and packaging of prolactin: a quantitative
            electron microscope autoradiographic study of mammotrophs
            dissociated from rat pituitaries
  JOURNAL   Endocrinology 102 (1), 296-311 (1978)
   PUBMED   743954
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Shome,B. and Parlow,A.F.
  TITLE     Human pituitary prolactin (hPRL): the entire linear amino acid
            sequence
  JOURNAL   J Clin Endocrinol Metab 45 (5), 1112-1115 (1977)
   PUBMED   925136
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Jacobs,J.W. and Niall,H.D.
  TITLE     High sensitivity automated sequence determination of polypeptides
  JOURNAL   J Biol Chem 250 (10), 3629-3636 (1975)
   PUBMED   1126929
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from GQ305133.1 and CD106243.1.
            
            Summary: This gene encodes the anterior pituitary hormone
            prolactin. This secreted hormone is a growth regulator for many
            tissues, including cells of the immune system. It may also play a
            role in cell survival by suppressing apoptosis, and it is essential
            for lactation. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Aug
            2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ305133.1, X54393.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..227
                     /product="prolactin precursor"
                     /note="decidual prolactin; growth hormone A1; prolactin
                     peptide; luteotropin; luteotropic hormone"
                     /calculated_mol_wt=22898
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2996
     mat_peptide     29..227
                     /product="Prolactin. /id=PRO_0000032916"
                     /note="propagated from UniProtKB/Swiss-Prot (P01236.1)"
                     /calculated_mol_wt=22898
     Region          29..227
                     /region_name="prolactin_like"
                     /note="Prolactin (PRL or PRL1), chorionic
                     somatomammotropin, and related pituitary gland hormones;
                     cd10288"
                     /db_xref="CDD:198438"
     Site            order(29..31,39..41,46,49..50,55,58..59,83..84,94,
                     100..101,150,153,156..157,204..205,208..209,211..213,
                     215..216,219,227)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198438"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            59
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, partial;
                     propagated from UniProtKB/Swiss-Prot (P01236.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01239; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15687336; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15687336; propagated from
                     UniProtKB/Swiss-Prot (P01236.1)"
     CDS             1..227
                     /gene="PRL"
                     /gene_synonym="GHA1; pPRL"
                     /coded_by="NM_001163558.3:174..857"
                     /db_xref="CCDS:CCDS4548.1"
                     /db_xref="GeneID:5617"
                     /db_xref="HGNC:HGNC:9445"
                     /db_xref="MIM:176760"
ORIGIN      
        1 mnikgspwkg slllllvsnl llcqsvaplp icpggaarcq vtlrdlfdra vvlshyihnl
       61 ssemfsefdk rythgrgfit kainschtss latpedkeqa qqmnqkdfls livsilrswn
      121 eplyhlvtev rgmqeapeai lskaveieeq tkrllegmel ivsqvhpetk eneiypvwsg
      181 lpslqmadee srlsayynll hclrrdshki dnylkllkcr iihnnnc
//
LOCUS       NP_938149                966 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 3 precursor [Homo sapiens].
ACCESSION   NP_938149
VERSION     NP_938149.2
DBSOURCE    REFSEQ: accession NM_198335.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 966)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 966)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 966)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 966)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 966)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 966)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 966)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF144074.1, BC065266.1 and
            AA618561.1.
            
            On Feb 28, 2006 this sequence version replaced NP_938149.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (3) encodes the longest isoform
            (3, also known as the alpha2 isoform).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.144538.1,
                                           SRR1660809.46754.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..966
                     /product="neutral alpha-glucosidase AB isoform 3
                     precursor"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=106141
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     Region          266..406
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            305
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          406..873
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(451,564,624,637,640,673,698)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          849..918
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..966
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_198335.4:15..2915"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS41656.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 maavaavaar rrrswaslvl aflgvclgit lavdrsnfkt ceessfckrq rsirpglspy
       61 ralldslqlg pdsltvhlih evtkvllvle lqglqknmtr frideleprr pryrvpdvlv
      121 adppiarlsv sgrdensvel tmaegpykii ltarpfrldl ledrslllsv nargllefeh
      181 qraprvsfsd kvnltlgsiw dkiknlfsrq gskdpaegdg aqpeetprdg dkpeetqgka
      241 ekdepgawee tfkthsdskp ygpmsvgldf slpgmehvyg ipehadnlrl kvteggepyr
      301 lynldvfqye lynpmalygs vpvllahnph rdlgifwlna aetwvdissn tagktlfgkm
      361 mdylqgsget pqtdvrwmse tgiidvflll gpsisdvfrq yasltgtqal pplfslgyhq
      421 srwnyrdead vlevdqgfdd hnlpcdviwl diehadgkry ftwdpsrfpq prtmlerlas
      481 krrklvaivd phikvdsgyr vheelrnlgl yvktrdgsdy egwcwpgsag ypdftnptmr
      541 awwanmfsyd nyegsapnlf vwndmnepsv fngpevtmlk daqhyggweh rdvhniygly
      601 vhmatadglr qrsggmerpf vlaraffags qrfgavwtgd ntaewdhlki sipmclslgl
      661 vglsfcgadv ggffknpepe llvrwyqmga yqpffrahah ldtgrrepwl lpsqhndiir
      721 dalgqrysll pfwytllyqa hregipvmrp lwvqypqdvt tfniddqyll gdallvhpvs
      781 dsgahgvqvy lpgqgevwyd iqsyqkhhgp qtlylpvtls sipvfqrggt ivprwmrvrr
      841 ssecmkddpi tlfvalspqg taqgelfldd ghtfnyqtrq efllrrfsfs gntlvsssad
      901 peghfetpiw iervviigag kpaavvlqtk gspesrlsfq hdpetsvlvl rkpginvasd
      961 wsihlr
//
LOCUS       NP_001317547             404 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger TRAF-type-containing protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001317547 XP_006716625
VERSION     NP_001317547.1
DBSOURCE    REFSEQ: accession NM_001330618.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Asif,M., Khayyat,A.I.A., Alawbathani,S., Abdullah,U., Sanner,A.,
            Georgomanolis,T., Haasters,J., Becker,K., Budde,B., Becker,C.,
            Thiele,H., Baig,S.M., Isidoro-Garcia,M., Winter,D., Pogoda,H.M.,
            Muhammad,S., Hammerschmidt,M., Kraft,F., Kurth,I., Martin,H.G.,
            Wagner,M., Nurnberg,P. and Hussain,M.S.
  TITLE     Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia
  JOURNAL   Genet Med 26 (7), 101143 (2024)
   PUBMED   38641995
  REMARK    GeneRIF: Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia.
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Desaki,R., Sawada,G., Okumura,H., Ikeda,R., Tanabe,K., Komatsu,H.,
            Mimori,K., Mori,M., Kita,Y., Uchikado,Y., Arigami,T., Uenosono,Y.,
            Owaki,T., Ishigami,S. and Natsugoe,S.
  TITLE     As a Novel Prognostic Marker, Cysteine/histidine-rich 1 (CYHR1) is
            a Therapeutic Target in Patients with Esophageal Squamous Cell
            Carcinoma
  JOURNAL   Ann Surg Oncol 24 (2), 586-593 (2017)
   PUBMED   26676980
  REMARK    GeneRIF: High CYHR1 expression is associated with Esophageal
            Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Menon,R.P., Strom,M. and Hughes,R.C.
  TITLE     Interaction of a novel cysteine and histidine-rich cytoplasmic
            protein with galectin-3 in a carbohydrate-independent manner
  JOURNAL   FEBS Lett 470 (3), 227-231 (2000)
   PUBMED   10745073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084125.9, BQ956567.1, BG751889.1 and BC004544.2.
            
            On Aug 30, 2016 this sequence version replaced XP_006716625.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.594290.1, BG751889.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000530374.6/ ENSP00000433769.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..404
                     /product="zinc finger TRAF-type-containing protein 1
                     isoform 1"
                     /note="cysteine and histidine rich protein; cysteine and
                     histidine-rich protein 1; cysteine/histidine-rich 1;
                     cysteine and histidine rich 1; Zinc finger
                     TRAF-type-containing protein 1; zinc finger TRAF-type
                     containing 1"
                     /calculated_mol_wt=43682
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DTL6.1)"
     Region          100..161
                     /region_name="RING-HC_CYHR1"
                     /note="RING finger, HC subclass, found in cysteine and
                     histidine-rich protein 1 (CYHR1) and similar proteins;
                     cd16505"
                     /db_xref="CDD:438168"
     Region          166..>227
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          249..404
                     /region_name="CYHR1_C"
                     /note="C-terminal domain of cysteine and histidine-rich
                     protein 1 and similar proteins; cd22861"
                     /db_xref="CDD:439370"
     CDS             1..404
                     /gene="ZFTRAF1"
                     /gene_synonym="CHRP; CYHR1"
                     /coded_by="NM_001330618.2:218..1432"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS83335.1"
                     /db_xref="GeneID:50626"
                     /db_xref="HGNC:HGNC:17806"
                     /db_xref="MIM:616635"
ORIGIN      
        1 msgaeeaggg gpaagpagsv pagvgvgvga gpgaaagqaa aaalgeaagp glpdeaglag
       61 arqlqlqeaa gdpdappkkr lraaeaaeaa aaaaaagsgk leerlysvlc ctvcldlpka
      121 svyqctnghl mcagcfihll adarlkeeqa tcpncrceis kslccrnlav ekavselpse
      181 cgfclrqfpr sllerhqkee cqdrvtqcky krigcpwhgp fheltvheaa cahptktgse
      241 lmeildgmdq shrkemqlyn sifsllsfek igytevqfrp yrtddfitrl yyetprftvl
      301 nqtwvlkarv ndsernpnls ckrtlsfqll lkskvtaple csflllkgpy ddvrispviy
      361 hfvftnesne tdyvplpiid svecnkllaa kninlrlflf qiqk
//
LOCUS       NP_003791                597 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-capping enzyme isoform a [Homo sapiens].
ACCESSION   NP_003791
VERSION     NP_003791.3
DBSOURCE    REFSEQ: accession NM_003800.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Lombardi,O., Varshney,D., Phillips,N.M. and Cowling,V.H.
  TITLE     c-Myc deregulation induces mRNA capping enzyme dependency
  JOURNAL   Oncotarget 7 (50), 82273-82288 (2016)
   PUBMED   27756891
  REMARK    GeneRIF: c-Myc deregulation induces mRNA capping enzyme dependency
            in tumor cells.
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Mukherjee,C., Bakthavachalu,B. and Schoenberg,D.R.
  TITLE     The cytoplasmic capping complex assembles on adapter protein nck1
            bound to the proline-rich C-terminus of Mammalian capping enzyme
  JOURNAL   PLoS Biol 12 (8), e1001933 (2014)
   PUBMED   25137142
  REMARK    GeneRIF: These results identify a new domain of CE that is specific
            to its function in cytoplasmic capping, and a new role for Nck1 in
            regulating gene expression through its role as the scaffold for
            assembly of the cytoplasmic capping complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Niikura,Y. and Mizumoto,K.
  TITLE     Cloning and characterization of three human cDNAs encoding mRNA
            (guanine-7-)-methyltransferase, an mRNA cap methylase
  JOURNAL   Biochem Biophys Res Commun 251 (1), 27-34 (1998)
   PUBMED   9790902
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Pillutla,R.C., Yue,Z., Maldonado,E. and Shatkin,A.J.
  TITLE     Recombinant human mRNA cap methyltransferase binds capping
            enzyme/RNA polymerase IIo complexes
  JOURNAL   J Biol Chem 273 (34), 21443-21446 (1998)
   PUBMED   9705270
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Yamada-Okabe,T., Doi,R., Shimmi,O., Arisawa,M. and Yamada-Okabe,H.
  TITLE     Isolation and characterization of a human cDNA for mRNA 5'-capping
            enzyme
  JOURNAL   Nucleic Acids Res 26 (7), 1700-1706 (1998)
   PUBMED   9512541
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Tsukamoto,T., Shibagaki,Y., Murakoshi,T., Suzuki,M., Nakamura,A.,
            Gotoh,H. and Mizumoto,K.
  TITLE     Cloning and characterization of two human cDNAs encoding the mRNA
            capping enzyme
  JOURNAL   Biochem Biophys Res Commun 243 (1), 101-108 (1998)
   PUBMED   9473487
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Yue,Z., Maldonado,E., Pillutla,R., Cho,H., Reinberg,D. and
            Shatkin,A.J.
  TITLE     Mammalian capping enzyme complements mutant Saccharomyces
            cerevisiae lacking mRNA guanylyltransferase and selectively binds
            the elongating form of RNA polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12898-12903 (1997)
   PUBMED   9371772
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP256840.1, AB009022.1, BX537450.1, BC019954.1, AI193199.1 and
            BP396964.1.
            
            On Mar 27, 2007 this sequence version replaced NP_003791.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1790820.1, BC019954.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369485.9/ ENSP00000358497.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..597
                     /product="mRNA-capping enzyme isoform a"
                     /EC_number="2.7.7.50"
                     /EC_number="3.6.1.74"
                     /note="mRNA-capping enzyme; HCAP1; mRNA
                     guanylyltransferase; mRNA 5'-triphosphate monophosphatase"
                     /calculated_mol_wt=68426
     Region          1..212
                     /region_name="TPase"
                     /note="propagated from UniProtKB/Swiss-Prot (O60942.1)"
     Region          9..175
                     /region_name="Mce1_N"
                     /note="N-terminal triphosphatase domain of mRNA capping
                     enzyme; cd17664"
                     /db_xref="CDD:350502"
     Region          181..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60942.1)"
     Region          229..597
                     /region_name="GTase"
                     /note="propagated from UniProtKB/Swiss-Prot (O60942.1)"
     Region          248..461
                     /region_name="Adenylation_mRNA_capping"
                     /note="Adenylation domain of GTP-dependent mRNA capping
                     enzymes; cd07895"
                     /db_xref="CDD:185706"
     Site            order(271..273,292,294,299,345,362,413,441,456,458,460)
                     /site_type="active"
                     /db_xref="CDD:185706"
     Site            order(290,358,378..379,381..383,385,409,412,415..416)
                     /site_type="active"
                     /note="CTD docking site [active]"
                     /db_xref="CDD:185706"
     Region          330..386
                     /region_name="Interaction with POLR2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60942.1)"
     Region          465..558
                     /region_name="mRNA_cap_C"
                     /note="mRNA capping enzyme, C-terminal domain; pfam03919"
                     /db_xref="CDD:461093"
     Region          570..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60942.1)"
     CDS             1..597
                     /gene="RNGTT"
                     /gene_synonym="CAP1A; hCAP; HCE; HCE1"
                     /coded_by="NM_003800.5:210..2003"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5017.1"
                     /db_xref="GeneID:8732"
                     /db_xref="HGNC:HGNC:10073"
                     /db_xref="MIM:603512"
ORIGIN      
        1 mahnkipprw lncprrgqpv agrflplktm lgprydsqva eenrfhpsml snylkslkvk
       61 mgllvdltnt srfydrndie kegikyiklq ckghgecptt entetfirlc erfnernppe
      121 ligvhcthgf nrtgflicaf lvekmdwsie aavatfaqar ppgiykgdyl kelfrrygdi
      181 eeappppllp dwcfeddede dededgkkes epgssasfgk rrkerlklga iflegvtvkg
      241 vtqvttqpkl gevqqkchqf cgwegsgfpg aqpvsmdkqn iklldlkpyk vswkadgtry
      301 mmlidgtnev fmidrdnsvf hvsnlefpfr kdlrmhlsnt lldgemiidr vngqavpryl
      361 iydiikfnsq pvgdcdfnvr lqciereiis prhekmktgl idktqepfsv rnkpffdict
      421 srkllegnfa kevshemdgl ifqptgkykp grcddilkwk ppslnsvdfr lkitrmggeg
      481 llpqnvglly vggyerpfaq ikvtkelkqy dnkiieckfe nnswvfmrqr tdksfpnayn
      541 tamavcnsis npvtkemlfe fidrctaasq gqkrkhhldp dtelmppppp krprplt
//
LOCUS       NP_938148                944 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 2 precursor [Homo sapiens].
ACCESSION   NP_938148
VERSION     NP_938148.1
DBSOURCE    REFSEQ: accession NM_198334.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 944)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 944)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 944)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 944)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 944)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 944)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 944)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK026997.1, AK314370.1 and
            D42041.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (2) lacks an in-frame exon,
            compared to variant 3. The resulting isoform (2, also known as the
            alpha1 isoform) lacks an internal segment, compared to isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU794613.1, D42041.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356638.8/ ENSP00000349053.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..944
                     /product="neutral alpha-glucosidase AB isoform 2
                     precursor"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=103577
     sig_peptide     1..32
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3315
     mat_peptide     29..944
                     /product="Neutral alpha-glucosidase AB.
                     /id=PRO_0000018571"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14697.3)"
                     /calculated_mol_wt=103976
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14697.3)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:3881423; propagated from
                     UniProtKB/Swiss-Prot (Q14697.3)"
     Region          181..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14697.3)"
     Region          244..384
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            283
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          384..851
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(429,542,602,615,618,651,676)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          827..896
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..944
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_198334.3:15..2849"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS8026.1"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 maavaavaar rrrswaslvl aflgvclgit lavdrsnfkt ceessfckrq rsirpglspy
       61 ralldslqlg pdsltvhlih evtkvllvle lqglqknmtr frideleprr pryrvpdvlv
      121 adppiarlsv sgrdensvel tmaegpykii ltarpfrldl ledrslllsv nargllefeh
      181 qraprvsqgs kdpaegdgaq peetprdgdk peetqgkaek depgaweetf kthsdskpyg
      241 pmsvgldfsl pgmehvygip ehadnlrlkv teggepyrly nldvfqyely npmalygsvp
      301 vllahnphrd lgifwlnaae twvdissnta gktlfgkmmd ylqgsgetpq tdvrwmsetg
      361 iidvflllgp sisdvfrqya sltgtqalpp lfslgyhqsr wnyrdeadvl evdqgfddhn
      421 lpcdviwldi ehadgkryft wdpsrfpqpr tmlerlaskr rklvaivdph ikvdsgyrvh
      481 eelrnlglyv ktrdgsdyeg wcwpgsagyp dftnptmraw wanmfsydny egsapnlfvw
      541 ndmnepsvfn gpevtmlkda qhyggwehrd vhniyglyvh matadglrqr sggmerpfvl
      601 araffagsqr fgavwtgdnt aewdhlkisi pmclslglvg lsfcgadvgg ffknpepell
      661 vrwyqmgayq pffrahahld tgrrepwllp sqhndiirda lgqrysllpf wytllyqahr
      721 egipvmrplw vqypqdvttf niddqyllgd allvhpvsds gahgvqvylp gqgevwydiq
      781 syqkhhgpqt lylpvtlssi pvfqrggtiv prwmrvrrss ecmkddpitl fvalspqgta
      841 qgelflddgh tfnyqtrqef llrrfsfsgn tlvsssadpe ghfetpiwie rvviigagkp
      901 aavvlqtkgs pesrlsfqhd petsvlvlrk pginvasdws ihlr
//
LOCUS       NP_001394041              93 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform n [Homo sapiens].
ACCESSION   NP_001394041
VERSION     NP_001394041.1
DBSOURCE    REFSEQ: accession NM_001407112.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 93)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 93)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.152247.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..93
                     /product="protein max isoform n"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10028
     CDS             1..93
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407112.1:314..595"
                     /note="isoform n is encoded by transcript variant 30"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mccgkaradq vlcswgihfs sslmedaskr kfralekars saqlqtnyps sdnslytnak
       61 gstisafdgg sdsssesepe epqsrkklrm eas
//
LOCUS       NP_525021               1543 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family A member 10 [Homo sapiens].
ACCESSION   NP_525021
VERSION     NP_525021.3
DBSOURCE    REFSEQ: accession NM_080282.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1543)
  AUTHORS   Chen,H., Li,L., Qin,P., Xiong,H., Chen,R., Zhang,M. and Jiang,Q.
  TITLE     A 4-gene signature predicts prognosis of uterine serous carcinoma
  JOURNAL   BMC Cancer 21 (1), 154 (2021)
   PUBMED   33579221
  REMARK    GeneRIF: A 4-gene signature predicts prognosis of uterine serous
            carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1543)
  AUTHORS   Baecklund,F., Foo,J.N., Bracci,P., Darabi,H., Karlsson,R.,
            Hjalgrim,H., Rosenquist,R., Adami,H.O., Glimelius,B., Melbye,M.,
            Conde,L., Liu,J., Humphreys,K., Skibola,C.F. and Smedby,K.E.
  TITLE     A comprehensive evaluation of the role of genetic variation in
            follicular lymphoma survival
  JOURNAL   BMC Med Genet 15, 113 (2014)
   PUBMED   25294155
  REMARK    GeneRIF: Results suggest a possible role for multidrug resistance
            genes ABCA10 and ABCA6 in follicular lymphoma survival and add to
            the evidence that genetic variation in CD46 and IL8 may have
            prognostic implications follicular lymphoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1543)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   4  (residues 1 to 1543)
  AUTHORS   Wenzel,J.J., Kaminski,W.E., Piehler,A., Heimerl,S., Langmann,T. and
            Schmitz,G.
  TITLE     ABCA10, a novel cholesterol-regulated ABCA6-like ABC transporter
  JOURNAL   Biochem Biophys Res Commun 306 (4), 1089-1098 (2003)
   PUBMED   12821155
  REMARK    GeneRIF: ABCA10 is a novel member of the group of ABCA6-like
            transporters involved in macrophage lipid homeostasis
REFERENCE   5  (residues 1 to 1543)
  AUTHORS   Dean,M., Rzhetsky,A. and Allikmets,R.
  TITLE     The human ATP-binding cassette (ABC) transporter superfamily
  JOURNAL   Genome Res 11 (7), 1156-1166 (2001)
   PUBMED   11435397
  REMARK    Review article
REFERENCE   6  (residues 1 to 1543)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005495.2, AY247065.1 and
            C16161.1.
            
            On Jul 25, 2007 this sequence version replaced NP_525021.2.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            and White). This encoded protein is a member of the ABC1 subfamily.
            Members of the ABC1 subfamily comprise the only major ABC subfamily
            found exclusively in multicellular eukaryotes. This gene is
            clustered among 4 other ABC1 family members on 17q24, but neither
            the substrate nor the function of this gene is known. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY247065.1, AY028900.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.3"
     Protein         1..1543
                     /product="ATP-binding cassette sub-family A member 10"
                     /EC_number="7.6.2.-"
                     /note="ATP-binding cassette A10; ATP-binding cassette,
                     sub-family A (ABC1), member 10"
                     /calculated_mol_wt=175660
     Region          <37..1520
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            210..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            310..330
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            774..794
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            890..910
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            926..946
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            985..1005
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1014..1034
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1046..1066
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1073..1093
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Site            1113..1133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     Region          1153..1177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WWZ4.3)"
     CDS             1..1543
                     /gene="ABCA10"
                     /gene_synonym="EST698739"
                     /coded_by="NM_080282.4:913..5544"
                     /db_xref="CCDS:CCDS11684.1"
                     /db_xref="GeneID:10349"
                     /db_xref="HGNC:HGNC:30"
                     /db_xref="MIM:612508"
ORIGIN      
        1 mnkmalasfm kgrtvigtpd eetmdielpk kyhemvgvif sdtfsyrlkf nwgyripvik
       61 ehseytehcw amhgeifcyl akywlkgfva fqaainaaii evttnhsvme eltsviginm
      121 kippfiskge imnewfhftc lvsfssfiyf aslnvarerg kfkklmtvmg lresafwlsw
      181 gltyicfifi msifmalvit sipivfhtgf mviftlysly glslialafl msvlirkpml
      241 aglagflftv fwgclgftvl yrqlplslgw vlsllspfaf tagmaqithl dnylsgvifp
      301 dpsgdsykmi atffilafdt lfyliftlyf ervlpdkdgh gdsplfflks sfwskhqnth
      361 heifeneinp ehssddsfep vspefhgkea irirnvikey ngktgkveal qgiffdiyeg
      421 qitailghng agkstllnil sglsvstegs atiyntqlse itdmeeirkn igfcpqfnfq
      481 fdfltvrenl rvfakikgiq pkeveqevkr iimeldmqsi qdiiakklsg gqkrkltlgi
      541 ailgdpqvll ldeptagldp fsrhrvwsll kehkvdrlil fstqfmdead iladrkvfls
      601 ngklkcagss lflkrkwgig yhlslhrnem cdtekitsli kqhipdaklt teseeklvys
      661 lplektnkfp dlysdldkcs dqgirnyavs vtslnevfln legksaidep dfdigkqeki
      721 hvtrntgdes emeqvlcslp etrkavssaa lwrrqiyava tlrflklrre rrallclllv
      781 lgiafipiil ekimykvtre thcwefspsm yflsleqipk tpltsllivn ntgsniedlv
      841 hslkcqdivl eiddfrnrng sddpsyngai ivsgdqkdyr fsvacntkkl ncfpvlmgiv
      901 snalmgifnf teliqmests fsrddivldl gfidgsifll litncvspfi gmssisdykk
      961 nvqsqlwisg lwpsaywcgq alvdiplyfl ilfsihliyy fiflgfqlsw elmfvlvvci
     1021 igcavslifl tyvlsfifrk wrknngfwsf gffiilicvs timvstqyek lnlilcmifi
     1081 psftllgyvm lliqldfmrn ldsldnrine vnktillttl ipylqsvifl fvirclemky
     1141 gneimnkdpv frisprsret hpnpeepeee dedvqaervq aanaltapnl eeepvitasc
     1201 lhkeyyetkk scfstrkkki airnvsfcvk kgevlgllgh ngagkstsik mitgctkpta
     1261 gvvvlqgsra svrqqhdnsl kflgycpqen slwpkltmke hlelyaavkg lgkedaalsi
     1321 srlvealklq eqlkapvktl segikrklcf vlsilgnpsv vlldepftgm dpegqqqmwq
     1381 ilqatvknke rgtlltthym seaeavcdrm ammvsgtlrc igsiqhlknk fgrdylleik
     1441 mkeptqveal hteilklfpq aawqeryssl mayklpvedv hplsraffkl eamkqtfnle
     1501 eyslsqatle qvflelckeq elgnvddkid ttvewkllpq edp
//
LOCUS       NP_001394978             203 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger TRAF-type-containing protein 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001394978
VERSION     NP_001394978.1
DBSOURCE    REFSEQ: accession NM_001408049.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Asif,M., Khayyat,A.I.A., Alawbathani,S., Abdullah,U., Sanner,A.,
            Georgomanolis,T., Haasters,J., Becker,K., Budde,B., Becker,C.,
            Thiele,H., Baig,S.M., Isidoro-Garcia,M., Winter,D., Pogoda,H.M.,
            Muhammad,S., Hammerschmidt,M., Kraft,F., Kurth,I., Martin,H.G.,
            Wagner,M., Nurnberg,P. and Hussain,M.S.
  TITLE     Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia
  JOURNAL   Genet Med 26 (7), 101143 (2024)
   PUBMED   38641995
  REMARK    GeneRIF: Biallelic loss-of-function variants of ZFTRAF1 cause
            neurodevelopmental disorder with microcephaly and hypotonia.
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Desaki,R., Sawada,G., Okumura,H., Ikeda,R., Tanabe,K., Komatsu,H.,
            Mimori,K., Mori,M., Kita,Y., Uchikado,Y., Arigami,T., Uenosono,Y.,
            Owaki,T., Ishigami,S. and Natsugoe,S.
  TITLE     As a Novel Prognostic Marker, Cysteine/histidine-rich 1 (CYHR1) is
            a Therapeutic Target in Patients with Esophageal Squamous Cell
            Carcinoma
  JOURNAL   Ann Surg Oncol 24 (2), 586-593 (2017)
   PUBMED   26676980
  REMARK    GeneRIF: High CYHR1 expression is associated with Esophageal
            Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Menon,R.P., Strom,M. and Hughes,R.C.
  TITLE     Interaction of a novel cysteine and histidine-rich cytoplasmic
            protein with galectin-3 in a carbohydrate-independent manner
  JOURNAL   FEBS Lett 470 (3), 227-231 (2000)
   PUBMED   10745073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084125.9.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.32964.1,
                                           SRR14038197.1409446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..203
                     /product="zinc finger TRAF-type-containing protein 1
                     isoform 4"
                     /note="cysteine and histidine rich protein; cysteine and
                     histidine-rich protein 1; cysteine/histidine-rich 1;
                     cysteine and histidine rich 1; Zinc finger
                     TRAF-type-containing protein 1; zinc finger TRAF-type
                     containing 1"
                     /calculated_mol_wt=22635
     Region          <1..31
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          36..>97
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          119..>144
                     /region_name="CYHR1_C"
                     /note="C-terminal domain of cysteine and histidine-rich
                     protein 1 and similar proteins; cd22861"
                     /db_xref="CDD:439370"
     CDS             1..203
                     /gene="ZFTRAF1"
                     /gene_synonym="CHRP; CYHR1"
                     /coded_by="NM_001408049.1:57..668"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:50626"
                     /db_xref="HGNC:HGNC:17806"
                     /db_xref="MIM:616635"
ORIGIN      
        1 mcagcfihll adarlkeeqa tcpncrceis kslccrnlav ekavselpse cgfclrqfpr
       61 sllerhqkee cqdrvtqcky krigcpwhgp fheltvheaa cahptktgse lmeildgmdq
      121 shrkemqlyn sifsllsfek igytgeaprr llhatqvwvg glaarslgaa gsghwaltap
      181 dsraldklpv drwtprsrrq agd
//
LOCUS       NP_072053                202 aa            linear   PRI 20-NOV-2025
DEFINITION  somatotropin isoform 2 precursor [Homo sapiens].
ACCESSION   NP_072053
VERSION     NP_072053.1
DBSOURCE    REFSEQ: accession NM_022559.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Huang,X., Chen,H., Shangguan,H., Wu,W., Ai,Z., Chen,Z. and Chen,R.
  TITLE     The clinical and genetic aspects of six individuals with GH1
            variants and isolated growth hormone deficiency type II
  JOURNAL   Front Endocrinol (Lausanne) 15, 1363050 (2024)
   PUBMED   39435354
  REMARK    GeneRIF: The clinical and genetic aspects of six individuals with
            GH1 variants and isolated growth hormone deficiency type II.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Maimaituxun,G., Amano,T., Kenny,G.P., Mundel,T., Kajiki,M.,
            Tagawa,K., Katagiri,A., Tanabe,Y., Watanabe,K., Nishiyasu,T.,
            Kondo,N. and Fujii,N.
  TITLE     GH and IGF-1 in skin interstitial fluid and blood are associated
            with heat loss responses in exercising young adults
  JOURNAL   Eur J Appl Physiol 124 (8), 2285-2301 (2024)
   PUBMED   38446190
  REMARK    GeneRIF: GH and IGF-1 in skin interstitial fluid and blood are
            associated with heat loss responses in exercising young adults.
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Zhou,Z., Luo,Y., Li,K., Zhong,S., Zhu,Y., Yang,H., Wang,L.,
            Chen,S., Duan,L., Gong,F., Gong,G., Zhu,H. and Pan,H.
  TITLE     Brain white matter alterations in young adult male patients with
            childhood-onset growth hormone deficiency: a diffusion tensor
            imaging study
  JOURNAL   Endocrine 83 (3), 724-732 (2024)
   PUBMED   37936007
  REMARK    GeneRIF: Brain white matter alterations in young adult male
            patients with childhood-onset growth hormone deficiency: a
            diffusion tensor imaging study.
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Herman,R., Janez,A., Mikhailidis,D.P., Poredos,P., Blinc,A.,
            Sabovic,M., Studen,K.B., Schernthaner,G.H., Anagnostis,P.,
            Antignani,P.L. and Jensterle,M.
  TITLE     Growth Hormone, Atherosclerosis and Peripheral Arterial Disease:
            Exploring the Spectrum from Acromegaly to Growth Hormone Deficiency
  JOURNAL   Curr Vasc Pharmacol 22 (1), 28-35 (2024)
   PUBMED   37962050
  REMARK    GeneRIF: Growth Hormone, Atherosclerosis and Peripheral Arterial
            Disease: Exploring the Spectrum from Acromegaly to Growth Hormone
            Deficiency.
            Review article
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Fedorczak,A., Lewinski,A. and Stawerska,R.
  TITLE     Involvement of Sirtuin 1 in the Growth Hormone/Insulin-like Growth
            Factor 1 Signal Transduction and Its Impact on Growth Processes in
            Children
  JOURNAL   Int J Mol Sci 24 (20), 15406 (2023)
   PUBMED   37895086
  REMARK    GeneRIF: Involvement of Sirtuin 1 in the Growth
            Hormone/Insulin-like Growth Factor 1 Signal Transduction and Its
            Impact on Growth Processes in Children.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Akinci,A., Kanaka,C., Eble,A., Akar,N., Vidinlisan,S. and
            Mullis,P.E.
  TITLE     Isolated growth hormone (GH) deficiency type IA associated with a
            45-kilobase gene deletion within the human GH gene cluster
  JOURNAL   J Clin Endocrinol Metab 75 (2), 437-441 (1992)
   PUBMED   1322425
REFERENCE   7  (residues 1 to 202)
  AUTHORS   Estes,P.A., Cooke,N.E. and Liebhaber,S.A.
  TITLE     A native RNA secondary structure controls alternative splice-site
            selection and generates two human growth hormone isoforms
  JOURNAL   J Biol Chem 267 (21), 14902-14908 (1992)
   PUBMED   1634529
REFERENCE   8  (residues 1 to 202)
  AUTHORS   de Vos,A.M., Ultsch,M. and Kossiakoff,A.A.
  TITLE     Human growth hormone and extracellular domain of its receptor:
            crystal structure of the complex
  JOURNAL   Science 255 (5042), 306-312 (1992)
   PUBMED   1549776
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Roskam,W.G. and Rougeon,F.
  TITLE     Molecular cloning and nucleotide sequence of the human growth
            hormone structural gene
  JOURNAL   Nucleic Acids Res 7 (2), 305-320 (1979)
   PUBMED   386281
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Martial,J.A., Hallewell,R.A., Baxter,J.D. and Goodman,H.M.
  TITLE     Human growth hormone: complementary DNA cloning and expression in
            bacteria
  JOURNAL   Science 205 (4406), 602-607 (1979)
   PUBMED   377496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AV749353.1 and BC062475.1.
            
            Summary: The protein encoded by this gene is a member of the
            somatotropin/prolactin family of hormones which play an important
            role in growth control. The gene, along with four other related
            genes, is located at the growth hormone locus on chromosome 17
            where they are interspersed in the same transcriptional
            orientation; an arrangement which is thought to have evolved by a
            series of gene duplications. The five genes share a remarkably high
            degree of sequence identity. Alternative splicing generates
            additional isoforms of each of the five growth hormones, leading to
            further diversity and potential for specialization. This particular
            family member is expressed in the pituitary but not in placental
            tissue as is the case for the other four genes in the growth
            hormone locus. Mutations in or deletions of the gene lead to growth
            hormone deficiency and short stature. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            The encoded isoform (b) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062475.1, CD106929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2151358,
                                           SAMEA2153307 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..202
                     /product="somatotropin isoform 2 precursor"
                     /note="pituitary growth hormone; somatotropin; growth
                     hormone B5"
                     /calculated_mol_wt=20274
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2736
     Region          35..200
                     /region_name="somatotropin_like"
                     /note="Somatotropin or growth hormone (GH), placental
                     lactogen, and related pituitary gland hormones; cd10285"
                     /db_xref="CDD:198435"
     Site            order(35,38,41..42,44,47..48,51,58,60,72..75,78..79,127,
                     130..131,134,175,178..179,182..183,185..186,189..190,193,
                     200)
                     /site_type="other"
                     /note="receptor binding interface [polypeptide binding]"
                     /db_xref="CDD:198435"
     CDS             1..202
                     /gene="GH1"
                     /gene_synonym="GH; GH-N; GHB5; GHN; hGH; hGH-N; IGHD1A;
                     IGHD1B; IGHD2"
                     /coded_by="NM_022559.4:64..672"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS45760.1"
                     /db_xref="GeneID:2688"
                     /db_xref="HGNC:HGNC:4261"
                     /db_xref="MIM:139250"
ORIGIN      
        1 matgsrtsll lafgllclpw lqegsafpti plsrlfdnam lrahrlhqla fdtyqefnpq
       61 tslcfsesip tpsnreetqq ksnlellris llliqswlep vqflrsvfan slvygasdsn
      121 vydllkdlee giqtlmgrle dgsprtgqif kqtyskfdtn shnddallkn ygllycfrkd
      181 mdkvetflri vqcrsvegsc gf
//
LOCUS       NP_001309277             835 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex exonuclease RRP44 isoform c [Homo sapiens].
ACCESSION   NP_001309277 XP_006719841
VERSION     NP_001309277.1
DBSOURCE    REFSEQ: accession NM_001322348.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Favasuli,V.K., Ronchetti,D., Silvestris,I., Puccio,N., Fabbiano,G.,
            Traini,V., Todoerti,K., Erratico,S., Ciarrocchi,A., Fragliasso,V.,
            Giannandrea,D., Tumiatti,F., Chiaramonte,R., Torrente,Y.,
            Finelli,P., Morelli,E., Munshi,N.C., Bolli,N., Neri,A. and
            Taiana,E.
  TITLE     DIS3 depletion in multiple myeloma causes extensive perturbation in
            cell cycle progression and centrosome amplification
  JOURNAL   Haematologica 109 (1), 231-244 (2024)
   PUBMED   37439377
  REMARK    GeneRIF: DIS3 depletion in multiple myeloma causes extensive
            perturbation in cell cycle progression and centrosome
            amplification.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Johnstone,E.B., Gorsi,B., Coelho,E., Moore,B., Farr,A.M.,
            Cooper,A.R., Mardis,E.R., Rajkovic,A., Chow,C.Y., Yandell,M. and
            Welt,C.K.
  TITLE     DIS3 Variants are Associated With Primary Ovarian Insufficiency:
            Importance of Transcription/Translation in Oogenesis
  JOURNAL   J Clin Endocrinol Metab 108 (9), 2330-2335 (2023)
   PUBMED   36869713
  REMARK    GeneRIF: DIS3 Variants are Associated With Primary Ovarian
            Insufficiency: Importance of Transcription/Translation in
            Oogenesis.
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Ohguchi,Y. and Ohguchi,H.
  TITLE     DIS3: The Enigmatic Gene in Multiple Myeloma
  JOURNAL   Int J Mol Sci 24 (4), 4079 (2023)
   PUBMED   36835493
  REMARK    GeneRIF: DIS3: The Enigmatic Gene in Multiple Myeloma.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Gritti,I., Basso,V., Rinchai,D., Corigliano,F., Pivetti,S.,
            Gaviraghi,M., Rosano,D., Mazza,D., Barozzi,S., Roncador,M.,
            Parmigiani,G., Legube,G., Parazzoli,D., Cittaro,D., Bedognetti,D.,
            Mondino,A., Segalla,S. and Tonon,G.
  TITLE     Loss of ribonuclease DIS3 hampers genome integrity in myeloma by
            disrupting DNA:RNA hybrid metabolism
  JOURNAL   EMBO J 41 (22), e108040 (2022)
   PUBMED   36215697
  REMARK    GeneRIF: Loss of ribonuclease DIS3 hampers genome integrity in
            myeloma by disrupting DNA:RNA hybrid metabolism.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Fujiwara,N., Shigemoto,M., Hirayama,M., Fujita,K.I., Seno,S.,
            Matsuda,H., Nagahama,M. and Masuda,S.
  TITLE     MPP6 stimulates both RRP6 and DIS3 to degrade a specified subset of
            MTR4-sensitive substrates in the human nucleus
  JOURNAL   Nucleic Acids Res 50 (15), 8779-8806 (2022)
   PUBMED   35902094
  REMARK    GeneRIF: MPP6 stimulates both RRP6 and DIS3 to degrade a specified
            subset of MTR4-sensitive substrates in the human nucleus.
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Rozenblum,E., Vahteristo,P., Sandberg,T., Bergthorsson,J.T.,
            Syrjakoski,K., Weaver,D., Haraldsson,K., Johannsdottir,H.K.,
            Vehmanen,P., Nigam,S., Golberger,N., Robbins,C., Pak,E., Dutra,A.,
            Gillander,E., Stephan,D.A., Bailey-Wilson,J., Juo,S.H., Kainu,T.,
            Arason,A., Barkardottir,R.B., Nevanlinna,H., Borg,A. and
            Kallioniemi,O.P.
  TITLE     A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer
            development: identification and characterization of candidate genes
  JOURNAL   Hum Genet 110 (2), 111-121 (2002)
   PUBMED   11935316
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Shiomi,T., Fukushima,K., Suzuki,N., Nakashima,N., Noguchi,E. and
            Nishimoto,T.
  TITLE     Human dis3p, which binds to either GTP- or GDP-Ran, complements
            Saccharomyces cerevisiae dis3
  JOURNAL   J Biochem 123 (5), 883-890 (1998)
   PUBMED   9562621
  REMARK    GeneRIF: Dis3p is identical to Rrp44p, which comprises the exosome
            involved in ribosomal RNA processing. Similar to S. cerevisiae
            Dis3p, human Dis3p enhanced RCC1-stimulated nucleotide release from
            Ran, in a dose-dependent manner, and bound to GTP- or GDP-Ran.
            GeneRIF: S. cerevisiae Dis3p is identical to Rrp44p, which
            comprises the exosome involved in ribosomal RNA processing, S.
            cerevisiae Dis3p was found to be localized in the nucleolus.
            Erratum:[J Biochem (Tokyo) 1998 Jul;124(1):250]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL391384.18 and AL138695.13.
            
            On Apr 11, 2016 this sequence version replaced XP_006719841.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2100339.1,
                                           SRR14038193.1359177.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q21.33"
     Protein         1..835
                     /product="exosome complex exonuclease RRP44 isoform c"
                     /note="mitotic control protein dis3 homolog; exosome
                     component 11; exosome complex exonuclease RRP44; DIS3
                     exosome endoribonuclease and 3''-5'' exoribonuclease; DIS3
                     mitotic control homolog; ribosomal RNA-processing protein
                     44; DIS3 homolog, exosome endoribonuclease and 3'-5'
                     exoribonuclease"
                     /calculated_mol_wt=95169
     Region          <6..74
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          83..806
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     CDS             1..835
                     /gene="DIS3"
                     /gene_synonym="2810028N01Rik; dis3p; EXOSC11; KIAA1008;
                     RRP44"
                     /coded_by="NM_001322348.2:280..2787"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:22894"
                     /db_xref="HGNC:HGNC:20604"
                     /db_xref="MIM:607533"
ORIGIN      
        1 mcyctretyv eqeqgenand rndrairvaa kwynehlkkm sadnqlqvif itndrrnkek
       61 aieegipaft ceeyvkslta npelidrlac lseegneies gkiifsehlp lsklqqgiks
      121 gtylqgtfra srenyleatv wihgdneenk eiilqglkhl nravhediva vellpksqwv
      181 apssvvlhde gqneedveke eetermlkta vsekmlkptg rvvgiikrnw rpycgmlsks
      241 dikesrrhlf tpadkripri rietrqastl egrriivaid gwprnsrypn ghfvrnlgdv
      301 geketetevl llehdvphqp fsqavlsflp kmpwsitekd mknredlrhl cicsvdppgc
      361 tdiddalhcr elengnlevg vhiadvshfi rpgnaldqes arrgttvylc ekridmvpel
      421 lssnlcslkc dvdrlafsci wemnhnaeil ktkftksvin skasltyaea qlridsanmn
      481 ddittslrgl nklakilkkr riekgaltls spevrfhmds ethdpidlqt kelretnsmv
      541 eefmllanis vakkiheefs ehallrkhpa pppsnyeilv kaarsrnlei ktdtakslae
      601 sldqaesptf pylntllril atrcmmqavy fcsgmdndfh hyglaspiyt hftspirrya
      661 dvivhrllav aigadctype ltdkhkladi cknlnfrhkm aqyaqrasva fhtqlffksk
      721 givseeayil fvrknaivvl ipkyglegtv ffeekdkpnp qliyddeips lkiedtvfhv
      781 fdkvkvkiml dssnlqhqki rmslvepqip gisiptdtsn mdlngpkkkk mklgk
//
LOCUS       NP_001316154             703 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral alpha-glucosidase AB isoform 7 [Homo sapiens].
ACCESSION   NP_001316154 XP_016872903
VERSION     NP_001316154.1
DBSOURCE    REFSEQ: accession NM_001329225.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Xue,X., Wu,X., Liu,L., Liu,L. and Zhu,F.
  TITLE     ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by
            Decreasing GANAB in Recent-Onset Schizophrenia
  JOURNAL   Viruses 15 (6), 1298 (2023)
   PUBMED   37376599
  REMARK    GeneRIF: ERVW-1 Activates ATF6-Mediated Unfolded Protein Response
            by Decreasing GANAB in Recent-Onset Schizophrenia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Lin,Q., Pei,L., Zhao,Z., Zhuang,X. and Qin,H.
  TITLE     Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is a novel
            prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma
  JOURNAL   BMC Cancer 22 (1), 817 (2022)
   PUBMED   35879690
  REMARK    GeneRIF: Glycoprotein alpha-Subunit of Glucosidase II (GIIalpha) is
            a novel prognostic biomarker correlated with unfavorable outcome of
            urothelial carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Lv,D., Chen,J., Kang,Y., Luo,M., Chen,H., Cui,B., Wang,L., Wang,J.,
            Zhou,X., Feng,Y., Huang,L. and Zhang,P.
  TITLE     Protein Kinase D3 Promotes the Reconstruction of OSCC Immune Escape
            Niche Via Regulating MHC-I and Immune Inhibit Molecules Expression
  JOURNAL   J Immunother 44 (9), 339-347 (2021)
   PUBMED   34545012
  REMARK    GeneRIF: Protein Kinase D3 Promotes the Reconstruction of OSCC
            Immune Escape Niche Via Regulating MHC-I and Immune Inhibit
            Molecules Expression.
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Cui,B., Chen,J., Luo,M., Liu,Y., Chen,H., Lu,D., Wang,L., Kang,Y.,
            Feng,Y., Huang,L. and Zhang,P.
  TITLE     PKD3 promotes metastasis and growth of oral squamous cell carcinoma
            through positive feedback regulation with PD-L1 and activation of
            ERK-STAT1/3-EMT signalling
  JOURNAL   Int J Oral Sci 13 (1), 8 (2021)
   PUBMED   33692335
  REMARK    GeneRIF: PKD3 promotes metastasis and growth of oral squamous cell
            carcinoma through positive feedback regulation with PD-L1 and
            activation of ERK-STAT1/3-EMT signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 703)
  AUTHORS   van de Laarschot,L.F.M., Te Morsche,R.H.M., Hoischen,A.,
            Venselaar,H., Roelofs,H.M., Cnossen,W.R., Banales,J.M., Roepman,R.
            and Drenth,J.P.H.
  TITLE     Novel GANAB variants associated with polycystic liver disease
  JOURNAL   Orphanet J Rare Dis 15 (1), 302 (2020)
   PUBMED   33097077
  REMARK    GeneRIF: Novel GANAB variants associated with polycystic liver
            disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Arendt,C.W. and Ostergaard,H.L.
  TITLE     Identification of the CD45-associated 116-kDa and 80-kDa proteins
            as the alpha- and beta-subunits of alpha-glucosidase II
  JOURNAL   J Biol Chem 272 (20), 13117-13125 (1997)
   PUBMED   9148925
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Trombetta,E.S., Simons,J.F. and Helenius,A.
  TITLE     Endoplasmic reticulum glucosidase II is composed of a catalytic
            subunit, conserved from yeast to mammals, and a tightly bound
            noncatalytic HDEL-containing subunit
  JOURNAL   J Biol Chem 271 (44), 27509-27516 (1996)
   PUBMED   8910335
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Harris,P.C. and Torres,V.E.
  TITLE     Polycystic Kidney Disease, Autosomal Dominant
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301424
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Martiniuk,F., Ellenbogen,A. and Hirschhorn,R.
  TITLE     Identity of neutral alpha-glucosidase AB and the glycoprotein
            processing enzyme glucosidase II. Biochemical and genetic studies
  JOURNAL   J Biol Chem 260 (2), 1238-1242 (1985)
   PUBMED   3881423
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Martiniuk,F., Smith,M., Ellenbogen,A., Desnick,R.J., Astrin,K.,
            Mitra,J. and Hirschhorn,R.
  TITLE     Assignment of the gene for neutral alpha-glucosidase AB to
            chromosome 11
  JOURNAL   Cytogenet Cell Genet 35 (2), 110-116 (1983)
   PUBMED   6342981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6 and EU794613.1.
            
            On Jul 8, 2016 this sequence version replaced XP_016872903.1.
            
            Summary: This gene encodes the alpha subunit of glucosidase II and
            a member of the glycosyl hydrolase 31 family of proteins. The
            heterodimeric enzyme glucosidase II plays a role in protein folding
            and quality control by cleaving glucose residues from immature
            glycoproteins in the endoplasmic reticulum. Expression of the
            encoded protein is elevated in lung tumor tissue and in response to
            UV irradiation. Mutations in this gene cause autosomal-dominant
            polycystic kidney and liver disease. [provided by RefSeq, Jul
            2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.171892.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..703
                     /product="neutral alpha-glucosidase AB isoform 7"
                     /EC_number="3.2.1.207"
                     /note="alpha-glucosidase 2; mannosyl-oligosaccharide
                     alpha-1,3-glucosidase"
                     /calculated_mol_wt=79881
     Region          3..143
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            42
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          143..610
                     /region_name="GH31_GANC_GANAB_alpha"
                     /note="neutral alpha-glucosidase C, neutral
                     alpha-glucosidase AB; cd06603"
                     /db_xref="CDD:269889"
     Site            order(188,301,361,374,377,410,435)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:269889"
     Region          586..654
                     /region_name="DUF5110"
                     /note="Domain of unknown function (DUF5110); pfam17137"
                     /db_xref="CDD:465360"
     CDS             1..703
                     /gene="GANAB"
                     /gene_synonym="G2AN; GIIA; GIIalpha; GLUII; PKD3"
                     /coded_by="NM_001329225.2:791..2902"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:23193"
                     /db_xref="HGNC:HGNC:4138"
                     /db_xref="MIM:104160"
ORIGIN      
        1 msvgldfslp gmehvygipe hadnlrlkvt eggepyrlyn ldvfqyelyn pmalygsvpv
       61 llahnphrdl gifwlnaaet wvdissntag ktlfgkmmdy lqgsgetpqt dvrwmsetgi
      121 idvflllgps isdvfrqyas ltgtqalppl fslgyhqsrw nyrdeadvle vdqgfddhnl
      181 pcdviwldie hadgkryftw dpsrfpqprt mlerlaskrr klvaivdphi kvdsgyrvhe
      241 elrnlglyvk trdgsdyegw cwpgsagypd ftnptmraww anmfsydnye gsapnlfvwn
      301 dmnepsvfng pevtmlkdaq hyggwehrdv hniyglyvhm atadglrqrs ggmerpfvla
      361 raffagsqrf gavwtgdnta ewdhlkisip mclslglvgl sfcgadvggf fknpepellv
      421 rwyqmgayqp ffrahahldt grrepwllps qhndiirdal gqrysllpfw ytllyqahre
      481 gipvmrplwv qypqdvttfn iddqyllgda llvhpvsdsg ahgvqvylpg qgevwydiqs
      541 yqkhhgpqtl ylpvtlssip vfqrggtivp rwmrvrrsse cmkddpitlf valspqgtaq
      601 gelflddght fnyqtrqefl lrrfsfsgnt lvsssadpeg hfetpiwier vviigagkpa
      661 avvlqtkgsp esrlsfqhdp etsvlvlrkp ginvasdwsi hlr
//
LOCUS       NP_004906                678 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family G member 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_004906
VERSION     NP_004906.3
DBSOURCE    REFSEQ: accession NM_004915.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Yazdi,M.K., Alavi,M.S. and Roohbakhsh,A.
  TITLE     The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms
  JOURNAL   Basic Clin Pharmacol Toxicol 134 (4), 423-438 (2024)
   PUBMED   38275217
  REMARK    GeneRIF: The role of ATP-binding cassette transporter G1 (ABCG1) in
            Alzheimer's disease: A review of the mechanisms.
            Review article
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Zeng,G.G., Lei,Q., Jiang,W.L., Zhang,X.X., Nie,L., Gong,X. and
            Zheng,K.
  TITLE     A new perspective on the current and future development potential
            of ABCG1
  JOURNAL   Curr Probl Cardiol 49 (1 Pt C), 102161 (2024)
   PUBMED   37875209
  REMARK    GeneRIF: A new perspective on the current and future development
            potential of ABCG1.
            Review article
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Li,X., Shao,X., Kou,M., Wang,X., Ma,H., Grundberg,E., Bazzano,L.A.,
            Smith,S.R., Bray,G.A., Sacks,F.M. and Qi,L.
  TITLE     DNA Methylation at ABCG1 and Long-term Changes in Adiposity and Fat
            Distribution in Response to Dietary Interventions: The POUNDS Lost
            Trial
  JOURNAL   Diabetes Care 46 (12), 2201-2207 (2023)
   PUBMED   37770056
  REMARK    GeneRIF: DNA Methylation at ABCG1 and Long-term Changes in
            Adiposity and Fat Distribution in Response to Dietary
            Interventions: The POUNDS Lost Trial.
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Jin,J., Zhao,X., Zhu,C., Li,M., Wang,J., Fan,Y., Liu,C., Shen,C.
            and Yang,R.
  TITLE     Hypomethylation of ABCG1 in peripheral blood as a potential marker
            for the detection of coronary heart disease
  JOURNAL   Clin Epigenetics 15 (1), 120 (2023)
   PUBMED   37507725
  REMARK    GeneRIF: Hypomethylation of ABCG1 in peripheral blood as a
            potential marker for the detection of coronary heart disease.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Zhou,W., Sun,J., Huai,C., Liu,Y., Chen,L., Yi,Z., Lv,Q., Song,C.,
            Zhu,W., Liu,C., Weng,S., Wu,H., Sun,Y., Zhang,R., Wu,L., Li,M.,
            Zhu,J., Zhang,Y., Wei,M., Guo,Y., Huang,S., Zhang,N., Shen,R.,
            Zhang,Y., Du,H., Huang,H., He,L., Sun,X., Shen,L. and Qin,S.
  TITLE     Multi-omics analysis identifies rare variation in leptin/PPAR gene
            sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes
  JOURNAL   Mol Psychiatry 27 (12), 5195-5205 (2022)
   PUBMED   36065016
  REMARK    GeneRIF: Multi-omics analysis identifies rare variation in
            leptin/PPAR gene sets and hypermethylation of ABCG1 contribute to
            antipsychotics-induced metabolic syndromes.
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Venkateswaran,A., Repa,J.J., Lobaccaro,J.M., Bronson,A.,
            Mangelsdorf,D.J. and Edwards,P.A.
  TITLE     Human white/murine ABC8 mRNA levels are highly induced in
            lipid-loaded macrophages. A transcriptional role for specific
            oxysterols
  JOURNAL   J Biol Chem 275 (19), 14700-14707 (2000)
   PUBMED   10799558
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 817-822 (2000)
   PUBMED   10639163
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
   PUBMED   9034316
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm Genome 7 (9), 673-676 (1996)
   PUBMED   8703120
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am J Hum Genet 59 (1), 66-75 (1996)
   PUBMED   8659545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001622.1, BC029158.1,
            U34919.1 and X91249.1.
            
            On Apr 27, 2004 this sequence version replaced NP_004906.2.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol and phospholipids transport, and may
            regulate cellular lipid homeostasis in other cell types. Six
            alternative splice variants have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) differs in the 5' end-region
            compared to variant 1, which includes a part of the coding region.
            The resulting isoform (4) has a distinct and shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X91249.1, SRR18074968.149764.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..678
                     /product="ATP-binding cassette sub-family G member 1
                     isoform 4"
                     /EC_number="7.6.2.-"
                     /note="ABC transporter 8; ATP-binding cassette transporter
                     8; homolog of Drosophila white; ATP-binding cassette
                     sub-family G member 1; ATP-binding cassette transporter
                     member 1 of subfamily G; white protein homolog
                     (ATP-binding cassette transporter 8); ATP-binding
                     cassette, sub-family G (WHITE), member 1"
                     /calculated_mol_wt=75461
     Region          60..678
                     /region_name="3a01204"
                     /note="The Eye Pigment Precursor Transporter (EPP) Family
                     protein; TIGR00955"
                     /db_xref="CDD:273361"
     Site            427..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            457..477
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            507..525
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            534..555
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            568..586
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     Site            650..669
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P45844.3)"
     CDS             1..678
                     /gene="ABCG1"
                     /gene_synonym="ABC8; WHITE1"
                     /coded_by="NM_004915.4:124..2160"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13682.1"
                     /db_xref="GeneID:9619"
                     /db_xref="HGNC:HGNC:73"
                     /db_xref="MIM:603076"
ORIGIN      
        1 maclmaafsv gtamnassys aemtepksvc vsvdevvssn meatetdlln ghlkkvdnnl
       61 teaqrfsslp rraavniefr dlsysvpegp wwrkkgyktl lkgisgkfns gelvaimgps
      121 gagkstlmni lagyretgmk gavlinglpr dlrcfrkvsc yimqddmllp hltvqeammv
      181 sahlklqekd egrremvkei ltalgllsca ntrtgslsgg qrkrlaiale lvnnppvmff
      241 deptsgldsa scfqvvslmk glaqggrsii ctihqpsakl felfdqlyvl sqgqcvyrgk
      301 vcnlvpylrd lglncptyhn padfvmevas geygdqnsrl vravregmcd sdhkrdlggd
      361 aevnpflwhr pseevkqtkr lkglrkdsss megchsfsas cltqfcilfk rtflsimrds
      421 vlthlritsh igiglligll ylgigneakk vlsnsgflff smlflmfaal mptvltfple
      481 mgvflrehln ywyslkayyl aktmadvpfq imfpvaycsi vywmtsqpsd avrfvlfaal
      541 gtmtslvaqs lglligaast slqvatfvgp vtaipvllfs gffvsfdtip tylqwmsyis
      601 yvrygfegvi lsiygldred lhcdidetch fqkseailre ldvenaklyl dfivlgiffi
      661 slrliayfvl rykiraer
//
LOCUS       NP_001427                321 aa            linear   PRI 20-NOV-2025
DEFINITION  rRNA 2'-O-methyltransferase fibrillarin [Homo sapiens].
ACCESSION   NP_001427
VERSION     NP_001427.2
DBSOURCE    REFSEQ: accession NM_001436.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Zhang,D., Li,B., Xu,H., Li,J., Ma,C., Ge,W., Lu,C. and Cao,X.
  TITLE     Identification of FBLL1 as a neuron-specific RNA
            2'-O-methyltransferase mediating neuronal differentiation
  JOURNAL   Proc Natl Acad Sci U S A 121 (48), e2406961121 (2024)
   PUBMED   39570315
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Liu,Y., Shi,Q., Liu,Y., Li,X., Wang,Z., Huang,S., Chen,Z. and He,X.
  TITLE     Fibrillarin reprograms glucose metabolism by driving the
            enhancer-mediated transcription of PFKFB4 in liver cancer
  JOURNAL   Cancer Lett 602, 217190 (2024)
   PUBMED   39182558
  REMARK    GeneRIF: Fibrillarin reprograms glucose metabolism by driving the
            enhancer-mediated transcription of PFKFB4 in liver cancer.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Sun,X., Gao,C., Xu,X., Li,M., Zhao,X., Wang,Y., Wang,Y., Zhang,S.,
            Yan,Z., Liu,X. and Wu,C.
  TITLE     FBL promotes cancer cell resistance to DNA damage and BRCA1
            transcription via YBX1
  JOURNAL   EMBO Rep 24 (9), e56230 (2023)
   PUBMED   37489617
  REMARK    GeneRIF: FBL promotes cancer cell resistance to DNA damage and
            BRCA1 transcription via YBX1.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Decle-Carrasco,S., Rodriguez-Pina,A.L., Rodriguez-Zapata,L.C. and
            Castano,E.
  TITLE     Current research on viral proteins that interact with fibrillarin
  JOURNAL   Mol Biol Rep 50 (5), 4631-4643 (2023)
   PUBMED   36928641
  REMARK    GeneRIF: Current research on viral proteins that interact with
            fibrillarin.
            Review article
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Okano,Y., Steen,V.D. and Medsger,T.A. Jr.
  TITLE     Autoantibody to U3 nucleolar ribonucleoprotein (fibrillarin) in
            patients with systemic sclerosis
  JOURNAL   Arthritis Rheum 35 (1), 95-100 (1992)
   PUBMED   1731817
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Baserga,S.J., Yang,X.D. and Steitz,J.A.
  TITLE     An intact Box C sequence in the U3 snRNA is required for binding of
            fibrillarin, the protein common to the major family of nucleolar
            snRNPs
  JOURNAL   EMBO J 10 (9), 2645-2651 (1991)
   PUBMED   1714385
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Jansen,R.P., Hurt,E.C., Kern,H., Lehtonen,H., Carmo-Fonseca,M.,
            Lapeyre,B. and Tollervey,D.
  TITLE     Evolutionary conservation of the human nucleolar protein
            fibrillarin and its functional expression in yeast
  JOURNAL   J Cell Biol 113 (4), 715-729 (1991)
   PUBMED   2026646
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Aris,J.P. and Blobel,G.
  TITLE     cDNA cloning and sequencing of human fibrillarin, a conserved
            nucleolar protein recognized by autoimmune antisera
  JOURNAL   Proc Natl Acad Sci U S A 88 (3), 931-935 (1991)
   PUBMED   1846968
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Lischwe,M.A., Ochs,R.L., Reddy,R., Cook,R.G., Yeoman,L.C.,
            Tan,E.M., Reichlin,M. and Busch,H.
  TITLE     Purification and partial characterization of a nucleolar
            scleroderma antigen (Mr = 34,000; pI, 8.5) rich in
            NG,NG-dimethylarginine
  JOURNAL   J Biol Chem 260 (26), 14304-14310 (1985)
   PUBMED   2414294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG831506.1 and BC019260.1.
            
            On Jan 8, 2001 this sequence version replaced NP_001427.1.
            
            Summary: This gene product is a component of a nucleolar small
            nuclear ribonucleoprotein (snRNP) particle thought to participate
            in the first step in processing preribosomal RNA. It is associated
            with the U3, U8, and U13 small nuclear RNAs and is located in the
            dense fibrillar component (DFC) of the nucleolus. The encoded
            protein contains an N-terminal repetitive domain that is rich in
            glycine and arginine residues, like fibrillarins in other species.
            Its central region resembles an RNA-binding domain and contains an
            RNP consensus sequence. Antisera from approximately 8% of humans
            with the autoimmune disease scleroderma recognize fibrillarin.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019260.1, SRR1163658.428476.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221801.8/ ENSP00000221801.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..321
                     /product="rRNA 2'-O-methyltransferase fibrillarin"
                     /note="34-kD nucleolar scleroderma antigen; RNA, U3 small
                     nucleolar interacting protein 1; 34 kDa nucleolar
                     scleroderma antigen; histone-glutamine methyltransferase;
                     U6 snRNA 2'-O-methyltransferase fibrillarin"
                     /calculated_mol_wt=33653
     Region          1..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22087.2)"
     Site            8
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            15
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            21
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            24
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            27
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:P22509; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            34
                     /site_type="methylation"
     Site            36
                     /site_type="methylation"
     Region          82..320
                     /region_name="PTZ00146"
                     /note="fibrillarin; Provisional"
                     /db_xref="CDD:240291"
     Site            102
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30540930; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            121
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30540930; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Region          185..192
                     /region_name="RNP consensus sequence"
     Site            205
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30540930; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Site            206
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:30540930; propagated from
                     UniProtKB/Swiss-Prot (P22087.2)"
     Region          274..306
                     /region_name="Helical. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P22087.2)"
     CDS             1..321
                     /gene="FBL"
                     /gene_synonym="FIB; FLRN; Nop1; RNU3IP1"
                     /coded_by="NM_001436.4:80..1045"
                     /db_xref="CCDS:CCDS12545.1"
                     /db_xref="GeneID:2091"
                     /db_xref="HGNC:HGNC:3599"
                     /db_xref="MIM:134795"
ORIGIN      
        1 mkpgfsprgg gfggrggfgd rggrggrggf gggrgrgggf rgrgrggggg ggggggggrg
       61 gggfhsggnr grgrggkrgn qsgknvmvep hrhegvficr gkedalvtkn lvpgesvyge
      121 krvsisegdd kieyrawnpf rsklaaailg gvdqihikpg akvlylgaas gttvshvsdi
      181 vgpdglvyav efshrsgrdl inlakkrtni ipviedarhp hkyrmliamv dvifadvaqp
      241 dqtrivalna htflrngghf visikancid stasaeavfa sevkkmqqen mkpqeqltle
      301 pyerdhavvv gvyrpppkvk n
//
LOCUS       NP_001293014            1136 aa            linear   PRI 20-NOV-2025
DEFINITION  probable phospholipid-transporting ATPase IIB isoform 2 [Homo
            sapiens].
ACCESSION   NP_001293014 XP_005266748
VERSION     NP_001293014.1
DBSOURCE    REFSEQ: accession NM_001306085.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Yagi,T., Nakabuchi,R., Muranaka,Y., Tanaka,G., Katoh,Y.,
            Nakayama,K., Takatsu,H. and Shin,H.W.
  TITLE     Lipid flippases ATP9A and ATP9B form a complex and contribute to
            the exocytic pathway from the Golgi
  JOURNAL   Life Sci Alliance 8 (7), e202403163 (2025)
   PUBMED   40234049
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Eeles,R.A., Olama,A.A., Benlloch,S., Saunders,E.J.,
            Leongamornlert,D.A., Tymrakiewicz,M., Ghoussaini,M., Luccarini,C.,
            Dennis,J., Jugurnauth-Little,S., Dadaev,T., Neal,D.E., Hamdy,F.C.,
            Donovan,J.L., Muir,K., Giles,G.G., Severi,G., Wiklund,F.,
            Gronberg,H., Haiman,C.A., Schumacher,F., Henderson,B.E., Le
            Marchand,L., Lindstrom,S., Kraft,P., Hunter,D.J., Gapstur,S.,
            Chanock,S.J., Berndt,S.I., Albanes,D., Andriole,G., Schleutker,J.,
            Weischer,M., Canzian,F., Riboli,E., Key,T.J., Travis,R.C.,
            Campa,D., Ingles,S.A., John,E.M., Hayes,R.B., Pharoah,P.D.,
            Pashayan,N., Khaw,K.T., Stanford,J.L., Ostrander,E.A.,
            Signorello,L.B., Thibodeau,S.N., Schaid,D., Maier,C., Vogel,W.,
            Kibel,A.S., Cybulski,C., Lubinski,J., Cannon-Albright,L.,
            Brenner,H., Park,J.Y., Kaneva,R., Batra,J., Spurdle,A.B.,
            Clements,J.A., Teixeira,M.R., Dicks,E., Lee,A., Dunning,A.M.,
            Baynes,C., Conroy,D., Maranian,M.J., Ahmed,S., Govindasami,K.,
            Guy,M., Wilkinson,R.A., Sawyer,E.J., Morgan,A., Dearnaley,D.P.,
            Horwich,A., Huddart,R.A., Khoo,V.S., Parker,C.C., Van As,N.J.,
            Woodhouse,C.J., Thompson,A., Dudderidge,T., Ogden,C., Cooper,C.S.,
            Lophatananon,A., Cox,A., Southey,M.C., Hopper,J.L., English,D.R.,
            Aly,M., Adolfsson,J., Xu,J., Zheng,S.L., Yeager,M., Kaaks,R.,
            Diver,W.R., Gaudet,M.M., Stern,M.C., Corral,R., Joshi,A.D.,
            Shahabi,A., Wahlfors,T., Tammela,T.L., Auvinen,A., Virtamo,J.,
            Klarskov,P., Nordestgaard,B.G., Roder,M.A., Nielsen,S.F.,
            Bojesen,S.E., Siddiq,A., Fitzgerald,L.M., Kolb,S., Kwon,E.M.,
            Karyadi,D.M., Blot,W.J., Zheng,W., Cai,Q., McDonnell,S.K.,
            Rinckleb,A.E., Drake,B., Colditz,G., Wokolorczyk,D.,
            Stephenson,R.A., Teerlink,C., Muller,H., Rothenbacher,D.,
            Sellers,T.A., Lin,H.Y., Slavov,C., Mitev,V., Lose,F.,
            Srinivasan,S., Maia,S., Paulo,P., Lange,E., Cooney,K.A.,
            Antoniou,A.C., Vincent,D., Bacot,F., Tessier,D.C., Kote-Jarai,Z.
            and Easton,D.F.
  CONSRTM   COGS-Cancer Research UK GWAS-ELLIPSE (part of GAME-ON) Initiative;
            Australian Prostate Cancer Bioresource; UK Genetic Prostate Cancer
            Study Collaborators/British Association of Urological Surgeons'
            Section of Oncology; UK ProtecT (Prostate testing for cancer and
            Treatment) Study Collaborators; PRACTICAL (Prostate Cancer
            Association Group to Investigate Cancer-Associated Alterations in
            the Genome) Consortium
  TITLE     Identification of 23 new prostate cancer susceptibility loci using
            the iCOGS custom genotyping array
  JOURNAL   Nat Genet 45 (4), 385-391 (2013)
   PUBMED   23535732
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Tashiro-Yamaji,J., Shimizu,T., Hayashi,M., Yamana,H., Tanigawa,N.,
            Uchiyama,K., Kubota,T. and Yoshida,R.
  TITLE     Specific binding of HLA-B44 to human macrophage MHC receptor 1 on
            monocytes
  JOURNAL   Gene 501 (2), 127-134 (2012)
   PUBMED   22525042
  REMARK    GeneRIF: These results revealed that human human macrophage MHC
            receptor 1 on monocytes is a novel receptor specific for HLA-B44.
REFERENCE   4  (residues 1 to 1136)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   5  (residues 1 to 1136)
  AUTHORS   Nusbaum,C., Zody,M.C., Borowsky,M.L., Kamal,M., Kodira,C.D.,
            Taylor,T.D., Whittaker,C.A., Chang,J.L., Cuomo,C.A., Dewar,K.,
            FitzGerald,M.G., Yang,X., Abouelleil,A., Allen,N.R., Anderson,S.,
            Bloom,T., Bugalter,B., Butler,J., Cook,A., DeCaprio,D., Engels,R.,
            Garber,M., Gnirke,A., Hafez,N., Hall,J.L., Norman,C.H., Itoh,T.,
            Jaffe,D.B., Kuroki,Y., Lehoczky,J., Lui,A., Macdonald,P.,
            Mauceli,E., Mikkelsen,T.S., Naylor,J.W., Nicol,R., Nguyen,C.,
            Noguchi,H., O'Leary,S.B., O'Neill,K., Piqani,B., Smith,C.L.,
            Talamas,J.A., Topham,K., Totoki,Y., Toyoda,A., Wain,H.M.,
            Young,S.K., Zeng,Q., Zimmer,A.R., Fujiyama,A., Hattori,M.,
            Birren,B.W., Sakaki,Y. and Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 18
  JOURNAL   Nature 437 (7058), 551-555 (2005)
   PUBMED   16177791
  REMARK    Erratum:[Nature. 2005 Dec 1;438(7068):696. O'Neill, Keith [added]]
REFERENCE   6  (residues 1 to 1136)
  AUTHORS   Stanchi,F., Bertocco,E., Toppo,S., Dioguardi,R., Simionati,B.,
            Cannata,N., Zimbello,R., Lanfranchi,G. and Valle,G.
  TITLE     Characterization of 16 novel human genes showing high similarity to
            yeast sequences
  JOURNAL   Yeast 18 (1), 69-80 (2001)
   PUBMED   11124703
REFERENCE   7  (residues 1 to 1136)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1136)
  AUTHORS   Halleck,M.S., Pradhan,D., Blackman,C., Berkes,C., Williamson,P. and
            Schlegel,R.A.
  TITLE     Multiple members of a third subfamily of P-type ATPases identified
            by genomic sequences and ESTs
  JOURNAL   Genome Res 8 (4), 354-361 (1998)
   PUBMED   9548971
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY028472.1, BC125219.1, AL096735.1 and AW411030.1.
            
            On Apr 14, 2015 this sequence version replaced XP_005266748.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.131407.1,
                                           SRR1803615.78157.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..1136
                     /product="probable phospholipid-transporting ATPase IIB
                     isoform 2"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase IIB;
                     ATPase type IV, phospholipid transporting (P-type);
                     macrophage MHC receptor 1; ATPase, class II, type 9B;
                     ATPase phospholipid transporting 9B (putative)"
                     /calculated_mol_wt=128068
     Region          132..1056
                     /region_name="P-type_ATPase_APLT_Neo1-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Neo1p and human putative APLT,
                     ATP9B; cd07541"
                     /db_xref="CDD:319841"
     Site            147..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            174..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            410..431
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            order(468..470,633,657..659,719,766..768,848,851,854,874,
                     877)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319841"
     Region          503..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Region          576..660
                     /region_name="Cation_ATPase"
                     /note="Cation transport ATPase (P-type); pfam13246"
                     /db_xref="CDD:463817"
     Site            931..951
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            964..982
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1013..1031
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1039..1061
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1068..1088
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     Site            1095..1119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43861.4)"
     CDS             1..1136
                     /gene="ATP9B"
                     /gene_synonym="ATPASEP; ATPIIB; hMMR1; HUSSY-20; NEO1L"
                     /coded_by="NM_001306085.2:18..3428"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77202.1"
                     /db_xref="GeneID:374868"
                     /db_xref="HGNC:HGNC:13541"
                     /db_xref="MIM:614446"
ORIGIN      
        1 madqiplypv rsaaaaaanr kraayysaag prpgadrhsr yqledesahl demplmmsee
       61 gfeneesdyh tlprarimqr krglewfvcd gwkflctscc gwlinicrrk kelkartvwl
      121 gcpekceekh prnsiknqky nvftfipgvl yeqfkfflnl yflviscsqf vpalkigyly
      181 tywaplgfvl avtmtreaid efrrfqrdke vnsqlysklt vrgkvqvkss diqvgdliiv
      241 eknqripsdm vflrtsekag scfirtdqld getdwklkva vsctqqlpal gdlfsisayv
      301 yaqkpqmdih sfegtftred sdppihesls ientlwasti vasgtvigvv iytgketrsv
      361 mntsnpknkv glldlelnrl tkalflalva lsivmvtlqg fvgpwyrnlf rflllfsyii
      421 pislrvnldm gkavygwmmm kdenipgtvv rtstipeelg rlvylltdkt gtltqnemif
      481 krlhlgtvsy gadtmdeiqs hvrdsysqmq sqaggnntgs tplrkaqssa pkvrksvssr
      541 iheavkaivl chnvtpvyes ragvteetef aeadqdfsde nrtyqasspd evalvqwtes
      601 vgltlvsrdl tsmqlktpsg qvlsfcilql fpftseskrm gvivrdesta eitfymkgad
      661 vamspivqyn dwleeecgnm areglrtlvv akkalteeqy qdfesrytqa klsmhdrslk
      721 vaavvesler emellcltgv edqlqadvrp tlemlrnagi kiwmltgdkl etatciakss
      781 hlvsrtqdih ifrqvtsrge ahlelnafrr khdcalvisg dslevclkyy ehefvelacq
      841 cpavvccrcs ptqkarivtl lqqhtgrrtc aigdggndvs miqaadcgig iegkegkqas
      901 laadfsitqf rhigrllmvh grnsykrsaa lgqfvmhrgl iistmqavfs svfyfasvpl
      961 yqgflmvgya tiytmfpvfs lvldqdvkpe mamlypelyk dltkgrslsf ktfliwvlis
     1021 iyqggilmyg alvlfesefv hvvaisftal iltellmval tvrtwhwlmv vaeflslgcy
     1081 vsslaflney fdvafittvt flwkvsaitv vsclplyvlk ylrrklspps ycklas
//
LOCUS       NP_057036                243 aa            linear   PRI 20-NOV-2025
DEFINITION  RWD domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_057036
VERSION     NP_057036.2
DBSOURCE    REFSEQ: accession NM_015952.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Grotsch,H., Kunert,M., Mooslehner,K.A., Gao,Z., Struve,D.,
            Hughes,I.A., Hiort,O. and Werner,R.
  TITLE     RWDD1 interacts with the ligand binding domain of the androgen
            receptor and acts as a coactivator of androgen-dependent
            transactivation
  JOURNAL   Mol Cell Endocrinol 358 (1), 53-62 (2012)
   PUBMED   22406838
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290727.1, AK301089.1, CK817864.1 and AL121953.21.
            
            On Nov 22, 2004 this sequence version replaced NP_057036.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.48637.1,
                                           SRR1803615.227285.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000466444.7/ ENSP00000420357.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..243
                     /product="RWD domain-containing protein 1 isoform a"
                     /note="RWD domain-containing protein 1; DRG
                     family-regulatory protein 2"
                     /calculated_mol_wt=27808
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H446.1)"
     Region          4..119
                     /region_name="RWD_RWDD1"
                     /note="RWD domain of RWD domain-containing protein 1
                     (RWDD1) and related proteins; cd23816"
                     /db_xref="CDD:467652"
     Region          142..197
                     /region_name="Interaction with DRG2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H446.1)"
     Region          <144..>197
                     /region_name="DFRP_C"
                     /note="DRG Family Regulatory Proteins, Tma46; pfam16543"
                     /db_xref="CDD:465167"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H446.1)"
     Region          198..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H446.1)"
     CDS             1..243
                     /gene="RWDD1"
                     /gene_synonym="CGI-24; DFRP2; PTD013"
                     /coded_by="NM_015952.4:80..811"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34520.1"
                     /db_xref="GeneID:51389"
                     /db_xref="HGNC:HGNC:20993"
                     /db_xref="MIM:620844"
ORIGIN      
        1 mtdygeeqrn elealesiyp dsftvlsenp psftitvtse agendetvqt tlkftyseky
       61 pdeaplyeif sqenledndv sdilkllalq aeenlgmvmi ftlvtavqek lneivdqikt
      121 rreeekkqke keaeeaekql fhgtpvtien flnwkakfda elleikkkrm keeeqagknk
      181 lsgkqlfetd hnldtsdiqf ledagnnvev deslfqemdd leleddeddp dynpadpesd
      241 sad
//
LOCUS       NP_001394034              97 aa            linear   PRI 20-NOV-2025
DEFINITION  protein max isoform i [Homo sapiens].
ACCESSION   NP_001394034
VERSION     NP_001394034.1
DBSOURCE    REFSEQ: accession NM_001407105.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Nair,S.K. and Burley,S.K.
  TITLE     X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular
            bases of regulation by proto-oncogenic transcription factors
  JOURNAL   Cell 112 (2), 193-205 (2003)
   PUBMED   12553908
  REMARK    GeneRIF: X-ray structures of Myc-Max and Mad-Max recognizing DNA.
            Molecular bases of regulation by proto-oncogenic transcription
            factors.
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Lavigne,P., Crump,M.P., Gagne,S.M., Hodges,R.S., Kay,C.M. and
            Sykes,B.D.
  TITLE     Insights into the mechanism of heterodimerization from the 1H-NMR
            solution structure of the c-Myc-Max heterodimeric leucine zipper
  JOURNAL   J Mol Biol 281 (1), 165-181 (1998)
   PUBMED   9680483
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Grandori,C., Mac,J., Siebelt,F., Ayer,D.E. and Eisenman,R.N.
  TITLE     Myc-Max heterodimers activate a DEAD box gene and interact with
            multiple E box-related sites in vivo
  JOURNAL   EMBO J 15 (16), 4344-4357 (1996)
   PUBMED   8861962
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Else,T., Greenberg,S. and Fishbein,L.
  TITLE     Hereditary Paraganglioma-Pheochromocytoma Syndromes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301715
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Wechsler,D.S. and Dang,C.V.
  TITLE     Opposite orientations of DNA bending by c-Myc and Max
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7635-7639 (1992)
   PUBMED   1323849
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Gilladoga,A.D., Edelhoff,S., Blackwood,E.M., Eisenman,R.N. and
            Disteche,C.M.
  TITLE     Mapping of MAX to human chromosome 14 and mouse chromosome 12 by in
            situ hybridization
  JOURNAL   Oncogene 7 (6), 1249-1251 (1992)
   PUBMED   1594250
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Makela,T.P., Koskinen,P.J., Vastrik,I. and Alitalo,K.
  TITLE     Alternative forms of Max as enhancers or suppressors of Myc-ras
            cotransformation
  JOURNAL   Science 256 (5055), 373-377 (1992)
   PUBMED   1566084
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Wagner,A.J., Le Beau,M.M., Diaz,M.O. and Hay,N.
  TITLE     Expression, regulation, and chromosomal localization of the Max
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 3111-3115 (1992)
   PUBMED   1557420
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Blackwood,E.M. and Eisenman,R.N.
  TITLE     Max: a helix-loop-helix zipper protein that forms a
            sequence-specific DNA-binding complex with Myc
  JOURNAL   Science 251 (4998), 1211-1217 (1991)
   PUBMED   2006410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139022.4.
            
            Summary: The protein encoded by this gene is a member of the basic
            helix-loop-helix leucine zipper (bHLHZ) family of transcription
            factors. It is able to form homodimers and heterodimers with other
            family members, which include Mad, Mxi1 and Myc. Myc is an
            oncoprotein implicated in cell proliferation, differentiation and
            apoptosis. The homodimers and heterodimers compete for a common DNA
            target site (the E box) and rearrangement among these dimer forms
            provides a complex system of transcriptional regulation. Mutations
            of this gene have been reported to be associated with hereditary
            pheochromocytoma. A pseudogene of this gene is located on the long
            arm of chromosome 7. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2045754.1,
                                           SRR1660805.90638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..97
                     /product="protein max isoform i"
                     /note="class D basic helix-loop-helix protein 4; MYC
                     associated factor X"
                     /calculated_mol_wt=10571
     CDS             1..97
                     /gene="MAX"
                     /gene_synonym="bHLHd4; PDMCS"
                     /coded_by="NM_001407105.1:417..710"
                     /note="isoform i is encoded by transcript variant 23"
                     /db_xref="GeneID:4149"
                     /db_xref="HGNC:HGNC:6913"
                     /db_xref="MIM:154950"
ORIGIN      
        1 mlfwsskgka radqvlcswg ihfssslmed askrkfrale karssaqlqt nypssdnsly
       61 tnakgstisa fdggsdssse sepeepqsrk klrmeas
//
LOCUS       NP_001124000            1321 aa            linear   PRI 20-NOV-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001124000
VERSION     NP_001124000.1
DBSOURCE    REFSEQ: accession NM_001130528.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1321)
  AUTHORS   Bassey-Archibong,B.I., Rajendra Chokshi,C., Aghaei,N.,
            Kieliszek,A.M., Tatari,N., McKenna,D., Singh,M., Kalpana
            Subapanditha,M., Parmar,A., Mobilio,D., Savage,N., Lam,F.,
            Tokar,T., Provias,J., Lu,Y., Chafe,S.C., Swanton,C., Hynds,R.E.,
            Venugopal,C. and Singh,S.K.
  TITLE     An HLA-G/SPAG9/STAT3 axis promotes brain metastases
  JOURNAL   Proc Natl Acad Sci U S A 120 (8), e2205247120 (2023)
   PUBMED   36780531
  REMARK    GeneRIF: An HLA-G/SPAG9/STAT3 axis promotes brain metastases.
REFERENCE   2  (residues 1 to 1321)
  AUTHORS   Ramadan,R.A., Morsy,H., Samir,M., Shamseya,M., Shalaby,M. and
            El-Attar,E.A.
  TITLE     Significance of cancer testis-associated antigens (SPAG9 and
            FBXO39) in colon cancer
  JOURNAL   Indian J Cancer 59 (3), 394-401 (2022)
   PUBMED   34380828
  REMARK    GeneRIF: Significance of cancer testis-associated antigens (SPAG9
            and FBXO39) in colon cancer.
REFERENCE   3  (residues 1 to 1321)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1321)
  AUTHORS   Del Sarto,J., Gerlt,V., Friedrich,M.E., Anhlan,D., Wixler,V.,
            Teixeira,M.M., Boergeling,Y. and Ludwig,S.
  TITLE     Phosphorylation of JIP4 at S730 Presents Antiviral Properties
            against Influenza A Virus Infection
  JOURNAL   J Virol 95 (20), e0067221 (2021)
   PUBMED   34319782
  REMARK    GeneRIF: Phosphorylation of JIP4 at S730 Presents Antiviral
            Properties against Influenza A Virus Infection.
REFERENCE   5  (residues 1 to 1321)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1321)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   7  (residues 1 to 1321)
  AUTHORS   Yasuoka,H., Ihn,H., Medsger,T.A. Jr., Hirakata,M., Kawakami,Y.,
            Ikeda,Y. and Kuwana,M.
  TITLE     A novel protein highly expressed in testis is overexpressed in
            systemic sclerosis fibroblasts and targeted by autoantibodies
  JOURNAL   J Immunol 171 (12), 6883-6890 (2003)
   PUBMED   14662895
  REMARK    GeneRIF: Testicular antigen PHET is an auutoantigen recognized by
            sera from systemic sclerosis (SSc) patients with extensive fibrotic
            changes; the autoantibody response to PHET is induced by ectopic
            overexpression of PHET in dermal fibroblasts of SSc patients.
REFERENCE   8  (residues 1 to 1321)
  AUTHORS   Lee,C.M., Onesime,D., Reddy,C.D., Dhanasekaran,N. and Reddy,E.P.
  TITLE     JLP: A scaffolding protein that tethers JNK/p38MAPK signaling
            modules and transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14189-14194 (2002)
   PUBMED   12391307
REFERENCE   9  (residues 1 to 1321)
  AUTHORS   Ichijo,H.
  TITLE     From receptors to stress-activated MAP kinases
  JOURNAL   Oncogene 18 (45), 6087-6093 (1999)
   PUBMED   10557099
  REMARK    Review article
REFERENCE   10 (residues 1 to 1321)
  AUTHORS   Shankar,S., Mohapatra,B. and Suri,A.
  TITLE     Cloning of a novel human testis mRNA specifically expressed in
            testicular haploid germ cells, having unique palindromic sequences
            and encoding a leucine zipper dimerization motif
  JOURNAL   Biochem Biophys Res Commun 243 (2), 561-565 (1998)
   PUBMED   9480848
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005839.1, AK091921.1,
            BC146755.1 and AC005920.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cancer testis antigen
            gene family. The encoded protein functions as a scaffold protein
            that structurally organizes mitogen-activated protein kinases and
            mediates c-Jun-terminal kinase signaling. This protein also binds
            to kinesin-1 and may be involved in microtubule-based membrane
            transport. This protein may play a role in tumor growth and
            development. Alternate splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC153878.1, AB011088.3 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262013.12/ ENSP00000262013.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..1321
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     4 isoform 1"
                     /note="sperm surface protein; cancer/testis antigen 89;
                     JNK/SAPK-associated protein; JNK interacting protein;
                     c-Jun NH2-terminal kinase-associated leucine zipper
                     protein; Max-binding protein; C-Jun-amino-terminal
                     kinase-interacting protein 4; proliferation-inducing gene
                     6; lung cancer oncogene 4; sunday driver 1; protein highly
                     expressed in testis; human lung cancer oncogene 6 protein;
                     mitogen-activated protein kinase 8-interacting protein 4;
                     C-Jun N-terminal kinase protein-associated leucine-zipper
                     protein"
                     /calculated_mol_wt=146075
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          24..178
                     /region_name="Jnk-SapK_ap_N"
                     /note="JNK_SAPK-associated protein-1; pfam09744"
                     /db_xref="CDD:462875"
     Region          66..363
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          203..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q58A65; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q58A65; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          406..>461
                     /region_name="JIP_LZII"
                     /note="JNK-interacting protein leucine zipper II;
                     pfam16471"
                     /db_xref="CDD:465127"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          <449..>642
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          473..500
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          563..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          854..906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          952..>1306
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          1239..1266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            1264
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     CDS             1..1321
                     /gene="SPAG9"
                     /gene_synonym="CT89; HLC-6; HLC4; HLC6; JIP-4; JIP4; JLP;
                     PHET; PIG6"
                     /coded_by="NM_001130528.3:213..4178"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45740.1"
                     /db_xref="GeneID:9043"
                     /db_xref="HGNC:HGNC:14524"
                     /db_xref="MIM:605430"
ORIGIN      
        1 meledgvvyq eepggsgavm servsglags iyreferlig rydeevvkel mplvvavlen
       61 ldsvfaqdqe hqvelellrd dneqlitqye rekalrkhae ekfiefedsq eqekkdlqtr
      121 veslesqtrq lelkaknyad qisrleerea elkkeynalh qrhtemihny mehlertklh
      181 qlsgsdqles tahsrirker pislgifplp agdglltpda qkggetpgse qwkfqelsqp
      241 rshtslkvsn spepqkaveq edelsdvsqg gskattpast ansdvatipt dtplkeeneg
      301 fvkvtdapnk seiskhievq vaqetrnvst gsaeneekse vqaiiestpe ldmdkdlsgy
      361 kgsstptkgi enkafdrnte slfeelssag sgligdvdeg adllgmgrev enlilentql
      421 letknalniv kndliakvde ltcekdvlqg eleavkqakl kleeknrele eelrkaraea
      481 edarqkakdd ddsdiptaqr krftrvemar vlmernqyke rlmelqeavr wtemirasre
      541 npamqekkrs siwqffsrlf ssssnttkkp eppvnlkyna ptshvtpsvk krsstlsqlp
      601 gdkskafdfl seeteaslas rreqkreqyr qvkahvqked grvqafgwsl pqkykqvtng
      661 qgenkmknlp vpvylrplde kdtsmklwca vgvnlsggkt rdggsvvgas vfykdvagld
      721 tegskqrsas qssldkldqe lkeqqkelkn qeelsslvwi ctsthsatkv liidavqpgn
      781 ildsftvcns hvlciasvpg aretdypage dlsesgqvdk aslcgsmtsn ssaetdsllg
      841 gitvvgcsae gvtgaatsps tngaspvmdk ppemeaense vdenvptaee ateategnag
      901 saedtvdisq tgvytehvft dplgvqiped lspvyqssnd sdaykdqisv lpneqdlvre
      961 eaqkmssllp tmwlgaqngc lyvhssvaqw rkclhsiklk dsilsivhvk givlvaladg
     1021 tlaifhrgvd gqwdlsnyhl ldlgrphhsi rcmtvvhdkv wcgyrnkiyv vqpkamkiek
     1081 sfdahprkes qvrqlawvgd gvwvsirlds tlrlyhahty qhlqdvdiep yvskmlgtgk
     1141 lgfsfvrita lmvscnrlwv gtgngviisi pltetnktsg vpgnrpgsvi rvygdensdk
     1201 vtpgtfipyc smahaqlcfh ghrdavkffv avpgqvispq ssssgtdltg dkagpsaqep
     1261 gsqtplksml visggegyid frmgdegges ellgedlple psvtkaersh livwqvmygn
     1321 e
//
LOCUS       NP_001354456             554 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 20 [Homo sapiens].
ACCESSION   NP_001354456 XP_005270256
VERSION     NP_001354456.1
DBSOURCE    REFSEQ: accession NM_001367527.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270256.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.275052.1,
                                           SRR3476690.683250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..554
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 20"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=61465
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          422..549
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..554
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367527.1:95..1759"
                     /note="isoform 20 is encoded by transcript variant 20"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kepqttvvhn
      361 atdgikgste scnttteded lkaaplrtgn gssvpegrss rdrtapsagm qpqpslcssa
      421 mrkqeiikit eqlieainng dfeaytkicd pgltsfepea lgnlvegmdf hkfyfenlls
      481 knskpihtti lnphvhvige daaciayirl tqyidgqgrp rtsqseetrv whrrdgkwln
      541 vhyhcsgapa aplq
//
LOCUS       NP_001269521             296 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 7 isoform f precursor [Homo sapiens].
ACCESSION   NP_001269521 XP_005245442
VERSION     NP_001269521.1
DBSOURCE    REFSEQ: accession NM_001282592.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Chu,E., Wu,J., Kang,S.S. and Kang,Y.
  TITLE     SLAMF7 as a Promising Immunotherapeutic Target in Multiple Myeloma
            Treatments
  JOURNAL   Curr Oncol 30 (9), 7891-7903 (2023)
   PUBMED   37754488
  REMARK    GeneRIF: SLAMF7 as a Promising Immunotherapeutic Target in Multiple
            Myeloma Treatments.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Choe,U., Pham,Q., Kim,Y.S., Yu,L. and Wang,T.T.Y.
  TITLE     Identification and elucidation of cross talk between SLAM Family
            Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages
  JOURNAL   Sci Rep 13 (1), 11007 (2023)
   PUBMED   37420084
  REMARK    GeneRIF: Identification and elucidation of cross talk between SLAM
            Family Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   O'Connell,P., Blake,M.K., Godbehere,S., Amalfitano,A. and
            Aldhamen,Y.A.
  TITLE     SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity
  JOURNAL   J Neuroinflammation 19 (1), 241 (2022)
   PUBMED   36199066
  REMARK    GeneRIF: SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Simmons,D.P., Nguyen,H.N., Gomez-Rivas,E., Jeong,Y., Jonsson,A.H.,
            Chen,A.F., Lange,J.K., Dyer,G.S., Blazar,P., Earp,B.E.,
            Coblyn,J.S., Massarotti,E.M., Sparks,J.A., Todd,D.J., Rao,D.A.,
            Kim,E.Y. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership (AMP) RA/SLE Network
  TITLE     SLAMF7 engagement superactivates macrophages in acute and chronic
            inflammation
  JOURNAL   Sci Immunol 7 (68), eabf2846 (2022)
   PUBMED   35148199
  REMARK    GeneRIF: SLAMF7 engagement superactivates macrophages in acute and
            chronic inflammation.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Lee,J.K., Boles,K.S. and Mathew,P.A.
  TITLE     Molecular and functional characterization of a CS1 (CRACC) splice
            variant expressed in human NK cells that does not contain
            immunoreceptor tyrosine-based switch motifs
  JOURNAL   Eur J Immunol 34 (10), 2791-2799 (2004)
   PUBMED   15368295
  REMARK    GeneRIF: CS1-L and CS1-S may differentially regulate human NK cell
            functions
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Tovar,V., del Valle,J., Zapater,N., Martin,M., Romero,X.,
            Pizcueta,P., Bosch,J., Terhorst,C. and Engel,P.
  TITLE     Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family
            of leukocyte cell-surface receptors
  JOURNAL   Immunogenetics 54 (6), 394-402 (2002)
   PUBMED   12242590
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Murphy,J.J., Hobby,P., Vilarino-Varela,J., Bishop,B.,
            Iordanidou,P., Sutton,B.J. and Norton,J.D.
  TITLE     A novel immunoglobulin superfamily receptor (19A) related to CD2 is
            expressed on activated lymphocytes and promotes homotypic B-cell
            adhesion
  JOURNAL   Biochem J 361 (Pt 3), 431-436 (2002)
   PUBMED   11802771
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Bouchon,A., Cella,M., Grierson,H.L., Cohen,J.I. and Colonna,M.
  TITLE     Activation of NK cell-mediated cytotoxicity by a SAP-independent
            receptor of the CD2 family
  JOURNAL   J Immunol 167 (10), 5517-5521 (2001)
   PUBMED   11698418
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Boles,K.S. and Mathew,P.A.
  TITLE     Molecular cloning of CS1, a novel human natural killer cell
            receptor belonging to the CD2 subset of the immunoglobulin
            superfamily
  JOURNAL   Immunogenetics 52 (3-4), 302-307 (2001)
   PUBMED   11220635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388332.1, AK290706.1, AL121985.13 and BQ000581.1.
            
            On Sep 14, 2013 this sequence version replaced XP_005245442.1.
            
            Transcript Variant: This variant (6) lacks an alternate exon that
            results in a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (f, also known as CS1-S) has a
            distinct C-terminus and is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027867.1, SRR1163658.222647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..296
                     /product="SLAM family member 7 isoform f precursor"
                     /note="CD2-like receptor activating cytotoxic cells; 19A24
                     protein; novel LY9 (lymphocyte antigen 9) like protein;
                     protein 19A; CD2 subset 1; membrane protein FOAP-12"
                     /calculated_mol_wt=30289
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2311
     Region          27..125
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          50..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          88..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Region          102..107
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ25.1)"
     CDS             1..296
                     /gene="SLAMF7"
                     /gene_synonym="19A; CD319; CRACC; CS1"
                     /coded_by="NM_001282592.2:56..946"
                     /note="isoform f precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS60321.1"
                     /db_xref="GeneID:57823"
                     /db_xref="HGNC:HGNC:21394"
                     /db_xref="MIM:606625"
ORIGIN      
        1 magsptcltl iyilwqltgs aasgpvkelv gsvggavtfp lkskvkqvds ivwtfnttpl
       61 vtiqpeggti ivtqnrnrer vdfpdggysl klsklkknds giyyvgiyss slqqpstqey
      121 vlhvyehlsk pkvtmglqsn kngtcvtnlt ccmehgeedv iytwkalgqa aneshngsil
      181 piswrwgesd mtficvarnp vsrnfsspil arklcegaad dpdssmvllc lllvplllsl
      241 fvlglflwfl krerqeennp kgrsskygll hcgntekdgk spltahdarh tkaicl
//
LOCUS       NP_000386                897 aa            linear   PRI 20-NOV-2025
DEFINITION  cytokine receptor common subunit beta isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_000386
VERSION     NP_000386.1
DBSOURCE    REFSEQ: accession NM_000395.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 897)
  AUTHORS   Charlet,A., Kappenstein,M., Keye,P., Klasener,K., Endres,C.,
            Poggio,T., Gorantla,S.P., Kreutmair,S., Sanger,J., Illert,A.L.,
            Miething,C., Reth,M., Duyster,J., Rummelt,C. and von Bubnoff,N.
  TITLE     The IL-3, IL-5, and GM-CSF common receptor beta chain mediates
            oncogenic activity of FLT3-ITD-positive AML
  JOURNAL   Leukemia 36 (3), 701-711 (2022)
   PUBMED   34750506
  REMARK    GeneRIF: The IL-3, IL-5, and GM-CSF common receptor beta chain
            mediates oncogenic activity of FLT3-ITD-positive AML.
REFERENCE   2  (residues 1 to 897)
  AUTHORS   Rashid,M., Ali,R., Almuzzaini,B., Song,H., AlHallaj,A.,
            Abdulkarim,A.A., Mohamed Baz,O., Al Zahrani,H., Mustafa Sabeena,M.,
            Alharbi,W., Hussein,M. and Boudjelal,M.
  TITLE     Discovery of a novel potentially transforming somatic mutation in
            CSF2RB gene in breast cancer
  JOURNAL   Cancer Med 10 (22), 8138-8150 (2021)
   PUBMED   34729943
  REMARK    GeneRIF: Discovery of a novel potentially transforming somatic
            mutation in CSF2RB gene in breast cancer.
REFERENCE   3  (residues 1 to 897)
  AUTHORS   Benard,A., Jacobsen,A., Brunner,M., Krautz,C., Klosch,B.,
            Swierzy,I., Naschberger,E., Podolska,M.J., Kouhestani,D., David,P.,
            Birkholz,T., Castellanos,I., Trufa,D., Sirbu,H., Vetter,M.,
            Kremer,A.E., Hildner,K., Hecker,A., Edinger,F., Tenbusch,M.,
            Muhl-Zurbes,P., Steinkasserer,A., Richter,E., Streeck,H.,
            Berger,M.M., Brenner,T., Weigand,M.A., Swirski,F.K., Schett,G.,
            Grutzmann,R. and Weber,G.F.
  TITLE     Interleukin-3 is a predictive marker for severity and outcome
            during SARS-CoV-2 infections
  JOURNAL   Nat Commun 12 (1), 1112 (2021)
   PUBMED   33602937
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 897)
  AUTHORS   Sakaue,S., Yamaguchi,E., Inoue,Y., Takahashi,M., Hirata,J.,
            Suzuki,K., Ito,S., Arai,T., Hirose,M., Tanino,Y., Nikaido,T.,
            Ichiwata,T., Ohkouchi,S., Hirano,T., Takada,T., Miyawaki,S.,
            Dofuku,S., Maeda,Y., Nii,T., Kishikawa,T., Ogawa,K., Masuda,T.,
            Yamamoto,K., Sonehara,K., Tazawa,R., Morimoto,K., Takaki,M.,
            Konno,S., Suzuki,M., Tomii,K., Nakagawa,A., Handa,T., Tanizawa,K.,
            Ishii,H., Ishida,M., Kato,T., Takeda,N., Yokomura,K., Matsui,T.,
            Watanabe,M., Inoue,H., Imaizumi,K., Goto,Y., Kida,H., Fujisawa,T.,
            Suda,T., Yamada,T., Satake,Y., Ibata,H., Hizawa,N., Mochizuki,H.,
            Kumanogoh,A., Matsuda,F., Nakata,K., Hirota,T., Tamari,M. and
            Okada,Y.
  TITLE     Genetic determinants of risk in autoimmune pulmonary alveolar
            proteinosis
  JOURNAL   Nat Commun 12 (1), 1032 (2021)
   PUBMED   33589587
  REMARK    GeneRIF: Genetic determinants of risk in autoimmune pulmonary
            alveolar proteinosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 897)
  AUTHORS   Schulte,V., Sipol,A., Burdach,S. and Rieger-Fackeldey,E.
  TITLE     The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns
  JOURNAL   Neonatology 118 (2), 187-193 (2021)
   PUBMED   33784678
  REMARK    GeneRIF: The Truncated Splice Variant of the
            Granulocyte-Macrophage-Colony-Stimulating Factor Receptor beta-
            Chain in Peripheral Blood Serves as Severity Biomarker of
            Respiratory Failure in Newborns.
REFERENCE   6  (residues 1 to 897)
  AUTHORS   Sakamaki,K., Miyajima,I., Kitamura,T. and Miyajima,A.
  TITLE     Critical cytoplasmic domains of the common beta subunit of the
            human GM-CSF, IL-3 and IL-5 receptors for growth signal
            transduction and tyrosine phosphorylation
  JOURNAL   EMBO J 11 (10), 3541-3549 (1992)
   PUBMED   1396555
REFERENCE   7  (residues 1 to 897)
  AUTHORS   Torigoe,T., O'Connor,R., Santoli,D. and Reed,J.C.
  TITLE     Interleukin-3 regulates the activity of the LYN protein-tyrosine
            kinase in myeloid-committed leukemic cell lines
  JOURNAL   Blood 80 (3), 617-624 (1992)
   PUBMED   1638019
REFERENCE   8  (residues 1 to 897)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   9  (residues 1 to 897)
  AUTHORS   Shen,Y., Baker,E., Callen,D.F., Sutherland,G.R., Willson,T.A.,
            Rakar,S. and Gough,N.M.
  TITLE     Localization of the human GM-CSF receptor beta chain gene (CSF2RB)
            to chromosome 22q12.2-->q13.1
  JOURNAL   Cytogenet Cell Genet 61 (3), 175-177 (1992)
   PUBMED   1424804
REFERENCE   10 (residues 1 to 897)
  AUTHORS   Hayashida,K., Kitamura,T., Gorman,D.M., Arai,K., Yokota,T. and
            Miyajima,A.
  TITLE     Molecular cloning of a second subunit of the receptor for human
            granulocyte-macrophage colony-stimulating factor (GM-CSF):
            reconstitution of a high-affinity GM-CSF receptor
  JOURNAL   Proc Natl Acad Sci U S A 87 (24), 9655-9659 (1990)
   PUBMED   1702217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL008637.1, BC070085.1 and
            AL133392.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the common beta chain
            of the high affinity receptor for IL-3, IL-5 and CSF. Defects in
            this gene have been reported to be associated with protein alveolar
            proteinosis (PAP). [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2969825.1,
                                           SRR14038194.2573355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403662.8/ ENSP00000384053.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..897
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..897
                     /product="cytokine receptor common subunit beta isoform 2
                     precursor"
                     /note="interleukin 3 receptor/granulocyte-macrophage
                     colony stimulating factor 3 receptor, beta (high
                     affinity); cytokine receptor common subunit beta;
                     GM-CSF/IL-3/IL-5 receptor common beta-chain;
                     colony-stimulating factor-2 receptor, beta, low-affinity;
                     colony stimulating factor 2 receptor, beta, low-affinity
                     (granulocyte-macrophage); GM-CSF/IL-3/IL-5 receptor common
                     beta subunit; beta common cytokine receptor; beta-GM-CSF
                     receptor; colony stimulating factor 2 receptor beta common
                     subunit"
                     /calculated_mol_wt=95707
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
                     /calculated_mol_wt=1647
     mat_peptide     17..897
                     /product="Cytokine receptor common subunit beta.
                     /id=PRO_0000010862"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
                     /calculated_mol_wt=95707
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          133..233
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(133,204,219)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16754968,
                     ECO:0000269|PubMed:18692472; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(226..227,229..230)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          247..>324
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cl21522"
                     /db_xref="CDD:473895"
     Region          341..436
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            346
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          425..429
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            order(425..426,428..429)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            444..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          474..482
                     /region_name="Box 1 motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          498..517
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          532..630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Region          <548..867
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          648..812
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P26955; propagated from
                     UniProtKB/Swiss-Prot (P32927.2)"
     Region          830..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32927.2)"
     CDS             1..897
                     /gene="CSF2RB"
                     /gene_synonym="betaGMR; CD131; CDw131; IL3RB; IL5RB;
                     SMDP5"
                     /coded_by="NM_000395.3:223..2916"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS13936.1"
                     /db_xref="GeneID:1439"
                     /db_xref="HGNC:HGNC:2436"
                     /db_xref="MIM:138981"
ORIGIN      
        1 mvlaqgllsm allalcwers lagaeetipl qtlrcyndyt shitcrwadt qdaqrlvnvt
       61 lirrvnedll epvscdlsdd mpwsacphpr cvprrcvipc qsfvvtdvdy fsfqpdrplg
      121 trltvtltqh vqppeprdlq istdqdhfll twsvalgspq shwlspgdle fevvykrlqd
      181 swedaaills ntsqatlgpe hlmpsstyva rvrtrlapgs rlsgrpskws pevcwdsqpg
      241 deaqpqnlec ffdgaavlsc swevrkevas svsfglfykp spdageeecs pvlreglgsl
      301 htrhhcqipv pdpathgqyi vsvqprraek hikssvniqm appslnvtkd gdsyslrwet
      361 mkmryehidh tfeiqyrkdt atwkdsktet lqnahsmalp alepstrywa rvrvrtsrtg
      421 yngiwsewse arswdtesvl pmwvlalivi fltiavllal rfcgiygyrl rrkweekipn
      481 pskshlfqng saelwppgsm saftsgspph qgpwgsrfpe legvfpvgfg dsevspltie
      541 dpkhvcdpps gpdttpaasd lpteqppspq pgppaashtp ekqassfdfn gpylgpphsr
      601 slpdilgqpe ppqeggsqks pppgsleylc lpaggqvqlv plaqamgpgq aveverrpsq
      661 gaagspsles gggpappalg prvggqdqkd spvaipmssg dtedpgvasg yvssadlvft
      721 pnsgassvsl vpslglpsdq tpslcpglas gppgapgpvk sgfegyvelp piegrsprsp
      781 rnnpvppeak spvlnpgerp advsptspqp egllvlqqvg dycflpglgp gplslrskps
      841 spgpgpeikn ldqafqvkkp pgqavpqvpv iqlfkalkqq dylslppwev nkpgevc
//
LOCUS       NP_001355636             148 aa            linear   PRI 20-NOV-2025
DEFINITION  core-binding factor subunit beta isoform 3 [Homo sapiens].
ACCESSION   NP_001355636 XP_006721384
VERSION     NP_001355636.1
DBSOURCE    REFSEQ: accession NM_001368707.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 148)
  AUTHORS   Samsa,W.E., Zhang,Z. and Gong,Z.
  TITLE     CBFbeta Regulates RUNX3 ADP-Ribosylation to Mediate Homologous
            Recombination Repair
  JOURNAL   J Cell Physiol 240 (1), e31503 (2025)
   PUBMED   39696918
REFERENCE   2  (residues 1 to 148)
  AUTHORS   Beyltjens,T., Boudin,E., Revencu,N., Boeckx,N., Bertrand,M.,
            Schutz,L., Haack,T.B., Weber,A., Biliouri,E., Vinksel,M.,
            Zagozen,A., Peterlin,B., Pai,S., Telegrafi,A., Henderson,L.B.,
            Ells,C., Turner,L., Wuyts,W., Van Hul,W., Hendrickx,G. and
            Mortier,G.R.
  TITLE     Heterozygous pathogenic variants involving CBFB cause a new
            skeletal disorder resembling cleidocranial dysplasia
  JOURNAL   J Med Genet 60 (5), 498-504 (2023)
   PUBMED   36241386
  REMARK    GeneRIF: Heterozygous pathogenic variants involving CBFB cause a
            new skeletal disorder resembling cleidocranial dysplasia.
REFERENCE   3  (residues 1 to 148)
  AUTHORS   Malik,N., Kim,Y.I., Yan,H., Tseng,Y.C., du Bois,W., Ayaz,G.,
            Tran,A.D., Vera-Ramirez,L., Yang,H., Michalowski,A.M., Kruhlak,M.,
            Lee,M., Hunter,K.W. and Huang,J.
  TITLE     Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1280-1298 (2023)
   PUBMED   36799863
  REMARK    GeneRIF: Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer.
REFERENCE   4  (residues 1 to 148)
  AUTHORS   Khan,A.S., Campbell,K.J., Cameron,E.R. and Blyth,K.
  TITLE     The RUNX/CBFbeta Complex in Breast Cancer: A Conundrum of Context
  JOURNAL   Cells 12 (4), 641 (2023)
   PUBMED   36831308
  REMARK    GeneRIF: The RUNX/CFBbeta Complex in Breast Cancer: A Conundrum of
            Context.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 148)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   6  (residues 1 to 148)
  AUTHORS   Chiba,N., Watanabe,T., Nomura,S., Tanaka,Y., Minowa,M., Niki,M.,
            Kanamaru,R. and Satake,M.
  TITLE     Differentiation dependent expression and distinct subcellular
            localization of the protooncogene product, PEBP2beta/CBFbeta, in
            muscle development
  JOURNAL   Oncogene 14 (21), 2543-2552 (1997)
   PUBMED   9191054
REFERENCE   7  (residues 1 to 148)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 148)
  AUTHORS   Liu,P., Seidel,N., Bodine,D., Speck,N., Tarle,S. and Collins,F.S.
  TITLE     Acute myeloid leukemia with Inv (16) produces a chimeric
            transcription factor with a myosin heavy chain tail
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 547-553 (1994)
   PUBMED   7587111
REFERENCE   9  (residues 1 to 148)
  AUTHORS   Liu,P., Tarle,S.A., Hajra,A., Claxton,D.F., Marlton,P.,
            Freedman,M., Siciliano,M.J. and Collins,F.S.
  TITLE     Fusion between transcription factor CBF beta/PEBP2 beta and a
            myosin heavy chain in acute myeloid leukemia
  JOURNAL   Science 261 (5124), 1041-1044 (1993)
   PUBMED   8351518
REFERENCE   10 (residues 1 to 148)
  AUTHORS   Muller,C.W. and Schulz,G.E.
  TITLE     Structure of the complex of adenylate kinase from Escherichia coli
            with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate
  JOURNAL   J Mol Biol 202 (4), 909-912 (1988)
   PUBMED   2845103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009084.9 and AC074143.5.
            
            On Feb 19, 2019 this sequence version replaced XP_006721384.1.
            
            Summary: The protein encoded by this gene is the beta subunit of a
            heterodimeric core-binding transcription factor belonging to the
            PEBP2/CBF transcription factor family which master-regulates a host
            of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis
            (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory
            subunit; it allosterically enhances DNA binding by alpha subunit as
            the complex binds to the core site of various enhancers and
            promoters, including murine leukemia virus, polyomavirus enhancer,
            T-cell receptor enhancers and GM-CSF promoters. Alternative
            splicing generates two mRNA variants, each encoding a distinct
            carboxyl terminus. In some cases, a pericentric inversion of
            chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript
            consisting of the N terminus of core-binding factor beta in a
            fusion with the C-terminal portion of the smooth muscle myosin
            heavy chain 11. This chromosomal rearrangement is associated with
            acute myeloid leukemia of the M4Eo subtype. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: Variants 3 and 4 encode isoforms that are the
            same length, but have distinct protein sequences.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.714144.1,
                                           SRR14038194.1831359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..148
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..148
                     /product="core-binding factor subunit beta isoform 3"
                     /note="SL3/AKV core-binding factor beta subunit;
                     polyomavirus enhancer binding protein 2, beta subunit;
                     SL3-3 enhancer factor 1 beta subunit; CBF-beta; PEA2-beta;
                     PEBP2-beta; SL3-3 enhancer factor 1 subunit beta"
                     /calculated_mol_wt=17463
     Region          1..128
                     /region_name="CBF_beta"
                     /note="Core binding factor beta subunit; pfam02312"
                     /db_xref="CDD:396750"
     CDS             1..148
                     /gene="CBFB"
                     /gene_synonym="CLCD2; PEBP2B"
                     /coded_by="NM_001368707.1:260..706"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:865"
                     /db_xref="HGNC:HGNC:1539"
                     /db_xref="MIM:121360"
ORIGIN      
        1 mprvvpdqrs kfeneeffrk lsreceikyt gfrdrpheer qarfqnacrd grseivylka
       61 pmilngvcvi wkgwidlqrl dgmgclefde eraqqedala qqafeearrr trefedrdrs
      121 hreemearrq qdpspgsnlg ggddlklr
//
LOCUS       NP_001340059             347 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-B-cell leukemia transcription factor 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001340059
VERSION     NP_001340059.1
DBSOURCE    REFSEQ: accession NM_001353130.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Huang,N., Zhang,H., Huang,Z., Wu,X., Zhang,N., Jiang,Y., Chen,C.
            and Zhuang,J.
  TITLE     Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant in a
            Chinese Family Causing Recurrent Neonatal Death
  JOURNAL   Birth Defects Res 116 (8), e2396 (2024)
   PUBMED   39189629
  REMARK    GeneRIF: Whole Exome Sequencing Revealing a Novel PBX1 Gene Variant
            in a Chinese Family Causing Recurrent Neonatal Death.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Choi,S.C., Park,Y.P., Roach,T., Jimenez,D., Fisher,A., Zadeh,M.,
            Ma,L., Sobel,E.S., Ge,Y., Mohamadzadeh,M. and Morel,L.
  TITLE     Lupus susceptibility gene Pbx1 controls the development, stability,
            and function of regulatory T cells via Rtkn2 expression
  JOURNAL   Sci Adv 10 (13), eadi4310 (2024)
   PUBMED   38536923
  REMARK    GeneRIF: Lupus susceptibility gene Pbx1 controls the development,
            stability, and function of regulatory T cells via Rtkn2 expression.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Kao,T.W., Chen,H.H., Lin,J., Wang,T.L. and Shen,Y.A.
  TITLE     PBX1 as a novel master regulator in cancer: Its regulation,
            molecular biology, and therapeutic applications
  JOURNAL   Biochim Biophys Acta Rev Cancer 1879 (2), 189085 (2024)
   PUBMED   38341110
  REMARK    GeneRIF: PBX1 as a novel master regulator in cancer: Its
            regulation, molecular biology, and therapeutic applications.
            Review article
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Zhang,L., Guo,H., Zhang,X., Wang,L., Wei,F., Zhao,Y., Wang,B.,
            Meng,Y. and Li,Y.
  TITLE     Small nucleolar RNA Snora73 promotes psoriasis progression by
            sponging miR-3074-5p and regulating PBX1 expression
  JOURNAL   Funct Integr Genomics 24 (1), 15 (2024)
   PUBMED   38240925
  REMARK    GeneRIF: Small nucleolar RNA Snora73 promotes psoriasis progression
            by sponging miR-3074-5p and regulating PBX1 expression.
            Erratum:[Funct Integr Genomics. 2024 Jan 30;24(1):21. doi:
            10.1007/s10142-024-01306-1. PMID: 38286903]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Lu,Q., Knoepfler,P.S., Scheele,J., Wright,D.D. and Kamps,M.P.
  TITLE     Both Pbx1 and E2A-Pbx1 bind the DNA motif ATCAATCAA cooperatively
            with the products of multiple murine Hox genes, some of which are
            themselves oncogenes
  JOURNAL   Mol Cell Biol 15 (7), 3786-3795 (1995)
   PUBMED   7791786
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Monica,K., Galili,N., Nourse,J., Saltman,D. and Cleary,M.L.
  TITLE     PBX2 and PBX3, new homeobox genes with extensive homology to the
            human proto-oncogene PBX1
  JOURNAL   Mol Cell Biol 11 (12), 6149-6157 (1991)
   PUBMED   1682799
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Kamps,M.P., Murre,C., Sun,X.H. and Baltimore,D.
  TITLE     A new homeobox gene contributes the DNA binding domain of the
            t(1;19) translocation protein in pre-B ALL
  JOURNAL   Cell 60 (4), 547-555 (1990)
   PUBMED   1967983
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Nourse,J., Mellentin,J.D., Galili,N., Wilkinson,J., Stanbridge,E.,
            Smith,S.D. and Cleary,M.L.
  TITLE     Chromosomal translocation t(1;19) results in synthesis of a
            homeobox fusion mRNA that codes for a potential chimeric
            transcription factor
  JOURNAL   Cell 60 (4), 535-545 (1990)
   PUBMED   1967982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291415.1, BC143435.1,
            AL359255.12 and AL390119.25.
            
            Summary: This gene encodes a nuclear protein that belongs to the
            PBX homeobox family of transcriptional factors. Studies in mice
            suggest that this gene may be involved in the regulation of
            osteogenesis and required for skeletal patterning and programming.
            A chromosomal translocation, t(1;19) involving this gene and
            TCF3/E2A gene, is associated with pre-B-cell acute lymphoblastic
            leukemia. The resulting fusion protein, in which the DNA binding
            domain of E2A is replaced by the DNA binding domain of this
            protein, transforms cells by constitutively activating
            transcription of genes regulated by the PBX protein family.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2017].
            
            Transcript Variant: This variant (4) lacks an exon in the 5' coding
            region and uses an alternate start codon, compared to variant 1.
            The encoded isoform (4) has a shorter and distinct N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143435.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..347
                     /product="pre-B-cell leukemia transcription factor 1
                     isoform 4"
                     /note="pre-B-cell leukemia transcription factor 1;
                     homeobox protein PRL; homeobox protein PBX1; pre-B-cell
                     leukemia homeobox 1"
                     /calculated_mol_wt=37624
     Region          <4..149
                     /region_name="PBC"
                     /note="PBC domain; pfam03792"
                     /db_xref="CDD:461052"
     Region          151..211
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(151..155,157,177,183,196,198..199,202..203,205..207,
                     209..210)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(153,156,199,202..203,206)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     CDS             1..347
                     /gene="PBX1"
                     /gene_synonym="CAKUHED"
                     /coded_by="NM_001353130.1:277..1320"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5087"
                     /db_xref="HGNC:HGNC:8632"
                     /db_xref="MIM:176310"
ORIGIN      
        1 mrrrpvlsir gaqeeeptdp qlmrldnmll aegvagpekg ggsaaaaaaa aasggagsdn
       61 svehsdyrak lsqirqiyht elekyeqacn eftthvmnll reqsrtrpis pkeiermvsi
      121 ihrkfssiqm qlkqstceav milrsrflda rrkrrnfnkq ateilneyfy shlsnpypse
      181 eakeelakkc gitvsqvsnw fgnkrirykk nigkfqeean iyaaktavta tnvsahgsqa
      241 nspstpnsag ssssfnmsns gdlfmsvqsl ngdsyqgaqv ganvqsqvdt lrhvisqtgg
      301 ysdglaasqm yspqgisang gwqdattpss vtsptegpgs vhsdtsn
//
LOCUS       NP_001048                398 aa            linear   PRI 20-NOV-2025
DEFINITION  substance-K receptor [Homo sapiens].
ACCESSION   NP_001048
VERSION     NP_001048.2
DBSOURCE    REFSEQ: accession NM_001057.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Madsen,J.J., Petersen,J.E., Christensen,D.P., Hansen,J.B.,
            Schwartz,T.W., Frimurer,T.M. and Olsen,O.H.
  TITLE     Deciphering specificity and cross-reactivity in tachykinin NK1 and
            NK2 receptors
  JOURNAL   J Biol Chem 299 (12), 105438 (2023)
   PUBMED   37944618
  REMARK    GeneRIF: Deciphering specificity and cross-reactivity in tachykinin
            NK1 and NK2 receptors.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Nguyen,L.P., Cho,M., Nguyen,T.U., Park,H.K., Nguyen,H.T.,
            Mykhailova,K., Hurh,S., Kim,H.R., Seong,J.Y., Lee,C.S., Ham,B.J.
            and Hwang,J.I.
  TITLE     Neurokinin-2 receptor negatively modulates substance P responses by
            forming complex with Neurokinin-1 receptor
  JOURNAL   Cell Biosci 13 (1), 212 (2023)
   PUBMED   37968728
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Xiang,H., Toyoshima,Y., Shen,W., Wang,X., Okada,N., Kii,S.,
            Sugiyama,K., Nagato,T., Kobayashi,H., Ikeo,K., Hashimoto,S.,
            Tanino,M., Taketomi,A. and Kitamura,H.
  TITLE     IFN-alpha/beta-mediated NK2R expression is related to the
            malignancy of colon cancer cells
  JOURNAL   Cancer Sci 113 (8), 2513-2525 (2022)
   PUBMED   35561088
  REMARK    GeneRIF: IFN-alpha/beta-mediated NK2R expression is related to the
            malignancy of colon cancer cells.
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Sun,W., Yuan,Q., Zhang,H., Yang,F., Ling,S., Luo,Y., Lv,P., Eric
            Xu,H., Tian,C., Yin,W. and Shi,P.
  TITLE     Structural insights into the activation of neurokinin 2 receptor by
            neurokinin A
  JOURNAL   Cell Discov 8 (1), 72 (2022)
   PUBMED   35882833
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Dai,L., Perera,D.S., Burcher,E. and Liu,L.
  TITLE     Hemokinin-1 and substance P stimulate production of inflammatory
            cytokines and chemokines in human colonic mucosa via both NK1 and
            NK2 tachykinin receptors
  JOURNAL   Neuropeptides 82, 102061 (2020)
   PUBMED   32600668
  REMARK    GeneRIF: Hemokinin-1 and substance P stimulate production of
            inflammatory cytokines and chemokines in human colonic mucosa via
            both NK1 and NK2 tachykinin receptors.
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Maggi,C.A., Giuliani,S., Patacchini,R., Santicioli,P.,
            Theodorsson,E., Barbanti,G., Turini,D. and Giachetti,A.
  TITLE     Tachykinin antagonists inhibit nerve-mediated contractions in the
            circular muscle of the human ileum. Involvement of neurokinin-2
            receptors
  JOURNAL   Gastroenterology 102 (1), 88-96 (1992)
   PUBMED   1370160
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Morten,J.E., Hopkins,B., Powell,S.J. and Graham,A.
  TITLE     Human NK-2 receptor gene maps to chromosome region 10q11-21
  JOURNAL   Hum Genet 88 (2), 200-203 (1991)
   PUBMED   1661704
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Graham,A., Hopkins,B., Powell,S.J., Danks,P. and Briggs,I.
  TITLE     Isolation and characterisation of the human lung NK-2 receptor gene
            using rapid amplification of cDNA ends
  JOURNAL   Biochem Biophys Res Commun 177 (1), 8-16 (1991)
   PUBMED   1710456
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Cyr,C., South,V., Saltzman,A., Felder,S., Ricca,G.A., Jaye,M.,
            Huebner,K., Kagan,J., Croce,C.M., Schlessinger,J. et al.
  TITLE     Cloning, expression of the human substance K receptor, and analysis
            of its role in mitogenesis
  JOURNAL   Ann N Y Acad Sci 632, 426-427 (1991)
   PUBMED   1659297
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Gerard,N.P. and Gerard,C.
  TITLE     Molecular cloning of the human neurokinin-2 receptor cDNA by
            polymerase chain reaction and isolation of the gene
  JOURNAL   Ann N Y Acad Sci 632, 389-390 (1991)
   PUBMED   1659296
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA929480.1, BC033742.1 and AC016821.9.
            
            On Sep 22, 2007 this sequence version replaced NP_001048.1.
            
            Summary: This gene belongs to a family of genes that function as
            receptors for tachykinins.  Receptor affinities are specified by
            variations in the 5'-end of the sequence.  The receptors belonging
            to this family are characterized by interactions with G proteins
            and 7 hydrophobic transmembrane regions.  This gene encodes the
            receptor for the tachykinin neuropeptide substance K, also referred
            to as neurokinin A. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291996.1, BC033742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373306.5/ ENSP00000362403.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..398
                     /product="substance-K receptor"
                     /note="neurokinin 2 receptor; neurokinin A receptor; NK-2
                     receptor; seven transmembrane helix receptor; NK-2R;
                     neurokinin B receptor"
                     /calculated_mol_wt=44311
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21452.3)"
     Site            19
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21452.3)"
     Site            33..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Region          34..318
                     /region_name="7tmA_SKR_NK2R"
                     /note="substance-K receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd16004"
                     /db_xref="CDD:320670"
     Region          35..61
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320670"
     Region          68..94
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320670"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Site            order(90,93..94,106..111,113..114,117,160,162..166,194,
                     197..199,201..203,205..206,263,266..267,269..270,273,
                     285..286,288..290,293,296..297)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320670"
     Region          106..136
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320670"
     Site            108..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Region          147..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320670"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Region          194..223
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320670"
     Site            197..218
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Region          243..273
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320670"
     Site            252..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     Region          286..311
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320670"
     Site            291..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P21452.3)"
     CDS             1..398
                     /gene="TACR2"
                     /gene_synonym="NK2R; NKNAR; SKR; TAC2R"
                     /coded_by="NM_001057.3:596..1792"
                     /db_xref="CCDS:CCDS7293.1"
                     /db_xref="GeneID:6865"
                     /db_xref="HGNC:HGNC:11527"
                     /db_xref="MIM:162321"
ORIGIN      
        1 mgtcdivtea nissgpesnt tgitafsmps wqlalwatay lalvlvavtg naiviwiila
       61 hrrmrtvtny fivnlaladl cmaafnaafn fvyashniwy fgrafcyfqn lfpitamfvs
      121 iysmtaiaad rymaivhpfq prlsapstka viagiwlval alaspqcfys tvtmdqgatk
      181 cvvawpedsg gktlllyhlv vialiyflpl avmfvaysvi gltlwrravp ghqahganlr
      241 hlqamkkfvk tmvlvvltfa icwlpyhlyf ilgsfqediy chkfiqqvyl alfwlamsst
      301 mynpiiyccl nhrfrsgfrl afrccpwvtp tkedkleltp ttslstrvnr chtketlfma
      361 gdtapseats geagrpqdgs glwfgyglla ptkthvei
//
LOCUS       NP_001091886             954 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 7 isoform d [Homo sapiens].
ACCESSION   NP_001091886
VERSION     NP_001091886.1
DBSOURCE    REFSEQ: accession NM_001098416.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 954)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 954)
  AUTHORS   Maciejewski,K., Giers,M., Oleksiewicz,U. and Czerwinska,P.
  TITLE     The Epigenetic Modifiers HDAC2 and HDAC7 Inversely Associate with
            Cancer Stemness and Immunity in Solid Tumors
  JOURNAL   Int J Mol Sci 25 (14), 7841 (2024)
   PUBMED   39063083
  REMARK    GeneRIF: The Epigenetic Modifiers HDAC2 and HDAC7 Inversely
            Associate with Cancer Stemness and Immunity in Solid Tumors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 954)
  AUTHORS   Lu,W., Zhuang,G., Guan,Y., Li,Y., Liu,L. and Xiao,M.
  TITLE     Comprehensive analysis of HDAC7 expression and its prognostic value
            in diffuse large B cell lymphoma: A review
  JOURNAL   Medicine (Baltimore) 102 (45), e34577 (2023)
   PUBMED   37960766
  REMARK    GeneRIF: Comprehensive analysis of HDAC7 expression and its
            prognostic value in diffuse large B cell lymphoma: A review.
            Review article
REFERENCE   4  (residues 1 to 954)
  AUTHORS   Qin,X., Long,Y., Bai,X., Cao,L., Yan,H., Zhang,K., Wang,B. and
            Wu,X.
  TITLE     The disordered C terminus of ALKBH5 promotes phase separation and
            paraspeckles assembly
  JOURNAL   J Biol Chem 299 (8), 105071 (2023)
   PUBMED   37474102
REFERENCE   5  (residues 1 to 954)
  AUTHORS   Ling,S., Chen,T., Wang,S., Zhang,W., Zhou,R., Xia,X., Yao,Z.,
            Fan,Y., Ning,S., Liu,J., Qin,L., Tucker,H.O., Wang,N. and Guo,X.
  TITLE     Deacetylation of FOXP1 by HDAC7 potentiates self-renewal of
            mesenchymal stem cells
  JOURNAL   Stem Cell Res Ther 14 (1), 188 (2023)
   PUBMED   37507770
  REMARK    GeneRIF: Deacetylation of FOXP1 by HDAC7 potentiates self-renewal
            of mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 954)
  AUTHORS   Lemercier,C., Brocard,M.P., Puvion-Dutilleul,F., Kao,H.Y.,
            Albagli,O. and Khochbin,S.
  TITLE     Class II histone deacetylases are directly recruited by BCL6
            transcriptional repressor
  JOURNAL   J Biol Chem 277 (24), 22045-22052 (2002)
   PUBMED   11929873
  REMARK    GeneRIF: Class II histone deacetylases are directly recruited by
            BCL6 transcriptional repressor
REFERENCE   7  (residues 1 to 954)
  AUTHORS   Fischle,W., Dequiedt,F., Fillion,M., Hendzel,M.J., Voelter,W. and
            Verdin,E.
  TITLE     Human HDAC7 histone deacetylase activity is associated with HDAC3
            in vivo
  JOURNAL   J Biol Chem 276 (38), 35826-35835 (2001)
   PUBMED   11466315
REFERENCE   8  (residues 1 to 954)
  AUTHORS   Lee,H.J., Chun,M. and Kandror,K.V.
  TITLE     Tip60 and HDAC7 interact with the endothelin receptor a and may be
            involved in downstream signaling
  JOURNAL   J Biol Chem 276 (20), 16597-16600 (2001)
   PUBMED   11262386
REFERENCE   9  (residues 1 to 954)
  AUTHORS   Marks,P.A., Richon,V.M. and Rifkind,R.A.
  TITLE     Histone deacetylase inhibitors: inducers of differentiation or
            apoptosis of transformed cells
  JOURNAL   J Natl Cancer Inst 92 (15), 1210-1216 (2000)
   PUBMED   10922406
  REMARK    Review article
REFERENCE   10 (residues 1 to 954)
  AUTHORS   Kao,H.Y., Downes,M., Ordentlich,P. and Evans,R.M.
  TITLE     Isolation of a novel histone deacetylase reveals that class I and
            class II deacetylases promote SMRT-mediated repression
  JOURNAL   Genes Dev 14 (1), 55-66 (2000)
   PUBMED   10640276
  REMARK    GeneRIF: Characterization of the mouse HDAC7 ortholog.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC376749.1, BC064840.1 and
            BC020505.2.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene has sequence homology to members of the histone
            deacetylase family. This gene is orthologous to mouse HDAC7 gene
            whose protein promotes repression mediated via the transcriptional
            corepressor SMRT. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the mid-coding region, compared to variant 1. The resulting
            isoform (d) has the same N- and C-termini but is shorter than
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064840.1, AY321367.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..954
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..954
                     /product="histone deacetylase 7 isoform d"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase 7A; protein deacetylase HDAC7"
                     /calculated_mol_wt=102775
     Region          520..897
                     /region_name="HDAC7"
                     /note="Histone deacetylase 7; cd10008"
                     /db_xref="CDD:212532"
     Site            order(544,628,671..672,680..681,709,711,740,803,811..812,
                     843)
                     /site_type="active"
                     /db_xref="CDD:212532"
     CDS             1..954
                     /gene="HDAC7"
                     /gene_synonym="HD7; HD7A; HDAC7A"
                     /coded_by="NM_001098416.4:119..2983"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS41776.1"
                     /db_xref="GeneID:51564"
                     /db_xref="HGNC:HGNC:14067"
                     /db_xref="MIM:606542"
ORIGIN      
        1 mhspgadgtq vspgahycsp tgagcprpca dtpgpqpqpm dlrvgqrppv epppeptlla
       61 lqrpqrlhhh lflaglqqqr svepmrlsmd tpmpelqvgp qeqelrqllh kdkskrsava
      121 ssvvkqklae vilkkqqaal ertvhpnspg ipyrtleple tegatrsmls sflppvpslp
      181 sdppehfplr ktvsepnlkl rykpkksler rknpllrkes appslrrrpa etlgdsspss
      241 sstpasgcss pndsehgpnp ilgseadsdr rthptlgprg pilgsphtpl flphglepea
      301 ggtlpsrlqp illldpsgsh aplltvpglg plpfhfaqsl mtterlsgsg lhwplsrtrs
      361 eplppsatap pppgpmqprl eqlkthvqvi krsakpsekp rlrqipsaed letdgggpgq
      421 vvddglehre lghgqpearg paplqqhpqv llweqqrlag rlprgstgdt vllplaqggh
      481 rplsraqssp aapaslsape pasqarvlss setpartlpf ttgliydsvm lkhqcscgdn
      541 srhpehagri qsiwsrlqer glrsqceclr grkasleelq svhserhvll ygtnplsrlk
      601 ldngklagll aqrmfvmlpc ggvgvdtdti wnelhssnaa rwaagsvtdl afkvasrelk
      661 ngfavvrppg hhadhstamg fcffnsvaia crqlqqqska skilivdwdv hhgngtqqtf
      721 yqdpsvlyis lhrhddgnff pgsgavdevg agsgegfnvn vawaggldpp mgdpeylaaf
      781 rivvmpiare fspdlvlvsa gfdaaeghpa plggyhvsak cfgymtqqlm nlaggavvla
      841 legghdltai cdaseacvaa llgnrvdpls eegwkqkpnl nairsleavi rvhskywgcm
      901 qrlascpdsw vprvpgadke eveavtalas lsvgilaedr pseqlveeee pmnl
//
LOCUS       NP_742081                449 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 8 [Homo sapiens].
ACCESSION   NP_742081
VERSION     NP_742081.1
DBSOURCE    REFSEQ: accession NM_172084.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Borghi,R., Trivisano,M., Specchio,N., Tartaglia,M. and
            Compagnucci,C.
  TITLE     Understanding the pathogenetic mechanisms underlying altered
            neuronal function associated with CAMK2B mutations
  JOURNAL   Neurosci Biobehav Rev 152, 105299 (2023)
   PUBMED   37391113
  REMARK    GeneRIF: Understanding the pathogenetic mechanisms underlying
            altered neuronal function associated with CAMK2B mutations.
            Review article
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Nicole,O. and Pacary,E.
  TITLE     CaMKIIbeta in Neuronal Development and Plasticity: An Emerging
            Candidate in Brain Diseases
  JOURNAL   Int J Mol Sci 21 (19), 7272 (2020)
   PUBMED   33019657
  REMARK    GeneRIF: CaMKIIbeta in Neuronal Development and Plasticity: An
            Emerging Candidate in Brain Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Penades,J.R., Bernal,D., Revert,F., Johansson,C., Fresquet,V.J.,
            Cervera,J., Wieslander,J., Quinones,S. and Saus,J.
  TITLE     Characterization and expression of multiple alternatively spliced
            transcripts of the Goodpasture antigen gene region. Goodpasture
            antibodies recognize recombinant proteins representing the
            autoantigen and one of its alternative forms
  JOURNAL   Eur J Biochem 229 (3), 754-760 (1995)
   PUBMED   7758473
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Schworer,C.M., Colbran,R.J., Keefer,J.R. and Soderling,T.R.
  TITLE     Ca2+/calmodulin-dependent protein kinase II. Identification of a
            regulatory autophosphorylation site adjacent to the inhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 263 (27), 13486-13489 (1988)
   PUBMED   3417668
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550751.1, BX445032.2,
            AK290148.1, DB566810.1 and AC006454.4.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a beta chain.
            It is possible that distinct isoforms of this chain have different
            cellular localizations and interact differently with calmodulin.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (8), also known as beta 7, lacks
            an in-frame segment of the coding region, compared to variant 1. It
            encodes a shorter isoform (8), also known as beta 7 subunit, that
            is missing an internal segment compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF140350.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..449
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 8"
                     /EC_number="2.7.11.17"
                     /note="CaM kinase II beta subunit; CaM-kinase II beta
                     chain; proline rich calmodulin-dependent protein kinase;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit beta; caMK-II subunit beta"
                     /calculated_mol_wt=50824
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          291..301
                     /region_name="calmodulin-binding domain"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          317..444
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..449
                     /gene="CAMK2B"
                     /gene_synonym="CAM2; CAMK2; CAMKB; CaMKIIbeta; MRD54"
                     /coded_by="NM_172084.3:174..1523"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS5489.1"
                     /db_xref="GeneID:816"
                     /db_xref="HGNC:HGNC:1461"
                     /db_xref="MIM:607707"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsarkqe iiktteqlie avnngdfeay akicdpglts fepealgnlv
      361 egmdfhrfyf enllaknskp ihttilnphv hvigedaaci ayirltqyid gqgrprtsqs
      421 eetrvwhrrd gkwqnvhfhc sgapvaplq
//
LOCUS       NP_001185922             446 aa            linear   PRI 20-NOV-2025
DEFINITION  NAD kinase isoform 1 [Homo sapiens].
ACCESSION   NP_001185922
VERSION     NP_001185922.1
DBSOURCE    REFSEQ: accession NM_001198993.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Praharaj,P.P., Li,Y., Mary,C., Soflaee,M.H., Ryu,K., Kim,D.,
            Tran,D.H., Dey,T., Tom,H.J., Rion,H., Gelin,M., Lemoff,A.,
            Zacharias,L.G., Patricio,J.S., Mathews,T.P., Chen,Z., Lionne,C.,
            Hoxhaj,G. and Labesse,G.
  TITLE     Cryo-EM structure and regulation of human NAD kinase
  JOURNAL   Sci Adv 11 (4), eads2664 (2025)
   PUBMED   39854463
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Meng,X., Peng,F., Yu,S., Chi,X., Wang,W. and Shao,S.
  TITLE     Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1 axis
  JOURNAL   J Cancer Res Clin Oncol 150 (5), 228 (2024)
   PUBMED   38700533
  REMARK    GeneRIF: Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1
            axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wu,T., Ding,K., Wang,C., Lin,G., Xie,C., Chen,X., Li,Q., Yu,F.,
            Mao,Y., Hong,W., Lu,L. and Li,S.
  TITLE     G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation
  JOURNAL   FASEB J 38 (3), e23449 (2024)
   PUBMED   38315451
  REMARK    GeneRIF: G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Magni,G., Amici,A., Emanuelli,M., Orsomando,G., Raffaelli,N. and
            Ruggieri,S.
  TITLE     Enzymology of NAD+ homeostasis in man
  JOURNAL   Cell Mol Life Sci 61 (1), 19-34 (2004)
   PUBMED   14704851
  REMARK    Review article
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Lerner,F., Niere,M., Ludwig,A. and Ziegler,M.
  TITLE     Structural and functional characterization of human NAD kinase
  JOURNAL   Biochem Biophys Res Commun 288 (1), 69-74 (2001)
   PUBMED   11594753
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN349189.1, BC001709.1, BC024219.1, AL031282.1 and BM842058.1.
            
            Summary: NADK catalyzes the transfer of a phosphate group from ATP
            to NAD to generate NADP, which in its reduced form acts as an
            electron donor for biosynthetic reactions (Lerner et al., 2001
            [PubMed 11594753]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) has an alternate 5' UTR
            compared to variant 1. Variants 1, 2 and 5 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001709.1, AK291599.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..446
                     /product="NAD kinase isoform 1"
                     /EC_number="2.7.1.23"
                     /note="poly(P)/ATP NAD kinase"
                     /calculated_mol_wt=49097
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Region          <96..433
                     /region_name="pnk"
                     /note="bifunctional NADP phosphatase/NAD kinase; cl28462"
                     /db_xref="CDD:333282"
     CDS             1..446
                     /gene="NADK"
                     /gene_synonym="dJ283E3.1; NADK1"
                     /coded_by="NM_001198993.2:112..1452"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30565.1"
                     /db_xref="GeneID:65220"
                     /db_xref="HGNC:HGNC:29831"
                     /db_xref="MIM:611616"
ORIGIN      
        1 memeqekmtm nkelspdaaa yccsachgde twsynhpirg raksrslsas palgstkefr
       61 rtrslhgpcp vttfgpkacv lqnpqtimhi qdpasqrltw nkspksvlvi kkmrdasllq
      121 pfkelcthlm eenmivyvek kvledpaias desfgavkkk fctfredydd isnqidfiic
      181 lggdgtllya sslfqgsvpp vmafhlgslg fltpfsfenf qsqvtqvieg naavvlrsrl
      241 kvrvvkelrg kktavhnglg engsqaagld mdvgkqamqy qvlnevvidr gpssylsnvd
      301 vyldghlitt vqgdgvivst ptgstayaaa agasmihpnv paimitpicp hslsfrpivv
      361 pagvelkiml spearntawv sfdgrkrqei rhgdsisitt scyplpsicv rdpvsdwfes
      421 laqclhwnvr kkqahfeeee eeeeeg
//
LOCUS       NP_001161710            1058 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform h [Homo sapiens].
ACCESSION   NP_001161710
VERSION     NP_001161710.1
DBSOURCE    REFSEQ: accession NM_001168238.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1058)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1058)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1058)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1058)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1058)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1058)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1058)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512326.25, FJ542286.1,
            AL139132.16 and BQ014912.1.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (h) lacks an alternate in-frame
            exon in the 5' coding region and an alternate in-frame segment in
            the 3' coding region, compared to variant b, resulting in an
            isoform (h, also known as 1BSCTS) that is shorter than isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4547031.1, FJ542286.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1058
                     /product="tyrosine-protein kinase ABL2 isoform h"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=115687
     Region          90..143
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(95,97,100..102,104,119,123..124,135,137,139..140)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            order(99..102,121,123)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Region          148..241
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            order(159,187,200)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Region          260..522
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(273,275..277,294,296,341,343,347,395,406,424..426,
                     428,436,470,474)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(273,275,278,294,296,311,315,324,340..341,343,347,
                     395,405..406)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            order(288..289,319..321,325,367,399..400,518..519)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(365..366,369,454,457..458,487..488)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            405..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Site            order(424..426,428,436,470,474)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Region          939..1058
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1058
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_001168238.2:281..3457"
                     /note="isoform h is encoded by transcript variant h"
                     /db_xref="CCDS:CCDS53437.1"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mgqqvgrvge apglqqpqpr girgssaarp sgrrrdpagr ttetgfnift qhealhrpyg
       61 cdvepqalne airwsskenl lgatesdpnl fvalydfvas gdntlsitkg eklrvlgynq
      121 ngewsevrsk ngqgwvpsny itpvnslekh swyhgpvsrs aaeyllssli ngsflvrese
      181 sspgqlsisl ryegrvyhyr inttadgkvy vtaesrfstl aelvhhhstv adglvttlhy
      241 papkcnkptv ygvspihdkw emertditmk hklgggqyge vyvgvwkkys ltvavktlke
      301 dtmeveeflk eaavmkeikh pnlvqllgvc tleppfyivt eympygnlld ylrecnreev
      361 tavvllymat qissameyle kknfihrdla arnclvgenh vvkvadfgls rlmtgdtyta
      421 hagakfpikw tapeslaynt fsiksdvwaf gvllweiaty gmspypgidl sqvydllekg
      481 yrmeqpegcp pkvyelmrac wkwspadrps faethqafet mfhdssisee vaeelgraas
      541 sssvvpylpr lpilpsktrt lkkqvenken iegaqdaten sasslapgfi rgaqassgsp
      601 alprkqrdks psslledake tcftrdrkgg ffssfmkkrn aptppkrsss fremenqphk
      661 kyeltglpeq drmamtlprn cqrsklqler tvstssqpee nvdrandmlp kkseesaaps
      721 rerpkakllp rgatalplrt psgdlaitek dppgvgvagv aaapkgkekn ggarlgmagv
      781 pedgeqpgwp spakaapvlp tthnhkvpvl isptlkhtpa dvqligtdsq gnkfkllseh
      841 qvtssgdkdr prrvkpkcap ppppvmrllq hpsicsdpte eptaltagqs tsetqeggkk
      901 aalgavpisg kagrpvmppp qvplptssis pakmangtag tkvalrktkq aaekisadki
      961 skeallecad llssaltepv pnsqlvdtgh qlldycsgyv dcipqtrnkf afreavskle
     1021 lslqelqvss aaagvpgtnp vlnnllscvq eisdvvqr
//
LOCUS       NP_001007075             135 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL32 [Homo sapiens].
ACCESSION   NP_001007075
VERSION     NP_001007075.1
DBSOURCE    REFSEQ: accession NM_001007074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Xu,L., Wang,L., Jiang,C., Zhu,Q., Chen,R., Wang,J. and Wang,S.
  TITLE     Biological effect of ribosomal protein L32 on human breast cancer
            cell behavior
  JOURNAL   Mol Med Rep 22 (3), 2478-2486 (2020)
   PUBMED   32705264
  REMARK    GeneRIF: Biological effect of ribosomal protein L32 on human breast
            cancer cell behavior.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Vorobieva,N.V., Filipenko,M.L., Karpova,G.G., Mertvetsov,N.P. and
            Graphodatsky,A.S.
  TITLE     Assignment of the L32 ribosomal protein gene (RPL32) to human
            chromosome 3q13.3-->q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 190-191 (1997)
   PUBMED   9284913
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Young,J.A. and Trowsdale,J.
  TITLE     A processed pseudogene in an intron of the HLA-DP beta 1 chain gene
            is a member of the ribosomal protein L32 gene family
  JOURNAL   Nucleic Acids Res 13 (24), 8883-8891 (1985)
   PUBMED   3866218
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF960792.1, BC070209.1,
            AC034198.7 and CA436299.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L32E family of ribosomal proteins. It is located in the
            cytoplasm. Although some studies have mapped this gene to
            3q13.3-q21, it is believed to map to 3p25-p24. As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome.
            Alternatively spliced transcript variants encoding the same protein
            have been observed for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks a 5' exon but has an
            alternate segment in the 5' UTR, compared to variant 1. Variants 1,
            2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CV393038.1, SRR1803611.305830.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.2"
     Protein         1..135
                     /product="large ribosomal subunit protein eL32"
                     /note="60S ribosomal protein L32"
                     /calculated_mol_wt=15729
     Region          17..124
                     /region_name="Ribosomal_L32e"
                     /note="Ribosomal protein L32; pfam01655"
                     /db_xref="CDD:460283"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62910.2)"
     CDS             1..135
                     /gene="RPL32"
                     /gene_synonym="eL32; L32; PP9932"
                     /coded_by="NM_001007074.1:214..621"
                     /db_xref="CCDS:CCDS2614.1"
                     /db_xref="GeneID:6161"
                     /db_xref="HGNC:HGNC:10336"
ORIGIN      
        1 maalrplvkp kivkkrtkkf irhqsdryvk ikrnwrkprg idnrvrrrfk gqilmpnigy
       61 gsnkktkhml psgfrkflvh nvkelevllm cnksycaeia hnvssknrka iveraaqlai
      121 rvtnpnarlr seene
//
LOCUS       NP_001333430             291 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001333430
VERSION     NP_001333430.1
DBSOURCE    REFSEQ: accession NM_001346501.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Comeau,D., Belliveau,J., Bouhamdani,N. and Amor,M.B.
  TITLE     Expanding the phenotypic spectrum for CDK8-related disease: A case
            report
  JOURNAL   Am J Med Genet A 194 (5), e63537 (2024)
   PUBMED   38193604
  REMARK    GeneRIF: Expanding the phenotypic spectrum for CDK8-related
            disease: A case report.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Choi,H.Y., Zhu,Y., Zhao,X., Mehta,S., Hernandez,J.C., Lee,J.J.,
            Kou,Y., Machida,R., Giacca,M., Del Sal,G., Ray,R., Eoh,H.,
            Tahara,S.M., Chen,L., Tsukamoto,H. and Machida,K.
  TITLE     NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells
  JOURNAL   Exp Mol Med 56 (2), 461-477 (2024)
   PUBMED   38409448
  REMARK    GeneRIF: NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells.
            Erratum:[Exp Mol Med. 2024 Oct;56(10):2323. doi:
            10.1038/s12276-024-01325-9. PMID: 39465353]
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Chen,M., Li,J., Zhang,L., Wang,L., Cheng,C., Ji,H., Altilia,S.,
            Ding,X., Cai,G., Altomare,D., Shtutman,M., Byrum,S.D.,
            Mackintosh,S.G., Feoktistov,A., Soshnikova,N., Mogila,V.A.,
            Tatarskiy,V., Erokhin,M., Chetverina,D., Prawira,A., Ni,Y.,
            Urban,S., McInnes,C., Broude,E.V. and Roninson,I.B.
  TITLE     CDK8 and CDK19: positive regulators of signal-induced transcription
            and negative regulators of Mediator complex proteins
  JOURNAL   Nucleic Acids Res 51 (14), 7288-7313 (2023)
   PUBMED   37378433
  REMARK    GeneRIF: CDK8 and CDK19: positive regulators of signal-induced
            transcription and negative regulators of Mediator complex proteins.
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Rzymski,T., Mikula,M., Wiklik,K. and Brzozka,K.
  TITLE     CDK8 kinase--An emerging target in targeted cancer therapy
  JOURNAL   Biochim Biophys Acta 1854 (10 Pt B), 1617-1629 (2015)
   PUBMED   26006748
  REMARK    GeneRIF: Current state of the art confirms that further development
            of CDK8 inhibitors will translate into targeted therapies in
            oncology
            Review article
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Nemet,J., Jelicic,B., Rubelj,I. and Sopta,M.
  TITLE     The two faces of Cdk8, a positive/negative regulator of
            transcription
  JOURNAL   Biochimie 97, 22-27 (2014)
   PUBMED   24139904
  REMARK    GeneRIF: CDK8 regulates the transcription factors turnover,
            C-terminal domain phosphorylation, and regulates the activator or
            repressor functions. (Review)
            Review article
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cujec,T.P., Cho,H., Maldonado,E., Meyer,J., Reinberg,D. and
            Peterlin,B.M.
  TITLE     The human immunodeficiency virus transactivator Tat interacts with
            the RNA polymerase II holoenzyme
  JOURNAL   Mol Cell Biol 17 (4), 1817-1823 (1997)
   PUBMED   9121429
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Rickert,P., Seghezzi,W., Shanahan,F., Cho,H. and Lees,E.
  TITLE     Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase
            II
  JOURNAL   Oncogene 12 (12), 2631-2640 (1996)
   PUBMED   8700522
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Tassan,J.P., Jaquenoud,M., Leopold,P., Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of human cyclin-dependent kinase 8, a putative
            protein kinase partner for cyclin C
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8871-8875 (1995)
   PUBMED   7568034
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094784.1 and BM021938.1.
            
            Summary: This gene encodes a member of the cyclin-dependent protein
            kinase (CDK) family. CDK family members are known to be important
            regulators of cell cycle progression. This kinase and its
            regulatory subunit, cyclin C, are components of the Mediator
            transcriptional regulatory complex, involved in both
            transcriptional activation and repression by phosphorylation of the
            carboxy-terminal domain of the largest subunit of RNA polymerase
            II. This kinase regulates transcription by targeting the
            cyclin-dependent kinase 7 subunits of the general transcription
            initiation factor IIH, thus providing a link between the Mediator
            complex and the basal transcription machinery. Multiple pseudogenes
            of this gene have been identified. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (3) lacks an exon in the 5' region
            and uses a downstream start codon, compared to variant 1. It
            encodes isoform 3 which has a shorter N-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094784.1, SRR3476690.890251.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..291
                     /product="cyclin-dependent kinase 8 isoform 3"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="CDK8 protein kinase; protein kinase K35; cell
                     division protein kinase 8; mediator complex subunit CDK8;
                     mediator of RNA polymerase II transcription subunit CDK8"
                     /calculated_mol_wt=33070
     Region          <1..162
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..291
                     /gene="CDK8"
                     /gene_synonym="IDDHBA; K35"
                     /coded_by="NM_001346501.2:975..1850"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:1024"
                     /db_xref="HGNC:HGNC:1779"
                     /db_xref="MIM:603184"
ORIGIN      
        1 mgfarlfnsp lkpladldpv vvtfwyrape lllgarhytk aidiwaigci faelltsepi
       61 fhcrqedikt snpyhhdqld rifnvmgfpa dkdwedikkm pehstlmkdf rrntytncsl
      121 ikymekhkvk pdskafhllq klltmdpikr itseqamqdp yfledplpts dvfagcqipy
      181 pkreflteee pddkgdkknq qqqqgnnhtn gtghpgnqds shtqgpplkk vrvvppttts
      241 gglimtsdyq rsnphaaypn pgpstsqpqs smgysatsqq ppqyshqthr y
//
LOCUS       NP_001355927             342 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform a [Homo sapiens].
ACCESSION   NP_001355927 XP_006716854
VERSION     NP_001355927.1
DBSOURCE    REFSEQ: accession NM_001368998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_006716854.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.610310.1,
                                           SRR1803613.181256.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..342
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=38973
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          283..342
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..342
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368998.1:118..1146"
                     /note="isoform a is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS47956.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qaviemvqea
      301 grvtvrdgmp ellklplrch ecqqllpsip qlkehlrkhw tq
//
LOCUS       NP_001308745             629 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform m [Homo sapiens].
ACCESSION   NP_001308745
VERSION     NP_001308745.1
DBSOURCE    REFSEQ: accession NM_001321816.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.54950.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..629
                     /product="E3 ubiquitin-protein ligase CBL-B isoform m"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=69076
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          578..618
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(580..581,583..585,587..588,593,597)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..629
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321816.2:915..2804"
                     /note="isoform m is encoded by transcript variant 19"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikscdng hcmlngthgp ssekksnipd lsiylkgeda fdalppslpp pppparhsli
      481 ehskppgsss rpssgqdlfl lpsdpfvdla sgqvplppar rlpgenvktn rtsqdydqlp
      541 scsdgsqapa rppkprprrt apeihhrkph gpeaalenvd akiaklmgeg yafeevkral
      601 eiaqnnveva rsilrefafp ppvsprlnl
//
LOCUS       NP_055452                333 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial fission regulator 1 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_055452
VERSION     NP_055452.3
DBSOURCE    REFSEQ: accession NM_014637.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Li,Q.Y., Guo,Q., Luo,W.M., Luo,X.Y., Ji,Y.M., Xu,L.Q., Guo,J.L.,
            Shi,R.S., Li,F., Lin,C.Y., Zhang,J. and Ke,D.
  TITLE     Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma
  JOURNAL   Aging (Albany NY) 16 (1), 66-88 (2024)
   PUBMED   38170222
  REMARK    GeneRIF: Overexpression of MTFR1 promotes cancer progression and
            drug-resistance on cisplatin and is related to the immune
            microenvironment in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Chen,P., Zhong,J., Ye,J., He,Y., Liang,Z., Cheng,Y., Zheng,J.,
            Chen,H. and Chen,C.
  TITLE     miR-324-5p protects against oxidative stress-induced endothelial
            progenitor cell injury by targeting Mtfr1
  JOURNAL   J Cell Physiol 234 (12), 22082-22092 (2019)
   PUBMED   31066044
  REMARK    GeneRIF: Our results suggested that miR-324-5p protects against
            oxidative stress-induced endothelial progenitor cells injury by
            regulating Mtfr1.
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Monticone,M., Tonachini,L., Tavella,S., Degan,P., Biticchi,R.,
            Palombi,F., Puglisi,R., Boitani,C., Cancedda,R. and Castagnola,P.
  TITLE     Impaired expression of genes coding for reactive oxygen species
            scavenging enzymes in testes of Mtfr1/Chppr-deficient mice
  JOURNAL   Reproduction 134 (3), 483-492 (2007)
   PUBMED   17709566
  REMARK    GeneRIF: reports the role of mouse Mtfr1 in protecting cells from
            reactive oxygen species using Mtfr1-deficient mice.
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Puri,C., Tacchetti,C., Pinton,P.,
            Rizzuto,R., Cancedda,R., Tavella,S. and Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region (CHPPR) is a novel
            mitochondrial protein and promotes mitochondrial fission
  JOURNAL   J Cell Physiol 201 (3), 470-482 (2004)
   PUBMED   15389597
  REMARK    GeneRIF: reports full-length mRNA sequence of human MTFR1.
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Tonachini,L., Monticone,M., Di Marco,E., Zerega,B., Cancedda,R. and
            Castagnola,P.
  TITLE     Chondrocyte protein with a poly-proline region is a novel protein
            expressed by chondrocytes in vitro and in vivo
  JOURNAL   Biochim Biophys Acta 1577 (3), 421-429 (2002)
   PUBMED   12359332
  REMARK    GeneRIF: presents partial sequence of a human homolog of chicken
            MTFR1
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055822.10, BC036116.1 and
            AW157714.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 14, 2009 this sequence version replaced NP_055452.2.
            
            Summary: This gene encodes a mitochondrial protein that is
            characterized by a poly-proline rich region. A chicken homolog of
            this protein promotes mitochondrial fission and the mouse homolog
            protects cells from oxidative stress. A related pseudogene of this
            gene is found on chromosome X. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043498.2, BC036116.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000262146.9/
                                                  ENSP00000262146.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1"
     Protein         1..333
                     /product="mitochondrial fission regulator 1 isoform 1
                     precursor"
                     /note="chondrocyte protein with a poly-proline region"
                     /calculated_mol_wt=31469
     transit_peptide 1..48
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=5550
     Region          22..251
                     /region_name="Mito_fiss_reg"
                     /note="Mitochondrial fission regulator; pfam05308"
                     /db_xref="CDD:461620"
     mat_peptide     49..333
                     /product="Mitochondrial fission regulator 1.
                     /id=PRO_0000096622"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
                     /calculated_mol_wt=31469
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15390.2)"
     Region          177..198
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          179..304
                     /region_name="Necessary and sufficient to promote
                     mitochondrial fission. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     Region          288..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15390.2)"
     CDS             1..333
                     /gene="MTFR1"
                     /gene_synonym="CHPPR; FAM54A2"
                     /coded_by="NM_014637.4:132..1133"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6182.1"
                     /db_xref="GeneID:9650"
                     /db_xref="HGNC:HGNC:29510"
                     /db_xref="MIM:619414"
ORIGIN      
        1 mlgwikrlir mvfqqvgvsm qsvlwsrkpy gssrsivrki gtnlsliqcp rvqfqinsha
       61 tewspshpge davasfadvg wvakeegecs arlrtevrsr pplqddllff ekapsrqisl
      121 pdlsqeepql ktpalaneea lqkicalene laalraqiak ivtqqeqqnl tagdldsttf
      181 gtipphpppp ppplpppalg lhqstsavdl ikerrekran agktlvknnp kkpempnmle
      241 ilkemnsvkl rsvkrseqdv kpkpvdatdp aaliaealkk kfayryrsds qdevekgipk
      301 seseatserv lfgphmlkpt gkmkalienv sds
//
LOCUS       NP_001278770             376 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform Ik-7 [Homo sapiens].
ACCESSION   NP_001278770
VERSION     NP_001278770.1
DBSOURCE    REFSEQ: accession NM_001291841.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U40462.1 and JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (Ik-7) lacks two consecutive
            in-frame exons in the central coding region, compared to variant 1.
            The encoded isoform (Ik-7) is shorter than isoform 1. This isoform
            contains only one N-terminal zinc finger motif, and represents a
            non-DNA-binding, dominant-negative isoform (PMID:9892693).
            
            Sequence Note: The 5' UTR of this variant is incomplete because
            there are no full-length transcripts supporting this variant, and
            there is splicing ambiguity in the 5' UTR.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 9892693, 12937159
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..376
                     /product="DNA-binding protein Ikaros isoform Ik-7"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=41753
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          60..81
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..376
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291841.1:15..1145"
                     /note="isoform Ik-7 is encoded by transcript variant Ik-7"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvgkphkc
       61 gycgrsykqr ssleehkerc hnylesmglp gtlypvikee tnhsemaedl ckigserslv
      121 ldrlasnvak rkssmpqkfl gdkglsdtpy dssasyeken emmkshvmdq ainnainylg
      181 aeslrplvqt ppggsevvpv ispmyqlhkp laegtprsnh saqdsavenl lllskaklvp
      241 sereaspsns cqdstdtesn neeqrsgliy ltnhiaphar nglslkeehr aydllraase
      301 nsqdalrvvs tsgeqmkvyk cehcrvlfld hvmytihmgc hgfrdpfecn mcgyhsqdry
      361 efsshitrge hrfhms
//
LOCUS       NP_001278430            1161 aa            linear   PRI 20-NOV-2025
DEFINITION  structural maintenance of chromosomes protein 1B isoform 2 [Homo
            sapiens].
ACCESSION   NP_001278430 XP_005261623
VERSION     NP_001278430.1
DBSOURCE    REFSEQ: accession NM_001291501.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Shi,Z., Gao,H., Bai,X.C. and Yu,H.
  TITLE     Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  JOURNAL   Science 368 (6498), 1454-1459 (2020)
   PUBMED   32409525
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Rosario,R., Smith,R.W., Adams,I.R. and Anderson,R.A.
  TITLE     RNA immunoprecipitation identifies novel targets of DAZL in human
            foetal ovary
  JOURNAL   Mol Hum Reprod 23 (3), 177-186 (2017)
   PUBMED   28364521
  REMARK    GeneRIF: Through the translational regulation of novel RNA targets
            SMC1B and TEX11, DAZL may have a key role in regulating chromosome
            cohesion and DNA recombination; two processes fundamental in
            determining oocyte quality and whose establishment in foetal life
            may support lifelong fertility.
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Mannini,L., Cucco,F., Quarantotti,V., Amato,C., Tinti,M., Tana,L.,
            Frattini,A., Delia,D., Krantz,I.D., Jessberger,R. and Musio,A.
  TITLE     SMC1B is present in mammalian somatic cells and interacts with
            mitotic cohesin proteins
  JOURNAL   Sci Rep 5, 18472 (2015)
   PUBMED   26673124
  REMARK    GeneRIF: Data show that structural maintenance of chromosomes
            protein 1B (SMC1B) is expressed in primary fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1161)
  AUTHORS   Ansari,D., Andersson,R., Bauden,M.P., Andersson,B., Connolly,J.B.,
            Welinder,C., Sasor,A. and Marko-Varga,G.
  TITLE     Protein deep sequencing applied to biobank samples from patients
            with pancreatic cancer
  JOURNAL   J Cancer Res Clin Oncol 141 (2), 369-380 (2015)
   PUBMED   25216700
  REMARK    GeneRIF: High SMC1B expression is associated with pancreatic
            cancer.
REFERENCE   5  (residues 1 to 1161)
  AUTHORS   Lee,J. and Hirano,T.
  TITLE     RAD21L, a novel cohesin subunit implicated in linking homologous
            chromosomes in mammalian meiosis
  JOURNAL   J Cell Biol 192 (2), 263-276 (2011)
   PUBMED   21242291
REFERENCE   6  (residues 1 to 1161)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   7  (residues 1 to 1161)
  AUTHORS   Revenkova,E., Eijpe,M., Heyting,C., Gross,B. and Jessberger,R.
  TITLE     Novel meiosis-specific isoform of mammalian SMC1
  JOURNAL   Mol Cell Biol 21 (20), 6984-6998 (2001)
   PUBMED   11564881
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126208.1, AJ504806.2 and BG194018.1.
            
            On Apr 18, 2014 this sequence version replaced XP_005261623.2.
            
            Summary: SMC1L2 belongs to a family of proteins required for
            chromatid cohesion and DNA recombination during meiosis and mitosis
            (3:Revenkova et al., 2001 [PubMed 11564881]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons in the 3' coding region, compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC126208.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..1161
                     /product="structural maintenance of chromosomes protein 1B
                     isoform 2"
                     /note="mitosis-specific chromosome segregation protein
                     like protein beta; SMC1 (structural maintenance of
                     chromosomes 1, yeast)-like 1; structural maintenance of
                     chromosomes protein 1B; SMC protein 1B; SMC1 structural
                     maintenance of chromosomes 1-like 2"
                     /calculated_mol_wt=135659
     Region          3..994
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          4..>148
                     /region_name="ABC_SMC1_euk"
                     /note="ATP-binding cassette domain of eukaryotic SMC1
                     proteins; cd03275"
                     /db_xref="CDD:213242"
     Site            32..39
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213242"
     Site            134..137
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213242"
     Site            648
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14683; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     Site            713
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14683; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     Site            1033
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CU62; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     Region          <1088..1142
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            1107..1113
                     /site_type="other"
                     /note="H-loop/switch region"
                     /db_xref="CDD:213179"
     CDS             1..1161
                     /gene="SMC1B"
                     /gene_synonym="SMC1BETA; SMC1L2"
                     /coded_by="NM_001291501.2:33..3518"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74876.1"
                     /db_xref="GeneID:27127"
                     /db_xref="HGNC:HGNC:11112"
                     /db_xref="MIM:608685"
ORIGIN      
        1 mahlelllve nfkswrgrqv igpfrrftci igpngsgksn vmdalsfvmg ekianlrvkn
       61 iqelihgahi gkpisssasv kiiyveesge ektfariirg gcsefrfndn lvsrsvyiae
      121 lekigiivka qnclvfqgtv esisvkkpke rtqffeeist sgeligeyee kkrklqkaee
      181 daqfnfnkkk niaaerrqak lekeeaeryq slleelkmnk iqlqlfqlyh nekkihllnt
      241 klehvnrdls vkreslshhe nivkarkkeh gmltrqlqqt ekelksvetl lnqkrpqyik
      301 akentshhlk kldvakksik dsekqcskqe ddikaletel adldaawrsf ekqieeeilh
      361 kkrdieleas qldrykelke qvrkkvatmt qqleklqweq ktdeerlafe krrhgevqgn
      421 lkqikeqied hkkrieklee ytktcmdclk ekkqqeetlv deiektksrm sevneelnli
      481 rselqnagid thegkrqqkr aevlehlkrl ypdsvfgrlf dlchpihkky qlavtkvfgr
      541 fitaivvase kvakdcirfl keeraepetf laldyldikp inerlrelkg ckmvidvikt
      601 qfpqlkkviq fvcgnglvce tmeearhial sgperqktva ldgtlflksg visggssdlk
      661 ykarcwdeke lknlrdrrsq kiqelkglmk tlrketdlkq iqtliqgtqt rlkysqnele
      721 mikkkhlvaf yqeqsqlqse llniesqcim lsegikerqr rikefqekid kveddifqhf
      781 ceeigvenir efenkhvkrq qeidqkrlef ekqktrlnvq leysrshlkk klnkintlke
      841 tiqkgsedid hlkkaeencl qtvnelmakq qqlkdirvtq nssaekvqtq ieeerkkfla
      901 vdrevgklqk evvsiqtsle qkrlekhnll ldckvqdiei illsgslddi ievemgteae
      961 stqatidiye keeafeidys slkedlkalq sdqeieahlr lllqqvasqe dillktaapn
     1021 lralenlktv rdkfqestda feasrkearl crqefeqvkk rrydlftqcf ehvsisidqi
     1081 ykklcrnnsa qvssyikeqt qdqfqmivis lkeefysrad aligiypeyd dcmfsrvltl
     1141 dlsqypdteg qesskrhges r
//
LOCUS       NP_065852                414 aa            linear   PRI 20-NOV-2025
DEFINITION  arrestin domain-containing protein 3 isoform a [Homo sapiens].
ACCESSION   NP_065852
VERSION     NP_065852.1
DBSOURCE    REFSEQ: accession NM_020801.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Chen,M., Yin,B., Liu,Y., Li,M., Shen,S., Wu,J., Li,W. and Fan,J.
  TITLE     ARRDC3 regulates the targeted therapy sensitivity of clear cell
            renal cell carcinoma by promoting AXL degradation
  JOURNAL   Cell Cycle 23 (1), 56-69 (2024)
   PUBMED   38389126
  REMARK    GeneRIF: ARRDC3 regulates the targeted therapy sensitivity of clear
            cell renal cell carcinoma by promoting AXL degradation.
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Long,M. and Wang,S.
  TITLE     Hsa_circ_0001740 mediates trophoblast cell function via regulating
            miR-188-3p/ARRDC3
  JOURNAL   Mol Reprod Dev 90 (6), 406-416 (2023)
   PUBMED   37436094
  REMARK    GeneRIF: Hsa_circ_0001740 mediates trophoblast cell function via
            regulating miR-188-3p/ARRDC3.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Huang,C.N., Huang,S.P., Pao,J.B., Chang,T.Y., Lan,Y.H., Lu,T.L.,
            Lee,H.Z., Juang,S.H., Wu,P.P., Pu,Y.S., Hsieh,C.J. and Bao,B.Y.
  TITLE     Genetic polymorphisms in androgen receptor-binding sites predict
            survival in prostate cancer patients receiving androgen-deprivation
            therapy
  JOURNAL   Ann Oncol 23 (3), 707-713 (2012)
   PUBMED   21652578
  REMARK    GeneRIF: single-nucleotide polymorphisms in ARRDC3, FLT1, and SKAP1
            were significant predictors for survival androgen-deprivation
            therapy in prostate cancer patients.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Draheim,K.M., Chen,H.B., Tao,Q., Moore,N., Roche,M. and Lyle,S.
  TITLE     ARRDC3 suppresses breast cancer progression by negatively
            regulating integrin beta4
  JOURNAL   Oncogene 29 (36), 5032-5047 (2010)
   PUBMED   20603614
  REMARK    GeneRIF: ARRDC3 directly binds to a phosphorylated form of ITGbeta4
            leading to its internalization, ubiquitination and ultimate
            degradation, and suppress breast cancer progression.
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Nabhan,J.F., Pan,H. and Lu,Q.
  TITLE     Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase
            to mediate ubiquitination of the beta2-adrenergic receptor
  JOURNAL   EMBO Rep 11 (8), 605-611 (2010)
   PUBMED   20559325
  REMARK    GeneRIF: Data show that ARRDC3 interacts with NEDD4 through two
            conserved PPXY motifs and recruits NEDD4 to the activated
            beta2-adrenergic receptor.
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Patwari,P., Chutkow,W.A., Cummings,K., Verstraeten,V.L.,
            Lammerding,J., Schreiter,E.R. and Lee,R.T.
  TITLE     Thioredoxin-independent regulation of metabolism by the
            alpha-arrestin proteins
  JOURNAL   J Biol Chem 284 (37), 24996-25003 (2009)
   PUBMED   19605364
  REMARK    GeneRIF: Txnip regulates cellular metabolism independent of its
            binding to thioredoxin and the arrestin domains are crucial
            structural elements in metabolic functions of alpha-arrestin
            proteins
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Oka,S., Masutani,H., Liu,W., Horita,H., Wang,D., Kizaka-Kondoh,S.
            and Yodoi,J.
  TITLE     Thioredoxin-binding protein-2-like inducible membrane protein is a
            novel vitamin D3 and peroxisome proliferator-activated receptor
            (PPAR)gamma ligand target protein that regulates PPARgamma
            signaling
  JOURNAL   Endocrinology 147 (2), 733-743 (2006)
   PUBMED   16269462
  REMARK    GeneRIF: [Thioredoxin-binding protein-2-like inducible membrane
            protein, TLIMP] TLIMP, a novel VD3- or PPARgamma ligand-inducible
            membrane-associated protein, plays a regulatory role in cell
            proliferation and PPARgamma activation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX642781.1, AB037797.1,
            HY355442.1 and AC008799.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the arrestin family of
            proteins, which regulate G protein-mediated signaling. The encoded
            protein is thought to act as a regulator of breast cancer growth
            and progression by binding to a phosphorylated form of integrin
            beta4, a tumor-related antigen, targeting the integrin for
            internalization and degradation. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB037797.1, SRR18074969.2823903.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265138.4/ ENSP00000265138.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..414
                     /product="arrestin domain-containing protein 3 isoform a"
                     /note="TBP-2-like inducible membrane protein;
                     alpha-arrestin 3"
                     /calculated_mol_wt=46264
     Region          22..165
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     pfam00339"
                     /db_xref="CDD:425619"
     Region          187..314
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     smart01017"
                     /db_xref="CDD:214976"
     Region          346..349
                     /region_name="PPxY motif 1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     Region          391..394
                     /region_name="PPxY motif 2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     Region          393..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B67.1)"
     CDS             1..414
                     /gene="ARRDC3"
                     /gene_synonym="TLIMP"
                     /coded_by="NM_020801.4:226..1470"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34202.1"
                     /db_xref="GeneID:57561"
                     /db_xref="HGNC:HGNC:29263"
                     /db_xref="MIM:612464"
ORIGIN      
        1 mvlgkvkslt isfdclndsn vpvyssgdtv sgrvnlevtg eirvkslkih arghakvrwt
       61 esrnagsnta ytqnyteeve yfnhkdilig herdddnsee gfhtihsgrh eyafsfelpq
      121 tplatsfegr hgsvrywvka elhrpwllpv klkkeftvfe hidintpsll spqagtkekt
      181 lccwfctsgp islsakierk gytpgesiqi faeiencssr mvvpkaaiyq tqafyakgkm
      241 kevkqlvanl rgeslssgkt etwngkllki ppvspsildc siirveyslm vyvdipgamd
      301 lflnlplvig tiplhpfgsr tssvssqcsm nmnwlslslp erpeappsya evvteeqrrn
      361 nlapvsacdd feralqgplf ayiqefrflp pplyseidpn pdqsaddrps cpsr
//
LOCUS       NP_001308511             489 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 22 [Homo sapiens].
ACCESSION   NP_001308511
VERSION     NP_001308511.1
DBSOURCE    REFSEQ: accession NM_001321582.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 489)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (23) encodes isoform (22, also
            known as delta 7).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.4495.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..489
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 22"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=55233
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          357..484
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..489
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321582.2:671..2140"
                     /note="isoform 22 is encoded by transcript variant 23"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkkr kssssvqmme stessnttie dedvkarkqe
      361 iikvteqlie ainngdfeay tkicdpglta fepealgnlv egmdfhrfyf enalsksnkp
      421 ihtiilnphv hlvgddaaci ayirltqymd gsgmpktmqs eetrvwhrrd gkwqnvhfhr
      481 sgsptvpin
//
LOCUS       NP_653312                558 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 23 [Homo sapiens].
ACCESSION   NP_653312
VERSION     NP_653312.2
DBSOURCE    REFSEQ: accession NM_144711.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Wouters,M.M., Neefs,J.M., Kerchove d'Exaerde,Ad., Vanderwinden,J.M.
            and Smans,K.A.
  TITLE     Downregulation of two novel genes in Sl/Sld and W(LacZ)/Wv mouse
            jejunum
  JOURNAL   Biochem Biophys Res Commun 346 (2), 491-500 (2006)
   PUBMED   16765319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009967.8, BJ990781.1, BC010437.1 and BE326381.1.
            
            On Dec 20, 2003 this sequence version replaced NP_653312.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.50521.1,
                                           SRR1803612.227762.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392647.7/ ENSP00000376419.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..558
                     /product="kelch-like protein 23"
                     /note="kelch-like 23"
                     /calculated_mol_wt=63792
     Region          15..141
                     /region_name="BTB_POZ_KLHL23"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 23 (KLHL23); cd18252"
                     /db_xref="CDD:349561"
     Region          45..545
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          134..235
                     /region_name="BACK_KLHL23"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 23 (KLHL23); cd18462"
                     /db_xref="CDD:350537"
     Region          274..320
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     Region          310..355
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          321..369
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     Region          359..402
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          370..416
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     Region          406..495
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          418..466
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     Region          467..508
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     Region          498..545
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          510..557
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBE8.1)"
     CDS             1..558
                     /gene="KLHL23"
                     /gene_synonym="DITHP"
                     /coded_by="NM_144711.6:259..1935"
                     /db_xref="GeneID:151230"
                     /db_xref="HGNC:HGNC:27506"
ORIGIN      
        1 malkgqedyi ylfkdsthpv dfldafrtfy ldglftditl qcpsgiifhc hravlaacsn
       61 yfkamftadm kekfknkikl sgihhdileg lvnyaytsqi eitkrnvqsl leaadllqfl
      121 svkkacerfl vrhldidnci gmhsfaefhv cpelekesrr ilcskfkevw qqeefleisl
      181 ekflfilsrk nlsvwkeeai iepvikwtah dvenriecly nllsyinidi dpvylktalg
      241 lqrscllten kirsliynal npmhkeisqr statmyiigg yywhplsevh iwdpltnvwi
      301 qgaeipdytr esygvtclgp niyvtggyrt dniealdtvw iynsesdewt eglpmlnary
      361 yhcavtlggc vyalggyrkg apaeeaefyd plkekwipia nmikgvgnat acvlhdviyv
      421 igghcgyrgs ctydkvqsyn sdinewslit ssphpeyglc svpfenklyl vggqttitec
      481 ydpeqnewre iapmmerrme cgavimngci yvtggysysk gtylqsieky dpdlnkweiv
      541 gnlpsamrsh gcvcvynv
//
LOCUS       NP_852002                520 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 11 isoform 2 [Homo sapiens].
ACCESSION   NP_852002
VERSION     NP_852002.1
DBSOURCE    REFSEQ: accession NM_181357.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Wang,K., Liu,Y., Yu,Z., Gu,B., Hu,J., Huang,L., Ge,X., Xu,L.,
            Zhang,M., Zhao,J., Hu,M., Le,R., Wu,Q., Ye,S., Gao,S., Zhang,X.,
            Xu,R.M. and Li,G.
  TITLE     Phosphorylation at Ser68 facilitates DCAF11-mediated ubiquitination
            and degradation of CENP-A during the cell cycle
  JOURNAL   Cell Rep 37 (6), 109987 (2021)
   PUBMED   34758320
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zhang,X., Luukkonen,L.M., Eissler,C.L., Crowley,V.M., Yamashita,Y.,
            Schafroth,M.A., Kikuchi,S., Weinstein,D.S., Symons,K.T.,
            Nordin,B.E., Rodriguez,J.L., Wucherpfennig,T.G., Bauer,L.G.,
            Dix,M.M., Stamos,D., Kinsella,T.M., Simon,G.M., Baltgalvis,K.A. and
            Cravatt,B.F.
  TITLE     DCAF11 Supports Targeted Protein Degradation by Electrophilic
            Proteolysis-Targeting Chimeras
  JOURNAL   J Am Chem Soc 143 (13), 5141-5149 (2021)
   PUBMED   33783207
  REMARK    GeneRIF: DCAF11 Supports Targeted Protein Degradation by
            Electrophilic Proteolysis-Targeting Chimeras.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Siswanto,F.M., Oguro,A., Arase,S. and Imaoka,S.
  TITLE     WDR23 regulates the expression of Nrf2-driven drug-metabolizing
            enzymes
  JOURNAL   Drug Metab Pharmacokinet 35 (5), 441-455 (2020)
   PUBMED   32839090
  REMARK    GeneRIF: WDR23 regulates the expression of Nrf2-driven
            drug-metabolizing enzymes.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Jager,S., Cimermancic,P., Gulbahce,N., Johnson,J.R., McGovern,K.E.,
            Clarke,S.C., Shales,M., Mercenne,G., Pache,L., Li,K., Hernandez,H.,
            Jang,G.M., Roth,S.L., Akiva,E., Marlett,J., Stephens,M., D'Orso,I.,
            Fernandes,J., Fahey,M., Mahon,C., O'Donoghue,A.J., Todorovic,A.,
            Morris,J.H., Maltby,D.A., Alber,T., Cagney,G., Bushman,F.D.,
            Young,J.A., Chanda,S.K., Sundquist,W.I., Kortemme,T.,
            Hernandez,R.D., Craik,C.S., Burlingame,A., Sali,A., Frankel,A.D.
            and Krogan,N.J.
  TITLE     Global landscape of HIV-human protein complexes
  JOURNAL   Nature 481 (7381), 365-370 (2011)
   PUBMED   22190034
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Choe,K.P., Przybysz,A.J. and Strange,K.
  TITLE     The WD40 repeat protein WDR-23 functions with the CUL4/DDB1
            ubiquitin ligase to regulate nuclear abundance and activity of
            SKN-1 in Caenorhabditis elegans
  JOURNAL   Mol Cell Biol 29 (10), 2704-2715 (2009)
   PUBMED   19273594
  REMARK    GeneRIF: Includes the functional characterization of a similar
            protein in C. elegans and comparison to the human protein.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Olma,M.H., Roy,M., Le Bihan,T., Sumara,I., Maerki,S., Larsen,B.,
            Quadroni,M., Peter,M., Tyers,M. and Pintard,L.
  TITLE     An interaction network of the mammalian COP9 signalosome identifies
            Dda1 as a core subunit of multiple Cul4-based E3 ligases
  JOURNAL   J Cell Sci 122 (Pt 7), 1035-1044 (2009)
   PUBMED   19295130
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Scrima,A., Konickova,R., Czyzewski,B.K., Kawasaki,Y., Jeffrey,P.D.,
            Groisman,R., Nakatani,Y., Iwai,S., Pavletich,N.P. and Thoma,N.H.
  TITLE     Structural basis of UV DNA-damage recognition by the DDB1-DDB2
            complex
  JOURNAL   Cell 135 (7), 1213-1223 (2008)
   PUBMED   19109893
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB212727.1, AK057636.1,
            AK094478.1, BX406971.2 and AB209073.1.
            
            Summary: This gene encodes a WD repeat-containing protein that
            interacts with the COP9 signalosome, a macromolecular complex that
            interacts with cullin-RING E3 ligases and regulates their activity
            by hydrolyzing cullin-Nedd8 conjugates. Multiple alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Jul 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate in-frame segment in the 5' coding region,
            compared to variant 1, resulting in an isoform (2) that is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..520
                     /product="DDB1- and CUL4-associated factor 11 isoform 2"
                     /note="WD repeat domain 23; WD repeat-containing protein
                     23"
                     /calculated_mol_wt=58715
     Region          <154..485
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          154..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..237
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          243..279
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          284..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          333..368
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          414..444
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          460..484
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..520
                     /gene="DCAF11"
                     /gene_synonym="GL014; PRO2389; WDR23"
                     /coded_by="NM_181357.2:161..1723"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41929.1"
                     /db_xref="GeneID:80344"
                     /db_xref="HGNC:HGNC:20258"
                     /db_xref="MIM:613317"
ORIGIN      
        1 mgsrnsssag sgsgdpsegl prrgaglrrs eeeeeededv dlaqalldse eendrawdgr
       61 lgdrynppvd atpdtrelef neiktqvela tgqlglrraa qkhsfprmlh qrerglchrg
      121 sfslgeqsrv ishflpndlg ftdsysqkaf cgiyskdgqi fmsacqdqti rlydcrygrf
      181 rkfksikard vgwsvldvaf tpdgnhflys swsdyihicn iygegdthta ldlrpderrf
      241 avfsiavssd grevlggand gclyvfdreq nrrtlqiesh eddvnavafa dissqilfsg
      301 gddaickvwd rrtmreddpk pvgalaghqd gitfidskgd arylisnskd qtiklwdirr
      361 fssregmeas rqaatqqnwd yrwqqvpkka wrklklpgds slmtyrghgv lhtlircrfs
      421 pihstgqqfi ysgcstgkvv vydllsghiv kkltnhkacv rdvswhpfee kivssswdgn
      481 lrlwqyrqae yfqddmpese ecasapapvp qsstpfsspq
//
LOCUS       NP_001351005             272 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-H isoform 5 [Homo sapiens].
ACCESSION   NP_001351005 XP_016865503
VERSION     NP_001351005.1
DBSOURCE    REFSEQ: accession NM_001364076.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Zhang,T.Y., Chen,Y.Q., Tan,J.C., Zhou,J.A., Chen,W.N., Jiang,T.,
            Zha,J.Y., Zeng,X.K., Li,B.W., Wei,L.Q., Zou,Y., Zhang,L.Y.,
            Hong,Y.M., Wang,X.L., Zhu,R.Z., Xu,W.X., Xi,J., Wang,Q.Q., Pan,L.,
            Zhang,J., Luan,Y., Zhu,R.X., Wang,H., Chen,C. and Liu,N.N.
  TITLE     Global fungal-host interactome mapping identifies host targets of
            candidalysin
  JOURNAL   Nat Commun 15 (1), 1757 (2024)
   PUBMED   38413612
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Schutz,M., Wangen,C., Sommerer,M., Kogler,M., Eickhoff,J.,
            Degenhart,C., Klebl,B., Naing,Z., Egilmezer,E., Hamilton,S.T.,
            Rawlinson,W.D., Sticht,H. and Marschall,M.
  TITLE     Cytomegalovirus cyclin-dependent kinase ortholog vCDK/pUL97
            undergoes regulatory interaction with human cyclin H and CDK7 to
            codetermine viral replication efficiency
  JOURNAL   Virus Res 335, 199200 (2023)
   PUBMED   37591314
  REMARK    GeneRIF: Cytomegalovirus cyclin-dependent kinase ortholog
            vCDK/pUL97 undergoes regulatory interaction with human cyclin H and
            CDK7 to codetermine viral replication efficiency.
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Eki,T., Okumura,K., Abe,M., Kagotani,K., Taguchi,H., Murakami,Y.,
            Pan,Z.Q. and Hanaoka,F.
  TITLE     Mapping of the human genes encoding cyclin H (CCNH) and the
            CDK-activating kinase (CAK) assembly factor MAT1 (MNAT1) to
            chromosome bands 5q13.3-q14 and 14q23, respectively
  JOURNAL   Genomics 47 (1), 115-120 (1998)
   PUBMED   9465303
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Aprelikova,O., Xiong,Y. and Liu,E.T.
  TITLE     Both p16 and p21 families of cyclin-dependent kinase (CDK)
            inhibitors block the phosphorylation of cyclin-dependent kinases by
            the CDK-activating kinase
  JOURNAL   J Biol Chem 270 (31), 18195-18197 (1995)
   PUBMED   7629134
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Shiekhattar,R., Mermelstein,F., Fisher,R.P., Drapkin,R.,
            Dynlacht,B., Wessling,H.C., Morgan,D.O. and Reinberg,D.
  TITLE     Cdk-activating kinase complex is a component of human transcription
            factor TFIIH
  JOURNAL   Nature 374 (6519), 283-287 (1995)
   PUBMED   7533895
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Fisher,R.P. and Morgan,D.O.
  TITLE     A novel cyclin associates with MO15/CDK7 to form the CDK-activating
            kinase
  JOURNAL   Cell 78 (4), 713-724 (1994)
   PUBMED   8069918
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018754.6.
            
            On Jun 6, 2018 this sequence version replaced XP_016865503.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with CDK7 kinase and ring finger protein
            MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2
            kinases, thus functions as a CDK-activating kinase (CAK). This
            cyclin and its kinase partner are components of TFIIH, as well as
            RNA polymerase II protein complexes. They participate in two
            different transcriptional regulation processes, suggesting an
            important link between basal transcription control and the cell
            cycle machinery. A pseudogene of this gene is found on chromosome
            4. Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence compared to variant 3. The resulting isoform (5) is
            shorter at the N-terminus compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.260254.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..272
                     /product="cyclin-H isoform 5"
                     /note="CDK-activating kinase complex subunit;
                     cyclin-dependent kinase-activating kinase complex subunit;
                     CAK complex subunit; MO15-associated protein"
                     /calculated_mol_wt=31588
     Region          1..255
                     /region_name="ccl1"
                     /note="cyclin ccl1; TIGR00569"
                     /db_xref="CDD:129660"
     CDS             1..272
                     /gene="CCNH"
                     /gene_synonym="CAK; CycH; p34; p37"
                     /coded_by="NM_001364076.2:539..1357"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:902"
                     /db_xref="HGNC:HGNC:1594"
                     /db_xref="MIM:601953"
ORIGIN      
        1 mtlckyyekr llefcsvfkp amprsvvgta cmyfkrfyln nsvmeyhpri imltcaflac
       61 kvdefnvssp qfvgnlresp lgqekaleqi leyellliqq lnfhlivhnp yrpfegflid
      121 lktrypilen peilrktadd flnrialtda yllytpsqia ltailssasr agitmesyls
      181 eslmlkenrt clsqlldimk smrnlvkkye pprseevavl kqklerchsa elalnvitkk
      241 rkgyedddyv skkskheeia klwhqskvht yh
//
LOCUS       NP_005388                526 aa            linear   PRI 20-NOV-2025
DEFINITION  podocalyxin isoform 2 precursor [Homo sapiens].
ACCESSION   NP_005388
VERSION     NP_005388.2
DBSOURCE    REFSEQ: accession NM_005397.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 526)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 526)
  AUTHORS   Le Tran,N., Wang,Y., Bilandzic,M., Stephens,A. and Nie,G.
  TITLE     Podocalyxin promotes the formation of compact and chemoresistant
            cancer spheroids in high grade serous carcinoma
  JOURNAL   Sci Rep 14 (1), 7539 (2024)
   PUBMED   38553472
  REMARK    GeneRIF: Podocalyxin promotes the formation of compact and
            chemoresistant cancer spheroids in high grade serous carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 526)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 526)
  AUTHORS   Thach,B., Samarajeewa,N., Li,Y., Heng,S., Tsai,T., Pangestu,M.,
            Catt,S. and Nie,G.
  TITLE     Podocalyxin molecular characteristics and endometrial expression:
            high conservation between humans and macaques but divergence in
            micedagger
  JOURNAL   Biol Reprod 106 (6), 1143-1158 (2022)
   PUBMED   35284933
  REMARK    GeneRIF: Podocalyxin molecular characteristics and endometrial
            expression: high conservation between humans and macaques but
            divergence in micedagger.
REFERENCE   5  (residues 1 to 526)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 526)
  AUTHORS   Takeda,T., McQuistan,T., Orlando,R.A. and Farquhar,M.G.
  TITLE     Loss of glomerular foot processes is associated with uncoupling of
            podocalyxin from the actin cytoskeleton
  JOURNAL   J Clin Invest 108 (2), 289-301 (2001)
   PUBMED   11457882
REFERENCE   7  (residues 1 to 526)
  AUTHORS   Sassetti,C., Tangemann,K., Singer,M.S., Kershaw,D.B. and Rosen,S.D.
  TITLE     Identification of podocalyxin-like protein as a high endothelial
            venule ligand for L-selectin: parallels to CD34
  JOURNAL   J Exp Med 187 (12), 1965-1975 (1998)
   PUBMED   9625756
REFERENCE   8  (residues 1 to 526)
  AUTHORS   Kershaw,D.B., Wiggins,J.E., Wharram,B.L. and Wiggins,R.C.
  TITLE     Assignment of the human podocalyxin-like protein (PODXL) gene to
            7q32-q33
  JOURNAL   Genomics 45 (1), 239-240 (1997)
   PUBMED   9339384
REFERENCE   9  (residues 1 to 526)
  AUTHORS   Kershaw,D.B., Beck,S.G., Wharram,B.L., Wiggins,J.E., Goyal,M.,
            Thomas,P.E. and Wiggins,R.C.
  TITLE     Molecular cloning and characterization of human podocalyxin-like
            protein. Orthologous relationship to rabbit PCLP1 and rat
            podocalyxin
  JOURNAL   J Biol Chem 272 (25), 15708-15714 (1997)
   PUBMED   9188463
REFERENCE   10 (residues 1 to 526)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008264.10, AK055816.1,
            AK223573.1, BC042466.1 and BP355358.1.
            
            On Aug 12, 2003 this sequence version replaced NP_005388.1.
            
            Summary: This gene encodes a member of the sialomucin protein
            family. The encoded protein was originally identified as an
            important component of glomerular podocytes. Podocytes are highly
            differentiated epithelial cells with interdigitating foot processes
            covering the outer aspect of the glomerular basement membrane.
            Other biological activities of the encoded protein include: binding
            in a membrane protein complex with Na+/H+ exchanger regulatory
            factor to intracellular cytoskeletal elements, playing a role in
            hematopoetic cell differentiation, and being expressed in vascular
            endothelium cells and binding to L-selectin. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame alternate
            exon compared to variant 1, resulting in a shorter protein (isoform
            2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.86306.1,
                                           SRR7346977.2438416.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..526
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.3"
     Protein         1..526
                     /product="podocalyxin isoform 2 precursor"
                     /note="podocalyxin-like protein 1; GCTM-2 antigen"
                     /calculated_mol_wt=53110
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2294
     mat_peptide     23..526
                     /product="podocalyxin isoform 2"
                     /calculated_mol_wt=53110
     Region          <33..>293
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          326..526
                     /region_name="CD34_antigen"
                     /note="CD34/Podocalyxin family; pfam06365"
                     /db_xref="CDD:461884"
     CDS             1..526
                     /gene="PODXL"
                     /gene_synonym="gp135; Gp200; PC; PCLP; PCLP-1; PDX;
                     PODXL1"
                     /coded_by="NM_005397.4:270..1850"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS47714.1"
                     /db_xref="GeneID:5420"
                     /db_xref="HGNC:HGNC:9171"
                     /db_xref="MIM:602632"
ORIGIN      
        1 mrcalalsal llllstppll psspspspsp sqnatqtttd ssnktaptpa ssvtimatdt
       61 aqqstvptsk aneilasvka ttlgvssdsp gtttlaqqvs gpvnttvarg ggsgnpttti
      121 espkstksad tttvatstat akpnttssqn gaedttnsgg ksshsvttdl tstkaehltt
      181 phptsplspr qptsthpvat ptssghdhlm kissssstva ipgytftspg mtttlpssvi
      241 sqrtqqtssq mpasstapss qetvqptspa talrtptlpe tmsssptaas tthrypktps
      301 ptvahesnwa kcedletqtq sekqlvlnlt gntlcaggas deklislicr avkatfnpaq
      361 dkcgirlasv pgsqtvvvke itihtklpak dvyerlkdkw delkeagvsd mklgdqgppe
      421 eaedrfsmpl iitivcmasf lllvaalygc chqrlsqrkd qqrlteelqt vengyhdnpt
      481 levmetssem qekkvvslng elgdswivpl dnltkddlde eedthl
//
LOCUS       NP_444251                570 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase ZFP91 isoform 1 [Homo sapiens].
ACCESSION   NP_444251
VERSION     NP_444251.1
DBSOURCE    REFSEQ: accession NM_053023.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Liu,T.T., Yang,H., Zhuo,F.F., Yang,Z., Zhao,M.M., Guo,Q., Liu,Y.,
            Liu,D., Zeng,K.W. and Tu,P.F.
  TITLE     Atypical E3 ligase ZFP91 promotes small-molecule-induced E2F2
            transcription factor degradation for cancer therapy
  JOURNAL   EBioMedicine 86, 104353 (2022)
   PUBMED   36375317
  REMARK    GeneRIF: Atypical E3 ligase ZFP91 promotes small-molecule-induced
            E2F2 transcription factor degradation for cancer therapy.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Wu,W., Nelson,G.M., Koch,R., Donovan,K.A., Nowak,R.P.,
            Heavican-Foral,T.B., Nirmal,A.J., Liu,H., Yang,L., Duffy,J.,
            Powers,F., Stevenson,K.E., Jones,M.K., Ng,S.Y., Wu,G., Jain,S.,
            Xu,R., Amaka,S., Trevisani,C., Donaldson,N.L., Hagner,P.R., de
            Leval,L., Gaulard,P., Iqbal,J., Thakurta,A., Fischer,E.S.,
            Adelman,K. and Weinstock,D.M.
  TITLE     Overcoming IMiD resistance in T-cell lymphomas through potent
            degradation of ZFP91 and IKZF1
  JOURNAL   Blood 139 (13), 2024-2037 (2022)
   PUBMED   34936696
  REMARK    GeneRIF: Overcoming IMiD resistance in T-cell lymphomas through
            potent degradation of ZFP91 and IKZF1.
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Zhong,Y., Zhang,Z.H., Wang,J.Y., Xing,Y., Ri,M.H., Jin,H.L.,
            Zuo,H.X., Li,M.Y., Ma,J. and Jin,X.
  TITLE     Zinc finger protein 91 mediates necroptosis by initiating
            RIPK1-RIPK3-MLKL signal transduction in response to TNF receptor 1
            ligation
  JOURNAL   Toxicol Lett 356, 75-88 (2022)
   PUBMED   34942311
  REMARK    GeneRIF: Zinc finger protein 91 mediates necroptosis by initiating
            RIPK1-RIPK3-MLKL signal transduction in response to TNF receptor 1
            ligation.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Wang,F., Zhang,Y., Yu,X., Teng,X.L., Ding,R., Hu,Z., Wang,A.,
            Wang,Z., Ye,Y. and Zou,Q.
  TITLE     ZFP91 disturbs metabolic fitness and antitumor activity of
            tumor-infiltrating T cells
  JOURNAL   J Clin Invest 131 (19) (2021)
   PUBMED   34403361
  REMARK    GeneRIF: ZFP91 disturbs metabolic fitness and antitumor activity of
            tumor-infiltrating T cells.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Unoki,M., Okutsu,J. and Nakamura,Y.
  TITLE     Identification of a novel human gene, ZFP91, involved in acute
            myelogenous leukemia
  JOURNAL   Int J Oncol 22 (6), 1217-1223 (2003)
   PUBMED   12738986
  REMARK    GeneRIF: likely to play an important role in cell proliferation
            and/or anti-apoptosis, and may serve as a molecular marker for AML
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Iuchi,S.
  TITLE     Three classes of C2H2 zinc finger proteins
  JOURNAL   Cell Mol Life Sci 58 (4), 625-635 (2001)
   PUBMED   11361095
  REMARK    Review article
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Grottke,C., Mantwill,K., Dietel,M., Schadendorf,D. and Lage,H.
  TITLE     Identification of differentially expressed genes in human melanoma
            cells with acquired resistance to various antineoplastic drugs
  JOURNAL   Int J Cancer 88 (4), 535-546 (2000)
   PUBMED   11058868
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Saotome,Y., Winter,C.G. and Hirsh,D.
  TITLE     A widely expressed novel C2H2 zinc-finger protein with multiple
            consensus phosphorylation sites is conserved in mouse and man
  JOURNAL   Gene 152 (2), 233-238 (1995)
   PUBMED   7835706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001350.4, BC051743.1,
            AB056107.1, BP219969.1 and AI687439.1.
            
            Summary: The protein encoded by this gene is a member of the zinc
            finger family of proteins. The gene product contains C2H2-type
            domains, which are the classical zinc finger domains found in
            numerous nucleic acid-binding proteins. This protein functions as a
            regulator of the non-canonical NF-kappaB pathway in
            lymphotoxin-beta receptor signaling. Alternative splicing results
            in multiple transcript variants. A read-through transcript variant
            composed of ZFP91 and the downstream CNTF gene sequence has been
            identified, but it is thought to be non-coding. Read-through
            transcription of ZFP91 and CNTF has also been observed in mouse. A
            ZFP91-related pseudogene has also been identified on chromosome 2.
            [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB056107.1, SRR1660807.98663.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316059.7/ ENSP00000339030.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..570
                     /product="E3 ubiquitin-protein ligase ZFP91 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="zinc finger protein homologous to Zfp91 in mouse;
                     penta zinc finger protein; E3 ubiquitin-protein ligase
                     ZFP91; drug resistance-associated sequence in melanoma 8;
                     zinc finger protein 757; zinc finger protein 91 homolog;
                     RING-type E3 ubiquitin transferase ZFP91"
                     /calculated_mol_wt=63314
     Region          1..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JP5.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62511; propagated from
                     UniProtKB/Swiss-Prot (Q96JP5.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62511; propagated from
                     UniProtKB/Swiss-Prot (Q96JP5.1)"
     Region          338..368
                     /region_name="Interaction with MAP3K14/NIK.
                     /evidence=ECO:0000269|PubMed:20682767"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JP5.1)"
     Region          347..366
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(351,353,355,357..358,361..362,365,379,381,385..386,
                     389..390,393,407,409,411,413..414,417..418,421)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          374..394
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          401..422
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          402..422
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          432..448
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..570
                     /gene="ZFP91"
                     /gene_synonym="DMS-8; DSM-8; DSM8; FKSG11; PZF; ZFP-91;
                     ZNF757"
                     /coded_by="NM_053023.5:220..1932"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31553.1"
                     /db_xref="GeneID:80829"
                     /db_xref="HGNC:HGNC:14983"
                     /db_xref="MIM:619289"
ORIGIN      
        1 mpgeteeprp peqqdqegge aakaapeepq qrppeavaaa pagttssrvl rggrdrgraa
       61 aaaaaaavsr rrkaeyprrr rsspsarppd vpgqqpqaak spspvqgkks prllciekvt
      121 tdkdpkeeke eeddsalpqe vsiaasrpsr gwrssrtsvs rhrdtentrs srsktgslql
      181 icksepntdq ldydvgeehq spggisseee eeeeeemlis eeeipfkddp rdetykphle
      241 retpkprrks gkvkeekekk eikvevevev keeeneired eepprkrgrr rkddksprlp
      301 krrkkppiqy vrcemegcgt vlahprylqh hikyqhllkk kyvcphpscg rlfrlqkqll
      361 rhakhhtdqr dyiceycara fksshnlavh rmihtgekpl qceicgftcr qkaslnwhmk
      421 khdadsfyqf scnicgkkfe kkdsvvahka kshpevliae alaanagali tstdilgtnp
      481 esltqpsdgq glpllpeplg nstsgeclll eaegmsksyc sgtervslma dgkifvgsgs
      541 sggteglvmn sdilgattev liedsdsagp
//
LOCUS       NP_060624                202 aa            linear   PRI 20-NOV-2025
DEFINITION  histone chaperone ASF1B [Homo sapiens].
ACCESSION   NP_060624
VERSION     NP_060624.1
DBSOURCE    REFSEQ: accession NM_018154.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Zhang,P., Wang,P. and Wang,Y.
  TITLE     ASF1B is an essential prognostic indicator linked to the growth and
            resistance characteristics of bladder cancer
  JOURNAL   Tissue Cell 89, 102477 (2024)
   PUBMED   39018712
  REMARK    GeneRIF: ASF1B is an essential prognostic indicator linked to the
            growth and resistance characteristics of bladder cancer.
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Xiao,F., Zhu,H., Guo,Y., Zhang,Z., Sun,G., Xiao,Y., Hu,G., Huang,K.
            and Guo,H.
  TITLE     CIA-II is associated with lower-grade glioma survival and cell
            proliferation
  JOURNAL   CNS Neurosci Ther 30 (2), e14340 (2024)
   PUBMED   37452510
  REMARK    GeneRIF: CIA-II is associated with lower-grade glioma survival and
            cell proliferation.
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Zhang,Z. and Liu,S.
  TITLE     The interaction between ASF1B and TLK1 promotes the malignant
            progression of low-grade glioma
  JOURNAL   Ann Med 55 (1), 1111-1122 (2023)
   PUBMED   36947060
  REMARK    GeneRIF: The interaction between ASF1B and TLK1 promotes the
            malignant progression of low-grade glioma.
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Zhang,M., Zhang,L., Zhou,M., Wang,E., Meng,B., Li,Q., Wang,X.,
            Wang,Y. and Li,Q.
  TITLE     Anti-silencing function 1B promotes the progression of pancreatic
            cancer by activating c-Myc
  JOURNAL   Int J Oncol 62 (1) (2023)
   PUBMED   36416310
  REMARK    GeneRIF: Antisilencing function 1B promotes the progression of
            pancreatic cancer by activating cMyc.
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Groth,A., Ray-Gallet,D., Quivy,J.P., Lukas,J., Bartek,J. and
            Almouzni,G.
  TITLE     Human Asf1 regulates the flow of S phase histones during
            replicational stress
  JOURNAL   Mol Cell 17 (2), 301-311 (2005)
   PUBMED   15664198
REFERENCE   7  (residues 1 to 202)
  AUTHORS   Loyola,A. and Almouzni,G.
  TITLE     Histone chaperones, a supporting role in the limelight
  JOURNAL   Biochim Biophys Acta 1677 (1-3), 3-11 (2004)
   PUBMED   15020040
  REMARK    Review article
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Tagami,H., Ray-Gallet,D., Almouzni,G. and Nakatani,Y.
  TITLE     Histone H3.1 and H3.3 complexes mediate nucleosome assembly
            pathways dependent or independent of DNA synthesis
  JOURNAL   Cell 116 (1), 51-61 (2004)
   PUBMED   14718166
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Umehara,T. and Horikoshi,M.
  TITLE     Transcription initiation factor IID-interactive histone chaperone
            CIA-II implicated in mammalian spermatogenesis
  JOURNAL   J Biol Chem 278 (37), 35660-35667 (2003)
   PUBMED   12842904
  REMARK    GeneRIF: data suggest that CIA-II is a histone chaperone and is
            implicated in the regulation of mammalian spermatogenesis
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001466.1 and BC036521.1.
            
            Summary: This gene encodes a member of the H3/H4 family of histone
            chaperone proteins and is similar to the anti-silencing function-1
            gene in yeast. The encoded protein is the substrate of the
            tousled-like kinase family of cell cycle-regulated kinases, and may
            play a key role in modulating the nucleosome structure of chromatin
            by ensuring a constant supply of histones at sites of nucleosome
            assembly. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.93938.1, BC036521.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263382.8/ ENSP00000263382.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..202
                     /product="histone chaperone ASF1B"
                     /note="CCG1-interacting factor A-II; hAsf1; hAsf1b;
                     hCIA-II; anti-silencing function protein 1 homolog B; ASF1
                     anti-silencing function 1 homolog B"
                     /calculated_mol_wt=22302
     Region          1..156
                     /region_name="Interaction with histone H3.
                     /evidence=ECO:0000250|UniProtKB:Q9Y294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVP2.1)"
     Region          1..155
                     /region_name="Interaction with CHAF1B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVP2.1)"
     Region          1..154
                     /region_name="ASF1_hist_chap"
                     /note="ASF1 like histone chaperone; pfam04729"
                     /db_xref="CDD:461412"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TLK2.
                     /evidence=ECO:0000269|PubMed:20016786,
                     ECO:0000269|PubMed:35136069; propagated from
                     UniProtKB/Swiss-Prot (Q9NVP2.1)"
     CDS             1..202
                     /gene="ASF1B"
                     /gene_synonym="CIA-II"
                     /coded_by="NM_018154.3:134..742"
                     /db_xref="CCDS:CCDS12306.1"
                     /db_xref="GeneID:55723"
                     /db_xref="HGNC:HGNC:20996"
                     /db_xref="MIM:609190"
ORIGIN      
        1 makvsvlnva vlenpspfhs pfrfeisfec sealaddlew kiiyvgsaes eefdqildsv
       61 lvgpvpagrh mfvfqadapn pslipetdav gvtvvlitct yhgqefirvg yyvnneylnp
      121 elrenppmkp dfsqlqrnil asnprvtrfh inwdnnmdrl eaietqdpsl gcglplnctp
      181 ikglglpgci pgllpensmd ci
//
LOCUS       NP_002225                613 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium voltage-gated channel subfamily A member 5 [Homo
            sapiens].
ACCESSION   NP_002225
VERSION     NP_002225.2
DBSOURCE    REFSEQ: accession NM_002234.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Rahman,R.A., Zaman,B., Khan,M.R., Islam,M.S. and Rashid,M.H.
  TITLE     Computational Studies Show How the H463R Mutation Turns hKv1.5 into
            an Inactivation State
  JOURNAL   J Phys Chem B 128 (2), 429-439 (2024)
   PUBMED   38179652
  REMARK    GeneRIF: Computational Studies Show How the H463R Mutation Turns
            hKv1.5 into an Inactivation State.
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Vera-Zambrano,A., Lago-Docampo,M., Gallego,N.,
            Franco-Gonzalez,J.F., Morales-Cano,D., Cruz-Utrilla,A.,
            Villegas-Esguevillas,M., Fernandez-Malave,E., Escribano-Subias,P.,
            Tenorio-Castano,J.A., Perez-Vizcaino,F., Valverde,D., Gonzalez,T.
            and Cogolludo,A.
  CONSRTM   Spanish group of Ion Channels in Pulmonary Hypertension (SICPH)
            investigators
  TITLE     Novel Loss-of-Function KCNA5 Variants in Pulmonary Arterial
            Hypertension
  JOURNAL   Am J Respir Cell Mol Biol 69 (2), 147-158 (2023)
   PUBMED   36917789
  REMARK    GeneRIF: Novel Loss-of-Function KCNA5 Variants in Pulmonary
            Arterial Hypertension.
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Macias,A., de la Cruz,A., Peraza,D.A., Benito-Bueno,A., Gonzalez,T.
            and Valenzuela,C.
  TITLE     KV1.5-KVbeta1.3 Recycling Is PKC-Dependent
  JOURNAL   Int J Mol Sci 22 (3), 1336 (2021)
   PUBMED   33572906
  REMARK    GeneRIF: KV1.5-KVbeta1.3 Recycling Is PKC-Dependent.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Farah,A., Kabbage,M., Atafi,S., Gabteni,A.J., Barbirou,M.,
            Madhioub,M., Hamzaoui,L., Mohamed,M.A., Touinsi,H., Kchaou,A.O.,
            Chelbi,E., Boubaker,S., Abderrazek,R.B. and Bouhaouala-Zahar,B.
  TITLE     Selective expression of KCNA5 and KCNB1 genes in gastric and
            colorectal carcinoma
  JOURNAL   BMC Cancer 20 (1), 1179 (2020)
   PUBMED   33267786
  REMARK    GeneRIF: Selective expression of KCNA5 and KCNB1 genes in gastric
            and colorectal carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Mays,D.J., Foose,J.M., Philipson,L.H. and Tamkun,M.M.
  TITLE     Localization of the Kv1.5 K+ channel protein in explanted cardiac
            tissue
  JOURNAL   J Clin Invest 96 (1), 282-292 (1995)
   PUBMED   7615797
REFERENCE   7  (residues 1 to 613)
  AUTHORS   Crumb,W.J. Jr., Wible,B., Arnold,D.J., Payne,J.P. and Brown,A.M.
  TITLE     Blockade of multiple human cardiac potassium currents by the
            antihistamine terfenadine: possible mechanism for
            terfenadine-associated cardiotoxicity
  JOURNAL   Mol Pharmacol 47 (1), 181-190 (1995)
   PUBMED   7838127
REFERENCE   8  (residues 1 to 613)
  AUTHORS   Curran,M.E., Landes,G.M. and Keating,M.T.
  TITLE     Molecular cloning, characterization, and genomic localization of a
            human potassium channel gene
  JOURNAL   Genomics 12 (4), 729-737 (1992)
   PUBMED   1349297
REFERENCE   9  (residues 1 to 613)
  AUTHORS   Tamkun,M.M., Knoth,K.M., Walbridge,J.A., Kroemer,H., Roden,D.M. and
            Glover,D.M.
  TITLE     Molecular cloning and characterization of two voltage-gated K+
            channel cDNAs from human ventricle
  JOURNAL   FASEB J 5 (3), 331-337 (1991)
   PUBMED   2001794
REFERENCE   10 (residues 1 to 613)
  AUTHORS   Philipson,L.H., Hice,R.E., Schaefer,K., LaMendola,J., Bell,G.I.,
            Nelson,D.J. and Steiner,D.F.
  TITLE     Sequence and functional expression in Xenopus oocytes of a human
            insulinoma and islet potassium channel
  JOURNAL   Proc Natl Acad Sci U S A 88 (1), 53-57 (1991)
   PUBMED   1986382
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005906.1, BC099665.3,
            BM692565.1 and BM663787.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 29, 2002 this sequence version replaced NP_002225.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ino channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member contains six
            membrane-spanning domains with a shaker-type repeat in the fourth
            segment. It belongs to the delayed rectifier class, the function of
            which could restore the resting membrane potential of beta cells
            after depolarization and thereby contribute to the regulation of
            insulin secretion. This gene is intronless, and the gene is
            clustered with genes KCNA1 and KCNA6 on chromosome 12. Defects in
            this gene are a cause of familial atrial fibrillation type 7
            (ATFB7). [provided by RefSeq, May 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803613.198188.1,
                                        SRR1660807.110520.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252321.5/ ENSP00000252321.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.32"
     Protein         1..613
                     /product="potassium voltage-gated channel subfamily A
                     member 5"
                     /note="cardiac potassium channel; potassium channel 1;
                     insulinoma and islet potassium channel; voltage-gated
                     potassium channel protein Kv1.5; voltage-gated potassium
                     channel HK2; voltage-gated potassium channel subunit
                     Kv1.5; potassium voltage-gated channel, shaker-related
                     subfamily, member 5; potassium channel, voltage gated
                     shaker related subfamily A, member 5"
                     /calculated_mol_wt=67097
     Region          1..211
                     /region_name="Tetramerization domain.
                     /evidence=ECO:0000305|PubMed:20018952"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          1..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          61..82
                     /region_name="2 X 11 AA tandem repeat of
                     D-[SP]-G-V-R-P-L-P-P-L-P"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          120..246
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Site            248..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          249..526
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          282..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            324..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            396..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          418..431
                     /region_name="S4-S5 linker.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            432..453
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          480..485
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            495..523
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          532..559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P22460.4)"
     Region          611..613
                     /region_name="PDZ-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P22460.4)"
     CDS             1..613
                     /gene="KCNA5"
                     /gene_synonym="ATFB7; HCK1; HK2; HPCN1; KV1.5; PCN1"
                     /coded_by="NM_002234.4:270..2111"
                     /db_xref="CCDS:CCDS8536.1"
                     /db_xref="GeneID:3741"
                     /db_xref="HGNC:HGNC:6224"
                     /db_xref="MIM:176267"
ORIGIN      
        1 meialvplen ggamtvrggd earagcgqat ggelqcppta glsdgpkepa pkgrgaqrda
       61 dsgvrplppl pdpgvrplpp lpeelprprr pppedeeeeg dpglgtvedq algtaslhhq
      121 rvhinisglr fetqlgtlaq fpntllgdpa krlryfdplr neyffdrnrp sfdgilyyyq
      181 sggrlrrpvn vsldvfadei rfyqlgdeam erfredegfi keeekplprn efqrqvwlif
      241 eypessgsar aiaivsvlvi lisiitfcle tlpefrdere llrhppaphq ppapapgang
      301 sgvmappsgp tvapllprtl adpffivett cviwftfell vrffacpska gfsrnimnii
      361 dvvaifpyfi tlgtelaeqq pggggggqng qqamslailr virlvrvfri fklsrhskgl
      421 qilgktlqas mrelglliff lfigvilfss avyfaeadnq gthfssipda fwwavvtmtt
      481 vgygdmrpit vggkivgslc aiagvltial pvpvivsnfn yfyhretdhe epavlkeeqg
      541 tqsqgpgldr gvqrkvsgsr gsfckaggtl enadsarrgs cplekcnvka ksnvdlrrsl
      601 yalcldtsre tdl
//
LOCUS       NP_001007123             749 aa            linear   PRI 20-NOV-2025
DEFINITION  fibronectin type III and SPRY domain-containing protein 2 isoform a
            [Homo sapiens].
ACCESSION   NP_001007123 XP_058721
VERSION     NP_001007123.1
DBSOURCE    REFSEQ: accession NM_001007122.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Benson,M.A., Tinsley,C.L., Waite,A.J., Carlisle,F.A., Sweet,S.M.M.,
            Ehler,E., George,C.H., Lai,F.A., Martin-Rendon,E. and Blake,D.J.
  TITLE     Ryanodine receptors are part of the myospryn complex in cardiac
            muscle
  JOURNAL   Sci Rep 7 (1), 6312 (2017)
   PUBMED   28740084
  REMARK    GeneRIF: Data identify a novel muscle-expressed TRIM-related
            protein minispryn, encoded by Fsd2, that has extensive sequence
            similarity with the C-terminus of Cmya5. They appear to have
            originated by a chromosomal duplication and are found within
            evolutionarily-conserved gene clusters on different chromosomes.
            Both proteins co-localize with RyR2 at the junctional sarcoplasmic
            reticulum of isolated cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 749)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 749)
  AUTHORS   Dong,C., Beecham,A., Slifer,S., Wang,L., Blanton,S.H., Wright,C.B.,
            Rundek,T. and Sacco,R.L.
  TITLE     Genomewide linkage and peakwide association analyses of carotid
            plaque in Caribbean Hispanics
  JOURNAL   Stroke 41 (12), 2750-2756 (2010)
   PUBMED   20966410
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK122875.1, AC105339.9 and
            AL833295.1.
            
            On Nov 22, 2004 this sequence version replaced XP_058721.2.
            
            Summary: This gene encodes a protein that belongs to the FN3/SPRY
            family of proteins. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122875.1, AL833295.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968832,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334574.12/ ENSP00000335651.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..749
                     /product="fibronectin type III and SPRY domain-containing
                     protein 2 isoform a"
                     /note="SPRY domain containing 1; fibronectin type III and
                     SPRY domain-containing protein 2; SPRY domain-containing
                     protein 1; minispryn"
                     /calculated_mol_wt=85255
     Region          188..>333
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          <371..>561
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          372..457
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Site            order(372,440,455)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(456..457,459..460)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          565..740
                     /region_name="SPRY_PRY_TRIM76_like"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 76 (TRIM76)-like; cd12899"
                     /db_xref="CDD:293956"
     CDS             1..749
                     /gene="FSD2"
                     /gene_synonym="SPRYD1"
                     /coded_by="NM_001007122.4:183..2432"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45332.1"
                     /db_xref="GeneID:123722"
                     /db_xref="HGNC:HGNC:18024"
ORIGIN      
        1 meeesgeelg ldrstpkdfh fyhmdlydse drlhlfpeen trmrkvvqae manesrgagd
       61 gkaqrdlqee vdelvhlygl eddhelgdef vdeniprtgv seyppymmkr rdpareqrdw
      121 rlsgeaaeae dlgfggwgsa gqcqdlreay rythgrasee yecyvipeee deeeaadvfc
      181 vtcktpiraf qkvfdehkeh eviplneale sakdeihknm yklekqiiem enfanhleev
      241 fitveenfgk qeqnfeshyn eiletlaqky eekiqalgek kkeklealyg qlvscgenld
      301 tckelmetie emcheekvdf ikdavamadr lgkflktktd veisaqpefe dqtldfsdve
      361 qlmgsintip apsapvinpq vpnsatgssv rvcwslysdd tvesyqlsyr pvqdsspgtd
      421 qaeftvtvke tycsvtnlvp ntqyefwvta hnragpspss eravymtaps ppiiktkeir
      481 sceeavlicw esgnlnpvds ytveltqaes peasgvtesv vgiptcesvv qlqpgrsyii
      541 yvralnmggp svrsepatvh tigsyfrlnk dtchpwltis edgltavrse rrtparelsp
      601 sdthftrcva vmgnlipvrg hhywevevde hldyrvgvaf advrkqedlg anclswcmrh
      661 tfassrhkye flhnrttpdi ritvppkkig illdyehskl sffnvdlsqh lytfscqlhe
      721 fvhpcfslek pgclkvhngi smpkhvtfy
//
LOCUS       NP_000375               4563 aa            linear   PRI 20-NOV-2025
DEFINITION  apolipoprotein B-100 precursor [Homo sapiens].
ACCESSION   NP_000375
VERSION     NP_000375.3
DBSOURCE    REFSEQ: accession NM_000384.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4563)
  AUTHORS   Danner,R., Prochniak,L.M., Pereckas,M., Rouse,J.R., Wahhab,A.,
            Hackner,L.G. and Lochhead,R.B.
  TITLE     Identification of Major Histocompatibility Complex Class II
            Epitopes From Lyme Autoantigen Apolipoprotein B-100 and Borrelia
            burgdorferi Mcp4 in Murine Lyme Arthritis
  JOURNAL   J Infect Dis 230 (Supplement_1), S27-S39 (2024)
   PUBMED   39140726
  REMARK    GeneRIF: Identification of Major Histocompatibility Complex Class
            II Epitopes From Lyme Autoantigen Apolipoprotein B-100 and Borrelia
            burgdorferi Mcp4 in Murine Lyme Arthritis.
REFERENCE   2  (residues 1 to 4563)
  AUTHORS   De Oliveira-Gomes,D., Joshi,P.H., Peterson,E.D., Rohatgi,A.,
            Khera,A. and Navar,A.M.
  TITLE     Apolipoprotein B: Bridging the Gap Between Evidence and Clinical
            Practice
  JOURNAL   Circulation 150 (1), 62-79 (2024)
   PUBMED   38950110
  REMARK    GeneRIF: Apolipoprotein B: Bridging the Gap Between Evidence and
            Clinical Practice.
            Review article
REFERENCE   3  (residues 1 to 4563)
  AUTHORS   Mahsoub,N., Almenshawy,A., Taki Eldin,A.M., Abdel Hay,N.M.,
            Youssef,A.R., El-Farahaty,R.M., El-Sayed,K., Osman,A.M. and
            Elhennawy,E.S.
  TITLE     Association between Apo B, LDL-R and PCSK9 gene polymorphisms with
            coronary artery diseases in Egyptians
  JOURNAL   Mol Biol Rep 51 (1), 752 (2024)
   PUBMED   38874786
  REMARK    GeneRIF: Association between Apo B, LDL-R and PCSK9 gene
            polymorphisms with coronary artery diseases in Egyptians.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 4563)
  AUTHORS   Burnett,J.R., Hooper,A.J. and Hegele,R.A.
  TITLE     APOB-Related Familial Hypobetalipoproteinemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   33983694
REFERENCE   5  (residues 1 to 4563)
  AUTHORS   Ison,H.E., Clarke,S.L. and Knowles,J.W.
  TITLE     Familial Hypercholesterolemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24404629
REFERENCE   6  (residues 1 to 4563)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 4563)
  AUTHORS   Deeb,S.S., Failor,R.A., Brown,B.G., Brunzell,J.D., Albers,J.J.,
            Motulsky,A.G. and Wijsman,E.
  TITLE     Association of apolipoprotein B gene variants with plasma apoB and
            low density lipoprotein (LDL) cholesterol levels
  JOURNAL   Hum Genet 88 (4), 463-470 (1992)
   PUBMED   1346774
REFERENCE   8  (residues 1 to 4563)
  AUTHORS   Sehayek,E. and Eisenberg,S.
  TITLE     Mechanisms of inhibition by apolipoprotein C of apolipoprotein
            E-dependent cellular metabolism of human triglyceride-rich
            lipoproteins through the low density lipoprotein receptor pathway
  JOURNAL   J Biol Chem 266 (27), 18259-18267 (1991)
   PUBMED   1917954
REFERENCE   9  (residues 1 to 4563)
  AUTHORS   Navajas,M., Laurent,A.M., Moreel,J.F., Ragab,A., Cambou,J.P.,
            Cuny,G., Cambien,F. and Roizes,G.
  TITLE     Detection by denaturing gradient gel electrophoresis of a new
            polymorphism in the apolipoprotein B gene
  JOURNAL   Hum Genet 86 (1), 91-93 (1990)
   PUBMED   1979313
REFERENCE   10 (residues 1 to 4563)
  AUTHORS   Higuchi,K., Hospattankar,A.V., Law,S.W., Meglin,N., Cortright,J.
            and Brewer,H.B. Jr.
  TITLE     Human apolipoprotein B (apoB) mRNA: identification of two distinct
            apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA
            containing a premature in-frame translational stop codon, in both
            liver and intestine
  JOURNAL   Proc Natl Acad Sci U S A 85 (6), 1772-1776 (1988)
   PUBMED   2450346
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010872.8, KF456638.1 and
            AC115619.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 17, 2019 this sequence version replaced NP_000375.2.
            
            Summary: This gene product is the main apolipoprotein of
            chylomicrons and low density lipoproteins (LDL), and is the ligand
            for the LDL receptor. It occurs in plasma as two main isoforms,
            apoB-48 and apoB-100: the former is synthesized exclusively in the
            gut and the latter in the liver. The intestinal and the hepatic
            forms of apoB are encoded by a single gene from a single, very long
            mRNA. The two isoforms share a common N-terminal sequence. The
            shorter apoB-48 protein is produced after RNA editing of the
            apoB-100 transcript at residue 2180 (CAA->UAA), resulting in the
            creation of a stop codon, and early translation termination.
            Mutations in this gene or its regulatory region cause
            hypobetalipoproteinemia, normotriglyceridemic
            hypobetalipoproteinemia, and hypercholesterolemia due to
            ligand-defective apoB, diseases affecting plasma cholesterol and
            apoB levels. [provided by RefSeq, Dec 2019].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X04506.1, HM487065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233242.5/ ENSP00000233242.1
            RefSeq Select criteria :: based on single protein-coding transcript
            undergoes RNA editing  :: PMID: 16920700, 11727199
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.1"
     Protein         1..4563
                     /product="apolipoprotein B-100 precursor"
                     /note="apolipoprotein B-100; apolipoprotein B48;
                     apolipoprotein B (including Ag(x) antigen)"
                     /calculated_mol_wt=512801
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2765
     mat_peptide     28..4563
                     /product="apolipoprotein B-100"
                     /calculated_mol_wt=512801
     mat_peptide     28..2179
                     /product="apolipoprotein B-48"
                     /note="The intestinal-specific RNA editing of codon 2180
                     (CAA->UAA) creates a stop codon, resulting in early
                     translation termination"
                     /calculated_mol_wt=240777
     Region          32..126
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Bond            join(39,88)
                     /bond_type="disulfide"
     Region          46..597
                     /region_name="Vitellogenin_N"
                     /note="Lipoprotein amino terminal region; pfam01347"
                     /db_xref="CDD:460170"
     Bond            join(78,97)
                     /bond_type="disulfide"
     Site            185
                     /site_type="glycosylation"
     Bond            join(186,212)
                     /bond_type="disulfide"
     Region          232..306
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Bond            join(245,261)
                     /bond_type="disulfide"
     Bond            join(385,390)
                     /bond_type="disulfide"
     Bond            join(478,513)
                     /bond_type="disulfide"
     Region          632..937
                     /region_name="Vit_open_b-sht"
                     /note="Vitellinogen, open beta-sheet; pfam09172"
                     /db_xref="CDD:462702"
     Region          902..959
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Region          960..1071
                     /region_name="DUF1081"
                     /note="Domain of Unknown Function (DUF1081); pfam06448"
                     /db_xref="CDD:461916"
     Bond            join(966,976)
                     /bond_type="disulfide"
     Site            983
                     /site_type="glycosylation"
     Site            1112
                     /site_type="modified"
                     /note="polmitoylation site"
     Site            1368
                     /site_type="glycosylation"
     Site            1377
                     /site_type="glycosylation"
     Region          1448..>1865
                     /region_name="OM_channels"
                     /note="Porin superfamily. These outer membrane channels
                     share a beta-barrel structure that differ in strand and
                     shear number. Classical (gram-negative) porins are
                     non-specific channels for small hydrophillic molecules and
                     form 16 beta-stranded barrels (16,20)...; cl21487"
                     /db_xref="CDD:473880"
     Site            1523
                     /site_type="glycosylation"
     Site            2004
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Region          2043..2178
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Region          <2060..>2490
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
     Region          2180
                     /region_name="apoB-48 site of RNA editing"
                     /note="apoB-48, residue Gln(2180) is modified by RNA
                     editing from CAA to a stop codon UAA."
     Site            2239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            2560
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            2779
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            2982
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Region          3161..3236
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Region          3174..3184
                     /region_name="Basic (possible receptor binding region)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Bond            join(3194,3324)
                     /bond_type="disulfide"
     Site            3224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3358
                     /site_type="glycosylation"
     Region          3373..3393
                     /region_name="LDL receptor binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Region          3383..3516
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Region          3386..3394
                     /region_name="Basic (possible receptor binding region)"
                     /note="propagated from UniProtKB/Swiss-Prot (P04114.3)"
     Site            3411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3465
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            3895
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            4048
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            4052
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            4237
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Site            4431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P04114.3)"
     Region          4494..4550
                     /region_name="ApoB100_C"
                     /note="Apolipoprotein B100 C terminal; pfam12491"
                     /db_xref="CDD:463606"
     CDS             1..4563
                     /gene="APOB"
                     /gene_synonym="apoB-100; apoB-48; FCHL2; FLDB; LDLCQ4"
                     /coded_by="NM_000384.3:129..13820"
                     /db_xref="CCDS:CCDS1703.1"
                     /db_xref="GeneID:338"
                     /db_xref="HGNC:HGNC:603"
                     /db_xref="MIM:107730"
ORIGIN      
        1 mdpprpalla llalpallll llagaraeee mlenvslvcp kdatrfkhlr kytynyeaes
       61 ssgvpgtads rsatrinckv elevpqlcsf ilktsqctlk evygfnpegk allkktknse
      121 efaaamsrye lklaipegkq vflypekdep tyilnikrgi isallvppet eeakqvlfld
      181 tvygncsthf tvktrkgnva teisterdlg qcdrfkpirt gisplalikg mtrplstlis
      241 ssqscqytld akrkhvaeai ckeqhlflpf syknkygmva qvtqtlkled tpkinsrffg
      301 egtkkmglaf estkstsppk qaeavlktlq elkkltiseq niqranlfnk lvtelrglsd
      361 eavtsllpql ievsspitlq alvqcgqpqc sthilqwlkr vhanpllidv vtylvalipe
      421 psaqqlreif nmardqrsra tlyalshavn nyhktnptgt qelldianyl meqiqddctg
      481 dedytylilr vignmgqtme qltpelkssi lkcvqstkps lmiqkaaiqa lrkmepkdkd
      541 qevllqtfld daspgdkrla aylmlmrsps qadinkivqi lpweqneqvk nfvashiani
      601 lnseeldiqd lkklvkealk esqlptvmdf rkfsrnyqly ksvslpsldp asakiegnli
      661 fdpnnylpke smlkttltaf gfasadliei glegkgfept lealfgkqgf fpdsvnkaly
      721 wvngqvpdgv skvlvdhfgy tkddkheqdm vngimlsvek likdlkskev pearaylril
      781 geelgfaslh dlqllgklll mgartlqgip qmigevirkg skndfflhyi fmenafelpt
      841 gaglqlqiss sgviapgaka gvklevanmq aelvakpsvs vefvtnmgii ipdfarsgvq
      901 mntnffhesg leahvalkag klkfiipspk rpvkllsggn tlhlvsttkt evipplienr
      961 qswsvckqvf pglnyctsga ysnasstdsa syypltgdtr lelelrptge ieqysvsaty
     1021 elqredralv dtlkfvtqae gakqteatmt fkynrqsmtl ssevqipdfd vdlgtilrvn
     1081 destegktsy rltldiqnkk itevalmghl scdtkeerki kgvisiprlq aearseilah
     1141 wspaklllqm dssataygst vskrvawhyd eekiefewnt gtnvdtkkmt snfpvdlsdy
     1201 pkslhmyanr lldhrvpqtd mtfrhvgskl ivamsswlqk asgslpytqt lqdhlnslke
     1261 fnlqnmglpd fhipenlflk sdgrvkytln knslkieipl pfggkssrdl kmletvrtpa
     1321 lhfksvgfhl psrefqvptf tipklyqlqv pllgvldlst nvysnlynws asysggntst
     1381 dhfslraryh mkadsvvdll synvqgsget tydhkntftl scdgslrhkf ldsnikfshv
     1441 eklgnnpvsk gllifdasss wgpqmsasvh ldskkkqhlf vkevkidgqf rvssfyakgt
     1501 yglscqrdpn tgrlngesnl rfnssylqgt nqitgryedg tlsltstsdl qsgiikntas
     1561 lkyenyeltl ksdtngkykn fatsnkmdmt fskqnallrs eyqadyeslr ffsllsgsln
     1621 shglelnadi lgtdkinsga hkatlrigqd gistsattnl kcsllvlene lnaelglsga
     1681 smklttngrf rehnakfsld gkaaltelsl gsayqamilg vdsknifnfk vsqeglklsn
     1741 dmmgsyaemk fdhtnslnia glsldfsskl dniyssdkfy kqtvnlqlqp yslvttlnsd
     1801 lkynaldltn ngklrleplk lhvagnlkga yqnneikhiy aissaalsas ykadtvakvq
     1861 gvefshrlnt diaglasaid mstnynsdsl hfsnvfrsvm apftmtidah tngngklalw
     1921 gehtgqlysk fllkaeplaf tfshdykgst shhlvsrksi saalehkvsa lltpaeqtgt
     1981 wklktqfnnn eysqdldayn tkdkigvelt grtladltll dspikvplll sepiniidal
     2041 emrdavekpq eftivafvky dknqdvhsin lpffetlqey fernrqtiiv vlenvqrnlk
     2101 hinidqfvrk yraalgklpq qandylnsfn werqvshake kltaltkkyr itendiqial
     2161 ddakinfnek lsqlqtymiq fdqyikdsyd lhdlkiaian iideiieklk sldehyhirv
     2221 nlvktihdlh lfienidfnk sgsstaswiq nvdtkyqiri qiqeklqqlk rhiqnidiqh
     2281 lagklkqhie aidvrvlldq lgttisferi ndilehvkhf vinligdfev aekinafrak
     2341 vhelieryev dqqiqvlmdk lvelahqykl ketiqklsnv lqqvkikdyf eklvgfidda
     2401 vkklnelsfk tfiedvnkfl dmlikklksf dyhqfvdetn dkirevtqrl ngeiqalelp
     2461 qkaealklfl eetkatvavy leslqdtkit liinwlqeal ssaslahmka kfretledtr
     2521 drmyqmdiqq elqrylslvg qvystlvtyi sdwwtlaakn ltdfaeqysi qdwakrmkal
     2581 veqgftvpei ktilgtmpaf evslqalqka tfqtpdfivp ltdlripsvq infkdlknik
     2641 ipsrfstpef tilntfhips ftidfvemkv kiirtidqml nselqwpvpd iylrdlkved
     2701 iplaritlpd frlpeiaipe fiiptlnlnd fqvpdlhipe fqlphishti evptfgklys
     2761 ilkiqsplft ldanadigng ttsaneagia asitakgesk levlnfdfqa naqlsnpkin
     2821 plalkesvkf sskylrtehg semlffgnai egksntvasl htekntlels ngvivkinnq
     2881 ltldsntkyf hklnipkldf ssqadlrnei ktllkaghia wtssgkgswk wacprfsdeg
     2941 thesqisfti egpltsfgls nkinskhlrv nqnlvyesgs lnfskleiqs qvdsqhvghs
     3001 vltakgmalf gegkaeftgr hdahlngkvi gtlknslffs aqpfeitast nnegnlkvrf
     3061 plrltgkidf lnnyalflsp saqqaswqvs arfnqykynq nfsagnneni meahvginge
     3121 anldflnipl tipemrlpyt iittpplkdf slwektglke flkttkqsfd lsvkaqykkn
     3181 khrhsitnpl avlcefisqs iksfdrhfek nrnnaldfvt ksynetkikf dkykaekshd
     3241 elprtfqipg ytvpvvnvev spftiemsaf gyvfpkavsm psfsilgsdv rvpsytlilp
     3301 slelpvlhvp rnlklslpdf kelctishif ipamgnityd fsfkssvitl ntnaelfnqs
     3361 divahllsss ssvidalqyk legttrltrk rglklatals lsnkfvegsh nstvslttkn
     3421 mevsvatttk aqipilrmnf kqelngntks kptvsssmef kydfnssmly stakgavdhk
     3481 lslesltsyf siesstkgdv kgsvlsreys gtiaseanty lnskstrssv klqgtskidd
     3541 iwnlevkenf ageatlqriy slwehstknh lqleglfftn gehtskatle lspwqmsalv
     3601 qvhasqpssf hdfpdlgqev alnantknqk irwknevrih sgsfqsqvel sndqekahld
     3661 iagsleghlr flkniilpvy dkslwdflkl dvttsigrrq hlrvstafvy tknpngysfs
     3721 ipvkvladkf iipglklndl nsvlvmptfh vpftdlqvps ckldfreiqi ykklrtssfa
     3781 lnlptlpevk fpevdvltky sqpedslipf feitvpesql tvsqftlpks vsdgiaaldl
     3841 navankiadf elptiivpeq tieipsikfs vpagivipsf qaltarfevd spvynatwsa
     3901 slknkadyve tvldstcsst vqfleyelnv lgthkiedgt lasktkgtfa hrdfsaeyee
     3961 dgkyeglqew egkahlniks paftdlhlry qkdkkgists aaspavgtvg mdmdedddfs
     4021 kwnfyyspqs spdkkltifk telrvresde etqikvnwee eaasglltsl kdnvpkatgv
     4081 lydyvnkyhw ehtgltlrev ssklrrnlqn naewvyqgai rqiddidvrf qkaasgttgt
     4141 yqewkdkaqn lyqelltqeg qasfqglkdn vfdglvrvtq efhmkvkhli dslidflnfp
     4201 rfqfpgkpgi ytreelctmf irevgtvlsq vyskvhngse ilfsyfqdlv itlpfelrkh
     4261 klidvismyr ellkdlskea qevfkaiqsl kttevlrnlq dllqfifqli ednikqlkem
     4321 kftylinyiq deintifsdy ipyvfkllke nlclnlhkfn efiqnelqea sqelqqihqy
     4381 imalreeyfd psivgwtvky yeleekivsl iknllvalkd fhseyivsas nftsqlssqv
     4441 eqflhrniqe ylsiltdpdg kgkekiaels ataqeiiksq aiatkkiisd yhqqfryklq
     4501 dfsdqlsdyy ekfiaeskrl idlsiqnyht fliyitellk klqsttvmnp ymklapgelt
     4561 iil
//
LOCUS       NP_443135               1024 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-tubulin complex component 5 isoform a [Homo sapiens].
ACCESSION   NP_443135
VERSION     NP_443135.3
DBSOURCE    REFSEQ: accession NM_052903.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   Izumi,N., Fumoto,K., Izumi,S. and Kikuchi,A.
  TITLE     GSK-3beta regulates proper mitotic spindle formation in cooperation
            with a component of the gamma-tubulin ring complex, GCP5
  JOURNAL   J Biol Chem 283 (19), 12981-12991 (2008)
   PUBMED   18316369
  REMARK    GeneRIF: GSK-3beta regulates the localization of gamma-tubulin ring
            complex, including GCP5, to the spindle poles, thereby controlling
            the formation of proper mitotic spindles
REFERENCE   5  (residues 1 to 1024)
  AUTHORS   Bittel,D.C., Kibiryeva,N. and Butler,M.G.
  TITLE     Expression of 4 genes between chromosome 15 breakpoints 1 and 2 and
            behavioral outcomes in Prader-Willi syndrome
  JOURNAL   Pediatrics 118 (4), e1276-e1283 (2006)
   PUBMED   16982806
  REMARK    GeneRIF: quantitated mRNA levels of NIPA2, NIPA2,l CYFIP1, and GCP5
            in Prader-Willi syndrome and correlated levels with psychological
            and behavior scales
REFERENCE   6  (residues 1 to 1024)
  AUTHORS   Chai,J.H., Locke,D.P., Greally,J.M., Knoll,J.H., Ohta,T., Dunai,J.,
            Yavor,A., Eichler,E.E. and Nicholls,R.D.
  TITLE     Identification of four highly conserved genes between breakpoint
            hotspots BP1 and BP2 of the Prader-Willi/Angelman syndromes
            deletion region that have undergone evolutionary transposition
            mediated by flanking duplicons
  JOURNAL   Am J Hum Genet 73 (4), 898-925 (2003)
   PUBMED   14508708
  REMARK    GeneRIF: located in the genomic domain between break points 1 and 2
            on chromosome 15, of the Prader-Willi/Angelman syndromes
REFERENCE   7  (residues 1 to 1024)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 1024)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   9  (residues 1 to 1024)
  AUTHORS   Murphy,S.M., Preble,A.M., Patel,U.K., O'Connell,K.L., Dias,D.P.,
            Moritz,M., Agard,D., Stults,J.T. and Stearns,T.
  TITLE     GCP5 and GCP6: two new members of the human gamma-tubulin complex
  JOURNAL   Mol Biol Cell 12 (11), 3340-3352 (2001)
   PUBMED   11694571
REFERENCE   10 (residues 1 to 1024)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB067486.2 and BC071560.1.
            
            On Aug 30, 2007 this sequence version replaced NP_443135.2.
            
            Transcript Variant: This variant (1) encodes isoform a. Isoforms a
            and b are identical in length but differ in their C-termini.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC071560.1, AB067486.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000615383.5/ ENSP00000480316.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q11.2"
     Protein         1..1024
                     /product="gamma-tubulin complex component 5 isoform a"
                     /note="gamma-tubulin complex component GCP5; gamma-tubulin
                     complex component 5; tubulin gamma complex associated
                     protein 5"
                     /calculated_mol_wt=118190
     Region          15..108
                     /region_name="GCP5_NTD"
                     /note="N-terminal domain of gamma-tubulin complex
                     component 5 (GCP-5) and similar proteins; cd22572"
                     /db_xref="CDD:439339"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT8.1)"
     Region          271..577
                     /region_name="GCP_N_terminal"
                     /note="Gamma tubulin complex component N-terminal;
                     pfam17681"
                     /db_xref="CDD:465456"
     Region          521..545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT8.1)"
     Region          716..1017
                     /region_name="GCP_C_terminal"
                     /note="Gamma tubulin complex component C-terminal;
                     pfam04130"
                     /db_xref="CDD:461187"
     CDS             1..1024
                     /gene="TUBGCP5"
                     /gene_synonym="GCP5"
                     /coded_by="NM_052903.6:27..3101"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73698.1"
                     /db_xref="GeneID:114791"
                     /db_xref="HGNC:HGNC:18600"
                     /db_xref="MIM:608147"
ORIGIN      
        1 marhgppwsr ldaqqerdvr elvrgvaglq deadpnfqla lnfawsnfrf hrfldvnshk
       61 iektiegiye kfvihsdlsk aaswkrltee flnaplpsik eiktdahysi lslllclsds
      121 psnssyvetp rnkevekkdd fdwgkylmed eemdigpymd tpnwseesee endqqplsre
      181 dsgiqvdrtp leeqdqnrkl dpciswkdep ddrswlehhv vhqywtarps qfphslhlhs
      241 nlaavwdqhl yssdplyvpd drvlvtetqv iretlwllsg vkklfifqli dgkvtvrnni
      301 ivthlthscl rsvleqiaay gqvvfrlqef idevmghsse smlpgsgsvp kksteapfrt
      361 yqafmwalyk yfisfkeela eiekciinnd ttitlaivvd klaprlsqlk vlhkvfstgv
      421 aevppdtrnv vrashllntl ykaileydnv geaseqtvsl lfslwvetvr pylqtvdewi
      481 vhghlwdgar efiiqrnknv pvnhrdfwya tytlysvsek teneekmsdn asassgsdqg
      541 pssrqhtmvs flkpvlkqii magksmqllk nlqcaesttc qagardaerk slytlflesv
      601 qsrlrhgeds tpqvlteqqa tkenlmkmqs iaeshleldd vhdpllainf armyleqsdf
      661 hekfaggdvc vdrssesvtc qtfeltlrsc lyphidkqyl dccgnlmqtl kkdyrlveyl
      721 qamrnfflme ggdtmydfyt sifdkireke twqnvsflnv qlqeavgqry pedssrlsis
      781 fenvdtakkk lpvhildglt lsykvpwpvd ivislecqki ynqvfllllq ikwakysldv
      841 llfgelvsta ekprlkegli heqdtvaqfg pqkepvrqqi hrmfllrvkl mhfvnslhny
      901 imtrilhstg lefqhqveea kdldqlikih yrylstihdr cllrekvsfv keaimkvlnl
      961 almfadgwqa glgtwrmesi ekmesdfknc hmflvtilnk avcrgsfphl eslalslmag
     1021 meqs
//
LOCUS       NP_001315580             417 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 5
            [Homo sapiens].
ACCESSION   NP_001315580
VERSION     NP_001315580.1
DBSOURCE    REFSEQ: accession NM_001328651.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358075.10.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (9) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (5) is
            shorter at the N-terminus compared to isoform 1. Variants 6, 7, 8,
            and 9 all encode the same isoform (5).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.199728.1,
                                           SRR18074968.2492493.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..417
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 5"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=49060
     Region          15..123
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(28,46,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(69,96)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          128..288
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Site            order(151,158,169..171,173..175,177..178,181..182,
                     184..185,188..189,192,208,211..212,215,219,222,248..249,
                     252,255)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:214016"
     Region          307..410
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(321,339,341..342,359,361)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(360,371,393,396,400)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..417
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_001328651.1:78..1331"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 mtsavpngmk dssvslqdae wywgdisree vndklrdmpd gtflvrdast kmqgdytltl
       61 rkggnnklik iyhrdgkygf sdpltfnsvv elinhyhhes laqynpkldv klmypvsryq
      121 qdqlvkedni davgkklqey hsqyqekske ydrlyeeytr tsqeiqmkrt aieafnetik
      181 ifeeqchtqe qhskeyierf rregnekeie rimmnydklk srlgeihdsk mrleqdlknq
      241 aldnreidkk mnsikpdliq lrkirdqhlv wlnhkgvrqk rlnvwlgikn edadenyfin
      301 eedenlphyd ektwfvedin rvqaedllyg kpdgaflire sskkgcyacs vvadgevkhc
      361 viystargyg faepynlyss lkelvlhyqq tslvqhndsl nvrlaypvha qmpslcr
//
LOCUS       NP_001309119            1260 aa            linear   PRI 20-NOV-2025
DEFINITION  contactin-associated protein-like 4 isoform 10 [Homo sapiens].
ACCESSION   NP_001309119
VERSION     NP_001309119.1
DBSOURCE    REFSEQ: accession NM_001322190.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1260)
  AUTHORS   Hu,W., Wang,M., Sun,G., Zhang,L. and Lu,H.
  TITLE     Early B Cell Factor 3 (EBF3) attenuates Parkinson's disease through
            directly regulating contactin-associated protein-like 4 (CNTNAP4)
            transcription: An experimental study
  JOURNAL   Cell Signal 118, 111139 (2024)
   PUBMED   38479556
  REMARK    GeneRIF: Early B Cell Factor 3 (EBF3) attenuates Parkinson's
            disease through directly regulating contactin-associated
            protein-like 4 (CNTNAP4) transcription: An experimental study.
REFERENCE   2  (residues 1 to 1260)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1260)
  AUTHORS   Zhang,W., Zhou,M., Lu,W., Gong,J., Gao,F., Li,Y., Xu,X., Lin,Y.,
            Zhang,X., Ding,L., Zhang,Z., Li,G., Chen,X., Sun,X., Zhu,X., Xu,P.
            and Zhang,Y.
  TITLE     CNTNAP4 deficiency in dopaminergic neurons initiates parkinsonian
            phenotypes
  JOURNAL   Theranostics 10 (7), 3000-3021 (2020)
   PUBMED   32194851
  REMARK    GeneRIF: CNTNAP4 deficiency in dopaminergic neurons initiates
            parkinsonian phenotypes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1260)
  AUTHORS   Shangguan,Y., Xu,X., Ganbat,B., Li,Y., Wang,W., Yang,Y., Lu,X.,
            Du,C., Tian,X. and Wang,X.
  TITLE     CNTNAP4 Impacts Epilepsy Through GABAA Receptors Regulation:
            Evidence From Temporal Lobe Epilepsy Patients and Mouse Models
  JOURNAL   Cereb Cortex 28 (10), 3491-3504 (2018)
   PUBMED   28968899
  REMARK    GeneRIF: we demonstrated that the expression of
            contactin-associated protein-like 4 (CNTNAP4) was decreased in the
            temporal neocortex of epileptic patients
REFERENCE   5  (residues 1 to 1260)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Haralambieva,I.H., Lambert,N.D.,
            Pankratz,V.S. and Poland,G.A.
  TITLE     Genome-wide SNP associations with rubella-specific cytokine
            responses in measles-mumps-rubella vaccine recipients
  JOURNAL   Immunogenetics 66 (7-8), 493-499 (2014)
   PUBMED   24811271
REFERENCE   6  (residues 1 to 1260)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1260)
  AUTHORS   Nordgard,S.H., Johansen,F.E., Alnaes,G.I., Bucher,E., Syvanen,A.C.,
            Naume,B., Borresen-Dale,A.L. and Kristensen,V.N.
  TITLE     Genome-wide analysis identifies 16q deletion associated with
            survival, molecular subtypes, mRNA expression, and germline
            haplotypes in breast cancer patients
  JOURNAL   Genes Chromosomes Cancer 47 (8), 680-696 (2008)
   PUBMED   18398821
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1260)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 1260)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1260)
  AUTHORS   Spiegel,I., Salomon,D., Erne,B., Schaeren-Wiemers,N. and Peles,E.
  TITLE     Caspr3 and caspr4, two novel members of the caspr family are
            expressed in the nervous system and interact with PDZ domains
  JOURNAL   Mol Cell Neurosci 20 (2), 283-297 (2002)
   PUBMED   12093160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FO681478.1, AB100092.1,
            AC106741.3 and AC108125.4.
            
            Summary: This gene encodes a member of the neurexin protein family.
            Members of this family function in the vertebrate nervous system as
            cell adhesion molecules and receptors. This protein contains
            epidermal growth factor repeats and laminin G domains. In addition,
            it includes an F5/8 type C domain, discoidin/neuropilin- and
            fibrinogen-like domains, and thrombospondin N-terminal-like
            domains. This protein may also play a role in proper
            neurotransmission in the dopaminergic and GABAergic systems and
            mutations in this gene may be associated with certain psychiatric
            illnesses. A polymorphism in an intron of this gene may be
            associated with longevity. [provided by RefSeq, Apr 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.13045.1,
                                           SRR1803613.125746.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..1260
                     /product="contactin-associated protein-like 4 isoform 10"
                     /note="cell recognition molecule Caspr4; contactin
                     associated protein like 4"
                     /calculated_mol_wt=139876
     Region          54..176
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          212..>304
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          350..476
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          505..536
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          545..586
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     Region          556..>639
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; cl02436"
                     /db_xref="CDD:470578"
     Region          773..891
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          914..948
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          998..1128
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     CDS             1..1260
                     /gene="CNTNAP4"
                     /gene_synonym="CASPR4"
                     /coded_by="NM_001322190.2:263..4045"
                     /note="isoform 10 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS82015.1"
                     /db_xref="GeneID:85445"
                     /db_xref="HGNC:HGNC:18747"
                     /db_xref="MIM:610518"
ORIGIN      
        1 mgsvtgavlk tllllstqnw nrveagnsyd cddplvsalp qasfssssel ssshgpgfar
       61 lnrrdgaggw splvsnkyqw lqidlgerme vtavatqggy gssnwvtsyl lmfsdsgwnw
      121 kqyrqedsiw gfsgnanads vvyyrlqpsi karflrfipl ewnpkgrigm rievfgcayr
      181 sevvdldgks sllyrfdqks lspikdiisl kfktmqsdgi llhregpngd hitlqlrrar
      241 lfllinsgea klpststlvn ltlgsllddq hwhsvliqrl gkqvnftvde hrhhfharge
      301 fnlmnldyeg nvsfscsqpq smpvtflssr sylalpdfsg eeevsatfqf rtwnkaglll
      361 fselqlisgg illflsdgkl ksnlyqpgkl psditagvel ndgqwhsvsl sakknhlsva
      421 vdgqmasaap llgpeqiysg gtyyfggcpd ksfgskcksp lggfqgcmrl isisgkvvdl
      481 isvqqgslgn fsdlqidscg isdrclpnyc ehggecsqsw stfhcnctnt gyrgatchns
      541 iyeqsceayk hrgntsgfyy idsdgsgple pfllycnmte tawtiiqhng sdltrvrntn
      601 penpyagffe yvasmeqlqa tinraehceq eftyyckksr lvnkqdgtpl swwvgrtnet
      661 qtywggsspd lqkctcgleg ncidsqyycn cdadrnewtn dtgllaykeh lpvtkivitd
      721 tgrlhseaay klgpllcqgd rsfwnsasfd teasylhfpt fhgelsadvs fffkttassg
      781 vflenlgiad firielrspt vvtfsfdvgn gpfeisvqsp thfndnqwhh vrvernmkea
      841 slqvdqltpk tqpapadghv llqlnsqlfv ggtatrqrgf lgcirslqln gmtldleera
      901 qvtpevqpgc rghcssygkl crnggkcrer pigffcdctf saytgpfcsn eisayfgsgs
      961 sviynfqeny llsknsssha asfhgdmkls remikfsfrt trtpslllfv ssfykeylsv
     1021 iiakngslqi ryklnkyqep dvvnfdfknm adgqlhhimi nreegvvfie iddnrrrqvh
     1081 lssgtefsav kslvlgrile hsdvdqdtal agaqgftgcl savqlshvap lkaalhpshp
     1141 dpvtvtghvt esscmaqpgt datsrerths fadhsgtidd replanaiks dsavigglia
     1201 vvifillcit aiavriyqqk rlykrseakr senvdsaeav lkselniqna vnenqkeyff
//
LOCUS       NP_114428                552 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM234A [Homo sapiens].
ACCESSION   NP_114428
VERSION     NP_114428.1
DBSOURCE    REFSEQ: accession NM_032039.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Ding,K., de Andrade,M., Manolio,T.A., Crawford,D.C.,
            Rasmussen-Torvik,L.J., Ritchie,M.D., Denny,J.C., Masys,D.R.,
            Jouni,H., Pachecho,J.A., Kho,A.N., Roden,D.M., Chisholm,R. and
            Kullo,I.J.
  TITLE     Genetic variants that confer resistance to malaria are associated
            with red blood cell traits in African-Americans: an electronic
            medical record-based genome-wide association study
  JOURNAL   G3 (Bethesda) 3 (7), 1061-1068 (2013)
   PUBMED   23696099
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Teckchandani,A., Toida,N., Goodchild,J., Henderson,C., Watts,J.,
            Wollscheid,B. and Cooper,J.A.
  TITLE     Quantitative proteomics identifies a Dab2/integrin module
            regulating cell migration
  JOURNAL   J Cell Biol 186 (1), 99-111 (2009)
   PUBMED   19581412
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Wollscheid,B., Bausch-Fluck,D., Henderson,C., O'Brien,R., Bibel,M.,
            Schiess,R., Aebersold,R. and Watts,J.D.
  TITLE     Mass-spectrometric identification and relative quantification of
            N-linked cell surface glycoproteins
  JOURNAL   Nat Biotechnol 27 (4), 378-386 (2009)
   PUBMED   19349973
  REMARK    Erratum:[Nat Biotechnol. 2009 Sep;27(9):864]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN262982.1, AC004754.1, AL136542.1 and BC032112.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.258763.1,
                                           SRR1660805.192324.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399932.8/ ENSP00000382814.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..552
                     /product="protein FAM234A"
                     /note="protein ITFG3; integrin alpha FG-GAP repeat
                     containing 3"
                     /calculated_mol_wt=59529
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5M7W6; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            50..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            116
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            314
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X4.1)"
     Site            473
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9H0X4.1)"
     CDS             1..552
                     /gene="FAM234A"
                     /gene_synonym="C16orf9; gs19; ITFG3"
                     /coded_by="NM_032039.4:177..1835"
                     /db_xref="CCDS:CCDS10402.1"
                     /db_xref="GeneID:83986"
                     /db_xref="HGNC:HGNC:14163"
ORIGIN      
        1 mldhkdleae ihplkneerk sqenlgnpsk nednvksapp qsrlsrcraa afflslflcl
       61 fvvfvvsfvi pcpdrpasqr mwridysaav iydflavddi ngdriqdvlf lykntnssnn
      121 fsrscvdegf sspctfaaav sgangstlwe rpvaqdvalv ecavpqprgs eapsacilvg
      181 rpssfiavnl ftgetlwnhs ssfsgnasil spllqvpdvd gdgapdllvl tqereevsgh
      241 lysgstghqi glrgslgvdg esgfllhvtr tgahyilfpc asslcgcsvk glyekvtgsg
      301 gpfksdphwe smlnattrrm lshssgavry lmhvpgnaga dvllvgseaf vlldgqeltp
      361 rwtpkaahvl rkpifgrykp dtlavaveng tgtdrqilfl dlgtgavlcs lalpslpggp
      421 lsaslptadh rsafffwglh elgstsetet gearhslymf hptlprvlle lanvsthiva
      481 fdavlfepsr haayilltgp adseapglvs vikhkvrdlv pssrvvrlge ggpdsdqair
      541 drfsrlryqs ea
//
LOCUS       NP_001265231             142 aa            linear   PRI 20-NOV-2025
DEFINITION  diablo IAP-binding mitochondrial protein isoform 4 [Homo sapiens].
ACCESSION   NP_001265231
VERSION     NP_001265231.1
DBSOURCE    REFSEQ: accession NM_001278302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Zhang,D. and Yang,N.
  TITLE     In vivo and in vitro studies on the role of regulating Smac
            expression in the occurrence and development of colon cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (6), 206-210 (2024)
   PUBMED   38836659
  REMARK    GeneRIF: In vivo and in vitro studies on the role of regulating
            Smac expression in the occurrence and development of colon cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Li,Y., Song,Y. and Liang,Y.
  TITLE     AREL1 resists the apoptosis induced by TGF-beta by inhibiting SMAC
            in vascular endothelial cells
  JOURNAL   J Biochem Mol Toxicol 37 (10), e23439 (2023)
   PUBMED   37522329
  REMARK    GeneRIF: AREL1 resists the apoptosis induced by TGF-beta by
            inhibiting SMAC in vascular endothelial cells.
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Fu,J., Jin,Y. and Arend,L.J.
  TITLE     Smac3, a novel Smac/DIABLO splicing variant, attenuates the
            stability and apoptosis-inhibiting activity of X-linked inhibitor
            of apoptosis protein
  JOURNAL   J Biol Chem 278 (52), 52660-52672 (2003)
   PUBMED   14523016
  REMARK    GeneRIF: Smac3 is a novel Smac/DIABLO splicing variant and
            attenuates the stability and apoptosis-inhibiting activity of XIAP
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Roberts,D.L., Merrison,W., MacFarlane,M. and Cohen,G.M.
  TITLE     The inhibitor of apoptosis protein-binding domain of Smac is not
            essential for its proapoptotic activity
  JOURNAL   J Cell Biol 153 (1), 221-228 (2001)
   PUBMED   11285287
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Liu,Z., Sun,C., Olejniczak,E.T., Meadows,R.P., Betz,S.F., Oost,T.,
            Herrmann,J., Wu,J.C. and Fesik,S.W.
  TITLE     Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
  JOURNAL   Nature 408 (6815), 1004-1008 (2000)
   PUBMED   11140637
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Srinivasula,S.M., Datta,P., Fan,X.J., Fernandes-Alnemri,T.,
            Huang,Z. and Alnemri,E.S.
  TITLE     Molecular determinants of the caspase-promoting activity of
            Smac/DIABLO and its role in the death receptor pathway
  JOURNAL   J Biol Chem 275 (46), 36152-36157 (2000)
   PUBMED   10950947
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Chai,J., Du,C., Wu,J.W., Kyin,S., Wang,X. and Shi,Y.
  TITLE     Structural and biochemical basis of apoptotic activation by
            Smac/DIABLO
  JOURNAL   Nature 406 (6798), 855-862 (2000)
   PUBMED   10972280
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Verhagen,A.M., Ekert,P.G., Pakusch,M., Silke,J., Connolly,L.M.,
            Reid,G.E., Moritz,R.L., Simpson,R.J. and Vaux,D.L.
  TITLE     Identification of DIABLO, a mammalian protein that promotes
            apoptosis by binding to and antagonizing IAP proteins
  JOURNAL   Cell 102 (1), 43-53 (2000)
   PUBMED   10929712
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Du,C., Fang,M., Li,Y., Li,L. and Wang,X.
  TITLE     Smac, a mitochondrial protein that promotes cytochrome c-dependent
            caspase activation by eliminating IAP inhibition
  JOURNAL   Cell 102 (1), 33-42 (2000)
   PUBMED   10929711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA877400.1, BC046209.1,
            BC095468.1, JX679472.1, AK057778.1 and N66735.1.
            
            Summary: This gene encodes an inhibitor of apoptosis protein
            (IAP)-binding protein. The encoded mitochondrial protein enters the
            cytosol when cells undergo apoptosis, and allows activation of
            caspases by binding to inhibitor of apoptosis proteins.
            Overexpression of the encoded protein sensitizes tumor cells to
            apoptosis. A mutation in this gene is associated with young-adult
            onset of nonsyndromic deafness-64. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (5) differs in its 5' UTR and 5'
            coding region, uses an alternate start codon, and lacks an in-frame
            exon in the internal coding region, compared to variant 1. The
            encoded isoform (4) has a distinct N-terminus and is shorter,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM739108.1, BM746689.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155751, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 10929711; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..142
                     /product="diablo IAP-binding mitochondrial protein isoform
                     4"
                     /note="second mitochondria-derived activator of caspase;
                     direct IAP-binding protein with low pI; diablo homolog,
                     mitochondrial; diablo-like protein; second
                     mitochondria-derived activator of caspases"
                     /calculated_mol_wt=16255
     Region          <6..142
                     /region_name="Smac_DIABLO"
                     /note="Second Mitochondria-derived Activator of Caspases;
                     pfam09057"
                     /db_xref="CDD:462664"
     CDS             1..142
                     /gene="DIABLO"
                     /gene_synonym="DFNA64; SMAC"
                     /coded_by="NM_001278302.1:685..1113"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:56616"
                     /db_xref="HGNC:HGNC:21528"
                     /db_xref="MIM:605219"
ORIGIN      
        1 mksdfyfqav ytltslyrqy tsllgkmnse eedevwqvii garaemtskh qeylklettw
       61 mtavglsema aeaayqtgad qasitarnhi qlvklqveev hqlsrkaetk laeaqieelr
      121 qktqeegeer aeseqeaylr ed
//
LOCUS       NP_036387                950 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-3' exoribonuclease 2 isoform 2 [Homo sapiens].
ACCESSION   NP_036387
VERSION     NP_036387.2
DBSOURCE    REFSEQ: accession NM_012255.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 950)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 950)
  AUTHORS   Reiss,M., Keegan,J., Aldrich,A., Lyons,S.M. and Flynn,R.L.
  TITLE     The exoribonuclease XRN2 mediates degradation of the long
            non-coding telomeric RNA TERRA
  JOURNAL   FEBS Lett 597 (14), 1818-1836 (2023)
   PUBMED   37191774
  REMARK    GeneRIF: The exoribonuclease XRN2 mediates degradation of the long
            non-coding telomeric RNA TERRA.
REFERENCE   3  (residues 1 to 950)
  AUTHORS   Pieraccioli,M., Caggiano,C., Mignini,L., Zhong,C., Babini,G.,
            Lattanzio,R., Di Stasi,S., Tian,B., Sette,C. and Bielli,P.
  TITLE     The transcriptional terminator XRN2 and the RNA-binding protein
            Sam68 link alternative polyadenylation to cell cycle progression in
            prostate cancer
  JOURNAL   Nat Struct Mol Biol 29 (11), 1101-1112 (2022)
   PUBMED   36344846
  REMARK    GeneRIF: The transcriptional terminator XRN2 and the RNA-binding
            protein Sam68 link alternative polyadenylation to cell cycle
            progression in prostate cancer.
REFERENCE   4  (residues 1 to 950)
  AUTHORS   Dang,T.T., Lerner,M., Saunders,D., Smith,N., Gulej,R., Zalles,M.,
            Towner,R.A. and Morales,J.C.
  TITLE     XRN2 Is Required for Cell Motility and Invasion in Glioblastomas
  JOURNAL   Cells 11 (9), 1481 (2022)
   PUBMED   35563787
  REMARK    GeneRIF: XRN2 Is Required for Cell Motility and Invasion in
            Glioblastomas.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 950)
  AUTHORS   West,S., Gromak,N. and Proudfoot,N.J.
  TITLE     Human 5' --> 3' exonuclease Xrn2 promotes transcription termination
            at co-transcriptional cleavage sites
  JOURNAL   Nature 432 (7016), 522-525 (2004)
   PUBMED   15565158
  REMARK    GeneRIF: co-transcriptional cleavage acts as a precursor to
            termination by presenting a free RNA 5' end that is recognized by
            the human 5' --> 3' exonuclease Xrn2
REFERENCE   6  (residues 1 to 950)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   7  (residues 1 to 950)
  AUTHORS   Lejeune,F., Li,X. and Maquat,L.E.
  TITLE     Nonsense-mediated mRNA decay in mammalian cells involves decapping,
            deadenylating, and exonucleolytic activities
  JOURNAL   Mol Cell 12 (3), 675-687 (2003)
   PUBMED   14527413
REFERENCE   8  (residues 1 to 950)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 950)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 950)
  AUTHORS   Zhang,M., Yu,L., Xin,Y., Hu,P., Fu,Q., Yu,C. and Zhao,S.
  TITLE     Cloning and mapping of the XRN2 gene to human chromosome
            20p11.1-p11.2
  JOURNAL   Genomics 59 (2), 252-254 (1999)
   PUBMED   10409438
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC142960.1, AL136841.1 and
            AF152169.1.
            
            On Feb 22, 2002 this sequence version replaced NP_036387.1.
            
            Summary: This gene encodes a 5'-3' exonuclease that promotes
            transcription termination at cotranscriptional cleavage sites.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon, resulting in a distinct 5' UTR and the use of an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus , and is shorter, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF152169.1, AK001573.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377191.5/ ENSP00000366396.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..950
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.22"
     Protein         1..950
                     /product="5'-3' exoribonuclease 2 isoform 2"
                     /EC_number="3.1.13.-"
                     /note="DHP protein; DHM1-like protein"
                     /calculated_mol_wt=108452
     Region          1..787
                     /region_name="XRN1"
                     /note="5'-3' exonuclease [Replication, recombination and
                     repair]; COG5049"
                     /db_xref="CDD:227382"
     Site            286
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR1; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Region          408..508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR1; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            824
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            847
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            851
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            880
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR1; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            883
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR1;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            895
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Region          911..950
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0D6.1)"
     Site            946
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H0D6.1)"
     CDS             1..950
                     /gene="XRN2"
                     /coded_by="NM_012255.5:69..2921"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13144.1"
                     /db_xref="GeneID:22803"
                     /db_xref="HGNC:HGNC:12836"
                     /db_xref="MIM:608851"
ORIGIN      
        1 mgvpaffrwl srkypsiivn cveekpkecn gvkipvdask pnpndvefdn lyldmngiih
       61 pcthpedkpa pknedemmva ifeyidrlfs ivrprrllym aidgvaprak mnqqrsrrfr
      121 askegmeaav ekqrvreeil akggflppee ikerfdsnci tpgtefmdnl akclryyiad
      181 rlnndpgwkn ltvilsdasa pgegehkimd yirrqraqpn hdpnthhclc gadadlimlg
      241 lathepnfti ireefkpnkp kpcglcnqfg hevkdceglp rekkgkhdel adslpcaege
      301 fiflrlnvlr eylereltma slpftfdver siddwvfmcf fvgndflphl psleirenai
      361 drlvniyknv vhktggylte sgyvnlqrvq mimlavgeve dsifkkrkdd edsfrrrqke
      421 krkrmkrdqp aftpsgiltp halgsrnspg sqvasnprqa ayemrmqnns spsispntsf
      481 tsdgspsplg gikrkaedsd sepepednvr lweagwkqry yknkfdvdaa dekfrrkvvq
      541 syveglcwvl ryyyqgcasw kwyypfhyap fasdfegiad mpsdfekgtk pfkpleqlmg
      601 vfpaasgnfl ppswrklmsd pdssiidfyp edfaidlngk kyawqgvall pfvderrlra
      661 aleevypdlt peetrrnslg gdvlfvgkhh plhdfilely qtgstepvev ppelchgiqg
      721 kfsldeeail pdqivcspvp mlrdltqntv vsinfkdpqf aedyifkavm lpgarkpaav
      781 lkpsdwekss ngrqwkpqlg fnrdrrpvhl dqaafrtlgh vmprgsgtgi ysnaapppvt
      841 yqgnlyrpll rgqaqipklm snmrpqdswr gppplfqqqr fdrgvgaepl lpwnrmlqtq
      901 naafqpnqyq mlagpggypp rrddrggrqg ypregrkypl pppsgrynwn
//
LOCUS       NP_001341832            2742 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform j [Homo sapiens].
ACCESSION   NP_001341832
VERSION     NP_001341832.1
DBSOURCE    REFSEQ: accession NM_001354903.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2742)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2742)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2742)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2742)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2742)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2742)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2742)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2742)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2742)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2742)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2477753.1,
                                           SRR14372079.831789.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2742
                     /product="adenomatous polyposis coli protein isoform j"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=300309
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <307..365
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          364..407
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(398,402,406,441,445,449,485,489,493)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          411..452
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          415..452
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          459..494
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          502..543
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..588
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          552..586
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          590..630
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          594..630
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          631..918
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          935..1034
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1156..>1173
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1182..1267
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1190..1600
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1270..1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1536..1559
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1561..1614
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1615..1636
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1645..1738
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1772..1846
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1932..1951
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2122..2467
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2569..2742
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2742
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354903.2:60..8288"
                     /note="isoform j is encoded by transcript variant 12"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc vlmklsfdee
      361 hrhamnelgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg dvankatlcs
      421 mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka lmecalevkk
      481 estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai iesgggilrn
      541 vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn pkdqealwdm
      601 gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps lhvrkqkale
      661 aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs dnfntgnmtv
      721 lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg tsskrglqis
      781 ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth sntynftkse
      841 nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde skfcsygqyp
      901 adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar pkhiiedeik
      961 qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse tnrvgsnhgi
     1021 nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr hvdqpidysl
     1081 kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql hpssaqsrsg
     1141 qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq ttqeadsant
     1201 lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka vefssgaksp
     1261 sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs gmvsgiisps
     1321 dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa vnaavqrvqv
     1381 lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen dngneteseq
     1441 pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka kkpaqtaskl
     1501 pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf statslsdlt
     1561 iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip elddnkaeeg
     1621 dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk ptspvkpipq
     1681 nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne drvrgsfafd
     1741 sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese akvtshtelt
     1801 snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl qnfaientpv
     1861 cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks fhvedtpvcf
     1921 srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi lgedltldlk
     1981 diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd sdsilslksg
     2041 islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg kkvykslitg
     2101 kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp plktpasksp
     2161 segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr paqqplsrpi
     2221 qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr qmsqqnltkq
     2281 tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr serpvlvrqs
     2341 tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm slsthssvqa
     2401 ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh skhssslprv
     2461 stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt wrkikenefs
     2521 ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs grsptgntpp
     2581 vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap dqkgteikpg
     2641 qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr kssadstsar
     2701 psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_059447                893 aa            linear   PRI 20-NOV-2025
DEFINITION  major vault protein isoform 1 [Homo sapiens].
ACCESSION   NP_059447
VERSION     NP_059447.2
DBSOURCE    REFSEQ: accession NM_017458.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Li,C., Gao,M., Zha,N. and Guo,G.
  TITLE     The prognostic value and immunological role of MVP in pan-cancer
            study
  JOURNAL   Aging (Albany NY) 16 (10), 8497-8510 (2024)
   PUBMED   38713157
  REMARK    GeneRIF: The prognostic value and immunological role of MVP in
            pan-cancer study.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Taube,M., Lisiak,N., Toton,E. and Rubis,B.
  TITLE     Human Vault RNAs: Exploring Their Potential Role in Cellular
            Metabolism
  JOURNAL   Int J Mol Sci 25 (7), 4072 (2024)
   PUBMED   38612882
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Yu,C., Zhu,Q., Ma,C., Luo,C., Nie,L., Cai,H., Wang,Q., Wang,F.,
            Ren,H., Yan,H., Xu,K., Zhou,L., Zhang,C., Lu,G., Lu,Z., Zhu,Y. and
            Liu,S.
  TITLE     Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6
  JOURNAL   Front Immunol 14, 1289795 (2024)
   PUBMED   38264642
  REMARK    GeneRIF: Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Holzmann,K., Ambrosch,I., Elbling,L., Micksche,M. and Berger,W.
  TITLE     A small upstream open reading frame causes inhibition of human
            major vault protein expression from a ubiquitous mRNA splice
            variant
  JOURNAL   FEBS Lett 494 (1-2), 99-104 (2001)
   PUBMED   11297743
  REMARK    GeneRIF: MVP gene expression regulated by alternative splicing due
            to generation of an upstream open reading frame
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Dingemans,A.M., van Ark-Otte,J., van der Valk,P., Apolinario,R.M.,
            Scheper,R.J., Postmus,P.E. and Giaccone,G.
  TITLE     Expression of the human major vault protein LRP in human lung
            cancer samples and normal lung tissues
  JOURNAL   Ann Oncol 7 (6), 625-630 (1996)
   PUBMED   8879378
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Schroeijers,A.B., van
            der Valk,P. and Scheper,R.J.
  TITLE     Major vault protein LRP-related multidrug resistance
  JOURNAL   Eur J Cancer 32A (6), 979-984 (1996)
   PUBMED   8763338
  REMARK    Review article
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Giaccone,G.,
            Broxterman,H.J., Meijer,C.J., van der Valk,P. and Scheper,R.J.
  TITLE     Broad distribution of the multidrug resistance-related vault lung
            resistance protein in normal human tissues and tumors
  JOURNAL   Am J Pathol 148 (3), 877-887 (1996)
   PUBMED   8774142
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Slovak,M.L., Ho,J.P., Cole,S.P., Deeley,R.G., Greenberger,L., de
            Vries,E.G., Broxterman,H.J., Scheffer,G.L. and Scheper,R.J.
  TITLE     The LRP gene encoding a major vault protein associated with drug
            resistance maps proximal to MRP on chromosome 16: evidence that
            chromosome breakage plays a key role in MRP or LRP gene
            amplification
  JOURNAL   Cancer Res 55 (19), 4214-4219 (1995)
   PUBMED   7671223
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Scheffer,G.L., Wijngaard,P.L., Flens,M.J., Izquierdo,M.A.,
            Slovak,M.L., Pinedo,H.M., Meijer,C.J., Clevers,H.C. and
            Scheper,R.J.
  TITLE     The drug resistance-related protein LRP is the human major vault
            protein
  JOURNAL   Nat Med 1 (6), 578-582 (1995)
   PUBMED   7585126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA842337.1, BC008932.2,
            BU151678.1 and BM999583.1.
            
            On Apr 3, 2002 this sequence version replaced NP_059447.1.
            
            Summary: This gene encodes the major component of the vault
            complex. Vaults are multi-subunit ribonucleoprotein structures that
            may be involved in nucleo-cytoplasmic transport. The encoded
            protein may play a role in multiple cellular processes by
            regulating the MAP kinase, JAK/STAT and phosphoinositide
            3-kinase/Akt signaling pathways. The encoded protein also plays a
            role in multidrug resistance, and expression of this gene may be a
            prognostic marker for several types of cancer. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (1, also known as L-MVP) is the
            longest transcript. Variants 1 and 2 encode the same isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.42325.1,
                                           SRR1803612.32638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 11297743
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..893
                     /product="major vault protein isoform 1"
                     /note="lung resistance-related protein; testicular
                     secretory protein Li 30"
                     /calculated_mol_wt=99196
     Region          2..56
                     /region_name="MVP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          4..850
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     Region          57..111
                     /region_name="MVP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          112..164
                     /region_name="MVP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          165..217
                     /region_name="MVP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          218..272
                     /region_name="MVP 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          273..323
                     /region_name="MVP 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          324..379
                     /region_name="MVP 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          380..457
                     /region_name="MVP 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14764.4)"
     Region          458..520
                     /region_name="MVP 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          856..893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     CDS             1..893
                     /gene="MVP"
                     /gene_synonym="LRP; VAULT1"
                     /coded_by="NM_017458.3:194..2875"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10656.1"
                     /db_xref="GeneID:9961"
                     /db_xref="HGNC:HGNC:7531"
                     /db_xref="MIM:605088"
ORIGIN      
        1 mateefiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapmrm vtvpprhyct
       61 vanpvsrdaq glvlfdvtgq vrlrhadlei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkdgdkvvag dewlfegpgt yiprkevevv eiiqatiirq nqalrlrark
      181 ecwdrdgker vtgeewlvtt vgaylpavfe evldlvdavi ltektalhlr arrnfrdfrg
      241 vsrrtgeewl vtvqdteahv pdvheevlgv vpittlgphn ycvildpvgp dgknqlgqkr
      301 vvkgeksffl qpgeqleqgi qdvyvlseqq glllralqpl eegedeekvs hqagdhwlir
      361 gpleyvpsak vevveerqai pldenegiyv qdvktgkvra vigstymltq devlwekelp
      421 pgveellnkg qdpladrgek dtakslqpla prnktrvvsy rvphnaavqv ydyrekrarv
      481 vfgpelvslg peeqftvlsl sagrpkrpha rralclllgp dfftdvitie tadharlqlq
      541 laynwhfevn drkdpqetak lfsvpdfvgd ackaiasrvr gavasvtfdd fhknsariir
      601 tavfgfetse akgpdgmalp rprdqavfpq nglvvssvdv qsvepvdqrt rdalqrsvql
      661 aieittnsqe aaakheaqrl eqeargrler qkildqseae karkellele alsmavestg
      721 takaeaesra eaariegegs vlqaklkaqa laieteaelq rvqkvrelel vyaraqlele
      781 vskaqqlaev evkkfkqmte aigpstirdl avagpemqvk llqslglkst litdgstpin
      841 lfntafgllg mgpegqplgr rvasgpspge gispqsaqap qapgdnhvvp vlr
//
LOCUS       NP_009165                186 aa            linear   PRI 20-NOV-2025
DEFINITION  dynactin subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_009165
VERSION     NP_009165.1
DBSOURCE    REFSEQ: accession NM_007234.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Su,X., Li,H., Chen,S. and Qin,C.
  TITLE     Study on the Prognostic Values of Dynactin Genes in Low-Grade
            Glioma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211010143 (2021)
   PUBMED   33896271
  REMARK    GeneRIF: Study on the Prognostic Values of Dynactin Genes in
            Low-Grade Glioma.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Mills,D.R. and Jackson,C.L.
  TITLE     Assignment of p22 dynactin light chain (DCTN3) to human chromosome
            region 9p13 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 92 (1-2), 166 (2001)
   PUBMED   11306820
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Karki,S., Tokito,M.K. and Holzbaur,E.L.
  TITLE     A dynactin subunit with a highly conserved cysteine-rich motif
            interacts directly with Arp1
  JOURNAL   J Biol Chem 275 (7), 4834-4839 (2000)
   PUBMED   10671518
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Karki,S., LaMonte,B. and Holzbaur,E.L.
  TITLE     Characterization of the p22 subunit of dynactin reveals the
            localization of cytoplasmic dynein and dynactin to the midbody of
            dividing cells
  JOURNAL   J Cell Biol 142 (4), 1023-1034 (1998)
   PUBMED   9722614
  REMARK    Erratum:[J Cell Biol 1998 Oct 19;143(2):following 560]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA212054.1, BC107697.1 and
            CN257020.1.
            
            Summary: This gene encodes the smallest subunit of dynactin, a
            macromolecular complex consisting of 10 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation,
            cytokinesis, chromosome movement, nuclear positioning, and
            axonogenesis. This subunit, like most other dynactin subunits,
            exists only as a part of the dynactin complex. It is primarily an
            alpha-helical protein with very little coiled coil, and binds
            directly to the largest subunit (p150) of dynactin. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.555144.1,
                                           SRR5189661.24228.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259632.12/ ENSP00000259632.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..186
                     /product="dynactin subunit 3 isoform 1"
                     /note="dynactin light chain; dynactin complex subunit 22
                     kDa subunit; dynactin 3 (p22)"
                     /calculated_mol_wt=20988
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75935.1)"
     Region          10..170
                     /region_name="Dynactin_p22"
                     /note="Dynactin subunit p22; pfam07426"
                     /db_xref="CDD:462162"
     CDS             1..186
                     /gene="DCTN3"
                     /gene_synonym="DCTN-22; DCTN22"
                     /coded_by="NM_007234.5:32..592"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6560.1"
                     /db_xref="GeneID:11258"
                     /db_xref="HGNC:HGNC:2713"
                     /db_xref="MIM:607387"
ORIGIN      
        1 magltdlqrl qarveelerw vygpggargs rkvadglvkv qvalgnissk rervkilykk
       61 iedlikyldp eyidriaipd asklqfilae eqfilsqval leqvnalvpm ldsahikavp
      121 ehaarlqrla qihiqqqdqc veiteeskal leeynkttml lskqfvqwde llcqleaatq
      181 vkpaee
//
LOCUS       NP_997401                343 aa            linear   PRI 20-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit alpha isoform
            Calpha2 [Homo sapiens].
ACCESSION   NP_997401
VERSION     NP_997401.1
DBSOURCE    REFSEQ: accession NM_207518.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Shirani,M., Levin,S., Shebl,B., Requena,D., Finkelstein,T.M.,
            Johnson,D.S., Ng,D., Lalazar,G., Heissel,S., Hojrup,P., Molina,H.,
            de Jong,Y.P., Rice,C.M., Singhi,A.D., Torbenson,M.S., Coffino,P.,
            Lyons,B. and Simon,S.M.
  TITLE     Increased Protein Kinase A Activity Induces Fibrolamellar
            Hepatocellular Carcinoma Features Independent of DNAJB1
  JOURNAL   Cancer Res 84 (16), 2626-2644 (2024)
   PUBMED   38888469
  REMARK    GeneRIF: Increased Protein Kinase A Activity Induces Fibrolamellar
            Hepatocellular Carcinoma Features Independent of DNAJB1.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Beuschlein,F., Fassnacht,M., Assie,G., Calebiro,D., Stratakis,C.A.,
            Osswald,A., Ronchi,C.L., Wieland,T., Sbiera,S., Faucz,F.R.,
            Schaak,K., Schmittfull,A., Schwarzmayr,T., Barreau,O., Vezzosi,D.,
            Rizk-Rabin,M., Zabel,U., Szarek,E., Salpea,P., Forlino,A.,
            Vetro,A., Zuffardi,O., Kisker,C., Diener,S., Meitinger,T.,
            Lohse,M.J., Reincke,M., Bertherat,J., Strom,T.M. and Allolio,B.
  TITLE     Constitutive activation of PKA catalytic subunit in adrenal
            Cushing's syndrome
  JOURNAL   N Engl J Med 370 (11), 1019-1028 (2014)
   PUBMED   24571724
  REMARK    GeneRIF: Genetic alterations of the catalytic subunit of PKA were
            found to be associated with bilateral adrenal hyperplasias and
            unilateral cortisol-producing adrenal adenomas.
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Agustin,J.T., Wilkerson,C.G. and Witman,G.B.
  TITLE     The unique catalytic subunit of sperm cAMP-dependent protein kinase
            is the product of an alternative Calpha mRNA expressed specifically
            in spermatogenic cells
  JOURNAL   Mol Biol Cell 11 (9), 3031-3044 (2000)
   PUBMED   10982398
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Reinton,N., Orstavik,S., Haugen,T.B., Jahnsen,T., Tasken,K. and
            Skalhegg,B.S.
  TITLE     A novel isoform of human cyclic 3',5'-adenosine
            monophosphate-dependent protein kinase, c alpha-s, localizes to
            sperm midpiece
  JOURNAL   Biol Reprod 63 (2), 607-611 (2000)
   PUBMED   10906071
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Desseyn,J.L., Burton,K.A. and McKnight,G.S.
  TITLE     Expression of a nonmyristylated variant of the catalytic subunit of
            protein kinase A during male germ-cell development
  JOURNAL   Proc Natl Acad Sci U S A 97 (12), 6433-6438 (2000)
   PUBMED   10841548
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Maldonado,F. and Hanks,S.K.
  TITLE     A cDNA clone encoding human cAMP-dependent protein kinase catalytic
            subunit C alpha
  JOURNAL   Nucleic Acids Res 16 (16), 8189-8190 (1988)
   PUBMED   2843813
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Shoji,S., Titani,K., Demaille,J.G. and Fischer,E.H.
  TITLE     Sequence of two phosphorylated sites in the catalytic subunit of
            bovine cardiac muscle adenosine 3':5'-monophosphate-dependent
            protein kinase
  JOURNAL   J Biol Chem 254 (14), 6211-6214 (1979)
   PUBMED   221492
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Joh,T.H., Park,D.H. and Reis,D.J.
  TITLE     Direct phosphorylation of brain tyrosine hydroxylase by cyclic
            AMP-dependent protein kinase: mechanism of enzyme activation
  JOURNAL   Proc Natl Acad Sci U S A 75 (10), 4744-4748 (1978)
   PUBMED   33381
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022098.9, AK292284.1,
            BC108259.1 and BC039846.1.
            
            Summary: This gene encodes one of the catalytic subunits of protein
            kinase A, which exists as a tetrameric holoenzyme with two
            regulatory subunits and two catalytic subunits, in its inactive
            form. cAMP causes the dissociation of the inactive holoenzyme into
            a dimer of regulatory subunits bound to four cAMP and two free
            monomeric catalytic subunits. Four different regulatory subunits
            and three catalytic subunits have been identified in humans.
            cAMP-dependent phosphorylation of proteins by protein kinase A is
            important to many cellular processes, including differentiation,
            proliferation, and apoptosis. Constitutive activation of this gene
            caused either by somatic mutations, or genomic duplications of
            regions that include this gene, have been associated with
            hyperplasias and adenomas of the adrenal cortex and are linked to
            corticotropin-independent Cushing's syndrome. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. Tissue-specific isoforms that differ at the N-terminus
            have been described, and these isoforms may differ in the
            post-translational modifications that occur at the N-terminus of
            some isoforms. [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon and initiates translation at an alternate start
            codon, compared to variant 1. It encodes Calpha2, PMID:21812984
            (also known as C alpha-s, PMID: 10906071) which has a shorter and
            distinct N-terminus, compared to Calpha1. This variant is
            specifically expressed in spermatogenic cells and may be essential
            for male fertility.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3686746.1,
                                           SRR14038197.2444620.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..343
                     /product="cAMP-dependent protein kinase catalytic subunit
                     alpha isoform Calpha2"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit; PKA C-alpha;
                     protein kinase, cAMP-dependent, catalytic, alpha; protein
                     kinase, cAMP-dependent, alpha catalytic subunit"
                     /calculated_mol_wt=39691
     Region          34..323
                     /region_name="STKc_PKA"
                     /note="Catalytic subunit of the Serine/Threonine Kinase,
                     cAMP-dependent protein kinase; cd14209"
                     /db_xref="CDD:271111"
     Site            order(42..48,50,63,65,97,113..116,120,159,161,163..164,
                     166,176..177,320)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271111"
     Site            order(43..48,50,63,65,75,97,113..114,116,120,122,126,159,
                     161..164,166,176..177,180,191,193..196,223,227..229,
                     232..234,236,239,320,323)
                     /site_type="active"
                     /db_xref="CDD:271111"
     Site            order(44,46..47,75..77,120,122,126,159,161..163,180,
                     191..196,223,227..229,232..234,236,239..240,323)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271111"
     Site            order(46,76..77,79..80,120,122,126,161..163,180,187,
                     189..194,197,204..206,223,236..237,240..241,244,323)
                     /site_type="other"
                     /note="regulatory subunit interface [polypeptide binding]"
                     /db_xref="CDD:271111"
     Site            176..196
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271111"
     CDS             1..343
                     /gene="PRKACA"
                     /gene_synonym="CAFD1; PKACA; PPNAD4"
                     /coded_by="NM_207518.3:37..1068"
                     /note="isoform Calpha2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12305.1"
                     /db_xref="GeneID:5566"
                     /db_xref="HGNC:HGNC:9380"
                     /db_xref="MIM:601639"
ORIGIN      
        1 masnssdvke flakakedfl kkwespaqnt ahldqferik tlgtgsfgrv mlvkhketgn
       61 hyamkildkq kvvklkqieh tlnekrilqa vnfpflvkle fsfkdnsnly mvmeyvpgge
      121 mfshlrrigr fsepharfya aqivltfeyl hsldliyrdl kpenllidqq gyiqvtdfgf
      181 akrvkgrtwt lcgtpeylap eiilskgynk avdwwalgvl iyemaagypp ffadqpiqiy
      241 ekivsgkvrf pshfssdlkd llrnllqvdl tkrfgnlkng vndiknhkwf attdwiaiyq
      301 rkveapfipk fkgpgdtsnf ddyeeeeirv sinekcgkef sef
//
LOCUS       NP_065846                835 aa            linear   PRI 20-NOV-2025
DEFINITION  neuroligin-2 precursor [Homo sapiens].
ACCESSION   NP_065846
VERSION     NP_065846.1
DBSOURCE    REFSEQ: accession NM_020795.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Benner,O., Cast,T.P., Minamide,L.S., Lenninger,Z., Bamburg,J.R. and
            Chanda,S.
  TITLE     Multiple N-linked glycosylation sites critically modulate the
            synaptic abundance of neuroligin isoforms
  JOURNAL   J Biol Chem 299 (12), 105361 (2023)
   PUBMED   37865312
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Zhang,Z., Hou,M., Ou,H., Wang,D., Li,Z., Zhang,H. and Lu,J.
  TITLE     Expression and structural analysis of human neuroligin 2 and
            neuroligin 3 implicated in autism spectrum disorders
  JOURNAL   Front Endocrinol (Lausanne) 13, 1067529 (2022)
   PUBMED   36479216
  REMARK    GeneRIF: Expression and structural analysis of human neuroligin 2
            and neuroligin 3 implicated in autism spectrum disorders.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Schafer,J., Forster,L., Mey,I., Papadopoulos,T., Brose,N. and
            Steinem,C.
  TITLE     Neuroligin-2 dependent conformational activation of collybistin
            reconstituted in supported hybrid membranes
  JOURNAL   J Biol Chem 295 (52), 18604-18613 (2020)
   PUBMED   33127642
  REMARK    GeneRIF: Neuroligin-2 dependent conformational activation of
            collybistin reconstituted in supported hybrid membranes.
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Ali,H., Marth,L. and Krueger-Burg,D.
  TITLE     Neuroligin-2 as a central organizer of inhibitory synapses in
            health and disease
  JOURNAL   Sci Signal 13 (663) (2020)
   PUBMED   33443230
  REMARK    GeneRIF: Neuroligin-2 as a central organizer of inhibitory synapses
            in health and disease.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Scheiffele,P., Fan,J., Choih,J., Fetter,R. and Serafini,T.
  TITLE     Neuroligin expressed in nonneuronal cells triggers presynaptic
            development in contacting axons
  JOURNAL   Cell 101 (6), 657-669 (2000)
   PUBMED   10892652
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Philibert,R.A., Winfield,S.L., Sandhu,H.K., Martin,B.M. and
            Ginns,E.I.
  TITLE     The structure and expression of the human neuroligin-3 gene
  JOURNAL   Gene 246 (1-2), 303-310 (2000)
   PUBMED   10767552
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Kurschner,C., Mermelstein,P.G., Holden,W.T. and Surmeier,D.J.
  TITLE     CIPP, a novel multivalent PDZ domain protein, selectively interacts
            with Kir4.0 family members, NMDA receptor subunits, neurexins, and
            neuroligins
  JOURNAL   Mol Cell Neurosci 11 (3), 161-172 (1998)
   PUBMED   9647694
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Ichtchenko,K., Nguyen,T. and Sudhof,T.C.
  TITLE     Structures, alternative splicing, and neurexin binding of multiple
            neuroligins
  JOURNAL   J Biol Chem 271 (5), 2676-2682 (1996)
   PUBMED   8576240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113189.11, AF376802.1,
            BM800364.1, DR763679.1, EL949788.1, AA447769.1 and AI613237.1.
            
            Summary: This gene encodes a member of a family of neuronal cell
            surface proteins. Members of this family may act as splice
            site-specific ligands for beta-neurexins and may be involved in the
            formation and remodeling of central nervous system synapses.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF376802.1, SRR9304719.239650.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302926.7/ ENSP00000305288.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..835
                     /product="neuroligin-2 precursor"
                     /calculated_mol_wt=89408
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1431
     mat_peptide     15..835
                     /product="Neuroligin-2. /id=PRO_0000008643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
                     /calculated_mol_wt=89408
     Region          42..601
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            order(185..187,264..266,269,419..420,455,501,504)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(265,386,500)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          623..668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          678..698
                     /region_name="Required for interaction with LHFPL4.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            678..698
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q69ZK9; propagated from
                     UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     Region          790..835
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NFZ4.1)"
     CDS             1..835
                     /gene="NLGN2"
                     /coded_by="NM_020795.4:412..2919"
                     /db_xref="CCDS:CCDS11103.1"
                     /db_xref="GeneID:57555"
                     /db_xref="HGNC:HGNC:14290"
                     /db_xref="MIM:606479"
ORIGIN      
        1 mwllalclvg lagaqrgggg pgggapggpg lglgslgeer fpvvntaygr vrgvrrelnn
       61 eilgpvvqfl gvpyatpplg arrfqppeap aswpgvrnat tlppacpqnl hgalpaimlp
      121 vwftdnleaa atyvqnqsed clylnlyvpt edgpltkkrd eatlnppdtd irdpgkkpvm
      181 lflhggsyme gtgnmfdgsv laaygnviva tlnyrlgvlg flstgdqaak gnyglldqiq
      241 alrwlsenia hfggdperit ifgsgagasc vnllilshhs eglfqkaiaq sgtaisswsv
      301 nyqplkytrl laakvgcdre dsaeaveclr rkpsrelvdq dvqparyhia fgpvvdgdvv
      361 pddpeilmqq geflnydmli gvnqgeglkf vedsaesedg vsasafdftv snfvdnlygy
      421 pegkdvlret ikfmytdwad rdngemrrkt llalftdhqw vapavatakl hadyqspvyf
      481 ytfyhhcqae grpewadaah gdelpyvfgv pmvgatdlfp cnfskndvml savvmtywtn
      541 faktgdpnqp vpqdtkfiht kpnrfeevvw skfnskekqy lhiglkprvr dnyrankvaf
      601 wlelvphlhn lhtelftttt rlppyatrwp prppagapgt rrppppatlp pepepepgpr
      661 aydrfpgdsr dystelsvtv avgasllfln ilafaalyyk rdrrqelrcr rlsppggsgs
      721 gvpgggpllp aagrelppee elvslqlkrg ggvgadpaea lrpacppdyt lalrrapddv
      781 pllapgaltl lpsglgpppp ppppslhpfg pfppppptat shnntlphph sttrv
//
LOCUS       NP_055519                925 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 104 kDa [Homo sapiens].
ACCESSION   NP_055519 XP_375682
VERSION     NP_055519.1
DBSOURCE    REFSEQ: accession NM_014704.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 925)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   2  (residues 1 to 925)
  AUTHORS   Khoshbakht,S., Beheshtian,M., Fattahi,Z., Bazazzadegan,N.,
            Parsimehr,E., Fadaee,M., Vazehan,R., Faraji Zonooz,M.,
            Abolhassani,A., Makvand,M., Kariminejad,A., Celik,A., Kahrizi,K.
            and Najmabadi,H.
  TITLE     CEP104 and CEP290; Genes with Ciliary Functions Cause Intellectual
            Disability in Multiple Families
  JOURNAL   Arch Iran Med 24 (5), 364-373 (2021)
   PUBMED   34196201
  REMARK    GeneRIF: CEP104 and CEP290; Genes with Ciliary Functions Cause
            Intellectual Disability in Multiple Families.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 925)
  AUTHORS   Yamazoe,T., Nagai,T., Umeda,S., Sugaya,Y. and Mizuno,K.
  TITLE     Roles of TOG and jelly-roll domains of centrosomal protein CEP104
            in its functions in cilium elongation and Hedgehog signaling
  JOURNAL   J Biol Chem 295 (43), 14723-14736 (2020)
   PUBMED   32820051
  REMARK    GeneRIF: Roles of TOG and jelly-roll domains of centrosomal protein
            CEP104 in its functions in cilium elongation and Hedgehog
            signaling.
REFERENCE   4  (residues 1 to 925)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 925)
  AUTHORS   Crisci,A., Raleff,F., Bagdiul,I., Raabe,M., Urlaub,H., Rain,J.C.
            and Kramer,A.
  TITLE     Mammalian splicing factor SF1 interacts with SURP domains of U2
            snRNP-associated proteins
  JOURNAL   Nucleic Acids Res 43 (21), 10456-10473 (2015)
   PUBMED   26420826
REFERENCE   6  (residues 1 to 925)
  AUTHORS   Srour,M., Hamdan,F.F., McKnight,D., Davis,E., Mandel,H.,
            Schwartzentruber,J., Martin,B., Patry,L., Nassif,C.,
            Dionne-Laporte,A., Ospina,L.H., Lemyre,E., Massicotte,C.,
            Laframboise,R., Maranda,B., Labuda,D., Decarie,J.C., Rypens,F.,
            Goldsher,D., Fallet-Bianco,C., Soucy,J.F., Laberge,A.M., Maftei,C.,
            Boycott,K., Brais,B., Boucher,R.M., Rouleau,G.A., Katsanis,N.,
            Majewski,J., Elpeleg,O., Kukolich,M.K., Shalev,S. and Michaud,J.L.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Joubert Syndrome in French Canadians and Identification of
            Mutations in CEP104
  JOURNAL   Am J Hum Genet 97 (5), 744-753 (2015)
   PUBMED   26477546
  REMARK    GeneRIF: Mutations in CEP104 is associated with Joubert Syndrome.
REFERENCE   7  (residues 1 to 925)
  AUTHORS   Satish Tammana,T.V., Tammana,D., Diener,D.R. and Rosenbaum,J.
  TITLE     Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the
            ciliary tip during ciliary assembly
  JOURNAL   J Cell Sci 126 (Pt 21), 5018-5029 (2013)
   PUBMED   23970417
REFERENCE   8  (residues 1 to 925)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   9  (residues 1 to 925)
  AUTHORS   Kumar,K.N., Babcock,K.K., Johnson,P.S., Chen,X., Ahmad,M. and
            Michaelis,E.K.
  TITLE     Cloning of the cDNA for a brain glycine-, glutamate- and
            thienylcyclohexylpiperidine-binding protein
  JOURNAL   Biochem Biophys Res Commun 216 (1), 390-398 (1995)
   PUBMED   7488117
REFERENCE   10 (residues 1 to 925)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL691523.6 and AL365330.16.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2004 this sequence version replaced XP_375682.1.
            
            Summary: This gene encodes a centrosomal protein required for
            ciliogenesis and for ciliary tip structural integrity. The
            mammalian protein contains three amino-terminal hydrophobic
            domains, two glycosylation sites, four cysteine-rich motifs, and
            two regions with homology to the glutamate receptor ionotropic,
            NMDA 1 protein. During ciliogenesis, the encoded protein
            translocates from the distal tips of the centrioles to the tip of
            the elongating cilium. Knockdown of the protein in human retinal
            pigment cells results in severe defects in ciliogenesis with
            structural deformities at the ciliary tips. Allelic variants of
            this gene are associated with the autosomal-recessive disorder
            Joubert syndrome, which is characterized by a distinctive
            mid-hindbrain and cerebellar malformation, oculomotor apraxia,
            irregular breathing, developmental delay, and ataxia. [provided by
            RefSeq, Feb 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.131782.1,
                                           SRR1803616.70953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378230.8/ ENSP00000367476.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..925
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.32"
     Protein         1..925
                     /product="centrosomal protein of 104 kDa"
                     /note="centrosomal protein 104kDa"
                     /calculated_mol_wt=104317
     Region          432..460
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(452..453,456,459..460,498..499,502,505..506,509,
                     546..547,550,553..554,557,577..578,581,584..585,627..628,
                     631,634..635)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          481..509
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          528..558
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          529..567
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60308.1)"
     Region          564..585
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          604..640
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60308.1)"
     Region          607..636
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          883..925
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60308.1)"
     CDS             1..925
                     /gene="CEP104"
                     /gene_synonym="CFAP256; GlyBP; JBTS25; KIAA0562; MRT77;
                     ROC22"
                     /coded_by="NM_014704.4:338..3115"
                     /db_xref="CCDS:CCDS30571.1"
                     /db_xref="GeneID:9731"
                     /db_xref="HGNC:HGNC:24866"
                     /db_xref="MIM:616690"
ORIGIN      
        1 mphkigfvvv sssghedgfs arelmihapt vsgwrsprfc qfpqeivlqm vercrirklq
       61 llahqymiss kiefyisesl peyfapyqae rfrrlgyvsl cdnektgcka relksvyvda
      121 vgqflklifh qnhvnkyniy nqvalvaini igdpadfsde sntasrekli dhylghnsed
      181 palegtyark sdyisplddl afdmyqdpev aqiirklder kreavqkery dyakklkqai
      241 adlqkvgerl gryevekrca vekedydlak ekkqqmeqyr aevyeqlelh slldaelmrr
      301 pfdlplqpla rsgspchqkp mpslpqleer gtenqfaepf lqekpssysl tispqhsavd
      361 pllpatdphp kinaeslpyd erplpairkh ygeavvepem snadisdarr ggmlgepepl
      421 tekalreass aidvlgetlv aeaycktwsy redallalsk klmempvgtp kedlkntlra
      481 svflvrraik divtsvfqas lkllkmiitq yipkhklskl etahcverti pvlltrtgds
      541 sarlrvtaan fiqemalfke vkslqiipsy lvqplkanss vhlamsqmgl larllkdlgt
      601 gssgftidnv mkfsvsaleh rvyevretav riildmyrqh qasileylpp ddsntrrnil
      661 yktifegfak idgratdaem rarrkaatee aekqkkeeik alqgqlaalk eiqaevqeke
      721 sdavkpknqd iqggkaapae algipdehyl dnlcifcger sesfteegld lhywkhclml
      781 trcdhckqvv eissltehll tecdkkdgfg kcyrcseavf keelprhikh kdcnpakpek
      841 lanrcplche nfspgeeawk ahlmgpagct mnlrkthilq kapalqpgks savaasgplg
      901 skagskiptp kgglsksssr tyakr
//
LOCUS       NP_001658                184 aa            linear   PRI 20-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001658
VERSION     NP_001658.2
DBSOURCE    REFSEQ: accession NM_001667.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Lee,H., Choi,S., Ha,S., Yoon,S. and Kim,W.Y.
  TITLE     ARL2 is required for homologous recombination repair and colon
            cancer stem cell survival
  JOURNAL   FEBS Open Bio 12 (8), 1523-1533 (2022)
   PUBMED   35567502
  REMARK    GeneRIF: ARL2 is required for homologous recombination repair and
            colon cancer stem cell survival.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Bartolini,F., Bhamidipati,A., Thomas,S., Schwahn,U., Lewis,S.A. and
            Cowan,N.J.
  TITLE     Functional overlap between retinitis pigmentosa 2 protein and the
            tubulin-specific chaperone cofactor C
  JOURNAL   J Biol Chem 277 (17), 14629-14634 (2002)
   PUBMED   11847227
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Sharer,J.D., Shern,J.F., Van Valkenburgh,H., Wallace,D.C. and
            Kahn,R.A.
  TITLE     ARL2 and BART enter mitochondria and bind the adenine nucleotide
            transporter
  JOURNAL   Mol Biol Cell 13 (1), 71-83 (2002)
   PUBMED   11809823
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Bhamidipati,A., Lewis,S.A. and Cowan,N.J.
  TITLE     ADP ribosylation factor-like protein 2 (Arl2) regulates the
            interaction of tubulin-folding cofactor D with native tubulin
  JOURNAL   J Cell Biol 149 (5), 1087-1096 (2000)
   PUBMED   10831612
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Guru,S.C., Agarwal,S.K., Manickam,P., Olufemi,S.E., Crabtree,J.S.,
            Weisemann,J.M., Kester,M.B., Kim,Y.S., Wang,Y., Emmert-Buck,M.R.,
            Liotta,L.A., Spiegel,A.M., Boguski,M.S., Roe,B.A., Collins,F.S.,
            Marx,S.J., Burns,L. and Chandrasekharappa,S.C.
  TITLE     A transcript map for the 2.8-Mb region containing the multiple
            endocrine neoplasia type 1 locus
  JOURNAL   Genome Res 7 (7), 725-735 (1997)
   PUBMED   9253601
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Clark,J., Moore,L., Krasinskas,A., Way,J., Battey,J., Tamkun,J. and
            Kahn,R.A.
  TITLE     Selective amplification of additional members of the
            ADP-ribosylation factor (ARF) family: cloning of additional human
            and Drosophila ARF-like genes
  JOURNAL   Proc Natl Acad Sci U S A 90 (19), 8952-8956 (1993)
   PUBMED   8415637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG706294.1, BC002530.2 and AI631767.1.
            
            On Jun 6, 2007 this sequence version replaced NP_001658.1.
            
            Summary: This gene encodes a small GTP-binding protein of the RAS
            superfamily which functions as an ADP-ribosylation factor (ARF).
            The encoded protein is one of a functionally distinct group of
            ARF-like genes. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.712375.1,
                                           SRR1163657.315045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246747.9/ ENSP00000246747.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..184
                     /product="ADP-ribosylation factor-like protein 2 isoform
                     1"
                     /note="ADP-ribosylation factor-like protein 2;
                     ADP-ribosylation factor-like 2; ADP ribosylation factor
                     like GTPase 2"
                     /calculated_mol_wt=20747
     Region          3..175
                     /region_name="Arl2"
                     /note="Arf-like 2 (Arl2) GTPase; cd04154"
                     /db_xref="CDD:206720"
     Site            23..30
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206720"
     Site            order(25..31,46..47,69,125..126,128,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206720"
     Site            order(25..26,30,34,46..53,75,80)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206720"
     Site            35..50
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206720"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0J4; propagated from
                     UniProtKB/Swiss-Prot (P36404.4)"
     Site            order(47..51,56,66,70,76,78..80)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206720"
     Site            47
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206720"
     Site            order(48..55,65,76,79..80)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206720"
     Site            order(51..57,60..65)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206720"
     Site            66..83
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206720"
     Site            66..69
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206720"
     Site            125..128
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206720"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206720"
     CDS             1..184
                     /gene="ARL2"
                     /gene_synonym="ARFL2; MRCS1"
                     /coded_by="NM_001667.4:49..603"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8088.1"
                     /db_xref="GeneID:402"
                     /db_xref="HGNC:HGNC:693"
                     /db_xref="MIM:601175"
ORIGIN      
        1 mglltilkkm kqkerelrll mlgldnagkt tilkkfnged idtisptlgf niktlehrgf
       61 klniwdvggq kslrsywrny festdgliwv vdsadrqrmq dcqrelqsll veerlagatl
      121 lifankqdlp galssnaire vleldsirsh hwciqgcsav tgenllpgid wllddissri
      181 ftad
//
LOCUS       NP_001020414             633 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001020414
VERSION     NP_001020414.1
DBSOURCE    REFSEQ: accession NM_001025243.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Rao,Z., Ao,G., Zhang,Y., Jiang,Z., Li,L. and Hua,Z.
  TITLE     HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and
            inflammatory response alleviating renal injury in diabetic
            nephropathy
  JOURNAL   Immunobiology 229 (5), 152835 (2024)
   PUBMED   38986278
  REMARK    GeneRIF: HNRNP I promotes IRAK1 degradation to reduce podocyte
            apoptosis and inflammatory response alleviating renal injury in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Chen,J.J., Lu,T.Z., Wang,T., Yan,W.H., Zhong,F.Y., Qu,X.H.,
            Gong,X.C., Li,J.G., Tou,F.F., Jiang,L.P. and Han,X.J.
  TITLE     The m6A reader HNRNPC promotes glioma progression by enhancing the
            stability of IRAK1 mRNA through the MAPK pathway
  JOURNAL   Cell Death Dis 15 (6), 390 (2024)
   PUBMED   38830885
  REMARK    GeneRIF: The m6A reader HNRNPC promotes glioma progression by
            enhancing the stability of IRAK1 mRNA through the MAPK pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Zhou,M., Liu,Y., Xu,H., Chen,X., Zheng,N., Duan,Z., Ge,Y., Li,D.,
            Lin,T., Zeng,R., Chen,Q. and Li,M.
  TITLE     YTHDC1-Modified m6A Methylation of Hsa_circ_0102678 Promotes
            Keratinocyte Inflammation Induced by Cutibacterium acnes Biofilm
            through Regulating miR-146a/TRAF6 and IRAK1 Axis
  JOURNAL   J Innate Immun 15 (1), 822-835 (2023)
   PUBMED   37903473
  REMARK    GeneRIF: YTHDC1-Modified m6A Methylation of Hsa_circ_0102678
            Promotes Keratinocyte Inflammation Induced by Cutibacterium acnes
            Biofilm through Regulating miR-146a/TRAF6 and IRAK1 Axis.
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Muzio,M., Ni,J., Feng,P. and Dixit,V.M.
  TITLE     IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators
            of IL-1 signaling
  JOURNAL   Science 278 (5343), 1612-1615 (1997)
   PUBMED   9374458
REFERENCE   7  (residues 1 to 633)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   8  (residues 1 to 633)
  AUTHORS   DiDonato,J.A., Hayakawa,M., Rothwarf,D.M., Zandi,E. and Karin,M.
  TITLE     A cytokine-responsive IkappaB kinase that activates the
            transcription factor NF-kappaB
  JOURNAL   Nature 388 (6642), 548-554 (1997)
   PUBMED   9252186
REFERENCE   9  (residues 1 to 633)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 633)
  AUTHORS   Cao,Z., Henzel,W.J. and Gao,X.
  TITLE     IRAK: a kinase associated with the interleukin-1 receptor
  JOURNAL   Science 271 (5252), 1128-1131 (1996)
   PUBMED   8599092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2, L76191.1, BC054000.1,
            BC014963.1 and BE276817.1.
            
            Summary: This gene encodes the interleukin-1 receptor-associated
            kinase 1, one of two putative serine/threonine kinases that become
            associated with the interleukin-1 receptor (IL1R) upon stimulation.
            This gene is partially responsible for IL1-induced upregulation of
            the transcription factor NF-kappa B. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks an in-frame exon, as
            compared to variant 1. The encoded isoform 3 thus lacks an internal
            segment, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014963.1, DQ054788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..633
                     /product="interleukin-1 receptor-associated kinase 1
                     isoform 3"
                     /EC_number="2.7.11.1"
                     /note="Pelle homolog"
                     /calculated_mol_wt=67891
     Region          17..100
                     /region_name="Death_IRAK1"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-1; cd08794"
                     /db_xref="CDD:260061"
     Site            order(19..20,22..25,58,67..68,71..77,82)
                     /site_type="other"
                     /note="putative IRAK1-IRAK4 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:260061"
     Region          218..>434
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(218..221,224,226,237,239,272,288..291,340,344..345,
                     347,357..358)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271061"
     CDS             1..633
                     /gene="IRAK1"
                     /gene_synonym="IRAK; pelle"
                     /coded_by="NM_001025243.2:91..1992"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS35443.1"
                     /db_xref="GeneID:3654"
                     /db_xref="HGNC:HGNC:6112"
                     /db_xref="MIM:300283"
ORIGIN      
        1 maggpgpgep aapgaqhfly evppwvmcrf ykvmdalepa dwcqfaaliv rdqtelrlce
       61 rsgqrtasvl wpwinrnarv adlvhilthl qllrardiit awhppaplps pgttaprpss
      121 ipapaeaeaw sprklpssas tflspafpgs qthsgpelgl vpspaslwpp ppspapsstk
      181 pgpessvsll qgarpfpfcw plceisrgth nfseelkige ggfgcvyrav mrntvyavkr
      241 lkenadlewt avkqsfltev eqlsrfrhpn ivdfagycaq ngfyclvygf lpngsledrl
      301 hcqtqacppl swpqrldill gtaraiqflh qdspslihgd ikssnvllde rltpklgdfg
      361 larfsrfags spsqssmvar tqtvrgtlay lpeeyiktgr lavdtdtfsf gvvvletlag
      421 qravkthgar tkylvyerle klqavvagvp ghseaascip pspqensyvs stgrahsgaa
      481 pwqplaapsg asaqaaeqlq rgpnqpvesd eslgglsaal rswhltpscp ldpaplreag
      541 cpqgdtages swgsgpgsrp taveglalgs sasssseppq iiinparqkm vqklalyedg
      601 aldslqllss sslpglgleq drqgpeesde fqs
//
LOCUS       NP_005111               2177 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 12 [Homo
            sapiens].
ACCESSION   NP_005111
VERSION     NP_005111.2
DBSOURCE    REFSEQ: accession NM_005120.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2177)
  AUTHORS   Chen,J., Wang,T. and Mu,W.
  TITLE     A C->T Variation in 3'-Untranslated Region Elevates MED12 Protein
            Level in Breast Cancer That Relates to Better Prognosis
  JOURNAL   Genet Test Mol Biomarkers 28 (9), 343-350 (2024)
   PUBMED   39166292
  REMARK    GeneRIF: A C->T Variation in 3'-Untranslated Region Elevates MED12
            Protein Level in Breast Cancer That Relates to Better Prognosis.
REFERENCE   3  (residues 1 to 2177)
  AUTHORS   Li,Y., Asif,H., Feng,Y., Kim,J.J. and Wei,J.J.
  TITLE     Somatic MED12 Mutations in Myometrial Cells
  JOURNAL   Cells 13 (17), 1432 (2024)
   PUBMED   39273004
  REMARK    GeneRIF: Somatic MED12 Mutations in Myometrial Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2177)
  AUTHORS   Maia-Silva,D., Cunniff,P.J., Schier,A.C., Skopelitis,D.,
            Trousdell,M.C., Moresco,P., Gao,Y., Kechejian,V., He,X.Y.,
            Sahin,Y., Wan,L., Alpsoy,A., Liverpool,J., Krainer,A.R.,
            Egeblad,M., Spector,D.L., Fearon,D.T., Dos Santos,C.O.,
            Taatjes,D.J. and Vakoc,C.R.
  TITLE     Interaction between MED12 and DeltaNp63 activates basal identity in
            pancreatic ductal adenocarcinoma
  JOURNAL   Nat Genet 56 (7), 1377-1385 (2024)
   PUBMED   38886586
  REMARK    GeneRIF: Interaction between MED12 and DeltaNp63 activates basal
            identity in pancreatic ductal adenocarcinoma.
REFERENCE   5  (residues 1 to 2177)
  AUTHORS   Khan,N.H., McNally,R., Kim,J.J. and Wei,J.J.
  TITLE     Racial disparity in uterine leiomyoma: new insights of genetic and
            environmental burden in myometrial cells
  JOURNAL   Mol Hum Reprod 30 (3) (2024)
   PUBMED   38290796
  REMARK    GeneRIF: Racial disparity in uterine leiomyoma: new insights of
            genetic and environmental burden in myometrial cells.
            Review article
REFERENCE   6  (residues 1 to 2177)
  AUTHORS   Briault,S., Hill,R., Shrimpton,A., Zhu,D., Till,M., Ronce,N.,
            Margaritte-Jeannin,P., Baraitser,M., Middleton-Price,H.,
            Malcolm,S., Thompson,E., Hoo,J., Wilson,G., Romano,C., Guichet,A.,
            Pembrey,M., Fontes,M., Poustka,A. and Moraine,C.
  TITLE     A gene for FG syndrome maps in the Xq12-q21.31 region
  JOURNAL   Am J Med Genet 73 (1), 87-90 (1997)
   PUBMED   9375929
REFERENCE   7  (residues 1 to 2177)
  AUTHORS   Margolis,R.L., Abraham,M.R., Gatchell,S.B., Li,S.H., Kidwai,A.S.,
            Breschel,T.S., Stine,O.C., Callahan,C., McInnis,M.G. and Ross,C.A.
  TITLE     cDNAs with long CAG trinucleotide repeats from human brain
  JOURNAL   Hum Genet 100 (1), 114-122 (1997)
   PUBMED   9225980
REFERENCE   8  (residues 1 to 2177)
  AUTHORS   Fondell,J.D., Ge,H. and Roeder,R.G.
  TITLE     Ligand induction of a transcriptionally active thyroid hormone
            receptor coactivator complex
  JOURNAL   Proc Natl Acad Sci U S A 93 (16), 8329-8333 (1996)
   PUBMED   8710870
REFERENCE   9  (residues 1 to 2177)
  AUTHORS   Yamagata,K., Takeda,J., Menzel,S., Chen,X., Eng,S., Lim,L.R.,
            Concannon,P., Hanis,C.L., Spielman,R.S., Cox,N.J. and Bell,G.I.
  TITLE     Searching for NIDDM susceptibility genes: studies of genes with
            triplet repeats expressed in skeletal muscle
  JOURNAL   Diabetologia 39 (6), 725-730 (1996)
   PUBMED   8781769
REFERENCE   10 (residues 1 to 2177)
  AUTHORS   Lyons,M.J.
  TITLE     MED12-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301719
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB069668.1, AF117755.1,
            AF071309.1 and BM662470.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 14, 2006 this sequence version replaced NP_005111.1.
            
            Summary: The initiation of transcription is controlled in part by a
            large protein assembly known as the preinitiation complex. A
            component of this preinitiation complex is a 1.2 MDa protein
            aggregate called Mediator. This Mediator component binds with a
            CDK8 subcomplex which contains the protein encoded by this gene,
            mediator complex subunit 12 (MED12), along with MED13, CDK8 kinase,
            and cyclin C. The CDK8 subcomplex modulates Mediator-polymerase II
            interactions and thereby regulates transcription initiation and
            reinitation rates. The MED12 protein is essential for activating
            CDK8 kinase. Defects in this gene cause X-linked Opitz-Kaveggia
            syndrome, also known as FG syndrome, and Lujan-Fryns syndrome.
            [provided by RefSeq, Aug 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2496534.1,
                                           SRR14038191.1615767.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374080.8/ ENSP00000363193.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..2177
                     /product="mediator of RNA polymerase II transcription
                     subunit 12"
                     /note="thyroid hormone receptor-associated protein, 230
                     kDa subunit; trinucleotide repeat containing 11
                     (THR-associated protein, 230 kDa subunit); putative
                     mediator subunit 12; activator-recruited cofactor 240 kDa
                     component; CAG repeat protein 45; human opposite paired;
                     OPA-containing protein; trinucleotide repeat-containing
                     gene 11 protein; thyroid hormone receptor-associated
                     protein complex 230 kDa component; mediator of RNA
                     polymerase II transcription, subunit 12 homolog; Kohtalo
                     homolog"
                     /calculated_mol_wt=242952
     Region          12..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            80
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2AGH6; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          106..161
                     /region_name="Med12"
                     /note="Transcription mediator complex subunit Med12;
                     pfam09497"
                     /db_xref="CDD:462818"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          286..757
                     /region_name="Med12-LCEWAV"
                     /note="Eukaryotic Mediator 12 subunit domain; pfam12145"
                     /db_xref="CDD:463472"
     Region          323..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          627..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          690..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1241..1266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Site            1269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1394..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1450..1474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1616..2051
                     /region_name="Interaction with CTNNB1 and GLI3.
                     /evidence=ECO:0000269|PubMed:17000779"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1738..1829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            1798
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2AGH6; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1819..2022
                     /region_name="Med12-PQL"
                     /note="Eukaryotic Mediator 12 catenin-binding domain;
                     pfam12144"
                     /db_xref="CDD:463471"
     Site            1899
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A2AGH6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A2AGH6; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Site            1910
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2AGH6; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1919..1938
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          1967..1989
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Site            1994
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Site            2015
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q93074.4)"
     Region          2115..2149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     Region          2158..2177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93074.4)"
     CDS             1..2177
                     /gene="MED12"
                     /gene_synonym="ARC240; CAGH45; FGS1; HDKR; HOPA; Kto;
                     MED12S; OHDOX; OKS; OPA1; TNRC11; TRAP230"
                     /coded_by="NM_005120.3:160..6693"
                     /db_xref="CCDS:CCDS43970.1"
                     /db_xref="GeneID:9968"
                     /db_xref="HGNC:HGNC:11957"
                     /db_xref="MIM:300188"
ORIGIN      
        1 maafgilsye hrplkrprlg ppdvypqdpk qkedeltaln vkqgfnnqpa vsgdehgsak
       61 nvsfnpakis snfssiiaek lrcntlpdtg rrkpqvnqkd nfwlvtarsq saintwftdl
      121 agtkpltqla kkvpifskke evfgylakyt vpvmraawli kmtcayyaai setkvkkrhv
      181 dpfmewtqii tkylweqlqk maeyyrpgpa gsggcgstig plphdvevai rqwdytekla
      241 mfmfqdgmld rhefltwvle cfekirpged ellklllpll lrysgefvqs aylsrrlayf
      301 ctrrlalqld gvsshsshvi saqststlpt tpapqpptss tpstpfsdll mcpqhrplvf
      361 glscilqtil lccpsalvwh ysltdsrikt gspldhlpia psnlpmpegn saftqqvrak
      421 lreieqqike rgqavevrws fdkcqeatag ftigrvlhtl evldshsfer sdfsnsldsl
      481 cnrifglgps kdgheissdd davvsllcew avsckrsgrh ramvvaklle krqaeieaer
      541 cgeseaadek gsiasgslsa psapifqdvl lqfldtqapm ltdprseser veffnlvllf
      601 celirhdvfs hnmytctlis rgdlafgapg prppspfddp addpehkeae gsssskledp
      661 glsesmdidp sssvlfedme kpdfslfspt mpcegkgsps pekpdvekev kpppkekieg
      721 tlgvlydqpr hvqyathfpi pqeescshec nqrlvvlfgv gkqrddarha ikkitkdilk
      781 vlnrkgtaet dqlapivpln pgdltflgge dgqkrrrnrp eafptaedif akfqhlshyd
      841 qhqvtaqvsr nvleqitsfa lgmsyhlplv qhvqfifdlm eyslsisgli dfaiqllnel
      901 svveaelllk ssdlvgsytt slclcivavl rhyhacliln qdqmaqvfeg lcgvvkhgmn
      961 rsdgssaerc ilaylydlyt scshlknkfg elfsdfcskv kntiycnvep sesnmrwape
     1021 fmidtlenpa ahtftytglg kslsenpanr ysfvcnalmh vcvghhdpdr vndiailcae
     1081 ltgyckslsa ewlgvlkalc cssnngtcgf ndllcnvdvs dlsfhdslat fvailiarqc
     1141 llledlirca aipsllnaac seqdsepgar ltcrillhlf ktpqlnpcqs dgnkptvgir
     1201 sscdrhllaa sqnrivdgav favlkavfvl gdaelkgsgf tvtggteelp eeeggggsgg
     1261 rrqggrnisv etasldvyak yvlrsicqqe wvgerclksl cedsndlqdp vlssaqaqrl
     1321 mqlicyphrl ldnedgenpq rqrikrilqn ldqwtmrqss lelqlmikqt pnnemnslle
     1381 niakatievf qqsaetgsss gstasnmpss sktkpvlssl ersgvwlvap liaklptsvq
     1441 ghvlkaagee lekgqhlgss srkerdrqkq ksmsllsqqp flslvltclk gqdeqregll
     1501 tslysqvhqi vnnwrddqyl ddckpkqlmh ealklrlnlv ggmfdtvqrs tqqttewaml
     1561 lleiiisgtv dmqsnnelft tvldmlsvli ngtlaadmss isqgsmeenk raymnlakkl
     1621 qkelgerqsd slekvrqllp lpkqtrdvit cepqgslidt kgnkiagfds ifkkeglqvs
     1681 tkqkispwdl feglkpsapl swgwfgtvrv drrvargeeq qrlllyhthl rprprayyle
     1741 plplppedee ppaptllepe kkapeppktd kpgaappste erkkkstkgk krsqpatkte
     1801 dygmgpgrsg pygvtvppdl lhhpnpgsit hlnyrqgsig lytqnqplpa ggprvdpyrp
     1861 vrlpmqklpt rptypgvlpt tmtgvmglep ssyktsvyrq qqpavpqgqr lrqqlqqsqg
     1921 mlgqssvhqm tpsssyglqt sqgytpyvsh vglqqhtgpa gtmvppsyss qpyqsthpst
     1981 nptlvdptrh lqqrpsgyvh qqaptyghgl tstqrfshqt lqqtpmistm tpmsaqgvqa
     2041 gvrstailpe qqqqqqqqqq qqqqqqqqqq qqqqqqyhir qqqqqqilrq qqqqqqqqqq
     2101 qqqqqqqqqq qqqqqhqqqq qqqaappqpq pqsqpqfqrq glqqtqqqqq taalvrqlqq
     2161 qlsntqpqps tnifgry
//
LOCUS       NP_038460               1378 aa            linear   PRI 20-NOV-2025
DEFINITION  tonsoku-like protein [Homo sapiens].
ACCESSION   NP_038460
VERSION     NP_038460.4
DBSOURCE    REFSEQ: accession NM_013432.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1378)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1378)
  AUTHORS   Lee,H., Ha,S., Choi,S., Do,S., Yoon,S., Kim,Y.K. and Kim,W.Y.
  TITLE     Oncogenic Impact of TONSL, a Homologous Recombination Repair
            Protein at the Replication Fork, in Cancer Stem Cells
  JOURNAL   Int J Mol Sci 24 (11), 9530 (2023)
   PUBMED   37298484
  REMARK    GeneRIF: Oncogenic Impact of TONSL, a Homologous Recombination
            Repair Protein at the Replication Fork, in Cancer Stem Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1378)
  AUTHORS   Khatpe,A.S., Dirks,R., Bhat-Nakshatri,P., Mang,H., Batic,K.,
            Swiezy,S., Olson,J., Rao,X., Wang,Y., Tanaka,H., Liu,S., Wan,J.,
            Chen,D., Liu,Y., Fang,F., Althouse,S., Hulsey,E., Granatir,M.M.,
            Addison,R., Temm,C.J., Sandusky,G., Lee-Gosselin,A., Nephew,K.,
            Miller,K.D. and Nakshatri,H.
  TITLE     TONSL Is an Immortalizing Oncogene and a Therapeutic Target in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1345-1360 (2023)
   PUBMED   37057595
  REMARK    GeneRIF: TONSL Is an Immortalizing Oncogene and a Therapeutic
            Target in Breast Cancer.
REFERENCE   4  (residues 1 to 1378)
  AUTHORS   van Schie,J.J., de Lint,K., Pai,G.M., Rooimans,M.A., Wolthuis,R.M.
            and de Lange,J.
  TITLE     MMS22L-TONSL functions in sister chromatid cohesion in a pathway
            parallel to DSCC1-RFC
  JOURNAL   Life Sci Alliance 6 (2), e202201596 (2022)
   PUBMED   36622344
  REMARK    GeneRIF: MMS22L-TONSL functions in sister chromatid cohesion in a
            pathway parallel to DSCC1-RFC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1378)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1378)
  AUTHORS   Duro,E., Lundin,C., Ask,K., Sanchez-Pulido,L., MacArtney,T.J.,
            Toth,R., Ponting,C.P., Groth,A., Helleday,T. and Rouse,J.
  TITLE     Identification of the MMS22L-TONSL complex that promotes homologous
            recombination
  JOURNAL   Mol Cell 40 (4), 632-644 (2010)
   PUBMED   21055984
  REMARK    GeneRIF: MMS22L and TONSL are required for the maintenance of
            genome stability.
REFERENCE   7  (residues 1 to 1378)
  AUTHORS   O'Donnell,L., Panier,S., Wildenhain,J., Tkach,J.M., Al-Hakim,A.,
            Landry,M.C., Escribano-Diaz,C., Szilard,R.K., Young,J.T., Munro,M.,
            Canny,M.D., Kolas,N.K., Zhang,W., Harding,S.M., Ylanko,J.,
            Mendez,M., Mullin,M., Sun,T., Habermann,B., Datti,A., Bristow,R.G.,
            Gingras,A.C., Tyers,M.D., Brown,G.W. and Durocher,D.
  TITLE     The MMS22L-TONSL complex mediates recovery from replication stress
            and homologous recombination
  JOURNAL   Mol Cell 40 (4), 619-631 (2010)
   PUBMED   21055983
  REMARK    GeneRIF: These results indicate that MMS22L and TONSL are genome
            caretakers that stimulate the recombination-dependent repair of
            stalled or collapsed replication forks.
REFERENCE   8  (residues 1 to 1378)
  AUTHORS   Wang,Y., Fu,W., Xie,F., Wang,Y., Chu,X., Wang,H., Shen,M., Wang,Y.,
            Wang,Y., Sun,W., Lei,R., Yang,L., Wu,H., Foo,J., Liu,J., Jin,L. and
            Huang,W.
  TITLE     Common polymorphisms in ITGA2, PON1 and THBS2 are associated with
            coronary atherosclerosis in a candidate gene association study of
            the Chinese Han population
  JOURNAL   J Hum Genet 55 (8), 490-494 (2010)
   PUBMED   20485444
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1378)
  AUTHORS   Norman,D.A. and Barton,P.J.
  TITLE     Isolation, sequence, and chromosomal localisation of the human
            IkappaBR gene (NFKBIL2)
  JOURNAL   Ann Hum Genet 64 (Pt 1), 15-23 (2000)
   PUBMED   11246458
REFERENCE   10 (residues 1 to 1378)
  AUTHORS   Ray,P., Zhang,D.H., Elias,J.A. and Ray,A.
  TITLE     Cloning of a differentially expressed I kappa B-related protein
  JOURNAL   J Biol Chem 270 (18), 10680-10685 (1995)
   PUBMED   7738005
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084125.9, CN366457.1,
            BC008782.2, BF475381.1 and AC233992.5.
            
            On May 7, 2008 this sequence version replaced NP_038460.3.
            
            Summary: The protein encoded by this gene is thought to be a
            negative regulator of NF-kappa-B mediated transcription. The
            encoded protein may bind NF-kappa-B complexes and trap them in the
            cytoplasm, preventing them from entering the nucleus and
            interacting with the DNA. Phosphorylation of this protein targets
            it for degradation by the ubiquitination pathway, which frees the
            NF-kappa-B complexes to enter the nucleus. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008782.2, SRR1803616.59587.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409379.8/ ENSP00000386239.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1378
                     /product="tonsoku-like protein"
                     /note="nuclear factor of kappa light polypeptide gene
                     enhancer in B-cells inhibitor-like 2; I-kappa-B-related
                     protein; NF-kappa-B inhibitor-like protein 2; ikappaBR;
                     inhibitor of kappa B-related protein"
                     /calculated_mol_wt=150798
     Region          27..60
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          27..55
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(28,31..32,35..36,38,68,71..72,75..76,78..79,108,
                     111..112,115..116,119)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          43..>355
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          66..96
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          67..100
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          107..147
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          107..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          162..195
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Site            order(163,166..167,170..171,173,203,206..207,210..211,
                     213..214,243,246..247,250..251,254)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          163..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          195..231
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          202..235
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          242..275
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          242..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          276..300
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          311..344
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Site            order(316,319..320,322,353,356..357,360..361,363..364,391,
                     394..395,398..399,402)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          316..339
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          351..381
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          352..385
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          390..419
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          475..524
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          <517..>635
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(528,530,534..535,538..540,542..543,547,550,559,561,
                     563,567..568,571..573,575..576,580,583,592,594,596,
                     603..604,607..609,611..612,616,619)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          528..559
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          528..557
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          561..592
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          561..590
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          594..627
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          597..626
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          667..789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          <668..922
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Site            797
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZL6; propagated from
                     UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          842..933
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          <1024..1338
                     /region_name="RNA1"
                     /note="Ran GTPase-activating protein (RanGAP) involved in
                     mRNA processing and transport [Translation, ribosomal
                     structure and biogenesis]; COG5238"
                     /db_xref="CDD:444072"
     Region          1069..1093
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1072..1099
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1097..1122
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1100..1130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1128..1151
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1131..1158
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1159..1190
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1188..1212
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1191..1215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1216..1249
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1247..1270
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1250..1277
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1275..1300
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1278..1300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1308..1333
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          1331..1354
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HA7.2)"
     Region          1334..1355
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..1378
                     /gene="TONSL"
                     /gene_synonym="IKBR; NFKBIL2; SEMDSP"
                     /coded_by="NM_013432.5:27..4163"
                     /db_xref="CCDS:CCDS34968.2"
                     /db_xref="GeneID:4796"
                     /db_xref="HGNC:HGNC:7801"
                     /db_xref="MIM:604546"
ORIGIN      
        1 mslerelrql skakakaqra gqrreeaalc hqlgellagh gryaealeqh wqelqlrera
       61 ddplgcavah rkigerlaem edypaalqhq hqylelahsl rnhtelqraw atigrthldi
      121 ydhcqsrdal lqaqaafeks laivdeeleg tlaqgelnem rtrlylnlgl tfeslqqtal
      181 cndyfrksif laeqnhlyed lfrarynlgt ihwragqhsq amrclegare cahtmrkrfm
      241 eseccvviaq vlqdlgdfla akralkkayr lgsqkpvqra aicqnlqhvl avvrlqqqle
      301 eaegrdpqga mviceqlgdl fskagdfpra aeayqkqlrf aelldrpgae raiihvslat
      361 tlgdmkdhhg avrhyeeelr lrsgnvleea ktwlnialsr eeagdayell apcfqkalsc
      421 aqqaqrpqlq rqvlqhlhtv qlrlqpqeap etetrlrels vaededeeee aeeaaataes
      481 ealeagevel segeddtdgl tpqleedeel qghlgrrkgs kwnrrndmge tllhracieg
      541 qlrrvqdlvr qghplnprdy cgwtplheac nyghleivrf lldhgaavdd pggqgcegit
      601 plhdalncgh fevaelller gasvtlrtrk glspletlqq wvklyrrdld letrqkaram
      661 emllqaaasg qdphssqafh tpssllfdpe tspplspcpe ppsnstrlpe asqahvrvsp
      721 gqaapamarp rrsrhgpass ssssegedsa gparpsqkrp rcsataqrva awtpgpasnr
      781 eaatastsra ayqaairgvg saqsrlgpgp prghskalap qaalipeeec lagdwleldm
      841 pltrsrrprp rgtgdnrrps stsgsdsees rprarakqvr ltcmqscsap vnagpsslas
      901 eppgspstpr vsepsgdssa agqplgpapp ppirvrvqvq dhlflipvph ssdthsvawl
      961 aeqaaqryyq tcgllprltl rkegallapq dlipdvlqsn devlaevtsw dlppltdryr
     1021 racqslgqge hqqvlqavel qglglsfsac slaldqaqlt pllralklht alrelrlagn
     1081 rlgdkcvael vaalgtmpsl alldlssnhl gpeglrqlam glpgqatlqs leeldlsmnp
     1141 lgdgcgqsla sllhacplls tlrlqacgfg psfflshqta lgsafqdaeh lktlslsyna
     1201 lgapalartl qslpagtllh lelssvaagk gdsdlmepvf rylakegcal ahltlsanhl
     1261 gdkavrdlcr clslcpslis ldlsanpeis casleellst lqkrpqglsf lglsgcavqg
     1321 plglglwdki aaqlrelqlc srrlcaedrd alrqlqpsrp gpgectldhg sklffrrl
//
LOCUS       NP_001228                432 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-A2 [Homo sapiens].
ACCESSION   NP_001228
VERSION     NP_001228.2
DBSOURCE    REFSEQ: accession NM_001237.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Cao,M.G., Wang,Y., Yang,Z.M., Wang,Y., Wang,M.Q., Zhuo,S., Yang,Y.
            and Liu,C.S.
  TITLE     The effect of miR-381 on proliferation and prognosis of breast
            cancer by altering CCNA2 expression
  JOURNAL   J Obstet Gynaecol 44 (1), 2360547 (2024)
   PUBMED   38904638
  REMARK    GeneRIF: The effect of miR-381 on proliferation and prognosis of
            breast cancer by altering CCNA2 expression.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   He,Q., Qu,M., Xu,C., Wu,L., Xu,Y., Su,J., Bao,H., Shen,T., He,Y.,
            Cai,J., Xu,D., Zeng,L.H. and Wu,X.
  TITLE     Smoking-induced CCNA2 expression promotes lung adenocarcinoma
            tumorigenesis by boosting AT2/AT2-like cell differentiation
  JOURNAL   Cancer Lett 592, 216922 (2024)
   PUBMED   38704137
  REMARK    GeneRIF: Smoking-induced CCNA2 expression promotes lung
            adenocarcinoma tumorigenesis by boosting AT2/AT2-like cell
            differentiation.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Zhang,J., Di,Y., Zhang,B., Li,T., Li,D. and Zhang,H.
  TITLE     CDK1 and CCNA2 play important roles in oral squamous cell carcinoma
  JOURNAL   Medicine (Baltimore) 103 (16), e37831 (2024)
   PUBMED   38640322
  REMARK    GeneRIF: CDK1 and CCNA2 play important roles in oral squamous cell
            carcinoma.
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Hutchenreuther,J., Nguyen,J., Quesnel,K., Vincent,K.M.,
            Petitjean,L., Bourgeois,S., Boyd,M., Bou-Gharios,G., Postovit,L.M.
            and Leask,A.
  TITLE     Cancer-associated Fibroblast-specific Expression of the
            Matricellular Protein CCN1 Coordinates Neovascularization and
            Stroma Deposition in Melanoma Metastasis
  JOURNAL   Cancer Res Commun 4 (2), 556-570 (2024)
   PUBMED   38363129
  REMARK    GeneRIF: Cancer-associated Fibroblast-specific Expression of the
            Matricellular Protein CCN1 Coordinates Neovascularization and
            Stroma Deposition in Melanoma Metastasis.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Bailly,E., Pines,J., Hunter,T. and Bornens,M.
  TITLE     Cytoplasmic accumulation of cyclin B1 in human cells: association
            with a detergent-resistant compartment and with the centrosome
  JOURNAL   J Cell Sci 101 (Pt 3), 529-545 (1992)
   PUBMED   1387877
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Faha,B., Ewen,M.E., Tsai,L.H., Livingston,D.M. and Harlow,E.
  TITLE     Interaction between human cyclin A and adenovirus E1A-associated
            p107 protein
  JOURNAL   Science 255 (5040), 87-90 (1992)
   PUBMED   1532458
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Paterlini,P., De Mitri,M.S., Martin,C., Munnich,A. and Brechot,C.
  TITLE     A TaqI polymorphism in the human cyclin A gene
  JOURNAL   Nucleic Acids Res 19 (9), 2516 (1991)
   PUBMED   1675006
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Wang,J., Chenivesse,X., Henglein,B. and Brechot,C.
  TITLE     Hepatitis B virus integration in a cyclin A gene in a
            hepatocellular carcinoma
  JOURNAL   Nature 343 (6258), 555-557 (1990)
   PUBMED   1967822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079341.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2018 this sequence version replaced NP_001228.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members function as regulators of
            the cell cycle. This protein binds and activates cyclin-dependent
            kinase 2 and thus promotes transition through G1/S and G2/M.
            [provided by RefSeq, Aug 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4643867.21931.1,
                                           ERR4643888.33318.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274026.10/ ENSP00000274026.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q27"
     Protein         1..432
                     /product="cyclin-A2"
                     /note="cyclin-A"
                     /calculated_mol_wt=48420
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P20248.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20248.2)"
     Region          26..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20248.2)"
     Region          55..75
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20248.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P20248.2)"
     Region          98..161
                     /region_name="Cyclin_N2"
                     /note="Cyclin-A N-terminal APC/C binding region;
                     pfam16500"
                     /db_xref="CDD:465146"
     Region          175..305
                     /region_name="CYCLIN_CCNA2_rpt1"
                     /note="first cyclin box found in cyclin-A2 (CCNA2) and
                     similar proteins; cd20561"
                     /db_xref="CDD:410264"
     Site            order(177..179,181..182,185,228,263,266..270,274..275,
                     288..289,292,295..296,299..300,303..305)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410264"
     Site            order(210,213..214,216..217,220,224,250..252,254..255,
                     280..283,285..287,290,293..294,297)
                     /site_type="inhibition"
                     /note="inhibitor binding site [polypeptide binding]"
                     /db_xref="CDD:410264"
     Region          309..419
                     /region_name="CYCLIN_CCNA2_rpt2"
                     /note="second cyclin box found in cyclin-A2 (CCNA2) and
                     similar proteins; cd20564"
                     /db_xref="CDD:410267"
     Site            order(312..313,316)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410267"
     CDS             1..432
                     /gene="CCNA2"
                     /gene_synonym="CCN1; CCNA"
                     /coded_by="NM_001237.5:256..1554"
                     /db_xref="CCDS:CCDS3723.1"
                     /db_xref="GeneID:890"
                     /db_xref="HGNC:HGNC:1578"
                     /db_xref="MIM:123835"
ORIGIN      
        1 mlgnsapgpa treagsalla lqqtalqedq eninpekaap vqqprtraal avlksgnprg
       61 laqqqrpktr rvaplkdlpv ndehvtvppw kanskqpaft ihvdeaekea qkkpaesqki
      121 eredalafns aislpgprkp lvpldypmdg sfesphtmdm siiledekpv svnevpdyhe
      181 dihtylreme vkckpkvgym kkqpditnsm railvdwlve vgeeyklqne tlhlavnyid
      241 rflssmsvlr gklqlvgtaa mllaskfeei yppevaefvy itddtytkkq vlrmehlvlk
      301 vltfdlaapt vnqfltqyfl hqqpanckve slamflgels lidadpylky lpsviagaaf
      361 hlalytvtgq swpeslirkt gytleslkpc lmdlhqtylk apqhaqqsir ekyknskyhg
      421 vsllnppetl nl
//
LOCUS       NP_036388                495 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 212 [Homo sapiens].
ACCESSION   NP_036388
VERSION     NP_036388.2
DBSOURCE    REFSEQ: accession NM_012256.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Chung,H.J., Lee,J.R., Kim,T.M., Kim,S., Park,K., Kim,M.J., Jung,E.,
            Kim,S., Lee,E.A., Ra,J.S., Hwang,S., Lee,J.Y., Scharer,O.D.,
            Kim,Y., Myung,K. and Kim,H.
  TITLE     ZNF212 promotes genomic integrity through direct interaction with
            TRAIP
  JOURNAL   Nucleic Acids Res 51 (2), 631-649 (2023)
   PUBMED   36594163
  REMARK    GeneRIF: ZNF212 promotes genomic integrity through direct
            interaction with TRAIP.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Khang,R., Jo,A., Kang,H., Kim,H., Kwag,E., Lee,J.Y., Koo,O.,
            Park,J., Kim,H.K., Jo,D.G., Hwang,I., Ahn,J.Y., Lee,Y., Choi,J.Y.,
            Lee,Y.S. and Shin,J.H.
  TITLE     Loss of zinc-finger protein 212 leads to Purkinje cell death and
            locomotive abnormalities with phospholipase D3 downregulation
  JOURNAL   Sci Rep 11 (1), 22745 (2021)
   PUBMED   34815492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Gao,J., Li,W.X., Feng,S.Q., Yuan,Y.S., Wan,D.F., Han,W. and Yu,Y.
  TITLE     A protein-protein interaction network of transcription factors
            acting during liver cell proliferation
  JOURNAL   Genomics 91 (4), 347-355 (2008)
   PUBMED   18255255
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Becker,K.G., Nagle,J.W., Canning,R.D., Dehejia,A.M.,
            Polymeropoulos,M.H., Gado,A.M., Biddison,W.E. and Drew,P.D.
  TITLE     Molecular cloning and mapping of a novel human KRAB
            domain-containing C2H2-type zinc finger to chromosome 7q36.1
  JOURNAL   Genomics 41 (3), 502-504 (1997)
   PUBMED   9169157
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Becker,K.G., Nagle,J.W., Canning,R.D., Biddison,W.E., Ozato,K. and
            Drew,P.D.
  TITLE     Rapid isolation and characterization of 118 novel C2H2-type zinc
            finger cDNAs expressed in human brain
  JOURNAL   Hum Mol Genet 4 (4), 685-691 (1995)
   PUBMED   7633419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK074821.1 and BC022785.2.
            
            On Nov 8, 2002 this sequence version replaced NP_036388.1.
            
            Summary: This gene belongs to the C2H2-type zinc finger gene
            family. The zinc finger proteins are involved in gene regulation
            and development, and are quite conserved throughout evolution. Like
            this gene product, a third of the zinc finger proteins containing
            C2H2 fingers also contain the KRAB domain, which has been found to
            be involved in protein-protein interactions. [provided by RefSeq,
            Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022785.2, SRR1660807.111762.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335870.7/ ENSP00000338572.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..495
                     /product="zinc finger protein 212"
                     /note="Zinc finger protein C2H2-150"
                     /calculated_mol_wt=55317
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV6.3)"
     Region          142..180
                     /region_name="KRAB_A-box"
                     /note="KRAB (Kruppel-associated box) domain -A box;
                     cd07765"
                     /db_xref="CDD:143639"
     Region          264..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV6.3)"
     Region          316..338
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          318..338
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          337..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV6.3)"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(376,378,380,382..383,386..387,390,434,436,440..441,
                     444..445,448,462,464,466,468..469,472..473,476)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          429..449
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          455..477
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          457..477
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDV6.3)"
     CDS             1..495
                     /gene="ZNF212"
                     /gene_synonym="C2H2-150; ZNF182; ZNFC150"
                     /coded_by="NM_012256.4:129..1616"
                     /db_xref="CCDS:CCDS5896.1"
                     /db_xref="GeneID:7988"
                     /db_xref="HGNC:HGNC:13004"
                     /db_xref="MIM:602386"
ORIGIN      
        1 maesaparhr rkrrstplts stlpsqatek ssyfqtteis lwtvvaaiqa vekkmesqaa
       61 rlqslegrtg taekkladce kmavefgnql egkwavlgtl lqeygllqrr lenvenllrn
      121 rnfwilrlpp gskgeapkvs rslendgvcf teqewenled wqkelyrnvm esnyetlvsl
      181 kvlgqtegea elgtemlgdl eeegpggahp aggvmikqel qytqegpadl pgefsciaee
      241 qaflspeqte lwggqgssvl letgpgdstl eepvgsrvps ssrtvgcpkq kshrqvqldq
      301 ecgqglklkk dtsrpyecse ceitfrykqq lathlrshsg wgsctpeepe eslrprprlk
      361 pqtkkaklhq cdvclrsfsc kvslvthqrc hlqegpsagq hvqerfspns lvalpghipw
      421 rksrsslicg ycgksfshps dlvrhqriht gerpysctec eksfvqkqhl lqhqkihqre
      481 rgglalepgr pngll
//
LOCUS       NP_001357121             339 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357121
VERSION     NP_001357121.1
DBSOURCE    REFSEQ: accession NM_001370192.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Liu,J., Prickett,T.D., Elliott,E., Meroni,G. and Brautigan,D.L.
  TITLE     Phosphorylation and microtubule association of the Opitz syndrome
            protein mid-1 is regulated by protein phosphatase 2A via binding to
            the regulatory subunit alpha 4
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6650-6655 (2001)
   PUBMED   11371618
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Chung,H., Nairn,A.C., Murata,K. and Brautigan,D.L.
  TITLE     Mutation of Tyr307 and Leu309 in the protein phosphatase 2A
            catalytic subunit favors association with the alpha 4 subunit which
            promotes dephosphorylation of elongation factor-2
  JOURNAL   Biochemistry 38 (32), 10371-10376 (1999)
   PUBMED   10441131
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Onda,M., Inui,S., Maeda,K., Suzuki,M., Takahashi,E. and
            Sakaguchi,N.
  TITLE     Expression and chromosomal localization of the human alpha 4/IGBP1
            gene, the structure of which is closely related to the yeast TAP42
            protein of the rapamycin-sensitive signal transduction pathway
  JOURNAL   Genomics 46 (3), 373-378 (1997)
   PUBMED   9441740
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158141.14 and AL139111.20.
            
            Summary: The proliferation and differentiation of B cells is
            dependent upon a B-cell antigen receptor (BCR) complex. Binding of
            antigens to specific B-cell receptors results in a tyrosine
            phosphorylation reaction through the BCR complex and leads to
            multiple signal transduction pathways. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.73498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..339
                     /product="immunoglobulin-binding protein 1 isoform 1"
                     /note="protein phosphatase 2A, regulatory subunit alpha-4;
                     B cell signal transduction molecule alpha 4; bA351K23.1
                     (immunoglobulin binding protein 1 (CD79A)); protein
                     alpha-4; CD79a-binding protein 1; immunoglobulin (CD79A)
                     binding protein 1; renal carcinoma antigen NY-REN-16;
                     protein phosphatase 2/4/6 regulatory subunit"
                     /calculated_mol_wt=39091
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          12..329
                     /region_name="TAP42"
                     /note="TAP42-like family; pfam04177"
                     /db_xref="CDD:461209"
     Region          98..202
                     /region_name="Interaction with PPP2CA"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          221..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          225..290
                     /region_name="Interaction with MID1.
                     /evidence=ECO:0000269|PubMed:11806752"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Site            255..256
                     /site_type="cleavage"
                     /note="Cleavage, by calpain; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          289..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     CDS             1..339
                     /gene="IGBP1"
                     /gene_synonym="ALPHA-4; alpha4; IBP1; MRXS28"
                     /coded_by="NM_001370192.1:145..1164"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14396.1"
                     /db_xref="GeneID:3476"
                     /db_xref="HGNC:HGNC:5461"
                     /db_xref="MIM:300139"
ORIGIN      
        1 maaedelqlp rlpelfetgr qlldevevat epagsrivqe kvfkgldlle kaaemlsqld
       61 lfsrnedlee iastdlkyll vpafqgaltm kqvnpskrld hlqrarehfi nyltqchcyh
      121 vaefelpktm nnsaenhtan ssmaypslva masqrqakiq rykqkkeleh rlsamksave
      181 sgqaddervr eyyllhlqrw idisleeies idqeikilre rdssreasts nssrqerppv
      241 kpfiltrnma qakvfgagyp slptmtvsdw yeqhrkygal pdqgiakaap eefrkaaqqq
      301 eeqeekeeed deqtlhrare wddwkdthpr gygnrqnmg
//
LOCUS       NP_001177170             640 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 80 homolog isoform b [Homo
            sapiens].
ACCESSION   NP_001177170
VERSION     NP_001177170.1
DBSOURCE    REFSEQ: accession NM_001190241.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Bizaoui,V., Huber,C., Kohaut,E., Roume,J., Bonniere,M.,
            Attie-Bitach,T. and Cormier-Daire,V.
  TITLE     Mutations in IFT80 cause SRPS Type IV. Report of two families and
            review
  JOURNAL   Am J Med Genet A 179 (4), 639-644 (2019)
   PUBMED   30767363
  REMARK    GeneRIF: Mutations in IFT80 cause Short rib-polydactyly syndrome,
            Beemer type.
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Wang,R., Deng,X., Yuan,C., Xin,H., Liu,G., Zhu,Y., Jiang,X. and
            Wang,C.
  TITLE     IFT80 Improves Invasion Ability in Gastric Cancer Cell Line via
            ift80/p75NGFR/MMP9 Signaling
  JOURNAL   Int J Mol Sci 19 (11), 3616 (2018)
   PUBMED   30453504
  REMARK    GeneRIF: IFT80 plays an important role in invasion of gastric
            cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Huang,W., Kane,J.K. and Li,M.D.
  TITLE     Identification and characterization of a long isoform of human
            IFT80, IFT80-L
  JOURNAL   Biochem Biophys Res Commun 373 (4), 653-658 (2008)
   PUBMED   18601909
  REMARK    GeneRIF: Identification and characterization of a human IFT80 long
            isoform (namely IFT80-L), the carboxyl terminus of which shares the
            protein sequence of IFT80, is reported.
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Beales,P.L., Bland,E., Tobin,J.L., Bacchelli,C., Tuysuz,B.,
            Hill,J., Rix,S., Pearson,C.G., Kai,M., Hartley,J., Johnson,C.,
            Irving,M., Elcioglu,N., Winey,M., Tada,M. and Scambler,P.J.
  TITLE     IFT80, which encodes a conserved intraflagellar transport protein,
            is mutated in Jeune asphyxiating thoracic dystrophy
  JOURNAL   Nat Genet 39 (6), 727-729 (2007)
   PUBMED   17468754
  REMARK    GeneRIF: Mutations in IFT80 is associated with Jeune asphyxiating
            thoracic dystrophy
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
REFERENCE   9  (residues 1 to 640)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 640)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125342.1, BC030774.1,
            AB037795.1 and CA421514.1.
            
            Summary: The protein encoded by this gene is part of the
            intraflagellar transport complex B and is necessary for the
            function of motile and sensory cilia. Defects in this gene are a
            cause of asphyxiating thoracic dystrophy 2 (ATD2). Three transcript
            variants encoding two different isoforms have been found for this
            gene.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.97172.1,
                                           SRR1803615.136519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..640
                     /product="intraflagellar transport protein 80 homolog
                     isoform b"
                     /note="WD repeat domain 56; WD repeat-containing protein
                     56; intraflagellar transport 80 homolog"
                     /calculated_mol_wt=72518
     Region          <2..156
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          13..49
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          46..395
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(50,68,72,78..79,90..91,109,123..124,148,153,
                     166..167,196,221,226,232..233,245..246,268,290,306..307,
                     321..322,339,345..346,360..361,389,395)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          55..90
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          95..128
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..640
                     /gene="IFT80"
                     /gene_synonym="ATD2; CFAP167; FAP167; SRTD2; WDR56"
                     /coded_by="NM_001190241.2:758..2680"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54668.1"
                     /db_xref="GeneID:57560"
                     /db_xref="HGNC:HGNC:29262"
                     /db_xref="MIM:611177"
ORIGIN      
        1 mlrstlaqqg tpvysvawgp dsekvlytag kqliikplqp nakvlqwkah dgiilkvdwn
       61 svndlilsag edckykvwds ygrplynsqp hehpitsvaw apdgelfavg sfhtlrlcdk
      121 tgwsyalekp ntgsifniaw sidgtqiaga cgnghvvfah vveqhwewkn fqvtltkrra
      181 mqvrnvlnda vdllefrdrv ikaslnyahl vvstslqcyv fstknwntpi ifdlkegtvs
      241 lilqaerhfl lvdgssiyly syegrfissp kfpgmrtdil naqtvslsnd tiairdkade
      301 kiiflfeast gkplgdgkfl shkneileia ldqkgltndr kiafidknrd lcitsvkrfg
      361 keeqiiklgt mvhtlawndt cnilcglqdt rfivwyypnt vyvdrdilpk tlyerdasef
      421 sknphivsfv gnqvtirrad gslvhisitp ypailheyvs sskwedavrl crfvkeqtmw
      481 aclaamavan rdmttaeiay aaigeidkvq yinsiknlps keskmahill fsgniqeaei
      541 vllqaglvyq aiqininlyn weralelavk ykthvdtvla yrqkfletfg kqetnkrylh
      601 yaeglqidwe kikakiemei tkereqssss qssksiglkp
//
LOCUS       NP_829884               1116 aa            linear   PRI 20-NOV-2025
DEFINITION  ELKS/Rab6-interacting/CAST family member 1 isoform epsilon [Homo
            sapiens].
ACCESSION   NP_829884
VERSION     NP_829884.1
DBSOURCE    REFSEQ: accession NM_178040.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Ribolla,L.M., Sala,K., Tonoli,D., Ramella,M., Bracaglia,L.,
            Bonomo,I., Gonnelli,L., Lamarca,A., Brindisi,M., Pierattelli,R.,
            Provenzani,A. and de Curtis,I.
  TITLE     Interfering with the ERC1-LL5beta interaction disrupts plasma
            membrane-Associated platforms and affects tumor cell motility
  JOURNAL   PLoS One 18 (7), e0287670 (2023)
   PUBMED   37437062
  REMARK    GeneRIF: Interfering with the ERC1-LL5beta interaction disrupts
            plasma membrane-Associated platforms and affects tumor cell
            motility.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Ko,J., Na,M., Kim,S., Lee,J.R. and Kim,E.
  TITLE     Interaction of the ERC family of RIM-binding proteins with the
            liprin-alpha family of multidomain proteins
  JOURNAL   J Biol Chem 278 (43), 42377-42385 (2003)
   PUBMED   12923177
  REMARK    GeneRIF: In vitro results indicate that ERC2/CAST, an active
            zone-specific isoform, interacts with all of the known isoforms of
            liprin-alpha and that liprin-alpha1 associates with both ERC2 and
            ERC1b
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 1116)
  AUTHORS   Nakata,T., Yokota,T., Emi,M. and Minami,S.
  TITLE     Differential expression of multiple isoforms of the ELKS mRNAs
            involved in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 35 (1), 30-37 (2002)
   PUBMED   12203787
  REMARK    GeneRIF: Analysis of the gene structure of four isoforms (ELKS
            beta, ELKS gamma, ELKS delta, and ELKS epsilon) in a case of
            papillary thyroid carcinoma reveal that the isoforms are produced
            by alternative splicing.
REFERENCE   8  (residues 1 to 1116)
  AUTHORS   Monier,S., Jollivet,F., Janoueix-Lerosey,I., Johannes,L. and
            Goud,B.
  TITLE     Characterization of novel Rab6-interacting proteins involved in
            endosome-to-TGN transport
  JOURNAL   Traffic 3 (4), 289-297 (2002)
   PUBMED   11929610
REFERENCE   9  (residues 1 to 1116)
  AUTHORS   Yokota,T., Nakata,T., Minami,S., Inazawa,J. and Emi,M.
  TITLE     Genomic organization and chromosomal mapping of ELKS, a gene
            rearranged in a papillary thyroid carcinoma
  JOURNAL   J Hum Genet 45 (1), 6-11 (2000)
   PUBMED   10697956
REFERENCE   10 (residues 1 to 1116)
  AUTHORS   Nakata,T., Kitamura,Y., Shimizu,K., Tanaka,S., Fujimori,M.,
            Yokoyama,S., Ito,K. and Emi,M.
  TITLE     Fusion of a novel gene, ELKS, to RET due to translocation
            t(10;12)(q11;p13) in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 25 (2), 97-103 (1999)
   PUBMED   10337992
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR000847.1, AC004803.11,
            AB053471.1, AC004672.1, AC004671.1 and BM984956.1.
            
            Summary: The protein encoded by this gene is a member of a family
            of RIM-binding proteins. RIMs are active zone proteins that
            regulate neurotransmitter release. This gene has been found fused
            to the receptor-type tyrosine kinase gene RET by gene rearrangement
            due to the translocation t(10;12)(q11;p13) in thyroid papillary
            carcinoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (epsilon) encodes the longest
            isoform (epsilon).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB053471.1, BC132784.1 [ECO:0000331]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360905.9/ ENSP00000354158.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..1116
                     /product="ELKS/Rab6-interacting/CAST family member 1
                     isoform epsilon"
                     /note="RAB6 interacting protein 2"
                     /calculated_mol_wt=127956
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          154..982
                     /region_name="Cast"
                     /note="RIM-binding protein of the cytomatrix active zone;
                     pfam10174"
                     /db_xref="CDD:431111"
     Region          590..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            719..720
                     /site_type="other"
                     /note="Breakpoint for translocation to form ERC1-RET
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          814..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811U3; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          1068..1108
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     CDS             1..1116
                     /gene="ERC1"
                     /gene_synonym="Cast2; ELKS; ERC-1; RAB6IP2"
                     /coded_by="NM_178040.4:257..3607"
                     /note="isoform epsilon is encoded by transcript variant
                     epsilon"
                     /db_xref="CCDS:CCDS8508.1"
                     /db_xref="GeneID:23085"
                     /db_xref="HGNC:HGNC:17072"
                     /db_xref="MIM:607127"
ORIGIN      
        1 mygsarsvgk vepssqspgr sprlprsprl ghrrtnstgg ssgssvgggs gktlsmeniq
       61 slnaayatsg pmylsdhenv gsetpkstmt lgrsggrlpy gvrmtamgss pniassgvas
      121 dtiafgehhl ppvsmastvp hslrqardnt imdlqtqlke vlrendllrk dvevkeskls
      181 ssmnsiktfw spelkkeral rkdeaskiti wkeqyrvvqe enqhmqmtiq alqdelriqr
      241 dlnqlfqqds ssrtgepcva elteenfqrl haeherqake lfllrktlee melrietqkq
      301 tlnardesik kllemlqskg lsakateedh ertrrlaeae mhvhhlesll eqkekensml
      361 reemhrrfen apdsaktkal qtviemkdsk issmerglrd leeeiqmlks ngalsteere
      421 eemkqmevyr shskfmknkv eqlkeelssk eaqweelkkk aaglqaeigq vkqelsrkdt
      481 ellalqtkle tltnqfsdsk qhievlkesl takeqraail qtevdalrlr leeketmlnk
      541 ktkqiqdmae ekgtqageih dlkdmldvke rkvnvlqkki enlqeqlrdk ekqmsslker
      601 vkslqadttn tdtalttlee alaekertie rlkeqrdrde rekqeeidny kkdlkdlkek
      661 vsllqgdlse keaslldlke hasslassgl kkdsrlktle ialeqkkeec lkmesqlkka
      721 heaalearas pemsdriqhl ereitrykde sskaqaevdr lleilkeven ekndkdkkia
      781 elerqvkdqn kkvanlkhke qvekkksaqm leearrredn lndssqqlqd slrkkddrie
      841 eleealresv qitaeremvl aqeesartna ekqveellma mekvkqeles mkaklsstqq
      901 slaekethlt nlraerrkhl eevlemkqea llaaisekda niallelsss kkktqeevaa
      961 lkrekdrlvq qlkqqtqnrm klmadnyedd hfksshsnqt nhkpspdqii qplleldqnr
     1021 sklklyighl ttlchdrdpl ilrgltppas ynldddqaaw enelqkmtrg qlqdelekge
     1081 rdnaelqefa nailqqiadh cpdileqvvn aleess
//
LOCUS       NP_001182073             993 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory ankyrin repeat
            subunit B isoform A [Homo sapiens].
ACCESSION   NP_001182073
VERSION     NP_001182073.1
DBSOURCE    REFSEQ: accession NM_001195144.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 993)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 993)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 993)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 993)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 993)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 993)
  AUTHORS   Kariuki,S.N., Ghodke-Puranik,Y., Dorschner,J.M., Chrabot,B.S.,
            Kelly,J.A., Tsao,B.P., Kimberly,R.P., Alarcon-Riquelme,M.E.,
            Jacob,C.O., Criswell,L.A., Sivils,K.L., Langefeld,C.D.,
            Harley,J.B., Skol,A.D. and Niewold,T.B.
  TITLE     Genetic analysis of the pathogenic molecular sub-phenotype
            interferon-alpha identifies multiple novel loci involved in
            systemic lupus erythematosus
  JOURNAL   Genes Immun 16 (1), 15-23 (2015)
   PUBMED   25338677
REFERENCE   7  (residues 1 to 993)
  AUTHORS   Kapoor,M., Wang,J.C., Wetherill,L., Le,N., Bertelsen,S.,
            Hinrichs,A.L., Budde,J., Agrawal,A., Almasy,L., Bucholz,K.,
            Dick,D.M., Harari,O., Xiaoling,X., Hesselbrock,V., Kramer,J.,
            Nurnberger,J.I. Jr., Rice,J., Schuckit,M., Tischfield,J.,
            Porjesz,B., Edenberg,H.J., Bierut,L., Foroud,T. and Goate,A.
  TITLE     Genome-wide survival analysis of age at onset of alcohol dependence
            in extended high-risk COGA families
  JOURNAL   Drug Alcohol Depend 142, 56-62 (2014)
   PUBMED   24962325
REFERENCE   8  (residues 1 to 993)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 993)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 993)
  AUTHORS   Dechamps,C., Bach,S., Portetelle,D. and Vandenbol,M.
  TITLE     The Tre2 oncoprotein, implicated in Ewing's sarcoma, interacts with
            two components of the cytoskeleton
  JOURNAL   Biotechnol Lett 28 (4), 223-231 (2006)
   PUBMED   16555005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010746.8, AC013264.4 and AC017035.6.
            
            Sequence Note: This RefSeq record was created from genomic sequence
            data to make the sequence consistent with the reference genome
            assembly. There are no full-length human transcripts representing
            this variant; the genomic coordinates used for the transcript
            record are predicted based on partial human transcript alignments
            and on full-length homologous transcript and protein alignments
            with mouse NP_001074902.2 and chicken NP_001012933.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.240231.1,
                                           SRR1660807.82774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282272.15/ ENSP00000282272.9
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..993
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..993
                     /product="serine/threonine-protein phosphatase 6
                     regulatory ankyrin repeat subunit B isoform A"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     ankyrin repeat subunit B; ankyrin repeat domain-containing
                     protein 44; serine/threonine-protein phosphatase 6
                     regulatory subunit ARS-B"
                     /calculated_mol_wt=107473
     Region          7..36
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          10..61
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Region          11..38
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..71
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..69
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          54..343
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          73..102
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          76..104
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(79..80,83..85,87..88,92,95,104,106,108,112..113,
                     116..118,120..121,125,128,137,139,141,145..146,149..151,
                     153..154,158,161,170)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          106..135
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          139..170
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          139..168
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          172..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          172..201
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          205..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..234
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..267
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          253..534
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..301
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          305..336
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          305..334
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          338..367
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          371..400
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          375..402
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(404,406,410..411,414..416,418..419,423,426,435,437,
                     439,443..444,447..449,451..452,456,459,468,470,472,
                     476..477,489..491,493..494,517,520,529)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          404..435
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          404..433
                     /region_name="ANK 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          437..468
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          437..466
                     /region_name="ANK 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          470..529
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          470..498
                     /region_name="ANK 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          492..749
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          531..562
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          531..561
                     /region_name="ANK 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          564..597
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          566..595
                     /region_name="ANK 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          599..628
                     /region_name="ANK 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          600..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(601,605..606,609..611,613..614,618,621,630,633,635,
                     639..640,643..645,647..648,652,655,667,669,671,675..676,
                     679..681,683..684,688,691,700)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          633..667
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..662
                     /region_name="ANK 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          650..975
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          669..700
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          669..698
                     /region_name="ANK 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          702..733
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          702..731
                     /region_name="ANK 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          735..764
                     /region_name="ANK 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          771..836
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          771..800
                     /region_name="ANK 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          803..832
                     /region_name="ANK 24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          838..867
                     /region_name="ANK 25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          839..869
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(840,844..845,848..850,852..853,857,860,869,871,873,
                     877..878,881..883,885..886,890,894,903,905,907,911..912,
                     915..917,919..920,924,927,936)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          871..903
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          871..901
                     /region_name="ANK 26"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          905..936
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          905..934
                     /region_name="ANK 27"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          941..972
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          941..970
                     /region_name="ANK 28"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     CDS             1..993
                     /gene="ANKRD44"
                     /gene_synonym="ARSB; PP6-ARS-B"
                     /coded_by="NM_001195144.2:177..3158"
                     /note="isoform A is encoded by transcript variant A"
                     /db_xref="CCDS:CCDS74619.1"
                     /db_xref="GeneID:91526"
                     /db_xref="HGNC:HGNC:25259"
                     /db_xref="MIM:620861"
ORIGIN      
        1 mavlkltdqp plvqaifsgd peeirmlihk tedvntldse krtplhvaaf lgdaeiiell
       61 ilsgarvnak dnmwltplhr avasrseeav qvlikhsadv nardknwqtp lhvaaankav
      121 kcaeviipll ssvnvsdrgg rtalhhaaln ghvemvnlll akganinafd kkdrralhwa
      181 aymghldvva llinhgaevt ckdkkgytpl haaasngqin vvkhllnlgv eideinvygn
      241 talhiacyng qdavvnelid yganvnqpnn ngftplhfaa asthgalcle llvnngadvn
      301 iqskdgkspl hmtavhgrft rsqtliqngg eidcvdkdgn tplhvaaryg hellintlit
      361 sgadtakcgi hsmfplhlaa lnahsdccrk llssgfeidt pdkfgrtclh aaaaggnvec
      421 ikllqssgad fhkkdkcgrt plhyaaanch fhcietlvtt ganvnetddw grtalhyaaa
      481 sdmdrnktil gnahdnseel erarelkeke atlclefllq ndanpsirdk egynsihyaa
      541 ayghrqclel llertnsgfe esdsgatksp lhlaaynghh qalevllqsl vdldirdekg
      601 rtaldlaafk ghtecveali nqgasifvkd nvtkrtplha svinghtlcl rllleiadnp
      661 eavdvkdakg qtplmlavay ghidavslll ekeanvdtvd ilgctalhrg imtgheecvq
      721 mlleqevsil ckdsrgrtpl hyaaarghat wlsellqmal seedccfkdn qgytplhwac
      781 yngnenciev lleqkcfrkf ignpftplhc aiindhgnca slllgaidss ivscrddkgr
      841 tplhaaafad hveclqlllr hsapvnavdn sgktalmmaa engqagavdi lvnsaqadlt
      901 vkdkdlntpl hlacskghek callildkiq deslineknn alqtplhvaa rnglkvvvee
      961 llakgacvla vdenasrsng prstpgtavq kee
//
LOCUS       NP_001340209             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340209
VERSION     NP_001340209.1
DBSOURCE    REFSEQ: accession NM_001353280.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.110449.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353280.1:557..1093"
                     /note="isoform 2 is encoded by transcript variant 42"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001243608             488 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial ribonuclease P catalytic subunit isoform 3 [Homo
            sapiens].
ACCESSION   NP_001243608
VERSION     NP_001243608.1
DBSOURCE    REFSEQ: accession NM_001256679.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Zhang,E., Sun,Q., Zhang,C., Ma,H., Zhang,J., Ding,Y., Wang,G.,
            Jin,C., Jin,C., Fu,Y., Yan,C., Zhu,M., Wang,C., Dai,J., Jin,G.,
            Hu,Z., Shen,H. and Ma,H.
  TITLE     Comprehensive functional interrogation of susceptibility loci in
            GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC
  JOURNAL   Cancer Lett 585, 216646 (2024)
   PUBMED   38262497
  REMARK    GeneRIF: Comprehensive functional interrogation of susceptibility
            loci in GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC.
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Smith,T.B., Rea,A., Thomas,H.B., Thompson,K., Olahova,M.,
            Maroofian,R., Zamani,M., He,L., Sadeghian,S., Galehdari,H.,
            Lotan,N.S., Gilboa,T., Herman,K.C., McCorvie,T.J., Yue,W.W.,
            Houlden,H., Taylor,R.W., Newman,W.G. and O'Keefe,R.T.
  TITLE     Novel homozygous variants in PRORP expand the genotypic spectrum of
            combined oxidative phosphorylation deficiency 54
  JOURNAL   Eur J Hum Genet 31 (10), 1190-1194 (2023)
   PUBMED   37558808
  REMARK    GeneRIF: Novel homozygous variants in PRORP expand the genotypic
            spectrum of combined oxidative phosphorylation deficiency 54.
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Hochberg,I., Demain,L.A.M., Richer,J., Thompson,K., Urquhart,J.E.,
            Rea,A., Pagarkar,W., Rodriguez-Palmero,A., Schluter,A., Verdura,E.,
            Pujol,A., Quijada-Fraile,P., Amberger,A., Deutschmann,A.J.,
            Demetz,S., Gillespie,M., Belyantseva,I.A., McMillan,H.J.,
            Barzik,M., Beaman,G.M., Motha,R., Ng,K.Y., O'Sullivan,J.,
            Williams,S.G., Bhaskar,S.S., Lawrence,I.R., Jenkinson,E.M.,
            Zambonin,J.L., Blumenfeld,Z., Yalonetsky,S., Oerum,S.,
            Rossmanith,W., Yue,W.W., Zschocke,J., Munro,K.J., Battersby,B.J.,
            Friedman,T.B., Taylor,R.W., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics England Research Consortium
  TITLE     Bi-allelic variants in the mitochondrial RNase P subunit PRORP
            cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations
  JOURNAL   Am J Hum Genet 108 (11), 2195-2204 (2021)
   PUBMED   34715011
  REMARK    GeneRIF: Bi-allelic variants in the mitochondrial RNase P subunit
            PRORP cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations.
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Bhatta,A., Dienemann,C., Cramer,P. and Hillen,H.S.
  TITLE     Structural basis of RNA processing by human mitochondrial RNase P
  JOURNAL   Nat Struct Mol Biol 28 (9), 713-723 (2021)
   PUBMED   34489609
  REMARK    GeneRIF: Structural basis of RNA processing by human mitochondrial
            RNase P.
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Alsmadi,O., Muiya,P., Khalak,H., Al-Saud,H., Meyer,B.F.,
            Al-Mohanna,F., Alshahid,M. and Dzimiri,N.
  TITLE     Haplotypes encompassing the KIAA0391 and PSMA6 gene cluster confer
            a genetic link for myocardial infarction and coronary artery
            disease
  JOURNAL   Ann Hum Genet 73 (Pt 5), 475-483 (2009)
   PUBMED   19624571
  REMARK    GeneRIF: Haplotypes in KIAA0391 and PSMA6 genes is a genetic link
            for myocardial infarction and coronary artery disease.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Holzmann,J., Frank,P., Loffler,E., Bennett,K.L., Gerner,C. and
            Rossmanith,W.
  TITLE     RNase P without RNA: identification and functional reconstitution
            of the human mitochondrial tRNA processing enzyme
  JOURNAL   Cell 135 (3), 462-474 (2008)
   PUBMED   18984158
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Li,T., Faridi,R., Newman,W.G. and Friedman,T.B.
  TITLE     Perrault Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25254289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK301931.1, BP373829.1, AI431599.1 and AL121594.6.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (3) has a shorter N-terminus, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301931.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155751, SAMEA2159931
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..488
                     /product="mitochondrial ribonuclease P catalytic subunit
                     isoform 3"
                     /EC_number="3.1.26.5"
                     /note="mitochondrial ribonuclease P protein 3;
                     mitochondrial RNase P protein 3; mitochondrial RNase P
                     subunit 3; proteinaceous RNase P; mitochondrial
                     ribonuclease P catalytic subunit"
                     /calculated_mol_wt=56356
     Region          79..109
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          115..144
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          149..176
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          247..483
                     /region_name="PRORP"
                     /note="Protein-only RNase P; pfam16953"
                     /db_xref="CDD:465320"
     CDS             1..488
                     /gene="PRORP"
                     /gene_synonym="COXPD54; KIAA0391; MRPP3"
                     /coded_by="NM_001256679.2:111..1577"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58313.1"
                     /db_xref="GeneID:9692"
                     /db_xref="HGNC:HGNC:19958"
                     /db_xref="MIM:609947"
ORIGIN      
        1 mnsqtedhal apvrntiqlp tqplnseewd klkedlkent gktsfeswii sqmagchssi
       61 dvaksllawv aaknngivsy dllvkylylc vfhmqtsevi dvfeimkary ktleprgysl
      121 lirglihsdr wrealllled ikkvitpskk nyndciqgal lhqdvntawn lyqellghdi
      181 vpmletlkaf fdfgkdikdd nysnklldil sylrnnqlyp gesfahsikt wfesvpgkqw
      241 kgqfttvrks gqcsgcgkti esiqlspeey eclkgkimrd vidggdqyrk ttpqelkrfe
      301 nfiksrppfd vvidglnvak mfpkvresql llnvvsqlak rnlrllvlgr khmlrrssqw
      361 srdemeevqk qascffaddi seddpfllya tlhsgnhcrf itrdlmrdhk aclpdaktqr
      421 lffkwqqghq laivnrfpgs kltfqrilsy dtvvqttgds whipydedlv ercscevptk
      481 wlclhqkt
//
LOCUS       NP_079222                254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_079222 NP_001341022
VERSION     NP_079222.1
DBSOURCE    REFSEQ: accession NM_024946.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB101263.1, BC020536.1, AC009090.12 and CA308353.1.
            
            On Mar 23, 2018 this sequence version replaced NP_001341022.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.203948.1,
                                           SRR1803615.69265.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309137.13/ ENSP00000335808.6
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_024946.4:235..999"
                     /note="isoform a is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_683515               1235 aa            linear   PRI 20-NOV-2025
DEFINITION  structural maintenance of chromosomes protein 1B isoform 1 [Homo
            sapiens].
ACCESSION   NP_683515
VERSION     NP_683515.4
DBSOURCE    REFSEQ: accession NM_148674.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Shi,Z., Gao,H., Bai,X.C. and Yu,H.
  TITLE     Cryo-EM structure of the human cohesin-NIPBL-DNA complex
  JOURNAL   Science 368 (6498), 1454-1459 (2020)
   PUBMED   32409525
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Rosario,R., Smith,R.W., Adams,I.R. and Anderson,R.A.
  TITLE     RNA immunoprecipitation identifies novel targets of DAZL in human
            foetal ovary
  JOURNAL   Mol Hum Reprod 23 (3), 177-186 (2017)
   PUBMED   28364521
  REMARK    GeneRIF: Through the translational regulation of novel RNA targets
            SMC1B and TEX11, DAZL may have a key role in regulating chromosome
            cohesion and DNA recombination; two processes fundamental in
            determining oocyte quality and whose establishment in foetal life
            may support lifelong fertility.
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Mannini,L., Cucco,F., Quarantotti,V., Amato,C., Tinti,M., Tana,L.,
            Frattini,A., Delia,D., Krantz,I.D., Jessberger,R. and Musio,A.
  TITLE     SMC1B is present in mammalian somatic cells and interacts with
            mitotic cohesin proteins
  JOURNAL   Sci Rep 5, 18472 (2015)
   PUBMED   26673124
  REMARK    GeneRIF: Data show that structural maintenance of chromosomes
            protein 1B (SMC1B) is expressed in primary fibroblasts.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Ansari,D., Andersson,R., Bauden,M.P., Andersson,B., Connolly,J.B.,
            Welinder,C., Sasor,A. and Marko-Varga,G.
  TITLE     Protein deep sequencing applied to biobank samples from patients
            with pancreatic cancer
  JOURNAL   J Cancer Res Clin Oncol 141 (2), 369-380 (2015)
   PUBMED   25216700
  REMARK    GeneRIF: High SMC1B expression is associated with pancreatic
            cancer.
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Lee,J. and Hirano,T.
  TITLE     RAD21L, a novel cohesin subunit implicated in linking homologous
            chromosomes in mammalian meiosis
  JOURNAL   J Cell Biol 192 (2), 263-276 (2011)
   PUBMED   21242291
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Cobbe,N. and Heck,M.M.
  TITLE     The evolution of SMC proteins: phylogenetic analysis and structural
            implications
  JOURNAL   Mol Biol Evol 21 (2), 332-347 (2004)
   PUBMED   14660695
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Revenkova,E., Eijpe,M., Heyting,C., Gross,B. and Jessberger,R.
  TITLE     Novel meiosis-specific isoform of mammalian SMC1
  JOURNAL   Mol Cell Biol 21 (20), 6984-6998 (2001)
   PUBMED   11564881
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126208.1, AK125736.1, AJ504806.2 and BG194018.1.
            
            On Apr 18, 2014 this sequence version replaced NP_683515.3.
            
            Summary: SMC1L2 belongs to a family of proteins required for
            chromatid cohesion and DNA recombination during meiosis and mitosis
            (3:Revenkova et al., 2001 [PubMed 11564881]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000357450.9/ ENSP00000350036.4
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..1235
                     /product="structural maintenance of chromosomes protein 1B
                     isoform 1"
                     /note="mitosis-specific chromosome segregation protein
                     like protein beta; SMC1 (structural maintenance of
                     chromosomes 1, yeast)-like 1; structural maintenance of
                     chromosomes protein 1B; SMC protein 1B; SMC1 structural
                     maintenance of chromosomes 1-like 2"
                     /calculated_mol_wt=143658
     Region          3..1206
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            648
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14683; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     Site            713
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q14683; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     Site            1033
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CU62; propagated from
                     UniProtKB/Swiss-Prot (Q8NDV3.3)"
     CDS             1..1235
                     /gene="SMC1B"
                     /gene_synonym="SMC1BETA; SMC1L2"
                     /coded_by="NM_148674.5:33..3740"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43027.1"
                     /db_xref="GeneID:27127"
                     /db_xref="HGNC:HGNC:11112"
                     /db_xref="MIM:608685"
ORIGIN      
        1 mahlelllve nfkswrgrqv igpfrrftci igpngsgksn vmdalsfvmg ekianlrvkn
       61 iqelihgahi gkpisssasv kiiyveesge ektfariirg gcsefrfndn lvsrsvyiae
      121 lekigiivka qnclvfqgtv esisvkkpke rtqffeeist sgeligeyee kkrklqkaee
      181 daqfnfnkkk niaaerrqak lekeeaeryq slleelkmnk iqlqlfqlyh nekkihllnt
      241 klehvnrdls vkreslshhe nivkarkkeh gmltrqlqqt ekelksvetl lnqkrpqyik
      301 akentshhlk kldvakksik dsekqcskqe ddikaletel adldaawrsf ekqieeeilh
      361 kkrdieleas qldrykelke qvrkkvatmt qqleklqweq ktdeerlafe krrhgevqgn
      421 lkqikeqied hkkrieklee ytktcmdclk ekkqqeetlv deiektksrm sevneelnli
      481 rselqnagid thegkrqqkr aevlehlkrl ypdsvfgrlf dlchpihkky qlavtkvfgr
      541 fitaivvase kvakdcirfl keeraepetf laldyldikp inerlrelkg ckmvidvikt
      601 qfpqlkkviq fvcgnglvce tmeearhial sgperqktva ldgtlflksg visggssdlk
      661 ykarcwdeke lknlrdrrsq kiqelkglmk tlrketdlkq iqtliqgtqt rlkysqnele
      721 mikkkhlvaf yqeqsqlqse llniesqcim lsegikerqr rikefqekid kveddifqhf
      781 ceeigvenir efenkhvkrq qeidqkrlef ekqktrlnvq leysrshlkk klnkintlke
      841 tiqkgsedid hlkkaeencl qtvnelmakq qqlkdirvtq nssaekvqtq ieeerkkfla
      901 vdrevgklqk evvsiqtsle qkrlekhnll ldckvqdiei illsgslddi ievemgteae
      961 stqatidiye keeafeidys slkedlkalq sdqeieahlr lllqqvasqe dillktaapn
     1021 lralenlktv rdkfqestda feasrkearl crqefeqvkk rrydlftqcf ehvsisidqi
     1081 ykklcrnnsa qaflspenpe epylegisyn cvapgkrfmp mdnlsggekc vaalallfav
     1141 hsfrpapffv ldevdaaldn tnigkvssyi keqtqdqfqm ivislkeefy sradaligiy
     1201 peyddcmfsr vltldlsqyp dtegqesskr hgesr
//
LOCUS       NP_060786                615 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 26 isoform 2 [Homo sapiens].
ACCESSION   NP_060786
VERSION     NP_060786.1
DBSOURCE    REFSEQ: accession NM_018316.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Samudrala,S.S.K., North,L.M., Stamm,K.D., Earing,M.G.,
            Frommelt,M.A., Willes,R., Tripathi,S., Dsouza,N.R.,
            Zimmermann,M.T., Mahnke,D.K., Liang,H.L., Lund,M., Lin,C.W.,
            Geddes,G.C., Mitchell,M.E. and Tomita-Mitchell,A.
  TITLE     Novel KLHL26 variant associated with a familial case of Ebstein's
            anomaly and left ventricular noncompaction
  JOURNAL   Mol Genet Genomic Med 8 (4), e1152 (2020)
   PUBMED   31985165
  REMARK    GeneRIF: Novel KLHL26 variant associated with a familial case of
            Ebstein's anomaly and left ventricular noncompaction.
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Shi,M., Murray,J.C., Marazita,M.L., Munger,R.G., Ruczinski,I.,
            Hetmanski,J.B., Wu,T., Murray,T., Redett,R.J., Wilcox,A.J.,
            Lie,R.T., Jabs,E.W., Wu-Chou,Y.H., Chen,P.K., Wang,H., Ye,X.,
            Yeow,V., Chong,S.S., Shi,B., Christensen,K., Scott,A.F., Patel,P.,
            Cheah,F. and Beaty,T.H.
  TITLE     Genome wide study of maternal and parent-of-origin effects on the
            etiology of orofacial clefts
  JOURNAL   Am J Med Genet A 158A (4), 784-794 (2012)
   PUBMED   22419666
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA453727.1, AK001940.1, AC004476.1 and BC026319.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001940.1, SRR1660805.96974.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300976.9/ ENSP00000300976.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..615
                     /product="kelch-like protein 26 isoform 2"
                     /note="kelch-like protein 26; kelch-like 26"
                     /calculated_mol_wt=68009
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          45..165
                     /region_name="BTB_POZ_KLHL26"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 26 (KLHL26); cd18255"
                     /db_xref="CDD:349564"
     Region          160..256
                     /region_name="BACK_KLHL26"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 26 (KLHL26); cd18465"
                     /db_xref="CDD:350540"
     Region          310..361
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          340..589
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          352..399
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          362..413
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          403..447
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          414..460
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          450..496
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          461..508
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          498..545
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          510..559
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     Region          549..590
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          561..608
                     /region_name="Kelch 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53HC5.2)"
     CDS             1..615
                     /gene="KLHL26"
                     /coded_by="NM_018316.3:28..1875"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12384.1"
                     /db_xref="GeneID:55295"
                     /db_xref="HGNC:HGNC:25623"
ORIGIN      
        1 maesggssgg aggggafgag pgperpnsta dkngalkctf sapshstsll qglatlraqg
       61 qlldvvltin reafpahkvv laacsdyfra mftggmreas qdvielkgvs arglrhiidf
      121 aysaevtldl dcvqdvlgaa vflqmlpvve lceeflkaam svetclnigq mattfslasl
      181 resvdaftfr hflqiaeeed flrlplerlv fflqsnrlqs caeidlfraa vrwlqhdpar
      241 rprashvlch irfplmqsse lvdsvqtldi mvedvlcrqy lleafnyqvl pfrqhemqsp
      301 rtavrsdvps lvtfggtpyt dsdrsvsskv yqlpepgarh freltemevg cshtcvavld
      361 nfvyvaggqh lqyrsgegav dacyrydphl nrwlrlqamq esriqfqlnv lcgmvyatgg
      421 rnragslasv erycprrnew gyacslkrrt wghagaasgg rlyisggygi svedkkalhc
      481 ydpvadqwef kapmseprvl hamvgaggri yalggrmdhv drcfdvlave yyvpetdqwt
      541 svspmragqs eagccllerk iyivggynwr lnnvtgivqv yntdtdewer dlhfpesfag
      601 iacapvllpr agtrr
//
LOCUS       NP_002493                899 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit isoform b [Homo sapiens].
ACCESSION   NP_002493
VERSION     NP_002493.3
DBSOURCE    REFSEQ: accession NM_002502.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 899)
  AUTHORS   De Paolis,V., Troisi,V., Bordin,A., Pagano,F., Caputo,V. and
            Parisi,C.
  TITLE     Unconventional p65/p52 NF-kappaB module regulates key tumor
            microenvironment-related genes in breast tumor-associated
            macrophages (TAMs)
  JOURNAL   Life Sci 357, 123059 (2024)
   PUBMED   39278618
  REMARK    GeneRIF: Unconventional p65/p52 NF-kappaB module regulates key
            tumor microenvironment-related genes in breast tumor-associated
            macrophages (TAMs).
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Vallabhapurapu,S. and Karin,M.
  TITLE     Regulation and function of NF-kappaB transcription factors in the
            immune system
  JOURNAL   Annu Rev Immunol 27, 693-733 (2009)
   PUBMED   19302050
  REMARK    Review article
REFERENCE   4  (residues 1 to 899)
  AUTHORS   Heusch,M., Lin,L., Geleziunas,R. and Greene,W.C.
  TITLE     The generation of nfkb2 p52: mechanism and efficiency
  JOURNAL   Oncogene 18 (46), 6201-6208 (1999)
   PUBMED   10597218
REFERENCE   5  (residues 1 to 899)
  AUTHORS   Lombardi,L., Ciana,P., Cappellini,C., Trecca,D., Guerrini,L.,
            Migliazza,A., Maiolo,A.T. and Neri,A.
  TITLE     Structural and functional characterization of the promoter regions
            of the NFKB2 gene
  JOURNAL   Nucleic Acids Res 23 (12), 2328-2336 (1995)
   PUBMED   7541912
REFERENCE   6  (residues 1 to 899)
  AUTHORS   Liptay,S., Schmid,R.M., Nabel,E.G. and Nabel,G.J.
  TITLE     Transcriptional regulation of NF-kappa B2: evidence for kappa
            B-mediated positive and negative autoregulation
  JOURNAL   Mol Cell Biol 14 (12), 7695-7703 (1994)
   PUBMED   7969113
REFERENCE   7  (residues 1 to 899)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
REFERENCE   8  (residues 1 to 899)
  AUTHORS   Bours,V., Burd,P.R., Brown,K., Villalobos,J., Park,S., Ryseck,R.P.,
            Bravo,R., Kelly,K. and Siebenlist,U.
  TITLE     A novel mitogen-inducible gene product related to p50/p105-NF-kappa
            B participates in transactivation through a kappa B site
  JOURNAL   Mol Cell Biol 12 (2), 685-695 (1992)
   PUBMED   1531086
REFERENCE   9  (residues 1 to 899)
  AUTHORS   Schreck,R., Albermann,K. and Baeuerle,P.A.
  TITLE     Nuclear factor kappa B: an oxidative stress-responsive
            transcription factor of eukaryotic cells (a review)
  JOURNAL   Free Radic Res Commun 17 (4), 221-237 (1992)
   PUBMED   1473734
  REMARK    Review article
REFERENCE   10 (residues 1 to 899)
  AUTHORS   Schmid,R.M., Perkins,N.D., Duckett,C.S., Andrews,P.C. and
            Nabel,G.J.
  TITLE     Cloning of an NF-kappa B subunit which stimulates HIV transcription
            in synergy with p65
  JOURNAL   Nature 352 (6337), 733-736 (1991)
   PUBMED   1876189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121928.13.
            
            On Nov 2, 2006 this sequence version replaced NP_002493.2.
            
            Summary: This gene encodes a subunit of the transcription factor
            complex nuclear factor-kappa-B (NFkB). The NFkB complex is
            expressed in numerous cell types and functions as a central
            activator of genes involved in inflammation and immune function.
            The protein encoded by this gene can function as both a
            transcriptional activator or repressor depending on its
            dimerization partner. The p100 full-length protein is
            co-translationally processed into a p52 active form. Chromosomal
            rearrangements and translocations of this locus have been observed
            in B cell lymphomas, some of which may result in the formation of
            fusion proteins. There is a pseudogene for this gene on chromosome
            18. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 3' coding region, compared
            to variant 1. The encoded isoform (b) is shorter than isoform a.
            Variants 2, 3, and 4 encode the same isoform (b).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.39059.1, X61498.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..899
                     /product="nuclear factor NF-kappa-B p100 subunit isoform
                     b"
                     /note="nuclear factor NF-kappa-B p100 subunit; oncogene
                     Lyt-10; DNA-binding factor KBF2; lymphocyte translocation
                     chromosome 10 protein; transcription factor NFKB2; NFKB,
                     p52/p100 subunit; nuclear factor Kappa-B, subunit 2;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells 2 (p49/p100); nuclear factor of Kappa light chain
                     gene enhancer in B cells 2; nuclear factor NF-kappa-B p52
                     subunit"
                     /calculated_mol_wt=96547
     mat_peptide     1..454
                     /product="Nuclear factor NF-kappa-B p52 subunit.
                     /id=PRO_0000030322"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
                     /calculated_mol_wt=49423
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          337..341
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          346..377
                     /region_name="GRR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          438..706
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed);
                     propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            order(487,489,493..494,497..499,501..502,506,509,524,526,
                     528,532..533,536..538,540..541,545,548,557,559,561,
                     565..566,571..573,575..576,580,583)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          487..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          487..519
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            490..491
                     /site_type="other"
                     /note="Breakpoint for translocation to form NFKB2-IGHA1
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          526..557
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..555
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..591
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..586
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(599,601,605..606,609..611,613..614,618,621,630,633,
                     635,639..640,643..645,647..648,652,655,665,667,669,
                     673..674,677..679,681..682,686,689,698)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          599..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          599..628
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          633..665
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..663
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          667..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          667..696
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          698..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          729..758
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          774..849
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     CDS             1..899
                     /gene="NFKB2"
                     /gene_synonym="CVID10; H2TF1; LYT-10; LYT10; NF-kB2; p100;
                     p49/p100; p52"
                     /coded_by="NM_002502.6:165..2864"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41565.1"
                     /db_xref="GeneID:4791"
                     /db_xref="HGNC:HGNC:7795"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggaaggygga ggggslgffp sslayspyqs gagpmgcypg ggggaqmaat vpsrdsgeea
      421 aepsapsrtp qcepqapeml qrareynarl fglaqrsara lldygvtada rallagqrhl
      481 ltaqdengdt plhlaiihgq tsvieqivyv ihhaqdlgvv nltnhlhqtp lhlavitgqt
      541 svvsfllrvg adpalldrhg dsamhlalra gagapellra llqsgapavp qllhmpdfeg
      601 lypvhlavra rspecldllv dsgaeveate rqggrtalhl atemeelglv thlvtklran
      661 vnartfagnt plhlaaglgy ptltrlllka gadihaenee plcplpsppt sdsdsdsegp
      721 ekdtrssfrg htpldltcst kvktlllnaa qntmeppltp pspagpglsl gdtalqnleq
      781 lldgpeaqgs waelaerlgl rslvdtyrqt tspsgsllrs yelaggdlag llealsdmgl
      841 eegvrllrgp etrdklpste vkedsaygsq sveqeaeklg pppeppgglc hghpqpqvh
//
LOCUS       NP_001182029             142 aa            linear   PRI 20-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001182029 XP_005271288
VERSION     NP_001182029.1
DBSOURCE    REFSEQ: accession NM_001195100.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Hardy,S., Zolotarov,Y., Coleman,J., Roitman,S., Khursheed,H.,
            Aubry,I., Uetani,N. and Tremblay,M.L.
  TITLE     PRL-1/2 phosphatases control TRPM7 magnesium-dependent function to
            regulate cellular bioenergetics
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2221083120 (2023)
   PUBMED   36972446
  REMARK    GeneRIF: This study established the existence of a magnesium
            transporter protein complex (PTP4A2/CNNM3/TRPM7) governing the
            cellular uptake of this divalent cation. Moreover, PTP4A2 acts as a
            magnesium biosensor, controlling the activity of this complex to
            reprogram cellular metabolism.
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Li,Q., Bai,Y., Lyle,L.T., Yu,G., Amarasinghe,O., Nguele Meke,F.,
            Carlock,C. and Zhang,Z.Y.
  TITLE     Mechanism of PRL2 phosphatase-mediated PTEN degradation and
            tumorigenesis
  JOURNAL   Proc Natl Acad Sci U S A 117 (34), 20538-20548 (2020)
   PUBMED   32788364
  REMARK    GeneRIF: Mechanism of PRL2 phosphatase-mediated PTEN degradation
            and tumorigenesis.
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Cai,F., Huang,Y., Wang,M., Sun,M., Zhao,Y. and Hattori,M.
  TITLE     A FRET-based screening method to detect potential inhibitors of the
            binding of CNNM3 to PRL2
  JOURNAL   Sci Rep 10 (1), 12879 (2020)
   PUBMED   32733084
  REMARK    GeneRIF: A FRET-based screening method to detect potential
            inhibitors of the binding of CNNM3 to PRL2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Si,X., Zeng,Q., Ng,C.H., Hong,W. and Pallen,C.J.
  TITLE     Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase,
            with the beta-subunit of geranylgeranyltransferase II
  JOURNAL   J Biol Chem 276 (35), 32875-32882 (2001)
   PUBMED   11447212
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Zeng,Q., Hong,W. and Tan,Y.H.
  TITLE     Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
            phosphatases homologous to PRL-1
  JOURNAL   Biochem Biophys Res Commun 244 (2), 421-427 (1998)
   PUBMED   9514946
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Zhao,Z., Lee,C.C., Monckton,D.G., Yazdani,A., Coolbaugh,M.I.,
            Li,X., Bailey,J., Shen,Y. and Caskey,C.T.
  TITLE     Characterization and genomic mapping of genes and pseudogenes of a
            new human protein tyrosine phosphatase
  JOURNAL   Genomics 35 (1), 172-181 (1996)
   PUBMED   8661118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136115.21, BC018662.1 and
            BC070181.1.
            
            On Apr 22, 2019 this sequence version replaced XP_005271288.1.
            
            Summary: The protein encoded by this gene belongs to a small class
            of the protein tyrosine phosphatase (PTP) family. PTPs are cell
            signaling molecules that play regulatory roles in a variety of
            cellular processes. PTPs in this class contain a protein tyrosine
            phosphatase catalytic domain and a characteristic C-terminal
            prenylation motif. This PTP has been shown to primarily associate
            with plasmic and endosomal membrane through its C-terminal
            prenylation. This PTP was found to interact with the beta-subunit
            of Rab geranylgeranyltransferase II (beta GGT II), and thus may
            function as a regulator of GGT II activity. Overexpression of this
            gene in mammalian cells conferred a transformed phenotype, which
            suggested its role in tumorigenesis. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 11, 12 and 17. [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. This results
            in a shorter protein (isoform 3), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279870.2648.1,
                                           SRR1163658.195822.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..142
                     /product="protein tyrosine phosphatase type IVA 2 isoform
                     3"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase IVA; phosphatase of
                     regenerating liver 2; protein tyrosine phosphatase IVA2;
                     protein tyrosine phosphatase type IVA 2; PTP(CAAXII);
                     protein-tyrosine phosphatase of regenerating liver 2;
                     protein tyrosine phosphatase type IVA, member 2"
                     /calculated_mol_wt=16236
     Region          1..130
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..142
                     /gene="PTP4A2"
                     /gene_synonym="HH13; HH7-2; HU-PP-1; OV-1; PRL-2; PRL2;
                     ptp-IV1a; ptp-IV1b; PTP4A; PTPCAAX2"
                     /coded_by="NM_001195100.2:976..1404"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS59193.1"
                     /db_xref="GeneID:8073"
                     /db_xref="HGNC:HGNC:9635"
                     /db_xref="MIM:601584"
ORIGIN      
        1 mnrpapveis yenmrflith nptnatlnkf teelkkygvt tlvrvcdaty dkapvekegi
       61 hvldwpfddg apppnqivdd wlnllktkfr eepgccvavh cvaglgrkrr gafnskqlly
      121 lekyrpkmrl rfrdtnghcc vq
//
LOCUS       NP_006237                467 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            epsilon isoform isoform a [Homo sapiens].
ACCESSION   NP_006237
VERSION     NP_006237.1
DBSOURCE    REFSEQ: accession NM_006246.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Santos,A., Cristobal,I., Carames,C., Luque,M., Sanz-Alvarez,M.,
            Madoz-Gurpide,J., Rojo,F. and Garcia-Foncillas,J.
  TITLE     Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows High
            Functional Impact in Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 24 (9), 7779 (2023)
   PUBMED   37175484
  REMARK    GeneRIF: Deregulation of the miR-19b/PPP2R5E Signaling Axis Shows
            High Functional Impact in Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Virshup,D.M. and Shenolikar,S.
  TITLE     From promiscuity to precision: protein phosphatases get a makeover
  JOURNAL   Mol Cell 33 (5), 537-545 (2009)
   PUBMED   19285938
  REMARK    Review article
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Eichhorn,P.J., Creyghton,M.P. and Bernards,R.
  TITLE     Protein phosphatase 2A regulatory subunits and cancer
  JOURNAL   Biochim Biophys Acta 1795 (1), 1-15 (2009)
   PUBMED   18588945
  REMARK    Review article
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 467)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   8  (residues 1 to 467)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   10 (residues 1 to 467)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136038.5, CB989123.1,
            BC093766.1, L76703.1, AW134792.1, CK820060.1, AA782601.1 and
            AL118555.6.
            
            Summary: The protein encoded by this gene belongs to the
            phosphatase 2A regulatory subunit B family. Protein phosphatase 2A
            is one of the four major Ser/Thr phosphatases, and it is implicated
            in the negative control of cell growth and division. It consists of
            a common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes an epsilon isoform of the regulatory subunit B56 subfamily.
            Multiple transcript variants encoding several different isoforms
            have been found for this gene. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1 and 2
            both encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.4272.1, L76703.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337537.8/ ENSP00000337641.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..467
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit epsilon isoform isoform a"
                     /note="PP2A, B subunit, B' epsilon; PP2A, B subunit, B56
                     epsilon; PP2A, B subunit, PR61 epsilon; PP2A, B subunit,
                     R5 epsilon; serine/threonine protein phosphatase 2A, 56
                     kDa regulatory subunit, epsilon; protein phosphatase 2
                     regulatory subunit B', epsilon"
                     /calculated_mol_wt=54568
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16537.1)"
     Region          2..>67
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); cl27532"
                     /db_xref="CDD:474937"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16537.1)"
     Region          55..435
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..467
                     /gene="PPP2R5E"
                     /gene_synonym="B56E; B56epsilon"
                     /coded_by="NM_006246.5:607..2010"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9758.1"
                     /db_xref="GeneID:5529"
                     /db_xref="HGNC:HGNC:9313"
                     /db_xref="MIM:601647"
ORIGIN      
        1 mssapttpps vdkvdgfsrk svrkarqkrs qsssqfrsqg kpieltplpl lkdvpsseqp
       61 elflkklqqc cvifdfmdtl sdlkmkeykr stlnelvdyi tisrgclteq typevvrmvs
      121 cnifrtlpps dsnefdpeed eptleaswph lqlvyeffir flesqefqps iakkyidqkf
      181 vlqllelfds edprerdylk tvlhriygkf lglrafirkq inniflrfvy etehfngvae
      241 lleilgsiin gfalplkaeh kqflvkvlip lhtvrslslf haqlaycivq flekdpslte
      301 pvirglmkfw pktcsqkevm flgeleeild viepsqfvki qeplfkqiak cvssphfqva
      361 eralyywnne yimslieens nvilpimfss lyriskehwn paivalvynv lkafmemnst
      421 mfdeltatyk sdrqrekkke kereelwkkl edlelkrglr rdgiipt
//
LOCUS       NP_001354673             515 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform f precursor [Homo sapiens].
ACCESSION   NP_001354673
VERSION     NP_001354673.1
DBSOURCE    REFSEQ: accession NM_001367744.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (28), as well as variant 27,
            encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.32065.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..515
                     /product="rab5 GDP/GTP exchange factor isoform f
                     precursor"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=55489
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2955
     Region          182..244
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          294..394
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..515
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367744.1:143..1690"
                     /note="isoform f precursor is encoded by transcript
                     variant 28"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mwllrqpcla gfllqvlegr vpqsqaeads gglgaggagl allpwlecng aistycnlcf
       61 lgssdppasa sqvarttevc hhaqlqreee eafassqssq gaqsltfskf eekktnektr
      121 kvttvkkffs assrvgskke iqeakapsps inrqtsietd rvskefiefl ktfhktgqei
      181 ykqtklfleg mhykrdlsie eqsecaqdfy hnvaermqtr gkvppervek imdqiekyim
      241 trlykyvfcp ettddekkdl aiqkriralr wvtpqmlcvp vnedipevsd mvvkaitdii
      301 emdskrvprd klacitkcsk hifnaikitk nepasaddfl ptliyivlkg npprlqsniq
      361 yitrfcnpsr lmtgedgyyf tnlccavafi ekldaqslnl sqedfdryms gqtsprkqea
      421 eswspdaclg vkqmyknldl lsqlnerqer imneakklek dlidwtdgia revqdiveky
      481 pleikppnqp laaidsenve ndklppplqp qvyag
//
LOCUS       NP_001607                513 aa            linear   PRI 20-NOV-2025
DEFINITION  activin receptor type-2A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001607
VERSION     NP_001607.1
DBSOURCE    REFSEQ: accession NM_001616.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Fei,D., Wang,F., Wang,Y., Chen,J., Chen,S., Fan,L., Yang,L.,
            Ren,Q., Duangmano,S., Du,F., Liu,H., Zhou,J., Sheng,J., Zhao,Y.,
            Wu,X., Li,M., Xiao,Z., Zhang,Z. and Jiang,X.
  TITLE     Circular RNA ACVR2A promotes the progression of hepatocellular
            carcinoma through mir-511-5p targeting PI3K-Akt signaling pathway
  JOURNAL   Mol Cancer 23 (1), 159 (2024)
   PUBMED   39107843
  REMARK    GeneRIF: Circular RNA ACVR2A promotes the progression of
            hepatocellular carcinoma through mir-511-5p targeting PI3K-Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Zhang,H., Ruan,Q., Chen,C., Yu,H., Guan,S., Hu,D., Yang,C., Lin,R.
            and Zhuo,C.
  TITLE     Activin A/ACVR2A axis inhibits epithelial-to-mesenchymal transition
            in colon cancer by activating SMAD2
  JOURNAL   Mol Carcinog 62 (10), 1585-1598 (2023)
   PUBMED   37378449
  REMARK    GeneRIF: Activin A/ACVR2A axis inhibits epithelial-to-mesenchymal
            transition in colon cancer by activating SMAD2.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Sugii,H., Albougha,M.S., Adachi,O., Tomita,H., Tomokiyo,A.,
            Hamano,S., Hasegawa,D., Yoshida,S., Itoyama,T. and Maeda,H.
  TITLE     Activin A Promotes Osteoblastic Differentiation of Human
            Preosteoblasts through the ALK1-Smad1/5/9 Pathway
  JOURNAL   Int J Mol Sci 22 (24), 13491 (2021)
   PUBMED   34948289
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Yuza,K., Nagahashi,M., Ichikawa,H., Hanyu,T., Nakajima,M.,
            Shimada,Y., Ishikawa,T., Sakata,J., Takeuchi,S., Okuda,S.,
            Matsuda,Y., Abe,M., Sakimura,K., Takabe,K. and Wakai,T.
  TITLE     Activin a Receptor Type 2A Mutation Affects the Tumor Biology of
            Microsatellite Instability-High Gastric Cancer
  JOURNAL   J Gastrointest Surg 25 (9), 2231-2241 (2021)
   PUBMED   33420656
  REMARK    GeneRIF: Activin a Receptor Type 2A Mutation Affects the Tumor
            Biology of Microsatellite Instability-High Gastric Cancer.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Xu,J., McKeehan,K., Matsuzaki,K. and McKeehan,W.L.
  TITLE     Inhibin antagonizes inhibition of liver cell growth by activin by a
            dominant-negative mechanism
  JOURNAL   J Biol Chem 270 (11), 6308-6313 (1995)
   PUBMED   7890768
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Attisano,L., Carcamo,J., Ventura,F., Weis,F.M., Massague,J. and
            Wrana,J.L.
  TITLE     Identification of human activin and TGF beta type I receptors that
            form heteromeric kinase complexes with type II receptors
  JOURNAL   Cell 75 (4), 671-680 (1993)
   PUBMED   8242742
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Donaldson,C.J., Mathews,L.S. and Vale,W.W.
  TITLE     Molecular cloning and binding properties of the human type II
            activin receptor
  JOURNAL   Biochem Biophys Res Commun 184 (1), 310-316 (1992)
   PUBMED   1314589
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Matzuk,M.M. and Bradley,A.
  TITLE     Cloning of the human activin receptor cDNA reveals high
            evolutionary conservation
  JOURNAL   Biochim Biophys Acta 1130 (1), 105-108 (1992)
   PUBMED   1311955
  REMARK    Erratum:[Biochim Biophys Acta 1992 Jun 15;1131(2):243]
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Mathews,L.S. and Vale,W.W.
  TITLE     Expression cloning of an activin receptor, a predicted
            transmembrane serine kinase
  JOURNAL   Cell 65 (6), 973-982 (1991)
   PUBMED   1646080
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X62381.1, BC067417.1,
            DA531622.1, BG616903.1, AW162986.1, BM503220.1, W03601.1,
            DN918410.1, T07746.1 and BU676046.1.
            
            Summary: This gene encodes a receptor that mediates the functions
            of activins, which are members of the transforming growth
            factor-beta (TGF-beta) superfamily involved in diverse biological
            processes. The encoded protein is a transmembrane serine-threonine
            kinase receptor which mediates signaling by forming heterodimeric
            complexes with various combinations of type I and type II receptors
            and ligands in a cell-specific manner. The encoded type II receptor
            is primarily involved in ligand-binding and includes an
            extracellular ligand-binding domain, a transmembrane domain and a
            cytoplasmic serine-threonine kinase domain. This gene may be
            associated with susceptibility to preeclampsia, a pregnancy-related
            disease which can result in maternal and fetal morbidity and
            mortality. Alternative splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.268933.1,
                                           SRR1803616.12990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241416.12/ ENSP00000241416.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q22.3-q23.1"
     Protein         1..513
                     /product="activin receptor type-2A isoform 1 precursor"
                     /EC_number="2.7.11.30"
                     /note="activin receptor type-2A; activin A receptor, type
                     IIA"
                     /calculated_mol_wt=56022
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
                     /calculated_mol_wt=1844
     mat_peptide     20..513
                     /product="Activin receptor type-2A. /id=PRO_0000024398"
                     /note="propagated from UniProtKB/Swiss-Prot (P27037.1)"
                     /calculated_mol_wt=56022
     Region          25..119
                     /region_name="TFP_LU_ECD_ACVR2A"
                     /note="extracellular domain (ECD) found in activin
                     receptor type-2A (ACTR-IIA) and similar proteins; cd23631"
                     /db_xref="CDD:467151"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
     Site            136..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27037.1)"
     Region          196..485
                     /region_name="STKc_ACVR2a"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Activin Type IIA Receptor; cd14141"
                     /db_xref="CDD:271043"
     Site            order(198..202,206,217,219,247,267..270,274,276,322,324,
                     326..327,329,340,343,361..364)
                     /site_type="active"
                     /db_xref="CDD:271043"
     Site            order(198..204,206,217,219,267..268,270,274,326..327,329,
                     340)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271043"
     Site            order(202,274,276,322,324,326,343,361..364)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271043"
     Site            339..364
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271043"
     CDS             1..513
                     /gene="ACVR2A"
                     /gene_synonym="ACTRII; ACVR2"
                     /coded_by="NM_001616.5:125..1666"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS33301.1"
                     /db_xref="GeneID:92"
                     /db_xref="HGNC:HGNC:173"
                     /db_xref="MIM:102581"
ORIGIN      
        1 mgaaaklafa vfliscssga ilgrsetqec lffnanwekd rtnqtgvepc ygdkdkrrhc
       61 fatwknisgs ieivkqgcwl ddincydrtd cvekkdspev yfcccegnmc nekfsyfpem
      121 evtqptsnpv tpkppyynil lyslvplmli agivicafwv yrhhkmaypp vlvptqdpgp
      181 pppspllglk plqllevkar grfgcvwkaq llneyvavki fpiqdkqswq neyevyslpg
      241 mkhenilqfi gaekrgtsvd vdlwlitafh ekgslsdflk anvvswnelc hiaetmargl
      301 aylhedipgl kdghkpaish rdiksknvll knnltaciad fglalkfeag ksagdthgqv
      361 gtrrymapev legainfqrd aflridmyam glvlwelasr ctaadgpvde ymlpfeeeig
      421 qhpsledmqe vvvhkkkrpv lrdywqkhag mamlcetiee cwdhdaearl sagcvgerit
      481 qmqrltniit tedivtvvtm vtnvdfppke ssl
//
LOCUS       NP_001271227            1170 aa            linear   PRI 20-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
            isoform 3 [Homo sapiens].
ACCESSION   NP_001271227 XP_005254504
VERSION     NP_001271227.1
DBSOURCE    REFSEQ: accession NM_001284298.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1170)
  AUTHORS   Phoenix,K.N., Yue,Z., Yue,L., Cronin,C.G., Liang,B.T.,
            Hoeppner,L.H. and Claffey,K.P.
  TITLE     PLCbeta2 Promotes VEGF-Induced Vascular Permeability
  JOURNAL   Arterioscler Thromb Vasc Biol 42 (10), 1229-1241 (2022)
   PUBMED   35861069
  REMARK    GeneRIF: PLCbeta2 Promotes VEGF-Induced Vascular Permeability.
REFERENCE   2  (residues 1 to 1170)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1170)
  AUTHORS   Zhang,H., Xie,T., Shui,Y. and Qi,Y.
  TITLE     Knockdown of PLCB2 expression reduces melanoma cell viability and
            promotes melanoma cell apoptosis by altering Ras/Raf/MAPK signals
  JOURNAL   Mol Med Rep 21 (1), 420-428 (2020)
   PUBMED   31746389
  REMARK    GeneRIF: Knockdown of PLCB2 expression reduces melanoma cell
            viability and promotes melanoma cell apoptosis by altering
            Ras/Raf/MAPK signals.
REFERENCE   4  (residues 1 to 1170)
  AUTHORS   Bertagnolo,V., Grassilli,S., Volinia,S., Al-Qassab,Y., Brugnoli,F.,
            Vezzali,F., Lambertini,E., Palomba,M., Piubello,Q., Orvieto,E.,
            Natali,C., Piva,R., Croce,C.M. and Capitani,S.
  TITLE     Ectopic expression of PLC-beta2 in non-invasive breast tumor cells
            plays a protective role against malignant progression and is
            correlated with the deregulation of miR-146a
  JOURNAL   Mol Carcinog 58 (5), 708-721 (2019)
   PUBMED   30582225
  REMARK    GeneRIF: High PLCB2 expression is associated with breast cancer.
REFERENCE   5  (residues 1 to 1170)
  AUTHORS   Brugnoli,F., Grassilli,S., Lanuti,P., Marchisio,M., Al-Qassab,Y.,
            Vezzali,F., Capitani,S. and Bertagnolo,V.
  TITLE     Up-modulation of PLC-beta2 reduces the number and malignancy of
            triple-negative breast tumor cells with a CD133+/EpCAM+ phenotype:
            a promising target for preventing progression of TNBC
  JOURNAL   BMC Cancer 17 (1), 617 (2017)
   PUBMED   28870198
  REMARK    GeneRIF: this work adds substantial information about the role of
            PLC-beta2 in invasive breast tumors, demonstrating that its
            up-regulation in cells with a basal-B triple-negative phenotype is
            sufficient to down-modulate the expression of surface antigens
            crucial for malignancy and to reduce the number of cells with a
            stem-like phenotype.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1170)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   7  (residues 1 to 1170)
  AUTHORS   Buhl,A.M., Osawa,S. and Johnson,G.L.
  TITLE     Mitogen-activated protein kinase activation requires two signal
            inputs from the human anaphylatoxin C5a receptor
  JOURNAL   J Biol Chem 270 (34), 19828-19832 (1995)
   PUBMED   7649993
REFERENCE   8  (residues 1 to 1170)
  AUTHORS   Park,D., Jhon,D.Y., Kriz,R., Knopf,J. and Rhee,S.G.
  TITLE     Cloning, sequencing, expression, and Gq-independent activation of
            phospholipase C-beta 2
  JOURNAL   J Biol Chem 267 (23), 16048-16055 (1992)
   PUBMED   1644792
REFERENCE   9  (residues 1 to 1170)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1170)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA981116.1, BC136467.1 and
            AB209583.1.
            
            On Sep 27, 2013 this sequence version replaced XP_005254504.1.
            
            Summary: The protein encoded by this gene is a phosphodiesterase
            that catalyzes the hydrolysis of phosphatidylinositol
            4,5-bisphosphate to the second messengers inositol
            1,4,5-trisphosphate (IP3) and diacylglycerol. The encoded protein
            is activated by G proteins and has been shown to be involved in the
            type 2 taste receptor signal transduction pathway. In addition,
            nuclear factor kappa B can regulate the transcription of this gene,
            whose protein product is also an important regulator of platelet
            responses. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon, compared to variant 1. The encoded isoform (3) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136467.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..1170
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-2 isoform 3"
                     /EC_number="3.1.4.11"
                     /note="phosphoinositide phospholipase C-beta-2;
                     1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
                     beta-2"
                     /calculated_mol_wt=132380
     Region          12..141
                     /region_name="PH_14"
                     /note="PH domain; pfam17787"
                     /db_xref="CDD:465506"
     Region          149..299
                     /region_name="EFh_PI-PLCbeta2"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 2 (PI-PLC-beta2); cd16209"
                     /db_xref="CDD:320039"
     Region          149..178
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          182..211
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          220..249
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          266..299
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          311..649
                     /region_name="PI-PLCc_beta2"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta2; cd08624"
                     /db_xref="CDD:176561"
     Site            order(327..328,357,359,374,408,461,463,575,602,604)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176561"
     Site            order(327,374)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176561"
     Site            order(328,357,359,408)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176561"
     Region          460..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Region          681..802
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(700,725,757,761,763)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          928..964
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q00722.2)"
     Region          963..1138
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     CDS             1..1170
                     /gene="PLCB2"
                     /gene_synonym="PLC-beta-2"
                     /coded_by="NM_001284298.2:264..3776"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61591.1"
                     /db_xref="GeneID:5330"
                     /db_xref="HGNC:HGNC:9055"
                     /db_xref="MIM:604114"
ORIGIN      
        1 msllnpvllp pkvkaylsqg erfikwddet tvaspvilrv dpkgyylywt yqskemefld
       61 itsirdtrfg kfakmpksqk lrdvfnmdfp dnsfllktlt vvsgpdmvdl tfhnfvsyke
      121 nvgkawaedv lalvkhplta nasrstfldk ilvklkmqln segkipvknf fqmfpadrkr
      181 veaalsachl pkgkndainp edfpepvyks flmslcprpe ideiftsyha kakpymtkeh
      241 ltkfinqkqr dsrlnsllfp parpdqvqgl idkyepsgin aqrgqlspeg mvwflcgpen
      301 svlaqdklll hhdmtqplnh yfinsshnty ltagqfsgls saemyrqvll sgcrcveldc
      361 wkgkppdeep iithgftmtt diffkeaiea iaesafktsp ypiilsfenh vdsprqqakm
      421 aeycrtifgd mllteplekf plkpgvplps pedlrgkili knkknqfsgp tssskdtgge
      481 aegssppsap agegtvwage egteleeeev eeeeeeesgn ldeeeikkmq sdegtaglev
      541 tayeemsslv nyiqptkfvs fefsaqknrs yvissftelk aydllskasv qfvdynkrqm
      601 sriypkgtrm dssnympqmf wnagcqmval nfqtmdlpmq qnmavfefng qsgyllkhef
      661 mrrpdkqfnp fsvdridvvv attlsitvis gqflsersvr tyvevelfgl pgdpkrryrt
      721 klspstnsin pvwkeepfvf ekilmpelas lrvavmeegn kflghriipi nalnsgyhhl
      781 clhsesnmpl tmpalfifle mkdyipgawa dltvalanpi kffsahdtks vklkeamggl
      841 pekpfplasp vasqvngala ptsngspepr tasleelrel kgvvklqrrh ekelrelerr
      901 garrweellq rgaaqlaelg ppgvggvgac klgpgkgsrk krslpreesa gaapgegpeg
      961 vdgrvrelkd rlelellrqg eeqyecvlkr keqhvaeqis kmmelarekq aaelkalket
     1021 sendtkemkk kletkrleri qgmtkvttdk maqerlkrei nnshiqevvq vikqmtenle
     1081 rhqekleekq aacleqirem ekqfqkeala eyearmkgle aevkesvrac lrtcfpseak
     1141 dkperacecp pelceqdpli akadaqesrl
//
LOCUS       NP_001291868            1477 aa            linear   PRI 20-NOV-2025
DEFINITION  G patch domain-containing protein 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001291868
VERSION     NP_001291868.1
DBSOURCE    REFSEQ: accession NM_001304939.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1477)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1477)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
  REMARK    GeneRIF: GPATCH8 modulates mutant SF3B1 mis-splicing and
            pathogenicity in hematologic malignancies.
REFERENCE   3  (residues 1 to 1477)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1477)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 1477)
  AUTHORS   Kaneko,H., Kitoh,H., Matsuura,T., Masuda,A., Ito,M., Mottes,M.,
            Rauch,F., Ishiguro,N. and Ohno,K.
  TITLE     Hyperuricemia cosegregating with osteogenesis imperfecta is
            associated with a mutation in GPATCH8
  JOURNAL   Hum Genet 130 (5), 671-683 (2011)
   PUBMED   21594610
  REMARK    GeneRIF: Two missense single-nucleotide variants in ZPBP2 and
            GPATCH8 on chromosome 17 were identified that cosegregated with
            hyperuricemia in the Japanese family.
REFERENCE   6  (residues 1 to 1477)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 1477)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1477)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 1477)
  AUTHORS   Thornton,M.A., Poncz,M., Korostishevsky,M., Yakobson,E., Usher,S.,
            Seligsohn,U. and Peretz,H.
  TITLE     The human platelet alphaIIb gene is not closely linked to its
            integrin partner beta3
  JOURNAL   Blood 94 (6), 2039-2047 (1999)
   PUBMED   10477733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY048299.1, CN388519.1,
            BC136629.1 and BC024147.2.
            
            Summary: The protein encoded by this gene contains an
            RNA-processing domain, a zinc finger domain, a lysine-rich region
            and a serine-rich region. A mutation in the serine-rich region of
            the protein is thought to be associated with hyperuricemia (PMID:
            21594610). Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Feb
            2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.177818.1,
                                           SRR1803611.98650.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1477
                     /product="G patch domain-containing protein 8 isoform 2"
                     /note="g patch domain-containing protein 8"
                     /calculated_mol_wt=161199
     Region          15..57
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          <57..>182
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          111..138
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          147..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          298..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          394..516
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            454
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          554..1276
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            889
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            956
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1010
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          <1031..1291
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     CDS             1..1477
                     /gene="GPATCH8"
                     /gene_synonym="GPATC8; KIAA0553"
                     /coded_by="NM_001304939.2:37..4470"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23131"
                     /db_xref="HGNC:HGNC:29066"
                     /db_xref="MIM:614396"
ORIGIN      
        1 madrfsrfne drdfqdnigh rllqkhgwkl gqglgkslqg rtdpipivvk ydvmgmgrme
       61 meldyaedat errrvlevek edteelrqky kdyvdkekai akaledlran fycelcdkqy
      121 qkhqefdnhi nsydhahkqr lkdlkqrefa rnvssrsrkd ekkqekalrr lhelaeqrkq
      181 aecapgsgpm fkpttvavde eggeddkdes atnsgtgata scglgsefst dkggpftavq
      241 itnttglaqa pglasqgisf giknnlgtpl qklgvsfsfa kkapvklesi asvfkdhaee
      301 gtsedgtkpd ekssdqglqk vgdsdgssnl dgkkededpq dggslastls klkrmkreeg
      361 agatepeyyh yippahckvk pnfpfllfmr aseqmdgdnt thpknapesk kgsspkpksc
      421 ikaaasqgae ktvsevseqp ketsmtepse pgskaeakka lggdvsdqsl eshsqkvset
      481 qmcesnsske tslatpagke sqegpkhptg pffpvlskde stalqwpsel liftkaepsi
      541 syscnplyfd fklsrnkdar tkgtekpkdi gssskdhlqg ldpgepnksk evggekivrs
      601 sggrmdapas gsacsglnkq epggshgset edtgrslpsk kersgkshrh kkkkkhkkss
      661 khkrkhkadt eeksskaesg ekskkrkkrk rkknkssapa dsergpkpep pgsgspappr
      721 rrrraqddsq rrslpaeegs sgkkdegggg sssqdhggrk hkgelppssc qrragtkrss
      781 rsshrsqpss gdedsddass hrlhqkspsq yseeeeeeds gsehsrsrsr sgrrhsshrs
      841 srrsyssssd assdqscysr qrsysddsys dysdrsrrhs krshdsddsd yasskhrskr
      901 hkysssdddy slscsqsrsr srshtrersr srgrsrsssc srsrskrrsr sttahswqrs
      961 rsysrdrsrs trspsqrsgs rkrswghesp eerhsgrrdf irskiyrsqs phyfrsgrge
     1021 gpgkkddgrg ddskatgpps qnsnigtgrg segdcspedk nsvtakllle kiqsrkverk
     1081 psvseevqat pnkagpklkd ppqgyfgpkl ppslgnkpvl pligklpatr kpnkkceesg
     1141 lergeeqeqs eteegppgss dalfghqfps eettgplldp ppeesksgea tadhpvaplg
     1201 tpahsdcypg dptishnylp dpsdgdtles ldsssqpgpv essllpiapd lehfpsyapp
     1261 sgdpsiestd gaedaslapl esqpitftpe emekysklqq aaqqhiqqql lakqvkafpa
     1321 saalapatpa lqpihiqqpa tasatsittv qhailqhhaa aaaaaigihp hphpqplaqv
     1381 hhipqphltp islshlthsi ipghpatfla shpihiipas aihpgpftfh pvphaalypt
     1441 llaprpaaaa atalhlhpll hpifsgqdlq hppshgt
//
LOCUS       NP_001354659             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354659
VERSION     NP_001354659.1
DBSOURCE    REFSEQ: accession NM_001367730.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (14), as well as variants 3, 4,
            9-13, and 15-20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.117705.1,
                                           SRR1803616.158632.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367730.1:169..1644"
                     /note="isoform c is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_055516               1056 aa            linear   PRI 20-NOV-2025
DEFINITION  selenocysteine insertion sequence-binding protein 2-like isoform 2
            [Homo sapiens].
ACCESSION   NP_055516 XP_034905
VERSION     NP_055516.2
DBSOURCE    REFSEQ: accession NM_014701.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1056)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1056)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1056)
  AUTHORS   Chiu,S.C., Chen,K.C., Hsia,J.Y., Chuang,C.Y., Wan,C.X., Wei,T.W.,
            Huang,Y.J., Chen,J.M., Liao,Y.A. and Yu,C.R.
  TITLE     Overexpression of Aurora-A bypasses cytokinesis through
            phosphorylation of suppressed in lung cancer
  JOURNAL   Am J Physiol Cell Physiol 317 (3), C600-C612 (2019)
   PUBMED   31314582
  REMARK    GeneRIF: SLAN mediates the Aurora-A-triggered cytokinesis bypass
            and SLAN plays dual roles in that process depending on its
            phosphorylation status.
REFERENCE   4  (residues 1 to 1056)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 1056)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 1056)
  AUTHORS   Donovan,J. and Copeland,P.R.
  TITLE     Selenocysteine insertion sequence binding protein 2L is implicated
            as a novel post-transcriptional regulator of selenoprotein
            expression
  JOURNAL   PLoS One 7 (4), e35581 (2012)
   PUBMED   22530054
  REMARK    GeneRIF: SECISBP2L (SBP2L) interacts with all known human SECIS
            RNAs in vitro and selenoprotein mRNAs co-immunoprecipitate with
            endogenous SBP2L, suggesting a role in regulating selenoprotein
            expression.
REFERENCE   7  (residues 1 to 1056)
  AUTHORS   Yu,C.T., Hsia,J.Y., Hseih,Y.C., Su,L.J., Lee,T.C., Ku,C.F.,
            Chen,K.S., Chen,J.M., Wei,T.Y., Lee,Y.C., Huang,C.Y., Wu,Y.C.,
            Yang,C.Y. and Hsu,S.L.
  TITLE     The novel protein suppressed in lung cancer down-regulated in lung
            cancer tissues retards cell proliferation and inhibits the
            oncokinase Aurora-A
  JOURNAL   J Thorac Oncol 6 (6), 988-997 (2011)
   PUBMED   21566536
  REMARK    GeneRIF: SLAN, also known as KIAA0256. The novel protein suppressed
            in lung cancer down-regulated in lung cancer tissues retards cell
            proliferation and inhibits the oncokinase Aurora-A.
REFERENCE   8  (residues 1 to 1056)
  AUTHORS   Tomarev,S.I., Wistow,G., Raymond,V., Dubois,S. and Malyukova,I.
  TITLE     Gene expression profile of the human trabecular meshwork: NEIBank
            sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 44 (6), 2588-2596 (2003)
   PUBMED   12766061
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA394911.1, D87445.3, BM129242.1 and CD678675.1.
            
            On Mar 10, 2005 this sequence version replaced NP_055516.1.
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            CDS compared to variant 1. The resulting isoform (2) is shorter and
            lacks an internal segment compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D87445.3, SRR1660809.124923.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1056
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..1056
                     /product="selenocysteine insertion sequence-binding
                     protein 2-like isoform 2"
                     /note="selenocysteine insertion sequence-binding protein
                     2-like"
                     /calculated_mol_wt=116417
     Region          657..759
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..1056
                     /gene="SECISBP2L"
                     /gene_synonym="SBP2L; SLAN"
                     /coded_by="NM_014701.4:148..3318"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32234.1"
                     /db_xref="GeneID:9728"
                     /db_xref="HGNC:HGNC:28997"
                     /db_xref="MIM:615756"
ORIGIN      
        1 mdrapteqnv klsaevepfi pqkkspdtfm ipmalpndng svsgveptpi psylitcypf
       61 vqenqsnrqf plynndirwq qpnpnptgpy faypiisaqp pvsteytyyq lmpapcaqvm
      121 gfyhpfptpy sntfqaantv naittecter psqlgqvfpl sshrsrnsnr gsvvpkqqll
      181 qqhikskrpl vknvatqket naagpdsrsk ivllvdasqq tdfpsdiank slsettatml
      241 wkskgrrrra shptaessse qgaseadids dsgycspkhs nnqpaagalr npdsgtmnhv
      301 essmcaggvn wsnvtcqatq kkpwmeknqt fsrggrqteq rnnsqdedgf qelnengnak
      361 deniqqklss kvlddlpens pinivqtpip ittsvpkrak sqkkkalaaa lataqeysei
      421 smeqkklqea lskaagkknk tpvqldlgdm laalekqqqa mkarqitntr plsytvvtaa
      481 sfhtkdstnr kpltksqpcl tsfnsvdias skakkgkeke iaklkrptal kkvilkeree
      541 kkgrltvdhn llgseeptem hldfiddlpq eivsqedtgl smpsdtslsp asqnspycmt
      601 pvsqgspass gigspmasst itkihskrfr eycnqvlcke idecvtlllq elvsfqeriy
      661 qkdpvrakar rrlvmglrev tkhmklnkik cviispncek iqskggldea lynviamare
      721 qeipfvfalg rkalgrcvnk lvpvsvvgif nyfgaeslfn klvelteear kaykdmvaam
      781 eqeqaeealk nvkkvphhmg hsrnpsaasa isfcsvisep isevnekeye tnwrnmvets
      841 dgleasenek evsckhstse kpsklpfdtp pigkqpslva tgsttsatsa gkstasdkee
      901 vkpddlewas qqstetgsld gscrdllnss itsttstlvp gmleeeeded eeeeedythe
      961 pisvevqlns rieswvsetq rtmetlqlgk tlngseednv eqsgeeeaea pevlepgmds
     1021 eawtadqqas pgqqkssncs slnkehsdsn yttqtt
//
LOCUS       NP_001357401             557 aa            linear   PRI 20-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001357401 XP_011532908
VERSION     NP_001357401.1
DBSOURCE    REFSEQ: accession NM_001370472.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Chen,Y., Khazina,E., Izaurralde,E. and Weichenrieder,O.
  TITLE     Crystal structure and functional properties of the human CCR4-CAF1
            deadenylase complex
  JOURNAL   Nucleic Acids Res 49 (11), 6489-6510 (2021)
   PUBMED   34038562
  REMARK    GeneRIF: Crystal structure and functional properties of the human
            CCR4-CAF1 deadenylase complex.
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Raisch,T., Chang,C.T., Levdansky,Y., Muthukumar,S., Raunser,S. and
            Valkov,E.
  TITLE     Reconstitution of recombinant human CCR4-NOT reveals molecular
            insights into regulated deadenylation
  JOURNAL   Nat Commun 10 (1), 3173 (2019)
   PUBMED   31320642
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Morita,M., Siddiqui,N., Katsumura,S., Rouya,C., Larsson,O.,
            Nagashima,T., Hekmatnejad,B., Takahashi,A., Kiyonari,H., Zang,M.,
            St-Arnaud,R., Oike,Y., Giguere,V., Topisirovic,I.,
            Okada-Hatakeyama,M., Yamamoto,T. and Sonenberg,N.
  TITLE     Hepatic posttranscriptional network comprised of CCR4-NOT
            deadenylase and FGF21 maintains systemic metabolic homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 116 (16), 7973-7981 (2019)
   PUBMED   30926667
  REMARK    GeneRIF: Studied hepatic role in metabolic homeostasis of
            fibroblast growth factor 21(FGF21) and the 'CCR4-NOT complex' (a
            multisubunit protein complex composed of 'CCR4-NOT transcription
            complex subunit 6 like' (CNOT6L) and 'CCR4-NOT transcription
            complex subunit 6' (CNOT6). Results show CNOT6L plays a major role
            in regulation FGF21 levels.
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Morel,A.P., Sentis,S., Bianchin,C., Le Romancer,M., Jonard,L.,
            Rostan,M.C., Rimokh,R. and Corbo,L.
  TITLE     BTG2 antiproliferative protein interacts with the human CCR4
            complex existing in vivo in three cell-cycle-regulated forms
  JOURNAL   J Cell Sci 116 (Pt 14), 2929-2936 (2003)
   PUBMED   12771185
  REMARK    GeneRIF: CCR4 and BTG2 interact and have a role in cell-cycle
            regulation
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Chen,J., Chiang,Y.C. and Denis,C.L.
  TITLE     CCR4, a 3'-5' poly(A) RNA and ssDNA exonuclease, is the catalytic
            component of the cytoplasmic deadenylase
  JOURNAL   EMBO J 21 (6), 1414-1426 (2002)
   PUBMED   11889047
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Dupressoir,A., Morel,A.P., Barbot,W., Loireau,M.P., Corbo,L. and
            Heidmann,T.
  TITLE     Identification of four families of yCCR4- and Mg2+-dependent
            endonuclease-related proteins in higher eukaryotes, and
            characterization of orthologs of yCCR4 with a conserved
            leucine-rich repeat essential for hCAF1/hPOP2 binding
  JOURNAL   BMC Genomics 2, 9 (2001)
   PUBMED   11747467
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Okubo,K., Itoh,K., Fukushima,A., Yoshii,J. and Matsubara,K.
  TITLE     Monitoring cell physiology by expression profiles and discovering
            cell type-specific genes by compiled expression profiles
  JOURNAL   Genomics 30 (2), 178-186 (1995)
   PUBMED   8586417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034213.5 and AC122714.2.
            
            On May 8, 2019 this sequence version replaced XP_011532908.1.
            
            Summary: This gene encodes the catalytic component of the CCR4-NOT
            core transcriptional regulation complex. The encoded protein has a
            3'-5' RNase activity and prefers polyadenylated substrates. The
            CCR4-NOT complex plays a role in many cellular processes, including
            miRNA-mediated repression, mRNA degradation, and transcriptional
            regulation. [provided by RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.239524.1,
                                           SRR1803613.200998.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261951.9/ ENSP00000261951.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..557
                     /product="CCR4-NOT transcription complex subunit 6 isoform
                     1"
                     /EC_number="3.1.13.4"
                     /note="carbon catabolite repression 4 protein; cytoplasmic
                     deadenylase; carbon catabolite repressor protein 4
                     homolog"
                     /calculated_mol_wt=63176
     Region          <33..>133
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          33..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          53..75
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          75..96
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          76..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          98..120
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          99..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          121..143
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          122..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          153..557
                     /region_name="Nuclease domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          191..540
                     /region_name="Deadenylase_CCR4a"
                     /note="C-terminal deadenylase domain of CCR4a, also known
                     as CCR4-NOT transcription complex subunit 6; cd10313"
                     /db_xref="CDD:197340"
     Site            order(195,240,361,364,366,372,412,414,416,481,486,
                     490..491,531)
                     /site_type="active"
                     /db_xref="CDD:197340"
     Site            order(195,240,361,364,366,372,412,414,416,481,486,490,531)
                     /site_type="other"
                     /note="poly(A) RNA binding site [nucleotide binding]"
                     /db_xref="CDD:197340"
     Site            order(195,240,361,412,414,491,530..531)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197340"
     Site            order(195,240,530)
                     /site_type="other"
                     /note="Mg binding site A [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(361,414,531)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(412,414,531)
                     /site_type="other"
                     /note="Mg binding site B [ion binding]"
                     /db_xref="CDD:197340"
     CDS             1..557
                     /gene="CNOT6"
                     /gene_synonym="CCR4; Ccr4a"
                     /coded_by="NM_001370472.1:388..2061"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4455.1"
                     /db_xref="GeneID:57472"
                     /db_xref="HGNC:HGNC:14099"
                     /db_xref="MIM:608951"
ORIGIN      
        1 mpkekyeppd prrmytimss eeaangkksh waeleisgkv rslsaslwsl thltalhlsd
       61 nslsripsdi aklhnlvyld lssnkirslp aelgnmvslr elhlnnnllr vlpfelgklf
      121 qlqtlglkgn pltqdilnly qepdgtrrll nylldnlsgt akritteqpp prswimlqep
      181 drtrptalfs vmcynvlcdk yatrqlygyc pswalnwdyr kkaiiqeils cnadivslqe
      241 veteqyysff lvelkergyn gffspksrar tmseqerkhv dgcaiffkte kftlvqkhtv
      301 efnqlamans egseamlnrv mtkdnigvav llelrkesie mpsgkphlgt ekqlilvana
      361 hmhwdpeysd vklvqtmmfl sevkniidka srnlkssvlg efgtiplvlc adlnslpdsg
      421 vveylstggv etnhkdfkel rynesltnfs chgkngttng rithgfklqs ayesglmpyt
      481 nytfdfkgii dyifyskpql ntlgilgpld hhwlvennis gcphplipsd hfslfaqlel
      541 llpflpqvng ihlpgrr
//
LOCUS       NP_001008709             341 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase PP1-alpha catalytic subunit
            isoform 3 [Homo sapiens].
ACCESSION   NP_001008709
VERSION     NP_001008709.1
DBSOURCE    REFSEQ: accession NM_001008709.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Wang,Z., Song,A., Tao,B., Miao,M., Luo,Y.Q., Wang,J., Yin,Z.,
            Xiao,R., Zhou,X., Shang,X.Y., Hu,S., Liang,K., Danko,C.G. and
            Chen,F.X.
  TITLE     The phosphatase PP1 sustains global transcription by promoting RNA
            polymerase II pause release
  JOURNAL   Mol Cell 84 (24), 4824-4842 (2024)
   PUBMED   39603240
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Kelley,J.R., Dimitrova,E., Maciuszek,M., Nguyen,H.T.,
            Szczurek,A.T., Hughes,A.L., Blackledge,N.P., Kettenbach,A.N. and
            Klose,R.J.
  TITLE     The PNUTS phosphatase complex controls transcription pause release
  JOURNAL   Mol Cell 84 (24), 4843-4861 (2024)
   PUBMED   39603239
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Chen,Z., Li,Y., He,K., Yang,J., Deng,Q., Chen,Y. and Fu,Z.
  TITLE     CircGPRC5A enhances colorectal cancer progress by stabilizing
            PPP1CA and inducing YAP dephosphorylation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 334 (2023)
   PUBMED   38057879
  REMARK    GeneRIF: CircGPRC5A enhances colorectal cancer progress by
            stabilizing PPP1CA and inducing YAP dephosphorylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Saadat,M., Mizuno,Y., Kikuchi,K. and Yoshida,M.C.
  TITLE     Comparative mapping of the gene encoding the catalytic subunit of
            protein phosphatase type 1 alpha (PPP1CA) to human, rat, and mouse
            chromosomes
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 55-57 (1995)
   PUBMED   7736790
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Durfee,T., Becherer,K., Chen,P.L., Yeh,S.H., Yang,Y., Kilburn,A.E.,
            Lee,W.H. and Elledge,S.J.
  TITLE     The retinoblastoma protein associates with the protein phosphatase
            type 1 catalytic subunit
  JOURNAL   Genes Dev 7 (4), 555-569 (1993)
   PUBMED   8384581
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Barker,H.M., Jones,T.A., da Cruz e Silva,E.F., Spurr,N.K., Sheer,D.
            and Cohen,P.T.
  TITLE     Localization of the gene encoding a type I protein phosphatase
            catalytic subunit to human chromosome band 11q13
  JOURNAL   Genomics 7 (2), 159-166 (1990)
   PUBMED   2161401
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Carrey,E.A., Campbell,D.G. and Hardie,D.G.
  TITLE     Phosphorylation and activation of hamster carbamyl phosphate
            synthetase II by cAMP-dependent protein kinase. A novel mechanism
            for regulation of pyrimidine nucleotide biosynthesis
  JOURNAL   EMBO J 4 (13B), 3735-3742 (1985)
   PUBMED   4092695
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Hemmings,H.C. Jr., Greengard,P., Tung,H.Y. and Cohen,P.
  TITLE     DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent
            inhibitor of protein phosphatase-1
  JOURNAL   Nature 310 (5977), 503-505 (1984)
   PUBMED   6087160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL557336.3, S57501.1 and
            BC001888.1.
            
            Summary: The protein encoded by this gene is one of the three
            catalytic subunits of protein phosphatase 1 (PP1). This broadly
            expressed gene encodes the alpha subunit of the PP1 complex that
            associates with over 200 regulatory proteins to form holoenzymes
            which dephosphorylate their biological targets with high
            specificity. PP1 is a serine/threonine specific protein phosphatase
            known to be involved in the regulation of a variety of cellular
            processes, such as cell division, glycogen metabolism, muscle
            contractility, protein synthesis, and HIV-1 viral transcription.
            Increased PP1 activity has been observed in the end stage of heart
            failure. Studies suggest that PP1 is an important regulator of
            cardiac function and that PP1 deregulation is implicated in
            diabetes and multiple types of cancer. Three alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2020].
            
            Transcript Variant: This variant (3, also called PP-1 alpha 2) uses
            an alternate in-frame splice site at the 5' end of an exon compared
            to variant 1. The resulting isoform (3) has the same N- and
            C-termini but is longer compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1101051.1, S57501.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..341
                     /product="serine/threonine-protein phosphatase PP1-alpha
                     catalytic subunit isoform 3"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine protein phosphatase PP1-alpha 1
                     catalytic subunit; serine/threonine-protein phosphatase
                     PP1-alpha catalytic subunit; protein phosphatase 1,
                     catalytic subunit, alpha isozyme; testicular tissue
                     protein Li 155"
                     /calculated_mol_wt=38500
     Region          8..309
                     /region_name="MPP_PP1_PPKL"
                     /note="PP1, PPKL (PP1 and kelch-like) enzymes, and related
                     proteins, metallophosphatase domain; cd07414"
                     /db_xref="CDD:277359"
     Site            order(75,77,103,107,135..136,140..141,145,184,206..208,
                     217,231..233,259,283..287)
                     /site_type="active"
                     /db_xref="CDD:277359"
     Site            order(75,77,103,135,184,259)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277359"
     Site            order(107,140..141,145,206..208,217,231..233,283..287)
                     /site_type="other"
                     /note="natural toxin binding site [chemical binding]"
                     /db_xref="CDD:277359"
     Site            order(190,192,209,214,227,236,244..245,247..249,251..253,
                     268,272,299..300,302,304,306)
                     /site_type="other"
                     /note="MYPT1 binding site [polypeptide binding]"
                     /db_xref="CDD:277359"
     CDS             1..341
                     /gene="PPP1CA"
                     /gene_synonym="PP-1A; PP1A; PP1alpha; PPP1A"
                     /coded_by="NM_001008709.2:77..1102"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS31618.1"
                     /db_xref="GeneID:5499"
                     /db_xref="HGNC:HGNC:9281"
                     /db_xref="MIM:176875"
ORIGIN      
        1 msdseklnld siigrllegs rvltphcapv qgsrpgknvq lteneirglc lksreiflsq
       61 pilleleapl kicgdihgqy ydllrlfeyg gfppesnylf lgdyvdrgkq sleticllla
      121 ykikypenff llrgnhecas inriygfyde ckrryniklw ktftdcfncl piaaivdeki
      181 fcchgglspd lqsmeqirri mrptdvpdqg llcdllwsdp dkdvqgwgen drgvsftfga
      241 evvakflhkh dldlicrahq vvedgyeffa krqlvtlfsa pnycgefdna gammsvdetl
      301 mcsfqilkpa dknkgkygqf sglnpggrpi tpprnsakak k
//
LOCUS       NP_001025029             408 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 35 member F1 [Homo sapiens].
ACCESSION   NP_001025029 XP_167044
VERSION     NP_001025029.2
DBSOURCE    REFSEQ: accession NM_001029858.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Van den Bossche,F., Tevel,V., Gilis,F., Gaussin,J.F., Boonen,M. and
            Jadot,M.
  TITLE     Residence of the Nucleotide Sugar Transporter Family Members
            SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway
  JOURNAL   Int J Mol Sci 25 (12), 6718 (2024)
   PUBMED   38928424
  REMARK    GeneRIF: Residence of the Nucleotide Sugar Transporter Family
            Members SLC35F1 and SLC35F6 in the Endosomal/Lysosomal Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Qian,C., Wu,Z., Sun,R., Yu,H., Zeng,J., Rao,Y. and Li,Y.
  TITLE     Localization, proteomics, and metabolite profiling reveal a
            putative vesicular transporter for UDP-glucose
  JOURNAL   Elife 10, e65417 (2021)
   PUBMED   34269178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Eijgelsheim,M., Newton-Cheh,C., Sotoodehnia,N., de Bakker,P.I.,
            Muller,M., Morrison,A.C., Smith,A.V., Isaacs,A., Sanna,S., Dorr,M.,
            Navarro,P., Fuchsberger,C., Nolte,I.M., de Geus,E.J., Estrada,K.,
            Hwang,S.J., Bis,J.C., Ruckert,I.M., Alonso,A., Launer,L.J.,
            Hottenga,J.J., Rivadeneira,F., Noseworthy,P.A., Rice,K.M., Perz,S.,
            Arking,D.E., Spector,T.D., Kors,J.A., Aulchenko,Y.S., Tarasov,K.V.,
            Homuth,G., Wild,S.H., Marroni,F., Gieger,C., Licht,C.M.,
            Prineas,R.J., Hofman,A., Rotter,J.I., Hicks,A.A., Ernst,F.,
            Najjar,S.S., Wright,A.F., Peters,A., Fox,E.R., Oostra,B.A.,
            Kroemer,H.K., Couper,D., Volzke,H., Campbell,H., Meitinger,T.,
            Uda,M., Witteman,J.C., Psaty,B.M., Wichmann,H.E., Harris,T.B.,
            Kaab,S., Siscovick,D.S., Jamshidi,Y., Uitterlinden,A.G.,
            Folsom,A.R., Larson,M.G., Wilson,J.F., Penninx,B.W., Snieder,H.,
            Pramstaller,P.P., van Duijn,C.M., Lakatta,E.G., Felix,S.B.,
            Gudnason,V., Pfeufer,A., Heckbert,S.R., Stricker,B.H.,
            Boerwinkle,E. and O'Donnell,C.J.
  TITLE     Genome-wide association analysis identifies multiple loci related
            to resting heart rate
  JOURNAL   Hum Mol Genet 19 (19), 3885-3894 (2010)
   PUBMED   20639392
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Karasik,D., Hsu,Y.H., Zhou,Y., Cupples,L.A., Kiel,D.P. and
            Demissie,S.
  TITLE     Genome-wide pleiotropy of osteoporosis-related phenotypes: the
            Framingham Study
  JOURNAL   J Bone Miner Res 25 (7), 1555-1563 (2010)
   PUBMED   20200953
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Nolte,I.M., Wallace,C., Newhouse,S.J., Waggott,D., Fu,J.,
            Soranzo,N., Gwilliam,R., Deloukas,P., Savelieva,I., Zheng,D.,
            Dalageorgou,C., Farrall,M., Samani,N.J., Connell,J., Brown,M.,
            Dominiczak,A., Lathrop,M., Zeggini,E., Wain,L.V., Newton-Cheh,C.,
            Eijgelsheim,M., Rice,K., de Bakker,P.I., Pfeufer,A., Sanna,S.,
            Arking,D.E., Asselbergs,F.W., Spector,T.D., Carter,N.D.,
            Jeffery,S., Tobin,M., Caulfield,M., Snieder,H., Paterson,A.D.,
            Munroe,P.B. and Jamshidi,Y.
  CONSRTM   Wellcome Trust Case Control Consortium; DCCT/EDIC Research Group;
            QTGEN consortium; QTSCD consortium
  TITLE     Common genetic variation near the phospholamban gene is associated
            with cardiac repolarisation: meta-analysis of three genome-wide
            association studies
  JOURNAL   PLoS One 4 (7), e6138 (2009)
   PUBMED   19587794
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Vasan,R.S., Glazer,N.L., Felix,J.F., Lieb,W., Wild,P.S.,
            Felix,S.B., Watzinger,N., Larson,M.G., Smith,N.L., Dehghan,A.,
            Grosshennig,A., Schillert,A., Teumer,A., Schmidt,R., Kathiresan,S.,
            Lumley,T., Aulchenko,Y.S., Konig,I.R., Zeller,T., Homuth,G.,
            Struchalin,M., Aragam,J., Bis,J.C., Rivadeneira,F., Erdmann,J.,
            Schnabel,R.B., Dorr,M., Zweiker,R., Lind,L., Rodeheffer,R.J.,
            Greiser,K.H., Levy,D., Haritunians,T., Deckers,J.W., Stritzke,J.,
            Lackner,K.J., Volker,U., Ingelsson,E., Kullo,I., Haerting,J.,
            O'Donnell,C.J., Heckbert,S.R., Stricker,B.H., Ziegler,A.,
            Reffelmann,T., Redfield,M.M., Werdan,K., Mitchell,G.F., Rice,K.,
            Arnett,D.K., Hofman,A., Gottdiener,J.S., Uitterlinden,A.G.,
            Meitinger,T., Blettner,M., Friedrich,N., Wang,T.J., Psaty,B.M., van
            Duijn,C.M., Wichmann,H.E., Munzel,T.F., Kroemer,H.K.,
            Benjamin,E.J., Rotter,J.I., Witteman,J.C., Schunkert,H.,
            Schmidt,H., Volzke,H. and Blankenberg,S.
  TITLE     Genetic variants associated with cardiac structure and function: a
            meta-analysis and replication of genome-wide association data
  JOURNAL   JAMA 302 (2), 168-178 (2009)
   PUBMED   19584346
  REMARK    GeneRIF: Meta-analysis and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Newton-Cheh,C., Eijgelsheim,M., Rice,K.M., de Bakker,P.I., Yin,X.,
            Estrada,K., Bis,J.C., Marciante,K., Rivadeneira,F.,
            Noseworthy,P.A., Sotoodehnia,N., Smith,N.L., Rotter,J.I.,
            Kors,J.A., Witteman,J.C., Hofman,A., Heckbert,S.R., O'Donnell,C.J.,
            Uitterlinden,A.G., Psaty,B.M., Lumley,T., Larson,M.G. and
            Stricker,B.H.
  TITLE     Common variants at ten loci influence QT interval duration in the
            QTGEN Study
  JOURNAL   Nat Genet 41 (4), 399-406 (2009)
   PUBMED   19305408
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136478.9, Z95326.1, AL449196.1 and AL133379.3.
            
            On May 23, 2008 this sequence version replaced NP_001025029.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028615.1, SRR1803612.90006.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: locus in the vicinity of
                                      disease-associated variant(s)
            MANE Ensembl match     :: ENST00000360388.9/ ENSP00000353557.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.2-q22.31"
     Protein         1..408
                     /product="solute carrier family 35 member F1"
                     /calculated_mol_wt=45215
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Region          56..355
                     /region_name="SLC35F"
                     /note="Solute carrier family 35; pfam06027"
                     /db_xref="CDD:283644"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            129..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            311..331
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     Site            335..355
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T1Q4.2)"
     CDS             1..408
                     /gene="SLC35F1"
                     /gene_synonym="C6orf169; dJ230I3.1"
                     /coded_by="NM_001029858.4:464..1690"
                     /db_xref="CCDS:CCDS34524.1"
                     /db_xref="GeneID:222553"
                     /db_xref="HGNC:HGNC:21483"
                     /db_xref="MIM:620349"
ORIGIN      
        1 mippeqpqqq lqppspappn hvvttienlp aegsggggsl sassragvrq rirkvlnrem
       61 lisvalgqvl sllicgiglt skylsedfha ntpvfqsfln yillflvytt tlavrqgeen
      121 llailrrrww kymilglidl eanylvvkay qyttltsiql ldcfvipvvi llswffllir
      181 ykavhfigiv vcilgmgcmv gadvlvgrhq gagenklvgd llvlggatly gisnvweeyi
      241 irtlsrvefl gmiglfgaff sgiqlaimeh kellkvpwdw qigllyvgfs acmfglysfm
      301 pvvikktsat svnlslltad lyslfcglfl fhykfsglyl lsfftiligl vlysststyi
      361 aqdprvykqf rnpsgpvvdl pttaqvepsv tytslgqete eephvrva
//
LOCUS       NP_002660                514 aa            linear   PRI 20-NOV-2025
DEFINITION  pleiotropic regulator 1 isoform 1 [Homo sapiens].
ACCESSION   NP_002660
VERSION     NP_002660.1
DBSOURCE    REFSEQ: accession NM_002669.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Kwon,J.H. and Kim,S.H.
  TITLE     YBX1 promotes epithelial-mesenchymal transition in hepatocellular
            carcinoma via transcriptional regulation of PLRG1
  JOURNAL   Med Oncol 41 (11), 280 (2024)
   PUBMED   39400789
  REMARK    GeneRIF: YBX1 promotes epithelial-mesenchymal transition in
            hepatocellular carcinoma via transcriptional regulation of PLRG1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Ajuh,P. and Lamond,A.I.
  TITLE     Identification of peptide inhibitors of pre-mRNA splicing derived
            from the essential interaction domains of CDC5L and PLRG1
  JOURNAL   Nucleic Acids Res 31 (21), 6104-6116 (2003)
   PUBMED   14576297
  REMARK    GeneRIF: the interaction between CDC5L and PLRG1 is essential for
            pre-mRNA splicing
            Erratum:[Nucleic Acids Res. 2022 Aug 12;50(14):8400. doi:
            10.1093/nar/gkac623. PMID: 35848918]
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Ajuh,P., Sleeman,J., Chusainow,J. and Lamond,A.I.
  TITLE     A direct interaction between the carboxyl-terminal region of CDC5L
            and the WD40 domain of PLRG1 is essential for pre-mRNA splicing
  JOURNAL   J Biol Chem 276 (45), 42370-42381 (2001)
   PUBMED   11544257
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Ajuh,P., Kuster,B., Panov,K., Zomerdijk,J.C., Mann,M. and
            Lamond,A.I.
  TITLE     Functional analysis of the human CDC5L complex and identification
            of its components by mass spectrometry
  JOURNAL   EMBO J 19 (23), 6569-6581 (2000)
   PUBMED   11101529
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Nemeth,K., Salchert,K., Putnoky,P., Bhalerao,R., Koncz-Kalman,Z.,
            Stankovic-Stangeland,B., Bako,L., Mathur,J., Okresz,L., Stabel,S.,
            Geigenberger,P., Stitt,M., Redei,G.P., Schell,J. and Koncz,C.
  TITLE     Pleiotropic control of glucose and hormone responses by PRL1, a
            nuclear WD protein, in Arabidopsis
  JOURNAL   Genes Dev 12 (19), 3059-3073 (1998)
   PUBMED   9765207
  REMARK    GeneRIF: Study includes the isolation of a cDNA encoding the human
            PRL1 homolog.
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP314297.1, BC106004.1,
            AC107385.4 and AW291931.1.
            
            Summary: This gene encodes a core component of the cell division
            cycle 5-like (CDC5L) complex. The CDC5L complex is part of the
            spliceosome and is required for pre-mRNA splicing. The encoded
            protein plays a critical role in alternative splice site selection.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036046.1, SRR11853561.22706.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000499023.7/ ENSP00000424417.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..514
                     /product="pleiotropic regulator 1 isoform 1"
                     /note="pleiotropic regulator 1 (PRL1 homolog,
                     Arabidopsis); transport and golgi organization 4 homolog"
                     /calculated_mol_wt=57063
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O43660.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43660.1)"
     Region          135..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          196..490
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43660.1)"
     Region          202..241
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Site            order(203,221,225,231..232,244..245,263,267,273..274,
                     286..287,304,309,315..316,329,346,351,357..358,370..371,
                     389,393,398..399,411..412,428,433,439..440,452,461,479,
                     483,489..490)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          209..244
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          244..283
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          250..286
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          286..325
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          291..327
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          328..367
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          334..369
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          370..410
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          375..410
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43660.1)"
     Region          411..449
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          416..455
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          460..499
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O43660.1)"
     Region          465..489
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..514
                     /gene="PLRG1"
                     /gene_synonym="Cwc1; PRL1; PRP46; PRPF46; TANGO4"
                     /coded_by="NM_002669.4:93..1637"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34083.1"
                     /db_xref="GeneID:5356"
                     /db_xref="HGNC:HGNC:9089"
                     /db_xref="MIM:605961"
ORIGIN      
        1 mveevqkhsv htlvfrslkr thdmfvadng kpvpldeesh krkmaiklrn eygpvlhmpt
       61 skenlkekgp qnatdsyvhk qypanqgqev eyfvagthpy ppgpgvalta dtkiqrmpse
      121 saaqslaval plqtkadanr tapsgseyrh pgasdrpqpt amnsivmetg ntknsalmak
      181 kaptmpkpqw hppwklyrvi sghlgwvrci avepgnqwfv tgsadrtiki wdlasgklkl
      241 sltghistvr gvivstrspy lfscgedkqv kcwdleynkv irhyhghlsa vygldlhpti
      301 dvlvtcsrds tariwdvrtk asvhtlsght navatvrcqa aepqiitgsh dttirlwdlv
      361 agktrvtltn hkksvravvl hprhytfasg spdnikqwkf pdgsfiqnls ghnaiintlt
      421 vnsdgvlvsg adngtmhlwd wrtgynfqrv haavqpgsld sesgifacaf dqsesrllta
      481 eadktikvyr eddtateeth pvswkpeiik rkrf
//
LOCUS       NP_001166996             518 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein RO60 isoform 4 [Homo sapiens].
ACCESSION   NP_001166996
VERSION     NP_001166996.1
DBSOURCE    REFSEQ: accession NM_001173525.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Song,Y., Wei,F., Liu,Y., Han,F., Ma,L., Zhuang,Y., Pan,C., Jia,Z.
            and Gong,A.
  TITLE     IL-33/ST2 Activation Is involved in Ro60-Regulated Photosensitivity
            in Cutaneous Lupus Erythematosus
  JOURNAL   Mediators Inflamm 2022, 4955761 (2022)
   PUBMED   35909659
  REMARK    GeneRIF: IL-33/ST2 Activation Is involved in Ro60-Regulated
            Photosensitivity in Cutaneous Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Lee,A.Y.S., Beroukas,D., Brown,L., Lucchesi,C., Kaur,A., Gyedu,L.,
            Hughes,N., Ng,Y.H., Saran,O., Gordon,T.P. and Wang,J.J.
  TITLE     Identification of a unique anti-Ro60 subset with restricted
            serological and molecular profiles
  JOURNAL   Clin Exp Immunol 203 (1), 13-21 (2021)
   PUBMED   32852779
  REMARK    GeneRIF: Identification of a unique anti-Ro60 subset with
            restricted serological and molecular profiles.
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Leng,Y., Sim,S., Magidson,V. and Wolin,S.L.
  TITLE     Noncoding Y RNAs regulate the levels, subcellular distribution and
            protein interactions of their Ro60 autoantigen partner
  JOURNAL   Nucleic Acids Res 48 (12), 6919-6930 (2020)
   PUBMED   32469055
  REMARK    GeneRIF: Noncoding Y RNAs regulate the levels, subcellular
            distribution and protein interactions of their Ro60 autoantigen
            partner.
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Barcellos,K.S., Nonogaki,S., Enokihara,M.M., Teixeira,M.S. and
            Andrade,L.E.
  TITLE     Differential expression of Ro/SSA 60 kDa and La/SSB, but not Ro/SSA
            52 kDa, mRNA and protein in minor salivary glands from patients
            with primary Sjogren's syndrome
  JOURNAL   J Rheumatol 34 (6), 1283-1292 (2007)
   PUBMED   17552056
  REMARK    GeneRIF: Increased Ro/SSA 60 and La/SSB mRNA expression in minor
            salivary glands in primary Sjogren's syndrome (pSS) suggest that
            these 2 autoantigens, but not Ro/SSA 52, are involved in
            tissue-specific autoimmune response in pSS.
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Pruijn,G.J., Slobbe,R.L. and van Venrooij,W.J.
  TITLE     Analysis of protein--RNA interactions within Ro ribonucleoprotein
            complexes
  JOURNAL   Nucleic Acids Res 19 (19), 5173-5180 (1991)
   PUBMED   1833722
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Jitsukawa,T., Nakajima,S., Usui,J. and Watanabe,H.
  TITLE     Detection of anti-nuclear antibodies from patients with systemic
            rheumatic diseases by ELISA using HEp-2 cell nuclei
  JOURNAL   J Clin Lab Anal 5 (1), 49-53 (1991)
   PUBMED   1999763
REFERENCE   8  (residues 1 to 518)
  AUTHORS   James,J.A., Dickey,W.D., Fujisaku,A., O'Brien,C.A., Deutscher,S.L.,
            Keene,J.D. and Harley,J.B.
  TITLE     Antigenicity of a recombinant Ro (SS-A) fusion protein
  JOURNAL   Arthritis Rheum 33 (1), 102-106 (1990)
   PUBMED   1689160
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Ben-Chetrit,E., Gandy,B.J., Tan,E.M. and Sullivan,K.F.
  TITLE     Isolation and characterization of a cDNA clone encoding the 60-kD
            component of the human SS-A/Ro ribonucleoprotein autoantigen
  JOURNAL   J Clin Invest 83 (4), 1284-1292 (1989)
   PUBMED   2649513
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Deutscher,S.L., Harley,J.B. and Keene,J.D.
  TITLE     Molecular analysis of the 60-kDa human Ro ribonucleoprotein
  JOURNAL   Proc Natl Acad Sci U S A 85 (24), 9479-9483 (1988)
   PUBMED   3200833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX761715.1, AY205314.1, AL136370.4 and AI433657.1.
            
            Transcript Variant: This variant (4) contains an alternate exon in
            the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 4, which has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY205314.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.2"
     Protein         1..518
                     /product="RNA-binding protein RO60 isoform 4"
                     /note="Sjogren syndrome antigen A2 (60kD,
                     ribonucleoprotein autoantigen SS-A/Ro); gastric cancer
                     multi-drug resistance protein; TROVE domain family member
                     2; 60 kDa ribonucleoprotein Ro; sjoegren syndrome type A
                     antigen; Ro/SSA 60kDa; ro60 autoantigen; RNA-binding
                     protein RO60"
                     /calculated_mol_wt=58352
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          17..369
                     /region_name="TROVE"
                     /note="TROVE domain; pfam05731"
                     /db_xref="CDD:461724"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          120..284
                     /region_name="RNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          <363..489
                     /region_name="ViaA"
                     /note="Uncharacterized conserved protein, contains a von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG2425"
                     /db_xref="CDD:441973"
     CDS             1..518
                     /gene="RO60"
                     /gene_synonym="RORNP; SSA2; TROVE2"
                     /coded_by="NM_001173525.1:371..1927"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53451.1"
                     /db_xref="GeneID:6738"
                     /db_xref="HGNC:HGNC:11313"
                     /db_xref="MIM:600063"
ORIGIN      
        1 meesvnqmqp lnekqiansq dgyvwqvtdm nrlhrflcfg seggtyyike qklglenaea
       61 lirliedgrg ceviqeiksf sqegrttkqe pmlfalaics qcsdistkqa afkavsevcr
      121 ipthlftfiq fkkdlkesmk cgmwgralrk aiadwynekg gmalalavtk ykqrngwshk
      181 dllrlshlkp sseglaivtk yitkgwkevh elykekalsv etekllkyle avekvkrtrd
      241 elevihliee hrlvrehllt nhlkskevwk allqemplta llrnlgkmta nsvlepgnse
      301 vslvceklcn ekllkkarih pfhilialet yktghglrgk lkwrpdeeil kaldaafykt
      361 fktveptgkr fllavdvsas mnqrvlgsil nastvaaamc mvvtrtekds yvvafsdemv
      421 pcpvttdmtl qqvlmamsqi paggtdcslp miwaqktntp advfivftdn etfaggvhpa
      481 ialreyrkkm dipaklivcg mtsngftiad pddrdtvk
//
LOCUS       NP_054905                198 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 9 isoform 1 [Homo sapiens].
ACCESSION   NP_054905
VERSION     NP_054905.2
DBSOURCE    REFSEQ: accession NM_014186.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087277.11.
            
            On Aug 24, 2007 this sequence version replaced NP_054905.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.179907.1,
                                           SRR1803611.127114.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263401.10/ ENSP00000263401.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..198
                     /product="COMM domain-containing protein 9 isoform 1"
                     /note="COMM domain-containing protein 9"
                     /calculated_mol_wt=21688
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9P000.2)"
     Region          90..197
                     /region_name="Commd9"
                     /note="COMM_Domain containing protein 9. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04757"
                     /db_xref="CDD:240105"
     CDS             1..198
                     /gene="COMMD9"
                     /gene_synonym="C11orf55; HSPC166; LINC00610"
                     /coded_by="NM_014186.4:13..609"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7900.1"
                     /db_xref="GeneID:29099"
                     /db_xref="HGNC:HGNC:25014"
                     /db_xref="MIM:612299"
ORIGIN      
        1 maaltaehfa alqsllkass kdvvrqlcqe sfsssalglk klldvtcssl svtqeeaeel
       61 lqalhrltrl vafrdlssae ailalfpenf hqnlknlltk iilehvstwr teaqanqisl
      121 prlvdldwrv diktssdsis rmavptcllq mkiqedpslc gdkpsisavt velsketldt
      181 mldglgrird qlsavask
//
LOCUS       NP_061865                234 aa            linear   PRI 20-NOV-2025
DEFINITION  BTB/POZ domain-containing protein KCTD5 [Homo sapiens].
ACCESSION   NP_061865
VERSION     NP_061865.1
DBSOURCE    REFSEQ: accession NM_018992.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Rizk,R., Devost,D., Petrin,D. and Hebert,T.E.
  TITLE     KCTD Proteins Have Redundant Functions in Controlling Cellular
            Growth
  JOURNAL   Int J Mol Sci 25 (9), 4993 (2024)
   PUBMED   38732215
  REMARK    GeneRIF: KCTD Proteins Have Redundant Functions in Controlling
            Cellular Growth.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Muntean,B.S., Marwari,S., Li,X., Sloan,D.C., Young,B.D.,
            Wohlschlegel,J.A. and Martemyanov,K.A.
  TITLE     Members of the KCTD family are major regulators of cAMP signaling
  JOURNAL   Proc Natl Acad Sci U S A 119 (1) (2022)
   PUBMED   34934014
  REMARK    GeneRIF: Members of the KCTD family are major regulators of cAMP
            signaling.
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Canales,J., Cruz,P., Diaz,N., Riquelme,D., Leiva-Salcedo,E. and
            Cerda,O.
  TITLE     K+ Channel Tetramerization Domain 5 (KCTD5) Protein Regulates Cell
            Migration, Focal Adhesion Dynamics and Spreading through Modulation
            of Ca2+ Signaling and Rac1 Activity
  JOURNAL   Cells 9 (10), 2273 (2020)
   PUBMED   33053687
  REMARK    GeneRIF: K(+) Channel Tetramerization Domain 5 (KCTD5) Protein
            Regulates Cell Migration, Focal Adhesion Dynamics and Spreading
            through Modulation of Ca(2+) Signaling and Rac1 Activity.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Ahmed,S.M., Theriault,B.L., Uppalapati,M., Chiu,C.W., Gallie,B.L.,
            Sidhu,S.S. and Angers,S.
  TITLE     KIF14 negatively regulates Rap1a-Radil signaling during breast
            cancer progression
  JOURNAL   J Cell Biol 199 (6), 951-967 (2012)
   PUBMED   23209302
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Dementieva,I.S., Tereshko,V., McCrossan,Z.A., Solomaha,E.,
            Araki,D., Xu,C., Grigorieff,N. and Goldstein,S.A.
  TITLE     Pentameric assembly of potassium channel tetramerization
            domain-containing protein 5
  JOURNAL   J Mol Biol 387 (1), 175-191 (2009)
   PUBMED   19361449
  REMARK    GeneRIF: structure reveals assemblies of five subunits while
            tetramers were anticipated; pentameric stoichiometry is observed
            also in solution by scanning transmission electron microscopy mass
            analysis and analytical ultracentrifugation
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Bayon,Y., Trinidad,A.G., de la Puerta,M.L., Del Carmen
            Rodriguez,M., Bogetz,J., Rojas,A., De Pereda,J.M., Rahmouni,S.,
            Williams,S., Matsuzawa,S., Reed,J.C., Crespo,M.S., Mustelin,T. and
            Alonso,A.
  TITLE     KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases
  JOURNAL   FEBS J 275 (15), 3900-3910 (2008)
   PUBMED   18573101
  REMARK    GeneRIF: Analysis of the interaction with cullin3 showed that, in
            addition to the BTB domain, some amino acids in the N-terminus of
            KCTD5 are required for binding to cullin3. Findings suggest that
            KCTD5 is a substrate-specific adaptor for cullin3-based E3 ligases
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Weger,S., Hammer,E., Gotz,A. and Heilbronn,R.
  TITLE     Identification of a cytoplasmic interaction partner of the large
            regulatory proteins Rep78/Rep68 of adeno-associated virus type 2
            (AAV-2)
  JOURNAL   Virology 362 (1), 192-206 (2007)
   PUBMED   17239418
  REMARK    GeneRIF: we have identified a novel cellular AAV-2 Rep78/Rep68
            interaction partner, KCTD5, located predominantly in the cytoplasm.
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Gandhi,T.K., Zhong,J., Mathivanan,S., Karthick,L., Chandrika,K.N.,
            Mohan,S.S., Sharma,S., Pinkert,S., Nagaraju,S., Periaswamy,B.,
            Mishra,G., Nandakumar,K., Shen,B., Deshpande,N., Nayak,R.,
            Sarker,M., Boeke,J.D., Parmigiani,G., Schultz,J., Bader,J.S. and
            Pandey,A.
  TITLE     Analysis of the human protein interactome and comparison with
            yeast, worm and fly interaction datasets
  JOURNAL   Nat Genet 38 (3), 285-293 (2006)
   PUBMED   16501559
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA134449.1 and BC007314.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000047.1, SRR1660805.185512.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301738.9/ ENSP00000301738.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..234
                     /product="BTB/POZ domain-containing protein KCTD5"
                     /note="potassium channel tetramerisation domain containing
                     5"
                     /calculated_mol_wt=25961
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NXV2.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXV2.1)"
     Region          40..151
                     /region_name="BTB_POZ_KCTD5"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein 5
                     (KCTD5); cd18390"
                     /db_xref="CDD:349698"
     Site            order(43,45,49,51..52,55..58,61,83,91..95,98,104,107..108,
                     110,112..119,121,124)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349698"
     Region          213..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXV2.1)"
     CDS             1..234
                     /gene="KCTD5"
                     /coded_by="NM_018992.4:27..731"
                     /db_xref="CCDS:CCDS10475.1"
                     /db_xref="GeneID:54442"
                     /db_xref="HGNC:HGNC:21423"
                     /db_xref="MIM:611285"
ORIGIN      
        1 maenhcells parggigagl ggglcrrcsa glgalaqrpg svskwvrlnv ggtyflttrq
       61 tlcrdpksfl yrlcqadpdl dsdkdetgay lidrdptyfg pvlnylrhgk lvinkdlaee
      121 gvleeaefyn itsliklvkd kirerdskts qvpvkhvyrv lqcqeeeltq mvstmsdgwk
      181 feqlvsigss ynygnedqae flcvvskelh ntpygtasep sekakilqer gsrm
//
LOCUS       NP_004365                 75 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome c oxidase subunit 6C [Homo sapiens].
ACCESSION   NP_004365
VERSION     NP_004365.1
DBSOURCE    REFSEQ: accession NM_004374.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Liu,S., Shao,F., Wang,Y., Zhang,Y., Yu,H., Zhang,N., He,L.,
            Kong,Q., Jiang,H. and Dong,Z.
  TITLE     COX6C expression driven by copy amplification of 8q22.2 regulates
            cell proliferation via mediation of mitosis by ROS-AMPK signaling
            in lung adenocarcinoma
  JOURNAL   Cell Death Dis 15 (1), 74 (2024)
   PUBMED   38242874
  REMARK    GeneRIF: COX6C expression driven by copy amplification of 8q22.2
            regulates cell proliferation via mediation of mitosis by ROS-AMPK
            signaling in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 75)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 75)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 75)
  AUTHORS   Kish,S.J., Mastrogiacomo,F., Guttman,M., Furukawa,Y., Taanman,J.W.,
            Dozic,S., Pandolfo,M., Lamarche,J., DiStefano,L. and Chang,L.J.
  TITLE     Decreased brain protein levels of cytochrome oxidase subunits in
            Alzheimer's disease and in hereditary spinocerebellar ataxia
            disorders: a nonspecific change?
  JOURNAL   J Neurochem 72 (2), 700-707 (1999)
   PUBMED   9930743
REFERENCE   7  (residues 1 to 75)
  AUTHORS   Hofmann,S., Lichtner,P., Schuffenhauer,S., Gerbitz,K.D. and
            Meitinger,T.
  TITLE     Assignment of the human genes coding for cytochrome c oxidase
            subunits Va (COX5A), VIc (COX6C) and VIIc (COX7C) to chromosome
            bands 15q25, 8q22-->q23 and 5q14 and of three pseudogenes (COX5AP1,
            COX6CP1, COX7CP1) to 14q22, 16p12 and 13q14-->q21 by FISH and
            radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 83 (3-4), 226-227 (1998)
   PUBMED   10072584
REFERENCE   8  (residues 1 to 75)
  AUTHORS   Lenka,N., Vijayasarathy,C., Mullick,J. and Avadhani,N.G.
  TITLE     Structural organization and transcription regulation of nuclear
            genes encoding the mammalian cytochrome c oxidase complex
  JOURNAL   Prog Nucleic Acid Res Mol Biol 61, 309-344 (1998)
   PUBMED   9752724
  REMARK    Review article
REFERENCE   9  (residues 1 to 75)
  AUTHORS   Wang,F.L., Wang,Y., Wong,W.K., Liu,Y., Addivinola,F.J., Liang,P.,
            Chen,L.B., Kantoff,P.W. and Pardee,A.B.
  TITLE     Two differentially expressed genes in normal human prostate tissue
            and in carcinoma
  JOURNAL   Cancer Res 56 (16), 3634-3637 (1996)
   PUBMED   8705997
REFERENCE   10 (residues 1 to 75)
  AUTHORS   Otsuka,M., Mizuno,Y., Yoshida,M., Kagawa,Y. and Ohta,S.
  TITLE     Nucleotide sequence of cDNA encoding human cytochrome c oxidase
            subunit VIc
  JOURNAL   Nucleic Acids Res 16 (22), 10916 (1988)
   PUBMED   2849755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105328.13.
            
            Summary: Cytochrome c oxidase, the terminal enzyme of the
            mitochondrial respiratory chain, catalyzes the electron transfer
            from reduced cytochrome c to oxygen. It is a heteromeric complex
            consisting of 3 catalytic subunits encoded by mitochondrial genes
            and multiple structural subunits encoded by nuclear genes. The
            mitochondrially-encoded subunits function in electron transfer, and
            the nuclear-encoded subunits may be involved in the regulation and
            assembly of the complex. This nuclear gene encodes subunit VIc,
            which has 77% amino acid sequence identity with mouse subunit VIc.
            This gene is up-regulated in prostate cancer cells. A pseudogene
            has been found on chromosomes 16p12. [provided by RefSeq, Jul
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA181749.1, SRR1660807.118684.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000520468.7/
                                                  ENSP00000428895.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..75
                     /product="cytochrome c oxidase subunit 6C"
                     /EC_number="7.1.1.9"
                     /note="cytochrome c oxidase subunit VIc preprotein;
                     cytochrome c oxidase polypeptide VIc; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=8650
     Region          6..74
                     /region_name="COX6C"
                     /note="Cytochrome c oxidase subunit VIc; pfam02937"
                     /db_xref="CDD:460756"
     Site            14..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P09669.2)"
     CDS             1..75
                     /gene="COX6C"
                     /coded_by="NM_004374.4:101..328"
                     /db_xref="CCDS:CCDS6284.1"
                     /db_xref="GeneID:1345"
                     /db_xref="HGNC:HGNC:2285"
                     /db_xref="MIM:124090"
ORIGIN      
        1 mapevlpkpr mrgllarrlr nhmavafvls lgvaalykfr vadqrkkaya dfyrnydvmk
       61 dfeemrkagi fqsvk
//
LOCUS       NP_001295099             804 aa            linear   PRI 20-NOV-2025
DEFINITION  AMP deaminase 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001295099 XP_005270809
VERSION     NP_001295099.1
DBSOURCE    REFSEQ: accession NM_001308170.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Flores-Mendez,M., Ohl,L., Roule,T., Zhou,Y., Tintos-Hernandez,J.A.,
            Walsh,K., Ortiz-Gonzalez,X.R. and Akizu,N.
  TITLE     IMPDH2 filaments protect from neurodegeneration in AMPD2 deficiency
  JOURNAL   EMBO Rep 25 (9), 3990-4012 (2024)
   PUBMED   39075237
  REMARK    GeneRIF: IMPDH2 filaments protect from neurodegeneration in AMPD2
            deficiency.
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Gilboa,T., Elefant,N., Meiner,V. and Hacohen,N.
  TITLE     Delineating the phenotype and genetic basis of AMPD2-related
            pontocerebellar hypoplasia
  JOURNAL   Neurogenetics 24 (1), 61-66 (2023)
   PUBMED   36445597
  REMARK    GeneRIF: Delineating the phenotype and genetic basis of
            AMPD2-related pontocerebellar hypoplasia.
REFERENCE   4  (residues 1 to 804)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 804)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 804)
  AUTHORS   Van den Bergh,F. and Sabina,R.L.
  TITLE     Characterization of human AMP deaminase 2 (AMPD2) gene expression
            reveals alternative transcripts encoding variable N-terminal
            extensions of isoform L
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 401-410 (1995)
   PUBMED   8526848
REFERENCE   7  (residues 1 to 804)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 804)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   9  (residues 1 to 804)
  AUTHORS   Mahnke-Zizelman,D.K. and Sabina,R.L.
  TITLE     Cloning of human AMP deaminase isoform E cDNAs. Evidence for a
            third AMPD gene exhibiting alternatively spliced 5'-exons
  JOURNAL   J Biol Chem 267 (29), 20866-20877 (1992)
   PUBMED   1400401
REFERENCE   10 (residues 1 to 804)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U16268.1, AK302939.1,
            BC007711.2 and BC030217.1.
            
            On Apr 28, 2015 this sequence version replaced XP_005270809.1.
            
            Summary: The protein encoded by this gene is important in purine
            metabolism by converting AMP to IMP. The encoded protein, which
            acts as a homotetramer, is one of three AMP deaminases found in
            mammals. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            lacks an exon in the 5' coding region compared to variant 4. This
            variant represents translation initiation at an alternate start
            codon compared to variant 4; the 5'-most initiation codon, as used
            in variant 4, is associated with a truncated ORF that would render
            the transcript a candidate for nonsense-mediated decay (NMD). Leaky
            scanning may allow translation initiation at an alternate start
            codon to encode an isoform (5) that is shorter and has a distinct
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.99011.1,
                                           SRR1803614.271134.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..804
                     /product="AMP deaminase 2 isoform 5"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L);
                     AMP deaminase 2"
                     /calculated_mol_wt=92787
     Region          142..785
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..804
                     /gene="AMPD2"
                     /gene_synonym="AMPD; PCH9; SPG63"
                     /coded_by="NM_001308170.1:195..2609"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:271"
                     /db_xref="HGNC:HGNC:469"
                     /db_xref="MIM:102771"
ORIGIN      
        1 mwqsqapaga aqtpplsppw sqpwhpihla lasprpnipl rsgpacrppl qlqelftrsl
       61 aeselrsapy efpeespieq leerrqrler qisqdvklep dillrakqdf lktdsdsdlq
      121 lykeqgegqg drslrerdvl erefqrvtis geekcgvpft dlldaaksvv ralfirekym
      181 alslqsfcpt trrylqqlae kpletrtyeq gpdtpvsada pvhppaleqh pyehcepstm
      241 pgdlglglrm vrgvvhvytr repdehcsev elpypdlqef vadvnvlmal iingpiksfc
      301 yrrlqylssk fqmhvllnem kelaaqkkvp hrdfynirkv dthihasscm nqkhllrfik
      361 ramkrhleei vhveqgreqt lrevfesmnl taydlsvdtl dvhadrntfh rfdkfnakyn
      421 pigesvlrei fiktdnrvsg kyfahiikev msdleeskyq naelrlsiyg rsrdewdkla
      481 rwavmhrvhs pnvrwlvqvp rlfdvyrtkg qlanfqemle niflplfeat vhpashpelh
      541 lflehvdgfd svddeskpen hvfnlesplp eawveednpp yayylyytfa nmamlnhlrr
      601 qrgfhtfvlr phcgeagpih hlvsafmlae nishglllrk apvlqylyyl aqigiamspl
      661 snnslflsyh rnplpeylsr glmvslstdd plqfhftkep lmeeysiatq vwklsscdmc
      721 elarnsvlms gfshkvkshw lgpnytkegp egndirrtnv pdirvgyrye tlcqelalit
      781 qavqsemlet ipeeagitms pgpq
//
LOCUS       NP_001304850             233 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001304850 XP_011527264
VERSION     NP_001304850.1
DBSOURCE    REFSEQ: accession NM_001317921.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA488236.1, AL160175.5,
            BM554265.1, BX359456.2 and BC019307.1.
            
            On Dec 15, 2015 this sequence version replaced XP_011527264.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1, 3, 4 and 5 encode the same isoform
            (Bcl-X(L), also known as Bcl-xL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.408181.1,
                                           SRR7346977.1271049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001317921.2:342..1043"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     5"
                     /db_xref="CCDS:CCDS13189.1"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001303270             397 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 12 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001303270
VERSION     NP_001303270.1
DBSOURCE    REFSEQ: accession NM_001316341.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Lv,J., Ma,S., Wang,X., Dang,J. and Ma,F.
  TITLE     PSMD12 promotes non-small cell lung cancer progression through
            activating the Nrf2/TrxR1 pathway
  JOURNAL   Genes Genomics 46 (3), 263-277 (2024)
   PUBMED   38243044
  REMARK    GeneRIF: PSMD12 promotes non-small cell lung cancer progression
            through activating the Nrf2/TrxR1 pathway.
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Ma,J., Zhou,W., Yuan,Y., Wang,B. and Meng,X.
  TITLE     PSMD12 interacts with CDKN3 and facilitates pancreatic cancer
            progression
  JOURNAL   Cancer Gene Ther 30 (8), 1072-1083 (2023)
   PUBMED   37037907
  REMARK    GeneRIF: PSMD12 interacts with CDKN3 and facilitates pancreatic
            cancer progression.
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Zhang,H., Li,C., Liao,S., Tu,Y., Sun,S., Yao,F., Li,Z. and Wang,Z.
  TITLE     PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer
  JOURNAL   Cancer Biol Ther 23 (1), 1-11 (2022)
   PUBMED   36137220
  REMARK    GeneRIF: PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer.
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Saito,A., Watanabe,T.K., Shimada,Y., Fujiwara,T., Slaughter,C.A.,
            DeMartino,G.N., Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p44.5 and p55, two
            regulatory subunits of the 26S proteasome
  JOURNAL   Gene 203 (2), 241-250 (1997)
   PUBMED   9426256
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Kanayama,H.O., Tamura,T., Ugai,S., Kagawa,S., Tanahashi,N.,
            Yoshimura,T., Tanaka,K. and Ichihara,A.
  TITLE     Demonstration that a human 26S proteolytic complex consists of a
            proteasome and multiple associated protein components and
            hydrolyzes ATP and ubiquitin-ligated proteins by closely linked
            mechanisms
  JOURNAL   Eur J Biochem 206 (2), 567-578 (1992)
   PUBMED   1317798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC366628.1, AC110921.9,
            BC065826.1 and BU616916.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. A pseudogene has been
            identified on chromosome 3. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065826.1, SRR14038195.2272866.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..397
                     /product="26S proteasome non-ATPase regulatory subunit 12
                     isoform 3"
                     /note="26S proteasome regulatory subunit p55; 26S
                     proteasome regulatory subunit RPN5; proteasome (prosome,
                     macropain) 26S subunit, non-ATPase, 12"
                     /calculated_mol_wt=46281
     Region          3..397
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     CDS             1..397
                     /gene="PSMD12"
                     /gene_synonym="p55; Rpn5; STISS"
                     /coded_by="NM_001316341.2:520..1713"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5718"
                     /db_xref="HGNC:HGNC:9557"
                     /db_xref="MIM:604450"
ORIGIN      
        1 mvstsrilva vvkmcyeake wdllneniml lskrrsqlkq avakmvqqcc tyveeitdlp
       61 iklrlidtlr mvtegkiyve ierarltktl atikeqngdv keaasilqel qvetygsmek
      121 kervefileq mrlclavkdy irtqiiskki ntkffqeent eklklkyynl miqldqhegs
      181 ylsickhyra iydtpciqae sekwqqalks vvlyvilapf dneqsdlvhr isgdkkleei
      241 pkykdllklf ttmelmrwst lvedygmelr kgslespatd vfgsteegek rwkdlknrvv
      301 ehnirimaky ytritmkrma qlldlsvdes eaflsnlvvn ktifakvdrl agiinfqrpk
      361 dpnnllndws qklnslmslv nktthliake emihnlq
//
LOCUS       NP_775840               1347 aa            linear   PRI 20-NOV-2025
DEFINITION  ubinuclein-2 [Homo sapiens].
ACCESSION   NP_775840 XP_376679 XP_379933 XP_944191
VERSION     NP_775840.3
DBSOURCE    REFSEQ: accession NM_173569.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1347)
  AUTHORS   Xie,Y., Tan,L., Wu,K., Li,D. and Li,C.
  TITLE     MiR-455-3p mediates PPARalpha through UBN2 to promote apoptosis and
            autophagy in acute myeloid leukemia cells
  JOURNAL   Exp Hematol 128, 77-88 (2023)
   PUBMED   37805161
  REMARK    GeneRIF: MiR-455-3p mediates PPARalpha through UBN2 to promote
            apoptosis and autophagy in acute myeloid leukemia cells.
REFERENCE   2  (residues 1 to 1347)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1347)
  AUTHORS   Ray-Gallet,D., Ricketts,M.D., Sato,Y., Gupta,K., Boyarchuk,E.,
            Senda,T., Marmorstein,R. and Almouzni,G.
  TITLE     Functional activity of the H3.3 histone chaperone complex HIRA
            requires trimerization of the HIRA subunit
  JOURNAL   Nat Commun 9 (1), 3103 (2018)
   PUBMED   30082790
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1347)
  AUTHORS   Pieragostino,D., Agnifili,L., Fasanella,V., D'Aguanno,S.,
            Mastropasqua,R., Di Ilio,C., Sacchetta,P., Urbani,A. and Del
            Boccio,P.
  TITLE     Shotgun proteomics reveals specific modulated protein patterns in
            tears of patients with primary open angle glaucoma naive to therapy
  JOURNAL   Mol Biosyst 9 (6), 1108-1116 (2013)
   PUBMED   23580065
REFERENCE   5  (residues 1 to 1347)
  AUTHORS   Banumathy,G., Somaiah,N., Zhang,R., Tang,Y., Hoffmann,J.,
            Andrake,M., Ceulemans,H., Schultz,D., Marmorstein,R. and Adams,P.D.
  TITLE     Human UBN1 is an ortholog of yeast Hpc2p and has an essential role
            in the HIRA/ASF1a chromatin-remodeling pathway in senescent cells
  JOURNAL   Mol Cell Biol 29 (3), 758-770 (2009)
   PUBMED   19029251
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009220.10, AI239540.1, AK125956.1, AI803206.1 and BM673408.1.
            
            On May 13, 2009 this sequence version replaced NP_775840.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK125956.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000473989.8/ ENSP00000418648.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..1347
                     /product="ubinuclein-2"
                     /calculated_mol_wt=145958
     Region          1..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          194..245
                     /region_name="HUN"
                     /note="HPC2 and ubinuclein domain; pfam08729"
                     /db_xref="CDD:462581"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          250..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80WC1; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80WC1; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80WC1; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          448..662
                     /region_name="UBN_AB"
                     /note="Ubinuclein conserved middle domain; pfam14075"
                     /db_xref="CDD:464081"
     Region          573..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          707..740
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          815..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          880..913
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          981..1006
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Region          1035..1218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            1068
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q80WC1; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     Site            1148
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6ZU65.2)"
     CDS             1..1347
                     /gene="UBN2"
                     /coded_by="NM_173569.4:249..4292"
                     /db_xref="CCDS:CCDS43655.2"
                     /db_xref="GeneID:254048"
                     /db_xref="HGNC:HGNC:21931"
                     /db_xref="MIM:613841"
ORIGIN      
        1 maeprrvafi slspvrrrea eypgperepe yprepprlep qpyreparae ppaprepapr
       61 sdaqppsrek plpqrevsra eppmslqrep prpeppppfp plplqppppr esasraeqpp
      121 rppretvrle lvlkdptdes cvefsypell lcgeqrkkli htedpfndeh qerqevemla
      181 kkfemkyggk prkhrkdrlq dlidigfgyd etdpfidnse aydelvpasl ttkyggfyin
      241 tgtlqfrqas dteedditdn qkhkppkvpk ikeddiemkk rkrkeegeke kkprkkvpkq
      301 lgvvalnshk sekkkkrykd slslaamirk fqkekdalkk esnpkvpvtl stpslnkppc
      361 aaaalgndvp dlnlssgdpd lpifvstneh elfqeaenal emlddfdfdr lldaasdgsp
      421 lsesggengt ttqptytsqv mpkvvptlpe glpvllekri edlrvaaklf deegrkkfft
      481 qdmnnilldi elqlqelgpv irsgvyshle afvpcnketl vkrlkklhln vqddrlrepl
      541 qklklavsnv mpeqlfkyqe dcqarsqakc aklqtdeere kngseeddde kpgkrvigpr
      601 kkfhwddtir tllcnlveik lgcyelepnk sqsaedylks fmetevkplw pkgwmqarml
      661 fkesrsvhnh ltsapakkkv ipapkpkvke vmvktlplhs fptmlkecsp kkdqktptsl
      721 vasvsgppts sstaaiaaas sssapaqeti clddsldedl sfhspsldlv sealavinng
      781 nkgppvgsri smpttkprpg lreeklasim sklplatpkk ldstqtthss sliaghtgpv
      841 pkkpqdlaht gissgliags siqnpkvsle plparllqqg lqrssqihts sssqthvsss
      901 sqaqiaassh algtseaqda ssltqvtkvh qhsavqqnyv splqatisks qtnpvvklsn
      961 npqlscsssl iktsdkplmy rlplstpspg ngsqgshplv srtvpsttts snylakamvs
     1021 qistqgfksp fsmaaspkla aspkpatspk plpspkpsas pkpslsakps vstklisksn
     1081 ptpkptvsps ssspnalvaq gshsstnspv hkqpsgmnis rqsptlnllp ssrtsglppt
     1141 knlqapsklt nssstgtvgk nslsgiamnv pasrgsnlns sganrtslsg gtgsgtqgat
     1201 kplstphrps tasgssvvta svqstagasl lanaspltlm tsplsvtnqn vtpfgmlggl
     1261 vpvtmpfqfp leifgfgtdt agvtttsgst saafhhsltq nllkglqpgg aqhaatlshs
     1321 plpahlqqaf hdggqskgdt klprksq
//
LOCUS       NP_001354461             510 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 25 [Homo sapiens].
ACCESSION   NP_001354461 XP_016872222
VERSION     NP_001354461.1
DBSOURCE    REFSEQ: accession NM_001367532.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872222.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.297217.1,
                                           SRR3476690.48584.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..510
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 25"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=57361
     Region          12..295
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..22,33,35,66,82..85,89,91,127..128,130,132..133,
                     135,148..149,152,167..171,173)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..22,33,35,66,82..85,89,132..133,135,148..149)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(89,91,127..128,130,132,152,167..171,173)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(148..158,161..171)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(286,288..295)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          378..505
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..510
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367532.1:95..1627"
                     /note="isoform 25 is encoded by transcript variant 25"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkcvkktstq eyaakiintk klsardhqkl erearicrll
       61 khpnivrlhd siseegfhyl vfdlvtggel fedivareyy seadashcih qilesvnhih
      121 qhdivhrdlk penlllaskc kgaavkladf glaievqgeq qawfgfagtp gylspevlrk
      181 dpygkpvdiw acgvilyill vgyppfwded qhklyqqika gaydfpspew dtvtpeaknl
      241 inqmltinpa kritadqalk hpwvcqrstv asmmhrqetv eclrkfnarr klkgailttm
      301 lvsrnfsaak sllnkksdgg vkpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik
      361 gstescnttt ededlkvrkq eiikiteqli eainngdfea ytkicdpglt sfepealgnl
      421 vegmdfhkfy fenllsknsk pihttilnph vhvigedaac iayirltqyi dgqgrprtsq
      481 seetrvwhrr dgkwlnvhyh csgapaaplq
//
LOCUS       NP_001035959            1091 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 12 member 6 isoform c [Homo sapiens].
ACCESSION   NP_001035959
VERSION     NP_001035959.1
DBSOURCE    REFSEQ: accession NM_001042494.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Loseth,S., Hoyer,H., Le,K.M., Delpire,E., Kinge,E., Lande,A.,
            Hilmarsen,H.T., Fagerheim,T., Nilssen,O. and Braathen,G.J.
  TITLE     Late-onset sensory-motor axonal neuropathy, a novel SLC12A6-related
            phenotype
  JOURNAL   Brain 146 (3), 912-922 (2023)
   PUBMED   36542484
  REMARK    GeneRIF: Late-onset sensory-motor axonal neuropathy, a novel
            SLC12A6-related phenotype.
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Ando,M., Higuchi,Y., Yuan,J., Yoshimura,A., Taniguchi,T., Takei,J.,
            Takeuchi,M., Hiramatsu,Y., Shimizu,F., Kubota,M., Takeshima,A.,
            Ueda,T., Koh,K., Nagaoka,U., Tokashiki,T., Sawai,S., Sakiyama,Y.,
            Hashiguchi,A., Sato,R., Kanda,T., Okamoto,Y. and Takashima,H.
  TITLE     Novel heterozygous variants of SLC12A6 in Japanese families with
            Charcot-Marie-Tooth disease
  JOURNAL   Ann Clin Transl Neurol 9 (7), 902-911 (2022)
   PUBMED   35733399
  REMARK    GeneRIF: Novel heterozygous variants of SLC12A6 in Japanese
            families with Charcot-Marie-Tooth disease.
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Bogdanova-Mihaylova,P., McNamara,P., Burton-Jones,S. and
            Murphy,S.M.
  TITLE     Expanding the phenotype of SLC12A6-associated sensorimotor
            neuropathy
  JOURNAL   BMJ Case Rep 14 (10), e244641 (2021)
   PUBMED   34706912
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Chi,G., Ebenhoch,R., Man,H., Tang,H., Tremblay,L.E., Reggiano,G.,
            Qiu,X., Bohstedt,T., Liko,I., Almeida,F.G., Garneau,A.P., Wang,D.,
            McKinley,G., Moreau,C.P., Bountra,K.D., Abrusci,P.,
            Mukhopadhyay,S.M.M., Fernandez-Cid,A., Slimani,S., Lavoie,J.L.,
            Burgess-Brown,N.A., Tehan,B., DiMaio,F., Jazayeri,A., Isenring,P.,
            Robinson,C.V. and Durr,K.L.
  TITLE     Phospho-regulation, nucleotide binding and ion access control in
            potassium-chloride cotransporters
  JOURNAL   EMBO J 40 (14), e107294 (2021)
   PUBMED   34031912
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
            Chernova,M.N., Brugnara,C. and Alper,S.L.
  TITLE     A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
            and C-terminal cytoplasmic domains are required for K-Cl
            cotransport activity
  JOURNAL   J Biol Chem 276 (45), 41870-41878 (2001)
   PUBMED   11551954
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Race,J.E., Makhlouf,F.N., Logue,P.J., Wilson,F.H., Dunham,P.B. and
            Holtzman,E.J.
  TITLE     Molecular cloning and functional characterization of KCC3, a new
            K-Cl cotransporter
  JOURNAL   Am J Physiol 277 (6), C1210-C1219 (1999)
   PUBMED   10600773
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
            and Gamba,G.
  TITLE     Cloning and characterization of KCC3 and KCC4, new members of the
            cation-chloride cotransporter gene family
  JOURNAL   J Biol Chem 274 (23), 16355-16362 (1999)
   PUBMED   10347194
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Hiki,K., D'Andrea,R.J., Furze,J., Crawford,J., Woollatt,E.,
            Sutherland,G.R., Vadas,M.A. and Gamble,J.R.
  TITLE     Cloning, characterization, and chromosomal location of a novel
            human K+-Cl- cotransporter
  JOURNAL   J Biol Chem 274 (15), 10661-10667 (1999)
   PUBMED   10187864
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Gauvreau,C., Brisson,J.D. and Dupre,N.
  TITLE     Hereditary Motor and Sensory Neuropathy with Agenesis of the Corpus
            Callosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021822.21, AF531259.1 and
            AC079203.9.
            
            Summary: This gene is a member of the K-Cl cotransporter (KCC)
            family. K-Cl cotransporters are integral membrane proteins that
            lower intracellular chloride concentrations below the
            electrochemical equilibrium potential. The proteins encoded by this
            gene are activated by cell swelling induced by hypotonic
            conditions. Alternate splicing results in multiple transcript
            variants encoding different isoforms. Mutations in this gene are
            associated with agenesis of the corpus callosum with peripheral
            neuropathy. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) has an additional exon in its
            5' UTR and uses an alternate in-frame splice site in the first
            protein coding exon, compared to variant 1. The encoded protein
            (isoform c) uses a downstream start codon, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF531259.1, AF477977.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..1091
                     /product="solute carrier family 12 member 6 isoform c"
                     /note="potassium chloride cotransporter 3; potassium
                     chloride cotransporter KCC3a-S3; potassium-chloride
                     transporter-3a; potassium-chloride transporter-3b; K-Cl
                     cotransporter 3; electroneutral potassium-chloride
                     cotransporter 3; solute carrier family 12
                     (potassium/chloride transporters), member 6; solute
                     carrier family 12 (potassium/chloride transporter), member
                     6"
                     /calculated_mol_wt=120994
     Region          50..1091
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     CDS             1..1091
                     /gene="SLC12A6"
                     /gene_synonym="ACCPN; CMT2II; KCC3; KCC3A; KCC3B"
                     /coded_by="NM_001042494.2:549..3824"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42012.1"
                     /db_xref="GeneID:9990"
                     /db_xref="HGNC:HGNC:10914"
                     /db_xref="MIM:604878"
ORIGIN      
        1 msemsgatts latvaldpps drtshpqdvi edlsqnsitg ehsqllddgh kkarnaylnn
       61 snyeegdeyf dknlalfeee mdtrpkvssl lnrmanytnl tqgakeheea enitegkkkp
      121 tktpqmgtfm gvylpclqni fgvilflrlt wvvgtagvlq afaivliccc ctmltaisms
      181 aiatngvvpa ggsyfmisra lgpefggavg lcfylgttfa aamyilgaie iflvyivpra
      241 aifhsddalk esaamlnnmr vygtaflvlm vlvvfigvry vnkfaslfla cvivsilaiy
      301 agaikssfap phfpvcmlgn rtlssrhidv csktkeinnm tvpsklwgff cnssqffnat
      361 cdeyfvhnnv tsiqgipgla sgiitenlws nylpkgeiie kpsakssdvl gslnheyvlv
      421 dittsftllv giffpsvtgi magsnrsgdl kdaqksipig tilailttsf vylsnvvlfg
      481 aciegvvlrd kfgdavkgnl vvgtlswpsp wvivigsffs tcgaglqslt gaprllqaia
      541 kdniipflrv fghskangep twallltaai aelgiliasl dlvapilsmf flmcylfvnl
      601 acalqtllrt pnwrprfryy hwalsfmgms iclalmfiss wyyaivamvi agmiykyiey
      661 qgaekewgdg irglslsaar fallrleegp phtknwrpql lvllkldedl hvkhprlltf
      721 asqlkagkgl tivgsvivgn flenygeala aeqtikhlme aekvkgfcql vvaaklregi
      781 shliqscglg gmkhntvvmg wpngwrqsed arawktfigt vrvttaahla llvaknisff
      841 psnveqfseg nidvwwivhd ggmlmllpfl lkqhkvwrkc siriftvaql ednsiqmkkd
      901 latflyhlri eaevevvemh dsdisaytye rtlmmeqrsq mlrhmrlskt erdreaqlvk
      961 drnsmlrlts igsdedeete tyqekvhmtw tkdkymasrg qkaksmegfq dllnmrpdqs
     1021 nvrrmhtavk lnevivnksh eaklvllnmp gpprnpegde nymeflevlt eglervllvr
     1081 gggsevitiy s
//
LOCUS       NP_060213                782 aa            linear   PRI 20-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_060213
VERSION     NP_060213.2
DBSOURCE    REFSEQ: accession NM_017743.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC412877.1, AK000290.1,
            AC105129.4 and BU753778.1.
            
            On Jan 31, 2002 this sequence version replaced NP_060213.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks two exons in the 3'
            coding region compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.179516.1,
                                           SRR1660803.213922.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..782
                     /product="dipeptidyl peptidase 8 isoform 2"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=89777
     Region          1..146
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          159..579
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          <657..775
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..782
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_017743.6:216..2564"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10209.1"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 maaameteql gveifetadc eeniesqdrp klepfyvery swsqlkklla dtrkyhgymm
       61 akaphdfmfv krndpdgphs driyylamsg enrentlfys eipktinraa vlmlswkpll
      121 dlfqatldyg mysreeellr erkrigtvgi asydyhqgsg tflfqagsgi yhvkdggpqg
      181 ftqqplrpnl vetscpnirm dpklcpadpd wiafihsndi wisnivtree rrltyvhnel
      241 anmeedarsa gvatfvlqee fdrysgywwc pkaettpsgg kilrilyeen deseveiihv
      301 tspmletrra dsfrypktgt anpkvtfkms eimidaegri idvidkeliq pfeilfegve
      361 yiaragwtpe gkyawsilld rsqtrlqivl ispelfipve ddvmerqrli esvpdsvtpl
      421 iiyeettdiw inihdifhvf pqsheeeief ifasecktgf rhlykitsil keskykrssg
      481 glpapsdfkc pikeeiaits gewevlgrhg sniqvdevrr lvyfegtkds plehhlyvvs
      541 yvnpgevtrl tdrgyshscc isqhcdffis kysnqknphc vslyklsspe ddptcktkef
      601 watildsagp lpdytppeif sfesttgftl ygmlykphdl qpgkkyptvl fiyggpqvai
      661 agapvtlwif ydtgyterym ghpdqneqgy ylgsvamqae kfpsepnrll llhgfldenv
      721 hfahtsills flvragkpyd lqiypqerhs irvpesgehy elhllhylqe nlgsriaalk
      781 vi
//
LOCUS       NP_000190                502 aa            linear   PRI 20-NOV-2025
DEFINITION  N-sulfoglucosamine sulfohydrolase isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_000190
VERSION     NP_000190.1
DBSOURCE    REFSEQ: accession NM_000199.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Yi,F., Hong,X., Kumar,A.B., Zong,C., Boons,G.J., Scott,C.R.,
            Turecek,F., Robinson,B.H. and Gelb,M.H.
  TITLE     Detection of mucopolysaccharidosis III-A (Sanfilippo Syndrome-A) in
            dried blood spots (DBS) by tandem mass spectrometry
  JOURNAL   Mol Genet Metab 125 (1-2), 59-63 (2018)
   PUBMED   30006231
  REMARK    GeneRIF: Sulfamidase activity in 238 random newborns was well
            elevated compared to the range of activities measured in dried
            blood spots from 8 patients previously confirmed to have
            mucopolysaccharidosis III-A.
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Truxal,K.V., Fu,H., McCarty,D.M., McNally,K.A., Kunkler,K.L.,
            Zumberge,N.A., Martin,L., Aylward,S.C., Alfano,L.N., Berry,K.M.,
            Lowes,L.P., Corridore,M., McKee,C., McBride,K.L. and Flanigan,K.M.
  TITLE     A prospective one-year natural history study of
            mucopolysaccharidosis types IIIA and IIIB: Implications for
            clinical trial design
  JOURNAL   Mol Genet Metab 119 (3), 239-248 (2016)
   PUBMED   27590925
  REMARK    GeneRIF: CSF enzyme activity levels for either SGSH (in MPS IIIA
            subjects) or NAGLU (in MPS IIIB) significantly differed from normal
            controls. Several other behavioral or functional measures were
            found to be uninformative in this population, including timed
            functional motor tests.
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Wilkin,J., Kerr,N.C., Byrd,K.W., Ward,J.C. and Iannaccone,A.
  TITLE     Characterization of a Case of Pigmentary Retinopathy in Sanfilippo
            Syndrome Type IIIA Associated with Compound Heterozygous Mutations
            in the SGSH Gene
  JOURNAL   Ophthalmic Genet 37 (2), 217-227 (2016)
   PUBMED   26331342
  REMARK    GeneRIF: We have identified ocular features of a patient with
            Sanfilippo syndrome type IIIA harboring a novel SGHS mutation that
            were not previously known to occur in this disease - namely, a
            progressive retinopathy with distinctive features, cystic macular
            changes responsive to carbonic anhydrase inhibitors, and complex
            electroretinographic abnormalities consistent with postreceptoral
            dysfunction.
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Blanch,L., Weber,B., Guo,X.H., Scott,H.S. and Hopwood,J.J.
  TITLE     Molecular defects in Sanfilippo syndrome type A
  JOURNAL   Hum Mol Genet 6 (5), 787-791 (1997)
   PUBMED   9158154
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Karageorgos,L.E., Guo,X.H., Blanch,L., Weber,B., Anson,D.S.,
            Scott,H.S. and Hopwood,J.J.
  TITLE     Structure and sequence of the human sulphamidase gene
  JOURNAL   DNA Res 3 (4), 269-271 (1996)
   PUBMED   8946167
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Scott,H.S., Blanch,L., Guo,X.H., Freeman,C., Orsborn,A., Baker,E.,
            Sutherland,G.R., Morris,C.P. and Hopwood,J.J.
  TITLE     Cloning of the sulphamidase gene and identification of mutations in
            Sanfilippo A syndrome
  JOURNAL   Nat Genet 11 (4), 465-467 (1995)
   PUBMED   7493035
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Wagner,V.F. and Northrup,H.
  TITLE     Mucopolysaccharidosis Type III
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31536183
REFERENCE   10 (residues 1 to 502)
  AUTHORS   van de Kamp,J.J., Niermeijer,M.F., von Figura,K. and Giesberts,M.A.
  TITLE     Genetic heterogeneity and clinical variability in the Sanfilippo
            syndrome (types A, B, and C)
  JOURNAL   Clin Genet 20 (2), 152-160 (1981)
   PUBMED   6796310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC319407.1, U30894.1,
            BU685248.1 and BP198470.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the enzyme sulfamidase; one of several
            enzymes involved in the lysosomal degradation of heparan sulfate.
            Mutations in this gene are associated with the lysosomal storage
            disease mucopolysaccaridosis IIIA, also known as Sanfilippo
            syndrome A, which results from impaired degradation of heparan
            sulfate. Transcripts of varying sizes have been reported but their
            biological validity has not been determined. [provided by RefSeq,
            Jun 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.229971.1, BC047318.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326317.11/ ENSP00000314606.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..502
                     /product="N-sulfoglucosamine sulfohydrolase isoform 1
                     precursor"
                     /EC_number="3.10.1.1"
                     /note="heparan sulfate sulfatase; sulfoglucosamine
                     sulfamidase; sulphamidase; mucopolysaccharidosis type
                     IIIA"
                     /calculated_mol_wt=54680
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2034
     mat_peptide     21..502
                     /product="N-sulphoglucosamine sulphohydrolase.
                     /id=PRO_0000033433"
                     /note="propagated from UniProtKB/Swiss-Prot (P51688.1)"
                     /calculated_mol_wt=54680
     Region          24..472
                     /region_name="SGSH"
                     /note="N-sulfoglucosamine sulfohydrolase (SGSH;
                     sulfamidase); cd16027"
                     /db_xref="CDD:293751"
     Site            order(31..32,70,123,125,181,273..274)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293751"
     Site            order(31..32,70,123,125,181,274)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293751"
     Site            41
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24816101,
                     ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV; propagated
                     from UniProtKB/Swiss-Prot (P51688.1)"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P51688.1)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:24816101,
                     ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV; propagated
                     from UniProtKB/Swiss-Prot (P51688.1)"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
                     ECO:0007744|PDB:4MIV; propagated from UniProtKB/Swiss-Prot
                     (P51688.1)"
     Site            order(367,390..391)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:293751"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
                     ECO:0007744|PDB:4MIV; propagated from UniProtKB/Swiss-Prot
                     (P51688.1)"
     CDS             1..502
                     /gene="SGSH"
                     /gene_synonym="HSS; MPS3A; SFMD"
                     /coded_by="NM_000199.5:21..1529"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11770.1"
                     /db_xref="GeneID:6448"
                     /db_xref="HGNC:HGNC:10818"
                     /db_xref="MIM:605270"
ORIGIN      
        1 mscpvpacca lllvlglcra rprnalllla ddggfesgay nnsaiatphl dalarrsllf
       61 rnaftsvssc spsraslltg lpqhqngmyg lhqdvhhfns fdkvrslpll lsqagvrtgi
      121 igkkhvgpet vypfdfayte engsvlqvgr nitrikllvr kflqtqddrp fflyvafhdp
      181 hrcghsqpqy gtfcekfgng esgmgripdw tpqaydpldv lvpyfvpntp aaradlaaqy
      241 ttvgrmdqgv glvlqelrda gvlndtlvif tsdngipfps grtnlywpgt aepllvsspe
      301 hpkrwgqvse ayvslldltp tildwfsipy psyaifgskt ihltgrsllp aleaeplwat
      361 vfgsqshhev tmsypmrsvq hrhfrlvhnl nfkmpfpidq dfyvsptfqd llnrttagqp
      421 tgwykdlrhy yyrarwelyd rsrdphetqn latdprfaql lemlrdqlak wqwethdpwv
      481 capdgvleek lspqcqplhn el
//
LOCUS       NP_001009552             309 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A catalytic subunit beta
            isoform [Homo sapiens].
ACCESSION   NP_001009552
VERSION     NP_001009552.1
DBSOURCE    REFSEQ: accession NM_001009552.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Jun,G.R., You,Y., Zhu,C., Meng,G., Chung,J., Panitch,R., Hu,J.,
            Xia,W., Bennett,D.A., Foroud,T.M., Wang,L.S., Haines,J.L.,
            Mayeux,R., Pericak-Vance,M.A., Schellenberg,G.D., Au,R.,
            Lunetta,K.L., Ikezu,T., Stein,T.D. and Farrer,L.A.
  CONSRTM   Alzheimer's Disease Genetics Consortium
  TITLE     Protein phosphatase 2A and complement component 4 are linked to the
            protective effect of APOE varepsilon2 for Alzheimer's disease
  JOURNAL   Alzheimers Dement 18 (11), 2042-2054 (2022)
   PUBMED   35142023
  REMARK    GeneRIF: Protein phosphatase 2A and complement component 4 are
            linked to the protective effect of APOE varepsilon2 for Alzheimer's
            disease.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Sergienko,N.M., Donner,D.G., Delbridge,L.M.D., McMullen,J.R. and
            Weeks,K.L.
  TITLE     Protein phosphatase 2A in the healthy and failing heart: New
            insights and therapeutic opportunities
  JOURNAL   Cell Signal 91, 110213 (2022)
   PUBMED   34902541
  REMARK    GeneRIF: Protein phosphatase 2A in the healthy and failing heart:
            New insights and therapeutic opportunities.
            Review article
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Goedert,M., Cohen,E.S., Jakes,R. and Cohen,P.
  TITLE     p42 MAP kinase phosphorylation sites in microtubule-associated
            protein tau are dephosphorylated by protein phosphatase 2A1.
            Implications for Alzheimer's disease [corrected]
  JOURNAL   FEBS Lett 312 (1), 95-99 (1992)
   PUBMED   1330687
  REMARK    Erratum:[FEBS Lett 1992 Nov 23;313(2):203]
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Khew-Goodall,Y., Mayer,R.E., Maurer,F., Stone,S.R. and
            Hemmings,B.A.
  TITLE     Structure and transcriptional regulation of protein phosphatase 2A
            catalytic subunit genes
  JOURNAL   Biochemistry 30 (1), 89-97 (1991)
   PUBMED   1846293
  REMARK    Erratum:[Biochemistry 1991 May 28;30(21):5328]
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Pallas,D.C., Shahrik,L.K., Martin,B.L., Jaspers,S., Miller,T.B.,
            Brautigan,D.L. and Roberts,T.M.
  TITLE     Polyoma small and middle T antigens and SV40 small t antigen form
            stable complexes with protein phosphatase 2A
  JOURNAL   Cell 60 (1), 167-176 (1990)
   PUBMED   2153055
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Virshup,D.M., Kauffman,M.G. and Kelly,T.J.
  TITLE     Activation of SV40 DNA replication in vitro by cellular protein
            phosphatase 2A
  JOURNAL   EMBO J 8 (12), 3891-3898 (1989)
   PUBMED   2555176
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Arino,J., Woon,C.W., Brautigan,D.L., Miller,T.B. Jr. and
            Johnson,G.L.
  TITLE     Human liver phosphatase 2A: cDNA and amino acid sequence of two
            catalytic subunit isotypes
  JOURNAL   Proc Natl Acad Sci U S A 85 (12), 4252-4256 (1988)
   PUBMED   2837763
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG716837.1, CF594136.1,
            AC009314.4, BC012022.1 and CA419001.1.
            
            Summary: This gene encodes the phosphatase 2A catalytic subunit.
            Protein phosphatase 2A is one of the four major Ser/Thr
            phosphatases, and it is implicated in the negative control of cell
            growth and division. It consists of a common heteromeric core
            enzyme, which is composed of a catalytic subunit and a constant
            regulatory subunit, that associates with a variety of regulatory
            subunits. This gene encodes a beta isoform of the catalytic
            subunit. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012022.1, X12656.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221138.9/ ENSP00000221138.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..309
                     /product="serine/threonine-protein phosphatase 2A
                     catalytic subunit beta isoform"
                     /EC_number="3.1.3.16"
                     /note="PP2A-beta; protein phosphatase type 2A catalytic
                     subunit; protein phosphatase 2, catalytic subunit, beta
                     isozyme; testicular tissue protein Li 146"
                     /calculated_mol_wt=35444
     Region          9..293
                     /region_name="MPP_PP2A_PP4_PP6"
                     /note="PP2A, PP4, and PP6 phosphoprotein phosphatases,
                     metallophosphatase domain; cd07415"
                     /db_xref="CDD:277360"
     Site            order(51,67,70..71,73..74,76,78..79,91,106..110,121..122,
                     125..126,130..131,134..135,143,268,277,287,293)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:277360"
     Site            order(57,59,85,89,117..118,122..123,127,167,189..191,200,
                     213..215,241,243,267..269)
                     /site_type="active"
                     /db_xref="CDD:277360"
     Site            order(57,59,85,117,167,241)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277360"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P62715; propagated from
                     UniProtKB/Swiss-Prot (P62714.1)"
     Site            309
                     /site_type="methylation"
                     /note="Leucine methyl ester.
                     /evidence=ECO:0000269|PubMed:8206937; propagated from
                     UniProtKB/Swiss-Prot (P62714.1)"
     CDS             1..309
                     /gene="PPP2CB"
                     /gene_synonym="PP2Abeta; PP2CB"
                     /coded_by="NM_001009552.2:398..1327"
                     /db_xref="CCDS:CCDS6079.1"
                     /db_xref="GeneID:5516"
                     /db_xref="HGNC:HGNC:9300"
                     /db_xref="MIM:176916"
ORIGIN      
        1 mddkaftkel dqwveqlnec kqlnenqvrt lcekakeilt kesnvqevrc pvtvcgdvhg
       61 qfhdlmelfr iggkspdtny lfmgdyvdrg yysvetvtll valkvryper itilrgnhes
      121 rqitqvygfy declrkygna nvwkyftdlf dylpltalvd gqifclhggl spsidtldhi
      181 raldrlqevp hegpmcdllw sdpddrggwg isprgagytf gqdisetfnh angltlvsra
      241 hqlvmegynw chdrnvvtif sapnycyrcg nqaaimeldd tlkysflqfd paprrgephv
      301 trrtpdyfl
//
LOCUS       NP_001317143             273 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 16 isoform 2 [Homo sapiens].
ACCESSION   NP_001317143 XP_011510369
VERSION     NP_001317143.1
DBSOURCE    REFSEQ: accession NM_001330214.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Zhu,Z., Xiang,Q., Li,S., Chen,C. and Shi,J.
  TITLE     Serine/Threonine kinase 16 phosphorylates STAT3 and confers a
            JAK2-Inhibition resistance phenotype in triple-negative breast
            cancer
  JOURNAL   Biochem Pharmacol 225, 116268 (2024)
   PUBMED   38723720
  REMARK    GeneRIF: Serine/Threonine kinase 16 phosphorylates STAT3 and
            confers a JAK2-Inhibition resistance phenotype in triple-negative
            breast cancer.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Peng,L., Guangshi,L., Wusman,L.B. and Tao,L.
  TITLE     STK16 promoted colorectal cancer progress in a c-MYC
            signaling-dependent manner
  JOURNAL   Mol Med 30 (1), 50 (2024)
   PUBMED   38622518
  REMARK    GeneRIF: STK16 promoted colorectal cancer progress in a c-MYC
            signaling-dependent manner.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Wang,X., Huang,R., Lu,Z., Wang,Z., Chen,X. and Huang,D.
  TITLE     Exosomes from M1-polarized macrophages promote apoptosis in lung
            adenocarcinoma via the miR-181a-5p/ETS1/STK16 axis
  JOURNAL   Cancer Sci 113 (3), 986-1001 (2022)
   PUBMED   35092121
  REMARK    GeneRIF: Exosomes from M1-polarized macrophages promote apoptosis
            in lung adenocarcinoma via the miR-181a-5p/ETS1/STK16 axis.
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Guinea,B., Ligos,J.M., Lain de Lera,T., Martin-Caballero,J.,
            Flores,J., Gonzalez de la Pena,M., Garcia-Castro,J. and Bernad,A.
  TITLE     Nucleocytoplasmic shuttling of STK16 (PKL12), a Golgi-resident
            serine/threonine kinase involved in VEGF expression regulation
  JOURNAL   Exp Cell Res 312 (2), 135-144 (2006)
   PUBMED   16310770
  REMARK    GeneRIF: The Endogenous STK16 subcellular localization was
            evaluated by indirect immunofluorescence in NRK cells,
            demonstrating a Golgi-associated pattern that appears to be
            independent of signals provided by integrin pathways.
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Ligos,J.M., de Lera,T.L., Hinderlich,S., Guinea,B., Sanchez,L.,
            Roca,R., Valencia,A. and Bernad,A.
  TITLE     Functional interaction between the Ser/Thr kinase PKL12 and
            N-acetylglucosamine kinase, a prominent enzyme implicated in the
            salvage pathway for GlcNAc recycling
  JOURNAL   J Biol Chem 277 (8), 6333-6343 (2002)
   PUBMED   11741987
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Ohta,S., Takeuchi,M., Deguchi,M., Tsuji,T., Gahara,Y. and Nagata,K.
  TITLE     A novel transcriptional factor with Ser/Thr kinase activity
            involved in the transforming growth factor (TGF)-beta signalling
            pathway
  JOURNAL   Biochem J 350 Pt 2 (Pt 2), 395-404 (2000)
   PUBMED   10947953
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Berson,A.E., Young,C., Morrison,S.L., Fujii,G.H., Sheung,J., Wu,B.,
            Bolen,J.B. and Burkhardt,A.L.
  TITLE     Identification and characterization of a myristylated and
            palmitylated serine/threonine protein kinase
  JOURNAL   Biochem Biophys Res Commun 259 (3), 533-538 (1999)
   PUBMED   10364453
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Ligos,J.M., Gerwin,N., Fernandez,P., Gutierrez-Ramos,J.C. and
            Bernad,A.
  TITLE     Cloning, expression analysis, and functional characterization of
            PKL12, a member of a new subfamily of ser/thr kinases
  JOURNAL   Biochem Biophys Res Commun 249 (2), 380-384 (1998)
   PUBMED   9712705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068946.4 and AK298471.1.
            
            On Aug 20, 2016 this sequence version replaced XP_011510369.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.16140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..273
                     /product="serine/threonine-protein kinase 16 isoform 2"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.10.2"
                     /note="protein kinase expressed in day 12 fetal liver;
                     serine/threonine-protein kinase 16; protein kinase PKL12;
                     TGF-beta-stimulated factor 1; myristoylated and
                     palmitoylated serine/threonine-protein kinase;
                     tyrosine-protein kinase STK16"
                     /calculated_mol_wt=30760
     Region          19..263
                     /region_name="STKc_16"
                     /note="Catalytic domain of Serine/Threonine Kinase 16;
                     cd13986"
                     /db_xref="CDD:270888"
     Site            order(26..30,34,47,49,78,98..101,105,107,148,150,152..153,
                     155,166,169)
                     /site_type="active"
                     /db_xref="CDD:270888"
     Site            order(26..30,34,47,49,78,98..101,105,148,150,152..153,155,
                     166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270888"
     CDS             1..273
                     /gene="STK16"
                     /gene_synonym="hPSK; KRCT; MPSK; PKL12; PSK; TSF1"
                     /coded_by="NM_001330214.1:105..926"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82573.1"
                     /db_xref="GeneID:8576"
                     /db_xref="HGNC:HGNC:11394"
                     /db_xref="MIM:604719"
ORIGIN      
        1 mghalcvcsr gtviidnkry lfiqklgegg fsyvdlvegl hdghfyalkr ilcheqqdre
       61 eaqreadmhr lfnhpnilrl vayclrerga kheawlllpf fkrgtlwnei erlkdkgnfl
      121 tedqilwlll gicrgleaih akgyahrdlk ptnillgdeg qpvlmdlgsm nqacihvegs
      181 rqaltlqslg cvlyammfge gpydmvfqkg dsvalavqnq lsipqsprhs salrqllnsm
      241 mtvdphqrph iplllsqlea lqppapgqht tqi
//
LOCUS       NP_055093                839 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock 70 kDa protein 4L isoform 1 [Homo sapiens].
ACCESSION   NP_055093
VERSION     NP_055093.2
DBSOURCE    REFSEQ: accession NM_014278.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Zhu,M., Huang,Y., Tang,J., Shao,S., Zhang,L., Zhou,Y., He,S. and
            Wang,Y.
  TITLE     Role of Apg-1 in HSF1 activation and bortezomib sensitivity in
            myeloma cells
  JOURNAL   Exp Hematol 81, 50-59 (2020)
   PUBMED   31899217
  REMARK    GeneRIF: Apg-1 knockdown sensitized myeloma cells to bortezomib
            treatment, which may provide a new approach in multiple myeloma
            treatment.
REFERENCE   3  (residues 1 to 839)
  AUTHORS   Liu,X., Wang,X. and Liu,F.
  TITLE     Decreased expression of heat shock protein A4L in spermatozoa is
            positively related to poor human sperm quality
  JOURNAL   Mol Reprod Dev 86 (4), 379-386 (2019)
   PUBMED   30637842
  REMARK    GeneRIF: decreased expression of HSPA4L in immature and
            asthenozoospermic spermatozoa was validated by western blot
            analysis. Functional analysis revealed a correlation between HSPA4L
            and sperm motility by Spearman correlation analysis and its
            involvement in sperm-oocyte penetration by the human sperm-hamster
            egg penetration test.
REFERENCE   4  (residues 1 to 839)
  AUTHORS   Wang,S., Mo,Y., Midorikawa,K., Zhang,Z., Huang,G., Ma,N., Zhao,W.,
            Hiraku,Y., Oikawa,S. and Murata,M.
  TITLE     The potent tumor suppressor miR-497 inhibits cancer phenotypes in
            nasopharyngeal carcinoma by targeting ANLN and HSPA4L
  JOURNAL   Oncotarget 6 (34), 35893-35907 (2015)
   PUBMED   26486082
  REMARK    GeneRIF: Findings indicate that miR-497 is a potent tumor
            suppressor that inhibits cancer phenotypes by targeting ANLN and
            HSPA4L in NPC.
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Kuo,Y., Ren,S., Lao,U., Edgar,B.A. and Wang,T.
  TITLE     Suppression of polyglutamine protein toxicity by co-expression of a
            heat-shock protein 40 and a heat-shock protein 110
  JOURNAL   Cell Death Dis 4 (10), e833 (2013)
   PUBMED   24091676
  REMARK    GeneRIF: HSP40 and HSP110 function together in protein homeostasis
            control.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Mala,J.G. and Takeuchi,S.
  TITLE     Molecular cloning of OSP94: A significant biomarker protein of
            hypertensive human heart and a member of HSP110 family
  JOURNAL   Mol Biotechnol 42 (2), 175-194 (2009)
   PUBMED   19169850
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Takahashi,H., Furukawa,T., Yano,T., Sato,N., Takizawa,J.,
            Kurasaki,T., Abe,T., Narita,M., Masuko,M., Koyama,S., Toba,K.,
            Takahashi,M. and Aizawa,Y.
  TITLE     Identification of an overexpressed gene, HSPA4L, the product of
            which can provoke prevalent humoral immune responses in leukemia
            patients
  JOURNAL   Exp Hematol 35 (7), 1091-1099 (2007)
   PUBMED   17588478
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Colgan,S.P., Pitman,R.S., Nagaishi,T., Mizoguchi,A., Mizoguchi,E.,
            Mayer,L.F., Shao,L., Sartor,R.B., Subjeck,J.R. and Blumberg,R.S.
  TITLE     Intestinal heat shock protein 110 regulates expression of CD1d on
            intestinal epithelial cells
  JOURNAL   J Clin Invest 112 (5), 745-754 (2003)
   PUBMED   12952923
  REMARK    GeneRIF: a novel autocrine pathway of CD1d regulation by Hsp110.
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Nonoguchi,K., Tokuchi,H., Okuno,H., Watanabe,H., Egawa,H.,
            Saito,K., Ogawa,O. and Fujita,J.
  TITLE     Expression of Apg-1, a member of the Hsp110 family, in the human
            testis and sperm
  JOURNAL   Int J Urol 8 (6), 308-314 (2001)
   PUBMED   11389747
REFERENCE   10 (residues 1 to 839)
  AUTHORS   Nonoguchi,K., Itoh,K., Xue,J.H., Tokuchi,H., Nishiyama,H.,
            Kaneko,Y., Tatsumi,K., Okuno,H., Tomiwa,K. and Fujita,J.
  TITLE     Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110
            family, and chromosomal assignment of their genes
  JOURNAL   Gene 237 (1), 21-28 (1999)
   PUBMED   10524232
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC040560.1, AC093591.3 and
            BM679019.1.
            
            On Jun 9, 2003 this sequence version replaced NP_055093.1.
            
            Summary: The protein encoded by this gene is heat shock inducible
            and may act as a chaperone. The encoded protein can protect the
            heat-shocked cell against the harmful effects of aggregated
            proteins. This gene is highly expressed in leukemia cells and may
            be a good target for therapeutic intervention. Several transcripts
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.69021.1,
                                           SRR1660803.246850.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296464.9/ ENSP00000296464.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..839
                     /product="heat shock 70 kDa protein 4L isoform 1"
                     /note="heat shock protein (hsp110 family); heat shock 70
                     kDa protein 4L; testis tissue sperm-binding protein Li
                     64n; heat shock 70 kDa protein 4-like protein; osmotic
                     stress protein 94; heat shock 70-related protein APG-1;
                     heat shock 70kDa protein 4-like; HSPA4-like protein;
                     heat-shock protein family A member 4-like protein; heat
                     shock protein family H member 3"
                     /calculated_mol_wt=94382
     Region          2..384
                     /region_name="ASKHA_NBD_HSP70_HSPA4L"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 4L (HSPA4L) and similar proteins; cd11738"
                     /db_xref="CDD:466844"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95757.3)"
     Region          503..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95757.3)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95757.3)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48722; propagated from
                     UniProtKB/Swiss-Prot (O95757.3)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95757.3)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O95757.3)"
     Region          786..839
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95757.3)"
     CDS             1..839
                     /gene="HSPA4L"
                     /gene_synonym="APG-1; APG1; HSPH3; Osp94"
                     /coded_by="NM_014278.4:230..2749"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3734.1"
                     /db_xref="GeneID:22824"
                     /db_xref="HGNC:HGNC:17041"
                     /db_xref="MIM:619077"
ORIGIN      
        1 msvvgidlgf lncyiavars ggietianey sdrctpacis lgsrtraign aaksqivtnv
       61 rntihgfkkl hgrsfddpiv qterirlpye lqkmpngsag vkvryleeer pfaieqvtgm
      121 llaklketse nalkkpvadc visipsfftd aerrsvmaaa qvaglnclrl mnettavala
      181 ygiykqdlpp ldekprnvvf idmghsayqv lvcafnkgkl kvlattfdpy lggrnfdeal
      241 vdyfcdefkt kykinvkens rallrlyqec eklkklmsan asdlplniec fmndldvssk
      301 mnraqfeqlc asllarvepp lkavmeqanl qredissiei vggatripav keqitkfflk
      361 disttlnade avargcalqc ailspafkvr efsitdlvpy sitlrwktsf edgsgecevf
      421 cknhpapfsk vitfhkkepf eleafytnlh evpypdarig sftiqnvfpq sdgdsskvkv
      481 kvrvnihgif svasasviek qnlegdhsda pmetetsfkn enkdnmdkmq vdqeeghqkc
      541 haehtpeeei dhtgaktksa vsdkqdrlnq tlkkgkvksi dlpiqsslcr qlgqdllnsy
      601 ienegkmimq dklekernda knaveeyvyd frdrlgtvye kfitpedlsk lsavledten
      661 wlyedgedqp kqvyvdklqe lkkygqpiqm kymeheerpk alndlgkkiq lvmkvieayr
      721 nkderydhld ptemekvekc isdamswlns kmnaqnklsl tqdpvvkvse ivakskeldn
      781 fcnpiiykpk pkaevpedkp kansehngpm dgqsgtetks dstkdssqht kssgemevd
//
LOCUS       NP_002789                239 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-6 isoform 1 [Homo sapiens].
ACCESSION   NP_002789
VERSION     NP_002789.1
DBSOURCE    REFSEQ: accession NM_002798.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Belich,M.P., Glynne,R.J., Senger,G., Sheer,D. and Trowsdale,J.
  TITLE     Proteasome components with reciprocal expression to that of the
            MHC-encoded LMP proteins
  JOURNAL   Curr Biol 4 (9), 769-776 (1994)
   PUBMED   7820546
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Akiyama,K., Yokota,K., Kagawa,S., Shimbara,N., Tamura,T.,
            Akioka,H., Nothwang,H.G., Noda,C., Tanaka,K. and Ichihara,A.
  TITLE     cDNA cloning and interferon gamma down-regulation of proteasomal
            subunits X and Y
  JOURNAL   Science 265 (5176), 1231-1234 (1994)
   PUBMED   8066462
REFERENCE   9  (residues 1 to 239)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Lee,L.W., Moomaw,C.R., Orth,K., McGuire,M.J., DeMartino,G.N. and
            Slaughter,C.A.
  TITLE     Relationships among the subunits of the high molecular weight
            proteinase, macropain (proteasome)
  JOURNAL   Biochim Biophys Acta 1037 (2), 178-185 (1990)
   PUBMED   2306472
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF671774.1 and BC000835.2.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. The
            encoded protein is a member of the proteasome B-type family, also
            known as the T1B family, and is a 20S core beta subunit in the
            proteasome. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.44608.1,
                                           SRR5189661.178261.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270586.8/ ENSP00000270586.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..239
                     /product="proteasome subunit beta type-6 isoform 1"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit delta; PSY large multifunctional
                     protease Y; proteasome delta chain; macropain delta chain;
                     multicatalytic endopeptidase complex delta chain;
                     proteasome catalytic subunit 1; proteasome subunit Y;
                     proteasome (prosome, macropain) subunit, beta type, 6;
                     proteasome subunit beta 6; proteasome subunit beta1;
                     beta-1; proteasome subunit beta-1"
                     /calculated_mol_wt=25227
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P28072.4)"
     mat_peptide     35..239
                     /product="Proteasome subunit beta type-6.
                     /id=PRO_0000026614"
                     /note="propagated from UniProtKB/Swiss-Prot (P28072.4)"
                     /calculated_mol_wt=21904
     Region          35..222
                     /region_name="proteasome_beta_type_6"
                     /note="proteasome beta type-6 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03762"
                     /db_xref="CDD:239731"
     Site            order(35,51,53,67,164,201,204..205)
                     /site_type="active"
                     /db_xref="CDD:239731"
     Site            order(53,56,58..63,83,85,100,112,115..116,118..119,122,
                     125,149,151,153..156,159,167..168,170..171,174..176,192,
                     199..202,205..206)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239731"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28072.4)"
     CDS             1..239
                     /gene="PSMB6"
                     /gene_synonym="DELTA; LMPY"
                     /coded_by="NM_002798.3:32..751"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11056.1"
                     /db_xref="GeneID:5694"
                     /db_xref="HGNC:HGNC:9543"
                     /db_xref="MIM:600307"
ORIGIN      
        1 maatllaarg agpapawgpe aftpdwesre vstgttimav qfdggvvlga dsrtttgsyi
       61 anrvtdkltp ihdrifccrs gsaadtqava davtyqlgfh sielnepplv htaaslfkem
      121 cyryredlma giiiagwdpq eggqvysvpm ggmmvrqsfa iggsgssyiy gyvdatyreg
      181 mtkeeclqft analalamer dgssggvirl aaiaesgver qvllgdqipk favatlppa
//
LOCUS       NP_005322                142 aa            linear   PRI 20-NOV-2025
DEFINITION  hemoglobin subunit theta-1 [Homo sapiens].
ACCESSION   NP_005322
VERSION     NP_005322.1
DBSOURCE    REFSEQ: accession NM_005331.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Giardina,B., Messana,I., Scatena,R. and Castagnola,M.
  TITLE     The multiple functions of hemoglobin
  JOURNAL   Crit Rev Biochem Mol Biol 30 (3), 165-196 (1995)
   PUBMED   7555018
  REMARK    Review article
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Kim,J.H., Yu,C.Y., Bailey,A., Hardison,R. and Shen,C.K.
  TITLE     Unique sequence organization and erythroid cell-specific nuclear
            factor-binding of mammalian theta 1 globin promoters
  JOURNAL   Nucleic Acids Res 17 (14), 5687-5700 (1989)
   PUBMED   2569721
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Higgs,D.R., Vickers,M.A., Wilkie,A.O., Pretorius,I.M., Jarman,A.P.
            and Weatherall,D.J.
  TITLE     A review of the molecular genetics of the human alpha-globin gene
            cluster
  JOURNAL   Blood 73 (5), 1081-1104 (1989)
   PUBMED   2649166
  REMARK    Review article
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Ley,T.J., Maloney,K.A., Gordon,J.I. and Schwartz,A.L.
  TITLE     Globin gene expression in erythroid human fetal liver cells
  JOURNAL   J Clin Invest 83 (3), 1032-1038 (1989)
   PUBMED   2921315
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Gonzalez-Redondo,J.M., Han,I.S., Gu,Y.C. and Huisman,T.H.
  TITLE     Nucleotide sequence of the human theta 1-globin gene
  JOURNAL   Biochem Genet 26 (3-4), 207-211 (1988)
   PUBMED   3408475
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Hsu,S.L., Marks,J., Shaw,J.P., Tam,M., Higgs,D.R., Shen,C.C. and
            Shen,C.K.
  TITLE     Structure and expression of the human theta 1 globin gene
  JOURNAL   Nature 331 (6151), 94-96 (1988)
   PUBMED   3422341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z84721.1 and BC056686.1.
            
            Summary: Theta-globin mRNA is found in human fetal erythroid tissue
            but not in adult erythroid or other nonerythroid tissue. The
            theta-1 gene may be expressed very early in embryonic life, perhaps
            sometime before 5 weeks. Theta-1 is a member of the human
            alpha-globin gene cluster that involves five functional genes and
            two pseudogenes. The order of genes is: 5' - zeta - pseudozeta - mu
            - pseudoalpha-2 -pseudoalpha-1 - alpha-2 - alpha-1 - theta-1 - 3'.
            Research supports a transcriptionally active role for the gene and
            a functional role for the peptide in specific cells, possibly those
            of early erythroid tissue. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC056686.1, CD580449.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000199708.3/ ENSP00000199708.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..142
                     /product="hemoglobin subunit theta-1"
                     /note="theta-1-globin; hemoglobin theta-1 chain;
                     hemoglobin, theta 1"
                     /calculated_mol_wt=15377
     Region          3..142
                     /region_name="Hb-alpha-like"
                     /note="Hemoglobin alpha, zeta, mu, theta, and related Hb
                     subunits; cd08927"
                     /db_xref="CDD:381263"
     Site            order(32,35..36,42..43,93,95..96,104,108,111..112,
                     118..120,123..124,127,141..142)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381263"
     Site            order(33,43..44,59,62..63,66,84,88,98..99,102,137)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:381263"
     CDS             1..142
                     /gene="HBQ1"
                     /gene_synonym="HBQ"
                     /coded_by="NM_005331.5:29..457"
                     /db_xref="CCDS:CCDS10400.1"
                     /db_xref="GeneID:3049"
                     /db_xref="HGNC:HGNC:4833"
                     /db_xref="MIM:142240"
ORIGIN      
        1 malsaedral vralwkklgs nvgvytteal ertflafpat ktyfshldls pgssqvrahg
       61 qkvadalsla verlddlpha lsalshlhac qlrvdpasfq llghcllvtl arhypgdfsp
      121 alqasldkfl shvisalvse yr
//
LOCUS       NP_001356492             146 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform b [Homo sapiens].
ACCESSION   NP_001356492
VERSION     NP_001356492.1
DBSOURCE    REFSEQ: accession NM_001369563.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BE791671.1, AA918118.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA2162823
                                    [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..146
                     /product="large ribosomal subunit protein uL22 isoform b"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=16963
     Region          <1..127
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     CDS             1..146
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369563.1:42..482"
                     /note="isoform b is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS56070.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mhirkatkyl kdvtlqkqcv pfrrynggvg rcaqakqwgw tqgrwpkksa efllhmlkna
       61 esnaelkgld vdslviehiq vnkapkmrrr tyrahgrinp ymsspchiem iltekeqivp
      121 kpeeevaqkk kisqkklkkq klmare
//
LOCUS       NP_001003796             128 aa            linear   PRI 20-NOV-2025
DEFINITION  NHP2-like protein 1 [Homo sapiens].
ACCESSION   NP_001003796
VERSION     NP_001003796.1
DBSOURCE    REFSEQ: accession NM_001003796.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Zhang,D., Li,B., Xu,H., Li,J., Ma,C., Ge,W., Lu,C. and Cao,X.
  TITLE     Identification of FBLL1 as a neuron-specific RNA
            2'-O-methyltransferase mediating neuronal differentiation
  JOURNAL   Proc Natl Acad Sci U S A 121 (48), e2406961121 (2024)
   PUBMED   39570315
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Chang,M.S., Sasaki,H., Campbell,M.S., Kraeft,S.K., Sutherland,R.,
            Yang,C.Y., Liu,Y., Auclair,D., Hao,L., Sonoda,H., Ferland,L.H. and
            Chen,L.B.
  TITLE     HRad17 colocalizes with NHP2L1 in the nucleolus and redistributes
            after UV irradiation
  JOURNAL   J Biol Chem 274 (51), 36544-36549 (1999)
   PUBMED   10593953
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Nottrott,S., Hartmuth,K., Fabrizio,P., Urlaub,H., Vidovic,I.,
            Ficner,R. and Luhrmann,R.
  TITLE     Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP
            protein with the 5' stem-loop of U4 snRNA
  JOURNAL   EMBO J 18 (21), 6119-6133 (1999)
   PUBMED   10545122
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Zhu,X. and Naz,R.K.
  TITLE     Fertilization antigen-1: cDNA cloning, testis-specific expression,
            and immunocontraceptive effects
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4704-4709 (1997)
   PUBMED   9114055
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Saito,H., Fujiwara,T., Shin,S., Okui,K. and Nakamura,Y.
  TITLE     Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a
            protein highly homologous to yeast nuclear protein NHP2
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 191-193 (1996)
   PUBMED   8978773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF552526.1, D50420.1 and
            BI770951.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Originally named because of its sequence similarity to the
            Saccharomyces cerevisiae NHP2 (non-histone protein 2), this protein
            appears to be a highly conserved nuclear protein that is a
            component of the [U4/U6.U5] tri-snRNP. It binds to the 5' stem-loop
            of U4 snRNA. Two transcript variants encoding the same protein have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 use different start codons but
            encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.67582.1,
                                           SRR5189661.62648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401959.6/ ENSP00000383949.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..128
                     /product="NHP2-like protein 1"
                     /note="non-histone chromosome protein 2-like 1; sperm
                     specific antigen 1; SNU13 homolog, small nuclear
                     ribonucleoprotein (U4/U6.U5); high mobility group-like
                     nuclear protein 2 homolog 1; NHP2 non-histone chromosome
                     protein 2-like 1; [U4/U6.U5] tri-snRNP 15.5 kD RNA binding
                     protein; U4/U6.U5 tri-snRNP 15.5 kDa protein"
                     /calculated_mol_wt=14042
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P55769.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in NHP2-like protein 1,
                     N-terminally processed. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P55769.3)"
     Region          7..128
                     /region_name="SNU13"
                     /note="U4/U6.U5 small nuclear ribonucleoprotein SNU13;
                     cd21104"
                     /db_xref="CDD:411046"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0T1; propagated from
                     UniProtKB/Swiss-Prot (P55769.3)"
     Site            order(36..41,44,48,60..61,65,86,95..100)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411046"
     Region          36..48
                     /region_name="Interaction with U4 snRNA and U4atac snRNA.
                     /evidence=ECO:0000269|PubMed:17412961,
                     ECO:0000269|PubMed:21784869"
                     /note="propagated from UniProtKB/Swiss-Prot (P55769.3)"
     Site            order(40,43..44,47,62,64..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:411046"
     Site            61
                     /site_type="other"
                     /note="Interaction with U4 snRNA and U4atac snRNA.
                     /evidence=ECO:0000269|PubMed:17412961,
                     ECO:0000269|PubMed:21784869; propagated from
                     UniProtKB/Swiss-Prot (P55769.3)"
     Site            86
                     /site_type="other"
                     /note="Interaction with U4 snRNA and U4atac snRNA.
                     /evidence=ECO:0000269|PubMed:17412961,
                     ECO:0000269|PubMed:21784869; propagated from
                     UniProtKB/Swiss-Prot (P55769.3)"
     Region          96..128
                     /region_name="Important for U4 snRNA-binding.
                     /evidence=ECO:0000269|PubMed:10545122"
                     /note="propagated from UniProtKB/Swiss-Prot (P55769.3)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P55769.3)"
     CDS             1..128
                     /gene="SNU13"
                     /gene_synonym="15.5K; FA-1; FA1; NHP2L1; NHPX; OTK27;
                     SNRNP15-5; SPAG12; SSFA1"
                     /coded_by="NM_001003796.2:72..458"
                     /db_xref="CCDS:CCDS33653.1"
                     /db_xref="GeneID:4809"
                     /db_xref="HGNC:HGNC:7819"
                     /db_xref="MIM:601304"
ORIGIN      
        1 mteadvnpka ypladahltk klldlvqqsc nykqlrkgan eatktlnrgi sefivmaada
       61 epleiilhlp llcedknvpy vfvrskqalg racgvsrpvi acsvtikegs qlkqqiqsiq
      121 qsierllv
//
LOCUS       NP_001275644            1134 aa            linear   PRI 20-NOV-2025
DEFINITION  catenin delta-2 isoform 2 [Homo sapiens].
ACCESSION   NP_001275644 XP_005248311
VERSION     NP_001275644.1
DBSOURCE    REFSEQ: accession NM_001288715.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Assendorp,N., Fossati,M., Libe-Philippot,B., Christopoulou,E.,
            Depp,M., Rapone,R., Dingli,F., Loew,D., Vanderhaeghen,P. and
            Charrier,C.
  TITLE     CTNND2 moderates the pace of synaptic maturation and links human
            evolution to synaptic neoteny
  JOURNAL   Cell Rep 43 (10), 114797 (2024)
   PUBMED   39352808
  REMARK    GeneRIF: CTNND2 moderates the pace of synaptic maturation and links
            human evolution to synaptic neoteny.
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Pauly,M., Krumbiegel,M., Trumpp,S., Braig,S., Rupprecht,T.,
            Kraus,C., Uebe,S., Reis,A. and Vasileiou,G.
  TITLE     Severe manifestation of Rauch-Azzarello syndrome associated with
            biallelic deletion of CTNND2
  JOURNAL   Clin Genet 106 (2), 180-186 (2024)
   PUBMED   38604781
  REMARK    GeneRIF: Severe manifestation of Rauch-Azzarello syndrome
            associated with biallelic deletion of CTNND2.
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Li,M., Nopparat,J., Aguilar,B.J., Chen,Y.H., Zhang,J., Du,J.,
            Ai,X., Luo,Y., Jiang,Y., Boykin,C. and Lu,Q.
  TITLE     Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression
  JOURNAL   Oncogene 39 (22), 4358-4374 (2020)
   PUBMED   32313227
  REMARK    GeneRIF: Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression.
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   Lu,Q., Paredes,M., Medina,M., Zhou,J., Cavallo,R., Peifer,M.,
            Orecchio,L. and Kosik,K.S.
  TITLE     delta-catenin, an adhesive junction-associated protein which
            promotes cell scattering
  JOURNAL   J Cell Biol 144 (3), 519-532 (1999)
   PUBMED   9971746
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 1134)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   9  (residues 1 to 1134)
  AUTHORS   Zhou,J., Liyanage,U., Medina,M., Ho,C., Simmons,A.D., Lovett,M. and
            Kosik,K.S.
  TITLE     Presenilin 1 interaction in the brain with a novel member of the
            Armadillo family
  JOURNAL   Neuroreport 8 (8), 2085-2090 (1997)
   PUBMED   9223106
REFERENCE   10 (residues 1 to 1134)
  AUTHORS   Simmons,A.D., Overhauser,J. and Lovett,M.
  TITLE     Isolation of cDNAs from the Cri-du-chat critical region by direct
            screening of a chromosome 5-specific cDNA library
  JOURNAL   Genome Res 7 (2), 118-127 (1997)
   PUBMED   9049630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC332925.1, AK226124.1,
            AB013805.1, U52828.1, AI680877.1, U52351.1 and AC010626.6.
            
            On Jan 1, 2014 this sequence version replaced XP_005248311.1.
            
            Summary: This gene encodes an adhesive junction associated protein
            of the armadillo/beta-catenin superfamily and is implicated in
            brain and eye development and cancer formation. The protein encoded
            by this gene promotes the disruption of E-cadherin based adherens
            junction to favor cell spreading upon stimulation by hepatocyte
            growth factor. This gene is overexpressed in prostate
            adenocarcinomas and is associated with decreased expression of
            tumor suppressor E-cadherin in this tissue. This gene resides in a
            region of the short arm of chromosome 5 that is deleted in Cri du
            Chat syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Dec
            2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding region, uses a downstream start codon, compared to variant
            1.  The resulting protein (isoform 2) has a shorter and distinct
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK226124.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..1134
                     /product="catenin delta-2 isoform 2"
                     /note="catenin (cadherin-associated protein), delta 2
                     (neural plakophilin-related arm-repeat protein); T-cell
                     delta-catenin; neurojungin"
                     /calculated_mol_wt=122952
     Region          72..>443
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          459..>632
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          461..486
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(477,481,485,519,523,527,564,568,572)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          490..530
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          494..530
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          534..575
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          538..573
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          580..631
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          743..784
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          747..784
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          794..829
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          794..828
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          835..881
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          883..927
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          887..922
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..1134
                     /gene="CTNND2"
                     /gene_synonym="GT24; NPRAP"
                     /coded_by="NM_001288715.1:272..3676"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75228.1"
                     /db_xref="GeneID:1501"
                     /db_xref="HGNC:HGNC:2516"
                     /db_xref="MIM:604275"
ORIGIN      
        1 mssmssaeeq fqwqsqdgqk diedelttgl elvdscirsl qesgildpqd ystgerpsll
       61 sqsalqlnsk pegsfqypas yhsnqtlalg ettpsqlpar gtqaratgqs fsqgttsrag
      121 hlagpepapp ppppprepfa pslgsafhlp dappaaaaaa lyyssstlpa pprggsplaa
      181 pqggsptklq rggsapegat yaaprgsspk qspsrlaksy stsspinivv ssaglspirv
      241 tspptvqsti ssspihqlss tigtyatlsp tkrlvhaseq yskhsqelya tatlqrpgsl
      301 aagsrasyss qhghlgpelr alqspehhid piyedrvyqk ppmrslsqsq gdplppahtg
      361 tyrtstapss pgvdsvplqr tgsqhgpqna aaatfqrasy aagpasnyad pyrqlqycps
      421 vespysksgp alppegtlar spsidsiqkd prefgwrdpe lpeviqmlqh qfpsvqsnaa
      481 aylqhlcfgd nkikaeirrq ggiqllvdll dhrmtevhrs acgalrnlvy gkanddnkia
      541 lkncggipal vrllrkttdl eirelvtgvl wnlsscdalk mpiiqdalav ltnaviiphs
      601 gwensplqdd rkiqlhssqv lrnatgclrn vssageearr rmrecdgltd allyviqsal
      661 gsseidsktv encvcilrnl syrlaaetsq gqhmgtdeld gllcgeangk daessgcwgk
      721 kkkkkksqdq wdgvgplpdc aeppkgiqml whpsivkpyl tllsecsnpd tlegaagalq
      781 nlaagswkws vyiraavrke kglpilvell ridndrvvca vatalrnmal dvrnkeligk
      841 yamrdlvhrl pggnnsnnta skamsddtvt avcctlhevi tknmenakal rdaggieklv
      901 giskskgdkh spkvvkaasq vlnsmwqyrd lrslykkdgw sqyhfvasss tierdrqrpy
      961 sssrtpsisp vrvspnnrsa sapaspremi slkerktdye ctgsnatyhg akgehtsrkd
     1021 amtaqntgis tlyrnsygap aedikhnqvs aqpvpqepsr kdyetyqpfq nstrnydesf
     1081 fedqvhhrpp aseytmhlgl kstgnyvdfy saarpyseln yetshypasp dswv
//
LOCUS       NP_001292492              71 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin-like protein 4A isoform 4 [Homo sapiens].
ACCESSION   NP_001292492
VERSION     NP_001292492.1
DBSOURCE    REFSEQ: accession NM_001305563.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Wood,K.A., Ellingford,J.M., Thomas,H.B., Douzgou,S., Beaman,G.M.,
            Hobson,E., Prescott,K., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics UK Research Consortium
  TITLE     Expanding the genotypic spectrum of TXNL4A variants in Burn-McKeown
            syndrome
  JOURNAL   Clin Genet 101 (2), 255-259 (2022)
   PUBMED   34713892
  REMARK    GeneRIF: Expanding the genotypic spectrum of TXNL4A variants in
            Burn-McKeown syndrome.
REFERENCE   5  (residues 1 to 71)
  AUTHORS   Wieczorek,D., Newman,W.G., Wieland,T., Berulava,T., Kaffe,M.,
            Falkenstein,D., Beetz,C., Graf,E., Schwarzmayr,T., Douzgou,S.,
            Clayton-Smith,J., Daly,S.B., Williams,S.G., Bhaskar,S.S.,
            Urquhart,J.E., Anderson,B., O'Sullivan,J., Boute,O., Gundlach,J.,
            Czeschik,J.C., van Essen,A.J., Hazan,F., Park,S., Hing,A.,
            Kuechler,A., Lohmann,D.R., Ludwig,K.U., Mangold,E., Steenpass,L.,
            Zeschnigk,M., Lemke,J.R., Lourenco,C.M., Hehr,U., Prott,E.C.,
            Waldenberger,M., Bohmer,A.C., Horsthemke,B., O'Keefe,R.T.,
            Meitinger,T., Burn,J., Ludecke,H.J. and Strom,T.M.
  TITLE     Compound heterozygosity of low-frequency promoter deletions and
            rare loss-of-function mutations in TXNL4A causes Burn-McKeown
            syndrome
  JOURNAL   Am J Hum Genet 95 (6), 698-707 (2014)
   PUBMED   25434003
  REMARK    GeneRIF: Reporter gene and in vivo assays showed that the promoter
            deletions led to reduced expression of TXNL4A. Depletion of TXNL4A
            (Dib1) in yeast demonstrated reduced assembly of the tri-snRNP
            complex.
REFERENCE   6  (residues 1 to 71)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   7  (residues 1 to 71)
  AUTHORS   Zhang,Y., Lindblom,T., Chang,A., Sudol,M., Sluder,A.E. and
            Golemis,E.A.
  TITLE     Evidence that dim1 associates with proteins involved in pre-mRNA
            splicing, and delineation of residues essential for dim1
            interactions with hnRNP F and Npw38/PQBP-1
  JOURNAL   Gene 257 (1), 33-43 (2000)
   PUBMED   11054566
REFERENCE   8  (residues 1 to 71)
  AUTHORS   Reuter,K., Nottrott,S., Fabrizio,P., Luhrmann,R. and Ficner,R.
  TITLE     Identification, characterization and crystal structure analysis of
            the human spliceosomal U5 snRNP-specific 15 kD protein
  JOURNAL   J Mol Biol 294 (2), 515-525 (1999)
   PUBMED   10610776
REFERENCE   9  (residues 1 to 71)
  AUTHORS   Zhang,Y.Z., Gould,K.L., Dunbrack,R.L. Jr., Cheng,H., Roder,H. and
            Golemis,E.A.
  TITLE     The evolutionarily conserved Dim1 protein defines a novel branch of
            the thioredoxin fold superfamily
  JOURNAL   Physiol Genomics 1 (3), 109-118 (1999)
   PUBMED   11015569
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 71)
  AUTHORS   Ludecke,H.J. and Wieczorek,D.
  TITLE     TXNL4A-Related Craniofacial Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413799
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090360.9, AV729855.2,
            BQ011103.1 and BC001046.2.
            
            Summary: The protein encoded by this gene is a member of the U5
            small ribonucleoprotein particle (snRNP), and is involved in
            pre-mRNA splicing. This protein contains a thioredoxin-like fold
            and it is expected to interact with multiple proteins.
            Protein-protein interactions have been observed with the
            polyglutamine tract-binding protein 1 (PQBP1). Mutations in both
            the coding region and promoter region of this gene have been
            associated with Burn-McKeown syndrome, which is a rare disorder
            characterized by craniofacial dysmorphisms, cardiac defects,
            hearing loss, and bilateral choanal atresia. A pseudogene of this
            gene is found on chromosome 2. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (4) contains two alternate exons
            in its 5' UTR, lacks a portion of the 5' coding region, and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (4) has a shorter N-terminus than
            isoform 1. Variants 4 and 5 encode the same isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.1490217.1, BQ011103.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..71
                     /product="thioredoxin-like protein 4A isoform 4"
                     /note="thioredoxin-like 4; DIM1 protein homolog;
                     thioredoxin-like U5 snRNP protein U5-15kD; spliceosomal U5
                     snRNP-specific 15 kDa protein"
                     /calculated_mol_wt=8332
     Region          <1..71
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     CDS             1..71
                     /gene="TXNL4A"
                     /gene_synonym="BMKS; DIB1; DIM1; SNRNP15; TXNL4; U5-15kD"
                     /coded_by="NM_001305563.2:204..419"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82260.1"
                     /db_xref="GeneID:10907"
                     /db_xref="HGNC:HGNC:30551"
                     /db_xref="MIM:611595"
ORIGIN      
        1 myelydpctv mfffrnkhim idlgtgnnnk inwamedkqe mvdiietvyr garkgrglvv
       61 spkdystkyr y
//
LOCUS       NP_001291492             193 aa            linear   PRI 20-NOV-2025
DEFINITION  INO80 complex subunit E isoform 3 [Homo sapiens].
ACCESSION   NP_001291492 XP_006721104
VERSION     NP_001291492.1
DBSOURCE    REFSEQ: accession NM_001304563.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Cox,E., Hwang,W., Uzoma,I., Hu,J., Guzzo,C.M., Jeong,J.,
            Matunis,M.J., Qian,J., Zhu,H. and Blackshaw,S.
  TITLE     Global Analysis of SUMO-Binding Proteins Identifies SUMOylation as
            a Key Regulator of the INO80 Chromatin Remodeling Complex
  JOURNAL   Mol Cell Proteomics 16 (5), 812-823 (2017)
   PUBMED   28254775
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Vassileva,I., Yanakieva,I., Peycheva,M., Gospodinov,A. and
            Anachkova,B.
  TITLE     The mammalian INO80 chromatin remodeling complex is required for
            replication stress recovery
  JOURNAL   Nucleic Acids Res 42 (14), 9074-9086 (2014)
   PUBMED   25016522
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL525020.3, BU528528.1, BC047712.2 and AC093512.2.
            
            On Feb 3, 2015 this sequence version replaced XP_006721104.1.
            
            Transcript Variant: This variant (3) contains an alternate exon in
            the 3' end compared to variant 1. The resulting isoform (3) has a
            shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.227280.1,
                                           SRR1163658.515915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..193
                     /product="INO80 complex subunit E isoform 3"
                     /note="coiled-coil domain containing 95; coiled-coil
                     domain-containing protein 95"
                     /calculated_mol_wt=21315
     CDS             1..193
                     /gene="INO80E"
                     /gene_synonym="CCDC95"
                     /coded_by="NM_001304563.2:71..652"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:283899"
                     /db_xref="HGNC:HGNC:26905"
ORIGIN      
        1 mngpadgevd ykkkyrnlkr klkfliyehe cfqeelrkaq rkllkvsrdk sflldrllqy
       61 envdedssds datassdnse tegtpklsdt papkrkrspp lggapspssl slppstgfpl
      121 qasgvpspyl sslassrypp fpsdylalql pepsplrpkr ekrprlprkl ksarsgcrae
      181 eldlgeaagr ess
//
LOCUS       NP_005373                916 aa            linear   PRI 20-NOV-2025
DEFINITION  neurofilament medium polypeptide isoform 1 [Homo sapiens].
ACCESSION   NP_005373
VERSION     NP_005373.2
DBSOURCE    REFSEQ: accession NM_005382.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Runge,K., Balla,A., Fiebich,B.L., Maier,S.J., von Zedtwitz,K.,
            Nickel,K., Dersch,R., Domschke,K., Tebartz van Elst,L. and
            Endres,D.
  TITLE     Neurodegeneration Markers in the Cerebrospinal Fluid of 100
            Patients with Schizophrenia Spectrum Disorder
  JOURNAL   Schizophr Bull 49 (2), 464-473 (2023)
   PUBMED   36200879
  REMARK    GeneRIF: Neurodegeneration Markers in the Cerebrospinal Fluid of
            100 Patients with Schizophrenia Spectrum Disorder.
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Li,D., Zhao,W., Zhang,X., Lv,H., Li,C. and Sun,L.
  TITLE     NEFM DNA methylation correlates with immune infiltration and
            survival in breast cancer
  JOURNAL   Clin Epigenetics 13 (1), 112 (2021)
   PUBMED   34001208
  REMARK    GeneRIF: NEFM DNA methylation correlates with immune infiltration
            and survival in breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Ding,Y., Reed,D.R., Baltazar,M.C. and Price,R.A.
  TITLE     RFLP for BgI II at the human neurofilament medium chain (NEF3) gene
            locus
  JOURNAL   Nucleic Acids Res 20 (6), 1429 (1992)
   PUBMED   1348579
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Xu,Z.S., Liu,W.S. and Willard,M.B.
  TITLE     Identification of six phosphorylation sites in the COOH-terminal
            tail region of the rat neurofilament protein M
  JOURNAL   J Biol Chem 267 (7), 4467-4471 (1992)
   PUBMED   1537832
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Chin,T.K., Harding,S.E. and Eagles,P.A.
  TITLE     Characterization of two proteolytically derived soluble
            polypeptides from the neurofilament triplet components NFM and NFH
  JOURNAL   Biochem J 264 (1), 53-60 (1989)
   PUBMED   2557834
REFERENCE   9  (residues 1 to 916)
  AUTHORS   Lee,V.M., Otvos,L. Jr., Carden,M.J., Hollosi,M., Dietzschold,B. and
            Lazzarini,R.A.
  TITLE     Identification of the major multiphosphorylation site in mammalian
            neurofilaments
  JOURNAL   Proc Natl Acad Sci U S A 85 (6), 1998-2002 (1988)
   PUBMED   2450354
REFERENCE   10 (residues 1 to 916)
  AUTHORS   Myers,M.W., Lazzarini,R.A., Lee,V.M., Schlaepfer,W.W. and
            Nelson,D.L.
  TITLE     The human mid-size neurofilament subunit: a repeated protein
            sequence and the relationship of its gene to the intermediate
            filament gene family
  JOURNAL   EMBO J 6 (6), 1617-1626 (1987)
   PUBMED   3608989
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC071752.1, BC096757.1 and
            BP311096.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 28, 2007 this sequence version replaced NP_005373.1.
            
            Summary: Neurofilaments are type IV intermediate filament
            heteropolymers composed of light, medium, and heavy chains.
            Neurofilaments comprise the axoskeleton and functionally maintain
            neuronal caliber. They may also play a role in intracellular
            transport to axons and dendrites. This gene encodes the medium
            neurofilament protein. This protein is commonly used as a biomarker
            of neuronal damage. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.88845.1,
                                           SRR1803616.189930.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221166.10/ ENSP00000221166.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..916
                     /product="neurofilament medium polypeptide isoform 1"
                     /note="neurofilament, medium polypeptide 150kDa;
                     neurofilament triplet M protein; neurofilament-3 (150 kD
                     medium); 160 kDa neurofilament protein; neurofilament
                     medium polypeptide; neurofilament 3"
                     /calculated_mol_wt=102341
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          2..104
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          10..74
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            42
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            47
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          100..411
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          105..136
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          137..149
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          150..248
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          249..265
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          266..287
                     /region_name="Coil 2A"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          <274..850
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          288..291
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Region          292..412
                     /region_name="Coil 2B"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          413..916
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            431
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          485..851
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            559
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Region          614..691
                     /region_name="6 X 13 AA approximate tandem repeats of
                     K-S-P-V-[PS]-K-S-P-V-E-E-[KA]-[GAK]"
                     /note="propagated from UniProtKB/Swiss-Prot (P07197.3)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            646
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O77788; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P08553; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12839; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     Site            837
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P07197.3)"
     CDS             1..916
                     /gene="NEFM"
                     /gene_synonym="NEF3; NF-M; NFM"
                     /coded_by="NM_005382.2:34..2784"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6046.1"
                     /db_xref="GeneID:4741"
                     /db_xref="HGNC:HGNC:7734"
                     /db_xref="MIM:162250"
ORIGIN      
        1 msytldslgn psayrrvtet rssfsrvsgs pssgfrsqsw srgspstvss sykrsmlapr
       61 layssamlss aessldfsqs ssllnggsgp ggdyklsrsn ekeqlqglnd rfagyiekvh
      121 yleqqnkeie aeiqalrqkq ashaqlgday dqeirelrat lemvnhekaq vqldsdhlee
      181 dihrlkerfe eearlrddte aairalrkdi eeaslvkvel dkkvqslqde vaflrsnhee
      241 evadllaqiq ashitverkd ylktdistal keirsqlesh sdqnmhqaee wfkcryaklt
      301 eaaeqnkeai rsakeeiaey rrqlqsksie lesvrgtkes lerqlsdiee rhnhdlssyq
      361 dtiqqlenel rgtkwemarh lreyqdllnv kmaldieiaa yrkllegeet rfstfagsit
      421 gplythrppi tisskiqkpk veapklkvqh kfveeiieet kvedekseme ealtaiteel
      481 avsmkeekke aaeekeeepe aeeeevaakk spvkatapev keeegekeee egqeeeeeed
      541 egaksdqaee ggsekegsse keegeqeege teaeaegeea eakeekkvee kseevatkee
      601 lvadakvekp ekakspvpks pveekgkspv pkspveekgk spvpkspvee kgkspvpksp
      661 veekgkspvs kspveekaks pvpkspveea kskaevgkge qkeeeekevk eapkeekvek
      721 keekpkdvpe kkkaespvke eavaevvtit ksvkvhleke tkeegkplqq ekekekagge
      781 ggseeegsdk gakgsrkedi avngevegke eveqetkekg sgreeekgvv tngldlspad
      841 ekkggdksee kvvvtktvek itseggdgat kyitksvtvt qkveeheetf eeklvstkkv
      901 ekvtshaivk evtqsd
//
LOCUS       NP_001280099             542 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 2 [Homo sapiens].
ACCESSION   NP_001280099 XP_005249918
VERSION     NP_001280099.1
DBSOURCE    REFSEQ: accession NM_001293170.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Borghi,R., Trivisano,M., Specchio,N., Tartaglia,M. and
            Compagnucci,C.
  TITLE     Understanding the pathogenetic mechanisms underlying altered
            neuronal function associated with CAMK2B mutations
  JOURNAL   Neurosci Biobehav Rev 152, 105299 (2023)
   PUBMED   37391113
  REMARK    GeneRIF: Understanding the pathogenetic mechanisms underlying
            altered neuronal function associated with CAMK2B mutations.
            Review article
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Nicole,O. and Pacary,E.
  TITLE     CaMKIIbeta in Neuronal Development and Plasticity: An Emerging
            Candidate in Brain Diseases
  JOURNAL   Int J Mol Sci 21 (19), 7272 (2020)
   PUBMED   33019657
  REMARK    GeneRIF: CaMKIIbeta in Neuronal Development and Plasticity: An
            Emerging Candidate in Brain Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Penades,J.R., Bernal,D., Revert,F., Johansson,C., Fresquet,V.J.,
            Cervera,J., Wieslander,J., Quinones,S. and Saus,J.
  TITLE     Characterization and expression of multiple alternatively spliced
            transcripts of the Goodpasture antigen gene region. Goodpasture
            antibodies recognize recombinant proteins representing the
            autoantigen and one of its alternative forms
  JOURNAL   Eur J Biochem 229 (3), 754-760 (1995)
   PUBMED   7758473
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Schworer,C.M., Colbran,R.J., Keefer,J.R. and Soderling,T.R.
  TITLE     Ca2+/calmodulin-dependent protein kinase II. Identification of a
            regulatory autophosphorylation site adjacent to the inhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 263 (27), 13486-13489 (1988)
   PUBMED   3417668
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550751.1, AK290148.1,
            AF078803.1, AK294138.1 and BQ130578.1.
            
            On May 31, 2014 this sequence version replaced XP_005249918.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a beta chain.
            It is possible that distinct isoforms of this chain have different
            cellular localizations and interact differently with calmodulin.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (9) lacks multiple alternate
            in-frame exons in the 3' coding region and differs in the 3' UTR,
            compared to variant 1. The encoded protein (isoform 2) is shorter
            than isoform 1. Variants 2 and 9 encode the same protein (isoform
            2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.828614.1,
                                           SRR1803616.149285.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..542
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 2"
                     /EC_number="2.7.11.17"
                     /note="CaM kinase II beta subunit; CaM-kinase II beta
                     chain; proline rich calmodulin-dependent protein kinase;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit beta; caMK-II subunit beta"
                     /calculated_mol_wt=60256
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          410..537
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..542
                     /gene="CAMK2B"
                     /gene_synonym="CAM2; CAMK2; CAMKB; CaMKIIbeta; MRD54"
                     /coded_by="NM_001293170.2:174..1802"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS5484.1"
                     /db_xref="GeneID:816"
                     /db_xref="HGNC:HGNC:1461"
                     /db_xref="MIM:607707"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsvgrqt tapatmstaa sgttmglveq aksllnkkad gvkpqtnstk
      361 nsaaatspkg tlppaalepq ttvihnpvdg ikessdsant tiededakar kqeiiktteq
      421 lieavnngdf eayakicdpg ltsfepealg nlvegmdfhr fyfenllakn skpihttiln
      481 phvhvigeda aciayirltq yidgqgrprt sqseetrvwh rrdgkwqnvh fhcsgapvap
      541 lq
//
LOCUS       NP_005755                114 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZK1-interacting protein 1 precursor [Homo sapiens].
ACCESSION   NP_005755
VERSION     NP_005755.1
DBSOURCE    REFSEQ: accession NM_005764.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Hiraizumi,M., Akashi,T., Murasaki,K., Kishida,H., Kumanomidou,T.,
            Torimoto,N., Nureki,O. and Miyaguchi,I.
  TITLE     Transport and inhibition mechanism of the human SGLT2-MAP17 glucose
            transporter
  JOURNAL   Nat Struct Mol Biol 31 (1), 159-169 (2024)
   PUBMED   38057552
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Cui,W., Niu,Y., Sun,Z., Liu,R. and Chen,L.
  TITLE     Structures of human SGLT in the occluded state reveal
            conformational changes during sugar transport
  JOURNAL   Nat Commun 14 (1), 2920 (2023)
   PUBMED   37217492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Hsiao,S.Y., Weng,S.M., Hsiao,J.R., Wu,Y.Y., Wu,J.E., Tung,C.H.,
            Shen,W.L., Sun,S.F., Huang,W.T., Lin,C.Y., Chen,S.H., Hong,T.M.,
            Chen,Y.L. and Chang,J.Y.
  TITLE     MiR-455-5p suppresses PDZK1IP1 to promote the motility of oral
            squamous cell carcinoma and accelerate clinical cancer invasion by
            regulating partial epithelial-to-mesenchymal transition
  JOURNAL   J Exp Clin Cancer Res 42 (1), 40 (2023)
   PUBMED   36737832
  REMARK    GeneRIF: MiR-455-5p suppresses PDZK1IP1 to promote the motility of
            oral squamous cell carcinoma and accelerate clinical cancer
            invasion by regulating partial epithelial-to-mesenchymal
            transition.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Wang,K., Liu,S., Tian,Y., Liu,C., Gui,Z., Yu,T. and Zhang,L.
  TITLE     PDZK1 Interacting Protein 1 Promotes the Progression of Papillary
            Thyroid Cancer
  JOURNAL   J Clin Endocrinol Metab 107 (9), 2449-2461 (2022)
   PUBMED   35727731
  REMARK    GeneRIF: PDZK1 Interacting Protein 1 Promotes the Progression of
            Papillary Thyroid Cancer.
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Niu,Y., Liu,R., Guan,C., Zhang,Y., Chen,Z., Hoerer,S., Nar,H. and
            Chen,L.
  TITLE     Structural basis of inhibition of the human SGLT2-MAP17 glucose
            transporter
  JOURNAL   Nature 601 (7892), 280-284 (2022)
   PUBMED   34880493
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Silver,D.L., Wang,N. and Vogel,S.
  TITLE     Identification of small PDZK1-associated protein, DD96/MAP17, as a
            regulator of PDZK1 and plasma high density lipoprotein levels
  JOURNAL   J Biol Chem 278 (31), 28528-28532 (2003)
   PUBMED   12754212
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Gottgens,B., Barton,L.M., Chapman,M.A., Sinclair,A.M., Knudsen,B.,
            Grafham,D., Gilbert,J.G., Rogers,J., Bentley,D.R. and Green,A.R.
  TITLE     Transcriptional regulation of the stem cell leukemia gene
            (SCL)--comparative analysis of five vertebrate SCL loci
  JOURNAL   Genome Res 12 (5), 749-759 (2002)
   PUBMED   11997341
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Kocher,O., Comella,N., Tognazzi,K. and Brown,L.F.
  TITLE     Identification and partial characterization of PDZK1: a novel
            protein containing PDZ interaction domains
  JOURNAL   Lab Invest 78 (1), 117-125 (1998)
   PUBMED   9461128
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Kocher,O., Cheresh,P. and Lee,S.W.
  TITLE     Identification and partial characterization of a novel
            membrane-associated protein (MAP17) up-regulated in human
            carcinomas and modulating cell replication and tumor growth
  JOURNAL   Am J Pathol 149 (2), 493-500 (1996)
   PUBMED   8701988
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Kocher,O., Cheresh,P., Brown,L.F. and Lee,S.W.
  TITLE     Identification of a novel gene, selectively up-regulated in human
            carcinomas, using the differential display technique
  JOURNAL   Clin Cancer Res 1 (10), 1209-1215 (1995)
   PUBMED   9815914
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM924665.1, BI763294.1 and AL135960.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG748872.1, BU600457.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294338.7/ ENSP00000294338.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..114
                     /product="PDZK1-interacting protein 1 precursor"
                     /note="membrane-associated protein 17; epithelial protein
                     up-regulated in carcinoma, membrane associated protein 17;
                     17 kDa membrane-associated protein"
                     /calculated_mol_wt=10275
     Region          1..114
                     /region_name="MAP17"
                     /note="Membrane-associated protein 117 kDa,
                     PDZK1-interacting protein 1; pfam15807"
                     /db_xref="CDD:464886"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1970
     Site            29..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13113.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQH0; propagated from
                     UniProtKB/Swiss-Prot (Q13113.1)"
     Region          94..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13113.1)"
     CDS             1..114
                     /gene="PDZK1IP1"
                     /gene_synonym="DD96; MAP17; SPAP"
                     /coded_by="NM_005764.4:105..449"
                     /db_xref="CCDS:CCDS546.1"
                     /db_xref="GeneID:10158"
                     /db_xref="HGNC:HGNC:16887"
                     /db_xref="MIM:607178"
ORIGIN      
        1 msalsllilg lltavppasc qqglgnlqpw mqgliavavf lvlvaiafav nhfwcqeepe
       61 pahmiltvgn kadgvlvgtd gryssmaasf rssehenaye nvpeeegkvr stpm
//
LOCUS       NP_001354642             891 aa            linear   PRI 20-NOV-2025
DEFINITION  la-related protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001354642
VERSION     NP_001354642.1
DBSOURCE    REFSEQ: accession NM_001367713.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Ma,J., Dong,D., Qi,H., Li,J., Yu,H., Hu,X., Sun,L. and Shen,L.
  TITLE     LARP1, an RNA-binding protein, participates in ovarian cancer cell
            survival by regulating mitochondrial oxidative phosphorylation in
            response to the influence of the PI3K/mTOR pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (8), 167453 (2024)
   PUBMED   39111634
  REMARK    GeneRIF: LARP1, an RNA-binding protein, participates in ovarian
            cancer cell survival by regulating mitochondrial oxidative
            phosphorylation in response to the influence of the PI3K/mTOR
            pathway.
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Chettle,J., Louie,R.J., Larner,O., Best,R., Chen,K., Morris,J.,
            Dedeic,Z., Childers,A., Rogers,R.C., DuPont,B.R., Skinner,C.,
            Kury,S., Uguen,K., Planes,M., Monteil,D., Li,M., Eliyahu,A.,
            Greenbaum,L., Mor,N., Besnard,T., Isidor,B., Cogne,B., Blesson,A.,
            Comi,A., Wentzensen,I.M., Vuocolo,B., Lalani,S.R., Sierra,R.,
            Berry,L., Carter,K., Sanders,S.J. and Blagden,S.P.
  TITLE     LARP1 haploinsufficiency is associated with an autosomal dominant
            neurodevelopmental disorder
  JOURNAL   HGG Adv 5 (4), 100345 (2024)
   PUBMED   39182167
  REMARK    GeneRIF: LARP1 haploinsufficiency is associated with an autosomal
            dominant neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Smith,B.C. and Silvers,R.
  TITLE     1H, 13C, and 15N resonance assignments of the La Motif of the human
            La-related protein 1
  JOURNAL   Biomol NMR Assign 18 (1), 111-118 (2024)
   PUBMED   38691336
  REMARK    GeneRIF: [1]H, [13]C, and [15]N resonance assignments of the La
            Motif of the human La-related protein 1.
REFERENCE   5  (residues 1 to 891)
  AUTHORS   Kozlov,G., Jiang,J., Rutherford,T., Noronha,A.M., Wilds,C.J. and
            Gehring,K.
  TITLE     Enhanced binding of guanylated poly(A) RNA by the LaM domain of
            LARP1
  JOURNAL   RNA Biol 21 (1), 7-16 (2024)
   PUBMED   39016322
  REMARK    GeneRIF: Enhanced binding of guanylated poly(A) RNA by the LaM
            domain of LARP1.
REFERENCE   6  (residues 1 to 891)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 891)
  AUTHORS   Burrows,C., Abd Latip,N., Lam,S.J., Carpenter,L., Sawicka,K.,
            Tzolovsky,G., Gabra,H., Bushell,M., Glover,D.M., Willis,A.E. and
            Blagden,S.P.
  TITLE     The RNA binding protein Larp1 regulates cell division, apoptosis
            and cell migration
  JOURNAL   Nucleic Acids Res 38 (16), 5542-5553 (2010)
   PUBMED   20430826
REFERENCE   8  (residues 1 to 891)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 891)
  AUTHORS   Horke,S., Reumann,K., Schweizer,M., Will,H. and Heise,T.
  TITLE     Nuclear trafficking of La protein depends on a newly identified
            nucleolar localization signal and the ability to bind RNA
  JOURNAL   J Biol Chem 279 (25), 26563-26570 (2004)
   PUBMED   15060081
  REMARK    GeneRIF: Nuclear trafficking of La protein depends on a newly
            identified nucleolar localization signal and the ability to bind
            RNA
REFERENCE   10 (residues 1 to 891)
  AUTHORS   Chauvet,S., Maurel-Zaffran,C., Miassod,R., Jullien,N., Pradel,J.
            and Aragnol,D.
  TITLE     dlarp, a new candidate Hox target in Drosophila whose orthologue in
            mouse is expressed at sites of epithelium/mesenchymal interactions
  JOURNAL   Dev Dyn 218 (3), 401-413 (2000)
   PUBMED   10878606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008379.7 and AC112169.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.19185.1,
                                           SRR1803614.214706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..891
                     /product="la-related protein 1 isoform 3"
                     /note="la-related protein 1; La ribonucleoprotein domain
                     family member 1"
                     /calculated_mol_wt=102304
     Region          199..271
                     /region_name="LARP_1"
                     /note="La RNA-binding domain of La-related protein 1;
                     cd08037"
                     /db_xref="CDD:153406"
     Region          <202..350
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Site            order(205,208..209,214,217..218,220,239..241)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153406"
     Region          680..720
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          721..759
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     CDS             1..891
                     /gene="LARP1"
                     /gene_synonym="Lar1; LARP; Lhp1"
                     /coded_by="NM_001367713.1:239..2914"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93807.1"
                     /db_xref="GeneID:23367"
                     /db_xref="HGNC:HGNC:29531"
                     /db_xref="MIM:612059"
ORIGIN      
        1 mkeqekgegs dskespktks desgeekngd edcqrggqkk kgnkhkwvpl qidmkpevpr
       61 eklasrptrp peprhipanr geikgsesat yvpvapptpa wqpeikpepa whdqdetssv
      121 ksdgaggara sfrgrgrgrg rgrgrgrggt rthfdyqfgy rkfdgvegpr tpkymnnity
      181 yfdnvsstel ysvdqellkd yikrqieyyf svdnlerdff lrrkmdadgf lpitliasfh
      241 rvqalttdis lifaalkdsk vveivdekvr rreepekwpl ppivdysqtd fsqllncpef
      301 vprqhyqket esapgsprav tpvptkteev snlktlpkgl saslpdldse nwievkkrpr
      361 psparpkkse esrfshltsl pqqlpsqqlm skdqdeqeel dflfdeemeq mdgrkntfta
      421 wsdeesdyei ddrdvnkili vtqtphymrr hpggdrtgnh tsrakmsael akvindglfy
      481 yeqdlwaekf epeysqikqe venfkkvnmi sreqfdtltp eppvdpnqev ppgpprfqqv
      541 ptdalanklf gapepstiar slpttvpesp nyrntrtprt prtpqlkdss qtsrfypvvk
      601 egrtldakmp rkrktrhssn ppleshvgwv mdsrehrprt asissspseg tptvgsygct
      661 pqslpkfqhp shellkengf tqhvyhkyrr rclnerkrlg igqsqemntl frfwsfflrd
      721 hfnkkmyeef kqlaledake gyrygleclf ryysyglekk frldifkdfq eetvkdyeag
      781 qlyglekfwa flkyskaknl didpklqeyl gkfrrledfr vdppmgeegn hkrhsvvagg
      841 gggegrkrcp sqsssrpaam isqpptpptg qpvredakwt sqhsntqtlg k
//
LOCUS       NP_001308777             205 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 4 isoform 9 [Homo sapiens].
ACCESSION   NP_001308777
VERSION     NP_001308777.1
DBSOURCE    REFSEQ: accession NM_001321848.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068338.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.457242.1,
                                           ERR3218374.757125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..205
                     /product="COMM domain-containing protein 4 isoform 9"
                     /note="COMM domain-containing protein 4"
                     /calculated_mol_wt=21734
     Region          31..204
                     /region_name="Commd4"
                     /note="COMM_Domain containing protein 4. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04752"
                     /db_xref="CDD:240100"
     CDS             1..205
                     /gene="COMMD4"
                     /coded_by="NM_001321848.2:76..693"
                     /note="isoform 9 is encoded by transcript variant 11"
                     /db_xref="GeneID:54939"
                     /db_xref="HGNC:HGNC:26027"
                     /db_xref="MIM:616701"
ORIGIN      
        1 mrgrqvapet gggctglsan tvcagvravs lssvklrllc sqvlkellgq gidyekilkl
       61 tadakfesgd vkatvavlsf ilssaakhsv dgeslsselq qlglpkehaa slcrcyeekq
      121 splqkhlrvc slrmnrlagv gwrvdytlss sllqsveepm vhlrlevaaa pgtpaqpvam
      181 slsadkfqvl laelkqaqtl msslg
//
LOCUS       NP_974197                333 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing protein GIPC1 isoform 1 [Homo sapiens].
ACCESSION   NP_974197
VERSION     NP_974197.1
DBSOURCE    REFSEQ: accession NM_202468.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gu,X., Jiao,K., Yue,D., Wang,X., Qiao,K., Gao,M., Lin,J., Sun,C.,
            Zhao,C., Zhu,W. and Xi,J.
  TITLE     Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report
  JOURNAL   Neuromuscul Disord 33 (9), 93-97 (2023)
   PUBMED   37550168
  REMARK    GeneRIF: Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Fan,Y., Shen,S., Yang,J., Yao,D., Li,M., Mao,C., Wang,Y., Hao,X.,
            Ma,D., Li,J., Shi,J., Guo,M., Li,S., Yuan,Y., Liu,F., Yang,Z.,
            Zhang,S., Hu,Z., Fan,L., Liu,H., Zhang,C., Wang,Y., Wang,Q.,
            Zheng,H., He,Y., Song,B., Xu,Y. and Shi,C.
  TITLE     GIPC1 CGG Repeat Expansion Is Associated with Movement Disorders
  JOURNAL   Ann Neurol 91 (5), 704-715 (2022)
   PUBMED   35152460
  REMARK    GeneRIF: GIPC1 CGG Repeat Expansion Is Associated with Movement
            Disorders.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Wang,L.H., Kalb,R.G. and Strittmatter,S.M.
  TITLE     A PDZ protein regulates the distribution of the transmembrane
            semaphorin, M-SemF
  JOURNAL   J Biol Chem 274 (20), 14137-14146 (1999)
   PUBMED   10318831
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Bunn,R.C., Jensen,M.A. and Reed,B.C.
  TITLE     Protein interactions with the glucose transporter binding protein
            GLUT1CBP that provide a link between GLUT1 and the cytoskeleton
  JOURNAL   Mol Biol Cell 10 (4), 819-832 (1999)
   PUBMED   10198040
REFERENCE   8  (residues 1 to 333)
  AUTHORS   De Vries,L., Lou,X., Zhao,G., Zheng,B. and Farquhar,M.G.
  TITLE     GIPC, a PDZ domain containing protein, interacts specifically with
            the C terminus of RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 95 (21), 12340-12345 (1998)
   PUBMED   9770488
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Rousset,R., Fabre,S., Desbois,C., Bantignies,F. and Jalinot,P.
  TITLE     The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
            with the PDZ domain of cellular proteins
  JOURNAL   Oncogene 16 (5), 643-654 (1998)
   PUBMED   9482110
REFERENCE   10 (residues 1 to 333)
  AUTHORS   De Vries,L., Elenko,E., Hubler,L., Jones,T.L. and Farquhar,M.G.
  TITLE     GAIP is membrane-anchored by palmitoylation and interacts with the
            activated (GTP-bound) form of G alpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15203-15208 (1996)
   PUBMED   8986788
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012318.7, AK290252.1 and BC000410.2.
            
            Summary: GIPC1 is a scaffolding protein that regulates cell surface
            receptor expression and trafficking (Lee et al., 2008 [PubMed
            18775991]).[supplied by OMIM, Apr 2009].
            
            Transcript Variant: This variant (3) lacks an exon in the 5' UTR,
            compared to variant 1. Variants 1, 3 and 5 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.174462.1,
                                           SRR3476690.1019614.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..333
                     /product="PDZ domain-containing protein GIPC1 isoform 1"
                     /note="GLUT1 C-terminal binding protein; IGF-1 receptor
                     interacting protein 1; regulator of G-protein signalling
                     19 interacting protein 1; PDZ domain-containing protein
                     GIPC1; tax interaction protein 2; RGS19-interacting
                     protein 1; RGS-GAIP-interacting protein; GAIP
                     C-terminus-interacting protein"
                     /calculated_mol_wt=35918
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          126..219
                     /region_name="PDZ_GIPC1"
                     /note="PDZ domain of PDZ domain-containing protein GIPC1;
                     cd23077"
                     /db_xref="CDD:467290"
     Site            order(142..148,158,161,191,195,198..199)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467290"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          223..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          261..325
                     /region_name="GH2_GIPC"
                     /note="GIPC-homology 2 (GH2) domain found in the GIPC
                     family; cd21180"
                     /db_xref="CDD:409666"
     Site            order(273,276..281,311)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409666"
     Site            order(274..278,280,282..283,310..312,314,316)
                     /site_type="other"
                     /note="myosin VI binding site [polypeptide binding]"
                     /db_xref="CDD:409666"
     CDS             1..333
                     /gene="GIPC1"
                     /gene_synonym="C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1;
                     NIP; OPDM2; RGS19IP1; SEMCAP; SYNECTIIN; SYNECTIN; TIP-2"
                     /coded_by="NM_202468.3:210..1211"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS12310.1"
                     /db_xref="GeneID:10755"
                     /db_xref="HGNC:HGNC:1226"
                     /db_xref="MIM:605072"
ORIGIN      
        1 mplglgrrkk applveneea epgrgglgvg epgplggggs ggpqmglppp ppalrprlvf
       61 htqlahgspt griegftnvk elygkiaeaf rlptaevmfc tlnthkvdmd kllggqigle
      121 dfifahvkgq rkevevfkse dalgltitdn gagyafikri kegsvidhih lisvgdmiea
      181 ingqsllgcr hyevarllke lprgrtftlk lteprkafdm isqrsaggrp gsgpqlgtgr
      241 gtlrlrsrgp atvedlpsaf eekaiekvdd llesymgird telaatmvel gkdkrnpdel
      301 aealderlgd fafpdefvfd vwgaigdakv gry
//
LOCUS       NP_055904               2517 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-9 [Homo sapiens].
ACCESSION   NP_055904
VERSION     NP_055904.1
DBSOURCE    REFSEQ: accession NM_015089.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2517)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2517)
  AUTHORS   Horn-Ghetko,D., Hopf,L.V.M., Tripathi-Giesgen,I., Du,J.,
            Kostrhon,S., Vu,D.T., Beier,V., Steigenberger,B., Prabu,J.R.,
            Stier,L., Bruss,E.M., Mann,M., Xiong,Y. and Schulman,B.A.
  TITLE     Noncanonical assembly, neddylation and chimeric cullin-RING/RBR
            ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex
  JOURNAL   Nat Struct Mol Biol 31 (7), 1083-1094 (2024)
   PUBMED   38605244
  REMARK    GeneRIF: Noncanonical assembly, neddylation and chimeric
            cullin-RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase
            complex.
REFERENCE   3  (residues 1 to 2517)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2517)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   5  (residues 1 to 2517)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   6  (residues 1 to 2517)
  AUTHORS   Ko,H.S., Kim,S.W., Sriram,S.R., Dawson,V.L. and Dawson,T.M.
  TITLE     Identification of far upstream element-binding protein-1 as an
            authentic Parkin substrate
  JOURNAL   J Biol Chem 281 (24), 16193-16196 (2006)
   PUBMED   16672220
  REMARK    GeneRIF: FUBP1 is an authentic substrate of Parkin that might play
            an important role in development of Parkinson disease pathology
            along with aminoacyl-tRNA synthetase interacting multifunctional
            protein type 2
REFERENCE   7  (residues 1 to 2517)
  AUTHORS   Cheng,J., Kapranov,P., Drenkow,J., Dike,S., Brubaker,S., Patel,S.,
            Long,J., Stern,D., Tammana,H., Helt,G., Sementchenko,V.,
            Piccolboni,A., Bekiranov,S., Bailey,D.K., Ganesh,M., Ghosh,S.,
            Bell,I., Gerhard,D.S. and Gingeras,T.R.
  TITLE     Transcriptional maps of 10 human chromosomes at 5-nucleotide
            resolution
  JOURNAL   Science 308 (5725), 1149-1154 (2005)
   PUBMED   15790807
REFERENCE   8  (residues 1 to 2517)
  AUTHORS   Nikolaev,A.Y., Li,M., Puskas,N., Qin,J. and Gu,W.
  TITLE     Parc: a cytoplasmic anchor for p53
  JOURNAL   Cell 112 (1), 29-40 (2003)
   PUBMED   12526791
  REMARK    GeneRIF: Parc, a Parkin-like ubiquitin ligase,is a critical
            regulator in controlling p53 subcellular cytoplasmic localization
            and subsequent function.
REFERENCE   9  (residues 1 to 2517)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 2517)
  AUTHORS   Moynihan,T.P., Ardley,H.C., Nuber,U., Rose,S.A., Jones,P.F.,
            Markham,A.F., Scheffner,M. and Robinson,P.A.
  TITLE     The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with
            RING finger/IBR motif-containing domains of HHARI and H7-AP1
  JOURNAL   J Biol Chem 274 (43), 30963-30968 (1999)
   PUBMED   10521492
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL133375.25, AJ318215.1, KF458162.1 and BC002879.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AJ318215.1, AY145132.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252050.9/ ENSP00000252050.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..2517
                     /product="cullin-9"
                     /note="parkin-like cytoplasmic p53 binding protein;
                     p53-associated parkin-like cytoplasmic protein;
                     UbcH7-associated protein 1; CUL-9"
                     /calculated_mol_wt=281100
     Region          276..296
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          366..440
                     /region_name="Cul7"
                     /note="Mouse development and cellular proliferation
                     protein Cullin-7; pfam11515"
                     /db_xref="CDD:463286"
     Region          576..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          1167..1297
                     /region_name="APC10-like"
                     /note="APC10-like DOC1 domains in E3 ubiquitin ligases
                     that mediate substrate ubiquitination; cl02148"
                     /db_xref="CDD:382862"
     Site            order(1193,1221,1227,1229,1289)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176482"
     Region          1432..1466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Site            1457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          <1469..1814
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          1664..1685
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          1864..1944
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     Region          2066..2283
                     /region_name="TRIAD supradomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          2068..2120
                     /region_name="RING-HC_RBR_CUL9"
                     /note="RING finger, HC subclass, found in cullin-9 (CUL-9)
                     and similar proteins; cd16624"
                     /db_xref="CDD:438286"
     Region          2146..2219
                     /region_name="BRcat_RBR_CUL9"
                     /note="BRcat domain found in cullin-9 (CUL-9) and similar
                     proteins; cd20347"
                     /db_xref="CDD:439008"
     Region          2227..2284
                     /region_name="Rcat_RBR_CUL9"
                     /note="Rcat domain found in cullin-9 (CUL-9) and similar
                     proteins; cd20359"
                     /db_xref="CDD:439020"
     Site            2436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IWT3.2)"
     Region          2442..2517
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IWT3.2)"
     CDS             1..2517
                     /gene="CUL9"
                     /gene_synonym="H7AP1; PARC"
                     /coded_by="NM_015089.4:64..7617"
                     /db_xref="CCDS:CCDS4890.1"
                     /db_xref="GeneID:23113"
                     /db_xref="HGNC:HGNC:15982"
                     /db_xref="MIM:607489"
ORIGIN      
        1 mvgerhagdl mvplgprlqa ypeelirqrp ghdghpeyli rwsvlkcgev gkvgveegka
       61 ehilmwlsap evyancpgll geralskglq hepagvsgsf prdpggldev amgemeadvq
      121 alvrraarql aesgtpslta avlhtihvls ayasigpltg vfretgaldl lmhmlcnpep
      181 qirrsagkml qalaahdags rahvllslsq qdgieqhmdf dsrytllelf aettsseehc
      241 mafegihlpq ipgkllfslv krylcvtsll dqlnsspelg agdqsspcat reksrgqrel
      301 efsmavgnli selvrsmgwa rnlseqgmsp prptrsifqp yisgpslllp tivttprrqg
      361 wvfrqrsefs srsgygeyvq qtlqpgmrvr mlddyeeisa gdegefrqsn ngippvqvfw
      421 qstgrtywvh whmleilgpe eatedkasaa vekgagatvl gtafpswdwn pmdglyplpy
      481 lqpepqkner vgyltqaeww ellffikkld lceqqpifqn lwknldetlg ekalgeisvs
      541 vemaesllqv lssrfegstl ndllnsqiyt kygllsneps ssstsrnhsc tpdpeeesks
      601 easfseeete slkakaeapk teaeptktrt etpmaqsdsq lfnqllvteg mtlptemkea
      661 asemaralrg pgprssldqh vaavvatvqi ssldtnlqls glsalsqave evterdhplv
      721 rpdrslrekl vkmlvelltn qvgekmvvvq alrllyllmt khewrplfar eggiyavlvc
      781 mqeyktsvlv qqaglaalkm lavassseip tfvtgrdsih slfdaqmtre ifasidsatr
      841 pgsesllltv paavilmlnt egcssaarng llllnlllcn hhtlgdqiit qelrdtlfrh
      901 sgiaprtepm pttrtilmml lnryseppgs peraaletpi iqgqdgspel lirslvggps
      961 aellldlerv lcregspgga vrpllkrlqq etqpfllllr tldapgpnkt lllsvlrvit
     1021 rlldfpeamv lpwhevlepc lnclsgpssd seivqeltcf lhrlasmhkd yavvlcclga
     1081 keilskvldk hsaqlllgce lrdlvtecek yaqlysnlts silagciqmv lgqiedhrrt
     1141 hqpinipffd vflrhlcqgs svevkedkcw ekvevssnph raskltdhnp ktywesngst
     1201 gshyitlhmh rgvlvrqltl lvasedssym parvvvfggd stscigteln tvnvmpsasr
     1261 villenlnrf wpiiqirikr cqqggidtrv rgvevlgpkp tfwplfreql crrtclfyti
     1321 raqawsrdia edhrrllqlc prlnrvlrhe qnfadrflpd deaaqalgkt cwealvsplv
     1381 qnitspdaeg vsalgwlldq yleqretsrn plsraasfas rvrrlchllv hvepppgpsp
     1441 epstrpfskn skgrdrspap spvlpssslr nitqcwlsvv qeqvsrflaa awrapdfvpr
     1501 ycklyehlqr agselfgpra afmlalrsgf sgallqqsfl taahmseqfa ryidqqiqgg
     1561 liggapgvem lgqlqrhlep imvlsglela ttfehfyqhy madrllsfgs swlegavleq
     1621 iglcfpnrlp qlmlqslsts eelqrqfhlf qlqrldklfl eqedeeekrl eeeeeeeeee
     1681 eaekelfied pspaisilvl sprcwpvspl cylyhprkcl ptefcdaldr fssfysqsqn
     1741 hpvldmgphr rlqwtwlgra elqfgkqilh vstvqmwlll kfnqteevsv etllkdsdls
     1801 pelllqalvp ltsgngpltl hegqdfphgg vlrlhepgpq rsgealwlip pqaylnvekd
     1861 egrtleqkrn llscllvril kahgekglhi dqlvclvlea wqkgpnppgt lghtvaggva
     1921 ctstdvlsci lhllgqgyvk rrddrpqilm yaapepmgpc rgqadvpfcg sqsetskpsp
     1981 eavatlaslq lpagrtmspq eveglmkqtv rqvqetlnle pdvaqhllah shwgaeqllq
     2041 sysedpepll laaglcvhqa qavpvrpdhc pvcvsplgcd ddlpslccmh ycckscwney
     2101 lttrieqnlv lnctcpiadc paqptgafir aivsspevis kyekallrgy vescsnltwc
     2161 tnpqgcdril crqglgcgtt cskcgwascf ncsfpeahyp ascghmsqwv ddggyydgms
     2221 veaqskhlak liskrcpscq apieknegcl hmtcakcnhg fcwrclkswk pnhkdyyncs
     2281 amvskaarqe krfqdynerc tfhhqarefa vnlrnrvsai hevppprsft flndacqgle
     2341 qarkvlayac vysfysqdae ymdvveqqte nlelhtnalq illeetllrc rdlasslrll
     2401 radclstgme llrriqerll ailqhsaqdf rvglqspsve aweakgpnmp gsqpqassgp
     2461 eaeeeeedde ddvpewqqde fdeeldndsf sydesenldq etfffgdeee dedeayd
//
LOCUS       NP_000071                493 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholine receptor subunit epsilon precursor [Homo sapiens].
ACCESSION   NP_000071
VERSION     NP_000071.1
DBSOURCE    REFSEQ: accession NM_000080.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Kastreva,K., Chamova,T., Blagoeva,S., Bichev,S., Mihaylova,V.,
            Meyer,S., Thompson,R., Cherninkova,S., Guergueltcheva,V.,
            Lochmuller,H. and Tournev,I.
  TITLE     Characterization of Clinical Phenotypes in Congenital Myasthenic
            Syndrome Associated with the c.1327delG Frameshift Mutation in
            CHRNE Encoding the Acetylcholine Receptor Epsilon Subunit
  JOURNAL   J Neuromuscul Dis 11 (5), 1011-1020 (2024)
   PUBMED   38995797
  REMARK    GeneRIF: Characterization of Clinical Phenotypes in Congenital
            Myasthenic Syndrome Associated with the c.1327delG Frameshift
            Mutation in CHRNE Encoding the Acetylcholine Receptor Epsilon
            Subunit.
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Mishra,S., Nair,K.V. and Shukla,A.
  TITLE     Delineation of molecular characteristics of congenital myasthenic
            syndromes in Indian families and review of literature
  JOURNAL   Clin Dysmorphol 32 (4), 162-167 (2023)
   PUBMED   37646703
  REMARK    GeneRIF: Delineation of molecular characteristics of congenital
            myasthenic syndromes in Indian families and review of literature.
            Review article
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Angelini,C., Lispi,L., Salvoro,C., Mostacciuolo,M.L. and Vazza,G.
  TITLE     Clinical and genetic characterization of an Italian family with
            slow-channel syndrome
  JOURNAL   Neurol Sci 40 (3), 503-507 (2019)
   PUBMED   30542963
  REMARK    GeneRIF: This study report a family with progressive proximal and
            distal weakness in which an accurate electrophysiological and CHRNE
            mutation led to a final diagnosis of congenital myasthenic
            syndromes.
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Estephan,E.P., Sobreira,C.F.D.R., Dos Santos,A.C.J.,
            Tomaselli,P.J., Marques,W. Jr., Ortega,R.P.M., Costa,M.C.M., da
            Silva,A.M.S., Mendonca,R.H., Caldas,V.M., Zambon,A.A., Abath
            Neto,O., Marchiori,P.E., Heise,C.O., Reed,U.C., Azuma,Y., Topf,A.,
            Lochmuller,H. and Zanoteli,E.
  TITLE     A common CHRNE mutation in Brazilian patients with congenital
            myasthenic syndrome
  JOURNAL   J Neurol 265 (3), 708-713 (2018)
   PUBMED   29383513
  REMARK    GeneRIF: Study found a pretest probability of CHRNE c.130dupG
            mutation of 31.9% in at least one allele of CMS patients, and when
            considering only homozygous patients the percentage is still high
            (26.4%); percentages notably increase ifonly patients with impaired
            eye movement and improvement of symptoms with pyridostigmine are
            considered.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Shen,X.M., Brengman,J.M., Shen,S., Durmus,H., Preethish-Kumar,V.,
            Yuceyar,N., Vengalil,S., Nalini,A., Deymeer,F., Sine,S.M. and
            Engel,A.G.
  TITLE     Mutations causing congenital myasthenia reveal principal coupling
            pathway in the acetylcholine receptor epsilon-subunit
  JOURNAL   JCI Insight 3 (2), 97826 (2018)
   PUBMED   29367459
  REMARK    GeneRIF: Study identified 2 potentially novel homozygous mutations
            in the AChR epsilon-subunit, epsilonR218W at a position equivalent
            to alphaR209, and E184K at a position equivalent to alphaE175, in 3
            unrelated congenital myasthenic patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Gomez,C.M. and Gammack,J.T.
  TITLE     A leucine-to-phenylalanine substitution in the acetylcholine
            receptor ion channel in a family with the slow-channel syndrome
  JOURNAL   Neurology 45 (5), 982-985 (1995)
   PUBMED   7538206
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Ohno,K., Hutchinson,D.O., Milone,M., Brengman,J.M., Bouzat,C.,
            Sine,S.M. and Engel,A.G.
  TITLE     Congenital myasthenic syndrome caused by prolonged acetylcholine
            receptor channel openings due to a mutation in the M2 domain of the
            epsilon subunit
  JOURNAL   Proc Natl Acad Sci U S A 92 (3), 758-762 (1995)
   PUBMED   7531341
REFERENCE   8  (residues 1 to 493)
  AUTHORS   Beeson,D., Brydson,M., Betty,M., Jeremiah,S., Povey,S., Vincent,A.
            and Newsom-Davis,J.
  TITLE     Primary structure of the human muscle acetylcholine receptor. cDNA
            cloning of the gamma and epsilon subunits
  JOURNAL   Eur J Biochem 215 (2), 229-238 (1993)
   PUBMED   7688301
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Yu,X.M. and Hall,Z.W.
  TITLE     Extracellular domains mediating epsilon subunit interactions of
            muscle acetylcholine receptor
  JOURNAL   Nature 352 (6330), 64-67 (1991)
   PUBMED   1712080
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233723.2 and X66403.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Acetylcholine receptors at mature mammalian neuromuscular
            junctions are pentameric protein complexes composed of four
            subunits in the ratio of two alpha subunits to one beta, one
            epsilon, and one delta subunit. The acetylcholine receptor changes
            subunit composition shortly after birth when the epsilon subunit
            replaces the gamma subunit seen in embryonic receptors. Mutations
            in the epsilon subunit are associated with congenital myasthenic
            syndrome. [provided by RefSeq, Sep 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X66403.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159607 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649488.2/ ENSP00000497829.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..493
                     /product="acetylcholine receptor subunit epsilon
                     precursor"
                     /note="cholinergic receptor, nicotinic, epsilon
                     polypeptide; acetylcholine receptor subunit epsilon; AchR
                     epsilon subunit; cholinergic receptor, nicotinic epsilon;
                     acetylcholine receptor, nicotinic, epsilon (muscle);
                     cholinergic receptor, nicotinic, epsilon (muscle);
                     myasthenia gravis, familial infantile, 1"
                     /calculated_mol_wt=52739
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1977
     mat_peptide     21..493
                     /product="Acetylcholine receptor subunit epsilon.
                     /id=PRO_0000000329"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04844.2)"
                     /calculated_mol_wt=52739
     Region          49..239
                     /region_name="LGIC_ECD_nAChR_E"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit epsilon (CHRNE); cd19030"
                     /db_xref="CDD:349831"
     Site            order(59,61,67..68,75,97,99,108..109,111,113..114,118,
                     120..121,125..127,129,139,141,143,147,169,239)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349831"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04844.2)"
     Region          148..162
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349831"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q04844.2)"
     Site            240..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04844.2)"
     Region          247..474
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            273..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04844.2)"
     Site            307..328
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04844.2)"
     Site            457..480
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04844.2)"
     CDS             1..493
                     /gene="CHRNE"
                     /gene_synonym="ACHRE; CMS1A1; CMS1D; CMS1E; CMS2A; CMS4A;
                     CMS4B; CMS4C; FCCMS; FIM1; FIMG; FIMG1; MGI; SCCMS"
                     /coded_by="NM_000080.4:36..1517"
                     /db_xref="CCDS:CCDS11058.1"
                     /db_xref="GeneID:1145"
                     /db_xref="HGNC:HGNC:1966"
                     /db_xref="MIM:100725"
ORIGIN      
        1 maraplgvll llgllgrgvg kneelrlyhh lfnnydpgsr pvrepedtvt islkvtltnl
       61 islnekeetl ttsvwigidw qdyrlnyskd dfggietlrv pselvwlpei vlennidgqf
      121 gvaydanvlv yeggsvtwlp paiyrsvcav evtyfpfdwq ncslifrsqt ynaeeveftf
      181 avdndgktin kididteayt engewaidfc pgvirrhhgg atdgpgetdv iysliirrkp
      241 lfyviniivp cvlisglvll ayflpaqagg qkctvsinvl laqtvflfli aqkipetsls
      301 vpllgrflif vmvvatlivm ncvivlnvsq rtptthamsp rlrhvllell prllgspppp
      361 eapraasppr rassvglllr aeelilkkpr selvfegqrh rqgtwtaafc qslgaaapev
      421 rccvdavnfv aestrdqeat geevsdwvrm gnaldnicfw aalvlfsvgs sliflgayfn
      481 rvpdlpyapc iqp
//
LOCUS       NP_001244123             555 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001244123
VERSION     NP_001244123.1
DBSOURCE    REFSEQ: accession NM_001257194.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Ying,S., Guo,Q. and Zhang,C.
  TITLE     KLHL3-dependent WNK4 degradation affected by potassium through the
            neddylation and autophagy pathway
  JOURNAL   BMC Nephrol 24 (1), 217 (2023)
   PUBMED   37481568
  REMARK    GeneRIF: KLHL3-dependent WNK4 degradation affected by potassium
            through the neddylation and autophagy pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Lin,Y., Li,Q. and Jin,X.
  TITLE     Kelch-like protein 3 in human disease and therapy
  JOURNAL   Mol Biol Rep 49 (10), 9813-9824 (2022)
   PUBMED   35585379
  REMARK    GeneRIF: Kelch-like protein 3 in human disease and therapy.
            Review article
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Chen,Z., Zhang,J., Murillo-de-Ozores,A.R., Castaneda-Bueno,M.,
            D'Amico,F., Heilig,R., Manning,C.E., Sorrell,F.J., D'Angiolella,V.,
            Fischer,R., Mulder,M.P.C., Gamba,G., Alessi,D.R. and Bullock,A.N.
  TITLE     Sequence and structural variations determining the recruitment of
            WNK kinases to the KLHL3 E3 ligase
  JOURNAL   Biochem J 479 (5), 661-675 (2022)
   PUBMED   35179207
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Etges,A., Hellmig,N., Walenda,G., Haddad,B.G., Machtens,J.P.,
            Morosan,T., Rump,L.C. and Scholl,U.I.
  TITLE     A Novel Homozygous KLHL3 Mutation as a Cause of Autosomal Recessive
            Pseudohypoaldosteronism Type II Diagnosed Late in Life
  JOURNAL   Nephron 146 (4), 418-428 (2022)
   PUBMED   35093948
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Yang,C.L., Zhu,X. and Ellison,D.H.
  TITLE     The thiazide-sensitive Na-Cl cotransporter is regulated by a WNK
            kinase signaling complex
  JOURNAL   J Clin Invest 117 (11), 3403-3411 (2007)
   PUBMED   17975670
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Kahle,K.T., Wilson,F.H., Leng,Q., Lalioti,M.D., O'Connell,A.D.,
            Dong,K., Rapson,A.K., MacGregor,G.G., Giebisch,G., Hebert,S.C. and
            Lifton,R.P.
  TITLE     WNK4 regulates the balance between renal NaCl reabsorption and K+
            secretion
  JOURNAL   Nat Genet 35 (4), 372-376 (2003)
   PUBMED   14608358
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Lai,F., Orelli,B.J., Till,B.G., Godley,L.A., Fernald,A.A.,
            Pamintuan,L. and Le Beau,M.M.
  TITLE     Molecular characterization of KLHL3, a human homologue of the
            Drosophila kelch gene
  JOURNAL   Genomics 66 (1), 65-75 (2000)
   PUBMED   10843806
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF208070.1, AB032955.1 and
            AC106775.3.
            
            Summary: This gene is ubiquitously expressed and encodes a
            full-length protein which has an N-terminal BTB domain followed by
            a BACK domain and six kelch-like repeats in the C-terminus. These
            kelch-like repeats promote substrate ubiquitination of bound
            proteins via interaction of the BTB domain with the CUL3 (cullin 3)
            component of a cullin-RING E3 ubiquitin ligase (CRL) complex.
            Muatations in this gene cause pseudohypoaldosteronism type IID
            (PHA2D); a rare Mendelian syndrome featuring hypertension,
            hyperkalaemia and metabolic acidosis. Alternative splicing results
            in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Mar 2012].
            
            Transcript Variant: This variant (2) lacks a 5' coding exon and has
            an alternate 5' exon which results in the use of a downstream
            in-frame start codon, compared to variant 1. These differences
            result in a protein (isoform 2; also known as KLHL3b) with a
            shorter N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF208070.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..555
                     /product="kelch-like protein 3 isoform 2"
                     /note="kelch-like protein 3"
                     /calculated_mol_wt=61359
     Region          1..117
                     /region_name="BTB_POZ_KLHL3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 3 (KLHL3); cd18339"
                     /db_xref="CDD:349648"
     Region          15..534
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Site            order(41..42,45..46,50..53,60..63,93,96..97,99,104)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349648"
     Region          115..244
                     /region_name="BACK_KLHL3"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 3 (KLHL3); cd18513"
                     /db_xref="CDD:350588"
     Site            order(128..131,133)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:350588"
     Region          265..301
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          305..348
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          352..396
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          399..444
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..492
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          495..541
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..555
                     /gene="KLHL3"
                     /gene_synonym="PHA2D"
                     /coded_by="NM_001257194.1:716..2383"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58970.1"
                     /db_xref="GeneID:26249"
                     /db_xref="HGNC:HGNC:6354"
                     /db_xref="MIM:605775"
ORIGIN      
        1 mgkafkvmne lrskqllcdv mivaedveie ahrvvlaacs pyfcamftgd mseskakkie
       61 ikdvdgqtls klidyiytae ievteenvqv llpaasllql mdvrqnccdf lqsqlhptnc
      121 lgirafadvh tctdllqqan ayaeqhfpev mlgeeflsls ldqvcsliss dkltvsseek
      181 vfeaviswin yeketrlehm aklmehvrlp llprdylvqt veeealiknn ntckdfliea
      241 mkyhllpldq rlliknprtk prtpvslpkv mivvggqapk airsvecydf eedrwdqiae
      301 lpsrrcragv vfmaghvyav ggfngslrvr tvdvydgvkd qwtsiasmqe rrstlgaavl
      361 ndllyavggf dgstglasve aysyktnewf fvapmntrrs svgvgvvegk lyavggydga
      421 srqclstveq ynpatnewiy vadmstrrsg agvgvlsgql yatgghdgpl vrksvevydp
      481 gtntwkqvad mnmcrrnagv cavngllyvv ggddgscnla sveyynpvtd kwtllptnms
      541 tgrsyagvav ihksl
//
LOCUS       NP_001129241             364 aa            linear   PRI 20-NOV-2025
DEFINITION  poliovirus receptor isoform gamma precursor [Homo sapiens].
ACCESSION   NP_001129241
VERSION     NP_001129241.1
DBSOURCE    REFSEQ: accession NM_001135769.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Sun,T., Yang,N., Li,L., Zhang,X., Liu,H., Kusuman,N., Chu,J.,
            Lu,G., Aji,T., Bi,X. and Lin,R.
  TITLE     sCD155 as a potential marker for diagnosing the vascular invasion
            in hepatic alveolar echinococcosis
  JOURNAL   Acta Trop 255, 107203 (2024)
   PUBMED   38604326
  REMARK    GeneRIF: sCD155 as a potential marker for diagnosing the vascular
            invasion in hepatic alveolar echinococcosis.
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Baker,F.L., Smith,K.A., Mylabathula,P.L., Zuniga,T.M., Diak,D.M.,
            Batatinha,H., Niemiro,G.M., Seckeler,M.D., Pedlar,C.R.,
            O'Connor,D.P., Colombo,J., Katsanis,E. and Simpson,R.J.
  TITLE     Exercise-induced beta2-adrenergic Receptor Activation Enhances the
            Antileukemic Activity of Expanded gammadelta T-Cells via DNAM-1
            Upregulation and PVR/Nectin-2 Recognition
  JOURNAL   Cancer Res Commun 4 (5), 1253-1267 (2024)
   PUBMED   38592213
  REMARK    GeneRIF: Exercise-induced beta2-adrenergic Receptor Activation
            Enhances the Antileukemic Activity of Expanded gammadelta T-Cells
            via DNAM-1 Upregulation and PVR/Nectin-2 Recognition.
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Tahara,S., Okumura,G., Matsuo,T., Shibuya,A. and Shibuya,K.
  TITLE     Essential role of CD155 glycosylation in functional binding to
            DNAM-1 on natural killer cells
  JOURNAL   Int Immunol 36 (6), 317-325 (2024)
   PUBMED   38289706
  REMARK    GeneRIF: Essential role of CD155 glycosylation in functional
            binding to DNAM-1 on natural killer cells.
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Liang,J., Liao,L., Xie,L., Tang,W., Yu,X., Lu,Y., Chen,H., Xu,J.,
            Sun,L., Wu,H., Cui,C. and Tan,Y.
  TITLE     PITPNC1 Suppress CD8+ T cell immune function and promote
            radioresistance in rectal cancer by modulating FASN/CD155
  JOURNAL   J Transl Med 22 (1), 117 (2024)
   PUBMED   38291470
  REMARK    GeneRIF: PITPNC1 Suppress CD8[+] T cell immune function and promote
            radioresistance in rectal cancer by modulating FASN/CD155.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Zibert,A. and Wimmer,E.
  TITLE     N glycosylation of the virus binding domain is not essential for
            function of the human poliovirus receptor
  JOURNAL   J Virol 66 (12), 7368-7373 (1992)
   PUBMED   1331527
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Koike,S., Ise,I. and Nomoto,A.
  TITLE     Functional domains of the poliovirus receptor
  JOURNAL   Proc Natl Acad Sci U S A 88 (10), 4104-4108 (1991)
   PUBMED   1851992
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Koike,S., Horie,H., Ise,I., Okitsu,A., Yoshida,M., Iizuka,N.,
            Takeuchi,K., Takegami,T. and Nomoto,A.
  TITLE     The poliovirus receptor protein is produced both as membrane-bound
            and secreted forms
  JOURNAL   EMBO J 9 (10), 3217-3224 (1990)
   PUBMED   2170108
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Schonk,D., van Dijk,P., Riegmann,P., Trapman,J., Holm,C.,
            Willcocks,T.C., Sillekens,P., van Venrooij,W., Wimmer,E., Geurts
            van Kessel,A. et al.
  TITLE     Assignment of seven genes to distinct intervals on the midportion
            of human chromosome 19q surrounding the myotonic dystrophy gene
            region
  JOURNAL   Cytogenet Cell Genet 54 (1-2), 15-19 (1990)
   PUBMED   1701111
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Mendelsohn,C.L., Wimmer,E. and Racaniello,V.R.
  TITLE     Cellular receptor for poliovirus: molecular cloning, nucleotide
            sequence, and expression of a new member of the immunoglobulin
            superfamily
  JOURNAL   Cell 56 (5), 855-865 (1989)
   PUBMED   2538245
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK300349.1 and AC243964.3.
            
            Summary: The protein encoded by this gene is a transmembrane
            glycoprotein belonging to the immunoglobulin superfamily. The
            external domain mediates cell attachment to the extracellular
            matrix molecule vitronectin, while its intracellular domain
            interacts with the dynein light chain Tctex-1/DYNLT1. The gene is
            specific to the primate lineage, and serves as a cellular receptor
            for poliovirus in the first step of poliovirus replication.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (gamma) lacks an internal segment including the putative
            transmembrane domain, compared to isoform alpha, resulting in its
            secretion into serum and cerebrospinal fluid.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.655418.1,
                                           DRR138522.404272.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..364
                     /product="poliovirus receptor isoform gamma precursor"
                     /note="nectin-like protein 5; poliovirus receptor"
                     /calculated_mol_wt=36519
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2803
     Region          29..141
                     /region_name="IgV_1_Nectin-2_NecL-5_like_CD112_CD155"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-2, nectin-like protein 5, and similar domains;
                     cd20989"
                     /db_xref="CDD:409581"
     Region          29..52
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409581"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409581"
     Region          35..39
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409581"
     Region          44..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409581"
     Region          53..61
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409581"
     Region          62..68
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409581"
     Region          63..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409581"
     Region          69..86
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409581"
     Region          76..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409581"
     Region          83..86
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409581"
     Region          87..127
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409581"
     Region          91..97
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409581"
     Region          105..112
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409581"
     Region          119..127
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409581"
     Region          128..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409581"
     Region          131..141
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409581"
     Region          132..141
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409581"
     Region          145..241
                     /region_name="IgC1_2_Nectin-2_Necl-5_like"
                     /note="Second immunoglobulin (Ig) domain of Nectin-2 and
                     Nectin-like protein 5, and similar domains; member of the
                     C1-set of the Ig superfamily (IgSF) domains; cd07703"
                     /db_xref="CDD:409500"
     Region          145..151
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409500"
     Region          162..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409500"
     Region          174..180
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409500"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409500"
     Region          187..195
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409500"
     Region          200..208
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409500"
     Region          218..225
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409500"
     Region          231..237
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409500"
     Region          244..329
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          262..266
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..280
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          295..299
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          309..314
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          324..327
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..364
                     /gene="PVR"
                     /gene_synonym="CD155; HVED; Necl-5; NECL5; PVS; TAGE4"
                     /coded_by="NM_001135769.3:188..1282"
                     /note="isoform gamma precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS46106.1"
                     /db_xref="GeneID:5817"
                     /db_xref="HGNC:HGNC:9705"
                     /db_xref="MIM:173850"
ORIGIN      
        1 maramaaawp lllvallvls wpppgtgdvv vqaptqvpgf lgdsvtlpcy lqvpnmevth
       61 vsqltwarhg esgsmavfhq tqgpsysesk rlefvaarlg aelrnaslrm fglrvedegn
      121 ytclfvtfpq gsrsvdiwlr vlakpqntae vqkvqltgep vpmarcvstg grppaqitwh
      181 sdlggmpnts qvpgflsgtv tvtslwilvp ssqvdgknvt ckvehesfek pqlltvnltv
      241 yyppevsisg ydnnwylgqn eatltcdars npeptgynws ttmgplppfa vaqgaqllir
      301 pvdkpinttl icnvtnalga rqaeltvqvk gtehasasan ghvsysavsr ensssqdpqt
      361 egtr
//
LOCUS       NP_001245143             659 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-2 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001245143
VERSION     NP_001245143.1
DBSOURCE    REFSEQ: accession NM_001258214.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Zare,M., Hesampour,F., Poordast,T., Valibeigi,M., Enayatmehri,M.,
            Ahmadi,S., Nasri,F. and Gharesi-Fard,B.
  TITLE     Association between gene polymorphisms of IL-12, IL-12 receptor and
            IL-27 and organ involvement in Iranian endometriosis patients
  JOURNAL   Int J Immunogenet 50 (1), 24-33 (2023)
   PUBMED   36328955
  REMARK    GeneRIF: Association between gene polymorphisms of IL-12, IL-12
            receptor and IL-27 and organ involvement in Iranian endometriosis
            patients.
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Fu,Y., Liu,L. and Wu,H.
  TITLE     Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic Obstructive
            Pulmonary Disease
  JOURNAL   Int J Chron Obstruct Pulmon Dis 17, 1671-1683 (2022)
   PUBMED   35923356
  REMARK    GeneRIF: Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic
            Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Ye,C., Yano,H., Workman,C.J. and Vignali,D.A.A.
  TITLE     Interleukin-35: Structure, Function and Its Impact on
            Immune-Related Diseases
  JOURNAL   J Interferon Cytokine Res 41 (11), 391-406 (2021)
   PUBMED   34788131
  REMARK    Review article
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Wang,X., Zhou,S., Fan,M., Wang,P., Fang,H., Bian,F., Huang,T. and
            Du,X.
  TITLE     Expressions of IL-12 and its receptors in patients with lumbar disc
            herniation and their relationship with clinical efficacy
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 66 (7), 5-11 (2020)
   PUBMED   33287915
  REMARK    GeneRIF: Expressions of IL-12 and its receptors in patients with
            lumbar disc herniation and their relationship with clinical
            efficacy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Rogge,L., Barberis-Maino,L., Biffi,M., Passini,N., Presky,D.H.,
            Gubler,U. and Sinigaglia,F.
  TITLE     Selective expression of an interleukin-12 receptor component by
            human T helper 1 cells
  JOURNAL   J Exp Med 185 (5), 825-831 (1997)
   PUBMED   9120388
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Presky,D.H., Yang,H., Minetti,L.J., Chua,A.O., Nabavi,N., Wu,C.Y.,
            Gately,M.K. and Gubler,U.
  TITLE     A functional interleukin 12 receptor complex is composed of two
            beta-type cytokine receptor subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 14002-14007 (1996)
   PUBMED   8943050
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB126833.1, DA223630.1,
            AK294494.1, U64198.1, AL389925.10 and AL358512.9.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein identified as a subunit of the interleukin 12 receptor
            complex. The coexpression of this and IL12RB1 proteins was shown to
            lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. The expression of this
            gene is up-regulated by interferon gamma in Th1 cells, and plays a
            role in Th1 cell differentiation. The up-regulation of this gene is
            found to be associated with a number of infectious diseases, such
            as Crohn's disease and leprosy, which is thought to contribute to
            the inflammatory response and host defense. Several transcript
            variants encoding different isoforms and non-protein coding
            transcripts have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate coding exon compared to variant 1, that causes a
            frameshift. Variants 2 and 7 encode the same isoform (b), which has
            a shorter and distinct C-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..659
                     /product="interleukin-12 receptor subunit beta-2 isoform b
                     precursor"
                     /note="interleukin-12 receptor beta-2 chain; IL-12R
                     subunit beta-2; IL-12 receptor subunit beta-2; interleukin
                     12 receptor, beta 2"
                     /calculated_mol_wt=71527
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3099
     mat_peptide     24..659
                     /product="interleukin-12 receptor subunit beta-2 isoform
                     b"
                     /calculated_mol_wt=71955
     Region          28..110
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          224..316
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(224,286,304)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          305..309
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(305..306,308..309)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          <368..>608
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          423..511
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(507..508,510..511)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            623..643
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     CDS             1..659
                     /gene="IL12RB2"
                     /coded_by="NM_001258214.1:729..2708"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS58006.1"
                     /db_xref="GeneID:3595"
                     /db_xref="HGNC:HGNC:5972"
                     /db_xref="MIM:601642"
ORIGIN      
        1 mahtfrgcsl afmfiitwll ikakidackr gdvtvkpshv illgstvnit cslkprqgcf
       61 hysrrnklil ykfdrrinfh hghslnsqvt glplgttlfv cklacinsde iqicgaeifv
      121 gvapeqpqnl sciqkgeqgt vactwergrd thlyteytlq lsgpknltwq kqckdiycdy
      181 ldfginltpe spesnftakv tavnslgsss slpstftfld ivrplppwdi rikfqkasvs
      241 rctlywrdeg lvllnrlryr psnsrlwnmv nvtkakgrhd lldlkpftey efqissklhl
      301 ykgswsdwse slraqtpeee ptgmldvwym krhidysrqq islfwknlsv seargkilhy
      361 qvtlqeltgg kamtqnitgh tswttviprt gnwavavsaa nskgsslptr inimnlceag
      421 llaprqvsan segmdnilvt wqpprkdpsa vqeyvvewre lhpggdtqvp lnwlrsrpyn
      481 vsalisenik syicyeirvy alsgdqggcs silgnskhka plsgphinai teekgsilis
      541 wnsipvqeqm gcllhyriyw kerdsnsqpq lceipyrvsq nshpinslqp rvtyvlwmta
      601 ltaagesshg nerefclqgk anwmafvaps iciaiimvgi fsthyfqqkr rhscpwtgs
//
LOCUS       NP_001340522             519 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform f [Homo sapiens].
ACCESSION   NP_001340522 XP_006720286
VERSION     NP_001340522.1
DBSOURCE    REFSEQ: accession NM_001353593.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 20, 2017 this sequence version replaced XP_006720286.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.126113.1,
                                           SRR7346977.862492.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..519
                     /product="lysosomal cobalamin transporter ABCD4 isoform f"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=58822
     Region          1..516
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..519
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353593.2:165..1724"
                     /note="isoform f is encoded by transcript variant 8"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mlivlnstlk sfdqftcnll yvswrkdlte hlhrlyfrgr ayytlnvlrd didnpdqris
       61 qdverfcrql ssmaskliis pftlvyytyq cfqstgwlgp vsifgyfilg tvvnktlmgp
      121 ivmklvhqek legdfrfkhm qirvnaepaa fyraghvehm rtdrrlqrll qtqrelmske
      181 lwlyigintf dylgsilsyv viaipifsgv ygdlspaels tlvsknafvc iyliscftql
      241 idlsttlsdv agythrigql retlldmslk sqdceilges ewgldtppgw paaepadtaf
      301 llervsisap ssdkplikdl slkisegqsl litgntgtgk tsllrvlggl wtstrgsvqm
      361 ltdfgphgvl flpqkpfftd gtlreqviyp lkevypdsgs adderilrfl elaglsnlva
      421 rtegldqqvd wnwydvlspg emqrlsfarl fylqpkyavl deatsaltee veselyrigq
      481 qlgmtfisvg hrqslekfhs lvlklcgggr welmrikve
//
LOCUS       NP_001354593             822 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform aa [Homo sapiens].
ACCESSION   NP_001354593
VERSION     NP_001354593.1
DBSOURCE    REFSEQ: accession NM_001367664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.95147.1,
                                           SRR1660805.121247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..822
                     /product="SUN domain-containing protein 1 isoform aa"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=90982
     Region          62..328
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          454..507
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(454,457..458,461,464..465,468..469,471..472,
                     475..476,478..479,482..483,485..486,489,492..493,496,
                     499..500,503..504,506..507)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          466..>599
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          584..642
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          685..820
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..822
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367664.1:52..2520"
                     /note="isoform aa is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS94043.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld ahtaahsqsp
      241 rlpgragtlw hiwacagyfl lqilrrigav gqavsrtaws alwlavvapg kaasgvfwwl
      301 gigwyqfvtl iswlnvfllt rclrnickfl vlliplflll aglslrgqgn ffsflpvlnw
      361 asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl
      421 relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev rmshledilg
      481 klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd
      541 avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt
      601 hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg
      661 silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls
      721 mmihpaaftl ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm
      781 fqalkrpddt afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_001311324             382 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001311324
VERSION     NP_001311324.1
DBSOURCE    REFSEQ: accession NM_001324395.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 382)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, BC009259.2, AC108449.5 and BQ019252.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.226490.1,
                                           SRR7346977.1151602.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..382
                     /product="homeobox-containing protein 1 isoform 9"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=43004
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..382
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324395.2:342..1490"
                     /note="isoform 9 is encoded by transcript variant 16"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr aniaailesh gidvqspggh
      361 snsddvdgnd yseqgltlsk al
//
LOCUS       NP_705616                707 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor E isoform 5 [Homo sapiens].
ACCESSION   NP_705616
VERSION     NP_705616.2
DBSOURCE    REFSEQ: accession NM_153483.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Wang,J., Wang,X., Wang,M., Wang,J., Wu,Y. and Qi,X.
  TITLE     Clinical significance of Interleukin 17 receptor E in diabetic
            nephropathy
  JOURNAL   Int Immunopharmacol 120, 110324 (2023)
   PUBMED   37235960
  REMARK    GeneRIF: Clinical significance of Interleukin 17 receptor E in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Jiang,Y., Wang,L., Peng,Y., Qin,J., Tan,A. and Wang,S.
  TITLE     Interleukin 17 receptor E identifies heterogeneous T helper 17
            cells in peritoneal fluid of moderate and severe endometriosis
            patients
  JOURNAL   Clin Exp Immunol 207 (3), 360-369 (2022)
   PUBMED   35553626
  REMARK    GeneRIF: Interleukin 17 receptor E identifies heterogeneous T
            helper 17 cells in peritoneal fluid of moderate and severe
            endometriosis patients.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Swedik,S., Madola,A. and Levine,A.
  TITLE     IL-17C in human mucosal immunity: More than just a middle child
  JOURNAL   Cytokine 146, 155641 (2021)
   PUBMED   34293699
  REMARK    Review article
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Barati,M., Sinaeian,M., Shokrollahi Barough,M., Pak,F., Semnani,V.,
            Kokhaei,P. and Momtazi-Borojeni,A.A.
  TITLE     Evaluation of Interleukin 25 and Interleukin 25 Receptor Expression
            in Peripheral Blood Mononuclear Cells of Breast Cancer Patients and
            Normal Subjects
  JOURNAL   J Interferon Cytokine Res 40 (3), 139-144 (2020)
   PUBMED   31905037
  REMARK    GeneRIF: Evaluation of Interleukin 25 and Interleukin 25 Receptor
            Expression in Peripheral Blood Mononuclear Cells of Breast Cancer
            Patients and Normal Subjects.
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Nies,J.F. and Panzer,U.
  TITLE     IL-17C/IL-17RE: Emergence of a Unique Axis in TH17 Biology
  JOURNAL   Front Immunol 11, 341 (2020)
   PUBMED   32174926
  REMARK    GeneRIF: IL-17C/IL-17RE: Emergence of a Unique Axis in TH17
            Biology.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Wu,B., Jin,M., Zhang,Y., Wei,T. and Bai,Z.
  TITLE     Evolution of the IL17 receptor family in chordates: a new subfamily
            IL17REL
  JOURNAL   Immunogenetics 63 (12), 835-845 (2011)
   PUBMED   21732179
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Chang,S.H., Reynolds,J.M., Pappu,B.P., Chen,G., Martinez,G.J. and
            Dong,C.
  TITLE     Interleukin-17C promotes Th17 cell responses and autoimmune disease
            via interleukin-17 receptor E
  JOURNAL   Immunity 35 (4), 611-621 (2011)
   PUBMED   21982598
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Song,X., Zhu,S., Shi,P., Liu,Y., Shi,Y., Levin,S.D. and Qian,Y.
  TITLE     IL-17RE is the functional receptor for IL-17C and mediates mucosal
            immunity to infection with intestinal pathogens
  JOURNAL   Nat Immunol 12 (12), 1151-1158 (2011)
   PUBMED   21993849
  REMARK    GeneRIF: IL-17RE as a receptor of IL-17C that regulates early
            innate immunity to intestinal pathogens.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Ramirez-Carrozzi,V., Sambandam,A., Luis,E., Lin,Z., Jeet,S.,
            Lesch,J., Hackney,J., Kim,J., Zhou,M., Lai,J., Modrusan,Z., Sai,T.,
            Lee,W., Xu,M., Caplazi,P., Diehl,L., de Voss,J., Balazs,M.,
            Gonzalez,L. Jr., Singh,H., Ouyang,W. and Pappu,R.
  TITLE     IL-17C regulates the innate immune function of epithelial cells in
            an autocrine manner
  JOURNAL   Nat Immunol 12 (12), 1159-1166 (2011)
   PUBMED   21993848
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Li,T.S., Li,X.N., Chang,Z.J., Fu,X.Y. and Liu,L.
  TITLE     Identification and functional characterization of a novel
            interleukin 17 receptor: a possible mitogenic activation through
            ras/mitogen-activated protein kinase signaling pathway
  JOURNAL   Cell Signal 18 (8), 1287-1298 (2006)
   PUBMED   16310341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA592287.1, BC137077.1 and
            AK074238.1.
            
            On Jul 23, 2010 this sequence version replaced NP_705616.1.
            
            Summary: This gene encodes a transmembrane protein that functions
            as the receptor for interleukin-17C. The encoded protein signals to
            downstream components of the mitogen activated protein kinase
            (MAPK) pathway. Activity of this protein is important in the immune
            response to bacterial pathogens. Alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Sep 2013].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            initiates translation at an alternate start codon, compared to
            variant 1. The encoded isoform (5) is longer and has a distinct
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137077.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..707
                     /product="interleukin-17 receptor E isoform 5"
                     /note="IL-17 receptor E"
                     /calculated_mol_wt=78931
     Region          119..488
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          528..651
                     /region_name="SEFIR"
                     /note="SEFIR domain; cl23749"
                     /db_xref="CDD:474043"
     CDS             1..707
                     /gene="IL17RE"
                     /coded_by="NM_153483.2:5..2128"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:132014"
                     /db_xref="HGNC:HGNC:18439"
                     /db_xref="MIM:614995"
ORIGIN      
        1 mgaspnlmla pfllllthsr splsfrpcsh vpgaliaqkp mgssrlaall lplllividl
       61 sdsagigfrh lphwntrcpl ashtddsftg ssayipcrtw walfstkpwc vrvwhcsrcl
      121 cqhllsggsg lqrglfhllv qkskksstfk fyrrhkmpap aqrkllprrh lsekshhisi
      181 pspdishkgl rskrtqpsdp etweslprld sqrhggpefs fdllpearai rvtissgpev
      241 svrlchqwal eceelsspyd vqkivsgght velpyefllp clcieasylq edtvrrkkcp
      301 fqswpeaygs dfwksvhftd ysqhtqmvma ltlrcplkle aalcqrhdwh tlckdlpnat
      361 aresdgwyvl ekvdlhpqlc fkfsfgnssh vecphqtgsl tswnvsmdtq aqqlilhfss
      421 rmhatfsaaw slpglgqdtl vppvytvsqa rgsspvsldl iipflrpgcc vlvwrsdvqf
      481 awkhllcpdv syrhlgllil allalltllg vvlaltcrrp qsgpgparpv lllhaadsea
      541 qrrlvgalae llraalgggr dvivdlwegr hvarvgplpw lwaartrvar eqgtvlllws
      601 gadlrpvsgp dpraapllal lhaaprplll layfsrlcak gdippplral pryrllrdlp
      661 rllraldarp faeatswgrl garqrrqsrl elcsrlerea arladlg
//
LOCUS       NP_060298                199 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_060298
VERSION     NP_060298.2
DBSOURCE    REFSEQ: accession NM_017828.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 199)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 199)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 199)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 199)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 199)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 199)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 199)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 199)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 199)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 199)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI829484.1 and BC068998.1.
            
            On Jun 10, 2002 this sequence version replaced NP_060298.1.
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.16500.1,
                                           SRR5189661.153514.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267935.13/ ENSP00000267935.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..199
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..199
                     /product="COMM domain-containing protein 4 isoform 1"
                     /note="COMM domain-containing protein 4"
                     /calculated_mol_wt=21633
     Region          25..198
                     /region_name="Commd4"
                     /note="COMM_Domain containing protein 4. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04752"
                     /db_xref="CDD:240100"
     CDS             1..199
                     /gene="COMMD4"
                     /coded_by="NM_017828.5:28..627"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10277.1"
                     /db_xref="GeneID:54939"
                     /db_xref="HGNC:HGNC:26027"
                     /db_xref="MIM:616701"
ORIGIN      
        1 mrfrfcgdld cpdwvlaeis tlakmssvkl rllcsqvlke llgqgidyek ilkltadakf
       61 esgdvkatva vlsfilssaa khsvdgesls selqqlglpk ehaaslcrcy eekqsplqkh
      121 lrvcslrmnr lagvgwrvdy tlsssllqsv eepmvhlrle vaaapgtpaq pvamslsadk
      181 fqvllaelkq aqtlmsslg
//
LOCUS       NP_001294949             824 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase catalytic subunit type 3 isoform 2
            [Homo sapiens].
ACCESSION   NP_001294949 XP_011524332
VERSION     NP_001294949.1
DBSOURCE    REFSEQ: accession NM_001308020.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Gong,M., Peng,C., Yang,C., Wang,Z., Qian,H., Hu,X., Zhou,P.,
            Shan,C. and Ding,Q.
  TITLE     Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and PIK3C3 as
            crucial entry factors for Ebola virus infection
  JOURNAL   PLoS Pathog 20 (8), e1012444 (2024)
   PUBMED   39173055
  REMARK    GeneRIF: Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and
            PIK3C3 as crucial entry factors for Ebola virus infection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Tahoun,M. and Sadaka,A.S.
  TITLE     Deregulated expression of autophagy genes; PIK3C3 and RAB7A in
            COVID-19 patients
  JOURNAL   Hum Immunol 85 (3), 110801 (2024)
   PUBMED   38609772
  REMARK    GeneRIF: Deregulated expression of autophagy genes; PIK3C3 and
            RAB7A in COVID-19 patients.
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Jia,M., Yue,X., Sun,W., Zhou,Q., Chang,C., Gong,W., Feng,J., Li,X.,
            Zhan,R., Mo,K., Zhang,L., Qian,Y., Sun,Y., Wang,A., Zou,Y.,
            Chen,W., Li,Y., Huang,L., Yang,Y., Zhao,Y. and Cheng,X.
  TITLE     ULK1-mediated metabolic reprogramming regulates Vps34 lipid kinase
            activity by its lactylation
  JOURNAL   Sci Adv 9 (22), eadg4993 (2023)
   PUBMED   37267363
  REMARK    GeneRIF: ULK1-mediated metabolic reprogramming regulates Vps34
            lipid kinase activity by its lactylation.
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Borgatti,P., Zauli,G., Colamussi,M.L., Gibellini,D., Previati,M.,
            Cantley,L.L. and Capitani,S.
  TITLE     Extracellular HIV-1 Tat protein activates phosphatidylinositol 3-
            and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells
  JOURNAL   Eur J Immunol 27 (11), 2805-2811 (1997)
   PUBMED   9394803
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Panaretou,C., Domin,J., Cockcroft,S. and Waterfield,M.D.
  TITLE     Characterization of p150, an adaptor protein for the human
            phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by
            phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase
            complex
  JOURNAL   J Biol Chem 272 (4), 2477-2485 (1997)
   PUBMED   8999962
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Volinia,S., Dhand,R., Vanhaesebroeck,B., MacDougall,L.K., Stein,R.,
            Zvelebil,M.J., Domin,J., Panaretou,C. and Waterfield,M.D.
  TITLE     A human phosphatidylinositol 3-kinase complex related to the yeast
            Vps34p-Vps15p protein sorting system
  JOURNAL   EMBO J 14 (14), 3339-3348 (1995)
   PUBMED   7628435
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Vogel,L.B. and Fujita,D.J.
  TITLE     The SH3 domain of p56lck is involved in binding to
            phosphatidylinositol 3'-kinase from T lymphocytes
  JOURNAL   Mol Cell Biol 13 (12), 7408-7417 (1993)
   PUBMED   7504174
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB450556.1, AK298517.1, AC087683.5 and CA945171.1.
            
            On Apr 22, 2015 this sequence version replaced XP_011524332.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298517.1, SRR14372079.2563668.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..824
                     /product="phosphatidylinositol 3-kinase catalytic subunit
                     type 3 isoform 2"
                     /EC_number="2.7.1.137"
                     /note="PI3K type 3; PI3-kinase type 3; PtdIns-3-kinase
                     type 3; phosphatidylinositol 3-kinase p100 subunit;
                     phosphoinositide-3-kinase, class 3; vacuolar protein
                     sorting 34 homolog"
                     /calculated_mol_wt=94270
     Region          <24..123
                     /region_name="C2_PI3K_class_III"
                     /note="C2 domain present in class III phosphatidylinositol
                     3-kinases (PI3Ks); cd08397"
                     /db_xref="CDD:176042"
     Region          220..440
                     /region_name="PI3Ka_III"
                     /note="Phosphoinositide 3-kinase (PI3K) class III,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, PI3Ks class III...; cd00870"
                     /db_xref="CDD:238442"
     Region          476..820
                     /region_name="PI3Kc_III"
                     /note="Catalytic domain of Class III Phosphoinositide
                     3-kinase; cd00896"
                     /db_xref="CDD:270628"
     Site            order(549,551..553,555,571,573,576,607,619..622,626,629,
                     685,687,697..698)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270628"
     Site            677..685
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270628"
     Site            698..717
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270628"
     CDS             1..824
                     /gene="PIK3C3"
                     /gene_synonym="hVps34; Vps34; VPS34"
                     /coded_by="NM_001308020.2:59..2533"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77180.1"
                     /db_xref="GeneID:5289"
                     /db_xref="HGNC:HGNC:8974"
                     /db_xref="MIM:602609"
ORIGIN      
        1 mgeaekfhyi yscdldinvq lkiwnewlkl pvkypdlprn aqvaltiwdv ygpgkavpvg
       61 gttvslfgky gmfrqgmhdl kvwpnveadg septktpgrt sstlsedqms rlakltkahr
      121 qghmvkvdwl drltfreiem inesekrssn fmylmvefrc vkcddkeygi vyyekdgdes
      181 spiltsfelv kvpdpqmsme nlveskhhkl arslrsgpsd hdlkpnaatr dqlniivsyp
      241 ptkqltyeeq dlvwkfryyl tnqekaltkf lkcvnwdlpq eakqalellg kwkpmdveds
      301 lellsshytn ptvrryavar lrqaddedll myllqlvqal kyenfddikn gleptkkdsq
      361 ssvsenvsns ginsaeidss qiitsplpsv sspppasktk evpdgenleq dlctflisra
      421 cknstlanyl ywyviveced qdtqqrdpkt hemylnvmrr fsqallkgdk svrvmrslla
      481 aqqtfvdrlv hlmkavqres gnrkkknerl qallgdnekm nlsdvelipl plepqvkirg
      541 iipetatlfk salmpaqlff ktedggkypv ifkhgddlrq dqlilqiisl mdkllrkenl
      601 dlkltpykvl atstkhgfmq fiqsvpvaev ldtegsiqnf frkyapseng pngisaevmd
      661 tyvkscagyc vityilgvgd rhldnllltk tgklfhidfg yilgrdpkpl pppmklnkem
      721 vegmggtqse qyqefrkqcy taflhlrrys nlilnlfslm vdanipdial epdktvkkvq
      781 dkfrldlsde eavhymqsli desvhalfaa vveqihkfaq ywrk
//
LOCUS       NP_001230733             201 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger C4H2 domain-containing protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001230733
VERSION     NP_001230733.1
DBSOURCE    REFSEQ: accession NM_001243804.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Wongkittichote,P., Choi,T.I., Kim,O.H., Riley,K., Koeberl,D.,
            Narayanan,V., Ramsey,K., Balak,C., Schwartz,C.E.,
            Cueto-Gonzalez,A.M., Casadesus,F.M., Kim,C.H. and Shinawi,M.S.
  TITLE     Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord
  JOURNAL   Clin Genet 103 (2), 167-178 (2023)
   PUBMED   36250278
  REMARK    GeneRIF: Expanding allelic and phenotypic spectrum of ZC4H2-related
            disorder: A novel hypomorphic variant and high prevalence of
            tethered cord.
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Li,Y., Yang,C., Wang,H., Zhao,L., Kong,Q., Cang,Y., Zhao,S., Lv,L.,
            Li,Y., Mao,B. and Ma,P.
  TITLE     Sequential stabilization of RNF220 by RLIM and ZC4H2 during
            cerebellum development and Shh-group medulloblastoma progression
  JOURNAL   J Mol Cell Biol 14 (1) (2022)
   PUBMED   35040952
  REMARK    GeneRIF: Sequential stabilization of RNF220 by RLIM and ZC4H2
            during cerebellum development and Shh-group medulloblastoma
            progression.
            Erratum:[J Mol Cell Biol. 2022 May 25;14(2):mjac030. doi:
            10.1093/jmcb/mjac030. PMID: 35639540]
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Lombard,Z., Park,C., Makova,K.D. and Ramsay,M.
  TITLE     A computational approach to candidate gene prioritization for
            X-linked mental retardation using annotation-based binary filtering
            and motif-based linear discriminatory analysis
  JOURNAL   Biol Direct 6, 30 (2011)
   PUBMED   21668950
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Kroncke,K.D. and Klotz,L.O.
  TITLE     Zinc fingers as biologic redox switches?
  JOURNAL   Antioxid Redox Signal 11 (5), 1015-1027 (2009)
   PUBMED   19132878
  REMARK    Review article
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Gamsjaeger,R., Liew,C.K., Loughlin,F.E., Crossley,M. and
            Mackay,J.P.
  TITLE     Sticky fingers: zinc-fingers as protein-recognition motifs
  JOURNAL   Trends Biochem Sci 32 (2), 63-70 (2007)
   PUBMED   17210253
  REMARK    Review article
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Miles,J.H. and Carpenter,N.J.
  TITLE     Unique X-linked mental retardation syndrome with fingertip arches
            and contractures linked to Xq21.31
  JOURNAL   Am J Med Genet 38 (2-3), 215-223 (1991)
   PUBMED   2018061
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP376634.1, CX782941.1 and
            AK001547.1.
            
            Summary: This gene encodes a member of the zinc finger
            domain-containing protein family. This family member has a
            C-terminal zinc finger domain that is characterized by four
            cysteine residues and two histidine residues, and it also includes
            a coiled-coil region. This protein has been detected as an
            autoantigen in hepatocellular carcinoma patients. This gene has
            been identified as a potential candidate for X-linked cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and uses a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (2) has a
            distinct N-terminus and is shorter than isoform 1. Both variants 2
            and 4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.252767.1,
                                           SRR14372080.2213111.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.2"
     Protein         1..201
                     /product="zinc finger C4H2 domain-containing protein
                     isoform 2"
                     /note="hepatocellular carcinoma-associated antigen 127;
                     zinc finger C4H2 domain-containing protein; zinc finger,
                     C4H2 domain containing"
                     /calculated_mol_wt=23380
     Region          1..198
                     /region_name="zf-C4H2"
                     /note="Zinc finger-containing protein; pfam10146"
                     /db_xref="CDD:462963"
     CDS             1..201
                     /gene="ZC4H2"
                     /gene_synonym="HCA127; KIAA1166; MCS; MRXS4; WRWF; WRWFFR;
                     WWS"
                     /coded_by="NM_001243804.2:130..735"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55431.1"
                     /db_xref="GeneID:55906"
                     /db_xref="HGNC:HGNC:24931"
                     /db_xref="MIM:300897"
ORIGIN      
        1 mekikarlka efealeseer hlkeykqemd lllqekmahv eelrlihadi nvmentikqs
       61 endlnklles trrlhdeykp lkehvdalrm tlglqrlpdl ceeeeklsld yfekqkaewq
      121 tepqeppipe slaaaaaaaq qlqvarkqdt rqtatfrqqp ppmkaclsch qqihrnapic
      181 plckaksrsr npkkpkrkqd e
//
LOCUS       NP_002380                392 aa            linear   PRI 20-NOV-2025
DEFINITION  membrane cofactor protein isoform 1 precursor [Homo sapiens].
ACCESSION   NP_002380
VERSION     NP_002380.3
DBSOURCE    REFSEQ: accession NM_002389.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Grodstein,F., Lemos,B., Yang,J., de Paiva Lopes,K., Vialle,R.A.,
            Seyfried,N., Wang,Y., Shireby,G., Hannon,E., Thomas,A., Brookes,K.,
            Mill,J., De Jager,P.L. and Bennett,D.A.
  TITLE     Genetic architecture of epigenetic cortical clock age in brain
            tissue from older individuals: alterations in CD46 and other loci
  JOURNAL   Epigenetics 19 (1), 2392050 (2024)
   PUBMED   39169872
  REMARK    GeneRIF: Genetic architecture of epigenetic cortical clock age in
            brain tissue from older individuals: alterations in CD46 and other
            loci.
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Thi,T.N., Thanh,H.D., Nguyen,V.T., Kwon,S.Y., Moon,C., Hwang,E.C.
            and Jung,C.
  TITLE     Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9
  JOURNAL   Int J Oncol 65 (1) (2024)
   PUBMED   38847230
  REMARK    GeneRIF: Complement regulatory protein CD46 promotes bladder cancer
            metastasis through activation of MMP9.
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Vassiliev,P., Gusev,E., Komelkova,M., Kochetkov,A., Dobrynina,M.
            and Sarapultsev,A.
  TITLE     Computational Analysis of CD46 Protein Interaction with SARS-CoV-2
            Structural Proteins: Elucidating a Putative Viral Entry Mechanism
            into Human Cells
  JOURNAL   Viruses 15 (12), 2297 (2023)
   PUBMED   38140538
  REMARK    GeneRIF: Computational Analysis of CD46 Protein Interaction with
            SARS-CoV-2 Structural Proteins: Elucidating a Putative Viral Entry
            Mechanism into Human Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Richards,A., Kemp,E.J., Liszewski,M.K., Goodship,J.A., Lampe,A.K.,
            Decorte,R., Muslumanoglu,M.H., Kavukcu,S., Filler,G., Pirson,Y.,
            Wen,L.S., Atkinson,J.P. and Goodship,T.H.
  TITLE     Mutations in human complement regulator, membrane cofactor protein
            (CD46), predispose to development of familial hemolytic uremic
            syndrome
  JOURNAL   Proc Natl Acad Sci U S A 100 (22), 12966-12971 (2003)
   PUBMED   14566051
  REMARK    GeneRIF: Mutations predispose to development of familial hemolytic
            uremic syndrome.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Russell,S.M., Sparrow,R.L., McKenzie,I.F. and Purcell,D.F.
  TITLE     Tissue-specific and allelic expression of the complement regulator
            CD46 is controlled by alternative splicing
  JOURNAL   Eur J Immunol 22 (6), 1513-1518 (1992)
   PUBMED   1601037
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Adams,E.M., Brown,M.C., Nunge,M., Krych,M. and Atkinson,J.P.
  TITLE     Contribution of the repeating domains of membrane cofactor protein
            (CD46) of the complement system to ligand binding and cofactor
            activity
  JOURNAL   J Immunol 147 (9), 3005-3011 (1991)
   PUBMED   1717583
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Post,T.W., Liszewski,M.K., Adams,E.M., Tedja,I., Miller,E.A. and
            Atkinson,J.P.
  TITLE     Membrane cofactor protein of the complement system: alternative
            splicing of serine/threonine/proline-rich exons and cytoplasmic
            tails produces multiple isoforms that correlate with protein
            phenotype
  JOURNAL   J Exp Med 174 (1), 93-102 (1991)
   PUBMED   1711570
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Lublin,D.M., Liszewski,M.K., Post,T.W., Arce,M.A., Le Beau,M.M.,
            Rebentisch,M.B., Lemons,L.S., Seya,T. and Atkinson,J.P.
  TITLE     Molecular cloning and chromosomal localization of human membrane
            cofactor protein (MCP). Evidence for inclusion in the multigene
            family of complement-regulatory proteins
  JOURNAL   J Exp Med 168 (1), 181-194 (1988)
   PUBMED   3260937
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB078198.1, X59410.1,
            BC030594.2 and AI589224.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 6, 2003 this sequence version replaced NP_002380.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            protein and is a regulatory part of the complement system. The
            encoded protein has cofactor activity for inactivation of
            complement components C3b and C4b by serum factor I, which protects
            the host cell from damage by complement. In addition, the encoded
            protein can act as a receptor for the Edmonston strain of measles
            virus, human herpesvirus-6, and type IV pili of pathogenic
            Neisseria. Finally, the protein encoded by this gene may be
            involved in the fusion of the spermatozoa with the oocyte during
            fertilization. Mutations at this locus have been associated with
            susceptibility to hemolytic uremic syndrome. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X59410.1, SRR11853566.2682.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.2"
     Protein         1..392
                     /product="membrane cofactor protein isoform 1 precursor"
                     /note="CD46 antigen, complement regulatory protein;
                     membrane cofactor protein (CD46, trophoblast-lymphocyte
                     cross-reactive antigen); complement membrane cofactor
                     protein; measles virus receptor; trophoblast leucocyte
                     common antigen; antigen identified by monoclonal antibody
                     TRA-2-10; trophoblast leukocyte common antigen; CD46
                     molecule, complement regulatory protein"
                     /calculated_mol_wt=39897
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3869
     mat_peptide     35..392
                     /product="membrane cofactor protein isoform 1"
                     /calculated_mol_wt=39897
     Region          54..285
                     /region_name="PHA02927"
                     /note="secreted complement-binding protein; Provisional"
                     /db_xref="CDD:222943"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20010840,
                     ECO:0007744|PDB:3INB, ECO:0007744|PDB:3L89; propagated
                     from UniProtKB/Swiss-Prot (P15529.3)"
     Site            163
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            290
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Region          291..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            291
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            292
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            298
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            300
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            302
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            303
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            304
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            305
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            306
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            307
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            309
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            312
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            313
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            315
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            320
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            326
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            344..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P15529.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10657632; propagated from
                     UniProtKB/Swiss-Prot (P15529.3)"
     CDS             1..392
                     /gene="CD46"
                     /gene_synonym="AHUS2; MCP; MIC10; TLX; TRA2.10"
                     /coded_by="NM_002389.4:176..1354"
                     /note="isoform 1 precursor is encoded by transcript
                     variant a"
                     /db_xref="CCDS:CCDS1485.1"
                     /db_xref="GeneID:4179"
                     /db_xref="HGNC:HGNC:6953"
                     /db_xref="MIM:120920"
ORIGIN      
        1 meppgrrecp fpswrfpgll laamvlllys fsdaceeppt feameligkp kpyyeigerv
       61 dykckkgyfy ipplathtic drnhtwlpvs ddacyretcp yirdplngqa vpangtyefg
      121 yqmhficneg yyligeeily celkgsvaiw sgkppicekv lctpppkikn gkhtfsevev
      181 feyldavtys cdpapgpdpf sligestiyc gdnsvwsraa peckvvkcrf pvvengkqis
      241 gfgkkfyyka tvmfecdkgf yldgsdtivc dsnstwdppv pkclkvlpps stkppalshs
      301 vstssttksp assasgprpt ykppvsnypg ypkpeegild sldvwviavi viaivvgvav
      361 icvvpyrylq rrkkkgtylt dethrevkft sl
//
LOCUS       NP_075012                262 aa            linear   PRI 20-NOV-2025
DEFINITION  survival motor neuron protein isoform b [Homo sapiens].
ACCESSION   NP_075012 XP_942045
VERSION     NP_075012.1
DBSOURCE    REFSEQ: accession NM_022874.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Nurputra,D.K., Sofian,J., Iskandar,K., Triono,A., Herini,E.S.,
            Sunartini and Ulhaq,Z.S.
  TITLE     Multidisciplinary approach on divergent outcomes in spinal muscular
            atrophies: comparing DYNC1H1 and SMN1 gene mutations
  JOURNAL   Neurol Sci 45 (9), 4583-4588 (2024)
   PUBMED   38806879
  REMARK    GeneRIF: Multidisciplinary approach on divergent outcomes in spinal
            muscular atrophies: comparing DYNC1H1 and SMN1 gene mutations.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Polverini,E., Squeri,P. and Gherardi,V.
  TITLE     Effect of E134K pathogenic mutation of SMN protein on SMN-SmD1
            interaction, with implication in spinal muscular atrophy: A
            molecular dynamics study
  JOURNAL   Int J Biol Macromol 275 (Pt 2), 133663 (2024)
   PUBMED   38969036
  REMARK    GeneRIF: Effect of E134K pathogenic mutation of SMN protein on
            SMN-SmD1 interaction, with implication in spinal muscular atrophy:
            A molecular dynamics study.
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Li,L., Menezes,M.P., Smith,M., Forbes,R., Zuchner,S., Burgess,A.,
            Woodcock,I.R., Delatycki,M.B. and Yiu,E.M.
  TITLE     Rare homozygous disease-associated sequence variants in children
            with spinal muscular atrophy: a phenotypic description and review
            of the literature
  JOURNAL   Neuromuscul Disord 37, 29-35 (2024)
   PUBMED   38520993
  REMARK    GeneRIF: Rare homozygous disease-associated sequence variants in
            children with spinal muscular atrophy: a phenotypic description and
            review of the literature.
            Review article
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Valsecchi,V., Errico,F., Bassareo,V., Marino,C., Nuzzo,T.,
            Brancaccio,P., Laudati,G., Casamassa,A., Grimaldi,M., D'Amico,A.,
            Carta,M., Bertini,E., Pignataro,G., D'Ursi,A.M. and Usiello,A.
  TITLE     SMN deficiency perturbs monoamine neurotransmitter metabolism in
            spinal muscular atrophy
  JOURNAL   Commun Biol 6 (1), 1155 (2023)
   PUBMED   37957344
  REMARK    GeneRIF: SMN deficiency perturbs monoamine neurotransmitter
            metabolism in spinal muscular atrophy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Bussaglia,E., Clermont,O., Tizzano,E., Lefebvre,S., Burglen,L.,
            Cruaud,C., Urtizberea,J.A., Colomer,J., Munnich,A., Baiget,M. et
            al.
  TITLE     A frame-shift deletion in the survival motor neuron gene in Spanish
            spinal muscular atrophy patients
  JOURNAL   Nat Genet 11 (3), 335-337 (1995)
   PUBMED   7581461
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Gennarelli,M., Lucarelli,M., Capon,F., Pizzuti,A., Merlini,L.,
            Angelini,C., Novelli,G. and Dallapiccola,B.
  TITLE     Survival motor neuron gene transcript analysis in muscles from
            spinal muscular atrophy patients
  JOURNAL   Biochem Biophys Res Commun 213 (1), 342-348 (1995)
   PUBMED   7639755
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Lefebvre,S., Burglen,L., Reboullet,S., Clermont,O., Burlet,P.,
            Viollet,L., Benichou,B., Cruaud,C., Millasseau,P., Zeviani,M. et
            al.
  TITLE     Identification and characterization of a spinal muscular
            atrophy-determining gene
  JOURNAL   Cell 80 (1), 155-165 (1995)
   PUBMED   7813012
REFERENCE   9  (residues 1 to 262)
  AUTHORS   van der Steege,G., Draaijers,T.G., Grootscholten,P.M., Osinga,J.,
            Anzevino,R., Velona,I., Den Dunnen,J.T., Scheffer,H., Brahe,C., van
            Ommen,G.J. et al.
  TITLE     A provisional transcript map of the spinal muscular atrophy (SMA)
            critical region
  JOURNAL   Eur J Hum Genet 3 (2), 87-95 (1995)
   PUBMED   7552146
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Prior,T.W., Leach,M.E. and Finanger,E.L.
  TITLE     Spinal Muscular Atrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139834.2 and BC062723.1.
            
            On Mar 4, 2006 this sequence version replaced XP_942045.1.
            
            Summary: This gene is part of a 500 kb inverted duplication on
            chromosome 5q13. This duplicated region contains at least four
            genes and repetitive elements which make it prone to rearrangements
            and deletions. The repetitiveness and complexity of the sequence
            have also caused difficulty in determining the organization of this
            genomic region. The telomeric and centromeric copies of this gene
            are nearly identical and encode the same protein. However,
            mutations in this gene, the telomeric copy, are associated with
            spinal muscular atrophy; mutations in the centromeric copy do not
            lead to disease. The centromeric copy may be a modifier of disease
            caused by mutation in the telomeric copy. The critical sequence
            difference between the two genes is a single nucleotide in exon 7,
            which is thought to be an exon splice enhancer. Note that the nine
            exons of both the telomeric and centromeric copies are designated
            historically as exon 1, 2a, 2b, and 3-8. It is thought that gene
            conversion events may involve the two genes, leading to varying
            copy numbers of each gene. The protein encoded by this gene
            localizes to both the cytoplasm and the nucleus. Within the
            nucleus, the protein localizes to subnuclear bodies called gems
            which are found near coiled bodies containing high concentrations
            of small ribonucleoproteins (snRNPs). This protein forms
            heteromeric complexes with proteins such as SIP1 and GEMIN4, and
            also interacts with several proteins known to be involved in the
            biogenesis of snRNPs, such as hnRNP U protein and the small
            nucleolar RNA binding protein. Multiple transcript variants
            encoding distinct isoforms have been described. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (b) lacks an alternate in-frame
            exon in the 3' CDS compared to variant d. The resulting protein
            (isoform b) is shorter but has the same N- and C- termini compared
            to isoform d.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803617.93871.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..262
                     /product="survival motor neuron protein isoform b"
                     /note="gemin-1; component of gems 1; survival motor neuron
                     1 protein; tudor domain containing 16A"
                     /calculated_mol_wt=28403
     Region          26..259
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     CDS             1..262
                     /gene="SMN1"
                     /gene_synonym="BCD541; GEMIN1; SMA; SMA1; SMA2; SMA3;
                     SMA4; SMA@; SMN; SMNT; T-BCD541; TDRD16A"
                     /coded_by="NM_022874.2:164..952"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS34182.1"
                     /db_xref="GeneID:6606"
                     /db_xref="HGNC:HGNC:11117"
                     /db_xref="MIM:600354"
ORIGIN      
        1 mamssggsgg gvpeqedsvl frrgtgqsdd sdiwddtali kaydkavasf khalkngdic
       61 etsgkpkttp krkpakknks qkkntaaslq qwkvgdkcsa iwsedgciyp atiasidfkr
      121 etcvvvytgy gnreeqnlsd llspicevan nieqnaqene nesqvstdes ensrspgnks
      181 dnikpksapw nsflpppppm pgprlgpgki ipppppicpd slddadalgs mliswymsgy
      241 htgyymgfrq nqkegrcshs ln
//
LOCUS       NP_071440                399 aa            linear   PRI 20-NOV-2025
DEFINITION  ras-related GTP-binding protein C isoform 1 [Homo sapiens].
ACCESSION   NP_071440
VERSION     NP_071440.1
DBSOURCE    REFSEQ: accession NM_022157.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Reijnders,M.R.F., Seibt,A., Brugger,M., Lamers,I.J.C., Ott,T.,
            Klaas,O., Horvath,J., Rose,A.M.S., Craghill,I.M., Brunet,T.,
            Graf,E., Mayerhanser,K., Hellebrekers,D., Pauck,D., Neuen-Jacob,E.,
            Rodenburg,R.J.T., Wieczorek,D., Klee,D., Mayatepek,E., Driessen,G.,
            Bindermann,R., Averdunk,L., Lohmeier,K., Sinnema,M.,
            Stegmann,A.P.A., Roepman,R., Poulter,J.A. and Distelmaier,F.
  TITLE     De novo missense variants in RRAGC lead to a fatal mTORopathy of
            early childhood
  JOURNAL   Genet Med 25 (7), 100838 (2023)
   PUBMED   37057673
  REMARK    GeneRIF: De novo missense variants in RRAGC lead to a fatal
            mTORopathy of early childhood.
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Cui,Z., Napolitano,G., de Araujo,M.E.G., Esposito,A.,
            Monfregola,J., Huber,L.A., Ballabio,A. and Hurley,J.H.
  TITLE     Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex
  JOURNAL   Nature 614 (7948), 572-579 (2023)
   PUBMED   36697823
  REMARK    GeneRIF: Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator
            megacomplex.
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Sekiguchi,T., Todaka,Y., Wang,Y., Hirose,E., Nakashima,N. and
            Nishimoto,T.
  TITLE     A novel human nucleolar protein, Nop132, binds to the G proteins,
            RRAG A/C/D
  JOURNAL   J Biol Chem 279 (9), 8343-8350 (2004)
   PUBMED   14660641
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Park,I.H., Bachmann,R., Shirazi,H. and Chen,J.
  TITLE     Regulation of ribosomal S6 kinase 2 by mammalian target of
            rapamycin
  JOURNAL   J Biol Chem 277 (35), 31423-31429 (2002)
   PUBMED   12087098
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Sekiguchi,T., Hirose,E., Nakashima,N., Ii,M. and Nishimoto,T.
  TITLE     Novel G proteins, Rag C and Rag D, interact with GTP-binding
            proteins, Rag A and Rag B
  JOURNAL   J Biol Chem 276 (10), 7246-7257 (2001)
   PUBMED   11073942
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI461665.1, AK315791.1,
            BC016668.1, CA449149.1, CX761032.1, CB132041.1, HY264464.1,
            HY202961.1 and BQ003663.1.
            
            Summary: This gene encodes a member of the GTR/RAG GTP-binding
            protein family. The encoded protein is a monomeric guanine
            nucleotide-binding protein which forms a heterodimer with RRAGA and
            RRAGB and is primarily localized to the cytoplasm. The encoded
            protein promotes intracellular localization of the mTOR complex.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1000533.1,
                                           SRR1803613.61984.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373001.4/ ENSP00000362092.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..399
                     /product="ras-related GTP-binding protein C isoform 1"
                     /note="Rag C protein; ras-related GTP-binding protein C;
                     GTPase-interacting protein 2"
                     /calculated_mol_wt=44093
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB90.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HB90.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HB90.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HB90.1)"
     Region          63..237
                     /region_name="RagC_like"
                     /note="Rag GTPase, subfamily of Ras-related GTPases,
                     includes Ras-related GTP-binding proteins C and D;
                     cd11385"
                     /db_xref="CDD:206745"
     Site            68..75
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206745"
     Site            order(73..76,119,178..179,181,219..221)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206745"
     Site            96
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206745"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99K70; propagated from
                     UniProtKB/Swiss-Prot (Q9HB90.1)"
     Site            100..102
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206745"
     Site            116..119
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206745"
     Site            order(118..119,138..139)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206745"
     Site            178..181
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206745"
     Site            219..221
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206745"
     CDS             1..399
                     /gene="RRAGC"
                     /gene_synonym="GTR2; LNGODS; LNGOS; RAGC; TIB929"
                     /coded_by="NM_022157.4:127..1326"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS430.1"
                     /db_xref="GeneID:64121"
                     /db_xref="HGNC:HGNC:19902"
                     /db_xref="MIM:608267"
ORIGIN      
        1 mslqygaeet plagsygaad sfpkdfgygv eeeeeeaaaa gggvgagagg gcgpggadss
       61 kprillmglr rsgkssiqkv vfhkmspnet lflestnkiy kddisnssfv nfqiwdfpgq
      121 mdffdptfdy emifrgtgal iyvidaqddy mealtrlhit vskaykvnpd mnfevfihkv
      181 dglsddhkie tqrdihqran ddladaglek lhlsfyltsi ydhsifeafs kvvqklipql
      241 ptlenllnif isnsgiekaf lfdvvskiyi atdsspvdmq syelccdmid vvidvsciyg
      301 lkedgsgsay dkesmaiikl nnttvlylke vtkflalvci lreesferkg lidynfhcfr
      361 kaihevfevg vtshrscghq tsasslkalt hngtprnai
//
LOCUS       NP_001354632             885 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform nnn [Homo sapiens].
ACCESSION   NP_001354632
VERSION     NP_001354632.1
DBSOURCE    REFSEQ: accession NM_001367703.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 885)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 885)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 885)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 885)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..885
                     /product="SUN domain-containing protein 1 isoform nnn"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=98238
     Region          62..422
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          548..601
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(548,551..552,555,558..559,562..563,565..566,
                     569..570,572..573,576..577,579..580,583,586..587,590,
                     593..594,597..598,600..601)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          560..>693
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          678..736
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          779..883
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..885
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367703.1:52..2709"
                     /note="isoform nnn is encoded by transcript variant 66"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca gyfllqilrr
      361 igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv flltrclrni
      421 ckflvllipl flllaglslr gqgnffsflp vlnwasmhrt qrvddpqdvf kpttsrlkqp
      481 lqgdseafpw hwmsgveqqv aslsgqchhh genlrelttl lqklqarvdq meggaagpsa
      541 svrdavgqpp retdfmafhq ehevrmshle dilgklreks eaiqkeleqt kqktisavge
      601 qllptvehlq leldqlksel sswrhvktgc etvdavqerv dvqvremvkl lfsedqqggs
      661 leqllqrfss qfvskgdlqt mlrdlqlqil rnvthhvsvt kqlptseavv savseagasg
      721 iteaqaraiv nsalklysqd ktgmvdfale sgggsilstr csetyetkta lmslfgiplw
      781 yfsqsprvvi qpdiypgncw afkgsqgylv vrlsmmihpa aftlehipkt lsptgnissa
      841 pkdfavykrp ddtafqivel rifsnwghpe ytclyrfrvh gepvk
//
LOCUS       NP_001316524             608 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_001316524 XP_011523008
VERSION     NP_001316524.1
DBSOURCE    REFSEQ: accession NM_001329595.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Qiu,Q.M., Liu,G., Li,W.N., Shi,Q.W., Zhu,F.X. and Lu,G.X.
  TITLE     [Mutation of KLHL-10 in idiopathic infertile males with
            azoospermia, oligospermia or asthenospermia]
  JOURNAL   Zhonghua Nan Ke Xue 15 (11), 974-979 (2009)
   PUBMED   20218307
  REMARK    GeneRIF: The KLHL-10 gene is not a major contributor to
            azoospermia, oligospermia or asthenospermia in Chinese population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Yatsenko,A.N., Roy,A., Chen,R., Ma,L., Murthy,L.J., Yan,W.,
            Lamb,D.J. and Matzuk,M.M.
  TITLE     Non-invasive genetic diagnosis of male infertility using
            spermatozoal RNA: KLHL10 mutations in oligozoospermic patients
            impair homodimerization
  JOURNAL   Hum Mol Genet 15 (23), 3411-3419 (2006)
   PUBMED   17047026
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Yan,W., Ma,L., Burns,K.H. and Matzuk,M.M.
  TITLE     Haploinsufficiency of kelch-like protein homolog 10 causes
            infertility in male mice
  JOURNAL   Proc Natl Acad Sci U S A 101 (20), 7793-7798 (2004)
   PUBMED   15136734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA361625.1 and AY495339.1.
            
            On Jul 20, 2016 this sequence version replaced XP_011523008.1.
            
            Summary: The protein encoded by this gene belongs to the kelch
            repeat-containing family, and contains an N-terminal BTB/POZ domain
            a BACK domain and six C-terminal kelch repeats. Kelch domains are
            thought to form a four stranded beta-sheet blade structure that can
            fold into a beta-propeller domain when multiple kelch repeats are
            found together. Mutations in this gene have been associated with
            oligozoospermia in some infertile males. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein (isoform
            1).
            
            ##Evidence-Data-START##
            CDS exon combination :: AY495339.1, HM005417.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..608
                     /product="kelch-like protein 10 isoform 1"
                     /note="kelch-like protein 10; testicular tissue protein Li
                     104"
                     /calculated_mol_wt=68811
     Region          36..572
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          292..339
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          329..372
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          340..386
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          376..420
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          388..433
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          423..466
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          434..480
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          470..513
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          481..527
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6JEL3; propagated from
                     UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          517..561
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          529..574
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     CDS             1..608
                     /gene="KLHL10"
                     /gene_synonym="SPGF11"
                     /coded_by="NM_001329595.1:276..2102"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42340.1"
                     /db_xref="GeneID:317719"
                     /db_xref="HGNC:HGNC:18829"
                     /db_xref="MIM:608778"
ORIGIN      
        1 memesaaast rfhqphmerk msamaceifn elrlegklcd vvikvngfef sahknilcsc
       61 ssyfralfts gwnntekkvy nipgispdmm kliieyaytr tvpitpdnve kllaaadqfn
      121 imgivrgcce flkselcldn cigickftdy yycpelrqka ymfilhnfee mvkvsaefle
      181 lsvtelkdii ekdelnvkqe davfeailkw ishdpqnrkq hisillpkvr lalmhaeyfm
      241 nnvkmndyvk dseeckpvii nalkamydln mngpsnsdft npltrprlpy ailfaiggws
      301 ggsptnaiea ydaradrwvn vtceeespra yhgaaylkgy vyiiggfdsv dyfnsvkrfd
      361 pvkktwhqva pmhsrrcyvs vtvlgnfiya mggfdgyvrl ntaeryepet nqwtliapmh
      421 eqrsdasatt lygkvyicgg fngneclfta evyntesnqw tviapmrsrr sgigviayge
      481 hvyavggfdg anrlrsaeay spvantwrti ptmfnprsnf gievvddllf vvggfngftt
      541 tfnvecydek tdewydahdm siyrsalscc vvpglanvee yaarrdnfpg lalrdevkys
      601 aststlpv
//
LOCUS       NP_001138843             626 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 3 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001138843
VERSION     NP_001138843.1
DBSOURCE    REFSEQ: accession NM_001145371.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Masuda,S., Onishi,H., Iwamoto,N., Imaizumi,A., Koga,S., Nagao,S.,
            Sakanashi,K., Itoyama,S., Fujimura,A., Komune,N., Kogo,R.,
            Umebayashi,M., Morisaki,T. and Nakagawa,T.
  TITLE     Inhibition of PTPN3 Expressed in Activated Lymphocytes Enhances the
            Antitumor Effects of Anti-PD-1 Therapy in Head and Neck Cancer,
            Especially in Hypoxic Environments
  JOURNAL   J Immunother 47 (3), 89-97 (2024)
   PUBMED   38297883
  REMARK    GeneRIF: Inhibition of PTPN3 Expressed in Activated Lymphocytes
            Enhances the Antitumor Effects of Anti-PD-1 Therapy in Head and
            Neck Cancer, Especially in Hypoxic Environments.
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Zhou,Z., Lin,Z., Wang,M., Wang,L., Ji,Y., Yang,J., Yang,Y., Zhu,G.
            and Liu,T.
  TITLE     Identification and verification of PTPN3 as a novel biomarker in
            predicting cancer prognosis, immunity, and immunotherapeutic
            efficacy
  JOURNAL   Eur J Med Res 29 (1), 12 (2024)
   PUBMED   38173048
  REMARK    GeneRIF: Identification and verification of PTPN3 as a novel
            biomarker in predicting cancer prognosis, immunity, and
            immunotherapeutic efficacy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and
            Tonks,N.K.
  TITLE     Serine phosphorylation-dependent association of the band
            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta
            protein
  JOURNAL   J Biol Chem 272 (43), 27281-27287 (1997)
   PUBMED   9341175
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and
            Yachi,A.
  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase
            PTPH1 mRNA in human hepatocellular carcinoma
  JOURNAL   J Gastroenterol 29 (6), 727-732 (1994)
   PUBMED   7874267
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,
            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.
  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a
            cytosolic protein tyrosine phosphatase homologous to
            cytoskeletal-associated proteins
  JOURNAL   Int J Cancer 55 (6), 947-951 (1993)
   PUBMED   8253532
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,
            Adachi,M., Imai,K. and Yachi,A.
  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human
            colon
  JOURNAL   Tumour Biol 13 (3), 180-186 (1992)
   PUBMED   1626183
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Yang,Q. and Tonks,N.K.
  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine
            phosphatase with homology to the cytoskeletal-associated proteins
            band 4.1, ezrin, and talin
  JOURNAL   Proc Natl Acad Sci U S A 88 (14), 5949-5953 (1991)
   PUBMED   1648725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC342461.1, AK296388.1,
            BC126117.1, BC033716.1, DB173093.1, AK096975.1 and AL359963.29.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This protein contains a C-terminal PTP
            domain and an N-terminal domain homologous to the band 4.1
            superfamily of cytoskeletal-associated proteins. P97, a cell cycle
            regulator involved in a variety of membrane related functions, has
            been shown to be a substrate of this PTP. This PTP was also found
            to interact with, and be regulated by adaptor protein 14-3-3 beta.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, and
            initiates translation from an in-frame downstream AUG, resulting in
            an isoform (5) with a shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.212223.1,
                                           SRR1660805.202861.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..626
                     /product="tyrosine-protein phosphatase non-receptor type 3
                     isoform 5"
                     /EC_number="3.1.3.48"
                     /note="cytoskeletal-associated protein tyrosine
                     phosphatase; protein-tyrosine phosphatase H1"
                     /calculated_mol_wt=70849
     Region          <1..22
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          219..308
                     /region_name="PDZ_PTPN3-4-like"
                     /note="PDZ domain of tyrosine-protein phosphatase
                     non-receptor type 3 (PTPN3), tyrosine-protein phosphatase
                     non-receptor type 4 (PTNP4), and related domains; cd06706"
                     /db_xref="CDD:467190"
     Site            order(233..239,251,254,285,289,292..293)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467190"
     Region          344..617
                     /region_name="PTPc-N3"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 3; cd14600"
                     /db_xref="CDD:350448"
     CDS             1..626
                     /gene="PTPN3"
                     /gene_synonym="PTP-H1; PTPH1"
                     /coded_by="NM_001145371.2:386..2266"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:5774"
                     /db_xref="HGNC:HGNC:9655"
                     /db_xref="MIM:176877"
ORIGIN      
        1 mlnyrscknl wkscvehhtf fqakkllpqe knvlsqywtm gsrntkksvn nqyckkvigg
       61 mvwnpamrrs lsvehletks lpsrsppitp nwrsprlrhe irkprhssad nlanemtyit
      121 etedvfytyk gslapqdsds evsqnrsphq eslsennpaq syltqkssss vspssnapgs
      181 cspdgvdqql lddfhrvtkg gstedasqyy cdkndngdsy lvliritpde dgkfgfnlkg
      241 gvdqkmplvv srinpespad tcipklnegd qivlingrdi sehthdqvvm fikasreshs
      301 relalvirrr avrsfadfks edelnqlfpe aifpmcpegg dtlegsmaql kkglesgtvl
      361 iqfeqlyrkk pglaitfakl pqnldknryk dvlpydttrv llqgnedyin asyvnmeipa
      421 anlvnkyiat qgplphtcaq fwqvvwdqkl slivmlttlt ergrtkchqy wpdppdvmnh
      481 ggfhiqcqse dctiayvsre mlvtntqtge ehtvthlqyv awpdhgvpdd ssdflefvny
      541 vrslrvdsep vlvhcsagig rtgvlvtmet amclternlp iypldivrkm rdqrammvqt
      601 ssqykfvcea ilrvyeeglv qmldps
//
LOCUS       NP_000800                554 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-4 isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_000800
VERSION     NP_000800.2
DBSOURCE    REFSEQ: accession NM_000809.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Sajan,S.A., Gradisch,R., Vogel,F.D., Coffey,A.J., Salyakina,D.,
            Soler,D., Jayakar,P., Jayakar,A., Bianconi,S.E., Cooper,A.H.,
            Liu,S., William,N., Benkel-Herrenbruck,I., Maiwald,R., Heller,C.,
            Biskup,S., Leiz,S., Westphal,D.S., Wagner,M., Clarke,A.,
            Stockner,T., Ernst,M., Kesari,A. and Krenn,M.
  TITLE     De novo variants in GABRA4 are associated with a neurological
            phenotype including developmental delay, behavioral abnormalities
            and epilepsy
  JOURNAL   Eur J Hum Genet 32 (8), 912-919 (2024)
   PUBMED   38565639
  REMARK    GeneRIF: De novo variants in GABRA4 are associated with a
            neurological phenotype including developmental delay, behavioral
            abnormalities and epilepsy.
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Sente,A., Desai,R., Naydenova,K., Malinauskas,T., Jounaidi,Y.,
            Miehling,J., Zhou,X., Masiulis,S., Hardwick,S.W., Chirgadze,D.Y.,
            Miller,K.W. and Aricescu,A.R.
  TITLE     Differential assembly diversifies GABAA receptor structures and
            signalling
  JOURNAL   Nature 604 (7904), 190-194 (2022)
   PUBMED   35355020
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Vogel,F.D., Krenn,M., Westphal,D.S., Graf,E., Wagner,M., Leiz,S.,
            Koniuszewski,F., Auge-Stock,M., Kramer,G., Scholze,P. and Ernst,M.
  TITLE     A de novo missense variant in GABRA4 alters receptor function in an
            epileptic and neurodevelopmental phenotype
  JOURNAL   Epilepsia 63 (4), e35-e41 (2022)
   PUBMED   35152403
  REMARK    GeneRIF: A de novo missense variant in GABRA4 alters receptor
            function in an epileptic and neurodevelopmental phenotype.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Han,W., Shepard,R.D. and Lu,W.
  TITLE     Regulation of GABAARs by Transmembrane Accessory Proteins
  JOURNAL   Trends Neurosci 44 (2), 152-165 (2021)
   PUBMED   33234346
  REMARK    Review article
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Riley,J.D., Delahunty,C., Alsadah,A., Mazzola,S. and Astbury,C.
  TITLE     Further evidence of GABRA4 and TOP3B as autism susceptibility genes
  JOURNAL   Eur J Med Genet 63 (5), 103876 (2020)
   PUBMED   32028044
  REMARK    GeneRIF: Further evidence of GABRA4 and TOP3B as autism
            susceptibility genes.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Whiting,P.J., Bonnert,T.P., McKernan,R.M., Farrar,S., Le
            Bourdelles,B., Heavens,R.P., Smith,D.W., Hewson,L., Rigby,M.R.,
            Sirinathsinghji,D.J., Thompson,S.A. and Wafford,K.A.
  TITLE     Molecular and functional diversity of the expanding GABA-A receptor
            gene family
  JOURNAL   Ann N Y Acad Sci 868, 645-653 (1999)
   PUBMED   10414349
  REMARK    Review article
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Ebert,V., Scholze,P. and Sieghart,W.
  TITLE     Extensive heterogeneity of recombinant gamma-aminobutyric acidA
            receptors expressed in alpha 4 beta 3 gamma 2-transfected human
            embryonic kidney 293 cells
  JOURNAL   Neuropharmacology 35 (9-10), 1323-1330 (1996)
   PUBMED   9014148
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Yang,W., Drewe,J.A. and Lan,N.C.
  TITLE     Cloning and characterization of the human GABAA receptor alpha 4
            subunit: identification of a unique diazepam-insensitive binding
            site
  JOURNAL   Eur J Pharmacol 291 (3), 319-325 (1995)
   PUBMED   8719416
REFERENCE   9  (residues 1 to 554)
  AUTHORS   McLean,P.J., Farb,D.H. and Russek,S.J.
  TITLE     Mapping of the alpha 4 subunit gene (GABRA4) to human chromosome 4
            defines an alpha 2-alpha 4-beta 1-gamma 1 gene cluster: further
            evidence that modern GABAA receptor gene clusters are derived from
            an ancestral cluster
  JOURNAL   Genomics 26 (3), 580-586 (1995)
   PUBMED   7607683
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK090780.1, AC107383.3 and
            BC037926.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 4, 2003 this sequence version replaced NP_000800.1.
            
            Summary: Gamma-aminobutyric acid (GABA) is the major inhibitory
            neurotransmitter in the mammalian brain where it acts at GABA-A
            receptors, which are ligand-gated chloride channels. Chloride
            conductance of these channels can be modulated by agents such as
            benzodiazepines that bind to the GABA-A receptor. At least 16
            distinct subunits of GABA-A receptors have been identified. This
            gene encodes subunit alpha-4, which is involved in the etiology of
            autism and eventually increases autism risk through interaction
            with another subunit, gamma-aminobutyric acid receptor beta-1
            (GABRB1). Alternatively spliced transcript variants encoding
            different isoforms have been found in this gene.[provided by
            RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.222538.1,
                                           SRR1660809.260239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264318.4/ ENSP00000264318.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..554
                     /product="gamma-aminobutyric acid receptor subunit alpha-4
                     isoform 1 precursor"
                     /note="gamma-aminobutyric acid receptor subunit alpha-4;
                     GABA(A) receptor, alpha 4; gamma-aminobutyric acid A
                     receptor alpha 4; gamma-aminobutyric acid (GABA) A
                     receptor, alpha 4; gamma-aminobutyric acid type A receptor
                     alpha4 subunit; GABAAR subunit alpha-4"
                     /calculated_mol_wt=58064
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48169.2)"
                     /calculated_mol_wt=3577
     Region          13..541
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     36..554
                     /product="Gamma-aminobutyric acid receptor subunit
                     alpha-4. /id=PRO_0000000441"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
                     /calculated_mol_wt=58064
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P48169.2)"
     Region          57..255
                     /region_name="LGIC_ECD_GABAAR_A4"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-4 (GABAAR-A4 or GABRA4); cd19037"
                     /db_xref="CDD:349838"
     Site            order(70,98)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349838"
     Site            order(82,84..85,90..91,98,100..101,118,120..121,130..135,
                     138,140,142..143,149..151,153,163..165,193,255)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349838"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:35355020,
                     ECO:0007744|PDB:7QN7; propagated from UniProtKB/Swiss-Prot
                     (P48169.2)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:35355020,
                     ECO:0007744|PDB:7QN7; propagated from UniProtKB/Swiss-Prot
                     (P48169.2)"
     Region          172..186
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349838"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Site            319..341
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Region          350..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Region          397..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Region          452..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Region          495..515
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     Site            518..540
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P48169.2)"
     CDS             1..554
                     /gene="GABRA4"
                     /coded_by="NM_000809.4:158..1822"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3473.1"
                     /db_xref="GeneID:2557"
                     /db_xref="HGNC:HGNC:4078"
                     /db_xref="MIM:137141"
ORIGIN      
        1 mvsakkvpai alsagvsfal lrflclavcl nespgqnqke eklctenftr ildslldgyd
       61 nrlrpgfggp vtevktdiyv tsfgpvsdve meytmdvffr qtwidkrlky dgpieilrln
      121 nmmvtkvwtp dtffrngkks vshnmtapnk lfrimrngti lytmrltisa ecpmrlvdfp
      181 mdghacplkf gsyaypksem iytwtkgpek svevpkesss lvqydligqt vssetiksit
      241 geyivmtvyf hlrrkmgyfm iqtyipcimt vilsqvsfwi nkesvpartv fgittvltmt
      301 tlsisarhsl pkvsyatamd wfiavcfafv fsaliefaav nyftniqmek akrktskppq
      361 evpaapvqre khpeaplqnt nanlnmrkrt nalvhsesdv gnrtevgnhs sksstvvqes
      421 skgtprsyla sspnpfsran aaetisaara lpsasptsir tgymprkasv gsastrhvfg
      481 srlqrikttv ntigatgkls atpppsappp sgsgtskidk yarilfpvtf gafnmvywvv
      541 ylskdtmeks eslm
//
LOCUS       NP_001357091             676 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001357091 XP_024308249
VERSION     NP_001357091.1
DBSOURCE    REFSEQ: accession NM_001370162.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            On May 2, 2019 this sequence version replaced XP_024308249.1.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.117974.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..676
                     /product="synaptotagmin-like protein 4 isoform 2"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=76624
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..>622
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..676
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001370162.1:277..2307"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtvniqpili ecllcartrg rlssctdmct dkcdpdcqel
      661 hnlptkkiyk ptymdq
//
LOCUS       NP_001341029             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341029 XP_016879187
VERSION     NP_001341029.1
DBSOURCE    REFSEQ: accession NM_001354100.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 4, 2017 this sequence version replaced XP_016879187.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.174896.1,
                                           SRR1660807.86629.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354100.2:1131..1895"
                     /note="isoform a is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_060108                208 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 18 [Homo
            sapiens].
ACCESSION   NP_060108 XP_003403766
VERSION     NP_060108.2
DBSOURCE    REFSEQ: accession NM_017638.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Xuan,Y. and Wang,Y.
  TITLE     Long non-coding RNA SNHG3 promotes progression of gastric cancer by
            regulating neighboring MED18 gene methylation
  JOURNAL   Cell Death Dis 10 (10), 694 (2019)
   PUBMED   31534128
  REMARK    GeneRIF: Long non-coding RNA SNHG3 promotes progression of gastric
            cancer by regulating neighboring MED18 gene methylation.
            Erratum:[Cell Death Dis. 2022 Mar 11;13(3):226. doi:
            10.1038/s41419-022-04698-9. PMID: 35277490]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Parmely,T.J., Florens,L., Zybailov,B.,
            Swanson,S.K., Banks,C.A., Jin,J., Cai,Y., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     A set of consensus mammalian mediator subunits identified by
            multidimensional protein identification technology
  JOURNAL   Mol Cell 14 (5), 685-691 (2004)
   PUBMED   15175163
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Tomomori-Sato,C., Sato,S., Parmely,T.J., Banks,C.A., Sorokina,I.,
            Florens,L., Zybailov,B., Washburn,M.P., Brower,C.S., Conaway,R.C.
            and Conaway,J.W.
  TITLE     A mammalian mediator subunit that shares properties with
            Saccharomyces cerevisiae mediator subunit Cse2
  JOURNAL   J Biol Chem 279 (7), 5846-5851 (2004)
   PUBMED   14638676
REFERENCE   8  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Parmely,T.J., Sorokina,I.,
            Brower,C.S., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian homolog of Drosophila melanogaster transcriptional
            coactivator intersex is a subunit of the mammalian Mediator complex
  JOURNAL   J Biol Chem 278 (50), 49671-49674 (2003)
   PUBMED   14576168
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   10 (residues 1 to 208)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK000052.1 and AL353622.33.
            
            On or before Aug 3, 2011 this sequence version replaced
            XP_003403766.1, NP_060108.1.
            
            Summary: MED18 is a component of the Mediator complex, which is a
            coactivator for DNA-binding factors that activate transcription via
            RNA polymerase II (Sato et al., 2003 [PubMed 12584197]).[supplied
            by OMIM, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.176063.1,
                                           SRR1803613.139732.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373842.9/ ENSP00000362948.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..208
                     /product="mediator of RNA polymerase II transcription
                     subunit 18"
                     /note="TRAP/mediator complex subunit p28b; mediator of RNA
                     polymerase II transcription, subunit 18 homolog"
                     /calculated_mol_wt=23532
     Region          19..203
                     /region_name="Med18"
                     /note="Med18 protein; pfam09637"
                     /db_xref="CDD:462845"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BUE0.1)"
     CDS             1..208
                     /gene="MED18"
                     /gene_synonym="p28b; SRB5"
                     /coded_by="NM_017638.3:208..834"
                     /db_xref="CCDS:CCDS322.1"
                     /db_xref="GeneID:54797"
                     /db_xref="HGNC:HGNC:25944"
                     /db_xref="MIM:612384"
ORIGIN      
        1 meappvtmmp vtggtinmme yllqgsvldh sleslihrlr glcdnmepet fldhemvfll
       61 kgqqaspfvl rarrsmdrag apwhlrylgq pemgdknrha lvrncvdiat senltdflme
      121 mgfrmdhefv akghlfrkgi mkimvykifr ilvpgntdst ealslsylve lsvvapagqd
      181 mvsddmknfa eqlkplvhle kidpkrlm
//
LOCUS       NP_004417               1004 aa            linear   PRI 20-NOV-2025
DEFINITION  polyhomeotic-like protein 1 isoform a [Homo sapiens].
ACCESSION   NP_004417 XP_208080
VERSION     NP_004417.2
DBSOURCE    REFSEQ: accession NM_004426.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1004)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1004)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1004)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1004)
  AUTHORS   Chen,L., Tong,Q., Chen,X., Jiang,P., Yu,H., Zhao,Q., Sun,L.,
            Liu,C., Gu,B., Zheng,Y., Fei,L., Jiang,X., Li,W., Volpe,G.,
            Abdul,M.M., Guo,G., Zhang,J., Qian,P., Sun,Q., Neculai,D.,
            Esteban,M.A., Li,C., Wen,F. and Ji,J.
  TITLE     PHC1 maintains pluripotency by organizing genome-wide chromatin
            interactions of the Nanog locus
  JOURNAL   Nat Commun 12 (1), 2829 (2021)
   PUBMED   33990559
  REMARK    GeneRIF: PHC1 maintains pluripotency by organizing genome-wide
            chromatin interactions of the Nanog locus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1004)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1004)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 1004)
  AUTHORS   Ohta,H., Tokimasa,S., Zou,Z., Funaki,S., Kurahashi,H.,
            Takahashi,Y., Kimura,M., Matsuoka,R., Horie,M., Hara,J., Shimada,K.
            and Takihara,Y.
  TITLE     Structure and chromosomal localization of the RAE28/HPH1 gene, a
            human homologue of the polyhomeotic gene
  JOURNAL   DNA Seq 11 (1-2), 61-73 (2000)
   PUBMED   10902910
REFERENCE   8  (residues 1 to 1004)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   9  (residues 1 to 1004)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   10 (residues 1 to 1004)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006581.16, CN388285.1,
            CN388283.1, BC073964.1, CN388316.1, U89277.1, BX640639.1 and
            BM473731.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 28, 2005 this sequence version replaced NP_004417.1.
            
            Summary: This gene is a homolog of the Drosophila polyhomeotic
            gene, which is a member of the Polycomb group of genes. The gene
            product is a component of a multimeric protein complex that
            contains EDR2 and the vertebrate Polycomb protein BMH1. The gene
            product, the EDR2 protein, and the Drosophila polyhomeotic protein
            share 2 highly conserved domains, named homology domains I and II.
            These domains are involved in protein-protein interactions and may
            mediate heterodimerization of the protein encoded by this gene and
            the EDR2 protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.94174.1,
                                           SRR1803614.280198.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000544916.6/ ENSP00000437659.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1004
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..1004
                     /product="polyhomeotic-like protein 1 isoform a"
                     /note="early development regulator 1 (homolog of
                     polyhomeotic 1); early development regulatory protein 1;
                     polyhomeotic-like 1"
                     /calculated_mol_wt=105403
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          212..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          261..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          432..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          <474..670
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          556..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Region          636..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          828..935
                     /region_name="PHC2_SAM_assoc"
                     /note="Unstructured region on Polyhomeotic-like protein 1
                     and 2; pfam16616"
                     /db_xref="CDD:465202"
     Region          848..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78364.3)"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Site            922
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P78364.3)"
     Region          935..1003
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(953..954,988..989,992..993,996)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(964..968,970..971,974..975,979,984)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..1004
                     /gene="PHC1"
                     /gene_synonym="EDR1; HPH1; MCPH11; RAE28"
                     /coded_by="NM_004426.3:368..3382"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8597.1"
                     /db_xref="GeneID:1911"
                     /db_xref="HGNC:HGNC:3182"
                     /db_xref="MIM:602978"
ORIGIN      
        1 meteseqnsn stngssssgg ssrpqiaqms lyerqavqal qalqrqpnaa qyfhqfmlqq
       61 qlsnaqlhsl aavqqatiaa srqasspnts ttqqqttttq asinlattsa aqlisrsqsv
      121 sspsattltq svllgnttsp plnqsqaqmy lrpqlgnllq vnrtlgrnvp lasqlilmpn
      181 gavaavqqev psaqspgvha dadqvqnlav rnqqasaqgp qmqgstqkai ppgaspvssl
      241 sqassqalav aqassgatnq slnlsqaggg sgnsipgsmg pggggqahgg lgqlpssgmg
      301 ggscprkgtg vvqplpaaqt vtvsqgsqte aesaaakkae adgsgqqnvg mnltrtatpa
      361 psqtlissat ytqiqphsli qqqqqihlqq kqvviqqqia ihhqqqfqhr qsqllhtath
      421 lqlaqqqqqq qqqqqqqqqp qattltapqp pqvpptqqvp psqsqqqaqt lvvqpmlqss
      481 plslppdaap kppipiqskp pvapikppql gaakmsaaqq ppphipvqvv gtrqpgtaqa
      541 qalglaqlaa avptsrgmpg tvqsgqahla ssppssqapg alqecpptla pgmtlapvqg
      601 tahvvkggat tsspvvaqvp aafymqsvhl pgkpqtlavk rkadseeerd dvstlgsmlp
      661 akaspvaesp kvmdeksslg ekaesvanvn antpsselva ltpapsvppp tlamvsrqmg
      721 dskppqaivk pqilthiieg fviqegaepf pvgcsqllke sekplqtglp tgltenqsgg
      781 plgvdspsae ldkkanllkc eycgkyapae qfrgskrfcs mtcakrynvs cshqfrlkrk
      841 kmkefqeany arvrrrgprr sssdiaraki qgkchrgqed ssrgsdnssy dealsptspg
      901 plsvraghge rdlgnpntap ptpelhginp vflssnpsrw sveevyefia slqgcqeiae
      961 efrsqeidgq allllkeehl msamniklgp alkicakinv lket
//
LOCUS       NP_006529                138 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 6 [Homo sapiens].
ACCESSION   NP_006529
VERSION     NP_006529.1
DBSOURCE    REFSEQ: accession NM_006538.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 138)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            AF032458.1, BC033694.1 and AI268146.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (6, also known as BimL) lacks an
            in-frame segment in the 5' coding coding region, compared to
            variant 1. The resulting isoform (6) is shorter, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290377.1, SRR1163658.144006.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..138
                     /product="bcl-2-like protein 11 isoform 6"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=15836
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     Region          76..106
                     /region_name="Bclx_interact"
                     /note="Bcl-x interacting, BH3 domain; pfam08945"
                     /db_xref="CDD:462643"
     CDS             1..138
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_006538.5:289..705"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS42731.1"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qdrspapmsc dkstqtpspp
       61 cqafnhylsa masmrqaepa dmrpeiwiaq elrrigdefn ayyarrvfln nyqaaedhpr
      121 mvilrllryi vrlvwrmh
//
LOCUS       NP_001287789            1032 aa            linear   PRI 20-NOV-2025
DEFINITION  probable ATP-dependent RNA helicase DDX46 isoform 1 [Homo sapiens].
ACCESSION   NP_001287789 XP_005272199
VERSION     NP_001287789.1
DBSOURCE    REFSEQ: accession NM_001300860.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1032)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1032)
  AUTHORS   Yang,G., Wang,Y., Wang,K., Liu,X. and Yang,J.
  TITLE     Oncogenic DDX46 promotes pancreatic cancer development and
            gemcitabine resistance by facilitating the JMJD6/CDK4 signaling
            pathway
  JOURNAL   Neoplasma 71 (3), 231-242 (2024)
   PUBMED   38764294
  REMARK    GeneRIF: Oncogenic DDX46 promotes pancreatic cancer development and
            gemcitabine resistance by facilitating the JMJD6/CDK4 signaling
            pathway.
REFERENCE   3  (residues 1 to 1032)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    GeneRIF: Mechanisms of the RNA helicases DDX42 and DDX46 in human
            U2 snRNP assembly.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1032)
  AUTHORS   Ma,Z., Song,J., Hua,Y., Wang,Y., Cao,W., Wang,H. and Hou,L.
  TITLE     The role of DDX46 in breast cancer proliferation and invasiveness:
            A potential therapeutic target
  JOURNAL   Cell Biol Int 47 (1), 283-291 (2023)
   PUBMED   36200534
  REMARK    GeneRIF: The role of DDX46 in breast cancer proliferation and
            invasiveness: A potential therapeutic target.
REFERENCE   5  (residues 1 to 1032)
  AUTHORS   Tholen,J., Razew,M., Weis,F. and Galej,W.P.
  TITLE     Structural basis of branch site recognition by the human
            spliceosome
  JOURNAL   Science 375 (6576), 50-57 (2022)
   PUBMED   34822310
REFERENCE   6  (residues 1 to 1032)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   7  (residues 1 to 1032)
  AUTHORS   Sigal,A., Milo,R., Cohen,A., Geva-Zatorsky,N., Klein,Y., Alaluf,I.,
            Swerdlin,N., Perzov,N., Danon,T., Liron,Y., Raveh,T.,
            Carpenter,A.E., Lahav,G. and Alon,U.
  TITLE     Dynamic proteomics in individual human cells uncovers widespread
            cell-cycle dependence of nuclear proteins
  JOURNAL   Nat Methods 3 (7), 525-531 (2006)
   PUBMED   16791210
REFERENCE   8  (residues 1 to 1032)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1032)
  AUTHORS   Xu,Y.Z., Newnham,C.M., Kameoka,S., Huang,T., Konarska,M.M. and
            Query,C.C.
  TITLE     Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP
            association with intron RNA
  JOURNAL   EMBO J 23 (2), 376-385 (2004)
   PUBMED   14713954
  REMARK    GeneRIF: Prp5 forms a bridge between U1 and U2 Small Nuclear
            Ribonucleoproteins at the time of pre-spliceosome formation
REFERENCE   10 (residues 1 to 1032)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
  REMARK    GeneRIF: characterization of protein associated with the human 17S
            U2 snRNP and one of its stable subunits, SF3b; results indicate
            that Prp5 plays an important role in pre-mRNA splicing, acting
            during or prior to prespliceosome assembly
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF244218.1, BK000565.1,
            AC010301.7 and BU608108.1.
            
            On Jul 15, 2014 this sequence version replaced XP_005272199.1.
            
            Summary: This gene encodes a member of the DEAD box protein family.
            DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure, such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The protein encoded by this gene is a
            component of the 17S U2 snRNP complex; it plays an important role
            in pre-mRNA splicing. Multiple alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.182204.1,
                                           SRR1803614.104240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000452510.7/ ENSP00000416534.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..1032
                     /product="probable ATP-dependent RNA helicase DDX46
                     isoform 1"
                     /EC_number="3.6.4.13"
                     /note="RNA helicase; Prp5-like DEAD-box protein; probable
                     ATP-dependent RNA helicase DDX46; PRP5 homolog; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 46; DEAD box protein 46"
                     /calculated_mol_wt=117331
     Region          1..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62780; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            263
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Region          361..582
                     /region_name="DEADc_DDX46"
                     /note="DEAD-box helicase domain of DEAD box protein 46;
                     cd17953"
                     /db_xref="CDD:350711"
     Region          372..400
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            order(374,392,394..396,399,417..423,529..530)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350711"
     Region          378..793
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          529..532
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Site            904
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q569Z5; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     Region          929..1031
                     /region_name="KH-I_DDX46"
                     /note="type I K homology (KH) RNA-binding domain found in
                     DEAD box protein 46 (DDX46) and similar proteins; cd22473"
                     /db_xref="CDD:411901"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L014.2)"
     CDS             1..1032
                     /gene="DDX46"
                     /gene_synonym="Prp5; PRPF5"
                     /coded_by="NM_001300860.2:161..3259"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75306.1"
                     /db_xref="GeneID:9879"
                     /db_xref="HGNC:HGNC:18681"
                     /db_xref="MIM:617848"
ORIGIN      
        1 mgresrhyrk rsasrgrsgs rsrsrspsdk rskrgddrrs rsrdrdrrre rsrsrdkrrs
       61 rsrdrkrlrr srsrerdrsr errrsrsrdr rrsrsrsrgr rsrssspgnk skktenrsrs
      121 kektdggess kekkkdkddk edekekdagn fdqnkleeem rkrkervekw reeqrkkame
      181 nigelkkeie emkqgkkwsl edddddeddp aeaekegnem egeeldplda ymeevkeevk
      241 kfnmrsvkgg ggnekksgpt vtkvvtvvtt kkavvdsdkk kgelmendqd ameysseeee
      301 vdlqtaltgy qtkqrkllep vdhgkieyep frknfyvevp elakmsqeev nvfrlemegi
      361 tvkgkgcpkp ikswvqcgis mkilnslkkh gyekptpiqt qaipaimsgr dligiaktgs
      421 gktiafllpm frhimdqrsl eegegpiavi mtptrelalq itkeckkfsk tlglrvvcvy
      481 ggtgiseqia elkrgaeiiv ctpgrmidml aansgrvtnl rrvtyvvlde adrmfdmgfe
      541 pqvmrivdnv rpdrqtvmfs atfprameal arrilskpie vqvggrsvvc sdveqqvivi
      601 eeekkflkll ellghyqesg sviifvdkqe hadgllkdlm rasypcmslh ggidqydrds
      661 iindfkngtc kllvatsvaa rgldvkhlil vvnyscpnhy edyvhragrt gragnkgyay
      721 tfitedqary agdiikalel sgtavppdle klwsdfkdqq kaegkiikks sgfsgkgfkf
      781 deteqalane rkklqkaalg lqdsddedaa vdideqiesm fnskkrvkdm aapgtssvpa
      841 ptagnaekle iakrlalrin aqknlgiesq vdvmqqatna ilrggtilap tvsaktiaeq
      901 laekinakln yvplekqeee rqdggqnesf kryeeelein dfpqtarwkv tskealqris
      961 eyseaaitir gtyfppgkep kegerkiyla iesanelavq kakaeitrli keelirlqns
     1021 yqptnkgryk vl
//
LOCUS       NP_005707                333 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing protein GIPC1 isoform 1 [Homo sapiens].
ACCESSION   NP_005707
VERSION     NP_005707.1
DBSOURCE    REFSEQ: accession NM_005716.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gu,X., Jiao,K., Yue,D., Wang,X., Qiao,K., Gao,M., Lin,J., Sun,C.,
            Zhao,C., Zhu,W. and Xi,J.
  TITLE     Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report
  JOURNAL   Neuromuscul Disord 33 (9), 93-97 (2023)
   PUBMED   37550168
  REMARK    GeneRIF: Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Fan,Y., Shen,S., Yang,J., Yao,D., Li,M., Mao,C., Wang,Y., Hao,X.,
            Ma,D., Li,J., Shi,J., Guo,M., Li,S., Yuan,Y., Liu,F., Yang,Z.,
            Zhang,S., Hu,Z., Fan,L., Liu,H., Zhang,C., Wang,Y., Wang,Q.,
            Zheng,H., He,Y., Song,B., Xu,Y. and Shi,C.
  TITLE     GIPC1 CGG Repeat Expansion Is Associated with Movement Disorders
  JOURNAL   Ann Neurol 91 (5), 704-715 (2022)
   PUBMED   35152460
  REMARK    GeneRIF: GIPC1 CGG Repeat Expansion Is Associated with Movement
            Disorders.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Wang,L.H., Kalb,R.G. and Strittmatter,S.M.
  TITLE     A PDZ protein regulates the distribution of the transmembrane
            semaphorin, M-SemF
  JOURNAL   J Biol Chem 274 (20), 14137-14146 (1999)
   PUBMED   10318831
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Bunn,R.C., Jensen,M.A. and Reed,B.C.
  TITLE     Protein interactions with the glucose transporter binding protein
            GLUT1CBP that provide a link between GLUT1 and the cytoskeleton
  JOURNAL   Mol Biol Cell 10 (4), 819-832 (1999)
   PUBMED   10198040
REFERENCE   8  (residues 1 to 333)
  AUTHORS   De Vries,L., Lou,X., Zhao,G., Zheng,B. and Farquhar,M.G.
  TITLE     GIPC, a PDZ domain containing protein, interacts specifically with
            the C terminus of RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 95 (21), 12340-12345 (1998)
   PUBMED   9770488
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Rousset,R., Fabre,S., Desbois,C., Bantignies,F. and Jalinot,P.
  TITLE     The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
            with the PDZ domain of cellular proteins
  JOURNAL   Oncogene 16 (5), 643-654 (1998)
   PUBMED   9482110
REFERENCE   10 (residues 1 to 333)
  AUTHORS   De Vries,L., Elenko,E., Hubler,L., Jones,T.L. and Farquhar,M.G.
  TITLE     GAIP is membrane-anchored by palmitoylation and interacts with the
            activated (GTP-bound) form of G alpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15203-15208 (1996)
   PUBMED   8986788
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012318.7 and BC000410.2.
            
            Summary: GIPC1 is a scaffolding protein that regulates cell surface
            receptor expression and trafficking (Lee et al., 2008 [PubMed
            18775991]).[supplied by OMIM, Apr 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1, 3 and 5
            encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.220035.1,
                                           SRR3476690.263788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393033.9/ ENSP00000376753.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..333
                     /product="PDZ domain-containing protein GIPC1 isoform 1"
                     /note="GLUT1 C-terminal binding protein; IGF-1 receptor
                     interacting protein 1; regulator of G-protein signalling
                     19 interacting protein 1; PDZ domain-containing protein
                     GIPC1; tax interaction protein 2; RGS19-interacting
                     protein 1; RGS-GAIP-interacting protein; GAIP
                     C-terminus-interacting protein"
                     /calculated_mol_wt=35918
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          126..219
                     /region_name="PDZ_GIPC1"
                     /note="PDZ domain of PDZ domain-containing protein GIPC1;
                     cd23077"
                     /db_xref="CDD:467290"
     Site            order(142..148,158,161,191,195,198..199)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467290"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          223..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          261..325
                     /region_name="GH2_GIPC"
                     /note="GIPC-homology 2 (GH2) domain found in the GIPC
                     family; cd21180"
                     /db_xref="CDD:409666"
     Site            order(273,276..281,311)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409666"
     Site            order(274..278,280,282..283,310..312,314,316)
                     /site_type="other"
                     /note="myosin VI binding site [polypeptide binding]"
                     /db_xref="CDD:409666"
     CDS             1..333
                     /gene="GIPC1"
                     /gene_synonym="C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1;
                     NIP; OPDM2; RGS19IP1; SEMCAP; SYNECTIIN; SYNECTIN; TIP-2"
                     /coded_by="NM_005716.4:266..1267"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12310.1"
                     /db_xref="GeneID:10755"
                     /db_xref="HGNC:HGNC:1226"
                     /db_xref="MIM:605072"
ORIGIN      
        1 mplglgrrkk applveneea epgrgglgvg epgplggggs ggpqmglppp ppalrprlvf
       61 htqlahgspt griegftnvk elygkiaeaf rlptaevmfc tlnthkvdmd kllggqigle
      121 dfifahvkgq rkevevfkse dalgltitdn gagyafikri kegsvidhih lisvgdmiea
      181 ingqsllgcr hyevarllke lprgrtftlk lteprkafdm isqrsaggrp gsgpqlgtgr
      241 gtlrlrsrgp atvedlpsaf eekaiekvdd llesymgird telaatmvel gkdkrnpdel
      301 aealderlgd fafpdefvfd vwgaigdakv gry
//
LOCUS       NP_001355174             175 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-crystallin B chain isoform 1 [Homo sapiens].
ACCESSION   NP_001355174
VERSION     NP_001355174.1
DBSOURCE    REFSEQ: accession NM_001368245.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Wang,X., Chen,K., Yao,Y., Lin,Y., Yang,J., Zhu,Y. and Zhou,B.
  TITLE     TGFbeta1-Induced Fibrotic Responses of Conjunctival Fibroblasts
            through the Wnt/beta-Catenin/CRYAB Signaling Pathway
  JOURNAL   Am J Pathol 194 (9), 1764-1779 (2024)
   PUBMED   38879081
  REMARK    GeneRIF: TGFbeta1-Induced Fibrotic Responses of Conjunctival
            Fibroblasts through the Wnt/beta-Catenin/CRYAB Signaling Pathway.
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Rodina,N., Hornung,S., Sarkar,R., Suladze,S., Peters,C.,
            Schmid,P.W.N., Niu,Z., Haslbeck,M., Buchner,J., Kapurniotu,A. and
            Reif,B.
  TITLE     Modulation of Alzheimer's Disease Abeta40 Fibril Polymorphism by
            the Small Heat Shock Protein alphaB-Crystallin
  JOURNAL   J Am Chem Soc 146 (28), 19077-19087 (2024)
   PUBMED   38973199
  REMARK    GeneRIF: Modulation of Alzheimer's Disease Abeta40 Fibril
            Polymorphism by the Small Heat Shock Protein alphaB-Crystallin.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Tian,B., Li,X., Li,W., Shi,Z., He,X., Wang,S., Zhu,X., Shi,N.,
            Li,Y., Wan,P. and Zhu,C.
  TITLE     CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1
  JOURNAL   Aging (Albany NY) 16 (10), 8965-8979 (2024)
   PUBMED   38787373
  REMARK    GeneRIF: CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Derham,B.K. and Harding,J.J.
  TITLE     Alpha-crystallin as a molecular chaperone
  JOURNAL   Prog Retin Eye Res 18 (4), 463-509 (1999)
   PUBMED   10217480
  REMARK    GeneRIF: Alpha crystallin is a moonlighting protein that functions
            as a heat shock protein as well as a lens crystallin.
            Review article
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Selcen,D. and Engel,A.G.
  TITLE     Myofibrillar Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301672
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Ortwerth,B.J., Slight,S.H., Prabhakaram,M., Sun,Y. and Smith,J.B.
  TITLE     Site-specific glycation of lens crystallins by ascorbic acid
  JOURNAL   Biochim Biophys Acta 1117 (2), 207-215 (1992)
   PUBMED   1525182
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Iwaki,A., Iwaki,T., Goldman,J.E., Ogomori,K., Tateishi,J. and
            Sakaki,Y.
  TITLE     Accumulation of alpha B-crystallin in brains of patients with
            Alexander's disease is not due to an abnormality of the 5'-flanking
            and coding sequence of the genomic DNA
  JOURNAL   Neurosci Lett 140 (1), 89-92 (1992)
   PUBMED   1407707
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Kato,K., Shinohara,H., Goto,S., Inaguma,Y., Morishita,R. and
            Asano,T.
  TITLE     Copurification of small heat shock protein with alpha B crystallin
            from human skeletal muscle
  JOURNAL   J Biol Chem 267 (11), 7718-7725 (1992)
   PUBMED   1560006
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Kramps,J.A., de Man,B.M. and de Jong,W.W.
  TITLE     The primary structure of the B2 chain of human alpha-crystallin
  JOURNAL   FEBS Lett 74 (1), 82-84 (1977)
   PUBMED   838078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000907.6.
            
            Summary: Mammalian lens crystallins are divided into alpha, beta,
            and gamma families. Alpha crystallins are composed of two gene
            products: alpha-A and alpha-B, for acidic and basic, respectively.
            Alpha crystallins can be induced by heat shock and are members of
            the small heat shock protein (HSP20) family. They act as molecular
            chaperones although they do not renature proteins and release them
            in the fashion of a true chaperone; instead they hold them in large
            soluble aggregates. These heterogeneous aggregates consist of 30-40
            subunits; the alpha-A and alpha-B subunits have a 3:1 ratio,
            respectively. Two additional functions of alpha crystallins are an
            autokinase activity and participation in the intracellular
            architecture. The encoded protein has been identified as a
            moonlighting protein based on its ability to perform
            mechanistically distinct functions. Alpha-A and alpha-B gene
            products are differentially expressed; alpha-A is preferentially
            restricted to the lens and alpha-B is expressed widely in many
            tissues and organs. Elevated expression of alpha-B crystallin
            occurs in many neurological diseases; a missense mutation
            cosegregated in a family with a desmin-related myopathy.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.44348.1, BU556902.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 10217480
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..175
                     /product="alpha-crystallin B chain isoform 1"
                     /note="heat-shock 20 kD like-protein; alpha-crystallin B
                     chain; heat shock protein beta-5; rosenthal fiber
                     component; renal carcinoma antigen NY-REN-27; epididymis
                     secretory protein Li 101; heat shock protein family B
                     member 5"
                     /calculated_mol_wt=20028
     Region          1..55
                     /region_name="Crystallin"
                     /note="Alpha crystallin A chain, N terminal; pfam00525"
                     /db_xref="CDD:425732"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:8142454,
                     ECO:0000269|PubMed:838078; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8175657; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            41
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:28939839; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11158243,
                     ECO:0000269|PubMed:8175657; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            48
                     /site_type="other"
                     /note="Susceptible to oxidation; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11158243,
                     ECO:0000269|PubMed:8175657, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02511.2)"
     Site            60
                     /site_type="other"
                     /note="Susceptible to oxidation; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Region          67..150
                     /region_name="ACD_alphaB-crystallin_HspB5"
                     /note="Alpha-crystallin domain found in the small heat
                     shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa).
                     sHsps are molecular chaperones that suppress protein
                     aggregation and protect against cell stress, and are
                     generally active as large oligomers...; cd06498"
                     /db_xref="CDD:107246"
     Site            order(68..72,78,80,82..83,120,141..142)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107246"
     Site            68
                     /site_type="other"
                     /note="Susceptible to oxidation; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, partial.
                     /evidence=ECO:0000269|PubMed:11369851,
                     ECO:0000269|PubMed:22120592; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Region          146..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02511.2)"
     Site            166
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:22120592; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     Site            170
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000250|UniProtKB:P23928; propagated from
                     UniProtKB/Swiss-Prot (P02511.2)"
     CDS             1..175
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2; MFM2A; MFM2B"
                     /coded_by="NM_001368245.1:237..764"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS8351.1"
                     /db_xref="GeneID:1410"
                     /db_xref="HGNC:HGNC:2389"
                     /db_xref="MIM:123590"
ORIGIN      
        1 mdiaihhpwi rrpffpfhsp srlfdqffge hllesdlfpt stslspfylr ppsflrapsw
       61 fdtglsemrl ekdrfsvnld vkhfspeelk vkvlgdviev hgkheerqde hgfisrefhr
      121 kyripadvdp ltitsslssd gvltvngprk qvsgpertip itreekpavt aapkk
//
LOCUS       NP_694592                534 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase Fyn isoform b [Homo sapiens].
ACCESSION   NP_694592 XP_005266947
VERSION     NP_694592.1
DBSOURCE    REFSEQ: accession NM_153047.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Zhu,J., Shi,L. and Su,Y.
  TITLE     FYN as an emerging biological biomarker for prognosis and potential
            therapeutic target in LGG
  JOURNAL   Neurol Res 46 (9), 787-795 (2024)
   PUBMED   38752708
  REMARK    GeneRIF: FYN as an emerging biological biomarker for prognosis and
            potential therapeutic target in LGG.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Yang,K., Belrose,J., Trepanier,C.H., Lei,G., Jackson,M.F. and
            MacDonald,J.F.
  TITLE     Fyn, a potential target for Alzheimer's disease
  JOURNAL   J Alzheimers Dis 27 (2), 243-252 (2011)
   PUBMED   21799250
  REMARK    GeneRIF: [review] Recent evidence cited in this review suggests
            that alterations in Fyn, a Src family kinase, might contribute to
            Alzheimer's disease pathogenesis.
            Review article
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Saito,Y.D., Jensen,A.R., Salgia,R. and Posadas,E.M.
  TITLE     Fyn: a novel molecular target in cancer
  JOURNAL   Cancer 116 (7), 1629-1637 (2010)
   PUBMED   20151426
  REMARK    Review article
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Rigley,K., Slocombe,P., Proudfoot,K., Wahid,S., Mandair,K. and
            Bebbington,C.
  TITLE     Human p59fyn(T) regulates OKT3-induced calcium influx by a
            mechanism distinct from PIP2 hydrolysis in Jurkat T cells
  JOURNAL   J Immunol 154 (3), 1136-1145 (1995)
   PUBMED   7822789
  REMARK    Erratum:[J Immunol 1995 Apr 15;154(8):4223]
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Gout,I., Dhand,R., Panayotou,G., Fry,M.J., Hiles,I., Otsu,M. and
            Waterfield,M.D.
  TITLE     Expression and characterization of the p85 subunit of the
            phosphatidylinositol 3-kinase complex and a related p85 beta
            protein by using the baculovirus expression system
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 395-405 (1992)
   PUBMED   1334406
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Thomas,P.M. and Samelson,L.E.
  TITLE     The glycophosphatidylinositol-anchored Thy-1 molecule interacts
            with the p60fyn protein tyrosine kinase in T cells
  JOURNAL   J Biol Chem 267 (17), 12317-12322 (1992)
   PUBMED   1351058
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Brickell,P.M.
  TITLE     The p60c-src family of protein-tyrosine kinases: structure,
            regulation, and function
  JOURNAL   Crit Rev Oncog 3 (4), 401-446 (1992)
   PUBMED   1384720
  REMARK    Review article
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Kawakami,T., Pennington,C.Y. and Robbins,K.C.
  TITLE     Isolation and oncogenic potential of a novel human src-like gene
  JOURNAL   Mol Cell Biol 6 (12), 4195-4201 (1986)
   PUBMED   3099169
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Semba,K., Nishizawa,M., Miyajima,N., Yoshida,M.C., Sukegawa,J.,
            Yamanashi,Y., Sasaki,M., Yamamoto,T. and Toyoshima,K.
  TITLE     yes-related protooncogene, syn, belongs to the protein-tyrosine
            kinase family
  JOURNAL   Proc Natl Acad Sci U S A 83 (15), 5459-5463 (1986)
   PUBMED   3526330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158035.14, AL109916.17 and
            Z97989.1.
            
            On May 9, 2019 this sequence version replaced XP_005266947.1.
            
            Summary: This gene is a member of the protein-tyrosine kinase
            oncogene family. It encodes a membrane-associated tyrosine kinase
            that has been implicated in the control of cell growth. The protein
            associates with the p85 subunit of phosphatidylinositol 3-kinase
            and interacts with the fyn-binding protein. Alternatively spliced
            transcript variants encoding distinct isoforms exist. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, and
            lacks an alternate in-frame exon but includes a different in-frame
            exon in the central coding region, compared to variant 1. The
            encoded isoform (b) is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4481267.1,
                                           SRR18074968.628059.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..534
                     /product="tyrosine-protein kinase Fyn isoform b"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase Fyn; src-like kinase; c-syn
                     protooncogene; tyrosine kinase p59fyn(T); OKT3-induced
                     calcium influx regulator; src/yes-related novel;
                     proto-oncogene Syn; proto-oncogene c-Fyn; FYN oncogene
                     related to SRC, FGR, YES"
                     /calculated_mol_wt=60010
     Region          85..140
                     /region_name="SH3_Fyn_Yrk"
                     /note="Src homology 3 domain of Fyn and Yrk Protein
                     Tyrosine Kinases; cd12006"
                     /db_xref="CDD:212939"
     Site            order(91,93,96..97,100,116..119,132,134,136..137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Site            order(93,96..100,116,119,132)
                     /site_type="other"
                     /note="SAP interaction site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Region          145..245
                     /region_name="SH2_Src_Fyn"
                     /note="Src homology 2 (SH2) domain found in Fyn; cd10368"
                     /db_xref="CDD:198231"
     Site            order(156,176,178..181,186,202,204,237)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198231"
     Site            order(156,176,202,204)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198231"
     Site            order(203,231)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198231"
     Region          258..531
                     /region_name="PTKc_Fyn"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fyn; cd05070"
                     /db_xref="CDD:270655"
     Site            order(274,276..278,282,294,296,339..342,346,387,391..392,
                     394,405,422..426,435,469)
                     /site_type="active"
                     /db_xref="CDD:270655"
     Site            order(274,277,282,294,296,339..342,346,387,389,392,394,
                     405)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270655"
     Site            order(288,290,322,325,327,340,366,370,398,518)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(376,379..380,443,505..507,509,511..512,515,519,
                     522..523,527)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(387,391,422..426,435,469)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270655"
     Site            404..428
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270655"
     CDS             1..534
                     /gene="FYN"
                     /gene_synonym="p59-FYN; SLK; SYN"
                     /coded_by="NM_153047.4:227..1831"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5095.1"
                     /db_xref="GeneID:2534"
                     /db_xref="HGNC:HGNC:4037"
                     /db_xref="MIM:137025"
ORIGIN      
        1 mgcvqckdke atklteerdg slnqssgyry gtdptpqhyp sfgvtsipny nnfhaaggqg
       61 ltvfggvnss shtgtlrtrg gtgvtlfval ydyeartedd lsfhkgekfq ilnssegdww
      121 earslttget gyipsnyvap vdsiqaeewy fgklgrkdae rqllsfgnpr gtflireset
      181 tkgayslsir dwddmkgdhv khykirkldn ggyyittraq fetlqqlvqh ysekadglcf
      241 nltviassct pqtsglakda wevarrslcl ekklgqgcfa evwlgtwngn tkvaiktlkp
      301 gtmspesfle eaqimkklkh dklvqlyavv seepiyivte ymnkgslldf lkdgegralk
      361 lpnlvdmaaq vaagmayier mnyihrdlrs anilvgngli ckiadfglar liedneytar
      421 qgakfpikwt apeaalygrf tiksdvwsfg illtelvtkg rvpypgmnnr evleqvergy
      481 rmpcpqdcpi slhelmihcw kkdpeerptf eylqsfledy ftatepqyqp genl
//
LOCUS       NP_066565                496 aa            linear   PRI 20-NOV-2025
DEFINITION  glycylpeptide N-tetradecanoyltransferase 1 [Homo sapiens].
ACCESSION   NP_066565
VERSION     NP_066565.1
DBSOURCE    REFSEQ: accession NM_021079.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Qiu,P., Li,X., Gong,M., Wen,P., Wen,J., Xu,L. and Wang,G.
  TITLE     SPI1 Mediates N-Myristoyltransferase 1 to Advance Gastric Cancer
            Progression via PI3K/AKT/mTOR Pathway
  JOURNAL   Can J Gastroenterol Hepatol 2023, 2021515 (2023)
   PUBMED   36967718
  REMARK    GeneRIF: SPI1 Mediates N-Myristoyltransferase 1 to Advance Gastric
            Cancer Progression via PI3K/AKT/mTOR Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Zhang,T., Goel,A., Xu,X., Wu,Y., Tang,E., Zhang,F., Li,Y., Li,H.,
            Cai,Y. and Weng,W.
  TITLE     N-mytistoyltransferase 1 and 2 are potential tumor suppressors and
            novel targets of miR-182 in human non-small cell lung carcinomas
  JOURNAL   Lung Cancer 171, 70-81 (2022)
   PUBMED   35930829
  REMARK    GeneRIF: N-mytistoyltransferase 1 and 2 are potential tumor
            suppressors and novel targets of miR-182 in human non-small cell
            lung carcinomas.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Tang,M., Xia,Y., Xiao,T., Cao,R., Cao,Y. and Ouyang,B.
  TITLE     Structural Exploration on Palmitoyltransferase DHHC3 from Homo
            sapiens
  JOURNAL   Polymers (Basel) 14 (15), 3013 (2022)
   PUBMED   35893977
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Sun,Y., Guan,Z., Sheng,Q., Duan,W., Zhao,H., Zhou,J., Deng,Q. and
            Pei,X.
  TITLE     N-myristoyltransferase-1 deficiency blocks myristoylation of
            LAMTOR1 and inhibits bladder cancer progression
  JOURNAL   Cancer Lett 529, 126-138 (2022)
   PUBMED   34999170
  REMARK    GeneRIF: N-myristoyltransferase-1 deficiency blocks myristoylation
            of LAMTOR1 and inhibits bladder cancer progression.
REFERENCE   6  (residues 1 to 496)
  AUTHORS   Duronio,R.J., Reed,S.I. and Gordon,J.I.
  TITLE     Mutations of human myristoyl-CoA:protein N-myristoyltransferase
            cause temperature-sensitive myristic acid auxotrophy in
            Saccharomyces cerevisiae
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 4129-4133 (1992)
   PUBMED   1570339
REFERENCE   7  (residues 1 to 496)
  AUTHORS   Wice,B.M. and Gordon,J.I.
  TITLE     A strategy for isolation of cDNAs encoding proteins affecting human
            intestinal epithelial cell growth and differentiation:
            characterization of a novel gut-specific N-myristoylated annexin
  JOURNAL   J Cell Biol 116 (2), 405-422 (1992)
   PUBMED   1530946
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Pal,R., Reitz,M.S. Jr., Tschachler,E., Gallo,R.C.,
            Sarngadharan,M.G. and Veronese,F.D.
  TITLE     Myristoylation of gag proteins of HIV-1 plays an important role in
            virus assembly
  JOURNAL   AIDS Res Hum Retroviruses 6 (6), 721-730 (1990)
   PUBMED   2194551
REFERENCE   9  (residues 1 to 496)
  AUTHORS   Bryant,M. and Ratner,L.
  TITLE     Myristoylation-dependent replication and assembly of human
            immunodeficiency virus 1
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 523-527 (1990)
   PUBMED   2405382
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Mumby,S.M., Heukeroth,R.O., Gordon,J.I. and Gilman,A.G.
  TITLE     G-protein alpha-subunit expression, myristoylation, and membrane
            association in COS cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 728-732 (1990)
   PUBMED   2153964
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC006569.2, AC116493.10, AC002117.2 and BC006538.2.
            
            Summary: Myristate, a rare 14-carbon saturated fatty acid, is
            cotranslationally attached by an amide linkage to the N-terminal
            glycine residue of cellular and viral proteins with diverse
            functions. N-myristoyltransferase (NMT; EC 2.3.1.97) catalyzes the
            transfer of myristate from CoA to proteins. N-myristoylation
            appears to be irreversible and is required for full expression of
            the biologic activities of several N-myristoylated proteins,
            including the alpha subunit of the signal-transducing guanine
            nucleotide-binding protein (G protein) GO (GNAO1; MIM 139311)
            (Duronio et al., 1992 [PubMed 1570339]).[supplied by OMIM, Nov
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006538.2, SRR1660805.232373.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258960.7/ ENSP00000258960.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..496
                     /product="glycylpeptide N-tetradecanoyltransferase 1"
                     /EC_number="2.3.1.97"
                     /note="alternative, short form NMT-S; long form, NMT-L;
                     type I N-myristoyltransferase; myristoyl-CoA:protein
                     N-myristoyltransferase 1; protein-lysine
                     myristoyltransferase NMT1"
                     /calculated_mol_wt=56675
     Region          1..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30419.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70310; propagated from
                     UniProtKB/Swiss-Prot (P30419.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P30419.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30419.2)"
     Region          86..484
                     /region_name="NMT1"
                     /note="N-myristoyl transferase [Lipid metabolism];
                     COG5092"
                     /db_xref="CDD:227423"
     CDS             1..496
                     /gene="NMT1"
                     /gene_synonym="HsNMT1; NMT"
                     /coded_by="NM_021079.5:14..1504"
                     /db_xref="CCDS:CCDS11494.1"
                     /db_xref="GeneID:4836"
                     /db_xref="HGNC:HGNC:7857"
                     /db_xref="MIM:160993"
ORIGIN      
        1 madesetavk ppapplpqmm egngnghehc sdceneedns ynrgglspan dtgakkkkkk
       61 qkkkkekgse tdsaqdqpvk mnslpaeriq eiqkaielfs vgqgpaktme easkrsyqfw
      121 dtqpvpklge vvnthgpvep dkdnirqepy tlpqgftwda ldlgdrgvlk elytllneny
      181 vedddnmfrf dyspefllwa lrppgwlpqw hcgvrvvssr klvgfisaip anihiydtek
      241 kmveinflcv hkklrskrva pvlireitrr vhlegifqav ytagvvlpkp vgtcrywhrs
      301 lnprklievk fshlsrnmtm qrtmklyrlp etpktaglrp metkdipvvh qlltrylkqf
      361 hltpvmsqee vehwfypqen iidtfvvena ngevtdflsf ytlpstimnh pthkslkaay
      421 sfynvhtqtp lldlmsdalv lakmkgfdvf naldlmenkt fleklkfgig dgnlqyylyn
      481 wkcpsmgaek vglvlq
//
LOCUS       NP_004903                736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004903
VERSION     NP_004903.2
DBSOURCE    REFSEQ: accession NM_004912.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Jun 11, 2003 this sequence version replaced NP_004903.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (2) lacks the 5' exon but has an
            alternate segment in the 5' UTR, as compared to variant 1. Variants
            1-4 encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF296765.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_004912.4:1095..3305"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001026788              90 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome c oxidase assembly protein COX19 [Homo sapiens].
ACCESSION   NP_001026788
VERSION     NP_001026788.1
DBSOURCE    REFSEQ: accession NM_001031617.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Gao,S., Zhang,H., Zhang,X., Wang,J., Bai,W. and Jiang,B.
  TITLE     COX19 Is a New Target of MACC1 and Promotes Colorectal Cancer
            Progression by Regulating Copper Transport in Mitochondria
  JOURNAL   J Nutr 154 (2), 381-394 (2024)
   PUBMED   38141772
  REMARK    GeneRIF: COX19 Is a New Target of MACC1 and Promotes Colorectal
            Cancer Progression by Regulating Copper Transport in Mitochondria.
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Nyvltova,E., Dietz,J.V., Seravalli,J., Khalimonchuk,O. and
            Barrientos,A.
  TITLE     Coordination of metal center biogenesis in human cytochrome c
            oxidase
  JOURNAL   Nat Commun 13 (1), 3615 (2022)
   PUBMED   35750769
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Fischer,M., Horn,S., Belkacemi,A., Kojer,K., Petrungaro,C.,
            Habich,M., Ali,M., Kuttner,V., Bien,M., Kauff,F., Dengjel,J.,
            Herrmann,J.M. and Riemer,J.
  TITLE     Protein import and oxidative folding in the mitochondrial
            intermembrane space of intact mammalian cells
  JOURNAL   Mol Biol Cell 24 (14), 2160-2170 (2013)
   PUBMED   23676665
REFERENCE   6  (residues 1 to 90)
  AUTHORS   Leary,S.C., Cobine,P.A., Nishimura,T., Verdijk,R.M., de Krijger,R.,
            de Coo,R., Tarnopolsky,M.A., Winge,D.R. and Shoubridge,E.A.
  TITLE     COX19 mediates the transduction of a mitochondrial redox signal
            from SCO1 that regulates ATP7A-mediated cellular copper efflux
  JOURNAL   Mol Biol Cell 24 (6), 683-691 (2013)
   PUBMED   23345593
  REMARK    GeneRIF: COX19 is necessary for the transduction of a
            SCO1-dependent mitochondrial redox signal that regulates
            ATP7A-mediated cellular copper efflux.
REFERENCE   7  (residues 1 to 90)
  AUTHORS   Sacconi,S., Trevisson,E., Pistollato,F., Baldoin,M.C.,
            Rezzonico,R., Bourget,I., Desnuelle,C., Tenconi,R., Basso,G.,
            DiMauro,S. and Salviati,L.
  TITLE     hCOX18 and hCOX19: two human genes involved in cytochrome c oxidase
            assembly
  JOURNAL   Biochem Biophys Res Commun 337 (3), 832-839 (2005)
   PUBMED   16212937
  REMARK    GeneRIF: Both hCox18p and hCox19p present significant amino acid
            identity with the corresponding yeast polypeptides and reveal
            highly conserved functional domains.
REFERENCE   8  (residues 1 to 90)
  AUTHORS   Tay,S.K., Nesti,C., Mancuso,M., Schon,E.A., Shanske,S., Bonilla,E.,
            Davidson,M.M. and Dimauro,S.
  TITLE     Studies of COX16, COX19, and PET191 in human cytochrome-c oxidase
            deficiency
  JOURNAL   Arch Neurol 61 (12), 1935-1937 (2004)
   PUBMED   15596615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY957566.1, AC073957.7 and AA437231.1.
            
            Summary: COX19 encodes a cytochrome c oxidase (COX)-assembly
            protein. The S. cerevisiae Cox19 protein may play a role in metal
            transport to the mitochondrial intermembrane space and assembly of
            complex IV of the mitochondrial respiratory chain (Sacconi et al.,
            2005 [PubMed 16212937]).[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY957566.1, SRR1660803.247765.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344111.4/ ENSP00000342015.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..90
                     /product="cytochrome c oxidase assembly protein COX19"
                     /note="hCOX19; COX19 cytochrome c oxidase assembly
                     homolog; cytochrome c oxidase assembly homolog 19; COX19,
                     cytochrome c oxidase assembly factor"
                     /calculated_mol_wt=10263
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49B96.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q49B96.1)"
     Region          30..64
                     /region_name="CHCH"
                     /note="CHCH domain; pfam06747"
                     /db_xref="CDD:429096"
     Region          30..40
                     /region_name="Cx9C motif 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49B96.1)"
     Region          51..61
                     /region_name="Cx9C motif 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q49B96.1)"
     CDS             1..90
                     /gene="COX19"
                     /coded_by="NM_001031617.3:41..313"
                     /db_xref="CCDS:CCDS34582.1"
                     /db_xref="GeneID:90639"
                     /db_xref="HGNC:HGNC:28074"
                     /db_xref="MIM:610429"
ORIGIN      
        1 mstamnfgtk sfqprppdkg sfpldhlgec ksfkekfmkc lhnnnfenal crkeskeyle
       61 crmerklmlq epleklgfgd ltsgkseakk
//
LOCUS       NP_079461               1990 aa            linear   PRI 20-NOV-2025
DEFINITION  protein TANC2 isoform 1 [Homo sapiens].
ACCESSION   NP_079461 XP_005257260 XP_371074 XP_947427
VERSION     NP_079461.2
DBSOURCE    REFSEQ: accession NM_025185.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1990)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1990)
  AUTHORS   Broniarczyk,J.K., Massimi,P., Trejo-Cerro,O., Myers,M.P. and
            Banks,L.
  TITLE     HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in a
            PBM-Dependent Manner and Promotes Increased Cell Proliferation
  JOURNAL   J Virol 96 (22), e0136522 (2022)
   PUBMED   36326272
  REMARK    GeneRIF: HPV-18E6 Inhibits Interactions between TANC2 and SNX27 in
            a PBM-Dependent Manner and Promotes Increased Cell Proliferation.
REFERENCE   3  (residues 1 to 1990)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1990)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1990)
  AUTHORS   Kim,S.G., Lee,S., Kim,Y., Park,J., Woo,D., Kim,D., Li,Y., Shin,W.,
            Kang,H., Yook,C., Lee,M., Kim,K., Roh,J.D., Ryu,J., Jung,H.,
            Um,S.M., Yang,E., Kim,H., Han,J., Heo,W.D. and Kim,E.
  TITLE     Tanc2-mediated mTOR inhibition balances mTORC1/2 signaling in the
            developing mouse brain and human neurons
  JOURNAL   Nat Commun 12 (1), 2695 (2021)
   PUBMED   33976205
  REMARK    GeneRIF: Tanc2-mediated mTOR inhibition balances mTORC1/2 signaling
            in the developing mouse brain and human neurons.
            Erratum:[Nat Commun. 2022 Nov 1;13(1):6544. doi:
            10.1038/s41467-022-33972-9. PMID: 36319630]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1990)
  AUTHORS   Guo,H., Bettella,E., Marcogliese,P.C., Zhao,R., Andrews,J.C.,
            Nowakowski,T.J., Gillentine,M.A., Hoekzema,K., Wang,T., Wu,H.,
            Jangam,S., Liu,C., Ni,H., Willemsen,M.H., van Bon,B.W., Rinne,T.,
            Stevens,S.J.C., Kleefstra,T., Brunner,H.G., Yntema,H.G., Long,M.,
            Zhao,W., Hu,Z., Colson,C., Richard,N., Schwartz,C.E., Romano,C.,
            Castiglia,L., Bottitta,M., Dhar,S.U., Erwin,D.J., Emrick,L.,
            Keren,B., Afenjar,A., Zhu,B., Bai,B., Stankiewicz,P., Herman,K.,
            Mercimek-Andrews,S., Juusola,J., Wilfert,A.B., Abou Jamra,R.,
            Buttner,B., Mefford,H.C., Muir,A.M., Scheffer,I.E., Regan,B.M.,
            Malone,S., Gecz,J., Cobben,J., Weiss,M.M., Waisfisz,Q.,
            Bijlsma,E.K., Hoffer,M.J.V., Ruivenkamp,C.A.L., Sartori,S., Xia,F.,
            Rosenfeld,J.A., Bernier,R.A., Wangler,M.F., Yamamoto,S., Xia,K.,
            Stegmann,A.P.A., Bellen,H.J., Murgia,A. and Eichler,E.E.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Disruptive mutations in TANC2 define a neurodevelopmental syndrome
            associated with psychiatric disorders
  JOURNAL   Nat Commun 10 (1), 4679 (2019)
   PUBMED   31616000
  REMARK    GeneRIF: Pediatric patients with disruptive TANC2 mutations present
            with autism, intellectual disability, and delayed language and
            motor development. In addition to a variable degree of epilepsy and
            facial dysmorphism, we observe a pattern of more complex
            psychiatric dysfunction or behavioral problems in adult probands or
            carrier parents.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1990)
  AUTHORS   Stucchi,R., Plucinska,G., Hummel,J.J.A., Zahavi,E.E., Guerra San
            Juan,I., Klykov,O., Scheltema,R.A., Altelaar,A.F.M. and
            Hoogenraad,C.C.
  TITLE     Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM
            Controls DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to
            Postsynaptic Sites
  JOURNAL   Cell Rep 24 (3), 685-700 (2018)
   PUBMED   30021165
REFERENCE   8  (residues 1 to 1990)
  AUTHORS   Gasparini,A., Tosatto,S.C.E., Murgia,A. and Leonardi,E.
  TITLE     Dynamic scaffolds for neuronal signaling: in silico analysis of the
            TANC protein family
  JOURNAL   Sci Rep 7 (1), 6829 (2017)
   PUBMED   28754924
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1990)
  AUTHORS   Mahmood,S.F., Gruel,N., Chapeaublanc,E., Lescure,A., Jones,T.,
            Reyal,F., Vincent-Salomon,A., Raynal,V., Pierron,G., Perez,F.,
            Camonis,J., Del Nery,E., Delattre,O., Radvanyi,F. and
            Bernard-Pierrot,I.
  TITLE     A siRNA screen identifies RAD21, EIF3H, CHRAC1 and TANC2 as driver
            genes within the 8q23, 8q24.3 and 17q23 amplicons in breast cancer
            with effects on cell growth, survival and transformation
  JOURNAL   Carcinogenesis 35 (3), 670-682 (2014)
   PUBMED   24148822
  REMARK    GeneRIF: -RAD21 and EIF3H, both on chromosome 8q23, CHRAC1 on
            chromosome 8q24.3 and TANC2 on chromosome 17q23-were confirmed to
            be driver genes regulating the proliferation/survival of clonogenic
            breast cancer cells
REFERENCE   10 (residues 1 to 1990)
  AUTHORS   Han,S., Nam,J., Li,Y., Kim,S., Cho,S.H., Cho,Y.S., Choi,S.Y.,
            Choi,J., Han,K., Kim,Y., Na,M., Kim,H., Bae,Y.C., Choi,S.Y. and
            Kim,E.
  TITLE     Regulation of dendritic spines, spatial memory, and embryonic
            development by the TANC family of PSD-95-interacting proteins
  JOURNAL   J Neurosci 30 (45), 15102-15112 (2010)
   PUBMED   21068316
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005972.1, AC006270.1, AC015923.8 and AC005828.1.
            
            On or before Dec 21, 2018 this sequence version replaced
            XP_005257260.1, XP_371074.3, XP_947427.1, NP_079461.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2146236,
                              SAMEA2146982 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1990
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2-q23.3"
     Protein         1..1990
                     /product="protein TANC2 isoform 1"
                     /note="putative ankyrin-repeat containing protein; rolling
                     pebbles homolog B; protein TANC2; tetratricopeptide
                     repeat, ankyrin repeat and coiled-coil domain-containing
                     protein 2"
                     /calculated_mol_wt=219520
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          129..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          396..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          846..878
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          856..>1150
                     /region_name="PHA03095"
                     /note="ankyrin-like protein; Provisional"
                     /db_xref="CDD:222980"
     Region          884..913
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          889..915
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(890..891,894..896,898..899,903,906,915,917,919,
                     923..924,927..929,931..932,936,939,948,950,952,956..957,
                     960..962,964..965,969,972)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          917..948
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          917..946
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          950..979
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          990..1019
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1026..1267
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1033..1062
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1034..1064
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1066..1097
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1066..1095
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1099..1128
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1100..1130
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1101,1105..1106,1109..1111,1113..1114,1118,1121,
                     1130,1132,1134,1138..1139,1142..1144,1146..1147,1151,1154,
                     1163,1165,1167,1171..1172,1175..1177,1179..1180,1184,1187,
                     1196)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1132..1163
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1132..1161
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1165..1196
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1165..1194
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1198..1227
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1198..1223
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1244..1277
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1247..1272
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1248..1249,1252..1253,1255,1292,1295..1296,
                     1299..1300,1302..1303,1326,1329..1330,1333..1334,1337)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1251..>1365
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          1277..1320
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1291..1324
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1325..1358
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1325..1353
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1372..1401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          <1427..1656
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1430..1586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1563
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1576
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1692..1718
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1783..1803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1821..1843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Site            1928
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:A2A690; propagated from
                     UniProtKB/Swiss-Prot (Q9HCD6.3)"
     Region          1968..1990
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCD6.3)"
     CDS             1..1990
                     /gene="TANC2"
                     /gene_synonym="IDDALDS; rols; ROLSA"
                     /coded_by="NM_025185.4:539..6511"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45754.1"
                     /db_xref="GeneID:26115"
                     /db_xref="HGNC:HGNC:30212"
                     /db_xref="MIM:615047"
ORIGIN      
        1 mfrnslkmll tggkssrknr ssdggseepp drrqssvdsr qsrsgqggis tesdcafepd
       61 yavpplpvse gdaeqelgpp psvdeaantl mtrlgfllge kvtevqpgdq ysmevqdenq
      121 tsaitqrisp cstltsstas ppasspcstl ppistnatak dcsygavtsp tstlesrdsg
      181 iiatltsyse nvertkyage sskelgsggn ikpwqsqkss mdsclyrvde nmtastysln
      241 kipernletv lsqsvqsipl ylmprpnsva atssahledl ayldeqrhtp lrtslrmprq
      301 smggartqqd lrvrfapyrp pdislkpllf evpsittesv fvgrdwvfhe idaqlqssna
      361 svnqgvvivg nigfgktaii srlvalschg trmrqiasds phaspkhvda nrelpltqpp
      421 sahssitsgs cpgtpemrrr qeeamrrlas qvvayhycqa dnaytclvpe fvhnvaallc
      481 rspqltayre qllrephlqs mlslrscvqd pmasfrrgvl eplenlhker kipdedfiil
      541 idglneaefh kpdygdtivs flskmigkfp swlklivtvr tslqeitkll pfhrifldrl
      601 eeneaidqdl qayilhrihs sseiqnnisl ngkmdnttfg klsshlktls qgsylylklt
      661 fdliekgylv lksssykvvp vslsevyllq cnmkfptqss fdrvmpllnv avaslhpltd
      721 ehifqainag siegtlewed fqqrmenlsm flikrrdmtr mfvhpsfrew liwreegekt
      781 kflcdprsgh tllafwfsrq egklnrqqti elghhilkah ifkglskkvg vsssilqglw
      841 isysteglsm alaslrnlyt pnikvsrlli lgganinyrt evlnnapilc vqshlgytem
      901 valllefgan vdassesglt plgyaaaagy lsivvllckk rakvdhldkn gqcalvhaal
      961 rghlevvkfl iqcdwtmagq qqgvfkksha iqqaliaaas mgyteivsyl ldlpekdeee
     1021 veraqinsfd slwgetalta aagrgklevc rllleqgaav aqpnrrgavp lfstvrqghw
     1081 qivdlllthg advnmadkqg rtplmmaase ghlgtvdfll aqgasialmd kegltalswa
     1141 clkghlsvvr slvdngaatd hadkngrtpl dlaafygdae vvqflvdhga miehvdysgm
     1201 rpldravgcr ntsvvvtllk kgakigpatw amatskpdim iillsklmee gdmfykkgkv
     1261 keaaqryqya lkkfpregfg edlktfrelk vslllnlsrc rrkmndfgma eefatkalel
     1321 kpksyeayya rarakrssrq faaaledlne aiklcpnnre iqrlllrvee ecrqmqqpqq
     1381 pppppqpqqq lpeeaepepq hediysvqdi feeeyleqdv envsiglqte arpsqglpvi
     1441 qsppsspphr dsayissspl gshqvfdfrs sssvgsptrq tyqstspals pthqnshyrp
     1501 spphtspahq ggsyrfsppp vggqgkeyps pppsplrrgp qyrasppaes msvyrsqsgs
     1561 pvryqqetsv sqlpgrpksp lskmaqrpyq mpqlpvavpq qglrlqpaka qivrsnqpsp
     1621 avhsstvipt gaygqvahsm askyqssqgd igvsqsrlvy qgsiggivgd grpvqhvqas
     1681 lsagaicqhg gltkedlpqr pssayrggvr ysqtpqigrs qsasyypvch skldlersss
     1741 qlgspdvshl irrpisvnpn eikphpptpr pllhsqsvgl rfspssnsis stsnltptfr
     1801 psssiqqmei plkpayersc delspvsptq ggypseptrs rttpfmgiid ktartqqyph
     1861 lhqqnrtwav ssvdtvlspt spgnlpqpes fsppssisni afynktnnaq nghlleddyy
     1921 sphgmlangs rgdllervsq assypdvkva rtlpvaqayq dnlyrqlsrd srqgqtspik
     1981 pkrpfvesnv
//
LOCUS       NP_001356800            1167 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 7 [Homo sapiens].
ACCESSION   NP_001356800
VERSION     NP_001356800.1
DBSOURCE    REFSEQ: accession NM_001369871.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1167)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1167)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1167)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1167)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1167)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1167)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1167)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590238.9 and AL358113.21.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1949221.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968832,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1167
                     /product="tight junction protein 2 isoform 7"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=131237
     Region          9..95
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(20..26,44,47,75,79,82..83)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          121..>203
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          160..>251
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          283..361
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(283..289,294..310,313..315,318,320..321,328,
                     336..337,339..340,352..358)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(295..301,307,310,340,344,347..348)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          486..567
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(497..503,513,516,545,549,552..553)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          581..643
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(590,592,595,599,620..621,637,639..640)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          677..856
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1167
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_001369871.1:348..3851"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 meeliweqyt vtlqkdskrg fgiavsggrd nphfengets ivisdvlpgg padgllqend
       61 rvvmvngtpm edvlhsfavq qlrksgkvaa ivvkrprkvq vaalqasppl dqddrafevm
      121 defdgrsfrs gysersrlns hggrsrswed spergrpher arsrerdlsr drsrgrsler
      181 gldqdhartr drsrgrsler gldhdfgpsr drdrdrsrgr sidqdyeray hraydpdyer
      241 ayspeyrrga rhdarsrgpr srsrehphsr spspeprgrp gpigvllmks raneeyglrl
      301 gsqifvkemt rtglatkdgn lhegdiilki ngtvtenmsl tdarklieks rgklqlvvlr
      361 dsqqtlinip slndsdseie diseiesnrs fspeerrhqy sdydyhssse klkerpssre
      421 dtpsrlsrmg atptpfkstg diagtvvpet nkepryqedp papqpkaapr tflrpspede
      481 aiygpntkmv rfkkgdsvgl rlaggndvgi fvagiqegts aeqeglqegd qilkvntqdf
      541 rglvredavl ylleipkgem vtilaqsrad vyrdilacgr gdsffirshf eceketpqsl
      601 aftrgevfrv vdtlydgklg nwlavrigne lekglipnks raeqmasvqn aqrdnagdra
      661 dfwrmrgqrs gvkknlrksr edltavvsvs tkfpayervl lreagfkrpv vlfgpiadia
      721 meklanelpd wfqtaktepk dagsekstgv vrlntvrqii eqdkhalldv tpkavdllny
      781 tqwfpiviff npdsrqgvkt mrqrlnptsn kssrklfdqa nklkktcahl ftatinlnsa
      841 ndswfgslkd tiqhqqgeav wvsegkmegm dddpedrmsy ltamgadyls cdsrlisdfe
      901 dtdgeggayt dneldepaee plvssitrss epvqheesir kpspepraqm rraassdqlr
      961 dnspppafkp eppkaktqnk eesydfsksy eyksnpsava gnetpgastk gypppvaakp
     1021 tfgrsilkps tpippqegee vgesseeqdn apksvlgkvk ifekmdhkar lqrmqelqea
     1081 qnarieiaqk hpdiyavpik thkpdpgtpq htssrppepq kapsrpyqdt rgsygsdaee
     1141 eeyrqqlseh skrgyygqsa ryrdtel
//
LOCUS       NP_001007240             543 aa            linear   PRI 20-NOV-2025
DEFINITION  eEF1A lysine and N-terminal methyltransferase isoform 3 [Homo
            sapiens].
ACCESSION   NP_001007240
VERSION     NP_001007240.1
DBSOURCE    REFSEQ: accession NM_001007239.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Boulter,M. and Biggar,K.K.
  TITLE     Biological Relevance of Dual Lysine and N-Terminal
            Methyltransferase METTL13
  JOURNAL   Biomolecules 14 (9), 1112 (2024)
   PUBMED   39334878
  REMARK    GeneRIF: Biological Relevance of Dual Lysine and N-Terminal
            Methyltransferase METTL13.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Ni,H., Liang,C., Zhou,Z., Jiang,B., Li,Y., Shang,H. and Yu,X.
  TITLE     METTL13 promotes nasopharyngeal carcinoma progression through
            regulating the ZEB1/TPT1 axis
  JOURNAL   J Gene Med 25 (5), e3476 (2023)
   PUBMED   36735630
  REMARK    GeneRIF: METTL13 promotes nasopharyngeal carcinoma progression
            through regulating the ZEB1/TPT1 axis.
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Liu,Z., Sun,T., Piao,C., Zhang,Z. and Kong,C.
  TITLE     METTL13 inhibits progression of clear cell renal cell carcinoma
            with repression on PI3K/AKT/mTOR/HIF-1alpha pathway and c-Myc
            expression
  JOURNAL   J Transl Med 19 (1), 209 (2021)
   PUBMED   33985542
  REMARK    GeneRIF: METTL13 inhibits progression of clear cell renal cell
            carcinoma with repression on PI3K/AKT/mTOR/HIF-1alpha pathway and
            c-Myc expression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Takahashi,A., Tokita,H., Takahashi,K., Takeoka,T., Murayama,K.,
            Tomotsune,D., Ohira,M., Iwamatsu,A., Ohara,K., Yazaki,K., Koda,T.,
            Nakagawara,A. and Tani,K.
  TITLE     A novel potent tumour promoter aberrantly overexpressed in most
            human cancers
  JOURNAL   Sci Rep 1, 15 (2011)
   PUBMED   22355534
  REMARK    Erratum:[Sci Rep. 2013;3:49]
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 543)
  AUTHORS   Wilcox,E., Riazuddin,S. and Riazuddin,S.
  TITLE     Some deafness-causing mutations can be silenced with the
            appropriate gene partner
  JOURNAL   ScientificWorldJournal 1, 202-203 (2001)
   PUBMED   12805671
  REMARK    GeneRIF: The DFNM1 gene modified the phenotype of a inherited
            deafness family possibly by silencing the DFNB26 mutated gene.
            Review article
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Riazuddin,S., Castelein,C.M., Ahmed,Z.M., Lalwani,A.K.,
            Mastroianni,M.A., Naz,S., Smith,T.N., Liburd,N.A., Friedman,T.B.,
            Griffith,A.J., Riazuddin,S. and Wilcox,E.R.
  TITLE     Dominant modifier DFNM1 suppresses recessive deafness DFNB26
  JOURNAL   Nat Genet 26 (4), 431-434 (2000)
   PUBMED   11101839
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI091265.1, AL049669.1 and BX094025.1.
            
            Transcript Variant: This variant (3) lacks an in-frame segment in
            the 5' coding region, as compared to variant 1. The encoded isoform
            3 thus lacks an internal segment, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL049669.1, SRR1803611.93908.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.3"
     Protein         1..543
                     /product="eEF1A lysine and N-terminal methyltransferase
                     isoform 3"
                     /note="methyltransferase-like protein 13; antiapoptotic
                     protein FEAT; methyltransferase like 13; eEF1A-KNMT;
                     deafness (recessive, non-syndromic) modifier 1; deafness
                     (autosomal recessive, nonsyndromic) modifier 1; deafness
                     (recessive, nonsyndromic) modifier 1; faint expression in
                     normal tissues, aberrant overexpression in tumors; eEF1A
                     lysine and N-terminal methyltransferase; methyltransferase
                     13, eEF1A lysine and N-terminal methyltransferase"
                     /calculated_mol_wt=60997
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8N6R0.1)"
     Region          52..150
                     /region_name="Methyltransf_25"
                     /note="Methyltransferase domain; pfam13649"
                     /db_xref="CDD:463945"
     Region          <343..483
                     /region_name="SpeE"
                     /note="Spermidine synthase (polyamine
                     aminopropyltransferase) [Amino acid transport and
                     metabolism]; COG0421"
                     /db_xref="CDD:440190"
     CDS             1..543
                     /gene="METTL13"
                     /gene_synonym="5630401D24Rik; CGI-01; DFNB26; DFNB26M;
                     DFNM1; EEF1AKNMT; feat; KIAA0859"
                     /coded_by="NM_001007239.2:309..1940"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS30936.1"
                     /db_xref="GeneID:51603"
                     /db_xref="HGNC:HGNC:24248"
                     /db_xref="MIM:617987"
ORIGIN      
        1 mnllpkssre fgsvdywekf fqqrgkkafe wygtylelcg vlhkyikpre kvlvigcgns
       61 elseqlydvg yrdivnidis evvikqmkec natrrpqmsf lkmdmtqmef pdasfqvvld
      121 kgtldavltd eeektlqqvd rmlaevgrvl qgretewlfg mdegrkqlaa sagfrrlitv
      181 alhrgqqyes mdhiqaelsa rvmelapagm ptqqqvpfls vggdigvrtv qhqdcsplsg
      241 dyviedvqgd dkryfrrlif lsnrnvvqse arllkdvshk aqkkrkkdrk kqrpadaedl
      301 paapgqsidk sylccehhka miaglallrn pellleipla llvvglgggs lplfvhdhfp
      361 kscidaveid psmlevatqw fgfsqsdrmk vhiadgldyi aslagggear pcydvimfdv
      421 dskdptlgms cpppafveqs flqkvksilt pegvfilnlv crdlglkdsv laglkavfpl
      481 lyvrriegev neilfcqlhp eqklatpell etaqalertl rkpgrgwddt yvlsdmlktv
      541 kiv
//
LOCUS       NP_001290473             192 aa            linear   PRI 20-NOV-2025
DEFINITION  prefoldin subunit 3 isoform 3 [Homo sapiens].
ACCESSION   NP_001290473 XP_005274786
VERSION     NP_001290473.1
DBSOURCE    REFSEQ: accession NM_001303544.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Miao,H., Gao,W., Zhong,L., Li,H., Chen,D., Xu,C., Wen,Z. and
            Chen,Y.
  TITLE     VBP1 promotes tumor proliferation as a part of the hypoxia-related
            signature in esophageal squamous cell carcinoma
  JOURNAL   Hum Cell 37 (4), 1141-1155 (2024)
   PUBMED   38700744
  REMARK    GeneRIF: VBP1 promotes tumor proliferation as a part of the
            hypoxia-related signature in esophageal squamous cell carcinoma.
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Clifford,S.C., Walsh,S., Hewson,K., Green,E.K., Brinke,A.,
            Green,P.M., Gianelli,F., Eng,C. and Maher,E.R.
  TITLE     Genomic organization and chromosomal localization of the human CUL2
            gene and the role of von Hippel-Lindau tumor suppressor-binding
            protein (CUL2 and VBP1) mutation and loss in renal-cell carcinoma
            development
  JOURNAL   Genes Chromosomes Cancer 26 (1), 20-28 (1999)
   PUBMED   10441001
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Hemberger,M., Himmelbauer,H., Neumann,H.P., Plate,K.H.,
            Schwarzkopf,G. and Fundele,R.
  TITLE     Expression of the von Hippel-Lindau-binding protein-1 (Vbp1) in
            fetal and adult mouse tissues
  JOURNAL   Hum Mol Genet 8 (2), 229-236 (1999)
   PUBMED   9931330
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Brinke,A., Green,P.M. and Giannelli,F.
  TITLE     Characterization of the gene (VBP1) and transcript for the von
            Hippel-Lindau binding protein and isolation of the highly conserved
            murine homologue
  JOURNAL   Genomics 45 (1), 105-112 (1997)
   PUBMED   9339366
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Tsuchiya,H., Iseda,T. and Hino,O.
  TITLE     Identification of a novel protein (VBP-1) binding to the von
            Hippel-Lindau (VHL) tumor suppressor gene product
  JOURNAL   Cancer Res 56 (13), 2881-2885 (1996)
   PUBMED   8674032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301646.1, BC009570.1 and
            AA626259.1.
            
            On Jan 13, 2015 this sequence version replaced XP_005274786.2.
            
            Summary: The protein encoded by this gene interacts with the Von
            Hippel-Lindau protein to form an intracellular complex. The encoded
            protein functions as a chaperone protein, and may play a role in
            the transport of the Von Hippel-Lindau protein from the perinuclear
            granules to the nucleus or cytoplasm. Alternative splicing and the
            use of alternate transcription start sites results in multiple
            transcript variants encoding different protein isoforms. [provided
            by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (3) has a distinct N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301646.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..192
                     /product="prefoldin subunit 3 isoform 3"
                     /note="prefoldin subunit 3; von Hippel-Lindau binding
                     protein 1"
                     /calculated_mol_wt=22123
     Region          47..175
                     /region_name="Prefoldin_3"
                     /note="Prefoldin subunit 3; cd23156"
                     /db_xref="CDD:467472"
     Region          47..86
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467472"
     Site            order(48,51..52,55,159,162..163,165..167,169..170)
                     /site_type="other"
                     /note="prefoldin/TRiC interface [polypeptide binding]"
                     /db_xref="CDD:467472"
     Site            order(75,78..79,82..83,85..86,96..103,105..114,117..121,
                     125..130,139)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467472"
     Region          133..175
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467472"
     CDS             1..192
                     /gene="VBP1"
                     /gene_synonym="HIBBJ46; PFD3; PFDN3; VBP-1"
                     /coded_by="NM_001303544.1:164..742"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS78525.1"
                     /db_xref="GeneID:7411"
                     /db_xref="HGNC:HGNC:12662"
                     /db_xref="MIM:300133"
ORIGIN      
        1 mapqpmihtq qglrtsspst pspehqedvd sfmkqpgnet adtvlkklde qyqkykfmel
       61 nlaqkkrrlk gqipeikqtl eilkymqkkk estnsmetrf lladnlycka svpptdkvcl
      121 wlganvmley dideaqalle knlstatknl dsleedldfl rdqftttevn marvynwdvk
      181 rrnkddstkn ka
//
LOCUS       NP_001002909            1502 aa            linear   PRI 20-NOV-2025
DEFINITION  G patch domain-containing protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_001002909 XP_290758
VERSION     NP_001002909.1
DBSOURCE    REFSEQ: accession NM_001002909.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1502)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1502)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
  REMARK    GeneRIF: GPATCH8 modulates mutant SF3B1 mis-splicing and
            pathogenicity in hematologic malignancies.
REFERENCE   3  (residues 1 to 1502)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1502)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 1502)
  AUTHORS   Kaneko,H., Kitoh,H., Matsuura,T., Masuda,A., Ito,M., Mottes,M.,
            Rauch,F., Ishiguro,N. and Ohno,K.
  TITLE     Hyperuricemia cosegregating with osteogenesis imperfecta is
            associated with a mutation in GPATCH8
  JOURNAL   Hum Genet 130 (5), 671-683 (2011)
   PUBMED   21594610
  REMARK    GeneRIF: Two missense single-nucleotide variants in ZPBP2 and
            GPATCH8 on chromosome 17 were identified that cosegregated with
            hyperuricemia in the Japanese family.
REFERENCE   6  (residues 1 to 1502)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 1502)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1502)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 1502)
  AUTHORS   Thornton,M.A., Poncz,M., Korostishevsky,M., Yakobson,E., Usher,S.,
            Seligsohn,U. and Peretz,H.
  TITLE     The human platelet alphaIIb gene is not closely linked to its
            integrin partner beta3
  JOURNAL   Blood 94 (6), 2039-2047 (1999)
   PUBMED   10477733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY048299.1, AK025600.1,
            BC136629.1 and BC024147.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2004 this sequence version replaced XP_290758.5.
            
            Summary: The protein encoded by this gene contains an
            RNA-processing domain, a zinc finger domain, a lysine-rich region
            and a serine-rich region. A mutation in the serine-rich region of
            the protein is thought to be associated with hyperuricemia (PMID:
            21594610). Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Feb
            2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.12881.1,
                                           SRR1660805.222318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000591680.6/ ENSP00000467556.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1502
                     /product="G patch domain-containing protein 8 isoform 1"
                     /note="g patch domain-containing protein 8"
                     /calculated_mol_wt=164067
     Region          40..82
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Region          <82..>207
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          136..163
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          172..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          323..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          419..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            479
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          579..1301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1009
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1033
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Region          <1056..1316
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Site            1081
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     Site            1175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A6A1; propagated from
                     UniProtKB/Swiss-Prot (Q9UKJ3.2)"
     CDS             1..1502
                     /gene="GPATCH8"
                     /gene_synonym="GPATC8; KIAA0553"
                     /coded_by="NM_001002909.4:37..4545"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32666.1"
                     /db_xref="GeneID:23131"
                     /db_xref="HGNC:HGNC:29066"
                     /db_xref="MIM:614396"
ORIGIN      
        1 madrfsrfne drdfqgnhfd qyeeghleie qasldkpies dnighrllqk hgwklgqglg
       61 kslqgrtdpi pivvkydvmg mgrmemeldy aedaterrrv levekedtee lrqkykdyvd
      121 kekaiakale dlranfycel cdkqyqkhqe fdnhinsydh ahkqrlkdlk qrefarnvss
      181 rsrkdekkqe kalrrlhela eqrkqaecap gsgpmfkptt vavdeegged dkdesatnsg
      241 tgatascglg sefstdkggp ftavqitntt glaqapglas qgisfgiknn lgtplqklgv
      301 sfsfakkapv klesiasvfk dhaeegtsed gtkpdekssd qglqkvgdsd gssnldgkke
      361 dedpqdggsl astlsklkrm kreegagate peyyhyippa hckvkpnfpf llfmraseqm
      421 dgdntthpkn apeskkgssp kpkscikaaa sqgaektvse vseqpketsm tepsepgska
      481 eakkalggdv sdqsleshsq kvsetqmces nssketslat pagkesqegp khptgpffpv
      541 lskdestalq wpselliftk aepsisyscn plyfdfklsr nkdartkgte kpkdigsssk
      601 dhlqgldpge pnkskevgge kivrssggrm dapasgsacs glnkqepggs hgsetedtgr
      661 slpskkersg kshrhkkkkk hkksskhkrk hkadteekss kaesgekskk rkkrkrkknk
      721 ssapadserg pkpeppgsgs papprrrrra qddsqrrslp aeegssgkkd eggggsssqd
      781 hggrkhkgel ppsscqrrag tkrssrsshr sqpssgdeds ddasshrlhq kspsqyseee
      841 eeedsgsehs rsrsrsgrrh sshrssrrsy ssssdassdq scysrqrsys ddsysdysdr
      901 srrhskrshd sddsdyassk hrskrhkyss sdddyslscs qsrsrsrsht rersrsrgrs
      961 rssscsrsrs krrsrsttah swqrsrsysr drsrstrsps qrsgsrkrsw ghespeerhs
     1021 grrdfirski yrsqsphyfr sgrgegpgkk ddgrgddska tgppsqnsni gtgrgsegdc
     1081 spedknsvta klllekiqsr kverkpsvse evqatpnkag pklkdppqgy fgpklppslg
     1141 nkpvlpligk lpatrkpnkk ceesglerge eqeqseteeg ppgssdalfg hqfpseettg
     1201 plldpppees ksgeatadhp vaplgtpahs dcypgdptis hnylpdpsdg dtlesldsss
     1261 qpgpvessll piapdlehfp syappsgdps iestdgaeda slaplesqpi tftpeemeky
     1321 sklqqaaqqh iqqqllakqv kafpasaala patpalqpih iqqpatasat sittvqhail
     1381 qhhaaaaaaa igihphphpq plaqvhhipq phltpislsh lthsiipghp atflashpih
     1441 iipasaihpg pftfhpvpha alyptllapr paaaaatalh lhpllhpifs gqdlqhppsh
     1501 gt
//
LOCUS       NP_001356342             297 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356342 XP_016881951
VERSION     NP_001356342.1
DBSOURCE    REFSEQ: accession NM_001369413.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 297)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 297)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138128.1, AC139353.3 and
            AC092309.3.
            
            On Apr 9, 2019 this sequence version replaced XP_016881951.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.130189.1,
                                           SRR14038195.610980.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..297
                     /product="DNA excision repair protein ERCC-1 isoform 2"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=32431
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          220..297
                     /region_name="HhH2, dimerization with ERCC4/XPF.
                     /evidence=ECO:0000269|PubMed:16338413"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          <251..293
                     /region_name="MUS81"
                     /note="ERCC4-type crossover junction endonuclease
                     [Replication, recombination and repair]; COG1948"
                     /db_xref="CDD:441551"
     CDS             1..297
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369413.1:152..1045"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS12662.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq karrlfdvlh epflkvp
//
LOCUS       NP_001340231             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 3 [Homo sapiens].
ACCESSION   NP_001340231 XP_016869042
VERSION     NP_001340231.1
DBSOURCE    REFSEQ: accession NM_001353302.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869042.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.261048.1,
                                           SRR1803616.164624.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 3"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36689
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353302.1:281..1255"
                     /note="isoform 3 is encoded by transcript variant 64"
                     /db_xref="CCDS:CCDS94340.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnlikvltr didhnaahff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_064574                101 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription and mRNA export factor ENY2 isoform 1 [Homo sapiens].
ACCESSION   NP_064574
VERSION     NP_064574.1
DBSOURCE    REFSEQ: accession NM_020189.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Li,W., Atanassov,B.S., Lan,X., Mohan,R.D., Swanson,S.K.,
            Farria,A.T., Florens,L., Washburn,M.P., Workman,J.L. and
            Dent,S.Y.R.
  TITLE     Cytoplasmic ATXN7L3B Interferes with Nuclear Functions of the SAGA
            Deubiquitinase Module
  JOURNAL   Mol Cell Biol 36 (22), 2855-2866 (2016)
   PUBMED   27601583
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   7  (residues 1 to 101)
  AUTHORS   Georgieva,S., Nabirochkina,E., Dilworth,F.J., Eickhoff,H.,
            Becker,P., Tora,L., Georgiev,P. and Soldatov,A.
  TITLE     The novel transcription factor e(y)2 interacts with TAF(II)40 and
            potentiates transcription activation on chromatin templates
  JOURNAL   Mol Cell Biol 21 (15), 5223-5231 (2001)
   PUBMED   11438676
REFERENCE   8  (residues 1 to 101)
  AUTHORS   Brand,M., Moggs,J.G., Oulad-Abdelghani,M., Lejeune,F.,
            Dilworth,F.J., Stevenin,J., Almouzni,G. and Tora,L.
  TITLE     UV-damaged DNA-binding protein in the TFTC complex links DNA damage
            recognition to nucleosome acetylation
  JOURNAL   EMBO J 20 (12), 3187-3196 (2001)
   PUBMED   11406595
REFERENCE   9  (residues 1 to 101)
  AUTHORS   Brand,M., Yamamoto,K., Staub,A. and Tora,L.
  TITLE     Identification of TATA-binding protein-free TAFII-containing
            complex subunits suggests a role in nucleosome acetylation and
            signal transduction
  JOURNAL   J Biol Chem 274 (26), 18285-18289 (1999)
   PUBMED   10373431
REFERENCE   10 (residues 1 to 101)
  AUTHORS   Wieczorek,E., Brand,M., Jacq,X. and Tora,L.
  TITLE     Function of TAF(II)-containing complex without TBP in transcription
            by RNA polymerase II
  JOURNAL   Nature 393 (6681), 187-191 (1998)
   PUBMED   9603525
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF173296.1, AK095651.1 and BU737295.1.
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA292445.1, SRR1660805.187602.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521688.6/ ENSP00000429986.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..101
                     /product="transcription and mRNA export factor ENY2
                     isoform 1"
                     /note="enhancer of yellow 2 transcription factor homolog;
                     transcription and mRNA export factor ENY2; enhancer of
                     yellow 2 homolog"
                     /calculated_mol_wt=11397
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NPA8.1)"
     Region          16..94
                     /region_name="EnY2"
                     /note="Transcription factor e(y)2; pfam10163"
                     /db_xref="CDD:462972"
     CDS             1..101
                     /gene="ENY2"
                     /gene_synonym="DC6; e(y)2; Sus1"
                     /coded_by="NM_020189.6:123..428"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43762.1"
                     /db_xref="GeneID:56943"
                     /db_xref="HGNC:HGNC:24449"
                     /db_xref="MIM:619015"
ORIGIN      
        1 mvvskmnkda qmraainqkl ietgererlk ellrakliec gwkdqlkahc kevikekgle
       61 hvtvddlvae itpkgralvp dsvkkellqr irtflaqhas l
//
LOCUS       NP_001306163             117 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL34 [Homo sapiens].
ACCESSION   NP_001306163
VERSION     NP_001306163.1
DBSOURCE    REFSEQ: accession NM_001319234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Zhu,Y., Ren,C., Jiang,D., Yang,L., Chen,Y., Li,F., Wang,B. and
            Zhang,Y.
  TITLE     RPL34-AS1-induced RPL34 inhibits cervical cancer cell tumorigenesis
            via the MDM2-P53 pathway
  JOURNAL   Cancer Sci 112 (5), 1811-1821 (2021)
   PUBMED   33675124
  REMARK    GeneRIF: RPL34-AS1-induced RPL34 inhibits cervical cancer cell
            tumorigenesis via the MDM2-P53 pathway.
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Yang,S., Cui,J., Yang,Y., Liu,Z., Yan,H., Tang,C., Wang,H., Qin,H.,
            Li,X., Li,J., Wang,W., Huang,Y. and Gao,H.
  TITLE     Over-expressed RPL34 promotes malignant proliferation of non-small
            cell lung cancer cells
  JOURNAL   Gene 576 (1 Pt 3), 421-428 (2016)
   PUBMED   26526135
  REMARK    GeneRIF: over-expressed RPL34 may promote malignant proliferation
            of NSCLC cells, thus playing an important role in development and
            progress of NSCLC
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 117)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 117)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB132938.1 and DA779124.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L34E family of ribosomal proteins. It is located in the
            cytoplasm. This gene originally was thought to be located at 17q21,
            but it has been mapped to 4q. Overexpression of this gene has been
            observed in some cancer cells. Alternative splicing results in
            multiple transcript variants, all encoding the same isoform. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome.
            [provided by RefSeq, Feb 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB132938.1, BU860884.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..117
                     /product="large ribosomal subunit protein eL34"
                     /note="60S ribosomal protein L34; leukemia-associated
                     protein"
                     /calculated_mol_wt=13162
     Region          1..96
                     /region_name="Ribosomal_L34e"
                     /note="Ribosomal protein L34e; pfam01199"
                     /db_xref="CDD:426119"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49207.3)"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49207.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1R9; propagated from
                     UniProtKB/Swiss-Prot (P49207.3)"
     CDS             1..117
                     /gene="RPL34"
                     /gene_synonym="eL34; L34"
                     /coded_by="NM_001319234.1:183..536"
                     /db_xref="CCDS:CCDS3680.1"
                     /db_xref="GeneID:6164"
                     /db_xref="HGNC:HGNC:10340"
                     /db_xref="MIM:616862"
ORIGIN      
        1 mvqrltyrrr lsyntasnkt rlsrtpgnri vylytkkvgk apksacgvcp grlrgvravr
       61 pkvlmrlskt kkhvsraygg smcakcvrdr ikraflieeq kivvkvlkaq aqsqkak
//
LOCUS       NP_974199                333 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing protein GIPC1 isoform 1 [Homo sapiens].
ACCESSION   NP_974199
VERSION     NP_974199.1
DBSOURCE    REFSEQ: accession NM_202470.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Gu,X., Jiao,K., Yue,D., Wang,X., Qiao,K., Gao,M., Lin,J., Sun,C.,
            Zhao,C., Zhu,W. and Xi,J.
  TITLE     Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report
  JOURNAL   Neuromuscul Disord 33 (9), 93-97 (2023)
   PUBMED   37550168
  REMARK    GeneRIF: Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report.
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Fan,Y., Shen,S., Yang,J., Yao,D., Li,M., Mao,C., Wang,Y., Hao,X.,
            Ma,D., Li,J., Shi,J., Guo,M., Li,S., Yuan,Y., Liu,F., Yang,Z.,
            Zhang,S., Hu,Z., Fan,L., Liu,H., Zhang,C., Wang,Y., Wang,Q.,
            Zheng,H., He,Y., Song,B., Xu,Y. and Shi,C.
  TITLE     GIPC1 CGG Repeat Expansion Is Associated with Movement Disorders
  JOURNAL   Ann Neurol 91 (5), 704-715 (2022)
   PUBMED   35152460
  REMARK    GeneRIF: GIPC1 CGG Repeat Expansion Is Associated with Movement
            Disorders.
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Wang,L.H., Kalb,R.G. and Strittmatter,S.M.
  TITLE     A PDZ protein regulates the distribution of the transmembrane
            semaphorin, M-SemF
  JOURNAL   J Biol Chem 274 (20), 14137-14146 (1999)
   PUBMED   10318831
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Bunn,R.C., Jensen,M.A. and Reed,B.C.
  TITLE     Protein interactions with the glucose transporter binding protein
            GLUT1CBP that provide a link between GLUT1 and the cytoskeleton
  JOURNAL   Mol Biol Cell 10 (4), 819-832 (1999)
   PUBMED   10198040
REFERENCE   8  (residues 1 to 333)
  AUTHORS   De Vries,L., Lou,X., Zhao,G., Zheng,B. and Farquhar,M.G.
  TITLE     GIPC, a PDZ domain containing protein, interacts specifically with
            the C terminus of RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 95 (21), 12340-12345 (1998)
   PUBMED   9770488
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Rousset,R., Fabre,S., Desbois,C., Bantignies,F. and Jalinot,P.
  TITLE     The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
            with the PDZ domain of cellular proteins
  JOURNAL   Oncogene 16 (5), 643-654 (1998)
   PUBMED   9482110
REFERENCE   10 (residues 1 to 333)
  AUTHORS   De Vries,L., Elenko,E., Hubler,L., Jones,T.L. and Farquhar,M.G.
  TITLE     GAIP is membrane-anchored by palmitoylation and interacts with the
            activated (GTP-bound) form of G alpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15203-15208 (1996)
   PUBMED   8986788
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012318.7, AF089816.1 and BC000410.2.
            
            Summary: GIPC1 is a scaffolding protein that regulates cell surface
            receptor expression and trafficking (Lee et al., 2008 [PubMed
            18775991]).[supplied by OMIM, Apr 2009].
            
            Transcript Variant: This variant (5) lacks two consecutive exons in
            the 5' UTR, compared to variant 1. Variants 1, 3 and 5 encode the
            same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF089816.1, SRR3476690.12519.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..333
                     /product="PDZ domain-containing protein GIPC1 isoform 1"
                     /note="GLUT1 C-terminal binding protein; IGF-1 receptor
                     interacting protein 1; regulator of G-protein signalling
                     19 interacting protein 1; PDZ domain-containing protein
                     GIPC1; tax interaction protein 2; RGS19-interacting
                     protein 1; RGS-GAIP-interacting protein; GAIP
                     C-terminus-interacting protein"
                     /calculated_mol_wt=35918
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          126..219
                     /region_name="PDZ_GIPC1"
                     /note="PDZ domain of PDZ domain-containing protein GIPC1;
                     cd23077"
                     /db_xref="CDD:467290"
     Site            order(142..148,158,161,191,195,198..199)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467290"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          223..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14908.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14908.2)"
     Region          261..325
                     /region_name="GH2_GIPC"
                     /note="GIPC-homology 2 (GH2) domain found in the GIPC
                     family; cd21180"
                     /db_xref="CDD:409666"
     Site            order(273,276..281,311)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409666"
     Site            order(274..278,280,282..283,310..312,314,316)
                     /site_type="other"
                     /note="myosin VI binding site [polypeptide binding]"
                     /db_xref="CDD:409666"
     CDS             1..333
                     /gene="GIPC1"
                     /gene_synonym="C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1;
                     NIP; OPDM2; RGS19IP1; SEMCAP; SYNECTIIN; SYNECTIN; TIP-2"
                     /coded_by="NM_202470.3:122..1123"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS12310.1"
                     /db_xref="GeneID:10755"
                     /db_xref="HGNC:HGNC:1226"
                     /db_xref="MIM:605072"
ORIGIN      
        1 mplglgrrkk applveneea epgrgglgvg epgplggggs ggpqmglppp ppalrprlvf
       61 htqlahgspt griegftnvk elygkiaeaf rlptaevmfc tlnthkvdmd kllggqigle
      121 dfifahvkgq rkevevfkse dalgltitdn gagyafikri kegsvidhih lisvgdmiea
      181 ingqsllgcr hyevarllke lprgrtftlk lteprkafdm isqrsaggrp gsgpqlgtgr
      241 gtlrlrsrgp atvedlpsaf eekaiekvdd llesymgird telaatmvel gkdkrnpdel
      301 aealderlgd fafpdefvfd vwgaigdakv gry
//
LOCUS       NP_001310874             971 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001310874 XP_005254202
VERSION     NP_001310874.1
DBSOURCE    REFSEQ: accession NM_001323945.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 971)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 971)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 971)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 971)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 971)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 971)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Apr 23, 2016 this sequence version replaced XP_005254202.1.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.103133.1,
                                           SRR1803614.277865.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..971
                     /product="DIS3-like exonuclease 1 isoform 2"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=110988
     Region          <1..105
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          155..783
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          798..873
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..971
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323945.2:745..3660"
                     /note="isoform 2 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS10214.1"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mqtacqavqh qrgrrqynkl rnllkdarhd cilfanefqq ccylprerge smekwqtrsi
       61 ynaavwyyhh cqdrmpivmv tedeeaiqqy gsetegvfvi tfknyldnfw pdlkaahelc
      121 dsilqsrrer enesqeshgk eypehlplev leagiksgry iqgilnvnkh raqieafvrl
      181 qgasskdsdl vsdilihgmk arnrsihgdv vvvellpkne wkgrtvalce ndcddkasge
      241 spsepmptgr vvgilqknwr dyvvtfpske evqsqgknaq kilvtpwdyr ipkiristqq
      301 aetlqdfrvv vridswests vypnghfvrv lgrigdlege iatilvensi svipfseaqm
      361 cempvntpes pwkvspeeeq krkdlrkshl vfsidpkgce dvddtlsvrt lnngnlelgv
      421 hiadvthfva pnsyidiear trattyylad rrydmlpsvl sadlcsllgg vdryavsimw
      481 eldkasyeik kvwygrtiir sayklfyeaa qelldgnlsv vddipefkdl deksrqakle
      541 elvwaigklt diarhvrakr dgcgaleleg vevcvqlddk knihdlipkq plevhetvae
      601 cmilanhwva kkiwesfphq allrqhppph qeffselrec akakgffidt rsnktladsl
      661 dnandphdpi vnrllrsmat qamsnalyfs tgscaeeefh hyglaldkyt hftspirrys
      721 divvhrllma aiskdkkmei kgnlfsnkdl eelcrhinnr nqaaqhsqkq stelfqcmyf
      781 kdkdpateer cisdgviysi rtngvllfip rfgikgaayl knkdglvisc gpdscsewkp
      841 gslqrfqnki tstttdgesv tfhlfdhvtv risiqasrch sdtirleiis nkpykipnte
      901 lihqsspllk selvkevtks veeaqlaqev kvniiqeeyq eyrqtkgrsl ytlleeirdl
      961 alldvsnnyg i
//
LOCUS       NP_001091074              69 aa            linear   PRI 20-NOV-2025
DEFINITION  X antigen family member 1 isoform d [Homo sapiens].
ACCESSION   NP_001091074
VERSION     NP_001091074.1
DBSOURCE    REFSEQ: accession NM_001097605.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Mori,M., Funakoshi,T., Kameyama,K., Kawakami,Y., Sato,E.,
            Nakayama,E., Amagai,M. and Tanese,K.
  TITLE     Lack of XAGE-1b and NY-ESO-1 in metastatic lymph nodes may predict
            the potential survival of stage III melanoma patients
  JOURNAL   J Dermatol 44 (6), 671-680 (2017)
   PUBMED   28105694
  REMARK    GeneRIF: In 22 melanoma patients with stage III lymph node
            metastasis, overall survival was significantly higher in the
            XAGE-1b and NY-ESO-1 double-negative group than in the other
            groups.
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Sato,S., Noguchi,Y., Ohara,N., Uenaka,A., Shimono,M., Nakagawa,K.,
            Koizumi,F., Ishida,T., Yoshino,T., Shiratori,Y. and Nakayama,E.
  TITLE     Identification of XAGE-1 isoforms: predominant expression of
            XAGE-1b in testis and tumors
  JOURNAL   Cancer Immun 7, 5 (2007)
   PUBMED   17335148
  REMARK    GeneRIF: XAGE-1b is a promising target molecule for a cancer
            vaccine against lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Nakagawa,K., Noguchi,Y., Uenaka,A., Sato,S., Okumura,H., Tanaka,M.,
            Shimono,M., Ali Eldib,A.M., Ono,T., Ohara,N., Yoshino,T.,
            Yamashita,K., Tsunoda,T., Aoe,M., Shimizu,N. and Nakayama,E.
  TITLE     XAGE-1 expression in non-small cell lung cancer and antibody
            response in patients
  JOURNAL   Clin Cancer Res 11 (15), 5496-5503 (2005)
   PUBMED   16061866
  REMARK    GeneRIF: XAGE-1b is highly and strongly expressed in lung
            adenocarcinoma and immunogenic in patients
REFERENCE   6  (residues 1 to 69)
  AUTHORS   Zendman,A.J., Van Kraats,A.A., Weidle,U.H., Ruiter,D.J. and Van
            Muijen,G.N.
  TITLE     The XAGE family of cancer/testis-associated genes: alignment and
            expression profile in normal tissues, melanoma lesions and Ewing's
            sarcoma
  JOURNAL   Int J Cancer 99 (3), 361-369 (2002)
   PUBMED   11992404
  REMARK    GeneRIF: The XAGE family of cancer/testis-associated genes:
            alignment and expression profile in normal tissues, melanoma
            lesions and Ewing's sarcoma
REFERENCE   7  (residues 1 to 69)
  AUTHORS   Egland,K.A., Kumar,V., Duray,P. and Pastan,I.
  TITLE     Characterization of overlapping XAGE-1 transcripts encoding a
            cancer testis antigen expressed in lung, breast, and other types of
            cancers
  JOURNAL   Mol Cancer Ther 1 (7), 441-450 (2002)
   PUBMED   12479262
  REMARK    GeneRIF: transcription of the XAGE-1 gene is initiated from two
            distinct start sites, resulting in two overlapping transcripts,
            XAGE-1a and XAGE-1b; XAGE-1 is expressed in a diverse range of
            cancers
REFERENCE   8  (residues 1 to 69)
  AUTHORS   Zendman,A.J., van Kraats,A.A., den Hollander,A.I., Weidle,U.H.,
            Ruiter,D.J. and van Muijen,G.N.
  TITLE     Characterization of XAGE-1b, a short major transcript of
            cancer/testis-associated gene XAGE-1, induced in melanoma
            metastasis
  JOURNAL   Int J Cancer 97 (2), 195-204 (2002)
   PUBMED   11774264
REFERENCE   9  (residues 1 to 69)
  AUTHORS   Liu,X.F., Helman,L.J., Yeung,C., Bera,T.K., Lee,B. and Pastan,I.
  TITLE     XAGE-1, a new gene that is frequently expressed in Ewing's sarcoma
  JOURNAL   Cancer Res 60 (17), 4752-4755 (2000)
   PUBMED   10987281
REFERENCE   10 (residues 1 to 69)
  AUTHORS   Brinkmann,U., Vasmatzis,G., Lee,B. and Pastan,I.
  TITLE     Novel genes in the PAGE and GAGE family of tumor antigens found by
            homology walking in the dbEST database
  JOURNAL   Cancer Res 59 (7), 1445-1448 (1999)
   PUBMED   10197611
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX510359.5.
            
            Summary: This gene is a member of the XAGE subfamily, which belongs
            to the GAGE family. The GAGE genes are expressed in a variety of
            tumors and in some fetal and reproductive tissues. This gene is
            strongly expressed in Ewing's sarcoma, alveolar rhabdomyosarcoma
            and normal testis. The protein encoded by this gene contains a
            nuclear localization signal and shares a sequence similarity with
            other GAGE/PAGE proteins. Because of the expression pattern and the
            sequence similarity, this protein also belongs to a family of CT
            (cancer-testis) antigens. Alternative splicing of this gene, in
            addition to alternative transcription start sites, results in
            multiple transcript variants. [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (d, also known as XAGE-1d) starts
            at a downstream transcription start site, and uses an alternate
            splice site in an internal exon that causes a frameshift in the 3'
            coding region, compared to variant a. The encoded isoform (d) has a
            distinct and shorter C-terminus, compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..69
                     /product="X antigen family member 1 isoform d"
                     /note="cancer/testis associated protein; cancer/testis
                     antigen family 12, member 1e; G antigen family D member 2;
                     protein XAGE-1; cancer/testis antigen 12.1; X antigen
                     family, member 1C; X antigen family, member 1D;
                     cancer/testis antigen family 12, member 1d; cancer/testis
                     antigen family 12, member 1c; X antigen family member 1E;
                     cancer/testis antigen family 12, member 1b"
                     /calculated_mol_wt=7834
     CDS             1..69
                     /gene="XAGE1B"
                     /gene_synonym="CT12.1; CT12.1b; CT12.1C; CT12.1D; CT12.1E;
                     CTP9; GAGED2; XAGE-1; XAGE1; XAGE1C; XAGE1D; XAGE1E"
                     /coded_by="NM_001097605.2:136..345"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS48128.1"
                     /db_xref="GeneID:653067"
                     /db_xref="HGNC:HGNC:25400"
                     /db_xref="MIM:300289"
ORIGIN      
        1 mespkkknqq lkvgilhlgs rqkkiriqlr sqvlgremrd megdlqelhq sntgdksgfg
       61 frrqgednt
//
LOCUS       NP_003128                655 aa            linear   PRI 20-NOV-2025
DEFINITION  SRSF protein kinase 1 [Homo sapiens].
ACCESSION   NP_003128
VERSION     NP_003128.3
DBSOURCE    REFSEQ: accession NM_003137.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Wang,J.J., Roy,S.K. and Xu,Y.M.
  TITLE     Spatiotemporal expression and coexpression patterns of SRPK1 in the
            human brain: A neurodevelopmental perspective
  JOURNAL   Brain Behav 14 (1), e3341 (2024)
   PUBMED   38376036
  REMARK    GeneRIF: Spatiotemporal expression and coexpression patterns of
            SRPK1 in the human brain: A neurodevelopmental perspective.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Huang,J.Q., Duan,L.X., Liu,Q.Y., Li,H.F., Hu,A.P., Song,J.W.,
            Lin,C., Huang,B., Yao,D., Peng,B., Sun,Y., Wen,Y., Yang,L., Xu,X.
            and Gong,L.Y.
  TITLE     Serine-arginine protein kinase 1 (SRPK1) promotes EGFR-TKI
            resistance by enhancing GSK3beta Ser9 autophosphorylation
            independent of its kinase activity in non-small-cell lung cancer
  JOURNAL   Oncogene 42 (15), 1233-1246 (2023)
   PUBMED   36869126
  REMARK    GeneRIF: Serine-arginine protein kinase 1 (SRPK1) promotes EGFR-TKI
            resistance by enhancing GSK3beta Ser9 autophosphorylation
            independent of its kinase activity in non-small-cell lung cancer.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Guo,W. and Hu,Z.
  TITLE     SRPK1 promotes sepsis-induced acute lung injury via regulating
            PI3K/AKT/FOXO3 signaling
  JOURNAL   Immunopharmacol Immunotoxicol 45 (2), 203-212 (2023)
   PUBMED   36226860
  REMARK    GeneRIF: SRPK1 promotes sepsis-induced acute lung injury via
            regulating PI3K/AKT/FOXO3 signaling.
REFERENCE   5  (residues 1 to 655)
  AUTHORS   He,C., Liu,B., Wang,H.Y., Wu,L., Zhao,G., Huang,C., Liu,Y., Shan,B.
            and Liu,L.
  TITLE     Inhibition of SRPK1, a key splicing regulator, exhibits antitumor
            and chemotherapeutic-sensitizing effects on extranodal NK/T-cell
            lymphoma cells
  JOURNAL   BMC Cancer 22 (1), 1100 (2022)
   PUBMED   36303126
  REMARK    GeneRIF: Inhibition of SRPK1, a key splicing regulator, exhibits
            antitumor and chemotherapeutic-sensitizing effects on extranodal
            NK/T-cell lymphoma cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Papoutsopoulou,S., Nikolakaki,E. and Giannakouros,T.
  TITLE     SRPK1 and LBR protein kinases show identical substrate
            specificities
  JOURNAL   Biochem Biophys Res Commun 255 (3), 602-607 (1999)
   PUBMED   10049757
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Tronchere,H., Wang,J. and Fu,X.D.
  TITLE     A protein related to splicing factor U2AF35 that interacts with
            U2AF65 and SR proteins in splicing of pre-mRNA
  JOURNAL   Nature 388 (6640), 397-400 (1997)
   PUBMED   9237760
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Colwill,K., Feng,L.L., Yeakley,J.M., Gish,G.D., Caceres,J.F.,
            Pawson,T. and Fu,X.D.
  TITLE     SRPK1 and Clk/Sty protein kinases show distinct substrate
            specificities for serine/arginine-rich splicing factors
  JOURNAL   J Biol Chem 271 (40), 24569-24575 (1996)
   PUBMED   8798720
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC038292.1, AK299591.1,
            Z99128.1 and BX648697.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 17, 2004 this sequence version replaced NP_003128.2.
            
            Summary: This gene encodes a serine/arginine protein kinase
            specific for the SR (serine/arginine-rich domain) family of
            splicing factors. The protein localizes to the nucleus and the
            cytoplasm. It is thought to play a role in regulation of both
            constitutive and alternative splicing by regulating intracellular
            localization of splicing factors. Alternative splicing of this gene
            results in multiple transcript variants. Additional alternatively
            spliced transcript variants have been described for this gene, but
            their full length nature have not been determined.[provided by
            RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.85279.1,
                                           SRR1803613.123013.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373825.7/ ENSP00000362931.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..655
                     /product="SRSF protein kinase 1"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 1; serine/arginine-rich
                     splicing factor kinase 1; serine/threonine-protein kinase
                     SRPK1; SR-protein-specific kinase 1"
                     /calculated_mol_wt=74194
     Region          69..>282
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(86..89,92,94,107,109,145,165..168,213,217..218,220)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271118"
     Region          <477..653
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..655
                     /gene="SRPK1"
                     /gene_synonym="SFRSK1"
                     /coded_by="NM_003137.5:43..2010"
                     /db_xref="CCDS:CCDS47415.1"
                     /db_xref="GeneID:6732"
                     /db_xref="HGNC:HGNC:11305"
                     /db_xref="MIM:601939"
ORIGIN      
        1 merkvlalqa rkkrtkakkd kaqrksetqh rgsaphsesd lpeqeeeilg sdddeqedpn
       61 dyckggyhlv kigdlfngry hvirklgwgh fstvwlswdi qgkkfvamkv vksaehytet
      121 aldeirllks vrnsdpndpn remvvqlldd fkisgvngth icmvfevlgh hllkwiiksn
      181 yqglplpcvk kiiqqvlqgl dylhtkcrii htdikpenil lsvneqyirr laaeatewqr
      241 sgapppsgsa vstapqpkpa dkmsknkkkk lkkkqkrqae llekrmqeie emekesgpgq
      301 krpnkqeese spverplken ppnkmtqekl eesstigqdq tlmerdtegg aaeincngvi
      361 evinytqnsn netlrhkedl hnandcdvqn lnqessflss qngdsstsqe tdsctpitse
      421 vsdtmvcqss stvgqsfseq hisqlqesir aeipcedeqe qehngpldnk gkstagnflv
      481 nplepknaek lkvkiadlgn acwvhkhfte diqtrqyrsl evligsgynt padiwstacm
      541 afelatgdyl fephsgeeyt rdedhialii ellgkvprkl ivagkyskef ftkkgdlkhi
      601 tklkpwglfe vlvekyewsq eeaagftdfl lpmlelipek rataaeclrh pwlns
//
LOCUS       NP_001350126             456 aa            linear   PRI 20-NOV-2025
DEFINITION  glycerol-3-phosphate acyltransferase 4 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001350126 XP_011542695
VERSION     NP_001350126.1
DBSOURCE    REFSEQ: accession NM_001363197.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Chang,C.L., Weigel,A.V., Ioannou,M.S., Pasolli,H.A., Xu,C.S.,
            Peale,D.R., Shtengel,G., Freeman,M., Hess,H.F., Blackstone,C. and
            Lippincott-Schwartz,J.
  TITLE     Spastin tethers lipid droplets to peroxisomes and directs fatty
            acid trafficking through ESCRT-III
  JOURNAL   J Cell Biol 218 (8), 2583-2599 (2019)
   PUBMED   31227594
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Zhu,X.G., Nicholson Puthenveedu,S., Shen,Y., La,K., Ozlu,C.,
            Wang,T., Klompstra,D., Gultekin,Y., Chi,J., Fidelin,J., Peng,T.,
            Molina,H., Hang,H.C., Min,W. and Birsoy,K.
  TITLE     CHP1 Regulates Compartmentalized Glycerolipid Synthesis by
            Activating GPAT4
  JOURNAL   Mol Cell 74 (1), 45-58 (2019)
   PUBMED   30846317
  REMARK    GeneRIF: GPAT4 activity requires CHP1 to be N-myristoylated,
            forming a key molecular interface between the two proteins,
            regulating glycerolipid metabolism.
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Cooper,D.E., Grevengoed,T.J., Klett,E.L. and Coleman,R.A.
  TITLE     Glycerol-3-phosphate Acyltransferase Isoform-4 (GPAT4) Limits
            Oxidation of Exogenous Fatty Acids in Brown Adipocytes
  JOURNAL   J Biol Chem 290 (24), 15112-15120 (2015)
   PUBMED   25918168
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Chen,Y.Q., Kuo,M.S., Li,S., Bui,H.H., Peake,D.A., Sanders,P.E.,
            Thibodeaux,S.J., Chu,S., Qian,Y.W., Zhao,Y., Bredt,D.S.,
            Moller,D.E., Konrad,R.J., Beigneux,A.P., Young,S.G. and Cao,G.
  TITLE     AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase
  JOURNAL   J Biol Chem 283 (15), 10048-10057 (2008)
   PUBMED   18238778
  REMARK    GeneRIF: AGPAT6 is a microsomal GPAT, and we propose renaming this
            enzyme GPAT4.
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Tan,X.J., Huang,Z.P., Li,L.Y., Nie,D.S., Zhong,C.G., Fu,J.J. and
            Lu,G.X.
  TITLE     Molecular cloning and preliminary function study of a novel human
            gene, TSARG7, related to spermatogenesis
  JOURNAL   Yi Chuan Xue Bao 33 (4), 294-303 (2006)
   PUBMED   16625827
  REMARK    GeneRIF: we have cloned a novel human gene and this gene may play
            an important role in human spermatogenesis and sexual maturation.
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Li,D., Yu,L., Wu,H., Shan,Y., Guo,J., Dang,Y., Wei,Y. and Zhao,S.
  TITLE     Cloning and identification of the human LPAAT-zeta gene, a novel
            member of the lysophosphatidic acid acyltransferase family
  JOURNAL   J Hum Genet 48 (8), 438-442 (2003)
   PUBMED   12938015
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Lehner,R. and Kuksis,A.
  TITLE     Biosynthesis of triacylglycerols
  JOURNAL   Prog Lipid Res 35 (2), 169-201 (1996)
   PUBMED   8944226
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB479618.1, AF406612.1, BU149203.1, AC009630.14 and BU620295.1.
            
            On May 11, 2018 this sequence version replaced XP_011542695.1.
            
            Summary: Lysophosphatidic acid acyltransferases (EC 2.3.1.51)
            catalyze the conversion of lysophosphatidic acid (LPA) to
            phosphatidic acid (PA). LPA and PA are involved in signal
            transduction and lipid biosynthesis.[supplied by OMIM, Apr 2004].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.189460.1,
                                           SRR1803613.31437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..456
                     /product="glycerol-3-phosphate acyltransferase 4 isoform 1
                     precursor"
                     /EC_number="2.3.1.15"
                     /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
                     zeta; 1-AGP acyltransferase 6; glycerol-3-phosphate
                     acyltransferase 6; testis spermatogenesis
                     apoptosis-related protein 7; lysophosphatidic acid
                     acyltransferase zeta; 1-acylglycerol-3-phosphate
                     O-acyltransferase 6 (lysophosphatidic acid
                     acyltransferase, zeta)"
                     /calculated_mol_wt=48012
     sig_peptide     1..37
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UL3.1)"
                     /calculated_mol_wt=4077
     mat_peptide     38..456
                     /product="Glycerol-3-phosphate acyltransferase 4.
                     /id=PRO_0000024703"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL3.1)"
                     /calculated_mol_wt=48012
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL3.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL3.1)"
     Region          218..427
                     /region_name="LPLAT_LPCAT1-like"
                     /note="Lysophospholipid Acyltransferases (LPLATs) of
                     Glycerophospholipid Biosynthesis: LPCAT1-like; cd07991"
                     /db_xref="CDD:153253"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UL3.1)"
     Site            order(248,251,253,267..270,323..325)
                     /site_type="active"
                     /note="putative acyl-acceptor binding pocket [active]"
                     /db_xref="CDD:153253"
     Region          248..253
                     /region_name="HXXXXD motif.
                     /evidence=ECO:0000250|UniProtKB:Q9D517"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL3.1)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UL3.1)"
     Site            328
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UL3.1)"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UL3.1)"
     CDS             1..456
                     /gene="GPAT4"
                     /gene_synonym="1-AGPAT 6; AGPAT6; LPAAT-zeta; LPAATZ;
                     TSARG7"
                     /coded_by="NM_001363197.2:914..2284"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS6117.1"
                     /db_xref="GeneID:137964"
                     /db_xref="HGNC:HGNC:20880"
                     /db_xref="MIM:608143"
ORIGIN      
        1 mflllpfdsl ivnllgislt vlftlllvfi ivpaifgvsf girklymksl lkifawatlr
       61 mergakeknh qlykpytngi iakdptslee eikeirrsgs skaldntpef elsdifyfcr
      121 kgmetimdde vtkrfsaeel eswnllsrtn ynfqyislrl tvlwglgvli rycfllplri
      181 alaftgisll vvgttvvgyl pngrfkefms khvhlmcyri cvraltaiit yhdrenrprn
      241 ggicvanhts pidviilasd gyyamvgqvh gglmgviqra mvkacphvwf ersevkdrhl
      301 vakrltehvq dksklpilif pegtcinnts vmmfkkgsfe igatvypvai kydpqfgdaf
      361 wnsskygmvt yllrmmtswa ivcsvwylpp mtreadedav qfanrvksai arqgglvdll
      421 wdgglkrekv kdtfkeeqqk lyskmivgnh kdrsrs
//
LOCUS       NP_005969                 98 aa            linear   PRI 20-NOV-2025
DEFINITION  protein S100-A2 isoform 1 [Homo sapiens].
ACCESSION   NP_005969
VERSION     NP_005969.2
DBSOURCE    REFSEQ: accession NM_005978.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Zeng,T., Ren,W., Zeng,H., Wang,D., Wu,X. and Xu,G.
  TITLE     TFAP2A Activates S100A2 to Mediate Glutamine Metabolism and Promote
            Lung Adenocarcinoma Metastasis
  JOURNAL   Clin Respir J 18 (8), e13825 (2024)
   PUBMED   39187936
  REMARK    GeneRIF: TFAP2A Activates S100A2 to Mediate Glutamine Metabolism
            and Promote Lung Adenocarcinoma Metastasis.
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Yang,J., Wan,S., Zhao,M., Cai,H., Gao,Y. and Wang,H.
  TITLE     Multi-omics Analysis Identifies Hypoxia Subtypes and S100A2 as an
            Immunosuppressive Factor in Cervical Cancer
  JOURNAL   Reprod Sci 31 (1), 107-121 (2024)
   PUBMED   37648942
  REMARK    GeneRIF: Multi-omics Analysis Identifies Hypoxia Subtypes and
            S100A2 as an Immunosuppressive Factor in Cervical Cancer.
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Zhang,J., Wang,Z., Liang,Z., Jin,C., Shi,Y., Fan,M., Hu,X. and
            Wan,Y.
  TITLE     NFIC1 inhibits the migration and invasion of MDA-MB-231 cells
            through S100A2-mediated inactivation of MEK/ERK pathway
  JOURNAL   Arch Biochem Biophys 734, 109497 (2023)
   PUBMED   36574914
  REMARK    GeneRIF: NFIC1 inhibits the migration and invasion of MDA-MB-231
            cells through S100A2-mediated inactivation of MEK/ERK pathway.
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Yan,J., Huang,Y.J., Huang,Q.Y., Liu,P.X. and Wang,C.S.
  TITLE     Transcriptional activation of S100A2 expression by HIF-1alpha via
            binding to the hypomethylated hypoxia response elements in HCC
            cells
  JOURNAL   Mol Carcinog 61 (5), 494-507 (2022)
   PUBMED   35107180
  REMARK    GeneRIF: Transcriptional activation of S100A2 expression by
            HIF-1alpha via binding to the hypomethylated hypoxia response
            elements in HCC cells.
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Schafer,B.W. and Heizmann,C.W.
  TITLE     The S100 family of EF-hand calcium-binding proteins: functions and
            pathology
  JOURNAL   Trends Biochem Sci 21 (4), 134-140 (1996)
   PUBMED   8701470
  REMARK    Review article
REFERENCE   7  (residues 1 to 98)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
   PUBMED   7759097
REFERENCE   8  (residues 1 to 98)
  AUTHORS   Engelkamp,D., Schafer,B.W., Mattei,M.G., Erne,P. and Heizmann,C.W.
  TITLE     Six S100 genes are clustered on human chromosome 1q21:
            identification of two genes coding for the two previously
            unreported calcium-binding proteins S100D and S100E
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6547-6551 (1993)
   PUBMED   8341667
REFERENCE   9  (residues 1 to 98)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 98)
  AUTHORS   Lee,S.W., Tomasetto,C., Swisshelm,K., Keyomarsi,K. and Sager,R.
  TITLE     Down-regulation of a member of the S100 gene family in mammary
            carcinoma cells and reexpression by azadeoxycytidine treatment
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2504-2508 (1992)
   PUBMED   1372446
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX470102.12.
            
            On Oct 4, 2018 this sequence version replaced NP_005969.1.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may have a
            tumor suppressor function. Chromosomal rearrangements and altered
            expression of this gene have been implicated in breast cancer.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM557967.1, ERR279848.6495.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368708.9/ ENSP00000357697.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..98
                     /product="protein S100-A2 isoform 1"
                     /note="protein S100-A2"
                     /calculated_mol_wt=10986
     Region          4..91
                     /region_name="S-100"
                     /note="S-100 domain, which represents the largest family
                     within the superfamily of proteins carrying the Ca-binding
                     EF-hand motif. Note that this S-100 hierarchy contains
                     only S-100 EF-hand domains, other EF-hands have been
                     modeled separately. S100 proteins are...; cd00213"
                     /db_xref="CDD:238131"
     Site            order(4..21,27..29,38..39,41..43,71..74,76..77,79..82,
                     84..91)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238131"
     Site            order(21,26,29,34..35,64,66,68,70,72,75)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238131"
     CDS             1..98
                     /gene="S100A2"
                     /gene_synonym="CAN19; S100L"
                     /coded_by="NM_005978.4:350..646"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1044.2"
                     /db_xref="GeneID:6273"
                     /db_xref="HGNC:HGNC:10492"
                     /db_xref="MIM:176993"
ORIGIN      
        1 mmcssleqal avlvttfhky scqegdkfkl skgemkellh kelpsfvgek vdeeglkklm
       61 gsldensdqq vdfqeyavfl alitvmcndf fqgcpdrp
//
LOCUS       NP_060823               1132 aa            linear   PRI 20-NOV-2025
DEFINITION  mis18-binding protein 1 [Homo sapiens].
ACCESSION   NP_060823
VERSION     NP_060823.3
DBSOURCE    REFSEQ: accession NM_018353.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1132)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1132)
  AUTHORS   Thamkachy,R., Medina-Pritchard,B., Park,S.H., Chiodi,C.G., Zou,J.,
            de la Torre-Barranco,M., Shimanaka,K., Abad,M.A., Gallego
            Paramo,C., Feederle,R., Ruksenaite,E., Heun,P., Davies,O.R.,
            Rappsilber,J., Schneidman-Duhovny,D., Cho,U.S. and Jeyaprakash,A.A.
  TITLE     Structural basis for Mis18 complex assembly and its implications
            for centromere maintenance
  JOURNAL   EMBO Rep 25 (8), 3348-3372 (2024)
   PUBMED   38951710
REFERENCE   3  (residues 1 to 1132)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1132)
  AUTHORS   Cuijpers,S.A.G., Willemstein,E. and Vertegaal,A.C.O.
  TITLE     Converging Small Ubiquitin-like Modifier (SUMO) and Ubiquitin
            Signaling: Improved Methodology Identifies Co-modified Target
            Proteins
  JOURNAL   Mol Cell Proteomics 16 (12), 2281-2295 (2017)
   PUBMED   28951443
  REMARK    GeneRIF: Results confirm the regulation of MIS18BP1 via
            SUMO-ubiquitin crosstalk during mitosis.
REFERENCE   5  (residues 1 to 1132)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 1132)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 1132)
  AUTHORS   Maddox,P.S., Hyndman,F., Monen,J., Oegema,K. and Desai,A.
  TITLE     Functional genomics identifies a Myb domain-containing protein
            family required for assembly of CENP-A chromatin
  JOURNAL   J Cell Biol 176 (6), 757-763 (2007)
   PUBMED   17339379
REFERENCE   8  (residues 1 to 1132)
  AUTHORS   Fujita,Y., Hayashi,T., Kiyomitsu,T., Toyoda,Y., Kokubu,A., Obuse,C.
            and Yanagida,M.
  TITLE     Priming of centromere for CENP-A recruitment by human hMis18alpha,
            hMis18beta, and M18BP1
  JOURNAL   Dev Cell 12 (1), 17-30 (2007)
   PUBMED   17199038
  REMARK    GeneRIF: Three human proteins essential for centromere/kinetochore
            structure and function, hMis18alpha, hMis18beta, and M18BP1, the
            complex of which is accumulated specifically at the telophase-G1
            centromere, are identified.[Mis18alpha, Mis18beta, M18BP1]
REFERENCE   9  (residues 1 to 1132)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 1132)
  AUTHORS   Gunther,M., Laithier,M. and Brison,O.
  TITLE     A set of proteins interacting with transcription factor Sp1
            identified in a two-hybrid screening
  JOURNAL   Mol Cell Biochem 210 (1-2), 131-142 (2000)
   PUBMED   10976766
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB067490.1, BC065544.1 and AW971491.1.
            
            On Feb 6, 2004 this sequence version replaced NP_060823.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065544.1, SRR1660805.98110.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310806.9/ ENSP00000309790.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.2"
     Protein         1..1132
                     /product="mis18-binding protein 1"
                     /note="putative protein p243 which interacts with
                     transcription factor Sp1; kinetochore null 2 homolog;
                     kinetochore-associated protein KNL-2 homolog; P243;
                     hsKNL-2"
                     /calculated_mol_wt=128955
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          123..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          306..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          383..470
                     /region_name="SANTA"
                     /note="SANTA (SANT Associated); pfam09133"
                     /db_xref="CDD:462689"
     Region          482..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          765..798
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Region          879..925
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(880,913..914,916..917,919..921,923..925)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          923..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1086
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1087
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P0N0.1)"
     CDS             1..1132
                     /gene="MIS18BP1"
                     /gene_synonym="C14orf106; HSA242977; KNL2; M18BP1"
                     /coded_by="NM_018353.5:260..3658"
                     /db_xref="CCDS:CCDS9684.1"
                     /db_xref="GeneID:55320"
                     /db_xref="HGNC:HGNC:20190"
                     /db_xref="MIM:618139"
ORIGIN      
        1 miatplkhsr iylppeassq rrnlpmdaif fdsipsgtlt pvkdlvkyqn sslklndhkk
       61 nqflkmttfn nknifqstml teattsnssl disaikpnkd glknkanyes pgkiflrmke
      121 kvlrdkqeqp srnssllepq ksgnnetftp nrvekkklqh tylceekenn ksfqsddssl
      181 rasvqgvple ssnndiflpv kqkiqcqqek kaplhnltye lptlnqeqen flavearnkt
      241 ltraqlakqi fhskesivat tkskkdtfvl esvdsadeqf qntnaetlst ncipikngsl
      301 lmvsdsertt egtsqqkvke gngktvpget glpgsmkdtc kivlatprlh itiprrskrn
      361 isklspprif qtvtnglkkn qvvqlqewmi ksinnntaic vegklidvtn iywhsnviie
      421 riehnklrti sgnvyilkgm idqismkeag ypnylirkfm fgfpenwkeh idnfleqlra
      481 geknrektkq kqktgrsvrd irksmkndar enqtdtaqra tttydfdcdn lelksnkhse
      541 spgatelnmc hsncqnkptl rfpddqvnnt iqngggddls nqeligkkey kmsskklkig
      601 ertneriiks qkqetteeld vsidiltsre qffsdeerky mainqkkayi lvtplksrkv
      661 ieqrcmrynl sagtikavtd fvipecqkks pisksmgtle ntfeghkskn kedcderdll
      721 tvnrkikisn lekeqmltsd fkkntrllpk lkkienqvam sfykhqsspd lsseesetek
      781 eikrkaevkk tkagntkeav vhlrkstrnt snipvilepe teesenefyi kqkkarpsvk
      841 etlqksgvrk efpiteavgs dktnrhplec lpgliqdkew nekelqklhc afaslpkhkp
      901 gfwsevaaav gsrspeecqr kymenprgkg sqkhvtkkkp anskgqngkr gdadqkqtik
      961 itakvgtlkr kqqmrefleq lpkddhddff sttplqhqri llpsfqdsed dddilpnmdk
     1021 npttpssvif plvktpqcqh vspgmlgsin rndcdkyvfr mqkyhksngg ivwgnikkkl
     1081 vetdfstptp rrktpfntdl gensgigklf tnavesldee ekdyyfsnsd sa
//
LOCUS       NP_387506                398 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein mS29 isoform 1 [Homo sapiens].
ACCESSION   NP_387506
VERSION     NP_387506.1
DBSOURCE    REFSEQ: accession NM_033657.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Smith,T.B., Kopajtich,R., Demain,L.A.M., Rea,A., Thomas,H.B.,
            Schiff,M., Beetz,C., Joss,S., Conway,G.S., Shukla,A., Yeole,M.,
            Radhakrishnan,P., Azzouz,H., Ben Chehida,A., Elmaleh-Berges,M.,
            Glasgow,R.I.C., Thompson,K., Olahova,M., He,L., Jenkinson,E.M.,
            Jahic,A., Belyantseva,I.A., Barzik,M., Urquhart,J.E.,
            O'Sullivan,J., Williams,S.G., Bhaskar,S.S., Carrera,S.,
            Blakes,A.J.M., Banka,S., Yue,W.W., Ellingford,J.M., Houlden,H.,
            Munro,K.J., Friedman,T.B., Taylor,R.W., Prokisch,H., O'Keefe,R.T.
            and Newman,W.G.
  CONSRTM   DDD Study
  TITLE     Bi-allelic variants in DAP3 result in reduced assembly of the
            mitoribosomal small subunit with altered apoptosis and a
            Perrault-syndrome-spectrum phenotype
  JOURNAL   Am J Hum Genet 112 (1), 59-74 (2025)
   PUBMED   39701103
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Tan,S., Zhang,X., Guo,X., Pan,G., Yan,L., Ding,Z., Li,R., Wang,D.,
            Yan,Y., Dong,Z. and Li,T.
  TITLE     DAP3 promotes mitochondrial activity and tumour progression in
            hepatocellular carcinoma by regulating MT-ND5 expression
  JOURNAL   Cell Death Dis 15 (7), 540 (2024)
   PUBMED   39080251
  REMARK    GeneRIF: DAP3 promotes mitochondrial activity and tumour
            progression in hepatocellular carcinoma by regulating MT-ND5
            expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Sui,L., Zeng,J., Zhao,H., Ye,L., Martin,T.A., Sanders,A.J.,
            Ruge,F., Jiang,A., Dou,Q.P., Hargest,R., Song,X. and Jiang,W.G.
  TITLE     Death associated protein-3 (DAP3) and DAP3 binding cell death
            enhancer-1 (DELE1) in human colorectal cancer, and their impacts on
            clinical outcome and chemoresistance
  JOURNAL   Int J Oncol 62 (1) (2023)
   PUBMED   36382667
  REMARK    GeneRIF: Death associated protein3 (DAP3) and DAP3 binding cell
            death enhancer1 (DELE1) in human colorectal cancer, and their
            impacts on clinical outcome and chemoresistance.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Han,M.J., Chiu,D.T. and Koc,E.C.
  TITLE     Regulation of mitochondrial ribosomal protein S29 (MRPS29)
            expression by a 5'-upstream open reading frame
  JOURNAL   Mitochondrion 10 (3), 274-283 (2010)
   PUBMED   20079882
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Morgan,C.J., Jacques,C., Savagner,F., Tourmen,Y., Mirebeau,D.P.,
            Malthiery,Y. and Reynier,P.
  TITLE     A conserved N-terminal sequence targets human DAP3 to mitochondria
  JOURNAL   Biochem Biophys Res Commun 280 (1), 177-181 (2001)
   PUBMED   11162496
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Hulkko,S.M., Wakui,H. and Zilliacus,J.
  TITLE     The pro-apoptotic protein death-associated protein 3 (DAP3)
            interacts with the glucocorticoid receptor and affects the receptor
            function
  JOURNAL   Biochem J 349 Pt 3 (Pt 3), 885-893 (2000)
   PUBMED   10903152
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Kissil,J.L. and Kimchi,A.
  TITLE     Assignment of death associated protein 3 (DAP3) to human chromosome
            1q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 252 (1997)
   PUBMED   9284927
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Kissil,J.L., Deiss,L.P., Bayewitch,M., Raveh,T., Khaspekov,G. and
            Kimchi,A.
  TITLE     Isolation of DAP3, a novel mediator of interferon-gamma-induced
            cell death
  JOURNAL   J Biol Chem 270 (46), 27932-27936 (1995)
   PUBMED   7499268
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC107488.1, AL162734.15 and
            BQ183744.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 28S subunit protein that also
            participates in apoptotic pathways which are initiated by tumor
            necrosis factor-alpha, Fas ligand, and gamma interferon. This
            protein potentially binds ATP/GTP and might be a functional partner
            of the mitoribosomal protein S27. Multiple alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. Pseudogenes corresponding to this gene are found on
            chromosomes 1q and 2q. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) has an additional segment in
            the 5' UTR, as compared to variant 2. Variants 1, 2 and 3 encode
            the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.165957.1,
                                           SRR1803614.277959.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            regulatory uORF                    :: PMID: 20079882
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..398
                     /product="small ribosomal subunit protein mS29 isoform 1"
                     /note="mitochondrial 28S ribosomal protein S29; 28S
                     ribosomal protein S29, mitochondrial; ionizing radiation
                     resistance conferring protein; mitochondrial small
                     ribosomal subunit protein mS29"
                     /calculated_mol_wt=43102
     transit_peptide 1..21
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P51398.1)"
                     /calculated_mol_wt=2483
     mat_peptide     22..398
                     /product="Small ribosomal subunit protein mS29.
                     /id=PRO_0000087717"
                     /note="propagated from UniProtKB/Swiss-Prot (P51398.1)"
                     /calculated_mol_wt=43102
     Region          39..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51398.1)"
     Region          99..393
                     /region_name="DAP3"
                     /note="Mitochondrial ribosomal death-associated protein 3;
                     pfam10236"
                     /db_xref="CDD:431160"
     Site            175
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51398.1)"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51398.1)"
     CDS             1..398
                     /gene="DAP3"
                     /gene_synonym="bMRP-10; DAP-3; MRP-S29; MRPS29; mS29;
                     PRLTS7; S29mt"
                     /coded_by="NM_033657.2:158..1354"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1120.1"
                     /db_xref="GeneID:7818"
                     /db_xref="HGNC:HGNC:2673"
                     /db_xref="MIM:602074"
ORIGIN      
        1 mmlkgitrli srihkldpgr flhmgtqarq siaahldnqv pvespraisr tnendpakhg
       61 dqhegqhyni spqdletvfp hglpprfvmq vktfseaclm vrkpalellh ylkntsfayp
      121 airyllygek gtgktlslch vihfcakqdw lilhipdahl wvkncrdllq ssynkqrfdq
      181 pleastwlkn fkttnerfln qikvqekyvw nkrestekgs plgevveqgi trvrnatdav
      241 givlkelkrq sslgmfhllv avdginalwg rttlkredks piapeelalv hnlrkmmknd
      301 whggaivsal sqtgslfkpr kaylpqellg kegfdaldpf ipilvsnynp kefesciqyy
      361 lennwlqhek apteegkkel lflsnanpsl lerhcayl
//
LOCUS       NP_001308508             512 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 19 [Homo sapiens].
ACCESSION   NP_001308508 XP_005263315
VERSION     NP_001308508.1
DBSOURCE    REFSEQ: accession NM_001321579.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 512)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Mar 26, 2016 this sequence version replaced XP_005263315.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.131449.1,
                                           SRR1660807.155071.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..512
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 19"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57631
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..512
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321579.2:671..2209"
                     /note="isoform 19 is encoded by transcript variant 20"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalsks nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt
      481 mqseetrvwh rrdgkwqnvh fhrsgsptvp ik
//
LOCUS       NP_001309391             274 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3 domain-binding protein 5-like isoform 2 [Homo sapiens].
ACCESSION   NP_001309391
VERSION     NP_001309391.1
DBSOURCE    REFSEQ: accession NM_001322462.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Jenkins,M.L., Margaria,J.P., Stariha,J.T.B., Hoffmann,R.M.,
            McPhail,J.A., Hamelin,D.J., Boulanger,M.J., Hirsch,E. and
            Burke,J.E.
  TITLE     Structural determinants of Rab11 activation by the guanine
            nucleotide exchange factor SH3BP5
  JOURNAL   Nat Commun 9 (1), 3772 (2018)
   PUBMED   30217979
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK125837.1, AL732583.5 and BC010871.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK125837.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..274
                     /product="SH3 domain-binding protein 5-like isoform 2"
                     /note="SH3 domain-binding protein 5-like; SH3BP-5-like"
                     /calculated_mol_wt=29992
     Region          <7..164
                     /region_name="SH3BP5"
                     /note="SH3 domain-binding protein 5 (SH3BP5); pfam05276"
                     /db_xref="CDD:461608"
     CDS             1..274
                     /gene="SH3BP5L"
                     /coded_by="NM_001322462.1:1581..2405"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:80851"
                     /db_xref="HGNC:HGNC:29360"
                     /db_xref="MIM:620652"
ORIGIN      
        1 mkptllaqqe tqkaalryer avsmhnaare mvfvaeqgvm adknrldptw qemlnhatck
       61 vneaeeerlr gerehqrvtr lcqqaearvq alqktlrrai gksrpyfelk aqfsqileeh
      121 kakvteleqq vaqaktrysv alrnleqise qiharrrggl pphplgprrs spvgaeagpe
      181 dmedgdsgie gaegagleeg sslgpgpapd tdtlsllslr tvasdlqkcd svehlrglsd
      241 hvsldgqelg trsggrrgsd ggarggrhqr svsl
//
LOCUS       NP_057632                401 aa            linear   PRI 20-NOV-2025
DEFINITION  Golgi membrane protein 1 [Homo sapiens].
ACCESSION   NP_057632
VERSION     NP_057632.2
DBSOURCE    REFSEQ: accession NM_016548.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Lin,Y.F., Liao,L.Z., Wang,S.Y., Zhang,S.Z., Zhong,X.B., Zhou,H.M.,
            Xu,X.F., Xiong,Z.Y., Huang,Y.Q., Liu,M.H., Guo,Y., Liao,X.X. and
            Zhuang,X.D.
  TITLE     Causal Association of Golgi Protein 73 With Coronary Artery
            Disease: Evidence from Proteomics and Mendelian Randomization
  JOURNAL   Int J Med Sci 21 (11), 2127-2138 (2024)
   PUBMED   39239555
  REMARK    GeneRIF: Causal Association of Golgi Protein 73 With Coronary
            Artery Disease: Evidence from Proteomics and Mendelian
            Randomization.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Huang,F., Guo,J., Zhao,N., Hou,M., Gai,X., Yang,S., Cai,P.,
            Wang,Y., Ma,Q., Zhao,Q., Li,L., Yang,H., Jing,Y., Jin,D., Hu,Z.,
            Zha,X., Wang,H., Mao,Y., Liu,F. and Zhang,H.
  TITLE     PTEN deficiency potentiates HBV-associated liver cancer development
            through augmented GP73/GOLM1
  JOURNAL   J Transl Med 22 (1), 254 (2024)
   PUBMED   38459588
  REMARK    GeneRIF: PTEN deficiency potentiates HBV-associated liver cancer
            development through augmented GP73/GOLM1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Zhang,Z., Leng,X.K., Zhai,Y.Y., Zhang,X., Sun,Z.W., Xiao,J.Y.,
            Lu,J.F., Liu,K., Xia,B., Gao,Q., Jia,M., Xu,C.Q., Jiang,Y.N.,
            Zhang,X.G., Tao,K.S. and Wu,J.W.
  TITLE     Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress
  JOURNAL   Nat Commun 15 (1), 1908 (2024)
   PUBMED   38459023
  REMARK    GeneRIF: Deficiency of ASGR1 promotes liver injury by increasing
            GP73-mediated hepatic endoplasmic reticulum stress.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Liu,S., Ma,J., Chen,P., Liu,S., Guo,Y., Tan,M., Guo,X., Feng,Y.,
            Wang,Q., Li,W., Yang,C., Gao,B., Hua,Y., Liu,N., Song,H., He,R.,
            Wang,R., Gao,Q., Liu,C. and Qi,X.
  TITLE     Novel serum biomarker of Golgi protein 73 for the diagnosis of
            clinically significant portal hypertension in patients with
            compensated cirrhosis
  JOURNAL   J Med Virol 96 (1), e29380 (2024)
   PUBMED   38235849
  REMARK    GeneRIF: Novel serum biomarker of Golgi protein 73 for the
            diagnosis of clinically significant portal hypertension in patients
            with compensated cirrhosis.
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Kladney,R.D., Tollefson,A.E., Wold,W.S. and Fimmel,C.J.
  TITLE     Upregulation of the Golgi protein GP73 by adenovirus infection
            requires the E1A CtBP interaction domain
  JOURNAL   Virology 301 (2), 236-246 (2002)
   PUBMED   12359426
  REMARK    GeneRIF: GP73 as a novel adenovirus-induced cellular protein whose
            expression is regulated through the CID of the E1A protein
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Puri,S., Bachert,C., Fimmel,C.J. and Linstedt,A.D.
  TITLE     Cycling of early Golgi proteins via the cell surface and endosomes
            upon lumenal pH disruption
  JOURNAL   Traffic 3 (9), 641-653 (2002)
   PUBMED   12191016
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Bauer,K., Zemlin,M., Hummel,M., Pfeiffer,S., Karstaedt,J.,
            Steinhauser,G., Xiao,X., Versmold,H. and Berek,C.
  TITLE     Diversification of Ig heavy chain genes in human preterm neonates
            prematurely exposed to environmental antigens
  JOURNAL   J Immunol 169 (3), 1349-1356 (2002)
   PUBMED   12133958
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Kladney,R.D., Cui,X., Bulla,G.A., Brunt,E.M. and Fimmel,C.J.
  TITLE     Expression of GP73, a resident Golgi membrane protein, in viral and
            nonviral liver disease
  JOURNAL   Hepatology 35 (6), 1431-1440 (2002)
   PUBMED   12029628
  REMARK    GeneRIF: increased expression of GP73 in hepatocytes appears to be
            a general feature of advanced liver disease, and may be regulated
            via distinct pathways that involve hepatotropic viruses or
            cytokines.
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Kladney,R.D., Bulla,G.A., Guo,L., Mason,A.L., Tollefson,A.E.,
            Simon,D.J., Koutoubi,Z. and Fimmel,C.J.
  TITLE     GP73, a novel Golgi-localized protein upregulated by viral
            infection
  JOURNAL   Gene 249 (1-2), 53-65 (2000)
   PUBMED   10831838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL533767.3, AK027717.1 and
            BC001740.1.
            
            On Apr 4, 2003 this sequence version replaced NP_057632.1.
            
            Summary: The Golgi complex plays a key role in the sorting and
            modification of proteins exported from the endoplasmic reticulum.
            The protein encoded by this gene is a type II Golgi transmembrane
            protein. It processes proteins synthesized in the rough endoplasmic
            reticulum and assists in the transport of protein cargo through the
            Golgi apparatus. The expression of this gene has been observed to
            be upregulated in response to viral infection. Alternatively
            spliced transcript variants encoding the same protein have been
            described for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 2. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027717.1, BC001740.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388712.7/ ENSP00000373364.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..401
                     /product="Golgi membrane protein 1"
                     /note="golgi phosphoprotein 2; golgi membrane protein
                     GP73; golgi protein, 73-kD; epididymis luminal protein 46"
                     /calculated_mol_wt=45202
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826; propagated from
                     UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Site            13..35
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Region          <35..>213
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490;
                     propagated from UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Region          178..401
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBJ4.1)"
     CDS             1..401
                     /gene="GOLM1"
                     /gene_synonym="bA379P1.3; C9orf155; GOLPH2; GP73; HEL46;
                     PSEC0257"
                     /coded_by="NM_016548.4:170..1375"
                     /db_xref="CCDS:CCDS35054.1"
                     /db_xref="GeneID:51280"
                     /db_xref="HGNC:HGNC:15451"
                     /db_xref="MIM:606804"
ORIGIN      
        1 mmglgngrrs mkspplvlaa lvaciivlgf nywiassrsv dlqtrimele grvrraaaer
       61 gavelkknef qgelekqreq ldkiqsshnf qlesvnklyq dekavlvnni ttgerlirvl
      121 qdqlktlqrn ygrlqqdvlq fqknqtnler kfsydlsqci nqmkevkeqc eerieevtkk
      181 gneavasrdl senndqrqql qalsepqprl qaaglphtev pqgkgnvlgn sksqtpapss
      241 evvldskrqv ekeetneiqv vneepqrdrl pqepgreqvv edrpvggrgf ggagelgqtp
      301 qvqaalsvsq enpemegper dqlvipdgqe eeqeaagegr nqqklrgedd ynmdeneaes
      361 etdkqaalag ndrnidvfnv edqkrdtinl ldqrekrnht l
//
LOCUS       NP_001308742             673 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform l [Homo sapiens].
ACCESSION   NP_001308742
VERSION     NP_001308742.1
DBSOURCE    REFSEQ: accession NM_001321813.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 17 and 18 encode the same isoform (l).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.98246.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..673
                     /product="E3 ubiquitin-protein ligase CBL-B isoform l"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=73781
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          622..662
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(624..625,627..629,631..632,637,641)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..673
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321813.1:984..3005"
                     /note="isoform l is encoded by transcript variant 18"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikscdng hcmlngthgp ssekksnipd lsiylkgdvf dsasdpvplp parpptrdnp
      481 khgsslnrtp sdydllippl gedafdalpp slppppppar hsliehskpp gsssrpssgq
      541 dlfllpsdpf vdlasgqvpl pparrlpgen vktnrtsqdy dqlpscsdgs qaparppkpr
      601 prrtapeihh rkphgpeaal envdakiakl mgegyafeev kraleiaqnn vevarsilre
      661 fafpppvspr lnl
//
LOCUS       NP_006442                479 aa            linear   PRI 20-NOV-2025
DEFINITION  polyadenylate-binding protein-interacting protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006442
VERSION     NP_006442.2
DBSOURCE    REFSEQ: accession NM_006451.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Yin,G., Jia,S., Zhang,Y., Xian,Y., Guo,Y. and Liu,Q.
  TITLE     YAP1-activated ZNF131 promotes hepatocellular carcinoma cell
            proliferation through transcriptional regulation of PAIP1
  JOURNAL   Arch Biochem Biophys 754, 109921 (2024)
   PUBMED   38341068
  REMARK    GeneRIF: YAP1-activated ZNF131 promotes hepatocellular carcinoma
            cell proliferation through transcriptional regulation of PAIP1.
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Swarup,N., Hong,K.O., Chawla,K., Choi,S.J., Shin,J.A., Oh,K.Y.,
            Yoon,H.J., Lee,J.I., Cho,S.D. and Hong,S.D.
  TITLE     Effect of PAIP1 on the metastatic potential and prognostic
            significance in oral squamous cell carcinoma
  JOURNAL   Int J Oral Sci 14 (1), 9 (2022)
   PUBMED   35153296
  REMARK    GeneRIF: Effect of PAIP1 on the metastatic potential and prognostic
            significance in oral squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Deo,R.C., Sonenberg,N. and Burley,S.K.
  TITLE     X-ray structure of the human hyperplastic discs protein: an
            ortholog of the C-terminal domain of poly(A)-binding protein
  JOURNAL   Proc Natl Acad Sci U S A 98 (8), 4414-4419 (2001)
   PUBMED   11287654
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Khaleghpour,K., Svitkin,Y.V., Craig,A.W., DeMaria,C.T., Deo,R.C.,
            Burley,S.K. and Sonenberg,N.
  TITLE     Translational repression by a novel partner of human poly(A)
            binding protein, Paip2
  JOURNAL   Mol Cell 7 (1), 205-216 (2001)
   PUBMED   11172725
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Gray,N.K., Coller,J.M., Dickson,K.S. and Wickens,M.
  TITLE     Multiple portions of poly(A)-binding protein stimulate translation
            in vivo
  JOURNAL   EMBO J 19 (17), 4723-4733 (2000)
   PUBMED   10970864
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Craig,A.W., Haghighat,A., Yu,A.T. and Sonenberg,N.
  TITLE     Interaction of polyadenylate-binding protein with the eIF4G
            homologue PAIP enhances translation
  JOURNAL   Nature 392 (6675), 520-523 (1998)
   PUBMED   9548260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015937.2, DB089732.1 and
            AC114956.2.
            
            On Dec 11, 2001 this sequence version replaced NP_006442.1.
            
            Summary: The protein encoded by this gene interacts with
            poly(A)-binding protein and with the cap-binding complex eIF4A. It
            is involved in translational initiation and protein biosynthesis.
            Overexpression of this gene in COS7 cells stimulates translation.
            Alternative splicing occurs at this locus and three transcript
            variants encoding three distinct isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136920.1, AF013758.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306846.8/ ENSP00000302768.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p12"
     Protein         1..479
                     /product="polyadenylate-binding protein-interacting
                     protein 1 isoform 1"
                     /note="PABC1-interacting protein 1; polyadenylate-binding
                     protein-interacting protein 1; PAIP-1; PABP-interacting
                     protein 1"
                     /calculated_mol_wt=53394
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H074.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:37316325,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9H074.1)"
     Site            21
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H074.1)"
     Region          <35..>123
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          116..143
                     /region_name="PABPC1-interacting motif-2 (PAM2)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H074.1)"
     Region          157..375
                     /region_name="PAIP1 middle domain (PAIP1M).
                     /evidence=ECO:0000303|PubMed:33876849"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H074.1)"
     Region          160..376
                     /region_name="MIF4G"
                     /note="MIF4G domain; pfam02854"
                     /db_xref="CDD:397130"
     Region          435..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H074.1)"
     Region          440..479
                     /region_name="PABPC1-interacting motif-1 (PAM1)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H074.1)"
     CDS             1..479
                     /gene="PAIP1"
                     /coded_by="NM_006451.5:232..1671"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3947.1"
                     /db_xref="GeneID:10605"
                     /db_xref="HGNC:HGNC:16945"
                     /db_xref="MIM:605184"
ORIGIN      
        1 msdgfdrapg agrgrsrglg rggggpeggg fpngagpaer arhqppqpka pgflqppplr
       61 qprttpppga qcevpaspqr psrpgalpeq trplrappss qdkipqqnse samakpqvvv
      121 apvlmsklsv napefypsgy sssytesyed gcedyptlse yvqdflnhlt eqpgsfetei
      181 eqfaetlngc vttddalqel veliyqqats ipnfsymgar lcnylshhlt ispqsgnfrq
      241 lllqrcrtey evkdqaakgd evtrkrfhaf vlflgelyln leikgtngqv tradilqvgl
      301 rellnalfsn pmddnlicav kllkltgsvl edawkekgkm dmeeiiqrie nvvldancsr
      361 dvkqmllklv elrssnwgrv hatstyreat pendpnyfmn eptfytsdgv pftaadpdyq
      421 ekyqellere dffpdyeeng tdlsgagdpy lddiddemdp eieeayekfc leserkrkq
//
LOCUS       NP_001340174             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340174
VERSION     NP_001340174.1
DBSOURCE    REFSEQ: accession NM_001353245.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.14620.1,
                                           SRR1803615.247622.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353245.1:302..1276"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_207837               1308 aa            linear   PRI 20-NOV-2025
DEFINITION  contactin-associated protein-like 4 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_207837
VERSION     NP_207837.2
DBSOURCE    REFSEQ: accession NM_033401.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1308)
  AUTHORS   Hu,W., Wang,M., Sun,G., Zhang,L. and Lu,H.
  TITLE     Early B Cell Factor 3 (EBF3) attenuates Parkinson's disease through
            directly regulating contactin-associated protein-like 4 (CNTNAP4)
            transcription: An experimental study
  JOURNAL   Cell Signal 118, 111139 (2024)
   PUBMED   38479556
  REMARK    GeneRIF: Early B Cell Factor 3 (EBF3) attenuates Parkinson's
            disease through directly regulating contactin-associated
            protein-like 4 (CNTNAP4) transcription: An experimental study.
REFERENCE   2  (residues 1 to 1308)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1308)
  AUTHORS   Zhang,W., Zhou,M., Lu,W., Gong,J., Gao,F., Li,Y., Xu,X., Lin,Y.,
            Zhang,X., Ding,L., Zhang,Z., Li,G., Chen,X., Sun,X., Zhu,X., Xu,P.
            and Zhang,Y.
  TITLE     CNTNAP4 deficiency in dopaminergic neurons initiates parkinsonian
            phenotypes
  JOURNAL   Theranostics 10 (7), 3000-3021 (2020)
   PUBMED   32194851
  REMARK    GeneRIF: CNTNAP4 deficiency in dopaminergic neurons initiates
            parkinsonian phenotypes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1308)
  AUTHORS   Shangguan,Y., Xu,X., Ganbat,B., Li,Y., Wang,W., Yang,Y., Lu,X.,
            Du,C., Tian,X. and Wang,X.
  TITLE     CNTNAP4 Impacts Epilepsy Through GABAA Receptors Regulation:
            Evidence From Temporal Lobe Epilepsy Patients and Mouse Models
  JOURNAL   Cereb Cortex 28 (10), 3491-3504 (2018)
   PUBMED   28968899
  REMARK    GeneRIF: we demonstrated that the expression of
            contactin-associated protein-like 4 (CNTNAP4) was decreased in the
            temporal neocortex of epileptic patients
REFERENCE   5  (residues 1 to 1308)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Haralambieva,I.H., Lambert,N.D.,
            Pankratz,V.S. and Poland,G.A.
  TITLE     Genome-wide SNP associations with rubella-specific cytokine
            responses in measles-mumps-rubella vaccine recipients
  JOURNAL   Immunogenetics 66 (7-8), 493-499 (2014)
   PUBMED   24811271
REFERENCE   6  (residues 1 to 1308)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1308)
  AUTHORS   Nordgard,S.H., Johansen,F.E., Alnaes,G.I., Bucher,E., Syvanen,A.C.,
            Naume,B., Borresen-Dale,A.L. and Kristensen,V.N.
  TITLE     Genome-wide analysis identifies 16q deletion associated with
            survival, molecular subtypes, mRNA expression, and germline
            haplotypes in breast cancer patients
  JOURNAL   Genes Chromosomes Cancer 47 (8), 680-696 (2008)
   PUBMED   18398821
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1308)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 1308)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1308)
  AUTHORS   Spiegel,I., Salomon,D., Erne,B., Schaeren-Wiemers,N. and Peles,E.
  TITLE     Caspr3 and caspr4, two novel members of the caspr family are
            expressed in the nervous system and interact with PDZ domains
  JOURNAL   Mol Cell Neurosci 20 (2), 283-297 (2002)
   PUBMED   12093160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB051550.2, AC106741.3,
            BM544789.1, Z44514.1 and AC108125.4.
            
            On Oct 19, 2006 this sequence version replaced NP_207837.1.
            
            Summary: This gene encodes a member of the neurexin protein family.
            Members of this family function in the vertebrate nervous system as
            cell adhesion molecules and receptors. This protein contains
            epidermal growth factor repeats and laminin G domains. In addition,
            it includes an F5/8 type C domain, discoidin/neuropilin- and
            fibrinogen-like domains, and thrombospondin N-terminal-like
            domains. This protein may also play a role in proper
            neurotransmission in the dopaminergic and GABAergic systems and
            mutations in this gene may be associated with certain psychiatric
            illnesses. A polymorphism in an intron of this gene may be
            associated with longevity. [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.58095.1,
                                           SRR1803615.200799.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000611870.5/ ENSP00000479811.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..1308
                     /product="contactin-associated protein-like 4 isoform 1
                     precursor"
                     /note="cell recognition molecule Caspr4; contactin
                     associated protein like 4"
                     /calculated_mol_wt=142591
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
                     /calculated_mol_wt=2702
     mat_peptide     26..1308
                     /product="Contactin-associated protein-like 4.
                     /id=PRO_0000019510"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0A0.3)"
                     /calculated_mol_wt=142591
     Region          54..176
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Region          212..341
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            260
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            285
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            359
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          398..524
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            538
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          553..584
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Site            574
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          593..634
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          604..>687
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; cl02436"
                     /db_xref="CDD:470578"
     Site            625
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            637
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            706
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            748
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          821..939
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          962..996
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            1023
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Region          1046..1176
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Site            1073
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0A0.3)"
     Site            1242..1262
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0A0.3)"
     CDS             1..1308
                     /gene="CNTNAP4"
                     /gene_synonym="CASPR4"
                     /coded_by="NM_033401.5:263..4189"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS73915.1"
                     /db_xref="GeneID:85445"
                     /db_xref="HGNC:HGNC:18747"
                     /db_xref="MIM:610518"
ORIGIN      
        1 mgsvtgavlk tllllstqnw nrveagnsyd cddplvsalp qasfssssel ssshgpgfar
       61 lnrrdgaggw splvsnkyqw lqidlgerme vtavatqggy gssnwvtsyl lmfsdsgwnw
      121 kqyrqedsiw gfsgnanads vvyyrlqpsi karflrfipl ewnpkgrigm rievfgcayr
      181 sevvdldgks sllyrfdqks lspikdiisl kfktmqsdgi llhregpngd hitlqlrrar
      241 lfllinsgea klpststlvn ltlgsllddq hwhsvliqrl gkqvnftvde hrhhfharge
      301 fnlmnldyei sfggipapgk svsfphrnfh gclenlyyng vdiidlakqq kpqiiamgnv
      361 sfscsqpqsm pvtflssrsy lalpdfsgee evsatfqfrt wnkaglllfs elqlisggil
      421 lflsdgklks nlyqpgklps ditagvelnd gqwhsvslsa kknhlsvavd gqmasaapll
      481 gpeqiysggt yyfggcpdks fgskcksplg gfqgcmrlis isgkvvdlis vqqgslgnfs
      541 dlqidscgis drclpnyceh ggecsqswst fhcnctntgy rgatchnsiy eqsceaykhr
      601 gntsgfyyid sdgsgplepf llycnmteta wtiiqhngsd ltrvrntnpe npyagffeyv
      661 asmeqlqati nraehceqef tyyckksrlv nkqdgtplsw wvgrtnetqt ywggsspdlq
      721 kctcglegnc idsqyycncd adrnewtndt gllaykehlp vtkivitdtg rlhseaaykl
      781 gpllcqgdrs fwnsasfdte asylhfptfh gelsadvsff fkttassgvf lenlgiadfi
      841 rielrsptvv tfsfdvgngp feisvqspth fndnqwhhvr vernmkeasl qvdqltpktq
      901 papadghvll qlnsqlfvgg tatrqrgflg cirslqlngm tldleeraqv tpevqpgcrg
      961 hcssygklcr nggkcrerpi gffcdctfsa ytgpfcsnei sayfgsgssv iynfqenyll
     1021 sknssshaas fhgdmklsre mikfsfrttr tpslllfvss fykeylsvii akngslqiry
     1081 klnkyqepdv vnfdfknmad gqlhhiminr eegvvfieid dnrrrqvhls sgtefsavks
     1141 lvlgrilehs dvdqdtalag aqgftgclsa vqlshvaplk aalhpshpdp vtvtghvtes
     1201 scmaqpgtda tsrerthsfa dhsgtiddre planaiksds aviggliavv ifillcitai
     1261 avriyqqkrl ykrseakrse nvdsaeavlk selniqnavn enqkeyff
//
LOCUS       NP_001341224            1460 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001341224 XP_005251958
VERSION     NP_001341224.1
DBSOURCE    REFSEQ: accession NM_001354295.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On Aug 29, 2017 this sequence version replaced XP_005251958.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.190407.1,
                                           SRR1660805.57015.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1460
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 2"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=162767
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Site            172
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          574..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          739..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          846..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          889..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          1245..1308
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1356..1457
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1460
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001354295.2:216..4598"
                     /note="isoform 2 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS65131.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgkpd ktlrfslcsd nlegisegps nrsnsvssld legesvselg
      601 agpsgsngve alqlleheqa ttqdnlddkl rkfeirdmmg ltddrdiset vsetwstdvl
      661 gsdfdpnide drlqeiagaa aenmlgsllc lpgsgsvlld pctgstiset tseawsvevl
      721 psdseapdlk qeerlqeles csglgstsdd tdvrevssrp stpglsvvsg isatsedipn
      781 kiedlrsecs sdfggkdsvt spdmdeithg ahqltsppsq sesllamfdp lsshegasav
      841 vrpkvhyarp shpppdppil egavggnear lpnfgshvlt paemeafkqr hsyperlvrs
      901 rssdivssvr rpmsdpswnr rpgneerelp paaaigatsl vaaphsssss pskdssrget
      961 eerkdsddek sdrnrpwwrk rfvsampkap ipfrkkekqe kdkddlgpdr fstltddpsp
     1021 rlsaqaqvae dildkyrnai krtspsdgam anyestevmg dgesahdspr dealqnisad
     1081 dlpdsasqaa hpqdsafsyr dakkklrlal csadsvafpv lthstrnglp dhtdpednei
     1141 vcflkvqiae ainlqdknlm aqlqetmrcv crfdnrtcrk llasiaedyr krapyiaylt
     1201 rcrqglqttq ahlerllqrv lrdkevanry fttvcvrlll eskekkiref iqdfqkltaa
     1261 ddktaqvedf lqflygamaq dviwqnasee qlqdaqlaie rsvmnrifkl afypnqdgdi
     1321 lrdqvlhehi qrlskvvtan hralqipevy lreapwpsaq seirtisayk tprdkvqcil
     1381 rmcstimnll slanedsvpg addfvpvlvf vlikanppcl lstvqyissf yasclsgees
     1441 ywwmqftaav efiktiddrk
//
LOCUS       NP_004353                610 aa            linear   PRI 20-NOV-2025
DEFINITION  calmegin precursor [Homo sapiens].
ACCESSION   NP_004353
VERSION     NP_004353.1
DBSOURCE    REFSEQ: accession NM_004362.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Li,C., He,J., Chen,J., Zhao,J., Gu,D., Hixson,J.E., Rao,D.C.,
            Jaquish,C.E., Gu,C.C., Chen,J., Huang,J., Chen,S. and Kelly,T.N.
  TITLE     Genome-Wide Gene-Sodium Interaction Analyses on Blood Pressure: The
            Genetic Epidemiology Network of Salt-Sensitivity Study
  JOURNAL   Hypertension 68 (2), 348-355 (2016)
   PUBMED   27271309
  REMARK    GeneRIF: In gene-based analysis CLGN1 represented one of a cluster
            of genes, which interacted with sodium to influence Blood Pressure.
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Ikawa,M., Nakanishi,T., Yamada,S., Wada,I., Kominami,K., Tanaka,H.,
            Nozaki,M., Nishimune,Y. and Okabe,M.
  TITLE     Calmegin is required for fertilin alpha/beta heterodimerization and
            sperm fertility
  JOURNAL   Dev Biol 240 (1), 254-261 (2001)
   PUBMED   11784061
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Yoshinaga,K., Tanii,I. and Toshimori,K.
  TITLE     Molecular chaperone calmegin localization to the endoplasmic
            reticulum of meiotic and post-meiotic germ cells in the mouse
            testis
  JOURNAL   Arch Histol Cytol 62 (3), 283-293 (1999)
   PUBMED   10495883
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Tanaka,H., Ikawa,M., Tsuchida,J., Nozaki,M., Suzuki,M.,
            Fujiwara,T., Okabe,M. and Nishimune,Y.
  TITLE     Cloning and characterization of the human Calmegin gene encoding
            putative testis-specific chaperone
  JOURNAL   Gene 204 (1-2), 159-163 (1997)
   PUBMED   9434179
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Ikawa,M., Wada,I., Kominami,K., Watanabe,D., Toshimori,K.,
            Nishimune,Y. and Okabe,M.
  TITLE     The putative chaperone calmegin is required for sperm fertility
  JOURNAL   Nature 387 (6633), 607-611 (1997)
   PUBMED   9177349
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Watanabe,D., Yamada,K., Nishina,Y., Tajima,Y., Koshimizu,U.,
            Nagata,A. and Nishimune,Y.
  TITLE     Molecular cloning of a novel Ca(2+)-binding protein (calmegin)
            specifically expressed during male meiotic germ cell development
  JOURNAL   J Biol Chem 269 (10), 7744-7749 (1994)
   PUBMED   8126001
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC396076.1, BC028357.2 and
            D86322.1.
            
            Summary: Calmegin is a testis-specific endoplasmic reticulum
            chaperone protein.  CLGN may play a role in spermatogeneisis and
            infertility. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the shorter transcript.
            Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86322.1, SRR1803617.222683.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325617.10/ ENSP00000326699.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..610
                     /product="calmegin precursor"
                     /note="testis tissue sperm-binding protein Li 79P"
                     /calculated_mol_wt=67832
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2225
     Region          62..429
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27824; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Region          258..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          317..350
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          339..352
                     /region_name="2-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          356..369
                     /region_name="2-2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          370..383
                     /region_name="2-3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          384..397
                     /region_name="2-4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Site            472..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Region          521..610
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14967.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52194; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52194; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52194; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P52194; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P27824; propagated from
                     UniProtKB/Swiss-Prot (O14967.1)"
     CDS             1..610
                     /gene="CLGN"
                     /coded_by="NM_004362.3:122..1954"
                     /db_xref="CCDS:CCDS3751.1"
                     /db_xref="GeneID:1047"
                     /db_xref="HGNC:HGNC:2060"
                     /db_xref="MIM:601858"
ORIGIN      
        1 mhfqafwlcl gllfisinae fmdddveted feenseeidv neselsseik yktpqpigev
       61 yfaetfdsgr lagwvlskak kddmdeeisi ydgrweieel kenqvpgdrg lvlksrakhh
      121 aisavlakpf ifadkplivq yevnfqdgid cggayiklla dtddlilenf ydktsyiimf
      181 gpdkcgedyk lhfifrhkhp ktgvfeekha kppdvdlkkf ftdrkthlyt lvmnpddtfe
      241 vlvdqtvvnk gslledvvpp ikppkeiedp ndkkpeewde rakipdpsav kpedwdesep
      301 aqiedssvvk pagwlddepk fipdpnaekp ddwnedtdge weapqilnpa crigcgewkp
      361 pmidnpkykg vwrpplvdnp nyqgiwsprk ipnpdyfedd hpflltsfsa lglelwsmts
      421 diyfdnfiic sekevadhwa adgwrwkimi anankpgvlk qlmaaaeghp wlwliylvta
      481 gvpialitsf cwprkvkkkh kdteykktdi cipqtkgvle qeekeekaal ekpmdleeek
      541 kqndgemlek eeesepeeks eeeieiiegq eesnqsnksg sedemkeade stgsgdgpik
      601 svrkrrvrkd
//
LOCUS       NP_005668                455 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholinesterase collagenic tail peptide isoform I precursor
            [Homo sapiens].
ACCESSION   NP_005668
VERSION     NP_005668.2
DBSOURCE    REFSEQ: accession NM_005677.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Hesami,O., Ramezani,M., Ghasemi,A., Fatehi,F., Okhovat,A.A.,
            Ziaadini,B., Kariminejad,A. and Nafissi,S.
  TITLE     COLQ-Congenital myasthenic syndrome in an Iranian cohort: the
            clinical and genetics spectrum
  JOURNAL   Orphanet J Rare Dis 19 (1), 113 (2024)
   PUBMED   38475910
  REMARK    GeneRIF: COLQ-Congenital myasthenic syndrome in an Iranian cohort:
            the clinical and genetics spectrum.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Barbeau,S., Semprez,F., Dobbertin,A., Merriadec,L., Roussange,F.,
            Eymard,B., Sternberg,D., Fournier,E., Karasoy,H., Martinat,C. and
            Legay,C.
  TITLE     Molecular Analysis of a Congenital Myasthenic Syndrome Due to a
            Pathogenic Variant Affecting the C-Terminus of ColQ
  JOURNAL   Int J Mol Sci 24 (22), 16217 (2023)
   PUBMED   38003406
  REMARK    GeneRIF: Molecular Analysis of a Congenital Myasthenic Syndrome Due
            to a Pathogenic Variant Affecting the C-Terminus of ColQ.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Mishra,S., Nair,K.V. and Shukla,A.
  TITLE     Delineation of molecular characteristics of congenital myasthenic
            syndromes in Indian families and review of literature
  JOURNAL   Clin Dysmorphol 32 (4), 162-167 (2023)
   PUBMED   37646703
  REMARK    GeneRIF: Delineation of molecular characteristics of congenital
            myasthenic syndromes in Indian families and review of literature.
            Review article
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Uyen Dao,T.M., Barbeau,S., Messeant,J., Della-Gaspera,B.,
            Bouceba,T., Semprez,F., Legay,C. and Dobbertin,A.
  TITLE     The collagen ColQ binds to LRP4 and regulates the activation of the
            Muscle-Specific Kinase-LRP4 receptor complex by agrin at the
            neuromuscular junction
  JOURNAL   J Biol Chem 299 (8), 104962 (2023)
   PUBMED   37356721
  REMARK    GeneRIF: The collagen ColQ binds to LRP4 and regulates the
            activation of the Muscle-Specific Kinase-LRP4 receptor complex by
            agrin at the neuromuscular junction.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Deprez,P. and Inestrosa,N.C.
  TITLE     Molecular modeling of the collagen-like tail of asymmetric
            acetylcholinesterase
  JOURNAL   Protein Eng 13 (1), 27-34 (2000)
   PUBMED   10679527
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Altamirano,C.V. and Lockridge,O.
  TITLE     Conserved aromatic residues of the C-terminus of human
            butyrylcholinesterase mediate the association of tetramers
  JOURNAL   Biochemistry 38 (40), 13414-13422 (1999)
   PUBMED   10529218
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Ohno,K., Brengman,J.M., Felice,K.J., Cornblath,D.R. and Engel,A.G.
  TITLE     Congenital end-plate acetylcholinesterase deficiency caused by a
            nonsense mutation and an A-->G splice-donor-site mutation at
            position +3 of the collagenlike-tail-subunit gene (COLQ): how does
            G at position +3 result in aberrant splicing?
  JOURNAL   Am J Hum Genet 65 (3), 635-644 (1999)
   PUBMED   10441569
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Donger,C., Krejci,E., Serradell,A.P., Eymard,B., Bon,S., Nicole,S.,
            Chateau,D., Gary,F., Fardeau,M., Massoulie,J. and Guicheney,P.
  TITLE     Mutation in the human acetylcholinesterase-associated collagen
            gene, COLQ, is responsible for congenital myasthenic syndrome with
            end-plate acetylcholinesterase deficiency (Type Ic)
  JOURNAL   Am J Hum Genet 63 (4), 967-975 (1998)
   PUBMED   9758617
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Ohno,K., Brengman,J., Tsujino,A. and Engel,A.G.
  TITLE     Human endplate acetylcholinesterase deficiency caused by mutations
            in the collagen-like tail subunit (ColQ) of the asymmetric enzyme
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9654-9659 (1998)
   PUBMED   9689136
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF057036.1, AK128401.1 and
            AI554171.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 10, 2002 this sequence version replaced NP_005668.1.
            
            Summary: This gene encodes the subunit of a collagen-like molecule
            associated with acetylcholinesterase in skeletal muscle. Each
            molecule is composed of three identical subunits. Each subunit
            contains a proline-rich attachment domain (PRAD) that binds an
            acetylcholinesterase tetramer to anchor the catalytic subunit of
            the enzyme to the basal lamina. Mutations in this gene are
            associated with endplate acetylcholinesterase deficiency. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (I) encodes the longest protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF057036.1, SRR1803611.51101.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383788.10/ ENSP00000373298.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..455
                     /product="acetylcholinesterase collagenic tail peptide
                     isoform I precursor"
                     /note="single strand of homotrimeric collagen-like tail
                     subunit of asymmetric acetylcholinesterase; AChE Q
                     subunit; acetylcholinesterase-associated collagen;
                     collagenic tail of endplate acetylcholinesterase;
                     acetylcholinesterase collagenic tail peptide;
                     collagen-like tail subunit (single strand of homotrimer)
                     of asymmetric acetylcholinesterase"
                     /calculated_mol_wt=44498
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3287
     mat_peptide     23..455
                     /product="acetylcholinesterase collagenic tail peptide
                     isoform I"
                     /calculated_mol_wt=45285
     Region          51..67
                     /region_name="proline-rich attachment domain (PRAD)"
     Region          90..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y215.2)"
     Region          <105..>290
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          130..133
                     /region_name="Heparan sulfate proteoglycan binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y215.2)"
     Region          235..238
                     /region_name="Heparan sulfate proteoglycan binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y215.2)"
     Region          373..>397
                     /region_name="myxo_disulf_rpt"
                     /note="Myxococcus cysteine-rich repeat; TIGR02232"
                     /db_xref="CDD:200169"
     CDS             1..455
                     /gene="COLQ"
                     /gene_synonym="CMS5; EAD"
                     /coded_by="NM_005677.4:82..1449"
                     /note="isoform I precursor is encoded by transcript
                     variant I"
                     /db_xref="CCDS:CCDS33709.1"
                     /db_xref="GeneID:8292"
                     /db_xref="HGNC:HGNC:2226"
                     /db_xref="MIM:603033"
ORIGIN      
        1 mvvlnpmtlg iylqlfflsi vsqptfinsv lpisaalpsl dqkkrgghka cclltppppp
       61 lfpppffrgg rspllspdmk nlmleletsq spcmqgslgs pgppgpqgpp glpgktgpkg
      121 ekgelgrpgr kgrpgppgvp gmpgpigwpg pegprgekgd lgmmglpgsr gpmgskgypg
      181 srgekgsrge kgdlgpkgek gfpgfpgmlg qkgemgpkge pgiaghrgpt grpgkrgkqg
      241 qkgdsgvmgp pgkpgpsgqp grpgppgppp agqlimgpkg ergfpgppgr clcgptmnvn
      301 npsygesvyg pssprvpvif vvnnqeeler lntqnaiafr rdqrslyfkd slgwlpiqlt
      361 pfypvdytad qhgtcgdgll qpgeecddgn sdvgddcirc hraycgdghr hegvedcdgs
      421 dfgyltcety lpgsygdlqc tqycyidstp cryft
//
LOCUS       NP_001307847             297 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001307847 XP_006718145
VERSION     NP_001307847.1
DBSOURCE    REFSEQ: accession NM_001320918.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Zhou,L., Chen,Z., Zou,Y., Zhang,X., Wang,Z., Zhu,H., Lin,J.,
            Huang,Z., Zheng,L., Chen,J., Xie,M., Zhang,M., Zhang,R., Zhu,M.,
            Wang,Z., Zhou,H., Gao,S., Yin,Y., Wu,Y. and Kang,T.
  TITLE     ASB7 is a negative regulator of H3K9me3 homeostasis
  JOURNAL   Science 389 (6757), 309-316 (2025)
   PUBMED   40440427
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Van Matre,S., Huq,S., Akana,L., Eldridge,D.E., Zuniga,O.,
            Rodrigues,H. and Wolfe,A.R.
  TITLE     Enhanced radiosensitivity of pancreatic cancer achieved through
            inhibition of Cyclin-dependent kinase 1
  JOURNAL   Radiother Oncol 200, 110531 (2024)
   PUBMED   39270987
  REMARK    GeneRIF: Enhanced radiosensitivity of pancreatic cancer achieved
            through inhibition of Cyclin-dependent kinase 1.
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Vishwakarma,K.K., Kolthur,U.S. and Venkatramani,R.
  TITLE     Multiple Functional Protein-Protein Interaction Interfaces
            Allosterically Regulate ATP-Binding in Cyclin-Dependent Kinase-1
  JOURNAL   Proteins 92 (11), 1329-1342 (2024)
   PUBMED   39012208
  REMARK    GeneRIF: Multiple Functional Protein-Protein Interaction Interfaces
            Allosterically Regulate ATP-Binding in Cyclin-Dependent Kinase-1.
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Luo,C., He,J., Yang,Y., Wu,K., Fu,X., Cheng,J., Ming,Y., Liu,W. and
            Peng,Y.
  TITLE     SRSF9 promotes cell proliferation and migration of glioblastoma
            through enhancing CDK1 expression
  JOURNAL   J Cancer Res Clin Oncol 150 (6), 292 (2024)
   PUBMED   38842611
  REMARK    GeneRIF: SRSF9 promotes cell proliferation and migration of
            glioblastoma through enhancing CDK1 expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Parker,L.L. and Piwnica-Worms,H.
  TITLE     Inactivation of the p34cdc2-cyclin B complex by the human WEE1
            tyrosine kinase
  JOURNAL   Science 257 (5078), 1955-1957 (1992)
   PUBMED   1384126
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Dutta,A. and Stillman,B.
  TITLE     cdc2 family kinases phosphorylate a human cell DNA replication
            factor, RPA, and activate DNA replication
  JOURNAL   EMBO J 11 (6), 2189-2199 (1992)
   PUBMED   1318195
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Azzi,L., Meijer,L., Reed,S.I., Pidikiti,R. and Tung,H.Y.
  TITLE     Interaction between the cell-cycle-control proteins p34cdc2 and
            p9CKShs2. Evidence for two cooperative binding domains in p9CKShs2
  JOURNAL   Eur J Biochem 203 (3), 353-360 (1992)
   PUBMED   1310466
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Nazarenko,S.A., Ostroverhova,N.V. and Spurr,N.K.
  TITLE     Regional assignment of the human cell cycle control gene CDC2 to
            chromosome 10q21 by in situ hybridization
  JOURNAL   Hum Genet 87 (5), 621-622 (1991)
   PUBMED   1916766
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Lee,M.G. and Nurse,P.
  TITLE     Complementation used to clone a human homologue of the fission
            yeast cell cycle control gene cdc2
  JOURNAL   Nature 327 (6117), 31-35 (1987)
   PUBMED   3553962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA823877.1, BC014563.1,
            BQ308742.1 and BU633268.1.
            
            On Mar 10, 2016 this sequence version replaced XP_006718145.1.
            
            Summary: The protein encoded by this gene is a member of the
            Ser/Thr protein kinase family. This protein is a catalytic subunit
            of the highly conserved protein kinase complex known as M-phase
            promoting factor (MPF), which is essential for G2/M phase
            transitions of eukaryotic cell cycle. Mitotic cyclins stably
            associate with this protein and function as regulatory subunits.
            The kinase activity of this protein is controlled by cyclin
            accumulation and destruction through the cell cycle. The
            phosphorylation and dephosphorylation of this protein also play
            important regulatory roles in cell cycle control. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2023].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.229947.1,
                                           SRR1660809.1145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.2"
     Protein         1..297
                     /product="cyclin-dependent kinase 1 isoform 1"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="cell division cycle 2, G1 to S and G2 to M; cell
                     division control protein 2 homolog; p34 protein kinase;
                     cell cycle controller CDC2; cell division protein kinase
                     1"
                     /calculated_mol_wt=33964
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Region          3..287
                     /region_name="STKc_CDK1_euk"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 1 from higher eukaryotes;
                     cd07861"
                     /db_xref="CDD:270845"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PKR.
                     /evidence=ECO:0000269|PubMed:20395957; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P11440; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            order(10..13,18,31,33,50,64,80..83,86,88..89,128,130,
                     132..133,135,146,149,161,163..166,168,206..207)
                     /site_type="active"
                     /db_xref="CDD:270845"
     Site            order(10..13,18,31,33,64,80..83,86,89,132..133,135,146)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270845"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKMYT1.
                     /evidence=ECO:0000269|PubMed:7569953,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PKMYT1, WEE1, WEE2 and
                     PKC/PRKCD. /evidence=ECO:0000269|PubMed:19917613,
                     ECO:0000269|PubMed:29606300, ECO:0000269|PubMed:7569953,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            order(37,42..44,46,49..50,52..53,56..57,71,117,120..123,
                     151..153,155..156,160..161,273,277..279)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270845"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            order(50,88,128,130,149,161,163..166,168,206..207)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270845"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            145..168
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270845"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CAK.
                     /evidence=ECO:0000269|PubMed:20360007,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P06493.3)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P06493.3)"
     CDS             1..297
                     /gene="CDK1"
                     /gene_synonym="CDC2; CDC28A; P34CDC2"
                     /coded_by="NM_001320918.1:155..1048"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS44408.1"
                     /db_xref="GeneID:983"
                     /db_xref="HGNC:HGNC:1722"
                     /db_xref="MIM:116940"
ORIGIN      
        1 medytkieki gegtygvvyk grhkttgqvv amkkirlese eegvpstair eisllkelrh
       61 pnivslqdvl mqdsrlylif eflsmdlkky ldsippgqym dsslvksyly qilqgivfch
      121 srrvlhrdlk pqnlliddkg tikladfgla rafgipirvy thevvtlwyr spevllgsar
      181 ystpvdiwsi gtifaelatk kplfhgdsei dqlfrifral gtpnnevwpe veslqdyknt
      241 fpkwkpgsla shvknldeng ldllskmliy dpakrisgkm alnhpyfndl dnqikkm
//
LOCUS       NP_001308520             503 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 29 [Homo sapiens].
ACCESSION   NP_001308520
VERSION     NP_001308520.1
DBSOURCE    REFSEQ: accession NM_001321591.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 503)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.128520.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..503
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 29"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=56779
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          371..498
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..503
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321591.2:671..2182"
                     /note="isoform 29 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS93610.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkkr kssssvqmme pqttvihnpd gnkestessn
      361 ttiededvka rkqeiikvte qlieainngd feaytkicdp gltafepeal gnlvegmdfh
      421 rfyfenalsk snkpihtiil nphvhlvgdd aaciayirlt qymdgsgmpk tmqseetrvw
      481 hrrdgkwqnv hfhrsgsptv pik
//
LOCUS       NP_001171892              89 aa            linear   PRI 20-NOV-2025
DEFINITION  FXYD domain-containing ion transport regulator 4 precursor [Homo
            sapiens].
ACCESSION   NP_001171892
VERSION     NP_001171892.1
DBSOURCE    REFSEQ: accession NM_001184963.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Vedovato,N. and Gadsby,D.C.
  TITLE     Route, mechanism, and implications of proton import during Na+/K+
            exchange by native Na+/K+-ATPase pumps
  JOURNAL   J Gen Physiol 143 (4), 449-464 (2014)
   PUBMED   24688018
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Lee,J.H., Cheng,R., Honig,L.S., Feitosa,M., Kammerer,C.M.,
            Kang,M.S., Schupf,N., Lin,S.J., Sanders,J.L., Bae,H., Druley,T.,
            Perls,T., Christensen,K., Province,M. and Mayeux,R.
  TITLE     Genome wide association and linkage analyses identified three
            loci-4q25, 17q23.2, and 10q11.21-associated with variation in
            leukocyte telomere length: the Long Life Family Study
  JOURNAL   Front Genet 4, 310 (2014)
   PUBMED   24478790
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Mishra,N.K., Peleg,Y., Cirri,E., Belogus,T., Lifshitz,Y.,
            Voelker,D.R., Apell,H.J., Garty,H. and Karlish,S.J.
  TITLE     FXYD proteins stabilize Na,K-ATPase: amplification of specific
            phosphatidylserine-protein interactions
  JOURNAL   J Biol Chem 286 (11), 9699-9712 (2011)
   PUBMED   21228272
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Sweadner,K.J., Arystarkhova,E., Donnet,C. and Wetzel,R.K.
  TITLE     FXYD proteins as regulators of the Na,K-ATPase in the kidney
  JOURNAL   Ann N Y Acad Sci 986, 382-387 (2003)
   PUBMED   12763854
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Crowell,K.J., Franzin,C.M., Koltay,A., Lee,S., Lucchese,A.M.,
            Snyder,B.C. and Marassi,F.M.
  TITLE     Expression and characterization of the FXYD ion transport
            regulators for NMR structural studies in lipid micelles and lipid
            bilayers
  JOURNAL   Biochim Biophys Acta 1645 (1), 15-21 (2003)
   PUBMED   12535606
  REMARK    GeneRIF: molecular cloning, protein expression, sequencing and NMR
            structure determination
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Garty,H., Lindzen,M., Scanzano,R., Aizman,R., Fuzesi,M.,
            Goldshleger,R., Farman,N., Blostein,R. and Karlish,S.J.
  TITLE     A functional interaction between CHIF and Na-K-ATPase: implication
            for regulation by FXYD proteins
  JOURNAL   Am J Physiol Renal Physiol 283 (4), F607-F615 (2002)
   PUBMED   12217851
  REMARK    GeneRIF: CHIF can act as tissue-specific modulators of Na-K-ATPase
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Beguin,P., Crambert,G., Guennoun,S., Garty,H., Horisberger,J.D. and
            Geering,K.
  TITLE     CHIF, a member of the FXYD protein family, is a regulator of
            Na,K-ATPase distinct from the gamma-subunit
  JOURNAL   EMBO J 20 (15), 3993-4002 (2001)
   PUBMED   11483503
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Sweadner,K.J. and Rael,E.
  TITLE     The FXYD gene family of small ion transport regulators or channels:
            cDNA sequence, protein signature sequence, and expression
  JOURNAL   Genomics 68 (1), 41-56 (2000)
   PUBMED   10950925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY358584.1 and BC054876.1.
            
            Summary: This gene encodes a member of a family of small membrane
            proteins that share a 35-amino acid signature sequence domain,
            beginning with the sequence PFXYD and containing 7 invariant and 6
            highly conserved amino acids. The approved human gene nomenclature
            for the family is FXYD-domain containing ion transport regulator.
            FXYD4, originally named CHIF for channel-inducing factor, has been
            shown to modulate the properties of the Na,K-ATPase, as has FXYD2,
            also known as the gamma subunit of the Na,K-ATPase, and FXYD7.
            Transmembrane topology has been established for FXYD4 and two
            family members (FXYD1 and FXYD2), with the N-terminus extracellular
            and the C-terminus on the cytoplasmic side of the membrane.
            Alternatively spliced transcript variants encoding the same protein
            have been found.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) represents use of an alternate
            splice acceptor site in the 5' UTR, as compared to variant 1. This
            variant is likely to only be found in individuals with the A allele
            of SNP rs10899795, which is polymorphic in most populations.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358584.1, ERR279849.4214.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.21"
     Protein         1..89
                     /product="FXYD domain-containing ion transport regulator 4
                     precursor"
                     /note="channel-inducing factor"
                     /calculated_mol_wt=7393
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1998
     mat_peptide     20..89
                     /product="FXYD domain-containing ion transport regulator
                     4"
                     /calculated_mol_wt=7393
     Region          21..68
                     /region_name="FXYD4"
                     /note="FXYD domain-containing ion transport regulator 4;
                     cd20322"
                     /db_xref="CDD:410558"
     Site            order(30,32,34,37..38,41..42,44..45,48,51..53,55..56,58)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410558"
     Site            39..59
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P59646.2)"
     CDS             1..89
                     /gene="FXYD4"
                     /gene_synonym="CHIF"
                     /coded_by="NM_001184963.1:197..466"
                     /db_xref="GeneID:53828"
                     /db_xref="HGNC:HGNC:4028"
                     /db_xref="MIM:616926"
ORIGIN      
        1 mervtlalll lagltalean dpfankddpf yydwknlqls glicggllai agiaavlsgk
       61 ckckssqkqh spvpekaipl itpgsattc
//
LOCUS       NP_055527               1707 aa            linear   PRI 20-NOV-2025
DEFINITION  histone-lysine N-methyltransferase SETD1A [Homo sapiens].
ACCESSION   NP_055527 XP_049380
VERSION     NP_055527.1
DBSOURCE    REFSEQ: accession NM_014712.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1707)
  AUTHORS   Hoshii,T., Kikuchi,S., Kujirai,T., Masuda,T., Ito,T., Yasuda,S.,
            Matsumoto,M., Rahmutulla,B., Fukuyo,M., Murata,T., Kurumizaka,H.
            and Kaneda,A.
  TITLE     BOD1L mediates chromatin binding and non-canonical function of H3K4
            methyltransferase SETD1A
  JOURNAL   Nucleic Acids Res 52 (16), 9463-9480 (2024)
   PUBMED   38989615
  REMARK    GeneRIF: BOD1L mediates chromatin binding and non-canonical
            function of H3K4 methyltransferase SETD1A.
REFERENCE   3  (residues 1 to 1707)
  AUTHORS   Colijn,M.A., Carrion,P., Poirier-Morency,G., Rogic,S., Torres,I.,
            Menon,M., Lisonek,M., Cook,C., DeGraaf,A., Thammaiah,S.P.,
            Neelakant,H., Willaeys,V., Leonova,O., White,R.F., Yip,S.,
            Mungall,A.J., MacLeod,P.M., Gibson,W.T., Sullivan,P.F., Honer,W.G.,
            Pavlidis,P. and Stowe,R.M.
  TITLE     SETD1A variant-associated psychosis: A systematic review of the
            clinical literature and description of two new cases
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 129, 110888 (2024)
   PUBMED   37918557
  REMARK    GeneRIF: SETD1A variant-associated psychosis: A systematic review
            of the clinical literature and description of two new cases.
REFERENCE   4  (residues 1 to 1707)
  AUTHORS   Amin,H.M., Szabo,B., Abukhairan,R., Zeke,A., Kardos,J., Schad,E.
            and Tantos,A.
  TITLE     In Vivo and In Vitro Characterization of the RNA Binding Capacity
            of SETD1A (KMT2F)
  JOURNAL   Int J Mol Sci 24 (22), 16032 (2023)
   PUBMED   38003223
  REMARK    GeneRIF: In Vivo and In Vitro Characterization of the RNA Binding
            Capacity of SETD1A (KMT2F).
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1707)
  AUTHORS   Chen,J., Xu,Z., Huang,H., Tang,Y., Shan,H. and Xiao,F.
  TITLE     SETD1A drives stemness by reprogramming the epigenetic landscape in
            hepatocellular carcinoma stem cells
  JOURNAL   JCI Insight 8 (18), e168375 (2023)
   PUBMED   37581938
  REMARK    GeneRIF: SETD1A drives stemness by reprogramming the epigenetic
            landscape in hepatocellular carcinoma stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1707)
  AUTHORS   Cho,Y.W., Hong,T., Hong,S., Guo,H., Yu,H., Kim,D., Guszczynski,T.,
            Dressler,G.R., Copeland,T.D., Kalkum,M. and Ge,K.
  TITLE     PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
            methyltransferase complex
  JOURNAL   J Biol Chem 282 (28), 20395-20406 (2007)
   PUBMED   17500065
REFERENCE   7  (residues 1 to 1707)
  AUTHORS   Narayanan,A., Ruyechan,W.T. and Kristie,T.M.
  TITLE     The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4
            trimethylation at herpesvirus immediate early promoters for
            initiation of infection
  JOURNAL   Proc Natl Acad Sci U S A 104 (26), 10835-10840 (2007)
   PUBMED   17578910
  REMARK    GeneRIF: HCF-1 was required for recruitment of the histone
            methyltransferases Set1 and MLL1, leading to histone H3K4
            trimethylation and transcriptional activation.
REFERENCE   8  (residues 1 to 1707)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   9  (residues 1 to 1707)
  AUTHORS   Lee,J.H. and Skalnik,D.G.
  TITLE     CpG-binding protein (CXXC finger protein 1) is a component of the
            mammalian Set1 histone H3-Lys4 methyltransferase complex, the
            analogue of the yeast Set1/COMPASS complex
  JOURNAL   J Biol Chem 280 (50), 41725-41731 (2005)
   PUBMED   16253997
REFERENCE   10 (residues 1 to 1707)
  AUTHORS   Wysocka,J., Myers,M.P., Laherty,C.D., Eisenman,R.N. and Herr,W.
  TITLE     Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone
            H3-K4 methyltransferase are tethered together selectively by the
            cell-proliferation factor HCF-1
  JOURNAL   Genes Dev 17 (7), 896-911 (2003)
   PUBMED   12670868
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB002337.2 and BC027450.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2004 this sequence version replaced XP_049380.2.
            
            Summary: The protein encoded by this gene is a component of a
            histone methyltransferase (HMT) complex that produces mono-, di-,
            and trimethylated histone H3 at Lys4. Trimethylation of histone H3
            at lysine 4 (H3K4me3) is a chromatin modification known to
            generally mark the transcription start sites of active genes. The
            protein contains SET domains, a RNA recognition motif domain and is
            a member of the class V-like SAM-binding methyltransferase
            superfamily. [provided by RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002337.2, SRR9304718.128347.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262519.14/ ENSP00000262519.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..1707
                     /product="histone-lysine N-methyltransferase SETD1A"
                     /EC_number="2.1.1.364"
                     /note="hSET1A; lysine N-methyltransferase 2F; SET
                     domain-containing protein 1A; set1/Ash2 histone
                     methyltransferase complex subunit SET1"
                     /calculated_mol_wt=185904
     Region          60..89
                     /region_name="Interaction with WDR82.
                     /evidence=ECO:0000269|PubMed:37030068"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          92..186
                     /region_name="RRM_Set1A"
                     /note="RNA recognition motif in vertebrate histone-lysine
                     N-methyltransferase Setd1A (Set1A); cd12548"
                     /db_xref="CDD:409964"
     Region          194..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          331..363
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          381..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Region          506..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Region          834..854
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          891..1251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Region          <1070..>1130
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            1103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15047.3)"
     Region          1264..1293
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1299..1303
                     /region_name="HCFC1-binding motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1307..1417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1415..1450
                     /region_name="Interaction with CFP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1425..1562
                     /region_name="N-SET"
                     /note="COMPASS (Complex proteins associated with Set1p)
                     component N; pfam11764"
                     /db_xref="CDD:463344"
     Region          1450..1537
                     /region_name="Interaction with ASH2L, RBBP5 and WDR5.
                     /evidence=ECO:0000269|PubMed:17998332"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1472..1499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1492..1497
                     /region_name="WDR5 interaction motif (WIN).
                     /evidence=ECO:0000269|PubMed:22266653,
                     ECO:0000269|PubMed:22665483"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1537..1542
                     /region_name="RxxxRR motif.
                     /evidence=ECO:0000250|UniProtKB:P38827"
                     /note="propagated from UniProtKB/Swiss-Prot (O15047.3)"
     Region          1556..1703
                     /region_name="SET_SETD1"
                     /note="SET domain (including post-SET domain) found in SET
                     domain-containing protein 1 (SETD1) and similar proteins;
                     cd19169"
                     /db_xref="CDD:380946"
     Site            order(1577..1580,1597,1623..1628,1642..1647,1655..1657,
                     1666,1682..1687,1689..1692)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:380946"
     Site            order(1577..1580,1623,1643..1647,1684,1689..1692)
                     /site_type="other"
                     /note="putative SAM binding site"
                     /db_xref="CDD:380946"
     Site            order(1649,1690,1692,1697)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:380946"
     CDS             1..1707
                     /gene="SETD1A"
                     /gene_synonym="EPEDD; EPEO2; KMT2F; NEDSID; Set1; Set1A"
                     /coded_by="NM_014712.3:227..5350"
                     /db_xref="CCDS:CCDS32435.1"
                     /db_xref="GeneID:9739"
                     /db_xref="HGNC:HGNC:29010"
                     /db_xref="MIM:611052"
ORIGIN      
        1 mdqegggdgq kapsfqwrny klivdpaldp alrrpsqkvy rydgvhfsvn dskyipvedl
       61 qdprchvrsk nrdfslpvpk fkldefyigq iplkevtfar lndnvretfl kdmcrkygev
      121 eeveillhpr trkhlglarv lftstrgake tvknlhltsv mgniihaqld ikgqqrmkyy
      181 elivngsytp qtvptggkal sekfqgsgaa tetaesrrrs ssdtaaypag ttavgtpgng
      241 tpcsqdtsfs ssrqdtpssf gqftpqssqg tpytsrgstp ysqdsaysss ttstsfkprr
      301 sensyqdafs rrhfsassas ttastaiaat taatasssas ssslssssss sssssssqfr
      361 ssdanypayy eswnryqrht sypprratre eppgapfaen taerfppsyt sylppepsrp
      421 tdqdyrppas eapppeppep ggggggggps pereevrtsp rpasparsgs papettnesv
      481 pfaqhsslds riemllkeqr skfsflasdt eeeeenssmv lgardtgsev psgsghgpct
      541 pppapanfed vaptgsgepg atrespkang qnqaspcssg ddmeisdddr ggspppaptp
      601 pqqppppppp ppppppylas lplgypphqp ayllpprpdg ppppeypppp pppphiydfv
      661 nslelmdrlg aqwggmpmsf qmqtqmltrl hqlrqgkgli aasagppgga fgeaflpfpp
      721 pqeaayglpy alyaqgqegr gaysreayhl pmpmaaeplp sssvsgeear lppreeaela
      781 egktlptagt vgrvlamlvq emksimqrdl nrkmvenvaf gafdqwwesk eekakpfqna
      841 akqqakeedk ektklkepgl lslvdwaksg gttgieafaf gsglrgalrl psfkvkrkep
      901 seiseaseek rprpstpaee deddpeqeke agepgrpgtk ppkrdeergk tqgkhrksfa
      961 ldsegeeasq esssekdeed deedeededr eeavdttkke tevsdgedee sdssskcsly
     1021 adsdgendst sdsessssss ssssssssss sssssssses ssedeeeeer paalpsaspp
     1081 prevpvptpa pvevpvperv agspvtplpe qeasparpag pteesppsap lrppeppagp
     1141 papaprpder psspipllpp pkkrrktvsf saievvpape pppatppqak fpgpasrkap
     1201 rgvertirnl pldhaslvks wpeevsrggr sraggrgrlt eeeeaepgte vdlavladla
     1261 ltparrglpa lpavedseat etsdeaerpr pllshilleh nyalavkptp papalrppep
     1321 vpapaalfss padevleape vvvaeaeepk pqqlqqqree geeegeeege eeeeessdss
     1381 sssdgegalr rrslrsharr rrpppppppp pprayeprse feqmtilydi wnsgldsedm
     1441 sylrltyerl lqqtsgadwl ndthwvhhti tnlttpkrkr rpqdgprehq tgsarsegyy
     1501 piskkekdky ldvcpvsarq legvdtqgtn rvlserrseq rrllsaigts aimdsdllkl
     1561 nqlkfrkkkl rfgrsrihew glfamepiaa demvieyvgq nirqmvadmr ekryvqegig
     1621 ssylfrvdhd tiidatkcgn larfinhcct pncyakviti esqkkiviys kqpigvdeei
     1681 tydykfpled nkipclcgte scrgsln
//
LOCUS       NP_001015056             513 aa            linear   PRI 20-NOV-2025
DEFINITION  rhotekin isoform c [Homo sapiens].
ACCESSION   NP_001015056
VERSION     NP_001015056.1
DBSOURCE    REFSEQ: accession NM_001015056.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Li,B., Chen,P., Chang,Y., Qi,J., Fu,H. and Guo,H.
  TITLE     Let-7a inhibits tumor cell growth and metastasis by directly
            targeting RTKN in human colon cancer
  JOURNAL   Biochem Biophys Res Commun 478 (2), 739-745 (2016)
   PUBMED   27498032
  REMARK    GeneRIF: Let-7a microRNA inhibits tumor cell growth and metastasis
            by directly targeting RTKN in human colon cancer.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Katoh,H. and Negishi,M.
  TITLE     RhoG activates Rac1 by direct interaction with the Dock180-binding
            protein Elmo
  JOURNAL   Nature 424 (6947), 461-464 (2003)
   PUBMED   12879077
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Sharfe,N., Freywald,A., Toro,A., Dadi,H. and Roifman,C.
  TITLE     Ephrin stimulation modulates T cell chemotaxis
  JOURNAL   Eur J Immunol 32 (12), 3745-3755 (2002)
   PUBMED   12516569
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Reynaud,C., Fabre,S. and Jalinot,P.
  TITLE     The PDZ protein TIP-1 interacts with the Rho effector rhotekin and
            is involved in Rho signaling to the serum response element
  JOURNAL   J Biol Chem 275 (43), 33962-33968 (2000)
   PUBMED   10940294
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Fu,Q., Yu,L., Liu,Q., Zhang,J., Zhang,H. and Zhao,S.
  TITLE     Molecular cloning, expression characterization, and mapping of a
            novel putative inhibitor of rho GTPase activity, RTKN, to
            D2S145-D2S286
  JOURNAL   Genomics 66 (3), 328-332 (2000)
   PUBMED   10873388
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Jang,W., Weber,J.S., Harkins,E.B. and Meisler,M.H.
  TITLE     Localization of the rhotekin gene RTKN on the physical maps of
            mouse chromosome 6 and human chromosome 2p13 and exclusion as a
            candidate for mnd2 and LGMD2B
  JOURNAL   Genomics 40 (3), 506-507 (1997)
   PUBMED   9073523
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AW410753.1, BQ721791.1,
            BC017727.1 and BQ574374.1.
            
            Summary: This gene encodes a scaffold protein that interacts with
            GTP-bound Rho proteins. Binding of this protein inhibits the GTPase
            activity of Rho proteins. This protein may interfere with the
            conversion of active, GTP-bound Rho to the inactive GDP-bound form
            by RhoGAP. Rho proteins regulate many important cellular processes,
            including cytokinesis, transcription, smooth muscle contraction,
            cell growth and transformation. Dysregulation of the Rho signal
            transduction pathway has been implicated in many forms of cancer.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region and uses a downstream start codon, compared to
            variant 1. The encoded protein (isoform c) is shorter than isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF290512.1, SRR1803617.69040.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..513
                     /product="rhotekin isoform c"
                     /calculated_mol_wt=56535
     Region          <1..41
                     /region_name="HR1"
                     /note="Protein kinase C-related kinase homology region 1
                     (HR1) domain that binds Rho family small GTPases; cl00087"
                     /db_xref="CDD:469609"
     Region          67..220
                     /region_name="Anillin"
                     /note="Cell division protein anillin; pfam08174"
                     /db_xref="CDD:462393"
     Region          259..369
                     /region_name="PH_rhotekin2"
                     /note="Anillin Pleckstrin homology (PH) domain; cd13249"
                     /db_xref="CDD:270069"
     CDS             1..513
                     /gene="RTKN"
                     /gene_synonym="RTKN-1"
                     /coded_by="NM_001015056.1:271..1812"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42699.1"
                     /db_xref="GeneID:6242"
                     /db_xref="HGNC:HGNC:10466"
                     /db_xref="MIM:602288"
ORIGIN      
        1 mregacklla acsqreqale atksllvcns rilsymgelq rrkeaqvlgk tsrrpsdsgp
       61 paerspcrgr vcisdlripl mwkdteyfkn kgdlhrwavf lllqlgehiq dtemilvdrt
      121 ltdisfqsnv lfaeagpdfe lrlelygacv eeegaltggp krlatklsss lgrssgrrvr
      181 asldsaggsg sspillptpv vggpryhlla httltlaavq dgfrthdltl asheenpawl
      241 plygsvccrl aaqplcmtqp tasgtlrvqq agemqnwaqv hgvlkgtnlf cyrqpedadt
      301 geeplltiav nketrvrage ldqalgrpft lsisnqygdd evthtlqtes realqswmea
      361 lwqlffdmsq wkqccdeimk ietpaprkpp qalakqgsly hemaiepldd iaavtdiltq
      421 regarletpp pwlamftdqp alpnpcspas vapapdwthp lpwgrprtfs ldavppdhsp
      481 rarsvaplpp qrsprtrglc skgqprtwlq spv
//
LOCUS       NP_001354571             780 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform m [Homo sapiens].
ACCESSION   NP_001354571
VERSION     NP_001354571.1
DBSOURCE    REFSEQ: accession NM_001367642.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.136764.1,
                                           SRR1660807.135922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..780
                     /product="SUN domain-containing protein 1 isoform m"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=86638
     Region          62..286
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <360..>584
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          412..465
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(412,415..416,419,422..423,426..427,429..430,
                     433..434,436..437,440..441,443..444,447,450..451,454,
                     457..458,461..462,464..465)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          542..600
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          643..778
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..780
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367642.1:52..2394"
                     /note="isoform m is encoded by transcript variant 13"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv revlredghl
      241 svngealwka asgvfwwlgi gwyqfvtlis wlnvflltrc lrnickflvl liplflllag
      301 lslrgqgnff sflpvlnwas mhrtqrvddp qdvfkpttsr lkqplqgdse afpwhwmsgv
      361 eqqvaslsgq chhhgenlre lttllqklqa rvdqmeggaa gpsasvrdav gqppretdfm
      421 afhqehevrm shledilgkl rekseaiqke leqtkqktis avgeqllptv ehlqleldql
      481 kselsswrhv ktgcetvdav qervdvqvre mvkllfsedq qggsleqllq rfssqfvskg
      541 dlqtmlrdlq lqilrnvthh vsvtkqlpts eavvsavsea gasgiteaqa raivnsalkl
      601 ysqdktgmvd falesgggsi lstrcsetye tktalmslfg iplwyfsqsp rvviqpdiyp
      661 gncwafkgsq gylvvrlsmm ihpaaftleh ipktlsptgn issapkdfav ygleneyqee
      721 gqllgqftyd qdgeslqmfq alkrpddtaf qivelrifsn wghpeytcly rfrvhgepvk
//
LOCUS       NP_680544                163 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p25-like protein [Homo sapiens].
ACCESSION   NP_680544
VERSION     NP_680544.1
DBSOURCE    REFSEQ: accession NM_148178.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Rosenblad,M.A., Lopez,M.D., Piccinelli,P. and Samuelsson,T.
  TITLE     Inventory and analysis of the protein subunits of the ribonucleases
            P and MRP provides further evidence of homology between the yeast
            and human enzymes
  JOURNAL   Nucleic Acids Res 34 (18), 5145-5156 (2006)
   PUBMED   16998185
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL528391.3 and BC032136.2.
            
            Summary: This gene encodes a protein that appears to belong to a
            family of evolutionarily related proteins (DUF78), that may share
            one or more domains in common. Members of this family are small
            archaebacterial proteins with no known function. Alternative
            splicing has been observed at this locus and two variants, both
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript. Variants 1 and 2 encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.120323.1, AL528391.3
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465413 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378959.9/ ENSP00000368242.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..163
                     /product="ribonuclease P protein subunit p25-like protein"
                     /note="alba-like protein C9orf23; rpp25-like protein;
                     RNase P protein subunit-like p25; ribonuclease P/MRP 25kDa
                     subunit-like"
                     /calculated_mol_wt=17500
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5L8.1)"
     Region          27..89
                     /region_name="Alba"
                     /note="pfam01918"
                     /db_xref="CDD:426509"
     Region          129..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5L8.1)"
     CDS             1..163
                     /gene="RPP25L"
                     /gene_synonym="bA296L22.5; C9orf23"
                     /coded_by="NM_148178.3:71..562"
                     /db_xref="CCDS:CCDS6559.1"
                     /db_xref="GeneID:138716"
                     /db_xref="HGNC:HGNC:19909"
ORIGIN      
        1 mehyrkagsv elpapspmpq lppdtlemrv rdgskirnll glalgrlegg sarhvvfsgs
       61 graagkavsc aeivkrrvpg lhqltklrfl qtedswvpas pdtgldpltv rrhvpavwvl
      121 lsrdpldpne cgyqppgapp glgsmpsssc gprsrrrard trs
//
LOCUS       NP_059990                860 aa            linear   PRI 20-NOV-2025
DEFINITION  M-phase phosphoprotein 8 [Homo sapiens].
ACCESSION   NP_059990 XP_167894
VERSION     NP_059990.2
DBSOURCE    REFSEQ: accession NM_017520.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Nikolopoulos,N., Oda,S.I., Prigozhin,D.M. and Modis,Y.
  TITLE     Structure and Methyl-lysine Binding Selectivity of the HUSH Complex
            Subunit MPP8
  JOURNAL   J Mol Biol 437 (2), 168890 (2025)
   PUBMED   39638237
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Li,T., Li,N., Wang,L., Li,J. and Zhang,X.
  TITLE     MPP8 Promotes Proliferation and Restrains Apoptosis in Osteosarcoma
            by Regulating p38alphaMAPK Pathway
  JOURNAL   Technol Cancer Res Treat 20, 1533033821995272 (2021)
   PUBMED   33596786
  REMARK    GeneRIF: MPP8 Promotes Proliferation and Restrains Apoptosis in
            Osteosarcoma by Regulating p38alphaMAPK Pathway.
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Kokura,K., Sun,L., Bedford,M.T. and Fang,J.
  TITLE     Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing
            and promotes tumour cell motility and invasion
  JOURNAL   EMBO J 29 (21), 3673-3687 (2010)
   PUBMED   20871592
  REMARK    GeneRIF: MPP8 mediates E-cadherin gene silencing and promotes
            breast tumour cell motility and invasion.
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Maksimov,V.V., Arman,I.P. and Tarantul,V.Z.
  TITLE     [Identification of the proteins interacting with neuroprotective
            peptide humanin in a yeast two-hybrid system]
  JOURNAL   Genetika 42 (2), 274-277 (2006)
   PUBMED   16583711
REFERENCE   8  (residues 1 to 860)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   9  (residues 1 to 860)
  AUTHORS   Umeda,M., Nishitani,H. and Nishimoto,T.
  TITLE     A novel nuclear protein, Twa1, and Muskelin comprise a complex with
            RanBPM
  JOURNAL   Gene 303, 47-54 (2003)
   PUBMED   12559565
REFERENCE   10 (residues 1 to 860)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA672302.1, BC003542.1, AL354808.24 and R60056.1.
            
            On or before Jan 24, 2004 this sequence version replaced
            XP_167894.1, NP_059990.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.262443.1, BC003542.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361479.10/ ENSP00000355388.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..860
                     /product="M-phase phosphoprotein 8"
                     /EC_number="2.4.2.30"
                     /note="M-phase phosphoprotein, mpp8; two hybrid-associated
                     protein 3 with RanBPM"
                     /calculated_mol_wt=97051
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          58..108
                     /region_name="CD_MMP8"
                     /note="chromodomain of M-phase phosphoprotein 8; cd18633"
                     /db_xref="CDD:349283"
     Site            order(58..61,80,83,89,91,95..96,98..102)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349283"
     Site            59
                     /site_type="other"
                     /note="Interaction with histone H3K9me3.
                     /evidence=ECO:0000269|PubMed:21419134; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          80..87
                     /region_name="Histone H3K9me3 binding.
                     /evidence=ECO:0000269|PubMed:21419134"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          129..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          <200..>550
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          206..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TYA6; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000305|PubMed:23416073; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          431..560
                     /region_name="Interaction with humanin.
                     /evidence=ECO:0000269|PubMed:23532874"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99549.2)"
     Region          458..496
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          485..746
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(600,602,606..607,610..612,614..615,619,622,631,633,
                     635,639..640,643..645,647..648,652,655,664,666,668,
                     672..673,676..678,680..681,685,688)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          600..631
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          600..629
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          633..664
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..662
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          666..695
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          666..695
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     Region          699..728
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99549.2)"
     CDS             1..860
                     /gene="MPHOSPH8"
                     /gene_synonym="HSMPP8; mpp8; TWA3"
                     /coded_by="NM_017520.4:91..2673"
                     /db_xref="CCDS:CCDS9287.1"
                     /db_xref="GeneID:54737"
                     /db_xref="HGNC:HGNC:29810"
                     /db_xref="MIM:611626"
ORIGIN      
        1 meqvaegarv tavpvsaads teelaeveeg vgvvgednda aargaeafgd seedgedvfe
       61 vekildmkte ggkvlykvrw kgytsdddtw epeihledck evllefrkki aenkakavrk
      121 diqrlslnnd ifeansdsdq qsetkedtsp kkkkkklrqr eekspddlkk kkakagklkd
      181 kskpdlessl eslvfdlrtk kriseakeel keskkpkkde vketkelkkv kkgeirdlkt
      241 ktredpkenr ktkkekfves qvesessvln dspfpeddse glhsdsreek qntksarera
      301 gqdmglehgf ekpldsamsa eedtdvrgrr kkktprkaed trenrklenk naflekktvp
      361 kkqrnqdrsk saaeleklmp vsaqtpkgrr lsgeerglws tdsaeedket krneskekyq
      421 krhdsdkeek grkepkglkt lkeirnafdl fkltpeeknd vsennrkree ipldfktidd
      481 hktkenkqsl kerrntrdet dtwayiaaeg dqevldsvcq adensdgrqq ilslgmdlql
      541 ewmkledfqk hldgkdenfa atdaipsnvl rdavkngdyi tvkvalnsne eynldqedss
      601 gmtlvmlaaa ggqddllrll itkgakvngr qkngttalih aaeknflttv ailleagafv
      661 nvqqsngeta lmkackrgns divrlviecg adcnilskhq nsalhfakqs nnvlvydllk
      721 nhletlsrva eetikdyfea rlallepvfp iachrlcegp dfstdfnykp pqnipegsgi
      781 llfifhanfl gkeviarlcg pcsvqavvln dkfqlpvfld shfvysfspv agpnklfirl
      841 teapsakvkl ligayrvqlq
//
LOCUS       NP_000381                653 aa            linear   PRI 20-NOV-2025
DEFINITION  rab proteins geranylgeranyltransferase component A 1 isoform a
            [Homo sapiens].
ACCESSION   NP_000381
VERSION     NP_000381.1
DBSOURCE    REFSEQ: accession NM_000390.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Sarkar,H., Tracey-White,D., Hagag,A.M., Burgoyne,T., Nair,N.,
            Jensen,L.D., Edwards,M.M. and Moosajee,M.
  TITLE     Loss of REP1 impacts choroidal melanogenesis and vasculogenesis in
            choroideremia
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166963 (2024)
   PUBMED   37989423
  REMARK    GeneRIF: Loss of REP1 impacts choroidal melanogenesis and
            vasculogenesis in choroideremia.
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Iwagawa,T., Masumoto,H., Tabuchi,H., Tani,K., Conklin,B.R. and
            Watanabe,S.
  TITLE     Evaluation of CRISPR/Cas9 exon-skipping vector for choroideremia
            using human induced pluripotent stem cell-derived RPE
  JOURNAL   J Gene Med 25 (2), e3464 (2023)
   PUBMED   36413603
  REMARK    GeneRIF: Evaluation of CRISPR/Cas9 exon-skipping vector for
            choroideremia using human induced pluripotent stem cell-derived
            RPE.
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 653)
  AUTHORS   van Bokhoven,H., van den Hurk,J.A., Bogerd,L., Philippe,C.,
            Gilgenkrantz,S., de Jong,P., Ropers,H.H. and Cremers,F.P.
  TITLE     Cloning and characterization of the human choroideremia gene
  JOURNAL   Hum Mol Genet 3 (7), 1041-1046 (1994)
   PUBMED   7981670
REFERENCE   6  (residues 1 to 653)
  AUTHORS   MacDonald,I.M., Hume,S., Zhai,Y. and Xu,M.
  TITLE     Choroideremia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301511
REFERENCE   7  (residues 1 to 653)
  AUTHORS   van den Hurk,J.A., van de Pol,T.J., Molloy,C.M., Brunsmann,F.,
            Ruther,K., Zrenner,E., Pinckers,A.J., Pawlowitzki,I.H.,
            Bleeker-Wagemakers,E.M., Wieringa,B. et al.
  TITLE     Detection and characterization of point mutations in the
            choroideremia candidate gene by PCR-SSCP analysis and direct DNA
            sequencing
  JOURNAL   Am J Hum Genet 50 (6), 1195-1202 (1992)
   PUBMED   1598901
REFERENCE   8  (residues 1 to 653)
  AUTHORS   Sankila,E.M., Tolvanen,R., van den Hurk,J.A., Cremers,F.P. and de
            la Chapelle,A.
  TITLE     Aberrant splicing of the CHM gene is a significant cause of
            choroideremia
  JOURNAL   Nat Genet 1 (2), 109-113 (1992)
   PUBMED   1302003
REFERENCE   9  (residues 1 to 653)
  AUTHORS   Molloy,C.M., van de Pol,T.J., Brohet,R.M., Ropers,H.H. and
            Cremers,F.P.
  TITLE     Three RFLPs for pZ11 (DXS540) in the choroideremia gene at Xq21.2
  JOURNAL   Nucleic Acids Res 20 (6), 1434 (1992)
   PUBMED   1373238
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Merry,D.E., Janne,P.A., Landers,J.E., Lewis,R.A. and Nussbaum,R.L.
  TITLE     Isolation of a candidate gene for choroideremia
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2135-2139 (1992)
   PUBMED   1549574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X78121.1, AK291160.1,
            AL022401.2 and BU688880.1.
            
            Summary: This gene encodes component A of the RAB geranylgeranyl
            transferase holoenzyme. In the dimeric holoenzyme, this subunit
            binds unprenylated Rab GTPases and then presents them to the
            catalytic Rab GGTase subunit for the geranylgeranyl transfer
            reaction. Rab GTPases need to be geranylgeranyled on either one or
            two cysteine residues in their C-terminus to localize to the
            correct intracellular membrane. Mutations in this gene are a cause
            of choroideremia; also known as tapetochoroidal dystrophy (TCD).
            This X-linked disease is characterized by progressive dystrophy of
            the choroid, retinal pigment epithelium and retina. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.341389.1,
                                           SRR14038191.932767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357749.7/ ENSP00000350386.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.2"
     Protein         1..653
                     /product="rab proteins geranylgeranyltransferase component
                     A 1 isoform a"
                     /note="rab proteins geranylgeranyltransferase component A
                     1; choroideremia (Rab escort protein 1); CHM, Rab escort
                     protein 1"
                     /calculated_mol_wt=73345
     Region          13..>54
                     /region_name="NAD_binding_8"
                     /note="NAD(P)-binding Rossmann-like domain; pfam13450"
                     /db_xref="CDD:433218"
     Region          225..542
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Region          606..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24386.3)"
     CDS             1..653
                     /gene="CHM"
                     /gene_synonym="DXS540; GGTA; HSD-32; REP-1; TCD"
                     /coded_by="NM_000390.4:27..1988"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14454.1"
                     /db_xref="GeneID:1121"
                     /db_xref="HGNC:HGNC:1940"
                     /db_xref="MIM:300390"
ORIGIN      
        1 madtlpsefd vivigtglpe siiaaacsrs grrvlhvdsr syyggnwasf sfsgllswlk
       61 eyqensdivs dspvwqdqil eneeaialsr kdktiqhvev fcyasqdlhe dveeagalqk
      121 nhalvtsans teaadsaflp tedeslstms cemlteqtps sdpenalevn gaevtgeken
      181 hcddktcvps tsaedmsenv piaedtteqp kknritysqi ikegrrfnid lvskllysrg
      241 llidlliksn vsryaefkni trilafregr veqvpcsrad vfnskqltmv ekrmlmkflt
      301 fcmeyekypd eykgyeeitf yeylktqklt pnlqyivmhs iamtsetass tidglkatkn
      361 flhclgrygn tpflfplygq gelpqcfcrm cavfggiycl rhsvqclvvd kesrkckaii
      421 dqfgqriise hflvedsyfp enmcsrvqyr qisravlitd rsvlktdsdq qisiltvpae
      481 epgtfavrvi elcsstmtcm kgtylvhltc tssktaredl esvvqklfvp ytemeieneq
      541 vekprilwal yfnmrdssdi srscyndlps nvyvcsgpdc glgndnavkq aetlfqeicp
      601 nedfcppppn pediildgds lqpeasessa ipeansetfk estnlgnlee sse
//
LOCUS       NP_001155053             369 aa            linear   PRI 20-NOV-2025
DEFINITION  POC1 centriolar protein homolog A isoform 3 [Homo sapiens].
ACCESSION   NP_001155053
VERSION     NP_001155053.1
DBSOURCE    REFSEQ: accession NM_001161581.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Li,Z.H., Li,J.Y., Wu,Z.T., Zhu,Y.J., Zhuo,T., Nong,J.S., Qian,J.,
            Peng,H.J., Dai,L., Wang,Y.Y., Chen,M.W. and Zeng,X.C.
  TITLE     Upregulation of POC1A in lung adenocarcinoma promotes tumour
            progression and predicts poor prognosis
  JOURNAL   J Cell Mol Med 28 (6), e18135 (2024)
   PUBMED   38429900
  REMARK    GeneRIF: Upregulation of POC1A in lung adenocarcinoma promotes
            tumour progression and predicts poor prognosis.
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Perge,K., Capel,E., Villanueva,C., Gautheron,J., Diallo,S.,
            Auclair,M., Rondeau,S., Morichon,R., Brioude,F., Jeru,I., Rossi,M.,
            Nicolino,M. and Vigouroux,C.
  TITLE     Ciliopathy due to POC1A deficiency: clinical and metabolic
            features, and cellular modeling
  JOURNAL   Eur J Endocrinol 190 (2), 151-164 (2024)
   PUBMED   38245004
  REMARK    GeneRIF: Ciliopathy due to POC1A deficiency: clinical and metabolic
            features, and cellular modeling.
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Zhao,Q., Gao,S., Chen,X. and Zhu,X.
  TITLE     POC1A, prognostic biomarker of immunosuppressive microenvironment
            in cancer
  JOURNAL   Aging (Albany NY) 14 (12), 5195-5210 (2022)
   PUBMED   35748773
  REMARK    GeneRIF: POC1A, prognostic biomarker of immunosuppressive
            microenvironment in cancer.
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Mericq,V., Huang-Doran,I., Al-Naqeb,D., Basaure,J., Castiglioni,C.,
            de Bruin,C., Hendriks,Y., Bertini,E., Alkuraya,F.S., Losekoot,M.,
            Al-Rubeaan,K., Semple,R.K. and Wit,J.M.
  TITLE     Biallelic POC1A variants cause syndromic severe insulin resistance
            with muscle cramps
  JOURNAL   Eur J Endocrinol 186 (5), 543-552 (2022)
   PUBMED   35234134
  REMARK    GeneRIF: Biallelic POC1A variants cause syndromic severe insulin
            resistance with muscle cramps.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Sarig,O., Nahum,S., Rapaport,D., Ishida-Yamamoto,A.,
            Fuchs-Telem,D., Qiaoli,L., Cohen-Katsenelson,K., Spiegel,R.,
            Nousbeck,J., Israeli,S., Borochowitz,Z.U., Padalon-Brauch,G.,
            Uitto,J., Horowitz,M., Shalev,S. and Sprecher,E.
  TITLE     Short stature, onychodysplasia, facial dysmorphism, and
            hypotrichosis syndrome is caused by a POC1A mutation
  JOURNAL   Am J Hum Genet 91 (2), 337-342 (2012)
   PUBMED   22840363
  REMARK    GeneRIF: Short stature, onychodysplasia, facial dysmorphism, and
            hypotrichosis syndrome is caused by a POC1A mutation.
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Pearson,C.G., Osborn,D.P., Giddings,T.H. Jr., Beales,P.L. and
            Winey,M.
  TITLE     Basal body stability and ciliogenesis requires the conserved
            component Poc1
  JOURNAL   J Cell Biol 187 (6), 905-920 (2009)
   PUBMED   20008567
REFERENCE   9  (residues 1 to 369)
  AUTHORS   Keller,L.C., Geimer,S., Romijn,E., Yates,J. 3rd, Zamora,I. and
            Marshall,W.F.
  TITLE     Molecular architecture of the centriole proteome: the conserved
            WD40 domain protein POC1 is required for centriole duplication and
            length control
  JOURNAL   Mol Biol Cell 20 (4), 1150-1166 (2009)
   PUBMED   19109428
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Hames,R.S., Hames,R., Prosser,S.L., Euteneuer,U., Lopes,C.A.,
            Moore,W., Woodland,H.R. and Fry,A.M.
  TITLE     Pix1 and Pix2 are novel WD40 microtubule-associated proteins that
            colocalize with mitochondria in Xenopus germ plasm and centrosomes
            in human cells
  JOURNAL   Exp Cell Res 314 (3), 574-589 (2008)
   PUBMED   18068700
  REMARK    GeneRIF: Based on these data, we propose that Pix1 and Pix2 are
            microtubule-associated adaptor proteins that likely contribute to a
            range of developmental and cell division processes.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC110877.1, BC119693.2,
            CA944751.1 and AC115284.4.
            
            Summary: POC1 proteins contain an N-terminal WD40 domain and a
            C-terminal coiled coil domain and are part of centrosomes. They
            play an important role in basal body and cilia formation. This gene
            encodes one of the two POC1 proteins found in humans. Mutations in
            this gene result in short stature, onychodysplasia, facial
            dysmorphism, and hypotrichosis (SOFT) syndrome. [provided by
            RefSeq, Sep 2012].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region compared to variant 1 and initiates translation at an
            in-frame downstream AUG. The encoded isoform (3) has a shorter
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC119693.2, SRR18074969.2294682.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..369
                     /product="POC1 centriolar protein homolog A isoform 3"
                     /note="WD repeat domain 51A; WD repeat-containing protein
                     51A; POC1 centriolar protein homolog A; proteome of
                     centriole protein 1A"
                     /calculated_mol_wt=40805
     Region          <2..260
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          26..63
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          69..105
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          110..146
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          153..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          194..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..369
                     /gene="POC1A"
                     /gene_synonym="PIX2; SOFT; WDR51A"
                     /coded_by="NM_001161581.2:237..1346"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54591.1"
                     /db_xref="GeneID:25886"
                     /db_xref="HGNC:HGNC:24488"
                     /db_xref="MIM:614783"
ORIGIN      
        1 mdsclmvwhm kpqsrayrft ghkdavtcvn fspsghllas gsrdktvriw vpnvkgestv
       61 frahtatvrs vhfcsdgqsf vtasddktvk vwathrqkfl fslsqhinwv rcakfspdgr
      121 livsasddkt vklwdkssre cvhsycehgg fvtyvdfhps gtciaaagmd ntvkvwdvrt
      181 hrllqhyqlh saavnglsfh psgnylitas sdstlkildl megrllytlh ghqgpattva
      241 fsrtgeyfas ggsdeqvmvw ksnfdivdhg evtkvprppa tlassmgnlp evdfpvppgr
      301 grsvesvqsq pqepvsvpqt ltstlehivg qldvltqtvs ileqrltlte dklkqclenq
      361 qlimqratp
//
LOCUS       NP_001273769             599 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD finger protein 19 isoform c [Homo sapiens].
ACCESSION   NP_001273769 XP_005251962
VERSION     NP_001273769.1
DBSOURCE    REFSEQ: accession NM_001286840.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Johnson,T.S., Sudha,P., Liu,E., Becker,N., Robertson,S., Blaney,P.,
            Morgan,G., Chopra,V.S., Dos Santos,C., Nixon,M., Huang,K.,
            Suvannasankha,A., Zaid,M.A., Abonour,R. and Walker,B.A.
  TITLE     1q amplification and PHF19 expressing high-risk cells are
            associated with relapsed/refractory multiple myeloma
  JOURNAL   Nat Commun 15 (1), 4144 (2024)
   PUBMED   38755140
  REMARK    GeneRIF: 1q amplification and PHF19 expressing high-risk cells are
            associated with relapsed/refractory multiple myeloma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Xu,Y., Liu,W., Jiang,X., Li,J., Liu,Q., Su,F., Ruan,S., Zhang,Z.
            and Tao,F.
  TITLE     Regulation of hPCL3 isoforms' ubiquitination by TRIM21 in non-small
            cell lung cancer progression
  JOURNAL   Life Sci Alliance 6 (10), e202302060 (2023)
   PUBMED   37507137
  REMARK    GeneRIF: Regulation of hPCL3 isoforms' ubiquitination by TRIM21 in
            non-small cell lung cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Xiaoyun,S., Yuyuan,Z., Jie,X., Yingjie,N., Qing,X., Yuezhen,D. and
            Haiguang,X.
  TITLE     PHF19 activates hedgehog signaling and promotes tumorigenesis in
            hepatocellular carcinoma
  JOURNAL   Exp Cell Res 406 (1), 112690 (2021)
   PUBMED   34129846
  REMARK    GeneRIF: PHF19 activates hedgehog signaling and promotes
            tumorigenesis in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Li,Y., Gong,J. and Zhang,L.
  TITLE     PHD finger protein 19 expression in multiple myeloma: Association
            with clinical features, induction therapy outcome, disease
            progression, and survival
  JOURNAL   J Clin Lab Anal 35 (9), e23910 (2021)
   PUBMED   34390275
  REMARK    GeneRIF: PHD finger protein 19 expression in multiple myeloma:
            Association with clinical features, induction therapy outcome,
            disease progression, and survival.
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Ghislin,S., Deshayes,F., Middendorp,S., Boggetto,N. and
            Alcaide-Loridan,C.
  TITLE     PHF19 and Akt control the switch between proliferative and invasive
            states in melanoma
  JOURNAL   Cell Cycle 11 (8), 1634-1645 (2012)
   PUBMED   22487681
  REMARK    GeneRIF: PHF19 silencing reduces the cell proliferation rate and
            increases the transendothelial migration capacities of melanoma
            cell lines.
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Boulay,G., Rosnoblet,C., Guerardel,C., Angrand,P.O. and Leprince,D.
  TITLE     Functional characterization of human Polycomb-like 3 isoforms
            identifies them as components of distinct EZH2 protein complexes
  JOURNAL   Biochem J 434 (2), 333-342 (2011)
   PUBMED   21143197
  REMARK    GeneRIF: Functional characterization of human Polycomb-like 3
            isoforms identifies them as components of distinct EZH2 protein
            complexes
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Zhernakova,A., Stahl,E.A., Trynka,G., Raychaudhuri,S., Festen,E.A.,
            Franke,L., Westra,H.J., Fehrmann,R.S., Kurreeman,F.A., Thomson,B.,
            Gupta,N., Romanos,J., McManus,R., Ryan,A.W., Turner,G., Brouwer,E.,
            Posthumus,M.D., Remmers,E.F., Tucci,F., Toes,R., Grandone,E.,
            Mazzilli,M.C., Rybak,A., Cukrowska,B., Coenen,M.J., Radstake,T.R.,
            van Riel,P.L., Li,Y., de Bakker,P.I., Gregersen,P.K.,
            Worthington,J., Siminovitch,K.A., Klareskog,L., Huizinga,T.W.,
            Wijmenga,C. and Plenge,R.M.
  TITLE     Meta-analysis of genome-wide association studies in celiac disease
            and rheumatoid arthritis identifies fourteen non-HLA shared loci
  JOURNAL   PLoS Genet 7 (2), e1002004 (2011)
   PUBMED   21383967
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Gregersen,P.K., Amos,C.I., Lee,A.T., Lu,Y., Remmers,E.F.,
            Kastner,D.L., Seldin,M.F., Criswell,L.A., Plenge,R.M., Holers,V.M.,
            Mikuls,T.R., Sokka,T., Moreland,L.W., Bridges,S.L. Jr., Xie,G.,
            Begovich,A.B. and Siminovitch,K.A.
  TITLE     REL, encoding a member of the NF-kappaB family of transcription
            factors, is a newly defined risk locus for rheumatoid arthritis
  JOURNAL   Nat Genet 41 (7), 820-823 (2009)
   PUBMED   19503088
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Wang,S., Robertson,G.P. and Zhu,J.
  TITLE     A novel human homologue of Drosophila polycomblike gene is
            up-regulated in multiple cancers
  JOURNAL   Gene 343 (1), 69-78 (2004)
   PUBMED   15563832
  REMARK    GeneRIF: identification of a gene encoding a human homologue of the
            Drosophila polycomblike protein, hPCL3 gene, encoding two nuclear
            proteins, hPCL3S and hPCL3L; markedly overexpressed in many types
            of cancers
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX640713.1, AK303433.1, BC044224.1, BU632411.1 and AI193743.1.
            
            On Nov 15, 2013 this sequence version replaced XP_005251962.1.
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640713.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..599
                     /product="PHD finger protein 19 isoform c"
                     /note="polycomb like 3; polycomb-like protein 3; tudor
                     domain containing 19B"
                     /calculated_mol_wt=67516
     Region          58..114
                     /region_name="Tudor_PHF19"
                     /note="Tudor domain found in PHD finger protein1 (PHF19)
                     and similar proteins; cd20451"
                     /db_xref="CDD:410522"
     Site            order(66,68..69,71..76,93..97,99,107..108,111..114)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410522"
     Region          117..169
                     /region_name="PHD1_PHF19"
                     /note="PHD finger 1 found in PHD finger protein 19
                     (PHF19); cd15579"
                     /db_xref="CDD:277054"
     Site            order(117,131..135,139,162)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277054"
     Region          216..267
                     /region_name="PHD2_PHF19"
                     /note="PHD finger 2 found in PHD finger protein 19
                     (PHF19); cd15581"
                     /db_xref="CDD:277056"
     Site            order(216,228..232,236,260)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277056"
     Region          550..597
                     /region_name="Mtf2_C"
                     /note="Polycomb-like MTF2 factor 2; pfam14061"
                     /db_xref="CDD:464077"
     CDS             1..599
                     /gene="PHF19"
                     /gene_synonym="MTF2L1; PCL3; TDRD19B"
                     /coded_by="NM_001286840.1:68..1867"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75889.1"
                     /db_xref="GeneID:26147"
                     /db_xref="HGNC:HGNC:24566"
                     /db_xref="MIM:609740"
ORIGIN      
        1 mlvlvirgpy psaqcqgklm enraldpgtr dsygatshlp nkgalakvkn nfkdlmsklt
       61 egqyvlcrwt dglyylgkik rvssskqscl vtfednskyw vlwkdiqhag vpgeepkcni
      121 clgktsgpln eilicgkcgl gyhqqchipi agsadqpllt pwfcrrcifa lavrkggalk
      181 kgaiartlqa vkmvlsyqpe elewdsphrt nqqqcycycg gpgewylrml qcyrcrqwfh
      241 eactqclnep mmfgdrfylf fcsvcnqgpe yierlplrwv dvvhlalynl gvqskkkyfd
      301 feeilafvnh hwellqlgkl tstpvtdrgp hllnalnsyk srflcgkeik kkkcifrlri
      361 rvppnppgkl lpdkgllpne nsasselrkr gkskpgllph efqqqkrrvy rrkrskflle
      421 daipssdfts awstnhhlas ifdftldeiq slksassgqt ffsdvdstda astsgsasts
      481 lsydsrwtvg srkrklaaka ymplrakrwa aeldgrcpsd ssaegasvpe rpdegidsht
      541 fesiseddss lshlkssitn yfgaagrlac gekyqvlarr vtpegkvqyl vewegttpy
//
LOCUS       NP_001357155             189 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 E2 isoform 2 [Homo sapiens].
ACCESSION   NP_001357155 XP_005265490
VERSION     NP_001357155.1
DBSOURCE    REFSEQ: accession NM_001370226.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Hong,X., Ma,N., Li,D., Zhang,M., Dong,W., Huang,J., Ci,X. and
            Zhang,S.
  TITLE     UBE2E2 enhances Snail-mediated epithelial-mesenchymal transition
            and Nrf2-mediated antioxidant activity in ovarian cancer
  JOURNAL   Cell Death Dis 14 (2), 100 (2023)
   PUBMED   36765041
  REMARK    GeneRIF: UBE2E2 enhances Snail-mediated epithelial-mesenchymal
            transition and Nrf2-mediated antioxidant activity in ovarian
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Pringa,E., Martinez-Noel,G., Muller,U. and Harbers,K.
  TITLE     Interaction of the ring finger-related U-box motif of a nuclear dot
            protein with ubiquitin-conjugating enzymes
  JOURNAL   J Biol Chem 276 (22), 19617-19623 (2001)
   PUBMED   11274149
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Moynihan,T.P., Ardley,H.C., Nuber,U., Rose,S.A., Jones,P.F.,
            Markham,A.F., Scheffner,M. and Robinson,P.A.
  TITLE     The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with
            RING finger/IBR motif-containing domains of HHARI and H7-AP1
  JOURNAL   J Biol Chem 274 (43), 30963-30968 (1999)
   PUBMED   10521492
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Kimura,M., Hattori,T., Matsuda,Y., Yoshioka,T., Sumi,N., Umeda,Y.,
            Nakashima,S. and Okano,Y.
  TITLE     cDNA cloning, characterization, and chromosome mapping of UBE2E2
            encoding a human ubiquitin-conjugating E2 enzyme
  JOURNAL   Cytogenet Cell Genet 78 (2), 107-111 (1997)
   PUBMED   9371400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135966.2 and AC092038.3.
            
            On May 2, 2019 this sequence version replaced XP_005265490.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..189
                     /product="ubiquitin-conjugating enzyme E2 E2 isoform 2"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-conjugating enzyme E2E 2 (homologous to
                     yeast UBC4/5); ubiquitin-conjugating enzyme E2E 2 (UBC4/5
                     homolog, yeast); ubiquitin-protein ligase E2; ubiquitin
                     carrier protein E2; E2 ubiquitin-conjugating enzyme E2;
                     ubiquitin conjugating enzyme E2E 2"
                     /calculated_mol_wt=20664
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Region          58..171
                     /region_name="UBCc_UEV"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain/ubiquitin E2 variant (UEV) domain; cl49610"
                     /db_xref="CDD:483950"
     CDS             1..189
                     /gene="UBE2E2"
                     /gene_synonym="UBCH8"
                     /coded_by="NM_001370226.1:170..739"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:7325"
                     /db_xref="HGNC:HGNC:12478"
                     /db_xref="MIM:602163"
ORIGIN      
        1 msteaqrvdd spstsggssd gdqresvqqe pereqvqpkk kegkisskta aklstsakri
       61 qkelaeitld pppncsagpk gdniyewrst ilgppgsvye ggvfflditf spdypfkppk
      121 vtfrtriyhc ninsqgvicl dilkdnwspa ltiskvllsi cslltdcnpg dfeawpalpp
      181 sqlkwnllp
//
LOCUS       NP_002701                323 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase PP1-gamma catalytic subunit
            isoform 1 [Homo sapiens].
ACCESSION   NP_002701
VERSION     NP_002701.1
DBSOURCE    REFSEQ: accession NM_002710.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Feng,P., Wang,Y., Liu,N., Chen,Y., Hu,Y., Huang,Z., Liu,Y.,
            Zheng,S., Jiang,T., Xiao,X., Dai,W., Huang,P. and Xia,Y.
  TITLE     High expression of PPP1CC promotes NHEJ-mediated DNA repair leading
            to radioresistance and poor prognosis in nasopharyngeal carcinoma
  JOURNAL   Cell Death Differ 31 (5), 683-696 (2024)
   PUBMED   38589496
  REMARK    GeneRIF: High expression of PPP1CC promotes NHEJ-mediated DNA
            repair leading to radioresistance and poor prognosis in
            nasopharyngeal carcinoma.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Fonodi,M., Thalwieser,Z., Csortos,C. and Boratko,A.
  TITLE     TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In
            Vitro Neuronal Differentiation
  JOURNAL   Int J Mol Sci 24 (24), 17360 (2023)
   PUBMED   38139189
  REMARK    GeneRIF: TIMAP, a Regulatory Subunit of Protein Phosphatase 1,
            Inhibits In Vitro Neuronal Differentiation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Yadav,Y., Sharma,M. and Dey,C.S.
  TITLE     PP1gamma regulates neuronal insulin signaling and aggravates
            insulin resistance leading to AD-like phenotypes
  JOURNAL   Cell Commun Signal 21 (1), 82 (2023)
   PUBMED   37085815
  REMARK    GeneRIF: PP1gamma regulates neuronal insulin signaling and
            aggravates insulin resistance leading to AD-like phenotypes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Bonsor,D.A., Alexander,P., Snead,K., Hartig,N., Drew,M.,
            Messing,S., Finci,L.I., Nissley,D.V., McCormick,F., Esposito,D.,
            Rodriguez-Viciana,P., Stephen,A.G. and Simanshu,D.K.
  TITLE     Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF
            activation and Noonan syndrome
  JOURNAL   Nat Struct Mol Biol 29 (10), 966-977 (2022)
   PUBMED   36175670
  REMARK    GeneRIF: Structure of the SHOC2-MRAS-PP1C complex provides insights
            into RAF activation and Noonan syndrome.
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Egloff,M.P., Cohen,P.T., Reinemer,P. and Barford,D.
  TITLE     Crystal structure of the catalytic subunit of human protein
            phosphatase 1 and its complex with tungstate
  JOURNAL   J Mol Biol 254 (5), 942-959 (1995)
   PUBMED   7500362
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Van Eynde,A., Wera,S., Beullens,M., Torrekens,S., Van Leuven,F.,
            Stalmans,W. and Bollen,M.
  TITLE     Molecular cloning of NIPP-1, a nuclear inhibitor of protein
            phosphatase-1, reveals homology with polypeptides involved in RNA
            processing
  JOURNAL   J Biol Chem 270 (47), 28068-28074 (1995)
   PUBMED   7499293
REFERENCE   8  (residues 1 to 323)
  AUTHORS   MacKintosh,R.W., Dalby,K.N., Campbell,D.G., Cohen,P.T., Cohen,P.
            and MacKintosh,C.
  TITLE     The cyanobacterial toxin microcystin binds covalently to
            cysteine-273 on protein phosphatase 1
  JOURNAL   FEBS Lett 371 (3), 236-240 (1995)
   PUBMED   7556599
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Norman,S.A. and Mott,D.M.
  TITLE     Molecular cloning and chromosomal localization of a human skeletal
            muscle PP-1 gamma 1 cDNA
  JOURNAL   Mamm Genome 5 (1), 41-45 (1994)
   PUBMED   8111128
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Barker,H.M., Craig,S.P., Spurr,N.K. and Cohen,P.T.
  TITLE     Sequence of human protein serine/threonine phosphatase 1 gamma and
            localization of the gene (PPP1CC) encoding it to chromosome bands
            12q24.1-q24.2
  JOURNAL   Biochim Biophys Acta 1178 (2), 228-233 (1993)
   PUBMED   8394140
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA514523.1, BC014073.2,
            X74008.1, AW575661.1 and AC144522.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the protein
            phosphatase family, PP1 subfamily. PP1 is an ubiquitous
            serine/threonine phosphatase that regulates many cellular
            processes, including cell division. It is expressed in mammalian
            cells as three closely related isoforms, alpha, beta/delta and
            gamma, which have distinct localization patterns. This gene encodes
            the gamma isozyme. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.115674.1,
                                           SRR1803616.104681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150385, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335007.10/ ENSP00000335084.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..323
                     /product="serine/threonine-protein phosphatase PP1-gamma
                     catalytic subunit isoform 1"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase PP1-gamma
                     catalytic subunit; serine/threonine phosphatase 1 gamma;
                     protein phosphatase 1C catalytic subunit; protein
                     phosphatase 1, catalytic subunit, gamma isozyme"
                     /calculated_mol_wt=36853
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P36873.1)"
     Region          8..298
                     /region_name="MPP_PP1_PPKL"
                     /note="PP1, PPKL (PP1 and kelch-like) enzymes, and related
                     proteins, metallophosphatase domain; cd07414"
                     /db_xref="CDD:277359"
     Site            order(64,66,92,96,124..125,129..130,134,173,195..197,206,
                     220..222,248,272..276)
                     /site_type="active"
                     /db_xref="CDD:277359"
     Site            order(64,66,92,124,173,248)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277359"
     Site            order(96,129..130,134,195..197,206,220..222,272..276)
                     /site_type="other"
                     /note="natural toxin binding site [chemical binding]"
                     /db_xref="CDD:277359"
     Site            order(179,181,198,203,216,225,233..234,236..238,240..242,
                     257,261,288..289,291,293,295)
                     /site_type="other"
                     /note="MYPT1 binding site [polypeptide binding]"
                     /db_xref="CDD:277359"
     Site            273
                     /site_type="inhibition"
                     /note="Inhibition by microcystin toxin binding; propagated
                     from UniProtKB/Swiss-Prot (P36873.1)"
     Region          302..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36873.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P36873.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36873.1)"
     CDS             1..323
                     /gene="PPP1CC"
                     /gene_synonym="PP-1G; PP1C; PPP1G"
                     /coded_by="NM_002710.4:185..1156"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9150.1"
                     /db_xref="GeneID:5501"
                     /db_xref="HGNC:HGNC:9283"
                     /db_xref="MIM:176914"
ORIGIN      
        1 madldklnid siiqrllevr gskpgknvql qeneirglcl ksreiflsqp illeleaplk
       61 icgdihgqyy dllrlfeygg fppesnylfl gdyvdrgkqs leticlllay kikypenffl
      121 lrgnhecasi nriygfydec krryniklwk tftdcfnclp iaaivdekif cchgglspdl
      181 qsmeqirrim rptdvpdqgl lcdllwsdpd kdvlgwgend rgvsftfgae vvakflhkhd
      241 ldlicrahqv vedgyeffak rqlvtlfsap nycgefdnag ammsvdetlm csfqilkpae
      301 kkkpnatrpv tpprgmitkq akk
//
LOCUS       NP_079350               4012 aa            linear   PRI 20-NOV-2025
DEFINITION  extracellular matrix organizing protein FRAS1 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_079350
VERSION     NP_079350.5
DBSOURCE    REFSEQ: accession NM_025074.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4012)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4012)
  AUTHORS   Tang,Z.Y., Wang,X.M., Xu,C.W., Sun,Q.Q., Hua,Y.X., Zhou,Q.Y.,
            Hu,H.Y., Liu,S.B., Guo,Y.J., Ao,L., Che,X., Zhang,X.C., Heger,M.,
            Zheng,X., Liu,A.J., Wang,Q., Zhan,Z.J., Cheng,S.Q. and Pan,W.W.
  TITLE     DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway
  JOURNAL   Cell Mol Life Sci 81 (1), 421 (2024)
   PUBMED   39367995
  REMARK    GeneRIF: DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4012)
  AUTHORS   Wang,V., Geybels,M.S., Jordahl,K.M., Gerke,T., Hamid,A.,
            Penney,K.L., Markt,S.C., Freedman,M., Pomerantz,M., Lee,G.M.,
            Rana,H., Bornigen,D., Rebbeck,T.R., Huttenhower,C., Eeles,R.A.,
            Stanford,J.L., Consortium,P., Berndt,S.I., Claessens,F.,
            Sorensen,K.D., Park,J.Y., Vega,A., Usmani,N., Mucci,L. and
            Sweeney,C.J.
  TITLE     A polymorphism in the promoter of FRAS1 is a candidate SNP
            associated with metastatic prostate cancer
  JOURNAL   Prostate 81 (10), 683-693 (2021)
   PUBMED   33956343
  REMARK    GeneRIF: A polymorphism in the promoter of FRAS1 is a candidate SNP
            associated with metastatic prostate cancer.
REFERENCE   4  (residues 1 to 4012)
  AUTHORS   Al-Hamed,M.H., Sayer,J.A., Alsahan,N., Tulbah,M., Kurdi,W.,
            Ambusaidi,Q., Ali,W. and Imtiaz,F.
  TITLE     Novel loss of function variants in FRAS1 AND FREM2 underlie renal
            agenesis in consanguineous families
  JOURNAL   J Nephrol 34 (3), 893-900 (2021)
   PUBMED   32643034
  REMARK    GeneRIF: Novel loss of function variants in FRAS1 AND FREM2
            underlie renal agenesis in consanguineous families.
REFERENCE   5  (residues 1 to 4012)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 4012)
  AUTHORS   Short,K., Wiradjaja,F. and Smyth,I.
  TITLE     Let's stick together: the role of the Fras1 and Frem proteins in
            epidermal adhesion
  JOURNAL   IUBMB Life 59 (7), 427-435 (2007)
   PUBMED   17654118
  REMARK    GeneRIF: In this review, recent studies support direct interactions
            between Fras1 and Frem proteins and shed new light on their role in
            the regulation of epidermal-basement membrane adhesion and
            organogenesis during development.
            Review article
REFERENCE   7  (residues 1 to 4012)
  AUTHORS   Vrontou,S., Petrou,P., Meyer,B.I., Galanopoulos,V.K., Imai,K.,
            Yanagi,M., Chowdhury,K., Scambler,P.J. and Chalepakis,G.
  TITLE     Fras1 deficiency results in cryptophthalmos, renal agenesis and
            blebbed phenotype in mice
  JOURNAL   Nat Genet 34 (2), 209-214 (2003)
   PUBMED   12766770
REFERENCE   8  (residues 1 to 4012)
  AUTHORS   McGregor,L., Makela,V., Darling,S.M., Vrontou,S., Chalepakis,G.,
            Roberts,C., Smart,N., Rutland,P., Prescott,N., Hopkins,J.,
            Bentley,E., Shaw,A., Roberts,E., Mueller,R., Jadeja,S., Philip,N.,
            Nelson,J., Francannet,C., Perez-Aytes,A., Megarbane,A., Kerr,B.,
            Wainwright,B., Woolf,A.S., Winter,R.M. and Scambler,P.J.
  TITLE     Fraser syndrome and mouse blebbed phenotype caused by mutations in
            FRAS1/Fras1 encoding a putative extracellular matrix protein
  JOURNAL   Nat Genet 34 (2), 203-208 (2003)
   PUBMED   12766769
  REMARK    GeneRIF: Locus FS1 at chromosome 4q21 is associated with Fraser
            syndrome. Mutation analysis identified five frameshift mutations in
            FRAS1, which encodes one member of a family of novel proteins
            related to an extracellular matrix (ECM) protein found in sea
            urchin.
REFERENCE   9  (residues 1 to 4012)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 4012)
  AUTHORS   Gattuso,J., Patton,M.A. and Baraitser,M.
  TITLE     The clinical spectrum of the Fraser syndrome: report of three new
            cases and review
  JOURNAL   J Med Genet 24 (9), 549-555 (1987)
   PUBMED   3118036
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093652.5, DA725113.1,
            DA881824.1, BC131820.1, AC093886.2, AB040933.2, AC104808.4,
            BX647949.1 and BX647420.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 18, 2009 this sequence version replaced NP_079350.4.
            
            Summary: This gene encodes an extracellular matrix protein that
            appears to function in the regulation of epidermal-basement
            membrane adhesion and organogenesis during development. Mutations
            in this gene cause Fraser syndrome, a multisystem malformation that
            can include craniofacial, urogenital and respiratory system
            abnormalities. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2142853,
                              SAMEA2144120 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000512123.4/ ENSP00000422834.2
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.21"
     Protein         1..4012
                     /product="extracellular matrix organizing protein FRAS1
                     isoform 1 precursor"
                     /note="extracellular matrix protein FRAS1; Fraser syndrome
                     1; fraser syndrome 1 protein; extracellular matrix
                     organizing protein FRAS1"
                     /calculated_mol_wt=440898
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2759
     mat_peptide     27..4012
                     /product="extracellular matrix organizing protein FRAS1
                     isoform 1"
                     /calculated_mol_wt=440898
     Region          28..87
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          95..152
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          159..216
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          221..278
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; pfam00093"
                     /db_xref="CDD:278520"
     Region          285..342
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          367..416
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          396..>673
                     /region_name="VSP"
                     /note="Giardia variant-specific surface protein;
                     pfam03302"
                     /db_xref="CDD:146106"
     Region          409..460
                     /region_name="FU 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          462..505
                     /region_name="FU 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          507..553
                     /region_name="FU 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          555..599
                     /region_name="FU 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          602..647
                     /region_name="FU 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          649..705
                     /region_name="FU 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          691..1060
                     /region_name="VSP"
                     /note="Giardia variant-specific surface protein;
                     pfam03302"
                     /db_xref="CDD:146106"
     Region          708..753
                     /region_name="FU 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            728
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          755..800
                     /region_name="FU 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          803..852
                     /region_name="FU 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          854..900
                     /region_name="FU 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          903..948
                     /region_name="FU 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          952..997
                     /region_name="FU 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          999..1042
                     /region_name="FU 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1046..1089
                     /region_name="FU 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1046..1087
                     /region_name="FU"
                     /note="Furin-like repeats; smart00261"
                     /db_xref="CDD:214589"
     Site            1093
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1102..1198
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1102..1197
                     /region_name="CSPG 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1203..1310
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1217..1308
                     /region_name="CSPG 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1314..1438
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1329..1438
                     /region_name="CSPG 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1446..1574
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1463..1559
                     /region_name="CSPG 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1577..1691
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1595..1689
                     /region_name="CSPG 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1699..1811
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1710..1810
                     /region_name="CSPG 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1777
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1816..1938
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          1833..1936
                     /region_name="CSPG 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1941..2059
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Site            1948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          1957..2057
                     /region_name="CSPG 8.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            1978
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2073..2179
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2078..2177
                     /region_name="CSPG 9.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2183..2293
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2199..2291
                     /region_name="CSPG 10.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2297..2406
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2311..2404
                     /region_name="CSPG 11.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2425..2537
                     /region_name="Cadherin_3"
                     /note="Cadherin-like; pfam16184"
                     /db_xref="CDD:465048"
     Region          2439..2536
                     /region_name="CSPG 12.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01201"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          <2553..>2803
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Region          2555..2650
                     /region_name="Calx_beta"
                     /note="Domains in Na-Ca exchangers and integrin-beta4;
                     smart00237"
                     /db_xref="CDD:197594"
     Site            2563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2668
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2686
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Region          2798..2894
                     /region_name="Calx-beta"
                     /note="Calx-beta domain; cl02522"
                     /db_xref="CDD:413355"
     Region          <2907..>3134
                     /region_name="caca"
                     /note="sodium/calcium exchanger 1; TIGR00845"
                     /db_xref="CDD:273296"
     Site            2912
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            2989
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3074
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3680
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3879
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XX4.2)"
     Site            3906..3926
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XX4.2)"
     CDS             1..4012
                     /gene="FRAS1"
                     /gene_synonym="FRASRS1"
                     /coded_by="NM_025074.7:688..12726"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS54771.1"
                     /db_xref="GeneID:80144"
                     /db_xref="HGNC:HGNC:19185"
                     /db_xref="MIM:607830"
ORIGIN      
        1 mgvlkvwlgl alalaefavl phhsegacvy qdslladati wkpdscqscr chgdivickp
       61 avcrnpqcaf ekgevlqiaa nqccpecvlr tpgschhekk ihehgtewas spcsvcscnh
      121 gevrctpqpc pplscghqel afipegsccp vcvglgkpcs yeghvfqdge dwrlsrcakc
      181 lcrngvaqcf taqcqplfcn qdetvvrvpg kccpqcsars csaagqvyeh geqwsenact
      241 tcicdrgevr chkqaclplr cgkgqsrarr hgqcceecvs pagscsydgv vryqdemwkg
      301 sacefcmcdh gqvtcqtgec akvecardee lihldgkccp ecisrngycv yeetgefmss
      361 nasevkripe gekwedgpck vcecrgaqvt cyepscppcp vgtlalevkg qccpdctsvh
      421 chpdcltcsq spdhcdlcqd ptkllqngwc vhscglgfyq agslclacqp qcstctsgle
      481 csscqppllm rhgqcvptcg dgfyqdrhsc avchescagc wgptekhcla crdplhvlrd
      541 ggcesscgkg fynrqgtcsa cdqscdscgp ssprcltcte ktvlhdgkcm secpggyyad
      601 atgrckvchn scascsgptp shctacsppk alrqghclpr cgegfysdhg vckachsscl
      661 acmgpapshc tgckkpeegl qveqlsdvgi psgeclaqcr ahfylestgi ceachqscfr
      721 cagksphnct dcgpshvlld gqclsqcpdg yfhqegscte chptcrqchg plesdciscy
      781 phisltngnc rtscreeqfl nlvgycadch hlcqhcaadl hntgsiclrc qnahylllgd
      841 hcvpdcpsgy yaergackkc hsscrtcqgr gpfscsscdt nlvlshtgtc sttcfpghyl
      901 ddnhvcqpcn thcgscdsqa sctscrdpnk vllfgecqye scapqyyldf stntckecdw
      961 scsacsgplk tdclqcmdgy vlqdgacveq clssfyqdsg lckncdsycl qcqgphectr
     1021 ckgpflllea qcvqecgkgy fadhakhkct acpqgclqcs hrdrchlcdh gfflksglcv
     1081 yncvpgfsvh tsnetcsgki htpslhvngs lilpigsikp ldfsllnvqd qegrvedllf
     1141 hvvstptngq lvlsrngkev qldkagrfsw kdvnekkvrf vhskeklrkg ylflkisdqq
     1201 ffsepqlini qafstqapyv lrnevlhisr geratittqm ldirdddnpq dvvieiidpp
     1261 lhgqllqtlq spatpiyqfq ldelsrgllh yahdgsdsts dvavlqandg hsfhnilfqv
     1321 ktvpqndrgl qlvansmvwv peggmlqitn rilqaeapga saeeiiykit qdypqfgevv
     1381 llvnmpadsp adegqhlpdg rtatptstft qqdinegivw yrhsgapaqs dsfrfevssa
     1441 snaqtrlesh mfniailpqt peapkvslea slhmtaredg ltviqphsls finsekpsgk
     1501 ivynitlplh pnqgiiehrd hphspiryft qedinqgkvm yrpppaaphl qelmafsfag
     1561 lpesvkfhft vsdgehtspe mvltihllps dqqlpvfqvt aprlavspgg stsvglqvvv
     1621 rdaetapkel ffelrrppqh gvllkhtaef rrpmatgdtf tyedveknal qyihdgsstr
     1681 edsmeisvtd gltvtmlevr vevslsedrg prlaagssls itvaskstai itrshlayvd
     1741 dsspdpeiwi qlnylpsygt llrisgseve elsevsnftm edinnkkiry savfetdghl
     1801 vtdsfyfsvs dmdhnhldnq iftimitpae npppviafad litvdeggra plsfhhffat
     1861 ddddnlqrda iiklsalpky gcientgtgd rfgpetasdl easfpiqdvl enyiyyfqsv
     1921 hesiepthdi fsfyvsdgts rseihsinit ierkndeppr mtlqplrvql ssgvvisnss
     1981 lslqdldtpd nelifvltkk pdhghvlwrq taseplengr vlvqgstfty qdilaglvgy
     2041 vpsvpgmvvd efqfsltdgl hvdtgrmkiy telpasdtph lainqglqls agsvariteq
     2101 hlkvtdidsd dhqvmyimke dpgagrlqmm khgnleqisi kgpirsftqa disqghveys
     2161 hgtgepggsf afkfdvvdge gnrlidksfs isiledkspp vittnkglvl densvkkitt
     2221 lqlsatdqds gpteliyrit rqpqlghleh aaspgiqiss ftqadltsrn vqyvhsseae
     2281 khsdafsftl sdgvsevtqt fhitlhpvdd slpvvqnlgm rvqegmrkti tefelkavda
     2341 dteaesvtft ivqpprhgti ertsngqhfh ltstftmkdi yqnrvsyshd gsnslkdrft
     2401 ftvsdgtnpf fiieeggkei mtaapqpfrv dilpvddgtp rivtnlglqw leymdgkatn
     2461 litkkelltm dpdtedaqlv yeittgpkhg fvenklqpgr aaatftqedv nlgliryvlh
     2521 kekiremmds fqflvkdskp nvvsdnvfhi qwslisfkyt synvsekags vsvtvqrtgn
     2581 lnqyaivlcr teqgtassss rvssqpgqqd yveyagqvqf deredtksct ivindddvfe
     2641 nvesftvels mpayallgef tqakviindt edeptlefdk kiywvnesag flfapierkg
     2701 dassivsaic ytvpksamgs slyalesgsd fksrgmsaas rvifgpgvtm stcdvmlidd
     2761 seyeeeeefe ialadasdna rigrvatakv lisgpndast vslgntaftv sedagtvkip
     2821 virhgtdlst fasvwcatrp sdpasatpgv dyvpssrkve fgpgvieqyc tltilddtqy
     2881 pviegletfv vflssaqgae ltkpfqavia indtfqdvps mqfakdlllv kekegvlhvp
     2941 itrsgdlsye ssvrcytqsh saqvmedfee rqnadssrit flkgdkvknc tvyihddsmf
     3001 epeeqfrvyl glplgnhwsg arigknnmat itisndedap tiefeeaayq vrepagpdai
     3061 ailnikvirr gdqnrtskvr cstrdgsaqs gvdyypksrv lkfspgvdhi ffkveilsne
     3121 drewhesfsl vlgpddpvea vlgdvttatv tildqeaags lilpappivv tladydhvee
     3181 vtkegvkksp spgyplvcvt pcdphfprya vmkercseag inqtsvqfsw evaaptdgng
     3241 arspfetitd ntpftsvnhm vldsiyfsrr fhvrcvakav dkvghvgtpl rsnivtigtd
     3301 saichtpvva gtsrgfqaqs fiatlkyldv khkehpnrih isvqiphqdg mlplistmpl
     3361 hnlhfllses iyrhqhvcsn lvttydlrgi seagflddvv ydstalgpgy drpfqfdpsv
     3421 repktiqlyk hlnlkscvwt fdayydmtel idvcggsvta dfqvrdsaqs fltvhvplyv
     3481 syiyvtaprg waslehhtem efsffydtvl wrtgiqtdsv lsarlqiiri yiredgrlvi
     3541 efkthakfrg qfvmehhtlp evksfvltpd hlggiefdlq llwsaqtfds phqlwratss
     3601 ynrkdysgey tiylipctvq ptqpwvdpge kplactahap erflipiafq qtnrpvpvvy
     3661 slntefqlcn nekvflmdpn tsdmslaemd ykgafskgqi lygrvlwnpe qnlnsayklq
     3721 lekvylctgk dgyvpffdpt gtiynegpqy gciqpnkhlk hrfllldrnq pevtdkyfhd
     3781 vpfeahfase lpdfhvvsnm pgvdgftlkv dalykveagh qwylqviyii gpdtisgprv
     3841 qrsltaplrr nrrdlvepdg qlilddsliy dnegdqvkng tnmkslnlem qelavaasls
     3901 qtgasigsal aaimllllvf lvacfinrkc qkqrkkkpae dileeyplnt kvevpkrhpd
     3961 rveknvnrhy ctvrnvnils epeaaytfkg akvkrlnlev rvhnnlqdgt ev
//
LOCUS       NP_001341013             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341013 XP_016879181
VERSION     NP_001341013.1
DBSOURCE    REFSEQ: accession NM_001354084.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 29, 2017 this sequence version replaced XP_016879181.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.59348.1,
                                           SRR1803615.248012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354084.2:582..1346"
                     /note="isoform a is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_150593                138 aa            linear   PRI 20-NOV-2025
DEFINITION  extracellular glycoprotein lacritin precursor [Homo sapiens].
ACCESSION   NP_150593
VERSION     NP_150593.1
DBSOURCE    REFSEQ: accession NM_033277.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 138)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 138)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 138)
  AUTHORS   Georgiev,G.A., Gh,M.S., Romano,J., Dias Teixeira,K.L., Struble,C.,
            Ryan,D.S., Sia,R.K., Kitt,J.P., Harris,J.M., Hsu,K.L., Libby,A.,
            Odrich,M.G., Suarez,T., McKown,R.L. and Laurie,G.W.
  TITLE     Lacritin proteoforms prevent tear film collapse and maintain
            epithelial homeostasis
  JOURNAL   J Biol Chem 296, 100070 (2021)
   PUBMED   33187980
  REMARK    GeneRIF: Lacritin proteoforms prevent tear film collapse and
            maintain epithelial homeostasis.
REFERENCE   4  (residues 1 to 138)
  AUTHORS   Dias-Teixeira,K., Horton,X., McKown,R., Romano,J. and Laurie,G.W.
  TITLE     The Lacritin-Syndecan-1-Heparanase Axis in Dry Eye Disease
  JOURNAL   Adv Exp Med Biol 1221, 747-757 (2020)
   PUBMED   32274735
  REMARK    GeneRIF: The Lacritin-Syndecan-1-Heparanase Axis in Dry Eye Disease
            Review article
REFERENCE   5  (residues 1 to 138)
  AUTHORS   Aass,C., Norheim,I., Eriksen,E.F., Bornick,E.C., Thorsby,P.M. and
            Pepaj,M.
  TITLE     Establishment of a tear protein biomarker panel differentiating
            between Graves' disease with or without orbitopathy
  JOURNAL   PLoS One 12 (4), e0175274 (2017)
   PUBMED   28419103
  REMARK    GeneRIF: Data show increased levels of lysozyme C (LYZ), lacritin
            (LACRT) and zinc-alpha-2 glycoprotein 1 (AZGP1) in pooled tear
            fluid sample from Graves' disease (GD) patients with
            moderate-to-severe Graves' orbitopathy (GO) compared with GD
            patients without clinical signs of GO.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 138)
  AUTHORS   Koo,B.S., Lee,D.Y., Ha,H.S., Kim,J.C. and Kim,C.W.
  TITLE     Comparative analysis of the tear protein expression in blepharitis
            patients using two-dimensional electrophoresis
  JOURNAL   J Proteome Res 4 (3), 719-724 (2005)
   PUBMED   15952718
  REMARK    GeneRIF: Lacritin is one of nine tear proteins downregulated in
            patients suffering from blepharitis, or inflammation of the eyelid
            often associated with dry eye.
REFERENCE   7  (residues 1 to 138)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
  REMARK    GeneRIF: Lacritin is the sixth most common transcript in the human
            lacrimal gland based on EST sequencing, and is one of twenty-nine
            'lacrimal preferred' genes.
REFERENCE   8  (residues 1 to 138)
  AUTHORS   Weigelt,B., Bosma,A.J. and van 't Veer,L.J.
  TITLE     Expression of a novel lacrimal gland gene lacritin in human breast
            tissues
  JOURNAL   J Cancer Res Clin Oncol 129 (12), 735-736 (2003)
   PUBMED   14574570
  REMARK    GeneRIF: expressed in human breast tumors, breast cancer cell
            lines, and normal breast
REFERENCE   9  (residues 1 to 138)
  AUTHORS   Kumar,R., Huebner,A. and Laurie,G.W.
  TITLE     Genetic separation of the human lacritin gene ('LACRT') and triple
            A (Allgrove) syndrome on 12q13
  JOURNAL   Adv Exp Med Biol 506 (Pt A), 167-174 (2002)
   PUBMED   12613904
  REMARK    GeneRIF: Lacritin gene maps near but not within triple A syndome
            region. Alacrimia in triple a syndrome not due to mutation in
            lacritin gene.
REFERENCE   10 (residues 1 to 138)
  AUTHORS   Sanghi,S., Kumar,R., Lumsden,A., Dickinson,D., Klepeis,V.,
            Trinkaus-Randall,V., Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     cDNA and genomic cloning of lacritin, a novel secretion enhancing
            factor from the human lacrimal gland
  JOURNAL   J Mol Biol 310 (1), 127-139 (2001)
   PUBMED   11419941
  REMARK    GeneRIF: Tissue microarray of seventy-five different human tissues,
            including mammary gland, detected expression only in lacrimal
            acinar and salivary ductal cells.  Thyroid immunostaining was
            equivocal.  These data agree with Clonetech RNA dot blot analysis.
            GeneRIF: Lacritin is detected in human tears and promotes tear
            secretion in vitro when added to rat lacrimal acinar cells via a
            pathway apparently independent of the M3 receptor.  It is mitogenic
            at low ng/ml levels for salivary ductal cells.
            GeneRIF: Lacritin binds several basment membrane components
            (collagen IV, nidogen, fibronectin, laminin-1).  Also vitronectin,
            but not collagen I or heparin.  Yet it is secreted apically and
            possibly may form non-covalent complexes with tear fibronectin.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079310.20.
            
            Summary: The protein encoded by this gene is highly expressed in
            the lacrimal glands and localized primarily to secretory granules
            and secretory fluid. It augments lacrimal acinar cell secretion,
            promotes ductal cell proliferation, and stimulates signaling
            through tyrosine phosphorylation and release of calcium. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD724194.1, BC062217.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMN03465412
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257867.5/ ENSP00000257867.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..138
                     /product="extracellular glycoprotein lacritin precursor"
                     /note="extracellular glycoprotein lacritin"
                     /calculated_mol_wt=12264
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2000
     mat_peptide     20..138
                     /product="extracellular glycoprotein lacritin"
                     /calculated_mol_wt=12264
     Region          20..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ8.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ8.1)"
     CDS             1..138
                     /gene="LACRT"
                     /coded_by="NM_033277.2:55..471"
                     /db_xref="CCDS:CCDS8883.1"
                     /db_xref="GeneID:90070"
                     /db_xref="HGNC:HGNC:16430"
                     /db_xref="MIM:607360"
ORIGIN      
        1 mkfttllfla avagalvyae dassdstgad paqeagtskp neeisgpaep asppetttta
       61 qetsaaavqg takvtssrqe lnplksivek sillteqala kagkgmhggv pggkqfieng
      121 sefaqkllkk fsllkpwa
//
LOCUS       NP_006666                239 aa            linear   PRI 20-NOV-2025
DEFINITION  tetraspanin-9 [Homo sapiens].
ACCESSION   NP_006666 NP_112575
VERSION     NP_006666.1
DBSOURCE    REFSEQ: accession NM_006675.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Qi,Y., Lv,J., Liu,S., Sun,L., Wang,Y., Li,H., Qi,W. and Qiu,W.
  TITLE     TSPAN9 and EMILIN1 synergistically inhibit the migration and
            invasion of gastric cancer cells by increasing TSPAN9 expression
  JOURNAL   BMC Cancer 19 (1), 630 (2019)
   PUBMED   31242895
  REMARK    GeneRIF: expression of the membrane protein TSPAN9 regulates
            gastric cancer cell migration and invasion by inhibiting the
            FAK-RAS-ERK1/2 signaling pathway. The extracellular secretory
            protein EMILIN1 can increase this tumor suppressive effect by
            promoting the expression of TSPAN9.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Haining,E.J., Matthews,A.L., Noy,P.J., Romanska,H.M., Harris,H.J.,
            Pike,J., Morowski,M., Gavin,R.L., Yang,J., Milhiet,P.E.,
            Berditchevski,F., Nieswandt,B., Poulter,N.S., Watson,S.P. and
            Tomlinson,M.G.
  TITLE     Tetraspanin Tspan9 regulates platelet collagen receptor GPVI
            lateral diffusion and activation
  JOURNAL   Platelets 28 (7), 629-642 (2017)
   PUBMED   28032533
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Li,P.Y., Lv,J., Qi,W.W., Zhao,S.F., Sun,L.B., Liu,N., Sheng,J. and
            Qiu,W.S.
  TITLE     Tspan9 inhibits the proliferation, migration and invasion of human
            gastric cancer SGC7901 cells via the ERK1/2 pathway
  JOURNAL   Oncol Rep 36 (1), 448-454 (2016)
   PUBMED   27177197
  REMARK    GeneRIF: The proliferation, migration and invasion of human gastric
            cancer SGC7901 cells were significantly inhibited by overexpression
            of Tspan9.
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Stiles,K.M. and Kielian,M.
  TITLE     Role of TSPAN9 in Alphavirus Entry and Early Endosomes
  JOURNAL   J Virol 90 (9), 4289-4297 (2016)
   PUBMED   26865714
  REMARK    GeneRIF: TSPAN9 is an endosomal tetraspanin whose depletion has a
            pronounced effect on the entry of several viruses that fuse in the
            early endosome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Xie,T., Deng,L., Mei,P., Zhou,Y., Wang,B., Zhang,J., Lin,J.,
            Wei,Y., Zhang,X. and Xu,R.
  TITLE     Genome-wide association study combining pathway analysis for
            typical sporadic amyotrophic lateral sclerosis in Chinese Han
            populations
  JOURNAL   Neurobiol Aging 35 (7), 1778 (2014)
   PUBMED   24529757
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Kotha,J., Zhang,C., Longhurst,C.M., Lu,Y., Jacobs,J., Cheng,Y. and
            Jennings,L.K.
  TITLE     Functional relevance of tetraspanin CD9 in vascular smooth muscle
            cell injury phenotypes: a novel target for the prevention of
            neointimal hyperplasia
  JOURNAL   Atherosclerosis 203 (2), 377-386 (2009)
   PUBMED   18799160
  REMARK    GeneRIF: tetraspanin CD9 has a role in determining vascular smooth
            muscle cell injury phenotypes
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Protty,M.B., Watkins,N.A., Colombo,D., Thomas,S.G., Heath,V.L.,
            Herbert,J.M., Bicknell,R., Senis,Y.A., Ashman,L.K.,
            Berditchevski,F., Ouwehand,W.H., Watson,S.P. and Tomlinson,M.G.
  TITLE     Identification of Tspan9 as a novel platelet tetraspanin and the
            collagen receptor GPVI as a component of tetraspanin microdomains
  JOURNAL   Biochem J 417 (1), 391-400 (2009)
   PUBMED   18795891
  REMARK    GeneRIF: Findings suggest a role for Tspan9 in regulating platelet
            function in concert with other platelet tetraspanins and their
            associated proteins.
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Berditchevski,F.
  TITLE     Complexes of tetraspanins with integrins: more than meets the eye
  JOURNAL   J Cell Sci 114 (Pt 23), 4143-4151 (2001)
   PUBMED   11739647
  REMARK    Review article
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Serru,V., Dessen,P., Boucheix,C. and Rubinstein,E.
  TITLE     Sequence and expression of seven new tetraspans
  JOURNAL   Biochim Biophys Acta 1478 (1), 159-163 (2000)
   PUBMED   10719184
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125807.9, BC071881.1,
            AC005912.1 and AC005865.1.
            
            On Jan 7, 2005 this sequence version replaced NP_112575.1.
            
            Summary: The protein encoded by this gene is a member of the
            transmembrane 4 superfamily, also known as the tetraspanin family.
            Most of these members are cell-surface proteins that are
            characterized by the presence of four hydrophobic domains. The
            proteins mediate signal transduction events that play a role in the
            regulation of cell development, activation, growth and motility.
            Alternatively spliced transcripts encoding the same protein have
            been identified. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027366.1, SRR3476690.487745.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000011898.10/ ENSP00000011898.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33-p13.32"
     Protein         1..239
                     /product="tetraspanin-9"
                     /note="transmembrane 4 superfamily member tetraspan NET-5;
                     new EST tetraspan 5; tspan-9"
                     /calculated_mol_wt=26648
     Region          9..228
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75954.1)"
     Site            56..76
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75954.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75954.1)"
     Region          105..202
                     /region_name="NET-5_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), NET-5_like family. Tetraspanins
                     are trans-membrane proteins with 4 trans-membrane
                     segments. Both the N- and C-termini lie on the
                     intracellular side of the membrane. This alignment
                     model...; cd03165"
                     /db_xref="CDD:239418"
     Site            order(106,111,115,117..118,121,137,140..141,144..145)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239418"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75954.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75954.1)"
     CDS             1..239
                     /gene="TSPAN9"
                     /gene_synonym="NET-5; NET5; PP1057"
                     /coded_by="NM_006675.5:160..879"
                     /db_xref="CCDS:CCDS8520.1"
                     /db_xref="GeneID:10867"
                     /db_xref="HGNC:HGNC:21640"
                     /db_xref="MIM:613137"
ORIGIN      
        1 margclcclk ymmflfnlif wlcgcgllgv giwlsvsqgn fatfspsfps lsaanlviai
       61 gtivmvtgfl gclgaikenk clllsffivl lvillaelil lilffvymdk vnenakkdlk
      121 eglllyhten nvglknawni iqaemrccgv tdytdwypvl gentvpdrcc mensqgcgrn
      181 attplwrtgc yekvkmwfdd nkhvlgtvgm cilimqilgm afsmtlfqhi hrtgkkyda
//
LOCUS       NP_060954                550 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 22 member 11 isoform 1 [Homo sapiens].
ACCESSION   NP_060954
VERSION     NP_060954.1
DBSOURCE    REFSEQ: accession NM_018484.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Vavra,J., Pavelcova,K., Masinova,J., Hasikova,L., Bubenikova,E.,
            Urbanova,A., Mancikova,A. and Stiburkova,B.
  TITLE     Examining the Association of Rare Allelic Variants in Urate
            Transporters SLC22A11, SLC22A13, and SLC17A1 with Hyperuricemia and
            Gout
  JOURNAL   Dis Markers 2024, 5930566 (2024)
   PUBMED   38222853
  REMARK    GeneRIF: Examining the Association of Rare Allelic Variants in
            Urate Transporters SLC22A11, SLC22A13, and SLC17A1 with
            Hyperuricemia and Gout.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Yu,Z., Wang,H. and You,G.
  TITLE     The regulation of human organic anion transporter 4 by insulin-like
            growth factor 1 and protein kinase B signaling
  JOURNAL   Biochem Pharmacol 215, 115702 (2023)
   PUBMED   37487877
  REMARK    GeneRIF: The regulation of human organic anion transporter 4 by
            insulin-like growth factor 1 and protein kinase B signaling.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Louisse,J., Dellafiora,L., van den Heuvel,J.J.M.W., Rijkers,D.,
            Leenders,L., Dorne,J.C.M., Punt,A., Russel,F.G.M. and
            Koenderink,J.B.
  TITLE     Perfluoroalkyl substances (PFASs) are substrates of the renal human
            organic anion transporter 4 (OAT4)
  JOURNAL   Arch Toxicol 97 (3), 685-696 (2023)
   PUBMED   36436016
  REMARK    GeneRIF: Perfluoroalkyl substances (PFASs) are substrates of the
            renal human organic anion transporter 4 (OAT4).
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Giri,A.K., Prasad,G., Bandesh,K., Parekatt,V., Mahajan,A.,
            Banerjee,P., Kauser,Y., Chakraborty,S., Rajashekar,D., Sharma,A.,
            Mathur,S.K., Basu,A., McCarthy,M.I., Tandon,N. and Bharadwaj,D.
  CONSRTM   INDICO
  TITLE     Multifaceted genome-wide study identifies novel regulatory loci in
            SLC22A11 and ZNF45 for body mass index in Indians
  JOURNAL   Mol Genet Genomics 295 (4), 1013-1026 (2020)
   PUBMED   32363570
  REMARK    GeneRIF: our study discovered 3 novel population-specific
            functional genetic variants (rs6913677, rs2078267, rs8100011) in 2
            novel (SLC22A11 and ZNF45) and 1 earlier reported gene (BAI3) for
            BMI in Indians. Our study decodes key genomic loci underlying
            obesity phenotype in Indians that may serve as prospective drug
            targets in future
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Kimura,H., Takeda,M., Narikawa,S., Enomoto,A., Ichida,K. and
            Endou,H.
  TITLE     Human organic anion transporters and human organic cation
            transporters mediate renal transport of prostaglandins
  JOURNAL   J Pharmacol Exp Ther 301 (1), 293-298 (2002)
   PUBMED   11907186
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Babu,E., Takeda,M., Narikawa,S., Kobayashi,Y., Yamamoto,T.,
            Cha,S.H., Sekine,T., Sakthisekaran,D. and Endou,H.
  TITLE     Human organic anion transporters mediate the transport of
            tetracycline
  JOURNAL   Jpn J Pharmacol 88 (1), 69-76 (2002)
   PUBMED   11855680
  REMARK    GeneRIF: elucidation of the molecular mechanism for renal
            tetracycline transport by human organic anion transporters (hOATs)
            using proximal tubular cells stably expressing hOATs
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Sun,W., Wu,R.R., van Poelje,P.D. and Erion,M.D.
  TITLE     Isolation of a family of organic anion transporters from human
            liver and kidney
  JOURNAL   Biochem Biophys Res Commun 283 (2), 417-422 (2001)
   PUBMED   11327718
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Cha,S.H., Sekine,T., Kusuhara,H., Yu,E., Kim,J.Y., Kim,D.K.,
            Sugiyama,Y., Kanai,Y. and Endou,H.
  TITLE     Molecular cloning and characterization of multispecific organic
            anion transporter 4 expressed in the placenta
  JOURNAL   J Biol Chem 275 (6), 4507-4512 (2000)
   PUBMED   10660625
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC034384.1, AP001092.5,
            BI051409.1, AA331094.1 and BX094958.1.
            
            Summary: The protein encoded by this gene is involved in the
            sodium-independent transport and excretion of organic anions, some
            of which are potentially toxic. The encoded protein is an integral
            membrane protein and is found mainly in the kidney and in the
            placenta, where it may act to prevent potentially harmful organic
            anions from reaching the fetus. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034384.1, AK290791.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301891.9/ ENSP00000301891.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..550
                     /product="solute carrier family 22 member 11 isoform 1"
                     /note="solute carrier family 22 (organic anion/cation
                     transporter), member 11; organic anion transporter 4;
                     solute carrier family 22 (organic anion/urate
                     transporter), member 11; organic anion:dicarboxylate
                     exchanger OAT4"
                     /calculated_mol_wt=59841
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            99
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Region          106..511
                     /region_name="MFS_OAT"
                     /note="Organic anion transporters of the Major Facilitator
                     Superfamily of transporters; cd17374"
                     /db_xref="CDD:340932"
     Site            order(123..124,127..128,131,157,207..208,210..212,215,231,
                     234..235,238,353,356..357,360..362,365,385,389,440..441,
                     445,449,465,468..469,472..473,476)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340932"
     Site            143..163
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            175..195
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            347..367
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            379..399
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            403..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            431..451
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            464..484
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Site            491..511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     Region          531..550
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSA0.1)"
     CDS             1..550
                     /gene="SLC22A11"
                     /gene_synonym="hOAT4; OAT4"
                     /coded_by="NM_018484.4:60..1712"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8074.1"
                     /db_xref="GeneID:55867"
                     /db_xref="HGNC:HGNC:18120"
                     /db_xref="MIM:607097"
ORIGIN      
        1 mafsklleqa ggvglfqtlq vltfilpclm ipsqmllenf saaipghrcw thmldngsav
       61 stnmtpkall tisippgpnq gphqcrrfrq pqwqlldpna tatswseadt epcvdgwvyd
      121 rsvftstiva kwdlvcssqg lkplsqsifm sgilvgsfiw gllsyrfgrk pmlswcclql
      181 avagtstifa ptfviycglr fvaafgmagi flssltlmve wtttsrravt mtvvgcafsa
      241 gqaalgglaf alrdwrtlql aasvpffais liswwlpesa rwliikgkpd qalqelrkva
      301 ringhkeakn ltievlmssv keevasakep rsvldlfcvp vlrwrscaml vvnfsllisy
      361 yglvfdlqsl grdifllqal fgavdflgra ttalllsflg rrtiqagsqa maglailanm
      421 lvpqdlqtlr vvfavlgkgc fgisltclti ykaelfptpv rmtadgilht vgrlgammgp
      481 lilmsrqalp llppllygvi siasslvvlf flpetqglpl pdtiqdlesq kstaaqgnrq
      541 eavtvestsl
//
LOCUS       NP_065949                691 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium-binding and coiled-coil domain-containing protein 1 isoform
            1 [Homo sapiens].
ACCESSION   NP_065949
VERSION     NP_065949.1
DBSOURCE    REFSEQ: accession NM_020898.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 691)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 691)
  AUTHORS   Kumar,K., Chidambaram,R., Parashar,S. and Ferro-Novick,S.
  TITLE     RTN3L and CALCOCO1 function in parallel to maintain proteostasis in
            the endoplasmic reticulum
  JOURNAL   Autophagy 20 (9), 2067-2075 (2024)
   PUBMED   38818751
  REMARK    GeneRIF: RTN3L and CALCOCO1 function in parallel to maintain
            proteostasis in the endoplasmic reticulum.
REFERENCE   3  (residues 1 to 691)
  AUTHORS   Chen,W., Ouyang,X., Chen,L. and Li,L.
  TITLE     Multiple functions of CALCOCO family proteins in selective
            autophagy
  JOURNAL   J Cell Physiol 237 (9), 3505-3516 (2022)
   PUBMED   35853167
  REMARK    Review article
REFERENCE   4  (residues 1 to 691)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 691)
  AUTHORS   Nthiga,T.M., Kumar Shrestha,B., Sjottem,E., Bruun,J.A., Bowitz
            Larsen,K., Bhujabal,Z., Lamark,T. and Johansen,T.
  TITLE     CALCOCO1 acts with VAMP-associated proteins to mediate ER-phagy
  JOURNAL   EMBO J 39 (15), e103649 (2020)
   PUBMED   32525583
  REMARK    GeneRIF: CALCOCO1 acts with VAMP-associated proteins to mediate
            ER-phagy.
REFERENCE   6  (residues 1 to 691)
  AUTHORS   Yang,C.K., Kim,J.H. and Stallcup,M.R.
  TITLE     Role of the N-terminal activation domain of the coiled-coil
            coactivator in mediating transcriptional activation by beta-catenin
  JOURNAL   Mol Endocrinol 20 (12), 3251-3262 (2006)
   PUBMED   16931570
  REMARK    GeneRIF: The N terminus of CoCoA contains another activation domain
            , which is necessary and sufficient for synergistic activation of
            LEF1-mediated transcription by CoCoA and beta-catenin.
REFERENCE   7  (residues 1 to 691)
  AUTHORS   Kim,J.H., Yang,C.K. and Stallcup,M.R.
  TITLE     Downstream signaling mechanism of the C-terminal activation domain
            of transcriptional coactivator CoCoA
  JOURNAL   Nucleic Acids Res 34 (9), 2736-2750 (2006)
   PUBMED   16717280
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 691)
  AUTHORS   Yang,C.K., Kim,J.H., Li,H. and Stallcup,M.R.
  TITLE     Differential use of functional domains by coiled-coil coactivator
            in its synergistic coactivator function with beta-catenin or GRIP1
  JOURNAL   J Biol Chem 281 (6), 3389-3397 (2006)
   PUBMED   16344550
  REMARK    GeneRIF: CoCoA uses different combinations of functional domains in
            its synergistic coactivator function with beta-catenin or GRIP1
REFERENCE   9  (residues 1 to 691)
  AUTHORS   Takahashi,K., Inuzuka,M. and Ingi,T.
  TITLE     Cellular signaling mediated by calphoglin-induced activation of IPP
            and PGM
  JOURNAL   Biochem Biophys Res Commun 325 (1), 203-214 (2004)
   PUBMED   15522220
  REMARK    GeneRIF: Results report a novel human protein, calphoglin, which
            activates inorganic pyrophosphatase (IPP) and enhances
            phosphoglucomutase activity through the activated IPP.
REFERENCE   10 (residues 1 to 691)
  AUTHORS   Lee,S.Y., Obata,Y., Yoshida,M., Stockert,E., Williamson,B.,
            Jungbluth,A.A., Chen,Y.T., Old,L.J. and Scanlan,M.J.
  TITLE     Immunomic analysis of human sarcoma
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2651-2656 (2003)
   PUBMED   12601173
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315578.1, AL136895.1, BC003177.1 and AC076968.38.
            
            Transcript Variant: This variant (1) encodes the longer protein
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.174329.1,
                                           SRR1803615.19042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000550804.6/ ENSP00000449960.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..691
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..691
                     /product="calcium-binding and coiled-coil
                     domain-containing protein 1 isoform 1"
                     /note="coiled-coil leucine zipper coactivator 1;
                     calcium-binding and coiled-coil domain-containing protein
                     1; inorganic pyrophosphatase activator; sarcoma antigen
                     NY-SAR-3; coiled-coil coactivator protein"
                     /calculated_mol_wt=77205
     Region          1..190
                     /region_name="N-terminal AD (CTNNB1 binding site).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Region          1..30
                     /region_name="p300 KIX-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Region          15..118
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     Region          45..125
                     /region_name="Interaction with GATA1.
                     /evidence=ECO:0000250|UniProtKB:Q8CGU1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Region          122..596
                     /region_name="CALCOCO1"
                     /note="Calcium binding and coiled-coil domain (CALCOCO1)
                     like; pfam07888"
                     /db_xref="CDD:462303"
     Region          501..691
                     /region_name="C-terminal AD (CTNNB1 binding site),
                     interaction with CCAR1.
                     /evidence=ECO:0000250|UniProtKB:Q8CGU1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Region          514..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Z2.2)"
     Region          654..682
                     /region_name="Zn-C2H2_CALCOCO1"
                     /note="C2H2-type zinc binding domain found in
                     calcium-binding and coiled-coil domain-containing protein
                     1 (CALCOCO1) and similar proteins; cd21967"
                     /db_xref="CDD:412013"
     CDS             1..691
                     /gene="CALCOCO1"
                     /gene_synonym="calphoglin; Cocoa; PP13275"
                     /coded_by="NM_020898.3:74..2149"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8864.1"
                     /db_xref="GeneID:57658"
                     /db_xref="HGNC:HGNC:29306"
ORIGIN      
        1 meesplsrap srggvnflnv artyipntkv echytlppgt mpsasdwigi fkveaacvrd
       61 yhtfvwssvp esttdgspih tsvqfqasyl pkpgaqlyqf ryvnrqgqvc gqsppfqfre
      121 prpmdelvtl eeadggsdil lvvpkatvlq nqldesqqer ndlmqlklql egqvtelrsr
      181 vqeleralat arqehtelme qykgisrshg eiteerdils rqqgdhvari leleddiqti
      241 sekvltkeve ldrlrdtvka ltreqekllg qlkevqadke qseaelqvaq qenhhlnldl
      301 keakswqeeq saqaqrlkdk vaqmkdtlgq aqqrvaelep lkeqlrgaqe laassqqkat
      361 llgeelasaa aardrtiael hrsrlevaev ngrlaelglh lkeekcqwsk eragllqsve
      421 aekdkilkls aeilrlekav qeertqnqvf ktelarekds slvqlseskr eltelrsalr
      481 vlqkekeqlq eekqelleym rklearlekv adekwnedat tedeeaavgl scpaaltdse
      541 despedmrlp pyglcergdp gsspagprea splvvisqpa pisphlsgpa edsssdseae
      601 deksvlmaav qsggeeanll lpelgsafyd masgftvgtl setstggpat ptwkecpick
      661 erfpaesdkd aledhmdghf ffstqdpftf e
//
LOCUS       NP_775097                206 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI ethanolamine phosphate transferase, stabilizing subunit isoform
            2 [Homo sapiens].
ACCESSION   NP_775097
VERSION     NP_775097.1
DBSOURCE    REFSEQ: accession NM_173074.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Darmochwal-Kolarz,D. and Chara,A.
  TITLE     The Association of IL-17 and PlGF/sENG Ratio in Pre-Eclampsia and
            Adverse Pregnancy Outcomes
  JOURNAL   Int J Environ Res Public Health 20 (1), 768 (2022)
   PUBMED   36613090
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Martinez-Varea,A., Martinez-Saez,C., Domenech,J., Desco-Blay,J.,
            Monfort-Pitarch,S., Hueso,M. and Diago-Almela,V.
  TITLE     sFlt-1/PlGF Ratio at 24 Weeks Gestation in Twin Pregnancies as a
            Predictor of Preeclampsia or Fetal Growth Restriction
  JOURNAL   Fetal Diagn Ther 49 (4), 206-214 (2022)
   PUBMED   35609518
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Oshovskyy,V., Arbuzova,S., Nikolenko,M. and Mylytsya,K.
  TITLE     PREGNANCY OUTCOMES IN WOMEN WITH EXTREMELY HIGH SFLT-1/PIGF RATIO:
            CASE SERIES
  JOURNAL   Wiad Lek 75 (1), 141-143 (2022)
   PUBMED   35092264
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Salian,S., Benkerroum,H., Nguyen,T.T.M., Nampoothiri,S.,
            Kinoshita,T., Felix,T.M., Stewart,F., Sisodiya,S.M., Murakami,Y.
            and Campeau,P.M.
  TITLE     PIGF deficiency causes a phenotype overlapping with DOORS syndrome
  JOURNAL   Hum Genet 140 (6), 879-884 (2021)
   PUBMED   33386993
  REMARK    GeneRIF: PIGF deficiency causes a phenotype overlapping with DOORS
            syndrome.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Yang,S.H., Wang,X.L., Cai,J. and Wang,S.H.
  TITLE     Diagnostic Value of Circulating PIGF in Combination with Flt-1 in
            Early Cervical Cancer
  JOURNAL   Curr Med Sci 40 (5), 973-978 (2020)
   PUBMED   33123910
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Hong,Y., Maeda,Y., Watanabe,R., Inoue,N., Ohishi,K. and
            Kinoshita,T.
  TITLE     Requirement of PIG-F and PIG-O for transferring phosphoethanolamine
            to the third mannose in glycosylphosphatidylinositol
  JOURNAL   J Biol Chem 275 (27), 20911-20919 (2000)
   PUBMED   10781593
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Ohishi,K., Inoue,N., Endo,Y., Fujita,T., Takeda,J. and Kinoshita,T.
  TITLE     Structure and chromosomal localization of the GPI-anchor synthesis
            gene PIGF and its pseudogene psi PIGF
  JOURNAL   Genomics 29 (3), 804-807 (1995)
   PUBMED   8575782
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Kinoshita,T., Takahashi,M., Inoue,N., Miyata,T. and Takeda,J.
  TITLE     Expression cloning of genes for GPI-anchor biosynthesis
  JOURNAL   Braz J Med Biol Res 27 (2), 127-132 (1994)
   PUBMED   8081220
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Inoue,N., Kinoshita,T., Orii,T. and Takeda,J.
  TITLE     Cloning of a human gene, PIG-F, a component of
            glycosylphosphatidylinositol anchor biosynthesis, by a novel
            expression cloning strategy
  JOURNAL   J Biol Chem 268 (10), 6882-6885 (1993)
   PUBMED   8463218
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018682.4 and BC029408.1.
            
            Summary: This gene encodes a protein involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor, a glycolipid containing three mannose molecules in its
            core backbone, is found on many blood cells where it serves to
            anchor proteins to the cell surface. The encoded protein and
            another GPI synthesis protein, PIGO, function in the transfer of
            ethanolaminephosphate to the third mannose in GPI. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) includes an alternate exon in
            the 3' coding region compared to variant 1. The encoded isoform (2)
            is shorter and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021725.1, BQ935543.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..206
                     /product="GPI ethanolamine phosphate transferase,
                     stabilizing subunit isoform 2"
                     /EC_number="2.7.8.1"
                     /note="phosphatidylinositol-glycan biosynthesis class F
                     protein; PIG-F; GPI11 homolog; GPI ethanolamine phosphate
                     transferase 2, stabilizing subunit; GPI ethanolamine
                     phosphate transferase 3, stabilizing subunit; GPI
                     ethanolamine phosphate transferase, stabilizing subunit"
                     /calculated_mol_wt=23260
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07326.1)"
     Region          21..182
                     /region_name="PIG-F"
                     /note="GPI biosynthesis protein family Pig-F; pfam06699"
                     /db_xref="CDD:461990"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07326.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07326.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07326.1)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07326.1)"
     CDS             1..206
                     /gene="PIGF"
                     /gene_synonym="OORS"
                     /coded_by="NM_173074.3:94..714"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1828.1"
                     /db_xref="GeneID:5281"
                     /db_xref="HGNC:HGNC:8962"
                     /db_xref="MIM:600153"
ORIGIN      
        1 mkdndikrll ythllcifsi ilsvfipslf lenfsileth ltwlcicsgf vtavnlvlyl
       61 vvkpntsskr sslshkvtgf lkcciyflms cfsfhvifvl ygaplielal etflfavils
      121 tfttvpclcl lgpnlkawlr vfsrngvtsi wenslqitti ssfvgawlga lpipldwerp
      181 wqmtverkrs tyrslhvpcr glgtvk
//
LOCUS       NP_001353516             805 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 20 [Homo
            sapiens].
ACCESSION   NP_001353516
VERSION     NP_001353516.1
DBSOURCE    REFSEQ: accession NM_001366587.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 805)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 805)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 805)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 805)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 805)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 805)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 805)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 805)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 805)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.231354.1,
                                           SRR1803617.52389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..805
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..805
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 20"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=90455
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <507..>641
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..805
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366587.1:2344..4761"
                     /note="isoform 20 is encoded by transcript variant 25"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels eseedkggkm
      361 aaadsvqqrr qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp
      421 rkrqketspr mqmgkrwqsp vtksgrrrrs psppptrrrr spspappprr rrtptppprr
      481 rtpsppprrr spsprryspp iqrryspspp pkrrtasppp ppkrraspsp ppkrrvshsp
      541 ppkqrsspvt krrspslssk hrkgsspsrs trearspqpn krhspsprpr apqtsssppp
      601 vrrgassspq rrqspspstr pirrvsrtpe pkkikkaasp spqsvrrvss srsvsgspep
      661 aakkppapps pvqsqspstn wspavpvkka ksptpspspp rnsdqegggk kkkkkkdkkh
      721 kkdkkhkkhk khkkekavaa aaaaavtpaa iaaatttlaq eepvaapepk keteseaedn
      781 lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_005041                606 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform a [Homo sapiens].
ACCESSION   NP_005041
VERSION     NP_005041.1
DBSOURCE    REFSEQ: accession NM_005050.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC332064.1, AF009746.1,
            BQ893869.1, BC012815.2, DA799558.1, BM667379.1, BF062605.1 and
            AC005519.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.267629.1, AF009746.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356924.9/ ENSP00000349396.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..606
                     /product="lysosomal cobalamin transporter ABCD4 isoform a"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=68467
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Region          68..603
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            279..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     CDS             1..606
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_005050.4:23..1843"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9828.1"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt lleqfviyqv
       61 glipsqyygv lgnkdlegfk tltflavmli vlnstlksfd qftcnllyvs wrkdltehlh
      121 rlyfrgrayy tlnvlrddid npdqrisqdv erfcrqlssm askliispft lvyytyqcfq
      181 stgwlgpvsi fgyfilgtvv nktlmgpivm klvhqekleg dfrfkhmqir vnaepaafyr
      241 aghvehmrtd rrlqrllqtq relmskelwl yigintfdyl gsilsyvvia ipifsgvygd
      301 lspaelstlv sknafvciyl iscftqlidl sttlsdvagy thrigqlret lldmslksqd
      361 ceilgesewg ldtppgwpaa epadtaflle rvsisapssd kplikdlslk isegqsllit
      421 gntgtgktsl lrvlgglwts trgsvqmltd fgphgvlflp qkpfftdgtl reqviyplke
      481 vypdsgsadd erilrflela glsnlvarte gldqqvdwnw ydvlspgemq rlsfarlfyl
      541 qpkyavldea tsalteeves elyrigqqlg mtfisvghrq slekfhslvl klcgggrwel
      601 mrikve
//
LOCUS       NP_001354594             753 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform bb [Homo sapiens].
ACCESSION   NP_001354594
VERSION     NP_001354594.1
DBSOURCE    REFSEQ: accession NM_001367665.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..753
                     /product="SUN domain-containing protein 1 isoform bb"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=83344
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          416..469
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(416,419..420,423,426..427,430..431,433..434,
                     437..438,440..441,444..445,447..448,451,454..455,458,
                     461..462,465..466,468..469)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          428..>561
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          546..604
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          647..751
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..753
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367665.1:52..2313"
                     /note="isoform bb is encoded by transcript variant 28"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllglslrgq gnffsflpvl nwasmhrtqr vddpqdvfkp ttsrlkqplq gdseafpwhw
      361 msgveqqvas lsgqchhhge nlrelttllq klqarvdqme ggaagpsasv rdavgqppre
      421 tdfmafhqeh evrmshledi lgklreksea iqkeleqtkq ktisavgeql lptvehlqle
      481 ldqlkselss wrhvktgcet vdavqervdv qvremvkllf sedqqggsle qllqrfssqf
      541 vskgdlqtml rdlqlqilrn vthhvsvtkq lptseavvsa vseagasgit eaqaraivns
      601 alklysqdkt gmvdfalesg ggsilstrcs etyetktalm slfgiplwyf sqsprvviqp
      661 diypgncwaf kgsqgylvvr lsmmihpaaf tlehipktls ptgnissapk dfavykrpdd
      721 tafqivelri fsnwghpeyt clyrfrvhge pvk
//
LOCUS       NP_542141                249 aa            linear   PRI 20-NOV-2025
DEFINITION  BPI fold-containing family A member 2 precursor [Homo sapiens].
ACCESSION   NP_542141 XP_114180
VERSION     NP_542141.1
DBSOURCE    REFSEQ: accession NM_080574.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kota,S.K., Pernicone,E., Leaf,D.E., Stillman,I.E., Waikar,S.S. and
            Kota,S.B.
  TITLE     BPI Fold-Containing Family A Member 2/Parotid Secretory Protein Is
            an Early Biomarker of AKI
  JOURNAL   J Am Soc Nephrol 28 (12), 3473-3478 (2017)
   PUBMED   28775000
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Prokopovic,V., Popovic,M., Andjelkovic,U., Marsavelski,A.,
            Raskovic,B., Gavrovic-Jankulovic,M. and Polovic,N.
  TITLE     Isolation, biochemical characterization and anti-bacterial activity
            of BPIFA2 protein
  JOURNAL   Arch Oral Biol 59 (3), 302-309 (2014)
   PUBMED   24581853
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Zeng,Z., Feingold,E., Wang,X., Weeks,D.E., Lee,M., Cuenco,D.T.,
            Broffitt,B., Weyant,R.J., Crout,R., McNeil,D.W., Levy,S.M.,
            Marazita,M.L. and Shaffer,J.R.
  TITLE     Genome-wide association study of primary dentition pit-and-fissure
            and smooth surface caries
  JOURNAL   Caries Res 48 (4), 330-338 (2014)
   PUBMED   24556642
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Bingle,L., Barnes,F.A., Lunn,H., Musa,M., Webster,S., Douglas,C.W.,
            Cross,S.S., High,A.S. and Bingle,C.D.
  TITLE     Characterisation and expression of SPLUNC2, the human orthologue of
            rodent parotid secretory protein
  JOURNAL   Histochem Cell Biol 132 (3), 339-349 (2009)
   PUBMED   19499239
  REMARK    GeneRIF: multiple SPLUNC2 isoforms are found in the oral cavity and
            suggest that these proteins may be differentially regulated in
            distinct tissues where they may function in the innate immune
            response.
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Ramachandran,P., Boontheung,P., Xie,Y., Sondej,M., Wong,D.T. and
            Loo,J.A.
  TITLE     Identification of N-linked glycoproteins in human saliva by
            glycoprotein capture and mass spectrometry
  JOURNAL   J Proteome Res 5 (6), 1493-1503 (2006)
   PUBMED   16740002
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Bingle,C.D. and Craven,C.J.
  TITLE     PLUNC: a novel family of candidate host defence proteins expressed
            in the upper airways and nasopharynx
  JOURNAL   Hum Mol Genet 11 (8), 937-943 (2002)
   PUBMED   11971875
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC065726.1.
            
            On Mar 22, 2004 this sequence version replaced XP_114180.1.
            
            Summary: This gene encodes a member of the palate, lung and nasal
            epithelium clone (Plunc) family of proteins. Members of this family
            have been proposed to play a role in the local antibacterial
            response in nose, mouth and upper respiratory pathways. The encoded
            soluble salivary protein binds bacterial lipopolysaccharide (LPS)
            and inhibits bacterial growth. This gene is present in a gene
            cluster on chromosome 20. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065726.1, AK291854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354932.6/ ENSP00000347012.5
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..249
                     /product="BPI fold-containing family A member 2 precursor"
                     /note="short palate, lung and nasal epithelium
                     carcinoma-associated protein 2; parotid secretory protein"
                     /calculated_mol_wt=24925
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2105
     mat_peptide     19..249
                     /product="BPI fold-containing family A member 2.
                     /id=PRO_0000017184"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DR5.2)"
                     /calculated_mol_wt=25054
     Region          62..227
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q96DR5.2)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q96DR5.2)"
     CDS             1..249
                     /gene="BPIFA2"
                     /gene_synonym="bA49G10.1; C20orf70; PSP; SPLUNC2"
                     /coded_by="NM_080574.4:67..816"
                     /db_xref="CCDS:CCDS13214.1"
                     /db_xref="GeneID:140683"
                     /db_xref="HGNC:HGNC:16203"
                     /db_xref="MIM:621166"
ORIGIN      
        1 mlqlwklvll cgvltgtses lldnlgndls nvvdklepvl hegletvdnt lkgileklkv
       61 dlgvlqkssa wqlakqkaqe aekllnnvis kllptntdif glkisnslil dvkaepiddg
      121 kglnlsfpvt anvtvagpii gqiinlkasl dlltavtiet dpqthqpvav lgecasdpts
      181 islslldkhs qiinkfvnsv intlkstvss llqkeicpli rifihsldvn viqqvvdnpq
      241 hktqlqtli
//
LOCUS       NP_000797                456 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-1 precursor [Homo
            sapiens].
ACCESSION   NP_000797
VERSION     NP_000797.2
DBSOURCE    REFSEQ: accession NM_000806.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Amjad,M., Tabassum,A., Sher,K., Kumar,S., Zehra,S. and Fatima,S.
  TITLE     Impact of GABAA receptor gene variants (rs2279020 and rs211037) on
            the risk of predisposition to epilepsy: a case-control study
  JOURNAL   Neurol Sci 43 (7), 4431-4438 (2022)
   PUBMED   35150350
  REMARK    GeneRIF: Impact of GABAA receptor gene variants (rs2279020 and
            rs211037) on the risk of predisposition to epilepsy: a case-control
            study.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Kasaragod,V.B., Mortensen,M., Hardwick,S.W., Wahid,A.A.,
            Dorovykh,V., Chirgadze,D.Y., Smart,T.G. and Miller,P.S.
  TITLE     Mechanisms of inhibition and activation of extrasynaptic alphabeta
            GABAA receptors
  JOURNAL   Nature 602 (7897), 529-533 (2022)
   PUBMED   35140402
  REMARK    Erratum:[Nature. 2022 Apr;604(7905):E15. doi:
            10.1038/s41586-022-04663-8. PMID: 35332337]
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Riaz,M., Abbasi,M.H., Sheikh,N., Saleem,T. and Virk,A.O.
  TITLE     GABRA1 and GABRA6 gene mutations in idiopathic generalized epilepsy
            patients
  JOURNAL   Seizure 93, 88-94 (2021)
   PUBMED   34740144
  REMARK    GeneRIF: GABRA1 and GABRA6 gene mutations in idiopathic generalized
            epilepsy patients.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Kang,I., Lindquist,D.G., Kinane,T.B., Ercolani,L., Pritchard,G.A.
            and Miller,L.G.
  TITLE     Isolation and characterization of the promoter of the human GABAA
            receptor alpha 1 subunit gene
  JOURNAL   J Neurochem 62 (4), 1643-1646 (1994)
   PUBMED   8133292
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Johnson,K.J., Sander,T., Hicks,A.A., van Marle,A., Janz,D.,
            Mullan,M.J., Riley,B.P. and Darlison,M.G.
  TITLE     Confirmation of the localization of the human GABAA receptor alpha
            1-subunit gene (GABRA1) to distal 5q by linkage analysis
  JOURNAL   Genomics 14 (3), 745-748 (1992)
   PUBMED   1330891
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Schofield,P.R., Pritchett,D.B., Sontheimer,H., Kettenmann,H. and
            Seeburg,P.H.
  TITLE     Sequence and expression of human GABAA receptor alpha 1 and beta 1
            subunits
  JOURNAL   FEBS Lett 244 (2), 361-364 (1989)
   PUBMED   2465923
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Garrett,K.M., Duman,R.S., Saito,N., Blume,A.J., Vitek,M.P. and
            Tallman,J.F.
  TITLE     Isolation of a cDNA clone for the alpha subunit of the human GABA-A
            receptor
  JOURNAL   Biochem Biophys Res Commun 156 (2), 1039-1045 (1988)
   PUBMED   2847710
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289792.1, X14766.1 and
            AC021079.4.
            
            On Nov 14, 2003 this sequence version replaced NP_000797.1.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammalian brain where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. Chloride conductance of these
            channels can be modulated by agents such as benzodiazepines that
            bind to the GABA-A receptor. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene cause juvenile
            myoclonic epilepsy and childhood absence epilepsy type 4. Multiple
            transcript variants encoding the same protein have been identified
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) uses the 5'-most alternate
            exon in the 5' UTR. Variants 1-7 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289792.1, SRR1660807.235868.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..456
                     /product="gamma-aminobutyric acid receptor subunit alpha-1
                     precursor"
                     /note="gamma-aminobutyric acid receptor subunit alpha-1;
                     GABA(A) receptor subunit alpha-1; GABA(A) receptor, alpha
                     1; gamma-aminobutyric acid (GABA) A receptor, alpha 1;
                     gamma-aminobutyric acid type A receptor alpha1 subunit;
                     GABAAR subunit alpha-1"
                     /calculated_mol_wt=48795
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14867.3)"
                     /calculated_mol_wt=3026
     Region          14..442
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     28..456
                     /product="Gamma-aminobutyric acid receptor subunit
                     alpha-1. /id=PRO_0000000428"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
                     /calculated_mol_wt=48795
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14867.3)"
     Region          56..249
                     /region_name="LGIC_ECD_GABAAR_A1"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-1 (GABAAR-A1 or GABRA1); cd19034"
                     /db_xref="CDD:349835"
     Site            order(64,92)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349835"
     Site            order(76,78..79,84..85,92,94..95,112,114..115,124..129,
                     132,134,136..137,143..145,147,157..159,187,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349835"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29950725,
                     ECO:0000269|PubMed:30602789, ECO:0007744|PDB:6D6T,
                     ECO:0007744|PDB:6D6U, ECO:0007744|PDB:6I53; propagated
                     from UniProtKB/Swiss-Prot (P14867.3)"
     Region          166..180
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349835"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            312..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            422..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     CDS             1..456
                     /gene="GABRA1"
                     /gene_synonym="DEE19; ECA4; EIEE19; EJM; EJM5"
                     /coded_by="NM_000806.5:469..1839"
                     /db_xref="CCDS:CCDS4357.1"
                     /db_xref="GeneID:2554"
                     /db_xref="HGNC:HGNC:4075"
                     /db_xref="MIM:137160"
ORIGIN      
        1 mrkspglsdc lwawilllst ltgrsygqps lqdelkdntt vftrildrll dgydnrlrpg
       61 lgervtevkt difvtsfgpv sdhdmeytid vffrqswkde rlkfkgpmtv lrlnnlmask
      121 iwtpdtffhn gkksvahnmt mpnkllrite dgtllytmrl tvraecpmhl edfpmdahac
      181 plkfgsyayt raevvyewtr eparsvvvae dgsrlnqydl lgqtvdsgiv qsstgeyvvm
      241 tthfhlkrki gyfviqtylp cimtvilsqv sfwlnresvp artvfgvttv ltmttlsisa
      301 rnslpkvaya tamdwfiavc yafvfsalie fatvnyftkr gyawdgksvv pekpkkvkdp
      361 likknntyap tatsytpnla rgdpglatia ksatiepkev kpetkppepk ktfnsvskid
      421 rlsriafpll fgifnlvywa tylnrepqlk aptphq
//
LOCUS       NP_061195                502 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor B precursor [Homo sapiens].
ACCESSION   NP_061195
VERSION     NP_061195.2
DBSOURCE    REFSEQ: accession NM_018725.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Kawamura,K., Matsumura,Y., Kawamura,T., Araki,H., Hamada,N.,
            Kuramoto,K., Yagi,H., Onoyama,I., Asanoma,K. and Kato,K.
  TITLE     Endometrial senescence is mediated by interleukin 17 receptor B
            signaling
  JOURNAL   Cell Commun Signal 22 (1), 363 (2024)
   PUBMED   39010112
  REMARK    GeneRIF: Endometrial senescence is mediated by interleukin 17
            receptor B signaling.
            Erratum:[Cell Commun Signal. 2024 Jul 22;22(1):370. doi:
            10.1186/s12964-024-01754-z. PMID: 39039545]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 502)
  AUTHORS   van Sluis,M., Yu,Q., van der Woude,M., Gonzalo-Hansen,C.,
            Dealy,S.C., Janssens,R.C., Somsen,H.B., Ramadhin,A.R.,
            Dekkers,D.H.W., Wienecke,H.L., Demmers,J.J.P.G., Raams,A.,
            Davo-Martinez,C., Llerena Schiffmacher,D.A., van Toorn,M.,
            Hackes,D., Thijssen,K.L., Zhou,D., Lammers,J.G., Pines,A.,
            Vermeulen,W., Pothof,J., Demmers,J.A.A., van den Berg,D.L.C.,
            Lans,H. and Marteijn,J.A.
  TITLE     Transcription-coupled DNA-protein crosslink repair by CSB and
            CRL4CSA-mediated degradation
  JOURNAL   Nat Cell Biol 26 (5), 770-783 (2024)
   PUBMED   38600236
  REMARK    GeneRIF: Transcription-coupled DNA-protein crosslink repair by CSB
            and CRL4[CSA]-mediated degradation.
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Yuan,S.F., Su,C.W., Chan,L.P., Nguyen,H.D.H., Chen,Y.K., Du,J.K.,
            Cheng,K.H. and Wang,Y.Y.
  TITLE     IL17RB expression is associated with malignant cancer behaviors and
            poor prognosis in oral cancer
  JOURNAL   Oral Dis 30 (4), 2027-2038 (2024)
   PUBMED   37448179
  REMARK    GeneRIF: IL17RB expression is associated with malignant cancer
            behaviors and poor prognosis in oral cancer.
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Wilson,S.C., Caveney,N.A., Yen,M., Pollmann,C., Xiang,X.,
            Jude,K.M., Hafer,M., Tsutsumi,N., Piehler,J. and Garcia,K.C.
  TITLE     Organizing structural principles of the IL-17 ligand-receptor axis
  JOURNAL   Nature 609 (7927), 622-629 (2022)
   PUBMED   35863378
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Deng,J., Zhang,T., Liu,F., Han,Q., Li,Q., Guo,X., Ma,Y., Li,L. and
            Shao,G.
  TITLE     CRL4-DCAF8L2 E3 ligase promotes ubiquitination and degradation of
            BARD1
  JOURNAL   Biochem Biophys Res Commun 611, 107-113 (2022)
   PUBMED   35487060
  REMARK    GeneRIF: CRL4-DCAF8L2 E3 ligase promotes ubiquitination and
            degradation of BARD1.
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Lee,J., Ho,W.H., Maruoka,M., Corpuz,R.T., Baldwin,D.T.,
            Foster,J.S., Goddard,A.D., Yansura,D.G., Vandlen,R.L., Wood,W.I.
            and Gurney,A.L.
  TITLE     IL-17E, a novel proinflammatory ligand for the IL-17 receptor
            homolog IL-17Rh1
  JOURNAL   J Biol Chem 276 (2), 1660-1664 (2001)
   PUBMED   11058597
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Shi,Y., Ullrich,S.J., Zhang,J., Connolly,K., Grzegorzewski,K.J.,
            Barber,M.C., Wang,W., Wathen,K., Hodge,V., Fisher,C.L., Olsen,H.,
            Ruben,S.M., Knyazev,I., Cho,Y.H., Kao,V., Wilkinson,K.A.,
            Carrell,J.A. and Ebner,R.
  TITLE     A novel cytokine receptor-ligand pair. Identification, molecular
            characterization, and in vivo immunomodulatory activity
  JOURNAL   J Biol Chem 275 (25), 19167-19176 (2000)
   PUBMED   10749887
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Tian,E., Sawyer,J.R., Largaespada,D.A., Jenkins,N.A., Copeland,N.G.
            and Shaughnessy,J.D. Jr.
  TITLE     Evi27 encodes a novel membrane protein with homology to the IL17
            receptor
  JOURNAL   Oncogene 19 (17), 2098-2109 (2000)
   PUBMED   10815801
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Schwandner,R., Yamaguchi,K. and Cao,Z.
  TITLE     Requirement of tumor necrosis factor receptor-associated factor
            (TRAF)6 in interleukin 17 signal transduction
  JOURNAL   J Exp Med 191 (7), 1233-1240 (2000)
   PUBMED   10748240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA093617.1 and BC000980.1.
            
            On Jan 3, 2003 this sequence version replaced NP_061195.1.
            
            Summary: The protein encoded by this gene is a cytokine receptor.
            This receptor specifically binds to IL17B and IL17E, but does not
            bind to IL17 and IL17C. This receptor has been shown to mediate the
            activation of NF-kappaB and the production of IL8 induced by IL17E.
            The expression of the rat counterpart of this gene was found to be
            significantly up-regulated during intestinal inflammation, which
            suggested the immunoregulatory activity of this receptor. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.254406.1,
                                           SRR1803615.62904.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000288167.8/ ENSP00000288167.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..502
                     /product="interleukin-17 receptor B precursor"
                     /note="IL-17B receptor; interleukin 17 receptor homolog 1;
                     cytokine receptor CRL4; IL-17RB; IL-17Rh1; IL-17 receptor
                     B; IL-17 receptor homolog 1; cytokine receptor-like 4;
                     interleukin-17B receptor"
                     /calculated_mol_wt=54426
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1477
     mat_peptide     18..502
                     /product="interleukin-17 receptor B"
                     /calculated_mol_wt=54159
     Region          33..175
                     /region_name="IL17R_fnIII_D1"
                     /note="Interleukin-17 receptor, fibronectin-III-like
                     domain 1; pfam16556"
                     /db_xref="CDD:435426"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Region          176..268
                     /region_name="IL17R_fnIII_D2"
                     /note="Interleukin 17 receptor D; pfam16578"
                     /db_xref="CDD:465185"
     Site            183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRM6.2)"
     Region          332..479
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..502
                     /gene="IL17RB"
                     /gene_synonym="CRL4; EVI27; IL17BR; IL17RH1"
                     /coded_by="NM_018725.4:22..1530"
                     /db_xref="CCDS:CCDS2874.1"
                     /db_xref="GeneID:55540"
                     /db_xref="HGNC:HGNC:18015"
                     /db_xref="MIM:605458"
ORIGIN      
        1 mslvllslaa lcrsavprep tvqcgsetgp spewmlqhdl ipgdlrdlrv epvttsvatg
       61 dysilmnvsw vlradasirl lkatkicvtg ksnfqsyscv rcnyteafqt qtrpsggkwt
      121 fsyigfpvel ntvyfigahn ipnanmnedg psmsvnftsp gcldhimkyk kkcvkagslw
      181 dpnitackkn eetvevnftt tplgnrymal iqhstiigfs qvfephqkkq trasvvipvt
      241 gdsegatvql tpyfptcgsd cirhkgtvvl cpqtgvpfpl dnnkskpggw lpllllsllv
      301 atwvlvagiy lmwrherikk tsfstttllp pikvlvvyps eicfhhticy fteflqnhcr
      361 sevilekwqk kkiaemgpvq wlatqkkaad kvvfllsndv nsvcdgtcgk segspsensq
      421 dlfplafnlf csdlrsqihl hkyvvvyfre idtkddynal svcpkyhlmk datafcaell
      481 hvkqqvsagk rsqachdgcc sl
//
LOCUS       NP_550438                277 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxyguanosine kinase, mitochondrial isoform a precursor [Homo
            sapiens].
ACCESSION   NP_550438
VERSION     NP_550438.1
DBSOURCE    REFSEQ: accession NM_080916.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Guzman,H., Yazdani,S., Harmon,J.L., Chapman,K.A., Vitola,B.,
            Pyle,L., McKnight,H., Sigal,W., Lord,K., De Leon,D.D., Merchant,N.
            and Ganetzky,R.
  TITLE     Case report: Two unexpected cases of DGUOK-related mitochondrial
            DNA depletion syndrome presenting with hyperinsulinemic
            hypoglycemia
  JOURNAL   Front Endocrinol (Lausanne) 14, 1268135 (2023)
   PUBMED   38027095
  REMARK    GeneRIF: Case report: Two unexpected cases of DGUOK-related
            mitochondrial DNA depletion syndrome presenting with
            hyperinsulinemic hypoglycemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Unal,O., Hismi,B., Kilic,M., Gulsen,H.H., Coskun,T., Sivri,S.H.,
            Dursun,A., Yuce,A. and Tokatli,A.
  TITLE     Deoxyguanosine kinase deficiency: a report of four patients
  JOURNAL   J Pediatr Endocrinol Metab 30 (6), 697-702 (2017)
   PUBMED   28493820
  REMARK    GeneRIF: DGUOK deficiency and mutation is associated with
            mitochondrial DNA depletion syndromes.
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Jullig,M. and Eriksson,S.
  TITLE     Mitochondrial and submitochondrial localization of human
            deoxyguanosine kinase
  JOURNAL   Eur J Biochem 267 (17), 5466-5472 (2000)
   PUBMED   10951205
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Johansson,M., Bajalica-Lagercrantz,S., Lagercrantz,J. and
            Karlsson,A.
  TITLE     Localization of the human deoxyguanosine kinase gene (DGUOK) to
            chromosome 2p13
  JOURNAL   Genomics 38 (3), 450-451 (1996)
   PUBMED   8975728
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Wang,L., Hellman,U. and Eriksson,S.
  TITLE     Cloning and expression of human mitochondrial deoxyguanosine kinase
            cDNA
  JOURNAL   FEBS Lett 390 (1), 39-43 (1996)
   PUBMED   8706825
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning and expression of human deoxyguanosine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7258-7262 (1996)
   PUBMED   8692979
REFERENCE   10 (residues 1 to 277)
  AUTHORS   El-Hattab,A.W. and Scaglia,F.
  TITLE     Deoxyguanosine Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG708680.1, BC015757.1 and
            U41668.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: In mammalian cells, the phosphorylation of purine
            deoxyribonucleosides is mediated predominantly by two
            deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and
            mitochondrial deoxyguanosine kinase. The protein encoded by this
            gene is responsible for phosphorylation of purine
            deoxyribonucleosides in the mitochondrial matrix. In addition, this
            protein phosphorylates several purine deoxyribonucleoside analogs
            used in the treatment of lymphoproliferative disorders, and this
            phosphorylation is critical for the effectiveness of the analogs.
            Alternative splice variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.4192.1,
                                           SRR5189658.153031.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000264093.9/
                                                  ENSP00000264093.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..277
                     /product="deoxyguanosine kinase, mitochondrial isoform a
                     precursor"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxyguanosine kinase, mitochondrial;
                     deoxyadenosine kinase, mitochondrial"
                     /calculated_mol_wt=27961
     transit_peptide 1..39
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q16854.2)"
                     /calculated_mol_wt=4113
     mat_peptide     40..277
                     /product="Deoxyguanosine kinase, mitochondrial.
                     /id=PRO_0000016840"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16854.2)"
                     /calculated_mol_wt=27961
     Region          41..275
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            order(49,51..52,100,110..111,151,206,211)
                     /site_type="other"
                     /note="Substrate-binding site [chemical binding]"
                     /db_xref="CDD:238836"
     Site            118
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16854.2)"
     CDS             1..277
                     /gene="DGUOK"
                     /gene_synonym="dGK; MTDPS3; NCPH; NCPH1; PEOB4"
                     /coded_by="NM_080916.3:32..865"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1931.1"
                     /db_xref="GeneID:1716"
                     /db_xref="HGNC:HGNC:2858"
                     /db_xref="MIM:601465"
ORIGIN      
        1 maagrlflsr lrapfssmak splegvsssr glhagrgprr lsiegniavg kstfvklltk
       61 typewhvate pvatwqniqa agtqkactaq slgnlldmmy reparwsytf qtfsflsrlk
      121 vqlepfpekl lqarkpvqif ersvysdryi faknlfengs lsdiewhiyq dwhsfllwef
      181 asritlhgfi ylqaspqvcl krlyqraree ekgielayle qlhgqheawl ihkttklhfe
      241 almnipvlvl dvnddfseev tkqedlmrev ntfvknl
//
LOCUS       NP_001357339             144 aa            linear   PRI 20-NOV-2025
DEFINITION  protein BUD31 homolog [Homo sapiens].
ACCESSION   NP_001357339 XP_016868251
VERSION     NP_001357339.1
DBSOURCE    REFSEQ: accession NM_001370410.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wu,X., Fan,R., Zhang,Y., Duan,C., Yao,X., Liu,K., Lin,D. and
            Chen,Z.
  TITLE     The role of BUD31 in clear cell renal cell carcinoma: prognostic
            significance, alternative splicing, and tumor immune environment
  JOURNAL   Clin Exp Med 24 (1), 191 (2024)
   PUBMED   39136845
  REMARK    GeneRIF: The role of BUD31 in clear cell renal cell carcinoma:
            prognostic significance, alternative splicing, and tumor immune
            environment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Choudhry,M., Gamallat,Y., Khosh Kish,E., Seyedi,S., Gotto,G.,
            Ghosh,S. and Bismar,T.A.
  TITLE     Downregulation of BUD31 Promotes Prostate Cancer Cell Proliferation
            and Migration via Activation of p-AKT and Vimentin In Vitro
  JOURNAL   Int J Mol Sci 24 (7), 6055 (2023)
   PUBMED   37047027
  REMARK    GeneRIF: Downregulation of BUD31 Promotes Prostate Cancer Cell
            Proliferation and Migration via Activation of p-AKT and Vimentin In
            Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Xu,W., Huang,H., Yu,L. and Cao,L.
  TITLE     Meta-analysis of gene expression profiles indicates genes in
            spliceosome pathway are up-regulated in hepatocellular carcinoma
            (HCC)
  JOURNAL   Med Oncol 32 (4), 96 (2015)
   PUBMED   25731616
  REMARK    GeneRIF: High BUD31 expression is associated with hepatocellular
            carcinoma.
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Hsu,C.L., Liu,J.S., Wu,P.L., Guan,H.H., Chen,Y.L., Lin,A.C.,
            Ting,H.J., Pang,S.T., Yeh,S.D., Ma,W.L., Chen,C.J., Wu,W.G. and
            Chang,C.
  TITLE     Identification of a new androgen receptor (AR) co-regulator BUD31
            and related peptides to suppress wild-type and mutated AR-mediated
            prostate cancer growth via peptide screening and X-ray structure
            analysis
  JOURNAL   Mol Oncol 8 (8), 1575-1587 (2014)
   PUBMED   25091737
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Hla,T., Jackson,A.Q., Appleby,S.B. and Maciag,T.
  TITLE     Characterization of edg-2, a human homologue of the Xenopus
            maternal transcript G10 from endothelial cells
  JOURNAL   Biochim Biophys Acta 1260 (2), 227-229 (1995)
   PUBMED   7841202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004922.2.
            
            On May 7, 2019 this sequence version replaced XP_016868251.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.405506.1,
                                           SRR1163658.416355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..144
                     /product="protein BUD31 homolog"
                     /note="maternal G10 transcript; functional
                     spliceosome-associated protein 17; protein EDG-2; protein
                     G10 homolog; G10 maternal transcript homolog; BUD31
                     homolog"
                     /calculated_mol_wt=16869
     Region          1..143
                     /region_name="G10"
                     /note="G10 protein; pfam01125"
                     /db_xref="CDD:426066"
     Region          2..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Region          59..67
                     /region_name="Interaction with AR.
                     /evidence=ECO:0000269|PubMed:28076346"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41223.2)"
     CDS             1..144
                     /gene="BUD31"
                     /gene_synonym="Cwc14; EDG-2; EDG2; fSAP17; G10; YCR063W"
                     /coded_by="NM_001370410.1:199..633"
                     /db_xref="CCDS:CCDS5663.1"
                     /db_xref="GeneID:8896"
                     /db_xref="HGNC:HGNC:29629"
                     /db_xref="MIM:603477"
ORIGIN      
        1 mpkvkrsrka ppdgweliep tldeldqkmr eaetephegk rkveslwpif rihhqktryi
       61 fdlfykrkai srelyeycik egyadknlia kwkkqgyenl cclrciqtrd tnfgtncicr
      121 vpksklevgr iiecthcgcr gcsg
//
LOCUS       NP_000734                505 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-3 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_000734
VERSION     NP_000734.2
DBSOURCE    REFSEQ: accession NM_000743.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Chmielowiec,K., Chmielowiec,J., Stronska-Pluta,A., Trybek,G.,
            Smiarowska,M., Suchanecka,A., Wozniak,G., Jaron,A. and Grzywacz,A.
  TITLE     Association of Polymorphism CHRNA5 and CHRNA3 Gene in People
            Addicted to Nicotine
  JOURNAL   Int J Environ Res Public Health 19 (17), 10478 (2022)
   PUBMED   36078193
  REMARK    GeneRIF: Association of Polymorphism CHRNA5 and CHRNA3 Gene in
            People Addicted to Nicotine.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kitazaki,Y., Ikawa,M., Kishitani,T., Kamisawa,T., Nakane,S.,
            Nakamoto,Y. and Hamano,T.
  TITLE     Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies
  JOURNAL   Intern Med 60 (14), 2307-2313 (2021)
   PUBMED   33583893
  REMARK    GeneRIF: Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Shibao,C.A., Joos,K., Phillips,J.A. 3rd, Cogan,J., Newman,J.H.,
            Hamid,R., Meiler,J., Capra,J., Sheehan,J., Vetrini,F., Yang,Y.,
            Black,B., Diedrich,A., Roberston,D. and Biaggioni,I.
  TITLE     Familial Autonomic Ganglionopathy Caused by Rare CHRNA3 Genetic
            Variants
  JOURNAL   Neurology 97 (2), e145-e155 (2021)
   PUBMED   33947782
  REMARK    GeneRIF: Familial Autonomic Ganglionopathy Caused by Rare CHRNA3
            Genetic Variants.
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Yi,X., Li,W., Wang,Y., Chen,X., Ye,F., Sun,G. and Chen,J.
  TITLE     The relationship between CHRNA5/A3/B4 gene cluster polymorphisms
            and lung cancer risk: An updated meta-analysis and systematic
            review
  JOURNAL   Medicine (Baltimore) 100 (6), e24355 (2021)
   PUBMED   33578531
  REMARK    GeneRIF: The relationship between CHRNA5/A3/B4 gene cluster
            polymorphisms and lung cancer risk: An updated meta-analysis and
            systematic review.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Wang,F., Gerzanich,V., Wells,G.B., Anand,R., Peng,X., Keyser,K. and
            Lindstrom,J.
  TITLE     Assembly of human neuronal nicotinic receptor alpha5 subunits with
            alpha3, beta2, and beta4 subunits
  JOURNAL   J Biol Chem 271 (30), 17656-17665 (1996)
   PUBMED   8663494
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Raimondi,E., Rubboli,F., Moralli,D., Chini,B., Fornasari,D.,
            Tarroni,P., De Carli,L. and Clementi,F.
  TITLE     Chromosomal localization and physical linkage of the genes encoding
            the human alpha 3, alpha 5, and beta 4 neuronal nicotinic receptor
            subunits
  JOURNAL   Genomics 12 (4), 849-850 (1992)
   PUBMED   1572664
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Eng,C.M., Kozak,C.A., Beaudet,A.L. and Zoghbi,H.Y.
  TITLE     Mapping of multiple subunits of the neuronal nicotinic
            acetylcholine receptor to chromosome 15 in man and chromosome 9 in
            mouse
  JOURNAL   Genomics 9 (2), 278-282 (1991)
   PUBMED   2004777
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Mihovilovic,M. and Roses,A.D.
  TITLE     Expression of mRNAs in human thymus coding for the alpha 3 subunit
            of a neuronal acetylcholine receptor
  JOURNAL   Exp Neurol 111 (2), 175-180 (1991)
   PUBMED   1989896
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Papke,R.L. and Heinemann,S.F.
  TITLE     The role of the beta 4-subunit in determining the kinetic
            properties of rat neuronal nicotinic acetylcholine alpha
            3-receptors
  JOURNAL   J Physiol 440, 95-112 (1991)
   PUBMED   1725184
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Fornasari,D., Chini,B., Tarroni,P. and Clementi,F.
  TITLE     Molecular cloning of human neuronal nicotinic receptor alpha
            3-subunit
  JOURNAL   Neurosci Lett 111 (3), 351-356 (1990)
   PUBMED   2336208
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC006114.1, BC002996.1,
            AC027228.16, BM666615.1 and AI833126.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_000734.1.
            
            Summary: This locus encodes a member of the nicotinic acetylcholine
            receptor family of proteins. Members of this family of proteins
            form pentameric complexes comprised of both alpha and beta
            subunits. This locus encodes an alpha-type subunit, as it contains
            characteristic adjacent cysteine residues. The encoded protein is a
            ligand-gated ion channel that likely plays a role in
            neurotransmission. Polymorphisms in this gene have been associated
            with an increased risk of smoking initiation and an increased
            susceptibility to lung cancer. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098443.1, SRR1660805.149200.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000326828.6/
                                                ENSP00000315602.5
            RefSeq Select criteria           :: based on conservation,
                                                expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..505
                     /product="neuronal acetylcholine receptor subunit alpha-3
                     isoform 1 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     3; neuronal nicotinic acetylcholine receptor, alpha3
                     subunit; cholinergic receptor, nicotinic, alpha 3
                     (neuronal); cholinergic receptor, nicotinic alpha 3"
                     /calculated_mol_wt=54306
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3193
     Region          30..496
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     32..505
                     /product="Neuronal acetylcholine receptor subunit alpha-3.
                     /id=PRO_0000000346"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
                     /calculated_mol_wt=54306
     Region          35..241
                     /region_name="LGIC_ECD_nAChR_A3"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit alpha 3 (CHRNA3); cd19016"
                     /db_xref="CDD:349817"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            order(70,72,78..79,86,108,110,119..120,122,124..125,129,
                     131..132,136..138,140,150,152,154,158,180,240)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349817"
     Region          159..173
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349817"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            251..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            269..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            308..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            475..493
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     CDS             1..505
                     /gene="CHRNA3"
                     /gene_synonym="BAIPRCK; LNCR2; NACHRA3; PAOD2"
                     /coded_by="NM_000743.5:203..1720"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10305.1"
                     /db_xref="GeneID:1136"
                     /db_xref="HGNC:HGNC:1957"
                     /db_xref="MIM:118503"
ORIGIN      
        1 mgsgplslpl alspprllll lllsllpvar aseaehrlfe rlfedyneii rpvanvsdpv
       61 iihfevsmsq lvkvdevnqi metnlwlkqi wndyklkwnp sdyggaefmr vpaqkiwkpd
      121 ivlynnavgd fqvddktkal lkytgevtwi ppaifkssck idvtyfpfdy qnctmkfgsw
      181 sydkakidlv ligssmnlkd ywesgewaii kapgykhdik yncceeiypd ityslyirrl
      241 plfytinlii pcllisfltv lvfylpsdcg ekvtlcisvl lsltvfllvi tetipstslv
      301 ipligeyllf tmifvtlsiv itvfvlnvhy rtptthtmps wvktvflnll prvmfmtrpt
      361 snegnaqkpr plygaelsnl ncfsraeskg ckegypcqdg mcgychhrri kisnfsanlt
      421 rssssesvda vlslsalspe ikeaiqsvky iaenmkaqne akeiqddwky vamvidrifl
      481 wvftlvcilg taglflqplm areda
//
LOCUS       NP_001278771             366 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform Ik-7(del) [Homo sapiens].
ACCESSION   NP_001278771
VERSION     NP_001278771.1
DBSOURCE    REFSEQ: accession NM_001291842.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U40462.1 and JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (Ik-7(del)) lacks two consecutive
            in-frame exons in the central coding region, and uses an alternate
            in-frame splice site in the 3' coding region, compared to variant
            1. The encoded isoform (Ik-7(del)) is shorter than isoform 1. This
            isoform contains only one N-terminal zinc finger motif, and
            represents a non-DNA-binding, dominant-negative isoform
            (PMID:9892693).
            
            Sequence Note: The 5' UTR of this variant is incomplete because
            there are no full-length transcripts supporting this variant, and
            there is splicing ambiguity in the 5' UTR.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 9892693
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..366
                     /product="DNA-binding protein Ikaros isoform Ik-7(del)"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=40648
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          60..81
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..366
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291842.1:15..1115"
                     /note="isoform Ik-7(del) is encoded by transcript variant
                     Ik-7(del)"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvgkphkc
       61 gycgrsykqr ssleehkerc hnylesmglp gtlypvikee tnhsemaedl ckigserslv
      121 ldrlasnvak rdkglsdtpy dssasyeken emmkshvmdq ainnainylg aeslrplvqt
      181 ppggsevvpv ispmyqlhkp laegtprsnh saqdsavenl lllskaklvp sereaspsns
      241 cqdstdtesn neeqrsgliy ltnhiaphar nglslkeehr aydllraase nsqdalrvvs
      301 tsgeqmkvyk cehcrvlfld hvmytihmgc hgfrdpfecn mcgyhsqdry efsshitrge
      361 hrfhms
//
LOCUS       NP_002724                331 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-AMP-activated protein kinase subunit gamma-1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002724
VERSION     NP_002724.1
DBSOURCE    REFSEQ: accession NM_002733.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Bai,W., Guo,T., Wang,H., Li,B., Sun,Q., Wu,W., Zhang,J., Zhou,J.,
            Luo,J., Zhu,M., Lu,J., Li,P., Dong,B., Han,S., Pang,X., Zhang,G.,
            Bai,Y. and Wang,S.
  TITLE     S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming
  JOURNAL   EMBO Rep 25 (1), 128-143 (2024)
   PUBMED   38177907
  REMARK    GeneRIF: S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming.
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Dyck,J.R., Gao,G., Widmer,J., Stapleton,D., Fernandez,C.S.,
            Kemp,B.E. and Witters,L.A.
  TITLE     Regulation of 5'-AMP-activated protein kinase activity by the
            noncatalytic beta and gamma subunits
  JOURNAL   J Biol Chem 271 (30), 17798-17803 (1996)
   PUBMED   8663446
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Gao,G., Fernandez,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
            Dyck,J.R., Kemp,B.E. and Witters,L.A.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J Biol Chem 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Stapleton,D., Mitchelhill,K.I., Gao,G., Widmer,J., Michell,B.J.,
            Teh,T., House,C.M., Fernandez,C.S., Cox,T., Witters,L.A. and
            Kemp,B.E.
  TITLE     Mammalian AMP-activated protein kinase subfamily
  JOURNAL   J Biol Chem 271 (2), 611-614 (1996)
   PUBMED   8557660
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Hofmann,B., Nishanian,P., Nguyen,T., Insixiengmay,P. and Fahey,J.L.
  TITLE     Human immunodeficiency virus proteins induce the inhibitory
            cAMP/protein kinase A pathway in normal lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6676-6680 (1993)
   PUBMED   7688126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB020277.1, BC000358.2 and
            BM667691.1.
            
            Summary: The protein encoded by this gene is a regulatory subunit
            of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer
            consisting of an alpha catalytic subunit, and non-catalytic beta
            and gamma subunits. AMPK is an important energy-sensing enzyme that
            monitors cellular energy status. In response to cellular metabolic
            stresses, AMPK is activated, and thus phosphorylates and
            inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy
            beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in
            regulating de novo biosynthesis of fatty acid and cholesterol. This
            subunit is one of the gamma regulatory subunits of AMPK.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.114863.1,
                                           SRR3476690.679797.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000548065.7/ ENSP00000447433.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..331
                     /product="5'-AMP-activated protein kinase subunit gamma-1
                     isoform 1"
                     /note="AMPK gamma-1 chain; 5'-AMP-activated protein
                     kinase, gamma-1 subunit; AMPK gamma1; protein kinase,
                     AMP-activated, gamma 1 non-catalytic subunit"
                     /calculated_mol_wt=37448
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54619.1)"
     Region          38..174
                     /region_name="CBS_euAMPK_gamma-like_repeat1"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains found in AMP-activated
                     protein kinase gamma-like proteins, repeat 1; cd04618"
                     /db_xref="CDD:341388"
     Site            order(45,47..49,71..73,152,166,168,170..171,174)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341388"
     Region          45..118
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Site            order(71,85,89..90,93,130,152..154,170)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341388"
     Region          130..174
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Region          138..159
                     /region_name="AMPK pseudosubstrate"
                     /note="propagated from UniProtKB/Swiss-Prot (P54619.1)"
     Region          200..323
                     /region_name="CBS_euAMPK_gamma-like_repeat2"
                     /note="CBS pair domain found in 5'-AMP (adenosine
                     monophosphate)-activated protein kinase; cd04641"
                     /db_xref="CDD:341399"
     Site            order(201,203..205,227..229,299,312,314,316..317,320)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341399"
     Region          201..266
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     Site            order(227,240,244..245,248,277,299..301,316)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341399"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000250|UniProtKB:P80385; propagated from
                     UniProtKB/Swiss-Prot (P54619.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ULK1.
                     /evidence=ECO:0000250|UniProtKB:P80385; propagated from
                     UniProtKB/Swiss-Prot (P54619.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000250|UniProtKB:P80385; propagated from
                     UniProtKB/Swiss-Prot (P54619.1)"
     Region          277..320
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     CDS             1..331
                     /gene="PRKAG1"
                     /gene_synonym="AMPKG"
                     /coded_by="NM_002733.5:37..1032"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8777.1"
                     /db_xref="GeneID:5571"
                     /db_xref="HGNC:HGNC:9385"
                     /db_xref="MIM:602742"
ORIGIN      
        1 metvissdss pavenehpqe tpesnnsvyt sfmkshrcyd liptssklvv fdtslqvkka
       61 ffalvtngvr aaplwdskkq sfvgmltitd finilhryyk salvqiyele ehkietwrev
      121 ylqdsfkplv cispnaslfd avsslirnki hrlpvidpes gntlyilthk rilkflklfi
      181 tefpkpefms ksleelqigt yaniamvrtt tpvyvalgif vqhrvsalpv vdekgrvvdi
      241 yskfdvinla aektynnldv svtkalqhrs hyfegvlkcy lhetletiin rlveaevhrl
      301 vvvdendvvk givslsdilq alvltggekk p
//
LOCUS       NP_001155045             164 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor MafF isoform a [Homo sapiens].
ACCESSION   NP_001155045
VERSION     NP_001155045.1
DBSOURCE    REFSEQ: accession NM_001161573.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Moon,E.J., Mello,S.S., Li,C.G., Chi,J.T., Thakkar,K.,
            Kirkland,J.G., Lagory,E.L., Lee,I.J., Diep,A.N., Miao,Y., Rafat,M.,
            Vilalta,M., Castellini,L., Krieg,A.J., Graves,E.E., Attardi,L.D.
            and Giaccia,A.J.
  TITLE     The HIF target MAFF promotes tumor invasion and metastasis through
            IL11 and STAT3 signaling
  JOURNAL   Nat Commun 12 (1), 4308 (2021)
   PUBMED   34262028
  REMARK    GeneRIF: The HIF target MAFF promotes tumor invasion and metastasis
            through IL11 and STAT3 signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Ibrahim,M.K., Abdelhafez,T.H., Takeuchi,J.S., Wakae,K.,
            Sugiyama,M., Tsuge,M., Ito,M., Watashi,K., El Kassas,M., Kato,T.,
            Murayama,A., Suzuki,T., Chayama,K., Shimotohno,K., Muramatsu,M.,
            Aly,H.H. and Wakita,T.
  TITLE     MafF Is an Antiviral Host Factor That Suppresses Transcription from
            Hepatitis B Virus Core Promoter
  JOURNAL   J Virol 95 (15), e0076721 (2021)
   PUBMED   33980595
  REMARK    GeneRIF: MafF Is an Antiviral Host Factor That Suppresses
            Transcription from Hepatitis B Virus Core Promoter.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Kataoka,K., Yoshitomo-Nakagawa,K., Shioda,S. and Nishizawa,M.
  TITLE     A set of Hox proteins interact with the Maf oncoprotein to inhibit
            its DNA binding, transactivation, and transforming activities
  JOURNAL   J Biol Chem 276 (1), 819-826 (2001)
   PUBMED   11036080
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Kimura,T., Ivell,R., Rust,W., Mizumoto,Y., Ogita,K., Kusui,C.,
            Matsumura,Y., Azuma,C. and Murata,Y.
  TITLE     Molecular cloning of a human MafF homologue, which specifically
            binds to the oxytocin receptor gene in term myometrium
  JOURNAL   Biochem Biophys Res Commun 264 (1), 86-92 (1999)
   PUBMED   10527846
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Johnsen,O., Skammelsrud,N., Luna,L., Nishizawa,M., Prydz,H. and
            Kolsto,A.B.
  TITLE     Small Maf proteins interact with the human transcription factor
            TCF11/Nrf1/LCR-F1
  JOURNAL   Nucleic Acids Res 24 (21), 4289-4297 (1996)
   PUBMED   8932385
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Armstrong,J.A. and Emerson,B.M.
  TITLE     NF-E2 disrupts chromatin structure at human beta-globin locus
            control region hypersensitive site 2 in vitro
  JOURNAL   Mol Cell Biol 16 (10), 5634-5644 (1996)
   PUBMED   8816476
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Igarashi,K., Kataoka,K., Itoh,K., Hayashi,N., Nishizawa,M. and
            Yamamoto,M.
  TITLE     Regulation of transcription by dimerization of erythroid factor
            NF-E2 p45 with small Maf proteins
  JOURNAL   Nature 367 (6463), 568-572 (1994)
   PUBMED   8107826
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA425613.1, AK002001.1,
            DB319587.1, AJ010857.1 and AI610651.1.
            
            Summary: The protein encoded by this gene is a basic leucine zipper
            (bZIP) transcription factor that lacks a transactivation domain. It
            is known to bind the US-2 DNA element in the promoter of the
            oxytocin receptor (OTR) gene and most likely heterodimerizes with
            other leucine zipper-containing proteins to enhance expression of
            the OTR gene during term pregnancy. The encoded protein can also
            form homodimers, and since it lacks a transactivation domain, the
            homodimer may act as a repressor of transcription. This gene may
            also be involved in the cellular stress response. Multiple
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 3. Variants 1, 3, and 4 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA425613.1, DA872919.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..164
                     /product="transcription factor MafF isoform a"
                     /note="v-maf avian musculoaponeurotic fibrosarcoma
                     oncogene family protein F; transcription factor MAFF;
                     v-maf avian musculoaponeurotic fibrosarcoma oncogene
                     homolog F"
                     /calculated_mol_wt=17629
     Region          47..115
                     /region_name="bZIP_Maf_small"
                     /note="Basic leucine zipper (bZIP) domain of small
                     musculoaponeurotic fibrosarcoma (Maf) proteins: a
                     DNA-binding and dimerization domain; cd14717"
                     /db_xref="CDD:269865"
     Region          47..115
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269865"
     Region          51..76
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     Site            order(56..58,60..62,64..65,68..69,71..72)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269865"
     Site            order(72,75..76,79..80,82..83,86..87,89..90,93,96..97,100,
                     103..104,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269865"
     Region          78..>162
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     Region          79..93
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     Region          141..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     CDS             1..164
                     /gene="MAFF"
                     /gene_synonym="hMafF; U-MAF"
                     /coded_by="NM_001161573.1:97..591"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13968.1"
                     /db_xref="GeneID:23764"
                     /db_xref="HGNC:HGNC:6780"
                     /db_xref="MIM:604877"
ORIGIN      
        1 msvdplsska lkikrelsen tphlsdealm glsvrelnrh lrglsaeevt rlkqrrrtlk
       61 nrgyaascrv krvcqkeelq kqkselerev dklarenaam rleldalrgk cealqgfars
      121 vaaargpatl vapasvitiv kstpgsgsgp ahgpdpahgp ascs
//
LOCUS       NP_055414                606 aa            linear   PRI 20-NOV-2025
DEFINITION  melanoma-associated antigen D2 [Homo sapiens].
ACCESSION   NP_055414 NP_006778
VERSION     NP_055414.2
DBSOURCE    REFSEQ: accession NM_014599.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Yan,X., Hu,Y., Zhang,X., Gao,X., Zhao,Y., Peng,H., Ouyang,L. and
            Zhang,C.
  TITLE     Identification of a novel intronic mutation of MAGED2 gene in a
            Chinese family with antenatal Bartter syndrome
  JOURNAL   BMC Med Genomics 17 (1), 23 (2024)
   PUBMED   38238844
  REMARK    GeneRIF: Identification of a novel intronic mutation of MAGED2 gene
            in a Chinese family with antenatal Bartter syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Shi,X., Liu,C., Zheng,W., Cao,X., Li,W., Zhang,D., Zhu,J., Zhang,X.
            and Chen,Y.
  TITLE     Proteomic Analysis Revealed the Potential Role of MAGE-D2 in the
            Therapeutic Targeting of Triple-Negative Breast Cancer
  JOURNAL   Mol Cell Proteomics 23 (1), 100703 (2024)
   PUBMED   38128647
  REMARK    GeneRIF: Proteomic Analysis Revealed the Potential Role of MAGE-D2
            in the Therapeutic Targeting of Triple-Negative Breast Cancer.
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Nasrah,S., Radi,A., Daberkow,J.K., Hummler,H., Weber,S.,
            Seaayfan,E. and Komhoff,M.
  TITLE     MAGED2 Depletion Promotes Stress-Induced Autophagy by Impairing the
            cAMP/PKA Pathway
  JOURNAL   Int J Mol Sci 24 (17), 13433 (2023)
   PUBMED   37686237
  REMARK    GeneRIF: MAGED2 Depletion Promotes Stress-Induced Autophagy by
            Impairing the cAMP/PKA Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Seaayfan,E., Nasrah,S., Quell,L., Radi,A., Kleim,M.,
            Schermuly,R.T., Weber,S., Laghmani,K. and Komhoff,M.
  TITLE     Reciprocal Regulation of MAGED2 and HIF-1alpha Augments Their
            Expression under Hypoxia: Role of cAMP and PKA Type II
  JOURNAL   Cells 11 (21), 3424 (2022)
   PUBMED   36359819
  REMARK    GeneRIF: Reciprocal Regulation of MAGED2 and HIF-1alpha Augments
            Their Expression under Hypoxia: Role of cAMP and PKA Type II.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Harper,R., Xu,C., Di,P., Chen,Y., Privalsky,M. and Wu,R.
  TITLE     Identification of a novel MAGE D2 antisense RNA transcript in human
            tissues
  JOURNAL   Biochem Biophys Res Commun 324 (1), 199-204 (2004)
   PUBMED   15465002
  REMARK    GeneRIF: Results identified a cDNA clone, corresponding to MAGE D2
            mRNA, from primary human bronchial epithelial cells which exhibits
            increased expression in vitro after treatment with all-trans
            retinoic acid.
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Bertrand,M., Huijbers,I., Chomez,P. and De Backer,O.
  TITLE     Comparative expression analysis of the MAGED genes during
            embryogenesis and brain development
  JOURNAL   Dev Dyn 230 (2), 325-334 (2004)
   PUBMED   15162511
  REMARK    GeneRIF: Maged2 is mainly expressed in tissues of mesodermal origin
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Langnaese,K., Kloos,D.U., Wehnert,M., Seidel,B. and Wieacker,P.
  TITLE     Expression pattern and further characterization of human MAGED2 and
            identification of rodent orthologues
  JOURNAL   Cytogenet Cell Genet 94 (3-4), 233-240 (2001)
   PUBMED   11856887
  REMARK    GeneRIF: Expression pattern and further characterization of human
            MAGED2 and identification of rodent orthologues
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Kurt,R.A., Urba,W.J. and Schoof,D.D.
  TITLE     Isolation of genes overexpressed in freshly isolated breast cancer
            specimens
  JOURNAL   Breast Cancer Res Treat 59 (1), 41-48 (2000)
   PUBMED   10752678
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Lucas,S., Brasseur,F. and Boon,T.
  TITLE     A new MAGE gene with ubiquitous expression does not code for known
            MAGE antigens recognized by T cells
  JOURNAL   Cancer Res 59 (16), 4100-4103 (1999)
   PUBMED   10463614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY017171.1, BC000304.2 and
            BX647995.1.
            
            On or before Nov 4, 2002 this sequence version replaced
            NP_006778.1, NP_055414.1.
            
            Summary: This gene is a member of the MAGED gene family. The MAGED
            genes are clustered on chromosome Xp11. This gene is located in
            Xp11.2, a hot spot for X-linked intellectual disability (XLID).
            Mutations in this gene cause a form of transient antenatal
            Bartter's syndrome. This gene may also be involved in several types
            of cancer, including breast cancer and melanoma. The protein
            encoded by this gene is progressively recruited from the cytoplasm
            to the nucleoplasm during the interphase and after nucleolar stress
            and is thus thought to play a role in cell cycle regulation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) differs in the 5' UTR,
            compared to variant 2. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1105167.1,
                                           SRR1803614.29975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     Protein         1..606
                     /product="melanoma-associated antigen D2"
                     /note="MAGE-D2 antigen; breast cancer-associated gene 1
                     protein; hepatocellular carcinoma-associated protein
                     JCL-1; melanoma antigen family D, 2; melanoma antigen
                     family D2"
                     /calculated_mol_wt=64823
     Region          1..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          <11..161
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          248..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          286..454
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     Region          534..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     CDS             1..606
                     /gene="MAGED2"
                     /gene_synonym="11B6; BARTS5; BCG-1; BCG1; HCA10; MAGE-D2"
                     /coded_by="NM_014599.6:118..1938"
                     /db_xref="CCDS:CCDS14362.1"
                     /db_xref="GeneID:10916"
                     /db_xref="HGNC:HGNC:16353"
                     /db_xref="MIM:300470"
ORIGIN      
        1 msdtsesgag ltrfqaease kdsssmmqtl ltvtqnvevp etpkaskale vsedvkvska
       61 sgvskatevs ktpeareapa tqassttqlt dtqvlaaenk slaadtkkqn adpqavtmpa
      121 tetkkvshva dtkvntkaqe teaapsqapa depepesaaa qsqenqdtrp kvkakkarkv
      181 khldgeedgs sdqsqasgtt ggrrvskalm asmarrasrg piafwarras rtrlaawarr
      241 allslrspka rrgkarrraa klqssqepea ppprdvallq grandlvkyl lakdqtkipi
      301 krsdmlkdii keytdvypei ieragyslek vfgiqlkeid kndhlyills tleptdagil
      361 gttkdspklg llmvllsiif mngnrsseav iwevlrklgl rpgihhslfg dvkklitdef
      421 vkqkyldyar vpnsnppeye ffwglrsyye tskmkvlkfa ckvqkkdpke waaqyreame
      481 adlkaaaeaa aeakaraeir armgiglgse naagpcnwde adigpwakar iqagaeakak
      541 aqesgsastg aststnnsas asastsggfs agasltatlt fglfaglgga gastsgssga
      601 cgfsyk
//
LOCUS       NP_001186671              60 aa            linear   PRI 20-NOV-2025
DEFINITION  growth arrest and DNA damage-inducible protein GADD45 alpha isoform
            3 [Homo sapiens].
ACCESSION   NP_001186671
VERSION     NP_001186671.1
DBSOURCE    REFSEQ: accession NM_001199742.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 60)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 60)
  AUTHORS   Zhou,L., Bai,G., Song,Y., Liu,X., Li,X., Deng,Y., Si,Y., Shi,Y. and
            Li,H.
  TITLE     AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes
  JOURNAL   Endocr Relat Cancer 31 (9), e230330 (2024)
   PUBMED   38904412
  REMARK    GeneRIF: AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 60)
  AUTHORS   Hassan,N., Yi,H., Malik,B., Gaspard-Boulinc,L., Samaraweera,S.E.,
            Casolari,D.A., Seneviratne,J., Balachandran,A., Chew,T., Duly,A.,
            Carter,D.R., Cheung,B.B., Norris,M., Haber,M., Kavallaris,M.,
            Marshall,G.M., Zhang,X.D., Liu,T., Wang,J., Liebermann,D.A.,
            D'Andrea,R.J. and Wang,J.Y.
  TITLE     Loss of the stress sensor GADD45A promotes stem cell activity and
            ferroptosis resistance in LGR4/HOXA9-dependent AML
  JOURNAL   Blood 144 (1), 84-98 (2024)
   PUBMED   38579286
  REMARK    GeneRIF: Loss of the stress sensor GADD45A promotes stem cell
            activity and ferroptosis resistance in LGR4/HOXA9-dependent AML.
REFERENCE   4  (residues 1 to 60)
  AUTHORS   Yu,L.R., Han,X.Z., Tang,Y.Z., Liu,D., Luo,X.Q., Qiu,X.W., Feng,J.,
            Yuan,W.X. and Ding,J.Y.
  TITLE     Activation of the MEK/ERK Pathway Mediates the Inhibitory Effects
            of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A, HK2, and
            GADD45A
  JOURNAL   Front Biosci (Landmark Ed) 29 (4), 160 (2024)
   PUBMED   38682208
  REMARK    GeneRIF: Activation of the MEK/ERK Pathway Mediates the Inhibitory
            Effects of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A,
            HK2, and GADD45A.
REFERENCE   5  (residues 1 to 60)
  AUTHORS   Gebert,M., Bartoszewska,S., Opalinski,L., Collawn,J.F. and
            Bartoszewski,R.
  TITLE     IRE1-mediated degradation of pre-miR-301a promotes apoptosis
            through upregulation of GADD45A
  JOURNAL   Cell Commun Signal 21 (1), 322 (2023)
   PUBMED   37946177
  REMARK    GeneRIF: IRE1-mediated degradation of pre-miR-301a promotes
            apoptosis through upregulation of GADD45A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 60)
  AUTHORS   Chen,I.T., Smith,M.L., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Direct interaction of Gadd45 with PCNA and evidence for competitive
            interaction of Gadd45 and p21Waf1/Cip1 with PCNA
  JOURNAL   Oncogene 11 (10), 1931-1937 (1995)
   PUBMED   7478510
REFERENCE   7  (residues 1 to 60)
  AUTHORS   Kearsey,J.M., Coates,P.J., Prescott,A.R., Warbrick,E. and Hall,P.A.
  TITLE     Gadd45 is a nuclear cell cycle regulated protein which interacts
            with p21Cip1
  JOURNAL   Oncogene 11 (9), 1675-1683 (1995)
   PUBMED   7478594
REFERENCE   8  (residues 1 to 60)
  AUTHORS   Carrier,F., Smith,M.L., Bae,I., Kilpatrick,K.E., Lansing,T.J.,
            Chen,C.Y., Engelstein,M., Friend,S.H., Henner,W.D., Gilmer,T.M. et
            al.
  TITLE     Characterization of human Gadd45, a p53-regulated protein
  JOURNAL   J Biol Chem 269 (51), 32672-32677 (1994)
   PUBMED   7798274
REFERENCE   9  (residues 1 to 60)
  AUTHORS   Smith,M.L., Chen,I.T., Zhan,Q., Bae,I., Chen,C.Y., Gilmer,T.M.,
            Kastan,M.B., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Interaction of the p53-regulated protein Gadd45 with proliferating
            cell nuclear antigen
  JOURNAL   Science 266 (5189), 1376-1380 (1994)
   PUBMED   7973727
REFERENCE   10 (residues 1 to 60)
  AUTHORS   Papathanasiou,M.A., Kerr,N.C., Robbins,J.H., McBride,O.W., Alamo,I.
            Jr., Barrett,S.F., Hickson,I.D. and Fornace,A.J. Jr.
  TITLE     Induction by ionizing radiation of the gadd45 gene in cultured
            human cells: lack of mediation by protein kinase C
  JOURNAL   Mol Cell Biol 11 (2), 1009-1016 (1991)
   PUBMED   1990262
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314991.1, EF581092.1 and
            BU629410.1.
            
            Summary: This gene is a member of a group of genes whose transcript
            levels are increased following stressful growth arrest conditions
            and treatment with DNA-damaging agents. The protein encoded by this
            gene responds to environmental stresses by mediating activation of
            the p38/JNK pathway via MTK1/MEKK4 kinase. The DNA damage-induced
            transcription of this gene is mediated by both p53-dependent and
            -independent mechanisms. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene.[provided
            by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (3) lacks a coding exon, as
            compared to variant 1. The resulting isoform (3) has a shorter and
            distinct C-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF581092.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..60
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..60
                     /product="growth arrest and DNA damage-inducible protein
                     GADD45 alpha isoform 3"
                     /note="DNA damage-inducible transcript-1; growth arrest
                     and DNA damage-inducible protein GADD45 alpha; growth
                     arrest and DNA-damage-inducible 45 alpha; DDIT-1; DNA
                     damage-inducible transcript 1 protein"
                     /calculated_mol_wt=6534
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24522.1)"
     CDS             1..60
                     /gene="GADD45A"
                     /gene_synonym="DDIT1; GADD45"
                     /coded_by="NM_001199742.2:295..477"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72806.1"
                     /db_xref="GeneID:1647"
                     /db_xref="HGNC:HGNC:4095"
                     /db_xref="MIM:126335"
ORIGIN      
        1 mtleefsage qktermdkvg daleevlska lsqrtitvgv yeaakllnvi hihlngrilp
//
LOCUS       NP_005488                396 aa            linear   PRI 20-NOV-2025
DEFINITION  gap junction gamma-1 protein [Homo sapiens].
ACCESSION   NP_005488
VERSION     NP_005488.2
DBSOURCE    REFSEQ: accession NM_005497.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Maciunas,K., Snipas,M., Kraujalis,T., Kraujaliene,L. and
            Panfilov,A.V.
  TITLE     The role of the Cx43/Cx45 gap junction voltage gating on wave
            propagation and arrhythmogenic activity in cardiac tissue
  JOURNAL   Sci Rep 13 (1), 14863 (2023)
   PUBMED   37684404
  REMARK    GeneRIF: The role of the Cx43/Cx45 gap junction voltage gating on
            wave propagation and arrhythmogenic activity in cardiac tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Li,R.G., Xu,Y.J., Ye,W.G., Li,Y.J., Chen,H., Qiu,X.B., Yang,Y.Q.
            and Bai,D.
  TITLE     Connexin45 (GJC1) loss-of-function mutation contributes to familial
            atrial fibrillation and conduction disease
  JOURNAL   Heart Rhythm 18 (5), 684-693 (2021)
   PUBMED   33429106
  REMARK    GeneRIF: Connexin45 (GJC1) loss-of-function mutation contributes to
            familial atrial fibrillation and conduction disease.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Choi,E.J., Palacios-Prado,N., Saez,J.C. and Lee,J.
  TITLE     Identification of Cx45 as a Major Component of GJs in HeLa Cells
  JOURNAL   Biomolecules 10 (10), 1389 (2020)
   PUBMED   33003547
  REMARK    GeneRIF: Identification of Cx45 as a Major Component of GJs in HeLa
            Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Chanson,M., Scerri,I. and Suter,S.
  TITLE     Defective regulation of gap junctional coupling in cystic fibrosis
            pancreatic duct cells
  JOURNAL   J Clin Invest 103 (12), 1677-1684 (1999)
   PUBMED   10377174
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Vozzi,C., Dupont,E., Coppen,S.R., Yeh,H.I. and Severs,N.J.
  TITLE     Chamber-related differences in connexin expression in the human
            heart
  JOURNAL   J Mol Cell Cardiol 31 (5), 991-1003 (1999)
   PUBMED   10336839
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Kilarski,W.M., Dupont,E., Coppen,S., Yeh,H.I., Vozzi,C.,
            Gourdie,R.G., Rezapour,M., Ulmsten,U., Roomans,G.M. and Severs,N.J.
  TITLE     Identification of two further gap-junctional proteins, connexin40
            and connexin45, in human myometrial smooth muscle cells at term
  JOURNAL   Eur J Cell Biol 75 (1), 1-8 (1998)
   PUBMED   9523149
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Kanter,H.L., Saffitz,J.E. and Beyer,E.C.
  TITLE     Molecular cloning of two human cardiac gap junction proteins,
            connexin40 and connexin45
  JOURNAL   J Mol Cell Cardiol 26 (7), 861-868 (1994)
   PUBMED   7966354
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005180.3, CN299428.1 and
            BC096216.3.
            
            On Jul 6, 2005 this sequence version replaced NP_005488.1.
            
            Summary: This gene is a member of the connexin gene family. The
            encoded protein is a component of gap junctions, which are composed
            of arrays of intercellular channels that provide a route for the
            diffusion of low molecular weight materials from cell to cell.
            Alternatively spliced transcript variants encoding the same isoform
            have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.202909.1,
                                           SRR1803611.33011.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000592524.6/ ENSP00000467201.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..396
                     /product="gap junction gamma-1 protein"
                     /note="connexin-45; gap junction alpha-7 protein;
                     CTC-296K1.4; gap junction protein, gamma 1, 45kDa"
                     /calculated_mol_wt=45339
     Region          2..255
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            23..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            76..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Region          145..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            176..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Site            229..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     Region          353..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36383.2)"
     CDS             1..396
                     /gene="GJC1"
                     /gene_synonym="CX45; GJA7"
                     /coded_by="NM_005497.4:323..1513"
                     /db_xref="CCDS:CCDS11487.1"
                     /db_xref="GeneID:10052"
                     /db_xref="HGNC:HGNC:4280"
                     /db_xref="MIM:608655"
ORIGIN      
        1 mswsfltrll eeihnhstfv gkiwltvliv frivltavgg esiyydeqsk fvcnteqpgc
       61 envcydafap lshvrfwvfq iilvatpsvm ylgyaihkia kmehgeadkk aarskpyamr
      121 wkqhraleet eedneedpmm ypemelesdk enkeqsqpkp khdgrrrire dglmkiyvlq
      181 llartvfevg fligqyflyg fqvhpfyvcs rlpcphkidc fisrptekti fllimygvtg
      241 lclllniwem lhlgfgtird slnskrrele dpgaynypft wntpsappgy niavkpdqiq
      301 ytelsnakia ykqnkantaq eqqygsheen lpadlealqr eirmaqerld lavqayshqn
      361 nphgprekka kvgskagsnk stassksgdg ktsvwi
//
LOCUS       NP_001355067            1257 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-VI isoform 5 [Homo sapiens].
ACCESSION   NP_001355067
VERSION     NP_001355067.1
DBSOURCE    REFSEQ: accession NM_001368138.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1257)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1257)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1257)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   4  (residues 1 to 1257)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1257)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1257)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 1257)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 1257)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 1257)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 1257)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109897.30, AL136093.8 and
            AL392166.19.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1966682, SAMEA1968189
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..1257
                     /product="unconventional myosin-VI isoform 5"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=145409
     Region          71..754
                     /region_name="MYSc_Myo6"
                     /note="class VI myosin, motor domain; cd01382"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107,151..158,190..200,451..456)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276833"
     Site            151..158
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276833"
     Site            190..200
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276833"
     Site            451..456
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276833"
     Site            order(480..491,494..503)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276833"
     Site            688..698
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276833"
     Site            700..754
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276833"
     Region          765..912
                     /region_name="CBD_MYO6-like"
                     /note="calmodulin binding domain found in unconventional
                     myosin-VI and similar proteins; cd21759"
                     /db_xref="CDD:409646"
     Site            order(781,784..785,787..805,807..808,811..826,828,
                     831..832,835..836,881)
                     /site_type="other"
                     /note="calmodulin binding site [polypeptide binding]"
                     /db_xref="CDD:409646"
     Site            815..825
                     /site_type="other"
                     /note="IQ motif"
                     /db_xref="CDD:409646"
     Region          994..1062
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cd22294"
                     /db_xref="CDD:412090"
     Site            994..1019
                     /site_type="other"
                     /note="MIU motif"
                     /db_xref="CDD:412090"
     Region          1045..1085
                     /region_name="MyUb_Myo6"
                     /note="myosin VI ubiquitin-binding domain (MyUb) found in
                     unconventional myosin-VI and similar proteins; cd21958"
                     /db_xref="CDD:439319"
     Site            order(1050..1051,1053..1054,1080..1081,1083..1084)
                     /site_type="other"
                     /note="clathrin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Site            order(1053..1055,1058..1059,1061..1065,1067,1070..1071,
                     1074,1077..1078)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Region          1140..1230
                     /region_name="Myosin-VI_CBD"
                     /note="Myosin VI cargo binding domain; pfam16521"
                     /db_xref="CDD:465157"
     CDS             1..1257
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_001368138.1:233..4006"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveeafgna ktvrnnnssr fgkfveihfn ekssvvggfv shylleksri cvqgkeerny
      241 hifyrlcaga sedireklhl sspdnfryln rgctryfank etdkqilqnr kspeylkags
      301 mkdpllddhg dfirmctamk kiglddeekl dlfrvvagvl hlgnidfeea gstsggcnlk
      361 nksaqsleyc aellgldqdd lrvslttrvm lttaggtkgt vikvplkveq annardalak
      421 tvyshlfdhv vnrvnqcfpf etssyfigvl diagfeyfeh nsfeqfciny cneklqqffn
      481 erilkeeqel yqkeglgvne vhyvdnqdci dlieaklvgi ldildeenrl pqpsdqhfts
      541 avhqkhkdhf rltiprkskl avhrnirdde gfiirhfaga vcyettqfve knndalhmsl
      601 eslicesrdk firelfesst nnnkdtkqka gklsfisvgn kfktqlnlll dklrstgasf
      661 ircikpnlkm tshhfegaqi lsqlqcsgmv svldlmqggy psrasfhely nmykkympdk
      721 larldprlfc kalfkalgln endykfgltk vffrpgkfae fdqimksdpd hlaelvkrvn
      781 hwltcsrwkk vqwcslsvik lknkikyrae acikmqktir mwlckrrhkp ridglvkvgt
      841 lkkrldkfne vvsvlkdgkp emnkqiknle isidtlmaki kstmmtqeqi qkeydalvks
      901 seellsalqk kkqqeeeaer lrriqeemek erkrreedek rrrkeeeerr mklemeakrk
      961 qeeeerkkre ddekriqaev eaqlarqkee esqqqavleq errdrelalr iaqseaelis
     1021 deaqadlalr rgpavlatka aagtkkydls kwkyaelrdt intscdiell aacreefhrr
     1081 lkvyhawksk nkkrnteteq rapksvtdyd fapflnnspq qnpaaqipar qreiemnrqq
     1141 rffripfirp adqykdpqsk kkgwwyahfd gpwiarqmel hpdkppillv agkddmemce
     1201 lnleetgltr krgaeilprq feeiwercgg iqylqnaies rqarptyata mlqsllk
//
LOCUS       NP_057474                376 aa            linear   PRI 20-NOV-2025
DEFINITION  28S rRNA (uridine-N(3))-methyltransferase [Homo sapiens].
ACCESSION   NP_057474
VERSION     NP_057474.2
DBSOURCE    REFSEQ: accession NM_016390.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Dharmadhikari,A.V., Abad,M.A., Khan,S., Maroofian,R., Sands,T.T.,
            Ullah,F., Samejima,I., Shen,Y., Wear,M.A., Moore,K.E.,
            Kondakova,E., Mitina,N., Schaub,T., Lee,G.K., Umandap,C.H.,
            Berger,S.M., Iglesias,A.D., Popp,B., Abou Jamra,R., Gabriel,H.,
            Rentas,S., Rippert,A.L., Gray,C., Izumi,K., Conlin,L.K.,
            Koboldt,D.C., Mosher,T.M., Hickey,S.E., Albert,D.V.F., Norwood,H.,
            Lewanda,A.F., Dai,H., Liu,P., Mitani,T., Marafi,D., Eker,H.K.,
            Pehlivan,D., Posey,J.E., Lippa,N.C., Vena,N., Heinzen,E.L.,
            Goldstein,D.B., Mignot,C., de Sainte Agathe,J.M., Al-Sannaa,N.A.,
            Zamani,M., Sadeghian,S., Azizimalamiri,R., Seifia,T., Zaki,M.S.,
            Abdel-Salam,G.M.H., Abdel-Hamid,M.S., Alabdi,L., Alkuraya,F.S.,
            Dawoud,H., Lofty,A., Bauer,P., Zifarelli,G., Afzal,E., Zafar,F.,
            Efthymiou,S., Gossett,D., Towne,M.C., Yeneabat,R., Perez-Duenas,B.,
            Cazurro-Gutierrez,A., Verdura,E., Cantarin-Extremera,V.,
            Marques,A.D.V., Helwak,A., Tollervey,D., Wontakal,S.N.,
            Aggarwal,V.S., Rosenfeld,J.A., Tarabykin,V., Ohta,S., Lupski,J.R.,
            Houlden,H., Earnshaw,W.C., Davis,E.E., Jeyaprakash,A.A. and Liao,J.
  TITLE     RNA methyltransferase SPOUT1/CENP-32 links mitotic spindle
            organization with the neurodevelopmental disorder SpADMiSS
  JOURNAL   Nat Commun 16 (1), 1703 (2025)
   PUBMED   39962046
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Chen,J., Bai,Y., Huang,Y., Cui,M., Wang,Y., Gu,Z., Wu,X., Li,Y. and
            Rong,Y.S.
  TITLE     The Ptch/SPOUT1 methyltransferase deposits an m3U modification on
            28S rRNA for normal ribosomal function in flies and humans
  JOURNAL   Sci Adv 10 (50), eadr1743 (2024)
   PUBMED   39671501
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Ohta,S., Wood,L., Toramoto,I., Yagyu,K., Fukagawa,T. and
            Earnshaw,W.C.
  TITLE     CENP-32 is required to maintain centrosomal dominance in bipolar
            spindle assembly
  JOURNAL   Mol Biol Cell 26 (7), 1225-1237 (2015)
   PUBMED   25657325
  REMARK    GeneRIF: CENP-32 appears to be required for centrosomes to
            integrate into a fully functional spindle that not only nucleates
            astral microtubules, but also is able to nucleate and bind to
            kinetochore and central spindle microtubules.
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Zhang,F., Baumer,N., Rode,M., Ji,P., Zhang,T., Berdel,W.E. and
            Muller-Tidow,C.
  TITLE     The inhibitor of growth protein 5 (ING5) depends on INCA1 as a
            co-factor for its antiproliferative effects
  JOURNAL   PLoS One 6 (7), e21505 (2011)
   PUBMED   21750715
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL110193.1, BC046133.1, BC063644.1, AL441992.17 and BM997763.1.
            
            On Dec 4, 2003 this sequence version replaced NP_057474.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL110193.1, SRR11853564.27977.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361256.10/ ENSP00000354812.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..376
                     /product="28S rRNA (uridine-N(3))-methyltransferase"
                     /EC_number="2.1.1.-"
                     /note="centromere protein 32; putative methyltransferase
                     C9orf114; kinetochore-associated protein; ribosomal RNA
                     methyltransferase SPOUT1"
                     /calculated_mol_wt=41878
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T280.3)"
     Region          49..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T280.3)"
     Region          74..364
                     /region_name="Methyltrn_RNA_3"
                     /note="Putative RNA methyltransferase; pfam02598"
                     /db_xref="CDD:460611"
     CDS             1..376
                     /gene="SPOUT1"
                     /gene_synonym="C9orf114; CENP-32; CENP32; HSPC109; NEDGSB"
                     /coded_by="NM_016390.4:15..1145"
                     /db_xref="CCDS:CCDS6913.1"
                     /db_xref="GeneID:51490"
                     /db_xref="HGNC:HGNC:26933"
                     /db_xref="MIM:617614"
ORIGIN      
        1 maergrkrpc gpgehgqrie wrkwkqqkke ekkkwkdlkl mkklerqraq eeqakrleee
       61 eaaaekedrg rpytlsvalp gsildnaqsp elrtylagqi aracaifcvd eivvfdeegq
      121 daktvegeft gvgkkgqacv qlarilqyle cpqylrkaff pkhqdlqfag llnpldsphh
      181 mrqdeesefr egivvdrptr pghgsfvncg mkkevkidkn lepglrvtvr lnqqqhpdck
      241 tyhgkvvssq dprtkaglyw gytvrlascl savfaeapfq dgydltigts ergsdvasaq
      301 lpnfrhalvv fgglqgleag adadpnleva epsvlfdlyv ntcpgqgsrt irteeailis
      361 laalqpgliq agarht
//
LOCUS       NP_001337620             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337620
VERSION     NP_001337620.1
DBSOURCE    REFSEQ: accession NM_001350691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (27), as well as variants 1-4,
            9-26, and 28-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.47226.1,
                                           SRR1660807.41916.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350691.1:639..2849"
                     /note="isoform 1 is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001127757             435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_001127757
VERSION     NP_001127757.1
DBSOURCE    REFSEQ: accession NM_001134285.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647076.1, AB020639.1 and
            BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (4) lacks the 5' exon but has
            three alternate 5' exons and uses a downstream AUG start codon,
            compared to variant 1. The resulting isoform (2) is shorter at the
            N-terminus, compared to isoform 1. Variants 2-4, 9-15, and 17-21
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647076.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001134285.3:266..1573"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_001317368             456 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily D member 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001317368 XP_005257661
VERSION     NP_001317368.1
DBSOURCE    REFSEQ: accession NM_001330439.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Schim van der Loeff,I., Sprenkeler,E.G.G., Tool,A.T.J., Abinun,M.,
            Grainger,A., Engelhardt,K.R., van Houdt,M., Janssen,H.,
            Kuijpers,T.W. and Hambleton,S.
  TITLE     Defective neutrophil development and specific granule deficiency
            caused by a homozygous splice-site mutation in SMARCD2
  JOURNAL   J Allergy Clin Immunol 147 (6), 2381-2385 (2021)
   PUBMED   33279574
  REMARK    GeneRIF: Defective neutrophil development and specific granule
            deficiency caused by a homozygous splice-site mutation in SMARCD2.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Yucel,E., Karakus,I.S., Krolo,A., Kiykim,A., Heredia,R.J.,
            Tamay,Z., Cipe,F.E., Karakoc-Aydiner,E., Ozen,A., Karaman,S.,
            Boztug,K. and Baris,S.
  TITLE     Novel Frameshift Autosomal Recessive Loss-of-Function Mutation in
            SMARCD2 Encoding a Chromatin Remodeling Factor Mediates
            Granulopoiesis
  JOURNAL   J Clin Immunol 41 (1), 59-65 (2021)
   PUBMED   33025377
  REMARK    GeneRIF: Novel Frameshift Autosomal Recessive Loss-of-Function
            Mutation in SMARCD2 Encoding a Chromatin Remodeling Factor Mediates
            Granulopoiesis.
            Review article
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Phelan,M.L., Sif,S., Narlikar,G.J. and Kingston,R.E.
  TITLE     Reconstitution of a core chromatin remodeling complex from SWI/SNF
            subunits
  JOURNAL   Mol Cell 3 (2), 247-253 (1999)
   PUBMED   10078207
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Ring,H.Z., Vameghi-Meyers,V., Wang,W., Crabtree,G.R. and Francke,U.
  TITLE     Five SWI/SNF-related, matrix-associated, actin-dependent regulator
            of chromatin (SMARC) genes are dispersed in the human genome
  JOURNAL   Genomics 51 (1), 140-143 (1998)
   PUBMED   9693044
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK307944.1, AW375602.1 and
            BQ670607.1.
            
            On Aug 29, 2016 this sequence version replaced XP_005257661.2.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and has sequence similarity to
            the yeast Swp73 protein. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307944.1, SRR11853560.12877.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..456
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily D member
                     2 isoform 2"
                     /note="mammalian chromatin remodeling complex
                     BRG1-associated factor 60B; Swp73-like protein; chromatin
                     remodeling complex BAF60B subunit; SWI/SNF complex 60 kDa
                     subunit B; SWI/SNF related, matrix associated, actin
                     dependent regulator of chromatin, subfamily d, member 2;
                     SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily D member 2; 60 kDa
                     BRG-1/Brm-associated factor subunit B"
                     /calculated_mol_wt=52107
     Region          232..311
                     /region_name="SWIB_BAF60B"
                     /note="SWIB domain found in BRG1-associated factor 60B
                     (BAF60B) and similar proteins; cd17675"
                     /db_xref="CDD:349494"
     Site            order(254,257..258,260..261,264..265,270,275..276,278,295,
                     298..299)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349494"
     CDS             1..456
                     /gene="SMARCD2"
                     /gene_synonym="BAF60B; CRACD2; PRO2451; Rsc6p; SGD2"
                     /coded_by="NM_001330439.1:96..1466"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82187.1"
                     /db_xref="GeneID:6603"
                     /db_xref="HGNC:HGNC:11107"
                     /db_xref="MIM:601736"
ORIGIN      
        1 mspgnrmpma glqvgppags pfgaaaplrp gmpptmmdpf rkrllvpqaq ppmpaqrrgl
       61 krrkmadkvl pqrirelvpe sqaymdllaf erkldqtiar krmeiqeaik kpltqkrklr
      121 iyisntfsps kaegdsagta gtpggtpagd kvaswelrve gkllddpskq krkfssffks
      181 lvieldkely gpdnhlvewh rmpttqetdg fqvkrpgdln vkctlllmld hqppqykldp
      241 rlarllgvht qtraaimqal wlyikhnqlq dghereyinc nryfrqifsc grlrfseipm
      301 klagllqhpd pivinhvisv dpndqkktac ydidvevddp lkaqmsnfla sttnqqeias
      361 ldvkihetie sinqlktqrd fmlsfstdpq dfiqewlrsq rrdlkiitdv ignpeeerra
      421 afyhqpwaqe avgrhifakv qqrrqeleqv lgirlt
//
LOCUS       NP_150254                211 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL13 isoform 1 [Homo sapiens].
ACCESSION   NP_150254
VERSION     NP_150254.1
DBSOURCE    REFSEQ: accession NM_033251.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Costantini,A., Alm,J.J., Tonelli,F., Valta,H., Huber,C., Tran,A.N.,
            Daponte,V., Kirova,N., Kwon,Y.U., Bae,J.Y., Chung,W.Y., Tan,S.,
            Sznajer,Y., Nishimura,G., Nareoja,T., Warren,A.J.,
            Cormier-Daire,V., Kim,O.H., Forlino,A., Cho,T.J. and Makitie,O.
  TITLE     Novel RPL13 Variants and Variable Clinical Expressivity in a Human
            Ribosomopathy With Spondyloepimetaphyseal Dysplasia
  JOURNAL   J Bone Miner Res 36 (2), 283-297 (2021)
   PUBMED   32916022
  REMARK    GeneRIF: Novel RPL13 Variants and Variable Clinical Expressivity in
            a Human Ribosomopathy With Spondyloepimetaphyseal Dysplasia.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Yaseen,N.R. and Blobel,G.
  TITLE     Cloning and characterization of human karyopherin beta3
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4451-4456 (1997)
   PUBMED   9114010
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Adams,S.M., Helps,N.R., Sharp,M.G., Brammar,W.J., Walker,R.A. and
            Varley,J.M.
  TITLE     Isolation and characterization of a novel gene with differential
            expression in benign and malignant human breast tumours
  JOURNAL   Hum Mol Genet 1 (2), 91-96 (1992)
   PUBMED   1301162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020804.1 and AC092123.4.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L13E family of ribosomal proteins. It is located in the
            cytoplasm. This gene is expressed at significantly higher levels in
            benign breast lesions than in breast carcinomas. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (2) has a different 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020804.1, SRR1803613.213571.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..211
                     /product="large ribosomal subunit protein eL13 isoform 1"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L13; breast basic conserved
                     protein 1; large ribosomal subunit protein eL13; breast
                     basic conserved 1"
                     /calculated_mol_wt=24130
     Region          8..187
                     /region_name="Ribosomal_L13e"
                     /note="Ribosomal protein L13e; pfam01294"
                     /db_xref="CDD:460150"
     Site            16
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26373.4)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26373.4)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26373.4)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26373.4)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P26373.4)"
     CDS             1..211
                     /gene="RPL13"
                     /gene_synonym="BBC1; D16S444E; D16S44E; eL13; L13;
                     SEMDIST"
                     /coded_by="NM_033251.2:250..885"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10979.1"
                     /db_xref="GeneID:6137"
                     /db_xref="HGNC:HGNC:10303"
                     /db_xref="MIM:113703"
ORIGIN      
        1 mapsrngmvl kphfhkdwqr rvatwfnqpa rkirrrkarq akarriaprp asgpirpivr
       61 cptvryhtkv ragrgfslee lrvagihkkv artigisvdp rrrnkstesl qanvqrlkey
      121 rsklilfprk psapkkgdss aeelklatql tgpvmpvrnv ykkekarvit eeeknfkafa
      181 slrmaranar lfgirakrak eaaeqdvekk k
//
LOCUS       NP_001355929             288 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform h [Homo sapiens].
ACCESSION   NP_001355929 XP_016870326
VERSION     NP_001355929.1
DBSOURCE    REFSEQ: accession NM_001369000.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_016870326.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.166522.1,
                                           SRR7346977.612358.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..288
                     /product="aprataxin isoform h"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=32994
     Region          3..>44
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          110..211
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(204,206,208..210)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          229..288
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..288
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369000.1:322..1188"
                     /note="isoform h is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS75827.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqefeeea knpglethrk
       61 rkrsgnsdsi erdaaqeaea gtglepgsns gqcsvplkkg kdapikkesl ghwsqglkis
      121 mqdpkmqvyk deqvvvikdk ypkaryhwlv lpwtsisslk avarehlell khmhtvgekv
      181 ivdfagsskl rfrlgyhaip smshvhlhvi sqdfdspclk nkkhwnsfnt eyflesqavi
      241 emvqeagrvt vrdgmpellk lplrchecqq llpsipqlke hlrkhwtq
//
LOCUS       NP_005126               1099 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 12 member 6 isoform b [Homo sapiens].
ACCESSION   NP_005126
VERSION     NP_005126.1
DBSOURCE    REFSEQ: accession NM_005135.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1099)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1099)
  AUTHORS   Loseth,S., Hoyer,H., Le,K.M., Delpire,E., Kinge,E., Lande,A.,
            Hilmarsen,H.T., Fagerheim,T., Nilssen,O. and Braathen,G.J.
  TITLE     Late-onset sensory-motor axonal neuropathy, a novel SLC12A6-related
            phenotype
  JOURNAL   Brain 146 (3), 912-922 (2023)
   PUBMED   36542484
  REMARK    GeneRIF: Late-onset sensory-motor axonal neuropathy, a novel
            SLC12A6-related phenotype.
REFERENCE   3  (residues 1 to 1099)
  AUTHORS   Ando,M., Higuchi,Y., Yuan,J., Yoshimura,A., Taniguchi,T., Takei,J.,
            Takeuchi,M., Hiramatsu,Y., Shimizu,F., Kubota,M., Takeshima,A.,
            Ueda,T., Koh,K., Nagaoka,U., Tokashiki,T., Sawai,S., Sakiyama,Y.,
            Hashiguchi,A., Sato,R., Kanda,T., Okamoto,Y. and Takashima,H.
  TITLE     Novel heterozygous variants of SLC12A6 in Japanese families with
            Charcot-Marie-Tooth disease
  JOURNAL   Ann Clin Transl Neurol 9 (7), 902-911 (2022)
   PUBMED   35733399
  REMARK    GeneRIF: Novel heterozygous variants of SLC12A6 in Japanese
            families with Charcot-Marie-Tooth disease.
REFERENCE   4  (residues 1 to 1099)
  AUTHORS   Bogdanova-Mihaylova,P., McNamara,P., Burton-Jones,S. and
            Murphy,S.M.
  TITLE     Expanding the phenotype of SLC12A6-associated sensorimotor
            neuropathy
  JOURNAL   BMJ Case Rep 14 (10), e244641 (2021)
   PUBMED   34706912
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1099)
  AUTHORS   Chi,G., Ebenhoch,R., Man,H., Tang,H., Tremblay,L.E., Reggiano,G.,
            Qiu,X., Bohstedt,T., Liko,I., Almeida,F.G., Garneau,A.P., Wang,D.,
            McKinley,G., Moreau,C.P., Bountra,K.D., Abrusci,P.,
            Mukhopadhyay,S.M.M., Fernandez-Cid,A., Slimani,S., Lavoie,J.L.,
            Burgess-Brown,N.A., Tehan,B., DiMaio,F., Jazayeri,A., Isenring,P.,
            Robinson,C.V. and Durr,K.L.
  TITLE     Phospho-regulation, nucleotide binding and ion access control in
            potassium-chloride cotransporters
  JOURNAL   EMBO J 40 (14), e107294 (2021)
   PUBMED   34031912
REFERENCE   6  (residues 1 to 1099)
  AUTHORS   Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
            Chernova,M.N., Brugnara,C. and Alper,S.L.
  TITLE     A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
            and C-terminal cytoplasmic domains are required for K-Cl
            cotransport activity
  JOURNAL   J Biol Chem 276 (45), 41870-41878 (2001)
   PUBMED   11551954
REFERENCE   7  (residues 1 to 1099)
  AUTHORS   Race,J.E., Makhlouf,F.N., Logue,P.J., Wilson,F.H., Dunham,P.B. and
            Holtzman,E.J.
  TITLE     Molecular cloning and functional characterization of KCC3, a new
            K-Cl cotransporter
  JOURNAL   Am J Physiol 277 (6), C1210-C1219 (1999)
   PUBMED   10600773
REFERENCE   8  (residues 1 to 1099)
  AUTHORS   Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
            and Gamba,G.
  TITLE     Cloning and characterization of KCC3 and KCC4, new members of the
            cation-chloride cotransporter gene family
  JOURNAL   J Biol Chem 274 (23), 16355-16362 (1999)
   PUBMED   10347194
REFERENCE   9  (residues 1 to 1099)
  AUTHORS   Hiki,K., D'Andrea,R.J., Furze,J., Crawford,J., Woollatt,E.,
            Sutherland,G.R., Vadas,M.A. and Gamble,J.R.
  TITLE     Cloning, characterization, and chromosomal location of a novel
            human K+-Cl- cotransporter
  JOURNAL   J Biol Chem 274 (15), 10661-10667 (1999)
   PUBMED   10187864
REFERENCE   10 (residues 1 to 1099)
  AUTHORS   Gauvreau,C., Brisson,J.D. and Dupre,N.
  TITLE     Hereditary Motor and Sensory Neuropathy with Agenesis of the Corpus
            Callosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021822.21, AF108831.1 and
            AC079203.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the K-Cl cotransporter (KCC)
            family. K-Cl cotransporters are integral membrane proteins that
            lower intracellular chloride concentrations below the
            electrochemical equilibrium potential. The proteins encoded by this
            gene are activated by cell swelling induced by hypotonic
            conditions. Alternate splicing results in multiple transcript
            variants encoding different isoforms. Mutations in this gene are
            associated with agenesis of the corpus callosum with peripheral
            neuropathy. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate exon for the
            5' UTR and 5' coding region, compared to variant 1. The encoded
            protein (isoform b) is shorter and has a distinct N-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.125492.1,
                                           SRR1803612.163518.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1099
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..1099
                     /product="solute carrier family 12 member 6 isoform b"
                     /note="potassium chloride cotransporter 3; potassium
                     chloride cotransporter KCC3a-S3; potassium-chloride
                     transporter-3a; potassium-chloride transporter-3b; K-Cl
                     cotransporter 3; electroneutral potassium-chloride
                     cotransporter 3; solute carrier family 12
                     (potassium/chloride transporters), member 6; solute
                     carrier family 12 (potassium/chloride transporter), member
                     6"
                     /calculated_mol_wt=121960
     Region          58..1099
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     CDS             1..1099
                     /gene="SLC12A6"
                     /gene_synonym="ACCPN; CMT2II; KCC3; KCC3A; KCC3B"
                     /coded_by="NM_005135.2:143..3442"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10036.1"
                     /db_xref="GeneID:9990"
                     /db_xref="HGNC:HGNC:10914"
                     /db_xref="MIM:604878"
ORIGIN      
        1 mphftvtkve dpeegaaasi sqepsladik ariqdsdepd lsqnsitgeh sqllddghkk
       61 arnaylnnsn yeegdeyfdk nlalfeeemd trpkvsslln rmanytnltq gakeheeaen
      121 itegkkkptk tpqmgtfmgv ylpclqnifg vilflrltwv vgtagvlqaf aivlicccct
      181 mltaismsai atngvvpagg syfmisralg pefggavglc fylgttfaaa myilgaieif
      241 lvyivpraai fhsddalkes aamlnnmrvy gtaflvlmvl vvfigvryvn kfaslflacv
      301 ivsilaiyag aikssfapph fpvcmlgnrt lssrhidvcs ktkeinnmtv psklwgffcn
      361 ssqffnatcd eyfvhnnvts iqgipglasg iitenlwsny lpkgeiiekp sakssdvlgs
      421 lnheyvlvdi ttsftllvgi ffpsvtgima gsnrsgdlkd aqksipigti lailttsfvy
      481 lsnvvlfgac iegvvlrdkf gdavkgnlvv gtlswpspwv ivigsffstc gaglqsltga
      541 prllqaiakd niipflrvfg hskangeptw allltaaiae lgiliasldl vapilsmffl
      601 mcylfvnlac alqtllrtpn wrprfryyhw alsfmgmsic lalmfisswy yaivamviag
      661 miykyieyqg aekewgdgir glslsaarfa llrleegpph tknwrpqllv llkldedlhv
      721 khprlltfas qlkagkglti vgsvivgnfl enygealaae qtikhlmeae kvkgfcqlvv
      781 aaklregish liqscglggm khntvvmgwp ngwrqsedar awktfigtvr vttaahlall
      841 vaknisffps nveqfsegni dvwwivhdgg mlmllpfllk qhkvwrkcsi riftvaqled
      901 nsiqmkkdla tflyhlriea evevvemhds disaytyert lmmeqrsqml rhmrlskter
      961 dreaqlvkdr nsmlrltsig sdedeetety qekvhmtwtk dkymasrgqk aksmegfqdl
     1021 lnmrpdqsnv rrmhtavkln evivnkshea klvllnmpgp prnpegdeny meflevlteg
     1081 lervllvrgg gsevitiys
//
LOCUS       NP_057670                344 aa            linear   PRI 20-NOV-2025
DEFINITION  MAP3K12-binding inhibitory protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_057670
VERSION     NP_057670.2
DBSOURCE    REFSEQ: accession NM_016586.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Ochieng,J.K., Kundu,S.T., Bajaj,R., Leticia Rodriguez,B.,
            Fradette,J.J. and Gibbons,D.L.
  TITLE     MBIP (MAP3K12 binding inhibitory protein) drives NSCLC metastasis
            by JNK-dependent activation of MMPs
  JOURNAL   Oncogene 39 (43), 6719-6732 (2020)
   PUBMED   32963352
  REMARK    GeneRIF: MBIP (MAP3K12 binding inhibitory protein) drives NSCLC
            metastasis by JNK-dependent activation of MMPs.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Guelman,S., Kozuka,K., Mao,Y., Pham,V., Solloway,M.J., Wang,J.,
            Wu,J., Lill,J.R. and Zha,J.
  TITLE     The double-histone-acetyltransferase complex ATAC is essential for
            mammalian development
  JOURNAL   Mol Cell Biol 29 (5), 1176-1188 (2009)
   PUBMED   19103755
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Wang,Y.L., Faiola,F., Xu,M., Pan,S. and Martinez,E.
  TITLE     Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel
            NC2-like histone fold module that interacts with the TATA-binding
            protein
  JOURNAL   J Biol Chem 283 (49), 33808-33815 (2008)
   PUBMED   18838386
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Fukuyama,K., Yoshida,M., Yamashita,A., Deyama,T., Baba,M.,
            Suzuki,A., Mohri,H., Ikezawa,Z., Nakajima,H., Hirai,S. and Ohno,S.
  TITLE     MAPK upstream kinase (MUK)-binding inhibitory protein, a negative
            regulator of MUK/dual leucine zipper-bearing kinase/leucine zipper
            protein kinase
  JOURNAL   J Biol Chem 275 (28), 21247-21254 (2000)
   PUBMED   10801814
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Daley,M.D., Olee,T., Peng,H.Q., Soto-Gil,R.W., Chen,P.P. and
            Siminovitch,K.A.
  TITLE     Molecular characterization of the human immunoglobulin V lambda I
            germline gene repertoire
  JOURNAL   Mol Immunol 29 (9), 1031-1042 (1992)
   PUBMED   1495496
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL137226.3, AK315290.1 and AA761503.1.
            
            On Jan 28, 2009 this sequence version replaced NP_057670.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB038523.1, SRR3476690.1162714.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000416007.9/ ENSP00000399718.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.3"
     Protein         1..344
                     /product="MAP3K12-binding inhibitory protein 1 isoform 1"
                     /note="MUK-binding inhibitory protein; MAPK upstream
                     kinase-binding inhibitory protein"
                     /calculated_mol_wt=39150
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NS73.2)"
     Region          172..344
                     /region_name="Interaction with MAP3K12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS73.2)"
     Region          271..285
                     /region_name="Leucine-zipper 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS73.2)"
     Site            301
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99LQ1; propagated from
                     UniProtKB/Swiss-Prot (Q9NS73.2)"
     Region          314..329
                     /region_name="Leucine-zipper 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NS73.2)"
     CDS             1..344
                     /gene="MBIP"
                     /coded_by="NM_016586.3:50..1084"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9658.1"
                     /db_xref="GeneID:51562"
                     /db_xref="HGNC:HGNC:20427"
                     /db_xref="MIM:609431"
ORIGIN      
        1 maaatelnrp ssgdrnlerr crpnlsrevl yeifrslhtl vgqldlrddv vkitidwnkl
       61 qslsafqpal lfsaleqhil ylqpflaklq spikeentta veeigrtemg nknevndkfs
      121 igdlqeeekh kesdlrdvkk tqihfdpevv qikagkaeid rrisafierk qaeinennvr
      181 efcnvidcnq enscartdai ftpypgfksh vkvsrvvnty gpqtrpegip gsghkpnsml
      241 rdcgnqavee rlqnieahlr lqtggpvprd iyqrikkled kilelegisp eyfqsvsfsg
      301 krrkvqppqq nyslaeldek isalkqallr ksreaesmat hhlp
//
LOCUS       NP_001310338             261 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome inhibitor PI31 subunit isoform 5 [Homo sapiens].
ACCESSION   NP_001310338
VERSION     NP_001310338.1
DBSOURCE    REFSEQ: accession NM_001323409.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Yang,S., Tang,D., Zhao,Y.C., Liu,H., Luo,S., Stinchcombe,T.E.,
            Glass,C., Su,L., Shen,S., Christiani,D.C., Wang,Q. and Wei,Q.
  TITLE     Potentially functional variants of ERAP1, PSMF1 and NCF2 in the
            MHC-I-related pathway predict non-small cell lung cancer survival
  JOURNAL   Cancer Immunol Immunother 70 (10), 2819-2833 (2021)
   PUBMED   33651148
  REMARK    GeneRIF: Potentially functional variants of ERAP1, PSMF1 and NCF2
            in the MHC-I-related pathway predict non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 261)
  AUTHORS   McCutchen-Maloney,S.L., Matsuda,K., Shimbara,N., Binns,D.D.,
            Tanaka,K., Slaughter,C.A. and DeMartino,G.N.
  TITLE     cDNA cloning, expression, and functional characterization of PI31,
            a proline-rich inhibitor of the proteasome
  JOURNAL   J Biol Chem 275 (24), 18557-18565 (2000)
   PUBMED   10764772
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Tanahashi,N., Kawahara,H., Murakami,Y. and Tanaka,K.
  TITLE     The proteasome-dependent proteolytic system
  JOURNAL   Mol Biol Rep 26 (1-2), 3-9 (1999)
   PUBMED   10363639
  REMARK    Review article
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC398668.1, AL031665.19 and
            AA699495.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            protein that inhibits the activation of the proteasome by the 11S
            and 19S regulators. Alternative transcript variants have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1037405.1,
                                           SRR7410570.659976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..261
                     /product="proteasome inhibitor PI31 subunit isoform 5"
                     /note="proteasome inhibitor PI31 subunit; proteasome
                     (prosome, macropain) inhibitor subunit 1 (PI31)"
                     /calculated_mol_wt=28554
     Region          2..150
                     /region_name="Important for homodimerization and
                     interaction with FBXO7.
                     /evidence=ECO:0000269|PubMed:18495667"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          11..148
                     /region_name="PI31_Prot_N"
                     /note="PI31 proteasome regulator N-terminal; pfam11566"
                     /db_xref="CDD:463296"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          182..248
                     /region_name="PI31_Prot_C"
                     /note="PI31 proteasome regulator; pfam08577"
                     /db_xref="CDD:430086"
     Site            205
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            219
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            231
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     CDS             1..261
                     /gene="PSMF1"
                     /gene_synonym="PI31"
                     /coded_by="NM_001323409.2:173..958"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:9491"
                     /db_xref="HGNC:HGNC:9571"
                     /db_xref="MIM:617858"
ORIGIN      
        1 maglevlfas aapaitcrqd alvcflhwev vthgyfglgv gdqpgpndkk sellpagwnn
       61 nkdlyvlrye ykdgsrkllv kaitvessmi lnvleygsqq vadltlnldd yidaehlgdf
      121 hrtyknseel rsrivsgiit piheqwekan vssphrefpp atarevdplr ipphhphtsr
      181 qppwcdplgp fvvggedldp fgprrggmiv dplrsgfpra lidpssglpn rlppgavppg
      241 arfdpfgpig tsppgyvvtq t
//
LOCUS       NP_001316673             170 aa            linear   PRI 20-NOV-2025
DEFINITION  protein DPCD isoform 4 [Homo sapiens].
ACCESSION   NP_001316673
VERSION     NP_001316673.1
DBSOURCE    REFSEQ: accession NM_001329744.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Dos Santos Morais,R., Santo,P.E., Ley,M., Schelcher,C., Abel,Y.,
            Plassart,L., Desligniere,E., Chagot,M.E., Quinternet,M.,
            Paiva,A.C.F., Hessmann,S., Morellet,N., M F Sousa,P.,
            Vandermoere,F., Bertrand,E., Charpentier,B., Bandeiras,T.M.,
            Plisson-Chastang,C., Verheggen,C., Cianferani,S. and Manival,X.
  TITLE     Deciphering cellular and molecular determinants of human DPCD
            protein in complex with RUVBL1/RUVBL2 AAA-ATPases
  JOURNAL   J Mol Biol 434 (19), 167760 (2022)
   PUBMED   35901867
  REMARK    GeneRIF: Deciphering cellular and molecular determinants of human
            DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases.
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Zariwala,M., O'Neal,W.K., Noone,P.G., Leigh,M.W., Knowles,M.R. and
            Ostrowski,L.E.
  TITLE     Investigation of the possible role of a novel gene, DPCD, in
            primary ciliary dyskinesia
  JOURNAL   Am J Respir Cell Mol Biol 30 (4), 428-434 (2004)
   PUBMED   14630615
  REMARK    GeneRIF: a novel candidate gene for primary ciliary dyskinesia
            GeneRIF: The mouse homolog of this gene (named Dpcd, for Deleted in
            a mouse model of Primary Ciliary Dyskinesia) appears to be
            responsible for an inner arm defect in cilia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627424.8, BM782340.1 and
            BU681755.1.
            
            Summary: This gene in mouse encodes a protein that may be involved
            in the generation and maintenance of ciliated cells. In mouse,
            expression of this gene increases during ciliated cell
            differentiation, and disruption of this gene has been linked to
            primary ciliary dyskinesia. [provided by RefSeq, Jul 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM782340.1, BM782007.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..170
                     /product="protein DPCD isoform 4"
                     /note="protein DPCD; deleted in a mouse model of primary
                     ciliary dyskinesia; RP11-529I10.4"
                     /calculated_mol_wt=19355
     Region          6..>135
                     /region_name="DPCD"
                     /note="DPCD protein family; pfam14913"
                     /db_xref="CDD:464369"
     CDS             1..170
                     /gene="DPCD"
                     /coded_by="NM_001329744.2:17..529"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86141.1"
                     /db_xref="GeneID:25911"
                     /db_xref="HGNC:HGNC:24542"
                     /db_xref="MIM:616467"
ORIGIN      
        1 mavtgwlesl rtaqktallq dgrrkvhylf pdgkemaeey dektsellvr kwrvksalga
       61 mgqwqlevgd paplgagnlg pelikesnan pifmrkdtkm sfqwrirnlp ypkdvysvsv
      121 dqkerciivr ttnkkrtgwr llwtplamrc agvhgtpsei dtsylwmtpc
//
LOCUS       NP_001310873            1037 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001310873 XP_005254201
VERSION     NP_001310873.1
DBSOURCE    REFSEQ: accession NM_001323944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1037)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1037)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 1037)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1037)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1037)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 1037)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1037)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 1037)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 1037)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 1037)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            On Apr 23, 2016 this sequence version replaced XP_005254201.1.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.182580.1,
                                           SRR1803614.223921.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1037
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..1037
                     /product="DIS3-like exonuclease 1 isoform 6"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=118335
     Region          14..171
                     /region_name="PIN_Rrp44-like"
                     /note="VapC-like PIN domain of yeast exosome subunit Rrp44
                     endoribonuclease and other eukaryotic homologs; cd09862"
                     /db_xref="CDD:350211"
     Region          221..849
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          864..939
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..1037
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323944.2:273..3386"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mgrsragspr elqasccrce adiacfaatd gkllssdvth yvipdwkvvq dyleilefpe
       61 lkgiifmqta cqavqhqrgr rqynklrnll kdarhdcilf anefqqccyl prergesmek
      121 wqtrsiynaa vwyyhhcqdr mpivmvtede eaiqqygset egvfvitfkn yldnfwpdlk
      181 aahelcdsil qsrrerenes qeshgkeype hlplevleag iksgryiqgi lnvnkhraqi
      241 eafvrlqgas skdsdlvsdi lihgmkarnr sihgdvvvve llpknewkgr tvalcendcd
      301 dkasgespse pmptgrvvgi lqknwrdyvv tfpskeevqs qgknaqkilv tpwdyripki
      361 ristqqaetl qdfrvvvrid swestsvypn ghfvrvlgri gdlegeiati lvensisvip
      421 fseaqmcemp vntpespwkv speeeqkrkd lrkshlvfsi dpkgcedvdd tlsvrtlnng
      481 nlelgvhiad vthfvapnsy idieartrat tyyladrryd mlpsvlsadl csllggvdry
      541 avsimweldk asyeikkvwy grtiirsayk lfyeaaqell dgnlsvvddi pefkdldeks
      601 rqakleelvw aigkltdiar hvrakrdgcg alelegvevc vqlddkknih dlipkqplev
      661 hetvaecmil anhwvakkiw esfphqallr qhppphqeff selrecakak gffidtrsnk
      721 tladsldnan dphdpivnrl lrsmatqams nalyfstgsc aeeefhhygl aldkythfts
      781 pirrysdivv hrllmaaisk dkkmeikgnl fsnkdleelc rhinnrnqaa qhsqkqstel
      841 fqcmyfkdkd pateercisd gviysirtng vllfiprfgi kgaaylknkd glviscgpds
      901 csewkpgslq rfqnkitstt tdgesvtfhl fdhvtvrisi qasrchsdti rleiisnkpy
      961 kipntelihq sspllkselv kevtksveea qlaqevkvni iqeeyqeyrq tkgrslytll
     1021 eeirdlalld vsnnygi
//
LOCUS       NP_001008391             167 aa            linear   PRI 20-NOV-2025
DEFINITION  CGG triplet repeat-binding protein 1 [Homo sapiens].
ACCESSION   NP_001008391
VERSION     NP_001008391.1
DBSOURCE    REFSEQ: accession NM_001008390.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Patel,D., Patel,M., Datta,S. and Singh,U.
  TITLE     CGGBP1-dependent CTCF-binding sites restrict ectopic transcription
  JOURNAL   Cell Cycle 20 (22), 2387-2401 (2021)
   PUBMED   34585631
  REMARK    GeneRIF: CGGBP1-dependent CTCF-binding sites restrict ectopic
            transcription.
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Patel,M., Patel,D., Datta,S. and Singh,U.
  TITLE     CGGBP1-regulated cytosine methylation at CTCF-binding motifs
            resists stochasticity
  JOURNAL   BMC Genet 21 (1), 84 (2020)
   PUBMED   32727353
  REMARK    GeneRIF: CGGBP1-regulated cytosine methylation at CTCF-binding
            motifs resists stochasticity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Muller-Hartmann,H., Deissler,H., Naumann,F., Schmitz,B., Schroer,J.
            and Doerfler,W.
  TITLE     The human 20-kDa 5'-(CGG)(n)-3'-binding protein is targeted to the
            nucleus and affects the activity of the FMR1 promoter
  JOURNAL   J Biol Chem 275 (9), 6447-6452 (2000)
   PUBMED   10692448
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Deissler,H., Wilm,M., Genc,B., Schmitz,B., Ternes,T., Naumann,F.,
            Mann,M. and Doerfler,W.
  TITLE     Rapid protein sequencing by tandem mass spectrometry and cDNA
            cloning of p20-CGGBP. A novel protein that binds to the unstable
            triplet repeat 5'-d(CGG)n-3' in the human FMR1 gene
  JOURNAL   J Biol Chem 272 (27), 16761-16768 (1997)
   PUBMED   9201980
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Deissler,H., Behn-Krappa,A. and Doerfler,W.
  TITLE     Purification of nuclear proteins from human HeLa cells that bind
            specifically to the unstable tandem repeat (CGG)n in the human FMR1
            gene
  JOURNAL   J Biol Chem 271 (8), 4327-4334 (1996)
   PUBMED   8626781
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Meijer,H., de Graaff,E., Merckx,D.M., Jongbloed,R.J., de
            Die-Smulders,C.E., Engelen,J.J., Fryns,J.P., Curfs,P.M. and
            Oostra,B.A.
  TITLE     A deletion of 1.6 kb proximal to the CGG repeat of the FMR1 gene
            causes the clinical phenotype of the fragile X syndrome
  JOURNAL   Hum Mol Genet 3 (4), 615-620 (1994)
   PUBMED   8069307
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Hornstra,I.K., Nelson,D.L., Warren,S.T. and Yang,T.P.
  TITLE     High resolution methylation analysis of the FMR1 gene trinucleotide
            repeat region in fragile X syndrome
  JOURNAL   Hum Mol Genet 2 (10), 1659-1665 (1993)
   PUBMED   8268919
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119733.2, BU537042.1, BE501563.1, AJ000258.1, AL117392.1 and
            BC052980.1.
            
            Summary: This gene encodes a CGG repeat-binding protein that
            primarily localizes to the nucleus. CGG trinucleotide repeats are
            implicated in many disorders as they often act as transcription-
            and translation-regulatory elements, can produce hairpin structures
            which cause DNA replication errors, and form regions prone to
            chromosomal breakage. CGG repeats are also targets for CpG
            methylation. In addition to its ability to bind CGG repeats and
            regulate transcription, this gene is believed to play a role in DNA
            damage repair and telomere protection. In vitro studies indicate
            this protein does not bind to methylated CpG sequences. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.756214.1,
                                           SRR14038197.1444398.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000482016.6/ ENSP00000420374.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p11.1"
     Protein         1..167
                     /product="CGG triplet repeat-binding protein 1"
                     /note="p20-CGG binding protein; CGG-binding protein 1; 20
                     kDa CGG-binding protein; p20-CGGBP DNA-binding protein"
                     /calculated_mol_wt=18689
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UFW8.2)"
     Region          80..84
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UFW8.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UFW8.2)"
     CDS             1..167
                     /gene="CGGBP1"
                     /gene_synonym="CGGBP; p20-CGGBP"
                     /coded_by="NM_001008390.2:522..1025"
                     /db_xref="CCDS:CCDS43111.1"
                     /db_xref="GeneID:8545"
                     /db_xref="HGNC:HGNC:1888"
                     /db_xref="MIM:603363"
ORIGIN      
        1 merfvvtapp arnrsktaly vtpldrvtef ggelhedggk lfctscnvvl nhvrksaisd
       61 hlkskthtkr kaefeeqnvr kkqrpltasl qcnstaqtek vsviqdfvkm cleaniplek
      121 adhpavrafl srhvknggsi pksdqlrray lpdgyenenq llnsqdc
//
LOCUS       NP_000340                285 aa            linear   PRI 20-NOV-2025
DEFINITION  steroidogenic acute regulatory protein, mitochondrial [Homo
            sapiens].
ACCESSION   NP_000340
VERSION     NP_000340.2
DBSOURCE    REFSEQ: accession NM_000349.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Manna,P.R., Molehin,D., Ahmed,A.U., Yang,S. and Reddy,P.H.
  TITLE     Acetylation of Steroidogenic Acute Regulatory Protein Sensitizes
            17beta-Estradiol Regulation in Hormone-Sensitive Breast Cancer
            Cells
  JOURNAL   Int J Mol Sci 25 (16), 8732 (2024)
   PUBMED   39201419
  REMARK    GeneRIF: Acetylation of Steroidogenic Acute Regulatory Protein
            Sensitizes 17beta-Estradiol Regulation in Hormone-Sensitive Breast
            Cancer Cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Altinkilic,E.M., Augsburger,P., Pandey,A.V. and Fluck,C.E.
  TITLE     Clinical spectrum of human STAR variants and their
            genotype-phenotype correlation
  JOURNAL   J Endocrinol 262 (3), e240078 (2024)
   PUBMED   38913505
  REMARK    GeneRIF: Clinical spectrum of human STAR variants and their
            genotype-phenotype correlation.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Yahya,N.A., King,S.R., Shi,B., Shaaban,A., Whitfield,N.E., Yan,C.,
            Kordus,R.J., Whitman-Elia,G.F. and LaVoie,H.A.
  TITLE     Differential regulation of STARD1, STARD4 and STARD6 in the human
            ovary
  JOURNAL   J Endocrinol 262 (2), e230385 (2024)
   PUBMED   38829257
  REMARK    GeneRIF: Differential regulation of STARD1, STARD4 and STARD6 in
            the human ovary.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Phadte,A., Dhole,C., Hegishte,S., Sarathi,V., Lila,A., Gada,J.V.,
            Memon,S.S., Arya,S., Karlekar,M., Patil,V., Varthakavi,P.K.,
            Shah,N., Bhagwat,N.M. and Bandgar,T.
  TITLE     Steroidogenic acute regulatory protein (STAR) deficiency: Our
            experience and systematic review for phenotype-genotype correlation
  JOURNAL   Clin Endocrinol (Oxf) 100 (5), 431-440 (2024)
   PUBMED   38368602
  REMARK    GeneRIF: Steroidogenic acute regulatory protein (STAR) deficiency:
            Our experience and systematic review for phenotype-genotype
            correlation.
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Liu,B., Fu,B., Zhou,S., Wang,H., Bi,B., Guo,M., Cheng,J.C. and
            Fang,L.
  TITLE     Bone morphogenetic protein-9 downregulates StAR expression by
            inducing snail expression via SMAD1/5/8 signaling in human
            granulosa-lutein cells
  JOURNAL   Mol Cell Endocrinol 582, 112126 (2024)
   PUBMED   38109991
  REMARK    GeneRIF: Bone morphogenetic protein-9 downregulates StAR expression
            by inducing snail expression via SMAD1/5/8 signaling in human
            granulosa-lutein cells.
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Tee,M.K., Lin,D., Sugawara,T., Holt,J.A., Guiguen,Y.,
            Buckingham,B., Strauss,J.F. 3rd and Miller,W.L.
  TITLE     T-->A transversion 11 bp from a splice acceptor site in the human
            gene for steroidogenic acute regulatory protein causes congenital
            lipoid adrenal hyperplasia
  JOURNAL   Hum Mol Genet 4 (12), 2299-2305 (1995)
   PUBMED   8634702
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Gradi,A., Tang-Wai,R., McBride,H.M., Chu,L.L., Shore,G.C. and
            Pelletier,J.
  TITLE     The human steroidogenic acute regulatory (StAR) gene is expressed
            in the urogenital system and encodes a mitochondrial polypeptide
  JOURNAL   Biochim Biophys Acta 1258 (3), 228-233 (1995)
   PUBMED   7548191
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Sugawara,T., Lin,D., Holt,J.A., Martin,K.O., Javitt,N.B.,
            Miller,W.L. and Strauss,J.F. 3rd.
  TITLE     Structure of the human steroidogenic acute regulatory protein
            (StAR) gene: StAR stimulates mitochondrial cholesterol
            27-hydroxylase activity
  JOURNAL   Biochemistry 34 (39), 12506-12512 (1995)
   PUBMED   7547998
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Sugawara,T., Holt,J.A., Driscoll,D., Strauss,J.F. 3rd, Lin,D.,
            Miller,W.L., Patterson,D., Clancy,K.P., Hart,I.M., Clark,B.J. et
            al.
  TITLE     Human steroidogenic acute regulatory protein: functional activity
            in COS-1 cells, tissue-specific expression, and mapping of the
            structural gene to 8p11.2 and a pseudogene to chromosome 13
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 4778-4782 (1995)
   PUBMED   7761400
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Lin,D., Sugawara,T., Strauss,J.F. 3rd, Clark,B.J., Stocco,D.M.,
            Saenger,P., Rogol,A. and Miller,W.L.
  TITLE     Role of steroidogenic acute regulatory protein in adrenal and
            gonadal steroidogenesis
  JOURNAL   Science 267 (5205), 1828-1831 (1995)
   PUBMED   7892608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL526126.3, U17280.1,
            BC010550.1, AV706872.1, AV707696.1, AC084024.17 and AV706111.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 3, 2004 this sequence version replaced NP_000340.1.
            
            Summary: The protein encoded by this gene plays a key role in the
            acute regulation of steroid hormone synthesis by enhancing the
            conversion of cholesterol into pregnenolone. This protein permits
            the cleavage of cholesterol into pregnenolone by mediating the
            transport of cholesterol from the outer mitochondrial membrane to
            the inner mitochondrial membrane. Mutations in this gene are a
            cause of congenital lipoid adrenal hyperplasia (CLAH), also called
            lipoid CAH. A pseudogene of this gene is located on chromosome 13.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005654.1, SRR5189667.196142.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000276449.9/
                                                  ENSP00000276449.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..285
                     /product="steroidogenic acute regulatory protein,
                     mitochondrial"
                     /note="START domain containing 1; steroidogenic acute
                     regulator; StAR related lipid transfer (START) domain
                     containing 1; mitochondrial steroid acute regulatory
                     protein; cholesterol trafficker; START domain-containing
                     protein 1; testis secretory sperm-binding protein Li
                     241mP"
                     /calculated_mol_wt=31783
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10548884; propagated from
                     UniProtKB/Swiss-Prot (P49675.2)"
     Region          70..278
                     /region_name="START_STARD1-like"
                     /note="Cholesterol-binding START domain of mammalian
                     STARD1 and related proteins; cd08905"
                     /db_xref="CDD:176914"
     Site            order(99..100,108,120,122,133,137,144,147..148,150..151,
                     169,171..174,179,182,184,186,201,218,220..223,225,239,241,
                     243,245,247,249,256,258..260,262..264,267..268,271)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176914"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:10548884; propagated from
                     UniProtKB/Swiss-Prot (P49675.2)"
     CDS             1..285
                     /gene="STAR"
                     /gene_synonym="STARD1"
                     /coded_by="NM_000349.3:135..992"
                     /db_xref="CCDS:CCDS6102.1"
                     /db_xref="GeneID:6770"
                     /db_xref="HGNC:HGNC:11359"
                     /db_xref="MIM:600617"
ORIGIN      
        1 mllatfklca gssyrhmrnm kglrqqavma isqelnrral ggptpstwin qvrrrssllg
       61 srleetlysd qelaylqqge eamqkalgil snqegwkkes qqdngdkvms kvvpdvgkvf
      121 rlevvvdqpm erlyeelver meamgewnpn vkeikvlqki gkdtfithel aaeaagnlvg
      181 prdfvsvrca krrgstcvla gmatdfgnmp eqkgviraeh gptcmvlhpl agspsktklt
      241 wllsidlkgw lpksiinqvl sqtqvdfanh lrkrleshpa searc
//
LOCUS       NP_699202                690 aa            linear   PRI 20-NOV-2025
DEFINITION  ligand of Numb protein X 2 [Homo sapiens].
ACCESSION   NP_699202
VERSION     NP_699202.1
DBSOURCE    REFSEQ: accession NM_153371.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 690)
  AUTHORS   Liu,G.B., Zhan,T., Pan,Y.M., Zhang,D.W., Zheng,H.Z., Xu,B.,
            Li,T.T., Dong,C.L. and Cheng,Y.X.
  TITLE     LNX2 involves in the role of ghrelin to promote the neuronal
            differentiation of adipose tissue-derived mesenchymal stem cells
  JOURNAL   J Bioenerg Biomembr 55 (3), 195-205 (2023)
   PUBMED   37237241
  REMARK    GeneRIF: LNX2 involves in the role of ghrelin to promote the
            neuronal differentiation of adipose tissue-derived mesenchymal stem
            cells.
REFERENCE   2  (residues 1 to 690)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 690)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 690)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 690)
  AUTHORS   de la Rocha-Munoz,A., Nunez,E., Arribas-Gonzalez,E.,
            Lopez-Corcuera,B., Aragon,C. and de Juan-Sanz,J.
  TITLE     E3 ubiquitin ligases LNX1 and LNX2 are major regulators of the
            presynaptic glycine transporter GlyT2
  JOURNAL   Sci Rep 9 (1), 14944 (2019)
   PUBMED   31628376
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 690)
  AUTHORS   D'Agostino,M., Tornillo,G., Caporaso,M.G., Barone,M.V., Ghigo,E.,
            Bonatti,S. and Mottola,G.
  TITLE     Ligand of Numb proteins LNX1p80 and LNX2 interact with the human
            glycoprotein CD8alpha and promote its ubiquitylation and
            endocytosis
  JOURNAL   J Cell Sci 124 (Pt 21), 3545-3556 (2011)
   PUBMED   22045731
  REMARK    GeneRIF: LNX1 and LNX2 interact with CD8alpha and promote its
            ubiquitylation and endocytosis
REFERENCE   7  (residues 1 to 690)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 690)
  AUTHORS   Kumar,V., Matsuo,K., Takahashi,A., Hosono,N., Tsunoda,T.,
            Kamatani,N., Kong,S.Y., Nakagawa,H., Cui,R., Tanikawa,C., Seto,M.,
            Morishima,Y., Kubo,M., Nakamura,Y. and Matsuda,K.
  TITLE     Common variants on 14q32 and 13q12 are associated with DLBCL
            susceptibility
  JOURNAL   J Hum Genet 56 (6), 436-439 (2011)
   PUBMED   21471979
REFERENCE   9  (residues 1 to 690)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   10 (residues 1 to 690)
  AUTHORS   Rice,D.S., Northcutt,G.M. and Kurschner,C.
  TITLE     The Lnx family proteins function as molecular scaffolds for Numb
            family proteins
  JOURNAL   Mol Cell Neurosci 18 (5), 525-540 (2001)
   PUBMED   11922143
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB220129.1, BC036755.2, DN990012.1 and AK022995.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036755.2, SRR1660803.239226.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316334.5/ ENSP00000325929.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..690
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.2"
     Protein         1..690
                     /product="ligand of Numb protein X 2"
                     /note="PDZ domain containing ring finger 1; numb-binding
                     protein 2; PDZ domain-containing RING finger protein 1"
                     /calculated_mol_wt=75873
     Region          45..89
                     /region_name="mRING-HC-C3HC3D_LNX2"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in ligand of numb protein X 2 (LNX2); cd16780"
                     /db_xref="CDD:319694"
     Site            order(45,47..48,57,65..68)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:319694"
     Region          198..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N448.1)"
     Region          208..211
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N448.1)"
     Region          229..317
                     /region_name="PDZ1_LNX1_2-like"
                     /note="PDZ domain 1 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06677"
                     /db_xref="CDD:467165"
     Site            order(244..250,263,266,296,300,303..304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467165"
     Region          338..420
                     /region_name="PDZ2_LNX1_2-like"
                     /note="PDZ domain 2 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06678"
                     /db_xref="CDD:467166"
     Site            order(350..356,367,370,400,404,407..408)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467166"
     Region          418..455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N448.1)"
     Region          467..554
                     /region_name="PDZ3_LNX1_2-like"
                     /note="PDZ domain 3 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06679"
                     /db_xref="CDD:467167"
     Site            order(478..484,499,502,532,536,539..540)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467167"
     Region          599..687
                     /region_name="PDZ4_LNX1_2-like"
                     /note="PDZ domain 4 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06680"
                     /db_xref="CDD:467168"
     Site            order(610..616,631,634,664,668,671..672)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467168"
     CDS             1..690
                     /gene="LNX2"
                     /gene_synonym="PDZRN1"
                     /coded_by="NM_153371.4:256..2328"
                     /db_xref="CCDS:CCDS9323.1"
                     /db_xref="GeneID:222484"
                     /db_xref="HGNC:HGNC:20421"
                     /db_xref="MIM:609733"
ORIGIN      
        1 mgttsdemvs veqtssssln plcfecgqqh wtrenhlyny qnevdddlvc hiclqpllqp
       61 ldtpcghtfc ykclrnflqe kdfcpldrkr lhfklckkss ilvhklldkl lvlcpfssvc
      121 kdvmqrcdle ahlknrcpga shrrvalerr ktsrtqaeie nengptlldp agtlspeadc
      181 lgtgavpver hltsaslstw seepgldnpa feesagadtt qqplslpege ittieihrsn
      241 pyiqlgisiv ggnetplini viqevyrdgv iardgrllag dqilqvnnyn isnvshnyar
      301 avlsqpcntl hltvlrerrf gnrahnhsds nspreeifqv alhkrdsgeq lgiklvrrtd
      361 epgvfildll egglaaqdgr lssndrvlai nghdlkygtp elaaqiiqas gervnltiar
      421 pgkpqpgnti reagnhssss qhhtpppyys rpsshkdltq cvtcqekhit vkkepheslg
      481 mtvaggrgsk sgelpifvts vpphgclard grikrgdvll ningidltnl shseavamlk
      541 asaaspaval kalevqivee atqnaeeqps tfseneydas wspswvmwlg lpstlhschd
      601 ivlrrsylgs wgfsivggye enhtnqpffi ktivlgtpay ydgrlkcgdm ivavnglstv
      661 gmshsalvpm lkeqrnkvtl tvicwpgslv
//
LOCUS       NP_060997                311 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 16, NatA auxiliary subunit isoform 2
            [Homo sapiens].
ACCESSION   NP_060997
VERSION     NP_060997.2
DBSOURCE    REFSEQ: accession NM_018527.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Arnesen,T., Gromyko,D., Kagabo,D., Betts,M.J., Starheim,K.K.,
            Varhaug,J.E., Anderson,D. and Lillehaug,J.R.
  TITLE     A novel human NatA Nalpha-terminal acetyltransferase complex:
            hNaa16p-hNaa10p (hNat2-hArd1)
  JOURNAL   BMC Biochem 10, 15 (2009)
   PUBMED   19480662
  REMARK    GeneRIF: hNaa16p (NARG1L) interacts with hNaa10p (hArd1) making a
            distinct ribosome associated human NatA N-terminal
            acetyltransferase complex. hNAA16 is expressed in a variety of
            human cell lines and specific knockdown of hNAA16 induces cell
            death.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Arnesen,T., Betts,M.J., Pendino,F., Liberles,D.A., Anderson,D.,
            Caro,J., Kong,X., Varhaug,J.E. and Lillehaug,J.R.
  TITLE     Characterization of hARD2, a processed hARD1 gene duplicate,
            encoding a human protein N-alpha-acetyltransferase
  JOURNAL   BMC Biochem 7, 13 (2006)
   PUBMED   16638120
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB078940.1, BC032318.1 and AL590665.9.
            
            On Jul 31, 2003 this sequence version replaced NP_060997.1.
            
            Transcript Variant: This variant (2) lacks an internal coding exon
            and several 3' exons but has an alternate 3' segment, compared to
            variant 1. The resulting isoform (2) lacks an internal segment and
            has a shorter and distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032318.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..311
                     /product="N-alpha-acetyltransferase 16, NatA auxiliary
                     subunit isoform 2"
                     /note="NMDA receptor-regulated 1-like protein; NARG1-like
                     protein"
                     /calculated_mol_wt=36723
     Region          13..38
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          21..243
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          46..79
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          47..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          80..113
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          82..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(84..85,88..89,91,115,118..119,122..123,125..126,149,
                     152..153,156..157,160)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          113..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..184
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          148..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..>303
                     /region_name="NatA_aux_su"
                     /note="N-terminal acetyltransferase A, auxiliary subunit;
                     pfam12569"
                     /db_xref="CDD:463630"
     Region          224..257
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     CDS             1..311
                     /gene="NAA16"
                     /gene_synonym="NARG1L"
                     /coded_by="NM_018527.4:263..1198"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:79612"
                     /db_xref="HGNC:HGNC:26164"
                     /db_xref="MIM:619497"
ORIGIN      
        1 mpnvllppke snlfkrilkc yeqkqykngl kfckmilsnp kfaehgetla mkgltlnclg
       61 kkeeayefvr kglrndvksh vcwhvygllq rsdkkydeai kcyrnalkld kdnlqilrdl
      121 sllqiqmrdl egyretryql lqlrptqras wigyaiayhl lkdydmalkl leefrqtqqv
      181 ppnkidyeys elilyqnqvm readllqesl ehiemyekqi cdkllveeik geillklgrl
      241 keasevfknl idrnaenwcy yeglekalqi stleerlqiy eeiskqhpka itprrlpltl
      301 vpgfynpgtc y
//
LOCUS       NP_001354479            2857 aa            linear   PRI 20-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            4 [Homo sapiens].
ACCESSION   NP_001354479 XP_016864361
VERSION     NP_001354479.1
DBSOURCE    REFSEQ: accession NM_001367550.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2857)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2857)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2857)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2857)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2857)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2857)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2857)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2857)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2857)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2857)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079794.6, AC104796.4,
            AC092544.4, AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            
            On Dec 6, 2018 this sequence version replaced XP_016864361.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2857
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 4"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=318291
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2047
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2053
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2073..2170
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2201..2478
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2578..2842
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2585..2627
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2594..2630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2630..2673
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2636..2689
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2689..2729
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2694..2729
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2734..2763
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2771..2810
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2776..2810
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2813..2852
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2857
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001367550.1:475..9048"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93650.1"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehatded ilakgkqsir sqalgnqnse
     2041 neillegddd tlssvdekdl enlagpvsls tpaqlvapsv vvkgtlsvts selyfevdee
     2101 dpnfkkidpk ilayteglhg kwlfteirsi fsrryllqnt aleifmanrv avmfnfpdpa
     2161 tvkkvvnylp rvgvgtsfgl pqtrrislas prqlfkasnm tqrwqhreis nfeylmflnt
     2221 iagrsyndln qypvfpwvit nyeseeldlt lptnfrdlsk pigalnpkra affaeryesw
     2281 eddqvpkfhy gthystasfv lawllriepf ttyflnlqgg kfdhadrtfs sisrawrnsq
     2341 rdtsdikeli pefyylpemf vnfnnynlgv mddgtvvsdv elppwaktse efvhinrlal
     2401 esefvscqlh qwidlifgyk qqgpeavral nvfyyltyeg avnlnsitdp vlreaveaqi
     2461 rsfgqtpsql liephpprgs amqvylllqs plmftdkaqq dvimvlkfps nspvthvaan
     2521 tqpglatpav itvtanrlfa vnkwhnlpah qgavqdqpyq lpveidplia sntgmhrrqi
     2581 tdlldqsiqv hsqcfvitsd nryilvcgfw dksfrvystd tgrliqvvfg hwdvvtclar
     2641 sesyiggncy ilsgsrdatl llwywngkcs gigdnpgset aaprailtgh dyevtcaavc
     2701 aelglvlsgs qegpclihsm ngdllrtleg penclkpkli qasreghcvi fyenglfctf
     2761 svngklqatm etddniraiq lsrdgqyllt ggdrgvvvvr qvsdlkqlfa ypgcdagira
     2821 malsydqrci isgmasgsiv lfyndfnrwh heyqtry
//
LOCUS       NP_001171722            1000 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog isoform 10 [Homo sapiens].
ACCESSION   NP_001171722
VERSION     NP_001171722.1
DBSOURCE    REFSEQ: accession NM_001184793.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1000)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1000)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1000)
  AUTHORS   Zhang,J., Shi,Y., Ding,K., Yu,W., He,J. and Sun,B.
  TITLE     DCAF1 interacts with PARD3 to promote hepatocellular carcinoma
            progression and metastasis by activating the Akt signaling pathway
  JOURNAL   J Exp Clin Cancer Res 43 (1), 136 (2024)
   PUBMED   38711082
  REMARK    GeneRIF: DCAF1 interacts with PARD3 to promote hepatocellular
            carcinoma progression and metastasis by activating the Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1000)
  AUTHORS   Wu,J., Tan,H.Y., Chan,Y.T., Lu,Y., Feng,Z., Yuan,H., Zhang,C.,
            Feng,Y. and Wang,N.
  TITLE     PARD3 drives tumorigenesis through activating Sonic Hedgehog
            signalling in tumour-initiating cells in liver cancer
  JOURNAL   J Exp Clin Cancer Res 43 (1), 42 (2024)
   PUBMED   38317186
  REMARK    GeneRIF: PARD3 drives tumorigenesis through activating Sonic
            Hedgehog signalling in tumour-initiating cells in liver cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1000)
  AUTHORS   Gunji,D., Narumi,R., Muraoka,S., Isoyama,J., Ikemoto,N., Ishida,M.,
            Tomonaga,T., Sakai,Y., Obama,K. and Adachi,J.
  TITLE     Integrative analysis of cancer dependency data and comprehensive
            phosphoproteomics data revealed the EPHA2-PARD3 axis as a cancer
            vulnerability in KRAS-mutant colorectal cancer
  JOURNAL   Mol Omics 19 (8), 624-639 (2023)
   PUBMED   37232035
  REMARK    GeneRIF: Integrative analysis of cancer dependency data and
            comprehensive phosphoproteomics data revealed the EPHA2-PARD3 axis
            as a cancer vulnerability in KRAS-mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1000)
  AUTHORS   Ebnet,K., Suzuki,A., Horikoshi,Y., Hirose,T., Meyer Zu
            Brickwedde,M.K., Ohno,S. and Vestweber,D.
  TITLE     The cell polarity protein ASIP/PAR-3 directly associates with
            junctional adhesion molecule (JAM)
  JOURNAL   EMBO J 20 (14), 3738-3748 (2001)
   PUBMED   11447115
REFERENCE   7  (residues 1 to 1000)
  AUTHORS   Suzuki,A., Yamanaka,T., Hirose,T., Manabe,N., Mizuno,K.,
            Shimizu,M., Akimoto,K., Izumi,Y., Ohnishi,T. and Ohno,S.
  TITLE     Atypical protein kinase C is involved in the evolutionarily
            conserved par protein complex and plays a critical role in
            establishing epithelia-specific junctional structures
  JOURNAL   J Cell Biol 152 (6), 1183-1196 (2001)
   PUBMED   11257119
REFERENCE   8  (residues 1 to 1000)
  AUTHORS   Noda,Y., Takeya,R., Ohno,S., Naito,S., Ito,T. and Sumimoto,H.
  TITLE     Human homologues of the Caenorhabditis elegans cell polarity
            protein PAR6 as an adaptor that links the small GTPases Rac and
            Cdc42 to atypical protein kinase C
  JOURNAL   Genes Cells 6 (2), 107-119 (2001)
   PUBMED   11260256
REFERENCE   9  (residues 1 to 1000)
  AUTHORS   Johansson,A., Driessens,M. and Aspenstrom,P.
  TITLE     The mammalian homologue of the Caenorhabditis elegans polarity
            protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
            Rac1
  JOURNAL   J Cell Sci 113 (Pt 18), 3267-3275 (2000)
   PUBMED   10954424
REFERENCE   10 (residues 1 to 1000)
  AUTHORS   Joberty,G., Petersen,C., Gao,L. and Macara,I.G.
  TITLE     The cell-polarity protein Par6 links Par3 and atypical protein
            kinase C to Cdc42
  JOURNAL   Nat Cell Biol 2 (8), 531-539 (2000)
   PUBMED   10934474
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450337.24, AL138768.23,
            AL360233.21, AL392123.12 and AL390766.16.
            
            Summary: This gene encodes a member of the PARD protein family.
            PARD family members interact with other PARD family members and
            other proteins; they affect asymmetrical cell division and direct
            polarized cell growth. Multiple alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Oct 2011].
            
            Transcript Variant: This variant (10) uses three different splice
            sites, lacks most of the 3' coding region, and contains a different
            segment for its 3' end, compared to variant 1. The resulting
            protein (isoform 10) is shorter and has a distinct C-terminus when
            it is compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1000
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.22-p11.21"
     Protein         1..1000
                     /product="partitioning defective 3 homolog isoform 10"
                     /note="partitioning defective 3 homolog; atypical PKC
                     isotype-specific interacting protein; PAR3-alpha; CTCL
                     tumor antigen se2-5; bazooka; par-3 partitioning defective
                     3 homolog; par-3 family cell polarity regulator alpha;
                     protein phosphatase 1, regulatory subunit 118"
                     /calculated_mol_wt=109786
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          268..364
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(283..289,304,307,337,341,344..345)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          455..547
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(470..476,491,494,524,528,531..532)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          584..683
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(600..606,622,625,655,659,662..663)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     CDS             1..1000
                     /gene="PARD3"
                     /gene_synonym="ASIP; Baz; PAR3; PAR3alpha; PARD-3; PARD3A;
                     PPP1R118; SE2-5L16; SE2-5LT1; SE2-5T2"
                     /coded_by="NM_001184793.2:302..3304"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="GeneID:56288"
                     /db_xref="HGNC:HGNC:16051"
                     /db_xref="MIM:606745"
ORIGIN      
        1 mkvtvcfgrt rvvvpcgdgh mkvfsliqqa vtryrkaiak dpnywiqvhr lehgdggild
       61 lddilcdvad dkdrlvavfd eqdphhggdg tsasstgtqs peifgselgt nnvsafqpyq
      121 atseievtps vlranmplhv rrssdpalig lstsvsdsnf sseepsrknp trwsttagfl
      181 kqntagspkt cdrkkdenyr slprdtsnws nqfqrdnars slsashpmvg kwlekqeqde
      241 dgteednsrv epvghadtgl ehipnfsldd mvklvevpnd ggplgihvvp fsarggrtlg
      301 llvkrlekgg kaehenlfre ndcivrindg dlrnrrfeqa qhmfrqamrt piiwfhvvpa
      361 ankeqyeqls qseknnyyss rfspdsqyid nrsvnsaglh tvqraprlnh ppeqidshsr
      421 lphsahpsgk ppsapasapq nvfsttvssg yntkkigkrl niqlkkgteg lgfsitsrdv
      481 tiggsapiyv knilprgaai qdgrlkagdr lievngvdlv gksqeevvsl lrstkmegtv
      541 sllvfrqeda fhprelnaep sqmqipketk aededivltp dgtrefltfe vplndsgsag
      601 lgvsvkgnrs kenhadlgif vksiinggaa skdgrlrvnd qliavngesl lgktnqdame
      661 tlrrsmsteg nkrgmiqliv arriskcnel kspgsppgpe lpietalddr errishslys
      721 giegldesps rnaalsrimg kyqlsptvnm pqddtviied drlpvlpphl sdqssssshd
      781 dvgfvtadag twakaaisds adcslspdvd pvlafqregf grqtdetkln tvddqkagsp
      841 srdvgpslgl kksssleslq tavaevtlng dipfhrprpr iirgrgcnes fraaidksyd
      901 kpavddddeg metleedtee ssrsgresvs tasdqpshsl erqmngnqek gdktdrkkdk
      961 tgkekkkdrd kekdkmkakk gmlkglgdmf slaklkpekr
//
LOCUS       NP_001142                298 aa            linear   PRI 20-NOV-2025
DEFINITION  ADP/ATP translocase 1 [Homo sapiens].
ACCESSION   NP_001142
VERSION     NP_001142.2
DBSOURCE    REFSEQ: accession NM_001151.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Sui,J., Boatz,J.C., Shi,J., Hu,Q., Li,X., Zhang,Y., Konigshoff,M.
            and Kliment,C.R.
  TITLE     Loss of ANT1 Increases Fibrosis and Epithelial Cell Senescence in
            Idiopathic Pulmonary Fibrosis
  JOURNAL   Am J Respir Cell Mol Biol 69 (5), 556-569 (2023)
   PUBMED   37487137
  REMARK    GeneRIF: Loss of ANT1 Increases Fibrosis and Epithelial Cell
            Senescence in Idiopathic Pulmonary Fibrosis.
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Mishra,G., Coyne,L.P. and Chen,X.J.
  TITLE     Adenine nucleotide carrier protein dysfunction in human disease
  JOURNAL   IUBMB Life 75 (11), 911-925 (2023)
   PUBMED   37449547
  REMARK    GeneRIF: Adenine nucleotide carrier protein dysfunction in human
            disease.
            Review article
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Cimadamore-Werthein,C., Jaiquel Baron,S., King,M.S., Springett,R.
            and Kunji,E.R.
  TITLE     Human mitochondrial ADP/ATP carrier SLC25A4 operates with a
            ping-pong kinetic mechanism
  JOURNAL   EMBO Rep 24 (8), e57127 (2023)
   PUBMED   37278158
  REMARK    GeneRIF: Human mitochondrial ADP/ATP carrier SLC25A4 operates with
            a ping-pong kinetic mechanism.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Arbogast,S., Kotzur,H., Frank,C., Compagnone,N., Sutra,T.,
            Pillard,F., Pietri,S., Hmada,N., Moussa,D.M.A., Bride,J.,
            Franconnet,S., Mercier,J., Cristol,J.P., Dabauvalle,M.C. and
            Laoudj-Chenivesse,D.
  TITLE     ANT1 overexpression models: Some similarities with
            facioscapulohumeral muscular dystrophy
  JOURNAL   Redox Biol 56, 102450 (2022)
   PUBMED   36030628
  REMARK    GeneRIF: ANT1 overexpression models: Some similarities with
            facioscapulohumeral muscular dystrophy.
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Fan,Y.S., Yang,H.M. and Lin,C.C.
  TITLE     Assignment of the human muscle adenine nucleotide translocator gene
            (ANT1) to 4q35 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 60 (1), 29-30 (1992)
   PUBMED   1582253
REFERENCE   7  (residues 1 to 298)
  AUTHORS   Li,K., Warner,C.K., Hodge,J.A., Minoshima,S., Kudoh,J.,
            Fukuyama,R., Maekawa,M., Shimizu,Y., Shimizu,N. and Wallace,D.C.
  TITLE     A human muscle adenine nucleotide translocator gene has four exons,
            is located on chromosome 4, and is differentially expressed
  JOURNAL   J Biol Chem 264 (24), 13998-14004 (1989)
   PUBMED   2547778
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Cozens,A.L., Runswick,M.J. and Walker,J.E.
  TITLE     DNA sequences of two expressed nuclear genes for human
            mitochondrial ADP/ATP translocase
  JOURNAL   J Mol Biol 206 (2), 261-280 (1989)
   PUBMED   2541251
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Houldsworth,J. and Attardi,G.
  TITLE     Two distinct genes for ADP/ATP translocase are expressed at the
            mRNA level in adult human liver
  JOURNAL   Proc Natl Acad Sci U S A 85 (2), 377-381 (1988)
   PUBMED   2829183
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Neckelmann,N., Li,K., Wade,R.P., Shuster,R. and Wallace,D.C.
  TITLE     cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack
            of a leader peptide, divergence from a fibroblast translocator
            cDNA, and coevolution with mitochondrial DNA genes
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7580-7584 (1987)
   PUBMED   2823266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI544547.1, BC008664.1,
            AC093824.3, AC112237.1 and AC093592.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2004 this sequence version replaced NP_001142.1.
            
            Summary: This gene is a member of the mitochondrial carrier
            subfamily of solute carrier protein genes. The product of this gene
            functions as a gated pore that translocates ADP from the cytoplasm
            into the mitochondrial matrix and ATP from the mitochondrial matrix
            into the cytoplasm. The protein forms a homodimer embedded in the
            inner mitochondria membrane. Mutations in this gene have been shown
            to result in autosomal dominant progressive external opthalmoplegia
            and familial hypertrophic cardiomyopathy. [provided by RefSeq, Jun
            2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.48497.1,
                                           SRR1660805.245794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000281456.11/
                                                  ENSP00000281456.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.1"
     Protein         1..298
                     /product="ADP/ATP translocase 1"
                     /note="adenine nucleotide translocator 1 (skeletal
                     muscle); heart/skeletal muscle ATP/ADP translocator;
                     ADP,ATP carrier protein 1; ADP,ATP carrier protein,
                     heart/skeletal muscle; solute carrier family 25
                     (mitochondrial carrier; adenine nucleotide translocator),
                     member 4; progressive external ophthalmoplegia 3;
                     progressive external ophthalmoplegia 2; ADP/ATP carrier 1"
                     /calculated_mol_wt=32933
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine. /evidence=ECO:0000269|Ref.8;
                     propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          6..98
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          7..298
                     /region_name="PTZ00169"
                     /note="ADP/ATP transporter on adenylate translocase;
                     Provisional"
                     /db_xref="CDD:240302"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05962; propagated from
                     UniProtKB/Swiss-Prot (P12235.4)"
     Site            8..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Site            52
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q05962; propagated from
                     UniProtKB/Swiss-Prot (P12235.4)"
     Site            75..99
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          111..201
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Site            179..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Site            211..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          212..297
                     /region_name="Solcar 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          235..240
                     /region_name="Important for transport activity.
                     /evidence=ECO:0000269|PubMed:27693233"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Region          235..240
                     /region_name="Nucleotide carrier signature motif.
                     /evidence=ECO:0000250|UniProtKB:P02722"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     Site            274..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P12235.4)"
     CDS             1..298
                     /gene="SLC25A4"
                     /gene_synonym="AAC1; ANT; ANT 1; ANT1; MTDPS12; MTDPS12A;
                     PEO2; PEO3; PEOA2; T1"
                     /coded_by="NM_001151.4:108..1004"
                     /db_xref="CCDS:CCDS34114.1"
                     /db_xref="GeneID:291"
                     /db_xref="HGNC:HGNC:10990"
                     /db_xref="MIM:103220"
ORIGIN      
        1 mgdhawsflk dflaggvaaa vsktavapie rvklllqvqh askqisaekq ykgiidcvvr
       61 ipkeqgflsf wrgnlanvir yfptqalnfa fkdkykqlfl ggvdrhkqfw ryfagnlasg
      121 gaagatslcf vypldfartr laadvgkgaa qrefhglgdc iikifksdgl rglyqgfnvs
      181 vqgiiiyraa yfgvydtakg mlpdpknvhi fvswmiaqsv tavaglvsyp fdtvrrrmmm
      241 qsgrkgadim ytgtvdcwrk iakdegakaf fkgawsnvlr gmggafvlvl ydeikkyv
//
LOCUS       NP_060114                600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_060114
VERSION     NP_060114.2
DBSOURCE    REFSEQ: accession NM_017644.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY422472.1 and AC068769.19.
            
            On Dec 18, 2003 this sequence version replaced NP_060114.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (7), as well as variants 8-15,
            encodes isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY422472.1, SRR1660809.211238.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242810.11/ ENSP00000242810.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_017644.3:296..2098"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001306162             659 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-2 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001306162 XP_011539687
VERSION     NP_001306162.1
DBSOURCE    REFSEQ: accession NM_001319233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Zare,M., Hesampour,F., Poordast,T., Valibeigi,M., Enayatmehri,M.,
            Ahmadi,S., Nasri,F. and Gharesi-Fard,B.
  TITLE     Association between gene polymorphisms of IL-12, IL-12 receptor and
            IL-27 and organ involvement in Iranian endometriosis patients
  JOURNAL   Int J Immunogenet 50 (1), 24-33 (2023)
   PUBMED   36328955
  REMARK    GeneRIF: Association between gene polymorphisms of IL-12, IL-12
            receptor and IL-27 and organ involvement in Iranian endometriosis
            patients.
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Fu,Y., Liu,L. and Wu,H.
  TITLE     Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic Obstructive
            Pulmonary Disease
  JOURNAL   Int J Chron Obstruct Pulmon Dis 17, 1671-1683 (2022)
   PUBMED   35923356
  REMARK    GeneRIF: Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic
            Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Ye,C., Yano,H., Workman,C.J. and Vignali,D.A.A.
  TITLE     Interleukin-35: Structure, Function and Its Impact on
            Immune-Related Diseases
  JOURNAL   J Interferon Cytokine Res 41 (11), 391-406 (2021)
   PUBMED   34788131
  REMARK    Review article
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Wang,X., Zhou,S., Fan,M., Wang,P., Fang,H., Bian,F., Huang,T. and
            Du,X.
  TITLE     Expressions of IL-12 and its receptors in patients with lumbar disc
            herniation and their relationship with clinical efficacy
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 66 (7), 5-11 (2020)
   PUBMED   33287915
  REMARK    GeneRIF: Expressions of IL-12 and its receptors in patients with
            lumbar disc herniation and their relationship with clinical
            efficacy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Rogge,L., Barberis-Maino,L., Biffi,M., Passini,N., Presky,D.H.,
            Gubler,U. and Sinigaglia,F.
  TITLE     Selective expression of an interleukin-12 receptor component by
            human T helper 1 cells
  JOURNAL   J Exp Med 185 (5), 825-831 (1997)
   PUBMED   9120388
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Presky,D.H., Yang,H., Minetti,L.J., Chua,A.O., Nabavi,N., Wu,C.Y.,
            Gately,M.K. and Gubler,U.
  TITLE     A functional interleukin 12 receptor complex is composed of two
            beta-type cytokine receptor subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 14002-14007 (1996)
   PUBMED   8943050
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL389925.10, U64198.1,
            AK294494.1, AK316525.1, BC143248.1 and AL358512.9.
            
            On Feb 2, 2016 this sequence version replaced XP_011539687.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein identified as a subunit of the interleukin 12 receptor
            complex. The coexpression of this and IL12RB1 proteins was shown to
            lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. The expression of this
            gene is up-regulated by interferon gamma in Th1 cells, and plays a
            role in Th1 cell differentiation. The up-regulation of this gene is
            found to be associated with a number of infectious diseases, such
            as Crohn's disease and leprosy, which is thought to contribute to
            the inflammatory response and host defense. Several transcript
            variants encoding different isoforms and non-protein coding
            transcripts have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            lacks an alternate exon in the 3' coding region, resulting in a
            frameshift and an early stop codon, compared to variant 1. Variants
            2 and 7 encode the same isoform (b), which has a shorter and
            distinct C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316525.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..659
                     /product="interleukin-12 receptor subunit beta-2 isoform b
                     precursor"
                     /note="interleukin-12 receptor beta-2 chain; IL-12R
                     subunit beta-2; IL-12 receptor subunit beta-2; interleukin
                     12 receptor, beta 2"
                     /calculated_mol_wt=71955
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
                     /calculated_mol_wt=2671
     mat_peptide     24..659
                     /product="interleukin-12 receptor subunit beta-2 isoform
                     b"
                     /calculated_mol_wt=71955
     Region          28..110
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          224..316
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(224,286,304)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          305..309
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(305..306,308..309)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          <368..>608
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          423..511
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(507..508,510..511)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            623..643
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     CDS             1..659
                     /gene="IL12RB2"
                     /coded_by="NM_001319233.1:725..2704"
                     /note="isoform b precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS58006.1"
                     /db_xref="GeneID:3595"
                     /db_xref="HGNC:HGNC:5972"
                     /db_xref="MIM:601642"
ORIGIN      
        1 mahtfrgcsl afmfiitwll ikakidackr gdvtvkpshv illgstvnit cslkprqgcf
       61 hysrrnklil ykfdrrinfh hghslnsqvt glplgttlfv cklacinsde iqicgaeifv
      121 gvapeqpqnl sciqkgeqgt vactwergrd thlyteytlq lsgpknltwq kqckdiycdy
      181 ldfginltpe spesnftakv tavnslgsss slpstftfld ivrplppwdi rikfqkasvs
      241 rctlywrdeg lvllnrlryr psnsrlwnmv nvtkakgrhd lldlkpftey efqissklhl
      301 ykgswsdwse slraqtpeee ptgmldvwym krhidysrqq islfwknlsv seargkilhy
      361 qvtlqeltgg kamtqnitgh tswttviprt gnwavavsaa nskgsslptr inimnlceag
      421 llaprqvsan segmdnilvt wqpprkdpsa vqeyvvewre lhpggdtqvp lnwlrsrpyn
      481 vsalisenik syicyeirvy alsgdqggcs silgnskhka plsgphinai teekgsilis
      541 wnsipvqeqm gcllhyriyw kerdsnsqpq lceipyrvsq nshpinslqp rvtyvlwmta
      601 ltaagesshg nerefclqgk anwmafvaps iciaiimvgi fsthyfqqkr rhscpwtgs
//
LOCUS       NP_689680                608 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_689680
VERSION     NP_689680.2
DBSOURCE    REFSEQ: accession NM_152467.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Qiu,Q.M., Liu,G., Li,W.N., Shi,Q.W., Zhu,F.X. and Lu,G.X.
  TITLE     [Mutation of KLHL-10 in idiopathic infertile males with
            azoospermia, oligospermia or asthenospermia]
  JOURNAL   Zhonghua Nan Ke Xue 15 (11), 974-979 (2009)
   PUBMED   20218307
  REMARK    GeneRIF: The KLHL-10 gene is not a major contributor to
            azoospermia, oligospermia or asthenospermia in Chinese population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Yatsenko,A.N., Roy,A., Chen,R., Ma,L., Murthy,L.J., Yan,W.,
            Lamb,D.J. and Matzuk,M.M.
  TITLE     Non-invasive genetic diagnosis of male infertility using
            spermatozoal RNA: KLHL10 mutations in oligozoospermic patients
            impair homodimerization
  JOURNAL   Hum Mol Genet 15 (23), 3411-3419 (2006)
   PUBMED   17047026
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Yan,W., Ma,L., Burns,K.H. and Matzuk,M.M.
  TITLE     Haploinsufficiency of kelch-like protein homolog 10 causes
            infertility in male mice
  JOURNAL   Proc Natl Acad Sci U S A 101 (20), 7793-7798 (2004)
   PUBMED   15136734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY495339.1 and AC125257.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 7, 2007 this sequence version replaced NP_689680.1.
            
            Summary: The protein encoded by this gene belongs to the kelch
            repeat-containing family, and contains an N-terminal BTB/POZ domain
            a BACK domain and six C-terminal kelch repeats. Kelch domains are
            thought to form a four stranded beta-sheet blade structure that can
            fold into a beta-propeller domain when multiple kelch repeats are
            found together. Mutations in this gene have been associated with
            oligozoospermia in some infertile males. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein
            (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.362446.1, HM005417.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293303.5/ ENSP00000293303.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..608
                     /product="kelch-like protein 10 isoform 1"
                     /note="kelch-like protein 10; testicular tissue protein Li
                     104"
                     /calculated_mol_wt=68811
     Region          36..572
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          292..339
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          329..372
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          340..386
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          376..420
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          388..433
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          423..466
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          434..480
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          470..513
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          481..527
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6JEL3; propagated from
                     UniProtKB/Swiss-Prot (Q6JEL2.1)"
     Region          517..561
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          529..574
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6JEL2.1)"
     CDS             1..608
                     /gene="KLHL10"
                     /gene_synonym="SPGF11"
                     /coded_by="NM_152467.5:109..1935"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42340.1"
                     /db_xref="GeneID:317719"
                     /db_xref="HGNC:HGNC:18829"
                     /db_xref="MIM:608778"
ORIGIN      
        1 memesaaast rfhqphmerk msamaceifn elrlegklcd vvikvngfef sahknilcsc
       61 ssyfralfts gwnntekkvy nipgispdmm kliieyaytr tvpitpdnve kllaaadqfn
      121 imgivrgcce flkselcldn cigickftdy yycpelrqka ymfilhnfee mvkvsaefle
      181 lsvtelkdii ekdelnvkqe davfeailkw ishdpqnrkq hisillpkvr lalmhaeyfm
      241 nnvkmndyvk dseeckpvii nalkamydln mngpsnsdft npltrprlpy ailfaiggws
      301 ggsptnaiea ydaradrwvn vtceeespra yhgaaylkgy vyiiggfdsv dyfnsvkrfd
      361 pvkktwhqva pmhsrrcyvs vtvlgnfiya mggfdgyvrl ntaeryepet nqwtliapmh
      421 eqrsdasatt lygkvyicgg fngneclfta evyntesnqw tviapmrsrr sgigviayge
      481 hvyavggfdg anrlrsaeay spvantwrti ptmfnprsnf gievvddllf vvggfngftt
      541 tfnvecydek tdewydahdm siyrsalscc vvpglanvee yaarrdnfpg lalrdevkys
      601 aststlpv
//
LOCUS       NP_001292493              71 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin-like protein 4A isoform 4 [Homo sapiens].
ACCESSION   NP_001292493
VERSION     NP_001292493.1
DBSOURCE    REFSEQ: accession NM_001305564.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Wood,K.A., Ellingford,J.M., Thomas,H.B., Douzgou,S., Beaman,G.M.,
            Hobson,E., Prescott,K., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics UK Research Consortium
  TITLE     Expanding the genotypic spectrum of TXNL4A variants in Burn-McKeown
            syndrome
  JOURNAL   Clin Genet 101 (2), 255-259 (2022)
   PUBMED   34713892
  REMARK    GeneRIF: Expanding the genotypic spectrum of TXNL4A variants in
            Burn-McKeown syndrome.
REFERENCE   5  (residues 1 to 71)
  AUTHORS   Wieczorek,D., Newman,W.G., Wieland,T., Berulava,T., Kaffe,M.,
            Falkenstein,D., Beetz,C., Graf,E., Schwarzmayr,T., Douzgou,S.,
            Clayton-Smith,J., Daly,S.B., Williams,S.G., Bhaskar,S.S.,
            Urquhart,J.E., Anderson,B., O'Sullivan,J., Boute,O., Gundlach,J.,
            Czeschik,J.C., van Essen,A.J., Hazan,F., Park,S., Hing,A.,
            Kuechler,A., Lohmann,D.R., Ludwig,K.U., Mangold,E., Steenpass,L.,
            Zeschnigk,M., Lemke,J.R., Lourenco,C.M., Hehr,U., Prott,E.C.,
            Waldenberger,M., Bohmer,A.C., Horsthemke,B., O'Keefe,R.T.,
            Meitinger,T., Burn,J., Ludecke,H.J. and Strom,T.M.
  TITLE     Compound heterozygosity of low-frequency promoter deletions and
            rare loss-of-function mutations in TXNL4A causes Burn-McKeown
            syndrome
  JOURNAL   Am J Hum Genet 95 (6), 698-707 (2014)
   PUBMED   25434003
  REMARK    GeneRIF: Reporter gene and in vivo assays showed that the promoter
            deletions led to reduced expression of TXNL4A. Depletion of TXNL4A
            (Dib1) in yeast demonstrated reduced assembly of the tri-snRNP
            complex.
REFERENCE   6  (residues 1 to 71)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   7  (residues 1 to 71)
  AUTHORS   Zhang,Y., Lindblom,T., Chang,A., Sudol,M., Sluder,A.E. and
            Golemis,E.A.
  TITLE     Evidence that dim1 associates with proteins involved in pre-mRNA
            splicing, and delineation of residues essential for dim1
            interactions with hnRNP F and Npw38/PQBP-1
  JOURNAL   Gene 257 (1), 33-43 (2000)
   PUBMED   11054566
REFERENCE   8  (residues 1 to 71)
  AUTHORS   Reuter,K., Nottrott,S., Fabrizio,P., Luhrmann,R. and Ficner,R.
  TITLE     Identification, characterization and crystal structure analysis of
            the human spliceosomal U5 snRNP-specific 15 kD protein
  JOURNAL   J Mol Biol 294 (2), 515-525 (1999)
   PUBMED   10610776
REFERENCE   9  (residues 1 to 71)
  AUTHORS   Zhang,Y.Z., Gould,K.L., Dunbrack,R.L. Jr., Cheng,H., Roder,H. and
            Golemis,E.A.
  TITLE     The evolutionarily conserved Dim1 protein defines a novel branch of
            the thioredoxin fold superfamily
  JOURNAL   Physiol Genomics 1 (3), 109-118 (1999)
   PUBMED   11015569
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 71)
  AUTHORS   Ludecke,H.J. and Wieczorek,D.
  TITLE     TXNL4A-Related Craniofacial Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413799
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090360.9, AV729855.2,
            BQ011103.1 and BC001046.2.
            
            Summary: The protein encoded by this gene is a member of the U5
            small ribonucleoprotein particle (snRNP), and is involved in
            pre-mRNA splicing. This protein contains a thioredoxin-like fold
            and it is expected to interact with multiple proteins.
            Protein-protein interactions have been observed with the
            polyglutamine tract-binding protein 1 (PQBP1). Mutations in both
            the coding region and promoter region of this gene have been
            associated with Burn-McKeown syndrome, which is a rare disorder
            characterized by craniofacial dysmorphisms, cardiac defects,
            hearing loss, and bilateral choanal atresia. A pseudogene of this
            gene is found on chromosome 2. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (5) contains an alternate exon in
            its 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at a downstream start codon, compared to variant 1. The
            encoded isoform (4) has a shorter N-terminus than isoform 1.
            Variants 4 and 5 encode the same isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.83641.1,
                                           SRR1803614.77392.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..71
                     /product="thioredoxin-like protein 4A isoform 4"
                     /note="thioredoxin-like 4; DIM1 protein homolog;
                     thioredoxin-like U5 snRNP protein U5-15kD; spliceosomal U5
                     snRNP-specific 15 kDa protein"
                     /calculated_mol_wt=8332
     Region          <1..71
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     CDS             1..71
                     /gene="TXNL4A"
                     /gene_synonym="BMKS; DIB1; DIM1; SNRNP15; TXNL4; U5-15kD"
                     /coded_by="NM_001305564.2:147..362"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82260.1"
                     /db_xref="GeneID:10907"
                     /db_xref="HGNC:HGNC:30551"
                     /db_xref="MIM:611595"
ORIGIN      
        1 myelydpctv mfffrnkhim idlgtgnnnk inwamedkqe mvdiietvyr garkgrglvv
       61 spkdystkyr y
//
LOCUS       NP_444295                561 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquilin-1 isoform 2 [Homo sapiens].
ACCESSION   NP_444295
VERSION     NP_444295.1
DBSOURCE    REFSEQ: accession NM_053067.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Zhao,S., Li,J., Duan,S., Liu,C., Wang,H., Lu,J., Zhao,N., Sheng,X.,
            Wu,Y., Li,Y., Sun,B. and Liu,L.
  TITLE     UBQLN1 links proteostasis and mitochondria function to telomere
            maintenance in human embryonic stem cells
  JOURNAL   Stem Cell Res Ther 15 (1), 180 (2024)
   PUBMED   38902824
  REMARK    GeneRIF: UBQLN1 links proteostasis and mitochondria function to
            telomere maintenance in human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Zhou,H., Xie,C., Xie,Y., He,Y., Chen,Y., Zhang,C., Zhang,Y.,
            Zhao,Y. and Liu,H.
  TITLE     UBQLN1 deficiency mediates telomere shortening and IPF through
            interacting with RPA1
  JOURNAL   PLoS Genet 19 (7), e1010856 (2023)
   PUBMED   37463174
  REMARK    GeneRIF: UBQLN1 deficiency mediates telomere shortening and IPF
            through interacting with RPA1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Hanaoka,E., Ozaki,T., Ohira,M., Nakamura,Y., Suzuki,M.,
            Takahashi,E., Moriya,H., Nakagawara,A. and Sakiyama,S.
  TITLE     Molecular cloning and expression analysis of the human DA41 gene
            and its mapping to chromosome 9q21.2-q21.3
  JOURNAL   J Hum Genet 45 (3), 188-191 (2000)
   PUBMED   10807547
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Wu,A.L., Wang,J., Zheleznyak,A. and Brown,E.J.
  TITLE     Ubiquitin-related proteins regulate interaction of vimentin
            intermediate filaments with the plasma membrane
  JOURNAL   Mol Cell 4 (4), 619-625 (1999)
   PUBMED   10549293
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Ozaki,T., Hanaoka,E., Naka,M., Nakagawara,A. and Sakiyama,S.
  TITLE     Cloning and characterization of rat BAT3 cDNA
  JOURNAL   DNA Cell Biol 18 (6), 503-512 (1999)
   PUBMED   10390159
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Ozaki,T., Kondo,K., Nakamura,Y., Ichimiya,S., Nakagawara,A. and
            Sakiyama,S.
  TITLE     Interaction of DA41, a DAN-binding protein, with the epidermal
            growth factor-like protein, S(1-5)
  JOURNAL   Biochem Biophys Res Commun 237 (2), 245-250 (1997)
   PUBMED   9268694
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Ozaki,T., Hishiki,T., Toyama,Y., Yuasa,S., Nakagawara,A. and
            Sakiyama,S.
  TITLE     Identification of a new cellular protein that can interact
            specifically with DAN
  JOURNAL   DNA Cell Biol 16 (8), 985-991 (1997)
   PUBMED   9303440
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA317805.1, BC010066.2 and
            BC039294.1.
            
            Summary: This gene encodes an ubiquitin-like protein (ubiquilin)
            that shares a high degree of similarity with related products in
            yeast, rat and frog. Ubiquilins contain an N-terminal
            ubiquitin-like domain and a C-terminal ubiquitin-associated domain.
            They physically associate with both proteasomes and ubiquitin
            ligases, and thus are thought to functionally link the
            ubiquitination machinery to the proteasome to affect in vivo
            protein degradation. This ubiquilin has also been shown to modulate
            accumulation of presenilin proteins, and it is found in lesions
            associated with Alzheimer's and Parkinson's disease. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) is missing an alternate 3'
            coding exon, compared to transcript variant 1. The resulting
            protein (isoform 2) is 28 aa shorter when compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1720133.1, BC010066.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.32"
     Protein         1..561
                     /product="ubiquilin-1 isoform 2"
                     /note="hPLIC-1; protein linking IAP with cytoskeleton 1;
                     testicular tissue protein Li 219; DSK2 homolog"
                     /calculated_mol_wt=59089
     Region          35..107
                     /region_name="Ubl_PLICs"
                     /note="ubiquitin-like (Ubl) domain found in eukaryotic
                     protein linking integrin-associated protein (IAP, also
                     known as CD47) with cytoskeleton (PLIC) proteins; cd01808"
                     /db_xref="CDD:340506"
     Site            order(42,79..84,100..103,105,107)
                     /site_type="other"
                     /note="Pru interaction site [polypeptide binding]"
                     /db_xref="CDD:340506"
     Site            order(72,75,79,81..84,86,103,105..107)
                     /site_type="other"
                     /note="putative S5a binding site"
                     /db_xref="CDD:340506"
     Region          182..219
                     /region_name="STI1"
                     /note="Heat shock chaperonin-binding motif; smart00727"
                     /db_xref="CDD:128966"
     Region          212..256
                     /region_name="STI1"
                     /note="STI1 domain; cl17974"
                     /db_xref="CDD:450205"
     Region          390..435
                     /region_name="STI1"
                     /note="Heat shock chaperonin-binding motif; smart00727"
                     /db_xref="CDD:128966"
     Region          518..557
                     /region_name="UBA_PLICs"
                     /note="UBA domain of eukaryotic protein linking
                     integrin-associated protein (IAP, also known as CD47) with
                     cytoskeleton (PLIC) proteins; cd14399"
                     /db_xref="CDD:270582"
     Site            order(528..533,549,552..554,556..557)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270582"
     CDS             1..561
                     /gene="UBQLN1"
                     /gene_synonym="DA41; DSK2; PLIC-1; UBQN; XDRP1"
                     /coded_by="NM_053067.3:280..1965"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6664.1"
                     /db_xref="GeneID:29979"
                     /db_xref="HGNC:HGNC:12508"
                     /db_xref="MIM:605046"
ORIGIN      
        1 maesgesggp pgsqdsaaga egagapaaaa saepkimkvt vktpkekeef avpenssvqq
       61 fkeeiskrfk shtdqlvlif agkilkdqdt lsqhgihdgl tvhlviktqn rpqdhsaqqt
      121 ntagsnvtts stpnsnstsg satsnpfglg glgglaglss lglnttnfse lqsqmqrqll
      181 snpemmvqim enpfvqsmls npdlmrqlim anpqmqqliq rnpeishmln npdimrqtle
      241 larnpammqe mmrnqdrals nlesipggyn alrrmytdiq epmlsaaqeq fggnpfaslv
      301 sntssgegsq psrtenrdpl pnpwapqtsq sssassgtas tvggttgsta sgtsgqstta
      361 pnlvpgvgas mfntpgmqsl lqqitenpql mqnmlsapym rsmmqslsqn pdlaaqmqnp
      421 dtlsamsnpr amqallqiqq glqtlateap glipgftpgl galgstggss gtngsnatps
      481 entsptagtt epghqqfiqq mlqalagvnp qlqnpevrfq qqleqlsamg flnreanlqa
      541 liatggdina aierllgsqp s
//
LOCUS       NP_001121089             364 aa            linear   PRI 20-NOV-2025
DEFINITION  fructose-bisphosphate aldolase A isoform 1 [Homo sapiens].
ACCESSION   NP_001121089
VERSION     NP_001121089.1
DBSOURCE    REFSEQ: accession NM_001127617.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Xu,Z., Lv,C., Gao,J., Cui,Y., Liu,W., He,Z. and He,L.
  TITLE     LncRNA ACVR2B-as1 interacts with ALDOA to regulate the self-renewal
            and apoptosis of human spermatogonial stem cells by controlling
            glycolysis activity
  JOURNAL   Cell Mol Life Sci 81 (1), 391 (2024)
   PUBMED   39254854
  REMARK    GeneRIF: LncRNA ACVR2B-as1 interacts with ALDOA to regulate the
            self-renewal and apoptosis of human spermatogonial stem cells by
            controlling glycolysis activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Yeh,C.Y., Cai,H.Y., Kuo,H.H., Lin,Y.Y., He,Z.J., Cheng,H.C.,
            Yang,C.J., Huang,C.F. and Chang,Y.C.
  TITLE     ALDOA coordinates PDE3A through the beta-catenin/ID3 axis to
            stimulate cancer metastasis and M2 polarization in lung cancer with
            EGFR mutations
  JOURNAL   Biochem Biophys Res Commun 696, 149489 (2024)
   PUBMED   38244313
  REMARK    GeneRIF: ALDOA coordinates PDE3A through the beta-catenin/ID3 axis
            to stimulate cancer metastasis and M2 polarization in lung cancer
            with EGFR mutations.
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Mukai,T., Arai,Y., Yatsuki,H., Joh,K. and Hori,K.
  TITLE     An additional promoter functions in the human aldolase A gene, but
            not in rat
  JOURNAL   Eur J Biochem 195 (3), 781-787 (1991)
   PUBMED   1999195
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Izzo,P., Costanzo,P., Lupo,A., Rippa,E., Paolella,G. and
            Salvatore,F.
  TITLE     Human aldolase A gene. Structural organization and tissue-specific
            expression by multiple promoters and alternate mRNA processing
  JOURNAL   Eur J Biochem 174 (4), 569-578 (1988)
   PUBMED   3391172
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Kishi,H., Mukai,T., Hirono,A., Fujii,H., Miwa,S. and Hori,K.
  TITLE     Human aldolase A deficiency associated with a hemolytic anemia:
            thermolabile aldolase due to a single base mutation
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8623-8627 (1987)
   PUBMED   2825199
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Maire,P., Gautron,S., Hakim,V., Gregori,C., Mennecier,F. and
            Kahn,A.
  TITLE     Characterization of three optional promoters in the 5' region of
            the human aldolase A gene
  JOURNAL   J Mol Biol 197 (3), 425-438 (1987)
   PUBMED   3441006
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Sakakibara,M., Mukai,T. and Hori,K.
  TITLE     Nucleotide sequence of a cDNA clone for human aldolase: a messenger
            RNA in the liver
  JOURNAL   Biochem Biophys Res Commun 131 (1), 413-420 (1985)
   PUBMED   3840020
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Rehbein-Thoner,M. and Pfleiderer,G.
  TITLE     The changes in aldolase isoenzyme pattern during development of the
            human kidney and small intestine--demonstrated in organ extracts
            and tissue sections
  JOURNAL   Hoppe Seylers Z Physiol Chem 358 (2), 169-180 (1977)
   PUBMED   844801
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Pfleiderer,G., Thoner,M. and Wachsmuth,E.D.
  TITLE     Histological examination of the aldolase monomer composition of
            cells from human kidney and hypernephroid carcinoma
  JOURNAL   Beitr Pathol 156 (3), 266-279 (1975)
   PUBMED   766744
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA899482.1, BX647566.1 and
            BU855133.1.
            
            Summary: This gene encodes a member of the class I
            fructose-bisphosphate aldolase protein family. The encoded protein
            is a glycolytic enzyme that catalyzes the reversible conversion of
            fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and
            dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C),
            encoded by three different genes, are differentially expressed
            during development. Mutations in this gene have been associated
            with Glycogen Storage Disease XII, an autosomal recessive disorder
            associated with hemolytic anemia. Disruption of this gene also
            plays a role in the progression of multiple types of cancers.
            Related pseudogenes have been identified on chromosomes 3 and 10.
            [provided by RefSeq, Sep 2017].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. Variants 2, 3, 4, 7, 8, 9, and 10 encode the
            same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279875.3176.1,
                                           SRR1163655.487494.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..364
                     /product="fructose-bisphosphate aldolase A isoform 1"
                     /EC_number="4.1.2.13"
                     /note="fructose-1,6-bisphosphate triosephosphate-lyase;
                     muscle-type aldolase; lung cancer antigen NY-LU-1;
                     epididymis secretory sperm binding protein Li 87p;
                     aldolase A, fructose-bisphosphate"
                     /calculated_mol_wt=39289
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P05065; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Region          15..364
                     /region_name="Glycolytic"
                     /note="Fructose-bisphosphate aldolase class-I; pfam00274"
                     /db_xref="CDD:459742"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P04075.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04075.2)"
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            111
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P09972; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05065; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            330
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            364
                     /site_type="other"
                     /note="Necessary for preference for fructose
                     1,6-bisphosphate over fructose 1-phosphate; propagated
                     from UniProtKB/Swiss-Prot (P04075.2)"
     CDS             1..364
                     /gene="ALDOA"
                     /gene_synonym="ALDA; GSD12; HEL-S-87p"
                     /coded_by="NM_001127617.2:310..1404"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS10668.1"
                     /db_xref="GeneID:226"
                     /db_xref="HGNC:HGNC:414"
                     /db_xref="MIM:103850"
ORIGIN      
        1 mpyqypaltp eqkkelsdia hrivapgkgi laadestgsi akrlqsigte nteenrrfyr
       61 qllltaddrv npciggvilf hetlyqkadd grpfpqviks kggvvgikvd kgvvplagtn
      121 getttqgldg lsercaqykk dgadfakwrc vlkigehtps alaimenanv laryasicqq
      181 ngivpivepe ilpdgdhdlk rcqyvtekvl aavykalsdh hiylegtllk pnmvtpghac
      241 tqkfsheeia matvtalrrt vppavtgitf lsggqseeea sinlnainkc pllkpwaltf
      301 sygralqasa lkawggkken lkaaqeeyvk ralanslacq gkytpsgqag aaaseslfvs
      361 nhay
//
LOCUS       NP_001124293             108 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 22 homolog isoform c [Homo
            sapiens].
ACCESSION   NP_001124293
VERSION     NP_001124293.1
DBSOURCE    REFSEQ: accession NM_001130821.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Silva,D.A., Huang,X., Behal,R.H., Cole,D.G. and Qin,H.
  TITLE     The RABL5 homolog IFT22 regulates the cellular pool size and the
            amount of IFT particles partitioned to the flagellar compartment in
            Chlamydomonas reinhardtii
  JOURNAL   Cytoskeleton (Hoboken) 69 (1), 33-48 (2012)
   PUBMED   22076686
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Adhiambo,C., Blisnick,T., Toutirais,G., Delannoy,E. and Bastin,P.
  TITLE     A novel function for the atypical small G protein Rab-like 5 in the
            assembly of the trypanosome flagellum
  JOURNAL   J Cell Sci 122 (Pt 6), 834-841 (2009)
   PUBMED   19240117
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA709553.1, DN993868.1, BC004522.2, AC006329.5 and CA841889.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. Variants 3 through 6
            encode the same isoform (c), which is shorter at the N-terminus,
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.314718.1,
                                           SRR6380200.68597.9 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..108
                     /product="intraflagellar transport protein 22 homolog
                     isoform c"
                     /note="RAB, member of RAS oncogene family-like 5; rab-like
                     protein 5; RAB, member RAS oncogene family-like 5;
                     intraflagellar transport protein 22 homolog;
                     intraflagellar transport 22 homolog"
                     /calculated_mol_wt=12262
     CDS             1..108
                     /gene="IFT22"
                     /gene_synonym="CFAP9; FAP9; RABL5"
                     /coded_by="NM_001130821.3:366..692"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47671.1"
                     /db_xref="GeneID:64792"
                     /db_xref="HGNC:HGNC:21895"
                     /db_xref="MIM:620505"
ORIGIN      
        1 mkdahgvviv fnadipshrk ememwyscfv qqpslqdtqc mliahhkpgs gddkgslsls
       61 pplnklklvh snleddpeei rmefikylks iinsmsesrd reemsimt
//
LOCUS       NP_001353497             835 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001353497
VERSION     NP_001353497.1
DBSOURCE    REFSEQ: accession NM_001366568.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.55303.1,
                                           SRR1803616.98051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..835
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 6"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=94173
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <537..>671
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..835
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366568.1:2344..4851"
                     /note="isoform 6 is encoded by transcript variant 8"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels eseedkggkm aaadsvqqrr qyrrqnqqss sdsgssssse
      421 derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr mqmgkrwqsp vtksgrrrrs
      481 psppptrrrr spspappprr rrtptppprr rtpsppprrr spsprryspp iqrryspspp
      541 pkrrtasppp ppkrraspsp ppkrrvshsp ppkqrsspvt krrspslssk hrkgsspsrs
      601 trearspqpn krhspsprpr apqtsssppp vrrgassspq rrqspspstr pirrvsrtpe
      661 pkkikkaasp spqsvrrvss srsvsgspep aakkppapps pvqsqspstn wspavpvkka
      721 ksptpspspp rnsdqegggk kkkkkkdkkh kkdkkhkkhk khkkekavaa aaaaavtpaa
      781 iaaatttlaq eepvaapepk keteseaedn lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_006101                341 aa            linear   PRI 20-NOV-2025
DEFINITION  CD2 antigen cytoplasmic tail-binding protein 2 [Homo sapiens].
ACCESSION   NP_006101
VERSION     NP_006101.1
DBSOURCE    REFSEQ: accession NM_006110.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Riabov Bassat,D., Visanpattanasin,S., Vorlander,M.K., Fin,L.,
            Phillips,A.W. and Plaschka,C.
  TITLE     Structural basis of human U5 snRNP late biogenesis and recycling
  JOURNAL   Nat Struct Mol Biol 31 (5), 747-751 (2024)
   PUBMED   38467876
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Freund,C., Dotsch,V., Nishizawa,K., Reinherz,E.L. and Wagner,G.
  TITLE     The GYF domain is a novel structural fold that is involved in
            lymphoid signaling through proline-rich sequences
  JOURNAL   Nat Struct Biol 6 (7), 656-660 (1999)
   PUBMED   10404223
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Nishizawa,K., Freund,C., Li,J., Wagner,G. and Reinherz,E.L.
  TITLE     Identification of a proline-binding motif regulating CD2-triggered
            T lymphocyte activation
  JOURNAL   Proc Natl Acad Sci U S A 95 (25), 14897-14902 (1998)
   PUBMED   9843987
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Dustin,M.L., Olszowy,M.W., Holdorf,A.D., Li,J., Bromley,S.,
            Desai,N., Widder,P., Rosenberger,F., van der Merwe,P.A., Allen,P.M.
            and Shaw,A.S.
  TITLE     A novel adaptor protein orchestrates receptor patterning and
            cytoskeletal polarity in T-cell contacts
  JOURNAL   Cell 94 (5), 667-677 (1998)
   PUBMED   9741631
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Behrens,S.E. and Luhrmann,R.
  TITLE     Immunoaffinity purification of a [U4/U6.U5] tri-snRNP from human
            cells
  JOURNAL   Genes Dev 5 (8), 1439-1452 (1991)
   PUBMED   1831175
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Bach,M., Winkelmann,G. and Luhrmann,R.
  TITLE     20S small nuclear ribonucleoprotein U5 shows a surprisingly complex
            protein composition
  JOURNAL   Proc Natl Acad Sci U S A 86 (16), 6038-6042 (1989)
   PUBMED   2527369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB135964.1, BC001947.1 and
            AB033004.1.
            
            Summary: This gene encodes a bi-functional protein. In the
            cytoplasm, the encoded protein binds the cytoplasmic tail of human
            surface antigen CD2 via its C-terminal GYF domain, and regulate
            CD2-triggered T lymphocyte activation. In the nucleus, this protein
            is a component of the U5 small nuclear ribonucleoprotein complex
            and is involved in RNA splicing. A pseudogene has been identified
            on chromosome 7. Alternative splicing results in multiple
            transcript variants but their biological validity has not been
            determined. [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (1) represents the shorter and
            more abundant transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.218207.1,
                                           SRR1803614.124003.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305596.8/ ENSP00000304903.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..341
                     /product="CD2 antigen cytoplasmic tail-binding protein 2"
                     /note="U5 snRNP 52K protein; CD2 cytoplasmic
                     domain-binding protein 2; protein phosphatase 1,
                     regulatory subunit 59"
                     /calculated_mol_wt=37515
     Region          1..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95400.1)"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWK3; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Region          131..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95400.1)"
     Region          178..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95400.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95400.1)"
     Region          280..340
                     /region_name="GYF"
                     /note="GYF domain: contains conserved Gly-Tyr-Phe
                     residues; Proline-binding domain in CD2-binding and other
                     proteins. Involved in signaling lymphocyte activity. Also
                     present in other unrelated proteins (mainly unknown)
                     derived from diverse eukaryotic species; cd00072"
                     /db_xref="CDD:238027"
     Site            297..313
                     /site_type="active"
                     /note="proline binding motif [active]"
                     /db_xref="CDD:238027"
     Site            order(307,312..313)
                     /site_type="active"
                     /note="proline interaction residues [active]"
                     /db_xref="CDD:238027"
     CDS             1..341
                     /gene="CD2BP2"
                     /gene_synonym="FWP010; LIN1; PPP1R59; Snu40; U5-52K"
                     /coded_by="NM_006110.3:124..1149"
                     /db_xref="CCDS:CCDS10675.1"
                     /db_xref="GeneID:10421"
                     /db_xref="HGNC:HGNC:1656"
                     /db_xref="MIM:604470"
ORIGIN      
        1 mpkrkvtfqg vgdeededei ivpkkklvdp vagsggpgsr fkgkhsldsd eeeddddggs
       61 skydilased vegqeaatlp seggvritpf nlqeemeegh fdadgnyfln rdaqirdswl
      121 dnidwvkire rppgqrqasd seeedslgqt smsaqalleg llelllpret vagalrrlga
      181 rgggkgrkgp gqpsspqrld rlsgladqmv argnlgvyqe trerlamrlk glgcqtlgph
      241 nptpppsldm faeelaeeel etptptqrge aesrgdglvd vmweykwent gdaelygpft
      301 saqmqtwvse gyfpdgvycr kldppggqfy nskridfdly t
//
LOCUS       NP_003153                780 aa            linear   PRI 20-NOV-2025
DEFINITION  striatin [Homo sapiens].
ACCESSION   NP_003153
VERSION     NP_003153.2
DBSOURCE    REFSEQ: accession NM_003162.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 780)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 780)
  AUTHORS   Gholami,S.K., Heydarpour,M., Williams,J.S., Pojoga,L.H.,
            Adler,G.K., Williams,G.H. and Romero,J.R.
  TITLE     Striatin Gene Variants Are Associated With Salt Sensitivity of
            Blood Pressure by Mechanisms That Differ in Women and Men
  JOURNAL   Hypertension 81 (2), 330-339 (2024)
   PUBMED   38018471
  REMARK    GeneRIF: Striatin Gene Variants Are Associated With Salt
            Sensitivity of Blood Pressure by Mechanisms That Differ in Women
            and Men.
REFERENCE   3  (residues 1 to 780)
  AUTHORS   Viveka,M., Chaturvedula,L., Ram,A.K. and Vairappan,B.
  TITLE     Placental expression of striatin & endothelial nitric oxide
            synthase in women with & without pre-eclampsia
  JOURNAL   Indian J Med Res 157 (4), 345-352 (2023)
   PUBMED   37147942
  REMARK    GeneRIF: Placental expression of striatin & endothelial nitric
            oxide synthase in women with & without pre-eclampsia.
REFERENCE   4  (residues 1 to 780)
  AUTHORS   Liu,L., Weber,A., Linne,U., Shehata,M., Pleschka,S., Kracht,M. and
            Schmitz,M.L.
  TITLE     Phosphorylation of Influenza A Virus Matrix Protein 1 at Threonine
            108 Controls Its Multimerization State and Functional Association
            with the STRIPAK Complex
  JOURNAL   mBio 14 (1), e0323122 (2023)
   PUBMED   36602306
  REMARK    GeneRIF: Phosphorylation of Influenza A Virus Matrix Protein 1 at
            Threonine 108 Controls Its Multimerization State and Functional
            Association with the STRIPAK Complex.
REFERENCE   5  (residues 1 to 780)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 780)
  AUTHORS   Gaillard,S., Bartoli,M., Castets,F. and Monneron,A.
  TITLE     Striatin, a calmodulin-dependent scaffolding protein, directly
            binds caveolin-1
  JOURNAL   FEBS Lett 508 (1), 49-52 (2001)
   PUBMED   11707266
REFERENCE   7  (residues 1 to 780)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
REFERENCE   8  (residues 1 to 780)
  AUTHORS   Moreno,C.S., Park,S., Nelson,K., Ashby,D., Hubalek,F., Lane,W.S.
            and Pallas,D.C.
  TITLE     WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are
            members of a novel family of calmodulin-binding proteins that
            associate with protein phosphatase 2A
  JOURNAL   J Biol Chem 275 (8), 5257-5263 (2000)
   PUBMED   10681496
REFERENCE   9  (residues 1 to 780)
  AUTHORS   Moqrich,A., Mattei,M.G., Bartoli,M., Rakitina,T., Baillat,G.,
            Monneron,A. and Castets,F.
  TITLE     Cloning of human striatin cDNA (STRN), gene mapping to 2p22-p21,
            and preferential expression in brain
  JOURNAL   Genomics 51 (1), 136-139 (1998)
   PUBMED   9693043
REFERENCE   10 (residues 1 to 780)
  AUTHORS   Castets,F., Bartoli,M., Barnier,J.V., Baillat,G., Salin,P.,
            Moqrich,A., Bourgeois,J.P., Denizot,F., Rougon,G., Calothy,G. and
            Monneron,A.
  TITLE     A novel calmodulin-binding protein, belonging to the WD-repeat
            family, is localized in dendrites of a subset of CNS neurons
  JOURNAL   J Cell Biol 134 (4), 1051-1062 (1996)
   PUBMED   8769426
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007404.4, AJ223814.1, AK026934.1 and AC007382.3.
            
            On Aug 16, 2004 this sequence version replaced NP_003153.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.9708.1,
                                           SRR1803617.227778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263918.9/ ENSP00000263918.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..780
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.2"
     Protein         1..780
                     /product="striatin"
                     /note="striatin, calmodulin binding protein; protein
                     phosphatase 2 regulatory subunit B'''alpha"
                     /calculated_mol_wt=86001
     Region          49..173
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          55..63
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          124..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Region          149..166
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O55106; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43815.4)"
     Region          289..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          365..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          455..779
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          461..500
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Site            order(462,480,484,490..491,514..515,533,537,543..544,
                     567..568,585,590,596..597,616,633,642..643,655..656,681,
                     685,691..692,704..705,722,727,733..734,746..747,769,773,
                     779)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          468..514
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          514..553
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          520..567
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          567..606
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          572..608
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          616..654
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          662..701
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          667..703
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          704..743
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          709..745
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          750..780
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O43815.4)"
     Region          755..779
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..780
                     /gene="STRN"
                     /gene_synonym="PPP2R6A; SG2NA; STRN1"
                     /coded_by="NM_003162.4:74..2416"
                     /db_xref="CCDS:CCDS1784.1"
                     /db_xref="GeneID:6801"
                     /db_xref="HGNC:HGNC:11424"
                     /db_xref="MIM:614765"
ORIGIN      
        1 mdeqagpgvf fsnnhpgagg akglgplaea aaagdgaaaa gaaraqyslp gilhflqhew
       61 arfeveraqw everaelqaq iaflqgerkg qenlkkdlvr rikmleyalk qerakyhklk
      121 ygtelnqgdm kppsydsdeg netevqpqqn sqlmwkqgrq llrqylqevg ytdtildvks
      181 krvrallgfs sdvtdreddk nqdsvvngte aevketamia kseltdsasv ldnfkflesa
      241 aadfsdeded ddvdgreksv idtstivrkk alpdsgedrd tkealkefdf lvtseegdne
      301 srsagdgtdw ekedqclmpe awnvdqgvit klkeqykker kgkkgvkrpn rsklqdmlan
      361 lrdvdelpsl qpsvgspsrp sssrlpehei nradevealt fppssgksfi mgadealese
      421 lglgelaglt vaneadslty diannkdalr ktwnpkftlr shfdgirala fhpiepvlit
      481 asedhtlkmw nlqktapakk stsldvepiy tfrahkgpvl cvvmssngeq cysggtdgli
      541 qgwnttnpni dpydsydpsv lrgpllghtd avwglaysaa hqrllscsad gtlrlwntte
      601 vapalsvfnd tkelgipasv dlvssdpshm vasfskgyts ifnmetqqri ltlesnvdtt
      661 ansscqinrv ishptlpisi tahedrhikf ydnntgklih smvahleavt slavdpngly
      721 lmsgshdcsi rlwnlesktc iqeftahrkk feesihdvaf hpskcyiasa gadalakvfv
//
LOCUS       NP_002052                274 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate--cysteine ligase regulatory subunit isoform 1 [Homo
            sapiens].
ACCESSION   NP_002052
VERSION     NP_002052.1
DBSOURCE    REFSEQ: accession NM_002061.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Da,D., Pan,Z., Zeng,L., Dang,Y., Dang,C., Huang,Y., Shi,D. and
            Li,H.
  TITLE     Glutamate-cysteine ligase catalytic and its modifier function as
            novel immunotargets in gastric adenocarcinoma
  JOURNAL   Asian J Surg 46 (1), 143-149 (2023)
   PUBMED   35241341
  REMARK    GeneRIF: Glutamate-cysteine ligase catalytic and its modifier
            function as novel immunotargets in gastric adenocarcinoma.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Yang,C., Xi,M., Liu,H., Bai,H., Jiang,C., Liu,Q. and Fan,P.
  TITLE     Association of Polymorphisms of Glutamate Cysteine Ligase Genes
            GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women
  JOURNAL   Reprod Sci 29 (6), 1790-1800 (2022)
   PUBMED   34642912
  REMARK    GeneRIF: Association of Polymorphisms of Glutamate Cysteine Ligase
            Genes GCLC C-129 T and GCLM C-588 T with Risk of Polycystic Ovary
            Syndrome in Chinese Women.
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Mazloomi,S., Khodadadi,I., Alizadeh,N. and Shafiee,G.
  TITLE     Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia
  JOURNAL   Pregnancy Hypertens 23, 163-168 (2021)
   PUBMED   33421846
  REMARK    GeneRIF: Association of glutamate cystein ligase (GCL) activity
            Peroxiredoxin 4 (prxR4) and apelin levels in women with
            preeclampsia.
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Misra,I. and Griffith,O.W.
  TITLE     Expression and purification of human gamma-glutamylcysteine
            synthetase
  JOURNAL   Protein Expr Purif 13 (2), 268-276 (1998)
   PUBMED   9675072
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Sierra-Rivera,E., Dasouki,M., Summar,M.L., Krishnamani,M.R.,
            Meredith,M., Rao,P.N., Phillips,J.A. 3rd and Freeman,M.L.
  TITLE     Assignment of the human gene (GLCLR) that encodes the regulatory
            subunit of gamma-glutamylcysteine synthetase to chromosome 1p21
  JOURNAL   Cytogenet Cell Genet 72 (2-3), 252-254 (1996)
   PUBMED   8978789
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Tsuchiya,K., Mulcahy,R.T., Reid,L.L., Disteche,C.M. and
            Kavanagh,T.J.
  TITLE     Mapping of the glutamate-cysteine ligase catalytic subunit gene
            (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of
            the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22
            and mouse chromosome 3H1-3
  JOURNAL   Genomics 30 (3), 630-632 (1995)
   PUBMED   8825659
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Gipp,J.J., Bailey,H.H. and Mulcahy,R.T.
  TITLE     Cloning and sequencing of the cDNA for the light subunit of human
            liver gamma-glutamylcysteine synthetase and relative mRNA levels
            for heavy and light subunits in human normal tissues
  JOURNAL   Biochem Biophys Res Commun 206 (2), 584-589 (1995)
   PUBMED   7826375
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290449.1, BC041809.1,
            CB123306.1, CN272168.1, BQ049850.1, N53134.1, CN422503.1,
            BF513627.1, BM982562.1 and BU754400.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase, is the first rate limiting
            enzyme of glutathione synthesis. The enzyme consists of two
            subunits, a heavy catalytic subunit and a light regulatory subunit.
            Gamma glutamylcysteine synthetase deficiency has been implicated in
            some forms of hemolytic anemia. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1898476.1,
                                           SRR14038193.3111008.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370238.8/ ENSP00000359258.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..274
                     /product="glutamate--cysteine ligase regulatory subunit
                     isoform 1"
                     /EC_number="6.3.2.2"
                     /note="GSC light chain; glutamate-cysteine ligase
                     (gamma-glutamylcysteine synthetase), regulatory (30.8kD);
                     glutamate-cysteine ligase regulatory protein; GCS light
                     chain; glutamate-cysteine ligase modifier subunit delta2
                     alternative splicing; gamma-ECS regulatory subunit;
                     gamma-glutamylcysteine synthetase regulatory subunit"
                     /calculated_mol_wt=30596
     Region          <86..>211
                     /region_name="AKR_SF"
                     /note="Aldo-keto reductase (AKR) superfamily; cl00470"
                     /db_xref="CDD:444925"
     Site            263
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48507.1)"
     CDS             1..274
                     /gene="GCLM"
                     /gene_synonym="GLCLR"
                     /coded_by="NM_002061.4:268..1092"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS746.1"
                     /db_xref="GeneID:2730"
                     /db_xref="HGNC:HGNC:4312"
                     /db_xref="MIM:601176"
ORIGIN      
        1 mgtdsraaka llarartlhl qtgnllnwgr lrkkcpsths eelhdciqkt lnewssqinp
       61 dlvrefpdvl ectvshavek inpdereemk vsaklfives nsssstrsav dmacsvlgva
      121 qldsviiasp piedgvnlsl ehlqpyweel enlvqskkiv aigtsdldkt qleqlyqwaq
      181 vkpnsnqvnl asccvmppdl tafakqfdiq llthndpkel lseasfqeal qesipdiqah
      241 ewvplwllry svivksrgii kskgyilqak rrgs
//
LOCUS       NP_783165                576 aa            linear   PRI 20-NOV-2025
DEFINITION  WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing
            protein 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_783165
VERSION     NP_783165.1
DBSOURCE    REFSEQ: accession NM_175575.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: WFIKKN2 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Monestier,O. and Blanquet,V.
  TITLE     WFIKKN1 and WFIKKN2: 'Companion' proteins regulating TGFB activity
  JOURNAL   Cytokine Growth Factor Rev 32, 75-84 (2016)
   PUBMED   27325460
  REMARK    GeneRIF: In this review, we summarize current knowledge about the
            WFIKKN proteins and propose that they are 'companion' proteins for
            various growth factors by providing localized and sustained
            presentation of TGFB proteins to their respective receptors, thus
            regulating the balance between the activation of Smad and non-Smad
            pathways by TGFB.
            Review article
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Szlama,G., Trexler,M. and Patthy,L.
  TITLE     Latent myostatin has significant activity and this activity is
            controlled more efficiently by WFIKKN1 than by WFIKKN2
  JOURNAL   FEBS J 280 (16), 3822-3839 (2013)
   PUBMED   23829672
  REMARK    GeneRIF: Data suggest that myostatin binding to its receptor
            (activin receptors type II) can be blocked by WFIKKN1 but not
            WFIKKN2; various forms of myostatin (promyostatin, myostatin
            pro-domain, and latent/processed myostatin) bind WFIKKN1 but not
            WFIKKN2.
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Dieli-Conwright,C.M., Spektor,T.M., Rice,J.C., Sattler,F.R. and
            Schroeder,E.T.
  TITLE     Hormone therapy and maximal eccentric exercise alters
            myostatin-related gene expression in postmenopausal women
  JOURNAL   J Strength Cond Res 26 (5), 1374-1382 (2012)
   PUBMED   22395277
  REMARK    GeneRIF: After eccentric exercise, postmenopausal women not using
            hormone therapy (HT) expressed higher levels of GASP-1 while
            postmenopausal women using HT showed a significant increased
            expression over controls.
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Hill,J.J., Qiu,Y., Hewick,R.M. and Wolfman,N.M.
  TITLE     Regulation of myostatin in vivo by growth and differentiation
            factor-associated serum protein-1: a novel protein with protease
            inhibitor and follistatin domains
  JOURNAL   Mol Endocrinol 17 (6), 1144-1154 (2003)
   PUBMED   12595574
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Nagy,A., Trexler,M. and Patthy,L.
  TITLE     Expression, purification and characterization of the second
            Kunitz-type protease inhibitor domain of the human WFIKKN protein
  JOURNAL   Eur J Biochem 270 (9), 2101-2107 (2003)
   PUBMED   12709070
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Trexler,M., Banyai,L. and Patthy,L.
  TITLE     Distinct expression pattern of two related human proteins
            containing multiple types of protease-inhibitory modules
  JOURNAL   Biol Chem 383 (1), 223-228 (2002)
   PUBMED   11928817
  REMARK    GeneRIF: Newly discovered WFIKKNPR gene structure and tissue
            distribution of gene expression is commpared with that of the
            WFIKKN gene in adult and fetal tissues and organs
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY358142.1, AF468657.1,
            BG221308.1 and AC091062.5.
            
            Summary: The WFIKKN1 protein contains a WAP domain, follistatin
            domain, immunoglobulin domain, two tandem Kunitz domains, and an
            NTR domain. This gene encodes a WFIKKN1-related protein which has
            the same domain organization as the WFIKKN1 protein. The WAP-type,
            follistatin type, Kunitz-type, and NTR-type protease inhibitory
            domains may control the action of multiple types of proteases.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127743.1, AY358142.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311378.5/ ENSP00000311184.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..576
                     /product="WAP, Kazal, immunoglobulin, Kunitz and NTR
                     domain-containing protein 2 isoform 1 precursor"
                     /note="WFIKKN-related protein; WAP, FS, Ig, two KU and NTR
                     module related protein; multivalent protease inhibitor
                     protein; WAP, kazal, immunoglobulin, kunitz and NTR
                     domain-containing protein 2; growth and differentiation
                     factor-associated serum protein 1; WAP, follistatin,
                     immunoglobulin, kunitz and NTR domain-containing-related
                     protein; WAP four-disulfide core domain 20B"
                     /calculated_mol_wt=59940
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4020
     Region          42..91
                     /region_name="WAP"
                     /note="WAP-type (Whey Acidic Protein) 'four-disulfide
                     core'; pfam00095"
                     /db_xref="CDD:459672"
     Region          138..174
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cd00104"
                     /db_xref="CDD:238052"
     Site            140..141
                     /site_type="other"
                     /note="Reactive bond.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00798; propagated
                     from UniProtKB/Swiss-Prot (Q8TEU8.1)"
     Region          210..304
                     /region_name="IgI_3_WFIKKN-like"
                     /note="Third immunoglobulin-like domain of the human
                     WFIKKN (WAP, follistatin, immunoglobulin, Kunitz and NTR
                     domain-containing protein), and similar domains; member of
                     the I-set of Ig superfamily (IgSF) domains; cd05765"
                     /db_xref="CDD:409422"
     Region          210..213
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409422"
     Region          218..221
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409422"
     Region          226..233
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409422"
     Region          240..245
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409422"
     Region          246..248
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409422"
     Region          250..255
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409422"
     Region          263..269
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409422"
     Region          283..291
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409422"
     Region          294..304
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409422"
     Site            319
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TEU8.1)"
     Region          327..378
                     /region_name="Kunitz_WFIKKN_1-like"
                     /note="first Kunitz domain of WAP, Kazal, immunoglobulin,
                     Kunitz and NTR domain-containing proteins; cd22605"
                     /db_xref="CDD:438648"
     Site            order(334..338,340..342,357,361)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438648"
     Region          385..437
                     /region_name="Kunitz_WFIKKN_2-like"
                     /note="second Kunitz domain of WAP, Kazal, immunoglobulin,
                     Kunitz and NTR domain-containing proteins; cd22606"
                     /db_xref="CDD:438649"
     Site            order(392..396,398..400,415,419)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438649"
     Region          455..563
                     /region_name="NTR_WFIKKN"
                     /note="NTR domain, WFIKKN subfamily; WFIKKN proteins
                     contain a C-terminal NTR domain and are putative secreted
                     proteins which may be multivalent protease inhibitors that
                     act on serine proteases as well as metalloproteases. Human
                     WFIKKN and a related protein...; cd03575"
                     /db_xref="CDD:239630"
     Site            order(478,532,539,541)
                     /site_type="active"
                     /note="Metzincin-binding interface [active]"
                     /db_xref="CDD:239630"
     Site            519
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TEU8.1)"
     CDS             1..576
                     /gene="WFIKKN2"
                     /gene_synonym="GASP-1; hGASP-1; WFDC20B; WFIKKNRP"
                     /coded_by="NM_175575.6:353..2083"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS11575.1"
                     /db_xref="GeneID:124857"
                     /db_xref="HGNC:HGNC:30916"
                     /db_xref="MIM:610895"
ORIGIN      
        1 mwaprcrrfw srweqvaall llllllgvpp rslalppiry shagicpndm npnlwvdaqs
       61 tcrrecetdq ecetyekccp nvcgtkscva arymdvkgkk gpvgmpkeat cdhfmclqqg
      121 secdiwdgqp vckckdrcek epsftcasdg ltyynrcymd aeacskgitl avvtcryhft
      181 wpntsppppe ttmhpttasp etpeldmaap allnnpvhqs vtmgetvsfl cdvvgrprpe
      241 itwekqledr envvmrpnhv rgnvvvtnia qlviynaqlq dagiytctar nvagvlradf
      301 plsvvrghqa aatsesspng tafpaaeclk ppdsedcgee qtrwhfdaqa nncltftfgh
      361 chrnlnhfet yeacmlacms gplaacslpa lqgpckayap rwaynsqtgq cqsfvyggce
      421 gngnnfesre aceescpfpr gnqrcrackp rqklvtsfcr sdfvilgrvs elteepdsgr
      481 alvtvdevlk dekmglkflg qeplevtllh vdwacpcpnv tvsempliim gevdggmaml
      541 rpdsfvgass arrvrklrev mhkktcdvlk eflglh
//
LOCUS       NP_001139332            1024 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonucleases P/MRP protein subunit POP1 [Homo sapiens].
ACCESSION   NP_001139332
VERSION     NP_001139332.1
DBSOURCE    REFSEQ: accession NM_001145860.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1024)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1024)
  AUTHORS   Liang,F. and Huang,S.
  TITLE     PGC-1alpha inhibits NLRP3 signaling through transcriptional
            activation of POP1 to alleviate inflammation and strengthen
            osteogenic differentiation of lipopolysaccharide-induced human
            periodontal stem cells
  JOURNAL   Prostaglandins Other Lipid Mediat 174, 106853 (2024)
   PUBMED   38763227
  REMARK    GeneRIF: PGC-1alpha inhibits NLRP3 signaling through
            transcriptional activation of POP1 to alleviate inflammation and
            strengthen osteogenic differentiation of lipopolysaccharide-induced
            human periodontal stem cells.
REFERENCE   3  (residues 1 to 1024)
  AUTHORS   Zhu,M., Wu,C., Wu,X., Song,G., Li,M. and Wang,Q.
  TITLE     POP1 promotes the progression of breast cancer through maintaining
            telomere integrity
  JOURNAL   Carcinogenesis 44 (3), 252-262 (2023)
   PUBMED   37010429
  REMARK    GeneRIF: POP1 promotes the progression of breast cancer through
            maintaining telomere integrity.
REFERENCE   4  (residues 1 to 1024)
  AUTHORS   de Almeida,L., Devi,S., Indramohan,M., Huang,Q.Q.,
            Ratsimandresy,R.A., Pope,R.M., Dorfleutner,A. and Stehlik,C.
  TITLE     POP1 inhibits MSU-induced inflammasome activation and ameliorates
            gout
  JOURNAL   Front Immunol 13, 912069 (2022)
   PUBMED   36225929
  REMARK    GeneRIF: POP1 inhibits MSU-induced inflammasome activation and
            ameliorates gout.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1024)
  AUTHORS   He,X., Wang,J., Yu,H., Lv,W., Wang,Y., Zhang,Q., Liu,Z. and Wu,Y.
  TITLE     Clinical significance for diagnosis and prognosis of POP1 and its
            potential role in breast cancer: a comprehensive analysis based on
            multiple databases
  JOURNAL   Aging (Albany NY) 14 (17), 6936-6956 (2022)
   PUBMED   36084948
  REMARK    GeneRIF: Clinical significance for diagnosis and prognosis of POP1
            and its potential role in breast cancer: a comprehensive analysis
            based on multiple databases.
REFERENCE   6  (residues 1 to 1024)
  AUTHORS   Jiang,T., Guerrier-Takada,C. and Altman,S.
  TITLE     Protein-RNA interactions in the subunits of human nuclear RNase P
  JOURNAL   RNA 7 (7), 937-941 (2001)
   PUBMED   11455963
REFERENCE   7  (residues 1 to 1024)
  AUTHORS   Pluk,H., van Eenennaam,H., Rutjes,S.A., Pruijn,G.J. and van
            Venrooij,W.J.
  TITLE     RNA-protein interactions in the human RNase MRP ribonucleoprotein
            complex
  JOURNAL   RNA 5 (4), 512-524 (1999)
   PUBMED   10199568
REFERENCE   8  (residues 1 to 1024)
  AUTHORS   Dundr,M. and Olson,M.O.
  TITLE     Partially processed pre-rRNA is preserved in association with
            processing components in nucleolus-derived foci during mitosis
  JOURNAL   Mol Biol Cell 9 (9), 2407-2422 (1998)
   PUBMED   9725903
REFERENCE   9  (residues 1 to 1024)
  AUTHORS   Schmiedeknecht,G., Buchler,C. and Schmitz,G.
  TITLE     A bidirectional promoter connects the p14.5 gene to the gene for
            RNase P and RNase MRP protein subunit hPOP1
  JOURNAL   Biochem Biophys Res Commun 241 (1), 59-67 (1997)
   PUBMED   9405234
REFERENCE   10 (residues 1 to 1024)
  AUTHORS   Lygerou,Z., Pluk,H., van Venrooij,W.J. and Seraphin,B.
  TITLE     hPop1: an autoantigenic protein subunit shared by the human RNase P
            and RNase MRP ribonucleoproteins
  JOURNAL   EMBO J 15 (21), 5936-5948 (1996)
   PUBMED   8918471
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X99302.1, AK291434.1, D31765.1,
            AP003439.2 and BF511088.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the protein subunit of two different
            small nucleolar ribonucleoprotein complexes: the endoribonuclease
            for mitochondrial RNA processing complex and the ribonuclease P
            complex. The encoded protein is a ribonuclease that localizes to
            the nucleus and functions in pre-RNA processing. This protein is
            also an autoantigen in patients suffering from connective tissue
            diseases. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.265777.1,
                                           SRR1803616.101407.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401707.7/ ENSP00000385787.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1024
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..1024
                     /product="ribonucleases P/MRP protein subunit POP1"
                     /EC_number="3.1.26.5"
                     /note="processing of precursors 1; hPOP1; processing of
                     precursor 1, ribonuclease P/MRP subunit; POP1 homolog,
                     ribonuclease P/MRP subunit"
                     /calculated_mol_wt=114578
     Region          1..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Region          107..257
                     /region_name="POP1"
                     /note="Ribonucleases P/MRP protein subunit POP1;
                     pfam06978"
                     /db_xref="CDD:429227"
     Region          365..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99575.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99575.2)"
     Region          617..708
                     /region_name="POPLD"
                     /note="POPLD (NUC188) domain; pfam08170"
                     /db_xref="CDD:462391"
     Region          722..762
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q99575.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Region          773..792
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Region          819..838
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     Region          911..936
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99575.2)"
     CDS             1..1024
                     /gene="POP1"
                     /gene_synonym="ANXD2"
                     /coded_by="NM_001145860.2:101..3175"
                     /db_xref="CCDS:CCDS6277.1"
                     /db_xref="GeneID:10940"
                     /db_xref="HGNC:HGNC:30129"
                     /db_xref="MIM:602486"
ORIGIN      
        1 msnakerkha kkmrnqptnv tlssgfvadr gvkhhsggek pfqaqkqeph pgtsrqrqtr
       61 vnphslpdpe vneqssskgm frkkggwkag pegtsqeipk yitastfaqa raaeisamlk
      121 avtqkssnsl vfqtlprhmr rramshnvkr lprrlqeiaq keaekavhqk kehsknkchk
      181 arrchmnrtl efnrrqkkni wlethiwhak rfhmvkkwgy clgerptvks hracyramtn
      241 rcllqdlsyy cclelkgkee eilkalsgmc nidtgltfaa vhclsgkrqg slvlyrvnky
      301 premlgpvtf iwksqrtpgd psesrqlwiw lhptlkqdil eeikaacqcv epiksavcia
      361 dplptpsqek sqtelpdeki gkkrkrkddg enakpikkii gdgtrdpclp yswispttgi
      421 iisdltmemn rfrligplsh silteaikaa svhtvgedte etphrwwiet ckkpdsvslh
      481 crqeaifell ggitspaeip agtilgltvg dprinlpqkk skalpnpekc qdnekvrqll
      541 legvpvecth sfiwnqdick svtenkisdq dlnrmrsell vpgsqlilgp heskipilli
      601 qqpgkvtged rlgwgsgwdv llpkgwgmaf wipfiyrgvr vgglkesavh sqykrspnvp
      661 gdfpdcpagm lfaeeqaknl lekykrrppa krpnyvklgt lapfccpweq ltqdwesrvq
      721 ayeepsvass pngkesdlrr sevpcapmpk kthqpsdevg tsiehpreae evmdagcqes
      781 agperitdqe asenhvaatg shlcvlrsrk llkqlsawcg pssedsrggr rapgrgqqgl
      841 treaclsilg hfpralvwvs lsllskgspe phtmicvpak edflqlhedw hycgpqeskh
      901 sdpfrskilk qkekkkrekr qkpgrassdg pageepvagq ealtlglwsg plprvtlhcs
      961 rtllgfvtqg dfsmavgcge algfvsltgl ldmlssqpaa qrglvllrpp aslqyrfari
     1021 aiev
//
LOCUS       NP_001030344              25 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein eS32 [Homo sapiens].
ACCESSION   NP_001030344
VERSION     NP_001030344.1
DBSOURCE    REFSEQ: accession NM_001035267.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 25)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 25)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 25)
  AUTHORS   Geng,W., Ren,J., Shi,H., Qin,F., Xu,X., Xiao,S., Jiao,Y. and
            Wang,A.
  TITLE     RPL41 sensitizes retinoblastoma cells to chemotherapeutic drugs via
            ATF4 degradation
  JOURNAL   J Cell Physiol 236 (3), 2214-2225 (2021)
   PUBMED   32783256
  REMARK    GeneRIF: RPL41 sensitizes retinoblastoma cells to chemotherapeutic
            drugs via ATF4 degradation.
REFERENCE   4  (residues 1 to 25)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 25)
  AUTHORS   Yang,G. and Zong,H.
  TITLE     Overexpression of PDZK1IP1, EEF1A2 and RPL41 genes in intrahepatic
            cholangiocarcinoma
  JOURNAL   Mol Med Rep 13 (6), 4786-4790 (2016)
   PUBMED   27082702
  REMARK    GeneRIF: Differential gene expression analysis demonstrated
            significant upregulation of PDZK1IP1, EEF1A2 and RPL41
            (ENSG00000279483) genes in the intrahepatic cholangiocarcinoma
            samples when compared with the matched paratumor samples.
REFERENCE   6  (residues 1 to 25)
  AUTHORS   Go,H., Miyado,K. and Taniguchi,S.
  TITLE     Genomic structure of the human ribosomal protein L41 gene
  JOURNAL   Biochem Mol Biol Int 46 (6), 1227-1231 (1998)
   PUBMED   9891856
REFERENCE   7  (residues 1 to 25)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 25)
  AUTHORS   Lee,J.H., Kim,J.M., Kim,M.S., Lee,Y.T., Marshak,D.R. and Bae,Y.S.
  TITLE     The highly basic ribosomal protein L41 interacts with the beta
            subunit of protein kinase CKII and stimulates phosphorylation of
            DNA topoisomerase IIalpha by CKII
  JOURNAL   Biochem Biophys Res Commun 238 (2), 462-467 (1997)
   PUBMED   9299532
REFERENCE   9  (residues 1 to 25)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 25)
  AUTHORS   Klaudiny,J., von der Kammer,H. and Scheit,K.H.
  TITLE     Characterization by cDNA cloning of the mRNA of a highly basic
            human protein homologous to the yeast ribosomal protein YL41
  JOURNAL   Biochem Biophys Res Commun 187 (2), 901-906 (1992)
   PUBMED   1326959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF673574.1, BC082759.1,
            BC064907.1 and AC034102.32.
            
            Transcript Variant: This variant (2) is the longer transcript,
            containing a unique segment in the 5' UTR, compared to variant 1.
            Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA604697.1, SRR1163658.187316.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000546591.6/ ENSP00000449026.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..25
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..25
                     /product="small ribosomal subunit protein eS32"
                     /note="60S ribosomal protein L41; homologue of yeast
                     ribosomal protein YL41; HG12 protein; large ribosomal
                     subunit protein eL41"
                     /calculated_mol_wt=3325
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62945.1)"
     Region          1..24
                     /region_name="Ribosomal_L41"
                     /note="Ribosomal protein L41; pfam05162"
                     /db_xref="CDD:428342"
     CDS             1..25
                     /gene="RPL41"
                     /gene_synonym="eL41; L41"
                     /coded_by="NM_001035267.2:156..233"
                     /db_xref="CCDS:CCDS44919.1"
                     /db_xref="GeneID:6171"
                     /db_xref="HGNC:HGNC:10354"
                     /db_xref="MIM:613315"
ORIGIN      
        1 mrakwrkkrm rrlkrkrrkm rqrsk
//
LOCUS       NP_001243022             374 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001243022
VERSION     NP_001243022.1
DBSOURCE    REFSEQ: accession NM_001256093.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Zheng,H., Liu,M., Shi,S., Huang,H., Yang,X., Luo,Z., Song,Y.,
            Xu,Q., Li,T., Xue,L., Lu,F. and Wang,J.
  TITLE     MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer
  JOURNAL   Mol Oncol 18 (5), 1327-1346 (2024)
   PUBMED   38383842
  REMARK    GeneRIF: MAP4K4 and WT1 mediate SOX6-induced cellular senescence by
            synergistically activating the ATF2-TGFbeta2-Smad2/3 signaling
            pathway in cervical cancer.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Mi,L., Gao,J., Li,N., Liu,Y., Zhang,N., Gao,Y., Peng,X., Zhang,L.
            and Xu,K.
  TITLE     Human umbilical cord mesenchymal stem cell-derived exosomes loaded
            miR-451a targets ATF2 to improve rheumatoid arthritis
  JOURNAL   Int Immunopharmacol 127, 111365 (2024)
   PUBMED   38104370
  REMARK    GeneRIF: Human umbilical cord mesenchymal stem cell-derived
            exosomes loaded miR-451a targets ATF2 to improve rheumatoid
            arthritis.
            Erratum:[Int Immunopharmacol. 2025 Dec 3;166:115619. doi:
            10.1016/j.intimp.2025.115619. PMID: 41046222]
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Dai,W., Hong,L., Xiao,W., Zhang,L., Sha,W., Yu,Z., Liu,X., Liu,S.,
            Xiao,Y., Yang,P., Peng,Y., Zhang,J., Lin,J., Wu,X., Tang,W.,
            Lin,Z., Xiang,L., Li,J., Pei,M. and Wang,J.
  TITLE     The ATF2/miR-3913-5p/CREB5 axis is involved in the cell
            proliferation and metastasis of colorectal cancer
  JOURNAL   Commun Biol 6 (1), 1026 (2023)
   PUBMED   37816820
  REMARK    GeneRIF: The ATF2/miR-3913-5p/CREB5 axis is involved in the cell
            proliferation and metastasis of colorectal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Meng,H., Li,J., Sun,H., Lin,Y., Xu,H. and Zhang,N.
  TITLE     The transcription factor ATF2 promotes gastric cancer progression
            by activating the METTL3/cyclin D1 pathway
  JOURNAL   Drug Dev Res 84 (6), 1325-1334 (2023)
   PUBMED   37421203
  REMARK    GeneRIF: The transcription factor ATF2 promotes gastric cancer
            progression by activating the METTL3/cyclin D1 pathway.
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Bhoumik,A., Takahashi,S., Breitweiser,W., Shiloh,Y., Jones,N. and
            Ronai,Z.
  TITLE     ATM-dependent phosphorylation of ATF2 is required for the DNA
            damage response
  JOURNAL   Mol Cell 18 (5), 577-587 (2005)
   PUBMED   15916964
  REMARK    GeneRIF: Data demonstrate that the protein kinase ATM
            phosphorylates ATF2 on serines 490 and 498 following ionizing
            radiation (IR).
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Kim,S.J., Wagner,S., Liu,F., O'Reilly,M.A., Robbins,P.D. and
            Green,M.R.
  TITLE     Retinoblastoma gene product activates expression of the human
            TGF-beta 2 gene through transcription factor ATF-2
  JOURNAL   Nature 358 (6384), 331-334 (1992)
   PUBMED   1641004
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Hai,T. and Curran,T.
  TITLE     Cross-family dimerization of transcription factors Fos/Jun and
            ATF/CREB alters DNA binding specificity
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3720-3724 (1991)
   PUBMED   1827203
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Hoeffler,J.P., Lustbader,J.W. and Chen,C.Y.
  TITLE     Identification of multiple nuclear factors that interact with
            cyclic adenosine 3',5'-monophosphate response element-binding
            protein and activating transcription factor-2 by protein-protein
            interactions
  JOURNAL   Mol Endocrinol 5 (2), 256-266 (1991)
   PUBMED   1828107
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Denys,H., Desmet,R., Stragier,M., Vergison,R. and Lemahieu,S.F.
  TITLE     Cystitis emphysematosa
  JOURNAL   Acta Urol Belg 45 (4), 327-331 (1977)
   PUBMED   602896
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA995464.1, DQ003048.1,
            BC107698.1 and BX648469.1.
            
            Summary: This gene encodes a transcription factor that is a member
            of the leucine zipper family of DNA binding proteins. The encoded
            protein has been identified as a moonlighting protein based on its
            ability to perform mechanistically distinct functions This protein
            binds to the cAMP-responsive element (CRE), an octameric
            palindrome. It forms a homodimer or a heterodimer with c-Jun and
            stimulates CRE-dependent transcription. This protein is also a
            histone acetyltransferase (HAT) that specifically acetylates
            histones H2B and H4 in vitro; thus it may represent a class of
            sequence-specific factors that activate transcription by direct
            effects on chromatin components. The encoded protein may also be
            involved in cell's DNA damage response independent of its role in
            transcriptional regulation. Several alternatively spliced
            transcript variants have been found for this gene [provided by
            RefSeq, Jan 2014].
            
            Transcript Variant: This variant (5) lacks an internal exon, and
            uses an alternate acceptor splice site at the 3' terminal exon
            compared to variant 1. This results in translation initiation from
            another start site, and a shorter isoform (4) with distinct N- and
            C- termini compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ003048.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 15916964
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..374
                     /product="cyclic AMP-dependent transcription factor ATF-2
                     isoform 4"
                     /EC_number="2.3.1.48"
                     /note="cAMP responsive element binding protein 2,
                     formerly; cyclic AMP-dependent transcription factor ATF-2;
                     histone acetyltransferase ATF2; cAMP-dependent
                     transcription factor ATF-2; cAMP response element-binding
                     protein CRE-BP1; cyclic AMP-responsive element-binding
                     protein 2"
                     /calculated_mol_wt=40620
     Region          9..44
                     /region_name="GCN4_cent"
                     /note="GCN4 central activation domain-like acidic
                     activation domain; cd12192"
                     /db_xref="CDD:213399"
     Site            order(18..19,21..22,30..31,33..35,37..38,42..44)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:213399"
     Region          <32..284
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          296..356
                     /region_name="bZIP_ATF2"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-2 (ATF-2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14687"
                     /db_xref="CDD:269835"
     Region          296..356
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269835"
     Site            order(297,301,303..305,308,310..312,314..316)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269835"
     Site            order(315,322..323,325..326,329..330,333,336..337,340,
                     343..344,346..347,350..351,354..355)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269835"
     CDS             1..374
                     /gene="ATF2"
                     /gene_synonym="CRE-BP1; CREB-2; CREB2; HB16; TREB7"
                     /coded_by="NM_001256093.2:374..1498"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:1386"
                     /db_xref="HGNC:HGNC:784"
                     /db_xref="MIM:123811"
ORIGIN      
        1 mycawmwpdq tptptrflkn ceevglfnel aspfenefkk aseddikkmp ldlsplatpi
       61 irskieepsv vetthqdspl phpesttsde kevplaqtaq ptsaivrpas lqvpnvllts
      121 sdssviiqqa vpsptsstvi tqapssnrpi vpvpgpfpll lhlpngqtmp vaipasitss
      181 nvhvpaavpl vrpvtmvpsv pgipgpsspq pvqseakmrl kaaltqqhpp vtngdtvkgh
      241 gsglvrtqse esrpqslqqp atsttetpas pahttpqtqs tsgrrrraan edpdekrrkf
      301 lernraaasr crqkrkvwvq slekkaedls slngqlqsev tllrnevaql kqlllahkdc
      361 pvtamqkksg yhrk
//
LOCUS       NP_001306123             820 aa            linear   PRI 20-NOV-2025
DEFINITION  exocyst complex component 6 isoform c [Homo sapiens].
ACCESSION   NP_001306123
VERSION     NP_001306123.1
DBSOURCE    REFSEQ: accession NM_001319194.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Chang,H., Jeung,H.C., Jung,J.J., Kim,T.S., Rha,S.Y. and Chung,H.C.
  TITLE     Identification of genes associated with chemosensitivity to
            SAHA/taxane combination treatment in taxane-resistant breast cancer
            cells
  JOURNAL   Breast Cancer Res Treat 125 (1), 55-63 (2011)
   PUBMED   20224928
REFERENCE   7  (residues 1 to 820)
  AUTHORS   France,Y.E., Boyd,C., Coleman,J. and Novick,P.J.
  TITLE     The polarity-establishment component Bem1p interacts with the
            exocyst complex through the Sec15p subunit
  JOURNAL   J Cell Sci 119 (Pt 5), 876-888 (2006)
   PUBMED   16478783
  REMARK    GeneRIF: The SEC15 protein plays a crucial role in integrating the
            signals between Sec4p and the components of the
            early-polarity-establishment machinery.
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Zhang,X.M., Ellis,S., Sriratana,A., Mitchell,C.A. and Rowe,T.
  TITLE     Sec15 is an effector for the Rab11 GTPase in mammalian cells
  JOURNAL   J Biol Chem 279 (41), 43027-43034 (2004)
   PUBMED   15292201
  REMARK    GeneRIF: Sec15 has a role as an effector for the Rab11 GTPase in
            mammalian cells
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Hsu,S.C., TerBush,D., Abraham,M. and Guo,W.
  TITLE     The exocyst complex in polarized exocytosis
  JOURNAL   Int Rev Cytol 233, 243-265 (2004)
   PUBMED   15037366
  REMARK    Review article
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Brymora,A., Valova,V.A., Larsen,M.R., Roufogalis,B.D. and
            Robinson,P.J.
  TITLE     The brain exocyst complex interacts with RalA in a GTP-dependent
            manner: identification of a novel mammalian Sec3 gene and a second
            Sec15 gene
  JOURNAL   J Biol Chem 276 (32), 29792-29797 (2001)
   PUBMED   11406615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590080.25, AL392103.6,
            AL157705.19 and AL358613.16.
            
            Summary: The protein encoded by this gene is highly similar to the
            Saccharomyces cerevisiae SEC15 gene product, which is essential for
            vesicular traffic from the Golgi apparatus to the cell surface in
            yeast. It is one of the components of a multiprotein complex
            required for exocytosis. The 5' portion of this gene and two
            neighboring cytochrome p450 genes are included in a deletion that
            results in an autosomal-dominant form of nonsyndromic optic nerve
            aplasia (ONA). Alternative splicing and the use of alternative
            promoters results in multiple transcript variants. A paralogous
            gene encoding a similar protein is present on chromosome 2.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300285.1, SRR14038195.309191.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.33"
     Protein         1..820
                     /product="exocyst complex component 6 isoform c"
                     /note="exocyst complex component Sec15A; SEC15-like
                     protein 3; SEC15-like 1; rsec15-like protein"
                     /calculated_mol_wt=95206
     Region          472..778
                     /region_name="Sec15"
                     /note="Exocyst complex subunit Sec15-like; pfam04091"
                     /db_xref="CDD:461169"
     CDS             1..820
                     /gene="EXOC6"
                     /gene_synonym="EXOC6A; SEC15; SEC15L; SEC15L1; SEC15L3;
                     Sec15p"
                     /coded_by="NM_001319194.2:214..2676"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:54536"
                     /db_xref="HGNC:HGNC:23196"
                     /db_xref="MIM:609672"
ORIGIN      
        1 mccvggagsc sdtgklgacr amleeetdqt yenvlaeiqs felpveatlr svyddqpnah
       61 kkfmekldac irnhdkeiek mcnfhhqgfv daitellkvr tdaeklkvqv tdtnrrfqda
      121 gkevivhted iircriqqrn ittvveklql clpvlemysk lkeqmsakry ysalktmeql
      181 envyfpwvsq yrfcqlmien lpklredike ismsdlkdfl esirkhsdki getamkqaqh
      241 qktfsvslqk qnkmkfgknm yinrdripee rnetvlkhsl eeedeneeei ltvqdlvdfs
      301 pvyrclhiys vlgdeetfen yyrkqrkkqa rlvlqpqsnm hetvdgyrry ftqivgffvv
      361 edhilhvtqg lvtraytdel wnmalskiia vlrahssyct dpdlvlelkn ltvifadtlq
      421 gygfpvnrlf dllfeirdqy netllkkwag vfrdifeedn yspipvvnee eykiviskfp
      481 fqdpdlekqs fpkkfpmsqs vphiyiqvke fiyaslkfse slhrssteid dmlrkstnll
      541 ltrtlsscll nlirkphigl telvqiiint thleqackyl edfitnitni sqetvhttrl
      601 yglstfkdar haaegeiytk lnqkidefvq ladydwtmse pdgrasgylm dlinflrsif
      661 qvfthlpgkv aqtacmsacq hlstslmqml ldselkqism gavqqfnldv iqcelfasse
      721 pvpgfqgdtl qlafidlrql ldlfmvwdws tyladygqpa skylrvnpnt altllekmkd
      781 tskknnifaq frkndrdkqk lietvvkqlr slvngmsqhm
//
LOCUS       NP_006263                 92 aa            linear   PRI 20-NOV-2025
DEFINITION  protein S100-B [Homo sapiens].
ACCESSION   NP_006263
VERSION     NP_006263.1
DBSOURCE    REFSEQ: accession NM_006272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Shi,H., Zhang,Y., Yang,Y., Zhang,H., Li,W., Zhong,Z. and Lv,L.
  TITLE     Serum S100B protein and white matter changes in schizophrenia
            before and after medication
  JOURNAL   Brain Res Bull 210, 110927 (2024)
   PUBMED   38485004
  REMARK    GeneRIF: Serum S100B protein and white matter changes in
            schizophrenia before and after medication.
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Yan,A.
  TITLE     Application value of serum S100B combined with glucose metabolism
            indexes in predicting adverse pregnancy outcomes of patients with
            severe preeclampsia
  JOURNAL   J Hum Hypertens 38 (3), 232-237 (2024)
   PUBMED   38160207
  REMARK    GeneRIF: Application value of serum S100B combined with glucose
            metabolism indexes in predicting adverse pregnancy outcomes of
            patients with severe preeclampsia.
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Michetti,F., Di Sante,G., Clementi,M.E., Valeriani,F.,
            Mandarano,M., Ria,F., Di Liddo,R., Rende,M. and Romano Spica,V.
  TITLE     The Multifaceted S100B Protein: A Role in Obesity and Diabetes?
  JOURNAL   Int J Mol Sci 25 (2), 776 (2024)
   PUBMED   38255850
  REMARK    GeneRIF: The Multifaceted S100B Protein: A Role in Obesity and
            Diabetes?
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Yue,P., Zhang,L. and Wang,B.
  TITLE     Effects of interventional vascular embolization at different timing
            on prognosis and serum S100 calcium-binding protein B level of
            patients with aneurysmal subarachnoid hemorrhage
  JOURNAL   Afr Health Sci 23 (3), 561-568 (2023)
   PUBMED   38357151
  REMARK    GeneRIF: Effects of interventional vascular embolization at
            different timing on prognosis and serum S100 calcium-binding
            protein B level of patients with aneurysmal subarachnoid
            hemorrhage.
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Morii,K., Tanaka,R., Takahashi,Y., Minoshima,S., Fukuyama,R.,
            Shimizu,N. and Kuwano,R.
  TITLE     Structure and chromosome assignment of human S100 alpha and beta
            subunit genes
  JOURNAL   Biochem Biophys Res Commun 175 (1), 185-191 (1991)
   PUBMED   1998503
  REMARK    Erratum:[Biochem Biophys Res Commun 1991 Jun 14;177(2):894]
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Allore,R.J., Friend,W.C., O'Hanlon,D., Neilson,K.M., Baumal,R.,
            Dunn,R.J. and Marks,A.
  TITLE     Cloning and expression of the human S100 beta gene
  JOURNAL   J Biol Chem 265 (26), 15537-15543 (1990)
   PUBMED   2394738
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Duncan,A.M., Higgins,J., Dunn,R.J., Allore,R. and Marks,A.
  TITLE     Refined sublocalization of the human gene encoding the beta subunit
            of the S100 protein (S100B) and confirmation of a subtle t(9;21)
            translocation using in situ hybridization
  JOURNAL   Cytogenet Cell Genet 50 (4), 234-235 (1989)
   PUBMED   2530061
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Baudier,J. and Cole,R.D.
  TITLE     Interactions between the microtubule-associated tau proteins and
            S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent
            protein kinase II
  JOURNAL   J Biol Chem 263 (12), 5876-5883 (1988)
   PUBMED   2833519
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Allore,R., O'Hanlon,D., Price,R., Neilson,K., Willard,H.F.,
            Cox,D.R., Marks,A. and Dunn,R.J.
  TITLE     Gene encoding the beta subunit of S100 protein is on chromosome 21:
            implications for Down syndrome
  JOURNAL   Science 239 (4845), 1311-1313 (1988)
   PUBMED   2964086
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA310307.1, BC001766.1,
            EB386131.1 and AP000339.2.
            
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21; however, this gene is
            located at 21q22.3. This protein may function in Neurite extension,
            proliferation of melanoma cells, stimulation of Ca2+ fluxes,
            inhibition of PKC-mediated phosphorylation, astrocytosis and axonal
            proliferation, and inhibition of microtubule assembly. Chromosomal
            rearrangements and altered expression of this gene have been
            implicated in several neurological, neoplastic, and other types of
            diseases, including Alzheimer's disease, Down's syndrome, epilepsy,
            amyotrophic lateral sclerosis, melanoma, and type I diabetes.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.311408.1,
                                           SRR1660807.308821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291700.9/ ENSP00000291700.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..92
                     /product="protein S100-B"
                     /note="S100 calcium-binding protein, beta (neural); S-100
                     calcium-binding protein, beta chain; S-100 protein subunit
                     beta"
                     /calculated_mol_wt=10582
     Region          2..89
                     /region_name="S-100B"
                     /note="S-100B domain found in proteins similar to S100B.
                     S100B is a calcium-binding protein belonging to a large
                     S100 vertebrate-specific protein family within the EF-hand
                     superfamily of calcium-binding proteins. Note that the
                     S-100 hierarchy, to which this...; cd05027"
                     /db_xref="CDD:240154"
     Site            order(2..5,7..19,26,36,39..41,71..72,74..75,78..80,82..83,
                     87..89)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:240154"
     Site            2
                     /site_type="blocked"
                     /note="Blocked amino end (Ser), alternate.
                     /evidence=ECO:0000269|PubMed:4031854; propagated from
                     UniProtKB/Swiss-Prot (P04271.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P02638; propagated from
                     UniProtKB/Swiss-Prot (P04271.2)"
     Site            order(19,22,24,27,32,62,64,66,68,73)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:240154"
     Region          19..32
                     /region_name="Calcium binding region"
     Site            order(43..48,50,52..53,56..57,80..81,84..85,87..88)
                     /site_type="other"
                     /note="NDR kinase binding site [polypeptide binding]"
                     /db_xref="CDD:240154"
     Site            order(47,49,53,56..57,60,72,77,80..81,84..85,87..88)
                     /site_type="active"
                     /note="TRTK-12 binding site [active]"
                     /db_xref="CDD:240154"
     Region          62..73
                     /region_name="Calcium binding region"
     CDS             1..92
                     /gene="S100B"
                     /gene_synonym="NEF; S100; S100-B; S100beta"
                     /coded_by="NM_006272.3:72..350"
                     /db_xref="CCDS:CCDS13736.1"
                     /db_xref="GeneID:6285"
                     /db_xref="HGNC:HGNC:10500"
                     /db_xref="MIM:176990"
ORIGIN      
        1 mselekamva lidvfhqysg regdkhklkk selkelinne lshfleeike qevvdkvmet
       61 ldndgdgecd fqefmafvam vttacheffe he
//
LOCUS       NP_001106177             715 aa            linear   PRI 20-NOV-2025
DEFINITION  scinderin isoform 1 [Homo sapiens].
ACCESSION   NP_001106177
VERSION     NP_001106177.1
DBSOURCE    REFSEQ: accession NM_001112706.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Li,Y., Tang,L., Dang,G., Ma,M. and Tang,X.
  TITLE     Scinderin Promotes Hydrogen Peroxide-induced Lens Epithelial Cell
            Injury in Age-related Cataract
  JOURNAL   Curr Mol Med 24 (11), 1426-1436 (2024)
   PUBMED   37936437
  REMARK    GeneRIF: Scinderin Promotes Hydrogen Peroxide-induced Lens
            Epithelial Cell Injury in Age-related Cataract.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Perez-Castro,L., Venkateswaran,N., Garcia,R., Hao,Y.H.,
            Lafita-Navarro,M.C., Kim,J., Segal,D., Saponzik,E., Chang,B.J.,
            Fiolka,R., Danuser,G., Xu,L., Brabletz,T. and Conacci-Sorrell,M.
  TITLE     The AHR target gene scinderin activates the WNT pathway by
            facilitating the nuclear translocation of beta-catenin
  JOURNAL   J Cell Sci 135 (20) (2022)
   PUBMED   36148682
  REMARK    GeneRIF: The AHR target gene scinderin activates the WNT pathway by
            facilitating the nuclear translocation of beta-catenin.
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Zhang,Z.H., Lian,X.Y., Li,X.X., He,P.F., Lin,J. and Qian,J.
  TITLE     [Clinical Study of SCIN Expression and Dromoter Methylation in
            Patients with Chronic Myeloid Leukemia]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 27 (3), 646-651 (2019)
   PUBMED   31204912
  REMARK    GeneRIF: down-regulation of SCIN expression may relate with the
            progression of chronic myeloid leukemia
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Trifaro,J.M., Rose,S.D. and Marcu,M.G.
  TITLE     Scinderin, a Ca2+-dependent actin filament severing protein that
            controls cortical actin network dynamics during secretion
  JOURNAL   Neurochem Res 25 (1), 133-144 (2000)
   PUBMED   10685613
  REMARK    Review article
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Lueck,A., Brown,D. and Kwiatkowski,D.J.
  TITLE     The actin-binding proteins adseverin and gelsolin are both highly
            expressed but differentially localized in kidney and intestine
  JOURNAL   J Cell Sci 111 (Pt 24), 3633-3643 (1998)
   PUBMED   9819354
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Rodriguez Del Castillo,A., Vitale,M.L. and Trifaro,J.M.
  TITLE     Ca2+ and pH determine the interaction of chromaffin cell scinderin
            with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate
            and its cellular distribution during nicotinic-receptor stimulation
            and protein kinase C activation
  JOURNAL   J Cell Biol 119 (4), 797-810 (1992)
   PUBMED   1331119
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Rodriguez Del Castillo,A., Vitale,M.L., Tchakarov,L. and
            Trifaro,J.M.
  TITLE     Human platelets contain scinderin, a Ca(2+)-dependent actin
            filament-severing protein
  JOURNAL   Thromb Haemost 67 (2), 248-251 (1992)
   PUBMED   1621245
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Rodriguez Del Castillo,A., Lemaire,S., Tchakarov,L.,
            Jeyapragasan,M., Doucet,J.P., Vitale,M.L. and Trifaro,J.M.
  TITLE     Chromaffin cell scinderin, a novel calcium-dependent actin
            filament-severing protein
  JOURNAL   EMBO J 9 (1), 43-52 (1990)
   PUBMED   2153078
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290363.1, BC021090.1, CA447429.1 and AC011891.3.
            
            Summary: SCIN is a Ca(2+)-dependent actin-severing and -capping
            protein (Zunino et al., 2001 [PubMed 11568009]).[supplied by OMIM,
            May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.93047.1,
                                           SRR1660807.32051.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297029.10/ ENSP00000297029.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.3"
     Protein         1..715
                     /product="scinderin isoform 1"
                     /note="adseverin"
                     /calculated_mol_wt=80358
     Region          1..363
                     /region_name="Actin-severing. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6U3.4)"
     Region          10..121
                     /region_name="gelsolin_S1_like"
                     /note="Gelsolin sub-domain 1-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11290"
                     /db_xref="CDD:200446"
     Site            order(27..28,66,72..73,75..77,79..81,83..84,95,97)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200446"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q60604; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6U3.4)"
     Region          136..225
                     /region_name="gelsolin_S2_like"
                     /note="Gelsolin sub-domain 2-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11289"
                     /db_xref="CDD:200445"
     Region          246..346
                     /region_name="gelsolin_S3_like"
                     /note="Gelsolin sub-domain 3-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11292"
                     /db_xref="CDD:200448"
     Site            order(341,346)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:200448"
     Region          364..715
                     /region_name="Ca(2+)-dependent actin binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6U3.4)"
     Region          390..486
                     /region_name="gelsolin_S4_like"
                     /note="Gelsolin sub-domain 4-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11293"
                     /db_xref="CDD:200449"
     Site            order(406..407,441,447..448,450..452,454..456,458..459,
                     470,472)
                     /site_type="other"
                     /note="putative actin binding interface [polypeptide
                     binding]"
                     /db_xref="CDD:200449"
     Site            477
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200449"
     Region          508..598
                     /region_name="gelsolin_S5_like"
                     /note="Gelsolin sub-domain 5-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11288"
                     /db_xref="CDD:200444"
     Site            516
                     /site_type="other"
                     /note="putative nucleotide binding residue [chemical
                     binding]"
                     /db_xref="CDD:200444"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q60604; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6U3.4)"
     Region          613..711
                     /region_name="gelsolin_S6_like"
                     /note="Gelsolin sub-domain 6-like domain found in
                     gelsolin, severin, villin, and related proteins; cd11291"
                     /db_xref="CDD:200447"
     CDS             1..715
                     /gene="SCIN"
                     /coded_by="NM_001112706.3:68..2215"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47545.1"
                     /db_xref="GeneID:85477"
                     /db_xref="HGNC:HGNC:21695"
                     /db_xref="MIM:613416"
ORIGIN      
        1 marelyheef aragkqaglq vwrieklelv pvpqsahgdf yvgdaylvlh taktsrgfty
       61 hlhfwlgkec sqdestaaai ftvqmddylg gkpvqnrelq gyesndfvsy fkgglkykag
      121 gvasglnhvl tndltakrll hvkgrrvvra tevplswdsf nkgdcfiidl gteiyqwcgs
      181 scnkyerlka nqvatgiryn erkgrseliv veegsepsel ikvlgekpel pdggddddii
      241 adisnrkmak lymvsdasgs mrvtvvaeen pfsmamllse ecfildhgaa kqifvwkgkd
      301 anpqerkaam ktaeeflqqm nyskntqiqv lpeggetpif kqffkdwrdk dqsdgfgkvy
      361 vtekvaqikq ipfdasklhs spqmaaqhnm vddgsgkvei wrvenngriq vdqnsygefy
      421 ggdcyiilyt yprgqiiytw qganatrdel ttsafltvql drslggqavq irvsqgkepv
      481 hllslfkdkp liiykngtsk kggqapappt rlfqvrrnla sitrivevdv danslnsndv
      541 fvlklpqnsg yiwvgkgasq eeekgaeyva svlkcktlri qegeepeefw nslggkkdyq
      601 tsplletqae dhpprlygcs nktgrfviee ipgeftqddl aeddvmllda weqifiwigk
      661 danevekkes lksakmylet dpsgrdkrtp iviikqghep ptftgwflgw dsskw
//
LOCUS       NP_001230006             123 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell-specific surface glycoprotein CD28 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001230006
VERSION     NP_001230006.1
DBSOURCE    REFSEQ: accession NM_001243077.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Xiong,Y., Taleb,M., Misawa,K., Hou,Z., Banerjee,S.,
            Amador-Molina,A., Jones,D.R., Chintala,N.K. and Adusumilli,P.S.
  TITLE     c-Kit signaling potentiates CAR T cell efficacy in solid tumors by
            CD28- and IL-2-independent co-stimulation
  JOURNAL   Nat Cancer 4 (7), 1001-1015 (2023)
   PUBMED   37336986
  REMARK    GeneRIF: c-Kit signaling potentiates CAR T cell efficacy in solid
            tumors by CD28- and IL-2-independent co-stimulation.
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Pulanco,M.C., Madsen,A.T., Tanwar,A., Corrigan,D.T. and Zang,X.
  TITLE     Recent advancements in the B7/CD28 immune checkpoint families: new
            biology and clinical therapeutic strategies
  JOURNAL   Cell Mol Immunol 20 (7), 694-713 (2023)
   PUBMED   37069229
  REMARK    GeneRIF: Recent advancements in the B7/CD28 immune checkpoint
            families: new biology and clinical therapeutic strategies.
            Review article
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Mai,H.L., Degauque,N., Lorent,M., Rimbert,M., Renaudin,K.,
            Danger,R., Kerleau,C., Tilly,G., Vivet,A., Le Bot,S., Delbos,F.,
            Walencik,A., Giral,M. and Brouard,S.
  TITLE     Kidney allograft rejection is associated with an imbalance of B
            cells, regulatory T cells and differentiated CD28-CD8+ T cells:
            analysis of a cohort of 1095 graft biopsies
  JOURNAL   Front Immunol 14, 1151127 (2023)
   PUBMED   37168864
  REMARK    GeneRIF: Kidney allograft rejection is associated with an imbalance
            of B cells, regulatory T cells and differentiated CD28-CD8+ T
            cells: analysis of a cohort of 1095 graft biopsies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Gelemanovic,A., Catipovic Ardalic,T., Pribisalic,A., Hayward,C.,
            Kolcic,I. and Polasek,O.
  TITLE     Genome-Wide Meta-Analysis Identifies Multiple Novel Rare Variants
            to Predict Common Human Infectious Diseases Risk
  JOURNAL   Int J Mol Sci 24 (8), 7006 (2023)
   PUBMED   37108169
  REMARK    GeneRIF: Genome-Wide Meta-Analysis Identifies Multiple Novel Rare
            Variants to Predict Common Human Infectious Diseases Risk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Liu,T.H., Lei,J.Y., Mai,Y.G. and Fang,J.P.
  TITLE     [Clinical Analysis of Pediatric Acute Leukemia Complicated with
            Septic Shock]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1708-1714 (2022)
   PUBMED   36476893
  REMARK    GeneRIF: [Clinical Analysis of Pediatric Acute Leukemia Complicated
            with Septic Shock].
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Fraser,J.D., Newton,M.E. and Weiss,A.
  TITLE     CD28 and T cell antigen receptor signal transduction coordinately
            regulate interleukin 2 gene expression in response to superantigen
            stimulation
  JOURNAL   J Exp Med 175 (4), 1131-1134 (1992)
   PUBMED   1313075
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Zocchi,M.R., Poggi,A., Crosti,F., Tongiani,S. and Rugarli,C.
  TITLE     Signalling in human tumour infiltrating lymphocytes: the CD28
            molecule is functional and is physically associated with the CD45R0
            molecule
  JOURNAL   Eur J Cancer 28A (4-5), 749-754 (1992)
   PUBMED   1355979
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Gimmi,C.D., Freeman,G.J., Gribben,J.G., Sugita,K., Freedman,A.S.,
            Morimoto,C. and Nadler,L.M.
  TITLE     B-cell surface antigen B7 provides a costimulatory signal that
            induces T cells to proliferate and secrete interleukin 2
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6575-6579 (1991)
   PUBMED   1650475
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Linsley,P.S., Brady,W., Grosmaire,L., Aruffo,A., Damle,N.K. and
            Ledbetter,J.A.
  TITLE     Binding of the B cell activation antigen B7 to CD28 costimulates T
            cell proliferation and interleukin 2 mRNA accumulation
  JOURNAL   J Exp Med 173 (3), 721-730 (1991)
   PUBMED   1847722
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Lafage-Pochitaloff,M., Costello,R., Couez,D., Simonetti,J.,
            Mannoni,P., Mawas,C. and Olive,D.
  TITLE     Human CD28 and CTLA-4 Ig superfamily genes are located on
            chromosome 2 at bands q33-q34
  JOURNAL   Immunogenetics 31 (3), 198-201 (1990)
   PUBMED   2156778
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125238.5, AF222341.1,
            AK303421.1, J02988.1, DA939711.1, AW241446.1, AA311148.1 and
            BF509568.1.
            
            Summary: The protein encoded by this gene is essential for T-cell
            proliferation and survival, cytokine production, and T-helper
            type-2 development. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (2) uses an alternate, in-frame
            donor splice site at one of the coding exons compared to variant 1.
            This results in a shorter isoform (2) missing an internal protein
            segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR991236.1, AF222341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..123
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 2 precursor"
                     /calculated_mol_wt=12032
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1999
     mat_peptide     19..123
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 2"
                     /calculated_mol_wt=12032
     Region          21..>42
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..123
                     /gene="CD28"
                     /gene_synonym="IMD123; Tp44"
                     /coded_by="NM_001243077.2:59..430"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:940"
                     /db_xref="HGNC:HGNC:1653"
                     /db_xref="MIM:186760"
ORIGIN      
        1 mlrlllalnl fpsiqvtgnk ilvkqspmlv aydnavnlsw khlcpsplfp gpskpfwvlv
       61 vvggvlacys llvtvafiif wvrskrsrll hsdymnmtpr rpgptrkhyq pyapprdfaa
      121 yrs
//
LOCUS       NP_060489                146 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 9 [Homo
            sapiens].
ACCESSION   NP_060489 NP_612436
VERSION     NP_060489.1
DBSOURCE    REFSEQ: accession NM_018019.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Franzese,M., Zanfardino,M., Soricelli,A., Coppola,A., Maiello,C.,
            Salvatore,M., Schiano,C. and Napoli,C.
  TITLE     Familial Dilated Cardiomyopathy: A Novel MED9 Short Isoform
            Identification
  JOURNAL   Int J Mol Sci 25 (5), 3057 (2024)
   PUBMED   38474301
  REMARK    GeneRIF: Familial Dilated Cardiomyopathy: A Novel MED9 Short
            Isoform Identification.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Tsai,K.L., Tomomori-Sato,C., Sato,S., Conaway,R.C., Conaway,J.W.
            and Asturias,F.J.
  TITLE     Subunit architecture and functional modular rearrangements of the
            transcriptional mediator complex
  JOURNAL   Cell 157 (6), 1430-1444 (2014)
   PUBMED   24882805
  REMARK    Erratum:[Cell. 2014 Jul 17;158(2):463]
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Sato,S., Tomomori-Sato,C., Parmely,T.J., Florens,L., Zybailov,B.,
            Swanson,S.K., Banks,C.A., Jin,J., Cai,Y., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     A set of consensus mammalian mediator subunits identified by
            multidimensional protein identification technology
  JOURNAL   Mol Cell 14 (5), 685-691 (2004)
   PUBMED   15175163
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Tomomori-Sato,C., Sato,S., Parmely,T.J., Banks,C.A., Sorokina,I.,
            Florens,L., Zybailov,B., Washburn,M.P., Brower,C.S., Conaway,R.C.
            and Conaway,J.W.
  TITLE     A mammalian mediator subunit that shares properties with
            Saccharomyces cerevisiae mediator subunit Cse2
  JOURNAL   J Biol Chem 279 (7), 5846-5851 (2004)
   PUBMED   14638676
  REMARK    GeneRIF: the FLJ10193 protein, which we designate Med25, is a bona
            fide subunit of the mammalian Mediator complex
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073621.21.
            
            On Nov 4, 2002 this sequence version replaced NP_612436.1.
            
            Summary: The multiprotein Mediator complex is a coactivator
            required for activation of RNA polymerase II transcription by DNA
            bound transcription factors. The protein encoded by this gene is
            thought to be a subunit of the Mediator complex. This gene is
            located within the Smith-Magenis syndrome region on chromosome 17.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000647.2, SRR1803612.23972.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268711.4/ ENSP00000268711.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..146
                     /product="mediator of RNA polymerase II transcription
                     subunit 9"
                     /note="mediator subunit 25; mediator of RNA polymerase II
                     transcription, subunit 9 homolog"
                     /calculated_mol_wt=16272
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWA0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NWA0.1)"
     Region          54..137
                     /region_name="Med9-C"
                     /note="Mediator complex subunit 9 (Med9) C-terminal domain
                     family; cd21431"
                     /db_xref="CDD:467847"
     Site            order(55,58,62,65..66,69,86..87,90,94,105,109..111,
                     113..114,117..118,120..121,123..124,127..128)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467847"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NWA0.1)"
     CDS             1..146
                     /gene="MED9"
                     /gene_synonym="MED25"
                     /coded_by="NM_018019.3:43..483"
                     /db_xref="CCDS:CCDS11184.1"
                     /db_xref="GeneID:55090"
                     /db_xref="HGNC:HGNC:25487"
                     /db_xref="MIM:609878"
ORIGIN      
        1 masagvaagr qaedvlppts dqplpdtkpl pppqpppvpa pqpqqspapr pqspararee
       61 enysflplvh niikcmdkds pevhqdlnal kskfqemrkl istmpgihls peqqqqqlqs
      121 lreqvrtkne llqkykslcm feipke
//
LOCUS       NP_116190                310 aa            linear   PRI 20-NOV-2025
DEFINITION  junctional adhesion molecule C isoform 1 precursor [Homo sapiens].
ACCESSION   NP_116190 NP_113658
VERSION     NP_116190.3
DBSOURCE    REFSEQ: accession NM_032801.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Peng,J., Chen,Y. and Yin,A.
  TITLE     JAM3 promotes cervical cancer metastasis by activating the
            HIF-1alpha/VEGFA pathway
  JOURNAL   BMC Womens Health 24 (1), 293 (2024)
   PUBMED   38760803
  REMARK    GeneRIF: JAM3 promotes cervical cancer metastasis by activating the
            HIF-1alpha/VEGFA pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Shi,Y., Feng,X., Zhang,Y., Gao,J., Bao,W., Wang,J.D. and Bai,J.F.
  TITLE     Downregulation of JAM3 occurs in cholangiocarcinoma by
            hypermethylation: A potential molecular marker for diagnosis and
            prognosis
  JOURNAL   J Cell Mol Med 28 (2), e18038 (2024)
   PUBMED   38124399
  REMARK    GeneRIF: Downregulation of JAM3 occurs in cholangiocarcinoma by
            hypermethylation: A potential molecular marker for diagnosis and
            prognosis.
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Li,X., He,S., Zhao,X., Sun,D., Wu,S., Xu,D. and Li,Y.
  TITLE     High-grade cervical lesions diagnosed by JAM3/PAX1 methylation in
            high-risk human papillomavirus-infected patients
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 48 (12), 1820-1829 (2023)
   PUBMED   38448375
  REMARK    GeneRIF: High-grade cervical lesions diagnosed by JAM3/PAX1
            methylation in high-risk human papillomavirus-infected patients.
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Yang,W., Guo,C., Herman,J.G., Zhu,C., Lv,H., Su,X., Zhang,L.,
            Zhang,M. and Guo,M.
  TITLE     Epigenetic silencing of JAM3 promotes esophageal cancer development
            by activating Wnt signaling
  JOURNAL   Clin Epigenetics 14 (1), 164 (2022)
   PUBMED   36461092
  REMARK    GeneRIF: Epigenetic silencing of JAM3 promotes esophageal cancer
            development by activating Wnt signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Cunningham,S.A., Rodriguez,J.M., Arrate,M.P., Tran,T.M. and
            Brock,T.A.
  TITLE     JAM2 interacts with alpha4beta1. Facilitation by JAM3
  JOURNAL   J Biol Chem 277 (31), 27589-27592 (2002)
   PUBMED   12070135
  REMARK    GeneRIF: Facilitates JAM2 interaction with alpha4beta1
            GeneRIF: Functions as a facilitator for JAM2/alpha4beta1
            interactions
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Phillips,H.M., Renforth,G.L., Spalluto,C., Hearn,T., Curtis,A.R.,
            Craven,L., Havarani,B., Clement-Jones,M., English,C., Stumper,O.,
            Salmon,T., Hutchinson,S., Jackson,M.S. and Wilson,D.I.
  TITLE     Narrowing the critical region within 11q24-qter for hypoplastic
            left heart and identification of a candidate gene, JAM3, expressed
            during cardiogenesis
  JOURNAL   Genomics 79 (4), 475-478 (2002)
   PUBMED   11944976
  REMARK    GeneRIF: JAM3 is a strong candidate gene for hypoplastic left heart
            syndrome
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Liang,T.W., Chiu,H.H., Gurney,A., Sidle,A., Tumas,D.B., Schow,P.,
            Foster,J., Klassen,T., Dennis,K., DeMarco,R.A., Pham,T., Frantz,G.
            and Fong,S.
  TITLE     Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2
            interacts with T, NK, and dendritic cells through JAM 3
  JOURNAL   J Immunol 168 (4), 1618-1626 (2002)
   PUBMED   11823489
  REMARK    GeneRIF: molecular cloning & role as VE-JAM/JAM 2 receptor
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Aurrand-Lions,M., Johnson-Leger,C., Wong,C., Du Pasquier,L. and
            Imhof,B.A.
  TITLE     Heterogeneity of endothelial junctions is reflected by differential
            expression and specific subcellular localization of the three JAM
            family members
  JOURNAL   Blood 98 (13), 3699-3707 (2001)
   PUBMED   11739175
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Arrate,M.P., Rodriguez,J.M., Tran,T.M., Brock,T.A. and
            Cunningham,S.A.
  TITLE     Cloning of human junctional adhesion molecule 3 (JAM3) and its
            identification as the JAM2 counter-receptor
  JOURNAL   J Biol Chem 276 (49), 45826-45832 (2001)
   PUBMED   11590146
  REMARK    GeneRIF: Cloning of human junctional adhesion molecule 3 (JAM3) and
            its identification as the JAM2 counter-receptor.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ416101.1 and AP001775.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2011 this sequence version replaced NP_116190.2.
            
            Summary: Tight junctions represent one mode of cell-to-cell
            adhesion in epithelial or endothelial cell sheets, forming
            continuous seals around cells and serving as a physical barrier to
            prevent solutes and water from passing freely through the
            paracellular space. The protein encoded by this immunoglobulin
            superfamily gene member is localized in the tight junctions between
            high endothelial cells. Unlike other proteins in this family, the
            this protein is unable to adhere to leukocyte cell lines and only
            forms weak homotypic interactions. The encoded protein is a member
            of the junctional adhesion molecule protein family and acts as a
            receptor for another member of this family. A mutation in an intron
            of this gene is associated with hemorrhagic destruction of the
            brain, subependymal calcification, and congenital cataracts.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Apr 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC057284.1, AJ416101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299106.9/ ENSP00000299106.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q25"
     Protein         1..310
                     /product="junctional adhesion molecule C isoform 1
                     precursor"
                     /note="junctional adhesion molecule C"
                     /calculated_mol_wt=31439
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3600
     mat_peptide     32..310
                     /product="Junctional adhesion molecule C.
                     /id=PRO_0000015071"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX67.1)"
                     /calculated_mol_wt=31439
     Region          33..136
                     /region_name="IgV_1_JAM1-like"
                     /note="First Ig-like domain of Junctional adhesion
                     molecule-1 (JAM1)and similar domains; a member of the
                     V-set of IgSF domains; cd20946"
                     /db_xref="CDD:409538"
     Region          33..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          33..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409538"
     Region          40..44
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409538"
     Region          47..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409538"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          63..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409538"
     Region          64..71
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          74..88
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          74..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          82..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          89..118
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409538"
     Region          98..102
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409538"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BX67.1)"
     Region          111..119
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409538"
     Region          119..126
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          126..135
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409538"
     Region          127..136
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409538"
     Region          142..237
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409542"
     Region          170..174
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409542"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q9BX67.1)"
     Region          202..206
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409542"
     Region          216..221
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409542"
     Region          230..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409542"
     Site            242..262
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX67.1)"
     CDS             1..310
                     /gene="JAM3"
                     /gene_synonym="JAM-2; JAM-3; JAM-C; JAMC"
                     /coded_by="NM_032801.5:13..945"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8494.2"
                     /db_xref="GeneID:83700"
                     /db_xref="HGNC:HGNC:15532"
                     /db_xref="MIM:606871"
ORIGIN      
        1 malrrpprlr lcarlpdffl lllfrgclig avnlkssnrt pvvqefesve lsciitdsqt
       61 sdpriewkki qdeqttyvff dnkiqgdlag raeilgktsl kiwnvtrrds alyrcevvar
      121 ndrkeideiv ieltvqvkpv tpvcrvpkav pvgkmatlhc qeseghprph yswyrndvpl
      181 ptdsranprf rnssfhlnse tgtlvftavh kddsgqyyci asndagsarc eeqemevydl
      241 niggiiggvl vvlavlalit lgiccayrrg yfinnkqdge syknpgkpdg vnyirtdeeg
      301 dfrhkssfvi
//
LOCUS       NP_001353137             871 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353137 XP_016861307
VERSION     NP_001353137.1
DBSOURCE    REFSEQ: accession NM_001366208.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861307.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.21818.1,
                                           SRR14038195.797519.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366208.1:227..2842"
                     /note="isoform 8 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_001339880             633 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 21 [Homo sapiens].
ACCESSION   NP_001339880 XP_016868774
VERSION     NP_001339880.1
DBSOURCE    REFSEQ: accession NM_001352951.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 633)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 633)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 633)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 633)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 633)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 633)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 633)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 633)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 633)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 633)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868774.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1861540.1,
                                           SRR14038196.3520793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..633
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..633
                     /product="DNA repair-scaffolding protein isoform 21"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=69263
     Region          <5..119
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          271..600
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..633
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352951.1:581..2482"
                     /note="isoform 21 is encoded by transcript variant 26"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mrscrsfprg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt vkilelheec
       61 amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv rifppwqkli
      121 ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi kgltnnspei
      181 qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga gvrvvvqrvy
      241 slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar qlegkscslv
      301 gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa lcyiltahpn
      361 lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql kslllleqre
      421 iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl ffkdalrdqg
      481 rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq gtvvgvdest
      541 afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr srpqcrvkvk
      601 vgarpehart psslqhseav aaqhflpaev crr
//
LOCUS       NP_001018060             204 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC8 isoform a [Homo
            sapiens].
ACCESSION   NP_001018060
VERSION     NP_001018060.1
DBSOURCE    REFSEQ: accession NM_001018050.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Franca,M.M., Han,X., Funari,M.F.A., Lerario,A.M., Nishi,M.Y.,
            Fontenele,E.G.P., Domenice,S., Jorge,A.A.L., Garcia-Galiano,D.,
            Elias,C.F. and Mendonca,B.B.
  TITLE     Exome Sequencing Reveals the POLR3H Gene as a Novel Cause of
            Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 104 (7), 2827-2841 (2019)
   PUBMED   30830215
  REMARK    GeneRIF: A pathogenic homozygous missense mutation (c.149A>G;
            p.Asp50Gly) in the POLR3H gene in two unrelated families with
            primary ovarian insufficiency was identified.
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Owen,T.J., O'Neil,J.D., Dawson,C.W., Hu,C., Chen,X., Yao,Y.,
            Wood,V.H., Mitchell,L.E., White,R.J., Young,L.S. and Arrand,J.R.
  TITLE     Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase
            III-dependent EBER expression through induction of EBER-associated
            cellular transcription factors
  JOURNAL   Mol Cancer 9, 241 (2010)
   PUBMED   20843307
  REMARK    GeneRIF: Findings reveal that RNA polymerase III-dependent EBER
            expression through induction of cellular transcription factors and
            add to the repertoire of EBNA1's transcription-regulatory
            properties.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Greco-Stewart,V.S., Schissel,E. and Pelchat,M.
  TITLE     The hepatitis delta virus RNA genome interacts with the human RNA
            polymerases I and III
  JOURNAL   Virology 386 (1), 12-15 (2009)
   PUBMED   19246067
  REMARK    GeneRIF: The authors demonstrate the interaction of both RNA
            polymerase I and III with hepatitis delta virus RNA, both in vitro
            and in human cells.
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA449644.1, DA238361.1, AB051452.1, AK000365.1, AL023553.5 and
            BM701572.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1, 3, 5, and 6 encode the same
            isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.243919.1,
                                           SRR1803616.103110.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355209.9/ ENSP00000347345.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..204
                     /product="DNA-directed RNA polymerase III subunit RPC8
                     isoform a"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC8;
                     polymerase (RNA) III subunit H; RNA nucleotidyltransferase
                     (DNA-directed); RNA polymerase III subunit C8;
                     DNA-directed RNA polymerase III subunit H; DNA-directed
                     RNA polymerase III subunit 22.9 kDa polypeptide;
                     polymerase (RNA) III (DNA directed) polypeptide H
                     (22.9kD)"
                     /calculated_mol_wt=22787
     Region          2..81
                     /region_name="RNAP_III_Rpc25_N"
                     /note="Rpc25, N-terminal ribonucleoprotein (RNP) domain.
                     Rpc25 is a subunit of eukaryotic RNA polymerase (RNAP) III
                     and is homologous to Rpa43 of eukaryotic RNAP I, Rpb7 of
                     eukaryotic RNAP II, and RpoE of archaeal RNAP. Rpc25 has
                     two domains, an N-terminal RNP...; cd04330"
                     /db_xref="CDD:239822"
     Site            order(2..6,8,28,31..32,46..49,73,78,80)
                     /site_type="other"
                     /note="Rpc17 interaction site [polypeptide binding]"
                     /db_xref="CDD:239822"
     Region          83..201
                     /region_name="RNA_pol_Rbc25"
                     /note="RNA polymerase III subunit Rpc25; pfam08292"
                     /db_xref="CDD:400543"
     Region          158..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y535.1)"
     CDS             1..204
                     /gene="POLR3H"
                     /gene_synonym="C25; RPC22.9; RPC8"
                     /coded_by="NM_001018050.4:370..984"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14018.1"
                     /db_xref="GeneID:171568"
                     /db_xref="HGNC:HGNC:30349"
                     /db_xref="MIM:619801"
ORIGIN      
        1 mfvlvemvdt vrippwqfer klndsiaeel nkklankvvy nvglciclfd itkledayvf
       61 pgdgashtkv hfrcvvfhpf ldeiligkik gcspegvhvs lgffddilip peslqqpakf
      121 deaeqvwvwe yeteegahdl ymdtgeeirf rvvdesfvdt sptgpssada ttsseelpkk
      181 eapytlvgsi sepglgllsw wtsn
//
LOCUS       NP_078942                315 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha- and gamma-adaptin-binding protein p34 isoform 1 [Homo
            sapiens].
ACCESSION   NP_078942
VERSION     NP_078942.3
DBSOURCE    REFSEQ: accession NM_024666.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Gram,S.B., Jorgensen,A.S.F., Bygum,A., Brusgaard,K. and
            Ousager,L.B.
  TITLE     Identification of a founder variant AAGAB c.370C>T, p.Arg124Ter in
            patients with punctate palmoplantar keratoderma in Southern Denmark
  JOURNAL   Clin Genet 105 (5), 561-566 (2024)
   PUBMED   38311882
  REMARK    GeneRIF: Identification of a founder variant AAGAB c.370C>T,
            p.Arg124Ter in patients with punctate palmoplantar keratoderma in
            Southern Denmark.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Giehl,K.A., Eckstein,G.N., Pasternack,S.M., Praetzel-Wunder,S.,
            Ruzicka,T., Lichtner,P., Seidl,K., Rogers,M., Graf,E., Langbein,L.,
            Braun-Falco,M., Betz,R.C. and Strom,T.M.
  TITLE     Nonsense mutations in AAGAB cause punctate palmoplantar keratoderma
            type Buschke-Fischer-Brauer
  JOURNAL   Am J Hum Genet 91 (4), 754-759 (2012)
   PUBMED   23000146
  REMARK    GeneRIF: Identification of two heterozygous nonsense
            mutations-c.370C>T (p.Arg124) and c.481C>T (p.Arg161)-in AAGAB in
            patients with punctate palmoplantar keratoderma type
            Buschke-Fischer-Brauer.
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Lei,S.F., Papasian,C.J. and Deng,H.W.
  TITLE     Polymorphisms in predicted miRNA binding sites and osteoporosis
  JOURNAL   J Bone Miner Res 26 (1), 72-78 (2011)
   PUBMED   20641033
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Martinez-Mir,A., Zlotogorski,A., Londono,D., Gordon,D., Grunn,A.,
            Uribe,E., Horev,L., Ruiz,I.M., Davalos,N.O., Alayan,O., Liu,J.,
            Gilliam,T.C., Salas-Alanis,J.C. and Christiano,A.M.
  TITLE     Identification of a locus for type I punctate palmoplantar
            keratoderma on chromosome 15q22-q24
  JOURNAL   J Med Genet 40 (12), 872-878 (2003)
   PUBMED   14684683
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Page,L.J., Sowerby,P.J., Lui,W.W. and Robinson,M.S.
  TITLE     Gamma-synergin: an EH domain-containing protein that interacts with
            gamma-adaptin
  JOURNAL   J Cell Biol 146 (5), 993-1004 (1999)
   PUBMED   10477754
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA688370.1, BC047026.1,
            BC035852.1, AL136715.1, CB243401.1, BQ185328.1 and AC012568.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 24, 2007 this sequence version replaced NP_078942.2.
            
            Summary: The protein encoded by this gene interacts with the
            gamma-adaptin and alpha-adaptin subunits of complexes involved in
            clathrin-coated vesicle trafficking. Mutations in this gene are
            associated with type I punctate palmoplantar keratoderma.
            Alternatively spliced transcript variants have been found for this
            gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.163727.1,
                                           SRR1803614.94777.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261880.10/ ENSP00000261880.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..315
                     /product="alpha- and gamma-adaptin-binding protein p34
                     isoform 1"
                     /note="alpha- and gamma-adaptin-binding protein p34;
                     punctate palmoplantar keratoderma type I"
                     /calculated_mol_wt=34463
     Region          155..294
                     /region_name="Adaptin_binding"
                     /note="Alpha and gamma adaptin binding protein p34;
                     pfam10199"
                     /db_xref="CDD:462994"
     Region          197..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PD74.1)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6PD74.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q6PD74.1)"
     CDS             1..315
                     /gene="AAGAB"
                     /gene_synonym="KPPP1; p34; PPKP1; PPKP1A"
                     /coded_by="NM_024666.5:31..978"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42050.1"
                     /db_xref="GeneID:79719"
                     /db_xref="HGNC:HGNC:25662"
                     /db_xref="MIM:614888"
ORIGIN      
        1 maagvpcalv tscssvfsgd qlvqhilgte dlivevtsnd avrfypwtid nkyysadinl
       61 cvvpnkflvt aeiaesvqaf vvyfdstqks gldsvsswlp lakawlpevm ilvcdrvsed
      121 ginrqkaqew cikhgfelve lspeelpeed ddfpestgvk rivqalnanv wsnvvmkndr
      181 nqgfsllnsl tgtnhsigsa dpchpeqphl paadstesls dhrggasntt daqvdsivdp
      241 mldldiqela slttgggdve nferlfsklk emkdkaatlp heqrkvhaek vakafwmaig
      301 gdrdeiegls sdeeh
//
LOCUS       NP_001357497             662 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4A isoform 3 [Homo sapiens].
ACCESSION   NP_001357497 XP_011508178
VERSION     NP_001357497.1
DBSOURCE    REFSEQ: accession NM_001370568.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_011508178.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.283106.1,
                                           SRR1803617.262388.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..662
                     /product="semaphorin-4A isoform 3"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=72720
     Region          1..396
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     Region          397..441
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          467..539
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          477..481
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          489..493
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          508..512
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          522..527
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..662
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001370568.1:309..2297"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 mipwpasdrk ksecafkkks netqcfnfir vlvsynvthl ytcgtfafsp actfielqds
       61 yllpisedkv megkgqspfd pahkhtavlv dgmlysgtmn nflgsepilm rtlgsqpvlk
      121 tdnflrwlhh dasfvaaips tqvvyfffee tasefdffer lhtsrvarvc kndvggekll
      181 qkkwttflka qllctqpgql pfnvirhavl lpadsptaph iyavftsqwq vggtrssavc
      241 afslldierv fkgkykelnk etsrwttyrg petnprpgsc svgpssdkal tfmkdhflmd
      301 eqvvgtpllv ksgveytrla vetaqgldgh shlvmylgtt tgslhkavvs gdssahlvee
      361 iqlfpdpepv rnlqlaptqg avfvgfsggv wrvprancsv yescvdcvla rdphcawdpe
      421 srtccllsap nlnswkqdme rgnpewacas gpmsrslrpq srpqiikevl avpnsilelp
      481 cphlsalasy ywshgpaavp easstvyngs lllivqdgvg glyqcwaten gfsypvisyw
      541 vdsqdqtlal dpelagipre hvkvpltrvs ggaalaaqqs ywphfvtvtv lfalvlsgal
      601 iilvasplra lrargkvqgc etlrpgekap lsreqhlqsp kecrtsasdv dadnnclgte
      661 va
//
LOCUS       NP_001357270             215 aa            linear   PRI 20-NOV-2025
DEFINITION  high mobility group protein B1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357270 XP_024305110
VERSION     NP_001357270.1
DBSOURCE    REFSEQ: accession NM_001370341.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 215)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353648.27.
            
            On May 7, 2019 this sequence version replaced XP_024305110.1.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1080622.1,
                                           SRR14038191.3021020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..215
                     /product="high mobility group protein B1 isoform 1"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=24763
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..163
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156,159,162..163)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          150..183
                     /region_name="Binding to AGER/RAGE.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          161..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          178..184
                     /region_name="Nuclear localization signal (NLS) 2.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            184
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..215
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001370341.1:183..830"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS9335.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekdia ayrakgkpda akkgvvkaek
      181 skkkkeeeed eedeedeeee edeededeee dddde
//
LOCUS       NP_057395                106 aa            linear   PRI 20-NOV-2025
DEFINITION  ATPase inhibitor, mitochondrial isoform 1 precursor [Homo sapiens].
ACCESSION   NP_057395
VERSION     NP_057395.1
DBSOURCE    REFSEQ: accession NM_016311.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Carroll,J., Watt,I.N., Wright,C.J., Ding,S., Fearnley,I.M. and
            Walker,J.E.
  TITLE     The inhibitor protein IF1 from mammalian mitochondria inhibits ATP
            hydrolysis but not ATP synthesis by the ATP synthase complex
  JOURNAL   J Biol Chem 300 (3), 105690 (2024)
   PUBMED   38280428
  REMARK    GeneRIF: The inhibitor protein IF1 from mammalian mitochondria
            inhibits ATP hydrolysis but not ATP synthesis by the ATP synthase
            complex.
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Lengele,L., Rolland,Y., Martinez,L.O., Guyonnet,S., Parini,A.,
            Lucas,A., Vellas,B. and Barreto,P.S.
  CONSRTM   MAPT/DSA Group
  TITLE     Longitudinal Associations Between ATPase Inhibitory Factor 1,
            Growth Differentiation Factor-15, and Nutritional Status in Older
            Adults From the MAPT Study
  JOURNAL   J Gerontol A Biol Sci Med Sci 79 (1) (2024)
   PUBMED   37804244
  REMARK    GeneRIF: Longitudinal Associations Between ATPase Inhibitory Factor
            1, Growth Differentiation Factor-15, and Nutritional Status in
            Older Adults From the MAPT Study.
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Sgarbi,G., Righetti,R., Del Dotto,V., Grillini,S., Giorgio,V.,
            Baracca,A. and Solaini,G.
  TITLE     The pro-oncogenic protein IF1 does not contribute to the Warburg
            effect and is not regulated by PKA in cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (1), 166879 (2024)
   PUBMED   37689158
  REMARK    GeneRIF: The pro-oncogenic protein IF1 does not contribute to the
            Warburg effect and is not regulated by PKA in cancer cells.
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Dominguez-Zorita,S., Romero-Carraminana,I., Santacatterina,F.,
            Esparza-Molto,P.B., Simo,C., Del-Arco,A., Nunez de Arenas,C.,
            Saiz,J., Barbas,C. and Cuezva,J.M.
  TITLE     IF1 ablation prevents ATP synthase oligomerization, enhances
            mitochondrial ATP turnover and promotes an adenosine-mediated
            pro-inflammatory phenotype
  JOURNAL   Cell Death Dis 14 (7), 413 (2023)
   PUBMED   37433784
  REMARK    GeneRIF: IF1 ablation prevents ATP synthase oligomerization,
            enhances mitochondrial ATP turnover and promotes an
            adenosine-mediated pro-inflammatory phenotype.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Burwick,N.R., Wahl,M.L., Fang,J., Zhong,Z., Moser,T.L., Li,B.,
            Capaldi,R.A., Kenan,D.J. and Pizzo,S.V.
  TITLE     An Inhibitor of the F1 subunit of ATP synthase (IF1) modulates the
            activity of angiostatin on the endothelial cell surface
  JOURNAL   J Biol Chem 280 (3), 1740-1745 (2005)
   PUBMED   15528193
REFERENCE   7  (residues 1 to 106)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Aggeler,R., Coons,J., Taylor,S.W., Ghosh,S.S., Garcia,J.J.,
            Capaldi,R.A. and Marusich,M.F.
  TITLE     A functionally active human F1F0 ATPase can be purified by
            immunocapture from heart tissue and fibroblast cell lines. Subunit
            structure and activity studies
  JOURNAL   J Biol Chem 277 (37), 33906-33912 (2002)
   PUBMED   12110673
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Cabezon,E., Runswick,M.J., Leslie,A.G. and Walker,J.E.
  TITLE     The structure of bovine IF(1), the regulatory subunit of
            mitochondrial F-ATPase
  JOURNAL   EMBO J 20 (24), 6990-6996 (2001)
   PUBMED   11742976
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Ichikawa,N., Ushida,S., Kawabata,M. and Masazumi,Y.
  TITLE     Nucleotide sequence of cDNA coding the mitochondrial precursor
            protein of the ATPase inhibitor from humans
  JOURNAL   Biosci Biotechnol Biochem 63 (12), 2225-2227 (1999)
   PUBMED   10664857
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP271519.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI458221.1, BP271519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000335514.10/
                                                  ENSP00000335203.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..106
                     /product="ATPase inhibitor, mitochondrial isoform 1
                     precursor"
                     /note="ATPase inhibitor protein; ATPase inhibitor,
                     mitochondrial; ATP synthase inhibitor protein; IF1; IF(1);
                     inhibitor of F(1)F(o)-ATPase; ATPase inhibitory factor 1;
                     ATP synthase F1 subunit epsilon"
                     /calculated_mol_wt=9517
     transit_peptide 1..25
                     /calculated_mol_wt=2750
     mat_peptide     26..106
                     /product="ATPase inhibitor, mitochondrial isoform 1"
                     /calculated_mol_wt=9517
     Region          26..52
                     /region_name="N-terminal inhibitory region.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII2.1)"
     Region          26..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII2.1)"
     Region          <36..87
                     /region_name="IATP"
                     /note="Mitochondrial ATPase inhibitor, IATP; pfam04568"
                     /db_xref="CDD:428014"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UII2.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UII2.1)"
     Region          74..106
                     /region_name="Antiparallel alpha-helical coiled coil
                     region. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UII2.1)"
     CDS             1..106
                     /gene="ATP5IF1"
                     /gene_synonym="ATPI; ATPIF1; ATPIP; IP"
                     /coded_by="NM_016311.5:61..381"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS319.1"
                     /db_xref="GeneID:93974"
                     /db_xref="HGNC:HGNC:871"
                     /db_xref="MIM:614981"
ORIGIN      
        1 mavtalaart wlgvwgvrtm qargfgsdqs envdrgagsi reaggafgkr eqaeeeryfr
       61 aqsreqlaal kkhheeeivh hkkeierlqk eierhkqkik mlkhdd
//
LOCUS       NP_073752               1460 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFX7 isoform 1 [Homo sapiens].
ACCESSION   NP_073752
VERSION     NP_073752.6
DBSOURCE    REFSEQ: accession NM_022841.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068726.5, AC084783.2 and KF456052.1.
            
            On Jan 10, 2019 this sequence version replaced NP_073752.5.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138518.675153.1,
                                           DRR138518.479905.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000559447.8/ ENSP00000453281.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1460
                     /product="DNA-binding protein RFX7 isoform 1"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=157221
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          43..100
                     /region_name="RFX5_N"
                     /note="RFX5 N-terminal domain; pfam18326"
                     /db_xref="CDD:375753"
     Region          105..183
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          188..193
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and RFXANK. /evidence=ECO:0000269|PubMed:25752541,
                     ECO:0000312|PDB:6MEW"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          <258..568
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          308..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          404..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          468..>745
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          481..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          632..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            704
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          917..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     CDS             1..1460
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_022841.7:438..4820"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92005.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 maeeqqqppp qqpdahqqlp psapnsgval palvpglpgt easalqhkik nsicktvqsk
       61 vdcilqevek ftdleklyly lqlpsglsng eksdqnamss sraqqmhafs wirntleehp
      121 etslpkqevy deyksycdnl gyhplsaadf gkimknvfpn mkarrlgtrg kskycysglr
      181 kkafvhmptl pnldfhktgd glegaepsgq lqnideevis sacrlvcewa qkvlsqpfdt
      241 vlelarflvk shyigtksma altvmaaapa gmkgitqpsa fiptaesnsf qpqvktlpsp
      301 idakqqlqrk iqkkqqeqkl qsplpgesaa kksesatsng vtnlpngnps ilspqpigiv
      361 vaavpspipv qrtrqlvtsp spmsssdgkv lplnvqvvtq hmqsvkqapk tpqnvpaspg
      421 gdrsarhryp qilpkpants altirspttv lftsspikta vvpashmssl nvvkmttisl
      481 tpsnsntplk hsasvssatg tteesrsvpq ikngsvvslq spgsrsssag gtsavevkve
      541 petssdehpv qcqensdeak apqtpsallg qksntdgalq kpsnegviei katkvcdqrt
      601 kcksrcneml pgtstgnnqs titlsvasqn ltftsssspp ngdsinkdpk lctksprkrl
      661 sstlqetqvp pvkkpiveql saatiegqkq gsvkkdqkvp hsgktegsta gaqipskvsv
      721 nvsshiganq plnssalvis dsaleqqttp ssspdikvkl egsvflldsd sksvgsfnpn
      781 gwqqitkdse fisasceqqq disvmtipeh sdindleksv welegmpqdt ysqqlhsqiq
      841 esslnqiqah ssdqlplqse lkefepsvsq tnesyfpfdd eltqdsivee lvlmeqqmsm
      901 nnshsygncl gmtlqsqsvt pgapmsshts sthfyhpihs ngtpihtptp tptptptptp
      961 tptptsemia gsqslsresp csrlaqttpv dsalgssrht pigtphsncs ssvppspvec
     1021 rnpfaftpis ssmayhdasi vssspvkpmq rpmathpdkt klewmnngys gvgnssvsgh
     1081 gilpsyqelv edrfrkphaf avpgqsyqsq srhhdthfgr ltpvspvqhq gatvnntnkq
     1141 egfavpapld nkgtnssass nfrcrsvspa vhrqrnlsgs tlypvsnipr snvtpfgspv
     1201 tpevhvftnv htdacannia qrsqsvpltv mmqtafpnal qkqanskkit nvllskldsd
     1261 nddavrglgm nnlpsnytar mnltqileps tvfpsanpqn midsstsvye fqtpsyltks
     1321 nstgqinfsp gdnqaqseig eqqldfnstv kdllsgdslq tnqqlvgqga sdltntasdf
     1381 ssdirlssel sgsindlntl dpnllfdpgr qqgqddeatl eelkndplfq qicsesmnsm
     1441 tssgfewies kdhptvemlg
//
LOCUS       NP_001164190             868 aa            linear   PRI 20-NOV-2025
DEFINITION  breast cancer anti-estrogen resistance protein 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001164190
VERSION     NP_001164190.1
DBSOURCE    REFSEQ: accession NM_001170719.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Delage,L., Lambert,M., Bardel,E., Kundlacz,C., Chartoire,D.,
            Conchon,A., Peugnet,A.L., Gorka,L., Auberger,P., Jacquel,A.,
            Soussain,C., Destaing,O., Delecluse,H.J., Delecluse,S., Merabet,S.,
            Traverse-Glehen,A., Salles,G., Bachy,E., Billaud,M.,
            Ghesquieres,H., Genestier,L., Rouault,J.P. and Sujobert,P.
  TITLE     BTG1 inactivation drives lymphomagenesis and promotes lymphoma
            dissemination through activation of BCAR1
  JOURNAL   Blood 141 (10), 1209-1220 (2023)
   PUBMED   36375119
  REMARK    GeneRIF: BTG1 inactivation drives lymphomagenesis and promotes
            lymphoma dissemination through activation of BCAR1.
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Li,H., Li,L., Qiu,X., Zhang,J. and Hua,Z.
  TITLE     The interaction of CFLAR with p130Cas promotes cell migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (2), 119390 (2023)
   PUBMED   36400248
  REMARK    GeneRIF: The interaction of CFLAR with p130Cas promotes cell
            migration.
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Camacho Leal Mdel,P., Sciortino,M., Tornillo,G., Colombo,S.,
            Defilippi,P. and Cabodi,S.
  TITLE     p130Cas/BCAR1 scaffold protein in tissue homeostasis and
            pathogenesis
  JOURNAL   Gene 562 (1), 1-7 (2015)
   PUBMED   25727852
  REMARK    GeneRIF: BCAR1 has a pivotal role in the regulation of tissue
            homeostasis in pathological conditions such as cancer. (Review)
            Review article
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Nikonova,A.S., Gaponova,A.V., Kudinov,A.E. and Golemis,E.A.
  TITLE     CAS proteins in health and disease: an update
  JOURNAL   IUBMB Life 66 (6), 387-395 (2014)
   PUBMED   24962474
  REMARK    Review article
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Barrett,A., Pellet-Many,C., Zachary,I.C., Evans,I.M. and Frankel,P.
  TITLE     p130Cas: a key signalling node in health and disease
  JOURNAL   Cell Signal 25 (4), 766-777 (2013)
   PUBMED   23277200
  REMARK    Review article
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Brinkman,A., van der Flier,S., Kok,E.M. and Dorssers,L.C.
  TITLE     BCAR1, a human homologue of the adapter protein p130Cas, and
            antiestrogen resistance in breast cancer cells
  JOURNAL   J Natl Cancer Inst 92 (2), 112-120 (2000)
   PUBMED   10639512
REFERENCE   8  (residues 1 to 868)
  AUTHORS   Vuori,K., Hirai,H., Aizawa,S. and Ruoslahti,E.
  TITLE     Introduction of p130cas signaling complex formation upon
            integrin-mediated cell adhesion: a role for Src family kinases
  JOURNAL   Mol Cell Biol 16 (6), 2606-2613 (1996)
   PUBMED   8649368
REFERENCE   9  (residues 1 to 868)
  AUTHORS   Sakai,R., Iwamatsu,A., Hirano,N., Ogawa,S., Tanaka,T., Mano,H.,
            Yazaki,Y. and Hirai,H.
  TITLE     A novel signaling molecule, p130, forms stable complexes in vivo
            with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
  JOURNAL   EMBO J 13 (16), 3748-3756 (1994)
   PUBMED   8070403
REFERENCE   10 (residues 1 to 868)
  AUTHORS   Dorssers,L.C., van Agthoven,T., Dekker,A., van Agthoven,T.L. and
            Kok,E.M.
  TITLE     Induction of antiestrogen resistance in human breast cancer cells
            by random insertional mutagenesis using defective retroviruses:
            identification of bcar-1, a common integration site
  JOURNAL   Mol Endocrinol 7 (7), 870-878 (1993)
   PUBMED   8413311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC310094.1, AK295809.1,
            AB040024.1, BU730553.1, AC009078.6 and BQ016861.1.
            
            Summary: The protein encoded by this gene is a member of the
            Crk-associated substrate (CAS) family of scaffold proteins,
            characterized by the presence of multiple protein-protein
            interaction domains and many serine and tyrosine phosphorylation
            sites. The encoded protein contains a Src-homology 3 (SH3) domain,
            a proline-rich domain, a substrate domain which contains 15 repeat
            of the YxxP consensus phosphorylation motif for Src family kinases,
            a serine-rich domain, and a bipartite Src-binding domain, which can
            bind both SH2 and SH3 domains. This adaptor protein functions in
            multiple cellular pathways, including in cell motility, apoptosis
            and cell cycle control. Dysregulation of this gene can have a wide
            range of effects, affecting different pathways, including cardiac
            development, vascular smooth muscle cells, liver and kidney
            function, endothelial migration, and cancer. [provided by RefSeq,
            Sep 2017].
            
            Transcript Variant: This variant (7) has an alternate 5' sequence,
            as compared to variant 1. The resulting isoform (7) is shorter and
            has a different N-terminus, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294513.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..868
                     /product="breast cancer anti-estrogen resistance protein 1
                     isoform 7"
                     /note="Cas scaffolding protein family member 1;
                     Crk-associated substrate p130Cas; breast cancer
                     anti-estrogen resistance protein 1; BCAR1, Cas family
                     scaffolding protein; BCAR1, Cas family scaffold protein"
                     /calculated_mol_wt=93006
     Region          3..69
                     /region_name="SH3_BCAR1"
                     /note="Src homology 3 domain of the CAS (Crk-Associated
                     Substrate) scaffolding protein family member, Breast
                     Cancer Anti-estrogen Resistance 1; cd12001"
                     /db_xref="CDD:212934"
     Site            order(10,12,15,19,40..41,54,56..57)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212934"
     Region          <89..481
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          452..608
                     /region_name="Serine_rich_CAS"
                     /note="Serine rich Four helix bundle domain of CAS
                     (Crk-Associated Substrate) scaffolding proteins; a protein
                     interaction module; cl07433"
                     /db_xref="CDD:471673"
     Region          652..862
                     /region_name="CAS_C"
                     /note="Crk-Associated Substrate C-terminal domain;
                     pfam12026"
                     /db_xref="CDD:463437"
     CDS             1..868
                     /gene="BCAR1"
                     /gene_synonym="CAS; CAS1; CASS1; CRKAS; P130Cas"
                     /coded_by="NM_001170719.3:93..2699"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS54037.1"
                     /db_xref="GeneID:9564"
                     /db_xref="HGNC:HGNC:971"
                     /db_xref="MIM:602941"
ORIGIN      
        1 menvlakaly dnvaespdel sfrkgdimtv leqdtqgldg wwlcslhgrq givpgnrlki
       61 lvgmydkkpa gpgpgppatp aqpqpglhap appasqytpm lpntyqpqpd svylvptpsk
      121 aqqglyqvpg pspqfqsppa kqtstfskqt phhpfpspat dlyqvppgpg gpaqdiyqvp
      181 psagmghdiy qvppsmdtrs wegtkppakv vvptrvgqgy vyeaaqpeqd eydiprhlla
      241 pgpqdiydvp pvrgllpsqy gqevydtppm avkgpngrdp llevydvpps vekglppsnh
      301 havydvppsv skdvpdgpll reetydvppa fakakpfdpa rtplvlaapp pdsppaedvy
      361 dvpppapdly dvppglrrpg pgtlydvpre rvlppevadg gvvdsgvyav pppaereapa
      421 egkrlsasst gstrssqsas slevagpgre plelevavea larlqqgvsa tvahlldlag
      481 sagatgswrs psepqeplvq dlqaavaavq savhellefa rsavgnaaht sdralhakls
      541 rqlqkmedvh qtlvahgqal dagrggsgat ledldrlvac sravpedakq lasflhgnas
      601 llfrrtkata pgpegggtlh pnptdktssi qsrplpsppk ftsqdspdgq yenseggwme
      661 dydyvhlqgk eefektqkel lekgsitrqg ksqlelqqlk qferleqevs rpidhdlanw
      721 tpaqplapgr tgglgpsdrq lllfyleqce anlttltnav dafftavatn qppkifvahs
      781 kfvilsahkl vfigdtlsrq akaadvrsqv thysnllcdl lrgivattka aalqypspsa
      841 aqdmvervke lghstqqfrr vlgqlaaa
//
LOCUS       NP_001229410             165 aa            linear   PRI 20-NOV-2025
DEFINITION  probable RNA-binding protein EIF1AD [Homo sapiens].
ACCESSION   NP_001229410
VERSION     NP_001229410.1
DBSOURCE    REFSEQ: accession NM_001242481.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Yu,J. and Marintchev,A.
  TITLE     Comparative sequence and structure analysis of eIF1A and eIF1AD
  JOURNAL   BMC Struct Biol 18 (1), 11 (2018)
   PUBMED   30180896
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Smirnova,E.V., Rakitina,T.V., Bogatova,O.V., Ivanova,D.L.,
            Vorobyeva,E.E., Lipkin,A.V., Kostanyan,I.A. and Lipkin,V.M.
  TITLE     Novel protein haponin regulates cellular response to oxidative
            stress
  JOURNAL   Dokl Biochem Biophys 440, 225-227 (2011)
   PUBMED   22095125
  REMARK    GeneRIF: Novel protein haponin regulates cellular response to
            oxidative stress.
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Vonarshenko,A.V., Radchenko,V.V., Gapon,M.V., Rodionov,I.L.,
            Babichenko,I.I., Kakuev,D.L., Artamonov,I.D., Garkovenko,A.V.,
            D'iachkova,L.G., Lipkin,V.M. and Kostanian,I.A.
  TITLE     [Identification and expression of haponin, a new protein from HL-60
            cells]
  JOURNAL   Bioorg Khim 33 (6), 653-656 (2007)
   PUBMED   18173130
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP328412.1, BE791453.1, AI831454.1, BE669813.1 and AP006287.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.178571.1,
                                           SRR1660803.45698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000533544.6/ ENSP00000434056.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..165
                     /product="probable RNA-binding protein EIF1AD"
                     /note="eukaryotic translation initiation factor 1A
                     domain-containing protein"
                     /calculated_mol_wt=18922
     Region          6..12
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          25..102
                     /region_name="S1_eIF1AD_like"
                     /note="eukaryotic translation initiation factor 1A domain
                     containing protein (eIF1AD)-like, S1-like RNA-binding
                     domain. eIF1AD is also known as MGC11102 protein. Little
                     is known about the function of eIF1AD. S1-like RNA-binding
                     domains are found in a wide...; cd05792"
                     /db_xref="CDD:240218"
     Site            order(33..34,38,52..55,58,63)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240218"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          56..65
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          112..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     CDS             1..165
                     /gene="EIF1AD"
                     /gene_synonym="haponin; OBELIX"
                     /coded_by="NM_001242481.2:365..862"
                     /db_xref="CCDS:CCDS8124.1"
                     /db_xref="GeneID:84285"
                     /db_xref="HGNC:HGNC:28147"
                     /db_xref="MIM:618473"
ORIGIN      
        1 msqatkrkhv vkevlgehiv psdqqqivrv lrtpgnnlhe vetaqgqrfl vsmpskyrkn
       61 iwikrgdfli vdpieegekv kaeisfvlck dhvrslqkeg fwpeafseva ekhnnrnrqt
      121 qpelpaepql sgeesssedd sdlfvntnrr qyheseeese eeeaa
//
LOCUS       NP_036376                535 aa            linear   PRI 20-NOV-2025
DEFINITION  large neutral amino acids transporter small subunit 2 isoform a
            [Homo sapiens].
ACCESSION   NP_036376
VERSION     NP_036376.2
DBSOURCE    REFSEQ: accession NM_012244.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Crocco,P., Dato,S., La Grotta,R., Passarino,G. and Rose,G.
  TITLE     Evidence for a relationship between genetic polymorphisms of the
            L-DOPA transporter LAT2/4F2hc and risk of hypertension in the
            context of chronic kidney disease
  JOURNAL   BMC Med Genomics 17 (1), 163 (2024)
   PUBMED   38890684
  REMARK    GeneRIF: Evidence for a relationship between genetic polymorphisms
            of the L-DOPA transporter LAT2/4F2hc and risk of hypertension in
            the context of chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Wang,F.M., Xu,L.Q., Zhang,Z.C., Guo,Q., Du,Z.P., Lei,Y., Han,X.,
            Wu,C.Y., Zhao,F. and Chen,J.L.
  TITLE     SLC7A8 overexpression inhibits the growth and metastasis of lung
            adenocarcinoma and is correlated with a dismal prognosis
  JOURNAL   Aging (Albany NY) 16 (2), 1605-1619 (2024)
   PUBMED   38244585
  REMARK    GeneRIF: SLC7A8 overexpression inhibits the growth and metastasis
            of lung adenocarcinoma and is correlated with a dismal prognosis.
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Meng,F., Wang,L., Gao,G., Chen,J., Wang,X., Wu,G. and Miu,Y.
  TITLE     Identification and verification of microRNA signature and key genes
            in the development of osteosarcoma with lung metastasis
  JOURNAL   Medicine (Baltimore) 101 (49), e32258 (2022)
   PUBMED   36626488
  REMARK    GeneRIF: Identification and verification of microRNA signature and
            key genes in the development of osteosarcoma with lung metastasis.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Min,Q., Wang,Y., Wu,Q., Li,X., Teng,H., Fan,J., Cao,Y., Fan,P. and
            Zhan,Q.
  TITLE     Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma
  JOURNAL   JCI Insight 6 (17), e150203 (2021)
   PUBMED   34494553
  REMARK    GeneRIF: Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Yan,R., Li,Y., Muller,J., Zhang,Y., Singer,S., Xia,L., Zhong,X.,
            Gertsch,J., Altmann,K.H. and Zhou,Q.
  TITLE     Mechanism of substrate transport and inhibition of the human
            LAT1-4F2hc amino acid transporter
  JOURNAL   Cell Discov 7 (1), 16 (2021)
   PUBMED   33758168
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Broer,A., Friedrich,B., Wagner,C.A., Fillon,S., Ganapathy,V.,
            Lang,F. and Broer,S.
  TITLE     Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2
            requires different domains
  JOURNAL   Biochem J 355 (Pt 3), 725-731 (2001)
   PUBMED   11311135
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Rossier,G., Meier,C., Bauch,C., Summa,V., Sordat,B., Verrey,F. and
            Kuhn,L.C.
  TITLE     LAT2, a new basolateral 4F2hc/CD98-associated amino acid
            transporter of kidney and intestine
  JOURNAL   J Biol Chem 274 (49), 34948-34954 (1999)
   PUBMED   10574970
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Bassi,M.T., Sperandeo,M.P., Incerti,B., Bulfone,A., Pepe,A.,
            Surace,E.M., Gattuso,C., De Grandi,A., Buoninconti,A., Riboni,M.,
            Manzoni,M., Andria,G., Ballabio,A., Borsani,G. and Sebastio,G.
  TITLE     SLC7A8, a gene mapping within the lysinuric protein intolerance
            critical region, encodes a new member of the
            glycoprotein-associated amino acid transporter family
  JOURNAL   Genomics 62 (2), 297-303 (1999)
   PUBMED   10610726
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Pineda,M., Fernandez,E., Torrents,D., Estevez,R., Lopez,C.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  TITLE     Identification of a membrane protein, LAT-2, that Co-expresses with
            4F2 heavy chain, an L-type amino acid transport activity with broad
            specificity for small and large zwitterionic amino acids
  JOURNAL   J Biol Chem 274 (28), 19738-19744 (1999)
   PUBMED   10391915
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Borsani,G., Bassi,M.T., Sperandeo,M.P., De Grandi,A.,
            Buoninconti,A., Riboni,M., Manzoni,M., Incerti,B., Pepe,A.,
            Andria,G., Ballabio,A. and Sebastio,G.
  TITLE     SLC7A7, encoding a putative permease-related protein, is mutated in
            patients with lysinuric protein intolerance
  JOURNAL   Nat Genet 21 (3), 297-301 (1999)
   PUBMED   10080183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK223610.1, AL365343.2, AK313465.1, BX248288.1, AB037669.1 and
            AF135830.1.
            
            On Jul 28, 2003 this sequence version replaced NP_036376.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y18483.1, AK223610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316902.12/ ENSP00000320378.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..535
                     /product="large neutral amino acids transporter small
                     subunit 2 isoform a"
                     /note="solute carrier family 7 (amino acid transporter,
                     L-type), member 8; solute carrier family 7 (cationic amino
                     acid transporter, y+ system), member 8; large neutral
                     amino acids transporter small subunit 2; integral membrane
                     protein E16H; L-type amino acid transporter 2; solute
                     carrier family 7 (amino acid transporter light chain, L
                     system), member 8"
                     /calculated_mol_wt=58251
     Region          1..497
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXW9; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            74..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            117..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            134
                     /site_type="other"
                     /note="Important for substrate specificity.
                     /evidence=ECO:0000269|PubMed:34848541; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            182..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            231..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            246
                     /site_type="other"
                     /note="Important for substrate specificity.
                     /evidence=ECO:0000269|PubMed:34848541; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            266..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            313..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            365..382
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            387..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            424..446
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Site            447..466
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     Region          502..535
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI5.1)"
     CDS             1..535
                     /gene="SLC7A8"
                     /gene_synonym="LAT2; LPI-PC1"
                     /coded_by="NM_012244.4:747..2354"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9590.1"
                     /db_xref="GeneID:23428"
                     /db_xref="HGNC:HGNC:11066"
                     /db_xref="MIM:604235"
ORIGIN      
        1 meegarhrnn tekkhpggge sdaspeagsg gggvalkkei glvsacgiiv gniigsgifv
       61 spkgvlenag svglalivwi vtgfitvvga lcyaelgvti pksggdysyv kdifgglagf
      121 lrlwiavlvi yptnqavial tfsnyvlqpl fptcfppesg lrllaaicll lltwvncssv
      181 rwatrvqdif tagkllalal iiimgivqic kgeyfwlepk nafenfqepd iglvalaflq
      241 gsfayggwnf lnyvteelvd pyknlpraif isiplvtfvy vfanvayvta mspqellasn
      301 avavtfgekl lgvmawimpi svalstfggv ngslftssrl ffagareghl psvlamihvk
      361 rctpipallf tcistllmlv tsdmytliny vgfinylfyg vtvagqivlr wkkpdiprpi
      421 kinllfpiiy llfwafllvf slwsepvvcg iglaimltgv pvyflgvywq hkpkcfsdfi
      481 elltlvsqkm cvvvypever gsgteeaned meeqqqpmyq ptptkdkdva gqpqp
//
LOCUS       NP_001265645             621 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 4 [Homo sapiens].
ACCESSION   NP_001265645
VERSION     NP_001265645.1
DBSOURCE    REFSEQ: accession NM_001278716.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Nguyen-Dien,G.T., Townsend,B., Kulkarni,P.G., Kozul,K.L., Ooi,S.S.,
            Eldershaw,D.N., Weeratunga,S., Liu,M., Jones,M.J., Millard,S.S.,
            Ng,D.C., Pagano,M., Bonfim-Melo,A., Schneider,T., Komander,D.,
            Lazarou,M., Collins,B.M. and Pagan,J.K.
  TITLE     PPTC7 antagonizes mitophagy by promoting BNIP3 and NIX degradation
            via SCFFBXL4
  JOURNAL   EMBO Rep 25 (8), 3324-3347 (2024)
   PUBMED   38992176
  REMARK    GeneRIF: PPTC7 antagonizes mitophagy by promoting BNIP3 and NIX
            degradation via SCF[FBXL4].
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Kulkarni,P., Nguyen-Dien,G.T., Kozul,K.L. and Pagan,J.K.
  TITLE     FBXL4: safeguarding against mitochondrial depletion through
            suppression of mitophagy
  JOURNAL   Autophagy 20 (6), 1459-1461 (2024)
   PUBMED   38423516
  REMARK    GeneRIF: FBXL4: safeguarding against mitochondrial depletion
            through suppression of mitophagy.
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Gao,K., Chen,Y., Mo,R. and Wang,C.
  TITLE     Excessive BNIP3- and BNIP3L-dependent mitophagy underlies the
            pathogenesis of FBXL4-mutated mitochondrial DNA depletion syndrome
  JOURNAL   Autophagy 20 (2), 460-462 (2024)
   PUBMED   37876279
  REMARK    GeneRIF: Excessive BNIP3- and BNIP3L-dependent mitophagy underlies
            the pathogenesis of FBXL4-mutated mitochondrial DNA depletion
            syndrome.
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Nguyen-Dien,G.T., Kozul,K.L., Cui,Y., Townsend,B., Kulkarni,P.G.,
            Ooi,S.S., Marzio,A., Carrodus,N., Zuryn,S., Pagano,M., Parton,R.G.,
            Lazarou,M., Millard,S.S., Taylor,R.W., Collins,B.M., Jones,M.J. and
            Pagan,J.K.
  TITLE     FBXL4 suppresses mitophagy by restricting the accumulation of NIX
            and BNIP3 mitophagy receptors
  JOURNAL   EMBO J 42 (13), e112767 (2023)
   PUBMED   37161784
  REMARK    GeneRIF: FBXL4 suppresses mitophagy by restricting the accumulation
            of NIX and BNIP3 mitophagy receptors.
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Kipreos,E.T. and Pagano,M.
  TITLE     The F-box protein family
  JOURNAL   Genome Biol 1 (5), REVIEWS3002 (2000)
   PUBMED   11178263
  REMARK    Review article
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Almannai,M., Dai,H., El-Hattab,A.W. and Wong,L.J.C.
  TITLE     FBXL4-Related Encephalomyopathic Mitochondrial DNA Depletion
            Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28383868
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA782779.1, DA391493.1,
            BC091484.1 and AL022395.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the F-box protein family,
            which are characterized by an approximately 40 amino acid motif,
            the F-box. F-box proteins constitute one subunit of modular E3
            ubiquitin ligase complexes, called SCF complexes, which function in
            phosphorylation-dependent ubiquitination. The F-box domain mediates
            protein-protein interactions and binds directly to S-phase
            kinase-associated protein 1. In addition to an F-box domain, the
            encoded protein contains at least 9 tandem leucine-rich repeats.
            The ubiquitin ligase complex containing the encoded protein may
            function in cell-cycle control by regulating levels of
            lysine-specific demethylase 4A. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1050775.1,
                                           SRR1803616.61138.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369244.7/ ENSP00000358247.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1-q16.2"
     Protein         1..621
                     /product="F-box/LRR-repeat protein 4"
                     /calculated_mol_wt=69966
     Site            28
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BH70; propagated from
                     UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          280..326
                     /region_name="F-box_FBXL4"
                     /note="F-box domain found in F-box/LRR-repeat protein 4
                     (FBXL4) and similar proteins; cd22117"
                     /db_xref="CDD:438889"
     Site            order(283,287,290..291,294..295,299,301..302,306..308,310)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438889"
     Region          295..317
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          318..346
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          347..376
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          376..397
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          377..398
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          394..601
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          402..421
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          403..427
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          427..448
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          428..452
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          452..474
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          453..480
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          480..501
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          481..506
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          504..524
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          507..534
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          532..558
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          535..560
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          559..583
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          561..586
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          584..609
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKA2.2)"
     Region          587..612
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..621
                     /gene="FBXL4"
                     /gene_synonym="FBL4; FBL5; MTDPS13"
                     /coded_by="NM_001278716.2:450..2315"
                     /db_xref="CCDS:CCDS5041.1"
                     /db_xref="GeneID:26235"
                     /db_xref="HGNC:HGNC:13601"
                     /db_xref="MIM:605654"
ORIGIN      
        1 mspvfpmltv ltmfyyiclr rrartatrge mmnthraies nsqtsplnae vvqyakevvd
       61 fsshygsens msytmwnlag vpnvfpssgd ftqtavfrty gtwwdqcpsa slpfkrtppn
      121 fqsqdyvelt feqqvyptav hvletyhpga virilacsan pyspnppaev rweilwserp
      181 tkvnasqarq fkpcikqinf ptnlirlevn sslleyytel davvlhgvkd kpvlslktsl
      241 idmndiedda yaekdgcgmd slnkkfssav lgegpnngyf dklpyeliql ilnhltlpdl
      301 crlaqtckll sqhccdplqy ihlnlqpywa klddtslefl qsrctlvqwl nlswtgnrgf
      361 isvagfsrfl kvcgselvrl elscshflne tclevisemc pnlqalnlss cdklppqafn
      421 hiaklcslkr lvlyrtkveq tallsilnfc selqhlslgs cvmiedydvi asmigakckk
      481 lrtldlwrck nitengiael asgcplleel dlgwcptlqs stgcftrlah qlpnlqklfl
      541 tanrsvcdtd idelacnctr lqqldilgtr mvspaslrkl lesckdlsll dvsfcsqidn
      601 ravlelnasf pkvfikksft q
//
LOCUS       NP_001307970             479 aa            linear   PRI 20-NOV-2025
DEFINITION  ammonium transporter Rh type C [Homo sapiens].
ACCESSION   NP_001307970 XP_011519965
VERSION     NP_001307970.1
DBSOURCE    REFSEQ: accession NM_001321041.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,Q., Liu,J., Yao,D., Shi,J.X., Liu,Y.J., Wei,Y.G. and Guo,S.
  TITLE     Comprehensive Analysis to Identify Rh Family C Glycoprotein (RHCG)
            as the Causative Gene for Psoriasis and Search for Alternative
            Treatment Modalities
  JOURNAL   Drug Des Devel Ther 17, 2593-2611 (2023)
   PUBMED   37664450
  REMARK    GeneRIF: Comprehensive Analysis to Identify Rh Family C
            Glycoprotein (RHCG) as the Causative Gene for Psoriasis and Search
            for Alternative Treatment Modalities.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Chen,P., Liu,C., Li,P., Wang,Q., Gao,X., Wu,H. and Huang,J.
  TITLE     High RhCG expression predicts poor survival and promotes migration
            and proliferation of gastric cancer via keeping intracellular
            alkaline
  JOURNAL   Exp Cell Res 386 (2), 111740 (2020)
   PUBMED   31756312
  REMARK    GeneRIF: High RhCG level was correlated with poor prognosis of
            gastric cancer patients.
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Verlander,J.W., Miller,R.T., Frank,A.E., Royaux,I.E., Kim,Y.H. and
            Weiner,I.D.
  TITLE     Localization of the ammonium transporter proteins RhBG and RhCG in
            mouse kidney
  JOURNAL   Am J Physiol Renal Physiol 284 (2), F323-F337 (2003)
   PUBMED   12388412
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Chen,B.S., Xu,Z.X., Xu,X., Cai,Y., Han,Y.L., Wang,J., Xia,S.H.,
            Hu,H., Wei,F., Wu,M. and Wang,M.R.
  TITLE     RhCG is downregulated in oesophageal squamous cell carcinomas, but
            expressed in multiple squamous epithelia
  JOURNAL   Eur J Cancer 38 (14), 1927-1936 (2002)
   PUBMED   12204676
  REMARK    Erratum:[Eur J Cancer. 2003 Feb;39(3):405.]
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Marini,A.M., Matassi,G., Raynal,V., Andre,B., Cartron,J.P. and
            Cherif-Zahar,B.
  TITLE     The human Rhesus-associated RhAG protein and a kidney homologue
            promote ammonium transport in yeast
  JOURNAL   Nat Genet 26 (3), 341-344 (2000)
   PUBMED   11062476
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Liu,Z., Chen,Y., Mo,R., Hui,C., Cheng,J.F., Mohandas,N. and
            Huang,C.H.
  TITLE     Characterization of human RhCG and mouse Rhcg as novel nonerythroid
            Rh glycoprotein homologues predominantly expressed in kidney and
            testis
  JOURNAL   J Biol Chem 275 (33), 25641-25651 (2000)
   PUBMED   10852913
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Ridgwell,K., Spurr,N.K., Laguda,B., MacGeoch,C., Avent,N.D. and
            Tanner,M.J.
  TITLE     Isolation of cDNA clones for a 50 kDa glycoprotein of the human
            erythrocyte membrane associated with Rh (rhesus) blood-group
            antigen expression
  JOURNAL   Biochem J 287 (Pt 1) (Pt 1), 223-228 (1992)
   PUBMED   1417776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK313238.1 and BC015461.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011519965.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279852.602.1, ERR279831.4205.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2156670 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..479
                     /product="ammonium transporter Rh type C"
                     /note="Rh type C glycoprotein; Rhesus blood group, C
                     glycoprotein; rh glycoprotein kidney; tumor-related
                     protein DRC2; rh family type C glycoprotein; rhesus blood
                     group family type C glycoprotein"
                     /calculated_mol_wt=53048
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20457942; propagated from
                     UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Region          60..435
                     /region_name="Ammonium_transp"
                     /note="Ammonium Transporter Family; cl03012"
                     /db_xref="CDD:445985"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            124..144
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            178..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            346..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     Site            395..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBD6.1)"
     CDS             1..479
                     /gene="RHCG"
                     /gene_synonym="C15orf6; PDRC2; RHGK; SLC42A3"
                     /coded_by="NM_001321041.2:40..1479"
                     /db_xref="CCDS:CCDS10351.1"
                     /db_xref="GeneID:51458"
                     /db_xref="HGNC:HGNC:18140"
                     /db_xref="MIM:605381"
ORIGIN      
        1 mawntnlrwr lpltclllqv imvilfgvfv rydfeadahw wserthknls dmenefyyry
       61 psfqdvhvmv fvgfgflmtf lqrygfsavg fnfllaafgi qwallmqgwf hflqdryivv
      121 gvenlinadf cvasvcvafg avlgkvspiq llimtffqvt lfavnefill nllkvkdagg
      181 smtihtfgay fgltvtrily rrnleqsker qnsvyqsdlf amigtlflwm ywpsfnsais
      241 yhgdsqhraa intycslaac vltsvaissa lhkkgkldmv hiqnatlagg vavgtaaemm
      301 lmpygaliig fvcgiistlg fvyltpfles rlhiqdtcgi nnlhgipgii ggivgavtaa
      361 saslevygke glvhsfdfqg fngdwtartq gkfqiygllv tlamalmggi ivglilrlpf
      421 wgqpsdencf edavywempe gnstvyiped ptfkpsgpsv psvpmvsplp massvplvp
//
LOCUS       NP_055487                583 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial ribonuclease P catalytic subunit isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_055487 XP_375074
VERSION     NP_055487.2
DBSOURCE    REFSEQ: accession NM_014672.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Zhang,E., Sun,Q., Zhang,C., Ma,H., Zhang,J., Ding,Y., Wang,G.,
            Jin,C., Jin,C., Fu,Y., Yan,C., Zhu,M., Wang,C., Dai,J., Jin,G.,
            Hu,Z., Shen,H. and Ma,H.
  TITLE     Comprehensive functional interrogation of susceptibility loci in
            GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC
  JOURNAL   Cancer Lett 585, 216646 (2024)
   PUBMED   38262497
  REMARK    GeneRIF: Comprehensive functional interrogation of susceptibility
            loci in GWASs identified KIAA0391 as a novel oncogenic driver via
            regulating pyroptosis in NSCLC.
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Smith,T.B., Rea,A., Thomas,H.B., Thompson,K., Olahova,M.,
            Maroofian,R., Zamani,M., He,L., Sadeghian,S., Galehdari,H.,
            Lotan,N.S., Gilboa,T., Herman,K.C., McCorvie,T.J., Yue,W.W.,
            Houlden,H., Taylor,R.W., Newman,W.G. and O'Keefe,R.T.
  TITLE     Novel homozygous variants in PRORP expand the genotypic spectrum of
            combined oxidative phosphorylation deficiency 54
  JOURNAL   Eur J Hum Genet 31 (10), 1190-1194 (2023)
   PUBMED   37558808
  REMARK    GeneRIF: Novel homozygous variants in PRORP expand the genotypic
            spectrum of combined oxidative phosphorylation deficiency 54.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Hochberg,I., Demain,L.A.M., Richer,J., Thompson,K., Urquhart,J.E.,
            Rea,A., Pagarkar,W., Rodriguez-Palmero,A., Schluter,A., Verdura,E.,
            Pujol,A., Quijada-Fraile,P., Amberger,A., Deutschmann,A.J.,
            Demetz,S., Gillespie,M., Belyantseva,I.A., McMillan,H.J.,
            Barzik,M., Beaman,G.M., Motha,R., Ng,K.Y., O'Sullivan,J.,
            Williams,S.G., Bhaskar,S.S., Lawrence,I.R., Jenkinson,E.M.,
            Zambonin,J.L., Blumenfeld,Z., Yalonetsky,S., Oerum,S.,
            Rossmanith,W., Yue,W.W., Zschocke,J., Munro,K.J., Battersby,B.J.,
            Friedman,T.B., Taylor,R.W., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics England Research Consortium
  TITLE     Bi-allelic variants in the mitochondrial RNase P subunit PRORP
            cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations
  JOURNAL   Am J Hum Genet 108 (11), 2195-2204 (2021)
   PUBMED   34715011
  REMARK    GeneRIF: Bi-allelic variants in the mitochondrial RNase P subunit
            PRORP cause mitochondrial tRNA processing defects and pleiotropic
            multisystem presentations.
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Bhatta,A., Dienemann,C., Cramer,P. and Hillen,H.S.
  TITLE     Structural basis of RNA processing by human mitochondrial RNase P
  JOURNAL   Nat Struct Mol Biol 28 (9), 713-723 (2021)
   PUBMED   34489609
  REMARK    GeneRIF: Structural basis of RNA processing by human mitochondrial
            RNase P.
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Alsmadi,O., Muiya,P., Khalak,H., Al-Saud,H., Meyer,B.F.,
            Al-Mohanna,F., Alshahid,M. and Dzimiri,N.
  TITLE     Haplotypes encompassing the KIAA0391 and PSMA6 gene cluster confer
            a genetic link for myocardial infarction and coronary artery
            disease
  JOURNAL   Ann Hum Genet 73 (Pt 5), 475-483 (2009)
   PUBMED   19624571
  REMARK    GeneRIF: Haplotypes in KIAA0391 and PSMA6 genes is a genetic link
            for myocardial infarction and coronary artery disease.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Holzmann,J., Frank,P., Loffler,E., Bennett,K.L., Gerner,C. and
            Rossmanith,W.
  TITLE     RNase P without RNA: identification and functional reconstitution
            of the human mitochondrial tRNA processing enzyme
  JOURNAL   Cell 135 (3), 462-474 (2008)
   PUBMED   18984158
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Anantharaman,V. and Aravind,L.
  TITLE     The NYN domains: novel predicted RNAses with a PIN domain-like fold
  JOURNAL   RNA Biol 3 (1), 18-27 (2006)
   PUBMED   17114934
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Li,T., Faridi,R., Newman,W.G. and Friedman,T.B.
  TITLE     Perrault Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25254289
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA459368.1, BX161394.1, AA838769.1 and AL121594.6.
            
            On or before May 1, 2005 this sequence version replaced
            XP_375074.1, NP_055487.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1 and 6 both encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.119171.1,
                                           SRR1803612.144679.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000534898.9/ ENSP00000440915.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..583
                     /product="mitochondrial ribonuclease P catalytic subunit
                     isoform 1 precursor"
                     /EC_number="3.1.26.5"
                     /note="mitochondrial ribonuclease P protein 3;
                     mitochondrial RNase P protein 3; mitochondrial RNase P
                     subunit 3; proteinaceous RNase P; mitochondrial
                     ribonuclease P catalytic subunit"
                     /calculated_mol_wt=62099
     transit_peptide 1..45
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O15091.2)"
                     /calculated_mol_wt=5235
     mat_peptide     46..583
                     /product="Mitochondrial ribonuclease P catalytic subunit.
                     /id=PRO_0000050749"
                     /note="propagated from UniProtKB/Swiss-Prot (O15091.2)"
                     /calculated_mol_wt=62099
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15091.2)"
     Region          174..204
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          210..239
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          244..271
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     Region          342..578
                     /region_name="PRORP"
                     /note="Protein-only RNase P; pfam16953"
                     /db_xref="CDD:465320"
     CDS             1..583
                     /gene="PRORP"
                     /gene_synonym="COXPD54; KIAA0391; MRPP3"
                     /coded_by="NM_014672.4:379..2130"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32063.1"
                     /db_xref="GeneID:9692"
                     /db_xref="HGNC:HGNC:19958"
                     /db_xref="MIM:609947"
ORIGIN      
        1 mtfylfgirs fpklwkspyl glgpghsyvs lfladrcgir nqqrlfslkt mspqntkatn
       61 liakarylrk degsnkqvys vphfflagaa kersqmnsqt edhalapvrn tiqlptqpln
      121 seewdklked lkentgktsf eswiisqmag chssidvaks llawvaaknn givsydllvk
      181 ylylcvfhmq tsevidvfei mkaryktlep rgysllirgl ihsdrwreal llledikkvi
      241 tpskknyndc iqgallhqdv ntawnlyqel lghdivpmle tlkaffdfgk dikddnysnk
      301 lldilsylrn nqlypgesfa hsiktwfesv pgkqwkgqft tvrksgqcsg cgktiesiql
      361 speeyeclkg kimrdvidgg dqyrkttpqe lkrfenfiks rppfdvvidg lnvakmfpkv
      421 resqlllnvv sqlakrnlrl lvlgrkhmlr rssqwsrdem eevqkqascf faddiseddp
      481 fllyatlhsg nhcrfitrdl mrdhkaclpd aktqrlffkw qqghqlaivn rfpgskltfq
      541 rilsydtvvq ttgdswhipy dedlvercsc evptkwlclh qkt
//
LOCUS       NP_542161                305 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein with serine-rich domain 1 isoform a [Homo
            sapiens].
ACCESSION   NP_542161
VERSION     NP_542161.1
DBSOURCE    REFSEQ: accession NM_080594.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kumari,S., Adhikary,A. and Singh,K.K.
  TITLE     BioID proximity mapping reveals novel SAP18 interactions in the
            prespliceosomal complex
  JOURNAL   Biochem Biophys Res Commun 738, 150944 (2024)
   PUBMED   39522233
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Wang,X., Ling,R., Peng,Y., Qiu,W. and Chen,D.
  TITLE     RNPS1 stabilizes NAT10 protein to facilitate translation in cancer
            via tRNA ac4C modification
  JOURNAL   Int J Oral Sci 16 (1), 6 (2024)
   PUBMED   38246918
  REMARK    GeneRIF: RNPS1 stabilizes NAT10 protein to facilitate translation
            in cancer via tRNA ac[4]C modification.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Deka,B., Chandra,P., Yadav,P., Rehman,A., Kumari,S.,
            Kunnumakkara,A.B. and Singh,K.K.
  TITLE     RNPS1 functions as an oncogenic splicing factor in cervical cancer
            cells
  JOURNAL   IUBMB Life 75 (6), 514-529 (2023)
   PUBMED   36300671
  REMARK    GeneRIF: RNPS1 functions as an oncogenic splicing factor in
            cervical cancer cells.
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Mayeda,A., Badolato,J., Kobayashi,R., Zhang,M.Q., Gardiner,E.M. and
            Krainer,A.R.
  TITLE     Purification and characterization of human RNPS1: a general
            activator of pre-mRNA splicing
  JOURNAL   EMBO J 18 (16), 4560-4570 (1999)
   PUBMED   10449421
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Loyer,P., Trembley,J.H., Lahti,J.M. and Kidd,V.J.
  TITLE     The RNP protein, RNPS1, associates with specific isoforms of the
            p34cdc2-related PITSLRE protein kinase in vivo
  JOURNAL   J Cell Sci 111 (Pt 11), 1495-1506 (1998)
   PUBMED   9580558
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Burn,T.C., Connors,T.D., Van Raay,T.J., Dackowski,W.R.,
            Millholland,J.M., Klinger,K.W. and Landes,G.M.
  TITLE     Generation of a transcriptional map for a 700-kb region surrounding
            the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis
            type 2 (TSC2) disease genes on human chromosome 16p3.3
  JOURNAL   Genome Res 6 (6), 525-537 (1996)
   PUBMED   8828041
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Badolato,J., Gardiner,E., Morrison,N. and Eisman,J.
  TITLE     Identification and characterisation of a novel human RNA-binding
            protein
  JOURNAL   Gene 166 (2), 323-327 (1995)
   PUBMED   8543184
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA818573.1, BQ059026.1 and
            BC108316.1.
            
            Summary: This gene encodes a protein that is part of a
            post-splicing multiprotein complex involved in both mRNA nuclear
            export and mRNA surveillance. mRNA surveillance detects exported
            mRNAs with truncated open reading frames and initiates
            nonsense-mediated mRNA decay (NMD). When translation ends upstream
            from the last exon-exon junction, this triggers NMD to degrade
            mRNAs containing premature stop codons. This protein binds to the
            mRNA and remains bound after nuclear export, acting as a
            nucleocytoplasmic shuttling protein. This protein contains many
            serine residues. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2013].
            
            Transcript Variant: This variant (2) represents the predominant
            transcript and encodes the longest isoform (a). Variants 1, 2, and
            3 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.109776.1,
                                           SRR3476690.38899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320225.10/ ENSP00000315859.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..305
                     /product="RNA-binding protein with serine-rich domain 1
                     isoform a"
                     /note="SR protein; RNA-binding protein S1, serine-rich
                     domain; SR-related protein LDC2; RNA binding protein with
                     serine-rich domain"
                     /calculated_mol_wt=34077
     Region          1..220
                     /region_name="Necessary for interaction with the cleaved
                     p110 isoform of CDC2L1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          1..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          1..161
                     /region_name="Necessary for interaction with SRP54,
                     nuclear localization and exon-skipping.
                     /evidence=ECO:0000269|PubMed:14729963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:15684395; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          69..121
                     /region_name="Necessary for interactions with UPF2 and
                     UPF3B and UPF2-dependent NMD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          156..242
                     /region_name="Necessary for interaction with PNN and
                     exon-skipping"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          159..244
                     /region_name="Interaction with SAP18 and ACIN1.
                     /evidence=ECO:0000269|PubMed:20966198"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          163..236
                     /region_name="RRM_RNPS1"
                     /note="RNA recognition motif (RRM) found in RNA-binding
                     protein with serine-rich domain 1 (RNPS1) and similar
                     proteins; cd12365"
                     /db_xref="CDD:409800"
     Site            order(169..173,175..176,179..180,183..184,195,200..201,
                     221..231)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409800"
     Site            218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          238..305
                     /region_name="Necessary for interaction with TRA2B,
                     nuclear localization and exon-skipping.
                     /evidence=ECO:0000269|PubMed:14729963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          240..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     CDS             1..305
                     /gene="RNPS1"
                     /gene_synonym="E5.1"
                     /coded_by="NM_080594.4:190..1107"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10465.1"
                     /db_xref="GeneID:10921"
                     /db_xref="HGNC:HGNC:10080"
                     /db_xref="MIM:606447"
ORIGIN      
        1 mdlsgvkkks llgvkennkk sstrapsptk rkdrsdeksk drskdkgatk essekdrgrd
       61 ktrkrrsass gssstrsrss stsssgssts tgsssgssss sassrsgsss tsrsssssss
      121 sgspspsrrr hdnrrrsrsk skppkrdeke rkrrspspkp tkvhigrltr nvtkdhimei
      181 fstygkikmi dmpvermhph lskgyayvef enpdeaekal khmdggqidg qeitatavla
      241 pwprppprrf spprrmlppp pmwrrspprm rrrsrsprrr spvrrrsrsp grrrhrsrss
      301 snssr
//
LOCUS       NP_001341305            1030 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-tubulin complex component 5 isoform g [Homo sapiens].
ACCESSION   NP_001341305 XP_016877381
VERSION     NP_001341305.1
DBSOURCE    REFSEQ: accession NM_001354376.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1030)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 1030)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1030)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 1030)
  AUTHORS   Izumi,N., Fumoto,K., Izumi,S. and Kikuchi,A.
  TITLE     GSK-3beta regulates proper mitotic spindle formation in cooperation
            with a component of the gamma-tubulin ring complex, GCP5
  JOURNAL   J Biol Chem 283 (19), 12981-12991 (2008)
   PUBMED   18316369
  REMARK    GeneRIF: GSK-3beta regulates the localization of gamma-tubulin ring
            complex, including GCP5, to the spindle poles, thereby controlling
            the formation of proper mitotic spindles
REFERENCE   5  (residues 1 to 1030)
  AUTHORS   Bittel,D.C., Kibiryeva,N. and Butler,M.G.
  TITLE     Expression of 4 genes between chromosome 15 breakpoints 1 and 2 and
            behavioral outcomes in Prader-Willi syndrome
  JOURNAL   Pediatrics 118 (4), e1276-e1283 (2006)
   PUBMED   16982806
  REMARK    GeneRIF: quantitated mRNA levels of NIPA2, NIPA2,l CYFIP1, and GCP5
            in Prader-Willi syndrome and correlated levels with psychological
            and behavior scales
REFERENCE   6  (residues 1 to 1030)
  AUTHORS   Chai,J.H., Locke,D.P., Greally,J.M., Knoll,J.H., Ohta,T., Dunai,J.,
            Yavor,A., Eichler,E.E. and Nicholls,R.D.
  TITLE     Identification of four highly conserved genes between breakpoint
            hotspots BP1 and BP2 of the Prader-Willi/Angelman syndromes
            deletion region that have undergone evolutionary transposition
            mediated by flanking duplicons
  JOURNAL   Am J Hum Genet 73 (4), 898-925 (2003)
   PUBMED   14508708
  REMARK    GeneRIF: located in the genomic domain between break points 1 and 2
            on chromosome 15, of the Prader-Willi/Angelman syndromes
REFERENCE   7  (residues 1 to 1030)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 1030)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   9  (residues 1 to 1030)
  AUTHORS   Murphy,S.M., Preble,A.M., Patel,U.K., O'Connell,K.L., Dias,D.P.,
            Moritz,M., Agard,D., Stults,J.T. and Stearns,T.
  TITLE     GCP5 and GCP6: two new members of the human gamma-tubulin complex
  JOURNAL   Mol Biol Cell 12 (11), 3340-3352 (2001)
   PUBMED   11694571
REFERENCE   10 (residues 1 to 1030)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116166.6 and AC090764.35.
            
            On Aug 29, 2017 this sequence version replaced XP_016877381.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.145746.1,
                                           SRR1803615.247317.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1030
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q11.2"
     Protein         1..1030
                     /product="gamma-tubulin complex component 5 isoform g"
                     /note="gamma-tubulin complex component GCP5; gamma-tubulin
                     complex component 5; tubulin gamma complex associated
                     protein 5"
                     /calculated_mol_wt=118882
     Region          15..108
                     /region_name="GCP5_NTD"
                     /note="N-terminal domain of gamma-tubulin complex
                     component 5 (GCP-5) and similar proteins; cd22572"
                     /db_xref="CDD:439339"
     Region          155..203
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT8.1)"
     Region          271..577
                     /region_name="GCP_N_terminal"
                     /note="Gamma tubulin complex component N-terminal;
                     pfam17681"
                     /db_xref="CDD:465456"
     Region          521..545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT8.1)"
     Region          716..999
                     /region_name="GCP_C_terminal"
                     /note="Gamma tubulin complex component C-terminal;
                     pfam04130"
                     /db_xref="CDD:461187"
     CDS             1..1030
                     /gene="TUBGCP5"
                     /gene_synonym="GCP5"
                     /coded_by="NM_001354376.2:27..3119"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="GeneID:114791"
                     /db_xref="HGNC:HGNC:18600"
                     /db_xref="MIM:608147"
ORIGIN      
        1 marhgppwsr ldaqqerdvr elvrgvaglq deadpnfqla lnfawsnfrf hrfldvnshk
       61 iektiegiye kfvihsdlsk aaswkrltee flnaplpsik eiktdahysi lslllclsds
      121 psnssyvetp rnkevekkdd fdwgkylmed eemdigpymd tpnwseesee endqqplsre
      181 dsgiqvdrtp leeqdqnrkl dpciswkdep ddrswlehhv vhqywtarps qfphslhlhs
      241 nlaavwdqhl yssdplyvpd drvlvtetqv iretlwllsg vkklfifqli dgkvtvrnni
      301 ivthlthscl rsvleqiaay gqvvfrlqef idevmghsse smlpgsgsvp kksteapfrt
      361 yqafmwalyk yfisfkeela eiekciinnd ttitlaivvd klaprlsqlk vlhkvfstgv
      421 aevppdtrnv vrashllntl ykaileydnv geaseqtvsl lfslwvetvr pylqtvdewi
      481 vhghlwdgar efiiqrnknv pvnhrdfwya tytlysvsek teneekmsdn asassgsdqg
      541 pssrqhtmvs flkpvlkqii magksmqllk nlqcaesttc qagardaerk slytlflesv
      601 qsrlrhgeds tpqvlteqqa tkenlmkmqs iaeshleldd vhdpllainf armyleqsdf
      661 hekfaggdvc vdrssesvtc qtfeltlrsc lyphidkqyl dccgnlmqtl kkdyrlveyl
      721 qamrnfflme ggdtmydfyt sifdkireke twqnvsflnv qlqeavgqry pedssrlsis
      781 fenvdtakkk lpvhildglt lsykvpwpvd ivislecqki ynqvfllllq ikwakysldv
      841 llfgelvsta ekprlkegli heqdtvaqfg pqkepvrqqi hrmfllrvkl mhfvnslhny
      901 imtrilhstg lefqhqveea kdldqlikih yrylstihdr cllrekvsfv keaimkvlnl
      961 almfadgwqa glgtwrmesi ekmesdfknc hmflvtilnk avcrgsfphw lpvvcirrws
     1021 llstgglggt
//
LOCUS       NP_803876                337 aa            linear   PRI 20-NOV-2025
DEFINITION  ras association domain-containing protein 6 isoform a [Homo
            sapiens].
ACCESSION   NP_803876
VERSION     NP_803876.1
DBSOURCE    REFSEQ: accession NM_177532.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Kuleape,J.A., Hossain,S., Sinclear,C.K., Shimizu,T., Iwasa,H.,
            Maruyama,J., Arimoto-Matsuzaki,K., Nishina,H. and Hata,Y.
  TITLE     DNA Damage Triggers the Nuclear Accumulation of RASSF6 Tumor
            Suppressor Protein via CDK9 and BAF53 To Regulate p53 Target Gene
            Transcription
  JOURNAL   Mol Cell Biol 42 (2), e0031021 (2022)
   PUBMED   34898277
  REMARK    GeneRIF: DNA Damage Triggers the Nuclear Accumulation of RASSF6
            Tumor Suppressor Protein via CDK9 and BAF53 To Regulate p53 Target
            Gene Transcription.
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Zhou,W., Liu,Y. and Wu,X.
  TITLE     Down-regulation of circITCH promotes osteosarcoma development and
            resistance to doxorubicin via the miR-524/RASSF6 axis
  JOURNAL   J Gene Med 23 (10), e3373 (2021)
   PUBMED   34151476
  REMARK    GeneRIF: Down-regulation of circITCH promotes osteosarcoma
            development and resistance to doxorubicin via the miR-524/RASSF6
            axis.
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Bozdogan,O., Guresci,S., Ocalan,D. and Bozdogan,N.
  TITLE     Kindlin-3 and RASSF6 are probable biomarkers for predicting
            metastasis in cutaneous melanoma
  JOURNAL   Pol J Pathol 72 (3), 237-244 (2021)
   PUBMED   35048636
  REMARK    GeneRIF: Kindlin-3 and RASSF6 are probable biomarkers for
            predicting metastasis in cutaneous melanoma.
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Hesson,L.B., Dunwell,T.L., Cooper,W.N., Catchpoole,D., Brini,A.T.,
            Chiaramonte,R., Griffiths,M., Chalmers,A.D., Maher,E.R. and
            Latif,F.
  TITLE     The novel RASSF6 and RASSF10 candidate tumour suppressor genes are
            frequently epigenetically inactivated in childhood leukaemias
  JOURNAL   Mol Cancer 8, 42 (2009)
   PUBMED   19570220
  REMARK    GeneRIF: Sequencing revealed RASSF6 and RASSF10 were the only RASSF
            members with a high frequency of leukaemia-specific methylation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Hillian,A.D., Londono,D., Dunn,J.M., Goddard,K.A., Pace,R.G.,
            Knowles,M.R. and Drumm,M.L.
  CONSRTM   CF Gene Modifier Study Group
  TITLE     Modulation of cystic fibrosis lung disease by variants in
            interleukin-8
  JOURNAL   Genes Immun 9 (6), 501-508 (2008)
   PUBMED   18563170
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Allen,N.P., Donninger,H., Vos,M.D., Eckfeld,K., Hesson,L.,
            Gordon,L., Birrer,M.J., Latif,F. and Clark,G.J.
  TITLE     RASSF6 is a novel member of the RASSF family of tumor suppressors
  JOURNAL   Oncogene 26 (42), 6203-6211 (2007)
   PUBMED   17404571
  REMARK    GeneRIF: Demonstrates properties of a Ras effector and tumor
            suppressor but exhibits biological properties that are unique and
            distinct from those of other family members.
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Ikeda,M., Hirabayashi,S., Fujiwara,N., Mori,H., Kawata,A., Iida,J.,
            Bao,Y., Sato,Y., Iida,T., Sugimura,H. and Hata,Y.
  TITLE     Ras-association domain family protein 6 induces apoptosis via both
            caspase-dependent and caspase-independent pathways
  JOURNAL   Exp Cell Res 313 (7), 1484-1495 (2007)
   PUBMED   17367779
  REMARK    GeneRIF: These findings indicate that RASSF6 is implicated in
            apoptosis in HeLa cells and that it triggers both caspase-dependent
            and caspase-independent pathways.
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Hull,J., Rowlands,K., Lockhart,E., Sharland,M., Moore,C.,
            Hanchard,N. and Kwiatkowski,D.P.
  TITLE     Haplotype mapping of the bronchiolitis susceptibility locus near
            IL8
  JOURNAL   Hum Genet 114 (3), 272-279 (2004)
   PUBMED   14605870
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074250.6.
            
            Summary: This gene encodes a member of the Ras-association domain
            family (RASSF). Members of this family form the core of a highly
            conserved tumor suppressor network, the Salvador-Warts-Hippo (SWH)
            pathway. The protein encoded by this gene is a Ras effector protein
            that induces apoptosis. A genomic region containing this gene has
            been linked to susceptibility to viral bronchiolitis. Alternative
            splicing results in multiple transcript variants and protein
            isoforms. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. It encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749283.1, AY217664.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307439.10/ ENSP00000303877.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..337
                     /product="ras association domain-containing protein 6
                     isoform a"
                     /note="Ras association (RalGDS/AF-6) domain family 6;
                     putative RAS binding protein; ras association
                     domain-containing protein 6; Ras association (RalGDS/AF-6)
                     domain family member 6"
                     /calculated_mol_wt=39673
     Region          187..273
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Region          283..328
                     /region_name="SARAH_RASSF6"
                     /note="C-terminal SARAH domain found in Ras-association
                     domain-containing protein 6 (RASSF6); cd21895"
                     /db_xref="CDD:439189"
     Site            order(284..285,287,289,292,296,299..300,302..303,306..307,
                     310..311,313..314,317..318,321,324..325)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:439189"
     CDS             1..337
                     /gene="RASSF6"
                     /coded_by="NM_177532.5:184..1197"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3559.1"
                     /db_xref="GeneID:166824"
                     /db_xref="HGNC:HGNC:20796"
                     /db_xref="MIM:612620"
ORIGIN      
        1 mtmmahqyps wifinektfi treqlnsllk tynifyenqk nlhilygete dgklivegml
       61 difwgvkrpi qlkiqdekpf ssftsmkssd vfsskgmtrw gefddlyris eldrtqipms
      121 ekrnsqedyl syhsntlkph akdepdspvl yrtmseaalv rkrmkplmmd rkerqknras
      181 inghfynhet sifipafese tkvrvnsnmr teevikqllq kfkienspqd falhiifatg
      241 eqrrlkktdi pllqrllqgp seknariflm dkdaeeissd vaqyinfhfs llesilqrln
      301 eeekreiqri vtkfnkekai ilkclqnklv iktettv
//
LOCUS       NP_689866                201 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 E2 isoform 1 [Homo sapiens].
ACCESSION   NP_689866
VERSION     NP_689866.1
DBSOURCE    REFSEQ: accession NM_152653.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Hong,X., Ma,N., Li,D., Zhang,M., Dong,W., Huang,J., Ci,X. and
            Zhang,S.
  TITLE     UBE2E2 enhances Snail-mediated epithelial-mesenchymal transition
            and Nrf2-mediated antioxidant activity in ovarian cancer
  JOURNAL   Cell Death Dis 14 (2), 100 (2023)
   PUBMED   36765041
  REMARK    GeneRIF: UBE2E2 enhances Snail-mediated epithelial-mesenchymal
            transition and Nrf2-mediated antioxidant activity in ovarian
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Pringa,E., Martinez-Noel,G., Muller,U. and Harbers,K.
  TITLE     Interaction of the ring finger-related U-box motif of a nuclear dot
            protein with ubiquitin-conjugating enzymes
  JOURNAL   J Biol Chem 276 (22), 19617-19623 (2001)
   PUBMED   11274149
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Moynihan,T.P., Ardley,H.C., Nuber,U., Rose,S.A., Jones,P.F.,
            Markham,A.F., Scheffner,M. and Robinson,P.A.
  TITLE     The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with
            RING finger/IBR motif-containing domains of HHARI and H7-AP1
  JOURNAL   J Biol Chem 274 (43), 30963-30968 (1999)
   PUBMED   10521492
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Kimura,M., Hattori,T., Matsuda,Y., Yoshioka,T., Sumi,N., Umeda,Y.,
            Nakashima,S. and Okano,Y.
  TITLE     cDNA cloning, characterization, and chromosome mapping of UBE2E2
            encoding a human ubiquitin-conjugating E2 enzyme
  JOURNAL   Cytogenet Cell Genet 78 (2), 107-111 (1997)
   PUBMED   9371400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK057886.1, BC022332.1, CB851345.1 and AC116992.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.220419.1,
                                           SRR1803612.17213.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396703.6/ ENSP00000379931.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..201
                     /product="ubiquitin-conjugating enzyme E2 E2 isoform 1"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-conjugating enzyme E2E 2 (homologous to
                     yeast UBC4/5); ubiquitin-conjugating enzyme E2E 2 (UBC4/5
                     homolog, yeast); ubiquitin-protein ligase E2; ubiquitin
                     carrier protein E2; E2 ubiquitin-conjugating enzyme E2;
                     ubiquitin conjugating enzyme E2E 2"
                     /calculated_mol_wt=22124
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Region          58..198
                     /region_name="UBCc_UBE2E"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 E1-E3 and
                     related proteins; cd23793"
                     /db_xref="CDD:467413"
     CDS             1..201
                     /gene="UBE2E2"
                     /gene_synonym="UBCH8"
                     /coded_by="NM_152653.4:147..752"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2637.1"
                     /db_xref="GeneID:7325"
                     /db_xref="HGNC:HGNC:12478"
                     /db_xref="MIM:602163"
ORIGIN      
        1 msteaqrvdd spstsggssd gdqresvqqe pereqvqpkk kegkisskta aklstsakri
       61 qkelaeitld pppncsagpk gdniyewrst ilgppgsvye ggvfflditf spdypfkppk
      121 vtfrtriyhc ninsqgvicl dilkdnwspa ltiskvllsi cslltdcnpa dplvgsiatq
      181 ymtnraehdr marqwtkrya t
//
LOCUS       NP_001268355             154 aa            linear   PRI 20-NOV-2025
DEFINITION  dynactin subunit 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001268355
VERSION     NP_001268355.1
DBSOURCE    REFSEQ: accession NM_001281426.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Su,X., Li,H., Chen,S. and Qin,C.
  TITLE     Study on the Prognostic Values of Dynactin Genes in Low-Grade
            Glioma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211010143 (2021)
   PUBMED   33896271
  REMARK    GeneRIF: Study on the Prognostic Values of Dynactin Genes in
            Low-Grade Glioma.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Mills,D.R. and Jackson,C.L.
  TITLE     Assignment of p22 dynactin light chain (DCTN3) to human chromosome
            region 9p13 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 92 (1-2), 166 (2001)
   PUBMED   11306820
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Karki,S., Tokito,M.K. and Holzbaur,E.L.
  TITLE     A dynactin subunit with a highly conserved cysteine-rich motif
            interacts directly with Arp1
  JOURNAL   J Biol Chem 275 (7), 4834-4839 (2000)
   PUBMED   10671518
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Karki,S., LaMonte,B. and Holzbaur,E.L.
  TITLE     Characterization of the p22 subunit of dynactin reveals the
            localization of cytoplasmic dynein and dynactin to the midbody of
            dividing cells
  JOURNAL   J Cell Biol 142 (4), 1023-1034 (1998)
   PUBMED   9722614
  REMARK    Erratum:[J Cell Biol 1998 Oct 19;143(2):following 560]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA212054.1, BC107697.1,
            BI596981.1 and CN257020.1.
            
            Summary: This gene encodes the smallest subunit of dynactin, a
            macromolecular complex consisting of 10 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation,
            cytokinesis, chromosome movement, nuclear positioning, and
            axonogenesis. This subunit, like most other dynactin subunits,
            exists only as a part of the dynactin complex. It is primarily an
            alpha-helical protein with very little coiled coil, and binds
            directly to the largest subunit (p150) of dynactin. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 3' coding region, which results in a translational
            frameshift, compared to variant 1. The encoded isoform (4) has a
            shorter and distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.435255.1,
                                           SRR1163657.142314.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..154
                     /product="dynactin subunit 3 isoform 4"
                     /note="dynactin light chain; dynactin complex subunit 22
                     kDa subunit; dynactin 3 (p22)"
                     /calculated_mol_wt=17096
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O75935.1)"
     Region          10..>137
                     /region_name="Dynactin_p22"
                     /note="Dynactin subunit p22; pfam07426"
                     /db_xref="CDD:462162"
     CDS             1..154
                     /gene="DCTN3"
                     /gene_synonym="DCTN-22; DCTN22"
                     /coded_by="NM_001281426.2:32..496"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:11258"
                     /db_xref="HGNC:HGNC:2713"
                     /db_xref="MIM:607387"
ORIGIN      
        1 magltdlqrl qarveelerw vygpggargs rkvadglvkv qvalgnissk rervkilykk
       61 iedlikyldp eyidriaipd asklqfilae eqfilsqval leqvnalvpm ldsahikavp
      121 ehaarlqrla qihiqqqfls vlhfgptgpv cgnh
//
LOCUS       NP_001356627             613 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear protein localization protein 4 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001356627 XP_011523283
VERSION     NP_001356627.1
DBSOURCE    REFSEQ: accession NM_001369698.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Bekkari,H., Benmakhlouf,Y., Nourouti,N.G., Barakat,A. and
            Mechita,M.B.
  TITLE     Study of Clinical Characteristics of Intellectual Disability in
            Morocco
  JOURNAL   Innov Clin Neurosci 21 (7-9), 10-14 (2024)
   PUBMED   39329031
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Wang,N., Zhu,D., Liu,Y., Wu,J., Wang,M., Jin,S., Fu,F., Li,B.,
            Ji,H., Du,C. and Zheng,Z.
  TITLE     NPLOC4 is a potential target and a poor prognostic signature in
            lung squamous cell carcinoma
  JOURNAL   Sci Rep 13 (1), 20430 (2023)
   PUBMED   37993584
  REMARK    GeneRIF: NPLOC4 is a potential target and a poor prognostic
            signature in lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Nguyen,T.Q., My Le,L.T., Kim,D.H., Ko,K.S., Lee,H.T., Kim
            Nguyen,Y.T., Kim,H.S., Han,B.W., Kang,W. and Yang,J.K.
  TITLE     Structural basis for the interaction between human Npl4 and
            Npl4-binding motif of human Ufd1
  JOURNAL   Structure 30 (11), 1530-1537 (2022)
   PUBMED   36087575
  REMARK    GeneRIF: Structural basis for the interaction between human Npl4
            and Npl4-binding motif of human Ufd1.
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Fujisawa,R., Polo Rivera,C. and Labib,K.P.M.
  TITLE     Multiple UBX proteins reduce the ubiquitin threshold of the
            mammalian p97-UFD1-NPL4 unfoldase
  JOURNAL   Elife 11, e76763 (2022)
   PUBMED   35920641
  REMARK    GeneRIF: Multiple UBX proteins reduce the ubiquitin threshold of
            the mammalian p97-UFD1-NPL4 unfoldase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 613)
  AUTHORS   McConnell,E., Lass,A. and Wojcik,C.
  TITLE     Ufd1-Npl4 is a negative regulator of cholera toxin
            retrotranslocation
  JOURNAL   Biochem Biophys Res Commun 355 (4), 1087-1090 (2007)
   PUBMED   17331469
  REMARK    GeneRIF: Ufd1-Npl4 is a negative regulator of retrotranslocation,
            delaying the retrotranslocation of endoplasmic reticulum-associated
            degradation substrates independently of its association with VCP
REFERENCE   7  (residues 1 to 613)
  AUTHORS   Arrigoni,R., Alam,S.L., Wamstad,J.A., Bardwell,V.J., Sundquist,W.I.
            and Schreiber-Agus,N.
  TITLE     The Polycomb-associated protein Rybp is a ubiquitin binding protein
  JOURNAL   FEBS Lett 580 (26), 6233-6241 (2006)
   PUBMED   17070805
  REMARK    Erratum:[FEBS Lett. 2006 Dec 11;580(28-29):6754]
REFERENCE   8  (residues 1 to 613)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   9  (residues 1 to 613)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   10 (residues 1 to 613)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC139530.3 and AC137896.5.
            
            On Apr 16, 2019 this sequence version replaced XP_011523283.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.243716.1,
                                           SRR1660803.141033.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..613
                     /product="nuclear protein localization protein 4 homolog
                     isoform 2"
                     /note="nuclear protein localization protein 4 homolog;
                     nuclear protein localization 4 homolog; NPLOC4 ubiquitin
                     recognition factor"
                     /calculated_mol_wt=68431
     Region          1..80
                     /region_name="UN_NPL4"
                     /note="Nuclear pore localization protein NPL4; pfam11543"
                     /db_xref="CDD:431926"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          105..245
                     /region_name="zf-NPL4"
                     /note="NPL4 family, putative zinc binding region;
                     pfam05020"
                     /db_xref="CDD:461523"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60670; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          249..560
                     /region_name="NPL4"
                     /note="NPL4 family; pfam05021"
                     /db_xref="CDD:461524"
     Region          589..611
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          589..608
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     CDS             1..613
                     /gene="NPLOC4"
                     /gene_synonym="NPL4"
                     /coded_by="NM_001369698.1:183..2024"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:55666"
                     /db_xref="HGNC:HGNC:18261"
                     /db_xref="MIM:606590"
ORIGIN      
        1 maesiiirvq spdgvkrita tkretaatfl kkvakefgfq nngfsvyinr nktgeitass
       61 nkslnllkik hgdllflfps slagpsseme tsvppgfkvf gapnvvedei dqylskqdgk
      121 iyrsrdpqlc rhgplgkcvh cvplepfded ylnhleppvk hmsfhayirk ltggadkgkf
      181 valeniscki ksgceghlpw pngictkcqp saitlnrqky rhvdnimfen htvadrfldf
      241 wrktgnqhfg ylygrytehk diplgiraev aaiyeppqig tqnslelled pkaevvdeia
      301 aklglrkvgw iftdlvsedt rkgtvrysrn kdtyflssee citagdfqnk hpnmcrlspd
      361 ghfgskfvta vatglslagg pdnqvhfegy qvsnqcmalv rdecllpckd apelgyakes
      421 sseqyvpdvf ykdvdkfgne itqlarplpv eyliidittt fpkdpvytfs isqnpfpien
      481 rdvlgetqdf hslatylsqn tssvfldtis dfhlllflvt nevmplqdsi sllleavrtr
      541 neelaqtwkr seqwatieql cstvggqlpg lheygavggs thtataamwa cqhctfmnqp
      601 gtghcemcsl prt
//
LOCUS       NP_001139193             358 aa            linear   PRI 20-NOV-2025
DEFINITION  homer protein homolog 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001139193
VERSION     NP_001139193.1
DBSOURCE    REFSEQ: accession NM_001145721.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Chen,L., Shan,X., Wan,X., Zha,W. and Fan,R.
  TITLE     HOMER3 promotes liver hepatocellular carcinoma cancer progression
            by -upregulating EZH2 and mediating miR-361/GPNMB axis
  JOURNAL   Pathol Res Pract 254, 155150 (2024)
   PUBMED   38266459
  REMARK    GeneRIF: HOMER3 promotes liver hepatocellular carcinoma cancer
            progression by -upregulating EZH2 and mediating miR-361/GPNMB axis.
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Peixoto,A., Ferreira,D., Azevedo,R., Freitas,R., Fernandes,E.,
            Relvas-Santos,M., Gaiteiro,C., Soares,J., Cotton,S., Teixeira,B.,
            Paulo,P., Lima,L., Palmeira,C., Martins,G., Oliveira,M.J.,
            Silva,A.M.N., Santos,L.L. and Ferreira,J.A.
  TITLE     Glycoproteomics identifies HOMER3 as a potentially targetable
            biomarker triggered by hypoxia and glucose deprivation in bladder
            cancer
  JOURNAL   J Exp Clin Cancer Res 40 (1), 191 (2021)
   PUBMED   34108014
  REMARK    GeneRIF: Glycoproteomics identifies HOMER3 as a potentially
            targetable biomarker triggered by hypoxia and glucose deprivation
            in bladder cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Ishiguro,K. and Xavier,R.
  TITLE     Homer-3 regulates activation of serum response element in T cells
            via its EVH1 domain
  JOURNAL   Blood 103 (6), 2248-2256 (2004)
   PUBMED   14645007
  REMARK    GeneRIF: Homer-3 may be involved in the regulation of SRE
            activation in T cells via interaction between its EVH1 domain and
            C/EBP beta.
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Norton,N., Williams,H.J., Williams,N.M., Spurlock,G., Zammit,S.,
            Jones,G., Jones,S., Owen,R., O'Donovan,M.C. and Owen,M.J.
  TITLE     Mutation screening of the Homer gene family and association
            analysis in schizophrenia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 120B (1), 18-21 (2003)
   PUBMED   12815733
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Soloviev,M.M., Ciruela,F., Chan,W.Y. and McIlhinney,R.A.
  TITLE     Molecular characterisation of two structurally distinct groups of
            human homers, generated by extensive alternative splicing
  JOURNAL   J Mol Biol 295 (5), 1185-1200 (2000)
   PUBMED   10653696
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Tu,J.C., Xiao,B., Yuan,J.P., Lanahan,A.A., Leoffert,K., Li,M.,
            Linden,D.J. and Worley,P.F.
  TITLE     Homer binds a novel proline-rich motif and links group 1
            metabotropic glutamate receptors with IP3 receptors
  JOURNAL   Neuron 21 (4), 717-726 (1998)
   PUBMED   9808459
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Xiao,B., Tu,J.C., Petralia,R.S., Yuan,J.P., Doan,A., Breder,C.D.,
            Ruggiero,A., Lanahan,A.A., Wenthold,R.J. and Worley,P.F.
  TITLE     Homer regulates the association of group 1 metabotropic glutamate
            receptors with multivalent complexes of homer-related, synaptic
            proteins
  JOURNAL   Neuron 21 (4), 707-716 (1998)
   PUBMED   9808458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AW606967.1, AF093265.1,
            AC002985.1 and CN284196.1.
            
            Summary: This gene encodes a member of the HOMER family of
            postsynaptic density scaffolding proteins that share a similar
            domain structure consisting of an N-terminal
            Enabled/vasodilator-stimulated phosphoprotein homology 1 domain
            which mediates protein-protein interactions, and a carboxy-terminal
            coiled-coil domain and two leucine zipper motifs that are involved
            in self-oligomerization. The encoded protein binds numerous other
            proteins including group I metabotropic glutamate receptors,
            inositol 1,4,5-trisphosphate receptors and amyloid precursor
            proteins and has been implicated in diverse biological functions
            such as neuronal signaling, T-cell activation and trafficking of
            amyloid beta peptides. Alternative splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (3), termed Homer-3A00, differs in
            the 5' UTR and uses an alternate in-frame splice site in the 3'
            coding region compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF093265.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..358
                     /product="homer protein homolog 3 isoform 2"
                     /note="Homer, neuronal immediate early gene, 3; homer
                     protein homolog 3; homer homolog 3; homer scaffolding
                     protein 3"
                     /calculated_mol_wt=39348
     Region          1..80
                     /region_name="Required for interaction with NFATC2.
                     /evidence=ECO:0000269|PubMed:18218901"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Region          6..114
                     /region_name="EVH1_Homer_Vesl"
                     /note="Homer/Vesl family proteins EVH1 domain; cd01206"
                     /db_xref="CDD:269917"
     Site            order(27,73,77,92)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269917"
     Region          114..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X5; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JP6; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     CDS             1..358
                     /gene="HOMER3"
                     /gene_synonym="HOMER-3; VESL3"
                     /coded_by="NM_001145721.1:100..1176"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46023.1"
                     /db_xref="GeneID:9454"
                     /db_xref="HGNC:HGNC:17514"
                     /db_xref="MIM:604800"
ORIGIN      
        1 mstareqpif strahvfqid patkrnwipa gkhaltvsyf ydatrnvyri isiggakaii
       61 nstvtpnmtf tktsqkfgqw adsrantvyg lgfaseqhlt qfaekfqevk eaarlareks
      121 qdggeltspa lglashqvpp splvsangpg eeklfrsqsa dapgpterer lkkmlsegsv
      181 gevqweaeff alqdsnnkla galreanaaa aqwrqqleaq raeaerlrqr vaeleaqaas
      241 evtptgekeg lgqgqsleql ealvqtkdqe iqtlksqtgg prealeaaer eetqqkvqtr
      301 naelehqlra mersleeara ereraraevg raaqlldvsl felselregl arlaeaap
//
LOCUS       NP_787128                378 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 13 isoform 2 [Homo
            sapiens].
ACCESSION   NP_787128
VERSION     NP_787128.2
DBSOURCE    REFSEQ: accession NM_175932.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 378)
  AUTHORS   He,S., Cao,R., Mao,Y., Li,N., Wang,Y., Ma,H. and Tian,K.
  TITLE     Alternative splicing of PSMD13 mediated by genetic variants is
            significantly associated with endometrial cancer risk
  JOURNAL   J Gynecol Oncol 34 (3), e40 (2023)
   PUBMED   36731897
  REMARK    GeneRIF: Alternative splicing of PSMD13 mediated by genetic
            variants is significantly associated with endometrial cancer risk.
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 378)
  AUTHORS   Hori,T., Kato,S., Saeki,M., DeMartino,G.N., Slaughter,C.A.,
            Takeuchi,J., Toh-e,A. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p28 (Nas6p) and p40.5
            (Nas7p), two novel regulatory subunits of the 26S proteasome
  JOURNAL   Gene 216 (1), 113-122 (1998)
   PUBMED   9714768
REFERENCE   9  (residues 1 to 378)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   10 (residues 1 to 378)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC136475.7, AK094775.1, AL556906.3 and AA931044.1.
            
            On Sep 25, 2007 this sequence version replaced NP_787128.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. Two transcripts encoding
            different isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks an alternate segment and
            uses a different splice site in the 5' coding region, compared to
            variant 1. These differences cause a frameshift and then a
            restoration in the reading frame. Isoform 2 has a slightly shorter
            N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.186832.1, AK094775.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..378
                     /product="26S proteasome non-ATPase regulatory subunit 13
                     isoform 2"
                     /note="26S proteasome subunit p40.5; 26S proteasome
                     regulatory subunit S11; 26S proteasome non-ATPase
                     regulatory subunit 13; 26S proteasome regulatory subunit
                     p40.5; 26S proteasome regulatory subunit RPN9; proteasome
                     (prosome, macropain) 26S subunit, non-ATPase, 13"
                     /calculated_mol_wt=42812
     Region          233..337
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..378
                     /gene="PSMD13"
                     /gene_synonym="HSPC027; p40.5; Rpn9; S11"
                     /coded_by="NM_175932.3:75..1211"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44504.1"
                     /db_xref="GeneID:5719"
                     /db_xref="HGNC:HGNC:9558"
                     /db_xref="MIM:603481"
ORIGIN      
        1 mkdvpgflqq sqnsgpgqpa vwhrleelyt knfmktlsvn lntgkslssv fhfenecida
       61 rrcskaggfy frvnplslve iilhvvrqmt dpnvaltfle ktrekvkssd eavilcktai
      121 galklnigdl qvtketiedv eemlnnlpgv tsvhsrfydl sskyyqtign hasyykdalr
      181 flgcvdikdl pvseqqeraf tlglagllge gvfnfgellm hpvleslrnt drqwlidtly
      241 afnsgnverf qtlktawgqq pdlaaneaql lrkiqllclm emtftrpanh rqltfeeiak
      301 sakitvneve llvmkalsvg lvkgsidevd krvhmtwvqp rvldlqqikg mkdrlefwct
      361 dvksmemlve hqahdilt
//
LOCUS       NP_001308735             722 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform j [Homo sapiens].
ACCESSION   NP_001308735
VERSION     NP_001308735.1
DBSOURCE    REFSEQ: accession NM_001321806.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 14 and 15 encode the same isoform (j).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4265097.1,
                                           SRR14038197.1567718.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..722
                     /product="E3 ubiquitin-protein ligase CBL-B isoform j"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=79175
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          671..711
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(673..674,676..678,680..681,686,690)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..722
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321806.2:739..2907"
                     /note="isoform j is encoded by transcript variant 14"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikctgpl anslsektrd pveedddeyk ipsshpvsln sqpshchnvk ppvrscdngh
      481 cmlngthgps sekksnipdl siylkgdvfd sasdpvplpp arpptrdnpk hgsslnrtps
      541 dydllipplg edafdalpps lpppppparh sliehskppg sssrpssgqd lfllpsdpfv
      601 dlasgqvplp parrlpgenv ktnrtsqdyd qlpscsdgsq aparppkprp rrtapeihhr
      661 kphgpeaale nvdakiaklm gegyafeevk raleiaqnnv evarsilref afpppvsprl
      721 nl
//
LOCUS       NP_001354685             414 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform m [Homo sapiens].
ACCESSION   NP_001354685
VERSION     NP_001354685.1
DBSOURCE    REFSEQ: accession NM_001367756.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.246702.1,
                                           SRR1660803.243825.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..414
                     /product="rab5 GDP/GTP exchange factor isoform m"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=47895
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          81..143
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          193..293
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..414
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367756.1:78..1322"
                     /note="isoform m is encoded by transcript variant 40"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkaspsi nrqtsietdr
       61 vskefieflk tfhktgqeiy kqtklflegm hykrdlsiee qsecaqdfyh nvaermqtrg
      121 kvpperveki mdqiekyimt rlykyvfcpe ttddekkdla iqkriralrw vtpqmlcvpv
      181 nedipevsdm vvkaitdiie mdskrvprdk lacitkcskh ifnaikitkn epasaddflp
      241 tliyivlkgn pprlqsniqy itrfcnpsrl mtgedgyyft nlccavafie kldaqslnls
      301 qedfdrymsg qtsprkqeae swspdaclgv kqmyknldll sqlnerqeri mneakklekd
      361 lidwtdgiar evqdivekyp leikppnqpl aaidsenven dklppplqpq vyag
//
LOCUS       NP_653186                553 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 22 member 12 isoform a [Homo sapiens].
ACCESSION   NP_653186
VERSION     NP_653186.2
DBSOURCE    REFSEQ: accession NM_144585.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   He,J., Liu,G., Kong,F., Tan,Q., Wang,Z., Yang,M., He,Y., Jia,X.,
            Yan,C., Wang,C. and Qian,H.
  TITLE     Structural basis for the transport and substrate selection of human
            urate transporter 1
  JOURNAL   Cell Rep 43 (8), 114628 (2024)
   PUBMED   39146184
  REMARK    GeneRIF: Structural basis for the transport and substrate selection
            of human urate transporter 1.
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Perdomo-Ramirez,A., Ramos-Trujillo,E. and Claverie-Martin,F.
  CONSRTM   RenalTube Group
  TITLE     New SLC22A12 (URAT1) Variant Associated with Renal Hypouricemia
            Identified by Whole-Exome Sequencing Analysis and Bioinformatics
            Predictions
  JOURNAL   Genes (Basel) 14 (9), 1823 (2023)
   PUBMED   37761963
  REMARK    GeneRIF: New SLC22A12 (URAT1) Variant Associated with Renal
            Hypouricemia Identified by Whole-Exome Sequencing Analysis and
            Bioinformatics Predictions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Perdomo-Ramirez,A., Cordoba-Lanus,E., Trujillo-Frias,C.J.,
            Gonzalez-Navasa,C., Ramos-Trujillo,E., Luis-Yanes,M.I.,
            Garcia-Nieto,V. and Claverie-Martin,F.
  CONSRTM   RenalTube
  TITLE     Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9) in
            Spanish Patients with Renal Hypouricemia: Founder Effect of SLC2A9
            Variant c.374C>T; p.(T125M)
  JOURNAL   Int J Mol Sci 24 (9), 8455 (2023)
   PUBMED   37176161
  REMARK    GeneRIF: Pathogenic Variants of SLC22A12 (URAT1) and SLC2A9 (GLUT9)
            in Spanish Patients with Renal Hypouricemia: Founder Effect of
            SLC2A9 Variant c.374C>T; p.(T125M).
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Vargas-Morales,J.M., Guevara-Cruz,M., Aradillas-Garcia,C., G
            Noriega,L., Tovar,A. and Alegria-Torres,J.A.
  TITLE     Polymorphisms of the genes ABCG2, SLC22A12 and XDH and their
            relation with hyperuricemia and hypercholesterolemia in Mexican
            young adults
  JOURNAL   F1000Res 10, 217 (2021)
   PUBMED   34631016
  REMARK    GeneRIF: Polymorphisms of the genes ABCG2, SLC22A12 and XDH and
            their relation with hyperuricemia and hypercholesterolemia in
            Mexican young adults.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Anzai,N., Miyazaki,H., Noshiro,R., Khamdang,S., Chairoungdua,A.,
            Shin,H.J., Enomoto,A., Sakamoto,S., Hirata,T., Tomita,K., Kanai,Y.
            and Endou,H.
  TITLE     The multivalent PDZ domain-containing protein PDZK1 regulates
            transport activity of renal urate-anion exchanger URAT1 via its C
            terminus
  JOURNAL   J Biol Chem 279 (44), 45942-45950 (2004)
   PUBMED   15304510
  REMARK    GeneRIF: PDZK1 plays a role in regulating the functional activity
            of URAT1-mediated urate transport in the apical membrane of renal
            proximal tubules.
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Iwai,N., Mino,Y., Hosoyamada,M., Tago,N., Kokubo,Y. and Endou,H.
  TITLE     A high prevalence of renal hypouricemia caused by inactive SLC22A12
            in Japanese
  JOURNAL   Kidney Int 66 (3), 935-944 (2004)
   PUBMED   15327384
  REMARK    GeneRIF: SLC22A12 is a major gene for hypouricemia but not
            hyperuricemia in Japanese.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Ichida,K., Hosoyamada,M., Hisatome,I., Enomoto,A., Hikita,M.,
            Endou,H. and Hosoya,T.
  TITLE     Clinical and molecular analysis of patients with renal hypouricemia
            in Japan-influence of URAT1 gene on urinary urate excretion
  JOURNAL   J Am Soc Nephrol 15 (1), 164-173 (2004)
   PUBMED   14694169
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Gisler,S.M., Pribanic,S., Bacic,D., Forrer,P., Gantenbein,A.,
            Sabourin,L.A., Tsuji,A., Zhao,Z.S., Manser,E., Biber,J. and
            Murer,H.
  TITLE     PDZK1: I. a major scaffolder in brush borders of proximal tubular
            cells
  JOURNAL   Kidney Int 64 (5), 1733-1745 (2003)
   PUBMED   14531806
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Enomoto,A., Kimura,H., Chairoungdua,A., Shigeta,Y., Jutabha,P.,
            Cha,S.H., Hosoyamada,M., Takeda,M., Sekine,T., Igarashi,T.,
            Matsuo,H., Kikuchi,Y., Oda,T., Ichida,K., Hosoya,T., Shimokata,K.,
            Niwa,T., Kanai,Y. and Endou,H.
  TITLE     Molecular identification of a renal urate anion exchanger that
            regulates blood urate levels
  JOURNAL   Nature 417 (6887), 447-452 (2002)
   PUBMED   12024214
  REMARK    GeneRIF: Molecular identification of a renal urate anion exchanger
            that regulates blood urate levels
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB050269.1, DA631511.1,
            BC053348.1 and AP001092.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 3, 2002 this sequence version replaced NP_653186.1.
            
            Summary: The protein encoded by this gene is a member of the
            organic anion transporter (OAT) family, and it acts as a urate
            transporter to regulate urate levels in blood. This protein is an
            integral membrane protein primarily found in epithelial cells of
            the proximal tubule of the kidney. An elevated level of serum
            urate, hyperuricemia, is associated with increased incidences of
            gout, and mutations in this gene cause renal hypouricemia type 1.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053348.1, AB050269.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377574.6/ ENSP00000366797.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..553
                     /product="solute carrier family 22 member 12 isoform a"
                     /note="solute carrier family 22 (organic anion/cation
                     transporter), member 12; urate transporter 1; urate anion
                     exchanger 1; renal-specific transporter; organic anion
                     transporter 4-like protein; solute carrier family 22
                     (organic anion/urate transporter), member 12; urate:anion
                     antiporter SLC22A12; urate anion transporter 1"
                     /calculated_mol_wt=59499
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96S37.1)"
     Region          109..516
                     /region_name="MFS_OAT"
                     /note="Organic anion transporters of the Major Facilitator
                     Superfamily of transporters; cd17374"
                     /db_xref="CDD:340932"
     Site            order(126..127,130..131,134,160,210..211,213..215,218,234,
                     237..238,241,357,360..361,364..366,369,389,393,444..445,
                     449,453,469,472..473,476..477,480)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340932"
     Site            146..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            195..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            378..398
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            407..427
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            435..455
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            466..486
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            495..515
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S37.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8CFZ5; propagated from
                     UniProtKB/Swiss-Prot (Q96S37.1)"
     CDS             1..553
                     /gene="SLC22A12"
                     /gene_synonym="hURAT1; OAT4L; RST; UAT; URAT1"
                     /coded_by="NM_144585.4:338..1999"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8075.1"
                     /db_xref="GeneID:116085"
                     /db_xref="HGNC:HGNC:17989"
                     /db_xref="MIM:607096"
ORIGIN      
        1 mafselldlv gglgrfqvlq tmalmvsimw lctqsmlenf saavpshrcw aplldnstaq
       61 asilgslspe allaisippg pnqrphqcrr frqpqwqlld pnatatswse adtepcvdgw
      121 vydrsiftst ivakwnlvcd shalkpmaqs iylagilvga aacgpasdrf grrlvltwsy
      181 lqmavmgtaa afapafpvyc lfrfllafav agvmmntgtl lmewtaarar plvmtlnslg
      241 fsfghgltaa vaygvrdwtl lqlvvsvpff lcflyswwla esarwllttg rldwglqelw
      301 rvaaingkga vqdtltpevl lsamreelsm gqppaslgtl lrmpglrfrt cistlcwfaf
      361 gftffglald lqalgsnifl lqmfigvvdi pakmgallll shlgrrptla aslllaglci
      421 lantlvphem galrsalavl glggvgaaft citiysself ptvlrmtavg lgqmaargga
      481 ilgplvrllg vhgpwlpllv ygtvpvlsgl aalllpetqs lplpdtiqdv qnqavkkath
      541 gtlgnsvlks tqf
//
LOCUS       NP_001201836             495 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 48 isoform 2 [Homo sapiens].
ACCESSION   NP_001201836
VERSION     NP_001201836.1
DBSOURCE    REFSEQ: accession NM_001214907.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Lichter,P., Bray,P., Ried,T., Dawid,I.B. and Ward,D.C.
  TITLE     Clustering of C2-H2 zinc finger motif sequences within telomeric
            and fragile site regions of human chromosomes
  JOURNAL   Genomics 13 (4), 999-1007 (1992)
   PUBMED   1505991
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Bray,P., Lichter,P., Thiesen,H.J., Ward,D.C. and Dawid,I.B.
  TITLE     Characterization and mapping of human genes encoding zinc finger
            proteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9563-9567 (1991)
   PUBMED   1946370
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA492655.1, AC116348.3 and CA434624.1.
            
            Transcript Variant: This variant (4) has an alternate 5' exon,
            resulting in a downstream AUG start codon, compared to variant 1.
            The resulting isoform (2) is shorter at the N-terminus, compared to
            isoform 1. Variants 4 and 5 both encode the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA492655.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..495
                     /product="zinc finger protein 48 isoform 2"
                     /note="zinc finger protein 553"
                     /calculated_mol_wt=53857
     Region          3..26
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          19..39
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(24,26,28,30..31,34..35,38,76,78,82..83,86..87,90,
                     104,106,108,110..111,114..115,118)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          67..476
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          71..91
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          99..119
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          154..174
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          182..202
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(187,189,191,193..194,197..198,201,215,217,221..222,
                     225..226,229,243,245,247,249..250,253..254,257)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          210..230
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          238..258
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          330..350
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(335,337,339,341..342,345..346,349,363,365,369..370,
                     373..374,377,427,429,431,433..434,437..438,441)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          358..378
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          422..442
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          450..470
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     CDS             1..495
                     /gene="ZNF48"
                     /gene_synonym="ZNF553"
                     /coded_by="NM_001214907.1:388..1875"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS73868.1"
                     /db_xref="GeneID:197407"
                     /db_xref="HGNC:HGNC:13114"
ORIGIN      
        1 msdlvkhqrt htgekpykcg vcgkgfgdss arikhqrths gekpyrarpp aqgppkiprs
       61 ripagerpti cgecgksfrq ssdlvkhqrt htgekpykcg icgkgfgdss arikhqrthr
      121 geqpprpvvp rrqpsraata atqgpkaqdk pyictdcgkr fvlscsllsh qrshlgpkpf
      181 gcdvcgkefa rgsdlvkhlr vhtgekpylc pecgkgfads sarvkhlrth sgerphacpe
      241 cdrtfslsst llrhrlthme pqdfsfpgyp lpalipsppp pplgtspplt prspshsgep
      301 fglpglepep ggpqageppp plagdkphkc pecgkgfrrs sdlvkhhrvh tgekpylcpe
      361 cgkgfadssa rvkhlrthrg erarppppst llrphnppgp vpmaprprvr aqpsgpsqph
      421 vcgfcgkefp rssdlvkhrr thtgekpykc aecgkgfgds sarikhqrgh lvltpfgigd
      481 grarplkqea atgle
//
LOCUS       NP_001355047             475 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 3 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001355047
VERSION     NP_001355047.1
DBSOURCE    REFSEQ: accession NM_001368118.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Ergun,S., Guney,S., Temiz,E., Petrovic,N. and Gunes,S.
  TITLE     Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
  JOURNAL   Anticancer Agents Med Chem 18 (12), 1695-1701 (2018)
   PUBMED   30019650
  REMARK    GeneRIF: Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Jin,L., Wang,T., Jiang,S., Chen,M., Zhang,R., Hu,C., Jia,W. and
            Liu,Z.
  TITLE     The Association of a Genetic Variant in SCAF8-CNKSR3 with Diabetic
            Kidney Disease and Diabetic Retinopathy in a Chinese Population
  JOURNAL   J Diabetes Res 2017, 6542689 (2017)
   PUBMED   28401168
  REMARK    GeneRIF: SCAF8-CNKSR3 variant rs955333 was not associated with
            diabetic kidney disease but showed association with diabetic
            retinopathy in Chinese type 2 diabetes patients
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Lake,S.L., Damato,B.E., Kalirai,H., Dodson,A.R., Taktak,A.F.,
            Lloyd,B.H. and Coupland,S.E.
  TITLE     Single nucleotide polymorphism array analysis of uveal melanomas
            reveals that amplification of CNKSR3 is correlated with improved
            patient survival
  JOURNAL   Am J Pathol 182 (3), 678-687 (2013)
   PUBMED   23357503
  REMARK    GeneRIF: Cox regression and Kaplan-Meier survival analysis
            identified that amplification of the CNKSR3 gene (log-rank, P =
            0.022) with an associated increase in its protein expression
            (log-rank, P = 0.011) correlated with longer patient survival.
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Okada,Y., Sim,X., Go,M.J., Wu,J.Y., Gu,D., Takeuchi,F.,
            Takahashi,A., Maeda,S., Tsunoda,T., Chen,P., Lim,S.C., Wong,T.Y.,
            Liu,J., Young,T.L., Aung,T., Seielstad,M., Teo,Y.Y., Kim,Y.J.,
            Lee,J.Y., Han,B.G., Kang,D., Chen,C.H., Tsai,F.J., Chang,L.C.,
            Fann,S.J., Mei,H., Rao,D.C., Hixson,J.E., Chen,S., Katsuya,T.,
            Isono,M., Ogihara,T., Chambers,J.C., Zhang,W., Kooner,J.S.,
            Albrecht,E., Yamamoto,K., Kubo,M., Nakamura,Y., Kamatani,N.,
            Kato,N., He,J., Chen,Y.T., Cho,Y.S., Tai,E.S. and Tanaka,T.
  CONSRTM   KidneyGen Consortium; CKDGen Consortium; GUGC consortium
  TITLE     Meta-analysis identifies multiple loci associated with kidney
            function-related traits in east Asian populations
  JOURNAL   Nat Genet 44 (8), 904-909 (2012)
   PUBMED   22797727
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Shin,S., Park,J.S., Kim,Y.J., Oh,T., An,S. and Park,C.S.
  TITLE     Differential gene expression profile in PBMCs from subjects with
            AERD and ATA: a gene marker for AERD
  JOURNAL   Mol Genet Genomics 287 (5), 361-371 (2012)
   PUBMED   22457146
  REMARK    GeneRIF: two gene markers (CNKSR3 and SPTBN2) differentiate between
            aspirin-exacerbated respiratory disease and aspirin-tolerant asthma
            with a perfect discriminative power
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Pankratz,N., Beecham,G.W., DeStefano,A.L., Dawson,T.M.,
            Doheny,K.F., Factor,S.A., Hamza,T.H., Hung,A.Y., Hyman,B.T.,
            Ivinson,A.J., Krainc,D., Latourelle,J.C., Clark,L.N., Marder,K.,
            Martin,E.R., Mayeux,R., Ross,O.A., Scherzer,C.R., Simon,D.K.,
            Tanner,C., Vance,J.M., Wszolek,Z.K., Zabetian,C.P., Myers,R.H.,
            Payami,H., Scott,W.K. and Foroud,T.
  CONSRTM   PD GWAS Consortium
  TITLE     Meta-analysis of Parkinson's disease: identification of a novel
            locus, RIT2
  JOURNAL   Ann Neurol 71 (3), 370-384 (2012)
   PUBMED   22451204
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Attar,M.A., Salem,J.C., Pursel,H.S. and Santy,L.C.
  TITLE     CNK3 and IPCEF1 produce a single protein that is required for HGF
            dependent Arf6 activation and migration
  JOURNAL   Exp Cell Res 318 (3), 228-237 (2012)
   PUBMED   22085542
  REMARK    GeneRIF: CNK3 and IPCEF1 produce a single protein that is required
            for HGF dependent Arf6 activation and migration.
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Ziera,T., Irlbacher,H., Fromm,A., Latouche,C., Krug,S.M., Fromm,M.,
            Jaisser,F. and Borden,S.A.
  TITLE     Cnksr3 is a direct mineralocorticoid receptor target gene and plays
            a key role in the regulation of the epithelial sodium channel
  JOURNAL   FASEB J 23 (11), 3936-3946 (2009)
   PUBMED   19567370
  REMARK    GeneRIF: CNKSR3, a homologue of scaffold proteins involved in MAPK
            pathway regulation, is a direct target of MR and is required for
            the maintenance of transepithelial sodium transport in the kidney.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK309680.1 and AL357075.17.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK309680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.2"
     Protein         1..475
                     /product="connector enhancer of kinase suppressor of ras 3
                     isoform 4"
                     /note="connector enhancer of kinase suppressor of ras 3;
                     membrane associated guanylate kinase, WW and PDZ domain
                     containing 1; maguin-like protein; CNK homolog protein 3;
                     connector enhancer of KSR 3; membrane-associated guanylate
                     kinase-interacting protein-like 1"
                     /calculated_mol_wt=52513
     Region          1..92
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          130..210
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(142..148,158,161,191,195,198..199)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          252..465
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     CDS             1..475
                     /gene="CNKSR3"
                     /gene_synonym="CNK3; CNK3/IPCEF1; MAGI1"
                     /coded_by="NM_001368118.1:352..1779"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94023.1"
                     /db_xref="GeneID:154043"
                     /db_xref="HGNC:HGNC:23034"
                     /db_xref="MIM:617476"
ORIGIN      
        1 mknlvlklra sshnlqnyis srrkspaydg ntsrkapnef ltsvveliga akallawldr
       61 apftgitdfs vtknkiiqlc ldltttvqkd cfvaemedkv ltvvkvlngi cdktirsttd
      121 pvmsqcacle evhlpnikpg eglgmyikst ydglhvitgt tenspadrsq kihagdeviq
      181 vnqqtvvgwq lknlvkklre nptgvvlllk krptgsfnft paplknlrwk pplvqtsppp
      241 attqspestm dtslkkeksa ildlyipppp avpysprden gsfvyggssk ckqplpgpkg
      301 sespnsfldq esrrrrftia dsdqlpgysv etnilptkmr ektpsygkpr plsmpadgnw
      361 mgivdpfarp rghgrkgeda lcryfsneri ppiieesssp pyrfsrptte rhlvrgadyi
      421 rgsrcyinsd lhssatipfq eegtkkksgs satkssstep sllvswftrl kllth
//
LOCUS       NP_116166               1338 aa            linear   PRI 20-NOV-2025
DEFINITION  adhesion G protein-coupled receptor A2 precursor [Homo sapiens].
ACCESSION   NP_116166
VERSION     NP_116166.9
DBSOURCE    REFSEQ: accession NM_032777.10
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1338)
  AUTHORS   Shen,Y., Cui,Q., Xiao,L., Wang,L., Li,Q., Zhang,R., Chen,Z. and
            Niu,J.
  TITLE     Down-regulated Wnt7a and GPR124 in early-onset preeclampsia
            placentas reduce invasion and migration of trophoblast cells
  JOURNAL   J Perinat Med 52 (1), 41-49 (2023)
   PUBMED   37694534
  REMARK    GeneRIF: Down-regulated Wnt7a and GPR124 in early-onset
            preeclampsia placentas reduce invasion and migration of trophoblast
            cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1338)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1338)
  AUTHORS   America,M., Bostaille,N., Eubelen,M., Martin,M., Stainier,D.Y.R.
            and Vanhollebeke,B.
  TITLE     An integrated model for Gpr124 function in Wnt7a/b signaling among
            vertebrates
  JOURNAL   Cell Rep 39 (9), 110902 (2022)
   PUBMED   35649360
  REMARK    GeneRIF: An integrated model for Gpr124 function in Wnt7a/b
            signaling among vertebrates.
REFERENCE   4  (residues 1 to 1338)
  AUTHORS   Ta,S., Rong,X., Guo,Z.N., Jin,H., Zhang,P., Li,F., Li,Z., Lin,L.,
            Zheng,C., Gu,Q., Zhang,Y., Liu,W., Yang,Y. and Chang,J.
  TITLE     Variants of WNT7A and GPR124 are associated with hemorrhagic
            transformation following intravenous thrombolysis in ischemic
            stroke
  JOURNAL   CNS Neurosci Ther 27 (1), 71-81 (2021)
   PUBMED   32991049
  REMARK    GeneRIF: Variants of WNT7A and GPR124 are associated with
            hemorrhagic transformation following intravenous thrombolysis in
            ischemic stroke.
REFERENCE   5  (residues 1 to 1338)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1338)
  AUTHORS   Vallon,M. and Essler,M.
  TITLE     Proteolytically processed soluble tumor endothelial marker (TEM) 5
            mediates endothelial cell survival during angiogenesis by linking
            integrin alpha(v)beta3 to glycosaminoglycans
  JOURNAL   J Biol Chem 281 (45), 34179-34188 (2006)
   PUBMED   16982628
  REMARK    GeneRIF: Proteolytically processed soluble tumor endothelial marker
            TEM5 mediates endothelial cell survival during angiogenesis by
            linking integrin alpha(v)beta3 to glycosaminoglycans
REFERENCE   7  (residues 1 to 1338)
  AUTHORS   Bjarnadottir,T.K., Fredriksson,R., Hoglund,P.J., Gloriam,D.E.,
            Lagerstrom,M.C. and Schioth,H.B.
  TITLE     The human and mouse repertoire of the adhesion family of
            G-protein-coupled receptors
  JOURNAL   Genomics 84 (1), 23-33 (2004)
   PUBMED   15203201
REFERENCE   8  (residues 1 to 1338)
  AUTHORS   Yamamoto,Y., Irie,K., Asada,M., Mino,A., Mandai,K. and Takai,Y.
  TITLE     Direct binding of the human homologue of the Drosophila disc large
            tumor suppressor gene to seven-pass transmembrane proteins, tumor
            endothelial marker 5 (TEM5), and a novel TEM5-like protein
  JOURNAL   Oncogene 23 (22), 3889-3897 (2004)
   PUBMED   15021905
REFERENCE   9  (residues 1 to 1338)
  AUTHORS   Fredriksson,R., Gloriam,D.E., Hoglund,P.J., Lagerstrom,M.C. and
            Schioth,H.B.
  TITLE     There exist at least 30 human G-protein-coupled receptors with long
            Ser/Thr-rich N-termini
  JOURNAL   Biochem Biophys Res Commun 301 (3), 725-734 (2003)
   PUBMED   12565841
REFERENCE   10 (residues 1 to 1338)
  AUTHORS   Carson-Walter,E.B., Watkins,D.N., Nanda,A., Vogelstein,B.,
            Kinzler,K.W. and St Croix,B.
  TITLE     Cell surface tumor endothelial markers are conserved in mice and
            humans
  JOURNAL   Cancer Res 61 (18), 6649-6655 (2001)
   PUBMED   11559528
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA569569.1, AY090637.1, AF378755.1, AL110244.1, AI346793.1,
            AC138356.3 and AC130304.12.
            
            On Jul 21, 2010 this sequence version replaced NP_116166.8.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF378755.1, AK074099.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412232.3/ ENSP00000406367.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..1338
                     /product="adhesion G protein-coupled receptor A2
                     precursor"
                     /note="tumor endothelial marker 5; G-protein coupled
                     receptor 124"
                     /calculated_mol_wt=139129
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3537
     mat_peptide     34..1338
                     /product="Adhesion G protein-coupled receptor A2.
                     /id=PRO_0000012898"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
                     /calculated_mol_wt=139129
     Region          82..106
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          86..109
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          <88..>232
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          88..144
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          107..130
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          110..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          131..154
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          134..157
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          156..178
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          158..181
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          182..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          257..343
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            275
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          351..417
                     /region_name="HRM"
                     /note="Hormone receptor domain; cl02422"
                     /db_xref="CDD:413313"
     Region          362..364
                     /region_name="RGD. /evidence=ECO:0000269|PubMed:16982628"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            369..370
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin.
                     /evidence=ECO:0000269|PubMed:22013897; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            398..399
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin.
                     /evidence=ECO:0000269|PubMed:22013897; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          565..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          708..752
                     /region_name="GPS"
                     /note="GPCR proteolysis site, GPS, motif; pfam01825"
                     /db_xref="CDD:460350"
     Region          710..759
                     /region_name="GPS.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00098"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          766..1081
                     /region_name="7tmB2_GPR124"
                     /note="G protein-coupled receptor 124, member of the class
                     B2 family of seven-transmembrane G protein-coupled
                     receptors; cd15998"
                     /db_xref="CDD:320664"
     Region          768..793
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320664"
     Site            772..792
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            order(773,777,822,825..826,829,836,843,924..925,927,929,
                     1033,1036,1051,1055)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:320664"
     Region          805..827
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320664"
     Site            808..828
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            833..853
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          836..863
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320664"
     Region          884..904
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320664"
     Site            887..907
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          921..950
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320664"
     Site            925..945
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          958..991
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1014..1041
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320664"
     Site            1020..1040
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1048..1073
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320664"
     Site            1048..1068
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1088..1126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Site            1107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1150..1196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1218..1309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     Region          1335..1338
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:15021905"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96PE1.2)"
     CDS             1..1338
                     /gene="ADGRA2"
                     /gene_synonym="GPR124; TEM5"
                     /coded_by="NM_032777.10:387..4403"
                     /db_xref="CCDS:CCDS6097.2"
                     /db_xref="GeneID:25960"
                     /db_xref="HGNC:HGNC:17849"
                     /db_xref="MIM:606823"
ORIGIN      
        1 mgaggrrmrg aparlllpll pwlllllape argapgcpls irsckcsger pkglsggvpg
       61 parrrvvcsg gdlpeppepg llpngtvtll lsnnkitglr ngsflglsll ekldlrnnii
      121 stvqpgaflg lgelkrldls nnrigcltse tfqglprllr lnisgnifss lqpgvfdelp
      181 alkvvdlgte fltcdchlrw llpwaqnrsl qlsehtlcay psalhaqalg slqeaqlcce
      241 galelhthhl ipslrqvvfq gdrlpfqcsa sylgndtrir wyhnrapveg deqagillae
      301 slihdctfit seltlshigv wasgewectv smaqgnaskk veivvletsa sycpaervan
      361 nrgdfrwprt lagitayqsc lqypftsvpl gggapgtras rrcdragrwe pgdyshclyt
      421 nditrvlytf vlmpinasna ltlahqlrvy taeaasfsdm mdvvyvaqmi qkflgyvdqi
      481 kelvevmvdm asnlmlvdeh llwlaqredk acsrivgale riggaalsph aqhisvnarn
      541 valeaylikp hsyvgltcta fqrreggvpg trpgspgqnp ppepeppadq qlrfrcttgr
      601 pnvslssfhi knsvalasiq lppslfsslp aalappvppd ctlqllvfrn grlfhshsnt
      661 srpgaagpgk rrgvatpvif agtsgcgvgn ltepvavslr hwaegaepva awwsqegpge
      721 aggwtsegcq lrssqpnvsa lhcqhlgnva vlmelsafpr evggagaglh pvvypctall
      781 llclfatiit yilnhssirv srkgwhmlln lcfhiamtsa vfaggitltn yqmvcqavgi
      841 tlhysslstl lwmgvkarvl hkeltwrapp pqegdpalpt pspmlrfyli aggipliicg
      901 itaavnihny rdhspycwlv wrpslgafyi pvalillitw iyflcaglrl rgplaqnpka
      961 gnsrasleag eelrgstrlr gsgpllsdsg sllatgsarv gtpgppedgd slyspgvqlg
     1021 alvtthflyl amwacgalav sqrwlprvvc sclygvaasa lglfvfthhc arrrdvrasw
     1081 raccppaspa aphappralp aaaedgspvf gegppslkss psgssghpla lgpckltnlq
     1141 laqsqvceag aaaggegepe pagtrgnlah rhpnnvhhgr rahksrakgh rageacgknr
     1201 lkalrggaag alellssesg slhnsptdsy lgssrnspga glqlegepml tpsegsdtsa
     1261 aplseagrag qrrsasrdsl kgggalekes hrrsyplnaa slngapkggk yddvtlmgae
     1321 vasggcmktg lwksettv
//
LOCUS       NP_006234                486 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            alpha isoform isoform 1 [Homo sapiens].
ACCESSION   NP_006234
VERSION     NP_006234.1
DBSOURCE    REFSEQ: accession NM_006243.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Ambjorn,S.M., Duxin,J.P., Hertz,E.P.T., Nasa,I., Duro,J., Kruse,T.,
            Lopez-Mendez,B., Rymarczyk,B., Cressey,L.E., van Overeem Hansen,T.,
            Kettenbach,A.N., Oestergaard,V.H., Lisby,M. and Nilsson,J.
  TITLE     A complex of BRCA2 and PP2A-B56 is required for DNA repair by
            homologous recombination
  JOURNAL   Nat Commun 12 (1), 5748 (2021)
   PUBMED   34593815
  REMARK    GeneRIF: A complex of BRCA2 and PP2A-B56 is required for DNA repair
            by homologous recombination.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 486)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   7  (residues 1 to 486)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Fuhrer,D.K. and Yang,Y.C.
  TITLE     Complex formation of JAK2 with PP2A, P13K, and Yes in response to
            the hematopoietic cytokine interleukin-11
  JOURNAL   Biochem Biophys Res Commun 224 (2), 289-296 (1996)
   PUBMED   8702385
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Zolnierowicz,S., Van Hoof,C., Andjelkovic,N., Cron,P., Stevens,I.,
            Merlevede,W., Goris,J. and Hemmings,B.A.
  TITLE     The variable subunit associated with protein phosphatase 2A0
            defines a novel multimember family of regulatory subunits
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 187-194 (1996)
   PUBMED   8694763
REFERENCE   10 (residues 1 to 486)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL451060.13 and L42373.1.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes an alpha isoform of the regulatory subunit B56 subfamily.
            Alternative transcript variants encoding distinct isoforms have
            been found for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110883.1, L42373.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261461.7/ ENSP00000261461.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..486
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit alpha isoform isoform 1"
                     /note="PR61alpha; protein phosphatase 2 regulatory subunit
                     B', alpha"
                     /calculated_mol_wt=56063
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15172.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15172.1)"
     Region          64..442
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..486
                     /gene="PPP2R5A"
                     /gene_synonym="B56A; B56alpha; PR61A"
                     /coded_by="NM_006243.4:702..2162"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1503.1"
                     /db_xref="GeneID:5525"
                     /db_xref="HGNC:HGNC:9309"
                     /db_xref="MIM:601643"
ORIGIN      
        1 mssssppaga asaaisasek vdgftrksvr kaqrqkrsqg ssqfrsqgsq aelhplpqlk
       61 datsneqqel fcqklqqcci lfdfmdsvsd lkskeikrat lnelveyvst nrgvivesay
      121 sdivkmisan ifrtlppsdn pdfdpeedep tleaswphiq lvyefflrfl espdfqpsia
      181 kryidqkfvq qllelfdsed prerdflktv lhriygkflg lrafirkqin niflrfiyet
      241 ehfngvaell eilgsiingf alplkaehkq flmkvlipmh takglalfha qlaycvvqfl
      301 ekdttltepv irgllkfwpk tcsqkevmfl geieeildvi eptqfkkiee plfkqiskcv
      361 ssshfqvaer alyfwnneyi lslieenidk ilpimfasly kiskehwnpt ivalvynvlk
      421 tlmemngklf ddltssykae rqrekkkele reelwkklee lklkkalekq nsaynmhsil
      481 sntsae
//
LOCUS       NP_004243                358 aa            linear   PRI 20-NOV-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF1 [Homo sapiens].
ACCESSION   NP_004243
VERSION     NP_004243.1
DBSOURCE    REFSEQ: accession NM_004252.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Marini,F., Giusti,F., Marasco,E., Xumerle,L., Kwiatkowska,K.M.,
            Garagnani,P., Biver,E., Ferrari,S., Iolascon,G., Iantomasi,T. and
            Brandi,M.L.
  TITLE     High frequency of heterozygous rare variants of the SLC34A1 and
            SLC9A3R1 genes in patients with atypical femur fracture
  JOURNAL   Eur J Endocrinol 188 (1) (2023)
   PUBMED   36762943
  REMARK    GeneRIF: High frequency of heterozygous rare variants of the
            SLC34A1 and SLC9A3R1 genes in patients with atypical femur
            fracture.
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Wang,S., Raab,R.W., Schatz,P.J., Guggino,W.B. and Li,M.
  TITLE     Peptide binding consensus of the NHE-RF-PDZ1 domain matches the
            C-terminal sequence of cystic fibrosis transmembrane conductance
            regulator (CFTR)
  JOURNAL   FEBS Lett 427 (1), 103-108 (1998)
   PUBMED   9613608
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Hall,R.A., Premont,R.T., Chow,C.W., Blitzer,J.T., Pitcher,J.A.,
            Claing,A., Stoffel,R.H., Barak,L.S., Shenolikar,S., Weinman,E.J.,
            Grinstein,S. and Lefkowitz,R.J.
  TITLE     The beta2-adrenergic receptor interacts with the Na+/H+-exchanger
            regulatory factor to control Na+/H+ exchange
  JOURNAL   Nature 392 (6676), 626-630 (1998)
   PUBMED   9560162
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Murthy,A., Gonzalez-Agosti,C., Cordero,E., Pinney,D., Candia,C.,
            Solomon,F., Gusella,J. and Ramesh,V.
  TITLE     NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common
            interactor for merlin and ERM (MERM) proteins
  JOURNAL   J Biol Chem 273 (3), 1273-1276 (1998)
   PUBMED   9430655
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Reczek,D., Berryman,M. and Bretscher,A.
  TITLE     Identification of EBP50: A PDZ-containing phosphoprotein that
            associates with members of the ezrin-radixin-moesin family
  JOURNAL   J Cell Biol 139 (1), 169-179 (1997)
   PUBMED   9314537
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Yun,C.H., Oh,S., Zizak,M., Steplock,D., Tsao,S., Tse,C.M.,
            Weinman,E.J. and Donowitz,M.
  TITLE     cAMP-mediated inhibition of the epithelial brush border Na+/H+
            exchanger, NHE3, requires an associated regulatory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3010-3015 (1997)
   PUBMED   9096337
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1997 Sep 2;94(18):10006]
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Weinman,E.J., Steplock,D., Wang,Y. and Shenolikar,S.
  TITLE     Characterization of a protein cofactor that mediates protein kinase
            A regulation of the renal brush border membrane Na(+)-H+ exchanger
  JOURNAL   J Clin Invest 95 (5), 2143-2149 (1995)
   PUBMED   7738182
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX761192.1 and BC053350.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a sodium/hydrogen exchanger regulatory
            cofactor. The protein interacts with and regulates various proteins
            including the cystic fibrosis transmembrane conductance regulator
            and G-protein coupled receptors such as the beta2-adrenergic
            receptor and the parathyroid hormone 1 receptor. The protein also
            interacts with proteins that function as linkers between integral
            membrane and cytoskeletal proteins. The protein localizes to
            actin-rich structures including membrane ruffles, microvilli, and
            filopodia. Mutations in this gene result in hypophosphatemic
            nephrolithiasis/osteoporosis type 2, and loss of heterozygosity of
            this gene is implicated in breast cancer.[provided by RefSeq, Sep
            2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1081478.1,
                                           SRR3476690.1085605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262613.10/ ENSP00000262613.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..358
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF1"
                     /note="Na+/H+ exchange regulatory co-factor;
                     ezrin-radixin-moesin binding phosphoprotein-50; regulatory
                     cofactor of Na(+)/H(+) exchanger; SLC9A3 regulator 1;
                     solute carrier family 9, subfamily A (NHE3, cation proton
                     antiporter 3), member 3 regulator 1; Na(+)/H(+) exchange
                     regulatory cofactor 1"
                     /calculated_mol_wt=38737
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O14745.4)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Region          13..92
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(23..29,40,43,72,76,79..80)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Region          114..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14745.4)"
     Region          153..232
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            order(163..169,180,183,212,216,219..220)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          235..358
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Region          277..358
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14745.4)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q28619; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70441; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P70441; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70441; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70441; propagated from
                     UniProtKB/Swiss-Prot (O14745.4)"
     CDS             1..358
                     /gene="NHERF1"
                     /gene_synonym="EBP50; NHE-RF; NHERF; NHERF-1; NPHLOP2;
                     SLC9A3R1"
                     /coded_by="NM_004252.5:220..1296"
                     /db_xref="CCDS:CCDS11705.1"
                     /db_xref="GeneID:9368"
                     /db_xref="HGNC:HGNC:11075"
                     /db_xref="MIM:604990"
ORIGIN      
        1 msadaaagap lprlcclekg pngygfhlhg ekgklgqyir lvepgspaek agllagdrlv
       61 evngenveke thqqvvsrir aalnavrllv vdpetdeqlq klgvqvreel lraqeapgqa
      121 eppaaaevqg agneneprea dkshpeqrel rprlctmkkg psgygfnlhs dkskpgqfir
      181 svdpdspaea sglraqdriv evngvcmegk qhgdvvsair aggdetkllv vdretdeffk
      241 kcrvipsqeh lngplpvpft ngeiqkensr ealaeaales prpalvrsas sdtseelnsq
      301 dsppkqdsta psstsssdpi ldfnislama kerahqkrss krapqmdwsk knelfsnl
//
LOCUS       NP_001316488             240 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial import inner membrane translocase subunit TIM50
            isoform 2 [Homo sapiens].
ACCESSION   NP_001316488 XP_016882961
VERSION     NP_001316488.1
DBSOURCE    REFSEQ: accession NM_001329559.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Crameri,J.J., Palmer,C.S., Stait,T., Jackson,T.D., Lynch,M.,
            Sinclair,A., Frajman,L.E., Compton,A.G., Coman,D., Thorburn,D.R.,
            Frazier,A.E. and Stojanovski,D.
  TITLE     Reduced Protein Import via TIM23 SORT Drives Disease Pathology in
            TIMM50-Associated Mitochondrial Disease
  JOURNAL   Mol Cell Biol 44 (6), 226-244 (2024)
   PUBMED   38828998
REFERENCE   2  (residues 1 to 240)
  AUTHORS   Iglesias-Martinez,L.F., Rauch,N., Wynne,K., McCann,B., Kolch,W. and
            Rauch,J.
  TITLE     Interactome dynamics of RAF1-BRAF kinase monomers and dimers
  JOURNAL   Sci Data 10 (1), 203 (2023)
   PUBMED   37045861
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Moudi,M., Vahidi Mehrjardi,M.Y., Hozhabri,H., Metanat,Z.,
            Kalantar,S.M., Taheri,M., Ghasemi,N. and Dehghani,M.
  TITLE     Novel variants underlying autosomal recessive neurodevelopmental
            disorders with intellectual disability in Iranian consanguineous
            families
  JOURNAL   J Clin Lab Anal 36 (2), e24241 (2022)
   PUBMED   35019165
  REMARK    GeneRIF: Novel variants underlying autosomal recessive
            neurodevelopmental disorders with intellectual disability in
            Iranian consanguineous families.
REFERENCE   4  (residues 1 to 240)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Metwally,E., Zhao,G., Wang,Q. and Zhang,Y.Q.
  TITLE     Ttm50 facilitates calpain activation by anchoring it to calcium
            stores and increasing its sensitivity to calcium
  JOURNAL   Cell Res 31 (4), 433-449 (2021)
   PUBMED   32848200
REFERENCE   6  (residues 1 to 240)
  AUTHORS   Guo,Y., Cheong,N., Zhang,Z., De Rose,R., Deng,Y., Farber,S.A.,
            Fernandes-Alnemri,T. and Alnemri,E.S.
  TITLE     Tim50, a component of the mitochondrial translocator, regulates
            mitochondrial integrity and cell death
  JOURNAL   J Biol Chem 279 (23), 24813-24825 (2004)
   PUBMED   15044455
  REMARK    GeneRIF: Tim50 is important for both mitochondrial function and
            early neuronal development
REFERENCE   7  (residues 1 to 240)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Yamamoto,H., Esaki,M., Kanamori,T., Tamura,Y., Nishikawa,Si. and
            Endo,T.
  TITLE     Tim50 is a subunit of the TIM23 complex that links protein
            translocation across the outer and inner mitochondrial membranes
  JOURNAL   Cell 111 (4), 519-528 (2002)
   PUBMED   12437925
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Bauer,M.F., Gempel,K., Reichert,A.S., Rappold,G.A., Lichtner,P.,
            Gerbitz,K.D., Neupert,W., Brunner,M. and Hofmann,S.
  TITLE     Genetic and structural characterization of the human mitochondrial
            inner membrane translocase
  JOURNAL   J Mol Biol 289 (1), 69-82 (1999)
   PUBMED   10339406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC121146.1, BC050082.1,
            AC011500.7 and BC014674.1.
            
            On Jul 19, 2016 this sequence version replaced XP_016882961.1.
            
            Summary: This gene encodes a subunit of the TIM23 inner
            mitochondrial membrane translocase complex. The encoded protein
            functions as the receptor subunit that recognizes the mitochondrial
            targeting signal, or presequence, on protein cargo that is destined
            for the mitochondrial inner membrane and matrix. This protein may
            also play a role in maintaining the membrane permeability barrier,
            and knockdown of this gene in human cells results in the release of
            cytochrome c and apoptosis. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, uses a
            downstream translation start site and lacks an alternate in-frame
            exon in its 5' coding region compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC121146.1, AY444561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..240
                     /product="mitochondrial import inner membrane translocase
                     subunit TIM50 isoform 2"
                     /note="homolog of yeast Tim50; Tim50-like protein;
                     mitochondrial import inner membrane translocase subunit
                     TIM50"
                     /calculated_mol_wt=27448
     Region          34..149
                     /region_name="HAD_FCP1-like"
                     /note="human CTD phosphatase subunit 1 (CTDP1/FCP1) and
                     related proteins; belongs to the haloacid
                     dehalogenase-like superfamily; cd07521"
                     /db_xref="CDD:319823"
     Site            order(40..44,48..49,80..83,87,119,135..136,138..140)
                     /site_type="active"
                     /db_xref="CDD:319823"
     CDS             1..240
                     /gene="TIMM50"
                     /gene_synonym="MGCA9; TIM50; TIM50L"
                     /coded_by="NM_001329559.2:297..1019"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:92609"
                     /db_xref="HGNC:HGNC:23656"
                     /db_xref="MIM:607381"
ORIGIN      
        1 mvprflmsst mmiieptspc llpdplqepy yqppytlvle ltgvllhpew slatgwrfkk
       61 rpgietlfqq laplyeivif tsetgmtafp lidsvdphgf isyrlfrdat rymdghhvkd
      121 isclnrdpar vvvvdckkea frlqpyngva lrpwdgnsdd rvlldlsafl ktialngved
      181 vrtvlehyal eddplaafkq rqsrleqeeq qrlaelsksn kqnlflgslt srlwprskqp
//
LOCUS       NP_788276                506 aa            linear   PRI 20-NOV-2025
DEFINITION  CDK5 regulatory subunit-associated protein 3 isoform b [Homo
            sapiens].
ACCESSION   NP_788276
VERSION     NP_788276.1
DBSOURCE    REFSEQ: accession NM_176096.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Zhuo,R., Zhang,Z., Chen,Y., Li,G., Du,S., Guo,X., Yang,R., Tao,Y.,
            Li,X., Fang,F., Xie,Y., Wu,D., Yang,Y., Yang,C., Yin,H., Qian,G.,
            Wang,H., Yu,J., Jia,S., Zhu,F., Feng,C., Wang,J., Xu,Y., Li,Z.,
            Shi,L., Wang,X., Pan,J. and Wang,J.
  TITLE     CDK5RAP3 is a novel super-enhancer-driven gene activated by master
            TFs and regulates ER-Phagy in neuroblastoma
  JOURNAL   Cancer Lett 591, 216882 (2024)
   PUBMED   38636893
  REMARK    GeneRIF: CDK5RAP3 is a novel super-enhancer-driven gene activated
            by master TFs and regulates ER-Phagy in neuroblastoma.
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Zhang,C., Du,F.H., Wang,R.X., Han,W.B., Lv,X., Zeng,L.H. and
            Chen,G.Q.
  TITLE     TSPAN6 reinforces the malignant progression of glioblastoma via
            interacting with CDK5RAP3 and regulating STAT3 signaling pathway
  JOURNAL   Int J Biol Sci 20 (7), 2440-2453 (2024)
   PUBMED   38725860
  REMARK    GeneRIF: TSPAN6 reinforces the malignant progression of
            glioblastoma via interacting with CDK5RAP3 and regulating STAT3
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Xie,Y.H., He,X.H., Tang,Y.T., Li,J.J., Pan,Z.M., Qin,W.X., Wan,D.F.
            and Gu,J.R.
  TITLE     Cloning and characterization of human IC53-2, a novel CDK5
            activator binding protein
  JOURNAL   Cell Res 13 (2), 83-91 (2003)
   PUBMED   12737517
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Chen,J., Liu,B., Liu,Y., Han,Y., Yu,H., Zhang,Y., Lu,L., Zhen,Y.
            and Hui,R.
  TITLE     A novel gene IC53 stimulates ECV304 cell proliferation and is
            upregulated in failing heart
  JOURNAL   Biochem Biophys Res Commun 294 (1), 161-166 (2002)
   PUBMED   12054757
  REMARK    GeneRIF: IC53 is a novel gene, mainly expressed in vascular
            endothelial cells and mediates cell proliferation
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Ching,Y.P., Pang,A.S., Lam,W.H., Qi,R.Z. and Wang,J.H.
  TITLE     Identification of a neuronal Cdk5 activator-binding protein as Cdk5
            inhibitor
  JOURNAL   J Biol Chem 277 (18), 15237-15240 (2002)
   PUBMED   11882646
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Wang,X., Ching,Y.P., Lam,W.H., Qi,Z., Zhang,M. and Wang,J.H.
  TITLE     Identification of a common protein association region in the
            neuronal Cdk5 activator
  JOURNAL   J Biol Chem 275 (41), 31763-31769 (2000)
   PUBMED   10915792
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Ching,Y.P., Qi,Z. and Wang,J.H.
  TITLE     Cloning of three novel neuronal Cdk5 activator binding proteins
  JOURNAL   Gene 242 (1-2), 285-294 (2000)
   PUBMED   10721722
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Shirabe,K., Yubisui,T., Borgese,N., Tang,C.Y., Hultquist,D.E. and
            Takeshita,M.
  TITLE     Enzymatic instability of NADH-cytochrome b5 reductase as a cause of
            hereditary methemoglobinemia type I (red cell type)
  JOURNAL   J Biol Chem 267 (28), 20416-20421 (1992)
   PUBMED   1400360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK023722.1 and AA427702.1.
            
            Summary: This gene encodes a protein that has been reported to
            function in signaling pathways governing transcriptional regulation
            and cell cycle progression. It may play a role in tumorigenesis and
            metastasis. A pseudogene of this gene is located on the long arm of
            chromosome 20. Alternative splicing results in multiple transcript
            variants that encode different isoforms. [provided by RefSeq, May
            2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and has
            multiple coding region differences compared to variant 1. These
            differences cause translation initiation at an alternate AUG and
            result in an isoform (b) with a longer N-terminus, compared to
            isoform e.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.158098.1,
                                           SRR3476690.1032021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338399.9/ ENSP00000344683.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..506
                     /product="CDK5 regulatory subunit-associated protein 3
                     isoform b"
                     /note="ischemic heart CDK5 activator-binding protein C53;
                     LXXLL/leucine-zipper-containing ARFbinding protein; CDK5
                     regulatory subunit associated protein IC53-2;
                     LXXLL/leucine-zipper-containing ARF-binding protein"
                     /calculated_mol_wt=56790
     Region          4..503
                     /region_name="CDK5RAP3"
                     /note="CDK5 regulatory subunit-associated protein 3;
                     pfam05600"
                     /db_xref="CDD:461688"
     Region          267..270
                     /region_name="Shuffled ATG8-binding motif 1.
                     /evidence=ECO:0000269|PubMed:32851973,
                     ECO:0000269|PubMed:36762703"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB5.2)"
     Region          269..506
                     /region_name="Required for interaction with UFL1 and
                     mediates interaction with CHEK1.
                     /evidence=ECO:0000269|PubMed:19223857,
                     ECO:0000269|PubMed:20228063"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB5.2)"
     Region          292..295
                     /region_name="Shuffled ATG8-binding motif 2.
                     /evidence=ECO:0000269|PubMed:32851973,
                     ECO:0000269|PubMed:36762703"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB5.2)"
     Region          310..313
                     /region_name="Shuffled ATG8-binding motif 3.
                     /evidence=ECO:0000269|PubMed:32851973,
                     ECO:0000269|PubMed:36762703"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB5.2)"
     Region          355..370
                     /region_name="RPL10a-binding domain (RBD).
                     /evidence=ECO:0000269|PubMed:38383789"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JB5.2)"
     CDS             1..506
                     /gene="CDK5RAP3"
                     /gene_synonym="C53; HSF-27; IC53; LZAP; MST016;
                     OK/SW-cl.114; PP1553"
                     /coded_by="NM_176096.3:35..1555"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42356.1"
                     /db_xref="GeneID:80279"
                     /db_xref="HGNC:HGNC:18673"
                     /db_xref="MIM:608202"
ORIGIN      
        1 medhqhvpid iqtsklldwl vdrrhcslkw qslvltirek inaaiqdmpe seeiaqllsg
       61 syihyfhclr ildllkgtea stknifgrys sqrmkdwqei ialyekdnty lvelssllvr
      121 nvnyeipslk kqiakcqqlq qeysrkeeec qagaaemreq fyhsckqygi tgenvrgell
      181 alvkdlpsql aeigaaaqqs lgeaidvyqa svgfvcespt eqvlpmlrfv qkrgnstvye
      241 wrtgtepsvv erphleelpe qvaedaidwg dfgveavseg tdsgisaeaa gidwgifpes
      301 dskdpggdgi dwgddavalq itvleagtqa pegvargpda ltlleytetr nqfldelmel
      361 eiflaqrave lseeadvlsv sqfqlapail qgqtkekmvt mvsvledlig kltslqlqhl
      421 fmilaspryv drvteflqqk lkqsqllalk kelmvqkqqe aleeqaalep kldlllektk
      481 elqklieadi skrysgrpvn lmgtsl
//
LOCUS       NP_001290366             286 aa            linear   PRI 20-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290366
VERSION     NP_001290366.1
DBSOURCE    REFSEQ: accession NM_001303437.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP398345.1, AW340131.1,
            DB160394.1, HY007091.1, BP209696.1, AK056946.1 and CA312679.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY007091.1, T10199.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303437.1:1268..2128"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_001096137             261 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-4 isoform 1 [Homo sapiens].
ACCESSION   NP_001096137
VERSION     NP_001096137.1
DBSOURCE    REFSEQ: accession NM_001102667.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Bai,Y., Zheng,J., Cheng,L., Liu,Q., Zhao,G., Li,J., Gu,Y., Xu,W.,
            Wang,M., Wei,Q. and Zhang,R.
  TITLE     Potentially functional genetic variants of VAV2 and PSMA4 in the
            immune-activation pathway and non-small cell lung cancer survival
  JOURNAL   J Gene Med 24 (10), e3447 (2022)
   PUBMED   36039727
  REMARK    GeneRIF: Potentially functional genetic variants of VAV2 and PSMA4
            in the immune-activation pathway and non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Palmer,A., Rivett,A.J., Thomson,S., Hendil,K.B., Butcher,G.W.,
            Fuertes,G. and Knecht,E.
  TITLE     Subpopulations of proteasomes in rat liver nuclei, microsomes and
            cytosol
  JOURNAL   Biochem J 316 (Pt 2) (Pt 2), 401-407 (1996)
   PUBMED   8687380
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Castano,J.G., Mahillo,E., Arizti,P. and Arribas,J.
  TITLE     Phosphorylation of C8 and C9 subunits of the multicatalytic
            proteinase by casein kinase II and identification of the C8
            phosphorylation sites by direct mutagenesis
  JOURNAL   Biochemistry 35 (12), 3782-3789 (1996)
   PUBMED   8619999
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Arribas,J., Arizti,P. and Castano,J.G.
  TITLE     Antibodies against the C2 COOH-terminal region discriminate the
            active and latent forms of the multicatalytic proteinase complex
  JOURNAL   J Biol Chem 269 (17), 12858-12864 (1994)
   PUBMED   8175701
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Tamura,T., Lee,D.H., Osaka,F., Fujiwara,T., Shin,S., Chung,C.H.,
            Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning and sequence analysis of cDNAs for five major
            subunits of human proteasomes (multi-catalytic proteinase
            complexes)
  JOURNAL   Biochim Biophys Acta 1089 (1), 95-102 (1991)
   PUBMED   2025653
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG528289.1, BU930105.1,
            BG616186.1, CD365826.1 and BG208993.1.
            
            Summary: This gene encodes a core alpha subunit of the 20S
            proteosome, which is a highly ordered ring-shaped structure
            composed of four rings of 28 non-identical subunits. Proteasomes
            cleave peptides in an ATP- and ubiquitin-dependent manner.
            [provided by RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.135415.1,
                                           SRR1163655.116428.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..261
                     /product="proteasome subunit alpha type-4 isoform 1"
                     /EC_number="3.4.25.1"
                     /note="proteasome component C9; proteasome subunit HC9;
                     proteasome subunit L; macropain subunit C9; alpha-3;
                     multicatalytic endopeptidase complex subunit C9;
                     proteasome subunit alpha type-4; proteasome (prosome,
                     macropain) subunit, alpha type, 4; proteasome subunit
                     alpha 4; proteasome subunit alpha3; proteasome subunit
                     alpha-3"
                     /calculated_mol_wt=29353
     Region          3..216
                     /region_name="proteasome_alpha_type_4"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03752"
                     /db_xref="CDD:239721"
     Site            order(7..10,12..13,15..16,20,23,26..27,30,38,53,55..56,
                     80..82,84..85,116,119,122..123,126..130,148,153..154,156,
                     158..159,161)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239721"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25789.1)"
     Site            order(32,48,50,64,166)
                     /site_type="active"
                     /db_xref="CDD:239721"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17323924; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     Site            176
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P25789.1)"
     Region          240..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25789.1)"
     CDS             1..261
                     /gene="PSMA4"
                     /gene_synonym="HC9; HsT17706; PSC9"
                     /coded_by="NM_001102667.2:83..868"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10303.1"
                     /db_xref="GeneID:5685"
                     /db_xref="HGNC:HGNC:9533"
                     /db_xref="MIM:176846"
ORIGIN      
        1 msrrydsrtt ifspegrlyq veyameaigh agtclgilan dgvllaaerr nihklldevf
       61 fsekiyklne dmacsvagit sdanvltnel rliaqryllq yqepipceql vtalcdikqa
      121 ytqfggkrpf gvsllyigwd khygfqlyqs dpsgnyggwk atcignnsaa avsmlkqdyk
      181 egemtlksal alaikvlnkt mdvsklsaek veiatltren gktvirvlkq keveqlikkh
      241 eeeeakaere kkekeqkekd k
//
LOCUS       NP_001290472             233 aa            linear   PRI 20-NOV-2025
DEFINITION  prefoldin subunit 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001290472
VERSION     NP_001290472.1
DBSOURCE    REFSEQ: accession NM_001303543.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Miao,H., Gao,W., Zhong,L., Li,H., Chen,D., Xu,C., Wen,Z. and
            Chen,Y.
  TITLE     VBP1 promotes tumor proliferation as a part of the hypoxia-related
            signature in esophageal squamous cell carcinoma
  JOURNAL   Hum Cell 37 (4), 1141-1155 (2024)
   PUBMED   38700744
  REMARK    GeneRIF: VBP1 promotes tumor proliferation as a part of the
            hypoxia-related signature in esophageal squamous cell carcinoma.
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Clifford,S.C., Walsh,S., Hewson,K., Green,E.K., Brinke,A.,
            Green,P.M., Gianelli,F., Eng,C. and Maher,E.R.
  TITLE     Genomic organization and chromosomal localization of the human CUL2
            gene and the role of von Hippel-Lindau tumor suppressor-binding
            protein (CUL2 and VBP1) mutation and loss in renal-cell carcinoma
            development
  JOURNAL   Genes Chromosomes Cancer 26 (1), 20-28 (1999)
   PUBMED   10441001
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Hemberger,M., Himmelbauer,H., Neumann,H.P., Plate,K.H.,
            Schwarzkopf,G. and Fundele,R.
  TITLE     Expression of the von Hippel-Lindau-binding protein-1 (Vbp1) in
            fetal and adult mouse tissues
  JOURNAL   Hum Mol Genet 8 (2), 229-236 (1999)
   PUBMED   9931330
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Brinke,A., Green,P.M. and Giannelli,F.
  TITLE     Characterization of the gene (VBP1) and transcript for the von
            Hippel-Lindau binding protein and isolation of the highly conserved
            murine homologue
  JOURNAL   Genomics 45 (1), 105-112 (1997)
   PUBMED   9339366
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Tsuchiya,H., Iseda,T. and Hino,O.
  TITLE     Identification of a novel protein (VBP-1) binding to the von
            Hippel-Lindau (VHL) tumor suppressor gene product
  JOURNAL   Cancer Res 56 (13), 2881-2885 (1996)
   PUBMED   8674032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX682237.7, U96759.1,
            BC009570.1 and AA626259.1.
            
            Summary: The protein encoded by this gene interacts with the Von
            Hippel-Lindau protein to form an intracellular complex. The encoded
            protein functions as a chaperone protein, and may play a role in
            the transport of the Von Hippel-Lindau protein from the perinuclear
            granules to the nucleus or cytoplasm. Alternative splicing and the
            use of alternate transcription start sites results in multiple
            transcript variants encoding different protein isoforms. [provided
            by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (2) initiates transcription at an
            alternate position and has a longer 5' terminal exon than variant
            1. It initiates translation at an alternate start codon and the
            encoded isoform (2) has a longer N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U96759.1, SRR1660809.91031.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..233
                     /product="prefoldin subunit 3 isoform 2"
                     /note="prefoldin subunit 3; von Hippel-Lindau binding
                     protein 1"
                     /calculated_mol_wt=26404
     Region          88..216
                     /region_name="Prefoldin_3"
                     /note="Prefoldin subunit 3; cd23156"
                     /db_xref="CDD:467472"
     Region          88..127
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467472"
     Site            order(89,92..93,96,200,203..204,206..208,210..211)
                     /site_type="other"
                     /note="prefoldin/TRiC interface [polypeptide binding]"
                     /db_xref="CDD:467472"
     Site            order(116,119..120,123..124,126..127,137..144,146..155,
                     158..162,166..171,180)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467472"
     Region          174..216
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467472"
     CDS             1..233
                     /gene="VBP1"
                     /gene_synonym="HIBBJ46; PFD3; PFDN3; VBP-1"
                     /coded_by="NM_001303543.1:103..804"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:7411"
                     /db_xref="HGNC:HGNC:12662"
                     /db_xref="MIM:300133"
ORIGIN      
        1 mnvhgdgeag lqvrtsqsrn pggrrpgrqs raripkmaav kdscgkgema tgngrrlhlg
       61 ipeavfvedv dsfmkqpgne tadtvlkkld eqyqkykfme lnlaqkkrrl kgqipeikqt
      121 leilkymqkk kestnsmetr flladnlyck asvpptdkvc lwlganvmle ydideaqall
      181 eknlstatkn ldsleedldf lrdqftttev nmarvynwdv krrnkddstk nka
//
LOCUS       NP_001180202             410 aa            linear   PRI 20-NOV-2025
DEFINITION  retinoblastoma-binding protein 5 isoform 3 [Homo sapiens].
ACCESSION   NP_001180202
VERSION     NP_001180202.1
DBSOURCE    REFSEQ: accession NM_001193273.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Patel,A., Dharmarajan,V., Vought,V.E. and Cosgrove,M.S.
  TITLE     On the mechanism of multiple lysine methylation by the human mixed
            lineage leukemia protein-1 (MLL1) core complex
  JOURNAL   J Biol Chem 284 (36), 24242-24256 (2009)
   PUBMED   19556245
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Southall,S.M., Wong,P.S., Odho,Z., Roe,S.M. and Wilson,J.R.
  TITLE     Structural basis for the requirement of additional factors for MLL1
            SET domain activity and recognition of epigenetic marks
  JOURNAL   Mol Cell 33 (2), 181-191 (2009)
   PUBMED   19187761
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Scacheri,P.C., Davis,S., Odom,D.T., Crawford,G.E., Perkins,S.,
            Halawi,M.J., Agarwal,S.K., Marx,S.J., Spiegel,A.M., Meltzer,P.S.
            and Collins,F.S.
  TITLE     Genome-wide analysis of menin binding provides insights into MEN1
            tumorigenesis
  JOURNAL   PLoS Genet 2 (4), e51 (2006)
   PUBMED   16604156
  REMARK    GeneRIF: analysis of menin's role as a tumor suppressor and binding
            sites of Rbbp5 and MLL1
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Saijo,M., Sakai,Y., Kishino,T., Niikawa,N., Matsuura,Y., Morino,K.,
            Tamai,K. and Taya,Y.
  TITLE     Molecular cloning of a human protein that binds to the
            retinoblastoma protein and chromosomal mapping
  JOURNAL   Genomics 27 (3), 511-519 (1995)
   PUBMED   7558034
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA797022.1, AK296978.1,
            BC075059.2, AL583832.14 and BQ020418.1.
            
            Summary: This gene encodes a ubiquitously expressed nuclear protein
            which belongs to a highly conserved subfamily of WD-repeat
            proteins. The encoded protein binds directly to retinoblastoma
            protein, which regulates cell proliferation. It interacts
            preferentially with the underphosphorylated retinoblastoma protein
            via the E1A-binding pocket B. Three alternatively spliced
            transcript variants that encode different protein isoforms have
            been described for this gene. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (3) uses two different splice
            sites in the coding region which results in the use of a downstream
            start codon, compared to variant 1. The resulting protein (isoform
            3) is shorter when it is compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296978.1, SRR14038193.1468714.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..410
                     /product="retinoblastoma-binding protein 5 isoform 3"
                     /note="SWD1, Set1c WD40 repeat protein, homolog; RBBP-5;
                     retinoblastoma-binding protein RBQ-3;
                     retinoblastoma-binding protein 5"
                     /calculated_mol_wt=44687
     Region          <30..194
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          75..120
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          125..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..410
                     /gene="RBBP5"
                     /gene_synonym="RBQ3; SWD1"
                     /coded_by="NM_001193273.2:431..1663"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5929"
                     /db_xref="HGNC:HGNC:9888"
                     /db_xref="MIM:600697"
ORIGIN      
        1 mksapvmltl sdskhvvlpv dddsdlnvva sfdrrgeyiy tgnakgkilv lktdsqdlva
       61 sfrvttgtsn ttaiksiefa rkgscflint adriirvydg reiltcgrdg epepmqklqd
      121 lvnrtpwkkc cfsgdgeyiv agsarqhaly iweksignlv kilhgtrgel lldvawhpvr
      181 piiasissgv vsiwaqnqve nwsafapdfk eldenveyee resefdiede dksepeqtga
      241 daaedeevdv tsvdpiaafc ssdeeledsk allylpiape vedpeenpyg pppdavqtsl
      301 mdegassekk rqssadgsqp pkkkpkttni elqgvpndev hpllgvkgdg kskkkqagrp
      361 kgskgkekds pfkpklykgd rglplegsak gkvqaelsqp ltggaisell
//
LOCUS       NP_002938                121 aa            linear   PRI 20-NOV-2025
DEFINITION  replication protein A 14 kDa subunit [Homo sapiens].
ACCESSION   NP_002938 XP_005249878
VERSION     NP_002938.1
DBSOURCE    REFSEQ: accession NM_002947.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Liang,L., Zhao,Z., Jin,Q., Zhang,S., Zhao,Z. and Li,X.
  TITLE     RPA3 promotes the proliferation, migration, and invasion of gliomas
            by activating the PI3K-AKT-mTOR pathway
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (5), 80-86 (2023)
   PUBMED   37571896
  REMARK    GeneRIF: RPA3 promotes the proliferation, migration, and invasion
            of gliomas by activating the PI3K-AKT-mTOR pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Chen,L., Hu,K., Liu,Y., Liu,L., Tang,J. and Qin,X.
  TITLE     Knockdown of replication protein A 3 induces protective autophagy
            and enhances cisplatin sensitivity in lung adenocarcinoma by
            inhibiting AKT/mTOR signaling via binding to cyclin-dependent
            kinases regulatory subunit 2
  JOURNAL   Drug Dev Res 83 (7), 1589-1599 (2022)
   PUBMED   35903032
  REMARK    GeneRIF: Knockdown of replication protein A 3 induces protective
            autophagy and enhances cisplatin sensitivity in lung adenocarcinoma
            by inhibiting AKT/mTOR signaling via binding to cyclin-dependent
            kinases regulatory subunit 2.
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Sun,D., Zhang,K., Fu,Q., Zhang,H., Liu,S., Wang,H., Xu,Z. and
            Wang,J.
  TITLE     Overexpression of replication protein A3 is associated with
            unfavorable outcome in bladder urothelial carcinoma
  JOURNAL   J Cancer Res Ther 17 (3), 771-776 (2021)
   PUBMED   34269312
  REMARK    GeneRIF: Overexpression of replication protein A3 is associated
            with unfavorable outcome in bladder urothelial carcinoma.
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Keshav,K.F., Chen,C. and Dutta,A.
  TITLE     Rpa4, a homolog of the 34-kilodalton subunit of the replication
            protein A complex
  JOURNAL   Mol Cell Biol 15 (6), 3119-3128 (1995)
   PUBMED   7760808
REFERENCE   7  (residues 1 to 121)
  AUTHORS   He,Z., Henricksen,L.A., Wold,M.S. and Ingles,C.J.
  TITLE     RPA involvement in the damage-recognition and incision steps of
            nucleotide excision repair
  JOURNAL   Nature 374 (6522), 566-569 (1995)
   PUBMED   7700386
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Umbricht,C.B., Griffin,C.A., Hawkins,A.L., Grzeschik,K.H.,
            O'Connell,P., Leach,R., Green,E.D. and Kelly,T.J.
  TITLE     High-resolution genomic mapping of the three human replication
            protein A genes (RPA1, RPA2, and RPA3)
  JOURNAL   Genomics 20 (2), 249-257 (1994)
   PUBMED   8020972
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Umbricht,C.B., Erdile,L.F., Jabs,E.W. and Kelly,T.J.
  TITLE     Cloning, overexpression, and genomic mapping of the 14-kDa subunit
            of human replication protein A
  JOURNAL   J Biol Chem 268 (9), 6131-6138 (1993)
   PUBMED   8454588
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Kenny,M.K., Schlegel,U., Furneaux,H. and Hurwitz,J.
  TITLE     The role of human single-stranded DNA binding protein and its
            individual subunits in simian virus 40 DNA replication
  JOURNAL   J Biol Chem 265 (13), 7693-7700 (1990)
   PUBMED   2159011
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC009868.2, AC004948.2 and AI243725.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005249878.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009868.2 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968540,
                                           SAMEA2142348 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223129.8/ ENSP00000223129.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.3"
     Protein         1..121
                     /product="replication protein A 14 kDa subunit"
                     /note="RF-A protein 3; replication factor A protein 3;
                     replication protein A3, 14kDa"
                     /calculated_mol_wt=13438
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylvaline.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P35244.1)"
     Region          5..113
                     /region_name="Rep_fac-A_3"
                     /note="Replication factor A protein 3; pfam08661"
                     /db_xref="CDD:462551"
     CDS             1..121
                     /gene="RPA3"
                     /gene_synonym="REPA3; RP-A p14"
                     /coded_by="NM_002947.5:1173..1538"
                     /db_xref="CCDS:CCDS5356.1"
                     /db_xref="GeneID:6119"
                     /db_xref="HGNC:HGNC:10291"
                     /db_xref="MIM:179837"
ORIGIN      
        1 mvdmmdlprs rinagmlaqf idkpvcfvgr lekihptgkm filsdgegkn gtielmepld
       61 eeisgivevv grvtakatil ctsyvqfked shpfdlglyn eavkiihdfp qfyplgivqh
      121 d
//
LOCUS       NP_002622                483 aa            linear   PRI 20-NOV-2025
DEFINITION  6-phosphogluconate dehydrogenase, decarboxylating isoform 1 [Homo
            sapiens].
ACCESSION   NP_002622
VERSION     NP_002622.2
DBSOURCE    REFSEQ: accession NM_002631.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Wu,J., Chen,Y., Zou,H., Xu,K., Hou,J., Wang,M., Tian,S., Gao,M.,
            Ren,Q., Sun,C., Lu,S., Wang,Q., Shu,Y., Wang,S. and Wang,X.
  TITLE     6-Phosphogluconate dehydrogenase promotes glycolysis and fatty acid
            synthesis by inhibiting the AMPK pathway in lung adenocarcinoma
            cells
  JOURNAL   Cancer Lett 601, 217177 (2024)
   PUBMED   39179096
  REMARK    GeneRIF: 6-Phosphogluconate dehydrogenase promotes glycolysis and
            fatty acid synthesis by inhibiting the AMPK pathway in lung
            adenocarcinoma cells.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Qiao,R., Wei,M., Chen,H., Zhang,X., Zhang,J., Gao,L., Ma,H.,
            Wang,Y. and Li,L.
  TITLE     Critical Role of 6-Phosphogluconate Dehydrogenase in TAp73-Mediated
            Cancer Cell Proliferation
  JOURNAL   Mol Cancer Res 21 (8), 825-835 (2023)
   PUBMED   37071129
  REMARK    GeneRIF: Critical Role of 6-Phosphogluconate Dehydrogenase in
            TAp73-Mediated Cancer Cell Proliferation.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Cao,J., Sun,X., Zhang,X. and Chen,D.
  TITLE     6PGD Upregulation is Associated with Chemo- and Immuno-Resistance
            of Renal Cell Carcinoma via AMPK Signaling-Dependent NADPH-Mediated
            Metabolic Reprograming
  JOURNAL   Am J Med Sci 360 (3), 279-286 (2020)
   PUBMED   32829780
  REMARK    GeneRIF: 6PGD Upregulation is Associated with Chemo- and
            Immuno-Resistance of Renal Cell Carcinoma via AMPK
            Signaling-Dependent NADPH-Mediated Metabolic Reprograming.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Xu,K., He,Z., Chen,M., Wang,N., Zhang,D., Yang,L., Xu,Z. and Xu,H.
  TITLE     HIF-1alpha regulates cellular metabolism, and Imatinib resistance
            by targeting phosphogluconate dehydrogenase in gastrointestinal
            stromal tumors
  JOURNAL   Cell Death Dis 11 (7), 586 (2020)
   PUBMED   32719331
  REMARK    GeneRIF: HIF-1alpha regulates cellular metabolism, and Imatinib
            resistance by targeting phosphogluconate dehydrogenase in
            gastrointestinal stromal tumors.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Gao,X., Zhao,L., Liu,S., Li,Y., Xia,S., Chen,D., Wang,M., Wu,S.,
            Dai,Q., Vu,H., Zacharias,L., DeBerardinis,R., Lim,E., Metallo,C.,
            Boggon,T.J., Lonial,S., Lin,R., Mao,H., Pan,Y., Shan,C. and Chen,J.
  TITLE     gamma-6-Phosphogluconolactone, a Byproduct of the Oxidative Pentose
            Phosphate Pathway, Contributes to AMPK Activation through
            Inhibition of PP2A
  JOURNAL   Mol Cell 76 (6), 857-871 (2019)
   PUBMED   31586547
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Komatsu,N., Kido,A., Kimura,Y. and Oya,M.
  TITLE     PGD phenotyping in bloodstains, organ tissues, dental pulps and
            hair roots by isoelectric focusing
  JOURNAL   Forensic Sci Int 48 (2), 185-194 (1990)
   PUBMED   2283141
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Beutler,E. and Kuhl,W.
  TITLE     Limiting role of 6-phosphogluconolactonase in erythrocyte hexose
            monophosphate pathway metabolism
  JOURNAL   J Lab Clin Med 106 (5), 573-577 (1985)
   PUBMED   3932573
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Beutler,E., Kuhl,W. and Gelbart,T.
  TITLE     6-Phosphogluconolactonase deficiency, a hereditary erythrocyte
            enzyme deficiency: possible interaction with glucose-6-phosphate
            dehydrogenase deficiency
  JOURNAL   Proc Natl Acad Sci U S A 82 (11), 3876-3878 (1985)
   PUBMED   3858849
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Povey,S., Morton,N.E. and Sherman,S.L.
  TITLE     Report of the Committee on the Genetic Constitution of Chromosomes
            1 and 2
  JOURNAL   Cytogenet Cell Genet 40 (1-4), 67-106 (1985)
   PUBMED   3864603
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Douglas,G.R., McAlpine,P.J. and Hamerton,J.L.
  TITLE     Regional localization of loci for human PGM and 6PGD on human
            chromosome one by use of hybrids of Chinese hamster-human somatic
            cells
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2737-2740 (1973)
   PUBMED   4517931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY049516.1, BC000368.2,
            AL139424.21 and HY245069.1.
            
            On Dec 18, 2003 this sequence version replaced NP_002622.1.
            
            Summary: 6-phosphogluconate dehydrogenase is the second
            dehydrogenase in the pentose phosphate shunt. Deficiency of this
            enzyme is generally asymptomatic, and the inheritance of this
            disorder is autosomal dominant. Hemolysis results from combined
            deficiency of 6-phosphogluconate dehydrogenase and
            6-phosphogluconolactonase suggesting a synergism of the two
            enzymopathies. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.3268.1,
                                           SRR5189661.73809.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270776.13/ ENSP00000270776.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..483
                     /product="6-phosphogluconate dehydrogenase,
                     decarboxylating isoform 1"
                     /EC_number="1.1.1.44"
                     /note="6-phosphogluconate dehydrogenase, decarboxylating"
                     /calculated_mol_wt=53009
     Region          2..469
                     /region_name="Gnd"
                     /note="6-phosphogluconate dehydrogenase [Carbohydrate
                     transport and metabolism]; COG0362"
                     /db_xref="CDD:440131"
     Site            38
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCD0; propagated from
                     UniProtKB/Swiss-Prot (P52209.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCD0; propagated from
                     UniProtKB/Swiss-Prot (P52209.3)"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P52209.3)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCD0; propagated from
                     UniProtKB/Swiss-Prot (P52209.3)"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P52209.3)"
     CDS             1..483
                     /gene="PGD"
                     /gene_synonym="6PGD"
                     /coded_by="NM_002631.4:55..1506"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS113.1"
                     /db_xref="GeneID:5226"
                     /db_xref="HGNC:HGNC:8891"
                     /db_xref="MIM:172200"
ORIGIN      
        1 maqadialig lavmgqnlil nmndhgfvvc afnrtvskvd dflaneakgt kvvgaqslke
       61 mvsklkkprr iillvkagqa vddfieklvp lldtgdiiid ggnseyrdtt rrcrdlkakg
      121 ilfvgsgvsg geegarygps lmpggnkeaw phiktifqgi aakvgtgepc cdwvgdegag
      181 hfvkmvhngi eygdmqlice ayhlmkdvlg maqdemaqaf edwnktelds flieitanil
      241 kfqdtdgkhl lpkirdsagq kgtgkwtais aleygvpvtl igeavfarcl sslkderiqa
      301 skklkgpqkf qfdgdkksfl edirkalyas kiisyaqgfm llrqaatefg wtlnyggial
      361 mwrggciirs vflgkikdaf drnpelqnll lddffksave ncqdswrrav stgvqagipm
      421 pcfttalsfy dgyrhemlpa sliqaqrdyf gahtyellak pgqfihtnwt ghggtvssss
      481 yna
//
LOCUS       NP_002784                241 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-1 [Homo sapiens].
ACCESSION   NP_002784
VERSION     NP_002784.1
DBSOURCE    REFSEQ: accession NM_002793.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Munipalli,S.B. and Yenugu,S.
  TITLE     Uroplakin 1a Interacts with Regucalcin and Proteasome Subunit Beta
            1
  JOURNAL   Reprod Sci 30 (12), 3520-3528 (2023)
   PUBMED   37468792
  REMARK    GeneRIF: Uroplakin 1a Interacts with Regucalcin and Proteasome
            Subunit Beta 1.
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Hisamatsu,H. and Tanaka,K.
  TITLE     The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
            subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
            by fluorescence in situ hybridization
  JOURNAL   Genomics 27 (2), 377-379 (1995)
   PUBMED   7558012
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Tamura,T., Osaka,F., Kawamura,Y., Higuti,T., Ishida,N.,
            Nothwang,H.G., Tsurumi,C., Tanaka,K. and Ichihara,A.
  TITLE     Isolation and characterization of alpha-type HC3 and beta-type HC5
            subunit genes of human proteasomes
  JOURNAL   J Mol Biol 244 (1), 117-124 (1994)
   PUBMED   7966316
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Tamura,T., Lee,D.H., Osaka,F., Fujiwara,T., Shin,S., Chung,C.H.,
            Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning and sequence analysis of cDNAs for five major
            subunits of human proteasomes (multi-catalytic proteinase
            complexes)
  JOURNAL   Biochim Biophys Acta 1089 (1), 95-102 (1991)
   PUBMED   2025653
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Lee,L.W., Moomaw,C.R., Orth,K., McGuire,M.J., DeMartino,G.N. and
            Slaughter,C.A.
  TITLE     Relationships among the subunits of the high molecular weight
            proteinase, macropain (proteasome)
  JOURNAL   Biochim Biophys Acta 1037 (2), 178-185 (1990)
   PUBMED   2306472
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP369175.1, BC020807.1 and
            BQ685374.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. This gene is tightly
            linked to the TBP (TATA-binding protein) gene in human and in
            mouse, and is transcribed in the opposite orientation in both
            species. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.404183.1, HM005585.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153733, SAMEA2467144
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262193.7/ ENSP00000262193.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..241
                     /product="proteasome subunit beta type-1"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit HC5; beta-6; proteasome
                     component C5; macropain subunit C5; proteasome gamma
                     chain; multicatalytic endopeptidase complex subunit C5;
                     proteasome beta 1 subunit; proteasome (prosome, macropain)
                     subunit, beta type, 1; proteasome subunit beta 1;
                     proteasome subunit beta6; testicular secretory protein Li
                     45; proteasome subunit beta-6"
                     /calculated_mol_wt=26358
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Region          30..241
                     /region_name="proteasome_beta_type_1"
                     /note="proteasome beta type-1 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03757"
                     /db_xref="CDD:239726"
     Site            order(38,54,56,70,168,214,217..218)
                     /site_type="active"
                     /db_xref="CDD:239726"
     Site            order(56,59,61..66,86,88,103,115,118..119,121..122,125,
                     128,153,155,157..160,163,171..172,174..175,178..180,205,
                     212..215,218..219)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239726"
     Site            58
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P20618.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Site            68
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:O09061; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P20618.2)"
     Site            209
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P20618.2)"
     CDS             1..241
                     /gene="PSMB1"
                     /gene_synonym="HC5; NEDMHAL; PMSB1; PSC5"
                     /coded_by="NM_002793.4:66..791"
                     /db_xref="CCDS:CCDS34577.1"
                     /db_xref="GeneID:5689"
                     /db_xref="HGNC:HGNC:9537"
                     /db_xref="MIM:602017"
ORIGIN      
        1 mlsstamysa pgrdlgmeph raagplqlrf spyvfnggti laiagedfai vasdtrlseg
       61 fsihtrdspk cykltdktvi gcsgfhgdcl tltkiiearl kmykhsnnka mttgaiaaml
      121 stilysrrff pyyvyniigg ldeegkgavy sfdpvgsyqr dsfkaggsas amlqplldnq
      181 vgfknmqnve hvplsldram rlvkdvfisa aerdvytgda lricivtkeg ireetvslrk
      241 d
//
LOCUS       NP_112577                 86 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3B subunit 5 [Homo sapiens].
ACCESSION   NP_112577
VERSION     NP_112577.1
DBSOURCE    REFSEQ: accession NM_031287.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 86)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 86)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 86)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 86)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 86)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 86)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   7  (residues 1 to 86)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
REFERENCE   8  (residues 1 to 86)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   9  (residues 1 to 86)
  AUTHORS   Martinez,E., Palhan,V.B., Tjernberg,A., Lymar,E.S., Gamper,A.M.,
            Kundu,T.K., Chait,B.T. and Roeder,R.G.
  TITLE     Human STAGA complex is a chromatin-acetylating transcription
            coactivator that interacts with pre-mRNA splicing and DNA
            damage-binding factors in vivo
  JOURNAL   Mol Cell Biol 21 (20), 6782-6795 (2001)
   PUBMED   11564863
REFERENCE   10 (residues 1 to 86)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK074417.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: CD387862.1, BG706269.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367569.4/ ENSP00000356541.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..86
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..86
                     /product="splicing factor 3B subunit 5"
                     /note="pre-mRNA-splicing factor SF3b 10 kDa subunit;
                     splicing factor 3b, subunit 5, 10kDa"
                     /calculated_mol_wt=10004
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     Region          3..77
                     /region_name="SF3b10"
                     /note="Splicing factor 3B subunit 10 (SF3b10); pfam07189"
                     /db_xref="CDD:462114"
     Site            5
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:27720643; propagated from
                     UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     Region          15..76
                     /region_name="Interaction with SF3B1 and SF3B3.
                     /evidence=ECO:0000269|PubMed:27720643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     Site            20
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:27720643; propagated from
                     UniProtKB/Swiss-Prot (Q9BWJ5.1)"
     CDS             1..86
                     /gene="SF3B5"
                     /gene_synonym="SF3b10; Ysf3"
                     /coded_by="NM_031287.3:77..337"
                     /db_xref="CCDS:CCDS5204.1"
                     /db_xref="GeneID:83443"
                     /db_xref="HGNC:HGNC:21083"
                     /db_xref="MIM:617847"
ORIGIN      
        1 mtdrytihsq lehlqskyig tghadttkwe wlvnqhrdsy csymghfdll nyfaiaenes
       61 karvrfnlme kmlqpcgppa dkpeen
//
LOCUS       NP_001305790             180 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxyguanosine kinase, mitochondrial isoform d [Homo sapiens].
ACCESSION   NP_001305790 XP_005264231
VERSION     NP_001305790.1
DBSOURCE    REFSEQ: accession NM_001318861.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Guzman,H., Yazdani,S., Harmon,J.L., Chapman,K.A., Vitola,B.,
            Pyle,L., McKnight,H., Sigal,W., Lord,K., De Leon,D.D., Merchant,N.
            and Ganetzky,R.
  TITLE     Case report: Two unexpected cases of DGUOK-related mitochondrial
            DNA depletion syndrome presenting with hyperinsulinemic
            hypoglycemia
  JOURNAL   Front Endocrinol (Lausanne) 14, 1268135 (2023)
   PUBMED   38027095
  REMARK    GeneRIF: Case report: Two unexpected cases of DGUOK-related
            mitochondrial DNA depletion syndrome presenting with
            hyperinsulinemic hypoglycemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Unal,O., Hismi,B., Kilic,M., Gulsen,H.H., Coskun,T., Sivri,S.H.,
            Dursun,A., Yuce,A. and Tokatli,A.
  TITLE     Deoxyguanosine kinase deficiency: a report of four patients
  JOURNAL   J Pediatr Endocrinol Metab 30 (6), 697-702 (2017)
   PUBMED   28493820
  REMARK    GeneRIF: DGUOK deficiency and mutation is associated with
            mitochondrial DNA depletion syndromes.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Jullig,M. and Eriksson,S.
  TITLE     Mitochondrial and submitochondrial localization of human
            deoxyguanosine kinase
  JOURNAL   Eur J Biochem 267 (17), 5466-5472 (2000)
   PUBMED   10951205
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Johansson,M., Bajalica-Lagercrantz,S., Lagercrantz,J. and
            Karlsson,A.
  TITLE     Localization of the human deoxyguanosine kinase gene (DGUOK) to
            chromosome 2p13
  JOURNAL   Genomics 38 (3), 450-451 (1996)
   PUBMED   8975728
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Wang,L., Hellman,U. and Eriksson,S.
  TITLE     Cloning and expression of human mitochondrial deoxyguanosine kinase
            cDNA
  JOURNAL   FEBS Lett 390 (1), 39-43 (1996)
   PUBMED   8706825
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning and expression of human deoxyguanosine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7258-7262 (1996)
   PUBMED   8692979
REFERENCE   10 (residues 1 to 180)
  AUTHORS   El-Hattab,A.W. and Scaglia,F.
  TITLE     Deoxyguanosine Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU099795.1, AC073046.7,
            BG575800.1 and U41668.1.
            
            On Jan 14, 2016 this sequence version replaced XP_005264231.1.
            
            Summary: In mammalian cells, the phosphorylation of purine
            deoxyribonucleosides is mediated predominantly by two
            deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and
            mitochondrial deoxyguanosine kinase. The protein encoded by this
            gene is responsible for phosphorylation of purine
            deoxyribonucleosides in the mitochondrial matrix. In addition, this
            protein phosphorylates several purine deoxyribonucleoside analogs
            used in the treatment of lymphoproliferative disorders, and this
            phosphorylation is critical for the effectiveness of the analogs.
            Alternative splice variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) contains an alternate exon and
            lacks another alternate exon compared to variant 1. The resulting
            isoform (d) is shorter at the N-terminus compared to isoform a.
            Variants 4 and 5 both encode the same isoform (d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.297050.1,
                                           SRR1163658.234018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..180
                     /product="deoxyguanosine kinase, mitochondrial isoform d"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxyguanosine kinase, mitochondrial;
                     deoxyadenosine kinase, mitochondrial"
                     /calculated_mol_wt=21577
     Region          1..178
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            21
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..180
                     /gene="DGUOK"
                     /gene_synonym="dGK; MTDPS3; NCPH; NCPH1; PEOB4"
                     /coded_by="NM_001318861.2:296..838"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:1716"
                     /db_xref="HGNC:HGNC:2858"
                     /db_xref="MIM:601465"
ORIGIN      
        1 mmyreparws ytfqtfsfls rlkvqlepfp ekllqarkpv qifersvysd ryifaknlfe
       61 ngslsdiewh iyqdwhsfll wefasritlh gfiylqaspq vclkrlyqra reeekgiela
      121 yleqlhgqhe awlihkttkl hfealmnipv lvldvnddfs eevtkqedlm revntfvknl
//
LOCUS       NP_699179                598 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_699179
VERSION     NP_699179.2
DBSOURCE    REFSEQ: accession NM_153348.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Mao,C., Li,S., Che,J., Liu,D., Mao,X. and Rao,H.
  TITLE     The ubiquitin ligase UBR4 and the deubiquitylase USP5 modulate the
            stability of DNA mismatch repair protein MLH1
  JOURNAL   J Biol Chem 300 (8), 107592 (2024)
   PUBMED   39032648
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Zhou,H.L., Grimmett,Z.W., Venetos,N.M., Stomberski,C.T., Qian,Z.,
            McLaughlin,P.J., Bansal,P.K., Zhang,R., Reynolds,J.D., Premont,R.T.
            and Stamler,J.S.
  TITLE     An enzyme that selectively S-nitrosylates proteins to regulate
            insulin signaling
  JOURNAL   Cell 186 (26), 5812-5825 (2023)
   PUBMED   38056462
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Gautam,Y., Caldwell,J., Kottyan,L., Chehade,M., Dellon,E.S.,
            Rothenberg,M.E. and Mersha,T.B.
  CONSRTM   Consortium of Eosinophilic Gastrointestinal Disease Researchers
            (CEGIR) investigators
  TITLE     Genome-wide admixture and association analysis identifies African
            ancestry-specific risk loci of eosinophilic esophagitis in African
            Americans
  JOURNAL   J Allergy Clin Immunol 151 (5), 1337-1350 (2023)
   PUBMED   36400179
  REMARK    GeneRIF: Genome-wide admixture and association analysis identifies
            African ancestry-specific risk loci of eosinophilic esophagitis in
            African Americans.
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Hopf,L.V.M., Baek,K., Klugel,M., von Gronau,S., Xiong,Y. and
            Schulman,B.A.
  TITLE     Structure of CRL7FBXW8 reveals coupling with CUL1-RBX1/ROC1 for
            multi-cullin-RING E3-catalyzed ubiquitin ligation
  JOURNAL   Nat Struct Mol Biol 29 (9), 854-862 (2022)
   PUBMED   35982156
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Okabe,H., Lee,S.H., Phuchareon,J., Albertson,D.G., McCormick,F. and
            Tetsu,O.
  TITLE     A critical role for FBXW8 and MAPK in cyclin D1 degradation and
            cancer cell proliferation
  JOURNAL   PLoS One 1 (1), e128 (2006)
   PUBMED   17205132
  REMARK    GeneRIF: FBXW8 plays an essential role in cancer cell proliferation
            through proteolysis of cyclin D1. It may present new opportunities
            to develop therapies targeting destruction of cyclin D1 or its
            regulator E3 ligase selectively.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Watanabe,N., Arai,H., Nishihara,Y., Taniguchi,M., Watanabe,N.,
            Hunter,T. and Osada,H.
  TITLE     M-phase kinases induce phospho-dependent ubiquitination of somatic
            Wee1 by SCFbeta-TrCP
  JOURNAL   Proc Natl Acad Sci U S A 101 (13), 4419-4424 (2004)
   PUBMED   15070733
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Dias,D.C., Dolios,G., Wang,R. and Pan,Z.Q.
  TITLE     CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29
            to form an SCF-like complex
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16601-16606 (2002)
   PUBMED   12481031
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC083806.16, AC127164.2 and
            AC026368.37.
            
            On May 16, 2003 this sequence version replaced NP_699179.1.
            
            Summary: This gene encodes a member of the F-box protein family,
            members of which are characterized by an approximately 40 amino
            acid motif, the F-box. The F-box proteins constitute one of the
            four subunits of ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into three classes:
            Fbws containing WD-40 domains, Fbls containing leucine-rich
            repeats, and Fbxs containing either different protein-protein
            interaction modules or no recognizable motifs. The protein encoded
            by this gene contains a WD-40 domain, in addition to an F-box
            motif, so it belongs to the Fbw class. Alternatively spliced
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037296.2, DRR138509.21041.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652555.1/ ENSP00000498999.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.22"
     Protein         1..598
                     /product="F-box/WD repeat-containing protein 8 isoform 1"
                     /note="F-box and WD-40 domain protein 8; F-box only
                     protein 29; F-box/WD repeat-containing protein 8; F-box
                     and WD-40 domain-containing protein 8"
                     /calculated_mol_wt=67263
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          17..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BIA4; propagated from
                     UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BIA4; propagated from
                     UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          113..160
                     /region_name="F-box_FBXW8"
                     /note="F-box domain found in F-box/WD repeat-containing
                     protein 8 (FBXW8) and similar proteins; cd22134"
                     /db_xref="CDD:438906"
     Site            order(119,123,126..127,130..131,135,137..138,142..144,146)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438906"
     Region          191..530
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          201..250
                     /region_name="WD 1. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          213..253
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          259..299
                     /region_name="WD 2. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          260..297
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          300..340
                     /region_name="WD 3. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          341..383
                     /region_name="WD 4. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          384..429
                     /region_name="WD 5. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          430..475
                     /region_name="WD 6. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          436..472
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          476..513
                     /region_name="WD 7. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     Region          478..513
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          514..561
                     /region_name="WD 8. /evidence=ECO:0000269|PubMed:35982156,
                     ECO:0007744|PDB:7Z8B"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3Y1.2)"
     CDS             1..598
                     /gene="FBXW8"
                     /gene_synonym="FBW6; FBW8; FBX29; FBXO29; FBXW6"
                     /coded_by="NM_153348.3:89..1885"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9182.1"
                     /db_xref="GeneID:26259"
                     /db_xref="HGNC:HGNC:13597"
                     /db_xref="MIM:609073"
ORIGIN      
        1 mddysldefr rrwqeelaqa qapkkrrrpe aaerrarrpe vgsgrgeqas gdpalaqrll
       61 egagrppaar atraegqdva srsrsplare gagggeqlvd qlirdlnemn dvpffdiqlp
      121 yelainifqy ldrkelgrca qvsktwkvia edevlwyrlc qqeghlpdss isdyscwkli
      181 fqecrakehm lrtnwknrkg avselehvpd tvlcdvhshd gvviagytsg dvrvwdtrtw
      241 dyvapflese deedepgmqp nvsfvrinss lavaayedgf lniwdlrtgk ypvhrfehda
      301 riqalalsqd datvatasaf dvvmlspnee gywqiaaefe vpklvqylei vpetrrypva
      361 vaaagdlmyl lkaedsartl lyahgppvtc ldvsanqvaf gvqglgwvye gskilvysle
      421 agrrllklgn vlrdftcvnl sdsppnlmvs gnmdgrvrih dlrsgnials lsahqlrvsa
      481 vqmddwkivs ggeeglvsvw dyrmnqklwe vysghpvqhi sfsshslita nvpyqtvmrn
      541 adldsftthr rhrgliraye favdqlafqs plpvcrsscd amathyydla lafpynhv
//
LOCUS       NP_001241                277 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 5 isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001241
VERSION     NP_001241.1
DBSOURCE    REFSEQ: accession NM_001250.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Ahmed,H.A., Abdelkreem,E., Hamed,E.O., Abo Elmahassen,N.M. and
            Younis,M.A.A.
  TITLE     Frequency of CD40-1C>T polymorphism (rs1883832) and association
            with response to treatment in children with primary immune
            thrombocytopenia
  JOURNAL   Pediatr Blood Cancer 71 (12), e31356 (2024)
   PUBMED   39350313
  REMARK    GeneRIF: Frequency of CD40-1C>T polymorphism (rs1883832) and
            association with response to treatment in children with primary
            immune thrombocytopenia.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Meng,H., Li,L., Nan,M., Ding,Y., Li,Y. and Zhang,M.
  TITLE     ZG16 enhances the maturation of dendritic cells via induction of
            CD40 and contributes to the antitumor immunity in pancreatic cancer
  JOURNAL   Oncogene 43 (43), 3184-3196 (2024)
   PUBMED   39261658
  REMARK    GeneRIF: ZG16 enhances the maturation of dendritic cells via
            induction of CD40 and contributes to the antitumor immunity in
            pancreatic cancer.
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Aydin,S., Darko,K., Detchou,D. and Barrie,U.
  TITLE     A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40
  JOURNAL   Neurosurg Rev 47 (1), 571 (2024)
   PUBMED   39242402
  REMARK    GeneRIF: A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Naseri,S., Cordova,M.M., Wenthe,J., Lovgren,T., Eriksson,E.,
            Loskog,A. and Ullenhag,G.J.
  TITLE     CD40 stimulation via CD40 ligand enhances adenovirus-mediated
            tumour immunogenicity including 'find-me', 'eat-me', and 'kill-me'
            signalling
  JOURNAL   J Cell Mol Med 28 (7), e18162 (2024)
   PUBMED   38494863
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Foy,T.M., Laman,J.D., Ledbetter,J.A., Aruffo,A., Claassen,E. and
            Noelle,R.J.
  TITLE     gp39-CD40 interactions are essential for germinal center formation
            and the development of B cell memory
  JOURNAL   J Exp Med 180 (1), 157-163 (1994)
   PUBMED   7516405
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Banchereau,J., Bazan,F., Blanchard,D., Briere,F., Galizzi,J.P., van
            Kooten,C., Liu,Y.J., Rousset,F. and Saeland,S.
  TITLE     The CD40 antigen and its ligand
  JOURNAL   Annu Rev Immunol 12, 881-922 (1994)
   PUBMED   7516669
  REMARK    Review article
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Stamenkovic,I., Clark,E.A. and Seed,B.
  TITLE     A B-lymphocyte activation molecule related to the nerve growth
            factor receptor and induced by cytokines in carcinomas
  JOURNAL   EMBO J 8 (5), 1403-1410 (1989)
   PUBMED   2475341
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Clark,E.A. and Ledbetter,J.A.
  TITLE     Activation of human B cells mediated through two distinct cell
            surface differentiation antigens, Bp35 and Bp50
  JOURNAL   Proc Natl Acad Sci U S A 83 (12), 4494-4498 (1986)
   PUBMED   3487090
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Paulie,S., Ehlin-Henriksson,B., Mellstedt,H., Koho,H., Ben-Aissa,H.
            and Perlmann,P.
  TITLE     A p50 surface antigen restricted to human urinary bladder
            carcinomas and B lymphocytes
  JOURNAL   Cancer Immunol Immunother 20 (1), 23-28 (1985)
   PUBMED   2998589
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM761221.1, BC012419.1,
            BC064518.1, BX364284.2 and AL035662.65.
            
            Summary: This gene is a member of the TNF-receptor superfamily. The
            encoded protein is a receptor on antigen-presenting cells of the
            immune system and is essential for mediating a broad variety of
            immune and inflammatory responses including T cell-dependent
            immunoglobulin class switching, memory B cell development, and
            germinal center formation. AT-hook transcription factor AKNA is
            reported to coordinately regulate the expression of this receptor
            and its ligand, which may be important for homotypic cell
            interactions. Adaptor protein TNFR2 interacts with this receptor
            and serves as a mediator of the signal transduction. The
            interaction of this receptor and its ligand is found to be
            necessary for amyloid-beta-induced microglial activation, and thus
            is thought to be an early event in Alzheimer disease pathogenesis.
            Mutations affecting this gene are the cause of autosomal recessive
            hyper-IgM immunodeficiency type 3 (HIGM3). Multiple alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Nov 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222896.1, SRR1660803.138274.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372285.8/ ENSP00000361359.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..277
                     /product="tumor necrosis factor receptor superfamily
                     member 5 isoform 1 precursor"
                     /note="CD40L receptor; B cell-associated molecule; B cell
                     surface antigen CD40; tumor necrosis factor receptor
                     superfamily member 5; CD40 molecule, TNF receptor
                     superfamily member 5"
                     /calculated_mol_wt=28387
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2250
     mat_peptide     21..277
                     /product="Tumor necrosis factor receptor superfamily
                     member 5. /id=PRO_0000034559"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
                     /calculated_mol_wt=28387
     Region          25..60
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          26..186
                     /region_name="TNFRSF5"
                     /note="Tumor necrosis factor receptor superfamily member 5
                     (TNFRSF5), also known as CD40; cd13407"
                     /db_xref="CDD:276912"
     Region          26..59
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276912"
     Region          61..103
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          62..103
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276912"
     Site            order(65..66,73..74,76..79,82,84,86,119)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276912"
     Region          104..144
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          105..143
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276912"
     Region          145..187
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          146..186
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276912"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25942.1)"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25942.1)"
     Site            194..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          223..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     CDS             1..277
                     /gene="CD40"
                     /gene_synonym="Bp50; CDW40; p50; TNFRSF5"
                     /coded_by="NM_001250.6:31..864"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13393.1"
                     /db_xref="GeneID:958"
                     /db_xref="HGNC:HGNC:11919"
                     /db_xref="MIM:109535"
ORIGIN      
        1 mvrlplqcvl wgclltavhp epptacrekq ylinsqccsl cqpgqklvsd cteftetecl
       61 pcgesefldt wnrethchqh kycdpnlglr vqqkgtsetd tictceegwh ctseacescv
      121 lhrscspgfg vkqiatgvsd ticepcpvgf fsnvssafek chpwtscetk dlvvqqagtn
      181 ktdvvcgpqd rlralvvipi ifgilfaill vlvfikkvak kptnkaphpk qepqeinfpd
      241 dlpgsntaap vqetlhgcqp vtqedgkesr isvqerq
//
LOCUS       NP_002638                887 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase catalytic subunit type 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_002638
VERSION     NP_002638.2
DBSOURCE    REFSEQ: accession NM_002647.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Gong,M., Peng,C., Yang,C., Wang,Z., Qian,H., Hu,X., Zhou,P.,
            Shan,C. and Ding,Q.
  TITLE     Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and PIK3C3 as
            crucial entry factors for Ebola virus infection
  JOURNAL   PLoS Pathog 20 (8), e1012444 (2024)
   PUBMED   39173055
  REMARK    GeneRIF: Genome-wide CRISPR/Cas9 screen identifies SLC39A9 and
            PIK3C3 as crucial entry factors for Ebola virus infection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Tahoun,M. and Sadaka,A.S.
  TITLE     Deregulated expression of autophagy genes; PIK3C3 and RAB7A in
            COVID-19 patients
  JOURNAL   Hum Immunol 85 (3), 110801 (2024)
   PUBMED   38609772
  REMARK    GeneRIF: Deregulated expression of autophagy genes; PIK3C3 and
            RAB7A in COVID-19 patients.
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Jia,M., Yue,X., Sun,W., Zhou,Q., Chang,C., Gong,W., Feng,J., Li,X.,
            Zhan,R., Mo,K., Zhang,L., Qian,Y., Sun,Y., Wang,A., Zou,Y.,
            Chen,W., Li,Y., Huang,L., Yang,Y., Zhao,Y. and Cheng,X.
  TITLE     ULK1-mediated metabolic reprogramming regulates Vps34 lipid kinase
            activity by its lactylation
  JOURNAL   Sci Adv 9 (22), eadg4993 (2023)
   PUBMED   37267363
  REMARK    GeneRIF: ULK1-mediated metabolic reprogramming regulates Vps34
            lipid kinase activity by its lactylation.
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Borgatti,P., Zauli,G., Colamussi,M.L., Gibellini,D., Previati,M.,
            Cantley,L.L. and Capitani,S.
  TITLE     Extracellular HIV-1 Tat protein activates phosphatidylinositol 3-
            and Akt/PKB kinases in CD4+ T lymphoblastoid Jurkat cells
  JOURNAL   Eur J Immunol 27 (11), 2805-2811 (1997)
   PUBMED   9394803
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Panaretou,C., Domin,J., Cockcroft,S. and Waterfield,M.D.
  TITLE     Characterization of p150, an adaptor protein for the human
            phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by
            phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase
            complex
  JOURNAL   J Biol Chem 272 (4), 2477-2485 (1997)
   PUBMED   8999962
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Milani,D., Mazzoni,M., Borgatti,P., Zauli,G., Cantley,L. and
            Capitani,S.
  TITLE     Extracellular human immunodeficiency virus type-1 Tat protein
            activates phosphatidylinositol 3-kinase in PC12 neuronal cells
  JOURNAL   J Biol Chem 271 (38), 22961-22964 (1996)
   PUBMED   8798481
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Volinia,S., Dhand,R., Vanhaesebroeck,B., MacDougall,L.K., Stein,R.,
            Zvelebil,M.J., Domin,J., Panaretou,C. and Waterfield,M.D.
  TITLE     A human phosphatidylinositol 3-kinase complex related to the yeast
            Vps34p-Vps15p protein sorting system
  JOURNAL   EMBO J 14 (14), 3339-3348 (1995)
   PUBMED   7628435
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Vogel,L.B. and Fujita,D.J.
  TITLE     The SH3 domain of p56lck is involved in binding to
            phosphatidylinositol 3'-kinase from T lymphocytes
  JOURNAL   Mol Cell Biol 13 (12), 7408-7417 (1993)
   PUBMED   7504174
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB450556.1, BC053651.1, CA945171.1 and AC087683.5.
            
            On Sep 16, 2003 this sequence version replaced NP_002638.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.226042.1,
                                           SRR1803617.105756.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262039.9/ ENSP00000262039.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..887
                     /product="phosphatidylinositol 3-kinase catalytic subunit
                     type 3 isoform 1"
                     /EC_number="2.7.1.137"
                     /note="PI3K type 3; PI3-kinase type 3; PtdIns-3-kinase
                     type 3; phosphatidylinositol 3-kinase p100 subunit;
                     phosphoinositide-3-kinase, class 3; vacuolar protein
                     sorting 34 homolog"
                     /calculated_mol_wt=101419
     Region          26..186
                     /region_name="C2_PI3K_class_III"
                     /note="C2 domain present in class III phosphatidylinositol
                     3-kinases (PI3Ks); cd08397"
                     /db_xref="CDD:176042"
     Region          149..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q6PF93; propagated from
                     UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:Q6PF93; propagated from
                     UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88763; propagated from
                     UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Region          283..503
                     /region_name="PI3Ka_III"
                     /note="Phosphoinositide 3-kinase (PI3K) class III,
                     accessory domain (PIK domain); PIK domain is conserved in
                     all PI3 and PI4-kinases. Its role is unclear but it has
                     been suggested to be involved in substrate presentation.
                     In general, PI3Ks class III...; cd00870"
                     /db_xref="CDD:238442"
     Region          447..467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Region          539..883
                     /region_name="PI3Kc_III"
                     /note="Catalytic domain of Class III Phosphoinositide
                     3-kinase; cd00896"
                     /db_xref="CDD:270628"
     Region          611..617
                     /region_name="G-loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            order(612,614..616,618,634,636,639,670,682..685,689,692,
                     748,750,760..761)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270628"
     Region          740..748
                     /region_name="Catalytic loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            740..748
                     /site_type="active"
                     /note="catalytic loop [active]"
                     /db_xref="CDD:270628"
     Region          759..780
                     /region_name="Activation loop.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00269"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEB9.1)"
     Site            761..780
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270628"
     CDS             1..887
                     /gene="PIK3C3"
                     /gene_synonym="hVps34; Vps34; VPS34"
                     /coded_by="NM_002647.4:59..2722"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11920.1"
                     /db_xref="GeneID:5289"
                     /db_xref="HGNC:HGNC:8974"
                     /db_xref="MIM:602609"
ORIGIN      
        1 mgeaekfhyi yscdldinvq lkigslegkr eqksykavle dpmlkfsgly qetcsdlyvt
       61 cqvfaegkpl alpvrtsyka fstrwnwnew lklpvkypdl prnaqvalti wdvygpgkav
      121 pvggttvslf gkygmfrqgm hdlkvwpnve adgseptktp grtsstlsed qmsrlakltk
      181 ahrqghmvkv dwldrltfre ieminesekr ssnfmylmve frcvkcddke ygivyyekdg
      241 desspiltsf elvkvpdpqm smenlveskh hklarslrsg psdhdlkpna atrdqlniiv
      301 sypptkqlty eeqdlvwkfr yyltnqekal tkflkcvnwd lpqeakqale llgkwkpmdv
      361 edslellssh ytnptvrrya varlrqadde dllmyllqlv qalkyenfdd ikngleptkk
      421 dsqssvsenv snsginsaei dssqiitspl psvsspppas ktkevpdgen leqdlctfli
      481 sracknstla nylywyvive cedqdtqqrd pkthemylnv mrrfsqallk gdksvrvmrs
      541 llaaqqtfvd rlvhlmkavq resgnrkkkn erlqallgdn ekmnlsdvel iplplepqvk
      601 irgiipetat lfksalmpaq lffktedggk ypvifkhgdd lrqdqlilqi islmdkllrk
      661 enldlkltpy kvlatstkhg fmqfiqsvpv aevldtegsi qnffrkyaps engpngisae
      721 vmdtyvksca gycvityilg vgdrhldnll ltktgklfhi dfgyilgrdp kplpppmkln
      781 kemvegmggt qseqyqefrk qcytaflhlr rysnlilnlf slmvdanipd ialepdktvk
      841 kvqdkfrldl sdeeavhymq slidesvhal faavveqihk faqywrk
//
LOCUS       NP_006445                209 aa            linear   PRI 20-NOV-2025
DEFINITION  max dimerization protein 4 [Homo sapiens].
ACCESSION   NP_006445
VERSION     NP_006445.1
DBSOURCE    REFSEQ: accession NM_006454.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Coutier,J., Auvre,F., Lemaitre,G., Lataillade,J.J., Deleuze,J.F.,
            Romeo,P.H., Martin,M.T. and Fortunel,N.O.
  TITLE     MXD4/MAD4 Regulates Human Keratinocyte Precursor Fate
  JOURNAL   J Invest Dermatol 143 (1), 105-114 (2023)
   PUBMED   36007550
  REMARK    GeneRIF: MXD4/MAD4 Regulates Human Keratinocyte Precursor Fate.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Hu,C.L., Chen,B.Y., Li,Z., Yang,T., Xu,C.H., Yang,R., Yu,P.C.,
            Zhao,J., Liu,T., Liu,N., Shan,B., Zhang,Q., Song,J., Fei,M.Y.,
            Zong,L.J., Zhang,J.Y., Wu,J.C., Chen,S.B., Wang,Y., Chang,B.,
            Hou,D., Liu,P., Jiang,Y., Li,X., Chen,X., Deng,C.H., Ren,Y.Y.,
            Wang,R., Jin,J., Xue,K., Zhang,Y., Du,M., Shi,J., Wu,L.Y.,
            Chang,C.K., Shen,S., Chen,Z., Chen,S.J., Liu,X., Sun,X.J., Zheng,M.
            and Wang,L.
  TITLE     Targeting UHRF1-SAP30-MXD4 axis for leukemia initiating cell
            eradication in myeloid leukemia
  JOURNAL   Cell Res 32 (12), 1105-1123 (2022)
   PUBMED   36302855
  REMARK    GeneRIF: Targeting UHRF1-SAP30-MXD4 axis for leukemia initiating
            cell eradication in myeloid leukemia.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Van Treeck,B.J., Thangaiah,J.J., Torres-Mora,J., Stevens,T.M.,
            Rothermundt,C., Fassan,M., Loupakis,F., Diebold,J., Hornick,J.L.,
            Halling,K.C. and Folpe,A.L.
  TITLE     NUTM1-rearranged colorectal sarcoma: a clinicopathologically and
            genetically distinctive malignant neoplasm with a poor prognosis
  JOURNAL   Mod Pathol 34 (8), 1547-1557 (2021)
   PUBMED   33714983
  REMARK    GeneRIF: NUTM1-rearranged colorectal sarcoma: a
            clinicopathologically and genetically distinctive malignant
            neoplasm with a poor prognosis.
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Conacci-Sorrell,M., McFerrin,L. and Eisenman,R.N.
  TITLE     An overview of MYC and its interactome
  JOURNAL   Cold Spring Harb Perspect Med 4 (1), a014357 (2014)
   PUBMED   24384812
  REMARK    Review article
            Erratum:[Cold Spring Harb Perspect Med. 2014 Apr;4(4).
            doi:10.1101/cshperspect.a023325]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Yang,W., Yang,X., David,G. and Dorsey,J.F.
  TITLE     Dissecting the complex regulation of Mad4 in glioblastoma
            multiforme cells
  JOURNAL   Cancer Biol Ther 13 (13), 1339-1348 (2012)
   PUBMED   22895069
  REMARK    GeneRIF: The E3 ligase activity of c-IAP1 was not required for
            downregulation of Mad4 expression.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Jiang,D.J., Yu,H.X., Hexige,S.Y., Guo,Z.K., Wang,X., Ma,L.J.,
            Chen,Z., Zhao,S.Y. and Yu,L.
  TITLE     Human liver specific transcriptional factor TCP10L binds to MAD4
  JOURNAL   J Biochem Mol Biol 37 (4), 402-407 (2004)
   PUBMED   15469726
  REMARK    GeneRIF: Data suggest that the biological function of the
            interaction between T-complex protein 10-like and MAD4 may be to
            maintain the differentiation state in liver cells.
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Kime,L. and Wright,S.C.
  TITLE     Mad4 is regulated by a transcriptional repressor complex that
            contains Miz-1 and c-Myc
  JOURNAL   Biochem J 370 (Pt 1), 291-298 (2003)
   PUBMED   12418961
  REMARK    GeneRIF: regulation by a transcriptional repressor complex that
            contains Miz-1 and c-Myc
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Cairo,S., Merla,G., Urbinati,F., Ballabio,A. and Reymond,A.
  TITLE     WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted
            region, is a new member of the Mlx transcription factor network
  JOURNAL   Hum Mol Genet 10 (6), 617-627 (2001)
   PUBMED   11230181
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Billin,A.N., Eilers,A.L., Queva,C. and Ayer,D.E.
  TITLE     Mlx, a novel Max-like BHLHZip protein that interacts with the Max
            network of transcription factors
  JOURNAL   J Biol Chem 274 (51), 36344-36350 (1999)
   PUBMED   10593926
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158068.18.
            
            Summary: This gene is a member of the MAD gene family . The MAD
            genes encode basic helix-loop-helix-leucine zipper proteins that
            heterodimerize with MAX protein, forming a transcriptional
            repression complex. The MAD proteins compete for MAX binding with
            MYC, which heterodimerizes with MAX forming a transcriptional
            activation complex. Studies in rodents suggest that the MAD genes
            are tumor suppressors and contribute to the regulation of cell
            growth in differentiating tissues. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.215519.1, AF082740.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337190.7/ ENSP00000337889.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..209
                     /product="max dimerization protein 4"
                     /note="Mad4 homolog; max dimerizer 4; max-associated
                     protein 4; class C basic helix-loop-helix protein 12;
                     max-interacting transcriptional repressor MAD4"
                     /calculated_mol_wt=23397
     Region          6..23
                     /region_name="Interaction with SIN3A and SIN3B.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14582.2)"
     Region          53..140
                     /region_name="bHLHzip_Mad4"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-associated protein 4 (Mad4) and similar
                     proteins; cd18929"
                     /db_xref="CDD:381499"
     misc_feature    55..133
                     /note="basic Helix-loop-helix-leucine zipper"
     Site            order(58..59,62..63,65..66,70,89..91)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381499"
     Site            order(69..70,72..77,79..80,92,95,99,101..103,105..106,
                     108..109,112,116,119..120,122..123,126..127,129..130)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381499"
     Site            order(69,72..73,75..76,79..80,92,95,99,101..103,105..106,
                     108..109,112,116,119..120,122..123,126..127,129..130)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381499"
     Region          140..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14582.2)"
     CDS             1..209
                     /gene="MXD4"
                     /gene_synonym="bHLHc12; MAD4; MST149; MSTP149"
                     /coded_by="NM_006454.3:130..759"
                     /db_xref="CCDS:CCDS3361.1"
                     /db_xref="GeneID:10608"
                     /db_xref="HGNC:HGNC:13906"
                     /db_xref="MIM:620016"
ORIGIN      
        1 melnsllill eaaeylerrd reaehgyasv lpfdgdfare ktkaaglvrk apnnrsshne
       61 lekhrraklr lyleqlkqlv plgpdstrht tlsllkrakv hikkleeqdr ralsikeqlq
      121 qehrflkrrl eqlsvqsver vrtdstgsav stddseqevd iegmefgpge ldsvgsssda
      181 ddhyslqsgt ggdsgfgphc rrlgrpals
//
LOCUS       NP_004189                494 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-6 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_004189
VERSION     NP_004189.1
DBSOURCE    REFSEQ: accession NM_004198.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Su,J., Yu,Z., Yin,Z., Zhang,Z., Zhao,J., Meng,Y., Li,R., Gao,Y.,
            Zhang,H., Yu,R. and Zhao,Y.
  TITLE     Molecular insights into the alpha6beta4 nicotinic acetylcholine
            receptor function and ligand recognition
  JOURNAL   Nat Commun 16 (1), 3153 (2025)
   PUBMED   40175361
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Zhang,F., Zhang,M., Yuan,X., Tao,Y. and Wang,J.
  TITLE     Involvement of CHRNA6 in the Immune Response in Lung Squamous Cell
            Carcinoma and its Potential as a Drug Target for the Disease
  JOURNAL   Curr Pharm Des 29 (26), 2091-2100 (2023)
   PUBMED   37680128
  REMARK    GeneRIF: Involvement of CHRNA6 in the Immune Response in Lung
            Squamous Cell Carcinoma and its Potential as a Drug Target for the
            Disease.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Wen,L., Han,H., Liu,Q., Su,K., Yang,Z., Cui,W., Yuan,W., Ma,Y.,
            Fan,R., Chen,J., Jiang,K., Jiang,X., Payne,T.J., Wang,J. and
            Li,M.D.
  TITLE     Significant association of the CHRNB3-CHRNA6 gene cluster with
            nicotine dependence in the Chinese Han population
  JOURNAL   Sci Rep 7 (1), 9745 (2017)
   PUBMED   28851948
  REMARK    GeneRIF: This study is the first showing that CHRNB3/A6 are highly
            associated with nicotine dependence in a large Chinese Han sample.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Arvaniti,M., Jensen,M.M., Soni,N., Wang,H., Klein,A.B., Thiriet,N.,
            Pinborg,L.H., Muldoon,P.P., Wienecke,J., Imad Damaj,M.,
            Kohlmeier,K.A., Gondre-Lewis,M.C., Mikkelsen,J.D. and Thomsen,M.S.
  TITLE     Functional interaction between Lypd6 and nicotinic acetylcholine
            receptors
  JOURNAL   J Neurochem 138 (6), 806-820 (2016)
   PUBMED   27344019
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Zeiger,J.S., Haberstick,B.C., Schlaepfer,I., Collins,A.C.,
            Corley,R.P., Crowley,T.J., Hewitt,J.K., Hopfer,C.J., Lessem,J.,
            McQueen,M.B., Rhee,S.H. and Ehringer,M.A.
  TITLE     The neuronal nicotinic receptor subunit genes (CHRNA6 and CHRNB3)
            are associated with subjective responses to tobacco
  JOURNAL   Hum Mol Genet 17 (5), 724-734 (2008)
   PUBMED   18055561
  REMARK    GeneRIF: CHRNA6 is associated with subjective responses to tobacco.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Ebihara,M., Ohba,H., Ohno,S.I. and Yoshikawa,T.
  TITLE     Genomic organization and promoter analysis of the human nicotinic
            acetylcholine receptor alpha6 subunit (CHNRA6) gene: Alu and other
            elements direct transcriptional repression
  JOURNAL   Gene 298 (1), 101-108 (2002)
   PUBMED   12406580
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Bonati,M.T., Combi,R., Asselta,R., Duga,S., Malcovati,M.,
            Oldani,A., Zucconi,M., Ferini-Strambi,L., Dalpra,L. and
            Tenchini,M.L.
  TITLE     Exclusion of linkage of nine neuronal nicotinic acetylcholine
            receptor subunit genes expressed in brain in autosomal dominant
            nocturnal frontal lobe epilepsy in four unrelated families
  JOURNAL   J Neurol 249 (8), 967-974 (2002)
   PUBMED   12195439
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Graham,A., Court,J.A., Martin-Ruiz,C.M., Jaros,E., Perry,R.,
            Volsen,S.G., Bose,S., Evans,N., Ince,P., Kuryatov,A., Lindstrom,J.,
            Gotti,C. and Perry,E.K.
  TITLE     Immunohistochemical localisation of nicotinic acetylcholine
            receptor subunits in human cerebellum
  JOURNAL   Neuroscience 113 (3), 493-507 (2002)
   PUBMED   12150770
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Le Novere,N., Zoli,M. and Changeux,J.P.
  TITLE     Neuronal nicotinic receptor alpha 6 subunit mRNA is selectively
            concentrated in catecholaminergic nuclei of the rat brain
  JOURNAL   Eur J Neurosci 8 (11), 2428-2439 (1996)
   PUBMED   8950106
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC307404.1 and BC014456.1.
            
            Summary: This gene encodes an alpha subunit of neuronal nicotinic
            acetylcholine receptors. These receptors consist of five subunits
            and function as ion channels involved in neurotransmission. The
            encoded protein is a subunit of neuronal nicotinic acetylcholine
            receptors that mediate dopaminergic neurotransmission and are
            activated by acetylcholine and exogenous nicotine. Alternatively
            spliced transcript variants have been observed for this gene.
            Single nucleotide polymorphisms in this gene have been associated
            with both nicotine and alcohol dependence. [provided by RefSeq, Dec
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014456.1, SRR1803616.215210.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276410.7/ ENSP00000276410.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..494
                     /product="neuronal acetylcholine receptor subunit alpha-6
                     isoform 1 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     6; neuronal acetylcholine receptor subunit alpha-6;
                     acetylcholine receptor, nicotinic, alpha 6 (neuronal);
                     cholinergic receptor, nicotinic, alpha 6 (neuronal);
                     cholinergic receptor, nicotinic alpha 6; alpha(alpha)6
                     nicotinic acetylcholine receptor (nAChR) subunit"
                     /calculated_mol_wt=53669
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3248
     mat_peptide     31..494
                     /product="neuronal acetylcholine receptor subunit alpha-6
                     isoform 1"
                     /calculated_mol_wt=53669
     Region          34..484
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          34..240
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            54
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15825.1)"
     Site            order(69,71,77..78,85,107,109,118..119,121,123..124,
                     135..137,139,149,151,153,157,179,239)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15825.1)"
     Site            240..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15825.1)"
     Site            272..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15825.1)"
     Site            306..327
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15825.1)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (Q15825.1)"
     Site            466..484
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15825.1)"
     CDS             1..494
                     /gene="CHRNA6"
                     /gene_synonym="CHNRA6"
                     /coded_by="NM_004198.3:357..1841"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6135.1"
                     /db_xref="GeneID:8973"
                     /db_xref="HGNC:HGNC:15963"
                     /db_xref="MIM:606888"
ORIGIN      
        1 mltskgqgfl hgglclwlcv ftpffkgcvg cateerlfhk lfshynqfir pvenvsdpvt
       61 vhfevaitql anvdevnqim etnlwlrhiw ndyklrwdpm eydgietlrv padkiwkpdi
      121 vlynnavgdf qvegktkall kyngmitwtp paifksscpm ditffpfdhq ncslkfgswt
      181 ydkaeidlli igskvdmndf wenseweiid asgykhdiky ncceeiytdi tysfyirrlp
      241 mfytinliip clfisfltvl vfylpsdcge kvtlcisvll sltvfllvit etipstslvv
      301 plvgeyllft mifvtlsivv tvfvlnihyr tptthtmprw vktvflkllp qvllmrwpld
      361 ktrgtgsdav prglarrpak gklashgepr hlkecfhchk snelatskrr lshqplqwvv
      421 ensehspeve dvinsvqfia enmkshnetk eveddwkyva mvvdrvflwv fiivcvfgta
      481 glflqpllgn tgks
//
LOCUS       NP_001310458             623 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing regulatory glutamine/lysine-rich protein 1 isoform e [Homo
            sapiens].
ACCESSION   NP_001310458 XP_006714598
VERSION     NP_001310458.1
DBSOURCE    REFSEQ: accession NM_001323529.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Chang,C., Rajasekaran,M., Qiao,Y., Dong,H., Wang,Y., Xia,H.,
            Deivasigamani,A., Wu,M., Sekar,K., Gao,H., Sun,M., Niu,Y., Li,Q.,
            Tao,L., Yan,Z., Wang,M., Chen,S., Zhao,S., Chen,D., Li,L., Yang,F.,
            Gao,H., Chen,B., Su,L., Xu,L., Chen,Y., Seshachalam,V.P., Chen,G.,
            Gunaratne,J., Hong,W., Shi,J., Chen,G., Grierson,D.S., Chabot,B.,
            Xie,T., Hui,K.M. and Chen,J.
  TITLE     The aberrant upregulation of exon 10-inclusive SREK1 through SRSF10
            acts as an oncogenic driver in human hepatocellular carcinoma
  JOURNAL   Nat Commun 13 (1), 1363 (2022)
   PUBMED   35296659
  REMARK    GeneRIF: The aberrant upregulation of exon 10-inclusive SREK1
            through SRSF10 acts as an oncogenic driver in human hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Abudureheman,Z., Li,L., Zhong,X., Xu,J., Gong,H., Yilamujiang,S.,
            Ren,J., Xie,C., Zheng,A., Tuerxun,D., Abudukadeer,A., Aini,P.,
            Xu,A. and Zou,X.
  TITLE     The rs74794265 SNP of the SREK1 Gene is Associated with COPD in
            Kashi, China
  JOURNAL   Int J Chron Obstruct Pulmon Dis 16, 2631-2636 (2021)
   PUBMED   34556983
  REMARK    GeneRIF: The rs74794265 SNP of the SREK1 Gene is Associated with
            COPD in Kashi, China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Heese,K., Fujita,M., Akatsu,H., Yamamoto,T., Kosaka,K., Nagai,Y.
            and Sawada,T.
  TITLE     The splicing regulatory protein p18SRP is down-regulated in
            Alzheimer's disease brain
  JOURNAL   J Mol Neurosci 24 (2), 269-276 (2004)
   PUBMED   15456940
  REMARK    GeneRIF: p18SRP is a lysine-rich zinc finger domain-containing
            protein that interacts with the serine-arginine-rich splicing
            regulatory protein SRrp86; it is downregulated in brain of
            Alzheimer disease patients.
REFERENCE   7  (residues 1 to 623)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Li,J., Barnard,D.C. and Patton,J.G.
  TITLE     A unique glutamic acid-lysine (EK) domain acts as a splicing
            inhibitor
  JOURNAL   J Biol Chem 277 (42), 39485-39492 (2002)
   PUBMED   12183448
  REMARK    GeneRIF: the unique glutamic acid-lysine domain of SRrp86 plays a
            modulatory role controlling serine-arginine domain function
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Barnard,D.C., Li,J., Peng,R. and Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 through coactivation
            and repression of specific SR proteins
  JOURNAL   RNA 8 (4), 526-533 (2002)
   PUBMED   11991645
  REMARK    GeneRIF: SRrp86 can activate SRp20 and repress SC35 in a
            dose-dependent manner both in vitro and in vivo
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Barnard,D.C. and Patton,J.G.
  TITLE     Identification and characterization of a novel serine-arginine-rich
            splicing regulatory protein
  JOURNAL   Mol Cell Biol 20 (9), 3049-3057 (2000)
   PUBMED   10757789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025442.6 and AC008772.6.
            
            On Apr 22, 2016 this sequence version replaced XP_006714598.1.
            
            Summary: This gene encodes a member of a family of
            serine/arginine-rich (SR) splicing proteins containing RNA
            recognition motif (RRM) domains. The encoded protein interacts with
            other SR proteins to modulate splice site selection. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.105292.1,
                                           SRR1803613.31706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..623
                     /product="splicing regulatory glutamine/lysine-rich
                     protein 1 isoform e"
                     /note="splicing factor, arginine/serine-rich 12;
                     serine-arginine-rich splicing regulatory protein 508;
                     serine/arginine-rich-splicing regulatory protein 86;
                     splicing regulatory glutamine/lysine-rich protein 1;
                     splicing regulatory glutamic acid/lysine-rich protein 1"
                     /calculated_mol_wt=71431
     Region          20..99
                     /region_name="RRM1_SREK1"
                     /note="RNA recognition motif 1 (RRM1) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12519"
                     /db_xref="CDD:409941"
     Region          178..263
                     /region_name="RRM2_SREK1"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12260"
                     /db_xref="CDD:409705"
     CDS             1..623
                     /gene="SREK1"
                     /gene_synonym="SFRS12; SRrp508; SRrp86"
                     /coded_by="NM_001323529.2:78..1949"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="GeneID:140890"
                     /db_xref="HGNC:HGNC:17882"
                     /db_xref="MIM:609268"
ORIGIN      
        1 mnsgggfglg lgfgltptsv iqvtnlssav tseqmrtlfs flgeieelrl yppdnaplaf
       61 sskvcyvkfr dpssvgvaqh ltntvfidra livvpcaegk ipeeskalsl lapaptmtsl
      121 mpgagllpip tpnplttlgv slsslgaipa aaldpniatl geipqpplmg nvdpskidei
      181 rrtvyvgnln sqtttadqll effkqvgevk fvrmagdetq ptrfafvefa dqnsvprala
      241 fngvmfgdrp lkinhsnnai vkppemtpqa aakeleevmk rvreaqsfis aaiepesgks
      301 nerkggrsrs htrsksrsss kshsrrkrsq skhrsrshnr srsrqkdrrr sksphkkrsk
      361 srerrksrsr shsrdkrkdt rekikekerv kekdrekere rekerekeke rgknkdrdke
      421 rekdrekdke kdrerereke hekdrdkeke keqdkekere kdrskeidek rkkdkksrtp
      481 prsynasrrs rsssrerrrr rsrsssrspr tsktikrkss rspsprrnkk dkkrekerdh
      541 iserrerers tsmrkssndr dgkeklekns tslkekehnk epdssvskev ddkdaprtee
      601 nkiqhngncq lneenlstkt eav
//
LOCUS       NP_001357516             171 aa            linear   PRI 20-NOV-2025
DEFINITION  tudor-interacting repair regulator protein isoform 5 [Homo
            sapiens].
ACCESSION   NP_001357516
VERSION     NP_001357516.1
DBSOURCE    REFSEQ: accession NM_001370587.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 171)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 171)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 171)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 171)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 171)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138508.21207.1, BG469758.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..171
                     /product="tudor-interacting repair regulator protein
                     isoform 5"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=18813
     Region          23..>142
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..171
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001370587.1:10..525"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92097.1"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lmqmrfdgll
       61 gfpggfvdrr fwsledglnr vlglglgclr lteadylssh ltegphrvva hlyarqltle
      121 qlhaveisav hsrdhglevl nmmpeeklve alaaatekqk kalekllpas s
//
LOCUS       NP_001368               4307 aa            linear   PRI 20-NOV-2025
DEFINITION  cytoplasmic dynein 2 heavy chain 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001368
VERSION     NP_001368.2
DBSOURCE    REFSEQ: accession NM_001377.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4307)
  AUTHORS   Piceci-Sparascio,F., Micale,L., Torres,B., Guida,V., Consoli,F.,
            Torrente,I., Onori,A., Frustaci,E., D'Asdia,M.C., Petrizzelli,F.,
            Bernardini,L., Mancini,C., Soli,F., Cocciadiferro,D.,
            Guadagnolo,D., Mastromoro,G., Putotto,C., Fontana,F.,
            Brunetti-Pierri,N., Novelli,A., Pizzuti,A., Marino,B.,
            Digilio,M.C., Mazza,T., Dallapiccola,B., Ruiz-Perez,V.L.,
            Tartaglia,M., Castori,M. and De Luca,A.
  TITLE     Clinical variability in DYNC2H1-related skeletal ciliopathies
            includes Ellis-van Creveld syndrome
  JOURNAL   Eur J Hum Genet 31 (4), 479-484 (2023)
   PUBMED   36599940
  REMARK    GeneRIF: Clinical variability in DYNC2H1-related skeletal
            ciliopathies includes Ellis-van Creveld syndrome.
REFERENCE   2  (residues 1 to 4307)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4307)
  AUTHORS   Lee,J., Lee,H., Lee,Y.M., Kuht,H.J., Thomas,M.G., Kim,S.J.,
            Lee,S.T. and Han,J.
  TITLE     DYNC2H1 variants cause Leber congenital amaurosis without syndromic
            features
  JOURNAL   Clin Genet 100 (1), 111-113 (2021)
   PUBMED   33755199
  REMARK    GeneRIF: DYNC2H1 variants cause Leber congenital amaurosis without
            syndromic features.
REFERENCE   4  (residues 1 to 4307)
  AUTHORS   Xia,C.L., Xiao,S.Q., Yang,X., Liu,C.X., Qiu,H., Jiang,H.K.,
            Li-Ling,J. and Lyu,Y.
  TITLE     Radiological and histopathological features of short
            rib-polydactyly syndrome type III and identification of two novel
            DYNC2H1 variants
  JOURNAL   Mol Med Rep 23 (6) (2021)
   PUBMED   33846808
  REMARK    GeneRIF: Radiological and histopathological features of short
            ribpolydactyly syndrome type III and identification of two novel
            DYNC2H1 variants.
REFERENCE   5  (residues 1 to 4307)
  AUTHORS   Thakur,S., Gupta,R., Bansal,D., Singh,C., Agarwal,D. and
            Saxena,K.K.
  TITLE     Clinical insights and molecular study of three foetuses with
            DYNC2H1 gene mutation causing short rib thoracic dystrophy
  JOURNAL   Clin Genet 99 (6), 853-854 (2021)
   PUBMED   33694158
  REMARK    GeneRIF: Clinical insights and molecular study of three foetuses
            with DYNC2H1 gene mutation causing short rib thoracic dystrophy.
REFERENCE   6  (residues 1 to 4307)
  AUTHORS   Kastury,K., Taylor,W.E., Gutierrez,M., Ramirez,L., Coucke,P.J., Van
            Hauwe,P., Van Camp,G. and Bhasin,S.
  TITLE     Chromosomal mapping of two members of the human dynein gene family
            to chromosome regions 7p15 and 11q13 near the deafness loci DFNA 5
            and DFNA 11
  JOURNAL   Genomics 44 (3), 362-364 (1997)
   PUBMED   9325061
REFERENCE   7  (residues 1 to 4307)
  AUTHORS   Criswell,P.S., Ostrowski,L.E. and Asai,D.J.
  TITLE     A novel cytoplasmic dynein heavy chain: expression of DHC1b in
            mammalian ciliated epithelial cells
  JOURNAL   J Cell Sci 109 (Pt 7), 1891-1898 (1996)
   PUBMED   8832411
REFERENCE   8  (residues 1 to 4307)
  AUTHORS   Vaisberg,E.A., Grissom,P.M. and McIntosh,J.R.
  TITLE     Mammalian cells express three distinct dynein heavy chains that are
            localized to different cytoplasmic organelles
  JOURNAL   J Cell Biol 133 (4), 831-842 (1996)
   PUBMED   8666668
REFERENCE   9  (residues 1 to 4307)
  AUTHORS   Gibbons,B.H., Asai,D.J., Tang,W.J., Hays,T.S. and Gibbons,I.R.
  TITLE     Phylogeny and expression of axonemal and cytoplasmic dynein genes
            in sea urchins
  JOURNAL   Mol Biol Cell 5 (1), 57-70 (1994)
   PUBMED   8186465
REFERENCE   10 (residues 1 to 4307)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001486.5, AP003382.3,
            AP000817.4, AP002961.2, AP003461.2 and AP002829.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 13, 2010 this sequence version replaced NP_001368.1.
            
            Summary: This gene encodes a large cytoplasmic dynein protein that
            is involved in retrograde transport in the cilium and has a role in
            intraflagellar transport, a process required for ciliary/flagellar
            assembly. Mutations in this gene cause a heterogeneous spectrum of
            conditions related to altered primary cilium function and often
            involve polydactyly, abnormal skeletogenesis, and polycystic
            kidneys. Alternative splicing results in multiple transcript
            variants encoding distinct proteins. [provided by RefSeq, Jan
            2010].
            
            Transcript Variant: This variant (1) lacks an in-frame exon in the
            3' coding region, compared to variant 2. This results in a protein
            (isoform 1) that is seven aa shorter than isoform 2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB290167.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375735.7/ ENSP00000364887.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3"
     Protein         1..4307
                     /product="cytoplasmic dynein 2 heavy chain 1 isoform 1"
                     /note="cytoplasmic dynein 2 heavy chain 1; dynein heavy
                     chain 11; dynein heavy chain, isotype 1B; dynein,
                     cytoplasmic, heavy polypeptide 2; dynein cytoplasmic heavy
                     chain 2"
                     /calculated_mol_wt=492493
     Region          1..1650
                     /region_name="Stem. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          <234..674
                     /region_name="DHC_N1"
                     /note="Dynein heavy chain, N-terminal region 1; pfam08385"
                     /db_xref="CDD:462457"
     Region          1120..1518
                     /region_name="DHC_N2"
                     /note="Dynein heavy chain, N-terminal region 2; pfam08393"
                     /db_xref="CDD:462462"
     Region          <1361..4016
                     /region_name="DYN1"
                     /note="Dynein, heavy chain [Cytoskeleton]; COG5245"
                     /db_xref="CDD:227570"
     Region          1651..1986
                     /region_name="AAA_6"
                     /note="Hydrolytic ATP binding site of dynein motor region;
                     pfam12774"
                     /db_xref="CDD:463697"
     Region          1651..1875
                     /region_name="AAA 1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          1938..2161
                     /region_name="AAA 2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          2251..2505
                     /region_name="AAA 3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          2617..2863
                     /region_name="AAA 4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          2881..3169
                     /region_name="Stalk. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          3244..3473
                     /region_name="AAA 5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          3690..3905
                     /region_name="AAA 6. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCM8.4)"
     Region          4011..4304
                     /region_name="Dynein_C"
                     /note="Dynein heavy chain C-terminal domain; pfam18199"
                     /db_xref="CDD:465677"
     CDS             1..4307
                     /gene="DYNC2H1"
                     /gene_synonym="ATD3; DHC1b; DHC2; DNCH2; DYH1B; hdhc11;
                     SRPS2B; SRTD3"
                     /coded_by="NM_001377.3:150..13073"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53701.1"
                     /db_xref="GeneID:79659"
                     /db_xref="HGNC:HGNC:2962"
                     /db_xref="MIM:603297"
ORIGIN      
        1 mangtadvrk lfiftttqny fglmselwdq pllcnclein nflddgnqml lrvqrsdagi
       61 sfsntiefgd tkdkvlvffk lrpevitden lhdnilvssm lespisslyq avrqvfapml
      121 lkdqewsrnf dpklqnllse leaglgivlr rsdtnltklk fkeddtrgil tpsdefqfwi
      181 eqahrgnkqi skeranyfke lfetiarefy nldslsllev vdlvettqdv vddvwrqteh
      241 dhypesrmlh lldiiggsfg rfvqkklgtl nlwedpyylv keslkagisi ceqwvivcnh
      301 ltgqvwqryv phpwknekyf petldklgkr leevlairti hekflyflpa seekiicltr
      361 vfepftglnp vqynpytepl wkaavsqyek iiapaeqkia gklknyisei qdspqqllqa
      421 flkykelvkr ptiskelmle retllarlvd sikdfrldfe nrcrgipgda sgplsgknls
      481 evvnsivwvr qlelkvddti kiaeallsdl pgfrcfhqsa kdlldqlkly eqeqfddwsr
      541 diqsglsdsr sglcieassr imeldsndgl lkvhysdrlv illrevrqls algfvipaki
      601 qqvaniaqkf ckqaiilkqv ahfynsidqq miqsqrpmml qsalafeqii knskagsggk
      661 sqitwdnpke legyiqklqn aaerlatenr klrkwhttfc ekvvvlmnid llrqqqrwkd
      721 glqelrtgla tveaqgfqas dmhawkqhwn hqlykalehq yqmglealne nlpeinidlt
      781 ykqgrlqfrp pfeeirakyy remkrfigip nqfkgvgeag desifsimid rnasgfltif
      841 skaedlfrrl savlhqhkew ivigqvdmea lvekhlftvh dweknfkalk ikgkeverlp
      901 savkvdclni ncnpvktvid dliqklfdll vlslkksiqa hlheidtfvt eamevltimp
      961 qsveeigdan lqysklqerk peilplfqea edknrllrtv agggletisn lkakwdkfel
     1021 mmeshqlmik dqievmkgnv ksrlqiyyqe lekfkarwdq lkpgddviet gqhntldksa
     1081 klikekkief ddlevtrkkl vddchhfrle epnfslassi skdiescaqi wafyeefqqg
     1141 fqemanedwi tfrtktylfe eflmnwhdrl rkveehsvmt vklqsevdky kivipilkyv
     1201 rgehlspdhw ldlfrllglp rgtslekllf gdllrvadti vakaadlkdl nsraqgevti
     1261 realreldlw gvgavftlid yedsqsrtmk likdwkdivn qvgdnrcllq slkdspyykg
     1321 fedkvsiwer klaeldeylq nlnhiqrkwv ylepifgrga lpkeqtrfnr vdedfrsimt
     1381 dikkdnrvtt ltthagirns lltildqlqr cqkslnefle ekrsafprfy figdddllei
     1441 lgqstnpsvi qshlkklfag insvcfdeks khitamksle gevvpfknkv plsnnvetwl
     1501 ndlalemkkt leqllkecvt tgrssqgavd pslfpsqilc laeqikfted venaikdhsl
     1561 hqietqlvnk leqytnidts sedpgntesg ilelklkali ldiihnidvv kqlnqiqvht
     1621 tedwawkkql rfymksdhtc cvqmvdsefq ytyeyqgnas klvytpltdk cyltltqamk
     1681 mglggnpygp agtgktesvk alggllgrqv lvfncdegid vksmgrifvg lvkcgawgcf
     1741 defnrleesv lsavsmqiqt iqdalknhrt vcellgkeve vnsnsgifit mnpagkgygg
     1801 rqklpdnlkq lfrpvamshp dneliaevil ysegfkdakv lsrklvaifn lsrelltpqq
     1861 hydwglralk tvlrgsgnll rqlnksgttq naneshivvq alrlntmskf tftdctrfda
     1921 likdvfpgie lkeveydels aalkqvfeea nyeiipnqik kalelyeqlc qrmgvvivgp
     1981 sgagkstlwr mlraalcktg kvvkqytmnp kampryqllg hidmdtrews dgvltnsarq
     2041 vvrepqdvss wiicdgdidp ewieslnsvl ddnrlltmps geriqfgpnv nfvfethdls
     2101 caspatisrm gmiflsdeet dlnslikswl rnqpaeyrnn lenwigdyfe kalqwvlkqn
     2161 dyvvetslvg tvmnglshlh gcrdhdefii nlirglggnl nmksrleftk evfhwaresp
     2221 pdfhkpmdty ydstrgrlat yvlkkpedlt addfsngltl pviqtpdmqr gldyfkpwls
     2281 sdtkqpfilv gpegcgkgml lryafsqlrs tqiatvhcsa qttsrhllqk lsqtcmvist
     2341 ntgrvyrpkd cerlvlylkd inlpkldkwg tstlvaflqq vltyqgfyde nlewvgleni
     2401 qivasmsagg rlgrhklttr ftsivrlcsi dypereqlqt iygaylepvl hknlknhsiw
     2461 gssskiylla gsmvqvyeqv rakftvddys hyfftpcilt qwvlglfryd leggssnhpl
     2521 dyvleivaye arrlfrdkiv gakelhlfdi iltsvfqgdw gsdildnmsd sfyvtwgarh
     2581 nsgaraapgq plpphgkplg klnstdlkdv ikkglihygr dnqnldillf hevleymsri
     2641 drvlsfpggs lllagrsgvg rrtitslvsh mhgavlfspk isrgyelkqf kndlkhvlql
     2701 agieaqqvvl lledyqfvhp tfleminsll ssgevpglyt leeleplllp lkdqasqdgf
     2761 fgpvfnyfty riqqnlhivl imdsansnfm incesnpalh kkcqvlwmeg wsnssmkkip
     2821 emlfsetggg ekyndkkrke ekkknsvdpd flksfllihe sckaygatps rymtflhvys
     2881 aissskkkel lkrqshlqag vsklneakal vdelnrkage qsvllktkqd eadaalqmit
     2941 vsmqdaseqk telerlkhri aeevvkieer knkiddelke vqplvneakl avgnikpesl
     3001 seirslrmpp dvirdilegv lrlmgifdts wvsmksflak rgvrediatf darniskeir
     3061 esveellfkn kgsfdpknak rastaaapla awvkaniqys hvlerihple teqaglesnl
     3121 kktedrkrkl eellnsvgqk vselkekfqs rtseaaklea evskaqetik aaevlinqld
     3181 rehkrwnaqv veiteelatl pkraqlaaaf itylsaapes lrktcleewt ksaglekfdl
     3241 rrflcteseq liwkseglps ddlsienalv ilqsrvcpfl idpssqatew lkthlkdsrl
     3301 evinqqdsnf italelavrf gktliiqemd gvepvlypll rrdlvaqgpr yvvqigdkii
     3361 dyneefrlfl strnpnpfip pdaasivtev nftttrsglr gqllaltiqh ekpdleeqkt
     3421 kllqqeedkk iqlakleesl letlatsqgn ilenkdlies lnqtkassal iqeslkesyk
     3481 lqisldqerd aylplaesas kmyfiisdls kinnmyrfsl aaflrlfqra lqnkqdsent
     3541 eqriqsliss lqhmvyeyic rclfkadqlm falhfvrgmh pelfqenewd tftgvvvgdm
     3601 lrkadsqqki rdqlpswidq erswavatlk ialpslyqtl cfedaalwrt yynnsmceqe
     3661 fpsilakkvs lfqqilvvqa lrpdrlqsam alfacktlgl kevsplplnl krlyketlei
     3721 epiliiispg adpsqelqel anaersgecy hqvamgqgqa dlaiqmlkec arngdwlclk
     3781 nlhlvvswlp vlekelntlq pkdtfrlwlt aevhpnftpi llqsslkity esppglkknl
     3841 mrtyeswtpe qiskkdnthr ahalfslawf haacqerrny ipqgwtkfye fslsdlragy
     3901 niidrlfdga kdvqwefvhg llenaiyggr idnyfdlrvl qsylkqffns svidvfnqrn
     3961 kksifpysvs lpqscsildy raviekiped dkpsffglpa niarssqrmi ssqvisqlri
     4021 lgrsitagsk fdreiwsnel spvlnlwkkl nqnsnlihqk vpppndrqgs pilsfiileq
     4081 fnairlvqsv hqslaalskv irgttllsse vqklasalln qkcplawqsk wegpedplqy
     4141 lrglvarala iqnwvdkaek qallsetldl selfhpdtfl nalrqetara vgrsvdslkf
     4201 vaswkgrlqe aklqikisgl llegcsfdgn qlsenqldsp svssvlpcfm gwipqdacgp
     4261 yspdecislp vytsaerdrv vtnidvpcgg nqdqwiqcga alflknq
//
LOCUS       NP_006510                113 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein light chain Tctex-type 1 isoform 1 [Homo sapiens].
ACCESSION   NP_006510
VERSION     NP_006510.1
DBSOURCE    REFSEQ: accession NM_006519.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Schwarzer,C., Barnikol-Watanabe,S., Thinnes,F.P. and Hilschmann,N.
  TITLE     Voltage-dependent anion-selective channel (VDAC) interacts with the
            dynein light chain Tctex1 and the heat-shock protein PBP74
  JOURNAL   Int J Biochem Cell Biol 34 (9), 1059-1070 (2002)
   PUBMED   12009301
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Mueller,S., Cao,X., Welker,R. and Wimmer,E.
  TITLE     Interaction of the poliovirus receptor CD155 with the dynein light
            chain Tctex-1 and its implication for poliovirus pathogenesis
  JOURNAL   J Biol Chem 277 (10), 7897-7904 (2002)
   PUBMED   11751937
  REMARK    GeneRIF: Association with Tctex-1 and, hence, with the dynein motor
            complex may offer an explanation for how poliovirus hijacks the
            cellular transport machinery to retrogradely ascend along the axon
            to the neuronal cell body.
REFERENCE   7  (residues 1 to 113)
  AUTHORS   Strovel,E.T., Wu,D. and Sussman,D.J.
  TITLE     Protein phosphatase 2Calpha dephosphorylates axin and activates
            LEF-1-dependent transcription
  JOURNAL   J Biol Chem 275 (4), 2399-2403 (2000)
   PUBMED   10644691
REFERENCE   8  (residues 1 to 113)
  AUTHORS   Nagano,F., Orita,S., Sasaki,T., Naito,A., Sakaguchi,G., Maeda,M.,
            Watanabe,T., Kominami,E., Uchiyama,Y. and Takai,Y.
  TITLE     Interaction of Doc2 with tctex-1, a light chain of cytoplasmic
            dynein. Implication in dynein-dependent vesicle transport
  JOURNAL   J Biol Chem 273 (46), 30065-30068 (1998)
   PUBMED   9804756
REFERENCE   9  (residues 1 to 113)
  AUTHORS   King,S.M., Dillman,J.F. 3rd, Benashski,S.E., Lye,R.J.,
            Patel-King,R.S. and Pfister,K.K.
  TITLE     The mouse t-complex-encoded protein Tctex-1 is a light chain of
            brain cytoplasmic dynein
  JOURNAL   J Biol Chem 271 (50), 32281-32287 (1996)
   PUBMED   8943288
REFERENCE   10 (residues 1 to 113)
  AUTHORS   Watanabe,T.K., Fujiwara,T., Shimizu,F., Okuno,S., Suzuki,M.,
            Takahashi,E., Nakamura,Y. and Hirai,Y.
  TITLE     Cloning, expression, and mapping of TCTEL1, a putative human
            homologue of murine Tcte1, to 6q
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 153-156 (1996)
   PUBMED   8646886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY171700.1, AL589931.14,
            BC105588.1 and BU675683.1.
            
            Summary: This gene encodes a component of the motor complex,
            cytoplasmic dynein, which transports cellular cargo along
            microtubules in the cell. The encoded protein regulates the length
            of primary cilia which are sensory organelles found on the surface
            of cells. The protein encoded by this gene interacts with viral
            proteins, like the minor capsid protein L2 of human papillomavirus,
            and is required for dynein-mediated delivery of the viral nucleic
            acid to the host nucleus. This protein interacts with oncogenic
            nucleoporins to disrupt gene regulation and cause leukemic
            transformation. Pseudogenes of this gene are present on chromosomes
            4 and 17. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Apr
            2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.123843.1,
                                           SRR5189661.171423.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367089.8/ ENSP00000356056.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..113
                     /product="dynein light chain Tctex-type 1 isoform 1"
                     /note="t-complex-associated-testis-expressed 1-like 1;
                     T-complex testis-specific protein 1 homolog"
                     /calculated_mol_wt=12321
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P63172.1)"
     Region          12..113
                     /region_name="DLC-like_DYNLT1"
                     /note="dynein light chain (DLC)-like domain found in
                     dynein light chain Tctex-type 1 (DYNLT1) and similar
                     proteins; cd21462"
                     /db_xref="CDD:412010"
     Region          41..113
                     /region_name="Interaction with GNB1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P63172.1)"
     Site            order(62,64..70,74..84,86,90,109,111)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:412010"
     CDS             1..113
                     /gene="DYNLT1"
                     /gene_synonym="CW-1; TCTEL1; tctex-1; TCTEX1"
                     /coded_by="NM_006519.4:36..377"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5257.1"
                     /db_xref="GeneID:6993"
                     /db_xref="HGNC:HGNC:11697"
                     /db_xref="MIM:601554"
ORIGIN      
        1 medyqaaeet afvvdevsni vkeaiesaig gnayqhskvn qwttnvveqt lsqltklgkp
       61 fkyivtcvim qkngaglhta sscfwdsstd gsctvrwenk tmycivsafg lsi
//
LOCUS       NP_001355048             380 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 3 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001355048
VERSION     NP_001355048.1
DBSOURCE    REFSEQ: accession NM_001368119.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Ergun,S., Guney,S., Temiz,E., Petrovic,N. and Gunes,S.
  TITLE     Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
  JOURNAL   Anticancer Agents Med Chem 18 (12), 1695-1701 (2018)
   PUBMED   30019650
  REMARK    GeneRIF: Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Jin,L., Wang,T., Jiang,S., Chen,M., Zhang,R., Hu,C., Jia,W. and
            Liu,Z.
  TITLE     The Association of a Genetic Variant in SCAF8-CNKSR3 with Diabetic
            Kidney Disease and Diabetic Retinopathy in a Chinese Population
  JOURNAL   J Diabetes Res 2017, 6542689 (2017)
   PUBMED   28401168
  REMARK    GeneRIF: SCAF8-CNKSR3 variant rs955333 was not associated with
            diabetic kidney disease but showed association with diabetic
            retinopathy in Chinese type 2 diabetes patients
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Lake,S.L., Damato,B.E., Kalirai,H., Dodson,A.R., Taktak,A.F.,
            Lloyd,B.H. and Coupland,S.E.
  TITLE     Single nucleotide polymorphism array analysis of uveal melanomas
            reveals that amplification of CNKSR3 is correlated with improved
            patient survival
  JOURNAL   Am J Pathol 182 (3), 678-687 (2013)
   PUBMED   23357503
  REMARK    GeneRIF: Cox regression and Kaplan-Meier survival analysis
            identified that amplification of the CNKSR3 gene (log-rank, P =
            0.022) with an associated increase in its protein expression
            (log-rank, P = 0.011) correlated with longer patient survival.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Okada,Y., Sim,X., Go,M.J., Wu,J.Y., Gu,D., Takeuchi,F.,
            Takahashi,A., Maeda,S., Tsunoda,T., Chen,P., Lim,S.C., Wong,T.Y.,
            Liu,J., Young,T.L., Aung,T., Seielstad,M., Teo,Y.Y., Kim,Y.J.,
            Lee,J.Y., Han,B.G., Kang,D., Chen,C.H., Tsai,F.J., Chang,L.C.,
            Fann,S.J., Mei,H., Rao,D.C., Hixson,J.E., Chen,S., Katsuya,T.,
            Isono,M., Ogihara,T., Chambers,J.C., Zhang,W., Kooner,J.S.,
            Albrecht,E., Yamamoto,K., Kubo,M., Nakamura,Y., Kamatani,N.,
            Kato,N., He,J., Chen,Y.T., Cho,Y.S., Tai,E.S. and Tanaka,T.
  CONSRTM   KidneyGen Consortium; CKDGen Consortium; GUGC consortium
  TITLE     Meta-analysis identifies multiple loci associated with kidney
            function-related traits in east Asian populations
  JOURNAL   Nat Genet 44 (8), 904-909 (2012)
   PUBMED   22797727
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Shin,S., Park,J.S., Kim,Y.J., Oh,T., An,S. and Park,C.S.
  TITLE     Differential gene expression profile in PBMCs from subjects with
            AERD and ATA: a gene marker for AERD
  JOURNAL   Mol Genet Genomics 287 (5), 361-371 (2012)
   PUBMED   22457146
  REMARK    GeneRIF: two gene markers (CNKSR3 and SPTBN2) differentiate between
            aspirin-exacerbated respiratory disease and aspirin-tolerant asthma
            with a perfect discriminative power
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Pankratz,N., Beecham,G.W., DeStefano,A.L., Dawson,T.M.,
            Doheny,K.F., Factor,S.A., Hamza,T.H., Hung,A.Y., Hyman,B.T.,
            Ivinson,A.J., Krainc,D., Latourelle,J.C., Clark,L.N., Marder,K.,
            Martin,E.R., Mayeux,R., Ross,O.A., Scherzer,C.R., Simon,D.K.,
            Tanner,C., Vance,J.M., Wszolek,Z.K., Zabetian,C.P., Myers,R.H.,
            Payami,H., Scott,W.K. and Foroud,T.
  CONSRTM   PD GWAS Consortium
  TITLE     Meta-analysis of Parkinson's disease: identification of a novel
            locus, RIT2
  JOURNAL   Ann Neurol 71 (3), 370-384 (2012)
   PUBMED   22451204
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Attar,M.A., Salem,J.C., Pursel,H.S. and Santy,L.C.
  TITLE     CNK3 and IPCEF1 produce a single protein that is required for HGF
            dependent Arf6 activation and migration
  JOURNAL   Exp Cell Res 318 (3), 228-237 (2012)
   PUBMED   22085542
  REMARK    GeneRIF: CNK3 and IPCEF1 produce a single protein that is required
            for HGF dependent Arf6 activation and migration.
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Ziera,T., Irlbacher,H., Fromm,A., Latouche,C., Krug,S.M., Fromm,M.,
            Jaisser,F. and Borden,S.A.
  TITLE     Cnksr3 is a direct mineralocorticoid receptor target gene and plays
            a key role in the regulation of the epithelial sodium channel
  JOURNAL   FASEB J 23 (11), 3936-3946 (2009)
   PUBMED   19567370
  REMARK    GeneRIF: CNKSR3, a homologue of scaffold proteins involved in MAPK
            pathway regulation, is a direct target of MR and is required for
            the maintenance of transepithelial sodium transport in the kidney.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY328894.1 and AL357075.17.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY328894.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.2"
     Protein         1..380
                     /product="connector enhancer of kinase suppressor of ras 3
                     isoform 5"
                     /note="connector enhancer of kinase suppressor of ras 3;
                     membrane associated guanylate kinase, WW and PDZ domain
                     containing 1; maguin-like protein; CNK homolog protein 3;
                     connector enhancer of KSR 3; membrane-associated guanylate
                     kinase-interacting protein-like 1"
                     /calculated_mol_wt=41973
     Region          35..115
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(47..53,63,66,96,100,103..104)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          157..370
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     CDS             1..380
                     /gene="CNKSR3"
                     /gene_synonym="CNK3; CNK3/IPCEF1; MAGI1"
                     /coded_by="NM_001368119.1:314..1456"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:154043"
                     /db_xref="HGNC:HGNC:23034"
                     /db_xref="MIM:617476"
ORIGIN      
        1 medkvltvvk vlngicdkti rsttdpvmsq cacleevhlp nikpgeglgm yikstydglh
       61 vitgttensp adrsqkihag deviqvnqqt vvgwqlknlv kklrenptgv vlllkkrptg
      121 sfnftpaplk nlrwkpplvq tspppattqs pestmdtslk keksaildly ippppavpys
      181 prdengsfvy ggsskckqpl pgpkgsespn sfldqesrrr rftiadsdql pgysvetnil
      241 ptkmrektps ygkprplsmp adgnwmgivd pfarprghgr kgedalcryf snerippiie
      301 esssppyrfs rptterhlvr gadyirgsrc yinsdlhssa tipfqeegtk kksgssatks
      361 sstepsllvs wftrlkllth
//
LOCUS       NP_056219                907 aa            linear   PRI 20-NOV-2025
DEFINITION  whirlin isoform 1 [Homo sapiens].
ACCESSION   NP_056219 XP_027012
VERSION     NP_056219.3
DBSOURCE    REFSEQ: accession NM_015404.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   AitRaise,I., Amalou,G., Redouane,S., Charoute,H., Snoussi,K.,
            Abdelghaffar,H., Bonnet,C., Petit,C. and Barakat,A.
  TITLE     Novel pathogenic WHRN variant causing hearing loss in a moroccan
            family
  JOURNAL   Mol Biol Rep 50 (12), 10663-10669 (2023)
   PUBMED   37924449
  REMARK    GeneRIF: Novel pathogenic WHRN variant causing hearing loss in a
            moroccan family.
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Visconti,L., Malagrino,F., Troilo,F., Pagano,L., Toto,A. and
            Gianni,S.
  TITLE     Folding and Misfolding of a PDZ Tandem Repeat
  JOURNAL   J Mol Biol 433 (7), 166862 (2021)
   PUBMED   33539879
  REMARK    GeneRIF: Folding and Misfolding of a PDZ Tandem Repeat.
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Lin,L., Shi,Y., Wang,M., Wang,C., Lu,Q., Zhu,J. and Zhang,R.
  TITLE     Phase separation-mediated condensation of Whirlin-Myo15-Eps8
            stereocilia tip complex
  JOURNAL   Cell Rep 34 (8), 108770 (2021)
   PUBMED   33626355
  REMARK    GeneRIF: Phase separation-mediated condensation of
            Whirlin-Myo15-Eps8 stereocilia tip complex.
REFERENCE   5  (residues 1 to 907)
  AUTHORS   van Wijk,E., van der Zwaag,B., Peters,T., Zimmermann,U., Te
            Brinke,H., Kersten,F.F., Marker,T., Aller,E., Hoefsloot,L.H.,
            Cremers,C.W., Cremers,F.P., Wolfrum,U., Knipper,M., Roepman,R. and
            Kremer,H.
  TITLE     The DFNB31 gene product whirlin connects to the Usher protein
            network in the cochlea and retina by direct association with USH2A
            and VLGR1
  JOURNAL   Hum Mol Genet 15 (5), 751-765 (2006)
   PUBMED   16434480
  REMARK    GeneRIF: This paper concludes that this protein plays a role in
            photoreceptor and hair cell synapse organization in the related rat
            gene.
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Mburu,P., Mustapha,M., Varela,A., Weil,D., El-Amraoui,A.,
            Holme,R.H., Rump,A., Hardisty,R.E., Blanchard,S., Coimbra,R.S.,
            Perfettini,I., Parkinson,N., Mallon,A.M., Glenister,P.,
            Rogers,M.J., Paige,A.J., Moir,L., Clay,J., Rosenthal,A., Liu,X.Z.,
            Blanco,G., Steel,K.P., Petit,C. and Brown,S.D.
  TITLE     Defects in whirlin, a PDZ domain molecule involved in stereocilia
            elongation, cause deafness in the whirler mouse and families with
            DFNB31
  JOURNAL   Nat Genet 34 (4), 421-428 (2003)
   PUBMED   12833159
  REMARK    GeneRIF: Defects in whirlin, a PDZ domain molecule involved in
            stereocilia elongation, cause deafness in the whirler mouse and
            families with DFNB31.
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Yap,C.C., Liang,F., Yamazaki,Y., Muto,Y., Kishida,H., Hayashida,T.,
            Hashikawa,T. and Yano,R.
  TITLE     CIP98, a novel PDZ domain protein, is expressed in the central
            nervous system and interacts with calmodulin-dependent serine
            kinase
  JOURNAL   J Neurochem 85 (1), 123-134 (2003)
   PUBMED   12641734
  REMARK    GeneRIF: This paper describes a PDZ domain protein and its role in
            synaptic transmission in the related rat gene.
REFERENCE   8  (residues 1 to 907)
  AUTHORS   Mustapha,M., Chouery,E., Chardenoux,S., Naboulsi,M., Paronnaud,J.,
            Lemainque,A., Megarbane,A., Loiselet,J., Weil,D., Lathrop,M. and
            Petit,C.
  TITLE     DFNB31, a recessive form of sensorineural hearing loss, maps to
            chromosome 9q32-34
  JOURNAL   Eur J Hum Genet 10 (3), 210-212 (2002)
   PUBMED   11973626
REFERENCE   9  (residues 1 to 907)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 907)
  AUTHORS   Koenekoop,R., Arriaga,M., Trzupek,K.M. and Lentz,J.
  TITLE     Usher Syndrome Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138895.16, BC142614.1,
            BC142684.1 and BC136416.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 5, 2010 this sequence version replaced NP_056219.2.
            
            Summary: This gene is thought to function in the organization and
            stabilization of sterocilia elongation and actin cystoskeletal
            assembly, based on studies of the related mouse gene. Mutations in
            this gene have been associated with autosomal recessive
            non-syndromic deafness and Usher Syndrome. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Nov
            2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142614.1, AB040959.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000362057.4/ ENSP00000354623.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..907
                     /product="whirlin isoform 1"
                     /note="CASK-interacting protein CIP98; autosomal recessive
                     deafness type 31 protein"
                     /calculated_mol_wt=96427
     Region          37..112
                     /region_name="HN_L-whirlin_R1_like"
                     /note="first harmonin_N_like domain (repeat 1) of the long
                     isoform of whirlin, and related domains; cd07356"
                     /db_xref="CDD:259822"
     Site            order(39,43,56,59,62..63,66)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259822"
     Region          138..219
                     /region_name="PDZ1_FL-whirlin"
                     /note="PDZ domain 1 of the full-length isoform of whirlin
                     and related domains; cd06740"
                     /db_xref="CDD:467222"
     Site            order(151..157,169,172,201,205,208..209)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467222"
     Region          243..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          277..360
                     /region_name="PDZ2_FL-whirlin"
                     /note="PDZ domain 2 of the full-length isoform of whirlin
                     and related domains; cd06741"
                     /db_xref="CDD:467223"
     Site            order(289..295,307,310,339,343,346..347)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467223"
     Region          419..499
                     /region_name="HN_L-whirlin_R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of the
                     long isoform of whirlin, and related domains; cd07357"
                     /db_xref="CDD:259823"
     Site            order(420,423,427,440,443,446..447,450)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259823"
     Region          502..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          565..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          <581..>817
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          684..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          742..815
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          814..904
                     /region_name="PDZ3_FL-whirlin-like"
                     /note="PDZ domain 3 of the full-length isoform of whirlin,
                     PDZ domain 1 of the short isoform of whirlin, and related
                     domains; cd06742"
                     /db_xref="CDD:467224"
     Site            order(825..831,844,847,877,881,884..885)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467224"
     CDS             1..907
                     /gene="WHRN"
                     /gene_synonym="CIP98; DFNB31; PDZD7B; USH2D; WI"
                     /coded_by="NM_015404.4:673..3396"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6806.1"
                     /db_xref="GeneID:25861"
                     /db_xref="HGNC:HGNC:16361"
                     /db_xref="MIM:607928"
ORIGIN      
        1 mnapldglsv sssstgslgs aagaggggga glrllsanvr qlhqaltall seaereqfth
       61 clnayharrn vfdlvrtlrv lldspvkrrl lpmlrlvipr sdqllfdqyt aeglylpatt
      121 pyrqpawggp dsagpgevrl vslrrakahe glgfsirggs ehgvgiyvsl vepgslaeke
      181 glrvgdqilr vndkslarvt haeavkalkg skklvlsvys agripggyvt nhiytwvdpq
      241 grsisppsgl pqphggalrq qegdrrstlh llqggdekkv nlvlgdgrsl gltirggaey
      301 glgiyitgvd pgseaegsgl kvgdqilevn grsflnilhd eavrllkssr hliltvkdvg
      361 rlpharttvd etkwiassri retmansagf lgdlttegin kpgfykgpag sqvtlsslgn
      421 qtrvlleeqa rhllneqeha tmayyldeyr ggsvsvealv malfkllnth akfsllsevr
      481 gtispqdler fdhlvlrrei esmkarqppg pgagdtysmv sysdtgsstg shgtsttvss
      541 arntldleet geavqgnina lpdvsvddvr stsqglssfk plprppplaq gndlplgqpr
      601 klgredlqpp ssmpscsgtv fsapqnrspp agtaptpgts saqdlpsspi yasvspanps
      661 skrpldahla lvnqhpigpf prvqspphlk spsaeatvag gcllppspsg hpdqtgtnqh
      721 fvmvevhrpd sepdvnevra lpqtrtastl sqlsdsgqtl sedsgvdage aeasapgrgr
      781 qsvstksrss kelprnerpt dgankppgll eptstlvrvk ksaatlgiai eggantrqpl
      841 privtiqrgg sahncgqlkv ghvilevngl tlrgkehrea ariiaeafkt kdrdyidflv
      901 tefnvml
//
LOCUS       NP_689889                434 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 15 isoform 1 [Homo sapiens].
ACCESSION   NP_689889
VERSION     NP_689889.1
DBSOURCE    REFSEQ: accession NM_152676.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Zhao,Y., Shim,N., Cui,Y.H., Kang,J.H., Yoo,K.C., Kim,S., Yi,J.M.,
            Kim,M.J., Yoon,J.H. and Lee,S.J.
  TITLE     FBXO15 plays a critical suppressive functional role in regulation
            of breast cancer progression
  JOURNAL   Signal Transduct Target Ther 6 (1), 211 (2021)
   PUBMED   34083507
  REMARK    GeneRIF: FBXO15 plays a critical suppressive functional role in
            regulation of breast cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Zeng,Z., Feingold,E., Wang,X., Weeks,D.E., Lee,M., Cuenco,D.T.,
            Broffitt,B., Weyant,R.J., Crout,R., McNeil,D.W., Levy,S.M.,
            Marazita,M.L. and Shaffer,J.R.
  TITLE     Genome-wide association study of primary dentition pit-and-fissure
            and smooth surface caries
  JOURNAL   Caries Res 48 (4), 330-338 (2014)
   PUBMED   24556642
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Simino,J., Sung,Y.J., Kume,R., Schwander,K. and Rao,D.C.
  TITLE     Gene-alcohol interactions identify several novel blood pressure
            loci including a promising locus near SLC16A9
  JOURNAL   Front Genet 4, 277 (2013)
   PUBMED   24376456
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Porcu,E., Medici,M., Pistis,G., Volpato,C.B., Wilson,S.G.,
            Cappola,A.R., Bos,S.D., Deelen,J., den Heijer,M., Freathy,R.M.,
            Lahti,J., Liu,C., Lopez,L.M., Nolte,I.M., O'Connell,J.R.,
            Tanaka,T., Trompet,S., Arnold,A., Bandinelli,S., Beekman,M.,
            Bohringer,S., Brown,S.J., Buckley,B.M., Camaschella,C., de
            Craen,A.J., Davies,G., de Visser,M.C., Ford,I., Forsen,T.,
            Frayling,T.M., Fugazzola,L., Gogele,M., Hattersley,A.T.,
            Hermus,A.R., Hofman,A., Houwing-Duistermaat,J.J., Jensen,R.A.,
            Kajantie,E., Kloppenburg,M., Lim,E.M., Masciullo,C., Mariotti,S.,
            Minelli,C., Mitchell,B.D., Nagaraja,R., Netea-Maier,R.T.,
            Palotie,A., Persani,L., Piras,M.G., Psaty,B.M., Raikkonen,K.,
            Richards,J.B., Rivadeneira,F., Sala,C., Sabra,M.M., Sattar,N.,
            Shields,B.M., Soranzo,N., Starr,J.M., Stott,D.J., Sweep,F.C.,
            Usala,G., van der Klauw,M.M., van Heemst,D., van Mullem,A.,
            Vermeulen,S.H., Visser,W.E., Walsh,J.P., Westendorp,R.G., Widen,E.,
            Zhai,G., Cucca,F., Deary,I.J., Eriksson,J.G., Ferrucci,L.,
            Fox,C.S., Jukema,J.W., Kiemeney,L.A., Pramstaller,P.P.,
            Schlessinger,D., Shuldiner,A.R., Slagboom,E.P., Uitterlinden,A.G.,
            Vaidya,B., Visser,T.J., Wolffenbuttel,B.H., Meulenbelt,I.,
            Rotter,J.I., Spector,T.D., Hicks,A.A., Toniolo,D., Sanna,S.,
            Peeters,R.P. and Naitza,S.
  TITLE     A meta-analysis of thyroid-related traits reveals novel loci and
            gender-specific differences in the regulation of thyroid function
  JOURNAL   PLoS Genet 9 (2), e1003266 (2013)
   PUBMED   23408906
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Tokuzawa,Y., Kaiho,E., Maruyama,M., Takahashi,K., Mitsui,K.,
            Maeda,M., Niwa,H. and Yamanaka,S.
  TITLE     Fbx15 is a novel target of Oct3/4 but is dispensable for embryonic
            stem cell self-renewal and mouse development
  JOURNAL   Mol Cell Biol 23 (8), 2699-2708 (2003)
   PUBMED   12665572
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084702.4, BI829755.1,
            BC029579.1 and BU729305.1.
            
            Summary: Members of the F-box protein family, such as FBXO15, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the shorter protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029579.1, SRR3476690.651089.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.3"
     Protein         1..434
                     /product="F-box only protein 15 isoform 1"
                     /note="F-box only protein 15"
                     /calculated_mol_wt=49319
     Region          1..43
                     /region_name="F-box_FBXO15"
                     /note="F-box domain found in F-box only protein 15
                     (FBXO15) and similar proteins; cd22093"
                     /db_xref="CDD:438865"
     Site            order(1,5,8..9,12..13,17,19..20,24..26,28)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438865"
     CDS             1..434
                     /gene="FBXO15"
                     /gene_synonym="FBX15"
                     /coded_by="NM_152676.3:407..1711"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:201456"
                     /db_xref="HGNC:HGNC:13617"
                     /db_xref="MIM:609093"
ORIGIN      
        1 mpseillkif syldavsllc tgcvsrrfyh landnfiwig iystafspar snwkfnsvek
       61 iamsmsflsv qdkeagywkk eyitkqiasv kaaladilkp vnpytglpvk tkealrifgl
      121 gwaiilkekg gkeyimehvd lsindtsvtv iwygkkwpcl aslstldlcg mtpvftdwyk
      181 tptkhrlrwh sliakynlsh ltistmigcd rlirifclhp gllvgvwkke eelafvmanl
      241 hfhhlverst lgsatipyel pphspfldds peyglhgyql hvdlhsggvf ylcgtfrnlf
      301 tkrgniengh vklivihlkn nrehlpligk vglswktdif dgcikscsmm dvtlldehgk
      361 pfwcfsspvc lrspatpsds ssflgqtynv dyvdaegrvh velvwirete eylivnlvly
      421 lsiakinhwf gtey
//
LOCUS       NP_001356514             642 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform u [Homo sapiens].
ACCESSION   NP_001356514 XP_016881426
VERSION     NP_001356514.1
DBSOURCE    REFSEQ: accession NM_001369585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881426.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.234708.1,
                                           SRR1660803.116124.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..642
                     /product="transcription factor 4 isoform u"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68352
     Region          533..617
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(541,545,547..549,551,556,577..578)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(554..555,558..559,561..562,565,569,579,582,586,589,
                     592..597)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..642
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369585.1:156..2084"
                     /note="isoform u is encoded by transcript variant 45"
                     /db_xref="CCDS:CCDS86672.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqs llggdmdmgn pgtlsptkpg
      121 sqyyqyssnn prrrplhssa mevqtkkvrk vppglpssvy apsastadyn rdspgypssk
      181 patstfpssf fmqdghhssd pwssssgmnq pgyagmlgns shipqsssyc slhpherlsy
      241 pshssadins slppmstfhr sgtnhystss ctppangtds imanrgsgaa gssqtgdalg
      301 kalasiyspd htnnsfssnp stpvgsppsl sagtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit snnddedltp eqkaereker
      541 rmannarerl rvrdineafk elgrmvqlhl ksdkpqtkll ilhqavavil sleqqvrern
      601 lnpkaaclkr reeekvssep pplslagphp gmgdasnhmg qm
//
LOCUS       NP_004783                754 aa            linear   PRI 20-NOV-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase G [Homo sapiens].
ACCESSION   NP_004783
VERSION     NP_004783.2
DBSOURCE    REFSEQ: accession NM_004792.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Szlavicz,E., Szabo,K., Groma,G., Bata-Csorgo,Z., Pagani,F.,
            Kemeny,L. and Szell,M.
  TITLE     Splicing factors differentially expressed in psoriasis alter mRNA
            maturation of disease-associated EDA+ fibronectin
  JOURNAL   Mol Cell Biochem 436 (1-2), 189-199 (2017)
   PUBMED   28589370
  REMARK    GeneRIF: results indicate that LUC7L3, PPIG, and SFRS18 are not
            only implicated in EDA+ fibronectin formation, but also that they
            could possess multiple roles in psoriasis-associated molecular
            abnormalities.
            Erratum:[Mol Cell Biochem. 2017 Dec;436(1-2):201. doi:
            10.1007/s11010-017-3105-y. PMID: 28770468]
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Nakamura,K., Aizawa,K., Aung,K.H., Yamauchi,J. and Tanoue,A.
  TITLE     Zebularine upregulates expression of CYP genes through inhibition
            of DNMT1 and PKR in HepG2 cells
  JOURNAL   Sci Rep 7, 41093 (2017)
   PUBMED   28112215
  REMARK    GeneRIF: The finding that zebularine upregulates CYP gene
            expression through DNMT1 and PKR modulation sheds light on the
            mechanisms controlling hepatocyte function and thus may aid in the
            development of new in-vitro systems using high-functioning
            hepatocytes
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Dubourg,B., Kamphausen,T., Weiwad,M., Jahreis,G., Feunteun,J.,
            Fischer,G. and Modjtahedi,N.
  TITLE     The human nuclear SRcyp is a cell cycle-regulated cyclophilin
  JOURNAL   J Biol Chem 279 (21), 22322-22330 (2004)
   PUBMED   15016823
  REMARK    GeneRIF: human nuclear SRcyp is a cell cycle-regulated cyclophilin
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Bourquin,J.P., Stagljar,I., Meier,P., Moosmann,P., Silke,J.,
            Baechi,T., Georgiev,O. and Schaffner,W.
  TITLE     A serine/arginine-rich nuclear matrix cyclophilin interacts with
            the C-terminal domain of RNA polymerase II
  JOURNAL   Nucleic Acids Res 25 (11), 2055-2061 (1997)
   PUBMED   9153302
REFERENCE   10 (residues 1 to 754)
  AUTHORS   Nestel,F.P., Colwill,K., Harper,S., Pawson,T. and Anderson,S.K.
  TITLE     RS cyclophilins: identification of an NK-TR1-related cyclophilin
  JOURNAL   Gene 180 (1-2), 151-155 (1996)
   PUBMED   8973360
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG615922.1, X99717.1, CA418130.1 and AC016772.9.
            
            On Feb 17, 2004 this sequence version replaced NP_004783.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.83671.1,
                                           SRR1803617.72391.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260970.8/ ENSP00000260970.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..754
                     /product="peptidyl-prolyl cis-trans isomerase G"
                     /EC_number="5.2.1.8"
                     /note="Clk-associating RS-cyclophilin; peptidyl-prolyl
                     isomerase G (cyclophilin G); SR-related CTD-associated
                     factor 10; CASP10; SR-cyp; PPIase G; rotamase G;
                     SR-cyclophilin; CARS-cyclophilin"
                     /calculated_mol_wt=88486
     Region          8..175
                     /region_name="cyclophilin"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases. This family contains eukaryotic, bacterial and
                     archeal proteins which exhibit a peptidylprolyl cis- trans
                     isomerases activity (PPIase, Rotamase) and in addition
                     bind the immunosuppressive drug...; cl00197"
                     /db_xref="CDD:469651"
     Site            order(67,69,72..73,75,113..114,123,125,133..134,138)
                     /site_type="active"
                     /db_xref="CDD:238907"
     Region          182..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Region          <392..752
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13427.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            748
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13427.2)"
     CDS             1..754
                     /gene="PPIG"
                     /gene_synonym="CARS-Cyp; CYP; SCAF10; SRCyp"
                     /coded_by="NM_004792.3:210..2474"
                     /db_xref="CCDS:CCDS2235.1"
                     /db_xref="GeneID:9360"
                     /db_xref="HGNC:HGNC:14650"
                     /db_xref="MIM:606093"
ORIGIN      
        1 mgikvqrprc ffdiainnqp agrvvfelfs dvcpktcenf rclctgekgt gkstqkplhy
       61 ksclfhrvvk dfmvqggdfs egngrggesi yggffedesf avkhnkefll smanrgkdtn
      121 gsqffittkp tphldghhvv fgqvisgqev vreienqktd aaskpfaevr ilscgelipk
      181 skvkkeekkr hkssssssss ssdsdsssds qsssdssdse sateekskkr kkkhrknsrk
      241 hkkekkkrkk skksassese aenleaqpqs tvrpeeippi penrflmrks ppkadekerk
      301 nrerererec nppnsqpasy qrrllvtrsg rkikgrgprr yrtpsrsrsr drfrrsetpp
      361 hwrqemqraq rmrvssgerw ikgdkselne ikenqrspvr vkerkitdhr nvsespnrkn
      421 ekekkvkdhk snskerdirr nsekddkykn kvkkraksks rskskeksks kerdskhnrn
      481 eekrmrsrsk grdhenvkek ekqsdskgkd qersrskeks kqlesksneh dhskskekdr
      541 raqsrsrecd itkgkhsyns rtrersrsrd rsrrvrsrth drdrsrskey hryreqeyrr
      601 rgrsrsrerr tppgrsrskd rrrrrrdsrs sereesqsrn kdkyrnqesk sshrkenses
      661 ekrmysksrd hnssnnsrek kadrdqspfs kikqssqdne lkssmlknke dekirssvek
      721 enqkskgqen dhvheknkkf dhesspgtde dksg
//
LOCUS       NP_116172                237 aa            linear   PRI 20-NOV-2025
DEFINITION  3-oxoacyl-[acyl-carrier-protein] reductase [Homo sapiens].
ACCESSION   NP_116172
VERSION     NP_116172.2
DBSOURCE    REFSEQ: accession NM_032783.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Bains,O.S., Grigliatti,T.A., Reid,R.E. and Riggs,K.W.
  TITLE     Naturally occurring variants of human aldo-keto reductases with
            reduced in vitro metabolism of daunorubicin and doxorubicin
  JOURNAL   J Pharmacol Exp Ther 335 (3), 533-545 (2010)
   PUBMED   20837989
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Chen,Z., Kastaniotis,A.J., Miinalainen,I.J., Rajaram,V.,
            Wierenga,R.K. and Hiltunen,J.K.
  TITLE     17beta-hydroxysteroid dehydrogenase type 8 and carbonyl reductase
            type 4 assemble as a ketoacyl reductase of human mitochondrial FAS
  JOURNAL   FASEB J 23 (11), 3682-3691 (2009)
   PUBMED   19571038
  REMARK    GeneRIF: Hs17beta-HSD8 and HsCBR4 show a strong genetic interaction
            in vivo in yeast, where, only if they are expressed together, they
            rescue the respiratory deficiency and restore the lipoic acid
            content of oar1Delta cells.
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Endo,S., Matsunaga,T., Kitade,Y., Ohno,S., Tajima,K., El-Kabbani,O.
            and Hara,A.
  TITLE     Human carbonyl reductase 4 is a mitochondrial NADPH-dependent
            quinone reductase
  JOURNAL   Biochem Biophys Res Commun 377 (4), 1326-1330 (2008)
   PUBMED   19000905
  REMARK    GeneRIF: CBR4 is a mitochondrial NADPH-dependent reductase for o-
            and p-quinones.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA217727.1, AC021151.8, BC033650.1 and AL833393.1.
            
            On Dec 20, 2003 this sequence version replaced NP_116172.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833393.1, SRR1803614.275197.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306193.8/ ENSP00000303525.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q32.3"
     Protein         1..237
                     /product="3-oxoacyl-[acyl-carrier-protein] reductase"
                     /EC_number="1.1.1.100"
                     /EC_number="1.6.5.10"
                     /note="carbonic reductase 4; carbonyl reductase family
                     member 4; quinone reductase CBR4; KAR beta subunit; short
                     chain dehydrogenase/reductase family 45C member 1;
                     3-ketoacyl-[acyl-carrier-protein] reductase beta subunit"
                     /calculated_mol_wt=25170
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8N4T8.3)"
     Region          3..233
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     Site            order(9,11..12,14,33..35,83..85,133..135,148,152,178..181)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187594"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91VT4; propagated from
                     UniProtKB/Swiss-Prot (Q8N4T8.3)"
     Site            96
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91VT4; propagated from
                     UniProtKB/Swiss-Prot (Q8N4T8.3)"
     Site            order(107,135,148,152)
                     /site_type="active"
                     /db_xref="CDD:187594"
     Site            169
                     /site_type="other"
                     /note="Important for interaction with acyl carrier protein
                     (ACP). /evidence=ECO:0000305|PubMed:25203508; propagated
                     from UniProtKB/Swiss-Prot (Q8N4T8.3)"
     Site            195
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q91VT4; propagated from
                     UniProtKB/Swiss-Prot (Q8N4T8.3)"
     CDS             1..237
                     /gene="CBR4"
                     /gene_synonym="SDR45C1"
                     /coded_by="NM_032783.5:167..880"
                     /db_xref="CCDS:CCDS3812.1"
                     /db_xref="GeneID:84869"
                     /db_xref="HGNC:HGNC:25891"
                     /db_xref="MIM:619394"
ORIGIN      
        1 mdkvcavfgg srgigravaq lmarkgyrla viarnlegak aaagdlggdh lafscdvake
       61 hdvqntfeel ekhlgrvnfl vnaaginrdg llvrtktedm vsqlhtnllg smltckaamr
      121 tmiqqqggsi vnvgsivglk gnsgqsvysa skgglvgfsr alakevarkk irvnvvapgf
      181 vhtdmtkdlk eehlkknipl grfgetieva havvfllesp yitghvlvvd gglqlil
//
LOCUS       NP_056290                518 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM98A isoform 1 [Homo sapiens].
ACCESSION   NP_056290 XP_043885
VERSION     NP_056290.3
DBSOURCE    REFSEQ: accession NM_015475.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Wang,N., Guo,Y., Song,L., Tong,T. and Fan,X.
  TITLE     Circular RNA intraflagellar transport 80 facilitates endometrial
            cancer progression through modulating miR-545-3p/FAM98A signaling
  JOURNAL   J Gynecol Oncol 33 (1), e2 (2022)
   PUBMED   34783205
  REMARK    GeneRIF: Circular RNA intraflagellar transport 80 facilitates
            endometrial cancer progression through modulating miR-545-3p/FAM98A
            signaling.
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Li,Z., Li,N., Sun,X. and Wang,J.
  TITLE     FAM98A promotes cancer progression in endometrial carcinoma
  JOURNAL   Mol Cell Biochem 459 (1-2), 131-139 (2019)
   PUBMED   31114934
  REMARK    GeneRIF: Mechanistically, it was demonstrated that miR-142-3p
            directly targeted FAM98A, and modulated its expression.
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Schou,K.B., Andersen,J.S. and Pedersen,L.B.
  TITLE     A divergent calponin homology (NN-CH) domain defines a novel
            family: implications for evolution of ciliary IFT complex B
            proteins
  JOURNAL   Bioinformatics 30 (7), 899-902 (2014)
   PUBMED   24257188
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Popow,J., Englert,M., Weitzer,S., Schleiffer,A., Mierzwa,B.,
            Mechtler,K., Trowitzsch,S., Will,C.L., Luhrmann,R., Soll,D. and
            Martinez,J.
  TITLE     HSPC117 is the essential subunit of a human tRNA splicing ligase
            complex
  JOURNAL   Science 331 (6018), 760-764 (2011)
   PUBMED   21311021
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Yang,H.C., Liang,Y.J., Wu,Y.L., Chung,C.M., Chiang,K.M., Ho,H.Y.,
            Ting,C.T., Lin,T.H., Sheu,S.H., Tsai,W.C., Chen,J.H., Leu,H.B.,
            Yin,W.H., Chiu,T.Y., Chen,C.I., Fann,C.S., Wu,J.Y., Lin,T.N.,
            Lin,S.J., Chen,Y.T., Chen,J.W. and Pan,W.H.
  TITLE     Genome-wide association study of young-onset hypertension in the
            Han Chinese population of Taiwan
  JOURNAL   PLoS One 4 (5), e5459 (2009)
   PUBMED   19421330
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA310995.1, BC136768.1, BC060860.1 and AC017050.9.
            
            On Dec 17, 2004 this sequence version replaced NP_056290.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.107418.1,
                                           SRR3476690.402691.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238823.13/ ENSP00000238823.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..518
                     /product="protein FAM98A isoform 1"
                     /note="protein FAM98A"
                     /calculated_mol_wt=55142
     Region          28..327
                     /region_name="DUF2465"
                     /note="Protein of unknown function (DUF2465); pfam10239"
                     /db_xref="CDD:463016"
     Region          297..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCA5.2)"
     Region          434..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCA5.2)"
     CDS             1..518
                     /gene="FAM98A"
                     /coded_by="NM_015475.5:79..1635"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33179.1"
                     /db_xref="GeneID:25940"
                     /db_xref="HGNC:HGNC:24520"
                     /db_xref="MIM:620904"
ORIGIN      
        1 mecdlmetdi lesledlgyk gplledgals qavsagassp eftklcawlv selrvlckle
       61 envqatnsps eaeefqlevs gllgemncpy lsltsgdvtk rlliqkncll lltylisele
      121 aarmlcvnap pkkaqegggs evfqelkgic ialgmskppa nitmfqffsg iekklketla
      181 kvppnhvgkp llkkpmgpah wekieainqa ianeyevrrk llikrldvtv qsfgwsdrak
      241 sqteklakvy qpkrsvlspk ttisvahlla arqdlskilr tssgsirekt acainkvlmg
      301 rvpdrggrpn eieppppemp pwqkrqdgpq qqtggrgggr ggyehssygg rggheqgggr
      361 ggrggydhgg rgggrgnkhq ggwtdggsgg gggyqdggyr dsgfqpggyh gghssggyqg
      421 ggyggfqtss sytgsgyqgg gyqqdnryqd gghhgdrggg rggrggrggr ggragqgggw
      481 ggrgsqnyhq ggqfeqhfqh ggyqynhsgf gqgrhyts
//
LOCUS       NP_001341755             671 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator
            1-alpha isoform 4 [Homo sapiens].
ACCESSION   NP_001341755
VERSION     NP_001341755.1
DBSOURCE    REFSEQ: accession NM_001354826.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Liang,F. and Huang,S.
  TITLE     PGC-1alpha inhibits NLRP3 signaling through transcriptional
            activation of POP1 to alleviate inflammation and strengthen
            osteogenic differentiation of lipopolysaccharide-induced human
            periodontal stem cells
  JOURNAL   Prostaglandins Other Lipid Mediat 174, 106853 (2024)
   PUBMED   38763227
  REMARK    GeneRIF: PGC-1alpha inhibits NLRP3 signaling through
            transcriptional activation of POP1 to alleviate inflammation and
            strengthen osteogenic differentiation of lipopolysaccharide-induced
            human periodontal stem cells.
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Kuang,J., Fang,J., Hu,S., Yang,X. and Fan,X.
  TITLE     MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS OF
            SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF PGC-1Alpha
  JOURNAL   Shock 62 (3), 426-436 (2024)
   PUBMED   38888503
  REMARK    GeneRIF: MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS
            OF SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF
            PGC-1Alpha.
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Mesarosova,L., Scheper,M., Iyer,A., Anink,J.J., Mills,J.D. and
            Aronica,E.
  TITLE     miR-193b-3p/ PGC-1alpha pathway regulates an insulin dependent
            anti-inflammatory response in Parkinson's disease
  JOURNAL   Neurobiol Dis 199, 106587 (2024)
   PUBMED   38950713
  REMARK    GeneRIF: miR-193b-3p/ PGC-1alpha pathway regulates an insulin
            dependent anti-inflammatory response in Parkinson's disease.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Yu,T., Gao,Q., Zhang,G., Li,T., Liu,X., Li,C., Zheng,L., Sun,X.,
            Wu,J., Cao,H., Bi,F., Wang,R., Liang,H., Li,X., Zhou,Y., Lv,L. and
            Shan,H.
  TITLE     lncRNA Gm20257 alleviates pathological cardiac hypertrophy by
            modulating the PGC-1alpha-mitochondrial complex IV axis
  JOURNAL   Front Med 18 (4), 664-677 (2024)
   PUBMED   38926249
  REMARK    GeneRIF: lncRNA Gm20257 alleviates pathological cardiac hypertrophy
            by modulating the PGC-1alpha-mitochondrial complex IV axis.
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Zhou,S., Taskintuna,K., Hum,J., Gulati,J., Olaya,S., Steinman,J.
            and Golestaneh,N.
  TITLE     PGC-1alpha repression dysregulates lipid metabolism and induces
            lipid droplet accumulation in retinal pigment epithelium
  JOURNAL   Cell Death Dis 15 (6), 385 (2024)
   PUBMED   38824126
  REMARK    GeneRIF: PGC-1alpha repression dysregulates lipid metabolism and
            induces lipid droplet accumulation in retinal pigment epithelium.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Esterbauer,H., Oberkofler,H., Krempler,F. and Patsch,W.
  TITLE     Human peroxisome proliferator activated receptor gamma coactivator
            1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
            localization, and tissue expression
  JOURNAL   Genomics 62 (1), 98-102 (1999)
   PUBMED   10585775
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Puigserver,P., Adelmant,G., Wu,Z., Fan,M., Xu,J., O'Malley,B. and
            Spiegelman,B.M.
  TITLE     Activation of PPARgamma coactivator-1 through transcription factor
            docking
  JOURNAL   Science 286 (5443), 1368-1371 (1999)
   PUBMED   10558993
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Wu,Z., Puigserver,P., Andersson,U., Zhang,C., Adelmant,G.,
            Mootha,V., Troy,A., Cinti,S., Lowell,B., Scarpulla,R.C. and
            Spiegelman,B.M.
  TITLE     Mechanisms controlling mitochondrial biogenesis and respiration
            through the thermogenic coactivator PGC-1
  JOURNAL   Cell 98 (1), 115-124 (1999)
   PUBMED   10412986
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Puigserver,P., Wu,Z., Park,C.W., Graves,R., Wright,M. and
            Spiegelman,B.M.
  TITLE     A cold-inducible coactivator of nuclear receptors linked to
            adaptive thermogenesis
  JOURNAL   Cell 92 (6), 829-839 (1998)
   PUBMED   9529258
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Spanos,N.P., Spillane,J. and McPeake,J.D.
  TITLE     Cognitive strategies and response to suggestion in hypnotic and
            task-motivated subjects
  JOURNAL   Am J Clin Hypn 18 (4), 254-262 (1976)
   PUBMED   1258810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC115110.3, AC092846.5 and
            AC092834.3.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that regulates the genes involved in energy metabolism.
            This protein interacts with PPARgamma, which permits the
            interaction of this protein with multiple transcription factors.
            This protein can interact with, and regulate the activities of,
            cAMP response element binding protein (CREB) and nuclear
            respiratory factors (NRFs). It provides a direct link between
            external physiological stimuli and the regulation of mitochondrial
            biogenesis, and is a major factor that regulates muscle fiber type
            determination. This protein may be also involved in controlling
            blood pressure, regulating cellular cholesterol homoeostasis, and
            the development of obesity. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6), as well as variant 4, encodes
            isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.46066.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..671
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-alpha isoform 4"
                     /note="ligand effect modulator-6; L-PGC-1alpha; PPAR gamma
                     coactivator variant form; PGC-1-alpha; PPARGC-1-alpha;
                     PPARAGCIalpha; PPARgamma coactivator 1alpha"
                     /calculated_mol_wt=77008
     Region          548..638
                     /region_name="RRM_PPARGC1A"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-alpha
                     (PGC-1alpha, or PPARGC-1-alpha) and similar proteins;
                     cd12623"
                     /db_xref="CDD:410034"
     CDS             1..671
                     /gene="PPARGC1A"
                     /gene_synonym="LEM6; PGC-1(alpha); PGC-1alpha; PGC-1v;
                     PGC1; PGC1A; PPARGC1"
                     /coded_by="NM_001354826.2:1028..3043"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS87211.1"
                     /db_xref="GeneID:10891"
                     /db_xref="HGNC:HGNC:9237"
                     /db_xref="MIM:604517"
ORIGIN      
        1 mpdgtpppqe aeepsllkkl llapantqls ynecsglstq nhanhnhrir tnpaivkten
       61 swsnkaksic qqqkpqrrpc sellkylttn ddpphtkpte nrnssrdkct skkkshtqsq
      121 sqhlqakptt lslpltpesp ndpkgspfen ktiertlsve lsgtagltpp ttpphkanqd
      181 npfraspklk sscktvvppp skkprysess gtqgnnstkk gpeqselyaq lskssvltgg
      241 heerktkrps lrlfgdhdyc qsinskteil inisqelqds rqlenkdvss dwqgqicsst
      301 dsdqcylret leaskqvspc strkqlqdqe iraelnkhfg hpsqavfdde adktgelrds
      361 dfsneqfskl pmfinsglam dglfddsede sdklsypwdg tqsyslfnvs pscssfnspc
      421 rdsvsppksl fsqrpqrmrs rsrsfsrhrs csrspysrsr srspgsrsss rscyyyessh
      481 yrhrthrnsp lyvrsrsrsp ysrrprydsy eeyqherlkr eeyrreyekr eserakqrer
      541 qrqkaieerr viyvgkirpd ttrtelrdrf evfgeieect vnlrddgdsy gfityrytcd
      601 afaalengyt lrrsnetdfe lyfcgrkqff ksnyadldsn sddfdpastk skydsldfds
      661 llkeaqrslr r
//
LOCUS       NP_478144                873 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 4 isoform
            1 [Homo sapiens].
ACCESSION   NP_478144
VERSION     NP_478144.1
DBSOURCE    REFSEQ: accession NM_058237.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 873)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 873)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 873)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 873)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   5  (residues 1 to 873)
  AUTHORS   Chen,G.I., Tisayakorn,S., Jorgensen,C., D'Ambrosio,L.M.,
            Goudreault,M. and Gingras,A.C.
  TITLE     PP4R4/KIAA1622 forms a novel stable cytosolic complex with
            phosphoprotein phosphatase 4
  JOURNAL   J Biol Chem 283 (43), 29273-29284 (2008)
   PUBMED   18715871
  REMARK    GeneRIF: PP4R4 forms a novel cytosolic complex with PP4c,
            independent from the complexes containing PP4R1, PP4R2.PP4R3, and
            alpha4, and the regulatory subunits of PP4c have evolved different
            modes of interaction with the catalytic subunit
REFERENCE   6  (residues 1 to 873)
  AUTHORS   Namciu,S.J., Friedman,R.D., Marsden,M.D., Sarausad,L.M.,
            Jasoni,C.L. and Fournier,R.E.
  TITLE     Sequence organization and matrix attachment regions of the human
            serine protease inhibitor gene cluster at 14q32.1
  JOURNAL   Mamm Genome 15 (3), 162-178 (2004)
   PUBMED   15014966
REFERENCE   7  (residues 1 to 873)
  AUTHORS   Andrade,M.A., Petosa,C., O'Donoghue,S.I., Muller,C.W. and Bork,P.
  TITLE     Comparison of ARM and HEAT protein repeats
  JOURNAL   J Mol Biol 309 (1), 1-18 (2001)
   PUBMED   11491282
  REMARK    Review article
REFERENCE   8  (residues 1 to 873)
  AUTHORS   Groves,M.R., Hanlon,N., Turowski,P., Hemmings,B.A. and Barford,D.
  TITLE     The structure of the protein phosphatase 2A PR65/A subunit reveals
            the conformation of its 15 tandemly repeated HEAT motifs
  JOURNAL   Cell 96 (1), 99-110 (1999)
   PUBMED   9989501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB480905.1, BC068491.1 and
            AB046842.1.
            
            Summary: The protein encoded by this gene is a HEAT-like
            repeat-containing protein. The HEAT repeat is a tandemly repeated,
            37-47 amino acid long module occurring in a number of cytoplasmic
            proteins. Arrays of HEAT repeats form a rod-like helical structure
            and appear to function as protein-protein interaction surfaces. The
            repeat-containing region of this protein has some similarity to the
            constant regulatory domain of the protein phosphatase 2A PR65/A
            subunit. The encoded protein binds protein serine/threonine
            phosphatase 4c in the cytoplasm. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.137306.1,
                                           SRR1660803.23201.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304338.8/ ENSP00000305924.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..873
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12-q32.13"
     Protein         1..873
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 4 isoform 1"
                     /note="HEAT-like repeat-containing protein;
                     serine/threonine-protein phosphatase 4 regulatory subunit
                     4; cilia and flagella associated protein 14"
                     /calculated_mol_wt=99321
     Region          135..159
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(151..152,155,158..159,191..192,195,198..199,202,
                     230..231,234,237..238,241,269..270,273,276..277)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          173..202
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          205..243
                     /region_name="HEAT-like repeat region"
     Region          212..242
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          213..251
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Region          244..282
                     /region_name="HEAT-like repeat region"
     Region          251..277
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          252..290
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Region          392..427
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Region          396..422
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          433..460
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          713..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0Y0; propagated from
                     UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Site            797
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0Y0; propagated from
                     UniProtKB/Swiss-Prot (Q6NUP7.1)"
     Region          822..873
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NUP7.1)"
     CDS             1..873
                     /gene="PPP4R4"
                     /gene_synonym="CFAP14; KIAA1622; PP4R4"
                     /coded_by="NM_058237.2:145..2766"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9921.1"
                     /db_xref="GeneID:57718"
                     /db_xref="HGNC:HGNC:23788"
                     /db_xref="MIM:616790"
ORIGIN      
        1 mhppppaaam dfsqnslfgy medlqeltii erpvrrslkt peeierltvd edlsdierav
       61 yllsagqdvq gtsvianlpf lmrqnptetl rrvlpkvrea lhvagvemql taamsfltil
      121 qdesvsihay thsflqvill hlehrdtgvs nawletllsv ievlpketlr heilnplvsk
      181 aqlsqtvqsr lvsckilgkl tnkfdahtik reilplvksl cqdveyevrs cmcrqlenia
      241 qgigteltks vvlpeliels rdegssvrla afetlvnlld ifdtddrsqt ilplvksfce
      301 ksfkadesil islsfhlgkl chglygiftp dqhlrflefy kklctlglqq enghnenqip
      361 pqileqekky isvrkncayn fpamivfvdp knfhmelyst ffclchdpev pvrytiaicf
      421 yevskllnsg vylihkelit llqdeslevl dalidhlpei lelmstgges svqenklssl
      481 pdlipaltaa eqraaaslkw rthekllqky aclphvissd qiyyrflqrm ftimmtnnvl
      541 pvqkaasrtl ciflrynrkq eqrheviqkl ieqlgqgksy wnrlrfldtc efiieifsks
      601 ffckyfflpa ielthdpvan vrmklcyllp kvkstlkipa dkhllqqlem cvrkllcqek
      661 dkdvlaivkr tvleldrmem smdafqkkfy ekdlldqeke reelllleme qlekekqqnd
      721 grpmsdkmfe kkrrdtktpt qslpknipis vpgpssvtps tskeikkskl irsqsfnnqa
      781 fhakygnlek caskssttgy ttsvsglgkt svlsladdsf rtrnassvps sfspntplps
      841 tsrgtgnsvd pkssgskdtq prkatlksrk snp
//
LOCUS       NP_003712                260 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFXANK isoform a [Homo sapiens].
ACCESSION   NP_003712
VERSION     NP_003712.1
DBSOURCE    REFSEQ: accession NM_003721.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM682278.1, AF094760.1 and
            AW411190.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.928654.1, AF094760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303088.9/ ENSP00000305071.2
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..260
                     /product="DNA-binding protein RFXANK isoform a"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=27971
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          89..118
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          <94..249
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          94..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(123,125,129..130,133..135,137..138,142,145,154,156,
                     158,162..163,166..168,170..171,175,178,187,189,191,
                     195..196,199..201,203..204,208,211)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          156..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..185
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..218
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..217
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          222..251
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     CDS             1..260
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_003721.4:447..1229"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12395.1"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqagsslkhs ttltnrqrgn evsalpatld slsihqlaaq geldqlkehl rkgdnlvnkp
      121 dergftpliw asafgeietv rfllewgadp hilakeresa lslastggyt divglllerd
      181 vdiniydwng gtpllyavrg nhvkcveall argadlttea dsgytpmdla valgyrkvqq
      241 vienhilklf qsnlvpadpe
//
LOCUS       NP_443152                875 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 29 [Homo sapiens].
ACCESSION   NP_443152 XP_001717506 XP_001717585 XP_945468
VERSION     NP_443152.1
DBSOURCE    REFSEQ: accession NM_052920.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Yao,L., Hao,Q., Wang,M., Chen,Y., Cao,H., Zhang,Q., Yu,K.,
            Jiang,Y., Shao,Z., Zhou,X. and Xu,Y.
  TITLE     KLHL29-mediated DDX3X degradation promotes chemosensitivity by
            abrogating cell cycle checkpoint in triple-negative breast cancer
  JOURNAL   Oncogene 42 (47), 3514-3528 (2023)
   PUBMED   37845393
  REMARK    GeneRIF: KLHL29-mediated DDX3X degradation promotes
            chemosensitivity by abrogating cell cycle checkpoint in
            triple-negative breast cancer.
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Mychaleckyj,J.C., Havt,A., Nayak,U., Pinkerton,R., Farber,E.,
            Concannon,P., Lima,A.A. and Guerrant,R.L.
  TITLE     Genome-Wide Analysis in Brazilians Reveals Highly Differentiated
            Native American Genome Regions
  JOURNAL   Mol Biol Evol 34 (3), 559-574 (2017)
   PUBMED   28100790
  REMARK    GeneRIF: Brazilian Amerindian ancestry compared to Asian, European,
            and African Genomes.SNPs within or proximal to CIITA (rs6498115),
            SMC6 (rs1834619), and KLHL29 (rs2288697) were most differentiated
            in the Amerindian-specific branch. SNPs in ADAMTS9 (rs7631391),
            DOCK2 (rs77594147), SLC28A1 (rs28649017), ARHGAP5 (rs7151991), and
            CIITA (rs45601437) in the Asian comparison.
REFERENCE   6  (residues 1 to 875)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Murea,M., Lu,L., Ma,L., Hicks,P.J., Divers,J., McDonough,C.W.,
            Langefeld,C.D., Bowden,D.W. and Freedman,B.I.
  TITLE     Genome-wide association scan for survival on dialysis in
            African-Americans with type 2 diabetes
  JOURNAL   Am J Nephrol 33 (6), 502-509 (2011)
   PUBMED   21546767
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 875)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 875)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012506.9, AC011239.5, DR002067.1, BC013982.1, AB067508.1 and
            BE142100.1.
            
            On or before Aug 30, 2009 this sequence version replaced
            XP_945468.2, XP_001717506.2, XP_001717585.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2146236,
                              SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000486442.6/ ENSP00000420659.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.1"
     Protein         1..875
                     /product="kelch-like protein 29"
                     /note="kelch repeat and BTB (POZ) domain containing 9;
                     kelch repeat and BTB domain-containing protein 9;
                     kelch-like 29"
                     /calculated_mol_wt=94098
     Region          <50..290
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          115..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          248..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          312..438
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          333..860
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          432..533
                     /region_name="BACK_KLHL29_KBTBD9"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 29 (KLHL29); cd18468"
                     /db_xref="CDD:350543"
     Region          577..621
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          585..635
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          626..669
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          637..683
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          673..716
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          684..730
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          720..808
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          732..778
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          779..821
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     Region          811..857
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          822..870
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CT2.3)"
     CDS             1..875
                     /gene="KLHL29"
                     /gene_synonym="KBTBD9"
                     /coded_by="NM_052920.2:756..3383"
                     /db_xref="CCDS:CCDS54335.1"
                     /db_xref="GeneID:114818"
                     /db_xref="HGNC:HGNC:29404"
ORIGIN      
        1 msrhhsrfer dyrvgwdrre wsvngthgtt sicsvtsgag ggtasslsvr pgllplpvvp
       61 srlptpatap apcttgssea itslvassas avttkapgis kgdsqsqgla tsirwgqtpi
      121 nqstpwdtde ppskqmresd npgtgpwvtt vaagnqptli ahsygvaqpp tfspavnvqa
      181 pvigvtpslp phvgpqlplm pghyslpqpp sqplssvvvn mpaqalyasp qplavstlpg
      241 vgqvarpgpt avgnghmagp llpppppaqp satlpsgapa tngppttdsa hglqmlrtig
      301 vgkyeftdpg hpremlkeln qqrrakaftd lkivvegref evhqnvlasc slyfkdliqr
      361 svqdsgqggr eklelvlsnl qadvlellle fvytgslvid sanaktllea askfqfhtfc
      421 kvcvsflekq ltasnclgvl amaeamqcse lyhmakafal qifpevaaqe eilsiskddf
      481 iayvsndsln tkaeelvyet vikwikkdpa trtqyaaell avvrlpfihp syllnvvdne
      541 eliksseacr dlvneakryh mlpharqemq tprtrprlsa gvaevivlvg grqmvgmtqr
      601 slvavtcwnp qnnkwyplas lpfydreffs vvsagdniyl sggmesgvtl advwcymsll
      661 dnwnlvsrmt vprcrhnslv ydgkiytlgg lgvagnvdhv erydtitnqw eavaplpkav
      721 hsaaatvcgg kiyvfggvne agraagvlqs yvpqtntwsf iespmidnky apavtlngfv
      781 filggayara ttiydpekgn ikagpnmnhs rqfcsavvld gkiyatggiv ssegpalgnm
      841 eayepttntw tllphmpcpv frhgcvvikk yiqsg
//
LOCUS       NP_078976                396 aa            linear   PRI 20-NOV-2025
DEFINITION  smad nuclear-interacting protein 1 [Homo sapiens].
ACCESSION   NP_078976
VERSION     NP_078976.2
DBSOURCE    REFSEQ: accession NM_024700.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Chen,W., Xu,Z., Jiang,J., Chen,L., Chen,Y., Yu,T., Chen,H. and
            Shi,R.
  TITLE     LncRNA MSC-AS1 regulates SNIP1 SUMOylation-mediated EMT by binding
            to SENP1 to promote intestinal fibrosis in Crohn's disease
  JOURNAL   Int J Biol Macromol 262 (Pt 1), 129921 (2024)
   PUBMED   38309408
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Chen,Y., Guo,W., Lu,W., Guo,X., Gao,W. and Yin,Z.
  TITLE     SNIP1 reduces extracellular matrix degradation and inflammation via
            inhibiting the NF-kappaB signaling pathway in osteoarthritis
  JOURNAL   Arch Biochem Biophys 747, 109764 (2023)
   PUBMED   37739115
  REMARK    GeneRIF: SNIP1 reduces extracellular matrix degradation and
            inflammation via inhibiting the NF-kappaB signaling pathway in
            osteoarthritis.
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Puffenberger,E.G., Jinks,R.N., Sougnez,C., Cibulskis,K.,
            Willert,R.A., Achilly,N.P., Cassidy,R.P., Fiorentini,C.J.,
            Heiken,K.F., Lawrence,J.J., Mahoney,M.H., Miller,C.J., Nair,D.T.,
            Politi,K.A., Worcester,K.N., Setton,R.A., Dipiazza,R.,
            Sherman,E.A., Eastman,J.T., Francklyn,C., Robey-Bond,S.,
            Rider,N.L., Gabriel,S., Morton,D.H. and Strauss,K.A.
  TITLE     Genetic mapping and exome sequencing identify variants associated
            with five novel diseases
  JOURNAL   PLoS One 7 (1), e28936 (2012)
   PUBMED   22279524
  REMARK    GeneRIF: Study identified sequence variants in the known
            disease-causing genes SLC6A3 and FLVCR1, and present evidence to
            strongly support the pathogenicity of variants identified in
            TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Cui,Q., Lim,S.K., Zhao,B. and Hoffmann,F.M.
  TITLE     Selective inhibition of TGF-beta responsive genes by
            Smad-interacting peptide aptamers from FoxH1, Lef1 and CBP
  JOURNAL   Oncogene 24 (24), 3864-3874 (2005)
   PUBMED   15750622
  REMARK    GeneRIF: Smad-binding peptide aptamers can be developed to
            selectively inhibit TGF-beta-induced gene expression.
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Roche,K.C., Wiechens,N., Owen-Hughes,T. and Perkins,N.D.
  TITLE     The FHA domain protein SNIP1 is a regulator of the cell cycle and
            cyclin D1 expression
  JOURNAL   Oncogene 23 (50), 8185-8195 (2004)
   PUBMED   15378006
  REMARK    GeneRIF: define both a new function for SNIP1 and identify a
            previously unrecognized regulator of the cell cycle and cyclin D1
            expression
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Lin,Y., Martin,J., Gruendler,C., Farley,J., Meng,X., Li,B.Y.,
            Lechleider,R., Huff,C., Kim,R.H., Grasser,W.A., Paralkar,V. and
            Wang,T.
  TITLE     A novel link between the proteasome pathway and the signal
            transduction pathway of the bone morphogenetic proteins (BMPs)
  JOURNAL   BMC Cell Biol 3, 15 (2002)
   PUBMED   12097147
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Kim,R.H., Flanders,K.C., Birkey Reffey,S., Anderson,L.A.,
            Duckett,C.S., Perkins,N.D. and Roberts,A.B.
  TITLE     SNIP1 inhibits NF-kappa B signaling by competing for its binding to
            the C/H1 domain of CBP/p300 transcriptional co-activators
  JOURNAL   J Biol Chem 276 (49), 46297-46304 (2001)
   PUBMED   11567019
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Kim,R.H., Wang,D., Tsang,M., Martin,J., Huff,C., de
            Caestecker,M.P., Parks,W.T., Meng,X., Lechleider,R.J., Wang,T. and
            Roberts,A.B.
  TITLE     A novel smad nuclear interacting protein, SNIP1, suppresses
            p300-dependent TGF-beta signal transduction
  JOURNAL   Genes Dev 14 (13), 1605-1616 (2000)
   PUBMED   10887155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP364813.1, BC027040.1 and
            AL034379.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 3, 2002 this sequence version replaced NP_078976.1.
            
            Summary: This gene encodes a protein that contains a coiled-coil
            motif and C-terminal forkhead-associated (FHA) domain. The encoded
            protein functions as a transcriptional coactivator that increases
            c-Myc activity and inhibits transforming growth factor beta
            (TGF-beta) and nuclear factor kappa-B (NF-kB) signaling. The
            encoded protein also regulates the stability of cyclin D1 mRNA, and
            may play a role in cell proliferation and cancer progression.
            Mutations in this gene are a cause of psychomotor retardation,
            epilepsy, and craniofacial dysmorphism (PMRED). [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.269461.1,
                                           SRR1803613.235319.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296215.8/ ENSP00000296215.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..396
                     /product="smad nuclear-interacting protein 1"
                     /note="PML1 homolog; FHA domain-containing protein SNIP1"
                     /calculated_mol_wt=45647
     Region          1..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Region          24..>208
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5M9G6; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5M9G6; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Region          224..372
                     /region_name="FHA_SNIP1"
                     /note="forkhead associated (FHA) domain found in Smad
                     nuclear-interacting protein 1 (SNIP1) and similar
                     proteins; cd22718"
                     /db_xref="CDD:438770"
     Site            order(232,261..263,296)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438770"
     Site            order(284..286,300..301,303,333,335..336)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438770"
     Region          373..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAD8.1)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD8.1)"
     CDS             1..396
                     /gene="SNIP1"
                     /gene_synonym="NEDHCS; PML1; PMRED"
                     /coded_by="NM_024700.4:65..1255"
                     /db_xref="CCDS:CCDS419.1"
                     /db_xref="GeneID:79753"
                     /db_xref="HGNC:HGNC:30587"
                     /db_xref="MIM:608241"
ORIGIN      
        1 mkavkserer gsrrrhrdgd vvlpagvvvk qerlspevap pahrrpdhsg gspspptsep
       61 arsghrgnra rgvsrsppkk knkasgrrsk sprskrnrsp hhstvkvkqe redhprrgre
      121 drqhrepseq ehrrarnsdr drhrghshqr rtsnerpgsg qgqgrdrdtq nlqaqeeere
      181 fynarrrehr qrndvggggs esqelvprpg gnnkekevpa kekpsfelsg alledtntfr
      241 gvvikysepp earipkkrwr lypfkndevl pvmyihrqsa yllgrhrria dipidhpscs
      301 kqhavfqyrl veytradgtv grrvkpyiid lgsgngtfln nkriepqryy elkekdvlkf
      361 gfssreyvll hessdtseid rkddedeeee eevsds
//
LOCUS       NP_001138435             343 aa            linear   PRI 20-NOV-2025
DEFINITION  NF-kappa-B inhibitor-like protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001138435
VERSION     NP_001138435.1
DBSOURCE    REFSEQ: accession NM_001144963.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Strenn,N., Hovey,D., Jonsson,L., Anckarsater,H., Lundstrom,S.,
            Lichtenstein,P. and Ekman,A.
  TITLE     Associations between autistic-like traits and polymorphisms in
            NFKBIL1
  JOURNAL   Acta Neuropsychiatr 31 (4), 220-229 (2019)
   PUBMED   31162003
  REMARK    GeneRIF: Study found significant associations for two single
            nucleotide polymorphisms in NFKBIL1: rs2239707 showed a significant
            distribution of genotype frequencies in the case-control analysis
            both for all individuals combined and in boys only, and rs2230365
            was significantly associated with the ALTs-module language
            impairment in boys only.
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Gichohi-Wainaina,W.N., Melse-Boonstra,A., Swinkels,D.W.,
            Zimmermann,M.B., Feskens,E.J. and Towers,G.W.
  TITLE     Common Variants and Haplotypes in the TF, TNF-alpha, and TMPRSS6
            Genes Are Associated with Iron Status in a Female Black South
            African Population
  JOURNAL   J Nutr 145 (5), 945-953 (2015)
   PUBMED   25809685
  REMARK    GeneRIF: genetic association studies in a population of black women
            in South Africa: Data suggest that an SNP in NFKBIL1 (rs2071592) is
            associated with iron status/iron-deficiency anemia in the
            population studied.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   de la Concha,E.G., Fernandez-Arquero,M., Lopez-Nava,G., Martin,E.,
            Allcock,R.J., Conejero,L., Paredes,J.G. and Diaz-Rubio,M.
  TITLE     Susceptibility to severe ulcerative colitis is associated with
            polymorphism in the central MHC gene IKBL
  JOURNAL   Gastroenterology 119 (6), 1491-1495 (2000)
   PUBMED   11113070
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Neville,M.J. and Campbell,R.D.
  TITLE     A new member of the Ig superfamily and a V-ATPase G subunit are
            among the predicted products of novel genes close to the TNF locus
            in the human MHC
  JOURNAL   J Immunol 162 (8), 4745-4754 (1999)
   PUBMED   10202016
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Shiina,T., Tamiya,G., Oka,A., Yamagata,T., Yamagata,N., Kikkawa,E.,
            Goto,K., Mizuki,N., Watanabe,K., Fukuzumi,Y., Taguchi,S.,
            Sugawara,C., Ono,A., Chen,L., Yamazaki,M., Tashiro,H., Ando,A.,
            Ikemura,T., Kimura,M. and Inoko,H.
  TITLE     Nucleotide sequencing analysis of the 146-kilobase segment around
            the IkBL and MICA genes at the centromeric end of the HLA class I
            region
  JOURNAL   Genomics 47 (3), 372-382 (1998)
   PUBMED   9480751
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Albertella,M.R. and Campbell,R.D.
  TITLE     Characterization of a novel gene in the human major
            histocompatibility complex that encodes a potential new member of
            the I kappa B family of proteins
  JOURNAL   Hum Mol Genet 3 (5), 793-799 (1994)
   PUBMED   8081366
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Iris,F.J., Bougueleret,L., Prieur,S., Caterina,D., Primas,G.,
            Perrot,V., Jurka,J., Rodriguez-Tome,P., Claverie,J.M., Dausset,J.
            et al.
  TITLE     Dense Alu clustering and a potential new member of the NF kappa B
            family within a 90 kilobase HLA class III segment
  JOURNAL   Nat Genet 3 (2), 137-145 (1993)
   PUBMED   8499947
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC370256.1, BC143671.1,
            AF097422.1 and X77909.1.
            
            Summary: This gene encodes a divergent member of the I-kappa-B
            family of proteins. Its function has not been determined. The gene
            lies within the major histocompatibility complex (MHC) class I
            region on chromosome 6. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2009].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice junction at
            the 3' end of an exon compared to variant 1. The resulting isoform
            (4) is shorter at the N-terminus and lacks an alternate internal
            segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP195124.1, HY092806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..343
                     /product="NF-kappa-B inhibitor-like protein 1 isoform 4"
                     /note="I-kappa-B-like protein; NF-kappa-B inhibitor-like
                     protein 1; ikappaBL; inhibitor of kappa B-like protein;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells inhibitor-like 1"
                     /calculated_mol_wt=38860
     Region          <20..>115
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          41..72
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..>231
                     /region_name="DDRGK"
                     /note="DDRGK domain; pfam09756"
                     /db_xref="CDD:370664"
     CDS             1..343
                     /gene="NFKBIL1"
                     /gene_synonym="IKBL; NFKBIL"
                     /coded_by="NM_001144963.2:136..1167"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:4795"
                     /db_xref="HGNC:HGNC:7800"
                     /db_xref="MIM:601022"
ORIGIN      
        1 mastsrrqrr errfrrylsa grlvraqall qrhpgldvda gqppplhrac arhdapalcl
       61 llrlgadpah qdrhgdtalh aaarqgpday tdfflpllsr cpsamgiknk dgetpgqilg
      121 wgppwdsaee eeeddasker ewrqklqgda shetqepesf sawsdrlare haqkcqqqqr
      181 eaegsrrppr aegssqswrq qeeeqrlfre rarakeeelr esrarraqea lgdrepkptr
      241 agpreehprg agrgslwrfg dvpwpcpggg dpeamaaalv argppleeqg alrrylrvqq
      301 vrwhpdrflq rfrsqietwe lgrvmgavta lsqalnrhae alk
//
LOCUS       NP_001295374             168 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 50 isoform 2 [Homo sapiens].
ACCESSION   NP_001295374 XP_005247851
VERSION     NP_001295374.1
DBSOURCE    REFSEQ: accession NM_001308445.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Reddi,R., Saddanapu,V., Chinthapalli,D.K., Sankoju,P., Sripadi,P.
            and Addlagatta,A.
  TITLE     Human Naa50 Protein Displays Broad Substrate Specificity for
            Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL
            ANALYSIS USING TETRAPEPTIDE LIBRARY
  JOURNAL   J Biol Chem 291 (39), 20530-20538 (2016)
   PUBMED   27484799
  REMARK    GeneRIF: Because Naa10 is reported to acetylate all amino termini
            that are devoid of methionine and Naa50 acetylates all other
            peptides that are followed by methionine
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Starheim,K.K., Gromyko,D., Evjenth,R., Ryningen,A., Varhaug,J.E.,
            Lillehaug,J.R. and Arnesen,T.
  TITLE     Knockdown of human N alpha-terminal acetyltransferase complex C
            leads to p53-dependent apoptosis and aberrant human Arl8b
            localization
  JOURNAL   Mol Cell Biol 29 (13), 3569-3581 (2009)
   PUBMED   19398576
  REMARK    GeneRIF: Data show that with MAK3 knockdown, p53 is stabilized and
            phosphorylated and there is a significant transcriptional
            activation of proapoptotic genes downstream of p53, and that
            localization of Arl8b is altered, suggesting that Arl8b is a Mak3
            substrate.
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Hou,F., Chu,C.W., Kong,X., Yokomori,K. and Zou,H.
  TITLE     The acetyltransferase activity of San stabilizes the mitotic
            cohesin at the centromeres in a shugoshin-independent manner
  JOURNAL   J Cell Biol 177 (4), 587-597 (2007)
   PUBMED   17502424
  REMARK    GeneRIF: May be specifically required for the maintenance of
            centromeric cohesion in mitosis.
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Arnesen,T., Anderson,D., Torsvik,J., Halseth,H.B., Varhaug,J.E. and
            Lillehaug,J.R.
  TITLE     Cloning and characterization of hNAT5/hSAN: an evolutionarily
            conserved component of the NatA protein N-alpha-acetyltransferase
            complex
  JOURNAL   Gene 371 (2), 291-295 (2006)
   PUBMED   16507339
  REMARK    GeneRIF: The first description of the human homologue of Nat5p/San,
            hNAT5, the third component of the human NatA
            N-alpha-acetyltransferase complex
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC108693.5, AL601126.1 and BX102492.1.
            
            On May 5, 2015 this sequence version replaced XP_005247851.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. It
            encodes isoform 2 which is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.20858.1,
                                           SRR1803614.121389.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.31"
     Protein         1..168
                     /product="N-alpha-acetyltransferase 50 isoform 2"
                     /EC_number="2.3.1.258"
                     /note="N-acetyltransferase 5; N-acetyltransferase 13
                     (GCN5-related); N-acetyltransferase san homolog; natE
                     catalytic subunit; N-epsilon-acetyltransferase 50"
                     /calculated_mol_wt=19180
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; N6-acetyllysine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Region          56..154
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     CDS             1..168
                     /gene="NAA50"
                     /gene_synonym="hNaa50p; MAK3; NAT13; NAT13P; NAT5; NAT5P;
                     SAN"
                     /coded_by="NM_001308445.2:301..807"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77791.1"
                     /db_xref="GeneID:80218"
                     /db_xref="HGNC:HGNC:29533"
                     /db_xref="MIM:610834"
ORIGIN      
        1 mkgrielgdv tphnikqlkr lnqvifpvsy ndkfykdvle vgelaklayf ndiavgavcc
       61 rvdhsqnqkr lyimtlgcla pyrrlgigtk mlnhvlnice kdgtfdniyl hvqisnesai
      121 dfyrkfgfei ietkknyykr iepadahvlq knlkvpsgqn advqktdn
//
LOCUS       NP_004480                327 aa            linear   PRI 20-NOV-2025
DEFINITION  G protein pathway suppressor 2 [Homo sapiens].
ACCESSION   NP_004480 NP_116329
VERSION     NP_004480.1
DBSOURCE    REFSEQ: accession NM_004489.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Zhao,L., Gu,C., Zhang,Y., Yan,J., Qiu,L., Qin,X. and Wang,Y.
  TITLE     Regulation mechanism of GPS2 on PGC-1alpha/Drp1-mediated
            mitochondrial dynamics in inflammation of acute lung injury
  JOURNAL   Int Immunopharmacol 140, 112838 (2024)
   PUBMED   39116501
  REMARK    GeneRIF: Regulation mechanism of GPS2 on PGC-1alpha/Drp1-mediated
            mitochondrial dynamics in inflammation of acute lung injury.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Lu,Y., Ma,W.B., Ren,G.M., Li,Y.T., Wang,T., Zhan,Y.Q., Xiang,S.S.,
            Chen,H., Gao,H.Y., Zhao,K., Yu,M., Li,C.Y., Yang,X.M. and Yin,R.H.
  TITLE     GPS2 promotes erythroid differentiation in K562 erythroleukemia
            cells primarily via NCOR1
  JOURNAL   Int J Hematol 120 (2), 157-166 (2024)
   PUBMED   38814500
  REMARK    GeneRIF: GPS2 promotes erythroid differentiation in K562
            erythroleukemia cells primarily via NCOR1.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Si,Y., Zhang,H., Peng,P., Zhu,C., Shen,J., Xiong,Y., Liu,X.,
            Xiang,Y., Li,W., Ren,Y., Wan,F., Zhang,L. and Liu,Y.
  TITLE     G protein pathway suppressor 2 suppresses gastric cancer by
            destabilizing epidermal growth factor receptor
  JOURNAL   Cancer Sci 112 (12), 4867-4882 (2021)
   PUBMED   34609770
  REMARK    GeneRIF: G protein pathway suppressor 2 suppresses gastric cancer
            by destabilizing epidermal growth factor receptor.
            Erratum:[Cancer Sci. 2025 Jan;116(1):279. doi: 10.1111/cas.16391.
            PMID: 39500631]
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Degenhardt,Y.Y. and Silverstein,S.J.
  TITLE     Gps2, a protein partner for human papillomavirus E6 proteins
  JOURNAL   J Virol 75 (1), 151-160 (2001)
   PUBMED   11119584
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Peng,Y.C., Breiding,D.E., Sverdrup,F., Richard,J. and Androphy,E.J.
  TITLE     AMF-1/Gps2 binds p300 and enhances its interaction with
            papillomavirus E2 proteins
  JOURNAL   J Virol 74 (13), 5872-5879 (2000)
   PUBMED   10846067
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Breiding,D.E., Sverdrup,F., Grossel,M.J., Moscufo,N., Boonchai,W.
            and Androphy,E.J.
  TITLE     Functional interaction of a novel cellular protein with the
            papillomavirus E2 transactivation domain
  JOURNAL   Mol Cell Biol 17 (12), 7208-7219 (1997)
   PUBMED   9372953
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Jin,D.Y., Teramoto,H., Giam,C.Z., Chun,R.F., Gutkind,J.S. and
            Jeang,K.T.
  TITLE     A human suppressor of c-Jun N-terminal kinase 1 activation by tumor
            necrosis factor alpha
  JOURNAL   J Biol Chem 272 (41), 25816-25823 (1997)
   PUBMED   9325311
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Spain,B.H., Bowdish,K.S., Pacal,A.R., Staub,S.F., Koo,D.,
            Chang,C.Y., Xie,W. and Colicelli,J.
  TITLE     Two human cDNAs, including a homolog of Arabidopsis FUS6 (COP11),
            suppress G-protein- and mitogen-activated protein kinase-mediated
            signal transduction in yeast and mammalian cells
  JOURNAL   Mol Cell Biol 16 (12), 6698-6706 (1996)
   PUBMED   8943324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026954.14 and BC013652.1.
            
            On Oct 6, 2004 this sequence version replaced NP_116329.1.
            
            Summary: This gene encodes a protein involved in G
            protein-mitogen-activated protein kinase (MAPK) signaling cascades.
            When overexpressed in mammalian cells, this gene could potently
            suppress a RAS- and MAPK-mediated signal and interfere with JNK
            activity, suggesting that the function of this gene may be signal
            repression. The encoded protein is an integral subunit of the
            NCOR1-HDAC3 (nuclear receptor corepressor 1-histone deacetylase 3)
            complex, and it was shown that the complex inhibits JNK activation
            through this subunit and thus could potentially provide an
            alternative mechanism for hormone-mediated antagonism of AP1
            (activator protein 1) function. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.68963.1,
                                           SRR1803612.98914.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380728.7/ ENSP00000370104.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..327
                     /product="G protein pathway suppressor 2"
                     /note="GPS-2"
                     /calculated_mol_wt=36558
     Region          5..292
                     /region_name="G_path_suppress"
                     /note="G-protein pathway suppressor; pfam15991"
                     /db_xref="CDD:464961"
     Region          26..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          61..94
                     /region_name="interaction with SUMO.
                     /evidence=ECO:0000269|PubMed:20159957"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          177..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Region          253..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     Site            312
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13227.3)"
     Site            323
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:19917673,
                     ECO:0007744|PubMed:24129315; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0000269|PubMed:19917673;
                     propagated from UniProtKB/Swiss-Prot (Q13227.3)"
     CDS             1..327
                     /gene="GPS2"
                     /gene_synonym="AMF-1"
                     /coded_by="NM_004489.5:98..1081"
                     /db_xref="CCDS:CCDS11100.1"
                     /db_xref="GeneID:2874"
                     /db_xref="HGNC:HGNC:4550"
                     /db_xref="MIM:601935"
ORIGIN      
        1 mpallerpkl snamaralhr himmererkr qeeeevdkmm eqkmkeeqer rkkkemeerm
       61 sleetkeqil kleekllalq eekhqlflql kkvlheeekr rrkeqsdltt ltsaayqqsl
      121 tvhtgthlls mqgspgghnr pgtlmaadra kqmfgpqvlt trhyvgsaaa fagtpehgqf
      181 qgspggaygt aqppphygpt qpayspsqql rapsafpavq ylsqpqpqpy avhghfqptq
      241 tgflqpggal slqkqmehan qqtgfsdsss lrpmhpqalh papgllaspq lpvqmqpagk
      301 sgfaatsqpg prlpfiqhsq nprfyhk
//
LOCUS       NP_001313509             239 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-7 isoform b [Homo sapiens].
ACCESSION   NP_001313509
VERSION     NP_001313509.1
DBSOURCE    REFSEQ: accession NM_001326580.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Wu,J., Zhang,H., Yang,L., Chen,Y., Li,J., Yang,M., Zhang,X., He,C.,
            Wang,X. and Xu,X.
  TITLE     Syntaxin 7 modulates seizure activity in epilepsy
  JOURNAL   Neurobiol Dis 181, 106118 (2023)
   PUBMED   37031804
  REMARK    GeneRIF: Syntaxin 7 modulates seizure activity in epilepsy.
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Parveen,S., Khamari,A., Raju,J., Coppolino,M.G. and Datta,S.
  TITLE     Syntaxin 7 contributes to breast cancer cell invasion by promoting
            invadopodia formation
  JOURNAL   J Cell Sci 135 (12) (2022)
   PUBMED   35762511
  REMARK    GeneRIF: Syntaxin 7 contributes to breast cancer cell invasion by
            promoting invadopodia formation.
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Miao,G., Zhao,H., Li,Y., Ji,M., Chen,Y., Shi,Y., Bi,Y., Wang,P. and
            Zhang,H.
  TITLE     ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
            assembly of the SNARE complex required for autolysosome formation
  JOURNAL   Dev Cell 56 (4), 427-442 (2021)
   PUBMED   33422265
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Nakamura,N., Yamamoto,A., Wada,Y. and Futai,M.
  TITLE     Syntaxin 7 mediates endocytic trafficking to late endosomes
  JOURNAL   J Biol Chem 275 (9), 6523-6529 (2000)
   PUBMED   10692457
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Prekeris,R., Yang,B., Oorschot,V., Klumperman,J. and Scheller,R.H.
  TITLE     Differential roles of syntaxin 7 and syntaxin 8 in endosomal
            trafficking
  JOURNAL   Mol Biol Cell 10 (11), 3891-3908 (1999)
   PUBMED   10564279
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Wong,S.H., Xu,Y., Zhang,T. and Hong,W.
  TITLE     Syntaxin 7, a novel syntaxin member associated with the early
            endosomal compartment
  JOURNAL   J Biol Chem 273 (1), 375-380 (1998)
   PUBMED   9417091
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Wang,H., Frelin,L. and Pevsner,J.
  TITLE     Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle
            trafficking to lysosomes
  JOURNAL   Gene 199 (1-2), 39-48 (1997)
   PUBMED   9358037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL589691.4 and AL357034.18.
            
            Summary: The protein encoded by this gene is a syntaxin family
            membrane receptor involved in vesicle transport. The encoded
            protein binds alpha-SNAP, an important regulator of transport
            vesicle fusion. Along with syntaxin 13, this protein plays a role
            in the ordered fusion of endosomes and lysosomes with the
            phagosome. [provided by RefSeq, May 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, 3' UTR,
            and 3' coding sequence compared to variant 1. The resulting isoform
            (b) has a shorter and distinct C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.672504.1,
                                           SRR1163657.354526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.2"
     Protein         1..239
                     /product="syntaxin-7 isoform b"
                     /calculated_mol_wt=27269
     Region          18..119
                     /region_name="Syntaxin_2"
                     /note="Syntaxin-like protein; pfam14523"
                     /db_xref="CDD:464199"
     Region          168..227
                     /region_name="SNARE_syntaxin7"
                     /note="SNARE motif of syntaxin 7; cd15875"
                     /db_xref="CDD:277228"
     Site            order(171..172,174..176,178..179,181..183,185..186,
                     188..193,195..197,199..200,202..204,206..207,209..214,
                     216..221,223..225)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277228"
     Site            199
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277228"
     CDS             1..239
                     /gene="STX7"
                     /coded_by="NM_001326580.2:169..888"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87441.1"
                     /db_xref="GeneID:8417"
                     /db_xref="HGNC:HGNC:11442"
                     /db_xref="MIM:603217"
ORIGIN      
        1 msytpgvggd paqlaqriss niqkitqcsv eiqrtlnqlg tpqdspelrq qlqqkqqytn
       61 qlaketdkyi kefgslpttp seqrqrkiqk drlvaeftts ltnfqkvqrq aaerekefva
      121 rvrassrvsg sfpedssker nlvswesqtq pqvqvqdeei teddlrlihe ressirqlea
      181 dimdineifk dlgmmiheqg dvidsieanv enaevhvqqa nqqlsraady qkkdscmlm
//
LOCUS       NP_001295753             154 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3B subunit 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001295753
VERSION     NP_001295753.1
DBSOURCE    REFSEQ: accession NM_001308824.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Hagerstrand,D., Oder,B., Cortese,D., Qu,Y., Binzer-Panchal,A.,
            Osterholm,C., Del Peso Santos,T., Rabbani,L., Asl,H.F.,
            Skaftason,A., Ljungstrom,V., Lundholm,A., Koutroumani,M.,
            Haider,Z., Jylha,C., Mollstedt,J., Mansouri,L., Plevova,K.,
            Agathangelidis,A., Scarfo,L., Armand,M., Muggen,A.F., Kay,N.E.,
            Shanafelt,T., Rossi,D., Orre,L.M., Pospisilova,S., Barylyuk,K.,
            Davi,F., Vesterlund,M., Langerak,A.W., Lehtio,J., Ghia,P.,
            Stamatopoulos,K., Sutton,L.A. and Rosenquist,R.
  TITLE     The non-canonical BAF chromatin remodeling complex is a novel
            target of spliceosome dysregulation in SF3B1-mutated chronic
            lymphocytic leukemia
  JOURNAL   Leukemia 38 (11), 2429-2442 (2024)
   PUBMED   39261602
  REMARK    GeneRIF: The non-canonical BAF chromatin remodeling complex is a
            novel target of spliceosome dysregulation in SF3B1-mutated chronic
            lymphocytic leukemia.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Guo,Y., Wang,X., Du,Y., Zhao,Y., Gao,L., Hao,Y., Lv,D., Feng,X.,
            Zhai,Y., Zou,B., Han,J., Xu,E., Yang,Y., Yang,B., Xi,Y. and
            Zhang,L.
  TITLE     The splicing factor SF3B1 confers ferroptosis resistance and
            promotes lung adenocarcinoma progression via upregulation of
            SLC7A11
  JOURNAL   Cancer Gene Ther 31 (10), 1498-1510 (2024)
   PUBMED   39127833
  REMARK    GeneRIF: The splicing factor SF3B1 confers ferroptosis resistance
            and promotes lung adenocarcinoma progression via upregulation of
            SLC7A11.
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Will,C.L., Schneider,C., MacMillan,A.M., Katopodis,N.F.,
            Neubauer,G., Wilm,M., Luhrmann,R. and Query,C.C.
  TITLE     A novel U2 and U11/U12 snRNP protein that associates with the
            pre-mRNA branch site
  JOURNAL   EMBO J 20 (16), 4536-4546 (2001)
   PUBMED   11500380
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Isono,K., Abe,K., Tomaru,Y., Okazaki,Y., Hayashizaki,Y. and
            Koseki,H.
  TITLE     Molecular cloning, genetic mapping, and expression of the mouse
            Sf3b1 (SAP155) gene for the U2 snRNP component of spliceosome
  JOURNAL   Mamm Genome 12 (3), 192-198 (2001)
   PUBMED   11252167
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Das,R., Zhou,Z. and Reed,R.
  TITLE     Functional association of U2 snRNP with the ATP-independent
            spliceosomal complex E
  JOURNAL   Mol Cell 5 (5), 779-787 (2000)
   PUBMED   10882114
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Pauling,M.H., McPheeters,D.S. and Ares,M. Jr.
  TITLE     Functional Cus1p is found with Hsh155p in a multiprotein splicing
            factor associated with U2 snRNA
  JOURNAL   Mol Cell Biol 20 (6), 2176-2185 (2000)
   PUBMED   10688664
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Wang,C., Chua,K., Seghezzi,W., Lees,E., Gozani,O. and Reed,R.
  TITLE     Phosphorylation of spliceosomal protein SAP 155 coupled with
            splicing catalysis
  JOURNAL   Genes Dev 12 (10), 1409-1414 (1998)
   PUBMED   9585501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY054349.1, AK294851.1 and
            BC046140.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes subunit 1 of the splicing factor 3b
            protein complex. Splicing factor 3b, together with splicing factor
            3a and a 12S RNA unit, forms the U2 small nuclear
            ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a
            complex binds pre-mRNA upstream of the intron's branch site in a
            sequence independent manner and may anchor the U2 snRNP to the
            pre-mRNA. Splicing factor 3b is also a component of the minor
            U12-type spliceosome. The carboxy-terminal two-thirds of subunit 1
            have 22 non-identical, tandem HEAT repeats that form rod-like,
            helical structures. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks several exons and its 3'
            terminal exon extends past a splice site that is used in variant 1.
            This results in a novel 3' coding region and 3' UTR, compared to
            variant 1. It encodes isoform 3 which is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046140.1, SRR1803616.169864.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..154
                     /product="splicing factor 3B subunit 1 isoform 3"
                     /note="pre-mRNA splicing factor SF3b, 155 kDa subunit;
                     pre-mRNA processing 10; spliceosome-associated protein
                     155; splicing factor 3b, subunit 1, 155kDa"
                     /calculated_mol_wt=17278
     CDS             1..154
                     /gene="SF3B1"
                     /gene_synonym="Hsh155; MDS; PRP10; PRPF10; SAP155;
                     SF3b155"
                     /coded_by="NM_001308824.1:95..559"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82550.1"
                     /db_xref="GeneID:23451"
                     /db_xref="HGNC:HGNC:10768"
                     /db_xref="MIM:605590"
ORIGIN      
        1 makiakthed ieaqireiqg kkaaldeaqg vgldstgyyd qeiyggsdsr fagyvtsiaa
       61 teledddddy ssstsllgqk kpgyhapval lndipqsteq ydpfaehrpp kiadredeyk
      121 khrrtmiisp erldpfadgn sfplfykyse iyly
//
LOCUS       NP_005783                160 aa            linear   PRI 20-NOV-2025
DEFINITION  M-phase phosphoprotein 6 [Homo sapiens].
ACCESSION   NP_005783
VERSION     NP_005783.2
DBSOURCE    REFSEQ: accession NM_005792.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Yoshikatsu,Y., Ishida,Y., Sudo,H., Yuasa,K., Tsuji,A. and
            Nagahama,M.
  TITLE     NVL2, a nucleolar AAA-ATPase, is associated with the nuclear
            exosome and is involved in pre-rRNA processing
  JOURNAL   Biochem Biophys Res Commun 464 (3), 780-786 (2015)
   PUBMED   26166824
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Schilders,G., Raijmakers,R., Raats,J.M. and Pruijn,G.J.
  TITLE     MPP6 is an exosome-associated RNA-binding protein involved in 5.8S
            rRNA maturation
  JOURNAL   Nucleic Acids Res 33 (21), 6795-6804 (2005)
   PUBMED   16396833
  REMARK    GeneRIF: MPP6 is a nucleolus-specific exosome co-factor required
            for its role in the maturation of 5.8S rRNA.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
  REMARK    GeneRIF: MPP6 was found to be associated with the exosome, a
            multiprotein complex involved in RNA degradation.
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AW175781.1, BU595100.1, BU622913.1 and AI831131.1.
            
            On Nov 30, 2006 this sequence version replaced NP_005783.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222667.1, SRR1163657.208941.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258169.9/ ENSP00000258169.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.3"
     Protein         1..160
                     /product="M-phase phosphoprotein 6"
                     /calculated_mol_wt=18893
     Region          8..135
                     /region_name="MPP6"
                     /note="M-phase phosphoprotein 6; pfam10175"
                     /db_xref="CDD:462978"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99547.2)"
     Region          116..133
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99547.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99547.2)"
     CDS             1..160
                     /gene="MPHOSPH6"
                     /gene_synonym="MPP; MPP-6; MPP6"
                     /coded_by="NM_005792.2:50..532"
                     /db_xref="CCDS:CCDS10937.1"
                     /db_xref="GeneID:10200"
                     /db_xref="HGNC:HGNC:7214"
                     /db_xref="MIM:605500"
ORIGIN      
        1 maaerktrls knllrmkfmq rgldsetkkq leeeekkiis eehwyldlpe lkekesfiie
       61 eqsfllcedl lygrmsfrgf npeveklmlq mnakhkaeev edetveldvs deemarryet
      121 lvgtigkkfa rkrdhanyee dengditpik akkmflkpqd
//
LOCUS       NP_005076               2090 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear pore complex protein Nup214 isoform 2 [Homo sapiens].
ACCESSION   NP_005076 NP_705906
VERSION     NP_005076.3
DBSOURCE    REFSEQ: accession NM_005085.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2090)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2090)
  AUTHORS   Choi,Y.J., Min,Y.K., Lee,S.T., Choi,J.R. and Shin,S.
  TITLE     NUP214 Rearrangements in Leukemia Patients: A Case Series From a
            Single Institution
  JOURNAL   Ann Lab Med 44 (4), 335-342 (2024)
   PUBMED   38145892
  REMARK    GeneRIF: NUP214 Rearrangements in Leukemia Patients: A Case Series
            From a Single Institution.
REFERENCE   3  (residues 1 to 2090)
  AUTHORS   Wang,J., Zhan,Q.R., Lu,X.X., Zhang,L.J., Wang,X.X. and Zhang,H.Y.
  TITLE     The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review
  JOURNAL   Medicine (Baltimore) 101 (30), e29294 (2022)
   PUBMED   35905214
  REMARK    GeneRIF: The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2090)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 2090)
  AUTHORS   Zheng,Y.Z., Wen,J.J., Wang,L.Y., Zheng,H., Hua,X.L., Li,J. and
            Hu,J.D.
  TITLE     [SET-NUP214-positive pediatric acute myeloid leukemia: a report of
            two cases]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 42 (9), 769 (2021)
   PUBMED   34753234
  REMARK    GeneRIF: [SET-NUP214-positive pediatric acute myeloid leukemia: a
            report of two cases].
REFERENCE   6  (residues 1 to 2090)
  AUTHORS   Napetschnig,J., Blobel,G. and Hoelz,A.
  TITLE     Crystal structure of the N-terminal domain of the human
            protooncogene Nup214/CAN
  JOURNAL   Proc Natl Acad Sci U S A 104 (6), 1783-1788 (2007)
   PUBMED   17264208
  REMARK    GeneRIF: A mechanism is proposed by which the C-terminal peptide
            extension is involved in nuclear pore complex assembly.
REFERENCE   7  (residues 1 to 2090)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   8  (residues 1 to 2090)
  AUTHORS   Kraemer,D., Wozniak,R.W., Blobel,G. and Radu,A.
  TITLE     The human CAN protein, a putative oncogene product associated with
            myeloid leukemogenesis, is a nuclear pore complex protein that
            faces the cytoplasm
  JOURNAL   Proc Natl Acad Sci U S A 91 (4), 1519-1523 (1994)
   PUBMED   8108440
REFERENCE   9  (residues 1 to 2090)
  AUTHORS   von Lindern,M., Fornerod,M., van Baal,S., Jaegle,M., de Wit,T.,
            Buijs,A. and Grosveld,G.
  TITLE     The translocation (6;9), associated with a specific subtype of
            acute myeloid leukemia, results in the fusion of two genes, dek and
            can, and the expression of a chimeric, leukemia-specific dek-can
            mRNA
  JOURNAL   Mol Cell Biol 12 (4), 1687-1697 (1992)
   PUBMED   1549122
REFERENCE   10 (residues 1 to 2090)
  AUTHORS   von Lindern,M., Poustka,A., Lerach,H. and Grosveld,G.
  TITLE     The (6;9) chromosome translocation, associated with a specific
            subtype of acute nonlymphocytic leukemia, leads to aberrant
            transcription of a target gene on 9q34
  JOURNAL   Mol Cell Biol 10 (8), 4016-4026 (1990)
   PUBMED   2370860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB062584.1, AB159230.1,
            BC045620.1 and BC105998.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 20, 2003 this sequence version replaced
            NP_705906.1, NP_005076.2.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. This gene is a member of the
            FG-repeat-containing nucleoporins. The protein encoded by this gene
            is localized to the cytoplasmic face of the nuclear pore complex
            where it is required for proper cell cycle progression and
            nucleocytoplasmic transport. The 3' portion of this gene forms a
            fusion gene with the DEK gene on chromosome 6 in a t(6,9)
            translocation associated with acute myeloid leukemia and
            myelodysplastic syndrome. Alternative splicing of this gene results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) represents the longest
            transcript and encodes the longest isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X64228.1, SRR1803612.247797.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359428.10/ ENSP00000352400.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2090
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..2090
                     /product="nuclear pore complex protein Nup214 isoform 2"
                     /note="CAN protein, putative oncogene; nuclear pore
                     complex protein Nup214; nucleoporin 214kDa"
                     /calculated_mol_wt=213489
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          39..91
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          41..404
                     /region_name="Seven-bladed beta propeller"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          <94..265
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          96..144
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          152..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          155..>216
                     /region_name="ANAPC4_WD40"
                     /note="Anaphase-promoting complex subunit 4 WD40 domain;
                     pfam12894"
                     /db_xref="CDD:403945"
     Region          196..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          236..1418
                     /region_name="44 X 2 AA repeats of F-G.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          243..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          304..350
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          362..401
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          422..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            444..445
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          450..586
                     /region_name="(Microbial infection) Binds human adenovirus
                     5 (HAdV-5) protein L3 (hexon).
                     /evidence=ECO:0000269|PubMed:25410864"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          481..2076
                     /region_name="11 X 5 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          489..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          <512..>689
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          597..700
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            678
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          740..768
                     /region_name="Leucine-zipper 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            812..813
                     /site_type="other"
                     /note="Breakpoint; propagated from UniProtKB/Swiss-Prot
                     (P35658.2)"
     Region          861..882
                     /region_name="Leucine-zipper 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          987..1009
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1023
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          <1033..1712
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1045
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1081
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1128..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1168..1213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1234..1316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1312
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1337..1408
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Site            1353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1409..2084
                     /region_name="18 X 4 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1427..2085
                     /region_name="11 X 3 AA approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1438..1467
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1479..1539
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1596..>2080
                     /region_name="COG4625"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal beta-barrel porin domain [Function unknown]"
                     /db_xref="CDD:443664"
     Site            1840..1841
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          1884..1903
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     Region          1916..1977
                     /region_name="Nup214_FG"
                     /note="Nucleoporin Nup214 phenylalanine-glycine (FG)
                     domain; pfam18617"
                     /db_xref="CDD:408399"
     Site            1916..1917
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1963
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1967..1968
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; Breakpoint for
                     translocation to form the NUP214-SQSTM1 fusion protein.
                     /evidence=ECO:0000269|PubMed:20851865; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            1985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Site            2071..2072
                     /site_type="other"
                     /note="Breakpoint for translocation to form the
                     NUP214-ABL1 fusion protein.
                     /evidence=ECO:0000269|PubMed:15361874; propagated from
                     UniProtKB/Swiss-Prot (P35658.2)"
     Region          2085..2086
                     /region_name="44. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35658.2)"
     CDS             1..2090
                     /gene="NUP214"
                     /gene_synonym="CAIN; CAN; IIAE9"
                     /coded_by="NM_005085.4:120..6392"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6940.1"
                     /db_xref="GeneID:8021"
                     /db_xref="HGNC:HGNC:8064"
                     /db_xref="MIM:114350"
ORIGIN      
        1 mgdemdamip eremkdfqfr alkkvrifds peelpkerss llavsnkygl vfaggasglq
       61 ifptknlliq nkpgddpnki vdkvqgllvp mkfpihhlal scdnltlsac mmsseygsii
      121 affdvrtfsn eakqqkrpfa yhkllkdagg mvidmkwnpt vpsmvavcla dgsiavlqvt
      181 etvkvcatlp stvavtsvcw spkgkqlavg kqngtvvqyl ptlqekkvip cppfyesdhp
      241 vrvldvlwig tyvfaivyaa adgtletspd vvmallpkke ekhpeifvnf mepcygscte
      301 rqhhyylsyi eewdlvlaas aastevsila rqsdqinwes wlledssrae lpvtdksdds
      361 lpmgvvvdyt nqveitisde ktlppapvlm llstdgvlcp fyminqnpgv ksliktperl
      421 slegerqpks pgstpttpts sqapqkldas aaaapaslpp sspaapiatf sllpaggapt
      481 vfsfgssslk ssatvtgepp syssgsdssk aapgpgpstf sfvppskasl aptpaaspva
      541 psaasfsfgs sgfkptlest pvpsvsapni amkpsfppst savkvnlsek ftaaatstpv
      601 sssqsappms pfssaskpaa sgplshptpl sappssvplk ssvlpspsgr saqgssspvp
      661 smvqksprit ppaakpgspq akslqpavae kqghqwkdsd pvmagigeei ahfqkeleel
      721 kartskacfq vgtseemkml rtesddlhtf lleikettes lhgdisslkt tllegfagve
      781 eareqnernr dsgylhllyk rpldpkseaq lqeirrlhqy vkfavqdvnd vldlewdqhl
      841 eqkkkqrhll vperetlfnt lannreiinq qrkrlnhlvd slqqlrlykq tslwslssav
      901 psqssihsfd sdleslcnal lkttieshtk slpkvpakls pmkqaqlrnf lakrktppvr
      961 stapaslsrs aflsqryyed ldevsstssv sqslesedar tsckddeavv qaprhapvvr
     1021 tpsiqpsllp haapfakshl vhgsspgvmg tsvatsaski ipqgadstml atktvkhgap
     1081 spshpisapq aaaaaalrrq masqapavnt ltestlknvp qvvnvqelkn npatpstamg
     1141 ssvpystakt phpvltpvaa nqakqgslin slkpsgptpa sgqlssgdka sgtakietav
     1201 tstpsasgqf skpfsfspsg tgfnfgiitp tpssnftaaq gatpstkess qpdafssggg
     1261 skpsyeaipe ssppsgitsa snttpgepaa sssrpvapsg talsttsskl etppsklgel
     1321 lfpsslaget lgsfsglrvg qaddstkptn kasstsltst qptktsgvps gfnftappvl
     1381 gkhteppvts satttsvapp aatstsstav fgslpvtsag ssgvisfggt slsagktsfs
     1441 fgsqqtnstv ppsappptta atplptsfpt lsfgsllssa ttpslpmsag rsteeatssa
     1501 lpekpgdsev sasaasllee qqsaqlpqap pqtsdsvkke pvlaqpavsn sgtaasstsl
     1561 valsaeatpa ttgvpdarte avppassfsv pgqtavtaaa issagpvave tsstpiasst
     1621 tsivapgpsa eaaafgtvts gssvfaqppa assssafnql tnntatapsa tpvfgqvaas
     1681 tapslfgqqt gstastaaat pqvsssgfss pafgttapgv fgqttfgqas vfgqsassaa
     1741 svfsfsqpgf ssvpafgqpa sstptstsgs vfgaasstss sssfsfgqss pntggglfgq
     1801 snapafgqsp gfgqggsvfg gtsaatttaa tsgfsfcqas gfgssntgsv fgqaastggi
     1861 vfgqqsssss gsvfgsgntg rgggffsglg gkpsqdaank npfssasggf gstatsntsn
     1921 lfgnsgaktf ggfasssfge qkptgtfssg ggsvasqgfg fsspnktggf gaapvfgspp
     1981 tfggspgfgg vpafgsapaf tsplgstggk vfgegtaaas aggfgfgsss nttsfgtlas
     2041 qnaptfgsls qqtsgfgtqs sgfsgfgsgt ggfsfgsnns svqgfggwrs
//
LOCUS       NP_001240841            1159 aa            linear   PRI 20-NOV-2025
DEFINITION  TBC1 domain family member 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001240841
VERSION     NP_001240841.1
DBSOURCE    REFSEQ: accession NM_001253912.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Wang,Q., Rong,P., Zhang,W., Yang,X., Chen,L., Cao,Y., Liu,M.,
            Feng,W., Ouyang,Q., Chen,Q., Li,H., Liang,H., Meng,F., Wang,H.Y.
            and Chen,S.
  TITLE     TBC1D1 is an energy-responsive polarization regulator of
            macrophages via governing ROS production in obesity
  JOURNAL   Sci China Life Sci 67 (9), 1899-1914 (2024)
   PUBMED   38902450
  REMARK    GeneRIF: TBC1D1 is an energy-responsive polarization regulator of
            macrophages via governing ROS production in obesity.
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Song,D., Yang,Q., Li,L., Wei,Y., Zhang,C., Du,H., Ren,G. and Li,H.
  TITLE     Novel prognostic biomarker TBC1D1 is associated with immunotherapy
            resistance in gliomas
  JOURNAL   Front Immunol 15, 1372113 (2024)
   PUBMED   38529286
  REMARK    GeneRIF: Novel prognostic biomarker TBC1D1 is associated with
            immunotherapy resistance in gliomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1159)
  AUTHORS   Cai,J., Jiang,Y., Chen,P., Liang,J., Zhang,Y., Yuan,R., Fan,H.,
            Zhong,Y., Cai,J., Cheng,S. and Zhang,Y.
  TITLE     TBC1D1 represses glioma progression by altering the integrity of
            the cytoskeleton
  JOURNAL   Aging (Albany NY) 16 (1), 431-444 (2024)
   PUBMED   38189823
  REMARK    GeneRIF: TBC1D1 represses glioma progression by altering the
            integrity of the cytoskeleton.
REFERENCE   5  (residues 1 to 1159)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 1159)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   7  (residues 1 to 1159)
  AUTHORS   Roach,W.G., Chavez,J.A., Miinea,C.P. and Lienhard,G.E.
  TITLE     Substrate specificity and effect on GLUT4 translocation of the Rab
            GTPase-activating protein Tbc1d1
  JOURNAL   Biochem J 403 (2), 353-358 (2007)
   PUBMED   17274760
  REMARK    GeneRIF: form of Tbc1d1 also inhibited GLUT4 translocation and that
            this effect also required a functional GAP domain
REFERENCE   8  (residues 1 to 1159)
  AUTHORS   Stone,S., Abkevich,V., Russell,D.L., Riley,R., Timms,K., Tran,T.,
            Trem,D., Frank,D., Jammulapati,S., Neff,C.D., Iliev,D., Gress,R.,
            He,G., Frech,G.C., Adams,T.D., Skolnick,M.H., Lanchbury,J.S.,
            Gutin,A., Hunt,S.C. and Shattuck,D.
  TITLE     TBC1D1 is a candidate for a severe obesity gene and evidence for a
            gene/gene interaction in obesity predisposition
  JOURNAL   Hum Mol Genet 15 (18), 2709-2720 (2006)
   PUBMED   16893906
  REMARK    GeneRIF: coding variant R125W affects obesity susceptibility,
            delimits the location of an obesity gene at 4q34-35 and identifies
            a gene/gene interaction that influences the risk for obesity
            predisposition
REFERENCE   9  (residues 1 to 1159)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   10 (residues 1 to 1159)
  AUTHORS   White,R.A., Pasztor,L.M., Richardson,P.M. and Zon,L.I.
  TITLE     The gene encoding TBC1D1 with homology to the tre-2/USP6 oncogene,
            BUB2, and cdc16 maps to mouse chromosome 5 and human chromosome 4
  JOURNAL   Cytogenet Cell Genet 89 (3-4), 272-275 (2000)
   PUBMED   10965142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB036208.1, BC050321.1, AK295746.1, BQ672157.1, AW364769.1,
            CR996632.1 and AK074954.1.
            
            Summary: TBC1D1 is the founding member of a family of proteins
            sharing a 180- to 200-amino acid TBC domain presumed to have a role
            in regulating cell growth and differentiation. These proteins share
            significant homology with TRE2 (USP6; MIM 604334), yeast Bub2, and
            CDC16 (MIM 603461) (White et al., 2000 [PubMed 10965142]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) has multiple differences in
            the coding region, but maintains the reading frame, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295746.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400288, SAMN03465421
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1159
                     /product="TBC1 domain family member 1 isoform 2"
                     /note="TBC1 (tre-2/USP6, BUB2, cdc16) domain family,
                     member 1"
                     /calculated_mol_wt=131248
     Region          21..150
                     /region_name="PTB"
                     /note="Phosphotyrosine-binding (PTB) PH-like fold;
                     cd00934"
                     /db_xref="CDD:269911"
     Site            order(24,112,133)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269911"
     Site            order(93..96,105..106,119,144,148)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269911"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          164..371
                     /region_name="PTB_TBC1D1_like"
                     /note="TBC1 domain family member 1 and related proteins
                     Phosphotyrosine-binding (PTB) domain; cd01269"
                     /db_xref="CDD:269967"
     Site            order(176,330,353)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269967"
     Region          203..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:24879834; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            order(319..324,337,364,368)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269967"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          532..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          564..587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24879834; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000250|UniProtKB:Q60949; propagated from
                     UniProtKB/Swiss-Prot (Q86TI0.2)"
     Region          784..839
                     /region_name="DUF3350"
                     /note="Domain of unknown function (DUF3350); pfam11830"
                     /db_xref="CDD:463365"
     Region          891..>1028
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Region          1085..1147
                     /region_name="ZapB"
                     /note="Cell division protein ZapB, interacts with FtsZ
                     [Cell cycle control, cell division, chromosome
                     partitioning]; COG3074"
                     /db_xref="CDD:442308"
     CDS             1..1159
                     /gene="TBC1D1"
                     /gene_synonym="TBC; TBC1"
                     /coded_by="NM_001253912.2:359..3838"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58897.1"
                     /db_xref="GeneID:23216"
                     /db_xref="HGNC:HGNC:11578"
                     /db_xref="MIM:609850"
ORIGIN      
        1 mepitftark hllsnevsvd fglqlvgslp vhslttmpml pwvvaevrrl srqstrkepv
       61 tkqvrlcvsp sglrcepepg rsqqwdpliy ssifeckpqr vhklihnshd psyfaclike
      121 davhrqsicy vfkaddqtkv peiissirqa gkiarqeelh cpsefddtfs kkfevlfcgr
      181 vtvahkkapp alideciekf nhvsgsrgse sprpnpphaa ptgsqepvrr pmrksfsqpg
      241 lrslafrkel qdgglrssgf fssfeesdie nhlisghniv qptdieenrt mlftigqsev
      301 ylispdtkki aleknfkeis fcsqgirhvd hfgficress ggggfhfvcy vfqctnealv
      361 deimmtlkqa ftvaavqqta kapaqlcegc plqslhklce riegmnsskt klelqkhltt
      421 ltnqeqatif eevqklrprn eqreneliis flrclyeekq kehihigemk qtsqmaaeni
      481 gselppsatr frldmlknka krsltesles ilsrgnkarg lqehsisvdl dsslsstlsn
      541 tskepsvcek ealpisessf kllgssedls sdseshlpee paplspqqaf rrrantlshf
      601 piecqeppqp argspgvsqr klmryhsvst etphernvdp spvgeskhrp gqssapappp
      661 rlnpsasspn ffkylkhnss geqsgnavpk sisyrnalrk klhssssvpn flkflapvde
      721 nntsdfmntk rdfeskanhl gdsggtpvkt rrhswrqqif lrvatpqkac dsssryedys
      781 elgelpprsp lepvcedgpf gpppeekkrt srelrelwqk ailqqilllr mekenqklqa
      841 sendllnkrl kldyeeitpc lkevttvwek mlstpgrski kfdmekmhsa vgqgvprhhr
      901 geiwkflaeq fhlkhqfpsk qqpkdvpyke llkqltsqqh ailidlgrtf pthpyfsaql
      961 gagqlslyni lkayslldqe vgycqglsfv agilllhmse eeafkmlkfl mfdmglrkqy
     1021 rpdmiilqme ktinqvfemd iakqlqayev eyhvlqeeli dssplsdnqr mdklektnss
     1081 lrkqnldlle qlqvangriq sleatiekll ssesklkqam ltlelersal lqtveelrrr
     1141 saepsdrepe ctqpeptgd
//
LOCUS       NP_001336662             343 aa            linear   PRI 20-NOV-2025
DEFINITION  PWWP domain-containing protein 2A isoform e [Homo sapiens].
ACCESSION   NP_001336662
VERSION     NP_001336662.1
DBSOURCE    REFSEQ: accession NM_001349733.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Hong,H., Sun,Y., Deng,H., Yuan,K., Chen,J., Liu,W. and Cui,Z.
  TITLE     Dysregulation of cPWWP2A-miR-579 axis mediates
            dexamethasone-induced cytotoxicity in human osteoblasts
  JOURNAL   Biochem Biophys Res Commun 517 (3), 491-498 (2019)
   PUBMED   31376935
  REMARK    GeneRIF: It has been shown that dysregulation of the circular RNA
            PWWP2A-miR-579 axis is involved in dexamethasone-induced
            cytotoxicity in human osteoblasts.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Zhang,T., Wei,G., Millard,C.J., Fischer,R., Konietzny,R.,
            Kessler,B.M., Schwabe,J.W.R. and Brockdorff,N.
  TITLE     A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to
            regulate transcription at active genes
  JOURNAL   Nat Commun 9 (1), 3798 (2018)
   PUBMED   30228260
  REMARK    GeneRIF: Study in HeLa, HEK293F, and mouse embryonic stem cells
            reveal that loss of PWWP2A/B leads to increases in histone
            acetylation predominantly at highly expressed genes, accompanied by
            decreases in Pol II elongation. Collectively, these findings
            suggest a role for PWWP2A/B in regulating transcription through the
            fine-tuning of histone acetylation dynamics at actively transcribed
            genes.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Punzeler,S., Link,S., Wagner,G., Keilhauer,E.C., Kronbeck,N.,
            Spitzer,R.M., Leidescher,S., Markaki,Y., Mentele,E., Regnard,C.,
            Schneider,K., Takahashi,D., Kusakabe,M., Vardabasso,C., Zink,L.M.,
            Straub,T., Bernstein,E., Harata,M., Leonhardt,H., Mann,M.,
            Rupp,R.A. and Hake,S.B.
  TITLE     Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural
            crest differentiation
  JOURNAL   EMBO J 36 (15), 2263-2279 (2017)
   PUBMED   28645917
  REMARK    GeneRIF: Thus, PWWP2A is a novel H2A.Z-specific multivalent
            chromatin binder providing a surprising link between H2A.Z,
            chromosome segregation, and organ development.
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008706.5, DB450981.1, BC105110.1, AI288438.1, BC035076.2,
            BC039106.1, AV720552.1 and CB218424.1.
            
            Transcript Variant: This variant (5) contains an alternate exon in
            the 5' region, resulting in use of a downstream start codon
            compared to variant 1. The encoded isoform (e) has a shorter
            N-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.151201.1,
                                           SRR1660805.181409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162823 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..343
                     /product="PWWP domain-containing protein 2A isoform e"
                     /note="PWWP domain-containing protein 2A; MSTP101"
                     /calculated_mol_wt=38455
     CDS             1..343
                     /gene="PWWP2A"
                     /gene_synonym="MST101"
                     /coded_by="NM_001349733.2:784..1815"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:114825"
                     /db_xref="HGNC:HGNC:29406"
                     /db_xref="MIM:617823"
ORIGIN      
        1 mplqsntfqe gtevkceang avpddpspvp hpelslaesl wtskppplfh egapyppplf
       61 irdtynqsip qppprkikrp krkmyreept simnaiklrp rqvlcdkckn svvaekkeir
      121 kgssatdssk yedkkrrnes vttvnkklkt dhkvdgknqn esqkrnavvk vsniahsrgr
      181 vvkvsaqant skaqlstkkv lqsknmdhak arevlkiake kaqkkqnets tsknahskvh
      241 ftrryqnpss gslpprvrlk pqryrneend sslktglekm rsgkmapkpq srctstrsag
      301 lnkwqllhqt vtspaaplqc ltdhcgfrlg alkltvkraa qrh
//
LOCUS       NP_001108072             152 aa            linear   PRI 20-NOV-2025
DEFINITION  SUZ RNA-binding domain-containing isoform 1 [Homo sapiens].
ACCESSION   NP_001108072
VERSION     NP_001108072.1
DBSOURCE    REFSEQ: accession NM_001114600.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Deng,L., Gong,K. and Wang,G.
  TITLE     Hsa_circ_0008344 Promotes Glioma Tumor Progression and Angiogenesis
            Presumably by Regulating miR-638/SZRD1 Pathway
  JOURNAL   Neurotox Res 40 (3), 825-836 (2022)
   PUBMED   35394558
  REMARK    GeneRIF: Hsa_circ_0008344 Promotes Glioma Tumor Progression and
            Angiogenesis Presumably by Regulating miR-638/SZRD1 Pathway.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Geng,Y.B., Pan,C.C., Xu,C., Zuo,P.C., Wang,Y., Li,X.O. and
            Zhang,L.W.
  TITLE     Long non-coding RNA LINC00346 regulates proliferation and apoptosis
            by targeting miR-128-3p/SZRD1 axis in glioma
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (18), 9581-9590 (2020)
   PUBMED   33015801
  REMARK    GeneRIF: Long non-coding RNA LINC00346 regulates proliferation and
            apoptosis by targeting miR-128-3p/SZRD1 axis in glioma.
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB501645.1, AB097046.1, BC010631.1 and AL358794.19.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.511386.1,
                                           SRR3476690.308028.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401088.9/ ENSP00000383866.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..152
                     /product="SUZ RNA-binding domain-containing isoform 1"
                     /note="putative MAPK activating protein PM20,PM21; SUZ
                     RNA-binding domain-containing; putative MAPK-activating
                     protein PM18/PM20/PM22; UPF0485 protein C1orf144; SUZ
                     domain-containing protein 1"
                     /calculated_mol_wt=16866
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q7Z422.1)"
     Region          30..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z422.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z422.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z422.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z422.1)"
     Region          56..107
                     /region_name="SUZ"
                     /note="SUZ domain; pfam12752"
                     /db_xref="CDD:463689"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z422.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z422.1)"
     Region          119..151
                     /region_name="SUZ-C"
                     /note="SUZ-C motif; pfam12901"
                     /db_xref="CDD:463745"
     CDS             1..152
                     /gene="SZRD1"
                     /gene_synonym="C1orf144"
                     /coded_by="NM_001114600.3:17..475"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44065.1"
                     /db_xref="GeneID:26099"
                     /db_xref="HGNC:HGNC:30232"
                     /db_xref="MIM:620682"
ORIGIN      
        1 medeevaesw eeaadsgeid rrlekklkit qkesrksksp pkvpiviqdd slpagpppqi
       61 rilkrptsng vvsspnstsr ptlpvkslaq reaeyaeark rilgsaspee eqekpildrp
      121 trisqpedsr qpnnvirqpl gpdgsqgfkq rr
//
LOCUS       NP_001252                372 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 9 [Homo sapiens].
ACCESSION   NP_001252
VERSION     NP_001252.1
DBSOURCE    REFSEQ: accession NM_001261.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kwon,N., Lu,Y.C., Thompson,E.N., Mancuso,R.I., Wang,L., Zhang,P.X.
            and Krause,D.S.
  TITLE     CDK9 phosphorylates RUNX1 to promote megakaryocytic fate in
            megakaryocytic-erythroid progenitors
  JOURNAL   Blood 144 (17), 1800-1812 (2024)
   PUBMED   39102635
  REMARK    GeneRIF: CDK9 phosphorylates RUNX1 to promote megakaryocytic fate
            in megakaryocytic-erythroid progenitors.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Walker,R.L., Hornicek,F.J. and Duan,Z.
  TITLE     Transcriptional regulation and therapeutic potential of
            cyclin-dependent kinase 9 (CDK9) in sarcoma
  JOURNAL   Biochem Pharmacol 226, 116342 (2024)
   PUBMED   38848777
  REMARK    GeneRIF: Transcriptional regulation and therapeutic potential of
            cyclin-dependent kinase 9 (CDK9) in sarcoma.
            Review article
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Eaton,J.D., Board,J., Davidson,L., Estell,C. and West,S.
  TITLE     Human promoter directionality is determined by transcriptional
            initiation and the opposing activities of INTS11 and CDK9
  JOURNAL   Elife 13, 92764 (2024)
   PUBMED   38976490
  REMARK    GeneRIF: Human promoter directionality is determined by
            transcriptional initiation and the opposing activities of INTS11
            and CDK9.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Zhou,Q. and Sharp,P.A.
  TITLE     Tat-SF1: cofactor for stimulation of transcriptional elongation by
            HIV-1 Tat
  JOURNAL   Science 274 (5287), 605-610 (1996)
   PUBMED   8849451
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Yang,X., Herrmann,C.H. and Rice,A.P.
  TITLE     The human immunodeficiency virus Tat proteins specifically
            associate with TAK in vivo and require the carboxyl-terminal domain
            of RNA polymerase II for function
  JOURNAL   J Virol 70 (7), 4576-4584 (1996)
   PUBMED   8676484
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Best,J.L., Presky,D.H., Swerlick,R.A., Burns,D.K. and Chu,W.
  TITLE     Cloning of a full-length cDNA sequence encoding a cdc2-related
            protein kinase from human endothelial cells
  JOURNAL   Biochem Biophys Res Commun 208 (2), 562-568 (1995)
   PUBMED   7695608
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Herrmann,C.H. and Rice,A.P.
  TITLE     Lentivirus Tat proteins specifically associate with a cellular
            protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal
            domain of the large subunit of RNA polymerase II: candidate for a
            Tat cofactor
  JOURNAL   J Virol 69 (3), 1612-1620 (1995)
   PUBMED   7853496
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Grana,X., De Luca,A., Sang,N., Fu,Y., Claudio,P.P., Rosenblatt,J.,
            Morgan,D.O. and Giordano,A.
  TITLE     PITALRE, a nuclear CDC2-related protein kinase that phosphorylates
            the retinoblastoma protein in vitro
  JOURNAL   Proc Natl Acad Sci U S A 91 (9), 3834-3838 (1994)
   PUBMED   8170997
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB120461.1, BC001968.1,
            BX091973.1, BE549667.1 and AL162586.26.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            cyclin-dependent protein kinase (CDK) family. CDK family members
            are highly similar to the gene products of S. cerevisiae cdc28, and
            S. pombe cdc2, and known as important cell cycle regulators. This
            kinase was found to be a component of the multiprotein complex
            TAK/P-TEFb, which is an elongation factor for RNA polymerase
            II-directed transcription and functions by phosphorylating the
            C-terminal domain of the largest subunit of RNA polymerase II. This
            protein forms a complex with and is regulated by its regulatory
            subunit cyclin T or cyclin K. HIV-1 Tat protein was found to
            interact with this protein and cyclin T, which suggested a possible
            involvement of this protein in AIDS. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.80290.1,
                                           SRR1803615.115236.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373264.5/ ENSP00000362361.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..372
                     /product="cyclin-dependent kinase 9"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="serine/threonine protein kinase PITALRE; cell
                     division protein kinase 9; CDC2-related kinase; cell
                     division cycle 2-like protein kinase 4; tat-associated
                     kinase complex catalytic subunit"
                     /calculated_mol_wt=42647
     Region          6..315
                     /region_name="STKc_CDK9"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 9; cd07865"
                     /db_xref="CDD:270848"
     Site            order(8..13,57..59,61,64,68,71,81..84,86,99)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270848"
     Site            order(25..28,33,46,48,65,79,103..106,109,111..112,149,151,
                     153..154,156,167,170,186,188..191,193,231..232)
                     /site_type="active"
                     /db_xref="CDD:270848"
     Site            order(25..28,33,46,48,79,103..106,109,112,153..154,156,
                     167)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270848"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            44
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300/CBP, PCAF/KAT2B and
                     GCN5/KAT2A. /evidence=ECO:0000269|PubMed:17452463,
                     ECO:0000269|PubMed:18250157; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by PCAF/KAT2B and GCN5/KAT2A.
                     /evidence=ECO:0000269|PubMed:18250157,
                     ECO:0000269|PubMed:28426094; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            order(65,111,149,151,170,186,188..191,193,231..232)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270848"
     Site            order(166..180,183..193)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270848"
     Region          166..191
                     /region_name="T-loop"
                     /note="propagated from UniProtKB/Swiss-Prot (P50750.3)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21533037; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CaMK1D.
                     /evidence=ECO:0000269|PubMed:15965233,
                     ECO:0000269|PubMed:18483222, ECO:0000269|PubMed:18566585,
                     ECO:0000269|PubMed:18829461, ECO:0000269|PubMed:20535204,
                     ECO:0000269|PubMed:20851342, ECO:0000269|PubMed:21448926,
                     ECO:0000269|PubMed:21779453, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P50750.3)"
     Region          343..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50750.3)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9 and PKA.
                     /evidence=ECO:0000269|PubMed:10958691,
                     ECO:0000269|PubMed:18566585, ECO:0000269|PubMed:39603239,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK9.
                     /evidence=ECO:0000269|PubMed:10958691,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000269|PubMed:10958691; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK9.
                     /evidence=ECO:0000269|PubMed:10958691; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK9.
                     /evidence=ECO:0000269|PubMed:10958691; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK9.
                     /evidence=ECO:0000269|PubMed:18566585; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK9.
                     /evidence=ECO:0000269|PubMed:18566585; propagated from
                     UniProtKB/Swiss-Prot (P50750.3)"
     CDS             1..372
                     /gene="CDK9"
                     /gene_synonym="C-2k; CDC2L4; CTK1; PITALRE; TAK"
                     /coded_by="NM_001261.4:116..1234"
                     /db_xref="CCDS:CCDS6879.1"
                     /db_xref="GeneID:1025"
                     /db_xref="HGNC:HGNC:1780"
                     /db_xref="MIM:603251"
ORIGIN      
        1 makqydsvec pfcdevskye klakigqgtf gevfkarhrk tgqkvalkkv lmenekegfp
       61 italreikil qllkhenvvn lieicrtkas pynrckgsiy lvfdfcehdl agllsnvlvk
      121 ftlseikrvm qmllnglyyi hrnkilhrdm kaanvlitrd gvlkladfgl arafslakns
      181 qpnrytnrvv tlwyrppell lgerdygppi dlwgagcima emwtrspimq gnteqhqlal
      241 isqlcgsitp evwpnvdnye lyeklelvkg qkrkvkdrlk ayvrdpyald lidkllvldp
      301 aqridsddal nhdffwsdpm psdlkgmlst hltsmfeyla pprrkgsqit qqstnqsrnp
      361 attnqtefer vf
//
LOCUS       NP_001280134             827 aa            linear   PRI 20-NOV-2025
DEFINITION  major vault protein isoform 3 [Homo sapiens].
ACCESSION   NP_001280134
VERSION     NP_001280134.1
DBSOURCE    REFSEQ: accession NM_001293205.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 827)
  AUTHORS   Li,C., Gao,M., Zha,N. and Guo,G.
  TITLE     The prognostic value and immunological role of MVP in pan-cancer
            study
  JOURNAL   Aging (Albany NY) 16 (10), 8497-8510 (2024)
   PUBMED   38713157
  REMARK    GeneRIF: The prognostic value and immunological role of MVP in
            pan-cancer study.
REFERENCE   2  (residues 1 to 827)
  AUTHORS   Taube,M., Lisiak,N., Toton,E. and Rubis,B.
  TITLE     Human Vault RNAs: Exploring Their Potential Role in Cellular
            Metabolism
  JOURNAL   Int J Mol Sci 25 (7), 4072 (2024)
   PUBMED   38612882
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 827)
  AUTHORS   Yu,C., Zhu,Q., Ma,C., Luo,C., Nie,L., Cai,H., Wang,Q., Wang,F.,
            Ren,H., Yan,H., Xu,K., Zhou,L., Zhang,C., Lu,G., Lu,Z., Zhu,Y. and
            Liu,S.
  TITLE     Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6
  JOURNAL   Front Immunol 14, 1289795 (2024)
   PUBMED   38264642
  REMARK    GeneRIF: Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 827)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 827)
  AUTHORS   Holzmann,K., Ambrosch,I., Elbling,L., Micksche,M. and Berger,W.
  TITLE     A small upstream open reading frame causes inhibition of human
            major vault protein expression from a ubiquitous mRNA splice
            variant
  JOURNAL   FEBS Lett 494 (1-2), 99-104 (2001)
   PUBMED   11297743
  REMARK    GeneRIF: MVP gene expression regulated by alternative splicing due
            to generation of an upstream open reading frame
REFERENCE   6  (residues 1 to 827)
  AUTHORS   Dingemans,A.M., van Ark-Otte,J., van der Valk,P., Apolinario,R.M.,
            Scheper,R.J., Postmus,P.E. and Giaccone,G.
  TITLE     Expression of the human major vault protein LRP in human lung
            cancer samples and normal lung tissues
  JOURNAL   Ann Oncol 7 (6), 625-630 (1996)
   PUBMED   8879378
REFERENCE   7  (residues 1 to 827)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Schroeijers,A.B., van
            der Valk,P. and Scheper,R.J.
  TITLE     Major vault protein LRP-related multidrug resistance
  JOURNAL   Eur J Cancer 32A (6), 979-984 (1996)
   PUBMED   8763338
  REMARK    Review article
REFERENCE   8  (residues 1 to 827)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Giaccone,G.,
            Broxterman,H.J., Meijer,C.J., van der Valk,P. and Scheper,R.J.
  TITLE     Broad distribution of the multidrug resistance-related vault lung
            resistance protein in normal human tissues and tumors
  JOURNAL   Am J Pathol 148 (3), 877-887 (1996)
   PUBMED   8774142
REFERENCE   9  (residues 1 to 827)
  AUTHORS   Slovak,M.L., Ho,J.P., Cole,S.P., Deeley,R.G., Greenberger,L., de
            Vries,E.G., Broxterman,H.J., Scheffer,G.L. and Scheper,R.J.
  TITLE     The LRP gene encoding a major vault protein associated with drug
            resistance maps proximal to MRP on chromosome 16: evidence that
            chromosome breakage plays a key role in MRP or LRP gene
            amplification
  JOURNAL   Cancer Res 55 (19), 4214-4219 (1995)
   PUBMED   7671223
REFERENCE   10 (residues 1 to 827)
  AUTHORS   Scheffer,G.L., Wijngaard,P.L., Flens,M.J., Izquierdo,M.A.,
            Slovak,M.L., Pinedo,H.M., Meijer,C.J., Clevers,H.C. and
            Scheper,R.J.
  TITLE     The drug resistance-related protein LRP is the human major vault
            protein
  JOURNAL   Nat Med 1 (6), 578-582 (1995)
   PUBMED   7585126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ291366.1, KJ534885.1,
            BC015623.2 and BM999583.1.
            
            Summary: This gene encodes the major component of the vault
            complex. Vaults are multi-subunit ribonucleoprotein structures that
            may be involved in nucleo-cytoplasmic transport. The encoded
            protein may play a role in multiple cellular processes by
            regulating the MAP kinase, JAK/STAT and phosphoinositide
            3-kinase/Akt signaling pathways. The encoded protein also plays a
            role in multidrug resistance, and expression of this gene may be a
            prognostic marker for several types of cancer. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            central coding region, compared to variant 1. The resulting isoform
            (3) lacks an internal segment, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KJ534885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..827
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..827
                     /product="major vault protein isoform 3"
                     /note="lung resistance-related protein; testicular
                     secretory protein Li 30"
                     /calculated_mol_wt=91839
     Region          4..784
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     CDS             1..827
                     /gene="MVP"
                     /gene_synonym="LRP; VAULT1"
                     /coded_by="NM_001293205.1:36..2519"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:9961"
                     /db_xref="HGNC:HGNC:7531"
                     /db_xref="MIM:605088"
ORIGIN      
        1 mateefiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapmrm vtvpprhyct
       61 vanpvsrdaq glvlfdvtgq vrlrhadlei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkdgdkvvag dewlfegpgt yiprkevevv eiiqatiirq nqalrlrark
      181 ecwdrdgker vtgeewlvtt vgaylpavfe evldlvdavi ltektalhlr arrnfrdfrg
      241 vsrrtgeewl vtvqdteahv pdvheevlgv vpittlgphn ycvildpvgp dgknqlgqkr
      301 vvkgeksffl qpgeqleqgi qdvyvlseqq glllralqpl eegedeekvs hqagdhwlir
      361 gpleyvpsak vevveerqai pldenegiyv qdvktgkvra vigstymltq devlwekelp
      421 pgveellnkg qdpladrgek dtakslqpla prnktrvvsy rvphnaavqv ydyrekrarh
      481 fevndrkdpq etaklfsvpd fvgdackaia srvrgavasv tfddfhknsa riirtavfgf
      541 etseakgpdg malprprdqa vfpqnglvvs svdvqsvepv dqrtrdalqr svqlaieitt
      601 nsqeaaakhe aqrleqearg rlerqkildq seaekarkel lelealsmav estgtakaea
      661 esraeaarie gegsvlqakl kaqalaiete aelqrvqkvr elelvyaraq lelevskaqq
      721 laevevkkfk qmteaigpst irdlavagpe mqvkllqslg lkstlitdgs tpinlfntaf
      781 gllgmgpegq plgrrvasgp spgegispqs aqapqapgdn hvvpvlr
//
LOCUS       NP_001340525             468 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform h [Homo sapiens].
ACCESSION   NP_001340525 XP_005267998
VERSION     NP_001340525.1
DBSOURCE    REFSEQ: accession NM_001353596.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_005267998.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (11), as well as variant 10,
            encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.243889.1,
                                           SRR1803617.198579.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..468
                     /product="lysosomal cobalamin transporter ABCD4 isoform h"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=51813
     Region          <53..465
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..468
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353596.2:304..1710"
                     /note="isoform h is encoded by transcript variant 11"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mtsitrtsas artwsdsags saawpassss prspssttlt saskgwlgpv sifgyfilgt
       61 vvnktlmgpi vmklvhqekl egdfrfkhmq irvnaepaaf yraghvehmr tdrrlqrllq
      121 tqrelmskel wlyigintfd ylgsilsyvv iaipifsgvy gdlspaelst lvsknafvci
      181 yliscftqli dlsttlsdva gythrigqlr etlldmslks qdceilgese wgldtppgwp
      241 aaepadtafl lervsisaps sdkplikdls lkisegqsll itgntgtgkt sllrvlgglw
      301 tstrgsvqml tdfgphgvlf lpqkpfftdg tlreqviypl kevypdsgsa dderilrfle
      361 laglsnlvar tegldqqvdw nwydvlspge mqrlsfarlf ylqpkyavld eatsalteev
      421 eselyrigqq lgmtfisvgh rqslekfhsl vlklcgggrw elmrikve
//
LOCUS       NP_775101                837 aa            linear   PRI 20-NOV-2025
DEFINITION  SLIT and NTRK-like protein 4 precursor [Homo sapiens].
ACCESSION   NP_775101
VERSION     NP_775101.1
DBSOURCE    REFSEQ: accession NM_173078.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Kuo,F.C., Huang,Y.C., Yen,M.R., Lee,C.H., Hsu,K.F., Yang,H.Y.,
            Wu,L.W., Lu,C.H., Hsu,Y.J. and Chen,P.Y.
  TITLE     Aberrant overexpression of HOTAIR inhibits abdominal adipogenesis
            through remodelling of genome-wide DNA methylation and
            transcription
  JOURNAL   Mol Metab 60, 101473 (2022)
   PUBMED   35292404
  REMARK    GeneRIF: Aberrant overexpression of HOTAIR inhibits abdominal
            adipogenesis through remodelling of genome-wide DNA methylation and
            transcription.
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Yim,Y.S., Kwon,Y., Nam,J., Yoon,H.I., Lee,K., Kim,D.G., Kim,E.,
            Kim,C.H. and Ko,J.
  TITLE     Slitrks control excitatory and inhibitory synapse formation with
            LAR receptor protein tyrosine phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 110 (10), 4057-4062 (2013)
   PUBMED   23345436
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2024 Jun 18;121(25):e2410441121.
            doi: 10.1073/pnas.2410441121. PMID: 38870062]
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Haakensen,V.D., Bjoro,T., Luders,T., Riis,M., Bukholm,I.K.,
            Kristensen,V.N., Troester,M.A., Homen,M.M., Ursin,G.,
            Borresen-Dale,A.L. and Helland,A.
  TITLE     Serum estradiol levels associated with specific gene expression
            patterns in normal breast tissue and in breast carcinomas
  JOURNAL   BMC Cancer 11, 332 (2011)
   PUBMED   21812955
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Loset,M., Mundal,S.B., Johnson,M.P., Fenstad,M.H., Freed,K.A.,
            Lian,I.A., Eide,I.P., Bjorge,L., Blangero,J., Moses,E.K. and
            Austgulen,R.
  TITLE     A transcriptional profile of the decidua in preeclampsia
  JOURNAL   Am J Obstet Gynecol 204 (1), 84 (2011)
   PUBMED   20934677
REFERENCE   8  (residues 1 to 837)
  AUTHORS   Aruga,J., Yokota,N. and Mikoshiba,K.
  TITLE     Human SLITRK family genes: genomic organization and expression
            profiling in normal brain and brain tumor tissue
  JOURNAL   Gene 315, 87-94 (2003)
   PUBMED   14557068
REFERENCE   9  (residues 1 to 837)
  AUTHORS   Aruga,J. and Mikoshiba,K.
  TITLE     Identification and characterization of Slitrk, a novel neuronal
            transmembrane protein family controlling neurite outgrowth
  JOURNAL   Mol Cell Neurosci 24 (1), 117-129 (2003)
   PUBMED   14550773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239921.3.
            
            Summary: This gene encodes a transmembrane protein belonging to the
            the SLITRK family. These family members include two N-terminal
            leucine-rich repeat domains similar to those found in the axonal
            growth-controlling protein SLIT, as well as C-terminal regions
            similar to neurotrophin receptors. Studies of an homologous protein
            in mouse suggest that this family member functions to suppress
            neurite outgrowth. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.99580.1,
                                           SRR1803612.6973.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq27.3"
     Protein         1..837
                     /product="SLIT and NTRK-like protein 4 precursor"
                     /note="slit and trk like gene 4"
                     /calculated_mol_wt=92309
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2041
     mat_peptide     19..837
                     /product="SLIT and NTRK-like protein 4.
                     /evidence=ECO:0000255. /id=PRO_0000032679"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
                     /calculated_mol_wt=92309
     Region          <59..>213
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          60..81
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          63..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          84..105
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          108..129
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          109..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          132..153
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          133..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          156..177
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          157..179
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..200
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          180..204
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..295
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          213..>253
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          296..371
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          <358..>531
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          372..402
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          378..399
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          402..423
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          403..426
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          426..447
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          427..450
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          450..471
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          451..472
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          474..495
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          475..496
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          497..518
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          498..522
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          502..>563
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Site            619..639
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     CDS             1..837
                     /gene="SLITRK4"
                     /coded_by="NM_173078.5:264..2777"
                     /db_xref="CCDS:CCDS14679.1"
                     /db_xref="GeneID:139065"
                     /db_xref="HGNC:HGNC:23502"
                     /db_xref="MIM:300562"
ORIGIN      
        1 mflwlflils alisstnads disveicnvc scvsvenvly vncekvsvyr pnqlkppwsn
       61 fyhlnfqnnf lnilypntfl nfshavslhl gnnklqnieg gaflglsalk qlhlnnnelk
      121 ilradtflgi enleylqady nlikyierga fnklhklkvl ilndnlisfl pdnifrfasl
      181 thldirgnri qklpyigvle higrvvelql ednpwncscd llplkawlen mpyniyigea
      241 icetpsdlyg rllketnkqe lcpmgtgsdf dvrilppsql engyttpngh ttqtslhrlv
      301 tkppkttnps kisgivagka lsnrnlsqiv syqtrvpplt pcpapcfckt hpsdlglsvn
      361 cqekniqsms elipkplnak klhvngnsik dvdvsdftdf egldllhlgs nqitvikgdv
      421 fhnltnlrrl ylngnqierl ypeifsglhn lqylyleynl ikeisagtfd smpnlqllyl
      481 nnnllkslpv yifsgaplar lnlrnnkfmy lpvsgvldql qsltqidleg npwdctcdlv
      541 alklwvekls dgivvkelkc etpvqfanie lkslkneilc pkllnkpsap ftspapaitf
      601 ttplgpirsp pggpvplsil ilsilvvlil tvfvafcllv fvlrrnkkpt vkheglgnpd
      661 cgsmqlqlrk hdhktnkkdg lsteafipqt ieqmskshtc glkesetgfm fsdppgqkvv
      721 mrnvadkekd llhvdtrkrl stideldelf psrdsnvfiq nfleskkeyn sigvsgfeir
      781 ypekqpdkks kksliggnhs kivveqrkse yfelkaklqs spdylqvlee qtalnki
//
LOCUS       NP_001303292             330 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001303292
VERSION     NP_001303292.1
DBSOURCE    REFSEQ: accession NM_001316363.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Fatalska,A., Hodgson,G., Freund,S.M.V., Maslen,S.L., Morgan,T.,
            Thorkelsson,S.R., van Slegtenhorst,M., Lorenz,S., Andreeva,A.,
            Kaat,L.D. and Bertolotti,A.
  TITLE     Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit
            PPP1R15B
  JOURNAL   Mol Cell 84 (3), 506-521 (2024)
   PUBMED   38159565
  REMARK    GeneRIF: Recruitment of trimeric eIF2 by phosphatase non-catalytic
            subunit PPP1R15B.
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 330)
  AUTHORS   Das,S., Maiti,T., Das,K. and Maitra,U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 5
            (eIF5) with the beta-subunit of eIF2
  JOURNAL   J Biol Chem 272 (50), 31712-31718 (1997)
   PUBMED   9395514
REFERENCE   7  (residues 1 to 330)
  AUTHORS   Brand,S.R., Kobayashi,R. and Mathews,M.B.
  TITLE     The Tat protein of human immunodeficiency virus type 1 is a
            substrate and inhibitor of the interferon-induced, virally
            activated protein kinase, PKR
  JOURNAL   J Biol Chem 272 (13), 8388-8395 (1997)
   PUBMED   9079663
REFERENCE   8  (residues 1 to 330)
  AUTHORS   Welsh,G.I., Price,N.T., Bladergroen,B.A., Bloomberg,G. and
            Proud,C.G.
  TITLE     Identification of novel phosphorylation sites in the beta-subunit
            of translation initiation factor eIF-2
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1279-1288 (1994)
   PUBMED   8024572
REFERENCE   9  (residues 1 to 330)
  AUTHORS   Pathak,V.K., Nielsen,P.J., Trachsel,H. and Hershey,J.W.
  TITLE     Structure of the beta subunit of translational initiation factor
            eIF-2
  JOURNAL   Cell 54 (5), 633-639 (1988)
   PUBMED   3044606
REFERENCE   10 (residues 1 to 330)
  AUTHORS   Safer,B., Adams,S.L., Anderson,W.F. and Merrick,W.C.
  TITLE     Binding of MET-TRNAf and GTP to homogeneous initiation factor MP
  JOURNAL   J Biol Chem 250 (23), 9076-9082 (1975)
   PUBMED   1104615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY005227.1, BX429051.2,
            AL031668.23 and CA436754.1.
            
            Summary: Eukaryotic translation initiation factor 2 (EIF-2)
            functions in the early steps of protein synthesis by forming a
            ternary complex with GTP and initiator tRNA and binding to a 40S
            ribosomal subunit. EIF-2 is composed of three subunits, alpha,
            beta, and gamma, with the protein encoded by this gene representing
            the beta subunit. The beta subunit catalyzes the exchange of GDP
            for GTP, which recycles the EIF-2 complex for another round of
            initiation. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2015].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.328020.1, BX429051.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..330
                     /product="eukaryotic translation initiation factor 2
                     subunit 2 isoform 2"
                     /note="eukaryotic translation initiation factor 2 subunit
                     2; protein phosphatase 1, regulatory subunit 67;
                     eukaryotic translation initiation factor 2, subunit 2
                     beta, 38kDa; eIF2-beta"
                     /calculated_mol_wt=37901
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Region          136..161
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20042.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Region          196..305
                     /region_name="eIF2B_5"
                     /note="domain present in translation initiation factor
                     eIF2B and eIF5; smart00653"
                     /db_xref="CDD:214764"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41035; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            262
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     Site            290
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P20042.2)"
     CDS             1..330
                     /gene="EIF2S2"
                     /gene_synonym="eIF-2-beta; EIF2; EIF2B; EIF2beta; PPP1R67"
                     /coded_by="NM_001316363.2:134..1126"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:8894"
                     /db_xref="HGNC:HGNC:3266"
                     /db_xref="MIM:603908"
ORIGIN      
        1 msgdemifdp tmskkkkkkk kpfmldeegd tqteetqpse tkevepepte dkdleadeed
       61 trkkdasddl ddlnffnqkk kkkktkkifd ideaeegvki esdvqeptep eddldimlgn
      121 kkkkkknvkf pdedeilekd ealedednkk ddgisfsnqt gpawagserd ytyeellnrv
      181 fnimreknpd mvagekrkfv mkppqvvrvg tkktsfvnft dickllhrqp khllafllae
      241 lgtsgsidgn nqlvikgrfq qkqienvlrr yikeyvtcht crspdtilqk dtrlyflqce
      301 tchsrcsvas iktgfqavtg kraqlrakan
//
LOCUS       NP_001271342             551 aa            linear   PRI 20-NOV-2025
DEFINITION  2-hydroxyacyl-CoA lyase 1 isoform b [Homo sapiens].
ACCESSION   NP_001271342 XP_005265095
VERSION     NP_001271342.1
DBSOURCE    REFSEQ: accession NM_001284413.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Kitamura,T., Seki,N. and Kihara,A.
  TITLE     Phytosphingosine degradation pathway includes fatty acid
            alpha-oxidation reactions in the endoplasmic reticulum
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), E2616-E2623 (2017)
   PUBMED   28289220
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Mezzar,S., de Schryver,E. and Van Veldhoven,P.P.
  TITLE     RP-HPLC-fluorescence analysis of aliphatic aldehydes: application
            to aldehyde-generating enzymes HACL1 and SGPL1
  JOURNAL   J Lipid Res 55 (3), 573-582 (2014)
   PUBMED   24323699
  REMARK    GeneRIF: Data show that a easy assay for 2-hydroxyacyl-CoA lyase
            (HACL1) and sphingosine-1-phosphate lyase (SGPL1) activities was
            developed.
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Wanders,R.J. and Waterham,H.R.
  TITLE     Biochemistry of mammalian peroxisomes revisited
  JOURNAL   Annu Rev Biochem 75, 295-332 (2006)
   PUBMED   16756494
  REMARK    Review article
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Foulon,V., Sniekers,M., Huysmans,E., Asselberghs,S., Mahieu,V.,
            Mannaerts,G.P., Van Veldhoven,P.P. and Casteels,M.
  TITLE     Breakdown of 2-hydroxylated straight chain fatty acids via
            peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the
            alpha-oxidation of straight chain fatty acids
  JOURNAL   J Biol Chem 280 (11), 9802-9812 (2005)
   PUBMED   15644336
  REMARK    GeneRIF: 2-hydroxyphytanoyl-CoA lyase has a role in the breakdown
            of long chain 2-hydroxyfatty acids
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Foulon,V., Antonenkov,V.D., Croes,K., Waelkens,E., Mannaerts,G.P.,
            Van Veldhoven,P.P. and Casteels,M.
  TITLE     Purification, molecular cloning, and expression of
            2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine
            pyrophosphate-dependent enzyme that catalyzes the carbon-carbon
            bond cleavage during alpha-oxidation of 3-methyl-branched fatty
            acids
  JOURNAL   Proc Natl Acad Sci U S A 96 (18), 10039-10044 (1999)
   PUBMED   10468558
  REMARK    GeneRIF: peroxisomal thiamine-pyrophosphate depending enzyme
            required for the degradation of phytanic acid, catalyzing the
            cleavage of 2-hydroxyphytanoyl-CoA lyase into formyl-CoA and
            pristanal
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA609383.1, AK301546.1, AA643224.1 and AC027129.6.
            
            On Oct 1, 2013 this sequence version replaced XP_005265095.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (b) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301546.1, SRR1803617.37189.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..551
                     /product="2-hydroxyacyl-CoA lyase 1 isoform b"
                     /EC_number="4.1.2.63"
                     /note="2-hydroxyphytanol-CoA lyase; phytanoyl-CoA
                     2-hydroxylase 2; 1600020H07Rik; phytanoyl-CoA hydroxylase
                     2; 2-hydroxyphytanoyl-CoA lyase"
                     /calculated_mol_wt=60934
     Region          7..536
                     /region_name="PRK09259"
                     /note="putative oxalyl-CoA decarboxylase; Validated"
                     /db_xref="CDD:236433"
     CDS             1..551
                     /gene="HACL1"
                     /gene_synonym="2-HPCL; HPCL; HPCL2; PHYH2"
                     /coded_by="NM_001284413.2:107..1762"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS68360.1"
                     /db_xref="GeneID:26061"
                     /db_xref="HGNC:HGNC:17856"
                     /db_xref="MIM:604300"
ORIGIN      
        1 mpdsnfaers eeqvsgakvi aqalktqdve yifgivgipv teiaiaaqql gikyigmrne
       61 qaacyaasai gyltsrpllv iggssernqe tmgafqefpq veacrlytkf sarpssieai
      121 pfviekavrs siygrpgacy vdipadfvnl qvnvnsikym ercmsppism aetsavctaa
      181 svirnakqpl liigkgaaya haeesikklv eqyklpflpt pmgkgvvpdn hpycvgaars
      241 ralqfadviv lfgarlnwil hfglppryqp dvkfiqvdic aeelgnnvkp avtllgniha
      301 vtkqlleeld ktpwqyppes kwwktlrekm ksneaaskel askkslpmny ytvfyhvqeq
      361 lprdcfvvse gantmdigrt vlqnylprhr ldagtfgtmg vglgfaiaaa vvakdrspgq
      421 wiicvegdsa fgfsgmevet icrynlpiil lvvnnngiyq gfdtdtwkem lkfqdatavv
      481 ppmcllpnsh yeqvmtafgg kgyfvqtpee lqkslrqsla dttkpslini miepqatrka
      541 qdfhwltrsn m
//
LOCUS       NP_004555                557 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
            isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004555
VERSION     NP_004555.1
DBSOURCE    REFSEQ: accession NM_004564.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Friederich,M.W., Timal,S., Powell,C.A., Dallabona,C., Kurolap,A.,
            Palacios-Zambrano,S., Bratkovic,D., Derks,T.G.J., Bick,D.,
            Bouman,K., Chatfield,K.C., Damouny-Naoum,N., Dishop,M.K.,
            Falik-Zaccai,T.C., Fares,F., Fedida,A., Ferrero,I., Gallagher,R.C.,
            Garesse,R., Gilberti,M., Gonzalez,C., Gowan,K., Habib,C.,
            Halligan,R.K., Kalfon,L., Knight,K., Lefeber,D., Mamblona,L.,
            Mandel,H., Mory,A., Ottoson,J., Paperna,T., Pruijn,G.J.M.,
            Rebelo-Guiomar,P.F., Saada,A., Sainz,B. Jr., Salvemini,H.,
            Schoots,M.H., Smeitink,J.A., Szukszto,M.J., Ter Horst,H.J., van den
            Brandt,F., van Spronsen,F.J., Veltman,J.A., Wartchow,E.,
            Wintjes,L.T., Zohar,Y., Fernandez-Moreno,M.A., Baris,H.N.,
            Donnini,C., Minczuk,M., Rodenburg,R.J. and Van Hove,J.L.K.
  TITLE     Pathogenic variants in glutamyl-tRNAGln amidotransferase subunits
            cause a lethal mitochondrial cardiomyopathy disorder
  JOURNAL   Nat Commun 9 (1), 4065 (2018)
   PUBMED   30283131
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Nagao,A., Suzuki,T., Katoh,T., Sakaguchi,Y. and Suzuki,T.
  TITLE     Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
  JOURNAL   Proc Natl Acad Sci U S A 106 (38), 16209-16214 (2009)
   PUBMED   19805282
  REMARK    GeneRIF: Studies showed in vitro Gln-tRNA(Gln) formation catalyzed
            by the recombinant mtGluRS and hGatCAB.
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Petruzzella,V., Tiranti,V., Fernandez,P., Ianna,P., Carrozzo,R. and
            Zeviani,M.
  TITLE     Identification and characterization of human cDNAs specific to
            BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the
            formation and function of the mitochondrial respiratory chain
  JOURNAL   Genomics 54 (3), 494-504 (1998)
   PUBMED   9878253
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC130348.1 and AC092611.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067838.1, SRR1803614.40659.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000263985.11/
                                                  ENSP00000263985.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..557
                     /product="glutamyl-tRNA(Gln) amidotransferase subunit B,
                     mitochondrial isoform 1 precursor"
                     /note="cytochrome oxidase assembly factor PET112 homolog;
                     cytochrome c oxidase assembly factor PET112 homolog;
                     glutamyl-tRNA(Gln) amidotransferase, subunit B"
                     /calculated_mol_wt=57394
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O75879.1)"
                     /calculated_mol_wt=4488
     Region          26..45
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75879.1)"
     mat_peptide     42..557
                     /product="Glutamyl-tRNA(Gln) amidotransferase subunit B,
                     mitochondrial. /id=PRO_0000010710"
                     /note="propagated from UniProtKB/Swiss-Prot (O75879.1)"
                     /calculated_mol_wt=57394
     Region          62..556
                     /region_name="GatB"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase B subunit
                     [Translation, ribosomal structure and biogenesis];
                     COG0064"
                     /db_xref="CDD:439834"
     CDS             1..557
                     /gene="GATB"
                     /gene_synonym="COXPD41; HSPC199; PET112; PET112L"
                     /coded_by="NM_004564.3:26..1699"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3776.1"
                     /db_xref="GeneID:5188"
                     /db_xref="HGNC:HGNC:8849"
                     /db_xref="MIM:603645"
ORIGIN      
        1 maapmlrwgc rgrrwafarv dggschrrga ptgstsnqir gessvaqqpl htaqktrkge
       61 hkwaavvgle ihaqissnsk lfsgsqvrfs appnslvsff daslpgtlpv lnrrcveaav
      121 mtglalnchi nkkslfdrkh yfyadlpagy qitqqrlpia vngsliygvc agkkqsqvip
      181 ktvrikqiql eqdsgkslhd nlrsqtlidl nragvgllev vlepdmscge eaatavrelq
      241 lilqalgtsq anmaegqlrv danisvhhpg eplgvrtevk nlnsirflak aidyeiqrqi
      301 nelenggeil netrsfhhkl gctmsmrdke gkqdyrfmpe pnlpplvlyd atslpagadp
      361 qqvinidqir etlpelpsvt reklvqqygm llehsftlln evglleffqn viketraepk
      421 kvtswvlntf lgylkqqnla vsespvtpsa laelldllds rtisssaakq vfeelwkreg
      481 ktpgqivsek qlelmqdqga leqlchsvme ahpqvvmdvk nrnprainkl iglvrkatqs
      541 radpvmikei lekklsl
//
LOCUS       NP_000883                638 aa            linear   PRI 20-NOV-2025
DEFINITION  plasma kallikrein isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_000883
VERSION     NP_000883.2
DBSOURCE    REFSEQ: accession NM_000892.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 638)
  AUTHORS   Longhurst,H.J., Lindsay,K., Petersen,R.S., Fijen,L.M., Gurugama,P.,
            Maag,D., Butler,J.S., Shah,M.Y., Golden,A., Xu,Y., Boiselle,C.,
            Vogel,J.D., Abdelhady,A.M., Maitland,M.L., McKee,M.D., Seitzer,J.,
            Han,B.W., Soukamneuth,S., Leonard,J., Sepp-Lorenzino,L.,
            Clark,E.D., Lebwohl,D. and Cohn,D.M.
  TITLE     CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary Angioedema
  JOURNAL   N Engl J Med 390 (5), 432-441 (2024)
   PUBMED   38294975
  REMARK    GeneRIF: CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary
            Angioedema.
REFERENCE   2  (residues 1 to 638)
  AUTHORS   Schachtl-Riess,J.F., Schonherr,S., Lamina,C., Forer,L., Coassin,S.,
            Streiter,G., Kheirkhah,A., Li,Y., Meiselbach,H., Di Maio,S.,
            Eckardt,K.U., Kottgen,A. and Kronenberg,F.
  CONSRTM   GCKD investigators
  TITLE     KLKB1 and CLSTN2 are associated with HDL-mediated cholesterol
            efflux capacity in a genome-wide association study
  JOURNAL   Atherosclerosis 368, 1-11 (2023)
   PUBMED   36812656
  REMARK    GeneRIF: KLKB1 and CLSTN2 are associated with HDL-mediated
            cholesterol efflux capacity in a genome-wide association study.
REFERENCE   3  (residues 1 to 638)
  AUTHORS   Feng,L., Liu,Y., Chen,M. and Hu,Y.
  TITLE     [Matrix metalloproteinase 14 and plasma kallikrein 1 may be
            potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 34 (7), 676-681 (2022)
   PUBMED   36100402
  REMARK    GeneRIF: [Matrix metalloproteinase 14 and plasma kallikrein 1 may
            be potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis].
REFERENCE   4  (residues 1 to 638)
  AUTHORS   Wan,J., Vadaq,N., Konings,J., Jaeger,M., Kumar,V., de Laat,B.,
            Joosten,L., Netea,M.G., van der Ven,A.J., de Groot,P.G., de Mast,Q.
            and Roest,M.
  TITLE     Kallikrein augments the anticoagulant function of the protein C
            system in thrombin generation
  JOURNAL   J Thromb Haemost 20 (1), 48-57 (2022)
   PUBMED   34532976
  REMARK    GeneRIF: Kallikrein augments the anticoagulant function of the
            protein C system in thrombin generation.
REFERENCE   5  (residues 1 to 638)
  AUTHORS   Beaubien,G., Rosinski-Chupin,I., Mattei,M.G., Mbikay,M.,
            Chretien,M. and Seidah,N.G.
  TITLE     Gene structure and chromosomal localization of plasma kallikrein
  JOURNAL   Biochemistry 30 (6), 1628-1635 (1991)
   PUBMED   1993180
REFERENCE   6  (residues 1 to 638)
  AUTHORS   Chung,D.W., Fujikawa,K., McMullen,B.A. and Davie,E.W.
  TITLE     Human plasma prekallikrein, a zymogen to a serine protease that
            contains four tandem repeats
  JOURNAL   Biochemistry 25 (9), 2410-2417 (1986)
   PUBMED   3521732
REFERENCE   7  (residues 1 to 638)
  AUTHORS   Thompson,R.E., Mandle,R. Jr. and Kaplan,A.P.
  TITLE     Studies of binding of prekallikrein and Factor XI to high molecular
            weight kininogen and its light chain
  JOURNAL   Proc Natl Acad Sci U S A 76 (10), 4862-4866 (1979)
   PUBMED   291905
REFERENCE   8  (residues 1 to 638)
  AUTHORS   Mandle,R.J. Jr. and Kaplan,A.P.
  TITLE     Hageman-factor-dependent fibrinolysis: generation of fibrinolytic
            activity by the interaction of human activated factor XI and
            plasminogen
  JOURNAL   Blood 54 (4), 850-862 (1979)
   PUBMED   89876
REFERENCE   9  (residues 1 to 638)
  AUTHORS   Aznar,J.A., Espana,F., Aznar,J., Tascon,A. and Jimenez,C.
  TITLE     Fletcher factor deficiency: report of a new family
  JOURNAL   Scand J Haematol 21 (2), 94-98 (1978)
   PUBMED   694428
REFERENCE   10 (residues 1 to 638)
  AUTHORS   Meier,H.L., Pierce,J.V., Colman,R.W. and Kaplan,A.P.
  TITLE     Activation and function of human Hageman factor. The role of high
            molecular weight kininogen and prekallikrein
  JOURNAL   J Clin Invest 60 (1), 18-31 (1977)
   PUBMED   874082
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292624.1, M13143.2,
            CN265612.1 and AW182528.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 27, 2005 this sequence version replaced NP_000883.1.
            
            Summary: This gene encodes a glycoprotein that participates in the
            surface-dependent activation of blood coagulation, fibrinolysis,
            kinin generation and inflammation. The encoded preproprotein
            present in plasma as a non-covalent complex with high molecular
            weight kininogen undergoes proteolytic processing mediated by
            activated coagulation factor XII to generate a disulfide-linked,
            heterodimeric serine protease comprised of heavy and light chains.
            Certain mutations in this gene cause prekallikrein deficiency.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292624.1, SRR5189664.88222.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264690.11/ ENSP00000264690.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..638
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.2"
     Protein         1..638
                     /product="plasma kallikrein isoform 1 preproprotein"
                     /EC_number="3.4.21.34"
                     /note="kallikrein B, plasma (Fletcher factor) 1;
                     kininogenin; plasma prekallikrein; plasma kallikrein"
                     /calculated_mol_wt=69177
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2184
     mat_peptide     20..390
                     /product="Plasma kallikrein heavy chain.
                     /id=PRO_0000028021"
                     /note="propagated from UniProtKB/Swiss-Prot (P03952.2)"
                     /calculated_mol_wt=41398
     Region          21..104
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(37,39,50)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          111..194
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(127,129,140)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:3521732; propagated from
                     UniProtKB/Swiss-Prot (P03952.2)"
     Region          201..284
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(217,219,230)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          292..375
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(308,310,321)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     mat_peptide     391..638
                     /product="Plasma kallikrein light chain.
                     /id=PRO_0000028022"
                     /note="propagated from UniProtKB/Swiss-Prot (P03952.2)"
                     /calculated_mol_wt=27798
     Region          391..621
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            391
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            396
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     Site            order(434,483,578)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            453
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:3521732; propagated from
                     UniProtKB/Swiss-Prot (P03952.2)"
     Site            494
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:3521732;
                     propagated from UniProtKB/Swiss-Prot (P03952.2)"
     Site            order(572,597,599)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..638
                     /gene="KLKB1"
                     /gene_synonym="KLK3; PKK; PKKD; PPK"
                     /coded_by="NM_000892.5:83..1999"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS34120.1"
                     /db_xref="GeneID:3818"
                     /db_xref="HGNC:HGNC:6371"
                     /db_xref="MIM:229000"
ORIGIN      
        1 milfkqatyf islfatvscg cltqlyenaf frggdvasmy tpnaqycqmr ctfhprcllf
       61 sflpassind mekrfgcflk dsvtgtlpkv hrtgavsghs lkqcghqisa chrdiykgvd
      121 mrgvnfnvsk vssveecqkr ctsnircqff syatqtfhka eyrnncllky spggtptaik
      181 vlsnvesgfs lkpcalseig chmnifqhla fsdvdvarvl tpdafvcrti ctyhpnclff
      241 tfytnvwkie sqrnvcllkt sesgtpssst pqentisgys lltckrtlpe pchskiypgv
      301 dfggeelnvt fvkgvnvcqe tctkmircqf ftysllpedc keekckcflr lsmdgsptri
      361 aygtqgssgy slrlcntgdn svcttktstr ivggtnsswg ewpwqvslqv kltaqrhlcg
      421 gslighqwvl taahcfdglp lqdvwriysg ilnlsditkd tpfsqikeii ihqnykvseg
      481 nhdialiklq aplnytefqk piclpskgdt stiytncwvt gwgfskekge iqnilqkvni
      541 plvtneecqk ryqdykitqr mvcagykegg kdackgdsgg plvckhngmw rlvgitswge
      601 gcarreqpgv ytkvaeymdw ilektqssdg kaqmqspa
//
LOCUS       NP_001106984             753 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform d [Homo sapiens].
ACCESSION   NP_001106984
VERSION     NP_001106984.1
DBSOURCE    REFSEQ: accession NM_001113512.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AB177848.1,
            BC033905.1, BC060776.1, BM677392.1, DB180957.1 and AK093326.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (4) lacks two alternate in-frame
            exons compared to variant 3. The resulting protein (isoform d) is
            shorter than isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033905.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..753
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     d"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=84346
     Region          3..86
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Region          88..134
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          138..191
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(143,145,148,151..152,167,169..171,182,184,186..187)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          222..399
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(228,232,326,350..351,354..355,357..358,361..362,
                     365..366,369,395,399)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          430..528
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          588..678
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     CDS             1..753
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001113512.2:909..3170"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45069.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mnsaeqtvtw litlgvlesp kktisdpegf lqaslkdgvv lcrllerllp gtiektfdan
       61 dlyqgqnfnk vlsslvtlnk vtadiglgsd svcarpsshr iksfdslgsq slhtrtsklf
      121 qgqyrsldmt dnsnnqlvvr akfnfqqtne delsfskgdv ihvtrveegg wwegtlngrt
      181 gwfpsnyvre vkasekpvsp ksgtlksppk gfdttainks yynvvlqnil eteneyskel
      241 qtvlstylrp lqtseklssa nisylmgnle eicsfqqmlv qsleectklp eaqqrvggcf
      301 lnlmpqmktl yltycanhps avnvltehse elgefmetkg asspgilvlt tglskpfmrl
      361 dkyptllkel erhmedyhtd rqdiqksmaa fknlsaqcqe vrkrkelelq ilteairnwe
      421 gddiktlgnv tymsqvliqc agseeknery lllfpnvllm lsasprmsgf iyqgklpttg
      481 mtitkledse nhrnafeisg smierilvsc nnqqdlqewv ehlqkqtkvt svgnptikph
      541 svpshtlpsh pvtpsskhad skpapltpay htlphpshhg tphttinwgp leppktpkpw
      601 slsclrpapp lrpsaalcyk edlskspktm kkllpkrkpe rkpsdeefas rkstaaleed
      661 aqilkvieay ctsaktrqtl nstwqgtdlm hnhvladddq psldslgrrs slsrlepsdl
      721 sedsdydsiw tahsyrmgst srksccsyis hqn
//
LOCUS       NP_001166879            1025 aa            linear   PRI 20-NOV-2025
DEFINITION  obscurin-like protein 1 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001166879
VERSION     NP_001166879.1
DBSOURCE    REFSEQ: accession NM_001173408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Tuysuz,B., Alp Unkar,Z., Turan,H., Gezdirici,A., Uludag Alkaya,D.,
            Kasap,B., Yesil,G., Vural,M. and Ercan,O.
  TITLE     Natural history of facial and skeletal features from neonatal
            period to adulthood in a 3M syndrome cohort with biallelic CUL7 or
            OBSL1 variants
  JOURNAL   Eur J Med Genet 64 (12), 104346 (2021)
   PUBMED   34597859
  REMARK    GeneRIF: Natural history of facial and skeletal features from
            neonatal period to adulthood in a 3M syndrome cohort with biallelic
            CUL7 or OBSL1 variants.
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Isik,E., Arican,D., Atik,T., Ooi,J.E., Darcan,S., Ozen,S., Simsek
            Kiper,P.O., Utine,E., Cogulu,O. and Ozkinay,F.
  TITLE     A rare cause of syndromic short stature: 3M syndrome in three
            families
  JOURNAL   Am J Med Genet A 185 (2), 461-468 (2021)
   PUBMED   33258289
  REMARK    GeneRIF: A rare cause of syndromic short stature: 3M syndrome in
            three families.
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Jacob,P. and Girisha,K.M.
  TITLE     Three M syndrome 2 in two Indian patients
  JOURNAL   Am J Med Genet A 185 (2), 614-616 (2021)
   PUBMED   33135300
  REMARK    GeneRIF: Three M syndrome 2 in two Indian patients.
REFERENCE   4  (residues 1 to 1025)
  AUTHORS   Wang,P., Yan,F., Li,Z., Yu,Y., Parnell,S.E. and Xiong,Y.
  TITLE     Impaired plasma membrane localization of ubiquitin ligase complex
            underlies 3-M syndrome development
  JOURNAL   J Clin Invest 129 (10), 4393-4407 (2019)
   PUBMED   31343991
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1025)
  AUTHORS   Simsek-Kiper,P.O., Taskiran,E., Kosukcu,C., Arslan,U.E.,
            Cormier-Daire,V., Gonc,N., Ozon,A., Alikasifoglu,A., Kandemir,N.,
            Utine,G.E., Alanay,Y., Alikasifoglu,M. and Boduroglu,K.
  TITLE     Further expanding the mutational spectrum and investigation of
            genotype-phenotype correlation in 3M syndrome
  JOURNAL   Am J Med Genet A 179 (7), 1157-1172 (2019)
   PUBMED   30980518
  REMARK    GeneRIF: The mutational spectrum of CUL7, OBSL1, and investigation
            of genotype-phenotype correlation in 3M syndrome has been reported.
REFERENCE   6  (residues 1 to 1025)
  AUTHORS   Hanson,D., Murray,P.G., Sud,A., Temtamy,S.A., Aglan,M.,
            Superti-Furga,A., Holder,S.E., Urquhart,J., Hilton,E., Manson,F.D.,
            Scambler,P., Black,G.C. and Clayton,P.E.
  TITLE     The primordial growth disorder 3-M syndrome connects ubiquitination
            to the cytoskeletal adaptor OBSL1
  JOURNAL   Am J Hum Genet 84 (6), 801-806 (2009)
   PUBMED   19481195
  REMARK    GeneRIF: Loss of OBSL1 leads to downregulation of CUL7 and results
            in primordial growth disorder 3-M syndrome.
REFERENCE   7  (residues 1 to 1025)
  AUTHORS   Fukuzawa,A., Lange,S., Holt,M., Vihola,A., Carmignac,V.,
            Ferreiro,A., Udd,B. and Gautel,M.
  TITLE     Interactions with titin and myomesin target obscurin and
            obscurin-like 1 to the M-band: implications for hereditary
            myopathies
  JOURNAL   J Cell Sci 121 (11), 1841-1851 (2008)
   PUBMED   18477606
  REMARK    GeneRIF: N-terminal Ig-domains of Obsl1 and Obscurin (Obsc) bind to
            titin-M10 and myomesin. Titin mutations, linked to limb-girdle
            muscular dystrophy 2J (LGMD2J) or Salih myopathy, weaken or
            abrogate titin-Obsc and titin-Obsl1 binding.
REFERENCE   8  (residues 1 to 1025)
  AUTHORS   Geisler,S.B., Robinson,D., Hauringa,M., Raeker,M.O., Borisov,A.B.,
            Westfall,M.V. and Russell,M.W.
  TITLE     Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to
            obscurin
  JOURNAL   Genomics 89 (4), 521-531 (2007)
   PUBMED   17289344
  REMARK    GeneRIF: report the cloning and characterization of OBSL1; OBSL1 is
            located on human chromosome 2q35 within 100 kb of SPEG, another
            gene related to obscurin
REFERENCE   9  (residues 1 to 1025)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   10 (residues 1 to 1025)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB475523.1, CK904385.1,
            EF063638.1 and AF035292.1.
            
            Summary: Cytoskeletal adaptor proteins function in linking the
            internal cytoskeleton of cells to the cell membrane. This gene
            encodes a cytoskeletal adaptor protein, which is a member of the
            Unc-89/obscurin family. The protein contains multiple N- and
            C-terminal immunoglobulin (Ig)-like domains and a central
            fibronectin type 3 domain. Mutations in this gene cause 3M syndrome
            type 2. Alternatively spliced transcript variants encoding
            different isoforms have been found in this gene. [provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (3) lacks multiple 3' exons but
            has an alternate 3' exon, as compared to variant 1. The resulting
            isoform (3, also known as isoform B) is much shorter and has a
            different C-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007201.1, SRR7346977.856104.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..1025
                     /product="obscurin-like protein 1 isoform 3 precursor"
                     /EC_number="2.7.11.18"
                     /note="obscurin-like protein 1; obscurin like 1"
                     /calculated_mol_wt=110244
     sig_peptide     1..29
                     /calculated_mol_wt=3048
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75147.4)"
     Region          12..88
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          17..19
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          29..33
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     mat_peptide     30..1025
                     /product="obscurin-like protein 1 isoform 3"
                     /calculated_mol_wt=110244
     Region          42..46
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..86
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          85..94
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          106..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          134..226
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          145..149
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          158..162
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          182..196
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          206..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          257..336
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          263..267
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..280
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          302..306
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          316..321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          329..332
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..426
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          358..362
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          371..374
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          395..399
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          409..414
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          432..510
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          446..450
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          458..462
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          480..484
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          494..499
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          503..506
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          518..602
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(518,584,599)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          736..801
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          746..750
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          771..775
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          785..790
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          794..797
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          827..892
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          837..841
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          862..866
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          876..881
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          885..888
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          918..983
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          928..932
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          953..957
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          967..972
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          976..979
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1025
                     /gene="OBSL1"
                     /coded_by="NM_001173408.2:308..3385"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS54433.1"
                     /db_xref="GeneID:23363"
                     /db_xref="HGNC:HGNC:29092"
                     /db_xref="MIM:610991"
ORIGIN      
        1 mkassgdqgs ppcflrfprp vrvvsgaeae lkcvvlgepp pvvvwekggq qlaaserlsf
       61 padgaehgll ltaalptdag vyvcrarnaa geayaaaavt vleppasdpe lqpaerplps
      121 pgsgegapvf ltgprsqwvl rgaevvltcr agglpeptly wekdgmalde vwdsshfalq
      181 pgraedgpga slalrilaar lpdsgvyvch arnahghaqa gallqvhqpp esppadpdea
      241 papvveplkc apktfwvneg khakfrcyvm gkpepeiewh wegrpllpdr rrlmyrdrdg
      301 gfvlkvlycq akdrglyvca arnsagqtls avqlhvkepr lrftrplqdv egrehgiavl
      361 eckvpnsrip tawfredqrl lpcrkyeqie egtvrrliih rlkadddgiy lcemrgrvrt
      421 vanvtvkgpi lkrlprkldv legenavllv etleagvegr wsrdgeelpv icqsssghmh
      481 alvlpgvtre dagevtfslg nsrtttllrv kcvkhsppgp pilaemfkgh kntvlltwkp
      541 pepapetpfi yrlerqevgs edwiqcfsie kagavevpgd cvpsegdyrf rictvsghgr
      601 sphvvfhgsa hlvptarlva gledvqvydg edavfsldls tiiqgtwfln geelksnepe
      661 gqvepgalry rieqkglqhr lilhavkhqd sgalvgfscp gvqdsaalti qespvhilsp
      721 qdrvsltftt servvltcel srvdfpatwy kdgqkveese llvvkmdgrk hrlilpeakv
      781 qdsgefecrt egvsaffgvt vqdppvhivd prehvfvhai tsecvmlace vdredapvrw
      841 ykdgqevees dfvvlenegp hrrlvlpatq psdggefqcv agdecayftv titdvsswiv
      901 ypsgkvyvaa vrlervvltc elcrpwaevr wtkdgeevve spalllqked tvrrlvlpav
      961 qledsgeylc eiddesasft vtvtesyqsq dssnnnpelc vllkkpktrr lwsrfppwrr
     1021 tagte
//
LOCUS       NP_001290071             783 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase PDZRN3 isoform 5 [Homo sapiens].
ACCESSION   NP_001290071
VERSION     NP_001290071.1
DBSOURCE    REFSEQ: accession NM_001303142.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Jiao,B., Zhang,H., Jiang,H., Liu,S., Wang,Y., Chen,Y., Duan,H.,
            Niu,Y., Shen,M., Wang,H. and Dai,Y.
  TITLE     Granulysin-mediated reduction of PDZRN3 induces Cx43 gap junctions
            activity exacerbating skin damage in trichloroethylene
            hypersensitivity syndrome
  JOURNAL   Ecotoxicol Environ Saf 274, 116174 (2024)
   PUBMED   38471344
  REMARK    GeneRIF: Granulysin-mediated reduction of PDZRN3 induces Cx43 gap
            junctions activity exacerbating skin damage in trichloroethylene
            hypersensitivity syndrome.
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Otsuka,Y., Furihata,T., Nakagawa,K., Ohno,Y., Reien,Y., Ouchi,M.,
            Wakashin,H., Tsuruoka,S. and Anzai,N.
  TITLE     Sodium-coupled monocarboxylate transporter 1 interacts with the
            RING finger- and PDZ domain-containing protein PDZRN3
  JOURNAL   J Physiol Sci 69 (4), 635-642 (2019)
   PUBMED   31098988
  REMARK    GeneRIF: PDZRN3 may regulate SMCT1 function by interfering with the
            interaction between SMCT1 and PDZK1.
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Thomas,M. and Banks,L.
  TITLE     PDZRN3/LNX3 is a novel target of human papillomavirus type 16
            (HPV-16) and HPV-18 E6
  JOURNAL   J Virol 89 (2), 1439-1444 (2015)
   PUBMED   25355882
  REMARK    GeneRIF: Authors show that HPV-16 and HPV-18 E6 can target PDZRN3
            in a PDZ- and proteasome-dependent manner and provide a connection
            between the papillomavirus life cycle and differentiation-related
            STAT signaling.
REFERENCE   5  (residues 1 to 783)
  AUTHORS   Sewduth,R.N., Jaspard-Vinassa,B., Peghaire,C., Guillabert,A.,
            Franzl,N., Larrieu-Lahargue,F., Moreau,C., Fruttiger,M.,
            Dufourcq,P., Couffinhal,T. and Duplaa,C.
  TITLE     The ubiquitin ligase PDZRN3 is required for vascular morphogenesis
            through Wnt/planar cell polarity signalling
  JOURNAL   Nat Commun 5, 4832 (2014)
   PUBMED   25198863
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 783)
  AUTHORS   Murea,M., Lu,L., Ma,L., Hicks,P.J., Divers,J., McDonough,C.W.,
            Langefeld,C.D., Bowden,D.W. and Freedman,B.I.
  TITLE     Genome-wide association scan for survival on dialysis in
            African-Americans with type 2 diabetes
  JOURNAL   Am J Nephrol 33 (6), 502-509 (2011)
   PUBMED   21546767
REFERENCE   7  (residues 1 to 783)
  AUTHORS   Honda,T., Yamamoto,H., Ishii,A. and Inui,M.
  TITLE     PDZRN3 negatively regulates BMP-2-induced osteoblast
            differentiation through inhibition of Wnt signaling
  JOURNAL   Mol Biol Cell 21 (18), 3269-3277 (2010)
   PUBMED   20668165
  REMARK    GeneRIF: These results indicate that PDZRN3 plays an important role
            in negative feedback control of BMP-2-induced osteoblast
            differentiation in C2C12 cells through inhibition of
            Wnt3a-beta-catenin signaling.
REFERENCE   8  (residues 1 to 783)
  AUTHORS   Ko,J.A., Kimura,Y., Matsuura,K., Yamamoto,H., Gondo,T. and Inui,M.
  TITLE     PDZRN3 (LNX3, SEMCAP3) is required for the differentiation of C2C12
            myoblasts into myotubes
  JOURNAL   J Cell Sci 119 (Pt 24), 5106-5113 (2006)
   PUBMED   17118964
REFERENCE   9  (residues 1 to 783)
  AUTHORS   Meyer,G., Varoqueaux,F., Neeb,A., Oschlies,M. and Brose,N.
  TITLE     The complexity of PDZ domain-mediated interactions at glutamatergic
            synapses: a case study on neuroligin
  JOURNAL   Neuropharmacology 47 (5), 724-733 (2004)
   PUBMED   15458844
REFERENCE   10 (residues 1 to 783)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of PDZRN3 and PDZRN4 genes in
            silico
  JOURNAL   Int J Mol Med 13 (4), 607-613 (2004)
   PUBMED   15010864
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC370885.1, AK299560.1,
            AB029018.1 and AW661852.1.
            
            Summary: This gene encodes a member of the LNX (Ligand of Numb
            Protein-X) family of RING-type ubiquitin E3 ligases. This protein
            may function in vascular morphogenesis and the differentiation of
            adipocytes, osteoblasts and myoblasts. This protein may be targeted
            for degradation by the human papilloma virus E6 protein.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (5) lacks several exons and uses
            an alternate 5' terminal exon, compared to variant 1. These
            differences result in a distinct 5' UTR and cause translation
            initiation at an alternate downstream start codon, compared to
            variant 1. The resulting protein (isoform 5) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.259393.1,
                                           SRR7410570.221011.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p13"
     Protein         1..783
                     /product="E3 ubiquitin-protein ligase PDZRN3 isoform 5"
                     /EC_number="2.3.2.27"
                     /note="likely ortholog of mouse semaF cytoplasmic domain
                     associated protein 3; E3 ubiquitin-protein ligase PDZRN3;
                     ligand of Numb protein X 3; semaphorin cytoplasmic
                     domain-associated protein 3; RING-type E3 ubiquitin
                     transferase PDZRN3"
                     /calculated_mol_wt=89014
     Region          <23..54
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          137..220
                     /region_name="PDZ2-PDZRN4-like"
                     /note="PDZ domain 2 of PDZ domain-containing RING finger
                     protein 4 (PDZRN4), PDZRN3-B, and related domains;
                     cd06716"
                     /db_xref="CDD:467200"
     Site            order(147..153,167,170,198,202,205..206)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467200"
     CDS             1..783
                     /gene="PDZRN3"
                     /gene_synonym="LNX3; SEMACAP3; SEMCAP3"
                     /coded_by="NM_001303142.2:289..2640"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS77771.1"
                     /db_xref="GeneID:23024"
                     /db_xref="HGNC:HGNC:17704"
                     /db_xref="MIM:609729"
ORIGIN      
        1 mgcslcslqk qeeqykllye vcqvngrdls rathdqavea fktakepivv qvlrrtprtk
       61 mftppsesql vdtgtqtdit fehimaltkm sspsppvldp yllpeehpsa heyydpndyi
      121 gdihqemdre eleleevdly rmnsqdklgl tvcyrtdded digiyiseid pnsiaakdgr
      181 iregdriiqi ngievqnree avalltseen knfslliarp elqldegwmd ddrndflddl
      241 hmdmleeqhh qamqftasvl qqkkhdedgg ttdtatilsn qhekdsgvgr tdestrndes
      301 seqenngdda tassnplagq rkltcsqdtl gsgdlpfsne sfisadctda dylgipvdec
      361 erfrellelk cqvksatpyg lyypsgplda gksdpesvdk elellneelr sieleclsiv
      421 rahkmqqlke qyreswmlhn sgfrnyntsi dvrrhelsdi telpeksdkd sssayntges
      481 crstpltlei spdnslrraa egiscpsseg avgtteaygp asknllsite dpevgtptys
      541 pslkeldpnq pleskerras dgsrsptpsq klgsaylpsy hhspykhahi pahaqhyqsy
      601 mqliqqksav eyaqsqmslv smckdlsspt pseprmewkv kirsdgtryi tkrpvrdrll
      661 reralkiree rsgmttddda vsemkmgryw skeerkqhlv kakeqrrrre fmmqsrldcl
      721 keqqaaddrk emnilelshk kmmkkrnkki fdnwmtiqel lthgtkspdg trvynsflsv
      781 ttv
//
LOCUS       NP_859050                667 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A
            beta isoform isoform b [Homo sapiens].
ACCESSION   NP_859050
VERSION     NP_859050.1
DBSOURCE    REFSEQ: accession NM_181699.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Peng,S., He,T., Liu,Y., Zheng,L., Zhong,Y., Niu,Z., Zhang,M. and
            Yang,S.
  TITLE     Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B by
            Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs
  JOURNAL   Stem Cell Rev Rep 19 (6), 1981-1993 (2023)
   PUBMED   37243830
  REMARK    GeneRIF: Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B
            by Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs.
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Du,M., Yuan,L., Zhang,Z., Zhang,C., Zhu,M., Zhang,Z., Li,R.,
            Zhao,X., Liang,H., Li,Y., Jiang,H., Qiao,J. and Yin,Y.
  TITLE     PPP2R1B is modulated by ubiquitination and is essential for
            spermatogenesis
  JOURNAL   FASEB J 35 (5), e21564 (2021)
   PUBMED   33913576
  REMARK    GeneRIF: PPP2R1B is modulated by ubiquitination and is essential
            for spermatogenesis.
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Adler,H.T., Nallaseth,F.S., Walter,G. and Tkachuk,D.C.
  TITLE     HRX leukemic fusion proteins form a heterocomplex with the
            leukemia-associated protein SET and protein phosphatase 2A
  JOURNAL   J Biol Chem 272 (45), 28407-28414 (1997)
   PUBMED   9353299
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Hendrix,P., Mayer-Jackel,R.E., Cron,P., Goris,J., Hofsteenge,J.,
            Merlevede,W. and Hemmings,B.A.
  TITLE     Structure and expression of a 72-kDa regulatory subunit of protein
            phosphatase 2A. Evidence for different size forms produced by
            alternative splicing
  JOURNAL   J Biol Chem 268 (20), 15267-15276 (1993)
   PUBMED   8392071
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Kamibayashi,C., Lickteig,R.L., Estes,R., Walter,G. and Mumby,M.C.
  TITLE     Expression of the A subunit of protein phosphatase 2A and
            characterization of its interactions with the catalytic and
            regulatory subunits
  JOURNAL   J Biol Chem 267 (30), 21864-21872 (1992)
   PUBMED   1328247
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Hemmings,B.A., Adams-Pearson,C., Maurer,F., Muller,P., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Stone,S.R.
  TITLE     alpha- and beta-forms of the 65-kDa subunit of protein phosphatase
            2A have a similar 39 amino acid repeating structure
  JOURNAL   Biochemistry 29 (13), 3166-3173 (1990)
   PUBMED   2159327
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001781.5, AF087438.1,
            BC027596.2 and DB527885.1.
            
            Summary: This gene encodes a constant regulatory subunit of protein
            phosphatase 2. Protein phosphatase 2 is one of the four major
            Ser/Thr phosphatases, and it is implicated in the negative control
            of cell growth and division. It consists of a common heteromeric
            core enzyme, which is composed of a catalytic subunit and a
            constant regulatory subunit, that associates with a variety of
            regulatory subunits. The constant regulatory subunit A serves as a
            scaffolding molecule to coordinate the assembly of the catalytic
            subunit and a variable regulatory B subunit. This gene encodes a
            beta isoform of the constant regulatory subunit A. Mutations in
            this gene have been associated with some lung and colon cancers.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Apr 2010].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and the
            3' coding region, compared to variant 1. The resulting isoform (b)
            contains a longer and distinct C-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.409813.1,
                                           SRR1803612.163235.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..667
                     /product="serine/threonine-protein phosphatase 2A 65 kDa
                     regulatory subunit A beta isoform isoform b"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, structural/regulatory
                     subunit A, beta; protein phosphatase 2, regulatory subunit
                     A, beta"
                     /calculated_mol_wt=73454
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P30154.3)"
     Region          20..58
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          25..49
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(41..42,45,48..49,79..80,83,86..87,90,118..119,122,
                     125..126,129,157..158,161,164..165,195..196,199,202..203)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          59..96
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          63..90
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          97..135
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          100..130
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          102..239
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          136..173
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          139..165
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          174..212
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          175..204
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          193..364
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          213..251
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          216..246
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          252..290
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          257..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(273..274,277,280..281,312..313,316,319..320,323,
                     355..356,359,362..363,366,394..395,398,401..402,433..434,
                     437,440..441)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          291..333
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          295..323
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          334..372
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          337..367
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          373..411
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          376..402
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          378..478
                     /region_name="HEAT_2"
                     /note="HEAT repeats; pfam13646"
                     /db_xref="CDD:433376"
     Region          412..450
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          413..442
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          451..489
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          454..480
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          490..528
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          491..520
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          529..567
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (P30154.3)"
     Region          530..556
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          571..597
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..667
                     /gene="PPP2R1B"
                     /gene_synonym="PP2A-Abeta; PR65B"
                     /coded_by="NM_181699.3:29..2032"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8348.1"
                     /db_xref="GeneID:5519"
                     /db_xref="HGNC:HGNC:9303"
                     /db_xref="MIM:603113"
ORIGIN      
        1 magaselgtg pgaaggdgdd slypiavlid elrnedvqlr lnsikklsti alalgvertr
       61 sellpfltdt iydedevlla laeqlgnftg lvggpdfahc llpplenlat veetvvrdka
      121 veslrqisqe htpvaleayf vplvkrlasg dwftsrtsac glfsvcypra snavkaeirq
      181 qfrslcsddt pmvrraaask lgefakvlel dsvkseivpl ftslasdeqd svrllaveac
      241 vsiaqllsqd dletlvmptl rqaaedkswr vrymvadrfs elqkamgpki tlndlipafq
      301 nllkdceaev raaaahkvke lgenlpiedr etiimnqilp yikelvsdtn qhvksalasv
      361 imglstilgk entiehllpl flaqlkdecp dvrlniisnl dcvnevigir qlsqsllpai
      421 velaedakwr vrlaiieymp llagqlgvef fdeklnslcm awlvdhvyai reaatnnlmk
      481 lvqkfgtewa qntivpkvlv mandpnylhr mttlfcinal seacgqeitt kqmlpivlkm
      541 agdqvanvrf nvakslqkig pildtnalqg evkpvlqklg qdedmdvkyf aqeaisvvaq
      601 rlrklefpvk dsgepsvpra dknhfprptv pgedmgkgpv yqlrgdtrdt laqlgiaelv
      661 hfsqstd
//
LOCUS       NP_958846                258 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 5 [Homo sapiens].
ACCESSION   NP_958846
VERSION     NP_958846.1
DBSOURCE    REFSEQ: accession NM_201438.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK129910.1, BC039832.1 and
            AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (5) has multiple differences
            compared to variant 1. The resulting isoform (5) has distinct N-
            and C-termini, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040449.1, BI906155.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..258
                     /product="periphilin-1 isoform 5"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=29653
     Region          237..>256
                     /region_name="Lge1_periphilin-like"
                     /note="Eukaryotic transcriptional regulatory protein Lge1,
                     periphilin, and similar proteins; cl13008"
                     /db_xref="CDD:448781"
     CDS             1..258
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_201438.2:106..882"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mayrrdemws egryeyerip rerapprshp sdesgyrwtr ddhsasrqpe yrdmrdgfrr
       61 ksfysshyar erspykrdnt ffrespvgrk dsphsrsgss vssrsysper sksysfhqsq
      121 hrksvrpgas ykrqnegnpe rdkerpvqsl ktsrdtspss gsavssskvl dkpsrlteke
      181 laeaaskwaa ekleksdesn lpeiseyeag staplftdqp eepesntthg ielfedsqlt
      241 trskaiaskt keieqvrv
//
LOCUS       NP_057502                590 aa            linear   PRI 20-NOV-2025
DEFINITION  merlin isoform 2 [Homo sapiens].
ACCESSION   NP_057502
VERSION     NP_057502.2
DBSOURCE    REFSEQ: accession NM_016418.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Bian,Z., Xu,C., Wang,X., Zhang,B., Xiao,Y., Liu,L., Zhao,S.,
            Huang,N., Yang,F., Zhang,Y., Xue,S., Wang,X., Pan,Q. and Sun,F.
  TITLE     TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates Metabolic and
            Immune Advantages in Hepatocellular Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2402578 (2024)
   PUBMED   39005234
  REMARK    GeneRIF: TRIM65/NF2/YAP1 Signaling Coordinately Orchestrates
            Metabolic and Immune Advantages in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Vlashi,R., Sun,F., Zheng,C., Zhang,X., Liu,J. and Chen,G.
  TITLE     The molecular biology of NF2/Merlin on tumorigenesis and
            development
  JOURNAL   FASEB J 38 (13), e23809 (2024)
   PUBMED   38967126
  REMARK    GeneRIF: The molecular biology of NF2/Merlin on tumorigenesis and
            development.
            Review article
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Lei,Z., Niu,J., Cai,H., Kong,Z., Ding,X., Dong,Y., Zhang,D., Li,X.,
            Shao,J., Lin,A., Zhou,R., Yang,S. and Yan,Q.
  TITLE     NF2 regulates IP3R-mediated Ca2+ signal and apoptosis in
            meningiomas
  JOURNAL   FASEB J 38 (13), e23737 (2024)
   PUBMED   38953724
  REMARK    GeneRIF: NF2 regulates IP3R-mediated Ca[2+] signal and apoptosis in
            meningiomas.
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Chen,Y., Steiner,S., Hagedorn,C., Kollar,S., Pliego-Mendieta,A.,
            Haberecker,M., Plock,J., Britschgi,C., Planas-Paz,L. and Pauli,C.
  TITLE     Acquired NF2 mutation confers resistance to TRK inhibition in an ex
            vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell model
  JOURNAL   J Pathol 263 (2), 257-269 (2024)
   PUBMED   38613194
  REMARK    GeneRIF: Acquired NF2 mutation confers resistance to TRK inhibition
            in an ex vivo LMNA::NTRK1-rearranged soft-tissue sarcoma cell
            model.
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Ma,W., Zhang,J., Chen,W., Liu,N. and Wu,T.
  TITLE     The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 117 (2024)
   PUBMED   38641672
  REMARK    GeneRIF: The histone lysine acetyltransferase KAT2B inhibits
            cholangiocarcinoma growth: evidence for interaction with SP1 to
            regulate NF2-YAP signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 590)
  AUTHORS   den Bakker,M.A., Tascilar,M., Riegman,P.H., Hekman,A.C.,
            Boersma,W., Janssen,P.J., de Jong,T.A., Hendriks,W., van der
            Kwast,T.H. and Zwarthoff,E.C.
  TITLE     Neurofibromatosis type 2 protein co-localizes with elements of the
            cytoskeleton
  JOURNAL   Am J Pathol 147 (5), 1339-1349 (1995)
   PUBMED   7485397
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Evans,D.G., Bourn,D., Wallace,A., Ramsden,R.T., Mitchell,J.D. and
            Strachan,T.
  TITLE     Diagnostic issues in a family with late onset type 2
            neurofibromatosis
  JOURNAL   J Med Genet 32 (6), 470-474 (1995)
   PUBMED   7666400
REFERENCE   8  (residues 1 to 590)
  AUTHORS   Honda,M., Arai,E., Sawada,S., Ohta,A. and Niimura,M.
  TITLE     Neurofibromatosis 2 and neurilemmomatosis gene are identical
  JOURNAL   J Invest Dermatol 104 (1), 74-77 (1995)
   PUBMED   7798645
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Evans,D.G.
  TITLE     NF2-Related Schwannomatosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301380
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Arai,E., Ikeuchi,T., Karasawa,S., Tamura,A., Yamamoto,K., Kida,M.,
            Ichimura,K., Yuasa,Y. and Tonomura,A.
  TITLE     Constitutional translocation t(4;22) (q12;q12.2) associated with
            neurofibromatosis type 2
  JOURNAL   Am J Med Genet 44 (2), 163-167 (1992)
   PUBMED   1456285
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN419318.1, AF369658.1,
            AC004882.3 and BC071653.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 4, 2003 this sequence version replaced NP_057502.1.
            
            Summary: This gene encodes a protein that is similar to some
            members of the ERM (ezrin, radixin, moesin) family of proteins that
            link cytoskeletal components with proteins in the cell membrane.
            The encoded protein is involved in regulation of contact-dependent
            inhibition of cell proliferation and functions in cell-cell
            adhesion and transmembrane signaling. The encoded protein has been
            shown to interact with cell-surface proteins, proteins involved in
            cytoskeletal dynamics, and proteins involved in regulating ion
            transport. Disruption of this protein's function has been
            implicated in tumorigenesis and metastasis. Mutations in this gene
            are associated with neurofibromatosis type II which is
            characterized by nervous system and skin tumors and ocular
            abnormalities. [provided by RefSeq, May 2022].
            
            Transcript Variant: This variant (2) includes an alternate exon,
            compared to variant 1, that causes a frameshift. The resulting
            protein (isoform 2), one of the two predominant isoforms, has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF369658.1, SRR1803613.168137.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..590
                     /product="merlin isoform 2"
                     /note="moesin-ezrin-radixin like; neurofibromin 2
                     (bilateral acoustic neuroma); schwannomin;
                     moesin-ezrin-radizin-like protein; schwannomerlin; merlin;
                     moesin-ezrin-radixin-like protein; neurofibromin-2;
                     bilateral acoustic neurofibromatosis"
                     /calculated_mol_wt=68959
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     Region          23..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..312
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(258..259,261..267,276,297,300..301,304)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(258,261..268,276,297,300..301,304)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(294,298)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            297..312
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          307..>367
                     /region_name="PLN03086"
                     /note="PRLI-interacting factor K; Provisional"
                     /db_xref="CDD:178635"
     Region          346..465
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Region          518..>579
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PAK.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P35240.1)"
     CDS             1..590
                     /gene="NF2"
                     /gene_synonym="ACN; BANF; merlin-1; SCH; SWNV"
                     /coded_by="NM_016418.5:444..2216"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13862.1"
                     /db_xref="GeneID:4771"
                     /db_xref="HGNC:HGNC:7773"
                     /db_xref="MIM:607379"
ORIGIN      
        1 magaiasrms fsslkrkqpk tftvrivtmd aemefncemk wkgkdlfdlv crtlglretw
       61 ffglqytikd tvawlkmdkk vldhdvskee pvtfhflakf ypenaeeelv qeitqhlffl
      121 qvkkqildek iycppeasvl lasyavqaky gdydpsvhkr gflaqeellp krvinlyqmt
      181 pemweerita wyaehrgrar deaemeylki aqdlemygvn yfairnkkgt elllgvdalg
      241 lhiydpenrl tpkisfpwne irnisysdke ftikpldkki dvfkfnsskl rvnklilqlc
      301 ignhdlfmrr rkadslevqq mkaqareeka rkqmerqrla rekqmreeae rtrdelerrl
      361 lqmkeeatma nealmrseet adllaekaqi teeeakllaq kaaeaeqemq rikatairte
      421 eekrlmeqkv leaevlalkm aeeserrake adqlkqdlqe areaerrakq klleiatkpt
      481 yppmnpipap lppdipsfnl igdslsfdfk dtdmkrlsme iekekveyme kskhlqeqln
      541 elkteiealk lkeretaldi lhnensdrgg sskhntikkp qaqgrrpici
//
LOCUS       NP_060354                328 aa            linear   PRI 20-NOV-2025
DEFINITION  PIN2/TERF1-interacting telomerase inhibitor 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060354
VERSION     NP_060354.4
DBSOURCE    REFSEQ: accession NM_017884.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 328)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 328)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 328)
  AUTHORS   Yang,M., Chen,F., Yu,C., Cai,Z., Zhong,Q., Feng,J., Li,G., Shen,C.
            and Wen,Z.
  TITLE     PinX1-Promoted Autophagy Inhibits Cell Proliferation and Induces
            Cell Apoptosis by Inhibiting the NF-kappaB/p65 Signaling Pathway in
            Nasopharyngeal Carcinoma
  JOURNAL   Front Biosci (Landmark Ed) 28 (8), 170 (2023)
   PUBMED   37664923
  REMARK    GeneRIF: PinX1-Promoted Autophagy Inhibits Cell Proliferation and
            Induces Cell Apoptosis by Inhibiting the NF-kappaB/p65 Signaling
            Pathway in Nasopharyngeal Carcinoma.
REFERENCE   4  (residues 1 to 328)
  AUTHORS   Qi,Y.Y., Liu,X.R., He,Y.X., Zhou,M., Ning,X.H., Zhai,Y.L.,
            Zhang,X.X., Wang,X.Y., Zhao,Y.F., Cui,Y. and Zhao,Z.Z.
  TITLE     Association of the PINX1 Variant rs6984094, Which Lengthens
            Telomeres, with Systemic Lupus Erythematosus Susceptibility in
            Chinese Populations
  JOURNAL   J Immunol Res 2021, 7079359 (2021)
   PUBMED   34337078
  REMARK    GeneRIF: Association of the PINX1 Variant rs6984094, Which
            Lengthens Telomeres, with Systemic Lupus Erythematosus
            Susceptibility in Chinese Populations.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 328)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 328)
  AUTHORS   Liao,C., Zhao,M.J., Zhao,J., Song,H., Pineau,P., Marchio,A.,
            Dejean,A., Tiollais,P., Wang,H.Y. and Li,T.P.
  TITLE     Mutation analysis of novel human liver-related putative tumor
            suppressor gene in hepatocellular carcinoma
  JOURNAL   World J Gastroenterol 9 (1), 89-93 (2003)
   PUBMED   12508358
  REMARK    GeneRIF: Data show that liver-related putative tumor suppressor
            gene (LPTS) mutations occur in hepatocellular carcinoma but are
            infrequent and of little effect on the telomerase inhibitory
            function of the protein.
REFERENCE   7  (residues 1 to 328)
  AUTHORS   Liao,C., Zhao,M.J., Zhao,J., Jia,D., Song,H. and Li,Z.P.
  TITLE     Over-expression of LPTS-L in hepatocellular carcinoma cell line
            SMMC-7721 induces crisis
  JOURNAL   World J Gastroenterol 8 (6), 1050-1052 (2002)
   PUBMED   12439923
  REMARK    GeneRIF: Over-expression of LPTS-L can induce hepatoma cells into
            crisis due to the reduction of telomerase activity.
REFERENCE   8  (residues 1 to 328)
  AUTHORS   Guglielmi,B. and Werner,M.
  TITLE     The yeast homolog of human PinX1 is involved in rRNA and small
            nucleolar RNA maturation, not in telomere elongation inhibition
  JOURNAL   J Biol Chem 277 (38), 35712-35719 (2002)
   PUBMED   12107183
  REMARK    GeneRIF: role in rRNA and small nucleolar RNA maturation, not in
            telomere elongation inhibition
REFERENCE   9  (residues 1 to 328)
  AUTHORS   Zhou,X.Z. and Lu,K.P.
  TITLE     The Pin2/TRF1-interacting protein PinX1 is a potent telomerase
            inhibitor
  JOURNAL   Cell 107 (3), 347-359 (2001)
   PUBMED   11701125
REFERENCE   10 (residues 1 to 328)
  AUTHORS   Liao,C., Zhao,M., Song,H., Uchida,K., Yokoyama,K.K. and Li,T.
  TITLE     Identification of the gene for a novel liver-related putative tumor
            suppressor at a high-frequency loss of heterozygosity region of
            chromosome 8p23 in human hepatocellular carcinoma
  JOURNAL   Hepatology 32 (4 Pt 1), 721-727 (2000)
   PUBMED   11003615
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF418553.1 and AC105001.3.
            
            On Jun 10, 2007 this sequence version replaced NP_060354.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.524727.1, AJ344104.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314787.8/ ENSP00000318966.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..328
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..328
                     /product="PIN2/TERF1-interacting telomerase inhibitor 1
                     isoform 1"
                     /note="hepatocellular carcinoma-related putative tumor
                     suppressor; PIN2-interacting protein 1; pin2-interacting
                     protein X1; 67-11-3 protein; protein 67-11-3;
                     TRF1-interacting protein 1; liver-related putative tumor
                     suppressor"
                     /calculated_mol_wt=36904
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     Region          24..69
                     /region_name="G_patch"
                     /note="glycine rich nucleic binding domain; smart00443"
                     /db_xref="CDD:197727"
     Site            50..51
                     /site_type="other"
                     /note="(Microbial infection) Cleavage by enterovirus 71
                     protease 3C. /evidence=ECO:0000269|PubMed:27847364;
                     propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     Region          147..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     Region          189..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     Region          254..328
                     /region_name="Telomerase inhibitory domain (TID)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZX5; propagated from
                     UniProtKB/Swiss-Prot (Q96BK5.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZX5; propagated from
                     UniProtKB/Swiss-Prot (Q96BK5.2)"
     Region          287..297
                     /region_name="TBM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BK5.2)"
     CDS             1..328
                     /gene="PINX1"
                     /gene_synonym="Gno1; LPTL; LPTS; Pxr1"
                     /coded_by="NM_017884.6:120..1106"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47801.1"
                     /db_xref="GeneID:54984"
                     /db_xref="HGNC:HGNC:30046"
                     /db_xref="MIM:606505"
ORIGIN      
        1 msmlaerrrk qkwavdpqnt awsnddskfg qrmlekmgws kgkglgaqeq gatdhikvqv
       61 knnhlglgat innednwiah qddfnqllae lntchgqett dssdkkekks fsleekskis
      121 knrvhymkft kgkdlssrsk tdldcifgkr qskktpegda spstpeenet tttsaftiqe
      181 yfakrmaalk nkpqvpvpgs disetqverk rgkkrnkeat gkdvesylqp kakrhtegkp
      241 eraeaqerva kkksapaeeq lrgpcwdqss kasaqdagdh vqppegrdft lkpkkrrgkk
      301 klqkpveiae datleetlvk kkkkkdsk
//
LOCUS       NP_001357498             592 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4A isoform 4 [Homo sapiens].
ACCESSION   NP_001357498 XP_011508181
VERSION     NP_001357498.1
DBSOURCE    REFSEQ: accession NM_001370569.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_011508181.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.200780.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..592
                     /product="semaphorin-4A isoform 4"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=64679
     Region          <1..326
                     /region_name="Sema"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorins and plexins; cl15693"
                     /db_xref="CDD:472829"
     Region          327..371
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          397..469
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          407..411
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          419..423
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          438..442
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          452..457
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..592
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001370569.1:536..2314"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 megkgqspfd pahkhtavlv dgmlysgtmn nflgsepilm rtlgsqpvlk tdnflrwlhh
       61 dasfvaaips tqvvyfffee tasefdffer lhtsrvarvc kndvggekll qkkwttflka
      121 qllctqpgql pfnvirhavl lpadsptaph iyavftsqwq vggtrssavc afslldierv
      181 fkgkykelnk etsrwttyrg petnprpgsc svgpssdkal tfmkdhflmd eqvvgtpllv
      241 ksgveytrla vetaqgldgh shlvmylgtt tgslhkavvs gdssahlvee iqlfpdpepv
      301 rnlqlaptqg avfvgfsggv wrvprancsv yescvdcvla rdphcawdpe srtccllsap
      361 nlnswkqdme rgnpewacas gpmsrslrpq srpqiikevl avpnsilelp cphlsalasy
      421 ywshgpaavp easstvyngs lllivqdgvg glyqcwaten gfsypvisyw vdsqdqtlal
      481 dpelagipre hvkvpltrvs ggaalaaqqs ywphfvtvtv lfalvlsgal iilvasplra
      541 lrargkvqgc etlrpgekap lsreqhlqsp kecrtsasdv dadnnclgte va
//
LOCUS       NP_001231533             536 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydropyrimidinase-related protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001231533
VERSION     NP_001231533.1
DBSOURCE    REFSEQ: accession NM_001244604.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Li,S., Guo,Y., Takahashi,M., Suzuki,H., Kosaki,K. and Ohshima,T.
  TITLE     Forebrain commissure formation in zebrafish embryo requires the
            binding of KLC1 to CRMP2
  JOURNAL   Dev Neurobiol 84 (3), 203-216 (2024)
   PUBMED   38830696
  REMARK    GeneRIF: Forebrain commissure formation in zebrafish embryo
            requires the binding of KLC1 to CRMP2.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Kurita,H., Ueda,M., Kimura,M., Okuda,A., Ohuchi,K., Hozumi,I. and
            Inden,M.
  TITLE     Zinc Deficiency Decreases Neurite Extension via CRMP2 Signal
            Pathway
  JOURNAL   Biol Pharm Bull 47 (4), 796-800 (2024)
   PUBMED   38583951
  REMARK    GeneRIF: Zinc Deficiency Decreases Neurite Extension via CRMP2
            Signal Pathway.
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Feuer,K.L., Peng,X., Yovo,C.K. and Avramopoulos,D.
  TITLE     DPYSL2/CRMP2 isoform B knockout in human iPSC-derived glutamatergic
            neurons confirms its role in mTOR signaling and neurodevelopmental
            disorders
  JOURNAL   Mol Psychiatry 28 (10), 4353-4362 (2023)
   PUBMED   37479784
  REMARK    GeneRIF: DPYSL2/CRMP2 isoform B knockout in human iPSC-derived
            glutamatergic neurons confirms its role in mTOR signaling and
            neurodevelopmental disorders.
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Soutar,M.P., Thornhill,P., Cole,A.R. and Sutherland,C.
  TITLE     Increased CRMP2 phosphorylation is observed in Alzheimer's disease;
            does this tell us anything about disease development?
  JOURNAL   Curr Alzheimer Res 6 (3), 269-278 (2009)
   PUBMED   19519308
  REMARK    Review article
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Gu,Y. and Ihara,Y.
  TITLE     Evidence that collapsin response mediator protein-2 is involved in
            the dynamics of microtubules
  JOURNAL   J Biol Chem 275 (24), 17917-17920 (2000)
   PUBMED   10770920
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Gu,Y., Hamajima,N. and Ihara,Y.
  TITLE     Neurofibrillary tangle-associated collapsin response mediator
            protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518,
            and Ser-522
  JOURNAL   Biochemistry 39 (15), 4267-4275 (2000)
   PUBMED   10757975
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Kitamura,K., Takayama,M., Hamajima,N., Nakanishi,M., Sasaki,M.,
            Endo,Y., Takemoto,T., Kimura,H., Iwaki,M. and Nonaka,M.
  TITLE     Characterization of the human dihydropyrimidinase-related protein 2
            (DRP-2) gene
  JOURNAL   DNA Res 6 (5), 291-297 (1999)
   PUBMED   10574455
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Hamajima,N., Matsuda,K., Sakata,S., Tamaki,N., Sasaki,M. and
            Nonaka,M.
  TITLE     A novel gene family defined by human dihydropyrimidinase and three
            related proteins with differential tissue distribution
  JOURNAL   Gene 180 (1-2), 157-163 (1996)
   PUBMED   8973361
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Goshima,Y., Nakamura,F., Strittmatter,P. and Strittmatter,S.M.
  TITLE     Collapsin-induced growth cone collapse mediated by an intracellular
            protein related to UNC-33
  JOURNAL   Nature 376 (6540), 509-514 (1995)
   PUBMED   7637782
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP222303.1, AK299077.1,
            BX463316.2, AC015564.13 and BC056408.1.
            
            Summary: This gene encodes a member of the collapsin response
            mediator protein family. Collapsin response mediator proteins form
            homo- and hetero-tetramers and facilitate neuron guidance, growth
            and polarity. The encoded protein promotes microtubule assembly and
            is required for Sema3A-mediated growth cone collapse, and also
            plays a role in synaptic signaling through interactions with
            calcium channels. This gene has been implicated in multiple
            neurological disorders, and hyperphosphorylation of the encoded
            protein may play a key role in the development of Alzheimer's
            disease. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (3) has a shorter N-terminus, compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.133392.1,
                                           SRR1803613.66143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..536
                     /product="dihydropyrimidinase-related protein 2 isoform 3"
                     /note="dihydropyrimidinase-related protein 2; collapsin
                     response mediator protein hCRMP-2; unc-33-like
                     phosphoprotein 2"
                     /calculated_mol_wt=58032
     Region          1..430
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(8..9,144,165,168,171,194,198,202,205,232..233,
                     235..236,354,359,364)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(37,39,129,162,218,296)
                     /site_type="active"
                     /db_xref="CDD:238639"
     CDS             1..536
                     /gene="DPYSL2"
                     /gene_synonym="CRMP-2; CRMP2; DHPRP2; DRP-2; DRP2; N2A3;
                     ULIP-2; ULIP2"
                     /coded_by="NM_001244604.2:199..1809"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS59096.1"
                     /db_xref="GeneID:1808"
                     /db_xref="HGNC:HGNC:3014"
                     /db_xref="MIM:602463"
ORIGIN      
        1 medglikqig enlivpggvk tieahsrmvi pggidvhtrf qmpdqgmtsa ddffqgtkaa
       61 laggttmiid hvvpepgtsl laafdqwrew adsksccdys lhvdisewhk giqeemealv
      121 kdhgvnsflv ymafkdrfql tdcqiyevls virdigaiaq vhaengdiia eeqqrildlg
      181 itgpeghvls rpeeveaeav nraitianqt ncplyitkvm skssaeviaq arkkgtvvyg
      241 epitaslgtd gshywsknwa kaaafvtspp lspdpttpdf lnsllscgdl qvtgsahctf
      301 ntaqkavgkd nftlipegtn gteermsviw dkavvtgkmd enqfvavtst naakvfnlyp
      361 rkgriavgsd adlviwdpds vktisakthn ssleynifeg mecrgsplvv isqgkivled
      421 gtlhvtegsg ryiprkpfpd fvykrikars rlaelrgvpr glydgpvcev svtpktvtpa
      481 ssaktspakq qappvrnlhq sgfslsgaqi ddniprrttq rivappggra nitslg
//
LOCUS       NP_036265                871 aa            linear   PRI 20-NOV-2025
DEFINITION  coatomer subunit gamma-2 isoform 1 [Homo sapiens].
ACCESSION   NP_036265 XP_351747
VERSION     NP_036265.3
DBSOURCE    REFSEQ: accession NM_012133.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Amano,G., Matsuzaki,S., Mori,Y., Miyoshi,K., Han,S., Shikada,S.,
            Takamura,H., Yoshimura,T. and Katayama,T.
  TITLE     SCYL1 arginine methylation by PRMT1 is essential for neurite
            outgrowth via Golgi morphogenesis
  JOURNAL   Mol Biol Cell 31 (18), 1963-1973 (2020)
   PUBMED   32583741
  REMARK    GeneRIF: SCYL1 arginine methylation by PRMT1 is essential for
            neurite outgrowth via Golgi morphogenesis.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Wolpin,B.M., Rizzato,C., Kraft,P., Kooperberg,C., Petersen,G.M.,
            Wang,Z., Arslan,A.A., Beane-Freeman,L., Bracci,P.M., Buring,J.,
            Canzian,F., Duell,E.J., Gallinger,S., Giles,G.G., Goodman,G.E.,
            Goodman,P.J., Jacobs,E.J., Kamineni,A., Klein,A.P., Kolonel,L.N.,
            Kulke,M.H., Li,D., Malats,N., Olson,S.H., Risch,H.A., Sesso,H.D.,
            Visvanathan,K., White,E., Zheng,W., Abnet,C.C., Albanes,D.,
            Andreotti,G., Austin,M.A., Barfield,R., Basso,D., Berndt,S.I.,
            Boutron-Ruault,M.C., Brotzman,M., Buchler,M.W.,
            Bueno-de-Mesquita,H.B., Bugert,P., Burdette,L., Campa,D.,
            Caporaso,N.E., Capurso,G., Chung,C., Cotterchio,M., Costello,E.,
            Elena,J., Funel,N., Gaziano,J.M., Giese,N.A., Giovannucci,E.L.,
            Goggins,M., Gorman,M.J., Gross,M., Haiman,C.A., Hassan,M.,
            Helzlsouer,K.J., Henderson,B.E., Holly,E.A., Hu,N., Hunter,D.J.,
            Innocenti,F., Jenab,M., Kaaks,R., Key,T.J., Khaw,K.T., Klein,E.A.,
            Kogevinas,M., Krogh,V., Kupcinskas,J., Kurtz,R.C., LaCroix,A.,
            Landi,M.T., Landi,S., Le Marchand,L., Mambrini,A., Mannisto,S.,
            Milne,R.L., Nakamura,Y., Oberg,A.L., Owzar,K., Patel,A.V.,
            Peeters,P.H., Peters,U., Pezzilli,R., Piepoli,A., Porta,M.,
            Real,F.X., Riboli,E., Rothman,N., Scarpa,A., Shu,X.O.,
            Silverman,D.T., Soucek,P., Sund,M., Talar-Wojnarowska,R.,
            Taylor,P.R., Theodoropoulos,G.E., Thornquist,M., Tjonneland,A.,
            Tobias,G.S., Trichopoulos,D., Vodicka,P., Wactawski-Wende,J.,
            Wentzensen,N., Wu,C., Yu,H., Yu,K., Zeleniuch-Jacquotte,A.,
            Hoover,R., Hartge,P., Fuchs,C., Chanock,S.J.,
            Stolzenberg-Solomon,R.S. and Amundadottir,L.T.
  TITLE     Genome-wide association study identifies multiple susceptibility
            loci for pancreatic cancer
  JOURNAL   Nat Genet 46 (9), 994-1000 (2014)
   PUBMED   25086665
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Schneider,E., Mayer,S., El Hajj,N., Jensen,L.R., Kuss,A.W.,
            Zischler,H., Kondova,I., Bontrop,R.E., Navarro,B., Fuchs,E.,
            Zechner,U. and Haaf,T.
  TITLE     Methylation and expression analyses of the 7q autism susceptibility
            locus genes MEST, COPG2, and TSGA14 in human and anthropoid primate
            cortices
  JOURNAL   Cytogenet Genome Res 136 (4), 278-287 (2012)
   PUBMED   22456293
  REMARK    GeneRIF: In cortices, the MEST promoter was hemimethylated, as
            expected for a differentially methylated imprinting control region,
            whereas the COPG2 and TSGA14 promoters were completely
            demethylated, typical for transcriptionally active non-imprinted
            genes.
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Wegmann,D., Hess,P., Baier,C., Wieland,F.T. and Reinhard,C.
  TITLE     Novel isotypic gamma/zeta subunits reveal three coatomer complexes
            in mammals
  JOURNAL   Mol Cell Biol 24 (3), 1070-1080 (2004)
   PUBMED   14729954
REFERENCE   6  (residues 1 to 871)
  AUTHORS   Yamasaki,K., Hayashida,S., Miura,K., Masuzaki,H., Ishimaru,T.,
            Niikawa,N. and Kishino,T.
  TITLE     The novel gene, gamma2-COP (COPG2), in the 7q32 imprinted domain
            escapes genomic imprinting
  JOURNAL   Genomics 68 (3), 330-335 (2000)
   PUBMED   10995575
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Harter,C. and Wieland,F.T.
  TITLE     A single binding site for dilysine retrieval motifs and p23 within
            the gamma subunit of coatomer
  JOURNAL   Proc Natl Acad Sci U S A 95 (20), 11649-11654 (1998)
   PUBMED   9751720
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Lowe,M. and Kreis,T.E.
  TITLE     In vivo assembly of coatomer, the COP-I coat precursor
  JOURNAL   J Biol Chem 271 (48), 30725-30730 (1996)
   PUBMED   8940050
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Newman,A., Suarez,C., Lee,W.S. and Honrubia,V.
  TITLE     Afferent innervation of the vestibular nuclei in the chinchilla.
            II. Description of the vestibular nerve and nuclei
  JOURNAL   Brain Res 597 (2), 278-297 (1992)
   PUBMED   1472999
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK291409.1, AF157833.1, HY355769.1 and BX089636.1.
            
            On Jun 15, 2006 this sequence version replaced NP_036265.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291409.1, HM005552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000425248.5/ ENSP00000402346.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.2"
     Protein         1..871
                     /product="coatomer subunit gamma-2 isoform 1"
                     /note="coat protein, nonclathrin, gamma-2-cop; coatomer
                     subunit gamma-2; gamma-2-coat protein; testicular
                     secretory protein Li 12; coatomer protein complex subunit
                     gamma 2; COPI coat complex subunit gamma 2"
                     /calculated_mol_wt=97492
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          7..866
                     /region_name="SEC21"
                     /note="Vesicle coat complex COPI, gamma subunit
                     [Intracellular trafficking and secretion]; COG5240"
                     /db_xref="CDD:227565"
     Region          64..101
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          283..320
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          288..313
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          321..355
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          323..354
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          356..392
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          363..385
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          395..430
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          398..423
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          435..461
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          467..504
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBF2.1)"
     Region          471..501
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          508..534
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Y678; propagated from
                     UniProtKB/Swiss-Prot (Q9UBF2.1)"
     CDS             1..871
                     /gene="COPG2"
                     /gene_synonym="2-COP; gamma-2-COP"
                     /coded_by="NM_012133.6:81..2696"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75662.1"
                     /db_xref="GeneID:26958"
                     /db_xref="HGNC:HGNC:2237"
                     /db_xref="MIM:604355"
ORIGIN      
        1 mikkfdkkde esgsgsnpfq hleksavlqe arifnetpin prrclhiltk ilyllnqgeh
       61 fgtteateaf famtrlfqsn dqtlrrmcyl tikematise dviivtsslt kdmtgkedvy
      121 rgpairalcr itdgtmlqai erymkqaivd kvssvsssal vsslhmmkis ydvvkrwine
      181 aqeaassdni mvqyhalgvl yhlrkndrla vskmlnkftk sglksqfayc mliriasrll
      241 ketedghesp lfdfiesclr nkhemviyea asaiihlpnc tarelapavs vlqlfcsspk
      301 palryaavrt lnkvamkhps avtacnldle nlitdsnrsi atlaittllk tgsessvdrl
      361 mkqissfvse isdefkvvvv qaisalcqky prkhsvmmtf lsnmlrddgg feykraivdc
      421 iisiveenpe skeaglahlc efiedcehtv latkilhllg kegprtpvps kyirfifnrv
      481 vleneavraa avsalakfga qnesllpsil vllqrcmmdt ddevrdratf ylnvlqqrqm
      541 alnatyifng ltvsvpgmek alhqytleps ekpfdmksip lamapvfeqk aeitlvatkp
      601 eklapsrqdi fqeqlaaipe flnigplfks sepvqlteae teyfvrcikh mftnhivfqf
      661 dctntlndql lekvtvqmep sdsyevlsci papslpynqp gicytlvrlp dddptavags
      721 fsctmkftvr dcdpntgvpd edgyddeyvl edlevtvsdh iqkvlkpnfa aaweevgdtf
      781 ekeetfalss tktleeavnn iitflgmqpc ersdkvpenk nshslylagi frggydllvr
      841 srlaladgvt mqvtvrsker tpvdvilasv g
//
LOCUS       NP_001129498             368 aa            linear   PRI 20-NOV-2025
DEFINITION  protein SEC13 homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001129498
VERSION     NP_001129498.1
DBSOURCE    REFSEQ: accession NM_001136026.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Jiang,C., Dai,X., He,S., Zhou,H., Fang,L., Guo,J., Liu,S.,
            Zhang,T., Pan,W., Yu,H., Fu,T., Li,D., Inuzuka,H., Wang,P., Xiao,J.
            and Wei,W.
  TITLE     Ring domains are essential for GATOR2-dependent mTORC1 activation
  JOURNAL   Mol Cell 83 (1), 74-89 (2023)
   PUBMED   36528027
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Valenstein,M.L., Rogala,K.B., Lalgudi,P.V., Brignole,E.J., Gu,X.,
            Saxton,R.A., Chantranupong,L., Kolibius,J., Quast,J.P. and
            Sabatini,D.M.
  TITLE     Structure of the nutrient-sensing hub GATOR2
  JOURNAL   Nature 607 (7919), 610-616 (2022)
   PUBMED   35831510
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Mammoto,A., Sasaki,T., Kim,Y. and Takai,Y.
  TITLE     Physical and functional interaction of rabphilin-11 with mammalian
            Sec13 protein. Implication in vesicle trafficking
  JOURNAL   J Biol Chem 275 (18), 13167-13170 (2000)
   PUBMED   10747849
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Shaywitz,D.A., Orci,L., Ravazzola,M., Swaroop,A. and Kaiser,C.A.
  TITLE     Human SEC13Rp functions in yeast and is located on transport
            vesicles budding from the endoplasmic reticulum
  JOURNAL   J Cell Biol 128 (5), 769-777 (1995)
   PUBMED   7876304
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Swaroop,A., Yang-Feng,T.L., Liu,W., Gieser,L., Barrow,L.L.,
            Chen,K.C., Agarwal,N., Meisler,M.H. and Smith,D.I.
  TITLE     Molecular characterization of a novel human gene, SEC13R, related
            to the yeast secretory pathway gene SEC13, and mapping to a
            conserved linkage group on human chromosome 3p24-p25 and mouse
            chromosome 6
  JOURNAL   Hum Mol Genet 3 (8), 1281-1286 (1994)
   PUBMED   7987303
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301999.1 and BC091506.1.
            
            Summary: The protein encoded by this gene belongs to the SEC13
            family of WD-repeat proteins. It is a constituent of the
            endoplasmic reticulum and the nuclear pore complex. It has
            similarity to the yeast SEC13 protein, which is required for
            vesicle biogenesis from endoplasmic reticulum during the transport
            of proteins. Multiple alternatively spliced transcript variants
            have been found. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301999.1, SRR18074969.3671363.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..368
                     /product="protein SEC13 homolog isoform 3"
                     /note="SEC13-related protein; SEC13 homolog, nuclear pore
                     and COPII coating complex component; protein SEC13
                     homolog; SEC13-like protein 1; GATOR complex protein
                     SEC13; GATOR2 complex protein SEC13; SEC13 homolog,
                     nuclear pore and COPII coat complex component"
                     /calculated_mol_wt=40616
     Region          <71..335
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          107..147
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          152..198
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          206..255
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          261..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          311..337
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..368
                     /gene="SEC13"
                     /gene_synonym="D3S1231E; npp-20; SEC13L1; SEC13R"
                     /coded_by="NM_001136026.3:101..1207"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS63540.1"
                     /db_xref="GeneID:6396"
                     /db_xref="HGNC:HGNC:10697"
                     /db_xref="MIM:600152"
ORIGIN      
        1 mrepvltwcv plellcshpl plsaflksqv klytyracag kdemgkmvsv intvdtshed
       61 mihdaqmdyy gtrlatcssd rsvkifdvrn ggqiliadlr ghegpvwqva wahpmygnil
      121 ascsydrkvi iwreengtwe kshehaghds svnsvcwaph dyglilacgs sdgaisllty
      181 tgegqwevkk innahtigcn avswapavvp gslidhpsgq kpnyikrfas ggcdnliklw
      241 keeedgqwke eqkleahsdw vrdvawapsi glptstiasc sqdgrvfiwt cddassntws
      301 pkllhkfndv vwhvswsita nilavsggdn kvtlwkesvd gqwvcisdvn kgqgsvsasv
      361 tegqqneq
//
LOCUS       NP_001166896             906 aa            linear   PRI 20-NOV-2025
DEFINITION  whirlin isoform 3 [Homo sapiens].
ACCESSION   NP_001166896
VERSION     NP_001166896.1
DBSOURCE    REFSEQ: accession NM_001173425.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 906)
  AUTHORS   AitRaise,I., Amalou,G., Redouane,S., Charoute,H., Snoussi,K.,
            Abdelghaffar,H., Bonnet,C., Petit,C. and Barakat,A.
  TITLE     Novel pathogenic WHRN variant causing hearing loss in a moroccan
            family
  JOURNAL   Mol Biol Rep 50 (12), 10663-10669 (2023)
   PUBMED   37924449
  REMARK    GeneRIF: Novel pathogenic WHRN variant causing hearing loss in a
            moroccan family.
REFERENCE   2  (residues 1 to 906)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 906)
  AUTHORS   Visconti,L., Malagrino,F., Troilo,F., Pagano,L., Toto,A. and
            Gianni,S.
  TITLE     Folding and Misfolding of a PDZ Tandem Repeat
  JOURNAL   J Mol Biol 433 (7), 166862 (2021)
   PUBMED   33539879
  REMARK    GeneRIF: Folding and Misfolding of a PDZ Tandem Repeat.
REFERENCE   4  (residues 1 to 906)
  AUTHORS   Lin,L., Shi,Y., Wang,M., Wang,C., Lu,Q., Zhu,J. and Zhang,R.
  TITLE     Phase separation-mediated condensation of Whirlin-Myo15-Eps8
            stereocilia tip complex
  JOURNAL   Cell Rep 34 (8), 108770 (2021)
   PUBMED   33626355
  REMARK    GeneRIF: Phase separation-mediated condensation of
            Whirlin-Myo15-Eps8 stereocilia tip complex.
REFERENCE   5  (residues 1 to 906)
  AUTHORS   van Wijk,E., van der Zwaag,B., Peters,T., Zimmermann,U., Te
            Brinke,H., Kersten,F.F., Marker,T., Aller,E., Hoefsloot,L.H.,
            Cremers,C.W., Cremers,F.P., Wolfrum,U., Knipper,M., Roepman,R. and
            Kremer,H.
  TITLE     The DFNB31 gene product whirlin connects to the Usher protein
            network in the cochlea and retina by direct association with USH2A
            and VLGR1
  JOURNAL   Hum Mol Genet 15 (5), 751-765 (2006)
   PUBMED   16434480
  REMARK    GeneRIF: This paper concludes that this protein plays a role in
            photoreceptor and hair cell synapse organization in the related rat
            gene.
REFERENCE   6  (residues 1 to 906)
  AUTHORS   Mburu,P., Mustapha,M., Varela,A., Weil,D., El-Amraoui,A.,
            Holme,R.H., Rump,A., Hardisty,R.E., Blanchard,S., Coimbra,R.S.,
            Perfettini,I., Parkinson,N., Mallon,A.M., Glenister,P.,
            Rogers,M.J., Paige,A.J., Moir,L., Clay,J., Rosenthal,A., Liu,X.Z.,
            Blanco,G., Steel,K.P., Petit,C. and Brown,S.D.
  TITLE     Defects in whirlin, a PDZ domain molecule involved in stereocilia
            elongation, cause deafness in the whirler mouse and families with
            DFNB31
  JOURNAL   Nat Genet 34 (4), 421-428 (2003)
   PUBMED   12833159
  REMARK    GeneRIF: Defects in whirlin, a PDZ domain molecule involved in
            stereocilia elongation, cause deafness in the whirler mouse and
            families with DFNB31.
REFERENCE   7  (residues 1 to 906)
  AUTHORS   Yap,C.C., Liang,F., Yamazaki,Y., Muto,Y., Kishida,H., Hayashida,T.,
            Hashikawa,T. and Yano,R.
  TITLE     CIP98, a novel PDZ domain protein, is expressed in the central
            nervous system and interacts with calmodulin-dependent serine
            kinase
  JOURNAL   J Neurochem 85 (1), 123-134 (2003)
   PUBMED   12641734
  REMARK    GeneRIF: This paper describes a PDZ domain protein and its role in
            synaptic transmission in the related rat gene.
REFERENCE   8  (residues 1 to 906)
  AUTHORS   Mustapha,M., Chouery,E., Chardenoux,S., Naboulsi,M., Paronnaud,J.,
            Lemainque,A., Megarbane,A., Loiselet,J., Weil,D., Lathrop,M. and
            Petit,C.
  TITLE     DFNB31, a recessive form of sensorineural hearing loss, maps to
            chromosome 9q32-34
  JOURNAL   Eur J Hum Genet 10 (3), 210-212 (2002)
   PUBMED   11973626
REFERENCE   9  (residues 1 to 906)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 906)
  AUTHORS   Koenekoop,R., Arriaga,M., Trzupek,K.M. and Lentz,J.
  TITLE     Usher Syndrome Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138895.16, BC142614.1,
            BC014524.1, BC142684.1 and BC136416.1.
            
            Summary: This gene is thought to function in the organization and
            stabilization of sterocilia elongation and actin cystoskeletal
            assembly, based on studies of the related mouse gene. Mutations in
            this gene have been associated with autosomal recessive
            non-syndromic deafness and Usher Syndrome. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Nov
            2016].
            
            Transcript Variant: This variant (3) contains an alternate,
            in-frame splice site in the 3' coding region, compared to variant
            1. The encoded protein (isoform 3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014524.1, DRR138513.461575.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..906
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..906
                     /product="whirlin isoform 3"
                     /note="CASK-interacting protein CIP98; autosomal recessive
                     deafness type 31 protein"
                     /calculated_mol_wt=96356
     Region          37..112
                     /region_name="HN_L-whirlin_R1_like"
                     /note="first harmonin_N_like domain (repeat 1) of the long
                     isoform of whirlin, and related domains; cd07356"
                     /db_xref="CDD:259822"
     Site            order(39,43,56,59,62..63,66)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259822"
     Region          138..219
                     /region_name="PDZ1_FL-whirlin"
                     /note="PDZ domain 1 of the full-length isoform of whirlin
                     and related domains; cd06740"
                     /db_xref="CDD:467222"
     Site            order(151..157,169,172,201,205,208..209)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467222"
     Region          243..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          277..360
                     /region_name="PDZ2_FL-whirlin"
                     /note="PDZ domain 2 of the full-length isoform of whirlin
                     and related domains; cd06741"
                     /db_xref="CDD:467223"
     Site            order(289..295,307,310,339,343,346..347)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467223"
     Region          419..499
                     /region_name="HN_L-whirlin_R2_like"
                     /note="second harmonin_N_like domain (repeat 2) of the
                     long isoform of whirlin, and related domains; cd07357"
                     /db_xref="CDD:259823"
     Site            order(420,423,427,440,443,446..447,450)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259823"
     Region          502..540
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          565..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          <581..>816
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          684..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P202.4)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P202.4)"
     Region          813..903
                     /region_name="PDZ3_FL-whirlin-like"
                     /note="PDZ domain 3 of the full-length isoform of whirlin,
                     PDZ domain 1 of the short isoform of whirlin, and related
                     domains; cd06742"
                     /db_xref="CDD:467224"
     Site            order(824..830,843,846,876,880,883..884)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467224"
     CDS             1..906
                     /gene="WHRN"
                     /gene_synonym="CIP98; DFNB31; PDZD7B; USH2D; WI"
                     /coded_by="NM_001173425.2:673..3393"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25861"
                     /db_xref="HGNC:HGNC:16361"
                     /db_xref="MIM:607928"
ORIGIN      
        1 mnapldglsv sssstgslgs aagaggggga glrllsanvr qlhqaltall seaereqfth
       61 clnayharrn vfdlvrtlrv lldspvkrrl lpmlrlvipr sdqllfdqyt aeglylpatt
      121 pyrqpawggp dsagpgevrl vslrrakahe glgfsirggs ehgvgiyvsl vepgslaeke
      181 glrvgdqilr vndkslarvt haeavkalkg skklvlsvys agripggyvt nhiytwvdpq
      241 grsisppsgl pqphggalrq qegdrrstlh llqggdekkv nlvlgdgrsl gltirggaey
      301 glgiyitgvd pgseaegsgl kvgdqilevn grsflnilhd eavrllkssr hliltvkdvg
      361 rlpharttvd etkwiassri retmansagf lgdlttegin kpgfykgpag sqvtlsslgn
      421 qtrvlleeqa rhllneqeha tmayyldeyr ggsvsvealv malfkllnth akfsllsevr
      481 gtispqdler fdhlvlrrei esmkarqppg pgagdtysmv sysdtgsstg shgtsttvss
      541 arntldleet geavqgnina lpdvsvddvr stsqglssfk plprppplaq gndlplgqpr
      601 klgredlqpp ssmpscsgtv fsapqnrspp agtaptpgts saqdlpsspi yasvspanps
      661 skrpldahla lvnqhpigpf prvqspphlk spsaeatvag gcllppspsg hpdqtgtnqh
      721 fvmvevhrpd sepdvnevra lpqtrtstls qlsdsgqtls edsgvdagea easapgrgrq
      781 svstksrssk elprnerptd gankppglle ptstlvrvkk saatlgiaie ggantrqplp
      841 rivtiqrggs ahncgqlkvg hvilevnglt lrgkehreaa riiaeafktk drdyidflvt
      901 efnvml
//
LOCUS       NP_001350922             646 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform a [Homo sapiens].
ACCESSION   NP_001350922
VERSION     NP_001350922.1
DBSOURCE    REFSEQ: accession NM_001363993.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.238525.1,
                                           SRR1163655.132369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..646
                     /product="calnexin isoform a"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=73279
     Region          125..494
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     CDS             1..646
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001363993.1:212..2152"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 myqkentqwl rnlavtapil easnpvgegq gvksrkapes sskcisfhtg gleimegkwl
       61 lcmllvlgta iveahdghdd dvidieddld dvieevedsk pdttappssp kvtykapvpt
      121 gevyfadsfd rgtlsgwils kakkddtdde iakydgkwev eemkesklpg dkglvlmsra
      181 khhaisakln kpflfdtkpl ivqyevnfqn giecggayvk llsktpelnl dqfhdktpyt
      241 imfgpdkcge dyklhfifrh knpktgiyee khakrpdadl ktyftdkkth lytlilnpdn
      301 sfeilvdqsv vnsgnllndm tppvnpsrei edpedrkped wderpkipdp eavkpddwde
      361 dapakipdee atkpegwldd epeyvpdpda ekpedwdedm dgeweapqia nprcesapgc
      421 gvwqrpvidn pnykgkwkpp midnpsyqgi wkprkipnpd ffedlepfrm tpfsaiglel
      481 wsmtsdiffd nfiicadrri vddwandgwg lkkaadgaae pgvvgqmiea aeerpwlwvv
      541 yiltvalpvf lvilfccsgk kqtsgmeykk tdapqpdvke eeeekeeekd kgdeeeegee
      601 kleekqksda eedggtvsqe eedrkpkaee deilnrsprn rkprre
//
LOCUS       NP_055073               1530 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptonemal complex protein 2 [Homo sapiens].
ACCESSION   NP_055073 XP_005260304
VERSION     NP_055073.2
DBSOURCE    REFSEQ: accession NM_014258.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1530)
  AUTHORS   Li,J., Schilit,S.L.P., Liang,S., Qin,N., Teng,X. and Zhang,J.
  TITLE     Novel Loss-of-Function SYCP2 Variants in Infertile Males Upgrade
            the Gene-Disease Clinical Validity Classification for SYCP2 and
            Male Infertility to Strong
  JOURNAL   Genes (Basel) 15 (8), 1092 (2024)
   PUBMED   39202451
  REMARK    GeneRIF: Novel Loss-of-Function SYCP2 Variants in Infertile Males
            Upgrade the Gene-Disease Clinical Validity Classification for SYCP2
            and Male Infertility to Strong.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1530)
  AUTHORS   Schilit,S.L.P., Menon,S., Friedrich,C., Kammin,T., Wilch,E.,
            Hanscom,C., Jiang,S., Kliesch,S., Talkowski,M.E., Tuttelmann,F.,
            MacQueen,A.J. and Morton,C.C.
  TITLE     SYCP2 Translocation-Mediated Dysregulation and Frameshift Variants
            Cause Human Male Infertility
  JOURNAL   Am J Hum Genet 106 (1), 41-57 (2020)
   PUBMED   31866047
  REMARK    GeneRIF: SYCP2 Translocation-Mediated Dysregulation and Frameshift
            Variants Cause Human Male Infertility.
REFERENCE   3  (residues 1 to 1530)
  AUTHORS   Cahoon,C.K. and Hawley,R.S.
  TITLE     Regulating the construction and demolition of the synaptonemal
            complex
  JOURNAL   Nat Struct Mol Biol 23 (5), 369-377 (2016)
   PUBMED   27142324
  REMARK    Review article
REFERENCE   4  (residues 1 to 1530)
  AUTHORS   Masterson,L., Sorgeloos,F., Winder,D., Lechner,M., Marker,A.,
            Malhotra,S., Sudhoff,H., Jani,P., Goon,P. and Sterling,J.
  TITLE     Deregulation of SYCP2 predicts early stage human
            papillomavirus-positive oropharyngeal carcinoma: A prospective
            whole transcriptome analysis
  JOURNAL   Cancer Sci 106 (11), 1568-1575 (2015)
   PUBMED   26334652
  REMARK    GeneRIF: SYCP2 may contribute to genetic instability during
            HPV-associated cancer development
REFERENCE   5  (residues 1 to 1530)
  AUTHORS   Aston,K.I., Krausz,C., Laface,I., Ruiz-Castane,E. and Carrell,D.T.
  TITLE     Evaluation of 172 candidate polymorphisms for association with
            oligozoospermia or azoospermia in a large cohort of men of European
            descent
  JOURNAL   Hum Reprod 25 (6), 1383-1397 (2010)
   PUBMED   20378615
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1530)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   7  (residues 1 to 1530)
  AUTHORS   Schalk,J.A., Offenberg,H.H., Peters,E., Groot,N.P., Hoovers,J.M.
            and Heyting,C.
  TITLE     Isolation and characterization of the human SCP2 cDNA and
            chromosomal localization of the gene
  JOURNAL   Mamm Genome 10 (6), 642-644 (1999)
   PUBMED   10341103
REFERENCE   8  (residues 1 to 1530)
  AUTHORS   Offenberg,H.H., Schalk,J.A., Meuwissen,R.L., van Aalderen,M.,
            Kester,H.A., Dietrich,A.J. and Heyting,C.
  TITLE     SCP2: a major protein component of the axial elements of
            synaptonemal complexes of the rat
  JOURNAL   Nucleic Acids Res 26 (11), 2572-2579 (1998)
   PUBMED   9592139
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX649108.1, AL109928.33,
            AL158092.30 and DB636651.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Dec 17, 2015 this sequence version replaced
            XP_005260304.1, NP_055073.1.
            
            Summary: The synaptonemal complex is a proteinaceous structure that
            links homologous chromosomes during the prophase of meiosis. The
            protein encoded by this gene is a major component of the
            synaptonemal complex and may bind DNA at scaffold attachment
            regions. The encoded protein requires synaptonemal complex protein
            3, but not 1, for inclusion in the synaptonemal complex. [provided
            by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX649108.1, BX648091.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357552.8/ ENSP00000350162.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..1530
                     /product="synaptonemal complex protein 2"
                     /note="synaptonemal complex lateral element protein"
                     /calculated_mol_wt=175508
     Region          9..187
                     /region_name="SYCP2_ARLD"
                     /note="Synaptonemal complex 2 armadillo-repeat-like
                     domain; pfam18581"
                     /db_xref="CDD:465809"
     Region          278..389
                     /region_name="SYCP2_SLD"
                     /note="Synaptonemal complex 2 Spt16M-like domain;
                     pfam18584"
                     /db_xref="CDD:465811"
     Region          439..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Region          496..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Region          653..676
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70608; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Region          693..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Region          755..795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Region          962..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70608; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70608; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     Site            1339
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CUU3; propagated from
                     UniProtKB/Swiss-Prot (Q9BX26.2)"
     CDS             1..1530
                     /gene="SYCP2"
                     /gene_synonym="SCP-2; SCP2; SPGF1"
                     /coded_by="NM_014258.4:209..4801"
                     /db_xref="CCDS:CCDS13482.1"
                     /db_xref="GeneID:10388"
                     /db_xref="HGNC:HGNC:11490"
                     /db_xref="MIM:604105"
ORIGIN      
        1 mpirpdlqql ekciddalrk ndfkplktll qidicedvki kcskqffhkv dnlicrelnk
       61 edihnvsail vsvgrcgkni svlgqagllt mikqgliqkm vawfekskdi iqsqgnskde
      121 avlnmiedlv dlllvihdvs degkkqvves fvpricslvi dsrvniciqq eiikkmnaml
      181 dkmpqdarki lsnqemlilm ssmgerilda gdydlqvgiv ealcrmttek qrqelahqwf
      241 smdfiakafk rikdsefetd criflnlvng mlgdkrrvft fpclsafldk yelqipsdek
      301 leefwidfnl gsqtlsfyia gdnddhqwea vtvpeekvqi ysievreskk lltiilkntv
      361 kiskregkel llyfdaslei tnvtqkifga tkhresirkq gisvaktslh ilfdasgsqi
      421 lvpesqispv geelvslkek skspkefakp skyiknsdkg nrnnsqlekt tpskrkmsea
      481 smivsgadry tmrspvlfsn tsipprrrri kpplqmtssa ekpsvsqtse nrvdnaaslk
      541 srssegrhrr dnidkhikta kcventenkn vefpnqnfse lqdvipdsqa aekrdhtilp
      601 gvldnicgnk ihskwacwtp vtnielcnnq rastssgdtl nqdivinkkl tkqkssssis
      661 dhnsegtgkv kykkeqtdhi kidkaevevc kkhnqqqnhp kysgqknten akqsdwpves
      721 ettfksvlln ktieesliyr kkyilskdvn tatcdknpsa sknvqshrka ekeltselns
      781 wdskqkkmre kskgkeftnv aeslisqink ryktkddiks trklkeslin sgfsnkpvvq
      841 lskekvqkks yrklkttfvn vtsecpvndv ynfnlngadd piiklgiqef qatakeacad
      901 rsirlvgprn hdelkssvkt kdkkiitnhq kknlfsdtet eyrcddsktd iswlrepksk
      961 pqlidysrnk nvknhksgks rsslekgqps skmtpsknit kkmdktipeg rirlprkatk
     1021 tkknykdlsn seseceqefs hsfkenipvk eenihsrmkt vklpkkqqkv fcaetekels
     1081 kqwknssllk dairdncldl sprslsgsps sievtrciek itekdftqdy dcitksispy
     1141 pktsslesln snsgvggtik spknneknfl casescspip rplflprhtp tksntivnrk
     1201 kisslvltqe tqnsnsysdv ssysseerfm eiesphinen yiqskreesh lasslsksse
     1261 grektwfdmp cdathvsgpt qhlsrkriyi ednlsnsnev emeekgerra nllpkklcki
     1321 edadhhihkm sesvsslstn dfsipwetwq nefagiemty etyerlnsef krrnnirhkm
     1381 lsyfttqswk taqqhlrtmn hqsqdsrikk ldkfqfiiie elenfekdsq slkdlekefv
     1441 dfwekifqkf sayqkseqqr lhllktslak svfcntdsee tvftsemclm kedmkvlqdr
     1501 llkdmleeel lnvrrelmsv fmshernanv
//
LOCUS       NP_001355045             561 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001355045
VERSION     NP_001355045.1
DBSOURCE    REFSEQ: accession NM_001368116.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Ergun,S., Guney,S., Temiz,E., Petrovic,N. and Gunes,S.
  TITLE     Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
  JOURNAL   Anticancer Agents Med Chem 18 (12), 1695-1701 (2018)
   PUBMED   30019650
  REMARK    GeneRIF: Significance of miR-15a-5p and CNKSR3 as Novel Prognostic
            Biomarkers in Non-Small Cell Lung Cancer
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Jin,L., Wang,T., Jiang,S., Chen,M., Zhang,R., Hu,C., Jia,W. and
            Liu,Z.
  TITLE     The Association of a Genetic Variant in SCAF8-CNKSR3 with Diabetic
            Kidney Disease and Diabetic Retinopathy in a Chinese Population
  JOURNAL   J Diabetes Res 2017, 6542689 (2017)
   PUBMED   28401168
  REMARK    GeneRIF: SCAF8-CNKSR3 variant rs955333 was not associated with
            diabetic kidney disease but showed association with diabetic
            retinopathy in Chinese type 2 diabetes patients
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Lake,S.L., Damato,B.E., Kalirai,H., Dodson,A.R., Taktak,A.F.,
            Lloyd,B.H. and Coupland,S.E.
  TITLE     Single nucleotide polymorphism array analysis of uveal melanomas
            reveals that amplification of CNKSR3 is correlated with improved
            patient survival
  JOURNAL   Am J Pathol 182 (3), 678-687 (2013)
   PUBMED   23357503
  REMARK    GeneRIF: Cox regression and Kaplan-Meier survival analysis
            identified that amplification of the CNKSR3 gene (log-rank, P =
            0.022) with an associated increase in its protein expression
            (log-rank, P = 0.011) correlated with longer patient survival.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Okada,Y., Sim,X., Go,M.J., Wu,J.Y., Gu,D., Takeuchi,F.,
            Takahashi,A., Maeda,S., Tsunoda,T., Chen,P., Lim,S.C., Wong,T.Y.,
            Liu,J., Young,T.L., Aung,T., Seielstad,M., Teo,Y.Y., Kim,Y.J.,
            Lee,J.Y., Han,B.G., Kang,D., Chen,C.H., Tsai,F.J., Chang,L.C.,
            Fann,S.J., Mei,H., Rao,D.C., Hixson,J.E., Chen,S., Katsuya,T.,
            Isono,M., Ogihara,T., Chambers,J.C., Zhang,W., Kooner,J.S.,
            Albrecht,E., Yamamoto,K., Kubo,M., Nakamura,Y., Kamatani,N.,
            Kato,N., He,J., Chen,Y.T., Cho,Y.S., Tai,E.S. and Tanaka,T.
  CONSRTM   KidneyGen Consortium; CKDGen Consortium; GUGC consortium
  TITLE     Meta-analysis identifies multiple loci associated with kidney
            function-related traits in east Asian populations
  JOURNAL   Nat Genet 44 (8), 904-909 (2012)
   PUBMED   22797727
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Shin,S., Park,J.S., Kim,Y.J., Oh,T., An,S. and Park,C.S.
  TITLE     Differential gene expression profile in PBMCs from subjects with
            AERD and ATA: a gene marker for AERD
  JOURNAL   Mol Genet Genomics 287 (5), 361-371 (2012)
   PUBMED   22457146
  REMARK    GeneRIF: two gene markers (CNKSR3 and SPTBN2) differentiate between
            aspirin-exacerbated respiratory disease and aspirin-tolerant asthma
            with a perfect discriminative power
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Pankratz,N., Beecham,G.W., DeStefano,A.L., Dawson,T.M.,
            Doheny,K.F., Factor,S.A., Hamza,T.H., Hung,A.Y., Hyman,B.T.,
            Ivinson,A.J., Krainc,D., Latourelle,J.C., Clark,L.N., Marder,K.,
            Martin,E.R., Mayeux,R., Ross,O.A., Scherzer,C.R., Simon,D.K.,
            Tanner,C., Vance,J.M., Wszolek,Z.K., Zabetian,C.P., Myers,R.H.,
            Payami,H., Scott,W.K. and Foroud,T.
  CONSRTM   PD GWAS Consortium
  TITLE     Meta-analysis of Parkinson's disease: identification of a novel
            locus, RIT2
  JOURNAL   Ann Neurol 71 (3), 370-384 (2012)
   PUBMED   22451204
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Attar,M.A., Salem,J.C., Pursel,H.S. and Santy,L.C.
  TITLE     CNK3 and IPCEF1 produce a single protein that is required for HGF
            dependent Arf6 activation and migration
  JOURNAL   Exp Cell Res 318 (3), 228-237 (2012)
   PUBMED   22085542
  REMARK    GeneRIF: CNK3 and IPCEF1 produce a single protein that is required
            for HGF dependent Arf6 activation and migration.
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Ziera,T., Irlbacher,H., Fromm,A., Latouche,C., Krug,S.M., Fromm,M.,
            Jaisser,F. and Borden,S.A.
  TITLE     Cnksr3 is a direct mineralocorticoid receptor target gene and plays
            a key role in the regulation of the epithelial sodium channel
  JOURNAL   FASEB J 23 (11), 3936-3946 (2009)
   PUBMED   19567370
  REMARK    GeneRIF: CNKSR3, a homologue of scaffold proteins involved in MAPK
            pathway regulation, is a direct target of MR and is required for
            the maintenance of transepithelial sodium transport in the kidney.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL357075.17.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.127483.1,
                                           SRR1803611.234515.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.2"
     Protein         1..561
                     /product="connector enhancer of kinase suppressor of ras 3
                     isoform 1"
                     /note="connector enhancer of kinase suppressor of ras 3;
                     membrane associated guanylate kinase, WW and PDZ domain
                     containing 1; maguin-like protein; CNK homolog protein 3;
                     connector enhancer of KSR 3; membrane-associated guanylate
                     kinase-interacting protein-like 1"
                     /calculated_mol_wt=62443
     Region          <24..78
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            order(26,51,55,60..67,69..70,73)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          86..178
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          216..296
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(228..234,244,247,277,281,284..285)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          338..551
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     CDS             1..561
                     /gene="CNKSR3"
                     /gene_synonym="CNK3; CNK3/IPCEF1; MAGI1"
                     /coded_by="NM_001368116.1:309..1994"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:154043"
                     /db_xref="HGNC:HGNC:23034"
                     /db_xref="MIM:617476"
ORIGIN      
        1 mqtsaewpvr sylsyllral pfqglddclq qyvhkferek ingeqllqis hqdleelgvt
       61 righqelvle avdllcalny gletdnmknl vlklrasshn lqnyissrrk spaydgntsr
      121 kapnefltsv veligaakal lawldrapft gitdfsvtkn kiiqlcldlt ttvqkdcfva
      181 emedkvltvv kvlngicdkt irsttdpvms qcacleevhl pnikpgeglg myikstydgl
      241 hvitgttens padrsqkiha gdeviqvnqq tvvgwqlknl vkklrenptg vvlllkkrpt
      301 gsfnftpapl knlrwkpplv qtspppattq spestmdtsl kkeksaildl yippppavpy
      361 sprdengsfv yggsskckqp lpgpkgsesp nsfldqesrr rrftiadsdq lpgysvetni
      421 lptkmrektp sygkprplsm padgnwmgiv dpfarprghg rkgedalcry fsnerippii
      481 eesssppyrf srptterhlv rgadyirgsr cyinsdlhss atipfqeegt kkksgssatk
      541 ssstepsllv swftrlkllt h
//
LOCUS       NP_001098684             534 aa            linear   PRI 20-NOV-2025
DEFINITION  set1/Ash2 histone methyltransferase complex subunit ASH2 isoform b
            [Homo sapiens].
ACCESSION   NP_001098684
VERSION     NP_001098684.1
DBSOURCE    REFSEQ: accession NM_001105214.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Batbayar,G., Ishimura,A., Lyu,H., Wanna-Udom,S., Meguro-Horike,M.,
            Terashima,M., Horike,S.I., Takino,T. and Suzuki,T.
  TITLE     ASH2L, a COMPASS core subunit, is involved in the cell invasion and
            migration of triple-negative breast cancer cells through the
            epigenetic control of histone H3 lysine 4 methylation
  JOURNAL   Biochem Biophys Res Commun 669, 19-29 (2023)
   PUBMED   37262949
  REMARK    GeneRIF: ASH2L, a COMPASS core subunit, is involved in the cell
            invasion and migration of triple-negative breast cancer cells
            through the epigenetic control of histone H3 lysine 4 methylation.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Lee,Y.T., Ayoub,A., Park,S.H., Sha,L., Xu,J., Mao,F., Zheng,W.,
            Zhang,Y., Cho,U.S. and Dou,Y.
  TITLE     Mechanism for DPY30 and ASH2L intrinsically disordered regions to
            modulate the MLL/SET1 activity on chromatin
  JOURNAL   Nat Commun 12 (1), 2953 (2021)
   PUBMED   34012049
  REMARK    GeneRIF: Mechanism for DPY30 and ASH2L intrinsically disordered
            regions to modulate the MLL/SET1 activity on chromatin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Li,X., Qu,M., Zhang,J., Chen,K. and Ma,X.
  TITLE     CircASH2L facilitates tumor-like biologic behaviours and
            inflammation of fibroblast-like synoviocytes via miR-129-5p/HIPK2
            axis in rheumatoid arthritis
  JOURNAL   J Orthop Surg Res 16 (1), 302 (2021)
   PUBMED   33964939
  REMARK    GeneRIF: CircASH2L facilitates tumor-like biologic behaviours and
            inflammation of fibroblast-like synoviocytes via miR-129-5p/HIPK2
            axis in rheumatoid arthritis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Hughes,C.M., Rozenblatt-Rosen,O., Milne,T.A., Copeland,T.D.,
            Levine,S.S., Lee,J.C., Hayes,D.N., Shanmugam,K.S.,
            Bhattacharjee,A., Biondi,C.A., Kay,G.F., Hayward,N.K., Hess,J.L.
            and Meyerson,M.
  TITLE     Menin associates with a trithorax family histone methyltransferase
            complex and with the hoxc8 locus
  JOURNAL   Mol Cell 13 (4), 587-597 (2004)
   PUBMED   14992727
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Wysocka,J., Myers,M.P., Laherty,C.D., Eisenman,R.N. and Herr,W.
  TITLE     Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone
            H3-K4 methyltransferase are tethered together selectively by the
            cell-proliferation factor HCF-1
  JOURNAL   Genes Dev 17 (7), 896-911 (2003)
   PUBMED   12670868
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Wang,J., Zhou,Y., Yin,B., Du,G., Huang,X., Li,G., Shen,Y., Yuan,J.
            and Qiang,B.
  TITLE     ASH2L: alternative splicing and downregulation during induced
            megakaryocytic differentiation of multipotential leukemia cell
            lines
  JOURNAL   J Mol Med (Berl) 79 (7), 399-405 (2001)
   PUBMED   11466562
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Ikegawa,S., Isomura,M., Koshizuka,Y. and Nakamura,Y.
  TITLE     Cloning and characterization of ASH2L and Ash2l, human and mouse
            homologs of the Drosophila ash2 gene
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 167-172 (1999)
   PUBMED   10393421
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA156139.1, BC015936.2 and AC084024.17.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (b) has a shorter N-terminus, compared to isoform
            a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.87010.1,
                                           SRR1803611.234285.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..534
                     /product="set1/Ash2 histone methyltransferase complex
                     subunit ASH2 isoform b"
                     /note="set1/Ash2 histone methyltransferase complex subunit
                     ASH2; ASH2-like protein; ash2 (absent, small, or
                     homeotic)-like"
                     /calculated_mol_wt=60077
     Region          7..56
                     /region_name="PHD_ash2p_like"
                     /note="PHD finger found in Schizosaccharomyces pombe Set1
                     complex component ash2 (spAsh2p) and similar proteins;
                     cd15583"
                     /db_xref="CDD:277058"
     Site            order(7,19..23,27,51)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277058"
     Region          298..489
                     /region_name="SPRY_Ash2"
                     /note="SPRY domain in Ash2; cd12872"
                     /db_xref="CDD:293932"
     CDS             1..534
                     /gene="ASH2L"
                     /gene_synonym="ASH2; ASH2L1; ASH2L2; Bre2"
                     /coded_by="NM_001105214.2:442..2046"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47840.1"
                     /db_xref="GeneID:9070"
                     /db_xref="HGNC:HGNC:744"
                     /db_xref="MIM:604782"
ORIGIN      
        1 mdtqagsvde engrqlgeve lqcgictkwf tadtfgidts sclpfmtnys fhcnvchhsg
       61 ntyflrkqan lkemclsala nltwqsrtqd ehpktmfskd kdiipfidky wecmttrqrp
      121 gkmtwpnniv ktmskerdvf lvkehpdpgs kdpeedypkf glldqdlsni gpaydnqkqs
      181 savstsgnln ggiaagssgk grgakrkqqd ggttgttkka rsdplfsaqr lpphgypleh
      241 pfnkdgyryi laepdphapd pekleldcwa gkpipgdlyr aclyervlla lhdrapqlki
      301 sddrltvvge kgysmvrash gvrkgawyfe itvdemppdt aarlgwsqpl gnlqaplgyd
      361 kfsyswrskk gtkfhqsigk hyssgygqgd vlgfyinlpe dtetakslpd tykdkalikf
      421 ksylyfeekd fvdkaekslk qtphseiify kngvnqgvay kdifegvyfp aislyksctv
      481 sinfgpcfky ppkdltyrpm sdmgwgavve htladvlyhv etevdgrrsp pwep
//
LOCUS       NP_579812                253 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin alpha Fc receptor isoform h [Homo sapiens].
ACCESSION   NP_579812
VERSION     NP_579812.1
DBSOURCE    REFSEQ: accession NM_133278.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Liu,Q. and Stadtmueller,B.M.
  TITLE     SIgA structures bound to Streptococcus pyogenes M4 and human CD89
            provide insights into host-pathogen interactions
  JOURNAL   Nat Commun 14 (1), 6726 (2023)
   PUBMED   37872175
  REMARK    GeneRIF: SIgA structures bound to Streptococcus pyogenes M4 and
            human CD89 provide insights into host-pathogen interactions.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Wu,H., Wang,X., Yang,Z., Zhao,Q., Wen,Y., Li,X., Zhang,W. and
            Gao,R.
  TITLE     Serum Soluble CD89-IgA Complexes Are Elevated in IgA Nephropathy
            without Immunosuppressant History
  JOURNAL   Dis Markers 2020, 8393075 (2020)
   PUBMED   32076466
  REMARK    GeneRIF: Serum Soluble CD89-IgA Complexes Are Elevated in IgA
            Nephropathy without Immunosuppressant History.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Pleass,R.J., Andrews,P.D., Kerr,M.A. and Woof,J.M.
  TITLE     Alternative splicing of the human IgA Fc receptor CD89 in
            neutrophils and eosinophils
  JOURNAL   Biochem J 318 (Pt 3) (Pt 3), 771-777 (1996)
   PUBMED   8836118
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Patry,C., Sibille,Y., Lehuen,A. and Monteiro,R.C.
  TITLE     Identification of Fc alpha receptor (CD89) isoforms generated by
            alternative splicing that are differentially expressed between
            blood monocytes and alveolar macrophages
  JOURNAL   J Immunol 156 (11), 4442-4448 (1996)
   PUBMED   8666819
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Morton,H.C., Schiel,A.E., Janssen,S.W. and van de Winkel,J.G.
  TITLE     Alternatively spliced forms of the human myeloid Fc alpha receptor
            (CD89) in neutrophils
  JOURNAL   Immunogenetics 43 (4), 246-247 (1996)
   PUBMED   8575829
REFERENCE   7  (residues 1 to 253)
  AUTHORS   de Wit,T.P., Morton,H.C., Capel,P.J. and van de Winkel,J.G.
  TITLE     Structure of the gene for the human myeloid IgA Fc receptor (CD89)
  JOURNAL   J Immunol 155 (3), 1203-1209 (1995)
   PUBMED   7636188
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Kremer,E.J., Kalatzis,V., Baker,E., Callen,D.F., Sutherland,G.R.
            and Maliszewski,C.R.
  TITLE     The gene for the human IgA Fc receptor maps to 19q13.4
  JOURNAL   Hum Genet 89 (1), 107-108 (1992)
   PUBMED   1577457
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Maliszewski,C.R., March,C.J., Schoenborn,M.A., Gimpel,S. and
            Shen,L.
  TITLE     Expression cloning of a human Fc receptor for IgA
  JOURNAL   J Exp Med 172 (6), 1665-1672 (1990)
   PUBMED   2258698
REFERENCE   10 (residues 1 to 253)
  AUTHORS   Kimata,H. and Saxon,A.
  TITLE     Subset of natural killer cells is induced by immune complexes to
            display Fc receptors for IgE and IgA and demonstrates isotype
            regulatory function
  JOURNAL   J Clin Invest 82 (1), 160-167 (1988)
   PUBMED   2455732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290922.1, X92559.1 and
            AC245128.3.
            
            Summary: This gene is a member of the immunoglobulin gene
            superfamily and encodes a receptor for the Fc region of IgA. The
            receptor is a transmembrane glycoprotein present on the surface of
            myeloid lineage cells such as neutrophils, monocytes, macrophages,
            and eosinophils, where it mediates immunologic responses to
            pathogens. It interacts with IgA-opsonized targets and triggers
            several immunologic defense processes, including phagocytosis,
            antibody-dependent cell-mediated cytotoxicity, and stimulation of
            the release of inflammatory mediators. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (8, also known as deltaS266Ec2 or
            U13) lacks an in-frame exon in the 5' coding region and uses an
            alternate in-frame splice site in the 3' coding region, compared to
            variant 1. The encoded isoform (h) is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X92559.1, D87862.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..253
                     /product="immunoglobulin alpha Fc receptor isoform h"
                     /note="immunoglobulin alpha Fc receptor; Fc fragment of
                     IgA, receptor for; Fc fragment of IgA receptor"
                     /calculated_mol_wt=28212
     Region          16..107
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          17..21
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          25..28
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          31..38
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          45..50
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(49,89,96)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          60..63
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          72..76
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          84..90
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          100..107
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          113..>185
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          130..134
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          143..147
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          164..168
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..183
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..253
                     /gene="FCAR"
                     /gene_synonym="CD89; CTB-61M7.2; FcalphaR; FcalphaRI"
                     /coded_by="NM_133278.4:56..817"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS42623.1"
                     /db_xref="GeneID:2204"
                     /db_xref="HGNC:HGNC:3608"
                     /db_xref="MIM:147045"
ORIGIN      
        1 mdpkqttllc lgdfpmpfis aksspvipld gsvkiqcqai reayltqlmi iknstyreig
       61 rrlkfwnetd pefvidhmda nkagryqcqy righyrfrys dtlelvvtgl ygkpflsadr
      121 glvlmpgeni sltcssahip fdrfslakeg elslpqhqsg ehpanfslgp vdlnvsgiyr
      181 cydsihqdyt tqnlirmava glvlvallai lvenwhshta lnkeasadva epswsqqmcq
      241 pgltfartps vck
//
LOCUS       NP_001307378             385 aa            linear   PRI 20-NOV-2025
DEFINITION  protein spinster homolog 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001307378 XP_011522029
VERSION     NP_001307378.1
DBSOURCE    REFSEQ: accession NM_001320449.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Eshibona,N., Giwa,A., Rossouw,S.C., Gamieldien,J., Christoffels,A.
            and Bendou,H.
  TITLE     Upregulation of FHL1, SPNS3, and MPZL2 predicts poor prognosis in
            pediatric acute myeloid leukemia patients with FLT3-ITD mutation
  JOURNAL   Leuk Lymphoma 63 (8), 1897-1906 (2022)
   PUBMED   35249471
  REMARK    GeneRIF: Upregulation of FHL1, SPNS3, and MPZL2 predicts poor
            prognosis in pediatric acute myeloid leukemia patients with
            FLT3-ITD mutation.
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Hong,Y., Tian,X., Wang,M., Chen,C. and Sun,A.
  TITLE     Bioinformatics-based identification of SPNS3 (Spinster homolog 3)
            as a prognostic biomarker of apoptosis resistance in acute myeloid
            leukemia
  JOURNAL   Bioengineered 12 (1), 7837-7848 (2021)
   PUBMED   34608834
  REMARK    GeneRIF: Bioinformatics-based identification of SPNS3 (Spinster
            homolog 3) as a prognostic biomarker of apoptosis resistance in
            acute myeloid leukemia.
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Jacobsson,J.A., Haitina,T., Lindblom,J. and Fredriksson,R.
  TITLE     Identification of six putative human transporters with structural
            similarity to the drug transporter SLC22 family
  JOURNAL   Genomics 90 (5), 595-609 (2007)
   PUBMED   17714910
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116910.11, BC023646.2 and AK172832.1.
            
            On Feb 24, 2016 this sequence version replaced XP_011522029.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region and uses a downstream start codon compared to
            variant 1. It encodes isoform 2 which has a shorter N-terminus
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023646.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..385
                     /product="protein spinster homolog 3 isoform 2"
                     /note="protein spinster homolog 3; sphingolipid
                     transporter 3 (putative); solute carrier family 63 member
                     3; SPNS sphingolipid transporter 3 (putative)"
                     /calculated_mol_wt=41208
     Region          <8..338
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(23..24,26..28,31,51,54..55,58,140,143..144,147..149,
                     152,192,196,249..250,254,258,278,281..282,285..286,289)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
     CDS             1..385
                     /gene="SPNS3"
                     /gene_synonym="SLC62A3; SLC63A3"
                     /coded_by="NM_001320449.2:273..1430"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:201305"
                     /db_xref="HGNC:HGNC:28433"
                     /db_xref="MIM:611701"
ORIGIN      
        1 mlvcfrlysw lfflsrgivg tgsasystia ptvlgdlfvr dqrtrvlavf yifipvgsgl
       61 gyvlgsavtm ltgnwrwalr vmpcleaval illillvpdp prgaaetqge gavggfrssw
      121 cedvrylgkn wsfvwstlgv tamafvtgal gfwapkflle arvvhglqpp cfqepcsnpd
      181 slifgaltim tgvigvilga eaarrykkvi pgaeplicas sllatapcly lalvlapttl
      241 lasyvflglg elllscnwav vadillsvvv prcrgtaeal qitvghilgd agspyltgli
      301 ssvlrarrpd sylqrfrslq qsflccafvi algggcfllt alylerdetr awqpvtgtpd
      361 sndvdsndle rqgllsgaga steep
//
LOCUS       NP_056280               1508 aa            linear   PRI 20-NOV-2025
DEFINITION  gem-associated protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_056280
VERSION     NP_056280.2
DBSOURCE    REFSEQ: accession NM_015465.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1508)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1508)
  AUTHORS   Zhang,J., Liu,X., Zhu,G., Wan,L., Liang,Y., Li,N., Huang,M. and
            Yang,G.
  TITLE     Expanding the clinical phenotype and genetic spectrum of GEMIN5
            disorders: Early-infantile developmental and epileptic
            encephalopathies
  JOURNAL   Brain Behav 14 (5), e3535 (2024)
   PUBMED   38773790
  REMARK    GeneRIF: Expanding the clinical phenotype and genetic spectrum of
            GEMIN5 disorders: Early-infantile developmental and epileptic
            encephalopathies.
REFERENCE   3  (residues 1 to 1508)
  AUTHORS   Cascajo-Almenara,M.V., Julia-Palacios,N., Urreizti,R.,
            Sanchez-Cuesta,A., Fernandez-Ayala,D.M., Garcia-Diaz,E., Oliva,C.,
            O Callaghan,M.D.M., Paredes-Fuentes,A.J., Moreno-Lozano,P.J.,
            Muchart,J., Nascimento,A., Ortez,C.I., Natera-de Benito,D.,
            Pineda,M., Rivera,N., Fortuna,T.R., Rajan,D.S., Navas,P.,
            Salviati,L., Palau,F., Yubero,D., Garcia-Cazorla,A., Pandey,U.B.,
            Santos-Ocana,C. and Artuch,R.
  TITLE     Mutations of GEMIN5 are associated with coenzyme Q10 deficiency:
            long-term follow-up after treatment
  JOURNAL   Eur J Hum Genet 32 (4), 426-434 (2024)
   PUBMED   38316953
  REMARK    GeneRIF: Mutations of GEMIN5 are associated with coenzyme Q10
            deficiency: long-term follow-up after treatment.
REFERENCE   4  (residues 1 to 1508)
  AUTHORS   Francisco-Velilla,R., Abellan,S., Garcia-Martin,J.A., Oliveros,J.C.
            and Martinez-Salas,E.
  TITLE     Alternative splicing events driven by altered levels of GEMIN5
            undergo translation
  JOURNAL   RNA Biol 21 (1), 23-34 (2024)
   PUBMED   39194147
  REMARK    GeneRIF: Alternative splicing events driven by altered levels of
            GEMIN5 undergo translation.
REFERENCE   5  (residues 1 to 1508)
  AUTHORS   Lee,J.H., Horak,C.E., Khanna,C., Meng,Z., Yu,L.R., Veenstra,T.D.
            and Steeg,P.S.
  TITLE     Alterations in Gemin5 expression contribute to alternative mRNA
            splicing patterns and tumor cell motility
  JOURNAL   Cancer Res 68 (3), 639-644 (2008)
   PUBMED   18245461
  REMARK    GeneRIF: The data provide the first demonstration that alterations
            in the expression of Gemin5, a spliceosome protein, can effect both
            specific splicing events and tumor cell motility.
REFERENCE   6  (residues 1 to 1508)
  AUTHORS   Fierro-Monti,I., Mohammed,S., Matthiesen,R., Santoro,R.,
            Burns,J.S., Williams,D.J., Proud,C.G., Kassem,M., Jensen,O.N. and
            Roepstorff,P.
  TITLE     Quantitative proteomics identifies Gemin5, a scaffolding protein
            involved in ribonucleoprotein assembly, as a novel partner for
            eukaryotic initiation factor 4E
  JOURNAL   J Proteome Res 5 (6), 1367-1378 (2006)
   PUBMED   16739988
REFERENCE   7  (residues 1 to 1508)
  AUTHORS   Yong,J., Wan,L. and Dreyfuss,G.
  TITLE     Why do cells need an assembly machine for RNA-protein complexes?
  JOURNAL   Trends Cell Biol 14 (5), 226-232 (2004)
   PUBMED   15130578
  REMARK    Review article
REFERENCE   8  (residues 1 to 1508)
  AUTHORS   Paushkin,S., Gubitz,A.K., Massenet,S. and Dreyfuss,G.
  TITLE     The SMN complex, an assemblyosome of ribonucleoproteins
  JOURNAL   Curr Opin Cell Biol 14 (3), 305-312 (2002)
   PUBMED   12067652
  REMARK    Review article
REFERENCE   9  (residues 1 to 1508)
  AUTHORS   Gubitz,A.K., Mourelatos,Z., Abel,L., Rappsilber,J., Mann,M. and
            Dreyfuss,G.
  TITLE     Gemin5, a novel WD repeat protein component of the SMN complex that
            binds Sm proteins
  JOURNAL   J Biol Chem 277 (7), 5631-5636 (2002)
   PUBMED   11714716
  REMARK    GeneRIF: we report the identification of an additional component of
            the SMN complex, a novel WD repeat protein termed Gemin5. Gemin5
            binds SMN directly and is a component of the SMN complex
REFERENCE   10 (residues 1 to 1508)
  AUTHORS   Sleeman,J.E. and Lamond,A.I.
  TITLE     Newly assembled snRNPs associate with coiled bodies before
            speckles, suggesting a nuclear snRNP maturation pathway
  JOURNAL   Curr Biol 9 (19), 1065-1074 (1999)
   PUBMED   10531003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA400244.1, BC036894.1,
            BC014147.2, BX329222.2, AK074066.2, AL117665.1 and AC008421.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 28, 2007 this sequence version replaced NP_056280.1.
            
            Summary: This gene encodes a WD repeat protein that is a component
            of the survival of motor neurons (SMN) complex. The SMN complex
            plays a critical role in mRNA splicing through the assembly of
            spliceosomal small nuclear ribonucleoproteins (snRNPs), and may
            also mediate the assembly and transport of other classes of
            ribonucleoproteins. The encoded protein is the snRNA-binding
            component of the SMN complex. Dysregulation of this gene may play a
            role in alternative mRNA splicing and tumor cell motility.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Nov
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074066.2, BC113614.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285873.8/ ENSP00000285873.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..1508
                     /product="gem-associated protein 5 isoform 1"
                     /calculated_mol_wt=168459
     Region          1..124
                     /region_name="Important for interaction with U1 snRNA.
                     /evidence=ECO:0000269|PubMed:19377484"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          13..15
                     /region_name="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
                     ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            33
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
                     ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L; propagated
                     from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          55..456
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          68..107
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..148
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          112..149
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          150..189
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          154..193
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          193..264
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          228..279
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          280..321
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            284
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K;
                     propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          288..325
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          331..377
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          333..374
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            335
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K;
                     propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          <348..710
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Site            359
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5GXI, ECO:0007744|PDB:5H1K,
                     ECO:0007744|PDB:5H1L; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          377..417
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            381
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5GXI,
                     ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1L; propagated
                     from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          382..422
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            422
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0007744|PDB:5H1K;
                     propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          424..464
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            426
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5H1K; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          429..468
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          468..509
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            470
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5H1K; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          474..538
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            474
                     /site_type="other"
                     /note="Interaction with U4 snRNA and with the
                     7-methylguanosine cap of RNA molecules.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
                     ECO:0007744|PDB:5H1M, ECO:0007744|PDB:5TEF; propagated
                     from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          533..573
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          542..575
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            556
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5H1K; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          576..622
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            579
                     /site_type="other"
                     /note="Interaction with U4 snRNA.
                     /evidence=ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5H1K; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          582..636
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          637..677
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            641
                     /site_type="other"
                     /note="Interaction with U4 snRNA and with the
                     7-methylguanosine cap of RNA molecules.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
                     ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5TEF; propagated
                     from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          642..679
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            660
                     /site_type="other"
                     /note="Interaction with U4 snRNA and with the
                     7-methylguanosine cap of RNA molecules.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881601, ECO:0000269|Ref.27,
                     ECO:0007744|PDB:5H1K, ECO:0007744|PDB:5H1M,
                     ECO:0007744|PDB:5TEF; propagated from UniProtKB/Swiss-Prot
                     (Q8TEQ6.3)"
     Region          680..720
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            684
                     /site_type="other"
                     /note="Interaction with U4 snRNA and with the
                     7-methylguanosine cap of RNA molecules.
                     /evidence=ECO:0000269|PubMed:27834343,
                     ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601,
                     ECO:0007744|PDB:5GXH, ECO:0007744|PDB:5H1K; propagated
                     from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          685..722
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          715..790
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Site            847
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          1313..1343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     Region          1389..1428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ6.3)"
     CDS             1..1508
                     /gene="GEMIN5"
                     /gene_synonym="GEMIN-5; NEDCAM"
                     /coded_by="NM_015465.5:79..4605"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4330.1"
                     /db_xref="GeneID:25929"
                     /db_xref="HGNC:HGNC:20043"
                     /db_xref="MIM:607005"
ORIGIN      
        1 mgqeprtlpp spnwycarcs davpgglfgf aartsvflvr vgpgagespg tppfrvigel
       61 vghtervsgf tfshhpgqyn lcatssddgt vkiwdvetkt vvtehalhqh tistlhwspr
      121 vkdlivsgde kgvvfcywfn rndsqhlfie prtifcltcs phhedlvaig ykdgivviid
      181 iskkgevihr lrghddeihs iawcplpged clsinqeets eeaeitngna vaqapvtkgc
      241 ylatgskdqt iriwscsrgr gvmilklpfl krrgggidpt vkerlwltlh wpsnqptqlv
      301 sscfggellq wdltqswrrk ytlfsasseg qnhsrivfnl cplqteddkq lllstsmdrd
      361 vkcwdiatle cswtlpslgg fayslafssv digslaigvg dgmirvwntl siknnydvkn
      421 fwqgvkskvt alcwhptkeg clafgtddgk vglydtysnk ppqisstyhk ktvytlawgp
      481 pvppmslgge gdrpslalys cggegivlqh npwklsgeaf dinklirdtn sikyklpvht
      541 eiswkadgki malgnedgsi eifqipnlkl ictiqqhhkl vntiswhheh gsqpelsylm
      601 asgsnnaviy vhnlktvies spespvtite pyrtlsghta kitsvawsph hdgrlvsasy
      661 dgtaqvwdal reeplcnfrg hrgrllcvaw spldpdciys gaddfcvhkw ltsmqdhsrp
      721 pqgkksiele kkrlsqpkak pkkkkkptlr tpvklesidg neeesmkens gpvengvsdq
      781 egeeqarepe lpcglapavs repvictpvs sgfekskvti nnkvillkke ppkekpetli
      841 kkrkarsllp lstsldhrsk eelhqdclvl atakhsreln edvsadveer fhlglftdra
      901 tlyrmidieg kghlenghpe lfhqlmlwkg dlkgvlqtaa ergeltdnlv amapaagyhv
      961 wlwaveafak qlcfqdqyvk aashllsihk vyeavellks nhfyreaiai akarlrpedp
     1021 vlkdlylswg tvlerdghya vaakcylgat caydaakvla kkgdaaslrt aaelaaivge
     1081 delsaslalr caqelllann wvgaqealql heslqgqrlv fcllellsrh leekqlsegk
     1141 ssssyhtwnt gtegpfverv tavwksifsl dtpeqyqeaf qklqnikyps atnntpakql
     1201 llhichdltl avlsqqmasw deavqallra vvrsydsgsf timqevysaf lpdgcdhlrd
     1261 klgdhqspat pafksleaff lygrlyefww slsrpcpnss vwvraghrtl svepsqqldt
     1321 asteetdpet sqpepnrpse ldlrlteege rmlstfkelf sekhaslqns qrtvaevqet
     1381 laemirqhqk sqlckstang pdknepevea eqplcssqsq ckeeknepls lpeltkrlte
     1441 anqrmakfpe sikawpfpdv lecclvllli rshfpgclaq emqqqaqell qkygntktyr
     1501 rhcqtfcm
//
LOCUS       NP_001308439             287 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-10 isoform 16 [Homo sapiens].
ACCESSION   NP_001308439
VERSION     NP_001308439.1
DBSOURCE    REFSEQ: accession NM_001321510.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352441.450657.1,
                                           SRR14038195.684855.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..287
                     /product="septin-10 isoform 16"
                     /calculated_mol_wt=33341
     Region          <32..164
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            41..44
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            95..97
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..287
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321510.2:140..1003"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 massevarhl lfqshmatkt tcmssqgsdd eqivniipvi akadtvskte lqkfkiklms
       61 elvsngvqiy qfptdddtia kvnaamngql pfavvgsmde vkvgnkmvka rqypwgvvqv
      121 enenhcdfvk lremlictnm edlreqthtr hyelyrrckl eemgftdvgp enkpvsvqet
      181 yeakrhefhg erqrkeeemk qmfvqrvkek eailkeaere lqakfehlkr lhqeermkle
      241 ekrrlleeei iafskkkats eifhsqsfla tgsnlrkdkd rknsnfl
//
LOCUS       NP_057213                406 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 4 isoform 1 [Homo sapiens].
ACCESSION   NP_057213
VERSION     NP_057213.2
DBSOURCE    REFSEQ: accession NM_016129.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Cohen,H., Azriel,A., Cohen,T., Meraro,D., Hashmueli,S.,
            Bech-Otschir,D., Kraft,R., Dubiel,W. and Levi,B.Z.
  TITLE     Interaction between interferon consensus sequence-binding protein
            and COP9/signalosome subunit CSN2 (Trip15). A possible link between
            interferon regulatory factor signaling and the COP9/signalosome
  JOURNAL   J Biol Chem 275 (50), 39081-39089 (2000)
   PUBMED   10991940
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Naumann,M., Bech-Otschir,D., Huang,X., Ferrell,K. and Dubiel,W.
  TITLE     COP9 signalosome-directed c-Jun activation/stabilization is
            independent of JNK
  JOURNAL   J Biol Chem 274 (50), 35297-35300 (1999)
   PUBMED   10585392
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001148.1, BC004302.1 and
            BC009292.2.
            
            On Nov 18, 2003 this sequence version replaced NP_057213.1.
            
            Summary: This gene encodes one of eight subunits composing COP9
            signalosome, a highly conserved protein complex that functions as
            an important regulator in multiple signaling pathways. The
            structure and function of COP9 signalosome is similar to that of
            the 19S regulatory particle of 26S proteasome. COP9 signalosome has
            been shown to interact with SCF-type E3 ubiquitin ligases and act
            as a positive regulator of E3 ubiquitin ligases. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005665.1, SRR3476690.835033.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264389.7/ ENSP00000264389.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..406
                     /product="COP9 signalosome complex subunit 4 isoform 1"
                     /note="COP9 signalosome complex subunit 4; signalosome
                     subunit 4; JAB1-containing signalosome subunit 4; COP9
                     constitutive photomorphogenic homolog subunit 4; COP9
                     constitutive photomorphogenic-like protein subunit 4;
                     testis tissue sperm-binding protein Li 42a"
                     /calculated_mol_wt=46138
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:18850735,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9BT78.1)"
     Site            25
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BT78.1)"
     Region          <71..377
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     Region          264..362
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Region          365..406
                     /region_name="CSN4_RPN5_eIF3a"
                     /note="CSN4/RPN5/eIF3a helix turn helix domain; pfam18420"
                     /db_xref="CDD:375846"
     CDS             1..406
                     /gene="COPS4"
                     /gene_synonym="CSN4; SGN4"
                     /coded_by="NM_016129.3:43..1263"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3600.1"
                     /db_xref="GeneID:51138"
                     /db_xref="HGNC:HGNC:16702"
                     /db_xref="MIM:616008"
ORIGIN      
        1 maaavrqdla qlmnssgshk dlagkyrqil ekaiqlsgae qlealkafve amvnenvslv
       61 isrqlltdfc thlpnlpdst akeiyhftle kiqprvisfe eqvasirqhl asiyekeedw
      121 rnaaqvlvgi pletgqkqyn vdykletylk iarlyleddd pvqaeayinr asllqnestn
      181 eqlqihykvc yarvldyrrk fieaaqryne lsyktivhes erlealkhal hctilasagq
      241 qrsrmlatlf kdercqqlaa ygilekmyld riirgnqlqe faamlmphqk attadgssil
      301 draviehnll sasklynnit feelgallei paakaekias qmitegrmng fidqidgivh
      361 fetrealptw dkqiqslcfq vnnllekisq tapewtaqam eaqmaq
//
LOCUS       NP_001354633             789 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ooo [Homo sapiens].
ACCESSION   NP_001354633
VERSION     NP_001354633.1
DBSOURCE    REFSEQ: accession NM_001367704.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 789)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 789)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 789)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 789)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 789)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 789)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 789)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 789)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 789)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 789)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..789
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..789
                     /product="SUN domain-containing protein 1 isoform ooo"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=87416
     Region          62..295
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          421..474
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(421,424..425,428,431..432,435..436,438..439,
                     442..443,445..446,449..450,452..453,456,459..460,463,
                     466..467,470..471,473..474)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          433..>566
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          551..609
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          652..787
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..789
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367704.1:52..2421"
                     /note="isoform ooo is encoded by transcript variant 67"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld ahtaahsqsp
      241 rlpgragtlw hiwacagkaa sgvfwwlgig wyqfvtlisw lnvflltrcl rnickflvll
      301 iplflllagl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl kqplqgdsea
      361 fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag psasvrdavg
      421 qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa vgeqllptve
      481 hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq ggsleqllqr
      541 fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag asgiteaqar
      601 aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi plwyfsqspr
      661 vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni ssapkdfavy
      721 gleneyqeeg qllgqftydq dgeslqmfqa lkrpddtafq ivelrifsnw ghpeytclyr
      781 frvhgepvk
//
LOCUS       NP_001357117             662 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor beta activator LRRC32 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001357117 XP_016873016
VERSION     NP_001357117.1
DBSOURCE    REFSEQ: accession NM_001370188.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Ma,J., Chen,Y., Li,T., Cao,Y., Hu,B., Liu,Y., Zhang,Y., Li,X.,
            Liu,J., Zhang,W., Niu,H., Gao,J., Zhang,Z., Yue,K., Wang,J.,
            Bao,G., Wang,C., Wang,P.G., Zou,T. and Xie,S.
  TITLE     Suppression of lysosome metabolism-meditated GARP/TGF-beta1
            complexes specifically depletes regulatory T cells to inhibit
            breast cancer metastasis
  JOURNAL   Oncogene 43 (25), 1930-1940 (2024)
   PUBMED   38698265
  REMARK    GeneRIF: Suppression of lysosome metabolism-meditated
            GARP/TGF-beta1 complexes specifically depletes regulatory T cells
            to inhibit breast cancer metastasis.
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Zhang,X., Sharma,P., Maschmeyer,P., Hu,Y., Lou,M., Kim,J.,
            Fujii,H., Unutmaz,D., Schwabe,R.F. and Winau,F.
  TITLE     GARP on hepatic stellate cells is essential for the development of
            liver fibrosis
  JOURNAL   J Hepatol 79 (5), 1214-1225 (2023)
   PUBMED   37348791
  REMARK    GeneRIF: GARP on hepatic stellate cells is essential for the
            development of liver fibrosis.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Cai,H., Liu,Y., Dong,X., Jiang,F., Li,H., Ouyang,S., Yin,W., He,T.,
            Zeng,Q. and Yang,H.
  TITLE     Analysis of LAP+ and GARP+ Treg subsets in peripheral blood of
            patients with neuromyelitis optica spectrum disorders
  JOURNAL   Neurol Sci 44 (5), 1739-1747 (2023)
   PUBMED   36683084
  REMARK    GeneRIF: Analysis of LAP[+] and GARP[+] Treg subsets in peripheral
            blood of patients with neuromyelitis optica spectrum disorders.
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Lahimchi,M.R., Eslami,M. and Yousefi,B.
  TITLE     New insight into GARP striking role in cancer progression:
            application for cancer therapy
  JOURNAL   Med Oncol 40 (1), 33 (2022)
   PUBMED   36460874
  REMARK    GeneRIF: New insight into GARP striking role in cancer progression:
            application for cancer therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Maire,G., Forus,A., Foa,C., Bjerkehagen,B., Mainguene,C.,
            Kresse,S.H., Myklebost,O. and Pedeutour,F.
  TITLE     11q13 alterations in two cases of hibernoma: large heterozygous
            deletions and rearrangement breakpoints near GARP in 11q13.5
  JOURNAL   Genes Chromosomes Cancer 37 (4), 389-395 (2003)
   PUBMED   12800150
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Roubin,R., Pizette,S., Ollendorff,V., Planche,J., Birnbaum,D. and
            Delapeyriere,O.
  TITLE     Structure and developmental expression of mouse Garp, a gene
            encoding a new leucine-rich repeat-containing protein
  JOURNAL   Int J Dev Biol 40 (3), 545-555 (1996)
   PUBMED   8840187
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Ollendorff,V., Noguchi,T., deLapeyriere,O. and Birnbaum,D.
  TITLE     The GARP gene encodes a new member of the family of leucine-rich
            repeat-containing proteins
  JOURNAL   Cell Growth Differ 5 (2), 213-219 (1994)
   PUBMED   8180135
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Ollendorff,V., Szepetowski,P., Mattei,M.G., Gaudray,P. and
            Birnbaum,D.
  TITLE     New gene in the homologous human 11q13-q14 and mouse 7F chromosomal
            regions
  JOURNAL   Mamm Genome 2 (3), 195-200 (1992)
   PUBMED   1543912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001189.5 and KF455417.1.
            
            On May 2, 2019 this sequence version replaced XP_016873016.1.
            
            Summary: This gene encodes a type I membrane protein which contains
            20 leucine-rich repeats. Alterations in the chromosomal region
            11q13-11q14 are involved in several pathologies. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4), as well as variants 1, 2, and
            3, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.215971.1,
                                           DRR138528.307771.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..662
                     /product="transforming growth factor beta activator LRRC32
                     isoform a precursor"
                     /note="garpin; glycoprotein A repetitions predominant;
                     leucine-rich repeat-containing protein 32; transforming
                     growth factor beta activator LRRC32"
                     /calculated_mol_wt=70148
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1849
     Region          19..277
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     mat_peptide     20..662
                     /product="Transforming growth factor beta activator
                     LRRC32. /id=PRO_0000021615"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
                     /calculated_mol_wt=69949
     Site            order(28,31,33,36,38,51,54,56,59,61,75,78,80,83,85,99,102,
                     104,107,109,126,129,131,134,136,151,154,156,159,161,175,
                     178,180,183,185,199,202,204,207,209,220,223,225,228,230,
                     245,248,250,253,255,267,270,272,275,277)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          31..50
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(34..35,82,133,158,206,224,226,249,271)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          50..73
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          51..74
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          74..95
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          75..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          98..119
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          99..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          125..145
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          126..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="LRR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..219
                     /region_name="LRR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          199..219
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          220..244
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..240
                     /region_name="LRR 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          244..265
                     /region_name="LRR 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          245..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          266..286
                     /region_name="LRR 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          290..>574
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          316..339
                     /region_name="LRR 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          317..340
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          340..363
                     /region_name="LRR 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          341..364
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          364..385
                     /region_name="LRR 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          365..387
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          387..408
                     /region_name="LRR 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          388..411
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          411..432
                     /region_name="LRR 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          412..444
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          444..465
                     /region_name="LRR 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          445..463
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          467..488
                     /region_name="LRR 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          468..492
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          492..513
                     /region_name="LRR 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          493..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <496..654
                     /region_name="PLN03150"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:178695"
     Region          515..536
                     /region_name="LRR 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          516..537
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          537..558
                     /region_name="LRR 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          538..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          563..575
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            628..648
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     CDS             1..662
                     /gene="LRRC32"
                     /gene_synonym="CPPRDD; D11S833E; GARP"
                     /coded_by="NM_001370188.1:182..2170"
                     /note="isoform a precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS8245.1"
                     /db_xref="GeneID:2615"
                     /db_xref="HGNC:HGNC:4161"
                     /db_xref="MIM:137207"
ORIGIN      
        1 mrpqilllla lltlglaaqh qdkvpckmvd kkvscqvlgl lqvpsvlppd tetldlsgnq
       61 lrsilasplg fytalrhldl stneisflqp gafqalthle hlslahnrla matalsaggl
      121 gplprvtsld lsgnslysgl lerllgeaps lhtlslaens ltrltrhtfr dmpaleqldl
      181 hsnvlmdied gafeglprlt hlnlsrnslt cisdfslqql rvldlscnsi eafqtasqpq
      241 aefqltwldl renkllhfpd laalprliyl nlsnnlirlp tgppqdskgi hapsegwsal
      301 plsapsgnas grplsqllnl dlsyneieli pdsflehlts lcflnlsrnc lrtfearrlg
      361 slpclmlldl shnaletlel garalgslrt lllqgnalrd lppytfanla slqrlnlqgn
      421 rvspcggpde pgpsgcvafs gitslrslsl vdneiellra gaflhtplte ldlssnpgle
      481 vatgalggle aslevlalqg nglmvlqvdl pcficlkrln laenrlshlp awtqavslev
      541 ldlrnnsfsl lpgsamggle tslrrlylqg nplsccgngw laaqlhqgrv dvdatqdlic
      601 rfssqeevsl shvrpedcek gglkninlii iltfilvsai llttlaaccc vrrqkfnqqy
      661 ka
//
LOCUS       NP_001271319             295 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription cofactor vestigial-like protein 4 isoform e [Homo
            sapiens].
ACCESSION   NP_001271319 XP_005265666
VERSION     NP_001271319.1
DBSOURCE    REFSEQ: accession NM_001284390.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Wang,Z., Quan,Y., Hu,M., Xu,Y., Chen,Y., Jin,P., Ma,J., Chen,X.,
            Fan,J., Fan,X., Gong,Y., Li,M. and Wang,Y.
  TITLE     VGLL4-TEAD1 promotes vascular smooth muscle cell differentiation
            from human pluripotent stem cells via TET2
  JOURNAL   J Mol Cell Cardiol 176, 21-32 (2023)
   PUBMED   36657637
  REMARK    GeneRIF: VGLL4-TEAD1 promotes vascular smooth muscle cell
            differentiation from human pluripotent stem cells via TET2.
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Geng,H., Liu,G., Hu,J., Li,J., Wang,D., Zou,S. and Xu,X.
  TITLE     HOXB13 suppresses proliferation, migration and invasion, and
            promotes apoptosis of gastric cancer cells through transcriptional
            activation of VGLL4 to inhibit the involvement of TEAD4 in the
            Hippo signaling pathway
  JOURNAL   Mol Med Rep 24 (4) (2021)
   PUBMED   34396425
  REMARK    GeneRIF: HOXB13 suppresses proliferation, migration and invasion,
            and promotes apoptosis of gastric cancer cells through
            transcriptional activation of VGLL4 to inhibit the involvement of
            TEAD4 in the Hippo signaling pathway.
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Mesrouze,Y., Meyerhofer,M., Zimmermann,C., Fontana,P., Erdmann,D.
            and Chene,P.
  TITLE     Biochemical properties of VGLL4 from Homo sapiens and Tgi from
            Drosophila melanogaster and possible biological implications
  JOURNAL   Protein Sci 30 (9), 1871-1881 (2021)
   PUBMED   34075638
  REMARK    GeneRIF: Biochemical properties of VGLL4 from Homo sapiens and Tgi
            from Drosophila melanogaster and possible biological implications.
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Mickle,M., Adhikary,G., Shrestha,S., Xu,W. and Eckert,R.L.
  TITLE     VGLL4 inhibits YAP1/TEAD signaling to suppress the epidermal
            squamous cell carcinoma cancer phenotype
  JOURNAL   Mol Carcinog 60 (7), 497-507 (2021)
   PUBMED   34004031
  REMARK    GeneRIF: VGLL4 inhibits YAP1/TEAD signaling to suppress the
            epidermal squamous cell carcinoma cancer phenotype.
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Jin,H.S., Park,H.S., Shin,J.H., Kim,D.H., Jun,S.H., Lee,C.J. and
            Lee,T.H.
  TITLE     A novel inhibitor of apoptosis protein (IAP)-interacting protein,
            Vestigial-like (Vgl)-4, counteracts apoptosis-inhibitory function
            of IAPs by nuclear sequestration
  JOURNAL   Biochem Biophys Res Commun 412 (3), 454-459 (2011)
   PUBMED   21839727
  REMARK    GeneRIF: Vgl-4 may play a role in the apoptotic pathways by
            regulating translocation of IAPs between different cell
            compartments.
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Teng,A.C., Kuraitis,D., Deeke,S.A., Ahmadi,A., Dugan,S.G.,
            Cheng,B.L., Crowson,M.G., Burgon,P.G., Suuronen,E.J., Chen,H.H. and
            Stewart,A.F.
  TITLE     IRF2BP2 is a skeletal and cardiac muscle-enriched
            ischemia-inducible activator of VEGFA expression
  JOURNAL   FASEB J 24 (12), 4825-4834 (2010)
   PUBMED   20702774
  REMARK    GeneRIF: IRF2BP2 was identifies as a novel VGLL4 partner.
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Chen,H.H., Mullett,S.J. and Stewart,A.F.
  TITLE     Vgl-4, a novel member of the vestigial-like family of transcription
            cofactors, regulates alpha1-adrenergic activation of gene
            expression in cardiac myocytes
  JOURNAL   J Biol Chem 279 (29), 30800-30806 (2004)
   PUBMED   15140898
  REMARK    GeneRIF: Vgl-4 modulates the activity of TEF-1 factors and
            counteracts alpha1-adrenergic activation of gene expression in
            cardiac myocytes
            GeneRIF: A transcriptional cofactor of transcriptional enhancer
            factor-1 (TEF-1) transcription factors.  Interacts with TEF-1
            factors through 2 TDU (tondu) motifs.  Controls gene expression in
            cardiac myocytes.
            GeneRIF: This gene is named Vestigial-like 4, to distinguish it
            from 3 previously described genes Vgl-1, Vgl-2 and Vgl-3. Contains
            2 motifs, found in the Drosophila transcription cofactor Vestigial,
            that interact with the TEF-1 family of transcription factors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000763.2, DA383197.1, D50911.3 and BU682809.1.
            
            On Oct 1, 2013 this sequence version replaced XP_005265666.1.
            
            Transcript Variant: This variant (5) contains alternate 5' exon
            structure and it thus differs in the 5' UTR and 5' coding region,
            compared to variant 1. The encoded isoform (e) has a distinct
            N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.192725.1,
                                           SRR1660805.334196.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3-p25.2"
     Protein         1..295
                     /product="transcription cofactor vestigial-like protein 4
                     isoform e"
                     /note="Vestigial-like 4; transcription cofactor
                     vestigial-like protein 4; vestigial like 4"
                     /calculated_mol_wt=31474
     Region          27..229
                     /region_name="VGLL4"
                     /note="Transcription cofactor vestigial-like protein 4;
                     pfam15245"
                     /db_xref="CDD:464585"
     Region          239..254
                     /region_name="TDU"
                     /note="Short repeats in human TONDU, fly vestigial and
                     other proteins; smart00711"
                     /db_xref="CDD:197839"
     CDS             1..295
                     /gene="VGLL4"
                     /gene_synonym="VGL-4"
                     /coded_by="NM_001284390.2:278..1165"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS68343.1"
                     /db_xref="GeneID:9686"
                     /db_xref="HGNC:HGNC:28966"
                     /db_xref="MIM:618692"
ORIGIN      
        1 mtenthfdki pescalkswr hpglhhgeaa lrgepriqtl pvasalsshr tgpppispsk
       61 rkfsmepgde dldcdndhvs kmsrifnphl nktangdcrr dprersrspi eravaptmsl
      121 hgshlytslp slgleqplal tknsldasrp aglsptltpg erqqnrpsvi tcasagarnc
      181 nlshcpiahs gcaapgpasy rrppsaattc dpvveehfrr slgknykepe papnsvsitg
      241 svddhfakal gdtwlqikaa kdgassspes asrrgqpasp sahmvshshs psvvs
//
LOCUS       NP_000823                885 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 1 isoform GluN1-4a precursor
            [Homo sapiens].
ACCESSION   NP_000823
VERSION     NP_000823.4
DBSOURCE    REFSEQ: accession NM_000832.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Michalski,K. and Furukawa,H.
  TITLE     Structure and function of GluN1-3A NMDA receptor excitatory glycine
            receptor channel
  JOURNAL   Sci Adv 10 (15), eadl5952 (2024)
   PUBMED   38598639
REFERENCE   3  (residues 1 to 885)
  AUTHORS   Xu,Y., Song,R., Perszyk,R.E., Chen,W., Kim,S., Park,K.L.,
            Allen,J.P., Nocilla,K.A., Zhang,J., XiangWei,W., Tankovic,A.,
            McDaniels,E.D., Sheikh,R., Mizu,R.K., Karamchandani,M.M., Hu,C.,
            Kusumoto,H., Pecha,J., Cappuccio,G., Gaitanis,J., Sullivan,J.,
            Shashi,V., Petrovski,S., Jauss,R.T., Lee,H.K., Bozarth,X.,
            Lynch,D.R., Helbig,I., Pierson,T.M., Boerkoel,C.F., Myers,S.J.,
            Lemke,J.R., Benke,T.A., Yuan,H. and Traynelis,S.F.
  TITLE     De novo GRIN variants in M3 helix associated with neurological
            disorders control channel gating of NMDA receptor
  JOURNAL   Cell Mol Life Sci 81 (1), 153 (2024)
   PUBMED   38538865
  REMARK    GeneRIF: De novo GRIN variants in M3 helix associated with
            neurological disorders control channel gating of NMDA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 885)
  AUTHORS   Ragnarsson,L., Zhang,Z., Das,S.S., Tran,P., Andersson,A., des
            Portes,V., Desmettre Altuzarra,C., Remerand,G., Labalme,A.,
            Chatron,N., Sanlaville,D., Lesca,G., Anggono,V., Vetter,I. and
            Keramidas,A.
  TITLE     GRIN1 variants associated with neurodevelopmental disorders reveal
            channel gating pathomechanisms
  JOURNAL   Epilepsia 64 (12), 3377-3388 (2023)
   PUBMED   37734923
  REMARK    GeneRIF: GRIN1 variants associated with neurodevelopmental
            disorders reveal channel gating pathomechanisms.
REFERENCE   5  (residues 1 to 885)
  AUTHORS   McNearney,T.A. and Westlund,K.N.
  TITLE     Pluripotential GluN1 (NMDA NR1): Functional Significance in
            Cellular Nuclei in Pain/Nociception
  JOURNAL   Int J Mol Sci 24 (17), 13196 (2023)
   PUBMED   37686003
  REMARK    GeneRIF: Pluripotential GluN1 (NMDA NR1): Functional Significance
            in Cellular Nuclei in Pain/Nociception.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 885)
  AUTHORS   Zimmer,M., Fink,T.M., Franke,Y., Lichter,P. and Spiess,J.
  TITLE     Cloning and structure of the gene encoding the human
            N-methyl-D-aspartate receptor (NMDAR1)
  JOURNAL   Gene 159 (2), 219-223 (1995)
   PUBMED   7622053
REFERENCE   7  (residues 1 to 885)
  AUTHORS   Younkin,D.P., Tang,C.M., Hardy,M., Reddy,U.R., Shi,Q.Y.,
            Pleasure,S.J., Lee,V.M. and Pleasure,D.
  TITLE     Inducible expression of neuronal glutamate receptor channels in the
            NT2 human cell line
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2174-2178 (1993)
   PUBMED   7681588
REFERENCE   8  (residues 1 to 885)
  AUTHORS   Karp,S.J., Masu,M., Eki,T., Ozawa,K. and Nakanishi,S.
  TITLE     Molecular cloning and chromosomal localization of the key subunit
            of the human N-methyl-D-aspartate receptor
  JOURNAL   J Biol Chem 268 (5), 3728-3733 (1993)
   PUBMED   7679115
REFERENCE   9  (residues 1 to 885)
  AUTHORS   Platzer,K. and Lemke,J.R.
  TITLE     GRIN1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31219694
REFERENCE   10 (residues 1 to 885)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL929554.20 and L13266.1.
            
            On Dec 1, 2000 this sequence version replaced NP_000823.3.
            
            Summary: The protein encoded by this gene is a critical subunit of
            N-methyl-D-aspartate receptors, members of the glutamate receptor
            channel superfamily which are heteromeric protein complexes with
            multiple subunits arranged to form a ligand-gated ion channel.
            These subunits play a key role in the plasticity of synapses, which
            is believed to underlie memory and learning. Cell-specific factors
            are thought to control expression of different isoforms, possibly
            contributing to the functional diversity of the subunits.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (GluN1-4a, also known as NR1-1)
            lacks an alternate in-frame exon and uses an alternate splice site
            in the 3' coding region, compared to variant GluN1-1a. The
            resulting protein (isoform GluN1-4a, also known as isoform NR1-1)
            is shorter and has a different C-terminus, compared to isoform
            GluN1-1a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L13266.1, L05666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..885
                     /product="glutamate receptor ionotropic, NMDA 1 isoform
                     GluN1-4a precursor"
                     /note="N-methyl-D-aspartate receptor channel, subunit
                     zeta-1; glutamate [NMDA] receptor subunit zeta-1;
                     N-methyl-D-aspartate receptor subunit NR1; glutamate
                     receptor ionotropic, NMDA 1; glutamate receptor,
                     ionotropic, N-methyl D-aspartate 1; putative
                     NMDtranscript(altAcc_e2)"
                     /calculated_mol_wt=97376
     sig_peptide     1..18
                     /calculated_mol_wt=1957
     mat_peptide     19..885
                     /product="glutamate receptor ionotropic, NMDA 1 isoform
                     GluN1-4a"
                     /calculated_mol_wt=97376
     Region          25..383
                     /region_name="PBP1_iGluR_NMDA_NR1"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR1, an essential
                     channel-forming subunit of the NMDA receptor; cd06379"
                     /db_xref="CDD:380602"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:36309015,
                     ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E93,
                     ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E97,
                     ECO:0000312|PDB:8E98, ECO:0000312|PDB:8E99; propagated
                     from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            order(69..72,76,79,113,319,323,342)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Site            order(69..73,75..76,79..80,113..114,131,135,308..310,
                     319..320,322..323)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380602"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:36309015,
                     ECO:0000269|PubMed:36959261, ECO:0000312|PDB:8E92,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E97, ECO:0007744|PDB:7YFR; propagated
                     from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:36309015,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E97; propagated
                     from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:34186027,
                     ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E92,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E96, ECO:0000312|PDB:8E97,
                     ECO:0007744|PDB:7EOQ; propagated from UniProtKB/Swiss-Prot
                     (Q05586.1)"
     Site            300
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05586.1)"
     Site            350
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:36309015,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E96, ECO:0000312|PDB:8E97; propagated
                     from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:36309015,
                     ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E97; propagated from UniProtKB/Swiss-Prot
                     (Q05586.1)"
     Region          395..799
                     /region_name="PBP2_iGluR_NMDA_Nr1"
                     /note="The ligand-binding domain of the NR1 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13719"
                     /db_xref="CDD:270437"
     Site            440
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05586.1)"
     Site            471
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:34186027,
                     ECO:0000269|PubMed:36309015, ECO:0000269|PubMed:36959261,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E97, ECO:0000312|PDB:8E98,
                     ECO:0007744|PDB:7EOQ, ECO:0007744|PDB:7YFR; propagated
                     from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            491
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05586.1)"
     Site            order(516..519,521,523..525,668,687..688,692,732,753..755,
                     758,764,780..783,786)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:270437"
     Site            order(516..518,523,687..689,731..732)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270437"
     Site            560..580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05586.1)"
     Region          603..624
                     /region_name="Pore-forming.
                     /evidence=ECO:0000250|UniProtKB:A0A1L8F5J9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            628..648
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05586.1)"
     Site            674
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q05586.1)"
     Site            771
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:34186027,
                     ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E92,
                     ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94,
                     ECO:0000312|PDB:8E96, ECO:0000312|PDB:8E97,
                     ECO:0000312|PDB:8E98, ECO:0000312|PDB:8E99,
                     ECO:0007744|PDB:7EOQ; propagated from UniProtKB/Swiss-Prot
                     (Q05586.1)"
     Site            812..835
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05586.1)"
     Region          835..863
                     /region_name="CaM_bdg_C0"
                     /note="Calmodulin-binding domain C0 of NMDA receptor NR1
                     subunit; pfam10562"
                     /db_xref="CDD:402271"
     CDS             1..885
                     /gene="GRIN1"
                     /gene_synonym="DEE101; GluN1; hNR1; MRD8; NDHMSD; NDHMSR;
                     NMD-R1; NMDA1; NMDAR1; NR1"
                     /coded_by="NM_000832.7:334..2991"
                     /note="isoform GluN1-4a precursor is encoded by transcript
                     variant GluN1-4a"
                     /db_xref="CCDS:CCDS43910.1"
                     /db_xref="GeneID:2902"
                     /db_xref="HGNC:HGNC:4584"
                     /db_xref="MIM:138249"
ORIGIN      
        1 mstmrlltla llfscsvara acdpkivnig avlstrkheq mfreavnqan krhgswkiql
       61 natsvthkpn aiqmalsvce dlissqvyai lvshpptpnd hftptpvsyt agfyripvlg
      121 lttrmsiysd ksihlsflrt vppyshqssv wfemmrvysw nhiillvsdd hegraaqkrl
      181 etlleeresk aekvlqfdpg tknvtallme akelearvii lsaseddaat vyraaamlnm
      241 tgsgyvwlvg ereisgnalr yapdgilglq lingknesah isdavgvvaq avhelleken
      301 itdpprgcvg ntniwktgpl fkrvlmssky adgvtgrvef nedgdrkfan ysimnlqnrk
      361 lvqvgiyngt hvipndrkii wpggetekpr gyqmstrlki vtihqepfvy vkptlsdgtc
      421 keeftvngdp vkkvictgpn dtspgsprht vpqccygfci dlliklartm nftyevhlva
      481 dgkfgtqerv nnsnkkewng mmgellsgqa dmivapltin neraqyiefs kpfkyqglti
      541 lvkkeiprst ldsfmqpfqs tlwllvglsv hvvavmlyll drfspfgrfk vnseeeeeda
      601 ltlssamwfs wgvllnsgig egaprsfsar ilgmvwagfa miivasytan laaflvldrp
      661 eeritgindp rlrnpsdkfi yatvkqssvd iyfrrqvels tmyrhmekhn yesaaeaiqa
      721 vrdnklhafi wdsavlefea sqkcdlvttg elffrsgfgi gmrkdspwkq nvslsilksh
      781 engfmedldk twvryqecds rsnapatltf enmagvfmlv aggivagifl ifieiaykrh
      841 kdarrkqmql afaavnvwrk nlqqyhptdi tgplnlsdps vstvv
//
LOCUS       NP_001341835            2560 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform m [Homo sapiens].
ACCESSION   NP_001341835
VERSION     NP_001341835.1
DBSOURCE    REFSEQ: accession NM_001354906.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2560)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2560)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2560)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2560)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2560)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2560)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2560)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2560)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2560)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2560)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034955.1, SRR18074968.1981528.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2560
                     /product="adenomatous polyposis coli protein isoform m"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=279409
     Region          57..109
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          110..183
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          182..225
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(216,220,224,259,263,267,303,307,311)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          229..270
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          233..270
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          277..312
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          320..361
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          366..406
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          370..404
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          408..448
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          412..448
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          449..736
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          753..852
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          974..>991
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1000..1085
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1008..1418
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1088..1110
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1354..1377
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1379..1432
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1433..1454
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1463..1556
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1590..1664
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1750..1769
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1940..2285
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2387..2560
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2560
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354906.2:1095..8777"
                     /note="isoform m is encoded by transcript variant 15"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 mdhetasvls sssthsaprr ltshlgtkve mvysllsmlg thdkddmsrt llamsssqds
       61 cismrqsgcl plliqllhgn dkdsvllgns rgskearara saalhniihs qpddkrgrre
      121 irvlhlleqi raycetcwew qeahepgmdq dknpmpapve hqicpavcvl mklsfdeehr
      181 hamnelgglq aiaellqvdc emygltndhy sitlrryagm altnltfgdv ankatlcsmk
      241 gcmralvaql ksesedlqqv iasvlrnlsw radvnskktl revgsvkalm ecalevkkes
      301 tlksvlsalw nlsahctenk adicavdgal aflvgtltyr sqtntlaiie sgggilrnvs
      361 sliatnedhr qilrennclq tllqhlkshs ltivsnacgt lwnlsarnpk dqealwdmga
      421 vsmlknlihs khkmiamgsa aalrnlmanr pakykdanim spgsslpslh vrkqkaleae
      481 ldaqhlsetf dnidnlspka shrskqrhkq slygdyvfdt nrhddnrsdn fntgnmtvls
      541 pylnttvlps ssssrgslds srsekdrsle rergiglgny hpatenpgts skrglqistt
      601 aaqiakvmee vsaihtsqed rssgsttelh cvtdernalr rssaahthsn tynftksens
      661 nrtcsmpyak leykrssnds lnsvsssdgy gkrgqmkpsi esyseddesk fcsygqypad
      721 lahkihsanh mddndgeldt pinyslkysd eqlnsgrqsp sqnerwarpk hiiedeikqs
      781 eqrqsrnqst typvytestd dkhlkfqphf gqqecvspyr srgangsetn rvgsnhginq
      841 nvsqslcqed dyeddkptny seryseeeqh eeeerptnys ikyneekrhv dqpidyslky
      901 atdipssqkq sfsfsksssg qssktehmss ssentstpss nakrqnqlhp ssaqsrsgqp
      961 qkaatckvss inqetiqtyc vedtpicfsr csslsslssa edeigcnqtt qeadsantlq
     1021 iaeikekigt rsaedpvsev pavsqhprtk ssrlqgssls sesarhkave fssgakspsk
     1081 sgaqtpkspp ehyvqetplm fsrctsvssl dsfesrsias svqsepcsgm vsgiispsdl
     1141 pdspgqtmpp srsktppppp qtaqtkrevp knkaptaekr esgpkqaavn aavqrvqvlp
     1201 dadtllhfat estpdgfscs sslsalslde pfiqkdvelr imppvqendn gneteseqpk
     1261 esnenqekea ektidsekdl lddsddddie ileeciisam ptkssrkakk paqtasklpp
     1321 pvarkpsqlp vykllpsqnr lqpqkhvsft pgddmprvyc vegtpinfst atslsdltie
     1381 sppnelaage gvrggaqsge fekrdtipte grstdeaqgg ktssvtipel ddnkaeegdi
     1441 laecinsamp kgkshkpfrv kkimdqvqqa sasssapnkn qldgkkkkpt spvkpipqnt
     1501 eyrtrvrkna dsknnlnaer vfsdnkdskk qnlknnskvf ndklpnnedr vrgsfafdsp
     1561 hhytpiegtp ycfsrndsls sldfddddvd lsrekaelrk akenkeseak vtshteltsn
     1621 qqsanktqai akqpinrgqp kpilqkqstf pqsskdipdr gaatdeklqn faientpvcf
     1681 shnsslssls didqennnke nepiketepp dsqgepskpq asgyapksfh vedtpvcfsr
     1741 nsslsslsid seddllqeci ssampkkkkp srlkgdnekh sprnmggilg edltldlkdi
     1801 qrpdsehgls pdsenfdwka iqegansivs slhqaaaaac lsrqassdsd silslksgis
     1861 lgspfhltpd qeekpftsnk gprilkpgek stletkkies eskgikggkk vykslitgkv
     1921 rsnseisgqm kqplqanmps isrgrtmihi pgvrnsssst spvskkgppl ktpaskspse
     1981 gqtattsprg akpsvksels pvarqtsqig gsskapsrsg srdstpsrpa qqplsrpiqs
     2041 pgrnsispgr ngisppnkls qlprtsspst astkssgsgk msytspgrqm sqqnltkqtg
     2101 lsknassipr sesaskglnq mnngngankk velsrmsstk ssgsesdrse rpvlvrqstf
     2161 ikeapsptlr rkleesasfe slspssrpas ptrsqaqtpv lspslpdmsl sthssvqagg
     2221 wrklppnlsp tieyndgrpa krhdiarshs espsrlpinr sgtwkrehsk hssslprvst
     2281 wrrtgssssi lsassessek aksedekhvn sisgtkqske nqvsakgtwr kikenefspt
     2341 nstsqtvssg atngaesktl iyqmapavsk tedvwvried cpinnprsgr sptgntppvi
     2401 dsvsekanpn ikdskdnqak qnvgngsvpm rtvglenrln sfiqvdapdq kgteikpgqn
     2461 npvpvsetne ssivertpfs ssssskhssp sgtvaarvtp fnynpsprks sadstsarps
     2521 qiptpvnnnt kkrdsktdst essgtqspkr hsgsylvtsv
//
LOCUS       NP_001356507             646 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform y [Homo sapiens].
ACCESSION   NP_001356507 XP_016881423
VERSION     NP_001356507.1
DBSOURCE    REFSEQ: accession NM_001369578.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881423.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.123923.1,
                                           SRR1803614.137655.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..646
                     /product="transcription factor 4 isoform y"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68839
     Region          537..621
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(545,549,551..553,555,560,581..582)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(558..559,562..563,565..566,569,573,583,586,590,593,
                     596..601)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..646
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369578.1:156..2096"
                     /note="isoform y is encoded by transcript variant 38"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqs llggdmdmgn pgtlsptkpg
      121 sqyyqyssnn prrrplhssa mevqtkkvrk vppglpssvy apsastadyn rdspgypssk
      181 patstfpssf fmqdghhssd pwssssgmnq pgyagmlgns shipqsssyc slhpherlsy
      241 pshssadins slppmstfhr sgtnhystss ctppangtds imanrgsgaa gssqtgdalg
      301 kalasiyspd htnnsfssnp stpvgsppsl sagtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit rsrssnndde dltpeqkaer
      541 ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv
      601 rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_079497                250 aa            linear   PRI 20-NOV-2025
DEFINITION  Kv channel-interacting protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_079497
VERSION     NP_079497.2
DBSOURCE    REFSEQ: accession NM_025221.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 250)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 250)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 250)
  AUTHORS   Mosley,J.D., Shaffer,C.M., Van Driest,S.L., Weeke,P.E., Wells,Q.S.,
            Karnes,J.H., Velez Edwards,D.R., Wei,W.Q., Teixeira,P.L.,
            Bastarache,L., Crawford,D.C., Li,R., Manolio,T.A., Bottinger,E.P.,
            McCarty,C.A., Linneman,J.G., Brilliant,M.H., Pacheco,J.A.,
            Thompson,W., Chisholm,R.L., Jarvik,G.P., Crosslin,D.R.,
            Carrell,D.S., Baldwin,E., Ralston,J., Larson,E.B., Grafton,J.,
            Scrol,A., Jouni,H., Kullo,I.J., Tromp,G., Borthwick,K.M.,
            Kuivaniemi,H., Carey,D.J., Ritchie,M.D., Bradford,Y., Verma,S.S.,
            Chute,C.G., Veluchamy,A., Siddiqui,M.K., Palmer,C.N., Doney,A.,
            MahmoudPour,S.H., Maitland-van der Zee,A.H., Morris,A.D.,
            Denny,J.C. and Roden,D.M.
  TITLE     A genome-wide association study identifies variants in KCNIP4
            associated with ACE inhibitor-induced cough
  JOURNAL   Pharmacogenomics J 16 (3), 231-237 (2016)
   PUBMED   26169577
  REMARK    GeneRIF: Results indicate that SNPs in KCNIP4 may modulate ACE
            inhibitor-induced cough risk.
REFERENCE   4  (residues 1 to 250)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 250)
  AUTHORS   Kitazawa,M., Kubo,Y. and Nakajo,K.
  TITLE     The stoichiometry and biophysical properties of the Kv4 potassium
            channel complex with K+ channel-interacting protein (KChIP)
            subunits are variable, depending on the relative expression level
  JOURNAL   J Biol Chem 289 (25), 17597-17609 (2014)
   PUBMED   24811166
  REMARK    GeneRIF: Subunit counting by single-molecule imaging revealed that
            the bound number of KChIP4 in each Kv4.2.KChIP4 complex was
            dependent on the expression level of KChIP4.
REFERENCE   6  (residues 1 to 250)
  AUTHORS   Bonne,A., Vreede,L., Kuiper,R.P., Bodmer,D., Jansen,C., Eleveld,M.,
            van Erp,F., Arkesteijn,G., Hoogerbrugge,N., van Ravenswaaij,C.,
            Schoenmakers,E.F. and Geurts van Kessel,A.
  TITLE     Mapping of constitutional translocation breakpoints in renal cell
            cancer patients: identification of KCNIP4 as a candidate gene
  JOURNAL   Cancer Genet Cytogenet 179 (1), 11-18 (2007)
   PUBMED   17981209
  REMARK    GeneRIF: Mutation of KCNIP4 is associated with renal cell
            carcinoma.
REFERENCE   7  (residues 1 to 250)
  AUTHORS   Chen,C.P., Lee,L. and Chang,L.S.
  TITLE     Effects of metal-binding properties of human Kv channel-interacting
            proteins on their molecular structure and binding with Kv4.2
            channel
  JOURNAL   Protein J 25 (5), 345-351 (2006)
   PUBMED   16951992
  REMARK    GeneRIF: The conformational change with metal-bound KChIP4.1 is
            crucial for its interaction with Kv channel but not for KChIP2.2,
            and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and
            KChIP4.1 have different effects on their molecular structure.
REFERENCE   8  (residues 1 to 250)
  AUTHORS   Pruunsild,P. and Timmusk,T.
  TITLE     Structure, alternative splicing, and expression of the human and
            mouse KCNIP gene family
  JOURNAL   Genomics 86 (5), 581-593 (2005)
   PUBMED   16112838
REFERENCE   9  (residues 1 to 250)
  AUTHORS   Morohashi,Y., Hatano,N., Ohya,S., Takikawa,R., Watabiki,T.,
            Takasugi,N., Imaizumi,Y., Tomita,T. and Iwatsubo,T.
  TITLE     Molecular cloning and characterization of CALP/KChIP4, a novel
            EF-hand protein interacting with presenilin 2 and voltage-gated
            potassium channel subunit Kv4
  JOURNAL   J Biol Chem 277 (17), 14965-14975 (2002)
   PUBMED   11847232
  REMARK    GeneRIF: cloning and investigation of interaction with presenilin 2
            and voltage-gated potassium channel subunit Kv4
REFERENCE   10 (residues 1 to 250)
  AUTHORS   Holmqvist,M.H., Cao,J., Hernandez-Pineda,R., Jacobson,M.D.,
            Carroll,K.I., Sung,M.A., Betty,M., Ge,P., Gilbride,K.J.,
            Brown,M.E., Jurman,M.E., Lawson,D., Silos-Santiago,I., Xie,Y.,
            Covarrubias,M., Rhodes,K.J., Distefano,P.S. and An,W.F.
  TITLE     Elimination of fast inactivation in Kv4 A-type potassium channels
            by an auxiliary subunit domain
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 1035-1040 (2002)
   PUBMED   11805342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113606.3, BI596848.1,
            AF367023.1, BC032520.2, AC097505.2, AC104065.3 and BX648990.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 5, 2002 this sequence version replaced NP_079497.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belong
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium. This
            protein member also interacts with presenilin. Multiple
            alternatively spliced transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1, also known as KCHIP4.1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.271330.1,
                                           SRR1803611.185942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382152.7/ ENSP00000371587.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..250
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31-p15.2"
     Protein         1..250
                     /product="Kv channel-interacting protein 4 isoform 1"
                     /note="calsenilin-like protein; a-type potassium channel
                     modulatory protein 4; Kv channel interacting protein 4"
                     /calculated_mol_wt=28598
     Region          2..44
                     /region_name="KIS. /evidence=ECO:0000250|UniProtKB:Q6PHZ8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6PIL6.1)"
     Region          99..146
                     /region_name="EF-hand_8"
                     /note="EF-hand domain pair; pfam13833"
                     /db_xref="CDD:404678"
     Region          <128..235
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          237..250
                     /region_name="Interaction with KCND2.
                     /evidence=ECO:0000250|UniProtKB:Q8R426"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIL6.1)"
     CDS             1..250
                     /gene="KCNIP4"
                     /gene_synonym="CALP; KCHIP4"
                     /coded_by="NM_025221.6:142..894"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43216.1"
                     /db_xref="GeneID:80333"
                     /db_xref="HGNC:HGNC:30083"
                     /db_xref="MIM:608182"
ORIGIN      
        1 mnvrrvesis aqleeasstg gflyaqnstk rsikerlmkl lpcsaaktss paiqnsvede
       61 lematvrhrp ealelleaqs kftkkelqil yrgfknecps gvvneetfke iysqffpqgd
      121 sttyahflfn afdtdhngav sfedfikgls illrgtvqek lnwafnlydi nkdgyitkee
      181 mldimkaiyd mmgkctypvl kedaprqhve tffqkmdknk dgvvtidefi escqkdenim
      241 rsmqlfenvi
//
LOCUS       NP_001356371             377 aa            linear   PRI 20-NOV-2025
DEFINITION  NIF3-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001356371 XP_011509886
VERSION     NP_001356371.1
DBSOURCE    REFSEQ: accession NM_001369442.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Reed,C.J., Hutinet,G. and de Crecy-Lagard,V.
  TITLE     Comparative Genomic Analysis of the DUF34 Protein Family Suggests
            Role as a Metal Ion Chaperone or Insertase
  JOURNAL   Biomolecules 11 (9), 1282 (2021)
   PUBMED   34572495
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Merla,G., Howald,C., Antonarakis,S.E. and Reymond,A.
  TITLE     The subcellular localization of the ChoRE-binding protein, encoded
            by the Williams-Beuren syndrome critical region gene 14, is
            regulated by 14-3-3
  JOURNAL   Hum Mol Genet 13 (14), 1505-1514 (2004)
   PUBMED   15163635
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Tascou,S., Kang,T.W., Trappe,R., Engel,W. and Burfeind,P.
  TITLE     Identification and characterization of NIF3L1 BP1, a novel
            cytoplasmic interaction partner of the NIF3L1 protein
  JOURNAL   Biochem Biophys Res Commun 309 (2), 440-448 (2003)
   PUBMED   12951069
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Akiyama,H., Fujisawa,N., Tashiro,Y., Takanabe,N., Sugiyama,A. and
            Tashiro,F.
  TITLE     The role of transcriptional corepressor Nif3l1 in early stage of
            neural differentiation via cooperation with Trip15/CSN2
  JOURNAL   J Biol Chem 278 (12), 10752-10762 (2003)
   PUBMED   12522100
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Hadano,S., Yanagisawa,Y., Skaug,J., Fichter,K., Nasir,J.,
            Martindale,D., Koop,B.F., Scherer,S.W., Nicholson,D.W.,
            Rouleau,G.A., Ikeda,J. and Hayden,M.R.
  TITLE     Cloning and characterization of three novel genes, ALS2CR1,
            ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis
            (ALS2) critical region at chromosome 2q33-q34: candidate genes for
            ALS2
  JOURNAL   Genomics 71 (2), 200-213 (2001)
   PUBMED   11161814
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Tascou,S., Uedelhoven,J., Dixkens,C., Nayernia,K., Engel,W. and
            Burfeind,P.
  TITLE     Isolation and characterization of a novel human gene, NIF3L1, and
            its mouse ortholog, Nif3l1, highly conserved from bacteria to
            mammals
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 330-336 (2000)
   PUBMED   11124544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005037.2.
            
            On Apr 9, 2019 this sequence version replaced XP_011509886.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.24490.1,
                                           SRR1803611.223097.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..377
                     /product="NIF3-like protein 1 isoform 1"
                     /EC_number="3.5.4.16"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 1; NIF3 (Ngg1 interacting
                     factor 3, S.pombe homolog)-like 1; NIF3-like protein 1;
                     NIF3 NGG1 interacting factor 3-like 1; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 1 protein;
                     GTP cyclohydrolase I; putative GTP cyclohydrolase 1 type 2
                     NIF3L1"
                     /calculated_mol_wt=41837
     Region          33..354
                     /region_name="NIF3"
                     /note="NIF3 (NGG1p interacting factor 3); pfam01784"
                     /db_xref="CDD:426431"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Region          244..377
                     /region_name="Mediates interaction with COPS2.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     CDS             1..377
                     /gene="NIF3L1"
                     /gene_synonym="ALS2CR1; CALS-7; MDS015"
                     /coded_by="NM_001369442.1:1228..2361"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS46485.1"
                     /db_xref="GeneID:60491"
                     /db_xref="HGNC:HGNC:13390"
                     /db_xref="MIM:605778"
ORIGIN      
        1 mlsscvrpvp ttvrfvdsli cnssrsfmdl kallsslndf aslsfaeswd nvgllvepsp
       61 phtvntlflt ndlteevmee vlqkkadlil syhppifrpm kritwntwke rlviralenr
      121 vgiysphtay daapqgvnnw lakglgacts rpihpskapn yptegnhrve fnvnytqdld
      181 kvmsavkgid gvsvtsfsar tgneeqtrin lnctqkalmq vvdflsrnkq lyqkteilsl
      241 ekplllhtgm grlctldesv slatmidrik rhlklshirl algvgrtles qvkvvalcag
      301 sgssvlqgve adlyltgems hhdtldaasq ginvilcehs ntergflsdl rdmldshlen
      361 kiniilsetd rdplqvv
//
LOCUS       NP_001273081             223 aa            linear   PRI 20-NOV-2025
DEFINITION  myelin protein zero-like protein 3 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001273081 XP_005271484
VERSION     NP_001273081.1
DBSOURCE    REFSEQ: accession NM_001286152.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Ramani,S.R., Tom,I., Lewin-Koh,N., Wranik,B., Depalatis,L.,
            Zhang,J., Eaton,D. and Gonzalez,L.C.
  TITLE     A secreted protein microarray platform for extracellular protein
            interaction discovery
  JOURNAL   Anal Biochem 420 (2), 127-138 (2012)
   PUBMED   21982860
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Racz,P., Mink,M., Ordas,A., Cao,T., Szalma,S., Szauter,K.M. and
            Csiszar,K.
  TITLE     The human orthologue of murine Mpzl3 with predicted adhesive and
            immune functions is a potential candidate gene for immune-related
            hereditary hair loss
  JOURNAL   Exp Dermatol 18 (3), 261-263 (2009)
   PUBMED   19054061
  REMARK    GeneRIF: Homozygous or compound heterozygous mutations of MPZL3
            might be involved in immune-mediated human hereditary disorders
            with hair loss.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Cao,T., Racz,P., Szauter,K.M., Groma,G., Nakamatsu,G.Y.,
            Fogelgren,B., Pankotai,E., He,Q.P. and Csiszar,K.
  TITLE     Mutation in Mpzl3, a novel [corrected] gene encoding a predicted
            [corrected] adhesion protein, in the rough coat (rc) mice with
            severe skin and hair abnormalities
  JOURNAL   J Invest Dermatol 127 (6), 1375-1386 (2007)
   PUBMED   17273165
  REMARK    Erratum:[J Invest Dermatol. 2007 Nov;127(11):2678]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC417020.1, BC143897.1, BC113586.1 and AP002800.4.
            
            On Oct 31, 2013 this sequence version replaced XP_005271484.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site, compared to variant 1. The encoded isoform (b) is
            shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.131675.1, AK304292.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..223
                     /product="myelin protein zero-like protein 3 isoform b
                     precursor"
                     /note="myelin protein zero-like protein 3"
                     /calculated_mol_wt=21455
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3204
     Region          25..125
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          36..40
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          53..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          99..103
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          113..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..223
                     /gene="MPZL3"
                     /coded_by="NM_001286152.2:72..743"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS66241.1"
                     /db_xref="GeneID:196264"
                     /db_xref="HGNC:HGNC:27279"
                     /db_xref="MIM:611707"
ORIGIN      
        1 mqqrgaagsr gcalfpllgv lffqdahvrg yvgekiklkc tfkstsdvtd kltidwtyrp
       61 pssshtvsif hyqsfqyptt agtfrdrisw vgnvykgdas isisnptikd ngtfscavkn
      121 ppdvhhnipm teltvtergf gtmlssvall silvfvpsav vvalllvrmg rkaaglkkrs
      181 rsgykkssie vsddtdqeee eacmarlcvr caecldsdye ety
//
LOCUS       NP_001311318             406 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001311318 XP_005273696
VERSION     NP_001311318.1
DBSOURCE    REFSEQ: accession NM_001324389.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 406)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, AC040975.8, AC091558.7, AC108449.5 and BQ019252.1.
            
            On May 2, 2016 this sequence version replaced XP_005273696.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.260453.1,
                                           SRR3476690.993090.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..406
                     /product="homeobox-containing protein 1 isoform 6"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=45979
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..406
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324389.2:342..1562"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr anieaailes hgidvqspgg
      361 hsnsddvdgn dyseqdtwqv rngeeeegrs seggreaekv eeerri
//
LOCUS       NP_001350923             627 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform b precursor [Homo sapiens].
ACCESSION   NP_001350923 XP_024301993
VERSION     NP_001350923.1
DBSOURCE    REFSEQ: accession NM_001363994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 627)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 627)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294702.1 and AC113426.2.
            
            On Jun 5, 2018 this sequence version replaced XP_024301993.1.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294702.1, SRR1803613.146010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..627
                     /product="calnexin isoform b precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65396
     sig_peptide     1..55
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=6125
     Region          106..475
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     CDS             1..627
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001363994.1:76..1959"
                     /note="isoform b precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 madrrtptpf agcrlprqrr ardasqvsap gtrrimegkw llcmllvlgt aiveahdghd
       61 ddvidieddl ddvieeveds kpdttappss pkvtykapvp tgevyfadsf drgtlsgwil
      121 skakkddtdd eiakydgkwe veemkesklp gdkglvlmsr akhhaisakl nkpflfdtkp
      181 livqyevnfq ngiecggayv kllsktpeln ldqfhdktpy timfgpdkcg edyklhfifr
      241 hknpktgiye ekhakrpdad lktyftdkkt hlytlilnpd nsfeilvdqs vvnsgnllnd
      301 mtppvnpsre iedpedrkpe dwderpkipd peavkpddwd edapakipde eatkpegwld
      361 depeyvpdpd aekpedwded mdgeweapqi anprcesapg cgvwqrpvid npnykgkwkp
      421 pmidnpsyqg iwkprkipnp dffedlepfr mtpfsaigle lwsmtsdiff dnfiicadrr
      481 ivddwandgw glkkaadgaa epgvvgqmie aaeerpwlwv vyiltvalpv flvilfccsg
      541 kkqtsgmeyk ktdapqpdvk eeeeekeeek dkgdeeeege ekleekqksd aeedggtvsq
      601 eeedrkpkae edeilnrspr nrkprre
//
LOCUS       NP_783163                407 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasomal ubiquitin receptor ADRM1 isoform 1 [Homo sapiens].
ACCESSION   NP_783163
VERSION     NP_783163.1
DBSOURCE    REFSEQ: accession NM_175573.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Shao,Z., Wang,Y., He,Y., Zhang,C., Zhao,Y., Zhang,M., Li,Q. and
            Wang,J.
  TITLE     The high expression of ADRM1 in hepatocellular carcinoma is closely
            related to tumor immune infiltration and is regulated by
            miR-891a-5p
  JOURNAL   Sci Rep 14 (1), 14002 (2024)
   PUBMED   38890391
  REMARK    GeneRIF: The high expression of ADRM1 in hepatocellular carcinoma
            is closely related to tumor immune infiltration and is regulated by
            miR-891a-5p.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Osei-Amponsa,V., Chandravanshi,M., Lu,X., Magidson,V., Das,S.,
            Andresson,T., Dyba,M., Sabbasani,V.R., Swenson,R.E., Fromont,C.,
            Shrestha,B., Zhao,Y., Clapp,M.E., Chari,R. and Walters,K.J.
  TITLE     hRpn13 shapes the proteome and transcriptome through epigenetic
            factors HDAC8, PADI4, and transcription factor NF-kappaB p50
  JOURNAL   Mol Cell 84 (3), 522-537 (2024)
   PUBMED   38151017
  REMARK    GeneRIF: hRpn13 shapes the proteome and transcriptome through
            epigenetic factors HDAC8, PADI4, and transcription factor NF-kappaB
            p50.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Zhu,D. and Zhong,Q.
  TITLE     Potential of adhesion-regulating molecule 1 (ADRM1) as a biomarker
            for patients with renal clear-cell carcinoma or papillary-cell
            carcinoma
  JOURNAL   Asian J Surg 46 (10), 4666-4668 (2023)
   PUBMED   37268471
  REMARK    GeneRIF: Potential of adhesion-regulating molecule 1 (ADRM1) as a
            biomarker for patients with renal clear-cell carcinoma or
            papillary-cell carcinoma.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Xiao,J., Xie,Y., Duan,Q., Liu,T., Ye,R., Duan,X., Le,Z., Deng,N.
            and Liu,F.
  TITLE     LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models
  JOURNAL   Int Heart J 64 (4), 750-758 (2023)
   PUBMED   37518356
  REMARK    GeneRIF: LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models.
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Jorgensen,J.P., Lauridsen,A.M., Kristensen,P., Dissing,K.,
            Johnsen,A.H., Hendil,K.B. and Hartmann-Petersen,R.
  TITLE     Adrm1, a putative cell adhesion regulating protein, is a novel
            proteasome-associated factor
  JOURNAL   J Mol Biol 360 (5), 1043-1052 (2006)
   PUBMED   16815440
  REMARK    GeneRIF: Adrm1 has a specialised role in proteasome function.
            Identified Adrm1 as a novel component of the regulatory ATPase
            complex of the 26 S proteasome
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Lamerant,N. and Kieda,C.
  TITLE     Adhesion properties of adhesion-regulating molecule 1 protein on
            endothelial cells
  JOURNAL   FEBS J 272 (8), 1833-1844 (2005)
   PUBMED   15819879
  REMARK    GeneRIF: ARM-1 is a cytosolic protein associated with the plasma
            membrane. However, no cell surface expression of the protein was
            observed. These results suggest an indirect role of ARM-1 in
            adhesion rather than a direct role as an adhesion molecule
            itself.[ARM-1]
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Cascio,P., Call,M., Petre,B.M., Walz,T. and Goldberg,A.L.
  TITLE     Properties of the hybrid form of the 26S proteasome containing both
            19S and PA28 complexes
  JOURNAL   EMBO J 21 (11), 2636-2645 (2002)
   PUBMED   12032076
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Simins,A.B., Weighardt,H., Weidner,K.M., Weidle,U.H. and
            Holzmann,B.
  TITLE     Functional cloning of ARM-1, an adhesion-regulating molecule
            upregulated in metastatic tumor cells
  JOURNAL   Clin Exp Metastasis 17 (8), 641-648 (1999)
   PUBMED   10919708
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Shimada,S., Ogawa,M., Takahashi,M., Schlom,J. and Greiner,J.W.
  TITLE     Molecular cloning and characterization of the complementary DNA of
            an M(r) 110,000 antigen expressed by human gastric carcinoma cells
            and upregulated by gamma-interferon
  JOURNAL   Cancer Res 54 (14), 3831-3836 (1994)
   PUBMED   8033103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY029018.1, BC017245.2 and
            BR000321.1.
            
            Summary: This gene encodes a member of the adhesion regulating
            molecule 1 protein family. The encoded protein is a component of
            the proteasome where it acts as a ubiquitin receptor and recruits
            the deubiquitinating enzyme, ubiquitin carboxyl-terminal hydrolase
            L5. Increased levels of the encoded protein are associated with
            increased cell adhesion, which is likely an indirect effect of this
            intracellular protein. Dysregulation of this gene has been
            implicated in carcinogenesis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017245.2, SRR1163658.516773.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..407
                     /product="proteasomal ubiquitin receptor ADRM1 isoform 1"
                     /note="110 kDa cell membrane glycoprotein; M(r) 110,000
                     surface antigen; proteasomal ubiquitin receptor ADRM1;
                     rpn13 homolog; proteasome regulatory particle non-ATPase
                     13; proteasome ubiquitin receptor; adhesion regulating
                     molecule 1"
                     /calculated_mol_wt=42022
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          24..128
                     /region_name="PH_Rpn13"
                     /note="Pleckstrin homology-like domain of Regulatory
                     Particle Non-ATPase 13; cd13314"
                     /db_xref="CDD:270124"
     Site            order(53..54,56,73..80,98..100,103)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:270124"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          194..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          253..407
                     /region_name="Interaction with UCHL5.
                     /evidence=ECO:0000269|PubMed:20471946"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          274..381
                     /region_name="RPN13_C"
                     /note="UCH-binding domain; pfam16550"
                     /db_xref="CDD:465170"
     Region          379..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMB5; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     CDS             1..407
                     /gene="ADRM1"
                     /gene_synonym="ARM-1; ARM1; GP110; PSMD16"
                     /coded_by="NM_175573.2:152..1375"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13496.1"
                     /db_xref="GeneID:11047"
                     /db_xref="HGNC:HGNC:15759"
                     /db_xref="MIM:610650"
ORIGIN      
        1 mttsgalfps lvpgsrgasn kylvefragk mslkgttvtp dkrkglvyiq qtddslihfc
       61 wkdrtsgnve ddliifpddc efkrvpqcps grvyvlkfka gskrlffwmq epktdqdeeh
      121 crkvneylnn ppmpgalgas gssghelsal ggegglqsll gnmshsqlmq ligpaglggl
      181 gglgaltgpg lasllgssgp pgsssssssr sqsaavtpss ttsstratpa psapaaasat
      241 spspapssgn gastaasptq piqlsdlqsi latmnvpagp aggqqvdlas vltpeimapi
      301 lanadvqerl lpylpsgesl pqtadeiqnt ltspqfqqal gmfsaalasg qlgplmcqfg
      361 lpaeaveaan kgdveafaka mqnnakpeqk egdtkdkkde eedmsld
//
LOCUS       NP_001309168             233 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001309168 XP_011527263
VERSION     NP_001309168.1
DBSOURCE    REFSEQ: accession NM_001322239.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160175.5 and BC019307.1.
            
            On Apr 8, 2016 this sequence version replaced XP_011527263.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.140099.1,
                                           SRR3476690.1030546.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001322239.2:231..932"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     7"
                     /db_xref="CCDS:CCDS13189.1"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_009216                117 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor-associated protein-like 2 [Homo
            sapiens].
ACCESSION   NP_009216 NP_776083
VERSION     NP_009216.1
DBSOURCE    REFSEQ: accession NM_007285.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Jimenez-Moreno,N. and Lane,J.D.
  TITLE     ATG8 proteins are co-factors for human dopaminergic neuronal
            transcriptional control: implications for neuronal resilience in
            Parkinson disease
  JOURNAL   Autophagy 20 (4), 955-957 (2024)
   PUBMED   37312406
  REMARK    GeneRIF: ATG8 proteins are co-factors for human dopaminergic
            neuronal transcriptional control: implications for neuronal
            resilience in Parkinson disease.
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Toth,V., Vadaszi,H., Ravasz,L., Mittli,D., Matyas,D., Molnar,T.,
            Micsonai,A., Szaniszlo,T., Lorincz,P., Kovacs,R.A., Juhasz,T.,
            Beke-Somfai,T., Juhasz,G., Gyorffy,B.A., Kekesi,K.A. and Kardos,J.
  TITLE     Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and
            localizes to autophagosomes during induced autophagy
  JOURNAL   Cell Mol Life Sci 79 (9), 471 (2022)
   PUBMED   35932293
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Xin,Y., Yu,L., Chen,Z., Zheng,L., Fu,Q., Jiang,J., Zhang,P.,
            Gong,R. and Zhao,S.
  TITLE     Cloning, expression patterns, and chromosome localization of three
            human and two mouse homologues of GABA(A) receptor-associated
            protein
  JOURNAL   Genomics 74 (3), 408-413 (2001)
   PUBMED   11414770
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Ueno,T. and Kominami,E.
  TITLE     The human homolog of Saccharomyces cerevisiae Apg7p is a
            Protein-activating enzyme for multiple substrates including human
            Apg12p, GATE-16, GABARAP, and MAP-LC3
  JOURNAL   J Biol Chem 276 (3), 1701-1706 (2001)
   PUBMED   11096062
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Okazaki,N., Yan,J., Yuasa,S., Ueno,T., Kominami,E., Masuho,Y.,
            Koga,H. and Muramatsu,M.
  TITLE     Interaction of the Unc-51-like kinase and microtubule-associated
            protein light chain 3 related proteins in the brain: possible role
            of vesicular transport in axonal elongation
  JOURNAL   Brain Res Mol Brain Res 85 (1-2), 1-12 (2000)
   PUBMED   11146101
REFERENCE   9  (residues 1 to 117)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 117)
  AUTHORS   Sagiv,Y., Legesse-Miller,A., Porat,A. and Elazar,Z.
  TITLE     GATE-16, a membrane transport modulator, interacts with NSF and the
            Golgi v-SNARE GOS-28
  JOURNAL   EMBO J 19 (7), 1494-1504 (2000)
   PUBMED   10747018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB030710.1.
            
            On Mar 7, 2003 this sequence version replaced NP_776083.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.178644.1, BC029601.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000037243.7/ ENSP00000037243.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..117
                     /product="gamma-aminobutyric acid receptor-associated
                     protein-like 2"
                     /note="ganglioside expression factor 2; MAP1 light chain 3
                     related protein; general protein transport factor p16;
                     golgi-associated ATPase enhancer of 16 kDa; GABA(A)
                     receptor-associated protein-like 2"
                     /calculated_mol_wt=13536
     mat_peptide     1..116
                     /product="Gamma-aminobutyric acid receptor-associated
                     protein-like 2. /id=PRO_0000212373"
                     /note="propagated from UniProtKB/Swiss-Prot (P60520.1)"
                     /calculated_mol_wt=13520
     Region          5..116
                     /region_name="Ubl_ATG8_GABARAPL2"
                     /note="ubiquitin-like (Ubl) domain found in GABA type A
                     receptor associated protein like 2 (GABARAPL2, also known
                     as GATE16); cd17163"
                     /db_xref="CDD:340683"
     Site            24
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P60520.1)"
     Site            order(28,34..35,46,49,58..59,61..63,65..67,73,75..77,79,
                     82..83,86..88,112..116)
                     /site_type="other"
                     /note="Atg7 interaction site [polypeptide binding]"
                     /db_xref="CDD:340683"
     Site            order(36,61,65,73..77,79,82..83,86..87,108,110..116)
                     /site_type="other"
                     /note="Atg4 interaction site [polypeptide binding]"
                     /db_xref="CDD:340683"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P60520.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:31709703; propagated from
                     UniProtKB/Swiss-Prot (P60520.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:31709703; propagated from
                     UniProtKB/Swiss-Prot (P60520.1)"
     Site            116..117
                     /site_type="cleavage"
                     /note="Cleavage, by ATG4.
                     /evidence=ECO:0000269|PubMed:15169837; propagated from
                     UniProtKB/Swiss-Prot (P60520.1)"
     CDS             1..117
                     /gene="GABARAPL2"
                     /gene_synonym="ATG8; ATG8C; GATE-16; GATE16; GEF-2; GEF2"
                     /coded_by="NM_007285.7:109..462"
                     /db_xref="CCDS:CCDS10921.1"
                     /db_xref="GeneID:11345"
                     /db_xref="HGNC:HGNC:13291"
                     /db_xref="MIM:607452"
ORIGIN      
        1 mkwmfkedhs lehrcvesak irakypdrvp vivekvsgsq ivdidkrkyl vpsditvaqf
       61 mwiirkriql psekaiflfv dktvpqsslt mgqlyekekd edgflyvays gentfgf
//
LOCUS       NP_006452               1193 aa            linear   PRI 20-NOV-2025
DEFINITION  sperm-associated antigen 5 [Homo sapiens].
ACCESSION   NP_006452
VERSION     NP_006452.3
DBSOURCE    REFSEQ: accession NM_006461.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1193)
  AUTHORS   Pang,Y., Liu,Y., Chen,S., Zhang,J., Zeng,J., Pan,Y. and An,J.
  TITLE     [Biological role of SPAG5 in the malignant proliferation of gastric
            cancer cells]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (8), 1497-1507 (2024)
   PUBMED   39276045
  REMARK    GeneRIF: [Biological role of SPAG5 in the malignant proliferation
            of gastric cancer cells].
REFERENCE   3  (residues 1 to 1193)
  AUTHORS   Guo,L., Yuan,H., Zhu,H., Zhou,J., Wan,Z. and Zhou,Y.
  TITLE     SPAG5 deficiency activates autophagy to reduce atherosclerotic
            plaque formation in ApoE-/- mice
  JOURNAL   BMC Cardiovasc Disord 24 (1), 275 (2024)
   PUBMED   38807081
  REMARK    GeneRIF: SPAG5 deficiency activates autophagy to reduce
            atherosclerotic plaque formation in ApoE[-/-] mice.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1193)
  AUTHORS   Zhang,X., Wu,W., Li,X., He,F. and Zhang,L.
  TITLE     SPAG5 promotes the proliferation, migration, invasion, and
            epithelial-mesenchymal transformation of colorectal cancer cells by
            activating the PI3K/AKT signaling pathway
  JOURNAL   Chin J Physiol 66 (5), 365-371 (2023)
   PUBMED   37929348
  REMARK    GeneRIF: SPAG5 promotes the proliferation, migration, invasion, and
            epithelial-mesenchymal transformation of colorectal cancer cells by
            activating the PI3K/AKT signaling pathway.
REFERENCE   5  (residues 1 to 1193)
  AUTHORS   Li,H., Qin,Y., Huang,Y., Wang,J. and Ren,B.
  TITLE     SPAG5, the upstream protein of Wnt and the target of curcumin,
            inhibits hepatocellular carcinoma
  JOURNAL   Oncol Rep 50 (3) (2023)
   PUBMED   37539742
  REMARK    GeneRIF: SPAG5, the upstream protein of Wnt and the target of
            curcumin, inhibits hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 1193)
  AUTHORS   Yang,Y.C., Hsu,Y.T., Wu,C.C., Chen,H.T. and Chang,M.S.
  TITLE     Silencing of astrin induces the p53-dependent apoptosis by
            suppression of HPV18 E6 expression and sensitizes cells to
            paclitaxel treatment in HeLa cells
  JOURNAL   Biochem Biophys Res Commun 343 (2), 428-434 (2006)
   PUBMED   16546135
  REMARK    GeneRIF: These findings suggest that the silencing of astrin induce
            a p53-dependent apoptosis and has an additive effect on paclitaxel
            treatment.
REFERENCE   7  (residues 1 to 1193)
  AUTHORS   Le,X.F., Lammayot,A., Gold,D., Lu,Y., Mao,W., Chang,T., Patel,A.,
            Mills,G.B. and Bast,R.C. Jr.
  TITLE     Genes affecting the cell cycle, growth, maintenance, and drug
            sensitivity are preferentially regulated by anti-HER2 antibody
            through phosphatidylinositol 3-kinase-AKT signaling
  JOURNAL   J Biol Chem 280 (3), 2092-2104 (2005)
   PUBMED   15504738
REFERENCE   8  (residues 1 to 1193)
  AUTHORS   Gruber,J., Harborth,J., Schnabel,J., Weber,K. and Hatzfeld,M.
  TITLE     The mitotic-spindle-associated protein astrin is essential for
            progression through mitosis
  JOURNAL   J Cell Sci 115 (Pt 21), 4053-4059 (2002)
   PUBMED   12356910
REFERENCE   9  (residues 1 to 1193)
  AUTHORS   Mack,G.J. and Compton,D.A.
  TITLE     Analysis of mitotic microtubule-associated proteins using mass
            spectrometry identifies astrin, a spindle-associated protein
  JOURNAL   Proc Natl Acad Sci U S A 98 (25), 14434-14439 (2001)
   PUBMED   11724960
REFERENCE   10 (residues 1 to 1193)
  AUTHORS   Chang,M.S., Huang,C.J., Chen,M.L., Chen,S.T., Fan,C.C., Chu,J.M.,
            Lin,W.C. and Yang,Y.C.
  TITLE     Cloning and characterization of hMAP126, a new member of mitotic
            spindle-associated proteins
  JOURNAL   Biochem Biophys Res Commun 287 (1), 116-121 (2001)
   PUBMED   11549262
  REMARK    GeneRIF: hMap126 is abundantly expressed in testis and localized in
            mitotic spindle and may be involved in the functional and dynamic
            regulation of mitotic spindles.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI459711.1, BC000322.2 and
            BQ773438.1.
            
            On Aug 19, 2005 this sequence version replaced NP_006452.2.
            
            Summary: This gene encodes a protein associated with the mitotic
            spindle apparatus. The encoded protein may be involved in the
            functional and dynamic regulation of mitotic spindles. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF063308.1, SRR1660807.158831.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321765.10/ ENSP00000323300.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..1193
                     /product="sperm-associated antigen 5"
                     /note="mitotic spindle coiled-coil related protein;
                     astrin; mitotic spindle associated protein p126"
                     /calculated_mol_wt=134291
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TME2; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TME2; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Region          96..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:18055457; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Region          390..416
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R06.2)"
     Region          482..850
                     /region_name="Interaction with KNSTRN.
                     /evidence=ECO:0000269|PubMed:21402792"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96R06.2)"
     Region          <592..>1081
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            937
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:18055457; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:18055457; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:18055457; propagated from
                     UniProtKB/Swiss-Prot (Q96R06.2)"
     Region          <988..>1193
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1193
                     /gene="SPAG5"
                     /gene_synonym="DEEPEST; hMAP126; MAP126"
                     /coded_by="NM_006461.4:80..3661"
                     /db_xref="CCDS:CCDS32594.1"
                     /db_xref="GeneID:10615"
                     /db_xref="HGNC:HGNC:13452"
                     /db_xref="MIM:615562"
ORIGIN      
        1 mwrvkklsls lspspqtgkp smrtplrelt lqpgaltnsg krspacsslt pslcklglqe
       61 gsnnsspvdf vnnkrtdlss ehfshsskwl etcqhesdeq pldpipqiss tpktseeavd
      121 plgnymvkti vlvpsplgqq qdmifearld tmaetnsisl ngplrtddlv reevapcmgd
      181 rfsevaavse kpifqespsh lleesppnpc seqlhcskes lssrteavre dlvpsesnaf
      241 lpssvlwlsp stalaadfrv nhvdpeeeiv ehgameerem rfpthpkese tedqalvssv
      301 edilstcltp nlvemesqea pgpavedvgr ilgsdteswm splawlekgv ntsvmlenlr
      361 qslslpsmlr daaigttpfs tcsvgtwftp sapqekstnt sqtglvgtkh stseteqllc
      421 grppdltals rhdlednlls slvilevlsr qlrdwksqla vphpetqdss tqtdtshsgi
      481 tnklqhlkes hemgqalqqa rnvmqswvli skelisllhl sllhleedkt tvsqesrrae
      541 tlvcccfdll kklraklqsl kaereearhr eemalrgkda aeivleafca hasqrisqle
      601 qdlasmrefr gllkdaqtql vglhakqeel vqqtvsltst lqqdwrsmql dyttwtalls
      661 rsrqlteklt vksqqalqer dvaieekqev srvleqvsaq leeckgqteq lelensrlat
      721 dlraqlqila nmdsqlkelq sqhthcaqdl amkdellcql tqsneeqaaq wqkeemalkh
      781 mqaelqqqqa vlakevrdlk etlefadqen qvahlelgqv ecqlkttlev lrerslqcen
      841 lkdtvenlta klastiadnq eqdlektrqy sqklgllteq lqsltlflqt klkekteqet
      901 lllstacppt qehplpndrt flgsiltava deepestpvp llgsdksaft rvasmvslqp
      961 aetpgmeesl aemsimttel qslcsllqes keeairtlqr kicelqarlq aqeeqhqevq
     1021 kakeadiekl nqalclrykn ekelqeviqq qnekileqid ksgelislre evthltrslr
     1081 raetetkvlq ealagqldsn cqpmatnwiq ekvwlsqevd klrvmflemk nekeklmikf
     1141 qshrnileen lrrsdkelek lddivqhiyk tllsipevvr gckelqglle fls
//
LOCUS       NP_001341017             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341017 XP_016879173
VERSION     NP_001341017.1
DBSOURCE    REFSEQ: accession NM_001354088.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 29, 2017 this sequence version replaced XP_016879173.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AL834421.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354088.2:586..1350"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_000807                467 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit gamma-2 isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_000807
VERSION     NP_000807.2
DBSOURCE    REFSEQ: accession NM_000816.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Sui,J., Zhan,L., Ji,S., Wu,W., Chen,Y., Yun,F., Liang,W., Wang,J.,
            Cao,M., Shen,D. and Zhang,Q.
  TITLE     Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations
  JOURNAL   CNS Neurosci Ther 30 (2), e14583 (2024)
   PUBMED   38357846
  REMARK    GeneRIF: Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations.
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Ma,M., Zhao,J., Xie,D. and Chen,J.
  TITLE     Association between GABRG2 Gene Single Nucleotide Polymorphisms and
            Susceptibility to Ischemic Stroke in a Chinese Population
  JOURNAL   J Integr Neurosci 22 (6), 151 (2023)
   PUBMED   38176934
  REMARK    GeneRIF: Association between GABRG2 Gene Single Nucleotide
            Polymorphisms and Susceptibility to Ischemic Stroke in a Chinese
            Population.
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Kostrzewa,M., Kohler,A., Eppelt,K., Hellam,L., Fairweather,N.D.,
            Levy,E.R., Monaco,A.P. and Muller,U.
  TITLE     Assignment of genes encoding GABAA receptor subunits alpha 1, alpha
            6, beta 2, and gamma 2 to a YAC contig of 5q33
  JOURNAL   Eur J Hum Genet 4 (4), 199-204 (1996)
   PUBMED   8875185
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Moss,S.J., Doherty,C.A. and Huganir,R.L.
  TITLE     Identification of the cAMP-dependent protein kinase and protein
            kinase C phosphorylation sites within the major intracellular
            domains of the beta 1, gamma 2S, and gamma 2L subunits of the
            gamma-aminobutyric acid type A receptor
  JOURNAL   J Biol Chem 267 (20), 14470-14476 (1992)
   PUBMED   1321150
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Wilcox,A.S., Warrington,J.A., Gardiner,K., Berger,R., Whiting,P.,
            Altherr,M.R., Wasmuth,J.J., Patterson,D. and Sikela,J.M.
  TITLE     Human chromosomal localization of genes encoding the gamma 1 and
            gamma 2 subunits of the gamma-aminobutyric acid receptor indicates
            that members of this gene family are often clustered in the genome
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5857-5861 (1992)
   PUBMED   1321425
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA226729.1, BC074795.2,
            BC069348.1 and AC091984.3.
            
            On Dec 5, 2003 this sequence version replaced NP_000807.1.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammlian brain, where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene have been associated
            with epilepsy and febrile seizures. Multiple transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons, compared to variant 3. It encodes isoform 2 which is shorter
            than isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.79118.1,
                                           SRR1803615.59162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..467
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 2 precursor"
                     /note="gamma-aminobutyric acid receptor subunit gamma-2;
                     GABA(A) receptor subunit gamma-2; GABA(A) receptor, gamma
                     2; gamma-aminobutyric acid (GABA) A receptor, gamma 2;
                     gamma-aminobutyric acid type A receptor gamma2 subunit;
                     GABAAR subunit gamma-2"
                     /calculated_mol_wt=49854
     sig_peptide     1..39
                     /calculated_mol_wt=4327
     mat_peptide     40..467
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 2"
                     /calculated_mol_wt=49854
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18507.3)"
     Region          69..464
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          90..271
                     /region_name="LGIC_ECD_GABAAR_G"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit gamma; cd19000"
                     /db_xref="CDD:349801"
     Site            order(97,116)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349801"
     Site            order(100,102..103,108..109,116,118..119,136,138..139,
                     148..153,156,158,160..161,167..169,171,181..183,211,271)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349801"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P18507.3)"
     Region          190..204
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349801"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29950725,
                     ECO:0000269|PubMed:30602789, ECO:0007744|PDB:6D6T,
                     ECO:0007744|PDB:6I53; propagated from UniProtKB/Swiss-Prot
                     (P18507.3)"
     Site            276..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18507.3)"
     Site            303..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18507.3)"
     Site            335..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18507.3)"
     Region          425..442
                     /region_name="Interaction with GABARAP.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P18507.3)"
     Site            444..464
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P18507.3)"
     CDS             1..467
                     /gene="GABRG2"
                     /gene_synonym="CAE2; DEE74; ECA2; EIEE74; FEB8; GEFSP3"
                     /coded_by="NM_000816.3:359..1762"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS4358.1"
                     /db_xref="GeneID:2566"
                     /db_xref="HGNC:HGNC:4087"
                     /db_xref="MIM:137164"
ORIGIN      
        1 msspniwstg ssvystpvfs qkmtvwilll lslypgftsq ksdddyedya snktwvltpk
       61 vpegdvtvil nnllegydnk lrpdigvkpt lihtdmyvns igpvnainme ytidiffaqt
      121 wydrrlkfns tikvlrlnsn mvgkiwipdt ffrnskkada hwittpnrml riwndgrvly
      181 tlrltidaec qlqlhnfpmd ehscplefss ygypreeivy qwkrssvevg dtrswrlyqf
      241 sfvglrntte vvkttsgdyv vmsvyfdlsr rmgyftiqty ipctlivvls wvsfwinkda
      301 vpartslgit tvltmttlst iarkslpkvs yvtamdlfvs vcfifvfsal veygtlhyfv
      361 snrkpskdkd kkkknpapti dirprsatiq mnnathlqer deeygyecld gkdcasffcc
      421 fedcrtgawr hgrihiriak mdsyariffp tafclfnlvy wvsylyl
//
LOCUS       NP_071322                567 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_071322
VERSION     NP_071322.2
DBSOURCE    REFSEQ: accession NM_022039.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Song,W., Fu,J., Wu,J., Ren,J., Xiang,R., Kong,C. and Fu,T.
  TITLE     CircFBXW4 Suppresses Colorectal Cancer Progression by Regulating
            the MiR-338-5p/SLC5A7 Axis
  JOURNAL   Adv Sci (Weinh) 11 (18), e2300129 (2024)
   PUBMED   38461489
  REMARK    GeneRIF: CircFBXW4 Suppresses Colorectal Cancer Progression by
            Regulating the MiR-338-5p/SLC5A7 Axis.
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 567)
  AUTHORS   de Mollerat,X.J., Gurrieri,F., Morgan,C.T., Sangiorgi,E.,
            Everman,D.B., Gaspari,P., Amiel,J., Bamshad,M.J., Lyle,R.,
            Blouin,J.L., Allanson,J.E., Le Marec,B., Wilson,M., Braverman,N.E.,
            Radhakrishna,U., Delozier-Blanchet,C., Abbott,A., Elghouzzi,V.,
            Antonarakis,S., Stevenson,R.E., Munnich,A., Neri,G. and
            Schwartz,C.E.
  TITLE     A genomic rearrangement resulting in a tandem duplication is
            associated with split hand-split foot malformation 3 (SHFM3) at
            10q24
  JOURNAL   Hum Mol Genet 12 (16), 1959-1971 (2003)
   PUBMED   12913067
  REMARK    GeneRIF: a complex rearrangement associated with a approximately
            0.5 Mb tandem duplication ion containing a disrupted extra copy of
            the DACTYLIN gene and the entire LBX1 and beta-TRCP genes.
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Ianakiev,P., Kilpatrick,M.W., Dealy,C., Kosher,R., Korenberg,J.R.,
            Chen,X.N. and Tsipouras,P.
  TITLE     A novel human gene encoding an F-box/WD40 containing protein maps
            in the SHFM3 critical region on 10q24
  JOURNAL   Biochem Biophys Res Commun 261 (1), 64-70 (1999)
   PUBMED   10405324
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Gurrieri,F., Prinos,P., Tackels,D., Kilpatrick,M.W., Allanson,J.,
            Genuardi,M., Vuckov,A., Nanni,L., Sangiorgi,E., Garofalo,G.,
            Nunes,M.E., Neri,G., Schwartz,C. and Tsipouras,P.
  TITLE     A split hand-split foot (SHFM3) gene is located at 10q24-->25
  JOURNAL   Am J Med Genet 62 (4), 427-436 (1996)
   PUBMED   8723077
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Palmer,S.E., Scherer,S.W., Kukolich,M., Wijsman,E.M., Tsui,L.C.,
            Stephens,K. and Evans,J.P.
  TITLE     Evidence for locus heterogeneity in human autosomal dominant split
            hand/split foot malformation
  JOURNAL   Am J Hum Genet 55 (1), 21-26 (1994)
   PUBMED   7912888
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF281859.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 1, 2018 this sequence version replaced NP_071322.1.
            
            Summary: This gene is a member of the F-box/WD-40 gene family,
            which recruit specific target proteins through their WD-40
            protein-protein binding domains for ubiquitin mediated degradation.
            In mouse, a highly similar protein is thought to be responsible for
            maintaining the apical ectodermal ridge of developing limb buds;
            disruption of the mouse gene results in the absence of central
            digits, underdeveloped or absent metacarpal/metatarsal bones and
            syndactyly. This phenotype is remarkably similar to split
            hand-split foot malformation in humans, a clinically heterogeneous
            condition with a variety of modes of transmission. An autosomal
            recessive form has been mapped to the chromosomal region where this
            gene is located, and complex rearrangements involving duplications
            of this gene and others have been associated with the condition. A
            pseudogene of this locus has been mapped to one of the introns of
            the BCR gene on chromosome 22. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF281859.1, SRR1163655.35849.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331272.9/ ENSP00000359149.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..567
                     /product="F-box/WD repeat-containing protein 4 isoform 1"
                     /note="F-box and WD-40 domain protein 4; F-box/WD repeat
                     protein 4; dactylin; F-box/WD repeat-containing protein 4;
                     F-box and WD-40 domain-containing protein 4; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=61681
     Region          183..228
                     /region_name="F-box_FBXW4"
                     /note="F-box domain found in F-box/WD repeat-containing
                     protein 4 (FBXW4) and similar proteins; cd20090"
                     /db_xref="CDD:438853"
     Site            order(186,190,193..194,197..198,202,204..205,209..211,213)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438853"
     Region          307..545
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          361..397
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          402..442
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          452..488
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          495..531
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..567
                     /gene="FBXW4"
                     /gene_synonym="DAC; FBW4; FBWD4; SHFM3; SHSF3"
                     /coded_by="NM_022039.4:66..1769"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31271.2"
                     /db_xref="GeneID:6468"
                     /db_xref="HGNC:HGNC:10847"
                     /db_xref="MIM:608071"
ORIGIN      
        1 mgsqgrsgpp gnggpgegeg gearklqegr vargkrrkgk gkgkaragqg grgsgaegkp
       61 gpqtakeaag pgadagarac preeaeggrs veegargivk gvegsagagk eaqgreygkk
      121 eewrvrarrr egarpgraqg rggqawadia gtgvamaaaa geeeeeeeaa resaarpaag
      181 palwrlpeel lllicsyldm ralgrlaqvc rwlrrftscd llwrriaras lnsgftrlgt
      241 dlmtsvpvke rvkvsqnwrl grcregillk wrcsqmpwmq leddslyisq anfilayqfr
      301 pdgaslnrrp lgvfaghded vchfvlansh ivsaggdgki gihkihstft vkysaheqev
      361 ncvdckggii vsgsrdrtak vwplasgrlg qclhtiqted rvwsiaispl lssfvtgtac
      421 cghfsplriw dlnsgqlmth lgsdfppgag vldvmyespf tllscgydty vrywdlrtsv
      481 rkcvmeweep hdstlyclqt dgnhllatgs syygvvrlwd rrqraclhaf pltstplssp
      541 vyclrlttkh lyaalsynlh vldfqnp
//
LOCUS       NP_064623                914 aa            linear   PRI 20-NOV-2025
DEFINITION  inner centromere protein isoform 2 [Homo sapiens].
ACCESSION   NP_064623
VERSION     NP_064623.2
DBSOURCE    REFSEQ: accession NM_020238.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Redouane,S., Charoute,H., Harmak,H., Malki,A., Barakat,A. and
            Rouba,H.
  TITLE     Computational study of the potential impact of AURKC missense SNPs
            on AURKC-INCENP interaction and their correlation to
            macrozoospermia
  JOURNAL   J Biomol Struct Dyn 41 (19), 9503-9522 (2023)
   PUBMED   36326488
  REMARK    GeneRIF: Computational study of the potential impact of AURKC
            missense SNPs on AURKC-INCENP interaction and their correlation to
            macrozoospermia.
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Ibrahim,A., Miligy,I.M., Toss,M.S., Green,A.R. and Rakha,E.A.
  TITLE     High Inner Centromere Protein Expression Correlates with Aggressive
            Features and Predicts Poor Prognosis in Patients with Invasive
            Breast Cancer
  JOURNAL   Pathobiology 90 (6), 377-388 (2023)
   PUBMED   37031675
  REMARK    GeneRIF: High Inner Centromere Protein Expression Correlates with
            Aggressive Features and Predicts Poor Prognosis in Patients with
            Invasive Breast Cancer.
REFERENCE   4  (residues 1 to 914)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 914)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 914)
  AUTHORS   Ainsztein,A.M., Kandels-Lewis,S.E., Mackay,A.M. and Earnshaw,W.C.
  TITLE     INCENP centromere and spindle targeting: identification of
            essential conserved motifs and involvement of heterochromatin
            protein HP1
  JOURNAL   J Cell Biol 143 (7), 1763-1774 (1998)
   PUBMED   9864353
REFERENCE   7  (residues 1 to 914)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 914)
  AUTHORS   Martineau-Thuillier,S., Andreassen,P.R. and Margolis,R.L.
  TITLE     Colocalization of TD-60 and INCENP throughout G2 and mitosis:
            evidence for their possible interaction in signalling cytokinesis
  JOURNAL   Chromosoma 107 (6-7), 461-470 (1998)
   PUBMED   9914378
REFERENCE   9  (residues 1 to 914)
  AUTHORS   Earnshaw,W.C. and Mackay,A.M.
  TITLE     Role of nonhistone proteins in the chromosomal events of mitosis
  JOURNAL   FASEB J 8 (12), 947-956 (1994)
   PUBMED   8088460
  REMARK    Review article
REFERENCE   10 (residues 1 to 914)
  AUTHORS   Earnshaw,W.C. and Cooke,C.A.
  TITLE     Analysis of the distribution of the INCENPs throughout mitosis
            reveals the existence of a pathway of structural changes in the
            chromosomes during metaphase and early events in cleavage furrow
            formation
  JOURNAL   J Cell Sci 98 (Pt 4), 443-461 (1991)
   PUBMED   1860899
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC098576.1, CV569756.1, BC032678.1, AW839685.1, BC111732.1 and
            AP002793.4.
            
            On May 26, 2006 this sequence version replaced NP_064623.1.
            
            Summary: In mammalian cells, 2 broad groups of
            centromere-interacting proteins have been described: constitutively
            binding centromere proteins and 'passenger,' or transiently
            interacting, proteins (reviewed by Choo, 1997). The constitutive
            proteins include CENPA (centromere protein A; MIM 117139), CENPB
            (MIM 117140), CENPC1 (MIM 117141), and CENPD (MIM 117142). The term
            'passenger proteins' encompasses a broad collection of proteins
            that localize to the centromere during specific stages of the cell
            cycle (Earnshaw and Mackay, 1994 [PubMed 8088460]). These include
            CENPE (MIM 117143); MCAK (MIM 604538); KID (MIM 603213);
            cytoplasmic dynein (e.g., MIM 600112); CliPs (e.g., MIM 179838);
            and CENPF/mitosin (MIM 600236). The inner centromere proteins
            (INCENPs) (Earnshaw and Cooke, 1991 [PubMed 1860899]), the initial
            members of the passenger protein group, display a broad
            localization along chromosomes in the early stages of mitosis but
            gradually become concentrated at centromeres as the cell cycle
            progresses into mid-metaphase. During telophase, the proteins are
            located within the midbody in the intercellular bridge, where they
            are discarded after cytokinesis (Cutts et al., 1999 [PubMed
            10369859]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF282265.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..914
                     /product="inner centromere protein isoform 2"
                     /note="inner centromere protein INCENP; binds and
                     activates aurora-B and -C in vivo and in vitro;
                     chromosomal passenger protein; inner centromere protein
                     antigens 135/155kDa"
                     /calculated_mol_wt=104862
     Region          6..41
                     /region_name="INCENP_N"
                     /note="Chromosome passenger complex (CPC) protein INCENP N
                     terminal; pfam12178"
                     /db_xref="CDD:463484"
     Region          48..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          124..248
                     /region_name="Interaction with CBX5.
                     /evidence=ECO:0000269|PubMed:21346195"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          138..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          <141..>287
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          <142..513
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU62; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          167..171
                     /region_name="PXVXL/I motif.
                     /evidence=ECO:0000305|PubMed:21346195"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          190..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:15316025; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU62; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          285..316
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          371..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU62; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WU62; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          <531..>780
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          603..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          656..736
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          750..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          818..893
                     /region_name="Interaction with AURKC.
                     /evidence=ECO:0000269|PubMed:27332895"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          822..896
                     /region_name="IN box. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          822..841
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Region          823..877
                     /region_name="INCENP_ARK-bind"
                     /note="Inner centromere protein, ARK binding region;
                     pfam03941"
                     /db_xref="CDD:461100"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB and AURKC.
                     /evidence=ECO:0000269|PubMed:12925766,
                     ECO:0000269|PubMed:27332895; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            889
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and AURKC.
                     /evidence=ECO:0000269|PubMed:12925766,
                     ECO:0000269|PubMed:27332895; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and AURKC.
                     /evidence=ECO:0000269|PubMed:12925766,
                     ECO:0000269|PubMed:27332895, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            895
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS7.3)"
     CDS             1..914
                     /gene="INCENP"
                     /coded_by="NM_020238.3:165..2909"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31582.1"
                     /db_xref="GeneID:3619"
                     /db_xref="HGNC:HGNC:6058"
                     /db_xref="MIM:604411"
ORIGIN      
        1 mgttapgpih llelcdqklm eflcnmdnkd lvwleeiqee aermftrefs kepelmpktp
       61 sqknrrkkrr isyvqdenrd pirrrlsrrk srssqlssrr lrskdsvekl atvvgengsv
      121 lrrvtraaaa aaaatmalaa pssptpespt mltkkpednh tqcqlvpvve igiserqnae
      181 qhvtqlmste plprtlsptp asataptsqg iptsdeestp kkskariles itvsslmatp
      241 qdpkgqgvgt grsasklria qvspgprdsp afpdspwrer vlapilpdnf stptgsrtds
      301 qsvrhspiap sspspqvlaq kyslvakqes vvrrasrrla kktaeepaas griichsyle
      361 rllnvevpqk vgseqkeppe eaepvaaaep evpenngnns wphndteian stpnpkpaas
      421 spetpsagqq eaktdqadgp reppqsarrk rsykqavsel deeqhledee lqpprsktps
      481 spcpaskvvr plrtflhtvq rnqmlmtpts aprsvmksfi krntplrmdp kekerqrlen
      541 lrrkeeaeql rrqkveedkr rrleevklkr eerlrkvlqa rerveqmkee kkkqieqkfa
      601 qidektekak eerlaeekak kkaaakkmee vearrkqeee arrlrwlqqe eeerrhqell
      661 qkkkeeeqer lrkaaeakrl aeqreqerre qerreqerre qerreqerre qerqlaeqer
      721 rreqerlqae relqerekal rlqkeqlqre leekkkkeeq qrlaerqlqe eqekkakeaa
      781 gaskalnvtv dvqspactsy qmtpqghrap pkinpdnygm dlnsddstdd eahprkpipt
      841 wargtplsqa iihqyyhppn llelfgtilp ldledifkks kpryhkrtss avwnspplqg
      901 arvpsslays lkkh
//
LOCUS       NP_001308473             318 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial coenzyme A transporter SLC25A42 [Homo sapiens].
ACCESSION   NP_001308473 XP_011526238
VERSION     NP_001308473.1
DBSOURCE    REFSEQ: accession NM_001321544.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,R., Zhang,Z., Kyaw,A.K., Grabinska,K.A., Shah,H. and Shen,H.
  TITLE     Cellular pan-chain acyl-CoA profiling reveals SLC25A42/SLC25A16 in
            mitochondrial CoA import and metabolism
  JOURNAL   Nat Metab 7 (9), 1871-1888 (2025)
   PUBMED   40925986
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Taga,K. and Takeuchi,H.
  TITLE     Novel role of host protein SLC25A42 in the HIV-1 reactivation of
            latent HIV-1 provirus
  JOURNAL   Microbiol Immunol 68 (3), 90-99 (2024)
   PUBMED   38244193
  REMARK    GeneRIF: Novel role of host protein SLC25A42 in the HIV-1
            reactivation of latent HIV-1 provirus.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Almannai,M., Alasmari,A., Alqasmi,A., Faqeih,E., Al Mutairi,F.,
            Alotaibi,M., Samman,M.M., Eyaid,W., Aljadhai,Y.I., Shamseldin,H.E.,
            Craigen,W. and Alkuraya,F.S.
  TITLE     Expanding the phenotype of SLC25A42-associated mitochondrial
            encephalomyopathy
  JOURNAL   Clin Genet 93 (5), 1097-1102 (2018)
   PUBMED   29327420
  REMARK    GeneRIF: our report confirms the link between SLC25A42 and
            mitochondrial disease in humans, and suggests that pathogenic
            variants in SLC25A42 should be interpreted with the understanding
            that the associated phenotype may be highly variable.
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Palmieri,F.
  TITLE     The mitochondrial transporter family SLC25: identification,
            properties and physiopathology
  JOURNAL   Mol Aspects Med 34 (2-3), 465-484 (2013)
   PUBMED   23266187
  REMARK    GeneRIF: Compares and contrasts all the known human SLC25A* genes
            and includes functional information.
            Review article
REFERENCE   7  (residues 1 to 318)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Fiermonte,G., Paradies,E., Todisco,S., Marobbio,C.M. and
            Palmieri,F.
  TITLE     A novel member of solute carrier family 25 (SLC25A42) is a
            transporter of coenzyme A and adenosine 3',5'-diphosphate in human
            mitochondria
  JOURNAL   J Biol Chem 284 (27), 18152-18159 (2009)
   PUBMED   19429682
  REMARK    GeneRIF: The main physiological role of SLC25A42 is to import CoA
            into mitochondria in exchange for intramitochondrial (deoxy)adenine
            nucleotides and adenosine 3',5'-diphosphate
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Haitina,T., Lindblom,J., Renstrom,T. and Fredriksson,R.
  TITLE     Fourteen novel human members of mitochondrial solute carrier family
            25 (SLC25) widely expressed in the central nervous system
  JOURNAL   Genomics 88 (6), 779-790 (2006)
   PUBMED   16949250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC003038.1, AC004143.1,
            AC002126.1 and BX099926.1.
            
            On Mar 26, 2016 this sequence version replaced XP_011526238.1.
            
            Summary: This gene encodes a solute carrier family 25 protein.
            Solute carrier family 25 proteins are localized to mitochondria and
            play critical roles in the transport of molecules across the inner
            mitochondrial membrane. The encoded protein is a mitochondrial
            transporter for coenzyme A (CoA) and adenosine 3',5'-diphosphate.
            [provided by RefSeq, Feb 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.105956.1,
                                           SRR1163655.366358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..318
                     /product="mitochondrial coenzyme A transporter SLC25A42"
                     /calculated_mol_wt=35278
     Region          31..117
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          34..295
                     /region_name="PTZ00169"
                     /note="ADP/ATP transporter on adenylate translocase;
                     Provisional"
                     /db_xref="CDD:240302"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          129..214
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          224..312
                     /region_name="Solcar 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     CDS             1..318
                     /gene="SLC25A42"
                     /gene_synonym="MECREN"
                     /coded_by="NM_001321544.2:88..1044"
                     /db_xref="CCDS:CCDS32966.1"
                     /db_xref="GeneID:284439"
                     /db_xref="HGNC:HGNC:28380"
                     /db_xref="MIM:610823"
ORIGIN      
        1 mgngvkegpv rlhedaeavl sssvsskrdh rqvlssllsg alagalakta vapldrtkii
       61 fqvsskrfsa keafrvlyyt ylnegflslw rgnsatmvrv vpyaaiqfsa heeykrilgs
      121 yygfrgealp pwprlfagal agttaaslty pldlvrarma vtpkemysni fhvfirisre
      181 eglktlyhgf mptvlgvipy aglsfftyet lkslhreysg rrqpypferm ifgacaglig
      241 qsasypldvv rrrmqtagvt gyprasiart lrtivreega vrglykglsm nwvkgpiavg
      301 isfttfdlmq illrhlqs
//
LOCUS       NP_680480                520 aa            linear   PRI 20-NOV-2025
DEFINITION  RING-type E3 ubiquitin-protein ligase PPIL2 isoform a [Homo
            sapiens].
ACCESSION   NP_680480
VERSION     NP_680480.1
DBSOURCE    REFSEQ: accession NM_148175.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Carson,R., McKnight,A.J., Todd,S., Liu,W.W., Heggarty,S., Craig,D.,
            McGuinness,B., Irvine,G.B., Passmore,A.P. and Johnston,J.A.
  TITLE     Variation in RTN3 and PPIL2 genes does not influence platelet
            membrane beta-secretase activity or susceptibility to alzheimer's
            disease in the northern Irish population
  JOURNAL   Neuromolecular Med 11 (4), 337-344 (2009)
   PUBMED   19669607
  REMARK    GeneRIF: common genetic variation in the BACE1-interacting
            proteins, RTN3 an PPIL2, does not influence platelet b-secretase
            activity or susceptibility to Alzheimer's disease in this
            population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Pushkarsky,T., Yurchenko,V., Vanpouille,C., Brichacek,B.,
            Vaisman,I., Hatakeyama,S., Nakayama,K.I., Sherry,B. and
            Bukrinsky,M.I.
  TITLE     Cell surface expression of CD147/EMMPRIN is regulated by
            cyclophilin 60
  JOURNAL   J Biol Chem 280 (30), 27866-27871 (2005)
   PUBMED   15946952
  REMARK    GeneRIF: cyclophilin 60 regulates cell surface expression of
            CD147/EMMPRIN
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Hatakeyama,S., Yada,M., Matsumoto,M., Ishida,N. and Nakayama,K.I.
  TITLE     U box proteins as a new family of ubiquitin-protein ligases
  JOURNAL   J Biol Chem 276 (35), 33111-33120 (2001)
   PUBMED   11435423
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Wang,B.B., Hayenga,K.J., Payan,D.G. and Fisher,J.M.
  TITLE     Identification of a nuclear-specific cyclophilin which interacts
            with the proteinase inhibitor eglin c
  JOURNAL   Biochem J 314 (Pt 1) (Pt 1), 313-319 (1996)
   PUBMED   8660300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA863607.1, BC028385.2,
            U37221.1, AK127259.1, AA743164.1 and AP000553.1.
            
            Summary: This gene is a member of the cyclophilin family of
            peptidylprolyl isomerases. The cyclophilins are a highly conserved
            ubiquitous family, members of which play an important role in
            protein folding, immunosuppression by cyclosporin A, and infection
            of HIV-1 virions. This protein interacts with the proteinase
            inhibitor eglin c and is localized in the nucleus. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) lacks a segment in the 3' UTR
            compared to variant 1. Variants 1, 2 and 4 encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.77930.1,
                                           SRR1803617.56682.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21-q11.22"
     Protein         1..520
                     /product="RING-type E3 ubiquitin-protein ligase PPIL2
                     isoform a"
                     /EC_number="2.3.2.27"
                     /note="peptidylprolyl cis-trans isomerase;
                     cyclophilin-like protein CyP-60; peptidyl-prolyl cis-trans
                     isomerase-like 2; cyclophilin, 60kDa; PPIase;
                     cyclophilin-60; rotamase PPIL2; U-box domain containing 7;
                     peptidylprolyl isomerase (cyclophilin)-like 2; RING-type
                     E3 ubiquitin transferase isomerase-like 2; probable
                     inactive peptidyl-prolyl cis-trans isomerase-like 2;
                     RING-type E3 ubiquitin-protein ligase PPIL2"
                     /calculated_mol_wt=58693
     Region          38..110
                     /region_name="RING-Ubox_PPIL2"
                     /note="U-box domain, a modified RING finger, found in
                     peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and
                     similar proteins; cd16663"
                     /db_xref="CDD:438325"
     Region          100..159
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(103,106,122,124,127,130,143,146)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438324"
     Region          281..440
                     /region_name="cyclophilin_RING"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases (cyclophilins) having a modified RING finger
                     domain. This group includes the nuclear proteins, Human
                     hCyP-60 and Caenorhabditis elegans MOG-6 which, compared
                     to the archetypal cyclophilin Human...; cd01923"
                     /db_xref="CDD:238904"
     Site            order(322..323,328,379,381,389)
                     /site_type="active"
                     /db_xref="CDD:238904"
     Region          456..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13356.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13356.1)"
     Site            482
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13356.1)"
     CDS             1..520
                     /gene="PPIL2"
                     /gene_synonym="CYC4; Cyp-60; CYP60; hCyP-60; UBOX7"
                     /coded_by="NM_148175.3:89..1651"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13793.1"
                     /db_xref="GeneID:23759"
                     /db_xref="HGNC:HGNC:9261"
                     /db_xref="MIM:607588"
ORIGIN      
        1 mgkrqhqkdk myitcaeyth fyggkkpdlp qtnfrrlpfd hcslslqpfv ypvctpdgiv
       61 fdllnivpwl kkygtnpsng ekldgrslik lnfsknsegk yhcpvlftvf tnnthivavr
      121 ttgnvyayea veqlnikakn frdlltdepf srqdiitlqd ptnldkfnvs nfyhvknnmk
      181 iidpdeekak qdpsyylknt naetretlqe lykefkgdei laatmkapek kkvdklnaah
      241 ystgkvsasf tstamvpett heaaaidedv lryqfvkkkg yvrlhtnkgd lnlelhcdlt
      301 pktcenfirl ckkhyydgti fhrsirnfvi qggdptgtgt ggesywgkpf kdefrpnlsh
      361 tgrgilsman sgpnsnrsqf fitfrscayl dkkhtifgrv vggfdvltam envesdpktd
      421 rpkeeirida ttvfvdpyee adaqiaqerk tqlkvapetk vkssqpqags qgpqtfrqgv
      481 gkyinpaatk raaeeepsts atvpmskkkp srgfgdfssw
//
LOCUS       NP_001305638             609 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of MON1-CCZ1 complex isoform 5 [Homo sapiens].
ACCESSION   NP_001305638 XP_011524240
VERSION     NP_001305638.1
DBSOURCE    REFSEQ: accession NM_001318709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Yong,X., Jia,G., Liu,Z., Zhou,C., Yi,J., Tang,Y., Chen,L., Chen,L.,
            Wang,Y., Sun,Q., Billadeau,D.D., Su,Z. and Jia,D.
  TITLE     Cryo-EM structure of the Mon1-Ccz1-RMC1 complex reveals molecular
            basis of metazoan RAB7A activation
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2301725120 (2023)
   PUBMED   37216550
REFERENCE   2  (residues 1 to 609)
  AUTHORS   van den Boomen,D.J.H., Sienkiewicz,A., Berlin,I., Jongsma,M.L.M.,
            van Elsland,D.M., Luzio,J.P., Neefjes,J.J.C. and Lehner,P.J.
  TITLE     A trimeric Rab7 GEF controls NPC1-dependent lysosomal cholesterol
            export
  JOURNAL   Nat Commun 11 (1), 5559 (2020)
   PUBMED   33144569
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Vaites,L.P., Paulo,J.A., Huttlin,E.L. and Harper,J.W.
  TITLE     Systematic Analysis of Human Cells Lacking ATG8 Proteins Uncovers
            Roles for GABARAPs and the CCZ1/MON1 Regulator C18orf8/RMC1 in
            Macroautophagic and Selective Autophagic Flux
  JOURNAL   Mol Cell Biol 38 (1), e00392-17 (2017)
   PUBMED   29038162
  REMARK    GeneRIF: Authors identified C18orf8/RMC1 as a new subunit of the
            CCZ1-MON1 RAB7 guanine exchange factor (GEF) that positively
            regulates RAB7 recruitment to LE/autophagosomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Yuan,M., Chen,J. and Zeng,Z.
  TITLE     Knockdown of macrophage inhibitory cytokine-1 in RPMI-8226 human
            multiple myeloma cells inhibits osteoclastic differentiation
            through inhibiting the RANKL-Erk1/2 signaling pathway
  JOURNAL   Mol Med Rep 14 (6), 5199-5204 (2016)
   PUBMED   27779672
REFERENCE   6  (residues 1 to 609)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026634.11, DC383182.1, AK296230.1 and BC008305.1.
            
            On Jan 8, 2016 this sequence version replaced XP_011524240.1.
            
            Summary: This gene encodes a colon cancer associated protein.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (5) lacks two consecutive in-frame
            exons in the 5' coding region. The encoded isoform (5) is shorter
            than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296230.1, SRR1803614.110380.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..609
                     /product="regulator of MON1-CCZ1 complex isoform 5"
                     /note="colon cancer-associated protein Mic1; macrophage
                     inhibitory cytokine 1; uncharacterized protein C18orf8; WD
                     repeat domain 98; WD repeat-containing protein 98;
                     regulator of MON1-CCZ1 complex"
                     /calculated_mol_wt=69259
     Region          427..584
                     /region_name="Mic1"
                     /note="Colon cancer-associated protein Mic1-like;
                     pfam07035"
                     /db_xref="CDD:429257"
     CDS             1..609
                     /gene="RMC1"
                     /gene_synonym="C18orf8; HsT2591; Mic-1; MIC1; WDR98"
                     /coded_by="NM_001318709.1:150..1979"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82243.1"
                     /db_xref="GeneID:29919"
                     /db_xref="HGNC:HGNC:24326"
                     /db_xref="MIM:620267"
ORIGIN      
        1 mgeedyylel cerpvqfeka npvncvffde ankqvfavrs ggatgvvvkg pddrnpisfr
       61 mddkgevkci kfslenkila vqrtsktvvl pekrslkllk shnlnvnwym ycpesavill
      121 sttvlenvlq pfhfragtms klpkfeielp aapkstkpsl serdiamati ygqlyvlflr
      181 hhsrtsnstg aevvlyhlpr egackkmhil klnrtgkfal nvvdnlvvvh hqdtetsvif
      241 diklrgefdg svtfhhpvlp arsiqpyqip itgpaavtsq spvpcklyss swivfqpdii
      301 isasqgylwn lqvklepivn llpdkgrlmd fllqrkeckm vilsvcsqml sesdraslpv
      361 iatvfdklnh eykkyldaeq syamaveagq srsspllkrp vrtqavldqs dvythvlsaf
      421 vekkemphkf viavlmeyir slnqfqiavq hylhelvikt lvqhnlfyml hqflqyhvls
      481 dskplaclll slesfyppah qlsldmlkrl standeivev llskhqvlaa lrfirgiggh
      541 dnisarkfld aakqtednml fytifrffeq rnqrlrgspn ftpgehceeh vaffkqifgd
      601 qalmrpttf
//
LOCUS       NP_001310867             920 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001310867
VERSION     NP_001310867.1
DBSOURCE    REFSEQ: accession NM_001323938.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.183177.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..920
                     /product="DIS3-like exonuclease 1 isoform 3"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=104881
     Region          <1..54
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          104..732
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          747..822
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..920
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323938.2:359..3121"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mekwqtrsiy naavwyyhhc qdrmpivmvt edeeaiqqyg setegvfvit fknyldnfwp
       61 dlkaahelcd silqsrrere nesqeshgke ypehlplevl eagiksgryi qgilnvnkhr
      121 aqieafvrlq gasskdsdlv sdilihgmka rnrsihgdvv vvellpknew kgrtvalcen
      181 dcddkasges psepmptgrv vgilqknwrd yvvtfpskee vqsqgknaqk ilvtpwdyri
      241 pkiristqqa etlqdfrvvv ridswestsv ypnghfvrvl grigdlegei atilvensis
      301 vipfseaqmc empvntpesp wkvspeeeqk rkdlrkshlv fsidpkgced vddtlsvrtl
      361 nngnlelgvh iadvthfvap nsyidieart rattyyladr rydmlpsvls adlcsllggv
      421 dryavsimwe ldkasyeikk vwygrtiirs ayklfyeaaq elldgnlsvv ddipefkdld
      481 eksrqaklee lvwaigkltd iarhvrakrd gcgalelegv evcvqlddkk nihdlipkqp
      541 levhetvaec milanhwvak kiwesfphqa llrqhppphq effselreca kakgffidtr
      601 snktladsld nandphdpiv nrllrsmatq amsnalyfst gscaeeefhh yglaldkyth
      661 ftspirrysd ivvhrllmaa iskdkkmeik gnlfsnkdle elcrhinnrn qaaqhsqkqs
      721 telfqcmyfk dkdpateerc isdgviysir tngvllfipr fgikgaaylk nkdglviscg
      781 pdscsewkpg slqrfqnkit stttdgesvt fhlfdhvtvr isiqasrchs dtirleiisn
      841 kpykipntel ihqsspllks elvkevtksv eeaqlaqevk vniiqeeyqe yrqtkgrsly
      901 tlleeirdla lldvsnnygi
//
LOCUS       NP_001340039             541 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform b [Homo sapiens].
ACCESSION   NP_001340039
VERSION     NP_001340039.1
DBSOURCE    REFSEQ: accession NM_001353110.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 541)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, AC026117.15,
            AC139764.5, AC109912.10 and BC014050.2.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.135559.1,
                                           SRR1803611.162437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..541
                     /product="centrosomal protein of 63 kDa isoform b"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=62884
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <136..464
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     CDS             1..541
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001353110.1:355..1980"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS43153.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveair preeslaekk ytsqgqgdld svlsqlnfth tsedllqaev tclegslesv
      361 satckqlsqe lmekyeelkr meahnneyka eikklkeqil qgeqsyssal egmkmeishl
      421 tqelhqrdit iastkgsssd mekrlraemq kaedkavehk eildqleslk lenrhlsemv
      481 mklelglhec slpvsplgsi atrfleeeel rshhilerld ahieelkres ektvrqftal
      541 k
//
LOCUS       NP_001356023             357 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001356023
VERSION     NP_001356023.1
DBSOURCE    REFSEQ: accession NM_001369094.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.216239.1,
                                           SRR1660805.40619.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..357
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform b"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=41097
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..356
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..357
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369094.1:214..1287"
                     /note="isoform b is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS31219.1"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkl fenfyfgslk lnsihisqrf tvdsfgnyas cgqidfs
//
LOCUS       NP_001353151             821 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 15 [Homo sapiens].
ACCESSION   NP_001353151 XP_016861311
VERSION     NP_001353151.1
DBSOURCE    REFSEQ: accession NM_001366222.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 821)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861311.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.579.1,
                                           SRR1803617.185655.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..821
                     /product="disks large homolog 1 isoform 15"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=90496
     Region          <105..140
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          139..227
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(150..156,173,176,206,210,213..214)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          236..320
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(245..251,268,271,301,305,308..309)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          321..382
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          380..470
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(392..398,409,412,442,446,449..450)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          499..565
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(504,526..527,548)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(507,509,512,521,539..540,559,561..562)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          630..808
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..821
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366222.1:65..2530"
                     /note="isoform 15 is encoded by transcript variant 31"
                     /db_xref="CCDS:CCDS93447.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mnyifgnntl lysrgsrggn tssshgsagp kqkhwakkgs sdelqaepep srwqqivaff
       61 trrhsfidci svatsstqpt eavlpspptv pvipvlpvpa entvilptip qanpppvlvn
      121 tdsletptyv ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga
      181 aaqdgrlrvn dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli
      241 kgpkglgfsi aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt
      301 heeavtalkn tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas
      361 paryspvska vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls
      421 gelrkgdrii svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq
      481 mmnssissgs gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew
      541 wqarqvtpdg esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt
      601 snasdsessy rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv
      661 phttrpkrdy evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg
      721 khcildvsgn aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe
      781 ftehftaivq gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_002786                205 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-3 [Homo sapiens].
ACCESSION   NP_002786
VERSION     NP_002786.2
DBSOURCE    REFSEQ: accession NM_002795.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   6  (residues 1 to 205)
  AUTHORS   McCusker,D., Jones,T., Sheer,D. and Trowsdale,J.
  TITLE     Genetic relationships of the genes encoding the human proteasome
            beta subunits and the proteasome PA28 complex
  JOURNAL   Genomics 45 (2), 362-367 (1997)
   PUBMED   9344661
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Nothwang,H.G., Tamura,T., Tanaka,K. and Ichihara,A.
  TITLE     Sequence analyses and inter-species comparisons of three novel
            human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine
            potential proteolytic active-site residues
  JOURNAL   Biochim Biophys Acta 1219 (2), 361-368 (1994)
   PUBMED   7918633
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG942618.1, BC002570.1 and
            BC013008.2.
            
            On Aug 29, 2002 this sequence version replaced NP_002786.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. The 26 S proteasome may be
            involved in trinucleotide repeat expansion, a phenomenon which is
            associated with many hereditary neurological diseases. Pseudogenes
            have been identified on chromosomes 2 and 12. Alternative splicing
            results in multiple transcript variants [provided by RefSeq, Sep
            2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.151399.1,
                                           SRR5189658.160197.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619426.5/ ENSP00000483688.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..205
                     /product="proteasome subunit beta type-3"
                     /EC_number="3.4.25.1"
                     /note="proteasome theta chain; proteasome (prosome,
                     macropain) subunit, beta type, 3; proteasome chain 13;
                     proteasome component C10-II; epididymis secretory sperm
                     binding protein; proteasome subunit beta 3; beta-3"
                     /calculated_mol_wt=22818
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P49720.2)"
     Region          6..201
                     /region_name="proteasome_beta_type_3"
                     /note="proteasome beta type-3 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03759"
                     /db_xref="CDD:239728"
     Site            order(9,25,27,41,141,178,181..182)
                     /site_type="active"
                     /db_xref="CDD:239728"
     Site            order(27,30,32..37,57,59,74,86,89..90,92..93,96,99,125,
                     127,129..132,136,144..145,147..148,151..153,169,176..179,
                     182..183)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239728"
     Site            77
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49720.2)"
     CDS             1..205
                     /gene="PSMB3"
                     /gene_synonym="HC10-II"
                     /coded_by="NM_002795.4:87..704"
                     /db_xref="CCDS:CCDS11328.1"
                     /db_xref="GeneID:5691"
                     /db_xref="HGNC:HGNC:9540"
                     /db_xref="MIM:602176"
ORIGIN      
        1 msimsyngga vmamkgkncv aiaadrrfgi qaqmvttdfq kifpmgdrly iglaglatdv
       61 qtvaqrlkfr lnlyelkegr qikpytlmsm vanllyekrf gpyytepvia gldpktfkpf
      121 icsldligcp mvtddfvvsg tcaeqmygmc eslwepnmdp dhlfetisqa mlnavdrdav
      181 sgmgvivhii ekdkittrtl karmd
//
LOCUS       NP_001352646             753 aa            linear   PRI 20-NOV-2025
DEFINITION  DISP complex protein LRCH3 isoform 5 [Homo sapiens].
ACCESSION   NP_001352646 XP_006713855
VERSION     NP_001352646.1
DBSOURCE    REFSEQ: accession NM_001365717.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 753)
  AUTHORS   O'Loughlin,T., Masters,T.A. and Buss,F.
  TITLE     The MYO6 interactome reveals adaptor complexes coordinating early
            endosome and cytoskeletal dynamics
  JOURNAL   EMBO Rep 19 (4) (2018)
   PUBMED   29467281
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Foussard,H., Ferrer,P., Valenti,P., Polesello,C., Carreno,S. and
            Payre,F.
  TITLE     LRCH proteins: a novel family of cytoskeletal regulators
  JOURNAL   PLoS One 5 (8), e12257 (2010)
   PUBMED   20805893
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055764.23, AC144530.11 and AC135893.2.
            
            On Sep 12, 2018 this sequence version replaced XP_006713855.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.214795.1,
                                           SRR7346977.1975644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..753
                     /product="DISP complex protein LRCH3 isoform 5"
                     /note="leucine-rich repeat and calponin homology
                     domain-containing protein 3; leucine-rich repeats and
                     calponin homology (CH) domain containing 3; DISP complex
                     protein LRCH3"
                     /calculated_mol_wt=83571
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <80..>286
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..145
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          633..741
                     /region_name="CH_LRCH3"
                     /note="calponin homology (CH) domain found in leucine-rich
                     repeat and calponin homology domain-containing protein 3;
                     cd21272"
                     /db_xref="CDD:409121"
     Site            order(634,638,693,695..696,699..700,702,712..720,726,
                     728..729,731..732,735..736,739)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409121"
     CDS             1..753
                     /gene="LRCH3"
                     /coded_by="NM_001365717.1:26..2287"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:84859"
                     /db_xref="HGNC:HGNC:28637"
ORIGIN      
        1 maaaglvava aaaeysgtva sggnlpgvhc gpssgagpgf gpgswsrsld raleeaavtg
       61 vlslsgrklr efprgaanhd ltdttradls rnrlseipie achfvslenl nlyqnciryi
      121 peailnlqal tflnisrnql stlpvhlcnl plkvliasnn klvslpeeig hlrhlmeldv
      181 scneiqtips qignlealrd lnvrrnhlvh lpeelaelpl irldfscnki ttipvcyrnl
      241 rhlqtitldn nplqsppaqi cikgkvhifk ylniqackia pdlpdydrrp lgfgscheel
      301 yssrpygald sgfnsvdsgd krwsgneptd efsdlplrva eitkeqrlrr esqyqenrgs
      361 lvvtnggveh dldqidyids ctaeeeeaev rqpkgpdpds lssqfmayie qrrishegsp
      421 vkpvairefq ktedmrrylh qnrvpaepss llslsashnq lshtdlelhq rreqlvertr
      481 reaqlaalqy eeekirtkqi qrdavldfvk qkasqspqkq hplldgvdge cpfpsrrsqh
      541 tddsalcmsd drpnallssp atetvhhspa ysfpaaiqrn qpqrpesflf ragvraetnk
      601 ghasplppsa apttdstdsi tgqnsrqree elelidqlrk hieyrlkvsl pcdlgaaltd
      661 gvvlchlanh vrprsvpsih vpspavpklt makcrrnven fleacrkigv pqeqlclplh
      721 ileekglsqv avtvqallel appkqqqhql sav
//
LOCUS       NP_001350110             285 aa            linear   PRI 20-NOV-2025
DEFINITION  UBX domain-containing protein 2B isoform 3 [Homo sapiens].
ACCESSION   NP_001350110 XP_005251222
VERSION     NP_001350110.1
DBSOURCE    REFSEQ: accession NM_001363181.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Mirzadeh,A., Kobakhidze,G., Vuillemot,R., Jonic,S. and Rouiller,I.
  TITLE     In silico prediction, characterization, docking studies and
            molecular dynamics simulation of human p97 in complex with p37
            cofactor
  JOURNAL   BMC Mol Cell Biol 23 (1), 39 (2022)
   PUBMED   36088301
  REMARK    GeneRIF: In silico prediction, characterization, docking studies
            and molecular dynamics simulation of human p97 in complex with p37
            cofactor.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Kracht,M., van den Boom,J., Seiler,J., Kroning,A., Kaschani,F.,
            Kaiser,M. and Meyer,H.
  TITLE     Protein Phosphatase-1 Complex Disassembly by p97 is Initiated
            through Multivalent Recognition of Catalytic and Regulatory
            Subunits by the p97 SEP-domain Adapters
  JOURNAL   J Mol Biol 432 (23), 6061-6074 (2020)
   PUBMED   33058883
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Trepte,P., Kruse,S., Kostova,S., Hoffmann,S., Buntru,A.,
            Tempelmeier,A., Secker,C., Diez,L., Schulz,A., Klockmeier,K.,
            Zenkner,M., Golusik,S., Rau,K., Schnoegl,S., Garner,C.C. and
            Wanker,E.E.
  TITLE     LuTHy: a double-readout bioluminescence-based two-hybrid technology
            for quantitative mapping of protein-protein interactions in
            mammalian cells
  JOURNAL   Mol Syst Biol 14 (7), e8071 (2018)
   PUBMED   29997244
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Luca,G., Haba-Rubio,J., Dauvilliers,Y., Lammers,G.J., Overeem,S.,
            Donjacour,C.E., Mayer,G., Javidi,S., Iranzo,A., Santamaria,J.,
            Peraita-Adrados,R., Hor,H., Kutalik,Z., Plazzi,G., Poli,F.,
            Pizza,F., Arnulf,I., Lecendreux,M., Bassetti,C., Mathis,J.,
            Heinzer,R., Jennum,P., Knudsen,S., Geisler,P., Wierzbicka,A.,
            Feketeova,E., Pfister,C., Khatami,R., Baumann,C. and Tafti,M.
  CONSRTM   European Narcolepsy Network
  TITLE     Clinical, polysomnographic and genome-wide association analyses of
            narcolepsy with cataplexy: a European Narcolepsy Network study
  JOURNAL   J Sleep Res 22 (5), 482-495 (2013)
   PUBMED   23496005
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Kress,E., Schwager,F., Holtackers,R., Seiler,J., Prodon,F.,
            Zanin,E., Eiteneuer,A., Toya,M., Sugimoto,A., Meyer,H., Meraldi,P.
            and Gotta,M.
  TITLE     The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by
            limiting the centrosomal recruitment of Aurora A
  JOURNAL   J Cell Biol 201 (4), 559-575 (2013)
   PUBMED   23649807
  REMARK    GeneRIF: human p37/p47 and their C. elegans orthologue UBXN-2
            regulate centrosome function in prophase by limiting the
            recruitment of Aurora A
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Kaneko,Y., Tamura,K., Totsukawa,G. and Kondo,H.
  TITLE     Phosphorylation of p37 is important for Golgi disassembly at
            mitosis
  JOURNAL   Biochem Biophys Res Commun 402 (1), 37-41 (2010)
   PUBMED   20875789
  REMARK    GeneRIF: these results demonstrate that p37 phosphorylation on
            Serine-56 and Threonine-59 is important for Golgi disassembly at
            mitosis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC113645.1, AK126300.1 and U79282.1.
            
            On May 10, 2018 this sequence version replaced XP_005251222.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.265915.1,
                                           SRR1803611.45772.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.1"
     Protein         1..285
                     /product="UBX domain-containing protein 2B isoform 3"
                     /note="UBX domain-containing protein 2B; p97 cofactor p37;
                     NSFL1 cofactor p37"
                     /calculated_mol_wt=31656
     Region          146..>182
                     /region_name="SEP"
                     /note="SEP domain; cl02662"
                     /db_xref="CDD:470648"
     Region          204..285
                     /region_name="UBX_UBXN2B"
                     /note="Ubiquitin regulatory domain X (UBX) found in UBX
                     domain protein 2B (UBXN2B) and similar proteins; cd17161"
                     /db_xref="CDD:340681"
     Site            order(212,214,216..217,220..221,223,257..258,260,276..279,
                     281,283)
                     /site_type="other"
                     /note="putative UBX-p97 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340681"
     CDS             1..285
                     /gene="UBXN2B"
                     /gene_synonym="p37"
                     /coded_by="NM_001363181.1:26..883"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:137886"
                     /db_xref="HGNC:HGNC:27035"
                     /db_xref="MIM:610686"
ORIGIN      
        1 maegggpepg eqerrssgpr ppsardlqla laelyedevk ckssksnrpk atvfksprtp
       61 pqrfyssehe ysglnivrps tgkivnelfk earehgavpl neatrasgdd ksksftgggy
      121 rlgssfckrs eyiygenqlq dvqillklws ngfslddgel rpyneptnaq flesvkrglt
      181 peivstpssp eeedksilna vvliddsvpt tkiqirladg srliqrfnst hrildvrnfi
      241 vqsrpefaal dfilvtsfpn keltdesltl leadilntvl lqqlk
//
LOCUS       NP_115716                126 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquinol-cytochrome c reductase complex assembly factor 2 [Homo
            sapiens].
ACCESSION   NP_115716
VERSION     NP_115716.1
DBSOURCE    REFSEQ: accession NM_032340.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Tucker,E.J., Wanschers,B.F., Szklarczyk,R., Mountford,H.S.,
            Wijeyeratne,X.W., van den Brand,M.A., Leenders,A.M.,
            Rodenburg,R.J., Reljic,B., Compton,A.G., Frazier,A.E., Bruno,D.L.,
            Christodoulou,J., Endo,H., Ryan,M.T., Nijtmans,L.G., Huynen,M.A.
            and Thorburn,D.R.
  TITLE     Mutations in the UQCC1-interacting protein, UQCC2, cause human
            complex III deficiency associated with perturbed cytochrome b
            protein expression
  JOURNAL   PLoS Genet 9 (12), e1004034 (2013)
   PUBMED   24385928
  REMARK    GeneRIF: This work provides insight into human complex III assembly
            by establishing that UQCC1 and UQCC2 are complex III assembly
            factors participating in cytochrome b biogenesis.
REFERENCE   7  (residues 1 to 126)
  AUTHORS   Calvo,S.E., Compton,A.G., Hershman,S.G., Lim,S.C., Lieber,D.S.,
            Tucker,E.J., Laskowski,A., Garone,C., Liu,S., Jaffe,D.B.,
            Christodoulou,J., Fletcher,J.M., Bruno,D.L., Goldblatt,J.,
            Dimauro,S., Thorburn,D.R. and Mootha,V.K.
  TITLE     Molecular diagnosis of infantile mitochondrial disease with
            targeted next-generation sequencing
  JOURNAL   Sci Transl Med 4 (118), 118ra10 (2012)
   PUBMED   22277967
  REMARK    GeneRIF: Strong candidate gene for mitochondrial disease, based on
            recessive mutations detected in infantile patients
REFERENCE   8  (residues 1 to 126)
  AUTHORS   Cambier,L., Rassam,P., Chabi,B., Mezghenna,K., Gross,R., Eveno,E.,
            Auffray,C., Wrutniak-Cabello,C., Lajoix,A.D. and Pomies,P.
  TITLE     M19 modulates skeletal muscle differentiation and insulin secretion
            in pancreatic beta-cells through modulation of respiratory chain
            activity
  JOURNAL   PLoS One 7 (2), e31815 (2012)
   PUBMED   22363741
  REMARK    GeneRIF: The function of M19, a novel mitochondrial nucleoid
            protein, is characterized in muscle and pancreatic beta-cells.
REFERENCE   9  (residues 1 to 126)
  AUTHORS   Sumitani,M., Kasashima,K., Ohta,E., Kang,D. and Endo,H.
  TITLE     Association of a novel mitochondrial protein M19 with mitochondrial
            nucleoids
  JOURNAL   J Biochem 146 (5), 725-732 (2009)
   PUBMED   19643811
  REMARK    GeneRIF: M19 associates with the nucleoid and likely regulates the
            organization and metabolism of mtDNA.
REFERENCE   10 (residues 1 to 126)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC006007.1, BI604191.1,
            CN261727.1 and AI688269.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a nucleoid protein localized to the
            mitochondria inner membrane. The encoded protein affects regulation
            of insulin secretion, mitochondrial ATP production, and myogenesis
            through modulation of mitochondrial respiratory chain activity.
            [provided by RefSeq, Oct 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.105486.1,
                                           SRR1660803.213719.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119, SAMEA2153932
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000607484.6/
                                                  ENSP00000476140.1
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..126
                     /product="ubiquinol-cytochrome c reductase complex
                     assembly factor 2"
                     /EC_number="2.7.4.21"
                     /note="cytochrome B protein synthesis 6 homolog;
                     mitochondrial protein M19; breast cancer-associated
                     protein SGA-81M; mitochondrial nucleoid factor 1"
                     /calculated_mol_wt=14744
     Region          6..86
                     /region_name="UQCC2_CBP6"
                     /note="Complex III assembly factor UQCC2/CBP6; pfam20180"
                     /db_xref="CDD:466331"
     CDS             1..126
                     /gene="UQCC2"
                     /gene_synonym="bA6B20.2; C6orf125; C6orf126; Cbp6; M19;
                     MC3DN7; MNF1"
                     /coded_by="NM_032340.4:15..395"
                     /db_xref="CCDS:CCDS4784.1"
                     /db_xref="GeneID:84300"
                     /db_xref="HGNC:HGNC:21237"
                     /db_xref="MIM:614461"
ORIGIN      
        1 maasryrrfl klceewpvde tkrgrdlgay lrqrvaqafr egentqvaep eacdqmyesl
       61 arlhsnyykh kyprprdtsf sglsleeykl ilstdtleel keidkgmwkk lqekfapkgp
      121 eedhka
//
LOCUS       NP_036422                766 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_036422
VERSION     NP_036422.3
DBSOURCE    REFSEQ: accession NM_012290.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Lin,H.Y., Mohammadhosseini,M., McClatchy,J., Villamor-Paya,M.,
            Jeng,S., Bottomly,D., Tsai,C.F., Posso,C., Jacobson,J., Adey,A.,
            Gosline,S., Liu,T., McWeeney,S., Stracker,T.H. and Agarwal,A.
  TITLE     The TLK-ASF1 histone chaperone pathway plays a critical role in
            IL-1beta-mediated AML progression
  JOURNAL   Blood 143 (26), 2749-2762 (2024)
   PUBMED   38498025
  REMARK    GeneRIF: The TLK-ASF1 histone chaperone pathway plays a critical
            role in IL-1beta-mediated AML progression.
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Kuang,L., Lu,A. and Yao,S.
  TITLE     CircTLK1 alleviates oxygen-glucose deprivation/reperfusion induced
            apoptosis in HK-2 cells through miR-136-5p/Bcl2 signal axis
  JOURNAL   Ren Fail 45 (1), 2236219 (2023)
   PUBMED   37462140
  REMARK    GeneRIF: CircTLK1 alleviates oxygen-glucose deprivation/reperfusion
            induced apoptosis in HK-2 cells through miR-136-5p/Bcl2 signal
            axis.
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Zhang,Z. and Liu,S.
  TITLE     The interaction between ASF1B and TLK1 promotes the malignant
            progression of low-grade glioma
  JOURNAL   Ann Med 55 (1), 1111-1122 (2023)
   PUBMED   36947060
  REMARK    GeneRIF: The interaction between ASF1B and TLK1 promotes the
            malignant progression of low-grade glioma.
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Ghosh,I. and De Benedetti,A.
  TITLE     Untousling the Role of Tousled-like Kinase 1 in DNA Damage Repair
  JOURNAL   Int J Mol Sci 24 (17), 13369 (2023)
   PUBMED   37686173
  REMARK    GeneRIF: Untousling the Role of Tousled-like Kinase 1 in DNA Damage
            Repair.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Li,Y., DeFatta,R., Anthony,C., Sunavala,G. and De Benedetti,A.
  TITLE     A translationally regulated Tousled kinase phosphorylates histone
            H3 and confers radioresistance when overexpressed
  JOURNAL   Oncogene 20 (6), 726-738 (2001)
   PUBMED   11314006
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Cabaniols,J.P., Ravichandran,V. and Roche,P.A.
  TITLE     Phosphorylation of SNAP-23 by the novel kinase SNAK regulates
            t-SNARE complex assembly
  JOURNAL   Mol Biol Cell 10 (12), 4033-4041 (1999)
   PUBMED   10588641
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009953.4, BC032657.1,
            AC010092.4 and DN604386.1.
            
            On Aug 14, 2003 this sequence version replaced NP_036422.2.
            
            Summary: The protein encoded by this gene is a serine/threonine
            kinase that may be involved in the regulation of chromatin
            assembly. The encoded protein is only active when it is
            phosphorylated, and this phosphorylation is cell cycle-dependent,
            with the maximal activity of this protein coming during S phase.
            The catalytic activity of this protein is diminished by DNA damage
            and by blockage of DNA replication. Three transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D50927.2, BC032657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431350.7/ ENSP00000411099.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..766
                     /product="serine/threonine-protein kinase tousled-like 1
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine threonine protein kinase;
                     serine/threonine-protein kinase tousled-like 1; SNARE
                     protein kinase SNAK"
                     /calculated_mol_wt=86569
     Region          1..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C0V0; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q86UE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Region          205..>426
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          346..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKI8.2)"
     Region          449..747
                     /region_name="STKc_TLK1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 1; cd14040"
                     /db_xref="CDD:270942"
     Site            order(462..466,470,483,485,521,538..541,545,547,586,588,
                     590..591,593,607,610,632..635)
                     /site_type="active"
                     /db_xref="CDD:270942"
     Site            order(462..466,470,483,485,521,538..541,545,586,588,
                     590..591,593,607)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270942"
     Site            order(466,545,547,586,588,590,610,632..635)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270942"
     Site            606..635
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270942"
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12660173; propagated from
                     UniProtKB/Swiss-Prot (Q9UKI8.2)"
     CDS             1..766
                     /gene="TLK1"
                     /gene_synonym="PKU-beta"
                     /coded_by="NM_012290.5:466..2766"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2241.1"
                     /db_xref="GeneID:9874"
                     /db_xref="HGNC:HGNC:11841"
                     /db_xref="MIM:608438"
ORIGIN      
        1 msvqsssgsl egppswsqls tsptpgsaaa arsllnhtpp sgrpregamd elhsldprrq
       61 ellearftgv asgstgstgs csvgakastn nessnhsfgs lgslsdkese tpekkqsess
      121 rgrkrkaenq nessqgksig grghkisdyf eyqggngssp vrgippairs pqnshshstp
      181 sssvrpnsps ptalafgdhp ivqpkqlsfk iiqtdltmlk laalesnkiq dlekkegrid
      241 dllrancdlr rqideqqkll ekykerlnkc ismskkllie kstqeklssr eksmqdrlrl
      301 ghfttvrhga sfteqwtdgf afqnlvkqqe wvnqqredie rqrkllakrk pptannsqap
      361 stnsepkqrk nkavngaend pfvrpnlpql ltlaeyheqe eifklrlghl kkeeaeiqae
      421 lerlervrnl hirelkrinn ednsqfkdhp tlnerylllh llgrggfsev ykafdlyeqr
      481 yaavkihqln kswrdekken yhkhacreyr ihkeldhpri vklydyfsld tdtfctvley
      541 cegndldfyl kqhklmseke arsivmqivn alrylneikp piihydlkpg nillvdgtac
      601 geikitdfgl skimdddsyg vdgmdltsqg agtywylppe cfvvgkeppk isnkvdvwsv
      661 gviffqclyg rkpfghnqsq qdilqentil katevqfpvk pvvsseakaf irrclayrke
      721 drfdvhqlan dpyllphmrr snssgnlhma gltasptpps ssiity
//
LOCUS       NP_001354677             325 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform g [Homo sapiens].
ACCESSION   NP_001354677
VERSION     NP_001354677.1
DBSOURCE    REFSEQ: accession NM_001367748.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 325)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 325)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 325)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 325)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 325)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 325)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 325)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 325)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 325)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 325)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (32), as well as variants 29-31,
            encodes isoform g.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.98563.1,
                                           SRR1803617.202246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..325
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..325
                     /product="rab5 GDP/GTP exchange factor isoform g"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=37488
     Region          4..54
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          104..204
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..325
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367748.1:380..1357"
                     /note="isoform g is encoded by transcript variant 32"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mhykrdlsie eqsecaqdfy hnvaermqtr gkvppervek imdqiekyim trlykyvfcp
       61 ettddekkdl aiqkriralr wvtpqmlcvp vnedipevsd mvvkaitdii emdskrvprd
      121 klacitkcsk hifnaikitk nepasaddfl ptliyivlkg npprlqsniq yitrfcnpsr
      181 lmtgedgyyf tnlccavafi ekldaqslnl sqedfdryms gqtsprkqea eswspdaclg
      241 vkqmyknldl lsqlnerqer imneakklek dlidwtdgia revqdiveky pleikppnqp
      301 laaidsenve ndklppplqp qvyag
//
LOCUS       NP_001171644             282 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 6 isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001171644
VERSION     NP_001171644.1
DBSOURCE    REFSEQ: accession NM_001184715.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Oba,T., Long,M.D., Ito,K.I. and Ito,F.
  TITLE     Clinical and immunological relevance of SLAMF6 expression in the
            tumor microenvironment of breast cancer and melanoma
  JOURNAL   Sci Rep 14 (1), 2394 (2024)
   PUBMED   38287061
  REMARK    GeneRIF: Clinical and immunological relevance of SLAMF6 expression
            in the tumor microenvironment of breast cancer and melanoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Xia,G., Li,Y., Pan,W., Qian,C., Ma,L., Zhou,J., Xu,H. and Cheng,C.
  TITLE     SLAMF6 is associated with the susceptibility and severity of
            rheumatoid arthritis in the Chinese population
  JOURNAL   J Orthop Surg Res 17 (1), 13 (2022)
   PUBMED   35016729
  REMARK    GeneRIF: SLAMF6 is associated with the susceptibility and severity
            of rheumatoid arthritis in the Chinese population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Liu,B., Zeng,L., Shao,Y. and Fu,R.
  TITLE     Expression and function of SLAMF6 in CD8+ T lymphocytes of patients
            with severe aplastic anemia
  JOURNAL   Cell Immunol 364, 104343 (2021)
   PUBMED   33774556
  REMARK    GeneRIF: Expression and function of SLAMF6 in CD8(+) T lymphocytes
            of patients with severe aplastic anemia.
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Fraser,C.C., Howie,D., Morra,M., Qiu,Y., Murphy,C., Shen,Q.,
            Gutierrez-Ramos,J.C., Coyle,A., Kingsbury,G.A. and Terhorst,C.
  TITLE     Identification and characterization of SF2000 and SF2001, two new
            members of the immune receptor SLAM/CD2 family
  JOURNAL   Immunogenetics 53 (10-11), 843-850 (2002)
   PUBMED   11862385
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Bottino,C., Falco,M., Parolini,S., Marcenaro,E., Augugliaro,R.,
            Sivori,S., Landi,E., Biassoni,R., Notarangelo,L.D., Moretta,L. and
            Moretta,A.
  TITLE     NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface
            molecule contributing to the inability of natural killer cells to
            kill Epstein-Barr virus-infected B cells in X-linked
            lymphoproliferative disease
  JOURNAL   J Exp Med 194 (3), 235-246 (2001)
   PUBMED   11489943
  REMARK    Erratum:[J Exp Med 2001 Sep 3;194(5):following 703]
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Lee,Y.J., Luisiri,P. and Clark,M.R.
  TITLE     A novel complex, p40/42, is constitutively associated with the B
            cell antigen receptor and phosphorylated upon receptor stimulation
  JOURNAL   J Immunol 157 (9), 3828-3837 (1996)
   PUBMED   8892612
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Kong,G., Dalton,M., Bubeck Wardenburg,J., Straus,D., Kurosaki,T.
            and Chan,A.C.
  TITLE     Distinct tyrosine phosphorylation sites in ZAP-70 mediate
            activation and negative regulation of antigen receptor function
  JOURNAL   Mol Cell Biol 16 (9), 5026-5035 (1996)
   PUBMED   8756661
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Hercend,T., Meuer,S., Brennan,A., Edson,M.A., Acuto,O.,
            Reinherz,E.L., Schlossman,S.F. and Ritz,J.
  TITLE     Natural killer-like function of activated T lymphocytes:
            differential blocking effects of monoclonal antibodies specific for
            a 90-kDa clonotypic structure
  JOURNAL   Cell Immunol 86 (2), 381-392 (1984)
   PUBMED   6610481
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303990.1, AJ277141.1 and
            AK125624.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein, belonging to the CD2 subfamily of the immunoglobulin
            superfamily. This encoded protein is expressed on Natural killer
            (NK), T, and B lymphocytes. It undergoes tyrosine phosphorylation
            and associates with the Src homology 2 domain-containing protein
            (SH2D1A) as well as with SH2 domain-containing phosphatases (SHPs).
            It functions as a coreceptor in the process of NK cell activation.
            It can also mediate inhibitory signals in NK cells from X-linked
            lymphoproliferative patients. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms.[provided
            by RefSeq, May 2010].
            
            Transcript Variant: This variant (3) uses multiple alternate splice
            sites in the coding region, compared to variant 1, which result in
            an isoform (3) with a shorter extracellular domain than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303990.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2-q23.3"
     Protein         1..282
                     /product="SLAM family member 6 isoform 3 precursor"
                     /note="activating NK receptor; natural killer-, T- and
                     B-cell antigen; NTBA receptor; NK-T-B-antigen"
                     /calculated_mol_wt=29516
     sig_peptide     1..21
                     /calculated_mol_wt=2512
     Region          <3..77
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     mat_peptide     22..282
                     /product="SLAM family member 6 isoform 3"
                     /calculated_mol_wt=29516
     Region          43..47
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          57..62
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          70..73
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          <100..158
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          100..104
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          114..118
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          139..142
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          143..148
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..282
                     /gene="SLAMF6"
                     /gene_synonym="CD352; KALI; KALIb; Ly108; NTB-A; NTBA;
                     SF2000"
                     /coded_by="NM_001184715.2:64..912"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:114836"
                     /db_xref="HGNC:HGNC:21392"
                     /db_xref="MIM:606446"
ORIGIN      
        1 mlwlfqsllf vfcfgpvphe tkspeihvtn pkqgkrlnft qsyslqlsnl kmedtgsyra
       61 qistktsakl ssytlrilrq lrniqvtnhs qlfqnmtcel hltcsvedad dnvsfrweal
      121 gntlssqpnl tvswdpriss eqdytciaen avsnlsfsvs aqklcedvki qytdtkmilf
      181 mvsgicivfg fiillllvlr krrdslslst qrtqgpesar nleyvsvspt nntvyasvth
      241 snreteiwtp rendtitiys tinhskeskp tfsrataldn vv
//
LOCUS       NP_001230440             435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_001230440
VERSION     NP_001230440.1
DBSOURCE    REFSEQ: accession NM_001243511.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647076.1, AY388460.1,
            DA293919.1, AB020639.1 and BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (11) uses an alternate exon
            structure in the 5' UTR and 5' coding region, compared to variant
            1. This results in a distinct 5' UTR and use of a downstream
            in-frame start codon. The encoded isoform (2) has a shorter
            N-terminus compared to isoform 1. Variants 2-4, 9-15, and 17-21
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.6451.1, SRR1803612.73108.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243511.3:142..1449"
                     /note="isoform 2 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_001354656             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354656
VERSION     NP_001354656.1
DBSOURCE    REFSEQ: accession NM_001367727.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006001.2 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (11), as well as variants 3, 4, 9,
            10, and 12-20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.242718.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367727.1:358..1833"
                     /note="isoform c is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001073922            2190 aa            linear   PRI 20-NOV-2025
DEFINITION  integrator complex subunit 1 [Homo sapiens].
ACCESSION   NP_001073922 NP_056489 XP_291222
VERSION     NP_001073922.2
DBSOURCE    REFSEQ: accession NM_001080453.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2190)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2190)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   3  (residues 1 to 2190)
  AUTHORS   Confino,S., Wexler,Y., Medvetzky,A., Elazary,Y., Ben-Moshe,Z.,
            Reiter,J., Dor,T., Edvardson,S., Prag,G., Harel,T. and Gothilf,Y.
  TITLE     A deleterious variant of INTS1 leads to disrupted sleep-wake cycles
  JOURNAL   Dis Model Mech 17 (8) (2024)
   PUBMED   39189071
  REMARK    GeneRIF: A deleterious variant of INTS1 leads to disrupted
            sleep-wake cycles.
REFERENCE   4  (residues 1 to 2190)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   5  (residues 1 to 2190)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   6  (residues 1 to 2190)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 2190)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 2190)
  AUTHORS   Nusbaum,C., Mikkelsen,T.S., Zody,M.C., Asakawa,S., Taudien,S.,
            Garber,M., Kodira,C.D., Schueler,M.G., Shimizu,A., Whittaker,C.A.,
            Chang,J.L., Cuomo,C.A., Dewar,K., FitzGerald,M.G., Yang,X.,
            Allen,N.R., Anderson,S., Asakawa,T., Blechschmidt,K., Bloom,T.,
            Borowsky,M.L., Butler,J., Cook,A., Corum,B., DeArellano,K.,
            DeCaprio,D., Dooley,K.T., Dorris,L. 3rd, Engels,R., Glockner,G.,
            Hafez,N., Hagopian,D.S., Hall,J.L., Ishikawa,S.K., Jaffe,D.B.,
            Kamat,A., Kudoh,J., Lehmann,R., Lokitsang,T., Macdonald,P.,
            Major,J.E., Matthews,C.D., Mauceli,E., Menzel,U., Mihalev,A.H.,
            Minoshima,S., Murayama,Y., Naylor,J.W., Nicol,R., Nguyen,C.,
            O'Leary,S.B., O'Neill,K., Parker,S.C., Polley,A., Raymond,C.K.,
            Reichwald,K., Rodriguez,J., Sasaki,T., Schilhabel,M., Siddiqui,R.,
            Smith,C.L., Sneddon,T.P., Talamas,J.A., Tenzin,P., Topham,K.,
            Venkataraman,V., Wen,G., Yamazaki,S., Young,S.K., Zeng,Q.,
            Zimmer,A.R., Rosenthal,A., Birren,B.W., Platzer,M., Shimizu,N. and
            Lander,E.S.
  TITLE     DNA sequence and analysis of human chromosome 8
  JOURNAL   Nature 439 (7074), 331-335 (2006)
   PUBMED   16421571
REFERENCE   9  (residues 1 to 2190)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 2190)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093734.3, DB113520.1, AI935093.1, BM553299.1, BM547069.1,
            BF346658.1, BX324321.2, AB037861.1 and BC069262.1.
            
            On or before Nov 22, 2007 this sequence version replaced
            NP_056489.1, NP_001073922.1.
            
            Summary: INTS1 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404767.8/ ENSP00000385722.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..2190
                     /product="integrator complex subunit 1"
                     /calculated_mol_wt=244167
     Region          1..61
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            47
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8N201.2)"
     Region          350..430
                     /region_name="DUF3677"
                     /note="Protein of unknown function (DUF3677); pfam12432"
                     /db_xref="CDD:463578"
     Region          922..945
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            1159..1179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N201.2)"
     Region          1311..1334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            1326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4S8; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            1327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4S8; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N201.2)"
     CDS             1..2190
                     /gene="INTS1"
                     /gene_synonym="INT1; NDCAGF; NET28"
                     /coded_by="NM_001080453.3:109..6681"
                     /db_xref="CCDS:CCDS47526.1"
                     /db_xref="GeneID:26173"
                     /db_xref="HGNC:HGNC:24555"
                     /db_xref="MIM:611345"
ORIGIN      
        1 mnrakpttvr rpsaaakpsg hpppgdfial gskgqanesk tastllkpap sglpserkrd
       61 aaaalssasa ltgltkrpkl sstpplsalg rlaeaavaek raispsikep svvpievlpt
      121 vlldeieaae legnddrieg vlcgavkqlk vtrakpdstl ylslmylaki kpnifategv
      181 iealcsllrr dasinfkakg nslvsvlacn llmaayeede nwpeifvkvy iedslgeriw
      241 vdsphcktfv dniqtafntr mpprsvllqg eagrvagdlg agssphpslt eeedsqtell
      301 iaeeklspeq egqlmpryee laesveeyvl dmlrdqlnrr qpidnvsrnl lrlltstcgy
      361 kevrllavqk lemwlqnpkl trpaqdllms vcmncnthgs edmdvishli kirlkpkvll
      421 nhfmlcirel lsahkdnlgt tiklvifnel ssarnpnnmq vlytalqhss elapkflamv
      481 fqdlltnkdd ylrasrallr eiikqtkhei nfqafclglm qerkepqyle mefkerfvvh
      541 itdvlavsmm lgitaqvkea giawdkgekr nlevlrsfqn qiaaiqrdav wwlhtvvpsi
      601 sklapkdyvh clhkvlfteq petyykwdnw ppesdrnffl rlcsevpile dtlmrilvig
      661 lsrelplgpa dameladhlv kraaavqadd vevlkvgrtq lidavlnlct yhhpeniqlp
      721 pgyqppnlai stlywkawpl llvvaafnpe niglaaweey ptlkmlmemv mtnnysyppc
      781 tltdeetrte mlnrelqtaq rekqeilafe ghlaaastkq titessslll sqltsldpqg
      841 pprrppphil dqvkslnqsl rlghllcrsr npdfllhiiq rqassqsmpw ladlvqsseg
      901 sldvlpvqcl cefllhdavd daasgeedde geskeqkakk rqrqqkqrql lgrlqdlllg
      961 pkadeqttce vldyflrrlg ssqvasrvla mkglslvlse gslrdgeeke ppmeedvgdt
     1021 dvlqgyqwll rdlprlplfd svrsttalal qqaihmetdp qtisayliyl sqhtpveeqa
     1081 qhsdlaldva rlvverstim shlfsklsps aasdavlsal lsifsryvrr mrqskegeev
     1141 yswsesqdqv flrwssgeta tmhilvvham villtlgppr addsefqall diwfpeekpl
     1201 ptaflvdtse ealllpdwlk lrmirsevlr lvdaalqdle pqqlllfvqs fgipvssmsk
     1261 llqfldqava hdpqtleqni mdknymahlv evqhergasg gqtfhsllta slpprrdste
     1321 apkpksspeq pigqgrirvg tqlrvlgped dlagmflqif plspdprwqs ssprpvalal
     1381 qqalgqelar vvqgspevpg itvrvlqala tllssphgga lvmsmhrshf lacpllrqlc
     1441 qyqrcvpqdt gfsslflkvl lqmlqwldsp gveggplraq lrmlasqasa grrlsdvrgg
     1501 llrlaealaf rqdlevvsst vraviatlrs geqcsvepdl iskvlqglie vrsphleell
     1561 taffsatada aspfpackpv vvvsslllqe eeplaggkpg adggsleavr lgpssgllvd
     1621 wlemldpevv sscpdlqlrl lfsrrkgkgq aqvpsfrpyl ltlfthqssw ptlhqcirvl
     1681 lgksreqrfd psasldflwa cihvpriwqg rdqrtpqkrr eelvlrvqgp elislvelil
     1741 aeaetrsqdg dtaacsliqa rlplllsccc gddesvrkvt ehlsgciqqw gdsvlgrrcr
     1801 dlllqlylqr pelrvpvpev llhsegaass svckldglih rfitlladts dsralenrga
     1861 dasmacrkla vahpllllrh lpmiaallhg rthlnfqefr qqnhlscflh vlgllellqp
     1921 hvfrsehqga lwdcllsfir lllnyrkssr hlaafinkfv qfihkyityn apaaisflqk
     1981 hadplhdlsf dnsdlvmlks llaglslpsr ddrtdrglde egeeessags lplvsvslft
     2041 pltaaemapy mkrlsrgqtv edllevlsdi demsrrrpei lsffstnlqr lmssaeeccr
     2101 nlafslalrs mqnspsiaaa flptfmyclg sqdfevvqta lrnlpeyall cqehaavllh
     2161 raflvgmygq mdpsaqisea lrilhmeavm
//
LOCUS       NP_006549                346 aa            linear   PRI 20-NOV-2025
DEFINITION  KH domain-containing, RNA-binding, signal transduction-associated
            protein 3 [Homo sapiens].
ACCESSION   NP_006549
VERSION     NP_006549.1
DBSOURCE    REFSEQ: accession NM_006558.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Wu,X., Qiu,L., Feng,H., Zhang,H., Yu,H., Du,Y., Wu,H., Zhu,S.,
            Ruan,Y. and Jiang,H.
  TITLE     KHDRBS3 promotes paclitaxel resistance and induces glycolysis
            through modulated MIR17HG/CLDN6 signaling in epithelial ovarian
            cancer
  JOURNAL   Life Sci 293, 120328 (2022)
   PUBMED   35051418
  REMARK    GeneRIF: KHDRBS3 promotes paclitaxel resistance and induces
            glycolysis through modulated MIR17HG/CLDN6 signaling in epithelial
            ovarian cancer.
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Boeckel,J.N., Mobius-Winkler,M., Muller,M., Rebs,S., Eger,N.,
            Schoppe,L., Tappu,R., Kokot,K.E., Kneuer,J.M., Gaul,S.,
            Bordalo,D.M., Lai,A., Haas,J., Ghanbari,M., Drewe-Boss,P., Liss,M.,
            Katus,H.A., Ohler,U., Gotthardt,M., Laufs,U., Streckfuss-Bomeke,K.
            and Meder,B.
  TITLE     SLM2 Is A Novel Cardiac Splicing Factor Involved in Heart Failure
            due to Dilated Cardiomyopathy
  JOURNAL   Genomics Proteomics Bioinformatics 20 (1), 129-146 (2022)
   PUBMED   34273561
  REMARK    GeneRIF: SLM2 Is A Novel Cardiac Splicing Factor Involved in Heart
            Failure due to Dilated Cardiomyopathy.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Ukai,S., Sakamoto,N., Taniyama,D., Harada,K., Honma,R.,
            Maruyama,R., Naka,K., Hinoi,T., Takakura,Y., Shimizu,W., Ohdan,H.
            and Yasui,W.
  TITLE     KHDRBS3 promotes multi-drug resistance and anchorage-independent
            growth in colorectal cancer
  JOURNAL   Cancer Sci 112 (3), 1196-1208 (2021)
   PUBMED   33423358
  REMARK    GeneRIF: KHDRBS3 promotes multi-drug resistance and
            anchorage-independent growth in colorectal cancer.
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Stoss,O., Olbrich,M., Hartmann,A.M., Konig,H., Memmott,J.,
            Andreadis,A. and Stamm,S.
  TITLE     The STAR/GSG family protein rSLM-2 regulates the selection of
            alternative splice sites
  JOURNAL   J Biol Chem 276 (12), 8665-8673 (2001)
   PUBMED   11118435
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Venables,J.P., Elliott,D.J., Makarova,O.V., Makarov,E.M.,
            Cooke,H.J. and Eperon,I.C.
  TITLE     RBMY, a probable human spermatogenesis factor, and other hnRNP G
            proteins interact with Tra2beta and affect splicing
  JOURNAL   Hum Mol Genet 9 (5), 685-694 (2000)
   PUBMED   10749975
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Lee,J. and Burr,J.G.
  TITLE     Salpalpha and Salpbeta, growth-arresting homologs of Sam68
  JOURNAL   Gene 240 (1), 133-147 (1999)
   PUBMED   10564820
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Venables,J.P., Vernet,C., Chew,S.L., Elliott,D.J., Cowmeadow,R.B.,
            Wu,J., Cooke,H.J., Artzt,K. and Eperon,I.C.
  TITLE     T-STAR/ETOILE: a novel relative of SAM68 that interacts with an
            RNA-binding protein implicated in spermatogenesis
  JOURNAL   Hum Mol Genet 8 (6), 959-969 (1999)
   PUBMED   10332027
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Di Fruscio,M., Chen,T. and Richard,S.
  TITLE     Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2:
            SLM-1 is a Src substrate during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 96 (6), 2710-2715 (1999)
   PUBMED   10077576
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC040914.5, BC032606.2, AF051321.1, BC106028.1 and CB155439.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.222284.1, AF051321.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355849.10/ ENSP00000348108.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.23"
     Protein         1..346
                     /product="KH domain-containing, RNA-binding, signal
                     transduction-associated protein 3"
                     /note="Sam68-like phosphotyrosine protein, T-STAR;
                     RNA-binding protein T-Star; sam68-like mammalian protein
                     2; KH domain containing, RNA binding, signal transduction
                     associated 3"
                     /calculated_mol_wt=38668
     Region          1..160
                     /region_name="Involved in homodimerization.
                     /evidence=ECO:0000269|PubMed:26758068"
                     /note="propagated from UniProtKB/Swiss-Prot (O75525.1)"
     Region          4..53
                     /region_name="Qua1"
                     /note="Qua1 domain; pfam16274"
                     /db_xref="CDD:465079"
     Region          48..160
                     /region_name="KH-I_KHDRBS3"
                     /note="type I K homology (KH) RNA-binding domain found in
                     KH domain-containing, RNA-binding, signal
                     transduction-associated protein 3 (KHDRBS3) and similar
                     proteins; cd22470"
                     /db_xref="CDD:411898"
     Site            order(48..49,51,58..61,66,125,128,137..138,141,144..145,
                     148..149,152,155)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:411898"
     Site            order(71,73..75,77..81,84..85,95..97,102..104)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411898"
     Region          212..251
                     /region_name="Interaction with SIAH1.
                     /evidence=ECO:0000269|PubMed:15163637"
                     /note="propagated from UniProtKB/Swiss-Prot (O75525.1)"
     Region          213..267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75525.1)"
     Region          266..320
                     /region_name="Sam68-YY"
                     /note="Tyrosine-rich domain of Sam68; pfam16568"
                     /db_xref="CDD:465182"
     Region          318..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75525.1)"
     CDS             1..346
                     /gene="KHDRBS3"
                     /gene_synonym="Etle; etoile; SALP; SLM-2; SLM2; T-STAR;
                     TSTAR"
                     /coded_by="NM_006558.3:412..1452"
                     /db_xref="CCDS:CCDS6374.1"
                     /db_xref="GeneID:10656"
                     /db_xref="HGNC:HGNC:18117"
                     /db_xref="MIM:610421"
ORIGIN      
        1 meekylpelm aekdsldpsf thalrlvnqe iekfqkgegk deekyidvvi nknmklgqkv
       61 lipvkqfpkf nfvgkllgpr gnslkrlqee tltkmsilgk gsmrdkakee elrksgeaky
      121 fhlnddlhvl ievfappaea yarmghalee ikkflipdyn deirqaqlqe ltylnggsen
      181 advpvvrgkp tlrtrgvpap aitrgrggvt arpvgvvvpr gtptprgvls trgpvsrgrg
      241 lltprargvp ptgyrppppp ptqetygeyd yddgygtayd eqsydsydns ystpaqsgad
      301 yydyghglse etydsygqee wtnsrhkaps artakgvyrd qpygry
//
LOCUS       NP_001309188             365 aa            linear   PRI 20-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 3 [Homo sapiens].
ACCESSION   NP_001309188 XP_005259427
VERSION     NP_001309188.1
DBSOURCE    REFSEQ: accession NM_001322259.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10, KR134287.1,
            KF672848.1 and BQ018270.1.
            
            On Apr 8, 2016 this sequence version replaced XP_005259427.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (3, also known as cyclin ET)
            encodes isoform 3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KR134287.1, ERR3218366.796986.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..365
                     /product="G1/S-specific cyclin-E1 isoform 3"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=41608
     Region          103..238
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            order(109..110,112,115..116,119..120,123,127,162,197,
                     201..205,209..210,227,230..231,234..235,238)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          <233..311
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..365
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001322259.2:187..1284"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mprerrerda kerdtmkedg gaefsarsrk rkanvtvflq dpdeemakid rtardqcgsq
       61 pwdnnavcad pcsliptpdk edddrvypns tckpriiaps rgsplpvlsw anreevwkim
      121 lnkektylrd qhfleqhpll qpkmrailld wlmevcevyk lhretfylaq dffdrymatq
      181 envvktllql igisslfiaa kleeiyppkl hqfayvtdga csgdeiltme lmimklldlc
      241 vldvdclefp ygilaasaly hfssselmqk vsgyqwcdie ncvkwmvpfa mviretgssk
      301 lkhfrgvade dahniqthrd sldlldkara kkamlseqnr asplpsgllt ppqsgkkqss
      361 gpema
//
LOCUS       NP_001317308             108 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-crystallin B chain isoform 2 [Homo sapiens].
ACCESSION   NP_001317308 XP_011540911
VERSION     NP_001317308.1
DBSOURCE    REFSEQ: accession NM_001330379.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Wang,X., Chen,K., Yao,Y., Lin,Y., Yang,J., Zhu,Y. and Zhou,B.
  TITLE     TGFbeta1-Induced Fibrotic Responses of Conjunctival Fibroblasts
            through the Wnt/beta-Catenin/CRYAB Signaling Pathway
  JOURNAL   Am J Pathol 194 (9), 1764-1779 (2024)
   PUBMED   38879081
  REMARK    GeneRIF: TGFbeta1-Induced Fibrotic Responses of Conjunctival
            Fibroblasts through the Wnt/beta-Catenin/CRYAB Signaling Pathway.
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Rodina,N., Hornung,S., Sarkar,R., Suladze,S., Peters,C.,
            Schmid,P.W.N., Niu,Z., Haslbeck,M., Buchner,J., Kapurniotu,A. and
            Reif,B.
  TITLE     Modulation of Alzheimer's Disease Abeta40 Fibril Polymorphism by
            the Small Heat Shock Protein alphaB-Crystallin
  JOURNAL   J Am Chem Soc 146 (28), 19077-19087 (2024)
   PUBMED   38973199
  REMARK    GeneRIF: Modulation of Alzheimer's Disease Abeta40 Fibril
            Polymorphism by the Small Heat Shock Protein alphaB-Crystallin.
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Tian,B., Li,X., Li,W., Shi,Z., He,X., Wang,S., Zhu,X., Shi,N.,
            Li,Y., Wan,P. and Zhu,C.
  TITLE     CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1
  JOURNAL   Aging (Albany NY) 16 (10), 8965-8979 (2024)
   PUBMED   38787373
  REMARK    GeneRIF: CRYAB suppresses ferroptosis and promotes osteogenic
            differentiation of human bone marrow stem cells via binding and
            stabilizing FTH1.
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Derham,B.K. and Harding,J.J.
  TITLE     Alpha-crystallin as a molecular chaperone
  JOURNAL   Prog Retin Eye Res 18 (4), 463-509 (1999)
   PUBMED   10217480
  REMARK    GeneRIF: Alpha crystallin is a moonlighting protein that functions
            as a heat shock protein as well as a lens crystallin.
            Review article
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Selcen,D. and Engel,A.G.
  TITLE     Myofibrillar Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301672
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Ortwerth,B.J., Slight,S.H., Prabhakaram,M., Sun,Y. and Smith,J.B.
  TITLE     Site-specific glycation of lens crystallins by ascorbic acid
  JOURNAL   Biochim Biophys Acta 1117 (2), 207-215 (1992)
   PUBMED   1525182
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Iwaki,A., Iwaki,T., Goldman,J.E., Ogomori,K., Tateishi,J. and
            Sakaki,Y.
  TITLE     Accumulation of alpha B-crystallin in brains of patients with
            Alexander's disease is not due to an abnormality of the 5'-flanking
            and coding sequence of the genomic DNA
  JOURNAL   Neurosci Lett 140 (1), 89-92 (1992)
   PUBMED   1407707
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Kato,K., Shinohara,H., Goto,S., Inaguma,Y., Morishita,R. and
            Asano,T.
  TITLE     Copurification of small heat shock protein with alpha B crystallin
            from human skeletal muscle
  JOURNAL   J Biol Chem 267 (11), 7718-7725 (1992)
   PUBMED   1560006
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Kramps,J.A., de Man,B.M. and de Jong,W.W.
  TITLE     The primary structure of the B2 chain of human alpha-crystallin
  JOURNAL   FEBS Lett 74 (1), 82-84 (1977)
   PUBMED   838078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000907.6, BQ437433.1 and
            BF339748.1.
            
            On Aug 29, 2016 this sequence version replaced XP_011540911.1.
            
            Summary: Mammalian lens crystallins are divided into alpha, beta,
            and gamma families. Alpha crystallins are composed of two gene
            products: alpha-A and alpha-B, for acidic and basic, respectively.
            Alpha crystallins can be induced by heat shock and are members of
            the small heat shock protein (HSP20) family. They act as molecular
            chaperones although they do not renature proteins and release them
            in the fashion of a true chaperone; instead they hold them in large
            soluble aggregates. These heterogeneous aggregates consist of 30-40
            subunits; the alpha-A and alpha-B subunits have a 3:1 ratio,
            respectively. Two additional functions of alpha crystallins are an
            autokinase activity and participation in the intracellular
            architecture. The encoded protein has been identified as a
            moonlighting protein based on its ability to perform
            mechanistically distinct functions. Alpha-A and alpha-B gene
            products are differentially expressed; alpha-A is preferentially
            restricted to the lens and alpha-B is expressed widely in many
            tissues and organs. Elevated expression of alpha-B crystallin
            occurs in many neurological diseases; a missense mutation
            cosegregated in a family with a desmin-related myopathy.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2019].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ709037.1, BQ437433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMN03267751
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            multifunctional gene product(s) :: PMID: 10217480
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..108
                     /product="alpha-crystallin B chain isoform 2"
                     /note="heat-shock 20 kD like-protein; alpha-crystallin B
                     chain; heat shock protein beta-5; rosenthal fiber
                     component; renal carcinoma antigen NY-REN-27; epididymis
                     secretory protein Li 101; heat shock protein family B
                     member 5"
                     /calculated_mol_wt=12122
     Region          1..83
                     /region_name="alpha-crystallin domain (ACD) found in
                     alpha-crystallin-type small heat shock proteins, and a
                     similar domain found in p23 (a cochaperone for Hsp90) and
                     in other p23-like proteins."
                     /note="The alpha-crystallin-Hsps_p23-like superfamily
                     includes the alpha-crystallin domain (ACD) of
                     alpha-crystallin-type small heat shock proteins (sHsps)
                     and a similar domain found in p23-like proteins. sHsps are
                     small stress induced proteins with monomeric...; cl00175"
                     /db_xref="CDD:469641"
     CDS             1..108
                     /gene="CRYAB"
                     /gene_synonym="CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101;
                     HSPB5; MFM2; MFM2A; MFM2B"
                     /coded_by="NM_001330379.1:84..410"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81626.1"
                     /db_xref="GeneID:1410"
                     /db_xref="HGNC:HGNC:2389"
                     /db_xref="MIM:123590"
ORIGIN      
        1 mrlekdrfsv nldvkhfspe elkvkvlgdv ievhgkheer qdehgfisre fhrkyripad
       61 vdpltitssl ssdgvltvng prkqvsgper tipitreekp avtaapkk
//
LOCUS       NP_874368                461 aa            linear   PRI 20-NOV-2025
DEFINITION  histone acetyltransferase KAT5 isoform 3 [Homo sapiens].
ACCESSION   NP_874368
VERSION     NP_874368.1
DBSOURCE    REFSEQ: accession NM_182709.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Wang,Y., Li,M., Chen,Y., Jiang,Y., Zhang,Z., Yan,Z., Liu,X. and
            Wu,C.
  TITLE     SPIN1 facilitates chemoresistance and HR repair by promoting Tip60
            binding to H3K9me3
  JOURNAL   EMBO Rep 25 (9), 3970-3989 (2024)
   PUBMED   39090319
  REMARK    GeneRIF: SPIN1 facilitates chemoresistance and HR repair by
            promoting Tip60 binding to H3K9me3.
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Sun,M., Yang,B., Xin,G., Wang,Y., Luo,J., Jiang,Q. and Zhang,C.
  TITLE     TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation
  JOURNAL   Sci China Life Sci 67 (9), 1957-1969 (2024)
   PUBMED   38763998
  REMARK    GeneRIF: TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Chen,H., Li,Y., Li,H., Chen,X., Fu,H., Mao,D., Chen,W., Lan,L.,
            Wang,C., Hu,K., Li,J., Zhu,C., Evans,I., Cheung,E., Lu,D., He,Y.,
            Behrens,A., Yin,D. and Zhang,C.
  TITLE     NBS1 lactylation is required for efficient DNA repair and
            chemotherapy resistance
  JOURNAL   Nature 631 (8021), 663-669 (2024)
   PUBMED   38961290
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Xuan,F., Xuan,H., Huang,M., He,W., Xu,H., Shi,X. and Wen,H.
  TITLE     The Tudor-knot Domain of KAT5 Regulates Nucleosomal Substrate
            Acetylation
  JOURNAL   J Mol Biol 436 (7), 168414 (2024)
   PUBMED   38141874
  REMARK    GeneRIF: The Tudor-knot Domain of KAT5 Regulates Nucleosomal
            Substrate Acetylation.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Brady,M.E., Ozanne,D.M., Gaughan,L., Waite,I., Cook,S., Neal,D.E.
            and Robson,C.N.
  TITLE     Tip60 is a nuclear hormone receptor coactivator
  JOURNAL   J Biol Chem 274 (25), 17599-17604 (1999)
   PUBMED   10364196
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Dechend,R., Hirano,F., Lehmann,K., Heissmeyer,V., Ansieau,S.,
            Wulczyn,F.G., Scheidereit,C. and Leutz,A.
  TITLE     The Bcl-3 oncoprotein acts as a bridging factor between
            NF-kappaB/Rel and nuclear co-regulators
  JOURNAL   Oncogene 18 (22), 3316-3323 (1999)
   PUBMED   10362352
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Kimura,A. and Horikoshi,M.
  TITLE     Tip60 acetylates six lysines of a specific class in core histones
            in vitro
  JOURNAL   Genes Cells 3 (12), 789-800 (1998)
   PUBMED   10096020
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Yamamoto,T. and Horikoshi,M.
  TITLE     Novel substrate specificity of the histone acetyltransferase
            activity of HIV-1-Tat interactive protein Tip60
  JOURNAL   J Biol Chem 272 (49), 30595-30598 (1997)
   PUBMED   9388189
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Kamine,J., Elangovan,B., Subramanian,T., Coleman,D. and
            Chinnadurai,G.
  TITLE     Identification of a cellular protein that specifically interacts
            with the essential cysteine region of the HIV-1 Tat transactivator
  JOURNAL   Virology 216 (2), 357-366 (1996)
   PUBMED   8607265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB003934.1, BC000166.3 and
            BU737532.1.
            
            Summary: The protein encoded by this gene belongs to the MYST
            family of histone acetyl transferases (HATs) and was originally
            isolated as an HIV-1 TAT-interactive protein. HATs play important
            roles in regulating chromatin remodeling, transcription and other
            nuclear processes by acetylating histone and nonhistone proteins.
            This protein is a histone acetylase that has a role in DNA repair
            and apoptosis and is thought to play an important role in signal
            transduction. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3), also known as beta, lacks two
            alternate in-frame segments, compared to variant 1, resulting in a
            shorter protein (isoform 3), that has a shorter N-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.177611.1,
                                           SRR1803615.269562.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..461
                     /product="histone acetyltransferase KAT5 isoform 3"
                     /EC_number="2.3.1.48"
                     /note="cPLA2 interacting protein; HIV-1 Tat interactive
                     protein, 60kDa; K-acetyltransferase 5; Tat interacting
                     protein, 60kDa; histone acetyltransferase KAT5;
                     cPLA(2)-interacting protein; 60 kDa Tat-interactive
                     protein; histone acetyltransferase HTATIP; K(lysine)
                     acetyltransferase 5; protein acetyltransferase KAT5;
                     protein crotonyltransferase KAT5; protein
                     2-hydroxyisobutyryltransferase KAT5; protein
                     lactyltransferase KAT5"
                     /calculated_mol_wt=52946
     Region          7..65
                     /region_name="Tudor-knot"
                     /note="RNA binding activity-knot of a chromodomain;
                     pfam11717"
                     /db_xref="CDD:432022"
     Site            order(22,28..30,45,47..50,54,56..59,61..62,69,72..73)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350845"
     Site            order(22,47,50,54)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350845"
     Region          43..452
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            order(44,46..51,53..57)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     Site            order(44,47,51,53,57)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     CDS             1..461
                     /gene="KAT5"
                     /gene_synonym="cPLA2; ESA1; HTATIP; HTATIP1; NEDFASB;
                     PLIP; TIP; TIP60; ZC2HC5"
                     /coded_by="NM_182709.3:17..1402"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS8109.1"
                     /db_xref="GeneID:10524"
                     /db_xref="HGNC:HGNC:5275"
                     /db_xref="MIM:601409"
ORIGIN      
        1 maevgeiieg crlpvlrrnq dnedewplae ilsvkdisgr klfyvhyidf nkrldewvth
       61 erldlkkiqf pkkeaktptk nglpgsrpgs perevkrkve vvspatpvps etapasvfpq
      121 ngaarravaa qpgrkrksnc lgtdedsqds sdgipsaprm tgslvsdrsh ddivtrmkni
      181 ecielgrhrl kpwyfspypq elttlpvlyl cefclkygrs lkclqrhltk cdlrhppgne
      241 iyrkgtisff eidgrknksy sqnlcllakc fldhktlyyd tdpflfyvmt eydckgfhiv
      301 gyfskekest edynvacilt lppyqrrgyg klliefsyel skvegktgtp ekplsdlgll
      361 syrsywsqti leilmglkse sgerpqitin eiseitsikk edvistlqyl nlinyykgqy
      421 iltlsedivd gheramlkrl lridskclhf tpkdwskrgk w
//
LOCUS       NP_001019801             521 aa            linear   PRI 20-NOV-2025
DEFINITION  runt-related transcription factor 2 isoform a [Homo sapiens].
ACCESSION   NP_001019801
VERSION     NP_001019801.3
DBSOURCE    REFSEQ: accession NM_001024630.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Komori,T.
  TITLE     Regulation of Skeletal Development and Maintenance by Runx2 and Sp7
  JOURNAL   Int J Mol Sci 25 (18), 10102 (2024)
   PUBMED   39337587
  REMARK    GeneRIF: Regulation of Skeletal Development and Maintenance by
            Runx2 and Sp7.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Vitale,E., Manicardi,V., Gugnoni,M., Torricelli,F., Donati,B.,
            Muccioli,S., Salviato,E., Rossi,T., Manzotti,G., Piana,S. and
            Ciarrocchi,A.
  TITLE     Exploring the transcriptional cooperation between RUNX2 and its
            associated elncRNA RAIN
  JOURNAL   Cell Death Dis 15 (9), 673 (2024)
   PUBMED   39271656
  REMARK    GeneRIF: Exploring the transcriptional cooperation between RUNX2
            and its associated elncRNA RAIN.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Yalaev,B., Tyurin,A., Akhiiarova,K. and Khusainova,R.
  TITLE     Hypomethylation of the RUNX2 Gene Is a New Potential Biomarker of
            Primary Osteoporosis in Men and Women
  JOURNAL   Int J Mol Sci 25 (13), 7312 (2024)
   PUBMED   39000419
  REMARK    GeneRIF: Hypomethylation of the RUNX2 Gene Is a New Potential
            Biomarker of Primary Osteoporosis in Men and Women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Drissi,H., Luc,Q., Shakoori,R., Chuva De Sousa Lopes,S., Choi,J.Y.,
            Terry,A., Hu,M., Jones,S., Neil,J.C., Lian,J.B., Stein,J.L., Van
            Wijnen,A.J. and Stein,G.S.
  TITLE     Transcriptional autoregulation of the bone related CBFA1/RUNX2 gene
  JOURNAL   J Cell Physiol 184 (3), 341-350 (2000)
   PUBMED   10911365
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Geoffroy,V., Corral,D.A., Zhou,L., Lee,B. and Karsenty,G.
  TITLE     Genomic organization, expression of the human CBFA1 gene, and
            evidence for an alternative splicing event affecting protein
            function
  JOURNAL   Mamm Genome 9 (1), 54-57 (1998)
   PUBMED   9434946
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Feldman,G.J., Robin,N.H., Brueton,L.A., Robertson,E.,
            Thompson,E.M., Siegel-Bartelt,J., Gasser,D.L., Bailey,L.C.,
            Zackai,E.H. and Muenke,M.
  TITLE     A gene for cleidocranial dysplasia maps to the short arm of
            chromosome 6
  JOURNAL   Am J Hum Genet 56 (4), 938-943 (1995)
   PUBMED   7717404
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Levanon,D., Negreanu,V., Bernstein,Y., Bar-Am,I., Avivi,L. and
            Groner,Y.
  TITLE     AML1, AML2, and AML3, the human members of the runt domain
            gene-family: cDNA structure, expression, and chromosomal
            localization
  JOURNAL   Genomics 23 (2), 425-432 (1994)
   PUBMED   7835892
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Ogawa,E., Maruyama,M., Kagoshima,H., Inuzuka,M., Lu,J., Satake,M.,
            Shigesada,K. and Ito,Y.
  TITLE     PEBP2/PEA2 represents a family of transcription factors homologous
            to the products of the Drosophila runt gene and the human AML1 gene
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6859-6863 (1993)
   PUBMED   8341710
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Machol,K., Mendoza-Londono,R. and Lee,B.
  TITLE     Cleidocranial Dysplasia Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301686
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096865.28, AL358135.19 and
            AL161907.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 9, 2009 this sequence version replaced NP_001019801.2.
            
            Summary: This gene is a member of the RUNX family of transcription
            factors and encodes a nuclear protein with an Runt DNA-binding
            domain. This protein is essential for osteoblastic differentiation
            and skeletal morphogenesis and acts as a scaffold for nucleic acids
            and regulatory factors involved in skeletal gene expression. The
            protein can bind DNA both as a monomer or, with more affinity, as a
            subunit of a heterodimeric complex. Two regions of potential
            trinucleotide repeat expansions are present in the N-terminal
            region of the encoded protein, and these and other mutations in
            this gene have been associated with the bone development disorder
            cleidocranial dysplasia (CCD). Transcript variants that encode
            different protein isoforms result from the use of alternate
            promoters as well as alternate splicing. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a, also known as OSF2/CBFA1a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments. There are no full-length
            transcripts supporting this RefSeq in human; however, it is
            represented based on PMID: 9434946, and full-length transcript
            support from the mouse homolog (GeneID: 12393, AF010284.1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2146982 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 9434946
            MANE Ensembl match        :: ENST00000647337.2/ ENSP00000495497.1
            RefSeq Select criteria    :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..521
                     /product="runt-related transcription factor 2 isoform a"
                     /note="core-binding factor, runt domain, alpha subunit 1;
                     acute myeloid leukemia 3 protein; SL3-3 enhancer factor 1
                     alpha A subunit; runt related transcription factor 2;
                     SL3/AKV core-binding factor alpha A subunit;
                     osteoblast-specific transcription factor 2; PEA2-alpha A;
                     PEBP2-alpha A; oncogene AML-3; polyomavirus
                     enhancer-binding protein 2 alpha A subunit"
                     /calculated_mol_wt=56517
     Region          18..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     Region          49..71
                     /region_name="polyglutamine repeat"
                     /note="23Q repeat"
     Region          73..89
                     /region_name="polyalanine repeat"
                     /note="17A repeat"
     Region          102..230
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          222..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     Region          242..258
                     /region_name="Required for interaction with FOXO1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     Region          <266..481
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Site            267
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q08775; propagated from
                     UniProtKB/Swiss-Prot (Q13950.2)"
     Region          336..439
                     /region_name="Interaction with KAT6A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q13950.2)"
     Region          374..468
                     /region_name="Interaction with KAT6B.
                     /evidence=ECO:0000269|PubMed:11965546"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     Region          430..521
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:16407259; propagated from
                     UniProtKB/Swiss-Prot (Q13950.2)"
     Region          460..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13950.2)"
     CDS             1..521
                     /gene="RUNX2"
                     /gene_synonym="AML3; CBF-alpha-1; CBFA1; CCD; CCD1; CLCD;
                     OSF-2; OSF2; PEA2aA; PEBP2aA"
                     /coded_by="NM_001024630.4:198..1763"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43467.2"
                     /db_xref="GeneID:860"
                     /db_xref="HGNC:HGNC:10472"
                     /db_xref="MIM:600211"
ORIGIN      
        1 masnslfstv tpcqqnffwd pstsrrfspp ssslqpgkms dvspvvaaqq qqqqqqqqqq
       61 qqqqqqqqqq qeaaaaaaaa aaaaaaaaav prlrpphdnr tmveiiadhp aelvrtdspn
      121 flcsvlpshw rcnktlpvaf kvvalgevpd gtvvtvmagn denysaelrn asavmknqva
      181 rfndlrfvgr sgrgksftlt itvftnppqv atyhraikvt vdgpreprrh rqklddskps
      241 lfsdrlsdlg riphpsmrvg vppqnprpsl nsapspfnpq gqsqitdprq aqssppwsyd
      301 qsypsylsqm tspsihsttp lsstrgtglp aitdvprris dddtatsdfc lwpstlskks
      361 qagaselgpf sdprqfpsis sltesrfsnp rmhypatfty tppvtsgmsl gmsatthyht
      421 ylpppypgss qsqsgpfqts stpylyygts sgsyqfpmvp ggdrspsrml ppctttsngs
      481 tllnpnlpnq ndgvdadgsh sssptvlnss grmdesvwrp y
//
LOCUS       NP_001077383             445 aa            linear   PRI 20-NOV-2025
DEFINITION  C-terminal-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001077383
VERSION     NP_001077383.1
DBSOURCE    REFSEQ: accession NM_001083914.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Pastoors,D., Havermans,M., Mulet-Lazaro,R., Brian,D., Noort,W.,
            Grasel,J., Hoogenboezem,R., Smeenk,L., Demmers,J.A.A., Milsom,M.D.,
            Enver,T., Groen,R.W.J., Bindels,E. and Delwel,R.
  TITLE     Oncogene EVI1 drives acute myeloid leukemia via a targetable
            interaction with CTBP2
  JOURNAL   Sci Adv 10 (20), eadk9076 (2024)
   PUBMED   38748792
  REMARK    GeneRIF: Oncogene EVI1 drives acute myeloid leukemia via a
            targetable interaction with CTBP2.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Cheung,C.H.Y., Cheng,C.K., Leung,K.T., Zhang,C., Ho,C.Y., Luo,X.,
            Kam,A.Y.F., Xia,T., Wan,T.S.K., Pitts,H.A., Chan,N.P.H.,
            Cheung,J.S., Wong,R.S.M., Zhang,X.B. and Ng,M.H.L.
  TITLE     C-terminal binding protein 2 is a novel tumor suppressor targeting
            the MYC-IRF4 axis in multiple myeloma
  JOURNAL   Blood Adv 8 (9), 2217-2234 (2024)
   PUBMED   38457926
  REMARK    GeneRIF: C-terminal binding protein 2 is a novel tumor suppressor
            targeting the MYC-IRF4 axis in multiple myeloma.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Sekiya,M., Ma,Y., Kainoh,K., Saito,K., Yamazaki,D., Tsuyuzaki,T.,
            Chen,W., Adi Putri,P.I.P., Ohno,H., Miyamoto,T., Takeuchi,Y.,
            Murayama,Y., Sugano,Y., Osaki,Y., Iwasaki,H., Yahagi,N., Suzuki,H.,
            Motomura,K., Matsuzaka,T., Murata,K., Mizuno,S., Takahashi,S. and
            Shimano,H.
  TITLE     Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function
  JOURNAL   Cell Rep 42 (8), 112914 (2023)
   PUBMED   37557182
  REMARK    GeneRIF: Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Holmes,M., Turner,J., Fox,A., Chisholm,O., Crossley,M. and Chong,B.
  TITLE     hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
            and modulates GATA-mediated activation
  JOURNAL   J Biol Chem 274 (33), 23491-23498 (1999)
   PUBMED   10438528
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and
            Otte,A.P.
  TITLE     C-Terminal binding protein is a transcriptional repressor that
            interacts with a specific class of vertebrate Polycomb proteins
  JOURNAL   Mol Cell Biol 19 (1), 777-787 (1999)
   PUBMED   9858600
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Turner,J. and Crossley,M.
  TITLE     Cloning and characterization of mCtBP2, a co-repressor that
            associates with basic Kruppel-like factor and other mammalian
            transcriptional regulators
  JOURNAL   EMBO J 17 (17), 5129-5140 (1998)
   PUBMED   9724649
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB456766.1, BC047018.1 and
            AL731571.3.
            
            Summary: This gene produces alternative transcripts encoding two
            distinct proteins. One protein is a transcriptional repressor,
            while the other isoform is a major component of specialized
            synapses known as synaptic ribbons. Both proteins contain a NAD+
            binding domain similar to NAD+-dependent 2-hydroxyacid
            dehydrogenases. A portion of the 3' untranslated region was used to
            map this gene to chromosome 21q21.3; however, it was noted that
            similar loci elsewhere in the genome are likely. Blast analysis
            shows that this gene is present on chromosome 10. Several
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (3) contains a distinct 5' UTR and
            5' CDS, compared to variant 2. Variants 1, 3, 4, and 5-8 all encode
            the same isoform (1), which has a distinct N-terminus that is 540
            aa shorter than the N-terminus of isoform 2. The protein is thought
            to bind to the C-terminus of the adenovirus E1A proteins. Studies
            in mice suggest that this protein is involved in transcriptional
            repression.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.955549.1,
                                           SRR11853560.4393.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..445
                     /product="C-terminal-binding protein 2 isoform 1"
                     /note="ribeye"
                     /calculated_mol_wt=48814
     Site            22
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     Region          34..352
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(103,106..107,272,321,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(106,134,186..187,189..191,209..213,242..244,246,249,
                     270..272,296..297,321,323..324)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          414..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56545.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     CDS             1..445
                     /gene="CTBP2"
                     /coded_by="NM_001083914.3:410..1747"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7643.1"
                     /db_xref="GeneID:1488"
                     /db_xref="HGNC:HGNC:2495"
                     /db_xref="MIM:602619"
ORIGIN      
        1 malvdkhkvk rqrldriceg irpqimngpl hprplvalld grdctvempi lkdlatvafc
       61 daqstqeihe kvlneavgam myhtitltre dlekfkalrv ivrigsgydn vdikaagelg
      121 iavcnipsaa veetadstic hilnlyrrnt wlyqalregt rvqsveqire vasgaarirg
      181 etlgligfgr tgqavavrak afgfsvifyd pylqdgiers lgvqrvytlq dllyqsdcvs
      241 lhcnlnehnh hlindftikq mrqgaflvna argglvdeka laqalkegri rgaaldvhes
      301 epfsfaqgpl kdapnlictp htawyseqas lemreaaate irraitgrip eslrncvnke
      361 ffvtsapwsv idqqaihpel ngatyryppg ivgvapgglp aamegiipgg ipvthnlptv
      421 ahpsqapspn qptkhgdnre hpneq
//
LOCUS       NP_001077054             829 aa            linear   PRI 20-NOV-2025
DEFINITION  rab GTPase-binding effector protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001077054
VERSION     NP_001077054.1
DBSOURCE    REFSEQ: accession NM_001083585.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 829)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 829)
  AUTHORS   Swanton,E., Bishop,N. and Woodman,P.
  TITLE     Human rabaptin-5 is selectively cleaved by caspase-3 during
            apoptosis
  JOURNAL   J Biol Chem 274 (53), 37583-37590 (1999)
   PUBMED   10608812
REFERENCE   7  (residues 1 to 829)
  AUTHORS   Neve,R.L., Coopersmith,R., McPhie,D.L., Santeufemio,C., Pratt,K.G.,
            Murphy,C.J. and Lynn,S.D.
  TITLE     The neuronal growth-associated protein GAP-43 interacts with
            rabaptin-5 and participates in endocytosis
  JOURNAL   J Neurosci 18 (19), 7757-7767 (1998)
   PUBMED   9742146
REFERENCE   8  (residues 1 to 829)
  AUTHORS   Vitale,G., Rybin,V., Christoforidis,S., Thornqvist,P.,
            McCaffrey,M., Stenmark,H. and Zerial,M.
  TITLE     Distinct Rab-binding domains mediate the interaction of Rabaptin-5
            with GTP-bound Rab4 and Rab5
  JOURNAL   EMBO J 17 (7), 1941-1951 (1998)
   PUBMED   9524117
REFERENCE   9  (residues 1 to 829)
  AUTHORS   Xiao,G.H., Shoarinejad,F., Jin,F., Golemis,E.A. and Yeung,R.S.
  TITLE     The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5
            GTPase activating protein (GAP) in modulating endocytosis
  JOURNAL   J Biol Chem 272 (10), 6097-6100 (1997)
   PUBMED   9045618
REFERENCE   10 (residues 1 to 829)
  AUTHORS   Stenmark,H., Vitale,G., Ullrich,O. and Zerial,M.
  TITLE     Rabaptin-5 is a direct effector of the small GTPase Rab5 in
            endocytic membrane fusion
  JOURNAL   Cell 83 (3), 423-432 (1995)
   PUBMED   8521472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB169027.1, BC041700.1, AF098638.1, DB124187.1, AL157499.1,
            EB387308.1 and BM678290.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1, resulting in
            an isoform (2) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.93406.1,
                                           SRR1660803.224528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..829
                     /product="rab GTPase-binding effector protein 1 isoform 2"
                     /note="rab GTPase-binding effector protein 1; rabaptin-5;
                     neurocrescin; rabaptin-4; rabaptin-5alpha; renal carcinoma
                     antigen NY-REN-17"
                     /calculated_mol_wt=95348
     Region          9..495
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     Region          533..806
                     /region_name="Rab5-bind"
                     /note="Rabaptin-like protein; pfam09311"
                     /db_xref="CDD:462752"
     CDS             1..829
                     /gene="RABEP1"
                     /gene_synonym="RAB5EP; RABPT5"
                     /coded_by="NM_001083585.3:204..2693"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42243.1"
                     /db_xref="GeneID:9135"
                     /db_xref="HGNC:HGNC:17677"
                     /db_xref="MIM:603616"
ORIGIN      
        1 maqpgpasqp dvslqqrvae lekinaeflr aqqqleqefn qkrakfkely lakeedlkrq
       61 navlqaaqdd lghlrtqlwe aqaemenika iatvsentkq eaidevkrqw reevaslqav
      121 mketvrdyeh qfhlrleqer tqwaqyresa ereiadlrrr lsegqeeenl enemkkaqed
      181 aeklrsvvmp mekeiaalkd klteaedkik eleaskvkel nhyleaeksc rtdlemyvav
      241 lntqksvlqe daeklrkelh evchlleqer qqhnqlkhtw qkandqfles qrllmrdmqr
      301 meivltseql rqveelkkkd qeddeqqrln krkdhkkadv eeeikipvvc altqeessaq
      361 lsneeehlds trgsvhslda glllpsgdpf sksdndmfkd glrraqstds lgtsgslqsk
      421 algynykaks agnldesdfg plvgadsvse nfdtaslgsl qmpsgfmltk dqeraikamt
      481 peqeetasll ssvtqgmesa yvspsgyrlv setewnllqk evhnagnklg rrcdmcsnye
      541 kqlqgiqiqe aetrdqvkkl qlmlrqandq lektmkdkqe ledfikqsse dsshqisalv
      601 lraqaseill eelqqglsqa krdvqeqmav lmqsreqvse elvrlqkdnd slqgkhslhv
      661 slqqaedfil pdttealrel vlkyrediin vrtaadhvee klkaeilflk eqiqaeqclk
      721 enleetlqle ienckeeias isslkaeler ikvekgqatv eqlmfeeknk aqrlqteldv
      781 seqvqrdfvk lsqtlqvqle rirqadsler irailndtkl tdinqlpet
//
LOCUS       NP_954634                500 aa            linear   PRI 20-NOV-2025
DEFINITION  adenylosuccinate synthetase isozyme 1 isoform 1 [Homo sapiens].
ACCESSION   NP_954634
VERSION     NP_954634.1
DBSOURCE    REFSEQ: accession NM_199165.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Saito,Y., Nishikawa,A., Iida,A., Mori-Yoshimura,M., Oya,Y.,
            Ishiyama,A., Komaki,H., Nakamura,S., Fujikawa,S., Kanda,T.,
            Yamadera,M., Sakiyama,H., Hayashi,S., Nonaka,I., Noguchi,S. and
            Nishino,I.
  TITLE     ADSSL1 myopathy is the most common nemaline myopathy in Japan with
            variable clinical features
  JOURNAL   Neurology 95 (11), e1500-e1511 (2020)
   PUBMED   32646962
  REMARK    GeneRIF: ADSSL1 myopathy is the most common nemaline myopathy in
            Japan with variable clinical features.
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Park,H.J., Shin,H.Y., Kim,S., Kim,S.H., Lee,Y., Lee,J.H.,
            Hong,J.M., Kim,S.M., Park,K.D., Choi,B.O., Lee,J.H. and Choi,Y.C.
  TITLE     Distal myopathy with ADSSL1 mutations in Korean patients
  JOURNAL   Neuromuscul Disord 27 (5), 465-472 (2017)
   PUBMED   28268051
  REMARK    GeneRIF: Study investigated the clinical manifestation in Korean
            patients with ADSSL1 mutations. Patients with ADSSL1 mutations
            demonstrated distal muscle weakness in adolescence, followed by
            quadriceps muscle weakness in the early 30s. All patients had mild
            facial weakness and two patients complained of easy fatigue while
            eating and chewing. Muscle biopsies and whole body muscle MR
            imaging findings are discussed.
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Rosenthal,S.L., Wang,X., Demirci,F.Y., Barmada,M.M., Ganguli,M.,
            Lopez,O.L. and Kamboh,M.I.
  TITLE     Beta-amyloid toxicity modifier genes and the risk of Alzheimer's
            disease
  JOURNAL   Am J Neurodegener Dis 1 (2), 191-198 (2012)
   PUBMED   22984654
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Sun,H., Li,N., Wang,X., Chen,T., Shi,L., Zhang,L., Wang,J., Wan,T.
            and Cao,X.
  TITLE     Molecular cloning and characterization of a novel muscle
            adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal
            cells
  JOURNAL   Mol Cell Biochem 269 (1-2), 85-94 (2005)
   PUBMED   15786719
  REMARK    GeneRIF: A novel muscle isozyme of adenylosuccinate synthetase,
            human AdSSL1, is identified from human bone marrow stromal cells.
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Iancu,C.V., Borza,T., Choe,J.Y., Fromm,H.J. and Honzatko,R.B.
  TITLE     Recombinant mouse muscle adenylosuccinate synthetase:
            overexpression, kinetics, and crystal structure
  JOURNAL   J Biol Chem 276 (45), 42146-42152 (2001)
   PUBMED   11560929
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Powell,S.M., Zalkin,H. and Dixon,J.E.
  TITLE     Cloning and characterization of the cDNA encoding human
            adenylosuccinate synthetase
  JOURNAL   FEBS Lett 303 (1), 4-10 (1992)
   PUBMED   1592113
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY011538.1, AK096720.1,
            BC047904.1 and AJ573490.1.
            
            Summary: This gene encodes a member of the adenylosuccinate
            synthase family of proteins. The encoded muscle-specific enzyme
            plays a role in the purine nucleotide cycle by catalyzing the first
            step in the conversion of inosine monophosphate (IMP) to adenosine
            monophosphate (AMP). Mutations in this gene may cause adolescent
            onset distal myopathy. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032039.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..500
                     /product="adenylosuccinate synthetase isozyme 1 isoform 1"
                     /EC_number="6.3.4.4"
                     /note="adenylosuccinate synthetase isozyme 1; M-type
                     adenylosuccinate synthetase; adenylosuccinate synthetase,
                     basic isozyme; adenylosuccinate synthetase, muscle
                     isozyme; adSS 1; AMPSase 1; IMP--aspartate ligase 1;
                     adenylosuccinate synthase like 1; adenylosuccinate
                     synthetase-like 1"
                     /calculated_mol_wt=54431
     Region          108..497
                     /region_name="Adenylsucc_synt"
                     /note="Adenylosuccinate synthetase; pfam00709"
                     /db_xref="CDD:459912"
     CDS             1..500
                     /gene="ADSS1"
                     /gene_synonym="ADSSL1; MPD5"
                     /coded_by="NM_199165.2:50..1552"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9991.1"
                     /db_xref="GeneID:122622"
                     /db_xref="HGNC:HGNC:20093"
                     /db_xref="MIM:612498"
ORIGIN      
        1 mvgrscgvat qrqgggqrpt nlaltlsssp ahstalpwlp prslqllsgh svpaqptphl
       61 psacggptrv tlgeerawrs hgsnagghtc lprrtagags ltpggerggn naghtvvvdg
      121 keydfhllps giintkavsf igngvvihlp glfeeaekne kkglkdwekr liisdrahlv
      181 fdfhqavdgl qevqrqaqeg knigttkkgi gptysskaar tglricdlls dfdefssrfk
      241 nlahqhqsmf ptleidiegq lkrlkgfaer irpmvrdgvy fmyealhgpp kkilvegana
      301 alldidfgty pfvtssnctv ggvctglgip pqnigdvygv vkayttrvgi gafpteqine
      361 iggllqtrgh ewgvttgrkr rcgwldlmil ryahmvngft alaltkldil dvlgevkvgv
      421 syklngkrip yfpanqemlq kveveyetlp gwkadttgar rwedlppqaq nyirfvenhv
      481 gvavkwvgvg ksresmiqlf
//
LOCUS       NP_001305452             522 aa            linear   PRI 20-NOV-2025
DEFINITION  centromere protein I isoform 3 [Homo sapiens].
ACCESSION   NP_001305452
VERSION     NP_001305452.1
DBSOURCE    REFSEQ: accession NM_001318523.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Feng,Z., Cui,G., Tan,J., Liu,P., Chen,Y., Jiang,Z., Han,Y.,
            Zeng,S., Shen,H. and Cai,C.
  TITLE     Immune infiltration related CENPI associates with the malignant
            features and drug resistance of lung adenocarcinoma
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (3), 167017 (2024)
   PUBMED   38232915
  REMARK    GeneRIF: Immune infiltration related CENPI associates with the
            malignant features and drug resistance of lung adenocarcinoma.
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Wang,J., Liu,X., Chu,H.J., Li,N., Huang,L.Y. and Chen,J.
  TITLE     Centromere Protein I (CENP-I) Is Upregulated in Gastric Cancer,
            Predicts Poor Prognosis, and Promotes Tumor Cell Proliferation and
            Migration
  JOURNAL   Technol Cancer Res Treat 20, 15330338211045510 (2021)
   PUBMED   34617858
  REMARK    GeneRIF: Centromere Protein I (CENP-I) Is Upregulated in Gastric
            Cancer, Predicts Poor Prognosis, and Promotes Tumor Cell
            Proliferation and Migration.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Liu,S.T., Hittle,J.C., Jablonski,S.A., Campbell,M.S., Yoda,K. and
            Yen,T.J.
  TITLE     Human CENP-I specifies localization of CENP-F, MAD1 and MAD2 to
            kinetochores and is essential for mitosis
  JOURNAL   Nat Cell Biol 5 (4), 341-345 (2003)
   PUBMED   12640463
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Roberts,R.G., Kendall,E., Vetrie,D. and Bobrow,M.
  TITLE     Sequence and chromosomal location of a human homologue of LRPR1, an
            FSH primary response gene
  JOURNAL   Genomics 37 (1), 122-124 (1996)
   PUBMED   8921378
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Slegtenhorst-Eegdeman,K.E., Post,M., Baarends,W.M., Themmen,A.P.
            and Grootegoed,J.A.
  TITLE     Regulation of gene expression in Sertoli cells by
            follicle-stimulating hormone (FSH): cloning and characterization of
            LRPR1, a primary response gene encoding a leucine-rich protein
  JOURNAL   Mol Cell Endocrinol 108 (1-2), 115-124 (1995)
   PUBMED   7758824
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012462.2.
            
            Summary: This gene encodes a centromere protein that is a component
            of the CENPA-NAC (nucleosome-associated) complex. This complex is
            critical for accurate chromosome alignment and segregation and it
            ensures proper mitotic progression. This protein regulates the
            recruitment of kinetochore-associated proteins that are required to
            generate the spindle checkpoint signal. The product of this gene is
            involved in the response of gonadal tissues to follicle-stimulating
            hormone. Mutations in this gene may be involved in human X-linked
            disorders of gonadal development and gametogenesis. Alternate
            splicing results in multiple transcript variants. A pseudogene of
            this gene is found on chromosome 13. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (3) has a shorter 5' UTR, lacks
            several 3' exon and has a terminal exon that extends past a splice
            site used in variant 1. The encoded isoform (3) has a shorter
            C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012462.2, SRR14038194.957549.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..522
                     /product="centromere protein I isoform 3"
                     /note="follicle-stimulating hormone primary response
                     protein; leucine-rich primary response protein 1; FSH
                     primary response 1; interphase centromere complex protein
                     19"
                     /calculated_mol_wt=59682
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92674.2)"
     Region          9..521
                     /region_name="CENP-I"
                     /note="Mis6; pfam07778"
                     /db_xref="CDD:429654"
     Site            order(141,145,149,179..180,183,186..187,190,193..196,
                     215..217,221,224,227..232,254)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:439352"
     CDS             1..522
                     /gene="CENPI"
                     /gene_synonym="CENP-I; FSHPRH1; LRPR1"
                     /coded_by="NM_001318523.1:14..1582"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS83482.1"
                     /db_xref="GeneID:2491"
                     /db_xref="HGNC:HGNC:3968"
                     /db_xref="MIM:300065"
ORIGIN      
        1 mspqkrvknv qaqnrtsqgs ssfqttlsaw kvkqdpsnsk niskhgqnnp vgdyehaddq
       61 aeedalqmav gyfekgpika sqnkdktlek hlktvenvaw knglaseeid illnialsgk
      121 fgnavntril kcmipatvis edsvvkavsw lcvgkcsgst kvlfyrwlva mfdfidrkeq
      181 inllygfffa slqddalcpy vchllylltk kenvkpfrvr klldlqakmg mqphlqalls
      241 lykffapali svslpvrkki yfknsenlwk tallavkqrn rgpspeplkl mlgpanvrpl
      301 krkwnslsvi pvlnsssytk ecgkkemsls dclnrsgsfp leqlqsfpql lqnihclelp
      361 sqmgsvlnns lllhyincvr depvllrfyy wlsqtlqeec iwykvnnyeh gkeftnfldt
      421 iiraecflqe gfysceafly kslplwdglc crsqflqlvs wipfssfsev kpllfdhlaq
      481 lfftstiyfk csvlqslkel lqnwllwlsm dihmkpvtns pl
//
LOCUS       NP_001025006             465 aa            linear   PRI 20-NOV-2025
DEFINITION  cerebral cavernous malformations 2 protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_001025006
VERSION     NP_001025006.1
DBSOURCE    REFSEQ: accession NM_001029835.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Chaussenot,A., Ayrignac,X., Chatron,N., Granchon-Riolzir,T.,
            Labauge,P., Tournier-Lasserve,E. and Riant,F.
  TITLE     Loss of heterozygosity in CCM2 cDNA revealing a structural variant
            causing multiple cerebral cavernous malformations
  JOURNAL   Eur J Hum Genet 32 (7), 876-878 (2024)
   PUBMED   38755314
  REMARK    GeneRIF: Loss of heterozygosity in CCM2 cDNA revealing a structural
            variant causing multiple cerebral cavernous malformations.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Gallione,C.J., Detter,M.R., Sheline,A., Christmas,H.M., Lee,C. and
            Marchuk,D.A.
  TITLE     Genetic genealogy uncovers a founder deletion mutation in the
            cerebral cavernous malformations 2 gene
  JOURNAL   Hum Genet 141 (11), 1761-1769 (2022)
   PUBMED   35488064
  REMARK    GeneRIF: Genetic genealogy uncovers a founder deletion mutation in
            the cerebral cavernous malformations 2 gene.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Denier,C., Goutagny,S., Labauge,P., Krivosic,V., Arnoult,M.,
            Cousin,A., Benabid,A.L., Comoy,J., Frerebeau,P., Gilbert,B.,
            Houtteville,J.P., Jan,M., Lapierre,F., Loiseau,H., Menei,P.,
            Mercier,P., Moreau,J.J., Nivelon-Chevallier,A., Parker,F.,
            Redondo,A.M., Scarabin,J.M., Tremoulet,M., Zerah,M., Maciazek,J.
            and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the MGC4607 gene cause cerebral cavernous
            malformations
  JOURNAL   Am J Hum Genet 74 (2), 326-337 (2004)
   PUBMED   14740320
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Liquori,C.L., Berg,M.J., Siegel,A.M., Huang,E., Zawistowski,J.S.,
            Stoffer,T., Verlaan,D., Balogun,F., Hughes,L., Leedom,T.P.,
            Plummer,N.W., Cannella,M., Maglione,V., Squitieri,F., Johnson,E.W.,
            Rouleau,G.A., Ptacek,L. and Marchuk,D.A.
  TITLE     Mutations in a gene encoding a novel protein containing a
            phosphotyrosine-binding domain cause type 2 cerebral cavernous
            malformations
  JOURNAL   Am J Hum Genet 73 (6), 1459-1464 (2003)
   PUBMED   14624391
  REMARK    GeneRIF: MGC4607 encodes a protein with a phosphotyrosine-binding
            domain that may be part of the complex pathway of integrin
            signaling that, when perturbed, causes abnormal vascular
            morphogenesis in the brain, leading to CCM formation.
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK098005.1, BC004903.2 and
            AI538498.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a scaffold protein that functions in the
            stress-activated p38 Mitogen-activated protein kinase (MAPK)
            signaling cascade. The protein interacts with SMAD specific E3
            ubiquitin protein ligase 1 (also known as SMURF1) via a
            phosphotyrosine binding domain to promote RhoA degradation. The
            protein is required for normal cytoskeletal structure, cell-cell
            interactions, and lumen formation in endothelial cells. Mutations
            in this gene result in cerebral cavernous malformations. Multiple
            transcript variants encoding different isoforms have been found for
            this gene.[provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK098005.1, SRR1163655.584448.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..465
                     /product="cerebral cavernous malformations 2 protein
                     isoform 1"
                     /note="malcavernin; cerebral cavernous malformations 2
                     protein; cerebral cavernous malformation 2; osmosensing
                     scaffold for MEKK3; CCM2 scaffolding protein"
                     /calculated_mol_wt=51282
     Region          64..258
                     /region_name="PTB_CCM2"
                     /note="Cerebral cavernous malformation 2 FERM domain
                     C-lobe; cd13166"
                     /db_xref="CDD:269987"
     Site            order(78,112,114,132)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269987"
     Site            order(136,143..146)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269987"
     Site            order(303..307,311..312,314,317..318,320..321,324,337,340,
                     343..345,347..348)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:259825"
     Region          308..402
                     /region_name="CCM2_C"
                     /note="Cerebral cavernous malformation protein,
                     harmonin-homology; pfam16545"
                     /db_xref="CDD:435415"
     CDS             1..465
                     /gene="CCM2"
                     /gene_synonym="C7orf22; OSM; PP10187"
                     /coded_by="NM_001029835.2:72..1469"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34630.1"
                     /db_xref="GeneID:83605"
                     /db_xref="HGNC:HGNC:21708"
                     /db_xref="MIM:607929"
ORIGIN      
        1 mhsscrqrrn qnlskeipqt efhtgysmen epgivspfkr vflkgeksrd kkahekvter
       61 rplhtvvlsl pervepdrll sdyiekevky lgqltsipgy lnpssrteil hfidnakrah
      121 qlpghltqeh davlslsayn vklawrdged iilrvpihdi aavsyvrdda ahlvvlktaq
      181 dpgispsqsl caessrglsa gslsesavgp veacclvila aeskvaaeel ccllgqvfqv
      241 vytestidfl draifdgast pthhlslhsd dsstkvdike tyeveastfc fpesvdvgga
      301 sphsktises elsasatell qdymltlrtk lssqeiqqfa allheyrnga sihefcinlr
      361 qlygdsrkfl llglrpfipe kdsqhfenfl etigvkdgrg iitdsfgrhr ralsttssst
      421 tngnratgss ddrsapsegd ewdrmisdis sdiealgcsm dqdsa
//
LOCUS       NP_612139                 77 aa            linear   PRI 20-NOV-2025
DEFINITION  V-type proton ATPase subunit G 2 isoform b [Homo sapiens].
ACCESSION   NP_612139
VERSION     NP_612139.1
DBSOURCE    REFSEQ: accession NM_138282.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Hohn,A., Sittig,A., Jung,T., Grimm,S. and Grune,T.
  TITLE     Lipofuscin is formed independently of macroautophagy and lysosomal
            activity in stress-induced prematurely senescent human fibroblasts
  JOURNAL   Free Radic Biol Med 53 (9), 1760-1769 (2012)
   PUBMED   22982048
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Mewar,D., Marinou,I., Lee,M.E., Timms,J.M., Kilding,R., Teare,M.D.,
            Read,R.C. and Wilson,A.G.
  TITLE     Haplotype-specific gene expression profiles in a telomeric major
            histocompatibility complex gene cluster and susceptibility to
            autoimmune diseases
  JOURNAL   Genes Immun 7 (8), 625-631 (2006)
   PUBMED   16971954
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Smith,A.N., Borthwick,K.J. and Karet,F.E.
  TITLE     Molecular cloning and characterization of novel tissue-specific
            isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and
            their evaluation in autosomal recessive distal renal tubular
            acidosis
  JOURNAL   Gene 297 (1-2), 169-177 (2002)
   PUBMED   12384298
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Neville,M.J. and Campbell,R.D.
  TITLE     A new member of the Ig superfamily and a V-ATPase G subunit are
            among the predicted products of novel genes close to the TNF locus
            in the human MHC
  JOURNAL   J Immunol 162 (8), 4745-4754 (1999)
   PUBMED   10202016
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Nelson,N. and Harvey,W.R.
  TITLE     Vacuolar and plasma membrane proton-adenosinetriphosphatases
  JOURNAL   Physiol Rev 79 (2), 361-385 (1999)
   PUBMED   10221984
  REMARK    Review article
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Finbow,M.E. and Harrison,M.A.
  TITLE     The vacuolar H+-ATPase: a universal proton pump of eukaryotes
  JOURNAL   Biochem J 324 (Pt 3) (Pt 3), 697-712 (1997)
   PUBMED   9210392
  REMARK    Review article
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Stevens,T.H. and Forgac,M.
  TITLE     Structure, function and regulation of the vacuolar (H+)-ATPase
  JOURNAL   Annu Rev Cell Dev Biol 13, 779-808 (1997)
   PUBMED   9442887
  REMARK    Review article
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Dautry-Varsat,A.
  TITLE     Receptor-mediated endocytosis: the intracellular journey of
            transferrin and its receptor
  JOURNAL   Biochimie 68 (3), 375-381 (1986)
   PUBMED   2874839
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA401769.1 and AL662801.7.
            
            Summary: This gene encodes a component of vacuolar ATPase
            (V-ATPase), a multisubunit enzyme that mediates acidification of
            intracellular compartments of eukaryotic cells. V-ATPase dependent
            acidification is necessary for such intracellular processes as
            protein sorting, zymogen activation, receptor-mediated endocytosis,
            and synaptic vesicle proton gradient generation. V-ATPase is
            composed of a cytosolic V1 domain and a transmembrane V0 domain.
            The V1 domain consists of three A and three B subunits, two G
            subunits plus the C, D, E, F, and H subunits. The V1 domain
            contains the ATP catalytic site. The V0 domain consists of five
            different subunits: a, c, c', c'', and d. Additional isoforms of
            many of the V1 and V0 subunit proteins are encoded by multiple
            genes or alternatively spliced transcript variants. This encoded
            protein is one of three V1 domain G subunit proteins. This gene had
            previous gene symbols of ATP6G and ATP6G2. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. Read-through transcription also exists between this gene
            and the downstream DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B
            (DDX39B) gene. [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1123564.1,
                                           SRR3476690.214045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..77
                     /product="V-type proton ATPase subunit G 2 isoform b"
                     /EC_number="7.1.2.2"
                     /note="vacuolar ATP synthase subunit G 2; V-ATPase 13 kDa
                     subunit 2; vacuolar proton pump G subunit 2;
                     H(+)-transporting two-sector ATPase, subunit G2; V-type
                     proton ATPase subunit G 2; ATPase, H+ transporting,
                     lysosomal (vacuolar proton pump); ATPase, H+ transporting,
                     lysosomal 13kDa, V1 subunit G2"
                     /calculated_mol_wt=8841
     Region          <1..66
                     /region_name="V-ATPase_G"
                     /note="Vacuolar (H+)-ATPase G subunit; pfam03179"
                     /db_xref="CDD:460836"
     CDS             1..77
                     /gene="ATP6V1G2"
                     /gene_synonym="ATP6G; ATP6G2; NG38; VMA10"
                     /coded_by="NM_138282.3:153..386"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4699.1"
                     /db_xref="GeneID:534"
                     /db_xref="HGNC:HGNC:862"
                     /db_xref="MIM:606853"
ORIGIN      
        1 meveqyrrer ehefqskqqa amgsqgnlsa eveqatrrqv qgmqssqqrn rervlaqllg
       61 mvcdvrpqvh pnyrisa
//
LOCUS       NP_001129488             746 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform d [Homo sapiens].
ACCESSION   NP_001129488
VERSION     NP_001129488.1
DBSOURCE    REFSEQ: accession NM_001136016.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 746)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK311717.1, AK295621.1,
            Y00264.1 and BM876312.1.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence and lacks an alternate in-frame exon compared to
            variant 1. The resulting isoform (d) has a shorter and distinct
            N-terminus and lacks an internal segment compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295621.1, SRR14372079.875247.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 20209079
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..746
                     /product="amyloid-beta precursor protein isoform d"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=84391
     Region          19..183
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          289..336
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(292..300,315,317,319)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          342..524
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     mat_peptide     648..689
                     /product="amyloid-beta precursor protein isoform d"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /exception="alternative processing"
                     /calculated_mol_wt=4514
     mat_peptide     648..687
                     /product="amyloid-beta precursor protein isoform d"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /calculated_mol_wt=4330
     Region          669..743
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Site            order(682..683,685..686,688..694,696..701)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     CDS             1..746
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_001136016.3:197..2437"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS56212.1"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mdqledllvl finyvptdgn agllaepqia mfcgrlnmhm nvqngkwdsd psgtktcidt
       61 kegilqycqe vypelqitnv veanqpvtiq nwckrgrkqc kthphfvipy rclvgefvsd
      121 allvpdkckf lhqermdvce thlhwhtvak etcsekstnl hdygmllpcg idkfrgvefv
      181 ccplaeesdn vdsadaeedd sdvwwggadt dyadgsedkv vevaeeeeva eveeeeaddd
      241 eddedgdeve eeaeepyeea terttsiatt tttttesvee vvrevcseqa etgpcramis
      301 rwyfdvtegk capffyggcg gnrnnfdtee ycmavcgsai pttaastpda vdkyletpgd
      361 enehahfqka kerleakhre rmsqvmrewe eaerqaknlp kadkkaviqh fqekvesleq
      421 eaanerqqlv ethmarveam lndrrrlale nyitalqavp prprhvfnml kkyvraeqkd
      481 rqhtlkhfeh vrmvdpkkaa qirsqvmthl rviyermnqs lsllynvpav aeeiqdevde
      541 llqkeqnysd dvlanmisep risygndalm psltetkttv ellpvngefs lddlqpwhsf
      601 gadsvpante nevepvdarp aadrglttrp gsgltnikte eisevkmdae frhdsgyevh
      661 hqklvffaed vgsnkgaiig lmvggvviat vivitlvmlk kkqytsihhg vvevdaavtp
      721 eerhlskmqq ngyenptykf feqmqn
//
LOCUS       NP_001363               4486 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein axonemal heavy chain 9 isoform 2 [Homo sapiens].
ACCESSION   NP_001363
VERSION     NP_001363.2
DBSOURCE    REFSEQ: accession NM_001372.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4486)
  AUTHORS   Wang,X., Shen,G., Yang,Y., Jiang,C., Ruan,T., Yang,X., Zhuo,L.,
            Zhang,Y., Ou,Y., Zhao,X., Long,S., Tang,X., Lin,T. and Shen,Y.
  TITLE     DNAH3 deficiency causes flagellar inner dynein arm loss and male
            infertility in humans and mice
  JOURNAL   Elife 13, 96755 (2024)
   PUBMED   39503742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4486)
  AUTHORS   Cadore,N.A., Lord,V.O., Recamonde-Mendoza,M., Kowalski,T.W. and
            Vianna,F.S.L.
  TITLE     Meta-analysis of Transcriptomic Data from Lung Autopsy and Cellular
            Models of SARS-CoV-2 Infection
  JOURNAL   Biochem Genet 62 (2), 892-914 (2024)
   PUBMED   37486510
  REMARK    GeneRIF: Meta-analysis of Transcriptomic Data from Lung Autopsy and
            Cellular Models of SARS-CoV-2 Infection.
REFERENCE   3  (residues 1 to 4486)
  AUTHORS   De Ita,M., Gaytan-Cervantes,J., Cisneros,B., Araujo,M.A.,
            Huicochea-Montiel,J.C., Cardenas-Conejo,A., Lazo-Cardenas,C.C.,
            Ramirez-Portillo,C.I., Feria-Kaiser,C., Peregrino-Bejarano,L.,
            Yanez-Gutierrez,L., Gonzalez-Torres,C. and Rosas-Vargas,H.
  TITLE     Clustering of Genetic Anomalies of Cilia Outer Dynein Arm and
            Central Apparatus in Patients with Transposition of the Great
            Arteries
  JOURNAL   Genes (Basel) 13 (9), 1662 (2022)
   PUBMED   36140829
  REMARK    GeneRIF: Clustering of Genetic Anomalies of Cilia Outer Dynein Arm
            and Central Apparatus in Patients with Transposition of the Great
            Arteries.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 4486)
  AUTHORS   Chen,W., Zhang,Y., Shen,L., Zhu,J., Cai,K., Lu,Z., Zeng,W., Zhao,J.
            and Zhou,X.
  TITLE     Biallelic DNAH9 mutations are identified in Chinese patients with
            defective left-right patterning and cilia-related complex
            congenital heart disease
  JOURNAL   Hum Genet 141 (8), 1339-1353 (2022)
   PUBMED   35050399
  REMARK    GeneRIF: Biallelic DNAH9 mutations are identified in Chinese
            patients with defective left-right patterning and cilia-related
            complex congenital heart disease.
REFERENCE   5  (residues 1 to 4486)
  AUTHORS   Tate,G.
  TITLE     Whole-exome sequencing reveals a combination of extremely rare
            single-nucleotide polymorphism of DNAH9 and RSPH1 genes in a
            Japanese fetus with situs viscerum inversus
  JOURNAL   Med Mol Morphol 54 (3), 275-280 (2021)
   PUBMED   34008076
  REMARK    GeneRIF: Whole-exome sequencing reveals a combination of extremely
            rare single-nucleotide polymorphism of DNAH9 and RSPH1 genes in a
            Japanese fetus with situs viscerum inversus.
REFERENCE   6  (residues 1 to 4486)
  AUTHORS   Reed,W., Carson,J.L., Moats-Staats,B.M., Lucier,T., Hu,P.,
            Brighton,L., Gambling,T.M., Huang,C.H., Leigh,M.W. and Collier,A.M.
  TITLE     Characterization of an axonemal dynein heavy chain expressed early
            in airway epithelial ciliogenesis
  JOURNAL   Am J Respir Cell Mol Biol 23 (6), 734-741 (2000)
   PUBMED   11104725
REFERENCE   7  (residues 1 to 4486)
  AUTHORS   Bartoloni,L., Blouin,J., Sainsbury,A.J., Gos,A., Morris,M.A.,
            Affara,N.A., DeLozier-Blanchet,C.D. and Antonarakis,S.E.
  TITLE     Assignment of the human dynein heavy chain gene DNAH17L to human
            chromosome 17p12 by in situ hybridization and radiation hybrid
            mapping
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 188-189 (1999)
   PUBMED   10393427
REFERENCE   8  (residues 1 to 4486)
  AUTHORS   Milisav,I., Jones,M.H. and Affara,N.A.
  TITLE     Characterization of a novel human dynein-related gene that is
            specifically expressed in testis
  JOURNAL   Mamm Genome 7 (9), 667-672 (1996)
   PUBMED   8703119
REFERENCE   9  (residues 1 to 4486)
  AUTHORS   Vaughan,K.T., Mikami,A., Paschal,B.M., Holzbaur,E.L., Hughes,S.M.,
            Echeverri,C.J., Moore,K.J., Gilbert,D.J., Copeland,N.G.,
            Jenkins,N.A. and Vallee,R.B.
  TITLE     Multiple mouse chromosomal loci for dynein-based motility
  JOURNAL   Genomics 36 (1), 29-38 (1996)
   PUBMED   8812413
REFERENCE   10 (residues 1 to 4486)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ404468.1, AC005701.1 and
            AF257737.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 7, 2006 this sequence version replaced NP_001363.1.
            
            Summary: This gene encodes the heavy chain subunit of axonemal
            dynein, a large multi-subunit molecular motor. Axonemal dynein
            attaches to microtubules and hydrolyzes ATP to mediate the movement
            of cilia and flagella. The gene expresses at least two transcript
            variants; additional variants have been described, but their full
            length nature has not been determined. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) is the longer transcript,
            lacking only one of 70 exons (exon 56). Its 5' UTR differs from
            variant 1.  Its encoded protein, isoform 2, uses the same reading
            frame as isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ404468.1, AF257737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158569, SAMN03267765
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262442.9/ ENSP00000262442.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..4486
                     /product="dynein axonemal heavy chain 9 isoform 2"
                     /note="dynein, axonemal, heavy polypeptide 9; DNAH9
                     variant protein; ciliary dynein heavy chain 9; axonemal
                     beta dynein heavy chain 9"
                     /calculated_mol_wt=511749
     Region          1..1831
                     /region_name="Stem. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          214..789
                     /region_name="DHC_N1"
                     /note="Dynein heavy chain, N-terminal region 1; pfam08385"
                     /db_xref="CDD:462457"
     Region          1258..4150
                     /region_name="DYN1"
                     /note="Dynein, heavy chain [Cytoskeleton]; COG5245"
                     /db_xref="CDD:227570"
     Region          1292..1698
                     /region_name="DHC_N2"
                     /note="Dynein heavy chain, N-terminal region 2; pfam08393"
                     /db_xref="CDD:462462"
     Region          1832..2158
                     /region_name="AAA_6"
                     /note="Hydrolytic ATP binding site of dynein motor region;
                     pfam12774"
                     /db_xref="CDD:463697"
     Region          1832..2053
                     /region_name="AAA 1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          2113..2334
                     /region_name="AAA 2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          2440..2688
                     /region_name="AAA 3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          2787..3036
                     /region_name="AAA 4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          3051..3341
                     /region_name="Stalk. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          3067..3410
                     /region_name="MT"
                     /note="Microtubule-binding stalk of dynein motor;
                     pfam12777"
                     /db_xref="CDD:463699"
     Region          3429..3656
                     /region_name="AAA 5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          3866..4092
                     /region_name="AAA 6. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYC9.3)"
     Region          4189..4484
                     /region_name="Dynein_C"
                     /note="Dynein heavy chain C-terminal domain; pfam18199"
                     /db_xref="CDD:465677"
     CDS             1..4486
                     /gene="DNAH9"
                     /gene_synonym="CILD40; DNAH17L; Dnahc9; DNEL1; DYH9;
                     HL-20; HL20"
                     /coded_by="NM_001372.4:30..13490"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11160.1"
                     /db_xref="GeneID:1770"
                     /db_xref="HGNC:HGNC:2953"
                     /db_xref="MIM:603330"
ORIGIN      
        1 mrlaeeraal aaenadgepg adrrlrllgt yvamslrpaa gawercagsa eaeqllqafl
       61 grdaaegprp llvvrpgprg lairpglevg pesglagaka lfflrtgpep pgpdsfrgav
      121 vcgdlpaapl ehlaalfsev vlpvlanekn rlnwphmice dvrrhahslq cdlsvileqv
      181 kgktllplpa gsekmefads ksetvldsid ksviyaiesa vikwsyqvqv vlkressqpl
      241 lqgenptpkv elefwksrye dlkyiynqlr titvrgmakl ldklqssyfp afkamyrdvv
      301 aalaeaqdih vhliplqrhl ealenaefpe vkpqlrpllh vvcliwatck syrspgrltv
      361 llqeicnlli qqasnylspe dllrsevees qrklqvvsdt lsffkqefqd rrenlhtyfk
      421 enqevkewdf qsslvfvrld gflgqlhvve gllktaldfh klgkvefsgv rgnalsqqvq
      481 qmheefqemy rllsgsssdc lylqstdfen dvsefnqkve dldrrlgtif iqafddapgl
      541 ehafklldia gnllerplva rdtsdkylvl iqmfnkdlda vrmiysqhvq eeaelgfspv
      601 hknmptvagg lrwaqelrqr iqgpfsnfgr ithpcmesae gkrmqqkyed mlsllekyet
      661 rlyedwcrtv seksqynlsq pllkrdpetk eitinfnpql isvlkemsyl epremkhmpe
      721 taaamfssrd fyrqlvanle lmanwynkvm ktllevefpl veeelqnidl rlraaeetln
      781 wktegicdyv teitssihdl eqriqktkdn veeiqnimkt wvtpifktkd gkresllsld
      841 drhdrmekyy nlikesglki halvqenlgl fsadptsniw ktyvnsidnl llngfflaie
      901 cslkyllent eckagltpif eaqlslaipe lvfypslesg vkggfcdive glitsifrip
      961 slvprlspqn gsphyqvdld gipdlanmrr tlmervqrmm glccgyqstf sqysylyved
     1021 rkevlgqfll yghiltpeei edhvedgipe nppllsqfkv qidsyetlye evcrlepikv
     1081 fdgwmkidir pfkasllnii krwsllfkqh lvdhvthsla nldafikkse sgllkkvekg
     1141 dfqglveimg hlmavkerqs ntdemfeplk qtiellktye qelpetvfkq leelpekwnn
     1201 ikkvaitvkq qvaplqanev tllrqrctaf daeqqqfweq fhkeapfrfd sihphqmlda
     1261 rhieiqqmes tmasisesas lfevnvpdyk qlrqcrkevc qlkelwdtig mvtssihawe
     1321 ttpwrninve ameleckqfa rhirnldkev rawdaftgle stvwntlssl ravaelqnpa
     1381 irerhwrqlm qatgvsftmd qdttlahllq lqlhhyedev rgivdkaake mgmektlkel
     1441 qttwagmefq yephprtnvp llcsdedlie vlednqvqlq nlvmskyvaf fleevsgwqk
     1501 klstvdavis iwfevqrtwt hlesiftgse diraqlpqds krfegididf kelaydaqki
     1561 pnvvqttnkp glyeklediq grlclcekal aeyldtkrla fprfyflsss dlldilsngt
     1621 apqqvqrhls klfdnmakmr fqldasgept ktslgmyske eeyvafsepc dcsgqveiwl
     1681 nhvlghmkat vrhemtegvt ayeekpreqw lfdhpaqval tctqiwwtte vgmafarlee
     1741 gyesamkdyy kkqvaqlktl itmligqlsk gdrqkimtic tidvhardvv akmiaqkvdn
     1801 aqaflwlsql rhrwddevkh cfanicdaqf lysyeylgnt prlvitpltd rcyitltqsl
     1861 hltmsgapag pagtgktett kdlgralgil vyvfncseqm dykscgniyk glaqtgawgc
     1921 fdefnrisve vlsvvavqvk siqdairdkk qwfsflgeei slnpsvgifi tmnpgyagrt
     1981 elpenlkslf rpcamvvpdf eliceimlva egfieaqsla rkfitlyqlc kellskqdhy
     2041 dwglraiksv lvvagslkrg dpdrpedqvl mrslrdfnip kivtddmpif mgligdlfpa
     2101 ldvprrrdpn fealvrkaiv dlklqaednf vlkvvqleel lavrhsvfvv ggagtgksqv
     2161 lrslhktyqi mkrrpvwtdl npkavtndel fgiinpatge wkdglfssim relanithdg
     2221 pkwilldgdi dpmwieslnt vmddnkvltl asneriplnp tmkllfeish lrtatpatvs
     2281 ragilyinpa dlgwnppvss wiekreiqte ranltilfdk ylptcldtlr trfkkiipip
     2341 eqsmvqmvch lleclltted ipadcpkeiy ehyfvfaaiw afggamvqdq lvdyraefsk
     2401 wwltefktvk fpsqgtifdy yidpetkkfe pwsklvpqfe fdpemplqac lvhtsetirv
     2461 cyfmerlmar qrpvmlvgta gtgksvlvga klasldpeay lvknvpfnyy ttsamlqavl
     2521 ekplekkagr nygppgnkkl iyfiddmnmp evdaygtvqp htiirqhldy ghwydrskls
     2581 lkeitnvqyv scmnptagsf tinprlqrhf svfvlsfpga dalssiysii ltqhlklgnf
     2641 paslqksipp lidlalafhq kiattflptg ikfhyifnlr dfanifqgil fssvecvkst
     2701 wdlirlylhe snrvyrdkmv eekdfdlfdk iqtevlkktf ddiedpveqt qspnlychfa
     2761 ngigepkymp vqswelltqt lvealenhne vntvmdlvlf edamrhvchi nrilesprgn
     2821 allvgvggsg kqsltrlaaf issmdvfqit lrkgyqiqdf kmdlaslclk agvknlntvf
     2881 lmtdaqvade rflvlindll asgeipdlys ddeveniisn vrnevksqgl vdnrencwkf
     2941 fidrirrqlk vtlcfspvgn klrvrsrkfp aivnctaihw fhewpqqale svslrflqnt
     3001 egieptvkqs iskfmafvht svnqtsqsyl sneqrynytt pksflefirl yqsllhrhrk
     3061 elkckterle ngllklhsts aqvddlkakl aaqevelkqk nedadkliqv vgvetdkvsr
     3121 ekamadeeeq kvavimlevk qkqkdceedl akaepaltaa qaalntlnkt nltelksfgs
     3181 pplavsnvsa avmvlmaprg rvpkdrswka akvtmakvdg fldslinfnk enihenclka
     3241 irpylqdpef npefvatksy aaaglcswvi nivrfyevfc dvepkrqaln katadltaaq
     3301 eklaaikaki ahlnenlakl tarfekatad klkcqqeaev tavtislanr lvgglasenv
     3361 rwadavqnfk qqertlcgdi llitafisyl gfftkkyrqs lldrtwrpyl sqlktpipvt
     3421 paldplrmlm ddadvaawqn eglpadrmsv enatilince rwplmvdpql qgikwiknky
     3481 gedlrvtqig qkgylqiieq aleagavvli enleesidpv lgpllgrevi kkgrfikigd
     3541 keceynpkfr lilhtklanp hyqpelqaqa tlinftvtrd gledqllaav vsmerpdleq
     3601 lksdltkqqn gfkitlktle dsllsrlssa sgnflgetvl venleitkqt aaevekkvqe
     3661 akvtevkine arehyrpaaa rasllyfimn dlskihpmyq fslkafsivf qkaveraapd
     3721 eslrervanl idsitfsvyq ytirglfecd kltylaqltf qillmnrevn aveldfllrs
     3781 pvqtgtaspv eflshqawga vkvlssmeef snldrdiegs akswkkfves ecpekeklpq
     3841 ewknktalqr lcmlramrpd rmtyalrdfv eeklgskyvv graldfatsf eesgpatpmf
     3901 filspgvdpl kdvesqgrkl gytfnnqnfh nvslgqgqev vaeaaldlaa kkghwvilqn
     3961 ihlvakwlst lekkleehse nshpefrvfm saepapspeg hiipqgilen sikitneppt
     4021 gmhanlhkal dnftqdtlem csretefksi lfalcyfhav vaerrkfgpq gwnrsypfnt
     4081 gdltisvnvl ynfleanakv pyddlrylfg eimygghitd dwdrrlcrty lgefirpeml
     4141 egelslapgf plpgnmdyng yhqyidaelp pespylyglh pnaeigfltq tseklfrtvl
     4201 elqprdsqar dgagatreek vkalleeile rvtdefnipe lmakveertp yivvafqecg
     4261 rmniltreiq rslrelelgl kgeltmtshm enlqnalyfd mvpeswarra ypstaglaaw
     4321 fpdllnrike leawtgdftm pstvwltgff npqsfltaim qstarknewp ldqmalqcdm
     4381 tkknreefrs ppregayihg lfmegacwdt qagiiteakl kdltppmpvm fikaipadkq
     4441 dcrsvyscpv yktsqrgpty vwtfnlktke npskwvlagv alllqi
//
LOCUS       NP_001305431             643 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol polyphosphate 5-phosphatase type IV isoform 2
            [Homo sapiens].
ACCESSION   NP_001305431 XP_005266151
VERSION     NP_001305431.1
DBSOURCE    REFSEQ: accession NM_001318502.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Zhai,D., Li,L., Chen,C., Wang,X., Liu,R. and Shan,Y.
  TITLE     INPP5E Regulates the Distribution of Phospholipids on Cilia in RPE1
            Cells
  JOURNAL   J Clin Lab Anal 38 (7), e25031 (2024)
   PUBMED   38514901
  REMARK    GeneRIF: INPP5E Regulates the Distribution of Phospholipids on
            Cilia in RPE1 Cells.
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Yinsheng,Z., Miyoshi,K., Qin,Y., Fujiwara,Y., Yoshimura,T. and
            Katayama,T.
  TITLE     TMEM67 is required for the gating function of the transition zone
            that controls entry of membrane-associated proteins ARL13B and
            INPP5E into primary cilia
  JOURNAL   Biochem Biophys Res Commun 636 (Pt 1), 162-169 (2022)
   PUBMED   36334440
  REMARK    GeneRIF: TMEM67 is required for the gating function of the
            transition zone that controls entry of membrane-associated proteins
            ARL13B and INPP5E into primary cilia.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Schembs,L., Willems,A., Hasenpusch-Theil,K., Cooper,J.D.,
            Whiting,K., Burr,K., Bostrand,S.M.K., Selvaraj,B.T., Chandran,S.
            and Theil,T.
  TITLE     The ciliary gene INPP5E confers dorsal telencephalic identity to
            human cortical organoids by negatively regulating Sonic hedgehog
            signaling
  JOURNAL   Cell Rep 39 (7), 110811 (2022)
   PUBMED   35584663
  REMARK    GeneRIF: The ciliary gene INPP5E confers dorsal telencephalic
            identity to human cortical organoids by negatively regulating Sonic
            hedgehog signaling.
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Kong,A.M., Speed,C.J., O'Malley,C.J., Layton,M.J., Meehan,T.,
            Loveland,K.L., Cheema,S., Ooms,L.M. and Mitchell,C.A.
  TITLE     Cloning and characterization of a 72-kDa inositol-polyphosphate
            5-phosphatase localized to the Golgi network
  JOURNAL   J Biol Chem 275 (31), 24052-24064 (2000)
   PUBMED   10806194
  REMARK    GeneRIF: Functional analysis of the mouse counterpart.
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Kisseleva,M.V., Wilson,M.P. and Majerus,P.W.
  TITLE     The isolation and characterization of a cDNA encoding
            phospholipid-specific inositol polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 275 (26), 20110-20116 (2000)
   PUBMED   10764818
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Saar,K., Al-Gazali,L., Sztriha,L., Rueschendorf,F., Nur-E-Kamal,M.,
            Reis,A. and Bayoumi,R.
  TITLE     Homozygosity mapping in families with Joubert syndrome identifies a
            locus on chromosome 9q34.3 and evidence for genetic heterogeneity
  JOURNAL   Am J Hum Genet 65 (6), 1666-1671 (1999)
   PUBMED   10577920
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL592301.14, AL832846.1 and
            BC028032.1.
            
            On Jan 8, 2016 this sequence version replaced XP_005266151.1.
            
            Summary: The protein encoded by this gene is an inositol
            1,4,5-trisphosphate (InsP3) 5-phosphatase. InsP3 5-phosphatases
            hydrolyze Ins(1,4,5)P3, which mobilizes intracellular calcium and
            acts as a second messenger mediating cell responses to various
            stimulation. Studies of the mouse counterpart suggest that this
            protein may hydrolyze phosphatidylinositol 3,4,5-trisphosphate and
            phosphatidylinositol 3,5-bisphosphate on the cytoplasmic Golgi
            membrane and thereby regulate Golgi-vesicular trafficking.
            Mutations in this gene cause Joubert syndrome; a clinically and
            genetically heterogenous group of disorders characterized by
            midbrain-hindbrain malformation and various associated ciliopathies
            that include retinal dystrophy, nephronophthisis, liver fibrosis
            and polydactyly. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in an internal exon, compared to variant 1. It encodes
            isoform 2 which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832846.1, SRR1803613.225672.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..643
                     /product="phosphatidylinositol polyphosphate 5-phosphatase
                     type IV isoform 2"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="phosphatidylinositol polyphosphate 5-phosphatase
                     type IV; 72 kDa inositol polyphosphate 5-phosphatase;
                     phosphatidylinositol-4,5-bisphosphate 5-phosphatase;
                     phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase"
                     /calculated_mol_wt=70034
     Region          1..193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRR6.2)"
     Region          <2..179
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          10..242
                     /region_name="13 X 4 AA repeats of P-X-X-P"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRR6.2)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRR6.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVR1; propagated from
                     UniProtKB/Swiss-Prot (Q9NRR6.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JII1; propagated from
                     UniProtKB/Swiss-Prot (Q9NRR6.2)"
     Region          295..592
                     /region_name="INPP5c_INPP5E-like"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of Inositol polyphosphate-5-phosphatase E
                     and related proteins; cd09095"
                     /db_xref="CDD:197329"
     Site            order(307,309,340,403..404,424,427,476,478,480,533..534,
                     549,555,582..583)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197329"
     Site            order(307,340,424,476,478,555,582..583)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197329"
     Site            order(340,403..404,424,427,480,533..534,549,582)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197329"
     Site            order(340,582)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197329"
     Site            order(424,478,583)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197329"
     Site            640
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000305|PubMed:24166846; propagated from
                     UniProtKB/Swiss-Prot (Q9NRR6.2)"
     CDS             1..643
                     /gene="INPP5E"
                     /gene_synonym="CORS1; CPD4; JBTS1; MORMS; pharbin;
                     PPI5PIV"
                     /coded_by="NM_001318502.2:427..2358"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:56623"
                     /db_xref="HGNC:HGNC:21474"
                     /db_xref="MIM:613037"
ORIGIN      
        1 mpskaenlrp sepapqppeg rtlqgqlpga ppaqragspp dapgsespal acstpatpsg
       61 edpparaapi aprpparprl eralslddkg wrrrrfrgsq edlearngts psrgsvqseg
      121 pgapahscsp pclstslqei pksrgvlsse rgspssggnp lsgvassspn lphrdaavag
      181 ssprlpsllp prpppalsld iasdslrtan kvdsdladyk lraqpllvra hsslgpgrpr
      241 splacddcsl rsakssfsll apirskdvrs rsylegslla sgallgadel aryfpdrnva
      301 lfvatwnmqg qkelppslde fllpaeadya qdlyvigvqe gcsdrrewet rlqetlgphy
      361 vllssaahgv lymslfirrd liwfcsevec stvttrivsq iktkgalgis ftffgtsflf
      421 itshftcdgk vaerlldytr tvqalvlprn vpdtnpyrss aadvttrfde vfwfgdfnfr
      481 lsggrtvvda llcqglvvdv pallqhdqli remrkgsifk gfqepdihfl psykfdigkd
      541 tydstskqrt psytdrvlyr srhkgdicpv sysscpgikt sdhrpvyglf rvkvrpgrdn
      601 iplaagkfdr elyllgikrr iskeiqrqqa lqsqnsstic svs
//
LOCUS       NP_076941                635 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich repeat and fibronectin type-III domain-containing
            protein 4 precursor [Homo sapiens].
ACCESSION   NP_076941
VERSION     NP_076941.2
DBSOURCE    REFSEQ: accession NM_024036.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Zheng,F., Zhai,X.L., Wang,W.J., Guo,K.P., Xiao,C.C. and Ni,Q.C.
  TITLE     [Expression and clinical significance of LRFN4 in colorectal cancer
            tissue]
  JOURNAL   Zhonghua Yi Xue Za Zhi 100 (22), 1745-1749 (2020)
   PUBMED   32536098
  REMARK    GeneRIF: [Expression and clinical significance of LRFN4 in
            colorectal cancer tissue].
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Liu,Y., Chen,X., Chen,X., Yang,X., Song,Q. and Wu,H.
  TITLE     High SALM3 Expression in Tumor Cells and Fibroblasts Is Correlated
            with Poor Prognosis in Gastric Cancer Patients
  JOURNAL   Dis Markers 2019, 8282414 (2019)
   PUBMED   31089399
  REMARK    GeneRIF: SALM3 is overexpressed in the tumor cells and fibroblasts
            of gastric cancer patients.  High SALM3 expression is associated
            with poor prognosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
  REMARK    GeneRIF: SALM3 regulates excitatory synapse development and
            locomotion behavior.
REFERENCE   6  (residues 1 to 635)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 635)
  AUTHORS   Konakahara,S., Saitou,M., Hori,S., Nakane,T., Murai,K., Itoh,R.,
            Shinsaka,A., Kohroki,J., Kawakami,T., Kajikawa,M. and Masuho,Y.
  TITLE     A neuronal transmembrane protein LRFN4 induces monocyte/macrophage
            migration via actin cytoskeleton reorganization
  JOURNAL   FEBS Lett 585 (14), 2377-2384 (2011)
   PUBMED   21704618
  REMARK    GeneRIF: Data indicate that LRFN4 signaling plays an important role
            in the migration of monocytes/macrophages.
REFERENCE   8  (residues 1 to 635)
  AUTHORS   Nam,J., Mah,W. and Kim,E.
  TITLE     The SALM/Lrfn family of leucine-rich repeat-containing cell
            adhesion molecules
  JOURNAL   Semin Cell Dev Biol 22 (5), 492-498 (2011)
   PUBMED   21736948
  REMARK    Review article
REFERENCE   9  (residues 1 to 635)
  AUTHORS   Morimura,N., Inoue,T., Katayama,K. and Aruga,J.
  TITLE     Comparative analysis of structure, expression and PSD95-binding
            capacity of Lrfn, a novel family of neuronal transmembrane proteins
  JOURNAL   Gene 380 (2), 72-83 (2006)
   PUBMED   16828986
REFERENCE   10 (residues 1 to 635)
  AUTHORS   Wang,C.Y., Chang,K., Petralia,R.S., Wang,Y.X., Seabold,G.K. and
            Wenthold,R.J.
  TITLE     A novel family of adhesion-like molecules that interacts with the
            NMDA receptor
  JOURNAL   J Neurosci 26 (8), 2174-2183 (2006)
   PUBMED   16495444
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003176.2, CN297399.1 and BC015581.2.
            
            On Dec 23, 2002 this sequence version replaced NP_076941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015581.2, SRR1163655.594494.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309602.5/ ENSP00000312535.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..635
                     /product="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 4 precursor"
                     /note="fibronectin type III, immunoglobulin and leucine
                     rich repeat domains 6; leucine-rich repeat and fibronectin
                     type-III domain-containing protein 4"
                     /calculated_mol_wt=65357
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1522
     mat_peptide     17..635
                     /product="Leucine-rich repeat and fibronectin type-III
                     domain-containing protein 4. /id=PRO_0000014843"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
                     /calculated_mol_wt=65357
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          49..70
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          50..73
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <52..>215
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          73..94
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          74..97
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          97..118
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          98..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          121..142
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          122..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          146..161
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          147..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          170..191
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          171..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          194..215
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          195..213
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          234..278
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          281..368
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          298..302
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409421"
     Region          311..315
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409421"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          334..338
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409421"
     Region          348..353
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409421"
     Region          361..364
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409421"
     Region          373..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          409..478
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            440
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            519..539
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          555..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          632..635
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     CDS             1..635
                     /gene="LRFN4"
                     /gene_synonym="FIGLER6; SALM3; SALM3."
                     /coded_by="NM_024036.5:682..2589"
                     /db_xref="CCDS:CCDS8153.1"
                     /db_xref="GeneID:78999"
                     /db_xref="HGNC:HGNC:28456"
                     /db_xref="MIM:612810"
ORIGIN      
        1 mappllllll asgaaacplp cvcqnlsesl stlcahrgll fvppnvdrrt velrladnfi
       61 qalgppdfrn mtglvdltls rnaitrigar afgdleslrs lhldgnrlve lgtgslrgpv
      121 nlqhlilsgn qlgriapgaf ddflesledl dlsynnlrqv pwagigampa lhtlnldhnl
      181 idalppgafa qlgqlsrldl tsnrlatlap dplfsrgrda easpaplvls fsgnplhcnc
      241 ellwlrrlar pddletcasp pglagryfwa vpegefscep pliarhtqrl wvlegqratl
      301 rcralgdpap tmhwvgpddr lvgnssrara fpngtleigv tgagdaggyt ciatnpagea
      361 tarvelrvla lphggnssae ggrpgpsdia asartaaege gtlesepavq vtevtatsgl
      421 vswgpgrpad pvwmfqiqyn ssedetliyr ivpasshhfl lkhlvpgady dlcllalspa
      481 agpsdltatr llgcahfstl pasplchalq ahvlggtltv avggvlvaal lvftvallvr
      541 grgagngrlp lklshvqsqt nggpsptpka hpprsppprp qrscsldlgd agcygyarrl
      601 ggawarrshs vhggllgagc rgvggsaerl eesvv
//
LOCUS       NP_079183                278 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 17 isoform 2 [Homo sapiens].
ACCESSION   NP_079183
VERSION     NP_079183.4
DBSOURCE    REFSEQ: accession NM_024907.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Shen,S., Jiang,M., Deng,W., Liu,X., Xiong,J., Zeng,Z., Zhao,H.,
            Zeng,X. and Fu,B.
  TITLE     Circ_0008717 promotes renal cell carcinoma progression by
            upregulating FBXO17 via targeting miR-217
  JOURNAL   J Gene Med 24 (11), e3418 (2022)
   PUBMED   35357059
  REMARK    GeneRIF: Circ_0008717 promotes renal cell carcinoma progression by
            upregulating FBXO17 via targeting miR-217.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Zheng,Z.M., Wang,Y.Y., Chen,M., Yang,H.L., Lai,Z.Z., Li,M.Q. and
            Shao,J.
  TITLE     FBXO17 Inhibits the Wnt/beta-Catenin Pathway and Proliferation of
            Ishikawa Cells
  JOURNAL   Int J Med Sci 19 (9), 1430-1441 (2022)
   PUBMED   36035375
  REMARK    GeneRIF: FBXO17 Inhibits the Wnt/beta-Catenin Pathway and
            Proliferation of Ishikawa Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Deng,C., Li,H. and Li,Q.
  TITLE     F-box protein 17 promotes glioma progression by regulating
            glycolysis pathway
  JOURNAL   Biosci Biotechnol Biochem 86 (4), 455-463 (2022)
   PUBMED   35044455
  REMARK    GeneRIF: F-box protein 17 promotes glioma progression by regulating
            glycolysis pathway.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Sun,D., Yang,K.S., Chen,J.L. and Wang,Z.B.
  TITLE     Identification and validation of an immune-associated RNA-binding
            proteins signature to predict clinical outcomes and therapeutic
            responses in colon cancer patients
  JOURNAL   World J Surg Oncol 19 (1), 314 (2021)
   PUBMED   34702278
  REMARK    GeneRIF: Identification and validation of an immune-associated
            RNA-binding proteins signature to predict clinical outcomes and
            therapeutic responses in colon cancer patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Glenn,K.A., Nelson,R.F., Wen,H.M., Mallinger,A.J. and Paulson,H.L.
  TITLE     Diversity in tissue expression, substrate binding, and SCF complex
            formation for a lectin family of ubiquitin ligases
  JOURNAL   J Biol Chem 283 (19), 12717-12729 (2008)
   PUBMED   18203720
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Szafranski,K., Schindler,S., Taudien,S., Hiller,M., Huse,K.,
            Jahn,N., Schreiber,S., Backofen,R. and Platzer,M.
  TITLE     Violating the splicing rules: TG dinucleotides function as
            alternative 3' splice sites in U2-dependent introns
  JOURNAL   Genome Biol 8 (8), R154 (2007)
   PUBMED   17672918
  REMARK    GeneRIF: the apparent occurrence of an unusual TG 3' splice site in
            intron 3 is discussed
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Ilyin,G.P., Serandour,A.L., Pigeon,C., Rialland,M., Glaise,D. and
            Guguen-Guillouzo,C.
  TITLE     A new subfamily of structurally related human F-box proteins
  JOURNAL   Gene 296 (1-2), 11-20 (2002)
   PUBMED   12383498
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Kipreos,E.T. and Pagano,M.
  TITLE     The F-box protein family
  JOURNAL   Genome Biol 1 (5), REVIEWS3002 (2000)
   PUBMED   11178263
  REMARK    Review article
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF594009.1, AF386743.1,
            BM711851.1, CA429117.1 and AI050825.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 10, 2002 this sequence version replaced NP_079183.3.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by the F-box motif. The F-box proteins
            constitute one of the four subunits of the ubiquitin protein ligase
            complex called SCFs (SKP1-cullin-F-box), which function in
            phosphorylation-dependent ubiquitination. The F-box proteins are
            divided into 3 classes: Fbws containing WD-40 domains, Fbls
            containing leucine-rich repeats, and Fbxs containing either
            different protein-protein interaction modules or no recognizable
            motifs. The protein encoded by this gene belongs to the Fbxs class
            and it contains an F-box domain. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) encodes the shorter isoform
            (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF386743.1, SRR1660805.194695.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292852.9/ ENSP00000292852.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..278
                     /product="F-box only protein 17 isoform 2"
                     /note="F-box only protein 26; F-box protein FBG4"
                     /calculated_mol_wt=31348
     Region          18..65
                     /region_name="F-box_FBXO17-like"
                     /note="F-box domain found in F-box only protein 17
                     (FBXO17), F-box only protein 27 (FBXO27) and similar
                     proteins; cd22169"
                     /db_xref="CDD:438940"
     Site            order(18,21..22,25,29,32,34,37,39,42..47,49..50)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438940"
     Region          100..273
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     CDS             1..278
                     /gene="FBXO17"
                     /gene_synonym="FBG4; Fbx17; FBX26; FBXO26"
                     /coded_by="NM_024907.7:175..1011"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12526.1"
                     /db_xref="GeneID:115290"
                     /db_xref="HGNC:HGNC:18754"
                     /db_xref="MIM:609094"
ORIGIN      
        1 mgarlsrrrl padpslalda lppellvqvl shvpprslvt rcrpvcrawr divdgptvwl
       61 lqlardrsae gralyavaqr clpsnedkee fplcalaryc lrapfgrnli fnscgeqgfr
      121 gwevehggng waieknltpv pgapsqtcfv tsfewcskrq lvdlvmegvw qelldsaqie
      181 icvadwwgar encgcvyqlr vrlldvyeke vvkfsaspdp vlqwtergcr qvshvftnfg
      241 kgiryvsfeq ygrdvsswvg hygalvthss vrvrirls
//
LOCUS       NP_001230217             487 aa            linear   PRI 20-NOV-2025
DEFINITION  nectin-3 isoform 3 [Homo sapiens].
ACCESSION   NP_001230217
VERSION     NP_001230217.1
DBSOURCE    REFSEQ: accession NM_001243288.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 487)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 487)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 487)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 487)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 487)
  AUTHORS   Lachke,S.A., Higgins,A.W., Inagaki,M., Saadi,I., Xi,Q., Long,M.,
            Quade,B.J., Talkowski,M.E., Gusella,J.F., Fujimoto,A.,
            Robinson,M.L., Yang,Y., Duong,Q.T., Shapira,I., Motro,B.,
            Miyoshi,J., Takai,Y., Morton,C.C. and Maas,R.L.
  TITLE     The cell adhesion gene PVRL3 is associated with congenital ocular
            defects
  JOURNAL   Hum Genet 131 (2), 235-250 (2012)
   PUBMED   21769484
REFERENCE   6  (residues 1 to 487)
  AUTHORS   Reymond,N., Fabre,S., Lecocq,E., Adelaide,J., Dubreuil,P. and
            Lopez,M.
  TITLE     Nectin4/PRR4, a new afadin-associated member of the nectin family
            that trans-interacts with nectin1/PRR1 through V domain interaction
  JOURNAL   J Biol Chem 276 (46), 43205-43215 (2001)
   PUBMED   11544254
REFERENCE   7  (residues 1 to 487)
  AUTHORS   Reymond,N., Borg,J.P., Lecocq,E., Adelaide,J., Campadelli-Fiume,G.,
            Dubreuil,P. and Lopez,M.
  TITLE     Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family
            that interacts with afadin
  JOURNAL   Gene 255 (2), 347-355 (2000)
   PUBMED   11024295
REFERENCE   8  (residues 1 to 487)
  AUTHORS   Satoh-Horikawa,K., Nakanishi,H., Takahashi,K., Miyahara,M.,
            Nishimura,M., Tachibana,K., Mizoguchi,A. and Takai,Y.
  TITLE     Nectin-3, a new member of immunoglobulin-like cell adhesion
            molecules that shows homophilic and heterophilic cell-cell adhesion
            activities
  JOURNAL   J Biol Chem 275 (14), 10291-10299 (2000)
   PUBMED   10744716
REFERENCE   9  (residues 1 to 487)
  AUTHORS   Takahashi,K., Nakanishi,H., Miyahara,M., Mandai,K., Satoh,K.,
            Satoh,A., Nishioka,H., Aoki,J., Nomoto,A., Mizoguchi,A. and
            Takai,Y.
  TITLE     Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited
            to cadherin-based adherens junctions through interaction with
            Afadin, a PDZ domain-containing protein
  JOURNAL   J Cell Biol 145 (3), 539-549 (1999)
   PUBMED   10225955
REFERENCE   10 (residues 1 to 487)
  AUTHORS   Lopez,M., Aoubala,M., Jordier,F., Isnardon,D., Gomez,S. and
            Dubreuil,P.
  TITLE     The human poliovirus receptor related 2 protein is a new
            hematopoietic/endothelial homophilic adhesion molecule
  JOURNAL   Blood 92 (12), 4602-4611 (1998)
   PUBMED   9845526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133477.2, AK075105.1,
            AC133436.2 and BQ025085.1.
            
            Summary: This gene encodes a member of the nectin family of
            proteins, which function as adhesion molecules at adherens
            junctions. This family member interacts with other nectin-like
            proteins and with afadin, a filamentous actin-binding protein
            involved in the regulation of directional motility, cell
            proliferation and survival. This gene plays a role in ocular
            development involving the ciliary body. Mutations in this gene are
            believed to result in congenital ocular defects. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and 5'
            coding region, uses a distinct start codon, and has alternate exon
            structure in the 3' coding region and 3' UTR, compared to variant
            1. The encoded isoform (3) has distinct N- and C-termini and is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075105.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..487
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13"
     Protein         1..487
                     /product="nectin-3 isoform 3"
                     /note="nectin 3; poliovirus receptor-related protein 3;
                     poliovirus receptor-related 3"
                     /calculated_mol_wt=54244
     Region          35..144
                     /region_name="IgV_1_Nectin-3_like"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-3 (also known as poliovirus receptor related
                     protein 3), and similar domains; cd05887"
                     /db_xref="CDD:409470"
     Region          35..58
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409470"
     Region          35..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409470"
     Region          41..45
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409470"
     Site            order(49..56,63..71,78..90,108..114,119..133,136..144)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409470"
     Region          50..58
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409470"
     Region          59..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409470"
     Region          64..70
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          65..70
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409470"
     Region          71..90
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          80..85
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          87..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          91..129
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          98..102
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409470"
     Region          107..114
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409470"
     Region          121..129
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409470"
     Region          130..133
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          133..143
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409470"
     Region          134..144
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409470"
     Region          147..242
                     /region_name="IgC1_2_Nectin-3-4_like"
                     /note="Second immunoglobulin (Ig) domain of nectin-3 and
                     nectin-4 (poliovirus receptor related protein 4), and
                     similar domains; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd07704"
                     /db_xref="CDD:409501"
     Region          147..153
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409501"
     Region          166..173
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409501"
     Region          178..184
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409501"
     Region          186..188
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409501"
     Region          190..197
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409501"
     Region          202..210
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409501"
     Region          220..227
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409501"
     Region          233..239
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409501"
     Region          246..332
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          264..268
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          278..282
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          297..302
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          312..317
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          327..330
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..487
                     /gene="NECTIN3"
                     /gene_synonym="CD113; CDW113; NECTIN-3; PPR3; PRR3; PVRL3;
                     PVRR3"
                     /coded_by="NM_001243288.2:605..2068"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58843.1"
                     /db_xref="GeneID:25945"
                     /db_xref="HGNC:HGNC:17664"
                     /db_xref="MIM:607147"
ORIGIN      
        1 maegwrwcfv rrtpgllrgp llprsfsgnp ralagpiive phvtavwgkn vslkclievn
       61 etitqiswek ihgkssqtva vhhpqygfsv qgeyqgrvlf knyslndati tlhnigfsds
      121 gkyickavtf plgnaqsstt vtvlveptvs likgpdslid ggnetvaaic iaatgkpvah
      181 idwegdlgem estttsfpne tatiisqykl fptrfargrr itcvvkhpal ekdirysfil
      241 diqyapevsv tgydgnwfvg rkgvnlkcna danpppfksv wsrldgqwpd gllasdntlh
      301 fvhpltfnys gvyickvtns lgqrsdqkvi yisdvpfkqt ssiavagavi gavlalfiia
      361 ifvtvlltpr kkrpsyldkv idlppthkpp plyeersppl pqkdlfqpeh lplqtqfker
      421 evgnlqhsng lnsrsfdyed enpvgedgiq qmyplynqmc yqdrspgkhh qnndpkrvyi
      481 dprehyv
//
LOCUS       NP_001353133             871 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353133 XP_016861306
VERSION     NP_001353133.1
DBSOURCE    REFSEQ: accession NM_001366204.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861306.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.75522.1,
                                           SRR1803613.6201.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366204.1:109..2724"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_001339875             665 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 18 [Homo sapiens].
ACCESSION   NP_001339875 XP_006716507
VERSION     NP_001339875.1
DBSOURCE    REFSEQ: accession NM_001352946.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_006716507.1.
            
            Transcript Variant: This variant (21), as well as variants 22 and
            23, encodes isoform 18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1286880.1,
                                           SRR14038194.2779052.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..665
                     /product="DNA repair-scaffolding protein isoform 18"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=72443
     Region          <5..119
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          271..655
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..665
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352946.1:544..2541"
                     /note="isoform 18 is encoded by transcript variant 21"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mrscrsfprg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt vkilelheec
       61 amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv rifppwqkli
      121 ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi kgltnnspei
      181 qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga gvrvvvqrvy
      241 slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar qlegkscslv
      301 gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa lcyiltahpn
      361 lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql kslllleqre
      421 iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl ffkdalrdqg
      481 rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq gtvvgvdest
      541 afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr srpqcrvkvk
      601 llqrsissll rfaagedgsy evksvlgkev gllncfvqsv tahptscigl eeiellsagg
      661 asaeh
//
LOCUS       NP_001268392            1211 aa            linear   PRI 20-NOV-2025
DEFINITION  structural maintenance of chromosomes protein 1A isoform 2 [Homo
            sapiens].
ACCESSION   NP_001268392
VERSION     NP_001268392.1
DBSOURCE    REFSEQ: accession NM_001281463.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Ibstedt,S., Piccinelli,P., Sydow,S., Koster,J. and Mertens,F.
  TITLE     Structural Variants in the SMC1A Gene Associated With Near-Haploidy
            in Undifferentiated Pleomorphic Sarcomas
  JOURNAL   Genes Chromosomes Cancer 63 (8), e23255 (2024)
   PUBMED   39149945
  REMARK    GeneRIF: Structural Variants in the SMC1A Gene Associated With
            Near-Haploidy in Undifferentiated Pleomorphic Sarcomas.
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Li,K., Dai,P., Li,J., Liu,L., Cheng,S., Fang,Q. and Wu,B.
  TITLE     AKT/FOXM1/STMN1 signaling pathway activation by SMC1A promotes
            tumor growth in breast cancer
  JOURNAL   J Gene Med 26 (1), e3661 (2024)
   PUBMED   38282144
  REMARK    GeneRIF: AKT/FOXM1/STMN1 signaling pathway activation by SMC1A
            promotes tumor growth in breast cancer.
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Liu,Y., Fang,X., Wang,Q., Xiao,D., Zhou,T., Kang,K., Peng,Z.,
            Ren,F. and Zhou,J.
  TITLE     SMC1A facilitates gastric cancer cell proliferation, migration, and
            invasion via promoting SNAIL activated EMT
  JOURNAL   BMC Gastroenterol 23 (1), 268 (2023)
   PUBMED   37537540
  REMARK    GeneRIF: SMC1A facilitates gastric cancer cell proliferation,
            migration, and invasion via promoting SNAIL activated EMT.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Chen,Y., Sharp,Z.D. and Lee,W.H.
  TITLE     HEC binds to the seventh regulatory subunit of the 26 S proteasome
            and modulates the proteolysis of mitotic cyclins
  JOURNAL   J Biol Chem 272 (38), 24081-24087 (1997)
   PUBMED   9295362
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Brown,C.J., Miller,A.P., Carrel,L., Rupert,J.L., Davies,K.E. and
            Willard,H.F.
  TITLE     The DXS423E gene in Xp11.21 escapes X chromosome inactivation
  JOURNAL   Hum Mol Genet 4 (2), 251-255 (1995)
   PUBMED   7757075
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Rocques,P.J., Clark,J., Ball,S., Crew,J., Gill,S.,
            Christodoulou,Z., Borts,R.H., Louis,E.J., Davies,K.E. and
            Cooper,C.S.
  TITLE     The human SB1.8 gene (DXS423E) encodes a putative chromosome
            segregation protein conserved in lower eukaryotes and prokaryotes
  JOURNAL   Hum Mol Genet 4 (2), 243-249 (1995)
   PUBMED   7757074
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Deardorff,M.A., Noon,S.E. and Krantz,I.D.
  TITLE     Cornelia de Lange Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233728.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Proper cohesion of sister chromatids is a prerequisite for
            the correct segregation of chromosomes during cell division. The
            cohesin multiprotein complex is required for sister chromatid
            cohesion. This complex is composed partly of two structural
            maintenance of chromosomes (SMC) proteins, SMC3 and either SMC1B or
            the protein encoded by this gene. Most of the cohesin complexes
            dissociate from the chromosomes before mitosis, although those
            complexes at the kinetochore remain. Therefore, the encoded protein
            is thought to be an important part of functional kinetochores. In
            addition, this protein interacts with BRCA1 and is phosphorylated
            by ATM, indicating a potential role for this protein in DNA repair.
            This gene, which belongs to the SMC gene family, is located in an
            area of the X-chromosome that escapes X inactivation. Mutations in
            this gene result in Cornelia de Lange syndrome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and has
            multiple coding region differences, compared to variant 1. These
            differences cause translation initiation at a downstream AUG and
            result in an isoform (2) with a shorter N-terminus, compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC171726.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..1211
                     /product="structural maintenance of chromosomes protein 1A
                     isoform 2"
                     /note="SMC1 (structural maintenance of chromosomes 1,
                     yeast)-like 1; segregation of mitotic chromosomes 1;
                     SMC-1-alpha; SMC protein 1A; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=140729
     Region          15..1188
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; pfam02463"
                     /db_xref="CDD:426784"
     CDS             1..1211
                     /gene="SMC1A"
                     /gene_synonym="CDLS2; DEE85; DXS423E; EIEE85; SB1.8; SMC1;
                     SMC1alpha; SMC1L1; SMCB"
                     /coded_by="NM_001281463.1:341..3976"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75985.1"
                     /db_xref="GeneID:8243"
                     /db_xref="HGNC:HGNC:11111"
                     /db_xref="MIM:300040"
ORIGIN      
        1 mlevsiptph ryvrgksnlm daisfvlgek tsnlrvktlr dlihgapvgk paanrafvsm
       61 vyseegaedr tfarvivggs seykinnkvv qlheyseele klgilikarn flvfqgaves
      121 iamknpkert alfeeisrsg elaqeydkrk kemvkaeedt qfnyhrkkni aaerkeakqe
      181 keeadryqrl kdevvraqvq lqlfklyhne veieklnkel asknkeiekd kkrmdkvede
      241 lkekkkelgk mmreqqqiek eikekdseln qkrpqyikak entshkikkl eaakkslqna
      301 qkhykkrkgd mdelekemls vekarqefee rmeeesqsqg rdltleenqv kkyhrlkeea
      361 skraatlaqe lekfnrdqka dqdrldleer kkveteakik qklreieenq kriekleeyi
      421 ttskqsleeq kklegeltee vemakrride inkelnqvme qlgdaridrq essrqqrkae
      481 imesikrlyp gsvygrlidl cqptqkkyqi avtkvlgknm daiivdsekt grdciqyike
      541 qrgepetflp ldylevkptd eklrelkgak lvidviryep phikkalqya cgnalvcdnv
      601 edarriafgg hqrhktvald gtlfqksgvi sggasdlkak arrwdekavd klkekkerlt
      661 eelkeqmkak rkeaelrqvq sqahglqmrl kysqsdleqt ktrhlalnlq eksklesela
      721 nfgprindik riiqsrerem kdlkekmnqv edevfeefcr eigvrniref eeekvkrqne
      781 iakkrlefen qktrlgiqld feknqlkedq dkvhmweqtv kkdeneiekl kkeeqrhmki
      841 idetmaqlqd lknqhlakks evndknheme eirkklggan kemthlqkev taietkleqk
      901 rsdrhnllqa ckmqdiklpl skgtmddisq eegssqgeds vsgsqrissi yarealieid
      961 ygdlcedlkd aqaeeeikqe mntlqqklne qqsvlqriaa pnmkamekle svrdkfqets
     1021 defeaarkra kkakqafeqi kkerfdrfna cfesvatnid eiykalsrns saqaflgpen
     1081 peepyldgin yncvapgkrf rpmdnlsgge ktvaalallf aihsykpapf fvldeidaal
     1141 dntnigkvan yikeqstcnf qaivislkee fytkaeslig vypeqgdcvi skvltfdltk
     1201 ypdanpnpne q
//
LOCUS       NP_001073926             713 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich repeat-containing protein 4B precursor [Homo sapiens].
ACCESSION   NP_001073926 XP_292778
VERSION     NP_001073926.1
DBSOURCE    REFSEQ: accession NM_001080457.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 713)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 713)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 713)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008743.9.
            
            On Jan 18, 2007 this sequence version replaced XP_292778.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX353402.2, HY109166.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMN03267772
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652263.1/ ENSP00000498662.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..713
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..713
                     /product="leucine-rich repeat-containing protein 4B
                     precursor"
                     /note="leucine-rich repeats and immunoglobulin-like
                     domains 4; leucine-rich repeat-containing protein 4B;
                     netrin-G3 ligand; netrin-G ligand-3"
                     /calculated_mol_wt=72638
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
                     /calculated_mol_wt=3815
     mat_peptide     36..713
                     /product="Leucine-rich repeat-containing protein 4B.
                     /id=PRO_0000231654"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
                     /calculated_mol_wt=72638
     Region          57..90
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          <87..>312
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          87..108
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          88..111
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          111..132
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          112..135
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          135..156
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          136..159
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          159..180
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          160..183
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          183..205
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          184..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..229
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          209..230
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          230..251
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          231..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          254..275
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          255..278
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          278..299
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          279..300
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            283
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          311..361
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          364..453
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Site            374
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          381..385
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          393..397
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            400
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          419..423
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            422
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          433..438
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            444
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          446..449
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            452
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          497..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Site            577..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P0C192; propagated from
                     UniProtKB/Swiss-Prot (Q9NT99.3)"
     Region          694..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NT99.3)"
     CDS             1..713
                     /gene="LRRC4B"
                     /gene_synonym="HSM; LRIG4; NGL-3"
                     /coded_by="NM_001080457.2:528..2669"
                     /db_xref="CCDS:CCDS42595.1"
                     /db_xref="GeneID:94030"
                     /db_xref="HGNC:HGNC:25042"
ORIGIN      
        1 marargspcp plppgrmswp hgallflwlf spplgagggg vavtsaaggg sppatscpva
       61 cscsnqasrv ictrrdlaev pasipvntry lnlqengiqv irtdtfkhlr hleilqlskn
      121 lvrkievgaf nglpslntle lfdnrlttvp tqafeylskl relwlrnnpi esipsyafnr
      181 vpslrrldlg elkrleyise aafeglvnlr ylnlgmcnlk dipnltalvr leelelsgnr
      241 ldlirpgsfq gltslrklwl mhaqvatier nafddlksle elnlshnnlm slphdlftpl
      301 hrlervhlnh npwhcncdvl wlswwlketv psnttccarc hapaglkgry igeldqshft
      361 cyapvivepp tdlnvtegma aelkcrtgts mtsvnwltpn gtlmthgsyr vrisvlhdgt
      421 lnftnvtvqd tgqytcmvtn sagnttasat lnvsavdpva aggtgsgggg pggsggvggg
      481 sggytyfttv tvetletqpg eealqprgte keppgpttdg vwgggrpgda agpassstta
      541 paprssrpte kaftvpitdv tenalkdldd vmkttkiiig cfvaitfmaa vmlvafyklr
      601 kqhqlhkhhg ptrtveiinv edelpaasav svaaaaavas gggvggdshl alpalerdhl
      661 nhhhyvaaaf kahyssnpsg ggcggkgppg lnsihepllf ksgskenvqe tqi
//
LOCUS       NP_001354573             762 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform o [Homo sapiens].
ACCESSION   NP_001354573
VERSION     NP_001354573.1
DBSOURCE    REFSEQ: accession NM_001367644.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 762)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 762)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 762)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 762)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 762)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 762)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 762)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 762)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 762)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 762)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.76896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..762
                     /product="SUN domain-containing protein 1 isoform o"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=84335
     Region          12..269
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <342..>566
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          394..447
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(394,397..398,401,404..405,408..409,411..412,
                     415..416,418..419,422..423,425..426,429,432..433,436,
                     439..440,443..444,446..447)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          524..582
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          625..760
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..762
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367644.1:105..2393"
                     /note="isoform o is encoded by transcript variant 15"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv
      181 revlredghl svngealcyf llqilrriga vgqavsrtaw salwlavvap gkaasgvfww
      241 lgigwyqfvt liswlnvfll trclrnickf lvlliplfll lglslrgqgn ffsflpvlnw
      301 asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl
      361 relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev rmshledilg
      421 klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd
      481 avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt
      541 hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg
      601 silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls
      661 mmihpaaftl ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm
      721 fqalkrpddt afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_036526                154 aa            linear   PRI 20-NOV-2025
DEFINITION  prefoldin subunit 2 [Homo sapiens].
ACCESSION   NP_036526
VERSION     NP_036526.2
DBSOURCE    REFSEQ: accession NM_012394.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Cowan,N.J. and Lewis,S.A.
  TITLE     A chaperone with a hydrophilic surface
  JOURNAL   Nat Struct Biol 6 (11), 990-991 (1999)
   PUBMED   10542082
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Hansen,W.J., Cowan,N.J. and Welch,W.J.
  TITLE     Prefoldin-nascent chain complexes in the folding of cytoskeletal
            proteins
  JOURNAL   J Cell Biol 145 (2), 265-277 (1999)
   PUBMED   10209023
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Eddleston,J., Murdoch,J.N., Copp,A.J. and Stanier,P.
  TITLE     Physical and transcriptional map of a 3-Mb region of mouse
            chromosome 1 containing the gene for the neural tube defect mutant
            loop-tail (Lp)
  JOURNAL   Genomics 56 (2), 149-159 (1999)
   PUBMED   10051400
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012464.1 and AF165883.1.
            
            On Jan 24, 2001 this sequence version replaced NP_036526.1.
            
            Summary: This gene encodes a member of the prefoldin beta subunit
            family. The encoded protein is one of six subunits of prefoldin, a
            molecular chaperone complex that binds and stabilizes newly
            synthesized polypeptides, thereby allowing them to fold correctly.
            The complex, consisting of two alpha and four beta subunits, forms
            a double beta barrel assembly with six protruding coiled-coils.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ646466.1, BM719541.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368010.4/ ENSP00000356989.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..154
                     /product="prefoldin subunit 2"
                     /note="prefoldin 2"
                     /calculated_mol_wt=16517
     Region          25..124
                     /region_name="Prefoldin_2"
                     /note="prefoldin subunit 2; cd23163"
                     /db_xref="CDD:467479"
     Region          25..64
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467479"
     Site            order(26,30,33..34,37..38,40..41,44..45,48,102,105,109,
                     113,116..117,120..121,124)
                     /site_type="other"
                     /note="prefoldin beta subunit /TRiC interface [polypeptide
                     binding]"
                     /db_xref="CDD:467479"
     Site            order(57,60,64..65,68..74,76..81,85..86,90)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467479"
     Region          84..124
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467479"
     Region          124..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHV9.1)"
     CDS             1..154
                     /gene="PFDN2"
                     /gene_synonym="PFD2"
                     /coded_by="NM_012394.4:12..476"
                     /db_xref="CCDS:CCDS1217.1"
                     /db_xref="GeneID:5202"
                     /db_xref="HGNC:HGNC:8867"
                     /db_xref="MIM:613466"
ORIGIN      
        1 maensgragk ssgsgagkga vsaeqviagf nrlrqeqrgl askaaeleme lnehslvidt
       61 lkevdetrkc yrmvggvlve rtvkevlpal ennkeqiqki ietltqqlqa kgkelnefre
      121 khnirlmged ekpaakense gagakassag vlvs
//
LOCUS       NP_004513                957 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin heavy chain isoform 5C [Homo sapiens].
ACCESSION   NP_004513 XP_943222 XP_948647
VERSION     NP_004513.1
DBSOURCE    REFSEQ: accession NM_004522.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 957)
  AUTHORS   Tong,D. and Fan,L.
  TITLE     LncRNA ZNF667-AS1 Targets miR-523-3p/KIF5C Axis to Hinder Colon
            Cancer Progression
  JOURNAL   Mol Biotechnol 66 (6), 1464-1476 (2024)
   PUBMED   37322260
  REMARK    GeneRIF: LncRNA ZNF667-AS1 Targets miR-523-3p/KIF5C Axis to Hinder
            Colon Cancer Progression.
REFERENCE   2  (residues 1 to 957)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 957)
  AUTHORS   Naim,A., Accogli,A., Amadori,E., D'Onofrio,G., Madia,F.,
            Tortora,D., Zara,F., Striano,P., Salpietro,V. and Severino,M.
  TITLE     Abnormal course of the corticospinal tracts in KIF5C-related
            encephalopathy
  JOURNAL   Eur J Med Genet 65 (11), 104622 (2022)
   PUBMED   36122673
  REMARK    GeneRIF: Abnormal course of the corticospinal tracts in
            KIF5C-related encephalopathy.
REFERENCE   4  (residues 1 to 957)
  AUTHORS   Li,W., Cheng,T., Dong,X., Chen,H., Yang,L., Qiu,Z. and Zhou,W.
  TITLE     KIF5C deficiency causes abnormal cortical neuronal migration,
            dendritic branching, and spine morphology in mice
  JOURNAL   Pediatr Res 92 (4), 995-1002 (2022)
   PUBMED   34966180
  REMARK    GeneRIF: KIF5C deficiency causes abnormal cortical neuronal
            migration, dendritic branching, and spine morphology in mice.
REFERENCE   5  (residues 1 to 957)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 957)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
REFERENCE   7  (residues 1 to 957)
  AUTHORS   Kanai,Y., Okada,Y., Tanaka,Y., Harada,A., Terada,S. and Hirokawa,N.
  TITLE     KIF5C, a novel neuronal kinesin enriched in motor neurons
  JOURNAL   J Neurosci 20 (17), 6374-6384 (2000)
   PUBMED   10964943
REFERENCE   8  (residues 1 to 957)
  AUTHORS   Xia,Ch., Rahman,A., Yang,Z. and Goldstein,L.S.
  TITLE     Chromosomal localization reveals three kinesin heavy chain genes in
            mouse
  JOURNAL   Genomics 52 (2), 209-213 (1998)
   PUBMED   9782088
REFERENCE   9  (residues 1 to 957)
  AUTHORS   Engelender,S., Sharp,A.H., Colomer,V., Tokito,M.K., Lanahan,A.,
            Worley,P., Holzbaur,E.L. and Ross,C.A.
  TITLE     Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued
            subunit of dynactin
  JOURNAL   Hum Mol Genet 6 (13), 2205-2212 (1997)
   PUBMED   9361024
REFERENCE   10 (residues 1 to 957)
  AUTHORS   Niclas,J., Navone,F., Hom-Booher,N. and Vale,R.D.
  TITLE     Cloning and localization of a conventional kinesin motor expressed
            exclusively in neurons
  JOURNAL   Neuron 12 (5), 1059-1072 (1994)
   PUBMED   7514426
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AW162840.1, AB011103.1,
            DA085551.1 and AB209191.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Oct 22, 2006 this sequence version replaced
            XP_948647.2, XP_943222.1.
            
            Summary: The protein encoded by this gene is a kinesin heavy chain
            subunit involved in the transport of cargo within the central
            nervous system. The encoded protein, which acts as a tetramer by
            associating with another heavy chain and two light chains,
            interacts with protein kinase CK2. Mutations in this gene have been
            associated with complex cortical dysplasia with other brain
            malformations-2. Two transcript variants, one protein-coding and
            the other non-protein coding, have been found for this gene.
            [provided by RefSeq, Jul 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011103.1, SRR1803612.248336.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000435030.6/ ENSP00000393379.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..957
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q23.1-q23.2"
     Protein         1..957
                     /product="kinesin heavy chain isoform 5C"
                     /note="kinesin heavy chain neuron-specific 2;
                     neuron-specific kinesin heavy chain 2; kinesin-1"
                     /calculated_mol_wt=109364
     Region          6..327
                     /region_name="KISc_KHC_KIF5"
                     /note="Kinesin motor domain, kinesin heavy chain (KHC) or
                     KIF5-like subgroup; cd01369"
                     /db_xref="CDD:276820"
     Site            order(16,86,89,91..94,232)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276820"
     Site            order(157..159,162,276,280..281)
                     /site_type="other"
                     /note="beta tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Site            order(158..160,162,238..240,249,253,257,276,281)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276820"
     Region          174..315
                     /region_name="Microtubule-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O60282.1)"
     Site            order(236,238..239,253,256..257,260)
                     /site_type="other"
                     /note="alpha tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Region          <412..907
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          836..905
                     /region_name="Khc_CBD_cc"
                     /note="cargo binding coiled-coil domain found in kinesin
                     heavy chains; cd23649"
                     /db_xref="CDD:467880"
     Region          859..956
                     /region_name="Globular"
                     /note="propagated from UniProtKB/Swiss-Prot (O60282.1)"
     Region          911..957
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60282.1)"
     CDS             1..957
                     /gene="KIF5C"
                     /gene_synonym="CDCBM2; KINN; NKHC; NKHC-2; NKHC2"
                     /coded_by="NM_004522.3:392..3265"
                     /db_xref="CCDS:CCDS74586.1"
                     /db_xref="GeneID:3800"
                     /db_xref="HGNC:HGNC:6325"
                     /db_xref="MIM:604593"
ORIGIN      
        1 madpaecsik vmcrfrplne aeilrgdkfi pkfkgdetvv igqgkpyvfd rvlppnttqe
       61 qvynacakqi vkdvlegyng tifaygqtss gkthtmegkl hdpqlmgiip riahdifdhi
      121 ysmdenlefh ikvsyfeiyl dkirdlldvs ktnlavhedk nrvpyvkgct erfvsspeev
      181 mdvidegkan rhvavtnmne hssrshsifl inikqenvet ekklsgklyl vdlagsekvs
      241 ktgaegavld eakninksls algnvisala egtkthvpyr dskmtrilqd slggncrtti
      301 viccspsvfn eaetkstlmf gqraktiknt vsvnleltae ewkkkyekek eknktlknvi
      361 qhlemelnrw rngeavpede qisakdqknl epcdntpiid niapvvagis teekekydee
      421 isslyrqldd kddeinqqsq laeklkqqml dqdellastr rdyekiqeel trlqieneaa
      481 kdevkevlqa leelavnydq ksqevedktr aneqltdela qktttltttq relsqlqels
      541 nhqkkratei lnlllkdlge iggiigtndv ktladvngvi eeeftmarly iskmksevks
      601 lvnrskqles aqmdsnrkmn aserelaacq llisqheaki ksltdymqnm eqkrrqlees
      661 qdslseelak lraqekmhev sfqdkekehl trlqdaeemk kaleqqmesh reahqkqlsr
      721 lrdeieekqk iideirdlnq klqleqekls sdynklkied qeremklekl lllndkreqa
      781 redlkgleet vsrelqtlhn lrklfvqdlt trvkksveld nddgggsaaq kqkisflenn
      841 leqltkvhkq lvrdnadlrc elpklekrlr ataervkale salkeakena mrdrkryqqe
      901 vdrikeavra knmarrahsa qiakpirpgh ypassptavh airggggsss nsthyqk
//
LOCUS       NP_001269883             531 aa            linear   PRI 20-NOV-2025
DEFINITION  protein arginine N-methyltransferase 5 isoform d [Homo sapiens].
ACCESSION   NP_001269883
VERSION     NP_001269883.1
DBSOURCE    REFSEQ: accession NM_001282954.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Kurdi,M., Alkhotani,A., Sabbagh,A., Faizo,E., Lary,A.I.,
            Bamaga,A.K., Almansouri,M., Hafiz,B., Alsharif,T. and Baeesa,S.
  TITLE     The interplay mechanism between IDH mutation, MGMT-promoter
            methylation, and PRMT5 activity in the progression of grade 4
            astrocytoma: unraveling the complex triad theory
  JOURNAL   Oncol Res 32 (6), 1037-1045 (2024)
   PUBMED   38827324
  REMARK    GeneRIF: The interplay mechanism between IDH mutation,
            MGMT-promoter methylation, and PRMT5 activity in the progression of
            grade 4 astrocytoma: unraveling the complex triad theory.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Abe,Y., Sano,T., Otsuka,N., Ogawa,M. and Tanaka,N.
  TITLE     PRMT5-mediated methylation of STAT3 is required for lung cancer
            stem cell maintenance and tumour growth
  JOURNAL   Commun Biol 7 (1), 593 (2024)
   PUBMED   38760429
  REMARK    GeneRIF: PRMT5-mediated methylation of STAT3 is required for lung
            cancer stem cell maintenance and tumour growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Zhang,X., Liu,Q., Wang,L. and Peng,Q.
  TITLE     Identification of protein methyltransferases 5 associated with
            ferroptosis and immune cell infiltration of head and neck squamous
            cell carcinoma
  JOURNAL   Aging (Albany NY) 16 (8), 7426-7436 (2024)
   PUBMED   38663941
  REMARK    GeneRIF: Identification of protein methyltransferases 5 associated
            with ferroptosis and immune cell infiltration of head and neck
            squamous cell carcinoma.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Liu,Y., Jiang,H., Hu,K., Zou,H., Zhang,W., Liu,J. and Jian,X.
  TITLE     CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP
            to regulate the translation and stability of CDK6 mRNA
  JOURNAL   PLoS One 19 (4), e0298947 (2024)
   PUBMED   38626179
  REMARK    GeneRIF: CircPRMT5 promotes progression of osteosarcoma by
            recruiting CNBP to regulate the translation and stability of CDK6
            mRNA.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Rho,J., Choi,S., Seong,Y.R., Cho,W.K., Kim,S.H. and Im,D.S.
  TITLE     Prmt5, which forms distinct homo-oligomers, is a member of the
            protein-arginine methyltransferase family
  JOURNAL   J Biol Chem 276 (14), 11393-11401 (2001)
   PUBMED   11152681
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Schwarzler,A., Kreienkamp,H.J. and Richter,D.
  TITLE     Interaction of the somatostatin receptor subtype 1 with the human
            homolog of the Shk1 kinase-binding protein from yeast
  JOURNAL   J Biol Chem 275 (13), 9557-9562 (2000)
   PUBMED   10734105
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Pollack,B.P., Kotenko,S.V., He,W., Izotova,L.S., Barnoski,B.L. and
            Pestka,S.
  TITLE     The human homologue of the yeast proteins Skb1 and Hsl7p interacts
            with Jak kinases and contains protein methyltransferase activity
  JOURNAL   J Biol Chem 274 (44), 31531-31542 (1999)
   PUBMED   10531356
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Gilbreth,M., Yang,P., Bartholomeusz,G., Pimental,R.A., Kansra,S.,
            Gadiraju,R. and Marcus,S.
  TITLE     Negative regulation of mitosis in fission yeast by the shk1
            interacting protein skb1 and its human homolog, Skb1Hs
  JOURNAL   Proc Natl Acad Sci U S A 95 (25), 14781-14786 (1998)
   PUBMED   9843966
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Krapivinsky,G., Pu,W., Wickman,K., Krapivinsky,L. and Clapham,D.E.
  TITLE     pICln binds to a mammalian homolog of a yeast protein involved in
            regulation of cell morphology
  JOURNAL   J Biol Chem 273 (18), 10811-10814 (1998)
   PUBMED   9556550
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC395183.1, AK300863.1 and
            AL833612.1.
            
            Summary: This gene encodes an enzyme that belongs to the
            methyltransferase family. The encoded protein catalyzes the
            transfer of methyl groups to the amino acid arginine, in target
            proteins that include histones, transcriptional elongation factors
            and the tumor suppressor p53. This gene plays a role in several
            cellular processes, including transcriptional regulation, and the
            assembly of small nuclear ribonucleoproteins. A pseudogene of this
            gene has been defined on chromosome 4. Alternative splicing results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (4) contains multiple differences
            in the 5' coding region, compared to variant 1, including
            initiation of translation at a downstream in-frame start codon. The
            encoded isoform (d) has a shorter N-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2666502.1, AK300863.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..531
                     /product="protein arginine N-methyltransferase 5 isoform
                     d"
                     /EC_number="2.1.1.320"
                     /note="protein arginine N-methyltransferase 5; HMT1 hnRNP
                     methyltransferase-like 5; jak-binding protein 1; 72 kDa
                     ICln-binding protein; shk1 kinase-binding protein 1
                     homolog; histone-arginine N-methyltransferase PRMT5; SKB1
                     homolog"
                     /calculated_mol_wt=60977
     Region          <1..184
                     /region_name="PRMT5_TIM"
                     /note="PRMT5 TIM barrel domain; pfam17285"
                     /db_xref="CDD:435840"
     Region          189..358
                     /region_name="PRMT5"
                     /note="PRMT5 arginine-N-methyltransferase; pfam05185"
                     /db_xref="CDD:428356"
     Region          362..529
                     /region_name="PRMT5_C"
                     /note="PRMT5 oligomerization domain; pfam17286"
                     /db_xref="CDD:435841"
     CDS             1..531
                     /gene="PRMT5"
                     /gene_synonym="HRMT1L5; HSL7; IBP72; JBP1; SKB1; SKB1Hs"
                     /coded_by="NM_001282954.2:300..1895"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:10419"
                     /db_xref="HGNC:HGNC:10894"
                     /db_xref="MIM:604045"
ORIGIN      
        1 mlqelnfgay lglpafllpl nqedntnlar vltnhihtgh hssmfwmrvp lvapedlrdd
       61 iienapttht eeysgeektw mwwhnfrtlc dyskriaval eigadlpsnh vidrwlgepi
      121 kaailptsif ltnkkgfpvl skmhqrlifr llklevqfii tgtnhhseke fcsylqyley
      181 lsqnrpppna yelfakgyed ylqsplqplm dnlesqtyev fekdpikysq yqqaiykcll
      241 drvpeeekdt nvqvlmvlga grgplvnasl raakqadrri klyaveknpn avvtlenwqf
      301 eewgsqvtvv ssdmrewvap ekadiivsel lgsfadnels pecldgaqhf lkddgvsipg
      361 eytsflapis ssklynevra crekdrdpea qfempyvvrl hnfhqlsapq pcftfshpnr
      421 dpmidnnryc tlefpvevnt vlhgfagyfe tvlyqditls irpethspgm fswfpilfpi
      481 kqpitvregq ticvrfwrcs nskkvwyewa vtapvcsaih nptgrsytig l
//
LOCUS       NP_060216                929 aa            linear   PRI 20-NOV-2025
DEFINITION  testis-expressed protein 10 isoform 1 [Homo sapiens].
ACCESSION   NP_060216
VERSION     NP_060216.2
DBSOURCE    REFSEQ: accession NM_017746.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Gordon,J., Chapus,F.L., Viverette,E.G., Williams,J.G.,
            Deterding,L.J., Krahn,J.M., Borgnia,M.J., Rodriguez,J., Warren,A.J.
            and Stanley,R.E.
  TITLE     Cryo-EM reveals the architecture of the PELP1-WDR18 molecular
            scaffold
  JOURNAL   Nat Commun 13 (1), 6783 (2022)
   PUBMED   36351913
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Zhou,H., Stein,C.B., Shafiq,T.A., Shipkovenska,G., Kalocsay,M.,
            Paulo,J.A., Zhang,J., Luo,Z., Gygi,S.P., Adelman,K. and Moazed,D.
  TITLE     Rixosomal RNA degradation contributes to silencing of Polycomb
            target genes
  JOURNAL   Nature 604 (7904), 167-174 (2022)
   PUBMED   35355014
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Liang,J.H., Xu,Q.D. and Gu,S.G.
  TITLE     LncRNA RSU1P2-microRNA let-7a-Testis-Expressed Protein 10 axis
            modulates tumorigenesis and cancer stem cell-like properties in
            liver cancer
  JOURNAL   Bioengineered 13 (2), 4285-4300 (2022)
   PUBMED   35156514
  REMARK    GeneRIF: LncRNA RSU1P2-microRNA let-7a-Testis-Expressed Protein 10
            axis modulates tumorigenesis and cancer stem cell-like properties
            in liver cancer.
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Luo,S., Wang,W., Feng,J. and Li,R.
  TITLE     TEX10 Promotes the Tumorigenesis and Radiotherapy Resistance of
            Urinary Bladder Carcinoma by Stabilizing XRCC6
  JOURNAL   J Immunol Res 2021, 5975893 (2021)
   PUBMED   34966825
  REMARK    GeneRIF: TEX10 Promotes the Tumorigenesis and Radiotherapy
            Resistance of Urinary Bladder Carcinoma by Stabilizing XRCC6.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 929)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 929)
  AUTHORS   Ding,J., Huang,X., Shao,N., Zhou,H., Lee,D.F., Faiola,F.,
            Fidalgo,M., Guallar,D., Saunders,A., Shliaha,P.V., Wang,H.,
            Waghray,A., Papatsenko,D., Sanchez-Priego,C., Li,D., Yuan,Y.,
            Lemischka,I.R., Shen,L., Kelley,K., Deng,H., Shen,X. and Wang,J.
  TITLE     Tex10 Coordinates Epigenetic Control of Super-Enhancer Activity in
            Pluripotency and Reprogramming
  JOURNAL   Cell Stem Cell 16 (6), 653-668 (2015)
   PUBMED   25936917
  REMARK    GeneRIF: Tex10 is a core component of the pluripotency network.
REFERENCE   7  (residues 1 to 929)
  AUTHORS   Fanis,P., Gillemans,N., Aghajanirefah,A., Pourfarzad,F.,
            Demmers,J., Esteghamat,F., Vadlamudi,R.K., Grosveld,F.,
            Philipsen,S. and van Dijk,T.B.
  TITLE     Five friends of methylated chromatin target of
            protein-arginine-methyltransferase[prmt]-1 (chtop), a complex
            linking arginine methylation to desumoylation
  JOURNAL   Mol Cell Proteomics 11 (11), 1263-1273 (2012)
   PUBMED   22872859
  REMARK    GeneRIF: Recruitment of the protein complex 5FMC to Zbp-89, a
            zinc-finger transcription factor, affects its sumoylation status
            and transactivation potential.[5FMC]
REFERENCE   8  (residues 1 to 929)
  AUTHORS   Yoshitake,H., Yokoi,H., Ishikawa,H., Maruyama,M., Endo,S.,
            Nojima,M., Yoshida,K., Yoshikawa,H., Suzuki,F., Takamori,K.,
            Fujiwara,H. and Araki,Y.
  TITLE     Overexpression of TEX101, a potential novel cancer marker, in head
            and neck squamous cell carcinoma
  JOURNAL   Cancer Biomark 12 (3), 141-148 (2012)
   PUBMED   23481573
  REMARK    GeneRIF: Data suggest that TEX101 is a cancer-related protein and
            may be useful as a marker for prognosis/diagnosis of and neck
            squamous cell carcinomas (HNSCC).
REFERENCE   9  (residues 1 to 929)
  AUTHORS   Finkbeiner,E., Haindl,M. and Muller,S.
  TITLE     The SUMO system controls nucleolar partitioning of a novel
            mammalian ribosome biogenesis complex
  JOURNAL   EMBO J 30 (6), 1067-1078 (2011)
   PUBMED   21326211
  REMARK    GeneRIF: These data define the PELP1-TEX10-WDR18 complex as a
            regulator of ribosome biogenesis and suggests that its
            SUMO-controlled distribution coordinates the rate of ribosome
            formation.
REFERENCE   10 (residues 1 to 929)
  AUTHORS   Dou,Y., Milne,T.A., Tackett,A.J., Smith,E.R., Fukuda,A.,
            Wysocka,J., Allis,C.D., Chait,B.T., Hess,J.L. and Roeder,R.G.
  TITLE     Physical association and coordinate function of the H3 K4
            methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
  JOURNAL   Cell 121 (6), 873-885 (2005)
   PUBMED   15960975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP336313.1, BC030652.2, AB060968.1 and AA436854.1.
            
            On Jun 11, 2009 this sequence version replaced NP_060216.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB060968.1, BC030652.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374902.9/ ENSP00000364037.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..929
                     /product="testis-expressed protein 10 isoform 1"
                     /note="testis expressed gene 10; testis-expressed sequence
                     10 protein; testis-expressed protein 10"
                     /calculated_mol_wt=105543
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXF1.2)"
     Region          99..137
                     /region_name="HEAT"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXF1.2)"
     Region          132..235
                     /region_name="Ipi1_N"
                     /note="Rix1 complex component involved in 60S ribosome
                     maturation; pfam12333"
                     /db_xref="CDD:463535"
     CDS             1..929
                     /gene="TEX10"
                     /gene_synonym="bA208F1.2; Ipi1"
                     /coded_by="NM_017746.4:181..2970"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6748.1"
                     /db_xref="GeneID:54881"
                     /db_xref="HGNC:HGNC:25988"
                     /db_xref="MIM:616717"
ORIGIN      
        1 mtkkrkrqhd fqkvklkvgk kkpklqnatp tnfktktihl peqlkedgtl ptnnrklnik
       61 dllsqmhhyn agvkqsallg lkdllsqypf iidahlsnil sevtavftdk danvrlaavq
      121 llqflapkir aeqispffpl vsahlssamt hitegiqeds lkvldilleq ypalitgrss
      181 illknfveli shqqlskgli nrdrsqswil svnpnrrlts qqwrlkvlvr lskflqalad
      241 gssrlreseg lqeqkenpha tsnsifinwk ehandqqhiq vyenggsqpn vssqfrlryl
      301 vgglsgvdeg lsstenlkgf ieiiipllie cwveavppql atpvgngier eplqvmqqvl
      361 niisllwkls kqqdethkle swlrknylid fkhhfmsrfp yvlkeitkhk rkepnksikh
      421 ctvlsnnidh lllnltlsdi mvslanastl qkdcswiemi rkfvtetled gsrlnskqln
      481 rllgvswrlm qiqpnredte tlikavytly qqrglilpvr tlllkffski yqteelrscr
      541 fryrskvlsr wlaglplqla hlgsrnpels tqlidiihta aarankellk slqatalriy
      601 dpqegavvvl padsqqrlvq lvyflpslpa dllsrlsrcc imgrlsssla amligilhmr
      661 ssfsgwkysa kdwlmsdvdy fsflfstltg fskeeltwlq slrgvphviq tqlspvllyl
      721 tdldqflhhw dvteavfhsl lviparsqnf dilqsaiskh lvgltvipds tagcvfgvic
      781 klldhtcvvs etllpflasc cysllyfllt iekgeaehlr krdklwgvcv silallprvl
      841 rlmlqslrvn rvgpeelpvv gqllrlllqh aplrthmltn ailvqqiikn ittlksgsvq
      901 eqwltdlhyc fnvyitghpq gpsalatvy
//
LOCUS       NP_001002879             683 aa            linear   PRI 20-NOV-2025
DEFINITION  THO complex subunit 5 [Homo sapiens].
ACCESSION   NP_001002879
VERSION     NP_001002879.1
DBSOURCE    REFSEQ: accession NM_001002879.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Pacheco-Fiallos,B., Vorlander,M.K., Riabov-Bassat,D., Fin,L.,
            O'Reilly,F.J., Ayala,F.I., Schellhaas,U., Rappsilber,J. and
            Plaschka,C.
  TITLE     mRNA recognition and packaging by the human transcription-export
            complex
  JOURNAL   Nature 616 (7958), 828-835 (2023)
   PUBMED   37020021
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Mun,S.H., Oh,B., Lee,M.J., Bae,S., Yang,Y. and Park-Min,K.H.
  TITLE     THOC5 regulates human osteoclastogenesis
  JOURNAL   Eur J Cell Biol 101 (3), 151248 (2022)
   PUBMED   35688054
  REMARK    GeneRIF: THOC5 regulates human osteoclastogenesis.
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Alqassim,E.Y., Sharma,S., Khan,A.N.M.N.H., Emmons,T.R., Cortes
            Gomez,E., Alahmari,A., Singel,K.L., Mark,J., Davidson,B.A., Robert
            McGray,A.J., Liu,Q., Lichty,B.D., Moysich,K.B., Wang,J., Odunsi,K.,
            Segal,B.H. and Baysal,B.E.
  TITLE     RNA editing enzyme APOBEC3A promotes pro-inflammatory M1 macrophage
            polarization
  JOURNAL   Commun Biol 4 (1), 102 (2021)
   PUBMED   33483601
  REMARK    GeneRIF: RNA editing enzyme APOBEC3A promotes pro-inflammatory M1
            macrophage polarization.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 683)
  AUTHORS   Mancini,A., Koch,A., Whetton,A.D. and Tamura,T.
  TITLE     The M-CSF receptor substrate and interacting protein FMIP is
            governed in its subcellular localization by protein kinase
            C-mediated phosphorylation, and thereby potentiates M-CSF-mediated
            differentiation
  JOURNAL   Oncogene 23 (39), 6581-6589 (2004)
   PUBMED   15221008
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Strasser,K., Masuda,S., Mason,P., Pfannstiel,J., Oppizzi,M.,
            Rodriguez-Navarro,S., Rondon,A.G., Aguilera,A., Struhl,K., Reed,R.
            and Hurt,E.
  TITLE     TREX is a conserved complex coupling transcription with messenger
            RNA export
  JOURNAL   Nature 417 (6886), 304-308 (2002)
   PUBMED   11979277
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Tamura,T., Mancini,A., Joos,H., Koch,A., Hakim,C., Dumanski,J.,
            Weidner,K.M. and Niemann,H.
  TITLE     FMIP, a novel Fms-interacting protein, affects
            granulocyte/macrophage differentiation
  JOURNAL   Oncogene 18 (47), 6488-6495 (1999)
   PUBMED   10597251
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Xie,Y.G., Han,F.Y., Peyrard,M., Ruttledge,M.H., Fransson,I.,
            DeJong,P., Collins,J., Dunham,I., Nordenskjold,M. and Dumanski,J.P.
  TITLE     Cloning of a novel, anonymous gene from a megabase-range YAC and
            cosmid contig in the neurofibromatosis type 2/meningioma region on
            human chromosome 22q12
  JOURNAL   Hum Mol Genet 2 (9), 1361-1368 (1993)
   PUBMED   8242058
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU187531.1, BX404329.2, CR456542.1, BX400943.2, AB023200.1 and
            BQ184247.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All four variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB023200.1, SRR1803612.129529.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..683
                     /product="THO complex subunit 5"
                     /note="functional spliceosome-associated protein 79;
                     NF2/meningioma region protein pK1.3; placental protein
                     39.2; THO complex 5; THO complex subunit 5 homolog;
                     Fms-interacting protein; PP39.2; hTREX90"
                     /calculated_mol_wt=78377
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          2..199
                     /region_name="Interaction with THOC7.
                     /evidence=ECO:0000269|PubMed:19059247"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          2..144
                     /region_name="Interaction with CSF1R.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BKT7; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Region          7..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          103..452
                     /region_name="FmiP_Thoc5"
                     /note="Fms-interacting protein/Thoc5; pfam09766"
                     /db_xref="CDD:462889"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:18373705,
                     ECO:0000269|PubMed:23032722; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Region          247..683
                     /region_name="Tandem RWD domains.
                     /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK, ECO:0007744|PDB:7ZNK,
                     ECO:0007744|PDB:7ZNL"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Region          301..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13769.2)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13769.2)"
     CDS             1..683
                     /gene="THOC5"
                     /gene_synonym="C22orf19; Fmip; fSAP79; PK1.3"
                     /coded_by="NM_001002879.1:220..2271"
                     /db_xref="CCDS:CCDS13859.1"
                     /db_xref="GeneID:8563"
                     /db_xref="HGNC:HGNC:19074"
                     /db_xref="MIM:612733"
ORIGIN      
        1 mssesskkrk pkvirsdgap aegkrnrsdt eqegkyysee aevdlrdpgr dyelykytcq
       61 elqrlmaeiq dlksrggkdv aieieerriq scvhfmtlkk lnrlahirlk kgrdqtheak
      121 qkvdayhlql qnllyevmhl qkeitkclef kskheeidlv sleefykeap pdiskaevtm
      181 gdphqqtlar ldweleqrkr laekyrecls nkekilkeie vkkeylsslq prlnsimqas
      241 lpvqeylfmp fdqahkqyet arhlppplyv lfvqataygq acdktlsvai egsvdeakal
      301 fkppedsqdd esdsdaeeeq ttkrrrptlg vqlddkrkem lkrhplsvml dlkckddsvl
      361 hltfyylmnl nimtvkakvt tamelitpis agdllspdsv lsclypgdhg kktpnpanqy
      421 qfdkvgiltl sdyvlelghp ylwvqklggl hfpkeqpqqt viadhslsas hmettmkllk
      481 trvqsrlalh kqfaslehgi vpvtsdcqyl fpakvvsrlv kwvtvahedy melhftkdiv
      541 daglagdtnl yymaliergt aklqaavvln pgyssippvf qlclnwkgek tnsnddnira
      601 megevnvcyk elcgpwpshq lltnqlqrlc vlldvylete shddsvegpk efpqekmclr
      661 lfrgpsrmkp fkynhpqgff shr
//
LOCUS       NP_001305075             500 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-33 isoform 2 [Homo sapiens].
ACCESSION   NP_001305075
VERSION     NP_001305075.1
DBSOURCE    REFSEQ: accession NM_001318146.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Takada-Takatori,Y.
  TITLE     [Donepezil Reduces Amyloid Precursor Protein Endocytosis by
            Resulting from Increase in the Expression of Sorting Nexin Protein
            33]
  JOURNAL   Yakugaku Zasshi 141 (6), 851-856 (2021)
   PUBMED   34078793
  REMARK    GeneRIF: [Donepezil Reduces Amyloid Precursor Protein Endocytosis
            by Resulting from Increase in the Expression of Sorting Nexin
            Protein 33].
            Review article
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Zhang,J., Zhang,X., Guo,Y., Xu,L. and Pei,D.
  TITLE     Sorting nexin 33 induces mammalian cell micronucleated phenotype
            and actin polymerization by interacting with Wiskott-Aldrich
            syndrome protein
  JOURNAL   J Biol Chem 284 (32), 21659-21669 (2009)
   PUBMED   19487689
  REMARK    GeneRIF: SNX33 plays a role in maintaining cell shape and cell
            cycle progression through its interaction with WASp
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Heiseke,A., Schobel,S., Lichtenthaler,S.F., Vorberg,I.,
            Groschup,M.H., Kretzschmar,H., Schatzl,H.M. and Nunziante,M.
  TITLE     The novel sorting nexin SNX33 interferes with cellular PrP
            formation by modulation of PrP shedding
  JOURNAL   Traffic 9 (7), 1116-1129 (2008)
   PUBMED   18419754
  REMARK    GeneRIF: SNX33 interferes with cellular PrP formation by modulation
            of PrP shedding
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Schobel,S., Neumann,S., Hertweck,M., Dislich,B., Kuhn,P.H.,
            Kremmer,E., Seed,B., Baumeister,R., Haass,C. and Lichtenthaler,S.F.
  TITLE     A novel sorting nexin modulates endocytic trafficking and
            alpha-secretase cleavage of the amyloid precursor protein
  JOURNAL   J Biol Chem 283 (21), 14257-14268 (2008)
   PUBMED   18353773
  REMARK    GeneRIF: identifies SNX33 as a new endocytic protein, which
            modulates amyloid precursor protein endocytosis and APP
            alpha-secretase cleavage, and demonstrates that the rate of APP
            endocytosis is a major control factor for APP alpha-secretase
            cleavage
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Seet,L.F. and Hong,W.
  TITLE     The Phox (PX) domain proteins and membrane traffic
  JOURNAL   Biochim Biophys Acta 1761 (8), 878-896 (2006)
   PUBMED   16782399
  REMARK    Review article
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Karkkainen,S., Hiipakka,M., Wang,J.H., Kleino,I., Vaha-Jaakkola,M.,
            Renkema,G.H., Liss,M., Wagner,R. and Saksela,K.
  TITLE     Identification of preferred protein interactions by phage-display
            of the human Src homology-3 proteome
  JOURNAL   EMBO Rep 7 (2), 186-191 (2006)
   PUBMED   16374509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC018775.1 and AK091291.1.
            
            Summary: The protein encoded by this gene is involved in
            cytoskeletal reorganization, vesicle trafficking, endocytosis, and
            mitosis. The encoded protein is essential for the creation of the
            cleavage furrow during mitosis and for completion of mitosis. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment compared to variant 1. The resulting isoform (2) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091291.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..500
                     /product="sorting nexin-33 isoform 2"
                     /note="SH3 and PX domain containing 3; SH3 and PX
                     domain-containing protein 3"
                     /calculated_mol_wt=56767
     Region          4..58
                     /region_name="SH3_SNX33"
                     /note="Src Homology 3 domain of Sorting Nexin 33; cd11896"
                     /db_xref="CDD:212829"
     Site            order(9,11,14,18,37..38,52,54..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212829"
     Region          68..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV41.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WV41.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WV41.1)"
     Region          230..354
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(266..268,292..293,306)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132819"
     Region          365..497
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     CDS             1..500
                     /gene="SNX33"
                     /gene_synonym="SH3PX3; SH3PXD3C; SNX30"
                     /coded_by="NM_001318146.1:97..1599"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:257364"
                     /db_xref="HGNC:HGNC:28468"
                     /db_xref="MIM:619107"
ORIGIN      
        1 malkgralyd fhsenkeeis iqqdedlvif setsldgwlq gqnsrgetgl fpasyveivr
       61 sgistnhady ssspagspga qvslynspsv asparsgggs gflsnqgsfe edddddwddw
      121 ddgctvveep ragglgtngh pplnlsypga ypsqhmafrp kpplerqdsl asakrgsvvg
      181 rnlnrfscfv rsgveafilg dvpmmakiae tysiemgprg pqwkanphpf acsvedptkq
      241 tkfkgiksyi sykltpthaa spvyrrykhf dwlynrllhk ftvisvphlp ekqatgrfee
      301 dfiekrkrrl ilwmdhmtsh pvlsqyegfq hflsclddkq wkmgkrraek demvgasfll
      361 tfqiptehqd lqdvedrvdt fkafskkmdd svlqlstvas elgllsnfpd iihlqkgafa
      421 kvkesqrmsd egrmvqdead girrrcrvvg falqaemnhf hqrreldfkh mmqnylrqqi
      481 lfyqrvgqql ektlrmydnl
//
LOCUS       NP_001274064             469 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 14 isoform a [Homo sapiens].
ACCESSION   NP_001274064 XP_005250491
VERSION     NP_001274064.1
DBSOURCE    REFSEQ: accession NM_001287135.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 469)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 469)
  AUTHORS   Zhao,Y., Chen,L., Xiang,Q., Lin,J., Jiang,S. and Li,W.
  TITLE     N6-methyladenosine-modified circCDK14 promotes ossification of the
            ligamentum flavum via epigenetic modulation by targeting AFF4
  JOURNAL   Cell Mol Life Sci 81 (1), 436 (2024)
   PUBMED   39414635
  REMARK    GeneRIF: N6-methyladenosine-modified circCDK14 promotes
            ossification of the ligamentum flavum via epigenetic modulation by
            targeting AFF4.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 469)
  AUTHORS   Parmasad,J.A., Ricke,K.M., Nguyen,B., Stykel,M.G., Buchner-Duby,B.,
            Bruce,A., Geertsma,H.M., Lian,E., Lengacher,N.A., Callaghan,S.M.,
            Joselin,A., Tomlinson,J.J., Schlossmacher,M.G., Stanford,W.L.,
            Ma,J., Brundin,P., Ryan,S.D. and Rousseaux,M.W.C.
  TITLE     Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy
  JOURNAL   Cell Death Dis 15 (4), 246 (2024)
   PUBMED   38575601
  REMARK    GeneRIF: Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 469)
  AUTHORS   Zhang,M., Kan,D., Zhang,B., Chen,X., Wang,C., Chen,S., Gao,W.,
            Yang,Z., Li,Y., Chen,Y., Zhu,S., Wen,S., Niu,Y. and Shang,Z.
  TITLE     P300/SP1 complex mediating elevated METTL1 regulates CDK14 mRNA
            stability via internal m7G modification in CRPC
  JOURNAL   J Exp Clin Cancer Res 42 (1), 215 (2023)
   PUBMED   37599359
  REMARK    GeneRIF: P300/SP1 complex mediating elevated METTL1 regulates CDK14
            mRNA stability via internal m7G modification in CRPC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 469)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 469)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 469)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   8  (residues 1 to 469)
  AUTHORS   Yang,T., Gao,Y.K. and Chen,J.Y.
  TITLE     KIAA0202, a human septin family member, interacting with hPFTAIRE1
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (4),
            520-525 (2002)
   PUBMED   12098780
REFERENCE   9  (residues 1 to 469)
  AUTHORS   Yang,T. and Chen,J.Y.
  TITLE     Identification and cellular localization of human PFTAIRE1
  JOURNAL   Gene 267 (2), 165-172 (2001)
   PUBMED   11313143
REFERENCE   10 (residues 1 to 469)
  AUTHORS   Lazzaro,M.A., Albert,P.R. and Julien,J.P.
  TITLE     A novel cdc2-related protein kinase expressed in the nervous system
  JOURNAL   J Neurochem 69 (1), 348-364 (1997)
   PUBMED   9202329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC002456.2, HY179664.1, DC420282.1, AF119833.1, AK297974.1,
            BC136477.1, BP336072.1, DB476188.1, AB020641.1, BM740394.1 and
            BC152436.1.
            
            On Nov 27, 2013 this sequence version replaced XP_005250491.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.197386.1,
                                           SRR1660809.234153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380050.8/ ENSP00000369390.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..469
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.13"
     Protein         1..469
                     /product="cyclin-dependent kinase 14 isoform a"
                     /EC_number="2.7.11.22"
                     /note="PFTAIRE protein kinase 1; cell division protein
                     kinase 14; serine/threonine-protein kinase PFTAIRE-1"
                     /calculated_mol_wt=52926
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94921.3)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94921.3)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (O94921.3)"
     Region          103..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94921.3)"
     Region          129..431
                     /region_name="STKc_PFTAIRE1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     PFTAIRE-1 kinase; cd07869"
                     /db_xref="CDD:143374"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94921.3)"
     Site            order(141..144,149,162,164,180,194,210..213,216,218..219,
                     256,258,260..261,263,274,277,289,291..294,296,334..335)
                     /site_type="active"
                     /db_xref="CDD:143374"
     Site            order(141..144,149,162,164,194,210..213,216,219,260..261,
                     263,274)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:143374"
     Site            order(172..174,176,179..180,182..183,186..187,199,201,206,
                     245,248..251,279,281..284,288..289,405,409..411)
                     /site_type="other"
                     /note="putative CDK/cyclin interface [polypeptide
                     binding]"
                     /db_xref="CDD:143374"
     Site            order(180,218,256,258,277,289,291..294,296,334..335)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:143374"
     Site            273..296
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:143374"
     Region          449..469
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94921.3)"
     CDS             1..469
                     /gene="CDK14"
                     /gene_synonym="PFTAIRE1; PFTK1"
                     /coded_by="NM_001287135.2:308..1717"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75626.1"
                     /db_xref="GeneID:5218"
                     /db_xref="HGNC:HGNC:8883"
                     /db_xref="MIM:610679"
ORIGIN      
        1 mcdliepqpa ekigkmkklr rtlsesfsri alkkddttfd eicvtkmstr ncqgmdsvik
       61 pldtipedkk vrvqrtqstf dpfekpanqv krvhsennac infktsstgk espkvrrhss
      121 pssptspkfg kadsyeklek lgegsyatvy kgkskvngkl valkvirlqe eegtpftair
      181 easllkglkh anivllhdii htketltlvf eyvhtdlcqy mdkhpgglhp dnvklflfql
      241 lrglsyihqr yilhrdlkpq nllisdtgel kladfglara ksvpshtysn evvtlwyrpp
      301 dvllgsteys tcldmwgvgc ifvemiqgva afpgmkdiqd qleriflvlg tpnedtwpgv
      361 hslphfkper ftlyssknlr qawnklsyvn haedlaskll qcspknrlsa qaalsheyfs
      421 dlpprlwelt dmssiftvpn vrlqpeages mrafgknnsy gkslsnskh
//
LOCUS       NP_000993                317 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL10 [Homo sapiens].
ACCESSION   NP_000993
VERSION     NP_000993.1
DBSOURCE    REFSEQ: accession NM_001002.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Ge,Y.L., Li,P.J., Bu,Y.R., Zhang,B., Xu,J., He,S.Y., Cao,Q.L.,
            Bai,Y.G., Ma,J., Zhang,L., Zhou,J. and Xie,M.J.
  TITLE     TNF-alpha and RPLP0 drive the apoptosis of endothelial cells and
            increase susceptibility to high-altitude pulmonary edema
  JOURNAL   Apoptosis 29 (9-10), 1600-1618 (2024)
   PUBMED   39110356
  REMARK    GeneRIF: TNF-alpha and RPLP0 drive the apoptosis of endothelial
            cells and increase susceptibility to high-altitude pulmonary edema.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Wang,Y.L., Zhao,W.W., Bai,S.M., Ma,Y., Yin,X.K., Feng,L.L.,
            Zeng,G.D., Wang,F., Feng,W.X., Zheng,J., Wang,Y.N., Zeng,B.,
            Liu,Q., Hung,M.C. and Wan,X.B.
  TITLE     DNA damage-induced paraspeckle formation enhances DNA repair and
            tumor radioresistance by recruiting ribosomal protein P0
  JOURNAL   Cell Death Dis 13 (8), 709 (2022)
   PUBMED   35974014
  REMARK    GeneRIF: DNA damage-induced paraspeckle formation enhances DNA
            repair and tumor radioresistance by recruiting ribosomal protein
            P0.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Towbin,H., Ramjoue,H.P., Kuster,H., Liverani,D. and Gordon,J.
  TITLE     Monoclonal antibodies against eucaryotic ribosomes. Use to
            characterize a ribosomal protein not previously identified and
            antigenically related to the acidic phosphoproteins P1/P2
  JOURNAL   J Biol Chem 257 (21), 12709-12715 (1982)
   PUBMED   6182142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BF131912.1, BC000087.2, BC019014.2 and AC004263.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein, which
            is the functional equivalent of the E. coli L10 ribosomal protein,
            belongs to the L10P family of ribosomal proteins. It is a neutral
            phosphoprotein with a C-terminal end that is nearly identical to
            the C-terminal ends of the acidic ribosomal phosphoproteins P1 and
            P2. The P0 protein can interact with P1 and P2 to form a pentameric
            complex consisting of P1 and P2 dimers, and a P0 monomer. The
            protein is located in the cytoplasm. Transcript variants derived
            from alternative splicing exist; they encode the same protein. As
            is typical for genes encoding ribosomal proteins, there are
            multiple processed pseudogenes of this gene dispersed through the
            genome. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the predominant transcript.
            It has a different 5' UTR than variant 2. They encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.187834.1,
                                           SRR5189664.41454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392514.9/ ENSP00000376299.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.23"
     Protein         1..317
                     /product="large ribosomal subunit protein uL10"
                     /note="acidic ribosomal phosphoprotein P0; 60S acidic
                     ribosomal protein P0; 60S ribosomal protein L10E;
                     ribosomal protein, large, P0; neutral ribosomal
                     phosphoprotein P0"
                     /calculated_mol_wt=34142
     Region          1..317
                     /region_name="PTZ00135"
                     /note="60S acidic ribosomal protein P0; Provisional"
                     /db_xref="CDD:240285"
     Site            order(10..11,14,57..60,63)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:240221"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P14869; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            order(96,116,120,139,142..143,146..147,149..152,170..172,
                     175..176,178..179,181)
                     /site_type="other"
                     /note="putative Interface with L7/L12 ribosomal proteins
                     [polypeptide binding]"
                     /db_xref="CDD:240221"
     Region          294..317
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05388.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P05388.1)"
     CDS             1..317
                     /gene="RPLP0"
                     /gene_synonym="L10E; LP0; P0; PRLP0; RPP0; uL10"
                     /coded_by="NM_001002.4:78..1031"
                     /db_xref="CCDS:CCDS9193.1"
                     /db_xref="GeneID:6175"
                     /db_xref="HGNC:HGNC:10371"
                     /db_xref="MIM:180510"
ORIGIN      
        1 mpredratwk snyflkiiql lddypkcfiv gadnvgskqm qqirmslrgk avvlmgkntm
       61 mrkairghle nnpalekllp hirgnvgfvf tkedlteird mllankvpaa aragaiapce
      121 vtvpaqntgl gpektsffqa lgittkisrg tieilsdvql iktgdkvgas eatllnmlni
      181 spfsfglviq qvfdngsiyn pevlditeet lhsrflegvr nvasvclqig yptvasvphs
      241 iingykrvla lsvetdytfp laekvkafla dpsafvaaap vaaattaapa aaaapakvea
      301 keeseesded mgfglfd
//
LOCUS       NP_004993                377 aa            linear   PRI 20-NOV-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9,
            mitochondrial precursor [Homo sapiens].
ACCESSION   NP_004993
VERSION     NP_004993.1
DBSOURCE    REFSEQ: accession NM_005002.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Nesti,C., Ticci,C., Rubegni,A., Doccini,S., Scaturro,G., Vetro,A.,
            Guerrini,R., Santorelli,F.M. and Procopio,E.
  TITLE     Additive effect of DNAJC30 and NDUFA9 mutations causing Leigh
            syndrome
  JOURNAL   J Neurol 270 (6), 3266-3269 (2023)
   PUBMED   36939934
  REMARK    GeneRIF: Additive effect of DNAJC30 and NDUFA9 mutations causing
            Leigh syndrome.
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Pinho,S.A., Costa,C.F., Deus,C.M., Pinho,S.L.C., Miranda-Santos,I.,
            Afonso,G., Bagshaw,O., Stuart,J.A., Oliveira,P.J. and
            Cunha-Oliveira,T.
  TITLE     Mitochondrial and metabolic remodelling in human skin fibroblasts
            in response to glucose availability
  JOURNAL   FEBS J 289 (17), 5198-5217 (2022)
   PUBMED   35213938
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Triepels,R.H., Hanson,B.J., van den Heuvel,L.P., Sundell,L.,
            Marusich,M.F., Smeitink,J.A. and Capaldi,R.A.
  TITLE     Human complex I defects can be resolved by monoclonal antibody
            analysis into distinct subunit assembly patterns
  JOURNAL   J Biol Chem 276 (12), 8892-8897 (2001)
   PUBMED   11112787
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Fearnley,I.M., Finel,M., Skehel,J.M. and Walker,J.E.
  TITLE     NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA
            sequences of the import precursors of the nuclear-encoded 39 kDa
            and 42 kDa subunits
  JOURNAL   Biochem J 278 (Pt 3) (Pt 3), 821-829 (1991)
   PUBMED   1832859
  REMARK    GeneRIF: Study identifies mitochondrial transit peptide and
            determines mature protein cleavage site in cow ortholog.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB110957.1, BC009311.2,
            L04490.1, R44283.1 and AC005832.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The encoded protein is a subunit of the hydrophobic
            protein fraction of the NADH:ubiquinone oxidoreductase (complex I),
            the first enzyme complex in the electron transport chain located in
            the inner mitochondrial membrane. A pseudogene has been identified
            on chromosome 12. [provided by RefSeq, May 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.189911.1,
                                           SRR1660805.158793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000266544.10/
                                                  ENSP00000266544.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.32"
     Protein         1..377
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 9, mitochondrial precursor"
                     /EC_number="7.1.1.2"
                     /note="NADH dehydrogenase (ubiquinone) Fe-S protein 2-like
                     (NADH-coenzyme Q reductase); short chain
                     dehydrogenase/reductase family 22E, member 1; complex I
                     39kDa subunit; NADH dehydrogenase (ubiquinone) 1 alpha
                     subcomplex, 9, 39kDa; CI-39kD; NADH-ubiquinone
                     oxidoreductase 39 kDa subunit"
                     /calculated_mol_wt=38900
     transit_peptide 1..35
                     /calculated_mol_wt=3627
     mat_peptide     36..377
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 9, mitochondrial"
                     /note="Inferred from cow ortholog."
                     /calculated_mol_wt=38900
     Region          54..326
                     /region_name="NDUFA9_like_SDR_a"
                     /note="NADH dehydrogenase (ubiquinone) 1 alpha subcomplex,
                     subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs;
                     cd05271"
                     /db_xref="CDD:187579"
     Site            order(60,62..65,84..86,129..131,144,167..169,180,184,
                     203..206)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187579"
     Site            order(180,184)
                     /site_type="active"
                     /db_xref="CDD:187579"
     Site            189
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DC69; propagated from
                     UniProtKB/Swiss-Prot (Q16795.2)"
     Site            370
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DC69; propagated from
                     UniProtKB/Swiss-Prot (Q16795.2)"
     CDS             1..377
                     /gene="NDUFA9"
                     /gene_synonym="CC6; CI-39k; CI39k; COQ11; MC1DN26;
                     NDUFS2L; SDR22E1"
                     /coded_by="NM_005002.5:14..1147"
                     /db_xref="CCDS:CCDS8532.1"
                     /db_xref="GeneID:4704"
                     /db_xref="HGNC:HGNC:7693"
                     /db_xref="MIM:603834"
ORIGIN      
        1 maaaaqsrvv rvlsmsrsai taiatsvchg ppcrqlhhal mphgkggrss vsgivatvfg
       61 atgflgryvv nhlgrmgsqv iipyrcdkyd imhlrpmgdl gqllflewda rdkdsirrvv
      121 qhsnvvinli grdwetknfd fedvfvkipq aiaqlskeag vekfihvshl naniksssry
      181 lrnkavgekv vrdafpeaii vkpsdifgre drflnsfasm hrfgpiplgs lgwktvkqpv
      241 yvvdvskgiv navkdpdang ksfafvgpsr yllfhlvkyi favahrlflp fplplfayrw
      301 varvfeispf epwitrdkve rmhitdmklp hlpgledlgi qatplelkai evlrrhrtyr
      361 wlsaeiedvk paktvni
//
LOCUS       NP_001278522             913 aa            linear   PRI 20-NOV-2025
DEFINITION  nephrocystin-4 isoform b [Homo sapiens].
ACCESSION   NP_001278522
VERSION     NP_001278522.1
DBSOURCE    REFSEQ: accession NM_001291593.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Girault,V., Stukalov,A., Carter-Timofte,M.E., Hertzog,J., Verin,M.,
            Austen,K., Haas,D.A., Oubraham,L., Piras,A., Maidl,S., Ollinger,R.,
            Rad,R., Protzer,U., Kaufer,B.B., Lebbink,R.J., Rehwinkel,J.,
            Mogensen,T.H. and Pichlmair,A.
  TITLE     Multi-proteomic profiling of the varicella-zoster virus-host
            interface reveals host susceptibilities to severe infection
  JOURNAL   Nat Microbiol 10 (8), 2048-2072 (2025)
   PUBMED   40739040
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Ali,A., Unar,A., Muhammad,Z., Dil,S., Zhang,B., Sadaf,H., Khan,M.,
            Ali,M., Khan,R., Shah,K.M.B., Ma,A., Jiang,X., Zhang,Y., Zhang,H.
            and Shi,Q.
  TITLE     A novel NPHP4 homozygous missense variant identified in infertile
            brothers with multiple morphological abnormalities of the sperm
            flagella
  JOURNAL   J Assist Reprod Genet 41 (1), 109-120 (2024)
   PUBMED   37831349
  REMARK    GeneRIF: A novel NPHP4 homozygous missense variant identified in
            infertile brothers with multiple morphological abnormalities of the
            sperm flagella.
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Otaki,Y., Watanabe,T., Sato,J., Kobayashi,Y., Aono,T., Saito,Y.,
            Goto,J., Takahashi,H., Arimoto,T., Sato,H., Konta,T., Ueno,Y. and
            Watanabe,M.
  TITLE     Association of Nephronophthisis 4 genetic variation with
            cardiorenal syndrome and cardiovascular events in Japanese general
            population: the Yamagata (Takahata) study
  JOURNAL   Heart Vessels 37 (4), 673-682 (2022)
   PUBMED   34591160
  REMARK    GeneRIF: Association of Nephronophthisis 4 genetic variation with
            cardiorenal syndrome and cardiovascular events in Japanese general
            population: the Yamagata (Takahata) study.
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Hoefele,J., Otto,E., Felten,H., Kuhn,K., Bley,T.A., Zauner,I.,
            Hildebrandt,F. and Neumann,H.P.
  TITLE     Clinical and histological presentation of 3 siblings with mutations
            in the NPHP4 gene
  JOURNAL   Am J Kidney Dis 43 (2), 358-364 (2004)
   PUBMED   14750102
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Otto,E., Hoefele,J., Ruf,R., Mueller,A.M., Hiller,K.S., Wolf,M.T.,
            Schuermann,M.J., Becker,A., Birkenhager,R., Sudbrak,R.,
            Hennies,H.C., Nurnberg,P. and Hildebrandt,F.
  TITLE     A gene mutated in nephronophthisis and retinitis pigmentosa encodes
            a novel protein, nephroretinin, conserved in evolution
  JOURNAL   Am J Hum Genet 71 (5), 1161-1167 (2002)
   PUBMED   12205563
  REMARK    GeneRIF: Encodes a novel protein, nephroretinin, that is conserved
            in evolution--for example, in the nematode Caenorhabditis elegans.
            GeneRIF: Recessive mutations in the NPHP4 gene, encoding the
            protein nephroretinin, in humans cause nephronophthisis type 4 and
            Senior-Loken syndrome.There is evolutionary conservation of the
            NPHP4 gene, with an ortholog in C. elegans.
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Mollet,G., Salomon,R., Gribouval,O., Silbermann,F., Bacq,D.,
            Landthaler,G., Milford,D., Nayir,A., Rizzoni,G., Antignac,C. and
            Saunier,S.
  TITLE     The gene mutated in juvenile nephronophthisis type 4 encodes a
            novel protein that interacts with nephrocystin
  JOURNAL   Nat Genet 32 (2), 300-305 (2002)
   PUBMED   12244321
  REMARK    GeneRIF: Interacts with NPHP1 protein, suggesting that these two
            proteins participate in a common signaling pathway; identification
            of five different mutations in unrelated individuals with
            nephronophthisis
            Erratum:[Nat Genet 2002 Nov;32(3):459]
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Donaldson,J.C., Dise,R.S., Ritchie,M.D. and Hanks,S.K.
  TITLE     Nephrocystin-conserved domains involved in targeting to epithelial
            cell-cell junctions, interaction with filamins, and establishing
            cell polarity
  JOURNAL   J Biol Chem 277 (32), 29028-29035 (2002)
   PUBMED   12006559
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Schuermann,M.J., Otto,E., Becker,A., Saar,K., Ruschendorf,F.,
            Polak,B.C., Ala-Mello,S., Hoefele,J., Wiedensohler,A., Haller,M.,
            Omran,H., Nurnberg,P. and Hildebrandt,F.
  TITLE     Mapping of gene loci for nephronophthisis type 4 and Senior-Loken
            syndrome, to chromosome 1p36
  JOURNAL   Am J Hum Genet 70 (5), 1240-1246 (2002)
   PUBMED   11920287
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314326.1 and AK124074.1.
            
            Summary: This gene encodes a protein involved in renal tubular
            development and function. This protein interacts with nephrocystin,
            and belongs to a multifunctional complex that is localized to
            actin- and microtubule-based structures. Mutations in this gene are
            associated with nephronophthisis type 4, a renal disease, and with
            Senior-Loken syndrome type 4, a combination of nephronophthisis and
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Apr 2014].
            
            Transcript Variant: This variant (2) lacks three exons and uses an
            alternate splice site in the 5' region, and initiates translation
            at an alternate downstream start codon, compared to variant 1. The
            encoded isoform (b) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314326.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..913
                     /product="nephrocystin-4 isoform b"
                     /note="POC10 centriolar protein homolog; nephroretinin"
                     /calculated_mol_wt=100832
     Region          <80..905
                     /region_name="NPHP4"
                     /note="Nephrocystin-4; cd22239"
                     /db_xref="CDD:412072"
     CDS             1..913
                     /gene="NPHP4"
                     /gene_synonym="POC10; SLSN4"
                     /coded_by="NM_001291593.2:1450..4191"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:261734"
                     /db_xref="HGNC:HGNC:19104"
                     /db_xref="MIM:607215"
ORIGIN      
        1 mhprslsvap kwsgglpgnh prplrefple agishleadl sqtslvlets iaeqlqelpf
       61 tplhapivvg tqtrssagqp srasmvllqs sgfpeildan kqpaeavsat epvtfnpqke
      121 esdclqsnem vlqflafsrv aqdcrgtswp ktvyftfqfy rfppattprl qlvqldeagq
      181 pssgalthil vpvsrdgtfd agspgfqlry mvgpgflkpg errcfaryla vqtlqidvwd
      241 gdsllligsa avqmkhllrq grpavqashe levvateyeq dnmvvsgdml gfgrvkpigv
      301 hsvvkgrlhl tlanvghpce qkvrgcstlp psrsrvisnd gasrfsggsl lttgssrrkh
      361 vvqaqkladv dselaamllt harqgkgpqd vsresdatrr rklermrsvr lqeaggdlgr
      421 rgtsvlaqqs vrtqhlrdlq viaayrertk aesiasllsl aittehtlha tlgvaeffef
      481 vlknphntqh tvtveidnpe lsvivdsqew rdfkgaaglh tpveedmfhl rgslapqlyl
      541 rphetahvpf kfqsfsagql amvqaspgls nekgmdavsp wkssavptkh akvlfrasgg
      601 kpiavlcltv elqphvvdqv frfyhpelsf lkkairlppw htfpgapvgm lgedppvhvr
      661 csdpnvicet qnvgpgeprd iflkvasgps peikdffvii ysdrwlatpt qtwqvylhsl
      721 qrvdvscvag qltrlslvlr gtqtvrkvra ftshpqelkt dpkgvfvlpp rgvqdlhvgv
      781 rplragsrfv hlnlvdvdch qlvaswlvcl ccrqpliska feimlaageg kgvnkrityt
      841 npypsrrtfh lhsdhpellr fredsfqvgg getytiglqf apsqrvgeee iliyindhed
      901 kneeafcvkv iyq
//
LOCUS       NP_001354575             828 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform q [Homo sapiens].
ACCESSION   NP_001354575 NP_001354636
VERSION     NP_001354575.1
DBSOURCE    REFSEQ: accession NM_001367646.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            On May 20, 2019 this sequence version replaced NP_001354636.1.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.157651.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..828
                     /product="SUN domain-containing protein 1 isoform q"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=92012
     Region          12..335
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <408..>632
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          460..513
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(460,463..464,467,470..471,474..475,477..478,
                     481..482,484..485,488..489,491..492,495,498..499,502,
                     505..506,509..510,512..513)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          590..648
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          691..826
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..828
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367646.1:105..2591"
                     /note="isoform q is encoded by transcript variant 17"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy
      241 ygrmnvrevl redghlsvng ealcyfllqi lrrigavgqa vsrtawsalw lavvapgkaa
      301 sgvfwwlgig wyqfvtlisw lnvflltrcl rnickflvll iplflllgls lrgqgnffsf
      361 lpvlnwasmh rtqrvddpqd vfkpttsrlk qplqgdseaf pwhwmsgveq qvaslsgqch
      421 hhgenlrelt tllqklqarv dqmeggaagp sasvrdavgq ppretdfmaf hqehevrmsh
      481 ledilgklre kseaiqkele qtkqktisav geqllptveh lqleldqlks elsswrhvkt
      541 gcetvdavqe rvdvqvremv kllfsedqqg gsleqllqrf ssqfvskgdl qtmlrdlqlq
      601 ilrnvthhvs vtkqlptsea vvsavseaga sgiteaqara ivnsalklys qdktgmvdfa
      661 lesgggsils trcsetyetk talmslfgip lwyfsqsprv viqpdiypgn cwafkgsqgy
      721 lvvrlsmmih paaftlehip ktlsptgnis sapkdfavyg leneyqeegq llgqftydqd
      781 geslqmfqal krpddtafqi velrifsnwg hpeytclyrf rvhgepvk
//
LOCUS       NP_001029082             557 aa            linear   PRI 20-NOV-2025
DEFINITION  TNF receptor-associated factor 5 isoform b [Homo sapiens].
ACCESSION   NP_001029082
VERSION     NP_001029082.1
DBSOURCE    REFSEQ: accession NM_001033910.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Cheng,W.L., Chao,S.P., Zhao,F., Cai,H.H., Zeng,Z., Cao,J.L.,
            Jin,Z., Deng,K.Q., Hu,X., Wang,H. and Lu,Z.
  TITLE     Tumor necrosis factor receptor-associated factor 5 protects against
            intimal hyperplasia by regulation of macrophage polarization via
            directly targeting PPARgamma
  JOURNAL   Inflamm Res 73 (6), 929-943 (2024)
   PUBMED   38642079
  REMARK    GeneRIF: Tumor necrosis factor receptor-associated factor 5
            protects against intimal hyperplasia by regulation of macrophage
            polarization via directly targeting PPARgamma.
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Wu,G., Wu,F., Zhou,Y.Q., Lu,W., Hu,F.L. and Fan,X.
  TITLE     Silencing of TRAF5 enhances necroptosis in hepatocellular carcinoma
            by inhibiting LTBR-mediated NF-kappaB signaling
  JOURNAL   PeerJ 11, e15551 (2023)
   PUBMED   37366426
  REMARK    GeneRIF: Silencing of TRAF5 enhances necroptosis in hepatocellular
            carcinoma by inhibiting LTBR-mediated NF-kappaB signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 557)
  AUTHORS   van Loo,G. and Bertrand,M.J.M.
  TITLE     Death by TNF: a road to inflammation
  JOURNAL   Nat Rev Immunol 23 (5), 289-303 (2023)
   PUBMED   36380021
  REMARK    Review article
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Zhang,F., Luo,B.H., Wu,Q.H., Li,Q.L. and Yang,K.D.
  TITLE     LncRNA HCG18 upregulates TRAF4/TRAF5 to facilitate proliferation,
            migration and EMT of epithelial ovarian cancer by targeting
            miR-29a/b
  JOURNAL   Mol Med 28 (1), 2 (2022)
   PUBMED   34983361
  REMARK    GeneRIF: LncRNA HCG18 upregulates TRAF4/TRAF5 to facilitate
            proliferation, migration and EMT of epithelial ovarian cancer by
            targeting miR-29a/b.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Hsu,H., Solovyev,I., Colombero,A., Elliott,R., Kelley,M. and
            Boyle,W.J.
  TITLE     ATAR, a novel tumor necrosis factor receptor family member, signals
            through TRAF2 and TRAF5
  JOURNAL   J Biol Chem 272 (21), 13471-13474 (1997)
   PUBMED   9153189
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Tang,X.X., Pleasure,D.E. and Ikegaki,N.
  TITLE     cDNA cloning, chromosomal localization, and expression pattern of
            EPLG8, a new member of the EPLG gene family encoding ligands of
            EPH-related protein-tyrosine kinase receptors
  JOURNAL   Genomics 41 (1), 17-24 (1997)
   PUBMED   9126477
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Aizawa,S., Nakano,H., Ishida,T., Horie,R., Nagai,M., Ito,K.,
            Yagita,H., Okumura,K., Inoue,J. and Watanabe,T.
  TITLE     Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2
            are involved in CD30-mediated NFkappaB activation
  JOURNAL   J Biol Chem 272 (4), 2042-2045 (1997)
   PUBMED   8999898
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Ishida,T.K., Tojo,T., Aoki,T., Kobayashi,N., Ohishi,T.,
            Watanabe,T., Yamamoto,T. and Inoue,J.
  TITLE     TRAF5, a novel tumor necrosis factor receptor-associated factor
            family protein, mediates CD40 signaling
  JOURNAL   Proc Natl Acad Sci U S A 93 (18), 9437-9442 (1996)
   PUBMED   8790348
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB290838.1, AB000509.1,
            U69108.1 and BU676629.1.
            
            Summary: The scaffold protein encoded by this gene is a member of
            the tumor necrosis factor receptor-associated factor (TRAF) protein
            family and contains a meprin and TRAF homology (MATH) domain, a
            RING-type zinc finger, and two TRAF-type zinc fingers. TRAF
            proteins are associated with, and mediate signal transduction from
            members of the TNF receptor superfamily. This protein is one of the
            components of a multiple protein complex which binds to tumor
            necrosis factor (TNF) receptor cytoplasmic domains and mediates
            TNF-induced activation. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction compared to variant 4. The resulting isoform (b)
            has the same N- and C-termini but is shorter compared to isoform a.
            Variants 1, 2, and 3 all encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000509.1, SRR14038191.1806335.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261464.10/ ENSP00000261464.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..557
                     /product="TNF receptor-associated factor 5 isoform b"
                     /note="RING finger protein 84"
                     /calculated_mol_wt=64275
     Region          39..94
                     /region_name="mRING-HC-C3HC3D_TRAF5"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tumor necrosis factor (TNF) receptor-associated
                     factor 5 (TRAF5) and similar proteins; cd16642"
                     /db_xref="CDD:438304"
     Site            order(42..43,57,59..63)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438304"
     Region          128..183
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          183..241
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          232..>398
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          345..557
                     /region_name="Interaction with EIF2AK2/PKR.
                     /evidence=ECO:0000269|PubMed:15121867"
                     /note="propagated from UniProtKB/Swiss-Prot (O00463.2)"
     Region          404..550
                     /region_name="MATH"
                     /note="MATH (meprin and TRAF-C homology) domain; an
                     independent folding unit with an eight-stranded
                     beta-sandwich structure found in meprins, TRAFs and other
                     proteins. Meprins comprise a class of extracellular
                     metalloproteases which are anchored to the membrane...;
                     cl02446"
                     /db_xref="CDD:445786"
     Site            order(462,518..520)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:238068"
     CDS             1..557
                     /gene="TRAF5"
                     /gene_synonym="MGC:39780; RNF84"
                     /coded_by="NM_001033910.3:59..1732"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1497.1"
                     /db_xref="GeneID:7188"
                     /db_xref="HGNC:HGNC:12035"
                     /db_xref="MIM:602356"
ORIGIN      
        1 mayseehkgm pcgfirqnsg nsisldfeps ieyqfverle erykcafchs vlhnphqtgc
       61 ghrfcqhcil slrelntvpi cpvdkeviks qevfkdncck revlnlyvyc snapgcnakv
      121 ilgryqdhlq qclfqpvqcs nekcrepvlr kdlkehlsas cqfrkekcly ckkdvvvinl
      181 qnheenlcpe ypvfcpnnca kiilktevde hlavcpeaeq dcpfkhygca vtdkrrnlqq
      241 hehsalrehm rlvleknvql eeqisdlhks leqkeskiqq laetikklek efkqfaqlfg
      301 kngsflpniq vfashidksa wleaqvhqll qmvnqqqnkf dlrplmeavd tvkqkitlle
      361 nndqrlavle eetnkhdthi nihkaqlskn eerfkllegt cyngkliwkv tdykmkkrea
      421 vdghtvsifs qsfytsrcgy rlcaraylng dgsgrgshls lyfvvmrgef dsllqwpfrq
      481 rvtlmlldqs gkknimetfk pdpnsssfkr pdgemniasg cprfvahsvl enaknayikd
      541 dtlflkvavd ltdledl
//
LOCUS       NP_005390                272 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-AMP-activated protein kinase subunit beta-2 [Homo sapiens].
ACCESSION   NP_005390
VERSION     NP_005390.1
DBSOURCE    REFSEQ: accession NM_005399.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Du,H., Wang,Y., Zhu,Y., Li,X., Zhu,T., Wu,Q. and Zha,F.
  TITLE     MiR-29b Alleviates High Glucose-induced Inflammation and Apoptosis
            in Podocytes by Down-regulating PRKAB2
  JOURNAL   Endocr Metab Immune Disord Drug Targets 24 (8), 981-990 (2024)
   PUBMED   38204237
  REMARK    GeneRIF: MiR-29b Alleviates High Glucose-induced Inflammation and
            Apoptosis in Podocytes by Down-regulating PRKAB2.
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Thornton,C., Snowden,M.A. and Carling,D.
  TITLE     Identification of a novel AMP-activated protein kinase beta subunit
            isoform that is highly expressed in skeletal muscle
  JOURNAL   J Biol Chem 273 (20), 12443-12450 (1998)
   PUBMED   9575201
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Stapleton,D., Woollatt,E., Mitchelhill,K.I., Nicholl,J.K.,
            Fernandez,C.S., Michell,B.J., Witters,L.A., Power,D.A.,
            Sutherland,G.R. and Kemp,B.E.
  TITLE     AMP-activated protein kinase isoenzyme family: subunit structure
            and chromosomal location
  JOURNAL   FEBS Lett 409 (3), 452-456 (1997)
   PUBMED   9224708
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Gao,G., Fernandez,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
            Dyck,J.R., Kemp,B.E. and Witters,L.A.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J Biol Chem 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Stapleton,D., Mitchelhill,K.I., Gao,G., Widmer,J., Michell,B.J.,
            Teh,T., House,C.M., Fernandez,C.S., Cox,T., Witters,L.A. and
            Kemp,B.E.
  TITLE     Mammalian AMP-activated protein kinase subfamily
  JOURNAL   J Biol Chem 271 (2), 611-614 (1996)
   PUBMED   8557660
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC053610.1, AC241584.3 and
            CA311731.1.
            
            Summary: The protein encoded by this gene is a regulatory subunit
            of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer
            consisting of an alpha catalytic subunit, and non-catalytic beta
            and gamma subunits. AMPK is an important energy-sensing enzyme that
            monitors cellular energy status. In response to cellular metabolic
            stresses, AMPK is activated, and thus phosphorylates and
            inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy
            beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in
            regulating de novo biosynthesis of fatty acid and cholesterol. This
            subunit may be a positive regulator of AMPK activity. It is highly
            expressed in skeletal muscle and thus may have tissue-specific
            roles. Multiple alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes a functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292820.1, BC053610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254101.4/ ENSP00000254101.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..272
                     /product="5'-AMP-activated protein kinase subunit beta-2"
                     /note="AMPK beta 2; AMPK beta-2 chain; 5'-AMP-activated
                     protein kinase, beta-2 subunit; protein kinase,
                     AMP-activated, beta 2 non-catalytic subunit; AMPK subunit
                     beta-2; AMP-activated protein kinase beta 2 non-catalytic
                     subunit"
                     /calculated_mol_wt=30171
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43741.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZH4; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZH4; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ULK1.
                     /evidence=ECO:0000250|UniProtKB:Q9QZH4; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Region          77..161
                     /region_name="AMPK1_CBM"
                     /note="Glycogen recognition site of AMP-activated protein
                     kinase; pfam16561"
                     /db_xref="CDD:465176"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QZH4; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     Region          183..272
                     /region_name="AMPKBI"
                     /note="5'-AMP-activated protein kinase beta subunit,
                     interation domain; smart01010"
                     /db_xref="CDD:214973"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43741.1)"
     CDS             1..272
                     /gene="PRKAB2"
                     /coded_by="NM_005399.5:66..884"
                     /db_xref="CCDS:CCDS925.1"
                     /db_xref="GeneID:5565"
                     /db_xref="HGNC:HGNC:9379"
                     /db_xref="MIM:602741"
ORIGIN      
        1 mgnttsdrvs gerhgakaar segagghapg kehkimvgst ddpsvfslpd sklpgdkefv
       61 swqqdledsv kptqqarptv irwseggkev fisgsfnnws tkiplikshn dfvaildlpe
      121 gehqykffvd gqwvhdpsep vvtsqlgtin nlihvkksdf evfdalklds messetscrd
      181 lsssppgpyg qemyafrsee rfksppilpp hllqvilnkd tniscdpall pepnhvmlnh
      241 lyalsikdsv mvlsathryk kkyvttllyk pi
//
LOCUS       NP_000199               1382 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin receptor isoform Long preproprotein [Homo sapiens].
ACCESSION   NP_000199
VERSION     NP_000199.2
DBSOURCE    REFSEQ: accession NM_000208.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1382)
  AUTHORS   Jorgensen,S.H., Emdal,K.B., Pedersen,A.K., Axelsen,L.N.,
            Kildegaard,H.F., Demozay,D., Pedersen,T.A., Gronborg,M., Slaaby,R.,
            Nielsen,P.K. and Olsen,J.V.
  TITLE     Multi-layered proteomics identifies insulin-induced upregulation of
            the EphA2 receptor via the ERK pathway which is dependent on low
            IGF1R level
  JOURNAL   Sci Rep 14 (1), 28856 (2024)
   PUBMED   39572596
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1382)
  AUTHORS   Rasheed,R.A., Rasheed,P.H. and Ali,A.M.
  TITLE     Metabolic and hormonal profiling in polycystic ovarian syndrome:
            insights into INSR gene variations
  JOURNAL   Mol Biol Rep 51 (1), 989 (2024)
   PUBMED   39287700
  REMARK    GeneRIF: Metabolic and hormonal profiling in polycystic ovarian
            syndrome: insights into INSR gene variations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1382)
  AUTHORS   Ciulei,G., Orasan,O.H., Cozma,A., Negrean,V., Para,I.,
            Ciumarnean,L., Leach,N., Lucaciu,R.L., Hangan,A.C. and
            Procopciuc,L.M.
  TITLE     Role of Vitamin D Receptor (BsmI-VDR) and Insulin Receptor
            (NsiI-A/G) Gene Polymorphisms in Colorectal Adenoma Susceptibility
  JOURNAL   Int J Mol Sci 25 (16), 8965 (2024)
   PUBMED   39201651
  REMARK    GeneRIF: Role of Vitamin D Receptor (BsmI-VDR) and Insulin Receptor
            (NsiI-A/G) Gene Polymorphisms in Colorectal Adenoma Susceptibility.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1382)
  AUTHORS   Hubbard,S.R.
  TITLE     The insulin receptor: both a prototypical and atypical receptor
            tyrosine kinase
  JOURNAL   Cold Spring Harb Perspect Biol 5 (3), a008946 (2013)
   PUBMED   23457259
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1382)
  AUTHORS   Mesika,A., Klar,A. and Falik Zaccai,T.C.
  TITLE     INSR-Related Severe Insulin Resistance Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29369573
REFERENCE   6  (residues 1 to 1382)
  AUTHORS   Gillis,D.
  TITLE     Nonsyndromic Genetic Hyperinsulinism Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301549
REFERENCE   7  (residues 1 to 1382)
  AUTHORS   Shekels,L.L., Smith,A.J., Van Etten,R.L. and Bernlohr,D.A.
  TITLE     Identification of the adipocyte acid phosphatase as a PAO-sensitive
            tyrosyl phosphatase
  JOURNAL   Protein Sci 1 (6), 710-721 (1992)
   PUBMED   1304913
REFERENCE   8  (residues 1 to 1382)
  AUTHORS   Cama,A., Quon,M.J., de la Luz Sierra,M. and Taylor,S.I.
  TITLE     Substitution of isoleucine for methionine at position 1153 in the
            beta-subunit of the human insulin receptor. A mutation that impairs
            receptor tyrosine kinase activity, receptor endocytosis, and
            insulin action
  JOURNAL   J Biol Chem 267 (12), 8383-8389 (1992)
   PUBMED   1314826
REFERENCE   9  (residues 1 to 1382)
  AUTHORS   Ullrich,A., Bell,J.R., Chen,E.Y., Herrera,R., Petruzzelli,L.M.,
            Dull,T.J., Gray,A., Coussens,L., Liao,Y.C., Tsubokawa,M. et al.
  TITLE     Human insulin receptor and its relationship to the tyrosine kinase
            family of oncogenes
  JOURNAL   Nature 313 (6005), 756-761 (1985)
   PUBMED   2983222
REFERENCE   10 (residues 1 to 1382)
  AUTHORS   Pedersen,O. and Beck-Nielsen,H.
  TITLE     A study of insulin receptors in human mononuclear leucocytes
  JOURNAL   Acta Endocrinol (Copenh) 83 (3), 556-564 (1976)
   PUBMED   185872
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125387.2, HY015976.1,
            BC117172.1, M10051.1, X02160.1, AC010606.7, AK025527.1 and
            BU684722.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 14, 2006 this sequence version replaced NP_000199.1.
            
            Summary: This gene encodes a member of the receptor tyrosine kinase
            family of proteins. The encoded preproprotein is proteolytically
            processed to generate alpha and beta subunits that form a
            heterotetrameric receptor. Binding of insulin or other ligands to
            this receptor activates the insulin signaling pathway, which
            regulates glucose uptake and release, as well as the synthesis and
            storage of carbohydrates, lipids and protein. Mutations in this
            gene underlie the inherited severe insulin resistance syndromes
            including type A insulin resistance syndrome, Donohue syndrome and
            Rabson-Mendenhall syndrome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (Long).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M10051.1, SRR14038194.2414418.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302850.10/ ENSP00000303830.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1382
                     /product="insulin receptor isoform Long preproprotein"
                     /EC_number="2.7.10.1"
                     /note="IR"
                     /calculated_mol_wt=153932
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2420
     mat_peptide     28..758
                     /product="Insulin receptor subunit alpha.
                     /id=PRO_0000016687"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
                     /calculated_mol_wt=83643
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862, ECO:0000269|PubMed:2983222;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          52..164
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            66
                     /site_type="other"
                     /note="Insulin-binding. /evidence=ECO:0000305; propagated
                     from UniProtKB/Swiss-Prot (P06213.4)"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          179..337
                     /region_name="Furin-like"
                     /note="Furin-like cysteine rich region; pfam00757"
                     /db_xref="CDD:395614"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23302862;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            282
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:23302862; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          359..472
                     /region_name="Recep_L_domain"
                     /note="Receptor L domain; pfam01030"
                     /db_xref="CDD:460032"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            401
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            424
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            445
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16894147,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            541
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:1472036,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          <582..>658
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          622..>665
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            633
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            651
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          686..708
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            698
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          733..741
                     /region_name="Insulin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          746..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     mat_peptide     763..1382
                     /product="Insulin receptor subunit beta.
                     /id=PRO_0000016689"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
                     /calculated_mol_wt=69711
     Site            769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:2983222; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            782
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          867..944
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            920
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            order(933..934,936..937)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            933
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          940..987
                     /region_name="Insulin_TMD"
                     /note="Insulin receptor trans-membrane segment; pfam17870"
                     /db_xref="CDD:465543"
     Site            957..979
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            992
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          999
                     /region_name="Important for interaction with IRS1, SHC1
                     and STAT5B. /evidence=ECO:0000269|PubMed:9428692"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            999
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1011
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          1016..1303
                     /region_name="PTKc_InsR"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Insulin Receptor; cd05061"
                     /db_xref="CDD:133192"
     Site            order(1032..1033,1037,1055,1057,1104,1106,1110,1159,
                     1163..1164,1177,1192,1194..1196,1198..1199,1208..1209,
                     1211,1242)
                     /site_type="active"
                     /db_xref="CDD:133192"
     Site            order(1032..1033,1037,1055,1057,1104,1106,1110,1163..1164,
                     1166,1177)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133192"
     Site            order(1046..1049,1127,1129,1169..1170,1295,1300)
                     /site_type="other"
                     /note="PTP1B noncatalytic binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            order(1163,1192,1194..1196,1198..1199,1208..1209,1211,
                     1242)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            1176..1201
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133192"
     Site            order(1183,1185..1186,1188..1189)
                     /site_type="other"
                     /note="APS (SH2 domain) interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133192"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375,
                     ECO:0000269|PubMed:9312016; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1189
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016;
                     propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            1190
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14690593,
                     ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887,
                     ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165,
                     ECO:0000269|PubMed:26584640, ECO:0000269|PubMed:3166375,
                     ECO:0000269|PubMed:9312016; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Site            1355
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     Region          1360..1382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Region          1361..1364
                     /region_name="PIK3R1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P06213.4)"
     Site            1361
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:3166375; propagated from
                     UniProtKB/Swiss-Prot (P06213.4)"
     CDS             1..1382
                     /gene="INSR"
                     /gene_synonym="CD220; HHF5"
                     /coded_by="NM_000208.4:524..4672"
                     /note="isoform Long preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12176.1"
                     /db_xref="GeneID:3643"
                     /db_xref="HGNC:HGNC:6091"
                     /db_xref="MIM:147670"
ORIGIN      
        1 matggrrgaa aapllvavaa lllgaaghly pgevcpgmdi rnnltrlhel encsvieghl
       61 qillmfktrp edfrdlsfpk limitdylll frvygleslk dlfpnltvir gsrlffnyal
      121 vifemvhlke lglynlmnit rgsvrieknn elcylatidw srildsvedn yivlnkddne
      181 ecgdicpgta kgktncpatv ingqfvercw thshcqkvcp tickshgcta eglcchsecl
      241 gncsqpddpt kcvacrnfyl dgrcvetcpp pyyhfqdwrc vnfsfcqdlh hkcknsrrqg
      301 chqyvihnnk cipecpsgyt mnssnllctp clgpcpkvch llegektids vtsaqelrgc
      361 tvingsliin irggnnlaae leanlgliee isgylkirrs yalvslsffr klrlirgetl
      421 eignysfyal dnqnlrqlwd wskhnltitq gklffhynpk lclseihkme evsgtkgrqe
      481 rndialktng dqascenell kfsyirtsfd killrwepyw ppdfrdllgf mlfykeapyq
      541 nvtefdgqda cgsnswtvvd idpplrsndp ksqnhpgwlm rglkpwtqya ifvktlvtfs
      601 derrtygaks diiyvqtdat npsvpldpis vsnsssqiil kwkppsdpng nithylvfwe
      661 rqaedselfe ldyclkglkl psrtwsppfe sedsqkhnqs eyedsagecc scpktdsqil
      721 keleessfrk tfedylhnvv fvprktssgt gaedprpsrk rrslgdvgnv tvavptvaaf
      781 pntsstsvpt speehrpfek vvnkeslvis glrhftgyri elqacnqdtp eercsvaayv
      841 sartmpeaka ddivgpvthe ifennvvhlm wqepkepngl ivlyevsyrr ygdeelhlcv
      901 srkhfalerg crlrglspgn ysvriratsl agngswtept yfyvtdyldv psniakiiig
      961 plifvflfsv vigsiylflr krqpdgplgp lyassnpeyl sasdvfpcsv yvpdewevsr
     1021 ekitllrelg qgsfgmvyeg nardiikgea etrvavktvn esaslrerie flneasvmkg
     1081 ftchhvvrll gvvskgqptl vvmelmahgd lksylrslrp eaennpgrpp ptlqemiqma
     1141 aeiadgmayl nakkfvhrdl aarncmvahd ftvkigdfgm trdiyetdyy rkggkgllpv
     1201 rwmapeslkd gvfttssdmw sfgvvlweit slaeqpyqgl sneqvlkfvm dggyldqpdn
     1261 cpervtdlmr mcwqfnpkmr ptfleivnll kddlhpsfpe vsffhseenk apeseeleme
     1321 fedmenvpld rsshcqreea ggrdggsslg fkrsyeehip ythmnggkkn griltlprsn
     1381 ps
//
LOCUS       NP_001350925             592 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform d precursor [Homo sapiens].
ACCESSION   NP_001350925
VERSION     NP_001350925.1
DBSOURCE    REFSEQ: accession NM_001363996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2063635.1,
                                           SRR14038197.1363882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..592
                     /product="calnexin isoform d precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65396
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     Region          71..440
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27824.2)"
     Region          260..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          276..409
                     /region_name="P domain (Extended arm).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          278..345
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          326..359
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          348..405
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          503..592
                     /region_name="Sufficient to mediate interaction with
                     SGIP1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          511..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK3.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     CDS             1..592
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001363996.1:43..1821"
                     /note="isoform d precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS4447.1"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 megkwllcml lvlgtaivea hdghdddvid ieddlddvie evedskpdtt appsspkvty
       61 kapvptgevy fadsfdrgtl sgwilskakk ddtddeiaky dgkweveemk esklpgdkgl
      121 vlmsrakhha isaklnkpfl fdtkplivqy evnfqngiec ggayvkllsk tpelnldqfh
      181 dktpytimfg pdkcgedykl hfifrhknpk tgiyeekhak rpdadlktyf tdkkthlytl
      241 ilnpdnsfei lvdqsvvnsg nllndmtppv npsreiedpe drkpedwder pkipdpeavk
      301 pddwdedapa kipdeeatkp egwlddepey vpdpdaekpe dwdedmdgew eapqianprc
      361 esapgcgvwq rpvidnpnyk gkwkppmidn psyqgiwkpr kipnpdffed lepfrmtpfs
      421 aiglelwsmt sdiffdnfii cadrrivddw andgwglkka adgaaepgvv gqmieaaeer
      481 pwlwvvyilt valpvflvil fccsgkkqts gmeykktdap qpdvkeeeee keeekdkgde
      541 eeegeeklee kqksdaeedg gtvsqeeedr kpkaeedeil nrsprnrkpr re
//
LOCUS       NP_005403                504 aa            linear   PRI 20-NOV-2025
DEFINITION  serine hydroxymethyltransferase, mitochondrial isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_005403
VERSION     NP_005403.2
DBSOURCE    REFSEQ: accession NM_005412.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Qiao,Z., Li,Y., Li,S., Liu,S. and Cheng,Y.
  TITLE     Hypoxia-induced SHMT2 protein lactylation facilitates glycolysis
            and stemness of esophageal cancer cells
  JOURNAL   Mol Cell Biochem 479 (11), 3063-3076 (2024)
   PUBMED   38175377
  REMARK    GeneRIF: Hypoxia-induced SHMT2 protein lactylation facilitates
            glycolysis and stemness of esophageal cancer cells.
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Han,T., Wang,Y., Cheng,M., Hu,Q., Wan,X., Huang,M., Liu,Y., Xun,W.,
            Xu,J., Wang,L., Luo,R., Yuan,Y., Wang,K. and Wang,J.
  TITLE     Phosphorylated SHMT2 Regulates Oncogenesis Through m6A Modification
            in Lung Adenocarcinoma
  JOURNAL   Adv Sci (Weinh) 11 (18), e2307834 (2024)
   PUBMED   38460155
  REMARK    GeneRIF: Phosphorylated SHMT2 Regulates Oncogenesis Through m[6]A
            Modification in Lung Adenocarcinoma.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Malatesta,M., Fornasier,E., Di Salvo,M.L., Tramonti,A.,
            Zangelmi,E., Peracchi,A., Secchi,A., Polverini,E., Giachin,G.,
            Battistutta,R., Contestabile,R. and Percudani,R.
  TITLE     One substrate many enzymes virtual screening uncovers missing genes
            of carnitine biosynthesis in human and mouse
  JOURNAL   Nat Commun 15 (1), 3199 (2024)
   PUBMED   38615009
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Shan,Y., Liu,D., Li,Y., Wu,C. and Ye,Y.
  TITLE     The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer
  JOURNAL   PeerJ 12, e16594 (2024)
   PUBMED   38188143
  REMARK    GeneRIF: The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Bennett,F.I. and Jackson,A.A.
  TITLE     Glycine is not formed through the amino transferase reaction in
            human or rat placenta
  JOURNAL   Placenta 19 (4), 329-331 (1998)
   PUBMED   9639330
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Girgis,S., Nasrallah,I.M., Suh,J.R., Oppenheim,E., Zanetti,K.A.,
            Mastri,M.G. and Stover,P.J.
  TITLE     Molecular cloning, characterization and alternative splicing of the
            human cytoplasmic serine hydroxymethyltransferase gene
  JOURNAL   Gene 210 (2), 315-324 (1998)
   PUBMED   9573390
  REMARK    GeneRIF: This paper compares the mitochondrial and cytoplasmic
            forms of this enzyme and suggests that the two genes are a result
            of a single gene duplication.
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Trakatellis,A., Dimitriadou,A. and Trakatelli,M.
  TITLE     Pyridoxine deficiency: new approaches in immunosuppression and
            chemotherapy
  JOURNAL   Postgrad Med J 73 (864), 617-622 (1997)
   PUBMED   9497969
  REMARK    Review article
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Stover,P.J., Chen,L.H., Suh,J.R., Stover,D.M., Keyomarsi,K. and
            Shane,B.
  TITLE     Molecular cloning, characterization, and regulation of the human
            mitochondrial serine hydroxymethyltransferase gene
  JOURNAL   J Biol Chem 272 (3), 1842-1848 (1997)
   PUBMED   8999870
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Garrow,T.A., Brenner,A.A., Whitehead,V.M., Chen,X.N., Duncan,R.G.,
            Korenberg,J.R. and Shane,B.
  TITLE     Cloning of human cDNAs encoding mitochondrial and cytosolic serine
            hydroxymethyltransferases and chromosomal localization
  JOURNAL   J Biol Chem 268 (16), 11910-11916 (1993)
   PUBMED   8505317
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Waziri,R., Baruah,S. and Sherman,A.D.
  TITLE     Abnormal serine-glycine metabolism in the brains of schizophrenics
  JOURNAL   Schizophr Res 8 (3), 233-243 (1993)
   PUBMED   8435385
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC386590.1, BC011911.2 and
            BC091501.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_005403.1.
            
            Summary: This gene encodes the mitochondrial form of a pyridoxal
            phosphate-dependent enzyme that catalyzes the reversible reaction
            of serine and tetrahydrofolate to glycine and 5,10-methylene
            tetrahydrofolate. The encoded product is primarily responsible for
            glycine synthesis. The activity of the encoded protein has been
            suggested to be the primary source of intracellular glycine. The
            gene which encodes the cytosolic form of this enzyme is located on
            chromosome 17. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.596213.1,
                                           SRR3476690.348619.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000328923.8/
                                                  ENSP00000333667.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..504
                     /product="serine hydroxymethyltransferase, mitochondrial
                     isoform 1 precursor"
                     /EC_number="2.1.2.1"
                     /note="glycine hydroxymethyltransferase; serine aldolase;
                     serine hydroxymethylase; threonine aldolase; GLY A+;
                     glycine auxotroph A, human complement for hamster; serine
                     methylase; epididymis secretory sperm binding protein Li
                     51e; serine hydroxymethyltransferase 2 (mitochondrial);
                     mitochondrial serine hydroxymethyltransferase"
                     /calculated_mol_wt=52560
     transit_peptide 1..29
                     /calculated_mol_wt=3451
     mat_peptide     30..504
                     /product="serine hydroxymethyltransferase, mitochondrial
                     isoform 1"
                     /calculated_mol_wt=52560
     Region          30..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P34897.3)"
     Region          45..502
                     /region_name="PLN03226"
                     /note="serine hydroxymethyltransferase; Provisional"
                     /db_xref="CDD:215639"
     Site            order(53,55,62..63,72,77,95,113..114,122,141,148,188..189,
                     328,346)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(76,96,106,143..144,171,226,251,254,279..280,286,425)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(76,171,280,425)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(98,105,166,170,172,320,410)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
     Site            103
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            181
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            196
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            297
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            356
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            464
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            469
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     Site            474
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P34897.3)"
     CDS             1..504
                     /gene="SHMT2"
                     /gene_synonym="GLYA; HEL-S-51e; mSHMT; NEDCASB; SHMT"
                     /coded_by="NM_005412.6:69..1583"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8934.1"
                     /db_xref="GeneID:6472"
                     /db_xref="HGNC:HGNC:10852"
                     /db_xref="MIM:138450"
ORIGIN      
        1 mlyfslfwaa rplqrcgqlv rmairaqhsn aaqtqtgean rgwtgqesls dsdpemwell
       61 qrekdrqcrg leliasenfc sraalealgs clnnkysegy pgkryyggae vvdeiellcq
      121 rraleafdld paqwgvnvqp ysgspanlav ytallqphdr imgldlpdgg hlthgymsdv
      181 krisatsiff esmpyklnpk tglidynqla ltarlfrprl iiagtsayar lidyarmrev
      241 cdevkahlla dmahisglva akvipspfkh adivtttthk tlrgarsgli fyrkgvkavd
      301 pktgreipyt fedrinfavf pslqggphnh aiaavavalk qactpmfrey slqvlknara
      361 madallergy slvsggtdnh lvlvdlrpkg ldgaraervl elvsitankn tcpgdrsait
      421 pgglrlgapa ltsrqfredd frrvvdfide gvniglevks ktaklqdfks fllkdsetsq
      481 rlanlrqrve qfarafpmpg fdeh
//
LOCUS       NP_001350452            1034 aa            linear   PRI 20-NOV-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 isoform 4
            precursor [Homo sapiens].
ACCESSION   NP_001350452 XP_005249818
VERSION     NP_001350452.1
DBSOURCE    REFSEQ: accession NM_001363523.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Whittle,E.F., Chilian,M., Karimiani,E.G., Progri,H., Buhas,D.,
            Kose,M., Ganetzky,R.D., Toosi,M.B., Torbati,P.N., Badv,R.S.,
            Shelihan,I., Yang,H., Elloumi,H.Z., Lee,S., Jamshidi,Y.,
            Pittman,A.M., Houlden,H., Ignatius,E., Rahman,S., Maroofian,R.,
            Yoon,W.H. and Carroll,C.J.
  TITLE     Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead
            to a neurodevelopmental disorder characterized by global
            developmental delay, movement disorder, and metabolic abnormalities
  JOURNAL   Genet Med 25 (2), 100332 (2023)
   PUBMED   36520152
  REMARK    GeneRIF: Biallelic variants in OGDH encoding oxoglutarate
            dehydrogenase lead to a neurodevelopmental disorder characterized
            by global developmental delay, movement disorder, and metabolic
            abnormalities.
REFERENCE   4  (residues 1 to 1034)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1034)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 1034)
  AUTHORS   McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
            Lindsay,J.G.
  TITLE     Subunit interactions in the mammalian alpha-ketoglutarate
            dehydrogenase complex. Evidence for direct association of the
            alpha-ketoglutarate dehydrogenase and dihydrolipoamide
            dehydrogenase components
  JOURNAL   J Biol Chem 273 (37), 24158-24164 (1998)
   PUBMED   9727038
REFERENCE   7  (residues 1 to 1034)
  AUTHORS   Koike,K.
  TITLE     The gene encoding human 2-oxoglutarate dehydrogenase: structural
            organization and mapping to chromosome 7p13-p14
  JOURNAL   Gene 159 (2), 261-266 (1995)
   PUBMED   7622061
REFERENCE   8  (residues 1 to 1034)
  AUTHORS   Szabo,P., Cai,X., Ali,G. and Blass,J.P.
  TITLE     Localization of the gene (OGDH) coding for the E1k component of the
            alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
  JOURNAL   Genomics 20 (2), 324-326 (1994)
   PUBMED   8020988
REFERENCE   9  (residues 1 to 1034)
  AUTHORS   Koike,K., Urata,Y. and Goto,S.
  TITLE     Cloning and nucleotide sequence of the cDNA encoding human
            2-oxoglutarate dehydrogenase (lipoamide)
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1963-1967 (1992)
   PUBMED   1542694
REFERENCE   10 (residues 1 to 1034)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011894.3 and AC004859.3.
            
            On May 24, 2018 this sequence version replaced XP_005249818.1.
            
            Summary: This gene encodes one subunit of the 2-oxoglutarate
            dehydrogenase complex. This complex catalyzes the overall
            conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
            and CO(2) during the Krebs cycle. The protein is located in the
            mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.
            A congenital deficiency in 2-oxoglutarate dehydrogenase activity is
            believed to lead to hypotonia, metabolic acidosis, and
            hyperlactatemia. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Sep 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.100068.1,
                                           SRR1660809.125355.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1034
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 4 precursor"
                     /EC_number="1.2.4.2"
                     /note="oxoglutarate dehydrogenase (succinyl-transferring);
                     oxoglutarate (alpha-ketoglutarate) dehydrogenase
                     (lipoamide); 2-oxoglutarate dehydrogenase, mitochondrial;
                     oxoglutarate decarboxylase; OGDC-E1; 2-oxoglutarate
                     dehydrogenase complex component E1; testicular tissue
                     protein Li 131; alpha-KGDH-E1; thiamine diphosphate
                     (ThDP)-dependent 2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=117113
     Region          49..1027
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     CDS             1..1034
                     /gene="OGDH"
                     /gene_synonym="AKGDH; E1k; E1o; HsOGDH; KGD1; OGDC;
                     OGDH-E1; OGDH2; OGDHD"
                     /coded_by="NM_001363523.2:55..3159"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS87498.1"
                     /db_xref="GeneID:4967"
                     /db_xref="HGNC:HGNC:8124"
                     /db_xref="MIM:613022"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
      121 dklvedhlav qslirayqvr ghhiakldpl giscvnfdda pvtvssnvdl avfkerlrml
      181 tvggfyglde sdldkvfhlp tttfiggqes alplreiirr lemaycqhig vefmfindle
      241 qcqwirqkfe tpgimqftne ekrtllarlv rstrfeeflq rkwssekrfg legcevlipa
      301 lktiidksse ngvdyvimgm phrgrlnvla nvirkeleqi fcqfdsklea adegsgdvky
      361 hlgmyhrrin rvtdrnitls lvanpshlea adpvvmgktk aeqfycgdte gkkvmsillh
      421 gdaafagqgi vyetfhlsdl psytthgtvh vvvnnqigft tdprmarssp yptdvarvvn
      481 apifhvnsdd peavmyvckv aaewrstfhk dvvvdlvcyr rnghnemdep mftqplmykq
      541 irkqkpvlqk yaellvsqgv vnqpeyeeei skydkiceea farskdekil hikhwldspw
      601 pgfftldgqp rsmscpstgl tedilthign vassvpvenf tihgglsril ktrgemvknr
      661 tvdwalaeym afgsllkegi hirlsgqdve rgtfshrhhv lhdqnvdkrt cipmnhlwpn
      721 qapytvcnss lseygvlgfe lgfamaspna lvlweaqfgd fhntaqciid qficpgqakw
      781 vrqngivlll phgmegmgpe hssarperfl qmcnddpdvl pdlkeanfdi nqlydcnwvv
      841 vncstpgnff hvlrrqillp frkpliiftp ksllrhpear ssfdemlpgt hfqrvipedg
      901 paaqnpenvk rllfctgkvy ydltrerkar dmvgqvaitr ieqlspfpfd lllkevqkyp
      961 naelawcqee hknqgyydyv kprlrttisr akpvwyagrd paaapatgnk kthltelqrl
     1021 ldtafdldvf knfs
//
LOCUS       NP_003609                894 aa            linear   PRI 20-NOV-2025
DEFINITION  mitogen-activated protein kinase kinase kinase kinase 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_003609
VERSION     NP_003609.2
DBSOURCE    REFSEQ: accession NM_003618.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Chuang,H.C., Hung,W.T., Chen,Y.M., Hsu,P.M., Yen,J.H., Lan,J.L. and
            Tan,T.H.
  TITLE     Genomic sequencing and functional analyses identify MAP4K3/GLK
            germline and somatic variants associated with systemic lupus
            erythematosus
  JOURNAL   Ann Rheum Dis 81 (2), 243-254 (2022)
   PUBMED   34610951
  REMARK    GeneRIF: Genomic sequencing and functional analyses identify
            MAP4K3/GLK germline and somatic variants associated with systemic
            lupus erythematosus.
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Song,Y., Zhang,F., Li,L., Song,B., Xu,J., Wang,G. and Zheng,Z.
  TITLE     MiR-338-3p inhibits growth of glioblastoma through targeting MAP4K3
  JOURNAL   Minerva Med 112 (4), 531-533 (2021)
   PUBMED   31578840
  REMARK    GeneRIF: MiR-338-3p inhibits growth of glioblastoma through
            targeting MAP4K3.
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 894)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 894)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
REFERENCE   7  (residues 1 to 894)
  AUTHORS   Yan,L., Mieulet,V., Burgess,D., Findlay,G.M., Sully,K., Procter,J.,
            Goris,J., Janssens,V., Morrice,N.A. and Lamb,R.F.
  TITLE     PP2A T61 epsilon is an inhibitor of MAP4K3 in nutrient signaling to
            mTOR
  JOURNAL   Mol Cell 37 (5), 633-642 (2010)
   PUBMED   20227368
  REMARK    GeneRIF: Amino acid sufficiency phosphorylates MAP4K3/Ser170,
            activating mTORC1, but amino acid restriction causes MAP4K3 to
            interact with PP2A(T61 epsilon), promoting dephosphorylation of
            Ser170, MAP4K3 inhibition, and, inhibition of mTORC1 signaling.
REFERENCE   8  (residues 1 to 894)
  AUTHORS   Lam,D. and Martins,L.M.
  TITLE     MAP4K3 enhances the expression of the BH3-only protein BID
  JOURNAL   Cell Cycle 8 (20), 3248-3249 (2009)
   PUBMED   19806019
REFERENCE   9  (residues 1 to 894)
  AUTHORS   Lam,D., Dickens,D., Reid,E.B., Loh,S.H., Moisoi,N. and Martins,L.M.
  TITLE     MAP4K3 modulates cell death via the post-transcriptional regulation
            of BH3-only proteins
  JOURNAL   Proc Natl Acad Sci U S A 106 (29), 11978-11983 (2009)
   PUBMED   19587239
  REMARK    GeneRIF: MAP4K3 orchestrates activation of BAX via the concerted
            posttranscriptional modulation of PUMA, BAD, and BIM.
REFERENCE   10 (residues 1 to 894)
  AUTHORS   Diener,K., Wang,X.S., Chen,C., Meyer,C.F., Keesler,G., Zukowski,M.,
            Tan,T.H. and Yao,Z.
  TITLE     Activation of the c-Jun N-terminal kinase pathway by a novel
            protein kinase related to human germinal center kinase
  JOURNAL   Proc Natl Acad Sci U S A 94 (18), 9687-9692 (1997)
   PUBMED   9275185
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA409370.1, AK291467.1,
            AC007684.3, AK021553.1 and AC079615.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 6, 2001 this sequence version replaced NP_003609.1.
            
            Summary: This gene encodes a member of the mitogen-activated
            protein kinase kinase kinase kinase family. The encoded protein
            activates key effectors in cell signalling, among them c-Jun.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060880.1, SRR1660809.155177.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263881.8/ ENSP00000263881.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..894
                     /product="mitogen-activated protein kinase kinase kinase
                     kinase 3 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="germinal center kinase-related protein kinase;
                     germinal center kinase-like kinase; MEK kinase kinase 3;
                     MAPK/ERK kinase kinase kinase 3"
                     /calculated_mol_wt=101185
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IVH8.1)"
     Region          15..273
                     /region_name="STKc_MAP4K3_like"
                     /note="Catalytic domain of Mitogen-activated protein
                     kinase kinase kinase kinase (MAP4K) 3-like
                     Serine/Threonine Kinases; cd06613"
                     /db_xref="CDD:270788"
     Site            order(22..26,30,43,45,74,90..93,96..97,100,136,138..141,
                     143,153..154,157,171..174,176,206,215)
                     /site_type="active"
                     /db_xref="CDD:270788"
     Site            order(22..26,30,43,45,74,90..93,96..97,100,140..141,143,
                     154)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270788"
     Site            order(25..26,136,138..140,157,171..174,176,206,215)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270788"
     Site            order(153..164,167..176)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270788"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JP0; propagated from
                     UniProtKB/Swiss-Prot (Q8IVH8.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q8IVH8.1)"
     Region          410..536
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVH8.1)"
     Region          561..874
                     /region_name="CNH"
                     /note="Domain found in NIK1-like kinases, mouse citron and
                     yeast ROM1, ROM2; smart00036"
                     /db_xref="CDD:214481"
     CDS             1..894
                     /gene="MAP4K3"
                     /gene_synonym="GLK; MAPKKKK3; MEKKK 3; MEKKK3; RAB8IPL1"
                     /coded_by="NM_003618.4:299..2983"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1803.1"
                     /db_xref="GeneID:8491"
                     /db_xref="HGNC:HGNC:6865"
                     /db_xref="MIM:604921"
ORIGIN      
        1 mnpgfdlsrr npqedfeliq rigsgtygdv ykarnvntge laaikvikle pgedfavvqq
       61 eiimmkdckh pnivayfgsy lrrdklwicm efcgggslqd iyhvtgplse lqiayvsret
      121 lqglyylhsk gkmhrdikga nilltdnghv kladfgvsaq itatiakrks figtpywmap
      181 evaaverkgg ynqlcdlwav gitaielael qppmfdlhpm ralflmtksn fqppklkdkm
      241 kwsnsfhhfv kmaltknpkk rptaekllqh pfvtqhltrs laielldkvn npdhstyhdf
      301 ddddpeplva vphrihstsr nvreektrse itfgqvkfdp plrketephh elpdsdgfld
      361 sseeiyytar snldlqleyg qghqggyflg anksllksve eelhqrghva hleddegddd
      421 eskhstlkak ippplppkpk sifipqemhs tedenqgtik rcpmsgspak psqvpprppp
      481 prlpphkpva lgngmssfql ngerdgslcq qqnehrgtnl srkekkdvpk pisnglpptp
      541 kvhmgacfsk vfngcplkih casswinpdt rdqylifgae egiytlnlne lhetsmeqlf
      601 prrctwlyvm nncllsisgk asqlyshnlp glfdyarqmq klpvaipahk lpdrilprkf
      661 svsakipetk wcqkccvvrn pytghkylcg alqtsivlle wvepmqkfml ikhidfpipc
      721 plrmfemlvv peqeyplvcv gvsrgrdfnq vvrfetvnpn stsswftesd tpqtnvthvt
      781 qlerdtilvc ldccikivnl qgrlkssrkl sseltfdfqi esivclqdsv lafwkhgmqg
      841 rsfrsnevtq eisdstrifr llgsdrvvvl esrptdnpta nsnlyilagh ensy
//
LOCUS       NP_001357589             776 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-1 [Homo sapiens].
ACCESSION   NP_001357589 XP_011514932
VERSION     NP_001357589.1
DBSOURCE    REFSEQ: accession NM_001370660.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Yang,T., Hu,J., Zhang,L., Liu,L., Pan,X., Zhou,Y., Wu,Y., Shi,X.,
            Obiegbusi,C.N. and Dong,X.
  TITLE     CircCUL1 inhibits trophoblast cell migration and invasion and
            promotes cell autophagy by sponging hsa-miR-30e-3p in fetal growth
            restriction via the ANXA1/PI3K/AKT axis
  JOURNAL   J Biochem Mol Toxicol 38 (7), e23759 (2024)
   PUBMED   39003567
  REMARK    GeneRIF: CircCUL1 inhibits trophoblast cell migration and invasion
            and promotes cell autophagy by sponging hsa-miR-30e-3p in fetal
            growth restriction via the ANXA1/PI3K/AKT axis.
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,Y., Huang,X., Wang,Y., Lei,Y., Yu,J., Yu,S., Gao,Y., Yang,J.,
            Zhao,F., Yu,H., Zeng,J., Chu,Y., Yang,M., Li,G., Xie,X. and
            Zhang,J.
  TITLE     NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer by
            Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins
  JOURNAL   Adv Sci (Weinh) 11 (9), e2305907 (2024)
   PUBMED   38126621
  REMARK    GeneRIF: NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer
            by Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Khalil,M.I., Yang,C., Vu,L., Chadha,S., Nabors,H., James,C.D.,
            Morgan,I.M. and Pyeon,D.
  TITLE     The membrane-associated ubiquitin ligase MARCHF8 stabilizes the
            human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in
            head and neck cancer
  JOURNAL   J Virol 98 (2), e0172623 (2024)
   PUBMED   38226814
  REMARK    GeneRIF: The membrane-associated ubiquitin ligase MARCHF8
            stabilizes the human papillomavirus oncoprotein E7 by degrading
            CUL1 and UBE2L3 in head and neck cancer.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Winston,J.T., Strack,P., Beer-Romero,P., Chu,C.Y., Elledge,S.J. and
            Harper,J.W.
  TITLE     The SCFbeta-TRCP-ubiquitin ligase complex associates specifically
            with phosphorylated destruction motifs in IkappaBalpha and
            beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
  JOURNAL   Genes Dev 13 (3), 270-283 (1999)
   PUBMED   9990852
  REMARK    Erratum:[Genes Dev 1999 Apr 15;13(8):1050]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Ng,R.W., Arooz,T., Yam,C.H., Chan,I.W., Lau,A.W. and Poon,R.Y.
  TITLE     Characterization of the cullin and F-box protein partner Skp1
  JOURNAL   FEBS Lett 438 (3), 183-189 (1998)
   PUBMED   9827542
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005229.2 and AC006323.3.
            
            On May 21, 2019 this sequence version replaced XP_011514932.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.422964.1,
                                           SRR1803615.131470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..776
                     /product="cullin-1"
                     /note="CUL-1"
                     /calculated_mol_wt=89548
     Region          21..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Site            63
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13616.2)"
     Region          706..768
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..776
                     /gene="CUL1"
                     /coded_by="NM_001370660.1:666..2996"
                     /db_xref="CCDS:CCDS34772.1"
                     /db_xref="GeneID:8454"
                     /db_xref="HGNC:HGNC:2551"
                     /db_xref="MIM:603134"
ORIGIN      
        1 msstrsqnph glkqigldqi wddlragiqq vytrqsmaks rymelythvy nyctsvhqsn
       61 qargagvpps kskkgqtpgg aqfvglelyk rlkeflknyl tnllkdgedl mdesvlkfyt
      121 qqwedyrfss kvlngicayl nrhwvrrecd egrkgiyeiy slalvtwrdc lfrplnkqvt
      181 navlklieke rngetintrl isgvvqsyve lglneddafa kgptltvyke sfesqfladt
      241 erfytreste flqqnpvtey mkkaearlle eqrrvqvylh estqdelark ceqvliekhl
      301 eifhtefqnl ldadknedlg rmynlvsriq dglgelkkll ethihnqgla aiekcgeaal
      361 ndpkmyvqtv ldvhkkynal vmsafnndag fvaaldkacg rfinnnavtk maqssskspe
      421 llarycdsll kkssknpeea eledtlnqvm vvfkyiedkd vfqkfyakml akrlvhqnsa
      481 sddaeasmis klkqacgfey tsklqrmfqd igvskdlneq fkkhltnsep ldldfsiqvl
      541 ssgswpfqqs ctfalpsele rsyqrftafy asrhsgrklt wlyqlskgel vtncfknryt
      601 lqastfqmai llqynteday tvqqltdstq ikmdilaqvl qillkskllv ledenanvde
      661 velkpdtlik lylgyknkkl rvninvpmkt eqkqeqetth knieedrkll iqaaivrimk
      721 mrkvlkhqql lgevltqlss rfkprvpvik kcidilieke ylervdgekd tysyla
//
LOCUS       NP_006806                201 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane emp24 domain-containing protein 2 isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_006806
VERSION     NP_006806.1
DBSOURCE    REFSEQ: accession NM_006815.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Sun,C., Zhang,Y., Wang,Z., Chen,J., Zhang,J. and Gu,Y.
  TITLE     TMED2 promotes glioma tumorigenesis by being involved in EGFR
            recycling transport
  JOURNAL   Int J Biol Macromol 262 (Pt 2), 130055 (2024)
   PUBMED   38354922
  REMARK    GeneRIF: TMED2 promotes glioma tumorigenesis by being involved in
            EGFR recycling transport.
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Liang,C., Zhang,H.Y., Wang,Y.Q., Yang,L.A., Du,Y.S., Luo,Y.,
            Zhang,T.C. and Xu,Y.
  TITLE     TMED2 Induces Cisplatin Resistance in Breast Cancer via Targeting
            the KEAP1-Nrf2 Pathway
  JOURNAL   Curr Med Sci 43 (5), 1023-1032 (2023)
   PUBMED   37615927
  REMARK    GeneRIF: TMED2 Induces Cisplatin Resistance in Breast Cancer via
            Targeting the KEAP1-Nrf2 Pathway.
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Goldberg,J.
  TITLE     Decoding of sorting signals by coatomer through a GTPase switch in
            the COPI coat complex
  JOURNAL   Cell 100 (6), 671-679 (2000)
   PUBMED   10761932
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Fullekrug,J., Suganuma,T., Tang,B.L., Hong,W., Storrie,B. and
            Nilsson,T.
  TITLE     Localization and recycling of gp27 (hp24gamma3): complex formation
            with other p24 family members
  JOURNAL   Mol Biol Cell 10 (6), 1939-1955 (1999)
   PUBMED   10359607
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Gommel,D., Orci,L., Emig,E.M., Hannah,M.J., Ravazzola,M.,
            Nickel,W., Helms,J.B., Wieland,F.T. and Sohn,K.
  TITLE     p24 and p23, the major transmembrane proteins of COPI-coated
            transport vesicles, form hetero-oligomeric complexes and cycle
            between the organelles of the early secretory pathway
  JOURNAL   FEBS Lett 447 (2-3), 179-185 (1999)
   PUBMED   10214941
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Fiedler,K., Veit,M., Stamnes,M.A. and Rothman,J.E.
  TITLE     Bimodal interaction of coatomer with the p24 family of putative
            cargo receptors
  JOURNAL   Science 273 (5280), 1396-1399 (1996)
   PUBMED   8703076
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Blum,R., Feick,P., Puype,M., Vandekerckhove,J., Klengel,R.,
            Nastainczyk,W. and Schulz,I.
  TITLE     Tmp21 and p24A, two type I proteins enriched in pancreatic
            microsomal membranes, are members of a protein family involved in
            vesicular trafficking
  JOURNAL   J Biol Chem 271 (29), 17183-17189 (1996)
   PUBMED   8663407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055713.29, BI086507.1 and BC025957.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.972817.1,
                                           SRR1660805.248900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262225.8/ ENSP00000262225.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..201
                     /product="transmembrane emp24 domain-containing protein 2
                     isoform 1 precursor"
                     /note="coated vesicle membrane protein; membrane protein
                     p24A; p24 family protein beta-1; transmembrane emp24
                     domain trafficking protein 2"
                     /calculated_mol_wt=20781
     Region          1..181
                     /region_name="Interaction with F2RL1.
                     /evidence=ECO:0000269|PubMed:17693410"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1999
     Region          20..196
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     mat_peptide     21..201
                     /product="Transmembrane emp24 domain-containing protein 2.
                     /id=PRO_0000010381"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
                     /calculated_mol_wt=20781
     Region          118..157
                     /region_name="Required for TMED10 and TMED2 cis-Golgi
                     network localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Site            169..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Region          194..201
                     /region_name="COPI vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     Region          194..195
                     /region_name="COPII vesicle coat-binding.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15363.1)"
     CDS             1..201
                     /gene="TMED2"
                     /gene_synonym="p24; P24A; p24b1; p24beta1; RNP24"
                     /coded_by="NM_006815.4:86..691"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9250.1"
                     /db_xref="GeneID:10959"
                     /db_xref="HGNC:HGNC:16996"
                     /db_xref="MIM:619642"
ORIGIN      
        1 mvtlaellvl laallatvsg yfvsidahae ecffervtsg tkmglifeva eggfldidve
       61 itgpdnkgiy kgdressgky tfaahmdgty kfcfsnrmst mtpkivmfti digeapkgqd
      121 meteahqnkl eeminelava mtavkheqey mevrerihra indntnsrvv lwsffealvl
      181 vamtlgqiyy lkrffevrrv v
//
LOCUS       NP_001332927             653 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 70 isoform 2 [Homo sapiens].
ACCESSION   NP_001332927 XP_005248375
VERSION     NP_001332927.1
DBSOURCE    REFSEQ: accession NM_001345998.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Mao,X., Wu,J., Zhang,Q., Zhang,S., Chen,X., Liu,X., Wei,M., Wan,X.,
            Qiu,L., Zeng,M., Lei,X., Liu,C. and Han,J.
  TITLE     Requirement of WDR70 for POLE3-mediated DNA double-strand breaks
            repair
  JOURNAL   Sci Adv 9 (36), eadh2358 (2023)
   PUBMED   37682991
  REMARK    GeneRIF: Requirement of WDR70 for POLE3-mediated DNA double-strand
            breaks repair.
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Tang,Z.Z., Wang,H.B., Zeng,M., Liu,C. and Li,D.H.
  TITLE     [DNA Repair Function and Mutation of an H2B Monoubiquitination
            Factor WDR70 in Ovarian Cancer]
  JOURNAL   Sichuan Da Xue Xue Bao Yi Xue Ban 48 (5), 693-698 (2017)
   PUBMED   29130659
  REMARK    GeneRIF: Ovarian cancer had different expression of WDR70 and H2B
            monoubiquitination compared with normal tissue
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Guo,L.D., Wang,D., Yang,F., Liang,Y.J., Yang,X.Q., Qin,Y.Y.,
            Ren,L.F., Zeng,M., Tang,Z.Z., Wang,X.J., Wang,S., Liu,C., Lou,J.Y.
            and Chen,J.
  TITLE     [Functional Analysis of DNA Damage Repair Factor WDR70 and Its
            Mutation in Ovarian Cancer]
  JOURNAL   Sichuan Da Xue Xue Bao Yi Xue Ban 47 (4), 501-506 (2016)
   PUBMED   28591950
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Zeng,M., Ren,L., Mizuno,K., Nestoras,K., Wang,H., Tang,Z., Guo,L.,
            Kong,D., Hu,Q., He,Q., Du,L., Carr,A.M. and Liu,C.
  TITLE     CRL4(Wdr70) regulates H2B monoubiquitination and facilitates
            Exo1-dependent resection
  JOURNAL   Nat Commun 7, 11364 (2016)
   PUBMED   27098497
  REMARK    GeneRIF: CRL4(Wdr70) regulates H2B monoubiquitination and
            facilitates Exo1-dependent DNA repair resection.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC117532.2, AC025469.6 and AC093269.3.
            
            On Sep 17, 2016 this sequence version replaced XP_005248375.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is 1 aa shorter compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.165034.1,
                                           SRR1803611.83038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..653
                     /product="WD repeat-containing protein 70 isoform 2"
                     /note="WD repeat-containing protein 70"
                     /calculated_mol_wt=72941
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          176..497
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          179..218
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            order(180,198,202,208..209,225,229,245,249,255..256,268,
                     281,304,310..311,330,347,352,358..359,373..374,394,398,
                     404..405,415..416,438,449,455..456,468..469,487,491,497)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          184..226
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          226..267
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          232..280
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          280..320
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          285..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          329..368
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          335..375
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          375..414
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          381..417
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          420..465
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          425..469
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            451
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          468..507
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          473..497
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          539..578
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          629..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     CDS             1..653
                     /gene="WDR70"
                     /coded_by="NM_001345998.2:51..2012"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55100"
                     /db_xref="HGNC:HGNC:25495"
                     /db_xref="MIM:617233"
ORIGIN      
        1 mersgpsevt gsdasgpdpq lavtmgftgf gkkartfdle amfeqtrrta versrktlar
       61 ekeeemnrek elrrqnedie ptssrsnvvr dcsksssrdt ssseseqssd ssddeligpp
      121 lppkmvgkpv nfmeedilgp lppplneeee eaeeeeeeee eeenpvhkip dsheitlkhg
      181 tktvsalgld psgarlvtgg ydydvkfwdf agmdasfkaf rslqpcechq ikslqysntg
      241 dmilvvsgss qakvidrdgf evmecikgdq yivdmantkg htamlhtgsw hpkikgefmt
      301 csndatvrtw evenpkkqks vfkprtmqgk kvipttctys rdgnliaaac qngsiqiwdr
      361 nltvhpkfhy kqahdsgtdt scvtfsydgn vlasrggdds lklwdirqfn kplfsasglp
      421 tmfpmtdccf spddklivtg tsiqrgcgsg klvfferrtf qrvyeiditd asvvrclwhp
      481 klnqimvgtg nglakvyydp nksqrgaklc vvktqrkakq aetltqdyii tphalpmfre
      541 prqrstrkql ekdrldplks hkpeppvagp grggrvgthg gtlssyivkn ialdktddsn
      601 preailrhak aaedspywvs paysktqpkt mfaqvesdde eaknepewkk rki
//
LOCUS       NP_001269341             344 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1 regulatory subunit 7 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001269341
VERSION     NP_001269341.1
DBSOURCE    REFSEQ: accession NM_001282412.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Jiang,Y., Scott,K.L., Kwak,S.J., Chen,R. and Mardon,G.
  TITLE     Sds22/PP1 links epithelial integrity and tumor suppression via
            regulation of myosin II and JNK signaling
  JOURNAL   Oncogene 30 (29), 3248-3260 (2011)
   PUBMED   21399659
  REMARK    GeneRIF: human Sds22 is focally deleted and downregulated in
            multiple carcinomas, and this downregulation correlates with tumor
            progression, suggesting that sds22 inactivation may contribute to
            tumorigenesis and metastatic potential
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Posch,M., Khoudoli,G.A., Swift,S., King,E.M., Deluca,J.G. and
            Swedlow,J.R.
  TITLE     Sds22 regulates aurora B activity and microtubule-kinetochore
            interactions at mitosis
  JOURNAL   J Cell Biol 191 (1), 61-74 (2010)
   PUBMED   20921135
  REMARK    GeneRIF: Sds22 specifically defines protein phosphatase 1 function
            and localization in mitosis.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Lesage,B., Beullens,M., Pedelini,L., Garcia-Gimeno,M.A.,
            Waelkens,E., Sanz,P. and Bollen,M.
  TITLE     A complex of catalytically inactive protein phosphatase-1
            sandwiched between Sds22 and inhibitor-3
  JOURNAL   Biochemistry 46 (31), 8909-8919 (2007)
   PUBMED   17630778
  REMARK    GeneRIF: Sds22 and Inhibitor-3 form a heterotrimeric complex with
            PP1, both in cell lysates and after purification. A pool of PP1 is
            complexly controlled by both Sds22 and Inhibitor-3.
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Ceulemans,H., Vulsteke,V., De Maeyer,M., Tatchell,K., Stalmans,W.
            and Bollen,M.
  TITLE     Binding of the concave surface of the Sds22 superhelix to the alpha
            4/alpha 5/alpha 6-triangle of protein phosphatase-1
  JOURNAL   J Biol Chem 277 (49), 47331-47337 (2002)
   PUBMED   12226088
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Ceulemans,H., Van Eynde,A., Perez-Callejon,E., Beullens,M.,
            Stalmans,W. and Bollen,M.
  TITLE     Structure and splice products of the human gene encoding sds22, a
            putative mitotic regulator of protein phosphatase-1
  JOURNAL   Eur J Biochem 262 (1), 36-42 (1999)
   PUBMED   10231361
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Renouf,S., Beullens,M., Wera,S., Van Eynde,A., Sikela,J.,
            Stalmans,W. and Bollen,M.
  TITLE     Molecular cloning of a human polypeptide related to yeast sds22, a
            regulator of protein phosphatase-1
  JOURNAL   FEBS Lett 375 (1-2), 75-78 (1995)
   PUBMED   7498485
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Berry,R., Stevens,T.J., Walter,N.A., Wilcox,A.S., Rubano,T.,
            Hopkins,J.A., Weber,J., Goold,R., Soares,M.B. and Sikela,J.M.
  TITLE     Gene-based sequence-tagged-sites (STSs) as the basis for a human
            gene map
  JOURNAL   Nat Genet 10 (4), 415-423 (1995)
   PUBMED   7670491
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA787059.1, AK308015.1,
            AC005237.2, BC000910.2 and BM676947.1.
            
            Summary: This gene encodes a protein subunit that regulates the
            activity of the serine/threonine phosphatase, protein
            phosphatase-1. The encoded protein is required for completion of
            the mitotic cycle and for targeting protein phosphatase-1 to
            mitotic kinetochores. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (5) uses an alternate 5'
            structure, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon compared to variant 1. The
            encoded protein (isoform 5) is shorter and has a distinct
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.219979.1,
                                           SRR1803612.278288.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..344
                     /product="protein phosphatase 1 regulatory subunit 7
                     isoform 5"
                     /note="protein phosphatase 1 regulatory subunit 22;
                     protein phosphatase 1, regulatory (inhibitor) subunit 7;
                     testis secretory sperm-binding protein Li 210a"
                     /calculated_mol_wt=39700
     Region          <67..182
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          84..105
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          106..127
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          128..149
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          147..338
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          150..171
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..193
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          194..215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          216..237
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          238..259
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          260..281
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..344
                     /gene="PPP1R7"
                     /gene_synonym="SDS22"
                     /coded_by="NM_001282412.1:133..1167"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:5510"
                     /db_xref="HGNC:HGNC:9295"
                     /db_xref="MIM:602877"
ORIGIN      
        1 mvdrrvesee sgdeegkkhs sgivadlseq slkdgeerge edpeeehelp vdmetinldr
       61 daedvdlnhy rigkiegfev lkkvktlclr qnlikcienl eelqslreld lydnqikkie
      121 nlealtelei ldisfnllrn iegvdkltrl kklflvnnki skienlsnlh qlqmlelgsn
      181 riraienidt ltnleslflg knkitklqnl daltnltvls mqsnrltkie glqnlvnlre
      241 lylshngiev ieglennnkl tmldiasnri kkienishlt elqefwmndn lleswsdlde
      301 lkgarsletv ylernplqkd pqyrrkvmla lpsvrqidat fvrf
//
LOCUS       NP_001161288             470 aa            linear   PRI 20-NOV-2025
DEFINITION  cilia- and flagella-associated protein 61 isoform 2 [Homo sapiens].
ACCESSION   NP_001161288
VERSION     NP_001161288.1
DBSOURCE    REFSEQ: accession NM_001167816.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Barbotin,A.L., Boursier,A., Jourdain,A.S., Moerman,A., Rabat,B.,
            Chehimi,M., Thuillier,C., Ghoumid,J. and Smol,T.
  TITLE     Identification of a novel CFAP61 homozygous splicing variant
            associated with multiple morphological abnormalities of the
            flagella
  JOURNAL   J Assist Reprod Genet 41 (6), 1499-1505 (2024)
   PUBMED   38775994
  REMARK    GeneRIF: Identification of a novel CFAP61 homozygous splicing
            variant associated with multiple morphological abnormalities of the
            flagella.
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Zhu,W., Mao,J., Qin,J. and Chen,X.
  TITLE     CFAP61 knockdown aggravates male infertility by inhibiting
            testosterone secretion by Leydig cells via the MAPK/COX-2 pathway
  JOURNAL   Funct Integr Genomics 23 (4), 340 (2023)
   PUBMED   37982895
  REMARK    GeneRIF: CFAP61 knockdown aggravates male infertility by inhibiting
            testosterone secretion by Leydig cells via the MAPK/COX-2 pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Hu,T., Meng,L., Tan,C., Luo,C., He,W.B., Tu,C., Zhang,H., Du,J.,
            Nie,H., Lu,G.X., Lin,G. and Tan,Y.Q.
  TITLE     Biallelic CFAP61 variants cause male infertility in humans and mice
            with severe oligoasthenoteratozoospermia
  JOURNAL   J Med Genet 60 (2), 144-153 (2023)
   PUBMED   35387802
  REMARK    GeneRIF: Biallelic CFAP61 variants cause male infertility in humans
            and mice with severe oligoasthenoteratozoospermia.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Ma,A., Zeb,A., Ali,I., Zhao,D., Khan,A., Zhang,B., Zhou,J.,
            Khan,R., Zhang,H., Zhang,Y., Khan,I., Shah,W., Ali,H., Javed,A.R.,
            Ma,H. and Shi,Q.
  TITLE     Biallelic Variants in CFAP61 Cause Multiple Morphological
            Abnormalities of the Flagella and Male Infertility
  JOURNAL   Front Cell Dev Biol 9, 803818 (2022)
   PUBMED   35174165
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Liu,S., Zhang,J., Kherraf,Z.E., Sun,S., Zhang,X., Cazin,C.,
            Coutton,C., Zouari,R., Zhao,S., Hu,F., Fourati Ben Mustapha,S.,
            Arnoult,C., Ray,P.F. and Liu,M.
  TITLE     CFAP61 is required for sperm flagellum formation and male fertility
            in human and mouse
  JOURNAL   Development 148 (23) (2021)
   PUBMED   34792097
  REMARK    GeneRIF: CFAP61 is required for sperm flagellum formation and male
            fertility in human and mouse.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Huang,T., Yin,Y., Liu,C., Li,M., Yu,X., Wang,X., Zhang,H.,
            Muhammad,T., Gao,F., Li,W., Chen,Z.J., Liu,H. and Ma,J.
  TITLE     Absence of murine CFAP61 causes male infertility due to multiple
            morphological abnormalities of the flagella
  JOURNAL   Sci Bull (Beijing) 65 (10), 854-864 (2020)
   PUBMED   36659204
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Blackburn,K., Bustamante-Marin,X., Yin,W., Goshe,M.B. and
            Ostrowski,L.E.
  TITLE     Quantitative Proteomic Analysis of Human Airway Cilia Identifies
            Previously Uncharacterized Proteins of High Abundance
  JOURNAL   J Proteome Res 16 (4), 1579-1592 (2017)
   PUBMED   28282151
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Dymek,E.E. and Smith,E.F.
  TITLE     A conserved CaM- and radial spoke associated complex mediates
            regulation of flagellar dynein activity
  JOURNAL   J Cell Biol 179 (3), 515-526 (2007)
   PUBMED   17967944
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL035454.18, AL117439.1 and AL049648.9.
            
            Transcript Variant: This variant (2) has multiple differences,
            compared to variant 1. The encoded isoform (2) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL117439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..470
                     /product="cilia- and flagella-associated protein 61
                     isoform 2"
                     /calculated_mol_wt=53420
     Region          17..266
                     /region_name="CFAP61_N"
                     /note="Cilia- and flagella-associated protein 61,
                     N-terminal domain; pfam16092"
                     /db_xref="CDD:465016"
     Region          278..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHU2.3)"
     CDS             1..470
                     /gene="CFAP61"
                     /gene_synonym="C20orf26; CaM-IP3; dJ1002M8.3; dJ1178H5.4;
                     SPGF84"
                     /coded_by="NM_001167816.1:9..1421"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54452.1"
                     /db_xref="GeneID:26074"
                     /db_xref="HGNC:HGNC:15872"
                     /db_xref="MIM:620381"
ORIGIN      
        1 msvltsprgk vevvhcrrte sqdvyciksl irkftcklfg klniiyllek anlavtlcnd
       61 keeimaqatf ldypnwnvak qddwvsvfre ldsdipctpl ntlfmhlfva vdeysvgcck
      121 eilrtvykav pelhfifliv psymslgstl itvfdqvgni pcltyeedfa vhichrhshy
      181 pqlhvrkarv edhddlmpif mrydtilket ygeyflaeli eaqdeenhav vcevegtavg
      241 fmsvcsrvnm qllhecfdlg pfhglcfphp ddvlespqdl svrrsqdael rsssqgsqki
      301 veelqepvsp dtmeniqgni areaaseeal tavqsgnvse pedieklsdi stgyaqyhhv
      361 ssrslaslvl peepvhfrpi yrgasaafci qlfcidekye arsldfmnfv fslfsdknfc
      421 vislphltpe ffliqnfvkm vpfntctleq dlyvfhragl lkniclgrss
//
LOCUS       NP_908932                364 aa            linear   PRI 20-NOV-2025
DEFINITION  fructose-bisphosphate aldolase A isoform 1 [Homo sapiens].
ACCESSION   NP_908932
VERSION     NP_908932.1
DBSOURCE    REFSEQ: accession NM_184043.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Xu,Z., Lv,C., Gao,J., Cui,Y., Liu,W., He,Z. and He,L.
  TITLE     LncRNA ACVR2B-as1 interacts with ALDOA to regulate the self-renewal
            and apoptosis of human spermatogonial stem cells by controlling
            glycolysis activity
  JOURNAL   Cell Mol Life Sci 81 (1), 391 (2024)
   PUBMED   39254854
  REMARK    GeneRIF: LncRNA ACVR2B-as1 interacts with ALDOA to regulate the
            self-renewal and apoptosis of human spermatogonial stem cells by
            controlling glycolysis activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Yeh,C.Y., Cai,H.Y., Kuo,H.H., Lin,Y.Y., He,Z.J., Cheng,H.C.,
            Yang,C.J., Huang,C.F. and Chang,Y.C.
  TITLE     ALDOA coordinates PDE3A through the beta-catenin/ID3 axis to
            stimulate cancer metastasis and M2 polarization in lung cancer with
            EGFR mutations
  JOURNAL   Biochem Biophys Res Commun 696, 149489 (2024)
   PUBMED   38244313
  REMARK    GeneRIF: ALDOA coordinates PDE3A through the beta-catenin/ID3 axis
            to stimulate cancer metastasis and M2 polarization in lung cancer
            with EGFR mutations.
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Mukai,T., Arai,Y., Yatsuki,H., Joh,K. and Hori,K.
  TITLE     An additional promoter functions in the human aldolase A gene, but
            not in rat
  JOURNAL   Eur J Biochem 195 (3), 781-787 (1991)
   PUBMED   1999195
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Izzo,P., Costanzo,P., Lupo,A., Rippa,E., Paolella,G. and
            Salvatore,F.
  TITLE     Human aldolase A gene. Structural organization and tissue-specific
            expression by multiple promoters and alternate mRNA processing
  JOURNAL   Eur J Biochem 174 (4), 569-578 (1988)
   PUBMED   3391172
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Kishi,H., Mukai,T., Hirono,A., Fujii,H., Miwa,S. and Hori,K.
  TITLE     Human aldolase A deficiency associated with a hemolytic anemia:
            thermolabile aldolase due to a single base mutation
  JOURNAL   Proc Natl Acad Sci U S A 84 (23), 8623-8627 (1987)
   PUBMED   2825199
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Maire,P., Gautron,S., Hakim,V., Gregori,C., Mennecier,F. and
            Kahn,A.
  TITLE     Characterization of three optional promoters in the 5' region of
            the human aldolase A gene
  JOURNAL   J Mol Biol 197 (3), 425-438 (1987)
   PUBMED   3441006
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Sakakibara,M., Mukai,T. and Hori,K.
  TITLE     Nucleotide sequence of a cDNA clone for human aldolase: a messenger
            RNA in the liver
  JOURNAL   Biochem Biophys Res Commun 131 (1), 413-420 (1985)
   PUBMED   3840020
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Rehbein-Thoner,M. and Pfleiderer,G.
  TITLE     The changes in aldolase isoenzyme pattern during development of the
            human kidney and small intestine--demonstrated in organ extracts
            and tissue sections
  JOURNAL   Hoppe Seylers Z Physiol Chem 358 (2), 169-180 (1977)
   PUBMED   844801
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Pfleiderer,G., Thoner,M. and Wachsmuth,E.D.
  TITLE     Histological examination of the aldolase monomer composition of
            cells from human kidney and hypernephroid carcinoma
  JOURNAL   Beitr Pathol 156 (3), 266-279 (1975)
   PUBMED   766744
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB151262.1, DA564075.1,
            BC013614.1 and BU855133.1.
            
            Summary: This gene encodes a member of the class I
            fructose-bisphosphate aldolase protein family. The encoded protein
            is a glycolytic enzyme that catalyzes the reversible conversion of
            fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and
            dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C),
            encoded by three different genes, are differentially expressed
            during development. Mutations in this gene have been associated
            with Glycogen Storage Disease XII, an autosomal recessive disorder
            associated with hemolytic anemia. Disruption of this gene also
            plays a role in the progression of multiple types of cancers.
            Related pseudogenes have been identified on chromosomes 3 and 10.
            [provided by RefSeq, Sep 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 2, 3, 4, 7, 8, 9, and 10 encode the
            same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.391428.1,
                                           SRR1803614.274350.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..364
                     /product="fructose-bisphosphate aldolase A isoform 1"
                     /EC_number="4.1.2.13"
                     /note="fructose-1,6-bisphosphate triosephosphate-lyase;
                     muscle-type aldolase; lung cancer antigen NY-LU-1;
                     epididymis secretory sperm binding protein Li 87p;
                     aldolase A, fructose-bisphosphate"
                     /calculated_mol_wt=39289
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P05065; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Region          15..364
                     /region_name="Glycolytic"
                     /note="Fructose-bisphosphate aldolase class-I; pfam00274"
                     /db_xref="CDD:459742"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P04075.2)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04075.2)"
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            111
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P09972; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P05065; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            330
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04075.2)"
     Site            364
                     /site_type="other"
                     /note="Necessary for preference for fructose
                     1,6-bisphosphate over fructose 1-phosphate; propagated
                     from UniProtKB/Swiss-Prot (P04075.2)"
     CDS             1..364
                     /gene="ALDOA"
                     /gene_synonym="ALDA; GSD12; HEL-S-87p"
                     /coded_by="NM_184043.2:249..1343"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10668.1"
                     /db_xref="GeneID:226"
                     /db_xref="HGNC:HGNC:414"
                     /db_xref="MIM:103850"
ORIGIN      
        1 mpyqypaltp eqkkelsdia hrivapgkgi laadestgsi akrlqsigte nteenrrfyr
       61 qllltaddrv npciggvilf hetlyqkadd grpfpqviks kggvvgikvd kgvvplagtn
      121 getttqgldg lsercaqykk dgadfakwrc vlkigehtps alaimenanv laryasicqq
      181 ngivpivepe ilpdgdhdlk rcqyvtekvl aavykalsdh hiylegtllk pnmvtpghac
      241 tqkfsheeia matvtalrrt vppavtgitf lsggqseeea sinlnainkc pllkpwaltf
      301 sygralqasa lkawggkken lkaaqeeyvk ralanslacq gkytpsgqag aaaseslfvs
      361 nhay
//
LOCUS       NP_001924                453 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydrolipoyllysine-residue succinyltransferase component of
            2-oxoglutarate dehydrogenase complex, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001924
VERSION     NP_001924.2
DBSOURCE    REFSEQ: accession NM_001933.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Anderson,N.M., Qin,X., Finan,J.M., Lam,A., Athoe,J., Missiaen,R.,
            Skuli,N., Kennedy,A., Saini,A.S., Tao,T., Zhu,S., Nissim,I.,
            Look,A.T., Qing,G., Simon,M.C. and Feng,H.
  TITLE     Metabolic Enzyme DLST Promotes Tumor Aggression and Reveals a
            Vulnerability to OXPHOS Inhibition in High-Risk Neuroblastoma
  JOURNAL   Cancer Res 81 (17), 4417-4430 (2021)
   PUBMED   34233924
  REMARK    GeneRIF: Metabolic Enzyme DLST Promotes Tumor Aggression and
            Reveals a Vulnerability to OXPHOS Inhibition in High-Risk
            Neuroblastoma.
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Buffet,A., Zhang,J., Rebel,H., Corssmit,E.P.M., Jansen,J.C.,
            Hensen,E.F., Bovee,J.V.M.G., Morini,A., Gimenez-Roqueplo,A.P.,
            Hes,F.J., Devilee,P., Favier,J. and Bayley,J.P.
  TITLE     Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma
  JOURNAL   J Clin Endocrinol Metab 106 (2), 459-471 (2021)
   PUBMED   33180916
  REMARK    GeneRIF: Germline DLST Variants Promote Epigenetic Modifications in
            Pheochromocytoma-Paraganglioma.
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Chuang,D.T., Fisher,C.W., Lau,K.S., Griffin,T.A., Wynn,R.M. and
            Cox,R.P.
  TITLE     Maple syrup urine disease: domain structure, mutations and exon
            skipping in the dihydrolipoyl transacylase (E2) component of the
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   Mol Biol Med 8 (1), 49-63 (1991)
   PUBMED   1943690
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Fregeau,D.R., Prindiville,T., Coppel,R.L., Kaplan,M., Dickson,E.R.
            and Gershwin,M.E.
  TITLE     Inhibition of alpha-ketoglutarate dehydrogenase activity by a
            distinct population of autoantibodies recognizing dihydrolipoamide
            succinyltransferase in primary biliary cirrhosis
  JOURNAL   Hepatology 11 (6), 975-981 (1990)
   PUBMED   2365294
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Ono,K., Hakozaki,M., Kimura,A. and Kochi,H.
  TITLE     Purification, resolution, and reconstitution of rat liver
            branched-chain alpha-keto acid dehydrogenase complex
  JOURNAL   J Biochem 101 (1), 19-27 (1987)
   PUBMED   3571202
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Kochi,H., Seino,H. and Ono,K.
  TITLE     Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate,
            and branched-chain alpha-keto acids in rat liver mitochondria:
            presence of interaction between the glycine cleavage system and
            alpha-keto acid dehydrogenase complexes
  JOURNAL   Arch Biochem Biophys 249 (2), 263-272 (1986)
   PUBMED   3753002
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289414.1, CX163292.1,
            CN422511.1, BM929953.1 and AI087261.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_001924.1.
            
            Summary: This gene encodes a mitochondrial protein that belongs to
            the 2-oxoacid dehydrogenase family. This protein is one of the
            three components (the E2 component) of the 2-oxoglutarate
            dehydrogenase complex that catalyzes the overall conversion of
            2-oxoglutarate to succinyl-CoA and CO(2). Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000302.2, SRR3476690.920610.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000334220.9/
                                                  ENSP00000335304.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..453
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 1 precursor"
                     /EC_number="2.3.1.61"
                     /note="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial; E2K; OGDC-E2; dihydrolipoamide
                     S-succinyltransferase (E2 component of 2-oxo-glutarate
                     complex)"
                     /calculated_mol_wt=41390
     transit_peptide 1..67
                     /calculated_mol_wt=7384
     mat_peptide     68..453
                     /product="dihydrolipoyllysine-residue succinyltransferase
                     component of 2-oxoglutarate dehydrogenase complex,
                     mitochondrial isoform 1"
                     /calculated_mol_wt=41390
     Region          71..453
                     /region_name="sucB"
                     /note="2-oxoglutarate dehydrogenase complex
                     dihydrolipoamide succinyltransferase (E2 component);
                     TIGR01347"
                     /db_xref="CDD:273565"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Region          152..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36957.4)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            272
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            273
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            277
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D2G2; propagated from
                     UniProtKB/Swiss-Prot (P36957.4)"
     CDS             1..453
                     /gene="DLST"
                     /gene_synonym="DLTS; KGD2; PGL7; PPGL7"
                     /coded_by="NM_001933.5:39..1400"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9833.1"
                     /db_xref="GeneID:1743"
                     /db_xref="HGNC:HGNC:2911"
                     /db_xref="MIM:126063"
ORIGIN      
        1 mlsrsrcvsr afsrslsafq kgncplgrrs lpgvslcqgp gypnsrkvvi nnsvfsvrff
       61 rttavckddl vtvktpafae svtegdvrwe kavgdtvaed evvceietdk tsvqvpspan
      121 gvieallvpd ggkveggtpl ftlrktgaap akakpaeapa aaapkaepta aavpppaapi
      181 ptqmppvpsp sqppsgkpvs avkptvappl aepgagkglr sehrekmnrm rqriaqrlke
      241 aqntcamltt fneidmsniq emrarhkeaf lkkhnlklgf msafvkasaf alqeqpvvna
      301 viddttkevv yrdyidisva vatprglvvp virnveamnf adiertitel gekarknela
      361 iedmdggtft isnggvfgsl fgtpiinppq sailgmhgif drpvaiggkv evrpmmyval
      421 tydhrlidgr eavtflrkik aavedprvll ldl
//
LOCUS       NP_054885                270 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 4 isoform 1
            [Homo sapiens].
ACCESSION   NP_054885
VERSION     NP_054885.1
DBSOURCE    REFSEQ: accession NM_014166.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Conaway,J.W., Florens,L., Sato,S., Tomomori-Sato,C., Parmely,T.J.,
            Yao,T., Swanson,S.K., Banks,C.A., Washburn,M.P. and Conaway,R.C.
  TITLE     The mammalian Mediator complex
  JOURNAL   FEBS Lett 579 (4), 904-908 (2005)
   PUBMED   15680972
  REMARK    Review article
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Malik,S., Gu,W., Wu,W., Qin,J. and Roeder,R.G.
  TITLE     The USA-derived transcriptional coactivator PC2 is a submodule of
            TRAP/SMCC and acts synergistically with other PCs
  JOURNAL   Mol Cell 5 (4), 753-760 (2000)
   PUBMED   10882111
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Rachez,C., Lemon,B.D., Suldan,Z., Bromleigh,V., Gamble,M.,
            Naar,A.M., Erdjument-Bromage,H., Tempst,P. and Freedman,L.P.
  TITLE     Ligand-dependent transcription activation by nuclear receptors
            requires the DRIP complex
  JOURNAL   Nature 398 (6730), 824-828 (1999)
   PUBMED   10235266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001934.1, AL158196.24 and
            AI613470.1.
            
            Summary: This gene encodes a component of the Mediator complex. The
            Mediator complex interacts with DNA-binding gene-specific
            transcription factors to modulate transcription by RNA polymerase
            II. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Jul
            2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.180219.1,
                                           SRR1660807.147776.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258648.7/ ENSP00000258648.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..270
                     /product="mediator of RNA polymerase II transcription
                     subunit 4 isoform 1"
                     /note="mediator of RNA polymerase II transcription subunit
                     4; activator-recruited cofactor 36 kDa component; vitamin
                     D3 receptor-interacting protein complex 36 kDa component;
                     mediator, 34-kD subunit, homolog; vitamin D
                     receptor-interacting protein, 36-kD"
                     /calculated_mol_wt=29614
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ6.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ6.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NPJ6.1)"
     Region          64..>189
                     /region_name="Med4"
                     /note="Vitamin-D-receptor interacting Mediator subunit 4;
                     pfam10018"
                     /db_xref="CDD:401849"
     Region          226..270
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ6.1)"
     CDS             1..270
                     /gene="MED4"
                     /gene_synonym="ARC36; DRIP36; HSPC126; TRAP36; VDRIP"
                     /coded_by="NM_014166.4:27..839"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9408.1"
                     /db_xref="GeneID:29079"
                     /db_xref="HGNC:HGNC:17903"
                     /db_xref="MIM:605718"
ORIGIN      
        1 maasssgeke kerlggglgv aggnstrerl lsaledlevl sreliemlai srnqkllqag
       61 eenqvlelli hrdgefqelm klalnqgkih hemqvlekev ekrdsdiqql qkqlkeaeqi
      121 latavyqake klksiekark gaisseeiik yahrisasna vcapltwvpg dprrpyptdl
      181 emrsgllgqm nnpstngvng hlpgdalaag rlpdvlapqy pwqsndmsmn mlppnhssdf
      241 lleppghnke neddveimst dssssssesd
//
LOCUS       NP_009048                242 aa            linear   PRI 20-NOV-2025
DEFINITION  thyrotropin releasing hormone preproprotein [Homo sapiens].
ACCESSION   NP_009048
VERSION     NP_009048.1
DBSOURCE    REFSEQ: accession NM_007117.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Gao,Y., Zhou,J.F., Mao,J.Y., Jiang,L. and Li,X.P.
  TITLE     Identification of the Thyrotropin-Releasing Hormone (TRH) as a
            Novel Biomarker in the Prognosis for Acute Myeloid Leukemia
  JOURNAL   Biomolecules 12 (10), 1359 (2022)
   PUBMED   36291567
  REMARK    GeneRIF: Identification of the Thyrotropin-Releasing Hormone (TRH)
            as a Novel Biomarker in the Prognosis for Acute Myeloid Leukemia.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Duan,J., Xu,P., Luan,X., Ji,Y., He,X., Song,N., Yuan,Q., Jin,Y.,
            Cheng,X., Jiang,H., Zheng,J., Zhang,S., Jiang,Y. and Xu,H.E.
  TITLE     Hormone- and antibody-mediated activation of the thyrotropin
            receptor
  JOURNAL   Nature 609 (7928), 854-859 (2022)
   PUBMED   35940204
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Kent,N.L., Young,S.L., Akison,L.K. and Cuffe,J.S.M.
  TITLE     Is the link between elevated TSH and gestational diabetes mellitus
            dependant on diagnostic criteria and thyroid antibody status: a
            systematic review and meta-analysis
  JOURNAL   Endocrine 74 (1), 38-49 (2021)
   PUBMED   33991314
  REMARK    GeneRIF: Is the link between elevated TSH and gestational diabetes
            mellitus dependant on diagnostic criteria and thyroid antibody
            status: a systematic review and meta-analysis.
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Puttipanyalears,C., Arayataweegool,A., Chalertpet,K.,
            Rattanachayoto,P., Mahattanasakul,P., Tangjaturonsasme,N.,
            Kerekhanjanarong,V., Mutirangura,A. and Kitkumthorn,N.
  TITLE     TRH site-specific methylation in oral and oropharyngeal squamous
            cell carcinoma
  JOURNAL   BMC Cancer 18 (1), 786 (2018)
   PUBMED   30081853
  REMARK    GeneRIF: cg01009664 of TRH as a potential biomarker for oral
            squamous cell carcinoma and oropharyngeal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Nillni,E.A.
  TITLE     Regulation of the hypothalamic thyrotropin releasing hormone (TRH)
            neuron by neuronal and peripheral inputs
  JOURNAL   Front Neuroendocrinol 31 (2), 134-156 (2010)
   PUBMED   20074584
  REMARK    Review article
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Yamada,M., Iwasaki,T., Satoh,T., Monden,T., Konaka,S., Murakami,M.,
            Iriuchijima,T. and Mori,M.
  TITLE     Activation of the thyrotropin-releasing hormone (TRH) receptor by a
            direct precursor of TRH, TRH-Gly
  JOURNAL   Neurosci Lett 196 (1-2), 109-112 (1995)
   PUBMED   7501234
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Pekary,A.E., Gwirtsman,H., Tourtellotte,W.W., Smith,V.P. and
            Hershman,J.M.
  TITLE     High levels of thyrotropin-releasing hormone precursor peptide
            immunoreactivity and binding substance occur in human cerebrospinal
            fluid
  JOURNAL   Neuroendocrinology 53 (3), 246-252 (1991)
   PUBMED   1904138
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Yamada,M., Wondisford,F.E., Radovick,S., Nakayama,Y.,
            Weintraub,B.D. and Wilber,J.F.
  TITLE     Assignment of human preprothyrotropin-releasing hormone (TRH) gene
            to chromosome 3
  JOURNAL   Somat Cell Mol Genet 17 (1), 97-100 (1991)
   PUBMED   1900134
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Yamada,M., Radovick,S., Wondisford,F.E., Nakayama,Y.,
            Weintraub,B.D. and Wilber,J.F.
  TITLE     Cloning and structure of human genomic DNA and hypothalamic cDNA
            encoding human prepro thyrotropin-releasing hormone
  JOURNAL   Mol Endocrinol 4 (4), 551-556 (1990)
   PUBMED   2126343
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313473.1 and AC083906.23.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the thyrotropin-releasing
            hormone family. Cleavage of the encoded proprotein releases mature
            thyrotropin-releasing hormone, which is a tripeptide hypothalamic
            regulatory hormone. The human proprotein contains six
            thyrotropin-releasing hormone tripeptides. Thyrotropin-releasing
            hormone is involved in the regulation and release of
            thyroid-stimulating hormone, as well as prolactin. Deficiency of
            this hormone has been associated with hypothalamic hypothyroidism.
            [provided by RefSeq, May 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110515.2, AK313473.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302649.4/ ENSP00000303452.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.1"
     Protein         1..242
                     /product="thyrotropin releasing hormone preproprotein"
                     /note="prothyroliberin; protirelin; TSH-releasing factor;
                     thyrotropin-releasing factor; pro-thyrotropin-releasing
                     hormone"
                     /calculated_mol_wt=24990
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2432
     Region          18..202
                     /region_name="TRH"
                     /note="Thyrotropin-releasing hormone (TRH); pfam05438"
                     /db_xref="CDD:461653"
     proprotein      25..242
                     /product="prothyrotropin releasing hormone"
                     /calculated_mol_wt=24990
     mat_peptide     84..86
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     mat_peptide     114..116
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     mat_peptide     135..137
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     mat_peptide     152..154
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     mat_peptide     186..188
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     mat_peptide     227..229
                     /product="thyrotropin releasing hormone"
                     /calculated_mol_wt=380
     CDS             1..242
                     /gene="TRH"
                     /gene_synonym="Pro-TRH; TRF"
                     /coded_by="NM_007117.5:113..841"
                     /db_xref="CCDS:CCDS3066.1"
                     /db_xref="GeneID:7200"
                     /db_xref="HGNC:HGNC:12298"
                     /db_xref="MIM:613879"
ORIGIN      
        1 mpgpwlllal altlnltgvp ggraqpeaaq qeavtaaehp glddflrqve rllflreniq
       61 rlqgdqgehs asqifqsdwl skrqhpgkre eeeeegveee eeeeggavgp hkrqhpgrre
      121 deaswsvdvt qhkrqhpgrr spwlayavpk rqhpgrrlad pkaqrsweee eeeeereedl
      181 mpekrqhpgk ralggpcgpq gaygqaglll gllddlsrsq gaeekrqhpg rraawvrepl
      241 ee
//
LOCUS       NP_065170                369 aa            linear   PRI 20-NOV-2025
DEFINITION  aspartate beta-hydroxylase domain-containing protein 2 [Homo
            sapiens].
ACCESSION   NP_065170
VERSION     NP_065170.2
DBSOURCE    REFSEQ: accession NM_020437.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z99714.2 and AL161993.1.
            
            On Jul 19, 2008 this sequence version replaced NP_065170.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.261045.1,
                                           SRR1163658.167493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215906.6/ ENSP00000215906.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..369
                     /product="aspartate beta-hydroxylase domain-containing
                     protein 2"
                     /calculated_mol_wt=41568
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ICH7.1)"
     Region          192..351
                     /region_name="Asp_Arg_Hydrox"
                     /note="Aspartyl/Asparaginyl beta-hydroxylase; pfam05118"
                     /db_xref="CDD:461552"
     Site            211
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6ICH7.1)"
     CDS             1..369
                     /gene="ASPHD2"
                     /coded_by="NM_020437.5:452..1561"
                     /db_xref="CCDS:CCDS13834.2"
                     /db_xref="GeneID:57168"
                     /db_xref="HGNC:HGNC:30437"
ORIGIN      
        1 mvwaplgppr tdcltllhtp skdspkmsle wlvawswsld glrdciatgi qsvrdcdtta
       61 vitvacllvl fvwycyhvgr eqprpyvsvn slmqaadang lqngyvycqs pecvrcthne
      121 glnqklyhnl qeyakrysws gmgrihkgir eqgrylnsrp siqkpevffl pdlpttpyfs
      181 rdaqkhdvev lernfqtilc efetlykafs ncslpqgwkm nstpsgewft fylvnqgvcv
      241 prncrkcprt yrllgslrtc ignnvfgnac isvlspgtvi tehygptnir irchlglktp
      301 ngcelvvgge pqcwaegrcl lfddsflhaa fhegsaedgp rvvfmvdlwh pnvaaaerqa
      361 ldfifapgr
//
LOCUS       NP_579808                209 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin alpha Fc receptor isoform f [Homo sapiens].
ACCESSION   NP_579808
VERSION     NP_579808.1
DBSOURCE    REFSEQ: accession NM_133274.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Liu,Q. and Stadtmueller,B.M.
  TITLE     SIgA structures bound to Streptococcus pyogenes M4 and human CD89
            provide insights into host-pathogen interactions
  JOURNAL   Nat Commun 14 (1), 6726 (2023)
   PUBMED   37872175
  REMARK    GeneRIF: SIgA structures bound to Streptococcus pyogenes M4 and
            human CD89 provide insights into host-pathogen interactions.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Wu,H., Wang,X., Yang,Z., Zhao,Q., Wen,Y., Li,X., Zhang,W. and
            Gao,R.
  TITLE     Serum Soluble CD89-IgA Complexes Are Elevated in IgA Nephropathy
            without Immunosuppressant History
  JOURNAL   Dis Markers 2020, 8393075 (2020)
   PUBMED   32076466
  REMARK    GeneRIF: Serum Soluble CD89-IgA Complexes Are Elevated in IgA
            Nephropathy without Immunosuppressant History.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Pleass,R.J., Andrews,P.D., Kerr,M.A. and Woof,J.M.
  TITLE     Alternative splicing of the human IgA Fc receptor CD89 in
            neutrophils and eosinophils
  JOURNAL   Biochem J 318 (Pt 3) (Pt 3), 771-777 (1996)
   PUBMED   8836118
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Patry,C., Sibille,Y., Lehuen,A. and Monteiro,R.C.
  TITLE     Identification of Fc alpha receptor (CD89) isoforms generated by
            alternative splicing that are differentially expressed between
            blood monocytes and alveolar macrophages
  JOURNAL   J Immunol 156 (11), 4442-4448 (1996)
   PUBMED   8666819
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Morton,H.C., Schiel,A.E., Janssen,S.W. and van de Winkel,J.G.
  TITLE     Alternatively spliced forms of the human myeloid Fc alpha receptor
            (CD89) in neutrophils
  JOURNAL   Immunogenetics 43 (4), 246-247 (1996)
   PUBMED   8575829
REFERENCE   7  (residues 1 to 209)
  AUTHORS   de Wit,T.P., Morton,H.C., Capel,P.J. and van de Winkel,J.G.
  TITLE     Structure of the gene for the human myeloid IgA Fc receptor (CD89)
  JOURNAL   J Immunol 155 (3), 1203-1209 (1995)
   PUBMED   7636188
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Kremer,E.J., Kalatzis,V., Baker,E., Callen,D.F., Sutherland,G.R.
            and Maliszewski,C.R.
  TITLE     The gene for the human IgA Fc receptor maps to 19q13.4
  JOURNAL   Hum Genet 89 (1), 107-108 (1992)
   PUBMED   1577457
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Maliszewski,C.R., March,C.J., Schoenborn,M.A., Gimpel,S. and
            Shen,L.
  TITLE     Expression cloning of a human Fc receptor for IgA
  JOURNAL   J Exp Med 172 (6), 1665-1672 (1990)
   PUBMED   2258698
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Kimata,H. and Saxon,A.
  TITLE     Subset of natural killer cells is induced by immune complexes to
            display Fc receptors for IgE and IgA and demonstrates isotype
            regulatory function
  JOURNAL   J Clin Invest 82 (1), 160-167 (1988)
   PUBMED   2455732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290922.1, D87857.1 and
            AC245128.3.
            
            Summary: This gene is a member of the immunoglobulin gene
            superfamily and encodes a receptor for the Fc region of IgA. The
            receptor is a transmembrane glycoprotein present on the surface of
            myeloid lineage cells such as neutrophils, monocytes, macrophages,
            and eosinophils, where it mediates immunologic responses to
            pathogens. It interacts with IgA-opsonized targets and triggers
            several immunologic defense processes, including phagocytosis,
            antibody-dependent cell-mediated cytotoxicity, and stimulation of
            the release of inflammatory mediators. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6, also known as U09) lacks an
            in-frame exon in the 5' coding region and uses an alternate splice
            site in the 3' coding region, which results in a frameshift,
            compared to variant 1. The encoded isoform (f) has a distinct
            C-terminus and is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D87857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..209
                     /product="immunoglobulin alpha Fc receptor isoform f"
                     /note="immunoglobulin alpha Fc receptor; Fc fragment of
                     IgA, receptor for; Fc fragment of IgA receptor"
                     /calculated_mol_wt=23263
     Region          16..107
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          17..21
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          25..28
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          31..38
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          45..50
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(49,89,96)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          60..63
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          72..76
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          84..90
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          100..107
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          113..>180
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          130..134
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          143..147
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          164..168
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..209
                     /gene="FCAR"
                     /gene_synonym="CD89; CTB-61M7.2; FcalphaR; FcalphaRI"
                     /coded_by="NM_133274.4:56..685"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS42625.1"
                     /db_xref="GeneID:2204"
                     /db_xref="HGNC:HGNC:3608"
                     /db_xref="MIM:147045"
ORIGIN      
        1 mdpkqttllc lgdfpmpfis aksspvipld gsvkiqcqai reayltqlmi iknstyreig
       61 rrlkfwnetd pefvidhmda nkagryqcqy righyrfrys dtlelvvtgl ygkpflsadr
      121 glvlmpgeni sltcssahip fdrfslakeg elslpqhqsg ehpanfslgp vdlnvsgiyr
      181 lhpprlhdae ldphgrgrtg prgslghtg
//
LOCUS       NP_001336188             817 aa            linear   PRI 20-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 3 isoform 5 [Homo sapiens].
ACCESSION   NP_001336188
VERSION     NP_001336188.1
DBSOURCE    REFSEQ: accession NM_001349259.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Wu,D., Zhao,L., Feng,Z., Yu,C., Ding,J., Wang,L., Wang,F., Liu,D.,
            Zhu,H., Xing,F., Conaway,J.W., Conaway,R.C., Cai,Y. and Jin,J.
  TITLE     O-Linked N-acetylglucosamine transferase 1 regulates global histone
            H4 acetylation via stabilization of the nonspecific lethal protein
            NSL3
  JOURNAL   J Biol Chem 292 (24), 10014-10025 (2017)
   PUBMED   28450392
  REMARK    GeneRIF: Data suggest that O-GlcNAc transferase 1 (OGT1)
            specifically binds to, O-GlcNAcylates, and stabilizes nonspecific
            lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates
            global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16.
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Chatterjee,A., Seyfferth,J., Lucci,J., Gilsbach,R., Preissl,S.,
            Bottinger,L., Martensson,C.U., Panhale,A., Stehle,T., Kretz,O.,
            Sahyoun,A.H., Avilov,S., Eimer,S., Hein,L., Pfanner,N., Becker,T.
            and Akhtar,A.
  TITLE     MOF Acetyl Transferase Regulates Transcription and Respiration in
            Mitochondria
  JOURNAL   Cell 167 (3), 722-738 (2016)
   PUBMED   27768893
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Meunier,S., Shvedunova,M., Van Nguyen,N., Avila,L., Vernos,I. and
            Akhtar,A.
  TITLE     An epigenetic regulator emerges as microtubule minus-end binding
            and stabilizing factor in mitosis
  JOURNAL   Nat Commun 6, 7889 (2015)
   PUBMED   26243146
  REMARK    GeneRIF: microtubule minus-end-binding protein, essential for
            spindle assembly and chromosome segregation
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Zhao,X., Su,J., Wang,F., Liu,D., Ding,J., Yang,Y., Conaway,J.W.,
            Conaway,R.C., Cao,L., Wu,D., Wu,M., Cai,Y. and Jin,J.
  TITLE     Crosstalk between NSL histone acetyltransferase and MLL/SET
            complexes: NSL complex functions in promoting histone H3K4
            di-methylation activity by MLL/SET complexes
  JOURNAL   PLoS Genet 9 (11), e1003940 (2013)
   PUBMED   24244196
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Rea,S., Xouri,G. and Akhtar,A.
  TITLE     Males absent on the first (MOF): from flies to humans
  JOURNAL   Oncogene 26 (37), 5385-5394 (2007)
   PUBMED   17694080
  REMARK    Review article
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Mendjan,S., Taipale,M., Kind,J., Holz,H., Gebhardt,P., Schelder,M.,
            Vermeulen,M., Buscaino,A., Duncan,K., Mueller,J., Wilm,M.,
            Stunnenberg,H.G., Saumweber,H. and Akhtar,A.
  TITLE     Nuclear pore components are involved in the transcriptional
            regulation of dosage compensation in Drosophila
  JOURNAL   Mol Cell 21 (6), 811-823 (2006)
   PUBMED   16543150
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079754.4.
            
            Transcript Variant: This variant (11) differs in the 5' UTR,
            contains an alternate exon in the 3' coding region, and initiates
            translation from a downstream start codon, compared to variant 1.
            The encoded isoform (5) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.131379.1,
                                           SRR18074969.979660.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..817
                     /product="KAT8 regulatory NSL complex subunit 3 isoform 5"
                     /note="serum inhibited-related protein; testis development
                     protein PRTD; NSL complex protein NSL3; non-specific
                     lethal 3 homolog"
                     /calculated_mol_wt=85987
     Region          <236..385
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
     CDS             1..817
                     /gene="KANSL3"
                     /gene_synonym="KIAA1310; NSL3; Rcd1"
                     /coded_by="NM_001349259.2:403..2856"
                     /note="isoform 5 is encoded by transcript variant 11"
                     /db_xref="GeneID:55683"
                     /db_xref="HGNC:HGNC:25473"
                     /db_xref="MIM:617742"
ORIGIN      
        1 mplydnqkar svmnecerhv ifartdadap pppedweehv nrtgwtmaqn klfnkilkal
       61 qsdrlarlan egacnepvlr rvavdkcarr vrqalasvsw dtkliqwlht tlvetlslpm
      121 laayldalqt lkgkiptlid rmlvssntkt gaagaealsl llkrpwdpav gvlshnkpsk
      181 lpgsplilia ssgpsssvfp tsrrhrfwqs qlsclgkvip vathllnngs gvgvlqcleh
      241 migavrskvl eihshfphkp iiligwntga lvachvsvme yvtavvclgf plltvdgprg
      301 dvddplldmk tpvlfvigqn slqchpeame dfrekiraen slvvvggadd nlriskakkk
      361 segltqsmvd rciqdeivdf ltgvltraeg hmgseprdqd aekkkkprdv arrdlafevp
      421 ergsrpaspa aklpaspsgs edlssvsssp tsspktkvtt vtsaqkssqi gssqllkrhv
      481 qrteavlthk qaqaqfaafl kqnmlvrkal ppgtssclfv pisseppeeg ekedlrvqlk
      541 rhhpssplpg sktskrpkik vslisqgdta ggpcapsqgs apeaaggkpi tmtlgqasag
      601 akeltglltt aksssseggv saspvpsvvs sstapsalht lqsrlvatsp gsslpgatsa
      661 ssllqglsfs lqdissktsg lpanpspgpa pqatsvklpt pmqslgaitt gtstivrtip
      721 vattlsslga tpggkptaih qlltngglak lasslpglaq isnqasglkv pttitltlrg
      781 qpsrittlsp mgsgaapsee sssqvlpsss qrlppap
//
LOCUS       NP_001354710             618 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 18 isoform 5 [Homo sapiens].
ACCESSION   NP_001354710
VERSION     NP_001354710.1
DBSOURCE    REFSEQ: accession NM_001367781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Ding,X., Barodia,S.K., Ma,L. and Goldberg,M.S.
  TITLE     Fbxl18 targets LRRK2 for proteasomal degradation and attenuates
            cell toxicity
  JOURNAL   Neurobiol Dis 98, 122-136 (2017)
   PUBMED   27890708
  REMARK    GeneRIF: Study showed that LRRK2 phosphorylation is required for
            LRRK2 to bind to Fbxl18, and that this interaction is important for
            regulating the amount of LRRK2 via ubiquitination of LRRK2 by the
            SCFFbxl18 ubiquitin ligase and subsequent proteasomal degradation
            of LRRK2. We also show that LRRK2 can induce caspase 8 mediated
            cell death and that the degradation of LRRK2 mediated by Fbxl18 can
            prevent LRRK2-mediated toxicity.
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Zhang,J., Yang,Z., Ou,J., Xia,X., Zhi,F. and Cui,J.
  TITLE     The F-box protein FBXL18 promotes glioma progression by promoting
            K63-linked ubiquitination of Akt
  JOURNAL   FEBS Lett 591 (1), 145-154 (2017)
   PUBMED   27926990
  REMARK    GeneRIF: FBXL18 plays an oncogenic role through promoting lysine
            63-linked ubiquitination of Akt in glioma.
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Liu,Y., Lear,T., Zhao,Y., Zhao,J., Zou,C., Chen,B.B. and
            Mallampalli,R.K.
  TITLE     F-box protein Fbxl18 mediates polyubiquitylation and proteasomal
            degradation of the pro-apoptotic SCF subunit Fbxl7
  JOURNAL   Cell Death Dis 6 (2), e1630 (2015)
   PUBMED   25654763
  REMARK    GeneRIF: Fbxl18 regulates apoptosis by mediating
            ubiquitin-dependent proteasomal degradation of the pro-apoptotic
            protein Fbxl7 that may impact cellular processes involved in cell
            cycle progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006483.3 and AC092171.4.
            
            Summary: The protein encoded by this gene is a member of a family
            of proteins that contain an approximately 40-amino acid F-box
            motif. This motif is important for interaction with SKP1 and for
            targeting some proteins for degradation. The encoded protein has
            been shown to control the cellular level of FBXL7, a protein that
            induces mitotic arrest, by targeting it for polyubiquitylation and
            proteasomal degradation. Members of the F-box protein family, such
            as FBXL18, are characterized by an approximately 40-amino acid
            F-box motif. F-box proteins interact with SKP1 through the F box,
            and they interact with ubiquitination targets through other protein
            interaction domains. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (6), as well as variant 5, encodes
            isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1163655.434799.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..618
                     /product="F-box/LRR-repeat protein 18 isoform 5"
                     /note="F-box/LRR-repeat protein 18"
                     /calculated_mol_wt=67771
     Region          1..575
                     /region_name="FBXL18_LRR"
                     /note="F-box/LRR-repeat protein 18, LRR; pfam19729"
                     /db_xref="CDD:466163"
     Region          192..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          245..284
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          285..314
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          315..384
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          351..376
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          385..432
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          433..459
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          460..489
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          490..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          516..540
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..618
                     /gene="FBXL18"
                     /gene_synonym="Fbl18"
                     /coded_by="NM_001367781.1:320..2176"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:80028"
                     /db_xref="HGNC:HGNC:21874"
                     /db_xref="MIM:609084"
ORIGIN      
        1 magcywlpgs tvehvarcrs lvkvnlsgch ltslrlskml salqhlrsla idvspgfdas
       61 qlsseckatl srvrelkqtl ftpsygvvpc ctslekllly feildrtreg ailsgqlmvg
      121 qsnvphyqnl rvfyarlapg yinqevvrly lavlsdrtpq nlhaflisvp gsfaesgatk
      181 nlldsmarnv vldalqlpks wlngssllqh mkfnnpfyfs fsrctlsggh liqqvinggk
      241 dlrslaslnl sgcvhclspd sllrkaeddi dssiletlva sccnlrhlnl saahhhsseg
      301 lgrhlcqlla rlrhlrslsl pvcsvadsap radrapaqpa mhavprgfgk kvrvgvqscp
      361 spfsgqacpq pssvfwsllk nlpflehlel igsnfssamp rnepairnsl ppcsraqsvg
      421 dsevaaigql aflrhltlaq lpsvltgsgl vniglqcqql rslslanlgm mgkvvympal
      481 sdmlkhckrl rdlrleqpyf sanaqffqal sqcpslqrlc lvsrsgtlqp davlafmarc
      541 lqvvmchlft geslatcksl qqsllrsfqa erpalnvvif pllhegltdv irdvplvhld
      601 eitlfksrva eeppnlww
//
LOCUS       NP_001306136             568 aa            linear   PRI 20-NOV-2025
DEFINITION  TNF receptor-associated factor 5 isoform a [Homo sapiens].
ACCESSION   NP_001306136
VERSION     NP_001306136.1
DBSOURCE    REFSEQ: accession NM_001319207.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Cheng,W.L., Chao,S.P., Zhao,F., Cai,H.H., Zeng,Z., Cao,J.L.,
            Jin,Z., Deng,K.Q., Hu,X., Wang,H. and Lu,Z.
  TITLE     Tumor necrosis factor receptor-associated factor 5 protects against
            intimal hyperplasia by regulation of macrophage polarization via
            directly targeting PPARgamma
  JOURNAL   Inflamm Res 73 (6), 929-943 (2024)
   PUBMED   38642079
  REMARK    GeneRIF: Tumor necrosis factor receptor-associated factor 5
            protects against intimal hyperplasia by regulation of macrophage
            polarization via directly targeting PPARgamma.
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Wu,G., Wu,F., Zhou,Y.Q., Lu,W., Hu,F.L. and Fan,X.
  TITLE     Silencing of TRAF5 enhances necroptosis in hepatocellular carcinoma
            by inhibiting LTBR-mediated NF-kappaB signaling
  JOURNAL   PeerJ 11, e15551 (2023)
   PUBMED   37366426
  REMARK    GeneRIF: Silencing of TRAF5 enhances necroptosis in hepatocellular
            carcinoma by inhibiting LTBR-mediated NF-kappaB signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 568)
  AUTHORS   van Loo,G. and Bertrand,M.J.M.
  TITLE     Death by TNF: a road to inflammation
  JOURNAL   Nat Rev Immunol 23 (5), 289-303 (2023)
   PUBMED   36380021
  REMARK    Review article
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Zhang,F., Luo,B.H., Wu,Q.H., Li,Q.L. and Yang,K.D.
  TITLE     LncRNA HCG18 upregulates TRAF4/TRAF5 to facilitate proliferation,
            migration and EMT of epithelial ovarian cancer by targeting
            miR-29a/b
  JOURNAL   Mol Med 28 (1), 2 (2022)
   PUBMED   34983361
  REMARK    GeneRIF: LncRNA HCG18 upregulates TRAF4/TRAF5 to facilitate
            proliferation, migration and EMT of epithelial ovarian cancer by
            targeting miR-29a/b.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Hsu,H., Solovyev,I., Colombero,A., Elliott,R., Kelley,M. and
            Boyle,W.J.
  TITLE     ATAR, a novel tumor necrosis factor receptor family member, signals
            through TRAF2 and TRAF5
  JOURNAL   J Biol Chem 272 (21), 13471-13474 (1997)
   PUBMED   9153189
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Tang,X.X., Pleasure,D.E. and Ikegaki,N.
  TITLE     cDNA cloning, chromosomal localization, and expression pattern of
            EPLG8, a new member of the EPLG gene family encoding ligands of
            EPH-related protein-tyrosine kinase receptors
  JOURNAL   Genomics 41 (1), 17-24 (1997)
   PUBMED   9126477
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Aizawa,S., Nakano,H., Ishida,T., Horie,R., Nagai,M., Ito,K.,
            Yagita,H., Okumura,K., Inoue,J. and Watanabe,T.
  TITLE     Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2
            are involved in CD30-mediated NFkappaB activation
  JOURNAL   J Biol Chem 272 (4), 2042-2045 (1997)
   PUBMED   8999898
REFERENCE   9  (residues 1 to 568)
  AUTHORS   Ishida,T.K., Tojo,T., Aoki,T., Kobayashi,N., Ohishi,T.,
            Watanabe,T., Yamamoto,T. and Inoue,J.
  TITLE     TRAF5, a novel tumor necrosis factor receptor-associated factor
            family protein, mediates CD40 signaling
  JOURNAL   Proc Natl Acad Sci U S A 93 (18), 9437-9442 (1996)
   PUBMED   8790348
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303286.1, AL590101.9,
            AB000509.1 and GD146999.1.
            
            Summary: The scaffold protein encoded by this gene is a member of
            the tumor necrosis factor receptor-associated factor (TRAF) protein
            family and contains a meprin and TRAF homology (MATH) domain, a
            RING-type zinc finger, and two TRAF-type zinc fingers. TRAF
            proteins are associated with, and mediate signal transduction from
            members of the TNF receptor superfamily. This protein is one of the
            components of a multiple protein complex which binds to tumor
            necrosis factor (TNF) receptor cytoplasmic domains and mediates
            TNF-induced activation. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303286.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..568
                     /product="TNF receptor-associated factor 5 isoform a"
                     /note="RING finger protein 84"
                     /calculated_mol_wt=65507
     Region          39..94
                     /region_name="mRING-HC-C3HC3D_TRAF5"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in tumor necrosis factor (TNF) receptor-associated
                     factor 5 (TRAF5) and similar proteins; cd16642"
                     /db_xref="CDD:438304"
     Site            order(42..43,57,59..63)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438304"
     Region          139..194
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          194..252
                     /region_name="zf-TRAF"
                     /note="TRAF-type zinc finger; pfam02176"
                     /db_xref="CDD:280357"
     Region          243..>409
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          356..568
                     /region_name="Interaction with EIF2AK2/PKR.
                     /evidence=ECO:0000269|PubMed:15121867"
                     /note="propagated from UniProtKB/Swiss-Prot (O00463.2)"
     Region          415..561
                     /region_name="MATH"
                     /note="MATH (meprin and TRAF-C homology) domain; an
                     independent folding unit with an eight-stranded
                     beta-sandwich structure found in meprins, TRAFs and other
                     proteins. Meprins comprise a class of extracellular
                     metalloproteases which are anchored to the membrane...;
                     cl02446"
                     /db_xref="CDD:445786"
     Site            order(473,529..531)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:239749"
     CDS             1..568
                     /gene="TRAF5"
                     /gene_synonym="MGC:39780; RNF84"
                     /coded_by="NM_001319207.2:59..1765"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="GeneID:7188"
                     /db_xref="HGNC:HGNC:12035"
                     /db_xref="MIM:602356"
ORIGIN      
        1 mayseehkgm pcgfirqnsg nsisldfeps ieyqfverle erykcafchs vlhnphqtgc
       61 ghrfcqhcil slrelntvpi cpvdkeviks qevfkdncck revlnlyvyc snapgcnakv
      121 ilgryqqvpl accyllqdhl qqclfqpvqc snekcrepvl rkdlkehlsa scqfrkekcl
      181 yckkdvvvin lqnheenlcp eypvfcpnnc akiilktevd ehlavcpeae qdcpfkhygc
      241 avtdkrrnlq qhehsalreh mrlvleknvq leeqisdlhk sleqkeskiq qlaetikkle
      301 kefkqfaqlf gkngsflpni qvfashidks awleaqvhql lqmvnqqqnk fdlrplmeav
      361 dtvkqkitll enndqrlavl eeetnkhdth inihkaqlsk neerfklleg tcyngkliwk
      421 vtdykmkkre avdghtvsif sqsfytsrcg yrlcarayln gdgsgrgshl slyfvvmrge
      481 fdsllqwpfr qrvtlmlldq sgkknimetf kpdpnsssfk rpdgemnias gcprfvahsv
      541 lenaknayik ddtlflkvav dltdledl
//
LOCUS       NP_001317565             268 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 11 isoform 3 [Homo sapiens].
ACCESSION   NP_001317565 XP_005265549
VERSION     NP_001317565.1
DBSOURCE    REFSEQ: accession NM_001330636.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Shi,J.Q., Liu,X.F. and Wang,C.
  TITLE     [Progress on the involvement of HDAC11 in the regulation of
            mammalian oocyte maturation and early embryonic development]
  JOURNAL   Sheng Li Xue Bao 76 (3), 438-446 (2024)
   PUBMED   38939938
  REMARK    GeneRIF: [Progress on the involvement of HDAC11 in the regulation
            of mammalian oocyte maturation and early embryonic development].
            Review article
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Byeon,H.E., Choi,S.E., Kim,Y., Choi,S., Lee,S.J., Kim,D.H., Mo,J.S.
            and Jeon,J.Y.
  TITLE     HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome Activation by
            Inducing YAP Expression in THP-1 Cells and PBMCs
  JOURNAL   Endocrinology 165 (3) (2024)
   PUBMED   38366363
  REMARK    GeneRIF: HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome
            Activation by Inducing YAP Expression in THP-1 Cells and PBMCs.
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Liu,Y., Tong,X., Hu,W. and Chen,D.
  TITLE     HDAC11: A novel target for improved cancer therapy
  JOURNAL   Biomed Pharmacother 166, 115418 (2023)
   PUBMED   37659201
  REMARK    GeneRIF: HDAC11: A novel target for improved cancer therapy.
            Review article
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Wu,H., Yin,X., Zhao,X., Wu,Z., Xiao,Y., Di,Q., Sun,P., Tang,H.,
            Quan,J. and Chen,W.
  TITLE     HDAC11 negatively regulates antifungal immunity by inhibiting Nos2
            expression via binding with transcriptional repressor STAT3
  JOURNAL   Redox Biol 56, 102461 (2022)
   PUBMED   36087429
  REMARK    GeneRIF: HDAC11 negatively regulates antifungal immunity by
            inhibiting Nos2 expression via binding with transcriptional
            repressor STAT3.
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Feng,W., Lu,Z., Luo,R.Z., Zhang,X., Seto,E., Liao,W.S. and Yu,Y.
  TITLE     Multiple histone deacetylases repress tumor suppressor gene ARHI in
            breast cancer
  JOURNAL   Int J Cancer 120 (8), 1664-1668 (2007)
   PUBMED   17230502
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Lindberg,D., Akerstrom,G. and Westin,G.
  TITLE     Mutational analyses of WNT7A and HDAC11 as candidate tumour
            suppressor genes in sporadic malignant pancreatic endocrine tumours
  JOURNAL   Clin Endocrinol (Oxf) 66 (1), 110-114 (2007)
   PUBMED   17201809
  REMARK    GeneRIF: the absence of tumour-specific somatic events in WNT7A and
            HDAC11 suggests that these genes are unlikely to have a classical
            tumour suppressor gene role in sporadic malignant pancreatic
            endocrine tumours
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Voelter-Mahlknecht,S., Ho,A.D. and Mahlknecht,U.
  TITLE     Chromosomal organization and localization of the novel class IV
            human histone deacetylase 11 gene
  JOURNAL   Int J Mol Med 16 (4), 589-598 (2005)
   PUBMED   16142391
  REMARK    GeneRIF: Fluorescence in situ hybridization analysis localized
            HDAC11 gene to chromosome 3p25, a region characterized by frequent
            gains and losses of chromosomal material in a number of various
            types of cancer.
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Bradbury,C.A., Khanim,F.L., Hayden,R., Bunce,C.M., White,D.A.,
            Drayson,M.T., Craddock,C. and Turner,B.M.
  TITLE     Histone deacetylases in acute myeloid leukaemia show a distinctive
            pattern of expression that changes selectively in response to
            deacetylase inhibitors
  JOURNAL   Leukemia 19 (10), 1751-1759 (2005)
   PUBMED   16121216
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Gao,L., Cueto,M.A., Asselbergs,F. and Atadja,P.
  TITLE     Cloning and functional characterization of HDAC11, a novel member
            of the human histone deacetylase family
  JOURNAL   J Biol Chem 277 (28), 25748-25755 (2002)
   PUBMED   11948178
  REMARK    GeneRIF: cloning and functional characterization
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC315722.1, DA157041.1,
            AC027124.5 and HY351163.1.
            
            On Aug 30, 2016 this sequence version replaced XP_005265549.1.
            
            Summary: This gene encodes a class IV histone deacetylase. The
            encoded protein is localized to the nucleus and may be involved in
            regulating the expression of interleukin 10. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Apr
            2009].
            
            Transcript Variant: This variant (3) lacks three exons in the
            coding region, compared to variant 1. It encodes isoform 3, which
            lacks an internal in-frame segment and is shorter, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.486453.1,
                                           SRR7346977.967541.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..268
                     /product="histone deacetylase 11 isoform 3"
                     /EC_number="3.5.1.98"
                     /calculated_mol_wt=30569
     Region          35..240
                     /region_name="HDAC_classIV"
                     /note="Histone deacetylase class IV also known as histone
                     deacetylase 11; cd09993"
                     /db_xref="CDD:212519"
     CDS             1..268
                     /gene="HDAC11"
                     /gene_synonym="HD11"
                     /coded_by="NM_001330636.2:43..849"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82738.1"
                     /db_xref="GeneID:79885"
                     /db_xref="HGNC:HGNC:19086"
                     /db_xref="MIM:607226"
ORIGIN      
        1 mlhttqlyqh vpetrwpivy sprynitfmg leklhpfdag kwgkvinflk eekllsdsml
       61 veareaseed llvvhtrryl nelkflferv egisratiid ldahqgnghe rdfmddkrvy
      121 imdvynrhiy pgdrfakqai rrkvelewgt eddeyldkve rnikkslqeh lpdvvvynag
      181 tdilegdrlg glsispagiv krdelvfrmv rgrrvpilmv tsggyqkrta riiadsilnl
      241 fglgligpes psvsaqnsdt pllppavp
//
LOCUS       NP_001341870             614 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-4A isoform 4 [Homo sapiens].
ACCESSION   NP_001341870
VERSION     NP_001341870.1
DBSOURCE    REFSEQ: accession NM_001354941.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Jia,Y., Huo,X., Wu,L., Zhang,H., Xu,W. and Leng,H.
  TITLE     circSNTB2 and CUL4A Induces Dysfunction of Nucleus Pulposus Cells
            by Competitively Binding miR-665
  JOURNAL   Biochem Genet 62 (2), 968-986 (2024)
   PUBMED   37507642
  REMARK    GeneRIF: circSNTB2 and CUL4A Induces Dysfunction of Nucleus
            Pulposus Cells by Competitively Binding miR-665.
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Tavlas,P., Nikou,S., Geramoutsou,C., Bosgana,P., Tsaniras,S.C.,
            Melachrinou,M., Maroulis,I. and Bravou,V.
  TITLE     CUL4A Ubiquitin Ligase Is an Independent Predictor of Overall
            Survival in Pancreatic Adenocarcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (2), 166-177 (2024)
   PUBMED   38423594
  REMARK    GeneRIF: CUL4A Ubiquitin Ligase Is an Independent Predictor of
            Overall Survival in Pancreatic Adenocarcinoma.
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Hu,Y., Zhang,R., Lu,S., Zhang,W., Wang,D., Ge,Y., Jiang,F., Qin,X.
            and Liu,Y.
  TITLE     S100 Calcium Binding Protein A16 Promotes Cell Proliferation by
            triggering LATS1 ubiquitin degradation mediated by CUL4A ligase to
            inhibit Hippo pathway in Glioma development
  JOURNAL   Int J Biol Sci 19 (7), 2034-2052 (2023)
   PUBMED   37151881
  REMARK    GeneRIF: S100 Calcium Binding Protein A16 Promotes Cell
            Proliferation by triggering LATS1 ubiquitin degradation mediated by
            CUL4A ligase to inhibit Hippo pathway in Glioma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Ito,T., Ando,H., Suzuki,T., Ogura,T., Hotta,K., Imamura,Y.,
            Yamaguchi,Y. and Handa,H.
  TITLE     Identification of a primary target of thalidomide teratogenicity
  JOURNAL   Science 327 (5971), 1345-1350 (2010)
   PUBMED   20223979
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
  REMARK    GeneRIF: crystallographic analyses of the virally hijacked form of
            the human DDB1-CUL4A-ROC1 machinery
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Chen,L.C., Manjeshwar,S., Lu,Y., Moore,D., Ljung,B.M., Kuo,W.L.,
            Dairkee,S.H., Wernick,M., Collins,C. and Smith,H.S.
  TITLE     The human homologue for the Caenorhabditis elegans cul-4 gene is
            amplified and overexpressed in primary breast cancers
  JOURNAL   Cancer Res 58 (16), 3677-3683 (1998)
   PUBMED   9721878
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Osaka,F., Kawasaki,H., Aida,N., Saeki,M., Chiba,T., Kawashima,S.,
            Tanaka,K. and Kato,S.
  TITLE     A new NEDD8-ligating system for cullin-4A
  JOURNAL   Genes Dev 12 (15), 2263-2268 (1998)
   PUBMED   9694792
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455959.1, DA394068.1,
            BC008308.1, AL136221.38 and BU631279.1.
            
            Summary: CUL4A is the ubiquitin ligase component of a multimeric
            complex involved in the degradation of DNA damage-response proteins
            (Liu et al., 2009 [PubMed 19481525]).[supplied by OMIM, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR14038193.4241438.1,
                                    SRR14038194.1770764.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..614
                     /product="cullin-4A isoform 4"
                     /note="CUL-4A"
                     /calculated_mol_wt=71259
     Region          1..515
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          543..608
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..614
                     /gene="CUL4A"
                     /coded_by="NM_001354941.2:449..2293"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="GeneID:8451"
                     /db_xref="HGNC:HGNC:2554"
                     /db_xref="MIM:603137"
ORIGIN      
        1 mimirsiflf ldrtyvlqns tlpsiwdmgl elfrthiisd kmvqsktidg illlierers
       61 geavdrsllr sllgmlsdlq vykdsfelkf leetnclyaa egqrlmqere vpeylnhvsk
      121 rleeegdrvi tyldhstqkp liacvekqll gehltailqk gldhlldenr vpdlaqmyql
      181 fsrvrggqqa llqhwseyik tfgtaivinp ekdkdmvqdl ldfkdkvdhv ievcfqkner
      241 fvnlmkesfe tfinkrpnkp aeliakhvds klragnkeat deelertldk imilfrfihg
      301 kdvfeafykk dlakrllvgk sasvdaeksm lsklkhecga aftsklegmf kdmelskdim
      361 vhfkqhmqnq sdsgpidltv niltmgywpt ytpmevhltp emiklqevfk afylgkhsgr
      421 klqwqttlgh avlkaefkeg kkefqvslfq tlvllmfneg dgfsfeeikm atgiedselr
      481 rtlqslacgk arvlikspkg kevedgdkfi fngefkhklf rikinqiqmk etveeqvstt
      541 ervfqdrqyq idaaivrimk mrktlghnll vselynqlkf pvkpgdlkkr ieslidrdym
      601 erdkdnpnqy hyva
//
LOCUS       NP_003932                505 aa            linear   PRI 20-NOV-2025
DEFINITION  actin nucleation-promoting factor WASL [Homo sapiens].
ACCESSION   NP_003932
VERSION     NP_003932.3
DBSOURCE    REFSEQ: accession NM_003941.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Cerutti,C., Lucotti,S., Menendez,S.T., Reymond,N., Garg,R.,
            Romero,I.A., Muschel,R. and Ridley,A.J.
  TITLE     IQGAP1 and NWASP promote human cancer cell dissemination and
            metastasis by regulating beta1-integrin via FAK and MRTF/SRF
  JOURNAL   Cell Rep 43 (4), 113989 (2024)
   PUBMED   38536816
  REMARK    GeneRIF: IQGAP1 and NWASP promote human cancer cell dissemination
            and metastasis by regulating beta1-integrin via FAK and MRTF/SRF.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Kim,H.S., Lee,Y.S., Dong,S.M., Kim,H.J., Lee,D.E., Kang,H.W.,
            Kim,M.J. and Park,J.S.
  TITLE     Neural Wiskott-Aldrich syndrome protein (N-WASP) promotes distant
            metastasis in pancreatic ductal adenocarcinoma via activation of
            LOXL2
  JOURNAL   Oncol Res 32 (4), 615-624 (2024)
   PUBMED   38560567
  REMARK    GeneRIF: Neural Wiskott-Aldrich syndrome protein (N-WASP) promotes
            distant metastasis in pancreatic ductal adenocarcinoma via
            activation of LOXL2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Yuen,W.S., Zhang,Q.H., Bourdais,A., Adhikari,D., Halet,G. and
            Carroll,J.
  TITLE     Polo-like kinase 1 promotes Cdc42-induced actin polymerization for
            asymmetric division in oocytes
  JOURNAL   Open Biol 13 (3), 220326 (2023)
   PUBMED   36883283
  REMARK    GeneRIF: Polo-like kinase 1 promotes Cdc42-induced actin
            polymerization for asymmetric division in oocytes.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Frugtniet,B.A., Ruge,F., Sanders,A.J., Owen,S., Harding,K.G.,
            Jiang,W.G. and Martin,T.A.
  TITLE     nWASP Inhibition Increases Wound Healing via TrKb/PLCgamma
            Signalling
  JOURNAL   Biomolecules 13 (2), 379 (2023)
   PUBMED   36830748
  REMARK    GeneRIF: nWASP Inhibition Increases Wound Healing via TrKb/PLCgamma
            Signalling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Qualmann,B., Roos,J., DiGregorio,P.J. and Kelly,R.B.
  TITLE     Syndapin I, a synaptic dynamin-binding protein that associates with
            the neural Wiskott-Aldrich syndrome protein
  JOURNAL   Mol Biol Cell 10 (2), 501-513 (1999)
   PUBMED   9950691
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Suetsugu,S., Miki,H. and Takenawa,T.
  TITLE     The essential role of profilin in the assembly of actin for
            microspike formation
  JOURNAL   EMBO J 17 (22), 6516-6526 (1998)
   PUBMED   9822597
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Suzuki,T., Miki,H., Takenawa,T. and Sasakawa,C.
  TITLE     Neural Wiskott-Aldrich syndrome protein is implicated in the
            actin-based motility of Shigella flexneri
  JOURNAL   EMBO J 17 (10), 2767-2776 (1998)
   PUBMED   9582270
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Miki,H., Sasaki,T., Takai,Y. and Takenawa,T.
  TITLE     Induction of filopodium formation by a WASP-related
            actin-depolymerizing protein N-WASP
  JOURNAL   Nature 391 (6662), 93-96 (1998)
   PUBMED   9422512
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Fukuoka,M., Miki,H. and Takenawa,T.
  TITLE     Identification of N-WASP homologs in human and rat brain
  JOURNAL   Gene 196 (1-2), 43-48 (1997)
   PUBMED   9322739
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC052955.1, BC028602.1 and
            DB380642.1.
            
            On Aug 31, 2004 this sequence version replaced NP_003932.2.
            
            Summary: This gene encodes a member of the Wiskott-Aldrich syndrome
            (WAS) protein family. Wiskott-Aldrich syndrome proteins share
            similar domain structure, and associate with a variety of signaling
            molecules to alter the actin cytoskeleton. The encoded protein is
            highly expressed in neural tissues, and interacts with several
            proteins involved in cytoskeletal organization, including cell
            division control protein 42 (CDC42) and the actin-related
            protein-2/3 (ARP2/3) complex. The encoded protein may be involved
            in the formation of long actin microspikes, and in neurite
            extension. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052955.1, SRR1660805.240690.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223023.5/ ENSP00000223023.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.32"
     Protein         1..505
                     /product="actin nucleation-promoting factor WASL"
                     /note="neural Wiskott-Aldrich syndrome protein;
                     Wiskott-Aldrich syndrome like"
                     /calculated_mol_wt=54696
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O00401.2)"
     Region          40..138
                     /region_name="EVH1_WASP-like"
                     /note="WASP family proteins EVH1 domain; cd01205"
                     /db_xref="CDD:269916"
     Site            order(40,42,47,51,66,68,75,77,79,92,104,112,118)
                     /site_type="other"
                     /note="WAS mutation hotspots"
                     /db_xref="CDD:269916"
     Site            order(49,51,57,107,109)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269916"
     Region          138..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00401.2)"
     Region          184..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00401.2)"
     Region          202..259
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(203,206,209,211,214,232,236)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238077"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TNK2.
                     /evidence=ECO:0000269|PubMed:16257963; propagated from
                     UniProtKB/Swiss-Prot (O00401.2)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FAK1 and TNK2.
                     /evidence=ECO:0000269|PubMed:16257963,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00401.2)"
     Region          266..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00401.2)"
     Site            307
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O00401.2)"
     Region          402..428
                     /region_name="WH2_N-WASP_r1"
                     /note="first tandem Wiskott Aldrich syndrome homology
                     region 2 (WH2 motif) repeat found in human Neural
                     Wiskott-Aldrich syndrome protein (N-WASP) and related
                     domains; cd22074"
                     /db_xref="CDD:409217"
     Site            order(405..406,408..410,412..414,419..422)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409217"
     Region          419..422
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409217"
     Region          429..453
                     /region_name="WH2_hN-WASP_r2_like"
                     /note="second tandem Wiskott Aldrich syndrome homology
                     region 2 (WH2 motif) repeat found in human Neural
                     Wiskott-Aldrich syndrome protein (N-WASP) and related
                     domains; cd22075"
                     /db_xref="CDD:409218"
     Site            order(434,436..438,440..442,445,447..449)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409218"
     Region          476..505
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00401.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00401.2)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O00401.2)"
     CDS             1..505
                     /gene="WASL"
                     /gene_synonym="N-WASP; NWASP; WASPB"
                     /coded_by="NM_003941.4:270..1787"
                     /db_xref="CCDS:CCDS34743.1"
                     /db_xref="GeneID:8976"
                     /db_xref="HGNC:HGNC:12735"
                     /db_xref="MIM:605056"
ORIGIN      
        1 mssvqqqppp prrvtnvgsl lltpqenesl ftflgkkcvt mssavvqlya adrncmwskk
       61 csgvaclvkd npqrsyflri fdikdgkllw eqelynnfvy nsprgyfhtf agdtcqvaln
      121 faneeeakkf rkavtdllgr rqrksekrrd ppngpnlpma tvdiknpeit tnrfygpqvn
      181 nishtkekkk gkakkkrltk adigtpsnfq highvgwdpn tgfdlnnldp elknlfdmcg
      241 iseaqlkdre tskviydfie ktggveavkn elrrqapppp ppsrggpppp pppphnsgpp
      301 pppargrgap ppppsrapta appppppsrp svavpppppn rmypppppal pssapsgppp
      361 pppsvlgvgp vapppppppp pppgpppppg lpsdgdhqvp ttagnkaall dqiregaqlk
      421 kveqnsrpvs csgrdalldq irqgiqlksv adgqestppt paptsgivga lmevmqkrsk
      481 aihssdeded eddeedfedd dewed
//
LOCUS       NP_115509                941 aa            linear   PRI 20-NOV-2025
DEFINITION  MYCBP-associated protein isoform 1 [Homo sapiens].
ACCESSION   NP_115509
VERSION     NP_115509.5
DBSOURCE    REFSEQ: accession NM_032133.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 941)
  AUTHORS   Zhou,Y., Tu,C., Coutton,C., Tang,J., Tian,S., Tang,S., Martinez,G.,
            Zhou,D., Tebbakh,C., Wang,J., Zouari,R., Zhou,X., Ben
            Mustapha,S.F., Wang,X., Wu,B., Geng,X., Liu,S., Jin,L., Shi,H.,
            Tan,Y.Q., Ray,P.F., Wang,L., Yang,X., Zhang,F. and Liu,C.
  TITLE     Homozygous deleterious variants in MYCBPAP induce
            asthenoteratozoospermia involving abnormal acrosome biogenesis,
            manchette structure and sperm tail assembly in humans and mice
  JOURNAL   Sci China Life Sci 68 (3), 777-792 (2025)
   PUBMED   39704931
REFERENCE   2  (residues 1 to 941)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   3  (residues 1 to 941)
  AUTHORS   Yukitake,H., Furusawa,M., Taira,T., Iguchi-Ariga,S.M. and Ariga,H.
  TITLE     AAT-1, a novel testis-specific AMY-1-binding protein, forms a
            quaternary complex with AMY-1, A-kinase anchor protein 84, and a
            regulatory subunit of cAMP-dependent protein kinase and is
            phosphorylated by its kinase
  JOURNAL   J Biol Chem 277 (47), 45480-45492 (2002)
   PUBMED   12223483
REFERENCE   4  (residues 1 to 941)
  AUTHORS   Yukitake,H., Furusawa,M., Taira,T., Iguchi-Ariga,S.M. and Ariga,H.
  TITLE     AMAP-1, a novel testis-specific AMY-1-binding protein, is
            differentially expressed during the course of spermatogenesis
  JOURNAL   Biochim Biophys Acta 1577 (1), 126-132 (2002)
   PUBMED   12151104
  REMARK    GeneRIF: sequence analysis of AMAP-1 and identification of AMY-1 as
            binding protein
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK303041.1 and AB083068.1.
            
            On Sep 28, 2018 this sequence version replaced NP_115509.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005627.1, AB083068.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000323776.11/
                                                ENSP00000323184.6
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..941
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..941
                     /product="MYCBP-associated protein isoform 1"
                     /note="Mycbp-associated protein; AMY1-associating protein
                     1; AMAM-1; AMY-1-binding protein 1; testis secretory
                     sperm-binding protein Li 214e"
                     /calculated_mol_wt=107479
     Region          193..612
                     /region_name="MYCBPAP"
                     /note="MYCBP-associated protein family; pfam14646"
                     /db_xref="CDD:464234"
     CDS             1..941
                     /gene="MYCBPAP"
                     /gene_synonym="AMAP-1; AMAP1"
                     /coded_by="NM_032133.6:237..3062"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32680.3"
                     /db_xref="GeneID:84073"
                     /db_xref="HGNC:HGNC:19677"
                     /db_xref="MIM:609835"
ORIGIN      
        1 mkslkkdsrl ritptrllea senvkekkra kgpeqptpti qeepepvsnv lqgddilala
       61 ikkedlkeqh iprltekedk rvitqkfiir klkpmdprrk vchlvarpan pdeatkpldy
      121 sgpgdsfdgs dqilphhilg slqdfkrial argntqlaer iptspclmtl isaegeskqk
      181 apkeekrppw apppqhnflk nwqrntalrk kqqealsehl kkpvsellmh tgetyrriqe
      241 erelidctlp trrdrkswen sgfwsrleyl gdemtglvmt ktktqrglme pithirkphs
      301 irvetglpaq rdasyrytwd rslfliyrrk elqrimeeld fsqqdidgle vvgkgwpfsa
      361 vtvedytvfe rsqgsssedt aylgtlasss dvsmpilgps llfcgkpacw irgsnpqdkr
      421 qvgiaahltf etlegektss eltvvnngtv aiwydwrrqh qpdtfqdlkk nrmqrfyfdn
      481 regvilpgei ktftfffksl tagvfrefwe frthptllgg ailqvnlhav sltqdvfede
      541 rkvlesklta heavtvvrev lqellmgvlt pertpspvda ylteedlfrh rnpplhyehq
      601 vvqslhqlwr qymtlpakae earpgdkehv spiatekasv naellprfrs pisetqvprp
      661 enealresgs qkarvgtksp qrksimeeil veespdvdst kspwepdglp llewnlcled
      721 frkavmvlpd enhredalmr lnkaalelcq kprplqsnll hqmclqlwrd vidslvghsm
      781 wlrsvlglpe ketiylnvpe eqdqksppim evkvpvgkag keerkgaaqe kkqlgikdke
      841 dkkgakllgk edrpnskkhk akddkkviks asqdrfsled ptpdiilssq epidplvmgk
      901 ytqslhsevr glldtlvtdl mvladelspi knveealrlc r
//
LOCUS       NP_002473                788 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear autoantigenic sperm protein isoform 2 [Homo sapiens].
ACCESSION   NP_002473
VERSION     NP_002473.2
DBSOURCE    REFSEQ: accession NM_002482.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 788)
  AUTHORS   Zhang,S., Yang,J., Ji,D., Meng,X., Zhu,C., Zheng,G., Glessner,J.,
            Qu,H.Q., Cui,Y., Liu,Y., Wang,W., Li,X., Zhang,H., Xiu,Z., Sun,Y.,
            Sun,L., Li,J., Hakonarson,H., Li,J. and Xia,Q.
  TITLE     NASP gene contributes to autism by epigenetic dysregulation of
            neural and immune pathways
  JOURNAL   J Med Genet 61 (7), 677-688 (2024)
   PUBMED   38443156
  REMARK    GeneRIF: NASP gene contributes to autism by epigenetic
            dysregulation of neural and immune pathways.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 788)
  AUTHORS   Qiu,Y., Pei,D., Wang,M., Wang,Q., Duan,W., Wang,L., Liu,K., Guo,Y.,
            Luo,L., Guo,Z., Guan,F., Wang,Z., Xing,A., Liu,Z., Ma,Z., Jiang,G.,
            Yan,D., Liu,X., Zhang,Z. and Wang,W.
  TITLE     Nuclear autoantigenic sperm protein facilitates glioblastoma
            progression and radioresistance by regulating the ANXA2/STAT3 axis
  JOURNAL   CNS Neurosci Ther 30 (4), e14709 (2024)
   PUBMED   38605477
  REMARK    GeneRIF: Nuclear autoantigenic sperm protein facilitates
            glioblastoma progression and radioresistance by regulating the
            ANXA2/STAT3 axis.
REFERENCE   3  (residues 1 to 788)
  AUTHORS   Chen,M.Z., Wang,S.A., Hsu,S.C., Silva,K.A.S. and Yang,F.M.
  TITLE     Home Dust Mites Promote MUC5AC Hyper-Expression by Modulating the
            sNASP/TRAF6 Axis in the Airway Epithelium
  JOURNAL   Int J Mol Sci 23 (16), 9405 (2022)
   PUBMED   36012669
  REMARK    GeneRIF: Home Dust Mites Promote MUC5AC Hyper-Expression by
            Modulating the sNASP/TRAF6 Axis in the Airway Epithelium.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 788)
  AUTHORS   Bao,H., Carraro,M., Flury,V., Liu,Y., Luo,M., Chen,L., Groth,A. and
            Huang,H.
  TITLE     NASP maintains histone H3-H4 homeostasis through two distinct H3
            binding modes
  JOURNAL   Nucleic Acids Res 50 (9), 5349-5368 (2022)
   PUBMED   35489058
REFERENCE   5  (residues 1 to 788)
  AUTHORS   Liu,C.P., Jin,W., Hu,J., Wang,M., Chen,J., Li,G. and Xu,R.M.
  TITLE     Distinct histone H3-H4 binding modes of sNASP reveal the basis for
            cooperation and competition of histone chaperones
  JOURNAL   Genes Dev 35 (23-24), 1610-1624 (2021)
   PUBMED   34819355
REFERENCE   6  (residues 1 to 788)
  AUTHORS   Alekseev,O.M., Bencic,D.C., Richardson,R.T., Widgren,E.E. and
            O'Rand,M.G.
  TITLE     Overexpression of the Linker histone-binding protein tNASP affects
            progression through the cell cycle
  JOURNAL   J Biol Chem 278 (10), 8846-8852 (2003)
   PUBMED   12509435
REFERENCE   7  (residues 1 to 788)
  AUTHORS   Richardson,R.T., Bencic,D.C. and O'Rand,M.G.
  TITLE     Comparison of mouse and human NASP genes and expression in human
            transformed and tumor cell lines
  JOURNAL   Gene 274 (1-2), 67-75 (2001)
   PUBMED   11674998
REFERENCE   8  (residues 1 to 788)
  AUTHORS   Richardson,R.T., Batova,I.N., Widgren,E.E., Zheng,L.X.,
            Whitfield,M., Marzluff,W.F. and O'Rand,M.G.
  TITLE     Characterization of the histone H1-binding protein, NASP, as a cell
            cycle-regulated somatic protein
  JOURNAL   J Biol Chem 275 (39), 30378-30386 (2000)
   PUBMED   10893414
REFERENCE   9  (residues 1 to 788)
  AUTHORS   Batova,I. and O'Rand,M.G.
  TITLE     Histone-binding domains in a human nuclear autoantigenic sperm
            protein
  JOURNAL   Biol Reprod 54 (6), 1238-1244 (1996)
   PUBMED   8724350
REFERENCE   10 (residues 1 to 788)
  AUTHORS   O'Rand,M.G., Richardson,R.T., Zimmerman,L.J. and Widgren,E.E.
  TITLE     Sequence and localization of human NASP: conservation of a Xenopus
            histone-binding protein
  JOURNAL   Dev Biol 154 (1), 37-44 (1992)
   PUBMED   1426632
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC361634.1, BC010105.2,
            AK291637.1 and CK300084.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 19, 2002 this sequence version replaced NP_002473.1.
            
            Summary: This gene encodes a H1 histone binding protein that is
            involved in transporting histones into the nucleus of dividing
            cells. Multiple isoforms are encoded by transcript variants of this
            gene. The somatic form is expressed in all mitotic cells, is
            localized to the nucleus, and is coupled to the cell cycle. The
            testicular form is expressed in embryonic tissues, tumor cells, and
            the testis. In male germ cells, this protein is localized to the
            cytoplasm of primary spermatocytes, the nucleus of spermatids, and
            the periacrosomal region of mature spermatozoa. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) represents the longest
            transcript and encodes the longest isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.2226.1, AK291637.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000350030.8/ ENSP00000255120.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..788
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..788
                     /product="nuclear autoantigenic sperm protein isoform 2"
                     /note="histone H1-binding protein; nuclear autoantigenic
                     sperm protein (histone-binding); NASP histone chaperone"
                     /calculated_mol_wt=85107
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Region          43..76
                     /region_name="TPR 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          114..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          116..127
                     /region_name="Histone-binding.
                     /evidence=ECO:0000269|PubMed:8724350"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          151..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Region          211..244
                     /region_name="Histone-binding.
                     /evidence=ECO:0000269|PubMed:8724350"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          <216..516
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            243
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MD9; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          469..512
                     /region_name="Histone-binding.
                     /evidence=ECO:0000269|PubMed:8724350"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          511..534
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          540..616
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          542..579
                     /region_name="SHNi-TPR"
                     /note="pfam10516"
                     /db_xref="CDD:402238"
     Region          542..575
                     /region_name="TPR 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          542..570
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(543,546..547,550..551,553,585,588..589,592..593,
                     595..596,617,620..621,624)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          575..613
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          584..617
                     /region_name="TPR 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00339"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Region          617..640
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Region          678..788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Region          716..722
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49321.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49321.2)"
     CDS             1..788
                     /gene="NASP"
                     /gene_synonym="FLB7527; HMDRA1; PRO1999"
                     /coded_by="NM_002482.4:107..2473"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS524.1"
                     /db_xref="GeneID:4678"
                     /db_xref="HGNC:HGNC:7644"
                     /db_xref="MIM:603185"
ORIGIN      
        1 mamestataa vaaelvsadk iedvpapsts adkvesldvd seakkllglg qkhlvmgdip
       61 aavnafqeaa sllgkkyget anecgeafff ygksllelar mengvlgnal egvhveeeeg
      121 ektedeslve nndnideear eelreqvyda mgekeeakkt edkslakpet dkeqdsemek
      181 ggredmdisk saeepqekvd ltldwltets eeakggaape gpneaevtsg kpeqevpdae
      241 eeksvsgtdv qeecrekggq ekqgevivsi eekpkevsee qpvvtlekqg taveveaesl
      301 dptvkpvdvg gdepeekvvt seneagkavl eqlvgqevpp aeespevtte aaeasaveag
      361 sevsekpgqe apvlpkdgav ngpsvvgdqt piepqtsier ltetkdgsgl eekvraklvp
      421 sqeetklsve eseaagdgvd tkvaqgatek spedkvqiaa neetqereeq mkegeetegs
      481 eeddkendkt eempndsvle nkslqeneee eignlelawd mldlakiifk rqetkeaqly
      541 aaqahlklge vsvesenyvq aveefqscln lqeqyleahd rllaethyql glaygynsqy
      601 deavaqfsks ievienrmav lneqvkeaeg ssaeykkeie elkellpeir ekiedakesq
      661 rsgnvaelal katlvessts gftpggggss vsmiasrkpt dgasssncvt dishlvrkkr
      721 kpeeesprkd dakkakqepe vnggsgdavp sgnevsenme eeaenqaesr aavegtveag
      781 atvestac
//
LOCUS       NP_005756                350 aa            linear   PRI 20-NOV-2025
DEFINITION  renin receptor precursor [Homo sapiens].
ACCESSION   NP_005756
VERSION     NP_005756.2
DBSOURCE    REFSEQ: accession NM_005765.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Oot,R.A. and Wilkens,S.
  TITLE     Human V-ATPase function is positively and negatively regulated by
            TLDc proteins
  JOURNAL   Structure 32 (7), 989-1000 (2024)
   PUBMED   38593795
  REMARK    GeneRIF: Human V-ATPase function is positively and negatively
            regulated by TLDc proteins.
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Ouyang,X. and Xu,C.
  TITLE     Targeting the (pro)renin receptor in cancers: from signaling to
            pathophysiological effects
  JOURNAL   J Cancer Res Clin Oncol 149 (6), 2595-2605 (2023)
   PUBMED   36153775
  REMARK    GeneRIF: Targeting the (pro)renin receptor in cancers: from
            signaling to pathophysiological effects.
            Review article
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Edelman,W.C., Kiianitsa,K., Virmani,T., Martinez,R.A., Young,J.E.,
            Keene,C.D., Bird,T.D., Raskind,W.H. and Korvatska,O.
  TITLE     Reduced gene dosage is a common mechanism of neuropathologies
            caused by ATP6AP2 splicing mutations
  JOURNAL   Parkinsonism Relat Disord 101, 31-38 (2022)
   PUBMED   35779466
  REMARK    GeneRIF: Reduced gene dosage is a common mechanism of
            neuropathologies caused by ATP6AP2 splicing mutations.
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Martin,J.H., Mohammed,R., Delforce,S.J., Skerrett-Byrne,D.A., de
            Meaultsart,C.C., Almazi,J.G., Stephens,A.N., Verrills,N.M.,
            Dimitriadis,E., Wang,Y., Lumbers,E.R. and Pringle,K.G.
  TITLE     Role of the prorenin receptor in endometrial cancer cell growth
  JOURNAL   Oncotarget 13, 587-599 (2022)
   PUBMED   35401936
  REMARK    GeneRIF: Role of the prorenin receptor in endometrial cancer cell
            growth.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Nguyen,G., Delarue,F., Burckle,C., Bouzhir,L., Giller,T. and
            Sraer,J.D.
  TITLE     Pivotal role of the renin/prorenin receptor in angiotensin II
            production and cellular responses to renin
  JOURNAL   J Clin Invest 109 (11), 1417-1427 (2002)
   PUBMED   12045255
  REMARK    GeneRIF: expression cloning of the human renin receptor
            complementary DNA encoding a 350-amino acid protein with a single
            transmembrane domain and no homology with any known membrane
            protein
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Hedera,P., Alvarado,D., Beydoun,A. and Fink,J.K.
  TITLE     Novel mental retardation-epilepsy syndrome linked to Xp21.1-p11.4
  JOURNAL   Ann Neurol 51 (1), 45-50 (2002)
   PUBMED   11782983
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Demirci,F.Y., White,N.J., Rigatti,B.W., Lewis,K.F. and Gorin,M.B.
  TITLE     Identification, genomic structure, and screening of the vacuolar
            proton-ATPase membrane sector-associated protein M8-9 gene within
            the COD1 critical region (Xp11.4)
  JOURNAL   Mol Vis 7, 234-239 (2001)
   PUBMED   11590366
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Ludwig,J., Kerscher,S., Brandt,U., Pfeiffer,K., Getlawi,F.,
            Apps,D.K. and Schagger,H.
  TITLE     Identification and characterization of a novel 9.2-kDa membrane
            sector-associated protein of vacuolar proton-ATPase from chromaffin
            granules
  JOURNAL   J Biol Chem 273 (18), 10939-10947 (1998)
   PUBMED   9556572
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092473.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 25, 2001 this sequence version replaced NP_005756.1.
            
            Summary: This gene encodes a protein that is associated with
            adenosine triphosphatases (ATPases). Proton-translocating ATPases
            have fundamental roles in energy conservation, secondary active
            transport, acidification of intracellular compartments, and
            cellular pH homeostasis. There are three classes of ATPases- F, P,
            and V. The vacuolar (V-type) ATPases have a transmembrane
            proton-conducting sector and an extramembrane catalytic sector. The
            encoded protein has been found associated with the transmembrane
            sector of the V-type ATPases. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.75728.1,
                                           SRR1660805.51821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000636580.2/ ENSP00000490083.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..350
                     /product="renin receptor precursor"
                     /note="ATPase, H+ transporting, lysosomal interacting
                     protein 2; ATPase, H+ transporting, lysosomal (vacuolar
                     proton pump) membrane sector associated protein M8-9;
                     V-ATPase M8.9 subunit; renin receptor; embryonic liver
                     differentiation factor 10; vacuolar proton ATP synthase
                     membrane sector associated protein M8-9; N14F;
                     renin/prorenin receptor; ATPase, H+ transporting,
                     lysosomal accessory protein 2; ER-localized type I
                     transmembrane adaptor; ATPase H(+)-transporting
                     lysosomal-interacting protein 2; ER-localized type I
                     transmembrane adapter; vacuolar ATP synthase membrane
                     sector-associated protein M8-9"
                     /calculated_mol_wt=37454
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1572
     Region          254..350
                     /region_name="Renin_r"
                     /note="Renin receptor-like protein; pfam07850"
                     /db_xref="CDD:462287"
     Site            275..276
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000305|PubMed:29127204; propagated from
                     UniProtKB/Swiss-Prot (O75787.2)"
     Site            277..278
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000305|PubMed:29127204; propagated from
                     UniProtKB/Swiss-Prot (O75787.2)"
     Site            303..323
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75787.2)"
     Region          346..350
                     /region_name="Mediates retrograde transport to the ER.
                     /evidence=ECO:0000269|PubMed:29127204"
                     /note="propagated from UniProtKB/Swiss-Prot (O75787.2)"
     CDS             1..350
                     /gene="ATP6AP2"
                     /gene_synonym="(P)RR; APT6M8-9; ATP6IP2; ATP6M8-9; CDG2R;
                     ELDF10; HT028; M8-9; MRXE; MRXSH; MSTP009; PRR; RENR;
                     XMRE; XPDS"
                     /coded_by="NM_005765.3:97..1149"
                     /db_xref="CCDS:CCDS14252.1"
                     /db_xref="GeneID:10159"
                     /db_xref="HGNC:HGNC:18305"
                     /db_xref="MIM:300556"
ORIGIN      
        1 mavfvvllal vagvlgnefs ilkspgsvvf rngnwpipge ripdvaalsm gfsvkedlsw
       61 pglavgnlfh rpratvmvmv kgvnklalpp gsvisyplen avpfsldsva nsihslfsee
      121 tpvvlqlaps eervymvgka nsvfedlsvt lrqlrnrlfq ensvlsslpl nslsrnnevd
      181 llflselqvl hdissllsrh khlakdhspd lyslelagld eigkrygeds eqfrdaskil
      241 vdalqkfadd myslyggnav velvtvksfd tslirktrti leakqaknpa spynlaykyn
      301 feysvvfnmv lwimialala viitsyniwn mdpgydsiiy rmtnqkirmd
//
LOCUS       NP_001340028             324 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            5 [Homo sapiens].
ACCESSION   NP_001340028 XP_016880358
VERSION     NP_001340028.1
DBSOURCE    REFSEQ: accession NM_001353099.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            On Jun 29, 2017 this sequence version replaced XP_016880358.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.82569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..324
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 5"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=35908
     Region          1..93
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          134..318
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..324
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353099.2:420..1394"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mgkvqvyqep nretrvqiqe svrgkdvfii qtvskdvntt imellimvya cktscaksii
       61 gvipyfpysk qckmrkrgsi vskllasmmc kaglthlitm dlhqkeiqgf fnipvdnlra
      121 spfllqyiqe eipdyrnavi vakspasakr aqsfaerlrl giavihgeaq daesdlvdgr
      181 hsppmvrsva aihpsleipm lipkekppit vvgdvggria iivddiiddv dsflaaaetl
      241 kergaykifv mathgllssd aprrieesai devvvtntip hevqklqcpk iktvdismil
      301 seairrihng esmsylfrni gldd
//
LOCUS       NP_002679                369 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-5 isoform 1 [Homo sapiens].
ACCESSION   NP_002679
VERSION     NP_002679.2
DBSOURCE    REFSEQ: accession NM_002688.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Marttinen,M., Ferreira,C.B., Paldanius,K.M.A., Takalo,M.,
            Natunen,T., Makinen,P., Leppanen,L., Leinonen,V., Tanigaki,K.,
            Kang,G., Hiroi,N., Soininen,H., Rilla,K., Haapasalo,A. and
            Hiltunen,M.
  TITLE     Presynaptic Vesicle Protein SEPTIN5 Regulates the Degradation of
            APP C-Terminal Fragments and the Levels of Abeta
  JOURNAL   Cells 9 (11), 2482 (2020)
   PUBMED   33203136
  REMARK    GeneRIF: Presynaptic Vesicle Protein SEPTIN5 Regulates the
            Degradation of APP C-Terminal Fragments and the Levels of Abeta.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Caltagarone,J., Rhodes,J., Honer,W.G. and Bowser,R.
  TITLE     Localization of a novel septin protein, hCDCrel-1, in neurons of
            human brain
  JOURNAL   Neuroreport 9 (12), 2907-2912 (1998)
   PUBMED   9760144
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Yagi,M., Zieger,B., Roth,G.J. and Ware,J.
  TITLE     Structure and expression of the human septin gene HCDCREL-1
  JOURNAL   Gene 212 (2), 229-236 (1998)
   PUBMED   9611266
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Hsu,S.C., Hazuka,C.D., Roth,R., Foletti,D.L., Heuser,J. and
            Scheller,R.H.
  TITLE     Subunit composition, protein interactions, and structures of the
            mammalian brain sec6/8 complex and septin filaments
  JOURNAL   Neuron 20 (6), 1111-1122 (1998)
   PUBMED   9655500
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Megonigal,M.D., Rappaport,E.F., Jones,D.H., Williams,T.M.,
            Lovett,B.D., Kelly,K.M., Lerou,P.H., Moulton,T., Budarf,M.L. and
            Felix,C.A.
  TITLE     t(11;22)(q23;q11.2) In acute myeloid leukemia of infant twins fuses
            MLL with hCDCrel, a cell division cycle gene in the genomic region
            of deletion in DiGeorge and velocardiofacial syndromes
  JOURNAL   Proc Natl Acad Sci U S A 95 (11), 6413-6418 (1998)
   PUBMED   9600980
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Aug 18;95(17):10344]
REFERENCE   9  (residues 1 to 369)
  AUTHORS   McKie,J.M., Sutherland,H.F., Harvey,E., Kim,U.J. and Scambler,P.J.
  TITLE     A human gene similar to Drosophila melanogaster peanut maps to the
            DiGeorge syndrome region of 22q11
  JOURNAL   Hum Genet 101 (1), 6-12 (1997)
   PUBMED   9385360
REFERENCE   10 (residues 1 to 369)
  AUTHORS   Zieger,B., Hashimoto,Y. and Ware,J.
  TITLE     Alternative expression of platelet glycoprotein Ib(beta) mRNA from
            an adjacent 5' gene with an imperfect polyadenylation signal
            sequence
  JOURNAL   J Clin Invest 99 (3), 520-525 (1997)
   PUBMED   9022087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC025261.1.
            
            On Aug 30, 2000 this sequence version replaced NP_002679.1.
            
            Summary: This gene is a member of the septin gene family of
            nucleotide binding proteins, originally described in yeast as cell
            division cycle regulatory proteins. Septins are highly conserved in
            yeast, Drosophila, and mouse and appear to regulate cytoskeletal
            organization. Disruption of septin function disturbs cytokinesis
            and results in large multinucleate or polyploid cells. This gene is
            mapped to 22q11, the region frequently deleted in DiGeorge and
            velocardiofacial syndromes. A translocation involving the MLL gene
            and this gene has also been reported in patients with acute myeloid
            leukemia. Alternative splicing results in multiple transcript
            variants. The presence of a non-consensus polyA signal (AACAAT) in
            this gene also results in read-through transcription into the
            downstream neighboring gene (GP1BB; platelet glycoprotein Ib),
            whereby larger, non-coding transcripts are produced. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025261.1, U74628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000455784.7/ ENSP00000391311.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..369
                     /product="septin-5 isoform 1"
                     /EC_number="3.1.5.1"
                     /note="peanut-like 1; cell division control related
                     protein 1; platelet glycoprotein Ib beta chain"
                     /calculated_mol_wt=42646
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Region          42..313
                     /region_name="Septin"
                     /note="pfam00735"
                     /db_xref="CDD:395596"
     Region          51..58
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            51..58
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(53..59,108,111,189..190,192,248..249)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            83..91
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            85
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          108..111
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            108..111
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(110..145,146..155)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            168
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Region          189..192
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            189..192
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99719.1)"
     Site            248..250
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2Q6; propagated from
                     UniProtKB/Swiss-Prot (Q99719.1)"
     CDS             1..369
                     /gene="SEPTIN5"
                     /gene_synonym="CDCREL; CDCREL-1; CDCREL1; H5; HCDCREL-1;
                     PNUTL1; SEPT5; Septin-5"
                     /coded_by="NM_002688.6:87..1196"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13764.1"
                     /db_xref="GeneID:5413"
                     /db_xref="HGNC:HGNC:9164"
                     /db_xref="MIM:602724"
ORIGIN      
        1 mstglryksk latpedkqdi dkqyvgfatl pnqvhrksvk kgfdftlmva gesglgkstl
       61 vhslfltdly kdrkllsaee risqtveilk htvdieekgv klkltivdtp gfgdavnnte
      121 cwkpitdyvd qqfeqyfrde sglnrkniqd nrvhcclyfi spfghglrpv dvgfmkalhe
      181 kvnivpliak adclvpseir klkerireei dkfgihvyqf pecdsdeded fkqqdrelke
      241 sapfavigsn tvveakgqrv rgrlypwgiv evenqahcdf vklrnmlirt hmhdlkdvtc
      301 dvhyenyrah ciqqmtsklt qdsrmespip ilplptpdae teklirmkde elrrmqemlq
      361 rmkqqmqdq
//
LOCUS       NP_612449                673 aa            linear   PRI 20-NOV-2025
DEFINITION  vasorin precursor [Homo sapiens].
ACCESSION   NP_612449
VERSION     NP_612449.2
DBSOURCE    REFSEQ: accession NM_138440.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Qin,Z., Zhong,Y., Li,P., Ma,Z., Kang,H., Huang,Y., Zhong,Y. and
            Wang,L.
  TITLE     Vasorin promotes endothelial differentiation of glioma stem cells
            via stimulating the transcription of VEGFR2
  JOURNAL   FASEB J 38 (10), e23682 (2024)
   PUBMED   38780524
  REMARK    GeneRIF: Vasorin promotes endothelial differentiation of glioma
            stem cells via stimulating the transcription of VEGFR2.
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Liang,J. and Smith,A.W.
  TITLE     The Oligomeric State of Vasorin in the Plasma Membrane Measured
            Non-Invasively by Quantitative Fluorescence Fluctuation
            Spectroscopy
  JOURNAL   Int J Mol Sci 25 (7), 4115 (2024)
   PUBMED   38612924
  REMARK    GeneRIF: The Oligomeric State of Vasorin in the Plasma Membrane
            Measured Non-Invasively by Quantitative Fluorescence Fluctuation
            Spectroscopy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Wan,F., Li,H., Huang,S., Sun,J., Li,J., Li,Y., Yang,L. and He,M.
  TITLE     Vasorin promotes proliferation and migration via STAT3 signaling
            and acts as a promising therapeutic target of hepatocellular
            carcinoma
  JOURNAL   Cell Signal 110, 110809 (2023)
   PUBMED   37454705
  REMARK    GeneRIF: Vasorin promotes proliferation and migration via STAT3
            signaling and acts as a promising therapeutic target of
            hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Taggi,M., Liuzzi,F., Botticelli,L., De Carlini,S., Longo,M.,
            Donno,V., Fabbiani,L. and La Marca,A.
  TITLE     Evidence for the expression of vasorin in the human female
            reproductive tissues
  JOURNAL   Gynecol Endocrinol 39 (1), 2224457 (2023)
   PUBMED   37331376
  REMARK    GeneRIF: Evidence for the expression of vasorin in the human female
            reproductive tissues.
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Ikeda,Y., Imai,Y., Kumagai,H., Nosaka,T., Morikawa,Y., Hisaoka,T.,
            Manabe,I., Maemura,K., Nakaoka,T., Imamura,T., Miyazono,K.,
            Komuro,I., Nagai,R. and Kitamura,T.
  TITLE     Vasorin, a transforming growth factor beta-binding protein
            expressed in vascular smooth muscle cells, modulates the arterial
            response to injury in vivo
  JOURNAL   Proc Natl Acad Sci U S A 101 (29), 10732-10737 (2004)
   PUBMED   15247411
  REMARK    GeneRIF: results suggest that down-regulation of vasorin expression
            contributes to neointimal formation after vascular injury and that
            vasorin modulates cellular responses to pathological stimuli in the
            vessel wall [vasorin]
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC068575.1, BC013767.1 and AC012676.5.
            
            On Feb 23, 2006 this sequence version replaced NP_612449.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068575.1, AY358299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304735.4/ ENSP00000306864.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..673
                     /product="vasorin precursor"
                     /note="protein slit-like 2"
                     /calculated_mol_wt=69357
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2374
     Region          23..54
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     mat_peptide     24..673
                     /product="Vasorin. /id=PRO_0000232630"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
                     /calculated_mol_wt=69357
     Region          34..56
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          52..74
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          57..77
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <72..>295
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          77..98
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          78..101
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..122
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          102..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            117
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320;
                     propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          125..146
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          126..149
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          149..170
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          150..193
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          171..191
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          193..214
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          194..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          217..238
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          218..240
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          240..262
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          241..265
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          265..287
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          266..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          270..>349
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          358..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Region          409..440
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          466..535
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            500
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6EMK4.1)"
     Site            576..596
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6EMK4.1)"
     CDS             1..673
                     /gene="VASN"
                     /gene_synonym="SLITL2"
                     /coded_by="NM_138440.3:156..2177"
                     /db_xref="CCDS:CCDS10514.1"
                     /db_xref="GeneID:114990"
                     /db_xref="HGNC:HGNC:18517"
                     /db_xref="MIM:608843"
ORIGIN      
        1 mcsrvplllp lllllalgpg vqgcpsgcqc sqpqtvfcta rqgttvprdv ppdtvglyvf
       61 engitmldag sfaglpglql ldlsqnqias lpsgvfqpla nlsnldltan rlheitnetf
      121 rglrrlerly lgknrirhiq pgafdtldrl lelklqdnel ralpplrlpr lllldlshns
      181 llalepgild tanvealrla glglqqldeg lfsrlrnlhd ldvsdnqler vppvirglrg
      241 ltrlrlagnt riaqlrpedl aglaalqeld vsnlslqalp gdlsglfprl rllaaarnpf
      301 ncvcplswfg pwvreshvtl aspeetrchf ppknagrlll eldyadfgcp attttatvpt
      361 trpvvrepta lssslaptwl sptepateap sppstapptv gpvpqpqdcp pstclnggtc
      421 hlgtrhhlac lcpegftgly cesqmgqgtr psptpvtprp prsltlgiep vsptslrvgl
      481 qrylqgssvq lrslrltyrn lsgpdkrlvt lrlpaslaey tvtqlrpnat ysvcvmplgp
      541 grvpegeeac geahtppavh snhapvtqar egnlplliap alaavllaal aavgaaycvr
      601 rgramaaaaq dkgqvgpgag plelegvkvp lepgpkateg ggealpsgse cevplmgfpg
      661 pglqsplhak pyi
//
LOCUS       NP_671712                229 aa            linear   PRI 20-NOV-2025
DEFINITION  Kv channel-interacting protein 4 isoform 4 [Homo sapiens].
ACCESSION   NP_671712
VERSION     NP_671712.1
DBSOURCE    REFSEQ: accession NM_147183.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Mosley,J.D., Shaffer,C.M., Van Driest,S.L., Weeke,P.E., Wells,Q.S.,
            Karnes,J.H., Velez Edwards,D.R., Wei,W.Q., Teixeira,P.L.,
            Bastarache,L., Crawford,D.C., Li,R., Manolio,T.A., Bottinger,E.P.,
            McCarty,C.A., Linneman,J.G., Brilliant,M.H., Pacheco,J.A.,
            Thompson,W., Chisholm,R.L., Jarvik,G.P., Crosslin,D.R.,
            Carrell,D.S., Baldwin,E., Ralston,J., Larson,E.B., Grafton,J.,
            Scrol,A., Jouni,H., Kullo,I.J., Tromp,G., Borthwick,K.M.,
            Kuivaniemi,H., Carey,D.J., Ritchie,M.D., Bradford,Y., Verma,S.S.,
            Chute,C.G., Veluchamy,A., Siddiqui,M.K., Palmer,C.N., Doney,A.,
            MahmoudPour,S.H., Maitland-van der Zee,A.H., Morris,A.D.,
            Denny,J.C. and Roden,D.M.
  TITLE     A genome-wide association study identifies variants in KCNIP4
            associated with ACE inhibitor-induced cough
  JOURNAL   Pharmacogenomics J 16 (3), 231-237 (2016)
   PUBMED   26169577
  REMARK    GeneRIF: Results indicate that SNPs in KCNIP4 may modulate ACE
            inhibitor-induced cough risk.
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Kitazawa,M., Kubo,Y. and Nakajo,K.
  TITLE     The stoichiometry and biophysical properties of the Kv4 potassium
            channel complex with K+ channel-interacting protein (KChIP)
            subunits are variable, depending on the relative expression level
  JOURNAL   J Biol Chem 289 (25), 17597-17609 (2014)
   PUBMED   24811166
  REMARK    GeneRIF: Subunit counting by single-molecule imaging revealed that
            the bound number of KChIP4 in each Kv4.2.KChIP4 complex was
            dependent on the expression level of KChIP4.
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Bonne,A., Vreede,L., Kuiper,R.P., Bodmer,D., Jansen,C., Eleveld,M.,
            van Erp,F., Arkesteijn,G., Hoogerbrugge,N., van Ravenswaaij,C.,
            Schoenmakers,E.F. and Geurts van Kessel,A.
  TITLE     Mapping of constitutional translocation breakpoints in renal cell
            cancer patients: identification of KCNIP4 as a candidate gene
  JOURNAL   Cancer Genet Cytogenet 179 (1), 11-18 (2007)
   PUBMED   17981209
  REMARK    GeneRIF: Mutation of KCNIP4 is associated with renal cell
            carcinoma.
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Chen,C.P., Lee,L. and Chang,L.S.
  TITLE     Effects of metal-binding properties of human Kv channel-interacting
            proteins on their molecular structure and binding with Kv4.2
            channel
  JOURNAL   Protein J 25 (5), 345-351 (2006)
   PUBMED   16951992
  REMARK    GeneRIF: The conformational change with metal-bound KChIP4.1 is
            crucial for its interaction with Kv channel but not for KChIP2.2,
            and that the Mg2+- and Ca2+-binding properties of KChIP2.2 and
            KChIP4.1 have different effects on their molecular structure.
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Pruunsild,P. and Timmusk,T.
  TITLE     Structure, alternative splicing, and expression of the human and
            mouse KCNIP gene family
  JOURNAL   Genomics 86 (5), 581-593 (2005)
   PUBMED   16112838
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Morohashi,Y., Hatano,N., Ohya,S., Takikawa,R., Watabiki,T.,
            Takasugi,N., Imaizumi,Y., Tomita,T. and Iwatsubo,T.
  TITLE     Molecular cloning and characterization of CALP/KChIP4, a novel
            EF-hand protein interacting with presenilin 2 and voltage-gated
            potassium channel subunit Kv4
  JOURNAL   J Biol Chem 277 (17), 14965-14975 (2002)
   PUBMED   11847232
  REMARK    GeneRIF: cloning and investigation of interaction with presenilin 2
            and voltage-gated potassium channel subunit Kv4
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Holmqvist,M.H., Cao,J., Hernandez-Pineda,R., Jacobson,M.D.,
            Carroll,K.I., Sung,M.A., Betty,M., Ge,P., Gilbride,K.J.,
            Brown,M.E., Jurman,M.E., Lawson,D., Silos-Santiago,I., Xie,Y.,
            Covarrubias,M., Rhodes,K.J., Distefano,P.S. and An,W.F.
  TITLE     Elimination of fast inactivation in Kv4 A-type potassium channels
            by an auxiliary subunit domain
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 1035-1040 (2002)
   PUBMED   11805342
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY118170.1, AC104065.3 and
            BX648990.1.
            
            Summary: This gene encodes a member of the family of voltage-gated
            potassium (Kv) channel-interacting proteins (KCNIPs), which belong
            to the recoverin branch of the EF-hand superfamily. Members of the
            KCNIP family are small calcium binding proteins. They all have
            EF-hand-like domains, and differ from each other in the N-terminus.
            They are integral subunit components of native Kv4 channel
            complexes. They may regulate A-type currents, and hence neuronal
            excitability, in response to changes in intracellular calcium. This
            protein member also interacts with presenilin. Multiple
            alternatively spliced transcript variants encoding distinct
            isoforms have been identified for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (4) has an alternate exon which
            contains an in-frame start codon, as compared to variant 1. Isoform
            4, also known as KCHIP4.4, thus has an alternate N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY118170.1, SRR1803615.13220.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31-p15.2"
     Protein         1..229
                     /product="Kv channel-interacting protein 4 isoform 4"
                     /note="calsenilin-like protein; a-type potassium channel
                     modulatory protein 4; Kv channel interacting protein 4"
                     /calculated_mol_wt=26371
     Region          78..125
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     Region          <107..214
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..229
                     /gene="KCNIP4"
                     /gene_synonym="CALP; KCHIP4"
                     /coded_by="NM_147183.3:1..690"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS3428.1"
                     /db_xref="GeneID:80333"
                     /db_xref="HGNC:HGNC:30083"
                     /db_xref="MIM:608182"
ORIGIN      
        1 mnleglemia vlivivlfvk lleqfgliea gledsvedel ematvrhrpe alelleaqsk
       61 ftkkelqily rgfknecpsg vvneetfkei ysqffpqgds ttyahflfna fdtdhngavs
      121 fedfikglsi llrgtvqekl nwafnlydin kdgyitkeem ldimkaiydm mgkctypvlk
      181 edaprqhvet ffqkmdknkd gvvtidefie scqkdenimr smqlfenvi
//
LOCUS       NP_001171033             556 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A
            beta isoform isoform d [Homo sapiens].
ACCESSION   NP_001171033
VERSION     NP_001171033.1
DBSOURCE    REFSEQ: accession NM_001177562.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Peng,S., He,T., Liu,Y., Zheng,L., Zhong,Y., Niu,Z., Zhang,M. and
            Yang,S.
  TITLE     Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B by
            Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs
  JOURNAL   Stem Cell Rev Rep 19 (6), 1981-1993 (2023)
   PUBMED   37243830
  REMARK    GeneRIF: Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B
            by Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs.
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Du,M., Yuan,L., Zhang,Z., Zhang,C., Zhu,M., Zhang,Z., Li,R.,
            Zhao,X., Liang,H., Li,Y., Jiang,H., Qiao,J. and Yin,Y.
  TITLE     PPP2R1B is modulated by ubiquitination and is essential for
            spermatogenesis
  JOURNAL   FASEB J 35 (5), e21564 (2021)
   PUBMED   33913576
  REMARK    GeneRIF: PPP2R1B is modulated by ubiquitination and is essential
            for spermatogenesis.
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Adler,H.T., Nallaseth,F.S., Walter,G. and Tkachuk,D.C.
  TITLE     HRX leukemic fusion proteins form a heterocomplex with the
            leukemia-associated protein SET and protein phosphatase 2A
  JOURNAL   J Biol Chem 272 (45), 28407-28414 (1997)
   PUBMED   9353299
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Hendrix,P., Mayer-Jackel,R.E., Cron,P., Goris,J., Hofsteenge,J.,
            Merlevede,W. and Hemmings,B.A.
  TITLE     Structure and expression of a 72-kDa regulatory subunit of protein
            phosphatase 2A. Evidence for different size forms produced by
            alternative splicing
  JOURNAL   J Biol Chem 268 (20), 15267-15276 (1993)
   PUBMED   8392071
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Kamibayashi,C., Lickteig,R.L., Estes,R., Walter,G. and Mumby,M.C.
  TITLE     Expression of the A subunit of protein phosphatase 2A and
            characterization of its interactions with the catalytic and
            regulatory subunits
  JOURNAL   J Biol Chem 267 (30), 21864-21872 (1992)
   PUBMED   1328247
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Hemmings,B.A., Adams-Pearson,C., Maurer,F., Muller,P., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Stone,S.R.
  TITLE     alpha- and beta-forms of the 65-kDa subunit of protein phosphatase
            2A have a similar 39 amino acid repeating structure
  JOURNAL   Biochemistry 29 (13), 3166-3173 (1990)
   PUBMED   2159327
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC402587.1, AK294716.1,
            AP001781.5, AF163473.1 and AP000925.6.
            
            Summary: This gene encodes a constant regulatory subunit of protein
            phosphatase 2. Protein phosphatase 2 is one of the four major
            Ser/Thr phosphatases, and it is implicated in the negative control
            of cell growth and division. It consists of a common heteromeric
            core enzyme, which is composed of a catalytic subunit and a
            constant regulatory subunit, that associates with a variety of
            regulatory subunits. The constant regulatory subunit A serves as a
            scaffolding molecule to coordinate the assembly of the catalytic
            subunit and a variable regulatory B subunit. This gene encodes a
            beta isoform of the constant regulatory subunit A. Mutations in
            this gene have been associated with some lung and colon cancers.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Apr 2010].
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            coding region compared to variant 1. The resulting isoform (d) is
            shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.235679.1,
                                           SRR1803615.120435.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..556
                     /product="serine/threonine-protein phosphatase 2A 65 kDa
                     regulatory subunit A beta isoform isoform d"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, structural/regulatory
                     subunit A, beta; protein phosphatase 2, regulatory subunit
                     A, beta"
                     /calculated_mol_wt=61183
     Region          25..49
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(41..42,45,48..49,79..80,83,86..87,90,118..119,122,
                     125..126,129,157..158,161,164..165)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          63..90
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          100..130
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          116..276
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          139..165
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          217..245
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          257..281
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(273..274,277,280..281,312..313,353,356..357,360,
                     388..389,392,395..396,399,427..428,431,434..435,466..467,
                     470,473..474)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          295..360
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          370..400
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          409..435
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          446..475
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          485..511
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          524..553
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..556
                     /gene="PPP2R1B"
                     /gene_synonym="PP2A-Abeta; PR65B"
                     /coded_by="NM_001177562.2:29..1699"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53708.1"
                     /db_xref="GeneID:5519"
                     /db_xref="HGNC:HGNC:9303"
                     /db_xref="MIM:603113"
ORIGIN      
        1 magaselgtg pgaaggdgdd slypiavlid elrnedvqlr lnsikklsti alalgvertr
       61 sellpfltdt iydedevlla laeqlgnftg lvggpdfahc llpplenlat veetvvrdka
      121 veslrqisqe htpvaleayf vplvkrlasg dwftsrtsac glfsvcypra snavkaeirq
      181 qfrslcsddt pmvrraaask lgefakvlel dsvkseivpl ftslasdeqd svrllaveac
      241 vsiaqllsqd dletlvmptl rqaaedkswr vrymvadrfs elqkamgpki tlndlipafq
      301 nllkdceaev raaaahkvke lgenlpiedr etiimnqilp yikcpdvrln iisnldcvne
      361 vigirqlsqs llpaivelae dakwrvrlai ieympllagq lgveffdekl nslcmawlvd
      421 hvyaireaat nnlmklvqkf gtewaqntiv pkvlvmandp nylhrmttlf cinalseacg
      481 qeittkqmlp ivlkmagdqv anvrfnvaks lqkigpildt nalqgevkpv lqklgqdedm
      541 dvkyfaqeai svlala
//
LOCUS       NP_003737                 89 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein light chain 1, cytoplasmic [Homo sapiens].
ACCESSION   NP_003737
VERSION     NP_003737.1
DBSOURCE    REFSEQ: accession NM_003746.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Greenwood,M., Gillard,B.T., Murphy,D. and Greenwood,M.P.
  TITLE     Dimerization of hub protein DYNLL1 and bZIP transcription factor
            CREB3L1 enhances transcriptional activation of CREB3L1 target genes
            like arginine vasopressin
  JOURNAL   Peptides 179, 171269 (2024)
   PUBMED   38960286
  REMARK    GeneRIF: Dimerization of hub protein DYNLL1 and bZIP transcription
            factor CREB3L1 enhances transcriptional activation of CREB3L1
            target genes like arginine vasopressin.
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Swift,M.L., Zhou,R., Syed,A., Moreau,L.A., Tomasik,B., Tainer,J.A.,
            Konstantinopoulos,P.A., D'Andrea,A.D., He,Y.J. and Chowdhury,D.
  TITLE     Dynamics of the DYNLL1-MRE11 complex regulate DNA end resection and
            recruitment of Shieldin to DSBs
  JOURNAL   Nat Struct Mol Biol 30 (10), 1456-1467 (2023)
   PUBMED   37696958
REFERENCE   4  (residues 1 to 89)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Crepieux,P., Kwon,H., Leclerc,N., Spencer,W., Richard,S., Lin,R.
            and Hiscott,J.
  TITLE     I kappaB alpha physically interacts with a cytoskeleton-associated
            protein through its signal response domain
  JOURNAL   Mol Cell Biol 17 (12), 7375-7385 (1997)
   PUBMED   9372968
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Jaffrey,S.R. and Snyder,S.H.
  TITLE     PIN: an associated protein inhibitor of neuronal nitric oxide
            synthase
  JOURNAL   Science 274 (5288), 774-777 (1996)
   PUBMED   8864115
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Dick,T., Ray,K., Salz,H.K. and Chia,W.
  TITLE     Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects
            and apoptotic cell death in Drosophila melanogaster
  JOURNAL   Mol Cell Biol 16 (5), 1966-1977 (1996)
   PUBMED   8628263
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU598428.1 and AC063943.23.
            
            Summary: Cytoplasmic dyneins are large enzyme complexes with a
            molecular mass of about 1,200 kD. They contain two force-producing
            heads formed primarily from dynein heavy chains, and stalks linking
            the heads to a basal domain, which contains a varying number of
            accessory intermediate chains. The complex is involved in
            intracellular transport and motility. The protein described in this
            record is a light chain and exists as part of this complex but also
            physically interacts with and inhibits the activity of neuronal
            nitric oxide synthase. Binding of this protein destabilizes the
            neuronal nitric oxide synthase dimer, a conformation necessary for
            activity, and it may regulate numerous biologic processes through
            its effects on nitric oxide synthase activity. Alternate
            transcriptional splice variants have been characterized. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) contains a distinct 5' UTR,
            including an alternate, downstream transcription initiation site.
            Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV759540.1, BM765041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242577.11/ ENSP00000242577.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..89
                     /product="dynein light chain 1, cytoplasmic"
                     /note="protein inhibitor of neuronal nitric oxide
                     synthase; dynein, cytoplasmic, light polypeptide 1; 8 kDa
                     dynein light chain; cytoplasmic dynein light polypeptide"
                     /calculated_mol_wt=10235
     Region          5..88
                     /region_name="DLC-like_DYNLL1_DYNLL2"
                     /note="dynein light chain (DLC)-like domain found in the
                     cytoplasmic dynein light chain 1 (DYNLL1) family; cd21452"
                     /db_xref="CDD:412000"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63167.1)"
     Region          67..89
                     /region_name="Interaction with ESR1.
                     /evidence=ECO:0000269|PubMed:15891768"
                     /note="propagated from UniProtKB/Swiss-Prot (P63167.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15193260,
                     ECO:0000269|PubMed:30464262, ECO:0000269|PubMed:37696958;
                     propagated from UniProtKB/Swiss-Prot (P63167.1)"
     CDS             1..89
                     /gene="DYNLL1"
                     /gene_synonym="DLC1; DLC8; DNCL1; DNCLC1; hdlc1; LC8;
                     LC8a; PIN"
                     /coded_by="NM_003746.3:111..380"
                     /db_xref="CCDS:CCDS9200.1"
                     /db_xref="GeneID:8655"
                     /db_xref="HGNC:HGNC:15476"
                     /db_xref="MIM:601562"
ORIGIN      
        1 mcdrkavikn admseemqqd svecatqale kyniekdiaa hikkefdkky nptwhcivgr
       61 nfgsyvthet khfiyfylgq vaillfksg
//
LOCUS       NP_001356681              78 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein Sm D2 isoform 3 [Homo sapiens].
ACCESSION   NP_001356681
VERSION     NP_001356681.1
DBSOURCE    REFSEQ: accession NM_001369752.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Chang,C., Li,L., Su,L., Yang,F., Zha,Q., Sun,M., Tao,L., Wang,M.,
            Song,K., Jiang,L., Gao,H., Liang,Y., Xu,C., Yong,C., Wang,M.,
            Huang,J., Liu,J., Jin,W., Lv,W., Dong,H., Li,Q., Bu,F., Yan,S.,
            Qi,H., Zhao,S., Zhu,Y., Wang,Y., Shi,J., Qiao,Y., Xu,J., Chabot,B.
            and Chen,J.
  TITLE     Intron Retention of DDX39A Driven by SNRPD2 is a Crucial Splicing
            Axis for Oncogenic MYC/Spliceosome Program in Hepatocellular
            Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2403387 (2024)
   PUBMED   39018261
  REMARK    GeneRIF: Intron Retention of DDX39A Driven by SNRPD2 is a Crucial
            Splicing Axis for Oncogenic MYC/Spliceosome Program in
            Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Kambach,C., Walke,S., Young,R., Avis,J.M., de la Fortelle,E.,
            Raker,V.A., Luhrmann,R., Li,J. and Nagai,K.
  TITLE     Crystal structures of two Sm protein complexes and their
            implications for the assembly of the spliceosomal snRNPs
  JOURNAL   Cell 96 (3), 375-387 (1999)
   PUBMED   10025403
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 78)
  AUTHORS   Lehmeier,T., Raker,V., Hermann,H. and Luhrmann,R.
  TITLE     cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
            ribonucleoproteins: evidence for a direct D1-D2 interaction
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12317-12321 (1994)
   PUBMED   7527560
REFERENCE   9  (residues 1 to 78)
  AUTHORS   Lehmeier,T., Foulaki,K. and Luhrmann,R.
  TITLE     Evidence for three distinct D proteins, which react differentially
            with anti-Sm autoantibodies, in the cores of the major snRNPs U1,
            U2, U4/U6 and U5
  JOURNAL   Nucleic Acids Res 18 (22), 6475-6484 (1990)
   PUBMED   1701240
REFERENCE   10 (residues 1 to 78)
  AUTHORS   Rokeach,L.A., Haselby,J.A. and Hoch,S.O.
  TITLE     Molecular cloning of a cDNA encoding the human Sm-D autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 85 (13), 4832-4836 (1988)
   PUBMED   3260384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007191.1 and DW433845.1.
            
            Summary: The protein encoded by this gene belongs to the small
            nuclear ribonucleoprotein core protein family. It is required for
            pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB146406.1, DW433845.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..78
                     /product="small nuclear ribonucleoprotein Sm D2 isoform 3"
                     /note="snRNP core protein D2; small nuclear
                     ribonucleoprotein Sm D2; small nuclear ribonucleoprotein
                     D2 polypeptide 16.5kDa"
                     /calculated_mol_wt=8646
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62316.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P62316.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62316.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62316.1)"
     Region          24..>60
                     /region_name="Sm_like"
                     /note="Sm and related proteins; cl00259"
                     /db_xref="CDD:469694"
     CDS             1..78
                     /gene="SNRPD2"
                     /gene_synonym="Sm-D2; SMD2; SNRPD1"
                     /coded_by="NM_001369752.1:66..302"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92646.1"
                     /db_xref="GeneID:6633"
                     /db_xref="HGNC:HGNC:11159"
                     /db_xref="MIM:601061"
ORIGIN      
        1 msllnkpkse mtpeelqkre eeefntgpls vltqsvknnt qvlincrnnk kllgrvkafd
       61 sasppcsppg tatwcwrt
//
LOCUS       NP_071451               1025 aa            linear   PRI 20-NOV-2025
DEFINITION  interferon-induced helicase C domain-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_071451
VERSION     NP_071451.2
DBSOURCE    REFSEQ: accession NM_022168.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1025)
  AUTHORS   Zhang,S., Huang,W., Wu,X., Chen,H., Wang,L., Chao,J., Xie,J. and
            Qiu,H.
  TITLE     IBR1, a novel endogenous IFIH1-binding dsRNA, governs IFIH1
            activation and M1 macrophage polarisation in ARDS
  JOURNAL   Clin Transl Med 14 (9), e70027 (2024)
   PUBMED   39313944
  REMARK    GeneRIF: IBR1, a novel endogenous IFIH1-binding dsRNA, governs
            IFIH1 activation and M1 macrophage polarisation in ARDS.
REFERENCE   2  (residues 1 to 1025)
  AUTHORS   Song,W., Bian,W.J., Li,H., Guo,Q.H., Wang,J., Tang,B., Zhang,J.Y.,
            Wei,W., Liu,X.R., Liao,W.P., Li,B. and He,N.
  TITLE     IFIH1 variants are associated with generalised epilepsy preceded by
            febrile seizures
  JOURNAL   J Med Genet 61 (9), 895-903 (2024)
   PUBMED   38964834
  REMARK    GeneRIF: IFIH1 variants are associated with generalised epilepsy
            preceded by febrile seizures.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1025)
  AUTHORS   Guney,M.H., Nagalekshmi,K., McCauley,S.M., Carbone,C., Aydemir,O.
            and Luban,J.
  TITLE     IFIH1 (MDA5) is required for innate immune detection of
            intron-containing RNA expressed from the HIV-1 provirus
  JOURNAL   Proc Natl Acad Sci U S A 121 (29), e2404349121 (2024)
   PUBMED   38985764
  REMARK    GeneRIF: IFIH1 (MDA5) is required for innate immune detection of
            intron-containing RNA expressed from the HIV-1 provirus.
REFERENCE   4  (residues 1 to 1025)
  AUTHORS   Chan,Y.J., Liu,N.T., Hsin,F., Lu,J.Y., Lin,J.Y. and Liu,H.M.
  TITLE     Temporal regulation of MDA5 inactivation by Caspase-3 dependent
            cleavage of 14-3-3eta
  JOURNAL   PLoS Pathog 20 (6), e1012287 (2024)
   PUBMED   38843304
  REMARK    GeneRIF: Temporal regulation of MDA5 inactivation by Caspase-3
            dependent cleavage of 14-3-3eta.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1025)
  AUTHORS   Rizk,S.K., Farag,A.G.A., El-Ghlban,S. and Eldin Metwally,I.S.
  TITLE     Identifying the association between polymorphisms in the GZMB and
            IFIH1 genes and psoriasis in Egyptians
  JOURNAL   J Immunoassay Immunochem 45 (3), 189-209 (2024)
   PUBMED   38733267
  REMARK    GeneRIF: Identifying the association between polymorphisms in the
            GZMB and IFIH1 genes and psoriasis in Egyptians.
REFERENCE   6  (residues 1 to 1025)
  AUTHORS   Kovacsovics,M., Martinon,F., Micheau,O., Bodmer,J.L., Hofmann,K.
            and Tschopp,J.
  TITLE     Overexpression of Helicard, a CARD-containing helicase cleaved
            during apoptosis, accelerates DNA degradation
  JOURNAL   Curr Biol 12 (10), 838-843 (2002)
   PUBMED   12015121
  REMARK    Erratum:[Curr Biol. 2002 Sep 17;12(18):1633.]
REFERENCE   7  (residues 1 to 1025)
  AUTHORS   Kang,D.C., Gopalkrishnan,R.V., Wu,Q., Jankowsky,E., Pyle,A.M. and
            Fisher,P.B.
  TITLE     mda-5: An interferon-inducible putative RNA helicase with
            double-stranded RNA-dependent ATPase activity and melanoma
            growth-suppressive properties
  JOURNAL   Proc Natl Acad Sci U S A 99 (2), 637-642 (2002)
   PUBMED   11805321
  REMARK    GeneRIF: mda-5: An interferon-inducible putative RNA helicase with
            double-stranded RNA-dependent ATPase activity and melanoma
            growth-suppressive properties
REFERENCE   8  (residues 1 to 1025)
  AUTHORS   Chaudhary,P.M., Eby,M.T., Jasmin,A., Kumar,A., Liu,L. and Hood,L.
  TITLE     Activation of the NF-kappaB pathway by caspase 8 and its homologs
  JOURNAL   Oncogene 19 (39), 4451-4460 (2000)
   PUBMED   11002417
REFERENCE   9  (residues 1 to 1025)
  AUTHORS   Lin,R., Heylbroeck,C., Genin,P., Pitha,P.M. and Hiscott,J.
  TITLE     Essential role of interferon regulatory factor 3 in direct
            activation of RANTES chemokine transcription
  JOURNAL   Mol Cell Biol 19 (2), 959-966 (1999)
   PUBMED   9891032
REFERENCE   10 (residues 1 to 1025)
  AUTHORS   Crow,Y.J.
  TITLE     Aicardi-Goutieres Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301648
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC046208.1, AF095844.1,
            BC111750.1 and AC007750.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 24, 2003 this sequence version replaced NP_071451.1.
            
            Summary: IFIH1 encodes MDA5 which is an intracellular sensor of
            viral RNA that triggers the innate immune response. Sensing RNA
            length and secondary structure, MDA5 binds dsRNA oligonucleotides
            with a modified DExD/H-box helicase core and a C-terminal domain,
            thus leading to a proinflammatory response that includes
            interferons. It has been shown that Coronaviruses (CoVs) as well as
            various other virus families, are capable of evading the
            MDA5-dependent interferon response, thus impeding the activation of
            the innate immune response to infection. MDA5 has also been shown
            to play an important role in enhancing natural killer cell function
            in malaria infection. In addition to its protective role in
            antiviral responses, MDA5 has been implicated in autoimmune and
            autoinflammatory diseases such as type 1 diabetes, systemic lupus
            erythematosus, and Aicardi-Goutieres syndrome[provided by RefSeq,
            Jul 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314611.1, AF095844.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000649979.2/ ENSP00000497271.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1025
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..1025
                     /product="interferon-induced helicase C domain-containing
                     protein 1"
                     /EC_number="3.6.4.13"
                     /note="helicard; DEAD/H (Asp-Glu-Ala-Asp/His) box
                     polypeptide; helicase with 2 CARD domains; RNA
                     helicase-DEAD box protein 116; murabutide down-regulated
                     protein; melanoma differentiation-associated protein 5;
                     CADM-140 autoantigen; clinically amyopathic
                     dermatomyositis autoantigen 140 kDa; RIG-I-like receptor
                     2; melanoma differentiation-associated gene 5"
                     /calculated_mol_wt=116558
     Region          8..99
                     /region_name="CARD_MDA5_r1"
                     /note="Caspase activation and recruitment domain found in
                     MDA5, first repeat; cd08818"
                     /db_xref="CDD:260077"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23499489,
                     ECO:0000269|PubMed:33727702; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Region          111..201
                     /region_name="CARD_MDA5_r2"
                     /note="Caspase activation and recruitment domain found in
                     MDA5, second repeat; cd08819"
                     /db_xref="CDD:260078"
     Site            208..209
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            216..217
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            251..252
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Region          271..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5F7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5F7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5F7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Region          306..521
                     /region_name="DEXHc_RLR-2"
                     /note="DEXH-box helicase domain of RLR-2; cd18074"
                     /db_xref="CDD:350832"
     Site            order(307..309,312,330..337,376)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350832"
     Site            order(364..367,391..393,413,419,447,450..452)
                     /site_type="other"
                     /note="nucleic acid binding site [nucleotide binding]"
                     /db_xref="CDD:350832"
     Region          548..694
                     /region_name="MDA5_ID"
                     /note="Insert domain of MDA5; cd12090"
                     /db_xref="CDD:277189"
     Site            order(579..580,583,587)
                     /site_type="other"
                     /note="helicase domain interface [polypeptide binding]"
                     /db_xref="CDD:277189"
     Site            order(579..580,583,587)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:277189"
     Site            order(587,590..591,594..595,598)
                     /site_type="other"
                     /note="RD interface [polypeptide binding]"
                     /db_xref="CDD:277189"
     Region          640..662
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R5F7; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Region          695..834
                     /region_name="SF2_C_dicer"
                     /note="C-terminal helicase domain of the endoribonuclease
                     Dicer; cd18802"
                     /db_xref="CDD:350189"
     Site            order(726..728,791,810,812)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350189"
     Site            order(795,797,822,824)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350189"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RIOK3.
                     /evidence=ECO:0000269|PubMed:25865883; propagated from
                     UniProtKB/Swiss-Prot (Q9BYX4.3)"
     Region          900..1015
                     /region_name="MDA5_C"
                     /note="C-terminal domain of Melanoma
                     differentiation-associated protein 5, a cytoplasmic viral
                     RNA receptor; cd15807"
                     /db_xref="CDD:276945"
     Site            order(924..928,970,972..974,981,983,1001..1004)
                     /site_type="other"
                     /note="dsRNA binding site [nucleotide binding]"
                     /db_xref="CDD:276945"
     CDS             1..1025
                     /gene="IFIH1"
                     /gene_synonym="AGS7; Hlcd; IDDM19; IMD95; MDA-5; MDA5;
                     RLR-2; SGMRT1"
                     /coded_by="NM_022168.4:378..3455"
                     /db_xref="CCDS:CCDS2217.1"
                     /db_xref="GeneID:64135"
                     /db_xref="HGNC:HGNC:18873"
                     /db_xref="MIM:606951"
ORIGIN      
        1 msngystden fryliscfra rvkmyiqvep vldyltflpa evkeqiqrtv atsgnmqave
       61 lllstlekgv whlgwtrefv ealrrtgspl aarymnpelt dlpspsfena hdeylqllnl
      121 lqptlvdkll vrdvldkcme eelltiedrn riaaaenngn esgvrellkr ivqkenwfsa
      181 flnvlrqtgn nelvqeltgs dcsesnaeie nlsqvdgpqv eeqllsttvq pnlekevwgm
      241 ennssessfa dssvvsesdt slaegsvscl deslghnsnm gsdsgtmgsd sdeenvaara
      301 spepelqlrp yqmevaqpal egkniiiclp tgsgktrvav yiakdhldkk kkasepgkvi
      361 vlvnkvllve qlfrkefqpf lkkwyrvigl sgdtqlkisf pevvkscdii istaqilens
      421 llnlengeda gvqlsdfsli iidechhtnk eavynnimrh ylmqklknnr lkkenkpvip
      481 lpqilgltas pgvggatkqa kaeehilklc anldaftikt vkenldqlkn qiqepckkfa
      541 iadatredpf keklleimtr iqtycqmspm sdfgtqpyeq waiqmekkaa kegnrkervc
      601 aehlrkynea lqindtirmi daythletfy neekdkkfav ieddsdeggd deycdgdede
      661 ddlkkplkld etdrflmtlf fennkmlkrl aenpeyenek ltklrntime qytrteesar
      721 giiftktrqs ayalsqwite nekfaevgvk ahhligaghs sefkpmtqne qkeviskfrt
      781 gkinlliatt vaeegldike cniviryglv tneiamvqar graradesty vlvahsgsgv
      841 iehetvndfr ekmmykaihc vqnmkpeeya hkilelqmqs imekkmktkr niakhyknnp
      901 slitflcknc svlacsgedi hviekmhhvn mtpefkelyi vrenkalqkk cadyqingei
      961 ickcgqawgt mmvhkgldlp clkirnfvvv fknnstkkqy kkwvelpitf pnldyseccl
     1021 fsded
//
LOCUS       NP_001087240             649 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin reductase 1, cytoplasmic isoform 5 [Homo sapiens].
ACCESSION   NP_001087240
VERSION     NP_001087240.1
DBSOURCE    REFSEQ: accession NM_001093771.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 649)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 649)
  AUTHORS   Hsieh,M.S., Ling,H.H., Setiawan,S.A., Hardianti,M.S., Fong,I.H.,
            Yeh,C.T. and Chen,J.H.
  TITLE     Therapeutic targeting of thioredoxin reductase 1 causes ferroptosis
            while potentiating anti-PD-1 efficacy in head and neck cancer
  JOURNAL   Chem Biol Interact 395, 111004 (2024)
   PUBMED   38636790
  REMARK    GeneRIF: Therapeutic targeting of thioredoxin reductase 1 causes
            ferroptosis while potentiating anti-PD-1 efficacy in head and neck
            cancer.
REFERENCE   3  (residues 1 to 649)
  AUTHORS   Shen,X., Xia,Y., Lu,H., Zheng,P., Wang,J., Chen,Y., Xu,C., Qiu,C.,
            Zhang,Y., Xiao,Z., Zou,P., Cui,R. and Ni,D.
  TITLE     Synergistic targeting of TrxR1 and ATM/AKT pathway in human colon
            cancer cells
  JOURNAL   Biomed Pharmacother 174, 116507 (2024)
   PUBMED   38565059
  REMARK    GeneRIF: Synergistic targeting of TrxR1 and ATM/AKT pathway in
            human colon cancer cells.
REFERENCE   4  (residues 1 to 649)
  AUTHORS   Nalvarte,I., Damdimopoulos,A.E., Ruegg,J. and Spyrou,G.
  TITLE     The expression and activity of thioredoxin reductase 1 splice
            variants v1 and v2 regulate the expression of genes associated with
            differentiation and adhesion
  JOURNAL   Biosci Rep 35 (6), e00269 (2015)
   PUBMED   26464515
  REMARK    GeneRIF: TXNRD1_v1 and TXNRD1_v2 have distinct roles in
            differentiation, possibly by altering the expression of the genes
            associated with differentiation, and further emphasize the
            importance in distinguishing each unique action of different TrxR1
            splice forms
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 649)
  AUTHORS   Dammeyer,P., Damdimopoulos,A.E., Nordman,T., Jimenez,A.,
            Miranda-Vizuete,A. and Arner,E.S.
  TITLE     Induction of cell membrane protrusions by the N-terminal
            glutaredoxin domain of a rare splice variant of human thioredoxin
            reductase 1
  JOURNAL   J Biol Chem 283 (5), 2814-2821 (2008)
   PUBMED   18042542
  REMARK    GeneRIF: the Grx domain of TXNRD1_v3 localizes first in the
            emerging cell membrane protrusion and is then followed into the
            protrusions by actin and subsequently by tubulin
REFERENCE   6  (residues 1 to 649)
  AUTHORS   Gladyshev,V.N., Jeang,K.T. and Stadtman,T.C.
  TITLE     Selenocysteine, identified as the penultimate C-terminal residue in
            human T-cell thioredoxin reductase, corresponds to TGA in the human
            placental gene
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 6146-6151 (1996)
   PUBMED   8650234
REFERENCE   7  (residues 1 to 649)
  AUTHORS   Tamura,T. and Stadtman,T.C.
  TITLE     A new selenoprotein from human lung adenocarcinoma cells:
            purification, properties, and thioredoxin reductase activity
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1006-1011 (1996)
   PUBMED   8577704
REFERENCE   8  (residues 1 to 649)
  AUTHORS   Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-linked peroxidase from human red blood cell: evidence
            for the existence of thioredoxin and thioredoxin reductase in human
            red blood cell
  JOURNAL   Biochem Biophys Res Commun 217 (3), 900-907 (1995)
   PUBMED   8554614
REFERENCE   9  (residues 1 to 649)
  AUTHORS   Gasdaska,P.Y., Gasdaska,J.R., Cochran,S. and Powis,G.
  TITLE     Cloning and sequencing of a human thioredoxin reductase
  JOURNAL   FEBS Lett 373 (1), 5-9 (1995)
   PUBMED   7589432
REFERENCE   10 (residues 1 to 649)
  AUTHORS   Schallreuter,K.U., Grebe,T., Pittelkow,M.R. and Wood,J.M.
  TITLE     [3H]-13-cis-retinoic acid covalently binds to thioredoxin reductase
            in human keratinocytes
  JOURNAL   Skin Pharmacol 4 (1), 14-20 (1991)
   PUBMED   2064786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC418649.1, AY057105.1,
            AK226071.1, BC018122.1 and AI097548.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the pyridine
            nucleotide-disulfide oxidoreductase family, and is a member of the
            thioredoxin (Trx) system. Three thioredoxin reductase (TrxR)
            isozymes are found in mammals. TrxRs are selenocysteine-containing
            flavoenzymes, which reduce thioredoxins, as well as other
            substrates, and play a key role in redox homoeostasis. This gene
            encodes an ubiquitously expressed, cytosolic form of TrxR, which
            functions as a homodimer containing FAD, and selenocysteine (Sec)
            at the active site. Sec is encoded by UGA codon that normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, the Sec insertion sequence
            (SECIS) element, which is necessary for the recognition of UGA as a
            Sec codon rather than as a stop signal. Alternative splicing,
            primarily at the 5' end, results in transcript variants encoding
            same or different isoforms, including a glutaredoxin-containing
            isoform that is predominantly expressed in testis. [provided by
            RefSeq, May 2017].
            
            Transcript Variant: This variant (7, also known as beta 1)
            represents use of an alternate upstream promoter, and contains
            additional exons at the 5' end compared to variant 1. The encoded
            isoform (5, also known as TXNRD1_v3 or v3) has a longer and
            distinct N-terminus, resulting from translation initiation at an
            in-frame upstream start codon, compared to isoform 1. It is
            predominantly expressed in Leydig cells of testis, and contains an
            atypical N-terminal glutaredoxin domain, which induces actin and
            tubulin polymerization, leading to formation of cell membrane
            protrusions (PMID:18042542).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005669.1, SRR1803611.267438.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match              :: ENST00000525566.6/
                                               ENSP00000434516.1
            protein contains selenocysteine :: PMID: 7589432, 8650234
            RefSeq Select criteria          :: based on conservation, longest
                                               protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..649
                     /product="thioredoxin reductase 1, cytoplasmic isoform 5"
                     /EC_number="1.8.1.9"
                     /EC_number="1.11.1.2"
                     /note="KM-102-derived reductase-like factor; thioredoxin
                     reductase GRIM-12; thioredoxin reductase 1, cytoplasmic;
                     oxidoreductase; thioredoxin reductase TR1; gene associated
                     with retinoic and IFN-induced mortality 12 protein;
                     selenoprotein TXNRD1; gene associated with retinoic and
                     interferon-induced mortality 12 protein; testis tissue
                     sperm-binding protein Li 46a; peroxidase TXNRD1"
                     /calculated_mol_wt=70775
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16881.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q16881.3)"
     Region          68..148
                     /region_name="GRX_GRXh_1_2_like"
                     /note="Glutaredoxin (GRX) family, GRX human class 1 and 2
                     (h_1_2)-like subfamily; composed of proteins similar to
                     human GRXs, approximately 10 kDa in size, and proteins
                     containing a GRX or GRX-like domain. GRX is a glutathione
                     (GSH) dependent reductase; cd03419"
                     /db_xref="CDD:239511"
     Site            order(73,76,78,118..121,132..135)
                     /site_type="other"
                     /note="GSH binding site [chemical binding]"
                     /db_xref="CDD:239511"
     Site            order(76,79)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239511"
     Region          145..149
                     /region_name="Required for interaction with ESR1 and ESR2.
                     /evidence=ECO:0000269|PubMed:15199063"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16881.3)"
     Region          161..649
                     /region_name="TGR"
                     /note="thioredoxin and glutathione reductase
                     selenoprotein; TIGR01438"
                     /db_xref="CDD:273624"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q16881.3)"
     Site            648
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..649
                     /gene="TXNRD1"
                     /gene_synonym="GRIM-12; TR; TR1; TRXR1; TXNR; TXNR1"
                     /coded_by="NM_001093771.3:25..1974"
                     /note="UGA stop codon recoded as selenocysteine; isoform 5
                     is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS53820.1"
                     /db_xref="GeneID:7296"
                     /db_xref="HGNC:HGNC:12437"
                     /db_xref="MIM:601112"
ORIGIN      
        1 mgcaegkava aaaptelqtk gkngdgrrrs akdhhpgktl penpagftst atadsrallq
       61 ayidghsvvi fsrstctrct evkklfkslc vpyfvleldq tedgralegt lselaaetdl
      121 pvvfvkqrki gghgptlkay qegrlqkllk mngpedlpks ydydliiigg gsgglaaake
      181 aaqygkkvmv ldfvtptplg trwglggtcv nvgcipkklm hqaallgqal qdsrnygwkv
      241 eetvkhdwdr mieavqnhig slnwgyrval rekkvvyena ygqfigphri katnnkgkek
      301 iysaerflia tgerprylgi pgdkeyciss ddlfslpycp gktlvvgasy valecagfla
      361 gigldvtvmv rsillrgfdq dmankigehm eehgikfirq fvpikveqie agtpgrlrvv
      421 aqstnseeii egeyntvmla igrdactrki gletvgvkin ektgkipvtd eeqtnvpyiy
      481 aigdiledkv eltpvaiqag rllaqrlyag stvkcdyenv pttvftpley gacglseeka
      541 vekfgeenie vyhsyfwple wtipsrdnnk cyakiicntk dnervvgfhv lgpnagevtq
      601 gfaaalkcgl tkkqldstig ihpvcaevft tlsvtkrsga silqagcug
//
LOCUS       NP_001354577             739 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform s [Homo sapiens].
ACCESSION   NP_001354577
VERSION     NP_001354577.1
DBSOURCE    REFSEQ: accession NM_001367648.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 739)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 739)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 739)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 739)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 739)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 739)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 739)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 739)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 739)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 739)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.177571.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..739
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..739
                     /product="SUN domain-containing protein 1 isoform s"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=81701
     Region          12..245
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <319..>543
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          371..424
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(371,374..375,378,381..382,385..386,388..389,
                     392..393,395..396,399..400,402..403,406,409..410,413,
                     416..417,420..421,423..424)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          501..559
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          602..737
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..739
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367648.1:105..2324"
                     /note="isoform s is encoded by transcript variant 19"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld
      181 ahtaahsqsp rlpgragtlw hiwacagkaa sgvfwwlgig wyqfvtlisw lnvflltrcl
      241 rnickflvll iplflllagl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl
      301 kqplqgdsea fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag
      361 psasvrdavg qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa
      421 vgeqllptve hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq
      481 ggsleqllqr fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag
      541 asgiteaqar aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi
      601 plwyfsqspr vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni
      661 ssapkdfavy gleneyqeeg qllgqftydq dgeslqmfqa lkrpddtafq ivelrifsnw
      721 ghpeytclyr frvhgepvk
//
LOCUS       NP_001336250             349 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001336250 XP_016861581
VERSION     NP_001336250.1
DBSOURCE    REFSEQ: accession NM_001349321.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Li,F., Niu,M., Qin,K., Guo,R., Yi,Y., Xu,J., Li,L., Xie,S., Fu,M.,
            Wen,N., Liao,W. and Xiao,Z.J.
  TITLE     FBXL2 promotes E47 protein instability to inhibit breast cancer
            stemness and paclitaxel resistance
  JOURNAL   Oncogene 42 (5), 339-350 (2023)
   PUBMED   36460773
  REMARK    GeneRIF: FBXL2 promotes E47 protein instability to inhibit breast
            cancer stemness and paclitaxel resistance.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Niu,M., Xu,J., Liu,Y., Li,Y., He,T., Ding,L., He,Y., Yi,Y., Li,F.,
            Guo,R., Gao,Y., Li,R., Li,L., Fu,M., Hu,Q., Luo,Y., Zhang,C.,
            Qin,K., Yi,J., Yu,S., Yang,J., Chen,H., Wang,L., Li,Z., Dong,B.,
            Qi,S., Ouyang,L., Zhang,Y., Cao,Y. and Xiao,Z.J.
  TITLE     FBXL2 counteracts Grp94 to destabilize EGFR and inhibit EGFR-driven
            NSCLC growth
  JOURNAL   Nat Commun 12 (1), 5919 (2021)
   PUBMED   34635651
  REMARK    GeneRIF: FBXL2 counteracts Grp94 to destabilize EGFR and inhibit
            EGFR-driven NSCLC growth.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Wang,C., Gale,M. Jr., Keller,B.C., Huang,H., Brown,M.S.,
            Goldstein,J.L. and Ye,J.
  TITLE     Identification of FBL2 as a geranylgeranylated cellular protein
            required for hepatitis C virus RNA replication
  JOURNAL   Mol Cell 18 (4), 425-434 (2005)
   PUBMED   15893726
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Ilyin,G.P., Rialland,M., Glaise,D. and Guguen-Guillouzo,C.
  TITLE     Identification of a novel Skp2-like mammalian protein containing
            F-box and leucine-rich repeats
  JOURNAL   FEBS Lett 459 (1), 75-79 (1999)
   PUBMED   10508920
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC123900.2 and AC122176.2.
            
            On Mar 11, 2017 this sequence version replaced XP_016861581.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbls class and, in addition to an F-box, contains 12 tandem
            leucine-rich repeats. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (6), as well as variants 4 and 5,
            encodes isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.233063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..349
                     /product="F-box/LRR-repeat protein 2 isoform 4"
                     /note="F-box protein containing leucine-rich repeats;
                     F-box/LRR-repeat protein 2; F-box protein FBL2/FBL3"
                     /calculated_mol_wt=38765
     Region          27..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          53..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          63..293
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          79..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          157..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          183..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          209..259
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          269..288
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..349
                     /gene="FBXL2"
                     /gene_synonym="FBL2; FBL3"
                     /coded_by="NM_001349321.2:500..1549"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:25827"
                     /db_xref="HGNC:HGNC:13598"
                     /db_xref="MIM:605652"
ORIGIN      
        1 mdaqksltvr llffstcysl srfcsklkhl dltscvsitn sslkgisegc rnleylnlsw
       61 cdqitkdgie alvrgcrglk alllrgctql edealkhiqn ychelvslnl qscsritdeg
      121 vvqicrgchr lqalclsgcs nltdasltal glncprlqil eaarcshltd agftllarnc
      181 helekmdlee cilitdstli qlsihcpklq alvslsfsdi ihllkmkeps hhnkklfgfs
      241 fckslshcel itddgilhls nstcgherlr vleldnclli tdvalehlen crglerlely
      301 dcqqvtragi krmraqlphv kvhayfapvt pptavagsgq rlcrccvil
//
LOCUS       NP_001287815             144 aa            linear   PRI 20-NOV-2025
DEFINITION  rho-related GTP-binding protein RhoD isoform 2 [Homo sapiens].
ACCESSION   NP_001287815 XP_005274020
VERSION     NP_001287815.1
DBSOURCE    REFSEQ: accession NM_001300886.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Kazmi,N., Robinson,T., Zheng,J., Kar,S., Martin,R.M. and
            Ridley,A.J.
  TITLE     Rho GTPase gene expression and breast cancer risk: a Mendelian
            randomization analysis
  JOURNAL   Sci Rep 12 (1), 1463 (2022)
   PUBMED   35087170
  REMARK    GeneRIF: Rho GTPase gene expression and breast cancer risk: a
            Mendelian randomization analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 144)
  AUTHORS   King,V.L., Leclair,N.K., Coulter,A.M. and Campellone,K.G.
  TITLE     The actin nucleation factors JMY and WHAMM enable a rapid Arp2/3
            complex-mediated intrinsic pathway of apoptosis
  JOURNAL   PLoS Genet 17 (4), e1009512 (2021)
   PUBMED   33872315
  REMARK    GeneRIF: The actin nucleation factors JMY and WHAMM enable a rapid
            Arp2/3 complex-mediated intrinsic pathway of apoptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Blom,M., Reis,K. and Aspenstrom,P.
  TITLE     RhoD localization and function is dependent on its GTP/GDP-bound
            state and unique N-terminal motif
  JOURNAL   Eur J Cell Biol 97 (6), 393-401 (2018)
   PUBMED   29776664
  REMARK    GeneRIF: The GTPase deficient atypical Rho GTPases, which have a
            stalled GTPase activity, RhoD has an elevated intrinsic GDP/GTP
            exchange activity, rendering the protein constitutively active.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Zanata,S.M., Hovatta,I., Rohm,B. and Puschel,A.W.
  TITLE     Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor
            activity in Semaphorin 3A-induced cytoskeletal collapse
  JOURNAL   J Neurosci 22 (2), 471-477 (2002)
   PUBMED   11784792
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Murphy,C., Saffrich,R., Olivo-Marin,J.C., Giner,A., Ansorge,W.,
            Fotsis,T. and Zerial,M.
  TITLE     Dual function of rhoD in vesicular movement and cell motility
  JOURNAL   Eur J Cell Biol 80 (6), 391-398 (2001)
   PUBMED   11484930
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Ridley,A.J.
  TITLE     Rho proteins: linking signaling with membrane trafficking
  JOURNAL   Traffic 2 (5), 303-310 (2001)
   PUBMED   11350626
  REMARK    Review article
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Kim,H.S., Choi,J.Y., Jung,A.R., Jang,K.L., Lee,W.H., Choi,W.C.,
            Crow,T.J. and Hyun,B.H.
  TITLE     Assignment of the human RhoHP1 gene (ARHD) to chromosome 11q14.3 by
            radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 53 (2000)
   PUBMED   10894936
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Shimizu,F., Watanabe,T.K., Okuno,S., Omori,Y., Fujiwara,T.,
            Takahashi,E. and Nakamura,Y.
  TITLE     Isolation of a novel human cDNA (rhoHP1) homologous to rho genes
  JOURNAL   Biochim Biophys Acta 1351 (1-2), 13-16 (1997)
   PUBMED   9116026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM761353.1, CN305061.1 and
            CB853597.1.
            
            On Jul 16, 2014 this sequence version replaced XP_005274020.2.
            
            Summary: Ras homolog, or Rho, proteins interact with protein
            kinases and may serve as targets for activated GTPase. They play a
            critical role in muscle differentiation. The protein encoded by
            this gene binds GTP and is a member of the small GTPase
            superfamily. It is involved in endosome dynamics and reorganization
            of the actin cytoskeleton, and it may coordinate membrane transport
            with the function of the cytoskeleton. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment compared to variant 1. The resulting isoform (2) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN305061.1, DRR138506.1835.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..144
                     /product="rho-related GTP-binding protein RhoD isoform 2"
                     /note="ras homolog gene family, member A; Rho-related
                     protein HP1; Rho-related GTP-binding protein RhoD; ras
                     homolog D; ras homolog gene family, member D"
                     /calculated_mol_wt=15615
     Region          16..144
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Site            order(26..32,63..64,66,106..108)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206648"
     Site            63..66
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            106..108
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..144
                     /gene="RHOD"
                     /gene_synonym="ARHD; Rho; RHOHP1; RHOM"
                     /coded_by="NM_001300886.2:57..491"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73330.1"
                     /db_xref="GeneID:29984"
                     /db_xref="HGNC:HGNC:670"
                     /db_xref="MIM:605781"
ORIGIN      
        1 mtaaqaagee appgvrsvkv vlvgdggcgk tsllmvfadg afpewypevn hfckkvpiiv
       61 vgcktdlrkd kslvnklrrn glepvtyhrg qemarsvgav aylecsarlh dnvhavfqea
      121 aevalssrgr nfwrritqgf cvvt
//
LOCUS       NP_001008895             759 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-4A isoform 1 [Homo sapiens].
ACCESSION   NP_001008895
VERSION     NP_001008895.1
DBSOURCE    REFSEQ: accession NM_001008895.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Jia,Y., Huo,X., Wu,L., Zhang,H., Xu,W. and Leng,H.
  TITLE     circSNTB2 and CUL4A Induces Dysfunction of Nucleus Pulposus Cells
            by Competitively Binding miR-665
  JOURNAL   Biochem Genet 62 (2), 968-986 (2024)
   PUBMED   37507642
  REMARK    GeneRIF: circSNTB2 and CUL4A Induces Dysfunction of Nucleus
            Pulposus Cells by Competitively Binding miR-665.
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Tavlas,P., Nikou,S., Geramoutsou,C., Bosgana,P., Tsaniras,S.C.,
            Melachrinou,M., Maroulis,I. and Bravou,V.
  TITLE     CUL4A Ubiquitin Ligase Is an Independent Predictor of Overall
            Survival in Pancreatic Adenocarcinoma
  JOURNAL   Cancer Genomics Proteomics 21 (2), 166-177 (2024)
   PUBMED   38423594
  REMARK    GeneRIF: CUL4A Ubiquitin Ligase Is an Independent Predictor of
            Overall Survival in Pancreatic Adenocarcinoma.
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Hu,Y., Zhang,R., Lu,S., Zhang,W., Wang,D., Ge,Y., Jiang,F., Qin,X.
            and Liu,Y.
  TITLE     S100 Calcium Binding Protein A16 Promotes Cell Proliferation by
            triggering LATS1 ubiquitin degradation mediated by CUL4A ligase to
            inhibit Hippo pathway in Glioma development
  JOURNAL   Int J Biol Sci 19 (7), 2034-2052 (2023)
   PUBMED   37151881
  REMARK    GeneRIF: S100 Calcium Binding Protein A16 Promotes Cell
            Proliferation by triggering LATS1 ubiquitin degradation mediated by
            CUL4A ligase to inhibit Hippo pathway in Glioma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Ito,T., Ando,H., Suzuki,T., Ogura,T., Hotta,K., Imamura,Y.,
            Yamaguchi,Y. and Handa,H.
  TITLE     Identification of a primary target of thalidomide teratogenicity
  JOURNAL   Science 327 (5971), 1345-1350 (2010)
   PUBMED   20223979
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
  REMARK    GeneRIF: crystallographic analyses of the virally hijacked form of
            the human DDB1-CUL4A-ROC1 machinery
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Chen,L.C., Manjeshwar,S., Lu,Y., Moore,D., Ljung,B.M., Kuo,W.L.,
            Dairkee,S.H., Wernick,M., Collins,C. and Smith,H.S.
  TITLE     The human homologue for the Caenorhabditis elegans cul-4 gene is
            amplified and overexpressed in primary breast cancers
  JOURNAL   Cancer Res 58 (16), 3677-3683 (1998)
   PUBMED   9721878
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Osaka,F., Kawasaki,H., Aida,N., Saeki,M., Chiba,T., Kawashima,S.,
            Tanaka,K. and Kato,S.
  TITLE     A new NEDD8-ligating system for cullin-4A
  JOURNAL   Genes Dev 12 (15), 2263-2268 (1998)
   PUBMED   9694792
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455959.1, BC008308.1,
            AL136221.38 and BU631279.1.
            
            Summary: CUL4A is the ubiquitin ligase component of a multimeric
            complex involved in the degradation of DNA damage-response proteins
            (Liu et al., 2009 [PubMed 19481525]).[supplied by OMIM, Oct 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.25465.1,
                                           SRR1660807.245263.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375440.9/ ENSP00000364589.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..759
                     /product="cullin-4A isoform 1"
                     /note="CUL-4A"
                     /calculated_mol_wt=87550
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13619.3)"
     Region          63..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Region          688..753
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; smart00884"
                     /db_xref="CDD:214883"
     CDS             1..759
                     /gene="CUL4A"
                     /coded_by="NM_001008895.4:16..2295"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41908.1"
                     /db_xref="GeneID:8451"
                     /db_xref="HGNC:HGNC:2554"
                     /db_xref="MIM:603137"
ORIGIN      
        1 madeaprkgs fsalvgrtng ltkpaalaaa pakpggaggs kklviknfrd rprlpdnytq
       61 dtwrklheav ravqsstsir ynleelyqav enlcshkvsp mlykqlrqac edhvqaqilp
      121 fredsldsvl flkkintcwq dhcrqmimir siflfldrty vlqnstlpsi wdmglelfrt
      181 hiisdkmvqs ktidgillli erersgeavd rsllrsllgm lsdlqvykds felkfleetn
      241 clyaaegqrl mqerevpeyl nhvskrleee gdrvityldh stqkpliacv ekqllgehlt
      301 ailqkgldhl ldenrvpdla qmyqlfsrvr ggqqallqhw seyiktfgta ivinpekdkd
      361 mvqdlldfkd kvdhvievcf qknerfvnlm kesfetfink rpnkpaelia khvdsklrag
      421 nkeatdeele rtldkimilf rfihgkdvfe afykkdlakr llvgksasvd aeksmlsklk
      481 hecgaaftsk legmfkdmel skdimvhfkq hmqnqsdsgp idltvniltm gywptytpme
      541 vhltpemikl qevfkafylg khsgrklqwq ttlghavlka efkegkkefq vslfqtlvll
      601 mfnegdgfsf eeikmatgie dselrrtlqs lacgkarvli kspkgkeved gdkfifngef
      661 khklfrikin qiqmketvee qvsttervfq drqyqidaai vrimkmrktl ghnllvsely
      721 nqlkfpvkpg dlkkriesli drdymerdkd npnqyhyva
//
LOCUS       NP_001915                165 aa            linear   PRI 20-NOV-2025
DEFINITION  growth arrest and DNA damage-inducible protein GADD45 alpha isoform
            1 [Homo sapiens].
ACCESSION   NP_001915
VERSION     NP_001915.1
DBSOURCE    REFSEQ: accession NM_001924.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Zhou,L., Bai,G., Song,Y., Liu,X., Li,X., Deng,Y., Si,Y., Shi,Y. and
            Li,H.
  TITLE     AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes
  JOURNAL   Endocr Relat Cancer 31 (9), e230330 (2024)
   PUBMED   38904412
  REMARK    GeneRIF: AGEs induce MMP-9 promoter demethylation through the
            GADD45alpha-mediated BER pathway to promote breast cancer
            metastasis in patients with diabetes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Hassan,N., Yi,H., Malik,B., Gaspard-Boulinc,L., Samaraweera,S.E.,
            Casolari,D.A., Seneviratne,J., Balachandran,A., Chew,T., Duly,A.,
            Carter,D.R., Cheung,B.B., Norris,M., Haber,M., Kavallaris,M.,
            Marshall,G.M., Zhang,X.D., Liu,T., Wang,J., Liebermann,D.A.,
            D'Andrea,R.J. and Wang,J.Y.
  TITLE     Loss of the stress sensor GADD45A promotes stem cell activity and
            ferroptosis resistance in LGR4/HOXA9-dependent AML
  JOURNAL   Blood 144 (1), 84-98 (2024)
   PUBMED   38579286
  REMARK    GeneRIF: Loss of the stress sensor GADD45A promotes stem cell
            activity and ferroptosis resistance in LGR4/HOXA9-dependent AML.
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Yu,L.R., Han,X.Z., Tang,Y.Z., Liu,D., Luo,X.Q., Qiu,X.W., Feng,J.,
            Yuan,W.X. and Ding,J.Y.
  TITLE     Activation of the MEK/ERK Pathway Mediates the Inhibitory Effects
            of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A, HK2, and
            GADD45A
  JOURNAL   Front Biosci (Landmark Ed) 29 (4), 160 (2024)
   PUBMED   38682208
  REMARK    GeneRIF: Activation of the MEK/ERK Pathway Mediates the Inhibitory
            Effects of Silvestrol on Nasopharyngeal Carcinoma Cells via RAP1A,
            HK2, and GADD45A.
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Gebert,M., Bartoszewska,S., Opalinski,L., Collawn,J.F. and
            Bartoszewski,R.
  TITLE     IRE1-mediated degradation of pre-miR-301a promotes apoptosis
            through upregulation of GADD45A
  JOURNAL   Cell Commun Signal 21 (1), 322 (2023)
   PUBMED   37946177
  REMARK    GeneRIF: IRE1-mediated degradation of pre-miR-301a promotes
            apoptosis through upregulation of GADD45A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Chen,I.T., Smith,M.L., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Direct interaction of Gadd45 with PCNA and evidence for competitive
            interaction of Gadd45 and p21Waf1/Cip1 with PCNA
  JOURNAL   Oncogene 11 (10), 1931-1937 (1995)
   PUBMED   7478510
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Kearsey,J.M., Coates,P.J., Prescott,A.R., Warbrick,E. and Hall,P.A.
  TITLE     Gadd45 is a nuclear cell cycle regulated protein which interacts
            with p21Cip1
  JOURNAL   Oncogene 11 (9), 1675-1683 (1995)
   PUBMED   7478594
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Carrier,F., Smith,M.L., Bae,I., Kilpatrick,K.E., Lansing,T.J.,
            Chen,C.Y., Engelstein,M., Friend,S.H., Henner,W.D., Gilmer,T.M. et
            al.
  TITLE     Characterization of human Gadd45, a p53-regulated protein
  JOURNAL   J Biol Chem 269 (51), 32672-32677 (1994)
   PUBMED   7798274
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Smith,M.L., Chen,I.T., Zhan,Q., Bae,I., Chen,C.Y., Gilmer,T.M.,
            Kastan,M.B., O'Connor,P.M. and Fornace,A.J. Jr.
  TITLE     Interaction of the p53-regulated protein Gadd45 with proliferating
            cell nuclear antigen
  JOURNAL   Science 266 (5189), 1376-1380 (1994)
   PUBMED   7973727
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Papathanasiou,M.A., Kerr,N.C., Robbins,J.H., McBride,O.W., Alamo,I.
            Jr., Barrett,S.F., Hickson,I.D. and Fornace,A.J. Jr.
  TITLE     Induction by ionizing radiation of the gadd45 gene in cultured
            human cells: lack of mediation by protein kinase C
  JOURNAL   Mol Cell Biol 11 (2), 1009-1016 (1991)
   PUBMED   1990262
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314991.1 and M60974.1.
            
            Summary: This gene is a member of a group of genes whose transcript
            levels are increased following stressful growth arrest conditions
            and treatment with DNA-damaging agents. The protein encoded by this
            gene responds to environmental stresses by mediating activation of
            the p38/JNK pathway via MTK1/MEKK4 kinase. The DNA damage-induced
            transcription of this gene is mediated by both p53-dependent and
            -independent mechanisms. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene.[provided
            by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.705608.1,
                                           SRR1163658.469431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370986.9/ ENSP00000360025.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..165
                     /product="growth arrest and DNA damage-inducible protein
                     GADD45 alpha isoform 1"
                     /note="DNA damage-inducible transcript-1; growth arrest
                     and DNA damage-inducible protein GADD45 alpha; growth
                     arrest and DNA-damage-inducible 45 alpha; DDIT-1; DNA
                     damage-inducible transcript 1 protein"
                     /calculated_mol_wt=18205
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24522.1)"
     Region          21..123
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     pfam01248"
                     /db_xref="CDD:426153"
     CDS             1..165
                     /gene="GADD45A"
                     /gene_synonym="DDIT1; GADD45"
                     /coded_by="NM_001924.4:295..792"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS640.1"
                     /db_xref="GeneID:1647"
                     /db_xref="HGNC:HGNC:4095"
                     /db_xref="MIM:126335"
ORIGIN      
        1 mtleefsage qktermdkvg daleevlska lsqrtitvgv yeaakllnvd pdnvvlclla
       61 adedddrdva lqihftliqa fccendinil rvsnpgrlae lllletdagp aasegaeqpp
      121 dlhcvlvtnp hssqwkdpal sqlicfcres rymdqwvpvi nlper
//
LOCUS       NP_001339862             855 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 6 [Homo sapiens].
ACCESSION   NP_001339862 XP_006716506
VERSION     NP_001339862.1
DBSOURCE    REFSEQ: accession NM_001352933.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_006716506.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.100385.1,
                                           SRR1803617.171387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..855
                     /product="DNA repair-scaffolding protein isoform 6"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=93674
     Region          3..309
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          461..845
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..855
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352933.1:225..2792"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 maqsltaeek titekhlelc prpkqettts kstsgltdit wsssgsdlsd edktlsqlqr
       61 delqfidwei dsdraeasdc defeddegav eisdcascas nqsltsdekl selpkpssie
      121 ileyssdsek eddlenvlli dsesphkyhv qfasdarqim erlidprtks tetilhtpqk
      181 ptakfprtpe nsakkkllrg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt
      241 vkilelheec amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv
      301 rifppwqkli ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi
      361 kgltnnspei qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga
      421 gvrvvvqrvy slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar
      481 qlegkscslv gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa
      541 lcyiltahpn lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql
      601 kslllleqre iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl
      661 ffkdalrdqg rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq
      721 gtvvgvdest afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr
      781 srpqcrvkvk llqrsissll rfaagedgsy evksvlgkev gllncfvqsv tahptscigl
      841 eeiellsagg asaeh
//
LOCUS       NP_003889               1496 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptojanin-2 isoform 1 [Homo sapiens].
ACCESSION   NP_003889
VERSION     NP_003889.1
DBSOURCE    REFSEQ: accession NM_003898.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1496)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1496)
  AUTHORS   Hou,W., Li,G.S., Gao,L., Lu,H.P., Zhou,H.F., Kong,J.L., Chen,G.,
            Xia,S. and Wei,H.Y.
  TITLE     SYNJ2 is a novel and potential biomarker for the prediction and
            treatment of cancers: from lung squamous cell carcinoma to
            pan-cancer
  JOURNAL   BMC Med Genomics 15 (1), 114 (2022)
   PUBMED   35581615
  REMARK    GeneRIF: SYNJ2 is a novel and potential biomarker for the
            prediction and treatment of cancers: from lung squamous cell
            carcinoma to pan-cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1496)
  AUTHORS   Zhang,R., Mo,W.J., Huang,L.S., Chen,J.T., Wu,W.Z., He,W.Y. and
            Feng,Z.B.
  TITLE     Identifying the Prognostic Risk Factors of Synaptojanin 2 and Its
            Underlying Perturbations Pathways in Hepatocellular Carcinoma
  JOURNAL   Bioengineered 12 (1), 855-874 (2021)
   PUBMED   33641617
  REMARK    GeneRIF: Identifying the Prognostic Risk Factors of Synaptojanin 2
            and Its Underlying Perturbations Pathways in Hepatocellular
            Carcinoma.
REFERENCE   4  (residues 1 to 1496)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1496)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1496)
  AUTHORS   Spaenij-Dekking,E.H., Van Delft,J., Van Der Meijden,E.,
            Hiemstra,H.S., Falkenburg,J.H., Koning,F., Drijfhout,J.W. and
            Kluin-Nelemans,J.C.
  TITLE     Synaptojanin 2 is recognized by HLA class II-restricted hairy cell
            leukemia-specific T cells
  JOURNAL   Leukemia 17 (12), 2467-2473 (2003)
   PUBMED   14562116
  REMARK    GeneRIF: Since Syn 2 is a phosphatidylinositol 4,5-biphosphatase
            involved in cell growth and rearrangement of actin filaments, the
            increased Syn 2 expression may correlate with the hairy cell
            leukemia etiology or the characteristic morphologic alterations.
REFERENCE   7  (residues 1 to 1496)
  AUTHORS   Zhong,R. and Ye,Z.H.
  TITLE     The SAC domain-containing protein gene family in Arabidopsis
  JOURNAL   Plant Physiol 132 (2), 544-555 (2003)
   PUBMED   12805586
REFERENCE   8  (residues 1 to 1496)
  AUTHORS   Rusk,N., Le,P.U., Mariggio,S., Guay,G., Lurisci,C., Nabi,I.R.,
            Corda,D. and Symons,M.
  TITLE     Synaptojanin 2 functions at an early step of clathrin-mediated
            endocytosis
  JOURNAL   Curr Biol 13 (8), 659-663 (2003)
   PUBMED   12699622
  REMARK    Erratum:[Curr Biol. 2003 Sep 30;13(19):1746]
REFERENCE   9  (residues 1 to 1496)
  AUTHORS   Nemoto,Y., Wenk,M.R., Watanabe,M., Daniell,L., Murakami,T.,
            Ringstad,N., Yamada,H., Takei,K. and De Camilli,P.
  TITLE     Identification and characterization of a synaptojanin 2 splice
            isoform predominantly expressed in nerve terminals
  JOURNAL   J Biol Chem 276 (44), 41133-41142 (2001)
   PUBMED   11498538
REFERENCE   10 (residues 1 to 1496)
  AUTHORS   Malecz,N., McCabe,P.C., Spaargaren,C., Qiu,R., Chuang,Y. and
            Symons,M.
  TITLE     Synaptojanin 2, a novel Rac1 effector that regulates
            clathrin-mediated endocytosis
  JOURNAL   Curr Biol 10 (21), 1383-1386 (2000)
   PUBMED   11084340
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294480.1, AF318616.1,
            AL139330.17 and AF086449.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The gene is a member of the inositol-polyphosphate
            5-phosphatase family. The encoded protein interacts with the
            ras-related C3 botulinum toxin substrate 1, which causes
            translocation of the encoded protein to the plasma membrane where
            it inhibits clathrin-mediated endocytosis. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1). This variant (1) is
            also known as synaptojanin 2B or 2B2 (SJ2B2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF318616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355585.9/ ENSP00000347792.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..1496
                     /product="synaptojanin-2 isoform 1"
                     /EC_number="3.1.3.36"
                     /note="inositol phosphate 5'-phosphatase 2; synaptic
                     inositol 1,4,5-trisphosphate 5-phosphatase 2;
                     phosphoinositide 5-phosphatase; inositol
                     polyphosphate-5-phosphatase H"
                     /calculated_mol_wt=165408
     Region          13..485
                     /region_name="COG5329"
                     /note="Phosphoinositide polyphosphatase (Sac family)
                     [Signal transduction mechanisms]"
                     /db_xref="CDD:227637"
     Region          530..861
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Site            order(538,587,685,726,728,802,854..855)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197333"
     Site            order(587,854)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197333"
     Site            order(685,728,855)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197333"
     Region          872..1008
                     /region_name="DUF1866"
                     /note="Domain of unknown function (DUF1866); pfam08952"
                     /db_xref="CDD:286093"
     Region          1027..1073
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     Region          <1035..1407
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1085..1166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15056.3)"
     Region          1190..1405
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     Site            1191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15056.3)"
     Region          1427..1473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15056.3)"
     CDS             1..1496
                     /gene="SYNJ2"
                     /gene_synonym="INPP5H"
                     /coded_by="NM_003898.4:100..4590"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5254.1"
                     /db_xref="GeneID:8871"
                     /db_xref="HGNC:HGNC:11504"
                     /db_xref="MIM:609410"
ORIGIN      
        1 malskglrll grlgaegdcs vlleargrdd cllfeagtva tlapeekevi kgqygkltda
       61 ygclgelrlk sggtslsflv lvtgctsvgr ipdaeiykit atdfyplqee akeeerlial
      121 kkilssgvfy fswpndgsrf dltvrtqkqg ddssewgnsf fwnqllhvpl rqhqvsccdw
      181 llkiicgvvt irtvyashkq akaclvsrvs certgtrfht rgvnddghvs nfveteqmiy
      241 mddgvssfvq irgsvplfwe qpglqvgshh lrlhrglean apafdrhmvl lkeqygqqvv
      301 vnllgsrgge evlnrafkkl lwaschagdt pminfdfhqf akggklekle tllrpqlklh
      361 wedfdvftkg envsprfqkg tlrmncldcl drtntvqsfi alevlhlqlk tlglsskpiv
      421 drfvesfkam wslnghslsk vftgsraleg kakvgklkdg arsmsrtiqs nffdgvkqea
      481 iklllvgdvy geevadkggm lldstallvt prilkamter qseftnfkri riamgtwnvn
      541 ggkqfrsnvl rtaeltdwll dspqlsgatd sqddsspadi favgfeemve lsagnivnas
      601 ttnkkmwgeq lqkaisrshr yilltsaqlv gvclyifvrp yhvpfirdva idtvktgmgg
      661 kagnkgavgi rfqfhstsfc ficshltagq sqvkernedy keitqklcfp mgrnvfshdy
      721 vfwcgdfnyr idltyeevfy fvkrqdwkkl lefdqlqlqk ssgkifkdfh egainfgpty
      781 kydvgsaayd tsdkcrtpaw tdrvlwwrkk hpfdktagel nlldsdldvd tkvrhtwspg
      841 alqyygrael qasdhrpvla ivevevqevd vgarervfqe vssfqgplda tvvvnlqspt
      901 leeknefped lrtelmqtlg sygtivlvri nqgqmlvtfa dshsalsvld vdgmkvkgra
      961 vkirpktkdw lkglreeiir krdsmapvsp tansclleen fdftsldyes egdiledded
     1021 ylvdefnqpg vsdselggdd lsdvpgptal appskspalt kkkqhptykd dadlvelkre
     1081 leavgefrhr spsrslsvpn rprppqppqr pppptglmvk ksasdasiss gthgqysilq
     1141 tarllpgapq qppkartgis kpynvkqikt tnaqeaeaai rclleargga seealsavap
     1201 rdleassepe ptpgaakpet pqappllprr ppprvpaikk ptlrrtgkpl speeqfeqqt
     1261 vhftigppet sveappvvta prvppvpkpr tfqpgkaaer pshrkpasde appgagasvp
     1321 ppleapplvp kvpprrkksa paafhlqvlq snsqllqglt ynssdspsgh ppaagtvfpq
     1381 gdflstssat spdsdgtkam kpeaapllgd yqdpfwnllh hpkllnntwl skssdpldsg
     1441 trspkrdpid pvsagasaak aelppdhehk tlghwvtisd qekrtalqvf dplakt
//
LOCUS       NP_075069                458 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 135 isoform 1 [Homo sapiens].
ACCESSION   NP_075069
VERSION     NP_075069.3
DBSOURCE    REFSEQ: accession NM_022918.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Hu,D., Tan,M., Lu,D., Kleiboeker,B., Liu,X., Park,H., Kravitz,A.V.,
            Shoghi,K.I., Tseng,Y.H., Razani,B., Ikeda,A. and Lodhi,I.J.
  TITLE     TMEM135 links peroxisomes to the regulation of brown fat
            mitochondrial fission and energy homeostasis
  JOURNAL   Nat Commun 14 (1), 6099 (2023)
   PUBMED   37773161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Wang,R., Zhang,M., Hu,Y., He,J., Lin,Q. and Peng,N.
  TITLE     MiR-100-5p inhibits osteogenic differentiation of human bone
            mesenchymal stromal cells by targeting TMEM135
  JOURNAL   Hum Cell 35 (6), 1671-1683 (2022)
   PUBMED   35947339
  REMARK    GeneRIF: MiR-100-5p inhibits osteogenic differentiation of human
            bone mesenchymal stromal cells by targeting TMEM135.
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Maharjan,Y., Lee,J.N., Kwak,S.A., Dutta,R.K., Park,C., Choe,S.K.
            and Park,R.
  TITLE     TMEM135 regulates primary ciliogenesis through modulation of
            intracellular cholesterol distribution
  JOURNAL   EMBO Rep 21 (5), e48901 (2020)
   PUBMED   32157776
  REMARK    GeneRIF: TMEM135 regulates primary ciliogenesis through modulation
            of intracellular cholesterol distribution.
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Zarsky,V. and Dolezal,P.
  TITLE     Evolution of the Tim17 protein family
  JOURNAL   Biol Direct 11 (1), 54 (2016)
   PUBMED   27760563
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Moayyeri,A., Hsu,Y.H., Karasik,D., Estrada,K., Xiao,S.M.,
            Nielson,C., Srikanth,P., Giroux,S., Wilson,S.G., Zheng,H.F.,
            Smith,A.V., Pye,S.R., Leo,P.J., Teumer,A., Hwang,J.Y., Ohlsson,C.,
            McGuigan,F., Minster,R.L., Hayward,C., Olmos,J.M.,
            Lyytikainen,L.P., Lewis,J.R., Swart,K.M., Masi,L., Oldmeadow,C.,
            Holliday,E.G., Cheng,S., van Schoor,N.M., Harvey,N.C., Kruk,M., del
            Greco,M. F, Igl,W., Trummer,O., Grigoriou,E., Luben,R., Liu,C.T.,
            Zhou,Y., Oei,L., Medina-Gomez,C., Zmuda,J., Tranah,G., Brown,S.J.,
            Williams,F.M., Soranzo,N., Jakobsdottir,J., Siggeirsdottir,K.,
            Holliday,K.L., Hannemann,A., Go,M.J., Garcia,M., Polasek,O.,
            Laaksonen,M., Zhu,K., Enneman,A.W., McEvoy,M., Peel,R., Sham,P.C.,
            Jaworski,M., Johansson,A., Hicks,A.A., Pludowski,P., Scott,R.,
            Dhonukshe-Rutten,R.A., van der Velde,N., Kahonen,M., Viikari,J.S.,
            Sievanen,H., Raitakari,O.T., Gonzalez-Macias,J., Hernandez,J.L.,
            Mellstrom,D., Ljunggren,O., Cho,Y.S., Volker,U., Nauck,M.,
            Homuth,G., Volzke,H., Haring,R., Brown,M.A., McCloskey,E.,
            Nicholson,G.C., Eastell,R., Eisman,J.A., Jones,G., Reid,I.R.,
            Dennison,E.M., Wark,J., Boonen,S., Vanderschueren,D., Wu,F.C.,
            Aspelund,T., Richards,J.B., Bauer,D., Hofman,A., Khaw,K.T.,
            Dedoussis,G., Obermayer-Pietsch,B., Gyllensten,U.,
            Pramstaller,P.P., Lorenc,R.S., Cooper,C., Kung,A.W., Lips,P.,
            Alen,M., Attia,J., Brandi,M.L., de Groot,L.C., Lehtimaki,T.,
            Riancho,J.A., Campbell,H., Liu,Y., Harris,T.B., Akesson,K.,
            Karlsson,M., Lee,J.Y., Wallaschofski,H., Duncan,E.L., O'Neill,T.W.,
            Gudnason,V., Spector,T.D., Rousseau,F., Orwoll,E., Cummings,S.R.,
            Wareham,N.J., Rivadeneira,F., Uitterlinden,A.G., Prince,R.L.,
            Kiel,D.P., Reeve,J. and Kaptoge,S.K.
  TITLE     Genetic determinants of heel bone properties: genome-wide
            association meta-analysis and replication in the GEFOS/GENOMOS
            consortium
  JOURNAL   Hum Mol Genet 23 (11), 3054-3068 (2014)
   PUBMED   24430505
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Exil,V.J., Silva Avila,D., Benedetto,A., Exil,E.A., Adams,M.R.,
            Au,C. and Aschner,M.
  TITLE     Stressed-induced TMEM135 protein is part of a conserved genetic
            network involved in fat storage and longevity regulation in
            Caenorhabditis elegans
  JOURNAL   PLoS One 5 (12), e14228 (2010)
   PUBMED   21151927
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Schrader,M. and Fahimi,H.D.
  TITLE     The peroxisome: still a mysterious organelle
  JOURNAL   Histochem Cell Biol 129 (4), 421-440 (2008)
   PUBMED   18274771
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Pei,L.
  TITLE     Pituitary tumor-transforming gene protein associates with ribosomal
            protein S10 and a novel human homologue of DnaJ in testicular cells
  JOURNAL   J Biol Chem 274 (5), 3151-3158 (1999)
   PUBMED   9915854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX648678.1, BC051462.1, AP000811.4 and DB325683.1.
            
            On Dec 15, 2009 this sequence version replaced NP_075069.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.60778.1,
                                           SRR1803611.269848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305494.6/ ENSP00000306344.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..458
                     /product="transmembrane protein 135 isoform 1"
                     /note="peroxisomal membrane protein 52; peroxisomal
                     protein 52"
                     /calculated_mol_wt=52160
     Region          9..142
                     /region_name="TMEM135_C_rich"
                     /note="N-terminal cysteine-rich region of Transmembrane
                     protein 135; pfam15982"
                     /db_xref="CDD:374269"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     Region          <299..351
                     /region_name="Tim17"
                     /note="Tim17/Tim22/Tim23/Pmp24 family; pfam02466"
                     /db_xref="CDD:460567"
     Site            331..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     Site            380..400
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UB9.2)"
     CDS             1..458
                     /gene="TMEM135"
                     /gene_synonym="PMP52"
                     /coded_by="NM_022918.4:113..1489"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8280.1"
                     /db_xref="GeneID:65084"
                     /db_xref="HGNC:HGNC:26167"
                     /db_xref="MIM:616360"
ORIGIN      
        1 maalsksiph ncyeightwh pscrvsflqi tggaleeslk iyaplyliaa ilrkrkldyy
       61 lhkllpeilq sasfltanga lymaffcilr kilgkfyswt pgfgaalpas yvailierks
      121 rrglltiyma nlatetlfrm gvargtittl rngevllfci taamymfffr ckdglkgftf
      181 salrfivgke eipthsfspe aayakveqkr eqheekpgrm nmiglvrkfv dsickhgprh
      241 rcckhyednc isycikgfir mfsvgyliqc clripsafrh lftqpsrlls lfynkenfql
      301 gaflgsfvsi ykgtscflrw irnlddelha iiagflagis mmfyksttis mylasklvet
      361 myfkgieagk vpyfphadti iysistaicf qaavmevqtl rpsywkfllr ltkgkfavmn
      421 rkvldvfgtg askhfqdfip rldpryttvt pelptefs
//
LOCUS       NP_000014                387 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-sarcoglycan isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000014
VERSION     NP_000014.1
DBSOURCE    REFSEQ: accession NM_000023.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Faheem,A., Masud,R., Nasir,R., Awan,Z.K., Nasir,H.A., Khan,Z.K.,
            Fayyaz,H. and Raza,S.I.
  TITLE     Exome sequencing revealed variants in SGCA and SIL1 genes
            underlying limb girdle muscular dystrophy and Marinesco-Sjogren
            syndrome patients
  JOURNAL   Mol Biol Rep 51 (1), 853 (2024)
   PUBMED   39060875
  REMARK    GeneRIF: Exome sequencing revealed variants in SGCA and SIL1 genes
            underlying limb girdle muscular dystrophy and Marinesco-Sjogren
            syndrome patients.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Escobar,H., Krause,A., Keiper,S., Kieshauer,J., Muthel,S., de
            Paredes,M.G., Metzler,E., Kuhn,R., Heyd,F. and Spuler,S.
  TITLE     Base editing repairs an SGCA mutation in human primary muscle stem
            cells
  JOURNAL   JCI Insight 6 (10), 145994 (2021)
   PUBMED   33848270
  REMARK    GeneRIF: Base editing repairs an SGCA mutation in human primary
            muscle stem cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 387)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Kawai,H., Akaike,M., Endo,T., Adachi,K., Inui,T., Mitsui,T.,
            Kashiwagi,S., Fujiwara,T., Okuno,S., Shin,S. et al.
  TITLE     Adhalin gene mutations in patients with autosomal recessive
            childhood onset muscular dystrophy with adhalin deficiency
  JOURNAL   J Clin Invest 96 (3), 1202-1207 (1995)
   PUBMED   7657792
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Piccolo,F., Roberds,S.L., Jeanpierre,M., Leturcq,F., Azibi,K.,
            Beldjord,C., Carrie,A., Recan,D., Chaouch,M., Reghis,A. et al.
  TITLE     Primary adhalinopathy: a common cause of autosomal recessive
            muscular dystrophy of variable severity
  JOURNAL   Nat Genet 10 (2), 243-245 (1995)
   PUBMED   7663524
  REMARK    Erratum:[Nat Genet 1995 Sep 11(1):104]
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Yang,B., Jung,D., Motto,D., Meyer,J., Koretzky,G. and Campbell,K.P.
  TITLE     SH3 domain-mediated interaction of dystroglycan and Grb2
  JOURNAL   J Biol Chem 270 (20), 11711-11714 (1995)
   PUBMED   7744812
REFERENCE   8  (residues 1 to 387)
  AUTHORS   McNally,E.M., Yoshida,M., Mizuno,Y., Ozawa,E. and Kunkel,L.M.
  TITLE     Human adhalin is alternatively spliced and the gene is located on
            chromosome 17q21
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9690-9694 (1994)
   PUBMED   7937874
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Roberds,S.L., Leturcq,F., Allamand,V., Piccolo,F., Jeanpierre,M.,
            Anderson,R.D., Lim,L.E., Lee,J.C., Tome,F.M., Romero,N.B. et al.
  TITLE     Missense mutations in the adhalin gene linked to autosomal
            recessive muscular dystrophy
  JOURNAL   Cell 78 (4), 625-633 (1994)
   PUBMED   8069911
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015909.14.
            
            Summary: This gene encodes a component of the
            dystrophin-glycoprotein complex (DGC), which is critical to the
            stability of muscle fiber membranes and to the linking of the actin
            cytoskeleton to the extracellular matrix. Its expression is thought
            to be restricted to striated muscle. Mutations in this gene result
            in type 2D autosomal recessive limb-girdle muscular dystrophy.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.985073.1, L34355.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262018.8/ ENSP00000262018.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..387
                     /product="alpha-sarcoglycan isoform 1 precursor"
                     /note="alpha-sarcoglycan; 50kD DAG; alpha-SG;
                     dystroglycan-2; 50 kDa dystrophin-associated glycoprotein;
                     sarcoglycan, alpha (50kDa dystrophin-associated
                     glycoprotein); limb girdle muscular dystrophy 2D"
                     /calculated_mol_wt=40432
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2461
     Region          21..347
                     /region_name="Sarcoglycan_2"
                     /note="Sarcoglycan alpha/epsilon; pfam05510"
                     /db_xref="CDD:461668"
     mat_peptide     24..387
                     /product="Alpha-sarcoglycan. /id=PRO_0000031673"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16586.1)"
                     /calculated_mol_wt=40432
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16586.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P82350; propagated from
                     UniProtKB/Swiss-Prot (Q16586.1)"
     CDS             1..387
                     /gene="SGCA"
                     /gene_synonym="50DAG; adhalin; ADL; DAG2; DMDA2; LGMD2D;
                     LGMDR3; SCARMD1"
                     /coded_by="NM_000023.4:37..1200"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32679.1"
                     /db_xref="GeneID:6442"
                     /db_xref="HGNC:HGNC:10805"
                     /db_xref="MIM:600119"
ORIGIN      
        1 maetlfwtpl lvvllaglgd teaqqttlhp lvgrvfvhtl dhetflslpe hvavppavhi
       61 tyhahlqghp dlprwlrytq rsphhpgfly gsatpedrgl qvievtaynr dsfdttrqrl
      121 vleigdpegp llpyqaeflv rshdaeevlp stpasrflsa lgglwepgel qllnvtsald
      181 rggrvplpie grkegvyikv gsaspfstcl kmvaspdsha rcaqgqppll scydtlaphf
      241 rvdwcnvtlv dksvpepade vptpgdgile hdpffcppte apdrdflvda lvtllvpllv
      301 allltlllay vmccrregrl krdlatsdiq mvhhctihgn teelrqmaas revprplstl
      361 pmfnvhtger lpprvdsaqv plildqh
//
LOCUS       NP_001191196             484 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-4 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001191196
VERSION     NP_001191196.1
DBSOURCE    REFSEQ: accession NM_001204267.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Sajan,S.A., Gradisch,R., Vogel,F.D., Coffey,A.J., Salyakina,D.,
            Soler,D., Jayakar,P., Jayakar,A., Bianconi,S.E., Cooper,A.H.,
            Liu,S., William,N., Benkel-Herrenbruck,I., Maiwald,R., Heller,C.,
            Biskup,S., Leiz,S., Westphal,D.S., Wagner,M., Clarke,A.,
            Stockner,T., Ernst,M., Kesari,A. and Krenn,M.
  TITLE     De novo variants in GABRA4 are associated with a neurological
            phenotype including developmental delay, behavioral abnormalities
            and epilepsy
  JOURNAL   Eur J Hum Genet 32 (8), 912-919 (2024)
   PUBMED   38565639
  REMARK    GeneRIF: De novo variants in GABRA4 are associated with a
            neurological phenotype including developmental delay, behavioral
            abnormalities and epilepsy.
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Sente,A., Desai,R., Naydenova,K., Malinauskas,T., Jounaidi,Y.,
            Miehling,J., Zhou,X., Masiulis,S., Hardwick,S.W., Chirgadze,D.Y.,
            Miller,K.W. and Aricescu,A.R.
  TITLE     Differential assembly diversifies GABAA receptor structures and
            signalling
  JOURNAL   Nature 604 (7904), 190-194 (2022)
   PUBMED   35355020
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Vogel,F.D., Krenn,M., Westphal,D.S., Graf,E., Wagner,M., Leiz,S.,
            Koniuszewski,F., Auge-Stock,M., Kramer,G., Scholze,P. and Ernst,M.
  TITLE     A de novo missense variant in GABRA4 alters receptor function in an
            epileptic and neurodevelopmental phenotype
  JOURNAL   Epilepsia 63 (4), e35-e41 (2022)
   PUBMED   35152403
  REMARK    GeneRIF: A de novo missense variant in GABRA4 alters receptor
            function in an epileptic and neurodevelopmental phenotype.
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Han,W., Shepard,R.D. and Lu,W.
  TITLE     Regulation of GABAARs by Transmembrane Accessory Proteins
  JOURNAL   Trends Neurosci 44 (2), 152-165 (2021)
   PUBMED   33234346
  REMARK    Review article
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Riley,J.D., Delahunty,C., Alsadah,A., Mazzola,S. and Astbury,C.
  TITLE     Further evidence of GABRA4 and TOP3B as autism susceptibility genes
  JOURNAL   Eur J Med Genet 63 (5), 103876 (2020)
   PUBMED   32028044
  REMARK    GeneRIF: Further evidence of GABRA4 and TOP3B as autism
            susceptibility genes.
REFERENCE   6  (residues 1 to 484)
  AUTHORS   Whiting,P.J., Bonnert,T.P., McKernan,R.M., Farrar,S., Le
            Bourdelles,B., Heavens,R.P., Smith,D.W., Hewson,L., Rigby,M.R.,
            Sirinathsinghji,D.J., Thompson,S.A. and Wafford,K.A.
  TITLE     Molecular and functional diversity of the expanding GABA-A receptor
            gene family
  JOURNAL   Ann N Y Acad Sci 868, 645-653 (1999)
   PUBMED   10414349
  REMARK    Review article
REFERENCE   7  (residues 1 to 484)
  AUTHORS   Ebert,V., Scholze,P. and Sieghart,W.
  TITLE     Extensive heterogeneity of recombinant gamma-aminobutyric acidA
            receptors expressed in alpha 4 beta 3 gamma 2-transfected human
            embryonic kidney 293 cells
  JOURNAL   Neuropharmacology 35 (9-10), 1323-1330 (1996)
   PUBMED   9014148
REFERENCE   8  (residues 1 to 484)
  AUTHORS   Yang,W., Drewe,J.A. and Lan,N.C.
  TITLE     Cloning and characterization of the human GABAA receptor alpha 4
            subunit: identification of a unique diazepam-insensitive binding
            site
  JOURNAL   Eur J Pharmacol 291 (3), 319-325 (1995)
   PUBMED   8719416
REFERENCE   9  (residues 1 to 484)
  AUTHORS   McLean,P.J., Farb,D.H. and Russek,S.J.
  TITLE     Mapping of the alpha 4 subunit gene (GABRA4) to human chromosome 4
            defines an alpha 2-alpha 4-beta 1-gamma 1 gene cluster: further
            evidence that modern GABAA receptor gene clusters are derived from
            an ancestral cluster
  JOURNAL   Genomics 26 (3), 580-586 (1995)
   PUBMED   7607683
REFERENCE   10 (residues 1 to 484)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107383.3, CD013892.1,
            BC035055.1 and BC037926.2.
            
            Summary: Gamma-aminobutyric acid (GABA) is the major inhibitory
            neurotransmitter in the mammalian brain where it acts at GABA-A
            receptors, which are ligand-gated chloride channels. Chloride
            conductance of these channels can be modulated by agents such as
            benzodiazepines that bind to the GABA-A receptor. At least 16
            distinct subunits of GABA-A receptors have been identified. This
            gene encodes subunit alpha-4, which is involved in the etiology of
            autism and eventually increases autism risk through interaction
            with another subunit, gamma-aminobutyric acid receptor beta-1
            (GABRB1). Alternatively spliced transcript variants encoding
            different isoforms have been found in this gene.[provided by
            RefSeq, Feb 2011].
            
            Transcript Variant: This variant (3) lacks a segment in the first
            splice junction, resulting in an upstream AUG start codon, and
            lacks an in-frame exon in the middle region, as compared to variant
            1. The resulting isoform (3) has a shorter and different N-terminus
            and lacks an internal segment, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD013892.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..484
                     /product="gamma-aminobutyric acid receptor subunit alpha-4
                     isoform 3"
                     /note="gamma-aminobutyric acid receptor subunit alpha-4;
                     GABA(A) receptor, alpha 4; gamma-aminobutyric acid A
                     receptor alpha 4; gamma-aminobutyric acid (GABA) A
                     receptor, alpha 4; gamma-aminobutyric acid type A receptor
                     alpha4 subunit; GABAAR subunit alpha-4"
                     /calculated_mol_wt=53755
     Region          5..471
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          38..229
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(63,65,71..72,79,97,99,111..112,114,116..117,
                     130..132,134,144,146,148,152,174)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349838"
     CDS             1..484
                     /gene="GABRA4"
                     /coded_by="NM_001204267.2:147..1601"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2557"
                     /db_xref="HGNC:HGNC:4078"
                     /db_xref="MIM:137141"
ORIGIN      
        1 mlqrwflprs lnespgqnqk eeklctenft rildslldgy dnrlrpgfgg pvtevktdiy
       61 vtsfgpvsdv emeytmdvff rqtwidkrlk ydgpieilrl nnmmvtkvwt pdtffrngkk
      121 svshnmtapn klfrimrngt ilytmrltis aecpmrlvdf pmdghacplk fgsyaypkse
      181 miytwtkgpe ksvevpkess slvqydligq tvssetiksi tgittvltmt tlsisarhsl
      241 pkvsyatamd wfiavcfafv fsaliefaav nyftniqmek akrktskppq evpaapvqre
      301 khpeaplqnt nanlnmrkrt nalvhsesdv gnrtevgnhs sksstvvqes skgtprsyla
      361 sspnpfsran aaetisaara lpsasptsir tgymprkasv gsastrhvfg srlqrikttv
      421 ntigatgkls atpppsappp sgsgtskidk yarilfpvtf gafnmvywvv ylskdtmeks
      481 eslm
//
LOCUS       NP_001185732             515 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4 gamma 3 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001185732
VERSION     NP_001185732.1
DBSOURCE    REFSEQ: accession NM_001198803.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Waskiewicz,A.J., Johnson,J.C., Penn,B., Mahalingam,M., Kimball,S.R.
            and Cooper,J.A.
  TITLE     Phosphorylation of the cap-binding protein eukaryotic translation
            initiation factor 4E by protein kinase Mnk1 in vivo
  JOURNAL   Mol Cell Biol 19 (3), 1871-1880 (1999)
   PUBMED   10022874
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Pyronnet,S., Imataka,H., Gingras,A.C., Fukunaga,R., Hunter,T. and
            Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) recruits
            mnk1 to phosphorylate eIF4E
  JOURNAL   EMBO J 18 (1), 270-279 (1999)
   PUBMED   9878069
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Gingras,A.C., Raught,B. and Sonenberg,N.
  TITLE     eIF4 initiation factors: effectors of mRNA recruitment to ribosomes
            and regulators of translation
  JOURNAL   Annu Rev Biochem 68, 913-963 (1999)
   PUBMED   10872469
  REMARK    Review article
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Imataka,H., Gradi,A. and Sonenberg,N.
  TITLE     A newly identified N-terminal amino acid sequence of human eIF4G
            binds poly(A)-binding protein and functions in poly(A)-dependent
            translation
  JOURNAL   EMBO J 17 (24), 7480-7489 (1998)
   PUBMED   9857202
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Gradi,A., Imataka,H., Svitkin,Y.V., Rom,E., Raught,B., Morino,S.
            and Sonenberg,N.
  TITLE     A novel functional human eukaryotic translation initiation factor
            4G
  JOURNAL   Mol Cell Biol 18 (1), 334-342 (1998)
   PUBMED   9418880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC030578.1, AL627311.16 and
            AL358392.19.
            
            Summary: The protein encoded by this gene is thought to be part of
            the eIF4F protein complex, which is involved in mRNA cap
            recognition and transport of mRNAs to the ribosome. Interestingly,
            a microRNA (miR-520c-3p) has been found that negatively regulates
            synthesis of the encoded protein, and this leads to a global
            decrease in protein translation and cell proliferation. Therefore,
            this protein is a key component of the anti-tumor activity of
            miR-520c-3p. [provided by RefSeq, May 2016].
            
            Transcript Variant: This variant (4) has an alternate 5' UTR and an
            additional in-frame exon in the 5' coding region, and lacks
            multiple 3' exons but has an alternate 3' exon, as compared to
            variant 1. The resulting isoform (4) has an extra internal segment
            and a distinct and much shorter C-terminus, as compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030578.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..515
                     /product="eukaryotic translation initiation factor 4 gamma
                     3 isoform 4"
                     /note="eIF-4-gamma 3; eIF-4-gamma II"
                     /calculated_mol_wt=55096
     Region          <1..>88
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     CDS             1..515
                     /gene="EIF4G3"
                     /gene_synonym="eIF-4G 3; eIF4G 3; eIF4GII"
                     /coded_by="NM_001198803.2:412..1959"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS59192.1"
                     /db_xref="GeneID:8672"
                     /db_xref="HGNC:HGNC:3298"
                     /db_xref="MIM:603929"
ORIGIN      
        1 mnsqpqtrsp faagprpphh qffqrpqiqp pratipnssp sirpgaqtpt avyqanqhim
       61 mvnhlpmpyp vpqgpqycip qyrhsgppyv gppqqypvqp pgpgpfypgp gpgdfpnayg
      121 tpfypsqpvy qsapiivptq qqpppakrek ktirirdpnq ggkditeeim sgggsrnptp
      181 pigrptstpt ppqqlpsqvp ehspvvygtv esahlaastp vtaasdqkqe ekpkpdpvlk
      241 spspvlrlvl sgekkeqegq tsettaivsi aelplppspt tvssvarsti aaptssalss
      301 qpifttaidd rcelsspred tipipsltsc tetsdplptn endddickkp csvapndipl
      361 vsstnlinei ngvseklsat esiveivkqe vlpltlelei lenppeemkl ecipapitps
      421 tvpsfpptpp tppaspphtp vivpaaattv sspsaaitvq rvleedesir tclsedakei
      481 qnkieveadg qteeildsqn lnsrrspvpe tsnec
//
LOCUS       NP_060552               1133 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060552
VERSION     NP_060552.4
DBSOURCE    REFSEQ: accession NM_018082.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1133)
  AUTHORS   Geroldi,A., Tozza,S., Fiorillo,C., Nolano,M., Fossa,P., Vitale,F.,
            Domi,R., Gaudio,A., Mammi,A., Patrone,S., Barbera,A., Origone,P.,
            Ponti,C., Sanguineri,F., Zara,F., Cataldi,M., Salpietro,V.,
            Venturi,C.B., Massucco,S., Schenone,A., Manganelli,F., Mandich,P.,
            Bellone,E. and Gotta,F.
  TITLE     A novel de novo variant in POLR3B gene associated with a primary
            axonal involvement of the largest nerve fibers
  JOURNAL   J Peripher Nerv Syst 28 (4), 620-628 (2023)
   PUBMED   37897416
  REMARK    GeneRIF: A novel de novo variant in POLR3B gene associated with a
            primary axonal involvement of the largest nerve fibers.
REFERENCE   2  (residues 1 to 1133)
  AUTHORS   Bai,H., Li,D., Zheng,Y. and Jiang,X.
  TITLE     Case report: Biallelic variants in POLR3B gene lead to 4H
            leukodystrophy from the study of brother and sister
  JOURNAL   Medicine (Baltimore) 101 (34), e30350 (2022)
   PUBMED   36042647
  REMARK    GeneRIF: Case report: Biallelic variants in POLR3B gene lead to 4H
            leukodystrophy from the study of brother and sister.
REFERENCE   3  (residues 1 to 1133)
  AUTHORS   Tetreault,M., Choquet,K., Orcesi,S., Tonduti,D., Balottin,U.,
            Teichmann,M., Fribourg,S., Schiffmann,R., Brais,B., Vanderver,A.
            and Bernard,G.
  TITLE     Recessive mutations in POLR3B, encoding the second largest subunit
            of Pol III, cause a rare hypomyelinating leukodystrophy
  JOURNAL   Am J Hum Genet 89 (5), 652-655 (2011)
   PUBMED   22036172
  REMARK    GeneRIF: Recessive mutations in POLR3B, encoding the second largest
            subunit of Pol III, cause a rare hypomyelinating leukodystrophy
REFERENCE   4  (residues 1 to 1133)
  AUTHORS   Saitsu,H., Osaka,H., Sasaki,M., Takanashi,J., Hamada,K.,
            Yamashita,A., Shibayama,H., Shiina,M., Kondo,Y., Nishiyama,K.,
            Tsurusaki,Y., Miyake,N., Doi,H., Ogata,K., Inoue,K. and
            Matsumoto,N.
  TITLE     Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits
            cause an autosomal-recessive hypomyelinating leukoencephalopathy
  JOURNAL   Am J Hum Genet 89 (5), 644-651 (2011)
   PUBMED   22036171
  REMARK    GeneRIF: Mutations in POLR3A and POLR3B encoding RNA Polymerase III
            subunits cause an autosomal-recessive hypomyelinating
            leukoencephalopathy
REFERENCE   5  (residues 1 to 1133)
  AUTHORS   Shen,E., Lei,Y., Liu,Q., Zheng,Y., Song,C., Marc,J., Wang,Y.,
            Sun,L. and Liang,Q.
  TITLE     Identification and characterization of INMAP, a novel interphase
            nucleus and mitotic apparatus protein that is involved in spindle
            formation and cell cycle progression
  JOURNAL   Exp Cell Res 315 (7), 1100-1116 (2009)
   PUBMED   19331820
  REMARK    GeneRIF: Results suggest that INMAP is a novel protein that plays
            essential role in spindle formation and cell-cycle progression.
REFERENCE   6  (residues 1 to 1133)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
  REMARK    GeneRIF: Data describe the purification and identification of RNA
            polymerase III subunits RPC2 and RPC5.
REFERENCE   7  (residues 1 to 1133)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   8  (residues 1 to 1133)
  AUTHORS   Bernard,G. and Vanderver,A.
  TITLE     POLR3-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22855961
REFERENCE   9  (residues 1 to 1133)
  AUTHORS   Balasubramanian,R. and Crowley,W.F. Jr.
  TITLE     Isolated Gonadotropin-Releasing Hormone (GnRH) Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301509
REFERENCE   10 (residues 1 to 1133)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX537447.1 and BC033724.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 5, 2009 this sequence version replaced NP_060552.3.
            
            Summary: This gene encodes the second largest subunit of RNA
            polymerase III, the polymerase responsible for synthesizing
            transfer and small ribosomal RNAs in eukaryotes. The largest
            subunit and the encoded protein form the catalytic center of RNA
            polymerase III. Mutations in this gene are a cause of
            hypomyelinating leukodystrophy. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537447.1, SRR1803615.228111.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000228347.9/ ENSP00000228347.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1133
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..1133
                     /product="DNA-directed RNA polymerase III subunit RPC2
                     isoform 1"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit B; RNA
                     polymerase III subunit C2; polymerase (RNA) III (DNA
                     directed) polypeptide B; DNA-directed RNA polymerase III
                     subunit RPC2; DNA-directed RNA polymerase III 127.6 kDa
                     polypeptide; interphase nucleus and mitotic apparatus
                     associated protein; polymerase (RNA) III subunit B"
                     /calculated_mol_wt=127655
     Region          39..1127
                     /region_name="RNA_pol_B_RPB2"
                     /note="RNA polymerase beta subunit. RNA polymerases
                     catalyse the DNA dependent polymerization of RNA.
                     Prokaryotes contain a single RNA polymerase compared to
                     three in eukaryotes (not including mitochondrial. and
                     chloroplast polymerases). Each RNA polymerase...; cd00653"
                     /db_xref="CDD:238353"
     Site            order(105,768,810,812,816..818,820)
                     /site_type="other"
                     /note="RPB12 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            429
                     /site_type="other"
                     /note="Critical in trapping poly(dT) in Pol III-mediated
                     transcription termination.
                     /evidence=ECO:0000305|PubMed:34675218; propagated from
                     UniProtKB/Swiss-Prot (Q9NW08.2)"
     Site            order(467,469..471,473,476,481,658,676..678,680,743..746,
                     749,751..753,904,906,908,930,932,935,938,943,947,964,991,
                     999..1001,1003,1016,1019..1021,1023..1024,1045..1047,1051,
                     1053..1054,1056,1058..1063,1065..1070,1074,1107,1111,1113,
                     1115..1116,1118,1120..1123,1125,1127)
                     /site_type="other"
                     /note="RPB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Region          539..600
                     /region_name="RNA_pol_Rpb2_4"
                     /note="RNA polymerase Rpb2, domain 4; pfam04566"
                     /db_xref="CDD:428012"
     Region          621..661
                     /region_name="RNA_pol_Rpb2_5"
                     /note="RNA polymerase Rpb2, domain 5; pfam04567"
                     /db_xref="CDD:428013"
     Site            order(716..717,738,740,761,764,913,926,953..954,956,987,
                     1004)
                     /site_type="other"
                     /note="RPB10 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(749,763,912,993)
                     /site_type="other"
                     /note="RPB11 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     Site            order(763..764,768,886,888,913..915,918,920..921,992..999,
                     1001)
                     /site_type="other"
                     /note="RPB3 interaction site [polypeptide binding]"
                     /db_xref="CDD:238353"
     CDS             1..1133
                     /gene="POLR3B"
                     /gene_synonym="C128; CMT1I; HLD8; INMAP; RPC2"
                     /coded_by="NM_018082.6:133..3534"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9105.1"
                     /db_xref="GeneID:55703"
                     /db_xref="HGNC:HGNC:30348"
                     /db_xref="MIM:614366"
ORIGIN      
        1 mdvlaeefgn ltpeqlaapi ptveekwrll paflkvkglv kqhidsfnyf inveikkimk
       61 anekvtsdad pmwylkylni yvglpdvees fnvtrpvsph ecrlrdmtys apitvdieyt
      121 rgsqriirna lpigrmpiml rssncvltgk tpaefaklne cpldpggyfi vkgvekvili
      181 qeqlsknrii veadrkgavg asvtssthek ksrtnmavkq grfylrhntl sedipiviif
      241 kamgvesdqe ivqmigteeh vmaafgpsle ecqkaqiftq mqalkyignk vrrqrmwggg
      301 pkktkieear ellastilth vpvkefnfra kciytavmvr rvilaqgdnk vddrdyygnk
      361 rlelagqlls llfedlfkkf nsemkkiadq vipkqraaqf dvvkhmrqdq itngmvnais
      421 tgnwslkrfk mdrqgvtqvl srlsyisalg mmtrissqfe ktrkvsgprs lqpsqwgmlc
      481 psdtpegeac glvknlalmt hittdmedgp ivklasnlgv edvnllcgee lsypnvflvf
      541 lngnilgvir dhkklvntfr lmrragyine fvsistnltd rcvyissdgg rlcrpyiivk
      601 kqkpavtnkh meelaqgyrn fedflheslv eyldvneend cnialyehti nkdtthleie
      661 pftllgvcag lipyphhnqs prntyqcamg kqamgtigyn qrnridtlmy llaypqkpmv
      721 ktktielief eklpagqnat vavmsysgyd iedalvlnka sldrgfgrcl vyknakctlk
      781 rytnqtfdkv mgpmldaatr kpiwrheild adgicspgek venkqvlvnk smptvtqipl
      841 egsnvpqqpq ykdvpitykg atdsyiekvm issnaedafl ikmllrqtrr peigdkfssr
      901 hgqkgvcgli vpqedmpfcd sgicpdiimn phgfpsrmtv gkliellagk agvldgrfhy
      961 gtafggskvk dvcedlvrhg ynylgkdyvt sgitgeplea yiyfgpvyyq klkhmvldkm
     1021 harargprav ltrqptegrs rdgglrlgem erdcligyga smlllerlmi ssdafevdvc
     1081 gqcgllgysg wchyckssch vsslripyac kllfqelqsm niiprlklsk yne
//
LOCUS       NP_006314               1268 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec24B isoform a [Homo sapiens].
ACCESSION   NP_006314 XP_946852 XP_950518
VERSION     NP_006314.2
DBSOURCE    REFSEQ: accession NM_006323.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Ryan,S.K., Zelic,M., Han,Y., Teeple,E., Chen,L., Sadeghi,M.,
            Shankara,S., Guo,L., Li,C., Pontarelli,F., Jensen,E.H., Comer,A.L.,
            Kumar,D., Zhang,M., Gans,J., Zhang,B., Proto,J.D., Saleh,J.,
            Dodge,J.C., Savova,V., Rajpal,D., Ofengeim,D. and Hammond,T.R.
  TITLE     Microglia ferroptosis is regulated by SEC24B and contributes to
            neurodegeneration
  JOURNAL   Nat Neurosci 26 (1), 12-26 (2023)
   PUBMED   36536241
  REMARK    GeneRIF: Microglia ferroptosis is regulated by SEC24B and
            contributes to neurodegeneration.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Yang,X.Y., Zhou,X.Y., Wang,Q.Q., Li,H., Chen,Y., Lei,Y.P., Ma,X.H.,
            Kong,P., Shi,Y., Jin,L., Zhang,T. and Wang,H.Y.
  TITLE     Mutations in the COPII vesicle component gene SEC24B are associated
            with human neural tube defects
  JOURNAL   Hum Mutat 34 (8), 1094-1101 (2013)
   PUBMED   23592378
  REMARK    GeneRIF: results show that functional mutations in SEC24B might
            contribute to the etiology of a subset of human Neural Tube Defects
            (NTDs).
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Tao,W.A., Wollscheid,B., O'Brien,R., Eng,J.K., Li,X.J.,
            Bodenmiller,B., Watts,J.D., Hood,L. and Aebersold,R.
  TITLE     Quantitative phosphoproteome analysis using a dendrimer conjugation
            chemistry and tandem mass spectrometry
  JOURNAL   Nat Methods 2 (8), 591-598 (2005)
   PUBMED   16094384
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC143268.1, BC040137.1,
            H15283.1 and AC105314.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 16, 2006 this sequence version replaced NP_006314.1.
            
            Summary: The protein encoded by this gene is a member of the SEC24
            subfamily of the SEC23/SEC24 family, which is involved in vesicle
            trafficking. The encoded protein is thought to be a cargo-binding
            component of the COPII vesicle, and is thought to be involved in
            the transport of secretory proteins from the endoplasmic reticulum
            to the Golgi apparatus. Mutations in this gene have been associated
            with neural tube defects, and are thought to be a result of a
            disruption in interactions with the protein encoded by the VANGL
            planar cell polarity protein 2 (VANGL2) gene. Alternative splicing
            results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) lacks an in-frame exon in the
            5' coding region and uses an alternate in-frame splice site in the
            central coding region, compared to variant 3. The encoded isoform
            (a) is shorter, compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC040137.1, SRR1803612.239683.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265175.5/ ENSP00000265175.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..1268
                     /product="protein transport protein Sec24B isoform a"
                     /note="protein transport protein Sec24B; SEC24 homolog B,
                     COPII coat complex component; secretory protein 24; SEC24
                     related gene family, member B"
                     /calculated_mol_wt=137287
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O95487.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95487.2)"
     Region          216..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Region          303..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95487.2)"
     Region          362..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Region          463..1259
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Region          605..629
                     /region_name="Zinc finger-like"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Region          1141..1213
                     /region_name="Gelsolin-like. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95487.2)"
     Site            1224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95487.2)"
     CDS             1..1268
                     /gene="SEC24B"
                     /gene_synonym="SEC24"
                     /coded_by="NM_006323.5:56..3862"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47124.1"
                     /db_xref="GeneID:10427"
                     /db_xref="HGNC:HGNC:10704"
                     /db_xref="MIM:607184"
ORIGIN      
        1 msapagsshp aasarippkf ggaavsgaaa pagpgagpap hqqngpaqnq mqvpsgyglh
       61 hqnyiapsgh ysqgpgkmts lpldtqcgdy ysalytvptq nvtpntvnqq pgaqqlysrg
      121 ppaphivgst lgsfqgaass ashlhtsasq pyssfvnhyn spamysasss vasqgfpstc
      181 ghyamstvsn aaypsvsyps lpagdtygqm ftsqnaptvr pvkdnsfsgq ntaishpspl
      241 pplpsqqhhq qqslsgystl twsspglpst qdnlirnhtg slavannnpt itvadslscp
      301 vmqnvqppks spvvstvlsg ssgssstrtp ptanhpvepv tsvtqpsell qqkgvqygey
      361 vnnqassapt plsstsddee eeeedeeagv dsssttssas pmpnsydale ggsypdmlss
      421 sasspapdpa pepdpasapa pasapapvvp qpskmakpfg ygyptlqpgy qnataplisg
      481 vqpsnpvysg fqqypqqypg vnqlsssigg lslqsspqpe slrpvnltqe rnilpmtpvw
      541 apvpnlnadl kklncspdsf rctltnipqt qallnkaklp lglllhpfrd ltqlpvitsn
      601 tivrcrscrt yinpfvsfid qrrwkcnlcy rvndvpeefm ynpltrsyge phkrpevqns
      661 tvefiassdy mlrppqpavy lfvldvshna veagyltilc qsllenldkl pgdsrtrigf
      721 mtfdstihfy nlqeglsqpq mlivsdiddv flptpdsllv nlyeskelik dllnalpnmf
      781 tntrethsal gpalqaafkl msptggrvsv fqtqlpslga gllqsredpn qrsstkvvqh
      841 lgpatdfykk laldcsgqqt avdlfllssq ysdlaslacm skysagciyy ypsfhythnp
      901 sqaeklqkdl kryltrkigf eavmrirctk glsmhtfhgn ffvrstdlls laninpdagf
      961 avqlsieesl tdtslvcfqt allytsskge rrirvhtlcl pvvssladvy agvdvqaaic
     1021 llanmavdrs vssslsdard alvnavvdsl saygstvsnl qhsalmapss lklfplyvla
     1081 llkqkafrtg tstrlddrvy amcqiksqpl vhlmkmihpn lyridrltde gavhvndriv
     1141 pqpplqklsa ekltregafl mdcgsvfyiw vgkgcdnnfi edvlgytnfa sipqkmthlp
     1201 eldtlssera rsfitwlrds rplspilhiv kdespakaef fqhliedrte aafsyyefll
     1261 hvqqqick
//
LOCUS       NP_703190                720 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor C isoform 1 precursor [Homo sapiens].
ACCESSION   NP_703190
VERSION     NP_703190.2
DBSOURCE    REFSEQ: accession NM_153460.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 720)
  AUTHORS   Arikan,S., Ozturk,O., Duygulu,S., Atalay,E.O. and Atalay,A.
  TITLE     Associations of IL-17 and IL-17 receptor polymorphisms with
            Behcet's disease in Denizli Province of Turkey
  JOURNAL   Immunol Res 71 (4), 600-608 (2023)
   PUBMED   36701075
  REMARK    GeneRIF: Associations of IL-17 and IL-17 receptor polymorphisms
            with Behcet's disease in Denizli Province of Turkey.
REFERENCE   2  (residues 1 to 720)
  AUTHORS   Kang,J.H., Park,S., Rho,J., Hong,E.J., Cho,Y.E., Won,Y.S. and
            Kwon,H.J.
  TITLE     IL-17A promotes Helicobacter pylori-induced gastric carcinogenesis
            via interactions with IL-17RC
  JOURNAL   Gastric Cancer 26 (1), 82-94 (2023)
   PUBMED   36125689
  REMARK    GeneRIF: IL-17A promotes Helicobacter pylori-induced gastric
            carcinogenesis via interactions with IL-17RC.
REFERENCE   3  (residues 1 to 720)
  AUTHORS   Goepfert,A., Barske,C., Lehmann,S., Wirth,E., Willemsen,J.,
            Gudjonsson,J.E., Ward,N.L., Sarkar,M.K., Hemmig,R., Kolbinger,F.
            and Rondeau,J.M.
  TITLE     IL-17-induced dimerization of IL-17RA drives the formation of the
            IL-17 signalosome to potentiate signaling
  JOURNAL   Cell Rep 41 (3), 111489 (2022)
   PUBMED   36260993
REFERENCE   4  (residues 1 to 720)
  AUTHORS   Huang,X., Li,Z., Shen,X., Nie,N. and Shen,Y.
  TITLE     IL-17 upregulates MCP-1 expression via Act1 / TRAF6 / TAK1 in
            experimental autoimmune myocarditis
  JOURNAL   Cytokine 152, 155823 (2022)
   PUBMED   35183823
  REMARK    Erratum:[Cytokine. 2022 Jun;154:155879. doi:
            10.1016/j.cyto.2022.155879. PMID: 35413623]
REFERENCE   5  (residues 1 to 720)
  AUTHORS   Schmidt,T., Luebbe,J., Kilian,C., Riedel,J.H., Hiekmann,S.,
            Asada,N., Ginsberg,P., Robben,L., Song,N., Kaffke,A., Peters,A.,
            Borchers,A., Flavell,R.A., Gagliani,N., Pelzcar,P., Huber,S.,
            Huber,T.B., Turner,J.E., Paust,H.J., Krebs,C.F. and Panzer,U.
  TITLE     IL-17 Receptor C Signaling Controls CD4+ TH17 Immune Responses and
            Tissue Injury in Immune-Mediated Kidney Diseases
  JOURNAL   J Am Soc Nephrol 32 (12), 3081-3098 (2021)
   PUBMED   35167487
  REMARK    GeneRIF: IL-17 Receptor C Signaling Controls CD4(+) TH17 Immune
            Responses and Tissue Injury in Immune-Mediated Kidney Diseases.
REFERENCE   6  (residues 1 to 720)
  AUTHORS   Haudenschild,D.R., Curtiss,S.B., Moseley,T.A. and Reddi,A.H.
  TITLE     Generation of interleukin-17 receptor-like protein (IL-17RL) in
            prostate by alternative splicing of RNA
  JOURNAL   Prostate 66 (12), 1268-1274 (2006)
   PUBMED   16688746
  REMARK    GeneRIF: IL-17RL exists as multiple isoforms due to extensive
            alternative splicing. Changes in RNA IL-17RL splicing occur in
            advanced cancers.
REFERENCE   7  (residues 1 to 720)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 720)
  AUTHORS   Gerritsen,M.E., Tomlinson,J.E., Zlot,C., Ziman,M. and Hwang,S.
  TITLE     Using gene expression profiling to identify the molecular basis of
            the synergistic actions of hepatocyte growth factor and vascular
            endothelial growth factor in human endothelial cells
  JOURNAL   Br J Pharmacol 140 (4), 595-610 (2003)
   PUBMED   14504135
  REMARK    Review article
REFERENCE   9  (residues 1 to 720)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 720)
  AUTHORS   Haudenschild,D., Moseley,T., Rose,L. and Reddi,A.H.
  TITLE     Soluble and transmembrane isoforms of novel interleukin-17
            receptor-like protein by RNA splicing and expression in prostate
            cancer
  JOURNAL   J Biol Chem 277 (6), 4309-4316 (2002)
   PUBMED   11706037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC381087.1, AK225650.1,
            AC018809.5, AF458065.1, AK096824.1 and AY358840.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 16, 2018 this sequence version replaced NP_703190.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that shares similarity with the interleukin-17 receptor (IL-17RA).
            Unlike IL-17RA, which is predominantly expressed in hemopoietic
            cells, and binds with high affinity to only IL-17A, this protein is
            expressed in nonhemopoietic tissues, and binds both IL-17A and
            IL-17F with similar affinities. The proinflammatory cytokines,
            IL-17A and IL-17F, have been implicated in the progression of
            inflammatory and autoimmune diseases. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            detected for this gene, and it has been proposed that soluble,
            secreted proteins lacking transmembrane and intracellular domains
            may function as extracellular antagonists to cytokine signaling.
            [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript containing all the coding exons, and encodes isoform 1
            (also known as IL-17RCFL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF458065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403601.8/ ENSP00000384969.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..720
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..720
                     /product="interleukin-17 receptor C isoform 1 precursor"
                     /note="IL17F receptor; IL-17RL; IL17Rhom; zcytoR14; IL-17
                     receptor C; interleukin-17 receptor homolog;
                     interleukin-17 receptor-like protein"
                     /calculated_mol_wt=76525
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          71..459
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          519..666
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..720
                     /gene="IL17RC"
                     /gene_synonym="CANDF9; IL17-RL; IL17RL"
                     /coded_by="NM_153460.4:219..2381"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS46746.1"
                     /db_xref="GeneID:84818"
                     /db_xref="HGNC:HGNC:18358"
                     /db_xref="MIM:610925"
ORIGIN      
        1 mpvpwfllsl algrspvvls lerlvgpqda thcspglscr lwdsdilclp gdivpapgpv
       61 lapthlqtel vlrcqketdc dlclrvavhl avhghweepe deekfggaad sgveeprnas
      121 lqaqvvlsfq ayptarcvll evqvpaalvq fgqsvgsvvy dcfeaalgse vriwsytqpr
      181 yekelnhtqq lpdcrglevw nsipscwalp wlnvsadgdn vhlvlnvsee qhfglslywn
      241 qvqgppkprw hknltgpqii tlnhtdlvpc lciqvwplep dsvrtnicpf redprahqnl
      301 wqaarlqllt lqswlldapc slpaeaalcw rapggdpcqp lvpplswenv tvdkvlefpl
      361 lkghpnlcvq vnsseklqlq eclwadslgp lkddvlllet rgpqdnrslc alepsgctsl
      421 pskastraar lgeyllqdlq sgqclqlwdd dlgalwacpm dkyihkrwal vwlacllfaa
      481 alslilllkk dhakgwlrll kqdvrsgaaa rgraalllys addsgferlv galasalcql
      541 plrvavdlws rrelsaqgpv awfhaqrrqt lqeggvvvll fspgavalcs ewlqdgvsgp
      601 gahgphdafr aslscvlpdf lqgrapgsyv gacfdrllhp davpalfrtv pvftlpsqlp
      661 dflgalqqpr aprsgrlqer aeqvsralqp aldsyfhppg tpapgrgvgp gagpgagdgt
//
LOCUS       NP_001287844             264 aa            linear   PRI 20-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 10
            [Homo sapiens].
ACCESSION   NP_001287844 XP_005271079
VERSION     NP_001287844.1
DBSOURCE    REFSEQ: accession NM_001300915.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA188681.1, BX647515.1,
            BC016285.1, BX369882.1 and AA761973.1.
            
            On Jul 16, 2014 this sequence version replaced XP_005271079.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Transcript Variant: This variant (10) differs in both the 5' and 3'
            exon structures, compared to variant 1. The encoded isoform (10)
            has distinct N- and C-termini and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647515.1, SRR7410570.16155.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..264
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 10"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=30367
     Region          48..>264
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(56..59,62,64,77,79,111,127..130,173,177..178,180,
                     190..191)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..264
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001300915.2:314..1108"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS72814.1"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 msarkssdas acssseisds fvkeflakak edflkkwenp tqnnagledf erkktlgtgs
       61 fgrvmlvkhk ateqyyamki ldkqkvvklk qiehtlnekr ilqavnfpfl vrleyafkdn
      121 snlymvmeyv pggemfshlr rigrfsepha rfyaaqivlt feylhsldli yrdlkpenll
      181 idhqgyiqvt dfgfakrvkg rtwtlcgtpe ylapeiilsk gynkavdwwa lgvliyemaa
      241 gyppffadqp iqiyekivsg kqnf
//
LOCUS       NP_001135915             508 aa            linear   PRI 20-NOV-2025
DEFINITION  enhancer of mRNA-decapping protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001135915
VERSION     NP_001135915.1
DBSOURCE    REFSEQ: accession NM_001142443.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Rudolph,C., Sigruener,A., Hartmann,A., Orso,E., Bals-Pratsch,M.,
            Gronwald,W., Seifert,B., Kalbitzer,H.R., Verdorfer,I.,
            Luetjens,C.M., Ortmann,O., Bornstein,S.R. and Schmitz,G.
  TITLE     ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and
            hYjeF_N3 comprise the YjeF_N domain protein family in humans with a
            role in spermiogenesis and oogenesis
  JOURNAL   Horm Metab Res 39 (5), 322-335 (2007)
   PUBMED   17533573
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Albrecht,M. and Lengauer,T.
  TITLE     Novel Sm-like proteins with long C-terminal tails and associated
            methyltransferases
  JOURNAL   FEBS Lett 569 (1-3), 18-26 (2004)
   PUBMED   15225602
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091230.23, BC021271.2,
            BM999594.1, AL133447.1 and CA440205.1.
            
            Summary: This gene encodes a protein that is important in mRNA
            degradation. The encoded protein is a component of a decapping
            complex that promotes efficient removal of the monomethylguanosine
            (m7G) cap from mRNAs, as part of the 5' to 3' mRNA decay pathway.
            Mutations in this gene have been identified in human patients with
            an autosomal recessive form of intellectual disability. [provided
            by RefSeq, May 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1-4 encode
            the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021271.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..508
                     /product="enhancer of mRNA-decapping protein 3 isoform 1"
                     /note="LSM16 homolog (EDC3, S. cerevisiae); enhancer of
                     mRNA-decapping protein 3; yjeF domain-containing protein
                     1; yjeF N-terminal domain-containing protein 2; yjeF
                     domain containing; enhancer of mRNA decapping 3 homolog"
                     /calculated_mol_wt=55947
     Region          1..79
                     /region_name="Required for P-body targeting and
                     interaction with DCP1A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          2..66
                     /region_name="LSm16_N"
                     /note="Like-Sm protein 16, N-terminal domain; cd01737"
                     /db_xref="CDD:212484"
     Site            order(2,5,28,33,56,59..64)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212484"
     Site            order(10..15,19..30,33..36)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212484"
     Site            order(29,55)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212484"
     Site            51..62
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212484"
     Region          95..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          102..194
                     /region_name="Edc3_linker"
                     /note="Linker region of enhancer of mRNA-decapping protein
                     3; pfam16598"
                     /db_xref="CDD:465188"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          191..296
                     /region_name="Required for interaction with DDX6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          198..301
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     Region          302..455
                     /region_name="YjeF_N"
                     /note="YjeF-related protein N-terminus; pfam03853"
                     /db_xref="CDD:427546"
     CDS             1..508
                     /gene="EDC3"
                     /gene_synonym="hYjeF_N2-15q23; LSM16; MRT50; YJDC; YJEFN2"
                     /coded_by="NM_001142443.3:468..1994"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10267.1"
                     /db_xref="GeneID:80153"
                     /db_xref="HGNC:HGNC:26114"
                     /db_xref="MIM:609842"
ORIGIN      
        1 matdwlgsiv sincgdslgv yqgrvsavdq vsqtisltrp fhngvkclvp evtfragdit
       61 elkileipgp gdnqhfgdlh qtelgpsgag cqvginqngt gkfvkkpass ssapqnipkr
      121 tdvksqdvav spqqqqcsks yvdrhmesls qsksfrrrhn swssssrhpn qatpkksglk
      181 ngqmknkdde cfgddieeip dtdfdfegnl alfdkaavfe eidtyerrsg trsrgipner
      241 ptryrhdeni lesepivyrr iivphnvske fctdsglvvp sisyelhkkl lsvaekhglt
      301 lerrlemtgv casqmaltll ggpnrlnpkn vhqrptvall cgphvkgaqg iscgrhlanh
      361 dvqvilflpn fvkmlesitn elslfsktqg qqvsslkdlp tspvdlvinc ldcpenvflr
      421 dqpwykaava wanqnrapvl sidppvheve qgidakwsla lglplplgeh agriylcdig
      481 ipqqvfqevg inyhspfgck fviplhsa
//
LOCUS       NP_001354601             774 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ii [Homo sapiens].
ACCESSION   NP_001354601
VERSION     NP_001354601.1
DBSOURCE    REFSEQ: accession NM_001367672.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.267048.1,
                                           SRR1803617.188107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..774
                     /product="SUN domain-containing protein 1 isoform ii"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=85774
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <365..>561
                     /region_name="rad50"
                     /note="TIGR00606"
                     /db_xref="CDD:129694"
     Region          407..459
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(409..410,413,416..417,420..421,423..424,427..428,
                     430..431,434..435,437..438,441,444..445,448,451..452,
                     455..456,458..459)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          536..594
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          637..772
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..774
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367672.1:52..2376"
                     /note="isoform ii is encoded by transcript variant 35"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllaglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl qgdseafpwh
      361 wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas tdfmafhqeh
      421 evrmshledi lgklreksea iqkeleqtkq ktisavgeql lptvehlqle ldqlkselss
      481 wrhvktgcet vdavqervdv qvremvkllf sedqqggsle qllqrfssqf vskgdlqtml
      541 rdlqlqilrn vthhvsvtkq lptseavvsa vseagasgit eaqaraivns alklysqdkt
      601 gmvdfalesg ggsilstrcs etyetktalm slfgiplwyf sqsprvviqp diypgncwaf
      661 kgsqgylvvr lsmmihpaaf tlehipktls ptgnissapk dfavyglene yqeegqllgq
      721 ftydqdgesl qmfqalkrpd dtafqivelr ifsnwghpey tclyrfrvhg epvk
//
LOCUS       NP_001290167             700 aa            linear   PRI 20-NOV-2025
DEFINITION  integrin beta-2 isoform 2 [Homo sapiens].
ACCESSION   NP_001290167
VERSION     NP_001290167.1
DBSOURCE    REFSEQ: accession NM_001303238.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 700)
  AUTHORS   Kling,L., Eulenberg-Gustavus,C., Jerke,U., Rousselle,A.,
            Eckardt,K.U., Schreiber,A. and Kettritz,R.
  TITLE     beta2-integrins control HIF1alpha activation in human neutrophils
  JOURNAL   Front Immunol 15, 1406967 (2024)
   PUBMED   39469705
  REMARK    GeneRIF: beta2-integrins control HIF1alpha activation in human
            neutrophils.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 700)
  AUTHORS   Xie,H., Jiang,Y., Xiang,Y., Wu,B., Zhao,J., Huang,R., Wang,M.,
            Wang,Y., Liu,J., Wu,D., Tian,D. and Bian,E.
  TITLE     Super-enhancer-driven LIF promotes the mesenchymal transition in
            glioblastoma by activating ITGB2 signaling feedback in microglia
  JOURNAL   Neuro Oncol 26 (8), 1438-1452 (2024)
   PUBMED   38554116
  REMARK    GeneRIF: Super-enhancer-driven LIF promotes the mesenchymal
            transition in glioblastoma by activating ITGB2 signaling feedback
            in microglia.
REFERENCE   3  (residues 1 to 700)
  AUTHORS   Li,J., Cao,D., Jiang,L., Zheng,Y., Shao,S., Zhuang,A. and Xiang,D.
  TITLE     ITGB2-ICAM1 axis promotes liver metastasis in BAP1-mutated uveal
            melanoma with retained hypoxia and ECM signatures
  JOURNAL   Cell Oncol (Dordr) 47 (3), 951-965 (2024)
   PUBMED   38150154
  REMARK    GeneRIF: ITGB2-ICAM1 axis promotes liver metastasis in BAP1-mutated
            uveal melanoma with retained hypoxia and ECM signatures.
REFERENCE   4  (residues 1 to 700)
  AUTHORS   Fawcett,J., Holness,C.L., Needham,L.A., Turley,H., Gatter,K.C.,
            Mason,D.Y. and Simmons,D.L.
  TITLE     Molecular cloning of ICAM-3, a third ligand for LFA-1,
            constitutively expressed on resting leukocytes
  JOURNAL   Nature 360 (6403), 481-484 (1992)
   PUBMED   1448173
REFERENCE   5  (residues 1 to 700)
  AUTHORS   Corbi,A.L., Vara,A., Ursa,A., Garcia Rodriguez,M.C., Fontan,G. and
            Sanchez-Madrid,F.
  TITLE     Molecular basis for a severe case of leukocyte adhesion deficiency
  JOURNAL   Eur J Immunol 22 (7), 1877-1881 (1992)
   PUBMED   1352501
REFERENCE   6  (residues 1 to 700)
  AUTHORS   Back,A.L., Kwok,W.W. and Hickstein,D.D.
  TITLE     Identification of two molecular defects in a child with leukocyte
            adherence deficiency
  JOURNAL   J Biol Chem 267 (8), 5482-5487 (1992)
   PUBMED   1347532
REFERENCE   7  (residues 1 to 700)
  AUTHORS   Nelson,C., Rabb,H. and Arnaout,M.A.
  TITLE     Genetic cause of leukocyte adhesion molecule deficiency. Abnormal
            splicing and a missense mutation in a conserved region of CD18
            impair cell surface expression of beta 2 integrins
  JOURNAL   J Biol Chem 267 (5), 3351-3357 (1992)
   PUBMED   1346613
REFERENCE   8  (residues 1 to 700)
  AUTHORS   Weitzman,J.B., Wells,C.E., Wright,A.H., Clark,P.A. and Law,S.K.
  TITLE     The gene organisation of the human beta 2 integrin subunit (CD18)
  JOURNAL   FEBS Lett 294 (1-2), 97-103 (1991)
   PUBMED   1683838
REFERENCE   9  (residues 1 to 700)
  AUTHORS   Law,S.K., Gagnon,J., Hildreth,J.E., Wells,C.E., Willis,A.C. and
            Wong,A.J.
  TITLE     The primary structure of the beta-subunit of the cell surface
            adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship
            to the fibronectin receptor
  JOURNAL   EMBO J 6 (4), 915-919 (1987)
   PUBMED   2954816
REFERENCE   10 (residues 1 to 700)
  AUTHORS   Kishimoto,T.K., O'Connor,K., Lee,A., Roberts,T.M. and Springer,T.A.
  TITLE     Cloning of the beta subunit of the leukocyte adhesion proteins:
            homology to an extracellular matrix receptor defines a novel
            supergene family
  JOURNAL   Cell 48 (4), 681-690 (1987)
   PUBMED   3028646
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU279404.1, AK303488.1,
            M15395.1 and CA447686.1.
            
            Summary: This gene encodes an integrin beta chain, which combines
            with multiple different alpha chains to form different integrin
            heterodimers. Integrins are integral cell-surface proteins that
            participate in cell adhesion as well as cell-surface mediated
            signalling. The encoded protein plays an important role in immune
            response and defects in this gene cause leukocyte adhesion
            deficiency. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (3) has a shorter 5' UTR, uses an
            alternate splice site in the 5' region, and initiates translation
            at a downstream start codon, compared to variant 1. The encoded
            isoform (2) has a shorter N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303488.1, SRR14038196.3517891.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..700
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..700
                     /product="integrin beta-2 isoform 2"
                     /note="integrin beta-2; leukocyte-associated antigens
                     CD18/11A, CD18/11B, CD18/11C; complement receptor C3
                     beta-subunit; cell surface adhesion glycoprotein
                     (LFA-1/CR3/P150,959 beta subunit precursor); leukocyte
                     cell adhesion molecule CD18; integrin beta chain, beta 2;
                     integrin, beta 2 (complement component 3 receptor 3 and 4
                     subunit)"
                     /calculated_mol_wt=77224
     Region          1..378
                     /region_name="INB"
                     /note="Integrin beta subunits (N-terminal portion of
                     extracellular region); smart00187"
                     /db_xref="CDD:197563"
     Region          <388..407
                     /region_name="I-EGF_1"
                     /note="Integrin beta epidermal growth factor like domain
                     1; pfam18372"
                     /db_xref="CDD:465729"
     Region          553..630
                     /region_name="Integrin_B_tail"
                     /note="Integrin beta tail domain; pfam07965"
                     /db_xref="CDD:462325"
     Region          658..697
                     /region_name="Integrin_b_cyt"
                     /note="Integrin beta cytoplasmic domain; pfam08725"
                     /db_xref="CDD:462580"
     CDS             1..700
                     /gene="ITGB2"
                     /gene_synonym="CD18; LAD; LCAMB; LFA-1; MAC-1; MF17; MFI7"
                     /coded_by="NM_001303238.2:333..2435"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:3689"
                     /db_xref="HGNC:HGNC:6155"
                     /db_xref="MIM:600065"
ORIGIN      
        1 mrgcaaddim dptslaetqe dhnggqkqls pqkvtlylrp gqaaafnvtf rrakgypidl
       61 yylmdlsysm lddlrnvkkl ggdllralne itesgrigfg sfvdktvlpf vnthpdklrn
      121 pcpnkekecq ppfafrhvlk ltnnsnqfqt evgkqlisgn ldapegglda mmqvaacpee
      181 igwrnvtrll vfatddgfhf agdgklgail tpndgrchle dnlykrsnef dypsvgqlah
      241 klaenniqpi favtsrmvkt yeklteiipk savgelseds snvvhlikna ynklssrvfl
      301 dhnalpdtlk vtydsfcsng vthrnqprgd cdgvqinvpi tfqvkvtate ciqeqsfvir
      361 algftdivtv qvlpqcecrc rdqsrdrslc hgkgflecgi crcdtgyigk ncecqtqgrs
      421 sqelegscrk dnnsiicsgl gdcvcgqclc htsdvpgkli ygqycecdti nceryngqvc
      481 ggpgrglcfc gkcrchpgfe gsacqcertt egclnprrve csgrgrcrcn vcechsgyql
      541 plcqecpgcp spcgkyisca eclkfekgpf gkncsaacpg lqlsnnpvkg rtckerdseg
      601 cwvaytleqq dgmdryliyv desrecvagp niaaivggtv agivligill lviwkalihl
      661 sdlreyrrfe keklksqwnn dnplfksatt tvmnpkfaes
//
LOCUS       NP_001336174             828 aa            linear   PRI 20-NOV-2025
DEFINITION  trafficking kinesin-binding protein 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001336174
VERSION     NP_001336174.1
DBSOURCE    REFSEQ: accession NM_001349245.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 828)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 828)
  AUTHORS   Baltrusaitis,E.E., Ravitch,E.E., Fenton,A.R., Perez,T.A.,
            Holzbaur,E.L.F. and Dominguez,R.
  TITLE     Interaction between the mitochondrial adaptor MIRO and the motor
            adaptor TRAK
  JOURNAL   J Biol Chem 299 (12), 105441 (2023)
   PUBMED   37949220
  REMARK    GeneRIF: Interaction between the mitochondrial adaptor MIRO and the
            motor adaptor TRAK.
REFERENCE   3  (residues 1 to 828)
  AUTHORS   Benhamida,J.K., Harmsen,H.J., Ma,D., William,C.M., Li,B.K.,
            Villafania,L., Sukhadia,P., Mullaney,K.A., Dewan,M.C., Vakiani,E.,
            Karajannis,M.A., Snuderl,M., Zagzag,D., Ladanyi,M., Rosenblum,M.K.
            and Bale,T.A.
  TITLE     Recurrent TRAK1::RAF1 Fusions in pediatric low-grade gliomas
  JOURNAL   Brain Pathol 33 (5), e13185 (2023)
   PUBMED   37399073
  REMARK    GeneRIF: Recurrent TRAK1::RAF1 Fusions in pediatric low-grade
            gliomas.
REFERENCE   4  (residues 1 to 828)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 828)
  AUTHORS   Wu,H., Liu,Y., Li,H., Du,C., Li,K., Dong,S., Meng,Q. and Zhang,H.
  TITLE     TRAK1-Mediated Abnormality of Mitochondrial Fission Increases
            Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Mol Neurobiol 58 (3), 1237-1247 (2021)
   PUBMED   33119838
  REMARK    GeneRIF: TRAK1-Mediated Abnormality of Mitochondrial Fission
            Increases Seizure Susceptibility in Temporal Lobe Epilepsy.
REFERENCE   6  (residues 1 to 828)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   7  (residues 1 to 828)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
  REMARK    GeneRIF: GRIF-1 and OIP106 have roles in protein and/or organelle
            transport in excitable cells in a manner analogous to glutamate
            receptor-interacting-protein 1
REFERENCE   8  (residues 1 to 828)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 828)
  AUTHORS   Iyer,S.P. and Hart,G.W.
  TITLE     Roles of the tetratricopeptide repeat domain in O-GlcNAc
            transferase targeting and protein substrate specificity
  JOURNAL   J Biol Chem 278 (27), 24608-24616 (2003)
   PUBMED   12724313
REFERENCE   10 (residues 1 to 828)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093414.3 and AC018358.20.
            
            Transcript Variant: This variant (6) encodes isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.4612.1,
                                           SRR1803612.128777.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..828
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..828
                     /product="trafficking kinesin-binding protein 1 isoform 6"
                     /note="OGT(O-Glc-NAc transferase)-interacting protein 106
                     KDa; 106 kDa O-GlcNAc transferase-interacting protein;
                     milton homolog 1; O-linked N-acetylglucosamine transferase
                     interacting protein 106; protein Milton; trafficking
                     protein, kinesin binding 1"
                     /calculated_mol_wt=91891
     Region          1..249
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          310..479
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     CDS             1..828
                     /gene="TRAK1"
                     /gene_synonym="DEE68; EIEE68; MILT1; OIP106"
                     /coded_by="NM_001349245.1:423..2909"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:22906"
                     /db_xref="HGNC:HGNC:29947"
                     /db_xref="MIM:608112"
ORIGIN      
        1 mtktyndida vtrlleeker dlelaarigq sllkknktlt ernelleeqv ehireevsql
       61 rhelsmkdel lqfytsaaee sepesvcstp lkrnessssv qnyfhldslq kklkdleeen
      121 vvlrseasql ktetityeek eqqlvndcvk elrdanvqia siseelakkt edaarqqeei
      181 thllsqivdl qkkakacave neelvqhlga akdaqrqlta elreledkya ecmemlheaq
      241 eelknlrnkt mpnttsrryh slglfpmdsl aaeiegtmrk elqleeaesp dithqkrvfe
      301 tvrninqvvk qrsltpspmn ipgsnqssam nsllsscvst prssfygsdi gnvvldnktn
      361 siileteaad lgnderskkp gtpgtpgshd letalrrlsl rrenylserr ffeeeqerkl
      421 qelaekgelr sgsltptesi mslgthsrfs eftgfsgmsf ssrsylpekl qivkplegsa
      481 tlhhwqqlaq phlggildpr pgvvtkgfrt ldvdldevyc lndfeeddta hhpgkcmsqt
      541 nstftfttcr ilhpsdeltr vtpslnsapt pacgstshlk stpvatpctp rrlslaesft
      601 ntrestttms tslglvwllk ergisaavyd pqswdragrg sllhsytpkm avipstppns
      661 pmqtptsspp sfefkctspp ydnflaskpa ssilrevrek nvrssesqtd vsvsnlnlvd
      721 kvrrfgvakv vnsgrahvpt lteeqgpllc gppgpapalv prglvpeglp lrcptvtsai
      781 gglqlnsgir rnrsfptmvg ssmqmkapvt ltsgilmgak lskqtslr
//
LOCUS       NP_005721                271 aa            linear   PRI 20-NOV-2025
DEFINITION  carboxy-terminal domain RNA polymerase II polypeptide A small
            phosphatase 2 [Homo sapiens].
ACCESSION   NP_005721
VERSION     NP_005721.3
DBSOURCE    REFSEQ: accession NM_005730.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Krasnov,G.S., Puzanov,G.A., Afanasyeva,M.A., Dashinimaev,E.B.,
            Vishnyakova,K.S., Beniaminov,A.D., Adzhubei,A.A., Kondratieva,T.T.,
            Yegorov,Y.E. and Senchenko,V.N.
  TITLE     Tumor suppressor properties of the small C-terminal domain
            phosphatases in non-small cell lung cancer
  JOURNAL   Biosci Rep 39 (12) (2019)
   PUBMED   31774910
  REMARK    GeneRIF: Tumor suppressor properties of the small C-terminal domain
            phosphatases in non-small cell lung cancer.
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Thompson,J., Lepikhova,T., Teixido-Travesa,N., Whitehead,M.A.,
            Palvimo,J.J. and Janne,O.A.
  TITLE     Small carboxyl-terminal domain phosphatase 2 attenuates
            androgen-dependent transcription
  JOURNAL   EMBO J 25 (12), 2757-2767 (2006)
   PUBMED   16724108
  REMARK    GeneRIF: These results suggest that SCP2 is involved in promoter
            clearance during steroid-activated transcription.
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Yeo,M., Lin,P.S., Dahmus,M.E. and Gill,G.N.
  TITLE     A novel RNA polymerase II C-terminal domain phosphatase that
            preferentially dephosphorylates serine 5
  JOURNAL   J Biol Chem 278 (28), 26078-26085 (2003)
   PUBMED   12721286
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Su,Y.A., Lee,M.M., Hutter,C.M. and Meltzer,P.S.
  TITLE     Characterization of a highly conserved gene (OS4) amplified with
            CDK4 in human sarcomas
  JOURNAL   Oncogene 15 (11), 1289-1294 (1997)
   PUBMED   9315096
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Beutler,E., Gelbart,T., West,C., Kuhl,W. and Lee,P.
  TITLE     A strategy for cloning the hereditary hemochromatosis gene
  JOURNAL   Blood Cells Mol Dis 21 (3), 207-216 (1995)
   PUBMED   8673473
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Su,Y.A., Trent,J.M., Guan,X.Y. and Meltzer,P.S.
  TITLE     Direct isolation of genes encoded within a homogeneously staining
            region by chromosome microdissection
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 9121-9125 (1994)
   PUBMED   8090779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CN313995.1, BC018922.2 and AC121759.9.
            
            On Apr 20, 2006 this sequence version replaced NP_005721.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF000152.1, AK226076.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398073.7/ ENSP00000381148.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..271
                     /product="carboxy-terminal domain RNA polymerase II
                     polypeptide A small phosphatase 2"
                     /EC_number="3.1.3.16"
                     /note="conserved gene amplified in osteosarcoma; nuclear
                     LIM interactor-interacting factor 2; small CTD phosphatase
                     2; NLI-interacting factor 2; protein OS-4; small
                     C-terminal domain phosphatase 2; CTD (carboxy-terminal
                     domain, RNA polymerase II, polypeptide A) small
                     phosphatase 2"
                     /calculated_mol_wt=30533
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14595.2)"
     Region          101..260
                     /region_name="HIF-SF_euk"
                     /note="Dullard-like phosphatase domain; TIGR02251"
                     /db_xref="CDD:274055"
     Site            order(107..111,115..116,162..165,169,201,217..218,
                     220..222)
                     /site_type="active"
                     /db_xref="CDD:319823"
     Site            163
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O14595.2)"
     Site            201
                     /site_type="other"
                     /note="Transition state stabilizer. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O14595.2)"
     CDS             1..271
                     /gene="CTDSP2"
                     /gene_synonym="OS4; PSR2; SCP2"
                     /coded_by="NM_005730.4:295..1110"
                     /db_xref="CCDS:CCDS41801.1"
                     /db_xref="GeneID:10106"
                     /db_xref="HGNC:HGNC:17077"
                     /db_xref="MIM:608711"
ORIGIN      
        1 mehgsiitqa rredalvltk qglvsksspk kprgrnifka lfccfraqhv gqsssstela
       61 aykeeantia ksdllqclqy qfyqipgtcl lpevteedqg ricvvidlde tlvhssfkpi
      121 nnadfivpie iegtthqvyv lkrpyvdefl rrmgelfecv lftaslakya dpvtdlldrc
      181 gvfrarlfre scvfhqgcyv kdlsrlgrdl rktlildnsp asyifhpena vpvqswfddm
      241 adtellnlip ifeelsgaed vytslgqlra p
//
LOCUS       NP_001123577             752 aa            linear   PRI 20-NOV-2025
DEFINITION  ceramide transfer protein isoform 3 [Homo sapiens].
ACCESSION   NP_001123577
VERSION     NP_001123577.1
DBSOURCE    REFSEQ: accession NM_001130105.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Horibata,Y. and Sugimoto,H.
  TITLE     The ceramide transport protein CERT is involved in
            alkylacylglycerol transfer from the ER to the Golgi for the
            biosynthesis of ether phospholipid
  JOURNAL   Arch Biochem Biophys 752, 109871 (2024)
   PUBMED   38110110
  REMARK    GeneRIF: The ceramide transport protein CERT is involved in
            alkylacylglycerol transfer from the ER to the Golgi for the
            biosynthesis of ether phospholipid.
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Gehin,C., Lone,M.A., Lee,W., Capolupo,L., Ho,S., Adeyemi,A.M.,
            Gerkes,E.H., Stegmann,A.P., Lopez-Martin,E., Bermejo-Sanchez,E.,
            Martinez-Delgado,B., Zweier,C., Kraus,C., Popp,B., Strehlow,V.,
            Grafe,D., Knerr,I., Jones,E.R., Zamuner,S., Abriata,L.A.,
            Kunnathully,V., Moeller,B.E., Vocat,A., Rommelaere,S.,
            Bocquete,J.P., Ruchti,E., Limoni,G., Van Campenhoudt,M.,
            Bourgeat,S., Henklein,P., Gilissen,C., van Bon,B.W., Pfundt,R.,
            Willemsen,M.H., Schieving,J.H., Leonardi,E., Soli,F., Murgia,A.,
            Guo,H., Zhang,Q., Xia,K., Fagerberg,C.R., Beier,C.P., Larsen,M.J.,
            Valenzuela,I., Fernandez-Alvarez,P., Xiong,S., Smigiel,R.,
            Lopez-Gonzalez,V., Armengol,L., Morleo,M., Selicorni,A.,
            Torella,A., Blyth,M., Cooper,N.S., Wilson,V., Oegema,R.,
            Herenger,Y., Garde,A., Bruel,A.L., Tran Mau-Them,F., Maddocks,A.B.,
            Bain,J.M., Bhat,M.A., Costain,G., Kannu,P., Marwaha,A.,
            Champaigne,N.L., Friez,M.J., Richardson,E.B., Gowda,V.K.,
            Srinivasan,V.M., Gupta,Y., Lim,T.Y., Sanna-Cherchi,S., Lemaitre,B.,
            Yamaji,T., Hanada,K., Burke,J.E., Jaksic,A.M., McCabe,B.D., De Los
            Rios,P., Hornemann,T., D'Angelo,G. and Gennarino,V.A.
  TITLE     CERT1 mutations perturb human development by disrupting
            sphingolipid homeostasis
  JOURNAL   J Clin Invest 133 (10), e165019 (2023)
   PUBMED   36976648
  REMARK    GeneRIF: CERT1 mutations perturb human development by disrupting
            sphingolipid homeostasis.
            Erratum:[J Clin Invest. 2025 Nov 3;135(21):e200195. doi:
            10.1172/JCI200195. PMID: 41178725]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Chung,L.H., Liu,D., Liu,X.T. and Qi,Y.
  TITLE     Ceramide Transfer Protein (CERT): An Overlooked Molecular Player in
            Cancer
  JOURNAL   Int J Mol Sci 22 (24), 13184 (2021)
   PUBMED   34947980
  REMARK    GeneRIF: Ceramide Transfer Protein (CERT): An Overlooked Molecular
            Player in Cancer.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Tamura,N., Sakai,S., Martorell,L., Colome,R., Mizuike,A., Goto,A.,
            Ortigoza-Escobar,J.D. and Hanada,K.
  TITLE     Intellectual-disability-associated mutations in the ceramide
            transport protein gene CERT1 lead to aberrant function and
            subcellular distribution
  JOURNAL   J Biol Chem 297 (5), 101338 (2021)
   PUBMED   34688657
  REMARK    GeneRIF: Intellectual-disability-associated mutations in the
            ceramide transport protein gene CERT1 lead to aberrant function and
            subcellular distribution.
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Kumagai,K., Yasuda,S., Okemoto,K., Nishijima,M., Kobayashi,S. and
            Hanada,K.
  TITLE     CERT mediates intermembrane transfer of various molecular species
            of ceramides
  JOURNAL   J Biol Chem 280 (8), 6488-6495 (2005)
   PUBMED   15596449
  REMARK    GeneRIF: results indicate that CERT can mediate transfer of various
            types of ceramides that naturally exist and their close relatives
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Hanada,K., Kumagai,K., Yasuda,S., Miura,Y., Kawano,M., Fukasawa,M.
            and Nishijima,M.
  TITLE     Molecular machinery for non-vesicular trafficking of ceramide
  JOURNAL   Nature 426 (6968), 803-809 (2003)
   PUBMED   14685229
  REMARK    GeneRIF: CERT mediates the intracellular trafficking of ceramide in
            a non-vesicular manner
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Raya,A., Revert-Ros,F., Martinez-Martinez,P., Navarro,S.,
            Rosello,E., Vieites,B., Granero,F., Forteza,J. and Saus,J.
  TITLE     Goodpasture antigen-binding protein, the kinase that phosphorylates
            the goodpasture antigen, is an alternatively spliced variant
            implicated in autoimmune pathogenesis
  JOURNAL   J Biol Chem 275 (51), 40392-40399 (2000)
   PUBMED   11007769
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Raya,A., Revert,F., Navarro,S. and Saus,J.
  TITLE     Characterization of a novel type of serine/threonine kinase that
            specifically phosphorylates the human goodpasture antigen
  JOURNAL   J Biol Chem 274 (18), 12642-12649 (1999)
   PUBMED   10212244
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Kalluri,R.
  TITLE     Goodpasture syndrome
  JOURNAL   Kidney Int 55 (3), 1120-1122 (1999)
   PUBMED   10027952
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096854.1, AK000604.1 and
            AC008897.7.
            
            Summary: This gene encodes a kinase that specifically
            phosphorylates the N-terminal region of the non-collagenous domain
            of the alpha 3 chain of type IV collagen, known as the Goodpasture
            antigen. Goodpasture disease is the result of an autoimmune
            response directed at this antigen. One isoform of this protein is
            also involved in ceramide intracellular transport. Three transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (3).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096854.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.3"
     Protein         1..752
                     /product="ceramide transfer protein isoform 3"
                     /EC_number="2.7.11.1"
                     /note="StAR-related lipid transfer (START) domain
                     containing 11; lipid-transfer protein CERTL; collagen type
                     IV alpha 3 binding protein; ceramide transfer protein;
                     collagen, type IV, alpha 3 (Goodpasture antigen) binding
                     protein"
                     /calculated_mol_wt=83577
     Region          154..253
                     /region_name="PH_GPBP"
                     /note="Goodpasture antigen binding protein Pleckstrin
                     homology (PH) domain; cd13283"
                     /db_xref="CDD:270100"
     Region          519..752
                     /region_name="START_STARD11-like"
                     /note="Ceramide-binding START domain of mammalian STARD11
                     and related domains; cd08872"
                     /db_xref="CDD:176881"
     Site            order(590,596,599..600,602..603,621,623..624,626..627,629,
                     632,634,636,658,675,677,679,707,711,713,722,725..726,
                     728..730,733)
                     /site_type="other"
                     /note="ceramide binding site [chemical binding]"
                     /db_xref="CDD:176881"
     CDS             1..752
                     /gene="CERT1"
                     /gene_synonym="CERT; CERTL; COL4A3BP; GPBP; MRD34; NEDHSF;
                     STARD11"
                     /coded_by="NM_001130105.1:138..2396"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47235.1"
                     /db_xref="GeneID:10087"
                     /db_xref="HGNC:HGNC:2205"
                     /db_xref="MIM:604677"
ORIGIN      
        1 mqhsciptpp spfsappafl pvvtresrrg lssggsagrn agvtataaaa dgwkgrlpsp
       61 lvllprsarc qarrrrggrt ssllllpptp eralfaspsp dpsprglgas sgaaegagag
      121 lllgcrasms dnqswnssgs eedpetesgp pvercgvlsk wtnyihgwqd rwvvlknnal
      181 syyksedete ygcrgsicls kavitphdfd ecrfdisvnd svwylraqdp dhrqqwidai
      241 eqhktesgyg sesslrrhgs mvslvsgasg ysatstssfk kghslrekla emetfrdilc
      301 rqvdtlqkyf dacadavskd elqrdkvved deddfpttrs dgdflhstng nkeklfphvt
      361 pkgingidfk geaitfkatt agilatlshc ielmvkreds wqkrldkete kkrrteeayk
      421 namtelkkks hfggpdyeeg pnslineeef fdaveaaldr qdkieeqsqs ekvrlhwpts
      481 lpsgdafssv gthrfvqkpy srsssmssid lvsasddvhr fssqveemvq nhmtyslqdv
      541 ggdanwqlvv eegemkvyrr eveengivld plkathavkg vtghevcnyf wnvdvrndwe
      601 ttienfhvve tladnaiiiy qthkrvwpas qrdvlylsvi rkipaltend petwivcnfs
      661 vdhdsaplnn rcvrakinva micqtlvspp egnqeisrdn ilckityvan vnpggwapas
      721 vlravakrey pkflkrftsy vqektagkpi lf
//
LOCUS       NP_001352680             263 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 1 [Homo sapiens].
ACCESSION   NP_001352680 XP_005257587
VERSION     NP_001352680.1
DBSOURCE    REFSEQ: accession NM_001365751.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5.
            
            On Sep 12, 2018 this sequence version replaced XP_005257587.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (6), as well as variant 1, encodes
            the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.241561.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..263
                     /product="MIF4G domain-containing protein isoform 1"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=29960
     Region          75..220
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..263
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001365751.1:187..978"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS58598.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkaps lectvacfet edgeysvcqr sysncsrlmp
       61 srcntqyrdp gavdlekvan vivdhslqdc vfskeagrmc yaiiqaeskq agqsvfrrgl
      121 lnrlqqeyqa reqlrarslq gwvcyvtfic nifdylrvnn mpmmalvnpv ydclfrlaqp
      181 dslskeeevd clvlqlhrvg eqlekmngqr mdelfvlird gfllptglss laqlllleii
      241 efraagwktt paahkyyyse vsd
//
LOCUS       NP_001335149             642 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform u [Homo sapiens].
ACCESSION   NP_001335149 XP_016881438
VERSION     NP_001335149.1
DBSOURCE    REFSEQ: accession NM_001348220.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP293388.1, AK301144.1 and
            AC091103.4.
            
            On Feb 8, 2017 this sequence version replaced XP_016881438.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (26) differs in the 5' UTR, lacks
            a portion of the 5' coding region, initiates translation at a
            downstream start codon, and uses two alternate in-frame splice
            sites compared to variant 3. The resulting isoform (u) is shorter
            at the N-terminus and lacks several internal amino acids compared
            to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.79274.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..642
                     /product="transcription factor 4 isoform u"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68352
     Region          533..617
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(541,545,547..549,551,556,577..578)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(554..555,558..559,561..562,565,569,579,582,586,589,
                     592..597)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..642
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348220.1:310..2238"
                     /note="isoform u is encoded by transcript variant 26"
                     /db_xref="CCDS:CCDS86672.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqs llggdmdmgn pgtlsptkpg
      121 sqyyqyssnn prrrplhssa mevqtkkvrk vppglpssvy apsastadyn rdspgypssk
      181 patstfpssf fmqdghhssd pwssssgmnq pgyagmlgns shipqsssyc slhpherlsy
      241 pshssadins slppmstfhr sgtnhystss ctppangtds imanrgsgaa gssqtgdalg
      301 kalasiyspd htnnsfssnp stpvgsppsl sagtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit snnddedltp eqkaereker
      541 rmannarerl rvrdineafk elgrmvqlhl ksdkpqtkll ilhqavavil sleqqvrern
      601 lnpkaaclkr reeekvssep pplslagphp gmgdasnhmg qm
//
LOCUS       NP_079384                433 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin epsilon and delta complex protein 2 [Homo sapiens].
ACCESSION   NP_079384
VERSION     NP_079384.2
DBSOURCE    REFSEQ: accession NM_025108.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Li,Y., Guo,B., Wang,L., Zhou,F., Yu,Z., Huang,Y., Chen,R.,
            Zhang,M., Zhang,K., Zheng,L., Jing,S., Hong,W. and Han,T.
  TITLE     TEDC2 plays an oncogenic role and serves as a therapeutic target of
            hepatocellular carcinoma
  JOURNAL   Dig Liver Dis 56 (5), 861-871 (2024)
   PUBMED   37867019
  REMARK    GeneRIF: TEDC2 plays an oncogenic role and serves as a therapeutic
            target of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Liu,Y., Zhu,J., Shen,J., Lu,Y., Pan,K., Tong,C. and Wang,Y.
  TITLE     A pan-cancer analysis of the prognostic implication and oncogenic
            role of tubulin epsilon and delta complex 2 (TEDC2) in human tumors
  JOURNAL   Front Immunol 14, 1272108 (2024)
   PUBMED   38239349
  REMARK    GeneRIF: A pan-cancer analysis of the prognostic implication and
            oncogenic role of tubulin epsilon and delta complex 2 (TEDC2) in
            human tumors.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Fang,L., Yu,W., Zhu,P., Yu,G. and Ye,B.
  TITLE     TEDC2 correlated with prognosis and immune microenvironment in lung
            adenocarcinoma
  JOURNAL   Sci Rep 13 (1), 5006 (2023)
   PUBMED   36973475
  REMARK    GeneRIF: TEDC2 correlated with prognosis and immune
            microenvironment in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Breslow,D.K., Hoogendoorn,S., Kopp,A.R., Morgens,D.W., Vu,B.K.,
            Kennedy,M.C., Han,K., Li,A., Hess,G.T., Bassik,M.C., Chen,J.K. and
            Nachury,M.V.
  TITLE     A CRISPR-based screen for Hedgehog signaling provides insights into
            ciliary function and ciliopathies
  JOURNAL   Nat Genet 50 (3), 460-471 (2018)
   PUBMED   29459677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC106820.4, AL559561.3 and BC018719.1.
            
            On Jan 9, 2006 this sequence version replaced NP_079384.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018719.1, AK301929.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361837.9/ ENSP00000355022.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..433
                     /product="tubulin epsilon and delta complex protein 2"
                     /note="uncharacterized protein C16orf59"
                     /calculated_mol_wt=46271
     Region          45..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L2K0.1)"
     Region          95..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L2K0.1)"
     Region          148..431
                     /region_name="DUF4693"
                     /note="Domain of unknown function (DUF4693); pfam15764"
                     /db_xref="CDD:464854"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2K0.1)"
     Region          326..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L2K0.1)"
     CDS             1..433
                     /gene="TEDC2"
                     /gene_synonym="C16orf59"
                     /coded_by="NM_025108.3:37..1338"
                     /db_xref="CCDS:CCDS10468.2"
                     /db_xref="GeneID:80178"
                     /db_xref="HGNC:HGNC:25849"
ORIGIN      
        1 mlpagcsrrl vaelqgalda caqrqlqleq slrvcrrllh aweptgtral kpppgpetng
       61 edplpactps pqdlkelefl tqalekavrv rrgitkager dkapslksrs ivtssgttas
      121 apphspgqag ghasdtrptk glrqttvpak ghperrllsv gdgtrvgmga rtprpgaglr
      181 dqqmapsaap qapeaftlke kghllrlpaa frkaasqnss lwaqlsstqt sdstdaaaak
      241 tqflqnmqta sggpqprlsa veveaeagrl rkacsllrlr mreelsaapm dwmqeyrcll
      301 tleglqamvg qclhrlqelr aavaeqpprp cpvgrppgas pscggraepa wspqllvyss
      361 tqelqtlaal klrvavldqq ihlekvlmae llplvsaaqp qgppwlalcr avhsllcegg
      421 arvltilrde pav
//
LOCUS       NP_001027005            1086 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit beta isoform b [Homo
            sapiens].
ACCESSION   NP_001027005
VERSION     NP_001027005.1
DBSOURCE    REFSEQ: accession NM_001031835.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Yang,W., Zhang,C., Li,Y., Jin,A., Sun,Y., Yang,X., Wang,B. and
            Guo,W.
  TITLE     Phosphorylase Kinase beta Represents a Novel Prognostic Biomarker
            and Inhibits Malignant Phenotypes of Liver Cancer Cell
  JOURNAL   Int J Biol Sci 15 (12), 2596-2606 (2019)
   PUBMED   31754332
  REMARK    GeneRIF: PHKB acts as a novel prognostic indicator for HCC, which
            exerts its suppression function via inactivating AKT and STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1086)
  AUTHORS   Wang,G., Shen,W., Liu,C.Y., Liu,Y., Wu,T., Cui,X., Yu,T., Zhu,Y.,
            Song,J., Du,P. and Cui,L.
  TITLE     Phosphorylase kinase beta affects colorectal cancer cell growth and
            represents a novel prognostic biomarker
  JOURNAL   J Cancer Res Clin Oncol 143 (6), 971-980 (2017)
   PUBMED   28275865
  REMARK    GeneRIF: PHKb affects colorectal cancer cell growth and represents
            a novel prognostic biomarker.
REFERENCE   5  (residues 1 to 1086)
  AUTHORS   Terashima,M., Fujita,Y., Togashi,Y., Sakai,K., De Velasco,M.A.,
            Tomida,S. and Nishio,K.
  TITLE     KIAA1199 interacts with glycogen phosphorylase kinase beta-subunit
            (PHKB) to promote glycogen breakdown and cancer cell survival
  JOURNAL   Oncotarget 5 (16), 7040-7050 (2014)
   PUBMED   25051373
  REMARK    GeneRIF: Analysis showed that the glycogen phosphorylase kinase
            beta-subunit (PHKB) interacted with the C-terminal region of
            KIAA1199 protein.
REFERENCE   6  (residues 1 to 1086)
  AUTHORS   van den Berg,I.E., van Beurden,E.A., de Klerk,J.B., van
            Diggelen,O.P., Malingre,H.E., Boer,M.M. and Berger,R.
  TITLE     Autosomal recessive phosphorylase kinase deficiency in liver,
            caused by mutations in the gene encoding the beta subunit (PHKB)
  JOURNAL   Am J Hum Genet 61 (3), 539-546 (1997)
   PUBMED   9326319
REFERENCE   7  (residues 1 to 1086)
  AUTHORS   Burwinkel,B., Maichele,A.J., Aagenaes,O., Bakker,H.D., Lerner,A.,
            Shin,Y.S., Strachan,J.A. and Kilimann,M.W.
  TITLE     Autosomal glycogenosis of liver and muscle due to phosphorylase
            kinase deficiency is caused by mutations in the phosphorylase
            kinase beta subunit (PHKB)
  JOURNAL   Hum Mol Genet 6 (7), 1109-1115 (1997)
   PUBMED   9215682
REFERENCE   8  (residues 1 to 1086)
  AUTHORS   Wullrich-Schmoll,A. and Kilimann,M.W.
  TITLE     Structure of the human gene encoding the phosphorylase kinase beta
            subunit (PHKB)
  JOURNAL   Eur J Biochem 238 (2), 374-380 (1996)
   PUBMED   8681948
REFERENCE   9  (residues 1 to 1086)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   10 (residues 1 to 1086)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC033657.1, AC007599.6 and
            AC092374.4.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, encoded by two different
            genes. The beta subunit is the same in both the muscle and hepatic
            isoforms, encoded by this gene, which is a member of the
            phosphorylase b kinase regulatory subunit family. The gamma subunit
            also includes the skeletal muscle and hepatic isoforms, encoded by
            two different genes. The delta subunit is a calmodulin and can be
            encoded by three different genes. The gamma subunits contain the
            active site of the enzyme, whereas the alpha and beta subunits have
            regulatory functions controlled by phosphorylation. The delta
            subunit mediates the dependence of the enzyme on calcium
            concentration. Mutations in this gene cause glycogen storage
            disease type 9B, also known as phosphorylase kinase deficiency of
            liver and muscle. Alternatively spliced transcript variants
            encoding different isoforms have been identified in this gene. Two
            pseudogenes have been found on chromosomes 14 and 20,
            respectively.[provided by RefSeq, Feb 2010].
            
            Transcript Variant: This variant (2) has an additional exon in the
            5' region and an alternate exon in the 3' region, as compared to
            variant 1. The resulting isoform (b) is shorter and has an
            alternate N-terminus and a different segment in the C-terminal
            region, as compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.109578.1,
                                           SRR1660807.110902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..1086
                     /product="phosphorylase b kinase regulatory subunit beta
                     isoform b"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase b kinase regulatory subunit beta;
                     phosphorylase kinase beta-subunit; phosphorylase kinase
                     subunit beta; phosphorylase kinase, beta"
                     /calculated_mol_wt=123694
     Region          42..>463
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          <744..871
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          891..1070
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     CDS             1..1086
                     /gene="PHKB"
                     /coded_by="NM_001031835.3:154..3414"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42161.1"
                     /db_xref="GeneID:5257"
                     /db_xref="HGNC:HGNC:8927"
                     /db_xref="MIM:172490"
ORIGIN      
        1 macspdavvs pssaflrsgs vyeplksinl prpdnetlwd kldhyyrivk stlllyqspt
       61 tglfptktcg gdqkakiqds lycaagawal alayrriddd kgrthelehs aikcmrgily
      121 cymrqadkvq qfkqdprptt clhsvfnvht gdellsyeey ghlqinavsl yllylvemis
      181 sglqiiyntd evsfiqnlvf cvervyrvpd fgvwergsky nngstelhss svglakaale
      241 aingfnlfgn qgcswsvifv dldahnrnrq tlcsllpres rshntdaall pcisypafal
      301 ddevlfsqtl dkvvrklkgk ygfkrflrdg yrtsledpnr cyykpaeikl fdgiecefpi
      361 fflymmidgv frgnpkqvqe yqdlltpvlh httegypvvp kyyyvpadfv eyeknnpgsq
      421 krfpsncgrd gklflwgqal yiiakllade lispkdidpv qryvplkdqr nvsmrfsnqg
      481 plendlvvhv aliaesqrlq vflntygiqt qtpqqvepiq iwpqqelvka ylqlginekl
      541 glsgrpdrpi gclgtskiyr ilgktvvcyp iifdlsdfym sqdvfllidd iknalqfikq
      601 ywkmhgrplf lvlirednir gsrfnpildm laalkkgiig gvkvhvdrlq tlisgavveq
      661 ldflrisdte elpefksfee leppkhskvk rqsstpsape lgqqpdvnis ewkdkpthei
      721 lqklndcscl asqaillgil lkregpnfit kegtvsdhie rvyrragsqk lwsvvrraas
      781 llskvvdsla psitnvlvqg kqvtlgafgh eeevisnpls prviqniiyy kcnthderea
      841 viqqelvihi gwiisnnpel fsgmlkirig wiihameyel qirggdkpal dlyqlspsev
      901 kqllldilqp qqngrcwlnr rqidgslnrt ptgfydrvwq ilertpngii vagkhlpqqp
      961 tlsdmtmyem nfsllvedtl gnidqpqyrq ivvellmvvs ivlernpele fqdkvdldrl
     1021 vkeafnefqk dqsrlkeiek qddmtsfynt pplgkrgtcs yltkavmnll legevkpnnd
     1081 dpclis
//
LOCUS       NP_037535                753 aa            linear   PRI 20-NOV-2025
DEFINITION  striatin-4 isoform 1 [Homo sapiens].
ACCESSION   NP_037535
VERSION     NP_037535.2
DBSOURCE    REFSEQ: accession NM_013403.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Czauderna,C., Poplawski,A., O'Rourke,C.J., Castven,D.,
            Perez-Aguilar,B., Becker,D., Heilmann-Heimbach,S., Odenthal,M.,
            Amer,W., Schmiel,M., Drebber,U., Binder,H., Ridder,D.A.,
            Schindeldecker,M., Straub,B.K., Galle,P.R., Andersen,J.B.,
            Thorgeirsson,S.S., Park,Y.N. and Marquardt,J.U.
  TITLE     Epigenetic modifications precede molecular alterations and drive
            human hepatocarcinogenesis
  JOURNAL   JCI Insight 6 (17), e146196 (2021)
   PUBMED   34375307
  REMARK    GeneRIF: Epigenetic modifications precede molecular alterations and
            drive human hepatocarcinogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Jeong,B.C., Bae,S.J., Ni,L., Zhang,X., Bai,X.C. and Luo,X.
  TITLE     Cryo-EM structure of the Hippo signaling integrator human STRIPAK
  JOURNAL   Nat Struct Mol Biol 28 (3), 290-299 (2021)
   PUBMED   33633399
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Di Bernardo,M.C., Crowther-Swanepoel,D., Broderick,P., Webb,E.,
            Sellick,G., Wild,R., Sullivan,K., Vijayakrishnan,J., Wang,Y.,
            Pittman,A.M., Sunter,N.J., Hall,A.G., Dyer,M.J., Matutes,E.,
            Dearden,C., Mainou-Fowler,T., Jackson,G.H., Summerfield,G.,
            Harris,R.J., Pettitt,A.R., Hillmen,P., Allsup,D.J., Bailey,J.R.,
            Pratt,G., Pepper,C., Fegan,C., Allan,J.M., Catovsky,D. and
            Houlston,R.S.
  TITLE     A genome-wide association study identifies six susceptibility loci
            for chronic lymphocytic leukemia
  JOURNAL   Nat Genet 40 (10), 1204-1210 (2008)
   PUBMED   18758461
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA510367.1, AF212940.1 and BC034604.1.
            
            On Mar 16, 2006 this sequence version replaced NP_037535.1.
            
            Transcript Variant: This variant (1) uses an alternate splice site
            in the central coding region, compared to variant 2. The resulting
            isoform (1) lacks an internal 7-aa segment, compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF212940.1, BC034604.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263280.11/ ENSP00000263280.4
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..753
                     /product="striatin-4 isoform 1"
                     /note="striatin, calmodulin binding protein 4; protein
                     phosphatase 2 regulatory subunit B'''gamma"
                     /calculated_mol_wt=80465
     Region          10..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          65..189
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          71..79
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          165..182
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          213..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          271..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          363..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          430..752
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          436..475
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            order(437,455,459,465..466,489..490,508,512,518..519,
                     542..543,560,565,571..572,587,608,613,618..619,633..634,
                     654,658,664..665,677..678,695,700,706..707,719,724,742,
                     746,752)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          443..489
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          489..528
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          495..542
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          542..581
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          547..586
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          587..628
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          594..630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          635..674
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          640..676
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          677..716
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          682..721
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          723..753
                     /region_name="WD 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          728..752
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..753
                     /gene="STRN4"
                     /gene_synonym="PPP2R6C; ZIN; zinedin"
                     /coded_by="NM_013403.3:21..2282"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12690.1"
                     /db_xref="GeneID:29888"
                     /db_xref="HGNC:HGNC:15721"
                     /db_xref="MIM:614767"
ORIGIN      
        1 mmeeraaaav aaaasscrpl gsgagpgptg aapvsapapg pgpagkgggg ggspgptagp
       61 eplslpgilh fiqhewarfe aekarweaer aelqaqvafl qgerkgqenl ktdlvrrikm
      121 leyalkqera kyhklkfgtd lnqgekkadv seqvsngpve svtlensplv wkegrqllrq
      181 yleevgytdt ildmrskrvr sllgrsleln gavepsegap rappgpagls ggesllvkqi
      241 eeqikrnaag kdgkerlggs vlgqipflqn cededsdedd eldsvqhkkq rvklpskalv
      301 pemededeed dsedainefd flgsgedgeg apdprrctvd gsphelesrr vklqgiladl
      361 rdvdglppkv tgpppgtpqp rphedvfimd tigggevslg dladltvtnd ndlscdlsds
      421 kdafkktwnp kftlrshydg irslafhhsq salltasedg tlklwnlqka vtakknaald
      481 vepihafrah rgpvlavamg snseycysgg adacihswki pdlsmdpydg ydpsvlshvl
      541 eghgdavwgl afsptsqrla scsadgtvri wdpsssspac lctfptaseh gvptsvafts
      601 tepahivasf rsgdtvlydm evgsalltle srgssgptqi nqvvshpnqp ltitahddrg
      661 irfldnrtgk pvhsmvahld avtclavdpn gaflmsgshd cslrlwsldn ktcvqeitah
      721 rkkheeaiha vachpskali asagadalak vfv
//
LOCUS       NP_001306093             249 aa            linear   PRI 20-NOV-2025
DEFINITION  BPI fold-containing family A member 2 precursor [Homo sapiens].
ACCESSION   NP_001306093 XP_005260338
VERSION     NP_001306093.1
DBSOURCE    REFSEQ: accession NM_001319164.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Kota,S.K., Pernicone,E., Leaf,D.E., Stillman,I.E., Waikar,S.S. and
            Kota,S.B.
  TITLE     BPI Fold-Containing Family A Member 2/Parotid Secretory Protein Is
            an Early Biomarker of AKI
  JOURNAL   J Am Soc Nephrol 28 (12), 3473-3478 (2017)
   PUBMED   28775000
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Prokopovic,V., Popovic,M., Andjelkovic,U., Marsavelski,A.,
            Raskovic,B., Gavrovic-Jankulovic,M. and Polovic,N.
  TITLE     Isolation, biochemical characterization and anti-bacterial activity
            of BPIFA2 protein
  JOURNAL   Arch Oral Biol 59 (3), 302-309 (2014)
   PUBMED   24581853
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Zeng,Z., Feingold,E., Wang,X., Weeks,D.E., Lee,M., Cuenco,D.T.,
            Broffitt,B., Weyant,R.J., Crout,R., McNeil,D.W., Levy,S.M.,
            Marazita,M.L. and Shaffer,J.R.
  TITLE     Genome-wide association study of primary dentition pit-and-fissure
            and smooth surface caries
  JOURNAL   Caries Res 48 (4), 330-338 (2014)
   PUBMED   24556642
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Bingle,L., Barnes,F.A., Lunn,H., Musa,M., Webster,S., Douglas,C.W.,
            Cross,S.S., High,A.S. and Bingle,C.D.
  TITLE     Characterisation and expression of SPLUNC2, the human orthologue of
            rodent parotid secretory protein
  JOURNAL   Histochem Cell Biol 132 (3), 339-349 (2009)
   PUBMED   19499239
  REMARK    GeneRIF: multiple SPLUNC2 isoforms are found in the oral cavity and
            suggest that these proteins may be differentially regulated in
            distinct tissues where they may function in the innate immune
            response.
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Ramachandran,P., Boontheung,P., Xie,Y., Sondej,M., Wong,D.T. and
            Loo,J.A.
  TITLE     Identification of N-linked glycoproteins in human saliva by
            glycoprotein capture and mass spectrometry
  JOURNAL   J Proteome Res 5 (6), 1493-1503 (2006)
   PUBMED   16740002
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Bingle,C.D., LeClair,E.E., Havard,S., Bingle,L., Gillingham,P. and
            Craven,C.J.
  TITLE     Phylogenetic and evolutionary analysis of the PLUNC gene family
  JOURNAL   Protein Sci 13 (2), 422-430 (2004)
   PUBMED   14739326
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Bingle,C.D. and Craven,C.J.
  TITLE     PLUNC: a novel family of candidate host defence proteins expressed
            in the upper airways and nasopharynx
  JOURNAL   Hum Mol Genet 11 (8), 937-943 (2002)
   PUBMED   11971875
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121901.20 and AY359055.1.
            
            On Jan 28, 2016 this sequence version replaced XP_005260338.1.
            
            Summary: This gene encodes a member of the palate, lung and nasal
            epithelium clone (Plunc) family of proteins. Members of this family
            have been proposed to play a role in the local antibacterial
            response in nose, mouth and upper respiratory pathways. The encoded
            soluble salivary protein binds bacterial lipopolysaccharide (LPS)
            and inhibits bacterial growth. This gene is present in a gene
            cluster on chromosome 20. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY359055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2150585
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..249
                     /product="BPI fold-containing family A member 2 precursor"
                     /note="short palate, lung and nasal epithelium
                     carcinoma-associated protein 2; parotid secretory protein"
                     /calculated_mol_wt=24925
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2105
     mat_peptide     19..249
                     /product="BPI fold-containing family A member 2.
                     /id=PRO_0000017184"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DR5.2)"
                     /calculated_mol_wt=25054
     Region          62..227
                     /region_name="LBP_BPI_CETP"
                     /note="LBP / BPI / CETP family, N-terminal domain;
                     pfam01273"
                     /db_xref="CDD:396022"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q96DR5.2)"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (Q96DR5.2)"
     CDS             1..249
                     /gene="BPIFA2"
                     /gene_synonym="bA49G10.1; C20orf70; PSP; SPLUNC2"
                     /coded_by="NM_001319164.2:145..894"
                     /db_xref="CCDS:CCDS13214.1"
                     /db_xref="GeneID:140683"
                     /db_xref="HGNC:HGNC:16203"
                     /db_xref="MIM:621166"
ORIGIN      
        1 mlqlwklvll cgvltgtses lldnlgndls nvvdklepvl hegletvdnt lkgileklkv
       61 dlgvlqkssa wqlakqkaqe aekllnnvis kllptntdif glkisnslil dvkaepiddg
      121 kglnlsfpvt anvtvagpii gqiinlkasl dlltavtiet dpqthqpvav lgecasdpts
      181 islslldkhs qiinkfvnsv intlkstvss llqkeicpli rifihsldvn viqqvvdnpq
      241 hktqlqtli
//
LOCUS       NP_001011718             579 aa            linear   PRI 20-NOV-2025
DEFINITION  XK-related protein 7 [Homo sapiens].
ACCESSION   NP_001011718 XP_293160
VERSION     NP_001011718.1
DBSOURCE    REFSEQ: accession NM_001011718.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY534245.1 and AL031658.11.
            
            On Feb 9, 2005 this sequence version replaced XP_293160.4.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY534245.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465404 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000562532.3/ ENSP00000477059.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..579
                     /product="XK-related protein 7"
                     /note="X Kell blood group precursor-related family, member
                     7; XK, Kell blood group complex subunit-related family,
                     member 7; X-linked Kx blood group related 7"
                     /calculated_mol_wt=63695
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Region          59..441
                     /region_name="XK-related"
                     /note="XK-related protein; pfam09815"
                     /db_xref="CDD:462912"
     Site            59..79
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Region          <117..172
                     /region_name="KLF9_13_N-like"
                     /note="Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16,
                     and similar proteins; cl41730"
                     /db_xref="CDD:425361"
     Region          146..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            384..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     Region          466..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5GH72.1)"
     CDS             1..579
                     /gene="XKR7"
                     /gene_synonym="C20orf159; dJ310O13.4"
                     /coded_by="NM_001011718.2:26..1765"
                     /db_xref="CCDS:CCDS33459.1"
                     /db_xref="GeneID:343702"
                     /db_xref="HGNC:HGNC:23062"
ORIGIN      
        1 maaksdgaaa saspdpegaa ggargsaggr geaaaaagpp gvvgaggpgp ryelrdccwv
       61 lcallvffsd gatdlwlaas yylqnqhtyf sltllfvllp slvvqllsfr wfvydysepa
      121 gspgpavstk dsvaggaais tkdsagafrt kegspepgpq papssasayr rrccrlciwl
      181 lqtlvhllql gqvwrylral ylglqsrwrg erlrrhfywq mlfesadvsm lrlletflrs
      241 apqlvlqlsl lvhrggapdl lpalstsasl vslawtlasy qkvlrdsrdd krplsykgav
      301 aqvlwhlfsi aarglafalf asvyklyfgi fivahwcvmt fwviqgetdf cmskweeiiy
      361 nmvvgiiyif cwfnvkegrs rrrmtlyhci vllenaaltg fwyssrnfst dfyslimvcv
      421 vassfalgif fmcvyycllh pngpmlgpqa pgcifrkase pcgppadait spprslprtt
      481 gaerdgasag eragtptppv fqvrpglppt pvartlrteg pviridlprk kypawdahfi
      541 drrlrktila leysspatpr lqyrsvgtsq elleyettv
//
LOCUS       NP_001026909             294 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SOCS box protein 9 isoform 1 [Homo sapiens].
ACCESSION   NP_001026909
VERSION     NP_001026909.1
DBSOURCE    REFSEQ: accession NM_001031739.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Li,N., Zhou,Q., Yi,Z., Zhang,H. and Zhou,D.
  TITLE     Ubiquitin protein E3 ligase ASB9 suppresses proliferation and
            promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation
  JOURNAL   Biol Res 56 (1), 4 (2023)
   PUBMED   36683111
  REMARK    GeneRIF: Ubiquitin protein E3 ligase ASB9 suppresses proliferation
            and promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Lumpkin,R.J., Ahmad,A.S., Blake,R., Condon,C.J. and Komives,E.A.
  TITLE     The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases
  JOURNAL   Mol Cell Proteomics 20, 100019 (2021)
   PUBMED   33268465
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Fei,X., Zhang,Y., Gu,X., Qiu,R., Mao,Y. and Ji,C.
  TITLE     Crystallization and preliminary X-ray analysis of the splice
            variant of human ankyrin repeat and suppressor of cytokine
            signaling box protein 9 (hASB9-2)
  JOURNAL   Protein Pept Lett 15 (6), 647-649 (2008)
   PUBMED   18680464
  REMARK    GeneRIF: The splice variant of hASB9, hASB9-2 protein, was cloned,
            overexpressed, and crystallized and the data showed that the cubic
            hASB9-2 crystal belongs to space group P4(3)32 with unit-cell
            parameters.
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Debrincat,M.A., Zhang,J.G., Willson,T.A., Silke,J., Connolly,L.M.,
            Simpson,R.J., Alexander,W.S., Nicola,N.A., Kile,B.T. and
            Hilton,D.J.
  TITLE     Ankyrin repeat and suppressors of cytokine signaling box protein
            asb-9 targets creatine kinase B for degradation
  JOURNAL   J Biol Chem 282 (7), 4728-4737 (2007)
   PUBMED   17148442
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Kohroki,J., Nishiyama,T., Nakamura,T. and Masuho,Y.
  TITLE     ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin
            ligase complexes
  JOURNAL   FEBS Lett 579 (30), 6796-6802 (2005)
   PUBMED   16325183
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA943920.1, BC013172.1 and
            BC001244.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the ankyrin repeat and
            suppressor of cytokine signaling (SOCS) box protein family. Members
            of this family can interact with the elongin B-C adapter complex
            via their SOCS box domain and further complex with the cullin and
            ring box proteins to form E3 ubiquitin ligase complexes. They may
            function to mediate the substrate-recognition of the E3 ubiquitin
            ligases. A transcribed pseudogene of this gene has been identified
            on chromosome 15. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Dec
            2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013172.1, SRR5189658.107568.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380488.9/ ENSP00000369855.4
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..294
                     /product="ankyrin repeat and SOCS box protein 9 isoform 1"
                     /note="ankyrin repeat and SOCS box protein 9; ankyrin
                     repeat and suppressor of cytokine signaling box protein 9;
                     ASB-9; testis tissue sperm-binding protein Li 57p"
                     /calculated_mol_wt=31727
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          22..253
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(35,37,41..42,45..47,49..50,54,57,66,68,70,74..75,
                     78..80,82..83,87,90,99,101,103,107..108,111..113,115..116,
                     120,123)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          35..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          35..64
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          68..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          68..97
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          101..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          101..130
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Site            103
                     /site_type="other"
                     /note="Essential for binding to CKB.
                     /evidence=ECO:0000269|PubMed:22418839; propagated from
                     UniProtKB/Swiss-Prot (Q96DX5.1)"
     Site            107
                     /site_type="other"
                     /note="Essential for binding to CKB.
                     /evidence=ECO:0000269|PubMed:22418839; propagated from
                     UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          133..162
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          136..164
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(139..140,143..145,147..148,152,155,164,166,168,
                     172..173,176..178,180..181,185,188,196,198,200,204..205,
                     208..210,212..213,217,220,229)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          166..196
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          166..195
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          198..229
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          198..227
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DX5.1)"
     Region          253..294
                     /region_name="SOCS_ASB_9_11"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB9 and 11 proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. The
                     general function of the SOCS box is the recruitment of the
                     ubiquitin-transferase system; cd03728"
                     /db_xref="CDD:239698"
     Site            order(254..259,265,275,281,286)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239698"
     CDS             1..294
                     /gene="ASB9"
                     /coded_by="NM_001031739.3:210..1094"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35208.1"
                     /db_xref="GeneID:140462"
                     /db_xref="HGNC:HGNC:17184"
                     /db_xref="MIM:300890"
ORIGIN      
        1 mdgkqggmdg skpagprdfp girllsnplm gdavsdwspm heaaihghql slrnlisqgw
       61 avniitadhv splheaclgg hlscvkillk hgaqvngvta dwhtplfnac vsgswdcvnl
      121 llqhgasvqp esdlaspihe aarrghvecv nsliayggni dhkishlgtp lylacenqqr
      181 acvkkllesg advnqgkgqd splhavarta seelacllmd fgadtqakna egkrpvelvp
      241 pesplaqlfl eregppslmq lcrlrirkcf giqqhhkitk lvlpedlkqf llhl
//
LOCUS       NP_001258780             365 aa            linear   PRI 20-NOV-2025
DEFINITION  ras-related GTP-binding protein C isoform 2 [Homo sapiens].
ACCESSION   NP_001258780
VERSION     NP_001258780.1
DBSOURCE    REFSEQ: accession NM_001271851.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 365)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 365)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 365)
  AUTHORS   Reijnders,M.R.F., Seibt,A., Brugger,M., Lamers,I.J.C., Ott,T.,
            Klaas,O., Horvath,J., Rose,A.M.S., Craghill,I.M., Brunet,T.,
            Graf,E., Mayerhanser,K., Hellebrekers,D., Pauck,D., Neuen-Jacob,E.,
            Rodenburg,R.J.T., Wieczorek,D., Klee,D., Mayatepek,E., Driessen,G.,
            Bindermann,R., Averdunk,L., Lohmeier,K., Sinnema,M.,
            Stegmann,A.P.A., Roepman,R., Poulter,J.A. and Distelmaier,F.
  TITLE     De novo missense variants in RRAGC lead to a fatal mTORopathy of
            early childhood
  JOURNAL   Genet Med 25 (7), 100838 (2023)
   PUBMED   37057673
  REMARK    GeneRIF: De novo missense variants in RRAGC lead to a fatal
            mTORopathy of early childhood.
REFERENCE   4  (residues 1 to 365)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 365)
  AUTHORS   Cui,Z., Napolitano,G., de Araujo,M.E.G., Esposito,A.,
            Monfregola,J., Huber,L.A., Ballabio,A. and Hurley,J.H.
  TITLE     Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex
  JOURNAL   Nature 614 (7948), 572-579 (2023)
   PUBMED   36697823
  REMARK    GeneRIF: Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator
            megacomplex.
REFERENCE   6  (residues 1 to 365)
  AUTHORS   Sekiguchi,T., Todaka,Y., Wang,Y., Hirose,E., Nakashima,N. and
            Nishimoto,T.
  TITLE     A novel human nucleolar protein, Nop132, binds to the G proteins,
            RRAG A/C/D
  JOURNAL   J Biol Chem 279 (9), 8343-8350 (2004)
   PUBMED   14660641
REFERENCE   7  (residues 1 to 365)
  AUTHORS   Park,I.H., Bachmann,R., Shirazi,H. and Chen,J.
  TITLE     Regulation of ribosomal S6 kinase 2 by mammalian target of
            rapamycin
  JOURNAL   J Biol Chem 277 (35), 31423-31429 (2002)
   PUBMED   12087098
REFERENCE   8  (residues 1 to 365)
  AUTHORS   Sekiguchi,T., Hirose,E., Nakashima,N., Ii,M. and Nishimoto,T.
  TITLE     Novel G proteins, Rag C and Rag D, interact with GTP-binding
            proteins, Rag A and Rag B
  JOURNAL   J Biol Chem 276 (10), 7246-7257 (2001)
   PUBMED   11073942
REFERENCE   9  (residues 1 to 365)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   10 (residues 1 to 365)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI461665.1, ES308561.1,
            AK298788.1, BC016668.1, AW327252.1, AK298573.1, CX761032.1,
            CB132041.1, HY264464.1, HY202961.1 and BQ003663.1.
            
            Summary: This gene encodes a member of the GTR/RAG GTP-binding
            protein family. The encoded protein is a monomeric guanine
            nucleotide-binding protein which forms a heterodimer with RRAGA and
            RRAGB and is primarily localized to the cytoplasm. The encoded
            protein promotes intracellular localization of the mTOR complex.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region, compared to variant 1. It encodes
            isoform 2 which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..365
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..365
                     /product="ras-related GTP-binding protein C isoform 2"
                     /note="Rag C protein; ras-related GTP-binding protein C;
                     GTPase-interacting protein 2"
                     /calculated_mol_wt=40131
     Region          63..255
                     /region_name="Gtr1_RagA"
                     /note="Gtr1/RagA G protein conserved region; pfam04670"
                     /db_xref="CDD:398377"
     Site            68..75
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206745"
     Site            order(73..76,85,144..145,147,185..187)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206745"
     Site            82..85
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206745"
     Site            order(84..85,104..105)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206745"
     Site            144..147
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206745"
     Site            185..187
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206745"
     CDS             1..365
                     /gene="RRAGC"
                     /gene_synonym="GTR2; LNGODS; LNGOS; RAGC; TIB929"
                     /coded_by="NM_001271851.2:127..1224"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:64121"
                     /db_xref="HGNC:HGNC:19902"
                     /db_xref="MIM:608267"
ORIGIN      
        1 mslqygaeet plagsygaad sfpkdfgygv eeeeeeaaaa gggvgagagg gcgpggadss
       61 kprillmglr rsgkssiqki wdfpgqmdff dptfdyemif rgtgaliyvi daqddymeal
      121 trlhitvska ykvnpdmnfe vfihkvdgls ddhkietqrd ihqranddla dagleklhls
      181 fyltsiydhs ifeafskvvq klipqlptle nllnifisns giekaflfdv vskiyiatds
      241 spvdmqsyel ccdmidvvid vsciyglked gsgsaydkes maiiklnntt vlylkevtkf
      301 lalvcilree sferkglidy nfhcfrkaih evfevgvtsh rscghqtsas slkalthngt
      361 prnai
//
LOCUS       NP_859066                693 aa            linear   PRI 20-NOV-2025
DEFINITION  CREB-regulated transcription coactivator 2 [Homo sapiens].
ACCESSION   NP_859066
VERSION     NP_859066.1
DBSOURCE    REFSEQ: accession NM_181715.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Carper,M.B., Goel,S., Zhang,A.M., Damrauer,J.S., Cohen,S.,
            Zimmerman,M.P., Gentile,G.M., Parag-Sharma,K., Murphy,R.M.,
            Sato,K., Nickel,K.P., Kimple,R.J., Yarbrough,W.G. and Amelio,A.L.
  TITLE     Activation of the CREB Coactivator CRTC2 by Aberrant Mitogen
            Signaling promotes oncogenic functions in HPV16 positive head and
            neck cancer
  JOURNAL   Neoplasia 29, 100799 (2022)
   PUBMED   35504112
  REMARK    GeneRIF: Activation of the CREB Coactivator CRTC2 by Aberrant
            Mitogen Signaling promotes oncogenic functions in HPV16 positive
            head and neck cancer.
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Wu,Z., Huang,X., Feng,Y., Handschin,C., Feng,Y., Gullicksen,P.S.,
            Bare,O., Labow,M., Spiegelman,B. and Stevenson,S.C.
  TITLE     Transducer of regulated CREB-binding proteins (TORCs) induce
            PGC-1alpha transcription and mitochondrial biogenesis in muscle
            cells
  JOURNAL   Proc Natl Acad Sci U S A 103 (39), 14379-14384 (2006)
   PUBMED   16980408
  REMARK    GeneRIF: These results strongly suggest that TORCs play a key role
            in linking these external signals to the transcriptional program of
            adaptive mitochondrial biogenesis by activating PGC-1alpha gene
            transcription.
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Siu,Y.T., Chin,K.T., Siu,K.L., Yee Wai Choy,E., Jeang,K.T. and
            Jin,D.Y.
  TITLE     TORC1 and TORC2 coactivators are required for tax activation of the
            human T-cell leukemia virus type 1 long terminal repeats
  JOURNAL   J Virol 80 (14), 7052-7059 (2006)
   PUBMED   16809310
  REMARK    GeneRIF: Thus, both TORC1/2 and p300 families of coactivators are
            essential for optimal activation of HTLV-1 transcription by Tax.
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Al-Hakim,A.K., Goransson,O., Deak,M., Toth,R., Campbell,D.G.,
            Morrice,N.A., Prescott,A.R. and Alessi,D.R.
  TITLE     14-3-3 cooperates with LKB1 to regulate the activity and
            localization of QSK and SIK
  JOURNAL   J Cell Sci 118 (Pt 23), 5661-5673 (2005)
   PUBMED   16306228
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Screaton,R.A., Conkright,M.D., Katoh,Y., Best,J.L., Canettieri,G.,
            Jeffries,S., Guzman,E., Niessen,S., Yates,J.R. 3rd, Takemori,H.,
            Okamoto,M. and Montminy,M.
  TITLE     The CREB coactivator TORC2 functions as a calcium- and
            cAMP-sensitive coincidence detector
  JOURNAL   Cell 119 (1), 61-74 (2004)
   PUBMED   15454081
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Iourgenko,V., Zhang,W., Mickanin,C., Daly,I., Jiang,C.,
            Hexham,J.M., Orth,A.P., Miraglia,L., Meltzer,J., Garza,D.,
            Chirn,G.W., McWhinnie,E., Cohen,D., Skelton,J., Terry,R., Yu,Y.,
            Bodian,D., Buxton,F.P., Zhu,J., Song,C. and Labow,M.A.
  TITLE     Identification of a family of cAMP response element-binding protein
            coactivators by genome-scale functional analysis in mammalian cells
  JOURNAL   Proc Natl Acad Sci U S A 100 (21), 12147-12152 (2003)
   PUBMED   14506290
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Conkright,M.D., Canettieri,G., Screaton,R., Guzman,E., Miraglia,L.,
            Hogenesch,J.B. and Montminy,M.
  TITLE     TORCs: transducers of regulated CREB activity
  JOURNAL   Mol Cell 12 (2), 413-423 (2003)
   PUBMED   14536081
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY360172.1, BC053562.1,
            AY726597.1 and BM987537.1.
            
            Summary: This gene encodes a member of the transducers of regulated
            cAMP response element-binding protein activity family of
            transcription coactivators. These proteins promote the
            transcription of genes targeted by the cAMP response
            element-binding protein, and therefore play an important role in
            many cellular processes. Under basal conditions the encoded protein
            is phosphorylated by AMP-activated protein kinase or the
            salt-inducible kinases and is sequestered in the cytoplasm. Upon
            activation by elevated cAMP or calcium, the encoded protein
            translocates to the nucleus and increases target gene expression.
            Single nucleotide polymorphisms in this gene may increase the risk
            of type 2 diabetes. A pseudogene of this gene is located on the
            long arm of chromosome 5. [provided by RefSeq, Dec 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053562.1, SRR1803611.28709.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368633.2/ ENSP00000357622.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..693
                     /product="CREB-regulated transcription coactivator 2"
                     /note="transducer of regulated cAMP response
                     element-binding protein (CREB) 2"
                     /calculated_mol_wt=73171
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          18..72
                     /region_name="TORC_N"
                     /note="Transducer of regulated CREB activity, N terminus;
                     pfam12884"
                     /db_xref="CDD:463738"
     Site            51
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            99
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            120
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            123
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            161
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          168..320
                     /region_name="TORC_M"
                     /note="Transducer of regulated CREB activity middle
                     domain; pfam12885"
                     /db_xref="CDD:463739"
     Site            168
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT6.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK, MARK2, SIK1 and SIK2.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0000269|PubMed:16817901, ECO:0000269|PubMed:17210223,
                     ECO:0000269|PubMed:18626018; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          271..287
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MARK2.
                     /evidence=ECO:0000269|PubMed:18626018; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          282..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          328..554
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            492
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15454081,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Region          615..692
                     /region_name="TORC_C"
                     /note="Transducer of regulated CREB activity, C terminus;
                     pfam12886"
                     /db_xref="CDD:463740"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U182; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     Site            629
                     /site_type="other"
                     /note="Required for ubiquitination and degradation.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q53ET0.2)"
     CDS             1..693
                     /gene="CRTC2"
                     /gene_synonym="TORC-2; TORC2"
                     /coded_by="NM_181715.3:116..2197"
                     /db_xref="CCDS:CCDS30875.1"
                     /db_xref="GeneID:200186"
                     /db_xref="HGNC:HGNC:27301"
                     /db_xref="MIM:608972"
ORIGIN      
        1 matsgangpg satasasnpr kfsekialqk qrqaeetaaf eevmmdigst rlqaqklrla
       61 ytrsshyggs lpnvnqigsg laefqsplhs pldssrstrh hglvervqrd prrmvsplrr
      121 ytrhidsspy spaylspppe sswrrtmawg nfpaekgqlf rlpsalnrts sdsalhtsvm
      181 npspqdtypg ptppsilpsr rggildgemd pkvpaieenl lddkhllkpw dakklsssss
      241 rprscevpgi nifpspdqpa nvpvlppamn tggslpdltn lhfppplptp ldpeetayps
      301 lsggnstsnl thtmthlgis rgmglgpgyd apglhsplsh pslqsslsnp nlqaslsspq
      361 pqlqgshshp slpasslarh vlpttslghp slsapalsss ssssstsspv lgapsypast
      421 pgasphhrrv plsplsllag padarrsqqq lpkqfsptms ptlssitqgv pldtsklstd
      481 qrlppypyss pslvlptqph tpkslqqpgl psqscsvqss ggqppgrqsh ygtpyppgps
      541 ghgqqsyhrp msdfnlgnle qfsmespsas lvldppgfse gpgflggegp mggpqdphtf
      601 nhqnlthcsr hgsgpniilt gdsspgfske iaaalagvpg fevsaaglel glgledelrm
      661 eplgleglnm lsdpcallpd paveesfrsd rlq
//
LOCUS       NP_974198                236 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing protein GIPC1 isoform 2 [Homo sapiens].
ACCESSION   NP_974198
VERSION     NP_974198.1
DBSOURCE    REFSEQ: accession NM_202469.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Gu,X., Jiao,K., Yue,D., Wang,X., Qiao,K., Gao,M., Lin,J., Sun,C.,
            Zhao,C., Zhu,W. and Xi,J.
  TITLE     Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report
  JOURNAL   Neuromuscul Disord 33 (9), 93-97 (2023)
   PUBMED   37550168
  REMARK    GeneRIF: Intrafamilial phenotypic heterogeneity in GIPC1-related
            oculopharyngodistal myopathy type 2: a case report.
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Fan,Y., Shen,S., Yang,J., Yao,D., Li,M., Mao,C., Wang,Y., Hao,X.,
            Ma,D., Li,J., Shi,J., Guo,M., Li,S., Yuan,Y., Liu,F., Yang,Z.,
            Zhang,S., Hu,Z., Fan,L., Liu,H., Zhang,C., Wang,Y., Wang,Q.,
            Zheng,H., He,Y., Song,B., Xu,Y. and Shi,C.
  TITLE     GIPC1 CGG Repeat Expansion Is Associated with Movement Disorders
  JOURNAL   Ann Neurol 91 (5), 704-715 (2022)
   PUBMED   35152460
  REMARK    GeneRIF: GIPC1 CGG Repeat Expansion Is Associated with Movement
            Disorders.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Wang,L.H., Kalb,R.G. and Strittmatter,S.M.
  TITLE     A PDZ protein regulates the distribution of the transmembrane
            semaphorin, M-SemF
  JOURNAL   J Biol Chem 274 (20), 14137-14146 (1999)
   PUBMED   10318831
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Bunn,R.C., Jensen,M.A. and Reed,B.C.
  TITLE     Protein interactions with the glucose transporter binding protein
            GLUT1CBP that provide a link between GLUT1 and the cytoskeleton
  JOURNAL   Mol Biol Cell 10 (4), 819-832 (1999)
   PUBMED   10198040
REFERENCE   8  (residues 1 to 236)
  AUTHORS   De Vries,L., Lou,X., Zhao,G., Zheng,B. and Farquhar,M.G.
  TITLE     GIPC, a PDZ domain containing protein, interacts specifically with
            the C terminus of RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 95 (21), 12340-12345 (1998)
   PUBMED   9770488
REFERENCE   9  (residues 1 to 236)
  AUTHORS   Rousset,R., Fabre,S., Desbois,C., Bantignies,F. and Jalinot,P.
  TITLE     The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
            with the PDZ domain of cellular proteins
  JOURNAL   Oncogene 16 (5), 643-654 (1998)
   PUBMED   9482110
REFERENCE   10 (residues 1 to 236)
  AUTHORS   De Vries,L., Elenko,E., Hubler,L., Jones,T.L. and Farquhar,M.G.
  TITLE     GAIP is membrane-anchored by palmitoylation and interacts with the
            activated (GTP-bound) form of G alpha i subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (26), 15203-15208 (1996)
   PUBMED   8986788
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012318.7, AK290948.1 and BC000410.2.
            
            Summary: GIPC1 is a scaffolding protein that regulates cell surface
            receptor expression and trafficking (Lee et al., 2008 [PubMed
            18775991]).[supplied by OMIM, Apr 2009].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. Variants 4
            and 6 encode the same isoform (2), which has a shorter N-terminus
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.701245.1,
                                           SRR3476690.673877.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..236
                     /product="PDZ domain-containing protein GIPC1 isoform 2"
                     /note="GLUT1 C-terminal binding protein; IGF-1 receptor
                     interacting protein 1; regulator of G-protein signalling
                     19 interacting protein 1; PDZ domain-containing protein
                     GIPC1; tax interaction protein 2; RGS19-interacting
                     protein 1; RGS-GAIP-interacting protein; GAIP
                     C-terminus-interacting protein"
                     /calculated_mol_wt=25941
     Region          29..122
                     /region_name="PDZ_GIPC1"
                     /note="PDZ domain of PDZ domain-containing protein GIPC1;
                     cd23077"
                     /db_xref="CDD:467290"
     Site            order(45..51,61,64,94,98,101..102)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467290"
     Region          164..228
                     /region_name="GH2_GIPC"
                     /note="GIPC-homology 2 (GH2) domain found in the GIPC
                     family; cd21180"
                     /db_xref="CDD:409666"
     Site            order(176,179..184,214)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409666"
     Site            order(177..181,183,185..186,213..215,217,219)
                     /site_type="other"
                     /note="myosin VI binding site [polypeptide binding]"
                     /db_xref="CDD:409666"
     CDS             1..236
                     /gene="GIPC1"
                     /gene_synonym="C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1;
                     NIP; OPDM2; RGS19IP1; SEMCAP; SYNECTIIN; SYNECTIN; TIP-2"
                     /coded_by="NM_202469.3:183..893"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12311.1"
                     /db_xref="GeneID:10755"
                     /db_xref="HGNC:HGNC:1226"
                     /db_xref="MIM:605072"
ORIGIN      
        1 mfctlnthkv dmdkllggqi gledfifahv kgqrkevevf ksedalglti tdngagyafi
       61 krikegsvid hihlisvgdm ieaingqsll gcrhyevarl lkelprgrtf tlklteprka
      121 fdmisqrsag grpgsgpqlg tgrgtlrlrs rgpatvedlp safeekaiek vddllesymg
      181 irdtelaatm velgkdkrnp delaealder lgdfafpdef vfdvwgaigd akvgry
//
LOCUS       NP_002028                537 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase Fyn isoform a [Homo sapiens].
ACCESSION   NP_002028
VERSION     NP_002028.1
DBSOURCE    REFSEQ: accession NM_002037.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Zhu,J., Shi,L. and Su,Y.
  TITLE     FYN as an emerging biological biomarker for prognosis and potential
            therapeutic target in LGG
  JOURNAL   Neurol Res 46 (9), 787-795 (2024)
   PUBMED   38752708
  REMARK    GeneRIF: FYN as an emerging biological biomarker for prognosis and
            potential therapeutic target in LGG.
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Yang,K., Belrose,J., Trepanier,C.H., Lei,G., Jackson,M.F. and
            MacDonald,J.F.
  TITLE     Fyn, a potential target for Alzheimer's disease
  JOURNAL   J Alzheimers Dis 27 (2), 243-252 (2011)
   PUBMED   21799250
  REMARK    GeneRIF: [review] Recent evidence cited in this review suggests
            that alterations in Fyn, a Src family kinase, might contribute to
            Alzheimer's disease pathogenesis.
            Review article
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Saito,Y.D., Jensen,A.R., Salgia,R. and Posadas,E.M.
  TITLE     Fyn: a novel molecular target in cancer
  JOURNAL   Cancer 116 (7), 1629-1637 (2010)
   PUBMED   20151426
  REMARK    Review article
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Rigley,K., Slocombe,P., Proudfoot,K., Wahid,S., Mandair,K. and
            Bebbington,C.
  TITLE     Human p59fyn(T) regulates OKT3-induced calcium influx by a
            mechanism distinct from PIP2 hydrolysis in Jurkat T cells
  JOURNAL   J Immunol 154 (3), 1136-1145 (1995)
   PUBMED   7822789
  REMARK    Erratum:[J Immunol 1995 Apr 15;154(8):4223]
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Gout,I., Dhand,R., Panayotou,G., Fry,M.J., Hiles,I., Otsu,M. and
            Waterfield,M.D.
  TITLE     Expression and characterization of the p85 subunit of the
            phosphatidylinositol 3-kinase complex and a related p85 beta
            protein by using the baculovirus expression system
  JOURNAL   Biochem J 288 (Pt 2) (Pt 2), 395-405 (1992)
   PUBMED   1334406
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Thomas,P.M. and Samelson,L.E.
  TITLE     The glycophosphatidylinositol-anchored Thy-1 molecule interacts
            with the p60fyn protein tyrosine kinase in T cells
  JOURNAL   J Biol Chem 267 (17), 12317-12322 (1992)
   PUBMED   1351058
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Brickell,P.M.
  TITLE     The p60c-src family of protein-tyrosine kinases: structure,
            regulation, and function
  JOURNAL   Crit Rev Oncog 3 (4), 401-446 (1992)
   PUBMED   1384720
  REMARK    Review article
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Kawakami,T., Pennington,C.Y. and Robbins,K.C.
  TITLE     Isolation and oncogenic potential of a novel human src-like gene
  JOURNAL   Mol Cell Biol 6 (12), 4195-4201 (1986)
   PUBMED   3099169
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Semba,K., Nishizawa,M., Miyajima,N., Yoshida,M.C., Sukegawa,J.,
            Yamanashi,Y., Sasaki,M., Yamamoto,T. and Toyoshima,K.
  TITLE     yes-related protooncogene, syn, belongs to the protein-tyrosine
            kinase family
  JOURNAL   Proc Natl Acad Sci U S A 83 (15), 5459-5463 (1986)
   PUBMED   3526330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA570412.1, M14333.1, Z97989.1
            and BP391373.1.
            
            Summary: This gene is a member of the protein-tyrosine kinase
            oncogene family. It encodes a membrane-associated tyrosine kinase
            that has been implicated in the control of cell growth. The protein
            associates with the p85 subunit of phosphatidylinositol 3-kinase
            and interacts with the fyn-binding protein. Alternatively spliced
            transcript variants encoding distinct isoforms exist. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M14333.1, M14676.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148, SAMN03267757
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354650.7/ ENSP00000346671.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..537
                     /product="tyrosine-protein kinase Fyn isoform a"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase Fyn; src-like kinase; c-syn
                     protooncogene; tyrosine kinase p59fyn(T); OKT3-induced
                     calcium influx regulator; src/yes-related novel;
                     proto-oncogene Syn; proto-oncogene c-Fyn; FYN oncogene
                     related to SRC, FGR, YES"
                     /calculated_mol_wt=60631
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC.
                     /evidence=ECO:0000269|PubMed:15537652; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     Region          14..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06241.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     Region          85..140
                     /region_name="SH3_Fyn_Yrk"
                     /note="Src homology 3 domain of Fyn and Yrk Protein
                     Tyrosine Kinases; cd12006"
                     /db_xref="CDD:212939"
     Site            order(91,93,96..97,100,116..119,132,134,136..137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Site            order(93,96..100,116,119,132)
                     /site_type="other"
                     /note="SAP interaction site [polypeptide binding]"
                     /db_xref="CDD:212939"
     Region          145..245
                     /region_name="SH2_Src_Fyn_isoform_a_like"
                     /note="Src homology 2 (SH2) domain found in Fyn isoform a
                     like proteins; cd10418"
                     /db_xref="CDD:198281"
     Site            order(156,176,178..181,186,202,204,237)
                     /site_type="other"
                     /note="autoinhibitory site [polypeptide binding]"
                     /db_xref="CDD:198281"
     Site            order(156,176,202,204)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198281"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P39688; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     Site            order(203,231)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198281"
     Region          261..534
                     /region_name="PTKc_Fyn"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fyn; cd05070"
                     /db_xref="CDD:270655"
     Site            order(277,279..281,285,297,299,342..345,349,390,394..395,
                     397,408,425..429,438,472)
                     /site_type="active"
                     /db_xref="CDD:270655"
     Site            order(277,280,285,297,299,342..345,349,390,392,395,397,
                     408)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270655"
     Site            order(291,293,325,328,330,343,369,373,401,521)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(379,382..383,446,508..510,512,514..515,518,522,
                     525..526,530)
                     /site_type="other"
                     /note="CSK binding interface [polypeptide binding]"
                     /db_xref="CDD:270655"
     Site            order(390,394,425..429,438,472)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270655"
     Site            407..431
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270655"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P39688; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by CSK.
                     /evidence=ECO:0000269|PubMed:1699196,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P06241.3)"
     CDS             1..537
                     /gene="FYN"
                     /gene_synonym="p59-FYN; SLK; SYN"
                     /coded_by="NM_002037.5:608..2221"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5094.1"
                     /db_xref="GeneID:2534"
                     /db_xref="HGNC:HGNC:4037"
                     /db_xref="MIM:137025"
ORIGIN      
        1 mgcvqckdke atklteerdg slnqssgyry gtdptpqhyp sfgvtsipny nnfhaaggqg
       61 ltvfggvnss shtgtlrtrg gtgvtlfval ydyeartedd lsfhkgekfq ilnssegdww
      121 earslttget gyipsnyvap vdsiqaeewy fgklgrkdae rqllsfgnpr gtflireset
      181 tkgayslsir dwddmkgdhv khykirkldn ggyyittraq fetlqqlvqh yseraaglcc
      241 rlvvpchkgm prltdlsvkt kdvweipres lqlikrlgng qfgevwmgtw ngntkvaikt
      301 lkpgtmspes fleeaqimkk lkhdklvqly avvseepiyi vteymnkgsl ldflkdgegr
      361 alklpnlvdm aaqvaagmay iermnyihrd lrsanilvgn glickiadfg larliedney
      421 tarqgakfpi kwtapeaaly grftiksdvw sfgilltelv tkgrvpypgm nnrevleqve
      481 rgyrmpcpqd cpislhelmi hcwkkdpeer ptfeylqsfl edyftatepq yqpgenl
//
LOCUS       NP_859051                603 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A
            beta isoform isoform c [Homo sapiens].
ACCESSION   NP_859051
VERSION     NP_859051.1
DBSOURCE    REFSEQ: accession NM_181700.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Peng,S., He,T., Liu,Y., Zheng,L., Zhong,Y., Niu,Z., Zhang,M. and
            Yang,S.
  TITLE     Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B by
            Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs
  JOURNAL   Stem Cell Rev Rep 19 (6), 1981-1993 (2023)
   PUBMED   37243830
  REMARK    GeneRIF: Lnc-PPP2R1B Mediates the Alternative Splicing of PPP2R1B
            by Interacting and Stabilizing HNRNPLL and Promotes Osteogenesis of
            MSCs.
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Du,M., Yuan,L., Zhang,Z., Zhang,C., Zhu,M., Zhang,Z., Li,R.,
            Zhao,X., Liang,H., Li,Y., Jiang,H., Qiao,J. and Yin,Y.
  TITLE     PPP2R1B is modulated by ubiquitination and is essential for
            spermatogenesis
  JOURNAL   FASEB J 35 (5), e21564 (2021)
   PUBMED   33913576
  REMARK    GeneRIF: PPP2R1B is modulated by ubiquitination and is essential
            for spermatogenesis.
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Adler,H.T., Nallaseth,F.S., Walter,G. and Tkachuk,D.C.
  TITLE     HRX leukemic fusion proteins form a heterocomplex with the
            leukemia-associated protein SET and protein phosphatase 2A
  JOURNAL   J Biol Chem 272 (45), 28407-28414 (1997)
   PUBMED   9353299
REFERENCE   7  (residues 1 to 603)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   8  (residues 1 to 603)
  AUTHORS   Hendrix,P., Mayer-Jackel,R.E., Cron,P., Goris,J., Hofsteenge,J.,
            Merlevede,W. and Hemmings,B.A.
  TITLE     Structure and expression of a 72-kDa regulatory subunit of protein
            phosphatase 2A. Evidence for different size forms produced by
            alternative splicing
  JOURNAL   J Biol Chem 268 (20), 15267-15276 (1993)
   PUBMED   8392071
REFERENCE   9  (residues 1 to 603)
  AUTHORS   Kamibayashi,C., Lickteig,R.L., Estes,R., Walter,G. and Mumby,M.C.
  TITLE     Expression of the A subunit of protein phosphatase 2A and
            characterization of its interactions with the catalytic and
            regulatory subunits
  JOURNAL   J Biol Chem 267 (30), 21864-21872 (1992)
   PUBMED   1328247
REFERENCE   10 (residues 1 to 603)
  AUTHORS   Hemmings,B.A., Adams-Pearson,C., Maurer,F., Muller,P., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Stone,S.R.
  TITLE     alpha- and beta-forms of the 65-kDa subunit of protein phosphatase
            2A have a similar 39 amino acid repeating structure
  JOURNAL   Biochemistry 29 (13), 3166-3173 (1990)
   PUBMED   2159327
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC402587.1, AK301705.1 and
            DB527885.1.
            
            Summary: This gene encodes a constant regulatory subunit of protein
            phosphatase 2. Protein phosphatase 2 is one of the four major
            Ser/Thr phosphatases, and it is implicated in the negative control
            of cell growth and division. It consists of a common heteromeric
            core enzyme, which is composed of a catalytic subunit and a
            constant regulatory subunit, that associates with a variety of
            regulatory subunits. The constant regulatory subunit A serves as a
            scaffolding molecule to coordinate the assembly of the catalytic
            subunit and a variable regulatory B subunit. This gene encodes a
            beta isoform of the constant regulatory subunit A. Mutations in
            this gene have been associated with some lung and colon cancers.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Apr 2010].
            
            Transcript Variant: This variant (3) lacks two in-frame exons in
            the 5' coding region and differs in the 3' UTR and the 3' coding
            region, compared to variant 1. The resulting isoform (c) contains a
            longer and distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301705.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.1"
     Protein         1..603
                     /product="serine/threonine-protein phosphatase 2A 65 kDa
                     regulatory subunit A beta isoform isoform c"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, structural/regulatory
                     subunit A, beta; protein phosphatase 2, regulatory subunit
                     A, beta"
                     /calculated_mol_wt=66486
     Region          26..175
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          41..62
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          79..101
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          114..142
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          129..300
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          152..182
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          193..217
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(209..210,213,216..217,248..249,252,255..256,259,
                     291..292,295,298..299,302,330..331,334,337..338,369..370,
                     373,376..377)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          231..259
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          273..303
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          312..338
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          314..414
                     /region_name="HEAT_2"
                     /note="HEAT repeats; pfam13646"
                     /db_xref="CDD:433376"
     Region          349..378
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          390..416
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          427..456
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          466..492
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          507..533
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..603
                     /gene="PPP2R1B"
                     /gene_synonym="PP2A-Abeta; PR65B"
                     /coded_by="NM_181700.2:29..1840"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53706.1"
                     /db_xref="GeneID:5519"
                     /db_xref="HGNC:HGNC:9303"
                     /db_xref="MIM:603113"
ORIGIN      
        1 magaselgtg pgaaggdgdd slypiavlid elrnedvqpp lenlatveet vvrdkavesl
       61 rqisqehtpv aleayfvplv krlasgdwft srtsacglfs vcyprasnav kaeirqqfrs
      121 lcsddtpmvr raaasklgef akvleldsvk seivplftsl asdeqdsvrl laveacvsia
      181 qllsqddlet lvmptlrqaa edkswrvrym vadrfselqk amgpkitlnd lipafqnllk
      241 dceaevraaa ahkvkelgen lpiedretii mnqilpyike lvsdtnqhvk salasvimgl
      301 stilgkenti ehllplflaq lkdecpdvrl niisnldcvn evigirqlsq sllpaivela
      361 edakwrvrla iieympllag qlgveffdek lnslcmawlv dhvyaireaa tnnlmklvqk
      421 fgtewaqnti vpkvlvmand pnylhrmttl fcinalseac gqeittkqml pivlkmagdq
      481 vanvrfnvak slqkigpild tnalqgevkp vlqklgqded mdvkyfaqea isvvaqrlrk
      541 lefpvkdsge psvpradknh fprptvpged mgkgpvyqlr gdtrdtlaql giaelvhfsq
      601 std
//
LOCUS       NP_001356804            1194 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 11 [Homo sapiens].
ACCESSION   NP_001356804 XP_005252371
VERSION     NP_001356804.1
DBSOURCE    REFSEQ: accession NM_001369875.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1194)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1194)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1194)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1194)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358113.21.
            
            On Apr 23, 2019 this sequence version replaced XP_005252371.1.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.77695.1,
                                           SRR1803616.171493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1194
                     /product="tight junction protein 2 isoform 11"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=134438
     Region          36..122
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(47..53,71,74,102,106,109..110)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          148..>230
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          187..>278
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          310..388
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(310..316,321..337,340..342,345,347..348,355,
                     363..364,366..367,379..385)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(322..328,334,337,367,371,374..375)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          513..594
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(524..530,540,543,572,576,579..580)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          608..670
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(617,619,622,626,647..648,664,666..667)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          704..883
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1194
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_001369875.1:8..3592"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 mktaqalhrm wiqavkklrr wkgrapgmee liweqytvtl qkdskrgfgi avsggrdnph
       61 fengetsivi sdvlpggpad gllqendrvv mvngtpmedv lhsfavqqlr ksgkvaaivv
      121 krprkvqvaa lqasppldqd drafevmdef dgrsfrsgys ersrlnshgg rsrswedspe
      181 rgrpherars rerdlsrdrs rgrslergld qdhartrdrs rgrslergld hdfgpsrdrd
      241 rdrsrgrsid qdyerayhra ydpdyerays peyrrgarhd arsrgprsrs rehphsrsps
      301 peprgrpgpi gvllmksran eeyglrlgsq ifvkemtrtg latkdgnlhe gdiilkingt
      361 vtenmsltda rklieksrgk lqlvvlrdsq qtlinipsln dsdseiedis eiesnrsfsp
      421 eerrhqysdy dyhssseklk erpssredtp srlsrmgatp tpfkstgdia gtvvpetnke
      481 pryqedppap qpkaaprtfl rpspedeaiy gpntkmvrfk kgdsvglrla ggndvgifva
      541 giqegtsaeq eglqegdqil kvntqdfrgl vredavlyll eipkgemvti laqsradvyr
      601 dilacgrgds ffirshfece ketpqslaft rgevfrvvdt lydgklgnwl avrignelek
      661 glipnksrae qmasvqnaqr dnagdradfw rmrgqrsgvk knlrksredl tavvsvstkf
      721 payervllre agfkrpvvlf gpiadiamek lanelpdwfq taktepkdag sekstgvvrl
      781 ntvrqiieqd khalldvtpk avdllnytqw fpiviffnpd srqgvktmrq rlnptsnkss
      841 rklfdqankl kktcahlfta tinlnsands wfgslkdtiq hqqgeavwvs egkmegmddd
      901 pedrmsylta mgadylscds rlisdfedtd geggaytdne ldepaeeplv ssitrssepv
      961 qheesirkps pepraqmrra assdqlrdns pppafkpepp kaktqnkees ydfsksyeyk
     1021 snpsavagne tpgastkgyp ppvaakptfg rsilkpstpi ppqegeevge sseeqdnapk
     1081 svlgkvkife kmdhkarlqr mqelqeaqna rieiaqkhpd iyavpikthk pdpgtpqhts
     1141 srppepqkap srpyqdtrgs ygsdaeeeey rqqlsehskr gyygqsaryr dtel
//
LOCUS       NP_001311320             405 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001311320
VERSION     NP_001311320.1
DBSOURCE    REFSEQ: accession NM_001324391.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 405)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, BC009259.2, AC108449.5 and BQ019252.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.3974.1, SRR1803615.7026.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..405
                     /product="homeobox-containing protein 1 isoform 7"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=45850
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..405
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324391.2:342..1559"
                     /note="isoform 7 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS83274.1"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr aniaailesh gidvqspggh
      361 snsddvdgnd yseqdtwqvr ngeeeegrss eggreaekve eerri
//
LOCUS       NP_203744                863 aa            linear   PRI 20-NOV-2025
DEFINITION  MICAL-like protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_203744
VERSION     NP_203744.1
DBSOURCE    REFSEQ: accession NM_033386.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 863)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 863)
  AUTHORS   Frisby,D., Murakonda,A.B., Ashraf,B., Dhawan,K., Almeida-Souza,L.,
            Naslavsky,N. and Caplan,S.
  TITLE     Endosomal actin branching, fission, and receptor recycling require
            FCHSD2 recruitment by MICAL-L1
  JOURNAL   Mol Biol Cell 35 (11), ar144 (2024)
   PUBMED   39382837
  REMARK    GeneRIF: Endosomal actin branching, fission, and receptor recycling
            require FCHSD2 recruitment by MICAL-L1.
REFERENCE   3  (residues 1 to 863)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 863)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 863)
  AUTHORS   Sikora,R., Bun,P., Danglot,L., Alqabandi,M., Bassereau,P.,
            Niedergang,F., Galli,T. and Zahraoui,A.
  TITLE     MICAL-L1 is required for cargo protein delivery to the cell surface
  JOURNAL   Biol Open 10 (6) (2021)
   PUBMED   34100897
  REMARK    GeneRIF: MICAL-L1 is required for cargo protein delivery to the
            cell surface.
REFERENCE   6  (residues 1 to 863)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 863)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 863)
  AUTHORS   Weide,T., Teuber,J., Bayer,M. and Barnekow,A.
  TITLE     MICAL-1 isoforms, novel rab1 interacting proteins
  JOURNAL   Biochem Biophys Res Commun 306 (1), 79-86 (2003)
   PUBMED   12788069
REFERENCE   9  (residues 1 to 863)
  AUTHORS   Terman,J.R., Mao,T., Pasterkamp,R.J., Yu,H.H. and Kolodkin,A.L.
  TITLE     MICALs, a family of conserved flavoprotein oxidoreductases,
            function in plexin-mediated axonal repulsion
  JOURNAL   Cell 109 (7), 887-900 (2002)
   PUBMED   12110185
REFERENCE   10 (residues 1 to 863)
  AUTHORS   Marzesco,A.M., Dunia,I., Pandjaitan,R., Recouvreur,M., Dauzonne,D.,
            Benedetti,E.L., Louvard,D. and Zahraoui,A.
  TITLE     The small GTPase Rab13 regulates assembly of functional tight
            junctions in epithelial cells
  JOURNAL   Mol Biol Cell 13 (6), 1819-1831 (2002)
   PUBMED   12058051
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR004306.1, AJ496196.1, AL834373.1, CA307559.1 and AL022311.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK000466.1, AL834373.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215957.10/ ENSP00000215957.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..863
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..863
                     /product="MICAL-like protein 1 isoform 3"
                     /note="molecule interacting with Rab13; MICAL-like protein
                     1"
                     /calculated_mol_wt=93310
     Region          4..110
                     /region_name="CH_MICALL1"
                     /note="calponin homology (CH) domain found in MICAL-like
                     protein 1; cd21252"
                     /db_xref="CDD:409101"
     Site            order(4,8,58,60..61,64..65,67,76..84,92,94..95,97..98,
                     101..102,105)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409101"
     Region          119..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          164..218
                     /region_name="LIM_Mical_like_1"
                     /note="This domain belongs to the LIM domain family which
                     are found on Mical (molecule interacting with CasL) like
                     proteins; cd09444"
                     /db_xref="CDD:188828"
     Site            order(164,167,185,188,191,194,214,217)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188828"
     Region          224..670
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          <246..667
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          425..427
                     /region_name="NPF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          633..635
                     /region_name="NPF2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          652..863
                     /region_name="Mediates the interaction with RAB13 and
                     RAB35 and intramolecular interaction with the CH domain.
                     /evidence=ECO:0000269|PubMed:21795389,
                     ECO:0000269|PubMed:21951725"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Region          687..808
                     /region_name="bMERB_dom"
                     /note="Bivalent Mical/EHBP Rab binding domain; pfam12130"
                     /db_xref="CDD:463467"
     Region          700..863
                     /region_name="Necessary and sufficient to associate with
                     tubular recycling endosome membranes, mediate phosphatidic
                     acid-binding and membrane tubulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N3F8.2)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BGT6; propagated from
                     UniProtKB/Swiss-Prot (Q8N3F8.2)"
     CDS             1..863
                     /gene="MICALL1"
                     /gene_synonym="MICAL-L1; MIRAB13"
                     /coded_by="NM_033386.4:127..2718"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13961.1"
                     /db_xref="GeneID:85377"
                     /db_xref="HGNC:HGNC:29804"
                     /db_xref="MIM:619563"
ORIGIN      
        1 magprgalla wcrrqcegyr gveirdlsss frdglafcai lhrhrpdlld fdslskdnvf
       61 ennrlafeva ekelgipall dpndmvsmsv pdclsimtyv sqyynhfcsp gqagvspprk
      121 glapcsppsv aptpvepedv aqgeelssgs lseqgtgqtp sstcaacqqh vhlvqrylad
      181 grlyhrhcfr crrcsstllp gayengpeeg tfvcaehcar lgpgtrsgtr pgpfsqpkqq
      241 hqqqlaedak dvpgggpsss apagaeadgp kaspearpqi ptkprvpgkl qelasppagr
      301 ptpaprkase sttpapptpr prsslqqenl veqagssslv ngrlhelpvp kprgtpkpse
      361 gtpaprkdpp witlvqaepk kkpaplppss spgppsqdsr qvenggteev aqpsptasle
      421 skpynpfeee eedkeeeapa apslatspal ghpestpksl hpwygitpts spktkkrpap
      481 rapsasplal hasrlshsep psatpspals veslssesas qtagaellep pavpksssep
      541 avhapgtpgn pvslstnssl assgelvepr veqmpqaspg laprtrgssg pqpakpcsga
      601 tptplllvgd rspvpspgss spqlqvkssc kenpfnrkps paaspatkka tkgskpvrpp
      661 apghgfplik rkvqadqyip eedihgemdt ierrldaleh rgvlleeklr gglnegredd
      721 mlvdwfklih ekhllvrres eliyvfkqqn leqrqadvey elrcllnkpe kdwteedrar
      781 ekvlmqelvt lieqrnaiin cldedrqree eedkmleami kkkefqreae pegkkkgkfk
      841 tmkmlkllgn krdakskspr dks
//
LOCUS       NP_004273                211 aa            linear   PRI 20-NOV-2025
DEFINITION  BAG family molecular chaperone regulator 2 [Homo sapiens].
ACCESSION   NP_004273
VERSION     NP_004273.1
DBSOURCE    REFSEQ: accession NM_004282.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Lauer,S.M., Omar,M.H., Golkowski,M.G., Kenerson,H.L., Lee,K.S.,
            Pascual,B.C., Lim,H.C., Forbush,K., Smith,F.D., Gordan,J.D.,
            Ong,S.E., Yeung,R.S. and Scott,J.D.
  TITLE     Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell survival
            and resistance to drug-induced apoptosis in fibrolamellar carcinoma
  JOURNAL   Cell Rep 43 (2), 113678 (2024)
   PUBMED   38236773
  REMARK    GeneRIF: Recruitment of BAG2 to DNAJ-PKAc scaffolds promotes cell
            survival and resistance to drug-induced apoptosis in fibrolamellar
            carcinoma.
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Iglesias-Martinez,L.F., Rauch,N., Wynne,K., McCann,B., Kolch,W. and
            Rauch,J.
  TITLE     Interactome dynamics of RAF1-BRAF kinase monomers and dimers
  JOURNAL   Sci Data 10 (1), 203 (2023)
   PUBMED   37045861
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Huang,X., Shi,D., Zou,X., Wu,X., Huang,S., Kong,L., Yang,M.,
            Xiao,Y., Chen,B., Chen,X., Ouyang,Y., Song,L., Jian,Y. and Lin,C.
  TITLE     BAG2 drives chemoresistance of breast cancer by exacerbating mutant
            p53 aggregate
  JOURNAL   Theranostics 13 (1), 339-354 (2023)
   PUBMED   36593950
  REMARK    GeneRIF: BAG2 drives chemoresistance of breast cancer by
            exacerbating mutant p53 aggregate.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Lima,R.S., Carrettiero,D.C. and Ferrari,M.F.R.
  TITLE     BAG2 prevents Tau hyperphosphorylation and increases p62/SQSTM1 in
            cell models of neurodegeneration
  JOURNAL   Mol Biol Rep 49 (8), 7623-7635 (2022)
   PUBMED   35612780
  REMARK    GeneRIF: BAG2 prevents Tau hyperphosphorylation and increases
            p62/SQSTM1 in cell models of neurodegeneration.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Ueda,K., Kosako,H., Fukui,Y. and Hattori,S.
  TITLE     Proteomic identification of Bcl2-associated athanogene 2 as a novel
            MAPK-activated protein kinase 2 substrate
  JOURNAL   J Biol Chem 279 (40), 41815-41821 (2004)
   PUBMED   15271996
  REMARK    GeneRIF: BAG2 was directly phosphorylated at serine 20 in vitro by
            MAPKAPK2 and MAPKAP2 is also required for phosphorylation of BAG2
            in vivo.
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Takayama,S., Xie,Z. and Reed,J.C.
  TITLE     An evolutionarily conserved family of Hsp70/Hsc70 molecular
            chaperone regulators
  JOURNAL   J Biol Chem 274 (2), 781-786 (1999)
   PUBMED   9873016
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Halse,R., Rochford,J.J., McCormack,J.G., Vandenheede,J.R.,
            Hemmings,B.A. and Yeaman,S.J.
  TITLE     Control of glycogen synthesis in cultured human muscle cells
  JOURNAL   J Biol Chem 274 (2), 776-780 (1999)
   PUBMED   9873015
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA874388.1, AL136311.7,
            AL050287.1, CA442969.1 and AL031321.1.
            
            Summary: BAG proteins compete with Hip for binding to the
            Hsc70/Hsp70 ATPase domain and promote substrate release. All the
            BAG proteins have an approximately 45-amino acid BAG domain near
            the C terminus but differ markedly in their N-terminal regions. The
            predicted BAG2 protein contains 211 amino acids. The BAG domains of
            BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase
            domain in vitro and in mammalian cells. All 3 proteins bind with
            high affinity to the ATPase domain of Hsc70 and inhibit its
            chaperone activity in a Hip-repressible manner. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.250176.1,
                                           SRR1803617.34704.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370693.5/ ENSP00000359727.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..211
                     /product="BAG family molecular chaperone regulator 2"
                     /note="dJ417I1.2 (BAG-family molecular chaperone regulator
                     2); bcl-2-associated athanogene 2; BCL2 associated
                     athanogene 2"
                     /calculated_mol_wt=23641
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95816.1)"
     Region          109..189
                     /region_name="BAG"
                     /note="BAG domains, present in regulator of Hsp70
                     proteins; smart00264"
                     /db_xref="CDD:214591"
     CDS             1..211
                     /gene="BAG2"
                     /gene_synonym="BAG-2; dJ417I1.2"
                     /coded_by="NM_004282.4:373..1008"
                     /db_xref="CCDS:CCDS4961.1"
                     /db_xref="GeneID:9532"
                     /db_xref="HGNC:HGNC:938"
                     /db_xref="MIM:603882"
ORIGIN      
        1 maqakinaka negrfcrsss madrssrlle sldqlelrve alreaatave qekeillemi
       61 hsiqnsqdmr qisdgereel nltanrlmgr tltvevsvet irnpqqqesl khatriidev
      121 vnkflddlgn akshlmslys acssevphgp vdqkfqsivi gcaledqkki krrletllrn
      181 iensdkaikl lehskgagsk tlqqnaesrf n
//
LOCUS       NP_001295146             390 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-gated potassium channel subunit beta-1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001295146 XP_005247810
VERSION     NP_001295146.1
DBSOURCE    REFSEQ: accession NM_001308217.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Quintanilha,J.C.F., Wang,J., Sibley,A.B., Jiang,C., Etheridge,A.S.,
            Shen,F., Jiang,G., Mulkey,F., Patel,J.N., Hertz,D.L., Dees,E.C.,
            McLeod,H.L., Bertagnolli,M., Rugo,H., Kindler,H.L., Kelly,W.K.,
            Ratain,M.J., Kroetz,D.L., Owzar,K., Schneider,B.P., Lin,D. and
            Innocenti,F.
  TITLE     Bevacizumab-induced hypertension and proteinuria: a genome-wide
            study of more than 1000 patients
  JOURNAL   Br J Cancer 126 (2), 265-274 (2022)
   PUBMED   34616010
  REMARK    GeneRIF: Bevacizumab-induced hypertension and proteinuria: a
            genome-wide study of more than 1000 patients.
            Erratum:[Br J Cancer. 2022 Jan;126(1):162. doi:
            10.1038/s41416-021-01617-1. PMID: 34853435]
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Macias,A., de la Cruz,A., Peraza,D.A., Benito-Bueno,A., Gonzalez,T.
            and Valenzuela,C.
  TITLE     KV1.5-KVbeta1.3 Recycling Is PKC-Dependent
  JOURNAL   Int J Mol Sci 22 (3), 1336 (2021)
   PUBMED   33572906
  REMARK    GeneRIF: KV1.5-KVbeta1.3 Recycling Is PKC-Dependent.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Cho,I.H., Panzera,L.C., Chin,M., Alpizar,S.A., Olveda,G.E.,
            Hill,R.A. and Hoppa,M.B.
  TITLE     The potassium channel subunit Kvbeta1 serves as a major control
            point for synaptic facilitation
  JOURNAL   Proc Natl Acad Sci U S A 117 (47), 29937-29947 (2020)
   PUBMED   33168717
  REMARK    GeneRIF: The potassium channel subunit Kvbeta1 serves as a major
            control point for synaptic facilitation.
REFERENCE   6  (residues 1 to 390)
  AUTHORS   England,S.K., Uebele,V.N., Kodali,J., Bennett,P.B. and Tamkun,M.M.
  TITLE     A novel K+ channel beta-subunit (hKv beta 1.3) is produced via
            alternative mRNA splicing
  JOURNAL   J Biol Chem 270 (48), 28531-28534 (1995)
   PUBMED   7499366
REFERENCE   7  (residues 1 to 390)
  AUTHORS   McCormack,K., McCormack,T., Tanouye,M., Rudy,B. and Stuhmer,W.
  TITLE     Alternative splicing of the human Shaker K+ channel beta 1 gene and
            functional expression of the beta 2 gene product
  JOURNAL   FEBS Lett 370 (1-2), 32-36 (1995)
   PUBMED   7649300
REFERENCE   8  (residues 1 to 390)
  AUTHORS   England,S.K., Uebele,V.N., Shear,H., Kodali,J., Bennett,P.B. and
            Tamkun,M.M.
  TITLE     Characterization of a voltage-gated K+ channel beta subunit
            expressed in human heart
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6309-6313 (1995)
   PUBMED   7603988
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Morales,M.J., Castellino,R.C., Crews,A.L., Rasmusson,R.L. and
            Strauss,H.C.
  TITLE     A novel beta subunit increases rate of inactivation of specific
            voltage-gated potassium channel alpha subunits
  JOURNAL   J Biol Chem 270 (11), 6272-6277 (1995)
   PUBMED   7890764
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Majumder,K., De Biasi,M., Wang,Z. and Wible,B.A.
  TITLE     Molecular cloning and functional expression of a novel potassium
            channel beta-subunit from human atrium
  JOURNAL   FEBS Lett 361 (1), 13-16 (1995)
   PUBMED   7890032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC410397.1, AK303287.1,
            AC092927.5 and BC043166.2.
            
            On Apr 28, 2015 this sequence version replaced XP_005247810.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member includes distinct isoforms
            which are encoded by alternatively spliced transcript variants of
            this gene. Some of these isoforms are beta subunits, which form
            heteromultimeric complexes with alpha subunits and modulate the
            activity of the pore-forming alpha subunits. [provided by RefSeq,
            Apr 2015].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. It encodes
            isoform 4 which is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.245574.1,
                                           SRR1803614.280971.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..390
                     /product="voltage-gated potassium channel subunit beta-1
                     isoform 4"
                     /note="potassium channel beta 3 chain; potassium channel
                     beta3 subunit; potassium channel shaker chain beta 1a;
                     K(+) channel subunit beta-1; potassium voltage-gated
                     channel, shaker-related subfamily, beta member 1; K+
                     channel Beta1a chain; potassium voltage-gated channel
                     subfamily A member regulatory beta subunit 1; potassium
                     channel, voltage gated subfamily A regulatory beta subunit
                     1"
                     /calculated_mol_wt=43173
     Region          89..382
                     /region_name="AKR_SF"
                     /note="Aldo-keto reductase (AKR) superfamily; cl00470"
                     /db_xref="CDD:444925"
     Site            order(107..109,137,142,170,211..212,237,266..272,327,
                     344..347,352,355..356)
                     /site_type="active"
                     /db_xref="CDD:381296"
     CDS             1..390
                     /gene="KCNAB1"
                     /gene_synonym="AKR6A3; hKvb3; hKvBeta3; KCNA1B; KV-BETA-1;
                     Kvb1.3"
                     /coded_by="NM_001308217.1:65..1237"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS77844.1"
                     /db_xref="GeneID:7881"
                     /db_xref="HGNC:HGNC:6228"
                     /db_xref="MIM:601141"
ORIGIN      
        1 mlaartgaag sqiseentkl rrqsgfsvag kdkspkkase nakdsslsps gesqlrarql
       61 allrevemnw ylklcdlsse httvcttgmp hrnlgksglr vsclglgtwv tfggqisdev
      121 aerlmtiaye sgvnlfdtae vyaagkaevi lgsiikkkgw rrsslvittk lywggkaete
      181 rglsrkhiie eivramthvi nqgmamywgt srwsameime aysvarqfnm ippvceqaey
      241 hlfqrekvev qlpelyhkig vgamtwspla cgiisgkygn gvpessrasl kcyqwlkeri
      301 vseegrkqqn klkdlspiae rlgctlpqla vawclrnegv ssvllgsstp eqlienlgai
      361 qvlpkmtshv vneidnilrn kpyskkdyrs
//
LOCUS       NP_001758                351 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell surface antigen CD2 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001758 XP_001720847 XP_001723066 XP_001723789
VERSION     NP_001758.2
DBSOURCE    REFSEQ: accession NM_001767.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Wu,M., Chen,Y., Hua,G. and Chunhui,L.
  TITLE     The CD2-CD58 axis: A novel marker predicting poor prognosis in
            patients with low-grade gliomas and potential therapeutic
            approaches
  JOURNAL   Immun Inflamm Dis 11 (10), e1022 (2023)
   PUBMED   37904707
  REMARK    GeneRIF: The CD2-CD58 axis: A novel marker predicting poor
            prognosis in patients with low-grade gliomas and potential
            therapeutic approaches.
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Romain,G., Strati,P., Rezvan,A., Fathi,M., Bandey,I.N.,
            Adolacion,J.R.T., Heeke,D., Liadi,I., Marques-Piubelli,M.L.,
            Solis,L.M., Mahendra,A., Vega,F., Cooper,L.J., Singh,H., Mattie,M.,
            Bot,A., Neelapu,S.S. and Varadarajan,N.
  TITLE     Multidimensional single-cell analysis identifies a role for
            CD2-CD58 interactions in clinical antitumor T cell responses
  JOURNAL   J Clin Invest 132 (17) (2022)
   PUBMED   35881486
  REMARK    GeneRIF: Multidimensional single-cell analysis identifies a role
            for CD2-CD58 interactions in clinical antitumor T cell responses.
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Fernandez Lahore,G., Forster,M., Johannesson,M., Sabatier,P.,
            Lonnblom,E., Aoun,M., He,Y., Nandakumar,K.S., Zubarev,R.A. and
            Holmdahl,R.
  TITLE     Polymorphic estrogen receptor binding site causes Cd2-dependent sex
            bias in the susceptibility to autoimmune diseases
  JOURNAL   Nat Commun 12 (1), 5565 (2021)
   PUBMED   34552089
  REMARK    GeneRIF: Polymorphic estrogen receptor binding site causes
            Cd2-dependent sex bias in the susceptibility to autoimmune
            diseases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Rozenova,K.A., Jevremovic,D., Reichard,K.K., Nguyen,P.,
            Otteson,G.E., Timm,M.M., Horna,P., Olteanu,H. and Shi,M.
  TITLE     CD2 and CD7 are sensitive flow cytometry screening markers for
            T-lineage acute leukemia(s): a study of 465 acute leukemia cases
  JOURNAL   Hum Pathol 114, 66-73 (2021)
   PUBMED   34019867
  REMARK    GeneRIF: CD2 and CD7 are sensitive flow cytometry screening markers
            for T-lineage acute leukemia(s): a study of 465 acute leukemia
            cases.
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Luzzati,A.L., Giacomini,E., Giordani,L., Pugliese,O., Viora,M. and
            Chersi,A.
  TITLE     The antigen-specific induction of normal human lymphocytes in vitro
            is down-regulated by a conserved HIV p24 epitope
  JOURNAL   Immunol Lett 33 (3), 307-314 (1992)
   PUBMED   1385321
  REMARK    Erratum:[Immunol Lett 1993 Jan;35(1):82]
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Hahn,W.C., Menu,E., Bothwell,A.L., Sims,P.J. and Bierer,B.E.
  TITLE     Overlapping but nonidentical binding sites on CD2 for CD58 and a
            second ligand CD59
  JOURNAL   Science 256 (5065), 1805-1807 (1992)
   PUBMED   1377404
REFERENCE   8  (residues 1 to 351)
  AUTHORS   Marie-Cardine,A., Maridonneau-Parini,I., Ferrer,M., Danielian,S.,
            Rothhut,B., Fagard,R., Dautry-Varsat,A. and Fischer,S.
  TITLE     The lymphocyte-specific tyrosine protein kinase p56lck is
            endocytosed in Jurkat cells stimulated via CD2
  JOURNAL   J Immunol 148 (12), 3879-3884 (1992)
   PUBMED   1351089
REFERENCE   9  (residues 1 to 351)
  AUTHORS   Bell,G.M., Seaman,W.E., Niemi,E.C. and Imboden,J.B.
  TITLE     The OX-44 molecule couples to signaling pathways and is associated
            with CD2 on rat T lymphocytes and a natural killer cell line
  JOURNAL   J Exp Med 175 (2), 527-536 (1992)
   PUBMED   1346273
REFERENCE   10 (residues 1 to 351)
  AUTHORS   Schraven,B., Samstag,Y., Altevogt,P. and Meuer,S.C.
  TITLE     Association of CD2 and CD45 on human T lymphocytes
  JOURNAL   Nature 345 (6270), 71-74 (1990)
   PUBMED   1970422
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD691699.1, AK313614.1 and
            BC033583.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 27, 2009 this sequence version replaced
            XP_001723066.1, XP_001720847.1, XP_001723789.1, NP_001758.1.
            
            Summary: The protein encoded by this gene is a surface antigen
            found on all peripheral blood T-cells. The encoded protein
            interacts with LFA3 (CD58) on antigen presenting cells to optimize
            immune recognition. A locus control region (LCR) has been found in
            the 3' flanking sequence of this gene. [provided by RefSeq, Jun
            2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223393.1, M16336.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369478.4/ ENSP00000358490.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.1"
     Protein         1..351
                     /product="T-cell surface antigen CD2 isoform 2 precursor"
                     /note="lymphocyte-function antigen-2; CD2 antigen (p50),
                     sheep red blood cell receptor; T-cell surface antigen CD2;
                     LFA-3 receptor; rosette receptor; erythrocyte receptor;
                     T-cell surface antigen T11/Leu-5"
                     /calculated_mol_wt=36886
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2580
     mat_peptide     25..351
                     /product="T-cell surface antigen CD2. /id=PRO_0000014600"
                     /note="propagated from UniProtKB/Swiss-Prot (P06729.2)"
                     /calculated_mol_wt=36886
     Region          29..127
                     /region_name="IgV_CD2_like_N"
                     /note="N-terminal immunoglobulin (Ig)-like domain of
                     T-cell surface antigen CD2, and similar domains; cd05775"
                     /db_xref="CDD:409431"
     Region          29..45
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409431"
     Region          29..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409431"
     Region          34..36
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409431"
     Region          39..46
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409431"
     Region          46..55
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409431"
     Region          56..61
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409431"
     Region          56..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409431"
     Region          61..75
                     /region_name="CD58 binding region 1.
                     /evidence=ECO:0000269|PubMed:2444890"
                     /note="propagated from UniProtKB/Swiss-Prot (P06729.2)"
     Region          62..78
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409431"
     Region          65..72
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409431"
     Region          75..78
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409431"
     Region          83..109
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409431"
     Region          83..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409431"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7994575,
                     ECO:0007744|PDB:1GYA, ECO:0007744|PDB:1HNF; propagated
                     from UniProtKB/Swiss-Prot (P06729.2)"
     Region          90..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409431"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409431"
     Region          106..120
                     /region_name="CD58 binding region 2.
                     /evidence=ECO:0000269|PubMed:2444890"
                     /note="propagated from UniProtKB/Swiss-Prot (P06729.2)"
     Region          110..118
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409431"
     Region          119..126
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409431"
     Region          119..125
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409431"
     Region          135..205
                     /region_name="C2-set"
                     /note="Immunoglobulin C2-set domain; pfam05790"
                     /db_xref="CDD:399065"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7994575,
                     ECO:0007744|PDB:1HNF; propagated from UniProtKB/Swiss-Prot
                     (P06729.2)"
     Site            150
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7994575,
                     ECO:0007744|PDB:1HNF; propagated from UniProtKB/Swiss-Prot
                     (P06729.2)"
     Site            210..235
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P06729.2)"
     Region          237..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06729.2)"
     Region          <265..>338
                     /region_name="Amelogenin"
                     /note="Amelogenins, cell adhesion proteins, play a role in
                     the biomineralisation of teeth; smart00818"
                     /db_xref="CDD:197891"
     CDS             1..351
                     /gene="CD2"
                     /gene_synonym="LFA-2; SRBC; T11"
                     /coded_by="NM_001767.5:64..1119"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS889.1"
                     /db_xref="GeneID:914"
                     /db_xref="HGNC:HGNC:1639"
                     /db_xref="MIM:186990"
ORIGIN      
        1 msfpckfvas fllifnvssk gavskeitna letwgalgqd inldipsfqm sddiddikwe
       61 ktsdkkkiaq frkeketfke kdtyklfkng tlkikhlktd dqdiykvsiy dtkgknvlek
      121 ifdlkiqerv skpkiswtci nttltcevmn gtdpelnlyq dgkhlklsqr vithkwttsl
      181 sakfkctagn kvskessvep vscpekgldi yliigicggg sllmvfvall vfyitkrkkq
      241 rsrrndeele trahrvatee rgrkphqipa stpqnpatsq hpppppghrs qapshrpppp
      301 ghrvqhqpqk rppapsgtqv hqqkgpplpr prvqpkpphg aaenslspss n
//
LOCUS       NP_055620                607 aa            linear   PRI 20-NOV-2025
DEFINITION  EPM2A-interacting protein 1 [Homo sapiens].
ACCESSION   NP_055620
VERSION     NP_055620.1
DBSOURCE    REFSEQ: accession NM_014805.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 607)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 607)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 607)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 607)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 607)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 607)
  AUTHORS   Perera,S., Mrkonjic,M., Rawson,J.B. and Bapat,B.
  TITLE     Functional effects of the MLH1-93G>A polymorphism on MLH1/EPM2AIP1
            promoter activity
  JOURNAL   Oncol Rep 25 (3), 809-815 (2011)
   PUBMED   21206982
  REMARK    GeneRIF: The -93G>A polymorphism modifies the efficiency of
            MLH1/EPM2AIP1 transcription.
REFERENCE   7  (residues 1 to 607)
  AUTHORS   Walker,L.C., Waddell,N., Ten Haaf,A., Grimmond,S. and Spurdle,A.B.
  CONSRTM   kConFab Investigators
  TITLE     Use of expression data and the CGEMS genome-wide breast cancer
            association study to identify genes that may modify risk in BRCA1/2
            mutation carriers
  JOURNAL   Breast Cancer Res Treat 112 (2), 229-236 (2008)
   PUBMED   18095154
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   8  (residues 1 to 607)
  AUTHORS   Chan,E.M., Young,E.J., Ianzano,L., Munteanu,I., Zhao,X.,
            Christopoulos,C.C., Avanzini,G., Elia,M., Ackerley,C.A.,
            Jovic,N.J., Bohlega,S., Andermann,E., Rouleau,G.A.,
            Delgado-Escueta,A.V., Minassian,B.A. and Scherer,S.W.
  TITLE     Mutations in NHLRC1 cause progressive myoclonus epilepsy
  JOURNAL   Nat Genet 35 (2), 125-127 (2003)
   PUBMED   12958597
REFERENCE   9  (residues 1 to 607)
  AUTHORS   Ianzano,L., Zhao,X.C., Minassian,B.A. and Scherer,S.W.
  TITLE     Identification of a novel protein interacting with laforin, the
            EPM2a progressive myoclonus epilepsy gene product
  JOURNAL   Genomics 81 (6), 579-587 (2003)
   PUBMED   12782127
  REMARK    GeneRIF: The EPM2AIP1 gene was identified and characterized in a
            screen for laforin-interacting proteins with a human brain cDNA
            library; the specificity of the interaction was confirmed;
            subcellular colocalization of laforin and EPM2AIP1 protein was
            demonstrated
REFERENCE   10 (residues 1 to 607)
  AUTHORS   Cai,S., Han,H.J. and Kohwi-Shigematsu,T.
  TITLE     Tissue-specific nuclear architecture and gene expression regulated
            by SATB1
  JOURNAL   Nat Genet 34 (1), 42-51 (2003)
   PUBMED   12692553
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY178832.1 and AC011816.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The EPM2A gene, which encodes laforin, is mutated in an
            autosomal recessive form of adolescent progressive myoclonus
            epilepsy. The protein encoded by this gene binds to laforin, but
            its function is not known. This gene is intronless. [provided by
            RefSeq, Oct 2008].
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803615.57690.1,
                                        SRR7346977.1761328.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322716.8/ ENSP00000406027.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..607
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..607
                     /product="EPM2A-interacting protein 1"
                     /note="laforin-interacting protein; EPM2A (laforin)
                     interacting protein 1"
                     /calculated_mol_wt=70239
     Region          20..79
                     /region_name="DUF4371"
                     /note="Domain of unknown function (DUF4371); cl46273"
                     /db_xref="CDD:480613"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q7L775.1)"
     CDS             1..607
                     /gene="EPM2AIP1"
                     /coded_by="NM_014805.4:55..1878"
                     /db_xref="CCDS:CCDS46790.1"
                     /db_xref="GeneID:9852"
                     /db_xref="HGNC:HGNC:19735"
                     /db_xref="MIM:607911"
ORIGIN      
        1 mwmtpkrskm evdealvfrp ewtqrylvve ppegdgalcl vcrrlivatr erdvrrhyea
       61 eheyyeryva dgeraalver lrqgdlpvas ftpeeraara glglcrllal kgrgwgegdf
      121 vyqcmevllr evlpehvsvl qgvdlspdit rqrilsidrn lrnqlfnrar dfkayslald
      181 dqafvayeny llvfirgvgp elevqedllt iinlthhfsv galmsailes lqtaglslqr
      241 mvglttthtl rmigensglv symrekavsp ncwnvihysg flhlellssy dvdvnqiint
      301 isewivlikt rgvrrpefqt lltesesehg ervngrclnn wlrrgktlkl ifslrkemea
      361 flvsvgattv hfsdkqwlcd fgflvdimeh lrelseelrv skvfaaaafd hictfevkln
      421 lfqrhieekn ltdfpalrev vdelkqqnke dekifdpdry qmvicrlqke ferhfkdlrf
      481 ikkdlelfsn pfnfkpeyap isvrveltkl qantnlwney rikdlgqfya glsaesypii
      541 kgvackvasl fdsnqiceka fsyltrnqht lsqpltdehl qalfrvatte mepgwddlvr
      601 ernesnp
//
LOCUS       NP_003085                 92 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein E isoform 1 [Homo sapiens].
ACCESSION   NP_003085
VERSION     NP_003085.1
DBSOURCE    REFSEQ: accession NM_003094.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Wu,Q., Liao,R., Miao,C., Hasnat,M., Li,L., Sun,L., Wang,X.,
            Yuan,Z., Jiang,Z., Zhang,L. and Yu,Q.
  TITLE     Oncofetal SNRPE promotes HCC tumorigenesis by regulating the FGFR4
            expression through alternative splicing
  JOURNAL   Br J Cancer 131 (1), 77-89 (2024)
   PUBMED   38796598
  REMARK    GeneRIF: Oncofetal SNRPE promotes HCC tumorigenesis by regulating
            the FGFR4 expression through alternative splicing.
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Fautsch,M.P. and Wieben,E.D.
  TITLE     Transcriptional regulation of the small nuclear ribonucleoprotein E
            protein gene. Identification of cis-acting sequences with homology
            to genes encoding ribosomal proteins
  JOURNAL   J Biol Chem 266 (34), 23288-23295 (1991)
   PUBMED   1835977
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Neiswanger,K., Stanford,D.R., Sparkes,R.S., Nishimura,D.,
            Mohandas,T., Klisak,I., Heinzmann,C. and Wieben,E.D.
  TITLE     Assignment of the gene for the small nuclear ribonucleoprotein E
            (SNRPE) to human chromosome 1q25-q43
  JOURNAL   Genomics 7 (4), 503-508 (1990)
   PUBMED   2143747
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Sauterer,R.A., Goyal,A. and Zieve,G.W.
  TITLE     Cytoplasmic assembly of small nuclear ribonucleoprotein particles
            from 6 S and 20 S RNA-free intermediates in L929 mouse fibroblasts
  JOURNAL   J Biol Chem 265 (2), 1048-1058 (1990)
   PUBMED   1688550
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Feeney,R.J., Sauterer,R.A., Feeney,J.L. and Zieve,G.W.
  TITLE     Cytoplasmic assembly and nuclear accumulation of mature small
            nuclear ribonucleoprotein particles
  JOURNAL   J Biol Chem 264 (10), 5776-5783 (1989)
   PUBMED   2522439
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Stanford,D.R., Rohleder,A., Neiswanger,K. and Wieben,E.D.
  TITLE     DNA sequence of a human Sm autoimmune antigen. The multigene family
            contains a processed pseudogene
  JOURNAL   J Biol Chem 262 (21), 9931-9934 (1987)
   PUBMED   2440864
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114402.2 and AC118554.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a core component of U
            small nuclear ribonucleoproteins, which are key components of the
            pre-mRNA processing spliceosome. The encoded protein plays a role
            in the 3' end processing of histone transcripts. This protein is
            one of the targets in the autoimmune disease systemic lupus
            erythematosus, and mutations in this gene have been associated with
            hypotrichosis. Several pseudogenes of this gene have been
            identified. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC090951.1, SRR18074967.497976.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000414487.7/
                                                  ENSP00000400591.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..92
                     /product="small nuclear ribonucleoprotein E isoform 1"
                     /note="sm protein E"
                     /calculated_mol_wt=10672
     Region          11..89
                     /region_name="Sm_E"
                     /note="Sm protein E; cd01718"
                     /db_xref="CDD:212465"
     Site            order(24,36,38,41,48..51,55,63,72,74,76..80,83..89)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212465"
     Site            order(33..39,41..53,55..59)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212465"
     Site            order(51,53..55,80,82)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212465"
     Site            76..87
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212465"
     CDS             1..92
                     /gene="SNRPE"
                     /gene_synonym="HYPT11; Sm-E; SME; snRNP-E"
                     /coded_by="NM_003094.4:62..340"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30979.1"
                     /db_xref="GeneID:6635"
                     /db_xref="HGNC:HGNC:11161"
                     /db_xref="MIM:128260"
ORIGIN      
        1 mayrgqgqkv qkvmvqpinl ifrylqnrsr iqvwlyeqvn mriegciigf deymnlvldd
       61 aeeihsktks rkqlgrimlk gdnitllqsv sn
//
LOCUS       NP_001006635             881 aa            linear   PRI 20-NOV-2025
DEFINITION  rho GTPase-activating protein 17 isoform 1 [Homo sapiens].
ACCESSION   NP_001006635
VERSION     NP_001006635.1
DBSOURCE    REFSEQ: accession NM_001006634.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Kreider-Letterman,G., Castillo,A., Mahlandt,E.K., Goedhart,J.,
            Rabino,A., Goicoechea,S. and Garcia-Mata,R.
  TITLE     ARHGAP17 regulates the spatiotemporal activity of Cdc42 at
            invadopodia
  JOURNAL   J Cell Biol 222 (2) (2023)
   PUBMED   36571786
  REMARK    GeneRIF: ARHGAP17 regulates the spatiotemporal activity of Cdc42 at
            invadopodia.
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Pan,S.L., Deng,Y.Y., Fu,J., Zhang,Y.H., Zhang,Z.J. and Qin,X.J.
  TITLE     ARHGAP17 enhances 5-Fluorouracil-induced apoptosis in colon cancer
            cells by suppressing Rac1
  JOURNAL   Neoplasma 69 (3), 640-647 (2022)
   PUBMED   35293764
  REMARK    GeneRIF: ARHGAP17 enhances 5-Fluorouracil-induced apoptosis in
            colon cancer cells by suppressing Rac1.
REFERENCE   5  (residues 1 to 881)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 881)
  AUTHORS   Yi,C., Troutman,S., Fera,D., Stemmer-Rachamimov,A., Avila,J.L.,
            Christian,N., Persson,N.L., Shimono,A., Speicher,D.W.,
            Marmorstein,R., Holmgren,L. and Kissil,J.L.
  TITLE     A tight junction-associated Merlin-angiomotin complex mediates
            Merlin's regulation of mitogenic signaling and tumor suppressive
            functions
  JOURNAL   Cancer Cell 19 (4), 527-540 (2011)
   PUBMED   21481793
REFERENCE   7  (residues 1 to 881)
  AUTHORS   Wells,C.D., Fawcett,J.P., Traweger,A., Yamanaka,Y., Goudreault,M.,
            Elder,K., Kulkarni,S., Gish,G., Virag,C., Lim,C., Colwill,K.,
            Starostine,A., Metalnikov,P. and Pawson,T.
  TITLE     A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
            proteins in epithelial cells
  JOURNAL   Cell 125 (3), 535-548 (2006)
   PUBMED   16678097
  REMARK    GeneRIF: We propose that Rich1 and Amot maintain TJ integrity by
            the coordinate regulation of Cdc42 and by linking specific
            components of the TJ to intracellular protein trafficking.
REFERENCE   8  (residues 1 to 881)
  AUTHORS   Richnau,N. and Aspenstrom,P.
  TITLE     Rich, a rho GTPase-activating protein domain-containing protein
            involved in signaling by Cdc42 and Rac1
  JOURNAL   J Biol Chem 276 (37), 35060-35070 (2001)
   PUBMED   11431473
REFERENCE   9  (residues 1 to 881)
  AUTHORS   Reczek,D. and Bretscher,A.
  TITLE     Identification of EPI64, a TBC/rabGAP domain-containing microvillar
            protein that binds to the first PDZ domain of EBP50 and E3KARP
  JOURNAL   J Cell Biol 153 (1), 191-206 (2001)
   PUBMED   11285285
REFERENCE   10 (residues 1 to 881)
  AUTHORS   Harada,A., Furuta,B., Takeuchi,K., Itakura,M., Takahashi,M. and
            Umeda,M.
  TITLE     Nadrin, a novel neuron-specific GTPase-activating protein involved
            in regulated exocytosis
  JOURNAL   J Biol Chem 275 (47), 36885-36891 (2000)
   PUBMED   10967100
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU187683.1 and BC080195.1.
            
            Summary: RICH1 is a GTPase-activating protein (GAP). GAPs stimulate
            the intrinsic GTP hydrolysis of small G proteins, such as RHOA (MIM
            165390), RAC1 (MIM 602048), and CDC42 (MIM 116952).[supplied by
            OMIM, Apr 2004].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC080195.1, AK291691.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000289968.11/ ENSP00000289968.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..881
                     /product="rho GTPase-activating protein 17 isoform 1"
                     /note="RhoGAP interacting with CIP4 homologs 1;
                     neuron-associated developmentally regulated protein;
                     rho-type GTPase-activating protein 17"
                     /calculated_mol_wt=95306
     Region          13..257
                     /region_name="BAR_Rich1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of RhoGAP
                     interacting with CIP4 homologs protein 1; cd07618"
                     /db_xref="CDD:153302"
     Site            order(21,24..25,32,34..35,38..39,41..42,70..71,73..74,
                     77..78,80..81,84,97,100..101,199,202..203,205,209,
                     212..213,215..216,219..220,223..224,226..227,230..231,
                     233..234)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153302"
     Region          246..446
                     /region_name="RhoGAP_nadrin"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain of Nadrin-like proteins. Nadrin,
                     also named Rich-1, has been shown to be involved in the
                     regulation of Ca2+-dependent exocytosis in neurons and
                     recently has been implicated in...; cd04386"
                     /db_xref="CDD:239851"
     Site            order(288,325,329,398,401..402,428)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239851"
     Site            288
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00172; propagated
                     from UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            288
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239851"
     Region          459..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Region          511..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68EM7.1)"
     Region          <520..789
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <522..>631
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            679
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Region          753..766
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UIA2; propagated from
                     UniProtKB/Swiss-Prot (Q68EM7.1)"
     CDS             1..881
                     /gene="ARHGAP17"
                     /gene_synonym="MST066; MST110; MSTP038; MSTP066; MSTP110;
                     NADRIN; PP367; PP4534; RICH-1; RICH1; WBP15"
                     /coded_by="NM_001006634.3:109..2754"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32409.1"
                     /db_xref="GeneID:55114"
                     /db_xref="HGNC:HGNC:18239"
                     /db_xref="MIM:608293"
ORIGIN      
        1 mkkqfnrmkq lanqtvgrae ktevlsedll qierrldtvr sichhshkrl vacfqgqhgt
       61 daerrhkklp ltalaqnmqe astqledsll gkmletcgda enqlalelsq hevfvekeiv
      121 dplygiaeve ipniqkqrkq larlvldwds vrarwnqahk ssgtnfqglp skidtlkeem
      181 deagnkveqc kdqlaadmyn fmakegeygk ffvtlleaqa dyhrkalavl ektlpemrah
      241 qdkwaekpaf gtpleehlkr sgreialpie acvmllletg mkeeglfrig agasklkklk
      301 aaldcstshl defysdphav agalksylre lpeplmtfnl yeewtqvasv qdqdkklqdl
      361 wrtcqklppq nfvnfrylik flaklaqtsd vnkmtpsnia ivlgpnllwa rnegtlaema
      421 aatsvhvvav iepiiqhadw ffpeevefnv seafvplttp ssnhsfhtgn dsdsgtlerk
      481 rpasmavmeg dlvkkesfgv klmdfqahrr ggtlnrkhis pafqpplppt dgstvvpagp
      541 epppqssrae sssgggtvps sagileqgps pgdgsppkpk dpvsaavpap grnnsqiasg
      601 qnqpqaaags hqlsmgqphn aagpsphtlr ravkkpapap pkpgnpppgh pggqsssgts
      661 qhppslspkp ptrspspptq htgqppgqps apsqlsaprr yssslspiqa pnhpppqppt
      721 qatplmhtkp nsqgppnpma lpsehgleqp shtppqtptp pstpplgkqn pslpapqtla
      781 ggnpetaqph agtlprprpv pkprnrpsvp pppqppgvhs agdssltnta ptaskivtds
      841 nsrvsephrs ifpemhsdsa skdvpgrill didndtesta l
//
LOCUS       NP_001180201             500 aa            linear   PRI 20-NOV-2025
DEFINITION  retinoblastoma-binding protein 5 isoform 2 [Homo sapiens].
ACCESSION   NP_001180201
VERSION     NP_001180201.1
DBSOURCE    REFSEQ: accession NM_001193272.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Patel,A., Dharmarajan,V., Vought,V.E. and Cosgrove,M.S.
  TITLE     On the mechanism of multiple lysine methylation by the human mixed
            lineage leukemia protein-1 (MLL1) core complex
  JOURNAL   J Biol Chem 284 (36), 24242-24256 (2009)
   PUBMED   19556245
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Southall,S.M., Wong,P.S., Odho,Z., Roe,S.M. and Wilson,J.R.
  TITLE     Structural basis for the requirement of additional factors for MLL1
            SET domain activity and recognition of epigenetic marks
  JOURNAL   Mol Cell 33 (2), 181-191 (2009)
   PUBMED   19187761
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Scacheri,P.C., Davis,S., Odom,D.T., Crawford,G.E., Perkins,S.,
            Halawi,M.J., Agarwal,S.K., Marx,S.J., Spiegel,A.M., Meltzer,P.S.
            and Collins,F.S.
  TITLE     Genome-wide analysis of menin binding provides insights into MEN1
            tumorigenesis
  JOURNAL   PLoS Genet 2 (4), e51 (2006)
   PUBMED   16604156
  REMARK    GeneRIF: analysis of menin's role as a tumor suppressor and binding
            sites of Rbbp5 and MLL1
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Saijo,M., Sakai,Y., Kishino,T., Niikawa,N., Matsuura,Y., Morino,K.,
            Tamai,K. and Taya,Y.
  TITLE     Molecular cloning of a human protein that binds to the
            retinoblastoma protein and chromosomal mapping
  JOURNAL   Genomics 27 (3), 511-519 (1995)
   PUBMED   7558034
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA797022.1, AK290137.1,
            BC037284.2, AL583832.14 and BQ020418.1.
            
            Summary: This gene encodes a ubiquitously expressed nuclear protein
            which belongs to a highly conserved subfamily of WD-repeat
            proteins. The encoded protein binds directly to retinoblastoma
            protein, which regulates cell proliferation. It interacts
            preferentially with the underphosphorylated retinoblastoma protein
            via the E1A-binding pocket B. Three alternatively spliced
            transcript variants that encode different protein isoforms have
            been described for this gene. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (2) uses a different splice site
            in the 3' coding region, compared to variant 1. The resulting
            protein (isoform 2) is shorter when it is compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037284.2, SRR14243140.7754638.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..500
                     /product="retinoblastoma-binding protein 5 isoform 2"
                     /note="SWD1, Set1c WD40 repeat protein, homolog; RBBP-5;
                     retinoblastoma-binding protein RBQ-3;
                     retinoblastoma-binding protein 5"
                     /calculated_mol_wt=54941
     Region          22..63
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          29..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <31..321
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          64..103
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          70..106
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          111..146
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          154..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          196..235
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          201..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..291
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7558034; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          254..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          293..331
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          298..321
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..366
                     /region_name="Interaction with ASH2L.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          344..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          371..380
                     /region_name="Interaction with WDR5.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     CDS             1..500
                     /gene="RBBP5"
                     /gene_synonym="RBQ3; SWD1"
                     /coded_by="NM_001193272.2:106..1608"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53463.1"
                     /db_xref="GeneID:5929"
                     /db_xref="HGNC:HGNC:9888"
                     /db_xref="MIM:600697"
ORIGIN      
        1 mnlellesfg qnypeeadgt ldcismaltc tfnrwgtlla vgcndgrivi wdfltrgiak
       61 iisahihpvc slcwsrdghk lvsastdniv sqwdvlsgdc dqrfrfpspi lkvqyhprdq
      121 nkvlvcpmks apvmltlsds khvvlpvddd sdlnvvasfd rrgeyiytgn akgkilvlkt
      181 dsqdlvasfr vttgtsntta iksiefarkg scflintadr iirvydgrei ltcgrdgepe
      241 pmqklqdlvn rtpwkkccfs gdgeyivags arqhalyiwe ksignlvkil hgtrgellld
      301 vawhpvrpii asissgvvsi waqnqvenws afapdfkeld enveyeeres efdiededks
      361 epeqtgadaa edeevdvtsv dpiaafcssd eeledskall ylpiapeved peenpygppp
      421 davqtslmde gassekkrqs sadgsqppkk kpkttnielq gvpndevhpl lgvkgdgksk
      481 kkqagrpkgs kaggaisell
//
LOCUS       NP_060947                417 aa            linear   PRI 20-NOV-2025
DEFINITION  actin-related protein 10 [Homo sapiens].
ACCESSION   NP_060947
VERSION     NP_060947.1
DBSOURCE    REFSEQ: accession NM_018477.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF220190.1, AL132989.5 and CB135721.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.656353.1,
                                           SRR1803615.92250.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254286.9/ ENSP00000254286.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..417
                     /product="actin-related protein 10"
                     /note="actin-related protein 11; actin related protein 10
                     homolog"
                     /calculated_mol_wt=46176
     Region          16..390
                     /region_name="ASKHA_NBD_Arp10"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein 10 (Arp10) and similar proteins; cd10207"
                     /db_xref="CDD:466813"
     CDS             1..417
                     /gene="ACTR10"
                     /gene_synonym="ACTR11; Arp10; Arp11; HARP11"
                     /coded_by="NM_018477.3:70..1323"
                     /db_xref="CCDS:CCDS32090.1"
                     /db_xref="GeneID:55860"
                     /db_xref="HGNC:HGNC:17372"
                     /db_xref="MIM:619731"
ORIGIN      
        1 mplyeglgsg gektavvidl geaftkcgfa getgprciip svikragmpk pvrvvqynin
       61 teelysylke fihilyfrhl lvnprdrrvv iiesvlcpsh fretltrvlf kyfevpsvll
      121 apshlmallt lginsamvld cgyreslvlp iyegipvlnc wgalplggka lhkeletqll
      181 eqctvdtsva keqslpsvmg svpegvledi kartcfvsdl krglkiqaak fnidgnnerp
      241 spppnvdypl dgekilhilg sirdsvveil feqdneeqsv atlildsliq cpidtrkqla
      301 enlvviggts mlpgflhrll aeirylvekp kykkalgtkt frihtppaka ncvawlggai
      361 fgalqdilgs rsvskeyynq tgripdwcsl nnpplemmfd vgktqpplmk rafstek
//
LOCUS       NP_001307658             865 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger and BTB domain-containing protein 21 isoform S [Homo
            sapiens].
ACCESSION   NP_001307658 XP_005261180
VERSION     NP_001307658.1
DBSOURCE    REFSEQ: accession NM_001320729.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Heckerman,D., Traynor,B.J., Picca,A., Calvani,R., Marzetti,E.,
            Hernandez,D., Nalls,M., Arepali,S., Ferrucci,L. and Landi,F.
  TITLE     Genetic variants associated with physical performance and
            anthropometry in old age: a genome-wide association study in the
            ilSIRENTE cohort
  JOURNAL   Sci Rep 7 (1), 15879 (2017)
   PUBMED   29158487
  REMARK    GeneRIF: Genotyping was accomplished on Infinium Human610-QUAD
            version 1. In the ilSIRENTE population, genetic variants in ZNF295
            and C2CD2 (rs928874 and rs1788355) on chromosome 21q22.3, were
            significantly associated with the 4-meter gait speed
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 865)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   7  (residues 1 to 865)
  AUTHORS   Wang,J., Kudoh,J., Takayanagi,A. and Shimizu,N.
  TITLE     Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is
            directly associated with ZFP161
  JOURNAL   Biochem Biophys Res Commun 327 (2), 615-627 (2005)
   PUBMED   15629158
  REMARK    GeneRIF: ZNF295 may be involved in the bi-directional control of
            gene expression in concert with ZFP161
REFERENCE   8  (residues 1 to 865)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 865)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 865)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP230048.1, BC063290.1 and AB041015.1.
            
            On Mar 4, 2016 this sequence version replaced XP_005261180.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            lacks an in-frame segment in the coding region compared to variant
            1. Variants 3 and 4 encode isoform S, which is shorter than isoform
            L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.260303.1,
                                           SRR1660803.95395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162946 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..865
                     /product="zinc finger and BTB domain-containing protein 21
                     isoform S"
                     /note="zinc finger and BTB domain-containing protein 21;
                     zinc finger protein 295"
                     /calculated_mol_wt=95677
     Region          12..123
                     /region_name="BTB_POZ_ZBTB21_ZNF295"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 21 (ZBTB21); cd18209"
                     /db_xref="CDD:349518"
     Region          545..572
                     /region_name="zf_C2H2_6"
                     /note="Zinc Finger domain; pfam18450"
                     /db_xref="CDD:408245"
     Region          710..730
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(715,717,719,721..722,725..726,729,743,745..747,
                     753..754,758)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          738..759
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          842..864
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     CDS             1..865
                     /gene="ZBTB21"
                     /gene_synonym="ZNF295"
                     /coded_by="NM_001320729.2:123..2720"
                     /note="isoform S is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS42934.1"
                     /db_xref="GeneID:49854"
                     /db_xref="HGNC:HGNC:13083"
                     /db_xref="MIM:616485"
ORIGIN      
        1 megllhyinp ahaisllsal neerlkgqlc dvllivgdqk frahknvlaa sseyfqslft
       61 nkenesqtvf qldfcepdaf dnvlnyiyss slfvekssla avqelgyslg isfltnivsk
      121 tpqapfptcp nrkkvfvedd enssqkrsvi vcqsrneaqg ktvsqnqpdv shtsrpspsi
      181 avkantnkph vpkpieplhn lsltekswpk dssvvyaksl ehsgslddpn rislvkrnav
      241 lpskplqdre amddkpgvsg qlpkgkalel alkrprppvl svcsssetpy llketnkgng
      301 qgedrnllyy sklglvipss gsgsgnqsid rsgplvksll rrslsmdsqv pvyspsidlk
      361 ssqgsssvss dapgnvlcal sqksslkdcs ektalddrpq vlqphrlrsf sasqstdreg
      421 aspvtevrik tepssplsdp sdiirvtvgd aattaaasss svtrdlslkt eddqkdmsrl
      481 pakrrfqadr rlpfkklkvn ehgspvsedn feegssptll dadfpdsdln kdefeqgshe
      541 rlcrnaavcp ycslrffspe lkqeheskce ykkltclecm rtfkssfsiw rhqvevhnqn
      601 nmaptenfsl pvldhngdvt gssrpqsqpe pnkvnhivtt kddnvfsdss eqvnfdseds
      661 sclpedlsls kqlkiqvkee pveeaeeeap eastapkeag pskeaslwpc ekcgkmftvh
      721 kqlerhqell csvkpfichv cnkafrtnfr lwshfqshms qaseesahke sevcpvptns
      781 psppplpppp plpkiqplep dsptglsenp tpateklfvp qesdtlfyha pplsaitfkr
      841 qfmcklchrt fktafslwsh eqthn
//
LOCUS       NP_056943                376 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription initiation factor IIA subunit 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_056943
VERSION     NP_056943.1
DBSOURCE    REFSEQ: accession NM_015859.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 376)
  AUTHORS   DeJong,J., Bernstein,R. and Roeder,R.G.
  TITLE     Human general transcription factor TFIIA: characterization of a
            cDNA encoding the small subunit and requirement for basal and
            activated transcription
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3313-3317 (1995)
   PUBMED   7724559
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Ozer,J., Moore,P.A., Bolden,A.H., Lee,A., Rosen,C.A. and
            Lieberman,P.M.
  TITLE     Molecular cloning of the small (gamma) subunit of human TFIIA
            reveals functions critical for activated transcription
  JOURNAL   Genes Dev 8 (19), 2324-2335 (1994)
   PUBMED   7958899
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Ha,I., Lane,W.S. and Reinberg,D.
  TITLE     Cloning of a human gene encoding the general transcription
            initiation factor IIB
  JOURNAL   Nature 352 (6337), 689-695 (1991)
   PUBMED   1876184
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136040.5, BC050703.1 and D14887.1.
            
            Summary: Accurate transcription initiation on TATA-containing class
            II genes involves the ordered assembly of RNA polymerase II
            (POLR2A; MIM 180660) and several general initiation factors
            (summarized by DeJong and Roeder, 1993 [PubMed 8224848]). One of
            these factors is TFIIA, which when purified from HeLa extracts
            consists of 35-, 19-, and 12-kD subunits.[supplied by OMIM, Jul
            2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.220546.1,
                                           SRR14038192.905847.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000553612.6/ ENSP00000452454.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.1"
     Protein         1..376
                     /product="transcription initiation factor IIA subunit 1
                     isoform 1"
                     /note="glucose regulated protein, 58kD pseudogene; general
                     transcription factor IIA, 1, 19/37kDa; TFIIA alpha/beta
                     subunits; transcription initiation factor IIA subunit 1;
                     general transcription factor IIA 1; transcription
                     initiation factor TFIIA 42 kDa subunit"
                     /calculated_mol_wt=41383
     mat_peptide     2..274
                     /product="Transcription initiation factor IIA alpha chain.
                     /id=PRO_0000042593"
                     /note="propagated from UniProtKB/Swiss-Prot (P52655.1)"
                     /calculated_mol_wt=29631
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     Region          13..376
                     /region_name="TFIIA"
                     /note="Transcription factor IIA, alpha/beta subunit;
                     pfam03153"
                     /db_xref="CDD:460829"
     Region          69..107
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52655.1)"
     Region          247..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52655.1)"
     Region          274..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52655.1)"
     Site            274..275
                     /site_type="cleavage"
                     /note="Cleavage, by TASP1; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     mat_peptide     275..376
                     /product="Transcription initiation factor IIA beta chain.
                     /id=PRO_0000042594"
                     /note="propagated from UniProtKB/Swiss-Prot (P52655.1)"
                     /calculated_mol_wt=11770
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TAF1.
                     /evidence=ECO:0000269|PubMed:11278496; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TAF1.
                     /evidence=ECO:0000269|PubMed:11278496; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TAF1.
                     /evidence=ECO:0000269|PubMed:11278496,
                     ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TAF1.
                     /evidence=ECO:0000269|PubMed:11278496,
                     ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P52655.1)"
     CDS             1..376
                     /gene="GTF2A1"
                     /gene_synonym="TF2A1; TFIIA; TFIIA-42; TFIIAL"
                     /coded_by="NM_015859.4:442..1572"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9873.1"
                     /db_xref="GeneID:2957"
                     /db_xref="HGNC:HGNC:4646"
                     /db_xref="MIM:600520"
ORIGIN      
        1 mansantntv pklyrsvied vindvrdifl ddgvdeqvlm elktlwenkl mqsravdgfh
       61 seeqqlllqv qqqhqpqqqq hhhhhhhqqa qpqqtvpqqa qtqqvlipas qqatapqviv
      121 pdskliqhmn asnmsaaata atlalpagvt pvqqiltnsg qllqvvraan gaqyifqpqq
      181 svvlqqqvip qmqpggvqap viqqvlaplp ggispqtgvi iqpqqilftg nktqvipttv
      241 aaptpaqaqi tatgqqqpqa qpaqtqaplv lqvdgtgdts seededeeed ydddeeedke
      301 kdgaedgqve eeplnseddv sdeegqelfd tenvvvcqyd kihrsknkwk fhlkdgimnl
      361 ngrdyifska igdaew
//
LOCUS       NP_001248329             118 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 9 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001248329
VERSION     NP_001248329.1
DBSOURCE    REFSEQ: accession NM_001261400.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Su,Y., Meng,L., Ge,C., Liu,Y., Zhang,C., Yang,Y., Tian,W. and
            Tian,H.
  TITLE     PSMD9 promotes the malignant progression of hepatocellular
            carcinoma by interacting with c-Cbl to activate EGFR signaling and
            recycling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 142 (2024)
   PUBMED   38745188
  REMARK    GeneRIF: PSMD9 promotes the malignant progression of hepatocellular
            carcinoma by interacting with c-Cbl to activate EGFR signaling and
            recycling.
            Erratum:[J Exp Clin Cancer Res. 2024 Oct 18;43(1):287. doi:
            10.1186/s13046-024-03209-2. PMID: 39420369]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Li,Y., Liu,X., Zhao,F., Zhao,Z., Li,X., Wang,J., Huang,B. and
            Chen,A.
  TITLE     Comprehensive analysis of PSMD family members and validation of
            PSMD9 as a potential therapeutic target in human glioblastoma
  JOURNAL   CNS Neurosci Ther 30 (2), e14366 (2024)
   PUBMED   37485655
  REMARK    GeneRIF: Comprehensive analysis of PSMD family members and
            validation of PSMD9 as a potential therapeutic target in human
            glioblastoma.
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Christie,J., Anthony,C.M., Harish,M., Mudartha,D., Ud Din
            Farooqee,S.B. and Venkatraman,P.
  TITLE     The interaction network of the proteasome assembly chaperone PSMD9
            regulates proteostasis
  JOURNAL   FEBS J 290 (23), 5581-5604 (2023)
   PUBMED   37665644
  REMARK    GeneRIF: The interaction network of the proteasome assembly
            chaperone PSMD9 regulates proteostasis.
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Del Bosque-Plata,L., Amin,M. and Gragnoli,C.
  TITLE     PSMD9 is linked to T2D age of onset, years of isolated and combined
            insulin therapy, irregular menses, and hot flashes
  JOURNAL   Eur Rev Med Pharmacol Sci 26 (23), 8873-8878 (2022)
   PUBMED   36524506
  REMARK    GeneRIF: PSMD9 is linked to T2D age of onset, years of isolated and
            combined insulin therapy, irregular menses, and hot flashes.
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Watanabe,T.K., Saito,A., Suzuki,M., Fujiwara,T., Takahashi,E.,
            Slaughter,C.A., DeMartino,G.N., Hendil,K.B., Chung,C.H.,
            Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and characterization of a human proteasomal modulator
            subunit, p27 (PSMD9)
  JOURNAL   Genomics 50 (2), 241-250 (1998)
   PUBMED   9653651
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002383.2, CB111716.1,
            BU726372.1, KF459562.1 and AC069503.25.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. Three transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.64096.1,
                                           SRR1660807.268049.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..118
                     /product="26S proteasome non-ATPase regulatory subunit 9
                     isoform 2"
                     /note="proteasome 26S non-ATPase regulatory subunit 9;
                     homolog of rat Bridge 1; 26S proteasome regulatory subunit
                     p27; 26S proteasome non-ATPase regulatory subunit 9;
                     proteasome (prosome, macropain) 26S subunit, non-ATPase,
                     9"
                     /calculated_mol_wt=12922
     Region          23..>47
                     /region_name="Nas2_N"
                     /note="Nas2 N_terminal domain; pfam18265"
                     /db_xref="CDD:465689"
     Region          <45..>110
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
     CDS             1..118
                     /gene="PSMD9"
                     /gene_synonym="p27; Rpn4"
                     /coded_by="NM_001261400.3:68..424"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58284.1"
                     /db_xref="GeneID:5715"
                     /db_xref="HGNC:HGNC:9567"
                     /db_xref="MIM:603146"
ORIGIN      
        1 msdeearqsg gssqagvvtv sdvqelmrrk eeieaqikan ydvlesglqv ddeivefgsv
       61 ntqnfqslhn igsvvqhseg kplnvtvirr gekhqlrlvp trwagkgllg cniiplqr
//
LOCUS       NP_001158245             300 aa            linear   PRI 20-NOV-2025
DEFINITION  branched-chain-amino-acid aminotransferase, mitochondrial isoform b
            [Homo sapiens].
ACCESSION   NP_001158245
VERSION     NP_001158245.1
DBSOURCE    REFSEQ: accession NM_001164773.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Kang,Z.R., Jiang,S., Han,J.X., Gao,Y., Xie,Y., Chen,J., Liu,Q.,
            Yu,J., Zhao,X., Hong,J., Chen,H., Chen,Y.X., Chen,H. and Fang,J.Y.
  TITLE     Deficiency of BCAT2-mediated branched-chain amino acid catabolism
            promotes colorectal cancer development
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166941 (2024)
   PUBMED   37926361
  REMARK    GeneRIF: Deficiency of BCAT2-mediated branched-chain amino acid
            catabolism promotes colorectal cancer development.
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Tian,Y., Ma,J., Wang,H., Yi,X., Wang,H., Zhang,H., Guo,S., Yang,Y.,
            Zhang,B., Du,J., Shi,Q., Gao,T., Guo,W. and Li,C.
  TITLE     BCAT2 promotes melanoma progression by activating lipogenesis via
            the epigenetic regulation of FASN and ACLY expressions
  JOURNAL   Cell Mol Life Sci 80 (11), 315 (2023)
   PUBMED   37801083
  REMARK    GeneRIF: BCAT2 promotes melanoma progression by activating
            lipogenesis via the epigenetic regulation of FASN and ACLY
            expressions.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Yennawar,N., Dunbar,J., Conway,M., Hutson,S. and Farber,G.
  TITLE     The structure of human mitochondrial branched-chain
            aminotransferase
  JOURNAL   Acta Crystallogr D Biol Crystallogr 57 (Pt 4), 506-515 (2001)
   PUBMED   11264579
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Than,N.G., Sumegi,B., Than,G.N., Bellyei,S. and Bohn,H.
  TITLE     Molecular cloning and characterization of placental tissue protein
            18 (PP18a)/human mitochondrial branched-chain aminotransferase
            (BCATm) and its novel alternatively spliced PP18b variant
  JOURNAL   Placenta 22 (2-3), 235-243 (2001)
   PUBMED   11170829
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Bledsoe,R.K., Dawson,P.A. and Hutson,S.M.
  TITLE     Cloning of the rat and human mitochondrial branched chain
            aminotransferases (BCATm)
  JOURNAL   Biochim Biophys Acta 1339 (1), 9-13 (1997)
   PUBMED   9165094
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Eden,A., Simchen,G. and Benvenisty,N.
  TITLE     Two yeast homologs of ECA39, a target for c-Myc regulation, code
            for cytosolic and mitochondrial branched-chain amino acid
            aminotransferases
  JOURNAL   J Biol Chem 271 (34), 20242-20245 (1996)
   PUBMED   8702755
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Bohn,H. and Winckler,W.
  TITLE     Isolation and characterization of four new placental tissue
            proteins (PP18, PP19, PP20, PP21)
  JOURNAL   Arch Gynecol 236 (4), 235-242 (1985)
   PUBMED   3896163
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Naylor,S.L. and Shows,T.B.
  TITLE     Branched-chain aminotransferase deficiency in Chinese hamster cells
            complemented by two independent genes on human chromosomes 12 and
            19
  JOURNAL   Somatic Cell Genet 6 (5), 641-652 (1980)
   PUBMED   6933702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA129578.1 and AF268048.1.
            
            Summary: This gene encodes a branched chain aminotransferase found
            in mitochondria. The encoded protein forms a dimer that catalyzes
            the first step in the production of the branched chain amino acids
            leucine, isoleucine, and valine. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (b) lacks two alternate in-frame
            exons in the 5' coding region, compared to variant a. The resulting
            isoform (b), also known as PP18b, lacks an internal segment near
            the N-terminus, compared to isoform a, which disrupts the transit
            peptide. This isoform is found in the cytosol.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF268048.1, SRR14372080.4170103.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..300
                     /product="branched-chain-amino-acid aminotransferase,
                     mitochondrial isoform b"
                     /EC_number="2.6.1.42"
                     /note="branched chain aminotransferase 2, mitochondrial;
                     placental protein 18; branched chain amino-acid
                     transaminase 2, mitochondrial"
                     /calculated_mol_wt=33646
     Region          2..290
                     /region_name="BCAT_beta_family"
                     /note="Branched-chain aminotransferase catalyses the
                     transamination of the branched-chain amino acids leusine,
                     isoleucine and valine to their respective alpha-keto
                     acids, alpha-ketoisocaproate,
                     alpha-keto-beta-methylvalerate and alpha-ketoisovalerate.
                     The...; cd01557"
                     /db_xref="CDD:238798"
     Site            order(10,34,90,137,142,172,204..205,248)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:238798"
     Site            137
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238798"
     CDS             1..300
                     /gene="BCAT2"
                     /gene_synonym="BCAM; BCATM; BCT2; HVLI; PP18"
                     /coded_by="NM_001164773.2:23..925"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS54290.1"
                     /db_xref="GeneID:587"
                     /db_xref="HGNC:HGNC:977"
                     /db_xref="MIM:113530"
ORIGIN      
        1 maaaalgqlf egmkafkgkd qqvrlfrpwl nmdrmlrsam rlclpsfdkl ellecirrli
       61 evdkdwvpda agtslyvrpv lignepslgv sqptrallfv ilcpvgayfp ggsvtpvsll
      121 adpafirawv ggvgnyklgg nygptvlvqq ealkrgceqv lwlygpdhql tevgtmnifv
      181 ywthedgvle lvtpplngvi lpgvvrqsll dmaqtwgefr vvertitmkq llraleegrv
      241 revfgsgtac qvcpvhrily kdrnlhiptm engpelilrf qkelkeiqyg irahewmfpv
//
LOCUS       NP_001273555             282 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein with serine-rich domain 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001273555 XP_005255107
VERSION     NP_001273555.1
DBSOURCE    REFSEQ: accession NM_001286626.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Kumari,S., Adhikary,A. and Singh,K.K.
  TITLE     BioID proximity mapping reveals novel SAP18 interactions in the
            prespliceosomal complex
  JOURNAL   Biochem Biophys Res Commun 738, 150944 (2024)
   PUBMED   39522233
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Wang,X., Ling,R., Peng,Y., Qiu,W. and Chen,D.
  TITLE     RNPS1 stabilizes NAT10 protein to facilitate translation in cancer
            via tRNA ac4C modification
  JOURNAL   Int J Oral Sci 16 (1), 6 (2024)
   PUBMED   38246918
  REMARK    GeneRIF: RNPS1 stabilizes NAT10 protein to facilitate translation
            in cancer via tRNA ac[4]C modification.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Deka,B., Chandra,P., Yadav,P., Rehman,A., Kumari,S.,
            Kunnumakkara,A.B. and Singh,K.K.
  TITLE     RNPS1 functions as an oncogenic splicing factor in cervical cancer
            cells
  JOURNAL   IUBMB Life 75 (6), 514-529 (2023)
   PUBMED   36300671
  REMARK    GeneRIF: RNPS1 functions as an oncogenic splicing factor in
            cervical cancer cells.
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Mayeda,A., Badolato,J., Kobayashi,R., Zhang,M.Q., Gardiner,E.M. and
            Krainer,A.R.
  TITLE     Purification and characterization of human RNPS1: a general
            activator of pre-mRNA splicing
  JOURNAL   EMBO J 18 (16), 4560-4570 (1999)
   PUBMED   10449421
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Loyer,P., Trembley,J.H., Lahti,J.M. and Kidd,V.J.
  TITLE     The RNP protein, RNPS1, associates with specific isoforms of the
            p34cdc2-related PITSLRE protein kinase in vivo
  JOURNAL   J Cell Sci 111 (Pt 11), 1495-1506 (1998)
   PUBMED   9580558
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Burn,T.C., Connors,T.D., Van Raay,T.J., Dackowski,W.R.,
            Millholland,J.M., Klinger,K.W. and Landes,G.M.
  TITLE     Generation of a transcriptional map for a 700-kb region surrounding
            the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis
            type 2 (TSC2) disease genes on human chromosome 16p3.3
  JOURNAL   Genome Res 6 (6), 525-537 (1996)
   PUBMED   8828041
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Badolato,J., Gardiner,E., Morrison,N. and Eisman,J.
  TITLE     Identification and characterisation of a novel human RNA-binding
            protein
  JOURNAL   Gene 166 (2), 323-327 (1995)
   PUBMED   8543184
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316132.1 and BC108316.1.
            
            On Nov 8, 2013 this sequence version replaced XP_005255107.1.
            
            Summary: This gene encodes a protein that is part of a
            post-splicing multiprotein complex involved in both mRNA nuclear
            export and mRNA surveillance. mRNA surveillance detects exported
            mRNAs with truncated open reading frames and initiates
            nonsense-mediated mRNA decay (NMD). When translation ends upstream
            from the last exon-exon junction, this triggers NMD to degrade
            mRNAs containing premature stop codons. This protein binds to the
            mRNA and remains bound after nuclear export, acting as a
            nucleocytoplasmic shuttling protein. This protein contains many
            serine residues. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2013].
            
            Transcript Variant: This variant (4) lacks an alternate exon
            compared to variant 2. The resulting isoform (b) has a shorter and
            distinct N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.196475.1,
                                           SRR3476690.626707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..282
                     /product="RNA-binding protein with serine-rich domain 1
                     isoform b"
                     /note="SR protein; RNA-binding protein S1, serine-rich
                     domain; SR-related protein LDC2; RNA binding protein with
                     serine-rich domain"
                     /calculated_mol_wt=31578
     Region          140..213
                     /region_name="RRM_RNPS1"
                     /note="RNA recognition motif (RRM) found in RNA-binding
                     protein with serine-rich domain 1 (RNPS1) and similar
                     proteins; cd12365"
                     /db_xref="CDD:409800"
     Site            order(146..150,152..153,156..157,160..161,172,177..178,
                     198..208)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409800"
     CDS             1..282
                     /gene="RNPS1"
                     /gene_synonym="E5.1"
                     /coded_by="NM_001286626.2:71..919"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS66907.1"
                     /db_xref="GeneID:10921"
                     /db_xref="HGNC:HGNC:10080"
                     /db_xref="MIM:606447"
ORIGIN      
        1 mapsptkrkd rsdekskdrs kdkgatkess ekdrgrdktr krrsassgss strsrsssts
       61 ssgsststgs ssgsssssas srsgssstsr ssssssssgs pspsrrrhdn rrrsrskskp
      121 pkrdekerkr rspspkptkv higrltrnvt kdhimeifst ygkikmidmp vermhphlsk
      181 gyayvefenp deaekalkhm dggqidgqei tatavlapwp rppprrfspp rrmlppppmw
      241 rrspprmrrr srsprrrspv rrrsrspgrr rhrsrsssns sr
//
LOCUS       NP_061180                257 aa            linear   PRI 20-NOV-2025
DEFINITION  type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase [Homo
            sapiens].
ACCESSION   NP_061180
VERSION     NP_061180.1
DBSOURCE    REFSEQ: accession NM_018710.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Nigorikawa,K., Fukushima,Y., Shimada,C., Matsumoto,D. and Nomura,W.
  TITLE     CRISPRa Analysis of Phosphoinositide Phosphatases Shows That
            TMEM55A Is a Positive Regulator of Autophagy
  JOURNAL   Biol Pharm Bull 47 (6), 1148-1153 (2024)
   PUBMED   38880622
  REMARK    GeneRIF: CRISPRa Analysis of Phosphoinositide Phosphatases Shows
            That TMEM55A Is a Positive Regulator of Autophagy.
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Ungewickell,A., Hugge,C., Kisseleva,M., Chang,S.C., Zou,J.,
            Feng,Y., Galyov,E.E., Wilson,M. and Majerus,P.W.
  TITLE     The identification and characterization of two
            phosphatidylinositol-4,5-bisphosphate 4-phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 102 (52), 18854-18859 (2005)
   PUBMED   16365287
  REMARK    GeneRIF: identification and characterization of two previously
            undescribed human enzymes, PtdIns-4,5-P(2) 4-phosphatase type I and
            type II
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK313783.1, CR749733.1 and AC087439.6.
            
            Summary: TMEM55A catalyzes the degradation of phosphatidylinositol
            4,5-bisphosphate (PtdIns-4,5-P2) by removing the 4-phosphate
            (Ungewickell et al., 2005 [PubMed 16365287]).[supplied by OMIM, Mar
            2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033892.1, SRR1803617.9944.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285419.8/ ENSP00000285419.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.3"
     Protein         1..257
                     /product="type 2 phosphatidylinositol 4,5-bisphosphate
                     4-phosphatase"
                     /EC_number="3.1.3.78"
                     /note="PtdIns-4,5-P(2) 4-phosphatase type II;
                     ptdIns-4,5-P2 4-Ptase II; type II phosphatidylinositol
                     4,5-bisphosphate 4-phosphatase; type 2 PtdIns-4,5-P2
                     4-Ptase; transmembrane protein 55A; type II
                     PtdIns-4,5-P(2) 4-phosphatase"
                     /calculated_mol_wt=27950
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L2.1)"
     Region          7..250
                     /region_name="Tmemb_55A"
                     /note="Transmembrane protein 55A; pfam09788"
                     /db_xref="CDD:462901"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N4L2.1)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CZX7; propagated from
                     UniProtKB/Swiss-Prot (Q8N4L2.1)"
     Region          107..113
                     /region_name="CX5R motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L2.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L2.1)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4L2.1)"
     CDS             1..257
                     /gene="PIP4P2"
                     /gene_synonym="TMEM55A"
                     /coded_by="NM_018710.3:111..884"
                     /db_xref="CCDS:CCDS6252.1"
                     /db_xref="GeneID:55529"
                     /db_xref="HGNC:HGNC:25452"
                     /db_xref="MIM:609864"
ORIGIN      
        1 maadgvders pllsashsgn vtptappylq esspraelpp pytaiaspda sgipvincrv
       61 cqslinldgk lhqhvvkctv cneatpiknp ptgkkyvrcp cncllickdt srrigcprpn
      121 crriinlgpv mliseeqpaq palpiqpegt rvvcghcgnt flwmelrfnt lakcphckki
      181 ssvgsalprr rccayitigm icifigvglt vgtpdfarrf ratyvswaia yllgliclir
      241 acywgairvs ypehsfa
//
LOCUS       NP_004038                205 aa            linear   PRI 20-NOV-2025
DEFINITION  V-type proton ATPase 21 kDa proteolipid subunit c'' isoform 1 [Homo
            sapiens].
ACCESSION   NP_004038
VERSION     NP_004038.1
DBSOURCE    REFSEQ: accession NM_004047.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Wang,L., Wu,D., Robinson,C.V., Wu,H. and Fu,T.M.
  TITLE     Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
            Assembly
  JOURNAL   Mol Cell 80 (3), 501-511 (2020)
   PUBMED   33065002
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Vasanthakumar,T. and Rubinstein,J.L.
  TITLE     Structure and Roles of V-type ATPases
  JOURNAL   Trends Biochem Sci 45 (4), 295-307 (2020)
   PUBMED   32001091
  REMARK    Review article
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Hohn,A., Sittig,A., Jung,T., Grimm,S. and Grune,T.
  TITLE     Lipofuscin is formed independently of macroautophagy and lysosomal
            activity in stress-induced prematurely senescent human fibroblasts
  JOURNAL   Free Radic Biol Med 53 (9), 1760-1769 (2012)
   PUBMED   22982048
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Forgac,M.
  TITLE     Structure and properties of the vacuolar (H+)-ATPases
  JOURNAL   J Biol Chem 274 (19), 12951-12954 (1999)
   PUBMED   10224039
  REMARK    Review article
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Nelson,N. and Harvey,W.R.
  TITLE     Vacuolar and plasma membrane proton-adenosinetriphosphatases
  JOURNAL   Physiol Rev 79 (2), 361-385 (1999)
   PUBMED   10221984
  REMARK    Review article
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Nishigori,H., Yamada,S., Tomura,H., Fernald,A.A., Le Beau,M.M.,
            Takeuchi,T. and Takeda,J.
  TITLE     Identification and characterization of the gene encoding a second
            proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F)
  JOURNAL   Genomics 50 (2), 222-228 (1998)
   PUBMED   9653649
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Finbow,M.E. and Harrison,M.A.
  TITLE     The vacuolar H+-ATPase: a universal proton pump of eukaryotes
  JOURNAL   Biochem J 324 (Pt 3) (Pt 3), 697-712 (1997)
   PUBMED   9210392
  REMARK    Review article
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Stevens,T.H. and Forgac,M.
  TITLE     Structure, function and regulation of the vacuolar (H+)-ATPase
  JOURNAL   Annu Rev Cell Dev Biol 13, 779-808 (1997)
   PUBMED   9442887
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D89052.1 and AI439545.1.
            
            Summary: This gene encodes a portion of the V0 domain of vacuolar
            ATPase (V-ATPase), a multisubunit enzyme that mediates
            acidification of eukaryotic intracellular organelles. Activity of
            this enzyme is necessary for such varied processes as protein
            sorting, zymogen activation, receptor-mediated endocytosis, and
            synaptic vesicle proton gradient generation. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.209847.1,
                                           SRR1163657.531589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000472174.7/ ENSP00000431605.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..205
                     /product="V-type proton ATPase 21 kDa proteolipid subunit
                     c'' isoform 1"
                     /EC_number="7.1.2.2"
                     /note="V-ATPase 21 kDa proteolipid subunit c''; vacuolar
                     ATP synthase 21 kDa proteolipid subunit; H(+)-transporting
                     two-sector ATPase, subunit F; V-type proton ATPase 21 kDa
                     proteolipid subunit; V-ATPase subunit c''; vacuolar proton
                     pump 21 kDa proteolipid subunit; ATPase, H+ transporting,
                     lysosomal, 21-KD, V0 subunit C-prime, prime; V-ATPase
                     subunit b; ATPase, H+ transporting, lysosomal, subunit F;
                     ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b;
                     vacuolar proton pump 21 kDa proteolipid subunit c'';
                     V-type proton ATPase 21 kDa proteolipid subunit c''"
                     /calculated_mol_wt=21275
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Region          49..111
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt1"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18177"
                     /db_xref="CDD:349417"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            98
                     /site_type="other"
                     /note="Essential for proton translocation.
                     /evidence=ECO:0000250|UniProtKB:Q2TA24; propagated from
                     UniProtKB/Swiss-Prot (Q99437.1)"
     Region          133..197
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt2"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18178"
                     /db_xref="CDD:349418"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     CDS             1..205
                     /gene="ATP6V0B"
                     /gene_synonym="ATP6F; HATPL; VMA16"
                     /coded_by="NM_004047.5:82..699"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS505.1"
                     /db_xref="GeneID:533"
                     /db_xref="HGNC:HGNC:861"
                     /db_xref="MIM:603717"
ORIGIN      
        1 mtglallysg vfvafwacal avgvcytifd lgfrfdvawf ltetspfmws nlgiglaisl
       61 svvgaawgiy itgssiiggg vkapriktkn lvsiifceav aiygiimaiv isnmaepfsa
      121 tdpkaighrn yhagysmfga gltvglsnlf cgvcvgivgs gaaladaqnp slfvkilive
      181 ifgsaiglfg vivailqtsr vkmgd
//
LOCUS       NP_055889               1770 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF1B isoform b [Homo sapiens].
ACCESSION   NP_055889
VERSION     NP_055889.2
DBSOURCE    REFSEQ: accession NM_015074.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Chen,W., Song,J., Liu,S., Tang,B., Shen,L., Zhu,J., Fang,S., Wu,F.,
            Zheng,L., Qiu,R., Chen,C., Gao,Y., Tu,J., Zhao,Z. and Ji,J.
  TITLE     USP9X promotes apoptosis in cholangiocarcinoma by modulation
            expression of KIF1Bbeta via deubiquitinating EGLN3
  JOURNAL   J Biomed Sci 28 (1), 44 (2021)
   PUBMED   34112167
  REMARK    GeneRIF: USP9X promotes apoptosis in cholangiocarcinoma by
            modulation expression of KIF1Bbeta via deubiquitinating EGLN3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Saito,M., Hayashi,Y., Suzuki,T., Tanaka,H., Hozumi,I. and Tsuji,S.
  TITLE     Linkage mapping of the gene for Charcot-Marie-Tooth disease type 2
            to chromosome 1p (CMT2A) and the clinical features of CMT2A
  JOURNAL   Neurology 49 (6), 1630-1635 (1997)
   PUBMED   9409358
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Gong,T.L., Burmeister,M. and Lomax,M.I.
  TITLE     The novel gene D4Mil1e maps to mouse chromosome 4 and human
            chromosome 1p36
  JOURNAL   Mamm Genome 7 (10), 790-791 (1996)
   PUBMED   8854876
REFERENCE   7  (residues 1 to 1770)
  AUTHORS   Nangaku,M., Sato-Yoshitake,R., Okada,Y., Noda,Y., Takemura,R.,
            Yamazaki,H. and Hirokawa,N.
  TITLE     KIF1B, a novel microtubule plus end-directed monomeric motor
            protein for transport of mitochondria
  JOURNAL   Cell 79 (7), 1209-1220 (1994)
   PUBMED   7528108
REFERENCE   8  (residues 1 to 1770)
  AUTHORS   Zuchner,S.
  TITLE     MFN2 Hereditary Motor and Sensory Neuropathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301684
REFERENCE   9  (residues 1 to 1770)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   10 (residues 1 to 1770)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA774937.1, AF257176.1,
            AB040881.2, BP239973.1, DA485632.1, DA113609.1, AB017133.1,
            AK025761.1 and AA609163.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 30, 2004 this sequence version replaced NP_055889.1.
            
            Transcript Variant: This variant (1) encodes isoform b, also called
            KIF1b-beta.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF257176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..1770
                     /product="kinesin-like protein KIF1B isoform b"
                     /EC_number="5.6.1.3"
                     /note="kinesin superfamily protein KIF1B; kinesin-like
                     protein KIF1B; Charcot-Marie-Tooth neuropathy type II"
                     /calculated_mol_wt=199132
     Region          4..355
                     /region_name="KISc_KIF1A_KIF1B"
                     /note="Kinesin motor domain, KIF1_like proteins; cd01365"
                     /db_xref="CDD:276816"
     Site            order(13,97,100,102..105,248)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276816"
     Site            order(301,304,307)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276816"
     Region          352..509
                     /region_name="Kinesin_assoc"
                     /note="Kinesin-associated; pfam16183"
                     /db_xref="CDD:465047"
     Region          484..593
                     /region_name="FHA_KIF1B"
                     /note="forkhead associated (FHA) domain found in
                     kinesin-like protein KIF1B; cd22727"
                     /db_xref="CDD:438779"
     Region          616..>673
                     /region_name="GimC"
                     /note="Prefoldin, chaperonin cofactor [Posttranslational
                     modification, protein turnover, chaperones]; COG1382"
                     /db_xref="CDD:440992"
     Region          799..846
                     /region_name="KIF1B"
                     /note="Kinesin protein 1B; pfam12423"
                     /db_xref="CDD:463574"
     Region          <910..929
                     /region_name="KIF1B"
                     /note="Kinesin protein 1B; pfam12423"
                     /db_xref="CDD:463574"
     Region          1220..1367
                     /region_name="DUF3694"
                     /note="Kinesin protein; pfam12473"
                     /db_xref="CDD:463599"
     Region          1651..1753
                     /region_name="PH_KIFIA_KIFIB"
                     /note="KIFIA and KIFIB protein pleckstrin homology (PH)
                     domain; cd01233"
                     /db_xref="CDD:269939"
     CDS             1..1770
                     /gene="KIF1B"
                     /gene_synonym="CMT2; CMT2A; CMT2A1; HMSNII; KLP; NBLST1"
                     /coded_by="NM_015074.3:253..5565"
                     /note="isoform b is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS111.1"
                     /db_xref="GeneID:23095"
                     /db_xref="HGNC:HGNC:16636"
                     /db_xref="MIM:605995"
ORIGIN      
        1 msgasvkvav rvrpfnsret skeskciiqm qgnstsiinp knpkeapksf sfdysywsht
       61 spedpcfasq nrvyndigke mllhafegyn vcifaygqtg agksytmmgk qeesqagiip
      121 qlceelfeki ndncneemsy svevsymeiy cervrdllnp knkgnlrvre hpllgpyved
      181 lsklavtsyt diadlmdagn kartvaatnm netssrshav ftivftqkkh dnetnlstek
      241 vskislvdla gseradstga kgtrlkegan inkslttlgk visalaevsk kkkktdfipy
      301 rdsvltwllr enlggnsrta mvaalspadi nydetlstlr yadrakqikc navinedpna
      361 klvrelkeev trlkdllraq glgdiidtsm gsltsspssc slssqvglts vtsiqerims
      421 tpggeeaier lkesekiiae lnetweeklr kteairmere allaemgvai redggtlgvf
      481 spkktphlvn lnedplmsec llyyikdgit rvgqadaerr qdivlsgahi keehcifrse
      541 rsnsgevivt lepcersety vngkrvsqpv qlrsgnriim gknhvfrfnh peqaraerek
      601 tpsaetpsep vdwtfaqrel lekqgidmkq emekrlqeme ilykkekeea dllleqqrld
      661 yesklqalqk qvetrslaae tteeeeeeee vpwtqhefel aqwafrkwks hqftslrdll
      721 wgnavylkea naisvelkkk vqfqfvlltd tlysplppel lptemekthe drpfprtvva
      781 vevqdlknga thywsleklk qrldlmremy dragemassa qdesettvtg sdpfydrfhw
      841 fklvgsspif hgcvnerlad rtpsptfsta dsditelade qqdemedfdd eafvddagsd
      901 agteegsdlf sdghdpfydr spwfilvgra fvylsnllyp vplihrvaiv sekgevrgfl
      961 rvavqaiaad eeapdygsgi rqsgtakisf dneyfnqsdf ssvamtrsgl sleelriveg
     1021 qgqssevitp peeisrindl dlksstlldg kmvmegfsee ignhlklgsa ftfrvtvlqa
     1081 sgilpeyadi fcqfnflhrh deafsteplk nngrgsplaf yhvqniavei tesfvdyikt
     1141 kpivfevfgh yqqhplhlqg qelnsppqpc rrffpppmpl skpvpatkln tmsktslgqs
     1201 mskydllvwf eiseleptge yipavvdhta glpcqgtfll hqgiqrritv tiihekgsel
     1261 hwkdvrelvv grirnkpevd eaavdailsl niisakylks shnssrtfyr feavwdsslh
     1321 nslllnrvtp ygekiymtls ayleldhciq pavitkdvcm vfysrdakis pprslrslfg
     1381 sgyskspdsn rvtgiyelsl ckmsdtgspg mqrrrrkild tsvayvrgee nlagwrprgd
     1441 slilehqwel eklellheve ktrhflllre rlgdsipksl sdslspslss gtlststsis
     1501 sqistttfes aitpsessgy dsgdieslvd rekelatkcl qllthtfnre fsqvhgsvsd
     1561 cklsdispig rdpsessfss atltpsstcp slvdsrsnsl dqktpeansr asspcpefeq
     1621 fqivpavetp ylaragknef lnlvpdieei rpssvvskkg ylhfkeplys nwakhfvvvr
     1681 rpyvfiynsd kdpvergiin lstaqveyse dqqamvktpn tfavctkhrg vllqalndkd
     1741 mndwlyafnp llagtirskl srrcpsqsky
//
LOCUS       NP_001356036             318 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356036
VERSION     NP_001356036.1
DBSOURCE    REFSEQ: accession NM_001369107.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.126562.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..318
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 12"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36303
     Region          20..85
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(29,31..33,35..39,42..43,46..47,52..55)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          94..317
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..318
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369107.1:429..1385"
                     /note="isoform 12 is encoded by transcript variant 28"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mecadepcda yeveqtpqgf rstlrapsll ykhivgkrgd trkkiemetk tsisipkpgq
       61 dgeivitgqh rngvisartr idvlldtfrr kqpfthflaf flnevevqeg flrfqeevla
      121 kcsmdhgvds sifqnpkklh ltigmlvlls eeeiqqtcem lqqckeefin disggkplev
      181 emagieymnd dpgmvdvlya kvhmkdgsnr lqelvdrvle rfqasglivk ewnsvklhat
      241 vmntlfrkdp naegrynlyt aegkyifker esfdgrnilk lfenfyfgsl klnsihisqr
      301 ftvdsfgnya scgqidfs
//
LOCUS       NP_004773                258 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptosomal-associated protein 29 [Homo sapiens].
ACCESSION   NP_004773
VERSION     NP_004773.1
DBSOURCE    REFSEQ: accession NM_004782.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Zheng,D., Tong,M., Zhang,S., Pan,Y., Zhao,Y., Zhong,Q. and Liu,X.
  TITLE     Human YKT6 forms priming complex with STX17 and SNAP29 to
            facilitate autophagosome-lysosome fusion
  JOURNAL   Cell Rep 43 (2), 113760 (2024)
   PUBMED   38340317
  REMARK    GeneRIF: Human YKT6 forms priming complex with STX17 and SNAP29 to
            facilitate autophagosome-lysosome fusion.
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Zhang,S., Tong,M., Zheng,D., Huang,H., Li,L., Ungermann,C., Pan,Y.,
            Luo,H., Lei,M., Tang,Z., Fu,W., Chen,S., Liu,X. and Zhong,Q.
  TITLE     C9orf72-catalyzed GTP loading of Rab39A enables HOPS-mediated
            membrane tethering and fusion in mammalian autophagy
  JOURNAL   Nat Commun 14 (1), 6360 (2023)
   PUBMED   37821429
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Matsui,K., Emoto,M., Fukuda,N., Nomiyama,R., Yamada,K. and
            Tanizawa,Y.
  TITLE     SNARE-binding protein synaptosomal-associated protein of 29 kDa
            (SNAP29) regulates the intracellular sequestration of glucose
            transporter 4 (GLUT4) vesicles in adipocytes
  JOURNAL   J Diabetes Investig 14 (1), 19-27 (2023)
   PUBMED   36181414
  REMARK    GeneRIF: SNARE-binding protein synaptosomal-associated protein of
            29 kDa (SNAP29) regulates the intracellular sequestration of
            glucose transporter 4 (GLUT4) vesicles in adipocytes.
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Rotem-Yehudar,R., Galperin,E. and Horowitz,M.
  TITLE     Association of insulin-like growth factor 1 receptor with EHD1 and
            SNAP29
  JOURNAL   J Biol Chem 276 (35), 33054-33060 (2001)
   PUBMED   11423532
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Saito,T., Guan,F., Papolos,D.F., Rajouria,N., Fann,C.S. and
            Lachman,H.M.
  TITLE     Polymorphism in SNAP29 gene promoter region associated with
            schizophrenia
  JOURNAL   Mol Psychiatry 6 (2), 193-201 (2001)
   PUBMED   11317222
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Mol Psychiatry 2001 Sep;6(5):605]
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Scales,S.J., Chen,Y.A., Yoo,B.Y., Patel,S.M., Doung,Y.C. and
            Scheller,R.H.
  TITLE     SNAREs contribute to the specificity of membrane fusion
  JOURNAL   Neuron 26 (2), 457-464 (2000)
   PUBMED   10839363
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Wong,S.H., Xu,Y., Zhang,T., Griffiths,G., Lowe,S.L.,
            Subramaniam,V.N., Seow,K.T. and Hong,W.
  TITLE     GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with
            syntaxin 6
  JOURNAL   Mol Biol Cell 10 (1), 119-134 (1999)
   PUBMED   9880331
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG773022.1, AF115436.1,
            AC007308.13 and CA427899.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene, a member of the SNAP25 gene family, encodes a
            protein involved in multiple membrane trafficking steps. Two other
            members of this gene family, SNAP23 and SNAP25, encode proteins
            that bind a syntaxin protein and mediate synaptic vesicle membrane
            docking and fusion to the plasma membrane. The protein encoded by
            this gene binds tightly to multiple syntaxins and is localized to
            intracellular membrane structures rather than to the plasma
            membrane. While the protein is mostly membrane-bound, a significant
            fraction of it is found free in the cytoplasm. Use of multiple
            polyadenylation sites has been noted for this gene. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.113951.1,
                                           SRR1660809.243742.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215730.12/ ENSP00000215730.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..258
                     /product="synaptosomal-associated protein 29"
                     /note="vesicle-membrane fusion protein SNAP-29; soluble 29
                     kDa NSF attachment protein; synaptosome associated protein
                     29kDa; synaptosomal-associated protein, 29kD;
                     synaptosomal-associated protein, 29kDa; cerebral
                     dysgenesis, neuropathy, ichthyosis and keratoderma
                     syndrome"
                     /calculated_mol_wt=28839
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95721.1)"
     Region          47..111
                     /region_name="SNARE_SNAP29N"
                     /note="N-terminal SNARE motif of SNAP29; cd15887"
                     /db_xref="CDD:277240"
     Site            order(49,52..57,59..64,66..67,70..71,73..78,80..81,83..85,
                     87..92,94..95,97..99,101..102,104..106,108..109,111)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277240"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            84
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277240"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Region          150..191
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95721.1)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Region          199..257
                     /region_name="SNARE_SNAP29C"
                     /note="C-terminal SNARE motif of SNAP29; cd15856"
                     /db_xref="CDD:277209"
     Site            order(203..206,208..210,212..214,216..217,219..224,
                     226..227,229..230,233..234,236..238,240..242,244..245,
                     247..248,251..252,254..255,257)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277209"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95721.1)"
     Site            230
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277209"
     CDS             1..258
                     /gene="SNAP29"
                     /gene_synonym="CEDNIK; SNAP-29"
                     /coded_by="NM_004782.4:105..881"
                     /db_xref="CCDS:CCDS13784.1"
                     /db_xref="GeneID:9342"
                     /db_xref="HGNC:HGNC:11133"
                     /db_xref="MIM:604202"
ORIGIN      
        1 msaypksynp fdddgedega rpapwrdard lpdgpdapad rqqylrqevl rraeataast
       61 srslalmyes ekvgvassee larqrgvler tekmvdkmdq dlkisqkhin siksvfgglv
      121 nyfkskpvet ppeqngtlts qpnnrlkeai stskeqeaky qashpnlrkl ddtdpvprga
      181 gsamstdayp knphlrayhq kidsnldels mglgrlkdia lgmqteieeq ddildrlttk
      241 vdkldvniks terkvrql
//
LOCUS       NP_078831                533 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 6 isoform 2 [Homo sapiens].
ACCESSION   NP_078831
VERSION     NP_078831.4
DBSOURCE    REFSEQ: accession NM_024555.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Lavie,J., Lalou,C., Mahfouf,W., Dupuy,J.W., Lacaule,A.,
            Cywinska,A.A., Lacombe,D., Duchene,A.M., Raymond,A.A.,
            Rezvani,H.R., Ngondo,R.P. and Benard,G.
  TITLE     The E3 ubiquitin ligase FBXL6 controls the quality of newly
            synthesized mitochondrial ribosomal proteins
  JOURNAL   Cell Rep 42 (6), 112579 (2023)
   PUBMED   37267103
  REMARK    GeneRIF: The E3 ubiquitin ligase FBXL6 controls the quality of
            newly synthesized mitochondrial ribosomal proteins.
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Feng,G., Sun,H. and Piao,M.
  TITLE     FBXL6 is dysregulated in keloids and promotes keloid fibroblast
            growth by inducing c-Myc expression
  JOURNAL   Int Wound J 20 (1), 131-139 (2023)
   PUBMED   35606330
  REMARK    GeneRIF: FBXL6 is dysregulated in keloids and promotes keloid
            fibroblast growth by inducing c-Myc expression.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Li,Y., Cui,K., Zhang,Q., Li,X., Lin,X., Tang,Y., Prochownik,E.V.
            and Li,Y.
  TITLE     FBXL6 degrades phosphorylated p53 to promote tumor growth
  JOURNAL   Cell Death Differ 28 (7), 2112-2125 (2021)
   PUBMED   33568778
  REMARK    GeneRIF: FBXL6 degrades phosphorylated p53 to promote tumor growth.
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Lievens,S., Vanderroost,N., Van der Heyden,J., Gesellchen,V.,
            Vidal,M. and Tavernier,J.
  TITLE     Array MAPPIT: high-throughput interactome analysis in mammalian
            cells
  JOURNAL   J Proteome Res 8 (2), 877-886 (2009)
   PUBMED   19159283
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Roukens,M.G., Alloul-Ramdhani,M., Moghadasi,S., Op den Brouw,M. and
            Baker,D.A.
  TITLE     Downregulation of vertebrate Tel (ETV6) and Drosophila Yan is
            facilitated by an evolutionarily conserved mechanism of
            F-box-mediated ubiquitination
  JOURNAL   Mol Cell Biol 28 (13), 4394-4406 (2008)
   PUBMED   18426905
  REMARK    GeneRIF: Fbl6 regulates Tel/Yan protein stability and allows
            appropriate spatiotemporal control of gene expression by these
            repressors.
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK026541.1 and AC233992.5.
            
            On Jul 19, 2013 this sequence version replaced NP_078831.3.
            
            Summary: This gene encodes a member of a family of proteins that
            are characterized by an F-box motif. The encoded protein also
            contains leucine-rich repeats. F-box-containing proteins comprise
            one of the subunits of the SCF (SKP1-cullin-F-box) complex, which
            functions in phosphorylation-dependent ubiquitination. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region, but maintains the reading frame, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026541.1, AK223088.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..533
                     /product="F-box/LRR-repeat protein 6 isoform 2"
                     /note="F-box protein Fbl6; F-box/LRR-repeat protein 6"
                     /calculated_mol_wt=57753
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          49..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          112..158
                     /region_name="F-box_FBXL6"
                     /note="F-box domain found in F-box/LRR-repeat protein 6
                     (FBXL6) and similar proteins; cd22119"
                     /db_xref="CDD:438891"
     Site            order(115,119,122..123,126..127,136,138..139,143..145,147)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438891"
     Region          177..203
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          185..215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          188..392
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          216..241
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          224..249
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          242..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          275..301
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          294..323
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          306..331
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          324..351
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          335..359
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          <351..502
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          352..379
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          362..387
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          380..403
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          388..413
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          417..443
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          436..468
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          447..475
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          469..493
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          476..501
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     CDS             1..533
                     /gene="FBXL6"
                     /gene_synonym="FBL6; FBL6A; PP14630"
                     /coded_by="NM_024555.6:26..1627"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47942.1"
                     /db_xref="GeneID:26233"
                     /db_xref="HGNC:HGNC:13603"
                     /db_xref="MIM:609076"
ORIGIN      
        1 maapasrqvr rraraaprpr saedwwwdrl aprgsgyhll qsdsmllvls epgparpraq
       61 rrasrrtprq pprgpsaaak pkaglrseaa aapapapapt ptpeegpdag wgdripleil
      121 vqifgllvaa dgpmpflgra arvcrrwqea asqpalwhtv tlssplvgrp akggvkaekk
      181 llaslewlmp nrfsqlqrlt lihwksqlvg eccprltflk lsgchgvtad alvmlakacc
      241 qlhsldlqhs mvestavvsf leeagsrmrk lwltyssqtt ailgallgsc cpqlqvlevs
      301 tginrnsipl qlpvealqkg cpqlqvlrll nlmwlpkppg rgvapgpgfp sleelclass
      361 tcnfvsnevl grllhgspnl rlldlrgcar itpaglqdlp creleqlhlg lygtsdrltl
      421 akegspfltq kwchtlreld lsgqgfsekd leqalaafls tpggshpalc slnlrgtrvt
      481 pstvssvisg cpgllylnle scrclprglk rayrgleevq wcleqlltsp sps
//
LOCUS       NP_061160               1097 aa            linear   PRI 20-NOV-2025
DEFINITION  apolipoprotein B receptor [Homo sapiens].
ACCESSION   NP_061160 NP_001411100 NP_877956
VERSION     NP_061160.3
DBSOURCE    REFSEQ: accession NM_018690.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1097)
  AUTHORS   Sun,J., Sun,L., Chen,W., Yin,X., Lu,Y. and Jiang,Q.
  TITLE     A family with hypothyroidism caused by fatty acid synthase and
            apolipoprotein B receptor mutations
  JOURNAL   Mol Med Rep 18 (6), 4904-4912 (2018)
   PUBMED   30272292
  REMARK    GeneRIF: the findings reported here demonstrated that patients with
            mutations in FASN (c.G7192T, p.A2398S) and APOBR (c.C1883G,
            p.T628R) may be predisposed to hypothyroidism. These mutations may
            disrupt the regulation of fatty acid biosynthesis and lipid
            metabolism. These findings may reveal the high degree of genetic
            heterogeneity in hypothyroidism phenotypes.
REFERENCE   2  (residues 1 to 1097)
  AUTHORS   Volckmar,A.L., Putter,C., Song,J.Y., Graniger,J., Knoll,N.,
            Wolters,B., Hebebrand,J., Scherag,A., Reinehr,T. and Hinney,A.
  TITLE     Analyses of non-synonymous obesity risk alleles in SH2B1
            (rs7498665) and APOB48R (rs180743) in obese children and
            adolescents undergoing a 1-year lifestyle intervention
  JOURNAL   Exp Clin Endocrinol Diabetes 121 (6), 334-337 (2013)
   PUBMED   23519644
  REMARK    GeneRIF: The obesity risk alleles of non-synonymous SNPs at SH2B1
            and APOB48R have no strong effect on weight loss-related phenotypes
            in overweight children after a 1-year lifestyle intervention.
REFERENCE   3  (residues 1 to 1097)
  AUTHORS   Bermudez,B., Lopez,S., Varela,L.M., Ortega,A., Pacheco,Y.M.,
            Moreda,W., Moreno-Luna,R., Abia,R. and Muriana,F.J.
  TITLE     Triglyceride-rich lipoprotein regulates APOB48 receptor gene
            expression in human THP-1 monocytes and macrophages
  JOURNAL   J Nutr 142 (2), 227-232 (2012)
   PUBMED   22190030
  REMARK    GeneRIF: These findings suggest that APOB48R represents a molecular
            target of postprandial lipoproteins via PPAR-dependent pathways in
            human monocytes and macrophages and advance an important link
            between postprandial metabolism of dietary fats and atherogenesis.
REFERENCE   4  (residues 1 to 1097)
  AUTHORS   Varela,L.M., Ortega,A., Bermudez,B., Lopez,S., Pacheco,Y.M.,
            Villar,J., Abia,R. and Muriana,F.J.
  TITLE     A high-fat meal promotes lipid-load and apolipoprotein B-48
            receptor transcriptional activity in circulating monocytes
  JOURNAL   Am J Clin Nutr 93 (5), 918-925 (2011)
   PUBMED   21367954
  REMARK    GeneRIF: investigation of apoB48R gene transcription in circulating
            monocytes: increase in apoB48R gene transcription following
            high-fat meal
REFERENCE   5  (residues 1 to 1097)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 1097)
  AUTHORS   Kawakami,A., Tani,M., Chiba,T., Yui,K., Shinozaki,S., Nakajima,K.,
            Tanaka,A., Shimokado,K. and Yoshida,M.
  TITLE     Pitavastatin inhibits remnant lipoprotein-induced macrophage foam
            cell formation through ApoB48 receptor-dependent mechanism
  JOURNAL   Arterioscler Thromb Vasc Biol 25 (2), 424-429 (2005)
   PUBMED   15591219
  REMARK    GeneRIF: Atherogenic remnant lipoproteins induced macrophage foam
            cell formation via apoB48R, indicating a potential role of apoB48R
            in atherosclerosis.
            Erratum:[Arterioscler Thromb Vasc Biol. 2013 Jun;33(6):e118]
REFERENCE   7  (residues 1 to 1097)
  AUTHORS   Fujita,Y., Ezura,Y., Bujo,H., Nakajima,T., Takahashi,K.,
            Kamimura,K., Iino,Y., Katayama,Y., Saito,Y. and Emi,M.
  TITLE     Association of nucleotide variations in the apolipoprotein B48
            receptor gene (APOB48R) with hypercholesterolemia
  JOURNAL   J Hum Genet 50 (4), 203-209 (2005)
   PUBMED   15830122
  REMARK    GeneRIF: Nucleotide variations in the apolipoprotein B48 receptor
            gene is associated with hypercholesterolemia
REFERENCE   8  (residues 1 to 1097)
  AUTHORS   Brown,M.L., Ramprasad,M.P., Umeda,P.K., Tanaka,A., Kobayashi,Y.,
            Watanabe,T., Shimoyamada,H., Kuo,W.L., Li,R., Song,R., Bradley,W.A.
            and Gianturco,S.H.
  TITLE     A macrophage receptor for apolipoprotein B48: cloning, expression,
            and atherosclerosis
  JOURNAL   Proc Natl Acad Sci U S A 97 (13), 7488-7493 (2000)
   PUBMED   10852956
REFERENCE   9  (residues 1 to 1097)
  AUTHORS   Ramprasad,M.P., Li,R., Bradley,W.A. and Gianturco,S.H.
  TITLE     Human THP-1 monocyte-macrophage membrane binding proteins: distinct
            receptor(s) for triglyceride-rich lipoproteins
  JOURNAL   Biochemistry 34 (28), 9126-9135 (1995)
   PUBMED   7619811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138894.2.
            
            On or before Dec 3, 2024 this sequence version replaced
            NP_001411100.1, NP_061160.2.
            
            Summary: Apolipoprotein B48 receptor is a macrophage receptor that
            binds to the apolipoprotein B48 of dietary triglyceride (TG)-rich
            lipoproteins. This receptor may provide essential lipids,
            lipid-soluble vitamins and other nutrients to reticuloendothelial
            cells. If overwhelmed with elevated plasma triglyceride, the
            apolipoprotein B48 receptor may contribute to foam cell formation,
            endothelial dysfunction, and atherothrombogenesis. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000564831.6/ ENSP00000457539.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1097
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..1097
                     /product="apolipoprotein B receptor"
                     /note="apolipoprotein B100 receptor; apolipoprotein B48
                     receptor; apolipoprotein B-100 receptor; apolipoprotein
                     B-48 receptor; apoB-48R"
                     /calculated_mol_wt=115503
     Region          64..249
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VD83.3)"
     Region          <108..>362
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <111..669
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          262..376
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VD83.3)"
     Region          410..739
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VD83.3)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VBT6; propagated from
                     UniProtKB/Swiss-Prot (Q0VD83.3)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q0VD83.3)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q0VD83.3)"
     Region          <586..>851
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VBT6; propagated from
                     UniProtKB/Swiss-Prot (Q0VD83.3)"
     Region          789..866
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VD83.3)"
     Region          889..1097
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0VD83.3)"
     CDS             1..1097
                     /gene="APOBR"
                     /gene_synonym="APOB100R; APOB48R"
                     /coded_by="NM_018690.4:40..3333"
                     /db_xref="CCDS:CCDS58442.1"
                     /db_xref="GeneID:55911"
                     /db_xref="HGNC:HGNC:24087"
                     /db_xref="MIM:605220"
ORIGIN      
        1 mdflrlylpg lhqalrgald slgtfvsyll gdavptvere aqaaeelgvv avgktgkive
       61 eeaqedlegl rgsqnegagr lrgpgddrrh evgssaveqt wgwgdgsshg sqaerqdsga
      121 getakaarcq epsahleark kskagsgacq drsgqaqerq esheqevnre erlrsweqee
      181 eeeevrarep gmargaesew twhgetegka gavgpkaagd nremeqgvre adageteepg
      241 aegagkgeev vvvekacest rawgtwgpga epedwgilgr eearttpgre earaildgee
      301 artisggeea etasggeeae tasggeeagt asggeeagia sggeagtasg geeagtasgg
      361 eeagtasggd eawttsgkee adllgvrqte ygavpgerll eatgkvwvle eegdeereae
      421 vspfpkqpqv lgterteeaa esqtagreav ggqeagesfe gqvdlrgkea emrqdlgira
      481 drarmeelvq aeeaqeergs srdpvaelps dgeaegtadl eatpearpee eltgeeseaa
      541 qtscgllgve wgglthsvtk gqgpelmgga qtptkqpeer eagevelmgv lalskeeqer
      601 sleagprhag svkpeaseaf pgawenrtrk dmergntqed aadgeqreee etaggqtlaa
      661 eaegdresel sevpeaggeg lttqdagcgt eegeasvsen qeldgstgad agpcpslgea
      721 yaretedeea eadrtsrrgw rlqavavglp dredaqtgsv aagimggdvv phisaagage
      781 alegvlgqgw dskekeeaaa gehaggqefg legsaeeevt grgsqveafe sreggpwggr
      841 veaeesagae dscgldpags qtaraegmga mveaggllek wtlleeeavg wqereqreds
      901 egrcgdyhpe geaprlldae glmvtggrra eaketepesl ehvrgqeeqp thqapaeaap
      961 esvgeaetae amgsarggaa nswseaplpg slldvsvprs rvhlsrsssq rrsrpsfrrt
     1021 paweqqeepp apnppeeels apeqrplqle eplepsplrh dgtpvparrr plghgfglah
     1081 pgmmqelqar lgrpkpq
//
LOCUS       NP_001278963             693 aa            linear   PRI 20-NOV-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 isoform a
            [Homo sapiens].
ACCESSION   NP_001278963
VERSION     NP_001278963.1
DBSOURCE    REFSEQ: accession NM_001292034.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Zhang,J., Cao,L., Gao,A., Ren,R., Yu,L., Li,Q., Liu,Y., Qi,W.,
            Hou,Y., Sui,W., Su,G., Zhang,Y., Zhang,C. and Zhang,M.
  TITLE     E3 ligase RNF99 negatively regulates TLR-mediated inflammatory
            immune response via K48-linked ubiquitination of TAB2
  JOURNAL   Cell Death Differ 30 (4), 966-978 (2023)
   PUBMED   36681779
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Koene,S., Klerx-Melis,F., Roest,A.A.W., Kleijwegt,M.C., Bootsma,M.,
            Haak,M.C., van Haeringen,M.H., Ruivenkamp,C.A.L., Nibbeling,E.A.R.
            and van Haeringen,A.
  TITLE     Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family
  JOURNAL   Am J Med Genet A 188 (12), 3510-3515 (2022)
   PUBMED   36000780
  REMARK    GeneRIF: Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Liu,H., Zhang,H., Fan,H., Tang,S. and Weng,J.
  TITLE     TAB2 Promotes the Biological Functions of Head and Neck Squamous
            Cell Carcinoma Cells via EMT and PI3K Pathway
  JOURNAL   Dis Markers 2022, 1217918 (2022)
   PUBMED   35978886
  REMARK    GeneRIF: TAB2 Promotes the Biological Functions of Head and Neck
            Squamous Cell Carcinoma Cells via EMT and PI3K Pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Takaesu,G., Kishida,S., Hiyama,A., Yamaguchi,K., Shibuya,H.,
            Irie,K., Ninomiya-Tsuji,J. and Matsumoto,K.
  TITLE     TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK
            by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
  JOURNAL   Mol Cell 5 (4), 649-658 (2000)
   PUBMED   10882101
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Mercurio,F., Zhu,H., Murray,B.W., Shevchenko,A., Bennett,B.L.,
            Li,J., Young,D.B., Barbosa,M., Mann,M., Manning,A. and Rao,A.
  TITLE     IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for
            NF-kappaB activation
  JOURNAL   Science 278 (5339), 860-866 (1997)
   PUBMED   9346484
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Deacon,K. and Blank,J.L.
  TITLE     Characterization of the mitogen-activated protein kinase kinase 4
            (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated
            by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not
            cause activation of p38 kinase in vivo
  JOURNAL   J Biol Chem 272 (22), 14489-14496 (1997)
   PUBMED   9162092
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Shibuya,H., Yamaguchi,K., Shirakabe,K., Tonegawa,A., Gotoh,Y.,
            Ueno,N., Irie,K., Nishida,E. and Matsumoto,K.
  TITLE     TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
            transduction
  JOURNAL   Science 272 (5265), 1179-1182 (1996)
   PUBMED   8638164
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138727.10, AB018276.2 and
            BC035910.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an activator of
            MAP3K7/TAK1, which is required for for the IL-1 induced activation
            of nuclear factor kappaB and MAPK8/JNK. This protein forms a kinase
            complex with TRAF6, MAP3K7 and TAB1, and it thus serves as an
            adaptor that links MAP3K7 and TRAF6. This protein, along with TAB1
            and MAP3K7, also participates in the signal transduction induced by
            TNFSF11/RANKl through the activation of the receptor activator of
            NF-kappaB (TNFRSF11A/RANK), which may regulate the development and
            function of osteoclasts. Studies of the related mouse protein
            indicate that it functions to protect against liver damage caused
            by chemical stressors. Mutations in this gene cause congenital
            heart defects, multiple types, 2 (CHTD2). Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1331247.1,
                                           SRR14038195.1545882.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153031, SAMEA2153980
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000637181.2/ ENSP00000490618.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.1"
     Protein         1..693
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 2 isoform a"
                     /note="TAK1-binding protein 2; mitogen-activated protein
                     kinase kinase kinase 7-interacting protein 2"
                     /calculated_mol_wt=76363
     Region          9..50
                     /region_name="CUE_TAB2_TAB3"
                     /note="CUE domain found in the N-terminal of
                     TGF-beta-activated kinase 1 and MAP3K7-binding proteins
                     TAB2, TAB3 and similar proteins; cd14362"
                     /db_xref="CDD:270545"
     Region          91..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          219..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          330..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          540..>619
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          642..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          667..690
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          668..687
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Site            673
                     /site_type="methylation"
                     /note="(Microbial infection) S-methylcysteine.
                     /evidence=ECO:0000269|PubMed:22158122,
                     ECO:0000269|PubMed:25412445; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          675..685
                     /region_name="Interaction with polyubiquitin.
                     /evidence=ECO:0000269|PubMed:19935683"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     CDS             1..693
                     /gene="TAB2"
                     /gene_synonym="CHTD2; MAP3K7IP2; TAB-2"
                     /coded_by="NM_001292034.3:394..2475"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5214.1"
                     /db_xref="GeneID:23118"
                     /db_xref="HGNC:HGNC:17075"
                     /db_xref="MIM:605101"
ORIGIN      
        1 maqgshqidf qvlhdlrqkf pevpevvvsr cmlqnnnnld accavlsqes trylygegdl
       61 nfsddsgisg lrnhmtslnl dlqsqniyhh gregsrmngs rtlthsisdg qlqggqsnse
      121 lfqqepqtap aqvpqgfnvf gmssssgasn saphlgfhlg skgtsslsqq tprfnpimvt
      181 lapniqtgrn tptslhihgv pppvlnspqg nsiyirpyit tpggttrqtq qhsgwvsqfn
      241 pmnpqqvyqp sqpgpwttcp asnplshtss qqpnqqghqt shvympissp ttsqpptihs
      301 sgssqssahs qyniqnistg prknqieikl eppqrnnssk lrssgprtss tsssvnsqtl
      361 nrnqptvyia asppntdelm srsqpkvyis anaatgdeqv mrnqptlfis tnsgasaasr
      421 nmsgqvsmgp afihhhppks raignnsats prvvvtqpnt kytfkitvsp nkppavspgv
      481 vsptfeltnl lnhpdhyvet eniqhltdpt lahvdriset rklsmgsdda aytqallvhq
      541 karmerlqre leiqkkkldk lksevnemen nltrrrlkrs nsisqipsle emqqlrscnr
      601 qlqididclt keidlfqarg phfnpsaihn fydnigfvgp vppkpkdqrs iiktpktqdt
      661 eddegaqwnc tactflnhpa lirceqcemp rhf
//
LOCUS       NP_001305325             436 aa            linear   PRI 20-NOV-2025
DEFINITION  plasma kallikrein isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001305325 XP_011530236
VERSION     NP_001305325.1
DBSOURCE    REFSEQ: accession NM_001318396.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Longhurst,H.J., Lindsay,K., Petersen,R.S., Fijen,L.M., Gurugama,P.,
            Maag,D., Butler,J.S., Shah,M.Y., Golden,A., Xu,Y., Boiselle,C.,
            Vogel,J.D., Abdelhady,A.M., Maitland,M.L., McKee,M.D., Seitzer,J.,
            Han,B.W., Soukamneuth,S., Leonard,J., Sepp-Lorenzino,L.,
            Clark,E.D., Lebwohl,D. and Cohn,D.M.
  TITLE     CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary Angioedema
  JOURNAL   N Engl J Med 390 (5), 432-441 (2024)
   PUBMED   38294975
  REMARK    GeneRIF: CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary
            Angioedema.
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Schachtl-Riess,J.F., Schonherr,S., Lamina,C., Forer,L., Coassin,S.,
            Streiter,G., Kheirkhah,A., Li,Y., Meiselbach,H., Di Maio,S.,
            Eckardt,K.U., Kottgen,A. and Kronenberg,F.
  CONSRTM   GCKD investigators
  TITLE     KLKB1 and CLSTN2 are associated with HDL-mediated cholesterol
            efflux capacity in a genome-wide association study
  JOURNAL   Atherosclerosis 368, 1-11 (2023)
   PUBMED   36812656
  REMARK    GeneRIF: KLKB1 and CLSTN2 are associated with HDL-mediated
            cholesterol efflux capacity in a genome-wide association study.
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Feng,L., Liu,Y., Chen,M. and Hu,Y.
  TITLE     [Matrix metalloproteinase 14 and plasma kallikrein 1 may be
            potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 34 (7), 676-681 (2022)
   PUBMED   36100402
  REMARK    GeneRIF: [Matrix metalloproteinase 14 and plasma kallikrein 1 may
            be potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis].
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Wan,J., Vadaq,N., Konings,J., Jaeger,M., Kumar,V., de Laat,B.,
            Joosten,L., Netea,M.G., van der Ven,A.J., de Groot,P.G., de Mast,Q.
            and Roest,M.
  TITLE     Kallikrein augments the anticoagulant function of the protein C
            system in thrombin generation
  JOURNAL   J Thromb Haemost 20 (1), 48-57 (2022)
   PUBMED   34532976
  REMARK    GeneRIF: Kallikrein augments the anticoagulant function of the
            protein C system in thrombin generation.
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Beaubien,G., Rosinski-Chupin,I., Mattei,M.G., Mbikay,M.,
            Chretien,M. and Seidah,N.G.
  TITLE     Gene structure and chromosomal localization of plasma kallikrein
  JOURNAL   Biochemistry 30 (6), 1628-1635 (1991)
   PUBMED   1993180
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Chung,D.W., Fujikawa,K., McMullen,B.A. and Davie,E.W.
  TITLE     Human plasma prekallikrein, a zymogen to a serine protease that
            contains four tandem repeats
  JOURNAL   Biochemistry 25 (9), 2410-2417 (1986)
   PUBMED   3521732
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Thompson,R.E., Mandle,R. Jr. and Kaplan,A.P.
  TITLE     Studies of binding of prekallikrein and Factor XI to high molecular
            weight kininogen and its light chain
  JOURNAL   Proc Natl Acad Sci U S A 76 (10), 4862-4866 (1979)
   PUBMED   291905
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Mandle,R.J. Jr. and Kaplan,A.P.
  TITLE     Hageman-factor-dependent fibrinolysis: generation of fibrinolytic
            activity by the interaction of human activated factor XI and
            plasminogen
  JOURNAL   Blood 54 (4), 850-862 (1979)
   PUBMED   89876
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Aznar,J.A., Espana,F., Aznar,J., Tascon,A. and Jimenez,C.
  TITLE     Fletcher factor deficiency: report of a new family
  JOURNAL   Scand J Haematol 21 (2), 94-98 (1978)
   PUBMED   694428
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Meier,H.L., Pierce,J.V., Colman,R.W. and Kaplan,A.P.
  TITLE     Activation and function of human Hageman factor. The role of high
            molecular weight kininogen and prekallikrein
  JOURNAL   J Clin Invest 60 (1), 18-31 (1977)
   PUBMED   874082
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292624.1, BC143911.1,
            AC110771.3 and AW182528.1.
            
            On Jan 8, 2016 this sequence version replaced XP_011530236.1.
            
            Summary: This gene encodes a glycoprotein that participates in the
            surface-dependent activation of blood coagulation, fibrinolysis,
            kinin generation and inflammation. The encoded preproprotein
            present in plasma as a non-covalent complex with high molecular
            weight kininogen undergoes proteolytic processing mediated by
            activated coagulation factor XII to generate a disulfide-linked,
            heterodimeric serine protease comprised of heavy and light chains.
            Certain mutations in this gene cause prekallikrein deficiency.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 1. It encodes isoform 3
            which is shorter and has a distinct N-terminus compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.2"
     Protein         1..436
                     /product="plasma kallikrein isoform 3 precursor"
                     /EC_number="3.4.21.34"
                     /note="kallikrein B, plasma (Fletcher factor) 1;
                     kininogenin; plasma prekallikrein; plasma kallikrein"
                     /calculated_mol_wt=45751
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2662
     Region          <51..82
                     /region_name="PAN_APPLE"
                     /note="PAN/APPLE-like domain; present in N-terminal (N)
                     domains of plasminogen/ hepatocyte growth factor proteins,
                     plasma prekallikrein/coagulation factor XI and microneme
                     antigen proteins, plant receptor-like protein kinases, and
                     various nematode and leech...; cl00112"
                     /db_xref="CDD:469620"
     Region          90..173
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(106,108,119)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          189..419
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            189
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(232,281,376)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(370,395,397)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..436
                     /gene="KLKB1"
                     /gene_synonym="KLK3; PKK; PKKD; PPK"
                     /coded_by="NM_001318396.2:720..2030"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:3818"
                     /db_xref="HGNC:HGNC:6371"
                     /db_xref="MIM:229000"
ORIGIN      
        1 mwmlpgfslq mllcvgpsap itptasslhs iqmygksshk geyawkiasq rnvcllktse
       61 sgtpssstpq entisgysll tckrtlpepc hskiypgvdf ggeelnvtfv kgvnvcqetc
      121 tkmircqfft ysllpedcke ekckcflrls mdgsptriay gtqgssgysl rlcntgdnsv
      181 cttktstriv ggtnsswgew pwqvslqvkl taqrhlcggs lighqwvlta ahcfdglplq
      241 dvwriysgil nlsditkdtp fsqikeiiih qnykvsegnh dialiklqap lnytefqkpi
      301 clpskgdtst iytncwvtgw gfskekgeiq nilqkvnipl vtneecqkry qdykitqrmv
      361 cagykeggkd ackgdsggpl vckhngmwrl vgitswgegc arreqpgvyt kvaeymdwil
      421 ektqssdgka qmqspa
//
LOCUS       NP_001212                499 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 3 [Homo sapiens].
ACCESSION   NP_001212
VERSION     NP_001212.2
DBSOURCE    REFSEQ: accession NM_001221.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 499)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI057019.1, DA113081.1,
            AB209288.1, AK055642.1, CF551834.1 and AC093900.3.
            
            On Dec 13, 2002 this sequence version replaced NP_001212.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extend of this RefSeq
            trasncript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2520756.1,
                                           SRR14038191.938285.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..499
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 3"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=56239
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13557.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16690701; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13557.3)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     CDS             1..499
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001221.4:671..2170"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS3703.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkes tessnttied edvkarkqei ikvteqliea
      361 inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe nalsksnkpi htiilnphvh
      421 lvgddaacia yirltqymdg sgmpktmqse etrvwhrrdg kwqnvhfhrs gsptvpikpp
      481 cipngkenfs ggtslwqni
//
LOCUS       NP_055102               1222 aa            linear   PRI 20-NOV-2025
DEFINITION  nodal modulator 1 precursor [Homo sapiens].
ACCESSION   NP_055102 XP_001716541
VERSION     NP_055102.3
DBSOURCE    REFSEQ: accession NM_014287.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1222)
  AUTHORS   Sundaram,A., Yamsek,M., Zhong,F., Hooda,Y., Hegde,R.S. and
            Keenan,R.J.
  TITLE     Substrate-driven assembly of a translocon for multipass membrane
            proteins
  JOURNAL   Nature 611 (7934), 167-172 (2022)
   PUBMED   36261522
REFERENCE   2  (residues 1 to 1222)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1222)
  AUTHORS   McGilvray,P.T., Anghel,S.A., Sundaram,A., Zhong,F., Trnka,M.J.,
            Fuller,J.R., Hu,H., Burlingame,A.L. and Keenan,R.J.
  TITLE     An ER translocon for multi-pass membrane protein biogenesis
  JOURNAL   Elife 9, e56889 (2020)
   PUBMED   32820719
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1222)
  AUTHORS   Perea,J., Garcia,J.L., Perez,J., Rueda,D., Arriba,M., Rodriguez,Y.,
            Urioste,M. and Gonzalez-Sarmiento,R.
  TITLE     NOMO-1 gene is deleted in early-onset colorectal cancer
  JOURNAL   Oncotarget 8 (15), 24429-24436 (2017)
   PUBMED   28416736
  REMARK    GeneRIF: Microsatellite-Stable (MSS) CRC showed a very high
            proportion of homozygous loss of NOMO1 (54 of 59 cases, 91.5%),
            while the deletion was observed in only 7 out of 16 MSI cases.
            Deletion of NOMO1 is a molecular marker predominantly associated
            with CRC, particularly MSS subtypes.
REFERENCE   6  (residues 1 to 1222)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   7  (residues 1 to 1222)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   8  (residues 1 to 1222)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   9  (residues 1 to 1222)
  AUTHORS   van Soest,S., Swart,J., Tijmes,N., Sandkuijl,L.A., Rommers,J. and
            Bergen,A.A.
  TITLE     A locus for autosomal recessive pseudoxanthoma elasticum, with
            penetrance of vascular symptoms in carriers, maps to chromosome
            16p13.1
  JOURNAL   Genome Res 7 (8), 830-834 (1997)
   PUBMED   9267806
REFERENCE   10 (residues 1 to 1222)
  AUTHORS   Templeton,N.S., Rodgers,L.A., Levy,A.T., Ting,K.L., Krutzsch,H.C.,
            Liotta,L.A. and Stetler-Stevenson,W.G.
  TITLE     Cloning and characterization of a novel human cDNA that has DNA
            similarity to the conserved region of the collagenase gene family
  JOURNAL   Genomics 12 (1), 175-176 (1992)
   PUBMED   1310294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136443.3, BI459869.1,
            BC065535.1, X57398.1 and AK125530.1.
            
            On or before Mar 29, 2008 this sequence version replaced
            XP_001716541.1, NP_055102.2.
            
            Summary: This gene encodes a protein originally thought to be
            related to the collagenase gene family. This gene is one of three
            highly similar genes in a region of duplication located on the p
            arm of chromosome 16. These three genes encode closely related
            proteins that may have the same function. The protein encoded by
            one of these genes has been identified as part of a protein complex
            that participates in the Nodal signaling pathway during vertebrate
            development. Mutations in ABCC6, which is located nearby, rather
            than mutations in this gene are associated with pseudoxanthoma
            elasticum (PXE). [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065535.1, SRR1803612.166766.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287667.12/ ENSP00000287667.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1222
                     /product="nodal modulator 1 precursor"
                     /note="pM5 protein, telomeric copy; nodal modulator 3; pM5
                     protein 3"
                     /calculated_mol_wt=131533
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2809
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15155.5)"
     Region          102..>556
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15155.5)"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q15155.5)"
     Region          <811..>1011
                     /region_name="ClfA"
                     /note="Clumping factor A-related surface protein, MSCRAMM
                     (microbial surface components recognizing adhesive matrix
                     molecules) family, DEv-IgG fold [Cell
                     wall/membrane/envelope biogenesis]; COG4932"
                     /db_xref="CDD:443959"
     Site            1156..1176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15155.5)"
     Region          1198..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15155.5)"
     Site            1205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6GQT9; propagated from
                     UniProtKB/Swiss-Prot (Q15155.5)"
     CDS             1..1222
                     /gene="NOMO1"
                     /gene_synonym="Nomo; PM5"
                     /coded_by="NM_014287.4:132..3800"
                     /db_xref="CCDS:CCDS10556.1"
                     /db_xref="GeneID:23420"
                     /db_xref="HGNC:HGNC:30060"
                     /db_xref="MIM:609157"
ORIGIN      
        1 mlvgqgagpl gpavvtaavv lllsgvgpah gsedivvgcg gfvksdvein yslieiklyt
       61 khgtlkyqtd capnngyfmi plydkgdfil kiepplgwsf epttvelhvd gvsdictkgg
      121 dinfvftgfs vngkvlskgq plgpagvqvs lrntgteaki qstvtqpggk faffkvlpgd
      181 yeilathptw alkeasttvr vtnsnanaas plivagynvs gsvrsdgepm kgvkfllfss
      241 lvtkedvlgc nvspvpgfqp qdeslvylcy tvsredgsfs fyslpsggyt vipfyrgeri
      301 tfdvapsrld ftvehdslki epvfhvmgfs vtgrvlngpe gdgvpeavvt lnnqikvktk
      361 adgsfrleni ttgtytihaq kehlyfetvt ikiapntpql adiiatgfsv cgqisiirfp
      421 dtvkqmnkyk vvlssqdkdk slvtvetdah gsfcfkakpg tykvqvmvpe aetragltlk
      481 pqtfpltvtn rpmmdvafvq flasvsgkvs cldtcgdllv tlqslsrqge krslqlsgkv
      541 namtftfdnv lpgkykisim hedwcwknks levevleddm savefrqtgy mlrcslshai
      601 tlefyqdgng renvgiynls kgvnrfclsk pgvykvtprs chrfeqafyt ydtsspsilt
      661 ltairhhvlg tittdkmmdv tvtikssids epalvlgplk svqelrreqq laeiearrqe
      721 rekngneege ermtkppvqe mvdelqgpfs ydfsywarsg ekitvtpssk ellfyppsme
      781 avvsgescpg klieihgkag lflegqihpe legveivise kgassplitv ftddkgaysv
      841 gplhsdleyt vtsqkegyvl tavegtigdf kayalagvsf eikaeddqpl pgvllslsgg
      901 lfrsnlltqd ngiltfsnls pgqyyfkpmm kefrfepssq mievqegqnl kititgyrta
      961 yscygtvssl ngepeqgvam eavgqndcsi ygedtvtdee gkfrlrgllp gcvyhvqlka
     1021 egndhieral phhrvievgn ndiddvniiv frqinqfdls gnvitsseyl ptlwvklyks
     1081 enldnpiqtv slgqslffhf ppllrdgeny vvlldstlpr sqydyilpqv sftavgyhkh
     1141 itlifnptrk lpeqdiaqgs yialpltllv llagynhdkl iplllqltsr lqgvralgqa
     1201 asdnsgpeda krqakkqktr rt
//
LOCUS       NP_067680                414 aa            linear   PRI 20-NOV-2025
DEFINITION  testis-specific Y-encoded-like protein 4 [Homo sapiens].
ACCESSION   NP_067680
VERSION     NP_067680.3
DBSOURCE    REFSEQ: accession NM_021648.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL134793.1, AB018264.1 and BC040453.1.
            
            On Apr 2, 2004 this sequence version replaced NP_067680.2.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR7346977.1459047.1,
                                        SRR1803612.213752.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000420283.3/ ENSP00000410943.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.1"
     Protein         1..414
                     /product="testis-specific Y-encoded-like protein 4"
                     /note="TSPY-like protein 4"
                     /calculated_mol_wt=44995
     Region          1..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ04.2)"
     Region          226..386
                     /region_name="PTZ00007"
                     /note="(NAP-L) nucleosome assembly protein -L;
                     Provisional; cl08298"
                     /db_xref="CDD:471807"
     Region          391..414
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ04.2)"
     CDS             1..414
                     /gene="TSPYL4"
                     /gene_synonym="dJ486I3.2"
                     /coded_by="NM_021648.5:68..1312"
                     /db_xref="CCDS:CCDS5106.1"
                     /db_xref="GeneID:23270"
                     /db_xref="HGNC:HGNC:21559"
                     /db_xref="MIM:619586"
ORIGIN      
        1 msgldggnkl plaqtgglaa pdhasgdpdr dqcqglreet eatqvmantg ggsletvaeg
       61 gasqdpvdcg palrvpvags rggaatkagq edappstkgl eaasaaeaad ssqkngcqlg
      121 eprgpagqka leacgagglg sqmipgkkak evttkkrais aavekegeag aameekkvvq
      181 kekkvaggvk eetrprapki nncmdsleai dqelsnvnaq adraflqler kfgrmrrlhm
      241 qrrsfiiqni pgfwvtafrn hpqlspmisg qdedmlrymi nleveelkhp ragckfkfif
      301 qgnpyfrneg lvkeyerrss grvvslstpi rwhrgqdpqa hihrnregnt ipsffnwfsd
      361 hsllefdria eiikgelwpn plqyylmgeg prrgirgppr qpvesarsfr fqsg
//
LOCUS       NP_001275711             317 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 8 isoform E [Homo sapiens].
ACCESSION   NP_001275711
VERSION     NP_001275711.1
DBSOURCE    REFSEQ: accession NM_001288782.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Ullah,A., Umair,M., Yousaf,M., Khan,S.A., Nazim-Ud-Din,M., Shah,K.,
            Ahmad,F., Azeem,Z., Ali,G., Alhaddad,B., Rafique,A., Jan,A.,
            Haack,T.B., Strom,T.M., Meitinger,T., Ghous,T. and Ahmad,W.
  TITLE     Sequence variants in four genes underlying Bardet-Biedl syndrome in
            consanguineous families
  JOURNAL   Mol Vis 23, 482-494 (2017)
   PUBMED   28761321
  REMARK    GeneRIF: Two novel mutations and three previously reported
            variants, identified in the present study, further extend the body
            of evidence implicating BBS6, BBS7, BBS8, and BBS10 in causing
            Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
  REMARK    GeneRIF: A homozygous null BBS8 mutation leads to Bardet-Biedl
            syndrome with randomization of left-right body axis symmetry, a
            known defect of the nodal cilium
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX247959.1, BX161472.1 and
            BU738965.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is involved in the formation of cilia. A
            mutation in this gene has also been implicated in nonsyndromic
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (5) differs in its 5' UTR, uses an
            alternate start codon and an alternate splice site in its 5' coding
            region, and lacks an exon in its 5' coding region, compared to
            variant 1. The encoded isoform (E) has a shorter and distinct
            N-terminus, compared to isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BX161472.1 [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..317
                     /product="tetratricopeptide repeat protein 8 isoform E"
                     /note="Bardet-Biedl syndrome type 8; TPR repeat protein 8"
                     /calculated_mol_wt=36259
     Site            order(32,35..36,38,61,64..65,68..69,71..72,95,98..99,
                     102..103,106)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          32..55
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          34..313
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          59..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          94..122
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          128..156
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(163,166..167,170..171,173,200,203..204,207..208,
                     210..211,234,237..238,241..242,245)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          163..190
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          195..228
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          233..259
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          267..292
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..317
                     /gene="TTC8"
                     /gene_synonym="BBS8; RP51"
                     /coded_by="NM_001288782.1:759..1712"
                     /note="isoform E is encoded by transcript variant 5"
                     /db_xref="GeneID:123016"
                     /db_xref="HGNC:HGNC:20087"
                     /db_xref="MIM:608132"
ORIGIN      
        1 milsyevilh aldlaalste hsqykdwwwk vqigkcyyrl gmyreaekqf ksalkqqemv
       61 dtflylakvy vsldqpvtal nlfkqgldkf pgevtllcgi ariyeemnnm ssaaeyykev
      121 lkqdnthvea iacigsnhfy sdqpeialrf yrrllqmgiy ngqlfnnlgl ccfyaqqydm
      181 tltsferals laeneeeaad vwynlghvav gigdtnlahq cfrlalvnnn nhaeaynnla
      241 vlemrkghve qarallqtas slaphmyeph fnfatisdki gdlqrsyvaa qkseaafpdh
      301 vdtqhlikql rqhfaml
//
LOCUS       NP_001357602             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001357602
VERSION     NP_001357602.1
DBSOURCE    REFSEQ: accession NM_001370673.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY208839.1, SRR1660807.4770.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001370673.1:560..1324"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_689997                798 aa            linear   PRI 20-NOV-2025
DEFINITION  cation channel sperm-associated auxiliary subunit delta precursor
            [Homo sapiens].
ACCESSION   NP_689997
VERSION     NP_689997.3
DBSOURCE    REFSEQ: accession NM_152784.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Lin,S., Ke,M., Zhang,Y., Yan,Z. and Wu,J.
  TITLE     Structure of a mammalian sperm cation channel complex
  JOURNAL   Nature 595 (7869), 746-750 (2021)
   PUBMED   34225353
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Brown,S.G., Miller,M.R., Lishko,P.V., Lester,D.H., Publicover,S.J.,
            Barratt,C.L.R. and Martins Da Silva,S.
  TITLE     Homozygous in-frame deletion in CATSPERE in a man producing
            spermatozoa with loss of CatSper function and compromised
            fertilizing capacity
  JOURNAL   Hum Reprod 33 (10), 1812-1816 (2018)
   PUBMED   30239785
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Chung,J.J., Navarro,B., Krapivinsky,G., Krapivinsky,L. and
            Clapham,D.E.
  TITLE     A novel gene required for male fertility and functional CATSPER
            channel formation in spermatozoa
  JOURNAL   Nat Commun 2, 153 (2011)
   PUBMED   21224844
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011499.5, AK128088.1 and BC043005.1.
            
            On Apr 8, 2006 this sequence version replaced NP_689997.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043005.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381624.4/ ENSP00000371037.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..798
                     /product="cation channel sperm-associated auxiliary
                     subunit delta precursor"
                     /note="transmembrane protein 146; catSperdelta;
                     catSper-delta; cation channel sperm-associated protein
                     subunit delta; cation channel sperm associated auxiliary
                     subunit delta"
                     /calculated_mol_wt=88226
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2261
     mat_peptide     21..798
                     /product="Cation channel sperm-associated auxiliary
                     subunit delta. /id=PRO_0000287150"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XM0.3)"
                     /calculated_mol_wt=88226
     Region          41..766
                     /region_name="CATSPERD"
                     /note="Cation channel sperm-associated protein subunit
                     delta; pfam15020"
                     /db_xref="CDD:464451"
     Site            123
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            230
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            240
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            538
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            630
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XM0.3)"
     Site            724..745
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XM0.3)"
     CDS             1..798
                     /gene="CATSPERD"
                     /gene_synonym="TMEM146"
                     /coded_by="NM_152784.4:102..2498"
                     /db_xref="CCDS:CCDS12149.2"
                     /db_xref="GeneID:257062"
                     /db_xref="HGNC:HGNC:28598"
                     /db_xref="MIM:617490"
ORIGIN      
        1 mlmlmlvaav tmwlrplvta qlcrsrtvrt gkvfnliqdv qgdrlyfhpt ttrlikhpce
       61 knialylgkq vfftmdnfet sllpftipts mqvgvpevts ahfagsllll vvdqkvyiyd
      121 yennswsmsl gikhpvthvs gdnccytgsl fcvhvsnlvf ayfrgdqisq tyiyysntgg
      181 fsfwkyhydr qaeiigslgg ifhffslsqv amlvvnqgkg mfkysdhpln rsfglsfdyn
      241 gtldiliapg qrgilllwfe nsllfshnag qlvdtvrvkk gdqtlfssif eakitihnia
      301 vtenelavit rednlyygnl givpssiikf adqyiwsedv almfrspgtl eiltplrdta
      361 fpafdfqkcl vniqallmdp elhvgkckie fltgefiyrm ytidmhsqle ltaslipqpg
      421 tsliplvmvs nphslgfqat fyengytsdg ntkykldifl kqqqhwgrtd snftsslkka
      481 tmstltvdia nkeiscvdik plstlisvgc dldkkiviqn kvsacsmgil dpltlqdnys
      541 fiiekefydp gfqgqqssed lhvfysyqql gcpllvyydt lwkpvvelwr kdsfqevida
      601 eyvllevngq fsysysltaq samctsqpqn wttmikefgg pffwnrenyv schdpnnnap
      661 lrwpdvqyqi lggrtanqii fghngfyvfy isivdpyysy cqletifsiy vygafpvqlv
      721 sagvvillii ssilgsvwla yktpkllrta rgrrikkcat qlcrrcktvc qfrasatara
      781 gteppgrhrt phggrsdh
//
LOCUS       NP_001308656             436 aa            linear   PRI 20-NOV-2025
DEFINITION  serine protease HTRA2, mitochondrial isoform 3 preproprotein [Homo
            sapiens].
ACCESSION   NP_001308656
VERSION     NP_001308656.1
DBSOURCE    REFSEQ: accession NM_001321727.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Aspholm,E.E., Lidman,J. and Burmann,B.M.
  TITLE     Structural basis of substrate recognition and allosteric activation
            of the proapoptotic mitochondrial HtrA2 protease
  JOURNAL   Nat Commun 15 (1), 4592 (2024)
   PUBMED   38816423
  REMARK    GeneRIF: Structural basis of substrate recognition and allosteric
            activation of the proapoptotic mitochondrial HtrA2 protease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Bi,P.Y., Killackey,S.A., Schweizer,L., Arnoult,D., Philpott,D.J.
            and Girardin,S.E.
  TITLE     Cytosolic retention of HtrA2 during mitochondrial protein import
            stress triggers the DELE1-HRI pathway
  JOURNAL   Commun Biol 7 (1), 391 (2024)
   PUBMED   38555279
  REMARK    GeneRIF: Cytosolic retention of HtrA2 during mitochondrial protein
            import stress triggers the DELE1-HRI pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Suzuki,Y., Takahashi-Niki,K., Akagi,T., Hashikawa,T. and
            Takahashi,R.
  TITLE     Mitochondrial protease Omi/HtrA2 enhances caspase activation
            through multiple pathways
  JOURNAL   Cell Death Differ 11 (2), 208-216 (2004)
   PUBMED   14605674
  REMARK    GeneRIF: protease activity of Omi/HtrA2 promotes caspase activation
            through multiple pathways
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Faccio,L., Fusco,C., Viel,A. and Zervos,A.S.
  TITLE     Tissue-specific splicing of Omi stress-regulated endoprotease leads
            to an inactive protease with a modified PDZ motif
  JOURNAL   Genomics 68 (3), 343-347 (2000)
   PUBMED   10995577
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Gray,C.W., Ward,R.V., Karran,E., Turconi,S., Rowles,A.,
            Viglienghi,D., Southan,C., Barton,A., Fantom,K.G., West,A.,
            Savopoulos,J., Hassan,N.J., Clinkenbeard,H., Hanning,C.,
            Amegadzie,B., Davis,J.B., Dingwall,C., Livi,G.P. and Creasy,C.L.
  TITLE     Characterization of human HtrA2, a novel serine protease involved
            in the mammalian cellular stress response
  JOURNAL   Eur J Biochem 267 (18), 5699-5710 (2000)
   PUBMED   10971580
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Savopoulos,J.W., Carter,P.S., Turconi,S., Pettman,G.R.,
            Karran,E.H., Gray,C.W., Ward,R.V., Jenkins,O. and Creasy,C.L.
  TITLE     Expression, purification, and functional analysis of the human
            serine protease HtrA2
  JOURNAL   Protein Expr Purif 19 (2), 227-234 (2000)
   PUBMED   10873535
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Faccio,L., Fusco,C., Chen,A., Martinotti,S., Bonventre,J.V. and
            Zervos,A.S.
  TITLE     Characterization of a novel human serine protease that has
            extensive homology to bacterial heat shock endoprotease HtrA and is
            regulated by kidney ischemia
  JOURNAL   J Biol Chem 275 (4), 2581-2588 (2000)
   PUBMED   10644717
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005041.2.
            
            Summary: This gene encodes a serine protease. The protein has been
            localized in the endoplasmic reticulum and interacts with an
            alternatively spliced form of mitogen-activated protein kinase 14.
            The protein has also been localized to the mitochondria with
            release to the cytosol following apoptotic stimulus. The protein is
            thought to induce apoptosis by binding the apoptosis inhibitory
            protein baculoviral IAP repeat-containing 4. Nuclear localization
            of this protein has also been observed. Alternate splicing of this
            gene results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF141306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..436
                     /product="serine protease HTRA2, mitochondrial isoform 3
                     preproprotein"
                     /EC_number="3.4.21.108"
                     /note="protease, serine, 25; HtrA-like serine protease;
                     high temperature requirement protein A2; Omi
                     stress-regulated endoprotease; serine protease HTRA2,
                     mitochondrial; serine protease 25; serine proteinase OMI;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=42940
     transit_peptide 1..31
                     /calculated_mol_wt=3460
     proprotein      32..436
                     /product="serine protease HTRA2, mitochondrial isoform 3
                     proprotein"
                     /calculated_mol_wt=42940
     mat_peptide     134..436
                     /product="serine protease HTRA2, mitochondrial isoform 3"
                     /calculated_mol_wt=32522
     Region          182..433
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
     CDS             1..436
                     /gene="HTRA2"
                     /gene_synonym="MGCA8; OMI; PARK13; PRSS25"
                     /coded_by="NM_001321727.1:603..1913"
                     /note="isoform 3 preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS92785.1"
                     /db_xref="GeneID:27429"
                     /db_xref="HGNC:HGNC:14348"
                     /db_xref="MIM:606441"
ORIGIN      
        1 maapragrga gwslrawral ggirwgrrpr ltpdlrallt sgtsdprarv tygtpslwar
       61 lsvgvtepra cltsgtpgpr aqltavtpdt rtreasensg trsrawlava lgaggavlll
      121 lwgggrgppa vlaavpsppp asprsqynfi advvektapa vvyieildrh pflgrevpis
      181 ngsgfvvaad glivtnahvv adrrrvrvrl lsgdtyeavv tavdpvadia tlriqtkepl
      241 ptlplgrsad vrqgefvvam gspfalqnti tsgivssaqr pardlglpqt nveyiqtdaa
      301 idfgnsggpl vnlarelgav slqdgevigv ntmkvtagis faipsdrlre flhrgekkns
      361 ssgisgsqrr yigvmmltls praglrpgdv ilaigeqmvq naedvyeavr tqsqlavqir
      421 rgretltlyv tpevte
//
LOCUS       NP_001304849             233 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001304849 XP_005260544
VERSION     NP_001304849.1
DBSOURCE    REFSEQ: accession NM_001317920.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA488236.1, AL160175.5,
            BM554265.1, DR156871.1 and BC019307.1.
            
            On Dec 15, 2015 this sequence version replaced XP_005260544.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 3, 4 and 5 encode the same isoform
            (Bcl-X(L), also known as Bcl-xL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.99598.1,
                                           SRR3476690.950881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001317920.2:213..914"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     4"
                     /db_xref="CCDS:CCDS13189.1"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001336354             600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_001336354 XP_005247611
VERSION     NP_001336354.1
DBSOURCE    REFSEQ: accession NM_001349425.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_005247611.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (14), as well as variants 7-13 and
            15, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.125625.1,
                                           SRR1660807.70126.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349425.1:250..2052"
                     /note="isoform b is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001275963             619 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin light chain 4 isoform a [Homo sapiens].
ACCESSION   NP_001275963 XP_005249530
VERSION     NP_001275963.1
DBSOURCE    REFSEQ: accession NM_001289034.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX640717.1, BC080637.1 and AK056393.1.
            
            On Jan 10, 2014 this sequence version replaced XP_005249530.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 3. Variants 1, 2 and 5
            encode the same isoform (a), which has a shorter N-terminus,
            compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.102688.1, BX640717.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..619
                     /product="kinesin light chain 4 isoform a"
                     /note="kinesin-like protein 8"
                     /calculated_mol_wt=68509
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          33..>148
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          55..88
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          154..201
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBS5; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          208..>409
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          211..244
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          212..239
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          253..286
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          253..281
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          295..328
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          295..323
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(296,299..300,303..304,306,338,341..342,345..346,
                     348..349,380,383..384,387..388,391)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          336..366
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          337..370
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          378..496
                     /region_name="TPR_12"
                     /note="Tetratricopeptide repeat; pfam13424"
                     /db_xref="CDD:315987"
     Region          379..412
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          379..406
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          464..497
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          510..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q07866; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5PQM2; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Region          598..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSK0.3)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NSK0.3)"
     CDS             1..619
                     /gene="KLC4"
                     /gene_synonym="bA387M24.3; CONDRHN; KNSL8"
                     /coded_by="NM_001289034.2:296..2155"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS4883.1"
                     /db_xref="GeneID:89953"
                     /db_xref="HGNC:HGNC:21624"
                     /db_xref="MIM:620909"
ORIGIN      
        1 msglvlgqrd epaghrlsqe eilgstrlvs qglealrseh qavlqslsqt ieclqqgghe
       61 eglvhekarq lrrsmeniel glseaqvmla lashlstves ekqklraqvr rlcqenqwlr
      121 delagtqqrl qrseqavaql eeekkhlefl gqlrqydedg htseekegda tkdslddlfp
      181 neeeedpsng lsrgqgataa qqggyeipar lrtlhnlviq yaaqgryeva vplckqaled
      241 lertsgrghp dvatmlnila lvyrdqnkyk eaahllndal sirestlgpd hpavaatlnn
      301 lavlygkrgk ykeaeplcqr aleirekvlg tnhpdvakql nnlallcqnq gkyeaveryy
      361 qralaiyegq lgpdnpnvar tknnlascyl kqgkyaeaet lykeiltrah vqefgsvddd
      421 hkpiwmhaee reemsksrhh eggtpyaeyg gwykackvss ptvnttlrnl galyrrqgkl
      481 eaaetleeca lrsrrqgtdp isqtkvaell gesdgrrtsq egpgdsvkfe ggedasvave
      541 wsgdgsgtlq rsgslgkird vlrrssellv rklqgteprp sssnmkraas lnylnqpsaa
      601 plqvsrglsa stmdlssss
//
LOCUS       NP_005171                326 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb complex protein BMI-1 [Homo sapiens].
ACCESSION   NP_005171
VERSION     NP_005171.4
DBSOURCE    REFSEQ: accession NM_005180.9
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Szustka,A. and Krzeslak,A.
  TITLE     BMI-1 in Breast Cancer - Biological Role and Clinical Implications
  JOURNAL   Cell Physiol Biochem 58 (5), 584-596 (2024)
   PUBMED   39429016
  REMARK    GeneRIF: BMI-1 in Breast Cancer - Biological Role and Clinical
            Implications.
            Review article
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Hsu,Y.C., Luo,C.W., Chang,S.J., Lai,C.Y., Yang,Y.T., Chen,Y.Z.,
            Liu,W.T., Wu,C.C., Sun,C.K., Hou,M.F. and Pan,M.R.
  TITLE     Targeting Bmi1 for Enhancing Anoikis Sensitivity and Inhibiting
            Metastasis in Colorectal Cancer
  JOURNAL   Cancer Genomics Proteomics 21 (5), 523-532 (2024)
   PUBMED   39191496
  REMARK    GeneRIF: Targeting Bmi1 for Enhancing Anoikis Sensitivity and
            Inhibiting Metastasis in Colorectal Cancer.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Li,Q., Fu,T., Wei,N., Wang,Q. and Zhang,X.
  TITLE     Bmi-1 promotes the proliferation, migration and invasion, and
            inhibits cell apoptosis of human retinoblastoma cells via RKIP
  JOURNAL   Sci Rep 14 (1), 14544 (2024)
   PUBMED   38914697
  REMARK    GeneRIF: Bmi-1 promotes the proliferation, migration and invasion,
            and inhibits cell apoptosis of human retinoblastoma cells via RKIP.
            Erratum:[Sci Rep. 2025 Aug 5;15(1):28521. doi:
            10.1038/s41598-025-11879-x. PMID: 40764337]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Park,I.K., Qian,D., Kiel,M., Becker,M.W., Pihalja,M.,
            Weissman,I.L., Morrison,S.J. and Clarke,M.F.
  TITLE     Bmi-1 is required for maintenance of adult self-renewing
            haematopoietic stem cells
  JOURNAL   Nature 423 (6937), 302-305 (2003)
   PUBMED   12714971
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Jacobs,J., Voncken,J.W., Jenkins,N.A., Copeland,N.G.,
            Satijn,D.P., Otte,A.P., Berns,A. and van Lohuizen,M.
  TITLE     MPc2, a new murine homolog of the Drosophila polycomb protein is a
            member of the mouse polycomb transcriptional repressor complex
  JOURNAL   J Mol Biol 273 (5), 993-1003 (1997)
   PUBMED   9367786
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Gunster,M.J., Satijn,D.P., Hamer,K.M., den Blaauwen,J.L., de
            Bruijn,D., Alkema,M.J., van Lohuizen,M., van Driel,R. and Otte,A.P.
  TITLE     Identification and characterization of interactions between the
            vertebrate polycomb-group protein BMI1 and human homologs of
            polyhomeotic
  JOURNAL   Mol Cell Biol 17 (4), 2326-2335 (1997)
   PUBMED   9121482
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Alkema,M.J., Bronk,M., Verhoeven,E., Otte,A., van 't Veer,L.J.,
            Berns,A. and van Lohuizen,M.
  TITLE     Identification of Bmi1-interacting proteins as constituents of a
            multimeric mammalian polycomb complex
  JOURNAL   Genes Dev 11 (2), 226-240 (1997)
   PUBMED   9009205
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Alkema,M.J., Wiegant,J., Raap,A.K., Berns,A. and van Lohuizen,M.
  TITLE     Characterization and chromosomal localization of the human
            proto-oncogene BMI-1
  JOURNAL   Hum Mol Genet 2 (10), 1597-1603 (1993)
   PUBMED   8268912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158211.29, DB225488.1,
            BC011652.2, BE008203.1 and AI274830.1.
            
            On Jan 23, 2003 this sequence version replaced NP_005171.3.
            
            Summary: This gene encodes a ring finger protein that is major
            component of the polycomb group complex 1 (PRC1). This complex
            functions through chromatin remodeling as an essential epigenetic
            repressor of multiple regulatory genes involved in embryonic
            development and self-renewal in somatic stem cells. This protein
            also plays a central role in DNA damage repair. This gene is an
            oncogene and aberrant expression is associated with numerous
            cancers and is associated with resistance to certain
            chemotherapies. A pseudogene of this gene is found on chromosome X.
            Read-through transcription also exists between this gene and the
            upstream COMM domain containing 3 (COMMD3) gene. [provided by
            RefSeq, Sep 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.241287.1,
                                           SRR1660805.206485.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376663.8/ ENSP00000365851.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..326
                     /product="polycomb complex protein BMI-1"
                     /note="murine leukemia viral (bmi-1) oncogene homolog; B
                     lymphoma Mo-MLV insertion region 1 homolog; ring finger
                     protein 51; polycomb group protein Bmi1; polycomb group
                     RING finger protein 4; BMI1 polycomb ring finger oncogene;
                     BMI1 polycomb ring finger proto-oncogene"
                     /calculated_mol_wt=36818
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          130..226
                     /region_name="RAWUL_PCGF4"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     4 (PCGF4); cd17165"
                     /db_xref="CDD:340685"
     Region          162..182
                     /region_name="Interaction with PHC2.
                     /evidence=ECO:0000269|PubMed:27827373"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          164..228
                     /region_name="Interaction with E4F1.
                     /evidence=ECO:0000269|PubMed:16882984"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     Region          236..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35226.2)"
     CDS             1..326
                     /gene="BMI1"
                     /gene_synonym="flvi-2/bmi-1; FLVI2/BMI1; PCGF4; RNF51"
                     /coded_by="NM_005180.9:618..1598"
                     /db_xref="CCDS:CCDS7138.1"
                     /db_xref="GeneID:648"
                     /db_xref="HGNC:HGNC:1066"
                     /db_xref="MIM:164831"
ORIGIN      
        1 mhrttrikit elnphlmcvl cggyfidatt iieclhsfck tcivrylets kycpicdvqv
       61 hktrpllnir sdktlqdivy klvpglfkne mkrrrdfyaa hpsadaangs nedrgevade
      121 dkriitddei islsieffdq nrldrkvnkd kekskeevnd krylrcpaam tvmhlrkflr
      181 skmdipntfq idvmyeeepl kdyytlmdia yiytwrrngp lplkyrvrpt ckrmkishqr
      241 dgltnagele sdsgsdkans paggipstss clpspstpvq sphpqfphis stmngtsnsp
      301 sgnhqssfan rprkssvngs satssg
//
LOCUS       NP_061882                274 aa            linear   PRI 20-NOV-2025
DEFINITION  toll-interacting protein isoform 1 [Homo sapiens].
ACCESSION   NP_061882
VERSION     NP_061882.2
DBSOURCE    REFSEQ: accession NM_019009.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Nouri,H.R., Schaunaman,N., Kraft,M., Li,L., Numata,M. and Chu,H.W.
  TITLE     Tollip deficiency exaggerates airway type 2 inflammation in mice
            exposed to allergen and influenza A virus: role of the ATP/IL-33
            signaling axis
  JOURNAL   Front Immunol 14, 1304758 (2023)
   PUBMED   38124753
  REMARK    GeneRIF: Tollip deficiency exaggerates airway type 2 inflammation
            in mice exposed to allergen and influenza A virus: role of the
            ATP/IL-33 signaling axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Demir,A.B., Baris,E., Kaner,U.B., Alotaibi,H., Atabey,N. and Koc,A.
  TITLE     Toll-interacting protein may affect doxorubicin resistance in
            hepatocellular carcinoma cell lines
  JOURNAL   Mol Biol Rep 50 (10), 8551-8563 (2023)
   PUBMED   37644370
  REMARK    GeneRIF: Toll-interacting protein may affect doxorubicin resistance
            in hepatocellular carcinoma cell lines.
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Kowalewski,A., Jaworski,D., Borowczak,J., Maniewski,M.,
            Szczerbowski,K., Antosik,P., Durslewicz,J., Smolinska,M.,
            Ligmanowska,J., Grzanka,D. and Szylberg,L.
  TITLE     TOLLIP Protein Expression Predicts Unfavorable Outcome in Renal
            Cell Carcinoma
  JOURNAL   Int J Mol Sci 23 (23), 14702 (2022)
   PUBMED   36499030
  REMARK    GeneRIF: TOLLIP Protein Expression Predicts Unfavorable Outcome in
            Renal Cell Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Venkatasubramanian,S., Pryor,R., Plumlee,C., Cohen,S.B.,
            Simmons,J.D., Warr,A.J., Graustein,A.D., Saha,A., Hawn,T.R.,
            Urdahl,K.B. and Shah,J.A.
  TITLE     TOLLIP Optimizes Dendritic Cell Maturation to Lipopolysaccharide
            and Mycobacterium tuberculosis
  JOURNAL   J Immunol 209 (3), 435-445 (2022)
   PUBMED   35803695
  REMARK    GeneRIF: TOLLIP Optimizes Dendritic Cell Maturation to
            Lipopolysaccharide and Mycobacterium tuberculosis.
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Jensen,L.E. and Whitehead,A.S.
  TITLE     IRAK1b, a novel alternative splice variant of interleukin-1
            receptor-associated kinase (IRAK), mediates interleukin-1 signaling
            and has prolonged stability
  JOURNAL   J Biol Chem 276 (31), 29037-29044 (2001)
   PUBMED   11397809
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Burns,K., Clatworthy,J., Martin,L., Martinon,F., Plumpton,C.,
            Maschera,B., Lewis,A., Ray,K., Tschopp,J. and Volpe,F.
  TITLE     Tollip, a new component of the IL-1RI pathway, links IRAK to the
            IL-1 receptor
  JOURNAL   Nat Cell Biol 2 (6), 346-351 (2000)
   PUBMED   10854325
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Volpe,F., Clatworthy,J., Kaptein,A., Maschera,B., Griffin,A.M. and
            Ray,K.
  TITLE     The IL1 receptor accessory protein is responsible for the
            recruitment of the interleukin-1 receptor associated kinase to the
            IL1/IL1 receptor I complex
  JOURNAL   FEBS Lett 419 (1), 41-44 (1997)
   PUBMED   9426216
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 274)
  AUTHORS   Nilsen,K.H.
  TITLE     Malignant lymphoma and rheumatic symptoms
  JOURNAL   N Z Med J 83 (563), 320-322 (1976)
   PUBMED   1085432
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB039994.1, AL136835.1 and
            AA861717.1.
            
            On Jun 10, 2002 this sequence version replaced NP_061882.1.
            
            Summary: This gene encodes a ubiquitin-binding protein that
            interacts with several Toll-like receptor (TLR) signaling cascade
            components. The encoded protein regulates inflammatory signaling
            and is involved in interleukin-1 receptor trafficking and in the
            turnover of IL1R-associated kinase. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.450488.1,
                                           SRR1660805.26131.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317204.11/ ENSP00000314733.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..274
                     /product="toll-interacting protein isoform 1"
                     /note="Toll-interacting protein; adapter protein"
                     /calculated_mol_wt=30151
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          52..172
                     /region_name="C2_Tollip"
                     /note="C2 domain present in Toll-interacting protein
                     (Tollip); cd04016"
                     /db_xref="CDD:175983"
     Site            order(74,121,123,129)
                     /site_type="other"
                     /note="putative Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175983"
     Region          133..136
                     /region_name="AIM1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          151..154
                     /region_name="AIM2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0E2.1)"
     Region          230..270
                     /region_name="CUE_TOLIP"
                     /note="CUE domain found in the C-terminal of
                     toll-interacting protein (Tollip) and similar proteins;
                     cd14363"
                     /db_xref="CDD:270546"
     CDS             1..274
                     /gene="TOLLIP"
                     /gene_synonym="IL-1RAcPIP"
                     /coded_by="NM_019009.4:135..959"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7723.1"
                     /db_xref="GeneID:54472"
                     /db_xref="HGNC:HGNC:16476"
                     /db_xref="MIM:606277"
ORIGIN      
        1 mattvstqrg pvyigelpqd flritptqqq rqvqldaqaa qqlqyggavg tvgrlnitvv
       61 qaklaknygm trmdpycrlr lgyavyetpt ahngaknprw nkvihctvpp gvdsfyleif
      121 derafsmddr iawthitipe slrqgkvedk wyslsgrqgd dkegminlvm syallpaamv
      181 mppqpvvlmp tvyqqgvgyv pitgmpavcs pgmvpvalpp aavnaqprcs eedlkaiqdm
      241 fpnmdqevir svleaqrgnk daainsllqm geep
//
LOCUS       NP_001338572             959 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001338572 XP_016884617
VERSION     NP_001338572.1
DBSOURCE    REFSEQ: accession NM_001351643.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 959)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 959)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 959)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 959)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 959)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 959)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 959)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, AL954743.9,
            AL671545.13 and AL096767.14.
            
            On May 17, 2017 this sequence version replaced XP_016884617.1.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Transcript Variant: This variant (7), as well as variant 1, encodes
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.113282.1,
                                           SRR7346977.1765658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..959
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=104104
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          408..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          657..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          <703..950
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3Q2; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          812..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     CDS             1..959
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001351643.2:498..3377"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS74881.1"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlvsthhl
      541 hsssededie gafpnelslq qafsdyqiqq mtanfvdqfg fndeefadqd dninapfdri
      601 aeinfnidad edspsaalfe accsdriqpf dddedediwe dsdtrcaarv marprfgaph
      661 asescskngp erggqdgkas leahrdapga gappapgkke appvegdseg amwtavfdep
      721 anstptapgv vrdvgssvwa agtsapeekg wakftdfqpf ccsesgprcs spvdtecsha
      781 egsrsqgpek afspaspcaw nvcvtrkapl lasdssssgg shsedgdqka asamdavsrg
      841 pgreapplpt varteeavgr vgcadsrlls pacpapkevt aapavavppe atvaittals
      901 kagpaiptpa vssalavavp lgpimavtaa pamvatlgtv tkdgktdapp egaalngpv
//
LOCUS       NP_001003785             137 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP synthase peripheral stalk subunit d, mitochondrial isoform b
            [Homo sapiens].
ACCESSION   NP_001003785
VERSION     NP_001003785.1
DBSOURCE    REFSEQ: accession NM_001003785.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Katz Shroitman,N., Yitzhaky,A., Ben Shachar,D., Gurwitz,D. and
            Hertzberg,L.
  TITLE     Meta-analysis of brain samples of individuals with schizophrenia
            detects down-regulation of multiple ATP synthase encoding genes in
            both females and males
  JOURNAL   J Psychiatr Res 158, 350-359 (2023)
   PUBMED   36640659
  REMARK    GeneRIF: Meta-analysis of brain samples of individuals with
            schizophrenia detects down-regulation of multiple ATP synthase
            encoding genes in both females and males.
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Song,K.H., Kim,J.H., Lee,Y.H., Bae,H.C., Lee,H.J., Woo,S.R.,
            Oh,S.J., Lee,K.M., Yee,C., Kim,B.W., Cho,H., Chung,E.J.,
            Chung,J.Y., Hewitt,S.M., Chung,T.W., Ha,K.T., Bae,Y.K., Mao,C.P.,
            Yang,A., Wu,T.C. and Kim,T.W.
  TITLE     Mitochondrial reprogramming via ATP5H loss promotes multimodal
            cancer therapy resistance
  JOURNAL   J Clin Invest 128 (9), 4098-4114 (2018)
   PUBMED   30124467
  REMARK    GeneRIF: ATP5H loss in the tumor is strongly linked to failure of
            therapy, disease progression, and poor survival in patients with
            cancer.
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Aggeler,R., Coons,J., Taylor,S.W., Ghosh,S.S., Garcia,J.J.,
            Capaldi,R.A. and Marusich,M.F.
  TITLE     A functionally active human F1F0 ATPase can be purified by
            immunocapture from heart tissue and fibroblast cell lines. Subunit
            structure and activity studies
  JOURNAL   J Biol Chem 277 (37), 33906-33912 (2002)
   PUBMED   12110673
REFERENCE   7  (residues 1 to 137)
  AUTHORS   Wang,H. and Oster,G.
  TITLE     Energy transduction in the F1 motor of ATP synthase
  JOURNAL   Nature 396 (6708), 279-282 (1998)
   PUBMED   9834036
REFERENCE   8  (residues 1 to 137)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   9  (residues 1 to 137)
  AUTHORS   Higuti,T., Kuroiwa,K., Miyazaki,S., Yoshihara,Y., Toda,H.,
            Kakuno,T. and Sakiyama,F.
  TITLE     The complete amino acid sequence of subunit d of rat liver
            mitochondrial H(+)-ATP synthase
  JOURNAL   J Biochem 114 (5), 714-717 (1993)
   PUBMED   7509337
REFERENCE   10 (residues 1 to 137)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032245.1 and AA608885.1.
            
            Summary: Mitochondrial ATP synthase catalyzes ATP synthesis,
            utilizing an electrochemical gradient of protons across the inner
            membrane during oxidative phosphorylation. It is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, which comprises the proton
            channel. The F1 complex consists of 5 different subunits (alpha,
            beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3
            beta, and a single representative of the other 3. The Fo seems to
            have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene
            encodes the d subunit of the Fo complex. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. In addition, three pseudogenes are
            located on chromosomes 9, 12 and 15. [provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (2) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            isoform (b), that is missing an internal segment compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032245.1, DRR138512.601131.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..137
                     /product="ATP synthase peripheral stalk subunit d,
                     mitochondrial isoform b"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit d; ATP synthase, H+ transporting,
                     mitochondrial F1F0, subunit d; ATP synthase peripheral
                     stalk subunit d, mitochondrial; ATP synthase, H+
                     transporting, mitochondrial Fo complex, subunit d; My032
                     protein; ATP synthase D chain, mitochondrial; ATP synthase
                     subunit d, mitochondrial; ATPase subunit d; ATP synthase,
                     H+ transporting, mitochondrial Fo complex subunit D"
                     /calculated_mol_wt=15642
     Region          3..131
                     /region_name="Mt_ATP-synt_D"
                     /note="ATP synthase D chain, mitochondrial (ATP5H);
                     pfam05873"
                     /db_xref="CDD:461764"
     CDS             1..137
                     /gene="ATP5PD"
                     /gene_synonym="APT5H; ATP5H; ATPQ"
                     /coded_by="NM_001003785.2:55..468"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32727.1"
                     /db_xref="GeneID:10476"
                     /db_xref="HGNC:HGNC:845"
                     /db_xref="MIM:618121"
ORIGIN      
        1 magrklalkt idwvafaeii pqnqkaiass lkswnetlts rlaalpenpp aidwayykan
       61 vakaglvddf ekkvkscaew vslskarive yekemekmkn lipfdqmtie dlneafpetk
      121 ldkkkypywp hqpienl
//
LOCUS       NP_001356454             152 aa            linear   PRI 20-NOV-2025
DEFINITION  protein eva-1 homolog A [Homo sapiens].
ACCESSION   NP_001356454
VERSION     NP_001356454.1
DBSOURCE    REFSEQ: accession NM_001369525.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Chen,Y., Wang,D., Yin,J., Krafft,P.R., Luo,X., Hao,D., Li,C.,
            Liu,Y., Li,L., Zhang,Y. and Zhu,C.
  TITLE     Increased TMEM166 Level in Patients with Postoperative Stroke after
            Carotid Endarterectomy
  JOURNAL   Neuroscience 549, 138-144 (2024)
   PUBMED   38734302
  REMARK    GeneRIF: Increased TMEM166 Level in Patients with Postoperative
            Stroke after Carotid Endarterectomy.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Canham,L., Sendac,S., Diagbouga,M.R., Wolodimeroff,E., Pirri,D.,
            Tardajos Ayllon,B., Feng,S., Souilhol,C., Chico,T.J.A., Evans,P.C.
            and Serbanovic-Canic,J.
  TITLE     EVA1A (Eva-1 Homolog A) Promotes Endothelial Apoptosis and
            Inflammatory Activation Under Disturbed Flow Via Regulation of
            Autophagy
  JOURNAL   Arterioscler Thromb Vasc Biol 43 (4), 547-561 (2023)
   PUBMED   36794585
  REMARK    GeneRIF: EVA1A (Eva-1 Homolog A) Promotes Endothelial Apoptosis and
            Inflammatory Activation Under Disturbed Flow Via Regulation of
            Autophagy.
            Erratum:[Arterioscler Thromb Vasc Biol. 2023 Jun;43(6):e230. doi:
            10.1161/ATV.0000000000000163. PMID: 37224275]
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Xu,Q., Liao,Z., Gong,Z., Liu,X., Yang,Y., Wang,Z., Yang,W., Hou,L.,
            Yang,J., Song,J., Liu,W., Wang,B., Hua,J., Pu,M. and Li,N.
  TITLE     Down-regulation of EVA1A by miR-103a-3p promotes hepatocellular
            carcinoma cells proliferation and migration
  JOURNAL   Cell Mol Biol Lett 27 (1), 93 (2022)
   PUBMED   36273122
  REMARK    GeneRIF: Down-regulation of EVA1A by miR-103a-3p promotes
            hepatocellular carcinoma cells proliferation and migration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Liao,Z., Gong,Z., Wang,Z., Yang,W., Liu,W., Hou,L., Liu,X., Hua,J.,
            Wang,B. and Li,N.
  TITLE     The Degradation of TMEM166 by Autophagy Promotes AMPK Activation to
            Protect SH-SY5Y Cells Exposed to MPP
  JOURNAL   Cells 11 (17), 2706 (2022)
   PUBMED   36078115
  REMARK    GeneRIF: The Degradation of TMEM166 by Autophagy Promotes AMPK
            Activation to Protect SH-SY5Y Cells Exposed to MPP().
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Xu,D., Yang,F., He,H., Hu,J., Lv,X., Ma,D. and Chen,Y.Y.
  TITLE     Expression of TMEM166 protein in human normal and tumor tissues
  JOURNAL   Appl Immunohistochem Mol Morphol 21 (6), 543-552 (2013)
   PUBMED   22495369
  REMARK    GeneRIF: TMEM166 expression was widely down-regulated in the cancer
            tissues.
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Li,L., Khatibi,N.H., Hu,Q., Yan,J., Chen,C., Han,J., Ma,D., Chen,Y.
            and Zhou,C.
  TITLE     Transmembrane protein 166 regulates autophagic and apoptotic
            activities following focal cerebral ischemic injury in rats
  JOURNAL   Exp Neurol 234 (1), 181-190 (2012)
   PUBMED   22227058
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Sun,W., Ma,X.M., Bai,J.P., Zhang,G.Q., Zhu,Y.J., Ma,H.M., Guo,H.,
            Chen,Y.Y. and Ding,J.B.
  TITLE     Transmembrane protein 166 expression in esophageal squamous cell
            carcinoma in Xinjiang, China
  JOURNAL   Asian Pac J Cancer Prev 13 (8), 3713-3716 (2012)
   PUBMED   23098460
  REMARK    GeneRIF: Low TMEM166 mRNA and protein expression is associated with
            esophageal squamous cell carcinoma.
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Wang,L., Yu,C., Lu,Y., He,P., Guo,J., Zhang,C., Song,Q., Ma,D.,
            Shi,T. and Chen,Y.
  TITLE     TMEM166, a novel transmembrane protein, regulates cell autophagy
            and apoptosis
  JOURNAL   Apoptosis 12 (8), 1489-1502 (2007)
   PUBMED   17492404
  REMARK    GeneRIF: TMEM166 is a novel regulator involved in both autophagy
            and apoptosis.
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP276065.1, BE892427.1, BC063016.1 and AK023453.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI837841.1, SRR9304717.360788.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p12"
     Protein         1..152
                     /product="protein eva-1 homolog A"
                     /note="transmembrane protein 166; protein FAM176A; family
                     with sequence similarity 176, member A"
                     /calculated_mol_wt=17339
     Region          1..60
                     /region_name="Necessary for the localization and
                     biological activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Region          13..152
                     /region_name="FAM176"
                     /note="FAM176 family; pfam14851"
                     /db_xref="CDD:464347"
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Region          70..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91WM6; propagated from
                     UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q9H8M9.1)"
     CDS             1..152
                     /gene="EVA1A"
                     /gene_synonym="FAM176A; TMEM166"
                     /coded_by="NM_001369525.1:540..998"
                     /db_xref="CCDS:CCDS1959.1"
                     /db_xref="GeneID:84141"
                     /db_xref="HGNC:HGNC:25816"
                     /db_xref="MIM:618990"
ORIGIN      
        1 mrlplshspe hvemallsni laaysfvsen peraalyfvs gvciglvltl aalvirisch
       61 tdcrrrpgkk flqdresssd ssdsedgsed tvsdlsvrrh rrfertlnkn vftsaeeler
      121 aqrleereri ireiwmngqp evpgtrslnr yy
//
LOCUS       NP_001300880             303 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 2 [Homo sapiens].
ACCESSION   NP_001300880 XP_011522373
VERSION     NP_001300880.1
DBSOURCE    REFSEQ: accession NM_001313951.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP225027.1, BE797606.1 and
            BC009751.2.
            
            On Sep 15, 2015 this sequence version replaced XP_011522373.1.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (5) contains a novel exon in the
            5' region, which results in translation initiation from an in-frame
            downstream start codon compared to variant 1. Variants 5 and 2
            encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1163657.249763.1, SRR1163655.470237.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed/partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..303
                     /product="aurora kinase B isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=34629
     Region          29..298
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(42..45,48,50,63,65,97,113..116,159,163..164,166,
                     176..177)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..303
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_001313951.1:251..1162"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58514.1"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 msrsnvqpta apgqkvmens sgtpdiltrh ftiddfeigr plgkgkfgnv ylarekkshf
       61 ivalkvlfks qiekegvehq lrreieiqah lhhpnilrly nyfydrrriy lileyaprge
      121 lykelqksct fdeqrtatim eeladalmyc hgkkvihrdi kpenlllglk gelkiadfgw
      181 svhapslrrk tmcgtldylp pemiegrmhn ekvdlwcigv lcyellvgnp pfesashnet
      241 yrrivkvdlk fpasvpmgaq dliskllrhn pserlplaqv sahpwvrans rrvlppsalq
      301 sva
//
LOCUS       NP_001336296             271 aa            linear   PRI 20-NOV-2025
DEFINITION  centromere protein K isoform 3 [Homo sapiens].
ACCESSION   NP_001336296 XP_011541836
VERSION     NP_001336296.1
DBSOURCE    REFSEQ: accession NM_001349367.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Li,G., Shen,J., Cheng,W., Wang,X., Wang,D., Song,Y., Chen,Y.,
            Li,X., Zhang,M., Ding,Y., Ma,X., Qian,Q., Zhang,G., Ji,J. and
            Liu,B.
  TITLE     CENPK orchestrates ovarian cancer progression via GOLPH3-Mediated
            activation of mTOR signaling
  JOURNAL   Mol Cell Endocrinol 589, 112253 (2024)
   PUBMED   38670220
  REMARK    GeneRIF: CENPK orchestrates ovarian cancer progression via
            GOLPH3-Mediated activation of mTOR signaling.
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Li,X., Han,Y.R., Xuefeng,X., Ma,Y.X., Xing,G.S., Yang,Z.W.,
            Zhang,Z., Shi,L. and Wu,X.L.
  TITLE     Lentivirus-mediated short hairpin RNA interference of CENPK
            inhibits growth of colorectal cancer cells with overexpression of
            Cullin 4A
  JOURNAL   World J Gastroenterol 28 (37), 5420-5443 (2022)
   PUBMED   36312839
  REMARK    GeneRIF: Lentivirus-mediated short hairpin RNA interference of
            CENPK inhibits growth of colorectal cancer cells with
            overexpression of Cullin 4A.
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Tian,H., Wang,F., Deng,Y., Ying,L., Fang,W., Chen,D., Miao,C.,
            Li,H., Sun,S., Ma,Y., Cai,H. and Guo,T.
  TITLE     Centromeric protein K (CENPK) promotes gastric cancer proliferation
            and migration via interacting with XRCC5
  JOURNAL   Gastric Cancer 25 (5), 879-895 (2022)
   PUBMED   35715658
  REMARK    GeneRIF: Centromeric protein K (CENPK) promotes gastric cancer
            proliferation and migration via interacting with XRCC5.
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Okada,M., Cheeseman,I.M., Hori,T., Okawa,K., McLeod,I.X.,
            Yates,J.R. 3rd, Desai,A. and Fukagawa,T.
  TITLE     The CENP-H-I complex is required for the efficient incorporation of
            newly synthesized CENP-A into centromeres
  JOURNAL   Nat Cell Biol 8 (5), 446-457 (2006)
   PUBMED   16622420
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Yamashita,A., Ito,M., Takamatsu,N. and Shiba,T.
  TITLE     Characterization of Solt, a novel SoxLZ/Sox6 binding protein
            expressed in adult mouse testis
  JOURNAL   FEBS Lett 481 (2), 147-151 (2000)
   PUBMED   10996314
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Taki,T., Hayashi,Y., Taniwaki,M., Seto,M., Ueda,R., Hanada,R.,
            Suzukawa,K., Yokota,J. and Morishita,K.
  TITLE     Fusion of the MLL gene with two different genes, AF-6 and
            AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8
            and 11 in infant leukemia
  JOURNAL   Oncogene 13 (10), 2121-2130 (1996)
   PUBMED   8950979
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG502832.1, BC005400.1, BG527280.1 and BC008504.1.
            
            On Mar 15, 2017 this sequence version replaced XP_011541836.1.
            
            Summary: CENPK is a subunit of a CENPH (MIM 605607)-CENPI (MIM
            300065)-associated centromeric complex that targets CENPA (MIM
            117139) to centromeres and is required for proper kinetochore
            function and mitotic progression (Okada et al., 2006 [PubMed
            16622420]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            an alternate splice site in its 5' coding region, resulting in use
            of an alternate start codon, compared to variant 1. The encoded
            isoform (3) has a slightly longer, but distinct N-terminus compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.1352282.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..271
                     /product="centromere protein K isoform 3"
                     /note="leucine zipper protein FKSG14; SoxLZ/Sox6-binding
                     protein Solt; protein AF-5alpha; interphase centromere
                     complex protein 37"
                     /calculated_mol_wt=31771
     Region          12..271
                     /region_name="CENP-K"
                     /note="Centromere-associated protein K; pfam11802"
                     /db_xref="CDD:463355"
     CDS             1..271
                     /gene="CENPK"
                     /gene_synonym="AF5alpha; CENP-K; FKSG14; P33; Solt"
                     /coded_by="NM_001349367.2:125..940"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:64105"
                     /db_xref="HGNC:HGNC:29479"
                     /db_xref="MIM:611502"
ORIGIN      
        1 mtlfqedldp dsttdvgdvt nteeelirec eemwkdmeec qnklsligte tltdsnaqls
       61 llimqvkclt aelsqwqkkt petipltedv litlgkeefq klrqdlemvl stkesknekl
      121 kedlereqrw ldeqqqimes lnvlhselkn kvetfsesri fnelktkmln ikeykeklls
      181 tlgefledhf plpdrsvkkk kkniqessvn litlhemlei linrlfdvph dpyvkisdsf
      241 wppyvelllr ngialrhped ptrirleafh q
//
LOCUS       NP_001116297             608 aa            linear   PRI 20-NOV-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001116297
VERSION     NP_001116297.1
DBSOURCE    REFSEQ: accession NM_001122825.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Wang,P., Gao,X., Zheng,W. and Zhang,J.
  TITLE     Potential impact of epithelial splicing regulatory protein 1
            (ESRP1) associated with tumor immunity in pancreatic adenocarcinoma
  JOURNAL   J Proteomics 308, 105277 (2024)
   PUBMED   39127164
  REMARK    GeneRIF: Potential impact of epithelial splicing regulatory protein
            1 (ESRP1) associated with tumor immunity in pancreatic
            adenocarcinoma.
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Chen,S., Zong,Y., Hou,Z., Deng,Z. and Xia,Z.
  TITLE     Splicing factor ESRP1 derived circ_0068162 promotes the progression
            of oral squamous cell carcinoma via the miR-186/JAG axis
  JOURNAL   Carcinogenesis 45 (3), 107-118 (2024)
   PUBMED   37966490
  REMARK    GeneRIF: Splicing factor ESRP1 derived circ_0068162 promotes the
            progression of oral squamous cell carcinoma via the miR-186/JAG
            axis.
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Liu,D., Dredge,B.K., Bert,A.G., Pillman,K.A., Toubia,J., Guo,W.,
            Dyakov,B.J.A., Migault,M.M., Conn,V.M., Conn,S.J., Gregory,P.A.,
            Gingras,A.C., Patel,D., Wu,B. and Goodall,G.J.
  TITLE     ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA
  JOURNAL   Nucleic Acids Res 52 (3), 1387-1403 (2024)
   PUBMED   38015468
  REMARK    GeneRIF: ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA.
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Wang,W., Taufalele,P.V., Millet,M., Homsy,K., Smart,K.,
            Berestesky,E.D., Schunk,C.T., Rowe,M.M., Bordeleau,F. and
            Reinhart-King,C.A.
  TITLE     Matrix stiffness regulates tumor cell intravasation through
            expression and ESRP1-mediated alternative splicing of MENA
  JOURNAL   Cell Rep 42 (4), 112338 (2023)
   PUBMED   37027295
  REMARK    GeneRIF: Matrix stiffness regulates tumor cell intravasation
            through expression and ESRP1-mediated alternative splicing of MENA.
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Warzecha,C.C., Shen,S., Xing,Y. and Carstens,R.P.
  TITLE     The epithelial splicing factors ESRP1 and ESRP2 positively and
            negatively regulate diverse types of alternative splicing events
  JOURNAL   RNA Biol 6 (5), 546-562 (2009)
   PUBMED   19829082
  REMARK    GeneRIF: results further establish ESRP1 and ESRP2 as global
            regulators of an epithelial splicing regulatory network.
REFERENCE   7  (residues 1 to 608)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
  REMARK    GeneRIF: ESRP1 and ESRP2 are epithelial cell-type-specific
            regulators of FGFR2 splicing.
REFERENCE   8  (residues 1 to 608)
  AUTHORS   Leontieva,O.V. and Ionov,Y.
  TITLE     RNA-binding motif protein 35A is a novel tumor suppressor for
            colorectal cancer
  JOURNAL   Cell Cycle 8 (3), 490-497 (2009)
   PUBMED   19177006
  REMARK    GeneRIF: Results demonstrate that RBM35A functions as a tumor
            suppressor in colon cancer cells, and suggest that RBM35A is
            involved in posttranscriptional regulation of a number of genes by
            exerting a differential effect on protein translation via 5'UTRs of
            mRNAs.
REFERENCE   9  (residues 1 to 608)
  AUTHORS   Rohan,S., Tu,J.J., Kao,J., Mukherjee,P., Campagne,F., Zhou,X.K.,
            Hyjek,E., Alonso,M.A. and Chen,Y.T.
  TITLE     Gene expression profiling separates chromophobe renal cell
            carcinoma from oncocytoma and identifies vesicular transport and
            cell junction proteins as differentially expressed genes
  JOURNAL   Clin Cancer Res 12 (23), 6937-6945 (2006)
   PUBMED   17145811
  REMARK    GeneRIF: The FLJ20171 gene was shown to effectively separate these
            two chromophobe renal cell carcinoma (RCC) and benign oncocytoma
            groups by quantitative reverse transcription-PCR using fresh tissue
            samples, with similar trends seen on formalin-fixed tissues.
REFERENCE   10 (residues 1 to 608)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647570.1, BC019932.3, BG212336.1, BG182742.1, BC052574.1 and
            AI990751.1.
            
            Summary: ESPR1 is an epithelial cell-type-specific splicing
            regulator (Warzecha et al., 2009 [PubMed 19285943]).[supplied by
            OMIM, Aug 2009].
            
            Transcript Variant: This variant (4) lacks multiple exons in the 3'
            coding region, compared to variant 1, which results in a protein
            (isoform 4) with a shorter, distinct C-terminus when compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019932.3, DRR138512.124239.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..608
                     /product="epithelial splicing regulatory protein 1 isoform
                     4"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=67534
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM1_ESRP1"
                     /note="RNA recognition motif 1 (RRM1) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12736"
                     /db_xref="CDD:410134"
     Region          310..419
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     Site            582
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     CDS             1..608
                     /gene="ESRP1"
                     /gene_synonym="DFNB109; RBM35A; RMB35A"
                     /coded_by="NM_001122825.2:146..1972"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS47896.1"
                     /db_xref="GeneID:54845"
                     /db_xref="HGNC:HGNC:25966"
                     /db_xref="MIM:612959"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illfwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki dveslssasq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdidkldvat mteylnfeks ssvsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcskmel iddntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptppii pvlpqqfvpp tnvrdcirlr glpyaatied ildflgefat dirthgvhmv
      481 lnhqgrpsgd afiqmksadr afmaaqkchk knmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppcklp clsppsytfp apaaviptea aiyqpsviln pralqpstay ypagtqlfmn
      601 ytayypsv
//
LOCUS       NP_001353145             853 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001353145 XP_011510808
VERSION     NP_001353145.1
DBSOURCE    REFSEQ: accession NM_001366216.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 853)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 853)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 853)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 853)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 853)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_011510808.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.138505.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..853
                     /product="disks large homolog 1 isoform 12"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=95035
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..172
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          171..259
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(182..188,205,208,238,242,245..246)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          268..352
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(277..283,300,303,333,337,340..341)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          353..414
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          412..502
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(424..430,441,444,474,478,481..482)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          531..597
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(536,558..559,580)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(539,541,544,553,571..572,591,593..594)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          662..840
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..853
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366216.1:495..3056"
                     /note="isoform 12 is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS93449.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kvngtdadye yeeitlergn
      181 sglgfsiagg tdnphigdds sifitkiitg gaaaqdgrlr vndcilrvne vdvrdvthsk
      241 avealkeags ivrlyvkrrk pvsekimeik likgpkglgf siaggvgnqh ipgdnsiyvt
      301 kiieggaahk dgklqigdkl lavnnvclee vtheeavtal kntsdfvylk vakptsmymn
      361 dgyappditn sssqpvdnhv spssflgqtp asparyspvs kavlgddeit reprkvvlhr
      421 gstglgfniv ggedgegifi sfilaggpad lsgelrkgdr iisvnsvdlr aasheqaaaa
      481 lknagqavti vaqyrpeeys rfeakihdlr eqmmnssiss gsgslrtsqk rslyvralfd
      541 ydktkdsglp sqglnfkfgd ilhvinasdd ewwqarqvtp dgesdevgvi pskrrvekke
      601 rarlktvkfn sktrdkgeip ddmgskglkh vtsnasdses syrgqeeyvl syepvnqqev
      661 nytrpviilg pmkdrinddl isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek
      721 diqehkfiea gqynnhlygt svqsvrevae kgkhcildvs gnaikrlqia qlypisifik
      781 pksmenimem nkrlteeqar ktferamkle qeftehftai vqgdtlediy nqvkqiieeq
      841 sgsyiwvpak ekl
//
LOCUS       NP_001273061             340 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p40 isoform b [Homo sapiens].
ACCESSION   NP_001273061 XP_005248877
VERSION     NP_001273061.1
DBSOURCE    REFSEQ: accession NM_001286132.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Mattijssen,S., Hinson,E.R., Onnekink,C., Hermanns,P., Zabel,B.,
            Cresswell,P. and Pruijn,G.J.
  TITLE     Viperin mRNA is a novel target for the human RNase MRP/RNase P
            endoribonuclease
  JOURNAL   Cell Mol Life Sci 68 (14), 2469-2480 (2011)
   PUBMED   21053045
  REMARK    GeneRIF: Data idenified two cleavage sites for RNase MRP/RNase P in
            the coding sequence of viperin mRNA.
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Welting,T.J., Kikkert,B.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Differential association of protein subunits with the human RNase
            MRP and RNase P complexes
  JOURNAL   RNA 12 (7), 1373-1382 (2006)
   PUBMED   16723659
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Welting,T.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Mutual interactions between subunits of the human RNase MRP
            ribonucleoprotein complex
  JOURNAL   Nucleic Acids Res 32 (7), 2138-2146 (2004)
   PUBMED   15096576
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Jarrous,N., Eder,P.S., Guerrier-Takada,C., Hoog,C. and Altman,S.
  TITLE     Autoantigenic properties of some protein subunits of catalytically
            active complexes of human ribonuclease P
  JOURNAL   RNA 4 (4), 407-417 (1998)
   PUBMED   9630247
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX951376.1, BC017871.1, BM015573.1, BU607286.1 and AL359643.27.
            
            On Oct 30, 2013 this sequence version replaced XP_005248877.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (b) that is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017871.1, ERR279837.1801.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p25.1"
     Protein         1..340
                     /product="ribonuclease P protein subunit p40 isoform b"
                     /EC_number="3.1.26.5"
                     /note="ribonuclease P (40 kD); ribonuclease P, 40kD
                     subunit; ribonuclease P1; ribonuclease P protein subunit
                     p40; RNase P subunit 1; RNaseP protein p40; ribonuclease
                     P/MRP 40kDa subunit"
                     /calculated_mol_wt=39196
     Region          75..320
                     /region_name="Ribonuc_P_40"
                     /note="Ribonuclease P 40kDa (Rpp40) subunit; pfam08584"
                     /db_xref="CDD:462526"
     CDS             1..340
                     /gene="RPP40"
                     /gene_synonym="bA428J1.3; RNASEP1"
                     /coded_by="NM_001286132.2:36..1058"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS69040.1"
                     /db_xref="GeneID:10799"
                     /db_xref="HGNC:HGNC:20992"
                     /db_xref="MIM:606117"
ORIGIN      
        1 matlrrlrea prhllvceks nfgnhksrhr hlvqthyyny rvsflipecg ilseelknlv
       61 mntgpyyfvk nlplhelitp efistfikkg klilsldkdt yeetglqghp sqfsgrkimk
      121 fivsidlmel slnldskkye riswsfkekk plkfdfllaw hktgseestm msyfskyqiq
      181 ehqpkvalst lrdlqcpvlq sselegtpev scralelfdw lgavfsnvdl nnepnnfist
      241 yccpepstvv akaylctitg filpekicll lehlchyfde pklapwvtls vqgfadspvs
      301 weknehgfrk ggehlynfvi fnnqdywlqm avgandhcpp
//
LOCUS       NP_054790               2063 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 1 [Homo sapiens].
ACCESSION   NP_054790
VERSION     NP_054790.2
DBSOURCE    REFSEQ: accession NM_014071.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2063)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2063)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 2063)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 2063)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 2063)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 2063)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 2063)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 2063)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 2063)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 2063)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18, CR749037.1,
            BC069829.1, AL109824.24 and AI498955.1.
            
            On Jun 27, 2003 this sequence version replaced NP_054790.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 3. Variants 1 and 3 encode the same isoform (1, also
            known as NCOA6-alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069829.1, SRR14038193.623769.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359003.7/ ENSP00000351894.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2063
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2063
                     /product="nuclear receptor coactivator 6 isoform 1"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=219015
     Region          1..1310
                     /region_name="NCOA1-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..1057
                     /region_name="CREBBP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..928
                     /region_name="TBP/GTF2A-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <152..544
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          281..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          520..>838
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          773..927
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          789..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          887..891
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          899..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1047
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <1056..1302
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1058
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1096
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1310..1353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1448..1474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1491..1495
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1641..2063
                     /region_name="EP300/CRSP3-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1738..1820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1819
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1822
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1837..1908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1995..2063
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            2018
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..2063
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_014071.5:344..6535"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13241.1"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglgg mpkrlppgfs agqanpnfmq gqvpsttatt
      541 pgnsgapqlq anqnvqhagg qgagppqnqm qvshgppnmm qpslmgihgn mnnqqagtsg
      601 vpqvnlsnmq gqpqqgppsq lmgmhqqivp sqgqmvqqqg tlnpqnpmil sraqlmpqgq
      661 mmvnppsqnl gpspqrmtpp kqmlsqqgpq mmaphnqmmg pqgqvllqqn pmieqimtnq
      721 mqgnkqqfnt qnqsnvmpgp aqimrgptpn mqgnmvqftg qmsgqmlpqq gpvnnspsqv
      781 mgiqgqvlrp pgpsphmaqq hgdpattann dvslsqmmpd vsiqqtnmvp phvqamqgns
      841 asgnhfsghg msfnapfsga pngnqmscgq npgfpvnkdv tltspllvnl lqsdisaghf
      901 gvnnkqnntn ankpkkkkpp rkkknsqqdl ntpdtrpagl eeadqpplpg eqginldnsg
      961 pklpefsnrp pgypsqpveq rplqqmppql mqhvapppqp pqqqpqpqlp qqqqppppsq
     1021 pqsqqqqqqq qqmmmmlmmq qdpksvrlpv sqnvhpprgp lnpdsqrmpm qqsgsvpvmv
     1081 slqgpasvpp spdkqrmpmp vntplgsnsr kmvyqespqn psssplaema slpeasgsea
     1141 psvpggpnnm pshvvlpqnq lmmtgpkpgp splsatqgat pqqppvnslp sshghhfpnv
     1201 aaptqtsrpk tpnrasprpy ypqtpnnrpp stepseisls perlnasiag lfppqinipl
     1261 pprpnlnrgf dqqglnpttl kaigqapsnl tmnpsnfatp qthkldsvvv nsgkqsnsga
     1321 tkraspsnsr rsspgssrkt tpspgrqnsk apkltlasqt naallqnvel prnvlvsptp
     1381 lanppvpgsf pnnsglnpqn stvsvaavgg vvednkesln vpqdsdcqns qsrkeqvnie
     1441 lkavpaqevk mvvpedqskk dgqpsdpnkl psveenknlv spamreapts lsqlldnsga
     1501 pnvtikppgl tdlevtppvv sgedlkkasv iptlqdlsss kepsnslnlp hsnelcsslv
     1561 hpelsevssn vapsippvms rpvssssist plppnqitvf vtsnpittsa ntsaalpthl
     1621 qsalmstvvt mpnagskvmv segqsaaqsn arpqfitpvf insssiiqvm kgsqpstipa
     1681 aplttnsglm ppsvavvgpl hipqnikfss apvppnalss spapniqtgr plvlssratp
     1741 vqlpsppcts spvvpshppv qqvkelnpde aspqvntsad qntlpssqst tmvsplltns
     1801 pgssgnrrsp vssskgkgkv dkigqilltk ackkvtgsle kgeeqygadg etegqgldtt
     1861 apglmgteql steldsktpt ppaptllkmt sspvgpgtas agpslpggal ptsvrsivtt
     1921 lvpselisav pttksnhggi aseslagglv eekvgshpel lpsiapsqnl vsketsttal
     1981 qasvarpele vnaaivsgqs sepkeiveks kipgrrnsrt eeptvasesv enghrkrssr
     2041 pasassstkd itsavqskrr ksk
//
LOCUS       NP_060557                674 aa            linear   PRI 20-NOV-2025
DEFINITION  nucleoporin NDC1 isoform 1 [Homo sapiens].
ACCESSION   NP_060557
VERSION     NP_060557.3
DBSOURCE    REFSEQ: accession NM_018087.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Smits,D.J., Dekker,J., Douben,H., Schot,R., Magee,H., Bakhtiari,S.,
            Koehler,K., Huebner,A., Schuelke,M., Darvish,H., Vosoogh,S.,
            Tafakhori,A., Jameie,M., Taghiabadi,E., Wilson,Y., Shah,M., van
            Slegtenhorst,M.A., Medici-van den Herik,E.G., van Ham,T.J.,
            Kruer,M.C. and Mancini,G.M.S.
  TITLE     Biallelic NDC1 variants that interfere with ALADIN binding are
            associated with neuropathy and triple A-like syndrome
  JOURNAL   HGG Adv 5 (4), 100327 (2024)
   PUBMED   39003500
  REMARK    GeneRIF: Biallelic NDC1 variants that interfere with ALADIN binding
            are associated with neuropathy and triple A-like syndrome.
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Liu,Y.P., Guo,G., Ren,M., Li,Y.R., Guo,D., She,J.J. and He,S.X.
  TITLE     NDC1 promotes hepatocellular carcinoma tumorigenesis by targeting
            BCAP31 to activate PI3K/AKT signaling
  JOURNAL   J Biochem Mol Toxicol 38 (2), e23647 (2024)
   PUBMED   38348718
  REMARK    GeneRIF: NDC1 promotes hepatocellular carcinoma tumorigenesis by
            targeting BCAP31 to activate PI3K/AKT signaling.
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Jiang,X.Y., Wang,L., Liu,Z.Y., Song,W.X., Zhou,M. and Xi,L.
  TITLE     TMEM48 promotes cell proliferation and invasion in cervical cancer
            via activation of the Wnt/beta-catenin pathway
  JOURNAL   J Recept Signal Transduct Res 41 (4), 371-377 (2021)
   PUBMED   32896205
  REMARK    GeneRIF: TMEM48 promotes cell proliferation and invasion in
            cervical cancer via activation of the Wnt/beta-catenin pathway.
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Akkafa,F., Koyuncu,I., Temiz,E., Dagli,H., Dilmec,F. and Akbas,H.
  TITLE     miRNA-mediated apoptosis activation through TMEM 48 inhibition in
            A549 cell line
  JOURNAL   Biochem Biophys Res Commun 503 (1), 323-329 (2018)
   PUBMED   29906465
  REMARK    GeneRIF: miR-421 can suppress TMEM48 so that leads the non-small
            cancer cell lines (A549) to apoptosis.
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Larder,R., Sim,M.F.M., Gulati,P., Antrobus,R., Tung,Y.C.L.,
            Rimmington,D., Ayuso,E., Polex-Wolf,J., Lam,B.Y.H., Dias,C.,
            Logan,D.W., Virtue,S., Bosch,F., Yeo,G.S.H., Saudek,V.,
            O'Rahilly,S. and Coll,A.P.
  TITLE     Obesity-associated gene TMEM18 has a role in the central control of
            appetite and body weight regulation
  JOURNAL   Proc Natl Acad Sci U S A 114 (35), 9421-9426 (2017)
   PUBMED   28811369
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Lau,C.K., Delmar,V.A. and Forbes,D.J.
  TITLE     Topology of yeast Ndc1p: predictions for the human NDC1/NET3
            homologue
  JOURNAL   Anat Rec A Discov Mol Cell Evol Biol 288 (7), 681-694 (2006)
   PUBMED   16779818
  REMARK    GeneRIF: Human homologue NDC1/NET3 contains three FG repeats in the
            C-terminus, a feature of many nuclear pore proteins.
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Stavru,F., Hulsmann,B.B., Spang,A., Hartmann,E., Cordes,V.C. and
            Gorlich,D.
  TITLE     NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear
            pore complexes
  JOURNAL   J Cell Biol 173 (4), 509-519 (2006)
   PUBMED   16702233
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Mansfeld,J., Guttinger,S., Hawryluk-Gara,L.A., Pante,N., Mall,M.,
            Galy,V., Haselmann,U., Muhlhausser,P., Wozniak,R.W., Mattaj,I.W.,
            Kutay,U. and Antonin,W.
  TITLE     The conserved transmembrane nucleoporin NDC1 is required for
            nuclear pore complex assembly in vertebrate cells
  JOURNAL   Mol Cell 22 (1), 93-103 (2006)
   PUBMED   16600873
REFERENCE   9  (residues 1 to 674)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 674)
  AUTHORS   Schirmer,E.C., Florens,L., Guan,T., Yates,J.R. 3rd and Gerace,L.
  TITLE     Nuclear membrane proteins with potential disease links found by
            subtractive proteomics
  JOURNAL   Science 301 (5638), 1380-1382 (2003)
   PUBMED   12958361
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC003082.2, AL049745.9 and AL354612.1.
            
            On Dec 11, 2009 this sequence version replaced NP_060557.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1509546.1,
                                           SRR18074969.2807434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371429.4/ ENSP00000360483.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..674
                     /product="nucleoporin NDC1 isoform 1"
                     /note="nucleoporin NDC1; transmembrane protein 48; nuclear
                     division cycle 1 homolog"
                     /calculated_mol_wt=76174
     Region          20..667
                     /region_name="Ndc1_Nup"
                     /note="Nucleoporin protein Ndc1-Nup; pfam09531"
                     /db_xref="CDD:462824"
     Site            25..45
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            69..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            166..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            273..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Region          394..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BTX1.2)"
     CDS             1..674
                     /gene="NDC1"
                     /gene_synonym="NEDAPA; NET3; TMEM48"
                     /coded_by="NM_018087.5:36..2060"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS583.1"
                     /db_xref="GeneID:55706"
                     /db_xref="HGNC:HGNC:25525"
                     /db_xref="MIM:610115"
ORIGIN      
        1 matavsrpca grsrdilwrv lgwrivasiv wsvlflpict tvfiifsrid lfhpiqwlsd
       61 sfsdlyssyv ifyflllsvv iiiisifnve fyavvpsipc srlaligkii hpqqlmhsfi
      121 haamgmvmaw caavitqgqy sflvvpctgt nsfgspaaqt clneyhlffl ltgafmgysy
      181 sllyfvnnmn ylpfpiiqqy kflrfrrsll llvkhscves lflvrnfcil yyflgyipka
      241 wistamnlhi deqvhrpldt vsgllnlsll yhvwlcgvfl lttwyvswil fkiyateahv
      301 fpvqppfaeg sdeclpkvln snpppiikyl alqdlmllsq yspsrrqevf slsqpgghph
      361 nwtaisrecl nllngmtqkl ilyqeaaatn grvsssypve pkklnspeet afqtpkssqm
      421 prpsvpplvk tslfssklst pdvvspfgtp fgssvmnrma gifdvntcyg spqspqlirr
      481 gprlwtsasd qqmtefsnps pstsisaegk tmrqpsviys wiqnkreqik nflskrvlim
      541 yffskhpeas iqavfsdaqm hiwaleglsh lvaasftedr fgvvqttlpa ilntlltlqe
      601 avdkyfklph asskpprisg slvdtsyktl rfafraslkt aiyritttfg ehlnavqasa
      661 ehqkrlqqfl efke
//
LOCUS       NP_543142                553 aa            linear   PRI 20-NOV-2025
DEFINITION  organic anion transporter 7 [Homo sapiens].
ACCESSION   NP_543142
VERSION     NP_543142.2
DBSOURCE    REFSEQ: accession NM_080866.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Nies,A.T., Weiss,S., Schaeffeler,E., Hannemann,A., Volker,U.,
            Wallaschofski,H. and Schwab,M.
  TITLE     The Membrane Transporter OAT7 (SLC22A9) Is Not a Susceptibility
            Factor for Osteoporosis in Europeans
  JOURNAL   Front Endocrinol (Lausanne) 11, 532 (2020)
   PUBMED   33013684
  REMARK    GeneRIF: The Membrane Transporter OAT7 (SLC22A9) Is Not a
            Susceptibility Factor for Osteoporosis in Europeans.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Mathialagan,S., Costales,C., Tylaska,L., Kimoto,E., Vildhede,A.,
            Johnson,J., Johnson,N., Sarashina,T., Hashizume,K.,
            Isringhausen,C.D., Vermeer,L.M.M., Wolff,A.R. and Rodrigues,A.D.
  TITLE     In vitro studies with two human organic anion transporters: OAT2
            and OAT7
  JOURNAL   Xenobiotica 48 (10), 1037-1049 (2018)
   PUBMED   28945155
  REMARK    GeneRIF: two human organic anion transporters OAT2 and OAT7
            activities were assessed.
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Vildhede,A., Kimoto,E., Rodrigues,A.D. and Varma,M.V.S.
  TITLE     Quantification of Hepatic Organic Anion Transport Proteins OAT2 and
            OAT7 in Human Liver Tissue and Primary Hepatocytes
  JOURNAL   Mol Pharm 15 (8), 3227-3235 (2018)
   PUBMED   29906129
  REMARK    GeneRIF: Large interindividual variability was noted in the hepatic
            expression of OAT2 (16-fold in human liver tissue and 23-fold in
            hepatocytes). OAT7, on the other hand, showed less interindividual
            variability (4-fold) in the livers, but high variability for the
            hepatocyte lots (27-fold). A significant positive correlation in
            OAT2 and OAT7 expression was observed, but expression levels were
            neither associated with age nor sex.
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Emami Riedmaier,A., Burk,O., van Eijck,B.A., Schaeffeler,E.,
            Klein,K., Fehr,S., Biskup,S., Muller,S., Winter,S., Zanger,U.M.,
            Schwab,M. and Nies,A.T.
  TITLE     Variability in hepatic expression of organic anion transporter
            7/SLC22A9, a novel pravastatin uptake transporter: impact of
            genetic and regulatory factors
  JOURNAL   Pharmacogenomics J 16 (4), 341-351 (2016)
   PUBMED   26239079
  REMARK    GeneRIF: Pravastatin is the first identified OAT7 drug substrate.
            Substantial inter-individual variability in hepatic OAT7
            expression, majorly driven by HNF4alpha, may contribute to
            pravastatin drug disposition and might affect response.
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Zhou,F., Hong,M. and You,G.
  TITLE     Regulation of human organic anion transporter 4 by progesterone and
            protein kinase C in human placental BeWo cells
  JOURNAL   Am J Physiol Endocrinol Metab 293 (1), E57-E61 (2007)
   PUBMED   17341544
  REMARK    GeneRIF: Both progesterone and activation of PKC inhibited hOAT4
            activity through redistribution of the transporter from cell
            surface to the intracellular compartments.
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Ekaratanawong,S., Anzai,N., Jutabha,P., Miyazaki,H., Noshiro,R.,
            Takeda,M., Kanai,Y., Sophasan,S. and Endou,H.
  TITLE     Human organic anion transporter 4 is a renal apical organic
            anion/dicarboxylate exchanger in the proximal tubules
  JOURNAL   J Pharmacol Sci 94 (3), 297-304 (2004)
   PUBMED   15037815
REFERENCE   8  (residues 1 to 553)
  AUTHORS   Ugele,B., St-Pierre,M.V., Pihusch,M., Bahn,A. and Hantschmann,P.
  TITLE     Characterization and identification of steroid sulfate transporters
            of human placenta
  JOURNAL   Am J Physiol Endocrinol Metab 284 (2), E390-E398 (2003)
   PUBMED   12409283
  REMARK    GeneRIF: uptake of steroid sulfates by isolated trophoblasts is
            mediated by OATP-B and OAT-4 suggesting a physiological role of
            both carrier proteins in placental uptake of fetal-derived steroid
            sulfates.
REFERENCE   9  (residues 1 to 553)
  AUTHORS   Sun,W., Wu,R.R., van Poelje,P.D. and Erion,M.D.
  TITLE     Isolation of a family of organic anion transporters from human
            liver and kidney
  JOURNAL   Biochem Biophys Res Commun 283 (2), 417-422 (2001)
   PUBMED   11327718
REFERENCE   10 (residues 1 to 553)
  AUTHORS   Cha,S.H., Sekine,T., Kusuhara,H., Yu,E., Kim,J.Y., Kim,D.K.,
            Sugiyama,Y., Kanai,Y. and Endou,H.
  TITLE     Molecular cloning and characterization of multispecific organic
            anion transporter 4 expressed in the placenta
  JOURNAL   J Biol Chem 275 (6), 4507-4512 (2000)
   PUBMED   10660625
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001880.4, AK074246.1, AF440402.1 and AP000484.5.
            
            On Feb 12, 2004 this sequence version replaced NP_543142.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF440402.1, AB074812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279178.4/ ENSP00000279178.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..553
                     /product="organic anion transporter 7"
                     /note="organic anion transporter 4; organic
                     anion/short-chain fatty acid exchanger; solute carrier
                     family 22 (organic anion/cation transporter), member 9;
                     solute carrier family 22 (organic anion transporter),
                     member 9"
                     /calculated_mol_wt=62038
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Region          109..517
                     /region_name="MFS_OAT"
                     /note="Organic anion transporters of the Major Facilitator
                     Superfamily of transporters; cd17374"
                     /db_xref="CDD:340932"
     Site            order(126..127,130..131,134,160,210..211,213..215,218,234,
                     237..238,241,358,361..362,365..367,370,390,394,445..446,
                     450,454,470,473..474,477..478,481)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340932"
     Site            144..164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            178..198
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            204..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            351..369
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            379..399
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            408..428
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            437..457
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            470..490
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Site            496..516
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     Region          528..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVM8.1)"
     CDS             1..553
                     /gene="SLC22A9"
                     /gene_synonym="HOAT4; OAT4; OAT7; ust3; UST3H"
                     /coded_by="NM_080866.3:273..1934"
                     /db_xref="CCDS:CCDS8043.1"
                     /db_xref="GeneID:114571"
                     /db_xref="HGNC:HGNC:16261"
                     /db_xref="MIM:607579"
ORIGIN      
        1 mafqdllgha gdlwrfqilq tvflsifava tylhfmlenf tafipghrcw vhildndtvs
       61 dndtgalsqd allrisipld snmrpekcrr fvhpqwqllh lngtfpntsd admepcvdgw
      121 vydrisfsst ivtewdlvcd sqsltsvakf vfmagmmvgg ilgghlsdrf grrfvlrwcy
      181 lqvaivgtca alaptfliyc slrflsgiaa mslitntiml iaewathrfq amgitlgmcp
      241 sgiafmtlag lafairdwhi lqlvvsvpyf vifltsswll esarwliinn kpeeglkelr
      301 kaahrsgmkn ardtltleil kstmkkelea aqkkkpslce mlhmpnickr isllsftrfa
      361 nfmayfglnl hvqhlgnnvf llqtlfgavi llancvapwa lkymnrrasq mllmfllaic
      421 llaiifvpqe mqtlrevlat lglgasalan tlafahgnev iptiiraram ginatfania
      481 galaplmmil svyspplpwi iygvfpfisg faflllpetr nkplfdtiqd eknerkdpre
      541 pkqedprvev tqf
//
LOCUS       NP_001339873             676 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 16 [Homo sapiens].
ACCESSION   NP_001339873
VERSION     NP_001339873.1
DBSOURCE    REFSEQ: accession NM_001352944.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.79137.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..676
                     /product="DNA repair-scaffolding protein isoform 16"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=74045
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14159.2)"
     Region          11..197
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          56..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14159.2)"
     Region          349..>608
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..676
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352944.1:82..2112"
                     /note="isoform 16 is encoded by transcript variant 19"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mprgsrargs krkrswntec psfpgerplq vrraglrtag aaaslseawl rcgegfqnts
       61 gnpsltaeek titekhlelc prpkqettts kstsgltdit wsssgsdlsd edktlsqlqr
      121 grksgvltvk ilelheecam qvamceqllg spatsssqsv aprpgaglkv lftketagyl
      181 rgrpqdtvri fppwqkliip sgscpvilnt yfcekvvake dsektcevyc pdiplprrsi
      241 slaqmfvikg ltnnspeiqv vcsgvattgt awthghkeak qriptstplr dslldvvesq
      301 gaaswpgagv rvvvqrvysl psrdstrgqq gassghtdpa gtracllvqd acgmfgevhl
      361 eftmskarql egkscslvgm kvlqkvtrgr tagifslidt lwppaiplkt pgrdqpceei
      421 kthlpppalc yiltahpnlg qidiidedpi yklyqppvtr clrdilqmnd lgtrcsfyat
      481 viyqkpqlks lllleqreiw llvtdvtlqt keerdprlpk tllvyvaplc vlgsevleal
      541 agaaphslff kdalrdqgri vcaertvlll qkpllsvvsg asscelpgpv mldsldsatp
      601 vnsicsvqel rseecprkgs gvvklfcpvr nrppdqlhwi ggnrasecrr glcrtlavaa
      661 gsvnfamwlq gwwwww
//
LOCUS       NP_060676                796 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 35 [Homo sapiens].
ACCESSION   NP_060676
VERSION     NP_060676.2
DBSOURCE    REFSEQ: accession NM_018206.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 796)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 796)
  AUTHORS   Rowlands,J. and Moore,D.J.
  TITLE     VPS35 and retromer dysfunction in Parkinson's disease
  JOURNAL   Philos Trans R Soc Lond B Biol Sci 379 (1899), 20220384 (2024)
   PUBMED   38368930
  REMARK    GeneRIF: VPS35 and retromer dysfunction in Parkinson's disease.
            Review article
REFERENCE   3  (residues 1 to 796)
  AUTHORS   Shiraishi,T., Bono,K., Hiraki,H., Manome,Y., Oka,H., Iguchi,Y. and
            Okano,H.J.
  TITLE     The impact of VPS35 D620N mutation on alternative autophagy and its
            reversal by estrogen in Parkinson's disease
  JOURNAL   Cell Mol Life Sci 81 (1), 103 (2024)
   PUBMED   38409392
  REMARK    GeneRIF: The impact of VPS35 D620N mutation on alternative
            autophagy and its reversal by estrogen in Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 796)
  AUTHORS   Zhou,Q., Qi,F., Zhou,C., Ji,J., Jiang,J., Wang,C., Zhao,Q., Jin,Y.,
            Wu,J., Cai,Q., Tian,H. and Zhang,J.
  TITLE     VPS35 promotes gastric cancer progression through integrin/FAK/SRC
            signalling-mediated IL-6/STAT3 pathway activation in a
            YAP-dependent manner
  JOURNAL   Oncogene 43 (2), 106-122 (2024)
   PUBMED   37950040
  REMARK    GeneRIF: VPS35 promotes gastric cancer progression through
            integrin/FAK/SRC signalling-mediated IL-6/STAT3 pathway activation
            in a YAP-dependent manner.
REFERENCE   5  (residues 1 to 796)
  AUTHORS   Zhang,P., Yu,L., Gao,J., Fu,Q., Dai,F., Zhao,Y., Zheng,L. and
            Zhao,S.
  TITLE     Cloning and characterization of human VPS35 and mouse Vps35 and
            mapping of VPS35 to human chromosome 16q13-q21
  JOURNAL   Genomics 70 (2), 253-257 (2000)
   PUBMED   11112353
REFERENCE   6  (residues 1 to 796)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   7  (residues 1 to 796)
  AUTHORS   Edgar,A.J. and Polak,J.M.
  TITLE     Human homologues of yeast vacuolar protein sorting 29 and 35
  JOURNAL   Biochem Biophys Res Commun 277 (3), 622-630 (2000)
   PUBMED   11062004
REFERENCE   8  (residues 1 to 796)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   9  (residues 1 to 796)
  AUTHORS   Dulski,J., Ross,O.A. and Wszolek,Z.K.
  TITLE     VPS35-Related Parkinson Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   28796472
REFERENCE   10 (residues 1 to 796)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007225.2 and AC012186.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 30, 2001 this sequence version replaced NP_060676.1.
            
            Summary: This gene belongs to a group of vacuolar protein sorting
            (VPS) genes. The encoded protein is a component of a large
            multimeric complex, termed the retromer complex, involved in
            retrograde transport of proteins from endosomes to the trans-Golgi
            network. The close structural similarity between the yeast and
            human proteins that make up this complex suggests a similarity in
            function. Expression studies in yeast and mammalian cells indicate
            that this protein interacts directly with VPS35, which serves as
            the core of the retromer complex. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093036.1, SRR11853566.10248.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299138.12/ ENSP00000299138.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..796
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q11.2"
     Protein         1..796
                     /product="vacuolar protein sorting-associated protein 35"
                     /note="maternal-embryonic 3; hVPS35; vacuolar protein
                     sorting 35 homolog"
                     /calculated_mol_wt=91576
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96QK1.2)"
     Region          15..752
                     /region_name="Vps35"
                     /note="Vacuolar protein sorting-associated protein 35;
                     pfam03635"
                     /db_xref="CDD:427414"
     Region          25..44
                     /region_name="Interaction with SNX3.
                     /evidence=ECO:0000269|PubMed:24344282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK1.2)"
     Region          205..215
                     /region_name="Interaction with SNX3.
                     /evidence=ECO:0000269|PubMed:24344282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK1.2)"
     Region          438..796
                     /region_name="Interaction with SLC11A2.
                     /evidence=ECO:0000269|PubMed:24344282"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK1.2)"
     Region          500..693
                     /region_name="Interaction with IGF2R cytoplasmic domain.
                     /evidence=ECO:0000269|PubMed:15078903"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QK1.2)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQH3; propagated from
                     UniProtKB/Swiss-Prot (Q96QK1.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQH3; propagated from
                     UniProtKB/Swiss-Prot (Q96QK1.2)"
     CDS             1..796
                     /gene="VPS35"
                     /gene_synonym="MEM3; PARK17"
                     /coded_by="NM_018206.6:46..2436"
                     /db_xref="CCDS:CCDS10721.1"
                     /db_xref="GeneID:55737"
                     /db_xref="HGNC:HGNC:13487"
                     /db_xref="MIM:601501"
ORIGIN      
        1 mpttqqspqd eqeklldeai qavkvqsfqm krcldknklm dalkhasnml gelrtsmlsp
       61 ksyyelymai sdelhylevy ltdefakgrk vadlyelvqy agniiprlyl litvgvvyvk
      121 sfpqsrkdil kdlvemcrgv qhplrglflr nyllqctrni lpdegeptde ettgdisdsm
      181 dfvllnfaem nklwvrmqhq ghsrdrekre rerqelrilv gtnlvrlsql egvnverykq
      241 ivltgileqv vncrdalaqe ylmeciiqvf pdefhlqtln pflracaelh qnvnvkniii
      301 alidrlalfa hredgpgipa diklfdifsq qvatviqsrq dmpsedvvsl qvslinlamk
      361 cypdrvdyvd kvlettveif nklnlehiat ssavskeltr llkipvdtyn niltvlklkh
      421 fhplfeyfdy esrksmscyv lsnvldynte ivsqdqvdsi mnlvstliqd qpdqpvedpd
      481 pedfadeqsl vgrfihllrs edpdqqylil ntarkhfgag gnqrirftlp plvfaayqla
      541 frykenskvd dkwekkcqki fsfahqtisa likaelaelp lrlflqgala ageigfenhe
      601 tvayefmsqa fslyedeisd skaqlaaitl iigtfermkc fseenheplr tqcalaaskl
      661 lkkpdqgrav stcahlfwsg rntdkngeel hggkrvmecl kkalkianqc mdpslqvqlf
      721 ieilnryiyf yekendavti qvlnqliqki redlpnless eeteqinkhf hntlehlrlr
      781 respesegpi yeglil
//
LOCUS       NP_060417                888 aa            linear   PRI 20-NOV-2025
DEFINITION  molybdenum cofactor sulfurase [Homo sapiens].
ACCESSION   NP_060417
VERSION     NP_060417.4
DBSOURCE    REFSEQ: accession NM_017947.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Peretz,H., Lagziel,A., Bittner,F., Kabha,M., Shtauber-Naamati,M.,
            Zhuravel,V., Usher,S., Rump,S., Wollers,S., Bork,B., Mandel,H.,
            Falik-Zaccai,T., Kalfon,L., Graessler,J., Zeharia,A., Heib,N.,
            Shalev,H., Landau,D. and Levartovsky,D.
  TITLE     Classical Xanthinuria in Nine Israeli Families and Two Isolated
            Cases from Germany: Molecular, Biochemical and Population Genetics
            Aspects
  JOURNAL   Biomedicines 9 (7), 788 (2021)
   PUBMED   34356852
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Rontani,P., Perche,O., Greetham,L., Jullien,N., Gepner,B.,
            Feron,F., Nivet,E. and Erard-Garcia,M.
  TITLE     Impaired expression of the COSMOC/MOCOS gene unit in ASD patient
            stem cells
  JOURNAL   Mol Psychiatry 26 (5), 1606-1618 (2021)
   PUBMED   32327736
  REMARK    GeneRIF: Impaired expression of the COSMOC/MOCOS gene unit in ASD
            patient stem cells.
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Taheri,M., Noroozi,R., Aghaei,K., Omrani,M.D. and Ghafouri-Fard,S.
  TITLE     The rs594445 in MOCOS gene is associated with risk of autism
            spectrum disorder
  JOURNAL   Metab Brain Dis 35 (3), 497-501 (2020)
   PUBMED   31900757
  REMARK    GeneRIF: The rs594445 in MOCOS gene is associated with risk of
            autism spectrum disorder.
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Peretz,H., Naamati,M.S., Levartovsky,D., Lagziel,A., Shani,E.,
            Horn,I., Shalev,H. and Landau,D.
  TITLE     Identification and characterization of the first mutation
            (Arg776Cys) in the C-terminal domain of the Human Molybdenum
            Cofactor Sulfurase (HMCS) associated with type II classical
            xanthinuria
  JOURNAL   Mol Genet Metab 91 (1), 23-29 (2007)
   PUBMED   17368066
  REMARK    GeneRIF: Two mutations, both in the N-terminal domain of the Human
            Molybdenum Cofactor Sulfurase (HMCS), were reported in patients
            with type II xanthinuria.
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Yamamoto,T., Moriwaki,Y., Takahashi,S., Tsutsumi,Z., Tuneyoshi,K.,
            Matsui,K., Cheng,J. and Hada,T.
  TITLE     Identification of a new point mutation in the human molybdenum
            cofactor sulferase gene that is responsible for xanthinuria type II
  JOURNAL   Metabolism 52 (11), 1501-1504 (2003)
   PUBMED   14624414
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Ichida,K., Matsumura,T., Sakuma,R., Hosoya,T. and Nishino,T.
  TITLE     Mutation of human molybdenum cofactor sulfurase gene is responsible
            for classical xanthinuria type II
  JOURNAL   Biochem Biophys Res Commun 282 (5), 1194-1200 (2001)
   PUBMED   11302742
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023043.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_060417.3.
            
            Summary: This gene encodes an enzyme that sulfurates the molybdenum
            cofactor which is required for activation of the xanthine
            dehydrogenase (XDH) and aldehyde oxidase (AO) enzymes. XDH
            catalyzes the conversion of hypoxanthine to uric acid via xanthine,
            as well as the conversion of allopurinol to oxypurinol, and
            pyrazinamide to 5-hydroxy pyrazinamide. Mutations in this gene
            cause the metabolic disorder classical xanthinuria type II which is
            characterized by the loss of XDH/XO and AO enzyme activity,
            decreased levels of uric acid in the urine, increased levels of
            xanthine and hypoxanthine in the serum and urine, formation of
            xanthine stones in the urinary tract, and myositis due to tissue
            deposition of xanthine. [provided by RefSeq, Apr 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000740.1, AK222886.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261326.6/ ENSP00000261326.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..888
                     /product="molybdenum cofactor sulfurase"
                     /EC_number="2.8.1.9"
                     /note="human molybdenum cofactor sulfurase"
                     /calculated_mol_wt=97989
     Region          28..866
                     /region_name="PLN02724"
                     /note="Molybdenum cofactor sulfurase"
                     /db_xref="CDD:215384"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96EN8.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EN8.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EN8.2)"
     CDS             1..888
                     /gene="MOCOS"
                     /gene_synonym="HMCS; MCS; MOS"
                     /coded_by="NM_017947.4:44..2710"
                     /db_xref="CCDS:CCDS11919.1"
                     /db_xref="GeneID:55034"
                     /db_xref="HGNC:HGNC:18234"
                     /db_xref="MIM:613274"
ORIGIN      
        1 magaaaesgr elwtfagsrd psaprlaygy gpgslrelra refsrlagtv yldhagatlf
       61 sqsqlesfts dlmentygnp hsqnissklt hdtveqvryr ilahfhttae dytviftags
      121 taalklvaea fpwvsqgpes sgsrfcyltd shtsvvgmrn vtmainvist pvrpedlwsa
      181 eersasasnp dcqlphlfcy paqsnfsgvr yplswieevk sgrlhpvstp gkwfvlldaa
      241 syvstspldl sahqadfvpi sfykifgfpt glgallvhnr aapllrktyf gggtasayla
      301 gedfyiprqs vaqrfedgti sfldvialkh gfdtlerltg gmenikqhtf tlaqytyval
      361 sslqypngap vvriysdsef sspevqgpii nfnvlddkgn iigysqvdkm aslynihlrt
      421 gcfcntgacq rhlgisnemv rkhfqaghvc gdnmdlidgq ptgsvrisfg ymstlddvqa
      481 flrfiidtrl hssgdwpvpq ahadtgetga psadsqadvi pavmgrrsls pqedaltgsr
      541 vwnnsstvna vpvappvcdv artqptpsek aagvlegalg phvvtnlyly pikscaafev
      601 trwpvgnqgl lydrswmvvn hngvclsqkq eprlcliqpf idlrqrimvi kakgmepiev
      661 pleensertq irqsrvcadr vstydcgeki sswlstffgr pchlikqssn sqrnakkkhg
      721 kdqlpgtmat lslvneaqyl lintssilel hrqlntsden gkeelfslkd lslrfranii
      781 ingkrafeee kwdeisigsl rfqvlgpchr cqmicidqqt gqrnqhvfqk lsesretkvn
      841 fgmylmhasl dlsspcflsv gsqvlpvlke nveghdlpas ekhqdvts
//
LOCUS       NP_001230436             396 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 5 [Homo sapiens].
ACCESSION   NP_001230436
VERSION     NP_001230436.1
DBSOURCE    REFSEQ: accession NM_001243507.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 396)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 396)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 396)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 396)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096634.2, DB220304.1,
            AK131193.1, AB362218.1, AB020639.1 and BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (8) lacks a 5' exon and an
            internal in-frame exon but has three alternate 5' exons and uses a
            downstream AUG start codon, compared to variant 1. The resulting
            isoform (5, also known as ERRgamma3) is shorter at the N-terminus
            and lacks an internal segment corresponding to the second zinc
            finger motif of the DNA binding domain (PMID:16460929), compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131193.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..396
                     /product="estrogen-related receptor gamma isoform 5"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=43942
     Region          99..156
                     /region_name="NR_DBD_like"
                     /note="DNA-binding domain of nuclear receptors is composed
                     of two C4-type zinc fingers; cl02596"
                     /db_xref="CDD:413390"
     Region          175..394
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(203,206,210,213,251,264,268,278..280,373,376,378)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(218,232,235..236,239..240,386..387,390..391)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            314
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..396
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243507.2:745..1935"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS58060.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgvrldr vrggrqkykr ridaenspyl npqlvqpakk pynkivshll
      181 vaepekiyam pdptvpdsdi kalttlcdla drelvviigw akhipgfstl sladqmsllq
      241 sawmeililg vvyrslsfed elvyaddyim dedqsklagl ldlnnailql vkkyksmkle
      301 keefvtlkai alansdsmhi edveavqklq dvlhealqdy eagqhmedpr ragkmlmtlp
      361 llrqtstkav qhfynikleg kvpmhklfle mleakv
//
LOCUS       NP_000822                919 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate receptor ionotropic, kainate 3 precursor [Homo sapiens].
ACCESSION   NP_000822
VERSION     NP_000822.2
DBSOURCE    REFSEQ: accession NM_000831.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 919)
  AUTHORS   Selvakumar,P., Lee,J., Khanra,N., He,C., Munguba,H., Kiese,L.,
            Broichhagen,J., Reiner,A., Levitz,J. and Meyerson,J.R.
  TITLE     Structural and compositional diversity in the kainate receptor
            family
  JOURNAL   Cell Rep 37 (4), 109891 (2021)
   PUBMED   34706237
REFERENCE   2  (residues 1 to 919)
  AUTHORS   Fang,G., Wu,Y. and Zhang,X.
  TITLE     CircASXL1 knockdown represses the progression of colorectal cancer
            by downregulating GRIK3 expression by sponging miR-1205
  JOURNAL   World J Surg Oncol 19 (1), 176 (2021)
   PUBMED   34127015
  REMARK    GeneRIF: CircASXL1 knockdown represses the progression of
            colorectal cancer by downregulating GRIK3 expression by sponging
            miR-1205.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 919)
  AUTHORS   Xiao,B., Kuang,Z., Zhang,W., Hang,J., Chen,L., Lei,T., He,Y.,
            Deng,C., Li,W., Lu,J., Qu,J., Zhou,Q., Hao,W., Sun,Z. and Li,L.
  TITLE     Glutamate Ionotropic Receptor Kainate Type Subunit 3 (GRIK3)
            promotes epithelial-mesenchymal transition in breast cancer cells
            by regulating SPDEF/CDH1 signaling
  JOURNAL   Mol Carcinog 58 (7), 1314-1323 (2019)
   PUBMED   30977227
  REMARK    GeneRIF: Mechanically, GRIK3 influenced a range of signaling
            pathways and key signal transducers, including two
            epithelial-mesenchymal transition regulators, SPDEF and CDH1.
            Moreover, overexpression of GRIK3 increased the expression of
            mesenchymal markers and decreased the expression of epithelial
            markers, resulting in the translocation of beta-catenin into the
            nucleus and the increased beta-catenin transcriptional activity.
REFERENCE   4  (residues 1 to 919)
  AUTHORS   Gong,B., Li,Y., Cheng,Z., Wang,P., Luo,L., Huang,H., Duan,S. and
            Liu,F.
  TITLE     GRIK3: A novel oncogenic protein related to tumor TNM stage, lymph
            node metastasis, and poor prognosis of GC
  JOURNAL   Tumour Biol 39 (6), 1010428317704364 (2017)
   PUBMED   28631555
  REMARK    GeneRIF: additional experiment showed that the lymph node
            metastasis tissues had higher GRIK3 expression than their matched
            primary gastric cancer (GC) tissues. These findings suggested that
            elevated GRIK3 expression could serve as an independent prognostic
            biomarker and a novel potential treatment target for patients with
            GC.
REFERENCE   5  (residues 1 to 919)
  AUTHORS   Wang,Y. and Tatakis,D.N.
  TITLE     Human gingiva transcriptome during wound healing
  JOURNAL   J Clin Periodontol 44 (4), 394-402 (2017)
   PUBMED   28005267
  REMARK    GeneRIF: GRIK3 expression is significantly downregulated in human
            masticatory mucosa during wound healing
REFERENCE   6  (residues 1 to 919)
  AUTHORS   Ripellino,J.A., Neve,R.L. and Howe,J.R.
  TITLE     Expression and heteromeric interactions of non-N-methyl-D-aspartate
            glutamate receptor subunits in the developing and adult cerebellum
  JOURNAL   Neuroscience 82 (2), 485-497 (1998)
   PUBMED   9466455
REFERENCE   7  (residues 1 to 919)
  AUTHORS   Flor,P.J., Van Der Putten,H., Ruegg,D., Lukic,S., Leonhardt,T.,
            Bence,M., Sansig,G., Knopfel,T. and Kuhn,R.
  TITLE     A novel splice variant of a metabotropic glutamate receptor, human
            mGluR7b
  JOURNAL   Neuropharmacology 36 (2), 153-159 (1997)
   PUBMED   9144652
REFERENCE   8  (residues 1 to 919)
  AUTHORS   Roche,K.W., Raymond,L.A., Blackstone,C. and Huganir,R.L.
  TITLE     Transmembrane topology of the glutamate receptor subunit GluR6
  JOURNAL   J Biol Chem 269 (16), 11679-11682 (1994)
   PUBMED   8163463
REFERENCE   9  (residues 1 to 919)
  AUTHORS   Nutt,S.L., Hoo,K.H., Rampersad,V., Deverill,R.M., Elliott,C.E.,
            Fletcher,E.J., Adams,S.L., Korczak,B., Foldes,R.L. and Kamboj,R.K.
  TITLE     Molecular characterization of the human EAA5 (GluR7) receptor: a
            high-affinity kainate receptor with novel potential RNA editing
            sites
  JOURNAL   Recept Channels 2 (4), 315-326 (1994)
   PUBMED   7719709
REFERENCE   10 (residues 1 to 919)
  AUTHORS   Puranam,R.S., Eubanks,J.H., Heinemann,S.F. and McNamara,J.O.
  TITLE     Chromosomal localization of gene for human glutamate receptor
            subunit-7
  JOURNAL   Somat Cell Mol Genet 19 (6), 581-588 (1993)
   PUBMED   8128318
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355386.9, DR003075.1,
            AJ249210.1, U16127.1, AW898512.1, AC117945.2, BG818719.1,
            DT217951.1, BQ446793.1 and BG057125.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 28, 2003 this sequence version replaced NP_000822.1.
            
            Summary: Glutamate receptors are the predominant excitatory
            neurotransmitter receptors in the mammalian brain and are activated
            in a variety of normal neurophysiologic processes. This gene
            product belongs to the kainate family of glutamate receptors, which
            are composed of four subunits and function as ligand-activated ion
            channels. It is not certain if the subunit encoded by this gene is
            subject to RNA editing as the other 2 family members (GRIK1 and
            GRIK2). A Ser310Ala polymorphism has been associated with
            schizophrenia, and there are conflicting reports of its association
            with the pathogenesis of delirium tremens in alcoholics. [provided
            by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.159793.1, U16127.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373091.8/ ENSP00000362183.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..919
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..919
                     /product="glutamate receptor ionotropic, kainate 3
                     precursor"
                     /note="excitatory amino acid receptor 5; glutamate
                     receptor 7; dJ1090M5.1 (glutamate receptor, ionotropic,
                     kainate 3 (GLUR7)); gluR-7; glutamate receptor ionotropic,
                     kainate 3"
                     /calculated_mol_wt=100318
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3737
     mat_peptide     32..919
                     /product="glutamate receptor ionotropic, kainate 3"
                     /calculated_mol_wt=100318
     Region          37..417
                     /region_name="PBP1_iGluR_Kainate"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the kainate receptors;
                     cd06382"
                     /db_xref="CDD:380605"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            order(90..92,96,127,179,182,186,189,192..193,203..206)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380605"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            415
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Region          433..801
                     /region_name="PBP2_iGluR_Kainate_GluR7"
                     /note="GluR7 subtype of kainate receptor, type 2
                     periplasmic-binding fold superfamily; cd13723"
                     /db_xref="CDD:270441"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            order(491,518..520,525)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270441"
     Site            order(521..523,526..527,531..534,537,695,761..762,
                     776..777,780..782,784..785,787..790)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270441"
     Site            548
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            564..584
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13003.3)"
     Site            637..657
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13003.3)"
     Site            752
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     Site            821..841
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13003.3)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q13002; propagated from
                     UniProtKB/Swiss-Prot (Q13003.3)"
     CDS             1..919
                     /gene="GRIK3"
                     /gene_synonym="EAA5; GLR7; GluK3; GLUR7; GluR7a"
                     /coded_by="NM_000831.4:408..3167"
                     /db_xref="CCDS:CCDS416.1"
                     /db_xref="GeneID:2899"
                     /db_xref="HGNC:HGNC:4581"
                     /db_xref="MIM:138243"
ORIGIN      
        1 mtapwrrlrs lvweywagll vcafwipdsr gmphvirigg ifeyadgpna qvmnaeehaf
       61 rfsaniinrn rtllpnttlt ydiqrihfhd sfeatkkacd qlalgvvaif gpsqgsctna
      121 vqsicnalev phiqlrwkhh pldnkdtfyv nlypdyasls haildlvqyl kwrsatvvyd
      181 dstglirlqe limapsryni rlkirqlpid sddsrpllke mkrgrefrii fdcshtmaaq
      241 ilkqamamgm mteyyhfift tldlyaldle pyrysgvnlt gfrilnvdnp hvsaivekws
      301 merlqaaprs esglldgvmm tdaallydav hivsvcyqra pqmtvnslqc hrhkawrfgg
      361 rfmnfikeaq wegltgrivf nktsglrtdf dldiislked glekvgvwsp adglniteva
      421 kgrgpnvtds ltnrslivtt vleepfvmfr ksdrtlygnd rfegycidll kelahilgfs
      481 yeirlvedgk ygaqddkgqw ngmvkelidh kadlavaplt ithvrekaid fskpfmtlgv
      541 silyrkpngt npsvfsflnp lspdiwmyvl laylgvscvl fviarfspye wydahpcnpg
      601 sevvennftl lnsfwfgmgs lmqqgselmp kalstriigg iwwfftliii ssytanlaaf
      661 ltvermespi dsaddlakqt kieygavkdg atmtffkksk istfekmwaf msskpsalvk
      721 nneegiqral tadyallmes ttieyvtqrn cnltqiggli dskgygigtp mgspyrdkit
      781 iailqlqeed klhimkekww rgsgcpeeen keasalgiqk iggifivlaa glvlsvlvav
      841 gefvyklrkt aereqrsfcs tvadeirfsl tcqrrvkhkp qppmmvktda vinmhtfndr
      901 rlpgkdsmac stslapvfp
//
LOCUS       NP_001167552            1062 aa            linear   PRI 20-NOV-2025
DEFINITION  NACHT, LRR and PYD domains-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001167552
VERSION     NP_001167552.1
DBSOURCE    REFSEQ: accession NM_001174081.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Rui,X., Zhang,X., Jia,X., Han,J., Wang,C., Cao,Q., Zhong,O.,
            Ding,J., Zhao,C., Zhang,J., Ling,X., Li,H., Ma,X., Meng,Q. and
            Huo,R.
  TITLE     Variants in NLRP2 and ZFP36L2, non-core components of the human
            subcortical maternal complex, cause female infertility with
            embryonic development arrest
  JOURNAL   Mol Hum Reprod 30 (9) (2024)
   PUBMED   39178021
  REMARK    GeneRIF: Variants in NLRP2 and ZFP36L2, non-core components of the
            human subcortical maternal complex, cause female infertility with
            embryonic development arrest.
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Gu,B., Le,G.H., Herrera,S., Blair,S.J., Meissner,T.B. and
            Strominger,J.L.
  TITLE     HLA-C expression in extravillous trophoblasts is determined by an
            ELF3-NLRP2/NLRP7 regulatory axis
  JOURNAL   Proc Natl Acad Sci U S A 121 (31), e2404229121 (2024)
   PUBMED   39052836
  REMARK    GeneRIF: HLA-C expression in extravillous trophoblasts is
            determined by an ELF3-NLRP2/NLRP7 regulatory axis.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Rossi,M.N., Matteo,V., Diomedi-Camassei,F., De Leo,E., Devuyst,O.,
            Lamkanfi,M., Caiello,I., Loricchio,E., Bellomo,F., Taranta,A.,
            Emma,F., De Benedetti,F. and Prencipe,G.
  TITLE     Nlrp2 deletion ameliorates kidney damage in a mouse model of
            cystinosis
  JOURNAL   Front Immunol 15, 1373224 (2024)
   PUBMED   38633264
  REMARK    GeneRIF: Nlrp2 deletion ameliorates kidney damage in a mouse model
            of cystinosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Fontalba,A., Gutierrez,O. and Fernandez-Luna,J.L.
  TITLE     NLRP2, an inhibitor of the NF-kappaB pathway, is transcriptionally
            activated by NF-kappaB and exhibits a nonfunctional allelic variant
  JOURNAL   J Immunol 179 (12), 8519-8524 (2007)
   PUBMED   18056399
  REMARK    GeneRIF: These findings provide molecular insight into the
            expression of NLRP2 by NF-kappaB.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Kinoshita,T., Wang,Y., Hasegawa,M., Imamura,R. and Suda,T.
  TITLE     PYPAF3, a PYRIN-containing APAF-1-like protein, is a feedback
            regulator of caspase-1-dependent interleukin-1beta secretion
  JOURNAL   J Biol Chem 280 (23), 21720-21725 (2005)
   PUBMED   15817483
  REMARK    GeneRIF: PYPAF3 is a feedback regulator of interleukin-1beta
            secretion, and PYPAF2 and PYPAF3, together with PYNOD, constitute
            an anti-inflammatory subgroup of PYRIN-containing apoptotic
            protease-activating factor-1-like proteins
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Bruey,J.M., Bruey-Sedano,N., Newman,R., Chandler,S., Stehlik,C. and
            Reed,J.C.
  TITLE     PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that
            regulates NF-kappaB and caspase-1 activation in macrophages
  JOURNAL   J Biol Chem 279 (50), 51897-51907 (2004)
   PUBMED   15456791
  REMARK    GeneRIF: functions as a modulator of the activation of NF-kappaB
            and pro-caspase-1 in macrophages
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Agostini,L., Martinon,F., Burns,K., McDermott,M.F., Hawkins,P.N.
            and Tschopp,J.
  TITLE     NALP3 forms an IL-1beta-processing inflammasome with increased
            activity in Muckle-Wells autoinflammatory disorder
  JOURNAL   Immunity 20 (3), 319-325 (2004)
   PUBMED   15030775
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Martinon,F., Hofmann,K. and Tschopp,J.
  TITLE     The pyrin domain: a possible member of the death domain-fold family
            implicated in apoptosis and inflammation
  JOURNAL   Curr Biol 11 (4), R118-R120 (2001)
   PUBMED   11250163
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Bertin,J. and DiStefano,P.S.
  TITLE     The PYRIN domain: a novel motif found in apoptosis and inflammation
            proteins
  JOURNAL   Cell Death Differ 7 (12), 1273-1274 (2000)
   PUBMED   11270363
  REMARK    Review article
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Tumer,Z., Eggermann,T., Maas,S., Bliek,J. and Mackay,D.
  TITLE     Maternal Effect Gene-Related Multilocus Imprinting Disturbances
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA856893.1, AF464764.1 and
            AK000784.1.
            
            Summary: This gene is a member of the nucleotide-binding and
            leucine-rich repeat receptor (NLR) family, and is predicted to
            contain an N-terminal pyrin effector domain (PYD), a
            centrally-located nucleotide-binding and oligomerization domain
            (NACHT) and C-terminal leucine-rich repeats (LRR). Members of this
            gene family are thought to be important regulators of immune
            responses. This gene product interacts with components of the IkB
            kinase (IKK) complex, and can regulate both caspase-1 and NF-kB
            (nuclear factor kappa-light-chain-enhancer of activated B cells)
            activity. The pyrin domain is necessary and sufficient for
            suppression of NF-kB activity. An allelic variant (rs147585490) has
            been found that is incapable of blocking the transcriptional
            activity of NF-kB. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF464764.1, SRR1163655.585492.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..1062
                     /product="NACHT, LRR and PYD domains-containing protein 2
                     isoform 1"
                     /note="NACHT, leucine rich repeat and PYD containing 2;
                     nucleotide-binding oligomerization domain, leucine rich
                     repeat and pyrin domain containing 2; NACHT, LRR and PYD
                     domains-containing protein 2; nucleotide-binding site
                     protein 1; PYRIN-containing APAF1-like protein 2; PYRIN
                     domain and NACHT domain-containing protein 1"
                     /calculated_mol_wt=120385
     Region          11..94
                     /region_name="Pyrin_NALPs"
                     /note="Pyrin death domain found in NALP proteins; cd08320"
                     /db_xref="CDD:260032"
     Region          46..>553
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          207..375
                     /region_name="NACHT"
                     /note="NACHT domain; pfam05729"
                     /db_xref="CDD:428606"
     Region          503..620
                     /region_name="NLRC4_HD2"
                     /note="NLRC4 helical domain HD2; pfam17776"
                     /db_xref="CDD:465499"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          757..784
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          785..812
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          788..1018
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          812..832
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          813..837
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          841..861
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          842..869
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          869..889
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          870..898
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          898..918
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          899..926
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          926..946
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          927..955
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          955..976
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          956..983
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          983..1003
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          1010..1033
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     CDS             1..1062
                     /gene="NLRP2"
                     /gene_synonym="CLR19.9; NALP2; NBS1; OZEMA18; PAN1;
                     PYPAF2"
                     /coded_by="NM_001174081.3:112..3300"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12913.1"
                     /db_xref="GeneID:55655"
                     /db_xref="HGNC:HGNC:22948"
                     /db_xref="MIM:609364"
ORIGIN      
        1 mvssaqmgfn lqalleqlsq delskfkyli ttfslahelq kiphkevdka dgkqlveilt
       61 thcdsywvem aslqvfekmh rmdlserakd evreaalksf nkrkplslgi trkerppldv
      121 demlerfkte aqaftetkgn viclgkevfk gkkpdkdnrc ryilktkfre mwkswpgdsk
      181 evqvmaeryk mlipfsnprv lpgpfsytvv lygpaglgkt tlaqklmldw aednlihkfk
      241 yafylscrel srlgpcsfae lvfrdwpelq ddiphilaqa rkilfvidgf delgaapgal
      301 iedicgdwek kkpvpvllgs llnrvmlpka allvttrpra lrdlrilaee piyirvegfl
      361 eedrrayflr hfgdedqamr afelmrsnaa lfqlgsapav cwivcttlkl qmekgedpvp
      421 tcltrtglfl rflcsrfpqg aqlrgalrtl sllaaqglwa qtsvlhredl erlgvqesdl
      481 rlfldgdilr qdrvskgcys fihlsfqqfl talfytleke eeedrdghtw digdvqklls
      541 gverlrnpdl iqagyysfgl anekrakele atfgcrmspd ikqellrcdi sckgghstvt
      601 dlqellgcly esqeeelvke vmaqfkeisl hlnavdvvps sfcvkhcrnl qkmslqvike
      661 nlpenvtase sdaeversqd dqhmlpfwtd lcsifgsnkd lmglaindsf lsaslvrilc
      721 eqiasdtchl qrvvfknisp adahrnlcla lrghktvtyl tlqgndqddm fpalcevlrh
      781 pecnlrylgl vscsattqqw adlslalevn qsltcvnlsd nelldegakl lyttlrhpkc
      841 flqrlslenc hlteanckdl aavlvvsrel thlclaknpi gntgvkflce glrypecklq
      901 tlvlwncdit sdgccdltkl lqekssllcl dlglnhigvk gmkflcealr kplcnlrclw
      961 lwgcsippfs cedlcsalsc nqslvtldlg qnplgssgvk mlfetltcss gtlrtlrlki
     1021 ddfndelnkl leeieeknpq liidtekhhp waerpsshdf mi
//
LOCUS       NP_001240811             130 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 27 isoform 3
            [Homo sapiens].
ACCESSION   NP_001240811
VERSION     NP_001240811.1
DBSOURCE    REFSEQ: accession NM_001253882.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Maroofian,R., Kaiyrzhanov,R., Cali,E., Zamani,M., Zaki,M.S.,
            Ferla,M., Tortora,D., Sadeghian,S., Saadi,S.M., Abdullah,U.,
            Karimiani,E.G., Efthymiou,S., Yesil,G., Alavi,S., Al Shamsi,A.M.,
            Tajsharghi,H., Abdel-Hamid,M.S., Saadi,N.W., Al Mutairi,F.,
            Alabdi,L., Beetz,C., Ali,Z., Toosi,M.B., Rudnik-Schoneborn,S.,
            Babaei,M., Isohanni,P., Muhammad,J., Khan,S., Al Shalan,M.,
            Hickey,S.E., Marom,D., Elhanan,E., Kurian,M.A., Marafi,D.,
            Saberi,A., Hamid,M., Spaull,R., Meng,L., Lalani,S., Maqbool,S.,
            Rahman,F., Seeger,J., Palculict,T.B., Lau,T., Murphy,D.,
            Mencacci,N.E., Steindl,K., Begemann,A., Rauch,A., Akbas,S.,
            Aslanger,A.D., Salpietro,V., Yousaf,H., Ben-Shachar,S., Ejeskar,K.,
            Al Aqeel,A.I., High,F.A., Armstrong-Javors,A.E., Zahraei,S.M.,
            Seifi,T., Zeighami,J., Shariati,G., Sedaghat,A., Asl,S.N.,
            Shahrooei,M., Zifarelli,G., Burglen,L., Ravelli,C., Zschocke,J.,
            Schatz,U.A., Ghavideldarestani,M., Kamel,W.A., Van Esch,H.,
            Hackenberg,A., Taylor,J.C., Al-Gazali,L., Bauer,P., Gleeson,J.J.,
            Alkuraya,F.S., Lupski,J.R., Galehdari,H., Azizimalamiri,R.,
            Chung,W.K., Baig,S.M., Houlden,H. and Severino,M.
  TITLE     Biallelic MED27 variants lead to variable ponto-cerebello-lental
            degeneration with movement disorders
  JOURNAL   Brain 146 (12), 5031-5043 (2023)
   PUBMED   37517035
  REMARK    GeneRIF: Biallelic MED27 variants lead to variable
            ponto-cerebello-lental degeneration with movement disorders.
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Wang,R., Yu,W., Zhu,T., Lin,F., Hua,C., Ru,L., Guo,P., Wan,X.,
            Xue,G., Guo,Z., Han,S., Lv,K., Zhang,G., Ge,H., Guo,W., Xu,L. and
            Deng,W.
  TITLE     MED27 plays a tumor-promoting role in breast cancer progression by
            targeting KLF4
  JOURNAL   Cancer Sci 114 (6), 2277-2292 (2023)
   PUBMED   36786527
  REMARK    GeneRIF: MED27 plays a tumor-promoting role in breast cancer
            progression by targeting KLF4.
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Han,X., Liu,H., Tang,X. and Zhao,Y.
  TITLE     Knockdown of mediator complex subunit 27 suppresses gastric cancer
            cell metastasis and angiogenesis via Wnt/beta-catenin pathway
  JOURNAL   Tissue Cell 79, 101973 (2022)
   PUBMED   36371844
  REMARK    GeneRIF: Knockdown of mediator complex subunit 27 suppresses
            gastric cancer cell metastasis and angiogenesis via
            Wnt/beta-catenin pathway.
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 130)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   7  (residues 1 to 130)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
REFERENCE   8  (residues 1 to 130)
  AUTHORS   Malik,S., Gu,W., Wu,W., Qin,J. and Roeder,R.G.
  TITLE     The USA-derived transcriptional coactivator PC2 is a submodule of
            TRAP/SMCC and acts synergistically with other PCs
  JOURNAL   Mol Cell 5 (4), 753-760 (2000)
   PUBMED   10882111
REFERENCE   9  (residues 1 to 130)
  AUTHORS   Ryu,S., Zhou,S., Ladurner,A.G. and Tjian,R.
  TITLE     The transcriptional cofactor complex CRSP is required for activity
            of the enhancer-binding protein Sp1
  JOURNAL   Nature 397 (6718), 446-450 (1999)
   PUBMED   9989412
REFERENCE   10 (residues 1 to 130)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP255072.1, CD388680.1 and
            BU069864.1.
            
            Summary: The activation of gene transcription is a multistep
            process that is triggered by factors that recognize transcriptional
            enhancer sites in DNA. These factors work with co-activators to
            direct transcriptional initiation by the RNA polymerase II
            apparatus. The protein encoded by this gene is a subunit of the
            CRSP (cofactor required for SP1 activation) complex, which, along
            with TFIID, is required for efficient activation by SP1. This
            protein is also a component of other multisubunit complexes e.g.
            thyroid hormone receptor-(TR-) associated proteins which interact
            with TR and facilitate TR function on DNA templates in conjunction
            with initiation factors and cofactors. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene, and a pseudogene of this gene is located on the long
            arm of chromosome 5. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (3) uses an alternate terminal
            exon and lacks a large portion of the 3' coding region, compared to
            variant 1. The encoded isoform (3) is significantly shorter and has
            a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CK300803.1, CK820315.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA2144333 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..130
                     /product="mediator of RNA polymerase II transcription
                     subunit 27 isoform 3"
                     /note="cofactor required for Sp1 transcriptional
                     activation, subunit 8, 34kDa; p37 TRAP/SMCC/PC2 subunit;
                     mediator of RNA polymerase II transcription subunit 27;
                     CRSP complex subunit 8; transcriptional coactivator
                     CRSP34; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=14695
     CDS             1..130
                     /gene="MED27"
                     /gene_synonym="CRAP34; CRSP34; CRSP8; MED3; NEDSCAC;
                     TRAP37"
                     /coded_by="NM_001253882.2:24..416"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS69689.1"
                     /db_xref="GeneID:9442"
                     /db_xref="HGNC:HGNC:2377"
                     /db_xref="MIM:605044"
ORIGIN      
        1 madvinvsvn leafsqaisa iqalrssvsr vfdclkdgmr nketlegrek afiahfqdnl
       61 hsvnrdlnel erlsnlvgkp senhplhnsg llsldpvqdk tplysqllqa ykwsnkkeql
      121 siprifhwkv
//
LOCUS       NP_001073271             952 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal alpha-glucosidase preproprotein [Homo sapiens].
ACCESSION   NP_001073271
VERSION     NP_001073271.1
DBSOURCE    REFSEQ: accession NM_001079803.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 952)
  AUTHORS   Colella,P.
  TITLE     Advances in Pompe Disease Treatment: From Enzyme Replacement to
            Gene Therapy
  JOURNAL   Mol Diagn Ther 28 (6), 703-719 (2024)
   PUBMED   39134822
  REMARK    Review article
REFERENCE   2  (residues 1 to 952)
  AUTHORS   Ruiz-Saavedra,S., Salazar,N., Suarez,A., Diaz,Y., Gonzalez Del
            Rey,C., Gonzalez,S. and de Los Reyes-Gavilan,C.G.
  TITLE     Human fecal alpha-glucosidase activity and its relationship with
            gut microbiota profiles and early stages of intestinal mucosa
            damage
  JOURNAL   Anaerobe 87, 102853 (2024)
   PUBMED   38614290
  REMARK    GeneRIF: Human fecal alpha-glucosidase activity and its
            relationship with gut microbiota profiles and early stages of
            intestinal mucosa damage.
REFERENCE   3  (residues 1 to 952)
  AUTHORS   Schoser,B., Raben,N., Varfaj,F., Walzer,M. and Toscano,A.
  TITLE     Acid alpha-glucosidase (GAA) activity and glycogen content in
            muscle biopsy specimens of patients with Pompe disease: A
            systematic review
  JOURNAL   Mol Genet Metab Rep 39, 101085 (2024)
   PUBMED   38698877
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 952)
  AUTHORS   Lim,J.A., Li,L. and Raben,N.
  TITLE     Pompe disease: from pathophysiology to therapy and back again
  JOURNAL   Front Aging Neurosci 6, 177 (2014)
   PUBMED   25183957
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 952)
  AUTHORS   Moreland,R.J., Jin,X., Zhang,X.K., Decker,R.W., Albee,K.L.,
            Lee,K.L., Cauthron,R.D., Brewer,K., Edmunds,T. and Canfield,W.M.
  TITLE     Lysosomal acid alpha-glucosidase consists of four different
            peptides processed from a single chain precursor
  JOURNAL   J Biol Chem 280 (8), 6780-6791 (2005)
   PUBMED   15520017
  REMARK    GeneRIF: data show that the mature forms of GAA characterized by
            polypeptides of 76 or 70 kDa are in fact larger molecular mass
            multicomponent enzyme complexes; peptides released during
            proteolytic processing remained tightly associated with the major
            species
REFERENCE   6  (residues 1 to 952)
  AUTHORS   Sperry,E., Leslie,N., Berry,L. and Pena,L.
  TITLE     Pompe Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301438
REFERENCE   7  (residues 1 to 952)
  AUTHORS   Martiniuk,F., Mehler,M., Bodkin,M., Tzall,S., Hirschhorn,K.,
            Zhong,N. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in an adult-onset patient
            with glycogenosis type II expressing only one allele
  JOURNAL   DNA Cell Biol 10 (9), 681-687 (1991)
   PUBMED   1684505
REFERENCE   8  (residues 1 to 952)
  AUTHORS   Zhong,N., Martiniuk,F., Tzall,S. and Hirschhorn,R.
  TITLE     Identification of a missense mutation in one allele of a patient
            with Pompe disease, and use of endonuclease digestion of
            PCR-amplified RNA to demonstrate lack of mRNA expression from the
            second allele
  JOURNAL   Am J Hum Genet 49 (3), 635-645 (1991)
   PUBMED   1652892
REFERENCE   9  (residues 1 to 952)
  AUTHORS   Hoefsloot,L.H., Hoogeveen-Westerveld,M., Kroos,M.A., van
            Beeumen,J., Reuser,A.J. and Oostra,B.A.
  TITLE     Primary structure and processing of lysosomal alpha-glucosidase;
            homology with the intestinal sucrase-isomaltase complex
  JOURNAL   EMBO J 7 (6), 1697-1704 (1988)
   PUBMED   3049072
REFERENCE   10 (residues 1 to 952)
  AUTHORS   Murray,A.K., Brown,B.I. and Brown,D.H.
  TITLE     The molecular heterogeneity of purified human liver lysosomal
            alpha-glucosidase (acid alpha-glucosidase)
  JOURNAL   Arch Biochem Biophys 185 (2), 511-524 (1978)
   PUBMED   24417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY101855.1, BC040431.1,
            BF206270.1, M34424.1, BQ711289.1 and BF344248.1.
            
            Summary: This gene encodes lysosomal alpha-glucosidase, which is
            essential for the degradation of glycogen to glucose in lysosomes.
            The encoded preproprotein is proteolytically processed to generate
            multiple intermediate forms and the mature form of the enzyme.
            Defects in this gene are the cause of glycogen storage disease II,
            also known as Pompe's disease, which is an autosomal recessive
            disorder with a broad clinical spectrum. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1783113.1,
                                           SRR7346977.1584163.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..952
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..952
                     /product="lysosomal alpha-glucosidase preproprotein"
                     /EC_number="3.2.1.20"
                     /note="lysosomal alpha-glucosidase; acid maltase;
                     aglucosidase alfa; glucosidase alpha, acid"
                     /calculated_mol_wt=102542
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=2800
     Region          47..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
     mat_peptide     70..952
                     /product="Lysosomal alpha-glucosidase. /id=PRO_0000018566"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=98009
     Region          81..132
                     /region_name="PD"
                     /note="P or trefoil or TFF domain; smart00018"
                     /db_xref="CDD:197472"
     Site            order(95,125..126)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:238059"
     Site            order(111,125)
                     /site_type="active"
                     /note="putative binding specificity loop [active]"
                     /db_xref="CDD:238059"
     mat_peptide     123..952
                     /product="76 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018567"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=92314
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Region          159..254
                     /region_name="NtCtMGAM_N"
                     /note="N-terminal barrel of NtMGAM and CtMGAM,
                     maltase-glucoamylase; pfam16863"
                     /db_xref="CDD:465286"
     mat_peptide     204..952
                     /product="70 kDa lysosomal alpha-glucosidase.
                     /id=PRO_0000018568"
                     /note="propagated from UniProtKB/Swiss-Prot (P10253.4)"
                     /calculated_mol_wt=82826
     Site            233
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Region          246..359
                     /region_name="GH31_N"
                     /note="N-terminal domain of glycosyl hydrolase family 31
                     (GH31); cd14752"
                     /db_xref="CDD:270212"
     Site            282
                     /site_type="active"
                     /db_xref="CDD:270212"
     Region          340..824
                     /region_name="Glyco_hydro_31"
                     /note="Glycosyl hydrolases family 31; pfam01055"
                     /db_xref="CDD:460044"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            470
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            652
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29061980,
                     ECO:0000269|PubMed:8435067, ECO:0000269|Ref.19,
                     ECO:0007744|PDB:5KZW, ECO:0007744|PDB:5NN3; propagated
                     from UniProtKB/Swiss-Prot (P10253.4)"
     Site            882
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:29061980, ECO:0000269|PubMed:8435067,
                     ECO:0000269|Ref.19, ECO:0007744|PDB:5KZW,
                     ECO:0007744|PDB:5NN3; propagated from UniProtKB/Swiss-Prot
                     (P10253.4)"
     Site            925
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:8435067; propagated from
                     UniProtKB/Swiss-Prot (P10253.4)"
     CDS             1..952
                     /gene="GAA"
                     /gene_synonym="IOPD; LOPD; LYAG"
                     /coded_by="NM_001079803.3:158..3016"
                     /db_xref="CCDS:CCDS32760.1"
                     /db_xref="GeneID:2548"
                     /db_xref="HGNC:HGNC:4065"
                     /db_xref="MIM:606800"
ORIGIN      
        1 mgvrhppcsh rllavcalvs lataallghi llhdfllvpr elsgsspvle ethpahqqga
       61 srpgprdaqa hpgrpravpt qcdvppnsrf dcapdkaitq eqceargccy ipakqglqga
      121 qmgqpwcffp psypsyklen lsssemgyta tltrttptff pkdiltlrld vmmetenrlh
      181 ftikdpanrr yevpletphv hsrapsplys vefseepfgv ivrrqldgrv llnttvaplf
      241 fadqflqlst slpsqyitgl aehlsplmls tswtritlwn rdlaptpgan lygshpfyla
      301 ledggsahgv fllnsnamdv vlqpspalsw rstggildvy iflgpepksv vqqyldvvgy
      361 pfmppywglg fhlcrwgyss taitrqvven mtrahfpldv qwndldymds rrdftfnkdg
      421 frdfpamvqe lhqggrrymm ivdpaisssg pagsyrpyde glrrgvfitn etgqpligkv
      481 wpgstafpdf tnptalawwe dmvaefhdqv pfdgmwidmn epsnfirgse dgcpnnelen
      541 ppyvpgvvgg tlqaaticas shqflsthyn lhnlygltea iashralvka rgtrpfvisr
      601 stfaghgrya ghwtgdvwss weqlassvpe ilqfnllgvp lvgadvcgfl gntseelcvr
      661 wtqlgafypf mrnhnsllsl pqepysfsep aqqamrkalt lryallphly tlfhqahvag
      721 etvarplfle fpkdsstwtv dhqllwgeal litpvlqagk aevtgyfplg twydlqtvpv
      781 ealgslpppp aaprepaihs egqwvtlpap ldtinvhlra gyiiplqgpg ltttesrqqp
      841 malavaltkg geargelfwd dgeslevler gaytqvifla rnntivnelv rvtsegaglq
      901 lqkvtvlgva tapqqvlsng vpvsnftysp dtkvldicvs llmgeqflvs wc
//
LOCUS       NP_114429                538 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 8 [Homo sapiens].
ACCESSION   NP_114429
VERSION     NP_114429.2
DBSOURCE    REFSEQ: accession NM_032040.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Zhang,L., Ren,D., Hu,X., Sun,J., Qi,C., Wang,Y., Lu,L. and Wei,M.
  TITLE     Establishment of the 3M syndrome animal model in CCDC8 knockout
            mice
  JOURNAL   Mol Biomed 4 (1), 24 (2023)
   PUBMED   37574524
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Isik,E., Arican,D., Atik,T., Ooi,J.E., Darcan,S., Ozen,S., Simsek
            Kiper,P.O., Utine,E., Cogulu,O. and Ozkinay,F.
  TITLE     A rare cause of syndromic short stature: 3M syndrome in three
            families
  JOURNAL   Am J Med Genet A 185 (2), 461-468 (2021)
   PUBMED   33258289
  REMARK    GeneRIF: A rare cause of syndromic short stature: 3M syndrome in
            three families.
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Jiang,X., Jia,X., Sun,J., Qi,C., Lu,L., Wang,Y., Zhang,L. and
            Wei,M.
  TITLE     Overexpressed coiled-coil domain containing protein 8 (CCDC8)
            mediates newly synthesized HIV-1 Gag lysosomal degradation
  JOURNAL   Sci Rep 10 (1), 11416 (2020)
   PUBMED   32651437
  REMARK    GeneRIF: Overexpressed coiled-coil domain containing protein 8
            (CCDC8) mediates newly synthesized HIV-1 Gag lysosomal degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Wang,P., Yan,F., Li,Z., Yu,Y., Parnell,S.E. and Xiong,Y.
  TITLE     Impaired plasma membrane localization of ubiquitin ligase complex
            underlies 3-M syndrome development
  JOURNAL   J Clin Invest 129 (10), 4393-4407 (2019)
   PUBMED   31343991
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Hanson,D., Murray,P.G., Coulson,T., Sud,A., Omokanye,A.,
            Stratta,E., Sakhinia,F., Bonshek,C., Wilson,L.C., Wakeling,E.,
            Temtamy,S.A., Aglan,M., Rosser,E.M., Mansour,S., Carcavilla,A.,
            Nampoothiri,S., Khan,W.I., Banerjee,I., Chandler,K.E., Black,G.C.
            and Clayton,P.E.
  TITLE     Mutations in CUL7, OBSL1 and CCDC8 in 3-M syndrome lead to
            disordered growth factor signalling
  JOURNAL   J Mol Endocrinol 49 (3), 267-275 (2012)
   PUBMED   23018678
  REMARK    GeneRIF: Mutations in CUL7, OBSL1 and CCDC8 in 3-M syndrome lead to
            disordered growth factor signalling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Dai,C., Tang,Y., Jung,S.Y., Qin,J., Aaronson,S.A. and Gu,W.
  TITLE     Differential effects on p53-mediated cell cycle arrest vs.
            apoptosis by p90
  JOURNAL   Proc Natl Acad Sci U S A 108 (47), 18937-18942 (2011)
   PUBMED   22084066
  REMARK    GeneRIF: p90 is a critical cofactor for p53-mediated apoptosis
            through promoting Tip60-mediated p53 acetylation.
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Hanson,D., Murray,P.G., O'Sullivan,J., Urquhart,J., Daly,S.,
            Bhaskar,S.S., Biesecker,L.G., Skae,M., Smith,C., Cole,T., Kirk,J.,
            Chandler,K., Kingston,H., Donnai,D., Clayton,P.E. and Black,G.C.
  TITLE     Exome sequencing identifies CCDC8 mutations in 3-M syndrome,
            suggesting that CCDC8 contributes in a pathway with CUL7 and OBSL1
            to control human growth
  JOURNAL   Am J Hum Genet 89 (1), 148-153 (2011)
   PUBMED   21737058
  REMARK    GeneRIF: We propose that CUL7, OBSL1, and CCDC8 are members of a
            pathway controlling mammalian growth.
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Hanson,D., Murray,P.G., Black,G.C. and Clayton,P.E.
  TITLE     The genetics of 3-M syndrome: unravelling a potential new
            regulatory growth pathway
  JOURNAL   Horm Res Paediatr 76 (6), 369-378 (2011)
   PUBMED   22156540
  REMARK    GeneRIF: discussion of roles of CCDC8, CUL7 (cullin 7), and OBSL1
            (obscurin-like 1) in growth and development using findings from
            patients with Miller-McKusick-Malvaux syndrome and Silver-Russell
            syndrome [REVIEW]
            Review article
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Hendrickx,A., Beullens,M., Ceulemans,H., Den Abt,T., Van Eynde,A.,
            Nicolaescu,E., Lesage,B. and Bollen,M.
  TITLE     Docking motif-guided mapping of the interactome of protein
            phosphatase-1
  JOURNAL   Chem Biol 16 (4), 365-371 (2009)
   PUBMED   19389623
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from JN703457.1, BC025243.1,
            AL136609.1 and AI301367.1.
            
            On Sep 11, 2008 this sequence version replaced NP_114429.1.
            
            Summary: This gene encodes a coiled-coil domain-containing protein.
            The encoded protein functions as a cofactor required for
            p53-mediated apoptosis following DNA damage, and may also play a
            role in growth through interactions with the cytoskeletal adaptor
            protein obscurin-like 1. Mutations in this gene are a cause of 3M
            syndrome-3 (3M3). [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: JN703457.1, AL136609.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307522.5/ ENSP00000303158.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..538
                     /product="coiled-coil domain-containing protein 8"
                     /note="protein phosphatase 1, regulatory subunit 20"
                     /calculated_mol_wt=59243
     Region          1..>57
                     /region_name="PNMA"
                     /note="pfam14893"
                     /db_xref="CDD:464357"
     Region          58..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W5.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W5.2)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W5.2)"
     Region          213..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W5.2)"
     Region          223..>437
                     /region_name="PRK12678"
                     /note="transcription termination factor Rho; Provisional"
                     /db_xref="CDD:237171"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W5.2)"
     Region          500..506
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2. /evidence=ECO:0000269|PubMed:25752541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W5.2)"
     CDS             1..538
                     /gene="CCDC8"
                     /gene_synonym="3M3; p90; PPP1R20"
                     /coded_by="NM_032040.5:755..2371"
                     /db_xref="CCDS:CCDS12685.1"
                     /db_xref="GeneID:83987"
                     /db_xref="HGNC:HGNC:25367"
                     /db_xref="MIM:614145"
ORIGIN      
        1 mlqigedvdy lliprevrla ggvwrviskp atkeaefrer ltqfleeegr tledvarime
       61 kstphppqpp kkpkeprvrr rvqqmvtppp rlvvgtydss nasdsefsdf etsrdksrqg
      121 prrgkkvrkm pvsylgskfl gsdlesedde elveaflrrq ekqpsappar rrvnlpvpmf
      181 ednlgpqlsk adrwreyvsq vswgklkrrv kgwapragpg vgearlasta vesagvssap
      241 egtspgdrlg nagdvcvpqa sprrwrpkin wasfrrrrke qtaptgqgad ieadqggeaa
      301 dsqreeaiad qregaagnqr agapadqgae aadnqreeaa dnqragapae egaeaadnqr
      361 eeaadnqrae apadqrsqgt dnhreeaadn qraeapadqg sevtdnqree avhdqrerap
      421 avqgadnqra qaragqraea ahnqragapg iqeaevsaaq gttgtapgar arkqvktvrf
      481 qtpgrfswfc krrrafwhtp rlptlpkrvp ragearnlrv lraearaeae qgeqedql
//
LOCUS       NP_001268383             259 aa            linear   PRI 20-NOV-2025
DEFINITION  methyl-CpG-binding domain protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001268383
VERSION     NP_001268383.1
DBSOURCE    REFSEQ: accession NM_001281454.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Leighton,G.O., Irvin,E.M., Kaur,P., Liu,M., You,C., Bhattaram,D.,
            Piehler,J., Riehn,R., Wang,H., Pan,H. and Williams,D.C. Jr.
  TITLE     Densely methylated DNA traps Methyl-CpG-binding domain protein 2
            but permits free diffusion by Methyl-CpG-binding domain protein 3
  JOURNAL   J Biol Chem 298 (10), 102428 (2022)
   PUBMED   36037972
  REMARK    GeneRIF: Densely methylated DNA traps Methyl-CpG-binding domain
            protein 2 but permits free diffusion by Methyl-CpG-binding domain
            protein 3.
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Yan,W., Han,Q., Gong,L., Zhan,X., Li,W., Guo,Z., Zhao,J., Li,T.,
            Bai,Z., Wu,J., Huang,Y., Lv,L., Zhao,H., Cai,H., Huang,S., Diao,X.,
            Chen,Y., Gong,W., Xia,Q., Man,J., Chen,L., Dai,G. and Zhou,T.
  TITLE     MBD3 promotes hepatocellular carcinoma progression and metastasis
            through negative regulation of tumour suppressor TFPI2
  JOURNAL   Br J Cancer 127 (4), 612-623 (2022)
   PUBMED   35501390
  REMARK    GeneRIF: MBD3 promotes hepatocellular carcinoma progression and
            metastasis through negative regulation of tumour suppressor TFPI2.
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Hendrich,B., Abbott,C., McQueen,H., Chambers,D., Cross,S. and
            Bird,A.
  TITLE     Genomic structure and chromosomal mapping of the murine and human
            Mbd1, Mbd2, Mbd3, and Mbd4 genes
  JOURNAL   Mamm Genome 10 (9), 906-912 (1999)
   PUBMED   10441743
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Tong,J.K., Hassig,C.A., Schnitzler,G.R., Kingston,R.E. and
            Schreiber,S.L.
  TITLE     Chromatin deacetylation by an ATP-dependent nucleosome remodelling
            complex
  JOURNAL   Nature 395 (6705), 917-921 (1998)
   PUBMED   9804427
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Zhang,Y., LeRoy,G., Seelig,H.P., Lane,W.S. and Reinberg,D.
  TITLE     The dermatomyositis-specific autoantigen Mi2 is a component of a
            complex containing histone deacetylase and nucleosome remodeling
            activities
  JOURNAL   Cell 95 (2), 279-289 (1998)
   PUBMED   9790534
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005943.1.
            
            Summary: DNA methylation is the major modification of eukaryotic
            genomes and plays an essential role in mammalian development. This
            gene belongs to a family of nuclear proteins which are
            characterized by the presence of a methyl-CpG binding domain (MBD).
            The encoded protein is a subunit of the NuRD, a multisubunit
            complex containing nucleosome remodeling and histone deacetylase
            activities. Unlike the other family members, the encoded protein is
            not capable of binding to methylated DNA. The protein mediates the
            association of metastasis-associated protein 2 with the core
            histone deacetylase complex. Alternative splicing results in
            multiple transcript variants of this gene. [provided by RefSeq, Jul
            2013].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. It
            encodes isoform 2, which lacks an internal segment and is shorter,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3137011.1, BC043619.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..259
                     /product="methyl-CpG-binding domain protein 3 isoform 2"
                     /calculated_mol_wt=28883
     Region          <5..47
                     /region_name="MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, MBD4, CLLD8-like, and
                     BAZ2A-like proteins constitute a family of proteins that
                     share the methyl-CpG-binding domain (MBD). The MBD
                     consists of about 70 residues and is defined as the
                     minimal region required for binding to...; cl00110"
                     /db_xref="CDD:469618"
     Region          50..116
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Region          120..211
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     CDS             1..259
                     /gene="MBD3"
                     /coded_by="NM_001281454.2:235..1014"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS62481.1"
                     /db_xref="GeneID:53615"
                     /db_xref="HGNC:HGNC:6918"
                     /db_xref="MIM:603573"
ORIGIN      
        1 merkspsgkk frskpqlary lggsmdlstf dfrtgkmlms kmnksrqrvr ydssnqvkgk
       61 pdlntalpvr qtasifkqpv tkitnhpsnk vksdpqkavd qprqlfwekk lsglnafdia
      121 eelvktmdlp kglqgvgpgc tdetllsaia salhtstmpi tgqlsaavek npgvwlnttq
      181 plckafmvtd edirkqeelv qqvrkrleea lmadmlahve elardgeapl dkacaeddde
      241 edeeeeeeep dpdpemehv
//
LOCUS       NP_058651                501 aa            linear   PRI 20-NOV-2025
DEFINITION  O-phosphoseryl-tRNA(Sec) selenium transferase isoform 1 [Homo
            sapiens].
ACCESSION   NP_058651 NP_722547
VERSION     NP_058651.3
DBSOURCE    REFSEQ: accession NM_016955.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Vishweswaraiah,S., Yilmaz,A., Saiyed,N., Khalid,A., Koladiya,P.R.,
            Pan,X., Macias,S., Robinson,A.C., Mann,D., Green,B.D.,
            Kerseviciute,I., Gordevicius,J., Radhakrishna,U. and Graham,S.F.
  TITLE     Integrative Analysis Unveils the Correlation of Aminoacyl-tRNA
            Biosynthesis Metabolites with the Methylation of the SEPSECS Gene
            in Huntington's Disease Brain Tissue
  JOURNAL   Genes (Basel) 14 (9), 1752 (2023)
   PUBMED   37761892
  REMARK    GeneRIF: Integrative Analysis Unveils the Correlation of
            Aminoacyl-tRNA Biosynthesis Metabolites with the Methylation of the
            SEPSECS Gene in Huntington's Disease Brain Tissue.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Puppala,A.K., Castillo Suchkou,J., French,R.L., Kiernan,K.A. and
            Simonovic,M.
  TITLE     Structural basis for the tRNA-dependent activation of the terminal
            complex of selenocysteine synthesis in humans
  JOURNAL   Nucleic Acids Res 51 (8), 4012-4026 (2023)
   PUBMED   36929010
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Ramadesikan,S., Hickey,S., De Los Reyes,E., Patel,A.D.,
            Franklin,S.J., Brennan,P., Crist,E., Lee,K., White,P.,
            McBride,K.L., Koboldt,D.C. and Wilson,R.K.
  TITLE     Biallelic SEPSECS variants in two siblings with pontocerebellar
            hypoplasia type 2D underscore the relevance of splice-disrupting
            synonymous variants in disease
  JOURNAL   Cold Spring Harb Mol Case Stud 8 (2), a006165 (2022)
   PUBMED   35091508
  REMARK    GeneRIF: Biallelic SEPSECS variants in two siblings with
            pontocerebellar hypoplasia type 2D underscore the relevance of
            splice-disrupting synonymous variants in disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Schoenmakers,E. and Chatterjee,K.
  TITLE     Human Genetic Disorders Resulting in Systemic Selenoprotein
            Deficiency
  JOURNAL   Int J Mol Sci 22 (23), 12927 (2021)
   PUBMED   34884733
  REMARK    GeneRIF: Human Genetic Disorders Resulting in Systemic
            Selenoprotein Deficiency.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Xu,X.M., Mix,H., Carlson,B.A., Grabowski,P.J., Gladyshev,V.N.,
            Berry,M.J. and Hatfield,D.L.
  TITLE     Evidence for direct roles of two additional factors, SECp43 and
            soluble liver antigen, in the selenoprotein synthesis machinery
  JOURNAL   J Biol Chem 280 (50), 41568-41575 (2005)
   PUBMED   16230358
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Herkel,J., Heidrich,B., Nieraad,N., Wies,I., Rother,M. and
            Lohse,A.W.
  TITLE     Fine specificity of autoantibodies to soluble liver antigen and
            liver/pancreas
  JOURNAL   Hepatology 35 (2), 403-408 (2002)
   PUBMED   11826415
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Volkmann,M., Martin,L., Baurle,A., Heid,H., Strassburg,C.P.,
            Trautwein,C., Fiehn,W. and Manns,M.P.
  TITLE     Soluble liver antigen: isolation of a 35-kd recombinant protein
            (SLA-p35) specifically recognizing sera from patients with
            autoimmune hepatitis
  JOURNAL   Hepatology 33 (3), 591-596 (2001)
   PUBMED   11230739
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Costa,M., Rodriguez-Sanchez,J.L., Czaja,A.J. and Gelpi,C.
  TITLE     Isolation and characterization of cDNA encoding the antigenic
            protein of the human tRNP(Ser)Sec complex recognized by
            autoantibodies from patients withtype-1 autoimmune hepatitis
  JOURNAL   Clin Exp Immunol 121 (2), 364-374 (2000)
   PUBMED   10931155
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Wies,I., Brunner,S., Henninger,J., Herkel,J., Kanzler,S., Meyer zum
            Buschenfelde,K.H. and Lohse,A.W.
  TITLE     Identification of target antigen for SLA/LP autoantibodies in
            autoimmune hepatitis
  JOURNAL   Lancet 355 (9214), 1510-1515 (2000)
   PUBMED   10801173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292476.1, BX648976.1,
            DA155173.1, CN429794.1, AC007073.2 and AW515989.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 13, 2009 this sequence version replaced
            NP_722547.2, NP_058651.2.
            
            Summary: The amino acid selenocysteine is the only amino acid that
            does not have its own tRNA synthetase. Instead, this amino acid is
            synthesized on its cognate tRNA in a three step process. The
            protein encoded by this gene catalyzes the third step in the
            process, the conversion of O-phosphoseryl-tRNA(Sec) to
            selenocysteinyl-tRNA(Sec).[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.158496.1,
                                           SRR1660807.126448.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382103.7/ ENSP00000371535.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..501
                     /product="O-phosphoseryl-tRNA(Sec) selenium transferase
                     isoform 1"
                     /EC_number="2.9.1.2"
                     /note="soluble liver antigen/liver pancreas antigen;
                     O-phosphoseryl-tRNA(Sec) selenium transferase; SLA/LP
                     autoantigen; liver-pancreas antigen; UGA suppressor
                     tRNA-associated protein; tRNA(Ser/Sec)-associated
                     antigenic protein"
                     /calculated_mol_wt=55595
     Region          1..44
                     /region_name="Tetramerization.
                     /evidence=ECO:0000269|PubMed:19608919"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HD40.2)"
     Region          12..458
                     /region_name="selenium_SpcS"
                     /note="O-phosphoseryl-tRNA(Sec) selenium transferase;
                     TIGR03531"
                     /db_xref="CDD:211833"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HD40.2)"
     Site            74
                     /site_type="other"
                     /note="May act as a substrate filter by repelling
                     compounds with a negatively charged alpha-carboxylate.
                     /evidence=ECO:0000250|UniProtKB:Q6P6M7; propagated from
                     UniProtKB/Swiss-Prot (Q9HD40.2)"
     Region          96..106
                     /region_name="Phosphate loop (P-loop).
                     /evidence=ECO:0000269|PubMed:19608919"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HD40.2)"
     Site            284
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     Region          474..493
                     /region_name="SLA/LP epitope.
                     /evidence=ECO:0000269|PubMed:11826415"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HD40.2)"
     CDS             1..501
                     /gene="SEPSECS"
                     /gene_synonym="LP; PCH2D; SecS; SLA; SLA-p35; SLA/LP"
                     /coded_by="NM_016955.4:81..1586"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3432.2"
                     /db_xref="GeneID:51091"
                     /db_xref="HGNC:HGNC:30605"
                     /db_xref="MIM:613009"
ORIGIN      
        1 mnresfaage rlvspayvrq gcearrsheh lirlllekgk cpengwdest lelflhelai
       61 mdsnnflgnc gvgeregrva salvarrhyr fihgigrsgd isavqpkaag ssllnkitns
      121 lvldiiklag vhtvancfvv pmatgmsltl cfltlrhkrp kakyiiwpri dqkscfksmi
      181 tagfepvvie nvlegdelrt dlkaveakvq elgpdcilci hsttscfapr vpdrleelav
      241 icanydiphi vnnaygvqss kcmhliqqga rvgridafvq sldknfmvpv ggaiiagfnd
      301 sfiqeiskmy pgrasaspsl dvlitllslg sngykkllke rkemfsylsn qikklseayn
      361 erllhtphnp islamtlktl dehrdkavtq lgsmlftrqv sgarvvplgs mqtvsgytfr
      421 gfmshtnnyp caylnaasai gmkmqdvdlf ikrldrclka vrkerskesd dnydktedvd
      481 ieemalkldn vlldtyqdas s
//
LOCUS       NP_001354681             368 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform i [Homo sapiens].
ACCESSION   NP_001354681
VERSION     NP_001354681.1
DBSOURCE    REFSEQ: accession NM_001367752.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006001.2 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.172280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..368
                     /product="rab5 GDP/GTP exchange factor isoform i"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=42704
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          159..221
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          271..360
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..368
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367752.1:159..1265"
                     /note="isoform i is encoded by transcript variant 36"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkaeiqe
      121 akapspsinr qtsietdrvs kefieflktf hktgqeiykq tklflegmhy krdlsieeqs
      181 ecaqdfyhnv aermqtrgkv ppervekimd qiekyimtrl ykyvfcpett ddekkdlaiq
      241 kriralrwvt pqmlcvpvne dipevsdmvv kaitdiiemd skrvprdkla citkcskhif
      301 naikitknep asaddflptl iyivlkgnpp rlqsniqyit rfcnpsrlmt gedgyyftnl
      361 vmlccgfh
//
LOCUS       NP_004086                118 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E-binding protein 1 [Homo
            sapiens].
ACCESSION   NP_004086
VERSION     NP_004086.1
DBSOURCE    REFSEQ: accession NM_004095.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Wu,X., Mi,T., Jin,L., Ren,C., Wang,J., Zhang,Z., Liu,J., Wang,Z.,
            Guo,P. and He,D.
  TITLE     Tumoral EIF4EBP1 regulates the crosstalk between tumor-associated
            macrophages and tumor cells in MRTK
  JOURNAL   Eur J Pharmacol 978, 176787 (2024)
   PUBMED   38944176
  REMARK    GeneRIF: Tumoral EIF4EBP1 regulates the crosstalk between
            tumor-associated macrophages and tumor cells in MRTK.
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Al-Lamki,R.S., Tolkovsky,A.M., Alawwami,M., Lu,W., Field,S.F.,
            Wang,J., Pober,J.S. and Bradley,J.R.
  TITLE     Tumor Necrosis Factor Receptor-2 Signals Clear-Cell Renal Carcinoma
            Proliferation via Phosphorylated 4E Binding Protein-1 and
            Mitochondrial Gene Translation
  JOURNAL   Am J Pathol 194 (7), 1374-1387 (2024)
   PUBMED   38537932
  REMARK    GeneRIF: Tumor Necrosis Factor Receptor-2 Signals Clear-Cell Renal
            Carcinoma Proliferation via Phosphorylated 4E Binding Protein-1 and
            Mitochondrial Gene Translation.
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Levy,T., Voeltzke,K., Hruby,L., Alasad,K., Bas,Z.,
            Snaebjornsson,M., Marciano,R., Scharov,K., Planque,M., Vriens,K.,
            Christen,S., Funk,C.M., Hassiepen,C., Kahler,A., Heider,B.,
            Picard,D., Lim,J.K.M., Stefanski,A., Bendrin,K., Vargas-Toscano,A.,
            Kahlert,U.D., Stuhler,K., Remke,M., Elkabets,M., Grunewald,T.G.P.,
            Reichert,A.S., Fendt,S.M., Schulze,A., Reifenberger,G., Rotblat,B.
            and Leprivier,G.
  TITLE     mTORC1 regulates cell survival under glucose starvation through
            4EBP1/2-mediated translational reprogramming of fatty acid
            metabolism
  JOURNAL   Nat Commun 15 (1), 4083 (2024)
   PUBMED   38744825
  REMARK    GeneRIF: mTORC1 regulates cell survival under glucose starvation
            through 4EBP1/2-mediated translational reprogramming of fatty acid
            metabolism.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Nagaraj,S., Stankiewicz-Drogon,A., Darzynkiewicz,E., Wojda,U. and
            Grzela,R.
  TITLE     miR-483-5p orchestrates the initiation of protein synthesis by
            facilitating the decrease in phosphorylated Ser209eIF4E and 4E-BP1
            levels
  JOURNAL   Sci Rep 14 (1), 4237 (2024)
   PUBMED   38378793
  REMARK    GeneRIF: miR-483-5p orchestrates the initiation of protein
            synthesis by facilitating the decrease in phosphorylated
            Ser209eIF4E and 4E-BP1 levels.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Feigenblum,D. and Schneider,R.J.
  TITLE     Cap-binding protein (eukaryotic initiation factor 4E) and
            4E-inactivating protein BP-1 independently regulate cap-dependent
            translation
  JOURNAL   Mol Cell Biol 16 (10), 5450-5457 (1996)
   PUBMED   8816458
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Haghighat,A., Mader,S., Pause,A. and Sonenberg,N.
  TITLE     Repression of cap-dependent translation by 4E-binding protein 1:
            competition with p220 for binding to eukaryotic initiation
            factor-4E
  JOURNAL   EMBO J 14 (22), 5701-5709 (1995)
   PUBMED   8521827
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Mader,S., Lee,H., Pause,A. and Sonenberg,N.
  TITLE     The translation initiation factor eIF-4E binds to a common motif
            shared by the translation factor eIF-4 gamma and the translational
            repressors 4E-binding proteins
  JOURNAL   Mol Cell Biol 15 (9), 4990-4997 (1995)
   PUBMED   7651417
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Pause,A., Belsham,G.J., Gingras,A.C., Donze,O., Lin,T.A.,
            Lawrence,J.C. Jr. and Sonenberg,N.
  TITLE     Insulin-dependent stimulation of protein synthesis by
            phosphorylation of a regulator of 5'-cap function
  JOURNAL   Nature 371 (6500), 762-767 (1994)
   PUBMED   7935836
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Haystead,T.A., Haystead,C.M., Hu,C., Lin,T.A. and Lawrence,J.C. Jr.
  TITLE     Phosphorylation of PHAS-I by mitogen-activated protein (MAP)
            kinase. Identification of a site phosphorylated by MAP kinase in
            vitro and in response to insulin in rat adipocytes
  JOURNAL   J Biol Chem 269 (37), 23185-23191 (1994)
   PUBMED   8083223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC004459.1 and AB044548.1.
            
            Summary: This gene encodes one member of a family of translation
            repressor proteins. The protein directly interacts with eukaryotic
            translation initiation factor 4E (eIF4E), which is a limiting
            component of the multisubunit complex that recruits 40S ribosomal
            subunits to the 5' end of mRNAs. Interaction of this protein with
            eIF4E inhibits complex assembly and represses translation. This
            protein is phosphorylated in response to various signals including
            UV irradiation and insulin signaling, resulting in its dissociation
            from eIF4E and activation of mRNA translation. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE739835.1, AB044548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338825.5/ ENSP00000340691.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..118
                     /product="eukaryotic translation initiation factor
                     4E-binding protein 1"
                     /note="eIF4E-binding protein 1; phosphorylated heat- and
                     acid-stable protein regulated by insulin 1"
                     /calculated_mol_wt=12449
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Region          9..118
                     /region_name="eIF_4EBP"
                     /note="Eukaryotic translation initiation factor 4E binding
                     protein (EIF4EBP); pfam05456"
                     /db_xref="CDD:461656"
     Region          25..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:12747827,
                     ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:29236692,
                     ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60876; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:12747827,
                     ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:29236692,
                     ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Region          54..60
                     /region_name="YXXXXLphi motif.
                     /evidence=ECO:0000250|UniProtKB:P70445"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Region          64..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2, MAPK1, MAPK3 and MTOR.
                     /evidence=ECO:0000269|PubMed:12588975,
                     ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:22578813,
                     ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:29750193,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:12747827,
                     ECO:0000269|PubMed:22578813, ECO:0000269|PubMed:25702871,
                     ECO:0000269|PubMed:29750193, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q60876; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2.
                     /evidence=ECO:0000269|PubMed:12588975,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12588975,
                     ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13541.3)"
     Region          114..118
                     /region_name="TOS motif.
                     /evidence=ECO:0000269|PubMed:12747827,
                     ECO:0000269|PubMed:24403073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13541.3)"
     CDS             1..118
                     /gene="EIF4EBP1"
                     /gene_synonym="4E-BP1; 4EBP1; BP-1; PHAS-I"
                     /coded_by="NM_004095.4:41..397"
                     /db_xref="CCDS:CCDS6100.1"
                     /db_xref="GeneID:1978"
                     /db_xref="HGNC:HGNC:3288"
                     /db_xref="MIM:602223"
ORIGIN      
        1 msggsscsqt psraipatrr vvlgdgvqlp pgdysttpgg tlfsttpggt riiydrkflm
       61 ecrnspvtkt pprdlptipg vtspssdepp measqshlrn spedkragge esqfemdi
//
LOCUS       NP_536739                676 aa            linear   PRI 20-NOV-2025
DEFINITION  GRB2-associated-binding protein 2 isoform a [Homo sapiens].
ACCESSION   NP_536739
VERSION     NP_536739.1
DBSOURCE    REFSEQ: accession NM_080491.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Abd-Elmawla,M.A., Elsabagh,Y.A. and Aborehab,N.M.
  TITLE     Association of XIST/miRNA155/Gab2/TAK1 cascade with the
            pathogenesis of anti-phospholipid syndrome and its effect on cell
            adhesion molecules and inflammatory mediators
  JOURNAL   Sci Rep 13 (1), 18790 (2023)
   PUBMED   37914735
  REMARK    GeneRIF: Association of XIST/miRNA155/Gab2/TAK1 cascade with the
            pathogenesis of anti-phospholipid syndrome and its effect on cell
            adhesion molecules and inflammatory mediators.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Yin,Y., Zhang,L., Li,Y., Zhang,C. and He,A.
  TITLE     Gab2 plays a carcinogenic role in ovarian cancer by regulating
            CrkII
  JOURNAL   J Ovarian Res 16 (1), 79 (2023)
   PUBMED   37085900
  REMARK    GeneRIF: Gab2 plays a carcinogenic role in ovarian cancer by
            regulating CrkII.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Huang,L., Liu,R., Zhou,P., Tian,Y. and Lu,Z.
  TITLE     miR-9 and miR-181a Target Gab2 to Inhibit the Proliferation and
            Migration of Hepatocellular Carcinoma HepG2 Cells
  JOURNAL   Genes (Basel) 13 (11), 2152 (2022)
   PUBMED   36421826
  REMARK    GeneRIF: miR-9 and miR-181a Target Gab2 to Inhibit the
            Proliferation and Migration of Hepatocellular Carcinoma HepG2
            Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Hibi,M. and Hirano,T.
  TITLE     Gab-family adapter molecules in signal transduction of cytokine and
            growth factor receptors, and T and B cell antigen receptors
  JOURNAL   Leuk Lymphoma 37 (3-4), 299-307 (2000)
   PUBMED   10752981
  REMARK    Review article
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Bone,H. and Welham,M.J.
  TITLE     Shc associates with the IL-3 receptor beta subunit, SHIP and Gab2
            following IL-3 stimulation. Contribution of Shc PTB and SH2 domains
  JOURNAL   Cell Signal 12 (3), 183-194 (2000)
   PUBMED   10704825
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Wickrema,A., Uddin,S., Sharma,A., Chen,F., Alsayed,Y., Ahmad,S.,
            Sawyer,S.T., Krystal,G., Yi,T., Nishada,K., Hibi,M., Hirano,T. and
            Platanias,L.C.
  TITLE     Engagement of Gab1 and Gab2 in erythropoietin signaling
  JOURNAL   J Biol Chem 274 (35), 24469-24474 (1999)
   PUBMED   10455108
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Zhao,C., Yu,D.H., Shen,R. and Feng,G.S.
  TITLE     Gab2, a new pleckstrin homology domain-containing adapter protein,
            acts to uncouple signaling from ERK kinase to Elk-1
  JOURNAL   J Biol Chem 274 (28), 19649-19654 (1999)
   PUBMED   10391903
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Nishida,K., Yoshida,Y., Itoh,M., Fukada,T., Ohtani,T.,
            Shirogane,T., Atsumi,T., Takahashi-Tezuka,M., Ishihara,K., Hibi,M.
            and Hirano,T.
  TITLE     Gab-family adapter proteins act downstream of cytokine and growth
            factor receptors and T- and B-cell antigen receptors
  JOURNAL   Blood 93 (6), 1809-1816 (1999)
   PUBMED   10068651
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003086.2 and AP002985.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the GRB2-associated binding
            protein (GAB) gene family. These proteins contain pleckstrin
            homology (PH) domain, and bind SHP2 tyrosine phosphatase and GRB2
            adapter protein. They act as adapters for transmitting various
            signals in response to stimuli through cytokine and growth factor
            receptors, and T- and B-cell antigen receptors. The protein encoded
            by this gene is the principal activator of phosphatidylinositol-3
            kinase in response to activation of the high affinity IgE receptor.
            Two alternatively spliced transcripts encoding different isoforms
            have been described for this gene. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB018413.1, BC131711.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361507.5/ ENSP00000354952.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..676
                     /product="GRB2-associated-binding protein 2 isoform a"
                     /note="Grb2-associated binder 2; growth factor receptor
                     bound protein 2-associated protein 2; pp100"
                     /calculated_mol_wt=74327
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          4..126
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          127..178
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1S8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1S8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          341..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          351..358
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1S8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1S8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          492..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          510..519
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          556..643
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19172738; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQC2.1)"
     Region          656..676
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQC2.1)"
     CDS             1..676
                     /gene="GAB2"
                     /coded_by="NM_080491.3:101..2131"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8259.1"
                     /db_xref="GeneID:9846"
                     /db_xref="HGNC:HGNC:14458"
                     /db_xref="MIM:606203"
ORIGIN      
        1 msgggdvvct gwlrksppek klrryawkkr wfilrsgrms gdpdvleyyk ndhskkplri
       61 inlnfceqvd agltfnkkel qdsfvfdikt sertfylvae teedmnkwvq sicqicgfnq
      121 aeestdslrn vssaghgprs spaelssssq hllrerkssa pshssqptlf tfeppvsnhm
      181 qptlstsapq eylylhqcis rraenarsas fsqgtrasfl mrsdtavqkl aqgnghcvng
      241 isgqvhgfys lpkpsrhnte frdstydlpr slashghtkg sltgsetdne dvytfktpsn
      301 tlcrefgdll vdnmdvpatp lsayqiprtf tldknhnamt vatpgdsaia ppprppkpsq
      361 aetprwgspq qrppisensr svaatiprrn tlpamdnsrl hrasscetye ypqrggesag
      421 rsaesmsdgv gsflpgkmiv grsdstnsed nyvpmnpgss tllameragd nsqsvyipms
      481 pgahhfdslg ypsttlpvhr gpsrgseiqp ppvnrnlkpd rkakptpldl rnntvidelp
      541 fkspitksws ranhtfnsss sqycrpistq sitstdsgds eenyvpmqnp vsaspvpsgt
      601 nspapkkstg svdylaldfq psspsphrkp stssvtsdek vdyvqvdkek tqalqntmqe
      661 wtdvrqssep skgakl
//
LOCUS       NP_001161400             570 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001161400
VERSION     NP_001161400.1
DBSOURCE    REFSEQ: accession NM_001167928.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291669.1, BM760155.1,
            BG032519.1, AB006537.1, BM194193.1 and BM973472.1.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. It encodes the membrane-bound isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.160968.1,
                                           SRR14038195.635380.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..570
                     /product="interleukin-1 receptor accessory protein isoform
                     1 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=63114
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     mat_peptide     21..570
                     /product="Interleukin-1 receptor accessory protein.
                     /id=PRO_0000015450"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
                     /calculated_mol_wt=63114
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          405..552
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          549..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     CDS             1..570
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_001167928.2:388..2100"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS3298.1"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk vpaprytvel
      361 acgfgatvll vvilivvyhv ywlemvlfyr ahfgtdetil dgkeydiyvs yarnaeeeef
      421 vlltlrgvle nefgyklcif drdslpggiv tdetlsfiqk srrllvvlsp nyvlqgtqal
      481 lelkaglenm asrgninvil vqykavketk vkelkraktv ltvikwkgek skypqgrfwk
      541 qlqvampvkk sprrsssdeq glsysslknv
//
LOCUS       NP_001351798            1248 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001351798
VERSION     NP_001351798.1
DBSOURCE    REFSEQ: accession NM_001364869.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1248)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 1248)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 1248)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 1248)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 1248)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 1248)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 1248)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 1248)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 1248)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 1248)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.135588.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..1248
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 6"
                     /calculated_mol_wt=144522
     Region          181..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          373..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          727..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          805..845
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          905..924
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          1106..1139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     Region          1224..1248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1MSJ5.4)"
     CDS             1..1248
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_001364869.1:8..3754"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS94301.1"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqknf lstsetdpst lgvslpiger lsakerlkle rnkeynqflr
      181 gkeessekfr qvekstepks qrnkkpigqv kpdltsqiqt scensegprk dvltpseaye
      241 ellnqrrlee dryrqlddei elrnrriikk aneevgisnl khqrfaskag ipdrrfhrfn
      301 edrvfdrryh rpdqdpevse emderfryes dfdrrlsrvy tndrmhrnkr gnmppmehdg
      361 dvieqsniri ssaenksapd netsksanqd tcspfagmlf ggedreliqr rkekyrlell
      421 eqmaeqqrnk rrekdlelrv aasgaqdpek spdrlkqfsv aprhfeemip perpriafqt
      481 plpplsapsv ppipsvhpvp sqnedlrsgl ssalgemvsp riaplppppl lpplatnyrt
      541 pyddayyfyg srntfdpsla yygsgmmgvq paayvsapvt hqlaqpvvnt vgqnelkits
      601 dqvinsglif edkpkpskqs lqsyqealqq qirereerrk kereekeeye akleaemrty
      661 npwgkgggga plrdakgnli tdlnrmhrqn idayhnpdar tyedkravvs ldpnlatsna
      721 enledaanks sghmqtqssp fargnvfgep ptelqikqqe lyknflrfqi eekkqreeae
      781 rerlriaeek eerrlaeqra riqqeyeeeq ekkrekeeeq rlkneehirl aeerqkeaer
      841 kkkeeeekyn lqlqhycerd nligeetkhm rqpspivpal qnkiasklqr ppsvdsiirs
      901 fihessmsra qsppvparkn qlraeeekkn vimelsemrk qlrseerrlq erllhmdsdd
      961 eipirkkern pmdifdmarh rlqapvrrqs pkgldaatfq nvhdfnelkd rdsetrvdlk
     1021 fmyldpprdh htleiqqqal lreqqkrlnr ikmqegakvd ldaipsakvr eqrmprddts
     1081 dflknslles dsafigayge typaieddvl pppsqlpsar errrnkwkgl didssrpnva
     1141 pdglslksis svnvdelrvr neermrrlne fhnkpintdd esslvdpddi mkhigddgsn
     1201 svatepwlrp gtsetlkrfm aeqlnqeqqq ipgkpgtftw qglstahg
//
LOCUS       NP_001340201             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340201
VERSION     NP_001340201.1
DBSOURCE    REFSEQ: accession NM_001353272.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.262284.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353272.1:727..1263"
                     /note="isoform 2 is encoded by transcript variant 34"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_055412                756 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxynucleotidyltransferase terminal-interacting protein 2 [Homo
            sapiens].
ACCESSION   NP_055412
VERSION     NP_055412.2
DBSOURCE    REFSEQ: accession NM_014597.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Yoshizawa,M., Shiozaki,A. and Ashihara,E.
  TITLE     Depletion of DNTTIP2 Induces Cell Cycle Arrest in Pancreatic Cancer
            Cells
  JOURNAL   Cancer Genomics Proteomics 21 (1), 18-29 (2024)
   PUBMED   38151292
  REMARK    GeneRIF: Depletion of DNTTIP2 Induces Cell Cycle Arrest in
            Pancreatic Cancer Cells.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Koiwai,K., Noma,S., Takahashi,Y., Hayano,T., Maezawa,S., Kouda,K.,
            Matsumoto,T., Suzuki,M., Furuichi,M. and Koiwai,O.
  TITLE     TdIF2 is a nucleolar protein that promotes rRNA gene promoter
            activity
  JOURNAL   Genes Cells 16 (7), 748-764 (2011)
   PUBMED   21668587
  REMARK    GeneRIF: The TdIF2 might promote hrDNAP activity by suppressing
            Tip60's HAT activity and promoting UBF acetylation.
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Edmiston,J.S., Archer,K.J., Scian,M.J., Joyce,A.R., Zedler,B.K. and
            Murrelle,E.L.
  TITLE     Gene expression profiling of peripheral blood leukocytes identifies
            potential novel biomarkers of chronic obstructive pulmonary disease
            in current and former smokers
  JOURNAL   Biomarkers 15 (8), 715-730 (2010)
   PUBMED   20887155
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Bu,H., Kashireddy,P., Chang,J., Zhu,Y.T., Zhang,Z., Zheng,W.,
            Rao,S.M. and Zhu,Y.J.
  TITLE     ERBP, a novel estrogen receptor binding protein enhancing the
            activity of estrogen receptor
  JOURNAL   Biochem Biophys Res Commun 317 (1), 54-59 (2004)
   PUBMED   15047147
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Fujita,K., Shimazaki,N., Ohta,Y., Kubota,T., Ibe,S., Toji,S.,
            Tamai,K., Fujisaki,S., Hayano,T. and Koiwai,O.
  TITLE     Terminal deoxynucleotidyltransferase forms a ternary complex with a
            novel chromatin remodeling protein with 82 kDa and core histone
  JOURNAL   Genes Cells 8 (6), 559-571 (2003)
   PUBMED   12786946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU134239.1, AL049796.28,
            AA832262.1 and AI436814.1.
            
            On Oct 26, 2004 this sequence version replaced NP_055412.1.
            
            Summary: This gene is thought to be involved in chromatin
            remodeling and gene transcription. The encoded nuclear protein
            binds to and enhances the transcriptional activity of the estrogen
            receptor alpha, and also interacts with terminal
            deoxynucleotidyltransferase. The expression profile of this gene is
            a potential biomarker for chronic obstructive pulmonary disease.
            [provided by RefSeq, Dec 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.116056.1,
                                           SRR1660809.206858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000436063.7/ ENSP00000411010.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..756
                     /product="deoxynucleotidyltransferase terminal-interacting
                     protein 2"
                     /note="estrogen receptor binding protein; acidic 82 kDa
                     protein mRNA; tdT-interacting factor 2; LPTS-interacting
                     protein 2"
                     /calculated_mol_wt=84338
     Region          1..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Region          156..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Region          510..547
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Region          548..605
                     /region_name="TdBR region, mediates interaction with DNTT"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q5QJE6.2)"
     Region          639..731
                     /region_name="Fcf2"
                     /note="Fcf2 pre-rRNA processing; pfam08698"
                     /db_xref="CDD:462566"
     CDS             1..756
                     /gene="DNTTIP2"
                     /gene_synonym="ERBP; FCF2; HSU15552; LPTS-RP2; TdIF2"
                     /coded_by="NM_014597.5:59..2329"
                     /db_xref="CCDS:CCDS44174.1"
                     /db_xref="GeneID:30836"
                     /db_xref="HGNC:HGNC:24013"
                     /db_xref="MIM:611199"
ORIGIN      
        1 mvvtrsarak asiqaasaes sgqksfaang iqahpesstg sdarttaesq ttgkqslipr
       61 tpkarkrksr ttgslpkgte pstdgetsea esnysvsehh dtilrvtrrr qiliacspvs
      121 svrkkpkvtp tkesyteeiv seaeshvsgi srivlptekt tgarrskaks ltdpsqesht
      181 eaisdaetss sdisfsgiat rrtrsmqrkl kaqtekkdsk ivpgnekqiv gtpvnsedsd
      241 trqtshlqar slseinkpnf ynndfdddfs hrsseniltv heqanveslk etkqnckdld
      301 edangitdeg keinekssql knlselqdts lqqlvsqrhs tpqnknavsv hsnlnseavm
      361 ksltqtfatv evgrwnnnkk spikasdltk fgdcggsdde eestvisvse dmnsegnvdf
      421 ecdtklytsa pntsqgkdns vllvlssdes qqsensenee dtlcfvensg qreslsgdtg
      481 slscdnalfv idttpgmsad knfyleeedk asevaieeek eeeedeksee dssdhdened
      541 efsdeedfln stkakllklt sssidpglsi kqlgglyinf nadklqsnkr tltqikekkk
      601 nellqkavit pdfeknhcvp pyseskyqlq kkrrkerqkt agdgwfgmka pemtnelknd
      661 lkalkmrasm dpkrfykknd rdgfpkyfqi gtivdnpadf yhsripkkqr krtiveella
      721 dsefrrynrr kyseimaeka anaagkkfrk kkkfrn
//
LOCUS       NP_001164654             197 aa            linear   PRI 20-NOV-2025
DEFINITION  EF-hand calcium-binding domain-containing protein 9 [Homo sapiens].
ACCESSION   NP_001164654 XP_001715952 XP_946145
VERSION     NP_001164654.1
DBSOURCE    REFSEQ: accession NM_001171183.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Lin,S., Ke,M., Zhang,Y., Yan,Z. and Wu,J.
  TITLE     Structure of a mammalian sperm cation channel complex
  JOURNAL   Nature 595 (7869), 746-750 (2021)
   PUBMED   34225353
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Brown,S.G., Miller,M.R., Lishko,P.V., Lester,D.H., Publicover,S.J.,
            Barratt,C.L.R. and Martins Da Silva,S.
  TITLE     Homozygous in-frame deletion in CATSPERE in a man producing
            spermatozoa with loss of CatSper function and compromised
            fertilizing capacity
  JOURNAL   Hum Reprod 33 (10), 1812-1816 (2018)
   PUBMED   30239785
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Grabarek,Z.
  TITLE     Structural basis for diversity of the EF-hand calcium-binding
            proteins
  JOURNAL   J Mol Biol 359 (3), 509-525 (2006)
   PUBMED   16678204
  REMARK    Review article
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Bhattacharya,S., Bunick,C.G. and Chazin,W.J.
  TITLE     Target selectivity in EF-hand calcium binding proteins
  JOURNAL   Biochim Biophys Acta 1742 (1-3), 69-79 (2004)
   PUBMED   15590057
  REMARK    Review article
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Maki,M., Kitaura,Y., Satoh,H., Ohkouchi,S. and Shibata,H.
  TITLE     Structures, functions and molecular evolution of the penta-EF-hand
            Ca2+-binding proteins
  JOURNAL   Biochim Biophys Acta 1600 (1-2), 51-60 (2002)
   PUBMED   12445459
  REMARK    Review article
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Lewit-Bentley,A. and Rety,S.
  TITLE     EF-hand calcium-binding proteins
  JOURNAL   Curr Opin Struct Biol 10 (6), 637-643 (2000)
   PUBMED   11114499
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024561.5, CN445899.1 and
            AI024830.1.
            
            On or before Jan 16, 2010 this sequence version replaced
            XP_946145.2, XP_001715952.2.
            
            Summary: This gene encodes a protein with a C-terminal EF-hand
            calcium-binding domain similar to that found in penta-EF-hand (PEF)
            protein family members. The EF-hand is a helix-loop-helix structure
            with a canonical twelve-residue sequence that coordinates a calcium
            molecule with pentagonal bipyramidal symmetry. [provided by RefSeq,
            Jul 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN445899.1, BU568218.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398186.5/ ENSP00000381247.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..197
                     /product="EF-hand calcium-binding domain-containing
                     protein 9"
                     /calculated_mol_wt=23806
     Region          29..162
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          177..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A8MZ26.2)"
     CDS             1..197
                     /gene="EFCAB9"
                     /coded_by="NM_001171183.2:2..595"
                     /db_xref="CCDS:CCDS54946.1"
                     /db_xref="GeneID:285588"
                     /db_xref="HGNC:HGNC:34530"
                     /db_xref="MIM:618520"
ORIGIN      
        1 mrlkqgsflw ylyldkiycl lsvrnvkala eyfhildvhg kntlndvlfy hflhhvtdlk
       61 kaqinivfdm ldwnavgeid fekfymlvcm llahqnhleg qfmyrhsrpv fdlldlkgdl
      121 rigaknfemy rflfniqkqe lkdlfrdfdi tgdnrlnyqe fklytiiytd klqkrqktee
      181 kekgerkrsl yskchik
//
LOCUS       NP_001340532             343 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform k [Homo sapiens].
ACCESSION   NP_001340532 XP_016877025
VERSION     NP_001340532.1
DBSOURCE    REFSEQ: accession NM_001353603.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877025.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (18), as well as variants 17, 19,
            and 20, encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.32946.1,
                                           SRR1803611.114247.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..343
                     /product="lysosomal cobalamin transporter ABCD4 isoform k"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=37800
     Region          <1..319
                     /region_name="SunT"
                     /note="ABC-type bacteriocin/lantibiotic exporters, contain
                     an N-terminal double-glycine peptidase domain [Defense
                     mechanisms]; COG2274"
                     /db_xref="CDD:441875"
     Region          124..335
                     /region_name="ABCD_peroxisomal_ALDP"
                     /note="ATP-binding cassette domain of peroxisomal
                     transporter, subfamily D; cd03223"
                     /db_xref="CDD:213190"
     CDS             1..343
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353603.2:589..1620"
                     /note="isoform k is encoded by transcript variant 18"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mrslllstvg intfdylgsi lsyvviaipi fsgvygdlsp aelstlvskn afvciylisc
       61 ftqlidlstt lsdvagythr igqlretlld mslksqdcei lgesewgldt ppgwpaaepa
      121 dtafllervs isapssdkpl ikdlslkise gqsllitgnt gtgktsllrv lgglwtstrg
      181 svqmltdfgp hgvlflpqkp fftdgtlreq viyplkevyp dsgsadderi lrflelagls
      241 nlvartegld qqvdwnwydv lspgemqrls farlfylqpk yavldeatsa lteevesely
      301 rigqqlgmtf isvghrqsle kfhslvlklc gggrwelmri kve
//
LOCUS       NP_001357525            1191 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase ID isoform d [Homo sapiens].
ACCESSION   NP_001357525
VERSION     NP_001357525.1
DBSOURCE    REFSEQ: accession NM_001370596.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1191)
  AUTHORS   Honsho,M., Mawatari,S. and Fujiki,Y.
  TITLE     ATP8B2-Mediated Asymmetric Distribution of Plasmalogens Regulates
            Plasmalogen Homeostasis and Plays a Role in Intracellular Signaling
  JOURNAL   Front Mol Biosci 9, 915457 (2022)
   PUBMED   35832735
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1191)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1191)
  AUTHORS   Takatsu,H., Tanaka,G., Segawa,K., Suzuki,J., Nagata,S., Nakayama,K.
            and Shin,H.W.
  TITLE     Phospholipid flippase activities and substrate specificities of
            human type IV P-type ATPases localized to the plasma membrane
  JOURNAL   J Biol Chem 289 (48), 33543-33556 (2014)
   PUBMED   25315773
  REMARK    Erratum:[J Biol Chem. 2016 Oct 7;291(41):21421. doi:
            10.1074/jbc.A114.593012. PMID: 27825076]
REFERENCE   4  (residues 1 to 1191)
  AUTHORS   Bryde,S., Hennrich,H., Verhulst,P.M., Devaux,P.F., Lenoir,G. and
            Holthuis,J.C.
  TITLE     CDC50 proteins are critical components of the human class-1
            P4-ATPase transport machinery
  JOURNAL   J Biol Chem 285 (52), 40562-40572 (2010)
   PUBMED   20961850
REFERENCE   5  (residues 1 to 1191)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   6  (residues 1 to 1191)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   7  (residues 1 to 1191)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   8  (residues 1 to 1191)
  AUTHORS   Harris,M.J. and Arias,I.M.
  TITLE     FIC1, a P-type ATPase linked to cholestatic liver disease, has
            homologues (ATP8B2 and ATP8B3) expressed throughout the body
  JOURNAL   Biochim Biophys Acta 1633 (2), 127-131 (2003)
   PUBMED   12880872
REFERENCE   9  (residues 1 to 1191)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1191)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162591.16.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.116486.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1191
                     /product="phospholipid-transporting ATPase ID isoform d"
                     /EC_number="7.6.2.1"
                     /note="phospholipid-transporting ATPase ID; probable
                     phospholipid-transporting ATPase ID; ATPase, class I, type
                     8B, member 2; P4-ATPase flippase complex alpha subunit
                     ATP8B2; 36/8-9 fusion protein with epitope for anti-lectin
                     antibody; ATPase, aminophospholipid transporter, class I,
                     type 8B, member 2"
                     /calculated_mol_wt=135277
     Region          31..973
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            order(392..394,537,560..562,627,675..677,789,792,795,815,
                     818)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     CDS             1..1191
                     /gene="ATP8B2"
                     /gene_synonym="ATPID"
                     /coded_by="NM_001370596.1:216..3791"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:57198"
                     /db_xref="HGNC:HGNC:13534"
                     /db_xref="MIM:605867"
ORIGIN      
        1 mavcakkrpp eeerrarand reynekfqya snciktskyn iltflpvnlf eqfqevanty
       61 flfllilqli pqisslswft tivplvlvlt itavkdatdd yfrhksdnqv nnrqsqvlin
      121 gilqqeqwmn vcvgdiikle nnqfvaadll llsssephgl cyietaeldg etnmkvrqai
      181 pvtselgdis klakfdgevi ceppnnkldk fsgtlywken kfplsnqnml lrgcvlrnte
      241 wcfglvifag pdtklmqnsg rtkfkrtsid rlmntlvlwi fgflvcmgvi laignaiweh
      301 evgmrfqvyl pwdeavdsaf fsgflsfwsy iiilntvvpi slyvsvevir lghsyfinwd
      361 kkmfcmkkrt paeartttln eelgqveyif sdktgtltqn imvfnkcsin ghsygdvfdv
      421 lghkaelger pepvdfsfnp ladkkflfwd pslleavkig dphtheffrl lslchtvmse
      481 eknegelyyk aqspdegalv taarnfgfvf rsrtpktitv hemgtaityq llaildfnni
      541 rkrmsvivrn pegkirlyck gadtilldrl hhstqellnt tmdhlneyag eglrtlvlay
      601 kdldeeyyee waerrlqasl aqdsredrla siyeeeslwy fqllgataie dklqqgvpet
      661 ialltlanik iwvltgdkqe tavnigysck mltddmtevf ivtghtvlev reelrkarek
      721 mmdssrsvgn gftyqdklss skltsvleav ageyalving hslahalead melefletac
      781 ackaviccrv tplqkaqvve lvkkykkavt laigdgandv smiktahigv gisgqegiqa
      841 vlasdysfsq fkflqrlllv hgrwsylrmc kflcyffykn faftmvhfwf gffcgfsaqt
      901 vydqyfitly nivytslpvl amgvfdqdvp eqrsmeypkl yepgqlnllf nkrefficia
      961 qgiytsvlmf fipygvfada trddgtqlad yqsfavtvat slvivvsvqi gldtgywtai
     1021 nhffiwgsla vyfailfamh snglfdmfpn qfrfvgnaqn tlaqptvwlt ivlttvvcim
     1081 pvvafrflrl nlkpdlsdtv rytqlvrkkq kaqhrcmrrv grtgsrrsgy afshqegfge
     1141 limsgknmrl sslalssftt rsssswiesl rrkksdsass psggadkplk g
//
LOCUS       NP_647599                475 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 7 [Homo sapiens].
ACCESSION   NP_647599
VERSION     NP_647599.1
DBSOURCE    REFSEQ: accession NM_139349.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF594020.1, AF043900.1,
            AC012508.10, AF070576.1 and BM711160.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (7) lacks three in-frame exons in
            the coding region, compared to variant 1. Isoform 7, also called
            IIc2 and S1/R3-c, is shorter than isoform 1 and binds dynamin and
            synaptojanin.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043900.1, SRR1660809.235220.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..475
                     /product="myc box-dependent-interacting protein 1 isoform
                     7"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=51606
     Region          31..241
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,197,200..201,203,208..209,211..212,215..216,
                     218..219,222..223,225..226,230,233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <239..>359
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          403..474
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(414..420,439,441..444,467,469..470)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..475
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_139349.3:212..1639"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS42743.1"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakaeeelik
      181 aqkvfeemnv dlqeelpslw nsrvgfyvnt fqsiagleen fhkemsklnq nlndvlvgle
      241 kqhgsntftv kaqpsdnapa kgnkspsppd gspaatpeir vnhepepagg atpgatlpks
      301 psqptespag slpsgepsaa egtfavswps qtaepgpaqp aeasevaggt qpaagaqepg
      361 etaaseaass slpavvvetf patvngtveg gsgagrldlp pgfmfkvqaq hdytatdtde
      421 lqlkagdvvl vipfqnpeeq degwlmgvke sdwnqhkele kcrgvfpenf tervp
//
LOCUS       NP_001305788             183 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxyguanosine kinase, mitochondrial isoform c precursor [Homo
            sapiens].
ACCESSION   NP_001305788
VERSION     NP_001305788.1
DBSOURCE    REFSEQ: accession NM_001318859.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Guzman,H., Yazdani,S., Harmon,J.L., Chapman,K.A., Vitola,B.,
            Pyle,L., McKnight,H., Sigal,W., Lord,K., De Leon,D.D., Merchant,N.
            and Ganetzky,R.
  TITLE     Case report: Two unexpected cases of DGUOK-related mitochondrial
            DNA depletion syndrome presenting with hyperinsulinemic
            hypoglycemia
  JOURNAL   Front Endocrinol (Lausanne) 14, 1268135 (2023)
   PUBMED   38027095
  REMARK    GeneRIF: Case report: Two unexpected cases of DGUOK-related
            mitochondrial DNA depletion syndrome presenting with
            hyperinsulinemic hypoglycemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Unal,O., Hismi,B., Kilic,M., Gulsen,H.H., Coskun,T., Sivri,S.H.,
            Dursun,A., Yuce,A. and Tokatli,A.
  TITLE     Deoxyguanosine kinase deficiency: a report of four patients
  JOURNAL   J Pediatr Endocrinol Metab 30 (6), 697-702 (2017)
   PUBMED   28493820
  REMARK    GeneRIF: DGUOK deficiency and mutation is associated with
            mitochondrial DNA depletion syndromes.
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Jullig,M. and Eriksson,S.
  TITLE     Mitochondrial and submitochondrial localization of human
            deoxyguanosine kinase
  JOURNAL   Eur J Biochem 267 (17), 5466-5472 (2000)
   PUBMED   10951205
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Johansson,M., Bajalica-Lagercrantz,S., Lagercrantz,J. and
            Karlsson,A.
  TITLE     Localization of the human deoxyguanosine kinase gene (DGUOK) to
            chromosome 2p13
  JOURNAL   Genomics 38 (3), 450-451 (1996)
   PUBMED   8975728
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Wang,L., Hellman,U. and Eriksson,S.
  TITLE     Cloning and expression of human mitochondrial deoxyguanosine kinase
            cDNA
  JOURNAL   FEBS Lett 390 (1), 39-43 (1996)
   PUBMED   8706825
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning and expression of human deoxyguanosine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7258-7262 (1996)
   PUBMED   8692979
REFERENCE   10 (residues 1 to 183)
  AUTHORS   El-Hattab,A.W. and Scaglia,F.
  TITLE     Deoxyguanosine Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU099795.1, EL584040.1,
            AC073046.7 and BC024019.1.
            
            Summary: In mammalian cells, the phosphorylation of purine
            deoxyribonucleosides is mediated predominantly by two
            deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and
            mitochondrial deoxyguanosine kinase. The protein encoded by this
            gene is responsible for phosphorylation of purine
            deoxyribonucleosides in the mitochondrial matrix. In addition, this
            protein phosphorylates several purine deoxyribonucleoside analogs
            used in the treatment of lymphoproliferative disorders, and this
            phosphorylation is critical for the effectiveness of the analogs.
            Alternative splice variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice junction and lacks two alternate exons compared to variant
            1. The resulting isoform (c) has the same N- and C-termini but is
            shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.109795.1,
                                           SRR7346977.121121.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..183
                     /product="deoxyguanosine kinase, mitochondrial isoform c
                     precursor"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxyguanosine kinase, mitochondrial;
                     deoxyadenosine kinase, mitochondrial"
                     /calculated_mol_wt=16636
     transit_peptide 1..39
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q16854.2)"
                     /calculated_mol_wt=4113
     Region          41..181
                     /region_name="NK"
                     /note="Nucleoside/nucleotide kinase (NK) is a protein
                     superfamily consisting of multiple families of enzymes
                     that share structural similarity and are functionally
                     related to the catalysis of the reversible phosphate group
                     transfer from nucleoside triphosphates...; cl17190"
                     /db_xref="CDD:450170"
     Site            order(45,50..53)
                     /site_type="active"
                     /db_xref="CDD:238461"
     CDS             1..183
                     /gene="DGUOK"
                     /gene_synonym="dGK; MTDPS3; NCPH; NCPH1; PEOB4"
                     /coded_by="NM_001318859.2:32..583"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:1716"
                     /db_xref="HGNC:HGNC:2858"
                     /db_xref="MIM:601465"
ORIGIN      
        1 maagrlflsr lrapfssmak splegvsssr glhagrgprr lsiegniavg kstfvklltk
       61 typewhvate pvatwqniqa agtqkactaq slgnlldmmy reparwsytf qtfsflsrlk
      121 vqlepfpekl lqarkpvqif erlhfealmn ipvlvldvnd dfseevtkqe dlmrevntfv
      181 knl
//
LOCUS       NP_006457                316 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC6 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006457
VERSION     NP_006457.2
DBSOURCE    REFSEQ: accession NM_006466.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Hu,P., Wu,S., Sun,Y., Yuan,C.C., Kobayashi,R., Myers,M.P. and
            Hernandez,N.
  TITLE     Characterization of human RNA polymerase III identifies orthologues
            for Saccharomyces cerevisiae RNA polymerase III subunits
  JOURNAL   Mol Cell Biol 22 (22), 8044-8055 (2002)
   PUBMED   12391170
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Mertens,C., Hofmann,I., Wang,Z., Teichmann,M., Sepehri Chong,S.,
            Schnolzer,M. and Franke,W.W.
  TITLE     Nuclear particles containing RNA polymerase III complexes
            associated with the junctional plaque protein plakophilin 2
  JOURNAL   Proc Natl Acad Sci U S A 98 (14), 7795-7800 (2001)
   PUBMED   11416169
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Jones,E., Kimura,H., Vigneron,M., Wang,Z., Roeder,R.G. and
            Cook,P.R.
  TITLE     Isolation and characterization of monoclonal antibodies directed
            against subunits of human RNA polymerases I, II, and III
  JOURNAL   Exp Cell Res 254 (1), 163-172 (2000)
   PUBMED   10623476
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Three human RNA polymerase III-specific subunits form a subcomplex
            with a selective function in specific transcription initiation
  JOURNAL   Genes Dev 11 (10), 1315-1326 (1997)
   PUBMED   9171375
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121893.21.
            
            On Aug 12, 2003 this sequence version replaced NP_006457.1.
            
            Summary: The protein encoded by this gene is one of more than a
            dozen subunits forming eukaryotic RNA polymerase III (RNA Pol III),
            which transcribes 5S ribosomal RNA and tRNA genes. This protein has
            been shown to bind both TFIIIB90 and TBP, two subunits of RNA
            polymerase III transcription initiation factor IIIB (TFIIIB).
            Unlike most of the other RNA Pol III subunits, the encoded protein
            is unique to this polymerase. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.180635.1,
                                           SRR3476690.1022305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377603.5/ ENSP00000366828.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..316
                     /product="DNA-directed RNA polymerase III subunit RPC6
                     isoform 1"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerase III subunit RPC6;
                     polymerase (RNA) III (DNA directed) polypeptide F, 39 kDa;
                     RNA polymerase III C39 subunit; RNA polymerase III subunit
                     C6; polymerase (RNA) III subunit F"
                     /calculated_mol_wt=35553
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H1D9.1)"
     Region          12..315
                     /region_name="RNA_pol_Rpc34"
                     /note="RNA polymerase Rpc34 subunit; pfam05158"
                     /db_xref="CDD:398703"
     CDS             1..316
                     /gene="POLR3F"
                     /gene_synonym="C34; IMD101; RPC39; RPC6"
                     /coded_by="NM_006466.4:118..1068"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13135.1"
                     /db_xref="GeneID:10621"
                     /db_xref="HGNC:HGNC:15763"
                     /db_xref="MIM:617455"
ORIGIN      
        1 maevkvkvqp pdadpveien riielchqfp hgitdqviqn emphieaqqr avainrllsm
       61 gqldllrsnt gllyrikdsq nagkmkgsdn qeklvyqiie dagnkgiwsr diryksnlpl
      121 teinkilknl eskklikavk svaaskkkvy mlynlqpdrs vtggawysdq dfesefvevl
      181 nqqcfkflqs kaetareskq npmiqrnssf asshevwkyi celgiskvel smedietiln
      241 tliydgkvem tiiaakegtv gsvdghmkly ravnpiippt glvrapcglc pvfddchegg
      301 eispsnciym tewlef
//
LOCUS       NP_055209                345 aa            linear   PRI 20-NOV-2025
DEFINITION  growth hormone-inducible transmembrane protein [Homo sapiens].
ACCESSION   NP_055209
VERSION     NP_055209.2
DBSOURCE    REFSEQ: accession NM_014394.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Huang,S., Liu,J., Hu,J., Hou,Y., Hu,M., Zhang,B., Luo,H., Fu,S.,
            Chen,Y., Liu,X., Chen,Z. and Wang,L.
  TITLE     GHITM regulates malignant phenotype and sensitivity to PD-1
            blockade of renal cancer cells via Notch signalling
  JOURNAL   J Cell Mol Med 28 (8), e18290 (2024)
   PUBMED   38588015
  REMARK    GeneRIF: GHITM regulates malignant phenotype and sensitivity to
            PD-1 blockade of renal cancer cells via Notch signalling.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Austin,S., Mekis,R., Mohammed,S.E.M., Scalise,M., Wang,W.A.,
            Galluccio,M., Pfeiffer,C., Borovec,T., Parapatics,K., Vitko,D.,
            Dinhopl,N., Demaurex,N., Bennett,K.L., Indiveri,C. and
            Nowikovsky,K.
  TITLE     TMBIM5 is the Ca2+ /H+ antiporter of mammalian mitochondria
  JOURNAL   EMBO Rep 23 (12), e54978 (2022)
   PUBMED   36321428
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Patron,M., Tarasenko,D., Nolte,H., Kroczek,L., Ghosh,M., Ohba,Y.,
            Lasarzewski,Y., Ahmadi,Z.A., Cabrera-Orefice,A., Eyiama,A.,
            Kellermann,T., Rugarli,E.I., Brandt,U., Meinecke,M. and Langer,T.
  TITLE     Regulation of mitochondrial proteostasis by the proton gradient
  JOURNAL   EMBO J 41 (16), e110476 (2022)
   PUBMED   35912435
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Zhou,J., Zhu,T., Hu,C., Li,H., Chen,G., Xu,G., Wang,S., Zhou,J. and
            Ma,D.
  TITLE     Comparative genomics and function analysis on BI1 family
  JOURNAL   Comput Biol Chem 32 (3), 159-162 (2008)
   PUBMED   18440869
  REMARK    GeneRIF: The tmbim5 may participate in cell death regulation by
            interacting with proteins of Bcl-2 family, promoting tumor
            metastasis, which is deduced from the evolutionary conservation of
            the membrane protein family containing multiple membrane spanning
            segments
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Oka,T., Sayano,T., Tamai,S., Yokota,S., Kato,H., Fujii,G. and
            Mihara,K.
  TITLE     Identification of a novel protein MICS1 that is involved in
            maintenance of mitochondrial morphology and apoptotic release of
            cytochrome c
  JOURNAL   Mol Biol Cell 19 (6), 2597-2608 (2008)
   PUBMED   18417609
  REMARK    GeneRIF: MICS1 individually functions in mitochondrial morphology
            and cytochrome c release.
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL603756.8, BC010354.1 and AC022389.9.
            
            On Nov 22, 2006 this sequence version replaced NP_055209.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.174360.1,
                                           SRR1803615.97173.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372134.6/ ENSP00000361207.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..345
                     /product="growth hormone-inducible transmembrane protein"
                     /note="mitochondrial morphology and cristae structure 1;
                     transmembrane BAX inhibitor motif containing 5; dermal
                     papilla-derived protein 2; transmembrane BAX inhibitor
                     motif-containing protein 5"
                     /calculated_mol_wt=32081
     transit_peptide 1..45
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9H3K2.2)"
                     /calculated_mol_wt=5142
     mat_peptide     46..345
                     /product="Growth hormone-inducible transmembrane protein.
                     /id=PRO_0000179119"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
                     /calculated_mol_wt=32081
     Region          81..344
                     /region_name="GHITM"
                     /note="Growth-hormone inducible transmembrane protein;
                     cd10431"
                     /db_xref="CDD:198413"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            126..146
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            191..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            214..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            245..265
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     Site            272..292
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3K2.2)"
     CDS             1..345
                     /gene="GHITM"
                     /gene_synonym="DERP2; HSPC282; MICS1; My021; PTD010;
                     TMBIM5"
                     /coded_by="NM_014394.3:125..1162"
                     /db_xref="CCDS:CCDS41542.1"
                     /db_xref="GeneID:27069"
                     /db_xref="HGNC:HGNC:17281"
                     /db_xref="MIM:619205"
ORIGIN      
        1 mlaarlvclr tlpsrvfhpa ftkaspvvkn sitknqwllt psreyatktr igirrgrtgq
       61 elkeaaleps mekifkidqm grwfvaggaa vglgalcyyg lglsneigai ekaviwpqyv
      121 kdrihstymy lagsigltal saiaisrtpv lmnfmmrgsw vtigvtfaam vgagmlvrsi
      181 pydqspgpkh lawllhsgvm gavvapltil ggplliraaw ytagivggls tvamcapsek
      241 flnmgaplgv glglvfvssl gsmflppttv agatlysvam ygglvlfsmf llydtqkvik
      301 raevspmygv qkydpinsml siymdtlnif mrvatmlatg gnrkk
//
LOCUS       NP_001011548             317 aa            linear   PRI 20-NOV-2025
DEFINITION  melanoma-associated antigen 4 [Homo sapiens].
ACCESSION   NP_001011548
VERSION     NP_001011548.1
DBSOURCE    REFSEQ: accession NM_001011548.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Hashimoto,K., Nishimura,S., Shinyashiki,Y., Ito,T., Kakinoki,R. and
            Akagi,M.
  TITLE     Involvement of NY-ESO-1 and MAGE-A4 in the pathogenesis of desmoid
            tumors
  JOURNAL   Medicine (Baltimore) 102 (22), e33908 (2023)
   PUBMED   37266606
  REMARK    GeneRIF: Involvement of NY-ESO-1 and MAGE-A4 in the pathogenesis of
            desmoid tumors.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Cai,R., Zhao,F., Zhou,H., Wang,Z., Lin,D., Huang,L., Xie,W.,
            Chen,J., Zhou,L., Zhang,N. and Huang,C.
  TITLE     A tumor-associated autoantibody panel for the detection of
            non-small cell lung cancer
  JOURNAL   Front Oncol 12, 1056572 (2022)
   PUBMED   36531074
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hashimoto,K., Nishimura,S., Ito,T., Oka,N., Kakinoki,R. and
            Akagi,M.
  TITLE     Clinicopathological assessment of cancer/testis antigens NY-ESO-1
            and MAGE-A4 in osteosarcoma
  JOURNAL   Eur J Histochem 66 (3), 3377 (2022)
   PUBMED   35736245
  REMARK    GeneRIF: Clinicopathological assessment of cancer/testis antigens
            NYESO1 and MAGEA4 in osteosarcoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Brasseur,F., Rimoldi,D., Lienard,D., Lethe,B., Carrel,S.,
            Arienti,F., Suter,L., Vanwijck,R., Bourlond,A., Humblet,Y. et al.
  TITLE     Expression of MAGE genes in primary and metastatic cutaneous
            melanoma
  JOURNAL   Int J Cancer 63 (3), 375-380 (1995)
   PUBMED   7591235
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Rogner,U.C., Wilke,K., Steck,E., Korn,B. and Poustka,A.
  TITLE     The melanoma antigen gene (MAGE) family is clustered in the
            chromosomal band Xq28
  JOURNAL   Genomics 29 (3), 725-731 (1995)
   PUBMED   8575766
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Imai,Y., Shichijo,S., Yamada,A., Katayama,T., Yano,H. and Itoh,K.
  TITLE     Sequence analysis of the MAGE gene family encoding human
            tumor-rejection antigens
  JOURNAL   Gene 160 (2), 287-290 (1995)
   PUBMED   7642112
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Ding,M., Beck,R.J., Keller,C.J. and Fenton,R.G.
  TITLE     Cloning and analysis of MAGE-1-related genes
  JOURNAL   Biochem Biophys Res Commun 202 (1), 549-555 (1994)
   PUBMED   8037761
REFERENCE   10 (residues 1 to 317)
  AUTHORS   De Plaen,E., Arden,K., Traversari,C., Gaforio,J.J., Szikora,J.P.,
            De Smet,C., Brasseur,F., van der Bruggen,P., Lethe,B., Lurquin,C.
            et al.
  TITLE     Structure, chromosomal localization, and expression of 12 genes of
            the MAGE family
  JOURNAL   Immunogenetics 40 (5), 360-369 (1994)
   PUBMED   7927540
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX479311.1 and AF274855.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the MAGEA gene family. The
            members of this family encode proteins with 50 to 80% sequence
            identity to each other. The promoters and first exons of the MAGEA
            genes show considerable variability, suggesting that the existence
            of this gene family enables the same function to be expressed under
            different transcriptional controls. The MAGEA genes are clustered
            at chromosomal location Xq28. They have been implicated in some
            hereditary disorders, such as dyskeratosis congenita. Several
            variants encoding the same protein have been found for this gene.
            [provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 5. All twelve variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX479311.1, DA912058.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276344.6/ ENSP00000276344.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..317
                     /product="melanoma-associated antigen 4"
                     /note="cancer/testis antigen family 1, member 4; MAGE-4
                     antigen; MAGE-41 antigen; MAGE-X2 antigen; cancer/testis
                     antigen 1.4; melanoma antigen family A, 4; melanoma
                     antigen family A4"
                     /calculated_mol_wt=34768
     Region          1..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43358.2)"
     Region          5..97
                     /region_name="MAGE_N"
                     /note="Melanoma associated antigen family N terminal;
                     pfam12440"
                     /db_xref="CDD:463582"
     Region          131..281
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     CDS             1..317
                     /gene="MAGEA4"
                     /gene_synonym="CT1.4; MAGE-41; MAGE-X2; MAGE4; MAGE4A;
                     MAGE4B"
                     /coded_by="NM_001011548.1:219..1172"
                     /db_xref="CCDS:CCDS14702.1"
                     /db_xref="GeneID:4103"
                     /db_xref="HGNC:HGNC:6802"
                     /db_xref="MIM:300175"
ORIGIN      
        1 msseqksqhc kpeegveaqe ealglvgaqa ptteeqeaav ssssplvpgt leevpaaesa
       61 gppqspqgas alpttisftc wrqpnegsss qeeegpstsp daeslfreal snkvdelahf
      121 llrkyrakel vtkaemlerv iknykrcfpv ifgkaseslk mifgidvkev dpasntytlv
      181 tclglsydgl lgnnqifpkt glliivlgti amegdsasee eiweelgvmg vydgrehtvy
      241 geprklltqd wvqenyleyr qvpgsnpary eflwgprala etsyvkvleh vvrvnarvri
      301 aypslreaal leeeegv
//
LOCUS       NP_001341829            2802 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform g [Homo sapiens].
ACCESSION   NP_001341829
VERSION     NP_001341829.1
DBSOURCE    REFSEQ: accession NM_001354900.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2802)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2802)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2802)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2802)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2802)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2802)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2802)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2802)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2802)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2802)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2347607.1,
                                           SRR14038192.3458524.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2802
                     /product="adenomatous polyposis coli protein isoform g"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=306683
     Region          68..148
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          281..333
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          334..407
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          431..467
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          471..512
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          475..512
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          522..554
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(545,549,553,592,596,600,637,641,645)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          562..603
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          608..648
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          612..646
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          650..690
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          654..690
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          691..978
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          995..1094
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1216..>1233
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1242..1327
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1250..1660
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1596..1619
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1621..1674
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1675..1696
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1705..1798
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1832..1906
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1992..2011
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2182..2527
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2629..2802
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2802
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354900.2:84..8492"
                     /note="isoform g is encoded by transcript variant 9"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 massgqidll erlkelnlds snfpgvklrs kmslrsygsr egsvssrsge cspvpmgsfp
       61 rrgfvngsre stgyleelek ersllladld keekekdwyy aqlqnltkri dslpltenfs
      121 lqtdmtrrql eyearqirva meeqlgtcqd mekraqrria riqqiekdil rirqllqsqa
      181 teaerssqnk hetgshdaer qnegqgvgei nmatsgngqg sttrmdheta svlssssths
      241 aprrltshlg tkvemvysll smlgthdkdd msrtllamss sqdscismrq sgclplliql
      301 lhgndkdsvl lgnsrgskea rarasaalhn iihsqpddkr grreirvlhl leqiraycet
      361 cwewqeahep gmdqdknpmp apvehqicpa vcvlmklsfd eehrhamnel grkatrgiss
      421 qelgqglsgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg dvankatlcs
      481 mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka lmecalevkk
      541 estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai iesgggilrn
      601 vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn pkdqealwdm
      661 gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps lhvrkqkale
      721 aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs dnfntgnmtv
      781 lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg tsskrglqis
      841 ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth sntynftkse
      901 nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde skfcsygqyp
      961 adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar pkhiiedeik
     1021 qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse tnrvgsnhgi
     1081 nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr hvdqpidysl
     1141 kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql hpssaqsrsg
     1201 qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq ttqeadsant
     1261 lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka vefssgaksp
     1321 sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs gmvsgiisps
     1381 dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa vnaavqrvqv
     1441 lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen dngneteseq
     1501 pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka kkpaqtaskl
     1561 pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf statslsdlt
     1621 iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip elddnkaeeg
     1681 dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk ptspvkpipq
     1741 nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne drvrgsfafd
     1801 sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese akvtshtelt
     1861 snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl qnfaientpv
     1921 cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks fhvedtpvcf
     1981 srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi lgedltldlk
     2041 diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd sdsilslksg
     2101 islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg kkvykslitg
     2161 kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp plktpasksp
     2221 segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr paqqplsrpi
     2281 qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr qmsqqnltkq
     2341 tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr serpvlvrqs
     2401 tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm slsthssvqa
     2461 ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh skhssslprv
     2521 stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt wrkikenefs
     2581 ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs grsptgntpp
     2641 vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap dqkgteikpg
     2701 qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr kssadstsar
     2761 psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_938051                505 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 8 isoform B [Homo sapiens].
ACCESSION   NP_938051
VERSION     NP_938051.1
DBSOURCE    REFSEQ: accession NM_198309.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Ullah,A., Umair,M., Yousaf,M., Khan,S.A., Nazim-Ud-Din,M., Shah,K.,
            Ahmad,F., Azeem,Z., Ali,G., Alhaddad,B., Rafique,A., Jan,A.,
            Haack,T.B., Strom,T.M., Meitinger,T., Ghous,T. and Ahmad,W.
  TITLE     Sequence variants in four genes underlying Bardet-Biedl syndrome in
            consanguineous families
  JOURNAL   Mol Vis 23, 482-494 (2017)
   PUBMED   28761321
  REMARK    GeneRIF: Two novel mutations and three previously reported
            variants, identified in the present study, further extend the body
            of evidence implicating BBS6, BBS7, BBS8, and BBS10 in causing
            Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
  REMARK    GeneRIF: A homozygous null BBS8 mutation leads to Bardet-Biedl
            syndrome with randomization of left-right body axis symmetry, a
            known defect of the nodal cilium
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX247959.1, AY366523.1 and
            BU738965.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is involved in the formation of cilia. A
            mutation in this gene has also been implicated in nonsyndromic
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' coding region, compared to variant 1. The encoded isoform (B) is
            shorter, compared to isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.230374.1, SRR1660809.231616.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..505
                     /product="tetratricopeptide repeat protein 8 isoform B"
                     /note="Bardet-Biedl syndrome type 8; TPR repeat protein 8"
                     /calculated_mol_wt=57153
     Region          30..169
                     /region_name="TTC8_N"
                     /note="N-terminal domain of tetratricopeptide repeat
                     domain 8; cd21341"
                     /db_xref="CDD:411061"
     Site            order(220,223..224,226,249,252..253,256..257,259..260,283,
                     286..287,290..291,294)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          220..243
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          222..501
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          247..277
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          282..310
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          316..344
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(351,354..355,358..359,361,388,391..392,395..396,
                     398..399,422,425..426,429..430,433)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          351..378
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          383..416
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          421..447
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          455..480
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..505
                     /gene="TTC8"
                     /gene_synonym="BBS8; RP51"
                     /coded_by="NM_198309.3:197..1714"
                     /note="isoform B is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9885.1"
                     /db_xref="GeneID:123016"
                     /db_xref="HGNC:HGNC:20087"
                     /db_xref="MIM:608132"
ORIGIN      
        1 mssemeplll awsyfrrrkf qlcadlctqm lekspydqaa wilkaralte mvyideidvd
       61 qegiaemmld enaiaqvprp gtslklpgtn qtggpsqavr pitqagrpit gflrpstqsg
      121 rpgtmeqair tprtaytarp itsssgrfvr lgtasmltsp dgpfinlsrl nltkysqkpk
      181 lakalfeyif hhendvktal dlaalstehs qykdwwwkvq igkcyyrlgm yreaekqfks
      241 alkqqemvdt flylakvyvs ldqpvtalnl fkqgldkfpg evtllcgiar iyeemnnmss
      301 aaeyykevlk qdnthveaia cigsnhfysd qpeialrfyr rllqmgiyng qlfnnlglcc
      361 fyaqqydmtl tsferalsla eneeeaadvw ynlghvavgi gdtnlahqcf rlalvnnnnh
      421 aeaynnlavl emrkghveqa rallqtassl aphmyephfn fatisdkigd lqrsyvaaqk
      481 seaafpdhvd tqhlikqlrq hfaml
//
LOCUS       NP_001335146             647 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform d [Homo sapiens].
ACCESSION   NP_001335146 XP_005266801
VERSION     NP_001335146.1
DBSOURCE    REFSEQ: accession NM_001348217.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP293388.1, AK301144.1,
            AK299169.1 and AC091103.4.
            
            On Feb 8, 2017 this sequence version replaced XP_005266801.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (23) differs in the 5' UTR, lacks
            a portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 3. The resulting
            isoform (d) is shorter at the N-terminus compared to isoform c.
            Variants 4, 23 and 24 all encode the same isoform (d).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.142019.1,
                                           SRR1660805.109801.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..647
                     /product="transcription factor 4 isoform d"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68967
     Region          538..622
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(546,550,552..554,556,561,582..583)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(559..560,563..564,566..567,570,574,584,587,591,594,
                     597..602)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..647
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348217.1:310..2253"
                     /note="isoform d is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS58629.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsagtavwsr nggqassspn yegplhslqs
      361 riedrlerld daihvlrnha vgpstampgg hgdmhgiigp shngamgglg sgygtgllsa
      421 nrhslmvgth redgvalrgs hsllpnqvpv pqlpvqsats pdlnppqdpy rgmppglqgq
      481 svssgsseik sddegdenlq dtkssedkkl dddkkdiksi trsrssnndd edltpeqkae
      541 rekerrmann arerlrvrdi neafkelgrm vqlhlksdkp qtkllilhqa vavilsleqq
      601 vrernlnpka aclkrreeek vsseppplsl agphpgmgda snhmgqm
//
LOCUS       NP_001310337             263 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome inhibitor PI31 subunit isoform 4 [Homo sapiens].
ACCESSION   NP_001310337
VERSION     NP_001310337.1
DBSOURCE    REFSEQ: accession NM_001323408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Yang,S., Tang,D., Zhao,Y.C., Liu,H., Luo,S., Stinchcombe,T.E.,
            Glass,C., Su,L., Shen,S., Christiani,D.C., Wang,Q. and Wei,Q.
  TITLE     Potentially functional variants of ERAP1, PSMF1 and NCF2 in the
            MHC-I-related pathway predict non-small cell lung cancer survival
  JOURNAL   Cancer Immunol Immunother 70 (10), 2819-2833 (2021)
   PUBMED   33651148
  REMARK    GeneRIF: Potentially functional variants of ERAP1, PSMF1 and NCF2
            in the MHC-I-related pathway predict non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 263)
  AUTHORS   McCutchen-Maloney,S.L., Matsuda,K., Shimbara,N., Binns,D.D.,
            Tanaka,K., Slaughter,C.A. and DeMartino,G.N.
  TITLE     cDNA cloning, expression, and functional characterization of PI31,
            a proline-rich inhibitor of the proteasome
  JOURNAL   J Biol Chem 275 (24), 18557-18565 (2000)
   PUBMED   10764772
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Tanahashi,N., Kawahara,H., Murakami,Y. and Tanaka,K.
  TITLE     The proteasome-dependent proteolytic system
  JOURNAL   Mol Biol Rep 26 (1-2), 3-9 (1999)
   PUBMED   10363639
  REMARK    Review article
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC398668.1, AL031665.19 and
            AA699495.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            protein that inhibits the activation of the proteasome by the 11S
            and 19S regulators. Alternative transcript variants have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.238746.1,
                                           SRR1803617.90327.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..263
                     /product="proteasome inhibitor PI31 subunit isoform 4"
                     /note="proteasome inhibitor PI31 subunit; proteasome
                     (prosome, macropain) inhibitor subunit 1 (PI31)"
                     /calculated_mol_wt=28826
     Region          2..150
                     /region_name="Important for homodimerization and
                     interaction with FBXO7.
                     /evidence=ECO:0000269|PubMed:18495667"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          11..148
                     /region_name="PI31_Prot_N"
                     /note="PI31 proteasome regulator N-terminal; pfam11566"
                     /db_xref="CDD:463296"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          182..248
                     /region_name="PI31_Prot_C"
                     /note="PI31 proteasome regulator; pfam08577"
                     /db_xref="CDD:430086"
     Site            205
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            219
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            231
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     CDS             1..263
                     /gene="PSMF1"
                     /gene_synonym="PI31"
                     /coded_by="NM_001323408.2:173..964"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82589.1"
                     /db_xref="GeneID:9491"
                     /db_xref="HGNC:HGNC:9571"
                     /db_xref="MIM:617858"
ORIGIN      
        1 maglevlfas aapaitcrqd alvcflhwev vthgyfglgv gdqpgpndkk sellpagwnn
       61 nkdlyvlrye ykdgsrkllv kaitvessmi lnvleygsqq vadltlnldd yidaehlgdf
      121 hrtyknseel rsrivsgiit piheqwekan vssphrefpp atarevdplr ipphhphtsr
      181 qppwcdplgp fvvggedldp fgprrggmiv dplrsgfpra lidpssglpn rlppgavppg
      241 arfdpfgpig tsppgprpdr rgq
//
LOCUS       NP_078921                229 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger matrin-type protein 4 isoform a [Homo sapiens].
ACCESSION   NP_078921
VERSION     NP_078921.1
DBSOURCE    REFSEQ: accession NM_024645.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Cheong,K.X., Yong,R.Y.Y., Tan,M.M.H., Tey,F.L.K. and Ang,B.C.H.
  TITLE     Association of VIPR2 and ZMAT4 with high myopia
  JOURNAL   Ophthalmic Genet 41 (1), 41-48 (2020)
   PUBMED   32166996
  REMARK    GeneRIF: Association of VIPR2 and ZMAT4 with high myopia.
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Verhoeven,V.J., Hysi,P.G., Wojciechowski,R., Fan,Q.,
            Guggenheim,J.A., Hohn,R., MacGregor,S., Hewitt,A.W., Nag,A.,
            Cheng,C.Y., Yonova-Doing,E., Zhou,X., Ikram,M.K., Buitendijk,G.H.,
            McMahon,G., Kemp,J.P., Pourcain,B.S., Simpson,C.L., Makela,K.M.,
            Lehtimaki,T., Kahonen,M., Paterson,A.D., Hosseini,S.M., Wong,H.S.,
            Xu,L., Jonas,J.B., Parssinen,O., Wedenoja,J., Yip,S.P., Ho,D.W.,
            Pang,C.P., Chen,L.J., Burdon,K.P., Craig,J.E., Klein,B.E.,
            Klein,R., Haller,T., Metspalu,A., Khor,C.C., Tai,E.S., Aung,T.,
            Vithana,E., Tay,W.T., Barathi,V.A., Chen,P., Li,R., Liao,J.,
            Zheng,Y., Ong,R.T., Doring,A., Evans,D.M., Timpson,N.J.,
            Verkerk,A.J., Meitinger,T., Raitakari,O., Hawthorne,F.,
            Spector,T.D., Karssen,L.C., Pirastu,M., Murgia,F., Ang,W.,
            Mishra,A., Montgomery,G.W., Pennell,C.E., Cumberland,P.M.,
            Cotlarciuc,I., Mitchell,P., Wang,J.J., Schache,M.,
            Janmahasatian,S., Igo,R.P. Jr., Lass,J.H., Chew,E., Iyengar,S.K.,
            Gorgels,T.G., Rudan,I., Hayward,C., Wright,A.F., Polasek,O.,
            Vatavuk,Z., Wilson,J.F., Fleck,B., Zeller,T., Mirshahi,A.,
            Muller,C., Uitterlinden,A.G., Rivadeneira,F., Vingerling,J.R.,
            Hofman,A., Oostra,B.A., Amin,N., Bergen,A.A., Teo,Y.Y., Rahi,J.S.,
            Vitart,V., Williams,C., Baird,P.N., Wong,T.Y., Oexle,K.,
            Pfeiffer,N., Mackey,D.A., Young,T.L., van Duijn,C.M., Saw,S.M.,
            Bailey-Wilson,J.E., Stambolian,D., Klaver,C.C. and Hammond,C.J.
  CONSRTM   Consortium for Refractive Error and Myopia (CREAM); Diabetes
            Control and Complications Trial/Epidemiology of Diabetes
            Interventions and Complications (DCCT/EDIC) Research Group;
            Wellcome Trust Case Control Consortium 2 (WTCCC2); Fuchs' Genetics
            Multi-Center Study Group
  TITLE     Genome-wide meta-analyses of multiancestry cohorts identify
            multiple new susceptibility loci for refractive error and myopia
  JOURNAL   Nat Genet 45 (3), 314-318 (2013)
   PUBMED   23396134
  REMARK    Erratum:[Nat Genet. 2013 Jun;45(2):712. Janmahasathian, Sarayut
            [corrected to Sarayut Janmahasatian]]
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Wan,J., Gao,Y., Zhao,X., Wu,Q., Fu,X., Shao,Y., Yang,H., Guan,M.,
            Yu,B. and Zhang,W.
  TITLE     The association between the copy-number variations of ZMAT4 and
            hematological malignancy
  JOURNAL   Hematology 16 (1), 20-23 (2011)
   PUBMED   21269563
  REMARK    GeneRIF: Examines the expression of ZMAT4 mRNA in the samples with
            1 or 2 copies of DNA, and observed a weak yet positive correlation
            between the relative expression level and gene dosage.
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Meigs,J.B., Manning,A.K., Fox,C.S., Florez,J.C., Liu,C.,
            Cupples,L.A. and Dupuis,J.
  TITLE     Genome-wide association with diabetes-related traits in the
            Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S16 (2007)
   PUBMED   17903298
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC048387.16, AK023904.1 and BC019598.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.202190.1, AK023904.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297737.11/ ENSP00000297737.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..229
                     /product="zinc finger matrin-type protein 4 isoform a"
                     /note="zinc finger matrin-type protein 4"
                     /calculated_mol_wt=25702
     Region          15..38
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          16..38
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(23..25,27..28,32,37,82,85..89,91..92)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          72..106
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          77..99
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          116..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H898.1)"
     Region          142..176
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          147..169
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(154..156,158..159,163,168,205,208..212,214..215)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          198..222
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          200..222
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..229
                     /gene="ZMAT4"
                     /coded_by="NM_024645.3:149..838"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34885.1"
                     /db_xref="GeneID:79698"
                     /db_xref="HGNC:HGNC:25844"
ORIGIN      
        1 mkssdidqdl ftdsyckvcs aqlisesqrv ahyesrkhas kvrlyymlhp rdggcpakrl
       61 rsengsdadm vdknkcctlc nmsftsavva dshyqgkiha krlklllgek tplkttatpl
      121 splkpprmdt apvvaspyqr rdsdrycglc aawfnnplma qqhydgkkhk knaarvalle
      181 qlgttldmge lrglrrnyrc ticsvslnsi eqyhahlkgs khqtnlknk
//
LOCUS       NP_871618                147 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D3 isoform 1 [Homo sapiens].
ACCESSION   NP_871618
VERSION     NP_871618.1
DBSOURCE    REFSEQ: accession NM_181889.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Yalcin,Z., Koot,D., Bezstarosti,K., Salas-Lloret,D.,
            Bleijerveld,O.B., Boersma,V., Falcone,M., Gonzalez-Prieto,R.,
            Altelaar,M., Demmers,J.A.A. and Jacobs,J.J.L.
  TITLE     Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control
  JOURNAL   Mol Cell Proteomics 22 (6), 100548 (2023)
   PUBMED   37059365
  REMARK    GeneRIF: Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control.
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jiang,C., Dai,X., He,S., Zhou,H., Fang,L., Guo,J., Liu,S.,
            Zhang,T., Pan,W., Yu,H., Fu,T., Li,D., Inuzuka,H., Wang,P., Xiao,J.
            and Wei,W.
  TITLE     Ring domains are essential for GATOR2-dependent mTORC1 activation
  JOURNAL   Mol Cell 83 (1), 74-89 (2023)
   PUBMED   36528027
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Ray,P., Nancarrow,D.J., Ferrer-Torres,D., Wang,Z., San Martinho,M.,
            Hinton,T., Wu,J.H., Wu,A., Turgeon,D.K., Hammer,M.A., Dame,M.K.,
            Lawrence,T.S., O'Brien,P.J., Spence,J.R., Beer,D.G. and Ray,D.
  TITLE     UBCH5 Family Members Differentially Impact Stabilization of Mutant
            p53 via RNF128 Iso1 During Barrett's Progression to Esophageal
            Adenocarcinoma
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (1), 129-149 (2022)
   PUBMED   34416429
  REMARK    GeneRIF: UBCH5 Family Members Differentially Impact Stabilization
            of Mutant p53 via RNF128 Iso1 During Barrett's Progression to
            Esophageal Adenocarcinoma.
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Rogakou,E.P., Pilch,D.R., Orr,A.H., Ivanova,V.S. and Bonner,W.M.
  TITLE     DNA double-stranded breaks induce histone H2AX phosphorylation on
            serine 139
  JOURNAL   J Biol Chem 273 (10), 5858-5868 (1998)
   PUBMED   9488723
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Jensen,J.P., Bates,P.W., Yang,M., Vierstra,R.D. and Weissman,A.M.
  TITLE     Identification of a family of closely related human ubiquitin
            conjugating enzymes
  JOURNAL   J Biol Chem 270 (51), 30408-30414 (1995)
   PUBMED   8530467
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Scheffner,M., Huibregtse,J.M. and Howley,P.M.
  TITLE     Identification of a human ubiquitin-conjugating enzyme that
            mediates the E6-AP-dependent ubiquitination of p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 8797-8801 (1994)
   PUBMED   8090726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY035067.1, AK315775.1,
            BC003395.1, AC018797.4 and BM967209.1.
            
            Summary: The modification of proteins with ubiquitin is an
            important cellular mechanism for targeting abnormal or short-lived
            proteins for degradation. Ubiquitination involves at least three
            classes of enzymes: ubiquitin-activating enzymes, or E1s,
            ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein
            ligases, or E3s. This gene encodes a member of the E2
            ubiquitin-conjugating enzyme family. This enzyme functions in the
            ubiquitination of the tumor-suppressor protein p53, which is
            induced by an E3 ubiquitin-protein ligase. [provided by RefSeq, Jan
            2017].
            
            Transcript Variant: This variant (5) has an alternate 5' UTR exon,
            and encodes the same isoform (1), as compared to variant 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.207746.1,
                                           SRR1803617.129054.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D3 isoform 1"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog,
                     yeast); ubiquitin-conjugating enzyme E2-17 kDa 3;
                     ubiquitin-protein ligase D3; ubiquitin carrier protein D3;
                     ubiquitin-conjugating enzyme E2(17)KB 3; ubiquitin
                     conjugating enzyme E2D 3; E2 ubiquitin-conjugating enzyme
                     D3; (E3-independent) E2 ubiquitin-conjugating enzyme D3;
                     ubiquitin-conjugating enzyme E2D 3 (homologous to yeast
                     UBC4/5)"
                     /calculated_mol_wt=16556
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="UBE2D3"
                     /gene_synonym="E2(17)KB3; UBC4/5; UBCH5C"
                     /coded_by="NM_181889.2:366..809"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3660.1"
                     /db_xref="GeneID:7323"
                     /db_xref="HGNC:HGNC:12476"
                     /db_xref="MIM:602963"
ORIGIN      
        1 malkrinkel sdlardppaq csagpvgddm fhwqatimgp ndspyqggvf fltihfptdy
       61 pfkppkvaft triyhpnins ngsicldilr sqwspaltis kvllsicsll cdpnpddplv
      121 peiariyktd rdkynrisre wtqkyam
//
LOCUS       NP_443163                331 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 6 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_443163
VERSION     NP_443163.1
DBSOURCE    REFSEQ: accession NM_052931.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Oba,T., Long,M.D., Ito,K.I. and Ito,F.
  TITLE     Clinical and immunological relevance of SLAMF6 expression in the
            tumor microenvironment of breast cancer and melanoma
  JOURNAL   Sci Rep 14 (1), 2394 (2024)
   PUBMED   38287061
  REMARK    GeneRIF: Clinical and immunological relevance of SLAMF6 expression
            in the tumor microenvironment of breast cancer and melanoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Xia,G., Li,Y., Pan,W., Qian,C., Ma,L., Zhou,J., Xu,H. and Cheng,C.
  TITLE     SLAMF6 is associated with the susceptibility and severity of
            rheumatoid arthritis in the Chinese population
  JOURNAL   J Orthop Surg Res 17 (1), 13 (2022)
   PUBMED   35016729
  REMARK    GeneRIF: SLAMF6 is associated with the susceptibility and severity
            of rheumatoid arthritis in the Chinese population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Liu,B., Zeng,L., Shao,Y. and Fu,R.
  TITLE     Expression and function of SLAMF6 in CD8+ T lymphocytes of patients
            with severe aplastic anemia
  JOURNAL   Cell Immunol 364, 104343 (2021)
   PUBMED   33774556
  REMARK    GeneRIF: Expression and function of SLAMF6 in CD8(+) T lymphocytes
            of patients with severe aplastic anemia.
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Fraser,C.C., Howie,D., Morra,M., Qiu,Y., Murphy,C., Shen,Q.,
            Gutierrez-Ramos,J.C., Coyle,A., Kingsbury,G.A. and Terhorst,C.
  TITLE     Identification and characterization of SF2000 and SF2001, two new
            members of the immune receptor SLAM/CD2 family
  JOURNAL   Immunogenetics 53 (10-11), 843-850 (2002)
   PUBMED   11862385
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Bottino,C., Falco,M., Parolini,S., Marcenaro,E., Augugliaro,R.,
            Sivori,S., Landi,E., Biassoni,R., Notarangelo,L.D., Moretta,L. and
            Moretta,A.
  TITLE     NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface
            molecule contributing to the inability of natural killer cells to
            kill Epstein-Barr virus-infected B cells in X-linked
            lymphoproliferative disease
  JOURNAL   J Exp Med 194 (3), 235-246 (2001)
   PUBMED   11489943
  REMARK    Erratum:[J Exp Med 2001 Sep 3;194(5):following 703]
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Lee,Y.J., Luisiri,P. and Clark,M.R.
  TITLE     A novel complex, p40/42, is constitutively associated with the B
            cell antigen receptor and phosphorylated upon receptor stimulation
  JOURNAL   J Immunol 157 (9), 3828-3837 (1996)
   PUBMED   8892612
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Kong,G., Dalton,M., Bubeck Wardenburg,J., Straus,D., Kurosaki,T.
            and Chan,A.C.
  TITLE     Distinct tyrosine phosphorylation sites in ZAP-70 mediate
            activation and negative regulation of antigen receptor function
  JOURNAL   Mol Cell Biol 16 (9), 5026-5035 (1996)
   PUBMED   8756661
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Hercend,T., Meuer,S., Brennan,A., Edson,M.A., Acuto,O.,
            Reinherz,E.L., Schlossman,S.F. and Ritz,J.
  TITLE     Natural killer-like function of activated T lymphocytes:
            differential blocking effects of monoclonal antibodies specific for
            a 90-kDa clonotypic structure
  JOURNAL   Cell Immunol 86 (2), 381-392 (1984)
   PUBMED   6610481
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB197632.1, BC113893.1 and
            AK125624.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein, belonging to the CD2 subfamily of the immunoglobulin
            superfamily. This encoded protein is expressed on Natural killer
            (NK), T, and B lymphocytes. It undergoes tyrosine phosphorylation
            and associates with the Src homology 2 domain-containing protein
            (SH2D1A) as well as with SH2 domain-containing phosphatases (SHPs).
            It functions as a coreceptor in the process of NK cell activation.
            It can also mediate inhibitory signals in NK cells from X-linked
            lymphoproliferative patients. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms.[provided
            by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, compared to variant 1, which results in an
            isoform (2) that is one amino acid shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK125624.1, AJ277141.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2-q23.3"
     Protein         1..331
                     /product="SLAM family member 6 isoform 2 precursor"
                     /note="activating NK receptor; natural killer-, T- and
                     B-cell antigen; NTBA receptor; NK-T-B-antigen"
                     /calculated_mol_wt=34888
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2405
     mat_peptide     22..331
                     /product="SLAM family member 6 isoform 2"
                     /calculated_mol_wt=34888
     Region          29..126
                     /region_name="Ig_SLAM-like_N"
                     /note="N-terminal immunoglobulin (Ig)-like domain of the
                     signaling lymphocyte activation molecule (SLAM) family;
                     cd16842"
                     /db_xref="CDD:409517"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409517"
     Region          36..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409517"
     Site            order(52,54,108,110,112)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409517"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          61..66
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409517"
     Region          73..78
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409517"
     Region          85..90
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409517"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          92..97
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409517"
     Region          105..112
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409517"
     Region          117..126
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409517"
     Site            137
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          <149..207
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          149..153
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          163..167
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          188..191
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..197
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DU3.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          282..287
                     /region_name="ITSM 1.
                     /evidence=ECO:0000250|UniProtKB:Q13291"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DU3.3)"
     Region          306..311
                     /region_name="ITSM 2.
                     /evidence=ECO:0000250|UniProtKB:Q13291"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DU3.3)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96DU3.3)"
     CDS             1..331
                     /gene="SLAMF6"
                     /gene_synonym="CD352; KALI; KALIb; Ly108; NTB-A; NTBA;
                     SF2000"
                     /coded_by="NM_052931.5:64..1059"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS1205.1"
                     /db_xref="GeneID:114836"
                     /db_xref="HGNC:HGNC:21392"
                     /db_xref="MIM:606446"
ORIGIN      
        1 mlwlfqsllf vfcfgpgnvv sqssltplmv ngilgesvtl plefpagekv nfitwlfnet
       61 slafivphet kspeihvtnp kqgkrlnftq syslqlsnlk medtgsyraq istktsakls
      121 sytlrilrql rniqvtnhsq lfqnmtcelh ltcsvedadd nvsfrwealg ntlssqpnlt
      181 vswdprisse qdytciaena vsnlsfsvsa qklcedvkiq ytdtkmilfm vsgicivfgf
      241 iillllvlrk rrdslslstq rtqgpesarn leyvsvsptn ntvyasvths nreteiwtpr
      301 endtitiyst inhskeskpt fsrataldnv v
//
LOCUS       NP_077007                342 aa            linear   PRI 20-NOV-2025
DEFINITION  methylosome protein WDR77 isoform 2 [Homo sapiens].
ACCESSION   NP_077007
VERSION     NP_077007.1
DBSOURCE    REFSEQ: accession NM_024102.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Xu,W., Huang,Z., Xiao,Y., Li,W., Xu,M., Zhao,Q. and Yi,P.
  TITLE     HNRNPC promotes estrogen receptor-positive breast cancer cell cycle
            by stabilizing WDR77 mRNA in an m6A-dependent manner
  JOURNAL   Mol Carcinog 63 (5), 859-873 (2024)
   PUBMED   38353359
  REMARK    GeneRIF: HNRNPC promotes estrogen receptor-positive breast cancer
            cell cycle by stabilizing WDR77 mRNA in an m6A-dependent manner.
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Ichikawa,T., Suekane,A., Nakahata,S., Iha,H., Shimoda,K.,
            Murakami,T. and Morishita,K.
  TITLE     Inhibition of PRMT5/MEP50 Arginine Methyltransferase Activity
            Causes Cancer Vulnerability in NDRG2low Adult T-Cell
            Leukemia/Lymphoma
  JOURNAL   Int J Mol Sci 25 (5), 2842 (2024)
   PUBMED   38474089
  REMARK    GeneRIF: Inhibition of PRMT5/MEP50 Arginine Methyltransferase
            Activity Causes Cancer Vulnerability in NDRG2[low] Adult T-Cell
            Leukemia/Lymphoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Mulvaney,K.M., Blomquist,C., Acharya,N., Li,R., Ranaghan,M.J.,
            O'Keefe,M., Rodriguez,D.J., Young,M.J., Kesar,D., Pal,D.,
            Stokes,M., Nelson,A.J., Jain,S.S., Yang,A., Mullin-Bernstein,Z.,
            Columbus,J., Bozal,F.K., Skepner,A., Raymond,D., LaRussa,S.,
            McKinney,D.C., Freyzon,Y., Baidi,Y., Porter,D., Aguirre,A.J.,
            Ianari,A., McMillan,B. and Sellers,W.R.
  TITLE     Molecular basis for substrate recruitment to the PRMT5 methylosome
  JOURNAL   Mol Cell 81 (17), 3481-3495 (2021)
   PUBMED   34358446
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Zhao,Y., Yu,T., Sun,J., Wang,F., Cheng,C., He,S., Chen,L., Xie,D.,
            Fu,L., Guan,X., Yan,A., Li,Y., Miao,G. and Zhu,X.
  TITLE     Germ-line mutations in WDR77 predispose to familial papillary
            thyroid cancer
  JOURNAL   Proc Natl Acad Sci U S A 118 (31) (2021)
   PUBMED   34326253
  REMARK    GeneRIF: Germ-line mutations in WDR77 predispose to familial
            papillary thyroid cancer.
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Yuan,H., Zhao,L., Yuan,Y., Yun,H., Zheng,W., Geng,Y., Yang,G.,
            Wang,Y., Zhao,M. and Zhang,X.
  TITLE     HBx represses WDR77 to enhance HBV replication by DDB1-mediated
            WDR77 degradation in the liver
  JOURNAL   Theranostics 11 (17), 8362-8378 (2021)
   PUBMED   34373747
  REMARK    GeneRIF: HBx represses WDR77 to enhance HBV replication by
            DDB1-mediated WDR77 degradation in the liver.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Yong,J., Wan,L. and Dreyfuss,G.
  TITLE     Why do cells need an assembly machine for RNA-protein complexes?
  JOURNAL   Trends Cell Biol 14 (5), 226-232 (2004)
   PUBMED   15130578
  REMARK    Review article
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Hosohata,K., Li,P., Hosohata,Y., Qin,J., Roeder,R.G. and Wang,Z.
  TITLE     Purification and identification of a novel complex which is
            involved in androgen receptor-dependent transcription
  JOURNAL   Mol Cell Biol 23 (19), 7019-7029 (2003)
   PUBMED   12972618
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Licciardo,P., Amente,S., Ruggiero,L., Monti,M., Pucci,P., Lania,L.
            and Majello,B.
  TITLE     The FCP1 phosphatase interacts with RNA polymerase II and with
            MEP50 a component of the methylosome complex involved in the
            assembly of snRNP
  JOURNAL   Nucleic Acids Res 31 (3), 999-1005 (2003)
   PUBMED   12560496
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Friesen,W.J., Wyce,A., Paushkin,S., Abel,L., Rappsilber,J., Mann,M.
            and Dreyfuss,G.
  TITLE     A novel WD repeat protein component of the methylosome binds Sm
            proteins
  JOURNAL   J Biol Chem 277 (10), 8243-8247 (2002)
   PUBMED   11756452
  REMARK    GeneRIF: Here, we describe a novel component of the methylosome, a
            50-kilodalton WD repeat protein termed methylosome protein 50
            (MEP50).
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB105102.1 and BC016946.1.
            
            Summary: The protein encoded by this gene is an androgen receptor
            coactivator that forms a complex with protein arginine
            methyltransferase 5, which modifies specific arginines to
            dimethylarginines in several spliceosomal Sm proteins. The encoded
            protein may be involved in the early stages of prostate cancer,
            with most of the protein being nuclear-localized in benign cells
            but cytoplasmic in cancer cells. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction in the 3' end compared to variant 1. The resulting
            isoform (2) has the same N- and C-termini but is shorter compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016946.1, SRR3476690.507710.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000235090.10/ ENSP00000235090.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..342
                     /product="methylosome protein WDR77 isoform 2"
                     /note="methylosome protein 50; androgen receptor cofactor
                     p44; WD repeat-containing protein 77; testis tissue
                     sperm-binding protein Li 44a; methylosome protein WDR77"
                     /calculated_mol_wt=36593
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          22..75
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          78..116
                     /region_name="WD 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          <94..322
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          123..162
                     /region_name="WD 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          128..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..205
                     /region_name="WD 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..250
                     /region_name="WD 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          214..252
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          253..293
                     /region_name="WD 6.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          258..294
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          295..330
                     /region_name="WD 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     CDS             1..342
                     /gene="WDR77"
                     /gene_synonym="HKMT1069; MEP-50; MEP50; Nbla10071; p44;
                     p44/Mep50"
                     /coded_by="NM_024102.4:88..1116"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS835.1"
                     /db_xref="GeneID:79084"
                     /db_xref="HGNC:HGNC:29652"
                     /db_xref="MIM:611734"
ORIGIN      
        1 mrketppplv ppaarewnlp pnapacmerq leaaryrsdg alllgassls grcwagslwl
       61 fkdpcaapne gfcsagvqte agvadltwvg ergilvasds gavelwelde netlivskfc
      121 kyehddivst vsvlssgtqa vsgskdicik vwdlaqqvvl ssyrahaaqv tcvaasphkd
      181 svflscsedn rillwdtrcp kpasqigcsa pgylptslaw hpqqsevfvf gdengtvslv
      241 dtkstscvls savhsqcvtg lvfsphsvpf laslsedcsl avldsslsel frsqahrdfv
      301 rdatwsplnh sllttvgwdh qvvhhvvpte plpapgpasv te
//
LOCUS       NP_001288070             156 aa            linear   PRI 20-NOV-2025
DEFINITION  iron-sulfur cluster assembly enzyme ISCU isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001288070 XP_005268817
VERSION     NP_001288070.1
DBSOURCE    REFSEQ: accession NM_001301141.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Crooks,D.R., Jeong,S.Y., Tong,W.H., Ghosh,M.C., Olivierre,H.,
            Haller,R.G. and Rouault,T.A.
  TITLE     Tissue specificity of a human mitochondrial disease:
            differentiation-enhanced mis-splicing of the Fe-S scaffold gene
            ISCU renders patient cells more sensitive to oxidative stress in
            ISCU myopathy
  JOURNAL   J Biol Chem 287 (48), 40119-40130 (2012)
   PUBMED   23035118
  REMARK    GeneRIF: ISCU protein deficiency in patients results from
            muscle-specific mis-splicing and oxidative stress.
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Nordin,A., Larsson,E., Thornell,L.E. and Holmberg,M.
  TITLE     Tissue-specific splicing of ISCU results in a skeletal muscle
            phenotype in myopathy with lactic acidosis, while complete loss of
            ISCU results in early embryonic death in mice
  JOURNAL   Hum Genet 129 (4), 371-378 (2011)
   PUBMED   21165651
  REMARK    GeneRIF: Data show that the highest level of incorrectly spliced
            ISCU mRNA was found in skeletal muscle.
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Sanaker,P.S., Toompuu,M., Hogan,V.E., He,L., Tzoulis,C.,
            Chrzanowska-Lightowlers,Z.M., Taylor,R.W. and Bindoff,L.A.
  TITLE     Differences in RNA processing underlie the tissue specific
            phenotype of ISCU myopathy
  JOURNAL   Biochim Biophys Acta 1802 (6), 539-544 (2010)
   PUBMED   20206689
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Olsson,A., Lind,L., Thornell,L.E. and Holmberg,M.
  TITLE     Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11
            and caused by an intron mutation in the ISCU gene resulting in a
            splicing defect
  JOURNAL   Hum Mol Genet 17 (11), 1666-1672 (2008)
   PUBMED   18296749
  REMARK    GeneRIF: Intron mutation in the ISCU gene, leading to incorrectly
            spliced mRNA, is the cause of myopathy with lactic acidosis in this
            family.
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Mochel,F., Knight,M.A., Tong,W.H., Hernandez,D., Ayyad,K.,
            Taivassalo,T., Andersen,P.M., Singleton,A., Rouault,T.A.,
            Fischbeck,K.H. and Haller,R.G.
  TITLE     Splice mutation in the iron-sulfur cluster scaffold protein ISCU
            causes myopathy with exercise intolerance
  JOURNAL   Am J Hum Genet 82 (3), 652-660 (2008)
   PUBMED   18304497
  REMARK    GeneRIF: Gene ISCU was identified as a candidate within a region of
            shared homozygosity among patients with myopathy with severe
            exercise intolerance and myoglobinuria.
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Tong,W.H. and Rouault,T.
  TITLE     Distinct iron-sulfur cluster assembly complexes exist in the
            cytosol and mitochondria of human cells
  JOURNAL   EMBO J 19 (21), 5692-5700 (2000)
   PUBMED   11060020
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Hwang,D.M., Dempsey,A., Tan,K.T. and Liew,C.C.
  TITLE     A modular domain of NifU, a nitrogen fixation cluster protein, is
            highly conserved in evolution
  JOURNAL   J Mol Evol 43 (5), 536-540 (1996)
   PUBMED   8875867
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Mochel,F. and Haller,R.G.
  TITLE     Myopathy with Deficiency of ISCU - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301757
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK057251.1, AC008119.6 and
            BQ020993.1.
            
            On Jul 23, 2014 this sequence version replaced XP_005268817.1.
            
            Summary: This gene encodes a component of the iron-sulfur (Fe-S)
            cluster scaffold. Fe-S clusters are cofactors that play a role in
            the function of a diverse set of enzymes, including those that
            regulate metabolism, iron homeostasis, and oxidative stress
            response. Alternative splicing results in transcript variants
            encoding different protein isoforms that localize either to the
            cytosol or to the mitochondrion. Mutations in this gene have been
            found in patients with hereditary myopathy with lactic acidosis. A
            disease-associated mutation in an intron may activate a cryptic
            splice site, resulting in the production of a splice variant
            encoding a putatively non-functional protein. A pseudogene of this
            gene is present on chromosome 1. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (4) contains an alternate exon in
            the 3' region, resulting in a different 3' coding region and 3'
            UTR, compared to variant 2. The encoded isoform (4) has a distinct,
            shorter C-terminus, compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057251.1, SRR14038191.450027.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..156
                     /product="iron-sulfur cluster assembly enzyme ISCU isoform
                     4 precursor"
                     /note="iron-sulfur cluster assembly enzyme ISCU,
                     mitochondrial; nifU-like N-terminal domain-containing
                     protein; IscU iron-sulfur cluster scaffold homolog"
                     /calculated_mol_wt=13266
     transit_peptide 1..34
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9H1K1.2)"
                     /calculated_mol_wt=3631
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:23508953; propagated from
                     UniProtKB/Swiss-Prot (Q9H1K1.2)"
     Site            order(34..37,40..41,69..70,95,97,134..135,137..138)
                     /site_type="other"
                     /note="trimerization site [polypeptide binding]"
                     /db_xref="CDD:143480"
     Region          35..139
                     /region_name="IscU_like"
                     /note="Iron-sulfur cluster scaffold-like proteins;
                     cl00528"
                     /db_xref="CDD:444957"
     Site            35
                     /site_type="other"
                     /note="Mediates ISCU dimerization and de novo [2Fe-2S]
                     cluster assembly. /evidence=ECO:0000269|PubMed:34824239;
                     propagated from UniProtKB/Swiss-Prot (Q9H1K1.2)"
     Site            order(69,95,138)
                     /site_type="active"
                     /db_xref="CDD:143480"
     CDS             1..156
                     /gene="ISCU"
                     /gene_synonym="2310020H20Rik; HML; hnifU; ISU2; NIFU;
                     NIFUN"
                     /coded_by="NM_001301141.1:1161..1631"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS73518.1"
                     /db_xref="GeneID:23479"
                     /db_xref="HGNC:HGNC:29882"
                     /db_xref="MIM:611911"
ORIGIN      
        1 maaagafrlr raasalllrs prlparelsa parlyhkkvv dhyenprnvg sldktsknvg
       61 tglvgapacg dvmklqiqvd ekgkivdarf ktfgcgsaia ssslatewvk gktveealti
      121 kntdiakelc lppvklhcsr kegmrnisln asmevy
//
LOCUS       NP_001311315             419 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001311315 XP_005273694
VERSION     NP_001311315.1
DBSOURCE    REFSEQ: accession NM_001324386.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 419)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, DQ153248.1, AC108449.5 and BQ019252.1.
            
            On May 2, 2016 this sequence version replaced XP_005273694.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.4504.1,
                                           SRR1803612.255656.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..419
                     /product="homeobox-containing protein 1 isoform 4"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=47018
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          352..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..419
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324386.2:342..1601"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr aniaailesh gidvqspggh
      361 snsddvdgnd yseqddstsh sdhqdpisla vemaavnhti lalarqgane iktealddd
//
LOCUS       NP_061821                462 aa            linear   PRI 20-NOV-2025
DEFINITION  ERBB receptor feedback inhibitor 1 [Homo sapiens].
ACCESSION   NP_061821
VERSION     NP_061821.1
DBSOURCE    REFSEQ: accession NM_018948.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Wang,H., Liu,H., Lu,G., Tang,X., Luo,S., Du,M., Christiani,D.C. and
            Wei,Q.
  TITLE     Potentially functional variants of ERRFI1 in hypoxia-related genes
            predict survival of non-small cell lung cancer patients
  JOURNAL   Cancer Med 13 (15), e70073 (2024)
   PUBMED   39096122
  REMARK    GeneRIF: Potentially functional variants of ERRFI1 in
            hypoxia-related genes predict survival of non-small cell lung
            cancer patients.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Kondo,N., Utsumi,T., Shimizu,Y., Takemoto,A., Oh-Hara,T.,
            Uchibori,K., Subat-Motoshi,S., Ninomiya,H., Takeuchi,K., Nishio,M.,
            Miyazaki,Y. and Katayama,R.
  TITLE     MIG6 loss confers resistance to ALK/ROS1 inhibitors in NSCLC
            through EGFR activation by low-dose EGF
  JOURNAL   JCI Insight 8 (24), e173688 (2023)
   PUBMED   37917191
  REMARK    GeneRIF: MIG6 loss confers resistance to ALK/ROS1 inhibitors in
            NSCLC through EGFR activation by low-dose EGF.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Jeong,O., Broaddus,R.R., Lessey,B.A., Risinger,J.I., Hunter,M.I.
            and Kim,T.H.
  TITLE     MIG-6 Is Critical for Progesterone Responsiveness in Human Complex
            Atypical Hyperplasia and Early-Stage Endometrial Cancer
  JOURNAL   Int J Mol Sci 23 (23), 14596 (2022)
   PUBMED   36498921
  REMARK    GeneRIF: MIG-6 Is Critical for Progesterone Responsiveness in Human
            Complex Atypical Hyperplasia and Early-Stage Endometrial Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Li,C., Edeni,D., Platkin,S., Liu,R., Li,J., Hossain,M., Rahman,M.,
            Islam,H., Phillips,J.L. and Xu,D.
  TITLE     Effect of Gene 33/Mig6/ERRFI1 on hexavalent chromium-induced
            transformation of human bronchial epithelial cells depends on the
            length of exposure
  JOURNAL   J Environ Sci Health C Toxicol Carcinog 40 (3-4), 227-247 (2022)
   PUBMED   36715065
  REMARK    GeneRIF: Effect of Gene 33/Mig6/ERRFI1 on hexavalent
            chromium-induced transformation of human bronchial epithelial cells
            depends on the length of exposure.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Hackel,P.O., Gishizky,M. and Ullrich,A.
  TITLE     Mig-6 is a negative regulator of the epidermal growth factor
            receptor signal
  JOURNAL   Biol Chem 382 (12), 1649-1662 (2001)
   PUBMED   11843178
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Fiorentino,L., Pertica,C., Fiorini,M., Talora,C., Crescenzi,M.,
            Castellani,L., Alema,S., Benedetti,P. and Segatto,O.
  TITLE     Inhibition of ErbB-2 mitogenic and transforming activity by RALT, a
            mitogen-induced signal transducer which binds to the ErbB-2 kinase
            domain
  JOURNAL   Mol Cell Biol 20 (20), 7735-7750 (2000)
   PUBMED   11003669
  REMARK    GeneRIF: MIG-6/RALT is a transcriptionally controlled inhibitor of
            mitogenic and transforming signals generated by the ErbB-2
            oncogene. MIG-6/RALT forms a physical complex with activated ErbB-2
            and co-localizes with ErbB-2 in living cells.
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Makkinje,A., Quinn,D.A., Chen,A., Cadilla,C.L., Force,T.,
            Bonventre,J.V. and Kyriakis,J.M.
  TITLE     Gene 33/Mig-6, a transcriptionally inducible adapter protein that
            binds GTP-Cdc42 and activates SAPK/JNK. A potential marker
            transcript for chronic pathologic conditions, such as diabetic
            nephropathy. Possible role in the response to persistent stress
  JOURNAL   J Biol Chem 275 (23), 17838-17847 (2000)
   PUBMED   10749885
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Wick,M., Burger,C., Funk,M. and Muller,R.
  TITLE     Identification of a novel mitogen-inducible gene (mig-6):
            regulation during G1 progression and differentiation
  JOURNAL   Exp Cell Res 219 (2), 527-535 (1995)
   PUBMED   7641805
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Chrapkiewicz,N.B., Davis,C.M., Chu,D.T., Caldwell,C.M. and
            Granner,D.K.
  TITLE     Rat gene 33: analysis of its structure, messenger RNA and basal
            promoter activity
  JOURNAL   Nucleic Acids Res 17 (16), 6651-6667 (1989)
   PUBMED   2780291
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB033666.1, AK096149.1, BC025337.1 and AL137274.1.
            
            Summary: ERRFI1 is a cytoplasmic protein whose expression is
            upregulated with cell growth (Wick et al., 1995 [PubMed 7641805]).
            It shares significant homology with the protein product of rat
            gene-33, which is induced during cell stress and mediates cell
            signaling (Makkinje et al., 2000 [PubMed 10749885]; Fiorentino et
            al., 2000 [PubMed 11003669]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.181073.1, AK096149.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151405 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377482.10/ ENSP00000366702.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..462
                     /product="ERBB receptor feedback inhibitor 1"
                     /note="receptor-associated late transducer;
                     mitogen-inducible gene 6 protein"
                     /calculated_mol_wt=50429
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          6..69
                     /region_name="GTPase_binding"
                     /note="GTPase binding; pfam09027"
                     /db_xref="CDD:430374"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          225..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JZ7; propagated from
                     UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          315..367
                     /region_name="Inhibitor_Mig-6"
                     /note="EGFR receptor inhibitor Mig-6; pfam11555"
                     /db_xref="CDD:463294"
     Region          334..363
                     /region_name="Interaction with EGFR and ERBB2 and
                     regulation of EGFR activation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Region          415..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UJM3.1)"
     CDS             1..462
                     /gene="ERRFI1"
                     /gene_synonym="GENE-33; MIG-6; MIG6; RALT"
                     /coded_by="NM_018948.4:226..1614"
                     /db_xref="CCDS:CCDS94.1"
                     /db_xref="GeneID:54206"
                     /db_xref="HGNC:HGNC:18185"
                     /db_xref="MIM:608069"
ORIGIN      
        1 msiagvaaqe irvplktgfl hngramgnmr ktywssrsef knnflnidpi tmayslnssa
       61 qerliplgha sksapmnghc faengpsqks slppllipps enlgpheedq vvcgfkkltv
      121 ngvcastppl tpiknspslf pcaplcergs rplpplpise alslddtdce vefltssdtd
      181 flledstlsd fkydvpgrrs frgcgqinya yfdtpavsaa dlsyvsdqng gvpdpnpppp
      241 qthrrlrrsh sgpagsfnkp airisnccih raspnsdedk pevpprvpip prpvkpdyrr
      301 wsaevtssty sdedrppkvp preplspsns rtpspkslps ylngvmpptq sfapdpkyvs
      361 skalqrqnse gsaskvpcil piiengkkvs sthyyllper ppyldkyekf freaeetngg
      421 aqiqplpadc gissatekpd sktkmdlggh vkrkhlsyvv sp
//
LOCUS       NP_056466                580 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD finger protein 19 isoform a [Homo sapiens].
ACCESSION   NP_056466 XP_045308
VERSION     NP_056466.1
DBSOURCE    REFSEQ: accession NM_015651.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Johnson,T.S., Sudha,P., Liu,E., Becker,N., Robertson,S., Blaney,P.,
            Morgan,G., Chopra,V.S., Dos Santos,C., Nixon,M., Huang,K.,
            Suvannasankha,A., Zaid,M.A., Abonour,R. and Walker,B.A.
  TITLE     1q amplification and PHF19 expressing high-risk cells are
            associated with relapsed/refractory multiple myeloma
  JOURNAL   Nat Commun 15 (1), 4144 (2024)
   PUBMED   38755140
  REMARK    GeneRIF: 1q amplification and PHF19 expressing high-risk cells are
            associated with relapsed/refractory multiple myeloma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Xu,Y., Liu,W., Jiang,X., Li,J., Liu,Q., Su,F., Ruan,S., Zhang,Z.
            and Tao,F.
  TITLE     Regulation of hPCL3 isoforms' ubiquitination by TRIM21 in non-small
            cell lung cancer progression
  JOURNAL   Life Sci Alliance 6 (10), e202302060 (2023)
   PUBMED   37507137
  REMARK    GeneRIF: Regulation of hPCL3 isoforms' ubiquitination by TRIM21 in
            non-small cell lung cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Xiaoyun,S., Yuyuan,Z., Jie,X., Yingjie,N., Qing,X., Yuezhen,D. and
            Haiguang,X.
  TITLE     PHF19 activates hedgehog signaling and promotes tumorigenesis in
            hepatocellular carcinoma
  JOURNAL   Exp Cell Res 406 (1), 112690 (2021)
   PUBMED   34129846
  REMARK    GeneRIF: PHF19 activates hedgehog signaling and promotes
            tumorigenesis in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Li,Y., Gong,J. and Zhang,L.
  TITLE     PHD finger protein 19 expression in multiple myeloma: Association
            with clinical features, induction therapy outcome, disease
            progression, and survival
  JOURNAL   J Clin Lab Anal 35 (9), e23910 (2021)
   PUBMED   34390275
  REMARK    GeneRIF: PHD finger protein 19 expression in multiple myeloma:
            Association with clinical features, induction therapy outcome,
            disease progression, and survival.
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Ghislin,S., Deshayes,F., Middendorp,S., Boggetto,N. and
            Alcaide-Loridan,C.
  TITLE     PHF19 and Akt control the switch between proliferative and invasive
            states in melanoma
  JOURNAL   Cell Cycle 11 (8), 1634-1645 (2012)
   PUBMED   22487681
  REMARK    GeneRIF: PHF19 silencing reduces the cell proliferation rate and
            increases the transendothelial migration capacities of melanoma
            cell lines.
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Boulay,G., Rosnoblet,C., Guerardel,C., Angrand,P.O. and Leprince,D.
  TITLE     Functional characterization of human Polycomb-like 3 isoforms
            identifies them as components of distinct EZH2 protein complexes
  JOURNAL   Biochem J 434 (2), 333-342 (2011)
   PUBMED   21143197
  REMARK    GeneRIF: Functional characterization of human Polycomb-like 3
            isoforms identifies them as components of distinct EZH2 protein
            complexes
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Zhernakova,A., Stahl,E.A., Trynka,G., Raychaudhuri,S., Festen,E.A.,
            Franke,L., Westra,H.J., Fehrmann,R.S., Kurreeman,F.A., Thomson,B.,
            Gupta,N., Romanos,J., McManus,R., Ryan,A.W., Turner,G., Brouwer,E.,
            Posthumus,M.D., Remmers,E.F., Tucci,F., Toes,R., Grandone,E.,
            Mazzilli,M.C., Rybak,A., Cukrowska,B., Coenen,M.J., Radstake,T.R.,
            van Riel,P.L., Li,Y., de Bakker,P.I., Gregersen,P.K.,
            Worthington,J., Siminovitch,K.A., Klareskog,L., Huizinga,T.W.,
            Wijmenga,C. and Plenge,R.M.
  TITLE     Meta-analysis of genome-wide association studies in celiac disease
            and rheumatoid arthritis identifies fourteen non-HLA shared loci
  JOURNAL   PLoS Genet 7 (2), e1002004 (2011)
   PUBMED   21383967
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Gregersen,P.K., Amos,C.I., Lee,A.T., Lu,Y., Remmers,E.F.,
            Kastner,D.L., Seldin,M.F., Criswell,L.A., Plenge,R.M., Holers,V.M.,
            Mikuls,T.R., Sokka,T., Moreland,L.W., Bridges,S.L. Jr., Xie,G.,
            Begovich,A.B. and Siminovitch,K.A.
  TITLE     REL, encoding a member of the NF-kappaB family of transcription
            factors, is a newly defined risk locus for rheumatoid arthritis
  JOURNAL   Nat Genet 41 (7), 820-823 (2009)
   PUBMED   19503088
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Wang,S., Robertson,G.P. and Zhu,J.
  TITLE     A novel human homologue of Drosophila polycomblike gene is
            up-regulated in multiple cancers
  JOURNAL   Gene 343 (1), 69-78 (2004)
   PUBMED   15563832
  REMARK    GeneRIF: identification of a gene encoding a human homologue of the
            Drosophila polycomblike protein, hPCL3 gene, encoding two nuclear
            proteins, hPCL3S and hPCL3L; markedly overexpressed in many types
            of cancers
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM784783.1, BC125076.1, BC044224.1, BU632411.1 and AI193743.1.
            
            On Jan 31, 2005 this sequence version replaced XP_045308.4.
            
            Transcript Variant: This variant (1) uses an alternate 5' terminal
            exon and it thus differs in its 5' UTR and initiates translation
            from a downstream in-frame start codon, compared to variant 3. The
            encoded isoform (a, also known as hPCL3L) is shorter at the
            N-terminus, compared to isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122744.1, BC125076.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373896.8/ ENSP00000363003.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.2"
     Protein         1..580
                     /product="PHD finger protein 19 isoform a"
                     /note="polycomb like 3; polycomb-like protein 3; tudor
                     domain containing 19B"
                     /calculated_mol_wt=65460
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          39..95
                     /region_name="Tudor_PHF19"
                     /note="Tudor domain found in PHD finger protein1 (PHF19)
                     and similar proteins; cd20451"
                     /db_xref="CDD:410522"
     Site            order(47,49..50,52..57,74..78,80,88..89,92..95)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410522"
     Site            47
                     /site_type="other"
                     /note="Histone H3K36me3 binding; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Site            55
                     /site_type="other"
                     /note="Histone H3K36me3 binding; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          74..80
                     /region_name="Histone H3K36me3 binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          98..150
                     /region_name="PHD1_PHF19"
                     /note="PHD finger 1 found in PHD finger protein 19
                     (PHF19); cd15579"
                     /db_xref="CDD:277054"
     Site            order(98,112..116,120,143)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277054"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          197..248
                     /region_name="PHD2_PHF19"
                     /note="PHD finger 2 found in PHD finger protein 19
                     (PHF19); cd15581"
                     /db_xref="CDD:277056"
     Site            order(197,209..213,217,241)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277056"
     Region          347..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          496..521
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          531..580
                     /region_name="Interaction with SUZ12.
                     /evidence=ECO:0000269|PubMed:29499137"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6S3.1)"
     Region          531..578
                     /region_name="Mtf2_C"
                     /note="Polycomb-like MTF2 factor 2; pfam14061"
                     /db_xref="CDD:464077"
     Region          531..544
                     /region_name="Important for PRC2 dimer stability.
                     /evidence=ECO:0000269|PubMed:31959557"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T6S3.1)"
     CDS             1..580
                     /gene="PHF19"
                     /gene_synonym="MTF2L1; PCL3; TDRD19B"
                     /coded_by="NM_015651.3:114..1856"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35116.1"
                     /db_xref="GeneID:26147"
                     /db_xref="HGNC:HGNC:24566"
                     /db_xref="MIM:609740"
ORIGIN      
        1 menraldpgt rdsygatshl pnkgalakvk nnfkdlmskl tegqyvlcrw tdglyylgki
       61 krvssskqsc lvtfednsky wvlwkdiqha gvpgeepkcn iclgktsgpl neilicgkcg
      121 lgyhqqchip iagsadqpll tpwfcrrcif alavrkggal kkgaiartlq avkmvlsyqp
      181 eelewdsphr tnqqqcycyc ggpgewylrm lqcyrcrqwf heactqclne pmmfgdrfyl
      241 ffcsvcnqgp eyierlplrw vdvvhlalyn lgvqskkkyf dfeeilafvn hhwellqlgk
      301 ltstpvtdrg phllnalnsy ksrflcgkei kkkkcifrlr irvppnppgk llpdkgllpn
      361 ensasselrk rgkskpgllp hefqqqkrrv yrrkrskfll edaipssdft sawstnhhla
      421 sifdftldei qslksassgq tffsdvdstd aastsgsast slsydsrwtv gsrkrklaak
      481 aymplrakrw aaeldgrcps dssaegasvp erpdegidsh tfesisedds slshlkssit
      541 nyfgaagrla cgekyqvlar rvtpegkvqy lvewegttpy
//
LOCUS       NP_060480                429 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 57 homolog [Homo sapiens].
ACCESSION   NP_060480
VERSION     NP_060480.1
DBSOURCE    REFSEQ: accession NM_018010.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Dong,K., Nihal,R., Meyer,T.J., Singh,S.P., Kaur,S. and Roberts,D.D.
  TITLE     CD47 and IFT57 Are Colinear Genes That Are Highly Coexpressed in
            Most Cancers and Exhibit Parallel Cancer-Specific Correlations with
            Survival
  JOURNAL   Int J Mol Sci 25 (16), 8956 (2024)
   PUBMED   39201643
  REMARK    GeneRIF: CD47 and IFT57 Are Colinear Genes That Are Highly
            Coexpressed in Most Cancers and Exhibit Parallel Cancer-Specific
            Correlations with Survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Baker,S.A., Freeman,K., Luby-Phelps,K., Pazour,G.J. and
            Besharse,J.C.
  TITLE     IFT20 links kinesin II with a mammalian intraflagellar transport
            complex that is conserved in motile flagella and sensory cilia
  JOURNAL   J Biol Chem 278 (36), 34211-34218 (2003)
   PUBMED   12821668
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Cheng,C.M., Huang,S.P., Chang,Y.F., Chung,W.Y. and Yuo,C.Y.
  TITLE     The viral death protein Apoptin interacts with Hippi, the protein
            interactor of Huntingtin-interacting protein 1
  JOURNAL   Biochem Biophys Res Commun 305 (2), 359-364 (2003)
   PUBMED   12745083
  REMARK    GeneRIF: Hippi interacts with the viral death protein Apoptin.
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Gervais,F.G., Singaraja,R., Xanthoudakis,S., Gutekunst,C.A.,
            Leavitt,B.R., Metzler,M., Hackam,A.S., Tam,J., Vaillancourt,J.P.,
            Houtzager,V., Rasper,D.M., Roy,S., Hayden,M.R. and Nicholson,D.W.
  TITLE     Recruitment and activation of caspase-8 by the
            Huntingtin-interacting protein Hip-1 and a novel partner Hippi
  JOURNAL   Nat Cell Biol 4 (2), 95-105 (2002)
   PUBMED   11788820
  REMARK    GeneRIF: Results show that pro-apoptotic Hippi-Hip-1 heterodimers
            can recruit procaspase-8 into a complex of Hippi, Hip-1 and
            procaspase-8, and launch apoptosis through components of the
            'extrinsic' cell-death pathway.
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Mattson,M.P.
  TITLE     Accomplices to neuronal death
  JOURNAL   Nature 415 (6870), 377-379 (2002)
   PUBMED   11807533
  REMARK    GeneRIF: critical for the death-promoting effects of mutant
            huntingtin protein in cultured cells
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Kalchman,M.A., Koide,H.B., McCutcheon,K., Graham,R.K., Nichol,K.,
            Nishiyama,K., Kazemi-Esfarjani,P., Lynn,F.C., Wellington,C.,
            Metzler,M., Goldberg,Y.P., Kanazawa,I., Gietz,R.D. and Hayden,M.R.
  TITLE     HIP1, a human homologue of S. cerevisiae Sla2p, interacts with
            membrane-associated huntingtin in the brain
  JOURNAL   Nat Genet 16 (1), 44-53 (1997)
   PUBMED   9140394
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA362330.1, BC011899.2, AC012020.17 and AF139576.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF139576.1, SRR1660803.177068.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2159764
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264538.4/ ENSP00000264538.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.12-q13.13"
     Protein         1..429
                     /product="intraflagellar transport protein 57 homolog"
                     /note="HIP1 protein interactor; estrogen-related receptor
                     beta like 1; huntingtin interacting protein-1 interacting
                     protein; HIP1-interacting protein; dermal papilla-derived
                     protein 8; estrogen-related receptor beta-like protein 1;
                     intraflagellar transport 57 homolog"
                     /calculated_mol_wt=48977
     Region          44..401
                     /region_name="IFT57"
                     /note="Intra-flagellar transport protein 57; pfam10498"
                     /db_xref="CDD:463118"
     Region          335..426
                     /region_name="pDED"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWB7.1)"
     CDS             1..429
                     /gene="IFT57"
                     /gene_synonym="ESRRBL1; HIPPI; MHS4R2; OFD18"
                     /coded_by="NM_018010.4:103..1392"
                     /db_xref="CCDS:CCDS2951.1"
                     /db_xref="GeneID:55081"
                     /db_xref="HGNC:HGNC:17367"
                     /db_xref="MIM:606621"
ORIGIN      
        1 mtaalavvtt sgledgvprs rgegtgevvl ergpgaayhm fvvmedlvek lkllryeeef
       61 lrksnlkaps rhyfalptnp geqfymfctl aawlinkagr pfeqpqeydd pnatisnils
      121 elrsfgrtad fppsklksgy gehvcyvldc faeealkyig ftwkrpiypv eeleeesvae
      181 ddaeltlnkv deefveeetd neenfidlnv lkaqtyhldm netakqedil esttdaaews
      241 levervlpql kvtirtdnkd wrihvdqmhq hrsgiesalk etkgfldklh neitrtleki
      301 ssrekyinnq lenlvqeyra aqaqlseake ryqqgnggvt ertrllsevm eelekvkqem
      361 eekgssmtdg aplvkikqsl tklkqetvem dirigiveht llqsklkeks nmtrnmhatv
      421 ipepatgfy
//
LOCUS       NP_004379                385 aa            linear   PRI 20-NOV-2025
DEFINITION  di-N-acetylchitobiase precursor [Homo sapiens].
ACCESSION   NP_004379
VERSION     NP_004379.1
DBSOURCE    REFSEQ: accession NM_004388.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Olszewski,S., Olszewska,E., Popko,J., Poskrobko,E., Sierakowski,S.
            and Zwierz,K.
  TITLE     Fibroblast-Like Synovial Cells in Rheumatoid Arthritis--the Impact
            of Infliximab on Hexosaminidase Activity
  JOURNAL   Adv Clin Exp Med 24 (5), 807-813 (2015)
   PUBMED   26768631
  REMARK    GeneRIF: Data indicate that infliximab changes the concentration of
            hexosaminidase (N-acetyl-beta-glucosaminidase; HEX) activity
            depending on the drug dose and time of administration.
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Aronson,N.N. and Halloran,B.A.
  TITLE     Optimum substrate size and specific anomer requirements for the
            reducing-end glycoside hydrolase di-N-acetylchitobiase
  JOURNAL   Biosci Biotechnol Biochem 70 (6), 1537-1541 (2006)
   PUBMED   16794344
  REMARK    GeneRIF: biochemical behavior of di-N-acetylchitobiase indicates it
            has three subsites, -2, -1, +1, in which the reducing-end trimer of
            any sized chitooligosaccharide is bound. The +1 site is specific
            for an alpha-anomer.
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Palmer,D.J., Kelly,V.C., Smit,A.M., Kuy,S., Knight,C.G. and
            Cooper,G.J.
  TITLE     Human colostrum: identification of minor proteins in the aqueous
            phase by proteomics
  JOURNAL   Proteomics 6 (7), 2208-2216 (2006)
   PUBMED   16502470
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Park,C., Meng,L., Stanton,L.H., Collins,R.E., Mast,S.W., Yi,X.,
            Strachan,H. and Moremen,K.W.
  TITLE     Characterization of a human core-specific lysosomal
            {alpha}1,6-mannosidase involved in N-glycan catabolism
  JOURNAL   J Biol Chem 280 (44), 37204-37216 (2005)
   PUBMED   16115860
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Hutchinson,T., Dwivedi,K., Rastogi,A., Prasad,R. and Pereira,B.M.
  TITLE     N-acetyl beta-D-glucosaminidase is not attached to human sperm
            membranes through the glycosylphosphatidyl inositol (GPI)-anchor
  JOURNAL   Asian J Androl 4 (1), 27-33 (2002)
   PUBMED   11907625
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Ahmad,W., Li,S., Chen,H., Tuck-Muller,C.M., Pittler,S.J. and
            Aronson,N.N. Jr.
  TITLE     Lysosomal chitobiase (CTB) and the G-protein gamma 5 subunit (GNG5)
            genes co-localize to human chromosome 1p22
  JOURNAL   Cytogenet Cell Genet 71 (1), 44-46 (1995)
   PUBMED   7606925
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Cloning and expression of the cDNA sequence encoding the lysosomal
            glycosidase di-N-acetylchitobiase
  JOURNAL   J Biol Chem 267 (27), 19607-19616 (1992)
   PUBMED   1527079
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Fisher,K.J. and Aronson,N.N. Jr.
  TITLE     Characterization of the cDNA and genomic sequence of a G protein
            gamma subunit (gamma 5)
  JOURNAL   Mol Cell Biol 12 (4), 1585-1591 (1992)
   PUBMED   1549114
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Aronson,N.N. Jr. and Kuranda,M.J.
  TITLE     Lysosomal degradation of Asn-linked glycoproteins
  JOURNAL   FASEB J 3 (14), 2615-2622 (1989)
   PUBMED   2531691
  REMARK    Review article
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Aronson,N.N. Jr., Backes,M. and Kuranda,M.J.
  TITLE     Rat liver chitobiase: purification, properties, and role in the
            lysosomal degradation of Asn-linked glycoproteins
  JOURNAL   Arch Biochem Biophys 272 (2), 290-300 (1989)
   PUBMED   2751306
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC126335.1, BC065191.1, AI339601.1 and AL359762.24.
            
            Summary: Chitobiase is a lysosomal glycosidase involved in
            degradation of asparagine-linked oligosaccharides on glycoproteins
            (Aronson and Kuranda, 1989 [PubMed 2531691]).[supplied by OMIM, Nov
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298703.1, SRR1660809.252331.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370630.6/ ENSP00000359664.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.3"
     Protein         1..385
                     /product="di-N-acetylchitobiase precursor"
                     /EC_number="3.2.1.-"
                     /note="di-N-acetylchitobiase; chitobiase, di-N-acetyl-"
                     /calculated_mol_wt=39756
     sig_peptide     1..38
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4022
     mat_peptide     39..385
                     /product="Di-N-acetylchitobiase. /id=PRO_0000011961"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01459.1)"
                     /calculated_mol_wt=39756
     Region          39..378
                     /region_name="GH18_chitobiase"
                     /note="Chitobiase (also known as di-N-acetylchitobiase) is
                     a lysosomal glycosidase that hydrolyzes the reducing-end
                     N-acetylglucosamine from the chitobiose core of
                     oligosaccharides during the ordered degradation of
                     asparagine-linked glycoproteins in eukaryotes; cd02875"
                     /db_xref="CDD:119354"
     Site            order(48,75,139,141,143,209..210,254,354)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:119354"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            262
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q01459.1)"
     CDS             1..385
                     /gene="CTBS"
                     /gene_synonym="CTB"
                     /coded_by="NM_004388.3:26..1183"
                     /db_xref="CCDS:CCDS698.1"
                     /db_xref="GeneID:1486"
                     /db_xref="HGNC:HGNC:2496"
                     /db_xref="MIM:600873"
ORIGIN      
        1 msrpqlrrwr lvssppsgvp glallallal lalrlaagtd cpcpepelcr pirhhpdfev
       61 fvfdvgqktw ksydwsqitt vatfgkydse lmcyahskga rvvlkgdvsl kdiidpafra
      121 swiaqklnla ktqymdgini dieqevncls peydaltalv kettdsfhre iegsqvtfdv
      181 awspknidrr cynytgiada cdflfvmsyd eqsqiwseci aaanapynqt ltgyndyikm
      241 sinpkklvmg vpwygydytc lnlsedhvct iakvpfrgap csdaagrqvp yktimkqins
      301 sisgnlwdkd qrapyynykd paghfhqvwy dnpqsislka tyiqnyrlrg igmwnancld
      361 ysgdavakqq teemwevlkp kllqr
//
LOCUS       NP_001160136             273 aa            linear   PRI 20-NOV-2025
DEFINITION  natural killer cell receptor 2B4 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001160136
VERSION     NP_001160136.1
DBSOURCE    REFSEQ: accession NM_001166664.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Mou,J., Xie,L., Xu,Y., Zhou,T., Liu,Y., Huang,Q., Tang,K., Tian,Z.,
            Xing,H., Qiu,S., Rao,Q., Wang,M. and Wang,J.
  TITLE     2B4 inhibits the apoptosis of natural killer cells through
            phosphorylated extracellular signal-related kinase/B-cell lymphoma
            2 signal pathway
  JOURNAL   Cytotherapy 25 (10), 1080-1090 (2023)
   PUBMED   37516949
  REMARK    GeneRIF: 2B4 inhibits the apoptosis of natural killer cells through
            phosphorylated extracellular signal-related kinase/B-cell lymphoma
            2 signal pathway.
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Mohammadi,M., Asgarian-Omran,H., Najafi,A., Valadan,R., Karami,H.,
            Naderisoraki,M., Zaboli,E., Eslami,M. and Tehrani,M.
  TITLE     Evaluation of mRNA Expression of CD244 and Its Adapter Molecules in
            CD8+ T Cells in Acute Leukemia
  JOURNAL   Iran Biomed J 27 (4), 214-218 (2023)
   PUBMED   37634081
  REMARK    GeneRIF: Evaluation of mRNA Expression of CD244 and Its Adapter
            Molecules in CD8+ T Cells in Acute Leukemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Huang,S., Liang,C., Zhao,Y., Deng,T., Tan,J., Lu,Y., Liu,S., Li,Y.
            and Chen,S.
  TITLE     Increased TOX expression concurrent with PD-1, Tim-3, and CD244 in
            T cells from patients with non-Hodgkin lymphoma
  JOURNAL   Asia Pac J Clin Oncol 18 (1), 143-149 (2022)
   PUBMED   33608984
  REMARK    GeneRIF: Increased TOX expression concurrent with PD-1, Tim-3, and
            CD244 in T cells from patients with non-Hodgkin lymphoma.
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Wu,X., Sharma,A., Oldenburg,J., Weiher,H., Essler,M., Skowasch,D.
            and Schmidt-Wolf,I.G.H.
  TITLE     NKG2D Engagement Alone Is Sufficient to Activate Cytokine-Induced
            Killer Cells While 2B4 Only Provides Limited Coactivation
  JOURNAL   Front Immunol 12, 731767 (2021)
   PUBMED   34691037
  REMARK    GeneRIF: NKG2D Engagement Alone Is Sufficient to Activate
            Cytokine-Induced Killer Cells While 2B4 Only Provides Limited
            Coactivation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Tangye,S.G., Lazetic,S., Woollatt,E., Sutherland,G.R., Lanier,L.L.
            and Phillips,J.H.
  TITLE     Cutting edge: human 2B4, an activating NK cell receptor, recruits
            the protein tyrosine phosphatase SHP-2 and the adaptor signaling
            protein SAP
  JOURNAL   J Immunol 162 (12), 6981-6985 (1999)
   PUBMED   10358138
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Brown,M.H., Boles,K., van der Merwe,P.A., Kumar,V., Mathew,P.A. and
            Barclay,A.N.
  TITLE     2B4, the natural killer and T cell immunoglobulin superfamily
            surface protein, is a ligand for CD48
  JOURNAL   J Exp Med 188 (11), 2083-2090 (1998)
   PUBMED   9841922
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Latchman,Y., McKay,P.F. and Reiser,H.
  TITLE     Identification of the 2B4 molecule as a counter-receptor for CD48
  JOURNAL   J Immunol 161 (11), 5809-5812 (1998)
   PUBMED   9834056
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Valiante,N.M. and Trinchieri,G.
  TITLE     Identification of a novel signal transduction surface molecule on
            human cytotoxic lymphocytes
  JOURNAL   J Exp Med 178 (4), 1397-1406 (1993)
   PUBMED   8376943
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Siu,G., Strauss,E.C., Lai,E. and Hood,L.E.
  TITLE     Analysis of a human V beta gene subfamily
  JOURNAL   J Exp Med 164 (5), 1600-1614 (1986)
   PUBMED   3772297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC028073.1 and BC041607.1.
            
            Summary: This gene encodes a cell surface receptor expressed on
            natural killer (NK) cells (and some T cells) that mediate non-major
            histocompatibility complex (MHC) restricted killing. The
            interaction between NK-cell and target cells via this receptor is
            thought to modulate NK-cell cytolytic activity. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (3) is lacking an in-frame coding
            exon compared to variant 1, resulting in a shorter isoform (3)
            missing an internal protein segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ245376.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..273
                     /product="natural killer cell receptor 2B4 isoform 3
                     precursor"
                     /note="NK cell activation inducing ligand NAIL; h2B4; NK
                     cell activation-inducing ligand; NK cell type I receptor
                     protein 2B4; SLAM family member 4; signaling lymphocytic
                     activation molecule 4; CD244 molecule, natural killer cell
                     receptor 2B4"
                     /calculated_mol_wt=28745
     sig_peptide     1..18
                     /calculated_mol_wt=2058
     mat_peptide     19..273
                     /product="natural killer cell receptor 2B4 isoform 3"
                     /calculated_mol_wt=28745
     Region          22..127
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          50..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21606496; propagated from
                     UniProtKB/Swiss-Prot (Q9BZW8.2)"
     Site            77
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21606496; propagated from
                     UniProtKB/Swiss-Prot (Q9BZW8.2)"
     Site            89
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21606496; propagated from
                     UniProtKB/Swiss-Prot (Q9BZW8.2)"
     Region          90..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          104..109
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          118..121
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..273
                     /gene="CD244"
                     /gene_synonym="2B4; NAIL; NKR2B4; Nmrk; SLAMF4"
                     /coded_by="NM_001166664.2:211..1032"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS53398.1"
                     /db_xref="GeneID:51744"
                     /db_xref="HGNC:HGNC:18171"
                     /db_xref="MIM:605554"
ORIGIN      
        1 mlgqvvtlil llllkvyqgk gcqgsadhvv sisgvplqlq pnsiqtkvds iawkkllpsq
       61 ngfhhilkwe ngslpsntsn drfsfivknl sllikaaqqq dsglyclevt sisgkvqtat
      121 fqvfvfefrf wpflviivil salflgtlac fcvwrrkrke kqsetspkef ltiyedvkdl
      181 ktrrnheqeq tfpgggstiy smiqsqssap tsqepaytly sliqpsrksg srkrnhspsf
      241 nstiyevigk sqpkaqnpar lsrkelenfd vys
//
LOCUS       NP_009298               1182 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform b [Homo sapiens].
ACCESSION   NP_009298
VERSION     NP_009298.1
DBSOURCE    REFSEQ: accession NM_007314.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1182)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1182)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1182)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1182)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1182)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1182)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1182)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1182)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1182)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1182)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512326.25, M35296.1,
            AL139132.16 and BQ014912.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (b) represents the longest
            transcript and encodes the longest isoform (b, also known as
            1BLCTL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M35296.1, SRR1803615.145147.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000502732.6/ ENSP00000427562.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1182
                     /product="tyrosine-protein kinase ABL2 isoform b"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=128212
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          2..106
                     /region_name="CAP"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          60..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          111..164
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(116,118,121..123,125,140,144..145,156,158,160..161)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(120..123,142,144)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          169..262
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(180,208,221)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15735735; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          281..543
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(294,296..298,315,317,362,364,368,416,427,445..447,
                     449,457,491,495)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(294,296,299,315,317,332,336,345,361..362,364,368,
                     416,426..427)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(309..310,340..342,346,388,420..421,539..540)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(386..387,390,475,478..479,508..509)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            426..450
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Region          427..451
                     /region_name="Kinase activation loop.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis and SRC-type
                     Tyr-kinases. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(445..447,449,457,491,495)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          611..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          654..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          658..660
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; Phosphotyrosine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          694..930
                     /region_name="F-actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          763..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            776
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          807..851
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          964..1024
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          1020..1182
                     /region_name="F-actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          1063..1182
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1182
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_007314.4:281..3829"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS30947.1"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mgqqvgrvge apglqqpqpr girgssaarp sgrrrdpagr ttetgfnift qhdhfascve
       61 dgfegdktgg sspealhrpy gcdvepqaln eairwssken llgatesdpn lfvalydfva
      121 sgdntlsitk geklrvlgyn qngewsevrs kngqgwvpsn yitpvnslek hswyhgpvsr
      181 saaeyllssl ingsflvres esspgqlsis lryegrvyhy rinttadgkv yvtaesrfst
      241 laelvhhhst vadglvttlh ypapkcnkpt vygvspihdk wemertditm khklgggqyg
      301 evyvgvwkky sltvavktlk edtmeveefl keaavmkeik hpnlvqllgv ctleppfyiv
      361 teympygnll dylrecnree vtavvllyma tqissameyl ekknfihrdl aarnclvgen
      421 hvvkvadfgl srlmtgdtyt ahagakfpik wtapeslayn tfsiksdvwa fgvllweiat
      481 ygmspypgid lsqvydllek gyrmeqpegc ppkvyelmra cwkwspadrp sfaethqafe
      541 tmfhdssise evaeelgraa ssssvvpylp rlpilpsktr tlkkqvenke niegaqdate
      601 nsasslapgf irgaqassgs palprkqrdk spsslledak etcftrdrkg gffssfmkkr
      661 naptppkrss sfremenqph kkyeltgnfs svaslqhadg fsftpaqqea nlvppkcygg
      721 sfaqrnlcnd dggggggsgt agggwsgitg fftprlikkt lglragkpta sddtskpfpr
      781 snstssmssg lpeqdrmamt lprncqrskl qlertvstss qpeenvdran dmlpkksees
      841 aapsrerpka kllprgatal plrtpsgdla itekdppgvg vagvaaapkg keknggarlg
      901 magvpedgeq pgwpspakaa pvlptthnhk vpvlisptlk htpadvqlig tdsqgnkfkl
      961 lsehqvtssg dkdrprrvkp kcapppppvm rllqhpsics dpteeptalt agqstsetqe
     1021 ggkkaalgav pisgkagrpv mpppqvplpt ssispakman gtagtkvalr ktkqaaekis
     1081 adkiskeall ecadllssal tepvpnsqlv dtghqlldyc sgyvdcipqt rnkfafreav
     1141 sklelslqel qvssaaagvp gtnpvlnnll scvqeisdvv qr
//
LOCUS       NP_113584               4374 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase HUWE1 isoform 1 [Homo sapiens].
ACCESSION   NP_113584 NP_005694 NP_060097 XP_497119
VERSION     NP_113584.3
DBSOURCE    REFSEQ: accession NM_031407.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 4374)
  AUTHORS   Lee,C., Park,S.H. and Yoon,S.K.
  TITLE     The E3 ligase HUWE1 increases the sensitivity of CRC to oxaliplatin
            through TOMM20 degradation
  JOURNAL   Oncogene 43 (9), 636-649 (2024)
   PUBMED   38184713
  REMARK    GeneRIF: The E3 ligase HUWE1 increases the sensitivity of CRC to
            oxaliplatin through TOMM20 degradation.
REFERENCE   3  (residues 1 to 4374)
  AUTHORS   Li,X.X., Xu,J.K., Su,W.J., Wu,H.L., Zhao,K., Zhang,C.M., Chen,X.K.
            and Yang,L.X.
  TITLE     The role of KDM4A-mediated histone methylation on temozolomide
            resistance in glioma cells through the HUWE1/ROCK2 axis
  JOURNAL   Kaohsiung J Med Sci 40 (2), 161-174 (2024)
   PUBMED   37873881
  REMARK    GeneRIF: The role of KDM4A-mediated histone methylation on
            temozolomide resistance in glioma cells through the HUWE1/ROCK2
            axis.
REFERENCE   4  (residues 1 to 4374)
  AUTHORS   Bernassola,F., Karin,M., Ciechanover,A. and Melino,G.
  TITLE     The HECT family of E3 ubiquitin ligases: multiple players in cancer
            development
  JOURNAL   Cancer Cell 14 (1), 10-21 (2008)
   PUBMED   18598940
  REMARK    Review article
REFERENCE   5  (residues 1 to 4374)
  AUTHORS   Zhong,Q., Gao,W., Du,F. and Wang,X.
  TITLE     Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the
            polyubiquitination of Mcl-1 and regulates apoptosis
  JOURNAL   Cell 121 (7), 1085-1095 (2005)
   PUBMED   15989957
  REMARK    GeneRIF: Mule is both required and sufficient for the
            polyubiquitination of Mcl-1; Mule is a unique BH3-containing E3
            ubiquitin ligase apical to Bcl-2 family proteins during DNA
            damage-induced apoptosis
            GeneRIF: Mule (HUWE1) poly-ubiquitinates anti-apoptotic gene Mcl-1.
REFERENCE   6  (residues 1 to 4374)
  AUTHORS   Chen,D., Kon,N., Li,M., Zhang,W., Qin,J. and Gu,W.
  TITLE     ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
  JOURNAL   Cell 121 (7), 1071-1083 (2005)
   PUBMED   15989956
  REMARK    GeneRIF: study modifies the current view of ARF-mediated p53
            activation and reveals that ARF-BP1 is a critical mediator of both
            the p53-independent and p53-dependent tumor suppressor functions of
            ARF
            GeneRIF: Ubiquitin ligase activity of ARF-BP1 (HUWE1) is inhibited
            by Arf.
REFERENCE   7  (residues 1 to 4374)
  AUTHORS   Liu,Z., Oughtred,R. and Wing,S.S.
  TITLE     Characterization of E3Histone, a novel testis ubiquitin protein
            ligase which ubiquitinates histones
  JOURNAL   Mol Cell Biol 25 (7), 2819-2831 (2005)
   PUBMED   15767685
REFERENCE   8  (residues 1 to 4374)
  AUTHORS   Gu,J., Dubner,R., Fornace,A.J. Jr. and Iadarola,M.J.
  TITLE     UREB1, a tyrosine phosphorylated nuclear protein, inhibits p53
            transactivation
  JOURNAL   Oncogene 11 (10), 2175-2178 (1995)
   PUBMED   7478539
REFERENCE   9  (residues 1 to 4374)
  AUTHORS   Turner,G., Gedeon,A. and Mulley,J.
  TITLE     X-linked mental retardation with heterozygous expression and
            macrocephaly: pericentromeric gene localization
  JOURNAL   Am J Med Genet 51 (4), 575-580 (1994)
   PUBMED   7943042
REFERENCE   10 (residues 1 to 4374)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DQ097177.1, BX323845.7,
            AY772009.1, AC231658.3, AB002310.3 and R60532.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 24, 2005 this sequence version replaced
            XP_497119.1, NP_113584.2.
            
            Summary: This gene encodes a protein containing a C-terminal HECT
            (E6AP type E3 ubiquitin protein ligase) domain that functions as an
            E3 ubiquitin ligase. The encoded protein is required for the
            ubiquitination and subsequent degradation of the anti-apoptotic
            protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)).
            This protein also ubiquitinates the p53 tumor suppressor, core
            histones, and DNA polymerase beta. Mutations in this gene are
            associated with Turner type X-linked syndromic cognitive
            disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ097177.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262854.11/ ENSP00000262854.6
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.22"
     Protein         1..4374
                     /product="E3 ubiquitin-protein ligase HUWE1 isoform 1"
                     /EC_number="2.3.2.26"
                     /note="Mcl-1 ubiquitin ligase E3; BJ-HCC-24 tumor antigen;
                     HECT domain protein LASU1; ARF-binding protein 1;
                     URE-binding protein 1; large structure of UREB1; upstream
                     regulatory element-binding protein 1; homologous to E6AP
                     carboxyl terminus homologous protein 9; HECT-type E3
                     ubiquitin transferase HUWE1; HECT, UBA and WWE domain
                     containing 1, E3 ubiquitin protein ligase"
                     /calculated_mol_wt=481762
     Region          92..367
                     /region_name="DUF908"
                     /note="Domain of Unknown Function (DUF908); pfam06012"
                     /db_xref="CDD:428721"
     Region          431..814
                     /region_name="DUF913"
                     /note="Domain of Unknown Function (DUF913); pfam06025"
                     /db_xref="CDD:461803"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          706..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          978..1001
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1014..1037
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1291..1320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1317..1356
                     /region_name="UBA_HUWE1"
                     /note="UBA domain found in eukaryotic E3 ubiquitin-protein
                     ligase HUWE1 and similar proteins; cd14288"
                     /db_xref="CDD:270474"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1396..1415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          1617..1678
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          1689..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            1907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2018..2065
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2035
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2262..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2267
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2356..2480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2554
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          2694..2970
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          <2735..3066
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            2751
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2889
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            2918
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3010..3043
                     /region_name="UBM"
                     /note="Ubiquitin binding region; pfam14377"
                     /db_xref="CDD:464159"
     Region          3036..3059
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3149
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q7TMY8; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3245..3267
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3404..3424
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3471..3512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3537..3568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3737..3758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3781..3848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3830
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          3894..3931
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3924
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Site            3927
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     Region          4019..4372
                     /region_name="HECTc"
                     /note="HECT domain; C-terminal catalytic domain of a
                     subclass of Ubiquitin-protein ligase (E3). It binds
                     specific ubiquitin-conjugating enzymes (E2), accepts
                     ubiquitin from E2, transfers ubiquitin to substrate lysine
                     side chains, and transfers additional...; cd00078"
                     /db_xref="CDD:238033"
     Site            order(4023,4053,4064,4125,4299,4335..4336,4339..4343,4363,
                     4371)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Site            order(4153,4156..4157,4159..4160,4163,4170,4172,
                     4176..4177,4179,4184,4189,4206,4210)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     Site            4271
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P51593; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6Z7.3)"
     CDS             1..4374
                     /gene="HUWE1"
                     /gene_synonym="ARF-BP1; HECTH9; HSPC272; Ib772; LASU1;
                     MRXST; MULE; URE-B1; UREB1"
                     /coded_by="NM_031407.7:394..13518"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35301.1"
                     /db_xref="GeneID:10075"
                     /db_xref="HGNC:HGNC:30892"
                     /db_xref="MIM:300697"
ORIGIN      
        1 mkvdrtklkk tpteapadcr alidklkvcn deqlllelqq iktwnigkce lyhwvdlldr
       61 fdgiladagq tvenmswmlv cdrpereqlk mlllavlnft allieysfsr hlyssiehlt
      121 tllassdmqv vlavlnllyv fskrsnyitr lgsdkrtpll trlqhlaesw ggkengfgla
      181 eccrdlhmmk yppsattlhf efyadpgaev kiekrttsnt lhyihieqld kisespseim
      241 esltkmysip kdkqmllfth irlahgfsnh rkrlqavqar lhaisilvys nalqesansi
      301 lynglieelv dvlqitdkql meikaaslrt ltsivhlert pklssiidct gtasyhgflp
      361 vlvrnciqam idpsmdpyph qfatalfsfl yhlasydagg ealvscgmme allkvikflg
      421 deqdqitfvt ravrvvdlit nldmaafqsh sglsifiyrl ehevdlcrke cpfvikpkiq
      481 rpnttqegee metdmdgvqc ipqraallks mlnflkkaiq dpafsdgirh vmdgslptsl
      541 khiisnaeyy gpslfllate vvtvfvfqep sllsslqdng ltdvmlhall ikdvpatrev
      601 lgslpnvfsa lclnarglqs fvqcqpferl fkvllspdyl pamrrrrssd plgdtasnlg
      661 savdelmrhq ptlktdatta iiklleeicn lgrdpkyicq kpsiqkadgt atappprsnh
      721 aaeeassede eeeevqamqs fnstqqnete pnqqvvgtee ripiplmdyi lnvmkfvesi
      781 lsnnttddhc qefvnqkgll plvtilglpn lpidfptsaa cqavagvcks iltlshepkv
      841 lqegllqlds ilssleplhr piespggsvl lrelacagnv adatlsaqat pllhaltaah
      901 ayimmfvhtc rvgqseirsi svnqwgsqlg lsvlsklsql ycslvwestv llslctpnsl
      961 psgcefgqad mqklvpkdek agttqggkrs dgeqdgaags mdastqglle gigldgdtla
     1021 pmetdeptas dskgkskitp amaarikqik pllsassrlg ralaelfgll vklcvgspvr
     1081 qrrshhaast ttaptpaars tasaltkllt kglswqpppy tptprfrltf ficsvgftsp
     1141 mlfderkypy hlmlqkflcs gghnalfetf nwalsmggkv pvseglehsd lpdgtgefld
     1201 awlmlvekmv npttvlesph slpaklpggv qnfpqfsalr flvvtqkaaf tciknlwnrk
     1261 plkvyggrma esmlailchi lrgepvirer lskekegsrg eedtgqeegg srrepqvnqq
     1321 qlqqlmdmgf trehameall ntstmeqate yllthpppim ggvvrdlsms eedqmmraia
     1381 mslgqdipmd qraespeeva crkeeeerka rekqeeeeak clekfqdadp leqdelhtft
     1441 dtmlpgcfhl ldelpdtvyr vcdlimtaik rngadyrdmi lkqvvnqvwe aadvlikaal
     1501 plttsdtktv sewisqmatl pqasnlatri llltllfeel klpcawvves sgilnvlikl
     1561 levvqpclqa akeqkevqtp kwitpvllli dfyektaiss krraqmtkyl qsnsnnwrwf
     1621 ddrsgrwcsy sasnnstids awksgetsvr ftagrrrytv qfttmvqvne etgnrrpvml
     1681 tllrvprlnk nsknsngqel ektleeskem dikrkenkgn dtplalestn teketsleet
     1741 kigeiliqgl tedmvtvlir acvsmlgvpv dpdtlhatlr lclrltrdhk yammfaelks
     1801 trmilnltqs sgfngftplv tlllrhiied pctlrhtmek vvrsaatsga gsttsgvvsg
     1861 slgsreinyi lrvlgpaacr npdiftevan ccirialpap rgsgtasdde fenlrikgpn
     1921 avqlvkttpl kpsplpvipd tikeviydml nalaayhape eadksdpkpg vmtqevgqll
     1981 qdmgddvyqq yrsltrqssd fdtqsgfsin sqvfaadgas tetsasgtsq geastpeesr
     2041 dgkkdkegdr aseegkqkgk gskplmptst ilrllaelvr syvgiatlia nysytvgqse
     2101 likedcsvla fvldhllpht qnaedkdtpa larlflasla aagsgtdaqv alvnevkaal
     2161 gralamaest ekharlqavm ciistimesc pstssfyssa taktqhngmn niirlflkkg
     2221 lvndlarvph sldlsspnma ntvnaalkpl etlsrivnqp sslfgsksas sknkseqdaq
     2281 gasqdsssnq qdpgepgeae vqeedhdvtq tevadgdimd geaetdsvvi agqpevlssq
     2341 emqveneled lidellerdg gsgnstiivs rsgedesqed vlmdeapsnl sqastlqanr
     2401 edsmnildpe deeehtqeed ssgsnededd sqdeeeeeee deeddqedde geegdedddd
     2461 dgsemelded ypdmnasplv rferfdredd liiefdnmfs satdippspg niptthplmv
     2521 rhadhssltl gsgssttrlt qgigrsqrtl rqltantght ihvhypgnrq pnpplilqrl
     2581 lgpsaaadil qlssslplqs rgrarllvgn ddvhiiarsd dellddffhd qstatsqagt
     2641 lssiptaltr wteeckvlda esmhdcvsvv kvsivnhlef lrdeeleerr ekrrkqlaee
     2701 etkitdkgke dkenrdqsaq ctasksndst eqnlsdgtpm pdsypttpss tdaatseske
     2761 tlgtlqssqq qptlptppal gevpqelqsp ageggsstql lmpvepeelg ptrpsgeaet
     2821 tqmelspapt itslsperae dsdaltavss qlegspmdts slasctleea vgdtsaagss
     2881 eqpragsstp gdappavaev qgrsdgsges aqppedsspp assessstrd savaisgads
     2941 rgileeplps tsseeedpla gislpegvdp sflaalpddi rrevlqnqlg irpptrtaps
     3001 tnssapavvg npgvtevspe flaalppaiq eevlaqqrae qqrrelaqna ssdtpmdpvt
     3061 fiqtlpsdlr rsvledmeds vlavmppdia aeaqalrreq earqrqlmhe rlfghsstsa
     3121 lsailrspaf tsrlsgnrgv qytrlavqrg gtfqmggsss hnrpsgsnvd tllrlrgrll
     3181 ldhealscll vllfvdepkl ntsrlhrvlr nlcyhaqtrh wvirsllsil qrsseselci
     3241 etpklttsee kgkksskscg ssshenrpld llhkmeskss nqlswlsvsm daalgcrtni
     3301 fqiqrsggrk htekhasggs tvhihpqaap vvcrhvldtl iqlakvfpsh ftqqrtketn
     3361 cesdrergnk acspcssqss ssgictdfwd llvkldnmnv srkgknsvks vpvsaggege
     3421 tspysleasp lgqlmnmlsh pvirrssllt ekllrllsli sialpenkvs eaqansgsga
     3481 sstttatstt stttttaast tptpptaptp vtsapalvaa taistivvaa sttvttptta
     3541 tttvsisptt kgskspakvs dggssstdfk mvssgltenq lqlsvevlts hscseegled
     3601 aanvllqlsr gdsgtrdtvl klllngarhl gytlckqigt llaelreynl eqqrraqcet
     3661 lspdglpeeq pqttklkgkm qsrfdmaenv vivasqkrpl ggrelqlpsm smltsktstq
     3721 kfflrvlqvi iqlrddtrra nkkakqtgrl gssglgsass iqaavrqlea eadaiiqmvr
     3781 egqrarrqqq aatsessqse asvrreespm dvdqpspsaq dtqsiasdgt pqgekekeer
     3841 ppelpllseq lsldelwdml geclkelees hdqhavlvlq paveafflvh atereskppv
     3901 rdtresqlah ikdeppplsp apltpatpss ldpffsreps smhissslpp dtqkflrfae
     3961 thrtvlnqil rqstthladg pfavlvdyir vldfdvkrky frqelerlde glrkedmavh
     4021 vrrdhvfeds yrelhrkspe emknrlyivf egeegqdagg llrewymiis remfnpmyal
     4081 frtspgdrvt ytinpsshcn pnhlsyfkfv grivakavyd nrllecyftr sfykhilgks
     4141 vrytdmesed yhfyqglvyl lendvstlgy dltfstevqe fgvcevrdlk pnganilvte
     4201 enkkeyvhlv cqmrmtgair kqlaaflegf yeiipkrlis ifteqelell isglptidid
     4261 dlksnteyhk yqsnsiqiqw fwralrsfdq adrakflqfv tgtskvplqg faalegmngi
     4321 qkfqihrddr stdrlpsaht cfnqldlpay esfeklrhml llaiqecseg fgla
//
LOCUS       NP_001354587             547 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform x [Homo sapiens].
ACCESSION   NP_001354587
VERSION     NP_001354587.1
DBSOURCE    REFSEQ: accession NM_001367658.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 547)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 547)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 547)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 547)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 547)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 547)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 547)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 547)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 547)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 547)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2155974,
                              SAMN02400289 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..547
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..547
                     /product="SUN domain-containing protein 1 isoform x"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=60816
     Region          179..232
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(179,182..183,186,189..190,193..194,196..197,
                     200..201,203..204,207..208,210..211,214,217..218,221,
                     224..225,228..229,231..232)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          191..>324
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          309..367
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          410..545
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..547
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367658.1:716..2359"
                     /note="isoform x is encoded by transcript variant 24"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mcrlllaads aqdrscgpgc vqdgvvgpla grgcsregsl wsvlvagdwm vpvcyfdfla
       61 ecvssyqvps khlqvfslah ptlpftsmhr tqrvddpqdv fkpttsrlkq plqgdseafp
      121 whwmsgveqq vaslsgqchh hgenlreltt llqklqarvd qmeggaagps asvrdavgqp
      181 pretdfmafh qehevrmshl edilgklrek seaiqkeleq tkqktisavg eqllptvehl
      241 qleldqlkse lsswrhvktg cetvdavqer vdvqvremvk llfsedqqgg sleqllqrfs
      301 sqfvskgdlq tmlrdlqlqi lrnvthhvsv tkqlptseav vsavseagas giteaqarai
      361 vnsalklysq dktgmvdfal esgggsilst rcsetyetkt almslfgipl wyfsqsprvv
      421 iqpdiypgnc wafkgsqgyl vvrlsmmihp aaftlehipk tlsptgniss apkdfavygl
      481 eneyqeegql lgqftydqdg eslqmfqalk rpddtafqiv elrifsnwgh peytclyrfr
      541 vhgepvk
//
LOCUS       NP_005902                395 aa            linear   PRI 20-NOV-2025
DEFINITION  S-adenosylmethionine synthase isoform type-2 [Homo sapiens].
ACCESSION   NP_005902
VERSION     NP_005902.1
DBSOURCE    REFSEQ: accession NM_005911.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Jiang,C., Liu,J., He,S., Xu,W., Huang,R., Pan,W., Li,X., Dai,X.,
            Guo,J., Zhang,T., Inuzuka,H., Wang,P., Asara,J.M., Xiao,J. and
            Wei,W.
  TITLE     PRMT1 orchestrates with SAMTOR to govern mTORC1 methionine sensing
            via Arg-methylation of NPRL2
  JOURNAL   Cell Metab 35 (12), 2183-2199 (2023)
   PUBMED   38006878
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Hunter,O.V., Ruiz,J.C., Flaherty,J.N. and Conrad,N.K.
  TITLE     Functional analysis of 3'-UTR hairpins supports a two-tiered model
            for posttranscriptional regulation of MAT2A by METTL16
  JOURNAL   RNA 29 (11), 1725-1737 (2023)
   PUBMED   37567786
  REMARK    GeneRIF: Functional analysis of 3'-UTR hairpins supports a
            two-tiered model for posttranscriptional regulation of MAT2A by
            METTL16.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Egri,S.B., Ouch,C., Chou,H.T., Yu,Z., Song,K., Xu,C. and Shen,K.
  TITLE     Cryo-EM structures of the human GATOR1-Rag-Ragulator complex reveal
            a spatial-constraint regulated GAP mechanism
  JOURNAL   Mol Cell 82 (10), 1836-1849 (2022)
   PUBMED   35338845
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Herre,C., Nshdejan,A., Klopfleisch,R., Corte,G.M. and
            Bahramsoltani,M.
  TITLE     Expression of vimentin, TPI and MAT2A in human dermal microvascular
            endothelial cells during angiogenesis in vitro
  JOURNAL   PLoS One 17 (4), e0266774 (2022)
   PUBMED   35482724
  REMARK    GeneRIF: Expression of vimentin, TPI and MAT2A in human dermal
            microvascular endothelial cells during angiogenesis in vitro.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Mao,Z., Liu,S., Cai,J., Huang,Z.Z. and Lu,S.C.
  TITLE     Cloning and functional characterization of the 5'-flanking region
            of human methionine adenosyltransferase 2A gene
  JOURNAL   Biochem Biophys Res Commun 248 (3), 479-484 (1998)
   PUBMED   9703951
REFERENCE   7  (residues 1 to 395)
  AUTHORS   De La Rosa,J., Ostrowski,J., Hryniewicz,M.M., Kredich,N.M.,
            Kotb,M., LeGros,H.L. Jr., Valentine,M. and Geller,A.M.
  TITLE     Chromosomal localization and catalytic properties of the
            recombinant alpha subunit of human lymphocyte methionine
            adenosyltransferase
  JOURNAL   J Biol Chem 270 (37), 21860-21868 (1995)
   PUBMED   7665609
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Horikawa,S. and Tsukada,K.
  TITLE     Molecular cloning and developmental expression of a human kidney
            S-adenosylmethionine synthetase
  JOURNAL   FEBS Lett 312 (1), 37-41 (1992)
   PUBMED   1426236
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Okada,G., Teraoka,H. and Tsukada,K.
  TITLE     Multiple species of mammalian S-adenosylmethionine synthetase.
            Partial purification and characterization
  JOURNAL   Biochemistry 20 (4), 934-940 (1981)
   PUBMED   7213623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC322518.1, BC001686.2 and
            AC016753.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene catalyzes the production
            of S-adenosylmethionine (AdoMet) from methionine and ATP. AdoMet is
            the key methyl donor in cellular processes. [provided by RefSeq,
            Jun 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.267421.1,
                                           SRR3476690.387103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306434.8/ ENSP00000303147.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..395
                     /product="S-adenosylmethionine synthase isoform type-2"
                     /EC_number="2.5.1.6"
                     /note="methionine adenosyltransferase II, alpha; MAT 2;
                     MAT-II; adoMet synthetase 2; methionine
                     adenosyltransferase 2; adoMet synthase 2; testicular
                     tissue protein Li 121"
                     /calculated_mol_wt=43530
     Region          16..395
                     /region_name="PTZ00104"
                     /note="S-adenosylmethionine synthase; Provisional"
                     /db_xref="CDD:240268"
     Site            order(19..21,23,57,59,61,66,68..70,134..137,139,181,183,
                     185,202,204,243,246,257..259,261..264,267,272..279,281,
                     285,317,319..323,328..329,331)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:350837"
     Site            order(23,29..31,55,70,113,116..117,133..134,179,181,206,
                     247,249..250,252,258,264..265,279..281,285,289,291,322)
                     /site_type="active"
                     /db_xref="CDD:350837"
     Site            order(23,29..30,179,181,265)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350837"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31153.1)"
     Region          113..125
                     /region_name="Flexible loop.
                     /evidence=ECO:0000250|UniProtKB:P0A817"
                     /note="propagated from UniProtKB/Swiss-Prot (P31153.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P31153.1)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31153.1)"
     CDS             1..395
                     /gene="MAT2A"
                     /gene_synonym="MATA2; MATII; SAMS2"
                     /coded_by="NM_005911.6:121..1308"
                     /db_xref="CCDS:CCDS1977.1"
                     /db_xref="GeneID:4144"
                     /db_xref="HGNC:HGNC:6904"
                     /db_xref="MIM:601468"
ORIGIN      
        1 mngqlngfhe afieegtflf tsesvgeghp dkicdqisda vldahlqqdp dakvacetva
       61 ktgmillage itsraavdyq kvvreavkhi gyddsskgfd yktcnvlval eqqspdiaqg
      121 vhldrneedi gagdqglmfg yatdeteecm pltivlahkl naklaelrrn gtlpwlrpds
      181 ktqvtvqymq drgavlpirv htivisvqhd eevcldemrd alkekvikav vpakyldedt
      241 iyhlqpsgrf viggpqgdag ltgrkiivdt yggwgahggg afsgkdytkv drsaayaarw
      301 vakslvkggl crrvlvqvsy aigvshplsi sifhygtsqk serelleivk knfdlrpgvi
      361 vrdldlkkpi yqrtaayghf grdsfpwevp kklky
//
LOCUS       NP_001277136             423 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-decapping enzyme 1A isoform e [Homo sapiens].
ACCESSION   NP_001277136 XP_005278417
VERSION     NP_001277136.1
DBSOURCE    REFSEQ: accession NM_001290207.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Wu,H., Zhang,J., Bai,Y., Zhang,S., Zhang,Z., Tong,W., Han,P.,
            Fu,B., Zhang,Y. and Shen,Z.
  TITLE     DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma
  JOURNAL   Aging (Albany NY) 13 (19), 23020-23035 (2021)
   PUBMED   34609335
  REMARK    GeneRIF: DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Leonard,D., Ajuh,P., Lamond,A.I. and Legerski,R.J.
  TITLE     hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA
            splicing
  JOURNAL   Biochem Biophys Res Commun 308 (4), 793-801 (2003)
   PUBMED   12927788
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Ingelfinger,D., Arndt-Jovin,D.J., Luhrmann,R. and Achsel,T.
  TITLE     The human LSm1-7 proteins colocalize with the mRNA-degrading
            enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
  JOURNAL   RNA 8 (12), 1489-1501 (2002)
   PUBMED   12515382
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
  REMARK    GeneRIF: These data suggest that a human decapping complex
            containing decapping enzymes hDcp1a and hDcp2 may be recruited to
            mRNAs containing premature termination codons by the hUpf proteins.
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Callebaut,I.
  TITLE     An EVH1/WH1 domain as a key actor in TGFbeta signalling
  JOURNAL   FEBS Lett 519 (1-3), 178-180 (2002)
   PUBMED   12023040
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Bai,R.Y., Koester,C., Ouyang,T., Hahn,S.A., Hammerschmidt,M.,
            Peschel,C. and Duyster,J.
  TITLE     SMIF, a Smad4-interacting protein that functions as a co-activator
            in TGFbeta signalling
  JOURNAL   Nat Cell Biol 4 (3), 181-190 (2002)
   PUBMED   11836524
  REMARK    GeneRIF: Overexpression of wild-type SMIF enhanced expression of
            TGFbeta/BMP regulated genes, whereas a dominant-negative SMIF
            mutant suppressed expression.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC371232.1, AA129009.1,
            AK295205.1, AC112218.2 and CD676826.1.
            
            On Mar 1, 2014 this sequence version replaced XP_005278417.1.
            
            Summary: Decapping is a key step in general and regulated mRNA
            decay. The protein encoded by this gene is a decapping enzyme. This
            protein and another decapping enzyme form a decapping complex,
            which interacts with the nonsense-mediated decay factor hUpf1 and
            may be recruited to mRNAs containing premature termination codons.
            This protein also participates in the TGF-beta signaling pathway.
            Alternative splicing of this gene results in multiple transcript
            variants. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (5) lacks an alternate internal
            exon in the 5' region, and it thus differs in its 5' UTR and
            initiates translation at a downstream in-frame start codon, and it
            also lacks an alternate in-frame exon in the central coding region,
            compared to variant 1. The encoded isoform (e) is shorter at the
            N-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..423
                     /product="mRNA-decapping enzyme 1A isoform e"
                     /EC_number="3.6.1.62"
                     /note="transcription factor SMIF; Smad4-interacting
                     transcriptional co-activator; mRNA-decapping enzyme 1A;
                     decapping enzyme hDcp1a; putative protein product of
                     Nbla00360; DCP1 decapping enzyme homolog A; DCP1 decapping
                     enzyme-like protein A"
                     /calculated_mol_wt=45176
     Region          380..422
                     /region_name="mRNA_decap_C"
                     /note="mRNA-decapping enzyme C-terminus; pfam16741"
                     /db_xref="CDD:465253"
     CDS             1..423
                     /gene="DCP1A"
                     /gene_synonym="HSA275986; Nbla00360; SMAD4IP1; SMIF"
                     /coded_by="NM_001290207.2:262..1533"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:55802"
                     /db_xref="HGNC:HGNC:18714"
                     /db_xref="MIM:607010"
ORIGIN      
        1 madvveeetr rsqqaardkq spsqangcsd hrpidileml srakdeyers apsghkhltv
       61 eelfgtslpk eqpavvglds eemerlpgda sqkepnsflp fpfeqlggap qsetlgvpsa
      121 ahhsvqpeit tpvlitpasi tqsnekhapt ytiplspvls ptlpaeapta qvppslprns
      181 tmmqavkttp rqrspllnqp vpelshasli anqspfrapl nvtntagtsl psvdllqklr
      241 ltpqhdqiqt qplgkgamva sfspaagqla tpesfiepps ktaaarvaas aslsnmvlap
      301 lqsmqqnqdp evfvqpkvls saipvagapl vtatttavss vllapsvfqq tvtrssdler
      361 kasspsplti gtpesqrkps iilsksqlqd tlihliknds sflstlhevy lqvltknkdn
      421 hnl
//
LOCUS       NP_006658                195 aa            linear   PRI 20-NOV-2025
DEFINITION  membrane-associated progesterone receptor component 1 isoform 1
            [Homo sapiens].
ACCESSION   NP_006658
VERSION     NP_006658.1
DBSOURCE    REFSEQ: accession NM_006667.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Guan,A., Dai,Z., Jiang,C., Sun,J., Yang,B., Xie,B. and Chen,Q.
  TITLE     PGRMC1 promotes NSCLC stemness phenotypes by disrupting
            TRIM56-mediated ubiquitination of AHR
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (7), 167440 (2024)
   PUBMED   39059592
  REMARK    GeneRIF: PGRMC1 promotes NSCLC stemness phenotypes by disrupting
            TRIM56-mediated ubiquitination of AHR.
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Wang,F., Ferreira,L.M.R., Mazzanti,A., Yu,H., Gu,B., Meissner,T.B.,
            Li,Q. and Strominger,J.L.
  TITLE     Progesterone-mediated remodeling of the maternal-fetal interface by
            a PGRMC1-dependent mechanism
  JOURNAL   J Reprod Immunol 163, 104244 (2024)
   PUBMED   38555747
  REMARK    GeneRIF: Progesterone-mediated remodeling of the maternal-fetal
            interface by a PGRMC1-dependent mechanism.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Badve,P. and Meier,K.K.
  TITLE     Defining Requirements for Heme Binding in PGRMC1 and Identifying
            Key Elements that Influence Protein Dimerization
  JOURNAL   Biochemistry 63 (7), 926-938 (2024)
   PUBMED   38489495
  REMARK    GeneRIF: Defining Requirements for Heme Binding in PGRMC1 and
            Identifying Key Elements that Influence Protein Dimerization.
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Liu,H., Franken,A., Bielfeld,A.P., Fehm,T., Niederacher,D.,
            Cheng,Z., Neubauer,H. and Stamm,N.
  TITLE     Progesterone-induced progesterone receptor membrane component 1
            rise-to-decline changes are essential for decidualization
  JOURNAL   Reprod Biol Endocrinol 22 (1), 20 (2024)
   PUBMED   38308254
  REMARK    GeneRIF: Progesterone-induced progesterone receptor membrane
            component 1 rise-to-decline changes are essential for
            decidualization.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Hand,R.A. and Craven,R.J.
  TITLE     Hpr6.6 protein mediates cell death from oxidative damage in MCF-7
            human breast cancer cells
  JOURNAL   J Cell Biochem 90 (3), 534-547 (2003)
   PUBMED   14523988
  REMARK    GeneRIF: Hpr6.6 regulates cell death through a novel oxidative
            damage response pathway.
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Shin,B.K., Wang,H., Yim,A.M., Le Naour,F., Brichory,F., Jang,J.H.,
            Zhao,R., Puravs,E., Tra,J., Michael,C.W., Misek,D.E. and
            Hanash,S.M.
  TITLE     Global profiling of the cell surface proteome of cancer cells
            uncovers an abundance of proteins with chaperone function
  JOURNAL   J Biol Chem 278 (9), 7607-7616 (2003)
   PUBMED   12493773
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Bernauer,S., Wehling,M., Gerdes,D. and Falkenstein,E.
  TITLE     The human membrane progesterone receptor gene: genomic structure
            and promoter analysis
  JOURNAL   DNA Seq 12 (1), 13-25 (2001)
   PUBMED   11697142
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Gerdes,D., Wehling,M., Leube,B. and Falkenstein,E.
  TITLE     Cloning and tissue expression of two putative steroid membrane
            receptors
  JOURNAL   Biol Chem 379 (7), 907-911 (1998)
   PUBMED   9705155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004835.2 and Y12711.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a putative membrane-associated
            progesterone steroid receptor. The protein is expressed
            predominantly in the liver and kidney. [provided by RefSeq, Mar
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y12711.2, BC034238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217971.8/ ENSP00000217971.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..195
                     /product="membrane-associated progesterone receptor
                     component 1 isoform 1"
                     /note="progesterone binding protein; membrane-associated
                     progesterone receptor component 1"
                     /calculated_mol_wt=21540
     Site            25..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00264.3)"
     Region          51..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00264.3)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00264.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00264.3)"
     Region          74..137
                     /region_name="Cyt-b5"
                     /note="Cytochrome b5-like Heme/Steroid binding domain;
                     pfam00173"
                     /db_xref="CDD:459698"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00264.3)"
     Region          173..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00264.3)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00264.3)"
     CDS             1..195
                     /gene="PGRMC1"
                     /gene_synonym="Dap1; HPR6.6; IZA; MPR"
                     /coded_by="NM_006667.5:80..667"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14576.1"
                     /db_xref="GeneID:10857"
                     /db_xref="HGNC:HGNC:16090"
                     /db_xref="MIM:300435"
ORIGIN      
        1 maaedvvatg adpsdlesgg llheiftspl nllllglcif llykivrgdq paasgdsddd
       61 eppplprlkr rdftpaelrr fdgvqdpril maingkvfdv tkgrkfygpe gpygvfagrd
      121 asrglatfcl dkealkdeyd dlsdltaaqq etlsdwesqf tfkyhhvgkl lkegeeptvy
      181 sdeeepkdes arknd
//
LOCUS       NP_803182                606 aa            linear   PRI 20-NOV-2025
DEFINITION  melanoma-associated antigen D2 [Homo sapiens].
ACCESSION   NP_803182
VERSION     NP_803182.1
DBSOURCE    REFSEQ: accession NM_177433.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Yan,X., Hu,Y., Zhang,X., Gao,X., Zhao,Y., Peng,H., Ouyang,L. and
            Zhang,C.
  TITLE     Identification of a novel intronic mutation of MAGED2 gene in a
            Chinese family with antenatal Bartter syndrome
  JOURNAL   BMC Med Genomics 17 (1), 23 (2024)
   PUBMED   38238844
  REMARK    GeneRIF: Identification of a novel intronic mutation of MAGED2 gene
            in a Chinese family with antenatal Bartter syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Shi,X., Liu,C., Zheng,W., Cao,X., Li,W., Zhang,D., Zhu,J., Zhang,X.
            and Chen,Y.
  TITLE     Proteomic Analysis Revealed the Potential Role of MAGE-D2 in the
            Therapeutic Targeting of Triple-Negative Breast Cancer
  JOURNAL   Mol Cell Proteomics 23 (1), 100703 (2024)
   PUBMED   38128647
  REMARK    GeneRIF: Proteomic Analysis Revealed the Potential Role of MAGE-D2
            in the Therapeutic Targeting of Triple-Negative Breast Cancer.
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Nasrah,S., Radi,A., Daberkow,J.K., Hummler,H., Weber,S.,
            Seaayfan,E. and Komhoff,M.
  TITLE     MAGED2 Depletion Promotes Stress-Induced Autophagy by Impairing the
            cAMP/PKA Pathway
  JOURNAL   Int J Mol Sci 24 (17), 13433 (2023)
   PUBMED   37686237
  REMARK    GeneRIF: MAGED2 Depletion Promotes Stress-Induced Autophagy by
            Impairing the cAMP/PKA Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Seaayfan,E., Nasrah,S., Quell,L., Radi,A., Kleim,M.,
            Schermuly,R.T., Weber,S., Laghmani,K. and Komhoff,M.
  TITLE     Reciprocal Regulation of MAGED2 and HIF-1alpha Augments Their
            Expression under Hypoxia: Role of cAMP and PKA Type II
  JOURNAL   Cells 11 (21), 3424 (2022)
   PUBMED   36359819
  REMARK    GeneRIF: Reciprocal Regulation of MAGED2 and HIF-1alpha Augments
            Their Expression under Hypoxia: Role of cAMP and PKA Type II.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Harper,R., Xu,C., Di,P., Chen,Y., Privalsky,M. and Wu,R.
  TITLE     Identification of a novel MAGE D2 antisense RNA transcript in human
            tissues
  JOURNAL   Biochem Biophys Res Commun 324 (1), 199-204 (2004)
   PUBMED   15465002
  REMARK    GeneRIF: Results identified a cDNA clone, corresponding to MAGE D2
            mRNA, from primary human bronchial epithelial cells which exhibits
            increased expression in vitro after treatment with all-trans
            retinoic acid.
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Bertrand,M., Huijbers,I., Chomez,P. and De Backer,O.
  TITLE     Comparative expression analysis of the MAGED genes during
            embryogenesis and brain development
  JOURNAL   Dev Dyn 230 (2), 325-334 (2004)
   PUBMED   15162511
  REMARK    GeneRIF: Maged2 is mainly expressed in tissues of mesodermal origin
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Langnaese,K., Kloos,D.U., Wehnert,M., Seidel,B. and Wieacker,P.
  TITLE     Expression pattern and further characterization of human MAGED2 and
            identification of rodent orthologues
  JOURNAL   Cytogenet Cell Genet 94 (3-4), 233-240 (2001)
   PUBMED   11856887
  REMARK    GeneRIF: Expression pattern and further characterization of human
            MAGED2 and identification of rodent orthologues
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Kurt,R.A., Urba,W.J. and Schoof,D.D.
  TITLE     Isolation of genes overexpressed in freshly isolated breast cancer
            specimens
  JOURNAL   Breast Cancer Res Treat 59 (1), 41-48 (2000)
   PUBMED   10752678
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Lucas,S., Brasseur,F. and Boon,T.
  TITLE     A new MAGE gene with ubiquitous expression does not code for known
            MAGE antigens recognized by T cells
  JOURNAL   Cancer Res 59 (16), 4100-4103 (1999)
   PUBMED   10463614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB467873.1, BC000304.2 and
            BX647995.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the MAGED gene family. The MAGED
            genes are clustered on chromosome Xp11. This gene is located in
            Xp11.2, a hot spot for X-linked intellectual disability (XLID).
            Mutations in this gene cause a form of transient antenatal
            Bartter's syndrome. This gene may also be involved in several types
            of cancer, including breast cancer and melanoma. The protein
            encoded by this gene is progressively recruited from the cytoplasm
            to the nucleoplasm during the interphase and after nucleolar stress
            and is thus thought to play a role in cell cycle regulation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (2) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.817157.1,
                                           SRR3476690.943828.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375068.6/ ENSP00000364209.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.21"
     Protein         1..606
                     /product="melanoma-associated antigen D2"
                     /note="MAGE-D2 antigen; breast cancer-associated gene 1
                     protein; hepatocellular carcinoma-associated protein
                     JCL-1; melanoma antigen family D, 2; melanoma antigen
                     family D2"
                     /calculated_mol_wt=64823
     Region          1..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          <11..161
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          248..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     Region          286..454
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     Region          534..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF1.2)"
     CDS             1..606
                     /gene="MAGED2"
                     /gene_synonym="11B6; BARTS5; BCG-1; BCG1; HCA10; MAGE-D2"
                     /coded_by="NM_177433.3:88..1908"
                     /db_xref="CCDS:CCDS14362.1"
                     /db_xref="GeneID:10916"
                     /db_xref="HGNC:HGNC:16353"
                     /db_xref="MIM:300470"
ORIGIN      
        1 msdtsesgag ltrfqaease kdsssmmqtl ltvtqnvevp etpkaskale vsedvkvska
       61 sgvskatevs ktpeareapa tqassttqlt dtqvlaaenk slaadtkkqn adpqavtmpa
      121 tetkkvshva dtkvntkaqe teaapsqapa depepesaaa qsqenqdtrp kvkakkarkv
      181 khldgeedgs sdqsqasgtt ggrrvskalm asmarrasrg piafwarras rtrlaawarr
      241 allslrspka rrgkarrraa klqssqepea ppprdvallq grandlvkyl lakdqtkipi
      301 krsdmlkdii keytdvypei ieragyslek vfgiqlkeid kndhlyills tleptdagil
      361 gttkdspklg llmvllsiif mngnrsseav iwevlrklgl rpgihhslfg dvkklitdef
      421 vkqkyldyar vpnsnppeye ffwglrsyye tskmkvlkfa ckvqkkdpke waaqyreame
      481 adlkaaaeaa aeakaraeir armgiglgse naagpcnwde adigpwakar iqagaeakak
      541 aqesgsastg aststnnsas asastsggfs agasltatlt fglfaglgga gastsgssga
      601 cgfsyk
//
LOCUS       NP_001116436             849 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 3B
            isoform 1 [Homo sapiens].
ACCESSION   NP_001116436
VERSION     NP_001116436.3
DBSOURCE    REFSEQ: accession NM_001122964.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 849)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Kristiansson,K., Perola,M., Tikkanen,E., Kettunen,J., Surakka,I.,
            Havulinna,A.S., Stancakova,A., Barnes,C., Widen,E., Kajantie,E.,
            Eriksson,J.G., Viikari,J., Kahonen,M., Lehtimaki,T.,
            Raitakari,O.T., Hartikainen,A.L., Ruokonen,A., Pouta,A., Jula,A.,
            Kangas,A.J., Soininen,P., Ala-Korpela,M., Mannisto,S.,
            Jousilahti,P., Bonnycastle,L.L., Jarvelin,M.R., Kuusisto,J.,
            Collins,F.S., Laakso,M., Hurles,M.E., Palotie,A., Peltonen,L.,
            Ripatti,S. and Salomaa,V.
  TITLE     Genome-wide screen for metabolic syndrome susceptibility Loci
            reveals strong lipid gene contribution but no evidence for common
            genetic basis for clustering of metabolic syndrome traits
  JOURNAL   Circ Cardiovasc Genet 5 (2), 242-249 (2012)
   PUBMED   22399527
REFERENCE   5  (residues 1 to 849)
  AUTHORS   Chen,G.I., Tisayakorn,S., Jorgensen,C., D'Ambrosio,L.M.,
            Goudreault,M. and Gingras,A.C.
  TITLE     PP4R4/KIAA1622 forms a novel stable cytosolic complex with
            phosphoprotein phosphatase 4
  JOURNAL   J Biol Chem 283 (43), 29273-29284 (2008)
   PUBMED   18715871
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Chowdhury,D., Xu,X., Zhong,X., Ahmed,F., Zhong,J., Liao,J.,
            Dykxhoorn,D.M., Weinstock,D.M., Pfeifer,G.P. and Lieberman,J.
  TITLE     A PP4-phosphatase complex dephosphorylates gamma-H2AX generated
            during DNA replication
  JOURNAL   Mol Cell 31 (1), 33-46 (2008)
   PUBMED   18614045
  REMARK    GeneRIF: A three-protein PP4 phosphatase complex in mammalian
            cells, containing PP4C, PP4R2, and PP4R3beta, specifically
            dephosphorylates ATR-mediated gamma-H2AX generated during DNA
            replication.
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 849)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   9  (residues 1 to 849)
  AUTHORS   Mendoza,M.C., Du,F., Iranfar,N., Tang,N., Ma,H., Loomis,W.F. and
            Firtel,R.A.
  TITLE     Loss of SMEK, a novel, conserved protein, suppresses MEK1 null cell
            polarity, chemotaxis, and gene expression defects
  JOURNAL   Mol Cell Biol 25 (17), 7839-7853 (2005)
   PUBMED   16107728
REFERENCE   10 (residues 1 to 849)
  AUTHORS   Kittler,R., Putz,G., Pelletier,L., Poser,I., Heninger,A.K.,
            Drechsel,D., Fischer,S., Konstantinova,I., Habermann,B.,
            Grabner,H., Yaspo,M.L., Himmelbauer,H., Korn,B., Neugebauer,K.,
            Pisabarro,M.T. and Buchholz,F.
  TITLE     An endoribonuclease-prepared siRNA screen in human cells identifies
            genes essential for cell division
  JOURNAL   Nature 432 (7020), 1036-1040 (2004)
   PUBMED   15616564
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            KF510821.1 and AC015982.9.
            
            On Nov 29, 2018 this sequence version replaced NP_001116436.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.243610.1,
                                           SRR1803613.78145.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616407.2/ ENSP00000483228.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..849
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 3B isoform 1"
                     /note="serine/threonine-protein phosphatase 4 regulatory
                     subunit 3B; SMEK homolog 2, suppressor of mek1"
                     /calculated_mol_wt=97328
     Region          7..>65
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q5MIZ7.2)"
     Region          168..359
                     /region_name="PP4R3"
                     /note="Phosphatase 4 regulatory subunit 3; pfam04802"
                     /db_xref="CDD:461435"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5MIZ7.2)"
     Region          714..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5MIZ7.2)"
     Site            840
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5MIZ7.2)"
     CDS             1..849
                     /gene="PPP4R3B"
                     /gene_synonym="FLFL2; PP4R3B; PSY2; SMEK2; smk1"
                     /coded_by="NM_001122964.3:338..2887"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46289.1"
                     /db_xref="GeneID:57223"
                     /db_xref="HGNC:HGNC:29267"
                     /db_xref="MIM:610352"
ORIGIN      
        1 msdtrrrvkv ytlnedrqwd drgtghvsst yveelkgmsl lvraesdgsl lleskinpnt
       61 ayqkqqdtli vwseaenydl alsfqekagc deiwekicqv qgkdpsvevt qdlideseee
      121 rfeempetsh lidlptceln kleeiadlvt svlsspirre klalaleneg yikkllqlfq
      181 acenlenteg lhhlyeiirg ilflnkatlf evmfsdecim dvvgcleydp alaqpkrhre
      241 fltktakfke vipitdselr qkihqtyrvq yiqdiilptp svfeenflst ltsfiffnkv
      301 eivsmlqede kflsevfaql tdeatdddkr relvnffkef cafsqtlqpq nrdaffktla
      361 klgilpalei vmgmddlqvr saatdifsyl vefspsmvre fvmqeaqqsd ddillinvvi
      421 eqmicdtdpe lggavqlmgl lrtlidpenm lattnkteks eflnffynhc mhvltapllt
      481 ntsedkcekd fflkhyrysw sfictpshsh shstpsssis qdnivgsnkn nticpdnyqt
      541 aqllalilel ltfcvehhty hiknyimnkd llrrvlvlmn skhtflalca lrfmrriigl
      601 kdefynryit kgnlfepvin alldngtryn llnsavielf efirvediks ltahivenfy
      661 kalesieyvq tfkglktkye qekdrqnqkl nsvpsilrsn rfrrdakale edeemwfned
      721 eeeegkavva pvekpkpedd fpdnyekfme tkkakesedk enlpkrtspg gfkftfshsa
      781 saangtnsks vvaqippats ngssskttnl ptsvtatkgs lvglvdypdd eeedeeeess
      841 prkrprlgs
//
LOCUS       NP_001300874             112 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming protein RhoA isoform 4 [Homo sapiens].
ACCESSION   NP_001300874
VERSION     NP_001300874.1
DBSOURCE    REFSEQ: accession NM_001313945.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Piao,J., Su,Z., He,J., Zhu,T., Fan,F., Wang,X., Yang,Z., Zhan,H.
            and Luo,D.
  TITLE     SphK1 deficiency ameliorates the development of atherosclerosis by
            inhibiting the S1P/S1PR3/Rhoa/ROCK pathway
  JOURNAL   Cell Signal 121, 111252 (2024)
   PUBMED   38852936
  REMARK    GeneRIF: SphK1 deficiency ameliorates the development of
            atherosclerosis by inhibiting the S1P/S1PR3/Rhoa/ROCK pathway.
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Hutchins,C.M. and Gorfe,A.A.
  TITLE     Intrinsically Disordered Membrane Anchors of Rheb, RhoA, and DiRas3
            Small GTPases: Molecular Dynamics, Membrane Organization, and
            Interactions
  JOURNAL   J Phys Chem B 128 (27), 6518-6528 (2024)
   PUBMED   38942776
  REMARK    GeneRIF: Intrinsically Disordered Membrane Anchors of Rheb, RhoA,
            and DiRas3 Small GTPases: Molecular Dynamics, Membrane
            Organization, and Interactions.
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Choi,J.H., Jeong,J., Kim,J., You,E., Keum,S., Song,S., Hwang,Y.E.,
            Ji,M., Park,K.S. and Rhee,S.
  TITLE     Genetic disruption of ATAT1 causes RhoA downregulation through
            abnormal truncation of C/EBPbeta
  JOURNAL   BMB Rep 57 (6), 293-298 (2024)
   PUBMED   38835115
  REMARK    GeneRIF: Genetic disruption of ATAT1 causes RhoA downregulation
            through abnormal truncation of C/EBPbeta.
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Fagan,K.P., Oliveira,L. and Pittler,S.J.
  TITLE     Sequence of rho small GTP-binding protein cDNAs from human retina
            and identification of novel 5' end cloning artifacts
  JOURNAL   Exp Eye Res 59 (2), 235-237 (1994)
   PUBMED   7835413
REFERENCE   7  (residues 1 to 112)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   8  (residues 1 to 112)
  AUTHORS   Moscow,J.A., Morrow,C.S., He,R., Mullenbach,G.T. and Cowan,K.H.
  TITLE     Structure and function of the 5'-flanking sequence of the human
            cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)
  JOURNAL   J Biol Chem 267 (9), 5949-5958 (1992)
   PUBMED   1556108
REFERENCE   9  (residues 1 to 112)
  AUTHORS   Cannizzaro,L.A., Madaule,P., Hecht,F., Axel,R., Croce,C.M. and
            Huebner,K.
  TITLE     Chromosome localization of human ARH genes, a ras-related gene
            family
  JOURNAL   Genomics 6 (2), 197-203 (1990)
   PUBMED   2407642
REFERENCE   10 (residues 1 to 112)
  AUTHORS   Yeramian,P., Chardin,P., Madaule,P. and Tavitian,A.
  TITLE     Nucleotide sequence of human rho cDNA clone 12
  JOURNAL   Nucleic Acids Res 15 (4), 1869 (1987)
   PUBMED   3822842
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK307220.1, AC121247.2,
            EL952052.1 and AI269293.1.
            
            Summary: This gene encodes a member of the Rho family of small
            GTPases, which cycle between inactive GDP-bound and active
            GTP-bound states and function as molecular switches in signal
            transduction cascades. Rho proteins promote reorganization of the
            actin cytoskeleton and regulate cell shape, attachment, and
            motility. Overexpression of this gene is associated with tumor cell
            proliferation and metastasis. Multiple alternatively spliced
            variants have been identified. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' region and uses a downstream start codon compared to
            variant 1. The resulting isoform (4) has a shorter N-terminus
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK307220.1, DC357784.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..112
                     /product="transforming protein RhoA isoform 4"
                     /EC_number="3.6.5.2"
                     /note="transforming protein RhoA; oncogene RHO H12;
                     Aplysia ras-related homolog 12; small GTP binding protein
                     RhoA; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=12589
     Region          <1..98
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            36..39
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            79..81
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..112
                     /gene="RHOA"
                     /gene_synonym="ARH12; ARHA; EDFAOB; RHO12; RHOH12"
                     /coded_by="NM_001313945.2:280..618"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:387"
                     /db_xref="HGNC:HGNC:667"
                     /db_xref="MIM:165390"
ORIGIN      
        1 mcfsidspds lenipekwtp evkhfcpnvp iilvgnkkdl rndehtrrel akmkqepvkp
       61 eegrdmanri gafgymecsa ktkdgvrevf ematraalqa rrgkkksgcl vl
//
LOCUS       NP_001271136             860 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 5 isoform 3 [Homo sapiens].
ACCESSION   NP_001271136 XP_005268219
VERSION     NP_001271136.1
DBSOURCE    REFSEQ: accession NM_001284207.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 860)
  AUTHORS   Radko-Juettner,S., Yue,H., Myers,J.A., Carter,R.D., Robertson,A.N.,
            Mittal,P., Zhu,Z., Hansen,B.S., Donovan,K.A., Hunkeler,M.,
            Rosikiewicz,W., Wu,Z., McReynolds,M.G., Roy Burman,S.S.,
            Schmoker,A.M., Mageed,N., Brown,S.A., Mobley,R.J., Partridge,J.F.,
            Stewart,E.A., Pruett-Miller,S.M., Nabet,B., Peng,J., Gray,N.S.,
            Fischer,E.S. and Roberts,C.W.M.
  TITLE     Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing
            SWI/SNF
  JOURNAL   Nature 628 (8007), 442-449 (2024)
   PUBMED   38538798
  REMARK    GeneRIF: Targeting DCAF5 suppresses SMARCB1-mutant cancer by
            stabilizing SWI/SNF.
            Erratum:[Nature. 2024 May;629(8012):E12. doi:
            10.1038/s41586-024-07402-3. PMID: 38684813]
REFERENCE   2  (residues 1 to 860)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 860)
  AUTHORS   Zhang,C., Leng,F., Saxena,L., Hoang,N., Yu,J., Alejo,S., Lee,L.,
            Qi,D., Lu,F., Sun,H. and Zhang,H.
  TITLE     Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and
            CRL4DCAF5 ubiquitin ligase
  JOURNAL   J Biol Chem 294 (2), 476-489 (2019)
   PUBMED   30442713
REFERENCE   4  (residues 1 to 860)
  AUTHORS   Leng,F., Yu,J., Zhang,C., Alejo,S., Hoang,N., Sun,H., Lu,F. and
            Zhang,H.
  TITLE     Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3
            and CRL4DCAF5 ubiquitin ligase
  JOURNAL   Nat Commun 9 (1), 1641 (2018)
   PUBMED   29691401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 860)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   6  (residues 1 to 860)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   7  (residues 1 to 860)
  AUTHORS   Lynch,R.A., Piper,M., Bankier,A., Bhugra,B., Surti,U., Liu,J.,
            Buckler,A., Dear,P.H. and Menon,A.G.
  TITLE     Genomic and functional map of the chromosome 14 t(12;14) breakpoint
            cluster region in uterine leiomyoma
  JOURNAL   Genomics 52 (1), 17-26 (1998)
   PUBMED   9740667
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL831932.2, AB058727.1, BX648006.1, BC136632.1, BC013239.1 and
            BM681039.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005268219.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (3) has a shorter N-terminus than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL831932.2, SRR1660803.180902.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..860
                     /product="DDB1- and CUL4-associated factor 5 isoform 3"
                     /note="breakpoint cluster region protein, uterine
                     leiomyoma, 2; WD repeat-containing protein 22"
                     /calculated_mol_wt=94568
     Region          <10..280
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          22..58
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          64..103
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          108..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          155..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          200..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..860
                     /gene="DCAF5"
                     /gene_synonym="BCRG2; BCRP2; D14S1461E; WDR22"
                     /coded_by="NM_001284207.1:219..2801"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61480.1"
                     /db_xref="GeneID:8816"
                     /db_xref="HGNC:HGNC:20224"
                     /db_xref="MIM:603812"
ORIGIN      
        1 meqaihsrvk piqlkgehhs nifclafnsg ntkvfsggnd eqvilhdves setldvfahe
       61 davyglsvsp vndnifasss ddgrvliwdi resphgepfc lanypsafhs vmfnpveprl
      121 latanskegv glwdirkpqs sllryggnls lqsamsvrfn sngtqllalr rrlppvlydi
      181 hsrlpvfqfd nqgyfnsctm ksccfagdrd qyilsgsddf nlymwripad peaggigrvv
      241 ngafmvlkgh rsivnqvrfn phtymicssg vekiikiwsp ykqpgctgdl dgrieddsrc
      301 lytheeyisl vlnsgsglsh dyanqsvqed prmmaffdsl vrreiegwss dsdsdlsest
      361 ilqlhagvse rsgytdsess aslprspppt vdesadnafh lgplrvtttn tvastpptpt
      421 cedaasrqqr lsalrryqdk rllalsnesd seenvcevel dtdlfprprs pspedessss
      481 ssssssedee elnerrastw qrnamrrrqk ttredkpsap ikptntyige dnydypqikv
      541 ddlsssptss perststlei qpsrasptsd iesverkiyk aykwlrysyi sysnnkdget
      601 slvtgeadeg ragtshkdnp apssskeacl niamaqrnqd lppegcskdt fkeetprtps
      661 ngpghehssh awaevpegts qdtgnsgsve hpfetkklng kalssraeep psppvpkasg
      721 stlnsgsgnc prtqsddsee rsleticanh nngrlhprpp hphnngqnlg elevvayssp
      781 ghsdtdrdns sltgtllhkd ccgsemacet pnagtredpt dtpatdssra vhghsglkrq
      841 rieledtdse nsssekklkt
//
LOCUS       NP_001309431             372 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-1A adrenergic receptor isoform 5 [Homo sapiens].
ACCESSION   NP_001309431
VERSION     NP_001309431.1
DBSOURCE    REFSEQ: accession NM_001322502.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Ren,C., Cui,L., Li,R., Song,X., Li,J., Xi,Q., Zhang,Z. and Zhao,L.
  TITLE     Hsa_circ_0080608 Attenuates Lung Cancer Progression by Functioning
            as a Competitive Endogenous RNA to Regulate the miR-661/ADRA1A
            Pathway
  JOURNAL   Horm Metab Res 55 (12), 876-884 (2023)
   PUBMED   37820700
  REMARK    GeneRIF: Hsa_circ_0080608 Attenuates Lung Cancer Progression by
            Functioning as a Competitive Endogenous RNA to Regulate the
            miR-661/ADRA1A Pathway.
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Su,M., Wang,J., Xiang,G., Do,H.N., Levitz,J., Miao,Y. and
            Huang,X.Y.
  TITLE     Structural basis of agonist specificity of alpha1A-adrenergic
            receptor
  JOURNAL   Nat Commun 14 (1), 4819 (2023)
   PUBMED   37563160
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Chechekhin,V., Ivanova,A., Kulebyakin,K., Sysoeva,V., Naida,D.,
            Arbatsky,M., Basalova,N., Karagyaur,M., Skryabina,M., Efimenko,A.,
            Grigorieva,O., Kalinina,N., Tkachuk,V. and Tyurin-Kuzmin,P.
  TITLE     Alpha1A- and Beta3-Adrenoceptors Interplay in Adipose Multipotent
            Mesenchymal Stromal Cells: A Novel Mechanism of Obesity-Driven
            Hypertension
  JOURNAL   Cells 12 (4), 585 (2023)
   PUBMED   36831252
  REMARK    GeneRIF: Alpha1A- and Beta3-Adrenoceptors Interplay in Adipose
            Multipotent Mesenchymal Stromal Cells: A Novel Mechanism of
            Obesity-Driven Hypertension.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Zhang,J., Fu,X., Lu,Y., Cheng,C., Wang,K., Zhu,Y. and Xie,Q.
  TITLE     Hypermethylation in the promoter region of the ADRA1A gene is
            associated with opioid use disorder in Han Chinese
  JOURNAL   Brain Res 1793, 148050 (2022)
   PUBMED   35964682
  REMARK    GeneRIF: Hypermethylation in the promoter region of the ADRA1A gene
            is associated with opioid use disorder in Han Chinese.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Baranova,T., Podyacheva,E., Zemlyanukhina,T., Berlov,D.,
            Danilova,M., Glotov,O. and Glotov,A.
  TITLE     Vascular Reactions of the Diving Reflex in Men and Women Carrying
            Different ADRA1A Genotypes
  JOURNAL   Int J Mol Sci 23 (16), 9433 (2022)
   PUBMED   36012699
  REMARK    GeneRIF: Vascular Reactions of the Diving Reflex in Men and Women
            Carrying Different ADRA1A Genotypes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Coge,F., Guenin,S.P., Renouard-Try,A., Rique,H., Ouvry,C.,
            Fabry,N., Beauverger,P., Nicolas,J.P., Galizzi,J.P., Boutin,J.A.
            and Canet,E.
  TITLE     Truncated isoforms inhibit [3H]prazosin binding and cellular
            trafficking of native human alpha1A-adrenoceptors
  JOURNAL   Biochem J 343 Pt 1 (Pt 1), 231-239 (1999)
   PUBMED   10493934
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Hirasawa,A., Shibata,K., Horie,K., Takei,Y., Obika,K., Tanaka,T.,
            Muramoto,N., Takagaki,K., Yano,J. and Tsujimoto,G.
  TITLE     Cloning, functional expression and tissue distribution of human
            alpha 1c-adrenoceptor splice variants
  JOURNAL   FEBS Lett 363 (3), 256-260 (1995)
   PUBMED   7737411
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Hoehe,M.R., Berrettini,W.H., Schwinn,D.A. and Hsieh,W.T.
  TITLE     A two-allele PstI RFLP for the alpha-1C adrenergic receptor gene
            (ADRA1C)
  JOURNAL   Hum Mol Genet 1 (5), 349 (1992)
   PUBMED   1363873
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Schwinn,D.A., Lomasney,J.W., Lorenz,W., Szklut,P.J., Fremeau,R.T.
            Jr., Yang-Feng,T.L., Caron,M.G., Lefkowitz,R.J. and Cotecchia,S.
  TITLE     Molecular cloning and expression of the cDNA for a novel alpha
            1-adrenergic receptor subtype
  JOURNAL   J Biol Chem 265 (14), 8183-8189 (1990)
   PUBMED   1970822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289548.1, AC022839.8,
            AK311558.1, AY491778.1, AC015564.13, BX101935.1 and AA568306.1.
            
            Summary: Alpha-1-adrenergic receptors (alpha-1-ARs) are members of
            the G protein-coupled receptor superfamily. They activate mitogenic
            responses and regulate growth and proliferation of many cells.
            There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of
            which signal through the Gq/11 family of G-proteins and different
            subtypes show different patterns of activation. This gene encodes
            alpha-1A-adrenergic receptor. Alternative splicing of this gene
            generates four transcript variants, which encode four different
            isoforms with distinct C-termini but having similar ligand binding
            properties. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY491778.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465415, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..372
                     /product="alpha-1A adrenergic receptor isoform 5"
                     /note="G protein coupled receptor; alpha-1A adrenoceptor;
                     alpha-1A adrenoreceptor; alpha-1C adrenergic receptor"
                     /calculated_mol_wt=40507
     Region          27..304
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          29..53
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320448"
     Region          62..84
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320448"
     Region          100..122
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320448"
     Region          145..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320448"
     Region          182..205
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320448"
     Region          271..293
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320448"
     CDS             1..372
                     /gene="ADRA1A"
                     /gene_synonym="ADRA1C; ADRA1L1; ALPHA1AAR"
                     /coded_by="NM_001322502.1:687..1805"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:148"
                     /db_xref="HGNC:HGNC:277"
                     /db_xref="MIM:104221"
ORIGIN      
        1 mvflsgnasd ssnctqppap vniskaillg vilgglilfg vlgnilvils vachrhlhsv
       61 thyyivnlav adllltstvl pfsaifevlg ywafgrvfcn iwaavdvlcc tasimglcii
      121 sidryigvsy plryptivtq rrglmallcv walslvisig plfgwrqpap edeticqine
      181 epgyvlfsal gsfylplaii lvmycrvyvv akresrglks glktdksdse qvtlrihrkn
      241 apaggsgmas aktkthfsvr llkfsrekka aktlgivvgc fvlcwlpffl vmpigththd
      301 mkpasrprll sllpkegehe thhwscdpls lestpgaqep cltlgftsls sihltkaqiq
      361 hvtvtdtgkt vt
//
LOCUS       NP_001317398             331 aa            linear   PRI 20-NOV-2025
DEFINITION  coatomer subunit epsilon isoform d [Homo sapiens].
ACCESSION   NP_001317398 XP_011525957
VERSION     NP_001317398.1
DBSOURCE    REFSEQ: accession NM_001330469.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Shima,D.T., Scales,S.J., Kreis,T.E. and Pepperkok,R.
  TITLE     Segregation of COPI-rich and anterograde-cargo-rich domains in
            endoplasmic-reticulum-to-Golgi transport complexes
  JOURNAL   Curr Biol 9 (15), 821-824 (1999)
   PUBMED   10469566
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Faulstich,D., Auerbach,S., Orci,L., Ravazzola,M., Wegchingel,S.,
            Lottspeich,F., Stenbeck,G., Harter,C., Wieland,F.T. and
            Tschochner,H.
  TITLE     Architecture of coatomer: molecular characterization of delta-COP
            and protein interactions within the complex
  JOURNAL   J Cell Biol 135 (1), 53-61 (1996)
   PUBMED   8858162
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002985.1 and AC005197.1.
            
            On Aug 29, 2016 this sequence version replaced XP_011525957.1.
            
            Summary: The product of this gene is an epsilon subunit of coatomer
            protein complex. Coatomer is a cytosolic protein complex that binds
            to dilysine motifs and reversibly associates with Golgi
            non-clathrin-coated vesicles. It is required for budding from Golgi
            membranes, and is essential for the retrograde Golgi-to-ER
            transport of dilysine-tagged proteins. Coatomer complex consists of
            at least the alpha, beta, beta', gamma, delta, epsilon and zeta
            subunits. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (4) uses an alternate exon in the
            central coding region compared to isoform a. The encoded isoform
            (d) is longer than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL523498.3, ERR3218370.499643.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..331
                     /product="coatomer subunit epsilon isoform d"
                     /note="coatomer epsilon subunit; epsilon coat protein;
                     coatomer subunit epsilon; coatomer protein complex subunit
                     epsilon; COPI coat complex subunit epsilon"
                     /calculated_mol_wt=36793
     Region          17..328
                     /region_name="Coatomer_E"
                     /note="Coatomer epsilon subunit; pfam04733"
                     /db_xref="CDD:398419"
     Region          238..268
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..331
                     /gene="COPE"
                     /gene_synonym="epsilon-COP"
                     /coded_by="NM_001330469.2:40..1035"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82321.1"
                     /db_xref="GeneID:11316"
                     /db_xref="HGNC:HGNC:2234"
                     /db_xref="MIM:606942"
ORIGIN      
        1 mappapgpas ggsgevdelf dvknafyigs yqqcineaqr vklssperdv erdvflyray
       61 laqrkfgvvl deikpssape lqavrmfady lahesrrdsi vaeldremsr svdvtnttfl
      121 lmaasiylhd qnpdaalral hqgdslewvs spgralhlea qpmeaaspdg rtamtvqill
      181 kldrldlark elkrmqdlde datltqlata wvslatggek lqdayyifqe madkcsptll
      241 llngqaachm aqgrweaaeg llqealdkds gypetlvnli vlsqhlgkpp evtnrylsql
      301 kdahrshpfi keyqakendf drlvlqyaps a
//
LOCUS       NP_001351757             287 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 15 [Homo sapiens].
ACCESSION   NP_001351757
VERSION     NP_001351757.1
DBSOURCE    REFSEQ: accession NM_001364828.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079684.16 and AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.109773.1,
                                           SRR1660805.371089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..287
                     /product="periphilin-1 isoform 15"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=33020
     Region          266..>285
                     /region_name="Lge1_periphilin-like"
                     /note="Eukaryotic transcriptional regulatory protein Lge1,
                     periphilin, and similar proteins; cl13008"
                     /db_xref="CDD:448781"
     CDS             1..287
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001364828.2:84..947"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdgynrl vnivpkkppl ldrpgegsyn ryyshvdyrd
       61 ydegrsfshd rrsgpphrgd esgyrwtrdd hsasrqpeyr dmrdgfrrks fysshyarer
      121 spykrdntff respvgrkds phsrsgssvs srsyspersk sysfhqsqhr nkerpvqslk
      181 tsrdtspssg savssskvld kpsrltekel aeaaskwaae kleksdesnl peiseyeags
      241 taplftdqpe epesntthgi elfedsqltt rskaiasktk eieqvrv
//
LOCUS       NP_004168                289 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-3 isoform 1 [Homo sapiens].
ACCESSION   NP_004168
VERSION     NP_004168.1
DBSOURCE    REFSEQ: accession NM_004177.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Shinozuka,T., Kanda,M., Sato,Y., Shimizu,D., Tanaka,C., Umeda,S.,
            Inokawa,Y., Hattori,N., Hayashi,M., Nakayama,G. and Kodera,Y.
  TITLE     Increased STX3 transcript and protein levels were associated with
            poor prognosis in two independent cohorts of esophageal squamous
            cell carcinoma patients
  JOURNAL   Cancer Med 12 (24), 22185-22195 (2023)
   PUBMED   38014487
  REMARK    GeneRIF: Increased STX3 transcript and protein levels were
            associated with poor prognosis in two independent cohorts of
            esophageal squamous cell carcinoma patients.
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Janecke,A.R., Liu,X., Adam,R., Punuru,S., Viestenz,A., Strauss,V.,
            Laass,M., Sanchez,E., Adachi,R., Schatz,M.P., Saboo,U.S.,
            Mittal,N., Rohrschneider,K., Escher,J., Ganesh,A., Al Zuhaibi,S.,
            Al Murshedi,F., AlSaleem,B., Alfadhel,M., Al Sinani,S.,
            Alkuraya,F.S., Huber,L.A., Muller,T., Heidelberger,R. and Janz,R.
  TITLE     Pathogenic STX3 variants affecting the retinal and intestinal
            transcripts cause an early-onset severe retinal dystrophy in
            microvillus inclusion disease subjects
  JOURNAL   Hum Genet 140 (8), 1143-1156 (2021)
   PUBMED   33974130
  REMARK    GeneRIF: Pathogenic STX3 variants affecting the retinal and
            intestinal transcripts cause an early-onset severe retinal
            dystrophy in microvillus inclusion disease subjects.
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Low,S.H., Vasanji,A., Nanduri,J., He,M., Sharma,N., Koo,M.,
            Drazba,J. and Weimbs,T.
  TITLE     Syntaxins 3 and 4 are concentrated in separate clusters on the
            plasma membrane before the establishment of cell polarity
  JOURNAL   Mol Biol Cell 17 (2), 977-989 (2006)
   PUBMED   16339081
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Riento,K., Galli,T., Jansson,S., Ehnholm,C., Lehtonen,E. and
            Olkkonen,V.M.
  TITLE     Interaction of Munc-18-2 with syntaxin 3 controls the association
            of apical SNAREs in epithelial cells
  JOURNAL   J Cell Sci 111 (Pt 17), 2681-2688 (1998)
   PUBMED   9701566
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Delgrossi,M.H., Breuza,L., Mirre,C., Chavrier,P. and Le Bivic,A.
  TITLE     Human syntaxin 3 is localized apically in human intestinal cells
  JOURNAL   J Cell Sci 110 (Pt 18), 2207-2214 (1997)
   PUBMED   9378770
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125660.1, BC007405.2,
            AP000640.5 and AA858058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The gene is a member of the syntaxin family. The encoded
            protein is targeted to the apical membrane of epithelial cells
            where it forms clusters and is important in establishing and
            maintaining polarity necessary for protein trafficking involving
            vesicle fusion and exocytosis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK125660.1, SRR1660805.201991.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337979.9/ ENSP00000338562.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..289
                     /product="syntaxin-3 isoform 1"
                     /note="syntaxin 3A; syntaxin 3B"
                     /calculated_mol_wt=33024
     Region          34..226
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          194..260
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(222,229,232)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            225
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     Site            264..284
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13277.3)"
     CDS             1..289
                     /gene="STX3"
                     /gene_synonym="DIAR12; MVID2; RDMVID; STX3A"
                     /coded_by="NM_004177.5:231..1100"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7975.1"
                     /db_xref="GeneID:6809"
                     /db_xref="HGNC:HGNC:11438"
                     /db_xref="MIM:600876"
ORIGIN      
        1 mkdrleqlka kqltqdddtd aveiaidnta fmdeffseie etrlnidkis ehveeakkly
       61 siilsapipe pktkddleql tteikkrann vrnklksmek hieedevrss adlrirksqh
      121 svlsrkfvev mtkyneaqvd frerskgriq rqleitgkkt tdeeleemle sgnpaiftsg
      181 iidsqiskqa lseiegrhkd ivrlessike lhdmfmdiam lvenqgemld nielnvmhtv
      241 dhvekardet kkavkyqsqa rkkliiiivl vvvllgilal iiglsvgln
//
LOCUS       NP_001560                712 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001560
VERSION     NP_001560.2
DBSOURCE    REFSEQ: accession NM_001569.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 712)
  AUTHORS   Rao,Z., Ao,G., Zhang,Y., Jiang,Z., Li,L. and Hua,Z.
  TITLE     HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and
            inflammatory response alleviating renal injury in diabetic
            nephropathy
  JOURNAL   Immunobiology 229 (5), 152835 (2024)
   PUBMED   38986278
  REMARK    GeneRIF: HNRNP I promotes IRAK1 degradation to reduce podocyte
            apoptosis and inflammatory response alleviating renal injury in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 712)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   3  (residues 1 to 712)
  AUTHORS   Chen,J.J., Lu,T.Z., Wang,T., Yan,W.H., Zhong,F.Y., Qu,X.H.,
            Gong,X.C., Li,J.G., Tou,F.F., Jiang,L.P. and Han,X.J.
  TITLE     The m6A reader HNRNPC promotes glioma progression by enhancing the
            stability of IRAK1 mRNA through the MAPK pathway
  JOURNAL   Cell Death Dis 15 (6), 390 (2024)
   PUBMED   38830885
  REMARK    GeneRIF: The m6A reader HNRNPC promotes glioma progression by
            enhancing the stability of IRAK1 mRNA through the MAPK pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 712)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   5  (residues 1 to 712)
  AUTHORS   Zhou,M., Liu,Y., Xu,H., Chen,X., Zheng,N., Duan,Z., Ge,Y., Li,D.,
            Lin,T., Zeng,R., Chen,Q. and Li,M.
  TITLE     YTHDC1-Modified m6A Methylation of Hsa_circ_0102678 Promotes
            Keratinocyte Inflammation Induced by Cutibacterium acnes Biofilm
            through Regulating miR-146a/TRAF6 and IRAK1 Axis
  JOURNAL   J Innate Immun 15 (1), 822-835 (2023)
   PUBMED   37903473
  REMARK    GeneRIF: YTHDC1-Modified m6A Methylation of Hsa_circ_0102678
            Promotes Keratinocyte Inflammation Induced by Cutibacterium acnes
            Biofilm through Regulating miR-146a/TRAF6 and IRAK1 Axis.
REFERENCE   6  (residues 1 to 712)
  AUTHORS   Muzio,M., Ni,J., Feng,P. and Dixit,V.M.
  TITLE     IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators
            of IL-1 signaling
  JOURNAL   Science 278 (5343), 1612-1615 (1997)
   PUBMED   9374458
REFERENCE   7  (residues 1 to 712)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   8  (residues 1 to 712)
  AUTHORS   DiDonato,J.A., Hayakawa,M., Rothwarf,D.M., Zandi,E. and Karin,M.
  TITLE     A cytokine-responsive IkappaB kinase that activates the
            transcription factor NF-kappaB
  JOURNAL   Nature 388 (6642), 548-554 (1997)
   PUBMED   9252186
REFERENCE   9  (residues 1 to 712)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 712)
  AUTHORS   Cao,Z., Henzel,W.J. and Gao,X.
  TITLE     IRAK: a kinase associated with the interleukin-1 receptor
  JOURNAL   Science 271 (5252), 1128-1131 (1996)
   PUBMED   8599092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2, L76191.1, BC054000.1,
            BE276817.1 and BC014963.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 5, 2005 this sequence version replaced NP_001560.1.
            
            Summary: This gene encodes the interleukin-1 receptor-associated
            kinase 1, one of two putative serine/threonine kinases that become
            associated with the interleukin-1 receptor (IL1R) upon stimulation.
            This gene is partially responsible for IL1-induced upregulation of
            the transcription factor NF-kappa B. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L76191.1, SRR14038194.2450777.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369980.8/ ENSP00000358997.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..712
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..712
                     /product="interleukin-1 receptor-associated kinase 1
                     isoform 1"
                     /EC_number="2.7.11.1"
                     /note="Pelle homolog"
                     /calculated_mol_wt=76406
     Region          17..100
                     /region_name="Death_IRAK1"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-1; cd08794"
                     /db_xref="CDD:260061"
     Site            order(19..20,22..25,58,67..68,71..77,82)
                     /site_type="other"
                     /note="putative IRAK1-IRAK4 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:260061"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCI.
                     /evidence=ECO:0000269|PubMed:14684752; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          105..187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Region          110..211
                     /region_name="ProST region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by IRAK4.
                     /evidence=ECO:0000305|PubMed:14625308; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          218..521
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(218..221,224,226,237,239,272,288..291,340,344..345,
                     347,357..358)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271061"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14625308; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          <509..>597
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          532..591
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51617.2)"
     Region          613..660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     Region          690..712
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51617.2)"
     CDS             1..712
                     /gene="IRAK1"
                     /gene_synonym="IRAK; pelle"
                     /coded_by="NM_001569.4:91..2229"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14740.1"
                     /db_xref="GeneID:3654"
                     /db_xref="HGNC:HGNC:6112"
                     /db_xref="MIM:300283"
ORIGIN      
        1 maggpgpgep aapgaqhfly evppwvmcrf ykvmdalepa dwcqfaaliv rdqtelrlce
       61 rsgqrtasvl wpwinrnarv adlvhilthl qllrardiit awhppaplps pgttaprpss
      121 ipapaeaeaw sprklpssas tflspafpgs qthsgpelgl vpspaslwpp ppspapsstk
      181 pgpessvsll qgarpfpfcw plceisrgth nfseelkige ggfgcvyrav mrntvyavkr
      241 lkenadlewt avkqsfltev eqlsrfrhpn ivdfagycaq ngfyclvygf lpngsledrl
      301 hcqtqacppl swpqrldill gtaraiqflh qdspslihgd ikssnvllde rltpklgdfg
      361 larfsrfags spsqssmvar tqtvrgtlay lpeeyiktgr lavdtdtfsf gvvvletlag
      421 qravkthgar tkylkdlvee eaeeagvalr stqstlqagl aadawaapia mqiykkhldp
      481 rpgpcppelg lglgqlaccc lhrrakrrpp mtqvyerlek lqavvagvpg hseaascipp
      541 spqensyvss tgrahsgaap wqplaapsga saqaaeqlqr gpnqpvesde slgglsaalr
      601 swhltpscpl dpaplreagc pqgdtagess wgsgpgsrpt aveglalgss asssseppqi
      661 iinparqkmv qklalyedga ldslqllsss slpglgleqd rqgpeesdef qs
//
LOCUS       NP_001349687             222 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 5 isoform 6
            precursor [Homo sapiens].
ACCESSION   NP_001349687 XP_016883626
VERSION     NP_001349687.1
DBSOURCE    REFSEQ: accession NM_001362758.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Ahmed,H.A., Abdelkreem,E., Hamed,E.O., Abo Elmahassen,N.M. and
            Younis,M.A.A.
  TITLE     Frequency of CD40-1C>T polymorphism (rs1883832) and association
            with response to treatment in children with primary immune
            thrombocytopenia
  JOURNAL   Pediatr Blood Cancer 71 (12), e31356 (2024)
   PUBMED   39350313
  REMARK    GeneRIF: Frequency of CD40-1C>T polymorphism (rs1883832) and
            association with response to treatment in children with primary
            immune thrombocytopenia.
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Meng,H., Li,L., Nan,M., Ding,Y., Li,Y. and Zhang,M.
  TITLE     ZG16 enhances the maturation of dendritic cells via induction of
            CD40 and contributes to the antitumor immunity in pancreatic cancer
  JOURNAL   Oncogene 43 (43), 3184-3196 (2024)
   PUBMED   39261658
  REMARK    GeneRIF: ZG16 enhances the maturation of dendritic cells via
            induction of CD40 and contributes to the antitumor immunity in
            pancreatic cancer.
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Aydin,S., Darko,K., Detchou,D. and Barrie,U.
  TITLE     A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40
  JOURNAL   Neurosurg Rev 47 (1), 571 (2024)
   PUBMED   39242402
  REMARK    GeneRIF: A call for clinical trials in glioblastoma multiforme for
            interleukin 4, interleukin 6, interleukin 13 and CD40.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Naseri,S., Cordova,M.M., Wenthe,J., Lovgren,T., Eriksson,E.,
            Loskog,A. and Ullenhag,G.J.
  TITLE     CD40 stimulation via CD40 ligand enhances adenovirus-mediated
            tumour immunogenicity including 'find-me', 'eat-me', and 'kill-me'
            signalling
  JOURNAL   J Cell Mol Med 28 (7), e18162 (2024)
   PUBMED   38494863
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Foy,T.M., Laman,J.D., Ledbetter,J.A., Aruffo,A., Claassen,E. and
            Noelle,R.J.
  TITLE     gp39-CD40 interactions are essential for germinal center formation
            and the development of B cell memory
  JOURNAL   J Exp Med 180 (1), 157-163 (1994)
   PUBMED   7516405
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Banchereau,J., Bazan,F., Blanchard,D., Briere,F., Galizzi,J.P., van
            Kooten,C., Liu,Y.J., Rousset,F. and Saeland,S.
  TITLE     The CD40 antigen and its ligand
  JOURNAL   Annu Rev Immunol 12, 881-922 (1994)
   PUBMED   7516669
  REMARK    Review article
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Stamenkovic,I., Clark,E.A. and Seed,B.
  TITLE     A B-lymphocyte activation molecule related to the nerve growth
            factor receptor and induced by cytokines in carcinomas
  JOURNAL   EMBO J 8 (5), 1403-1410 (1989)
   PUBMED   2475341
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Clark,E.A. and Ledbetter,J.A.
  TITLE     Activation of human B cells mediated through two distinct cell
            surface differentiation antigens, Bp35 and Bp50
  JOURNAL   Proc Natl Acad Sci U S A 83 (12), 4494-4498 (1986)
   PUBMED   3487090
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Paulie,S., Ehlin-Henriksson,B., Mellstedt,H., Koho,H., Ben-Aissa,H.
            and Perlmann,P.
  TITLE     A p50 surface antigen restricted to human urinary bladder
            carcinomas and B lymphocytes
  JOURNAL   Cancer Immunol Immunother 20 (1), 23-28 (1985)
   PUBMED   2998589
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035662.65.
            
            On Apr 26, 2018 this sequence version replaced XP_016883626.1.
            
            Summary: This gene is a member of the TNF-receptor superfamily. The
            encoded protein is a receptor on antigen-presenting cells of the
            immune system and is essential for mediating a broad variety of
            immune and inflammatory responses including T cell-dependent
            immunoglobulin class switching, memory B cell development, and
            germinal center formation. AT-hook transcription factor AKNA is
            reported to coordinately regulate the expression of this receptor
            and its ligand, which may be important for homotypic cell
            interactions. Adaptor protein TNFR2 interacts with this receptor
            and serves as a mediator of the signal transduction. The
            interaction of this receptor and its ligand is found to be
            necessary for amyloid-beta-induced microglial activation, and thus
            is thought to be an early event in Alzheimer disease pathogenesis.
            Mutations affecting this gene are the cause of autosomal recessive
            hyper-IgM immunodeficiency type 3 (HIGM3). Multiple alternatively
            spliced transcript variants of this gene encoding distinct isoforms
            have been reported. [provided by RefSeq, Nov 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.520929.1,
                                           SRR1163658.418638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..222
                     /product="tumor necrosis factor receptor superfamily
                     member 5 isoform 6 precursor"
                     /note="CD40L receptor; B cell-associated molecule; B cell
                     surface antigen CD40; tumor necrosis factor receptor
                     superfamily member 5; CD40 molecule, TNF receptor
                     superfamily member 5"
                     /calculated_mol_wt=22261
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2250
     Region          25..60
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          26..186
                     /region_name="TNFRSF5"
                     /note="Tumor necrosis factor receptor superfamily member 5
                     (TNFRSF5), also known as CD40; cd13407"
                     /db_xref="CDD:276912"
     Region          26..59
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276912"
     Region          61..103
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          62..103
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276912"
     Site            order(65..66,73..74,76..79,82,84,86,119)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276912"
     Region          104..144
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          105..143
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276912"
     Region          145..187
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     Region          146..186
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276912"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25942.1)"
     Site            180
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25942.1)"
     Site            194..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25942.1)"
     CDS             1..222
                     /gene="CD40"
                     /gene_synonym="Bp50; CDW40; p50; TNFRSF5"
                     /coded_by="NM_001362758.2:31..699"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:958"
                     /db_xref="HGNC:HGNC:11919"
                     /db_xref="MIM:109535"
ORIGIN      
        1 mvrlplqcvl wgclltavhp epptacrekq ylinsqccsl cqpgqklvsd cteftetecl
       61 pcgesefldt wnrethchqh kycdpnlglr vqqkgtsetd tictceegwh ctseacescv
      121 lhrscspgfg vkqiatgvsd ticepcpvgf fsnvssafek chpwtscetk dlvvqqagtn
      181 ktdvvcgpqd rlralvvipi ifgilfaill vlvfisgqea nq
//
LOCUS       NP_056126               1896 aa            linear   PRI 20-NOV-2025
DEFINITION  obscurin-like protein 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_056126 XP_001128426 XP_001131592 XP_051017 XP_943597
VERSION     NP_056126.1
DBSOURCE    REFSEQ: accession NM_015311.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1896)
  AUTHORS   Tuysuz,B., Alp Unkar,Z., Turan,H., Gezdirici,A., Uludag Alkaya,D.,
            Kasap,B., Yesil,G., Vural,M. and Ercan,O.
  TITLE     Natural history of facial and skeletal features from neonatal
            period to adulthood in a 3M syndrome cohort with biallelic CUL7 or
            OBSL1 variants
  JOURNAL   Eur J Med Genet 64 (12), 104346 (2021)
   PUBMED   34597859
  REMARK    GeneRIF: Natural history of facial and skeletal features from
            neonatal period to adulthood in a 3M syndrome cohort with biallelic
            CUL7 or OBSL1 variants.
REFERENCE   2  (residues 1 to 1896)
  AUTHORS   Isik,E., Arican,D., Atik,T., Ooi,J.E., Darcan,S., Ozen,S., Simsek
            Kiper,P.O., Utine,E., Cogulu,O. and Ozkinay,F.
  TITLE     A rare cause of syndromic short stature: 3M syndrome in three
            families
  JOURNAL   Am J Med Genet A 185 (2), 461-468 (2021)
   PUBMED   33258289
  REMARK    GeneRIF: A rare cause of syndromic short stature: 3M syndrome in
            three families.
REFERENCE   3  (residues 1 to 1896)
  AUTHORS   Jacob,P. and Girisha,K.M.
  TITLE     Three M syndrome 2 in two Indian patients
  JOURNAL   Am J Med Genet A 185 (2), 614-616 (2021)
   PUBMED   33135300
  REMARK    GeneRIF: Three M syndrome 2 in two Indian patients.
REFERENCE   4  (residues 1 to 1896)
  AUTHORS   Wang,P., Yan,F., Li,Z., Yu,Y., Parnell,S.E. and Xiong,Y.
  TITLE     Impaired plasma membrane localization of ubiquitin ligase complex
            underlies 3-M syndrome development
  JOURNAL   J Clin Invest 129 (10), 4393-4407 (2019)
   PUBMED   31343991
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1896)
  AUTHORS   Simsek-Kiper,P.O., Taskiran,E., Kosukcu,C., Arslan,U.E.,
            Cormier-Daire,V., Gonc,N., Ozon,A., Alikasifoglu,A., Kandemir,N.,
            Utine,G.E., Alanay,Y., Alikasifoglu,M. and Boduroglu,K.
  TITLE     Further expanding the mutational spectrum and investigation of
            genotype-phenotype correlation in 3M syndrome
  JOURNAL   Am J Med Genet A 179 (7), 1157-1172 (2019)
   PUBMED   30980518
  REMARK    GeneRIF: The mutational spectrum of CUL7, OBSL1, and investigation
            of genotype-phenotype correlation in 3M syndrome has been reported.
REFERENCE   6  (residues 1 to 1896)
  AUTHORS   Hanson,D., Murray,P.G., Sud,A., Temtamy,S.A., Aglan,M.,
            Superti-Furga,A., Holder,S.E., Urquhart,J., Hilton,E., Manson,F.D.,
            Scambler,P., Black,G.C. and Clayton,P.E.
  TITLE     The primordial growth disorder 3-M syndrome connects ubiquitination
            to the cytoskeletal adaptor OBSL1
  JOURNAL   Am J Hum Genet 84 (6), 801-806 (2009)
   PUBMED   19481195
  REMARK    GeneRIF: Loss of OBSL1 leads to downregulation of CUL7 and results
            in primordial growth disorder 3-M syndrome.
REFERENCE   7  (residues 1 to 1896)
  AUTHORS   Fukuzawa,A., Lange,S., Holt,M., Vihola,A., Carmignac,V.,
            Ferreiro,A., Udd,B. and Gautel,M.
  TITLE     Interactions with titin and myomesin target obscurin and
            obscurin-like 1 to the M-band: implications for hereditary
            myopathies
  JOURNAL   J Cell Sci 121 (11), 1841-1851 (2008)
   PUBMED   18477606
  REMARK    GeneRIF: N-terminal Ig-domains of Obsl1 and Obscurin (Obsc) bind to
            titin-M10 and myomesin. Titin mutations, linked to limb-girdle
            muscular dystrophy 2J (LGMD2J) or Salih myopathy, weaken or
            abrogate titin-Obsc and titin-Obsl1 binding.
REFERENCE   8  (residues 1 to 1896)
  AUTHORS   Geisler,S.B., Robinson,D., Hauringa,M., Raeker,M.O., Borisov,A.B.,
            Westfall,M.V. and Russell,M.W.
  TITLE     Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to
            obscurin
  JOURNAL   Genomics 89 (4), 521-531 (2007)
   PUBMED   17289344
  REMARK    GeneRIF: report the cloning and characterization of OBSL1; OBSL1 is
            located on human chromosome 2q35 within 100 kb of SPEG, another
            gene related to obscurin
REFERENCE   9  (residues 1 to 1896)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   10 (residues 1 to 1896)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB475523.1, CK904385.1,
            EF063638.1 and F30329.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Apr 9, 2007 this sequence version replaced
            XP_001131592.1, XP_051017.6, XP_001128426.1, XP_943597.2.
            
            Summary: Cytoskeletal adaptor proteins function in linking the
            internal cytoskeleton of cells to the cell membrane. This gene
            encodes a cytoskeletal adaptor protein, which is a member of the
            Unc-89/obscurin family. The protein contains multiple N- and
            C-terminal immunoglobulin (Ig)-like domains and a central
            fibronectin type 3 domain. Mutations in this gene cause 3M syndrome
            type 2. Alternatively spliced transcript variants encoding
            different isoforms have been found in this gene. [provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longest isoform (1, also known as isoform A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF063638.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404537.6/ ENSP00000385636.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1896
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..1896
                     /product="obscurin-like protein 1 isoform 1 precursor"
                     /EC_number="2.7.11.18"
                     /note="obscurin-like protein 1; obscurin like 1"
                     /calculated_mol_wt=203918
     sig_peptide     1..29
                     /calculated_mol_wt=3048
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75147.4)"
     Region          12..88
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          17..19
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          29..33
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     mat_peptide     30..1896
                     /product="obscurin-like protein 1 isoform 1"
                     /calculated_mol_wt=203918
     Region          42..46
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..86
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          85..94
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          106..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          134..226
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          145..149
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          158..162
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          182..196
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          206..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          257..336
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          263..267
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..280
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          302..306
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          316..321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          329..332
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..426
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          358..362
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          371..374
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          395..399
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          409..414
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          518..602
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(518,584,599)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          736..801
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          746..750
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          771..775
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          785..790
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          794..797
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          827..892
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          837..841
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          862..866
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          876..881
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          885..888
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          918..983
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          928..932
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          953..957
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          967..972
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          976..979
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1009..1074
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1019..1023
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1044..1048
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1058..1063
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1067..1070
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1097..1164
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1099..1103
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1111..1115
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1136..1140
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1150..1155
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1159..1162
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1178..1265
                     /region_name="Ig_Semaphorin_C"
                     /note="Immunoglobulin (Ig)-like domain at the C-terminus
                     of semaphorins; cd04979"
                     /db_xref="CDD:409368"
     Region          1178..1184
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409368"
     Region          1188..1196
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409368"
     Site            order(1190,1233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409368"
     Region          1202..1208
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409368"
     Region          1210..1213
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409368"
     Region          1218..1222
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409368"
     Region          1228..1235
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409368"
     Region          1241..1250
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409368"
     Region          1252..1265
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409368"
     Region          1273..1354
                     /region_name="IgI_C2_MyBP-C-like"
                     /note="Domain C2 of human cardiac Myosin Binding Protein C
                     and similar domains; a member of the I-set of IgSF
                     domains; cd20967"
                     /db_xref="CDD:409559"
     Region          1273..1275
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409559"
     Region          1278..1282
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409559"
     Region          1286..1292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409559"
     Region          1299..1304
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409559"
     Region          1307..1310
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409559"
     Region          1315..1320
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409559"
     Region          1323..1328
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409559"
     Region          1337..1343
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409559"
     Region          1346..1354
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409559"
     Region          1361..1444
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1377..1381
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1389..1393
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1414..1418
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1428..1433
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1437..1440
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1451..1522
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1466..1470
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1480..1484
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1505..1509
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1519..1524
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1528..1531
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1541..1624
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1557..1561
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1569..1573
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1594..1598
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1608..1613
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1617..1620
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1631..1714
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1646..1650
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1658..1662
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1683..1687
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1697..1702
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1725..1803
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1736..1740
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1749..1752
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1773..1777
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1815..1893
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          1838..1842
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1863..1867
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1877..1882
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1896
                     /gene="OBSL1"
                     /coded_by="NM_015311.3:308..5998"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS46520.1"
                     /db_xref="GeneID:23363"
                     /db_xref="HGNC:HGNC:29092"
                     /db_xref="MIM:610991"
ORIGIN      
        1 mkassgdqgs ppcflrfprp vrvvsgaeae lkcvvlgepp pvvvwekggq qlaaserlsf
       61 padgaehgll ltaalptdag vyvcrarnaa geayaaaavt vleppasdpe lqpaerplps
      121 pgsgegapvf ltgprsqwvl rgaevvltcr agglpeptly wekdgmalde vwdsshfalq
      181 pgraedgpga slalrilaar lpdsgvyvch arnahghaqa gallqvhqpp esppadpdea
      241 papvveplkc apktfwvneg khakfrcyvm gkpepeiewh wegrpllpdr rrlmyrdrdg
      301 gfvlkvlycq akdrglyvca arnsagqtls avqlhvkepr lrftrplqdv egrehgiavl
      361 eckvpnsrip tawfredqrl lpcrkyeqie egtvrrliih rlkadddgiy lcemrgrvrt
      421 vanvtvkgpi lkrlprkldv legenavllv etleagvegr wsrdgeelpv icqsssghmh
      481 alvlpgvtre dagevtfslg nsrtttllrv kcvkhsppgp pilaemfkgh kntvlltwkp
      541 pepapetpfi yrlerqevgs edwiqcfsie kagavevpgd cvpsegdyrf rictvsghgr
      601 sphvvfhgsa hlvptarlva gledvqvydg edavfsldls tiiqgtwfln geelksnepe
      661 gqvepgalry rieqkglqhr lilhavkhqd sgalvgfscp gvqdsaalti qespvhilsp
      721 qdrvsltftt servvltcel srvdfpatwy kdgqkveese llvvkmdgrk hrlilpeakv
      781 qdsgefecrt egvsaffgvt vqdppvhivd prehvfvhai tsecvmlace vdredapvrw
      841 ykdgqevees dfvvlenegp hrrlvlpatq psdggefqcv agdecayftv titdvsswiv
      901 ypsgkvyvaa vrlervvltc elcrpwaevr wtkdgeevve spalllqked tvrrlvlpav
      961 qledsgeylc eiddesasft vtvteppvri iyprdevtli avtlecvvlm celsredapv
     1021 rwykdgleve esealvlerd gprcrlvlpa aqpedggefv cdagddsaff tvtvtapper
     1081 ivhpaarsld lhfgapgrve lrcevapags qvrwykdgle veasdalqlg aegptrtltl
     1141 phaqpedage yvcetrheai tfnvilaepp vqflalettp splcvapgep vvlscelsra
     1201 gapvvwshng rpvqegegle lhaegprrvl ciqaagpaha glytcqsgaa pgapslsftv
     1261 qvaeppvrvv apeaaqtrvr stpggdlelv vhlsgpggpv rwykdgerla sqgrvqleqa
     1321 garqvlrvqg arsgdageyl cdapqdsrif lvsveepllv klvseltplt vhegddatfr
     1381 cevsppdadv twlrngavvt pgpqvemaqn gssriltlrg cqlgdagtvt lragstatsa
     1441 rlhvretell flrrlqdvra eegqdvclev etgrvgaaga vrwvrggqpl phdsrlsmaq
     1501 dghihrlfih gviladqgty gceshhdrtl arlsvrprql rvlrpledvt iseggsatfq
     1561 lelsqegvtg ewarggvqly pgpkchihsd ghrhrlvlng lgladsgcvs ftadslrcaa
     1621 rlivrevpvt ivrgphdlev tegdtatfec elsqaladvt wekdgnaltp sprlrlqalg
     1681 trrllqlrrc gpsdagtysc avgtaragpv rltvrertva vlselrsvsa regdgatfec
     1741 tvsevettgr welggrplrp garvrirqeg kkhilvlsel raedagevrf qagpaqslal
     1801 levealplqm crhpprektv lvgrravlev tvsrsgghvc wlregaelcp gdkyemrshg
     1861 pthslvihdv rpedqgtycc qagqdsthtr llvegn
//
LOCUS       NP_001193767            1455 aa            linear   PRI 20-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase zeta isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001193767
VERSION     NP_001193767.1
DBSOURCE    REFSEQ: accession NM_001206838.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1455)
  AUTHORS   Wang,Y., Suo,J., Wang,Z., Ran,K., Tian,Y., Han,W., Liu,Y. and
            Peng,X.
  TITLE     The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells modulates
            tumor-associated macrophage polarization
  JOURNAL   Cell Signal 120, 111191 (2024)
   PUBMED   38685521
  REMARK    GeneRIF: The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells
            modulates tumor-associated macrophage polarization.
REFERENCE   2  (residues 1 to 1455)
  AUTHORS   Nagai,K., Muto,Y., Miura,S., Takahashi,K., Naruse,Y., Hiruta,R.,
            Hashimoto,Y., Uzuki,M., Haga,Y., Fujii,R., Ueda,K., Kawaguchi,Y.,
            Fujii,M. and Kitazume,S.
  TITLE     Brain-specific glycosylation enzyme GnT-IX maintains levels of
            protein tyrosine phosphatase receptor PTPRZ, thereby mediating
            glioma growth
  JOURNAL   J Biol Chem 299 (9), 105128 (2023)
   PUBMED   37543361
  REMARK    GeneRIF: Brain-specific glycosylation enzyme GnT-IX maintains
            levels of protein tyrosine phosphatase receptor PTPRZ, thereby
            mediating glioma growth.
REFERENCE   3  (residues 1 to 1455)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1455)
  AUTHORS   Lacore,M.G., Delmas,C., Nicaise,Y., Kowalski-Chauvel,A.,
            Cohen-Jonathan-Moyal,E. and Seva,C.
  TITLE     The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells
  JOURNAL   Cells 11 (14), 2128 (2022)
   PUBMED   35883571
  REMARK    GeneRIF: The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1455)
  AUTHORS   Nagai,K., Fujii,M. and Kitazume,S.
  TITLE     Protein Tyrosine Phosphatase Receptor Type Z in Central Nervous
            System Disease
  JOURNAL   Int J Mol Sci 23 (8), 4414 (2022)
   PUBMED   35457233
  REMARK    GeneRIF: Protein Tyrosine Phosphatase Receptor Type Z in Central
            Nervous System Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1455)
  AUTHORS   Ariyama,T., Hasegawa,K., Inazawa,J., Mizuno,K., Ogimoto,M.,
            Katagiri,T. and Yakura,H.
  TITLE     Assignment of the human protein tyrosine phosphatase,
            receptor-type, zeta (PTPRZ) gene to chromosome band 7q31.3
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 52-54 (1995)
   PUBMED   7736789
REFERENCE   7  (residues 1 to 1455)
  AUTHORS   Levy,J.B., Canoll,P.D., Silvennoinen,O., Barnea,G., Morse,B.,
            Honegger,A.M., Huang,J.T., Cannizzaro,L.A., Park,S.H., Druck,T. et
            al.
  TITLE     The cloning of a receptor-type protein tyrosine phosphatase
            expressed in the central nervous system
  JOURNAL   J Biol Chem 268 (14), 10573-10581 (1993)
   PUBMED   8387522
REFERENCE   8  (residues 1 to 1455)
  AUTHORS   Krueger,N.X. and Saito,H.
  TITLE     A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is
            expressed in brain and has an N-terminal receptor domain homologous
            to carbonic anhydrases
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7417-7421 (1992)
   PUBMED   1323835
REFERENCE   9  (residues 1 to 1455)
  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.
  TITLE     Structural diversity and evolution of human receptor-like protein
            tyrosine phosphatases
  JOURNAL   EMBO J 9 (10), 3241-3252 (1990)
   PUBMED   2170109
REFERENCE   10 (residues 1 to 1455)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA454064.1, U88967.1, M93426.1
            and AK294062.1.
            
            Summary: This gene encodes a member of the receptor protein
            tyrosine phosphatase family. Expression of this gene is restricted
            to the central nervous system (CNS), and it may be involved in the
            regulation of specific developmental processes in the CNS.
            Alternatively spliced transcript variants encoding different
            isoforms have been described for this gene. [provided by RefSeq,
            May 2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            donor splice site at an internal coding exon compared to variant 1.
            This results in a shorter isoform (2) missing an internal protein
            segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.103693.1,
                                           SRR1803615.110224.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.32"
     Protein         1..1455
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 2 precursor"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor-type, zeta
                     polypeptide 1; protein tyrosine phosphatase,
                     receptor-type, Z polypeptide 1; receptor-type tyrosine
                     phosphatase beta/zeta; protein-tyrosine phosphatase
                     receptor type Z polypeptide 2"
                     /calculated_mol_wt=160755
     sig_peptide     1..24
                     /calculated_mol_wt=2837
     mat_peptide     25..1455
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 2"
                     /calculated_mol_wt=160755
     Region          45..298
                     /region_name="alpha_CARP_receptor_like"
                     /note="Carbonic anhydrase alpha related protein,
                     receptor_like subfamily. Carbonic anhydrase related
                     proteins (CARPs) are sequence similar to carbonic
                     anhydrases. Carbonic anhydrases are zinc-containing
                     enzymes that catalyze the reversible hydration of
                     carbon...; cd03122"
                     /db_xref="CDD:239396"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          313..401
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            order(397..398,400..401)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          442..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Region          477..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            587
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          628..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Site            629
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            637
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine,
                     alternate. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q62656; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62656; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            677
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          857..1134
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1217..1420
                     /region_name="R-PTP-Z-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase Z, repeat 2; cd17669"
                     /db_xref="CDD:350507"
     CDS             1..1455
                     /gene="PTPRZ1"
                     /gene_synonym="HPTPZ; HPTPzeta; phosphacan; PTP-ZETA;
                     PTP18; PTPRZ; PTPZ; R-PTP-zeta-2; RPTPB; RPTPbeta"
                     /coded_by="NM_001206838.2:340..4707"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:5803"
                     /db_xref="HGNC:HGNC:9685"
                     /db_xref="MIM:176891"
ORIGIN      
        1 mrilkrflac iqllcvcrld wangyyrqqr klveeigwsy tgalnqknwg kkyptcnspk
       61 qspinidedl tqvnvnlkkl kfqgwdktsl entfihntgk tveinltndy rvsggvsemv
      121 fkaskitfhw gkcnmssdgs ehslegqkfp lemqiycfda drfssfeeav kgkgklrals
      181 ilfevgteen ldfkaiidgv esvsrfgkqa aldpfillnl lpnstdkyyi yngsltsppc
      241 tdtvdwivfk dtvsisesql avfcevltmq qsgyvmlmdy lqnnfreqqy kfsrqvfssy
      301 tgkeeiheav cssepenvqa dpenytsllv twerprvvyd tmiekfavly qqldgedqtk
      361 hefltdgyqd lgailnnllp nmsyvlqiva ictnglygky sdqlivdmpt dnpeldlfpe
      421 ligteeiike eeegkdieeg aivnpgrdsa tnqirkkepq isttthynri gtkyneaktn
      481 rsptrgsefs gkgdvpntsl nstsqpvtkl atekdislts qtvtelppht vegtsaslnd
      541 gsktvlrsph mnlsgtaesl ntvsiteyee eslltsfkld tgaedssgss patsaipfis
      601 enisqgyifs senpetityd vlipesarna sedstssgse eslkdpsmeg nvwfpsstdi
      661 taqpdvgsgr esflqtnyte irvdesektt ksfsagpvms qgpsvtdlem phystfayfp
      721 tevtphaftp ssrqqdlvst vnvvysqttq pvyneasnss hesriglaeg lesekkavip
      781 lvivsaltfi clvvlvgili ywrkcfqtah fyledstspr vistpptpif pisddvgaip
      841 ikhfpkhvad lhassgftee fetlkefyqe vqsctvdlgi tadssnhpdn khknryiniv
      901 aydhsrvkla qlaekdgklt dyinanyvdg ynrpkayiaa qgplkstaed fwrmiwehnv
      961 evivmitnlv ekgrrkcdqy wpadgseeyg nflvtqksvq vlayytvrnf tlrntkikkg
     1021 sqkgrpsgrv vtqyhytqwp dmgvpeyslp vltfvrkaay akrhavgpvv vhcsagvgrt
     1081 gtyivldsml qqiqhegtvn ifgflkhirs qrnylvqtee qyvfihdtlv eailsketev
     1141 ldshihayvn allipgpagk tklekqfqll sqsniqqsdy saalkqcnre knrtssiipv
     1201 ersrvgissl sgegtdyina syimgyyqsn efiitqhpll htikdfwrmi wdhnaqlvvm
     1261 ipdgqnmaed efvywpnkde pincesfkvt lmaeehkcls neekliiqdf ileatqddyv
     1321 levrhfqcpk wpnpdspisk tfelisvike eaanrdgpmi vhdehggvta gtfcalttlm
     1381 hqlekensvd vyqvakminl mrpgvfadie qyqflykvil slvstrqeen pstsldsnga
     1441 alpdgniaes leslv
//
LOCUS       NP_060544                323 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor YJU2 [Homo sapiens].
ACCESSION   NP_060544
VERSION     NP_060544.2
DBSOURCE    REFSEQ: accession NM_018074.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Zhan,X., Yan,C., Zhang,X., Lei,J. and Shi,Y.
  TITLE     Structure of a human catalytic step I spliceosome
  JOURNAL   Science 359 (6375), 537-545 (2018)
   PUBMED   29301961
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Sorrells,S., Carbonneau,S., Harrington,E., Chen,A.T., Hast,B.,
            Milash,B., Pyati,U., Major,M.B., Zhou,Y., Zon,L.I., Stewart,R.A.,
            Look,A.T. and Jette,C.
  TITLE     Ccdc94 protects cells from ionizing radiation by inhibiting the
            expression of p53
  JOURNAL   PLoS Genet 8 (8), e1002922 (2012)
   PUBMED   22952453
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005578.1, AK001236.1 and AC008616.6.
            
            On Jun 9, 2003 this sequence version replaced NP_060544.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.378395.1,
                                           SRR3476690.506129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262962.12/ ENSP00000262962.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..323
                     /product="splicing factor YJU2"
                     /note="coiled-coil domain-containing protein 94;
                     coiled-coil domain containing 94"
                     /calculated_mol_wt=36955
     Region          9..318
                     /region_name="Saf4_Yju2"
                     /note="Saf4/Yju2 protein; pfam04502"
                     /db_xref="CDD:461333"
     Region          207..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW85.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BW85.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BW85.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW85.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D6J3; propagated from
                     UniProtKB/Swiss-Prot (Q9BW85.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D6J3; propagated from
                     UniProtKB/Swiss-Prot (Q9BW85.1)"
     CDS             1..323
                     /gene="YJU2"
                     /gene_synonym="CCDC94"
                     /coded_by="NM_018074.6:68..1039"
                     /db_xref="CCDS:CCDS12124.1"
                     /db_xref="GeneID:55702"
                     /db_xref="HGNC:HGNC:25518"
ORIGIN      
        1 mserkvlnky yppdfdpski pklklpkdrq yvvrlmapfn mrcktcgeyi ykgkkfnark
       61 etvqnevylg lpifrfyikc trclaeitfk tdpentdytm ehgatrnfqa eklleeeekr
      121 vqkeredeel nnpmkvlenr tkdsklemev lenlqelkdl nqrqahvdfe amlrqhrlse
      181 eerrrqqqee deqetaalle earkrrlled sdsedeaaps plqpalrpnp taildeapkp
      241 krkvevweqs vgslgsrppl srlvvvkkak adpdcsngqp qaaptpgapq nrkeanptpl
      301 tpgasslsql gayldsddsn gsn
//
LOCUS       NP_001007564             278 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin-like growth factor-binding protein-like 1 precursor [Homo
            sapiens].
ACCESSION   NP_001007564 XP_294567
VERSION     NP_001007564.1
DBSOURCE    REFSEQ: accession NM_001007563.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Hou,L., Feng,X., Zhu,Z., Mi,Y., He,Q., Yin,K. and Zhao,G.
  TITLE     IGFBPL1 inhibits macrophage lipid accumulation by enhancing the
            activation of IGR1R/LXRalpha/ABCG1 pathway
  JOURNAL   Aging (Albany NY) 15 (24), 14791-14802 (2023)
   PUBMED   38157252
  REMARK    GeneRIF: IGFBPL1 inhibits macrophage lipid accumulation by
            enhancing the activation of IGR1R/LXRalpha/ABCG1 pathway.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Pan,L., Cho,K.S., Wei,X., Xu,F., Lennikov,A., Hu,G., Tang,J.,
            Guo,S., Chen,J., Kriukov,E., Kyle,R., Elzaridi,F., Jiang,S.,
            Dromel,P.A., Young,M., Baranov,P., Do,C.W., Williams,R.W., Chen,J.,
            Lu,L. and Chen,D.F.
  TITLE     IGFBPL1 is a master driver of microglia homeostasis and resolution
            of neuroinflammation in glaucoma and brain tauopathy
  JOURNAL   Cell Rep 42 (8), 112889 (2023)
   PUBMED   37527036
  REMARK    GeneRIF: IGFBPL1 is a master driver of microglia homeostasis and
            resolution of neuroinflammation in glaucoma and brain tauopathy.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Butti,E., Cattaneo,S., Bacigaluppi,M., Cambiaghi,M., Scotti,G.M.,
            Brambilla,E., Ruffini,F., Sferruzza,G., Ripamonti,M., Simeoni,F.,
            Cacciaguerra,L., Zanghi,A., Quattrini,A., Fesce,R.,
            Panina-Bordignon,P., Giannese,F., Cittaro,D., Kuhlmann,T.,
            D'Adamo,P., Rocca,M.A., Taverna,S. and Martino,G.
  TITLE     Neural precursor cells tune striatal connectivity through the
            release of IGFBPL1
  JOURNAL   Nat Commun 13 (1), 7579 (2022)
   PUBMED   36482070
  REMARK    GeneRIF: Neural precursor cells tune striatal connectivity through
            the release of IGFBPL1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Liu,Y., Zhang,M., He,T., Yang,W., Wang,L., Zhang,L. and Guo,M.
  TITLE     Epigenetic silencing of IGFBPL1 promotes esophageal cancer growth
            by activating PI3K-AKT signaling
  JOURNAL   Clin Epigenetics 12 (1), 22 (2020)
   PUBMED   32041673
  REMARK    GeneRIF: Epigenetic silencing of IGFBPL1 promotes esophageal cancer
            growth by activating PI3K-AKT signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Guo,C., Cho,K.S., Li,Y., Tchedre,K., Antolik,C., Ma,J., Chew,J.,
            Utheim,T.P., Huang,X.A., Yu,H., Malik,M.T.A., Anzak,N. and
            Chen,D.F.
  TITLE     IGFBPL1 Regulates Axon Growth through IGF-1-mediated Signaling
            Cascades
  JOURNAL   Sci Rep 8 (1), 2054 (2018)
   PUBMED   29391597
  REMARK    GeneRIF: Expression of IGFBPL1 correlates with RGC axon growth, and
            acute knockdown of IGFBPL1 with shRNA or IGFBPL1 knockout in vivo
            impaired RGC axon growth.  IGFBPL1 binds IGF-1, induces calcium
            signaling mTOR phosphorylation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Kutsukake,M., Ishihara,R., Yoshie,M., Kogo,H. and Tamura,K.
  TITLE     Involvement of insulin-like growth factor-binding protein-related
            protein 1 in decidualization of human endometrial stromal cells
  JOURNAL   Mol Hum Reprod 13 (10), 737-743 (2007)
   PUBMED   17884839
  REMARK    GeneRIF: These results suggest that insulin-like growth
            factor-binding protein-related protein 1 may play a role in
            decidualization of human endometrial stromal cells.
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Smith,P., Nicholson,L.J., Syed,N., Payne,A., Hiller,L., Garrone,O.,
            Occelli,M., Gasco,M. and Crook,T.
  TITLE     Epigenetic inactivation implies independent functions for
            insulin-like growth factor binding protein (IGFBP)-related protein
            1 and the related IGFBPL1 in inhibiting breast cancer phenotypes
  JOURNAL   Clin Cancer Res 13 (14), 4061-4068 (2007)
   PUBMED   17634530
  REMARK    GeneRIF: Expression of IGFBPL1 is regulated by aberrant
            hypermethylation in breast cancer, implying that inactivation of
            these genes is involved in the pathogenesis of this malignancy.
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Cai,Z., Chen,H.T., Boyle,B., Rupp,F., Funk,W.D. and Dedera,D.A.
  TITLE     Identification of a novel insulin-like growth factor binding
            protein gene homologue with tumor suppressor like properties
  JOURNAL   Biochem Biophys Res Commun 331 (1), 261-266 (2005)
   PUBMED   15845387
  REMARK    GeneRIF: IGFBP-RP4 may be a novel putative tumor suppressor
            protein.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL135785.10.
            
            On Nov 29, 2004 this sequence version replaced XP_294567.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.261087.1,
                                           SRR1660803.135280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377694.2/ ENSP00000366923.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.1"
     Protein         1..278
                     /product="insulin-like growth factor-binding protein-like
                     1 precursor"
                     /note="insulin-like growth factor binding protein related
                     protein 4; IGFBP-related protein 10; insulin-like growth
                     factor-binding-related protein 4"
                     /calculated_mol_wt=26290
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WX77.1)"
                     /calculated_mol_wt=2734
     mat_peptide     26..278
                     /product="Insulin-like growth factor-binding protein-like
                     1. /id=PRO_0000297687"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WX77.1)"
                     /calculated_mol_wt=26290
     Region          <114..151
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8WX77.1)"
     Region          169..260
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          185..189
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          226..230
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          240..245
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          254..257
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..278
                     /gene="IGFBPL1"
                     /gene_synonym="bA113O24.1; IGFBP-RP4; IGFBPRP4"
                     /coded_by="NM_001007563.3:31..867"
                     /db_xref="CCDS:CCDS35017.1"
                     /db_xref="GeneID:347252"
                     /db_xref="HGNC:HGNC:20081"
                     /db_xref="MIM:610413"
ORIGIN      
        1 mprlslllpl llllllpllp plspslgird vggrrpkcgp crpegcpapa pcpapgisal
       61 decgccarcl gaegascggr aggrcgpglv casqaagaap egtglcvcaq rgtvcgsdgr
      121 sypsvcalrl rarhtprahp ghlhkardgp cefapvvvvp prsvhnvtga qvglscevra
      181 vptpvitwrk vtkspegtqa leelpgdhvn iavqvrggps dheatawili nplrkedegv
      241 yqchaanmvg eaeshstvtv ldlskyrsfh fpapddrm
//
LOCUS       NP_004271                174 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation elongation factor 1 epsilon-1 isoform 1
            [Homo sapiens].
ACCESSION   NP_004271
VERSION     NP_004271.1
DBSOURCE    REFSEQ: accession NM_004280.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Ding,L., Fang,Y., Li,Y., Hu,Q., Ai,M., Deng,K., Huang,X. and Xin,H.
  TITLE     AIMP3 inhibits cell growth and metastasis of lung adenocarcinoma
            through activating a miR-96-5p-AIMP3-p53 axis
  JOURNAL   J Cell Mol Med 25 (6), 3019-3030 (2021)
   PUBMED   33538115
  REMARK    GeneRIF: AIMP3 inhibits cell growth and metastasis of lung
            adenocarcinoma through activating a miR-96-5p-AIMP3-p53 axis.
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Khan,K., Baleanu-Gogonea,C., Willard,B., Gogonea,V. and Fox,P.L.
  TITLE     3-Dimensional architecture of the human multi-tRNA synthetase
            complex
  JOURNAL   Nucleic Acids Res 48 (15), 8740-8754 (2020)
   PUBMED   32644155
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Kim,C., Park,J.M., Song,Y., Kim,S. and Moon,J.
  TITLE     HIF1alpha-mediated AIMP3 suppression delays stem cell aging via the
            induction of autophagy
  JOURNAL   Aging Cell 18 (2), e12909 (2019)
   PUBMED   30706629
  REMARK    GeneRIF: The AIMP3 enhanced mitochondrial respiration and
            suppressed autophagic activity, indicating that the
            AIMP3-associated modulation of metabolism and autophagy is a key
            mechanism in the senescence of stem cells and further suggesting a
            novel target for interventions against aging.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Tao,Y., Fang,P., Kim,S., Guo,M., Young,N.L. and Marshall,A.G.
  TITLE     Mapping the contact surfaces in the Lamin A:AIMP3 complex by
            hydrogen/deuterium exchange FT-ICR mass spectrometry
  JOURNAL   PLoS One 12 (8), e0181869 (2017)
   PUBMED   28797100
  REMARK    GeneRIF: LmnA binds AIMP3 via its extreme C-terminus. Together
            these findings provide a structural insight for understanding the
            interaction between AIMP3 and LmnA in AIMP3 degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Cho,H.Y., Maeng,S.J., Cho,H.J., Choi,Y.S., Chung,J.M., Lee,S.,
            Kim,H.K., Kim,J.H., Eom,C.Y., Kim,Y.G., Guo,M., Jung,H.S.,
            Kang,B.S. and Kim,S.
  TITLE     Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric
            Glutathione Transferase-homology Domains
  JOURNAL   J Biol Chem 290 (49), 29313-29328 (2015)
   PUBMED   26472928
  REMARK    GeneRIF: analysis of the heterotetrameric complex structure of the
            glutathione transferase (GST) domains shared among the four MSC
            components, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA
            synthetase (EPRS), AIMP2 and AIMP3
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Shiba,K., Stello,T., Motegi,H., Noda,T., Musier-Forsyth,K. and
            Schimmel,P.
  TITLE     Human lysyl-tRNA synthetase accepts nucleotide 73 variants and
            rescues Escherichia coli double-defective mutant
  JOURNAL   J Biol Chem 272 (36), 22809-22816 (1997)
   PUBMED   9278442
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Escalante,C. and Yang,D.C.
  TITLE     Expression of human aspartyl-tRNA synthetase in Escherichia coli.
            Functional analysis of the N-terminal putative amphiphilic helix
  JOURNAL   J Biol Chem 268 (8), 6014-6023 (1993)
   PUBMED   8449960
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005291.1, AF054186.1,
            BG183264.1 and AI374688.1.
            
            Summary: This gene encodes a multifunctional protein that localizes
            to both the cytoplasm and nucleus. In the cytoplasm, the encoded
            protein is an auxiliary component of the macromolecular
            aminoacyl-tRNA synthase complex. However, its mouse homolog has
            been shown to translocate to the nucleus in response to DNA damage,
            and it plays a positive role in ATM/ATR-mediated p53 activation.
            Alternative splicing results in multiple transcript variants.
            Read-through transcription also exists between this gene and the
            neighboring downstream MUTED (muted homolog) gene. An
            EEF1E1-related pseudogene has been identified on chromosome 2.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.45773.1,
                                           SRR1660805.40425.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMN03267753
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379715.10/ ENSP00000369038.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..174
                     /product="eukaryotic translation elongation factor 1
                     epsilon-1 isoform 1"
                     /note="aminoacyl tRNA synthetase complex-interacting
                     multifunctional protein 3; ARS-interacting multifunctional
                     protein 3; p18 component of aminoacyl-tRNA synthetase
                     complex; multisynthase complex auxiliary component p18;
                     multisynthetase complex auxiliary component p18"
                     /calculated_mol_wt=19679
     Region          2..56
                     /region_name="N-terminal"
                     /note="propagated from UniProtKB/Swiss-Prot (O43324.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (O43324.1)"
     Region          57..63
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O43324.1)"
     Region          64..152
                     /region_name="C-terminal"
                     /note="propagated from UniProtKB/Swiss-Prot (O43324.1)"
     Region          65..165
                     /region_name="GST_C_AIMP3"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of Aminoacyl tRNA synthetase
                     complex-Interacting Multifunctional Protein 3; cd10305"
                     /db_xref="CDD:198338"
     Site            order(70,97,100..101,103..107,110..111,140,144,148,165)
                     /site_type="other"
                     /note="putative MetRS interface [polypeptide binding]"
                     /db_xref="CDD:198338"
     Site            order(75,78..79,113..115,118..119,122,157..159)
                     /site_type="other"
                     /note="N-terminal domain interface [polypeptide binding]"
                     /db_xref="CDD:198338"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O43324.1)"
     CDS             1..174
                     /gene="EEF1E1"
                     /gene_synonym="AIMP3; P18"
                     /coded_by="NM_004280.5:28..552"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4507.1"
                     /db_xref="GeneID:9521"
                     /db_xref="HGNC:HGNC:3212"
                     /db_xref="MIM:609206"
ORIGIN      
        1 maaaaelsll ekslglskgn kysaqgerqi pvlqtnngps ltglttiaah lvkqankeyl
       61 lgstaeekai vqqwleyrvt qvdghssknd ihtllkdlns yledkvyltg ynftladill
      121 yyglhrfivd ltvqekekyl nvsrwfchiq hypgirqhls svvfiknrly tnsh
//
LOCUS       NP_056477               1749 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 172 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_056477
VERSION     NP_056477.1
DBSOURCE    REFSEQ: accession NM_015662.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1749)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1749)
  AUTHORS   Neroldova,M., Ciara,E., Slatinska,J., Frankova,S., Liskova,P.,
            Kotalova,R., Globinovska,J., Safarikova,M., Pfeiferova,L.,
            Zunova,H., Mrazova,L., Stranecky,V., Vrbacka,A., Fabian,O.,
            Sticova,E., Skanderova,D., Sperl,J., Kalousova,M., Zima,T.,
            Macek,M., Pawlowska,J., Knisely,A.S., Kmoch,S. and Jirsa,M.
  TITLE     Exome sequencing reveals IFT172 variants in patients with
            non-syndromic cholestatic liver disease
  JOURNAL   PLoS One 18 (7), e0288907 (2023)
   PUBMED   37471416
  REMARK    GeneRIF: Exome sequencing reveals IFT172 variants in patients with
            non-syndromic cholestatic liver disease.
            Erratum:[PLoS One. 2025 Jan 30;20(1):e0318705. doi:
            10.1371/journal.pone.0318705. PMID: 39883651]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1749)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1749)
  AUTHORS   O'Seaghdha,C.M., Yang,Q., Glazer,N.L., Leak,T.S., Dehghan,A.,
            Smith,A.V., Kao,W.H., Lohman,K., Hwang,S.J., Johnson,A.D.,
            Hofman,A., Uitterlinden,A.G., Chen,Y.D., Brown,E.M.,
            Siscovick,D.S., Harris,T.B., Psaty,B.M., Coresh,J., Gudnason,V.,
            Witteman,J.C., Liu,Y.M., Kestenbaum,B.R., Fox,C.S. and Kottgen,A.
  CONSRTM   GEFOS Consortium
  TITLE     Common variants in the calcium-sensing receptor gene are associated
            with total serum calcium levels
  JOURNAL   Hum Mol Genet 19 (21), 4296-4303 (2010)
   PUBMED   20705733
REFERENCE   5  (residues 1 to 1749)
  AUTHORS   Kottgen,A., Pattaro,C., Boger,C.A., Fuchsberger,C., Olden,M.,
            Glazer,N.L., Parsa,A., Gao,X., Yang,Q., Smith,A.V., O'Connell,J.R.,
            Li,M., Schmidt,H., Tanaka,T., Isaacs,A., Ketkar,S., Hwang,S.J.,
            Johnson,A.D., Dehghan,A., Teumer,A., Pare,G., Atkinson,E.J.,
            Zeller,T., Lohman,K., Cornelis,M.C., Probst-Hensch,N.M.,
            Kronenberg,F., Tonjes,A., Hayward,C., Aspelund,T., Eiriksdottir,G.,
            Launer,L.J., Harris,T.B., Rampersaud,E., Mitchell,B.D.,
            Arking,D.E., Boerwinkle,E., Struchalin,M., Cavalieri,M.,
            Singleton,A., Giallauria,F., Metter,J., de Boer,I.H.,
            Haritunians,T., Lumley,T., Siscovick,D., Psaty,B.M.,
            Zillikens,M.C., Oostra,B.A., Feitosa,M., Province,M., de
            Andrade,M., Turner,S.T., Schillert,A., Ziegler,A., Wild,P.S.,
            Schnabel,R.B., Wilde,S., Munzel,T.F., Leak,T.S., Illig,T.,
            Klopp,N., Meisinger,C., Wichmann,H.E., Koenig,W., Zgaga,L.,
            Zemunik,T., Kolcic,I., Minelli,C., Hu,F.B., Johansson,A., Igl,W.,
            Zaboli,G., Wild,S.H., Wright,A.F., Campbell,H., Ellinghaus,D.,
            Schreiber,S., Aulchenko,Y.S., Felix,J.F., Rivadeneira,F.,
            Uitterlinden,A.G., Hofman,A., Imboden,M., Nitsch,D.,
            Brandstatter,A., Kollerits,B., Kedenko,L., Magi,R., Stumvoll,M.,
            Kovacs,P., Boban,M., Campbell,S., Endlich,K., Volzke,H.,
            Kroemer,H.K., Nauck,M., Volker,U., Polasek,O., Vitart,V.,
            Badola,S., Parker,A.N., Ridker,P.M., Kardia,S.L., Blankenberg,S.,
            Liu,Y., Curhan,G.C., Franke,A., Rochat,T., Paulweber,B.,
            Prokopenko,I., Wang,W., Gudnason,V., Shuldiner,A.R., Coresh,J.,
            Schmidt,R., Ferrucci,L., Shlipak,M.G., van Duijn,C.M., Borecki,I.,
            Kramer,B.K., Rudan,I., Gyllensten,U., Wilson,J.F., Witteman,J.C.,
            Pramstaller,P.P., Rettig,R., Hastie,N., Chasman,D.I., Kao,W.H.,
            Heid,I.M. and Fox,C.S.
  TITLE     New loci associated with kidney function and chronic kidney disease
  JOURNAL   Nat Genet 42 (5), 376-384 (2010)
   PUBMED   20383146
REFERENCE   6  (residues 1 to 1749)
  AUTHORS   Howard,P.W. and Maurer,R.A.
  TITLE     Identification of a conserved protein that interacts with specific
            LIM homeodomain transcription factors
  JOURNAL   J Biol Chem 275 (18), 13336-13342 (2000)
   PUBMED   10788441
REFERENCE   7  (residues 1 to 1749)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   8  (residues 1 to 1749)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   9  (residues 1 to 1749)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
REFERENCE   10 (residues 1 to 1749)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC394416.1, BC137126.1 and
            BC047294.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a subunit of the intraflagellar
            transport subcomplex IFT-B. Subcomplexes IFT-A and IFT-B are
            necessary for ciliary assembly and maintenance. Mutations in this
            gene have been associated with skeletal ciliopathies, with or
            without polydactyly, such as such short-rib thoracic dysplasias 1,
            9 or 10. [provided by RefSeq, Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.134858.1,
                                           SRR1803617.133332.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260570.8/ ENSP00000260570.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..1749
                     /product="intraflagellar transport protein 172 homolog
                     isoform 1"
                     /note="wimple homolog; selective LIM binding factor
                     homolog; intraflagellar transport protein 172 homolog;
                     intraflagellar transport 172 homolog"
                     /calculated_mol_wt=197446
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:20388717; propagated from
                     UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          14..53
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          17..318
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          20..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(33,37,43..44,55..56,83,87,93,98,111,127,132,
                     138..139,151,168,173,181..182,195..196,212,216,222..223,
                     234..235,256,261,266..267,276..277,303,314)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          64..103
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          69..110
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          110..148
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          116..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          150..191
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          155..194
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..233
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          200..248
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          238..278
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          284..323
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          483..520
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          521..559
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          593..624
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Site            672
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6VH22; propagated from
                     UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          692..725
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          808..>994
                     /region_name="SNAP"
                     /note="Soluble N-ethylmaleimide-sensitive factor (NSF)
                     Attachment Protein family; cl24038"
                     /db_xref="CDD:451671"
     Region          809..842
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          811..866
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          854..887
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          870..906
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          909..954
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276937"
     Region          912..945
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          947..970
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          971..1004
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1032..>1192
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          1042..1075
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1142..1175
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1155..>1288
                     /region_name="HemYx"
                     /note="Uncharacterized protein HemY, contains HemY_N
                     domain and TPR repeats (unrelated to protoporphyrinogen
                     oxidase HemY) [Function unknown]; COG3071"
                     /db_xref="CDD:442305"
     Region          1276..1309
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1345..1378
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1411..1445
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1447..1477
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     Region          1574..1607
                     /region_name="TPR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UG01.2)"
     CDS             1..1749
                     /gene="IFT172"
                     /gene_synonym="BBS20; NPHP17; osm-1; RP71; SLB; SRTD10;
                     wim"
                     /coded_by="NM_015662.3:91..5340"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1755.1"
                     /db_xref="GeneID:26160"
                     /db_xref="HGNC:HGNC:30391"
                     /db_xref="MIM:607386"
ORIGIN      
        1 mhlkhlrtll spqdgaakvt cmawsqnnak favctvdrvv llydehgerr dkfstkpadm
       61 kygrksymvk gmafspdstk iaigqtdnii yvykigedwg dkkvicnkfi qtsavtclqw
      121 paeyiivfgl aegkvrlant ktnksstiyg tesyvvsltt ncsgkgilsg hadgtivryf
      181 fddegsgesq gklvnhpcpp yalawatnsi vaagcdrkiv aygkeghmlq tfdysrdpqe
      241 refttavssp ggqsvvlgsy drlrvfnwip rrsiweeakp keitnlytit alawkrdgsr
      301 lcvgtlcggv eqfdcclrrs iyknkfelty vgpsqvivkn lssgtrvvlk shygyeveev
      361 kilgkerylv ahtsetlllg dlntnrlsei awqgsggnek yffenenvcm ifnageltlv
      421 eygnndtlgs vrtefmnphl isvrinercq rgtednkkla ylidiktiai vdliggynig
      481 tvshesrvdw lelnetghkl lfrdrklrlh lydiescskt milnfcsymq wvpgsdvlva
      541 qnrnslcvwy nieapervtm ftirgdvigl ergggktevm vmegvttvay tldegliefg
      601 taiddgnyir atafletlem tpeteamwkt lsklalearq lhiaercfsa lgqvakarfl
      661 hetneiadqv sreyggegtd fyqvrarlam leknyklaem ifleqnavee amgmyqelhr
      721 wdeciavaea kghpaleklr rsyyqwlmdt qqeeragelq esqgdglaai slylkaglpa
      781 kaarlvltre ellantelve hitaalikge lyeragdlfe kihnpqkale cyrkgnafmk
      841 avelarlafp vevvkleeaw gdhlvqqkql daainhyiea rcsikaieaa lgarqwkkai
      901 yildlqdrnt askyyplvaq hyaslqeyei aeelytkgdr tkdaidmytq agrweqahkl
      961 amkcmrpedv svlyitqaqe mekqgkyrea erlyvtvqep dlaitmykkh klyddmirlv
     1021 gkhhpdllsd thlhlgkele aegrlqeaey hyleaqewka tvnmyrasgl weeayrvart
     1081 qgganahkhv aylwakslgg eaavrllnkl glleaavdha adncsfefaf elsrlalkhk
     1141 tpevhlkyam fledegkfee aeaefiragk pkeavlmfvh nqdweaaqrv aeahdpdsva
     1201 evlvgqarga leekdfqkae glllraqrpg lalnyykeag lwsdalrick dyvpsqleal
     1261 qeeyereatk kgargvegfv eqarhweqag eysravdcyl kvrdsgnsgl aekcwmkaae
     1321 lsikflppqr nmevvlavgp qligigkhsa aaelylnldl vkeaidafie geewnkakrv
     1381 akeldpryed yvdqhykefl knqgkvdslv gvdviaaldl yveqgqwdkc ietatkqnyk
     1441 ilhkyvalya thliregssa qalalyvqhg apanpqnfni ykriftdmvs spgtncaeay
     1501 hswadlrdvl fnlcenlvks seanspahee fktmlliahy yatrsaaqsv kqletvaarl
     1561 svsllrhtql lpvdkafyea giaakavgwd nmafiflnrf ldltdaieeg tldgldhsdf
     1621 qdtdipfevp lpakqhvpea ereevrdwvl tvsmdqrleq vlprdergay easlvaastg
     1681 vralpclitg ypilrnkief krpgkaankd nwnkflmaik tshspvcqdv lkfisqwcgg
     1741 lpstsfsfq
//
LOCUS       NP_001354490            2140 aa            linear   PRI 20-NOV-2025
DEFINITION  dedicator of cytokinesis protein 7 isoform 7 [Homo sapiens].
ACCESSION   NP_001354490 XP_011540628
VERSION     NP_001354490.1
DBSOURCE    REFSEQ: accession NM_001367561.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2140)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2140)
  AUTHORS   Chen,W., Zhou,M., Guan,B., Xie,B., Liu,Y., He,J., Zhao,J., Zhao,Q.
            and Yan,D.
  TITLE     Tumour-associated macrophage-derived DOCK7-enriched extracellular
            vesicles drive tumour metastasis in colorectal cancer via the
            RAC1/ABCA1 axis
  JOURNAL   Clin Transl Med 14 (2), e1591 (2024)
   PUBMED   38385857
  REMARK    GeneRIF: Tumour-associated macrophage-derived DOCK7-enriched
            extracellular vesicles drive tumour metastasis in colorectal cancer
            via the RAC1/ABCA1 axis.
REFERENCE   4  (residues 1 to 2140)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 2140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 2140)
  AUTHORS   Nellist,M., Burgers,P.C., van den Ouweland,A.M., Halley,D.J. and
            Luider,T.M.
  TITLE     Phosphorylation and binding partner analysis of the TSC1-TSC2
            complex
  JOURNAL   Biochem Biophys Res Commun 333 (3), 818-826 (2005)
   PUBMED   15963462
REFERENCE   7  (residues 1 to 2140)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 2140)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   9  (residues 1 to 2140)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
REFERENCE   10 (residues 1 to 2140)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC103923.2, AL138847.14,
            AL451044.7 and AC096946.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 8, 2018 this sequence version replaced XP_011540628.1.
            
            Summary: The protein encoded by this gene is a guanine nucleotide
            exchange factor (GEF) that plays a role in axon formation and
            neuronal polarization. The encoded protein displays GEF activity
            toward RAC1 and RAC3 Rho small GTPases but not toward CDC42.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Dec 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000635253.2/ ENSP00000489124.1
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..2140
                     /product="dedicator of cytokinesis protein 7 isoform 7"
                     /note="dedicator of cytokinesis protein 7"
                     /calculated_mol_wt=242431
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          52..161
                     /region_name="DOCK_C-D_N"
                     /note="Dedicator of cytokinesis C/D, N terminal;
                     pfam11878"
                     /db_xref="CDD:463380"
     Region          138..183
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            381
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          560..737
                     /region_name="C2_Dock-C"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class C proteins; cd08696"
                     /db_xref="CDD:176078"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          888..971
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            900
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            909
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            964
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R1A4; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            1438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Region          1644..2118
                     /region_name="DHR2_DOCK7"
                     /note="Dock Homology Region 2, a GEF domain, of Class C
                     Dedicator of Cytokinesis 7; cd11703"
                     /db_xref="CDD:212576"
     Site            order(1799,1809,1811..1812,1814..1815,1818..1819,
                     1821..1822,1825..1826)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            order(1841,1843,1866,1869..1872,1874..1875,1894..1896,
                     1913..1915,1943..1946,1956..1957,1960,1962,1999..2000,
                     2003,2019..2020,2022..2023,2026..2028,2031..2033,
                     2036..2037,2040,2068,2090,2093)
                     /site_type="other"
                     /note="Rac/Cdc42 binding site [polypeptide binding]"
                     /db_xref="CDD:212576"
     Site            1962
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     Site            2031..2036
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212576"
     Site            2129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96N67.4)"
     CDS             1..2140
                     /gene="DOCK7"
                     /gene_synonym="DEE23; EIEE23; ZIR2"
                     /coded_by="NM_001367561.1:123..6545"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS90964.1"
                     /db_xref="GeneID:85440"
                     /db_xref="HGNC:HGNC:19190"
                     /db_xref="MIM:615730"
ORIGIN      
        1 maerrafaqk isrtvaaevr kqisgqysgs pqllknlniv gnishhttvp lteavdpvdl
       61 edylithpla vdsgplrdli efppddievv ysprdcrtlv savpeesemd phvrdcirsy
      121 tedwaivirk yhklgtgfnp ntldkqkerq kglpkqvfes deapdgnsyq ddqddlkrrs
      181 msiddtprgs wacsifdlkn slpdallpnl ldrtpneeid rqnddqrksn rhkelfalhp
      241 spdeeepier lsvpdipkeh fgqrllvkcl slkfeieiep ifaslalydv kekkkisenf
      301 yfdlnseqmk gllrphvppa aittlarsai fsitypsqdv flviklekvl qqgdigecae
      361 pymifkeada tknkeklekl ksqadqfcqr lgkyrmpfaw taihlmnivs sagslerdst
      421 eveistgerk gswserrnss ivgrrslert tsgddacnlt sfrpatltvt nffkqegdrl
      481 sdedlykfla dmrrpssvlr rlrpitaqlk idispapenp hycltpellq vklypdsrvr
      541 ptreilefpa rdvyvpntty rnllyiypqs lnfanrqgsa rnitvkvqfm ygedpsnamp
      601 vifgksscse fskeaytavv yhnrspdfhe eikvklpatl tdhhhllftf yhvscqqkqn
      661 tpletpvgyt wipmlqngrl ktgqfclpvs lekppqaysv lspevplpgm kwvdnhkgvf
      721 nvevvavssi htqdpyldkf falvnaldeh lfpvrigdmr imennlenel kssisalnss
      781 qlepvvrflh llldklillv irppviagqi vnlgqasfea masiinrlhk nlegnhdqhg
      841 rnsllasyih yvfrlpntyp nssspgpggl ggsvhyatma rsavrpasln lnrsrslsns
      901 npdisgtpts pddevrsiig skgldrsnsw vntggpkaap wgsnpspsae stqamdrscn
      961 rmsshtetss flqtltgrlp tkklfheela lqwvvcsgsv resalqqawf ffelmvksmv
     1021 hhlyfndkle aprksrfper fmddiaalvs tiasdivsrf qkdtemverl ntslafflnd
     1081 llsvmdrgfv fslikscykq vssklyslpn psvlvslrld flriicsheh yvtlnlpcsl
     1141 ltppaspsps vssatsqssg fstnvqdqki anmfelsvpf rqqhylaglv ltelavildp
     1201 daeglfglhk kvinmvhnll sshdsdprys dpqikarvam lylpligiim etvpqlydft
     1261 ethnqrgrpi ciatddyese sgsmisqtva maiagtsvpq ltrpgsfllt stsgrqhttf
     1321 saessrslli cllwvlknad etvlqkwftd lsvlqlnrll dllylcvscf eykgkkvfer
     1381 mnsltfkksk dmrakleeai lgsigarqem vrrsrgqlgt ytiasppers psgsafgsqe
     1441 nlrwrkdmth wrqntekldk sraeieheal idgnlatean liildtleiv vqtvsvtesk
     1501 esilggvlkv llhsmacnqs avylqhcfat qralvskfpe llfeeeteqc adlclrllrh
     1561 csssigtirs hasaslyllm rqnfeignnf arvkmqvtms lsslvgtsqn fneeflrrsl
     1621 ktiltyaeed lelrettfpd qvqdlvfnlh milsdtvkmk ehqedpemli dlmyriakgy
     1681 qtspdlrltw lqnmagkhse rsnhaeaaqc lvhsaalvae ylsmledrky lpvgcvtfqn
     1741 issnvleesa vsddvvspde egicsgkyft esglvglleq aaasfsmagm yeavnevykv
     1801 lipiheanrd akklstihgk lqeafskivh qstgwermfg tyfrvgfygt kfgdldeqef
     1861 vykepaitkl aeishrlegf ygerfgedvv evikdsnpvd kckldpnkay iqityvepyf
     1921 dtyemkdrit yfdknynlrr fmyctpftld grahgelheq fkrktiltts hafpyiktrv
     1981 nvthkeeiil tpievaiedm qkktqelafa thqdpadpkm lqmvlqgsvg ttvnqgplev
     2041 aqvflseips dpklfrhhnk lrlcfkdftk rcedalrknk sligpdqkey qrelernyhr
     2101 lkealqplin rkipqlykav lpvtchrdsf srmslrkmdl
//
LOCUS       NP_001122099             622 aa            linear   PRI 20-NOV-2025
DEFINITION  protein spire homolog 1 isoform c [Homo sapiens].
ACCESSION   NP_001122099
VERSION     NP_001122099.1
DBSOURCE    REFSEQ: accession NM_001128627.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Li,J., Xiong,N., West,K.L., Leung,M., Ching,Y.P., Huang,J.,
            Yuan,J., Yu,C.H., Leung,J. and Huen,M.
  TITLE     Nuclear F-actin assembly on damaged chromatin is regulated by
            DYRK1A and Spir1 phosphorylation
  JOURNAL   Nucleic Acids Res 52 (15), 8897-8912 (2024)
   PUBMED   38966995
  REMARK    GeneRIF: Nuclear F-actin assembly on damaged chromatin is regulated
            by DYRK1A and Spir1 phosphorylation.
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Scalzitti,S., Mariani,D., Setti,A., Colantoni,A., Lisi,M.,
            Bozzoni,I. and Martone,J.
  TITLE     Lnc-SMaRT Translational Regulation of Spire1, A New Player in
            Muscle Differentiation
  JOURNAL   J Mol Biol 434 (2), 167384 (2022)
   PUBMED   34863993
  REMARK    GeneRIF: Lnc-SMaRT Translational Regulation of Spire1, A New Player
            in Muscle Differentiation.
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Holthenrich,A., Terglane,J., Nass,J., Mietkowska,M., Kerkhoff,E.
            and Gerke,V.
  TITLE     Spire1 and Myosin Vc promote Ca2+-evoked externalization of von
            Willebrand factor in endothelial cells
  JOURNAL   Cell Mol Life Sci 79 (2), 96 (2022)
   PUBMED   35084586
  REMARK    GeneRIF: Spire1 and Myosin Vc promote Ca(2+)-evoked externalization
            of von Willebrand factor in endothelial cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 622)
  AUTHORS   Zeth,K., Pechlivanis,M., Samol,A., Pleiser,S., Vonrhein,C. and
            Kerkhoff,E.
  TITLE     Molecular basis of actin nucleation factor cooperativity: crystal
            structure of the Spir-1 kinase non-catalytic C-lobe domain
            (KIND)*formin-2 formin SPIR interaction motif (FSI) complex
  JOURNAL   J Biol Chem 286 (35), 30732-30739 (2011)
   PUBMED   21705804
  REMARK    GeneRIF: analysis of the molecular basis of the Spir1/formin-2
            interaction
REFERENCE   7  (residues 1 to 622)
  AUTHORS   Pfender,S., Kuznetsov,V., Pleiser,S., Kerkhoff,E. and Schuh,M.
  TITLE     Spire-type actin nucleators cooperate with Formin-2 to drive
            asymmetric oocyte division
  JOURNAL   Curr Biol 21 (11), 955-960 (2011)
   PUBMED   21620703
REFERENCE   8  (residues 1 to 622)
  AUTHORS   Pechlivanis,M., Samol,A. and Kerkhoff,E.
  TITLE     Identification of a short Spir interaction sequence at the
            C-terminal end of formin subgroup proteins
  JOURNAL   J Biol Chem 284 (37), 25324-25333 (2009)
   PUBMED   19605360
  REMARK    GeneRIF: both mammalian Spir proteins, Spir-1 and Spir-2, interact
            with mammalian Fmn subgroup proteins formin-1 and formin-2
REFERENCE   9  (residues 1 to 622)
  AUTHORS   Bosch,M., Le,K.H., Bugyi,B., Correia,J.J., Renault,L. and
            Carlier,M.F.
  TITLE     Analysis of the function of Spire in actin assembly and its synergy
            with formin and profilin
  JOURNAL   Mol Cell 28 (4), 555-568 (2007)
   PUBMED   18042452
  REMARK    GeneRIF: The multifunctional character of the WH2 domains allows
            Spire to sequester four G-actin subunits binding cooperatively in a
            tight SA(4) complex and to nucleate, sever, and cap filaments at
            their barbed ends.
REFERENCE   10 (residues 1 to 622)
  AUTHORS   Kerkhoff,E., Simpson,J.C., Leberfinger,C.B., Otto,I.M., Doerks,T.,
            Bork,P., Rapp,U.R., Raabe,T. and Pepperkok,R.
  TITLE     The Spir actin organizers are involved in vesicle transport
            processes
  JOURNAL   Curr Biol 11 (24), 1963-1968 (2001)
   PUBMED   11747823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB056921.1, BC115005.1 and AP001029.5.
            
            Summary: Spire proteins, such as SPIRE1, are highly conserved
            between species. They belong to the family of Wiskott-Aldrich
            homology region-2 (WH2) proteins, which are involved in actin
            organization (Kerkhoff et al., 2001 [PubMed 11747823]).[supplied by
            OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) lacks an in-frame exon and
            differs in the 5' UTR and coding sequence compared to variant 1.
            The resulting isoform (c) is shorter at the N-terminus and lacks an
            alternate segment compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.407188.1,
                                           SRR5189667.274070.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..622
                     /product="protein spire homolog 1 isoform c"
                     /note="protein spire homolog 1; spire actin nucleation
                     factor 1; spire family actin nucleation factor 1"
                     /calculated_mol_wt=71437
     Region          <1..116
                     /region_name="KIND"
                     /note="Kinase non-catalytic C-lobe domain; pfam16474"
                     /db_xref="CDD:465129"
     Region          140..171
                     /region_name="WH2_Spire_1-2_r1"
                     /note="first tandem Wiskott-Aldrich Syndrome Homology
                     (WASP) region 2 (WH2 motif) repeat of protein Spire
                     homologs 1 and 2; cd22065"
                     /db_xref="CDD:409208"
     Site            order(153..154,156..158,160..162,166..169)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409208"
     Region          166..169
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409208"
     Region          180..211
                     /region_name="WH2_Spire1_r2-like"
                     /note="second tandem Wiskott-Aldrich Syndrome Homology
                     (WASP) region 2 (WH2 motif) repeat of protein Spire
                     homolog 1 (Spir1), and related proteins; cd22078"
                     /db_xref="CDD:409221"
     Site            order(185..186,188..190,192..194,200..203)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409221"
     Region          200..203
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409221"
     Region          214..236
                     /region_name="WH2_Spire1-2_r3"
                     /note="third tandem Wiskott-Aldrich Syndrome Homology
                     (WASP) region 2 (WH2 motif) repeat of protein Spire
                     homologs 1 and 2; cd22186"
                     /db_xref="CDD:409226"
     Site            order(217..218,220..222,224..226,231..234)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409226"
     Region          245..268
                     /region_name="WH2_Spire1_r4"
                     /note="fourth tandem Wiskott-Aldrich Syndrome Homology
                     (WASP) region 2 (WH2 motif) repeat of protein Spire
                     homolog 1; cd22080"
                     /db_xref="CDD:409223"
     Site            order(249..250,252..254,256..258,263..266)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409223"
     Region          454..574
                     /region_name="FYVE_SPIR1"
                     /note="FYVE-related domain found in protein spire homolog
                     1 (Spire1) and similar proteins; cd15767"
                     /db_xref="CDD:277306"
     CDS             1..622
                     /gene="SPIRE1"
                     /gene_synonym="Spir-1"
                     /coded_by="NM_001128627.1:106..1974"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45830.1"
                     /db_xref="GeneID:56907"
                     /db_xref="HGNC:HGNC:30622"
                     /db_xref="MIM:609216"
ORIGIN      
        1 metevieslg iiiykaldyg lkeneerels ppleqlidhm antveadgsn degyeaaeeg
       61 lgdedekrki sairsyrdvm klcaahlpte sdapnhyqav cralfaetme lhtfltkiks
      121 akenlkkiqe meksdesstd leelknadwa rfwvqvmrdl rngvklkkvq erqynplpie
      181 yqltpyemlm ddirckrytl rkvmvngdip prlkksahei ildfirsrpp lnpvsarklk
      241 ptpprprslh erileeikae rklrpvspee irrsrldvtt pestknlves smvnggltsq
      301 tkenglstsq qvpaqrkkll raptlaelds seseeetlhk stssssvsps fpeepvleav
      361 strkkppkfl pisstpqper rqppqrrhsi eketptnvrq flppsrqssr sleefcypve
      421 claltveevm hirqvlvkae lekyqqykdi ytalkkgklc fccrtrrfsf ftwsytcqfc
      481 krpvcsqcck kmrlpskpys tlpifslgps alqrgessmr sekpstahhr plrsiarfss
      541 ksksmdksde elqfpkelme dwstmevcvd ckkfiseiis ssrrslvlan krarlkrktq
      601 sfymsspgps eycpsertis ei
//
LOCUS       NP_065952               1648 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD and RING finger domain-containing protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_065952 XP_290536
VERSION     NP_065952.2
DBSOURCE    REFSEQ: accession NM_020901.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1648)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1648)
  AUTHORS   Lin,H.W., Shih,T.W., Amanna,A. and Chang,M.S.
  TITLE     PHRF1 Promotes Cell Invasion by Modulating SOX4 Expression in
            Colorectal Cancer HCT116-p53-/- Cells
  JOURNAL   Anticancer Res 43 (12), 5437-5446 (2023)
   PUBMED   38030167
  REMARK    GeneRIF: PHRF1 Promotes Cell Invasion by Modulating SOX4 Expression
            in Colorectal Cancer HCT116-p53[-/-] Cells.
REFERENCE   3  (residues 1 to 1648)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1648)
  AUTHORS   An,C.H., Son,H.J., Yoo,N.J. and Lee,S.H.
  TITLE     Downregulation of a putative tumor suppressor gene PHRF1 in gastric
            and colorectal cancers
  JOURNAL   Pathol Res Pract 216 (6), 152984 (2020)
   PUBMED   32360246
  REMARK    GeneRIF: Downregulation of a putative tumor suppressor gene PHRF1
            in gastric and colorectal cancers.
REFERENCE   5  (residues 1 to 1648)
  AUTHORS   Wang,Y., Wang,H., Pan,T., Li,L., Li,J. and Yang,H.
  TITLE     Overexpression of PHRF1 attenuates the proliferation and
            tumorigenicity of non-small cell lung cancer cells
  JOURNAL   Oncotarget 7 (39), 64360-64370 (2016)
   PUBMED   27608840
  REMARK    GeneRIF: Overexpression of PHRF1 attenuated the proliferation and
            tumorigenicity of non-small cell lung cancer cell lines.
REFERENCE   6  (residues 1 to 1648)
  AUTHORS   Webb,R., Kelly,J.A., Somers,E.C., Hughes,T., Kaufman,K.M.,
            Sanchez,E., Nath,S.K., Bruner,G., Alarcon-Riquelme,M.E.,
            Gilkeson,G.S., Kamen,D.L., Richardson,B.C., Harley,J.B. and
            Sawalha,A.H.
  TITLE     Early disease onset is predicted by a higher genetic risk for lupus
            and is associated with a more severe phenotype in lupus patients
  JOURNAL   Ann Rheum Dis 70 (1), 151-156 (2011)
   PUBMED   20881011
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1648)
  AUTHORS   Sanchez,E., Webb,R.D., Rasmussen,A., Kelly,J.A., Riba,L.,
            Kaufman,K.M., Garcia-de la Torre,I., Moctezuma,J.F.,
            Maradiaga-Cecena,M.A., Cardiel-Rios,M.H., Acevedo,E.,
            Cucho-Venegas,M., Garcia,M.A., Gamron,S., Pons-Estel,B.A.,
            Vasconcelos,C., Martin,J., Tusie-Luna,T., Harley,J.B.,
            Richardson,B., Sawalha,A.H. and Alarcon-Riquelme,M.E.
  TITLE     Genetically determined Amerindian ancestry correlates with
            increased frequency of risk alleles for systemic lupus
            erythematosus
  JOURNAL   Arthritis Rheum 62 (12), 3722-3729 (2010)
   PUBMED   20848568
  REMARK    GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1648)
  AUTHORS   Salloum,R., Franek,B.S., Kariuki,S.N., Rhee,L., Mikolaitis,R.A.,
            Jolly,M., Utset,T.O. and Niewold,T.B.
  TITLE     Genetic variation at the IRF7/PHRF1 locus is associated with
            autoantibody profile and serum interferon-alpha activity in lupus
            patients
  JOURNAL   Arthritis Rheum 62 (2), 553-561 (2010)
   PUBMED   20112359
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1648)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 1648)
  AUTHORS   Harley,J.B., Alarcon-Riquelme,M.E., Criswell,L.A., Jacob,C.O.,
            Kimberly,R.P., Moser,K.L., Tsao,B.P., Vyse,T.J., Langefeld,C.D.,
            Nath,S.K., Guthridge,J.M., Cobb,B.L., Mirel,D.B., Marion,M.C.,
            Williams,A.H., Divers,J., Wang,W., Frank,S.G., Namjou,B.,
            Gabriel,S.B., Lee,A.T., Gregersen,P.K., Behrens,T.W., Taylor,K.E.,
            Fernando,M., Zidovetzki,R., Gaffney,P.M., Edberg,J.C., Rioux,J.D.,
            Ojwang,J.O., James,J.A., Merrill,J.T., Gilkeson,G.S., Seldin,M.F.,
            Yin,H., Baechler,E.C., Li,Q.Z., Wakeland,E.K., Bruner,G.R.,
            Kaufman,K.M. and Kelly,J.A.
  CONSRTM   International Consortium for Systemic Lupus Erythematosus Genetics
            (SLEGEN)
  TITLE     Genome-wide association scan in women with systemic lupus
            erythematosus identifies susceptibility variants in ITGAM, PXK,
            KIAA1542 and other loci
  JOURNAL   Nat Genet 40 (2), 204-210 (2008)
   PUBMED   18204446
  REMARK    GeneRIF: study presents four new regions having genetic
            associations with systemic lupus erythematosus in women of European
            descent: ITGAM, KIAA1542, PXK and rs10798269
            GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA656880.1, BC144293.1 and BC146771.1.
            
            On Jan 22, 2009 this sequence version replaced NP_065952.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site, compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..1648
                     /product="PHD and RING finger domain-containing protein 1
                     isoform 2"
                     /note="PHD and RING finger domain-containing protein 1;
                     CTD-binding SR-like protein rA9; protein phosphatase 1,
                     regulatory subunit 125"
                     /calculated_mol_wt=178449
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          <49..106
                     /region_name="DNA_pol_phi"
                     /note="DNA polymerase phi; pfam04931"
                     /db_xref="CDD:461488"
     Region          102..152
                     /region_name="mRING-HC-C3HC3D_PHRF1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in PHD and RING finger domain-containing protein 1
                     (PHRF1) and similar proteins; cd16635"
                     /db_xref="CDD:438297"
     Region          185..230
                     /region_name="PHD_PHRF1"
                     /note="PHD finger found in PHD and RING finger
                     domain-containing protein 1 (PHRF1); cd15536"
                     /db_xref="CDD:277011"
     Site            order(185,197..201,205,225)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277011"
     Region          324..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63625; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          533..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          643..870
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            863
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          887..1239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            916
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1280..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          <1288..1554
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1406..1438
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1454..1485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1525..1555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1629..1648
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     CDS             1..1648
                     /gene="PHRF1"
                     /gene_synonym="PPP1R125; RNF221"
                     /coded_by="NM_020901.4:145..5091"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44507.1"
                     /db_xref="GeneID:57661"
                     /db_xref="HGNC:HGNC:24351"
                     /db_xref="MIM:611780"
ORIGIN      
        1 mdddsldelv arspgpdghp qvgpadpagd feessvgssg dsgddsdseh gdgtdgedeg
       61 aseeedledr sgsedseddg etllevagtq gkleaagsfn sdddaescpi clnafrdqav
      121 gtpencahyf cldcivewsk nanscpvdrt lfkciciraq fggkilrkip ventkaseee
      181 edptfcevcg rsdredrlll cdgcdagyhm ecldpplqev pvdewfcpec aapgvvlaad
      241 agpvseeevs llladvvptt srlrpragrt raiartrqse rvratvnrnr istarrvqht
      301 pgrlgsslld eaieavatgl stavyqrplt prtparrkrk trrrkkvpgr kktpsgpsak
      361 skssatrskk rqhrvkkrrg kkvkseattr sriartlglr rpvhsscips vlkpvepslg
      421 llradigaas lslfgdpyel dpfdseelsa nplsplsakr ralsrsalqs hqpvarpvsv
      481 glsrrrlpaa vpepdleeep vpdllgsils gqsllmlgss dviihrdgsl sakraapvsf
      541 qrnsgslsrg eegfkgclqp ralpsgspaq gpsgnrpqst glscqgrsrt partagapvr
      601 ldlpaapgav qarnlsngsv pgfrqshspw fngtnkhtlp lasaaskiss rdskppcrsv
      661 vpgpplkpap rrtdiselpr ipkirrddgg grrdaapahg qsieipsaci srltgregtg
      721 qpgrgtraes eassrvprep gvhtgssrpp apsshgslap lgpsrgkgvg stfesfrini
      781 pgnmahssql sspgfcntfr pvddkeqrke npsplfsikk tkqlrsevyd psdptgsdss
      841 apgsspersg pgllpseitr tisinspkaq tvqavrcvts ytvesifgte pepplgpssa
      901 msklrgavaa egasdteree ptesqglaar lrrpsppepw deedgascst ffgseertvt
      961 cvtvvepeap pspdvlqaat hrvvelrpps rsrstsssrs rkkakrkrvs rehgrtrsgt
     1021 rsesrdrssr saspsvgeer prrqrskaks rrsssdrsss rerakrkkak dksrehrrgp
     1081 wghsrrtsrs rsgspgsssy ehyesrkkkk rrsasrprgr ecsptssler lcrhkhqrer
     1141 sherpdrkes vawprdrrkr rsrspssehr arehrrprsr ekwpqtrshs perkgavrea
     1201 spaplaqgep gredlptrlp algeahvspe vatadkaplq appvlevaae cepddldldy
     1261 gdsveaghvf ddfssdavfi qlddmsspps pestdssper dfplkpalpp aslavaaiqr
     1321 evslmhdedp sqppplpegt qephllrpda aekaeapssp dvapagkeds psasgrvqea
     1381 arpeevvsqt pllrsralvk rvtwnlqese ssapaedrap raplhrpqkp regawdmedv
     1441 aptgvrqvfs elpfpshvlp epgfpdtdps qvyspglppa paqpssippc alvsqptvqf
     1501 ilqgslplvg cgaaqtlapv paaltpasep asqataasns eektpaprla aektkkeeym
     1561 kklhmqerav eevklaikpf yqkrevtkee ykdilrkavq kichsksgei npvkvanlvk
     1621 ayvdkyrhmr rhkkpeagee pptqgaeg
//
LOCUS       NP_001137415             133 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex protein 8 isoform b [Homo sapiens].
ACCESSION   NP_001137415
VERSION     NP_001137415.1
DBSOURCE    REFSEQ: accession NM_001143943.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 133)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 133)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 133)
  AUTHORS   Bower,R., Tritschler,D., Vanderwaal,K., Perrone,C.A., Mueller,J.,
            Fox,L., Sale,W.S. and Porter,M.E.
  TITLE     The N-DRC forms a conserved biochemical complex that maintains
            outer doublet alignment and limits microtubule sliding in motile
            axonemes
  JOURNAL   Mol Biol Cell 24 (8), 1134-1152 (2013)
   PUBMED   23427265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB286332.1, AK302883.1 and
            AB209286.1.
            
            Summary: The gene encodes a protein that contains two EF-hand
            calcium-binding domains although its function has yet to be
            determined. Alternatively spliced transcripts have been observed.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2) represents the longest
            transcript and encodes the shortest protein (isoform b).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302883.1, DRR138524.485804.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..133
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..133
                     /product="dynein regulatory complex protein 8 isoform b"
                     /note="EF-hand calcium-binding domain-containing protein
                     2; dynein regulatory complex protein 8; EF-hand calcium
                     binding domain 2"
                     /calculated_mol_wt=15326
     Region          1..>122
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..133
                     /gene="DRC8"
                     /gene_synonym="CFAP200; EFCAB2"
                     /coded_by="NM_001143943.1:91..492"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44341.1"
                     /db_xref="GeneID:84288"
                     /db_xref="HGNC:HGNC:28166"
                     /db_xref="MIM:619617"
ORIGIN      
        1 madekdreei ivaefhkkik eafevfdhes nntvdvreig tiirslgccp tegelhdlia
       61 eveeeeptgy irfekflpvm teillerkyr pipedvllra fevldsakrg fltkdeliky
      121 mteedgvslr rpg
//
LOCUS       NP_001273446             327 aa            linear   PRI 20-NOV-2025
DEFINITION  adenosine 3'-phospho 5'-phosphosulfate transporter 1 isoform e
            [Homo sapiens].
ACCESSION   NP_001273446
VERSION     NP_001273446.1
DBSOURCE    REFSEQ: accession NM_001286517.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Guasto,A., Dubail,J., Aguilera-Albesa,S., Paganini,C., Vanhulle,C.,
            Haouari,W., Gorria-Redondo,N., Aznal-Sainz,E., Boddaert,N.,
            Planas-Serra,L., Schluter,A., Velez-Santamaria,V., Verdura,E.,
            Bruneel,A., Rossi,A., Huber,C., Pujol,A. and Cormier-Daire,V.
  TITLE     Biallelic variants in SLC35B2 cause a novel chondrodysplasia with
            hypomyelinating leukodystrophy
  JOURNAL   Brain 145 (10), 3711-3722 (2022)
   PUBMED   35325049
  REMARK    GeneRIF: Biallelic variants in SLC35B2 cause a novel
            chondrodysplasia with hypomyelinating leukodystrophy.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Uezato,A., Jitoku,D., Shimazu,D., Yamamoto,N., Kurumaji,A.,
            Iwayama,Y., Toyota,T., Yoshikawa,T., Haroutunian,V., Bentea,E.,
            Meller,J., Sullivan,C.R., Meador-Woodruff,J.H., McCullumsmith,R.E.
            and Nishikawa,T.
  TITLE     Differential genetic associations and expression of PAPST1/SLC35B2
            in bipolar disorder and schizophrenia
  JOURNAL   J Neural Transm (Vienna) 129 (7), 913-924 (2022)
   PUBMED   35501530
  REMARK    GeneRIF: Differential genetic associations and expression of
            PAPST1/SLC35B2 in bipolar disorder and schizophrenia.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Guo,D., Yu,X., Wang,D., Li,Z., Zhou,Y., Xu,G., Yuan,B., Qin,Y. and
            Chen,M.
  TITLE     SLC35B2 Acts in a Dual Role in the Host Sulfation Required for EV71
            Infection
  JOURNAL   J Virol 96 (9), e0204221 (2022)
   PUBMED   35420441
  REMARK    GeneRIF: SLC35B2 Acts in a Dual Role in the Host Sulfation Required
            for EV71 Infection.
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Guo,X.Y., Gao,X.D. and Fujita,M.
  TITLE     Sulfation of a FLAG tag mediated by SLC35B2 and TPST2 affects
            antibody recognition
  JOURNAL   PLoS One 16 (5), e0250805 (2021)
   PUBMED   33951064
  REMARK    GeneRIF: Sulfation of a FLAG tag mediated by SLC35B2 and TPST2
            affects antibody recognition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Xu,Q.F., Pan,Y.W., Li,L.C., Zhou,Z., Huang,Q.L., Pang,J.C.,
            Zhu,X.P., Ren,Y., Yang,H., Ohgaki,H. and Lv,S.Q.
  TITLE     MiR-22 is frequently downregulated in medulloblastomas and inhibits
            cell proliferation via the novel target PAPST1
  JOURNAL   Brain Pathol 24 (6), 568-583 (2014)
   PUBMED   24576181
  REMARK    GeneRIF: Results suggest that frequently downregulated miR-22
            expression is associated with cell proliferation in
            medulloblastomas, and this may be at least in part via PAPST1,
            which is a novel target of miR-22
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Kamiyama,S., Ichimiya,T., Ikehara,Y., Takase,T., Fujimoto,I.,
            Suda,T., Nakamori,S., Nakamura,M., Nakayama,F., Irimura,T.,
            Nakanishi,H., Watanabe,M., Narimatsu,H. and Nishihara,S.
  TITLE     Expression and the role of 3'-phosphoadenosine 5'-phosphosulfate
            transporters in human colorectal carcinoma
  JOURNAL   Glycobiology 21 (2), 235-246 (2011)
   PUBMED   20978009
  REMARK    GeneRIF: PAPS transporters play a role in the proliferation of
            colorectal carcinoma cells themselves and take part in a
            desmoplastic reaction to support cancer growth by controlling their
            sulfation status.
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Kamiyama,S., Suda,T., Ueda,R., Suzuki,M., Okubo,R., Kikuchi,N.,
            Chiba,Y., Goto,S., Toyoda,H., Saigo,K., Watanabe,M., Narimatsu,H.,
            Jigami,Y. and Nishihara,S.
  TITLE     Molecular cloning and identification of 3'-phosphoadenosine
            5'-phosphosulfate transporter
  JOURNAL   J Biol Chem 278 (28), 25958-25963 (2003)
   PUBMED   12716889
  REMARK    GeneRIF: PAPS1 has roles in PAPS transport and post-translational
            sulfation
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY044970.1, BI769501.1, AB106538.1, AK075456.1 and AK223028.1.
            
            Summary: Sulfotransferases (e.g., SULT4A1; MIM 608359) use an
            activated form of sulfate, 3-prime-phosphoadenosine
            5-prime-phosphosulfate (PAPS), as a common sulfate donor for
            sulfation of glycoproteins, proteoglycans, and glycolipids in the
            endoplasmic reticulum and Golgi apparatus. SLC35B2 is located in
            the microsomal membrane and transports PAPS from the cytosol, where
            it is synthesized, into the Golgi lumen (Kamiyama et al., 2003
            [PubMed 12716889]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (7) lacks an alternate exon,
            resulting in translation initiation at a downstream in-frame start
            codon, compared to variant 1. The encoded isoform (e) is shorter at
            the N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI769501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..327
                     /product="adenosine 3'-phospho 5'-phosphosulfate
                     transporter 1 isoform e"
                     /note="3'-phosphoadenosine 5'-phosphosulfate transporter;
                     adenosine 3'-phospho 5'-phosphosulfate transporter 1; PAPS
                     transporter 1; putative MAPK-activating protein PM15;
                     putative NF-kappa-B-activating protein 48; solute carrier
                     family 35 (adenosine 3'-phospho 5'-phosphosulfate
                     transporter), member B2"
                     /calculated_mol_wt=35769
     Region          6..307
                     /region_name="UAA"
                     /note="UAA transporter family; pfam08449"
                     /db_xref="CDD:462479"
     CDS             1..327
                     /gene="SLC35B2"
                     /gene_synonym="HLD26; PAPST1; SLL; UGTrel4"
                     /coded_by="NM_001286517.2:240..1223"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="GeneID:347734"
                     /db_xref="HGNC:HGNC:16872"
                     /db_xref="MIM:610788"
ORIGIN      
        1 mwqalkllfc atglqvsylt wgvlqervmt rsygatatsp gerftdsqfl vlmnrvlali
       61 vaglscvlck qprhgapmyr ysfaslsnvl sswcqyealk fvsfptqvla kaskvipvml
      121 mgklvsrrsy ehweyltatl isigvsmfll ssgpeprssp attlsglill agyiafdsft
      181 snwqdalfay kmssvqmmfg vnffsclftv gslleqgall egtrfmgrhs efaahallls
      241 icsacgqlfi fytigqfgaa vftiimtlrq afaillscll yghtvtvvgg lgvavvfaal
      301 llrvyargrl kqrgkkavpv espvqkv
//
LOCUS       NP_001274175            1417 aa            linear   PRI 20-NOV-2025
DEFINITION  recQ-like DNA helicase BLM isoform 1 [Homo sapiens].
ACCESSION   NP_001274175
VERSION     NP_001274175.1
DBSOURCE    REFSEQ: accession NM_001287246.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1417)
  AUTHORS   Silva,J.P.L., Donaires,F.S., Gutierrez-Rodrigues,F., Martins,D.J.,
            Carvalho,V.S., Santana,B.A., Cunha,R.L.G., Kajigaya,S.,
            Menck,C.F.M., Young,N.S., Kjeldsen,E. and Calado,R.T.
  TITLE     RecQ helicase expression in patients with telomeropathies
  JOURNAL   Mol Biol Rep 51 (1), 754 (2024)
   PUBMED   38874681
  REMARK    GeneRIF: RecQ helicase expression in patients with telomeropathies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1417)
  AUTHORS   Tsukada,K., Jones,S.E., Bannister,J., Durin,M.A., Vendrell,I.,
            Fawkes,M., Fischer,R., Kessler,B.M., Chapman,J.R. and
            Blackford,A.N.
  TITLE     BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint
            DNA molecule resolution
  JOURNAL   Mol Cell 84 (4), 640-658 (2024)
   PUBMED   38266639
  REMARK    GeneRIF: BLM and BRCA1-BARD1 coordinate complementary mechanisms of
            joint DNA molecule resolution.
REFERENCE   3  (residues 1 to 1417)
  AUTHORS   Liu,S., Atkinson,E., Paulucci-Holthauzen,A. and Wang,B.
  TITLE     A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism
            controlling BLM ubiquitination and G-quadruplex resolution
  JOURNAL   Nat Commun 14 (1), 6111 (2023)
   PUBMED   37777511
  REMARK    GeneRIF: A CK2 and SUMO-dependent, PML NB-involved regulatory
            mechanism controlling BLM ubiquitination and G-quadruplex
            resolution.
            Erratum:[Nat Commun. 2024 Feb 5;15(1):1077. doi:
            10.1038/s41467-024-45551-1. PMID: 38316763]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1417)
  AUTHORS   Danino,Y.M., Molitor,L., Rosenbaum-Cohen,T., Kaiser,S., Cohen,Y.,
            Porat,Z., Marmor-Kollet,H., Katina,C., Savidor,A., Rotkopf,R.,
            Ben-Isaac,E., Golani,O., Levin,Y., Monchaud,D., Hickson,I.D. and
            Hornstein,E.
  TITLE     BLM helicase protein negatively regulates stress granule formation
            through unwinding RNA G-quadruplex structures
  JOURNAL   Nucleic Acids Res 51 (17), 9369-9384 (2023)
   PUBMED   37503837
  REMARK    GeneRIF: BLM helicase protein negatively regulates stress granule
            formation through unwinding RNA G-quadruplex structures.
REFERENCE   5  (residues 1 to 1417)
  AUTHORS   Foucault,F., Vaury,C., Barakat,A., Thibout,D., Planchon,P.,
            Jaulin,C., Praz,F. and Amor-Gueret,M.
  TITLE     Characterization of a new BLM mutation associated with a
            topoisomerase II alpha defect in a patient with Bloom's syndrome
  JOURNAL   Hum Mol Genet 6 (9), 1427-1434 (1997)
   PUBMED   9285778
REFERENCE   6  (residues 1 to 1417)
  AUTHORS   Ellis,N.A., Groden,J., Ye,T.Z., Straughen,J., Lennon,D.J.,
            Ciocci,S., Proytcheva,M. and German,J.
  TITLE     The Bloom's syndrome gene product is homologous to RecQ helicases
  JOURNAL   Cell 83 (4), 655-666 (1995)
   PUBMED   7585968
REFERENCE   7  (residues 1 to 1417)
  AUTHORS   German,J., Roe,A.M., Leppert,M.F. and Ellis,N.A.
  TITLE     Bloom syndrome: an analysis of consanguineous families assigns the
            locus mutated to chromosome band 15q26.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6669-6673 (1994)
   PUBMED   8022833
REFERENCE   8  (residues 1 to 1417)
  AUTHORS   Langer,K., Cunniff,C.M. and Kucine,N.
  TITLE     Bloom Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301572
REFERENCE   9  (residues 1 to 1417)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   10 (residues 1 to 1417)
  AUTHORS   McDaniel,L.D. and Schultz,R.A.
  TITLE     Elevated sister chromatid exchange phenotype of Bloom syndrome
            cells is complemented by human chromosome 15
  JOURNAL   Proc Natl Acad Sci U S A 89 (17), 7968-7972 (1992)
   PUBMED   1518822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD707743.1, BP363946.1,
            BC143288.1, BC115032.1, DB520927.1 and AC124248.6.
            
            Summary: The Bloom syndrome is an autosomal recessive disorder
            characterized by growth deficiency, microcephaly and
            immunodeficiency among others. It is caused by homozygous or
            compound heterozygous mutation in the gene encoding DNA helicase
            RecQ protein on chromosome 15q26. This Bloom-associated helicase
            unwinds a variety of DNA substrates including Holliday junction,
            and is involved in several pathways contributing to the maintenance
            of genome stability. Identification of pathogenic Bloom variants is
            required for heterozygote testing in at-risk families. [provided by
            RefSeq, May 2020].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143288.1, SRR14038191.1613662.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..1417
                     /product="recQ-like DNA helicase BLM isoform 1"
                     /EC_number="5.6.2.4"
                     /note="bloom syndrome protein; recQ protein-like 3; Bloom
                     syndrome RecQ like helicase; DNA helicase, RecQ-like type
                     2; Bloom syndrome, RecQ helicase-like; recQ-like DNA
                     helicase BLM; DNA 3'-5' helicase BLM"
                     /calculated_mol_wt=158870
     Region          1..368
                     /region_name="BLM_N"
                     /note="N-terminal region of Bloom syndrome protein;
                     pfam16202"
                     /db_xref="CDD:465064"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          203..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          250..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          301..600
                     /region_name="Necessary for interaction with SPIDR.
                     /evidence=ECO:0000269|PubMed:23509288"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          362..414
                     /region_name="Necessary for dimerization and
                     homooligomerization.
                     /evidence=ECO:0000269|PubMed:28228481"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          372..412
                     /region_name="BDHCT"
                     /note="BDHCT (NUC031) domain; pfam08072"
                     /db_xref="CDD:462356"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          425..647
                     /region_name="BDHCT_assoc"
                     /note="BDHCT-box associated domain on Bloom syndrome
                     protein; pfam16204"
                     /db_xref="CDD:465065"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          657..1143
                     /region_name="recQ_fam"
                     /note="ATP-dependent DNA helicase, RecQ family; TIGR00614"
                     /db_xref="CDD:129701"
     Site            717
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          795..798
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            808
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            863
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          870..873
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          897..899
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            920
                     /site_type="other"
                     /note="3' overhang DNA-binding, via amide nitrogen.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Site            946
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Site            968
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Region          1000..1003
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          1094..1139
                     /region_name="DNA Holliday junction binding.
                     /evidence=ECO:0000269|PubMed:24257077"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          1110..1112
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            1110
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Region          1121..1125
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          1160..1166
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            1197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          1213..1292
                     /region_name="HRDC"
                     /note="Helicase and RNase D C-terminal; smart00341"
                     /db_xref="CDD:128635"
     Region          1227..1244
                     /region_name="Necessary for ssDNA and DNA Holliday
                     junction binding. /evidence=ECO:0000269|PubMed:20639533"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          1289..1417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            1296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            1310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          1334..1349
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     CDS             1..1417
                     /gene="BLM"
                     /gene_synonym="BS; MGRISCE1; RECQ2; RECQL2; RECQL3"
                     /coded_by="NM_001287246.2:210..4463"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10363.1"
                     /db_xref="GeneID:641"
                     /db_xref="HGNC:HGNC:1058"
                     /db_xref="MIM:604610"
ORIGIN      
        1 maavpqnnlq eqlerhsart lnnklslskp kfsgftfkkk tssdnnvsvt nvsvaktpvl
       61 rnkdvnvted fsfseplpnt tnqqrvkdff knapagqetq rggsksllpd flqtpkevvc
      121 ttqntptvkk srdtalkkle fssspdslst indwddmddf dtsetsksfv tppqshfvrv
      181 staqkskkgk rnffkaqlyt tntvktdlpp psseseqidl teeqkddsew lssdvicidd
      241 gpiaevhine daqesdslkt hlederdnse kkknleeael hstekvpcie fddddydtdf
      301 vppspeeiis assssskcls tlkdldtsdr kedvlstskd llskpekmsm qelnpetstd
      361 cdarqislqq qlihvmehic klidtipddk lklldcgnel lqqrnirrkl ltevdfnksd
      421 asllgslwry rpdsldgpme gdscptgnsm kelnfshlps nsvspgdcll tttlgktgfs
      481 atrknlferp lfnthlqksf vssnwaetpr lgkknessyf pgnvltstav kdqnkhtasi
      541 ndleretqps ydidnfdidd fdddddwedi mhnlaaskss taayqpikeg rpiksvserl
      601 ssaktdclpv sstaqninfs esiqnytdks aqnlasrnlk herfqslsfp htkemmkifh
      661 kkfglhnfrt nqleainaal lgedcfilmp tgggkslcyq lpacvspgvt vvisplrsli
      721 vdqvqkltsl dipatyltgd ktdseatniy lqlskkdpii kllyvtpeki casnrlistl
      781 enlyerklla rfvideahcv sqwghdfrqd ykrmnmlrqk fpsvpvmalt atanprvqkd
      841 iltqlkilrp qvfsmsfnrh nlkyyvlpkk pkkvafdcle wirkhhpyds giiyclsrre
      901 cdtmadtlqr dglaalayha glsdsardev qqkwinqdgc qvicatiafg mgidkpdvrf
      961 vihaslpksv egyyqesgra grdgeishcl lfytyhdvtr lkrlimmekd gnhhtrethf
     1021 nnlysmvhyc enitecrriq llayfgengf npdfckkhpd vscdnccktk dyktrdvtdd
     1081 vksivrfvqe hsssqgmrni khvgpsgrft mnmlvdiflg sksakiqsgi fgkgsaysrh
     1141 naerlfkkli ldkildedly inandqaiay vmlgnkaqtv lngnlkvdfm etensssvkk
     1201 qkalvakvsq reemvkkclg eltevckslg kvfgvhyfni fntvtlkkla eslssdpevl
     1261 lqidgvtedk lekygaevis vlqkysewts paedsspgis lsssrgpgrs aaeeldeeip
     1321 vsshyfaskt rnerkrkkmp asqrskrrkt assgskakgg satcrkissk tksssiigss
     1381 sashtsqats gansklgima ppkpinrpfl kpsyafs
//
LOCUS       NP_001337625             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337625 XP_011514958
VERSION     NP_001337625.1
DBSOURCE    REFSEQ: accession NM_001350696.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 21, 2017 this sequence version replaced XP_011514958.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (32), as well as variants 1-4,
            9-31, 33, and 34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.239858.1,
                                           SRR1660805.203094.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350696.1:462..2672"
                     /note="isoform 1 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_000523                539 aa            linear   PRI 20-NOV-2025
DEFINITION  propionyl-CoA carboxylase beta chain, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_000523
VERSION     NP_000523.2
DBSOURCE    REFSEQ: accession NM_000532.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Kurolap,A., Barel,D., Shaul Lotan,N., Wexler,I., Chai Gadot,C.,
            Mory,A., Barel,O., Almashanu,S. and Baris Feldman,H.
  TITLE     A common benign intronic deletion masking a pathogenic deep
            intronic PCCB variant - genome sequencing and RNA studies to the
            rescue
  JOURNAL   Mol Genet Metab 140 (3), 107702 (2023)
   PUBMED   37776842
  REMARK    GeneRIF: A common benign intronic deletion masking a pathogenic
            deep intronic PCCB variant - genome sequencing and RNA studies to
            the rescue.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Zhang,W., Zhang,M., Xu,Z., Yan,H., Wang,H., Jiang,J., Wan,J.,
            Tang,B., Liu,C., Chen,C. and Meng,Q.
  TITLE     Human forebrain organoid-based multi-omics analyses of PCCB as a
            schizophrenia associated gene linked to GABAergic pathways
  JOURNAL   Nat Commun 14 (1), 5176 (2023)
   PUBMED   37620341
  REMARK    GeneRIF: Human forebrain organoid-based multi-omics analyses of
            PCCB as a schizophrenia associated gene linked to GABAergic
            pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Tahara,T., Kraus,J.P. and Rosenberg,L.E.
  TITLE     An unusual insertion/deletion in the gene encoding the beta-subunit
            of propionyl-CoA carboxylase is a frequent mutation in Caucasian
            propionic acidemia
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1372-1376 (1990)
   PUBMED   2154743
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Baumgartner,E.R., Suormala,T.M., Wick,H., Probst,A.,
            Blauenstein,U., Bachmann,C. and Vest,M.
  TITLE     Biotinidase deficiency: a cause of subacute necrotizing
            encephalomyelopathy (Leigh syndrome). Report of a case with lethal
            outcome
  JOURNAL   Pediatr Res 26 (3), 260-266 (1989)
   PUBMED   2587127
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Waye,J.S., Gravel,R.A. and Willard,H.F.
  TITLE     Two PstI RFLPs in the PCCB gene on the long arm of chromosome 3
  JOURNAL   Nucleic Acids Res 16 (5), 2362 (1988)
   PUBMED   2895916
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Baumgartner,E.R., Bachmann,C., Brechbuhler,T. and Wick,H.
  TITLE     Acute neonatal nonketotic hyperglycinemia: normal propionate and
            methylmalonate metabolism
  JOURNAL   Pediatr Res 9 (7), 559-564 (1975)
   PUBMED   240144
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA090969.1 and BC013768.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 25, 2006 this sequence version replaced NP_000523.1.
            
            Summary: The protein encoded by this gene is a subunit of the
            propionyl-CoA carboxylase (PCC) enzyme, which is involved in the
            catabolism of propionyl-CoA. PCC is a mitochondrial enzyme that
            probably acts as a dodecamer of six alpha subunits and six beta
            subunits. This gene encodes the beta subunit of PCC. Defects in
            this gene are a cause of propionic acidemia type II (PA-2).
            Multiple transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.161574.1,
                                           SRR3476690.610353.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000251654.9/
                                                  ENSP00000251654.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..539
                     /product="propionyl-CoA carboxylase beta chain,
                     mitochondrial isoform 1 precursor"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, beta polypeptide;
                     propionyl-CoA carboxylase beta chain, mitochondrial;
                     PCCase subunit beta; propanoyl-CoA:carbon dioxide ligase
                     subunit beta; propionyl CoA carboxylase, beta polypeptide;
                     propionyl-CoA carboxylase beta subunit"
                     /calculated_mol_wt=58085
     Region          32..533
                     /region_name="Carboxyltransferase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01138"
                     /note="propagated from UniProtKB/Swiss-Prot (P05166.3)"
     Region          37..537
                     /region_name="MmdA"
                     /note="Acetyl-CoA carboxylase, carboxyltransferase
                     component [Lipid transport and metabolism]; COG4799"
                     /db_xref="CDD:443827"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P05166.3)"
     Site            99
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99MN9; propagated from
                     UniProtKB/Swiss-Prot (P05166.3)"
     Region          325..358
                     /region_name="Acyl-CoA binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P05166.3)"
     Site            474
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99MN9; propagated from
                     UniProtKB/Swiss-Prot (P05166.3)"
     Site            489
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99MN9; propagated from
                     UniProtKB/Swiss-Prot (P05166.3)"
     CDS             1..539
                     /gene="PCCB"
                     /coded_by="NM_000532.5:37..1656"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3089.1"
                     /db_xref="GeneID:5096"
                     /db_xref="HGNC:HGNC:8654"
                     /db_xref="MIM:232050"
ORIGIN      
        1 maaalrvaav garlsvlasg lraavrslcs qatsvnerie nkrrtallgg gqrridaqhk
       61 rgkltareri sllldpgsfv esdmfvehrc adfgmaadkn kfpgdsvvtg rgringrlvy
      121 vfsqdftvfg gslsgahaqk ickimdqait vgapviglnd sggariqegv eslagyadif
      181 lrnvtasgvi pqislimgpc aggavyspal tdftfmvkdt sylfitgpdv vksvtnedvt
      241 qeelggakth ttmsgvahra fendvdalcn lrdffnylpl ssqdpapvre chdpsdrlvp
      301 eldtivples tkaynmvdii hsvvdereff eimpnyakni ivgfarmngr tvgivgnqpk
      361 vasgcldins svkgarfvrf cdafniplit fvdvpgflpg taqeyggiir hgakllyafa
      421 eatvpkvtvi trkayggayd vmsskhlcgd tnyawptaei avmgakgave iifkghenve
      481 aaqaeyiekf anpfpaavrg fvddiiqpss trariccdld vlaskkvqrp wrkhanipl
//
LOCUS       NP_068817               1093 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec24A isoform 1 [Homo sapiens].
ACCESSION   NP_068817 XP_001128954 XP_001132082 XP_001132097
VERSION     NP_068817.1
DBSOURCE    REFSEQ: accession NM_021982.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Gomez-Navarro,N., Maldutyte,J., Poljak,K., Peak-Chew,S.Y., Orme,J.,
            Bisnett,B.J., Lamb,C.H., Boyce,M., Gianni,D. and Miller,E.A.
  TITLE     Selective inhibition of protein secretion by abrogating
            receptor-coat interactions during ER export
  JOURNAL   Proc Natl Acad Sci U S A 119 (31), e2202080119 (2022)
   PUBMED   35901214
  REMARK    GeneRIF: Selective inhibition of protein secretion by abrogating
            receptor-coat interactions during ER export.
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Zhang,Z., Yang,B., Zhou,S. and Wu,J.
  TITLE     CircRNA circ_SEC24A upregulates DNMT3A expression by sponging
            miR-26b-5p to aggravate osteoarthritis progression
  JOURNAL   Int Immunopharmacol 99, 107957 (2021)
   PUBMED   34325283
  REMARK    GeneRIF: CircRNA circ_SEC24A upregulates DNMT3A expression by
            sponging miR-26b-5p to aggravate osteoarthritis progression.
REFERENCE   4  (residues 1 to 1093)
  AUTHORS   Chen,X., Zhang,J., Liu,P., Wei,Y., Wang,X., Xiao,J., Wang,C.C. and
            Wang,L.
  TITLE     Proteolytic processing of secretory pathway kinase Fam20C by site-1
            protease promotes biomineralization
  JOURNAL   Proc Natl Acad Sci U S A 118 (32) (2021)
   PUBMED   34349020
REFERENCE   5  (residues 1 to 1093)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1093)
  AUTHORS   Tomarev,S.I., Wistow,G., Raymond,V., Dubois,S. and Malyukova,I.
  TITLE     Gene expression profile of the human trabecular meshwork: NEIBank
            sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 44 (6), 2588-2596 (2003)
   PUBMED   12766061
REFERENCE   7  (residues 1 to 1093)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   8  (residues 1 to 1093)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   9  (residues 1 to 1093)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   10 (residues 1 to 1093)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304060.1, BC019341.1,
            AJ131244.1, CD677660.1 and BM127845.1.
            
            On or before Oct 15, 2006 this sequence version replaced
            XP_001132097.1, XP_001132082.1, XP_001128954.1.
            
            Summary: The protein encoded by this gene belongs to a family of
            proteins that are homologous to yeast Sec24. This protein is a
            component of coat protein II (COPII)-coated vesicles that mediate
            protein transport from the endoplasmic reticulum. COPII acts in the
            cytoplasm to promote the transport of secretory, plasma membrane,
            and vacuolar proteins from the endoplasmic reticulum to the golgi
            complex. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.239877.1,
                                           SRR1660805.254531.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398844.7/ ENSP00000381823.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..1093
                     /product="protein transport protein Sec24A isoform 1"
                     /note="protein transport protein Sec24A; SEC24-related
                     protein A; SEC24 related gene family, member A; SEC24
                     family, member A; SEC24 homolog A, COPII coat complex
                     component"
                     /calculated_mol_wt=119619
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          <55..>159
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          60..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          189..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          237..1093
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Region          294..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          431..455
                     /region_name="Zinc finger-like"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          966..1038
                     /region_name="Gelsolin-like. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     CDS             1..1093
                     /gene="SEC24A"
                     /coded_by="NM_021982.3:293..3574"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43363.1"
                     /db_xref="GeneID:10802"
                     /db_xref="HGNC:HGNC:10703"
                     /db_xref="MIM:607183"
ORIGIN      
        1 msqpgipasg gapaslqaqn gaalasgspy tngpvqnall ssqesvsqgy nfqlpgsyph
       61 pipaktlnpv sgqsnyggsq gsgqtlnrpp vasnpvtpsl hsgpaprmpl pasqnpattp
      121 mpsssflpea nlppplnwqy nypstasqtn hcprassqpt vsgntslttn hqyvssgyps
      181 lqnsfiksgp svpplvnppl pttfqpgaph gpppaggppp vraltpltss yrdvpqplfn
      241 savnqegits ntnngsmvvh ssydeieggg llatpqltnk npkmsrsvgy sypslppgyq
      301 nttppgatgv ppsslnypsg pqaftqtplg anhlttsmsg lslqpeglrv vnllqernml
      361 pstplkppvp nlhediqkln cnpelfrctl tsipqtqall nkaklplgll lhpfkdlvql
      421 pvvtsstivr crscrtyinp fvsfldqrrw kcnlcyrvnd vpeeflynpl trvygephrr
      481 pevqnatief mapseymlrp pqppvylfvf dvshnavetg ylnsvcqsll dnldllpgnt
      541 rtkigfitfd stihfyglqe slsqpqmliv sdiedvfipm penllvnlne skelvqdllk
      601 tlpqmftktl etqsalgpal qaafklmspt ggrmsvfqtq lptlgvgalk preepnhrss
      661 akdihmtpst dfykklaldc sgqqvavdlf llsgqysdla slgcisrysa gsvyyypsyh
      721 hqhnpvqvqk lqkelqrylt rkigfeavmr irctkglsih tfhgnffvrs tdllslpnvn
      781 pdagyavqms veesltdtql vsfqsallyt sskgerrirv htlclpvvst lndvflgadv
      841 qaisgllanm avdrsmtasl sdardalvna vidslsayrs svlsnqqpgl mvpfslrlfp
      901 lfvlallkqk sfqtgtnarl derifamcqv knqplvylml tthpslyrvd nlsdegalni
      961 sdrtipqppi lqlsveklsr dgaflmdags vlmlwvgknc tqnflsqvlg vqnyasipqp
     1021 mtdlpeldtp esariiafis wlreqrpffp ilyvirdesp mkanflqnmi edrtesalsy
     1081 yefllhiqqq vnk
//
LOCUS       NP_003061               1590 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 2 isoform a [Homo sapiens].
ACCESSION   NP_003061
VERSION     NP_003061.3
DBSOURCE    REFSEQ: accession NM_003070.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1590)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1590)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z., Liu,Q., Zhang,Y., Xiong,S.
            and Zhang,S.
  TITLE     Expression of SMARCA2 and SMARCA4 in gastric adenocarcinoma and
            construction of a nomogram prognostic model
  JOURNAL   Int J Clin Oncol 28 (11), 1487-1500 (2023)
   PUBMED   37634210
  REMARK    GeneRIF: Expression of SMARCA2 and SMARCA4 in gastric
            adenocarcinoma and construction of a nomogram prognostic model.
REFERENCE   3  (residues 1 to 1590)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1590)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z.G., Zhang,M., Liu,Q.,
            Zhang,Y., Xiong,S. and Zhang,S.
  TITLE     Clinicopathological and prognostic significance of SWI/SNF complex
            subunits in undifferentiated gastric carcinoma
  JOURNAL   World J Surg Oncol 20 (1), 383 (2022)
   PUBMED   36464671
  REMARK    GeneRIF: Clinicopathological and prognostic significance of SWI/SNF
            complex subunits in undifferentiated gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1590)
  AUTHORS   Zhang,X., Chen,H., Song,Y., Chen,Z., Liu,X., Rong,P. and Ma,R.
  TITLE     Ten-year follow-up of Nicolaides-Baraitser syndrome with a de novo
            mutation and analysis of 58 gene loci of SMARCA2-associated NCBRS
  JOURNAL   Mol Genet Genomic Med 10 (9), e2009 (2022)
   PUBMED   35811451
  REMARK    GeneRIF: Ten-year follow-up of Nicolaides-Baraitser syndrome with a
            de novo mutation and analysis of 58 gene loci of SMARCA2-associated
            NCBRS.
REFERENCE   6  (residues 1 to 1590)
  AUTHORS   Aves,S.J., Hindley,J., Phear,G.A. and Tongue,N.
  TITLE     A fission yeast gene mapping close to suc1 encodes a protein
            containing two bromodomains
  JOURNAL   Mol Gen Genet 248 (4), 491-498 (1995)
   PUBMED   7565614
REFERENCE   7  (residues 1 to 1590)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   8  (residues 1 to 1590)
  AUTHORS   Muchardt,C., Yaniv,M. and Mattei,M.G.
  TITLE     Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2
            and Drosophila brm genes, to chromosome region 9p23-p24, by in situ
            hybridization
  JOURNAL   Mamm Genome 5 (4), 241-243 (1994)
   PUBMED   8012116
REFERENCE   9  (residues 1 to 1590)
  AUTHORS   Muchardt,C. and Yaniv,M.
  TITLE     A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
            Drosophila brm genes potentiates transcriptional activation by the
            glucocorticoid receptor
  JOURNAL   EMBO J 12 (11), 4279-4290 (1993)
   PUBMED   8223438
REFERENCE   10 (residues 1 to 1590)
  AUTHORS   Abdul-Rahman,O. and May,F.
  TITLE     SMARCA2-Related Nicolaides-Baraitser Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26468571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC040029.1, BC068252.1,
            X72889.1, AL558829.3, BC066596.1 and AK094076.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 4, 2004 this sequence version replaced NP_003061.2.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is highly similar to the brahma
            protein of Drosophila. Members of this family have helicase and
            ATPase activities and are thought to regulate transcription of
            certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI, which is required for
            transcriptional activation of genes normally repressed by
            chromatin. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene, which contains a
            trinucleotide repeat (CAG) length polymorphism. [provided by
            RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: X72889.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349721.8/ ENSP00000265773.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..1590
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     2 isoform a"
                     /note="global transcription activator homologous sequence;
                     SNF2-alpha; sucrose nonfermenting 2-like protein 2;
                     SNF2/SWI2-like protein 2; SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     a2; brahma homolog; probable global transcription
                     activator SNF2L2; BAF190B; protein brahma homolog;
                     BRG1-associated factor 190B; ATP-dependent helicase
                     SMARCA2; putative global transcription activator SNF2L2;
                     SWI/SNF related, matrix associated, actin dependent
                     regulator of chromatin, subfamily a, member 2"
                     /calculated_mol_wt=181149
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          <46..>450
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          95..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          173..207
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          212..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          436..508
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          551..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          589..632
                     /region_name="BRK"
                     /note="BRK domain; pfam07533"
                     /db_xref="CDD:462196"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          627..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          701..951
                     /region_name="DEXHc_SMARCA2"
                     /note="DEXH-box helicase domain of SMARCA2; cd18063"
                     /db_xref="CDD:350821"
     Region          720..>1202
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(751..757,791,851..852)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350821"
     Region          851..854
                     /region_name="DEGH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            997
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            999
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1259..1326
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Region          1333..>1419
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Region          1344..1383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            order(1361,1370,1373,1415,1419)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99926"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1382..1506
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1431,1436,1439,1478,1482,1488)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     Region          1506..1590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     CDS             1..1590
                     /gene="SMARCA2"
                     /gene_synonym="BAF190; BIS; BRM; hBRM; hSNF2a; NCBRS;
                     SAMRCA2; SNF2; SNF2L2; SNF2LA; Sth1p; SWI2"
                     /coded_by="NM_003070.5:95..4867"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34977.1"
                     /db_xref="GeneID:6595"
                     /db_xref="HGNC:HGNC:11098"
                     /db_xref="MIM:600014"
ORIGIN      
        1 mstptdpgam phpgpspgpg pspgpilgps pgpgpspgsv hsmmgpspgp psvshpmptm
       61 gstdfpqegm hqmhkpidgi hdkgivedih cgsmkgtgmr pphpgmgppq spmdqhsqgy
      121 msphpsplga pehvsspmsg ggptppqmpp sqpgalipgd pqamsqpnrg pspfspvqlh
      181 qlraqilayk mlargqplpe tlqlavqgkr tlpglqqqqq qqqqqqqqqq qqqqqqqqpq
      241 qqppqpqtqq qqqpalvnyn rpsgpgpels gpstpqklpv papggrpspa ppaaaqppaa
      301 avpgpsvpqp apgqpspvlq lqqkqsrisp iqkpqgldpv eilqereyrl qariahriqe
      361 lenlpgslpp dlrtkatvel kalrllnfqr qlrqevvacm rrdttletal nskaykrskr
      421 qtlrearmte klekqqkieq erkrrqkhqe ylnsilqhak dfkeyhrsva gkiqklskav
      481 atwhantere qkketeriek ermrrlmaed eegyrklidq kkdrrlayll qqtdeyvanl
      541 tnlvwehkqa qaakekkkrr rrkkkaeena eggesalgpd gepidessqm sdlpvkvtht
      601 etgkvlfgpe apkasqldaw lemnpgyeva prsdseesds dyeeedeeee ssrqeteeki
      661 lldpnseevs ekdakqiiet akqdvddeys mqysargsqs yytvahaise rvekqsalli
      721 ngtlkhyqlq glewmvslyn nnlngilade mglgktiqti alitylmehk rlngpyliiv
      781 plstlsnwty efdkwapsvv kisykgtpam rrslvpqlrs gkfnvlltty eyiikdkhil
      841 akirwkymiv deghrmknhh ckltqvlnth yvaprrillt gtplqnklpe lwallnfllp
      901 tifkscstfe qwfnapfamt gervdlneee tiliirrlhk vlrpfllrrl kkevesqlpe
      961 kveyvikcdm salqkilyrh mqakgilltd gsekdkkgkg gaktlmntim qlrkicnhpy
     1021 mfqhieesfa ehlgysngvi ngaelyrasg kfelldrilp klratnhrvl lfcqmtslmt
     1081 imedyfafrn flylrldgtt ksedraallk kfnepgsqyf ifllstragg lglnlqaadt
     1141 vvifdsdwnp hqdlqaqdra hrigqqnevr vlrlctvnsv eekilaaaky klnvdqkviq
     1201 agmfdqksss herraflqai leheeeneee devpddetln qmiarreeef dlfmrmdmdr
     1261 rredarnpkr kprlmeedel pswiikddae verltceeee ekifgrgsrq rrdvdysdal
     1321 tekqwlraie dgnleemeee vrlkkrkrrr nvdkdpaked vekakkrrgr ppaeklspnp
     1381 pkltkqmnai idtvinykdr cnvekvpsns qleiegnssg rqlsevfiql psrkelpeyy
     1441 elirkpvdfk kikerirnhk yrslgdlekd vmllchnaqt fnlegsqiye dsivlqsvfk
     1501 sarqkiakee esedesneee eeedeeeses eaksvkvkik lnkkddkgrd kgkgkkrpnr
     1561 gkakpvvsdf dsdeeqdere qsegsgtdde
//
LOCUS       NP_085143                665 aa            linear   PRI 20-NOV-2025
DEFINITION  dual specificity protein phosphatase 16 [Homo sapiens].
ACCESSION   NP_085143 XP_039106
VERSION     NP_085143.1
DBSOURCE    REFSEQ: accession NM_030640.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Shillingford,S., Zhang,L., Surovtseva,Y., Dorry,S., Lolis,E. and
            Bennett,A.M.
  TITLE     A novel site on dual-specificity phosphatase MKP7/DUSP16 is
            required for catalysis and MAPK binding
  JOURNAL   J Biol Chem 298 (12), 102617 (2022)
   PUBMED   36272649
  REMARK    GeneRIF: A novel site on dual-specificity phosphatase MKP7/DUSP16
            is required for catalysis and MAPK binding.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Low,H.B., Wong,Z.L., Wu,B., Kong,L.R., Png,C.W., Cho,Y.L., Li,C.W.,
            Xiao,F., Xin,X., Yang,H., Loo,J.M., Lee,F.Y.X., Tan,I.B.H.,
            DasGupta,R., Shen,H.M., Schwarz,H., Gascoigne,N.R.J., Goh,B.C.,
            Xu,X. and Zhang,Y.
  TITLE     DUSP16 promotes cancer chemoresistance through regulation of
            mitochondria-mediated cell death
  JOURNAL   Nat Commun 12 (1), 2284 (2021)
   PUBMED   33863904
  REMARK    GeneRIF: DUSP16 promotes cancer chemoresistance through regulation
            of mitochondria-mediated cell death.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Katagiri,C., Masuda,K., Urano,T., Yamashita,K., Araki,Y.,
            Kikuchi,K. and Shima,H.
  TITLE     Phosphorylation of Ser-446 determines stability of MKP-7
  JOURNAL   J Biol Chem 280 (15), 14716-14722 (2005)
   PUBMED   15689616
  REMARK    GeneRIF: activation of the ERK pathway strongly blocks JNK
            activation through stabilization of MKP-7 mediated by
            phosphorylation
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Hoornaert,I., Marynen,P., Goris,J., Sciot,R. and Baens,M.
  TITLE     MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for
            chromosome region 12p12-13, reduces BCR-ABL-induced transformation
  JOURNAL   Oncogene 22 (49), 7728-7736 (2003)
   PUBMED   14586399
  REMARK    GeneRIF: context-dependent role for DUSP16 on cell transformation
            and apoptosis.
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Masuda,K., Shima,H., Katagiri,C. and Kikuchi,K.
  TITLE     Activation of ERK induces phosphorylation of MAPK phosphatase-7, a
            JNK specific phosphatase, at Ser-446
  JOURNAL   J Biol Chem 278 (34), 32448-32456 (2003)
   PUBMED   12794087
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Willoughby,E.A., Perkins,G.R., Collins,M.K. and Whitmarsh,A.J.
  TITLE     The JNK-interacting protein-1 scaffold protein targets MAPK
            phosphatase-7 to dephosphorylate JNK
  JOURNAL   J Biol Chem 278 (12), 10731-10736 (2003)
   PUBMED   12524447
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Masuda,K., Shima,H., Watanabe,M. and Kikuchi,K.
  TITLE     MKP-7, a novel mitogen-activated protein kinase phosphatase,
            functions as a shuttle protein
  JOURNAL   J Biol Chem 276 (42), 39002-39011 (2001)
   PUBMED   11489891
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Tanoue,T., Yamamoto,T., Maeda,R. and Nishida,E.
  TITLE     A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and
            p38 alpha and beta MAPKs
  JOURNAL   J Biol Chem 276 (28), 26629-26639 (2001)
   PUBMED   11359773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092824.13, DB094627.1,
            AF506796.1 and AC007619.23.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 26, 2004 this sequence version replaced XP_039106.2.
            
            Summary: This gene encodes a mitogen-activated protein kinase
            phosphatase that is a member of the dual specificity protein
            phosphatase subfamily. These phosphatases inactivate their target
            kinases by dephosphorylating both the phosphoserine/threonine and
            phosphotyrosine residues. The encoded protein specifically
            regulates the c-Jun amino-terminal kinase (JNK) and extracellular
            signal-regulated kinase (ERK) pathways.[provided by RefSeq, May
            2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2222091.1,
                                           SRR1803614.86187.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298573.9/ ENSP00000298573.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..665
                     /product="dual specificity protein phosphatase 16"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="MAPK phosphatase-7; MAP kinase phosphatase 7;
                     mitogen-activated protein kinase phosphatase 7"
                     /calculated_mol_wt=72971
     Region          10..136
                     /region_name="DSP_MapKP"
                     /note="N-terminal regulatory rhodanese domain of dual
                     specificity phosphatases (DSP), such as Mapk Phosphatase.
                     This domain is believed to determine substrate specificity
                     by binding the substrate, such as ERK2, and activating the
                     C-terminal catalytic domain by...; cd01446"
                     /db_xref="CDD:238723"
     Site            55..57
                     /site_type="active"
                     /note="putative substrate binding residues [active]"
                     /db_xref="CDD:238723"
     Site            55
                     /site_type="acetylation"
                     /note="(Microbial infection) N6-acetyllysine, by EIS.
                     /evidence=ECO:0000269|PubMed:22547814; propagated from
                     UniProtKB/Swiss-Prot (Q9BY84.1)"
     Region          157..301
                     /region_name="DSP_DUSP16"
                     /note="dual specificity phosphatase domain of dual
                     specificity protein phosphatase 16; cd14646"
                     /db_xref="CDD:350494"
     Region          321..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY84.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000269|PubMed:12794087; propagated from
                     UniProtKB/Swiss-Prot (Q9BY84.1)"
     Region          449..505
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY84.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BY84.1)"
     Region          597..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY84.1)"
     CDS             1..665
                     /gene="DUSP16"
                     /gene_synonym="MKP-7; MKP7"
                     /coded_by="NM_030640.3:1113..3110"
                     /db_xref="CCDS:CCDS8650.1"
                     /db_xref="GeneID:80824"
                     /db_xref="HGNC:HGNC:17909"
                     /db_xref="MIM:607175"
ORIGIN      
        1 mahemigtqi vterlvalle sgtekvllid srpfveynts hileaininc sklmkrrlqq
       61 dkvliteliq hsakhkvdid csqkvvvydq ssqdvaslss dcfltvllgk leksfnsvhl
      121 laggfaefsr cfpglcegks tlvptcisqp clpvanigpt rilpnlylgc qrdvlnkelm
      181 qqngigyvln asntcpkpdf ipeshflrvp vndsfcekil pwldksvdfi ekakasngcv
      241 lvhclagisr satiaiayim krmdmsldea yrfvkekrpt ispnfnflgq lldyekkikn
      301 qtgasgpksk lkllhlekpn epvpavsegg qksetplspp cadsatseaa gqrpvhpasv
      361 psvpsvqpsl ledsplvqal sglhlsadrl edsnklkrsf sldiksvsys asmaaslhgf
      421 sssedaleyy kpsttldgtn klcqfspvqe lseqtpetsp dkeeasipkk lqtarpsdsq
      481 skrlhsvrts ssgtaqrsll splhrsgsve dnyhtsflfg lstsqqhltk saglglkgwh
      541 sdilapqtst psltsswyfa tesshfysas aiyggsasys ayscsqlptc gdqvysvrrr
      601 qkpsdradsr rswheespfe kqfkrrscqm efgesimsen rsreelgkvg sqssfsgsme
      661 iievs
//
LOCUS       NP_001186064             425 aa            linear   PRI 20-NOV-2025
DEFINITION  TRAF family member-associated NF-kappa-B activator isoform a [Homo
            sapiens].
ACCESSION   NP_001186064
VERSION     NP_001186064.1
DBSOURCE    REFSEQ: accession NM_001199135.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Li,S., Guo,Y., Hu,H., Gao,N., Yan,X., Zhou,Q. and Liu,H.
  TITLE     TANK shapes an immunosuppressive microenvironment and predicts
            prognosis and therapeutic response in glioma
  JOURNAL   Front Immunol 14, 1138203 (2023)
   PUBMED   37215097
  REMARK    GeneRIF: TANK shapes an immunosuppressive microenvironment and
            predicts prognosis and therapeutic response in glioma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Sui,L., Zhao,Y., Wang,W., Wu,P., Wang,Z., Yu,Y., Hou,Z., Tan,G. and
            Liu,Q.
  TITLE     SARS-CoV-2 Membrane Protein Inhibits Type I Interferon Production
            Through Ubiquitin-Mediated Degradation of TBK1
  JOURNAL   Front Immunol 12, 662989 (2021)
   PUBMED   34084167
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Mazzone,P., Congestri,M., Scudiero,I., Polvere,I., Voccola,S.,
            Zerillo,L., Telesio,G., Vito,P., Stilo,R. and Zotti,T.
  TITLE     UBAC1/KPC2 Regulates TLR3 Signaling in Human Keratinocytes through
            Functional Interaction with the CARD14/CARMA2sh-TANK Complex
  JOURNAL   Int J Mol Sci 21 (24), 9365 (2020)
   PUBMED   33316896
  REMARK    GeneRIF: UBAC1/KPC2 Regulates TLR3 Signaling in Human Keratinocytes
            through Functional Interaction with the CARD14/CARMA2sh-TANK
            Complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Nomura,F., Kawai,T., Nakanishi,K. and Akira,S.
  TITLE     NF-kappaB activation through IKK-i-dependent I-TRAF/TANK
            phosphorylation
  JOURNAL   Genes Cells 5 (3), 191-202 (2000)
   PUBMED   10759890
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Pomerantz,J.L. and Baltimore,D.
  TITLE     NF-kappaB activation by a signaling complex containing TRAF2, TANK
            and TBK1, a novel IKK-related kinase
  JOURNAL   EMBO J 18 (23), 6694-6704 (1999)
   PUBMED   10581243
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Chin,A.I., Shu,J., Shan Shi,C., Yao,Z., Kehrl,J.H. and Cheng,G.
  TITLE     TANK potentiates tumor necrosis factor receptor-associated
            factor-mediated c-Jun N-terminal kinase/stress-activated protein
            kinase activation through the germinal center kinase pathway
  JOURNAL   Mol Cell Biol 19 (10), 6665-6672 (1999)
   PUBMED   10490605
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Kaye,K.M., Devergne,O., Harada,J.N., Izumi,K.M., Yalamanchili,R.,
            Kieff,E. and Mosialos,G.
  TITLE     Tumor necrosis factor receptor associated factor 2 is a mediator of
            NF-kappa B activation by latent infection membrane protein 1, the
            Epstein-Barr virus transforming protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 11085-11090 (1996)
   PUBMED   8855313
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Rothe,M., Xiong,J., Shu,H.B., Williamson,K., Goddard,A. and
            Goeddel,D.V.
  TITLE     I-TRAF is a novel TRAF-interacting protein that regulates
            TRAF-mediated signal transduction
  JOURNAL   Proc Natl Acad Sci U S A 93 (16), 8241-8246 (1996)
   PUBMED   8710854
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009313.4 and AC009299.5.
            
            Summary: The TRAF (tumor necrosis factor receptor-associated
            factor) family of proteins associate with and transduce signals
            from members of the tumor necrosis factor receptor superfamily. The
            protein encoded by this gene is found in the cytoplasm and can bind
            to TRAF1, TRAF2, or TRAF3, thereby inhibiting TRAF function by
            sequestering the TRAFs in a latent state in the cytoplasm. For
            example, the protein encoded by this gene can block TRAF2 binding
            to LMP1, the Epstein-Barr virus transforming protein, and inhibit
            LMP1-mediated NF-kappa-B activation. Three alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (3) has an alternate 5' UTR exon
            compared to variant 1. Variants 1 and 2 encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.241497.1,
                                           SRR1660807.157603.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392749.7/ ENSP00000376505.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..425
                     /product="TRAF family member-associated NF-kappa-B
                     activator isoform a"
                     /note="TRAF family member-associated NF-KAPPA-B activator;
                     TRAF-interacting protein"
                     /calculated_mol_wt=47685
     Region          1..31
                     /region_name="Necessary for interaction with ZC3H12A.
                     /evidence=ECO:0000269|PubMed:25861989"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92844.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Region          70..191
                     /region_name="Necessary for interaction with TRAF6.
                     /evidence=ECO:0000269|PubMed:25861989"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92844.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92844.2)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Region          133..186
                     /region_name="TBD"
                     /note="TBD domain; pfam12845"
                     /db_xref="CDD:463729"
     Region          133..172
                     /region_name="Interaction with TBK1 and IKBKE.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92844.2)"
     Region          172..191
                     /region_name="TRAF family member interaction"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92844.2)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            197
                     /site_type="cleavage"
                     /note="Cleavage by EMCV protease 3C.
                     /evidence=ECO:0000269|PubMed:26363073; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            272..273
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by viral Seneca
                     Valley virus protease 3C.
                     /evidence=ECO:0000269|PubMed:28566380; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            291..292
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by viral Seneca
                     Valley virus protease 3C.
                     /evidence=ECO:0000269|PubMed:28566380; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            291
                     /site_type="cleavage"
                     /note="Cleavage by EMCV protease 3C.
                     /evidence=ECO:0000269|PubMed:26363073; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q92844.2)"
     CDS             1..425
                     /gene="TANK"
                     /gene_synonym="I-TRAF; ITRAF; TRAF2"
                     /coded_by="NM_001199135.3:109..1386"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2215.1"
                     /db_xref="GeneID:10010"
                     /db_xref="HGNC:HGNC:11562"
                     /db_xref="MIM:603893"
ORIGIN      
        1 mdknigeqln kayeafrqac mdrdsavkel qqktenyeqr ireqqeqlsl qqtiidklks
       61 qlllvnstqd nnygcvplle dsetrknnlt ldqpqdkvis giareklpkv rrqevssprk
      121 etsarslgsp llhergniek tfwdlkeefh kicmlakaqk dhlsklnipd tatetqcsvp
      181 iqctdktdkq ealfkpqakd dinrgapsit svtprglcrd eedtsfesls kfnvkfppmd
      241 ndstflhstp erpgilspat seavcqekfn mefrdnpgnf vkteetlfei qgidpiasai
      301 qnlkttdktk psnlvntcir ttldraaclp pgdhnalyvn sfplldpsda pfpsldspgk
      361 airgpqqpiw kpfpnqdsds vvlsgtdsel hiprvcefcq avfppsitsr gdflrhlnsh
      421 fnget
//
LOCUS       NP_001295017             234 aa            linear   PRI 20-NOV-2025
DEFINITION  protein Largen isoform 3 [Homo sapiens].
ACCESSION   NP_001295017
VERSION     NP_001295017.1
DBSOURCE    REFSEQ: accession NM_001308088.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Thiebaut,R., Esmiol,S., Lecine,P., Mahfouz,B., Hermant,A.,
            Nicoletti,C., Parnis,S., Perroy,J., Borg,J.P., Pascoe,L.,
            Hugot,J.P. and Ollendorff,V.
  TITLE     Characterization and Genetic Analyses of New Genes Coding for NOD2
            Interacting Proteins
  JOURNAL   PLoS One 11 (11), e0165420 (2016)
   PUBMED   27812135
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Yamamoto,K., Gandin,V., Sasaki,M., McCracken,S., Li,W.,
            Silvester,J.L., Elia,A.J., Wang,F., Wakutani,Y., Alexandrova,R.,
            Oo,Y.D., Mullen,P.J., Inoue,S., Itsumi,M., Lapin,V., Haight,J.,
            Wakeham,A., Shahinian,A., Ikura,M., Topisirovic,I., Sonenberg,N.
            and Mak,T.W.
  TITLE     Largen: a molecular regulator of mammalian cell size control
  JOURNAL   Mol Cell 53 (6), 904-915 (2014)
   PUBMED   24656129
  REMARK    GeneRIF: Largen, the product of a gene PRR16, increases cell size
            upon overexpression in human cells.
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Sakai,Y., Shaw,C.A., Dawson,B.C., Dugas,D.V., Al-Mohtaseb,Z.,
            Hill,D.E. and Zoghbi,H.Y.
  TITLE     Protein interactome reveals converging molecular pathways among
            autism disorders
  JOURNAL   Sci Transl Med 3 (86), 86ra49 (2011)
   PUBMED   21653829
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Barberi,T., Willis,L.M., Socci,N.D. and Studer,L.
  TITLE     Derivation of multipotent mesenchymal precursors from human
            embryonic stem cells
  JOURNAL   PLoS Med 2 (6), e161 (2005)
   PUBMED   15971941
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM728431.1, AF242769.1 and AI572206.1.
            
            Transcript Variant: This variant (4) contains alternate 5' exon
            structure, and it thus differs in the 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (3) is shorter at the N-terminus,
            compared to isoform 1. Both variants 3 and 4 encode isoform 3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM728431.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.1"
     Protein         1..234
                     /product="protein Largen isoform 3"
                     /note="mesenchymal stem cell protein DSC54; proline-rich
                     protein 16; protein Largen"
                     /calculated_mol_wt=25175
     Region          2..234
                     /region_name="DUF4589"
                     /note="Domain of unknown function (DUF4589); pfam15252"
                     /db_xref="CDD:464592"
     CDS             1..234
                     /gene="PRR16"
                     /gene_synonym="DSC54; LARGEN"
                     /coded_by="NM_001308088.1:373..1077"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS78053.1"
                     /db_xref="GeneID:51334"
                     /db_xref="HGNC:HGNC:29654"
                     /db_xref="MIM:615931"
ORIGIN      
        1 mtdssktdtl nssssgttas slekikvqan aplikppahp sailtvlrkp npppppprlt
       61 pvkcedpkrv vptanpvktn gtllrngglp ggpnkipngd iccipnsnld kapvqllmhr
      121 pekdrcpqag prervrfnek vqyhgycpdc dtryniknre vhlhsepvhp pgkiphqgpp
      181 lpptphlppf plenggmgis hsnsfppirp atvppptapk pqktilrkst tttv
//
LOCUS       NP_000419               1821 aa            linear   PRI 20-NOV-2025
DEFINITION  latent-transforming growth factor beta-binding protein 2 precursor
            [Homo sapiens].
ACCESSION   NP_000419 NP_114424
VERSION     NP_000419.1
DBSOURCE    REFSEQ: accession NM_000428.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1821)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1821)
  AUTHORS   Gao,L., Zhang,R., Zhang,W., Lan,Y., Li,X., Cai,Q. and Liu,J.
  TITLE     Integrated bioinformatics analysis and experimental validation on
            malignant progression and immune cell infiltration of LTBP2 in
            gliomas
  JOURNAL   BMC Cancer 24 (1), 1252 (2024)
   PUBMED   39390437
  REMARK    GeneRIF: Integrated bioinformatics analysis and experimental
            validation on malignant progression and immune cell infiltration of
            LTBP2 in gliomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1821)
  AUTHORS   Bozkurt,B., Bagci,O., Uzum,S. and Cora,T.
  TITLE     A novel LTBP2 gene variant in a Turkish family with juvenile-onset
            open-angle glaucoma
  JOURNAL   Ophthalmic Genet 45 (4), 384-389 (2024)
   PUBMED   38557215
  REMARK    GeneRIF: A novel LTBP2 gene variant in a Turkish family with
            juvenile-onset open-angle glaucoma.
REFERENCE   4  (residues 1 to 1821)
  AUTHORS   Chen,J., Wan,J., Jin,J., Jin,G., Zheng,Y., Zheng,D. and Zhong,L.
  TITLE     Autosomal Dominant Weill-Marchesani-Like Syndrome in a Chinese
            Family due to Novel Haplotypic Mutations in LTBP2
  JOURNAL   Ophthalmic Res 67 (1), 340-347 (2024)
   PUBMED   38772353
  REMARK    GeneRIF: Autosomal Dominant Weill-Marchesani-Like Syndrome in a
            Chinese Family due to Novel Haplotypic Mutations in LTBP2.
REFERENCE   5  (residues 1 to 1821)
  AUTHORS   Bashir,M.M., Han,M.D., Abrams,W.R., Tucker,T., Ma,R.I., Gibson,M.,
            Ritty,T., Mecham,R. and Rosenbloom,J.
  TITLE     Analysis of the human gene encoding latent transforming growth
            factor-beta-binding protein-2
  JOURNAL   Int J Biochem Cell Biol 28 (5), 531-542 (1996)
   PUBMED   8697098
REFERENCE   6  (residues 1 to 1821)
  AUTHORS   Chambaz,E.M., Souchelnitskiy,S., Pellerin,S., Defaye,G., Cochet,C.
            and Feige,J.J.
  TITLE     Transforming growth factors-beta s: a multifunctional cytokine
            family. Implication in the regulation of adrenocortical cell
            endocrine functions
  JOURNAL   Horm Res 45 (3-5), 222-226 (1996)
   PUBMED   8964588
  REMARK    Review article
REFERENCE   7  (residues 1 to 1821)
  AUTHORS   Li,X., Yin,W., Perez-Jurado,L., Bonadio,J. and Francke,U.
  TITLE     Mapping of human and murine genes for latent TGF-beta binding
            protein-2 (LTBP2)
  JOURNAL   Mamm Genome 6 (1), 42-45 (1995)
   PUBMED   7719025
REFERENCE   8  (residues 1 to 1821)
  AUTHORS   Moren,A., Olofsson,A., Stenman,G., Sahlin,P., Kanzaki,T.,
            Claesson-Welsh,L., ten Dijke,P., Miyazono,K. and Heldin,C.H.
  TITLE     Identification and characterization of LTBP-2, a novel latent
            transforming growth factor-beta-binding protein
  JOURNAL   J Biol Chem 269 (51), 32469-32478 (1994)
   PUBMED   7798248
REFERENCE   9  (residues 1 to 1821)
  AUTHORS   Abu-Amero,K.K. and Edward,D.P.
  TITLE     Primary Congenital Glaucoma
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301314
REFERENCE   10 (residues 1 to 1821)
  AUTHORS   Marzin,P., Cormier-Daire,V. and Tsilou,E.
  TITLE     Weill-Marchesani Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301293
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013451.8 and AC005479.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 14, 2004 this sequence version replaced NP_114424.1.
            
            Summary: The protein encoded by this gene belongs to the family of
            latent transforming growth factor (TGF)-beta binding proteins
            (LTBP), which are extracellular matrix proteins with multi-domain
            structure. This protein is the largest member of the LTBP family
            possessing unique regions and with most similarity to the
            fibrillins. It has thus been suggested that it may have multiple
            functions: as a member of the TGF-beta latent complex, as a
            structural component of microfibrils, and a role in cell adhesion.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC078659.1, AB209865.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261978.9/ ENSP00000261978.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..1821
                     /product="latent-transforming growth factor beta-binding
                     protein 2 precursor"
                     /note="LTBP-2"
                     /calculated_mol_wt=191198
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3873
     Region          <31..165
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          38..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Region          81..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Region          94..115
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Site            181
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          229..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Region          232..249
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Site            343
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          375..377
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Site            421
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08999; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          510..544
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Region          561..>595
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Site            616
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          622..>651
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(622,625,639)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          681..724
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Region          744..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Site            811
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          845..879
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          887..918
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(887,890,904)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          930..>960
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(930,933,947)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          970..1005
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(970,973,987)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1010..1041
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1010,1013,1027)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1051..1092
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Region          1093..1123
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF domain; pfam07645"
                     /db_xref="CDD:429571"
     Site            order(1093,1096,1110)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1135..1175
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1135,1138,1153)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1170
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          1176..1217
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1176,1179,1194)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1218..1249
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1218,1221,1235)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          1303..1335
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Site            order(1303,1306,1321)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Site            1309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          1423..1463
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Site            1430
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          1485..1518
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            1568
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14767.3)"
     Region          1593..1636
                     /region_name="TB"
                     /note="TB domain; pfam00683"
                     /db_xref="CDD:459903"
     Region          1639..1821
                     /region_name="C-terminal domain.
                     /evidence=ECO:0000269|PubMed:17293099"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14767.3)"
     Region          1774..>1808
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(1774,1777,1795)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     CDS             1..1821
                     /gene="LTBP2"
                     /gene_synonym="C14orf141; GLC3D; LTBP3; MSPKA; MSTP031;
                     WMS3"
                     /coded_by="NM_000428.3:294..5759"
                     /db_xref="CCDS:CCDS9831.1"
                     /db_xref="GeneID:4053"
                     /db_xref="HGNC:HGNC:6715"
                     /db_xref="MIM:602091"
ORIGIN      
        1 mrprtkarsp gralrnpwrg flpltlalfv gaghaqrdpv gryepaggda nrlrrpggsy
       61 paaaaakvys lfreqdapva glqpveraqp gwgsprrpte aearrpsraq qsrrvqppaq
      121 trrstplgqq qpaprtraap alprlgtpqr sgaapptppr grltgrnvcg gqccpgwtta
      181 nstnhcikpv ceppcqnrgs csrpqlcvcr sgfrgarcee vipdeefdpq nsrlaprrwa
      241 erspnlrrss aagegtlara qppapqsppa pqsppagtls glsqthpsqq hvglsrtvrl
      301 hptatassql ssnalppgpg leqrdgtqqa vplehpsspw glnltekikk ikivftptic
      361 kqtcarghca nscergdttt lysqgghghd pksgfriyfc qipclnggrc igrdecwcpa
      421 nstgkfchlp ipqpdreppg rgsrpralle aplkqstftl plsnqlasvn pslvkvhihh
      481 ppeasvqihq vaqvrggvee alvensvetr pppwlpaspg hslwdsnnip arsgepprpl
      541 ppaaprprgl lgrcylntvn gqcanpllel ttqedccgsv gafwgvtlca pcpprpaspv
      601 iengqlecpq gykrlnlthc qdinecltlg lckdaecvnt rgsylctcrp glmldpsrsr
      661 cvsdkaisml qglcyrslgp gtctlplaqr itkqicccsr vgkawgsece kcplpgteaf
      721 reicpaghgy tyassdirls mrkaeeeela rppreqgqrs sgalpgpaer qplrvvtdtw
      781 leagtipdkg dsqagqvtts vthapawvtg nattppmpeq giaeiqeeqv tpstdvlvtl
      841 stpgidrcaa gatnvcgpgt cvnlpdgyrc vcspgyqlhp sqayctddne clrdpckgkg
      901 rcinrvgsys cfcypgytla tsgatqecqd ineceqpgvc sggqctnteg syhcecdqgy
      961 imvrkghcqd inecrhpgtc pdgrcvnspg sytclaceeg yrgqsgscvd vnecltpgvc
     1021 ahgkctnleg sfrcsceqgy evtsdekgcq dvdecasras cptglclnte gsfacsacen
     1081 gywvnedgta cedldecafp gvcpsgvctn tagsfsckdc dggyrpsplg dscedvdece
     1141 dpqssclgge ckntvgsyqc lcpqgfqlan gtvcedvnec mgeehcaphg eclnshgsff
     1201 clcapgfvsa eggtscqdvd ecattdpcvg ghcvntegsf nclcetgfqp spesgecvdi
     1261 decedygdpv cgtwkcensp gsyrcvlgcq pgfhmapngd cididecand tmcgshgfcd
     1321 ntdgsfrclc dqgfeispsg wdcvdvnece lmlavcgaal cenvegsflc lcasdleeyd
     1381 aqeghcrprg aggqsmseap tgdhapaptr mdcysgqkgh apcssvlgrn ttqaeccctq
     1441 gaswgdacdl cpsedsaefs eicpsgkgyi pvegawtfgq tmytdadecv ifgpglcpng
     1501 rclntvpgyv clcnpgfhyd ashkkcedhd ecqdlaceng ecvntegsfh cfcsppltld
     1561 lsqqrcmnst sstedlpdhd ihmdicwkkv tndvcseplr ghrttytecc cqdgeawsqq
     1621 calcpprsse vyaqlcnvar ieaereagvh frpgyeygpg pddlhysiyg pdgapfynyl
     1681 gpedtvpepa fpntaghsad rtpilesplq pselqphyva shpeppagfe glqaeecgil
     1741 ngcengrcvr vregytcdcf egfqldaahm acvdvnecdd lngpavlcvh gycentegsy
     1801 rchcspgyva eagpphctak e
//
LOCUS       NP_001258932            1211 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium channel subfamily T member 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001258932
VERSION     NP_001258932.1
DBSOURCE    REFSEQ: accession NM_001272003.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1211)
  AUTHORS   Cole,B.A., Kalli,A.C., Pilati,N., Muench,S.P. and Lippiat,J.D.
  TITLE     A molecular switch in RCK2 triggers sodium-dependent activation of
            KNa1.1 (KCNT1) potassium channels
  JOURNAL   Biophys J 123 (14), 2145-2153 (2024)
   PUBMED   38605520
  REMARK    GeneRIF: A molecular switch in RCK2 triggers sodium-dependent
            activation of KNa1.1 (KCNT1) potassium channels.
REFERENCE   2  (residues 1 to 1211)
  AUTHORS   Yuan,T., Wang,Y., Jin,Y., Yang,H., Xu,S., Zhang,H., Chen,Q., Li,N.,
            Ma,X., Song,H., Peng,C., Geng,Z., Dong,J., Duan,G., Sun,Q.,
            Yang,Y., Yang,F. and Huang,Z.
  TITLE     Coupling of Slack and NaV1.6 sensitizes Slack to quinidine blockade
            and guides anti-seizure strategy development
  JOURNAL   Elife 12, 87559 (2024)
   PUBMED   38289338
  REMARK    GeneRIF: Coupling of Slack and NaV1.6 sensitizes Slack to quinidine
            blockade and guides anti-seizure strategy development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1211)
  AUTHORS   Zhang,J., Liu,S., Fan,J., Yan,R., Huang,B., Zhou,F., Yuan,T.,
            Gong,J., Huang,Z. and Jiang,D.
  TITLE     Structural basis of human Slo2.2 channel gating and modulation
  JOURNAL   Cell Rep 42 (8), 112858 (2023)
   PUBMED   37494189
REFERENCE   4  (residues 1 to 1211)
  AUTHORS   Hinckley,C.A., Zhu,Z., Chu,J.H., Gubbels,C., Danker,T.,
            Cherry,J.J., Whelan,C.D., Engle,S.J. and Nguyen,V.
  TITLE     Functional evaluation of epilepsy-associated KCNT1 variants in
            multiple cellular systems reveals a predominant gain of function
            impact on channel properties
  JOURNAL   Epilepsia 64 (8), 2126-2136 (2023)
   PUBMED   37177976
  REMARK    GeneRIF: Functional evaluation of epilepsy-associated KCNT1
            variants in multiple cellular systems reveals a predominant gain of
            function impact on channel properties.
REFERENCE   5  (residues 1 to 1211)
  AUTHORS   Barcia,G., Fleming,M.R., Deligniere,A., Gazula,V.R., Brown,M.R.,
            Langouet,M., Chen,H., Kronengold,J., Abhyankar,A., Cilio,R.,
            Nitschke,P., Kaminska,A., Boddaert,N., Casanova,J.L., Desguerre,I.,
            Munnich,A., Dulac,O., Kaczmarek,L.K., Colleaux,L. and Nabbout,R.
  TITLE     De novo gain-of-function KCNT1 channel mutations cause malignant
            migrating partial seizures of infancy
  JOURNAL   Nat Genet 44 (11), 1255-1259 (2012)
   PUBMED   23086397
  REMARK    GeneRIF: Our data identify KCNT1 as a major disease-associated gene
            in Malignant migrating partial seizures of infancy .
REFERENCE   6  (residues 1 to 1211)
  AUTHORS   Heron,S.E., Smith,K.R., Bahlo,M., Nobili,L., Kahana,E.,
            Licchetta,L., Oliver,K.L., Mazarib,A., Afawi,Z., Korczyn,A.,
            Plazzi,G., Petrou,S., Berkovic,S.F., Scheffer,I.E. and Dibbens,L.M.
  TITLE     Missense mutations in the sodium-gated potassium channel gene KCNT1
            cause severe autosomal dominant nocturnal frontal lobe epilepsy
  JOURNAL   Nat Genet 44 (11), 1188-1190 (2012)
   PUBMED   23086396
  REMARK    GeneRIF: Mutations in KCNT1 cause a severe form of ADNFLE and
            sporadic NFLE.
REFERENCE   7  (residues 1 to 1211)
  AUTHORS   Wei,A.D., Gutman,G.A., Aldrich,R., Chandy,K.G., Grissmer,S. and
            Wulff,H.
  TITLE     International Union of Pharmacology. LII. Nomenclature and
            molecular relationships of calcium-activated potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 463-472 (2005)
   PUBMED   16382103
  REMARK    Review article
REFERENCE   8  (residues 1 to 1211)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   9  (residues 1 to 1211)
  AUTHORS   Gertler,T., Bearden,D., Bhattacharjee,A. and Carvill,G.
  TITLE     KCNT1-Related Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30234941
REFERENCE   10 (residues 1 to 1211)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158822.19.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. This gene encodes a sodium-activated
            potassium channel subunit which is thought to function in ion
            conductance and developmental signaling pathways. Mutations in this
            gene cause the early-onset epileptic disorders, malignant migrating
            partial seizures of infancy and autosomal dominant nocturnal
            frontal lobe epilepsy. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region, uses an alternate splice site in the 5' region
            and contains an additional exon in the 3' coding region, compared
            to variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127272.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1211
                     /product="potassium channel subfamily T member 1 isoform
                     2"
                     /note="potassium channel, subfamily T, member 1; Sequence
                     like a calcium-activated K+ channel; potassium channel,
                     sodium activated subfamily T, member 1; sodium and
                     chloride-activated ATP-sensitive potassium channel Slo2.2"
                     /calculated_mol_wt=136856
     Region          114..297
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          229..305
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          459..553
                     /region_name="BK_channel_a"
                     /note="Calcium-activated BK potassium channel alpha
                     subunit; pfam03493"
                     /db_xref="CDD:460947"
     CDS             1..1211
                     /gene="KCNT1"
                     /gene_synonym="bA100C15.2; DEE14; EIEE14; ENFL5; KCa4.1;
                     KNa1.1; SLACK; Slo2.2"
                     /coded_by="NM_001272003.2:75..3710"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS65188.1"
                     /db_xref="GeneID:57582"
                     /db_xref="HGNC:HGNC:18865"
                     /db_xref="MIM:608167"
ORIGIN      
        1 mplpdgartp ggvcreargg gytnrtfefd dgqcaprvqv efyvnentfk erlklffikn
       61 qrsslrirlf nfslklltcl lyivrvlldd palgigcwgc pkqnysfnds sseinwapil
      121 wverkmtlwa iqvivaiisf letmlliyls ykgniweqif rvsfvlemin tlpfiitifw
      181 pplrnlfipv flncwlakha lenmindfhr ailrtqsamf nqvlilfctl lclvftggcr
      241 tcgiqhlera genlslltsf yfcivtfstv gygdvtpkiw psqllvvimi cvalvvlplq
      301 feelvylwme rqksggnysr hraqtekhvv lcvsslkidl lmdflnefya hprlqdyyvv
      361 ilcptemdvq vrrvlqiplw sqrviylqgs alkdqdlmra kmdngeacfi lssrnevdrt
      421 aadhqtilra wavkdfapnc plyvqilkpe nkfhvkfadh vvceeeckya mlalncicpa
      481 tstlitllvh tsrgqegqes peqwqrmygr csgnevyhir mgdskffrey egksftyaaf
      541 hahkkygvcl iglkrednks illnpgprhi laasdtcfyi nitkeensaf ifkqeekrkk
      601 rafsgqglhe gparlpvhsi iasmgtvamd lqgtehrptq sggggggskl alptengsgs
      661 rrpsiapvle ladssallpc dllsdqsede vtpsddegls vveyvkgypp nspyigsspt
      721 lchllpvkap fcclrldkgc khnsyedaka ygfknkliiv saetagngly nfivplrayy
      781 rsrkelnpiv llldnkpdhh fleaiccfpm vyymegsvdn ldsllqcgii yadnlvvvdk
      841 estmsaeedy madaktivnv qtmfrlfpsl sittelthps nmrfmqfrak dsyslalskl
      901 ekrerengsn lafmfrlpfa agrvfsisml dtllyqsfvk dymititrll lgldttpgsg
      961 ylcamkiteg dlwirtygrl fqklcsssae ipigiyrtes hvfstsephd lraqsqisvn
     1021 vedcedtrev kgpwgsragt ggssqgrhtg ggdpaehpll rrkslqwarr lsrkapkqag
     1081 raaaaewisq qrlslyrrse rqelselvkn rmkhlglptt gyedvanlta sdvmnrvnlg
     1141 ylqdemndhq ntlsyvlinp ppdtrlepsd ivylirsdpl ahvasssqsr ksscshklss
     1201 cnpetrdetq l
//
LOCUS       NP_001274066             340 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 14 isoform d [Homo sapiens].
ACCESSION   NP_001274066 XP_005250497
VERSION     NP_001274066.1
DBSOURCE    REFSEQ: accession NM_001287137.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Zhao,Y., Chen,L., Xiang,Q., Lin,J., Jiang,S. and Li,W.
  TITLE     N6-methyladenosine-modified circCDK14 promotes ossification of the
            ligamentum flavum via epigenetic modulation by targeting AFF4
  JOURNAL   Cell Mol Life Sci 81 (1), 436 (2024)
   PUBMED   39414635
  REMARK    GeneRIF: N6-methyladenosine-modified circCDK14 promotes
            ossification of the ligamentum flavum via epigenetic modulation by
            targeting AFF4.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Parmasad,J.A., Ricke,K.M., Nguyen,B., Stykel,M.G., Buchner-Duby,B.,
            Bruce,A., Geertsma,H.M., Lian,E., Lengacher,N.A., Callaghan,S.M.,
            Joselin,A., Tomlinson,J.J., Schlossmacher,M.G., Stanford,W.L.,
            Ma,J., Brundin,P., Ryan,S.D. and Rousseaux,M.W.C.
  TITLE     Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy
  JOURNAL   Cell Death Dis 15 (4), 246 (2024)
   PUBMED   38575601
  REMARK    GeneRIF: Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Zhang,M., Kan,D., Zhang,B., Chen,X., Wang,C., Chen,S., Gao,W.,
            Yang,Z., Li,Y., Chen,Y., Zhu,S., Wen,S., Niu,Y. and Shang,Z.
  TITLE     P300/SP1 complex mediating elevated METTL1 regulates CDK14 mRNA
            stability via internal m7G modification in CRPC
  JOURNAL   J Exp Clin Cancer Res 42 (1), 215 (2023)
   PUBMED   37599359
  REMARK    GeneRIF: P300/SP1 complex mediating elevated METTL1 regulates CDK14
            mRNA stability via internal m7G modification in CRPC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Yang,T., Gao,Y.K. and Chen,J.Y.
  TITLE     KIAA0202, a human septin family member, interacting with hPFTAIRE1
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (4),
            520-525 (2002)
   PUBMED   12098780
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Yang,T. and Chen,J.Y.
  TITLE     Identification and cellular localization of human PFTAIRE1
  JOURNAL   Gene 267 (2), 165-172 (2001)
   PUBMED   11313143
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Lazzaro,M.A., Albert,P.R. and Julien,J.P.
  TITLE     A novel cdc2-related protein kinase expressed in the nervous system
  JOURNAL   J Neurochem 69 (1), 348-364 (1997)
   PUBMED   9202329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC325068.1, AK296406.1, AK316026.1, BC136477.1, BP336072.1,
            DB476188.1, AB020641.1, BM740394.1 and BC152436.1.
            
            On Nov 27, 2013 this sequence version replaced XP_005250497.1.
            
            Transcript Variant: This variant (4) contains alternate 5' exon
            structure and it thus differs in the 5' UTR and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (d) has a distinct N-terminus and is shorter than
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.208073.1,
                                           SRR1803614.235150.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.13"
     Protein         1..340
                     /product="cyclin-dependent kinase 14 isoform d"
                     /EC_number="2.7.11.22"
                     /note="PFTAIRE protein kinase 1; cell division protein
                     kinase 14; serine/threonine-protein kinase PFTAIRE-1"
                     /calculated_mol_wt=38183
     Region          25..302
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..340
                     /gene="CDK14"
                     /gene_synonym="PFTAIRE1; PFTK1"
                     /coded_by="NM_001287137.1:312..1334"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS75628.1"
                     /db_xref="GeneID:5218"
                     /db_xref="HGNC:HGNC:8883"
                     /db_xref="MIM:610679"
ORIGIN      
        1 mlaltlrppp lakshlklgg tpaparvngk lvalkvirlq eeegtpftai reasllkglk
       61 hanivllhdi ihtketltlv feyvhtdlcq ymdkhpgglh pdnvklflfq llrglsyihq
      121 ryilhrdlkp qnllisdtge lkladfglar aksvpshtys nevvtlwyrp pdvllgstey
      181 stcldmwgvg cifvemiqgv aafpgmkdiq dqleriflvl gtpnedtwpg vhslphfkpe
      241 rftlyssknl rqawnklsyv nhaedlaskl lqcspknrls aqaalsheyf sdlpprlwel
      301 tdmssiftvp nvrlqpeage smrafgknns ygkslsnskh
//
LOCUS       NP_001137160            1054 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001137160
VERSION     NP_001137160.1
DBSOURCE    REFSEQ: accession NM_001143688.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 1054)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 1054)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 1054)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.129073.1,
                                           SRR1660807.228454.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319212.9/ ENSP00000321711.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..1054
                     /product="DIS3-like exonuclease 1 isoform 1"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=120657
     Region          11..188
                     /region_name="PIN_Rrp44-like"
                     /note="VapC-like PIN domain of yeast exosome subunit Rrp44
                     endoribonuclease and other eukaryotic homologs; cd09862"
                     /db_xref="CDD:350211"
     Site            order(22..26,28,30,88,92..93,100,104,118,121)
                     /site_type="other"
                     /note="exosome subunit interface [polypeptide binding]"
                     /db_xref="CDD:350211"
     Site            order(33,38,41,153)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:350211"
     Region          238..866
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          881..956
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     Site            989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF46.2)"
     CDS             1..1054
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001143688.3:30..3194"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45286.1"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mlqkrekvll lrtfqgrtlr ivrehylrpc vpchsplcpq paacshdgkl lssdvthyvi
       61 pdwkvvqdyl eilefpelkg iifmqtacqa vqhqrgrrqy nklrnllkda rhdcilfane
      121 fqqccylpre rgesmekwqt rsiynaavwy yhhcqdrmpi vmvtedeeai qqygsetegv
      181 fvitfknyld nfwpdlkaah elcdsilqsr rerenesqes hgkeypehlp levleagiks
      241 gryiqgilnv nkhraqieaf vrlqgasskd sdlvsdilih gmkarnrsih gdvvvvellp
      301 knewkgrtva lcendcddka sgespsepmp tgrvvgilqk nwrdyvvtfp skeevqsqgk
      361 naqkilvtpw dyripkiris tqqaetlqdf rvvvridswe stsvypnghf vrvlgrigdl
      421 egeiatilve nsisvipfse aqmcempvnt pespwkvspe eeqkrkdlrk shlvfsidpk
      481 gcedvddtls vrtlnngnle lgvhiadvth fvapnsyidi eartrattyy ladrrydmlp
      541 svlsadlcsl lggvdryavs imweldkasy eikkvwygrt iirsayklfy eaaqelldgn
      601 lsvvddipef kdldeksrqa kleelvwaig kltdiarhvr akrdgcgale legvevcvql
      661 ddkknihdli pkqplevhet vaecmilanh wvakkiwesf phqallrqhp pphqeffsel
      721 recakakgff idtrsnktla dsldnandph dpivnrllrs matqamsnal yfstgscaee
      781 efhhyglald kythftspir rysdivvhrl lmaaiskdkk meikgnlfsn kdleelcrhi
      841 nnrnqaaqhs qkqstelfqc myfkdkdpat eercisdgvi ysirtngvll fiprfgikga
      901 aylknkdglv iscgpdscse wkpgslqrfq nkitstttdg esvtfhlfdh vtvrisiqas
      961 rchsdtirle iisnkpykip ntelihqssp llkselvkev tksveeaqla qevkvniiqe
     1021 eyqeyrqtkg rslytlleei rdlalldvsn nygi
//
LOCUS       NP_001287907             120 aa            linear   PRI 20-NOV-2025
DEFINITION  Fanconi anemia core complex-associated protein 24 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001287907 XP_005259451
VERSION     NP_001287907.1
DBSOURCE    REFSEQ: accession NM_001300978.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Daschkey,S., Bienemann,K., Schuster,V., Kreth,H.W., Linka,R.M.,
            Honscheid,A., Fritz,G., Johannes,C., Fleckenstein,B., Kempkes,B.,
            Gombert,M., Ginzel,S. and Borkhardt,A.
  TITLE     Fatal Lymphoproliferative Disease in Two Siblings Lacking
            Functional FAAP24
  JOURNAL   J Clin Immunol 36 (7), 684-692 (2016)
   PUBMED   27473539
  REMARK    GeneRIF: This is the first report of an FAAP24 loss of function
            mutation found in human patients with EBV-associated
            lymphoproliferation.
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Yang,H., Zhang,T., Tao,Y., Wang,F., Tong,L. and Ding,J.
  TITLE     Structural insights into the functions of the FANCM-FAAP24 complex
            in DNA repair
  JOURNAL   Nucleic Acids Res 41 (22), 10573-10583 (2013)
   PUBMED   24003026
  REMARK    GeneRIF: Results show that the first HhH motif of FAAP24 is a
            potential binding site for DNA, which plays a critical role in
            targeting FANCM-FAAP24 to chromatin.
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Yan,Z., Delannoy,M., Ling,C., Daee,D., Osman,F., Muniandy,P.A.,
            Shen,X., Oostra,A.B., Du,H., Steltenpool,J., Lin,T., Schuster,B.,
            Decaillet,C., Stasiak,A., Stasiak,A.Z., Stone,S., Hoatlin,M.E.,
            Schindler,D., Woodcock,C.L., Joenje,H., Sen,R., de Winter,J.P.,
            Li,L., Seidman,M.M., Whitby,M.C., Myung,K., Constantinou,A. and
            Wang,W.
  TITLE     A histone-fold complex and FANCM form a conserved DNA-remodeling
            complex to maintain genome stability
  JOURNAL   Mol Cell 37 (6), 865-878 (2010)
   PUBMED   20347428
REFERENCE   7  (residues 1 to 120)
  AUTHORS   Collis,S.J., Ciccia,A., Deans,A.J., Horejsi,Z., Martin,J.S.,
            Maslen,S.L., Skehel,J.M., Elledge,S.J., West,S.C. and Boulton,S.J.
  TITLE     FANCM and FAAP24 function in ATR-mediated checkpoint signaling
            independently of the Fanconi anemia core complex
  JOURNAL   Mol Cell 32 (3), 313-324 (2008)
   PUBMED   18995830
  REMARK    GeneRIF: DNA damage recognition and remodeling activities of FANCM
            and FAAP24 cooperate to promote efficient activation of DNA damage
            checkpoints in Fanconi anemia.
REFERENCE   8  (residues 1 to 120)
  AUTHORS   Kim,J.M., Kee,Y., Gurtan,A. and D'Andrea,A.D.
  TITLE     Cell cycle-dependent chromatin loading of the Fanconi anemia core
            complex by FANCM/FAAP24
  JOURNAL   Blood 111 (10), 5215-5222 (2008)
   PUBMED   18174376
  REMARK    GeneRIF: FANCM is an anchor required for recruitment of the FA core
            complex to chromatin, and the FANCM/FAAP24 interaction is essential
            for this chromatin-loading activity
REFERENCE   9  (residues 1 to 120)
  AUTHORS   Gari,K., Decaillet,C., Stasiak,A.Z., Stasiak,A. and Constantinou,A.
  TITLE     The Fanconi anemia protein FANCM can promote branch migration of
            Holliday junctions and replication forks
  JOURNAL   Mol Cell 29 (1), 141-148 (2008)
   PUBMED   18206976
  REMARK    GeneRIF: FAAP24 is dispensable for DNA binding and branch migration
            activity of FANCM.
REFERENCE   10 (residues 1 to 120)
  AUTHORS   Ciccia,A., Ling,C., Coulthard,R., Yan,Z., Xue,Y., Meetei,A.R.,
            Laghmani el,H., Joenje,H., McDonald,N., de Winter,J.P., Wang,W. and
            West,S.C.
  TITLE     Identification of FAAP24, a Fanconi anemia core complex protein
            that interacts with FANCM
  JOURNAL   Mol Cell 25 (3), 331-343 (2007)
   PUBMED   17289582
  REMARK    GeneRIF: FAAP24 targets FANCM to structures that mimic
            intermediates formed during the replication/repair of damaged DNA.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD690094.1, CN368337.1, AK128668.1, BX390218.2, BC020247.1,
            BM679170.1 and AC011449.6.
            
            On Jul 17, 2014 this sequence version replaced XP_005259451.1.
            
            Summary: FAAP24 is a component of the Fanconi anemia (FA) core
            complex (see MIM 227650), which plays a crucial role in DNA damage
            response (Ciccia et al., 2007 [PubMed 17289582]).[supplied by OMIM,
            Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. It encodes isoform
            2, which is shorter at the N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CN368337.1, ERR3218366.971236.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..120
                     /product="Fanconi anemia core complex-associated protein
                     24 isoform 2"
                     /note="Fanconi anemia-associated protein of 24 kDa;
                     Fanconi anemia core complex associated protein 24"
                     /calculated_mol_wt=13061
     Region          <1..43
                     /region_name="XPF_nuclease-like"
                     /note="nuclease domain of XPF/MUS81 family proteins;
                     cl41760"
                     /db_xref="CDD:425391"
     Site            order(4,7..8,11)
                     /site_type="other"
                     /note="putative nucleic acid substrate binding site
                     [nucleotide binding]"
                     /db_xref="CDD:410852"
     Region          <14..119
                     /region_name="MUS81"
                     /note="ERCC4-type crossover junction endonuclease
                     [Replication, recombination and repair]; COG1948"
                     /db_xref="CDD:441551"
     CDS             1..120
                     /gene="FAAP24"
                     /gene_synonym="C19orf40"
                     /coded_by="NM_001300978.2:148..510"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74327.1"
                     /db_xref="GeneID:91442"
                     /db_xref="HGNC:HGNC:28467"
                     /db_xref="MIM:610884"
ORIGIN      
        1 mseqyfpalq kftvldlgmv llpvasqmea sclviqlvqe qtkepsknpl lgkkrallls
       61 epsllrtvqq ipgvgkvkap lllqkfpsiq qlsnasigel eqvvgqavaq qihafftqpr
//
LOCUS       NP_001290358             402 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 4
            [Homo sapiens].
ACCESSION   NP_001290358
VERSION     NP_001290358.1
DBSOURCE    REFSEQ: accession NM_001303429.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 402)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX507484.1, BC021622.1,
            AF028785.2, BX537388.1 and CR749649.1.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon in the central coding region compared to variant 1. The
            encoded isoform (4) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.799.1,
                                           SRR11853558.1026.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..402
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 4"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=47217
     Region          59..167
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(72,90,112,114)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(113,140)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          172..273
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Region          292..395
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(306,324,326..327,344,346)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(345,356,378,381,385)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..402
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_001303429.2:678..1886"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS76154.1"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 myntvwsmdr ddadwrevmm pystelifyi emdppalppk ppkpmtsavp ngmkdssvsl
       61 qdaewywgdi sreevndklr dmpdgtflvr dastkmqgdy tltlrkggnn klikiyhrdg
      121 kygfsdpltf nsvvelinhy hheslaqynp kldvklmypv sryqqdqlvk ednidavgkk
      181 lqeyhsqyqe kskeydrlye eytrtsqeiq mkrtaieafn etikifeeqc htqeqhskey
      241 ierfrregne keierwlnhk gvrqkrlnvw lgiknedade nyfineeden lphydektwf
      301 vedinrvqae dllygkpdga fliresskkg cyacsvvadg evkhcviyst argygfaepy
      361 nlysslkelv lhyqqtslvq hndslnvrla ypvhaqmpsl cr
//
LOCUS       NP_004350                236 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 R1 [Homo sapiens].
ACCESSION   NP_004350
VERSION     NP_004350.1
DBSOURCE    REFSEQ: accession NM_004359.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 236)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 236)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 236)
  AUTHORS   Zhang,S. and Sun,Y.
  TITLE     Targeting CDC34 E2 ubiquitin conjugating enzyme for lung cancer
            therapy
  JOURNAL   EBioMedicine 54, 102718 (2020)
   PUBMED   32268269
  REMARK    GeneRIF: Targeting CDC34 E2 ubiquitin conjugating enzyme for lung
            cancer therapy.
REFERENCE   4  (residues 1 to 236)
  AUTHORS   Zhao,X.C., Wang,G.Z., Wen,Z.S., Zhou,Y.C., Hu,Q., Zhang,B.,
            Qu,L.W., Gao,S.H., Liu,J., Ma,L., Zhang,Y.F., Zhang,C., Yu,H.,
            Zhang,D.L., Wang,M., Wang,C.L., Huang,Y.C., Liu,Z.H., Zhao,Y.,
            Chen,L. and Zhou,G.B.
  TITLE     Systematic identification of CDC34 that functions to stabilize EGFR
            and promote lung carcinogenesis
  JOURNAL   EBioMedicine 53, 102689 (2020)
   PUBMED   32114396
  REMARK    GeneRIF: Systematic identification of CDC34 that functions to
            stabilize EGFR and promote lung carcinogenesis.
REFERENCE   5  (residues 1 to 236)
  AUTHORS   Hill,S., Reichermeier,K., Scott,D.C., Samentar,L.,
            Coulombe-Huntington,J., Izzi,L., Tang,X., Ibarra,R., Bertomeu,T.,
            Moradian,A., Sweredoski,M.J., Caberoy,N., Schulman,B.A.,
            Sicheri,F., Tyers,M. and Kleiger,G.
  TITLE     Robust cullin-RING ligase function is established by a multiplicity
            of poly-ubiquitylation pathways
  JOURNAL   Elife 8, e51163 (2019)
   PUBMED   31868589
  REMARK    GeneRIF: UBE2R2 alone had negligible ubiquitylation activity at
            physiological concentrations and the ablation of UBE2R1/2 had no
            effect on the stability of SCF substrates in cells. A genome-wide
            CRISPR screen revealed that an additional E2 enzyme, UBE2G1,
            buffers against the loss of UBE2R1/2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 236)
  AUTHORS   Song,A., Wang,Q., Goebl,M.G. and Harrington,M.A.
  TITLE     Phosphorylation of nuclear MyoD is required for its rapid
            degradation
  JOURNAL   Mol Cell Biol 18 (9), 4994-4999 (1998)
   PUBMED   9710583
REFERENCE   7  (residues 1 to 236)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   8  (residues 1 to 236)
  AUTHORS   Pagano,M.
  TITLE     Cell cycle regulation by the ubiquitin pathway
  JOURNAL   FASEB J 11 (13), 1067-1075 (1997)
   PUBMED   9367342
  REMARK    Review article
REFERENCE   9  (residues 1 to 236)
  AUTHORS   King,R.W., Deshaies,R.J., Peters,J.M. and Kirschner,M.W.
  TITLE     How proteolysis drives the cell cycle
  JOURNAL   Science 274 (5293), 1652-1659 (1996)
   PUBMED   8939846
  REMARK    Review article
REFERENCE   10 (residues 1 to 236)
  AUTHORS   Plon,S.E., Leppig,K.A., Do,H.N. and Groudine,M.
  TITLE     Cloning of the human homolog of the CDC34 cell cycle gene by
            complementation in yeast
  JOURNAL   Proc Natl Acad Sci U S A 90 (22), 10484-10488 (1993)
   PUBMED   8248134
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011531.7 and AC011556.9.
            
            Summary: The protein encoded by this gene is a member of the
            ubiquitin-conjugating enzyme family. Ubiquitin-conjugating enzyme
            catalyzes the covalent attachment of ubiquitin to other proteins.
            This protein is a part of the large multiprotein complex, which is
            required for ubiquitin-mediated degradation of cell cycle G1
            regulators, and for the initiation of DNA replication. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009850.2, SRR1163655.656271.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215574.9/ ENSP00000215574.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..236
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..236
                     /product="ubiquitin-conjugating enzyme E2 R1"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2-32 KDA
                     complementing; ubiquitin carrier protein;
                     ubiquitin-protein ligase R1; ubiquitin-conjugating enzyme
                     E2-CDC34; cell division cycle 34 homolog; E2
                     ubiquitin-conjugating enzyme R1; (E3-independent) E2
                     ubiquitin-conjugating enzyme R1; cell division cycle 34,
                     ubiqiutin conjugating enzyme"
                     /calculated_mol_wt=26606
     Region          11..180
                     /region_name="UBCc_UBE2R"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin-conjugating enzyme E2 R1-R2 and
                     related proteins; cd23803"
                     /db_xref="CDD:467423"
     Region          98..113
                     /region_name="Important for ubiquitin transfer.
                     /evidence=ECO:0000269|PubMed:38326650"
                     /note="propagated from UniProtKB/Swiss-Prot (P49427.2)"
     Region          190..236
                     /region_name="SCF-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P49427.2)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11546811,
                     ECO:0000269|PubMed:17461777; propagated from
                     UniProtKB/Swiss-Prot (P49427.2)"
     Region          216..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49427.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11546811,
                     ECO:0000269|PubMed:17461777; propagated from
                     UniProtKB/Swiss-Prot (P49427.2)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11546811,
                     ECO:0000269|PubMed:12037680, ECO:0000269|PubMed:17461777;
                     propagated from UniProtKB/Swiss-Prot (P49427.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK2.
                     /evidence=ECO:0000269|PubMed:11546811; propagated from
                     UniProtKB/Swiss-Prot (P49427.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11546811; propagated from
                     UniProtKB/Swiss-Prot (P49427.2)"
     CDS             1..236
                     /gene="CDC34"
                     /gene_synonym="E2-CDC34; UBC3; UBCH3; UBE2R1"
                     /coded_by="NM_004359.2:173..883"
                     /db_xref="CCDS:CCDS12030.1"
                     /db_xref="GeneID:997"
                     /db_xref="HGNC:HGNC:1734"
                     /db_xref="MIM:116948"
ORIGIN      
        1 marplvpssq kalllelkgl qeepvegfrv tlvdegdlyn wevaifgppn tyyeggyfka
       61 rlkfpidypy sppafrfltk mwhpniyetg dvcisilhpp vddpqsgelp serwnptqnv
      121 rtillsvisl lnepntfspa nvdasvmyrk wkeskgkdre ytdiirkqvl gtkvdaerdg
      181 vkvpttlaey cvktkapapd egsdlfyddy yedgeveeea dscfgddedd sgtees
//
LOCUS       NP_068657                644 aa            linear   PRI 20-NOV-2025
DEFINITION  fibrinogen alpha chain isoform alpha precursor [Homo sapiens].
ACCESSION   NP_068657
VERSION     NP_068657.1
DBSOURCE    REFSEQ: accession NM_021871.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Moazzeni,A., Naderi,M., Dorgalaleh,A. and Alizadeh,S.
  TITLE     Fibrinogen Aalpha gene genotyping in patients with inherited
            afibrinogenemia deficiency; a novel mutation in Iranian
            afibrinogenemia patients
  JOURNAL   Blood Coagul Fibrinolysis 34 (8), 517-522 (2023)
   PUBMED   37823427
  REMARK    GeneRIF: Fibrinogen Aalpha gene genotyping in patients with
            inherited afibrinogenemia deficiency; a novel mutation in Iranian
            afibrinogenemia patients.
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Shao,X., Ma,J., Wang,Z., Sun,M., Huang,Z., Jiang,Z., Liu,X., Li,S.
            and Liu,Y.
  TITLE     [Genetic analysis of a Chinese pedigree affected with Congenital
            dysfibrinogenemia due to variant of FGG gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 40 (11), 1324-1329 (2023)
   PUBMED   37906135
  REMARK    GeneRIF: [Genetic analysis of a Chinese pedigree affected with
            Congenital dysfibrinogenemia due to variant of FGG gene].
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Maslow,A., Cheves,T., Joyce,M.F., Apruzzese,P. and Sweeney,J.
  TITLE     Interaction Between Platelet and Fibrinogen on Clot Strength in
            Healthy Patients
  JOURNAL   J Cardiothorac Vasc Anesth 37 (6), 942-947 (2023)
   PUBMED   36933991
  REMARK    GeneRIF: Interaction Between Platelet and Fibrinogen on Clot
            Strength in Healthy Patients.
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Cortuk,M., Yildizeli,B., Kurar,E., Kayis,S.A., Tanriverdi,E. and
            Cetinkaya,E.
  TITLE     Fibrinogen-Aalpha THR312ALA Polymorphism is Associated to Chronic
            Thromboembolic Pulmonary Hypertension in Turkey
  JOURNAL   Anatol J Cardiol 27 (3), 153-159 (2023)
   PUBMED   36856592
  REMARK    GeneRIF: Fibrinogen-Aalpha THR312ALA Polymorphism is Associated to
            Chronic Thromboembolic Pulmonary Hypertension in Turkey.
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Hoppe,B.
  TITLE     Fibrinogen and factor XIII at the intersection of coagulation,
            fibrinolysis and inflammation
  JOURNAL   Thromb Haemost 112 (4), 649-658 (2014)
   PUBMED   25182841
  REMARK    Review article
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Fish,R.J. and Neerman-Arbez,M.
  TITLE     Fibrinogen gene regulation
  JOURNAL   Thromb Haemost 108 (3), 419-426 (2012)
   PUBMED   22836683
  REMARK    GeneRIF: Regulation of the fibrinogen genes from proximal promoters
            and enhancers, the influence of acute-phase stimulation,
            post-transcriptional regulation by miRNAs and functional regulatory
            variants identified in genetic studies. Review.
            Review article
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Watt,K.W., Cottrell,B.A., Strong,D.D. and Doolittle,R.F.
  TITLE     Amino acid sequence studies on the alpha chain of human fibrinogen.
            Overlapping sequences providing the complete sequence
  JOURNAL   Biochemistry 18 (24), 5410-5416 (1979)
   PUBMED   518846
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Cottrell,B.A., Strong,D.D., Watt,K.W. and Doolittle,R.F.
  TITLE     Amino acid sequence studies on the alpha chain of human fibrinogen.
            Exact location of cross-linking acceptor sites
  JOURNAL   Biochemistry 18 (24), 5405-5410 (1979)
   PUBMED   518845
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Fretto,L.J., Ferguson,E.W., Steinman,H.M. and McKee,P.A.
  TITLE     Localization of the alpha-chain cross-link acceptor sites of human
            fibrin
  JOURNAL   J Biol Chem 253 (7), 2184-2195 (1978)
   PUBMED   632262
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Blomback,B., Hessel,B. and Hogg,D.
  TITLE     Disulfide bridges in nh2 -terminal part of human fibrinogen
  JOURNAL   Thromb Res 8 (5), 639-658 (1976)
   PUBMED   936108
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494953.1, CB122305.1,
            CD608675.1, AL531808.3, AL579998.3, J00127.1 and J00128.1.
            
            Summary: This gene encodes the alpha subunit of the coagulation
            factor fibrinogen, which is a component of the blood clot.
            Following vascular injury, the encoded preproprotein is
            proteolytically processed by thrombin during the conversion of
            fibrinogen to fibrin. Mutations in this gene lead to several
            disorders, including dysfibrinogenemia, hypofibrinogenemia,
            afibrinogenemia and renal amyloidosis. Alternative splicing results
            in multiple transcript variants, at least one of which encodes an
            isoform that undergoes proteolytic processing. [provided by RefSeq,
            Jan 2016].
            
            Transcript Variant: This variant (alpha) is alternatively spliced
            in the 3' coding region and 3' UTR, resulting in a shorter isoform
            (alpha) with a different carboxy-terminus compared to isoform
            alpha-E. The encoded isoform (alpha) may undergo proteolytic
            processing similar to isoform alpha-E.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.56643.1,
                                           SRR5189664.111793.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000403106.8/ ENSP00000385981.3
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..644
                     /product="fibrinogen alpha chain isoform alpha precursor"
                     /note="fibrinogen, A alpha polypeptide"
                     /calculated_mol_wt=67661
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2114
     Region          49..191
                     /region_name="Fib_alpha"
                     /note="Fibrinogen alpha/beta chain family; pfam08702"
                     /db_xref="CDD:462570"
     Region          445..509
                     /region_name="Fibrinogen_aC"
                     /note="Fibrinogen alpha C domain; pfam12160"
                     /db_xref="CDD:432370"
     Region          <465..>644
                     /region_name="PI3K_1B_p101"
                     /note="Phosphoinositide 3-kinase gamma adapter protein
                     p101 subunit; pfam10486"
                     /db_xref="CDD:463109"
     CDS             1..644
                     /gene="FGA"
                     /gene_synonym="AMYLD2; Fib2"
                     /coded_by="NM_021871.4:56..1990"
                     /note="isoform alpha precursor is encoded by transcript
                     variant alpha"
                     /db_xref="CCDS:CCDS47152.1"
                     /db_xref="GeneID:2243"
                     /db_xref="HGNC:HGNC:3661"
                     /db_xref="MIM:134820"
ORIGIN      
        1 mfsmrivclv lsvvgtawta dsgegdflae gggvrgprvv erhqsackds dwpfcsdedw
       61 nykcpsgcrm kglidevnqd ftnrinklkn slfeyqknnk dshslttnim eilrgdfssa
      121 nnrdntynrv sedlrsriev lkrkviekvq hiqllqknvr aqlvdmkrle vdidikirsc
      181 rgscsralar evdlkdyedq qkqleqviak dllpsrdrqh lplikmkpvp dlvpgnfksq
      241 lqkvppewka ltdmpqmrme lerpggneit rggstsygtg setesprnps sagswnsgss
      301 gpgstgnrnp gssgtggtat wkpgssgpgs tgswnsgssg tgstgnqnpg sprpgstgtw
      361 npgssergsa ghwtsessvs gstgqwhses gsfrpdspgs gnarpnnpdw gtfeevsgnv
      421 spgtrreyht eklvtskgdk elrtgkekvt sgsttttrrs csktvtktvi gpdghkevtk
      481 evvtsedgsd cpeamdlgtl sgigtldgfr hrhpdeaaff dtastgktfp gffspmlgef
      541 vsetesrgse sgiftntkes sshhpgiaef psrgksssys kqftsstsyn rgdstfesks
      601 ykmadeagse adhegthstk rghaksrpvr gihtsplgkp slsp
//
LOCUS       NP_065851                777 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 80 homolog isoform a [Homo
            sapiens].
ACCESSION   NP_065851
VERSION     NP_065851.1
DBSOURCE    REFSEQ: accession NM_020800.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 777)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 777)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 777)
  AUTHORS   Bizaoui,V., Huber,C., Kohaut,E., Roume,J., Bonniere,M.,
            Attie-Bitach,T. and Cormier-Daire,V.
  TITLE     Mutations in IFT80 cause SRPS Type IV. Report of two families and
            review
  JOURNAL   Am J Med Genet A 179 (4), 639-644 (2019)
   PUBMED   30767363
  REMARK    GeneRIF: Mutations in IFT80 cause Short rib-polydactyly syndrome,
            Beemer type.
REFERENCE   4  (residues 1 to 777)
  AUTHORS   Wang,R., Deng,X., Yuan,C., Xin,H., Liu,G., Zhu,Y., Jiang,X. and
            Wang,C.
  TITLE     IFT80 Improves Invasion Ability in Gastric Cancer Cell Line via
            ift80/p75NGFR/MMP9 Signaling
  JOURNAL   Int J Mol Sci 19 (11), 3616 (2018)
   PUBMED   30453504
  REMARK    GeneRIF: IFT80 plays an important role in invasion of gastric
            cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 777)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 777)
  AUTHORS   Huang,W., Kane,J.K. and Li,M.D.
  TITLE     Identification and characterization of a long isoform of human
            IFT80, IFT80-L
  JOURNAL   Biochem Biophys Res Commun 373 (4), 653-658 (2008)
   PUBMED   18601909
  REMARK    GeneRIF: Identification and characterization of a human IFT80 long
            isoform (namely IFT80-L), the carboxyl terminus of which shares the
            protein sequence of IFT80, is reported.
REFERENCE   7  (residues 1 to 777)
  AUTHORS   Beales,P.L., Bland,E., Tobin,J.L., Bacchelli,C., Tuysuz,B.,
            Hill,J., Rix,S., Pearson,C.G., Kai,M., Hartley,J., Johnson,C.,
            Irving,M., Elcioglu,N., Winey,M., Tada,M. and Scambler,P.J.
  TITLE     IFT80, which encodes a conserved intraflagellar transport protein,
            is mutated in Jeune asphyxiating thoracic dystrophy
  JOURNAL   Nat Genet 39 (6), 727-729 (2007)
   PUBMED   17468754
  REMARK    GeneRIF: Mutations in IFT80 is associated with Jeune asphyxiating
            thoracic dystrophy
REFERENCE   8  (residues 1 to 777)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
REFERENCE   9  (residues 1 to 777)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 777)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125342.1, AB037795.1 and
            CA421514.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is part of the
            intraflagellar transport complex B and is necessary for the
            function of motile and sensory cilia. Defects in this gene are a
            cause of asphyxiating thoracic dystrophy 2 (ATD2). Three transcript
            variants encoding two different isoforms have been found for this
            gene.[provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.83383.1,
                                           SRR1803616.40152.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326448.12/ ENSP00000312778.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..777
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..777
                     /product="intraflagellar transport protein 80 homolog
                     isoform a"
                     /note="WD repeat domain 56; WD repeat-containing protein
                     56; intraflagellar transport 80 homolog"
                     /calculated_mol_wt=87904
     Region          12..50
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          17..62
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <28..293
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          104..143
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          110..145
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          145..185
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          150..183
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          186..225
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          192..225
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..265
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          232..265
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..306
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          504..542
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     Region          758..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2H3.3)"
     CDS             1..777
                     /gene="IFT80"
                     /gene_synonym="ATD2; CFAP167; FAP167; SRTD2; WDR56"
                     /coded_by="NM_020800.3:127..2460"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3188.1"
                     /db_xref="GeneID:57560"
                     /db_xref="HGNC:HGNC:29262"
                     /db_xref="MIM:611177"
ORIGIN      
        1 mrlkisllke pkhqelvscv gwttaeelys csddhqivkw nlltsettqi vklpddiypi
       61 dfhwfpkslg vkkqtqaesf vltssdgkfh lisklgrvek sveahcgavl agrwnyegta
      121 lvtvgedgqi kiwsktgmlr stlaqqgtpv ysvawgpdse kvlytagkql iikplqpnak
      181 vlqwkahdgi ilkvdwnsvn dlilsagedc kykvwdsygr plynsqpheh pitsvawapd
      241 gelfavgsfh tlrlcdktgw syalekpntg sifniawsid gtqiagacgn ghvvfahvve
      301 qhwewknfqv tltkrramqv rnvlndavdl lefrdrvika slnyahlvvs tslqcyvfst
      361 knwntpiifd lkegtvslil qaerhfllvd gssiylysye grfisspkfp gmrtdilnaq
      421 tvslsndtia irdkadekii flfeastgkp lgdgkflshk neileialdq kgltndrkia
      481 fidknrdlci tsvkrfgkee qiiklgtmvh tlawndtcni lcglqdtrfi vwyypntvyv
      541 drdilpktly erdasefskn phivsfvgnq vtirradgsl vhisitpypa ilheyvsssk
      601 wedavrlcrf vkeqtmwacl aamavanrdm ttaeiayaai geidkvqyin siknlpskes
      661 kmahillfsg niqeaeivll qaglvyqaiq ininlynwer alelavkykt hvdtvlayrq
      721 kfletfgkqe tnkrylhyae glqidwekik akiemeitke reqssssqss ksiglkp
//
LOCUS       NP_001271169            1047 aa            linear   PRI 20-NOV-2025
DEFINITION  serine-rich coiled-coil domain-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001271169 XP_005269961
VERSION     NP_001271169.1
DBSOURCE    REFSEQ: accession NM_001284240.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Shirai,Y., Okuda,T., Oshima,K. and Nadano,D.
  TITLE     Characterization of human Ccser2 as a protein tracking the
            plus-ends of microtubules
  JOURNAL   BMC Res Notes 16 (1), 198 (2023)
   PUBMED   37684684
  REMARK    GeneRIF: Characterization of human Ccser2 as a protein tracking the
            plus-ends of microtubules.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU599757.1, AC074321.10, DC349473.1, AK298966.1, AF241785.1,
            AL356115.9 and BQ028021.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005269961.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.44316.1,
                                           SRR1660809.221944.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372088.8/ ENSP00000361160.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..1047
                     /product="serine-rich coiled-coil domain-containing
                     protein 2 isoform 1"
                     /note="protein GCAP14 homolog; protein FAM190B; family
                     with sequence similarity 190, member B; serine-rich
                     coiled-coil domain-containing protein 2"
                     /calculated_mol_wt=116783
     CDS             1..1047
                     /gene="CCSER2"
                     /gene_synonym="bA486O22.1; FAM190B; Gcap14; KIAA1128"
                     /coded_by="NM_001284240.2:260..3403"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS60582.1"
                     /db_xref="GeneID:54462"
                     /db_xref="HGNC:HGNC:29197"
                     /db_xref="MIM:619944"
ORIGIN      
        1 meektqiktf lgsklpkygt ksvrstlqpm pngtpvnllg tsknsnvksy iknngsdcps
       61 shsfnwrkan kyqlcaqgve epnntqnshd kiidpekrvp tqgmfdkngi kgglksvslf
      121 tsklakpstm fvssteelnq ksfsgpsnlg kftkgtllgr tsyssintpk sqlngfygnr
      181 sagsmqrpra nscatrsssg eslaqspdss ksincekmvr sqsfshsiqn sflppssitr
      241 shsfnravdl tkpyqnqqls irvplrssml trnsrqpevl ngnehlgygf nrpyaaggkk
      301 lalpngpgvt stlgyrmvhp sllkssrspf sgtmtvdgnk nspadtcvee datvlakdra
      361 ankdqelien esyrtknnqt mkhdakmryl sddvddisls slsssdkndl sedfsddfid
      421 iedsnrtrit peemslkeek hengppqdmf dspkenekaf sktdewidis vsdrsectkh
      481 tsgnnlvspd tdyragssfe lspsdssdgt ymwdeeglep ignvhpvgsy essemnsidi
      541 lnnlescdle dddlmldvdl pedaplenve cdnmnrfdrp drnvrqpqeg fwkrppqrws
      601 gqehyhlshp dhyhhhgksd lsrgspyres plghfesygg mpffqaqkmf vdvpentvil
      661 demtlrhmvq dctavktqll klkrllhqhd gsgslhdiql slpsspeped gdkvyknedl
      721 lneikqlkde ikkkdekiql lelqlatqhi chqkckeekc tyadkytqtp wrrippqvlq
      781 pssslprptd htqgklikpq riearsecsi qdmhqggahp eesfthvlhq esnygleeqp
      841 fssgpqltmd vakstpsean lnitvnaqep yhlannqisd mqfiptslqt ppesstvdqa
      901 krvgrnqspp vgymsqpksl qllkpsilss lvpppvsess psrtptckks piittcnsak
      961 lqptssqtnl annqnlkask lrppsgsfkq kqtnspqlep qsfqaktsip rpltqrkeim
     1021 qnpngnlhsg dclasnrysr lpkpkih
//
LOCUS       NP_001354619             882 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform aaa [Homo sapiens].
ACCESSION   NP_001354619
VERSION     NP_001354619.1
DBSOURCE    REFSEQ: accession NM_001367690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 882)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 882)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 882)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..882
                     /product="SUN domain-containing protein 1 isoform aaa"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=98164
     Region          62..389
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          514..567
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(514,517..518,521,524..525,528..529,531..532,
                     535..536,538..539,542..543,545..546,549,552..553,556,
                     559..560,563..564,566..567)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          526..>659
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          644..702
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          745..880
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..882
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367690.1:52..2700"
                     /note="isoform aaa is encoded by transcript variant 53"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca gkaasgvfww
      361 lgigwyqfvt liswlnvfll trclrnickf lvlliplfll lglslrgqgn ffsflpvlnw
      421 asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl
      481 relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev rmshledilg
      541 klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd
      601 avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt
      661 hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg
      721 silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls
      781 mmihpaaftl ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm
      841 fqalkrpddt afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_001070914             310 aa            linear   PRI 20-NOV-2025
DEFINITION  tRNA-splicing endonuclease subunit Sen34 isoform 1 [Homo sapiens].
ACCESSION   NP_001070914
VERSION     NP_001070914.1
DBSOURCE    REFSEQ: accession NM_001077446.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sekulovski,S., Devant,P., Panizza,S., Gogakos,T., Pitiriciu,A.,
            Heitmeier,K., Ramsay,E.P., Barth,M., Schmidt,C., Tuschl,T.,
            Baas,F., Weitzer,S., Martinez,J. and Trowitzsch,S.
  TITLE     Assembly defects of human tRNA splicing endonuclease contribute to
            impaired pre-tRNA processing in pontocerebellar hypoplasia
  JOURNAL   Nat Commun 12 (1), 5610 (2021)
   PUBMED   34584079
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Bierhals,T., Korenke,G.C., Uyanik,G. and Kutsche,K.
  TITLE     Pontocerebellar hypoplasia type 2 and TSEN2: review of the
            literature and two novel mutations
  JOURNAL   Eur J Med Genet 56 (6), 325-330 (2013)
   PUBMED   23562994
  REMARK    Review article
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Budde,B.S., Namavar,Y., Barth,P.G., Poll-The,B.T., Nurnberg,G.,
            Becker,C., van Ruissen,F., Weterman,M.A., Fluiter,K., te Beek,E.T.,
            Aronica,E., van der Knaap,M.S., Hohne,W., Toliat,M.R., Crow,Y.J.,
            Steinling,M., Voit,T., Roelenso,F., Brussel,W., Brockmann,K.,
            Kyllerman,M., Boltshauser,E., Hammersen,G., Willemsen,M.,
            Basel-Vanagaite,L., Krageloh-Mann,I., de Vries,L.S., Sztriha,L.,
            Muntoni,F., Ferrie,C.D., Battini,R., Hennekam,R.C., Grillo,E.,
            Beemer,F.A., Stoets,L.M., Wollnik,B., Nurnberg,P. and Baas,F.
  TITLE     tRNA splicing endonuclease mutations cause pontocerebellar
            hypoplasia
  JOURNAL   Nat Genet 40 (9), 1113-1118 (2008)
   PUBMED   18711368
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Paushkin,S.V., Patel,M., Furia,B.S., Peltz,S.W. and Trotta,C.R.
  TITLE     Identification of a human endonuclease complex reveals a link
            between tRNA splicing and pre-mRNA 3' end formation
  JOURNAL   Cell 117 (3), 311-321 (2004)
   PUBMED   15109492
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   7  (residues 1 to 310)
  AUTHORS   van Dijk,T. and Baas,F.
  TITLE     TSEN54 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN256589.1, AK226013.1,
            AK054944.1 and AC245052.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a catalytic subunit of the tRNA splicing
            endonuclease, which catalyzes the removal of introns from precursor
            tRNAs. The endonuclease complex is also associated with a pre-mRNA
            3-prime end processing factor. A mutation in this gene results in
            the neurological disorder pontocerebellar hypoplasia type 2.
            Multiple alternatively spliced variants, encoding the same protein,
            have been identified.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.166534.1, BC020805.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396388.3/ ENSP00000379671.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..310
                     /product="tRNA-splicing endonuclease subunit Sen34 isoform
                     1"
                     /EC_number="4.6.1.16"
                     /note="leukocyte receptor cluster (LRC) member 5;
                     tRNA-splicing endonuclease subunit Sen34; CTD-3093M3.1;
                     tRNA-intron endonuclease Sen34; leukocyte receptor cluster
                     member 5; TSEN34 tRNA splicing endonuclease subunit"
                     /calculated_mol_wt=33521
     Region          119..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSV6.1)"
     Region          218..306
                     /region_name="tRNA-intron_lyase_C"
                     /note="catalytic C-terminal domain of the tRNA-intron
                     lyase; cd22363"
                     /db_xref="CDD:411767"
     Site            order(220,226..227,232,236,238,243..244,258,260,263..265,
                     271..272,274..276,278..280,287,292,299..306)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:411767"
     Site            order(232,263..265,271..272,274..275,289,292,300..306)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:411767"
     Site            order(247,255,286)
                     /site_type="active"
                     /db_xref="CDD:411767"
     CDS             1..310
                     /gene="TSEN34"
                     /gene_synonym="LENG5; PCH2C; SEN34; SEN34L"
                     /coded_by="NM_001077446.4:58..990"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42609.1"
                     /db_xref="GeneID:79042"
                     /db_xref="HGNC:HGNC:15506"
                     /db_xref="MIM:608754"
ORIGIN      
        1 mlvvevangr slvwgaeavq alrerlgvgg rtvgalprgp rqnsrlglpl llmpeearll
       61 aeigavtlvs aprpdsrhhs laltsfkrqq eesfqeqsal aaearetrrq ellekitegq
      121 aakkqkleqa sgasssqeag ssqaakedet sdgqasgeqe eagpsssqag psngvaplpr
      181 sallvqlata rprpvkarpl dwrvqskdwp hagrpahelr ysiyrdlwer gfflsaagkf
      241 ggdflvypgd plrfhahyia qcwapedtip lqdlvaagrl gtsvrktlll cspqpdgkvv
      301 ytslqwaslq
//
LOCUS       NP_001354666             492 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform d [Homo sapiens].
ACCESSION   NP_001354666
VERSION     NP_001354666.1
DBSOURCE    REFSEQ: accession NM_001367737.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006001.2 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (21), as well as variants 22-24,
            encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.37439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..492
                     /product="rab5 GDP/GTP exchange factor isoform d"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56831
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          159..221
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          271..371
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..492
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367737.1:159..1637"
                     /note="isoform d is encoded by transcript variant 21"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkaeiqe
      121 akapspsinr qtsietdrvs kefieflktf hktgqeiykq tklflegmhy krdlsieeqs
      181 ecaqdfyhnv aermqtrgkv ppervekimd qiekyimtrl ykyvfcpett ddekkdlaiq
      241 kriralrwvt pqmlcvpvne dipevsdmvv kaitdiiemd skrvprdkla citkcskhif
      301 naikitknep asaddflptl iyivlkgnpp rlqsniqyit rfcnpsrlmt gedgyyftnl
      361 ccavafiekl daqslnlsqe dfdrymsgqt sprkqeaesw spdaclgvkq myknldllsq
      421 lnerqerimn eakklekdli dwtdgiarev qdivekyple ikppnqplaa idsenvendk
      481 lppplqpqvy ag
//
LOCUS       NP_002215               2671 aa            linear   PRI 20-NOV-2025
DEFINITION  inositol 1,4,5-trisphosphate-gated calcium channel ITPR3 [Homo
            sapiens].
ACCESSION   NP_002215
VERSION     NP_002215.2
DBSOURCE    REFSEQ: accession NM_002224.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2671)
  AUTHORS   Blanco,E., Camps,C., Bahal,S., Kerai,M.D., Ferla,M.P.,
            Rochussen,A.M., Handel,A.E., Golwala,Z.M., Spiridou Goncalves,H.,
            Kricke,S., Klein,F., Zhang,F., Zinghirino,F., Evans,G., Keane,T.M.,
            Lizot,S., Kusters,M.A.A., Iro,M.A., Patel,S.V., Morris,E.C.,
            Burns,S.O., Radcliffe,R., Vasudevan,P., Price,A., Gillham,O.,
            Valdebenito,G.E., Stewart,G.S., Worth,A., Adams,S.P., Duchen,M.,
            Andre,I., Adams,D.J., Santili,G., Gilmour,K.C., Hollander,G.A.,
            Davies,E.G., Taylor,J.C., Griffiths,G.M., Thrasher,A.J., Dhalla,F.
            and Kreins,A.Y.
  TITLE     Dominant negative variants in ITPR3 impair T cell Ca2+ dynamics
            causing combined immunodeficiency
  JOURNAL   J Exp Med 222 (1) (2025)
   PUBMED   39560673
REFERENCE   2  (residues 1 to 2671)
  AUTHORS   Molitor,A., Lederle,A., Radosavljevic,M., Sapuru,V., Zavorka
            Thomas,M.E., Yang,J., Shirin,M., Collin-Bund,V., Jerabkova-Roda,K.,
            Miao,Z., Bernard,A., Rolli,V., Grenot,P., Castro,C.N.,
            Rosenzwajg,M., Lewis,E.G., Person,R., Esperon-Moldes,U.S.,
            Kaare,M., Nokelainen,P.T., Batzir,N.A., Hoffer,G.Z., Paul,N.,
            Stemmelen,T., Naegely,L., Hanauer,A., Bibi-Triki,S., Grun,S.,
            Jung,S., Busnelli,I., Tripolszki,K., Al-Ali,R., Ordonez,N.,
            Bauer,P., Song,E., Zajo,K., Partida-Sanchez,S., Robledo-Avila,F.,
            Kumanovics,A., Louzoun,Y., Hirschler,A., Pichot,A., Toker,O.,
            Mejia,C.A.M., Parvaneh,N., Knapp,E., Hersh,J.H., Kenney,H.,
            Delmonte,O.M., Notarangelo,L.D., Goetz,J.G., Kahwash,S.B.,
            Carapito,C., Bajwa,R.P.S., Thomas,C., Ehl,S., Isidor,B.,
            Carapito,R., Abraham,R.S., Hite,R.K., Marcus,N., Bertoli-Avella,A.
            and Bahram,S.
  TITLE     A pleiotropic recurrent dominant ITPR3 variant causes a complex
            multisystemic disease
  JOURNAL   Sci Adv 10 (37), eado5545 (2024)
   PUBMED   39270020
  REMARK    GeneRIF: A pleiotropic recurrent dominant ITPR3 variant causes a
            complex multisystemic disease.
REFERENCE   3  (residues 1 to 2671)
  AUTHORS   Paknejad,N., Sapuru,V. and Hite,R.K.
  TITLE     Structural titration reveals Ca2+-dependent conformational
            landscape of the IP3 receptor
  JOURNAL   Nat Commun 14 (1), 6897 (2023)
   PUBMED   37898605
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2671)
  AUTHORS   Chen,J., Zhou,J., Jiang,Y., Wang,Y., Chen,C., Jiang,T. and Du,J.
  TITLE     Inositol 1,4,5-trisphosphate receptor gene variants are related to
            the risk of breast cancer in a Chinese population
  JOURNAL   J Gene Med 25 (2), e3463 (2023)
   PUBMED   36350267
  REMARK    GeneRIF: Inositol 1,4,5-trisphosphate receptor gene variants are
            related to the risk of breast cancer in a Chinese population.
REFERENCE   5  (residues 1 to 2671)
  AUTHORS   Neumann,J., Van Nieuwenhove,E., Terry,L.E., Staels,F., Knebel,T.R.,
            Welkenhuyzen,K., Ahmadzadeh,K., Baker,M.R., Gerbaux,M.,
            Willemsen,M., Barber,J.S., Serysheva,I.I., De Waele,L.,
            Vermeulen,F., Schlenner,S., Meyts,I., Yule,D.I., Bultynck,G.,
            Schrijvers,R., Humblet-Baron,S. and Liston,A.
  TITLE     Disrupted Ca2+ homeostasis and immunodeficiency in patients with
            functional IP3 receptor subtype 3 defects
  JOURNAL   Cell Mol Immunol 20 (1), 11-25 (2023)
   PUBMED   36302985
  REMARK    GeneRIF: Disrupted Ca[2+] homeostasis and immunodeficiency in
            patients with functional IP3 receptor subtype 3 defects.
            Erratum:[Cell Mol Immunol. 2023 Jan;20(1):114. doi:
            10.1038/s41423-022-00960-4. PMID: 36471115]
REFERENCE   6  (residues 1 to 2671)
  AUTHORS   Joseph,S.K., Lin,C., Pierson,S., Thomas,A.P. and Maranto,A.R.
  TITLE     Heteroligomers of type-I and type-III inositol trisphosphate
            receptors in WB rat liver epithelial cells
  JOURNAL   J Biol Chem 270 (40), 23310-23316 (1995)
   PUBMED   7559486
  REMARK    Erratum:[J Biol Chem 1996 Mar 29;271(13):7874]
REFERENCE   7  (residues 1 to 2671)
  AUTHORS   Maranto,A.R.
  TITLE     Primary structure, ligand binding, and localization of the human
            type 3 inositol 1,4,5-trisphosphate receptor expressed in
            intestinal epithelium
  JOURNAL   J Biol Chem 269 (2), 1222-1230 (1994)
   PUBMED   8288584
REFERENCE   8  (residues 1 to 2671)
  AUTHORS   Yamamoto-Hino,M., Sugiyama,T., Hikichi,K., Mattei,M.G.,
            Hasegawa,K., Sekine,S., Sakurada,K., Miyawaki,A., Furuichi,T.,
            Hasegawa,M. et al.
  TITLE     Cloning and characterization of human type 2 and type 3 inositol
            1,4,5-trisphosphate receptors
  JOURNAL   Recept Channels 2 (1), 9-22 (1994)
   PUBMED   8081734
REFERENCE   9  (residues 1 to 2671)
  AUTHORS   Bourguignon,L.Y., Jin,H., Iida,N., Brandt,N.R. and Zhang,S.H.
  TITLE     The involvement of ankyrin in the regulation of inositol
            1,4,5-trisphosphate receptor-mediated internal Ca2+ release from
            Ca2+ storage vesicles in mouse T-lymphoma cells
  JOURNAL   J Biol Chem 268 (10), 7290-7297 (1993)
   PUBMED   8385102
REFERENCE   10 (residues 1 to 2671)
  AUTHORS   Mahaut-Smith,M.P., Sage,S.O. and Rink,T.J.
  TITLE     Receptor-activated single channels in intact human platelets
  JOURNAL   J Biol Chem 265 (18), 10479-10483 (1990)
   PUBMED   1693919
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139044.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 26, 2007 this sequence version replaced NP_002215.1.
            
            Summary: This gene encodes a receptor for inositol
            1,4,5-trisphosphate, a second messenger that mediates the release
            of intracellular calcium. The receptor contains a calcium channel
            at the C-terminus and the ligand-binding site at the N-terminus.
            Knockout studies in mice suggest that type 2 and type 3 inositol
            1,4,5-trisphosphate receptors play a key role in exocrine secretion
            underlying energy metabolism and growth. [provided by RefSeq, Aug
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U01062.1, D26351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000605930.3/ ENSP00000475177.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..2671
                     /product="inositol 1,4,5-trisphosphate-gated calcium
                     channel ITPR3"
                     /note="inositol 1,4,5-triphosphate receptor, type 3;
                     insP3R3; type 3 InsP3 receptor; IP3 receptor"
                     /calculated_mol_wt=303977
     Region          4..230
                     /region_name="Ins145_P3_rec"
                     /note="Inositol 1,4,5-trisphosphate/ryanodine receptor;
                     pfam08709"
                     /db_xref="CDD:462572"
     Region          225..439
                     /region_name="beta-trefoil_MIR_ITPR3"
                     /note="MIR domain, beta-trefoil fold, found in inositol
                     1,4,5-trisphosphate receptor type 3 (ITPR3) and similar
                     proteins; cd23289"
                     /db_xref="CDD:467760"
     Site            order(246..247,249,372..374,386,425..426,428)
                     /site_type="other"
                     /note="homotetramer interface [polypeptide binding]"
                     /db_xref="CDD:467760"
     Site            order(266,268..270,276)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:467760"
     Region          322..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Region          475..670
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Site            916
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            934
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14573.2)"
     Region          1132..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Region          1191..1303
                     /region_name="RYDR_ITPR"
                     /note="RIH domain; pfam01365"
                     /db_xref="CDD:460175"
     Region          1809..1848
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            1813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14573.2)"
     Site            1832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            1834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14573.2)"
     Region          1865..1974
                     /region_name="RIH_assoc"
                     /note="RyR and IP3R Homology associated; pfam08454"
                     /db_xref="CDD:462482"
     Site            2203..2223
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2236..2256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Region          2265..2528
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            2265..2285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2326..2346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2369..2389
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2497..2517
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14573.2)"
     Site            2670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14573.2)"
     CDS             1..2671
                     /gene="ITPR3"
                     /gene_synonym="CMT1J; IMD132; IMD133; IP3R; IP3R-3; IP3R3"
                     /coded_by="NM_002224.4:282..8297"
                     /db_xref="CCDS:CCDS4783.1"
                     /db_xref="GeneID:3710"
                     /db_xref="HGNC:HGNC:6182"
                     /db_xref="MIM:147267"
ORIGIN      
        1 msemssflhi gdivslyaeg svngfistlg lvddrcvvep aagdldnppk kfrdclfkvc
       61 pmnrysaqkq ywkakqtkqd kekiadvvll qklqhaaqme qkqndtenkk vhgdvvkygs
      121 viqllhmksn kyltvnkrlp alleknamrv tldatgnegs wlfiqpfwkl rsngdnvvvg
      181 dkvilnpvna gqplhasnye lsdnagckev nsvncntswk inlfmqfrdh leevlkggdv
      241 vrlfhaeqek fltcdeykgk lqvflrttlr qsatsatssn alwevevvhh dpcrggaghw
      301 nglyrfkhla tgnylaaeen psykgdasdp kaagmgaqgr tgrrnageki kyclvavphg
      361 ndiaslfeld pttlqktdsf vprnsyvrlr hlctntwiqs tnvpidieee rpirlmlgtc
      421 ptkedkeafa ivsvpvseir dldfandass mlasavekln egfisqndrr fviqlledlv
      481 ffvsdvpnng qnvldimvtk pnrerqklmr eqnilkqvfg ilkapfrekg gegplvrlee
      541 lsdqknapyq hmfrlcyrvl rhsqedyrkn qehiakqfgm mqsqigydil aedtitallh
      601 nnrkllekhi tktevetfvs lvrknreprf ldylsdlcvs nhiaipvtqe lickcvldpk
      661 nsdilirtel rpvkemaqsh eylsieysee evwltwtdkn nehheksvrq laqearagna
      721 hdenvlsyyr yqlklfarmc ldrqylaide isqqlgvdli flcmademlp fdlrasfchl
      781 mlhvhvdrdp qelvtpvkfa rlwteiptai tikdydsnln asrddkknkf antmefvedy
      841 lnnvvseavp faneeknklt fevvslahnl iyfgfysfse llrltrtllg iidcvqgppa
      901 mlqayedpgg knvrrsiqgv ghmmstmvls rkqsvfsaps lsagasaaep ldrskfeene
      961 divvmetklk ileilqfiln vrldyrisyl lsvfkkefve vfpmqdsgad gtapafdstt
     1021 anmnldrige qaeamfgvgk tssmlevdde ggrmflrvli hltmhdyapl vsgalqllfk
     1081 hfsqrqeamh tfkqvqllis aqdvenykvi kseldrlrtm vekselwvdk kgsgkgeeve
     1141 agaakdkker ptdeegflhp pgekssenyq ivkgilerln kmcgvgeqmr kkqqrllknm
     1201 dahkvmldll qipydkgdak mmeilrythq flqkfcagnp gnqallhkhl hlfltpglle
     1261 aetmqhifln nyqlcseise pvlqhfvhll athgrhvqyl dflhtvikae gkyvkkcqdm
     1321 imteltnagd dvvvfyndka slahlldmmk aardgvedhs plmyhislvd llaacaegkn
     1381 vyteikctsl lpledvvsvv thedcitevk mayvnfvnhc yvdtevemke iytsnhiwtl
     1441 fenftldmar vcskrekrva dptlekyvls vvldtinaff sspfsensts lqthqtivvq
     1501 llqsttrlle cpwlqqqhkg sveacirtla mvakgraill pmdldahiss mlssgascaa
     1561 aaqrnassyk attrafprvt ptanqwdykn iieklqdiit aleerlkplv qaelsvlvdv
     1621 lhwpellfle gseayqrces ggflskliqh tkdlmeseek lcikvlrtlq qmllkktkyg
     1681 drgnqlrkml lqnylqnrks tsrgdlpdpi gtgldpdwsa iaatqcrldk egatklvcdl
     1741 itstknekif qesiglaihl ldggnteiqk sfhnlmmsdk kserffkvlh drmkraqqet
     1801 kstvavnmnd lgsqphedre pvdpttkgrv asfsipgsss ryslgpslrr ghevservqs
     1861 semgtsvlim qpilrflqll cenhnrdlqn flrcqnnktn ynlvcetlqf ldimcgsttg
     1921 glgllglyin ednvglviqt letlteycqg pchenqtciv thesngidii talilndisp
     1981 lckyrmdlvl qlkdnaskll lalmesrhds enaerilisl rpqelvdvik kaylqeeere
     2041 nsevsprevg hniyilalql srhnkqlqhl lkpvkriqee eaegissmls lnnkqlsqml
     2101 kssapaqeee edplayyenh tsqieivrqd rsmeqivfpv pgicqfltee tkhrlfttte
     2161 qdeqgskvsd ffdqssflhn emewqrklrs mpliywfsrr mtlwgsisfn lavfiniiia
     2221 ffypymegas tgvldsplis llfwilicfs iaalftkrys irplivalil rsiyylgigp
     2281 tlnilgalnl tnkivfvvsf vgnrgtfirg ykamvmdmef lyhvgyilts vlglfahelf
     2341 ysillfdliy reetlfnvik svtrngrsil ltallalilv ylfsivgflf lkddfilevd
     2401 rlpnnhstas plgmphgaaa fvdtcsgdkm dcvsglsvpe vleedrelds teracdtllm
     2461 civtvmnhgl rngggvgdil rkpskdeslf parvvydllf ffiviiivln lifgviidtf
     2521 adlrsekqkk eeilkttcfi cglerdkfdn ktvsfeehik lehnmwnyly fivlvrvknk
     2581 tdytgpesyv aqmiknknld wfprmramsl vsnegegeqn eirilqdkln stmklvshlt
     2641 aqlnelkeqm teqrkrrqrl gfvdvqncis r
//
LOCUS       NP_055426               5596 aa            linear   PRI 20-NOV-2025
DEFINITION  midasin [Homo sapiens].
ACCESSION   NP_055426
VERSION     NP_055426.1
DBSOURCE    REFSEQ: accession NM_014611.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 5596)
  AUTHORS   Zhou,H., Stein,C.B., Shafiq,T.A., Shipkovenska,G., Kalocsay,M.,
            Paulo,J.A., Zhang,J., Luo,Z., Gygi,S.P., Adelman,K. and Moazed,D.
  TITLE     Rixosomal RNA degradation contributes to silencing of Polycomb
            target genes
  JOURNAL   Nature 604 (7904), 167-174 (2022)
   PUBMED   35355014
REFERENCE   2  (residues 1 to 5596)
  AUTHORS   Raman,N., Weir,E. and Muller,S.
  TITLE     The AAA ATPase MDN1 Acts as a SUMO-Targeted Regulator in Mammalian
            Pre-ribosome Remodeling
  JOURNAL   Mol Cell 64 (3), 607-615 (2016)
   PUBMED   27814492
REFERENCE   3  (residues 1 to 5596)
  AUTHORS   Romes,E.M., Sobhany,M. and Stanley,R.E.
  TITLE     The Crystal Structure of the Ubiquitin-like Domain of Ribosome
            Assembly Factor Ytm1 and Characterization of Its Interaction with
            the AAA-ATPase Midasin
  JOURNAL   J Biol Chem 291 (2), 882-893 (2016)
   PUBMED   26601951
  REMARK    GeneRIF: the crystal structure of the UBL domain of the WDR12
            homologue from S. cerevisiae at 1.7 A resolution is reported and
            demonstrated that human midasin binds to WDR12 as well as Nle1
            through their respective UBL domains.
REFERENCE   4  (residues 1 to 5596)
  AUTHORS   Finkbeiner,E., Haindl,M. and Muller,S.
  TITLE     The SUMO system controls nucleolar partitioning of a novel
            mammalian ribosome biogenesis complex
  JOURNAL   EMBO J 30 (6), 1067-1078 (2011)
   PUBMED   21326211
REFERENCE   5  (residues 1 to 5596)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   6  (residues 1 to 5596)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   7  (residues 1 to 5596)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 5596)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 5596)
  AUTHORS   Garbarino,J.E. and Gibbons,I.R.
  TITLE     Expression and genomic analysis of midasin, a novel and highly
            conserved AAA protein distantly related to dynein
  JOURNAL   BMC Genomics 3, 18 (2002)
   PUBMED   12102729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP360573.1, AF503925.1, AL096678.8, BC036888.1 and AK027048.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF503925.1, SRR14038193.867704.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369393.8/ ENSP00000358400.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..5596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..5596
                     /product="midasin"
                     /note="MIDAS-containing protein; MDN1, midasin homolog;
                     dynein-related AAA-ATPase MDN1"
                     /calculated_mol_wt=632692
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          307..591
                     /region_name="AAA-ATPase protomer 1.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          325..453
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            329..336
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(330..337,401)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            397..402
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Region          480..604
                     /region_name="AAA_lid_7"
                     /note="Midasin AAA lid domain; pfam17867"
                     /db_xref="CDD:465540"
     Region          517..537
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          659..978
                     /region_name="AAA-ATPase protomer 2.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          659..>780
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          672..902
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            677..684
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(678..685,750)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            order(747,748..751)
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Region          915..1017
                     /region_name="AAA_lid_5"
                     /note="Midasin AAA lid domain; pfam17865"
                     /db_xref="CDD:407722"
     Region          1048..1316
                     /region_name="AAA-ATPase protomer 3.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          1079..1215
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            1084..1091
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(1085..1092,1151,1194)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            1148..1152
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            1214
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
     Region          1227..1328
                     /region_name="AAA_lid_7"
                     /note="Midasin AAA lid domain; pfam17867"
                     /db_xref="CDD:465540"
     Region          1362..1616
                     /region_name="AAA-ATPase protomer 4.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          1385..1540
                     /region_name="AAA_5"
                     /note="AAA domain (dynein-related subfamily); pfam07728"
                     /db_xref="CDD:400191"
     Site            1390..1397
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(1391..1398,1468,1522)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            1464..1469
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            1539
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
     Site            1683
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          1738..1995
                     /region_name="AAA-ATPase protomer 5.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          1748..1888
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            1753..1760
                     /site_type="other"
                     /note="Walker A motif"
                     /db_xref="CDD:99707"
     Site            order(1754..1761,1823,1868)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:99707"
     Site            1754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            1819..1824
                     /site_type="other"
                     /note="Walker B motif"
                     /db_xref="CDD:99707"
     Site            1887
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:99707"
     Region          1900..1999
                     /region_name="AAA_lid_7"
                     /note="Midasin AAA lid domain; pfam17867"
                     /db_xref="CDD:465540"
     Region          2053..2313
                     /region_name="AAA-ATPase protomer 6.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          <2220..2306
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Region          2418..4691
                     /region_name="Linker.
                     /evidence=ECO:0000250|UniProtKB:Q12019"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          3989..4008
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4212
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          4669..4688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          <4687..5321
                     /region_name="MDN1"
                     /note="Midasin, AAA ATPase with vWA domain, involved in
                     ribosome maturation [Translation, ribosomal structure and
                     biogenesis]; COG5271"
                     /db_xref="CDD:444083"
     Region          4700..5260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4889
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4898
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4937
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            4946
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Site            5015
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NU22.2)"
     Region          5323..5593
                     /region_name="vWA_midasin"
                     /note="VWA_Midasin: Midasin is a member of the AAA ATPase
                     family. The proteins of this family are unified by their
                     common archetectural organization that is based upon a
                     conserved ATPase domain. The AAA domain of midasin
                     contains six tandem AAA protomers. The...; cd01460"
                     /db_xref="CDD:238737"
     Site            order(5390,5392,5394,5461,5497)
                     /site_type="active"
                     /note="metal ion dependent adhesion site (MIDAS) [active]"
                     /db_xref="CDD:238737"
     CDS             1..5596
                     /gene="MDN1"
                     /gene_synonym="Rea1"
                     /coded_by="NM_014611.3:188..16978"
                     /db_xref="CCDS:CCDS5024.1"
                     /db_xref="GeneID:23195"
                     /db_xref="HGNC:HGNC:18302"
                     /db_xref="MIM:618200"
ORIGIN      
        1 mehfllevaa aplrliaakn eksrselgrf lakqvwtpqd rqcvlstlaq llldkdctvl
       61 vgrqlrplll dllernaeai kaggqinhdl herlcvsmsk lignhpdvlp falryfkdts
      121 pvfqrlfles sdanpvrygr rrmklrdlme aafkflqqeq svfrelwdws vcvpllrshd
      181 tlvrwytanc lalvtcmnee hklsflkkif nsdelihfrl rlleeaqlqd lekalvlanp
      241 evslwrkqke lqylqghlvs sdlsprvtav cgvvlpgqlp apgelggnrs ssreqelalr
      301 syvlvesvck slqtlamava sqnavllegp igcgktslve ylaavtgrtk ppqllkvqlg
      361 dqtdskmllg myrctdvpge fvwqpgtltq aatmghwill edidyapldv vsvlipllen
      421 gellipgrgd clkvapgfqf fatrrllscg gnwyrplnsh atlldkywtk ihldnldkre
      481 lnevlqsryp sllavvdhll diyiqltgek hhswsdssvg ceqapeevse arrenkrptl
      541 egrelslrdl lnwcnriahs fdssslsasl nifqealdcf tamlsehtsk lkmaevigsk
      601 lnisrkkaef fcqlykpeiv ineldlqvgr vrllrkqsea vhlqrekftf aatrpssvli
      661 eqlavcvskg epvllvgetg tgktstiqyl ahitghrlrv vnmnqqsdta dllggykpvd
      721 hkliwlplre afeelfaqtf skkqnftflg hiqtcyrqkr whdllrlmqh vhksavnkdg
      781 kdsetgllik ekweafglrl nhaqqqmkmt entllfafve gtlaqavkkg ewilldeinl
      841 aapeilecls gllegssgsl vlldrgdtep lvrhpdfrlf acmnpatdvg krnlppgirn
      901 rftelyveel eskedlqvli vdylkglsvn kntvqgiinf ytalrkesgt klvdgtghrp
      961 hyslrtlcra lrfaasnpcg niqrslyegf clgfltqldr ashpivqkli cqhivpgnvk
     1021 sllkqpipep kggrliqveg ywiavgdkep tidetyilts svklnlrdiv rvvsagtypv
     1081 liqgetsvgk tsliqwlaaa tgnhcvrinn hehtdiqeyi gcytsdssgk lvfkegvlid
     1141 amrkgywiil delnlaptdv lealnrlldd nrellvtetq evvkahprfm lfatqnppgl
     1201 yggrkvlsra frnrfvelhf delpsselet ilhkrcslpp sycsklvkvm ldlqsyrrss
     1261 svfagkqgfi tlrdlfrwae ryrlaeptek eydwlqhlan dgymllagrv rkqeeidviq
     1321 evlekhfkkk lcpqslfske nvlkllgkls tqistlecnf ghivwtegmr rlamlvgral
     1381 efgepvllvg dtgcgkttic qvfaalanqk lysvschlhm etsdflgglr pvrqkpndke
     1441 eidtsrlfew hdgplvqamk edgfflldei sladdsvler lnsvleveks lvlaekgspe
     1501 dkdseiellt agkkfrilat mnpggdfgkk elspalrnrf teiwcpqsts redliqiish
     1561 nlrpglclgr idpkgsdipe vmldfidwlt hqefgrkcvv sirdilswvn fmnkmgeeaa
     1621 lkrpeiistv tsfvhaaclv yidgigsgvt ssgfgtalla rkeclkflik rlakivrlte
     1681 yqknelkiyd rmkakeftgi dnlwgihpff iprgpvlhrn niadyalsag ttamnaqrll
     1741 ratklkkpil legspgvgkt slvgalakas gntlvrinls eqtditdlfg adlpveggkg
     1801 gefawrdgpl laalkaghwv vldelnlasq svleglnacf dhrgeiyvpe lgmsfqvqhe
     1861 ktkifgcqnp frqgggrkgl prsflnrftq vfvdpltvid mefiastlfp aieknivkkm
     1921 vafnnqidhe vtvekkwgqk ggpwefnlrd lfrwcqlmlv dqspgcydpg qhvflvyger
     1981 mrteedkkkv iavfkdvfgs nsnpymgtrl fritpydvql gysvlsrgsc vphpsrhpll
     2041 llhqsfqple simkcvqmsw mvilvgpasv gktslvqlla hltghtlkim amnsamdtte
     2101 llggfeqvdl irpwrrllek vegtvrallr dsllisadda evvlrawshf lltykpkclg
     2161 eggkaitmei vnkleavlll mqrlnnkins yckaefaklv eefrsfgvkl tqlasghshg
     2221 tfewvdsmlv qalksgdwll mdnvnfcnps vldrlnalle pggvltiser gmidgstpti
     2281 tpnpnfrlfl smdpvhgdis ramrnrglei yisgegdast pdnldlkvll hslglvgnsv
     2341 cdillalhte trstvvgspt ssvstliqta ilivqylqrg lsldrafsea cwevyvcsqh
     2401 spanrklvqa llekhvsslr ahetwgdsil gmglwpdsvp salfatedsh lstvrrdgqi
     2461 lvyclnrmsm ktsswtrsqp ftlqdlekim qspspenlkf navevntywi depdvlvmav
     2521 kllieratnq dwmlrvkwly hlaknipqgl esiqihleas aaslrnfysh slsgavsnvf
     2581 kilqpnttde fvipldprwn mqaldmirnl mdfdpqtdqp dqlfallesa anktiiyldr
     2641 ekrvfteanl vsvgskklre svlrmsfefh qdpesyhtlp heivvnlaaf felcdalvll
     2701 wvqssqgmvs dasaneilgs lrwrdrfwtv adtvkvdapg lallalhwhw vlkhlvhqip
     2761 rllmnyedky ykevqtvseh iqnclgsqtg gfagikklqk flgrpfpfkd klvvecfsql
     2821 kvlnkvlair eqmsalgesg wqedinrlqv vasqwtlkks llqawglilr aniledvsld
     2881 elknfvhaqc lelkakglsl gflekkhdea sslshpdlts vihltrsvql wpameylaml
     2941 wrykvtadfm aqaclrrcsk nqqpqineei shlisfclyh tpvtpqelrd lwsllhhqkv
     3001 speeitslws elfnsmfmsf wsstvttnpe ywlmwnplpg mqqreapksv ldstlkgpgn
     3061 lnrpifskcc fevltsswra spwdvsglpi lssshvtlge wvertqqlqd issmlwtnma
     3121 issvaefrrt dsqlqgqvlf rhlaglaell pesrrqeymq nceqlllgss qafqhvgqtl
     3181 gdmagqevlp kellcqllts lhhfvgeges krslpepaqr gslwvslgll qiqtwlpqar
     3241 fdpavkreyk lnyvkeelhq lqcewktrnl ssqlqtgrdl edevvvsysh phvrllrqrm
     3301 drldnltchl lkkqafrpql payeslvqei hhyvtsiaka pavqdlltrl lqalhidgpr
     3361 saqvaqsllk eeaswqqshh qfrkrlseey tfypdavspl qasilqlqhg mrlvaselht
     3421 slhssmvgad rlgtlatall afpsvgptfp tyyahadtlc svkseevlrg lgklilkrsg
     3481 gkelegkgqk acptreqllm nallylrshv lckgeldqra lqlfrhvcqe iisewdeqer
     3541 iaqekaeqes glyryrsrns rtalseeeee erefrkqfpl hekdfadilv qptleenkgt
     3601 sdgqeeeagt npallsqnsm qavmlihqql clnfarslwy qqtlppheak hylslflscy
     3661 qtgaslvthf yplmgvelnd rllgsqllac tlshntlfge apsdlmvkpd gpydfyqhpn
     3721 vpearqcqpv lqgfseavsh llqdwpehpa leqllvvmdr irsfplsspi skflngleil
     3781 lakaqdween asralslrkh ldlisqmiir wrklelncws msldntmkrh tekstkhwfs
     3841 iyqmlekhmq eqteeqeddk qmtlmllvst lqafiegssl gefhvrlqml lvfhchvllm
     3901 pqvegkdslc svlwnlyhyy kqffdrvqak ivelrsplek elkefvkisk wndvsfwsik
     3961 qsvekthrtl fkfmkkfeav lsepcrsslv esdkeeqpdf lprptdgaas elssiqnlnr
     4021 alretllaqp aagqatipew cqgaapsgle gellrrlpkl rkrmrkmclt fmkesplprl
     4081 vegldqftge vissvselqs lkvepsaeke kqrseakhil mqkqralsdl fkhlakigls
     4141 yrkglawars knpqemlhlh pldlqsalsi vsstqeadsr llteissswd gcqkyfyrsl
     4201 arharlnaal atpakemgmg nvercrgfsa hlmkmlvrqr rslttlseqw iilrnllscv
     4261 qeihsrlmgp qaypvafppq dgvqqwterl qhlamqcqil leqlswllqc cpsvgpapgh
     4321 gnvqvlgqpp gpclegpels kgqlcgvvld lipsnlsyps pipgsqlpsg crmrkqdhlw
     4381 qqsttrltem lktiktvkad vdkirqqsce tlfhswkdfe vcssalscls qvsvhlqgle
     4441 slfilpgmev eqrdsqmalv esleyvrgei skamadfttw kthlltsdsq ggnqmldegf
     4501 vedfseqmei airailcaiq nleerkneka eentdqaspq edyagferlq sghltklled
     4561 dfwadvstlh vqkiisaise llerlksyge dgtaakhlff sqscsllvrl vpvlssysdl
     4621 vlffltmsla thrstaklls vlaqvftela qkgfclpkef medsagegat efhdyegggi
     4681 gegegmkdvs dqigneeqve dtfqkgqekd kedpdsksdi kgednaiems edfdgkmhdg
     4741 eleeqeedde ksdseggdld khmgdlngee adklderlwg dddeeedeee ednkteetgp
     4801 gmdeedselv akddnldsgn snkdksqqdk keekeeaead dggqgedkin eqiderdyde
     4861 nevdpyhgnq ekvpepeald lpddlnldse dknggedtdn eegeeenple ikekpeeagh
     4921 eaeergetet dqnesqspqe peegpseddk aegeeemdtg addqdgdaaq hpeehseeqq
     4981 qsveekdkea deeggengpa dqgfqpqeee eredsdteeq vpealerkeh ascgqtgven
     5041 mqntqamela gaapekeqgk eehgsgaada nqaeghesnf iaqlasqkht rkntqsfkrk
     5101 pgqadnersm gdhnervhkr lrtvdtdsha eqgpaqqpqa qvedadafeh ikqgsdayda
     5161 qtydvaskeq qqsakdsgkd qeeeeiedtl mdteeqeefk aadveqlkpe eiksgttapl
     5221 gfdemeveiq tvkteedqdp rtdkahkete nekpersres tihtahqflm dtifqpflkd
     5281 vnelrqeler qlemwqpres gnpeeekvaa emwqsylilt aplsqrlcee lrlileptqa
     5341 aklkgdyrtg krlnirkvip yiasqfrkdk iwlrrtkpsk rqyqiclaid dsssmvdnht
     5401 kqlafeslav ignaltllev gqiavcsfge svkllhpfhe qfsdysgsqi lrlckfqqkk
     5461 tkiaqflesv anmfaaaqql sqnissetaq lllvvsdgrg lflegkervl aavqaarnan
     5521 ifvifvvldn pssrdsildi kvpifkgpge mpeirsymee fpfpyyiilr dvnalpetls
     5581 dalrqwfelv tasdhp
//
LOCUS       NP_056139                456 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal RNA-processing protein 8 [Homo sapiens].
ACCESSION   NP_056139
VERSION     NP_056139.1
DBSOURCE    REFSEQ: accession NM_015324.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Waku,T., Nakajima,Y., Yokoyama,W., Nomura,N., Kako,K.,
            Kobayashi,A., Shimizu,T. and Fukamizu,A.
  TITLE     NML-mediated rRNA base methylation links ribosomal subunit
            formation to cell proliferation in a p53-dependent manner
  JOURNAL   J Cell Sci 129 (12), 2382-2393 (2016)
   PUBMED   27149924
  REMARK    GeneRIF: NML depletion increases 60S ribosomal protein L11 (RPL11)
            levels in the ribosome-free fraction and protein levels of p53
            through an RPL11-MDM2 complex, which activates the p53 pathway.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Murayama,A., Ohmori,K., Fujimura,A., Minami,H., Yasuzawa-Tanaka,K.,
            Kuroda,T., Oie,S., Daitoku,H., Okuwaki,M., Nagata,K., Fukamizu,A.,
            Kimura,K., Shimizu,T. and Yanagisawa,J.
  TITLE     Epigenetic control of rDNA loci in response to intracellular energy
            status
  JOURNAL   Cell 133 (4), 627-639 (2008)
   PUBMED   18485871
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX417992.2, BC001071.2, AB007869.1, R51624.1 and AC009796.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB007869.1, SRR1803612.183196.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254605.11/ ENSP00000254605.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..456
                     /product="ribosomal RNA-processing protein 8"
                     /note="RRP8 methyltransferase homolog; nucleomethylin;
                     cerebral protein 1; ribosomal RNA processing 8,
                     methyltransferase, homolog"
                     /calculated_mol_wt=50584
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43159.2)"
     Region          52..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43159.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43159.2)"
     Region          242..456
                     /region_name="Methyltransf_8"
                     /note="Hypothetical methyltransferase; pfam05148"
                     /db_xref="CDD:398698"
     Site            order(315..319,334..335,345..347,363)
                     /site_type="other"
                     /note="S-adenosylmethionine binding site [chemical
                     binding]"
                     /db_xref="CDD:100107"
     CDS             1..456
                     /gene="RRP8"
                     /gene_synonym="KIAA0409; NML"
                     /coded_by="NM_015324.4:115..1485"
                     /db_xref="CCDS:CCDS31411.1"
                     /db_xref="GeneID:23378"
                     /db_xref="HGNC:HGNC:29030"
                     /db_xref="MIM:615818"
ORIGIN      
        1 mfeepewaea apvaaglgpv isrpppaass qnkgskrrql latlraleaa slsqhppslc
       61 isdseeeeee rkkkcpkkas fasasaevgk kgkkkcqkqg ppcsdseeev erkkkchkqa
      121 lvgsdsaede krkrkcqkha pinsaqhldn vdqtgpkawk gsttndppkq spgstspkpp
      181 htlsrkqwrn rqknkrrckn kfqppqvpdq apaeaptekt evspvprtds hearagalra
      241 rmaqrldgar frylneqlys gpssaaqrlf qedpeaflly hrgfqsqvkk wplqpvdria
      301 rdlrqrpasl vvadfgcgdc rlassirnpv hcfdlasldp rvtvcdmaqv pledesvdva
      361 vfclslmgtn irdfleeanr vlkpggllkv aevssrfedv rtflravtkl gfkivskdlt
      421 nshfflfdfq ktgpplvgpk aqlsglqlqp clykrr
//
LOCUS       NP_742077                517 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 4 [Homo sapiens].
ACCESSION   NP_742077
VERSION     NP_742077.1
DBSOURCE    REFSEQ: accession NM_172080.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Borghi,R., Trivisano,M., Specchio,N., Tartaglia,M. and
            Compagnucci,C.
  TITLE     Understanding the pathogenetic mechanisms underlying altered
            neuronal function associated with CAMK2B mutations
  JOURNAL   Neurosci Biobehav Rev 152, 105299 (2023)
   PUBMED   37391113
  REMARK    GeneRIF: Understanding the pathogenetic mechanisms underlying
            altered neuronal function associated with CAMK2B mutations.
            Review article
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Nicole,O. and Pacary,E.
  TITLE     CaMKIIbeta in Neuronal Development and Plasticity: An Emerging
            Candidate in Brain Diseases
  JOURNAL   Int J Mol Sci 21 (19), 7272 (2020)
   PUBMED   33019657
  REMARK    GeneRIF: CaMKIIbeta in Neuronal Development and Plasticity: An
            Emerging Candidate in Brain Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Penades,J.R., Bernal,D., Revert,F., Johansson,C., Fresquet,V.J.,
            Cervera,J., Wieslander,J., Quinones,S. and Saus,J.
  TITLE     Characterization and expression of multiple alternatively spliced
            transcripts of the Goodpasture antigen gene region. Goodpasture
            antibodies recognize recombinant proteins representing the
            autoantigen and one of its alternative forms
  JOURNAL   Eur J Biochem 229 (3), 754-760 (1995)
   PUBMED   7758473
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Schworer,C.M., Colbran,R.J., Keefer,J.R. and Soderling,T.R.
  TITLE     Ca2+/calmodulin-dependent protein kinase II. Identification of a
            regulatory autophosphorylation site adjacent to the inhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 263 (27), 13486-13489 (1988)
   PUBMED   3417668
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550751.1, AF083419.1,
            AC006454.4 and AK290148.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a beta chain.
            It is possible that distinct isoforms of this chain have different
            cellular localizations and interact differently with calmodulin.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (4), also known as beta e, lacks
            an in-frame segment of the coding region, compared to variant 1. It
            encodes a shorter isoform (4), also known as beta e subunit, that
            is missing an internal segment compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.203689.1,
                                           SRR1660803.244469.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..517
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 4"
                     /EC_number="2.7.11.17"
                     /note="CaM kinase II beta subunit; CaM-kinase II beta
                     chain; proline rich calmodulin-dependent protein kinase;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit beta; caMK-II subunit beta"
                     /calculated_mol_wt=57807
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          291..301
                     /region_name="calmodulin-binding domain"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          385..512
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..517
                     /gene="CAMK2B"
                     /gene_synonym="CAM2; CAMK2; CAMKB; CaMKIIbeta; MRD54"
                     /coded_by="NM_172080.3:174..1727"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS43573.1"
                     /db_xref="GeneID:816"
                     /db_xref="HGNC:HGNC:1461"
                     /db_xref="MIM:607707"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsaksll nkkadgvkpq tnstknsaaa tspkgtlppa alepqttvih
      361 npvdgikess dsanttiede dakarkqeii ktteqlieav nngdfeayak icdpgltsfe
      421 pealgnlveg mdfhrfyfen llaknskpih ttilnphvhv igedaaciay irltqyidgq
      481 grprtsqsee trvwhrrdgk wqnvhfhcsg apvaplq
//
LOCUS       NP_000361                278 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-tocopherol transfer protein isoform 1 [Homo sapiens].
ACCESSION   NP_000361 XP_001128514
VERSION     NP_000361.1
DBSOURCE    REFSEQ: accession NM_000370.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Jeridi,C., Rachdi,A., Nabli,F., Saied,Z., Zouari,R., Ben
            Mohamed,D., Ben Said,M., Masmoudi,S., Ben Sassi,S. and Amouri,R.
  TITLE     Genetic heterogeneity within a consanguineous family involving TTPA
            and SETX genes
  JOURNAL   J Neurogenet 37 (4), 124-130 (2023)
   PUBMED   38109176
  REMARK    GeneRIF: Genetic heterogeneity within a consanguineous family
            involving TTPA and SETX genes.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Ulatowski,L., Ghelfi,M., West,R., Atkinson,J., Finno,C.J. and
            Manor,D.
  TITLE     The tocopherol transfer protein mediates vitamin E trafficking
            between cerebellar astrocytes and neurons
  JOURNAL   J Biol Chem 298 (3), 101712 (2022)
   PUBMED   35150738
  REMARK    GeneRIF: The tocopherol transfer protein mediates vitamin E
            trafficking between cerebellar astrocytes and neurons.
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Arai,H. and Kono,N.
  TITLE     alpha-Tocopherol transfer protein (alpha-TTP)
  JOURNAL   Free Radic Biol Med 176, 162-175 (2021)
   PUBMED   34563650
  REMARK    GeneRIF: alpha-Tocopherol transfer protein (alpha-TTP).
            Review article
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Gotoda,T., Arita,M., Arai,H., Inoue,K., Yokota,T., Fukuo,Y.,
            Yazaki,Y. and Yamada,N.
  TITLE     Adult-onset spinocerebellar dysfunction caused by a mutation in the
            gene for the alpha-tocopherol-transfer protein
  JOURNAL   N Engl J Med 333 (20), 1313-1318 (1995)
   PUBMED   7566022
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Arita,M., Sato,Y., Miyata,A., Tanabe,T., Takahashi,E., Kayden,H.J.,
            Arai,H. and Inoue,K.
  TITLE     Human alpha-tocopherol transfer protein: cDNA cloning, expression
            and chromosomal localization
  JOURNAL   Biochem J 306 (Pt 2) (Pt 2), 437-443 (1995)
   PUBMED   7887897
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Ouahchi,K., Arita,M., Kayden,H., Hentati,F., Ben Hamida,M.,
            Sokol,R., Arai,H., Inoue,K., Mandel,J.L. and Koenig,M.
  TITLE     Ataxia with isolated vitamin E deficiency is caused by mutations in
            the alpha-tocopherol transfer protein
  JOURNAL   Nat Genet 9 (2), 141-145 (1995)
   PUBMED   7719340
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Ben Hamida,C., Doerflinger,N., Belal,S., Linder,C., Reutenauer,L.,
            Dib,C., Gyapay,G., Vignal,A., Le Paslier,D., Cohen,D. et al.
  TITLE     Localization of Friedreich ataxia phenotype with selective vitamin
            E deficiency to chromosome 8q by homozygosity mapping
  JOURNAL   Nat Genet 5 (2), 195-200 (1993)
   PUBMED   8252047
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Schuelke,M.
  TITLE     Ataxia with Vitamin E Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301419
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC058000.1, BC041784.1 and
            AC120042.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 20, 2006 this sequence version replaced XP_001128514.1.
            
            Summary: This gene encodes a soluble protein that binds
            alpha-trocopherol, a form of vitamin E, with high selectivity and
            affinity. This protein plays an important role in regulating
            vitamin E levels in the body by transporting vitamin E between
            membrane vesicles and facilitating the secretion of vitamin E from
            hepatocytes to circulating lipoproteins. Mutations in this gene
            cause hereditary vitamin E deficiency (ataxia with vitamin E
            deficiency, AVED) and retinitis pigmentosa. [provided by RefSeq,
            Nov 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.123094.1, BC041784.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260116.5/ ENSP00000260116.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q12.3"
     Protein         1..278
                     /product="alpha-tocopherol transfer protein isoform 1"
                     /note="tocopherol (alpha) transfer protein (ataxia
                     (Friedreich-like) with vitamin E deficiency); alpha-TTP"
                     /calculated_mol_wt=31619
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49638.1)"
     Region          <40..73
                     /region_name="CRAL_TRIO_N"
                     /note="CRAL/TRIO, N-terminal domain; smart01100"
                     /db_xref="CDD:215024"
     Region          99..247
                     /region_name="CRAL_TRIO"
                     /note="CRAL/TRIO domain; pfam00650"
                     /db_xref="CDD:459890"
     CDS             1..278
                     /gene="TTPA"
                     /gene_synonym="alphaTTP; ATTP; AVED; TTP1"
                     /coded_by="NM_000370.3:33..869"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6178.1"
                     /db_xref="GeneID:7274"
                     /db_xref="HGNC:HGNC:12404"
                     /db_xref="MIM:600415"
ORIGIN      
        1 maearsqpsa gpqlnalpdh spllqpglaa lrrrareagv plaplpltds fllrflrard
       61 fdldlawrll knyykwraec peisadlhpr siigllkagy hgvlrsrdpt gskvliyria
      121 hwdpkvftay dvfrvslits elivqevetq rngikaifdl egwqfshafq itpsvakkia
      181 avltdsfplk vrgihlinep vifhavfsmi kpfltekike rihmhgnnyk qsllqhfpdi
      241 lpleyggeef smedicqewt nfimksedyl ssisesiq
//
LOCUS       NP_001273903             718 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-catulin isoform b [Homo sapiens].
ACCESSION   NP_001273903 XP_005252349
VERSION     NP_001273903.1
DBSOURCE    REFSEQ: accession NM_001286974.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Wu,D., Zhu,J., Yang,F., Li,R., Liu,L., Liu,D., Liu,C., Qu,X.,
            Liu,H., Ji,M., Qin,X., Hua,L. and Xiang,Y.
  TITLE     CTNNAL1 deficiency suppresses CFTR expression in HDM-induced asthma
            mouse model through ROCK1-CAL signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1618-1629 (2023)
   PUBMED   37715489
  REMARK    GeneRIF: CTNNAL1 deficiency suppresses CFTR expression in
            HDM-induced asthma mouse model through ROCK1-CAL signaling pathway.
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Tung,C.H., Huang,M.F., Liang,C.H., Wu,Y.Y., Wu,J.E., Hsu,C.L.,
            Chen,Y.L. and Hong,T.M.
  TITLE     alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer
  JOURNAL   Theranostics 12 (3), 1173-1186 (2022)
   PUBMED   35154481
  REMARK    GeneRIF: alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Surpili,M.J., Delben,T.M. and Kobarg,J.
  TITLE     Identification of proteins that interact with the central
            coiled-coil region of the human protein kinase NEK1
  JOURNAL   Biochemistry 42 (51), 15369-15376 (2003)
   PUBMED   14690447
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Shieh,Y.S., Chang,L.C., Chiu,K.C., Wu,C.W. and Lee,H.S.
  TITLE     Cadherin and catenin expression in mucoepidermoid carcinoma:
            correlation with histopathologic grade, clinical stage, and patient
            outcome
  JOURNAL   J Oral Pathol Med 32 (5), 297-304 (2003)
   PUBMED   12694354
  REMARK    GeneRIF: Abnormal expression of alpha-catenin was seen in
            mucoepidermoid carcinoma.
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Park,B., Nguyen,N.T., Dutt,P., Merdek,K.D., Bashar,M.,
            Sterpetti,P., Tosolini,A., Testa,J.R. and Toksoz,D.
  TITLE     Association of Lbc Rho guanine nucleotide exchange factor with
            alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports
            serum response factor activation
  JOURNAL   J Biol Chem 277 (47), 45361-45370 (2002)
   PUBMED   12270917
  REMARK    GeneRIF: Results show that alpha-catulin co-expression leads to
            increased Lbc-induced serum response factor activation and may
            modulate Rho pathway signaling in vivo by providing a scaffold for
            the Lbc Rho guanine nucleotide exchange factor.
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Janssens,B., Staes,K. and van Roy,F.
  TITLE     Human alpha-catulin, a novel alpha-catenin-like molecule with
            conserved genomic structure, but deviating alternative splicing
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 341-347 (1999)
   PUBMED   10542337
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Zhang,J.S., Nelson,M., Wang,L., Liu,W., Qian,C.P., Shridhar,V.,
            Urrutia,R. and Smith,D.I.
  TITLE     Identification and chromosomal localization of CTNNAL1, a novel
            protein homologous to alpha-catenin
  JOURNAL   Genomics 54 (1), 149-154 (1998)
   PUBMED   9806841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022926.1, AF135021.1 and AI148526.1.
            
            On Nov 21, 2013 this sequence version replaced XP_005252349.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' terminal exon, which results in an alternate 3' coding
            region, compared to variant 1. The encoded isoform (b) has a
            distinct C-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.74941.1,
                                           SRR1803611.129151.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..718
                     /product="alpha-catulin isoform b"
                     /note="alpha-catulin; alpha2-catulin; catenin alpha-like
                     protein 1; alpha-catenin-related protein; catenin
                     (cadherin-associated protein), alpha-like 1"
                     /calculated_mol_wt=80022
     Region          31..675
                     /region_name="Vinculin"
                     /note="Vinculin family; pfam01044"
                     /db_xref="CDD:460040"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88327; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     CDS             1..718
                     /gene="CTNNAL1"
                     /gene_synonym="ACRP; alpha-CATU; CLLP"
                     /coded_by="NM_001286974.2:58..2214"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS69638.1"
                     /db_xref="GeneID:8727"
                     /db_xref="HGNC:HGNC:2512"
                     /db_xref="MIM:604785"
ORIGIN      
        1 maaspgpagv ggagavygsg ssgfaldsgl eiktrsveqt llplvsqitt linhkdntkk
       61 sdktlqaiqr vgqavnlavg rfvkvgeaia nenwdlkeei niacieakqa getiaaltdi
      121 tnlnhlesdg qitiftdktg vikaarllls svtkvlllad rvvikqiits rnkvlatmer
      181 lekvnsfqef vqifsqfgne mvefahlsgd rqndlkdekk kakmaaarav lekctmmllt
      241 asktclrhpn cesahknkeg vfdrmkvald kvieivtdck pngetdissi siftgikefk
      301 mniealrenl yfqskenlsv tlevilerme dftdsaytsh ehrerilels tqarmelqql
      361 isvwiqaqsk ktksiaeele lsilkishsl nelkkelhst atqlaadllk yhadhvvlka
      421 lkltgvegnl ealaeyackl seqkeqlvet crllrhisgt epleitciha eetfqvtgqq
      481 iisaaetltl hpsskiaken ldvfceawes qisdmstllr eindvfegrr gekygylslp
      541 kpmknnanlk slkpdkpdse eqakiaklgl klglltsdad ceiekwedqe neivqygrnm
      601 ssmayslylf trgegplkts qdlihqlevf aaeglkltss vqafskqlkd ddklmlllei
      661 nkliplchql qtvtktslqn kvflkvdkci tktrsmmall vqllslcykl lkksetry
//
LOCUS       NP_116558                275 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB3 [Homo sapiens].
ACCESSION   NP_116558
VERSION     NP_116558.1
DBSOURCE    REFSEQ: accession NM_032940.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Higman,B., Shugar,D.H., Stark,C.P., Ekstrom,G., Koppes,M.N.,
            Lynett,P., Dufresne,A., Haeussler,P.J., Geertsema,M., Gulick,S.,
            Mattox,A., Venditti,J.G., Walton,M.A.L., McCall,N., Mckittrick,E.,
            MacInnes,B., Bilderback,E.L., Tang,H., Willis,M.J., Richmond,B.,
            Reece,R.S., Larsen,C., Olson,B., Capra,J., Ayca,A., Bloom,C.,
            Williams,H., Bonno,D., Weiss,R., Keen,A., Skanavis,V. and Loso,M.
  TITLE     The 2015 landslide and tsunami in Taan Fiord, Alaska
  JOURNAL   Sci Rep 8 (1), 12993 (2018)
   PUBMED   30190595
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Burke,K.A., Janke,A.M., Rhine,C.L. and Fawzi,N.L.
  TITLE     Residue-by-Residue View of In Vitro FUS Granules that Bind the
            C-Terminal Domain of RNA Polymerase II
  JOURNAL   Mol Cell 60 (2), 231-241 (2015)
   PUBMED   26455390
  REMARK    GeneRIF: FUS low-complexicity phase separates to recruit RNA
            polymerase II C-terminal domain in vitro.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Fang,Z.P., Jiang,B.G., Zhang,F.B., Wang,A.D., Ji,Y.M., Xu,Y.F.,
            Li,J.C., Zhou,W.P., Zhou,W.J. and Han,H.X.
  TITLE     Rpb3 promotes hepatocellular carcinoma through its N-terminus
  JOURNAL   Oncotarget 5 (19), 9256-9268 (2014)
   PUBMED   25211001
  REMARK    GeneRIF: These findings suggest that N-terminus of Rpb3 selectively
            inhibits Rpb3-high-expression hepatocellular carcinoma cells
            proliferation. N-terminus of Rpb3 may be useful in treating
            patients diagnosed with Rpb3-high-expression hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Corbi,N., Batassa,E.M., Pisani,C., Onori,A., Di Certo,M.G.,
            Strimpakos,G., Fanciulli,M., Mattei,E. and Passananti,C.
  TITLE     The eEF1gamma subunit contacts RNA polymerase II and binds vimentin
            promoter region
  JOURNAL   PLoS One 5 (12), e14481 (2010)
   PUBMED   21217813
  REMARK    GeneRIF: eEF1gamma, in addition to its role in translation
            elongation complex, is involved in regulating Vimentin gene by
            contacting both pol II and the Vimentin promoter region and
            shuttling/nursing the Vimentin mRNA
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Pati,U.K. and Weissman,S.M.
  TITLE     The amino acid sequence of the human RNA polymerase II 33-kDa
            subunit hRPB 33 is highly conserved among eukaryotes
  JOURNAL   J Biol Chem 265 (15), 8400-8403 (1990)
   PUBMED   2187864
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Rubinstein,M.H.
  TITLE     A new granulation method for compressed tablets [proceedings]
  JOURNAL   J Pharm Pharmacol 28 Suppl, 67P (1976)
   PUBMED   12345
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI458170.1 and BC003159.1.
            
            Summary: This gene encodes the third largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. The product of this gene contains a
            cysteine rich region and exists as a heterodimer with another
            polymerase subunit, POLR2J. These two subunits form a core
            subassembly unit of the polymerase. A pseudogene has been
            identified on chromosome 21. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003159.1, SRR3476690.801283.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219252.10/ ENSP00000219252.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..275
                     /product="DNA-directed RNA polymerase II subunit RPB3"
                     /EC_number="2.7.7.6"
                     /note="RNA polymerase II subunit 3; RPB33; polymerase
                     (RNA) II (DNA directed) polypeptide C, 33kDa; RNA
                     polymerase II subunit B3; DNA-directed RNA polymerase II
                     subunit C; polymerase (RNA) II subunit C; DNA-directed RNA
                     polymerase II 33 kDa polypeptide"
                     /calculated_mol_wt=31310
     Region          7..266
                     /region_name="RNAP_II_RPB3"
                     /note="RPB3 subunit of Eukaryotic RNA polymerase II;
                     cd07031"
                     /db_xref="CDD:132909"
     Site            order(7..9,14..15,23,27,29..30,33,36,171..172,242,246,
                     249..250,253,259..260,263,266)
                     /site_type="other"
                     /note="RPB3 - RPB11 heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:132909"
     Site            order(32,35..36,40,60,62..63,66..67,173..174,179..181,
                     183..184,186..187,194..196,198,200,203..204)
                     /site_type="other"
                     /note="RPB3 - RPB2 interaction site [polypeptide binding]"
                     /db_xref="CDD:132909"
     Site            order(47..53,61,66,172..173,175)
                     /site_type="other"
                     /note="RPB3 - RPB12 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:132909"
     Site            order(58,67,70,114,116,147..149,152,154,175,180..181,234,
                     236)
                     /site_type="other"
                     /note="RPB3 - RPB10 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:132909"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P19387.2)"
     Site            order(193,222)
                     /site_type="other"
                     /note="RPB3 - RPB8 interaction site [polypeptide binding]"
                     /db_xref="CDD:132909"
     Site            order(198..200,222)
                     /site_type="other"
                     /note="RPB3 - RPB1 interaction site [polypeptide binding]"
                     /db_xref="CDD:132909"
     Region          203..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19387.2)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19387.2)"
     CDS             1..275
                     /gene="POLR2C"
                     /gene_synonym="hRPB33; hsRPB3; RPB3; RPB31"
                     /coded_by="NM_032940.3:47..874"
                     /db_xref="CCDS:CCDS10782.1"
                     /db_xref="GeneID:5432"
                     /db_xref="HGNC:HGNC:9189"
                     /db_xref="MIM:180663"
ORIGIN      
        1 mpyanqptvr iteltdenvk fiientdlav ansirrvfia evpiiaidwv qidanssvlh
       61 defiahrlgl iplisddivd klqysrdctc eefcpecsve ftldvrcned qtrhvtsrdl
      121 isnsprvipv tsrnrdndpn dyveqddili vklrkgqelr lrayakkgfg kehakwnpta
      181 gvafeydpdn alrhtvypkp eewpkseyse ldedesqapy dpngkperfy ynvescgslr
      241 petivlsals glkkklsdlq tqlsheiqsd vltin
//
LOCUS       NP_000716                484 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-3 isoform 1
            [Homo sapiens].
ACCESSION   NP_000716
VERSION     NP_000716.2
DBSOURCE    REFSEQ: accession NM_000725.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Chen,Z., Mondal,A., Abderemane-Ali,F., Jang,S., Niranjan,S.,
            Montano,J.L., Zaro,B.W. and Minor,D.L. Jr.
  TITLE     EMC chaperone-CaV structure reveals an ion channel assembly
            intermediate
  JOURNAL   Nature 619 (7969), 410-419 (2023)
   PUBMED   37196677
  REMARK    GeneRIF: EMC chaperone-CaV structure reveals an ion channel
            assembly intermediate.
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 484)
  AUTHORS   Murakami,M., Wissenbach,U. and Flockerzi,V.
  TITLE     Gene structure of the murine calcium channel beta3 subunit, cDNA
            and characterization of alternative splicing and transcription
            products
  JOURNAL   Eur J Biochem 236 (1), 138-143 (1996)
   PUBMED   8617257
REFERENCE   7  (residues 1 to 484)
  AUTHORS   Scott,V.E., De Waard,M., Liu,H., Gurnett,C.A., Venzke,D.P.,
            Lennon,V.A. and Campbell,K.P.
  TITLE     Beta subunit heterogeneity in N-type Ca2+ channels
  JOURNAL   J Biol Chem 271 (6), 3207-3212 (1996)
   PUBMED   8621722
REFERENCE   8  (residues 1 to 484)
  AUTHORS   Yamada,Y., Masuda,K., Li,Q., Ihara,Y., Kubota,A., Miura,T.,
            Nakamura,K., Fujii,Y., Seino,S. and Seino,Y.
  TITLE     The structures of the human calcium channel alpha 1 subunit
            (CACNL1A2) and beta subunit (CACNLB3) genes
  JOURNAL   Genomics 27 (2), 312-319 (1995)
   PUBMED   7557998
REFERENCE   9  (residues 1 to 484)
  AUTHORS   Collin,T., Lory,P., Taviaux,S., Courtieu,C., Guilbault,P., Berta,P.
            and Nargeot,J.
  TITLE     Cloning, chromosomal location and functional expression of the
            human voltage-dependent calcium-channel beta 3 subunit
  JOURNAL   Eur J Biochem 220 (1), 257-262 (1994)
   PUBMED   8119293
REFERENCE   10 (residues 1 to 484)
  AUTHORS   Rosenfeld,M.R., Wong,E., Dalmau,J., Manley,G., Posner,J.B., Sher,E.
            and Furneaux,H.M.
  TITLE     Cloning and characterization of a Lambert-Eaton myasthenic syndrome
            antigen
  JOURNAL   Ann Neurol 33 (1), 113-120 (1993)
   PUBMED   8494331
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL534844.3, AK289709.1 and
            AC117498.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 23, 2003 this sequence version replaced NP_000716.1.
            
            Summary: This gene encodes a regulatory beta subunit of the
            voltage-dependent calcium channel. Beta subunits are composed of
            five domains, which contribute to the regulation of surface
            expression and gating of calcium channels and may also play a role
            in the regulation of transcription factors and calcium transport.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.815854.1,
                                           SRR1803613.265143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301050.7/ ENSP00000301050.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..484
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-3 isoform 1"
                     /note="voltage-dependent L-type calcium channel subunit
                     beta-3; calcium channel, voltage-dependent, beta 3
                     subunit"
                     /calculated_mol_wt=54401
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54284.1)"
     Region          16..58
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          58..125
                     /region_name="SH3_CACNB3"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta3; cd12042"
                     /db_xref="CDD:212975"
     Site            order(68,70,73,84,102..103,119,121..122)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212975"
     Region          129..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54284.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54287; propagated from
                     UniProtKB/Swiss-Prot (P54284.1)"
     Region          176..356
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Region          195..345
                     /region_name="Mediates interaction with the alpha subunit.
                     /evidence=ECO:0000250|UniProtKB:P54287"
                     /note="propagated from UniProtKB/Swiss-Prot (P54284.1)"
     Region          387..484
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54284.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54287; propagated from
                     UniProtKB/Swiss-Prot (P54284.1)"
     CDS             1..484
                     /gene="CACNB3"
                     /gene_synonym="CAB3; CACNLB3"
                     /coded_by="NM_000725.4:435..1889"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8769.1"
                     /db_xref="GeneID:784"
                     /db_xref="HGNC:HGNC:1403"
                     /db_xref="MIM:601958"
ORIGIN      
        1 myddsyvpgf edseagsads ytsrpsldsd vsleedresa rrevesqaqq qlerakhkpv
       61 afavrtnvsy cgvldeecpv qgsgvnfeak dflhikekys ndwwigrlvk eggdiafips
      121 pqrlesirlk qeqkarrsgn psslsdignr rspppslakq kqkqaehvpp ydvvpsmrpv
      181 vlvgpslkgy evtdmmqkal fdflkhrfdg risitrvtad lslakrsvln npgkrtiier
      241 ssarssiaev qseierifel akslqlvvld adtinhpaql aktslapiiv fvkvsspkvl
      301 qrlirsrgks qmkhltvqmm aydklvqcpp esfdvilden qledacehla eylevywrat
      361 hhpapgpgll gppsaipglq nqqllgerge ehsplerdsl mpsdeasess rqawtgssqr
      421 ssrhleedya dayqdlyqph rqhtsglpsa nghdpqdrll aqdsehnhsd rnwqrnrpwp
      481 kdsy
//
LOCUS       NP_001307950             135 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001307950 XP_005260108
VERSION     NP_001307950.1
DBSOURCE    REFSEQ: accession NM_001321021.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Park,J., Wu,J., Szkop,K.J., Jeong,J., Jovanovic,P., Husmann,D.,
            Flores,N.M., Francis,J.W., Chen,Y.C., Benitez,A.M., Zahn,E.,
            Song,S., Ajani,J.A., Wang,L., Singh,K., Larsson,O., Garcia,B.A.,
            Topisirovic,I., Gozani,O. and Mazur,P.K.
  TITLE     SMYD5 methylation of rpL40 links ribosomal output to gastric cancer
  JOURNAL   Nature 632 (8025), 656-663 (2024)
   PUBMED   39048817
  REMARK    GeneRIF: SMYD5 methylation of rpL40 links ribosomal output to
            gastric cancer.
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Tong,L., Zheng,X., Wang,T., Gu,W., Shen,T., Yuan,W., Wang,S.,
            Xing,S., Liu,X., Zhang,C. and Zhang,C.
  TITLE     Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression
  JOURNAL   J Cell Mol Med 28 (6), e18164 (2024)
   PUBMED   38445807
  REMARK    GeneRIF: Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression.
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Lee,S.O., Kelliher,J.L., Song,W., Tengler,K., Sarkar,A., Dray,E.
            and Leung,J.W.C.
  TITLE     UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination
            and DNA repair
  JOURNAL   J Biol Chem 299 (8), 105043 (2023)
   PUBMED   37451480
  REMARK    GeneRIF: UBA80 and UBA52 fine-tune RNF168-dependent histone
            ubiquitination and DNA repair.
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Eastham,M.J., Pelava,A., Wells,G.R., Watkins,N.J. and Schneider,C.
  TITLE     RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion Proteins,
            Are Not Essential for p53 Signalling
  JOURNAL   Biomolecules 13 (6), 898 (2023)
   PUBMED   37371478
  REMARK    GeneRIF: RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion
            Proteins, Are Not Essential for p53 Signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin/52-residue ribosomal protein fusion gene
            subfamily (UbA52) is composed primarily of processed pseudogenes
  JOURNAL   Genomics 14 (2), 520-522 (1992)
   PUBMED   1330885
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin-52 amino acid fusion protein gene shares
            several structural features with mammalian ribosomal protein genes
  JOURNAL   Nucleic Acids Res 19 (5), 1035-1040 (1991)
   PUBMED   1850507
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Monia,B.P., Ecker,D.J., Jonnalagadda,S., Marsh,J., Gotlib,L.,
            Butt,T.R. and Crooke,S.T.
  TITLE     Gene synthesis, expression, and processing of human ubiquitin
            carboxyl extension proteins
  JOURNAL   J Biol Chem 264 (7), 4093-4103 (1989)
   PUBMED   2537304
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Salvesen,G., Lloyd,C. and Farley,D.
  TITLE     cDNA encoding a human homolog of yeast ubiquitin 1
  JOURNAL   Nucleic Acids Res 15 (13), 5485 (1987)
   PUBMED   3037496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG341101.1, AC005253.1,
            BQ428515.1, AF545864.1 and BU677484.1.
            
            On Mar 12, 2016 this sequence version replaced XP_005260108.1.
            
            Summary: Ubiquitin is a highly conserved nuclear and cytoplasmic
            protein that has a major role in targeting cellular proteins for
            degradation by the 26S proteosome. It is also involved in the
            maintenance of chromatin structure, the regulation of gene
            expression, and the stress response. Ubiquitin is synthesized as a
            precursor protein consisting of either polyubiquitin chains or a
            single ubiquitin moiety fused to an unrelated protein. This gene
            encodes a fusion protein consisting of ubiquitin at the N terminus
            and ribosomal protein L40 at the C terminus, a C-terminal extension
            protein (CEP). Multiple processed pseudogenes derived from this
            gene are present in the genome. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            initiates translation at an alternate start site, compared to
            variant 1. It encodes isoform 2, which has a longer N-terminus
            compared to isoform 1. This isoform (2) may undergo proteolytic
            processing similar to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.298596.1, CX782376.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..135
                     /product="ubiquitin-ribosomal protein eL40 fusion protein
                     isoform 2"
                     /note="ubiquitin-52 amino acid fusion protein; ubiquitin
                     carboxyl extension protein 52; ubiquitin-CEP52;
                     ubiquitin-60S ribosomal protein L40; ubiquitin-ribosomal
                     protein eL40 fusion protein"
                     /calculated_mol_wt=15385
     Region          8..83
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(13..16,18,41..44,47,49,51,53..56,75..83)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(15..19,38..42,47,49,51,53..56,75,77..83)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Region          86..133
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     CDS             1..135
                     /gene="UBA52"
                     /gene_synonym="CEP52; HUBCEP52; L40; RPL40"
                     /coded_by="NM_001321021.1:109..516"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="GeneID:7311"
                     /db_xref="HGNC:HGNC:12458"
                     /db_xref="MIM:191321"
ORIGIN      
        1 mmpkdanmqi fvktltgkti tlevepsdti envkakiqdk egippdqqrl ifagkqledg
       61 rtlsdyniqk estlhlvlrl rggiiepslr qlaqkyncdk micrkcyarl hpravncrkk
      121 kcghtnnlrp kkkvk
//
LOCUS       NP_001158162             478 aa            linear   PRI 20-NOV-2025
DEFINITION  anti-Muellerian hormone type-2 receptor isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001158162
VERSION     NP_001158162.1
DBSOURCE    REFSEQ: accession NM_001164690.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Colaco,S., Achrekar,S., Patil,A., Sawant,U., Desai,S., Mangoli,V.,
            Jirge,P.R., Modi,D. and Mahale,S.D.
  TITLE     Association of AMH and AMHR2 gene polymorphisms with ovarian
            response and pregnancy outcomes in Indian women
  JOURNAL   J Assist Reprod Genet 39 (7), 1633-1642 (2022)
   PUBMED   35713750
  REMARK    GeneRIF: Association of AMH and AMHR2 gene polymorphisms with
            ovarian response and pregnancy outcomes in Indian women.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Liu,Y., Wang,S., Lan,R. and Yang,J.
  TITLE     Identification of AMH and AMHR2 Variants Led to the Diagnosis of
            Persistent Mullerian Duct Syndrome in Three Cases
  JOURNAL   Genes (Basel) 13 (1), 159 (2022)
   PUBMED   35052499
  REMARK    GeneRIF: Identification of AMH and AMHR2 Variants Led to the
            Diagnosis of Persistent Mullerian Duct Syndrome in Three Cases.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Brunello,F.G. and Rey,R.A.
  TITLE     AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development
  JOURNAL   Sex Dev 16 (2-3), 138-146 (2022)
   PUBMED   34515230
  REMARK    GeneRIF: AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development.
            Review article
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Fang,J., Gao,G., Liu,J., Cai,L., Cui,Y. and Yang,X.
  TITLE     A novel mutation of AMHR2 in two brothers with persistent Mullerian
            duct syndrome and their intracytoplasmic sperm injection outcome
  JOURNAL   Mol Genet Genomic Med 9 (10), e1801 (2021)
   PUBMED   34480531
  REMARK    GeneRIF: A novel mutation of AMHR2 in two brothers with persistent
            Mullerian duct syndrome and their intracytoplasmic sperm injection
            outcome.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Faure,E., Gouedard,L., Imbeaud,S., Cate,R., Picard,J.Y., Josso,N.
            and di Clemente,N.
  TITLE     Mutant isoforms of the anti-Mullerian hormone type II receptor are
            not expressed at the cell membrane
  JOURNAL   J Biol Chem 271 (48), 30571-30575 (1996)
   PUBMED   8940028
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Imbeaud,S., Belville,C., Messika-Zeitoun,L., Rey,R., di
            Clemente,N., Josso,N. and Picard,J.Y.
  TITLE     A 27 base-pair deletion of the anti-mullerian type II receptor gene
            is the most common cause of the persistent mullerian duct syndrome
  JOURNAL   Hum Mol Genet 5 (9), 1269-1277 (1996)
   PUBMED   8872466
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Teixeira,J. and Donahoe,P.K.
  TITLE     Molecular biology of MIS and its receptors
  JOURNAL   J Androl 17 (4), 336-341 (1996)
   PUBMED   8889695
  REMARK    Review article
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Imbeaud,S., Faure,E., Lamarre,I., Mattei,M.G., di Clemente,N.,
            Tizard,R., Carre-Eusebe,D., Belville,C., Tragethon,L., Tonkin,C.,
            Nelson,J., McAuliffe,M., Bidart,J.M., Lababidi,A., Josso,N.,
            Cate,R.L. and Picard,J.Y.
  TITLE     Insensitivity to anti-mullerian hormone due to a mutation in the
            human anti-mullerian hormone receptor
  JOURNAL   Nat Genet 11 (4), 382-388 (1995)
   PUBMED   7493017
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Visser,J.A., McLuskey,A., van Beers,T., Weghuis,D.O., van
            Kessel,A.G., Grootegoed,J.A. and Themmen,A.P.
  TITLE     Structure and chromosomal localization of the human anti-mullerian
            hormone type II receptor gene
  JOURNAL   Biochem Biophys Res Commun 215 (3), 1029-1036 (1995)
   PUBMED   7488027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB020573.1, AK313593.1 and
            AJ572328.1.
            
            Summary: This gene encodes the receptor for the anti-Mullerian
            hormone (AMH) which, in addition to testosterone, results in male
            sex differentiation. AMH and testosterone are produced in the
            testes by different cells and have different effects. Testosterone
            promotes the development of male genitalia while the binding of AMH
            to the encoded receptor prevents the development of the mullerian
            ducts into uterus and Fallopian tubes. Mutations in this gene are
            associated with persistent Mullerian duct syndrome type II.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region which results in a frameshift and early
            stop codon compared to variant 1. The resulting protein (isoform 2)
            is shorter and has a distinct C-terminus compared to isoform 1.
            Variants 2 and 3 encode isoforms that are the same length, but have
            distinct protein sequences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313593.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..478
                     /product="anti-Muellerian hormone type-2 receptor isoform
                     2 precursor"
                     /EC_number="2.7.11.30"
                     /note="Mullerian inhibiting substance type II receptor;
                     MIS type II receptor; AMH type II receptor;
                     anti-Muellerian hormone type II receptor; Muellerian
                     inhibiting substance type II receptor; anti-Mullerian
                     hormone receptor, type II"
                     /calculated_mol_wt=50517
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1742
     Region          22..121
                     /region_name="TFP_LU_ECD_AMHR2"
                     /note="extracellular domain (ECD) found in anti-Muellerian
                     hormone type-2 receptor (AMHR2) and similar proteins;
                     cd23616"
                     /db_xref="CDD:467136"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16671.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16671.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16671.1)"
     Region          207..>429
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(209..212,215,217,228,230,258,279..282,333,337..338,
                     340,350..351)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..478
                     /gene="AMHR2"
                     /gene_synonym="AMHR; MISR2; MISRII; MRII"
                     /coded_by="NM_001164690.2:81..1517"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS55829.1"
                     /db_xref="GeneID:269"
                     /db_xref="HGNC:HGNC:465"
                     /db_xref="MIM:600956"
ORIGIN      
        1 mlgslglwal lptaveappn rrtcvffeap gvrgstktlg elldtgtelp rairclysrc
       61 cfgiwnltqd raqvemqgcr dsdepgcesl hcdpsprahp spgstlftcs cgtdfcnany
      121 shlpppgspg tpgsqgpqaa pgesiwmalv llglflllll llgsiilall qrknyrvrge
      181 pvpeprpdsg rdwsvelqel pelcfsqvir egghavvwag qlqgklvaik afpprsvaqf
      241 qaeralyelp glqhdhivrf itasrggpgr llsgpllvle lhpkgslchy ltqytsdwgs
      301 slrmalslaq glaflheerw qngqykpgia hrdlssqnvl iredgscaig dlglalvlpg
      361 ltqppawtpt qpqgpaaime agtqrymape lldktldlqd wgmalrradi yslalllwei
      421 lsrcpdlrpa vhhpsnwpmr qnwaiplplm sygpwqcrrg gvptshppga alpqtlmg
//
LOCUS       NP_647603                336 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            A isoform 2 [Homo sapiens].
ACCESSION   NP_647603
VERSION     NP_647603.1
DBSOURCE    REFSEQ: accession NM_139352.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Zhang,D.L. and Yang,N.
  TITLE     TNFAIP8 regulates cisplatin resistance through TAF-Ialpha and
            promotes malignant progression of esophageal cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (9), 4775-4784 (2020)
   PUBMED   32432789
  REMARK    GeneRIF: TNFAIP8 regulates cisplatin resistance through TAF-Ialpha
            and promotes malignant progression of esophageal cancer.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Miller,G., Panov,K.I., Friedrich,J.K., Trinkle-Mulcahy,L.,
            Lamond,A.I. and Zomerdijk,J.C.
  TITLE     hRRN3 is essential in the SL1-mediated recruitment of RNA
            Polymerase I to rRNA gene promoters
  JOURNAL   EMBO J 20 (6), 1373-1382 (2001)
   PUBMED   11250903
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Muth,V., Nadaud,S., Grummt,I. and Voit,R.
  TITLE     Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA
            polymerase I transcription
  JOURNAL   EMBO J 20 (6), 1353-1362 (2001)
   PUBMED   11250901
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Zhai,W. and Comai,L.
  TITLE     Repression of RNA polymerase I transcription by the tumor
            suppressor p53
  JOURNAL   Mol Cell Biol 20 (16), 5930-5938 (2000)
   PUBMED   10913176
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Di Pietro,C., Rapisarda,A., Amico,V., Bonaiuto,C., Viola,A.,
            Scalia,M., Motta,S., Amato,A., Engel,H., Messina,A., Sichel,G.,
            Grzeschik,K. and Purrello,M.
  TITLE     Genomic localization of the human genes TAF1A, TAF1B and TAF1C,
            encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I
            general transcription initiation factor SL1
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 133-136 (2000)
   PUBMED   10894955
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Comai,L., Zomerdijk,J.C., Beckmann,H., Zhou,S., Admon,A. and
            Tjian,R.
  TITLE     Reconstitution of transcription factor SL1: exclusive binding of
            TBP by SL1 or TFIID subunits
  JOURNAL   Science 266 (5193), 1966-1972 (1994)
   PUBMED   7801123
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Rudloff,U., Eberhard,D., Tora,L., Stunnenberg,H. and Grummt,I.
  TITLE     TBP-associated factors interact with DNA and govern species
            specificity of RNA polymerase I transcription
  JOURNAL   EMBO J 13 (11), 2611-2616 (1994)
   PUBMED   8013460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299536.1, AL592148.7 and
            AK001054.1.
            
            Summary: This gene encodes a subunit of the RNA polymerase I
            complex, Selectivity Factor I (SLI). The encoded protein is a TATA
            box-binding protein-associated factor that plays a role in the
            assembly of the RNA polymerase I preinitiation complex. Alternate
            splicing results in multiple transcript variants encoding multiple
            isoforms.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            lacks an in-frame exon in the 5' coding region, compared to variant
            1. These differences causes translation initiation at a downstream
            AUG and result in isoform (2) which has a shorter N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001054.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..336
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit A isoform 2"
                     /note="SL1, 48kD subunit; TBP-associated factor 1A;
                     transcription factor SL1; TATA box-binding
                     protein-associated factor 1A; transcription initiation
                     factor SL1/TIF-IB subunit A; RNA polymerase I-specific
                     TBP-associated factor 48 kDa; TATA-box binding protein
                     associated factor, RNA polymerase I, A; TATA box binding
                     protein (TBP)-associated factor, RNA polymerase I, A,
                     48kD; TATA box binding protein (TBP)-associated factor,
                     RNA polymerase I, A, 48kDa"
                     /calculated_mol_wt=39484
     Region          1..309
                     /region_name="TAF1_subA"
                     /note="TAF RNA Polymerase I subunit A; pfam14929"
                     /db_xref="CDD:434323"
     CDS             1..336
                     /gene="TAF1A"
                     /gene_synonym="MGC:17061; RAFI48; SL1; TAFI48"
                     /coded_by="NM_139352.2:382..1392"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1532.1"
                     /db_xref="GeneID:9015"
                     /db_xref="HGNC:HGNC:11532"
                     /db_xref="MIM:604903"
ORIGIN      
        1 mesfntfanr mknigvmnyl kislqhalyl lhhgmlkdak rnlseaetwr hgentssrei
       61 linliqaykg llqyytwsek kmelskldkd dyaynavaqd vfnhswktsa nisalikipg
      121 vwdpfvksyv emlefygdrd gaqevltnya ydekfpsnpn ahiylynflk rqkaprskli
      181 svlkilyqiv pshklmlefh tllrksekee hrklglevlf gvldfagctk nitawkylak
      241 ylknilmgnh lawvqeewns rknwwpgfhf syfwaksdwk edtalaceka fvaglllgkg
      301 cryfryilkq dhqilgkkik rmkrsvkkys ivnprl
//
LOCUS       NP_056248                226 aa            linear   PRI 20-NOV-2025
DEFINITION  EEF1A lysine methyltransferase 3 isoform a [Homo sapiens].
ACCESSION   NP_056248
VERSION     NP_056248.2
DBSOURCE    REFSEQ: accession NM_015433.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Shu,X., Li,X., Xiang,X., Wang,Q. and Wu,Q.
  TITLE     METTL21B is a prognostic biomarker and potential therapeutic target
            in low-grade gliomas
  JOURNAL   Aging (Albany NY) 13 (16), 20661-20683 (2021)
   PUBMED   34446611
  REMARK    GeneRIF: METTL21B is a prognostic biomarker and potential
            therapeutic target in low-grade gliomas.
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Hamey,J.J., Wienert,B., Quinlan,K.G.R. and Wilkins,M.R.
  TITLE     METTL21B Is a Novel Human Lysine Methyltransferase of Translation
            Elongation Factor 1A: Discovery by CRISPR/Cas9 Knockout
  JOURNAL   Mol Cell Proteomics 16 (12), 2229-2242 (2017)
   PUBMED   28663172
  REMARK    GeneRIF: Results have shown that METTL21B is a protein
            methyltransferase that methylates both isoforms of translation
            elongation factor eEF1A at lysine 165. Also, further data suggests
            that METTL21B has an evolutionarily important role for the
            methylation of lysine 165 in eEF1A.
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Malecki,J., Aileni,V.K., Ho,A.Y.Y., Schwarz,J., Moen,A.,
            Sorensen,V., Nilges,B.S., Jakobsson,M.E., Leidel,S.A. and
            Falnes,P.O.
  TITLE     The novel lysine specific methyltransferase METTL21B affects mRNA
            translation through inducible and dynamic methylation of Lys-165 in
            human eukaryotic elongation factor 1 alpha (eEF1A)
  JOURNAL   Nucleic Acids Res 45 (8), 4370-4389 (2017)
   PUBMED   28108655
  REMARK    GeneRIF: The present study identifies METTL21B as the enzyme
            responsible for methylation of eEF1A on Lys-165 and shows that this
            modification is dynamic, inducible and likely of regulatory
            importance.
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Cloutier,P., Lavallee-Adam,M., Faubert,D., Blanchette,M. and
            Coulombe,B.
  TITLE     A newly uncovered group of distantly related lysine
            methyltransferases preferentially interact with molecular
            chaperones to regulate their activity
  JOURNAL   PLoS Genet 9 (1), e1003210 (2013)
   PUBMED   23349634
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Kernstock,S., Davydova,E., Jakobsson,M., Moen,A., Pettersen,S.,
            Maelandsmo,G.M., Egge-Jacobsen,W. and Falnes,P.O.
  TITLE     Lysine methylation of VCP by a member of a novel human protein
            methyltransferase family
  JOURNAL   Nat Commun 3, 1038 (2012)
   PUBMED   22948820
  REMARK    GeneRIF: The METTL21B protein is here suggested to be a protein
            methyltransferase, as it is shown to belong to a family of 10 human
            methyltransferases, some of which are shown to have lysine specific
            protein methyltransferase activity.
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Gandhi,K.S., McKay,F.C., Cox,M., Riveros,C., Armstrong,N.,
            Heard,R.N., Vucic,S., Williams,D.W., Stankovich,J., Brown,M.,
            Danoy,P., Stewart,G.J., Broadley,S., Moscato,P., Lechner-Scott,J.,
            Scott,R.J. and Booth,D.R.
  CONSRTM   ANZgene Multiple Sclerosis Genetics Consortium
  TITLE     The multiple sclerosis whole blood mRNA transcriptome and genetic
            associations indicate dysregulation of specific T cell pathways in
            pathogenesis
  JOURNAL   Hum Mol Genet 19 (11), 2134-2143 (2010)
   PUBMED   20190274
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC016395.1 and AL050100.1.
            
            On Mar 30, 2004 this sequence version replaced NP_056248.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA938041.1, SRR1803611.110587.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300209.13/ ENSP00000300209.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..226
                     /product="EEF1A lysine methyltransferase 3 isoform a"
                     /note="family with sequence similarity 119, member B;
                     hepatocellularcarcinoma-associated antigen HCA557a;
                     methyltransferase-like protein 21B; eEF1A-KMT3;
                     hepatocellular carcinoma-associated antigen 557a;
                     methyltransferase like 21B; protein-lysine
                     methyltransferase METTL21B"
                     /calculated_mol_wt=24780
     Region          37..195
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     CDS             1..226
                     /gene="EEF1AKMT3"
                     /gene_synonym="FAM119B; METTL21B"
                     /coded_by="NM_015433.3:112..792"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8957.1"
                     /db_xref="GeneID:25895"
                     /db_xref="HGNC:HGNC:24936"
                     /db_xref="MIM:615258"
ORIGIN      
        1 madpgpdpes esesvfprev glfadsysek sqfcfcghvl titqnfgsrl gvaarvwdaa
       61 lslcnyfesq nvdfrgkkvi elgagtgivg ilaalqggdv titdlplale qiqgnvqanv
      121 paggqaqvra lswgidhhvf panydlvlga divyleptfp lllgtlqhlc rphgtiylas
      181 kmrkehgtes ffqhllpqhf qlelaqrded envniyrarh reprpa
//
LOCUS       NP_001184044             599 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate--cysteine ligase catalytic subunit isoform b [Homo
            sapiens].
ACCESSION   NP_001184044
VERSION     NP_001184044.1
DBSOURCE    REFSEQ: accession NM_001197115.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Xu,C., Bian,Z., Wang,X., Niu,N., Liu,L., Xiao,Y., Zhu,J., Huang,N.,
            Zhang,Y., Chen,Y., Wu,Q., Sun,F., Zhu,X. and Pan,Q.
  TITLE     SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 331 (2023)
   PUBMED   38049865
  REMARK    GeneRIF: SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Liu,C., Wu,X., Bing,X., Qi,W., Zhu,F., Guo,N., Li,C., Gao,X.,
            Cao,X., Zhao,M. and Xia,M.
  TITLE     H1N1 influenza virus infection through NRF2-KEAP1-GCLC pathway
            induces ferroptosis in nasal mucosal epithelial cells
  JOURNAL   Free Radic Biol Med 204, 226-242 (2023)
   PUBMED   37146698
  REMARK    GeneRIF: H1N1 influenza virus infection through NRF2-KEAP1-GCLC
            pathway induces ferroptosis in nasal mucosal epithelial cells.
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Luo,L., Zhang,Z., Weng,Y. and Zeng,J.
  TITLE     Ferroptosis-Related Gene GCLC Is a Novel Prognostic Molecular and
            Correlates with Immune Infiltrates in Lung Adenocarcinoma
  JOURNAL   Cells 11 (21), 3371 (2022)
   PUBMED   36359768
  REMARK    GeneRIF: Ferroptosis-Related Gene GCLC Is a Novel Prognostic
            Molecular and Correlates with Immune Infiltrates in Lung
            Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Bykanova,M.A., Solodilova,M.A., Azarova,I.E., Klyosova,E.Y.,
            Bushueva,O.Y., Polonikova,A.A., Churnosov,M.I. and Polonikov,A.V.
  TITLE     Genetic variation at the catalytic subunit of glutamate cysteine
            ligase contributes to the susceptibility to sporadic colorectal
            cancer: a pilot study
  JOURNAL   Mol Biol Rep 49 (7), 6145-6154 (2022)
   PUBMED   35386070
  REMARK    GeneRIF: Genetic variation at the catalytic subunit of glutamate
            cysteine ligase contributes to the susceptibility to sporadic
            colorectal cancer: a pilot study.
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Mulcahy,R.T. and Gipp,J.J.
  TITLE     Identification of a putative antioxidant response element in the
            5'-flanking region of the human gamma-glutamylcysteine synthetase
            heavy subunit gene
  JOURNAL   Biochem Biophys Res Commun 209 (1), 227-233 (1995)
   PUBMED   7726839
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Gipp,J.J., Chang,C. and Mulcahy,R.T.
  TITLE     Cloning and nucleotide sequence of a full-length cDNA for human
            liver gamma-glutamylcysteine synthetase
  JOURNAL   Biochem Biophys Res Commun 185 (1), 29-35 (1992)
   PUBMED   1350904
REFERENCE   8  (residues 1 to 599)
  AUTHORS   Beutler,E., Moroose,R., Kramer,L., Gelbart,T. and Forman,L.
  TITLE     Gamma-glutamylcysteine synthetase deficiency and hemolytic anemia
  JOURNAL   Blood 75 (1), 271-273 (1990)
   PUBMED   2294991
REFERENCE   9  (residues 1 to 599)
  AUTHORS   Lebo,R.V. and Kredich,N.M.
  TITLE     Inactivation of human gamma-glutamylcysteine synthetase by
            cystamine. Demonstration and quantification of enzyme-ligand
            complexes
  JOURNAL   J Biol Chem 253 (8), 2615-2623 (1978)
   PUBMED   24639
REFERENCE   10 (residues 1 to 599)
  AUTHORS   Konrad,P.N., Richards,F. 2nd, Valentine,W.N. and Paglia,D.E.
  TITLE     -Glutamyl-cysteine synthetase deficiency. A cause of hereditary
            hemolytic anemia
  JOURNAL   N Engl J Med 286 (11), 557-561 (1972)
   PUBMED   5058793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550814.1, AL531593.3,
            AK313480.1, AB516284.1, AB262176.1 and BC039894.1.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase is the first rate-limiting enzyme
            of glutathione synthesis. The enzyme consists of two subunits, a
            heavy catalytic subunit and a light regulatory subunit. This locus
            encodes the catalytic subunit, while the regulatory subunit is
            derived from a different gene located on chromosome 1p22-p21.
            Mutations at this locus have been associated with hemolytic anemia
            due to deficiency of gamma-glutamylcysteine synthetase and
            susceptibility to myocardial infarction.[provided by RefSeq, Oct
            2010].
            
            Transcript Variant: This variant (2, also referred to as delta4)
            lacks an in-frame exon in the 5' coding region, compared to variant
            1. This results in a shorter protein (isoform b), compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB516284.1, ERR3218371.357435.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..599
                     /product="glutamate--cysteine ligase catalytic subunit
                     isoform b"
                     /EC_number="6.3.2.2"
                     /note="gamma-glutamylcysteine synthetase; gamma-ECS; GCS
                     heavy chain"
                     /calculated_mol_wt=68499
     Region          <22..76
                     /region_name="PRK00087"
                     /note="bifunctional 4-hydroxy-3-methylbut-2-enyl
                     diphosphate reductase/30S ribosomal protein S1"
                     /db_xref="CDD:234623"
     Region          198..570
                     /region_name="GCS"
                     /note="Glutamate-cysteine ligase; pfam03074"
                     /db_xref="CDD:460796"
     CDS             1..599
                     /gene="GCLC"
                     /gene_synonym="CNSHA7; GCL; GCS; GLCL; GLCLC"
                     /coded_by="NM_001197115.2:457..2256"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75471.1"
                     /db_xref="GeneID:2729"
                     /db_xref="HGNC:HGNC:4311"
                     /db_xref="MIM:606857"
ORIGIN      
        1 mgllsqgspl sweetkrhad hvrrhgilqf lhiyhavkdr hkdvlkwgde veymlvsfdh
       61 enkkvrlvls gekvletlqe kgertnpnhp tlwrpeygsy miegtpgqpy ggtmsefntv
      121 eanmrkrrke atsileenqa lctitsfpst ltrnirhrrg ekvvinvpif kdkntpspfi
      181 etfteddeas raskpdhiym damgfgmgnc clqvtfqacs isearylydq laticpivma
      241 lsaaspfyrg yvsdidcrwg visasvddrt reergleplk nnnyrisksr ydsidsylsk
      301 cgekyndidl tidkeiyeql lqegidhlla qhvahlfird pltlfeekih lddanesdhf
      361 eniqstnwqt mrfkppppns digwrvefrp mevqltdfen sayvvfvvll trvilsykld
      421 fliplskvde nmkvaqkrda vlqgmfyfrk dickggnavv dgcgkaqnst elaaeeytlm
      481 sidtiingke gvfpglipil nsylenmevd vdtrcsilny lklikkrasg elmtvarwmr
      541 efianhpdyk qdsvitdemn yslilkcnqi anelcecpel lgsafrkvky sgsktdssn
//
LOCUS       NP_001012300             475 aa            linear   PRI 20-NOV-2025
DEFINITION  microspherule protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001012300
VERSION     NP_001012300.1
DBSOURCE    REFSEQ: accession NM_001012300.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Huang,C.J., Lyu,X. and Kang,J.
  TITLE     The molecular characteristics and functional roles of microspherule
            protein 1 (MCRS1) in gene expression, cell proliferation, and
            organismic development
  JOURNAL   Cell Cycle 22 (6), 619-632 (2023)
   PUBMED   36384428
  REMARK    GeneRIF: The molecular characteristics and functional roles of
            microspherule protein 1 (MCRS1) in gene expression, cell
            proliferation, and organismic development.
            Review article
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Laguillo-Diego,A., Kiewisz,R., Marti-Gomez,C., Baum,D.,
            Muller-Reichert,T. and Vernos,I.
  TITLE     MCRS1 modulates the heterogeneity of microtubule minus-end
            morphologies in mitotic spindles
  JOURNAL   Mol Biol Cell 34 (1), ar1 (2023)
   PUBMED   36350698
  REMARK    GeneRIF: MCRS1 modulates the heterogeneity of microtubule minus-end
            morphologies in mitotic spindles.
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Song,H., Li,Y., Chen,G., Xing,Z., Zhao,J., Yokoyama,K.K., Li,T. and
            Zhao,M.
  TITLE     Human MCRS2, a cell-cycle-dependent protein, associates with
            LPTS/PinX1 and reduces the telomere length
  JOURNAL   Biochem Biophys Res Commun 316 (4), 1116-1123 (2004)
   PUBMED   15044100
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Lin,D.Y. and Shih,H.M.
  TITLE     Essential role of the 58-kDa microspherule protein in the
            modulation of Daxx-dependent transcriptional repression as revealed
            by nucleolar sequestration
  JOURNAL   J Biol Chem 277 (28), 25446-25456 (2002)
   PUBMED   11948183
  REMARK    GeneRIF: role in the modulation of Daxx-dependent transcriptional
            repression
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Bruni,R. and Roizman,B.
  TITLE     Herpes simplex virus 1 regulatory protein ICP22 interacts with a
            new cell cycle-regulated factor and accumulates in a cell
            cycle-dependent fashion in infected cells
  JOURNAL   J Virol 72 (11), 8525-8531 (1998)
   PUBMED   9765390
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Ren,Y., Busch,R.K., Perlaky,L. and Busch,H.
  TITLE     The 58-kDa microspherule protein (MSP58), a nucleolar protein,
            interacts with nucleolar protein p120
  JOURNAL   Eur J Biochem 253 (3), 734-742 (1998)
   PUBMED   9654073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY336730.1 and BC011794.2.
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY336730.1, SRR14038197.1096343.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..475
                     /product="microspherule protein 1 isoform 2"
                     /note="INO80 complex subunit Q; cell cycle-regulated
                     factor (78 kDa); INO80 complex subunit J; 58 kDa
                     microspherule protein; cell cycle-regulated factor p78"
                     /calculated_mol_wt=52870
     Region          147..344
                     /region_name="MCRS_N"
                     /note="N-terminal region of micro-spherule protein;
                     pfam13325"
                     /db_xref="CDD:463845"
     Region          354..458
                     /region_name="FHA_MCRS1"
                     /note="forkhead associated (FHA) domain found in
                     microspherule protein 1 (MCRS1) and similar proteins;
                     cd22687"
                     /db_xref="CDD:438739"
     Site            order(379..380,401..402,404,421,423..424)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438739"
     CDS             1..475
                     /gene="MCRS1"
                     /gene_synonym="ICP22BP; INO80Q; MCRS2; MSP58; P78"
                     /coded_by="NM_001012300.1:1..1428"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31795.1"
                     /db_xref="GeneID:10445"
                     /db_xref="HGNC:HGNC:6960"
                     /db_xref="MIM:609504"
ORIGIN      
        1 mtrgtggtaq rgrsgpdsqg lldsslmasg tasrsedees lagqkrassq algtipkrrs
       61 ssrfikrkkf ddelvessla ksstrakgas gvepgrcsgs epsssekkkv skapstpvpp
      121 spapapgltk rvkkskqplq vtkdlgrwkp addlllinav lqtndltsvh lgvkfscrft
      181 lrevqerwya llydpviskl acqamrqlhp eaiaaiqska lfskaeeqll skvgstsqpt
      241 letfqdllhr hpdafylart akalqahwql mkqyylledq tvqplpkgdq vlnfsdaedl
      301 iddsklkdmr devlehelmv adrrqkreir qleqelhkwq vlvdsitgms spdfdnqtla
      361 vlrgrmvryl mrsreitlgr atkdnqidvd lslegpawki srkqgviklk nngdffiane
      421 grrpiyidgr pvlcgskwrl snnsvveias lrfvflinqd lialiraeaa kitpq
//
LOCUS       NP_001127879            1464 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2A isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001127879
VERSION     NP_001127879.1
DBSOURCE    REFSEQ: accession NM_001134407.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Xu,Y., Song,R., Perszyk,R.E., Chen,W., Kim,S., Park,K.L.,
            Allen,J.P., Nocilla,K.A., Zhang,J., XiangWei,W., Tankovic,A.,
            McDaniels,E.D., Sheikh,R., Mizu,R.K., Karamchandani,M.M., Hu,C.,
            Kusumoto,H., Pecha,J., Cappuccio,G., Gaitanis,J., Sullivan,J.,
            Shashi,V., Petrovski,S., Jauss,R.T., Lee,H.K., Bozarth,X.,
            Lynch,D.R., Helbig,I., Pierson,T.M., Boerkoel,C.F., Myers,S.J.,
            Lemke,J.R., Benke,T.A., Yuan,H. and Traynelis,S.F.
  TITLE     De novo GRIN variants in M3 helix associated with neurological
            disorders control channel gating of NMDA receptor
  JOURNAL   Cell Mol Life Sci 81 (1), 153 (2024)
   PUBMED   38538865
  REMARK    GeneRIF: De novo GRIN variants in M3 helix associated with
            neurological disorders control channel gating of NMDA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Lu,W., Yang,X., Zhong,W., Chen,G., Guo,X., Ye,Q., Xu,Y., Qi,Z.,
            Ye,Y., Zhang,J., Wang,Y., Wang,X., Wang,S., Zhao,Q., Zeng,W.,
            Huang,J., Ma,H. and Xie,J.
  TITLE     METTL14-mediated m6A epitranscriptomic modification contributes to
            chemotherapy-induced neuropathic pain by stabilizing GluN2A
            expression via IGF2BP2
  JOURNAL   J Clin Invest 134 (6), e174847 (2024)
   PUBMED   38319733
  REMARK    GeneRIF: METTL14-mediated m6A epitranscriptomic modification
            contributes to chemotherapy-induced neuropathic pain by stabilizing
            GluN2A expression via IGF2BP2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Shepard,N., Baez-Nieto,D., Iqbal,S., Kurganov,E., Budnik,N.,
            Campbell,A.J., Pan,J.Q., Sheng,M. and Farsi,Z.
  TITLE     Differential functional consequences of GRIN2A mutations associated
            with schizophrenia and neurodevelopmental disorders
  JOURNAL   Sci Rep 14 (1), 2798 (2024)
   PUBMED   38307912
  REMARK    GeneRIF: Differential functional consequences of GRIN2A mutations
            associated with schizophrenia and neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Sokolov,B.P. and Prockop,D.J.
  TITLE     A rapid and simple PCR-based method for isolation of cDNAs from
            differentially expressed genes
  JOURNAL   Nucleic Acids Res 22 (19), 4009-4015 (1994)
   PUBMED   7524031
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Strehlow,V., Myers,K.A., Morgan,A.T., Scheffer,I.E. and Lemke,J.R.
  TITLE     GRIN2A-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27683935
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022168.6, AB209695.1,
            U09002.1, AC006531.1 and AC007218.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the glutamate-gated ion
            channel protein family. The encoded protein is an
            N-methyl-D-aspartate (NMDA) receptor subunit. NMDA receptors are
            both ligand-gated and voltage-dependent, and are involved in
            long-term potentiation, an activity-dependent increase in the
            efficiency of synaptic transmission thought to underlie certain
            kinds of memory and learning. These receptors are permeable to
            calcium ions, and activation results in a calcium influx into
            post-synaptic cells, which results in the activation of several
            signaling cascades. Disruption of this gene is associated with
            focal epilepsy and speech disorder with or without cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Transcript variants 1 and 2 encode the same isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U09002.1, AB209695.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330684.4/ ENSP00000332549.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.2"
     Protein         1..1464
                     /product="glutamate receptor ionotropic, NMDA 2A isoform 1
                     precursor"
                     /note="N-methyl-D-aspartate receptor channel, subunit
                     epsilon-1; N-methyl-D-aspartate receptor subunit 2A;
                     N-methyl D-aspartate receptor subtype 2A; glutamate
                     receptor, ionotropic, N-methyl D-aspartate 2A; glutamate
                     receptor ionotropic, NMDA 2A; glutamate ionotropic
                     receptor NMDA 2A"
                     /calculated_mol_wt=162435
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2866
     Region          32..387
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(32,78..80,115,136,176,178,193,208..209,310..311)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            order(76..81,83..84,119..120,176,180,207,209,310..316,
                     320..322,333)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Region          403..802
                     /region_name="PBP2_iGluR_NMDA_Nr2"
                     /note="The ligand-binding domain of the NR2 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13718"
                     /db_xref="CDD:270436"
     Site            order(511..514,516,518..520,666,688..689,693,731,756..758,
                     761,767,783..786,789)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270436"
     Site            order(511..513,518,688..690,730..731)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270436"
     Region          839..1464
                     /region_name="NMDAR2_C"
                     /note="N-methyl D-aspartate receptor 2B3 C-terminus;
                     pfam10565"
                     /db_xref="CDD:463148"
     CDS             1..1464
                     /gene="GRIN2A"
                     /gene_synonym="EPND; FESD; GluN2A; LKS; NMDAR2A; NR2A"
                     /coded_by="NM_001134407.3:571..4965"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10539.1"
                     /db_xref="GeneID:2903"
                     /db_xref="HGNC:HGNC:4585"
                     /db_xref="MIM:138253"
ORIGIN      
        1 mgrvgywtll vlpallvwrg papsaaaekg ppalniavml ghshdvtere lrtlwgpeqa
       61 aglpldvnvv allmnrtdpk slithvcdlm sgarihglvf gddtdqeava qmldfissht
      121 fvpilgihgg asmimadkdp tstffqfgas iqqqatvmlk imqdydwhvf slvttifpgy
      181 refisfvktt vdnsfvgwdm qnvitldtsf edaktqvqlk kihssvilly cskdeavlil
      241 searslgltg ydffwivpsl vsgntelipk efpsglisvs yddwdyslea rvrdgigilt
      301 taassmlekf syipeakasc ygqmerpevp mhtlhpfmvn vtwdgkdlsf teegyqvhpr
      361 lvvivlnkdr ewekvgkwen htlslrhavw pryksfsdce pddnhlsivt leeapfvive
      421 didpltetcv rntvpcrkfv kinnstnegm nvkkcckgfc idilkklsrt vkftydlylv
      481 tngkhgkkvn nvwngmigev vyqravmavg sltineerse vvdfsvpfve tgisvmvsrs
      541 ngtvspsafl epfsasvwvm mfvmllivsa iavfvfeyfs pvgynrnlak gkaphgpsft
      601 igkaiwllwg lvfnnsvpvq npkgttskim vsvwaffavi flasytanla afmiqeefvd
      661 qvtglsdkkf qrphdysppf rfgtvpngst ernirnnypy mhqymtkfnq kgvedalvsl
      721 ktgkldafiy daavlnykag rdegcklvti gsgyifattg ygialqkgsp wkrqidlall
      781 qfvgdgemee letlwltgic hneknevmss qldidnmagv fymlaaamal slitfiwehl
      841 fywklrfcft gvcsdrpgll fsisrgiysc ihgvhieekk kspdfnltgs qsnmlkllrs
      901 aknissmsnm nssrmdspkr aadfiqrgsl imdmvsdkgn lmysdnrsfq gkesifgdnm
      961 nelqtfvanr qkdnlnnyvf qgqhpltlne snpntvevav steskansrp rqlwkksvds
     1021 irqdslsqnp vsqrdeatae nrthslkspr ylpeemahsd isetsnratc hrepdnsknh
     1081 ktkdnfkrsv askypkdcse vertylktks ssprdkiyti dgekepgfhl dppqfvenvt
     1141 lpenvdfpdp yqdpsenfrk gdstlpmnrn plhneeglsn ndqyklyskh ftlkdkgsph
     1201 setseryrqn sthcrsclsn mptysghftm rspfkcdacl rmgnlydide dqmlqetgnp
     1261 atgeqvyqqd waqnnalqlq knklrisrqh sydnivdkpr eldlsrpsrs islkdrerll
     1321 egnfygslfs vpssklsgkk sslfpqgled skrsksllpd htsdnpflhs hrddqrlvig
     1381 rcpsdpykhs lpsqavndsy lrsslrstas ycsrdsrghn dvyisehvmp yaanknnmys
     1441 tprvlnscsn rrvykkmpsi esdv
//
LOCUS       NP_057345                453 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin delta chain isoform 1 [Homo sapiens].
ACCESSION   NP_057345
VERSION     NP_057345.2
DBSOURCE    REFSEQ: accession NM_016261.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Wang,J.T., Kong,D., Hoerner,C.R., Loncarek,J. and Stearns,T.
  TITLE     Centriole triplet microtubules are required for stable centriole
            formation and inheritance in human cells
  JOURNAL   Elife 6, e29061 (2017)
   PUBMED   28906251
  REMARK    GeneRIF: Here, the authors report that centrioles in delta-tubulin
            and epsilon-tubulin null mutant human cells lack triplet
            microtubules and fail to undergo centriole maturation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Kato,A., Nagata,Y. and Todokoro,K.
  TITLE     Delta-tubulin is a component of intercellular bridges and both the
            early and mature perinuclear rings during spermatogenesis
  JOURNAL   Dev Biol 269 (1), 196-205 (2004)
   PUBMED   15081367
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Sidjanin,D.J., Zangerl,B., Johnson,J.L., Xue,F., Mellersh,C.,
            Ostrander,E.A., Acland,G. and Aguirre,G.D.
  TITLE     Cloning of the canine delta tubulin cDNA (TUBD) and mapping to CFA9
  JOURNAL   Anim Genet 33 (2), 161-162 (2002)
   PUBMED   12047234
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Smrzka,O.W., Delgehyr,N. and Bornens,M.
  TITLE     Tissue-specific expression and subcellular localisation of
            mammalian delta-tubulin
  JOURNAL   Curr Biol 10 (7), 413-416 (2000)
   PUBMED   10753753
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Chang,P. and Stearns,T.
  TITLE     Delta-tubulin and epsilon-tubulin: two new human centrosomal
            tubulins reveal new aspects of centrosome structure and function
  JOURNAL   Nat Cell Biol 2 (1), 30-35 (2000)
   PUBMED   10620804
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG682935.1, DA607129.1, AB030837.1, AK024741.1 and BX119803.1.
            
            On Jul 26, 2004 this sequence version replaced NP_057345.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and it encodes the longest protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.103777.1,
                                           SRR1803616.250902.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325752.8/ ENSP00000320797.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.1"
     Protein         1..453
                     /product="tubulin delta chain isoform 1"
                     /note="delta-tubulin; tubulin delta chain"
                     /calculated_mol_wt=50903
     Region          2..452
                     /region_name="delta_zeta_tubulin-like"
                     /note="The delta- and zeta-tubulin families; cd02189"
                     /db_xref="CDD:276958"
     Site            order(9..11,14..15,67..69,72,100..102,141..147,172,
                     174..175,182..183,206,210,224,227..228,231)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:276958"
     CDS             1..453
                     /gene="TUBD1"
                     /gene_synonym="TUBD"
                     /coded_by="NM_016261.4:287..1648"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11620.1"
                     /db_xref="GeneID:51174"
                     /db_xref="HGNC:HGNC:16811"
                     /db_xref="MIM:607344"
ORIGIN      
        1 msivtvqlgq cgnqigfevf dallsdshss qglcsmrene ayqasckerf fseeengvpi
       61 aravlvdmep kvinqmlska aqsgqwkygq hacfcqkqgs gnnwaygysv hgprheesim
      121 niirkevekc dsfsgffiim smaggtgsgl gafvtqnled qysnslkmnq iiwpygtgev
      181 ivqnynsilt lshlyrssda lllhendaih kicaklmnik qisfsdinqv lahqlgsvfq
      241 ptysaessfh yrrnplgdlm ehlvphpefk mlsvrniphm senslayttf twagllkhlr
      301 qmlisnakme egidrhvwpp lsglpplskm slnkdlhfnt sianlvilrg kdvqsadveg
      361 fkdpalytsw lkpvnafnvw ktqrafskye ksavlvsnsq flvkpldmiv gkawnmfask
      421 ayihqytkfg ieeedfldsf tsleqvvasy cnl
//
LOCUS       NP_006144                377 aa            linear   PRI 20-NOV-2025
DEFINITION  SH2/SH3 adapter protein NCK1 isoform 1 [Homo sapiens].
ACCESSION   NP_006144
VERSION     NP_006144.1
DBSOURCE    REFSEQ: accession NM_006153.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Deng,S., Zhang,Y., Wang,H., Liang,W., Xie,L., Li,N., Fang,Y.,
            Wang,Y., Liu,J., Chi,H., Sun,Y., Ye,R., Shan,L., Shi,J., Shen,Z.,
            Wang,Y., Wang,S., Brosseau,J.P., Wang,F., Liu,G., Quan,Y. and Xu,J.
  TITLE     ITPRIPL1 binds CD3epsilon to impede T cell activation and enable
            tumor immune evasion
  JOURNAL   Cell 187 (9), 2305-2323 (2024)
   PUBMED   38614099
REFERENCE   4  (residues 1 to 377)
  AUTHORS   He,P., Liu,Z., Qi,J., Shan,J. and Sheng,J.
  TITLE     Long noncoding RNA LINC00885 upregulates NCK1 to promote cell
            viability and migration of triple-negative breast cancer cells
            through sponging miR-654-3p
  JOURNAL   Cancer Biomark 39 (1), 63-78 (2024)
   PUBMED   37694355
  REMARK    GeneRIF: Long noncoding RNA LINC00885 upregulates NCK1 to promote
            cell viability and migration of triple-negative breast cancer cells
            through sponging miR-654-3p.
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Nuiyen,A., Rattanasri,A., Wipa,P., Roytrakul,S.,
            Wangteeraprasert,A., Pongcharoen,S. and Ngoenkam,J.
  TITLE     Lack of Nck1 protein and Nck-CD3 interaction caused the increment
            of lipid content in Jurkat T cells
  JOURNAL   BMC Mol Cell Biol 23 (1), 36 (2022)
   PUBMED   35902806
  REMARK    GeneRIF: Lack of Nck1 protein and Nck-CD3 interaction caused the
            increment of lipid content in Jurkat T cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Rivero-Lezcano,O.M., Marcilla,A., Sameshima,J.H. and Robbins,K.C.
  TITLE     Wiskott-Aldrich syndrome protein physically associates with Nck
            through Src homology 3 domains
  JOURNAL   Mol Cell Biol 15 (10), 5725-5731 (1995)
   PUBMED   7565724
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Rivero-Lezcano,O.M., Sameshima,J.H., Marcilla,A. and Robbins,K.C.
  TITLE     Physical association between Src homology 3 elements and the
            protein product of the c-cbl proto-oncogene
  JOURNAL   J Biol Chem 269 (26), 17363-17366 (1994)
   PUBMED   7517397
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Meisenhelder,J. and Hunter,T.
  TITLE     The SH2/SH3 domain-containing protein Nck is recognized by certain
            anti-phospholipase C-gamma 1 monoclonal antibodies, and its
            phosphorylation on tyrosine is stimulated by platelet-derived
            growth factor and epidermal growth factor treatment
  JOURNAL   Mol Cell Biol 12 (12), 5843-5856 (1992)
   PUBMED   1448108
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Park,D. and Rhee,S.G.
  TITLE     Phosphorylation of Nck in response to a variety of receptors,
            phorbol myristate acetate, and cyclic AMP
  JOURNAL   Mol Cell Biol 12 (12), 5816-5823 (1992)
   PUBMED   1333046
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Lehmann,J.M., Riethmuller,G. and Johnson,J.P.
  TITLE     Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of
            the src homology units SH2 and SH3
  JOURNAL   Nucleic Acids Res 18 (4), 1048 (1990)
   PUBMED   2107526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB117533.1, BC006403.2 and
            AC011597.27.
            
            Summary: The protein encoded by this gene is one of the signaling
            and transforming proteins containing Src homology 2 and 3 (SH2 and
            SH3) domains. It is located in the cytoplasm and is an adaptor
            protein involved in transducing signals from receptor tyrosine
            kinases to downstream signal recipients such as RAS. Alternatively
            spliced transcript variants encoding different isoforms have been
            found. [provided by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer protein (isoform 1). Variants 1
            and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.136471.1,
                                           SRR1803614.183094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..377
                     /product="SH2/SH3 adapter protein NCK1 isoform 1"
                     /note="NCK tyrosine kinase; non-catalytic region of
                     tyrosine kinase; SH2/SH3 adaptor protein NCK-alpha;
                     melanoma NCK protein; cytoplasmic protein NCK1; NCK
                     adapter protein 1; SH2/SH3 adapter protein NCK-alpha;
                     SH2/SH3 adapter protein NCK1"
                     /calculated_mol_wt=42733
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Region          3..61
                     /region_name="SH3_Nck1_1"
                     /note="First Src Homology 3 domain of Nck1 adaptor
                     protein; cd11900"
                     /db_xref="CDD:212833"
     Site            order(13,16..17,19..20,36..38,50,52..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212833"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P16333.1)"
     Region          108..162
                     /region_name="SH3_Nck1_2"
                     /note="Second Src Homology 3 domain of Nck1 adaptor
                     protein; cd11901"
                     /db_xref="CDD:212834"
     Site            order(115,117,120,124,142..143,156,158..159)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212834"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P16333.1)"
     Region          193..249
                     /region_name="SH3_Nck1_3"
                     /note="Third Src Homology 3 domain of Nck1 adaptor
                     protein; cd11904"
                     /db_xref="CDD:212837"
     Site            order(199,201,204,208,228..229,243,245..246)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212837"
     Region          280..376
                     /region_name="SH2_Nck1"
                     /note="Src homology 2 (SH2) domain found in Nck; cd10408"
                     /db_xref="CDD:198271"
     Site            order(289,308,310..312,318,331)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198271"
     Site            order(330,341,344,361..363)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198271"
     CDS             1..377
                     /gene="NCK1"
                     /gene_synonym="NCK; nck-1; NCKalpha"
                     /coded_by="NM_006153.6:131..1264"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3092.1"
                     /db_xref="GeneID:4690"
                     /db_xref="HGNC:HGNC:7664"
                     /db_xref="MIM:600508"
ORIGIN      
        1 maeevvvvak fdyvaqqeqe ldikknerlw llddskswwr vrnsmnktgf vpsnyverkn
       61 sarkasivkn lkdtlgigkv krkpsvpdsa spaddsfvdp gerlydlnmp ayvkfnymae
      121 redelslikg tkvivmekcs dgwwrgsyng qvgwfpsnyv teegdsplgd hvgslsekla
      181 avvnnlntgq vlhvvqalyp fsssndeeln fekgdvmdvi ekpendpeww kcrkingmvg
      241 lvpknyvtvm qnnpltsgle psppqcdyir psltgkfagn pwyygkvtrh qaemalnerg
      301 hegdflirds esspndfsvs lkaqgknkhf kvqlketvyc igqrkfstme elvehykkap
      361 iftseqgekl ylvkhls
//
LOCUS       NP_001158067            1036 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing RING finger protein 4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001158067
VERSION     NP_001158067.1
DBSOURCE    REFSEQ: accession NM_001164595.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Hu,T., Yang,H. and Han,Z.G.
  TITLE     PDZRN4 acts as a suppressor of cell proliferation in human liver
            cancer cell lines
  JOURNAL   Cell Biochem Funct 33 (7), 443-449 (2015)
   PUBMED   26486104
  REMARK    GeneRIF: Results showed that PDZRN4 might be a potential tumour
            suppressor gene and had anti-proliferative effect on hepatocellular
            carcinoma cell proliferation.
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Chu,M., Ji,X., Chen,W., Zhang,R., Sun,C., Wang,T., Luo,C., Gong,J.,
            Zhu,M., Fan,J., Hou,Z., Dai,J., Jin,G., Wu,T., Chen,F., Hu,Z.,
            Ni,C. and Shen,H.
  TITLE     A genome-wide association study identifies susceptibility loci of
            silica-related pneumoconiosis in Han Chinese
  JOURNAL   Hum Mol Genet 23 (23), 6385-6394 (2014)
   PUBMED   24986923
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Cavanillas,M.L., Fernandez,O., Comabella,M., Alcina,A., Fedetz,M.,
            Izquierdo,G., Lucas,M., Cenit,M.C., Arroyo,R., Vandenbroeck,K.,
            Alloza,I., Garcia-Barcina,M., Antiguedad,A., Leyva,L., Gomez,C.L.,
            Olascoaga,J., Otaegui,D., Blanco,Y., Saiz,A., Montalban,X.,
            Matesanz,F. and Urcelay,E.
  TITLE     Replication of top markers of a genome-wide association study in
            multiple sclerosis in Spain
  JOURNAL   Genes Immun 12 (2), 110-115 (2011)
   PUBMED   20944657
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Simons,R., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of PDZRN3 and PDZRN4 genes in
            silico
  JOURNAL   Int J Mol Med 13 (4), 607-613 (2004)
   PUBMED   15010864
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021651.17, AW297403.1, AK294535.1, AC090531.18 and BX640695.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.166859.1,
                                           SRR1803612.93624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000402685.7/ ENSP00000384197.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..1036
                     /product="PDZ domain-containing RING finger protein 4
                     isoform 1"
                     /note="IMAGE5767589; PDZ domain-containing RING finger
                     protein 4; SEMACAP3-like protein; ligand of Numb protein X
                     4"
                     /calculated_mol_wt=116973
     Region          12..64
                     /region_name="RING-HC_LNX4"
                     /note="RING finger, HC subclass, found in ligand of numb
                     protein X 4 (LNX4); cd16719"
                     /db_xref="CDD:438379"
     Site            order(18,21,33,35,38,41,52,56)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:438379"
     Region          221..312
                     /region_name="PDZ1-PDZRN4-like"
                     /note="PDZ domain 1 of PDZ domain-containing RING finger
                     protein 4 (PDZRN4), PDZRN3-B, and related domains;
                     cd06715"
                     /db_xref="CDD:467199"
     Site            order(233..239,259,262,292,296,299..300)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467199"
     Region          398..486
                     /region_name="PDZ2-PDZRN4-like"
                     /note="PDZ domain 2 of PDZ domain-containing RING finger
                     protein 4 (PDZRN4), PDZRN3-B, and related domains;
                     cd06716"
                     /db_xref="CDD:467200"
     Site            order(413..419,433,436,464,468,471..472)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467200"
     CDS             1..1036
                     /gene="PDZRN4"
                     /gene_synonym="LNX4; SAMCAP3L"
                     /coded_by="NM_001164595.2:137..3247"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53777.1"
                     /db_xref="GeneID:29951"
                     /db_xref="HGNC:HGNC:30552"
                     /db_xref="MIM:609730"
ORIGIN      
        1 mgfalerfae avdpaleckl cgqvleeplc tpcghvfcas cllpwavrrr rcplqcqpla
       61 pgelyrvlpl rsliqklrvq cdyrargcgh svrlheleah vehcdfgpar rlrsrggcas
      121 glgggevpar ggcgptprag rgggarggpp ggrwgrgrgp gprvlawrrr ekallaqlwa
      181 lqgevqltar ryqekftqym ahvrnfvgdl ggghrrdgeh kpftivlere ndtlgfniig
      241 grpnqnnqeg tstegiyvsk ilengpadra dgleihdkim evngkdlska theeaveafr
      301 nakepivvqv lrrtplsrpa ygmasevqlm nastqtditf ehimalaklr pptppvpdic
      361 pfllsdschs lhpmehefye dneyisslpa dadrtedfey eevelcrvss qeklgltvcy
      421 rtddeedtgi yvsevdpnsi aakdgrireg drilqinged vqnreeaval lsndeckriv
      481 llvarpeiql degwledern efleelnlem leeehneamq ptaneveqpk kqeeeegttd
      541 tatsssnnhe kdsgvgrtde slrndesseq enaaedpnst slkskrdlgq sqdtlgsvel
      601 qyneslvsge yidsdcignp dedcerfrql lelkckirnh geydlyysss tiecnqgeqe
      661 gvehelqlln eelrnielec qnimqahrlq kvtdqygdiw tlhdggfrny ntsidmqrgk
      721 lddimehpek sdkdsssayn taescrstpl tvdrspdssl prvinltnkk nlrstmaatq
      781 sssgqsskes tstkaktteq gcsaeskekv legsklpdqe kavsehipyl spyhsssyry
      841 anipaharhy qsymqliqqk saveyaqsql slvsmckesq kcsepkmewk vkirsdgtry
      901 itkrpvrdri lkeralkike ersgmttddd tmsemkmgry wskeerkqhl vrakeqrrrr
      961 efmmrsrlec lkespqsgse gkkeiniiel shkkmmkkrn kkildnwmti qelmthgaks
     1021 pdgtrvhnaf lsvttv
//
LOCUS       NP_777358                380 aa            linear   PRI 20-NOV-2025
DEFINITION  isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial isoform
            b precursor [Homo sapiens].
ACCESSION   NP_777358
VERSION     NP_777358.1
DBSOURCE    REFSEQ: accession NM_174869.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Bianco,L., Navarro,J., Michiels,C., Sangermano,R., Condroyer,C.,
            Antonio,A., Antropoli,A., Andrieu,C., Place,E.M., Pierce,E.A., El
            Shamieh,S., Smirnov,V., Kalatzis,V., Mansard,L., Roux,A.F.,
            Bocquet,B., Sahel,J.A., Meunier,I., Bujakowska,K.M., Audo,I. and
            Zeitz,C.
  TITLE     Identification of IDH3G, encoding the gamma subunit of
            mitochondrial isocitrate dehydrogenase, as a novel candidate gene
            for X-linked retinitis pigmentosa
  JOURNAL   Genet Med 27 (6), 101418 (2025)
   PUBMED   40119724
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Ma,T., Peng,Y., Huang,W., Liu,Y. and Ding,J.
  TITLE     The beta and gamma subunits play distinct functional roles in the
            alpha2betagamma heterotetramer of human NAD-dependent isocitrate
            dehydrogenase
  JOURNAL   Sci Rep 7, 41882 (2017)
   PUBMED   28139779
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Weiss,C., Zeng,Y., Huang,J., Sobocka,M.B. and Rushbrook,J.I.
  TITLE     Bovine NAD+-dependent isocitrate dehydrogenase: alternative
            splicing and tissue-dependent expression of subunit 1
  JOURNAL   Biochemistry 39 (7), 1807-1816 (2000)
   PUBMED   10677231
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Kim,Y.O., Koh,H.J., Kim,S.H., Jo,S.H., Huh,J.W., Jeong,K.S.,
            Lee,I.J., Song,B.J. and Huh,T.L.
  TITLE     Identification and functional characterization of a novel,
            tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta
            subunit isoform
  JOURNAL   J Biol Chem 274 (52), 36866-36875 (1999)
   PUBMED   10601238
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
  TITLE     Genomic organization of two novel genes on human Xq28: compact head
            to head arrangement of IDH gamma and TRAP delta is conserved in rat
            and mouse
  JOURNAL   Genomics 44 (1), 8-14 (1997)
   PUBMED   9286695
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Sandoval,N., Bauer,D., Brenner,V., Coy,J.F., Drescher,B.,
            Kioschis,P., Korn,B., Nyakatura,G., Poustka,A., Reichwald,K.,
            Rosenthal,A. and Platzer,M.
  TITLE     The genomic organization of a human creatine transporter (CRTR)
            gene located in Xq28
  JOURNAL   Genomics 35 (2), 383-385 (1996)
   PUBMED   8661155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI831096.1, BC000933.2 and
            U69268.1.
            
            Summary: Isocitrate dehydrogenases catalyze the oxidative
            decarboxylation of isocitrate to 2-oxoglutarate. These enzymes
            belong to two distinct subclasses, one of which utilizes NAD(+) as
            the electron acceptor and the other NADP(+). Five isocitrate
            dehydrogenases have been reported: three NAD(+)-dependent
            isocitrate dehydrogenases, which localize to the mitochondrial
            matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of
            which is mitochondrial and the other predominantly cytosolic.
            NAD(+)-dependent isocitrate dehydrogenases catalyze the
            allosterically regulated rate-limiting step of the tricarboxylic
            acid cycle. Each isozyme is a heterotetramer that is composed of
            two alpha subunits, one beta subunit, and one gamma subunit. The
            protein encoded by this gene is the gamma subunit of one isozyme of
            NAD(+)-dependent isocitrate dehydrogenase. This gene is a candidate
            gene for periventricular heterotopia. Several alternatively spliced
            transcript variants of this gene have been described, but only some
            of their full length natures have been determined. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding region resulting in a frameshift, compared to variant 1.
            Variant 2 encodes a shorter isoform (b) with a distinct C-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.120379.1,
                                           SRR1163658.2337.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..380
                     /product="isocitrate dehydrogenase [NAD] subunit gamma,
                     mitochondrial isoform b precursor"
                     /EC_number="1.1.1.41"
                     /note="NAD+-specific ICDH; IDH-gamma; isocitrate
                     dehydrogenase 3 (NAD(+)) gamma; isocitrate dehydrogenase,
                     NAD(+)-specific, mitochondrial, gamma subunit; isocitrate
                     dehydrogenase (NAD(+)) 3 gamma; isocitrate dehydrogenase
                     [NAD] subunit gamma, mitochondrial; NAD(+)-specific ICDH
                     subunit gamma; isocitric dehydrogenase subunit gamma; NAD
                     (H)-specific isocitrate dehydrogenase gamma subunit;
                     isocitrate dehydrogenase 3 (NAD+) gamma; isocitrate
                     dehydrogenase 3 gamma"
                     /calculated_mol_wt=37488
     transit_peptide 1..39
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P51553.1)"
                     /calculated_mol_wt=3998
     mat_peptide     40..380
                     /product="isocitrate dehydrogenase [NAD] subunit gamma,
                     mitochondrial isoform b"
                     /calculated_mol_wt=37488
     Region          52..364
                     /region_name="Iso_dh"
                     /note="Isocitrate/isopropylmalate dehydrogenase; cl00445"
                     /db_xref="CDD:444908"
     CDS             1..380
                     /gene="IDH3G"
                     /gene_synonym="H-IDHG; RP99"
                     /coded_by="NM_174869.3:50..1192"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS44019.1"
                     /db_xref="GeneID:3421"
                     /db_xref="HGNC:HGNC:5386"
                     /db_xref="MIM:300089"
ORIGIN      
        1 malkvatvag saakavlgpa llcrpwevlg ahevpsrnif seqtippsak yggrhtvtmi
       61 pgdgigpelm lhvksvfrha cvpvdfeevh vssnadeedi rnaimairrn rvalkgniet
      121 nhnlppshks rnnilrtsld lyanvihcks lpgvvtrhkd idilivrent egeysslehe
      181 svagvveslk iitkakslri aeyafklaqe sgrkkvtavh kanimklgdg lflqccreva
      241 arypqitfen mivdnttmql vsrpqqfdvm vmpnlygniv nnvcaglvgg pglvaganyg
      301 hvyavfetat rntgksiank nianptatll ascmmldhlk lhsyatsirk avlasmdnen
      361 vrfpshptll prpvspcsll
//
LOCUS       NP_001317587             737 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform e
            [Homo sapiens].
ACCESSION   NP_001317587 XP_016863644
VERSION     NP_001317587.1
DBSOURCE    REFSEQ: accession NM_001330658.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 737)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596608.1, BC027946.1,
            AC093804.3, BC088372.1, AC131953.1 and AL080130.1.
            
            On Aug 31, 2016 this sequence version replaced XP_016863644.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (8) lacks an exon in the 5' UTR,
            uses an alternate in-frame splice site and lacks an alternate
            in-frame exon in the central coding region, compared to variant 1,
            resulting in an isoform (e) that is shorter than isoform a.
            Variants 8 and 9 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.62033.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..737
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform e"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=80857
     Region          292..320
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          395..532
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(410,478,495)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(477..482,495,517,521)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Region          561..687
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(572,646,665)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(583,585,633..634,636..643,645,653,659,669,671,674,
                     678,681..682,684..685)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..737
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001330658.2:457..2670"
                     /note="isoform e is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS82918.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 msevlpadsg vdtlavfmas sgttdvtnrn spatppntln lrsshnelln aeikhtetkn
       61 stppkcrkky altniqaamg lsdpaaqpll gngsaniklv kngenqlrka aeqgqqdpnk
      121 nlsptavini tseklegkep hpqdssscei lpsqprrtks flnyyadlet sareleqnrg
      181 nhhgtaeeks qpvqgqasti igngdlllqk pnrpqssped gqvatvsssp etkkdhpktg
      241 aktdcalhri qnlapsdees swttlsqdsa spsspdetdi wsdhsfqtdp dlppgwkrvs
      301 diagtyywhi ptgttqwerp vsipadlqgs rkgslssvtp sptpenedlh aatvnpdpsl
      361 kefegatlry aslklrnaph pddddscsin sdpeakcfav rslgwvemae edlapgkssv
      421 avnncirqls yckndirdtv giwgegkdmy lilendmlsl vdpmdrsvlh sqpivsirvw
      481 gvgrdngrdf ayvardkdtr ilkchvfrcd tpakaiatsl heicskimae rknakalacs
      541 slqeranvnl dvplqvdfpt pktelvqkfh vqylgmlpvd kpvgmdilns aienlmtssn
      601 kedwlsvnmn vadatvtvis ekneeevlve crvrflsfmg vgkdvhtfaf imdtgnqrfe
      661 chvfwcepna gnvseavqaa cmlryqkclv arppsqkvrp ppppadsvtr rvttnvkrgv
      721 lslidtlkqk rpvtemp
//
LOCUS       NP_055955                644 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin--tyrosine ligase-like protein 12 [Homo sapiens].
ACCESSION   NP_055955
VERSION     NP_055955.1
DBSOURCE    REFSEQ: accession NM_015140.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Ceglowski,J., Hoffman,H.K., Neumann,A.J., Hoff,K.J., McCurdy,B.L.,
            Moore,J.K. and Prekeris,R.
  TITLE     TTLL12 is required for primary ciliary axoneme formation in
            polarized epithelial cells
  JOURNAL   EMBO Rep 25 (1), 198-227 (2024)
   PUBMED   38177908
  REMARK    GeneRIF: TTLL12 is required for primary ciliary axoneme formation
            in polarized epithelial cells.
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Brants,J., Semenchenko,K., Wasylyk,C., Robert,A., Carles,A.,
            Zambrano,A., Pradeau-Aubreton,K., Birck,C., Schalken,J.A., Poch,O.,
            de Mey,J. and Wasylyk,B.
  TITLE     Tubulin tyrosine ligase like 12, a TTLL family member with SET- and
            TTL-like domains and roles in histone and tubulin modifications and
            mitosis
  JOURNAL   PLoS One 7 (12), e51258 (2012)
   PUBMED   23251473
  REMARK    GeneRIF: results suggest that hTTLL12 has non-catalytic functions
            related to tubulin and histone modification, which could be linked
            to its effects on mitosis and chromosome number stability
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Wasylyk,C., Zambrano,A., Zhao,C., Brants,J., Abecassis,J.,
            Schalken,J.A., Rogatsch,H., Schaefer,G., Pycha,A., Klocker,H. and
            Wasylyk,B.
  TITLE     Tubulin tyrosine ligase like 12 links to prostate cancer through
            tubulin posttranslational modification and chromosome ploidy
  JOURNAL   Int J Cancer 127 (11), 2542-2553 (2010)
   PUBMED   20162578
  REMARK    GeneRIF: Results raise the possibility that TTLL12 could contribute
            to tumorigenesis through effects on the cytoskeleton, tubulin
            modification and chromosome number stability.
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Janke,C., Rogowski,K., Wloga,D., Regnard,C., Kajava,A.V.,
            Strub,J.M., Temurak,N., van Dijk,J., Boucher,D., van Dorsselaer,A.,
            Suryavanshi,S., Gaertig,J. and Edde,B.
  TITLE     Tubulin polyglutamylase enzymes are members of the TTL domain
            protein family
  JOURNAL   Science 308 (5729), 1758-1762 (2005)
   PUBMED   15890843
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z82214.23, BX411143.2, BC001070.2 and BE785973.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001070.2, SRR1803615.158732.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267761 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216129.7/ ENSP00000216129.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..644
                     /product="tubulin--tyrosine ligase-like protein 12"
                     /note="tubulin tyrosine ligase-like family, member 12;
                     inactive tubulin--tyrosine ligase-like protein 12"
                     /calculated_mol_wt=74273
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14166.2)"
     Region          346..642
                     /region_name="TTL"
                     /note="Tubulin-tyrosine ligase family; pfam03133"
                     /db_xref="CDD:397308"
     CDS             1..644
                     /gene="TTLL12"
                     /gene_synonym="dJ526I14.2"
                     /coded_by="NM_015140.4:66..2000"
                     /db_xref="CCDS:CCDS14047.1"
                     /db_xref="GeneID:23170"
                     /db_xref="HGNC:HGNC:28974"
                     /db_xref="MIM:619410"
ORIGIN      
        1 meaergperr paersspgqt peegaqalae faalhgpalr asgvperywg rllhklehev
       61 fdagevfgim qveeveeeed eaarevrkqq pnpgnelcyk vivtresglq aahpnsifli
      121 dhawtcrveh arqqlqqvpg llhrmanlmg iefhgelpst eavalvleem wkfnqtyqla
      181 hgtaeekmpv wyimdefgsr iqhadvpsfa tapffympqq vaytllwplr dldtgeevtr
      241 dfaygetdpl irkcmllpwa ptdmldlssc tpeppaehyq aileenkekl pldinpvvhp
      301 hghifkvytd vqqvasslth prftltqsea dadilfnfsh fkdyrklsqe rpgvllnqfp
      361 cenlltvkdc lasiarragg pegppwlprt fnlrtelpqf vsyfqqrerw gednhwickp
      421 wnlarsldth vtkslhsiir hrestpkvvs kyiespvlfl redvgkvkfd iryivllrsv
      481 rplrlfvydv fwlrfsnraf alndlddyek hftvmnydpd vvlkqvhcee fipefekqyp
      541 efpwtdvqae ifraftelfq vacakppplg lcdypssram yavdlmlkwd ngpdgrrvmq
      601 pqilevnfnp dceracryhp tffndvfstl fldqpggchv tclv
//
LOCUS       NP_001161940             505 aa            linear   PRI 20-NOV-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001161940
VERSION     NP_001161940.1
DBSOURCE    REFSEQ: accession NM_001168468.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Pouly,D., Chenaux,S., Martin,V., Babis,M., Koch,R., Nagoshi,E.,
            Katanaev,V.L., Gachon,F. and Staub,O.
  TITLE     USP2-45 Is a Circadian Clock Output Effector Regulating Calcium
            Absorption at the Post-Translational Level
  JOURNAL   PLoS One 11 (1), e0145155 (2016)
   PUBMED   26756164
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Reid,H.M., Turner,E.C., Mulvaney,E.P., Hyland,P.B., McLean,C. and
            Kinsella,B.T.
  TITLE     Interaction of the human prostacyclin receptor and the NHERF4
            family member intestinal and kidney enriched PDZ protein (IKEPP)
  JOURNAL   Biochim Biophys Acta 1823 (10), 1998-2012 (2012)
   PUBMED   22884631
  REMARK    GeneRIF: IKEPP was also found to be expressed in vascular
            endothelial cells where it co-localizes and complexes with the hIP
            Erratum:[Biochim Biophys Acta. 2015 Jan;1853(1):63-4]
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Zachos,N.C., Hodson,C., Kovbasnjuk,O., Li,X., Thelin,W.R., Cha,B.,
            Milgram,S. and Donowitz,M.
  TITLE     Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
            (NHERF4) dependent mechanism
  JOURNAL   Cell Physiol Biochem 22 (5-6), 693-704 (2008)
   PUBMED   19088451
  REMARK    GeneRIF: Regulation of NHE3 depends on the nature of the NHERF
            family member associating with NHE3 and the accompanying NHE3
            complexes.
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Thelin,W.R., Hodson,C.A. and Milgram,S.L.
  TITLE     Beyond the brush border: NHERF4 blazes new NHERF turf
  JOURNAL   J Physiol 567 (Pt 1), 13-19 (2005)
   PUBMED   15994182
  REMARK    Review article
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Kato,Y., Sai,Y., Yoshida,K., Watanabe,C., Hirata,T. and Tsuji,A.
  TITLE     PDZK1 directly regulates the function of organic cation/carnitine
            transporter OCTN2
  JOURNAL   Mol Pharmacol 67 (3), 734-743 (2005)
   PUBMED   15523054
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Hegedus,T., Sessler,T., Scott,R., Thelin,W., Bakos,E., Varadi,A.,
            Szabo,K., Homolya,L., Milgram,S.L. and Sarkadi,B.
  TITLE     C-terminal phosphorylation of MRP2 modulates its interaction with
            PDZ proteins
  JOURNAL   Biochem Biophys Res Commun 302 (3), 454-461 (2003)
   PUBMED   12615054
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Scott,R.O., Thelin,W.R. and Milgram,S.L.
  TITLE     A novel PDZ protein regulates the activity of guanylyl cyclase C,
            the heat-stable enterotoxin receptor
  JOURNAL   J Biol Chem 277 (25), 22934-22941 (2002)
   PUBMED   11950846
  REMARK    GeneRIF: A novel PDZ protein regulates the activity of guanylyl
            cyclase C, the heat-stable enterotoxin receptor.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA381610.1, AY047359.1 and AB094096.1.
            
            Summary: Guanylyl cyclase C (GCC, or GUCY2C; MIM 601330) produces
            cGMP following the binding of either endogenous ligands or
            heat-stable enterotoxins secreted by E. coli and other enteric
            bacteria. Activation of GCC initiates a signaling cascade that
            leads to phosphorylation of the cystic fibrosis transmembrane
            conductance regulator (CFTR; MIM 602421), followed by a net efflux
            of ions and water into the intestinal lumen. IKEPP is a regulatory
            protein that associates with GCC and regulates the amount of cGMP
            produced following receptor stimulation (Scott et al., 2002 [PubMed
            11950846]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315403.1, AY047359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355547.10/ ENSP00000347742.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..505
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF4
                     isoform 1"
                     /note="PDZ domain containing 2; natrium-phosphate
                     cotransporter IIa C-terminal-associated protein 2;
                     sodium-hydrogen exchanger regulatory factor 4; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF4; intestinal and
                     kidney enriched PDZ protein; NHERF-4; naPi-Cap2; PDZ
                     domain-containing protein 2; PDZ domain-containing protein
                     3; PDZ domain containing 3; na/Pi cotransporter
                     C-terminal-associated protein 2; Na(+)/H(+) exchange
                     regulatory cofactor 4"
                     /calculated_mol_wt=54086
     Region          48..127
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(59..65,76,79,108,112,115..116)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          156..233
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(166..170,181,184,213,217,220..221)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          262..344
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(272..278,292,295,324,328,331..332)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          409..478
                     /region_name="PDZ"
                     /note="Domain present in PSD-95, Dlg, and ZO-1/2;
                     smart00228"
                     /db_xref="CDD:214570"
     CDS             1..505
                     /gene="NHERF4"
                     /gene_synonym="IKEPP; PDZD3; PDZK2"
                     /coded_by="NM_001168468.2:21..1538"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53719.1"
                     /db_xref="GeneID:79849"
                     /db_xref="HGNC:HGNC:19891"
                     /db_xref="MIM:607146"
ORIGIN      
        1 mekaadlqdt asltlkfkfn pklgidnpvl slaedhdpyd pwslerprfc llskeegksf
       61 gfhlqqelgr aghvvcrvdp gtsaqrqglq egdrilavnn dvvehedyav vvrrirassp
      121 rvlltvlarh ahdvaraqlg edahlcptlg pgvrprlchi vkdeggfgfs vthgnqgpfw
      181 lvlstggaae ragvppgarl levngvsvek fthnqltrkl wqsgqqvtll vagpeveeqc
      241 rqlglplaap laegwalptk prclhlekgp qgfgfllree kgldgrpgqf lwevdpglpa
      301 kkagmqagdr lvavagesve glgheetvsr iqgqgscvsl tvvdpeadrf fsmvrlspll
      361 flenteapas prgsssaslv etedpsledt svpsvplgsr qcflypgpgg sygfrlscva
      421 sgprlfisqv tpggsaarag lqvgdvilev ngypvggqnd lerlqqlpea epplclklaa
      481 rslrgleawi ppgaaedwal asdll
//
LOCUS       NP_064706                582 aa            linear   PRI 20-NOV-2025
DEFINITION  max-binding protein MNT [Homo sapiens].
ACCESSION   NP_064706
VERSION     NP_064706.1
DBSOURCE    REFSEQ: accession NM_020310.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 582)
  AUTHORS   Zhao,G., Liang,J., Zhang,Y., Shan,G., Bian,Y., Gu,J., Zhan,C. and
            Ge,D.
  TITLE     MNT inhibits lung adenocarcinoma ferroptosis and chemosensitivity
            by suppressing SAT1
  JOURNAL   Commun Biol 7 (1), 680 (2024)
   PUBMED   38831092
  REMARK    GeneRIF: MNT inhibits lung adenocarcinoma ferroptosis and
            chemosensitivity by suppressing SAT1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 582)
  AUTHORS   Lavin,D.P., Abassi,L., Inayatullah,M. and Tiwari,V.K.
  TITLE     Mnt Represses Epithelial Identity To Promote
            Epithelial-to-Mesenchymal Transition
  JOURNAL   Mol Cell Biol 41 (11), e0018321 (2021)
   PUBMED   34460331
  REMARK    GeneRIF: Mnt Represses Epithelial Identity To Promote
            Epithelial-to-Mesenchymal Transition.
REFERENCE   3  (residues 1 to 582)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 582)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 582)
  AUTHORS   Lafita-Navarro,M.C., Liano-Pons,J., Quintanilla,A., Varela,I.,
            Blanco,R., Ourique,F., Bretones,G., Aresti,J., Molina,E.,
            Carroll,P., Hurlin,P., Romero,O.A., Sanchez-Cespedes,M.,
            Eisenman,R.N., Delgado,M.D. and Leon,J.
  TITLE     The MNT transcription factor autoregulates its expression and
            supports proliferation in MYC-associated factor X (MAX)-deficient
            cells
  JOURNAL   J Biol Chem 295 (7), 2001-2017 (2020)
   PUBMED   31919096
  REMARK    GeneRIF: The MNT transcription factor autoregulates its expression
            and supports proliferation in MYC-associated factor X
            (MAX)-deficient cells.
REFERENCE   6  (residues 1 to 582)
  AUTHORS   Meroni,G., Cairo,S., Merla,G., Messali,S., Brent,R., Ballabio,A.
            and Reymond,A.
  TITLE     Mlx, a new Max-like bHLHZip family member: the center stage of a
            novel transcription factors regulatory pathway?
  JOURNAL   Oncogene 19 (29), 3266-3277 (2000)
   PUBMED   10918583
REFERENCE   7  (residues 1 to 582)
  AUTHORS   Billin,A.N., Eilers,A.L., Queva,C. and Ayer,D.E.
  TITLE     Mlx, a novel Max-like BHLHZip protein that interacts with the Max
            network of transcription factors
  JOURNAL   J Biol Chem 274 (51), 36344-36350 (1999)
   PUBMED   10593926
REFERENCE   8  (residues 1 to 582)
  AUTHORS   Lo Nigro,C., Venesio,T., Reymond,A., Meroni,G., Alberici,P.,
            Cainarca,S., Enrico,F., Stack,M., Ledbetter,D.H., Liscia,D.S.,
            Ballabio,A. and Carrozzo,R.
  TITLE     The human ROX gene: genomic structure and mutation analysis in
            human breast tumors
  JOURNAL   Genomics 49 (2), 275-282 (1998)
   PUBMED   9598315
REFERENCE   9  (residues 1 to 582)
  AUTHORS   Hirotsune,S., Pack,S.D., Chong,S.S., Robbins,C.M., Pavan,W.J.,
            Ledbetter,D.H. and Wynshaw-Boris,A.
  TITLE     Genomic organization of the murine Miller-Dieker/lissencephaly
            region: conservation of linkage with the human region
  JOURNAL   Genome Res 7 (6), 625-634 (1997)
   PUBMED   9199935
REFERENCE   10 (residues 1 to 582)
  AUTHORS   Meroni,G., Reymond,A., Alcalay,M., Borsani,G., Tanigami,A.,
            Tonlorenzi,R., Lo Nigro,C., Messali,S., Zollo,M., Ledbetter,D.H.,
            Brent,R., Ballabio,A. and Carrozzo,R.
  TITLE     Rox, a novel bHLHZip protein expressed in quiescent cells that
            heterodimerizes with Max, binds a non-canonical E box and acts as a
            transcriptional repressor
  JOURNAL   EMBO J 16 (10), 2892-2906 (1997)
   PUBMED   9184233
  REMARK    Erratum:[EMBO J 1997 Oct 1;16(19):6055]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006435.7, CN428913.1,
            CN428911.1, X96401.1, BM469815.1, BQ675978.1, BM820333.1,
            BM876428.1, CA950091.1 and BM876168.1.
            
            Summary: The Myc/Max/Mad network comprises a group of transcription
            factors that co-interact to regulate gene-specific transcriptional
            activation or repression. This gene encodes a protein member of the
            Myc/Max/Mad network. This protein has a
            basic-Helix-Loop-Helix-zipper domain (bHLHzip) with which it binds
            the canonical DNA sequence CANNTG, known as the E box, following
            heterodimerization with Max proteins. This protein is likely a
            transcriptional repressor and an antagonist of Myc-dependent
            transcriptional activation and cell growth. This protein represses
            transcription by binding to DNA binding proteins at its N-terminal
            Sin3-interaction domain. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC117563.1, X96401.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000174618.5/ ENSP00000174618.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..582
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..582
                     /product="max-binding protein MNT"
                     /note="Max-interacting protein; myc antagonist MNT; class
                     D basic helix-loop-helix protein 3; MAX binding protein;
                     MNT, MAX dimerization protein"
                     /calculated_mol_wt=62169
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99583.1)"
     Region          18..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99583.1)"
     Region          220..296
                     /region_name="bHLHzip_Mnt"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in Max-binding protein Mnt and similar proteins;
                     cd11402"
                     /db_xref="CDD:381408"
     Site            order(225..226,229..230,232..233,237,255..257)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381408"
     Site            order(236..237,239..244,246..247,258,261,265,267..269,
                     271..272,274..275,278,282,285..286,288..289,292..293,
                     295..296)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381408"
     Site            order(236,239..240,242..243,246..247,258,261,265,267..269,
                     271..272,274..275,278,282,285..286,288..289,292..293,
                     295..296)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:381408"
     Region          <254..372
                     /region_name="CALCOCO1"
                     /note="Calcium binding and coiled-coil domain (CALCOCO1)
                     like; pfam07888"
                     /db_xref="CDD:462303"
     Region          271..299
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99583.1)"
     Region          319..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99583.1)"
     CDS             1..582
                     /gene="MNT"
                     /gene_synonym="bHLHd3; lncRNA-HAL; MAD6; MXD6; ROX"
                     /coded_by="NM_020310.3:349..2097"
                     /db_xref="CCDS:CCDS11018.1"
                     /db_xref="GeneID:4335"
                     /db_xref="HGNC:HGNC:7188"
                     /db_xref="MIM:603039"
ORIGIN      
        1 msietlleaa rflewqaqqq qrareeqerl rleqereqeq kkanslarla htlpveeprm
       61 eapplplspp apppappppl atpapltvip ipvvtnspqp lppppplpaa aqplplaprq
      121 palvgapgls ikepaplpsr pqvptpapll pdskatippn gspkplqplp tpvltiaphp
      181 gvqpqlapqq pppptlgtlk lapaeevkss eqkkrpggig trevhnklek nrrahlkecf
      241 etlkrnipnv ddkktsnlsv lrtalryiqs lkrkekeyeh emerlareki atqqrlaelk
      301 helsqwmdvl eidrvlrqtg qpeddqasts tasegednid edmeedragl gppklshrpq
      361 pellkstlpp psttpaplpp hphphphsva lppahlpvqq qqpqqktplp apppppaapa
      421 qtlvpapahl vatagggstv iahtatthas viqtvnhvlq gpggkhiahi apsapspavq
      481 lapatppigh itvhpatlnh vahlgsqlpl ypqpvavshi ahtlshqqvn gtaglgppat
      541 vmakpavgaq vvhhpqlvgq tvlnpvtmvt mpsfpvstlk la
//
LOCUS       NP_001008710             196 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein with multiple splicing isoform A [Homo
            sapiens].
ACCESSION   NP_001008710
VERSION     NP_001008710.1
DBSOURCE    REFSEQ: accession NM_001008710.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Gan,P., Wang,Z., Bezprozvannaya,S., McAnally,J.R., Tan,W., Li,H.,
            Bassel-Duby,R., Liu,N. and Olson,E.N.
  TITLE     RBPMS regulates cardiomyocyte contraction and cardiac function
            through RNA alternative splicing
  JOURNAL   Cardiovasc Res 120 (1), 56-68 (2024)
   PUBMED   37890031
  REMARK    GeneRIF: RBPMS regulates cardiomyocyte contraction and cardiac
            function through RNA alternative splicing.
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Gong,T.T., Liu,F.H., Xiao,Q., Li,Y.Z., Wei,Y.F., Xu,H.L., Cao,F.,
            Sun,M.L., Jiang,F.L., Tao,T., Ma,Q.P., Qin,X., Song,Y., Gao,S.,
            Wu,L., Zhao,Y.H., Huang,D.H. and Wu,Q.J.
  TITLE     SH3RF2 contributes to cisplatin resistance in ovarian cancer cells
            by promoting RBPMS degradation
  JOURNAL   Commun Biol 7 (1), 67 (2024)
   PUBMED   38195842
  REMARK    GeneRIF: SH3RF2 contributes to cisplatin resistance in ovarian
            cancer cells by promoting RBPMS degradation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Yang,Y., Lee,G.C., Nakagaki-Silva,E., Huang,Y., Peacey,M.,
            Partridge,R., Gooding,C. and Smith,C.W.J.
  TITLE     Cell-type specific regulator RBPMS switches alternative splicing
            via higher-order oligomerization and heterotypic interactions with
            other splicing regulators
  JOURNAL   Nucleic Acids Res 51 (18), 9961-9982 (2023)
   PUBMED   37548402
  REMARK    GeneRIF: Cell-type specific regulator RBPMS switches alternative
            splicing via higher-order oligomerization and heterotypic
            interactions with other splicing regulators.
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Bartsch,D., Kalamkar,K., Ahuja,G., Lackmann,J.W., Hescheler,J.,
            Weber,T., Bazzi,H., Clamer,M., Mendjan,S., Papantonis,A. and
            Kurian,L.
  TITLE     mRNA translational specialization by RBPMS presets the competence
            for cardiac commitment in hESCs
  JOURNAL   Sci Adv 9 (13), eade1792 (2023)
   PUBMED   36989351
  REMARK    GeneRIF: mRNA translational specialization by RBPMS presets the
            competence for cardiac commitment in hESCs.
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Sun,Y., Ding,L., Zhang,H., Han,J., Yang,X., Yan,J., Zhu,Y., Li,J.,
            Song,H. and Ye,Q.
  TITLE     Potentiation of Smad-mediated transcriptional activation by the
            RNA-binding protein RBPMS
  JOURNAL   Nucleic Acids Res 34 (21), 6314-6326 (2006)
   PUBMED   17099224
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Shimamoto,A., Kitao,S., Ichikawa,K., Suzuki,N., Yamabe,Y.,
            Imamura,O., Tokutake,Y., Satoh,M., Matsumoto,T., Kuromitsu,J.,
            Kataoka,H., Sugawara,K., Sugawara,M., Sugimoto,M., Goto,M. and
            Furuichi,Y.
  TITLE     A unique human gene that spans over 230 kb in the human chromosome
            8p11-12 and codes multiple family proteins sharing RNA-binding
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10913-10917 (1996)
   PUBMED   8855282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CX165198.1, BC003608.2,
            D84107.1, CX781149.1, CN360712.1 and BX097929.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the RNA recognition motif
            family of RNA-binding proteins. The RNA recognition motif is
            between 80-100 amino acids in length and family members contain one
            to four copies of the motif. The RNA recognition motif consists of
            two short stretches of conserved sequence, as well as a few highly
            conserved hydrophobic residues. The encoded protein has a single,
            putative RNA recognition motif in its N-terminus. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes isoform A. Variants 1
            and 4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.54264.1,
                                           SRR1660809.128176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397323.9/ ENSP00000380486.4
            NMD candidate          :: translation inferred from conservation
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..196
                     /product="RNA-binding protein with multiple splicing
                     isoform A"
                     /note="heart and RRM expressed sequence; RNA binding
                     protein with multiple splicing"
                     /calculated_mol_wt=21671
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVB0; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          23..98
                     /region_name="RRM_RBPMS"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing (RBP-MS);
                     cd12682"
                     /db_xref="CDD:410083"
     Site            27
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Site            61
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     Region          <64..>165
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Region          98..105
                     /region_name="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:26347403"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93062.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q93062.1)"
     CDS             1..196
                     /gene="RBPMS"
                     /gene_synonym="HERMES"
                     /coded_by="NM_001008710.3:553..1143"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6077.1"
                     /db_xref="GeneID:11030"
                     /db_xref="HGNC:HGNC:19097"
                     /db_xref="MIM:601558"
ORIGIN      
        1 mnnggkaeke ntpseanlqe eevrtlfvsg lpldikprel yllfrpfkgy egslikltsk
       61 qpvgfvsfds rseaeaakna lngirfdpei pqtlrlefak antkmaknkl vgtpnpstpl
      121 pntvpqfiar epyeltvpal ypsspevwap yplypaelap alpppaftyp aslhaqmrwl
      181 ppseatsqgw ksrqfc
//
LOCUS       NP_004939                840 aa            linear   PRI 20-NOV-2025
DEFINITION  desmocollin-1 isoform Dsc1b precursor [Homo sapiens].
ACCESSION   NP_004939
VERSION     NP_004939.1
DBSOURCE    REFSEQ: accession NM_004948.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 840)
  AUTHORS   Lapcik,P., Sulc,P., Janacova,L., Jilkova,K., Potesil,D.,
            Bouchalova,P., Muller,P. and Bouchal,P.
  TITLE     Desmocollin-1 is associated with pro-metastatic phenotype of
            luminal A breast cancer cells and is modulated by parthenolide
  JOURNAL   Cell Mol Biol Lett 28 (1), 68 (2023)
   PUBMED   37620794
  REMARK    GeneRIF: Desmocollin-1 is associated with pro-metastatic phenotype
            of luminal A breast cancer cells and is modulated by parthenolide.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 840)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 840)
  AUTHORS   Sliz,E., Huilaja,L., Pasanen,A., Laisk,T., Reimann,E., Magi,R.,
            Hannula-Jouppi,K., Peltonen,S., Salmi,T., Koulu,L., Tasanen,K. and
            Kettunen,J.
  CONSRTM   FinnGen; Estonian Biobank Research Team
  TITLE     Uniting biobank resources reveals novel genetic pathways modulating
            susceptibility for atopic dermatitis
  JOURNAL   J Allergy Clin Immunol 149 (3), 1105-1112 (2022)
   PUBMED   34454985
  REMARK    GeneRIF: Uniting biobank resources reveals novel genetic pathways
            modulating susceptibility for atopic dermatitis.
REFERENCE   4  (residues 1 to 840)
  AUTHORS   Zhang,Z., Zhu,H. and Hu,J.
  TITLE     CircRAB11FIP1 promoted autophagy flux of ovarian cancer through
            DSC1 and miR-129
  JOURNAL   Cell Death Dis 12 (2), 219 (2021)
   PUBMED   33637694
  REMARK    GeneRIF: CircRAB11FIP1 promoted autophagy flux of ovarian cancer
            through DSC1 and miR-129.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 840)
  AUTHORS   Faktor,J., Knopfova,L., Lapcik,P., Janacova,L., Paralova,V.,
            Bouchalova,P., Muller,P., Benes,P. and Bouchal,P.
  TITLE     Proteomics Identification and Validation of Desmocollin-1 and
            Catechol-O-Methyltransferase as Proteins Associated with Breast
            Cancer Cell Migration and Metastasis
  JOURNAL   Proteomics 19 (21-22), e1900073 (2019)
   PUBMED   31617665
  REMARK    GeneRIF: desmocollin-1 (DSC1) is validated as a protein connected
            with lymph node status of luminal A breast cancer, tumor grade, and
            Her-2 status and catechol-O-methyltransferase is successfully
            verified as a protein associated with lymph node metastasis of
            triple negative breast cancer.
REFERENCE   6  (residues 1 to 840)
  AUTHORS   King,I.A., Sullivan,K.H., Bennett,R. Jr. and Buxton,R.S.
  TITLE     The desmocollins of human foreskin epidermis: identification and
            chromosomal assignment of a third gene and expression patterns of
            the three isoforms
  JOURNAL   J Invest Dermatol 105 (3), 314-321 (1995)
   PUBMED   7665906
REFERENCE   7  (residues 1 to 840)
  AUTHORS   Troyanovsky,S.M., Troyanovsky,R.B., Eshkind,L.G., Leube,R.E. and
            Franke,W.W.
  TITLE     Identification of amino acid sequence motifs in desmocollin, a
            desmosomal glycoprotein, that are required for plakoglobin binding
            and plaque formation
  JOURNAL   Proc Natl Acad Sci U S A 91 (23), 10790-10794 (1994)
   PUBMED   7971964
REFERENCE   8  (residues 1 to 840)
  AUTHORS   King,I.A., Arnemann,J., Spurr,N.K. and Buxton,R.S.
  TITLE     Cloning of the cDNA (DSC1) coding for human type 1 desmocollin and
            its assignment to chromosome 18
  JOURNAL   Genomics 18 (2), 185-194 (1993)
   PUBMED   8288219
REFERENCE   9  (residues 1 to 840)
  AUTHORS   Troyanovsky,S.M., Eshkind,L.G., Troyanovsky,R.B., Leube,R.E. and
            Franke,W.W.
  TITLE     Contributions of cytoplasmic domains of desmosomal cadherins to
            desmosome assembly and intermediate filament anchorage
  JOURNAL   Cell 72 (4), 561-574 (1993)
   PUBMED   7679953
REFERENCE   10 (residues 1 to 840)
  AUTHORS   King,I.A., Magee,A.I., Rees,D.A. and Buxton,R.S.
  TITLE     Keratinization is associated with the expression of a new protein
            related to the desmosomal cadherins DGII/III
  JOURNAL   FEBS Lett 286 (1-2), 9-12 (1991)
   PUBMED   1713860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X72925.1, Z34522.1, AC012417.13
            and CU447407.1.
            
            Summary: The protein encoded by this gene is a calcium-dependent
            glycoprotein that is a member of the desmocollin subfamily of the
            cadherin superfamily. These desmosomal family members, along with
            the desmogleins, are found primarily in epithelial cells where they
            constitute the adhesive proteins of the desmosome cell-cell
            junction and are required for cell adhesion and desmosome
            formation. A subtype of IgA pemphigus, a life-threatening
            autoimmune disease, is characterized by the presence of
            autoantibodies that target the encoded protein. The desmosomal
            family members are arranged in two clusters on chromosome 18.
            Alternative splicing of this gene results in multiple transcript
            variants. At least one of these variants encodes a preproprotein
            that is proteolytically processed to generate the mature protein.
            [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (Dsc1b) includes an alternate exon
            in the 3' coding region, resulting in a frameshift and an early
            stop codon, compared to isoform Dsc1a. The encoded isoform (Dsc1b)
            is shorter than isoform Dsc1a. This isoform (Dsc1b) may undergo
            proteolytic processing similar to isoform Dsc1a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X72925.1, Z34522.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..840
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..840
                     /product="desmocollin-1 isoform Dsc1b precursor"
                     /note="desmosomal glycoprotein 2/3; cadherin family member
                     1"
                     /calculated_mol_wt=90843
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3011
     Region          29..109
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; smart01055"
                     /db_xref="CDD:214999"
     Region          139..233
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(145..146,201,203,234,236..237)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            165
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q08554.2)"
     Region          249..350
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(253..254,311,313,346,348..349)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          359..449
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17487921; propagated from
                     UniProtKB/Swiss-Prot (Q08554.2)"
     Region          485..567
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            546
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q08554.2)"
     Region          596..667
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cl46864"
                     /db_xref="CDD:481204"
     Site            692..714
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08554.2)"
     CDS             1..840
                     /gene="DSC1"
                     /gene_synonym="CDHF1; DG2/DG3"
                     /coded_by="NM_004948.3:263..2785"
                     /note="isoform Dsc1b precursor is encoded by transcript
                     variant Dsc1b"
                     /db_xref="CCDS:CCDS11895.1"
                     /db_xref="GeneID:1823"
                     /db_xref="HGNC:HGNC:3035"
                     /db_xref="MIM:125643"
ORIGIN      
        1 malasaapgs ifckqllfsl lvltllcdac qkvylrvpsh lqaetlvgkv nleeclksas
       61 lirssdpafr iledgsiytt hdlilsserk sfsiflsdgq rreqqeikvv lsarenkspk
      121 krhtkdtalk rskrrwapip aslmenslgp fpqhvqqiqs daaqnytify sisgpgvdke
      181 pfnlfyiekd tgdifctrsi drekyeqfal ygyattadgy apeyplplii kieddndnap
      241 yfehrvtift vpencrsgts vgkvtatdld epdtlhtrlk ykilqqipdh pkhfsihpdt
      301 gvittttpfl drekcdtyql imevrdmggq pfglfntgti tisledendn ppsftetsyv
      361 teveenridv eilrmkvqdq dlpntphska vykilqgnen gnfiistdpn tnegvlcvvk
      421 plnyevnrqv ilqvgvinea qfskaassqt ptmctttvtv kiidsdegpe chppvkviqs
      481 qdgfpagqel lgykaldpei ssgeglryqk lgdednwfei nqhtgdlrtl kvldreskfv
      541 knnqynisvv avdavgrsct gtlvvhlddy ndhapqidke vticqnnedf avlkpvdpdg
      601 pengppfqff ldnsasknwn ieekdgktai lrqrqnldyn yysvpiqikd rhglvathml
      661 tvrvcdcstp secrmkdkst rdvrpnvilg rwailamvlg svlllcilft cfcvtakrtv
      721 kkcfpediaq qnlivsnteg pgeevteani rlpmqtsnic dtsmsvgtvg gqgiktqqsf
      781 emvkggytld snkggghqtl esvkgvgqgd tgryaytdwq sftqprlgee sirghtlikn
//
LOCUS       NP_003785                450 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-4 [Homo sapiens].
ACCESSION   NP_003785
VERSION     NP_003785.1
DBSOURCE    REFSEQ: accession NM_003794.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Sugatha,J., Priya,A., Raj,P., Jaimon,E., Swaminathan,U., Jose,A.,
            Pucadyil,T.J. and Datta,S.
  TITLE     Insights into cargo sorting by SNX32 and its role in neurite
            outgrowth
  JOURNAL   Elife 12, e84396 (2023)
   PUBMED   37158588
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Ravussin,A., Brech,A., Tooze,S.A. and Stenmark,H.
  TITLE     The phosphatidylinositol 3-phosphate-binding protein SNX4 controls
            ATG9A recycling and autophagy
  JOURNAL   J Cell Sci 134 (3) (2021)
   PUBMED   33468622
  REMARK    GeneRIF: The phosphatidylinositol 3-phosphate-binding protein SNX4
            controls ATG9A recycling and autophagy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Leprince,C., Le Scolan,E., Meunier,B., Fraisier,V., Brandon,N., De
            Gunzburg,J. and Camonis,J.
  TITLE     Sorting nexin 4 and amphiphysin 2, a new partnership between
            endocytosis and intracellular trafficking
  JOURNAL   J Cell Sci 116 (Pt 10), 1937-1948 (2003)
   PUBMED   12668730
  REMARK    GeneRIF: Sorting nexin 4 and amphiphysin 2 have roles in
            endocytosis and intracellular trafficking
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Parks,W.T., Frank,D.B., Huff,C., Renfrew Haft,C., Martin,J.,
            Meng,X., de Caestecker,M.P., McNally,J.G., Reddi,A., Taylor,S.I.,
            Roberts,A.B., Wang,T. and Lechleider,R.J.
  TITLE     Sorting nexin 6, a novel SNX, interacts with the transforming
            growth factor-beta family of receptor serine-threonine kinases
  JOURNAL   J Biol Chem 276 (22), 19332-19339 (2001)
   PUBMED   11279102
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Wurthner,J.U., Frank,D.B., Felici,A., Green,H.M., Cao,Z.,
            Schneider,M.D., McNally,J.G., Lechleider,R.J. and Roberts,A.B.
  TITLE     Transforming growth factor-beta receptor-associated protein 1 is a
            Smad4 chaperone
  JOURNAL   J Biol Chem 276 (22), 19495-19502 (2001)
   PUBMED   11278302
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Barr,V.A., Haft,D.H. and
            Taylor,S.I.
  TITLE     Identification of a family of sorting nexin molecules and
            characterization of their association with receptors
  JOURNAL   Mol Cell Biol 18 (12), 7278-7287 (1998)
   PUBMED   9819414
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA289870.1, AK001835.1 and
            AI187416.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein associated with the long isoform of the
            leptin receptor and with receptor tyrosine kinases for
            platelet-derived growth factor, insulin, and epidermal growth
            factor in cell cultures, but its function is unknown. This protein
            may form oligomeric complexes with family members. Two transcript
            variants, one protein coding and the other non-protein coding, have
            been found for this gene. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and is the protein-coding variant.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.876872.1,
                                           SRR1660807.172311.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251775.9/ ENSP00000251775.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.2"
     Protein         1..450
                     /product="sorting nexin-4"
                     /calculated_mol_wt=51778
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95219.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O95219.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95219.1)"
     Region          58..184
                     /region_name="PX_SNX4"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 4; cd06864"
                     /db_xref="CDD:132774"
     Site            order(106..108,132..133,154)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132774"
     Region          205..448
                     /region_name="BAR_SNX4"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 4; cd07622"
                     /db_xref="CDD:153306"
     Site            order(226,229..230,233..234,236..237,240,243..244,247,
                     254..255,257..258,261,264..265,268..269,282,408,411..412,
                     414..416,419,422..423,425..427,429..430,433..434,436..437,
                     440..441,443..444)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153306"
     CDS             1..450
                     /gene="SNX4"
                     /gene_synonym="ATG24B"
                     /coded_by="NM_003794.4:31..1383"
                     /db_xref="CCDS:CCDS3032.1"
                     /db_xref="GeneID:8723"
                     /db_xref="HGNC:HGNC:11175"
                     /db_xref="MIM:605931"
ORIGIN      
        1 meqappdper qlqpaplepl gspdaglgaa vgkeaegage essgvdtmth nnfwlkkiei
       61 svseaekrtg rnamnmqety taylietrsv ehtdgqsvlt dslwrrysef ellrsyllvy
      121 yphivvpplp ekraefvwhk lsadnmdpdf verrriglen fllriashpi lcrdkifylf
      181 ltqegnwket vnetgfqlka dsrlkalnat frvknpdkrf tdlkhysdel qsvishllrv
      241 rarvadrlyg vykvhgnygr vfsewsaiek emgdglqsag hhmdvyassi ddiledeehy
      301 adqlkeylfy aealravcrk helmqydlem aaqdlaskkq qceelvtgtv rtfslkgmtt
      361 klfgqetpeq rearikvlee qinegeqqlk sknlegrefv knawadierf keqknrdlke
      421 alisyavmqi smckkgiqvw tnakecfskm
//
LOCUS       NP_001352681             222 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 4 [Homo sapiens].
ACCESSION   NP_001352681 XP_005257590
VERSION     NP_001352681.1
DBSOURCE    REFSEQ: accession NM_001365752.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5.
            
            On Sep 12, 2018 this sequence version replaced XP_005257590.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (7), as well as variants 4 and
            8-10, encodes isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.117196.1,
                                           SRR3476690.1075218.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..222
                     /product="MIF4G domain-containing protein isoform 4"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=25292
     Region          8..179
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..222
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001365752.1:340..1008"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS56044.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqaeskqa gqsvfrrgll nrlqqeyqar eqlrarslqg wvcyvtficn ifdylrvnnm
      121 pmmalvnpvy dclfrlaqpd slskeeevdc lvlqlhrvge qlekmngqrm delfvlirdg
      181 fllptglssl aqlllleiie fraagwkttp aahkyyysev sd
//
LOCUS       NP_001338573             933 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            7 [Homo sapiens].
ACCESSION   NP_001338573 XP_006724498
VERSION     NP_001338573.1
DBSOURCE    REFSEQ: accession NM_001351644.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, AL954743.9,
            AL671545.13 and AL096767.14.
            
            On May 17, 2017 this sequence version replaced XP_006724498.1.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.103436.1,
                                           SRR1803615.141061.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..933
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 7"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=101186
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          <674..928
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..933
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001351644.2:372..3173"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlafsdyq
      541 iqqmtanfvd qfgfndeefa dqddninapf driaeinfni dadedspsaa lfeaccsdri
      601 qpfdddeded iwedsdtrca arvmarprfg aphasescsk ngperggqdg kasleahrda
      661 pgagappapg kkeappvegd seagamwtav fdepanstpt apgvvrdvgs svwaagtsap
      721 eekgwakftd fqpfccsesg prcsspvdte cshaegsrsq gpekafspas pcawnvcvtr
      781 kapllasdss ssggshsedg dqkaasamda vsrgpgreap plptvartee avgrvgcads
      841 rllspacpap kevtaapava vppeatvait talskagpai ptpavssala vavplgpima
      901 vtaapamvat lgtvtkdgkt dappegaaln gpv
//
LOCUS       NP_001095123             156 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 9 isoform 2 [Homo sapiens].
ACCESSION   NP_001095123
VERSION     NP_001095123.1
DBSOURCE    REFSEQ: accession NM_001101653.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087277.11.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. It encodes
            isoform 2, which is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.10329.1,
                                           SRR1660809.296971.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..156
                     /product="COMM domain-containing protein 9 isoform 2"
                     /note="COMM domain-containing protein 9"
                     /calculated_mol_wt=17202
     Region          48..155
                     /region_name="Commd9"
                     /note="COMM_Domain containing protein 9. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04757"
                     /db_xref="CDD:240105"
     CDS             1..156
                     /gene="COMMD9"
                     /gene_synonym="C11orf55; HSPC166; LINC00610"
                     /coded_by="NM_001101653.2:13..483"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44571.1"
                     /db_xref="GeneID:29099"
                     /db_xref="HGNC:HGNC:25014"
                     /db_xref="MIM:612299"
ORIGIN      
        1 maaltaehfa alqsllkllq alhrltrlva frdlssaeai lalfpenfhq nlknlltkii
       61 lehvstwrte aqanqislpr lvdldwrvdi ktssdsisrm avptcllqmk iqedpslcgd
      121 kpsisavtve lsketldtml dglgrirdql savask
//
LOCUS       NP_689597                341 aa            linear   PRI 20-NOV-2025
DEFINITION  BBSome complex member BBS5 [Homo sapiens].
ACCESSION   NP_689597 XP_944982 XP_949464 XP_949467 XP_949472
VERSION     NP_689597.1
DBSOURCE    REFSEQ: accession NM_152384.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Bentley-Ford,M.R., Engle,S.E., Clearman,K.R., Haycraft,C.J.,
            Andersen,R.S., Croyle,M.J., Rains,A.B., Berbari,N.F. and Yoder,B.K.
  TITLE     A mouse model of BBS identifies developmental and homeostatic
            effects of BBS5 mutation and identifies novel pituitary
            abnormalities
  JOURNAL   Hum Mol Genet 30 (3-4), 234-246 (2021)
   PUBMED   33560420
  REMARK    GeneRIF: A mouse model of BBS identifies developmental and
            homeostatic effects of BBS5 mutation and identifies novel pituitary
            abnormalities.
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Hey,C.A.B., Larsen,L.J., Tumer,Z., Brondum-Nielsen,K., Gronskov,K.,
            Hjortshoj,T.D. and Moller,L.B.
  TITLE     BBS Proteins Affect Ciliogenesis and Are Essential for Hedgehog
            Signaling, but Not for Formation of iPSC-Derived RPE-65 Expressing
            RPE-Like Cells
  JOURNAL   Int J Mol Sci 22 (3), 1345 (2021)
   PUBMED   33572860
  REMARK    GeneRIF: BBS Proteins Affect Ciliogenesis and Are Essential for
            Hedgehog Signaling, but Not for Formation of iPSC-Derived RPE-65
            Expressing RPE-Like Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Li,J.B., Gerdes,J.M., Haycraft,C.J., Fan,Y., Teslovich,T.M.,
            May-Simera,H., Li,H., Blacque,O.E., Li,L., Leitch,C.C., Lewis,R.A.,
            Green,J.S., Parfrey,P.S., Leroux,M.R., Davidson,W.S., Beales,P.L.,
            Guay-Woodford,L.M., Yoder,B.K., Stormo,G.D., Katsanis,N. and
            Dutcher,S.K.
  TITLE     Comparative genomics identifies a flagellar and basal body proteome
            that includes the BBS5 human disease gene
  JOURNAL   Cell 117 (4), 541-552 (2004)
   PUBMED   15137946
  REMARK    GeneRIF: identified BBS5, a novel gene for Bardet-Biedl syndrome;
            it localizes to basal bodies, is under the regulatory control of
            daf-19, and is necessary for the generation of both cilia and
            flagella
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Young,T.L., Penney,L., Woods,M.O., Parfrey,P.S., Green,J.S.,
            Hefferton,D. and Davidson,W.S.
  TITLE     A fifth locus for Bardet-Biedl syndrome maps to chromosome 2q31
  JOURNAL   Am J Hum Genet 64 (3), 900-904 (1999)
   PUBMED   10053027
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Woods,M.O., Young,T.L., Parfrey,P.S., Hefferton,D., Green,J.S. and
            Davidson,W.S.
  TITLE     Genetic heterogeneity of Bardet-Biedl syndrome in a distinct
            Canadian population: evidence for a fifth locus
  JOURNAL   Genomics 55 (1), 2-9 (1999)
   PUBMED   9888993
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093899.3, AY604003.1,
            BC044593.1, BP311042.1, AK097935.1, H09195.1, CD245392.1,
            AL834305.1, AA043704.1 and CA336791.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_944982.1, XP_949464.1, XP_949467.1, XP_949472.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is required for the formation of cilia.
            Alternate transcriptional splice variants have been observed but
            have not been fully characterized. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY604003.1, SRR1803613.43466.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295240.8/ ENSP00000295240.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..341
                     /product="BBSome complex member BBS5"
                     /note="bardet-Biedl syndrome 5 protein"
                     /calculated_mol_wt=38624
     Region          7..339
                     /region_name="BBL5"
                     /note="Bardet-Biedl syndrome 5 protein; pfam07289"
                     /db_xref="CDD:462136"
     CDS             1..341
                     /gene="BBS5"
                     /coded_by="NM_152384.3:61..1086"
                     /db_xref="CCDS:CCDS2233.1"
                     /db_xref="GeneID:129880"
                     /db_xref="HGNC:HGNC:970"
                     /db_xref="MIM:603650"
ORIGIN      
        1 msvldalwed rdvrfdlsaq qmktrpgevl idcldsiedt kgnngdrgrl lvtnlrilwh
       61 slalsrvnvs vgyncilnit trtansklrg qtealyiltk cnstrfefif tnlvpgsprl
      121 ftsvmavhra yetskmyrdf klrsaliqnk qlrllpqehv ydkingvwnl ssdqgnlgtf
      181 fitnvrivwh anmndsfnvs ipylqirsik irdskfglal viessqqsgg yvlgfkidpv
      241 eklqesvkei nslhkvysas pifgvdyeme ekpqplealt veqiqddvei dsdghtdafv
      301 ayfadgnkqq drepvfseel glaieklkdg ftlqglwevm s
//
LOCUS       NP_001340207             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340207
VERSION     NP_001340207.1
DBSOURCE    REFSEQ: accession NM_001353278.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.197270.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353278.1:644..1180"
                     /note="isoform 2 is encoded by transcript variant 40"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001350768             180 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 54 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001350768 XP_016884080
VERSION     NP_001350768.1
DBSOURCE    REFSEQ: accession NM_001363839.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Gustafsson,M.O., Mohammad,D.K., Ylosmaki,E., Choi,H., Shrestha,S.,
            Wang,Q., Nore,B.F., Saksela,K. and Smith,C.I.
  TITLE     ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from
            a Human Src-Homology 3 (SH3) domain library
  JOURNAL   PLoS One 12 (4), e0174909 (2017)
   PUBMED   28369144
  REMARK    GeneRIF: the results show that the interaction between BTK and
            ANKRD54 is highly selective, since it was also identified in a
            screen using human SH3-domainome. A novel finding is that BTK not
            only binds to ANKRD54, but stands out as the preferred interactor,
            being highly dominant over all other human SH3-domains.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Gustafsson,M.O., Hussain,A., Mohammad,D.K., Mohamed,A.J.,
            Nguyen,V., Metalnikov,P., Colwill,K., Pawson,T., Smith,C.I. and
            Nore,B.F.
  TITLE     Regulation of nucleocytoplasmic shuttling of Bruton's tyrosine
            kinase (Btk) through a novel SH3-dependent interaction with ankyrin
            repeat domain 54 (ANKRD54)
  JOURNAL   Mol Cell Biol 32 (13), 2440-2453 (2012)
   PUBMED   22527282
  REMARK    GeneRIF: Liar is the first protein identified that specifically
            influences the nucleocytoplasmic shuttling of Btk and Txk and
            belongs to a rare group of known proteins carrying out this
            activity in a Crm1-dependent manner.
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z97630.11, DB449700.1, R59897.1 and BX368923.2.
            
            On Jun 3, 2018 this sequence version replaced XP_016884080.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.203529.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..180
                     /product="ankyrin repeat domain-containing protein 54
                     isoform 3"
                     /note="ankyrin repeat domain-containing protein 54;
                     lyn-interacting ankyrin repeat protein"
                     /calculated_mol_wt=20025
     Region          <7..>96
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          22..53
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <34..180
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          55..86
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..180
                     /gene="ANKRD54"
                     /gene_synonym="LIAR"
                     /coded_by="NM_001363839.1:260..802"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS87023.1"
                     /db_xref="GeneID:129138"
                     /db_xref="HGNC:HGNC:25185"
                     /db_xref="MIM:613383"
ORIGIN      
        1 mpmmwkqqll edgadpcaad dkgrtalhfa scngndqivq llldhgadpn qrdglgntpl
       61 hlaactnhvp vittllrgga rvdaldragr tplhlakskl nilqeghaqc leavrlevkq
      121 iihmlreyle rlgqheqrer lddlctrlqm tstkeqvdev tdllasftsl slqmqsmekr
//
LOCUS       NP_113673                446 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate-rich WD repeat-containing protein 1 [Homo sapiens].
ACCESSION   NP_113673
VERSION     NP_113673.3
DBSOURCE    REFSEQ: accession NM_031485.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Gaibee,Z., Warner,N., Bugda Gwilt,K., Li,W., Guan,R., Yourshaw,M.,
            Whittaker Hawkins,R., Zorbas,C., St-Germain,J., Tabatabaie,M.,
            Mao,S., Pinsk,V., Yerushalmi,B., Wang,L.K., Nelson,S.F.,
            Wozniak,L., Shouval,D.S., Matar,M., Assa,A., Frost,N., Jimenez,L.,
            Acra,S., Walters,T., Mouat,S., Li,M., Lafontaine,D.L.J., Tyska,M.,
            Raught,B., Avitzur,Y., Lencer,W.I., Goldenring,J.R., Martin,M.G.,
            Thiagarajah,J.R. and Muise,A.M.
  TITLE     The Genetic Architecture of Congenital Diarrhea and Enteropathy
  JOURNAL   N Engl J Med 392 (13), 1297-1309 (2025)
   PUBMED   40174224
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wei,S., Lu,S., Liang,L., Wang,X., Li,W., Li,T., Chen,L., Ju,E.,
            Zhang,X., Lai,Z., Huang,Y., Lu,X. and Gao,S.J.
  TITLE     GRWD1-WDR5-MLL2 Epigenetic Complex Mediates H3K4me3 Mark and Is
            Essential for Kaposi's Sarcoma-Associated Herpesvirus-Induced
            Cellular Transformation
  JOURNAL   mBio 12 (6), e0343121 (2021)
   PUBMED   34933446
  REMARK    GeneRIF: GRWD1-WDR5-MLL2 Epigenetic Complex Mediates H3K4me3 Mark
            and Is Essential for Kaposi's Sarcoma-Associated
            Herpesvirus-Induced Cellular Transformation.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wu,Y., Wu,X., Li,Y., Zhao,W., Yue,Y., Wu,B., Liu,J., Chen,X. and
            Shen,A.
  TITLE     Comprehensive Analysis of Glutamate-Rich WD Repeat-Containing
            Protein 1 and Its Potential Clinical Significance for Pancancer
  JOURNAL   Biomed Res Int 2021, 8201377 (2021)
   PUBMED   34616846
  REMARK    GeneRIF: Comprehensive Analysis of Glutamate-Rich WD
            Repeat-Containing Protein 1 and Its Potential Clinical Significance
            for Pancancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Wang,Q., Ren,H., Xu,Y., Jiang,J., Wudu,M., Liu,Z., Su,H., Jiang,X.,
            Zhang,Y., Zhang,B. and Qiu,X.
  TITLE     GRWD1 promotes cell proliferation and migration in non-small cell
            lung cancer by activating the Notch pathway
  JOURNAL   Exp Cell Res 387 (2), 111806 (2020)
   PUBMED   31891681
  REMARK    GeneRIF: GRWD1 promotes cell proliferation and migration in
            non-small cell lung cancer by activating the Notch pathway.
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Fujiyama,H., Tsuji,T., Hironaka,K., Yoshida,K., Sugimoto,N. and
            Fujita,M.
  TITLE     GRWD1 directly interacts with p53 and negatively regulates p53
            transcriptional activity
  JOURNAL   J Biochem 167 (1), 15-24 (2020)
   PUBMED   31545368
  REMARK    GeneRIF: findings suggest a novel oncogenic function of GRWD1 as a
            transcriptional regulator of p53 and that GRWD1 might be an
            attractive therapeutic target and prognostic marker in cancer
            therapy
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Miotto,B. and Struhl,K.
  TITLE     HBO1 histone acetylase is a coactivator of the replication
            licensing factor Cdt1
  JOURNAL   Genes Dev 22 (19), 2633-2638 (2008)
   PUBMED   18832067
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Higa,L.A., Wu,M., Ye,T., Kobayashi,R., Sun,H. and Zhang,H.
  TITLE     CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
            proteins and regulates histone methylation
  JOURNAL   Nat Cell Biol 8 (11), 1277-1283 (2006)
   PUBMED   17041588
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Gratenstein,K., Heggestad,A.D., Fortun,J., Notterpek,L.,
            Pestov,D.G. and Fletcher,B.S.
  TITLE     The WD-repeat protein GRWD1: potential roles in myeloid
            differentiation and ribosome biogenesis
  JOURNAL   Genomics 85 (6), 762-773 (2005)
   PUBMED   15885502
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Killian,A., Le Meur,N., Sesboue,R., Bourguignon,J., Bougeard,G.,
            Gautherot,J., Bastard,C., Frebourg,T. and Flaman,J.M.
  TITLE     Inactivation of the RRB1-Pescadillo pathway involved in ribosome
            biogenesis induces chromosomal instability
  JOURNAL   Oncogene 23 (53), 8597-8602 (2004)
   PUBMED   15467761
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Trzcinska,A.M., Girstun,A., Piekielko,A., Kowalska-Loth,B. and
            Staron,K.
  TITLE     Potential protein partners for the N-terminal domain of human
            topoisomerase I revealed by phage display
  JOURNAL   Mol Biol Rep 29 (4), 347-352 (2002)
   PUBMED   12549820
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA714522.1, BC002440.2 and
            AC008403.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 20, 2009 this sequence version replaced NP_113673.2.
            
            Summary: This gene encodes a glutamate-rich protein that contains
            five WD-repeat motifs. The encoded protein may play a critical role
            in ribosome biogenesis and may also play a role in histone
            methylation through interactions with CUL4-DDB1 ubiquitin E3
            ligase. [provided by RefSeq, Feb 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.202012.1,
                                           SRR1803617.274724.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253237.10/ ENSP00000253237.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..446
                     /product="glutamate-rich WD repeat-containing protein 1"
                     /note="WD repeat domain 28; regulator of ribosome
                     biogenesis 1 homolog; glutamate rich WD repeat protein
                     GRWD; CUL4- and DDB1-associated WDR protein 4"
                     /calculated_mol_wt=49288
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          44..112
                     /region_name="CAF1C_H4-bd"
                     /note="Histone-binding protein RBBP4 or subunit C of CAF1
                     complex; pfam12265"
                     /db_xref="CDD:463513"
     Region          54..110
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          110..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          163..204
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          204..>384
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          205..250
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          218..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          251..297
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          265..306
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          298..343
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          311..350
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          344..405
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BQ67.1)"
     Region          406..442
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ67.1)"
     CDS             1..446
                     /gene="GRWD1"
                     /gene_synonym="CDW4; DIAR14; GRWD; RRB1; WDR28"
                     /coded_by="NM_031485.4:24..1364"
                     /db_xref="CCDS:CCDS12720.1"
                     /db_xref="GeneID:83743"
                     /db_xref="HGNC:HGNC:21270"
                     /db_xref="MIM:610597"
ORIGIN      
        1 maarkgrrrt cetgepmeae sgdtssegpa qvylpgrgpp lregeelvmd eeayvlyhra
       61 qtgapclsfd ivrdhlgdnr telpltlylc agtqaesaqs nrlmmlrmhn lhgtkpppse
      121 gsdeeeeeed eedeeerkpq lelamvphyg ginrvrvswl geepvagvws ekgqvevfal
      181 rrllqvveep qalaaflrde qaqmkpifsf aghmgegfal dwsprvtgrl ltgdcqknih
      241 lwtptdggsw hvdqrpfvgh trsvedlqws ptentvfasc sadasiriwd iraapskacm
      301 lttatahdgd vnviswsrre pfllsggddg alkiwdlrqf ksgspvatfk qhvapvtsve
      361 whpqdsgvfa asgadhqitq wdlaverdpe agdveadpgl adlpqqllfv hqgetelkel
      421 hwhpqcpgll vstalsgfti frtisv
//
LOCUS       NP_057508                432 aa            linear   PRI 20-NOV-2025
DEFINITION  luc7-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_057508
VERSION     NP_057508.2
DBSOURCE    REFSEQ: accession NM_016424.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Daniels,N.J., Hershberger,C.E., Gu,X., Schueger,C.,
            DiPasquale,W.M., Brick,J., Saunthararajah,Y., Maciejewski,J.P. and
            Padgett,R.A.
  TITLE     Functional analyses of human LUC7-like proteins involved in
            splicing regulation and myeloid neoplasms
  JOURNAL   Cell Rep 35 (2), 108989 (2021)
   PUBMED   33852859
  REMARK    GeneRIF: Functional analyses of human LUC7-like proteins involved
            in splicing regulation and myeloid neoplasms.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Szlavicz,E., Olah,P., Szabo,K., Pagani,F., Bata-Csorgo,Z.,
            Kemeny,L. and Szell,M.
  TITLE     Analysis of psoriasis-relevant gene expression and exon usage
            alterations after silencing of SR-rich splicing regulators
  JOURNAL   Exp Dermatol 27 (6), 656-662 (2018)
   PUBMED   29512856
  REMARK    GeneRIF: In our present RNA-Seq experiment, we demonstrated that
            the LUC7L3 and SFRS18 splicing factors contribute to the regulation
            of several well-known psoriasis-associated pathways, including the
            IFN signalling pathway, antiviral immunity and ubiquitination.
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Szlavicz,E., Szabo,K., Groma,G., Bata-Csorgo,Z., Pagani,F.,
            Kemeny,L. and Szell,M.
  TITLE     Splicing factors differentially expressed in psoriasis alter mRNA
            maturation of disease-associated EDA+ fibronectin
  JOURNAL   Mol Cell Biochem 436 (1-2), 189-199 (2017)
   PUBMED   28589370
  REMARK    GeneRIF: results indicate that LUC7L3, PPIG, and SFRS18 are not
            only implicated in EDA+ fibronectin formation, but also that they
            could possess multiple roles in psoriasis-associated molecular
            abnormalities.
            Erratum:[Mol Cell Biochem. 2017 Dec;436(1-2):201. doi:
            10.1007/s11010-017-3105-y. PMID: 28770468]
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Umehara,H., Nishii,Y., Morishima,M., Kakehi,Y., Kioka,N.,
            Amachi,T., Koizumi,J., Hagiwara,M. and Ueda,K.
  TITLE     Effect of cisplatin treatment on speckled distribution of a
            serine/arginine-rich nuclear protein CROP/Luc7A
  JOURNAL   Biochem Biophys Res Commun 301 (2), 324-329 (2003)
   PUBMED   12565863
  REMARK    GeneRIF: These results suggest that cisplatin affects RNA splicing
            by changing the subnuclear distribution of proteins including
            cisplatin resistance-associated overexpressed protein (CROP).
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Chin,L.S., Singh,S.K., Wang,Q. and Murray,S.F.
  TITLE     Identification of okadaic-acid-induced genes by mRNA differential
            display in glioma cells
  JOURNAL   J Biomed Sci 7 (2), 152-159 (2000)
   PUBMED   10754390
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Nishii,Y., Morishima,M., Kakehi,Y., Umehara,K., Kioka,N.,
            Terano,Y., Amachi,T. and Ueda,K.
  TITLE     CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated
            from cisplatin-resistant cell line
  JOURNAL   FEBS Lett 465 (2-3), 153-156 (2000)
   PUBMED   10631324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA231851.1, BC047043.1,
            AK290540.1, AC005921.3 and CN271700.1.
            
            On Apr 4, 2002 this sequence version replaced NP_057508.1.
            
            Summary: This gene encodes a protein with an N-terminal half that
            contains cysteine/histidine motifs and leucine zipper-like repeats,
            and the C-terminal half is rich in arginine and glutamate residues
            (RE domain) and arginine and serine residues (RS domain). This
            protein localizes with a speckled pattern in the nucleus, and could
            be involved in the formation of splicesome via the RE and RS
            domains. Two alternatively spliced transcript variants encoding the
            same protein have been found for this gene. [provided by RefSeq,
            Aug 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.95361.1,
                                           SRR1660803.103232.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000505658.6/ ENSP00000425092.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..432
                     /product="luc7-like protein 3 isoform 1"
                     /note="LUC7-like 3; luc7-like protein 3; CRE-associated
                     protein 1; cAMP regulatory element-associated protein 1;
                     okadaic acid-inducible phosphoprotein OA48-18; cisplatin
                     resistance-associated-overexpressed protein"
                     /calculated_mol_wt=51335
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Region          4..246
                     /region_name="LUC7"
                     /note="LUC7 N_terminus; pfam03194"
                     /db_xref="CDD:460842"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            231
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Region          234..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95232.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O95232.2)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95232.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95232.2)"
     CDS             1..432
                     /gene="LUC7L3"
                     /gene_synonym="CRA; CREAP-1; CROP; hLuc7A; LUC7A; OA48-18"
                     /coded_by="NM_016424.5:131..1429"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11573.1"
                     /db_xref="GeneID:51747"
                     /db_xref="HGNC:HGNC:24309"
                     /db_xref="MIM:609434"
ORIGIN      
        1 misaaqllde lmgrdrnlap dekrsnvrwd hesvckyylc gfcpaelftn trsdlgpcek
       61 ihdenlrkqy ekssrfmkvg yerdflrylq sllaeverri rrgharlals qnqqssgaag
      121 ptgkneekiq vltdkidvll qqieelgseg kveeaqgmmk lveqlkeere llrsttstie
      181 sfaaqekqme vcevcgafli vgdaqsrvdd hlmgkqhmgy akikatveel keklrkrtee
      241 pdrderlkke kqereereke rerereerer krrreeeere kerardrerr krsrsrsrhs
      301 srtsdrrcsr srdhkrsrsr errrsrsrdr rrsrshdrse rkhrsrsrdr rrsksrdrks
      361 ykhrsksrdr eqdrkskeke krgsddkkss vksgsrekqs edtnteskes dtknevngts
      421 ediksegdtq sn
//
LOCUS       NP_001316485             211 aa            linear   PRI 20-NOV-2025
DEFINITION  receptor expression-enhancing protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001316485
VERSION     NP_001316485.1
DBSOURCE    REFSEQ: accession NM_001329556.3
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Zhang,L., Li,Y., Qin,L., Wu,Y. and Lei,B.
  TITLE     Autosomal Recessive Retinitis Pigmentosa Associated with Three
            Novel REEP6 Variants in Chinese Population
  JOURNAL   Genes (Basel) 12 (4), 537 (2021)
   PUBMED   33917198
  REMARK    GeneRIF: Autosomal Recessive Retinitis Pigmentosa Associated with
            Three Novel REEP6 Variants in Chinese Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Wellmann,A., Fogt,F., Hollerbach,S., Hahne,J., Koenig-Hoffmann,K.,
            Smeets,D. and Brinkmann,U.
  TITLE     Polymorphisms of the apoptosis-associated gene DP1L1 (deleted in
            polyposis 1-like 1) in colon cancer and inflammatory bowel disease
  JOURNAL   J Cancer Res Clin Oncol 136 (6), 795-802 (2010)
   PUBMED   19924442
  REMARK    GeneRIF: DP1L1 polymorphisms are associated with colon cancer and
            IBD. This indicates that DP1L1 plays a functional role in these
            conditions. Thus DP1L1 may be a diagnostic and therapeutic target
            for colon cancer and IBD.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Saito,H., Kubota,M., Roberts,R.W., Chi,Q. and Matsunami,H.
  TITLE     RTP family members induce functional expression of mammalian
            odorant receptors
  JOURNAL   Cell 119 (5), 679-691 (2004)
   PUBMED   15550249
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008201.1, BQ640333.1 and
            BU728980.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene may be involved in the
            transport of receptors from the endoplasmic reticulum (ER) to the
            cell surface. The encoded protein may also play a role in
            regulating ER membrane structure. This gene is required for the
            proper development of retinal rods and photoreceptors, with defects
            in this gene being associated with retinitis pigmentosa 77.
            [provided by RefSeq, May 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.585107.1,
                                           SRR3476690.489367.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000395479.10/ ENSP00000378861.5
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..211
                     /product="receptor expression-enhancing protein 6 isoform
                     1"
                     /note="deleted in polyposis 1-like 1; polyposis locus
                     protein 1-like 1; receptor expression-enhancing protein 6"
                     /calculated_mol_wt=23287
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HR9.2)"
     Region          66..143
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HR9.2)"
     Region          190..211
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HR9.2)"
     CDS             1..211
                     /gene="REEP6"
                     /gene_synonym="C19orf32; DP1L1; REEP6.1; REEP6.2; RP77;
                     TB1; TB2L1; Yip2f"
                     /coded_by="NM_001329556.3:90..725"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS92481.1"
                     /db_xref="GeneID:92840"
                     /db_xref="HGNC:HGNC:30078"
                     /db_xref="MIM:609346"
ORIGIN      
        1 mdglrqrveh fleqrnlvte vlgaleaktg vekrylaaga vtllslyllf gygasllcnl
       61 igfvypayas ikaiespskd ddtvwltywv vyalfglaef fsdlllswfp fyyvgkcafl
      121 lfcmaprpwn galmlyqrvv rplflrhhga vdrimndlsg raldaaagit rnvlqvlars
      181 ragitpvava gpstpleadl kpsqtpqpkd k
//
LOCUS       NP_001315566              90 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein E isoform 3 [Homo sapiens].
ACCESSION   NP_001315566
VERSION     NP_001315566.1
DBSOURCE    REFSEQ: accession NM_001328637.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 90)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 90)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 90)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 90)
  AUTHORS   Wu,Q., Liao,R., Miao,C., Hasnat,M., Li,L., Sun,L., Wang,X.,
            Yuan,Z., Jiang,Z., Zhang,L. and Yu,Q.
  TITLE     Oncofetal SNRPE promotes HCC tumorigenesis by regulating the FGFR4
            expression through alternative splicing
  JOURNAL   Br J Cancer 131 (1), 77-89 (2024)
   PUBMED   38796598
  REMARK    GeneRIF: Oncofetal SNRPE promotes HCC tumorigenesis by regulating
            the FGFR4 expression through alternative splicing.
REFERENCE   5  (residues 1 to 90)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 90)
  AUTHORS   Fautsch,M.P. and Wieben,E.D.
  TITLE     Transcriptional regulation of the small nuclear ribonucleoprotein E
            protein gene. Identification of cis-acting sequences with homology
            to genes encoding ribosomal proteins
  JOURNAL   J Biol Chem 266 (34), 23288-23295 (1991)
   PUBMED   1835977
REFERENCE   7  (residues 1 to 90)
  AUTHORS   Neiswanger,K., Stanford,D.R., Sparkes,R.S., Nishimura,D.,
            Mohandas,T., Klisak,I., Heinzmann,C. and Wieben,E.D.
  TITLE     Assignment of the gene for the small nuclear ribonucleoprotein E
            (SNRPE) to human chromosome 1q25-q43
  JOURNAL   Genomics 7 (4), 503-508 (1990)
   PUBMED   2143747
REFERENCE   8  (residues 1 to 90)
  AUTHORS   Sauterer,R.A., Goyal,A. and Zieve,G.W.
  TITLE     Cytoplasmic assembly of small nuclear ribonucleoprotein particles
            from 6 S and 20 S RNA-free intermediates in L929 mouse fibroblasts
  JOURNAL   J Biol Chem 265 (2), 1048-1058 (1990)
   PUBMED   1688550
REFERENCE   9  (residues 1 to 90)
  AUTHORS   Feeney,R.J., Sauterer,R.A., Feeney,J.L. and Zieve,G.W.
  TITLE     Cytoplasmic assembly and nuclear accumulation of mature small
            nuclear ribonucleoprotein particles
  JOURNAL   J Biol Chem 264 (10), 5776-5783 (1989)
   PUBMED   2522439
REFERENCE   10 (residues 1 to 90)
  AUTHORS   Stanford,D.R., Rohleder,A., Neiswanger,K. and Wieben,E.D.
  TITLE     DNA sequence of a human Sm autoimmune antigen. The multigene family
            contains a processed pseudogene
  JOURNAL   J Biol Chem 262 (21), 9931-9934 (1987)
   PUBMED   2440864
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114402.2 and AC118554.2.
            
            Summary: The protein encoded by this gene is a core component of U
            small nuclear ribonucleoproteins, which are key components of the
            pre-mRNA processing spliceosome. The encoded protein plays a role
            in the 3' end processing of histone transcripts. This protein is
            one of the targets in the autoimmune disease systemic lupus
            erythematosus, and mutations in this gene have been associated with
            hypotrichosis. Several pseudogenes of this gene have been
            identified. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14243140.7227926.1,
                                           SRR18074967.2403215.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..90
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..90
                     /product="small nuclear ribonucleoprotein E isoform 3"
                     /note="sm protein E"
                     /calculated_mol_wt=10231
     Region          17..87
                     /region_name="Sm_E"
                     /note="Sm protein E; cd01718"
                     /db_xref="CDD:212465"
     Site            order(22,34,36,39,46..49,53,61,70,72,74..78,81..87)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212465"
     Site            order(31..37,39..51,53..57)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212465"
     Site            order(49,51..53,78,80)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212465"
     Site            74..85
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212465"
     CDS             1..90
                     /gene="SNRPE"
                     /gene_synonym="HYPT11; Sm-E; SME; snRNP-E"
                     /coded_by="NM_001328637.2:76..348"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:6635"
                     /db_xref="HGNC:HGNC:11161"
                     /db_xref="MIM:128260"
ORIGIN      
        1 mdaakggkrt satvvqnlif rylqnrsriq vwlyeqvnmr iegciigfde ymnlvlddae
       61 eihsktksrk qlgrimlkgd nitllqsvsn
//
LOCUS       NP_001258882             231 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin polyglutamylase complex subunit 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001258882
VERSION     NP_001258882.1
DBSOURCE    REFSEQ: accession NM_001271953.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Ruse,C.I., Chin,H.G. and Pradhan,S.
  TITLE     Polyglutamylation: biology and analysis
  JOURNAL   Amino Acids 54 (4), 529-542 (2022)
   PUBMED   35357568
  REMARK    Review article
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Wang,L., Paudyal,S.C., Kang,Y., Owa,M., Liang,F.X., Spektor,A.,
            Knaut,H., Sanchez,I. and Dynlacht,B.D.
  TITLE     Regulators of tubulin polyglutamylation control nuclear shape and
            cilium disassembly by balancing microtubule and actin assembly
  JOURNAL   Cell Res 32 (2), 190-209 (2022)
   PUBMED   34782749
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Shaffer,J.R., Polk,D.E., Wang,X., Feingold,E., Weeks,D.E.,
            Lee,M.K., Cuenco,K.T., Weyant,R.J., Crout,R.J., McNeil,D.W. and
            Marazita,M.L.
  TITLE     Genome-wide association study of periodontal health measured by
            probing depth in adults ages 18-49 years
  JOURNAL   G3 (Bethesda) 4 (2), 307-314 (2014)
   PUBMED   24347629
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Janke,C., Rogowski,K., Wloga,D., Regnard,C., Kajava,A.V.,
            Strub,J.M., Temurak,N., van Dijk,J., Boucher,D., van Dorsselaer,A.,
            Suryavanshi,S., Gaertig,J. and Edde,B.
  TITLE     Tubulin polyglutamylase enzymes are members of the TTL domain
            protein family
  JOURNAL   Science 308 (5729), 1758-1762 (2005)
   PUBMED   15890843
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Kitazawa,H., Iida,J., Uchida,A., Haino-Fukushima,K., Itoh,T.J.,
            Hotani,H., Ookata,K., Murofushi,H., Bulinski,J.C., Kishimoto,T. and
            Hisanaga,S.
  TITLE     Ser787 in the proline-rich region of human MAP4 is a critical
            phosphorylation site that reduces its activity to promote tubulin
            polymerization
  JOURNAL   Cell Struct Funct 25 (1), 33-39 (2000)
   PUBMED   10791892
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009854.9, BU543495.1,
            AC090333.5, AA677381.1 and CA425930.1.
            
            Summary: This gene encodes a protein that is a component of the
            neuronal polyglutamylase complex, which plays a role in
            post-translational addition of glutamate residues to C-terminal
            tubulin tails. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Dec 2012].
            
            Transcript Variant: This variant (6) contains an alternate 3'
            terminal exon compared to variant 1. It encodes isoform 6 which has
            a distinct C-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.243026.1,
                                           SRR1163657.463508.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..231
                     /product="tubulin polyglutamylase complex subunit 2
                     isoform 6"
                     /note="polyglutamylase subunit 2"
                     /calculated_mol_wt=25733
     Region          44..192
                     /region_name="SMI1_KNR4"
                     /note="SMI1 / KNR4 family; smart00860"
                     /db_xref="CDD:214864"
     CDS             1..231
                     /gene="TPGS2"
                     /gene_synonym="C18orf10; HMFN0601; L17; PGs2"
                     /coded_by="NM_001271953.2:236..931"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:25941"
                     /db_xref="HGNC:HGNC:24561"
                     /db_xref="MIM:620710"
ORIGIN      
        1 meeeasspgl gcskphlekl tlgitriles spgvtevtii ekppaerhmi ssweqknncv
       61 mpedvknfyl mtngfhmtws vkldehiipl gsmainsisk ltqltqssmy slpnaptlad
      121 leddtheasd dqpekphfds rsvifeldsc ngsgkvclvy ksgkpalaed teiwfldral
      181 ywhfltdtft ayyrllithl glpqwqyaft sygispqaka wglatskesa a
//
LOCUS       NP_954856                478 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-1 isoform 3
            [Homo sapiens].
ACCESSION   NP_954856
VERSION     NP_954856.1
DBSOURCE    REFSEQ: accession NM_199248.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Despang,P., Salamon,S., Breitenkamp,A., Kuzmenkina,E. and
            Matthes,J.
  TITLE     Inhibitory effects on L- and N-type calcium channels by a novel
            CaVbeta1 variant identified in a patient with autism spectrum
            disorder
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 395 (4), 459-470 (2022)
   PUBMED   35122502
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Perez,C.F., Eltit,J.M., Lopez,J.R., Bodnar,D., Dulhunty,A.F.,
            Aditya,S. and Casarotto,M.G.
  TITLE     Functional and structural characterization of a novel malignant
            hyperthermia-susceptible variant of DHPR-beta1a subunit (CACNB1)
  JOURNAL   Am J Physiol Cell Physiol 314 (3), C323-C333 (2018)
   PUBMED   29212769
  REMARK    GeneRIF: Data show that mutant variant V156A results in instability
            of protein subdomains of beta1a subunit leading to a phenotype of
            Ca(2+) dysregulation that partly resembles that of other malignant
            hypertension-linked mutations of DHPR alpha1S subunit.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Dolphin,A.C.
  TITLE     Voltage-gated calcium channels and their auxiliary subunits:
            physiology and pathophysiology and pharmacology
  JOURNAL   J Physiol 594 (19), 5369-5390 (2016)
   PUBMED   27273705
  REMARK    Review article
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Collin,T., Wang,J.J., Nargeot,J. and Schwartz,A.
  TITLE     Molecular cloning of three isoforms of the L-type voltage-dependent
            calcium channel beta subunit from normal human heart
  JOURNAL   Circ Res 72 (6), 1337-1344 (1993)
   PUBMED   7916667
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Powers,P.A., Liu,S., Hogan,K. and Gregg,R.G.
  TITLE     Skeletal muscle and brain isoforms of a beta-subunit of human
            voltage-dependent calcium channels are encoded by a single gene
  JOURNAL   J Biol Chem 267 (32), 22967-22972 (1992)
   PUBMED   1385409
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Perez-Reyes,E., Castellano,A., Kim,H.S., Bertrand,P., Baggstrom,E.,
            Lacerda,A.E., Wei,X.Y. and Birnbaumer,L.
  TITLE     Cloning and expression of a cardiac/brain beta subunit of the
            L-type calcium channel
  JOURNAL   J Biol Chem 267 (3), 1792-1797 (1992)
   PUBMED   1370480
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Pragnell,M., Sakamoto,J., Jay,S.D. and Campbell,K.P.
  TITLE     Cloning and tissue-specific expression of the brain calcium channel
            beta-subunit
  JOURNAL   FEBS Lett 291 (2), 253-258 (1991)
   PUBMED   1657644
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP217857.1, M92302.1 and
            M76560.1.
            
            Summary: The protein encoded by this gene belongs to the calcium
            channel beta subunit family. It plays an important role in the
            calcium channel by modulating G protein inhibition, increasing peak
            calcium current, controlling the alpha-1 subunit membrane targeting
            and shifting the voltage dependence of activation and inactivation.
            Alternative splicing occurs at this locus and three transcript
            variants encoding three distinct isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3), also known as beta-1b1,
            betaB, and beta-1c, differs in the 3' UTR and 3' coding region,
            compared to variant 1. It encodes isoform 3 which is shorter and
            has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M76560.1, M92302.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..478
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-1 isoform 3"
                     /note="dihydropyridine-sensitive L-type, calcium channel
                     beta-1 subunit; calcium channel, voltage-dependent, beta 1
                     subunit; calcium channel, L type, beta 1 polypeptide;
                     voltage-dependent L-type calcium channel subunit beta-1;
                     calcium channel voltage-dependent subunit beta 1"
                     /calculated_mol_wt=52875
     Region          1..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02641.3)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54283; propagated from
                     UniProtKB/Swiss-Prot (Q02641.3)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54283; propagated from
                     UniProtKB/Swiss-Prot (Q02641.3)"
     Region          58..99
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54283; propagated from
                     UniProtKB/Swiss-Prot (Q02641.3)"
     Region          99..166
                     /region_name="SH3_CACNB1"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta-1; cd12041"
                     /db_xref="CDD:212974"
     Site            order(109,111,114,125,143..144,160,162..163)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212974"
     Region          179..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02641.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3Z5; propagated from
                     UniProtKB/Swiss-Prot (Q02641.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54283; propagated from
                     UniProtKB/Swiss-Prot (Q02641.3)"
     Region          228..408
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..478
                     /gene="CACNB1"
                     /gene_synonym="CAB1; CACNLB1; CCHLB1"
                     /coded_by="NM_199248.3:175..1611"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45665.1"
                     /db_xref="GeneID:782"
                     /db_xref="HGNC:HGNC:1401"
                     /db_xref="MIM:114207"
ORIGIN      
        1 mvqktsmsrg pyppsqeipm evfdpspqgk yskrkgrfkr sdgstssdtt snsfvrqgsa
       61 esytsrpsds dvsleedrea lrkeaerqal aqlekaktkp vafavrtnvg ynpspgdevp
      121 vqgvaitfep kdflhikeky nndwwigrlv kegcevgfip spvkldslrl lqeqklrqnr
      181 lgssksgdns ssslgdvvtg trrptppasa kqkqkstehv ppydvvpsmr piilvgpslk
      241 gyevtdmmqk alfdflkhrf dgrisitrvt adislakrsv lnnpskhiii ersntrssla
      301 evqseierif elartlqlva ldadtinhpa qlsktslapi ivyikitspk vlqrliksrg
      361 ksqskhlnvq iaaseklaqc ppemfdiild enqledaceh laeyleaywk athppsstpp
      421 npllnrtmat aalaaspapv snlqvqvlts lrrnlgfwgg lessqrgsvv pqeqeham
//
LOCUS       NP_004521                660 aa            linear   PRI 20-NOV-2025
DEFINITION  72 kDa type IV collagenase isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_004521
VERSION     NP_004521.1
DBSOURCE    REFSEQ: accession NM_004530.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Hung,C.C., Tsai,C.L., Chin,Y.T., Wang,Y.C., Liu,C.H., Lin,M.L.,
            Chen,S.S., He,J.L., Tsai,C.W., Su,C.H., Bau,D.T. and Chang,W.S.
  TITLE     Impacts of Matrix Metalloproteinase-2 Promoter Genotypes on Breast
            Cancer Risk
  JOURNAL   Cancer Genomics Proteomics 21 (5), 502-510 (2024)
   PUBMED   39191502
  REMARK    GeneRIF: Impacts of Matrix Metalloproteinase-2 Promoter Genotypes
            on Breast Cancer Risk.
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liang,S., Li,L., Guo,Z., Sun,H. and Yang,Y.
  TITLE     Co-expression of CD44v6 and MMP2 predicts lung metastasis and
            unfavorable prognosis in osteosarcoma
  JOURNAL   Future Oncol 20 (25), 1799-1806 (2024)
   PUBMED   39011948
  REMARK    GeneRIF: Co-expression of CD44v6 and MMP2 predicts lung metastasis
            and unfavorable prognosis in osteosarcoma.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   DeCoux,A., Lindsey,M.L., Villarreal,F., Garcia,R.A. and Schulz,R.
  TITLE     Myocardial matrix metalloproteinase-2: inside out and upside down
  JOURNAL   J Mol Cell Cardiol 77, 64-72 (2014)
   PUBMED   25261607
  REMARK    GeneRIF: The roles of MMP-2 in cardiac injury and repair. [Review]
            Review article
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Verslegers,M., Lemmens,K., Van Hove,I. and Moons,L.
  TITLE     Matrix metalloproteinase-2 and -9 as promising benefactors in
            development, plasticity and repair of the nervous system
  JOURNAL   Prog Neurobiol 105, 60-78 (2013)
   PUBMED   23567503
  REMARK    Review article
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Nagase,H., Visse,R. and Murphy,G.
  TITLE     Structure and function of matrix metalloproteinases and TIMPs
  JOURNAL   Cardiovasc Res 69 (3), 562-573 (2006)
   PUBMED   16405877
  REMARK    Review article
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Bhavani,G.S., Shah,H., Shukla,A. and Girisha,K.M.
  TITLE     Multicentric Osteolysis Nodulosis and Arthropathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413800
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Devarajan,P., Johnston,J.J., Ginsberg,S.S., Van Wart,H.E. and
            Berliner,N.
  TITLE     Structure and expression of neutrophil gelatinase cDNA. Identity
            with type IV collagenase from HT1080 cells
  JOURNAL   J Biol Chem 267 (35), 25228-25232 (1992)
   PUBMED   1460022
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Levy,A.T., Cioce,V., Sobel,M.E., Garbisa,S., Grigioni,W.F.,
            Liotta,L.A. and Stetler-Stevenson,W.G.
  TITLE     Increased expression of the Mr 72,000 type IV collagenase in human
            colonic adenocarcinoma
  JOURNAL   Cancer Res 51 (1), 439-444 (1991)
   PUBMED   1846313
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Huhtala,P., Chow,L.T. and Tryggvason,K.
  TITLE     Structure of the human type IV collagenase gene
  JOURNAL   J Biol Chem 265 (19), 11077-11082 (1990)
   PUBMED   2162831
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP341649.1, AK312711.1,
            AC007336.6, BX357054.2 and BQ004983.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the matrix metalloproteinase
            (MMP) gene family, that are zinc-dependent enzymes capable of
            cleaving components of the extracellular matrix and molecules
            involved in signal transduction. The protein encoded by this gene
            is a gelatinase A, type IV collagenase, that contains three
            fibronectin type II repeats in its catalytic site that allow
            binding of denatured type IV and V collagen and elastin. Unlike
            most MMP family members, activation of this protein can occur on
            the cell membrane. This enzyme can be activated extracellularly by
            proteases, or, intracellulary by its S-glutathiolation with no
            requirement for proteolytical removal of the pro-domain. This
            protein is thought to be involved in multiple pathways including
            roles in the nervous system, endometrial menstrual breakdown,
            regulation of vascularization, and metastasis. Mutations in this
            gene have been associated with Winchester syndrome and
            Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002576.2, SRR1803614.166162.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219070.9/ ENSP00000219070.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..660
                     /product="72 kDa type IV collagenase isoform 1
                     preproprotein"
                     /EC_number="3.4.24.24"
                     /note="neutrophil gelatinase; matrix metalloproteinase-II;
                     collagenase type IV-A; matrix metallopeptidase 2
                     (gelatinase A, 72kDa gelatinase, 72kDa type IV
                     collagenase); matrix metalloproteinase-2"
                     /calculated_mol_wt=70976
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2925
     Region          <70..97
                     /region_name="PG_binding_1"
                     /note="Putative peptidoglycan binding domain; pfam01471"
                     /db_xref="CDD:460223"
     Region          100..107
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
     mat_peptide     110..660
                     /product="72 kDa type IV collagenase. /id=PRO_0000028715"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
                     /calculated_mol_wt=62060
     Region          110..221
                     /region_name="Collagenase-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
     Region          118..446
                     /region_name="Peptidase_M10"
                     /note="Matrixin; pfam00413"
                     /db_xref="CDD:425668"
     Region          222..396
                     /region_name="Collagen-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
     Region          226..274
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(237,239,244,258,265,271,273)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          284..332
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(295,297,302,316,323,329,331)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          342..390
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(353,355,360,374,381,387,389)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          397..465
                     /region_name="Collagenase-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
     Region          414..660
                     /region_name="Required for inhibitor TIMP2 binding.
                     /evidence=ECO:0000269|PubMed:1655733"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
     mat_peptide     445..660
                     /product="PEX. /id=PRO_0000391626"
                     /note="propagated from UniProtKB/Swiss-Prot (P08253.2)"
                     /calculated_mol_wt=24390
     Region          466..660
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Site            order(476,478,521,523,569,571,618,620)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     Site            573
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08253.2)"
     Site            642
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P08253.2)"
     CDS             1..660
                     /gene="MMP2"
                     /gene_synonym="CLG4; CLG4A; MMP-2; MMP-II; MONA; TBE-1"
                     /coded_by="NM_004530.6:283..2265"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10752.1"
                     /db_xref="GeneID:4313"
                     /db_xref="HGNC:HGNC:7166"
                     /db_xref="MIM:120360"
ORIGIN      
        1 mealmargal tgplralcll gcllshaaaa pspiikfpgd vapktdkela vqylntfygc
       61 pkescnlfvl kdtlkkmqkf fglpqtgdld qntietmrkp rcgnpdvany nffprkpkwd
      121 knqityriig ytpdldpetv ddafarafqv wsdvtplrfs rihdgeadim infgrwehgd
      181 gypfdgkdgl lahafapgtg vggdshfddd elwtlgegqv vrvkygnadg eyckfpflfn
      241 gkeynsctdt grsdgflwcs ttynfekdgk ygfcphealf tmggnaegqp ckfpfrfqgt
      301 sydscttegr tdgyrwcgtt edydrdkkyg fcpetamstv ggnsegapcv fpftflgnky
      361 esctsagrsd gkmwcattan ydddrkwgfc pdqgyslflv aahefghamg lehsqdpgal
      421 mapiytytkn frlsqddikg iqelygaspd idlgtgptpt lgpvtpeick qdivfdgiaq
      481 irgeifffkd rfiwrtvtpr dkpmgpllva tfwpelpeki davyeapqee kavffagney
      541 wiysastler gypkpltslg lppdvqrvda afnwsknkkt yifagdkfwr ynevkkkmdp
      601 gfpkliadaw naipdnldav vdlqggghsy ffkgayylkl enqslksvkf gsiksdwlgc
//
LOCUS       NP_001334876             366 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 81 homolog isoform 3 [Homo
            sapiens].
ACCESSION   NP_001334876
VERSION     NP_001334876.1
DBSOURCE    REFSEQ: accession NM_001347947.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Zhou,Z., Qiu,H., Castro-Araya,R.F., Takei,R., Nakayama,K. and
            Katoh,Y.
  TITLE     Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome
  JOURNAL   Hum Mol Genet 31 (10), 1681-1693 (2022)
   PUBMED   34888642
  REMARK    GeneRIF: Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome.
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Perrault,I., Halbritter,J., Porath,J.D., Gerard,X., Braun,D.A.,
            Gee,H.Y., Fathy,H.M., Saunier,S., Cormier-Daire,V., Thomas,S.,
            Attie-Bitach,T., Boddaert,N., Taschner,M., Schueler,M.,
            Lorentzen,E., Lifton,R.P., Lawson,J.A., Garfa-Traore,M., Otto,E.A.,
            Bastin,P., Caillaud,C., Kaplan,J., Rozet,J.M. and Hildebrandt,F.
  TITLE     IFT81, encoding an IFT-B core protein, as a very rare cause of a
            ciliopathy phenotype
  JOURNAL   J Med Genet 52 (10), 657-665 (2015)
   PUBMED   26275418
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Bhogaraju,S., Cajanek,L., Fort,C., Blisnick,T., Weber,K.,
            Taschner,M., Mizuno,N., Lamla,S., Bastin,P., Nigg,E.A. and
            Lorentzen,E.
  TITLE     Molecular basis of tubulin transport within the cilium by IFT74 and
            IFT81
  JOURNAL   Science 341 (6149), 1009-1012 (2013)
   PUBMED   23990561
  REMARK    GeneRIF: this study found that the two core intraflagellar
            transport proteins IFT74 and IFT81 form a tubulin-binding module
            and mapped the interaction to a calponin homology domain of IFT81
            and a highly basic domain in IFT74.
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Peng,J., Yu,L., Horiuchi,M., Zhang,P., Huang,X., Zhang,Y., Li,D.,
            Jalil,M.A. and Zhao,S.
  TITLE     Identification of human CDV-1R and mouse Cdv-1R, two novel proteins
            with putative signal peptides, especially highly expressed in
            testis and increased with the male sex maturation
  JOURNAL   Mol Biol Rep 29 (4), 353-362 (2002)
   PUBMED   12549821
  REMARK    GeneRIF: inconsistent expression levels of human CDV-1 and mouse
            Cdv-1 in heart implied that cardiac hypertrophy in human SCD might
            not be associated with the abnormal expression of CDV-1
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Higashi,M., Kobayashi,K., Iijima,M., Wakana,S., Horiuchi,M.,
            Yasuda,T., Yoshida,G., Kanmura,Y. and Saheki,T.
  TITLE     Genomic organization and mapping of mouse CDV (carnitine
            deficiency-associated gene expressed in ventricle)-1 and its
            related CDV-1R gene
  JOURNAL   Mamm Genome 11 (12), 1053-1057 (2000)
   PUBMED   11130971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007546.6 and AC009730.17.
            
            Summary: The protein encoded by this gene, together with IFT74,
            forms a tubulin-binding module of intraflagellar transport complex
            B. This module is involved in transport of tubulin within the
            cilium, and the encoded protein is required for ciliogenesis.
            Mutations in this gene are a cause of short-rib polydactyly
            syndromes. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (5), as well as variant 6, encodes
            isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.24982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..366
                     /product="intraflagellar transport protein 81 homolog
                     isoform 3"
                     /note="carnitine deficiency-associated gene expressed in
                     ventricle 1; intraflagellar transport protein 81 homolog;
                     carnitine deficiency-associated protein expressed in
                     ventricle 1"
                     /calculated_mol_wt=43014
     Region          27..>182
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     Region          <49..>317
                     /region_name="mukB"
                     /note="chromosome partition protein MukB; PRK04863"
                     /db_xref="CDD:235316"
     CDS             1..366
                     /gene="IFT81"
                     /gene_synonym="CDV-1; CDV-1R; CDV1; CDV1R; DV1; SRTD19"
                     /coded_by="NM_001347947.2:875..1975"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:28981"
                     /db_xref="HGNC:HGNC:14313"
                     /db_xref="MIM:605489"
ORIGIN      
        1 mqslkinein teinqliekk mmrnepiegk lslyrqqasi isrkkeakae elqeakekla
       61 slereasvkr nqtrefdgte vlkgdefkry vnklrskstv fkkkhqiiae lkaefgllqr
      121 teellkqrhe niqqqlqtme ekkgisgysy tqeelervsa lksevdemkg rtlddmsemv
      181 kklyslvsek ksalasvike lrqlrqkyqe ltqecdekks qydscaagle snrskleqev
      241 rrlreeclqe esryhytncm iknlevqlrr atdemkayis sdqqekrkai reqytkntae
      301 qenlgkklre kqkvireshg pnmkqakmwr dleqlmeckk qcflkqqsqt sigqviqegg
      361 edrlil
//
LOCUS       NP_001340531             343 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform k [Homo sapiens].
ACCESSION   NP_001340531 XP_016877027
VERSION     NP_001340531.1
DBSOURCE    REFSEQ: accession NM_001353602.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877027.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (17), as well as variants 18-20,
            encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.225182.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..343
                     /product="lysosomal cobalamin transporter ABCD4 isoform k"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=37800
     Region          <1..319
                     /region_name="SunT"
                     /note="ABC-type bacteriocin/lantibiotic exporters, contain
                     an N-terminal double-glycine peptidase domain [Defense
                     mechanisms]; COG2274"
                     /db_xref="CDD:441875"
     Region          124..335
                     /region_name="ABCD_peroxisomal_ALDP"
                     /note="ATP-binding cassette domain of peroxisomal
                     transporter, subfamily D; cd03223"
                     /db_xref="CDD:213190"
     CDS             1..343
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353602.2:712..1743"
                     /note="isoform k is encoded by transcript variant 17"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mrslllstvg intfdylgsi lsyvviaipi fsgvygdlsp aelstlvskn afvciylisc
       61 ftqlidlstt lsdvagythr igqlretlld mslksqdcei lgesewgldt ppgwpaaepa
      121 dtafllervs isapssdkpl ikdlslkise gqsllitgnt gtgktsllrv lgglwtstrg
      181 svqmltdfgp hgvlflpqkp fftdgtlreq viyplkevyp dsgsadderi lrflelagls
      241 nlvartegld qqvdwnwydv lspgemqrls farlfylqpk yavldeatsa lteevesely
      301 rigqqlgmtf isvghrqsle kfhslvlklc gggrwelmri kve
//
LOCUS       NP_001308500             533 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 11 [Homo sapiens].
ACCESSION   NP_001308500 XP_005263309
VERSION     NP_001308500.1
DBSOURCE    REFSEQ: accession NM_001321571.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 533)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Mar 26, 2016 this sequence version replaced XP_005263309.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (12) encodes isoform (11, also
            known as delta 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.39452.1,
                                           SRR1803616.94415.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000511664.6/ ENSP00000425824.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 11"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=59874
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..533
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321571.2:671..2272"
                     /note="isoform 11 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS82949.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalsks nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt
      481 mqseetrvwh rrdgkwqnvh fhrsgsptvp ikppcipngk enfsggtslw qni
//
LOCUS       NP_001315577             417 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 5
            [Homo sapiens].
ACCESSION   NP_001315577
VERSION     NP_001315577.1
DBSOURCE    REFSEQ: accession NM_001328648.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL672043.15 and AL358075.10.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (5) is
            shorter at the N-terminus compared to isoform 1. Variants 6, 7, 8,
            and 9 all encode the same isoform (5).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.942.1,
                                           SRR1803614.230418.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..417
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 5"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=49060
     Region          15..123
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(28,46,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(69,96)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          128..288
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Site            order(151,158,169..171,173..175,177..178,181..182,
                     184..185,188..189,192,208,211..212,215,219,222,248..249,
                     252,255)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:214016"
     Region          307..410
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(321,339,341..342,359,361)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(360,371,393,396,400)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..417
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_001328648.1:92..1345"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 mtsavpngmk dssvslqdae wywgdisree vndklrdmpd gtflvrdast kmqgdytltl
       61 rkggnnklik iyhrdgkygf sdpltfnsvv elinhyhhes laqynpkldv klmypvsryq
      121 qdqlvkedni davgkklqey hsqyqekske ydrlyeeytr tsqeiqmkrt aieafnetik
      181 ifeeqchtqe qhskeyierf rregnekeie rimmnydklk srlgeihdsk mrleqdlknq
      241 aldnreidkk mnsikpdliq lrkirdqhlv wlnhkgvrqk rlnvwlgikn edadenyfin
      301 eedenlphyd ektwfvedin rvqaedllyg kpdgaflire sskkgcyacs vvadgevkhc
      361 viystargyg faepynlyss lkelvlhyqq tslvqhndsl nvrlaypvha qmpslcr
//
LOCUS       NP_001123609             745 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin superfamily containing leucine-rich repeat protein 2
            precursor [Homo sapiens].
ACCESSION   NP_001123609
VERSION     NP_001123609.1
DBSOURCE    REFSEQ: accession NM_001130137.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Alazami,A.M., Maddirevula,S., Seidahmed,M.Z., Albhlal,L.A. and
            Alkuraya,F.S.
  TITLE     A novel ISLR2-linked autosomal recessive syndrome of congenital
            hydrocephalus, arthrogryposis and abdominal distension
  JOURNAL   Hum Genet 138 (1), 105-107 (2019)
   PUBMED   30483960
  REMARK    GeneRIF: Deletion in ISLR2 gene is associated with autosomal
            recessive syndrome of congenital hydrocephalus, arthrogryposis and
            abdominal distension.
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI917487.1 and BC152429.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. All four transcripts encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI917487.1, BC028042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMN02400288
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..745
                     /product="immunoglobulin superfamily containing
                     leucine-rich repeat protein 2 precursor"
                     /note="immunoglobulin superfamily containing leucine-rich
                     repeat protein 2; leucine-rich repeat domain and
                     immunoglobulin domain-containing axon extension protein"
                     /calculated_mol_wt=76995
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2014
     mat_peptide     19..745
                     /product="Immunoglobulin superfamily containing
                     leucine-rich repeat protein 2. /id=PRO_0000317498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
                     /calculated_mol_wt=76995
     Region          36..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <51..>183
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          53..76
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          76..97
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          100..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..169
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          154..>228
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          232..359
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          287..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          375..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            590..610
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          656..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     CDS             1..745
                     /gene="ISLR2"
                     /gene_synonym="LINX"
                     /coded_by="NM_001130137.1:506..2743"
                     /db_xref="CCDS:CCDS10259.1"
                     /db_xref="GeneID:57611"
                     /db_xref="HGNC:HGNC:29286"
                     /db_xref="MIM:614179"
ORIGIN      
        1 mfplralwlv wallgvagsc pepcacvdky ahqfadcayk elrevpeglp anvttlslsa
       61 nkitvlrrga fadvtqvtsl wlahnevrtv epgalavlsq lknldlshnf issfpwsdlr
      121 nlsalqllkm nhnrlgslpr dalgalpdlr slrinnnrlr tlapgtfdal salshlqlyh
      181 npfhcgcglv wlqawaastr vslpepdsia casppalqgv pvyrlpalpc appsvhlsae
      241 ppleapgtpl raglafvlhc iadghptprl qwqlqipggt vvleppvlsg eddgvgaeeg
      301 egegdgdllt qtqaqtptpa pawpappatp rflalangsl lvpllsakea gvytcrahne
      361 lganstsirv avaatgppkh apgaggepdg qaptserkst akgrgnsvlp skpegkikgq
      421 glakvsilge tetepeedts egeeaedqil adpaeeqrcg ngdpsryvsn hafnqsaelk
      481 phvfelgvia ldvaerearv qltplaarwg pgpggaggap rpgrrplrll ylcpagggaa
      541 vqwsrveegv naywfrglrp gtnysvclal ageachvqvv fstkkelpsl lvivavsvfl
      601 lvlatvpllg aacchllakh pgkpyrlilr pqapdpmekr iaadfdpras yleseksypa
      661 ggeaggeepe dvqgeglded aeqgdpsgdl qreeslaacs lvesqskanq eefeagseys
      721 drlplgaeav niaqeingny rqtag
//
LOCUS       NP_001305792             174 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxyguanosine kinase, mitochondrial isoform e [Homo sapiens].
ACCESSION   NP_001305792
VERSION     NP_001305792.1
DBSOURCE    REFSEQ: accession NM_001318863.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Guzman,H., Yazdani,S., Harmon,J.L., Chapman,K.A., Vitola,B.,
            Pyle,L., McKnight,H., Sigal,W., Lord,K., De Leon,D.D., Merchant,N.
            and Ganetzky,R.
  TITLE     Case report: Two unexpected cases of DGUOK-related mitochondrial
            DNA depletion syndrome presenting with hyperinsulinemic
            hypoglycemia
  JOURNAL   Front Endocrinol (Lausanne) 14, 1268135 (2023)
   PUBMED   38027095
  REMARK    GeneRIF: Case report: Two unexpected cases of DGUOK-related
            mitochondrial DNA depletion syndrome presenting with
            hyperinsulinemic hypoglycemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Unal,O., Hismi,B., Kilic,M., Gulsen,H.H., Coskun,T., Sivri,S.H.,
            Dursun,A., Yuce,A. and Tokatli,A.
  TITLE     Deoxyguanosine kinase deficiency: a report of four patients
  JOURNAL   J Pediatr Endocrinol Metab 30 (6), 697-702 (2017)
   PUBMED   28493820
  REMARK    GeneRIF: DGUOK deficiency and mutation is associated with
            mitochondrial DNA depletion syndromes.
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Jullig,M. and Eriksson,S.
  TITLE     Mitochondrial and submitochondrial localization of human
            deoxyguanosine kinase
  JOURNAL   Eur J Biochem 267 (17), 5466-5472 (2000)
   PUBMED   10951205
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Johansson,M., Bajalica-Lagercrantz,S., Lagercrantz,J. and
            Karlsson,A.
  TITLE     Localization of the human deoxyguanosine kinase gene (DGUOK) to
            chromosome 2p13
  JOURNAL   Genomics 38 (3), 450-451 (1996)
   PUBMED   8975728
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Wang,L., Hellman,U. and Eriksson,S.
  TITLE     Cloning and expression of human mitochondrial deoxyguanosine kinase
            cDNA
  JOURNAL   FEBS Lett 390 (1), 39-43 (1996)
   PUBMED   8706825
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning and expression of human deoxyguanosine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7258-7262 (1996)
   PUBMED   8692979
REFERENCE   10 (residues 1 to 174)
  AUTHORS   El-Hattab,A.W. and Scaglia,F.
  TITLE     Deoxyguanosine Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU099795.1, BF975904.1 and
            U41668.1.
            
            Summary: In mammalian cells, the phosphorylation of purine
            deoxyribonucleosides is mediated predominantly by two
            deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and
            mitochondrial deoxyguanosine kinase. The protein encoded by this
            gene is responsible for phosphorylation of purine
            deoxyribonucleosides in the mitochondrial matrix. In addition, this
            protein phosphorylates several purine deoxyribonucleoside analogs
            used in the treatment of lymphoproliferative disorders, and this
            phosphorylation is critical for the effectiveness of the analogs.
            Alternative splice variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7) uses an alternate in-frame
            splice junction and lacks another alternate exon compared to
            variant 1. The resulting isoform (e) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform a.
            Variants 6 and 7 both encode the same isoform (e).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE729569.1, BE386450.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..174
                     /product="deoxyguanosine kinase, mitochondrial isoform e"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxyguanosine kinase, mitochondrial;
                     deoxyadenosine kinase, mitochondrial"
                     /calculated_mol_wt=20869
     Region          1..172
                     /region_name="NK"
                     /note="Nucleoside/nucleotide kinase (NK) is a protein
                     superfamily consisting of multiple families of enzymes
                     that share structural similarity and are functionally
                     related to the catalysis of the reversible phosphate group
                     transfer from nucleoside triphosphates...; cl17190"
                     /db_xref="CDD:450170"
     Site            21
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..174
                     /gene="DGUOK"
                     /gene_synonym="dGK; MTDPS3; NCPH; NCPH1; PEOB4"
                     /coded_by="NM_001318863.2:210..734"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="GeneID:1716"
                     /db_xref="HGNC:HGNC:2858"
                     /db_xref="MIM:601465"
ORIGIN      
        1 mmyreparws ytfqtfsfls rlkvqlepfp ekllqarkpv qiferyifak nlfengslsd
       61 iewhiyqdwh sfllwefasr itlhgfiylq aspqvclkrl yqrareeekg ielayleqlh
      121 gqheawlihk ttklhfealm nipvlvldvn ddfseevtkq edlmrevntf vknl
//
LOCUS       NP_001137299             315 aa            linear   PRI 20-NOV-2025
DEFINITION  microtubule-associated protein RP/EB family member 2 isoform 3
            [Homo sapiens].
ACCESSION   NP_001137299
VERSION     NP_001137299.1
DBSOURCE    REFSEQ: accession NM_001143827.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Chiang,D.Y., Verkerk,A.O., Victorio,R., Shneyer,B.I., van der
            Vaart,B., Jouni,M., Narendran,N., Kc,A., Sampognaro,J.R.,
            Vetrano-Olsen,F., Oh,J.S., Buys,E., de Jonge,B., Shah,D.A.,
            Kiviniemi,T., Burridge,P.W., Bezzina,C.R., Akhmanova,A. and
            MacRae,C.A.
  TITLE     The Role of MAPRE2 and Microtubules in Maintaining Normal
            Ventricular Conduction
  JOURNAL   Circ Res 134 (1), 46-59 (2024)
   PUBMED   38095085
  REMARK    GeneRIF: The Role of MAPRE2 and Microtubules in Maintaining Normal
            Ventricular Conduction.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Zhang,D., Pan,G., Cheng,N., Sun,L., Zhou,X., Li,C. and Zhao,J.
  TITLE     JUND facilitates proliferation and angiogenesis of esophageal
            squamous cell carcinoma cell via MAPRE2 up-regulation
  JOURNAL   Tissue Cell 81, 102010 (2023)
   PUBMED   36608637
  REMARK    GeneRIF: JUND facilitates proliferation and angiogenesis of
            esophageal squamous cell carcinoma cell via MAPRE2 up-regulation.
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Wadle,A., Thiel,G., Mischo,A., Jung,V., Pfreundschuh,M. and
            Renner,C.
  TITLE     Chromosomal localization and promoter analysis of the adenomatous
            polyposis coli binding protein RP1
  JOURNAL   Oncogene 20 (41), 5920-5929 (2001)
   PUBMED   11593399
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Su,L.K. and Qi,Y.
  TITLE     Characterization of human MAPRE genes and their proteins
  JOURNAL   Genomics 71 (2), 142-149 (2001)
   PUBMED   11161807
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Juwana,J.P., Henderikx,P., Mischo,A., Wadle,A., Fadle,N.,
            Gerlach,K., Arends,J.W., Hoogenboom,H., Pfreundschuh,M. and
            Renner,C.
  TITLE     EB/RP gene family encodes tubulin binding proteins
  JOURNAL   Int J Cancer 81 (2), 275-284 (1999)
   PUBMED   10188731
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Morrison,E.E., Wardleworth,B.N., Askham,J.M., Markham,A.F. and
            Meredith,D.M.
  TITLE     EB1, a protein which interacts with the APC tumour suppressor, is
            associated with the microtubule cytoskeleton throughout the cell
            cycle
  JOURNAL   Oncogene 17 (26), 3471-3477 (1998)
   PUBMED   10030671
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Berrueta,L., Kraeft,S.K., Tirnauer,J.S., Schuyler,S.C., Chen,L.B.,
            Hill,D.E., Pellman,D. and Bierer,B.E.
  TITLE     The adenomatous polyposis coli-binding protein EB1 is associated
            with cytoplasmic and spindle microtubules
  JOURNAL   Proc Natl Acad Sci U S A 95 (18), 10596-10601 (1998)
   PUBMED   9724749
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Renner,C., Pfitzenmeier,J.P., Gerlach,K., Held,G., Ohnesorge,S.,
            Sahin,U., Bauer,S. and Pfreundschuh,M.
  TITLE     RP1, a new member of the adenomatous polyposis coli-binding
            EB1-like gene family, is differentially expressed in activated T
            cells
  JOURNAL   J Immunol 159 (3), 1276-1283 (1997)
   PUBMED   9233623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294833.1, AC015967.8 and
            BM673789.1.
            
            Summary: The protein encoded by this gene shares significant
            homology to the adenomatous polyposis coli (APC) protein-binding
            EB1 gene family. This protein is a microtubule-associated protein
            that is necessary for spindle symmetry during mitosis. It is
            thought to play a role in the tumorigenesis of colorectal cancers
            and the proliferative control of normal cells. Alternative splicing
            of this gene results in multiple transcript variants. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (3) has alternate 5' exon
            structure and it thus differs in the 5' UTR and 5' coding region,
            compared to variant 1. The encoded isoform (3) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.21045.1,
                                           SRR1803612.142565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1-q12.2"
     Protein         1..315
                     /product="microtubule-associated protein RP/EB family
                     member 2 isoform 3"
                     /note="T-cell activation protein, EB1 family; APC-binding
                     protein EB1; end-binding protein 2; APC-binding protein
                     EB2"
                     /calculated_mol_wt=35610
     Region          47..301
                     /region_name="BIM1"
                     /note="Microtubule-binding protein involved in cell cycle
                     control [Cell division and chromosome partitioning /
                     Cytoskeleton]; COG5217"
                     /db_xref="CDD:227542"
     CDS             1..315
                     /gene="MAPRE2"
                     /gene_synonym="CSCSC2; EB1; EB2; RP1"
                     /coded_by="NM_001143827.3:151..1098"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45850.1"
                     /db_xref="GeneID:10982"
                     /db_xref="HGNC:HGNC:6891"
                     /db_xref="MIM:605789"
ORIGIN      
        1 mkqnrdqkcp vsqrnssfqq pgrkpgcssw gmavnvysts itqetmsrhd iiawvndivs
       61 lnytkveqlc sgaaycqfmd mlfpgcislk kvkfqakleh eyihnfkllq asfkrmnvdk
      121 vipveklvkg rfqdnldfiq wfkkfydany dgkeydpvea rqgqdaippp dpgeqifnlp
      181 kkshhanspt agaaksspaa kpgstpsrps sakrasssgs asksdkdlet qviqlneqvh
      241 slklalegve kerdfyfgkl reiellcqeh gqenddlvqr lmdilyasee heghteepea
      301 eeqaheqqpp qqeey
//
LOCUS       NP_808210                108 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein Sm D2 isoform 2 [Homo sapiens].
ACCESSION   NP_808210
VERSION     NP_808210.2
DBSOURCE    REFSEQ: accession NM_177542.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Chang,C., Li,L., Su,L., Yang,F., Zha,Q., Sun,M., Tao,L., Wang,M.,
            Song,K., Jiang,L., Gao,H., Liang,Y., Xu,C., Yong,C., Wang,M.,
            Huang,J., Liu,J., Jin,W., Lv,W., Dong,H., Li,Q., Bu,F., Yan,S.,
            Qi,H., Zhao,S., Zhu,Y., Wang,Y., Shi,J., Qiao,Y., Xu,J., Chabot,B.
            and Chen,J.
  TITLE     Intron Retention of DDX39A Driven by SNRPD2 is a Crucial Splicing
            Axis for Oncogenic MYC/Spliceosome Program in Hepatocellular
            Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2403387 (2024)
   PUBMED   39018261
  REMARK    GeneRIF: Intron Retention of DDX39A Driven by SNRPD2 is a Crucial
            Splicing Axis for Oncogenic MYC/Spliceosome Program in
            Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Kambach,C., Walke,S., Young,R., Avis,J.M., de la Fortelle,E.,
            Raker,V.A., Luhrmann,R., Li,J. and Nagai,K.
  TITLE     Crystal structures of two Sm protein complexes and their
            implications for the assembly of the spliceosomal snRNPs
  JOURNAL   Cell 96 (3), 375-387 (1999)
   PUBMED   10025403
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Lehmeier,T., Raker,V., Hermann,H. and Luhrmann,R.
  TITLE     cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
            ribonucleoproteins: evidence for a direct D1-D2 interaction
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12317-12321 (1994)
   PUBMED   7527560
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Lehmeier,T., Foulaki,K. and Luhrmann,R.
  TITLE     Evidence for three distinct D proteins, which react differentially
            with anti-Sm autoantibodies, in the cores of the major snRNPs U1,
            U2, U4/U6 and U5
  JOURNAL   Nucleic Acids Res 18 (22), 6475-6484 (1990)
   PUBMED   1701240
REFERENCE   10 (residues 1 to 108)
  AUTHORS   Rokeach,L.A., Haselby,J.A. and Hoch,S.O.
  TITLE     Molecular cloning of a cDNA encoding the human Sm-D autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 85 (13), 4832-4836 (1988)
   PUBMED   3260384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007191.1, BU531743.1 and
            AJ707552.1.
            
            On May 15, 2009 this sequence version replaced NP_808210.1.
            
            Summary: The protein encoded by this gene belongs to the small
            nuclear ribonucleoprotein core protein family. It is required for
            pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2009].
            
            Transcript Variant: This variant (2) includes an alternate exon and
            uses a downstream start codon compared to variant 1. Isoform 2 has
            a shorter N-terminus compared to isoform 1. Variants 2 and 3 both
            encode isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU531743.1, BQ877783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..108
                     /product="small nuclear ribonucleoprotein Sm D2 isoform 2"
                     /note="snRNP core protein D2; small nuclear
                     ribonucleoprotein Sm D2; small nuclear ribonucleoprotein
                     D2 polypeptide 16.5kDa"
                     /calculated_mol_wt=12267
     Region          14..103
                     /region_name="Sm_D2"
                     /note="Sm protein D2; cd01720"
                     /db_xref="CDD:212467"
     Site            order(15,18..19,37..39,51..52,54,92,94)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212467"
     Site            order(21,29,35..39,46..47,50..54,58..59,62..63,82..84,86,
                     88..94,96..102)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212467"
     Site            order(32..38,40..52,54..58)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212467"
     Site            88..99
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212467"
     CDS             1..108
                     /gene="SNRPD2"
                     /gene_synonym="Sm-D2; SMD2; SNRPD1"
                     /coded_by="NM_177542.3:250..576"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54281.1"
                     /db_xref="GeneID:6633"
                     /db_xref="HGNC:HGNC:11159"
                     /db_xref="MIM:601061"
ORIGIN      
        1 mtpeelqkre eeefntgpls vltqsvknnt qvlincrnnk kllgrvkafd rhcnmvlenv
       61 kemwtevpks gkgkkkskpv nkdryiskmf lrgdsvivvl rnpliagk
//
LOCUS       NP_001013424             688 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001013424
VERSION     NP_001013424.1
DBSOURCE    REFSEQ: accession NM_001013406.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (5) has an alternate 5' exon, and
            lacks 2 exons in the 5' UTR and an in-frame exon in the coding
            region, as compared to variant 1. The encoded isoform 2 lacks an
            internal segment, as compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055305.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..688
                     /product="krev interaction trapped protein 1 isoform 2"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=78519
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          <282..373
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(282..284,286..287,291,294,304,306,308,312..313,
                     316..318,320..321,325,328,338,340,342,346..347,353..355,
                     357..358,362)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          306..338
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          373..592
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          588..687
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(602,621,623,629)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(633,638..641,675,679,682..683)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            675..686
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..688
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001013406.2:584..2650"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS34679.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkygkveatr illekgkcnp
      301 nllngqlssp lhfaagggha eivqillnhp etdrhitdqq grsplnicee nkqnnweeaa
      361 kllkeainkp yekvriyrmd gsyrsvelkh gnnttvqqim egmrlsqetq qyftiwicse
      421 nlslqlkpyh kplqhvrdwp eilaeltnld pqretpqlfl rrdvrlplev ekqiedplai
      481 lilfdearyn llkgfytapd aklitlasll lqivygnyes kkhkqgflne enlksivpvt
      541 klkskaphwt nrilheyknl stsegvskem hhlqrmflqn cweiptygaa fftgqiftka
      601 spsnhkvipv yvgvnikglh llnmetkall islkygcfmw qlgdtdtcfq ihsmenkmsf
      661 ivhtkqaglv vkllmklngq lmpterns
//
LOCUS       NP_001158508            1019 aa            linear   PRI 20-NOV-2025
DEFINITION  2-oxoglutarate dehydrogenase complex component E1 isoform 3
            precursor [Homo sapiens].
ACCESSION   NP_001158508
VERSION     NP_001158508.1
DBSOURCE    REFSEQ: accession NM_001165036.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1019)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1019)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   3  (residues 1 to 1019)
  AUTHORS   Whittle,E.F., Chilian,M., Karimiani,E.G., Progri,H., Buhas,D.,
            Kose,M., Ganetzky,R.D., Toosi,M.B., Torbati,P.N., Badv,R.S.,
            Shelihan,I., Yang,H., Elloumi,H.Z., Lee,S., Jamshidi,Y.,
            Pittman,A.M., Houlden,H., Ignatius,E., Rahman,S., Maroofian,R.,
            Yoon,W.H. and Carroll,C.J.
  TITLE     Biallelic variants in OGDH encoding oxoglutarate dehydrogenase lead
            to a neurodevelopmental disorder characterized by global
            developmental delay, movement disorder, and metabolic abnormalities
  JOURNAL   Genet Med 25 (2), 100332 (2023)
   PUBMED   36520152
  REMARK    GeneRIF: Biallelic variants in OGDH encoding oxoglutarate
            dehydrogenase lead to a neurodevelopmental disorder characterized
            by global developmental delay, movement disorder, and metabolic
            abnormalities.
REFERENCE   4  (residues 1 to 1019)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1019)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 1019)
  AUTHORS   McCartney,R.G., Rice,J.E., Sanderson,S.J., Bunik,V., Lindsay,H. and
            Lindsay,J.G.
  TITLE     Subunit interactions in the mammalian alpha-ketoglutarate
            dehydrogenase complex. Evidence for direct association of the
            alpha-ketoglutarate dehydrogenase and dihydrolipoamide
            dehydrogenase components
  JOURNAL   J Biol Chem 273 (37), 24158-24164 (1998)
   PUBMED   9727038
REFERENCE   7  (residues 1 to 1019)
  AUTHORS   Koike,K.
  TITLE     The gene encoding human 2-oxoglutarate dehydrogenase: structural
            organization and mapping to chromosome 7p13-p14
  JOURNAL   Gene 159 (2), 261-266 (1995)
   PUBMED   7622061
REFERENCE   8  (residues 1 to 1019)
  AUTHORS   Szabo,P., Cai,X., Ali,G. and Blass,J.P.
  TITLE     Localization of the gene (OGDH) coding for the E1k component of the
            alpha-ketoglutarate dehydrogenase complex to chromosome 7p13-p11.2
  JOURNAL   Genomics 20 (2), 324-326 (1994)
   PUBMED   8020988
REFERENCE   9  (residues 1 to 1019)
  AUTHORS   Koike,K., Urata,Y. and Goto,S.
  TITLE     Cloning and nucleotide sequence of the cDNA encoding human
            2-oxoglutarate dehydrogenase (lipoamide)
  JOURNAL   Proc Natl Acad Sci U S A 89 (5), 1963-1967 (1992)
   PUBMED   1542694
REFERENCE   10 (residues 1 to 1019)
  AUTHORS   Reed,L.J. and Hackert,M.L.
  TITLE     Structure-function relationships in dihydrolipoamide
            acyltransferases
  JOURNAL   J Biol Chem 265 (16), 8971-8974 (1990)
   PUBMED   2188967
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304439.1, AK304690.1,
            AC004859.3 and BU682361.1.
            
            Summary: This gene encodes one subunit of the 2-oxoglutarate
            dehydrogenase complex. This complex catalyzes the overall
            conversion of 2-oxoglutarate (alpha-ketoglutarate) to succinyl-CoA
            and CO(2) during the Krebs cycle. The protein is located in the
            mitochondrial matrix and uses thiamine pyrophosphate as a cofactor.
            A congenital deficiency in 2-oxoglutarate dehydrogenase activity is
            believed to lead to hypotonia, metabolic acidosis, and
            hyperlactatemia. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms.[provided by RefSeq,
            Sep 2009].
            
            Transcript Variant: This variant (3) has multiple differences in
            the presence and absence of exons in the 5' coding region, compared
            to variant 1. These differences result in a shorter protein
            (isoform 3), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304439.1, DRR138528.900388.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1019
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..1019
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 3 precursor"
                     /EC_number="1.2.4.2"
                     /note="oxoglutarate dehydrogenase (succinyl-transferring);
                     oxoglutarate (alpha-ketoglutarate) dehydrogenase
                     (lipoamide); 2-oxoglutarate dehydrogenase, mitochondrial;
                     oxoglutarate decarboxylase; OGDC-E1; 2-oxoglutarate
                     dehydrogenase complex component E1; testicular tissue
                     protein Li 131; alpha-KGDH-E1; thiamine diphosphate
                     (ThDP)-dependent 2-oxoglutarate dehydrogenase"
                     /calculated_mol_wt=110919
     transit_peptide 1..40
                     /calculated_mol_wt=4613
     mat_peptide     41..1019
                     /product="2-oxoglutarate dehydrogenase complex component
                     E1 isoform 3"
                     /calculated_mol_wt=110919
     Region          49..1012
                     /region_name="SucA"
                     /note="2-oxoglutarate dehydrogenase complex, dehydrogenase
                     (E1) component, and related enzymes [Energy production and
                     conversion]; COG0567"
                     /db_xref="CDD:440333"
     CDS             1..1019
                     /gene="OGDH"
                     /gene_synonym="AKGDH; E1k; E1o; HsOGDH; KGD1; OGDC;
                     OGDH-E1; OGDH2; OGDHD"
                     /coded_by="NM_001165036.2:55..3114"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS55107.1"
                     /db_xref="GeneID:4967"
                     /db_xref="HGNC:HGNC:8124"
                     /db_xref="MIM:613022"
ORIGIN      
        1 mfhlrtcaak lrpltasqtv ktfsqnrpaa artfqqircy sapvaaepfl sgtssnyvee
       61 mycawlenpk svhkswdiff rntnagappg tayqsplpls rgslaavaha qslveaqpnv
      121 dklvedhlav qslirayqvr ghhiakldpl giscvnfdda pvtvssnvgf ygldesdldk
      181 vfhlptttfi ggqesalplr eiirrlemay cqhigvefmf indleqcqwi rqkfetpgim
      241 qftneekrtl larlvrstrf eeflqrkwss ekrfglegce vlipalktii dkssengvdy
      301 vimgmphrgr lnvlanvirk eleqifcqfd skleaadegs gdvkyhlgmy hrrinrvtdr
      361 nitlslvanp shleaadpvv mgktkaeqfy cgdtegkkvm sillhgdaaf agqgivyetf
      421 hlsdlpsytt hgtvhvvvnn qigfttdprm arsspyptdv arvvnapifh vnsddpeavm
      481 yvckvaaewr stfhkdvvvd lvcyrrnghn emdepmftqp lmykqirkqk pvlqkyaell
      541 vsqgvvnqpe yeeeiskydk iceeafarsk dekilhikhw ldspwpgfft ldgqprsmsc
      601 pstgltedil thignvassv pvenftihgg lsrilktrge mvknrtvdwa laeymafgsl
      661 lkegihirls gqdvergtfs hrhhvlhdqn vdkrtcipmn hlwpnqapyt vcnsslseyg
      721 vlgfelgfam aspnalvlwe aqfgdfhnta qciidqficp gqakwvrqng ivlllphgme
      781 gmgpehssar perflqmcnd dpdvlpdlke anfdinqlyd cnwvvvncst pgnffhvlrr
      841 qillpfrkpl iiftpksllr hpearssfde mlpgthfqrv ipedgpaaqn penvkrllfc
      901 tgkvyydltr erkardmvgq vaitrieqls pfpfdlllke vqkypnaela wcqeehknqg
      961 yydyvkprlr ttisrakpvw yagrdpaaap atgnkkthlt elqrlldtaf dldvfknfs
//
LOCUS       NP_001288059             158 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC2 isoform
            3 [Homo sapiens].
ACCESSION   NP_001288059
VERSION     NP_001288059.1
DBSOURCE    REFSEQ: accession NM_001301130.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Pusch,C., Wang,Z., Roe,B. and Blin,N.
  TITLE     Genomic structure of the RNA polymerase II small subunit (hRPB14.4)
            locus (POLRF) and mapping to 22q13.1 by sequence identity
  JOURNAL   Genomics 34 (3), 440-442 (1996)
   PUBMED   8786150
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Acker,J., Wintzerith,M., Vigneron,M. and Kedinger,C.
  TITLE     A 14.4 KDa acidic subunit of human RNA polymerase II with a
            putative leucine-zipper
  JOURNAL   DNA Seq 4 (5), 329-331 (1994)
   PUBMED   7803819
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP195499.1 and AK026327.1.
            
            Summary: This gene encodes the sixth largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. In yeast, this polymerase subunit, in
            combination with at least two other subunits, forms a structure
            that stabilizes the transcribing polymerase on the DNA template.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (3) contains an alternate 3' exon
            structure, resulting in a different 3' coding region and 3' UTR,
            compared to variant 1. The encoded isoform (3) has a distinct
            C-terminus and is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145245
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..158
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC2 isoform 3"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC2; RNA Polymerase II subunit 14.4 kD; DNA-directed
                     RNA polymerase II subunit F; RNA polymerases I, II, and
                     III subunit ABC2; DNA-directed RNA polymerases I, II, and
                     III 14.4 kDa polypeptide; polymerase (RNA) II (DNA
                     directed) polypeptide F; polymerase (RNA) II subunit F"
                     /calculated_mol_wt=17443
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61218.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P61218.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:O88828; propagated from
                     UniProtKB/Swiss-Prot (P61218.1)"
     Region          <26..>100
                     /region_name="RNA_pol_Rpb6"
                     /note="RNA polymerase Rpb6; cl14651"
                     /db_xref="CDD:449344"
     CDS             1..158
                     /gene="POLR2F"
                     /gene_synonym="HRBP14.4; POLRF; RPABC14.4; RPABC2;
                     RPB14.4; RPB6; RPC15"
                     /coded_by="NM_001301130.2:90..566"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS77673.1"
                     /db_xref="GeneID:5435"
                     /db_xref="HGNC:HGNC:9193"
                     /db_xref="MIM:604414"
ORIGIN      
        1 msdnednfdg ddfddveede glddlenaee egqenveilp sgerpqanqk rittpymtky
       61 erarvlgtra lqiamcapvm velegetdpl liamkelnar saseppgeep pwmdrgtrde
      121 hlpscpgcpa vasntrccpp aaclpgisls rrrrlree
//
LOCUS       NP_115712                223 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA replication complex GINS protein SLD5 [Homo sapiens].
ACCESSION   NP_115712
VERSION     NP_115712.1
DBSOURCE    REFSEQ: accession NM_032336.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Zhou,Y., Yan,J., Chen,H., Zhou,W. and Yang,J.
  TITLE     MicroRNA-133a-3p Inhibits Lung Adenocarcinoma Development and
            Cisplatin Resistance through Targeting GINS4
  JOURNAL   Cells Tissues Organs 213 (1), 55-66 (2024)
   PUBMED   36273455
  REMARK    GeneRIF: MicroRNA-133a-3p Inhibits Lung Adenocarcinoma Development
            and Cisplatin Resistance through Targeting GINS4.
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Tomioka,Y., Suetsugu,T., Seki,N., Tanigawa,K., Hagihara,Y.,
            Shinmura,M., Asai,S., Kikkawa,N., Inoue,H. and Mizuno,K.
  TITLE     The Molecular Pathogenesis of Tumor-Suppressive miR-486-5p and
            miR-486-3p Target Genes: GINS4 Facilitates Aggressiveness in Lung
            Adenocarcinoma
  JOURNAL   Cells 12 (14), 1885 (2023)
   PUBMED   37508549
  REMARK    GeneRIF: The Molecular Pathogenesis of Tumor-Suppressive miR-486-5p
            and miR-486-3p Target Genes: GINS4 Facilitates Aggressiveness in
            Lung Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Sun,L., Chen,S., Wang,T. and Bi,S.
  TITLE     Hsa_circ_0008673 Promotes Breast Cancer Progression by
            MiR-578/GINS4 Axis
  JOURNAL   Clin Breast Cancer 23 (3), 281-290 (2023)
   PUBMED   36628810
  REMARK    GeneRIF: Hsa_circ_0008673 Promotes Breast Cancer Progression by
            MiR-578/GINS4 Axis.
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Conte,M.I., Poli,M.C., Taglialatela,A., Leuzzi,G., Chinn,I.K.,
            Salinas,S.A., Rey-Jurado,E., Olivares,N., Veramendi-Espinoza,L.,
            Ciccia,A., Lupski,J.R., Aldave Becerra,J.C., Mace,E.M. and
            Orange,J.S.
  TITLE     Partial loss-of-function mutations in GINS4 lead to NK cell
            deficiency with neutropenia
  JOURNAL   JCI Insight 7 (21), e154948 (2022)
   PUBMED   36345943
  REMARK    GeneRIF: Partial loss-of-function mutations in GINS4 lead to NK
            cell deficiency with neutropenia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Im,J.S., Ki,S.H., Farina,A., Jung,D.S., Hurwitz,J. and Lee,J.K.
  TITLE     Assembly of the Cdc45-Mcm2-7-GINS complex in human cells requires
            the Ctf4/And-1, RecQL4, and Mcm10 proteins
  JOURNAL   Proc Natl Acad Sci U S A 106 (37), 15628-15632 (2009)
   PUBMED   19805216
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Chang,Y.P., Wang,G., Bermudez,V., Hurwitz,J. and Chen,X.S.
  TITLE     Crystal structure of the GINS complex and functional insights into
            its role in DNA replication
  JOURNAL   Proc Natl Acad Sci U S A 104 (31), 12685-12690 (2007)
   PUBMED   17652513
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Labib,K. and Gambus,A.
  TITLE     A key role for the GINS complex at DNA replication forks
  JOURNAL   Trends Cell Biol 17 (6), 271-278 (2007)
   PUBMED   17467990
  REMARK    Review article
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Kamada,K., Kubota,Y., Arata,T., Shindo,Y. and Hanaoka,F.
  TITLE     Structure of the human GINS complex and its assembly and functional
            interface in replication initiation
  JOURNAL   Nat Struct Mol Biol 14 (5), 388-396 (2007)
   PUBMED   17417653
  REMARK    GeneRIF: The C-terminal domains of the Sld5 and Psf1 subunits are
            connected by linker regions to the core complex, and the C-terminal
            domain of Sld5 is important for core complex assembly.
REFERENCE   10 (residues 1 to 223)
  AUTHORS   De Falco,M., Ferrari,E., De Felice,M., Rossi,M., Hubscher,U. and
            Pisani,F.M.
  TITLE     The human GINS complex binds to and specifically stimulates human
            DNA polymerase alpha-primase
  JOURNAL   EMBO Rep 8 (1), 99-103 (2007)
   PUBMED   17170760
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC005995.1 and AC009630.14.
            
            Summary: The yeast heterotetrameric GINS complex is made up of
            Sld5, Psf1 (GINS1; MIM 610608), Psf2 (GINS2; MIM 610609), and Psf3
            (GINS3; MIM 610610). The formation of the GINS complex is essential
            for the initiation of DNA replication in yeast and Xenopus egg
            extracts (Ueno et al., 2005 [PubMed 16287864]). See GINS1 for
            additional information about the GINS complex.[supplied by OMIM,
            Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313373.1, AK095334.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276533.4/ ENSP00000276533.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..223
                     /product="DNA replication complex GINS protein SLD5"
                     /note="SLD5 homolog"
                     /calculated_mol_wt=25916
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BRT9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in DNA replication complex GINS
                     protein SLD5, N-terminally processed.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BRT9.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BRT9.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BRT9.1)"
     Region          26..146
                     /region_name="GINS_A_Sld5"
                     /note="Alpha-helical domain of GINS complex protein Sld5;
                     cd11711"
                     /db_xref="CDD:212549"
     Site            order(52,55,93,97,101..102,122,125,127,129..139)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:212549"
     Region          165..223
                     /region_name="GINS_B_Sld5"
                     /note="beta-strand (B) domain of GINS complex protein
                     Sld5; cd21692"
                     /db_xref="CDD:412028"
     Region          166..223
                     /region_name="Important for GINS complex assembly"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRT9.1)"
     Site            order(166,168..170,172,190,199,202..207)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:412028"
     CDS             1..223
                     /gene="GINS4"
                     /gene_synonym="SLD5"
                     /coded_by="NM_032336.3:156..827"
                     /db_xref="CCDS:CCDS6116.1"
                     /db_xref="GeneID:84296"
                     /db_xref="HGNC:HGNC:28226"
                     /db_xref="MIM:610611"
ORIGIN      
        1 mteevdflgq dsdggseevv ltpaelierl eqawmnekfa pelleskpei vecvmeqleh
       61 meenlrrakr edlkvsihqm emeriryvls sylrcrlmki ekffphvlek ektrpegeps
      121 slspeelafa refmantesy lknvalkhmp pnlqkvdlfr avpkpdldsy vflrvrerqe
      181 nilvepdtde qrdyvidlek gsqhlirykt iaplvasgav qli
//
LOCUS       NP_055152                520 aa            linear   PRI 20-NOV-2025
DEFINITION  RING-type E3 ubiquitin-protein ligase PPIL2 isoform a [Homo
            sapiens].
ACCESSION   NP_055152
VERSION     NP_055152.1
DBSOURCE    REFSEQ: accession NM_014337.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Carson,R., McKnight,A.J., Todd,S., Liu,W.W., Heggarty,S., Craig,D.,
            McGuinness,B., Irvine,G.B., Passmore,A.P. and Johnston,J.A.
  TITLE     Variation in RTN3 and PPIL2 genes does not influence platelet
            membrane beta-secretase activity or susceptibility to alzheimer's
            disease in the northern Irish population
  JOURNAL   Neuromolecular Med 11 (4), 337-344 (2009)
   PUBMED   19669607
  REMARK    GeneRIF: common genetic variation in the BACE1-interacting
            proteins, RTN3 an PPIL2, does not influence platelet b-secretase
            activity or susceptibility to Alzheimer's disease in this
            population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Pushkarsky,T., Yurchenko,V., Vanpouille,C., Brichacek,B.,
            Vaisman,I., Hatakeyama,S., Nakayama,K.I., Sherry,B. and
            Bukrinsky,M.I.
  TITLE     Cell surface expression of CD147/EMMPRIN is regulated by
            cyclophilin 60
  JOURNAL   J Biol Chem 280 (30), 27866-27871 (2005)
   PUBMED   15946952
  REMARK    GeneRIF: cyclophilin 60 regulates cell surface expression of
            CD147/EMMPRIN
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Hatakeyama,S., Yada,M., Matsumoto,M., Ishida,N. and Nakayama,K.I.
  TITLE     U box proteins as a new family of ubiquitin-protein ligases
  JOURNAL   J Biol Chem 276 (35), 33111-33120 (2001)
   PUBMED   11435423
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Wang,B.B., Hayenga,K.J., Payan,D.G. and Fisher,J.M.
  TITLE     Identification of a nuclear-specific cyclophilin which interacts
            with the proteinase inhibitor eglin c
  JOURNAL   Biochem J 314 (Pt 1) (Pt 1), 313-319 (1996)
   PUBMED   8660300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000553.1.
            
            Summary: This gene is a member of the cyclophilin family of
            peptidylprolyl isomerases. The cyclophilins are a highly conserved
            ubiquitous family, members of which play an important role in
            protein folding, immunosuppression by cyclosporin A, and infection
            of HIV-1 virions. This protein interacts with the proteinase
            inhibitor eglin c and is localized in the nucleus. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 4 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.157620.1,
                                           SRR1803613.189868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398831.8/ ENSP00000381812.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21-q11.22"
     Protein         1..520
                     /product="RING-type E3 ubiquitin-protein ligase PPIL2
                     isoform a"
                     /EC_number="2.3.2.27"
                     /note="peptidylprolyl cis-trans isomerase;
                     cyclophilin-like protein CyP-60; peptidyl-prolyl cis-trans
                     isomerase-like 2; cyclophilin, 60kDa; PPIase;
                     cyclophilin-60; rotamase PPIL2; U-box domain containing 7;
                     peptidylprolyl isomerase (cyclophilin)-like 2; RING-type
                     E3 ubiquitin transferase isomerase-like 2; probable
                     inactive peptidyl-prolyl cis-trans isomerase-like 2;
                     RING-type E3 ubiquitin-protein ligase PPIL2"
                     /calculated_mol_wt=58693
     Region          38..110
                     /region_name="RING-Ubox_PPIL2"
                     /note="U-box domain, a modified RING finger, found in
                     peptidyl-prolyl cis-trans isomerase-like 2 (PPIL2) and
                     similar proteins; cd16663"
                     /db_xref="CDD:438325"
     Region          100..159
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Site            order(103,106,122,124,127,130,143,146)
                     /site_type="other"
                     /note="cross-brace motif"
                     /db_xref="CDD:438324"
     Region          281..440
                     /region_name="cyclophilin_RING"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases (cyclophilins) having a modified RING finger
                     domain. This group includes the nuclear proteins, Human
                     hCyP-60 and Caenorhabditis elegans MOG-6 which, compared
                     to the archetypal cyclophilin Human...; cd01923"
                     /db_xref="CDD:238904"
     Site            order(322..323,328,379,381,389)
                     /site_type="active"
                     /db_xref="CDD:238904"
     Region          456..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13356.1)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13356.1)"
     Site            482
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13356.1)"
     CDS             1..520
                     /gene="PPIL2"
                     /gene_synonym="CYC4; Cyp-60; CYP60; hCyP-60; UBOX7"
                     /coded_by="NM_014337.4:89..1651"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13793.1"
                     /db_xref="GeneID:23759"
                     /db_xref="HGNC:HGNC:9261"
                     /db_xref="MIM:607588"
ORIGIN      
        1 mgkrqhqkdk myitcaeyth fyggkkpdlp qtnfrrlpfd hcslslqpfv ypvctpdgiv
       61 fdllnivpwl kkygtnpsng ekldgrslik lnfsknsegk yhcpvlftvf tnnthivavr
      121 ttgnvyayea veqlnikakn frdlltdepf srqdiitlqd ptnldkfnvs nfyhvknnmk
      181 iidpdeekak qdpsyylknt naetretlqe lykefkgdei laatmkapek kkvdklnaah
      241 ystgkvsasf tstamvpett heaaaidedv lryqfvkkkg yvrlhtnkgd lnlelhcdlt
      301 pktcenfirl ckkhyydgti fhrsirnfvi qggdptgtgt ggesywgkpf kdefrpnlsh
      361 tgrgilsman sgpnsnrsqf fitfrscayl dkkhtifgrv vggfdvltam envesdpktd
      421 rpkeeirida ttvfvdpyee adaqiaqerk tqlkvapetk vkssqpqags qgpqtfrqgv
      481 gkyinpaatk raaeeepsts atvpmskkkp srgfgdfssw
//
LOCUS       NP_060343                421 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SOCS box protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_060343
VERSION     NP_060343.1
DBSOURCE    REFSEQ: accession NM_017873.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Zeng,W., Zhu,J.F., Guo,J., Huang,G.J., Ai,L.S., Zeng,Y. and
            Liao,W.J.
  TITLE     m6A-modified circFNDC3B inhibits colorectal cancer stemness and
            metastasis via RNF41-dependent ASB6 degradation
  JOURNAL   Cell Death Dis 13 (11), 1008 (2022)
   PUBMED   36446779
  REMARK    GeneRIF: m[6]A-modified circFNDC3B inhibits colorectal cancer
            stemness and metastasis via RNF41-dependent ASB6 degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Gong,L., Wang,K., Wang,M., Hu,R., Li,H., Gao,D. and Lin,M.
  TITLE     CUL5-ASB6 Complex Promotes p62/SQSTM1 Ubiquitination and
            Degradation to Regulate Cell Proliferation and Autophagy
  JOURNAL   Front Cell Dev Biol 9, 684885 (2021)
   PUBMED   34164402
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Kohroki,J., Nishiyama,T., Nakamura,T. and Masuho,Y.
  TITLE     ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin
            ligase complexes
  JOURNAL   FEBS Lett 579 (30), 6796-6802 (2005)
   PUBMED   16325183
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Wilcox,A., Katsanakis,K.D., Bheda,F. and Pillay,T.S.
  TITLE     Asb6, an adipocyte-specific ankyrin and SOCS box protein, interacts
            with APS to enable recruitment of elongins B and C to the insulin
            receptor signaling complex
  JOURNAL   J Biol Chem 279 (37), 38881-38888 (2004)
   PUBMED   15231829
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590369.18.
            
            Summary: The protein encoded by this gene belongs to a family of
            ankyrin repeat proteins that, along with four other protein
            families, contain a C-terminal SOCS box motif. Growing evidence
            suggests that the SOCS box, similar to the F-box, acts as a bridge
            between specific substrate-binding domains and the more generic
            proteins that comprise a large family of E3 ubiquitin protein
            ligases. Alternatively spliced transcript variants have been
            identified for this gene. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.254876.1,
                                           SRR1803617.22872.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000277458.5/ ENSP00000277458.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..421
                     /product="ankyrin repeat and SOCS box protein 6 isoform 1"
                     /note="ankyrin repeat and SOCS box protein 6"
                     /calculated_mol_wt=47005
     Region          17..>212
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          67..97
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          72..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..131
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          105..133
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(108..109,112..114,116..117,121,124,133,136,138,
                     142..143,146..147,149,151..152,156,159,168,170,172,
                     177..178,181..183,185..186,195,198)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          136..168
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          136..166
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          170..205
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          170..205
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          226..255
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          260..289
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          370..413
                     /region_name="SOCS_ASB6"
                     /note="SOCS (suppressors of cytokine signaling) box of
                     ASB6-like proteins. ASB family members have a C-terminal
                     SOCS box and an N-terminal ankyrin-related sequence. ASB6
                     interacts with the adaptor protein APS and recruits
                     elongin B/C to the insulin receptor...; cd03725"
                     /db_xref="CDD:239695"
     Site            order(371..376,382,393,399,404)
                     /site_type="other"
                     /note="putative elongin B/C interaction [polypeptide
                     binding]"
                     /db_xref="CDD:239695"
     CDS             1..421
                     /gene="ASB6"
                     /coded_by="NM_017873.4:153..1418"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6924.1"
                     /db_xref="GeneID:140459"
                     /db_xref="HGNC:HGNC:17181"
                     /db_xref="MIM:615051"
ORIGIN      
        1 mpflhgfrri ifeyqplvda ilgslgiqdp erqesldrps yvaseesril vltellerka
       61 hspfyqegvs nallkmaelg ltraadvllr hganlnfedp vtyytalhia vlrnqpdmve
      121 llvhhgadvn rrdrihessp ldlaseeper lpclqrlldl gadvnaadkh gktallhala
      181 ssdgvqihnt enirlllegg advkattkdg dtvftciifl lgetvggdke eaqminrfcf
      241 qvtrlllahg adpsecpahe slthiclksf klhfpllrfl lesgaayncs lhgascwsgf
      301 hiiferlcsh pgctedesha dllrkaetvl dlmvtnsqkl qlpenfdihp vgslaekiqa
      361 lhfslrqles yppplkhlcr vairlylqpw pvdvkvkalp lpdrlkwyll sehsgsvedd
      421 i
//
LOCUS       NP_064522                841 aa            linear   PRI 20-NOV-2025
DEFINITION  GRIP1-associated protein 1 [Homo sapiens].
ACCESSION   NP_064522
VERSION     NP_064522.4
DBSOURCE    REFSEQ: accession NM_020137.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 841)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 841)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 841)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 841)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 841)
  AUTHORS   Wilkinson,B., Evgrafov,O.V., Zheng,D., Hartel,N., Knowles,J.A.,
            Graham,N.A., Ichida,J.K. and Coba,M.P.
  TITLE     Endogenous Cell Type-Specific Disrupted in Schizophrenia 1
            Interactomes Reveal Protein Networks Associated With
            Neurodevelopmental Disorders
  JOURNAL   Biol Psychiatry 85 (4), 305-316 (2019)
   PUBMED   29961565
REFERENCE   6  (residues 1 to 841)
  AUTHORS   Hoogenraad,C.C., Popa,I., Futai,K., Martinez-Sanchez,E., Wulf,P.S.,
            van Vlijmen,T., Dortland,B.R., Oorschot,V., Govers,R., Monti,M.,
            Heck,A.J., Sheng,M., Klumperman,J., Rehmann,H., Jaarsma,D.,
            Kapitein,L.C. and van der Sluijs,P.
  TITLE     Neuron specific Rab4 effector GRASP-1 coordinates membrane
            specialization and maturation of recycling endosomes
  JOURNAL   PLoS Biol 8 (1), e1000283 (2010)
   PUBMED   20098723
  REMARK    Erratum:[PLoS Biol. 2010;8(9)
            doi:10.1371/annotation/b17dfb99-8809-4c5a-86c2-c2a0f7ca7f5e.
            Sanchez-Martinez, Emma [corrected to Martinez-Sanchez, Emma]]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 841)
  AUTHORS   Ye,B., Yu,W.P., Thomas,G.M. and Huganir,R.L.
  TITLE     GRASP-1 is a neuronal scaffold protein for the JNK signaling
            pathway
  JOURNAL   FEBS Lett 581 (23), 4403-4410 (2007)
   PUBMED   17761173
  REMARK    GeneRIF: Results suggest that GRASP-1 serves as a scaffold protein
            to facilitate MEKK-1 activation of JNK signaling in neurons.
REFERENCE   8  (residues 1 to 841)
  AUTHORS   Stinton,L.M., Selak,S. and Fritzler,M.J.
  TITLE     Identification of GRASP-1 as a novel 97 kDa autoantigen localized
            to endosomes
  JOURNAL   Clin Immunol 116 (2), 108-117 (2005)
   PUBMED   15897011
  REMARK    GeneRIF: GRASP-1 was identified as an soluble autoantigen that has
            numerous coiled-coil domains throughout the protein.
REFERENCE   9  (residues 1 to 841)
  AUTHORS   Ye,B., Sugo,N., Hurn,P.D. and Huganir,R.L.
  TITLE     Physiological and pathological caspase cleavage of the neuronal
            RasGEF GRASP-1 as detected using a cleavage site-specific antibody
  JOURNAL   Neuroscience 114 (1), 217-227 (2002)
   PUBMED   12207967
REFERENCE   10 (residues 1 to 841)
  AUTHORS   Ye,B., Liao,D., Zhang,X., Zhang,P., Dong,H. and Huganir,R.L.
  TITLE     GRASP-1: a neuronal RasGEF associated with the AMPA receptor/GRIP
            complex
  JOURNAL   Neuron 26 (3), 603-617 (2000)
   PUBMED   10896157
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233294.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_064522.3.
            
            Summary: This gene encodes a guanine nucleotide exchange factor for
            the Ras family of small G proteins (RasGEF). The encoded protein
            interacts in a complex with glutamate receptor interacting protein
            1 (GRIP1) and plays a role in the regulation of AMPA receptor
            function. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.171255.1,
                                           SRR1660803.126606.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376423.8/ ENSP00000365606.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..841
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..841
                     /product="GRIP1-associated protein 1"
                     /calculated_mol_wt=95875
     Region          2..>648
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Region          <193..>511
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          532..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V328.2)"
     Region          558..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            598..599
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3.
                     /evidence=ECO:0000250|UniProtKB:Q9JHZ4; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     mat_peptide     599..841
                     /product="GRASP-1 C-terminal chain. /id=PRO_0000441811"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V328.2)"
                     /calculated_mol_wt=27322
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Region          681..706
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHZ4; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VD04; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q4V328.2)"
     CDS             1..841
                     /gene="GRIPAP1"
                     /gene_synonym="GRASP-1"
                     /coded_by="NM_020137.5:36..2561"
                     /db_xref="CCDS:CCDS35248.1"
                     /db_xref="GeneID:56850"
                     /db_xref="HGNC:HGNC:18706"
                     /db_xref="MIM:300408"
ORIGIN      
        1 maqalseeef qrmqaqllel rtnnyqlsde lrkngvelts lrqkvayldk efskaqkals
       61 kskkaqevev llsenemlqa klhsqeedfr lqnstlmaef sklcsqmeql eqenqqlkeg
      121 aagagvaqag plvdgellrl qaentalqkn vaalqerygk eagkfsavse gqgdppggla
      181 ptvlapmpla evelkwemek eekrllweql qglesskqae tsrlqeelak lseklkkkqe
      241 sfcrlqteke tlfndsrnki eelqqrkead hkaqlartqk lqqeleaanq slaelrdqrq
      301 gerlehaaal ralqdqvsiq sadaqeqveg llaennalrt slaaleqiqt aktqelnmlr
      361 eqttglaael qqqqaeyedl mgqkddlnsq lqeslransr lleqlqeigq ekeqltqelq
      421 earksaekrk amldelamet lqeksqhkee lgavrlrhek evlgvrarye relrelhedk
      481 krqeeelrgq ireekartre letlqqtvee lqaqvhsmdg akgwferrlk eaeeslqqqq
      541 qeqeealkqc reqhaaelkg keeelqdvrd qleqaqeerd chlktisslk qevkdtvdgq
      601 rilekkgsaa lkdlkrqlhl erkradklqe rlqdiltnsk srsgleelvl semnspsrtq
      661 tgdsssissf syreilreke ssavparsls sspqaqpprp aelsdeevae lfqrlaetqq
      721 ekwmleekvk hlevssasma edlcrksaii etyvmdsrid vsvaaghtdr sglgsvlrdl
      781 vkpgdenlre mnkklqnmle eqltknmhlh kdmevlsqei vrlskecvgp pdpdlepget
      841 s
//
LOCUS       NP_001129198             420 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001129198
VERSION     NP_001129198.1
DBSOURCE    REFSEQ: accession NM_001135726.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 420)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, AC108449.5 and BQ019252.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, and 3 all encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.793364.1,
                                           SRR3476690.513903.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287701.15/ ENSP00000287701.10
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..420
                     /product="homeobox-containing protein 1 isoform 1"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=47147
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          353..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..420
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001135726.3:342..1604"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6071.1"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr anieaailes hgidvqspgg
      361 hsnsddvdgn dyseqddsts hsdhqdpisl avemaavnht ilalarqgan eiktealddd
//
LOCUS       NP_690601                300 aa            linear   PRI 20-NOV-2025
DEFINITION  actin-related protein 2/3 complex subunit 2 [Homo sapiens].
ACCESSION   NP_690601
VERSION     NP_690601.1
DBSOURCE    REFSEQ: accession NM_152862.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Poh,J., Ponsford,A.H., Boyd,J., Woodsmith,J., Stelzl,U., Wanker,E.,
            Harper,N., MacEwan,D. and Sanderson,C.M.
  TITLE     A functionally defined high-density NRF2 interactome reveals new
            conditional regulators of ARE transactivation
  JOURNAL   Redox Biol 37, 101686 (2020)
   PUBMED   32911434
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Skruber,K., Warp,P.V., Shklyarov,R., Thomas,J.D., Swanson,M.S.,
            Henty-Ridilla,J.L., Read,T.A. and Vitriol,E.A.
  TITLE     Arp2/3 and Mena/VASP Require Profilin 1 for Actin Network Assembly
            at the Leading Edge
  JOURNAL   Curr Biol 30 (14), 2651-2664 (2020)
   PUBMED   32470361
  REMARK    GeneRIF: Arp2/3 and Mena/VASP Require Profilin 1 for Actin Network
            Assembly at the Leading Edge.
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Al-Zeer,M.A., Dutkiewicz,M., von Hacht,A., Kreuzmann,D., Rohrs,V.
            and Kurreck,J.
  TITLE     Alternatively spliced variants of the 5'-UTR of the ARPC2 mRNA
            regulate translation by an internal ribosome entry site (IRES)
            harboring a guanine-quadruplex motif
  JOURNAL   RNA Biol 16 (11), 1622-1632 (2019)
   PUBMED   31387452
  REMARK    GeneRIF: Study provides evidence that the 5'-UTR1 of ARPC2 has
            internal ribosome entry site activity and regulates translation
            during stressful cellular conditions such as high cell density.
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Robinson,R.C., Turbedsky,K., Kaiser,D.A., Marchand,J.B.,
            Higgs,H.N., Choe,S. and Pollard,T.D.
  TITLE     Crystal structure of Arp2/3 complex
  JOURNAL   Science 294 (5547), 1679-1684 (2001)
   PUBMED   11721045
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Zhao,X., Yang,Z., Qian,M. and Zhu,X.
  TITLE     Interactions among subunits of human Arp2/3 complex: p20-Arc as the
            hub
  JOURNAL   Biochem Biophys Res Commun 280 (2), 513-517 (2001)
   PUBMED   11162547
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Naar,A.M., Beaurang,P.A., Zhou,S., Abraham,S., Solomon,W. and
            Tjian,R.
  TITLE     Composite co-activator ARC mediates chromatin-directed
            transcriptional activation
  JOURNAL   Nature 398 (6730), 828-832 (1999)
   PUBMED   10235267
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Machesky,L.M., Reeves,E., Wientjes,F., Mattheyse,F.J., Grogan,A.,
            Totty,N.F., Burlingame,A.L., Hsuan,J.J. and Segal,A.W.
  TITLE     Mammalian actin-related protein 2/3 complex localizes to regions of
            lamellipodial protrusion and is composed of evolutionarily
            conserved proteins
  JOURNAL   Biochem J 328 (Pt 1) (Pt 1), 105-112 (1997)
   PUBMED   9359840
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Welch,M.D., DePace,A.H., Verma,S., Iwamatsu,A. and Mitchison,T.J.
  TITLE     The human Arp2/3 complex is composed of evolutionarily conserved
            subunits and is localized to cellular regions of dynamic actin
            filament assembly
  JOURNAL   J Cell Biol 138 (2), 375-384 (1997)
   PUBMED   9230079
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG282181.1, AK290268.1 and
            CN291458.1.
            
            Summary: This gene encodes one of seven subunits of the human
            Arp2/3 protein complex. The Arp2/3 protein complex has been
            implicated in the control of actin polymerization in cells and has
            been conserved through evolution. The exact role of the protein
            encoded by this gene, the p34 subunit, has yet to be determined.
            Two alternatively spliced variants have been characterized to date.
            Additional alternatively spliced variants have been described but
            their full length nature has not been determined. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.750238.1,
                                           SRR5189652.54299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315717.10/ ENSP00000327137.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..300
                     /product="actin-related protein 2/3 complex subunit 2"
                     /note="ARP2/3 protein complex subunit 34; arp2/3 complex
                     34 kDa subunit; actin related protein 2/3 complex, subunit
                     2, 34kDa; testis tissue sperm-binding protein Li 53e"
                     /calculated_mol_wt=34202
     Region          57..284
                     /region_name="P34-Arc"
                     /note="Arp2/3 complex, 34 kD subunit p34-Arc; pfam04045"
                     /db_xref="CDD:461144"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15144.1)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15144.1)"
     CDS             1..300
                     /gene="ARPC2"
                     /gene_synonym="ARC34; p34-Arc; PNAS-139; PRO2446"
                     /coded_by="NM_152862.3:75..977"
                     /db_xref="CCDS:CCDS2410.1"
                     /db_xref="GeneID:10109"
                     /db_xref="HGNC:HGNC:705"
                     /db_xref="MIM:604224"
ORIGIN      
        1 millevnnri ieetlalkfe naaagnkpea vevtfadfdg vlyhisnpng dktkvmvsis
       61 lkfykelqah gadellkrvy gsflvnpesg ynvsllydle nlpaskdsiv hqagmlkrnc
      121 fasvfekyfq fqeegkegen ravihyrdde tmyveskkdr vtvvfstvfk ddddvvigkv
      181 fmqefkegrr ashtapqvlf shrepplelk dtdaavgdni gyitfvlfpr htnasardnt
      241 inlihtfrdy lhyhikcska yihtrmrakt sdflkvlnra rpdaekkemk titgktfssr
//
LOCUS       NP_059133                782 aa            linear   PRI 20-NOV-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 2 isoform 1
            [Homo sapiens].
ACCESSION   NP_059133
VERSION     NP_059133.1
DBSOURCE    REFSEQ: accession NM_017437.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Gutierrez,P.A., Baughman,K., Sun,Y. and Tong,L.
  TITLE     A real-time fluorescence assay for CPSF73, the nuclease for
            pre-mRNA 3'-end processing
  JOURNAL   RNA 27 (10), 1148-1154 (2021)
   PUBMED   34230059
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Sung,T.Y., Kim,M., Kim,T.Y., Kim,W.G., Park,Y., Song,D.E.,
            Park,S.Y., Kwon,H., Choi,Y.M., Jang,E.K., Jeon,M.J., Shong,Y.K.,
            Hong,S.J. and Kim,W.B.
  TITLE     Negative Expression of CPSF2 Predicts a Poorer Clinical Outcome in
            Patients with Papillary Thyroid Carcinoma
  JOURNAL   Thyroid 25 (9), 1020-1025 (2015)
   PUBMED   26148673
  REMARK    GeneRIF: CPSF2 may have a role in Papillary Thyroid Carcinoma
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Schul,W., Groenhout,B., Koberna,K., Takagaki,Y., Jenny,A.,
            Manders,E.M., Raska,I., van Driel,R. and de Jong,L.
  TITLE     The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are
            concentrated in nuclear domains closely associated with coiled
            bodies and newly synthesized RNA
  JOURNAL   EMBO J 15 (11), 2883-2892 (1996)
   PUBMED   8654386
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Jenny,A., Hauri,H.P. and Keller,W.
  TITLE     Characterization of cleavage and polyadenylation specificity factor
            and cloning of its 100-kilodalton subunit
  JOURNAL   Mol Cell Biol 14 (12), 8183-8190 (1994)
   PUBMED   7969155
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Bienroth,S., Keller,W. and Wahle,E.
  TITLE     Assembly of a processive messenger RNA polyadenylation complex
  JOURNAL   EMBO J 12 (2), 585-594 (1993)
   PUBMED   8440247
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB081880.1, BC060854.1, BC070095.1, AB037788.1 and AL121773.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.204380.1,
                                           SRR1660803.13981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298875.9/ ENSP00000298875.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..782
                     /product="cleavage and polyadenylation specificity factor
                     subunit 2 isoform 1"
                     /note="cleavage and polyadenylation specificity factor
                     subunit 2; CPSF 100kDa subunit; CPSF 100 kDa subunit;
                     cleavage and polyadenylation specificity factor 100 kDa
                     subunit; cleavage and polyadenylation specific factor 2,
                     100kDa"
                     /calculated_mol_wt=88356
     Region          7..204
                     /region_name="CPSF2-like_MBL-fold"
                     /note="cleavage and polyadenylation specificity factor
                     (CPSF) subunit 2 and related proteins; MBL-fold
                     metallo-hydrolase domain; cd16293"
                     /db_xref="CDD:293851"
     Site            order(16,62,64,66..67,153,175)
                     /site_type="active"
                     /db_xref="CDD:293851"
     Site            order(134..136,145,161,163,169,192)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:293851"
     Region          243..368
                     /region_name="Beta-Casp"
                     /note="Beta-Casp domain; smart01027"
                     /db_xref="CDD:214983"
     Region          407..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2I0.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P2I0.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P2I0.2)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P2I0.2)"
     Region          528..591
                     /region_name="RMMBL"
                     /note="Zn-dependent metallo-hydrolase RNA specificity
                     domain; pfam07521"
                     /db_xref="CDD:462191"
     Region          608..779
                     /region_name="CPSF100_C"
                     /note="Cleavage and polyadenylation factor 2 C-terminal;
                     pfam13299"
                     /db_xref="CDD:463836"
     Site            660
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P2I0.2)"
     CDS             1..782
                     /gene="CPSF2"
                     /gene_synonym="CPSF100"
                     /coded_by="NM_017437.3:254..2602"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9902.1"
                     /db_xref="GeneID:53981"
                     /db_xref="HGNC:HGNC:2325"
                     /db_xref="MIM:606028"
ORIGIN      
        1 mtsiiklttl sgvqeesalc yllqvdefrf lldcgwdehf smdiidslrk hvhqidavll
       61 shpdplhlga lpyavgklgl ncaiyatipv ykmgqmfmyd lyqsrhnted ftlftlddvd
      121 aafdkiqqlk fsqivnlkgk ghglsitplp aghmiggtiw kivkdgeeei vyavdfnhkr
      181 eihlngcsle mlsrpsllit dsfnatyvqp rrkqrdeqll tnvletlrgd gnvliavdta
      241 grvlelaqll dqiwrtkdag lgvyslalln nvsynvvefs ksqvewmsdk lmrcfedkrn
      301 npfqfrhlsl chglsdlarv pspkvvlasq pdlecgfsrd lfiqwcqdpk nsiiltyrtt
      361 pgtlarflid npsekiteie lrkrvklegk eleeylekek lkkeaakkle qskeadidss
      421 desdieedid qpsahktkhd lmmkgegsrk gsffkqakks ypmfpapeer ikwdeygeii
      481 kpedflvpel qateeekskl esgltngdep mdqdlsdvpt kcisttesie ikarvtyidy
      541 egrsdgdsik kiinqmkprq liivhgppea sqdlaeccra fggkdikvym pklhetvdat
      601 sethiyqvrl kdslvsslqf ckakdaelaw idgvldmrvs kvdtgvilee gelkddgeds
      661 emqveapsds sviaqqkamk slfgddeket geeseiiptl eplpphevpg hqsvfmnepr
      721 lsdfkqvllr egiqaefvgg vlvcnnqvav rrtetgrigl egclcqdfyr irdllyeqya
      781 iv
//
LOCUS       NP_001156333             230 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome c oxidase assembly protein COX11, mitochondrial isoform
            2 [Homo sapiens].
ACCESSION   NP_001156333
VERSION     NP_001156333.1
DBSOURCE    REFSEQ: accession NM_001162861.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Li,B., Yu,X. and Pang,F.
  TITLE     LncRNA FGD5-AS1 Alleviates Inflammation in Allergic Rhinitis
            through the miR-223-3p/COX11 Axis
  JOURNAL   Int Arch Allergy Immunol 185 (3), 201-211 (2024)
   PUBMED   38071964
  REMARK    GeneRIF: LncRNA FGD5-AS1 Alleviates Inflammation in Allergic
            Rhinitis through the miR-223-3p/COX11 Axis.
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Caron-Godon,C.A., Della Vecchia,S., Romano,A., Doccini,S., Dal
            Canto,F., Pasquariello,R., Rubegni,A., Battini,R., Santorelli,F.M.,
            Glerum,D.M. and Nesti,C.
  TITLE     Novel COX11 Mutations Associated with Mitochondrial Disorder:
            Functional Characterization in Patient Fibroblasts and
            Saccharomyces cerevisiae
  JOURNAL   Int J Mol Sci 24 (23), 16636 (2023)
   PUBMED   38068960
  REMARK    GeneRIF: Novel COX11 Mutations Associated with Mitochondrial
            Disorder: Functional Characterization in Patient Fibroblasts and
            Saccharomyces cerevisiae.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Rius,R., Bennett,N.K., Bhattacharya,K., Riley,L.G., Yuksel,Z.,
            Formosa,L.E., Compton,A.G., Dale,R.C., Cowley,M.J., Gayevskiy,V.,
            Al Tala,S.M., Almehery,A.A., Ryan,M.T., Thorburn,D.R., Nakamura,K.
            and Christodoulou,J.
  TITLE     Biallelic pathogenic variants in COX11 are associated with an
            infantile-onset mitochondrial encephalopathy
  JOURNAL   Hum Mutat 43 (12), 1970-1978 (2022)
   PUBMED   36030551
  REMARK    GeneRIF: Biallelic pathogenic variants in COX11 are associated with
            an infantile-onset mitochondrial encephalopathy.
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Esteves,F., Xavier,J.M., Ford,A.M., Rocha,C., Pharoah,P.D.P.,
            Caldas,C., Chin,S.F. and Maia,A.T.
  TITLE     Germline allelic expression of genes at 17q22 locus associates with
            risk of breast cancer
  JOURNAL   Eur J Cancer 172, 146-157 (2022)
   PUBMED   35772352
  REMARK    GeneRIF: Germline allelic expression of genes at 17q22 locus
            associates with risk of breast cancer.
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Nyvltova,E., Dietz,J.V., Seravalli,J., Khalimonchuk,O. and
            Barrientos,A.
  TITLE     Coordination of metal center biogenesis in human cytochrome c
            oxidase
  JOURNAL   Nat Commun 13 (1), 3615 (2022)
   PUBMED   35750769
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Ahmed,S., Thomas,G., Ghoussaini,M., Healey,C.S., Humphreys,M.K.,
            Platte,R., Morrison,J., Maranian,M., Pooley,K.A., Luben,R.,
            Eccles,D., Evans,D.G., Fletcher,O., Johnson,N., dos Santos
            Silva,I., Peto,J., Stratton,M.R., Rahman,N., Jacobs,K.,
            Prentice,R., Anderson,G.L., Rajkovic,A., Curb,J.D., Ziegler,R.G.,
            Berg,C.D., Buys,S.S., McCarty,C.A., Feigelson,H.S., Calle,E.E.,
            Thun,M.J., Diver,W.R., Bojesen,S., Nordestgaard,B.G., Flyger,H.,
            Dork,T., Schurmann,P., Hillemanns,P., Karstens,J.H.,
            Bogdanova,N.V., Antonenkova,N.N., Zalutsky,I.V., Bermisheva,M.,
            Fedorova,S., Khusnutdinova,E., Kang,D., Yoo,K.Y., Noh,D.Y.,
            Ahn,S.H., Devilee,P., van Asperen,C.J., Tollenaar,R.A.,
            Seynaeve,C., Garcia-Closas,M., Lissowska,J., Brinton,L.,
            Peplonska,B., Nevanlinna,H., Heikkinen,T., Aittomaki,K.,
            Blomqvist,C., Hopper,J.L., Southey,M.C., Smith,L., Spurdle,A.B.,
            Schmidt,M.K., Broeks,A., van Hien,R.R., Cornelissen,S., Milne,R.L.,
            Ribas,G., Gonzalez-Neira,A., Benitez,J., Schmutzler,R.K.,
            Burwinkel,B., Bartram,C.R., Meindl,A., Brauch,H., Justenhoven,C.,
            Hamann,U., Chang-Claude,J., Hein,R., Wang-Gohrke,S., Lindblom,A.,
            Margolin,S., Mannermaa,A., Kosma,V.M., Kataja,V., Olson,J.E.,
            Wang,X., Fredericksen,Z., Giles,G.G., Severi,G., Baglietto,L.,
            English,D.R., Hankinson,S.E., Cox,D.G., Kraft,P., Vatten,L.J.,
            Hveem,K., Kumle,M., Sigurdson,A., Doody,M., Bhatti,P.,
            Alexander,B.H., Hooning,M.J., van den Ouweland,A.M.,
            Oldenburg,R.A., Schutte,M., Hall,P., Czene,K., Liu,J., Li,Y.,
            Cox,A., Elliott,G., Brock,I., Reed,M.W., Shen,C.Y., Yu,J.C.,
            Hsu,G.C., Chen,S.T., Anton-Culver,H., Ziogas,A., Andrulis,I.L.,
            Knight,J.A., Beesley,J., Goode,E.L., Couch,F., Chenevix-Trench,G.,
            Hoover,R.N., Ponder,B.A., Hunter,D.J., Pharoah,P.D., Dunning,A.M.,
            Chanock,S.J. and Easton,D.F.
  CONSRTM   SEARCH; GENICA Consortium; kConFab; Australian Ovarian Cancer Study
            Group
  TITLE     Newly discovered breast cancer susceptibility loci on 3p24 and
            17q23.2
  JOURNAL   Nat Genet 41 (5), 585-590 (2009)
   PUBMED   19330027
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Guo,D., Ling,J., Wang,M.H., She,J.X., Gu,J. and Wang,C.Y.
  TITLE     Physical interaction and functional coupling between ACDP4 and the
            intracellular ion chaperone COX11, an implication of the role of
            ACDP4 in essential metal ion transport and homeostasis
  JOURNAL   Mol Pain 1, 15 (2005)
   PUBMED   15840172
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Leary,S.C., Kaufman,B.A., Pellecchia,G., Guercin,G.H., Mattman,A.,
            Jaksch,M. and Shoubridge,E.A.
  TITLE     Human SCO1 and SCO2 have independent, cooperative functions in
            copper delivery to cytochrome c oxidase
  JOURNAL   Hum Mol Genet 13 (17), 1839-1848 (2004)
   PUBMED   15229189
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Hiser,L., Di Valentin,M., Hamer,A.G. and Hosler,J.P.
  TITLE     Cox11p is required for stable formation of the Cu(B) and magnesium
            centers of cytochrome c oxidase
  JOURNAL   J Biol Chem 275 (1), 619-623 (2000)
   PUBMED   10617659
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Petruzzella,V., Tiranti,V., Fernandez,P., Ianna,P., Carrozzo,R. and
            Zeviani,M.
  TITLE     Identification and characterization of human cDNAs specific to
            BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the
            formation and function of the mitochondrial respiratory chain
  JOURNAL   Genomics 54 (3), 494-504 (1998)
   PUBMED   9878253
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF725369.1, AK293851.1,
            BM975167.1 and W33157.1.
            
            Summary: Cytochrome c oxidase (COX), the terminal component of the
            mitochondrial respiratory chain, catalyzes the electron transfer
            from reduced cytochrome c to oxygen. This component is a
            heteromeric complex consisting of 3 catalytic subunits encoded by
            mitochondrial genes and multiple structural subunits encoded by
            nuclear genes. The mitochondrially-encoded subunits function in
            electron transfer, and the nuclear-encoded subunits may function in
            the regulation and assembly of the complex. This nuclear gene
            encodes a protein which is not a structural subunit, but may be a
            heme A biosynthetic enzyme involved in COX formation, according to
            the yeast mutant studies. However, the studies in Rhodobacter
            sphaeroides suggest that this gene is not required for heme A
            biosynthesis, but required for stable formation of the Cu(B) and
            magnesium centers of COX. This human protein is predicted to
            contain a transmembrane domain localized in the mitochondrial inner
            membrane. Multiple transcript variants encoding different isoforms
            have been found for this gene. A related pseudogene has been found
            on chromosome 6. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region resulting in a frameshift, compared to
            variant 1. The resulting isoform (2) has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.83370.1, BQ432122.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..230
                     /product="cytochrome c oxidase assembly protein COX11,
                     mitochondrial isoform 2"
                     /note="cytochrome c oxidase subunit 11; COX11, cytochrome
                     c oxidase copper chaperone; cytochrome c oxidase assembly
                     protein COX11, mitochondrial; COX11 homolog, cytochrome c
                     oxidase assembly protein"
                     /calculated_mol_wt=25722
     Region          62..>216
                     /region_name="CtaG_Cox11"
                     /note="Cytochrome c oxidase assembly protein CtaG/Cox11;
                     cl01240"
                     /db_xref="CDD:470128"
     CDS             1..230
                     /gene="COX11"
                     /gene_synonym="COX11P; MC4DN23"
                     /coded_by="NM_001162861.2:140..832"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:1353"
                     /db_xref="HGNC:HGNC:2261"
                     /db_xref="MIM:603648"
ORIGIN      
        1 mgglwrpgwr cvpfcgwrwi hpgsptraae rvepflrpew sgtggaergl rwlgtwkrcs
       61 lrarhpalqp prrpkssnpf traqeeerrr qnkttltyva avavgmlgas yaavplyrly
      121 cqttglggsa vaghasdkie nmvpvkdrii kisfnadvha slqwnfrpqq teiyvvpget
      181 alafyraknp tdkpvigist ynivpfeagq yfnkiqvlss rlqsctestf
//
LOCUS       NP_001351449             586 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SLU7 isoform b [Homo sapiens].
ACCESSION   NP_001351449 XP_011532720
VERSION     NP_001351449.1
DBSOURCE    REFSEQ: accession NM_001364520.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Rojo,C., Fernandez-Barrena,M.G.,
            Avila,M.A., Arechederra,M. and Berasain,C.
  TITLE     SLU7: A New Hub of Gene Expression Regulation-From Epigenetics to
            Protein Stability in Health and Disease
  JOURNAL   Int J Mol Sci 23 (21), 13411 (2022)
   PUBMED   36362191
  REMARK    GeneRIF: SLU7: A New Hub of Gene Expression Regulation-From
            Epigenetics to Protein Stability in Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Jimenez,M., Elizalde,M., Azkona,M.,
            Uriarte,I., Latasa,M.U., Urtasun,R., Bilbao,I., Sangro,B.,
            Garcia-Ruiz,C., Fernandez-Checa,J.C., Corrales,F.J., Esquivel,A.,
            Pineda-Lucena,A., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     Splicing Factor SLU7 Prevents Oxidative Stress-Mediated Hepatocyte
            Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage
  JOURNAL   Hepatology 74 (5), 2791-2807 (2021)
   PUBMED   34170569
  REMARK    GeneRIF: Splicing Factor SLU7 Prevents Oxidative Stress-Mediated
            Hepatocyte Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Recalde,M., Garate-Rascon,M., Elizalde,M., Azkona,M., Latasa,M.U.,
            Barcena-Varela,M., Sangro,B., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     The splicing regulator SLU7 is required to preserve DNMT1 protein
            stability and DNA methylation
  JOURNAL   Nucleic Acids Res 49 (15), 8592-8609 (2021)
   PUBMED   34331453
  REMARK    GeneRIF: The splicing regulator SLU7 is required to preserve DNMT1
            protein stability and DNA methylation.
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Shomron,N., Reznik,M. and Ast,G.
  TITLE     Splicing factor hSlu7 contains a unique functional domain required
            to retain the protein within the nucleus
  JOURNAL   Mol Biol Cell 15 (8), 3782-3795 (2004)
   PUBMED   15181151
  REMARK    GeneRIF: The zinc-knuckle motif of hSlu7 determines the cellular
            localization of the protein through a nucleocytoplasmic-sensitive
            shuttling balance.
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     An upstream AG determines whether a downstream AG is selected
            during catalytic step II of splicing
  JOURNAL   Mol Cell Biol 21 (5), 1509-1514 (2001)
   PUBMED   11238888
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     The RNA splicing factor hSlu7 is required for correct 3'
            splice-site choice
  JOURNAL   Nature 402 (6758), 207-210 (1999)
   PUBMED   10647016
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     Human step II splicing factor hSlu7 functions in restructuring the
            spliceosome between the catalytic steps of splicing
  JOURNAL   Genes Dev 13 (7), 841-850 (1999)
   PUBMED   10197984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091842.3.
            
            On Jun 20, 2018 this sequence version replaced XP_011532720.1.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is a
            splicing factor that has been found to be essential during the
            second catalytic step in the pre-mRNA splicing process. It
            associates with the spliceosome and contains a zinc knuckle motif
            that is found in other splicing factors and is involved in
            protein-nucleic acid and protein-protein interactions. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4), as well as variants 2, 3, and
            5, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.212019.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..586
                     /product="pre-mRNA-splicing factor SLU7 isoform b"
                     /note="step II splicing factor SLU7; zinc knuckle motif
                     containing; pre-mRNA-splicing factor SLU7; SLU7 splicing
                     factor homolog; SLU7 homolog, splicing factor"
                     /calculated_mol_wt=68256
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          77..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          129..169
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          161..434
                     /region_name="Slu7"
                     /note="Pre-mRNA splicing Prp18-interacting factor;
                     pfam11708"
                     /db_xref="CDD:463326"
     Region          206..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          496..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     CDS             1..586
                     /gene="SLU7"
                     /gene_synonym="9G8; hSlu7"
                     /coded_by="NM_001364520.2:206..1966"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS4352.1"
                     /db_xref="GeneID:10569"
                     /db_xref="HGNC:HGNC:16939"
                     /db_xref="MIM:605974"
ORIGIN      
        1 msatvvdavn aaplsgskem sleepkkmtr edwrkkkele eqrklgnapa evdeegkdin
       61 phipqyissv pwyidpskrp tlkhqrpqpe kqkqfsssge wykrgvkens iitkyrkgac
      121 encgamthkk kdcferprrv gakftgtnia pdehvqpqlm fdydgkrdrw ngynpeehmk
      181 iveeyakvdl akrtlkaqkl qeelasgklv eqanspkhqw geeepnsqme kdhnsedede
      241 dkyaddidmp gqnfdskrri tvrnlrired iakylrnldp nsayydpktr amrenpyana
      301 gknpdevsya gdnfvrytgd tismaqtqlf aweaydkgse vhlqadptkl ellyksfkvk
      361 kedfkeqqke silekyggqe hldappaell laqtedyvey srhgtvikgq eravacskye
      421 edvkihnhth iwgsywkegr wgykcchsff kysyctgeag keivnseeci ineitgeesv
      481 kkpqtlmelh qeklkeekkk kkkkkkkhrk sssdsddeek kheklkkaln aeearllhvk
      541 etmqiderkr pynsmyetre pteeemeayr mkrqrpddpm asflgq
//
LOCUS       NP_056013               1261 aa            linear   PRI 20-NOV-2025
DEFINITION  protein cordon-bleu isoform b [Homo sapiens].
ACCESSION   NP_056013
VERSION     NP_056013.2
DBSOURCE    REFSEQ: accession NM_015198.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1261)
  AUTHORS   Abdul Majeed,S., Dunzendorfer,H., Weiner,J., Heiker,J.T., Kiess,W.,
            Korner,A. and Landgraf,K.
  TITLE     COBL, MKX and MYOC Are Potential Regulators of Brown Adipose Tissue
            Development Associated with Obesity-Related Metabolic Dysfunction
            in Children
  JOURNAL   Int J Mol Sci 24 (4), 3085 (2023)
   PUBMED   36834493
  REMARK    GeneRIF: COBL, MKX and MYOC Are Potential Regulators of Brown
            Adipose Tissue Development Associated with Obesity-Related
            Metabolic Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1261)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1261)
  AUTHORS   Husson,C., Renault,L., Didry,D., Pantaloni,D. and Carlier,M.F.
  TITLE     Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
            filament assembly
  JOURNAL   Mol Cell 43 (3), 464-477 (2011)
   PUBMED   21816349
  REMARK    GeneRIF: Cordon-Bleu works as a dynamizer of actin assembly by
            combining many properties of profilin with weak filament nucleating
            and powerful filament severing activities and sequestration of
            ADP-actin, which generate oscillatory polymerization kinetics.
REFERENCE   7  (residues 1 to 1261)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1261)
  AUTHORS   de Krom,M., Staal,W.G., Ophoff,R.A., Hendriks,J., Buitelaar,J.,
            Franke,B., de Jonge,M.V., Bolton,P., Collier,D., Curran,S., van
            Engeland,H. and van Ree,J.M.
  TITLE     A common variant in DRD3 receptor is associated with autism
            spectrum disorder
  JOURNAL   Biol Psychiatry 65 (7), 625-630 (2009)
   PUBMED   19058789
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1261)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
REFERENCE   10 (residues 1 to 1261)
  AUTHORS   Gasca,S., Hill,D.P., Klingensmith,J. and Rossant,J.
  TITLE     Characterization of a gene trap insertion into a novel gene,
            cordon-bleu, expressed in axial structures of the gastrulating
            mouse embryo
  JOURNAL   Dev Genet 17 (2), 141-154 (1995)
   PUBMED   7586755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC111496.1, AB014533.1,
            DA245843.1, BC045771.1 and AC004414.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 11, 2003 this sequence version replaced NP_056013.1.
            
            Summary: This gene encodes a protein that contains WH2 domains
            (WASP, Wiskott-Aldrich syndrome protein, homology domain-2) that
            interact with actin. The encoded actin regulator protein is
            required for growth and assembly of brush border microvilli that
            play a role in maintaining intestinal homeostasis. A similar
            protein in mouse functions in midbrain neural tube closure. A
            pseudogene of this gene is located on chromosome X. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, and uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. The
            encoded isoform (b) is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150263.1, AB014533.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265136.12/ ENSP00000265136.7
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.1"
     Protein         1..1261
                     /product="protein cordon-bleu isoform b"
                     /note="protein cordon-bleu"
                     /calculated_mol_wt=135486
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5NBX1; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          152..230
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          259..480
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          298..303
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          331..336
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q5NBX1; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          500..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            578
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          580..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          658..699
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          779..843
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            815
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          907..1104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            962
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1099..1131
                     /region_name="WH2_Wa_Cobl"
                     /note="first Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wa) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21799"
                     /db_xref="CDD:409197"
     Site            order(1110,1112..1114,1116..1118,1120,1124,1126..1130)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409197"
     Region          1120..1145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Region          1126..1129
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409197"
     Region          1145..1188
                     /region_name="WH2_Wb_Cobl"
                     /note="second Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wb) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21800"
                     /db_xref="CDD:409198"
     Site            order(1145,1147..1160,1166..1169,1171,1173..1174,
                     1176..1177,1180,1184..1188)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409198"
     Region          1166..1169
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409198"
     Site            1192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1196..1232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            1227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          1233..1258
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1237..1238,1240..1242,1244..1246,1254..1257)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1254..1257
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     CDS             1..1261
                     /gene="COBL"
                     /coded_by="NM_015198.5:177..3962"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34637.1"
                     /db_xref="GeneID:23242"
                     /db_xref="HGNC:HGNC:22199"
                     /db_xref="MIM:610317"
ORIGIN      
        1 mdaprasaak pptgrkmkar appppgkaat lhvhsdqkpp hdgalgsqqn lvrmkealra
       61 stmdvtvvlp sglekrsvln gshammdllv elclqnhlnp shhaleirss etqqplsfkp
      121 ntligtlnvh tvflkekvpe ekvkpgppkv peksvrlvvn ylrtqkavvr vspevplqni
      181 lpvicakcev spehvvllrd niageelels kslnelgike lyawdnrret frksslgnde
      241 tdkekkkflg ffkvnkrsns kgclttpnsp smhsrsltlg pslslgsisg vsvksemkkr
      301 rappppgsgp pvqdkasekv slgsqidlqk kkrrapappp pqppppspli pnrtedkeen
      361 rkstmvslpl gsgshcspdg apqvlseaee tvsvgscfas edttedsgvm sspsdivsld
      421 sqqdsmkykd kwatdqedcs dqdlagtpdl gpqksplwek ngsenshlrt ekavtasnde
      481 edlliagefr ktlaeldedl eemedsyetd tssltssihg asnhcpqdam iphgdtdaip
      541 vtfigevsdd pvdsglfsnr nnnagsfdse gvasrrdsla plqaehsqph ekareevpal
      601 hpashdvgkg irvalsnisk dgnlmetapr vtsfasnlht dnlnakvkdk vygcadgert
      661 qatervnsqp vnekdsndkn aalaptswhq rgqnpgksyr lkhglttyki ippksemrcy
      721 drdvslstga ikidelgnlv sphatgirii slsssvpeae sqpigkvref wrcnsvekhl
      781 grpsessarg ppstpvptqt qnpesrlqad pkpispqqks ahhegrnplg egrnqpptmg
      841 mghvrvpaah ttevtflkpq rrtssqyvas aiakrigapk vhadvvrphg yaekgyagka
      901 pvlaappvtv kddrtssphs etqgwkdgaq wpcvtppnnh gedlavgapp rgevigphrk
      961 lstqdrpaai hrsscfslvq ssqrdrvsvg qscgfsgkqs tssqeassas eprrapdgtd
     1021 pppphtsdtq acsrelvngs vrapghgeps hppggsgtes hillereekp svfstdgnet
     1081 dsiwppsifg pkkkfkpvvq rpvpkdtslh salmeaihsa ggkdrlrkta ehtgegrpak
     1141 lsyteaeger sallaairgh sgtcslrkva ssaseelqsf rdaalsaqgs esplledlgl
     1201 lsppaipppp pppsqalsap rtasrfstgt lsntadarqa lmdairsgtg aarlrkvpll
     1261 v
//
LOCUS       NP_001337615             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337615
VERSION     NP_001337615.1
DBSOURCE    REFSEQ: accession NM_001350686.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (22), as well as variants 1-4,
            9-21, and 23-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.217365.1,
                                           SRR1660809.10568.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350686.1:909..3119"
                     /note="isoform 1 is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_055283                258 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox protein VENTX [Homo sapiens].
ACCESSION   NP_055283
VERSION     NP_055283.1
DBSOURCE    REFSEQ: accession NM_014468.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 258)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 258)
  AUTHORS   Le,Y., Gao,H., Richards,W., Zhao,L., Bleday,R., Clancy,T. and
            Zhu,Z.
  TITLE     VentX expression in tumor-associated macrophages promotes
            phagocytosis and immunity against pancreatic cancers
  JOURNAL   JCI Insight 5 (14), 137088 (2020)
   PUBMED   32573491
  REMARK    GeneRIF: VentX expression in tumor-associated macrophages promotes
            phagocytosis and immunity against pancreatic cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 258)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 258)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 258)
  AUTHORS   Le,Y., Gao,H., Bleday,R. and Zhu,Z.
  TITLE     The homeobox protein VentX reverts immune suppression in the tumor
            microenvironment
  JOURNAL   Nat Commun 9 (1), 2175 (2018)
   PUBMED   29872044
  REMARK    GeneRIF: Findings suggest potential applications of homeobox
            protein VentX (VentX)-regulated tumor-associated macrophages (TAMs)
            in cancer immunotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 258)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 258)
  AUTHORS   Holland,P.W., Booth,H.A. and Bruford,E.A.
  TITLE     Classification and nomenclature of all human homeobox genes
  JOURNAL   BMC Biol 5, 47 (2007)
   PUBMED   17963489
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 258)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 258)
  AUTHORS   Moretti,P.A., Davidson,A.J., Baker,E., Lilley,B., Zon,L.I. and
            D'Andrea,R.J.
  TITLE     Molecular cloning of a human Vent-like homeobox gene
  JOURNAL   Genomics 76 (1-3), 21-29 (2001)
   PUBMED   11549314
REFERENCE   10 (residues 1 to 258)
  AUTHORS   Moreau-Aubry,A., Le Guiner,S., Labarriere,N., Gesnel,M.C.,
            Jotereau,F. and Breathnach,R.
  TITLE     A processed pseudogene codes for a new antigen recognized by a
            CD8(+) T cell clone on melanoma
  JOURNAL   J Exp Med 191 (9), 1617-1624 (2000)
   PUBMED   10790436
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445199.37.
            
            Summary: This gene encodes a member of the Vent family of
            homeodomain proteins. The encoded protein may function as a
            transcriptional repressor and be involved in mesodermal patterning
            and hemopoietic stem cell maintenance. Multiple pseudogenes exist
            for this gene. A transcribed pseudogene located on chromosome X may
            lead to antigen production in certain melanomas. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF068006.1, BC108915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325980.10/ ENSP00000357556.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.3"
     Protein         1..258
                     /product="homeobox protein VENTX"
                     /note="VENT-like homeobox 2; hemopoietic progenitor
                     homeobox protein VENTX2; VENT-like homeobox protein 2;
                     VENT homeobox homolog"
                     /calculated_mol_wt=27421
     Region          1..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95231.1)"
     Region          93..148
                     /region_name="Homeodomain"
                     /note="pfam00046"
                     /db_xref="CDD:459649"
     Region          227..248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95231.1)"
     CDS             1..258
                     /gene="VENTX"
                     /gene_synonym="HPX42B; NA88A; VENTX2"
                     /coded_by="NM_014468.4:61..837"
                     /db_xref="CCDS:CCDS7675.1"
                     /db_xref="GeneID:27287"
                     /db_xref="HGNC:HGNC:13639"
                     /db_xref="MIM:607158"
ORIGIN      
        1 mrlssspprg pqqlssfgsv dwlsqsscsg pthtprpadf slgslpgpgq tsgareppqa
       61 vsikeaagss nlpapertma glskepntlr aprvrtaftm eqvrtlegvf qhhqylsple
      121 rkrlaremql sevqiktwfq nrrmkhkrqm qdpqlhspfs gslhappafy stssglangl
      181 qllcpwapls gpqalmlppg sfwglcqvaq ealasagasc cgqplashpp tpgrpslgpa
      241 lstgprglca mpqtgdaf
//
LOCUS       NP_001335145             511 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform t [Homo sapiens].
ACCESSION   NP_001335145
VERSION     NP_001335145.1
DBSOURCE    REFSEQ: accession NM_001348216.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091103.4, DA664480.1,
            AK096862.1 and BM011452.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (22) contains an alternate exon in
            the 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon, compared to variant 3. The
            resulting isoform (t) is shorter at the N-terminus compared to
            isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.109208.1,
                                           SRR3476690.387360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..511
                     /product="transcription factor 4 isoform t"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=54524
     Region          402..486
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(410,414,416..418,420,425,446..447)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(423..424,427..428,430..431,434,438,448,451,455,458,
                     461..466)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..511
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348216.2:177..1712"
                     /note="isoform t is encoded by transcript variant 22"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mkfkqcrcsd tglccldheg kaevyapsas tadynrdspg ypsskpatst fpssffmqdg
       61 hhssdpwsss sgmnqpgyag mlgnsshipq sssycslhph erlsypshss adinsslppm
      121 stfhrsgtnh ystssctppa ngtdsimanr gsgaagssqt gdalgkalas iyspdhtnns
      181 fssnpstpvg sppslsagta vwsrnggqas sspnyegplh slqsriedrl erlddaihvl
      241 rnhavgpsta mpgghgdmhg iigpshngam gglgsgygtg llsanrhslm vgthredgva
      301 lrgshsllpn qvpvpqlpvq satspdlnpp qdpyrgmppg lqgqsvssgs seiksddegd
      361 enlqdtksse dkkldddkkd iksitrsrss nnddedltpe qkaerekerr mannarerlr
      421 vrdineafke lgrmvqlhlk sdkpqtklli lhqavavils leqqvrernl npkaaclkrr
      481 eeekvssepp plslagphpg mgdasnhmgq m
//
LOCUS       NP_001355639             143 aa            linear   PRI 20-NOV-2025
DEFINITION  core-binding factor subunit beta isoform 6 [Homo sapiens].
ACCESSION   NP_001355639 XP_016879302
VERSION     NP_001355639.1
DBSOURCE    REFSEQ: accession NM_001368710.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Samsa,W.E., Zhang,Z. and Gong,Z.
  TITLE     CBFbeta Regulates RUNX3 ADP-Ribosylation to Mediate Homologous
            Recombination Repair
  JOURNAL   J Cell Physiol 240 (1), e31503 (2025)
   PUBMED   39696918
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Beyltjens,T., Boudin,E., Revencu,N., Boeckx,N., Bertrand,M.,
            Schutz,L., Haack,T.B., Weber,A., Biliouri,E., Vinksel,M.,
            Zagozen,A., Peterlin,B., Pai,S., Telegrafi,A., Henderson,L.B.,
            Ells,C., Turner,L., Wuyts,W., Van Hul,W., Hendrickx,G. and
            Mortier,G.R.
  TITLE     Heterozygous pathogenic variants involving CBFB cause a new
            skeletal disorder resembling cleidocranial dysplasia
  JOURNAL   J Med Genet 60 (5), 498-504 (2023)
   PUBMED   36241386
  REMARK    GeneRIF: Heterozygous pathogenic variants involving CBFB cause a
            new skeletal disorder resembling cleidocranial dysplasia.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Malik,N., Kim,Y.I., Yan,H., Tseng,Y.C., du Bois,W., Ayaz,G.,
            Tran,A.D., Vera-Ramirez,L., Yang,H., Michalowski,A.M., Kruhlak,M.,
            Lee,M., Hunter,K.W. and Huang,J.
  TITLE     Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1280-1298 (2023)
   PUBMED   36799863
  REMARK    GeneRIF: Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer.
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Khan,A.S., Campbell,K.J., Cameron,E.R. and Blyth,K.
  TITLE     The RUNX/CBFbeta Complex in Breast Cancer: A Conundrum of Context
  JOURNAL   Cells 12 (4), 641 (2023)
   PUBMED   36831308
  REMARK    GeneRIF: The RUNX/CFBbeta Complex in Breast Cancer: A Conundrum of
            Context.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Chiba,N., Watanabe,T., Nomura,S., Tanaka,Y., Minowa,M., Niki,M.,
            Kanamaru,R. and Satake,M.
  TITLE     Differentiation dependent expression and distinct subcellular
            localization of the protooncogene product, PEBP2beta/CBFbeta, in
            muscle development
  JOURNAL   Oncogene 14 (21), 2543-2552 (1997)
   PUBMED   9191054
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Liu,P., Seidel,N., Bodine,D., Speck,N., Tarle,S. and Collins,F.S.
  TITLE     Acute myeloid leukemia with Inv (16) produces a chimeric
            transcription factor with a myosin heavy chain tail
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 547-553 (1994)
   PUBMED   7587111
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Liu,P., Tarle,S.A., Hajra,A., Claxton,D.F., Marlton,P.,
            Freedman,M., Siciliano,M.J. and Collins,F.S.
  TITLE     Fusion between transcription factor CBF beta/PEBP2 beta and a
            myosin heavy chain in acute myeloid leukemia
  JOURNAL   Science 261 (5124), 1041-1044 (1993)
   PUBMED   8351518
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Muller,C.W. and Schulz,G.E.
  TITLE     Structure of the complex of adenylate kinase from Escherichia coli
            with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate
  JOURNAL   J Mol Biol 202 (4), 909-912 (1988)
   PUBMED   2845103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009084.9 and AC074143.5.
            
            On Feb 19, 2019 this sequence version replaced XP_016879302.1.
            
            Summary: The protein encoded by this gene is the beta subunit of a
            heterodimeric core-binding transcription factor belonging to the
            PEBP2/CBF transcription factor family which master-regulates a host
            of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis
            (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory
            subunit; it allosterically enhances DNA binding by alpha subunit as
            the complex binds to the core site of various enhancers and
            promoters, including murine leukemia virus, polyomavirus enhancer,
            T-cell receptor enhancers and GM-CSF promoters. Alternative
            splicing generates two mRNA variants, each encoding a distinct
            carboxyl terminus. In some cases, a pericentric inversion of
            chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript
            consisting of the N terminus of core-binding factor beta in a
            fusion with the C-terminal portion of the smooth muscle myosin
            heavy chain 11. This chromosomal rearrangement is associated with
            acute myeloid leukemia of the M4Eo subtype. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: Variants 5 and 6 encode isoforms that are the
            same length, but have distinct protein sequences.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2002158.1,
                                           SRR14038192.3389605.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..143
                     /product="core-binding factor subunit beta isoform 6"
                     /note="SL3/AKV core-binding factor beta subunit;
                     polyomavirus enhancer binding protein 2, beta subunit;
                     SL3-3 enhancer factor 1 beta subunit; CBF-beta; PEA2-beta;
                     PEBP2-beta; SL3-3 enhancer factor 1 subunit beta"
                     /calculated_mol_wt=16884
     Region          1..128
                     /region_name="CBF_beta"
                     /note="Core binding factor beta subunit; pfam02312"
                     /db_xref="CDD:396750"
     CDS             1..143
                     /gene="CBFB"
                     /gene_synonym="CLCD2; PEBP2B"
                     /coded_by="NM_001368710.1:260..691"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:865"
                     /db_xref="HGNC:HGNC:1539"
                     /db_xref="MIM:121360"
ORIGIN      
        1 mprvvpdqrs kfeneeffrk lsreceikyt gfrdrpheer qarfqnacrd grseiafvat
       61 gtnlslqffp aswqgeqrqt psreyvdler eagkqedala qqafeearrr trefedrdrs
      121 hreemevrvs qllavtgkkt trp
//
LOCUS       NP_001679                256 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP synthase peripheral stalk subunit b, mitochondrial precursor
            [Homo sapiens].
ACCESSION   NP_001679
VERSION     NP_001679.2
DBSOURCE    REFSEQ: accession NM_001688.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Houstek,J., Andersson,U., Tvrdik,P., Nedergaard,J. and Cannon,B.
  TITLE     The expression of subunit c correlates with and thus may limit the
            biosynthesis of the mitochondrial F0F1-ATPase in brown adipose
            tissue
  JOURNAL   J Biol Chem 270 (13), 7689-7694 (1995)
   PUBMED   7706317
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Higuti,T., Tsurumi,C., Osaka,F., Kawamura,Y., Tsujita,H.,
            Yoshihara,Y., Tani,I., Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning of cDNA for the import precursor of human subunit
            B of H(+)-ATP synthase in mitochondria
  JOURNAL   Biochem Biophys Res Commun 178 (3), 1014-1020 (1991)
   PUBMED   1831354
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF237506.1, AL390195.10,
            AW778751.1 and AI754631.1.
            
            On Jun 10, 2002 this sequence version replaced NP_001679.1.
            
            Summary: This gene encodes a subunit of mitochondrial ATP synthase.
            Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an
            electrochemical gradient of protons across the inner membrane
            during oxidative phosphorylation. ATP synthase is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, comprising the proton channel.
            The catalytic portion of mitochondrial ATP synthase consists of 5
            different subunits (alpha, beta, gamma, delta, and epsilon)
            assembled with a stoichiometry of 3 alpha, 3 beta, and a single
            representative of the other 3. The proton channel seems to have
            nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes
            the b subunit of the proton channel. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291077.1, SRR14038191.3597740.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000369722.8/
                                                  ENSP00000358737.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..256
                     /product="ATP synthase peripheral stalk subunit b,
                     mitochondrial precursor"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit B1; ATP synthase, H+ transporting,
                     mitochondrial F0 complex, subunit b; ATP synthase
                     peripheral stalk subunit b, mitochondrial; ATP synthase B
                     chain, mitochondrial; H+-ATP synthase subunit b; ATP
                     synthase F(0) complex subunit B1, mitochondrial; ATP
                     synthase subunit b, mitochondrial; cell
                     proliferation-inducing protein 47; ATP synthase, H+
                     transporting, mitochondrial Fo complex subunit B1; ATPase
                     subunit b; ATP synthase proton-transporting mitochondrial
                     F(0) complex subunit B1"
                     /calculated_mol_wt=24626
     transit_peptide 1..42
                     /calculated_mol_wt=4301
     mat_peptide     43..256
                     /product="ATP synthase peripheral stalk subunit b,
                     mitochondrial"
                     /calculated_mol_wt=24626
     Region          83..244
                     /region_name="Mt_ATP-synt_B"
                     /note="Mitochondrial ATP synthase B chain precursor
                     (ATP-synt_B); pfam05405"
                     /db_xref="CDD:368426"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQQ7; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     Site            154
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQQ7; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     Site            162
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQQ7; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQQ7; propagated from
                     UniProtKB/Swiss-Prot (P24539.2)"
     CDS             1..256
                     /gene="ATP5PB"
                     /gene_synonym="ATP5F1; PIG47"
                     /coded_by="NM_001688.5:79..849"
                     /db_xref="CCDS:CCDS836.1"
                     /db_xref="GeneID:515"
                     /db_xref="HGNC:HGNC:840"
                     /db_xref="MIM:603270"
ORIGIN      
        1 mlsrvvlsaa ataapslkna aflgpgvlqa trtfhtgqph lvpvpplpey ggkvryglip
       61 eeffqflypk tgvtgpyvlg tglilyalsk eiyvisaetf talsvlgvmv ygikkygpfv
      121 adfadklneq klaqleeakq asiqhiqnai dteksqqalv qkrhylfdvq rnniamalev
      181 tyrerlyrvy kevknrldyh isvqnmmrrk eqehminwve khvvqsistq qeketiakci
      241 adlkllakka qaqpvm
//
LOCUS       NP_036218                886 aa            linear   PRI 20-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_036218
VERSION     NP_036218.1
DBSOURCE    REFSEQ: accession NM_012086.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 886)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 886)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 886)
  AUTHORS   Huang,S., Chen,J., Wang,H., Sun,B., Wang,H., Zhang,Z., Zhang,X. and
            Chen,Z.
  TITLE     Influenza A virus matrix protein 1 interacts with hTFIIIC102-s, a
            short isoform of the polypeptide 3 subunit of human general
            transcription factor IIIC
  JOURNAL   Arch Virol 154 (7), 1101-1110 (2009)
   PUBMED   19521658
REFERENCE   4  (residues 1 to 886)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   5  (residues 1 to 886)
  AUTHORS   Koch,H.B., Zhang,R., Verdoodt,B., Bailey,A., Zhang,C.D., Yates,J.R.
            3rd, Menssen,A. and Hermeking,H.
  TITLE     Large-scale identification of c-MYC-associated proteins using a
            combined TAP/MudPIT approach
  JOURNAL   Cell Cycle 6 (2), 205-217 (2007)
   PUBMED   17314511
REFERENCE   6  (residues 1 to 886)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   7  (residues 1 to 886)
  AUTHORS   Zhan,Y., Hegde,R., Srinivasula,S.M., Fernandes-Alnemri,T. and
            Alnemri,E.S.
  TITLE     Death effector domain-containing proteins DEDD and FLAME-3 form
            nuclear complexes with the TFIIIC102 subunit of human transcription
            factor IIIC
  JOURNAL   Cell Death Differ 9 (4), 439-447 (2002)
   PUBMED   11965497
  REMARK    GeneRIF: DEDD and FLAME-3 form nuclear complexes with TFIIIC102
REFERENCE   8  (residues 1 to 886)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   9  (residues 1 to 886)
  AUTHORS   Behar,G., Coleclough,C., Houlgatte,R., Auffray,C. and Lefkovits,I.
  TITLE     Human lymphocyte cDNA ordered library analyzed by 2D gel
            electrophoresis. 3. Analysis of individual clones
  JOURNAL   Appl Theor Electrophor 5 (2), 99-105 (1995)
   PUBMED   8573604
REFERENCE   10 (residues 1 to 886)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314718.1 and AC012486.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is part of the TFIIIC2
            complex, which binds to the promoters of small nuclear and
            cytoplasmic RNA genes in order to recruit RNA polymerase III. The
            TFIIIC2 complex is composed of six subunits. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.87922.1,
                                           SRR1803614.88328.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263956.8/ ENSP00000263956.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..886
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..886
                     /product="general transcription factor 3C polypeptide 3
                     isoform 1"
                     /note="general transcription factor 3C polypeptide 3;
                     TF3C-gamma; TFIIIC 102 kDa subunit; transcription factor
                     IIIC subunit gamma; general transcription factor IIIC,
                     polypeptide 3, 102kDa"
                     /calculated_mol_wt=101142
     Region          1..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          <146..351
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          149..182
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          152..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          183..216
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          183..211
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(184,187..188,191..192,194,218,221..222,225..226,
                     228..229,252,255..256,259..260,263)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          216..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          217..250
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          251..278
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          252..284
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          286..316
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..323
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          326..361
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          408..>514
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          421..454
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            order(422,425..426,429..430,432,457,460..461,464..465,
                     467..468,491,494..495,498..499,502)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          422..449
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          454..485
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          456..489
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          490..514
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          491..523
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          729..>842
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          733..766
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            order(741..742,744,768,771..772,775,778,780..781,812,
                     815..816,819..820,823)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          766..806
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          811..844
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          811..839
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          845..880
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..886
                     /gene="GTF3C3"
                     /gene_synonym="NEDFBS; TFIIIC102; TFiiiC2-102;
                     TFIIICgamma"
                     /coded_by="NM_012086.5:73..2733"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2316.1"
                     /db_xref="GeneID:9330"
                     /db_xref="HGNC:HGNC:4666"
                     /db_xref="MIM:604888"
ORIGIN      
        1 msgfspelid ylegkisfee ferrreerkt rekkslqekg klsaeenpdd sevpsssgin
       61 stksqdkdvn egetsdgvrk svhkvfasml geneddeeee eeeeeeeeee etpeqptagd
      121 vfvlemvlnr etkkmmkekr prsklpralr glmgeanirf argereeail mcmeiirqap
      181 layepfstla miyedqgdme kslqfeliaa hlnpsdteew vrlaemsleq dnikqaifcy
      241 tkalkyeptn vrylwerssl yeqmgdhkma mdgyrrilnl lspsdgerfm qlardmaksy
      301 yeandvtsai niideafskh qglvsmedvn iaaelyisnk qydkaleiit dfsgivlekk
      361 tseegtseen kapenvtcti pdgvpiditv klmvclvhln ileplnpllt tlveqnpedm
      421 gdlyldvaea fldvgeynsa lpllsalvcs erynlavvwl rhaeclkalg ymeraaesyg
      481 kvvdlaplhl darislstlq qqlgqpekal ealepmydpd tlaqdanaaq qelklllhrs
      541 tllfsqgkmy gyvdtlltml amllkvamnr aqvclisssk sgerhlylik vsrdkisdsn
      601 dqesancdak aifavltsvl tkddwwnlll kaiyslcdls rfqeaellvd ssleyysfyd
      661 drqkrkeley fglsaaildk nfrkaynyir imvmenvnkp qlwnifnqvt mhsqdvrhhr
      721 fclrlmlknp enhalcvlng hnafvsgsfk halgqyvqaf rthpdeplys fcigltfihm
      781 asqkyvlrrh alivqgfsfl nrylslrgpc qesfynlgrg lhqlglihla ihyyqkalel
      841 pplvvegiel dqldlrrdia ynlsliyqss gntgmaqtll ytycsi
//
LOCUS       NP_001308374             208 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane emp24 domain-containing protein 2 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001308374 XP_005253601
VERSION     NP_001308374.1
DBSOURCE    REFSEQ: accession NM_001321445.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Sun,C., Zhang,Y., Wang,Z., Chen,J., Zhang,J. and Gu,Y.
  TITLE     TMED2 promotes glioma tumorigenesis by being involved in EGFR
            recycling transport
  JOURNAL   Int J Biol Macromol 262 (Pt 2), 130055 (2024)
   PUBMED   38354922
  REMARK    GeneRIF: TMED2 promotes glioma tumorigenesis by being involved in
            EGFR recycling transport.
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Liang,C., Zhang,H.Y., Wang,Y.Q., Yang,L.A., Du,Y.S., Luo,Y.,
            Zhang,T.C. and Xu,Y.
  TITLE     TMED2 Induces Cisplatin Resistance in Breast Cancer via Targeting
            the KEAP1-Nrf2 Pathway
  JOURNAL   Curr Med Sci 43 (5), 1023-1032 (2023)
   PUBMED   37615927
  REMARK    GeneRIF: TMED2 Induces Cisplatin Resistance in Breast Cancer via
            Targeting the KEAP1-Nrf2 Pathway.
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Goldberg,J.
  TITLE     Decoding of sorting signals by coatomer through a GTPase switch in
            the COPI coat complex
  JOURNAL   Cell 100 (6), 671-679 (2000)
   PUBMED   10761932
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Fullekrug,J., Suganuma,T., Tang,B.L., Hong,W., Storrie,B. and
            Nilsson,T.
  TITLE     Localization and recycling of gp27 (hp24gamma3): complex formation
            with other p24 family members
  JOURNAL   Mol Biol Cell 10 (6), 1939-1955 (1999)
   PUBMED   10359607
REFERENCE   8  (residues 1 to 208)
  AUTHORS   Gommel,D., Orci,L., Emig,E.M., Hannah,M.J., Ravazzola,M.,
            Nickel,W., Helms,J.B., Wieland,F.T. and Sohn,K.
  TITLE     p24 and p23, the major transmembrane proteins of COPI-coated
            transport vesicles, form hetero-oligomeric complexes and cycle
            between the organelles of the early secretory pathway
  JOURNAL   FEBS Lett 447 (2-3), 179-185 (1999)
   PUBMED   10214941
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Fiedler,K., Veit,M., Stamnes,M.A. and Rothman,J.E.
  TITLE     Bimodal interaction of coatomer with the p24 family of putative
            cargo receptors
  JOURNAL   Science 273 (5280), 1396-1399 (1996)
   PUBMED   8703076
REFERENCE   10 (residues 1 to 208)
  AUTHORS   Blum,R., Feick,P., Puype,M., Vandekerckhove,J., Klengel,R.,
            Nastainczyk,W. and Schulz,I.
  TITLE     Tmp21 and p24A, two type I proteins enriched in pancreatic
            microsomal membranes, are members of a protein family involved in
            vesicular trafficking
  JOURNAL   J Biol Chem 271 (29), 17183-17189 (1996)
   PUBMED   8663407
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP226125.1, BI086507.1, DA559763.1, BC025957.1, CA445272.1,
            AI954929.1 and AC055713.29.
            
            On Mar 25, 2016 this sequence version replaced XP_005253601.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.278828.1,
                                           SRR1803615.26940.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..208
                     /product="transmembrane emp24 domain-containing protein 2
                     isoform 2 precursor"
                     /note="coated vesicle membrane protein; membrane protein
                     p24A; p24 family protein beta-1; transmembrane emp24
                     domain trafficking protein 2"
                     /calculated_mol_wt=21470
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1999
     Region          20..203
                     /region_name="EMP24_GP25L"
                     /note="emp24/gp25L/p24 family/GOLD; pfam01105"
                     /db_xref="CDD:426051"
     CDS             1..208
                     /gene="TMED2"
                     /gene_synonym="p24; P24A; p24b1; p24beta1; RNP24"
                     /coded_by="NM_001321445.2:86..712"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:10959"
                     /db_xref="HGNC:HGNC:16996"
                     /db_xref="MIM:619642"
ORIGIN      
        1 mvtlaellvl laallatvsg yfvsidahae ecffervtsg tkmglifeva eggfldidve
       61 itgpdnkgiy kgdressgky tfaahmdgty kfcfsnrmst mtpkivmfti digeapkgqd
      121 metegggdtw dahqnkleem inelavamta vkheqeymev rerihraind ntnsrvvlws
      181 ffealvlvam tlgqiyylkr ffevrrvv
//
LOCUS       NP_612144                740 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase DTX3L [Homo sapiens].
ACCESSION   NP_612144
VERSION     NP_612144.1
DBSOURCE    REFSEQ: accession NM_138287.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Zhu,K., Chatrin,C., Suskiewicz,M.J., Aucagne,V., Foster,B.,
            Kessler,B.M., Gibbs-Seymour,I., Ahel,D. and Ahel,I.
  TITLE     Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L
  JOURNAL   EMBO Rep 25 (10), 4172-4189 (2024)
   PUBMED   39242775
  REMARK    GeneRIF: Ubiquitylation of nucleic acids by DELTEX ubiquitin E3
            ligase DTX3L.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Chen,L., Niu,W., Zang,H. and Qiu,Y.
  TITLE     DTX3L Accelerates Pancreatic cancer Progression via FAK/PI3K/AKT
            Axis
  JOURNAL   Biochem Genet 62 (2), 814-830 (2024)
   PUBMED   37460862
  REMARK    GeneRIF: DTX3L Accelerates Pancreatic cancer Progression via
            FAK/PI3K/AKT Axis.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Zhu,K., Suskiewicz,M.J., Chatrin,C., Stromland,O., Dorsey,B.W.,
            Aucagne,V., Ahel,D. and Ahel,I.
  TITLE     DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic
            acids
  JOURNAL   Nucleic Acids Res 52 (2), 801-815 (2024)
   PUBMED   38000390
  REMARK    GeneRIF: DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on
            nucleic acids.
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Lin,S.
  TITLE     DTX3L mediated ubiquitination of cGAS suppresses antitumor immunity
            in pancreatic cancer
  JOURNAL   Biochem Biophys Res Commun 681, 106-110 (2023)
   PUBMED   37774567
  REMARK    GeneRIF: DTX3L mediated ubiquitination of cGAS suppresses antitumor
            immunity in pancreatic cancer.
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Yan,Q., Dutt,S., Xu,R., Graves,K., Juszczynski,P., Manis,J.P. and
            Shipp,M.A.
  TITLE     BBAP monoubiquitylates histone H4 at lysine 91 and selectively
            modulates the DNA damage response
  JOURNAL   Mol Cell 36 (1), 110-120 (2009)
   PUBMED   19818714
  REMARK    GeneRIF: Data directly implicate BBAP in the monoubiquitylation and
            additional posttranslational modification of histone H4 and an
            associated DNA damage response.
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Wilting,S.M., de Wilde,J., Meijer,C.J., Berkhof,J., Yi,Y., van
            Wieringen,W.N., Braakhuis,B.J., Meijer,G.A., Ylstra,B.,
            Snijders,P.J. and Steenbergen,R.D.
  TITLE     Integrated genomic and transcriptional profiling identifies
            chromosomal loci with altered gene expression in cervical cancer
  JOURNAL   Genes Chromosomes Cancer 47 (10), 890-905 (2008)
   PUBMED   18618715
  REMARK    GeneRIF: Overexpression of DTX3L, PIK3R4, ATP2C1, and SLC25A36, all
            located at 3q21.1-23 are associated with cervical cancer.
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Juszczynski,P., Kutok,J.L., Li,C., Mitra,J., Aguiar,R.C. and
            Shipp,M.A.
  TITLE     BAL1 and BBAP are regulated by a gamma interferon-responsive
            bidirectional promoter and are overexpressed in diffuse large
            B-cell lymphomas with a prominent inflammatory infiltrate
  JOURNAL   Mol Cell Biol 26 (14), 5348-5359 (2006)
   PUBMED   16809771
  REMARK    GeneRIF: BAL1 and BBAP are located on chromosome 3q21 in a
            head-to-head orientation and are regulated by a
            IFN-gamma-responsive bidirectional promoter.
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Takeyama,K., Aguiar,R.C., Gu,L., He,C., Freeman,G.J., Kutok,J.L.,
            Aster,J.C. and Shipp,M.A.
  TITLE     The BAL-binding protein BBAP and related Deltex family members
            exhibit ubiquitin-protein isopeptide ligase activity
  JOURNAL   J Biol Chem 278 (24), 21930-21937 (2003)
   PUBMED   12670957
  REMARK    GeneRIF: It is reported that BBAP and the human family of DTX
            proteins (DTX1, DTX2, and DTX3) function as E3 ligases based on
            their capacity for self-ubiquitination.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092908.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK125086.1, SRR1803614.119827.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296161.9/ ENSP00000296161.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..740
                     /product="E3 ubiquitin-protein ligase DTX3L"
                     /EC_number="2.3.2.27"
                     /note="B-lymphoma- and BAL-associated protein; rhysin2;
                     rhysin-2; deltex 3-like; deltex 3 like, E3 ubiquitin
                     ligase; RING-type E3 ubiquitin transferase DTX3L"
                     /calculated_mol_wt=83424
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Region          8..87
                     /region_name="RRM1_PAR14"
                     /note="RNA recognition motif 1 in vertebrate poly
                     [ADP-ribose] polymerase 14 (PARP-14); cd12300"
                     /db_xref="CDD:409741"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Region          96..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Region          195..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Region          524..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TDB6.1)"
     Region          556..611
                     /region_name="RING-HC_DTX3L"
                     /note="RING finger, HC subclass, found in protein
                     Deltex-3-like (DTX3L) and similar proteins; cd16712"
                     /db_xref="CDD:438372"
     Region          607..739
                     /region_name="DTC"
                     /note="Deltex C-terminal domain; pfam18102"
                     /db_xref="CDD:465650"
     Site            order(616..620,622,634,636,638..640,659..661,663,697,
                     710..711,719)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:193607"
     CDS             1..740
                     /gene="DTX3L"
                     /gene_synonym="BBAP; RNF143"
                     /coded_by="NM_138287.3:90..2312"
                     /db_xref="CCDS:CCDS3015.1"
                     /db_xref="GeneID:151636"
                     /db_xref="HGNC:HGNC:30323"
                     /db_xref="MIM:613143"
ORIGIN      
        1 mashlrppsp llvrvyksgp rvrrklesyf qsskssggge ctvstqehea pgtfrvefse
       61 raakervlkk gehqilvdek pvpiflvpte nsikkntrpq issltqsqae tpsgdmhqhe
      121 ghipnavdsc lqkifltvta dlncnlfske qrayittlcp sirkmeghdg iekvcgdfqd
      181 ierihqflse qfleseqkqq fspsmterkp lsqqerdsci spsepetkae qksnyfevpl
      241 pyfeyfkyic pdkinsiekr fgvnieiqes spnmvcldft ssrsgdleaa resfasefqk
      301 nteplkqecv sladskqank fkqelnhqft kllikekgge ltllgtqddi saakqkisea
      361 fvkipvklfa anymmnviev dsahykllet ellqeiseie krydicskvs ekgqktcilf
      421 eskdrqvdls vhayasfida fqhascqlmr evlllkslgk erkhlhqtkf addfrkrhpn
      481 vhfvlnqesm tltglpnhla kakqyvlkgg gmsslagkkl keghetpmdi dsddskaasp
      541 plkgsvssea seldkkekgi cvicmdtisn kkvlpkckhe fcapcinkam sykpicptcq
      601 tsygiqkgnq pegsmvftvs rdslpgyesf gtivitysmk agiqteehpn pgkrypgiqr
      661 taylpdnkeg rkvlkllyra fdqkliftvg ysrvlgvsdv itwndihhkt srfggpemyg
      721 ypdpsylkrv keelkakgie
//
LOCUS       NP_054774                676 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 81 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_054774
VERSION     NP_054774.2
DBSOURCE    REFSEQ: accession NM_014055.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Zhou,Z., Qiu,H., Castro-Araya,R.F., Takei,R., Nakayama,K. and
            Katoh,Y.
  TITLE     Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome
  JOURNAL   Hum Mol Genet 31 (10), 1681-1693 (2022)
   PUBMED   34888642
  REMARK    GeneRIF: Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome.
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Perrault,I., Halbritter,J., Porath,J.D., Gerard,X., Braun,D.A.,
            Gee,H.Y., Fathy,H.M., Saunier,S., Cormier-Daire,V., Thomas,S.,
            Attie-Bitach,T., Boddaert,N., Taschner,M., Schueler,M.,
            Lorentzen,E., Lifton,R.P., Lawson,J.A., Garfa-Traore,M., Otto,E.A.,
            Bastin,P., Caillaud,C., Kaplan,J., Rozet,J.M. and Hildebrandt,F.
  TITLE     IFT81, encoding an IFT-B core protein, as a very rare cause of a
            ciliopathy phenotype
  JOURNAL   J Med Genet 52 (10), 657-665 (2015)
   PUBMED   26275418
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Bhogaraju,S., Cajanek,L., Fort,C., Blisnick,T., Weber,K.,
            Taschner,M., Mizuno,N., Lamla,S., Bastin,P., Nigg,E.A. and
            Lorentzen,E.
  TITLE     Molecular basis of tubulin transport within the cilium by IFT74 and
            IFT81
  JOURNAL   Science 341 (6149), 1009-1012 (2013)
   PUBMED   23990561
  REMARK    GeneRIF: this study found that the two core intraflagellar
            transport proteins IFT74 and IFT81 form a tubulin-binding module
            and mapped the interaction to a calponin homology domain of IFT81
            and a highly basic domain in IFT74.
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Peng,J., Yu,L., Horiuchi,M., Zhang,P., Huang,X., Zhang,Y., Li,D.,
            Jalil,M.A. and Zhao,S.
  TITLE     Identification of human CDV-1R and mouse Cdv-1R, two novel proteins
            with putative signal peptides, especially highly expressed in
            testis and increased with the male sex maturation
  JOURNAL   Mol Biol Rep 29 (4), 353-362 (2002)
   PUBMED   12549821
  REMARK    GeneRIF: inconsistent expression levels of human CDV-1 and mouse
            Cdv-1 in heart implied that cardiac hypertrophy in human SCD might
            not be associated with the abnormal expression of CDV-1
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Higashi,M., Kobayashi,K., Iijima,M., Wakana,S., Horiuchi,M.,
            Yasuda,T., Yoshida,G., Kanmura,Y. and Saheki,T.
  TITLE     Genomic organization and mapping of mouse CDV (carnitine
            deficiency-associated gene expressed in ventricle)-1 and its
            related CDV-1R gene
  JOURNAL   Mamm Genome 11 (12), 1053-1057 (2000)
   PUBMED   11130971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP351086.1 and AF332010.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 11, 2003 this sequence version replaced NP_054774.1.
            
            Summary: The protein encoded by this gene, together with IFT74,
            forms a tubulin-binding module of intraflagellar transport complex
            B. This module is involved in transport of tubulin within the
            cilium, and the encoded protein is required for ciliogenesis.
            Mutations in this gene are a cause of short-rib polydactyly
            syndromes. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1 and 3
            both encode isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.222467.1, AF332010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242591.10/ ENSP00000242591.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..676
                     /product="intraflagellar transport protein 81 homolog
                     isoform 1"
                     /note="carnitine deficiency-associated gene expressed in
                     ventricle 1; intraflagellar transport protein 81 homolog;
                     carnitine deficiency-associated protein expressed in
                     ventricle 1"
                     /calculated_mol_wt=79615
     Region          2..121
                     /region_name="CH (calponin-homology)-like region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Region          3..126
                     /region_name="IFT81_CH"
                     /note="Intraflagellar transport 81 calponin homology
                     domain; pfam18383"
                     /db_xref="CDD:465736"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Region          <138..672
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     CDS             1..676
                     /gene="IFT81"
                     /gene_synonym="CDV-1; CDV-1R; CDV1; CDV1R; DV1; SRTD19"
                     /coded_by="NM_014055.4:527..2557"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41831.1"
                     /db_xref="GeneID:28981"
                     /db_xref="HGNC:HGNC:14313"
                     /db_xref="MIM:605489"
ORIGIN      
        1 msdqikfimd slnkepfrkn ynlitfdsle pmqllqvlsd vlaeidpkql vdireempeq
       61 takrmlsllg ilkykpsgna tdmstfrqgl vigskpviyp vlhwllqrtn elkkraylar
      121 fliklevpse flqdetvadt nkqyeelmea fktlhkeyeq lkisgfstae irkdisamee
      181 ekdqlikrve hlkkrvetaq nhqwmlkiar qlrvekeree ylaqqkqeqk nqlfhavqrl
      241 qrvqnqlksm rqaaadakpe slmkrleeei kfnlymvtek fpkelenkkk elhflqkvvs
      301 epamghsdll eleskinein teinqliekk mmrnepiegk lslyrqqasi isrkkeakae
      361 elqeakekla slereasvkr nqtrefdgte vlkgdefkry vnklrskstv fkkkhqiiae
      421 lkaefgllqr teellkqrhe niqqqlqtme ekkgisgysy tqeelervsa lksevdemkg
      481 rtlddmsemv kklyslvsek ksalasvike lrqlrqkyqe ltqecdekks qydscaagle
      541 snrskleqev rrlreeclqe esryhytncm iknlevqlrr atdemkayis sdqqekrkai
      601 reqytkntae qenlgkklre kqkvireshg pnmkqakmwr dleqlmeckk qcflkqqsqt
      661 sigqviqegg edrlil
//
LOCUS       NP_001269978            1012 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 8 isoform b [Homo sapiens].
ACCESSION   NP_001269978 XP_005254833
VERSION     NP_001269978.1
DBSOURCE    REFSEQ: accession NM_001283049.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Caba,C., Black,M., Liu,Y., DaDalt,A.A., Mallare,J., Fan,L.,
            Harding,R.J., Wang,Y.X., Vacratsis,P.O., Huang,R., Zhuang,Z. and
            Tong,Y.
  TITLE     Autoinhibition of ubiquitin-specific protease 8: Insights into
            domain interactions and mechanisms of regulation
  JOURNAL   J Biol Chem 300 (10), 107727 (2024)
   PUBMED   39214302
  REMARK    GeneRIF: Autoinhibition of ubiquitin-specific protease 8: Insights
            into domain interactions and mechanisms of regulation.
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Miao,H., Wang,L., Gong,F., Duan,L., Wang,L., Yao,Y., Feng,M.,
            Deng,K., Wang,R., Xiao,Y., Ling,Q., Zhu,H. and Lu,L.
  TITLE     A long-term prognosis study of human USP8-mutated ACTH-secreting
            pituitary neuroendocrine tumours
  JOURNAL   Clin Endocrinol (Oxf) 101 (1), 32-41 (2024)
   PUBMED   38691659
  REMARK    GeneRIF: A long-term prognosis study of human USP8-mutated
            ACTH-secreting pituitary neuroendocrine tumours.
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Xia,R., Jia,H., Fan,J., Liu,Y. and Jia,J.
  TITLE     USP8 promotes smoothened signaling by preventing its ubiquitination
            and changing its subcellular localization
  JOURNAL   PLoS Biol 10 (1), e1001238 (2012)
   PUBMED   22253573
  REMARK    GeneRIF: USP8 is a positive regulator in Hh signaling by
            down-regulating Smo ubiquitination and thereby mediating Smo
            intracellular trafficking.
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Wright,M.H., Berlin,I. and Nash,P.D.
  TITLE     Regulation of endocytic sorting by ESCRT-DUB-mediated
            deubiquitination
  JOURNAL   Cell Biochem Biophys 60 (1-2), 39-46 (2011)
   PUBMED   21448666
  REMARK    GeneRIF: Studies indicate that USP8/Ubpy and AMSH interact with
            ESCRT components to modulate the ubiquitination status of receptors
            and relevant sorting proteins.
            Review article
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Berlin,I., Higginbotham,K.M., Dise,R.S., Sierra,M.I. and Nash,P.D.
  TITLE     The deubiquitinating enzyme USP8 promotes trafficking and
            degradation of the chemokine receptor 4 at the sorting endosome
  JOURNAL   J Biol Chem 285 (48), 37895-37908 (2010)
   PUBMED   20876529
  REMARK    GeneRIF: USP8 promotes trafficking and degradation of CXCR4 at the
            sorting endosome.
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Mizuno,E., Kobayashi,K., Yamamoto,A., Kitamura,N. and Komada,M.
  TITLE     A deubiquitinating enzyme UBPY regulates the level of protein
            ubiquitination on endosomes
  JOURNAL   Traffic 7 (8), 1017-1031 (2006)
   PUBMED   16771824
  REMARK    GeneRIF: UBPY regulates the level of protein ubiquitination on
            endosomes, which is required for maintaining the morphology of the
            organelle
REFERENCE   8  (residues 1 to 1012)
  AUTHORS   Naviglio,S., Mattecucci,C., Matoskova,B., Nagase,T., Nomura,N., Di
            Fiore,P.P. and Draetta,G.F.
  TITLE     UBPY: a growth-regulated human ubiquitin isopeptidase
  JOURNAL   EMBO J 17 (12), 3241-3250 (1998)
   PUBMED   9628861
REFERENCE   9  (residues 1 to 1012)
  AUTHORS   Janssen,J.W., Schleithoff,L., Bartram,C.R. and Schulz,A.S.
  TITLE     An oncogenic fusion product of the phosphatidylinositol 3-kinase
            p85beta subunit and HUMORF8, a putative deubiquitinating enzyme
  JOURNAL   Oncogene 16 (13), 1767-1772 (1998)
   PUBMED   9582025
REFERENCE   10 (residues 1 to 1012)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296480.1, D29956.1,
            AC012170.6, BM751645.1, AA399951.1, AA399952.1 and AI276208.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005254833.1.
            
            Summary: This gene encodes a protein that belongs to the
            ubiquitin-specific processing protease family of proteins. The
            encoded protein is thought to regulate the morphology of the
            endosome by ubiquitination of proteins on this organelle and is
            involved in cargo sorting and membrane trafficking at the early
            endosome stage. This protein is required for the cell to enter the
            S phase of the cell cycle and also functions as a positive
            regulator in the Hedgehog signaling pathway in development.
            Pseudogenes of this gene are present on chromosomes 2 and 6.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (4) lacks three in-frame exons in
            the coding region compared to variant 1. The encoded isoform (b) is
            shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296480.1, SRR14038193.3017603.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..1012
                     /product="ubiquitin carboxyl-terminal hydrolase 8 isoform
                     b"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin carboxyl-terminal hydrolase 8; ubiquitin
                     isopeptidase Y; deubiquitinating enzyme 8;
                     ubiquitin-specific-processing protease 8; ubiquitin
                     thiolesterase 8"
                     /calculated_mol_wt=114949
     Region          115..227
                     /region_name="Rhodanese"
                     /note="Rhodanese-like domain; pfam00581"
                     /db_xref="CDD:425764"
     Region          298..>470
                     /region_name="tolA_full"
                     /note="TolA protein; TIGR02794"
                     /db_xref="CDD:274303"
     Region          671..1000
                     /region_name="UCH"
                     /note="Ubiquitin carboxyl-terminal hydrolase; pfam00443"
                     /db_xref="CDD:425685"
     Site            order(675,680,961,979)
                     /site_type="active"
                     /db_xref="CDD:239139"
     CDS             1..1012
                     /gene="USP8"
                     /gene_synonym="HumORF8; PITA4; SPG59; UBPY"
                     /coded_by="NM_001283049.2:176..3214"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61632.1"
                     /db_xref="GeneID:9101"
                     /db_xref="HGNC:HGNC:12631"
                     /db_xref="MIM:603158"
ORIGIN      
        1 mpavasvpke lylssslkdl nkktevkpek istkryeeae vrkkleekdr qeeaqrlqqk
       61 rqetgredgg tlakgslenv ldskdktqks ngeknekcet kekgaitake lytmmtdkni
      121 sliimdarrm qdyqdscilh slsvpeeais pgvtaswiea hlpddskdtw kkrgnveyvv
      181 lldwfssakd lqigttlrsl kdalfkwesk tvlrneplvl eggyenwllc ypqyttnakv
      241 tppprrqnee vsisldftyp sleesipskp aaqtppasie vdenielisg qnermgplni
      301 stpvepvaas ksdvspiiqp vpsiknvpqi drtkkpavkl peehrikses tnheqqspqs
      361 gkvipdrstk pvvfsptlml tdeekariha etallmeknk qekelrerqq eeqkeklrke
      421 eqeqkakkkq eaeeneitek qqkakeemek keseqakked ketsakrgke itgvkrqsks
      481 ehetsdakks vedrgkrcpt peiqkkstgd vphtsvtgds gsgkaqrepl trarseemgr
      541 ivpglpsgwa kfldpitgtf ryyhsptntv hmyppemaps sappstppth kakpqipaer
      601 drepsklkrs ysspditqai qeeekrkptv tptvnrenkp tcypkaeisr lsasqirnln
      661 pvfggsgpal tglrnlgntc ymnsilqclc naphladyfn rncyqddinr snllghkgev
      721 aeefgiimka lwtgqyryis pkdfkitigk indqfagysq qdsqelllfl mdglhedlnk
      781 adnrkrykee nndhlddfka aehawqkhkq lnesiivalf qgqfkstvqc ltchkksrtf
      841 eafmylslpl astskctlqd clrlfskeek ltdnnrfycs hcrarrdslk kieiwklppv
      901 llvhlkrfsy dgrwkqklqt svdfplenld lsqyvigpkn nlkkynlfsv snhyggldgg
      961 hytaycknaa rqrwfkfddh evsdisvssv kssaayilfy tslgprvtdv at
//
LOCUS       NP_002092                128 aa            linear   PRI 20-NOV-2025
DEFINITION  glycophorin-C isoform 1 [Homo sapiens].
ACCESSION   NP_002092 XP_945454
VERSION     NP_002092.1
DBSOURCE    REFSEQ: accession NM_002101.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Terada,N., Saitoh,Y., Saito,M., Yamada,T., Kamijo,A., Yoshizawa,T.
            and Sakamoto,T.
  TITLE     Recent Progress on Genetically Modified Animal Models for Membrane
            Skeletal Proteins: The 4.1 and MPP Families
  JOURNAL   Genes (Basel) 14 (10), 1942 (2023)
   PUBMED   37895291
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Lin,J.J., Loucks,C.M., Trueman,J.N., Drogemoller,B.I.,
            Wright,G.E.B., Yoshida,E.M., Ford,J.A., Lee,S.S., Kim,R.B.,
            Al-Judaibi,B., Schwarz,U.I., Ramji,A., Tam,E., Ross,C.J. and
            Carleton,B.C.
  TITLE     Novel variant in glycophorin c gene protects against
            ribavirin-induced anemia during chronic hepatitis C treatment
  JOURNAL   Biomed Pharmacother 143, 112195 (2021)
   PUBMED   34562771
  REMARK    GeneRIF: Novel variant in glycophorin c gene protects against
            ribavirin-induced anemia during chronic hepatitis C treatment.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Lobo,C.A., Rodriguez,M., Reid,M. and Lustigman,S.
  TITLE     Glycophorin C is the receptor for the Plasmodium falciparum
            erythrocyte binding ligand PfEBP-2 (baebl)
  JOURNAL   Blood 101 (11), 4628-4631 (2003)
   PUBMED   12576308
  REMARK    GeneRIF: Glycophorin C is identified as the receptor for PfEBP-2,
            the erythrocyte binding ligand of Plasmodium falciparum, and the
            binding domain on GPC is determined to be amino acid residues 14
            through 22 within exon 2.
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Maier,A.G., Duraisingh,M.T., Reeder,J.C., Patel,S.S., Kazura,J.W.,
            Zimmerman,P.A. and Cowman,A.F.
  TITLE     Plasmodium falciparum erythrocyte invasion through glycophorin C
            and selection for Gerbich negativity in human populations
  JOURNAL   Nat Med 9 (1), 87-92 (2003)
   PUBMED   12469115
  REMARK    GeneRIF: Data show that the receptor for Plasmodium falciparum
            erythrocyte-binding antigen 140 (EBA140) is glycophorin C (GYPC)
            and that this interaction mediates a principal P. falciparum
            invasion pathway into human erythrocytes.
REFERENCE   6  (residues 1 to 128)
  AUTHORS   King,M.J., Avent,N.D., Mallinson,G. and Reid,M.E.
  TITLE     Point mutation in the glycophorin C gene results in the expression
            of the blood group antigen Dha
  JOURNAL   Vox Sang 63 (1), 56-58 (1992)
   PUBMED   1413665
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Telen,M.J., Le Van Kim,C., Chung,A., Cartron,J.P. and Colin,Y.
  TITLE     Molecular basis for elliptocytosis associated with glycophorin C
            and D deficiency in the Leach phenotype
  JOURNAL   Blood 78 (6), 1603-1606 (1991)
   PUBMED   1884026
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Spring,F.A.
  TITLE     Immunochemical characterisation of the low-incidence antigen, Dha
  JOURNAL   Vox Sang 61 (1), 65-68 (1991)
   PUBMED   1719701
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Colin,Y., Le Van Kim,C., Tsapis,A., Clerget,M., d'Auriol,L.,
            London,J., Galibert,F. and Cartron,J.P.
  TITLE     Human erythrocyte glycophorin C. Gene structure and rearrangement
            in genetic variants
  JOURNAL   J Biol Chem 264 (7), 3773-3780 (1989)
   PUBMED   2917976
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Mattei,M.G., Colin,Y., Le Van Kim,C., Mattei,J.F. and Cartron,J.P.
  TITLE     Localization of the gene for human erythrocyte glycophorin C to
            chromosome 2, q14-q21
  JOURNAL   Hum Genet 74 (4), 420-422 (1986)
   PUBMED   3793105
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC106051.1 and AC013474.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_945454.1.
            
            Summary: Glycophorin C (GYPC) is an integral membrane glycoprotein.
            It is a minor species carried by human erythrocytes, but plays an
            important role in regulating the mechanical stability of red cells.
            A number of glycophorin C mutations have been described. The
            Gerbich and Yus phenotypes are due to deletion of exon 3 and 2,
            respectively. The Webb and Duch antigens, also known as glycophorin
            D, result from single point mutations of the glycophorin C gene.
            The glycophorin C protein has very little homology with
            glycophorins A and B. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC106051.1, X12496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259254.9/ ENSP00000259254.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..128
                     /product="glycophorin-C isoform 1"
                     /note="glycophorin-D; glycoconnectin; glycoprotein beta;
                     sialoglycoprotein D; Gerbich blood group antigen; Gerbich
                     antigen"
                     /calculated_mol_wt=13680
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04921.1)"
     Site            3
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            4
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            6
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            8
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            8
                     /site_type="other"
                     /note="Not glycosylated, in variant Webb antigen;
                     propagated from UniProtKB/Swiss-Prot (P04921.1)"
     Site            9
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            10
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            15
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            24
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            26
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            27
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            28
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            31
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            32
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            33
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:3571235,
                     ECO:0000269|PubMed:7106126; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Site            42
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:22171320,
                     ECO:0000269|PubMed:3571235, ECO:0000269|PubMed:7106126;
                     propagated from UniProtKB/Swiss-Prot (P04921.1)"
     Site            58..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P04921.1)"
     Region          80..98
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     Region          108..128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P04921.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04921.1)"
     CDS             1..128
                     /gene="GYPC"
                     /gene_synonym="CD236; CD236R; GE; GPC; GPD; GYPD; PAS-2;
                     PAS-2'"
                     /coded_by="NM_002101.5:107..493"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2136.1"
                     /db_xref="GeneID:2995"
                     /db_xref="HGNC:HGNC:4704"
                     /db_xref="MIM:110750"
ORIGIN      
        1 mwstrspnst awplslepdp gmasasttmh tttiaepdpg msgwpdgrme tstptimdiv
       61 viagviaava ivlvsllfvm lrymyrhkgt yhtneakgte faesadaalq gdpalqdagd
      121 ssrkeyfi
//
LOCUS       NP_064720                447 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform c [Homo sapiens].
ACCESSION   NP_064720 XP_005268006
VERSION     NP_064720.1
DBSOURCE    REFSEQ: accession NM_020324.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_005268006.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (3), as well as variant 13,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.537072.1,
                                           SRR1803616.33658.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..447
                     /product="lysosomal cobalamin transporter ABCD4 isoform c"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=50111
     Region          <32..444
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..447
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_020324.3:360..1703"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 maskliispf tlvyytyqcf qstgwlgpvs ifgyfilgtv vnktlmgpiv mklvhqekle
       61 gdfrfkhmqi rvnaepaafy raghvehmrt drrlqrllqt qrelmskelw lyigintfdy
      121 lgsilsyvvi aipifsgvyg dlspaelstl vsknafvciy liscftqlid lsttlsdvag
      181 ythrigqlre tlldmslksq dceilgesew gldtppgwpa aepadtafll ervsisapss
      241 dkplikdlsl kisegqslli tgntgtgkts llrvlgglwt strgsvqmlt dfgphgvlfl
      301 pqkpfftdgt lreqviyplk evypdsgsad derilrflel aglsnlvart egldqqvdwn
      361 wydvlspgem qrlsfarlfy lqpkyavlde atsalteeve selyrigqql gmtfisvghr
      421 qslekfhslv lklcgggrwe lmrikve
//
LOCUS       NP_001304096              68 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein G isoform d [Homo sapiens].
ACCESSION   NP_001304096
VERSION     NP_001304096.1
DBSOURCE    REFSEQ: accession NM_001317167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   6  (residues 1 to 68)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 68)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 68)
  AUTHORS   Plessel,G., Luhrmann,R. and Kastner,B.
  TITLE     Electron microscopy of assembly intermediates of the snRNP core:
            morphological similarities between the RNA-free (E.F.G) protein
            heteromer and the intact snRNP core
  JOURNAL   J Mol Biol 265 (2), 87-94 (1997)
   PUBMED   9020971
REFERENCE   9  (residues 1 to 68)
  AUTHORS   Hermann,H., Fabrizio,P., Raker,V.A., Foulaki,K., Hornig,H.,
            Brahms,H. and Luhrmann,R.
  TITLE     snRNP Sm proteins share two evolutionarily conserved sequence
            motifs which are involved in Sm protein-protein interactions
  JOURNAL   EMBO J 14 (9), 2076-2088 (1995)
   PUBMED   7744013
REFERENCE   10 (residues 1 to 68)
  AUTHORS   Heinrichs,V., Hackl,W. and Luhrmann,R.
  TITLE     Direct binding of small nuclear ribonucleoprotein G to the Sm site
            of small nuclear RNA. Ultraviolet light cross-linking of protein G
            to the AAU stretch within the Sm site (AAUUUGUGG) of U1 small
            nuclear ribonucleoprotein reconstituted in vitro
  JOURNAL   J Mol Biol 227 (1), 15-28 (1992)
   PUBMED   1387914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI290354.1 and AI742299.1.
            
            Summary: The protein encoded by this gene is a component of the U1,
            U2, U4, and U5 small nuclear ribonucleoprotein complexes,
            precursors of the spliceosome. The encoded protein may also be a
            part of the U7 small nuclear ribonucleoprotein complex, which
            participates in the processing of the 3' end of histone
            transcripts. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (4) uses an alternate exon in
            place of the first exon compared to variant 1. The resulting
            isoform (d) has a shorter and distinct N-terminus compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI290354.1, SRR14243140.11095447.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..68
                     /product="small nuclear ribonucleoprotein G isoform d"
                     /EC_number="1.8.1.4"
                     /note="small nuclear ribonucleoprotein G; snRNP-G; sm
                     protein G"
                     /calculated_mol_wt=7465
     Region          4..66
                     /region_name="Sm_G"
                     /note="Sm protein G; cd01719"
                     /db_xref="CDD:212466"
     Site            order(4,12,17,30,51,53..54,56,59..63,65)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212466"
     Site            order(9..15,17..29,31..35)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212466"
     Site            order(29,31,55,57)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212466"
     Site            51..62
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212466"
     CDS             1..68
                     /gene="SNRPG"
                     /gene_synonym="Sm-G; SMG"
                     /coded_by="NM_001317167.1:65..271"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82462.1"
                     /db_xref="GeneID:6637"
                     /db_xref="HGNC:HGNC:11163"
                     /db_xref="MIM:603542"
ORIGIN      
        1 mclfmdkkls lklnggrhvq gilrgfdpfm nlvidecvem atsgqqnnig mvvirgnsii
       61 mlealerv
//
LOCUS       NP_001229                410 aa            linear   PRI 20-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 1 [Homo sapiens].
ACCESSION   NP_001229
VERSION     NP_001229.1
DBSOURCE    REFSEQ: accession NM_001238.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10, AK291549.1,
            BC035498.2 and BQ018270.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (1, also known as cyclin EL)
            encodes isoform 1, also known as isoform E1L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.439579.1, BC035498.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262643.8/ ENSP00000262643.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..410
                     /product="G1/S-specific cyclin-E1 isoform 1"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=46946
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Region          103..239
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            order(109..110,112,115..116,119..120,123,127,162,197,
                     201..205,209..210,227,230..231,234..235,238..239)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          243..356
                     /region_name="CYCLIN_CCNE1_rpt2"
                     /note="second cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20581"
                     /db_xref="CDD:410284"
     Site            order(244,251..252,255,264..268,270,355..356)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410284"
     Region          378..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24864.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132, ECO:0000269|PubMed:8861947,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK2.
                     /evidence=ECO:0000269|PubMed:14536078,
                     ECO:0000269|PubMed:17434132; propagated from
                     UniProtKB/Swiss-Prot (P24864.2)"
     CDS             1..410
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001238.4:187..1419"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12419.1"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mprerrerda kerdtmkedg gaefsarsrk rkanvtvflq dpdeemakid rtardqcgsq
       61 pwdnnavcad pcsliptpdk edddrvypns tckpriiaps rgsplpvlsw anreevwkim
      121 lnkektylrd qhfleqhpll qpkmrailld wlmevcevyk lhretfylaq dffdrymatq
      181 envvktllql igisslfiaa kleeiyppkl hqfayvtdga csgdeiltme lmimkalkwr
      241 lspltivswl nvymqvayln dlhevllpqy pqqifiqiae lldlcvldvd clefpygila
      301 asalyhfsss elmqkvsgyq wcdiencvkw mvpfamvire tgssklkhfr gvadedahni
      361 qthrdsldll dkarakkaml seqnrasplp sglltppqsg kkqssgpema
//
LOCUS       NP_001278433             206 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase inhibitor 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001278433
VERSION     NP_001278433.1
DBSOURCE    REFSEQ: accession NM_001291504.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Bresch,A.M., Yerich,N., Wang,R. and Sperry,A.O.
  TITLE     The PP1 regulator PPP1R2 coordinately regulates AURKA and PP1 to
            control centrosome phosphorylation and maintain central spindle
            architecture
  JOURNAL   BMC Mol Cell Biol 21 (1), 84 (2020)
   PUBMED   33238888
  REMARK    GeneRIF: The PP1 regulator PPP1R2 coordinately regulates AURKA and
            PP1 to control centrosome phosphorylation and maintain central
            spindle architecture.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Kakinoki,Y., Somers,J. and Brautigan,D.L.
  TITLE     Multisite phosphorylation and the nuclear localization of
            phosphatase inhibitor 2-green fluorescent protein fusion protein
            during S phase of the cell growth cycle
  JOURNAL   J Biol Chem 272 (51), 32308-32314 (1997)
   PUBMED   9405437
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Permana,P.A. and Mott,D.M.
  TITLE     Genetic analysis of human type 1 protein phosphatase inhibitor 2 in
            insulin-resistant Pima Indians
  JOURNAL   Genomics 41 (1), 110-114 (1997)
   PUBMED   9126490
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Sanseau,P., Jackson,A., Alderton,R.P., Beck,S., Senger,G.,
            Sheer,D., Kelly,A. and Trowsdale,J.
  TITLE     Cloning and characterization of human phosphatase inhibitor-2
            (IPP-2) sequences
  JOURNAL   Mamm Genome 5 (8), 490-496 (1994)
   PUBMED   7949733
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Helps,N.R., Street,A.J., Elledge,S.J. and Cohen,P.T.
  TITLE     Cloning of the complete coding region for human protein phosphatase
            inhibitor 2 using the two hybrid system and expression of inhibitor
            2 in E. coli
  JOURNAL   FEBS Lett 340 (1-2), 93-98 (1994)
   PUBMED   8119416
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Park,I.K., Roach,P., Bondor,J., Fox,S.P. and DePaoli-Roach,A.A.
  TITLE     Molecular mechanism of the synergistic phosphorylation of
            phosphatase inhibitor-2. Cloning, expression, and site-directed
            mutagenesis of inhibitor-2
  JOURNAL   J Biol Chem 269 (2), 944-954 (1994)
   PUBMED   8288648
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069213.22.
            
            Summary: Protein phosphatase-1 (PP1) is one of the main eukaryotic
            serine/threonine phosphatases. The protein encoded by this gene
            binds to the catalytic subunit of PP1, strongly inhibiting its
            activity. Ten related pseudogenes have been found throughout the
            human genome. Several splice variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380201.76080.13,
                                           SRR6380202.91439.5 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..206
                     /product="protein phosphatase inhibitor 2 isoform 1"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase inhibitor 2; phosphoprotein
                     phosphatase"
                     /calculated_mol_wt=22940
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41236.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P11845; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Region          12..17
                     /region_name="Required for binding PPP1CC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P41236.2)"
     Region          43..55
                     /region_name="Required for binding PPP1CC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P41236.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:18250156; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Region          45..165
                     /region_name="IPP-2"
                     /note="Protein phosphatase inhibitor 2 (IPP-2); pfam04979"
                     /db_xref="CDD:461504"
     Site            73
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3.
                     /evidence=ECO:0000250|UniProtKB:P11845; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCL8; propagated from
                     UniProtKB/Swiss-Prot (P41236.2)"
     Region          148..151
                     /region_name="Required for binding PPP1CC catalytic
                     center, displacing metal ions and inhibition of PPP1CC
                     catalytic activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P41236.2)"
     Region          164..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41236.2)"
     CDS             1..206
                     /gene="PPP1R2"
                     /gene_synonym="IPP-2; IPP2; PPP1R2A"
                     /coded_by="NM_001291504.2:301..921"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:5504"
                     /db_xref="HGNC:HGNC:9288"
                     /db_xref="MIM:601792"
ORIGIN      
        1 maastashrp ikgilknkts ttssmvasae qprgnvdeel skksqkwdem nilatyhpad
       61 kdyglmkide pstpyhsmmg ddedacsdte ateamapdil arklaaaegl epkyriqeqe
      121 ssgeedsdls peergkkkrq femkrklhyn eglniklarq liskdlhddd edeemletad
      181 gesmnteesn qgstpsdqqq nklrss
//
LOCUS       NP_001106195             396 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 32A isoform 1 [Homo sapiens].
ACCESSION   NP_001106195
VERSION     NP_001106195.1
DBSOURCE    REFSEQ: accession NM_001112724.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 396)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 396)
  AUTHORS   Takamitsu,E., Fukunaga,K., Iio,Y., Moriya,K. and Utsumi,T.
  TITLE     Cell-free identification of novel N-myristoylated proteins from
            complementary DNA resources using bioorthogonal myristic acid
            analogues
  JOURNAL   Anal Biochem 464, 83-93 (2014)
   PUBMED   25043870
REFERENCE   3  (residues 1 to 396)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   4  (residues 1 to 396)
  AUTHORS   Koskinen,L.L., Einarsdottir,E., Korponay-Szabo,I.R., Kurppa,K.,
            Kaukinen,K., Sistonen,P., Pocsai,Z., Szeles,G., Adany,R., Maki,M.,
            Kere,J. and Saavalainen,P.
  TITLE     Fine mapping of the CELIAC2 locus on chromosome 5q31-q33 in the
            Finnish and Hungarian populations
  JOURNAL   Tissue Antigens 74 (5), 408-416 (2009)
   PUBMED   19845895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 396)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   6  (residues 1 to 396)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA110948.1, DR006392.1, BC021666.1, EB386256.1, DA231845.1 and
            AC009189.6.
            
            Transcript Variant: This variant (1) differs in the 3' UTR and
            coding sequence compared to variant 3. The resulting isoform (1)
            has a shorter and distinct C-terminus compared to isoform 3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.50348.1,
                                           SRR1660809.97822.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397936.8/ ENSP00000381030.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..396
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..396
                     /product="serine/threonine-protein kinase 32A isoform 1"
                     /EC_number="2.7.11.1"
                     /note="A930015B13Rik; serine/threonine-protein kinase 32A;
                     yet another novel kinase 1; CTB-108O6.2"
                     /calculated_mol_wt=46238
     Region          22..281
                     /region_name="STKc_Yank1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Yank1; cd05578"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,100..101,103,107,109,146,148,
                     150..151,153,163..164,167,180..185,215,221,224)
                     /site_type="active"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,101..103,107,146,148,150..151,
                     153,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270730"
     Site            order(33,107,109,146,148,150,167,180..185,215,221,224)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270730"
     Site            order(163..173,177..185)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270730"
     Region          373..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU08.2)"
     CDS             1..396
                     /gene="STK32A"
                     /gene_synonym="YANK1"
                     /coded_by="NM_001112724.2:271..1461"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47299.1"
                     /db_xref="GeneID:202374"
                     /db_xref="HGNC:HGNC:28317"
                     /db_xref="MIM:621310"
ORIGIN      
        1 mgantsrkpp vfdenedvnf dhfeilraig kgsfgkvciv qkndtkkmya mkymnkqkcv
       61 ernevrnvfk elqimqgleh pflvnlwysf qdeedmfmvv dlllggdlry hlqqnvhfke
      121 etvklficel vmaldylqnq riihrdmkpd nilldehghv hitdfniaam lpretqittm
      181 agtkpymape mfssrkgagy sfavdwwslg vtayellrgr rpyhirssts skeivhtfet
      241 tvvtypsaws qemvsllkkl lepnpdqrfs qlsdvqnfpy mndinwdavf qkrlipgfip
      301 nkgrlncdpt feleemiles kplhkkkkrl akkekdmrkc dssqtcllqe hldsvqkefi
      361 ifnrekvnrd fnkrqpnlal eqtkdpqged gqnnnl
//
LOCUS       NP_001306000             609 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphatase SAC1 isoform 1x [Homo sapiens].
ACCESSION   NP_001306000
VERSION     NP_001306000.1
DBSOURCE    REFSEQ: accession NM_001319071.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 609)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 609)
  AUTHORS   Popescu,M.A., Patriche,D., Dobrica,M.O., Pantazica,A.M., Flintoaca
            Alexandru,P.R., Rouille,Y., Popescu,C.I. and Branza-Nichita,N.
  TITLE     Sac1 phosphatidylinositol 4-phosphate phosphatase is a novel host
            cell factor regulating hepatitis B virus particles assembly and
            release
  JOURNAL   FEBS J 289 (23), 7486-7499 (2022)
   PUBMED   35816160
  REMARK    GeneRIF: Sac1 phosphatidylinositol 4-phosphate phosphatase is a
            novel host cell factor regulating hepatitis B virus particles
            assembly and release.
REFERENCE   3  (residues 1 to 609)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 609)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 609)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   6  (residues 1 to 609)
  AUTHORS   Liu,Y., Boukhelifa,M., Tribble,E., Morin-Kensicki,E., Uetrecht,A.,
            Bear,J.E. and Bankaitis,V.A.
  TITLE     The Sac1 phosphoinositide phosphatase regulates Golgi membrane
            morphology and mitotic spindle organization in mammals
  JOURNAL   Mol Biol Cell 19 (7), 3080-3096 (2008)
   PUBMED   18480408
  REMARK    GeneRIF: Sac1 executes an essential household function in mammals
            that involves organization of both Golgi membranes and mitotic
            spindles
REFERENCE   7  (residues 1 to 609)
  AUTHORS   Rohde,H.M., Cheong,F.Y., Konrad,G., Paiha,K., Mayinger,P. and
            Boehmelt,G.
  TITLE     The human phosphatidylinositol phosphatase SAC1 interacts with the
            coatomer I complex
  JOURNAL   J Biol Chem 278 (52), 52689-52699 (2003)
   PUBMED   14527956
  REMARK    GeneRIF: the enzymatic function of hSAC1 provides a switch for
            accessibility of the COPI interaction motif
REFERENCE   8  (residues 1 to 609)
  AUTHORS   Kiss,H., Kedra,D., Kiss,C., Kost-Alimova,M., Yang,Y., Klein,G.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The LZTFL1 gene is a part of a transcriptional map covering 250 kb
            within the common eliminated region 1 (C3CER1) in 3p21.3
  JOURNAL   Genomics 73 (1), 10-19 (2001)
   PUBMED   11352561
REFERENCE   9  (residues 1 to 609)
  AUTHORS   Nemoto,Y., Kearns,B.G., Wenk,M.R., Chen,H., Mori,K., Alb,J.G. Jr.,
            De Camilli,P. and Bankaitis,V.A.
  TITLE     Functional characterization of a mammalian Sac1 and mutants
            exhibiting substrate-specific defects in phosphoinositide
            phosphatase activity
  JOURNAL   J Biol Chem 275 (44), 34293-34305 (2000)
   PUBMED   10887188
REFERENCE   10 (residues 1 to 609)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC322649.1, AB020658.1 and
            CA335989.1.
            
            Summary: This gene encodes an integral membrane protein, which is
            localized to the endoplasmic reticulum, and functions as a
            phosphoinositide phosphatase that hydrolyzes phosphatidylinositol
            3-phosphate, phosphatidylinositol 4-phosphate, and
            phosphatidylinositol 3,5-bisphosphate. Deletion of this gene in
            mouse results in preimplantation lethality. Other studies suggest
            that this gene is also involved in the organization of golgi
            membranes and mitotic spindles. Alternatively spliced transcript
            variants have been found for this gene. A C-terminally extended
            isoform is also predicted to be produced by the use of an
            alternative in-frame, downstream translation termination codon via
            a stop codon readthrough mechanism.[provided by RefSeq, Dec 2017].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UGA termination codon. This
            RefSeq represents the longer isoform (1x). As the UGA stop codon
            has been reported to specify several alternative amino acids
            (tryptophan, cysteine, arginine and serine), its location in the
            longer isoform is denoted by an 'X'.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.32781.1,
                                           SRR1803617.37135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            stop codon readthrough :: inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..609
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..609
                     /product="phosphatidylinositol-3-phosphatase SAC1 isoform
                     1x"
                     /EC_number="3.1.3.64"
                     /note="suppressor of actin 1; phosphatidylinositide
                     phosphatase SAC1; suppressor of actin mutations 1-like
                     protein; SAC1 suppressor of actin mutations 1 like;
                     phosphatidylinositol-4-phosphate phosphatase;
                     phosphatidylinositol-3-phosphatase SAC1"
                     /calculated_mol_wt=69229
     Region          57..513
                     /region_name="COG5329"
                     /note="Phosphoinositide polyphosphatase (Sac family)
                     [Signal transduction mechanisms]"
                     /db_xref="CDD:227637"
     CDS             1..609
                     /gene="SACM1L"
                     /gene_synonym="SAC1"
                     /coded_by="NM_001319071.2:71..1900"
                     /note="isoform 1x is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS93257.1"
                     /db_xref="GeneID:22908"
                     /db_xref="HGNC:HGNC:17059"
                     /db_xref="MIM:606569"
ORIGIN      
        1 mataayeqlk lhitpekfyv eacddgaddv ltidrvstev tlavkkdvpp savtrpifgi
       61 lgtihlvagn ylivitkkik vgeffshvvw katdfdvlsy kktmlhltdi qlqdnktfla
      121 mlnhvlnvdg fyfsttydlt htlqrlsnts pefqemslle radqrfvwng hllrelsaqp
      181 evhrfalpvl hgfitmhscs ingkyfdwil isrrscfrag vryyvrgids eghaanfvet
      241 eqivhyngsk asfvqtrgsi pvfwsqrpnl kykplpqisk vanhmdgfqr hfdsqviiyg
      301 kqviinlinq kgsekpleqt fatmvsslgs gmmryiafdf hkecknmrwd rlsilldqva
      361 emqdelsyfl vdsagqvvan qegvfrsncm dcldrtnviq sllarrslqa qlqrlgvlhv
      421 gqkleeqdef ekiyknawad nanacakqya gtgalktdft rtgkrthlgl imdgwnsmir
      481 yyknnfsdgf rqdsidlflg nysvdelesh splsvprdwk flalpiimvv afsmciicll
      541 magdtwtetl ayvlfwgvas igtffiilyn gkdfvdaprl vqkekidxic icgkrlgled
      601 sivqnwsly
//
LOCUS       NP_003191                654 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor E2-alpha isoform E12 [Homo sapiens].
ACCESSION   NP_003191
VERSION     NP_003191.1
DBSOURCE    REFSEQ: accession NM_003200.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Collinson,R.J., Wilson,L., Boey,D., Ng,Z.Y., Mirzai,B., Chuah,H.S.,
            Howman,R., Grove,C.S., Malherbe,J.A.J., Leahy,M.F., Linden,M.D.,
            Fuller,K.A., Erber,W.N. and Guo,B.B.
  TITLE     Transcription factor 3 is dysregulated in megakaryocytes in
            myelofibrosis
  JOURNAL   Platelets 35 (1), 2304173 (2024)
   PUBMED   38303515
  REMARK    GeneRIF: Transcription factor 3 is dysregulated in megakaryocytes
            in myelofibrosis.
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Xie,W., Liu,W., Wang,L., Li,S., Liao,Z., Xu,H., Li,Y., Jiang,X. and
            Ren,C.
  TITLE     Embryonic stem cell related gene regulates alternative splicing of
            transcription factor 3 to maintain human embryonic stem cells'
            self-renewal and pluripotency
  JOURNAL   Stem Cells 42 (6), 540-553 (2024)
   PUBMED   38393342
  REMARK    GeneRIF: Embryonic stem cell related gene regulates alternative
            splicing of transcription factor 3 to maintain human embryonic stem
            cells' self-renewal and pluripotency.
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Li,Y., Li,R., Li,Y., Li,G., Zhao,Y., Mou,H., Chen,Y., Xiao,L. and
            Gong,K.
  TITLE     Transcription Factor TCF3 Promotes Macrophage-Mediated Inflammation
            and MMP Secretion in Abdominal Aortic Aneurysm by Regulating
            miR-143-5p /CCL20
  JOURNAL   J Cardiovasc Pharmacol 82 (6), 458-469 (2023)
   PUBMED   37721971
  REMARK    GeneRIF: Transcription Factor TCF3 Promotes Macrophage-Mediated
            Inflammation and MMP Secretion in Abdominal Aortic Aneurysm by
            Regulating miR-143-5p /CCL20.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Zhang,W., Nowotny,H., Theodoropoulou,M., Simon,J., Hemmer,C.M.,
            Bidlingmaier,M., Auer,M.K., Reincke,M., Uhlenhaut,H. and Reisch,N.
  TITLE     E47 as a novel glucocorticoid-dependent gene mediating lipid
            metabolism in patients with endogenous glucocorticoid excess
  JOURNAL   Front Endocrinol (Lausanne) 14, 1249863 (2023)
   PUBMED   38047107
  REMARK    GeneRIF: E47 as a novel glucocorticoid-dependent gene mediating
            lipid metabolism in patients with endogenous glucocorticoid excess.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Chakraborty,T., Martin,J.F. and Olson,E.N.
  TITLE     Analysis of the oligomerization of myogenin and E2A products in
            vivo using a two-hybrid assay system
  JOURNAL   J Biol Chem 267 (25), 17498-17501 (1992)
   PUBMED   1325437
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Inaba,T., Roberts,W.M., Shapiro,L.H., Jolly,K.W., Raimondi,S.C.,
            Smith,S.D. and Look,A.T.
  TITLE     Fusion of the leucine zipper gene HLF to the E2A gene in human
            acute B-lineage leukemia
  JOURNAL   Science 257 (5069), 531-534 (1992)
   PUBMED   1386162
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Lassar,A.B., Davis,R.L., Wright,W.E., Kadesch,T., Murre,C.,
            Voronova,A., Baltimore,D. and Weintraub,H.
  TITLE     Functional activity of myogenic HLH proteins requires
            hetero-oligomerization with E12/E47-like proteins in vivo
  JOURNAL   Cell 66 (2), 305-315 (1991)
   PUBMED   1649701
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006274.1, M31222.1,
            AC005321.1 and KC877695.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the E protein (class I)
            family of helix-loop-helix transcription factors. E proteins
            activate transcription by binding to regulatory E-box sequences on
            target genes as heterodimers or homodimers, and are inhibited by
            heterodimerization with inhibitor of DNA-binding (class IV)
            helix-loop-helix proteins. E proteins play a critical role in
            lymphopoiesis, and the encoded protein is required for B and T
            lymphocyte development. Deletion of this gene or diminished
            activity of the encoded protein may play a role in lymphoid
            malignancies. This gene is also involved in several chromosomal
            translocations that are associated with lymphoid malignancies
            including pre-B-cell acute lymphoblastic leukemia (t(1;19), with
            PBX1), childhood leukemia (t(19;19), with TFPT) and acute leukemia
            (t(12;19), with ZNF384). Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the short arm of chromosome
            9. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (E12). This isoform is
            also known as Pan-2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M31222.1, SRR14038193.1259148.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262965.12/ ENSP00000262965.5
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..654
                     /product="transcription factor E2-alpha isoform E12"
                     /note="VDR interacting repressor; transcription factor
                     E2-alpha; immunoglobulin transcription factor 1;
                     kappa-E2-binding factor; transcription factor ITF-1;
                     E2A-HLF fusion transcript protein; class B basic
                     helix-loop-helix protein 21; vitamin D
                     receptor-interacting repressor; negative vitamin D
                     response element-binding protein; helix-loop-helix protein
                     HE47; transcription factor 3 (E2A immunoglobulin enhancer
                     binding factors E12/E47); NOL1-TCF3 fusion"
                     /calculated_mol_wt=67469
     Region          19..27
                     /region_name="9aaTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          31..103
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Region          135..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Region          170..176
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          239..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          292..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          343..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P15806; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Site            371
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P15806; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Region          389..425
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          461..552
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Region          474..>574
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            483..484
                     /site_type="other"
                     /note="Breakpoint for translocation to form TCF3-PBX1
                     oncogene; propagated from UniProtKB/Swiss-Prot (P15923.1)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P15923.1)"
     Region          543..627
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(551,555,557..559,561,566,587..588)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(564..565,568..569,571..572,575,579,589,592,596,599,
                     602..607)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     Region          633..654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15923.1)"
     CDS             1..654
                     /gene="TCF3"
                     /gene_synonym="AGM8; AGM8A; AGM8B; bHLHb21; E2A; E47;
                     ITF1; p75; TCF-3; VDIR"
                     /coded_by="NM_003200.5:356..2320"
                     /note="isoform E12 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12074.1"
                     /db_xref="GeneID:6929"
                     /db_xref="HGNC:HGNC:11633"
                     /db_xref="MIM:147141"
ORIGIN      
        1 mnqpqrmapv gtdkelsdll dfsmmfplpv tngkgrpasl agaqfggsgl edrpssgswg
       61 sgdqssssfd psrtfsegth fteshsslss stflgpglgg ksgergayas fgrdagvggl
      121 tqagflsgel alnspgplsp sgmkgtsqyy psysgssrrr aadgsldtqp kkvrkvppgl
      181 pssvyppssg edygrdatay psaktpssty papfyvadgs lhpsaelwsp pgqagfgpml
      241 gggssplplp pgsgpvgssg ssstfgglhq hermgyqlhg aevngglpsa ssfssapgat
      301 yggvsshtpp vsgadsllgs rgttagssgd algkalasiy spdhssnnfs sspstpvgsp
      361 qglagtsqwp ragapgalsp sydgglhglq skiedhldea ihvlrshavg tagdmhtllp
      421 ghgalasgft gpmslggrha glvggshped glagstslmh nhaalpsqpg tlpdlsrppd
      481 sysglgraga taaaseikre ekedeentsa adhseeekke lkaprartsp dededdllpp
      541 eqkaereker rvannarerl rvrdineafk elgrmcqlhl nsekpqtkll ilhqavsvil
      601 nleqqvrern lnpkaaclkr reeekvsgvv gdpqmvlsap hpglseahnp aghm
//
LOCUS       NP_001073938             603 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 46 [Homo sapiens].
ACCESSION   NP_001073938 NP_036198 XP_371179
VERSION     NP_001073938.1
DBSOURCE    REFSEQ: accession NM_001080469.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Choppara,S., Ganga,S., Manne,R., Dutta,P., Singh,S. and Santra,M.K.
  TITLE     The SCFFBXO46 ubiquitin ligase complex mediates degradation of the
            tumor suppressor FBXO31 and thereby prevents premature cellular
            senescence
  JOURNAL   J Biol Chem 293 (42), 16291-16306 (2018)
   PUBMED   30171069
  REMARK    GeneRIF: reveal that FBXO46 is a crucial proteasomal regulator of
            FBXO31 and thereby prevents senescence in normal growth conditions
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007774.1 and AC007191.1.
            
            On or before Jul 21, 2016 this sequence version replaced
            NP_036198.1, XP_371179.1.
            
            Summary: Members of the F-box protein family, such as FBXO46, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.434298.1,
                                           SRR1163657.261446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317683.4/ ENSP00000410007.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..603
                     /product="F-box only protein 46"
                     /calculated_mol_wt=64500
     Region          20..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          <110..>300
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          111..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          235..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          326..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          396..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          473..519
                     /region_name="F-box_FBXO46"
                     /note="F-box domain found in F-box only protein 46
                     (FBXO46) and similar proteins; cd22177"
                     /db_xref="CDD:438948"
     Site            order(476,480,483..484,487..488,492,494..495,499..501,503)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438948"
     CDS             1..603
                     /gene="FBXO46"
                     /gene_synonym="20D7-FC4; Fbx46; FBXO34L"
                     /coded_by="NM_001080469.2:127..1938"
                     /db_xref="CCDS:CCDS46116.1"
                     /db_xref="GeneID:23403"
                     /db_xref="HGNC:HGNC:25069"
                     /db_xref="MIM:609117"
ORIGIN      
        1 mdrgsllpfq lwcprpfgty sqnqprppsa alkpsacpep gggaepdhgp ahsentppal
       61 atevpasqpa pllsaaaagd egrvlldtwy vikpgntkek vaffvahqcg ggsrassmkv
      121 kghwgsdssk akrrrrcldp tkappdpggr egppaaeegp asagedvdll svaemvalve
      181 qraalalqsy prpttpapvv fvsaeqggpa kgvgserrsg ggdcsrvaea vahfeaqrds
      241 pptkglrkee rpgpgpgevr iafrisngre prapdsglps ggggrpgcay pgspgpgara
      301 kdkitcdlyq lispsrdalp snvefllara deasegdspa parpedtppa pppppardcg
      361 asgfhvdvvv tgvvdeciff gkdgtknvke etvcltvspe eppppgqlff lqnrgpdgpp
      421 epppadspat apgpddaegt adtslcrlyr hvshdfleir fkiqrllepr qymlllpehv
      481 lvkifsflpt ralaalkctc hhfkgiieaf gvratdsrws rdplyrddpc kqcrkryekg
      541 dvslcrwhpk pyhhdlpygr sywmccrrad retpgcrlgl hdnnwvlpcn gpgggragre
      601 egr
//
LOCUS       NP_001349720             814 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit B isoform 1
            [Homo sapiens].
ACCESSION   NP_001349720 XP_016868241
VERSION     NP_001349720.1
DBSOURCE    REFSEQ: accession NM_001362791.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Huang,R., Nie,W., Mi,L., Yao,C. and Zhu,H.
  TITLE     EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma
  JOURNAL   Aging (Albany NY) 16 (8), 7311-7330 (2024)
   PUBMED   38687509
  REMARK    GeneRIF: EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma.
REFERENCE   4  (residues 1 to 814)
  AUTHORS   Fang,P., Han,Y., Qu,Y., Wang,X., Zhang,Y., Zhang,W., Zhang,N.,
            Li,G. and Ma,W.
  TITLE     EIF3B stabilizes PTGS2 expression by counteracting MDM2-mediated
            ubiquitination to promote the development and progression of
            malignant melanoma
  JOURNAL   Cancer Sci 113 (12), 4181-4192 (2022)
   PUBMED   36050601
  REMARK    GeneRIF: EIF3B stabilizes PTGS2 expression by counteracting
            MDM2-mediated ubiquitination to promote the development and
            progression of malignant melanoma.
REFERENCE   5  (residues 1 to 814)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 814)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
REFERENCE   7  (residues 1 to 814)
  AUTHORS   Chaudhuri,J., Chakrabarti,A. and Maitra,U.
  TITLE     Biochemical characterization of mammalian translation initiation
            factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the
            mammalian homologue of Saccharomyces cerevisiae protein Prt1
  JOURNAL   J Biol Chem 272 (49), 30975-30983 (1997)
   PUBMED   9388245
REFERENCE   8  (residues 1 to 814)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
REFERENCE   9  (residues 1 to 814)
  AUTHORS   Asano,K., Kinzy,T.G., Merrick,W.C. and Hershey,J.W.
  TITLE     Conservation and diversity of eukaryotic translation initiation
            factor eIF3
  JOURNAL   J Biol Chem 272 (2), 1101-1109 (1997)
   PUBMED   8995409
REFERENCE   10 (residues 1 to 814)
  AUTHORS   Kirken,R.A., Rui,H., Evans,G.A. and Farrar,W.L.
  TITLE     Characterization of an interleukin-2 (IL-2)-induced tyrosine
            phosphorylated 116-kDa protein associated with the IL-2 receptor
            beta-subunit
  JOURNAL   J Biol Chem 268 (30), 22765-22770 (1993)
   PUBMED   7693677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004971.3, U78525.1 and BC009986.1.
            
            On Apr 28, 2018 this sequence version replaced XP_016868241.1.
            
            Transcript Variant: This variant (3) differs in the 3' UTR compared
            to variant 2. Variants 1, 2 and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1350181.1,
                                           SRR1803614.241706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..814
                     /product="eukaryotic translation initiation factor 3
                     subunit B isoform 1"
                     /note="eukaryotic translation initiation factor 3, subunit
                     9 (eta, 116kD); eukaryotic translation initiation factor
                     3, subunit 9 eta, 116kDa; prt1 homolog; eukaryotic
                     translation initiation factor 3 subunit 9; protein
                     synthesis 1"
                     /calculated_mol_wt=92351
     Region          1..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          <4..161
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          124..413
                     /region_name="Sufficient for interaction with EIF3E"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          170..274
                     /region_name="Sufficient for interaction with EIF3J"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          184..264
                     /region_name="RRM_eIF3B"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     translation initiation factor 3 subunit B (eIF-3B) and
                     similar proteins; cd12278"
                     /db_xref="CDD:409720"
     Site            order(186,188,190..191,221,230,232,234,262,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409720"
     Site            order(189,192,199,202..203,205..207,209..210,213,249..252,
                     254..255,260..261)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409720"
     Site            209
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          305..805
                     /region_name="COG5354"
                     /note="Uncharacterized protein, contains Trp-Asp (WD)
                     repeat [General function prediction only]"
                     /db_xref="CDD:227657"
     Region          338..371
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          366..425
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          376..423
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          426..489
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          429..463
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          467..506
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          490..553
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          514..545
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          554..598
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          556..604
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          599..642
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          612..647
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          643..685
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          654..684
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..814
                     /gene="EIF3B"
                     /gene_synonym="EIF3-ETA; EIF3-P110; EIF3-P116; EIF3S9;
                     PRT1"
                     /coded_by="NM_001362791.2:96..2540"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5332.1"
                     /db_xref="GeneID:8662"
                     /db_xref="HGNC:HGNC:3280"
                     /db_xref="MIM:603917"
ORIGIN      
        1 mqdaenvavp eaaeeraepg qqqpaaeppp aegllrpagp gapeaagtea sseevgiaea
       61 gpesevrtep aaeaeaasgp sespsppaae elpgshaepp vpaqgeapge qardersdsr
      121 aqavsedagg negraaeaep ralengdade psfsdpedfv ddvseeellg dvlkdrpqea
      181 dgidsvivvd nvpqvgpdrl eklknvihki fskfgkitnd fypeedgktk gyifleyasp
      241 ahavdavkna dgykldkqht frvnlftdfd kymtisdewd ipekqpfkdl gnlrywleea
      301 ecrdqysvif esgdrtsifw ndvkdpvsie erarwtetyv rwspkgtyla tfhqrgialw
      361 ggekfkqiqr fshqgvqlid fspcerylvt fsplmdtqdd pqaiiiwdil tghkkrgfhc
      421 essahwpifk wshdgkffar mtldtlsiye tpsmglldkk slkisgikdf swspggniia
      481 fwvpedkdip arvtlmqlpt rqeirvrnlf nvvdcklhwq kngdylcvkv drtpkgtqgv
      541 vtnfeifrmr ekqvpvdvve mketiiafaw epngskfavl hgeaprisvs fyhvknngki
      601 elikmfdkqq antifwspqg qfvvlaglrs mngalafvdt sdctvmniae hymasdvewd
      661 ptgryvvtsv swwshkvdna ywlwtfqgrl lqknnkdrfc qllwrprppt llsqeqikqi
      721 kkdlkkyski feqkdrlsqs kaskelverr rtmmedfrky rkmaqelyme qknerlelrg
      781 gvdtdeldsn vddweeetie ffvteeiipl gnqe
//
LOCUS       NP_060147                704 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR8 [Homo
            sapiens].
ACCESSION   NP_060147
VERSION     NP_060147.2
DBSOURCE    REFSEQ: accession NM_017677.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Allen,E.A., Amato,C., Fortier,T.M., Velentzas,P., Wood,W. and
            Baehrecke,E.H.
  TITLE     A conserved myotubularin-related phosphatase regulates autophagy by
            maintaining autophagic flux
  JOURNAL   J Cell Biol 219 (11) (2020)
   PUBMED   32915229
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Yoo,K.Y., Son,J.Y., Lee,J.U., Shin,W., Im,D.W., Kim,S.J., Ryu,S.E.
            and Heo,Y.S.
  TITLE     Structure of the catalytic phosphatase domain of MTMR8:
            implications for dimerization, membrane association and reversible
            oxidation
  JOURNAL   Acta Crystallogr D Biol Crystallogr 71 (Pt 7), 1528-1539 (2015)
   PUBMED   26143924
  REMARK    GeneRIF: Here, the crystal structure of the phosphatase domain of
            MTMR8 is reported.
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Labuda,D., Yotova,V., Lefebvre,J.F., Moreau,C., Utermann,G. and
            Williams,S.M.
  TITLE     X-linked MTMR8 diversity and evolutionary history of sub-Saharan
            populations
  JOURNAL   PLoS One 8 (11), e80710 (2013)
   PUBMED   24282552
  REMARK    GeneRIF: East African population that gave rise to non-Africans
            underwent a selective sweep affecting the subcentromeric region
            where MTMR8 is located
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Zou,J., Zhang,C., Marjanovic,J., Kisseleva,M.V., Majerus,P.W. and
            Wilson,M.P.
  TITLE     Myotubularin-related protein (MTMR) 9 determines the enzymatic
            activity, substrate specificity, and role in autophagy of MTMR8
  JOURNAL   Proc Natl Acad Sci U S A 109 (24), 9539-9544 (2012)
   PUBMED   22647598
REFERENCE   9  (residues 1 to 704)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA691850.1, BC012399.1 and
            AL356317.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_060147.1.
            
            Summary: This gene encodes a member of the myotubularin-related
            family and is part of the MTMR6 subgroup. Family members are
            dual-specificity phosphatases and the encoded protein contains a
            phosphoinositide-binding domain (PID) and a SET-interacting domain
            (SID). Defects in other family members have been found in
            myotubular myopathic diseases. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012399.1, SRR1660803.207601.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374852.4/ ENSP00000363985.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq11.2"
     Protein         1..704
                     /product="phosphatidylinositol-3,5-bisphosphate
                     3-phosphatase MTMR8"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase"
                     /calculated_mol_wt=78788
     Region          1..103
                     /region_name="PH-GRAM_MTMR8"
                     /note="Myotubularian (MTM) related 8 protein (MTMR8)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13345"
                     /db_xref="CDD:270153"
     Region          126..433
                     /region_name="PTP-MTMR8"
                     /note="protein tyrosine phosphatase-like domain of
                     myotubularin related phosphoinositide phosphatase 8;
                     cd14584"
                     /db_xref="CDD:350432"
     Site            order(290,295..298,300..301,305,310)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:350432"
     CDS             1..704
                     /gene="MTMR8"
                     /coded_by="NM_017677.4:90..2204"
                     /db_xref="CCDS:CCDS14379.1"
                     /db_xref="GeneID:55613"
                     /db_xref="HGNC:HGNC:16825"
                     /db_xref="MIM:301061"
ORIGIN      
        1 mdhitvpkve nvklvdryvs kkpangilyl tathliyvea sgaarketwi alhhiatvek
       61 lpitslgcpl tlrcknfrva hfvldsdlvc hevyisllkl sqpalpedly afsynpkssk
      121 emresgwkli dpisdfgrmg ipnrnwtitd anrnyeicst yppeivvpks vtlgtvvgss
      181 kfrskervpv lsylykenna aicrcsqpls gfytrcvdde llleaisqtn pgsqfmyvvd
      241 trpklnaman raagkgyene dnyanirfrf mgienihvmr sslqkllevc elktptmsef
      301 lsglessgwl rhikaimdag ifitkavkve kasvlvhcsd gwdrtaqvcs vasilldpfy
      361 rtfkglmili ekewismghk fsqrcghldg dskevspift qfldciwqlm eqfpcafefn
      421 enflleihdh vfscqfgnfl gncqkdredl rvyekthsvw pflvqrkpdf rnplykgftm
      481 ygvlnpstvp yniqfwcgmy nrfdkglqpk qsmlesllei kkqramletd vhelekklkv
      541 rdeppeeict csqlgnilsq hlgspltnpl gfmgingdln tlmengtlsr egglraqmdq
      601 vksqgadlhh ncceivgslr ainisgdvgi seamgisgdm ctfeatgfsk dlgicgamdi
      661 seatgisgnl giseargfsg dmgilgdtgi skastkeady skhq
//
LOCUS       NP_055267                655 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 21 precursor
            [Homo sapiens].
ACCESSION   NP_055267 NP_057713
VERSION     NP_055267.1
DBSOURCE    REFSEQ: accession NM_014452.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Clay,S., Alladina,J., Smith,N.P., Visness,C.M., Wood,R.A.,
            O'Connor,G.T., Cohen,R.T., Khurana Hershey,G.K., Kercsmar,C.M.,
            Gruchalla,R.S., Gill,M.A., Liu,A.H., Kim,H., Kattan,M.,
            Bacharier,L.B., Rastogi,D., Rivera-Spoljaric,K., Robison,R.G.,
            Gergen,P.J., Busse,W.W., Villani,A.C., Cho,J.L., Medoff,B.D.,
            Gern,J.E., Jackson,D.J., Ober,C. and Dapas,M.
  TITLE     Gene-based association study of rare variants in children of
            diverse ancestries implicates TNFRSF21 in the development of
            allergic asthma
  JOURNAL   J Allergy Clin Immunol 153 (3), 809-820 (2024)
   PUBMED   37944567
  REMARK    GeneRIF: Gene-based association study of rare variants in children
            of diverse ancestries implicates TNFRSF21 in the development of
            allergic asthma.
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Cheng,J., Tang,Y., Cai,X. and Gong,J.
  TITLE     Long Noncoding RNAs Testis Development Related Gene 1 Aggravates
            Transforming Growth Factor-beta1-Induced Fibrogenesis and
            Inflammatory Response of Cardiac Fibroblasts Via miR-605-3p/Tumor
            Necrosis Factor Receptor Superfamily-21 Axis
  JOURNAL   J Cardiovasc Pharmacol 79 (3), 296-303 (2022)
   PUBMED   34775426
  REMARK    GeneRIF: Long Noncoding RNAs Testis Development Related Gene 1
            Aggravates Transforming Growth Factor-beta1-Induced Fibrogenesis
            and Inflammatory Response of Cardiac Fibroblasts Via
            miR-605-3p/Tumor Necrosis Factor Receptor Superfamily-21 Axis.
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Stegmann,S.K., Kuhl,S., Im,N.G., Diem-Dinh,D.T., Goertz,L.,
            Goldbrunner,R. and Timmer,M.
  TITLE     Death Receptor 6 as a Prognostic Marker in Low-grade Glioma
  JOURNAL   Anticancer Res 42 (3), 1237-1245 (2022)
   PUBMED   35220214
  REMARK    GeneRIF: Death Receptor 6 as a Prognostic Marker in Low-grade
            Glioma.
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Liu,Y., Chang,Y. and Cai,Y.
  TITLE     circTNFRSF21, a newly identified circular RNA promotes endometrial
            carcinoma pathogenesis through regulating miR-1227-MAPK13/ATF2 axis
  JOURNAL   Aging (Albany NY) 12 (8), 6774-6792 (2020)
   PUBMED   32299063
  REMARK    GeneRIF: circTNFRSF21, a newly identified circular RNA promotes
            endometrial carcinoma pathogenesis through regulating
            miR-1227-MAPK13/ATF2 axis.
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Cho,S.M., Kim,J., Ryu,H.J., Kim,J.J., Kim,H.H., Park,J.H.,
            Kim,H.T., Kim,K.H., Cho,H.Y., Oh,B., Park,C., Kimm,K., Jo,I.,
            Lee,J.E., Shin,H.D. and Lee,J.K.
  TITLE     Identification of single nucleotide polymorphisms in the tumor
            necrosis factor (TNF) and TNF receptor superfamily in the Korean
            population
  JOURNAL   Hum Immunol 65 (7), 710-718 (2004)
   PUBMED   15301860
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Kasof,G.M., Lu,J.J., Liu,D., Speer,B., Mongan,K.N., Gomes,B.C. and
            Lorenzi,M.V.
  TITLE     Tumor necrosis factor-alpha induces the expression of DR6, a member
            of the TNF receptor family, through activation of NF-kappaB
  JOURNAL   Oncogene 20 (55), 7965-7975 (2001)
   PUBMED   11753679
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Zhao,H., Yan,M., Wang,H., Erickson,S., Grewal,I.S. and Dixit,V.M.
  TITLE     Impaired c-Jun amino terminal kinase activity and T cell
            differentiation in death receptor 6-deficient mice
  JOURNAL   J Exp Med 194 (10), 1441-1448 (2001)
   PUBMED   11714751
  REMARK    GeneRIF: DR6 knockout mice are viable and fertile, and show
            hyperproliferation of T cells when stimulated.
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Liu,J., Na,S., Glasebrook,A., Fox,N., Solenberg,P.J., Zhang,Q.,
            Song,H.Y. and Yang,D.D.
  TITLE     Enhanced CD4+ T cell proliferation and Th2 cytokine production in
            DR6-deficient mice
  JOURNAL   Immunity 15 (1), 23-34 (2001)
   PUBMED   11485735
  REMARK    GeneRIF: DR6 mediates T cell proliferation and differentiation in
            mice.
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Pan,G., Bauer,J.H., Haridas,V., Wang,S., Liu,D., Yu,G., Vincenz,C.,
            Aggarwal,B.B., Ni,J. and Dixit,V.M.
  TITLE     Identification and functional characterization of DR6, a novel
            death domain-containing TNF receptor
  JOURNAL   FEBS Lett 431 (3), 351-356 (1998)
   PUBMED   9714541
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY007775.1 and AY358304.1.
            
            On Nov 4, 2002 this sequence version replaced NP_057713.1.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The encoded protein activates nuclear factor
            kappa-B and mitogen-activated protein kinase 8 (also called c-Jun
            N-terminal kinase 1), and induces cell apoptosis. Through its death
            domain, the encoded receptor interacts with tumor necrosis factor
            receptor type 1-associated death domain (TRADD) protein, which is
            known to mediate signal transduction of tumor necrosis factor
            receptors. Knockout studies in mice suggest that this gene plays a
            role in T-helper cell activation, and may be involved in
            inflammation and immune regulation. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.910204.1,
                                           SRR1803617.15433.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296861.2/ ENSP00000296861.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.3"
     Protein         1..655
                     /product="tumor necrosis factor receptor superfamily
                     member 21 precursor"
                     /note="death receptor 6; TNFR-related death receptor 6;
                     tumor necrosis factor receptor superfamily member 21"
                     /calculated_mol_wt=67789
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4075
     mat_peptide     42..655
                     /product="Tumor necrosis factor receptor superfamily
                     member 21. /id=PRO_0000034602"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
                     /calculated_mol_wt=67789
     Region          50..88
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          53..211
                     /region_name="TNFRSF21"
                     /note="Tumor necrosis factor receptor superfamily member
                     21 (TNFRSF21), also known as death receptor (DR6);
                     cd10583"
                     /db_xref="CDD:276909"
     Region          67..88
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276909"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          90..131
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          91..131
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..186
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276909"
     Region          133..167
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          170..211
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          243..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            252
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            257
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19654028; propagated from
                     UniProtKB/Swiss-Prot (O75509.1)"
     Region          318..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Site            350..370
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75509.1)"
     Region          414..497
                     /region_name="Death_TNFRSF21"
                     /note="Death domain of tumor necrosis factor receptor
                     superfamily member 21; cd08778"
                     /db_xref="CDD:176756"
     CDS             1..655
                     /gene="TNFRSF21"
                     /gene_synonym="BM-018; CD358; DR6"
                     /coded_by="NM_014452.5:395..2362"
                     /db_xref="CCDS:CCDS4921.1"
                     /db_xref="GeneID:27242"
                     /db_xref="HGNC:HGNC:13469"
                     /db_xref="MIM:605732"
ORIGIN      
        1 mgtspsssta lascsriarr atatmiagsl lllgflsttt aqpeqkasnl igtyrhvdra
       61 tgqvltcdkc pagtyvsehc tntslrvcss cpvgtftrhe ngiekchdcs qpcpwpmiek
      121 lpcaaltdre ctcppgmfqs natcaphtvc pvgwgvrkkg tetedvrckq cargtfsdvp
      181 ssvmkckayt dclsqnlvvi kpgtketdnv cgtlpsfsss tspspgtaif prpehmethe
      241 vpsstyvpkg mnstesnssa svrpkvlssi qegtvpdnts sargkedvnk tlpnlqvvnh
      301 qqgphhrhil kllpsmeatg geksstpikg pkrghprqnl hkhfdinehl pwmivlflll
      361 vlvvivvcsi rkssrtlkkg prqdpsaive kaglkksmtp tqnrekwiyy cnghgidilk
      421 lvaaqvgsqw kdiyqflcna serevaafsn gytadheray aalqhwtirg peaslaqlis
      481 alrqhrrndv vekirglmed ttqletdkla lpmspsplsp spipspnakl ensalltvep
      541 spqdknkgff vdesepllrc dstssgssal srngsfitke kkdtvlrqvr ldpcdlqpif
      601 ddmlhflnpe elrvieeipq aedkldrlfe iigvksqeas qtlldsvysh lpdll
//
LOCUS       NP_001183980             569 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase ZFP91 isoform 2 [Homo sapiens].
ACCESSION   NP_001183980
VERSION     NP_001183980.1
DBSOURCE    REFSEQ: accession NM_001197051.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Liu,T.T., Yang,H., Zhuo,F.F., Yang,Z., Zhao,M.M., Guo,Q., Liu,Y.,
            Liu,D., Zeng,K.W. and Tu,P.F.
  TITLE     Atypical E3 ligase ZFP91 promotes small-molecule-induced E2F2
            transcription factor degradation for cancer therapy
  JOURNAL   EBioMedicine 86, 104353 (2022)
   PUBMED   36375317
  REMARK    GeneRIF: Atypical E3 ligase ZFP91 promotes small-molecule-induced
            E2F2 transcription factor degradation for cancer therapy.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Wu,W., Nelson,G.M., Koch,R., Donovan,K.A., Nowak,R.P.,
            Heavican-Foral,T.B., Nirmal,A.J., Liu,H., Yang,L., Duffy,J.,
            Powers,F., Stevenson,K.E., Jones,M.K., Ng,S.Y., Wu,G., Jain,S.,
            Xu,R., Amaka,S., Trevisani,C., Donaldson,N.L., Hagner,P.R., de
            Leval,L., Gaulard,P., Iqbal,J., Thakurta,A., Fischer,E.S.,
            Adelman,K. and Weinstock,D.M.
  TITLE     Overcoming IMiD resistance in T-cell lymphomas through potent
            degradation of ZFP91 and IKZF1
  JOURNAL   Blood 139 (13), 2024-2037 (2022)
   PUBMED   34936696
  REMARK    GeneRIF: Overcoming IMiD resistance in T-cell lymphomas through
            potent degradation of ZFP91 and IKZF1.
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Zhong,Y., Zhang,Z.H., Wang,J.Y., Xing,Y., Ri,M.H., Jin,H.L.,
            Zuo,H.X., Li,M.Y., Ma,J. and Jin,X.
  TITLE     Zinc finger protein 91 mediates necroptosis by initiating
            RIPK1-RIPK3-MLKL signal transduction in response to TNF receptor 1
            ligation
  JOURNAL   Toxicol Lett 356, 75-88 (2022)
   PUBMED   34942311
  REMARK    GeneRIF: Zinc finger protein 91 mediates necroptosis by initiating
            RIPK1-RIPK3-MLKL signal transduction in response to TNF receptor 1
            ligation.
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Wang,F., Zhang,Y., Yu,X., Teng,X.L., Ding,R., Hu,Z., Wang,A.,
            Wang,Z., Ye,Y. and Zou,Q.
  TITLE     ZFP91 disturbs metabolic fitness and antitumor activity of
            tumor-infiltrating T cells
  JOURNAL   J Clin Invest 131 (19) (2021)
   PUBMED   34403361
  REMARK    GeneRIF: ZFP91 disturbs metabolic fitness and antitumor activity of
            tumor-infiltrating T cells.
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Unoki,M., Okutsu,J. and Nakamura,Y.
  TITLE     Identification of a novel human gene, ZFP91, involved in acute
            myelogenous leukemia
  JOURNAL   Int J Oncol 22 (6), 1217-1223 (2003)
   PUBMED   12738986
  REMARK    GeneRIF: likely to play an important role in cell proliferation
            and/or anti-apoptosis, and may serve as a molecular marker for AML
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Iuchi,S.
  TITLE     Three classes of C2H2 zinc finger proteins
  JOURNAL   Cell Mol Life Sci 58 (4), 625-635 (2001)
   PUBMED   11361095
  REMARK    Review article
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Grottke,C., Mantwill,K., Dietel,M., Schadendorf,D. and Lage,H.
  TITLE     Identification of differentially expressed genes in human melanoma
            cells with acquired resistance to various antineoplastic drugs
  JOURNAL   Int J Cancer 88 (4), 535-546 (2000)
   PUBMED   11058868
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Saotome,Y., Winter,C.G. and Hirsh,D.
  TITLE     A widely expressed novel C2H2 zinc-finger protein with multiple
            consensus phosphorylation sites is conserved in mouse and man
  JOURNAL   Gene 152 (2), 233-238 (1995)
   PUBMED   7835706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001350.4, BC051743.1,
            AB056107.1, BP219969.1 and AI687439.1.
            
            Summary: The protein encoded by this gene is a member of the zinc
            finger family of proteins. The gene product contains C2H2-type
            domains, which are the classical zinc finger domains found in
            numerous nucleic acid-binding proteins. This protein functions as a
            regulator of the non-canonical NF-kappaB pathway in
            lymphotoxin-beta receptor signaling. Alternative splicing results
            in multiple transcript variants. A read-through transcript variant
            composed of ZFP91 and the downstream CNTF gene sequence has been
            identified, but it is thought to be non-coding. Read-through
            transcription of ZFP91 and CNTF has also been observed in mouse. A
            ZFP91-related pseudogene has also been identified on chromosome 2.
            [provided by RefSeq, Oct 2010].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (2) that is 1 aa shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.214008.1,
                                           SRR1660809.223180.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..569
                     /product="E3 ubiquitin-protein ligase ZFP91 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="zinc finger protein homologous to Zfp91 in mouse;
                     penta zinc finger protein; E3 ubiquitin-protein ligase
                     ZFP91; drug resistance-associated sequence in melanoma 8;
                     zinc finger protein 757; zinc finger protein 91 homolog;
                     RING-type E3 ubiquitin transferase ZFP91"
                     /calculated_mol_wt=63227
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62511; propagated from
                     UniProtKB/Swiss-Prot (Q96JP5.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62511; propagated from
                     UniProtKB/Swiss-Prot (Q96JP5.1)"
     Region          337..367
                     /region_name="Interaction with MAP3K14/NIK.
                     /evidence=ECO:0000269|PubMed:20682767"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JP5.1)"
     Region          346..365
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(350,352,354,356..357,360..361,364,378,380,384..385,
                     388..389,392,406,408,410,412..413,416..417,420)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          373..393
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          400..421
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          401..421
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          431..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..569
                     /gene="ZFP91"
                     /gene_synonym="DMS-8; DSM-8; DSM8; FKSG11; PZF; ZFP-91;
                     ZNF757"
                     /coded_by="NM_001197051.2:220..1929"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:80829"
                     /db_xref="HGNC:HGNC:14983"
                     /db_xref="MIM:619289"
ORIGIN      
        1 mpgeteeprp peqqdqegge aakaapeepq qrppeavaaa pagttssrvl rggrdrgraa
       61 aaaaaaavsr rrkaeyprrr rsspsarppd vpgqqpqaak spspvqgkks prllciekvt
      121 tdkdpkeeke eeddsalpqe vsiaasrpsr gwrssrtsvs rhrdtentrs srsktgslql
      181 icksepntdq ldydvgeehq spggiseeee eeeeemlise eeipfkddpr detykphler
      241 etpkprrksg kvkeekekke ikvevevevk eeeneirede epprkrgrrr kddksprlpk
      301 rrkkppiqyv rcemegcgtv lahprylqhh ikyqhllkkk yvcphpscgr lfrlqkqllr
      361 hakhhtdqrd yiceycaraf ksshnlavhr mihtgekplq ceicgftcrq kaslnwhmkk
      421 hdadsfyqfs cnicgkkfek kdsvvahkak shpevliaea laanagalit stdilgtnpe
      481 sltqpsdgqg lpllpeplgn stsgecllle aegmsksycs gtervslmad gkifvgsgss
      541 ggteglvmns dilgattevl iedsdsagp
//
LOCUS       NP_005654                528 aa            linear   PRI 20-NOV-2025
DEFINITION  negative elongation factor A [Homo sapiens].
ACCESSION   NP_005654
VERSION     NP_005654.4
DBSOURCE    REFSEQ: accession NM_005663.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Ohe,S., Kubota,Y., Yamaguchi,K., Takagi,Y., Nashimoto,J.,
            Kozuka-Hata,H., Oyama,M., Furukawa,Y. and Takekawa,M.
  TITLE     ERK-mediated NELF-A phosphorylation promotes transcription
            elongation of immediate-early genes by releasing promoter-proximal
            pausing of RNA polymerase II
  JOURNAL   Nat Commun 13 (1), 7476 (2022)
   PUBMED   36463234
  REMARK    GeneRIF: ERK-mediated NELF-A phosphorylation promotes transcription
            elongation of immediate-early genes by releasing promoter-proximal
            pausing of RNA polymerase II.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Rawat,P., Boehning,M., Hummel,B., Aprile-Garcia,F., Pandit,A.S.,
            Eisenhardt,N., Khavaran,A., Niskanen,E., Vos,S.M., Palvimo,J.J.,
            Pichler,A., Cramer,P. and Sawarkar,R.
  TITLE     Stress-induced nuclear condensation of NELF drives transcriptional
            downregulation
  JOURNAL   Mol Cell 81 (5), 1013-1026 (2021)
   PUBMED   33548202
  REMARK    GeneRIF: Stress-induced nuclear condensation of NELF drives
            transcriptional downregulation.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Ping,Y.H. and Rana,T.M.
  TITLE     DSIF and NELF interact with RNA polymerase II elongation complex
            and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA
            polymerase II and DSIF during transcription elongation
  JOURNAL   J Biol Chem 276 (16), 12951-12958 (2001)
   PUBMED   11112772
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Wright,T.J., Costa,J.L., Naranjo,C., Francis-West,P. and
            Altherr,M.R.
  TITLE     Comparative analysis of a novel gene from the
            Wolf-Hirschhorn/Pitt-Rogers-Danks syndrome critical region
  JOURNAL   Genomics 59 (2), 203-212 (1999)
   PUBMED   10409432
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Yamaguchi,Y., Takagi,T., Wada,T., Yano,K., Furuya,A., Sugimoto,S.,
            Hasegawa,J. and Handa,H.
  TITLE     NELF, a multisubunit complex containing RD, cooperates with DSIF to
            repress RNA polymerase II elongation
  JOURNAL   Cell 97 (1), 41-51 (1999)
   PUBMED   10199401
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Wright,T.J., Ricke,D.O., Denison,K., Abmayr,S., Cotter,P.D.,
            Hirschhorn,K., Keinanen,M., McDonald-McGinn,D., Somer,M.,
            Spinner,N., Yang-Feng,T., Zackai,E. and Altherr,M.R.
  TITLE     A transcript map of the newly defined 165 kb Wolf-Hirschhorn
            syndrome critical region
  JOURNAL   Hum Mol Genet 6 (2), 317-324 (1997)
   PUBMED   9063753
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002764.2 and AB044549.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 27, 2018 this sequence version replaced NP_005654.3.
            
            Summary: This gene is expressed ubiquitously with higher levels in
            fetal than in adult tissues. It encodes a protein sharing 93%
            sequence identity with the mouse protein. Wolf-Hirschhorn syndrome
            (WHS) is a malformation syndrome associated with a hemizygous
            deletion of the distal short arm of chromosome 4. This gene is
            mapped to the 165 kb WHS critical region, and may play a role in
            the phenotype of the WHS or Pitt-Rogers-Danks syndrome. The encoded
            protein is found to be capable of reacting with HLA-A2-restricted
            and tumor-specific cytotoxic T lymphocytes, suggesting a target for
            use in specific immunotherapy for a large number of cancer
            patients. This protein has also been shown to be a member of the
            NELF (negative elongation factor) protein complex that participates
            in the regulation of RNA polymerase II transcription elongation.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.510001.1, BC002764.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382882.9/ ENSP00000372335.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..528
                     /product="negative elongation factor A"
                     /note="wolf-Hirschhorn syndrome candidate 2 protein"
                     /calculated_mol_wt=57146
     Region          125..188
                     /region_name="NELF-C/D-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01183"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Region          189..248
                     /region_name="RNAPII-binding.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01183"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Region          215..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Region          320..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3P2.3)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H3P2.3)"
     CDS             1..528
                     /gene="NELFA"
                     /gene_synonym="NELF-A; P/OKcl.15; WHSC2"
                     /coded_by="NM_005663.5:16..1602"
                     /db_xref="CCDS:CCDS3358.3"
                     /db_xref="GeneID:7469"
                     /db_xref="HGNC:HGNC:12768"
                     /db_xref="MIM:606026"
ORIGIN      
        1 masmresdtg lwlhnklgat delwappsia slltaavidn irlcfhglss avklklllgt
       61 lhlprrtvde mkgalmeiiq lasldsdpwv lmvadilksf pdtgslnlel eeqnpnvqdi
      121 lgelrekvge ceasamlple cqylnknalt tlagpltppv khfqlkrkpk satlraellq
      181 kstetaqqlk rsagvpfhak grgllrkmdt ttplkgipkq apfrsptaps vfsptgnrtp
      241 ippsrtllrk ergvklldis eldmvgagre akrrrktlda evvekpakee tvvenatpdy
      301 aaglvstqkl gslnnepalp stsylpstps vvpassyips setppapssr easrppeeps
      361 apsptlpaqf kqrapmynsg lspatptpaa ptspltpttp pavapttqtp pvamvapqtq
      421 apaqqqpkkn lsltreqmfa aqemfktank vtrpekalil gfmagsrenp cqeqgdviqi
      481 klsehtedlp kadgqgsttm lvdtvfemny atgqwtrfkk ykpmtnvs
//
LOCUS       NP_001164163             839 aa            linear   PRI 20-NOV-2025
DEFINITION  cancer-associated gene 1 protein isoform 1 [Homo sapiens].
ACCESSION   NP_001164163
VERSION     NP_001164163.1
DBSOURCE    REFSEQ: accession NM_001170692.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 839)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 839)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 839)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   4  (residues 1 to 839)
  AUTHORS   Kim,Y., Park,D., Kim,H., Choi,M., Lee,H., Lee,Y.S., Choe,J.,
            Kim,Y.M. and Jeoung,D.
  TITLE     miR-200b and cancer/testis antigen CAGE form a feedback loop to
            regulate the invasion and tumorigenic and angiogenic responses of a
            cancer cell line to microtubule-targeting drugs
  JOURNAL   J Biol Chem 288 (51), 36502-36518 (2013)
   PUBMED   24174534
  REMARK    GeneRIF: CAGE and miR-200b form a feedback regulatory loop.
REFERENCE   5  (residues 1 to 839)
  AUTHORS   Kunze,E. and Schlott,T.
  TITLE     High frequency of promoter methylation of the 14-3-3 sigma and
            CAGE-1 genes, but lack of hypermethylation of the caveolin-1 gene,
            in primary adenocarcinomas and signet ring cell carcinomas of the
            urinary bladder
  JOURNAL   Int J Mol Med 20 (4), 557-563 (2007)
   PUBMED   17786288
  REMARK    GeneRIF: The present data suggest that promoter methylation of the
            14-3-3 sigma and CAGE-1 genes plays a crucial role during the
            phenotypical morphogenesis of vesical adenocarcinomas including
            signet ring cell carcinomas by an epigenetic mechanism.
REFERENCE   6  (residues 1 to 839)
  AUTHORS   Parmigiani,R.B., Bettoni,F., Vibranovski,M.D., Lopes,M.H.,
            Martins,W.K., Cunha,I.W., Soares,F.A., Simpson,A.J., de Souza,S.J.
            and Camargo,A.A.
  TITLE     Characterization of a cancer/testis (CT) antigen gene family
            capable of eliciting humoral response in cancer patients
  JOURNAL   Proc Natl Acad Sci U S A 103 (48), 18066-18071 (2006)
   PUBMED   17114284
  REMARK    GeneRIF: CTSP-1 should be considered a promising candidate for
            cancer immunotherapy
REFERENCE   7  (residues 1 to 839)
  AUTHORS   Kunze,E., Wendt,M. and Schlott,T.
  TITLE     Promoter hypermethylation of the 14-3-3 sigma, SYK and CAGE-1 genes
            is related to the various phenotypes of urinary bladder carcinomas
            and associated with progression of transitional cell carcinomas
  JOURNAL   Int J Mol Med 18 (4), 547-557 (2006)
   PUBMED   16964403
  REMARK    GeneRIF: The different patterns of aberrant methylation of the
            CAGE-1 gene in the various histopathological cancer types of the
            urinary bladder point to a role in tumor cell differentiation.
REFERENCE   8  (residues 1 to 839)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 839)
  AUTHORS   Park,S., Lim,Y., Lee,D., Cho,B., Bang,Y.J., Sung,S., Kim,H.Y.,
            Kim,D.K., Lee,Y.S., Song,Y. and Jeoung,D.I.
  TITLE     Identification and characterization of a novel cancer/testis
            antigen gene CAGE-1
  JOURNAL   Biochim Biophys Acta 1625 (2), 173-182 (2003)
   PUBMED   12531476
  REMARK    GeneRIF: identification and characterization of CAGE-1 gene;
            displays testis-specific expression among normal tissues, and wide
            expression among various cancer tissues and cancer cell lines
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL139095.15.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments, including macaque AB070119.1.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000502583.6/ ENSP00000425493.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..839
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..839
                     /product="cancer-associated gene 1 protein isoform 1"
                     /note="cancer/testis antigen 95; cancer/testis antigen 3;
                     cancer-associated gene 1 protein; cancer/testis antigen
                     gene 1"
                     /calculated_mol_wt=97520
     Region          30..517
                     /region_name="CAGE1"
                     /note="Cancer-associated gene protein 1 family; pfam15066"
                     /db_xref="CDD:464481"
     Region          <432..>643
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..839
                     /gene="CAGE1"
                     /gene_synonym="bA69L16.7; CT3; CT95; CTAG3"
                     /coded_by="NM_001170692.2:565..3084"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54965.1"
                     /db_xref="GeneID:285782"
                     /db_xref="HGNC:HGNC:21622"
                     /db_xref="MIM:608304"
ORIGIN      
        1 mnkdyqkfws spsdpvhfev dtshekvesm sesdtmnvsn lsqgvmlshs picmettgtt
       61 cdlpqneikn fereneyest lcedaygtld nllndnnien ystnaliqpv dtisisslrq
      121 fetvckfhwv eafddemtek pefqsqvyny akdnnikqds fkeenpmets vsantdqlgn
      181 eyfrqppprs pplihcsgem lkftekslak siakesalnp sqppsflckt avpskeiqny
      241 geipemsvsy ekevtaegve rpeivstwss agiswrseac rencempdwe qsaeslqpvq
      301 edmalnevlq klkhtnrkqe vriqelqcsn lylekrvkel qmkitkqqvf idvinklken
      361 veeliedkyk iilekndtkk tlqnleevla ntqkhlqesr ndkemlqlqf kkikanyvcl
      421 qerymtemqq knksvsqyle mdktlskkee everlqqlkk elekatasal dllkrekeaq
      481 eqeflslqee fqklekenle erqklksrle klltqvrnlq fmsenertkn iklqqqinev
      541 knenaklkqq varseeqnyv pkfetaqlkd qleevlksdi tkdtktthsn llpdcspcee
      601 rlnpadikra sqlaskmhsl lalmvglltc qdiinsdaeh fkesekvsdi mlqklkslhl
      661 kkktldkell khkdrittfr eliakekafq dhaikvidcd sdeaksirdv ptllgakldk
      721 yhslneeldf litklghlle skenhcnrli eendkyqrhl gnlikkvtsy eeiiecadqr
      781 laishsqiah leernkhled lirkprekar kprskslenh pksmtmmpal fkenrndld
//
LOCUS       NP_001335144             455 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform s [Homo sapiens].
ACCESSION   NP_001335144
VERSION     NP_001335144.1
DBSOURCE    REFSEQ: accession NM_001348215.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013587.10, AK096862.1,
            BM011452.1 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (21) differs in the 5' UTR, lacks
            a portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 3. The resulting
            isoform (s) is shorter at the N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.828292.1,
                                           SRR3476690.155671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..455
                     /product="transcription factor 4 isoform s"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=48453
     Region          346..430
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(354,358,360..362,364,369,390..391)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(367..368,371..372,374..375,378,382,392,395,399,402,
                     405..410)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..455
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348215.2:205..1572"
                     /note="isoform s is encoded by transcript variant 21"
                     /db_xref="CCDS:CCDS86671.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mqdghhssdp wssssgmnqp gyagmlgnss hipqsssycs lhpherlsyp shssadinss
       61 lppmstfhrs gtnhystssc tppangtdsi manrgsgaag ssqtgdalgk alasiyspdh
      121 tnnsfssnps tpvgsppsls agtavwsrng gqassspnye gplhslqsri edrlerldda
      181 ihvlrnhavg pstampgghg dmhgiigpsh ngamgglgsg ygtgllsanr hslmvgthre
      241 dgvalrgshs llpnqvpvpq lpvqsatspd lnppqdpyrg mppglqgqsv ssgsseiksd
      301 degdenlqdt kssedkkldd dkkdiksitr srssnndded ltpeqkaere kerrmannar
      361 erlrvrdine afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr ernlnpkaac
      421 lkrreeekvs seppplslag phpgmgdasn hmgqm
//
LOCUS       NP_001293144            1081 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 827 isoform 1 [Homo sapiens].
ACCESSION   NP_001293144 XP_011529946
VERSION     NP_001293144.1
DBSOURCE    REFSEQ: accession NM_001306215.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1081)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1081)
  AUTHORS   Kim,K.Y., Kim,J.O., Kim,Y.S., Choi,J.E., Park,J.M., Han,K.,
            Park,D.H., Park,Y.C., Kim,B.T. and Hong,K.W.
  TITLE     Genome-wide association of individual vulnerability with
            alcohol-associated liver disease: A Korean genome and epidemiology
            study
  JOURNAL   Hepatology 75 (2), 391-402 (2022)
   PUBMED   34387878
  REMARK    GeneRIF: Genome-wide association of individual vulnerability with
            alcohol-associated liver disease: A Korean genome and epidemiology
            study.
REFERENCE   3  (residues 1 to 1081)
  AUTHORS   Hollensen,A.K., Thomsen,H.S., Lloret-Llinares,M., Kamstrup,A.B.,
            Jensen,J.M., Luckmann,M., Birkmose,N., Palmfeldt,J., Jensen,T.H.,
            Hansen,T.B. and Damgaard,C.K.
  TITLE     circZNF827 nucleates a transcription inhibitory complex to balance
            neuronal differentiation
  JOURNAL   Elife 9, e58478 (2020)
   PUBMED   33174841
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1081)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1081)
  AUTHORS   Yang,S.F., Sun,A.A., Shi,Y., Li,F. and Pickett,H.A.
  TITLE     Structural and functional characterization of the RBBP4-ZNF827
            interaction and its role in NuRD recruitment to telomeres
  JOURNAL   Biochem J 475 (16), 2667-2679 (2018)
   PUBMED   30045876
  REMARK    GeneRIF: RBBP4 forms a negatively charged channel that binds to
            ZNF827 through a network of electrostatic interactions.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1081)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   7  (residues 1 to 1081)
  AUTHORS   Chambers,J.C., Zhang,W., Sehmi,J., Li,X., Wass,M.N., Van der
            Harst,P., Holm,H., Sanna,S., Kavousi,M., Baumeister,S.E.,
            Coin,L.J., Deng,G., Gieger,C., Heard-Costa,N.L., Hottenga,J.J.,
            Kuhnel,B., Kumar,V., Lagou,V., Liang,L., Luan,J., Vidal,P.M., Mateo
            Leach,I., O'Reilly,P.F., Peden,J.F., Rahmioglu,N., Soininen,P.,
            Speliotes,E.K., Yuan,X., Thorleifsson,G., Alizadeh,B.Z.,
            Atwood,L.D., Borecki,I.B., Brown,M.J., Charoen,P., Cucca,F.,
            Das,D., de Geus,E.J., Dixon,A.L., Doring,A., Ehret,G.,
            Eyjolfsson,G.I., Farrall,M., Forouhi,N.G., Friedrich,N.,
            Goessling,W., Gudbjartsson,D.F., Harris,T.B., Hartikainen,A.L.,
            Heath,S., Hirschfield,G.M., Hofman,A., Homuth,G., Hypponen,E.,
            Janssen,H.L., Johnson,T., Kangas,A.J., Kema,I.P., Kuhn,J.P.,
            Lai,S., Lathrop,M., Lerch,M.M., Li,Y., Liang,T.J., Lin,J.P.,
            Loos,R.J., Martin,N.G., Moffatt,M.F., Montgomery,G.W., Munroe,P.B.,
            Musunuru,K., Nakamura,Y., O'Donnell,C.J., Olafsson,I.,
            Penninx,B.W., Pouta,A., Prins,B.P., Prokopenko,I., Puls,R.,
            Ruokonen,A., Savolainen,M.J., Schlessinger,D., Schouten,J.N.,
            Seedorf,U., Sen-Chowdhry,S., Siminovitch,K.A., Smit,J.H.,
            Spector,T.D., Tan,W., Teslovich,T.M., Tukiainen,T.,
            Uitterlinden,A.G., Van der Klauw,M.M., Vasan,R.S., Wallace,C.,
            Wallaschofski,H., Wichmann,H.E., Willemsen,G., Wurtz,P., Xu,C.,
            Yerges-Armstrong,L.M., Abecasis,G.R., Ahmadi,K.R., Boomsma,D.I.,
            Caulfield,M., Cookson,W.O., van Duijn,C.M., Froguel,P., Matsuda,K.,
            McCarthy,M.I., Meisinger,C., Mooser,V., Pietilainen,K.H.,
            Schumann,G., Snieder,H., Sternberg,M.J., Stolk,R.P., Thomas,H.C.,
            Thorsteinsdottir,U., Uda,M., Waeber,G., Wareham,N.J.,
            Waterworth,D.M., Watkins,H., Whitfield,J.B., Witteman,J.C.,
            Wolffenbuttel,B.H., Fox,C.S., Ala-Korpela,M., Stefansson,K.,
            Vollenweider,P., Volzke,H., Schadt,E.E., Scott,J., Jarvelin,M.R.,
            Elliott,P. and Kooner,J.S.
  CONSRTM   Alcohol Genome-wide Association (AlcGen) Consortium; Diabetes
            Genetics Replication and Meta-analyses (DIAGRAM+) Study; Genetic
            Investigation of Anthropometric Traits (GIANT) Consortium; Global
            Lipids Genetics Consortium; Genetics of Liver Disease (GOLD)
            Consortium; International Consortium for Blood Pressure
            (ICBP-GWAS); Meta-analyses of Glucose and Insulin-Related Traits
            Consortium (MAGIC)
  TITLE     Genome-wide association study identifies loci influencing
            concentrations of liver enzymes in plasma
  JOURNAL   Nat Genet 43 (11), 1131-1138 (2011)
   PUBMED   22001757
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1081)
  AUTHORS   Kim,Y.J., Go,M.J., Hu,C., Hong,C.B., Kim,Y.K., Lee,J.Y.,
            Hwang,J.Y., Oh,J.H., Kim,D.J., Kim,N.H., Kim,S., Hong,E.J.,
            Kim,J.H., Min,H., Kim,Y., Zhang,R., Jia,W., Okada,Y., Takahashi,A.,
            Kubo,M., Tanaka,T., Kamatani,N., Matsuda,K., Park,T., Oh,B.,
            Kimm,K., Kang,D., Shin,C., Cho,N.H., Kim,H.L., Han,B.G., Lee,J.Y.
            and Cho,Y.S.
  CONSRTM   MAGIC consortium
  TITLE     Large-scale genome-wide association studies in East Asians identify
            new genetic loci influencing metabolic traits
  JOURNAL   Nat Genet 43 (10), 990-995 (2011)
   PUBMED   21909109
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1081)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 1081)
  AUTHORS   Bubb,K.L., Bovee,D., Buckley,D., Haugen,E., Kibukawa,M.,
            Paddock,M., Palmieri,A., Subramanian,S., Zhou,Y., Kaul,R., Green,P.
            and Olson,M.V.
  TITLE     Scan of human genome reveals no new Loci under ancient balancing
            selection
  JOURNAL   Genetics 173 (4), 2165-2177 (2006)
   PUBMED   16751668
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX112429.1, AK225805.1, AK091130.1, AK094136.1, BC033248.1 and
            BU616184.1.
            
            On Apr 16, 2015 this sequence version replaced XP_011529946.1.
            
            Transcript Variant: This variant (1) represents longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225805.1, BC117407.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000508784.6/ ENSP00000421863.1
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1081
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.21-q31.22"
     Protein         1..1081
                     /product="zinc finger protein 827 isoform 1"
                     /calculated_mol_wt=119035
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          1..14
                     /region_name="Mediates direct interaction with RBBP4.
                     /evidence=ECO:0000269|PubMed:30045876"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          3..5
                     /region_name="RRK motif, mediates NuRD recruitment to
                     telomeres. /evidence=ECO:0000269|PubMed:25150861"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          259..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          307..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          355..>443
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          376..396
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(381,383,385,387..388,391..392,395,409,411,415..416,
                     419..420,423,440,442,444,446..447,450..451,454)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          404..424
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          435..455
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          819..839
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(824,826,828,830..831,834..835,838,852,854..856,
                     858..859,863,866)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          832..856
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          847..867
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          947..996
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q17R98.1)"
     Region          1021..1041
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1049..1069
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1081
                     /gene="ZNF827"
                     /coded_by="NM_001306215.2:417..3662"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS77968.1"
                     /db_xref="GeneID:152485"
                     /db_xref="HGNC:HGNC:27193"
                     /db_xref="MIM:617962"
ORIGIN      
        1 mprrkqeqpk rlpshvsrqe eaegelsege hwygnssetp seasygevqe nyklsledri
       61 qeqstspdts lgsttpssht lelvaldsev lrdslqcqdh lspgvsslcd ddpgsnkpls
      121 snlrrlleag slkldaaata ngrvespvnv gsnlsfspps hhaqqlsvla rklaekqeqn
      181 dqytpsnrfi wnqgkwlpns tttcslspds ailklkaaan avlqdksltr teetmrfesf
      241 sspfssqsas stlaalskkv sersltpgqe hpppassfls lasmtssaal lkevaaraag
      301 sllaekssll pedplpppps ekkpekvtpp pppppppppp pppqslelll lpvpkgrvsk
      361 psnsaseees gkpfqcpicg lvikrksywk rhmvihtglk shqcplcpfr carkdnlksh
      421 mkvhqhqdrg etfqcqlcpf tssrhfslkl hmrchqhflr teakvkeeip dpdvkgsphl
      481 sdsaclgqqr egggtelvgt mmtsntpert sqggagvspl lvkeepkedn glptsftlna
      541 adrpanhtkl kdpseyvans asalfsqdis vkmasdflmk lsaanqkepm nlnfkvkeep
      601 kegeslsttl prssyvfspe sevsapgvse dalkpqegkg svlrrdvsvk aasellmkls
      661 aesyketqmv kikeepmevd iqdshvsisp srnvgystli grekteplqk mpegrvpper
      721 nlfsqdisvk masellfqls ekvskehnht kentirttts pffsedtfrq spftsnskel
      781 lpsdsvlhgr isapetekiv leagnglpsw kfndqlfpcd vcgkvfgrqq tlsrhlslht
      841 eerkykchlc pyaakcranl nqhltvhsvk lvstdtediv savtsegsdg kkhpyyysch
      901 vcgfetelnv qfvshmslhv dkeqwmfsic ctacdfvtme eaeikthigt khtgedrktp
      961 sesnspssss lsalsdsans kddsdgsqkn kggnnllvis vmpgsqpsln seekpekgfe
     1021 cvfcnfvckt knmferhlqi hlitrmfecd vchkfmktpe qllehkkcht vptgglnsgq
     1081 w
//
LOCUS       NP_001340234             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 3 [Homo sapiens].
ACCESSION   NP_001340234
VERSION     NP_001340234.1
DBSOURCE    REFSEQ: accession NM_001353305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.160534.1,
                                           SRR3476690.15261.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 3"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36689
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353305.1:141..1115"
                     /note="isoform 3 is encoded by transcript variant 67"
                     /db_xref="CCDS:CCDS94340.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnlikvltr didhnaahff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_005410                851 aa            linear   PRI 20-NOV-2025
DEFINITION  signal transducer and activator of transcription 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_005410
VERSION     NP_005410.1
DBSOURCE    REFSEQ: accession NM_005419.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 851)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 851)
  AUTHORS   Huang,Z., Mai,Z., Kong,C., You,J., Lin,S., Gao,C., Zhang,W.,
            Chen,X., Xie,Q., Wang,H., Tang,S., Zhou,P., Gong,L. and Zhang,G.
  TITLE     African swine fever virus pB475L evades host antiviral innate
            immunity via targeting STAT2 to inhibit IFN-I signaling
  JOURNAL   J Biol Chem 300 (7), 107472 (2024)
   PUBMED   38879005
  REMARK    GeneRIF: African swine fever virus pB475L evades host antiviral
            innate immunity via targeting STAT2 to inhibit IFN-I signaling.
REFERENCE   3  (residues 1 to 851)
  AUTHORS   Calvo-Apalategi,A., Nevado,M.L., Bravo-Gallego,L.Y.,
            Gonzalez-Granado,L.I., Allende,L.M., Pena,R.R., Lopez-Granados,E.
            and Reyburn,H.T.
  TITLE     The lack of either IRF9, or STAT2, has surprisingly little effect
            on human natural killer cell development and function
  JOURNAL   Immunology 172 (3), 440-450 (2024)
   PUBMED   38514903
  REMARK    GeneRIF: The lack of either IRF9, or STAT2, has surprisingly little
            effect on human natural killer cell development and function.
REFERENCE   4  (residues 1 to 851)
  AUTHORS   Nowicka,H., Sekrecka,A., Blaszczyk,K., Kluzek,K., Chang,C.Y.,
            Wesoly,J., Lee,C.K. and Bluyssen,H.A.R.
  TITLE     ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced Transcription
            through Genome-Wide Binding of Phosphorylated and Unphosphorylated
            Complexes to Common ISRE-Containing ISGs
  JOURNAL   Int J Mol Sci 24 (24), 17635 (2023)
   PUBMED   38139463
  REMARK    GeneRIF: ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced
            Transcription through Genome-Wide Binding of Phosphorylated and
            Unphosphorylated Complexes to Common ISRE-Containing ISGs.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 851)
  AUTHORS   Gomes,J.A., Sgarioni,E., Boquett,J.A., Kowalski,T.W., Fraga,L.R.,
            Tercas-Trettel,A.C.P., da Silva,J.H., Ribeiro,B.F.R., Galera,M.F.,
            de Oliveira,T.M., Carvalho de Andrade,M.D.F., Carvalho,I.F.,
            Schuler-Faccini,L. and Vianna,F.S.L.
  TITLE     Investigation of the impact of AXL, TLR3, and STAT2 in congenital
            Zika syndrome through genetic polymorphisms and protein-protein
            interaction network analyses
  JOURNAL   Birth Defects Res 115 (16), 1500-1512 (2023)
   PUBMED   37526179
  REMARK    GeneRIF: Investigation of the impact of AXL, TLR3, and STAT2 in
            congenital Zika syndrome through genetic polymorphisms and
            protein-protein interaction network analyses.
REFERENCE   6  (residues 1 to 851)
  AUTHORS   Wang,Y., Song,Q., Huang,W., Lin,Y., Wang,X., Wang,C., Willard,B.,
            Zhao,C., Nan,J., Holvey-Bates,E., Wang,Z., Taylor,D., Yang,J. and
            Stark,G.R.
  TITLE     A virus-induced conformational switch of STAT1-STAT2 dimers boosts
            antiviral defenses
  JOURNAL   Cell Res 31 (2), 206-218 (2021)
   PUBMED   32759968
REFERENCE   7  (residues 1 to 851)
  AUTHORS   Uddin,S., Chamdin,A. and Platanias,L.C.
  TITLE     Interaction of the transcriptional activator Stat-2 with the type I
            interferon receptor
  JOURNAL   J Biol Chem 270 (42), 24627-24630 (1995)
   PUBMED   7559568
REFERENCE   8  (residues 1 to 851)
  AUTHORS   Marrero,M.B., Schieffer,B., Paxton,W.G., Heerdt,L., Berk,B.C.,
            Delafontaine,P. and Bernstein,K.E.
  TITLE     Direct stimulation of Jak/STAT pathway by the angiotensin II AT1
            receptor
  JOURNAL   Nature 375 (6528), 247-250 (1995)
   PUBMED   7746328
REFERENCE   9  (residues 1 to 851)
  AUTHORS   Yan,R., Qureshi,S., Zhong,Z., Wen,Z. and Darnell,J.E. Jr.
  TITLE     The genomic structure of the STAT genes: multiple exons in
            coincident sites in Stat1 and Stat2
  JOURNAL   Nucleic Acids Res 23 (3), 459-463 (1995)
   PUBMED   7885841
REFERENCE   10 (residues 1 to 851)
  AUTHORS   Fu,X.Y., Schindler,C., Improta,T., Aebersold,R. and Darnell,J.E.
            Jr.
  TITLE     The proteins of ISGF-3, the interferon alpha-induced
            transcriptional activator, define a gene family involved in signal
            transduction
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7840-7843 (1992)
   PUBMED   1502204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB482283.1 and BC051284.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the STAT
            protein family. In response to cytokines and growth factors, STAT
            family members are phosphorylated by the receptor associated
            kinases, and then form homo- or heterodimers that translocate to
            the cell nucleus where they act as transcription activators. In
            response to interferon (IFN), this protein forms a complex with
            STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in
            which this protein acts as a transactivator, but lacks the ability
            to bind DNA directly. The protein mediates innate antiviral
            activity. Mutations in this gene result in Immunodeficiency 44.
            [provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051284.1, SRR18074968.1920962.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000314128.9/ ENSP00000315768.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..851
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..851
                     /product="signal transducer and activator of transcription
                     2 isoform 1"
                     /note="interferon alpha induced transcriptional activator;
                     signal transducer and activator of transcription 2,
                     113kDa"
                     /calculated_mol_wt=97786
     Region          2..124
                     /region_name="STAT_int"
                     /note="STAT protein, protein interaction domain;
                     smart00964"
                     /db_xref="CDD:214942"
     Region          138..572
                     /region_name="Mediates interaction with USP18.
                     /evidence=ECO:0000269|PubMed:28165510"
                     /note="propagated from UniProtKB/Swiss-Prot (P52630.1)"
     Region          141..312
                     /region_name="STAT2_CCD"
                     /note="Coiled-coil domain of Signal Transducer and
                     Activator of Transcription 2 (STAT2); cd16852"
                     /db_xref="CDD:341077"
     Site            order(143..166,209..235,258..279)
                     /site_type="other"
                     /note="coiled-coil motif"
                     /db_xref="CDD:341077"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23139419; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23139419; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:23139419; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     Region          316..575
                     /region_name="Interaction with heartland virus NSs.
                     /evidence=ECO:0000269|PubMed:31040183"
                     /note="propagated from UniProtKB/Swiss-Prot (P52630.1)"
     Region          316..486
                     /region_name="Interaction with SFTSV virus NSs.
                     /evidence=ECO:0000269|PubMed:25631085"
                     /note="propagated from UniProtKB/Swiss-Prot (P52630.1)"
     Region          316..475
                     /region_name="STAT_DBD"
                     /note="DNA-binding domain of Signal Transducer and
                     Activator of Transcription (STAT); cl28920"
                     /db_xref="CDD:355796"
     Region          556..706
                     /region_name="SH2_STAT2"
                     /note="Src homology 2 (SH2) domain found in signal
                     transducer and activator of transcription (STAT) 2
                     proteins; cd10373"
                     /db_xref="CDD:198236"
     Site            order(583,601,627,629)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198236"
     Site            order(628,644)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198236"
     Site            order(638..639,695)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:198236"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by JAK.
                     /evidence=ECO:0000269|PubMed:7532278,
                     ECO:0000269|PubMed:9121453; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     Site            753
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     Region          784..838
                     /region_name="STAT2_C"
                     /note="Signal transducer and activator of transcription 2
                     C terminal; pfam12188"
                     /db_xref="CDD:432390"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52630.1)"
     CDS             1..851
                     /gene="STAT2"
                     /gene_synonym="IMD44; ISGF-3; P113; PTORCH3; STAT113"
                     /coded_by="NM_005419.4:58..2613"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8917.1"
                     /db_xref="GeneID:6773"
                     /db_xref="HGNC:HGNC:11363"
                     /db_xref="MIM:600556"
ORIGIN      
        1 maqwemlqnl dspfqdqlhq lyshsllpvd irqylavwie dqnwqeaalg sddskatmlf
       61 fhfldqlnye cgrcsqdpes lllqhnlrkf crdiqpfsqd ptqlaemifn llleekrili
      121 qaqraqleqg epvletpves qqheiesril dlrammeklv ksisqlkdqq dvfcfrykiq
      181 akgktpsldp hqtkeqkilq etlneldkrr kevldaskal lgrlttliel llpkleewka
      241 qqqkacirap idhgleqlet wftagakllf hlrqllkelk glsclvsyqd dpltkgvdlr
      301 naqvtellqr llhrafvvet qpcmpqtphr plilktgskf tvrtrllvrl qegnesltve
      361 vsidrnppql qgfrkfnilt snqktltpek gqsqgliwdf gyltlveqrs ggsgkgsnkg
      421 plgvteelhi isftvkytyq glkqelktdt lpvviisnmn qlsiawasvl wfnllspnlq
      481 nqqffsnppk apwsllgpal swqfssyvgr glnsdqlsml rnklfgqncr tedpllswad
      541 ftkresppgk lpfwtwldki lelvhdhlkd lwndgrimgf vsrsqerrll kktmsgtfll
      601 rfsesseggi tcswvehqdd dkvliysvqp ytkevlqslp lteiirhyql lteenipenp
      661 lrflypripr deafgcyyqe kvnlqerrky lkhrlivvsn rqvdelqqpl elkpepeles
      721 lelelglvpe pelsldlepl lkagldlgpe lesvlestle pvieptlcmv sqtvpepdqg
      781 pvsqpvpepd lpcdlrhlnt epmeifrncv kieeimpngd pllagqntvd evyvsrpshf
      841 ytdgplmpsd f
//
LOCUS       NP_001334965             887 aa            linear   PRI 20-NOV-2025
DEFINITION  protein PTHB1 isoform 2 [Homo sapiens].
ACCESSION   NP_001334965 XP_016867480
VERSION     NP_001334965.1
DBSOURCE    REFSEQ: accession NM_001348036.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074338.1, AC007312.1,
            AC087070.2, AC006195.1 and AC078833.5.
            
            On Jan 4, 2017 this sequence version replaced XP_016867480.1.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968832 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..887
                     /product="protein PTHB1 isoform 2"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=99150
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..819
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          685..765
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          850..887
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..887
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001348036.1:280..2943"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS43566.1"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptdrnpdgip rviqckfrlp lkliclpgqp
      541 sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf hflggaritv lasktsqryr
      601 iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi plqeyfelid hhfelringe
      661 kleellsera vqfraiqrrl larfkdktpa plqhldtlld gtykqviala daveenqgnl
      721 fqsftrlksa thlvillial wqklsadqva ileaaflplq edtqelgwee tvdaaishll
      781 ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls kggrlclstd aaapqtmvmp
      841 ggcttipesd leersveqds telftnhrhl taetprpevs plqgvse
//
LOCUS       NP_054860               1331 aa            linear   PRI 20-NOV-2025
DEFINITION  contactin-associated protein-like 2 precursor [Homo sapiens].
ACCESSION   NP_054860
VERSION     NP_054860.1
DBSOURCE    REFSEQ: accession NM_014141.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1331)
  AUTHORS   Greguletz,P., Plotz,M., Baade-Buttner,C., Bien,C.G., Eisenhut,K.,
            Geis,C., Handreka,R., Klausewitz,J., Kortvelyessy,P., Kovac,S.,
            Kraft,A., Lewerenz,J., Malter,M., Nagel,M., von Podewils,F.,
            Pruss,H., Rada,A., Rau,J., Rauer,S., Rossling,R., Seifert-Held,T.,
            Siebenbrodt,K., Suhs,K.W., Tauber,S.C., Thaler,F., Wagner,J.,
            Wickel,J., Leypoldt,F., Rittner,H.L., Sommer,C., Villmann,C. and
            Doppler,K.
  CONSRTM   GENERATE study group
  TITLE     Different pain phenotypes are associated with anti-Caspr2
            autoantibodies
  JOURNAL   J Neurol 271 (5), 2736-2744 (2024)
   PUBMED   38386048
  REMARK    GeneRIF: Different pain phenotypes are associated with anti-Caspr2
            autoantibodies.
REFERENCE   2  (residues 1 to 1331)
  AUTHORS   Ul Mudassir,B. and Agha,Z.
  TITLE     Novel and known minor alleles of CNTNAP2 gene variants are
            associated with comorbidity of intellectual disability and epilepsy
            phenotypes: a case-control association study reveals potential
            biomarkers
  JOURNAL   Mol Biol Rep 51 (1), 276 (2024)
   PUBMED   38315301
  REMARK    GeneRIF: Novel and known minor alleles of CNTNAP2 gene variants are
            associated with comorbidity of intellectual disability and epilepsy
            phenotypes: a case-control association study reveals potential
            biomarkers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1331)
  AUTHORS   Panza,N., Bianchini,C., Cetica,V., Balestrini,S., Barba,C.,
            Ferrari,A.R., Mei,D., Parmeggiani,L., Parrini,E. and Guerrini,R.
  TITLE     Bilateral temporal lobe dysplasia and seizure onset associated with
            biallelic CNTNAP2 variants
  JOURNAL   Epilepsia Open 9 (1), 417-423 (2024)
   PUBMED   37805811
  REMARK    GeneRIF: Bilateral temporal lobe dysplasia and seizure onset
            associated with biallelic CNTNAP2 variants.
REFERENCE   4  (residues 1 to 1331)
  AUTHORS   St George-Hyslop,F., Haneklaus,M., Kivisild,T. and Livesey,F.J.
  TITLE     Loss of CNTNAP2 Alters Human Cortical Excitatory Neuron
            Differentiation and Neural Network Development
  JOURNAL   Biol Psychiatry 94 (10), 780-791 (2023)
   PUBMED   37001843
  REMARK    GeneRIF: Loss of CNTNAP2 Alters Human Cortical Excitatory Neuron
            Differentiation and Neural Network Development.
REFERENCE   5  (residues 1 to 1331)
  AUTHORS   D'Onofrio,G., Accogli,A., Severino,M., Caliskan,H., Kokotovic,T.,
            Blazekovic,A., Jercic,K.G., Markovic,S., Zigman,T., Goran,K.,
            Barisic,N., Duranovic,V., Ban,A., Borovecki,F., Ramadza,D.P.,
            Baric,I., Fazeli,W., Herkenrath,P., Marini,C., Vittorini,R.,
            Gowda,V., Bouman,A., Rocca,C., Alkhawaja,I.A., Murtaza,B.N.,
            Rehman,M.M.U., Al Alam,C., Nader,G., Mancardi,M.M., Giacomini,T.,
            Srivastava,S., Alvi,J.R., Tomoum,H., Matricardi,S., Iacomino,M.,
            Riva,A., Scala,M., Madia,F., Pistorio,A., Salpietro,V., Minetti,C.,
            Riviere,J.B., Srour,M., Efthymiou,S., Maroofian,R., Houlden,H.,
            Vernes,S.C., Zara,F., Striano,P. and Nagy,V.
  TITLE     Genotype-phenotype correlation in contactin-associated protein-like
            2 (CNTNAP-2) developmental disorder
  JOURNAL   Hum Genet 142 (7), 909-925 (2023)
   PUBMED   37183190
  REMARK    GeneRIF: Genotype-phenotype correlation in contactin-associated
            protein-like 2 (CNTNAP-2) developmental disorder.
            Review article
REFERENCE   6  (residues 1 to 1331)
  AUTHORS   Denisenko-Nehrbass,N., Oguievetskaia,K., Goutebroze,L., Galvez,T.,
            Yamakawa,H., Ohara,O., Carnaud,M. and Girault,J.A.
  TITLE     Protein 4.1B associates with both Caspr/paranodin and Caspr2 at
            paranodes and juxtaparanodes of myelinated fibres
  JOURNAL   Eur J Neurosci 17 (2), 411-416 (2003)
   PUBMED   12542678
REFERENCE   7  (residues 1 to 1331)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   8  (residues 1 to 1331)
  AUTHORS   Spiegel,I., Salomon,D., Erne,B., Schaeren-Wiemers,N. and Peles,E.
  TITLE     Caspr3 and caspr4, two novel members of the caspr family are
            expressed in the nervous system and interact with PDZ domains
  JOURNAL   Mol Cell Neurosci 20 (2), 283-297 (2002)
   PUBMED   12093160
REFERENCE   9  (residues 1 to 1331)
  AUTHORS   Nakabayashi,K. and Scherer,S.W.
  TITLE     The human contactin-associated protein-like 2 gene (CNTNAP2) spans
            over 2 Mb of DNA at chromosome 7q35
  JOURNAL   Genomics 73 (1), 108-112 (2001)
   PUBMED   11352571
REFERENCE   10 (residues 1 to 1331)
  AUTHORS   Poliak,S., Gollan,L., Martinez,R., Custer,A., Einheber,S.,
            Salzer,J.L., Trimmer,J.S., Shrager,P. and Peles,E.
  TITLE     Caspr2, a new member of the neurexin superfamily, is localized at
            the juxtaparanodes of myelinated axons and associates with K+
            channels
  JOURNAL   Neuron 24 (4), 1037-1047 (1999)
   PUBMED   10624965
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073308.4, BC093780.1,
            AK315113.1 and AC083849.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the neurexin family which
            functions in the vertebrate nervous system as cell adhesion
            molecules and receptors. This protein, like other neurexin
            proteins, contains epidermal growth factor repeats and laminin G
            domains. In addition, it includes an F5/8 type C domain,
            discoidin/neuropilin- and fibrinogen-like domains, thrombospondin
            N-terminal-like domains and a putative PDZ binding site. This
            protein is localized at the juxtaparanodes of myelinated axons, and
            mediates interactions between neurons and glia during nervous
            system development and is also involved in localization of
            potassium channels within differentiating axons. This gene
            encompasses almost 1.5% of chromosome 7 and is one of the largest
            genes in the human genome. It is directly bound and regulated by
            forkhead box protein P2, a transcription factor related to speech
            and language development. This gene has been implicated in multiple
            neurodevelopmental disorders, including Gilles de la Tourette
            syndrome, schizophrenia, epilepsy, autism, ADHD and intellectual
            disability. [provided by RefSeq, Jul 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.85546.1,
                                           SRR1803616.265685.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361727.8/ ENSP00000354778.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35-q36.1"
     Protein         1..1331
                     /product="contactin-associated protein-like 2 precursor"
                     /note="cell recognition molecule Caspr2; homolog of
                     Drosophila neurexin IV; contactin associated protein like
                     2"
                     /calculated_mol_wt=145624
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2562
     Region          <70..180
                     /region_name="FA58C"
                     /note="Coagulation factor 5/8 C-terminal domain, discoidin
                     domain; Cell surface-attached carbohydrate-binding domain,
                     present in eukaryotes and assumed to have horizontally
                     transferred to eubacterial genomes; cd00057"
                     /db_xref="CDD:238014"
     Site            order(75,103,108)
                     /site_type="other"
                     /note="sugar binding site [chemical binding]"
                     /db_xref="CDD:238014"
     Region          216..345
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          375..527
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          555..590
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          598..634
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     Region          800..943
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          967..>992
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          1055..1187
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1282..1300
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1331
                     /gene="CNTNAP2"
                     /gene_synonym="AUTS15; CASPR2; CDFE; NRXN4; PTHSL1"
                     /coded_by="NM_014141.6:77..4072"
                     /db_xref="CCDS:CCDS5889.1"
                     /db_xref="GeneID:26047"
                     /db_xref="HGNC:HGNC:13830"
                     /db_xref="MIM:604569"
ORIGIN      
        1 mqaapragcg aalllwivss clcrawtaps tsqkcdeplv sglphvafss sssisgsysp
       61 gyakinkrgg aggwspsdsd hyqwlqvdfg nrkqisaiat qgrysssdwv tqyrmlysdt
      121 grnwkpyhqd gniwafpgni nsdgvvrhel qhpiiaryvr ivpldwngeg riglrievyg
      181 csywadvinf dghvvlpyrf rnkkmktlkd vialnfktse segvilhgeg qqgdyitlel
      241 kkaklvlsln lgsnqlgpiy ghtsvmtgsl lddhhwhsvv ierqgrsinl tldrsmqhfr
      301 tngefdyldl dyeitfggip fsgkpssssr knfkgcmesi nyngvnitdl arrkklepsn
      361 vgnlsfscve pytvpvffna tsylevpgrl nqdlfsvsfq frtwnpngll vfshfadnlg
      421 nveidltesk vgvhinitqt kmsqidissg sglndgqwhe vrflakenfa iltidgdeas
      481 avrtnsplqv ktgekyffgg flnqmnnssh svlqpsfqgc mqliqvddql vnlyevaqrk
      541 pgsfanvsid mcaiidrcvp nhcehggkcs qtwdsfkctc detgysgatc hnsiyepsce
      601 aykhlgqtsn yywidpdgsg plgplkvycn mtedkvwtiv shdlqmqtpv vgynpekysv
      661 tqlvysasmd qisaitdsae yceqyvsyfc kmsrllntpd gspytwwvgk anekhyywgg
      721 sgpgiqkcac giernctdpk yycncdadyk qwrkdagfls ykdhlpvsqv vvgdtdrqgs
      781 eaklsvgplr cqgdrnywna asfpnpssyl hfstfqgets adisfyfktl tpwgvflenm
      841 gkedfiklel ksatevsfsf dvgngpveiv vrsptplndd qwhrvtaern vkqaslqvdr
      901 lpqqirkapt eghtrlelys qlfvggaggq qgflgcirsl rmngvtldle erakvtsgfi
      961 sgcsghctsy gtncenggkc leryhgyscd csntaydgtf cnkdvgaffe egmwlrynfq
     1021 apatnardss srvdnapdqq nshpdlaqee irfsfsttka pcillyissf ttdflavlvk
     1081 ptgslqiryn lggtrepyni dvdhrnmang qphsvnitrh ektiflkldh ypsvsyhlps
     1141 ssdtlfnspk slflgkviet gkidqeihky ntpgftgcls rvqfnqiapl kaalrqtnas
     1201 ahvhiqgelv esncgasplt lspmssatdp whldhldsas adfpynpgqg qairngvnrn
     1261 saiiggviav viftilctlv flirymfrhk gtyhtneakg aesaesadaa imnndpnfte
     1321 tideskkewl i
//
LOCUS       NP_005079                695 aa            linear   PRI 20-NOV-2025
DEFINITION  A-kinase anchor protein 17A isoform 1 [Homo sapiens].
ACCESSION   NP_005079
VERSION     NP_005079.2
DBSOURCE    REFSEQ: accession NM_005088.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Jarnaess,E., Stokka,A.J., Kvissel,A.K., Skalhegg,B.S.,
            Torgersen,K.M., Scott,J.D., Carlson,C.R. and Tasken,K.
  TITLE     Splicing factor arginine/serine-rich 17A (SFRS17A) is an A-kinase
            anchoring protein that targets protein kinase A to splicing factor
            compartments
  JOURNAL   J Biol Chem 284 (50), 35154-35164 (2009)
   PUBMED   19840947
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Mangs,A.H., Speirs,H.J., Goy,C., Adams,D.J., Markus,M.A. and
            Morris,B.J.
  TITLE     XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265
  JOURNAL   Nucleic Acids Res 34 (17), 4976-4986 (2006)
   PUBMED   16982639
  REMARK    GeneRIF: The spliceosomal component XE7 resembles an SR-related
            splicing protein, and can influence alternative splicing.
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Ried,K., Rao,E., Schiebel,K. and Rappold,G.A.
  TITLE     Gene duplications as a recurrent theme in the evolution of the
            human pseudoautosomal region 1: isolation of the gene ASMTL
  JOURNAL   Hum Mol Genet 7 (11), 1771-1778 (1998)
   PUBMED   9736779
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Ellison,J.W., Ramos,C., Yen,P.H. and Shapiro,L.J.
  TITLE     Structure and expression of the human pseudoautosomal gene XE7
  JOURNAL   Hum Mol Genet 1 (9), 691-696 (1992)
   PUBMED   1302606
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Voland,J.R., Wyzykowski,R.J., Huang,M. and Dutton,R.W.
  TITLE     Cloning and sequencing of a trophoblast-endothelial-activated
            lymphocyte surface protein: cDNA sequence and genomic structure
  JOURNAL   Proc Natl Acad Sci U S A 89 (21), 10425-10429 (1992)
   PUBMED   1438229
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC016935.1, BC028151.1,
            BC015800.1, BM713425.1, M99578.1 and BM046630.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 23, 2004 this sequence version replaced NP_005079.1.
            
            Summary: This locus encodes a protein kinase A anchoring protein.
            The encoded protein is part of the spliceosome complex and is
            involved in the regulation of alternate splicing in some mRNA
            precursors. Alternatively spliced transcript variants have been
            identified for this gene.[provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.115823.1,
                                           SRR3476690.948348.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313871.9/ ENSP00000324827.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /chromosome="Y"
                     /map="X"
                     /map="Y"
     Protein         1..695
                     /product="A-kinase anchor protein 17A isoform 1"
                     /note="splicing factor, arginine/serine-rich 17A; A-kinase
                     anchor protein 17A; B-lymphocyte surface antigen;
                     pseudoautosomal gene XE7; protein kinase A-anchoring
                     protein 17A; A kinase (PRKA) anchor protein 17A"
                     /calculated_mol_wt=80605
     Region          83..112
                     /region_name="PKA-RI and PKA-RII subunit binding domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          143..265
                     /region_name="RRM_AKAP17A"
                     /note="RNA recognition motif (RRM) found in A-kinase
                     anchor protein 17A (AKAP-17A) and similar proteins;
                     cd12264"
                     /db_xref="CDD:409708"
     Region          279..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          <329..>443
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          425..454
                     /region_name="PKA-RI-alpha subunit binding domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Region          482..695
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02040.2)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q02040.2)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q02040.2)"
     CDS             1..695
                     /gene="AKAP17A"
                     /gene_synonym="721P; AKAP-17A; CCDC133; CXYorf3; DXYS155E;
                     PRKA17A; SFRS17A; XE7; XE7Y"
                     /coded_by="NM_005088.3:186..2273"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14116.1"
                     /db_xref="GeneID:8227"
                     /db_xref="HGNC:HGNC:18783"
                     /db_xref="MIM:312095"
                     /db_xref="MIM:465000"
ORIGIN      
        1 maaativhdt seavelcpay glylkpitkm tisvalpqlk qpgksisnwe vmerlkgmvq
       61 nhqfstlris kstmdfirfe gevenkslvk sflacldgkt iklsgfsdil kvraaefkid
      121 fptrhdwdsf frdakdmnet lpgerpdtih leglpckwfa lkesgsekps edvlvkvfek
      181 fgeirnvdip mldpyreemt grnfhtfsfg ghlnfeayvq yreymgfiqa msalrgmklm
      241 ykgedgkava cnikvsfdst khlsdasikk rqlerqklqe leqqreeqkr rekeaeerqr
      301 aeerkqkele elererkree klrkreqkqr drelrrnqkk leklqaeeqk qlqekiklee
      361 rklllaqrnl qsirliaell srakavklre qeqkeeklrl qqqeerrrlq eaelrrveee
      421 keralglqrk erelrerlls illskkpdds hthdelgvah adllqpvldi lqtvssgcvs
      481 attlhplggq ppagapkesp ahpeadgapk svngsvaeea pckevqsscr vvpedgspek
      541 rcpggvlsci pdnnqqpkgi paceqnvsrk dtrseqdkcn repskgrgra tgdgladrhk
      601 rersrarras sredgrprke rrphkkhayk ddsprrrsts pdhtrsrrsh skdrhrrers
      661 rerrgsasrk hsrhrrrser srsrspsrhr stwnr
//
LOCUS       NP_001308434             261 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-10 isoform 11 [Homo sapiens].
ACCESSION   NP_001308434
VERSION     NP_001308434.1
DBSOURCE    REFSEQ: accession NM_001321505.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.19008.1,
                                           SRR18074969.868491.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..261
                     /product="septin-10 isoform 11"
                     /calculated_mol_wt=30548
     Region          <1..138
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            15..18
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            69..71
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..261
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321505.2:336..1121"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 mknldskvni ipviakadtv sktelqkfki klmselvsng vqiyqfptdd dtiakvnaam
       61 ngqlpfavvg smdevkvgnk mvkarqypwg vvqvenenhc dfvklremli ctnmedlreq
      121 thtrhyelyr rckleemgft dvgpenkpvs vqetyeakrh efhgerqrke eemkqmfvqr
      181 vkekeailke aerelqakfe hlkrlhqeer mkleekrrll eeeiiafskk katseifhsq
      241 sflatgsnlr kdkdrknsnf l
//
LOCUS       NP_001354584             855 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform w [Homo sapiens].
ACCESSION   NP_001354584
VERSION     NP_001354584.1
DBSOURCE    REFSEQ: accession NM_001367655.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968189,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..855
                     /product="SUN domain-containing protein 1 isoform w"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=94881
     Region          12..372
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <446..>642
                     /region_name="rad50"
                     /note="TIGR00606"
                     /db_xref="CDD:129694"
     Region          488..540
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(490..491,494,497..498,501..502,504..505,508..509,
                     511..512,515..516,518..519,522,525..526,529,532..533,
                     536..537,539..540)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          617..675
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          718..853
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..855
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367655.1:105..2672"
                     /note="isoform w is encoded by transcript variant 23"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy
      241 ygrmnvrevl redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca
      301 gyfllqilrr igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv
      361 flltrclrni ckflvllipl flllaglslr gqgnffsflp vlnwasmhrt qrvddpqdvf
      421 kpttsrlkqp lqgdseafpw hwmsgveqqv aslsgqchhh genlrelttl lqklqarvdq
      481 meggaagpsa stdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq
      541 llptvehlql eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl
      601 eqllqrfssq fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi
      661 teaqaraivn salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy
      721 fsqsprvviq pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap
      781 kdfavyglen eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe
      841 ytclyrfrvh gepvk
//
LOCUS       NP_001357514             209 aa            linear   PRI 20-NOV-2025
DEFINITION  tudor-interacting repair regulator protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001357514
VERSION     NP_001357514.1
DBSOURCE    REFSEQ: accession NM_001370585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI823073.1, DRR138528.751381.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..209
                     /product="tudor-interacting repair regulator protein
                     isoform 3"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=22948
     Site            10
                     /site_type="other"
                     /note="Required for interaction with TP53BP1.
                     /evidence=ECO:0000269|PubMed:28241136; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ7.1)"
     Region          23..192
                     /region_name="NUDIX_U8_SnoRNA_DE_Nudt16"
                     /note="nucleoside diphosphate-linked moiety X)) motif 16;
                     cd18869"
                     /db_xref="CDD:467581"
     Region          116..203
                     /region_name="Interaction with PXN.
                     /evidence=ECO:0000250|UniProtKB:Q8VHN8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRJ7.1)"
     CDS             1..209
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001370585.1:10..639"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lmrfdgllgf
       61 pggfvdrrfw sledglnrvl glglgclrlt eadylsshlt egphrvvahl yarqltleql
      121 haveisavhs rdhglevlgl vrvplytqkd rvggfpnfls nafvstakcq llfalkvlnm
      181 mpeeklveal aaatekqkka lekllpass
//
LOCUS       NP_001350809             616 aa            linear   PRI 20-NOV-2025
DEFINITION  methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
            isoform 3 [Homo sapiens].
ACCESSION   NP_001350809 XP_006713765
VERSION     NP_001350809.1
DBSOURCE    REFSEQ: accession NM_001363880.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 616)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 616)
  AUTHORS   Feng,Y., Huang,J., Wang,F., Lin,Z., Luo,H., Li,Q., Wang,X., Liu,X.,
            Zhai,X., Gao,Q., Li,L., Zhang,Y., Wen,J., Zhang,L., Niu,T. and
            Zheng,Y.
  TITLE     Methylcrotonyl-CoA carboxylase subunit 1 (MCCA) regulates multidrug
            resistance in multiple myeloma
  JOURNAL   Life Sci 333, 122157 (2023)
   PUBMED   37805164
  REMARK    GeneRIF: Methylcrotonyl-CoA carboxylase subunit 1 (MCCA) regulates
            multidrug resistance in multiple myeloma.
REFERENCE   3  (residues 1 to 616)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 616)
  AUTHORS   Lim,J.L., Ng,E.Y., Lim,S.Y., Tan,A.H., Abdul-Aziz,Z., Ibrahim,K.A.,
            Gopalai,A.A., Tay,Y.W., Vijayanathan,Y., Toh,T.S., Lim,S.K.,
            Bee,P.C., Puvanarajah,S.D., Viswanathan,S., Looi,I., Lim,T.T.,
            Eow,G.B., Cheah,W.K., Tan,E.K. and Ahmad-Annuar,A.
  TITLE     Association study of MCCC1/LAMP3 and DGKQ variants with Parkinson's
            disease in patients of Malay ancestry
  JOURNAL   Neurol Sci 42 (10), 4203-4207 (2021)
   PUBMED   33559030
  REMARK    GeneRIF: Association study of MCCC1/LAMP3 and DGKQ variants with
            Parkinson's disease in patients of Malay ancestry.
REFERENCE   5  (residues 1 to 616)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 616)
  AUTHORS   Holzinger,A., Roschinger,W., Lagler,F., Mayerhofer,P.U.,
            Lichtner,P., Kattenfeld,T., Thuy,L.P., Nyhan,W.L., Koch,H.G.,
            Muntau,A.C. and Roscher,A.A.
  TITLE     Cloning of the human MCCA and MCCB genes and mutations therein
            reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase
            deficiency
  JOURNAL   Hum Mol Genet 10 (12), 1299-1306 (2001)
   PUBMED   11406611
REFERENCE   7  (residues 1 to 616)
  AUTHORS   Obata,K., Fukuda,T., Morishita,R., Abe,S., Asakawa,S.,
            Yamaguchi,S., Yoshino,M., Ihara,K., Murayama,K., Shigemoto,K.,
            Shimizu,N. and Kondo,I.
  TITLE     Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
            gene (MCCA): cDNA sequence, genomic organization, localization to
            chromosomal band 3q27, and expression
  JOURNAL   Genomics 72 (2), 145-152 (2001)
   PUBMED   11401427
REFERENCE   8  (residues 1 to 616)
  AUTHORS   Baumgartner,M.R., Almashanu,S., Suormala,T., Obie,C., Cole,R.N.,
            Packman,S., Baumgartner,E.R. and Valle,D.
  TITLE     The molecular basis of human 3-methylcrotonyl-CoA carboxylase
            deficiency
  JOURNAL   J Clin Invest 107 (4), 495-504 (2001)
   PUBMED   11181649
REFERENCE   9  (residues 1 to 616)
  AUTHORS   Gallardo,M.E., Desviat,L.R., Rodriguez,J.M., Esparza-Gordillo,J.,
            Perez-Cerda,C., Perez,B., Rodriguez-Pombo,P., Criado,O., Sanz,R.,
            Morton,D.H., Gibson,K.M., Le,T.P., Ribes,A., de Cordoba,S.R.,
            Ugarte,M. and Penalva,M.A.
  TITLE     The molecular basis of 3-methylcrotonylglycinuria, a disorder of
            leucine catabolism
  JOURNAL   Am J Hum Genet 68 (2), 334-346 (2001)
   PUBMED   11170888
REFERENCE   10 (residues 1 to 616)
  AUTHORS   Elpeleg,O.N., Havkin,S., Barash,V., Jakobs,C., Glick,B. and
            Shalev,R.S.
  TITLE     Familial hypotonia of childhood caused by isolated
            3-methylcrotonyl-coenzyme A carboxylase deficiency
  JOURNAL   J Pediatr 121 (3), 407-410 (1992)
   PUBMED   1517917
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104641.11 and AC108741.9.
            
            On Jun 3, 2018 this sequence version replaced XP_006713765.1.
            
            Summary: This gene encodes the large subunit of
            3-methylcrotonyl-CoA carboxylase. This enzyme functions as a
            heterodimer and catalyzes the carboxylation of 3-methylcrotonyl-CoA
            to form 3-methylglutaconyl-CoA. Mutations in this gene are
            associated with 3-Methylcrotonylglycinuria, an autosomal recessive
            disorder of leucine catabolism. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.756223.1,
                                           SRR1803613.61727.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 16023992, 11401427;
                                                  reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..616
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..616
                     /product="methylcrotonoyl-CoA carboxylase subunit alpha,
                     mitochondrial isoform 3"
                     /EC_number="6.4.1.4"
                     /note="3-methylcrotonyl-CoA carboxylase biotin-containing
                     subunit; methylcrotonoyl-Coenzyme A carboxylase 1 (alpha);
                     methylcrotonoyl-CoA carboxylase subunit alpha,
                     mitochondrial; 3-methylcrotonyl-CoA:carbon dioxide ligase
                     subunit alpha; MCCase subunit alpha; 3-methylcrotonyl-CoA
                     carboxylase 1; methylcrotonoyl-CoA carboxylase 1 (alpha);
                     methylcrotonoyl-CoA carboxylase alpha"
                     /calculated_mol_wt=68201
     Region          1..395
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          542..605
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(562,571..573,580)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            572
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..616
                     /gene="MCCC1"
                     /gene_synonym="MCC-B; MCCA; MCCCalpha"
                     /coded_by="NM_001363880.1:338..2188"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS87170.1"
                     /db_xref="GeneID:56922"
                     /db_xref="HGNC:HGNC:6936"
                     /db_xref="MIM:609010"
ORIGIN      
        1 mekiiqvakt saaqaihpgc gflsenmefa elckqegiif igpppsaird mgikstsksi
       61 maaagvpvve gyhgedqsdq clkeharrig ypvmikavrg gggkgmrivr seqefqeqle
      121 sarreakksf nddamliekf vdtprhvevq vfgdhhgnav ylferdcsvq rrhqkiieea
      181 papgiksevr kklgeaavra akavnyvgag tvefimdskh nfcfmemntr lqvehpvtem
      241 itgtdlvewq lriaagekip lsqeeitlqg hafeariyae dpsnnfmpva gplvhlstpr
      301 adpstrietg vrqgdevsvh ydpmiaklvv waadrqaalt klryslrqyn ivglhtnidf
      361 llnlsghpef eagnvhtdfi pqhhkqllls rkaaakeslc qaalglilke kamtdtftlq
      421 ahdqfspfss ssgrrlnisy trnmtlkdgk nnvaiavtyn hdgsysmqie dktfqvlgnl
      481 ysegdctylk csvngvaska kliilentiy lfskegsiei dipvpkylss vssqetqggp
      541 lapmtgtiek vfvkagdkvk agdslmvmia mkmehtiksp kdgtvkkvfy regaqanrht
      601 plvefeeees dkrese
//
LOCUS       NP_001357496             761 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001357496 XP_016857545
VERSION     NP_001357496.1
DBSOURCE    REFSEQ: accession NM_001370567.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_016857545.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.62185.1,
                                           SRR1660803.122934.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..761
                     /product="semaphorin-4A isoform 1 precursor"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=80167
     sig_peptide     1..32
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
                     /calculated_mol_wt=3425
     mat_peptide     33..761
                     /product="semaphorin-4A isoform 1"
                     /calculated_mol_wt=80167
     Region          55..495
                     /region_name="Sema_4A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4A (Sema4A); cd11256"
                     /db_xref="CDD:200517"
     Site            order(115..117,178,199,201..202,204,219,222,224,229,252,
                     276..280,282,361..362,386,390,393)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200517"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            order(253..254,256,259..261,295,297..299,301,303,326..328,
                     334..335,399,411)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200517"
     Region          496..540
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          566..638
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          576..580
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          588..592
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          607..611
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          621..626
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Site            684..704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          722..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     CDS             1..761
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001370567.1:32..2317"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS1132.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 malpalgldp wsllglflfq llqlllpttt aggggqgpmp rvryyagder ralsffhqkg
       61 lqdfdtllls gdgntlyvga reailaldiq dpgvprlknm ipwpasdrkk secafkkksn
      121 etqcfnfirv lvsynvthly tcgtfafspa ctfielqdsy llpisedkvm egkgqspfdp
      181 ahkhtavlvd gmlysgtmnn flgsepilmr tlgsqpvlkt dnflrwlhhd asfvaaipst
      241 qvvyfffeet asefdfferl htsrvarvck ndvggekllq kkwttflkaq llctqpgqlp
      301 fnvirhavll padsptaphi yavftsqwqv ggtrssavca fslldiervf kgkykelnke
      361 tsrwttyrgp etnprpgscs vgpssdkalt fmkdhflmde qvvgtpllvk sgveytrlav
      421 etaqgldghs hlvmylgttt gslhkavvsg dssahlveei qlfpdpepvr nlqlaptqga
      481 vfvgfsggvw rvprancsvy escvdcvlar dphcawdpes rtccllsapn lnswkqdmer
      541 gnpewacasg pmsrslrpqs rpqiikevla vpnsilelpc phlsalasyy wshgpaavpe
      601 asstvyngsl llivqdgvgg lyqcwateng fsypvisywv dsqdqtlald pelagipreh
      661 vkvpltrvsg gaalaaqqsy wphfvtvtvl falvlsgali ilvasplral rargkvqgce
      721 tlrpgekapl sreqhlqspk ecrtsasdvd adnnclgtev a
//
LOCUS       NP_001240308             204 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL15 isoform 1 [Homo sapiens].
ACCESSION   NP_001240308
VERSION     NP_001240308.1
DBSOURCE    REFSEQ: accession NM_001253379.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Wang,G., Qin,M., Zhang,B., Yan,Y., Yang,F., Chen,Q., Liu,Y.,
            Qiao,F. and Ni,Y.
  TITLE     Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification
  JOURNAL   Cell Biol Int 47 (10), 1749-1759 (2023)
   PUBMED   37431269
  REMARK    GeneRIF: Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification.
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Xu,C., He,X.Y., Ren,X.H., Han,D. and Cheng,S.X.
  TITLE     Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin in
            Living Circulating Tumor Cells at Single Cell Resolution To Study
            Tumor Heterogeneity
  JOURNAL   Anal Chem 94 (30), 10610-10616 (2022)
   PUBMED   35856393
  REMARK    GeneRIF: Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin
            in Living Circulating Tumor Cells at Single Cell Resolution To
            Study Tumor Heterogeneity.
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Wang,Q., Yang,C., Zhou,J., Wang,X., Wu,M. and Liu,Z.
  TITLE     Cloning and characterization of full-length human ribosomal protein
            L15 cDNA which was overexpressed in esophageal cancer
  JOURNAL   Gene 263 (1-2), 205-209 (2001)
   PUBMED   11223259
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI544251.1, AC124914.3,
            DA037869.1 and AI886077.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L15E family of ribosomal proteins and a component of the 60S
            subunit. This gene shares sequence similarity with the yeast
            ribosomal protein YL10 gene. Elevated expression of this gene has
            been observed in esophageal tumors and gastric cancer tissues, and
            deletion of this gene has been observed in a Diamond-Blackfan
            anemia (DBA) patient. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.253098.1,
                                           SRR1803614.102664.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..204
                     /product="large ribosomal subunit protein eL15 isoform 1"
                     /note="60S ribosomal protein L15; large ribosomal subunit
                     protein eL15"
                     /calculated_mol_wt=24015
     Region          2..191
                     /region_name="Ribosomal_L15e"
                     /note="Ribosomal L15; pfam00827"
                     /db_xref="CDD:459950"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61314; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P61313.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Region          165..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61313.2)"
     CDS             1..204
                     /gene="RPL15"
                     /gene_synonym="DBA12; EC45; eL15; L15; RPL10; RPLY10;
                     RPYL10"
                     /coded_by="NM_001253379.2:653..1267"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2640.1"
                     /db_xref="GeneID:6138"
                     /db_xref="HGNC:HGNC:10306"
                     /db_xref="MIM:604174"
ORIGIN      
        1 mgaykyiqel wrkkqsdvmr fllrvrcwqy rqlsalhrap rptrpdkarr lgykakqgyv
       61 iyrirvrrgg rkrpvpkgat ygkpvhhgvn qlkfarslqs vaeeragrhc galrvlnsyw
      121 vgedstykff evilidpfhk airrnpdtqw itkpvhkhre mrgltsagrk srglgkghkf
      181 hhtiggsrra awrrrntlql hryr
//
LOCUS       NP_000670                520 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-1B adrenergic receptor [Homo sapiens].
ACCESSION   NP_000670
VERSION     NP_000670.1
DBSOURCE    REFSEQ: accession NM_000679.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Su,M., Wang,J., Xiang,G., Do,H.N., Levitz,J., Miao,Y. and
            Huang,X.Y.
  TITLE     Structural basis of agonist specificity of alpha1A-adrenergic
            receptor
  JOURNAL   Nat Commun 14 (1), 4819 (2023)
   PUBMED   37563160
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Masukawa,D., Takahagi,R., Nakao,Y. and Goshima,Y.
  TITLE     L-DOPA Receptor GPR143 Functionally Couples with Adrenergic alpha1B
            Receptor at the Second Transmembrane Interface
  JOURNAL   Biol Pharm Bull 46 (7), 869-873 (2023)
   PUBMED   37394637
  REMARK    GeneRIF: L-DOPA Receptor GPR143 Functionally Couples with
            Adrenergic alpha1B Receptor at the Second Transmembrane Interface.
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Renkhold,L., Kollmann,R., Inderwiedenstrasse,L. and Kienitz,M.C.
  TITLE     PKC-isoform specific regulation of receptor desensitization and
            KCNQ1/KCNE1 K+ channel activity by mutant alpha1B-adrenergic
            receptors
  JOURNAL   Cell Signal 91, 110228 (2022)
   PUBMED   34958868
  REMARK    GeneRIF: PKC-isoform specific regulation of receptor
            desensitization and KCNQ1/KCNE1 K(+) channel activity by mutant
            alpha1B-adrenergic receptors.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Gao,X., Enten,G.A., DeSantis,A.J., Volkman,B.F., Gaponenko,V. and
            Majetschak,M.
  TITLE     Characterization of heteromeric complexes between chemokine (C-X-C
            motif) receptor 4 and alpha1-adrenergic receptors utilizing
            intermolecular bioluminescence resonance energy transfer assays
  JOURNAL   Biochem Biophys Res Commun 528 (2), 368-375 (2020)
   PUBMED   32085899
  REMARK    GeneRIF: Characterization of heteromeric complexes between
            chemokine (C-X-C motif) receptor 4 and alpha1-adrenergic receptors
            utilizing intermolecular bioluminescence resonance energy transfer
            assays.
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Hernandez-Espinosa,D.A., Reyes-Cruz,G. and Garcia-Sainz,J.A.
  TITLE     Roles of the G protein-coupled receptor kinase 2 and Rab5 in
            alpha1B-adrenergic receptor function and internalization
  JOURNAL   Eur J Pharmacol 867, 172846 (2020)
   PUBMED   31811856
  REMARK    GeneRIF: Study data indicate that GRK2 and RAB5 play key roles in
            alpha1B-adrenergic receptor phosphorylation, internalization, and
            desensitization. The possibility that RAB5 might form part of a
            signaling complex is suggested, as well as that GDP-Rab5 might
            interfere with the ability of GRK2 to catalyze alpha1B-adrenergic
            receptor phosphorylation.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Warrington,J.A. and Bengtsson,U.
  TITLE     High-resolution physical mapping of human 5q31-q33 using three
            methods: radiation hybrid mapping, interphase fluorescence in situ
            hybridization, and pulsed-field gel electrophoresis
  JOURNAL   Genomics 24 (2), 395-398 (1994)
   PUBMED   7698768
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Ramarao,C.S., Denker,J.M., Perez,D.M., Gaivin,R.J., Riek,R.P. and
            Graham,R.M.
  TITLE     Genomic organization and expression of the human alpha
            1B-adrenergic receptor
  JOURNAL   J Biol Chem 267 (30), 21936-21945 (1992)
   PUBMED   1328250
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Allen,L.F., Lefkowitz,R.J., Caron,M.G. and Cotecchia,S.
  TITLE     G-protein-coupled receptor genes as protooncogenes: constitutively
            activating mutation of the alpha 1B-adrenergic receptor enhances
            mitogenesis and tumorigenicity
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 11354-11358 (1991)
   PUBMED   1662393
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Lomasney,J.W., Cotecchia,S., Lorenz,W., Leung,W.Y., Schwinn,D.A.,
            Yang-Feng,T.L., Brownstein,M., Lefkowitz,R.J. and Caron,M.G.
  TITLE     Molecular cloning and expression of the cDNA for the alpha
            1A-adrenergic receptor. The gene for which is located on human
            chromosome 5
  JOURNAL   J Biol Chem 266 (10), 6365-6369 (1991)
   PUBMED   1706716
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Yang-Feng,T.L., Xue,F.Y., Zhong,W.W., Cotecchia,S., Frielle,T.,
            Caron,M.G., Lefkowitz,R.J. and Francke,U.
  TITLE     Chromosomal organization of adrenergic receptor genes
  JOURNAL   Proc Natl Acad Sci U S A 87 (4), 1516-1520 (1990)
   PUBMED   2154750
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011343.3, U03865.1,
            BQ576306.1 and AC068657.6.
            
            Summary: Alpha-1-adrenergic receptors (alpha-1-ARs) are members of
            the G protein-coupled receptor superfamily. They activate mitogenic
            responses and regulate growth and proliferation of many cells.
            There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of
            which signal through the Gq/11 family of G-proteins and different
            subtypes show different patterns of activation. This gene encodes
            alpha-1B-adrenergic receptor, which induces neoplastic
            transformation when transfected into NIH 3T3 fibroblasts and other
            cell lines. Thus, this normal cellular gene is identified as a
            protooncogene. This gene comprises 2 exons and a single large
            intron of at least 20 kb that interrupts the coding region.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U03865.1, BC136568.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306675.5/ ENSP00000306662.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..520
                     /product="alpha-1B adrenergic receptor"
                     /note="alpha-1B adrenoceptor; alpha-1B adrenoreceptor;
                     adrenergic, alpha-1B-, receptor"
                     /calculated_mol_wt=56705
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            24
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Site            34
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Region          46..359
                     /region_name="7tmA_alpha1B_AR"
                     /note="alpha-1 adrenergic receptors subtype B, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15326"
                     /db_xref="CDD:320449"
     Site            46..70
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          47..73
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320449"
     Region          80..106
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320449"
     Site            84..105
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Site            116..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          118..148
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320449"
     Site            order(121,125..126,129..130,197,204,207..208,211,307,
                     310..311,314,330,334,338)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320449"
     Region          160..183
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320449"
     Site            162..184
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          200..229
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320449"
     Site            202..224
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P97717; propagated from
                     UniProtKB/Swiss-Prot (P35368.3)"
     Region          287..317
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320449"
     Site            296..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          327..352
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320449"
     Site            327..351
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          368..380
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          394..432
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     Region          479..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35368.3)"
     CDS             1..520
                     /gene="ADRA1B"
                     /gene_synonym="ADRA1; ALPHA1BAR"
                     /coded_by="NM_000679.4:425..1987"
                     /db_xref="CCDS:CCDS4347.1"
                     /db_xref="GeneID:147"
                     /db_xref="HGNC:HGNC:278"
                     /db_xref="MIM:104220"
ORIGIN      
        1 mnpdldtghn tsapahwgel knanftgpnq tssnstlpql ditraisvgl vlgafilfai
       61 vgnilvilsv acnrhlrtpt nyfivnlama dlllsftvlp fsaalevlgy wvlgrifcdi
      121 waavdvlcct asilslcais idryigvrys lqyptlvtrr kailallsvw vlstvisigp
      181 llgwkepapn ddkecgvtee pfyalfsslg sfyiplavil vmycrvyiva krttknleag
      241 vmkemsnske ltlrihsknf hedtlsstka kghnprssia vklfkfsrek kaaktlgivv
      301 gmfilcwlpf fialplgslf stlkppdavf kvvfwlgyfn sclnpiiypc sskefkrafv
      361 rilgcqcrgr grrrrrrrrr lggcaytyrp wtrggslers qsrkdsldds gsclsgsqrt
      421 lpsaspspgy lgrgapppve lcafpewkap gallslpape ppgrrgrhds gplftfkllt
      481 epespgtdgg asnggceaaa dvangqpgfk snmplapgqf
//
LOCUS       NP_620116                192 aa            linear   PRI 20-NOV-2025
DEFINITION  apoptosis regulator BAX isoform alpha [Homo sapiens].
ACCESSION   NP_620116
VERSION     NP_620116.1
DBSOURCE    REFSEQ: accession NM_138761.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Dadsena,S., Cuevas Arenas,R., Vieira,G., Brodesser,S., Melo,M.N.
            and Garcia-Saez,A.J.
  TITLE     Lipid unsaturation promotes BAX and BAK pore activity during
            apoptosis
  JOURNAL   Nat Commun 15 (1), 4700 (2024)
   PUBMED   38830851
  REMARK    GeneRIF: Lipid unsaturation promotes BAX and BAK pore activity
            during apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Schweighofer,S.V., Jans,D.C., Keller-Findeisen,J., Folmeg,A.,
            Ilgen,P., Bates,M. and Jakobs,S.
  TITLE     Endogenous BAX and BAK form mosaic rings of variable size and
            composition on apoptotic mitochondria
  JOURNAL   Cell Death Differ 31 (4), 469-478 (2024)
   PUBMED   38503846
  REMARK    GeneRIF: Endogenous BAX and BAK form mosaic rings of variable size
            and composition on apoptotic mitochondria.
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Liu,X., Zhang,J., Wang,Z., Yan,M., Xu,M., Li,G., Shender,V.,
            Wei,J.J., Li,J., Shao,C., Zhang,S., Kong,B., Song,K. and Liu,Z.
  TITLE     Splicing Factor PQBP1 Curtails BAX Expression to Promote Ovarian
            Cancer Progression
  JOURNAL   Adv Sci (Weinh) 11 (15), e2306229 (2024)
   PUBMED   38342602
  REMARK    GeneRIF: Splicing Factor PQBP1 Curtails BAX Expression to Promote
            Ovarian Cancer Progression.
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Chen,Y., Li,S., Yang,Z., Wang,T., Yin,F., Zhao,X. and Zhang,Y.
  TITLE     Value of Bax and Bcl2 expression in peripheral blood mononuclear
            cells for clinical prognosis of patients with chronic heart failure
  JOURNAL   Medicine (Baltimore) 103 (3), e36943 (2024)
   PUBMED   38241555
  REMARK    GeneRIF: Value of Bax and Bcl2 expression in peripheral blood
            mononuclear cells for clinical prognosis of patients with chronic
            heart failure.
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Salomons,G.S., Buitenhuis,C.K., Martinez Munoz,C.,
            Verwijs-Jassen,M., Behrendt,H., Zsiros,J. and Smets,L.A.
  TITLE     Mutational analysis of Bax and Bcl-2 in childhood acute
            lymphoblastic leukaemia
  JOURNAL   Int J Cancer 79 (3), 273-277 (1998)
   PUBMED   9645350
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Apte,S.S., Mattei,M.G. and Olsen,B.R.
  TITLE     Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and
            isolation of a novel alternatively spliced transcript, BAX delta
  JOURNAL   Genomics 26 (3), 592-594 (1995)
   PUBMED   7607685
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Miyashita,T. and Reed,J.C.
  TITLE     Tumor suppressor p53 is a direct transcriptional activator of the
            human bax gene
  JOURNAL   Cell 80 (2), 293-299 (1995)
   PUBMED   7834749
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Krieger,N.S., Sessler,N.E. and Bushinsky,D.A.
  TITLE     Acidosis inhibits osteoblastic and stimulates osteoclastic activity
            in vitro
  JOURNAL   Am J Physiol 262 (3 Pt 2), F442-F448 (1992)
   PUBMED   1558161
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE396495.1, BC014175.2 and
            AI565203.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the BCL2
            protein family. BCL2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. This protein forms a
            heterodimer with BCL2, and functions as an apoptotic activator. The
            association and the ratio of BAX to BCL2 also determines survival
            or death of a cell following an apoptotic stimulus. This protein is
            reported to interact with, and increase the opening of, the
            mitochondrial voltage-dependent anion channel (VDAC), which leads
            to the loss in membrane potential and the release of cytochrome c.
            The expression of this gene is regulated by the tumor suppressor
            P53 and has been shown to be involved in P53-mediated apoptosis.
            Multiple alternatively spliced transcript variants, which encode
            different isoforms, have been reported for this gene. [provided by
            RefSeq, Dec 2019].
            
            Transcript Variant: This variant (alpha) has an alternate splice
            site in the 3' coding region which causes a frame-shift, compared
            to variant 1. The resulting isoform (alpha, also known as psi) has
            a shorter and different C terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014175.2, SRR1163657.238306.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345358.12/ ENSP00000263262.9
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..192
                     /product="apoptosis regulator BAX isoform alpha"
                     /note="apoptosis regulator BAX; bcl2-L-4; bcl-2-like
                     protein 4; BCL2-associated X protein omega; Baxdelta2G9;
                     BCL2 associated X protein; Baxdelta2omega;
                     Baxdelta2G9omega; Baxdelta2(G8)-RFS protein"
                     /calculated_mol_wt=21053
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q07812.1)"
     Region          5..192
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          59..73
                     /region_name="BH3. /evidence=ECO:0000269|PubMed:8521816"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     Site            63..71
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(66..67,69..70,76,79..80,90..91,94..95,98..99,106,
                     108..109,111..112,116,120,164)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          98..118
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     Site            order(98..100,105..117)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          150..165
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     Site            150..164
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            172..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     CDS             1..192
                     /gene="BAX"
                     /gene_synonym="BCL2L4"
                     /coded_by="NM_138761.4:55..633"
                     /note="isoform alpha is encoded by transcript variant
                     alpha"
                     /db_xref="CCDS:CCDS12742.1"
                     /db_xref="GeneID:581"
                     /db_xref="HGNC:HGNC:959"
                     /db_xref="MIM:600040"
ORIGIN      
        1 mdgsgeqprg ggptsseqim ktgalllqgf iqdragrmgg eapelaldpv pqdastkkls
       61 eclkrigdel dsnmelqrmi aavdtdspre vffrvaadmf sdgnfnwgrv valfyfaskl
      121 vlkalctkvp elirtimgwt ldflrerllg wiqdqggwdg llsyfgtptw qtvtifvagv
      181 ltasltiwkk mg
//
LOCUS       NP_079085                697 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_079085
VERSION     NP_079085.2
DBSOURCE    REFSEQ: accession NM_024809.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Liu,Q., Zhu,C. and Dong,Y.
  TITLE     LncRNA TCTN2 Promotes the Malignant Development of Hepatocellular
            Carcinoma via Regulating mIR-1285-3p/ARF6 Axis
  JOURNAL   Recent Pat Anticancer Drug Discov 18 (4), 517-527 (2023)
   PUBMED   36278455
  REMARK    GeneRIF: LncRNA TCTN2 Promotes the Malignant Development of
            Hepatocellular Carcinoma via Regulating mIR-1285-3p/ARF6 Axis.
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Litz Philipsborn,S., Hartmajer,S., Shtorch Asor,A., Vinovezky,M.,
            Regev,M., Singer,A. and Reinstein,E.
  TITLE     A founder mutation in TCTN2 causes Meckel-Gruber syndrome type 8
            among Jews of Ethiopian and Yemenite origin
  JOURNAL   Am J Med Genet A 185 (5), 1610-1613 (2021)
   PUBMED   33590725
  REMARK    GeneRIF: A founder mutation in TCTN2 causes Meckel-Gruber syndrome
            type 8 among Jews of Ethiopian and Yemenite origin.
REFERENCE   5  (residues 1 to 697)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 697)
  AUTHORS   Shaheen,R., Faqeih,E., Seidahmed,M.Z., Sunker,A., Alali,F.E.,
            AlQahtani,K. and Alkuraya,F.S.
  TITLE     A TCTN2 mutation defines a novel Meckel Gruber syndrome locus
  JOURNAL   Hum Mutat 32 (6), 573-578 (2011)
   PUBMED   21462283
  REMARK    GeneRIF: a truncating mutation in TCTN2 linked to Meckel Gruber
            syndrome was shown.
REFERENCE   7  (residues 1 to 697)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
  REMARK    GeneRIF: Network building strategy led to the proposal of
            candidates for new ciliopathy disease genes, leading to the
            identification of the first human mutations in the Nephronophthisis
            gene Ataxin10 (ATXN10) and Joubert syndrome gene Tectonic2 (TCTN2).
REFERENCE   8  (residues 1 to 697)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 697)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 697)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292153.1, BC009112.1 and
            BQ774678.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 4, 2003 this sequence version replaced NP_079085.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the tectonic family. Studies in mice suggest that this protein
            may be involved in hedgehog signaling, and essential for
            ciliogenesis. Mutations in this gene are associated with Meckel
            syndrome type 8. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ278870.1, AK056924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303372.7/ ENSP00000304941.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..697
                     /product="tectonic-2 isoform 1 precursor"
                     /calculated_mol_wt=74052
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
                     /calculated_mol_wt=2838
     mat_peptide     26..697
                     /product="Tectonic-2. /id=PRO_0000229798"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GX1.1)"
                     /calculated_mol_wt=74052
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Region          171..444
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     Site            391
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            669..689
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GX1.1)"
     CDS             1..697
                     /gene="TCTN2"
                     /gene_synonym="C12orf38; JBTS24; MKS8; TECT2"
                     /coded_by="NM_024809.5:129..2222"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9253.1"
                     /db_xref="GeneID:79867"
                     /db_xref="HGNC:HGNC:25774"
                     /db_xref="MIM:613846"
ORIGIN      
        1 mgfqppaall lrlfllqgil rllwgdlafi ppfirmsgpa vsaslvgdte gvtvslavlq
       61 deagilpipt cgvlnneted wsvtvipgak vlevtvrwkr gldwcssnet dsfsespcil
      121 qtllvsashn sscsahlliq veiyansslt hnasenvtvi pnqvyqplgp cpcnltagac
      181 dvrcccdqec ssnlttlfrr scftgvfggd vnppfdqlcs agtttrgvpd wfpflcvqsp
      241 lantpflgyf yhgavspkqd ssfevyvdtd akdfadfgyk qgdpimtvkk ayftipqvsl
      301 agqcmqnapv aflhnfdvkc vtnlelyqer dgiinakikn valggivtpk viyeeatdld
      361 kfitntetpl nngstprivn veehyifkwn nntiseinvk ifraeinahq kgimtqrfvv
      421 kflsynsgne eelsgnpgyq lgkpvralni nrmnnvttlh lwqsagrglc tsatfkpilf
      481 genvlsgcll evginenctq lrenaverld sliqathvam rgnsdyadls dgwleiirvd
      541 apdpgadpla ssvngmcldi pahlsirili sdagavegit qqeilgvetr fssvnwqyqc
      601 gltcehkadl lpisasvqfi kipaqlphpl trfqinytey dcnrnevcwp qllypwtqyy
      661 qgelhsqcva kglllllflt lalflsnpwt rickays
//
LOCUS       NP_001350665             479 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein AEBP2 isoform d [Homo sapiens].
ACCESSION   NP_001350665 XP_006719094
VERSION     NP_001350665.1
DBSOURCE    REFSEQ: accession NM_001363736.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Grau,D., Zhang,Y., Lee,C.H., Valencia-Sanchez,M., Zhang,J.,
            Wang,M., Holder,M., Svetlov,V., Tan,D., Nudler,E., Reinberg,D.,
            Walz,T. and Armache,K.J.
  TITLE     Structures of monomeric and dimeric PRC2:EZH1 reveal flexible
            modules involved in chromatin compaction
  JOURNAL   Nat Commun 12 (1), 714 (2021)
   PUBMED   33514705
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Kasinath,V., Beck,C., Sauer,P., Poepsel,S., Kosmatka,J., Faini,M.,
            Toso,D., Aebersold,R. and Nogales,E.
  TITLE     JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and
            other histone modifications
  JOURNAL   Science 371 (6527) (2021)
   PUBMED   33479123
  REMARK    GeneRIF: JARID2 and AEBP2 regulate PRC2 in the presence of
            H2AK119ub1 and other histone modifications.
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Zhang,Q., Wang,W. and Gao,Q.
  TITLE     beta-TRCP-mediated AEBP2 ubiquitination and destruction controls
            cisplatin resistance in ovarian cancer
  JOURNAL   Biochem Biophys Res Commun 523 (1), 274-279 (2020)
   PUBMED   31864706
  REMARK    GeneRIF: beta-TRCP-mediated AEBP2 ubiquitination and destruction
            controls cisplatin resistance in ovarian cancer.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Kasinath,V., Faini,M., Poepsel,S., Reif,D., Feng,X.A.,
            Stjepanovic,G., Aebersold,R. and Nogales,E.
  TITLE     Structures of human PRC2 with its cofactors AEBP2 and JARID2
  JOURNAL   Science 359 (6378), 940-944 (2018)
   PUBMED   29348366
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Ciferri,C., Lander,G.C., Maiolica,A., Herzog,F., Aebersold,R. and
            Nogales,E.
  TITLE     Molecular architecture of human polycomb repressive complex 2
  JOURNAL   Elife 1, e00005 (2012)
   PUBMED   23110252
  REMARK    GeneRIF: The first three-dimensional structure of the human
            polycomb repressive complex 2 complex bound to its cofactor AEBP2
            has been presented.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Soler Artigas,M., Loth,D.W., Wain,L.V., Gharib,S.A., Obeidat,M.,
            Tang,W., Zhai,G., Zhao,J.H., Smith,A.V., Huffman,J.E., Albrecht,E.,
            Jackson,C.M., Evans,D.M., Cadby,G., Fornage,M., Manichaikul,A.,
            Lopez,L.M., Johnson,T., Aldrich,M.C., Aspelund,T., Barroso,I.,
            Campbell,H., Cassano,P.A., Couper,D.J., Eiriksdottir,G.,
            Franceschini,N., Garcia,M., Gieger,C., Gislason,G.K., Grkovic,I.,
            Hammond,C.J., Hancock,D.B., Harris,T.B., Ramasamy,A.,
            Heckbert,S.R., Heliovaara,M., Homuth,G., Hysi,P.G., James,A.L.,
            Jankovic,S., Joubert,B.R., Karrasch,S., Klopp,N., Koch,B.,
            Kritchevsky,S.B., Launer,L.J., Liu,Y., Loehr,L.R., Lohman,K.,
            Loos,R.J., Lumley,T., Al Balushi,K.A., Ang,W.Q., Barr,R.G.,
            Beilby,J., Blakey,J.D., Boban,M., Boraska,V., Brisman,J.,
            Britton,J.R., Brusselle,G.G., Cooper,C., Curjuric,I., Dahgam,S.,
            Deary,I.J., Ebrahim,S., Eijgelsheim,M., Francks,C., Gaysina,D.,
            Granell,R., Gu,X., Hankinson,J.L., Hardy,R., Harris,S.E.,
            Henderson,J., Henry,A., Hingorani,A.D., Hofman,A., Holt,P.G.,
            Hui,J., Hunter,M.L., Imboden,M., Jameson,K.A., Kerr,S.M.,
            Kolcic,I., Kronenberg,F., Liu,J.Z., Marchini,J., McKeever,T.,
            Morris,A.D., Olin,A.C., Porteous,D.J., Postma,D.S., Rich,S.S.,
            Ring,S.M., Rivadeneira,F., Rochat,T., Sayer,A.A., Sayers,I.,
            Sly,P.D., Smith,G.D., Sood,A., Starr,J.M., Uitterlinden,A.G.,
            Vonk,J.M., Wannamethee,S.G., Whincup,P.H., Wijmenga,C.,
            Williams,O.D., Wong,A., Mangino,M., Marciante,K.D., McArdle,W.L.,
            Meibohm,B., Morrison,A.C., North,K.E., Omenaas,E., Palmer,L.J.,
            Pietilainen,K.H., Pin,I., Pola Sbreve Ek,O., Pouta,A., Psaty,B.M.,
            Hartikainen,A.L., Rantanen,T., Ripatti,S., Rotter,J.I., Rudan,I.,
            Rudnicka,A.R., Schulz,H., Shin,S.Y., Spector,T.D., Surakka,I.,
            Vitart,V., Volzke,H., Wareham,N.J., Warrington,N.M., Wichmann,H.E.,
            Wild,S.H., Wilk,J.B., Wjst,M., Wright,A.F., Zgaga,L., Zemunik,T.,
            Pennell,C.E., Nyberg,F., Kuh,D., Holloway,J.W., Boezen,H.M.,
            Lawlor,D.A., Morris,R.W., Probst-Hensch,N., Kaprio,J., Wilson,J.F.,
            Hayward,C., Kahonen,M., Heinrich,J., Musk,A.W., Jarvis,D.L.,
            Glaser,S., Jarvelin,M.R., Ch Stricker,B.H., Elliott,P.,
            O'Connor,G.T., Strachan,D.P., London,S.J., Hall,I.P., Gudnason,V.
            and Tobin,M.D.
  CONSRTM   International Lung Cancer Consortium; GIANT consortium
  TITLE     Genome-wide association and large-scale follow up identifies 16 new
            loci influencing lung function
  JOURNAL   Nat Genet 43 (11), 1082-1090 (2011)
   PUBMED   21946350
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Pasini,D., Cloos,P.A., Walfridsson,J., Olsson,L., Bukowski,J.P.,
            Johansen,J.V., Bak,M., Tommerup,N., Rappsilber,J. and Helin,K.
  TITLE     JARID2 regulates binding of the Polycomb repressive complex 2 to
            target genes in ES cells
  JOURNAL   Nature 464 (7286), 306-310 (2010)
   PUBMED   20075857
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Cao,R. and Zhang,Y.
  TITLE     SUZ12 is required for both the histone methyltransferase activity
            and the silencing function of the EED-EZH2 complex
  JOURNAL   Mol Cell 15 (1), 57-67 (2004)
   PUBMED   15225548
REFERENCE   10 (residues 1 to 479)
  AUTHORS   He,G.P., Kim,S. and Ro,H.S.
  TITLE     Cloning and characterization of a novel zinc finger transcriptional
            repressor. A direct role of the zinc finger motif in repression
  JOURNAL   J Biol Chem 274 (21), 14678-14684 (1999)
   PUBMED   10329662
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091805.16.
            
            On May 30, 2018 this sequence version replaced XP_006719094.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.219388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.3"
     Protein         1..479
                     /product="zinc finger protein AEBP2 isoform d"
                     /note="AE(adipocyte enhancer)-binding protein 2; zinc
                     finger protein AEBP2; adipocyte enhancer-binding protein
                     2"
                     /calculated_mol_wt=49886
     Region          <215..>339
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          266..286
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(270,272,274,276..277,280..281,285,303,305,309..310,
                     317..318,321,337,339,341,343..344,347..348,351)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          297..322
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          330..352
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..479
                     /gene="AEBP2"
                     /coded_by="NM_001363736.2:209..1648"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:121536"
                     /db_xref="HGNC:HGNC:24051"
                     /db_xref="MIM:617934"
ORIGIN      
        1 maaaitdmad leelsrlspl ppgspgsaar graeppeeee eeeeeeeeae aeavaallln
       61 ggsggggggg gggvgggeae tmsepspesa sqagededee eddeeeedes sssgggeees
      121 saeslvgssg gsssdetrsl spgaassssg dgdgkeglee pkgprgsqgg ggggsssssv
      181 vssggdegyg tggggssats ggrrgslems sdgeplsrmd sedsisstim dvdstissgr
      241 stpammngqg sttsssknia ynccwdqcqa cfnsspdlad hirsihvdgq rggvfvclwk
      301 gckvyntpst sqswlqrhml thsgdkpfkc vvggcnasfa sqgglarhvp thfsqqnssk
      361 vssqpkakee spskagmnkr rklknkrrrs lprphdffda qtldairhra icfnlsahie
      421 slgkghsvvf hstviakrke dsgkiklllh wmpeditmpq krlkrtlirk vfnlylskq
//
LOCUS       NP_001251                464 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 8 isoform 1 [Homo sapiens].
ACCESSION   NP_001251
VERSION     NP_001251.1
DBSOURCE    REFSEQ: accession NM_001260.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Comeau,D., Belliveau,J., Bouhamdani,N. and Amor,M.B.
  TITLE     Expanding the phenotypic spectrum for CDK8-related disease: A case
            report
  JOURNAL   Am J Med Genet A 194 (5), e63537 (2024)
   PUBMED   38193604
  REMARK    GeneRIF: Expanding the phenotypic spectrum for CDK8-related
            disease: A case report.
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Choi,H.Y., Zhu,Y., Zhao,X., Mehta,S., Hernandez,J.C., Lee,J.J.,
            Kou,Y., Machida,R., Giacca,M., Del Sal,G., Ray,R., Eoh,H.,
            Tahara,S.M., Chen,L., Tsukamoto,H. and Machida,K.
  TITLE     NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells
  JOURNAL   Exp Mol Med 56 (2), 461-477 (2024)
   PUBMED   38409448
  REMARK    GeneRIF: NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells.
            Erratum:[Exp Mol Med. 2024 Oct;56(10):2323. doi:
            10.1038/s12276-024-01325-9. PMID: 39465353]
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Chen,M., Li,J., Zhang,L., Wang,L., Cheng,C., Ji,H., Altilia,S.,
            Ding,X., Cai,G., Altomare,D., Shtutman,M., Byrum,S.D.,
            Mackintosh,S.G., Feoktistov,A., Soshnikova,N., Mogila,V.A.,
            Tatarskiy,V., Erokhin,M., Chetverina,D., Prawira,A., Ni,Y.,
            Urban,S., McInnes,C., Broude,E.V. and Roninson,I.B.
  TITLE     CDK8 and CDK19: positive regulators of signal-induced transcription
            and negative regulators of Mediator complex proteins
  JOURNAL   Nucleic Acids Res 51 (14), 7288-7313 (2023)
   PUBMED   37378433
  REMARK    GeneRIF: CDK8 and CDK19: positive regulators of signal-induced
            transcription and negative regulators of Mediator complex proteins.
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Rzymski,T., Mikula,M., Wiklik,K. and Brzozka,K.
  TITLE     CDK8 kinase--An emerging target in targeted cancer therapy
  JOURNAL   Biochim Biophys Acta 1854 (10 Pt B), 1617-1629 (2015)
   PUBMED   26006748
  REMARK    GeneRIF: Current state of the art confirms that further development
            of CDK8 inhibitors will translate into targeted therapies in
            oncology
            Review article
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Nemet,J., Jelicic,B., Rubelj,I. and Sopta,M.
  TITLE     The two faces of Cdk8, a positive/negative regulator of
            transcription
  JOURNAL   Biochimie 97, 22-27 (2014)
   PUBMED   24139904
  REMARK    GeneRIF: CDK8 regulates the transcription factors turnover,
            C-terminal domain phosphorylation, and regulates the activator or
            repressor functions. (Review)
            Review article
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Cujec,T.P., Cho,H., Maldonado,E., Meyer,J., Reinberg,D. and
            Peterlin,B.M.
  TITLE     The human immunodeficiency virus transactivator Tat interacts with
            the RNA polymerase II holoenzyme
  JOURNAL   Mol Cell Biol 17 (4), 1817-1823 (1997)
   PUBMED   9121429
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Rickert,P., Seghezzi,W., Shanahan,F., Cho,H. and Lees,E.
  TITLE     Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase
            II
  JOURNAL   Oncogene 12 (12), 2631-2640 (1996)
   PUBMED   8700522
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Tassan,J.P., Jaquenoud,M., Leopold,P., Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of human cyclin-dependent kinase 8, a putative
            protein kinase partner for cyclin C
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8871-8875 (1995)
   PUBMED   7568034
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094784.1, BC104492.1 and
            BM021447.1.
            
            Summary: This gene encodes a member of the cyclin-dependent protein
            kinase (CDK) family. CDK family members are known to be important
            regulators of cell cycle progression. This kinase and its
            regulatory subunit, cyclin C, are components of the Mediator
            transcriptional regulatory complex, involved in both
            transcriptional activation and repression by phosphorylation of the
            carboxy-terminal domain of the largest subunit of RNA polymerase
            II. This kinase regulates transcription by targeting the
            cyclin-dependent kinase 7 subunits of the general transcription
            initiation factor IIH, thus providing a link between the Mediator
            complex and the basal transcription machinery. Multiple pseudogenes
            of this gene have been identified. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1113401.1,
                                           SRR3476690.615108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381527.8/ ENSP00000370938.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..464
                     /product="cyclin-dependent kinase 8 isoform 1"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="CDK8 protein kinase; protein kinase K35; cell
                     division protein kinase 8; mediator complex subunit CDK8;
                     mediator of RNA polymerase II transcription subunit CDK8"
                     /calculated_mol_wt=53153
     Region          1..15
                     /region_name="Interaction with CCNC"
                     /note="propagated from UniProtKB/Swiss-Prot (P49336.1)"
     Region          3..335
                     /region_name="STKc_CDK8"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 8; cd07868"
                     /db_xref="CDD:270851"
     Site            order(3..6,9,13,58..59,61,64..65,67..69,71..73,84,86..88,
                     91..93,145..147)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270851"
     Site            order(27..30,35,50,52,65,79,97..100,103,105..106,151,153,
                     155..156,158,173,176,191,193..196,198,236..237)
                     /site_type="active"
                     /db_xref="CDD:270851"
     Site            order(27..30,35,50,52,79,97..100,103,106,155..156,158,173)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270851"
     Site            order(65,105,151,153,176,191,193..196,198,236..237)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270851"
     Site            172..198
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270851"
     Region          361..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49336.1)"
     CDS             1..464
                     /gene="CDK8"
                     /gene_synonym="IDDHBA; K35"
                     /coded_by="NM_001260.3:514..1908"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9317.1"
                     /db_xref="GeneID:1024"
                     /db_xref="HGNC:HGNC:1779"
                     /db_xref="MIM:603184"
ORIGIN      
        1 mdydfkvkls serervedlf eyegckvgrg tyghvykakr kdgkddkdya lkqiegtgis
       61 msacreiall relkhpnvis lqkvflshad rkvwllfdya ehdlwhiikf hraskankkp
      121 vqlprgmvks llyqildgih ylhanwvlhr dlkpanilvm gegpergrvk iadmgfarlf
      181 nsplkpladl dpvvvtfwyr apelllgarh ytkaidiwai gcifaellts epifhcrqed
      241 iktsnpyhhd qldrifnvmg fpadkdwedi kkmpehstlm kdfrrntytn cslikymekh
      301 kvkpdskafh llqklltmdp ikritseqam qdpyfledpl ptsdvfagcq ipypkreflt
      361 eeepddkgdk knqqqqqgnn htngtghpgn qdsshtqgpp lkkvrvvppt ttsgglimts
      421 dyqrsnphaa ypnpgpstsq pqssmgysat sqqppqyshq thry
//
LOCUS       NP_001356617             240 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin-like growth factor-binding protein 3 receptor isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001356617
VERSION     NP_001356617.1
DBSOURCE    REFSEQ: accession NM_001369688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Xu,W., Chao,R., Xie,X., Mao,Y., Chen,X., Chen,X. and Zhang,S.
  TITLE     IL13Ralpha2 as a crucial receptor for Chi3l1 in osteoclast
            differentiation and bone resorption through the MAPK/AKT pathway
  JOURNAL   Cell Commun Signal 22 (1), 81 (2024)
   PUBMED   38291404
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   D'Addio,F., Assi,E., Maestroni,A., Rossi,G., Usuelli,V.,
            Petrazzuolo,A., Nardini,M., Loretelli,C., Ben Nasr,M. and
            Fiorina,P.
  TITLE     TMEM219 regulates the transcription factor expression and
            proliferation of beta cells
  JOURNAL   Front Endocrinol (Lausanne) 15, 1306127 (2024)
   PUBMED   38318298
  REMARK    GeneRIF: TMEM219 regulates the transcription factor expression and
            proliferation of beta cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Knudson,K.M., Hwang,S., McCann,M.S., Joshi,B.H., Husain,S.R. and
            Puri,R.K.
  TITLE     Recent Advances in IL-13Ralpha2-Directed Cancer Immunotherapy
  JOURNAL   Front Immunol 13, 878365 (2022)
   PUBMED   35464460
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 240)
  AUTHORS   D'Addio,F., Maestroni,A., Assi,E., Ben Nasr,M., Amabile,G.,
            Usuelli,V., Loretelli,C., Bertuzzi,F., Antonioli,B., Cardarelli,F.,
            El Essawy,B., Solini,A., Gerling,I.C., Bianchi,C., Becchi,G.,
            Mazzucchelli,S., Corradi,D., Fadini,G.P., Foschi,D., Markmann,J.F.,
            Orsi,E., Skrha,J. Jr., Camboni,M.G., Abdi,R., James Shapiro,A.M.,
            Folli,F., Ludvigsson,J., Del Prato,S., Zuccotti,G. and Fiorina,P.
  TITLE     The IGFBP3/TMEM219 pathway regulates beta cell homeostasis
  JOURNAL   Nat Commun 13 (1), 684 (2022)
   PUBMED   35115561
  REMARK    GeneRIF: The IGFBP3/TMEM219 pathway regulates beta cell
            homeostasis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Joyce,S. and Nour,A.M.
  TITLE     Blocking transmembrane219 protein signaling inhibits autophagy and
            restores normal cell death
  JOURNAL   PLoS One 14 (6), e0218091 (2019)
   PUBMED   31220095
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 240)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   7  (residues 1 to 240)
  AUTHORS   He,C.H., Lee,C.G., Dela Cruz,C.S., Lee,C.M., Zhou,Y., Ahangari,F.,
            Ma,B., Herzog,E.L., Rosenberg,S.A., Li,Y., Nour,A.M., Parikh,C.R.,
            Schmidt,I., Modis,Y., Cantley,L. and Elias,J.A.
  TITLE     Chitinase 3-like 1 regulates cellular and tissue responses via
            IL-13 receptor alpha2
  JOURNAL   Cell Rep 4 (4), 830-841 (2013)
   PUBMED   23972995
  REMARK    Erratum:[Cell Rep. 2013 Nov 27;5(4):1156]
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Baxter,R.C.
  TITLE     Insulin-like growth factor binding protein-3 (IGFBP-3): Novel
            ligands mediate unexpected functions
  JOURNAL   J Cell Commun Signal 7 (3), 179-189 (2013)
   PUBMED   23700234
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Ingermann,A.R., Yang,Y.F., Han,J., Mikami,A., Garza,A.E.,
            Mohanraj,L., Fan,L., Idowu,M., Ware,J.L., Kim,H.S., Lee,D.Y. and
            Oh,Y.
  TITLE     Identification of a novel cell death receptor mediating
            IGFBP-3-induced anti-tumor effects in breast and prostate cancer
  JOURNAL   J Biol Chem 285 (39), 30233-30246 (2010)
   PUBMED   20353938
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Wood,N., Whitters,M.J., Jacobson,B.A., Witek,J., Sypek,J.P.,
            Kasaian,M., Eppihimer,M.J., Unger,M., Tanaka,T., Goldman,S.J.,
            Collins,M., Donaldson,D.D. and Grusby,M.J.
  TITLE     Enhanced interleukin (IL)-13 responses in mice lacking IL-13
            receptor alpha 2
  JOURNAL   J Exp Med 197 (6), 703-709 (2003)
   PUBMED   12642602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC120114.2 and AC093512.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1133500.1,
                                           SRR3476690.404854.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..240
                     /product="insulin-like growth factor-binding protein 3
                     receptor isoform 1 precursor"
                     /note="insulin-like growth factor-binding protein 3
                     receptor; testicular tissue protein Li 203"
                     /calculated_mol_wt=21870
     sig_peptide     1..38
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
                     /calculated_mol_wt=3872
     mat_peptide     39..240
                     /product="Insulin-like growth factor-binding protein 3
                     receptor. /id=PRO_0000329049"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XT9.1)"
                     /calculated_mol_wt=21870
     Region          48..169
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XT9.1)"
     CDS             1..240
                     /gene="TMEM219"
                     /gene_synonym="IGFBP-3R; IGFBP3R"
                     /coded_by="NM_001369688.1:1066..1788"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS42145.1"
                     /db_xref="GeneID:124446"
                     /db_xref="HGNC:HGNC:25201"
                     /db_xref="MIM:620290"
ORIGIN      
        1 mgncqaghnl hlclahhppl vcatlillll glsglglgsf llthrtglrs pdipqdwvsf
       61 lrsfgqltlc prngtvtgkw rgshvvgllt tlnfgdgpdr nktrtfqatv lgsqmglkgs
      121 sagqlvlita rvttertagt clyfsavpgi lpssqppisc seegagnatl sprmgeecvs
      181 vwsheglvlt klltseelal cgsrllvlgs flllfcgllc cvtamcfhpr reshwsrtrl
//
LOCUS       NP_001354689            1298 aa            linear   PRI 20-NOV-2025
DEFINITION  protein broad-minded isoform 2 [Homo sapiens].
ACCESSION   NP_001354689 XP_005266918
VERSION     NP_001354689.1
DBSOURCE    REFSEQ: accession NM_001367760.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Bocquet,B., Borday,C., Erkilic,N., Mamaeva,D., Donval,A.,
            Masson,C., Parain,K., Kaminska,K., Quinodoz,M., Perea-Romero,I.,
            Garcia-Garcia,G., Jimenez-Medina,C., Boukhaddaoui,H., Coget,A.,
            Leboucq,N., Calzetti,G., Gandolfi,S., Percesepe,A., Barili,V.,
            Uliana,V., Delsante,M., Bozzetti,F., Scholl,H.P., Corton,M.,
            Ayuso,C., Millan,J.M., Rivolta,C., Meunier,I., Perron,M. and
            Kalatzis,V.
  TITLE     TBC1D32 variants disrupt retinal ciliogenesis and cause retinitis
            pigmentosa
  JOURNAL   JCI Insight 8 (21), e169426 (2023)
   PUBMED   37768732
  REMARK    GeneRIF: TBC1D32 variants disrupt retinal ciliogenesis and cause
            retinitis pigmentosa.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Satoda,Y., Noguchi,T., Fujii,T., Taniguchi,A., Katoh,Y. and
            Nakayama,K.
  TITLE     BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1
  JOURNAL   Mol Biol Cell 33 (9), ar79 (2022)
   PUBMED   35609210
  REMARK    GeneRIF: BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1.
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Alsahan,N. and Alkuraya,F.S.
  TITLE     Confirming TBC1D32-related ciliopathy in humans
  JOURNAL   Am J Med Genet A 182 (8), 1985-1987 (2020)
   PUBMED   32573025
  REMARK    GeneRIF: Confirming TBC1D32-related ciliopathy in humans.
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Hietamaki,J., Gregory,L.C., Ayoub,S., Iivonen,A.P., Vaaralahti,K.,
            Liu,X., Brandstack,N., Buckton,A.J., Laine,T., Kansakoski,J.,
            Hero,M., Miettinen,P.J., Varjosalo,M., Wakeling,E., Dattani,M.T.
            and Raivio,T.
  TITLE     Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism
  JOURNAL   J Clin Endocrinol Metab 105 (6), 1748-1758 (2020)
   PUBMED   32060556
  REMARK    GeneRIF: Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism.
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Shaheen,R., Jiang,N., Alzahrani,F., Ewida,N., Al-Sheddi,T.,
            Alobeid,E., Musaev,D., Stanley,V., Hashem,M., Ibrahim,N.,
            Abdulwahab,F., Alshenqiti,A., Sonmez,F.M., Saqati,N., Alzaidan,H.,
            Al-Qattan,M.M., Al-Mohanna,F., Gleeson,J.G. and Alkuraya,F.S.
  TITLE     Bi-allelic Mutations in FAM149B1 Cause Abnormal Primary Cilium and
            a Range of Ciliopathy Phenotypes in Humans
  JOURNAL   Am J Hum Genet 104 (4), 731-737 (2019)
   PUBMED   30905400
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Adly,N., Alhashem,A., Ammari,A. and Alkuraya,F.S.
  TITLE     Ciliary genes TBC1D32/C6orf170 and SCLT1 are mutated in patients
            with OFD type IX
  JOURNAL   Hum Mutat 35 (1), 36-40 (2014)
   PUBMED   24285566
  REMARK    GeneRIF: study identified 2 cases with a severe ciliopathy
            phenotype consistent with oro-facio-digital syndrome type IX; the
            autozygome of each index harbored a single truncating variant and
            the affected genes (SCLT1 and TBC1D32/C6orf170) have roles in
            centrosomal biology and ciliogenesis; findings suggest a role of
            SCLT1 and TBC1D32 in ciliopathy pathogenesis
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Ko,H.W., Norman,R.X., Tran,J., Fuller,K.P., Fukuda,M. and
            Eggenschwiler,J.T.
  TITLE     Broad-minded links cell cycle-related kinase to cilia assembly and
            hedgehog signal transduction
  JOURNAL   Dev Cell 18 (2), 237-247 (2010)
   PUBMED   20159594
  REMARK    GeneRIF: Studies in mouse and zebrafish implicate that TBC1D32 is
            involved in sonic hedgehog signaling.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139098.15, AL589910.9,
            AL590225.4, AL365508.19 and AL035593.11.
            
            On Dec 14, 2018 this sequence version replaced XP_005266918.1.
            
            Summary: This gene encodes a TBC-domain containing protein. Studies
            of a similar protein in mouse and zebrafish suggest that the
            encoded protein is involved in sonic hedgehog signaling, and that
            it interacts with and stabilizes cell cycle-related kinase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.2539.1,
                                           SRR1803617.201353.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..1298
                     /product="protein broad-minded isoform 2"
                     /note="protein broad-minded; broad-minded homolog"
                     /calculated_mol_wt=149298
     Region          12..1295
                     /region_name="BROMI"
                     /note="Broad-minded protein; pfam14961"
                     /db_xref="CDD:464406"
     CDS             1..1298
                     /gene="TBC1D32"
                     /gene_synonym="ALHSA; BROMI; C6orf170; C6orf171; OFD9;
                     RP100"
                     /coded_by="NM_001367760.1:51..3947"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93996.1"
                     /db_xref="GeneID:221322"
                     /db_xref="HGNC:HGNC:21485"
                     /db_xref="MIM:615867"
ORIGIN      
        1 mahfssedqa mlqamlrrlf qsvkekitga pslecaeeil lhleetdenf hnyefvkylr
       61 qhigntlgsm ieeemekcts drnqgeecgy dtvvqqvtkr tqeskeykem mhylknimia
      121 vvesminkfe edetrnqerq kkiqkekshs yrtdncsdsd sslnqsykfc qgklqlildq
      181 ldpgqpkevr yealqtlcsa ppsdvlncen wttlcekltv slsdpdpvfs drilkfcaqt
      241 fllsplhmtk eiytslakyl esyflsrenh iptlsagvdi tnpnmtrllk kvrllneyqk
      301 eapsfwirhp ekymeeives tlslltvkhn qshvvsqkil dpiyffalvd tkavwfkkwm
      361 hahysrttvl rlletkyksl vttaiqqcvq yfemcktrka detlghskhc rnkqktfyyl
      421 gqelqyiyfi hslcllgrll iykqgrklfp iklknkkglv slidllvlft qliyyspscp
      481 kmtsaahsen yspasmvtev lwilsdqkec aveclynniv ietllqpihn lmkgneaspn
      541 csetalihia gilariasve eglilllyga nmnsseespt gahiiaqfsk klldedisif
      601 sgsemlpvvk gafisvcrhi ystceglqvl itynlhesia kawkktslls eriptpvegs
      661 dsvssvsqes qnimawednl lddllhfaat pkgllllqrt gainecvtfi fnryakklqv
      721 srhkkfgygv lvtrvastaa ggialkksgf inelitelws nleygrddvr vthprttpvd
      781 pidrscqksf lalvnllsyp aiyelvrnqd lpnkteyslr evptcvidii drliilnsea
      841 kirslfnyeq shifglrlls viccdldtll lleaqyqvse mllnaqeeni leiseshrdf
      901 iidglsvern hvlvrinlvg gplerilppr lleksdnpyp wpmfssyplp ncylsditrn
      961 agikqdndld klllclkisd kqtewiencq rqfckmmkak pdiisgeali ellekfvlhl
     1021 tespsecyfp sveytatdan vkneslssvq qlgikmtvry gkflsllkdg aendltwvlk
     1081 hcerflkqqq tsikssllcl qgnyaghdwf vsslfmimlg dkektfqflh qfsrlltsaf
     1141 lwlprlhiss ylpndtvesg ihpvyfcsth yiemllkael plvfsafhms gfapsqiclq
     1201 witqcfwnyl dwieichyia tcvflgpdyq vyiciavfkh lqqdilqhtq tqdlqvflke
     1261 ealhgfrvsd yfeymeileq nyrtvllrdm rnirlqst
//
LOCUS       NP_005057                707 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor, proline- and glutamine-rich [Homo sapiens].
ACCESSION   NP_005057
VERSION     NP_005057.1
DBSOURCE    REFSEQ: accession NM_005066.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Thivierge,C., Bellefeuille,M., Diwan,S.S., Dyakov,B.J.A.,
            Leventis,R., Perron,G., Najafabadi,H.S., Gravel,S.P., Gingras,A.C.
            and Duchaine,T.F.
  TITLE     Paraspeckle-independent co-transcriptional regulation of nuclear
            microRNA biogenesis by SFPQ
  JOURNAL   Cell Rep 43 (9), 114695 (2024)
   PUBMED   39250314
  REMARK    GeneRIF: Paraspeckle-independent co-transcriptional regulation of
            nuclear microRNA biogenesis by SFPQ.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Akhmedov,A.T. and Lopez,B.S.
  TITLE     Human 100-kDa homologous DNA-pairing protein is the splicing factor
            PSF and promotes DNA strand invasion
  JOURNAL   Nucleic Acids Res 28 (16), 3022-3030 (2000)
   PUBMED   10931916
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Lutz,C.S., Cooke,C., O'Connor,J.P., Kobayashi,R. and Alwine,J.C.
  TITLE     The snRNP-free U1A (SF-A) complex(es): identification of the
            largest subunit as PSF, the polypyrimidine-tract binding
            protein-associated splicing factor
  JOURNAL   RNA 4 (12), 1493-1499 (1998)
   PUBMED   9848648
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Teigelkamp,S., Mundt,C., Achsel,T., Will,C.L. and Luhrmann,R.
  TITLE     The human U5 snRNP-specific 100-kD protein is an RS
            domain-containing, putative RNA helicase with significant homology
            to the yeast splicing factor Prp28p
  JOURNAL   RNA 3 (11), 1313-1326 (1997)
   PUBMED   9409622
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Gozani,O., Patton,J.G. and Reed,R.
  TITLE     A novel set of spliceosome-associated proteins and the essential
            splicing factor PSF bind stably to pre-mRNA prior to catalytic step
            II of the splicing reaction
  JOURNAL   EMBO J 13 (14), 3356-3367 (1994)
   PUBMED   8045264
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Patton,J.G., Porro,E.B., Galceran,J., Tempst,P. and Nadal-Ginard,B.
  TITLE     Cloning and characterization of PSF, a novel pre-mRNA splicing
            factor
  JOURNAL   Genes Dev 7 (3), 393-406 (1993)
   PUBMED   8449401
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Zhang,W.W., Zhang,L.X., Busch,R.K., Farres,J. and Busch,H.
  TITLE     Purification and characterization of a DNA-binding heterodimer of
            52 and 100 kDa from HeLa cells
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 267-272 (1993)
   PUBMED   8439294
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Gower,H.J., Moore,S.E., Dickson,G., Elsom,V.L., Nayak,R. and
            Walsh,F.S.
  TITLE     Cloning and characterization of a myoblast cell surface antigen
            defined by 24.1D5 monoclonal antibody
  JOURNAL   Development 105 (4), 723-731 (1989)
   PUBMED   2480877
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590434.16, BC051192.1 and X70944.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.308940.1, GQ900958.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357214.6/ ENSP00000349748.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..707
                     /product="splicing factor, proline- and glutamine-rich"
                     /note="polypyrimidine tract-binding protein-associated
                     splicing factor; polypyrimidine tract binding protein
                     associated; splicing factor proline/glutamine rich
                     (polypyrimidine tract binding protein associated);
                     epididymis secretory sperm binding protein; PTB-associated
                     splicing factor; 100 kDa DNA-pairing protein; DNA-binding
                     p52/p100 complex, 100 kDa subunit; protein phosphatase 1,
                     regulatory subunit 140; splicing factor
                     proline/glutamine-rich"
                     /calculated_mol_wt=76019
     Region          1..273
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MKNK2.
                     /evidence=ECO:0000269|PubMed:17965020; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Region          9..27
                     /region_name="3 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            9
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8VIJ6;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8VIJ6; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VIJ6; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            236
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            242
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            245
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MKNK2.
                     /evidence=ECO:0000269|PubMed:17965020,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ALK.
                     /evidence=ECO:0000269|PubMed:17537995; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Region          296..366
                     /region_name="RRM1_PSF"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     polypyrimidine tract-binding protein
                     (PTB)-associated-splicing factor (PSF); cd12587"
                     /db_xref="CDD:410000"
     Site            314
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            338
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Region          372..451
                     /region_name="RRM2_PSF"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     polypyrimidine tract-binding protein
                     (PTB)-associated-splicing factor (PSF); cd12590"
                     /db_xref="CDD:410003"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            421
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Region          442..538
                     /region_name="NOPS_PSF"
                     /note="NOPS domain, including C-terminal coiled-coil
                     region, in polypyrimidine tract-binding protein
                     (PTB)-associated-splicing factor (PSF) and similar
                     proteins; cd12948"
                     /db_xref="CDD:240583"
     Site            order(442..444,446,452..461,464,470,472..476,478..481,
                     486..487,489..495,497..498,500..501,504..505,508..509,
                     511..512,515..516,519..520,522..523,526..527)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:240583"
     Site            472
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Region          <499..>599
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            571
                     /site_type="methylation"
                     /note="Dimethylated arginine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Region          579..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            662..663
                     /site_type="other"
                     /note="Breakpoint for translocation to form SFPQ-TFE3;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            681
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000269|Ref.4, ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20932480,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     Site            693
                     /site_type="methylation"
                     /note="Dimethylated arginine, alternate.
                     /evidence=ECO:0000269|Ref.4; Omega-N-methylarginine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P23246.2)"
     Site            695
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P23246.2)"
     CDS             1..707
                     /gene="SFPQ"
                     /gene_synonym="POMP100; PPP1R140; PSF"
                     /coded_by="NM_005066.3:97..2220"
                     /db_xref="CCDS:CCDS388.1"
                     /db_xref="GeneID:6421"
                     /db_xref="HGNC:HGNC:10774"
                     /db_xref="MIM:605199"
ORIGIN      
        1 msrdrfrsrg gggggfhrrg ggggrgglhd frspppgmgl nqnrgpmgpg pgqsgpkppi
       61 ppppphqqqq qpppqqpppq qppphqppph pqphqqqqpp pppqdsskpv vaqgpgpapg
      121 vgsappasss appatpptsg appgsgpgpt ptpppavtsa ppgappptpp ssgvpttppq
      181 aggpppppaa vpgpgpgpkq gpgpggpkgg kmpggpkpgg gpglstpggh pkpphrggge
      241 prggrqhhpp yhqqhhqgpp pggpggrsee kisdsegfka nlsllrrpge ktytqrcrlf
      301 vgnlpadite defkrlfaky gepgevfink gkgfgfikle sralaeiaka elddtpmrgr
      361 qlrvrfatha aalsvrnlsp yvsnelleea fsqfgpiera vvivddrgrs tgkgivefas
      421 kpaarkafer csegvflltt tprpvivepl eqlddedglp eklaqknpmy qkeretpprf
      481 aqhgtfeyey sqrwksldem ekqqreqvek nmkdakdkle semedayheh qanllrqdlm
      541 rrqeelrrme elhnqemqkr kemqlrqeee rrrreeemmi rqremeeqmr rqreesysrm
      601 gymdprerdm rmggggamnm gdpygsggqk fpplgggggi gyeanpgvpp atmsgsmmgs
      661 dmrterfgqg gagpvggqgp rgmgpgtpag ygrgreeyeg pnkkprf
//
LOCUS       NP_004840                275 aa            linear   PRI 20-NOV-2025
DEFINITION  autophagy protein 5 isoform a [Homo sapiens].
ACCESSION   NP_004840
VERSION     NP_004840.1
DBSOURCE    REFSEQ: accession NM_004849.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Li,S., Zhang,B.W., Lou,Q.Q., Liu,Y., Wei,Z.J., Huang,J., Yao,K.H.,
            Xu,Q.R., Fan,J., Xi,Y., Yang,L. and Chen,S.
  TITLE     ATG5 nonautophagically regulates inflammation and differentiation
            in mouse embryonic stem cells
  JOURNAL   Autophagy 20 (8), 1897-1898 (2024)
   PUBMED   38477302
  REMARK    GeneRIF: ATG5 nonautophagically regulates inflammation and
            differentiation in mouse embryonic stem cells.
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Li,Q., Wen,W., Wang,Y., Gong,T., Wang,X., Tan,Q., Fan,B., Xie,H.,
            Li,Y., Li,S., Yang,C., Zhou,Z., Duan,X., Lin,W. and Chen,L.
  TITLE     Autophagy-related protein 5 (ATG5) interacts with bone marrow
            stromal cell antigen 2 (BST2) to stimulate HBV replication through
            antagonizing the antiviral activity of BST2
  JOURNAL   J Med Virol 96 (5), e29659 (2024)
   PUBMED   38747016
  REMARK    GeneRIF: Autophagy-related protein 5 (ATG5) interacts with bone
            marrow stromal cell antigen 2 (BST2) to stimulate HBV replication
            through antagonizing the antiviral activity of BST2.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Chen,F., Wu,L., Zhang,M., Kan,M., Chen,H., Wang,X. and Qu,J.
  TITLE     Autophagy-related 5 in acute ischemic stroke: Variation and linkage
            with neurofunction, and survival
  JOURNAL   Ann Clin Transl Neurol 11 (4), 856-865 (2024)
   PUBMED   38530706
  REMARK    GeneRIF: Autophagy-related 5 in acute ischemic stroke: Variation
            and linkage with neurofunction, and survival.
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Qu,J., Wu,L., Zhang,M., Kan,M., Chen,H., Shi,Y., Wang,S., Wang,X.
            and Chen,F.
  TITLE     Serum autophagy-related gene 5 level in stroke patients:
            correlation with CD4+ T cells and cognition impairment during a
            3-year follow-up
  JOURNAL   Braz J Med Biol Res 57, e13019 (2024)
   PUBMED   38511768
  REMARK    GeneRIF: Serum autophagy-related gene 5 level in stroke patients:
            correlation with CD4+ T cells and cognition impairment during a
            3-year follow-up.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Ueno,T. and Kominami,E.
  TITLE     The human homolog of Saccharomyces cerevisiae Apg7p is a
            Protein-activating enzyme for multiple substrates including human
            Apg12p, GATE-16, GABARAP, and MAP-LC3
  JOURNAL   J Biol Chem 276 (3), 1701-1706 (2001)
   PUBMED   11096062
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Schmeiser,K., Armstrong,S., Hammond,E.M. and Grand,R.J.
  TITLE     Assignment of the yeast APG5 human homologue APG5L to chromosome
            band 6q21 by fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 87 (3-4), 213-214 (1999)
   PUBMED   10702672
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Mizushima,N., Sugita,H., Yoshimori,T. and Ohsumi,Y.
  TITLE     A new protein conjugation system in human. The counterpart of the
            yeast Apg12p conjugation system essential for autophagy
  JOURNAL   J Biol Chem 273 (51), 33889-33892 (1998)
   PUBMED   9852036
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Hammond,E.M., Brunet,C.L., Johnson,G.D., Parkhill,J., Milner,A.E.,
            Brady,G., Gregory,C.D. and Grand,R.J.
  TITLE     Homology between a human apoptosis specific protein and the product
            of APG5, a gene involved in autophagy in yeast
  JOURNAL   FEBS Lett 425 (3), 391-395 (1998)
   PUBMED   9563500
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Grand,R.J., Milner,A.E., Mustoe,T., Johnson,G.D., Owen,D.,
            Grant,M.L. and Gregory,C.D.
  TITLE     A novel protein expressed in mammalian cells undergoing apoptosis
  JOURNAL   Exp Cell Res 218 (2), 439-451 (1995)
   PUBMED   7796880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y11588.1 and BX537904.1.
            
            Summary: The protein encoded by this gene, in combination with
            autophagy protein 12, functions as an E1-like activating enzyme in
            a ubiquitin-like conjugating system. The encoded protein is
            involved in several cellular processes, including autophagic
            vesicle formation, mitochondrial quality control after oxidative
            damage, negative regulation of the innate antiviral immune
            response, lymphocyte development and proliferation, MHC II antigen
            presentation, adipocyte differentiation, and apoptosis. Several
            transcript variants encoding different protein isoforms have been
            found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Both variants 1 and
            2 encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y11588.1, SRR14038191.2970881.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369076.8/ ENSP00000358072.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..275
                     /product="autophagy protein 5 isoform a"
                     /note="apoptosis-specific protein; ATG5 autophagy related
                     5 homolog; APG5 autophagy 5-like"
                     /calculated_mol_wt=32316
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H1Y0.2)"
     Region          79..270
                     /region_name="APG5"
                     /note="Autophagy protein Apg5; pfam04106"
                     /db_xref="CDD:461175"
     CDS             1..275
                     /gene="ATG5"
                     /gene_synonym="APG5; APG5-LIKE; APG5L; ASP; hAPG5; SCAR25"
                     /coded_by="NM_004849.4:294..1121"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5055.1"
                     /db_xref="GeneID:9474"
                     /db_xref="HGNC:HGNC:589"
                     /db_xref="MIM:604261"
ORIGIN      
        1 mtddkdvlrd vwfgriptcf tlyqdeiter eaepyylllp rvsyltlvtd kvkkhfqkvm
       61 rqediseiwf eyegtplkwh ypigllfdll asssalpwni tvhfksfpek dllhcpskda
      121 ieahfmscmk eadalkhksq vinemqkkdh kqlwmglqnd rfdqfwainr klmeypaeen
      181 gfryipfriy qttterpfiq klfrpvaadg qlhtlgdllk evcpsaidpe dgekknqvmi
      241 hgiepmletp lqwlsehlsy pdnflhisii pqptd
//
LOCUS       NP_998890                 89 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein P1 isoform 2 [Homo sapiens].
ACCESSION   NP_998890
VERSION     NP_998890.1
DBSOURCE    REFSEQ: accession NM_213725.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Tripathi,M., Gauthier,K., Sandireddy,R., Zhou,J., Guptta,P.,
            Sakthivel,S., Teo,W.W., Naing,Y.T., Arul,K., Tikno,K., Park,S.H.,
            Wu,Y., Wang,L., Bay,B.H., Sun,L., Giguere,V., Chow,P.K.H.,
            Ghosh,S., McDonnell,D.P., Yen,P.M. and Singh,B.K.
  TITLE     Esrra regulates Rplp1-mediated translation of lysosome proteins
            suppressed in metabolic dysfunction-associated steatohepatitis and
            reversed by alternate day fasting
  JOURNAL   Mol Metab 87, 101997 (2024)
   PUBMED   39032642
  REMARK    GeneRIF: Esrra regulates Rplp1-mediated translation of lysosome
            proteins suppressed in metabolic dysfunction-associated
            steatohepatitis and reversed by alternate day fasting.
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Yang,W., Wang,H., Li,Z., Zhang,L., Liu,J., Kirchhoff,F., Huan,C.
            and Zhang,W.
  TITLE     RPLP1 restricts HIV-1 transcription by disrupting C/EBPbeta binding
            to the LTR
  JOURNAL   Nat Commun 15 (1), 5290 (2024)
   PUBMED   38906865
  REMARK    GeneRIF: RPLP1 restricts HIV-1 transcription by disrupting
            C/EBPbeta binding to the LTR.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Peterson,R., Minchella,P., Cui,W., Graham,A. and Nothnick,W.B.
  TITLE     RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 24 (3), 2690 (2023)
   PUBMED   36769010
  REMARK    GeneRIF: RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Chan,S.H., Hung,F.S., Chan,D.S. and Shaw,P.C.
  TITLE     Trichosanthin interacts with acidic ribosomal proteins P0 and P1
            and mitotic checkpoint protein MAD2B
  JOURNAL   Eur J Biochem 268 (7), 2107-2112 (2001)
   PUBMED   11277934
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Tchorzewski,M., Boldyreff,B., Issinger,O.G. and Grankowski,N.
  TITLE     Analysis of the protein-protein interactions between the human
            acidic ribosomal P-proteins: evaluation by the two hybrid system
  JOURNAL   Int J Biochem Cell Biol 32 (7), 737-746 (2000)
   PUBMED   10856704
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC027237.8, BM745938.1 and M17886.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1
            protein can interact with P0 and P2 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. Two alternatively spliced transcript
            variants that encode different proteins have been observed. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment, compared to variant 1, resulting in a shorter protein
            (isoform 2) when compared to isoform 1.
            
            CCDS Note: This CCDS ID represents a variant of the RPLP1 gene that
            is based on a splice pattern found in several ESTs, including
            BM768334.1, BM508180.1, EL948616.1 and AJ713466.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM768334.1, DRR138512.32340.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..89
                     /product="large ribosomal subunit protein P1 isoform 2"
                     /note="60S acidic ribosomal protein P1; acidic ribosomal
                     phosphoprotein P1; ribosomal protein, large, P1; large
                     ribosomal subunit protein P1"
                     /calculated_mol_wt=8673
     Region          6..88
                     /region_name="Ribosomal_P1_P2_L12p"
                     /note="Ribosomal protein P1, P2, and L12p. Ribosomal
                     proteins P1 and P2 are the eukaryotic proteins that are
                     functionally equivalent to bacterial L7/L12. L12p is the
                     archaeal homolog. Unlike other ribosomal proteins, the
                     archaeal L12p and eukaryotic P1 and P2...; cl21508"
                     /db_xref="CDD:473891"
     CDS             1..89
                     /gene="RPLP1"
                     /gene_synonym="LP1; P1; RPP1"
                     /coded_by="NM_213725.2:132..401"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10234.1"
                     /db_xref="GeneID:6176"
                     /db_xref="HGNC:HGNC:10372"
                     /db_xref="MIM:180520"
ORIGIN      
        1 masvselaci ysalilhdde vtvtalanvn igslicnvga ggpapaagaa paggpapsta
       61 aapaeekkve akkeeseesd ddmgfglfd
//
LOCUS       NP_000991                 51 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL39 [Homo sapiens].
ACCESSION   NP_000991
VERSION     NP_000991.1
DBSOURCE    REFSEQ: accession NM_001000.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 51)
  AUTHORS   Sun,F., Wei,Y., Liu,Z., Jie,Q., Yang,X., Long,P., Wang,J.,
            Xiong,Y., Li,Q., Quan,S. and Ma,Y.
  TITLE     Acylglycerol kinase promotes ovarian cancer progression and
            regulates mitochondria function by interacting with ribosomal
            protein L39
  JOURNAL   J Exp Clin Cancer Res 41 (1), 238 (2022)
   PUBMED   35934718
  REMARK    GeneRIF: Acylglycerol kinase promotes ovarian cancer progression
            and regulates mitochondria function by interacting with ribosomal
            protein L39.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 51)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 51)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 51)
  AUTHORS   Dave,B., Gonzalez,D.D., Liu,Z.B., Li,X., Wong,H., Granados,S.,
            Ezzedine,N.E., Sieglaff,D.H., Ensor,J.E., Miller,K.D., Radovich,M.,
            KarinaEtrovic,A., Gross,S.S., Elemento,O., Mills,G.B.,
            Gilcrease,M.Z. and Chang,J.C.
  TITLE     Role of RPL39 in Metaplastic Breast Cancer
  JOURNAL   J Natl Cancer Inst 109 (6), 2758642 (2016)
   PUBMED   28040796
  REMARK    GeneRIF: RPL39 mediated its cancer-promoting actions through iNOS
            signaling, which was driven by the RNA editing enzyme adenosine
            deaminase acting on RNA 1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 51)
  AUTHORS   Chaillou,T., Zhang,X. and McCarthy,J.J.
  TITLE     Expression of Muscle-Specific Ribosomal Protein L3-Like Impairs
            Myotube Growth
  JOURNAL   J Cell Physiol 231 (9), 1894-1902 (2016)
   PUBMED   26684695
REFERENCE   6  (residues 1 to 51)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 51)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 51)
  AUTHORS   Tsui,S.K., Lee,S.M., Fung,K.P., Waye,M.M. and Lee,C.Y.
  TITLE     Primary structures and sequence analysis of human ribosomal
            proteins L39 and S27
  JOURNAL   Biochem Mol Biol Int 40 (3), 611-616 (1996)
   PUBMED   8908372
REFERENCE   9  (residues 1 to 51)
  AUTHORS   Otsuka,S., Tanaka,M., Saito,S., Yoshimoto,K. and Itakura,M.
  TITLE     Molecular cloning of a cDNA encoding human ribosomal protein L39
  JOURNAL   Biochim Biophys Acta 1308 (2), 119-121 (1996)
   PUBMED   8764829
REFERENCE   10 (residues 1 to 51)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BX476041.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the S39E family of ribosomal proteins. It is located in the
            cytoplasm. In rat, the protein is the smallest, and one of the most
            basic, proteins of the ribosome. This gene is co-transcribed with
            the U69 small nucleolar RNA gene, which is located in its second
            intron. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.98803.1,
                                           SRR5189661.155159.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361575.4/ ENSP00000355315.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..51
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..51
                     /product="large ribosomal subunit protein eL39"
                     /note="60S ribosomal protein L39"
                     /calculated_mol_wt=6276
     Region          10..50
                     /region_name="Ribosomal_L39"
                     /note="Ribosomal L39 protein; pfam00832"
                     /db_xref="CDD:425894"
     CDS             1..51
                     /gene="RPL39"
                     /gene_synonym="eL39; L39; RPL39P42; RPL39_23_1806"
                     /coded_by="NM_001000.4:55..210"
                     /db_xref="CCDS:CCDS14586.1"
                     /db_xref="GeneID:6170"
                     /db_xref="HGNC:HGNC:10350"
                     /db_xref="MIM:300899"
ORIGIN      
        1 msshktfrik rflakkqkqn rpipqwirmk tgnkirynsk rrhwrrtklg l
//
LOCUS       NP_001356803            1047 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 10 [Homo sapiens].
ACCESSION   NP_001356803 XP_016870817
VERSION     NP_001356803.1
DBSOURCE    REFSEQ: accession NM_001369874.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1047)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1047)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1047)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1047)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1047)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1047)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1047)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1047)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1047)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1047)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358113.21.
            
            On Apr 23, 2019 this sequence version replaced XP_016870817.1.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.181986.1,
                                           SRR1660805.195335.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1047
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1047
                     /product="tight junction protein 2 isoform 10"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=118238
     Region          36..122
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(47..53,71,74,102,106,109..110)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          148..>230
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          187..>278
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          310..388
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(310..316,321..337,340..342,345,347..348,355,
                     363..364,366..367,379..385)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(322..328,334,337,367,371,374..375)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          513..594
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(524..530,540,543,572,576,579..580)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          608..670
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(617,619,622,626,647..648,664,666..667)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          704..883
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1047
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_001369874.1:8..3151"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS94416.1"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 mktaqalhrm wiqavkklrr wkgrapgmee liweqytvtl qkdskrgfgi avsggrdnph
       61 fengetsivi sdvlpggpad gllqendrvv mvngtpmedv lhsfavqqlr ksgkvaaivv
      121 krprkvqvaa lqasppldqd drafevmdef dgrsfrsgys ersrlnshgg rsrswedspe
      181 rgrpherars rerdlsrdrs rgrslergld qdhartrdrs rgrslergld hdfgpsrdrd
      241 rdrsrgrsid qdyerayhra ydpdyerays peyrrgarhd arsrgprsrs rehphsrsps
      301 peprgrpgpi gvllmksran eeyglrlgsq ifvkemtrtg latkdgnlhe gdiilkingt
      361 vtenmsltda rklieksrgk lqlvvlrdsq qtlinipsln dsdseiedis eiesnrsfsp
      421 eerrhqysdy dyhssseklk erpssredtp srlsrmgatp tpfkstgdia gtvvpetnke
      481 pryqedppap qpkaaprtfl rpspedeaiy gpntkmvrfk kgdsvglrla ggndvgifva
      541 giqegtsaeq eglqegdqil kvntqdfrgl vredavlyll eipkgemvti laqsradvyr
      601 dilacgrgds ffirshfece ketpqslaft rgevfrvvdt lydgklgnwl avrignelek
      661 glipnksrae qmasvqnaqr dnagdradfw rmrgqrsgvk knlrksredl tavvsvstkf
      721 payervllre agfkrpvvlf gpiadiamek lanelpdwfq taktepkdag sekstgvvrl
      781 ntvrqiieqd khalldvtpk avdllnytqw fpiviffnpd srqgvktmrq rlnptsnkss
      841 rklfdqankl kktcahlfta tinlnsands wfgslkdtiq hqqgeavwvs egkmegmddd
      901 pedrmsylta mgadylscds rlisdfedtd geggaytdne ldepaeeplv ssitrssepv
      961 qheeieiaqk hpdiyavpik thkpdpgtpq htssrppepq kapsrpyqdt rgsygsdaee
     1021 eeyrqqlseh skrgyygqsa ryrdtel
//
LOCUS       NP_001317221             495 aa            linear   PRI 20-NOV-2025
DEFINITION  metastasis-associated protein MTA2 isoform 2 [Homo sapiens].
ACCESSION   NP_001317221 XP_016874050
VERSION     NP_001317221.1
DBSOURCE    REFSEQ: accession NM_001330292.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Morgenstern,E., Molthof,C., Schwartz,U., Graf,J., Bruckmann,A.,
            Hombach,S. and Kretz,M.
  TITLE     lncRNA LINC00941 modulates MTA2/NuRD occupancy to suppress
            premature human epidermal differentiation
  JOURNAL   Life Sci Alliance 7 (7), e202302475 (2024)
   PUBMED   38649186
  REMARK    GeneRIF: lncRNA LINC00941 modulates MTA2/NuRD occupancy to suppress
            premature human epidermal differentiation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Xie,G., Lei,B., Yin,Z., Xu,F. and Liu,X.
  TITLE     CircMTA2 Drives Gastric Cancer Progression through Suppressing MTA2
            Degradation via Interacting with UCHL3
  JOURNAL   Int J Mol Sci 25 (5), 2817 (2024)
   PUBMED   38474064
  REMARK    GeneRIF: CircMTA2 Drives Gastric Cancer Progression through
            Suppressing MTA2 Degradation via Interacting with UCHL3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Huang,X., Tan,J., Chen,M., Zheng,W., Zou,S., Ye,X., Li,Y. and Wu,M.
  TITLE     Prognostic, Immunological, and Mutational Analysis of MTA2 in
            Pan-Cancer and Drug Screening for Hepatocellular Carcinoma
  JOURNAL   Biomolecules 13 (6), 883 (2023)
   PUBMED   37371463
  REMARK    GeneRIF: Prognostic, Immunological, and Mutational Analysis of MTA2
            in Pan-Cancer and Drug Screening for Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Wade,P.A., Gegonne,A., Jones,P.L., Ballestar,E., Aubry,F. and
            Wolffe,A.P.
  TITLE     Mi-2 complex couples DNA methylation to chromatin remodelling and
            histone deacetylation
  JOURNAL   Nat Genet 23 (1), 62-66 (1999)
   PUBMED   10471500
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Zhang,Y., Ng,H.H., Erdjument-Bromage,H., Tempst,P., Bird,A. and
            Reinberg,D.
  TITLE     Analysis of the NuRD subunits reveals a histone deacetylase core
            complex and a connection with DNA methylation
  JOURNAL   Genes Dev 13 (15), 1924-1935 (1999)
   PUBMED   10444591
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Futamura,M., Nishimori,H., Shiratsuchi,T., Saji,S., Nakamura,Y. and
            Tokino,T.
  TITLE     Molecular cloning, mapping, and characterization of a novel human
            gene, MTA1-L1, showing homology to a metastasis-associated gene,
            MTA1
  JOURNAL   J Hum Genet 44 (1), 52-56 (1999)
   PUBMED   9929979
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Xue,Y., Wong,J., Moreno,G.T., Young,M.K., Cote,J. and Wang,W.
  TITLE     NURD, a novel complex with both ATP-dependent chromatin-remodeling
            and histone deacetylase activities
  JOURNAL   Mol Cell 2 (6), 851-861 (1998)
   PUBMED   9885572
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Tong,J.K., Hassig,C.A., Schnitzler,G.R., Kingston,R.E. and
            Schreiber,S.L.
  TITLE     Chromatin deacetylation by an ATP-dependent nucleosome remodelling
            complex
  JOURNAL   Nature 395 (6705), 917-921 (1998)
   PUBMED   9804427
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Zhang,Y., LeRoy,G., Seelig,H.P., Lane,W.S. and Reinberg,D.
  TITLE     The dermatomyositis-specific autoantigen Mi2 is a component of a
            complex containing histone deacetylase and nucleosome remodeling
            activities
  JOURNAL   Cell 95 (2), 279-289 (1998)
   PUBMED   9790534
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301569.1, CR975270.1,
            BC053650.1 and BF590712.1.
            
            On Aug 29, 2016 this sequence version replaced XP_016874050.1.
            
            Summary: This gene encodes a protein that has been identified as a
            component of NuRD, a nucleosome remodeling deacetylase complex
            identified in the nucleus of human cells. It shows a very broad
            expression pattern and is strongly expressed in many tissues. It
            may represent one member of a small gene family that encode
            different but related proteins involved either directly or
            indirectly in transcriptional regulation. Their indirect effects on
            transcriptional regulation may include chromatin remodeling. It is
            closely related to another member of this family, a protein that
            has been correlated with the metastatic potential of certain
            carcinomas. These two proteins are so closely related that they
            share the same types of domains. These domains include two DNA
            binding domains, a dimerization domain, and a domain commonly found
            in proteins that methylate DNA. One of the proteins known to be a
            target protein for this gene product is p53. Deacetylation of p53
            is correlated with a loss of growth inhibition in transformed cells
            supporting a connection between these gene family members and
            metastasis. [provided by RefSeq, May 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301569.1, SRR18074969.3596053.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..495
                     /product="metastasis-associated protein MTA2 isoform 2"
                     /note="metastasis-associated protein 2; metastasis
                     associated gene family, member 2; metastasis-associated
                     1-like 1; metastasis -associated gene 1-like 1;
                     metastasis-associated protein MTA2; MTA1-L1 protein; p53
                     target protein in deacetylase complex"
                     /calculated_mol_wt=54906
     Region          <1..25
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Region          94..139
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(95,125..126,128..129,131..133,135..137)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          190..241
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          276..351
                     /region_name="MTA_R1"
                     /note="MTA R1 domain; pfam17226"
                     /db_xref="CDD:465388"
     CDS             1..495
                     /gene="MTA2"
                     /gene_synonym="MTA1L1; PID"
                     /coded_by="NM_001330292.2:720..2207"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81576.1"
                     /db_xref="GeneID:9219"
                     /db_xref="HGNC:HGNC:7411"
                     /db_xref="MIM:603947"
ORIGIN      
        1 memkvwdpdn pltdrqidqf lvvaravgtf araldcsssi rqpslhmsaa aasrditlfh
       61 amdtlqrngy dlakamstlv pqggpvlcrd emeewsasea mlfeealeky gkdfndirqd
      121 flpwkslasi vqfyymwktt dryiqqkrlk aaeadsklkq vyiptytkpn pnqiisvgsk
      181 pgmngagfqk gltceschtt qsaqwyawgp pnmqcrlcas cwiywkkygg lktptqlega
      241 trgttephsr ghlsrpeaqs lspyttsanr akllaknrqt fllqttkltr larrmcrdll
      301 qprraarrpy apinanaika ecsirlpkaa ktplkihplv rlplativkd lvaqaplkpk
      361 tprgtktpin rnqlsqnrgl ggimvkraye tmagagvpfs angrplasgi rsssqpaakr
      421 qklnpadapn pvvfvatkdt ralrkalthl emrraarrpn lplkvkptli avrppvplpa
      481 pshpastnep ivled
//
LOCUS       NP_663723                245 aa            linear   PRI 20-NOV-2025
DEFINITION  14-3-3 protein zeta/delta [Homo sapiens].
ACCESSION   NP_663723
VERSION     NP_663723.1
DBSOURCE    REFSEQ: accession NM_145690.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Lughmani,H., Patel,H. and Chakravarti,R.
  TITLE     Structural Features and Physiological Associations of Human
            14-3-3zeta Pseudogenes
  JOURNAL   Genes (Basel) 15 (4), 399 (2024)
   PUBMED   38674334
  REMARK    GeneRIF: Structural Features and Physiological Associations of
            Human 14-3-3zeta Pseudogenes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Shi,L., Wang,X., Guo,S., Gou,H., Shang,H., Jiang,X., Wei,C.,
            Wang,J., Li,C., Wang,L., Zhao,Z., Yu,W. and Yu,J.
  TITLE     TMEM65 promotes gastric tumorigenesis by targeting YWHAZ to
            activate PI3K-Akt-mTOR pathway and is a therapeutic target
  JOURNAL   Oncogene 43 (13), 931-943 (2024)
   PUBMED   38341472
  REMARK    GeneRIF: TMEM65 promotes gastric tumorigenesis by targeting YWHAZ
            to activate PI3K-Akt-mTOR pathway and is a therapeutic target.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Mukherjee,S., Roy,S., Mukherjee,S., Harikishore,A., Bhunia,A. and
            Mandal,A.K.
  TITLE     14-3-3 interaction with phosphodiesterase 8A sustains PKA signaling
            and downregulates the MAPK pathway
  JOURNAL   J Biol Chem 300 (3), 105725 (2024)
   PUBMED   38325743
  REMARK    GeneRIF: 14-3-3 interaction with phosphodiesterase 8A sustains PKA
            signaling and downregulates the MAPK pathway.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Koyama,S., Williams,L.T. and Kikuchi,A.
  TITLE     Characterization of the interaction of Raf-1 with ras p21 or 14-3-3
            protein in intact cells
  JOURNAL   FEBS Lett 368 (2), 321-325 (1995)
   PUBMED   7628630
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Liu,D., Bienkowska,J., Petosa,C., Collier,R.J., Fu,H. and
            Liddington,R.
  TITLE     Crystal structure of the zeta isoform of the 14-3-3 protein
  JOURNAL   Nature 376 (6536), 191-194 (1995)
   PUBMED   7603574
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Sato,T., Irie,S., Kitada,S. and Reed,J.C.
  TITLE     FAP-1: a protein tyrosine phosphatase that associates with Fas
  JOURNAL   Science 268 (5209), 411-415 (1995)
   PUBMED   7536343
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Kawamoto,S., Shoji,M., Setoguchi,Y., Kato,M., Hashizume,S.,
            Ichikawa,A., Osada,K., Katakura,Y., Tachibana,H. and Murakami,H.
  TITLE     Molecular cloning of the 31 kDa cytosolic phospholipase A2, as an
            antigen recognized by the lung cancer-specific human monoclonal
            antibody, AE6F4
  JOURNAL   Cytotechnology 17 (2), 103-108 (1995)
   PUBMED   7547034
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Zupan,L.A., Steffens,D.L., Berry,C.A., Landt,M. and Gross,R.W.
  TITLE     Cloning and expression of a human 14-3-3 protein mediating
            phospholipolysis. Identification of an arachidonoyl-enzyme
            intermediate during catalysis
  JOURNAL   J Biol Chem 267 (13), 8707-8710 (1992)
   PUBMED   1577711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC072426.1, BM783874.1 and
            AC027373.11.
            
            Summary: This gene product belongs to the 14-3-3 family of proteins
            which mediate signal transduction by binding to
            phosphoserine-containing proteins. This highly conserved protein
            family is found in both plants and mammals, and this protein is 99%
            identical to the mouse, rat and sheep orthologs. The encoded
            protein interacts with IRS1 protein, suggesting a role in
            regulating insulin sensitivity. Several transcript variants that
            differ in the 5' UTR but that encode the same protein have been
            identified for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (2) represents the longest
            transcript. All six transcripts encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.267178.1,
                                           SRR1660803.129561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395958.6/ ENSP00000379288.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..245
                     /product="14-3-3 protein zeta/delta"
                     /note="14-3-3 delta; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, delta polypeptide;
                     14-3-3 zeta; phospholipase A2; protein kinase C inhibitor
                     protein-1; tyrosine 3/tryptophan 5 -monooxygenase
                     activation protein, zeta polypeptide; 14-3-3
                     protein/cytosolic phospholipase A2; epididymis secretory
                     protein Li 93; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, zeta polypeptide;
                     epididymis secretory protein Li 3; epididymis luminal
                     protein 4"
                     /calculated_mol_wt=27614
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Region          2..230
                     /region_name="14-3-3_beta_zeta"
                     /note="14-3-3 beta and zeta isoforms of 14-3-3 protein;
                     cd10022"
                     /db_xref="CDD:206758"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            order(5,8..9,12..13,15..16,18,21,58,61,65,75,78..79,82,
                     85..86,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            order(41..42,45..46,49,117,120,127..128,165,169,172..173,
                     176,209..213,216..217,220,224)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            56
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P63103;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:11956222,
                     ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165,
                     ECO:0000269|PubMed:16376338; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            127
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P63103;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:15071501,
                     ECO:0000269|PubMed:15696159; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63102; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:31024343,
                     ECO:0000269|PubMed:9360956, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     CDS             1..245
                     /gene="YWHAZ"
                     /gene_synonym="14-3-3-zeta; HEL-S-3; HEL-S-93; HEL4;
                     KCIP-1; POPCHAS; YWHAD"
                     /coded_by="NM_145690.3:104..841"
                     /db_xref="CCDS:CCDS6290.1"
                     /db_xref="GeneID:7534"
                     /db_xref="HGNC:HGNC:12855"
                     /db_xref="MIM:601288"
ORIGIN      
        1 mdknelvqka klaeqaeryd dmaacmksvt eqgaelsnee rnllsvaykn vvgarrsswr
       61 vvssieqkte gaekkqqmar eyrekietel rdicndvlsl lekflipnas qaeskvfylk
      121 mkgdyyryla evaagddkkg ivdqsqqayq eafeiskkem qpthpirlgl alnfsvfyye
      181 ilnspekacs laktafdeai aeldtlsees ykdstlimql lrdnltlwts dtqgdeaeag
      241 eggen
//
LOCUS       NP_001354975            1005 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 7 isoform f [Homo sapiens].
ACCESSION   NP_001354975
VERSION     NP_001354975.1
DBSOURCE    REFSEQ: accession NM_001368046.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1005)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1005)
  AUTHORS   Maciejewski,K., Giers,M., Oleksiewicz,U. and Czerwinska,P.
  TITLE     The Epigenetic Modifiers HDAC2 and HDAC7 Inversely Associate with
            Cancer Stemness and Immunity in Solid Tumors
  JOURNAL   Int J Mol Sci 25 (14), 7841 (2024)
   PUBMED   39063083
  REMARK    GeneRIF: The Epigenetic Modifiers HDAC2 and HDAC7 Inversely
            Associate with Cancer Stemness and Immunity in Solid Tumors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1005)
  AUTHORS   Lu,W., Zhuang,G., Guan,Y., Li,Y., Liu,L. and Xiao,M.
  TITLE     Comprehensive analysis of HDAC7 expression and its prognostic value
            in diffuse large B cell lymphoma: A review
  JOURNAL   Medicine (Baltimore) 102 (45), e34577 (2023)
   PUBMED   37960766
  REMARK    GeneRIF: Comprehensive analysis of HDAC7 expression and its
            prognostic value in diffuse large B cell lymphoma: A review.
            Review article
REFERENCE   4  (residues 1 to 1005)
  AUTHORS   Qin,X., Long,Y., Bai,X., Cao,L., Yan,H., Zhang,K., Wang,B. and
            Wu,X.
  TITLE     The disordered C terminus of ALKBH5 promotes phase separation and
            paraspeckles assembly
  JOURNAL   J Biol Chem 299 (8), 105071 (2023)
   PUBMED   37474102
REFERENCE   5  (residues 1 to 1005)
  AUTHORS   Ling,S., Chen,T., Wang,S., Zhang,W., Zhou,R., Xia,X., Yao,Z.,
            Fan,Y., Ning,S., Liu,J., Qin,L., Tucker,H.O., Wang,N. and Guo,X.
  TITLE     Deacetylation of FOXP1 by HDAC7 potentiates self-renewal of
            mesenchymal stem cells
  JOURNAL   Stem Cell Res Ther 14 (1), 188 (2023)
   PUBMED   37507770
  REMARK    GeneRIF: Deacetylation of FOXP1 by HDAC7 potentiates self-renewal
            of mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1005)
  AUTHORS   Lemercier,C., Brocard,M.P., Puvion-Dutilleul,F., Kao,H.Y.,
            Albagli,O. and Khochbin,S.
  TITLE     Class II histone deacetylases are directly recruited by BCL6
            transcriptional repressor
  JOURNAL   J Biol Chem 277 (24), 22045-22052 (2002)
   PUBMED   11929873
  REMARK    GeneRIF: Class II histone deacetylases are directly recruited by
            BCL6 transcriptional repressor
REFERENCE   7  (residues 1 to 1005)
  AUTHORS   Fischle,W., Dequiedt,F., Fillion,M., Hendzel,M.J., Voelter,W. and
            Verdin,E.
  TITLE     Human HDAC7 histone deacetylase activity is associated with HDAC3
            in vivo
  JOURNAL   J Biol Chem 276 (38), 35826-35835 (2001)
   PUBMED   11466315
REFERENCE   8  (residues 1 to 1005)
  AUTHORS   Lee,H.J., Chun,M. and Kandror,K.V.
  TITLE     Tip60 and HDAC7 interact with the endothelin receptor a and may be
            involved in downstream signaling
  JOURNAL   J Biol Chem 276 (20), 16597-16600 (2001)
   PUBMED   11262386
REFERENCE   9  (residues 1 to 1005)
  AUTHORS   Marks,P.A., Richon,V.M. and Rifkind,R.A.
  TITLE     Histone deacetylase inhibitors: inducers of differentiation or
            apoptosis of transformed cells
  JOURNAL   J Natl Cancer Inst 92 (15), 1210-1216 (2000)
   PUBMED   10922406
  REMARK    Review article
REFERENCE   10 (residues 1 to 1005)
  AUTHORS   Kao,H.Y., Downes,M., Ordentlich,P. and Evans,R.M.
  TITLE     Isolation of a novel histone deacetylase reveals that class I and
            class II deacetylases promote SMRT-mediated repression
  JOURNAL   Genes Dev 14 (1), 55-66 (2000)
   PUBMED   10640276
  REMARK    GeneRIF: Characterization of the mouse HDAC7 ortholog.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004466.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene has sequence homology to members of the histone
            deacetylase family. This gene is orthologous to mouse HDAC7 gene
            whose protein promotes repression mediated via the transcriptional
            corepressor SMRT. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6) encodes the longest isoform
            (f).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1817137.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1005
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..1005
                     /product="histone deacetylase 7 isoform f"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase 7A; protein deacetylase HDAC7"
                     /calculated_mol_wt=108219
     Region          571..948
                     /region_name="HDAC7"
                     /note="Histone deacetylase 7; cd10008"
                     /db_xref="CDD:212532"
     Site            order(595,679,722..723,731..732,760,762,791,854,862..863,
                     894)
                     /site_type="active"
                     /db_xref="CDD:212532"
     CDS             1..1005
                     /gene="HDAC7"
                     /gene_synonym="HD7; HD7A; HDAC7A"
                     /coded_by="NM_001368046.1:119..3136"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:51564"
                     /db_xref="HGNC:HGNC:14067"
                     /db_xref="MIM:606542"
ORIGIN      
        1 mhspgadgtq vspgahycsp tgagcprpca dtpgpqpqpm dlrvgqrppv epppeptlla
       61 lqrpqrlhhh lflaglqqqr svepmrlsmd tpmpelqvgp qeqelrqllh kdkskrsava
      121 ssvvkqklae vilkkqqaal ertvhpnspg ipysvptplk qpwhsfcrtl epletegatr
      181 smlssflppv pslpsdppeh fplrktvsep nlklrykpkk slerrknpll rkesappslr
      241 rrpaetlgds spsssstpas gcsspndseh gpnpilgsea llgqrlrlqe tsvapfalpt
      301 vsllpaitlg lpaparadsd rrthptlgpr gpilgsphtp lflphglepe aggtlpsrlq
      361 pillldpsgs haplltvpgl gplpfhfaqs lmtterlsgs glhwplsrtr seplppsata
      421 ppppgpmqpr leqlkthvqv ikrsakpsek prlrqipsae dletdgggpg qvvddglehr
      481 elghgqpear gpaplqqhpq vllweqqrla grlprgstgd tvllplaqgg hrplsraqss
      541 paapaslsap epasqarvls ssetpartlp fttgliydsv mlkhqcscgd nsrhpehagr
      601 iqsiwsrlqe rglrsqcecl rgrkasleel qsvhserhvl lygtnplsrl kldngklagl
      661 laqrmfvmlp cggvgvdtdt iwnelhssna arwaagsvtd lafkvasrel kngfavvrpp
      721 ghhadhstam gfcffnsvai acrqlqqqsk askilivdwd vhhgngtqqt fyqdpsvlyi
      781 slhrhddgnf fpgsgavdev gagsgegfnv nvawaggldp pmgdpeylaa frivvmpiar
      841 efspdlvlvs agfdaaeghp aplggyhvsa kcfgymtqql mnlaggavvl alegghdlta
      901 icdaseacva allgnrvdpl seegwkqkpn lnairsleav irvhskywgc mqrlascpds
      961 wvprvpgadk eeveavtala slsvgilaed rpseqlveee epmnl
//
LOCUS       NP_000976                184 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform a [Homo sapiens].
ACCESSION   NP_000976
VERSION     NP_000976.1
DBSOURCE    REFSEQ: accession NM_000985.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ065502.1, SRR5189661.142702.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..184
                     /product="large ribosomal subunit protein uL22 isoform a"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21266
     Region          1..165
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     Region          160..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18621.3)"
     CDS             1..184
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_000985.5:271..825"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45865.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl
      181 mare
//
LOCUS       NP_705582                169 aa            linear   PRI 20-NOV-2025
DEFINITION  protein UXT isoform 1 [Homo sapiens].
ACCESSION   NP_705582
VERSION     NP_705582.1
DBSOURCE    REFSEQ: accession NM_153477.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Peng,W., Zeng,C., Xu,J., Zhao,H., Zhu,Q., Xu,H., Chen,H., Huang,H.,
            Zhou,Y. and Zhao,C.
  TITLE     Regulation of epithelial cell differentiation by the Ubiquitous
            expressed transcript isoform 1 in ulcerative colitis
  JOURNAL   J Gastroenterol Hepatol 38 (11), 2006-2017 (2023)
   PUBMED   37608570
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Lemma,R.B., Ledsaak,M., Fuglerud,B.M., Rodriguez-Castaneda,F.,
            Eskeland,R. and Gabrielsen,O.S.
  TITLE     MYB regulates the SUMO protease SENP1 and its novel interaction
            partner UXT, modulating MYB target genes and the SUMO landscape
  JOURNAL   J Biol Chem 299 (9), 105062 (2023)
   PUBMED   37468105
  REMARK    GeneRIF: MYB regulates the SUMO protease SENP1 and its novel
            interaction partner UXT, modulating MYB target genes and the SUMO
            landscape.
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Zhao,H., Chen,C., Yang,C., Mo,S., Zhao,H. and Tian,Y.
  TITLE     Prefoldin and prefoldin-like complex subunits as predictive
            biomarkers for hepatocellular carcinoma immunotherapy
  JOURNAL   Pathol Res Pract 232, 153808 (2022)
   PUBMED   35217267
  REMARK    GeneRIF: Prefoldin and prefoldin-like complex subunits as
            predictive biomarkers for hepatocellular carcinoma immunotherapy.
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Hu,X.C., Chu,J., Zhou,Y., Li,C.C., Zhou,G.J. and Jiang,G.Q.
  TITLE     HOXD9 transcriptionally induced UXT facilitate breast cancer
            progression via epigenetic modification of RND3
  JOURNAL   Cell Signal 90, 110188 (2022)
   PUBMED   34767964
  REMARK    GeneRIF: HOXD9 transcriptionally induced UXT facilitate breast
            cancer progression via epigenetic modification of RND3.
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Liu,L., Amy,V., Liu,G. and McKeehan,W.L.
  TITLE     Novel complex integrating mitochondria and the microtubular
            cytoskeleton with chromosome remodeling and tumor suppressor RASSF1
            deduced by in silico homology analysis, interaction cloning in
            yeast, and colocalization in cultured cells
  JOURNAL   In Vitro Cell Dev Biol Anim 38 (10), 582-594 (2002)
   PUBMED   12762840
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Thiselton,D.L., McDowall,J., Brandau,O., Ramser,J., d'Esposito,F.,
            Bhattacharya,S.S., Ross,M.T., Hardcastle,A.J. and Meindl,A.
  TITLE     An integrated, functionally annotated gene map of the DXS8026-ELK1
            interval on human Xp11.3-Xp11.23: potential hotspot for
            neurogenetic disorders
  JOURNAL   Genomics 79 (4), 560-572 (2002)
   PUBMED   11944989
  REMARK    Erratum:[Genomics 2002 Jun;79(6):891]
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Markus,S.M., Taneja,S.S., Logan,S.K., Li,W., Ha,S., Hittelman,A.B.,
            Rogatsky,I. and Garabedian,M.J.
  TITLE     Identification and characterization of ART-27, a novel coactivator
            for the androgen receptor N terminus
  JOURNAL   Mol Biol Cell 13 (2), 670-682 (2002)
   PUBMED   11854421
  REMARK    GeneRIF: UXT was identified in a screen for proteins that interact
            with the Androgen Receptor N-terminal activation domain.  We termed
            the protein Androgen Receptor Trapped clone 27 (ART-27).  ART-27
            appears to function as a transcriptional coactivator protein.
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Liu,L. and McKeehan,W.L.
  TITLE     Sequence analysis of LRPPRC and its SEC1 domain interaction
            partners suggests roles in cytoskeletal organization, vesicular
            trafficking, nucleocytosolic shuttling, and chromosome activity
  JOURNAL   Genomics 79 (1), 124-136 (2002)
   PUBMED   11827465
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Schroer,A., Schneider,S., Ropers,H. and Nothwang,H.
  TITLE     Cloning and characterization of UXT, a novel gene in human Xp11,
            which is widely and abundantly expressed in tumor tissue
  JOURNAL   Genomics 56 (3), 340-343 (1999)
   PUBMED   10087202
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA372561.1, AF083242.1 and
            BQ681820.1.
            
            Summary: The protein encoded by this gene functions as a cofactor
            that modulates androgen receptor-dependent transcription, and also
            plays a critical role in tumor necrosis factor-induced apoptosis.
            Expression of this gene may play a role in tumorigenesis.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Nov
            2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BE856894.1, BC000720.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..169
                     /product="protein UXT isoform 1"
                     /note="protein UXT; SKP2-associated alpha PFD 1;
                     ubiquitously expressed transcript protein; androgen
                     receptor trapped clone 27 protein"
                     /calculated_mol_wt=19466
     Region          32..158
                     /region_name="Prefoldin_UXT"
                     /note="protein UXT; cd23158"
                     /db_xref="CDD:467474"
     Region          33..71
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467474"
     Site            order(60,63..64,67..68,70..71,79..86,88..97,100..104,
                     108..113,122)
                     /site_type="other"
                     /note="putative prefoldin oligomer interface [polypeptide
                     binding]"
                     /db_xref="CDD:467474"
     Region          116..156
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467474"
     CDS             1..169
                     /gene="UXT"
                     /gene_synonym="ART-27; SKP2; STAP1"
                     /coded_by="NM_153477.3:218..727"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14284.1"
                     /db_xref="GeneID:8409"
                     /db_xref="HGNC:HGNC:12641"
                     /db_xref="MIM:300234"
ORIGIN      
        1 mvfplptpqe pimatppkrr aveatgekvl ryetfisdvl qrdlrkvldh rdkvyeqlak
       61 ylqlrnvier lqeakhsely mqvdlgcnff vdtvvpdtsr iyvalgygff leltlaealk
      121 fidrkssllt elsnsltkds mnikahihml leglrelqgl qnfpekphh
//
LOCUS       NP_001258864             146 aa            linear   PRI 20-NOV-2025
DEFINITION  thymidine kinase 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001258864
VERSION     NP_001258864.1
DBSOURCE    REFSEQ: accession NM_001271935.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Aoki,H., Higashi,M., Okita,M., Ando,N., Murayama,S., Ishikawa,K.
            and Yokota,T.
  TITLE     Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n
  JOURNAL   Cerebellum 22 (1), 70-84 (2023)
   PUBMED   35084690
  REMARK    GeneRIF: Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Dominguez-Gonzalez,C., Hernandez-Voth,A., de Fuenmayor-Fernandez de
            la Hoz,C.P., Guerrero,L.B., Moris,G., Garcia-Garcia,J., Muelas,N.,
            Leon Hernandez,J.C., Rabasa,M., Lora,D., Blazquez,A., Arenas,J. and
            Martin,M.A.
  TITLE     Metrics of progression and prognosis in untreated adults with
            thymidine kinase 2 deficiency: An observational study
  JOURNAL   Neuromuscul Disord 32 (9), 728-735 (2022)
   PUBMED   35907766
  REMARK    GeneRIF: Metrics of progression and prognosis in untreated adults
            with thymidine kinase 2 deficiency: An observational study.
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Wang,L. and Eriksson,S.
  TITLE     Mutational analyses of human thymidine kinase 2 reveal key residues
            in ATP-Mg2+ binding and catalysis
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 41 (3), 264-272 (2022)
   PUBMED   34758700
  REMARK    GeneRIF: Mutational analyses of human thymidine kinase 2 reveal key
            residues in ATP-Mg(2+) binding and catalysis.
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Kierdaszuk,B., Krawiec,K., Kazimierczuk,Z., Jacobsson,U.,
            Johansson,N.G., Munch-Petersen,B., Eriksson,S. and Shugar,D.
  TITLE     Substrate/inhibitor specificities of human deoxycytidine kinase
            (dCK) and thymidine kinases (TK1 and TK2)
  JOURNAL   Adv Exp Med Biol 431, 623-627 (1998)
   PUBMED   9598140
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning of the cDNA and chromosome localization of the gene for
            human thymidine kinase 2
  JOURNAL   J Biol Chem 272 (13), 8454-8458 (1997)
   PUBMED   9079672
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Wang,J., El-Hattab,A.W. and Wong,L.J.C.
  TITLE     TK2-Related Mitochondrial DNA Maintenance Defect, Myopathic Form
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23230576
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Jansson,O., Bohman,C., Munch-Petersen,B. and Eriksson,S.
  TITLE     Mammalian thymidine kinase 2. Direct photoaffinity labeling with
            [32P]dTTP of the enzyme from spleen, liver, heart and brain
  JOURNAL   Eur J Biochem 206 (2), 485-490 (1992)
   PUBMED   1597187
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Willecke,K., Teber,T., Kucherlapati,R.S. and Ruddle,F.H.
  TITLE     Human mitochondrial thymidine kinase is coded for by a gene on
            chromosome 16 of the nucleus
  JOURNAL   Somatic Cell Genet 3 (3), 237-245 (1977)
   PUBMED   605384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U77088.1, BC134344.1,
            BC113928.1, AC010542.7 and AL038860.1.
            
            Summary: This gene encodes a deoxyribonucleoside kinase that
            specifically phosphorylates thymidine, deoxycytidine, and
            deoxyuridine. The encoded enzyme localizes to the mitochondria and
            is required for mitochondrial DNA synthesis. Mutations in this gene
            are associated with a myopathic form of mitochondrial DNA depletion
            syndrome. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms, some of which lack transit
            peptide, so are not localized to mitochondria. [provided by RefSeq,
            Dec 2012].
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks a
            portion of the 5' coding region and two internal exons, and
            initiates translation at an alternate start codon, compared to
            variant 1. The encoded isoform (6) is not localized to
            mitochondria, and it has a distinct N-terminus, lacks an internal
            segment and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC113928.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..146
                     /product="thymidine kinase 2 isoform 6"
                     /EC_number="2.7.1.74"
                     /EC_number="2.7.1.21"
                     /note="mt-TK; thymidine kinase 2, mitochondrial;
                     deoxycytidine kinase TK2; 2'-deoxyuridine kinase TK2;
                     mitochondrial thymidine kinase"
                     /calculated_mol_wt=16804
     Region          22..>121
                     /region_name="NK"
                     /note="Nucleoside/nucleotide kinase (NK) is a protein
                     superfamily consisting of multiple families of enzymes
                     that share structural similarity and are functionally
                     related to the catalysis of the reversible phosphate group
                     transfer from nucleoside triphosphates...; cl17190"
                     /db_xref="CDD:450170"
     Site            order(26,31..34)
                     /site_type="active"
                     /db_xref="CDD:238836"
     CDS             1..146
                     /gene="TK2"
                     /gene_synonym="MTDPS2; MTTK; PEOB3; SCA31; TK2-EXT"
                     /coded_by="NM_001271935.1:9..449"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS92169.1"
                     /db_xref="GeneID:7084"
                     /db_xref="HGNC:HGNC:11831"
                     /db_xref="MIM:188250"
ORIGIN      
        1 mgafcqrpss dkeqekekks vicvegnias gkttcleffs natdvevlte pvskwrnvrg
       61 hnplglmyhd asrwgltlqt yvqltmldrh trpqvssvrl mersihsary ifvenlyrrn
      121 twkqftismr sgsskaafsp wqplfw
//
LOCUS       NP_001335049             564 aa            linear   PRI 20-NOV-2025
DEFINITION  tripartite motif-containing protein 16 isoform a [Homo sapiens].
ACCESSION   NP_001335049
VERSION     NP_001335049.1
DBSOURCE    REFSEQ: accession NM_001348120.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Guo,D., Zhang,M., Wei,T., Zhang,X., Shi,X., Tang,H., Ding,M.,
            Li,J., Zhang,S. and Guo,W.
  TITLE     NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16
  JOURNAL   Cell Mol Life Sci 81 (1), 167 (2024)
   PUBMED   38581570
  REMARK    GeneRIF: NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Li,S., Wang,J., Chen,H., Hou,J., Shen,T., Li,J., Zhou,B., Zhang,B.,
            Liu,H. and Jiang,D.K.
  TITLE     TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin pathway
  JOURNAL   Mol Carcinog 62 (11), 1686-1699 (2023)
   PUBMED   37477507
  REMARK    GeneRIF: TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin
            pathway.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Roshanazadeh,M.R., Adelipour,M., Sanaei,A., Chenane,H. and
            Rashidi,M.
  TITLE     TRIM3 and TRIM16 as potential tumor suppressors in breast cancer
            patients
  JOURNAL   BMC Res Notes 15 (1), 312 (2022)
   PUBMED   36180926
  REMARK    GeneRIF: TRIM3 and TRIM16 as potential tumor suppressors in breast
            cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Wang,Y., Wu,Y. and Xie,S.
  TITLE     CircPTK2 inhibits cell cisplatin (CDDP) resistance by targeting
            miR-942/TRIM16 axis in non-small cell lung cancer (NSCLC)
  JOURNAL   Bioengineered 13 (2), 3651-3664 (2022)
   PUBMED   35230201
  REMARK    GeneRIF: CircPTK2 inhibits cell cisplatin (CDDP) resistance by
            targeting miR-942/TRIM16 axis in non-small cell lung cancer
            (NSCLC).
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Gwinn,M.R., Whipkey,D.L., Tennant,L.B. and Weston,A.
  TITLE     Differential gene expression in normal human mammary epithelial
            cells treated with malathion monitored by DNA microarrays
  JOURNAL   Environ Health Perspect 113 (8), 1046-1051 (2005)
   PUBMED   16079077
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Beer,H.D., Munding,C., Dubois,N., Mamie,C., Hohl,D. and Werner,S.
  TITLE     The estrogen-responsive B box protein: a novel regulator of
            keratinocyte differentiation
  JOURNAL   J Biol Chem 277 (23), 20740-20749 (2002)
   PUBMED   11919186
  REMARK    GeneRIF: role in regulating keratinocyte differentiation
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Liu,H.L., Golder-Novoselsky,E., Seto,M.H., Webster,L., McClary,J.
            and Zajchowski,D.A.
  TITLE     The novel estrogen-responsive B-box protein (EBBP) gene is
            tamoxifen-regulated in cells expressing an estrogen receptor
            DNA-binding domain mutant
  JOURNAL   Mol Endocrinol 12 (11), 1733-1748 (1998)
   PUBMED   9817599
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005324.1.
            
            Summary: The protein encoded by this gene is a tripartite motif
            (TRIM) family member that contains two B box domains and a
            coiled-coiled region that are characteristic of the B box zinc
            finger protein family. While it lacks a RING domain found in other
            TRIM proteins, the encoded protein can homodimerize or
            heterodimerize with other TRIM proteins and has E3 ubiquitin ligase
            activity. This gene is also a tumor suppressor and is involved in
            secretory autophagy. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (2), as well as variants 1 and 3,
            encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.179090.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..564
                     /product="tripartite motif-containing protein 16 isoform
                     a"
                     /EC_number="2.3.2.27"
                     /note="estrogen-responsive B box protein; tripartite
                     motif-containing protein 16; E3 ubiquitin-protein ligase
                     TRIM16"
                     /calculated_mol_wt=63824
     Region          1..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95361.3)"
     Region          75..122
                     /region_name="Bbox1_TRIM16"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 16 (TRIM16) and similar proteins;
                     cd19839"
                     /db_xref="CDD:380897"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27693506; propagated from
                     UniProtKB/Swiss-Prot (O95361.3)"
     Region          129..173
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <164..>283
                     /region_name="CusB_dom_1"
                     /note="Cation efflux system protein CusB domain 1;
                     cl46872"
                     /db_xref="CDD:481212"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27693506; propagated from
                     UniProtKB/Swiss-Prot (O95361.3)"
     Region          365..546
                     /region_name="SPRY_PRY_TRIM16"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 16 (TRIM16); cd12890"
                     /db_xref="CDD:293948"
     CDS             1..564
                     /gene="TRIM16"
                     /gene_synonym="EBBP"
                     /coded_by="NM_001348120.1:767..2461"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11171.1"
                     /db_xref="GeneID:10626"
                     /db_xref="HGNC:HGNC:17241"
                     /db_xref="MIM:609505"
ORIGIN      
        1 maeldlmapg plprataqpp aplspdsgsp spdsgsaspv eeedvgssek lgreteeqds
       61 dsaeqgdpag egkevlcdfc lddtrrvkav kscltcmvny ceehlqphqv niklqshllt
      121 epvkdhnwry cpahhsplsa fccpdqqcic qdccqehsgh tivsldaarr dkeaelqctq
      181 ldlerklkln enaisrlqan qksvlvsvse vkavaemqfg ellaavrkaq anvmlfleek
      241 eqaalsqang ikahleyrsa emekskqele rmaaisntvq fleeyckfkn teditfpsvy
      301 vglkdklsgi rkvitestvh liqllenykk klqefskeee ydirtqvsav vqrkywtskp
      361 epstreqflq yayditfdpd tahkylrlqe enrkvtnttp wehpypdlps rflhwrqvls
      421 qqslylhryy feveifgagt yvgltckgid rkgeernsci sgnnfswslq wngkeftawy
      481 sdmetplkag pfrrlgvyid fpggilsfyg veydtmtlvh kfackfsepv yaafwlskke
      541 nairivdlge epekpapslv gtap
//
LOCUS       NP_002255                538 aa            linear   PRI 20-NOV-2025
DEFINITION  importin subunit alpha-5 [Homo sapiens].
ACCESSION   NP_002255
VERSION     NP_002255.3
DBSOURCE    REFSEQ: accession NM_002264.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Zhao,L., Wu,D., Qu,Q., Li,Z. and Yin,H.
  TITLE     Karyopherin Subunit Alpha 1 Enhances the Malignant Behaviors of
            Colon Cancer Cells via Promoting Nuclear Factor-kappaB p65 Nuclear
            Translocation
  JOURNAL   Dig Dis Sci 68 (7), 3018-3031 (2023)
   PUBMED   37038032
  REMARK    GeneRIF: Karyopherin Subunit Alpha 1 Enhances the Malignant
            Behaviors of Colon Cancer Cells via Promoting Nuclear Factor-kappaB
            p65 Nuclear Translocation.
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Jiang,L., Li,D., Wang,C., Liao,J., Liu,J., Wei,Q. and Wang,Y.
  TITLE     Decreased Expression of Karyopherin-alpha 1 is Related to the
            Malignant Degree of Cervical Cancer and is Critical for the
            Proliferation of Hela Cells
  JOURNAL   Pathol Oncol Res 28, 1610518 (2022)
   PUBMED   35991835
  REMARK    GeneRIF: Decreased Expression of Karyopherin-alpha 1 is Related to
            the Malignant Degree of Cervical Cancer and is Critical for the
            Proliferation of Hela Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Tsoi,H., Man,E.P., Leung,M.H., Mok,K.C., Chau,K.M., Wong,L.S.,
            Chan,W.L., Chan,S.Y., Luk,M.Y., Cheng,C.N. and Khoo,U.S.
  TITLE     KPNA1 regulates nuclear import of NCOR2 splice variant BQ323636.1
            to confer tamoxifen resistance in breast cancer
  JOURNAL   Clin Transl Med 11 (10), e554 (2021)
   PUBMED   34709749
  REMARK    GeneRIF: KPNA1 regulates nuclear import of NCOR2 splice variant
            BQ323636.1 to confer tamoxifen resistance in breast cancer.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Di Marzio,P., Choe,S., Ebright,M., Knoblauch,R. and Landau,N.R.
  TITLE     Mutational analysis of cell cycle arrest, nuclear localization and
            virion packaging of human immunodeficiency virus type 1 Vpr
  JOURNAL   J Virol 69 (12), 7909-7916 (1995)
   PUBMED   7494303
REFERENCE   7  (residues 1 to 538)
  AUTHORS   O'Neill,R.E., Jaskunas,R., Blobel,G., Palese,P. and Moroianu,J.
  TITLE     Nuclear import of influenza virus RNA can be mediated by viral
            nucleoprotein and transport factors required for protein import
  JOURNAL   J Biol Chem 270 (39), 22701-22704 (1995)
   PUBMED   7559393
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Sharova,N. and Bukrinskaya,A.
  TITLE     p17 and p17-containing gag precursors of input human
            immunodeficiency virus are transported into the nuclei of infected
            cells
  JOURNAL   AIDS Res Hum Retroviruses 7 (3), 303-306 (1991)
   PUBMED   2064827
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Mukaigawa,J. and Nayak,D.P.
  TITLE     Two signals mediate nuclear localization of influenza virus
            (A/WSN/33) polymerase basic protein 2
  JOURNAL   J Virol 65 (1), 245-253 (1991)
   PUBMED   1985200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA308391.1, U20620.1,
            BC003009.1 and AC083798.14.
            
            On Jan 30, 2009 this sequence version replaced NP_002255.2.
            
            Summary: The transport of molecules between the nucleus and the
            cytoplasm in eukaryotic cells is mediated by the nuclear pore
            complex (NPC), which consists of 60-100 proteins. Small molecules
            (up to 70 kD) can pass through the nuclear pore by nonselective
            diffusion while larger molecules are transported by an active
            process. The protein encoded by this gene belongs to the importin
            alpha family, and is involved in nuclear protein import. This
            protein interacts with the recombination activating gene 1 (RAG1)
            protein and is a putative substrate of the RAG1 ubiquitin ligase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) lacks an alternate exon
            compared to variant 2 and represents the protein-coding transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.80941.1,
                                           SRR1803616.269053.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344337.11/ ENSP00000343701.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.1"
     Protein         1..538
                     /product="importin subunit alpha-5"
                     /note="importin-alpha-S1; importin alpha 5; importin
                     subunit alpha-1; recombination activating gene cohort 2;
                     nucleoprotein interactor 1; SRP1-beta; RAG cohort protein
                     2; karyopherin alpha 1 (importin alpha 5)"
                     /calculated_mol_wt=60091
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in Importin subunit alpha-5,
                     N-terminally processed.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Region          33..516
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          42..51
                     /region_name="nuclear localization signal"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P52294.3)"
     Region          77..117
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          118..161
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          128..154
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(145,149,153,187,191,195,230,234,238)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          149..241
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250|UniProtKB:P52293"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          162..198
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          204..239
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          207..245
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          245..437
                     /region_name="Binding to RAG1.
                     /evidence=ECO:0000269|PubMed:8052633"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          256..281
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          289..325
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          318..406
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250|UniProtKB:P52293"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Site            order(356,360,364,398,402,406,441,445,449)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          373..409
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          413..457
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     Region          416..450
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          460..504
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (P52294.3)"
     CDS             1..538
                     /gene="KPNA1"
                     /gene_synonym="IPOA5; NPI-1; RCH2; SRP1"
                     /coded_by="NM_002264.4:189..1805"
                     /db_xref="CCDS:CCDS3013.1"
                     /db_xref="GeneID:3836"
                     /db_xref="HGNC:HGNC:6394"
                     /db_xref="MIM:600686"
ORIGIN      
        1 mttpgkenfr lksyknksln pdemrrrree eglqlrkqkr eeqlfkrrnv ataeeeteee
       61 vmsdggfhea qisnmemapg gvitsdmiem ifskspeqql satqkfrkll skepnppide
      121 vistpgvvar fveflkrken ctlqfesawv ltniasgnsl qtriviqaga vpifiellss
      181 efedvqeqav walgniagds tmcrdyvldc nilppllqlf skqnrltmtr navwalsnlc
      241 rgkspppefa kvspclnvls wllfvsdtdv ladacwalsy lsdgpndkiq avidagvcrr
      301 lvellmhndy kvvspalrav gnivtgddiq tqvilncsal qsllhllssp kesikkeacw
      361 tisnitagnr aqiqtvidan ifpalisilq taefrtrkea awaitnatsg gsaeqikylv
      421 elgcikplcd lltvmdskiv qvalngleni lrlgeqeakr ngtginpyca lieeaygldk
      481 ieflqshenq eiyqkafdli ehyfgteded ssiapqvdln qqqyifqqce apmegfql
//
LOCUS       NP_006588                646 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock cognate 71 kDa protein isoform 1 [Homo sapiens].
ACCESSION   NP_006588
VERSION     NP_006588.1
DBSOURCE    REFSEQ: accession NM_006597.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Yang,S., Li,M., Lian,G., Wu,Y., Cui,J. and Wang,L.
  TITLE     ABHD8 antagonizes inflammation by facilitating chaperone-mediated
            autophagy-mediated degradation of NLRP3
  JOURNAL   Autophagy 21 (2), 338-351 (2025)
   PUBMED   39225180
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Chaari,A., Saikia,N., Paul,P., Yousef,M., Ding,F. and Ladjimi,M.
  TITLE     Experimental and computational investigation of the effect of Hsc70
            structural variants on inhibiting amylin aggregation
  JOURNAL   Biophys Chem 309, 107235 (2024)
   PUBMED   38608617
  REMARK    GeneRIF: Experimental and computational investigation of the effect
            of Hsc70 structural variants on inhibiting amylin aggregation.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Rafiq,S., Mungure,I., Banz,Y., Niklaus,N.J., Kaufmann,T.,
            Muller,S., Jacquel,A., Robert,G., Auberger,P., Torbett,B.E.,
            Muller,S., Tschan,M.P. and Humbert,M.
  TITLE     HSPA8 Chaperone Complex Drives Chaperone-Mediated Autophagy
            Regulation in Acute Promyelocytic Leukemia Cell Differentiation
  JOURNAL   Pharmacology 109 (4), 216-230 (2024)
   PUBMED   38569476
  REMARK    GeneRIF: HSPA8 Chaperone Complex Drives Chaperone-Mediated
            Autophagy Regulation in Acute Promyelocytic Leukemia Cell
            Differentiation.
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Hattori,H., Liu,Y.C., Tohnai,I., Ueda,M., Kaneda,T., Kobayashi,T.,
            Tanabe,K. and Ohtsuka,K.
  TITLE     Intracellular localization and partial amino acid sequence of a
            stress-inducible 40-kDa protein in HeLa cells
  JOURNAL   Cell Struct Funct 17 (1), 77-86 (1992)
   PUBMED   1586970
REFERENCE   8  (residues 1 to 646)
  AUTHORS   DeLuca-Flaherty,C., McKay,D.B., Parham,P. and Hill,B.L.
  TITLE     Uncoating protein (hsc70) binds a conformationally labile domain of
            clathrin light chain LCa to stimulate ATP hydrolysis
  JOURNAL   Cell 62 (5), 875-887 (1990)
   PUBMED   1975516
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Lim,M.Y., Davis,N., Zhang,J.Y. and Bose,H.R. Jr.
  TITLE     The v-rel oncogene product is complexed with cellular proteins
            including its proto-oncogene product and heat shock protein 70
  JOURNAL   Virology 175 (1), 149-160 (1990)
   PUBMED   2155506
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Chiang,H.L., Terlecky,S.R., Plant,C.P. and Dice,J.F.
  TITLE     A role for a 70-kilodalton heat shock protein in lysosomal
            degradation of intracellular proteins
  JOURNAL   Science 246 (4928), 382-385 (1989)
   PUBMED   2799391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC395565.1, BC019816.2,
            AK222628.1 and AP000926.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the heat shock protein 70
            family, which contains both heat-inducible and constitutively
            expressed members. This protein belongs to the latter group, which
            are also referred to as heat-shock cognate proteins. It functions
            as a chaperone, and binds to nascent polypeptides to facilitate
            correct folding. It also functions as an ATPase in the disassembly
            of clathrin-coated vesicles during transport of membrane components
            through the cell. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1011269.1,
                                           SRR3476690.494591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000534624.6/ ENSP00000432083.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..646
                     /product="heat shock cognate 71 kDa protein isoform 1"
                     /EC_number="3.6.4.10"
                     /note="heat shock 70kd protein 10; constitutive heat shock
                     protein 70; lipopolysaccharide-associated protein 1;
                     LPS-associated protein 1; heat shock cognate protein 54;
                     heat shock cognate 71 kDa protein; N-myristoyltransferase
                     inhibitor protein 71; epididymis luminal protein 33;
                     epididymis secretory sperm binding protein Li 72p; heat
                     shock 70kDa protein 8; heat shock protein family A member
                     8"
                     /calculated_mol_wt=70767
     Region          1..613
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          2..386
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000305|PubMed:27474739"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330; propagated
                     from UniProtKB/Swiss-Prot (P11142.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Region          186..377
                     /region_name="Interaction with BAG1"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            246
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            328
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Region          394..509
                     /region_name="Substrate-binding domain (SBD).
                     /evidence=ECO:0000305|PubMed:27474739"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            469
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            512
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            524
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            561
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL21A, alternate.
                     /evidence=ECO:0000269|PubMed:23349634,
                     ECO:0000269|PubMed:23921388; N6,N6-dimethyllysine,
                     alternate. /evidence=ECO:0007744|PubMed:24129315;
                     propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            589
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            597
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            601
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Region          614..646
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     CDS             1..646
                     /gene="HSPA8"
                     /gene_synonym="HEL-33; HEL-S-72p; HSC54; HSC70; HSC71;
                     HSP71; HSP73; HSPA10; LAP-1; LAP1; NIP71"
                     /coded_by="NM_006597.6:79..2019"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8440.1"
                     /db_xref="GeneID:3312"
                     /db_xref="HGNC:HGNC:5241"
                     /db_xref="MIM:600816"
ORIGIN      
        1 mskgpavgid lgttyscvgv fqhgkveiia ndqgnrttps yvaftdterl igdaaknqva
       61 mnptntvfda krligrrfdd avvqsdmkhw pfmvvndagr pkvqveykge tksfypeevs
      121 smvltkmkei aeaylgktvt navvtvpayf ndsqrqatkd agtiaglnvl riineptaaa
      181 iaygldkkvg aernvlifdl gggtfdvsil tiedgifevk stagdthlgg edfdnrmvnh
      241 fiaefkrkhk kdisenkrav rrlrtacera krtlssstqa sieidslyeg idfytsitra
      301 rfeelnadlf rgtldpveka lrdakldksq ihdivlvggs tripkiqkll qdffngkeln
      361 ksinpdeava ygaavqaail sgdksenvqd lllldvtpls lgietaggvm tvlikrntti
      421 ptkqtqtftt ysdnqpgvli qvyegeramt kdnnllgkfe ltgippaprg vpqievtfdi
      481 dangilnvsa vdkstgkenk ititndkgrl skediermvq eaekykaede kqrdkvsskn
      541 slesyafnmk atvedeklqg kindedkqki ldkcneiinw ldknqtaeke efehqqkele
      601 kvcnpiitkl yqsaggmpgg mpggfpggga ppsggassgp tieevd
//
LOCUS       NP_001138437             854 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4-like isoform 2 [Homo sapiens].
ACCESSION   NP_001138437
VERSION     NP_001138437.1
DBSOURCE    REFSEQ: accession NM_001144965.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Chen,G., Pei,Y., Ye,Q., Xie,Z., Gyawali,L. and Liang,X.
  TITLE     NEDD4L-mediated RASGRP2 suppresses high-glucose and oxLDL-induced
            vascular endothelial cell dysfunctions by activating Rap1 and R-Ras
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119844 (2024)
   PUBMED   39260747
  REMARK    GeneRIF: NEDD4L-mediated RASGRP2 suppresses high-glucose and
            oxLDL-induced vascular endothelial cell dysfunctions by activating
            Rap1 and R-Ras.
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Wang,R., Wang,R., Zhou,S., Liu,T., Dang,J., Chen,Q., Chen,J. and
            Wang,Z.
  TITLE     Ubiquitination of angiotensin-converting enzyme 2 contributes to
            the development of pulmonary arterial hypertension mediated by
            neural precursor cell-expressed developmentally down-regulated gene
            4-Like
  JOURNAL   Respir Res 25 (1), 326 (2024)
   PUBMED   39210401
  REMARK    GeneRIF: Ubiquitination of angiotensin-converting enzyme 2
            contributes to the development of pulmonary arterial hypertension
            mediated by neural precursor cell-expressed developmentally
            down-regulated gene 4-Like.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Yang,B. and Kumar,S.
  TITLE     Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with
            distinct physiological functions
  JOURNAL   Cell Death Differ 17 (1), 68-77 (2010)
   PUBMED   19557014
  REMARK    Review article
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Russo,C.J., Melista,E., Cui,J., DeStefano,A.L., Bakris,G.L.,
            Manolis,A.J., Gavras,H. and Baldwin,C.T.
  TITLE     Association of NEDD4L ubiquitin ligase with essential hypertension
  JOURNAL   Hypertension 46 (3), 488-491 (2005)
   PUBMED   16103266
  REMARK    GeneRIF: Significant association between several SNPs and
            hypertension in US whites, Greek whites, and African-Americans.
            Genetic variation in NEDD4L may play role in development or
            progression of some forms of hypertension.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Qi,H., Grenier,J., Fournier,A. and Labrie,C.
  TITLE     Androgens differentially regulate the expression of NEDD4L
            transcripts in LNCaP human prostate cancer cells
  JOURNAL   Mol Cell Endocrinol 210 (1-2), 51-62 (2003)
   PUBMED   14615060
  REMARK    GeneRIF: Results describe the isolation of three new NEDD4L
            transcripts designated NEDD4Lf, NEDD4Lg and NEDD4Lh, which encode
            different forms of the NEDD4L protein.
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Itani,O.A., Campbell,J.R., Herrero,J., Snyder,P.M. and Thomas,C.P.
  TITLE     Alternate promoters and variable splicing lead to hNedd4-2 isoforms
            with a C2 domain and varying number of WW domains
  JOURNAL   Am J Physiol Renal Physiol 285 (5), F916-F929 (2003)
   PUBMED   12876068
  REMARK    GeneRIF: Alternate transcripts of Nedd4-2 may interact with ENaC
            differently. hNedd4-2 has role in regulation of ENaC. Protein
            domains are important for Nedd4-2 function.
            GeneRIF: Identification of multiple splice forms and 5' variants of
            Nedd4l.  5' variants inhibit ENaC-mediated Na+ transport when
            reconstituted in FRT epithelia.  Other splice forms encode Nedd4L
            isoforms with 2 to 4 WW domains having varying affinity for ENaC.
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Chen,H., Ross,C.A., Wang,N., Huo,Y., MacKinnon,D.F., Potash,J.B.,
            Simpson,S.G., McMahon,F.J., DePaulo,J.R. Jr. and McInnis,M.G.
  TITLE     NEDD4L on human chromosome 18q21 has multiple forms of transcripts
            and is a homologue of the mouse Nedd4-2 gene
  JOURNAL   Eur J Hum Genet 9 (12), 922-930 (2001)
   PUBMED   11840194
  REMARK    GeneRIF: Candidate gene for autosomal dominant orthostatic
            hypotensive disorder.
REFERENCE   9  (residues 1 to 854)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   10 (residues 1 to 854)
  AUTHORS   Nuber,U., Schwarz,S., Kaiser,P., Schneider,R. and Scheffner,M.
  TITLE     Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7
            (E2-F1) and characterization of their interaction with E6-AP and
            RSP5
  JOURNAL   J Biol Chem 271 (5), 2795-2800 (1996)
   PUBMED   8576257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107896.7, AY112983.1,
            BC032597.2 and AC090236.4.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein mediates the ubiquitination of
            multiple target substrates and plays a critical role in epithelial
            sodium transport by regulating the cell surface expression of the
            epithelial sodium channel, ENaC. Single nucleotide polymorphisms in
            this gene may be associated with essential hypertension.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Mar
            2012].
            
            Transcript Variant: This variant (f) uses an alternate first exon,
            compared to variant j, which results in the use of a downstream
            in-frame start codon. The encoded protein (isoform 2) has a shorter
            N-terminus that lacks a C2 domain, compared to isoform 1. Variants
            a, b, and f encode the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY112983.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..854
                     /product="E3 ubiquitin-protein ligase NEDD4-like isoform
                     2"
                     /EC_number="2.3.2.26"
                     /EC_number="2.3.2.36"
                     /note="ubiquitin-protein ligase Rsp5; HECT-type E3
                     ubiquitin transferase NED4L; neural precursor cell
                     expressed, developmentally down-regulated 4-like, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=98051
     Region          <1..32
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Region          77..103
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          <198..381
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          266..295
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          379..409
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(393,404)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          428..460
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(444,455)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(503,534,545,607,780,815..816,819..823,843,850)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          521..850
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(635,638..639,641..642,645,650,652,656..657,659,664,
                     669,686,690)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..854
                     /gene="NEDD4L"
                     /gene_synonym="hNEDD4-2; NEDD4-2; NEDD4.2; PVNH7; RSP5"
                     /coded_by="NM_001144965.2:566..3130"
                     /note="isoform 2 is encoded by transcript variant f"
                     /db_xref="CCDS:CCDS45875.1"
                     /db_xref="GeneID:23327"
                     /db_xref="HGNC:HGNC:7728"
                     /db_xref="MIM:606384"
ORIGIN      
        1 merpytfkdf llrprshksr vkgflrlkma ympknggqde ensdqrddme hgwevvdsnd
       61 sasqhqeelp ppplppgwee kvdnlgrtyy vnhnnrttqw hrpslmdvss esdnnirqin
      121 qeaahrrfrs rrhisedlep epseggdvpe pwetiseevn iagdslglal ppppaspgsr
      181 tspqelseel srrlqitpds ngeqfssliq repssrlrsc svtdavaeqg hlpppsapag
      241 rarsstvtgg eeptpsvayv httpglpsgw eerkdakgrt yyvnhnnrtt twtrpimqla
      301 edgasgsatn snnhliepqi rrprslsspt vtlsaplega kdspvrravk dtlsnpqspq
      361 pspynspkpq hkvtqsflpp gwemriapng rpffidhntk tttwedprlk fpvhmrskts
      421 lnpndlgplp pgweerihld grtfyidhns kitqwedprl qnpaitgpav pysrefkqky
      481 dyfrkklkkp adipnrfemk lhrnnifees yrrimsvkrp dvlkarlwie fesekgldyg
      541 gvarewffll skemfnpyyg lfeysatdny tlqinpnsgl cnedhlsyft figrvaglav
      601 fhgklldgff irpfykmmlg kqitlndmes vdseyynslk wilendptel dlmfcideen
      661 fgqtyqvdlk pngseimvtn enkreyidlv iqwrfvnrvq kqmnaflegf tellpidlik
      721 ifdenelell mcglgdvdvn dwrqhsiykn gycpnhpviq wfwkavllmd aekrirllqf
      781 vtgtsrvpmn gfaelygsng pqlftieqwg speklpraht cfnrldlppy etfedlrekl
      841 lmavenaqgf egvd
//
LOCUS       NP_001138416             172 aa            linear   PRI 20-NOV-2025
DEFINITION  myosin regulatory light chain 12B [Homo sapiens].
ACCESSION   NP_001138416
VERSION     NP_001138416.1
DBSOURCE    REFSEQ: accession NM_001144944.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Kiyomitsu,T. and Cheeseman,I.M.
  TITLE     Cortical dynein and asymmetric membrane elongation coordinately
            position the spindle in anaphase
  JOURNAL   Cell 154 (2), 391-402 (2013)
   PUBMED   23870127
  REMARK    Erratum:[Cell. 2013 Sep 12;154(6):1401]
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Umeda,D., Tachibana,H. and Yamada,K.
  TITLE     Epigallocatechin-3-O-gallate disrupts stress fibers and the
            contractile ring by reducing myosin regulatory light chain
            phosphorylation mediated through the target molecule 67 kDa laminin
            receptor
  JOURNAL   Biochem Biophys Res Commun 333 (2), 628-635 (2005)
   PUBMED   15946647
  REMARK    GeneRIF: These results suggest that EGCG inhibits the cell growth
            by reducing the MRLC phosphorylation and this effect is mediated by
            the 67LR.
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Li,T.B., Liu,X.H., Feng,S., Hu,Y., Yang,W.X., Han,Y., Wang,Y.G. and
            Gong,L.M.
  TITLE     Characterization of MR-1, a novel myofibrillogenesis regulator in
            human muscle
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 36 (6), 412-418 (2004)
   PUBMED   15188056
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Webb,R.C.
  TITLE     Smooth muscle contraction and relaxation
  JOURNAL   Adv Physiol Educ 27 (1-4), 201-206 (2003)
   PUBMED   14627618
  REMARK    Review article
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Iwasaki,T., Murata-Hori,M., Ishitobi,S. and Hosoya,H.
  TITLE     Diphosphorylated MRLC is required for organization of stress fibers
            in interphase cells and the contractile ring in dividing cells
  JOURNAL   Cell Struct Funct 26 (6), 677-683 (2001)
   PUBMED   11942626
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Olsson,P.A., Korhonen,L., Mercer,E.A. and Lindholm,D.
  TITLE     MIR is a novel ERM-like protein that interacts with myosin
            regulatory light chain and inhibits neurite outgrowth
  JOURNAL   J Biol Chem 274 (51), 36288-36292 (1999)
   PUBMED   10593918
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG696903.1 and CA307094.1.
            
            Summary: The activity of nonmuscle myosin II (see MYH9; MIM 160775)
            is regulated by phosphorylation of a regulatory light chain, such
            as MRLC2. This phosphorylation results in higher MgATPase activity
            and the assembly of myosin II filaments (Iwasaki et al., 2001
            [PubMed 11942626]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-3 all encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG696903.1, SRR7346977.517958.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.31"
     Protein         1..172
                     /product="myosin regulatory light chain 12B"
                     /note="myosin regulatory light chain 2; myosin regulatory
                     light chain MRLC2; MLC-2; MLC20; MLC-2A; SHUJUN-1; myosin
                     regulatory light chain 20 kDa; myosin, light chain 12B,
                     regulatory"
                     /calculated_mol_wt=19648
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14950.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MLCK and ZIPK/DAPK3.
                     /evidence=ECO:0000269|PubMed:11942626,
                     ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:15946647;
                     propagated from UniProtKB/Swiss-Prot (O14950.2)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MLCK and ZIPK/DAPK3.
                     /evidence=ECO:0000269|PubMed:11942626,
                     ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:15946647;
                     propagated from UniProtKB/Swiss-Prot (O14950.2)"
     Region          25..163
                     /region_name="PTZ00184"
                     /note="calmodulin; Provisional"
                     /db_xref="CDD:185504"
     CDS             1..172
                     /gene="MYL12B"
                     /gene_synonym="MLC-B; MRLC2"
                     /coded_by="NM_001144944.1:160..678"
                     /db_xref="CCDS:CCDS11831.1"
                     /db_xref="GeneID:103910"
                     /db_xref="HGNC:HGNC:29827"
                     /db_xref="MIM:609211"
ORIGIN      
        1 msskkaktkt tkkrpqrats nvfamfdqsq iqefkeafnm idqnrdgfid kedlhdmlas
       61 lgknptdayl dammneapgp inftmfltmf geklngtdpe dvirnafacf deeatgtiqe
      121 dylrellttm gdrftdeevd elyreapidk kgnfnyieft rilkhgakdk dd
//
LOCUS       NP_001354597             799 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ee [Homo sapiens].
ACCESSION   NP_001354597
VERSION     NP_001354597.1
DBSOURCE    REFSEQ: accession NM_001367668.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 799)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 799)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 799)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 799)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 799)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 799)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 799)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 799)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 799)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2151741 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..799
                     /product="SUN domain-containing protein 1 isoform ee"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=88339
     Region          12..306
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <379..>603
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          431..484
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(431,434..435,438,441..442,445..446,448..449,
                     452..453,455..456,459..460,462..463,466,469..470,473,
                     476..477,480..481,483..484)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          561..619
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          662..797
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..799
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367668.1:105..2504"
                     /note="isoform ee is encoded by transcript variant 31"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv
      181 revlredghl svngealcdd ckgkrhldah taahsqsprl pgragtlwhi wacagyfllq
      241 ilrrigavgq avsrtawsal wlavvapgka asgvfwwlgi gwyqfvtlis wlnvflltrc
      301 lrnickflvl liplflllgl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl
      361 kqplqgdsea fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag
      421 psasvrdavg qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa
      481 vgeqllptve hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq
      541 ggsleqllqr fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag
      601 asgiteaqar aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi
      661 plwyfsqspr vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni
      721 ssapkdfavy gleneyqeeg qllgqftydq dgeslqmfqa lkrpddtafq ivelrifsnw
      781 ghpeytclyr frvhgepvk
//
LOCUS       NP_690048                341 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase PDIK1L [Homo sapiens].
ACCESSION   NP_690048
VERSION     NP_690048.1
DBSOURCE    REFSEQ: accession NM_152835.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Polyanskaya,S.A., Moreno,R.Y., Lu,B., Feng,R., Yao,Y., Irani,S.,
            Klingbeil,O., Yang,Z., Wei,Y., Demerdash,O.E., Benjamin,L.A.,
            Weiss,M.J., Zhang,Y.J. and Vakoc,C.R.
  TITLE     SCP4-STK35/PDIK1L complex is a dual phospho-catalytic signaling
            dependency in acute myeloid leukemia
  JOURNAL   Cell Rep 38 (2), 110233 (2022)
   PUBMED   35021089
  REMARK    GeneRIF: SCP4-STK35/PDIK1L complex is a dual phospho-catalytic
            signaling dependency in acute myeloid leukemia.
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Taipale,M., Krykbaeva,I., Koeva,M., Kayatekin,C., Westover,K.D.,
            Karras,G.I. and Lindquist,S.
  TITLE     Quantitative analysis of HSP90-client interactions reveals
            principles of substrate recognition
  JOURNAL   Cell 150 (5), 987-1001 (2012)
   PUBMED   22939624
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Goyal,P., Behring,A., Kumar,A. and Siess,W.
  TITLE     Identifying and characterizing a novel protein kinase STK35L1 and
            deciphering its orthologs and close-homologs in vertebrates
  JOURNAL   PLoS One 4 (9), e6981 (2009)
   PUBMED   19756140
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Rual,J.F., Hirozane-Kishikawa,T., Hao,T., Bertin,N., Li,S.,
            Dricot,A., Li,N., Rosenberg,J., Lamesch,P., Vidalain,P.O.,
            Clingingsmith,T.R., Hartley,J.L., Esposito,D., Cheo,D., Moore,T.,
            Simmons,B., Sequerra,R., Bosak,S., Doucette-Stamm,L., Le Peuch,C.,
            Vandenhaute,J., Cusick,M.E., Albala,J.S., Hill,D.E. and Vidal,M.
  TITLE     Human ORFeome version 1.1: a platform for reverse proteomics
  JOURNAL   Genome Res 14 (10B), 2128-2135 (2004)
   PUBMED   15489335
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Guo,L., Ji,C., Gu,S., Ying,K., Cheng,H., Ni,X., Liu,J., Xie,Y. and
            Mao,Y.
  TITLE     Molecular cloning and characterization of a novel human kinase
            gene, PDIK1L
  JOURNAL   J Genet 82 (1-2), 27-32 (2003)
   PUBMED   14631099
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK312872.1, AL834290.1, BU742621.1 and AL391650.18.
            
            Transcript Variant: This variant (1) represents the shortest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.36699.1,
                                           SRR1660805.156441.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374269.2/ ENSP00000363387.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..341
                     /product="serine/threonine-protein kinase PDIK1L"
                     /EC_number="2.7.11.1"
                     /note="casein kinase"
                     /calculated_mol_wt=38415
     Region          7..331
                     /region_name="STKc_PDIK1L"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     PDLIM1 interacting kinase 1 like; cd13977"
                     /db_xref="CDD:270879"
     Site            order(14..18,22,35,37,68,119..122,126,128,164,166,
                     168..169,171,190,193,220..223)
                     /site_type="active"
                     /db_xref="CDD:270879"
     Site            order(14..18,22,35,37,68,119..122,126,164,166,168..169,
                     171,190)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270879"
     Site            order(18,126,128,164,166,168,193,220..223)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270879"
     Site            order(189..201,209..223)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270879"
     CDS             1..341
                     /gene="PDIK1L"
                     /gene_synonym="CLIK1L; STK35L2"
                     /coded_by="NM_152835.5:110..1135"
                     /db_xref="CCDS:CCDS274.1"
                     /db_xref="GeneID:149420"
                     /db_xref="HGNC:HGNC:18981"
                     /db_xref="MIM:610785"
ORIGIN      
        1 mvssqpkydl irevgrgsyg vvyeavirkt sarvavkkir chapenvela lrefwalssi
       61 ksqhpnvihl eecilqkdgm vqkmshgsns slylqlvets lkgeiafdpr sayylwfvmd
      121 fcdggdmney llsrkpnrkt ntsfmlqlss alaflhknqi ihrdlkpdni lisqtrldts
      181 dleptlkvad fglskvcsas gqnpeepvsv nkcflstacg tdfymapevw eghytakadi
      241 falgiiiwam leritfidte tkkellgsyv kqgteivpvg eallenpkme llipvkkksm
      301 ngrmkqlike mlaanpqdrp dafelelrlv qiafkdsswe t
//
LOCUS       NP_998787                424 aa            linear   PRI 20-NOV-2025
DEFINITION  STAM-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_998787
VERSION     NP_998787.1
DBSOURCE    REFSEQ: accession NM_213622.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Zhang,W., Xu,Z., Du,Y., Liu,T., Xiong,Z., Hu,J., Chen,L., Peng,X.
            and Zhou,F.
  TITLE     Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment
  JOURNAL   Cell Death Dis 15 (9), 657 (2024)
   PUBMED   39242557
  REMARK    GeneRIF: Identification of STAM-binding protein as a target for the
            treatment of gemcitabine resistance pancreatic cancer in a
            nutrient-poor microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Li,L., Yang,X., He,M., Xu,X., Xuan,X., Zhang,J., Zhang,L., Xu,H.
            and Li,D.
  TITLE     The expression and clinical significance of STAMBP in breast cancer
  JOURNAL   Mol Biol Rep 50 (1), 899-906 (2023)
   PUBMED   36309616
  REMARK    GeneRIF: The expression and clinical significance of STAMBP in
            breast cancer.
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Yang,Q., Yan,D., Zou,C., Xue,Q., Lin,S., Huang,Q., Li,X., Tang,D.,
            Chen,X. and Liu,J.
  TITLE     The deubiquitinating enzyme STAMBP is a newly discovered driver of
            triple-negative breast cancer progression that maintains RAI14
            protein stability
  JOURNAL   Exp Mol Med 54 (11), 2047-2059 (2022)
   PUBMED   36434041
  REMARK    GeneRIF: The deubiquitinating enzyme STAMBP is a newly discovered
            driver of triple-negative breast cancer progression that maintains
            RAI14 protein stability.
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Yu,S., E,C. and Yang,J.
  TITLE     STAM binding protein regulated by hsa_circ_0007334 exerts oncogenic
            potential in pancreatic cancer
  JOURNAL   Pancreatology 22 (7), 1003-1012 (2022)
   PUBMED   36089485
  REMARK    GeneRIF: STAM binding protein regulated by hsa_circ_0007334 exerts
            oncogenic potential in pancreatic cancer.
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Itoh,F., Asao,H., Sugamura,K., Heldin,C.H., ten Dijke,P. and
            Itoh,S.
  TITLE     Promoting bone morphogenetic protein signaling through negative
            regulation of inhibitory Smads
  JOURNAL   EMBO J 20 (15), 4132-4142 (2001)
   PUBMED   11483516
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Endo,K., Takeshita,T., Kasai,H., Sasaki,Y., Tanaka,N., Asao,H.,
            Kikuchi,K., Yamada,M., Chenb,M., O'Shea,J.J. and Sugamura,K.
  TITLE     STAM2, a new member of the STAM family, binding to the Janus
            kinases
  JOURNAL   FEBS Lett 477 (1-2), 55-61 (2000)
   PUBMED   10899310
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Tanaka,N., Kaneko,K., Asao,H., Kasai,H., Endo,Y., Fujita,T.,
            Takeshita,T. and Sugamura,K.
  TITLE     Possible involvement of a novel STAM-associated molecule 'AMSH' in
            intracellular signal transduction mediated by cytokines
  JOURNAL   J Biol Chem 274 (27), 19129-19135 (1999)
   PUBMED   10383417
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Asada,H., Ishii,N., Sasaki,Y., Endo,K., Kasai,H., Tanaka,N.,
            Takeshita,T., Tsuchiya,S., Konno,T. and Sugamura,K.
  TITLE     Grf40, A novel Grb2 family member, is involved in T cell signaling
            through interaction with SLP-76 and LAT
  JOURNAL   J Exp Med 189 (9), 1383-1390 (1999)
   PUBMED   10224278
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Carter,M.T., Mirzaa,G., McDonell,L.M. and Boycott,K.M.
  TITLE     Microcephaly-Capillary Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354023
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC073046.7, CX758449.1 and
            BC065574.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Cytokine-mediated signal transduction in the JAK-STAT
            cascade requires the involvement of adaptor molecules. One such
            signal-transducing adaptor molecule contains an SH3 domain that is
            required for induction of MYC and cell growth. The protein encoded
            by this gene binds to the SH3 domain of the signal-transducing
            adaptor molecule, and plays a critical role in cytokine-mediated
            signaling for MYC induction and cell cycle progression. Multiple
            alternatively spliced transcript variants encoding the same protein
            isoform have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.71487.1,
                                           SRR1803613.39904.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394070.7/ ENSP00000377633.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..424
                     /product="STAM-binding protein isoform 1"
                     /EC_number="3.1.2.15"
                     /note="associated molecule with the SH3 domain of STAM;
                     endosome-associated ubiquitin isopeptidase; testicular
                     secretory protein Li 54"
                     /calculated_mol_wt=47946
     Region          1..127
                     /region_name="Interaction with CHMP3.
                     /evidence=ECO:0000269|PubMed:17146056"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          13..117
                     /region_name="USP8_dimer"
                     /note="USP8 dimerization domain; pfam08969"
                     /db_xref="CDD:462647"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          227..231
                     /region_name="Interaction with STAM.
                     /evidence=ECO:0000269|PubMed:10383417"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11483516,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Region          254..424
                     /region_name="MPN_AMSH_like"
                     /note="Mov34/MPN/PAD-1 family; cd08066"
                     /db_xref="CDD:163697"
     Site            order(280,335,337,345,348)
                     /site_type="active"
                     /note="MPN+ (JAMM) motif [active]"
                     /db_xref="CDD:163697"
     Site            280
                     /site_type="other"
                     /note="Indirect zinc-binding.
                     /evidence=ECO:0000250|UniProtKB:Q96FJ0; propagated from
                     UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(282..284,309..313,316..317,320,323,329..330,333,335,
                     337,345,347..348,350..351,354..355,357..358,395)
                     /site_type="other"
                     /note="Distal ubiquitin recognition interface [polypeptide
                     binding]"
                     /db_xref="CDD:163697"
     Site            order(309,337,340..341,343,345..346,395..397)
                     /site_type="active"
                     /note="Proximal ubiquitin recognition interface [active]"
                     /db_xref="CDD:163697"
     Region          335..348
                     /region_name="JAMM motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01182"
                     /note="propagated from UniProtKB/Swiss-Prot (O95630.1)"
     Site            order(335,337,348)
                     /site_type="other"
                     /note="Zinc-binding site [ion binding]"
                     /db_xref="CDD:163697"
     CDS             1..424
                     /gene="STAMBP"
                     /gene_synonym="AMSH; MICCAP"
                     /coded_by="NM_213622.4:563..1837"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1929.1"
                     /db_xref="GeneID:10617"
                     /db_xref="HGNC:HGNC:16950"
                     /db_xref="MIM:606247"
ORIGIN      
        1 msdhgdvslp pedrvralsq lgsavevned ipprryfrsg veiirmasiy seegniehaf
       61 ilynkyitlf ieklpkhrdy ksavipekkd tvkklkeiaf pkaeelkael lkrytkeyte
      121 yneekkkeae elarnmaiqq elekekqrva qqkqqqleqe qfhafeemir nqelekerlk
      181 ivqefgkvdp glggplvpdl ekpsldvfpt ltvssiqpsd chttvrpakp pvvdrslkpg
      241 alsnsesipt idglrhvvvp grlcpqflql asantargve tcgilcgklm rneftithvl
      301 ipkqsagsdy cnteneeelf liqdqqglit lgwihthptq taflssvdlh thcsyqmmlp
      361 esvaivcspk fqetgffklt dhgleeissc rqkgfhphsk dpplfcscsh vtvvdravti
      421 tdlr
//
LOCUS       NP_006311                223 aa            linear   PRI 20-NOV-2025
DEFINITION  membrane-associated progesterone receptor component 2 [Homo
            sapiens].
ACCESSION   NP_006311
VERSION     NP_006311.3
DBSOURCE    REFSEQ: accession NM_006320.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Lintao,R.C.V., Richardson,L.S., Kammala,A.K., Chapa,J.,
            Yunque-Yap,D.A., Khanipov,K., Golovko,G., Dalmacio,L.M.M. and
            Menon,R.
  TITLE     PGRMC2 and HLA-G regulate immune homeostasis in a
            microphysiological model of human maternal-fetal membrane interface
  JOURNAL   Commun Biol 7 (1), 1041 (2024)
   PUBMED   39179795
  REMARK    GeneRIF: PGRMC2 and HLA-G regulate immune homeostasis in a
            microphysiological model of human maternal-fetal membrane
            interface.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Medina-Laver,Y., Gonzalez-Martin,R., de Castro,P.,
            Diaz-Hernandez,I., Alama,P., Quinonero,A., Palomar,A. and
            Dominguez,F.
  TITLE     Deciphering the role of PGRMC2 in the human endometrium during the
            menstrual cycle and in vitro decidualization using an in vitro
            approach
  JOURNAL   Hum Reprod 39 (5), 1042-1056 (2024)
   PUBMED   38452349
  REMARK    GeneRIF: Deciphering the role of PGRMC2 in the human endometrium
            during the menstrual cycle and in vitro decidualization using an in
            vitro approach.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Yokouchi-Konishi,T., Liu,Y. and Feng,L.
  TITLE     Progesterone receptor membrane component 2 is critical for human
            placental extravillous trophoblast invasion
  JOURNAL   Biol Reprod 109 (5), 759-771 (2023)
   PUBMED   37665239
  REMARK    GeneRIF: Progesterone receptor membrane component 2 is critical for
            human placental extravillous trophoblast invasion.
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Velazquez Hernandez,D.M., Vazquez-Martinez,E.R. and
            Camacho-Arroyo,I.
  TITLE     The role of progesterone receptor membrane component (PGRMC) in the
            endometrium
  JOURNAL   Steroids 184, 109040 (2022)
   PUBMED   35526781
  REMARK    GeneRIF: The role of progesterone receptor membrane component
            (PGRMC) in the endometrium.
            Review article
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Menon,R., Pearce,B., Velez,D.R., Merialdi,M., Williams,S.M.,
            Fortunato,S.J. and Thorsen,P.
  TITLE     Racial disparity in pathophysiologic pathways of preterm birth
            based on genetic variants
  JOURNAL   Reprod Biol Endocrinol 7, 62 (2009)
   PUBMED   19527514
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Velez,D.R., Fortunato,S., Thorsen,P., Lombardi,S.J., Williams,S.M.
            and Menon,R.
  TITLE     Spontaneous preterm birth in African Americans is associated with
            infection and inflammatory response gene variants
  JOURNAL   Am J Obstet Gynecol 200 (2), 209 (2009)
   PUBMED   19019335
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Velez,D.R., Fortunato,S.J., Thorsen,P., Lombardi,S.J.,
            Williams,S.M. and Menon,R.
  TITLE     Preterm birth in Caucasians is associated with coagulation and
            inflammation pathway gene variants
  JOURNAL   PLoS One 3 (9), e3283 (2008)
   PUBMED   18818748
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Losel,R., Breiter,S., Seyfert,M., Wehling,M. and Falkenstein,E.
  TITLE     Classic and non-classic progesterone receptors are both expressed
            in human spermatozoa
  JOURNAL   Horm Metab Res 37 (1), 10-14 (2005)
   PUBMED   15702432
  REMARK    GeneRIF: The expression of a novel progesterone-binding protein
            (hmPR1/PGMRC1) was investigated. Transcripts of this protein have
            been detected in human sperm.
REFERENCE   10 (residues 1 to 223)
  AUTHORS   Gerdes,D., Wehling,M., Leube,B. and Falkenstein,E.
  TITLE     Cloning and tissue expression of two putative steroid membrane
            receptors
  JOURNAL   Biol Chem 379 (7), 907-911 (1998)
   PUBMED   9705155
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK131272.1, AK091741.1 and AI375856.1.
            
            On Nov 29, 2018 this sequence version replaced NP_006311.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.349017.1,
                                           SRR11853562.25335.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296425.10/ ENSP00000296425.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.2"
     Protein         1..223
                     /product="membrane-associated progesterone receptor
                     component 2"
                     /note="progesterone membrane binding protein; steroid
                     receptor protein DG6"
                     /calculated_mol_wt=23687
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15173.1)"
     Site            15
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:37453717; propagated from
                     UniProtKB/Swiss-Prot (O15173.1)"
     Site            42..66
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15173.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O15173.1)"
     Region          104..167
                     /region_name="Cyt-b5"
                     /note="Cytochrome b5-like Heme/Steroid binding domain;
                     pfam00173"
                     /db_xref="CDD:459698"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15173.1)"
     Region          202..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15173.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15173.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15173.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O15173.1)"
     CDS             1..223
                     /gene="PGRMC2"
                     /gene_synonym="DG6; PMBP"
                     /coded_by="NM_006320.6:24..695"
                     /db_xref="CCDS:CCDS3739.3"
                     /db_xref="GeneID:10424"
                     /db_xref="HGNC:HGNC:16089"
                     /db_xref="MIM:607735"
ORIGIN      
        1 maagdgdvkl gtlgsgsess ndggsespgd agaaaegggw aaaalalltg ggemllnval
       61 valvllgayr lwvrwgrrgl gagagagees patslprmkk rdfsleqlrq ydgsrnpril
      121 lavngkvfdv tkgskfygpa gpygifagrd asrglatfcl dkdalrdeyd dlsdlnavqm
      181 esvrewemqf kekydyvgrl lkpgeepsey tdeedtkdhn kqd
//
LOCUS       NP_001353547             467 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of G-protein signaling 14 isoform 3 [Homo sapiens].
ACCESSION   NP_001353547 XP_005265852
VERSION     NP_001353547.1
DBSOURCE    REFSEQ: accession NM_001366618.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Wang,J., Guo,Y., He,Y., Qin,Y., Li,X., Yang,L., Liu,K. and Xiao,L.
  TITLE     Hepatic regulator of G protein signaling 14 ameliorates NAFLD
            through activating cAMP-AMPK signaling by targeting Gialpha1/3
  JOURNAL   Mol Metab 80, 101882 (2024)
   PUBMED   38237897
  REMARK    GeneRIF: Hepatic regulator of G protein signaling 14 ameliorates
            NAFLD through activating cAMP-AMPK signaling by targeting
            Gialpha1/3.
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Montanez-Miranda,C., Bramlett,S.N. and Hepler,J.R.
  TITLE     RGS14 expression in CA2 hippocampus, amygdala, and basal ganglia:
            Implications for human brain physiology and disease
  JOURNAL   Hippocampus 33 (3), 166-181 (2023)
   PUBMED   36541898
  REMARK    GeneRIF: RGS14 expression in CA2 hippocampus, amygdala, and basal
            ganglia: Implications for human brain physiology and disease.
            Review article
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Kimple,R.J., De Vries,L., Tronchere,H., Behe,C.I., Morris,R.A.,
            Gist Farquhar,M. and Siderovski,D.P.
  TITLE     RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
            guanine nucleotide dissociation inhibitor Activity
  JOURNAL   J Biol Chem 276 (31), 29275-29281 (2001)
   PUBMED   11387333
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Cho,H., Kozasa,T., Takekoshi,K., De Gunzburg,J. and Kehrl,J.H.
  TITLE     RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha-
            and G13alpha-mediated signaling pathways
  JOURNAL   Mol Pharmacol 58 (3), 569-576 (2000)
   PUBMED   10953050
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Traver,S., Bidot,C., Spassky,N., Baltauss,T., De Tand,M.F.,
            Thomas,J.L., Zalc,B., Janoueix-Lerosey,I. and Gunzburg,J.D.
  TITLE     RGS14 is a novel Rap effector that preferentially regulates the
            GTPase activity of galphao
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 19-29 (2000)
   PUBMED   10926822
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC146507.2.
            
            On Oct 13, 2018 this sequence version replaced XP_005265852.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains one RGS domain, two
            Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The
            protein attenuates the signaling activity of G-proteins by binding,
            through its GoLoco domain, to specific types of activated,
            GTP-bound G alpha subunits. Acting as a GTPase activating protein
            (GAP), the protein increases the rate of conversion of the GTP to
            GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.154317.1,
                                           SRR1803616.211548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..467
                     /product="regulator of G-protein signaling 14 isoform 3"
                     /calculated_mol_wt=51117
     Region          19..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          58..186
                     /region_name="RGS_RGS14"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS14 protein; cd08743"
                     /db_xref="CDD:188697"
     Site            order(88..90,92..93,130..135,137..138,165,167..169,173)
                     /site_type="other"
                     /note="putative G-alpha-3 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:188697"
     Region          192..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97492; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          302..372
                     /region_name="RBD1_RGS14"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 14 (RGS14); cd17137"
                     /db_xref="CDD:340657"
     Site            order(334,352)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340657"
     Region          373..444
                     /region_name="RBD2_RGS14"
                     /note="Ras-binding domain (RBD) 2 of regulator of G
                     protein signaling 14 (RGS14); cd17139"
                     /db_xref="CDD:340659"
     Site            order(385,407)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340659"
     CDS             1..467
                     /gene="RGS14"
                     /coded_by="NM_001366618.1:102..1505"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10636"
                     /db_xref="HGNC:HGNC:9996"
                     /db_xref="MIM:602513"
ORIGIN      
        1 mpgkpkhlgv pngrmvlavs dgelssttgp qgqgegrgss lsihslpsgp sspfpteeqp
       61 vaswalsfer llqdplglay fteflkkefs aenvtfwkac erfqqipasd tqqlaqearn
      121 iyqeflssqa lspvnidrqa wlgeevlaep rpdmfraqql qifnlmkfds yarfvksply
      181 recllaeaeg rplrepgssr lgspdatrkk pklkpgkslp lgveelgqlp pvegpggrpl
      241 rksfrrelgg tanaalrres qgslnssasl dlgflafvss kseshrkslg stegesesrp
      301 gkyccvylpd gtaslalarp gltirdmlag icekrglslp dikvylvgne qkalvldqdc
      361 tvladqevrl enritfelel talervvris akptkrlqea lqpilekhgl splevvlhrp
      421 gekqpldlgk lvssvaaqrl vldtlpgvki skardkspcr sqawwsc
//
LOCUS       NP_938017                198 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 17 [Homo sapiens].
ACCESSION   NP_938017 XP_117267
VERSION     NP_938017.2
DBSOURCE    REFSEQ: accession NM_198276.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Wang,S., Zhou,Q., Yan,S., Liu,C., Li,F., Feng,D. and He,M.
  TITLE     TMEM17 Promotes Tumor Progression in Glioblastoma by Activating the
            PI3K/AKT Pathway
  JOURNAL   Front Biosci (Landmark Ed) 29 (8), 285 (2024)
   PUBMED   39206901
  REMARK    GeneRIF: TMEM17 Promotes Tumor Progression in Glioblastoma by
            Activating the PI3K/AKT Pathway.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Zhang,X., Zhang,Y., Miao,Y., Zhou,H., Jiang,G. and Wang,E.
  TITLE     TMEM17 depresses invasion and metastasis in lung cancer cells via
            ERK signaling pathway
  JOURNAL   Oncotarget 8 (41), 70685-70694 (2017)
   PUBMED   29050311
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Li,C., Jensen,V.L., Park,K., Kennedy,J., Garcia-Gonzalo,F.R.,
            Romani,M., De Mori,R., Bruel,A.L., Gaillard,D., Doray,B., Lopez,E.,
            Riviere,J.B., Faivre,L., Thauvin-Robinet,C., Reiter,J.F.,
            Blacque,O.E., Valente,E.M. and Leroux,M.R.
  TITLE     MKS5 and CEP290 Dependent Assembly Pathway of the Ciliary
            Transition Zone
  JOURNAL   PLoS Biol 14 (3), e1002416 (2016)
   PUBMED   26982032
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Kenny,E.E., Pe'er,I., Karban,A., Ozelius,L., Mitchell,A.A.,
            Ng,S.M., Erazo,M., Ostrer,H., Abraham,C., Abreu,M.T., Atzmon,G.,
            Barzilai,N., Brant,S.R., Bressman,S., Burns,E.R., Chowers,Y.,
            Clark,L.N., Darvasi,A., Doheny,D., Duerr,R.H., Eliakim,R.,
            Giladi,N., Gregersen,P.K., Hakonarson,H., Jones,M.R., Marder,K.,
            McGovern,D.P., Mulle,J., Orr-Urtreger,A., Proctor,D.D., Pulver,A.,
            Rotter,J.I., Silverberg,M.S., Ullman,T., Warren,S.T., Waterman,M.,
            Zhang,W., Bergman,A., Mayer,L., Katz,S., Desnick,R.J., Cho,J.H. and
            Peter,I.
  TITLE     A genome-wide scan of Ashkenazi Jewish Crohn's disease suggests
            novel susceptibility loci
  JOURNAL   PLoS Genet 8 (3), e1002559 (2012)
   PUBMED   22412388
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR760587.1, BC047439.1 and AC093159.3.
            
            On Dec 13, 2008 this sequence version replaced NP_938017.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1113291.1,
                                           SRR5189667.224371.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267775 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335390.6/ ENSP00000335094.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..198
                     /product="transmembrane protein 17"
                     /calculated_mol_wt=22915
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86X19.2)"
     Region          45..151
                     /region_name="Transmemb_17"
                     /note="Predicted membrane protein; pfam09799"
                     /db_xref="CDD:462907"
     Site            45..65
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            110..130
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X19.2)"
     CDS             1..198
                     /gene="TMEM17"
                     /coded_by="NM_198276.3:67..663"
                     /db_xref="CCDS:CCDS1871.1"
                     /db_xref="GeneID:200728"
                     /db_xref="HGNC:HGNC:26623"
                     /db_xref="MIM:614950"
ORIGIN      
        1 melpdpvrqr lgnfsravfs dsnrtgpesn egpenemvss lalqmslyfn tyyfplwwvs
       61 simmlhmkys ilpdyykfiv itviilitli eairlylgyv gnlqekvpel agfwllslll
      121 qlplilfllf negltnlple kaihiiftlf lafqvvaafl tlrkmvnqla vrfhlqdfdr
      181 lsanrgdmrr mrscieei
//
LOCUS       NP_062817                985 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E transporter isoform a
            [Homo sapiens].
ACCESSION   NP_062817
VERSION     NP_062817.2
DBSOURCE    REFSEQ: accession NM_019843.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 985)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 985)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 985)
  AUTHORS   Ding,Y., Chen,S., Jin,J., Sun,Y., Chu,C., Kee,K., Xin,M. and Li,L.
  TITLE     POI-associated EIF4ENIF1 mutations exhibit impaired translation
            regulation abilities
  JOURNAL   Gene 917, 148456 (2024)
   PUBMED   38604507
  REMARK    GeneRIF: POI-associated EIF4ENIF1 mutations exhibit impaired
            translation regulation abilities.
REFERENCE   4  (residues 1 to 985)
  AUTHORS   Zuberek,J., Warzecha,M., Dobrowolski,M. and Modrak-Wojcik,A.
  TITLE     An intramolecular disulphide bond in human 4E-T affects its binding
            to eIF4E1a protein
  JOURNAL   Eur Biophys J 52 (6-7), 497-510 (2023)
   PUBMED   37798395
  REMARK    GeneRIF: An intramolecular disulphide bond in human 4E-T affects
            its binding to eIF4E1a protein.
REFERENCE   5  (residues 1 to 985)
  AUTHORS   Shang,L., Ren,S., Yang,X., Zhang,F., Jin,L., Zhang,X. and Wu,Y.
  TITLE     EIF4ENIF1 variants in two patients with non-syndromic premature
            ovarian insufficiency
  JOURNAL   Eur J Med Genet 65 (10), 104597 (2022)
   PUBMED   36030004
  REMARK    GeneRIF: EIF4ENIF1 variants in two patients with non-syndromic
            premature ovarian insufficiency.
REFERENCE   6  (residues 1 to 985)
  AUTHORS   Andrei,M.A., Ingelfinger,D., Heintzmann,R., Achsel,T.,
            Rivera-Pomar,R. and Luhrmann,R.
  TITLE     A role for eIF4E and eIF4E-transporter in targeting mRNPs to
            mammalian processing bodies
  JOURNAL   RNA 11 (5), 717-727 (2005)
   PUBMED   15840819
  REMARK    GeneRIF: human P bodies contain the cap-binding protein eIF4E and
            the related factor eIF4E-transporter (eIF4E-T), suggesting novel
            roles for these proteins in targeting mRNAs for 5' --> 3'
            degradation
REFERENCE   7  (residues 1 to 985)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 985)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 985)
  AUTHORS   Warner,D.R., Roberts,E.A., Greene,R.M. and Pisano,M.M.
  TITLE     Identification of novel Smad binding proteins
  JOURNAL   Biochem Biophys Res Commun 312 (4), 1185-1190 (2003)
   PUBMED   14651998
REFERENCE   10 (residues 1 to 985)
  AUTHORS   Dostie,J., Ferraiuolo,M., Pause,A., Adam,S.A. and Sonenberg,N.
  TITLE     A novel shuttling protein, 4E-T, mediates the nuclear import of the
            mRNA 5' cap-binding protein, eIF4E
  JOURNAL   EMBO J 19 (12), 3142-3156 (2000)
   PUBMED   10856257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314636.1 and BC032941.1.
            
            On Aug 29, 2009 this sequence version replaced NP_062817.1.
            
            Summary: The protein encoded by this gene is a nucleocytoplasmic
            shuttle protein for the translation initiation factor eIF4E. This
            shuttle protein interacts with the importin alpha-beta complex to
            mediate nuclear import of eIF4E. It is predominantly cytoplasmic;
            its own nuclear import is regulated by a nuclear localization
            signal and nuclear export signals. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            both encode isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.156767.1,
                                           SRR1660805.188778.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330125.10/ ENSP00000328103.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..985
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..985
                     /product="eukaryotic translation initiation factor 4E
                     transporter isoform a"
                     /note="2610509L04Rik; eukaryotic translation initiation
                     factor 4E transporter; eIF4E transporter; 4E-transporter"
                     /calculated_mol_wt=108070
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          30..711
                     /region_name="EIF4E-T"
                     /note="Nucleocytoplasmic shuttling protein for mRNA
                     cap-binding EIF4E; pfam10477"
                     /db_xref="CDD:371079"
     Region          30..36
                     /region_name="YXXXXLphi motif.
                     /evidence=ECO:0000269|PubMed:10856257,
                     ECO:0000269|PubMed:24335285"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          131..161
                     /region_name="Interaction with CSDE1.
                     /evidence=ECO:0000269|PubMed:27342281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          195..211
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          208..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          219..240
                     /region_name="Interaction with DDX6.
                     /evidence=ECO:0000269|PubMed:27342281"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          438..447
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          448..490
                     /region_name="Interaction with LSM14A.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          613..638
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000305|PubMed:10856257"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          664..693
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          695..713
                     /region_name="Interaction with PATL1.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          707..803
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          748..>935
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22966201; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          922..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Region          940..985
                     /region_name="Interaction with LSM14A.
                     /evidence=ECO:0000269|PubMed:26027925"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     Site            951
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NRA8.2)"
     CDS             1..985
                     /gene="EIF4ENIF1"
                     /gene_synonym="4E-T; Clast4"
                     /coded_by="NM_019843.4:177..3134"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13898.1"
                     /db_xref="GeneID:56478"
                     /db_xref="HGNC:HGNC:16687"
                     /db_xref="MIM:607445"
ORIGIN      
        1 mdrrsmgete sgdafldlkk ppaskcphry tkeelldike lphskqrpsc lsekydsdgv
       61 wdpekwhasl ypasgrsspv eslkkeldtd rpslvrrivd prervkeddl dvvlspqrrs
      121 fgggchvtaa vssrrsgspl ekdsdglrll ggrrigsgri isartfekdh rlsdkdlrdl
      181 rdrdrerdfk dkrfrrefgd skrvfgerrr ndsyteeepe wfsagptsqs etieltgfdd
      241 kileedhkgr krtrrrtasv kegivecngg vaeedevevi laqepaadqe vprdavlpeq
      301 spgdfdfnef fnldkvpcla smiedvlgeg svsasrfsrw fsnpsrsgsr ssslgstphe
      361 elerlagleq ailspgqnsg nyfapipled haenkvdile mlqkakvdlk pllsslsank
      421 eklkesshsg vvlsveevea glkglkvdqq vknstpfmae hleetlsavt nnrqlkkdgd
      481 mtafnklvst mkasgtlpsq pkvsrnlesh lmspaeipgq pvpknilqel lgqpvqrpas
      541 snllsglmgs lepttsllgq rapspplsqv fqtraasady lrpripspig ftpgpqqllg
      601 dpfqgmrkpm spitaqmsql elqqaalegl alphdlavqa anfyqpgfgk pqvdrtrdgf
      661 rnrqqrvtks papvhrgnss spapaasits mlspsftpts virkmyeske kskeepasgk
      721 aalgdskedt qkaseenlls sssvpsadrd sspttnskls alqrsscstp lsqanrytke
      781 qdyrpkatgr ktptlaspvp ttpflrpvhq vplvphvpmv rpahqlhpgl vqrmlaqgvh
      841 pqhlpsllqt gvlppgmdls hlqgisgpil gqpfyplpaa shpllnprpg tplhlamvqq
      901 qlqrsvlhpp gsgshaaavs vqttpqnvps rsglphmhsq lehrpsqrss spvglakwfg
      961 sdvlqqplps mpakvisvde leyrq
//
LOCUS       NP_932079                466 aa            linear   PRI 20-NOV-2025
DEFINITION  butyrophilin-like protein 3 precursor [Homo sapiens].
ACCESSION   NP_932079
VERSION     NP_932079.1
DBSOURCE    REFSEQ: accession NM_197975.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Kim,J.W., Rim,D., Ann,C.H. and Lee,S.H.
  TITLE     Frameshift mutations of immunomodulatory BTN2A1, BTN2A2, and BTNL3
            genes in colon cancers
  JOURNAL   Pathol Res Pract 249, 154769 (2023)
   PUBMED   37634314
  REMARK    GeneRIF: Frameshift mutations of immunomodulatory BTN2A1, BTN2A2,
            and BTNL3 genes in colon cancers.
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Bobyn,A., Zarrei,M., Zhu,Y., Hoffman,M., Brenner,D., Resnick,A.C.,
            Scherer,S.W. and Gallo,M.
  TITLE     Ancestry and frequency of genetic variants in the general
            population are confounders in the characterization of germline
            variants linked to cancer
  JOURNAL   BMC Med Genet 21 (1), 92 (2020)
   PUBMED   32375678
  REMARK    GeneRIF: analysis of genomic information from multiple non-cancer
            cohorts showed that both the NEGR1 promoter deletion and the
            BTNL3-8 deletion were CNVs occurring at high frequencies in the
            general population. Intriguingly, the upstream NEGR1 CNV deletion
            was homozygous in ~ 40% of individuals in the non-cancer
            population.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Vantourout,P., Laing,A., Woodward,M.J., Zlatareva,I., Apolonia,L.,
            Jones,A.W., Snijders,A.P., Malim,M.H. and Hayday,A.C.
  TITLE     Heteromeric interactions regulate butyrophilin (BTN) and BTN-like
            molecules governing gammadelta T cell biology
  JOURNAL   Proc Natl Acad Sci U S A 115 (5), 1039-1044 (2018)
   PUBMED   29339503
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Di Marco Barros,R., Roberts,N.A., Dart,R.J., Vantourout,P.,
            Jandke,A., Nussbaumer,O., Deban,L., Cipolat,S., Hart,R.,
            Iannitto,M.L., Laing,A., Spencer-Dene,B., East,P., Gibbons,D.,
            Irving,P.M., Pereira,P., Steinhoff,U. and Hayday,A.
  TITLE     Epithelia Use Butyrophilin-like Molecules to Shape Organ-Specific
            gammadelta T Cell Compartments
  JOURNAL   Cell 167 (1), 203-218 (2016)
   PUBMED   27641500
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Shibui,A., Tsunoda,T., Seki,N., Suzuki,Y., Sugano,S. and Sugane,K.
  TITLE     Cloning, expression analysis, and chromosomal localization of a
            novel butyrophilin-like receptor
  JOURNAL   J Hum Genet 44 (4), 249-252 (1999)
   PUBMED   10429365
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA431389.1, AK025267.1 and AY358385.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358385.1, AK025267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342868.7/ ENSP00000341787.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..466
                     /product="butyrophilin-like protein 3 precursor"
                     /note="butyrophilin-like receptor; butyrophilin-like
                     protein 3"
                     /calculated_mol_wt=50367
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1901
     mat_peptide     18..466
                     /product="Butyrophilin-like protein 3. /id=PRO_0000014540"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXE8.2)"
                     /calculated_mol_wt=50367
     Region          19..132
                     /region_name="IgV_MOG_like"
                     /note="Immunoglobulin (Ig)-like domain of myelin
                     oligodendrocyte glycoprotein (MOG); cd05713"
                     /db_xref="CDD:409378"
     Region          19..42
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409378"
     Region          20..24
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409378"
     Region          27..31
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409378"
     Region          34..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409378"
     Region          43..51
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409378"
     Site            order(49..50,69,80,117..118,120..121,123..124)
                     /site_type="other"
                     /note="Fab binding site [polypeptide binding]"
                     /db_xref="CDD:409378"
     Region          51..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409378"
     Region          52..56
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          57..75
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          61..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          77..117
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          84..89
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409378"
     Region          95..103
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409378"
     Region          118..120
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          120..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409378"
     Region          121..132
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409378"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXE8.2)"
     Region          289..461
                     /region_name="SPRY_PRY_C-I_1"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10,
                     TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38,
                     TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72,
                     NF7 and bloodthirsty; cd13733"
                     /db_xref="CDD:293968"
     CDS             1..466
                     /gene="BTNL3"
                     /gene_synonym="BTN9.1; BTNLR"
                     /coded_by="NM_197975.3:184..1584"
                     /db_xref="CCDS:CCDS47358.1"
                     /db_xref="GeneID:10917"
                     /db_xref="HGNC:HGNC:1143"
                     /db_xref="MIM:606192"
ORIGIN      
        1 mafvlilvls fyelvsgqwq vtgpgkfvqa lvgedavfsc slfpetsaea mevrffrnqf
       61 havvhlyrdg edweskqmpq yrgrtefvkd siaggrvslr lknitpsdig lygcwfssqi
      121 ydeeatwelr vaalgslpli sivgyvdggi qllclssgwf pqptakwkgp qgqdlssdsr
      181 anadgyslyd veisiivqen agsilcsihl aeqshevesk vligetffqp spwrlasill
      241 gllcgalcgv vmgmiivffk skgkiqaeld wrrkhgqael rdarkhavev tldpetahpk
      301 lcvsdlktvt hrkapqevph sekrftrksv vasqgfqagk hywevdvgqn vgwyvgvcrd
      361 dvdrgknnvt lspnngywvl rlttehlyft fnphfislpp stpptrvgvf ldyeggtisf
      421 fntndqsliy tlltcqfegl lrpyiqhamy deekgtpifi cpvswg
//
LOCUS       NP_620411                390 aa            linear   PRI 20-NOV-2025
DEFINITION  endothelial cell-selective adhesion molecule precursor [Homo
            sapiens].
ACCESSION   NP_620411
VERSION     NP_620411.2
DBSOURCE    REFSEQ: accession NM_138961.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Lecca,M., Pehlivan,D., Suner,D.H., Weiss,K., Coste,T., Zweier,M.,
            Oktay,Y., Danial-Farran,N., Rosti,V., Bonasoni,M.P., Malara,A.,
            Contro,G., Zuntini,R., Pollazzon,M., Pascarella,R., Neri,A.,
            Fusco,C., Marafi,D., Mitani,T., Posey,J.E., Bayramoglu,S.E.,
            Gezdirici,A., Hernandez-Rodriguez,J., Cladera,E.A., Miravet,E.,
            Roldan-Busto,J., Ruiz,M.A., Bauza,C.V., Ben-Sira,L., Sigaudy,S.,
            Begemann,A., Unger,S., Gungor,S., Hiz,S., Sonmezler,E., Zehavi,Y.,
            Jerdev,M., Balduini,A., Zuffardi,O., Horvath,R., Lochmuller,H.,
            Rauch,A., Garavelli,L., Tournier-Lasserve,E., Spiegel,R.,
            Lupski,J.R. and Errichiello,E.
  TITLE     Bi-allelic variants in the ESAM tight-junction gene cause a
            neurodevelopmental disorder associated with fetal intracranial
            hemorrhage
  JOURNAL   Am J Hum Genet 110 (4), 681-690 (2023)
   PUBMED   36996813
  REMARK    GeneRIF: Bi-allelic variants in the ESAM tight-junction gene cause
            a neurodevelopmental disorder associated with fetal intracranial
            hemorrhage.
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Ishibashi,T., Yokota,T., Tanaka,H., Ichii,M., Sudo,T., Satoh,Y.,
            Doi,Y., Ueda,T., Tanimura,A., Hamanaka,Y., Ezoe,S., Shibayama,H.,
            Oritani,K. and Kanakura,Y.
  TITLE     ESAM is a novel human hematopoietic stem cell marker associated
            with a subset of human leukemias
  JOURNAL   Exp Hematol 44 (4), 269-81 (2016)
   PUBMED   26774386
  REMARK    GeneRIF: ESAM is a novel human hematopoietic stem cell marker
            associated with a subset of human leukemias
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Nasdala,I., Wolburg-Buchholz,K., Wolburg,H., Kuhn,A., Ebnet,K.,
            Brachtendorf,G., Samulowitz,U., Kuster,B., Engelhardt,B.,
            Vestweber,D. and Butz,S.
  TITLE     A transmembrane tight junction protein selectively expressed on
            endothelial cells and platelets
  JOURNAL   J Biol Chem 277 (18), 16294-16303 (2002)
   PUBMED   11847224
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Sim,D.L., Yeo,W.M. and Chow,V.T.
  TITLE     The novel human HUEL (C4orf1) protein shares homology with the
            DNA-binding domain of the XPA DNA repair protein and displays
            nuclear translocation in a cell cycle-dependent manner
  JOURNAL   Int J Biochem Cell Biol 34 (5), 487-504 (2002)
   PUBMED   11906820
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Hirata,Ki., Ishida,T., Penta,K., Rezaee,M., Yang,E., Wohlgemuth,J.
            and Quertermous,T.
  TITLE     Cloning of an immunoglobulin family adhesion molecule selectively
            expressed by endothelial cells
  JOURNAL   J Biol Chem 276 (19), 16223-16231 (2001)
   PUBMED   11279107
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK075396.1 and AP000866.4.
            
            On Jun 7, 2007 this sequence version replaced NP_620411.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075396.1, SRR3476690.660945.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278927.10/ ENSP00000278927.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..390
                     /product="endothelial cell-selective adhesion molecule
                     precursor"
                     /note="2310008D05Rik; HUEL (C4orf1)-interacting protein;
                     endothelial cell-selective adhesion molecule; LP4791
                     protein"
                     /calculated_mol_wt=38129
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3066
     mat_peptide     30..390
                     /product="Endothelial cell-selective adhesion molecule.
                     /id=PRO_0000014752"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP7.1)"
                     /calculated_mol_wt=38129
     Region          40..150
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Region          154..158
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          166..241
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Region          194..198
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Region          221..226
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Region          316..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925F2; propagated from
                     UniProtKB/Swiss-Prot (Q96AP7.1)"
     CDS             1..390
                     /gene="ESAM"
                     /gene_synonym="NEDIHSS; W117m"
                     /coded_by="NM_138961.3:137..1309"
                     /db_xref="CCDS:CCDS8453.1"
                     /db_xref="GeneID:90952"
                     /db_xref="HGNC:HGNC:17474"
                     /db_xref="MIM:614281"
ORIGIN      
        1 mislpgplvt nllrflflgl salappsraq lqlhlpanrl qaveggevvl pawytlhgev
       61 sssqpwevpf vmwffkqkek edqvlsying vttskpgvsl vysmpsrnls lrleglqekd
      121 sgpyscsvnv qdkqgksrgh siktlelnvl vppappscrl qgvphvganv tlscqsprsk
      181 pavqyqwdrq lpsfqtffap aldvirgsls ltnlsssmag vyvckahnev gtaqcnvtle
      241 vstgpgaavv agavvgtlvg lgllaglvll yhrrgkalee pandikedai aprtlpwpks
      301 sdtiskngtl ssvtsaralr pphgpprpga ltptpslssq alpsprlptt dgahpqpisp
      361 ipggvsssgl srmgavpvmv paqsqagslv
//
LOCUS       NP_001280126             231 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CHIP isoform b [Homo sapiens].
ACCESSION   NP_001280126
VERSION     NP_001280126.1
DBSOURCE    REFSEQ: accession NM_001293197.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Cao,Y., Chen,F., Zhu,S., Zhu,D. and Qi,H.
  TITLE     Staphylococcus aureus infection initiates hypoxia-mediated STIP1
            homology and U-box containing protein 1 upregulation to trigger
            osteomyelitis
  JOURNAL   Toxicon 248, 108049 (2024)
   PUBMED   39059559
  REMARK    GeneRIF: Staphylococcus aureus infection initiates hypoxia-mediated
            STIP1 homology and U-box containing protein 1 upregulation to
            trigger osteomyelitis.
REFERENCE   3  (residues 1 to 231)
  AUTHORS   van Prooije,T.H., Pennings,M., Dorresteijn,L., Gardeitchik,T.,
            Odekerken,V.J.J., Oosterloo,M., Pedersen,A.,
            Verschuuren-Bemelmans,C.C., Vrancken,A., Kamsteeg,E.J. and van de
            Warrenburg,B.P.C.
  TITLE     A New Case Series Suggests That SCA48 (ATX/STUB1) Is Primarily a
            Monogenic Disorder
  JOURNAL   Mov Disord 39 (9), 1636-1640 (2024)
   PUBMED   38973070
  REMARK    GeneRIF: A New Case Series Suggests That SCA48 (ATX/STUB1) Is
            Primarily a Monogenic Disorder.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Baviera-Munoz,R., Carretero-Vilarroig,L., Pedro-Ibor,A., Jaijo,T.,
            Del Valle-Carranza,A., Martinez-Torres,I., Millan,J.M., Bataller,L.
            and Aller,E.
  TITLE     STUB1 Mutations as Possible Genetic Modifiers in Spinocerebellar
            Ataxia Type 8
  JOURNAL   Mov Disord 39 (9), 1641-1644 (2024)
   PUBMED   38962894
  REMARK    GeneRIF: STUB1 Mutations as Possible Genetic Modifiers in
            Spinocerebellar Ataxia Type 8.
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Tieliwaerdi,A., Aini,A., Amuti,M., Aierken,Y., Nijiati,M. and
            Luo,B.
  TITLE     STUB1 promotes the degradation of HSPB1 and induces ferroptosis in
            lung cancer cells
  JOURNAL   Environ Toxicol 39 (8), 4156-4170 (2024)
   PUBMED   38661247
  REMARK    GeneRIF: STUB1 promotes the degradation of HSPB1 and induces
            ferroptosis in lung cancer cells.
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Murata,S., Minami,Y., Minami,M., Chiba,T. and Tanaka,K.
  TITLE     CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded
            protein
  JOURNAL   EMBO Rep 2 (12), 1133-1138 (2001)
   PUBMED   11743028
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Jiang,J., Ballinger,C.A., Wu,Y., Dai,Q., Cyr,D.M., Hohfeld,J. and
            Patterson,C.
  TITLE     CHIP is a U-box-dependent E3 ubiquitin ligase: identification of
            Hsc70 as a target for ubiquitylation
  JOURNAL   J Biol Chem 276 (46), 42938-42944 (2001)
   PUBMED   11557750
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Connell,P., Ballinger,C.A., Jiang,J., Wu,Y., Thompson,L.J.,
            Hohfeld,J. and Patterson,C.
  TITLE     The co-chaperone CHIP regulates protein triage decisions mediated
            by heat-shock proteins
  JOURNAL   Nat Cell Biol 3 (1), 93-96 (2001)
   PUBMED   11146632
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Ballinger,C.A., Connell,P., Wu,Y., Hu,Z., Thompson,L.J., Yin,L.Y.
            and Patterson,C.
  TITLE     Identification of CHIP, a novel tetratricopeptide repeat-containing
            protein that interacts with heat shock proteins and negatively
            regulates chaperone functions
  JOURNAL   Mol Cell Biol 19 (6), 4535-4545 (1999)
   PUBMED   10330192
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Scanlan,M.J., Chen,Y.T., Williamson,B., Gure,A.O., Stockert,E.,
            Gordan,J.D., Tureci,O., Sahin,U., Pfreundschuh,M. and Old,L.J.
  TITLE     Characterization of human colon cancer antigens recognized by
            autologous antibodies
  JOURNAL   Int J Cancer 76 (5), 652-658 (1998)
   PUBMED   9610721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF217968.1, BC017178.1 and
            Z92544.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeat and a U-box that functions as a ubiquitin
            ligase/cochaperone. The encoded protein binds to and ubiquitinates
            shock cognate 71 kDa protein (Hspa8) and DNA polymerase beta
            (Polb), among other targets. Mutations in this gene cause
            spinocerebellar ataxia, autosomal recessive 16. Alternative
            splicing results in multiple transcript variants. There is a
            pseudogene for this gene on chromosome 2. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' region and initiates translation at a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (b) has a
            shorter N-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF217968.1, SRR1163658.29046.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..231
                     /product="E3 ubiquitin-protein ligase CHIP isoform b"
                     /EC_number="2.3.2.27"
                     /note="serologically defined colon cancer antigen 7; heat
                     shock protein A binding protein 2 (c-terminal); antigen
                     NY-CO-7; CLL-associated antigen KW-8; E3 ubiquitin-protein
                     ligase CHIP; carboxy terminus of Hsp70-interacting
                     protein; STIP1 homology and U-box containing protein 1, E3
                     ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase CHIP"
                     /calculated_mol_wt=26936
     Region          <1..>81
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          21..51
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          70..153
                     /region_name="CHIP_TPR_N"
                     /note="CHIP N-terminal tetratricopeptide repeat domain;
                     pfam18391"
                     /db_xref="CDD:436460"
     Region          155..225
                     /region_name="RING-Ubox_CHIP"
                     /note="U-box domain, a modified RING finger, found in
                     carboxyl terminus of HSP70-interacting protein (CHIP) and
                     similar proteins; cd16654"
                     /db_xref="CDD:438316"
     Site            order(155,157..158,162..163,165,174..175,177,179,187..188,
                     191..192,197..198,200,209..214,216..217,220)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438316"
     CDS             1..231
                     /gene="STUB1"
                     /gene_synonym="CHIP; HSPABP2; NY-CO-7; SCA48; SCAR16;
                     SDCCAG7; UBOX1"
                     /coded_by="NM_001293197.2:422..1117"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76797.1"
                     /db_xref="GeneID:10273"
                     /db_xref="HGNC:HGNC:11427"
                     /db_xref="MIM:607207"
ORIGIN      
        1 mqqheqalad crraleldgq svkahfflgq cqlemesyde aianlqrays lakeqrlnfg
       61 ddipsalria kkkrwnsiee rrihqeselh sylsrliaae rereleecqr nhegdeddsh
      121 vraqqaciea khdkymadmd elfsqvdekr kkrdipdylc gkisfelmre pcitpsgity
      181 drkdieehlq rvghfdpvtr spltqeqlip nlamkevida fisengwved y
//
LOCUS       NP_940820                887 aa            linear   PRI 20-NOV-2025
DEFINITION  protein PTHB1 isoform 2 [Homo sapiens].
ACCESSION   NP_940820
VERSION     NP_940820.1
DBSOURCE    REFSEQ: accession NM_198428.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL704922.1, BC103831.2,
            U85994.1 and AC078833.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.130830.1,
                                           SRR1803613.3201.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000242067.11/ ENSP00000242067.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..887
                     /product="protein PTHB1 isoform 2"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=99150
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..819
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          685..765
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          850..887
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..887
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_198428.3:490..3153"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43566.1"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptdrnpdgip rviqckfrlp lkliclpgqp
      541 sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf hflggaritv lasktsqryr
      601 iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi plqeyfelid hhfelringe
      661 kleellsera vqfraiqrrl larfkdktpa plqhldtlld gtykqviala daveenqgnl
      721 fqsftrlksa thlvillial wqklsadqva ileaaflplq edtqelgwee tvdaaishll
      781 ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls kggrlclstd aaapqtmvmp
      841 ggcttipesd leersveqds telftnhrhl taetprpevs plqgvse
//
LOCUS       NP_001193762             494 aa            linear   PRI 20-NOV-2025
DEFINITION  histone acetyltransferase KAT5 isoform 4 [Homo sapiens].
ACCESSION   NP_001193762
VERSION     NP_001193762.1
DBSOURCE    REFSEQ: accession NM_001206833.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Wang,Y., Li,M., Chen,Y., Jiang,Y., Zhang,Z., Yan,Z., Liu,X. and
            Wu,C.
  TITLE     SPIN1 facilitates chemoresistance and HR repair by promoting Tip60
            binding to H3K9me3
  JOURNAL   EMBO Rep 25 (9), 3970-3989 (2024)
   PUBMED   39090319
  REMARK    GeneRIF: SPIN1 facilitates chemoresistance and HR repair by
            promoting Tip60 binding to H3K9me3.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Sun,M., Yang,B., Xin,G., Wang,Y., Luo,J., Jiang,Q. and Zhang,C.
  TITLE     TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation
  JOURNAL   Sci China Life Sci 67 (9), 1957-1969 (2024)
   PUBMED   38763998
  REMARK    GeneRIF: TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation.
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Chen,H., Li,Y., Li,H., Chen,X., Fu,H., Mao,D., Chen,W., Lan,L.,
            Wang,C., Hu,K., Li,J., Zhu,C., Evans,I., Cheung,E., Lu,D., He,Y.,
            Behrens,A., Yin,D. and Zhang,C.
  TITLE     NBS1 lactylation is required for efficient DNA repair and
            chemotherapy resistance
  JOURNAL   Nature 631 (8021), 663-669 (2024)
   PUBMED   38961290
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Xuan,F., Xuan,H., Huang,M., He,W., Xu,H., Shi,X. and Wen,H.
  TITLE     The Tudor-knot Domain of KAT5 Regulates Nucleosomal Substrate
            Acetylation
  JOURNAL   J Mol Biol 436 (7), 168414 (2024)
   PUBMED   38141874
  REMARK    GeneRIF: The Tudor-knot Domain of KAT5 Regulates Nucleosomal
            Substrate Acetylation.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Brady,M.E., Ozanne,D.M., Gaughan,L., Waite,I., Cook,S., Neal,D.E.
            and Robson,C.N.
  TITLE     Tip60 is a nuclear hormone receptor coactivator
  JOURNAL   J Biol Chem 274 (25), 17599-17604 (1999)
   PUBMED   10364196
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Dechend,R., Hirano,F., Lehmann,K., Heissmeyer,V., Ansieau,S.,
            Wulczyn,F.G., Scheidereit,C. and Leutz,A.
  TITLE     The Bcl-3 oncoprotein acts as a bridging factor between
            NF-kappaB/Rel and nuclear co-regulators
  JOURNAL   Oncogene 18 (22), 3316-3323 (1999)
   PUBMED   10362352
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Kimura,A. and Horikoshi,M.
  TITLE     Tip60 acetylates six lysines of a specific class in core histones
            in vitro
  JOURNAL   Genes Cells 3 (12), 789-800 (1998)
   PUBMED   10096020
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Yamamoto,T. and Horikoshi,M.
  TITLE     Novel substrate specificity of the histone acetyltransferase
            activity of HIV-1-Tat interactive protein Tip60
  JOURNAL   J Biol Chem 272 (49), 30595-30598 (1997)
   PUBMED   9388189
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Kamine,J., Elangovan,B., Subramanian,T., Coleman,D. and
            Chinnadurai,G.
  TITLE     Identification of a cellular protein that specifically interacts
            with the essential cysteine region of the HIV-1 Tat transactivator
  JOURNAL   Virology 216 (2), 357-366 (1996)
   PUBMED   8607265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304664.1, BC013211.1 and
            BU737532.1.
            
            Summary: The protein encoded by this gene belongs to the MYST
            family of histone acetyl transferases (HATs) and was originally
            isolated as an HIV-1 TAT-interactive protein. HATs play important
            roles in regulating chromatin remodeling, transcription and other
            nuclear processes by acetylating histone and nonhistone proteins.
            This protein is a histone acetylase that has a role in DNA repair
            and apoptosis and is thought to play an important role in signal
            transduction. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The resulting
            protein (isoform 4) is shorter when it is compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.509510.1,
                                           SRR1803614.244957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..494
                     /product="histone acetyltransferase KAT5 isoform 4"
                     /EC_number="2.3.1.48"
                     /note="cPLA2 interacting protein; HIV-1 Tat interactive
                     protein, 60kDa; K-acetyltransferase 5; Tat interacting
                     protein, 60kDa; histone acetyltransferase KAT5;
                     cPLA(2)-interacting protein; 60 kDa Tat-interactive
                     protein; histone acetyltransferase HTATIP; K(lysine)
                     acetyltransferase 5; protein acetyltransferase KAT5;
                     protein crotonyltransferase KAT5; protein
                     2-hydroxyisobutyryltransferase KAT5; protein
                     lactyltransferase KAT5"
                     /calculated_mol_wt=56162
     Region          40..98
                     /region_name="Tudor-knot"
                     /note="RNA binding activity-knot of a chromodomain;
                     pfam11717"
                     /db_xref="CDD:432022"
     Site            order(55,61..63,78,80..83,87,89..92,94..95,102,105..106)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350845"
     Site            order(55,80,83,87)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350845"
     Region          76..485
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            order(77,79..84,86..90)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     Site            order(77,80,84,86,90)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     CDS             1..494
                     /gene="KAT5"
                     /gene_synonym="cPLA2; ESA1; HTATIP; HTATIP1; NEDFASB;
                     PLIP; TIP; TIP60; ZC2HC5"
                     /coded_by="NM_001206833.2:17..1501"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55771.1"
                     /db_xref="GeneID:10524"
                     /db_xref="HGNC:HGNC:5275"
                     /db_xref="MIM:601409"
ORIGIN      
        1 maevvspvpg agrrepgevg rargppvadp gvalspqgei iegcrlpvlr rnqdnedewp
       61 laeilsvkdi sgrklfyvhy idfnkrldew vtherldlkk iqfpkkeakt ptknglpgsr
      121 pgsperevkr kvevvspatp vpsetapasv fpqngaarra vaaqpgrkrk snclgtdeds
      181 qdssdgipsa prmtgslvsd rshddivtrm kniecielgr hrlkpwyfsp ypqelttlpv
      241 lylcefclky grslkclqrh ltkcdlrhpp gneiyrkgti sffeidgrkn ksysqnlcll
      301 akcfldhktl yydtdpflfy vmteydckgf hivgyfskek estedynvac iltlppyqrr
      361 gygklliefs yelskvegkt gtpekplsdl gllsyrsyws qtileilmgl ksesgerpqi
      421 tineiseits ikkedvistl qylnlinyyk gqyiltlsed ivdgheraml krllridskc
      481 lhftpkdwsk rgkw
//
LOCUS       NP_004413                736 aa            linear   PRI 20-NOV-2025
DEFINITION  segment polarity protein dishevelled homolog DVL-2 [Homo sapiens].
ACCESSION   NP_004413
VERSION     NP_004413.1
DBSOURCE    REFSEQ: accession NM_004422.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Omble,A., Mahajan,S., Bhoite,A. and Kulkarni,K.
  TITLE     Dishevelled2 activates WGEF via its interaction with a unique
            internal peptide motif of the GEF
  JOURNAL   Commun Biol 7 (1), 543 (2024)
   PUBMED   38714795
  REMARK    GeneRIF: Dishevelled2 activates WGEF via its interaction with a
            unique internal peptide motif of the GEF.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   He,R., Chen,Y., Qian,C., Hu,Y., Huang,X. and Tao,R.
  TITLE     Dishevelled segment polarity protein 2 promotes gastric cancer
            progression through Wnt/beta-catenin pathway
  JOURNAL   Tissue Cell 82, 102119 (2023)
   PUBMED   37257286
  REMARK    GeneRIF: Dishevelled segment polarity protein 2 promotes gastric
            cancer progression through Wnt/beta-catenin pathway.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Demirci,U., Orenay-Boyacioglu,S., Kasap,E., Gerceker,E., Bilgic,F.,
            Yuceyar,H., Yildirim,H., Baykan,A.R., Ellidokuz,E.B. and Korkmaz,M.
  TITLE     Overexpressions of RHOA, CSNK1A1, DVL2, FZD8, and LRP5 genes
            enhance gastric cancer development in the presence of Helicobacter
            pylori
  JOURNAL   Arab J Gastroenterol 24 (2), 91-97 (2023)
   PUBMED   36720664
  REMARK    GeneRIF: Overexpressions of RHOA, CSNK1A1, DVL2, FZD8, and LRP5
            genes enhance gastric cancer development in the presence of
            Helicobacter pylori.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Shen,J., Zha,Q., Yang,Q.H., Zhou,Y.Q., Liang,X., Chen,Y.J.,
            Qi,G.X., Zhang,X.J., Yao,W.B., Gao,X.D. and Chen,S.
  TITLE     Inhibiting von Hippel-Lindau protein-mediated Dishevelled
            ubiquitination protects against experimental parkinsonism
  JOURNAL   Acta Pharmacol Sin 44 (5), 940-953 (2023)
   PUBMED   36357669
  REMARK    GeneRIF: Inhibiting von Hippel-Lindau protein-mediated Dishevelled
            ubiquitination protects against experimental parkinsonism.
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Strovel,E.T., Wu,D. and Sussman,D.J.
  TITLE     Protein phosphatase 2Calpha dephosphorylates axin and activates
            LEF-1-dependent transcription
  JOURNAL   J Biol Chem 275 (4), 2399-2403 (2000)
   PUBMED   10644691
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Semenov,M.V. and Snyder,M.
  TITLE     Human dishevelled genes constitute a DHR-containing multigene
            family
  JOURNAL   Genomics 42 (2), 302-310 (1997)
   PUBMED   9192851
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Klingensmith,J., Yang,Y., Axelrod,J.D., Beier,D.R., Perrimon,N. and
            Sussman,D.J.
  TITLE     Conservation of dishevelled structure and function between flies
            and mice: isolation and characterization of Dvl2
  JOURNAL   Mech Dev 58 (1-2), 15-26 (1996)
   PUBMED   8887313
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Pizzuti,A., Amati,F., Calabrese,G., Mari,A., Colosimo,A.,
            Silani,V., Giardino,L., Ratti,A., Penso,D., Calza,L., Palka,G.,
            Scarlato,G., Novelli,G. and Dallapiccola,B.
  TITLE     cDNA characterization and chromosomal mapping of two human
            homologues of the Drosophila dishevelled polarity gene
  JOURNAL   Hum Mol Genet 5 (7), 953-958 (1996)
   PUBMED   8817329
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Greco,T.L., Sussman,D.J. and Camper,S.A.
  TITLE     Dishevelled-2 maps to human chromosome 17 and distal to Wnt3a and
            vestigial tail (vt) on mouse chromosome 11
  JOURNAL   Mamm Genome 7 (6), 475-476 (1996)
   PUBMED   8662242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG716400.1, CB994349.1,
            BC014844.1 and AK026019.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the dishevelled (dsh)
            protein family. The vertebrate dsh proteins have approximately 40%
            amino acid sequence similarity with Drosophila dsh. This gene
            encodes a 90-kD protein that undergoes posttranslational
            phosphorylation to form a 95-kD cytoplasmic protein, which may play
            a role in the signal transduction pathway mediated by multiple Wnt
            proteins. The mechanisms of dishevelled function in Wnt signaling
            are likely to be conserved among metazoans. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014844.1, SRR1660803.149730.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000005340.10/ ENSP00000005340.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..736
                     /product="segment polarity protein dishevelled homolog
                     DVL-2"
                     /note="dishevelled 2 (homologous to Drosophila dsh);
                     dishevelled, dsh homolog 2"
                     /calculated_mol_wt=78817
     Region          13..93
                     /region_name="DAX"
                     /note="Domain present in Dishevelled and axin; smart00021"
                     /db_xref="CDD:197474"
     Region          92..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     Region          125..263
                     /region_name="Dishevelled"
                     /note="Dishevelled specific domain; pfam02377"
                     /db_xref="CDD:460544"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O14641.1)"
     Region          250..355
                     /region_name="Required for interaction with FOXK2.
                     /evidence=ECO:0000269|PubMed:25805136"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     Region          267..353
                     /region_name="PDZ_Dishevelled-like"
                     /note="PDZ domain of segment polarity protein dishevelled
                     homolog DVL1, DVL2, DVL3, and related domains; cd06717"
                     /db_xref="CDD:467201"
     Site            order(277..283,297,300,330,334,337..338)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467201"
     Region          424..507
                     /region_name="DEP_dishevelled"
                     /note="DEP (Dishevelled, Egl-10, and Pleckstrin) domain
                     found in dishevelled-like proteins. Dishevelled-like
                     proteins play a key role in the transduction of the Wnt
                     signal from the cell surface to the nucleus, which in turn
                     is an important regulatory pathway...; cd04438"
                     /db_xref="CDD:239885"
     Region          515..726
                     /region_name="Dsh_C"
                     /note="Segment polarity protein dishevelled (Dsh) C
                     terminal; pfam12316"
                     /db_xref="CDD:463531"
     Region          558..675
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14641.1)"
     CDS             1..736
                     /gene="DVL2"
                     /coded_by="NM_004422.3:256..2466"
                     /db_xref="CCDS:CCDS11091.1"
                     /db_xref="GeneID:1856"
                     /db_xref="HGNC:HGNC:3086"
                     /db_xref="MIM:602151"
ORIGIN      
        1 magsstgggg vgetkviyhl deeetpylvk ipvpaeritl gdfksvlqrp agakyffksm
       61 dqdfgvvkee isddnarlpc fngrvvswlv ssdnpqpema ppvheprael appapplppl
      121 ppertsgigd srppsfhpnv ssshenlepe tetesvvslr rerprrrdss ehgagghrtg
      181 gpsrlerhla gyessstlmt selestslgd sdeedtmsrf sssteqssas rllkrhrrrr
      241 kqrpprlert ssfssvtdst mslniitvtl nmekynflgi sivgqsnerg dggiyigsim
      301 kggavaadgr iepgdmllqv ndmnfenmsn ddavrvlrdi vhkpgpivlt vakcwdpspq
      361 ayftlprnep iqpidpaawv shsaaltgtf paypgsssms titsgsslpd gcegrglsvh
      421 tdmasvtkam aapesglevr drmwlkitip naflgsdvvd wlyhhvegfp errearkyas
      481 gllkaglirh tvnkitfseq cyyvfgdlsg gcesylvnls lndndgssga sdqdtlaplp
      541 gatpwpllpt fsyqypaphp yspqpppyhe lssytygggs assqhsegsr ssgstrsdgg
      601 agrtgrpeer apesksgsgs esepssrggs lrrggeasgt sdggpppsrg stggapnlra
      661 hpglhpygpp pgmalpynpm mvvmmppppp pvppavqppg appvrdlgsv ppeltasrqs
      721 fhmamgnpse ffvdvm
//
LOCUS       NP_115811               1036 aa            linear   PRI 20-NOV-2025
DEFINITION  mitogen-activated protein kinase kinase kinase 21 [Homo sapiens].
ACCESSION   NP_115811
VERSION     NP_115811.2
DBSOURCE    REFSEQ: accession NM_032435.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1036)
  AUTHORS   Gong,M., Shen,F., Li,Y., Ming,L. and Hong,L.
  TITLE     MLK4 as an immune marker and its correlation with immune
            infiltration in Cervical squamous cell carcinoma and endocervical
            adenocarcinoma(CESC)
  JOURNAL   PLoS One 18 (8), e0290462 (2023)
   PUBMED   37594950
  REMARK    GeneRIF: MLK4 as an immune marker and its correlation with immune
            infiltration in Cervical squamous cell carcinoma and endocervical
            adenocarcinoma(CESC).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1036)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1036)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1036)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1036)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 1036)
  AUTHORS   Martini,M., Russo,M., Lamba,S., Vitiello,E., Crowley,E.H.,
            Sassi,F., Romanelli,D., Frattini,M., Marchetti,A. and Bardelli,A.
  TITLE     Mixed lineage kinase MLK4 is activated in colorectal cancers where
            it synergistically cooperates with activated RAS signaling in
            driving tumorigenesis
  JOURNAL   Cancer Res 73 (6), 1912-1921 (2013)
   PUBMED   23319808
  REMARK    GeneRIF: In establishing the role of MLK4 in intracellular
            signaling, we show it directly phosphorylates MEK1 (MAP2K1) and
            that MEK/ERK (MAPK1) signaling is impaired in MLK4 knockout cells
REFERENCE   7  (residues 1 to 1036)
  AUTHORS   Divaris,K., Monda,K.L., North,K.E., Olshan,A.F., Lange,E.M.,
            Moss,K., Barros,S.P., Beck,J.D. and Offenbacher,S.
  TITLE     Genome-wide association study of periodontal pathogen colonization
  JOURNAL   J Dent Res 91 (7 Suppl), 21S-28S (2012)
   PUBMED   22699663
REFERENCE   8  (residues 1 to 1036)
  AUTHORS   Seit-Nebi,A., Cheng,W., Xu,H. and Han,J.
  TITLE     MLK4 has negative effect on TLR4 signaling
  JOURNAL   Cell Mol Immunol 9 (1), 27-33 (2012)
   PUBMED   21602844
  REMARK    GeneRIF: MLK4 is a negative regulator of TLR4 signaling.
REFERENCE   9  (residues 1 to 1036)
  AUTHORS   Grassi,M.A., Tikhomirov,A., Ramalingam,S., Below,J.E., Cox,N.J. and
            Nicolae,D.L.
  TITLE     Genome-wide meta-analysis for severe diabetic retinopathy
  JOURNAL   Hum Mol Genet 20 (12), 2472-2481 (2011)
   PUBMED   21441570
REFERENCE   10 (residues 1 to 1036)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL133380.5 and AJ311798.1.
            
            On Aug 14, 2007 this sequence version replaced NP_115811.1.
            
            Sequence Note: This RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ311798.1, BC136648.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366624.8/ ENSP00000355583.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1036
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.2"
     Protein         1..1036
                     /product="mitogen-activated protein kinase kinase kinase
                     21"
                     /EC_number="2.7.11.25"
                     /note="mitogen-activated protein kinase kinase kinase
                     MLK4; mixed lineage kinase 4"
                     /calculated_mol_wt=113826
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          42..97
                     /region_name="SH3_MLK4"
                     /note="Src Homology 3 domain of Mixed Lineage Kinase 4;
                     cd12058"
                     /db_xref="CDD:212991"
     Site            order(47,49,52,56,79..80,93,95..96)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212991"
     Region          129..401
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(130..133,136,138,149,151,184,200..203,263,267..268,
                     270,288..289)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis and MAP4K1.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          425..446
                     /region_name="Leucine-zipper 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          460..481
                     /region_name="Leucine-zipper 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          517..551
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDG6; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VDG6; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          748..791
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     Region          923..954
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5TCX8.3)"
     CDS             1..1036
                     /gene="MAP3K21"
                     /gene_synonym="dJ862P8.3; MLK4"
                     /coded_by="NM_032435.3:306..3416"
                     /db_xref="CCDS:CCDS1598.1"
                     /db_xref="GeneID:84451"
                     /db_xref="HGNC:HGNC:29798"
                     /db_xref="MIM:614793"
ORIGIN      
        1 malrgaagat dtpvssagga pggsasssst ssggsasaga glwaalydye argedelslr
       61 rgqlvevlsq daavsgdegw wagqvqrrlg ifpanyvapc rpaaspappp srpsspvhva
      121 ferlelkeli gaggfgqvyr atwqgqevav kaarqdpeqd aaaaaesvrr earlfamlrh
      181 pniielrgvc lqqphlclvl efarggalnr alaaanaapd prapgprrar ripphvlvnw
      241 avqiargmly lheeafvpil hrdlkssnil llekiehddi cnktlkitdf glarewhrtt
      301 kmstagtyaw mapevikssl fskgsdiwsy gvllwelltg evpyrgidgl avaygvavnk
      361 ltlpipstcp epfaklmkec wqqdphirps falileqlta iegavmtemp qesfhsmqdd
      421 wkleiqqmfd elrtkekelr sreeeltraa lqqksqeell krreqqlaer eidvlereln
      481 ilifqlnqek pkvkkrkgkf krsrlklkdg hrislpsdfq hkitvqaspn ldkrrslnss
      541 sssppssptm mprlraiqlt sdesnktwgr ntvfrqeefe dvkrnfkkkg ctwgpnsiqm
      601 kdrtdckeri rplsdgnspw stiliknqkt mplaslfvdq pgsceepkls pdglehrkpk
      661 qiklpsqayi dlplgkdaqr enpaeaeswe eaasanaatv siemtptnsl srspqrkkte
      721 salygctvll asvalgldlr elhkaqaaee plpkeekkkr egifqrasks rrsaspptsl
      781 pstcgeassp pslplssalg ilstpsfstk cllqmdsedp lvdsapvtcd semltpdfcp
      841 tapgsgrepa lmprldtdcs vsrnlpssfl qqtcgnvpyc asskhrpshh rrtmsdgnpt
      901 ptgatiisat gasalplcps paphshlpre vspkkhstvh ivpqrrpasl rsrsdlpqay
      961 pqtavsqlaq tacvvgrpgp hptqflaake rtkshvpsll dadvegqsrd ytvplcrmrs
     1021 ktsrpsiyel ekefls
//
LOCUS       NP_060918               1230 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-associated NEDD8-dissociated protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060918
VERSION     NP_060918.2
DBSOURCE    REFSEQ: accession NM_018448.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1230)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1230)
  AUTHORS   Ao,Y.Q., Gao,J., Jin,C., Wang,S., Zhang,L.C., Deng,J., Chen,Z.W.,
            Wang,H.K., Jiang,J.H. and Ding,J.Y.
  TITLE     ASCC3 promotes the immunosuppression and progression of non-small
            cell lung cancer by impairing the type I interferon response via
            CAND1-mediated ubiquitination inhibition of STAT3
  JOURNAL   J Immunother Cancer 11 (12), e007766 (2023)
   PUBMED   38148115
  REMARK    GeneRIF: ASCC3 promotes the immunosuppression and progression of
            non-small cell lung cancer by impairing the type I interferon
            response via CAND1-mediated ubiquitination inhibition of STAT3.
            Erratum:[J Immunother Cancer. 2024 Jul 10;12(7):e007766corr1. doi:
            10.1136/jitc-2023-007766corr1. PMID: 38986545]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1230)
  AUTHORS   Pierce,N.W., Lee,J.E., Liu,X., Sweredoski,M.J., Graham,R.L.,
            Larimore,E.A., Rome,M., Zheng,N., Clurman,B.E., Hess,S., Shan,S.O.
            and Deshaies,R.J.
  TITLE     Cand1 promotes assembly of new SCF complexes through dynamic
            exchange of F box proteins
  JOURNAL   Cell 153 (1), 206-215 (2013)
   PUBMED   23453757
  REMARK    GeneRIF: Study shows that Cand1 can unambiguously stimulate SCF
            activity in vitro by enabling an F box protein-Skp1 complex to
            access Cul1 that was previously occupied by a different F box
            protein-Skp1 complex, and that Cand1 promotes assembly in vivo of
            new F box proteins with pre-existing Cul1 molecules.
REFERENCE   4  (residues 1 to 1230)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
  REMARK    GeneRIF: COMMD1 (copper metabolism MURR1 domain-containing protein
            1) regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding.
REFERENCE   5  (residues 1 to 1230)
  AUTHORS   Chua,Y.S., Boh,B.K., Ponyeam,W. and Hagen,T.
  TITLE     Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo
  JOURNAL   PLoS One 6 (1), e16071 (2011)
   PUBMED   21249194
  REMARK    GeneRIF: CAND1 does not function by sequestering cullins in vivo to
            prevent substrate receptor autoubiquitination and is likely to
            regulate cullin RING ligase activity via alternative mechanisms
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1230)
  AUTHORS   Goldenberg,S.J., Cascio,T.C., Shumway,S.D., Garbutt,K.C., Liu,J.,
            Xiong,Y. and Zheng,N.
  TITLE     Structure of the Cand1-Cul1-Roc1 complex reveals regulatory
            mechanisms for the assembly of the multisubunit cullin-dependent
            ubiquitin ligases
  JOURNAL   Cell 119 (4), 517-528 (2004)
   PUBMED   15537541
REFERENCE   7  (residues 1 to 1230)
  AUTHORS   Zheng,J., Yang,X., Harrell,J.M., Ryzhikov,S., Shim,E.H.,
            Lykke-Andersen,K., Wei,N., Sun,H., Kobayashi,R. and Zhang,H.
  TITLE     CAND1 binds to unneddylated CUL1 and regulates the formation of SCF
            ubiquitin E3 ligase complex
  JOURNAL   Mol Cell 10 (6), 1519-1526 (2002)
   PUBMED   12504026
  REMARK    GeneRIF: binds to unneddylated CUL1 and regulates the formation of
            SCF ubiquitin E3 ligase complex
REFERENCE   8  (residues 1 to 1230)
  AUTHORS   Liu,J., Furukawa,M., Matsumoto,T. and Xiong,Y.
  TITLE     NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of
            CUL1-SKP1 binding and SCF ligases
  JOURNAL   Mol Cell 10 (6), 1511-1518 (2002)
   PUBMED   12504025
  REMARK    GeneRIF: selectively binds to unneddylated CUL1 and is dissociated
            by CUL1 neddylation
REFERENCE   9  (residues 1 to 1230)
  AUTHORS   Yogosawa,S., Kayukawa,K., Kawata,T., Makino,Y., Inoue,S., Okuda,A.,
            Muramatsu,M. and Tamura,T.
  TITLE     Induced expression, localization, and chromosome mapping of a gene
            for the TBP-interacting protein 120A
  JOURNAL   Biochem Biophys Res Commun 266 (1), 123-128 (1999)
   PUBMED   10581176
REFERENCE   10 (residues 1 to 1230)
  AUTHORS   Yogosawa,S., Makino,Y., Yoshida,T., Kishimoto,T., Muramatsu,M. and
            Tamura,T.
  TITLE     Molecular cloning of a novel 120-kDa TBP-interacting protein
  JOURNAL   Biochem Biophys Res Commun 229 (2), 612-617 (1996)
   PUBMED   8954946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB064887.1, AL136810.1,
            AB020636.2, BQ024785.1 and AC078983.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_060918.1.
            
            Summary: This gene encodes an essential regulator of Cullin-RING
            ubiquitin ligases, which are in involved in ubiquitinylation of
            proteins degraded by the Ub proteasome system. The encoded protein
            binds to unneddylated cullin-RING box protein complexes and acts as
            an inhibitor of cullin neddylation and of Skp1, cullin, and F box
            ubiquitin ligase complex assembly and activity. In mammalian cell
            culture, this protein predominantly localizes to the cytoplasm.
            Knockdown of this gene in preadipocytes results in blocked
            adipogenesis. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.200182.1,
                                           SRR1803616.9626.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000545606.6/ ENSP00000442318.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.3-q15"
     Protein         1..1230
                     /product="cullin-associated NEDD8-dissociated protein 1
                     isoform 1"
                     /note="cullin-associated NEDD8-dissociated protein 1; p120
                     CAND1; TBP-interacting protein of 120 kDa A"
                     /calculated_mol_wt=136245
     Region          2..39
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          11..32
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          44..81
                     /region_name="HEAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          53..74
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            order(66..67,70,73..74,104..105,108,115..116,119,152..153,
                     156,159..160,163,193..194,197,200..201,235..236,239,
                     242..243)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          83..119
                     /region_name="HEAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          87..119
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          129..164
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          131..165
                     /region_name="HEAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          149..202
                     /region_name="HEAT_EZ"
                     /note="HEAT-like repeat; pfam13513"
                     /db_xref="CDD:463906"
     Region          171..208
                     /region_name="HEAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          175..201
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          210..247
                     /region_name="HEAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          211..243
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          248..282
                     /region_name="HEAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          255..285
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          289..366
                     /region_name="HEAT 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          296..359
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          315..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          370..407
                     /region_name="HEAT 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          372..397
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          424..467
                     /region_name="HEAT 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          471..510
                     /region_name="HEAT 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          515..552
                     /region_name="HEAT 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          563..602
                     /region_name="HEAT 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          573..600
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(587..588,591,594..595,600,626..627,630,633..634,637,
                     668..669,672,675..676,710..711,714,717..718)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          606..643
                     /region_name="HEAT 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          610..638
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          646..683
                     /region_name="HEAT 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          647..676
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          688..725
                     /region_name="HEAT 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          690..719
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          729..768
                     /region_name="HEAT 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          770..808
                     /region_name="HEAT 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            order(797..798,801,804..805,836..837,840,843..844,847,
                     874..875,878,881..882,885,910..911,914,917..918,953,
                     956..957)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          809..845
                     /region_name="HEAT 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          817..847
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          852..889
                     /region_name="HEAT 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          856..886
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          890..927
                     /region_name="HEAT 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          894..918
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          928..960
                     /region_name="HEAT 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          929..958
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          961..998
                     /region_name="HEAT 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Site            971
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          1002..1039
                     /region_name="HEAT 24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          1040..1202
                     /region_name="TIP120"
                     /note="TATA-binding protein interacting (TIP20);
                     pfam08623"
                     /db_xref="CDD:430111"
     Region          1043..1097
                     /region_name="HEAT 25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          1099..1133
                     /region_name="HEAT 26"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     Region          1140..1189
                     /region_name="HEAT 27"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VP6.2)"
     CDS             1..1230
                     /gene="CAND1"
                     /gene_synonym="TIP120; TIP120A"
                     /coded_by="NM_018448.5:361..4053"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8977.1"
                     /db_xref="GeneID:55832"
                     /db_xref="HGNC:HGNC:30688"
                     /db_xref="MIM:607727"
ORIGIN      
        1 masasyhisn llekmtssdk dfrfmatndl mtelqkdsik ldddserkvv kmilklledk
       61 ngevqnlavk clgplvskvk eyqvetivdt lctnmlsdke qlrdissigl ktvigelppa
      121 ssgsalaanv ckkitgrlts aiakqedvsv qlealdimad mlsrqggllv nfhpsiltcl
      181 lpqltsprla vrkrtiialg hlvmscgniv fvdliehlls elskndsmst trtyiqciaa
      241 isrqaghrig eylekiiplv vkfcnvddde lreyciqafe sfvrrcpkev yphvstiini
      301 clkyltydpn ynyddedede namdadggdd ddqgsddeys ddddmswkvr raaakcldav
      361 vstrhemlpe fyktvspali srfkereenv kadvfhayls llkqtrpvqs wlcdpdameq
      421 getpltmlqs qvpnivkalh kqmkeksvkt rqccfnmlte lvnvlpgalt qhipvlvpgi
      481 ifslndksss snlkidalsc lyvilcnhsp qvfhphvqal vppvvacvgd pfykitseal
      541 lvtqqlvkvi rpldqpssfd atpyikdlft ctikrlkaad idqevkerai scmgqiicnl
      601 gdnlgsdlpn tlqiflerlk neitrlttvk altliagspl kidlrpvlge gvpilasflr
      661 knqralklgt lsaldilikn ysdsltaami davldelppl isesdmhvsq maisflttla
      721 kvypsslski sgsilnelig lvrspllqgg alsamldffq alvvtgtnnl gymdllrmlt
      781 gpvysqstal thkqsyysia kcvaaltrac pkegpavvgq fiqdvknsrs tdsirllall
      841 slgevghhid lsgqlelksv ileafsspse evksaasyal gsisvgnlpe ylpfvlqeit
      901 sqpkrqylll hslkeiissa svvglkpyve niwalllkhc ecaeegtrnv vaeclgkltl
      961 idpetllprl kgylisgssy arssvvtavk ftisdhpqpi dpllkncigd flktledpdl
     1021 nvrrvalvtf nsaahnkpsl irdlldtvlp hlynetkvrk elirevemgp fkhtvddgld
     1081 irkaafecmy tlldscldrl difeflnhve dglkdhydik mltflmlvrl stlcpsavlq
     1141 rldrlveplr atcttkvkan svkqefekqd elkrsamrav aalltipeae ksplmsefqs
     1201 qissnpelaa ifesiqkdss stnlesmdts
//
LOCUS       NP_065939               1094 aa            linear   PRI 20-NOV-2025
DEFINITION  NHS-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_065939 XP_036299
VERSION     NP_065939.2
DBSOURCE    REFSEQ: accession NM_020888.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Guo,Y., Tian,S., Li,H., Zuo,S., Yu,C. and Sun,C.
  TITLE     Transcription factor KLF9 inhibits the proliferation, invasion, and
            migration of pancreatic cancer cells by repressing KIAA1522
  JOURNAL   Asia Pac J Clin Oncol 20 (3), 423-432 (2024)
   PUBMED   38520660
  REMARK    GeneRIF: Transcription factor KLF9 inhibits the proliferation,
            invasion, and migration of pancreatic cancer cells by repressing
            KIAA1522.
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Palukuri,M.V., Patil,R.S. and Marcotte,E.M.
  TITLE     Molecular complex detection in protein interaction networks through
            reinforcement learning
  JOURNAL   BMC Bioinformatics 24 (1), 306 (2023)
   PUBMED   37532987
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1094)
  AUTHORS   Ou,M., Chu,Y., Zhang,Q., Zhao,H. and Song,Q.
  TITLE     HOXA cluster antisense RNA 2 elevates KIAA1522 expression through
            microRNA-520d-3p and insulin like growth factor 2 mRNA binding
            protein 3 to promote the growth of vascular smooth muscle cells in
            thoracic aortic aneurysm
  JOURNAL   ESC Heart Fail 9 (5), 2955-2966 (2022)
   PUBMED   35730141
  REMARK    GeneRIF: HOXA cluster antisense RNA 2 elevates KIAA1522 expression
            through microRNA-520d-3p and insulin like growth factor 2 mRNA
            binding protein 3 to promote the growth of vascular smooth muscle
            cells in thoracic aortic aneurysm.
REFERENCE   5  (residues 1 to 1094)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1094)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 1094)
  AUTHORS   Wang,B., Jing,T., Jin,W., Chen,J., Wu,C., Wang,M. and Liu,Y.
  TITLE     KIAA1522 potentiates TNFalpha-NFkappaB signaling to antagonize
            platinum-based chemotherapy in lung adenocarcinoma
  JOURNAL   J Exp Clin Cancer Res 39 (1), 170 (2020)
   PUBMED   32854746
  REMARK    GeneRIF: KIAA1522 potentiates TNFalpha-NFkappaB signaling to
            antagonize platinum-based chemotherapy in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1094)
  AUTHORS   Li,Y., Wang,Y., Fan,H., Zhang,Z. and Li,N.
  TITLE     miR-125b-5p inhibits breast cancer cell proliferation, migration
            and invasion by targeting KIAA1522
  JOURNAL   Biochem Biophys Res Commun 504 (1), 277-282 (2018)
   PUBMED   30177391
  REMARK    GeneRIF: miR-125b-5p functions as a tumor suppressor and regulates
            breast cancer cell progression through targeting KIAA1522
REFERENCE   9  (residues 1 to 1094)
  AUTHORS   Liu,Y.Z., Yang,H., Cao,J., Jiang,Y.Y., Hao,J.J., Xu,X., Cai,Y. and
            Wang,M.R.
  TITLE     KIAA1522 is a novel prognostic biomarker in patients with non-small
            cell lung cancer
  JOURNAL   Sci Rep 6, 24786 (2016)
   PUBMED   27098511
  REMARK    GeneRIF: high expression of KIAA1522 can be used as an independent
            biomarker for predication of poor survival and platinum-resistance
            of NSCLC patients, and aberrant KIAA1522 might be a new target for
            the therapy of the disease.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1094)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2, AI587184.1, AB040955.1 and AL713671.1.
            
            On Aug 18, 2006 this sequence version replaced NP_065939.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401073.7/ ENSP00000383851.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..1094
                     /product="NHS-like protein 3 isoform 1"
                     /note="NHS-like protein 3"
                     /calculated_mol_wt=112931
     Region          <783..1059
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1094
                     /gene="NHSL3"
                     /gene_synonym="KIAA1522"
                     /coded_by="NM_020888.3:126..3410"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41298.1"
                     /db_xref="GeneID:57648"
                     /db_xref="HGNC:HGNC:29301"
ORIGIN      
        1 maarappaap aaeepgnpgg pprrkksrsg asglrrafsw lrgkrrkkka agaegaepaa
       61 prakkaedka krakgkgrgs akaendkhls vgpgqgpgsa vdehqdnvff psgrpphlee
      121 lhtqaqeglr slqhqekqkl nkggwdhgdt qsiqssrtgp dednisfcsq ttsyvaesst
      181 aedalsirse miqrkgstfr phdsfpksgk sgrrrrerrs tvlglpqhvq kelglrnere
      241 apgtprapga rdavriptvd grprgtsgmg arvslqalea eaeagaetea mlqrhidrvy
      301 rddtfvgrst gtrappltrp mslavpgltg gagpaeplsp amsispqaty lskliphavl
      361 pptvdvvalg rcslrtlsrc slhsaspasv rslgrfssvs spqprsrhps sssdtwshsq
      421 ssdtivsdgs tlsskggseg qpesstasns vvpppqggsg rgspsggsta easdtlsirs
      481 sgqlsgrsvs lrklkrpppp prrthslhqr glavpdgplg lppkperkqq pqlprppttg
      541 gsegagaapc ppnpanswvp glspggsrrp prspertlsp ssgyssqsgt ptlppkglag
      601 ppaspgkaqp pkpervtslr spgasvsssl tslcssssdp apsdrsgpqi ltplgdrfvi
      661 pphpkvpapf spppskprsp npaapalaap avvpgpvstt daspqspptp qttltplqes
      721 pviskdqspp pspppsyhpp ppptkkpevv veapsaseta eeplqdpnwp pppppapeeq
      781 dlsmadfppp eeaffsvasp epagpsgspe lvsspaasss satalqiqpp gspdpppapp
      841 apapassapg hvaklpqkep vgcskgggpp redvgaplvt psllqmvrlr svgapggapt
      901 palgpsapqk plrralsgra spvpapssgl haavrlkacs laaseglssa qpngppeaep
      961 rppqspasta sfifskgsrk lqlerpvspe tqadlqrnlv aelrsiseqr ppqapkkspk
     1021 apppvarkps vgvpppasps ypraepltap ptnglphtqd rtkrelaeng gvlqlvgpee
     1081 kmglpgsdsq kela
//
LOCUS       NP_001339964             769 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 5 [Homo sapiens].
ACCESSION   NP_001339964 XP_016880971
VERSION     NP_001339964.1
DBSOURCE    REFSEQ: accession NM_001353035.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 769)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 769)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 769)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 769)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 769)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002558.2.
            
            On Jun 28, 2017 this sequence version replaced XP_016880971.1.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2196707.1,
                                           SRR14038191.4224269.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..769
                     /product="cell division cycle protein 27 homolog isoform
                     5"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=85689
     Region          6..35
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          17..92
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          38..65
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          67..99
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          115..145
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Region          287..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          448..>671
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          465..495
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          499..528
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          501..527
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          533..563
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          561..>731
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          567..598
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          567..595
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(568,571..572,575..576,578,602,605..606,609..610,
                     612..613,636,639..640,643..644,647)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          600..630
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          601..631
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          635..667
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          635..663
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          669..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          670..702
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          703..731
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          704..734
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     CDS             1..769
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001353035.2:124..2433"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mtvlqepvqa aiwqalnhya yrdavflaer lyaevhseea lfllatcyyr sgkaykayrl
       61 lkghscttpq ckyllakccv dlsklaegeq ilsggvfnkq kshddivtef gdsacftlsl
      121 lghvycktdr lakgsecyqk slslnpflws pfeslceige kpdpdqtfkf tslqnfsncl
      181 pnscttqvpn hslshrqpet vltetpqdti elnrlnless nskyslntds svsyidsavi
      241 spdtvplgtg tsilskqvqn kpktgrsllg gpaalspltp sfgilpletp spgdgsylqn
      301 ytntppvidv pstgapskks varigqtgtk svfsqsgnsr evtpilaqtq ssgpqtsttp
      361 qvlsptitsp pnalprrssr lftsdssttk enskklkmkf ppkipnrktk sktnkggitq
      421 pnindsleit kldssiiseg kistitpqiq afnlqkaaae glmsllremg kgylalcsyn
      481 ckeainilsh lpshhyntgw vlcqigrayf elseymqaer ifsevrrien yrvegmeiys
      541 ttlwhlqkdv alsvlskdlt dmdknspeaw caagncfslq rehdiaikff qraiqvdpny
      601 ayaytllghe fvlteeldka lacfrnairv nprhynawyg lgmiyykqek fslaemhfqk
      661 aldinpqssv llchigvvqh alkksekald tlnkaividp knplckfhra svlfanekyk
      721 salqeleelk qivpkeslvy fligkilkep itrlkrqlis vifqmmrsq
//
LOCUS       NP_001269609            1460 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001269609 XP_005251959
VERSION     NP_001269609.1
DBSOURCE    REFSEQ: accession NM_001282680.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On Sep 17, 2013 this sequence version replaced XP_005251959.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.174962.1, BC114937.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297933.11/ ENSP00000297933.6
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1460
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 2"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=162767
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Site            172
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          574..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          739..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          846..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          889..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          1245..1308
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1356..1457
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1460
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001282680.3:333..4715"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS65131.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgkpd ktlrfslcsd nlegisegps nrsnsvssld legesvselg
      601 agpsgsngve alqlleheqa ttqdnlddkl rkfeirdmmg ltddrdiset vsetwstdvl
      661 gsdfdpnide drlqeiagaa aenmlgsllc lpgsgsvlld pctgstiset tseawsvevl
      721 psdseapdlk qeerlqeles csglgstsdd tdvrevssrp stpglsvvsg isatsedipn
      781 kiedlrsecs sdfggkdsvt spdmdeithg ahqltsppsq sesllamfdp lsshegasav
      841 vrpkvhyarp shpppdppil egavggnear lpnfgshvlt paemeafkqr hsyperlvrs
      901 rssdivssvr rpmsdpswnr rpgneerelp paaaigatsl vaaphsssss pskdssrget
      961 eerkdsddek sdrnrpwwrk rfvsampkap ipfrkkekqe kdkddlgpdr fstltddpsp
     1021 rlsaqaqvae dildkyrnai krtspsdgam anyestevmg dgesahdspr dealqnisad
     1081 dlpdsasqaa hpqdsafsyr dakkklrlal csadsvafpv lthstrnglp dhtdpednei
     1141 vcflkvqiae ainlqdknlm aqlqetmrcv crfdnrtcrk llasiaedyr krapyiaylt
     1201 rcrqglqttq ahlerllqrv lrdkevanry fttvcvrlll eskekkiref iqdfqkltaa
     1261 ddktaqvedf lqflygamaq dviwqnasee qlqdaqlaie rsvmnrifkl afypnqdgdi
     1321 lrdqvlhehi qrlskvvtan hralqipevy lreapwpsaq seirtisayk tprdkvqcil
     1381 rmcstimnll slanedsvpg addfvpvlvf vlikanppcl lstvqyissf yasclsgees
     1441 ywwmqftaav efiktiddrk
//
LOCUS       NP_003898                721 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit epsilon [Homo sapiens].
ACCESSION   NP_003898
VERSION     NP_003898.2
DBSOURCE    REFSEQ: accession NM_003907.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Nourmohammadi,P., Asadollahi,M., Karamzade,A., Eshaghkhani,Y.,
            Babaei,M., Golchehre,Z., Taheri,S.R., Hasani,S., Taghizadeh,M. and
            Keramatipour,M.
  TITLE     A novel missense variant in EIF2B5 identified in a consanguineous
            Iranian family with vanishing white matter disease and a brief
            review of the literature
  JOURNAL   J Genet 102 (2023)
   PUBMED   37674283
  REMARK    GeneRIF: A novel missense variant in EIF2B5 identified in a
            consanguineous Iranian family with vanishing white matter disease
            and a brief review of the literature.
            Review article
REFERENCE   2  (residues 1 to 721)
  AUTHORS   He,S.L., Zhao,X. and Yi,S.J.
  TITLE     CircAHNAK upregulates EIF2B5 expression to inhibit the progression
            of ovarian cancer by modulating the JAK2/STAT3 signaling pathway
  JOURNAL   Carcinogenesis 43 (10), 941-955 (2022)
   PUBMED   35710311
  REMARK    GeneRIF: CircAHNAK upregulates EIF2B5 expression to inhibit the
            progression of ovarian cancer by modulating the JAK2/STAT3
            signaling pathway.
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Keefe,M.D., Soderholm,H.E., Shih,H.Y., Stevenson,T.J.,
            Glaittli,K.A., Bowles,D.M., Scholl,E., Colby,S., Merchant,S.,
            Hsu,E.W. and Bonkowsky,J.L.
  TITLE     Vanishing white matter disease expression of truncated EIF2B5
            activates induced stress response
  JOURNAL   Elife 9, e56319 (2020)
   PUBMED   33300869
  REMARK    GeneRIF: Vanishing white matter disease expression of truncated
            EIF2B5 activates induced stress response.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Kimball,S.R., Heinzinger,N.K., Horetsky,R.L. and Jefferson,L.S.
  TITLE     Identification of interprotein interactions between the subunits of
            eukaryotic initiation factors eIF2 and eIF2B
  JOURNAL   J Biol Chem 273 (5), 3039-3044 (1998)
   PUBMED   9446619
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Welsh,G.I., Miller,C.M., Loughlin,A.J., Price,N.T. and Proud,C.G.
  TITLE     Regulation of eukaryotic initiation factor eIF2B: glycogen synthase
            kinase-3 phosphorylates a conserved serine which undergoes
            dephosphorylation in response to insulin
  JOURNAL   FEBS Lett 421 (2), 125-130 (1998)
   PUBMED   9468292
REFERENCE   7  (residues 1 to 721)
  AUTHORS   Asuru,A.I., Mellor,H., Thomas,N.S., Yu,L., Chen,J.J., Crosby,J.S.,
            Hartson,S.D., Kimball,S.R., Jefferson,L.S. and Matts,R.L.
  TITLE     Cloning and characterization of cDNAs encoding the epsilon-subunit
            of eukaryotic initiation factor-2B from rabbit and human
  JOURNAL   Biochim Biophys Acta 1307 (3), 309-317 (1996)
   PUBMED   8688466
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 721)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC013590.1 and AC131235.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 5, 2005 this sequence version replaced NP_003898.1.
            
            Summary: This gene encodes one of five subunits of eukaryotic
            translation initiation factor 2B (EIF2B), a GTP exchange factor for
            eukaryotic initiation factor 2 and an essential regulator for
            protein synthesis. Mutations in this gene and the genes encoding
            other EIF2B subunits have been associated with leukoencephalopathy
            with vanishing white matter. [provided by RefSeq, Nov 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.231381.1,
                                           SRR1803612.95745.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000648915.2/ ENSP00000497160.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..721
                     /product="translation initiation factor eIF2B subunit
                     epsilon"
                     /note="translation initiation factor eIF-2B subunit
                     epsilon; eIF-2B GDP-GTP exchange factor subunit epsilon;
                     eukaryotic translation initiation factor 2B, subunit 5
                     epsilon, 82kDa; eIF2B GDP-GTP exchange factor subunit
                     epsilon"
                     /calculated_mol_wt=80249
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13144.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q13144.3)"
     Site            19
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CHW4; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64350; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Region          43..257
                     /region_name="eIF-2B_epsilon_N"
                     /note="The N-terminal domain of epsilon subunit of the
                     eIF-2B is a subfamily of glycosyltransferase 2; cd04197"
                     /db_xref="CDD:133040"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64350; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q64350; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Region          361..439
                     /region_name="LbH_eIF2B_epsilon"
                     /note="eIF-2B epsilon subunit, central Left-handed
                     parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic
                     translation initiator, a guanine nucleotide exchange
                     factor (GEF) composed of five different subunits (alpha,
                     beta, gamma, delta and epsilon). eIF2B is...; cd05787"
                     /db_xref="CDD:100061"
     Region          444..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13144.3)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Region          523..547
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13144.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64350; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64350; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DYRK2.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13144.3)"
     Region          548..711
                     /region_name="W2_eIF2B_epsilon"
                     /note="C-terminal W2 domain of eukaryotic translation
                     initiation factor 2B epsilon; cd11558"
                     /db_xref="CDD:211396"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13144.3)"
     CDS             1..721
                     /gene="EIF2B5"
                     /gene_synonym="CACH; CLE; EIF-2B; EIF2Bepsilon; LVWM;
                     VWM5"
                     /coded_by="NM_003907.3:29..2194"
                     /db_xref="CCDS:CCDS3252.1"
                     /db_xref="GeneID:8893"
                     /db_xref="HGNC:HGNC:3261"
                     /db_xref="MIM:603945"
ORIGIN      
        1 maapvvappg vvvsrankrs gagpggsggg gargaeeepp pplqavlvad sfdrrffpis
       61 kdqprvllpl anvalidytl efltatgvqe tfvfccwkaa qikehllksk wcrptslnvv
      121 riitselyrs lgdvlrdvda kalvrsdfll vygdvisnin itraleehrl rrkleknvsv
      181 mtmifkessp shptrchedn vvvavdsttn rvlhfqktqg lrrfafplsl fqgssdgvev
      241 rydlldchis icspqvaqlf tdnfdyqtrd dfvrgllvne eilgnqihmh vtakeygarv
      301 snlhmysavc advirrwvyp ltpeanftds ttqscthsrh niyrgpevsl ghgsileenv
      361 llgsgtvigs ncfitnsvig pgchigdnvv ldqtylwqgv rvaagaqihq sllcdnaevk
      421 ervtlkprsv ltsqvvvgpn itlpegsvis lhppdaeede ddgefsddsg adqekdkvkm
      481 kgynpaevga agkgylwkaa gmnmeeeeel qqnlwglkin meeesesese qsmdseepds
      541 rggspqmddi kvfqnevlgt lqrgkeenis cdnlvleins lkyaynislk evmqvlshvv
      601 lefplqqmds pldssrycal llpllkawsp vfrnyikraa dhlealaaie dfflehealg
      661 ismakvlmaf yqleilaeet ilswfsqrdt tdkgqqlrkn qqlqrfiqwl keaeeessed
      721 d
//
LOCUS       NP_001230165             507 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform l [Homo sapiens].
ACCESSION   NP_001230165
VERSION     NP_001230165.1
DBSOURCE    REFSEQ: accession NM_001243236.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091103.4, AL518903.3,
            FR748222.1 and AK300038.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (12) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            3' end of an exon compared to variant 3. The resulting isoform (l)
            has a shorter and distinct N-terminus and lacks an alternate
            internal segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FR748222.1, ERR4368410.60984.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..507
                     /product="transcription factor 4 isoform l"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=54038
     Region          398..482
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(406,410,412..414,416,421,442..443)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(419..420,423..424,426..427,430,434,444,447,451,454,
                     457..462)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..507
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243236.2:177..1700"
                     /note="isoform l is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS58623.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mkfkqcrcsd tglccldheg kaevyapsas tadynrdspg ypsskpatst fpssffmqdg
       61 hhssdpwsss sgmnqpgyag mlgnsshipq sssycslhph erlsypshss adinsslppm
      121 stfhrsgtnh ystssctppa ngtdsimanr gsgaagssqt gdalgkalas iyspdhtnns
      181 fssnpstpvg sppslsagta vwsrnggqas sspnyegplh slqsriedrl erlddaihvl
      241 rnhavgpsta mpgghgdmhg iigpshngam gglgsgygtg llsanrhslm vgthredgva
      301 lrgshsllpn qvpvpqlpvq satspdlnpp qdpyrgmppg lqgqsvssgs seiksddegd
      361 enlqdtksse dkkldddkkd iksitsnndd edltpeqkae rekerrmann arerlrvrdi
      421 neafkelgrm vqlhlksdkp qtkllilhqa vavilsleqq vrernlnpka aclkrreeek
      481 vsseppplsl agphpgmgda snhmgqm
//
LOCUS       NP_005400                 94 aa            linear   PRI 20-NOV-2025
DEFINITION  C-X-C motif chemokine 11 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_005400
VERSION     NP_005400.1
DBSOURCE    REFSEQ: accession NM_005409.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 94)
  AUTHORS   Barbieri,F., Bajetto,A., Dellacasagrande,I., Solari,A., Wurth,R.,
            Fernandez,V., Rancati,S., Ceresa,D., Appolloni,I., De Luca,G.,
            Dono,M., Nozza,P., Schiapparelli,P., Gambaro,M., Fiaschi,P.,
            Gaggero,G., Costanzo,N., Thellung,S., Malatesta,P., Pagano,A.,
            Zona,G., De Pietri Tonelli,D. and Florio,T.
  TITLE     Stem-like signatures in human meningioma cells are under the
            control of CXCL11/CXCL12 chemokine activity
  JOURNAL   Neuro Oncol 25 (10), 1775-1787 (2023)
   PUBMED   37074930
  REMARK    GeneRIF: Stem-like signatures in human meningioma cells are under
            the control of CXCL11/CXCL12 chemokine activity.
REFERENCE   2  (residues 1 to 94)
  AUTHORS   Luttrell,L.M.
  TITLE     Reviews in molecular biology and biotechnology: transmembrane
            signaling by G protein-coupled receptors
  JOURNAL   Mol Biotechnol 39 (3), 239-264 (2008)
   PUBMED   18240029
  REMARK    Review article
REFERENCE   3  (residues 1 to 94)
  AUTHORS   Kouroumalis,A., Nibbs,R.J., Aptel,H., Wright,K.L., Kolios,G. and
            Ward,S.G.
  TITLE     The chemokines CXCL9, CXCL10, and CXCL11 differentially stimulate G
            alpha i-independent signaling and actin responses in human
            intestinal myofibroblasts
  JOURNAL   J Immunol 175 (8), 5403-5411 (2005)
   PUBMED   16210647
  REMARK    GeneRIF: This CSCR3 ligand has the ability to activate biochemical
            (e.g., PtdIns and MAP kinase activation) and functional events
            (actin reorganization) in intestinal myofibroblasts.
REFERENCE   4  (residues 1 to 94)
  AUTHORS   Booth,V., Clark-Lewis,I. and Sykes,B.D.
  TITLE     NMR structure of CXCR3 binding chemokine CXCL11 (ITAC)
  JOURNAL   Protein Sci 13 (8), 2022-2028 (2004)
   PUBMED   15273303
REFERENCE   5  (residues 1 to 94)
  AUTHORS   Colvin,R.A., Campanella,G.S., Sun,J. and Luster,A.D.
  TITLE     Intracellular domains of CXCR3 that mediate CXCL9, CXCL10, and
            CXCL11 function
  JOURNAL   J Biol Chem 279 (29), 30219-30227 (2004)
   PUBMED   15150261
  REMARK    GeneRIF: CXCL9, CXCL10, and CXCL11 functions are mediated by
            intracellular domains of CXCR3
REFERENCE   6  (residues 1 to 94)
  AUTHORS   Yang,D., Chen,Q., Hoover,D.M., Staley,P., Tucker,K.D., Lubkowski,J.
            and Oppenheim,J.J.
  TITLE     Many chemokines including CCL20/MIP-3alpha display antimicrobial
            activity
  JOURNAL   J Leukoc Biol 74 (3), 448-455 (2003)
   PUBMED   12949249
  REMARK    GeneRIF: CXCL11 displays antimicrobial activity against E. coli and
            S. aureus.
REFERENCE   7  (residues 1 to 94)
  AUTHORS   Xanthou,G., Duchesnes,C.E., Williams,T.J. and Pease,J.E.
  TITLE     CCR3 functional responses are regulated by both CXCR3 and its
            ligands CXCL9, CXCL10 and CXCL11
  JOURNAL   Eur J Immunol 33 (8), 2241-2250 (2003)
   PUBMED   12884299
  REMARK    GeneRIF: CXCR3 ligands inhibit CCR3-mediated functional responses
            of both human eosinophils and CCR3 transfectants induced by all
            three eotaxins, with CXCL11 being the most efficacious antagonist.
REFERENCE   8  (residues 1 to 94)
  AUTHORS   Basu,S., Schaefer,T.M., Ghosh,M., Fuller,C.L. and Reinhart,T.A.
  TITLE     Molecular cloning and sequencing of 25 different rhesus macaque
            chemokine cDNAs reveals evolutionary conservation among C, CC, CXC,
            AND CX3C families of chemokines
  JOURNAL   Cytokine 18 (3), 140-148 (2002)
   PUBMED   12126650
REFERENCE   9  (residues 1 to 94)
  AUTHORS   Tensen,C.P., Flier,J., Rampersad,S.S., Sampat-Sardjoepersad,S.,
            Scheper,R.J., Boorsma,D.M. and Willemze,R.
  TITLE     Genomic organization, sequence and transcriptional regulation of
            the human CXCL 11(1) gene
  JOURNAL   Biochim Biophys Acta 1446 (1-2), 167-172 (1999)
   PUBMED   10395932
REFERENCE   10 (residues 1 to 94)
  AUTHORS   Erdel,M., Laich,A., Utermann,G., Werner,E.R. and Werner-Felmayer,G.
  TITLE     The human gene encoding SCYB9B, a putative novel CXC chemokine,
            maps to human chromosome 4q21 like the closely related genes for
            MIG (SCYB9) and INP10 (SCYB10)
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 271-272 (1998)
   PUBMED   9730616
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP289021.1 and U66096.1.
            
            Summary: Chemokines are a group of small (approximately 8 to 14
            kD), mostly basic, structurally related molecules that regulate
            cell trafficking of various types of leukocytes through
            interactions with a subset of 7-transmembrane, G protein-coupled
            receptors. Chemokines also play fundamental roles in the
            development, homeostasis, and function of the immune system, and
            they have effects on cells of the central nervous system as well as
            on endothelial cells involved in angiogenesis or angiostasis.
            Chemokines are divided into 2 major subfamilies, CXC and CC. This
            antimicrobial gene is a CXC member of the chemokine superfamily.
            Its encoded protein induces a chemotactic response in activated
            T-cells and is the dominant ligand for CXC receptor-3. The gene
            encoding this protein contains 4 exons and at least three
            polyadenylation signals which might reflect cell-specific
            regulation of expression. IFN-gamma is a potent inducer of
            transcription of this gene. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U66096.1, BC110986.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000306621.8/
                                                  ENSP00000306884.3
            Protein has antimicrobial activity :: PMID: 12949249
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..94
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.1"
     Protein         1..94
                     /product="C-X-C motif chemokine 11 isoform 1 precursor"
                     /note="small inducible cytokine subfamily B (Cys-X-Cys),
                     member 11; chemokine (C-X-C motif) ligand 11; small
                     inducible cytokine subfamily B (Cys-X-Cys), member 9B;
                     C-X-C motif chemokine 11; small inducible cytokine B11;
                     beta-R1; interferon gamma-inducible protein 9;
                     interferon-inducible T-cell alpha chemoattractant"
                     /calculated_mol_wt=8307
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2076
     mat_peptide     22..94
                     /product="C-X-C motif chemokine 11 isoform 1"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     12949249]"
                     /calculated_mol_wt=8307
     Region          28..90
                     /region_name="Chemokine_CXC"
                     /note="1 of 4 subgroup designations based on the
                     arrangement of the two N-terminal cysteine residues;
                     includes a number of secreted growth factors and
                     interferons involved in mitogenic, chemotactic, and
                     inflammatory activity; many members contain an RCxC
                     motif...; cd00273"
                     /db_xref="CDD:238171"
     Site            order(28,31,45..46,49..51,61..64,66,71..72,75,82,86,
                     89..90)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            order(28..29,35,40..45,54..56,66..67,71..73,79,84)
                     /site_type="active"
                     /note="receptor binding site [active]"
                     /db_xref="CDD:238171"
     Site            order(28,31,49,51,61,63,66,71..72)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            order(29..30,32)
                     /site_type="active"
                     /note="RCXC motif [active]"
                     /db_xref="CDD:238171"
     Site            order(31..37,40..45)
                     /site_type="active"
                     /note="N-loop [active]"
                     /db_xref="CDD:238171"
     Site            order(33..34,36,40,44,63,66,71,73)
                     /site_type="active"
                     /note="receptor binding cleft [active]"
                     /db_xref="CDD:238171"
     Site            order(41,43,78,81,83..86,88)
                     /site_type="other"
                     /note="glycosaminoglycan (GAG) binding site [chemical
                     binding]"
                     /db_xref="CDD:238171"
     Site            order(43,46,65,67,71..72)
                     /site_type="other"
                     /note="putative glycosaminoglycan (GAG) binding site
                     [chemical binding]"
                     /db_xref="CDD:238171"
     Site            order(45..46,50,62,64,75,82,86,89..90)
                     /site_type="other"
                     /note="dimer interface (I form) [polypeptide binding]"
                     /db_xref="CDD:238171"
     Site            54..56
                     /site_type="other"
                     /note="30s-loop"
                     /db_xref="CDD:238171"
     Site            54..56
                     /site_type="other"
                     /note="GPH motif"
                     /db_xref="CDD:238171"
     Site            order(67,69..70)
                     /site_type="other"
                     /note="40s-loop"
                     /db_xref="CDD:238171"
     CDS             1..94
                     /gene="CXCL11"
                     /gene_synonym="b-R1; H174; I-TAC; IP-9; IP9; SCYB11;
                     SCYB9B"
                     /coded_by="NM_005409.5:84..368"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3574.1"
                     /db_xref="GeneID:6373"
                     /db_xref="HGNC:HGNC:10638"
                     /db_xref="MIM:604852"
ORIGIN      
        1 msvkgmaial avilcatvvq gfpmfkrgrc lcigpgvkav kvadiekasi mypsnncdki
       61 eviitlkenk gqrclnpksk qarliikkve rknf
//
LOCUS       NP_002790                277 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-7 precursor [Homo sapiens].
ACCESSION   NP_002790
VERSION     NP_002790.1
DBSOURCE    REFSEQ: accession NM_002799.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Hisamatsu,H., Shimbara,N., Saito,Y., Kristensen,P., Hendil,K.B.,
            Fujiwara,T., Takahashi,E., Tanahashi,N., Tamura,T., Ichihara,A. and
            Tanaka,K.
  TITLE     Newly identified pair of proteasomal subunits regulated
            reciprocally by interferon gamma
  JOURNAL   J Exp Med 183 (4), 1807-1816 (1996)
   PUBMED   8666937
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from GU727627.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. The
            encoded protein is a member of the proteasome B-type family, also
            known as the T1B family, and is a 20S core beta subunit in the
            proteasome. Expression of this catalytic subunit is downregulated
            by gamma interferon, and proteolytic processing is required to
            generate a mature subunit. A pseudogene of this gene is located on
            the long arm of chromosome 14. [provided by RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GU727627.1, SRR5189652.206633.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259457.8/ ENSP00000259457.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..277
                     /product="proteasome subunit beta type-7 precursor"
                     /EC_number="3.4.25.1"
                     /note="proteasome catalytic subunit 2; macropain chain Z;
                     proteasome subunit beta 7; proteasome subunit beta2;
                     proteasome subunit alpha; multicatalytic endopeptidase
                     complex chain Z; protein serine kinase c17; proteasome
                     subunit Z; proteasome subunit beta type-7; proteasome
                     (prosome, macropain) subunit, beta type, 7; epididymis
                     secretory sperm binding protein; beta-2; proteasome
                     subunit beta-2"
                     /calculated_mol_wt=29834
     mat_peptide     44..277
                     /product="Proteasome subunit beta type-7.
                     /id=PRO_0000026646"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99436.1)"
                     /calculated_mol_wt=25295
     Region          44..232
                     /region_name="proteasome_beta_type_7"
                     /note="proteasome beta type-7 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03763"
                     /db_xref="CDD:239732"
     Site            order(44,60,62,76,172,209,212..213)
                     /site_type="active"
                     /db_xref="CDD:239732"
     Site            order(62,65,67..72,92,94,109,121,124..125,127..128,131,
                     134,157,159,161..164,167,175..176,178..179,182..184,200,
                     207..210,213..214)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239732"
     Region          235..271
                     /region_name="Pr_beta_C"
                     /note="Proteasome beta subunits C terminal; pfam12465"
                     /db_xref="CDD:463597"
     CDS             1..277
                     /gene="PSMB7"
                     /coded_by="NM_002799.4:18..851"
                     /db_xref="CCDS:CCDS6855.1"
                     /db_xref="GeneID:5695"
                     /db_xref="HGNC:HGNC:9544"
                     /db_xref="MIM:604030"
ORIGIN      
        1 maavsvyapp vggfsfdncr rnavleadfa krgyklpkvr ktgttiagvv ykdgivlgad
       61 trategmvva dkncskihfi spniyccgag taadtdmttq lissnlelhs lstgrlprvv
      121 tanrmlkqml fryqgyigaa lvlggvdvtg phlysiyphg stdklpyvtm gsgslaamav
      181 fedkfrpdme eeeaknlvse aiaagifndl gsgsnidlcv isknkldflr pytvpnkkgt
      241 rlgryrcekg ttavltekit pleievleet vqtmdts
//
LOCUS       NP_002940                198 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein bL12m [Homo sapiens].
ACCESSION   NP_002940
VERSION     NP_002940.2
DBSOURCE    REFSEQ: accession NM_002949.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Rai,A.K., Sanghvi,S., Muthukumaran,N.S., Chandrasekera,D.,
            Kadam,A., Kishore,J., Kyriazis,I.D., Tomar,D., Ponnalagu,D.,
            Shettigar,V., Khan,M., Singh,H., Goukassian,D., Katare,R. and
            Garikipati,V.N.S.
  TITLE     Role of mitochondrial ribosomal protein L7/L12 (MRPL12) in diabetic
            ischemic heart disease
  JOURNAL   Free Radic Biol Med 222, 531-538 (2024)
   PUBMED   38977138
  REMARK    GeneRIF: Role of mitochondrial ribosomal protein L7/L12 (MRPL12) in
            diabetic ischemic heart disease.
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Paluch,K.V., Platz,K.R., Rudisel,E.J., Erdmann,R.R., Laurin,T.R.
            and Dittenhafer-Reed,K.E.
  TITLE     The role of lysine acetylation in the function of mitochondrial
            ribosomal protein L12
  JOURNAL   Proteins 92 (5), 583-592 (2024)
   PUBMED   38146092
  REMARK    GeneRIF: The role of lysine acetylation in the function of
            mitochondrial ribosomal protein L12.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Sun,Y., Liu,Y., Wang,P., Chang,L. and Huang,J.
  TITLE     The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma Tumorigenesis
            by Destabilizing MRPL12
  JOURNAL   Mol Biotechnol 66 (5), 1051-1061 (2024)
   PUBMED   38129673
  REMARK    GeneRIF: The m6A Reader YTHDC2 Suppresses Lung Adenocarcinoma
            Tumorigenesis by Destabilizing MRPL12.
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Ji,X., Yang,Z., Li,C., Zhu,S., Zhang,Y., Xue,F., Sun,S., Fu,T.,
            Ding,C., Liu,Y. and Wan,Q.
  TITLE     Mitochondrial ribosomal protein L12 potentiates hepatocellular
            carcinoma by regulating mitochondrial biogenesis and metabolic
            reprogramming
  JOURNAL   Metabolism 152, 155761 (2024)
   PUBMED   38104924
  REMARK    GeneRIF: Mitochondrial ribosomal protein L12 potentiates
            hepatocellular carcinoma by regulating mitochondrial biogenesis and
            metabolic reprogramming.
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Graack,H.R., Bryant,M.L. and O'Brien,T.W.
  TITLE     Identification of mammalian mitochondrial ribosomal proteins (MRPs)
            by N-terminal sequencing of purified bovine MRPs and comparison to
            data bank sequences: the large subribosomal particle
  JOURNAL   Biochemistry 38 (50), 16569-16577 (1999)
   PUBMED   10600119
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Marty,L., Taviaux,S. and Fort,P.
  TITLE     Expression and human chromosomal localization to 17q25 of the
            growth-regulated gene encoding the mitochondrial ribosomal protein
            MRPL12
  JOURNAL   Genomics 41 (3), 453-457 (1997)
   PUBMED   9169145
REFERENCE   10 (residues 1 to 198)
  AUTHORS   Marty,L. and Fort,P.
  TITLE     A delayed-early response nuclear gene encoding MRPL12, the
            mitochondrial homologue to the bacterial translational regulator
            L7/L12 protein
  JOURNAL   J Biol Chem 271 (19), 11468-11476 (1996)
   PUBMED   8626705
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139530.3, DA648796.1,
            BC002344.2 and AF105278.1.
            
            On Dec 31, 2002 this sequence version replaced NP_002940.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein which forms
            homodimers. In prokaryotic ribosomes, two L7/L12 dimers and one L10
            protein form the L8 protein complex. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.348680.1,
                                           SRR1803613.225094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000333676.8/
                                                  ENSP00000333837.3
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..198
                     /product="large ribosomal subunit protein bL12m"
                     /note="39S ribosomal protein L12, mitochondrial; MRP-L12;
                     mitochondrial large ribosomal subunit protein bL12m"
                     /calculated_mol_wt=21217
     Region          63..198
                     /region_name="RplL"
                     /note="Ribosomal protein L7/L12 [Translation, ribosomal
                     structure and biogenesis]; COG0222"
                     /db_xref="CDD:439992"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            138
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DB15; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            150
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            163
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            178
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:38146092; propagated from
                     UniProtKB/Swiss-Prot (P52815.2)"
     CDS             1..198
                     /gene="MRPL12"
                     /gene_synonym="5c5-2; bL12m; L12mt; MRP-L31/34; MRPL7;
                     MRPL7/L12; RPML12"
                     /coded_by="NM_002949.4:136..732"
                     /db_xref="CCDS:CCDS11785.1"
                     /db_xref="GeneID:6182"
                     /db_xref="HGNC:HGNC:10378"
                     /db_xref="MIM:602375"
ORIGIN      
        1 mlpaaarplw gpclglraaa frlarrqvpc vcavrhmrss ghqrcealag apldnapkey
       61 ppkiqqlvqd iasltlleis dlnellkktl kiqdvglvpm ggvmsgavpa aaaqeaveed
      121 ipiakerthf tvrlteakpv dkvklikeik nyiqginlvq akklveslpq eikanvakae
      181 aekikaalea vggtvvle
//
LOCUS       NP_001265248             439 aa            linear   PRI 20-NOV-2025
DEFINITION  leukocyte immunoglobulin-like receptor subfamily A member 1 isoform
            3 precursor [Homo sapiens].
ACCESSION   NP_001265248
VERSION     NP_001265248.1
DBSOURCE    REFSEQ: accession NM_001278319.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 439)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 439)
  AUTHORS   Wang,K.S., Liu,X., Aragam,N., Mullersman,J.E., Jian,X., Pan,Y. and
            Liu,Y.
  TITLE     Polymorphisms in ABLIM1 are associated with personality traits and
            alcohol dependence
  JOURNAL   J Mol Neurosci 46 (2), 265-271 (2012)
   PUBMED   21547531
REFERENCE   3  (residues 1 to 439)
  AUTHORS   Ryu,M., Chen,Y., Qi,J., Liu,J., Fan,Z., Nam,G., Shi,Y., Cheng,H.
            and Gao,G.F.
  TITLE     LILRA3 binds both classical and non-classical HLA class I molecules
            but with reduced affinities compared to LILRB1/LILRB2: structural
            evidence
  JOURNAL   PLoS One 6 (4), e19245 (2011)
   PUBMED   21559424
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 439)
  AUTHORS   Tedla,N., An,H., Borges,L., Vollmer-Conna,U., Bryant,K., Geczy,C.
            and McNeil,H.P.
  TITLE     Expression of activating and inhibitory leukocyte
            immunoglobulin-like receptors in rheumatoid synovium: correlations
            to disease activity
  JOURNAL   Tissue Antigens 77 (4), 305-316 (2011)
   PUBMED   21388353
REFERENCE   5  (residues 1 to 439)
  AUTHORS   Jones,D.C., Kosmoliaptsis,V., Apps,R., Lapaque,N., Smith,I.,
            Kono,A., Chang,C., Boyle,L.H., Taylor,C.J., Trowsdale,J. and
            Allen,R.L.
  TITLE     HLA class I allelic sequence and conformation regulate leukocyte
            Ig-like receptor binding
  JOURNAL   J Immunol 186 (5), 2990-2997 (2011)
   PUBMED   21270408
REFERENCE   6  (residues 1 to 439)
  AUTHORS   Brown,D., Trowsdale,J. and Allen,R.
  TITLE     The LILR family: modulators of innate and adaptive immune pathways
            in health and disease
  JOURNAL   Tissue Antigens 64 (3), 215-225 (2004)
   PUBMED   15304001
  REMARK    Review article
REFERENCE   7  (residues 1 to 439)
  AUTHORS   Allen,R.L., Raine,T., Haude,A., Trowsdale,J. and Wilson,M.J.
  TITLE     Leukocyte receptor complex-encoded immunomodulatory receptors show
            differing specificity for alternative HLA-B27 structures
  JOURNAL   J Immunol 167 (10), 5543-5547 (2001)
   PUBMED   11698424
REFERENCE   8  (residues 1 to 439)
  AUTHORS   Liu,W.R., Kim,J., Nwankwo,C., Ashworth,L.K. and Arm,J.P.
  TITLE     Genomic organization of the human leukocyte immunoglobulin-like
            receptors within the leukocyte receptor complex on chromosome
            19q13.4
  JOURNAL   Immunogenetics 51 (8-9), 659-669 (2000)
   PUBMED   10941837
REFERENCE   9  (residues 1 to 439)
  AUTHORS   Wilson,M.J., Torkar,M., Haude,A., Milne,S., Jones,T., Sheer,D.,
            Beck,S. and Trowsdale,J.
  TITLE     Plasticity in the organization and sequences of human KIR/ILT gene
            families
  JOURNAL   Proc Natl Acad Sci U S A 97 (9), 4778-4783 (2000)
   PUBMED   10781084
REFERENCE   10 (residues 1 to 439)
  AUTHORS   Borges,L., Hsu,M.L., Fanger,N., Kubin,M. and Cosman,D.
  TITLE     A family of human lymphoid and myeloid Ig-like receptors, some of
            which bind to MHC class I molecules
  JOURNAL   J Immunol 159 (11), 5192-5196 (1997)
   PUBMED   9548455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF025530.1, EU915602.1,
            BC063009.1 and BC032238.1.
            
            Summary: This gene encodes an activating member of the leukocyte
            immunoglobulin-like receptor (LIR) family, which is found in a gene
            cluster at chromosomal region 19q13.4. The encoded protein is
            predominantly expressed in B cells, interacts with major
            histocompatibility complex class I ligands, and contributes to the
            regulation of immune responses. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (3) has a shorter 5' UTR, lacks
            several exons and its 3'-terminal exon extends past a splice site
            that is used in variant 1. The encoded isoform (3) has a shorter
            and distinct C-terminus, compared to isoform 1. Isoform 3 lacks the
            transmembrane domain found in isoform 1 and is suspected to be
            soluble (PMID: 19658091).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU915602.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..439
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..439
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     A member 1 isoform 3 precursor"
                     /note="leukocyte immunoglobulin-like receptor 6; CD85
                     antigen-like family member I; leukocyte
                     immunoglobulin-like receptor, subfamily A (with TM
                     domain), member 1; leucocyte Ig-like receptor A1;
                     leukocyte immunoglobulin-like receptor subfamily A member
                     1"
                     /calculated_mol_wt=45418
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2519
     Region          28..118
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,107)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          111..118
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          124..219
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          153..157
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          180..184
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          212..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          225..318
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          242..246
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          254..258
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          280..284
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          294..299
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          311..314
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          325..419
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          342..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          354..358
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          380..384
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          394..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          412..415
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     CDS             1..439
                     /gene="LILRA1"
                     /gene_synonym="CD85I; LIR-6; LIR6"
                     /coded_by="NM_001278319.1:49..1368"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:11024"
                     /db_xref="HGNC:HGNC:6602"
                     /db_xref="MIM:604810"
ORIGIN      
        1 mtpivtvlic lrlslgprth vqagtlpkpt lwaepgsvit qgspvtlwcq giletqeyrl
       61 yrekktapwi tripqeivkk gqfpipsitw ehtgryrcfy gshtagwsep sdplelvvtg
      121 ayikptlsal pspvvtsggn vtlhcvsqva fgsfilckeg edehpqclns qprthgwsra
      181 ifsvgpvsps rrwsyrcyay dsnsphvwsl psdllellvl gvskkpslsv qpgpivapge
      241 sltlqcvsdv sydrfvlyke gerdflqlpg pqpqaglsqa nftlgpvsrs yggqyrcsga
      301 ynlssewsap sdpldiliag qfrgrpfisv hpgptvasge nvtllcqswg pfhtflltka
      361 gaadaplrlr siheypkyqa efpmspvtsa hsgtyrcygs lssnpyllsh psdslelmvs
      421 gaaetlsppq nksdskage
//
LOCUS       NP_001171645             221 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 6 isoform 4 precursor [Homo sapiens].
ACCESSION   NP_001171645
VERSION     NP_001171645.1
DBSOURCE    REFSEQ: accession NM_001184716.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Oba,T., Long,M.D., Ito,K.I. and Ito,F.
  TITLE     Clinical and immunological relevance of SLAMF6 expression in the
            tumor microenvironment of breast cancer and melanoma
  JOURNAL   Sci Rep 14 (1), 2394 (2024)
   PUBMED   38287061
  REMARK    GeneRIF: Clinical and immunological relevance of SLAMF6 expression
            in the tumor microenvironment of breast cancer and melanoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Xia,G., Li,Y., Pan,W., Qian,C., Ma,L., Zhou,J., Xu,H. and Cheng,C.
  TITLE     SLAMF6 is associated with the susceptibility and severity of
            rheumatoid arthritis in the Chinese population
  JOURNAL   J Orthop Surg Res 17 (1), 13 (2022)
   PUBMED   35016729
  REMARK    GeneRIF: SLAMF6 is associated with the susceptibility and severity
            of rheumatoid arthritis in the Chinese population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Liu,B., Zeng,L., Shao,Y. and Fu,R.
  TITLE     Expression and function of SLAMF6 in CD8+ T lymphocytes of patients
            with severe aplastic anemia
  JOURNAL   Cell Immunol 364, 104343 (2021)
   PUBMED   33774556
  REMARK    GeneRIF: Expression and function of SLAMF6 in CD8(+) T lymphocytes
            of patients with severe aplastic anemia.
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Fraser,C.C., Howie,D., Morra,M., Qiu,Y., Murphy,C., Shen,Q.,
            Gutierrez-Ramos,J.C., Coyle,A., Kingsbury,G.A. and Terhorst,C.
  TITLE     Identification and characterization of SF2000 and SF2001, two new
            members of the immune receptor SLAM/CD2 family
  JOURNAL   Immunogenetics 53 (10-11), 843-850 (2002)
   PUBMED   11862385
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Bottino,C., Falco,M., Parolini,S., Marcenaro,E., Augugliaro,R.,
            Sivori,S., Landi,E., Biassoni,R., Notarangelo,L.D., Moretta,L. and
            Moretta,A.
  TITLE     NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface
            molecule contributing to the inability of natural killer cells to
            kill Epstein-Barr virus-infected B cells in X-linked
            lymphoproliferative disease
  JOURNAL   J Exp Med 194 (3), 235-246 (2001)
   PUBMED   11489943
  REMARK    Erratum:[J Exp Med 2001 Sep 3;194(5):following 703]
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Lee,Y.J., Luisiri,P. and Clark,M.R.
  TITLE     A novel complex, p40/42, is constitutively associated with the B
            cell antigen receptor and phosphorylated upon receptor stimulation
  JOURNAL   J Immunol 157 (9), 3828-3837 (1996)
   PUBMED   8892612
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Kong,G., Dalton,M., Bubeck Wardenburg,J., Straus,D., Kurosaki,T.
            and Chan,A.C.
  TITLE     Distinct tyrosine phosphorylation sites in ZAP-70 mediate
            activation and negative regulation of antigen receptor function
  JOURNAL   Mol Cell Biol 16 (9), 5026-5035 (1996)
   PUBMED   8756661
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Hercend,T., Meuer,S., Brennan,A., Edson,M.A., Acuto,O.,
            Reinherz,E.L., Schlossman,S.F. and Ritz,J.
  TITLE     Natural killer-like function of activated T lymphocytes:
            differential blocking effects of monoclonal antibodies specific for
            a 90-kDa clonotypic structure
  JOURNAL   Cell Immunol 86 (2), 381-392 (1984)
   PUBMED   6610481
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB197632.1, AK301026.1,
            AW402723.1 and AK125624.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein, belonging to the CD2 subfamily of the immunoglobulin
            superfamily. This encoded protein is expressed on Natural killer
            (NK), T, and B lymphocytes. It undergoes tyrosine phosphorylation
            and associates with the Src homology 2 domain-containing protein
            (SH2D1A) as well as with SH2 domain-containing phosphatases (SHPs).
            It functions as a coreceptor in the process of NK cell activation.
            It can also mediate inhibitory signals in NK cells from X-linked
            lymphoproliferative patients. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms.[provided
            by RefSeq, May 2010].
            
            Transcript Variant: This variant (4) lacks an alternate exon in the
            5' coding region, compared to variant 1, which result in an isoform
            (4) with a shorter extracellular domain than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301026.1, BI834685.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2-q23.3"
     Protein         1..221
                     /product="SLAM family member 6 isoform 4 precursor"
                     /note="activating NK receptor; natural killer-, T- and
                     B-cell antigen; NTBA receptor; NK-T-B-antigen"
                     /calculated_mol_wt=22748
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2247
     mat_peptide     20..221
                     /product="SLAM family member 6 isoform 4"
                     /calculated_mol_wt=22748
     Region          <38..96
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          52..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          77..80
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..86
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..221
                     /gene="SLAMF6"
                     /gene_synonym="CD352; KALI; KALIb; Ly108; NTB-A; NTBA;
                     SF2000"
                     /coded_by="NM_001184716.2:64..729"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS53393.1"
                     /db_xref="GeneID:114836"
                     /db_xref="HGNC:HGNC:21392"
                     /db_xref="MIM:606446"
ORIGIN      
        1 mlwlfqsllf vfcfgpgqlr niqvtnhsql fqnmtcelhl tcsvedaddn vsfrwealgn
       61 tlssqpnltv swdprisseq dytciaenav snlsfsvsaq klcedvkiqy tdtkmilfmv
      121 sgicivfgfi illllvlrkr rdslslstqr tqgpaesarn leyvsvsptn ntvyasvths
      181 nreteiwtpr endtitiyst inhskeskpt fsrataldnv v
//
LOCUS       NP_001184222             677 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydropyrimidinase-related protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001184222
VERSION     NP_001184222.1
DBSOURCE    REFSEQ: accession NM_001197293.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Li,S., Guo,Y., Takahashi,M., Suzuki,H., Kosaki,K. and Ohshima,T.
  TITLE     Forebrain commissure formation in zebrafish embryo requires the
            binding of KLC1 to CRMP2
  JOURNAL   Dev Neurobiol 84 (3), 203-216 (2024)
   PUBMED   38830696
  REMARK    GeneRIF: Forebrain commissure formation in zebrafish embryo
            requires the binding of KLC1 to CRMP2.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Kurita,H., Ueda,M., Kimura,M., Okuda,A., Ohuchi,K., Hozumi,I. and
            Inden,M.
  TITLE     Zinc Deficiency Decreases Neurite Extension via CRMP2 Signal
            Pathway
  JOURNAL   Biol Pharm Bull 47 (4), 796-800 (2024)
   PUBMED   38583951
  REMARK    GeneRIF: Zinc Deficiency Decreases Neurite Extension via CRMP2
            Signal Pathway.
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Feuer,K.L., Peng,X., Yovo,C.K. and Avramopoulos,D.
  TITLE     DPYSL2/CRMP2 isoform B knockout in human iPSC-derived glutamatergic
            neurons confirms its role in mTOR signaling and neurodevelopmental
            disorders
  JOURNAL   Mol Psychiatry 28 (10), 4353-4362 (2023)
   PUBMED   37479784
  REMARK    GeneRIF: DPYSL2/CRMP2 isoform B knockout in human iPSC-derived
            glutamatergic neurons confirms its role in mTOR signaling and
            neurodevelopmental disorders.
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Soutar,M.P., Thornhill,P., Cole,A.R. and Sutherland,C.
  TITLE     Increased CRMP2 phosphorylation is observed in Alzheimer's disease;
            does this tell us anything about disease development?
  JOURNAL   Curr Alzheimer Res 6 (3), 269-278 (2009)
   PUBMED   19519308
  REMARK    Review article
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Gu,Y. and Ihara,Y.
  TITLE     Evidence that collapsin response mediator protein-2 is involved in
            the dynamics of microtubules
  JOURNAL   J Biol Chem 275 (24), 17917-17920 (2000)
   PUBMED   10770920
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Gu,Y., Hamajima,N. and Ihara,Y.
  TITLE     Neurofibrillary tangle-associated collapsin response mediator
            protein-2 (CRMP-2) is highly phosphorylated on Thr-509, Ser-518,
            and Ser-522
  JOURNAL   Biochemistry 39 (15), 4267-4275 (2000)
   PUBMED   10757975
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Kitamura,K., Takayama,M., Hamajima,N., Nakanishi,M., Sasaki,M.,
            Endo,Y., Takemoto,T., Kimura,H., Iwaki,M. and Nonaka,M.
  TITLE     Characterization of the human dihydropyrimidinase-related protein 2
            (DRP-2) gene
  JOURNAL   DNA Res 6 (5), 291-297 (1999)
   PUBMED   10574455
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Hamajima,N., Matsuda,K., Sakata,S., Tamaki,N., Sasaki,M. and
            Nonaka,M.
  TITLE     A novel gene family defined by human dihydropyrimidinase and three
            related proteins with differential tissue distribution
  JOURNAL   Gene 180 (1-2), 157-163 (1996)
   PUBMED   8973361
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Goshima,Y., Nakamura,F., Strittmatter,P. and Strittmatter,S.M.
  TITLE     Collapsin-induced growth cone collapse mediated by an intracellular
            protein related to UNC-33
  JOURNAL   Nature 376 (6540), 509-514 (1995)
   PUBMED   7637782
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015743.9, DA649686.1,
            AB209195.1, BX463316.2, BC056408.1 and AC015564.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the collapsin response
            mediator protein family. Collapsin response mediator proteins form
            homo- and hetero-tetramers and facilitate neuron guidance, growth
            and polarity. The encoded protein promotes microtubule assembly and
            is required for Sema3A-mediated growth cone collapse, and also
            plays a role in synaptic signaling through interactions with
            calcium channels. This gene has been implicated in multiple
            neurological disorders, and hyperphosphorylation of the encoded
            protein may play a key role in the development of Alzheimer's
            disease. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.100680.1,
                                           SRR1660803.227283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521913.7/ ENSP00000427985.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..677
                     /product="dihydropyrimidinase-related protein 2 isoform 1"
                     /note="dihydropyrimidinase-related protein 2; collapsin
                     response mediator protein hCRMP-2; unc-33-like
                     phosphoprotein 2"
                     /calculated_mol_wt=73372
     Region          122..571
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(133..134,136,149..150,285,306,309,312,335,339,343,
                     346,373..374,376..377,495,500,505)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(178,180,270,303,359,437)
                     /site_type="active"
                     /db_xref="CDD:238639"
     CDS             1..677
                     /gene="DPYSL2"
                     /gene_synonym="CRMP-2; CRMP2; DHPRP2; DRP-2; DRP2; N2A3;
                     ULIP-2; ULIP2"
                     /coded_by="NM_001197293.3:296..2329"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS83268.1"
                     /db_xref="GeneID:1808"
                     /db_xref="HGNC:HGNC:3014"
                     /db_xref="MIM:602463"
ORIGIN      
        1 maerkqsgka aedeevpaff knlgsgspkp rqkfcgmfcp vegssenkti dfdslsvgrg
       61 sgqvvaqqrd vahlgpdpqp pysrqgrrag gepsvesgrk veirrasgke alqnindqsd
      121 rllikggkiv nddqsfyadi ymedglikqi genlivpggv ktieahsrmv ipggidvhtr
      181 fqmpdqgmts addffqgtka alaggttmii dhvvpepgts llaafdqwre wadsksccdy
      241 slhvdisewh kgiqeemeal vkdhgvnsfl vymafkdrfq ltdcqiyevl svirdigaia
      301 qvhaengdii aeeqqrildl gitgpeghvl srpeeveaea vnraitianq tncplyitkv
      361 mskssaevia qarkkgtvvy gepitaslgt dgshywsknw akaaafvtsp plspdpttpd
      421 flnsllscgd lqvtgsahct fntaqkavgk dnftlipegt ngteermsvi wdkavvtgkm
      481 denqfvavts tnaakvfnly prkgriavgs dadlviwdpd svktisakth nssleynife
      541 gmecrgsplv visqgkivle dgtlhvtegs gryiprkpfp dfvykrikar srlaelrgvp
      601 rglydgpvce vsvtpktvtp assaktspak qqappvrnlh qsgfslsgaq iddniprrtt
      661 qrivappggr anitslg
//
LOCUS       NP_950238                268 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel regulatory subunit beta-1 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_950238 XP_001130615
VERSION     NP_950238.1
DBSOURCE    REFSEQ: accession NM_199037.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Popa-Fotea,N.M., Oprescu,N., Scafa-Udriste,A. and Micheu,M.M.
  TITLE     Impact of rs1805127 and rs55742440 Variants on Atrial Remodeling in
            Hypertrophic Cardiomyopathy Patients with Atrial Fibrillation: A
            Romanian Cohort Study
  JOURNAL   Int J Mol Sci 24 (24), 17244 (2023)
   PUBMED   38139087
  REMARK    GeneRIF: Impact of rs1805127 and rs55742440 Variants on Atrial
            Remodeling in Hypertrophic Cardiomyopathy Patients with Atrial
            Fibrillation: A Romanian Cohort Study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Li,Y., Yuan,T., Huang,B., Zhou,F., Peng,C., Li,X., Qiu,Y., Yang,B.,
            Zhao,Y., Huang,Z. and Jiang,D.
  TITLE     Structure of human NaV1.6 channel reveals Na+ selectivity and pore
            blockade by 4,9-anhydro-tetrodotoxin
  JOURNAL   Nat Commun 14 (1), 1030 (2023)
   PUBMED   36823201
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Fan,X., Huang,J., Jin,X. and Yan,N.
  TITLE     Cryo-EM structure of human voltage-gated sodium channel Nav1.6
  JOURNAL   Proc Natl Acad Sci U S A 120 (5), e2220578120 (2023)
   PUBMED   36696443
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Alghamdi,M.A., Al-Eitan,L.N., Asiri,A., Rababa'h,D.M.,
            Alqahtani,S.A., Aldarami,M.S., Alsaeedi,M.A., Almuidh,R.S.,
            Alzahrani,A.A., Sakah,A.H., El Nashar,E.M., Otaif,M.Y. and Abdel
            Ghaffar,N.F.
  TITLE     Association of sodium voltage-gated channel genes polymorphisms
            with epilepsy risk and prognosis in the Saudi population
  JOURNAL   Ann Med 54 (1), 1938-1951 (2022)
   PUBMED   35801810
  REMARK    GeneRIF: Association of sodium voltage-gated channel genes
            polymorphisms with epilepsy risk and prognosis in the Saudi
            population.
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Qin,N., D'Andrea,M.R., Lubin,M.L., Shafaee,N., Codd,E.E. and
            Correa,A.M.
  TITLE     Molecular cloning and functional expression of the human sodium
            channel beta1B subunit, a novel splicing variant of the beta1
            subunit
  JOURNAL   Eur J Biochem 270 (23), 4762-4770 (2003)
   PUBMED   14622265
  REMARK    GeneRIF: identification and characterization of a novel splicing
            variant; functional studies in oocytes demonstrate that the beta1B
            subunit increases the ionic current when coexpressed with the
            tetrodotoxin sensitive channel, NaV1.2
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Makita,N., Sloan-Brown,K., Weghuis,D.O., Ropers,H.H. and
            George,A.L. Jr.
  TITLE     Genomic organization and chromosomal assignment of the human
            voltage-gated Na+ channel beta 1 subunit gene (SCN1B)
  JOURNAL   Genomics 23 (3), 628-634 (1994)
   PUBMED   7851891
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Makita,N., Bennett,P.B. Jr. and George,A.L. Jr.
  TITLE     Voltage-gated Na+ channel beta 1 subunit mRNA expressed in adult
            human skeletal muscle, heart, and brain is encoded by a single gene
  JOURNAL   J Biol Chem 269 (10), 7571-7578 (1994)
   PUBMED   8125980
REFERENCE   8  (residues 1 to 268)
  AUTHORS   McClatchey,A.I., Cannon,S.C., Slaugenhaupt,S.A. and Gusella,J.F.
  TITLE     The cloning and expression of a sodium channel beta 1-subunit cDNA
            from human brain
  JOURNAL   Hum Mol Genet 2 (6), 745-749 (1993)
   PUBMED   8394762
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Hartshorne,R.P. and Catterall,W.A.
  TITLE     The sodium channel from rat brain. Purification and subunit
            composition
  JOURNAL   J Biol Chem 259 (3), 1667-1675 (1984)
   PUBMED   6319405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020907.6, BC067122.1 and
            AY391842.1.
            
            On Sep 20, 2006 this sequence version replaced XP_001130615.1.
            
            Summary: Voltage-gated sodium channels are heteromeric proteins
            that function in the generation and propagation of action
            potentials in muscle and neuronal cells. They are composed of one
            alpha and two beta subunits, where the alpha subunit provides
            channel activity and the beta-1 subunit modulates the kinetics of
            channel inactivation. This gene encodes a sodium channel beta-1
            subunit. Mutations in this gene result in generalized epilepsy with
            febrile seizures plus, Brugada syndrome 5, and defects in cardiac
            conduction. Multiple transcript variants encoding different
            isoforms have been found for this gene.[provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (b) differs in the 3' UTR and
            coding region compared to variant a. The resulting isoform (b) is
            longer and has a distinct C-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.2638.1,
                                           SRR1660807.237760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..268
                     /product="sodium channel regulatory subunit beta-1 isoform
                     b precursor"
                     /note="sodium channel subunit beta-1; sodium channel,
                     voltage-gated, type I, beta; sodium channel, voltage
                     gated, type I beta subunit; sodium channel regulatory
                     subunit beta-1"
                     /calculated_mol_wt=28670
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1788
     Region          23..147
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     CDS             1..268
                     /gene="SCN1B"
                     /gene_synonym="ATFB13; BRGDA5; DEE52; EIEE52; GEFSP1"
                     /coded_by="NM_199037.5:352..1158"
                     /note="isoform b precursor is encoded by transcript
                     variant b"
                     /db_xref="CCDS:CCDS46047.1"
                     /db_xref="GeneID:6324"
                     /db_xref="HGNC:HGNC:10586"
                     /db_xref="MIM:600235"
ORIGIN      
        1 mgrllalvvg aalvssacgg cvevdsetea vygmtfkilc isckrrsetn aetftewtfr
       61 qkgteefvki lryenevlql eederfegrv vwngsrgtkd lqdlsifitn vtynhsgdye
      121 chvyrllffe nyehntsvvk kihievvdkg esgaacpftv thrrarwrdr wqavdrtgwl
      181 cawpanrpqq raegegssps cplqlwplfl ssprrgqsmp vphrrsgyrt qlchlccmts
      241 grcllslsqr vvlglpgiii rcvsrgvv
//
LOCUS       NP_001341512             215 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-12 subunit alpha isoform 3 [Homo sapiens].
ACCESSION   NP_001341512
VERSION     NP_001341512.1
DBSOURCE    REFSEQ: accession NM_001354583.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Gao,L., Xiong,Y.J., Liang,Y.X., Huang,P.F., Liu,S., Xiao,Y.,
            Huang,Q., Wang,H. and Wu,H.M.
  TITLE     The effects of IL-27 and IL-35 gene variation and expression levels
            on the susceptibility and clinical manifestations of pulmonary
            tuberculosis
  JOURNAL   Front Immunol 15, 1267624 (2024)
   PUBMED   38690286
  REMARK    GeneRIF: The effects of IL-27 and IL-35 gene variation and
            expression levels on the susceptibility and clinical manifestations
            of pulmonary tuberculosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Sun,H., Ge,Y., Liu,J., Li,Z., Li,H., Zhao,T., Wang,X., Feng,Y.,
            Wang,H., Gao,S., Shi,L., Yang,S., Sun,P., Chang,A., Hao,J. and
            Huang,C.
  TITLE     Tumor-derived interleukin 35 mediates the dissemination of
            gemcitabine resistance in pancreatic adenocarcinoma
  JOURNAL   Oncogene 43 (11), 776-788 (2024)
   PUBMED   38243080
  REMARK    GeneRIF: Tumor-derived interleukin 35 mediates the dissemination of
            gemcitabine resistance in pancreatic adenocarcinoma.
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Hourani,T., Eivazitork,M., Balendran,T., Mc Lee,K., Hamilton,J.A.,
            Zhu,H.J., Iaria,J., Morokoff,A.P., Luwor,R.B. and Achuthan,A.A.
  TITLE     Signaling pathways underlying TGF-beta mediated suppression of
            IL-12A gene expression in monocytes
  JOURNAL   Mol Immunol 166, 101-109 (2024)
   PUBMED   38278031
  REMARK    GeneRIF: Signaling pathways underlying TGF-beta mediated
            suppression of IL-12A gene expression in monocytes.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Zysk,W., Sitko,K., Tukaj,S., Zaryczanska,A. and Trzeciak,M.
  TITLE     Altered Gene Expression of IL-35 and IL-36alpha in the Skin of
            Patients with Atopic Dermatitis
  JOURNAL   Int J Mol Sci 25 (1), 404 (2023)
   PUBMED   38203575
  REMARK    GeneRIF: Altered Gene Expression of IL-35 and IL-36alpha in the
            Skin of Patients with Atopic Dermatitis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 215)
  AUTHORS   D'Andrea,A., Rengaraju,M., Valiante,N.M., Chehimi,J., Kubin,M.,
            Aste,M., Chan,S.H., Kobayashi,M., Young,D., Nickbarg,E. et al.
  TITLE     Production of natural killer cell stimulatory factor (interleukin
            12) by peripheral blood mononuclear cells
  JOURNAL   J Exp Med 176 (5), 1387-1398 (1992)
   PUBMED   1357073
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Sieburth,D., Jabs,E.W., Warrington,J.A., Li,X., Lasota,J.,
            LaForgia,S., Kelleher,K., Huebner,K., Wasmuth,J.J. and Wolf,S.F.
  TITLE     Assignment of genes encoding a unique cytokine (IL12) composed of
            two unrelated subunits to chromosomes 3 and 5
  JOURNAL   Genomics 14 (1), 59-62 (1992)
   PUBMED   1358798
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Schoenhaut,D.S., Chua,A.O., Wolitzky,A.G., Quinn,P.M., Dwyer,C.M.,
            McComas,W., Familletti,P.C., Gately,M.K. and Gubler,U.
  TITLE     Cloning and expression of murine IL-12
  JOURNAL   J Immunol 148 (11), 3433-3440 (1992)
   PUBMED   1350290
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Wolf,S.F., Temple,P.A., Kobayashi,M., Young,D., Dicig,M., Lowe,L.,
            Dzialo,R., Fitz,L., Ferenz,C., Hewick,R.M. et al.
  TITLE     Cloning of cDNA for natural killer cell stimulatory factor, a
            heterodimeric cytokine with multiple biologic effects on T and
            natural killer cells
  JOURNAL   J Immunol 146 (9), 3074-3081 (1991)
   PUBMED   1673147
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Stern,A.S., Podlaski,F.J., Hulmes,J.D., Pan,Y.C., Quinn,P.M.,
            Wolitzky,A.G., Familletti,P.C., Stremlo,D.L., Truitt,T.,
            Chizzonite,R. et al.
  TITLE     Purification to homogeneity and partial characterization of
            cytotoxic lymphocyte maturation factor from human B-lymphoblastoid
            cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (17), 6808-6812 (1990)
   PUBMED   2204066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010370.5.
            
            Summary: This gene encodes a subunit of a cytokine that acts on T
            and natural killer cells, and has a broad array of biological
            activities. The cytokine is a disulfide-linked heterodimer composed
            of the 35-kD subunit encoded by this gene, and a 40-kD subunit that
            is a member of the cytokine receptor family. This cytokine is
            required for the T-cell-independent induction of interferon
            (IFN)-gamma, and is important for the differentiation of both Th1
            and Th2 cells. The responses of lymphocytes to this cytokine are
            mediated by the activator of transcription protein STAT4. Nitric
            oxide synthase 2A (NOS2A/NOS2) is found to be required for the
            signaling process of this cytokine in innate immunity. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD013916.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.33"
     Protein         1..215
                     /product="interleukin-12 subunit alpha isoform 3"
                     /note="IL35 subunit; cytotoxic lymphocyte maturation
                     factor 1, p35; interleukin 12, p35; IL-12, subunit p35; NF
                     cell stimulatory factor chain 1; interleukin-12 alpha
                     chain; interleukin-12 subunit alpha; CLMF p35; NK cell
                     stimulatory factor chain 1; cytotoxic lymphocyte
                     maturation factor 35 kDa subunit; interleukin 12A (natural
                     killer cell stimulatory factor 1, cytotoxic lymphocyte
                     maturation factor 1, p35)"
                     /calculated_mol_wt=23824
     Region          51..215
                     /region_name="IL12"
                     /note="Interleukin-12 alpha subunit; pfam03039"
                     /db_xref="CDD:460785"
     CDS             1..215
                     /gene="IL12A"
                     /gene_synonym="CLMF; IL-12A; NFSK; NKSF1; P35"
                     /coded_by="NM_001354583.2:223..870"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:3592"
                     /db_xref="HGNC:HGNC:5969"
                     /db_xref="MIM:161560"
ORIGIN      
        1 mwppgsasqp ppspaaatgl hpaarpvslq crlsmcpars lllvatlvll dhlslarnlp
       61 vatpdpgmfp clhhsqnllr avsnmlqkne sclnsretsf itngsclasr ktsfmmalcl
      121 ssiyedlkmy qvefktmnak llmdpkrqif ldqnmlavid elmqalnfns etvpqkssle
      181 epdfyktkik lcillhafri ravtidrvms ylnas
//
LOCUS       NP_001357084             177 aa            linear   PRI 20-NOV-2025
DEFINITION  DPY30 domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001357084 XP_024303595
VERSION     NP_001357084.1
DBSOURCE    REFSEQ: accession NM_001370155.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Li,S., Qiao,Y., Di,Q., Le,X., Zhang,L., Zhang,X., Zhang,C.,
            Cheng,J., Zong,S., Koide,S.S., Miao,S. and Wang,L.
  TITLE     Interaction of SH3P13 and DYDC1 protein: a germ cell component that
            regulates acrosome biogenesis during spermiogenesis
  JOURNAL   Eur J Cell Biol 88 (9), 509-520 (2009)
   PUBMED   19545932
  REMARK    Erratum:[Eur J Cell Biol. 2019 Jan;98(1):51-52. doi:
            10.1016/j.ejcb.2018.11.002. PMID: 30497823]
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359195.24.
            
            On May 2, 2019 this sequence version replaced XP_024303595.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. The encoded protein is involved in
            acrosome formation during spermatid development. This gene locus
            overlaps with a closely related gene on the opposite strand.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longer isoform (a). Variants 1-4 all
            encode the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.163222.1,
                                           SRR5189667.317847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 1 isoform a"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=20762
     Region          2..43
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC1"
                     /gene_synonym="DPY30D1"
                     /coded_by="NM_001370155.1:413..946"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS7366.1"
                     /db_xref="GeneID:143241"
                     /db_xref="HGNC:HGNC:23460"
                     /db_xref="MIM:615154"
ORIGIN      
        1 mesiylqkhl gacltqglae varvrpvdpi eylalwiyky kenvtmeqlr qkemaklere
       61 relalmeqem merlkaeell lqqqqlalql elemqekerq riqelqraqe qlgkemrmnm
      121 enlvrnedil hseeatldsg ktlaeisdry gapnlsrvee ldepmfsdia lnidqdl
//
LOCUS       NP_001167446             531 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001167446
VERSION     NP_001167446.1
DBSOURCE    REFSEQ: accession NM_001173975.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Xu,X., Gao,F., Wang,J., Long,C., Tao,L., Ding,L. and Ji,Y.
  TITLE     microRNA-216a-5p inhibits the development of gastric cancer through
            target combination with TCTN1
  JOURNAL   Minerva Med 114 (3), 323-331 (2023)
   PUBMED   32486612
  REMARK    GeneRIF: microRNA-216a-5p inhibits the development of gastric
            cancer through target combination with TCTN1.
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Bai,G., Wei,N., Li,F., Zhao,P., Meng,Z., Zou,B., Liu,Y., Xu,K.,
            Li,K., Yao,C. and Yang,P.
  TITLE     Function and transcriptional regulation of TCTN1 in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 47 (2) (2022)
   PUBMED   34859261
  REMARK    GeneRIF: Function and transcriptional regulation of TCTN1 in oral
            squamous cell carcinoma.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Wang,H., Jiang,W., Dai,M., Xiao,B., Xu,Y., Sun,Y., Liu,Y., Ying,X.,
            Sun,Y., Wei,W. and Ji,X.
  TITLE     [Diagnosis of two cases from one family with Joubert syndrome
            caused by novel mutations of TCTN1 gene by whole exome sequencing]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 36 (7), 686-689 (2019)
   PUBMED   31302911
  REMARK    GeneRIF: Two novel TCTN1 mutations were identified in a family with
            Joubert syndrome
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Alazami,A.M., Alshammari,M.J., Salih,M.A., Alzahrani,F., Hijazi,H.,
            Seidahmed,M.Z., Abu Safieh,L., Aldosary,M., Khan,A.O. and
            Alkuraya,F.S.
  TITLE     Molecular characterization of Joubert syndrome in Saudi Arabia
  JOURNAL   Hum Mutat 33 (10), 1423-1428 (2012)
   PUBMED   22693042
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    GeneRIF: Mutations in Tctn1 is associated with ciliopathies.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295514.1, AK092775.1,
            CA419765.1 and AC144522.12.
            
            Summary: This gene encodes a member of a family of secreted and
            transmembrane proteins. The orthologous gene in mouse functions
            downstream of smoothened and rab23 to modulate hedgehog signal
            transduction. This protein is a component of the tectonic-like
            complex, which forms a barrier between the ciliary axoneme and the
            basal body. A mutation in this gene was found in a family with
            Joubert syndrome-13. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 5' region, initiates translation at an alternate start
            codon, and uses an alternate in-frame splice site in the 3' coding
            region, compared to variant 1. The resulting isoform (4) has a
            distinct N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092775.1, SRR1803611.98566.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..531
                     /product="tectonic-1 isoform 4"
                     /calculated_mol_wt=57887
     Region          22..331
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..531
                     /gene="TCTN1"
                     /gene_synonym="JBTS13; TECT1"
                     /coded_by="NM_001173975.3:284..1879"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:79600"
                     /db_xref="HGNC:HGNC:26113"
                     /db_xref="MIM:609863"
ORIGIN      
        1 mcqllestvi qpqgdspvav lcvcdlspaq cdincccdpd cssvdfsvfs acsvpvvtgd
       61 sqfcsqkavi yslnftanpp qrvfelvdqi npsifcihit nykpalsfin pevpdennfd
      121 tlmktsdgft lnaesyvsft tkldiptaak yeygvplqts dsflrfpssl tsslctdnnp
      181 aaflvnqavk ctrkinleqc eeiealsmaf ysspeilrvp dsrkkvpitv qsiviqslnk
      241 tltrredtdv lqptlvnagh fslcvnvvle vkysltytda gevtkadlsf vlgtvssvvv
      301 plqqkfeihf lqentqpvpl sgnpgyvvgl plaagfqphk gsgiiqttnr ygqltilhst
      361 teqdclaleg vrtpvlfgyt mqsgcklrlt galpcqlvaq kvksllwgqg fpdyvapfgn
      421 sqaqdmldwv pihfitqsfn rkdscqlpga lvievkwtky gsllnpqaki vnvtanliss
      481 sfpeansgne rtilistavt fvdvsapaea gfrappaina rlpfnfffpf v
//
LOCUS       NP_001171679             837 aa            linear   PRI 20-NOV-2025
DEFINITION  SLIT and NTRK-like protein 4 precursor [Homo sapiens].
ACCESSION   NP_001171679
VERSION     NP_001171679.1
DBSOURCE    REFSEQ: accession NM_001184750.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Kuo,F.C., Huang,Y.C., Yen,M.R., Lee,C.H., Hsu,K.F., Yang,H.Y.,
            Wu,L.W., Lu,C.H., Hsu,Y.J. and Chen,P.Y.
  TITLE     Aberrant overexpression of HOTAIR inhibits abdominal adipogenesis
            through remodelling of genome-wide DNA methylation and
            transcription
  JOURNAL   Mol Metab 60, 101473 (2022)
   PUBMED   35292404
  REMARK    GeneRIF: Aberrant overexpression of HOTAIR inhibits abdominal
            adipogenesis through remodelling of genome-wide DNA methylation and
            transcription.
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Yim,Y.S., Kwon,Y., Nam,J., Yoon,H.I., Lee,K., Kim,D.G., Kim,E.,
            Kim,C.H. and Ko,J.
  TITLE     Slitrks control excitatory and inhibitory synapse formation with
            LAR receptor protein tyrosine phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 110 (10), 4057-4062 (2013)
   PUBMED   23345436
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2024 Jun 18;121(25):e2410441121.
            doi: 10.1073/pnas.2410441121. PMID: 38870062]
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Haakensen,V.D., Bjoro,T., Luders,T., Riis,M., Bukholm,I.K.,
            Kristensen,V.N., Troester,M.A., Homen,M.M., Ursin,G.,
            Borresen-Dale,A.L. and Helland,A.
  TITLE     Serum estradiol levels associated with specific gene expression
            patterns in normal breast tissue and in breast carcinomas
  JOURNAL   BMC Cancer 11, 332 (2011)
   PUBMED   21812955
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Loset,M., Mundal,S.B., Johnson,M.P., Fenstad,M.H., Freed,K.A.,
            Lian,I.A., Eide,I.P., Bjorge,L., Blangero,J., Moses,E.K. and
            Austgulen,R.
  TITLE     A transcriptional profile of the decidua in preeclampsia
  JOURNAL   Am J Obstet Gynecol 204 (1), 84 (2011)
   PUBMED   20934677
REFERENCE   8  (residues 1 to 837)
  AUTHORS   Aruga,J., Yokota,N. and Mikoshiba,K.
  TITLE     Human SLITRK family genes: genomic organization and expression
            profiling in normal brain and brain tumor tissue
  JOURNAL   Gene 315, 87-94 (2003)
   PUBMED   14557068
REFERENCE   9  (residues 1 to 837)
  AUTHORS   Aruga,J. and Mikoshiba,K.
  TITLE     Identification and characterization of Slitrk, a novel neuronal
            transmembrane protein family controlling neurite outgrowth
  JOURNAL   Mol Cell Neurosci 24 (1), 117-129 (2003)
   PUBMED   14550773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239921.3.
            
            Summary: This gene encodes a transmembrane protein belonging to the
            the SLITRK family. These family members include two N-terminal
            leucine-rich repeat domains similar to those found in the axonal
            growth-controlling protein SLIT, as well as C-terminal regions
            similar to neurotrophin receptors. Studies of an homologous protein
            in mouse suggest that this family member functions to suppress
            neurite outgrowth. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315044.1, SRR1803612.158140.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq27.3"
     Protein         1..837
                     /product="SLIT and NTRK-like protein 4 precursor"
                     /note="slit and trk like gene 4"
                     /calculated_mol_wt=92309
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2041
     mat_peptide     19..837
                     /product="SLIT and NTRK-like protein 4.
                     /evidence=ECO:0000255. /id=PRO_0000032679"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
                     /calculated_mol_wt=92309
     Region          <59..>213
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          60..81
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          63..84
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          84..105
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          85..108
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          108..129
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          109..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          132..153
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          133..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          156..177
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          157..179
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          179..200
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          180..204
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          205..295
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          213..>253
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          296..371
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            325
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          <358..>531
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          372..402
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          378..399
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          402..423
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          403..426
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          426..447
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          427..450
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          450..471
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          451..472
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          474..495
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          475..496
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          497..518
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     Region          498..522
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          502..>563
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Site            619..639
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW52.1)"
     CDS             1..837
                     /gene="SLITRK4"
                     /coded_by="NM_001184750.2:227..2740"
                     /db_xref="CCDS:CCDS14679.1"
                     /db_xref="GeneID:139065"
                     /db_xref="HGNC:HGNC:23502"
                     /db_xref="MIM:300562"
ORIGIN      
        1 mflwlflils alisstnads disveicnvc scvsvenvly vncekvsvyr pnqlkppwsn
       61 fyhlnfqnnf lnilypntfl nfshavslhl gnnklqnieg gaflglsalk qlhlnnnelk
      121 ilradtflgi enleylqady nlikyierga fnklhklkvl ilndnlisfl pdnifrfasl
      181 thldirgnri qklpyigvle higrvvelql ednpwncscd llplkawlen mpyniyigea
      241 icetpsdlyg rllketnkqe lcpmgtgsdf dvrilppsql engyttpngh ttqtslhrlv
      301 tkppkttnps kisgivagka lsnrnlsqiv syqtrvpplt pcpapcfckt hpsdlglsvn
      361 cqekniqsms elipkplnak klhvngnsik dvdvsdftdf egldllhlgs nqitvikgdv
      421 fhnltnlrrl ylngnqierl ypeifsglhn lqylyleynl ikeisagtfd smpnlqllyl
      481 nnnllkslpv yifsgaplar lnlrnnkfmy lpvsgvldql qsltqidleg npwdctcdlv
      541 alklwvekls dgivvkelkc etpvqfanie lkslkneilc pkllnkpsap ftspapaitf
      601 ttplgpirsp pggpvplsil ilsilvvlil tvfvafcllv fvlrrnkkpt vkheglgnpd
      661 cgsmqlqlrk hdhktnkkdg lsteafipqt ieqmskshtc glkesetgfm fsdppgqkvv
      721 mrnvadkekd llhvdtrkrl stideldelf psrdsnvfiq nfleskkeyn sigvsgfeir
      781 ypekqpdkks kksliggnhs kivveqrkse yfelkaklqs spdylqvlee qtalnki
//
LOCUS       NP_001341838             523 aa            linear   PRI 20-NOV-2025
DEFINITION  paraspeckle component 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001341838 XP_006719907
VERSION     NP_001341838.1
DBSOURCE    REFSEQ: accession NM_001354909.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Tripathi,S.K., Aneja,A., Borgaonkar,T. and Das,S.
  TITLE     PSPC1 Binds to HCV IRES and Prevents Ribosomal Protein S5 Binding,
            Inhibiting Viral RNA Translation
  JOURNAL   Viruses 16 (5), 738 (2024)
   PUBMED   38793620
  REMARK    GeneRIF: PSPC1 Binds to HCV IRES and Prevents Ribosomal Protein S5
            Binding, Inhibiting Viral RNA Translation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Qin,X., Long,Y., Bai,X., Cao,L., Yan,H., Zhang,K., Wang,B. and
            Wu,X.
  TITLE     The disordered C terminus of ALKBH5 promotes phase separation and
            paraspeckles assembly
  JOURNAL   J Biol Chem 299 (8), 105071 (2023)
   PUBMED   37474102
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Knott,G.J., Bond,C.S. and Fox,A.H.
  TITLE     The DBHS proteins SFPQ, NONO and PSPC1: a multipurpose molecular
            scaffold
  JOURNAL   Nucleic Acids Res 44 (9), 3989-4004 (2016)
   PUBMED   27084935
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Fox,A.H. and Lamond,A.I.
  TITLE     Paraspeckles
  JOURNAL   Cold Spring Harb Perspect Biol 2 (7), a000687 (2010)
   PUBMED   20573717
  REMARK    Review article
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Clemson,C.M., Hutchinson,J.N., Sara,S.A., Ensminger,A.W., Fox,A.H.,
            Chess,A. and Lawrence,J.B.
  TITLE     An architectural role for a nuclear noncoding RNA: NEAT1 RNA is
            essential for the structure of paraspeckles
  JOURNAL   Mol Cell 33 (6), 717-726 (2009)
   PUBMED   19217333
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Sasaki,Y.T., Ideue,T., Sano,M., Mituyama,T. and Hirose,T.
  TITLE     MENepsilon/beta noncoding RNAs are essential for structural
            integrity of nuclear paraspeckles
  JOURNAL   Proc Natl Acad Sci U S A 106 (8), 2525-2530 (2009)
   PUBMED   19188602
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Fox,A.H., Bond,C.S. and Lamond,A.I.
  TITLE     P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles
            in an RNA-dependent manner
  JOURNAL   Mol Biol Cell 16 (11), 5304-5315 (2005)
   PUBMED   16148043
  REMARK    GeneRIF: We map the domain within PSP1 that is mediating this
            interaction and show it is required for the correct localization of
            PSP1 to paraspeckles. This interaction is necessary but not
            sufficient for paraspeckle targeting by PSP1
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Fox,A.H., Lam,Y.W., Leung,A.K., Lyon,C.E., Andersen,J., Mann,M. and
            Lamond,A.I.
  TITLE     Paraspeckles: a novel nuclear domain
  JOURNAL   Curr Biol 12 (1), 13-25 (2002)
   PUBMED   11790299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354808.24.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2017 this sequence version replaced XP_006719907.1.
            
            Summary: This gene encodes a nucleolar protein that localizes to
            punctate subnuclear structures that occur close to splicing
            speckles, known as paraspeckles. These paraspeckles are composed of
            RNA-protein structures that include a non-coding RNA, NEAT1/Men
            epsilon/beta, and the Drosophila Behavior Human Splicing family of
            proteins, which include the product of this gene and the
            P54NRB/NONO and PSF/SFPQ proteins. Paraspeckles may function in the
            control of gene expression via an RNA nuclear retention mechanism.
            The protein encoded by this gene is found in paraspeckles in
            transcriptionally active cells, but it localizes to unique cap
            structures at the nucleolar periphery when RNA polymerase II
            transcription is inhibited, or during telophase. Alternative
            splicing of this gene results in multiple transcript variants. A
            related pseudogene, which is also located on chromosome 13, has
            been identified. [provided by RefSeq, Aug 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.129354.1,
                                           SRR1660805.72108.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338910.9/ ENSP00000343966.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..523
                     /product="paraspeckle component 1 isoform 1"
                     /note="paraspeckle protein 1"
                     /calculated_mol_wt=58613
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Region          81..151
                     /region_name="RRM1_PSP1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     paraspeckle protein 1 (PSP1); cd12586"
                     /db_xref="CDD:409999"
     Site            order(81,128,131..132,135..136,138)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409999"
     Region          125..358
                     /region_name="Sufficient for paraspeckles localization.
                     /evidence=ECO:0000269|PubMed:16148043"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Region          157..236
                     /region_name="RRM2_PSP1"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     paraspeckle protein 1 (PSP1 or PSPC1); cd12589"
                     /db_xref="CDD:410002"
     Site            order(162,165..171,175,178..179,184,186..191,196,200,
                     215..222,224..229,231)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410002"
     Region          227..320
                     /region_name="NOPS_PSPC1"
                     /note="NOPS domain, including C-terminal coiled-coil
                     region, in paraspeckle protein component 1 (PSPC1) and
                     similar proteins; cd12949"
                     /db_xref="CDD:240584"
     Site            order(227..229,231,237..240,242..246,249,254..255,
                     257..261,263..266,271..272,275..276,278..280,282..283,
                     285..286,289..290,293..294,296..297,300..301,304..305,
                     307..308,311..312,315)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:240584"
     Region          231..358
                     /region_name="Sufficient for perinucleolar caps
                     localization and interaction with NONO.
                     /evidence=ECO:0000269|PubMed:16148043"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Region          460..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Site            507
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q8WXF1.1)"
     CDS             1..523
                     /gene="PSPC1"
                     /gene_synonym="PSP1"
                     /coded_by="NM_001354909.2:189..1760"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS41870.1"
                     /db_xref="GeneID:55269"
                     /db_xref="HGNC:HGNC:20320"
                     /db_xref="MIM:612408"
ORIGIN      
        1 mmlrgnlkqv rieknparlr alesavgese paaaaamala lagepappap appedhpdee
       61 mgftidiksf lkpgektytq rcrlfvgnlp tditeedfkr lferygepse vfinrdrgfg
      121 firlesrtla eiakaeldgt ilksrplrir fathgaaltv knlspvvsne lleqafsqfg
      181 pvekavvvvd drgratgkgf vefaakppar kalercgdga flltttprpv ivepmeqfdd
      241 edglpeklmq ktqqyhkere qpprfaqpgt fefeyasrwk aldemekqqr eqvdrnirea
      301 kekleaemea arhehqlmlm rqdlmrrqee lrrleelrnq elqkrkqiql rheeehrrre
      361 eemirhreqe elrrqqegfk pnymenreqe mrmgdmgprg ainmgdafsp apagnqgppp
      421 mmgmnmnnra tipgppmgpg pamgpegaan mgtpmmpdng avhndrfpqg ppsqmgspmg
      481 srtgsetpqa pmsgvgpvsg gpggfgrgsq ggnfegpnkr rry
//
LOCUS       NP_055914               1202 aa            linear   PRI 20-NOV-2025
DEFINITION  calmodulin-binding transcription activator 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055914
VERSION     NP_055914.2
DBSOURCE    REFSEQ: accession NM_015099.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1202)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 1202)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1202)
  AUTHORS   Monies,D., Abou Al-Shaar,H., Goljan,E.A., Al-Younes,B.,
            Al-Breacan,M.M.A., Al-Saif,M.M., Wakil,S.M., Meyer,B.F.,
            Khabar,K.S.A. and Bohlega,S.
  TITLE     Identification of a novel genetic locus underlying tremor and
            dystonia
  JOURNAL   Hum Genomics 11 (1), 25 (2017)
   PUBMED   29110692
  REMARK    GeneRIF: Mutation of CAMTA2 resulting in post-transcriptional
            inhibition of its own gene activity likely underlies a novel
            syndromic tremulous dystonia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1202)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1202)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 1202)
  AUTHORS   Finkler,A., Ashery-Padan,R. and Fromm,H.
  TITLE     CAMTAs: calmodulin-binding transcription activators from plants to
            human
  JOURNAL   FEBS Lett 581 (21), 3893-3898 (2007)
   PUBMED   17689537
  REMARK    Review article
REFERENCE   7  (residues 1 to 1202)
  AUTHORS   Liu,N. and Olson,E.N.
  TITLE     Coactivator control of cardiovascular growth and remodeling
  JOURNAL   Curr Opin Cell Biol 18 (6), 715-722 (2006)
   PUBMED   17046230
  REMARK    Review article
REFERENCE   8  (residues 1 to 1202)
  AUTHORS   Song,K., Backs,J., McAnally,J., Qi,X., Gerard,R.D.,
            Richardson,J.A., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     The transcriptional coactivator CAMTA2 stimulates cardiac growth by
            opposing class II histone deacetylases
  JOURNAL   Cell 125 (3), 453-466 (2006)
   PUBMED   16678093
REFERENCE   9  (residues 1 to 1202)
  AUTHORS   Schwartz,R.J. and Schneider,M.D.
  TITLE     CAMTA in cardiac hypertrophy
  JOURNAL   Cell 125 (3), 427-429 (2006)
   PUBMED   16678087
  REMARK    Review article
REFERENCE   10 (residues 1 to 1202)
  AUTHORS   Bouche,N., Scharlat,A., Snedden,W., Bouchez,D. and Fromm,H.
  TITLE     A novel family of calmodulin-binding transcription activators in
            multicellular organisms
  JOURNAL   J Biol Chem 277 (24), 21851-21861 (2002)
   PUBMED   11925432
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004771.1, DB275145.1 and AB020716.1.
            
            On Apr 14, 2003 this sequence version replaced NP_055914.1.
            
            Summary: The protein encoded by this gene is a member of the
            calmodulin-binding transcription activator protein family. Members
            of this family share a common domain structure that consists of a
            transcription activation domain, a DNA-binding domain, and a
            calmodulin-binding domain. The encoded protein may be a
            transcriptional coactivator of genes involved in cardiac growth.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142695.1, AB020716.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000348066.8/ ENSP00000321813.7
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..1202
                     /product="calmodulin-binding transcription activator 2
                     isoform 1"
                     /calculated_mol_wt=131399
     Region          34..150
                     /region_name="CG-1"
                     /note="CG-1 domains are highly conserved domains of about
                     130 amino-acid residues; smart01076"
                     /db_xref="CDD:198144"
     Region          79..86
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00767"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          263..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          361..409
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          421..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          534..614
                     /region_name="TIG"
                     /note="IPT/TIG domain; pfam01833"
                     /db_xref="CDD:460355"
     Region          <710..811
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(710,712,716..717,720..722,724..725,729,744,753,755,
                     757,761..762,765..767,769..770,774,777,787,789,791,
                     795..796,799..801,803..804,808)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          710..753
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          712..745
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          755..787
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          757..787
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          791..821
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          817..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     Region          906..929
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94983.3)"
     CDS             1..1202
                     /gene="CAMTA2"
                     /coded_by="NM_015099.4:148..3756"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11063.1"
                     /db_xref="GeneID:23125"
                     /db_xref="HGNC:HGNC:18807"
                     /db_xref="MIM:611508"
ORIGIN      
        1 mntkdtteva enshhlkifl pkklleclpr cpllpperlr wntneeiasy litfekhdew
       61 lscapktrpq ngsiilynrk kvkyrkdgyl wkkrkdgktt redhmklkvq gmeclygcyv
      121 hssivptfhr rcywllqnpd ivlvhylnvp aledcgkgcs pifcsissdr rewlkwsree
      181 llgqlkpmfh gikwscgngt eefsvehlvq qildthptkp aprthaclcs gglgsgslth
      241 kcsstkhrii spkvepralt ltsiphahpp epppliaplp pelpkahtsp sssssssssg
      301 faepleirps pptsrggssr ggtaillltg leqraggltp trhlapqadp rpsmslavvv
      361 gtepsappap pspafdpdrf lnspqrgqty gggqgvspdf peaeaahtpc salepaaale
      421 pqaaargppp qsvaggrrgn cffiqdddsg eelkghgaap pipspppspp pspaplepss
      481 rvgrgealfg gpvgaselep fslssfpdlm gelisdeaps ipaptpqlsp alstitdfsp
      541 ewsypeggvk vlitgpwtea aehyscvfdh iavpaslvqp gvlrcycpah evglvslqva
      601 gregplsasv lfeyrarrfl slpstqldwl slddnqfrms ilerleqmek rmaeiaaagq
      661 vpcqgpdapp vqdegqgpgf earvvvlves miprstwkgp erlahgspfr gmsllhlaaa
      721 qgyarlietl sqwrsvetgs ldleqevdpl nvdhfsctpl mwacalghle aavllfrwnr
      781 qalsipdslg rlplsvahsr ghvrlarcle elqrqepsve ppfalsppss spdtglssvs
      841 spselsdgtf svtsayssap dgspppaplp asemtmedma pgqlssgvpe aplllmdyea
      901 tnskgplssl palppasddg aapedadspq avdvipvdmi slakqiieat perikredfv
      961 glpeagasmr ertgavglse tmswlasyle nvdhfpsstp pselpfergr lavpsapswa
     1021 eflsastsgk mesdfalltl sdheqrelye aarviqtafr kykgrrlkeq qevaaaviqr
     1081 cyrkykqltw ialkfalykk mtqaailiqs kfrsyyeqkr fqqsrraavl iqqhyrsyrr
     1141 rpgpphrtsa tlparnkgsf ltkkqdqaar kimrflrrcr hrmrelkqnq eleglpqpgl
     1201 at
//
LOCUS       NP_203752               1861 aa            linear   PRI 20-NOV-2025
DEFINITION  protein TANC1 isoform 1 [Homo sapiens].
ACCESSION   NP_203752 XP_043492
VERSION     NP_203752.2
DBSOURCE    REFSEQ: accession NM_033394.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1861)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1861)
  AUTHORS   Wu,D., Li,Y., Ren,Q., Pei,S., Wang,L., Yang,L., Chong,Y., Sun,S.,
            Hao,J. and Feng,F.
  TITLE     TANC1 methylation as a novel biomarker for the diagnosis of
            patients with anti-tuberculosis drug-induced liver injury
  JOURNAL   Sci Rep 11 (1), 17423 (2021)
   PUBMED   34465797
  REMARK    GeneRIF: TANC1 methylation as a novel biomarker for the diagnosis
            of patients with anti-tuberculosis drug-induced liver injury.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1861)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1861)
  AUTHORS   Yang,Q., Liu,H., Li,Z., Wang,Y. and Liu,W.
  TITLE     Purification and mutagenesis studies of TANC1 ankyrin repeats
            domain provide clues to understand mis-sense variants from diseases
  JOURNAL   Biochem Biophys Res Commun 514 (2), 358-364 (2019)
   PUBMED   31040020
  REMARK    GeneRIF: mis-sense variants tested in this study may either affect
            protein folding or disrupt the interaction between TANC1/2 AR
            domains and their binding partners
REFERENCE   6  (residues 1 to 1861)
  AUTHORS   Fachal,L., Gomez-Caamano,A., Barnett,G.C., Peleteiro,P.,
            Carballo,A.M., Calvo-Crespo,P., Kerns,S.L., Sanchez-Garcia,M.,
            Lobato-Busto,R., Dorling,L., Elliott,R.M., Dearnaley,D.P.,
            Sydes,M.R., Hall,E., Burnet,N.G., Carracedo,A., Rosenstein,B.S.,
            West,C.M., Dunning,A.M. and Vega,A.
  TITLE     A three-stage genome-wide association study identifies a
            susceptibility locus for late radiotherapy toxicity at 2q24.1
  JOURNAL   Nat Genet 46 (8), 891-894 (2014)
   PUBMED   24974847
REFERENCE   7  (residues 1 to 1861)
  AUTHORS   Avirneni-Vadlamudi,U., Galindo,K.A., Endicott,T.R., Paulson,V.,
            Cameron,S. and Galindo,R.L.
  TITLE     Drosophila and mammalian models uncover a role for the myoblast
            fusion gene TANC1 in rhabdomyosarcoma
  JOURNAL   J Clin Invest 122 (1), 403-407 (2012)
   PUBMED   22182840
REFERENCE   8  (residues 1 to 1861)
  AUTHORS   Granot-Hershkovitz,E., Raas-Rothschild,A., Frumkin,A., Granot,D.,
            Silverstein,S. and Abeliovich,D.
  TITLE     Complex chromosomal rearrangement in a girl with
            psychomotor-retardation and a de novo inversion: inv(2)(p15;q24.2)
  JOURNAL   Am J Med Genet A 155A (8), 1825-1832 (2011)
   PUBMED   21739571
REFERENCE   9  (residues 1 to 1861)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1861)
  AUTHORS   Suzuki,T., Li,W., Zhang,J.P., Tian,Q.B., Sakagami,H., Usuda,N.,
            Kondo,H., Fujii,T. and Endo,S.
  TITLE     A novel scaffold protein, TANC, possibly a rat homolog of
            Drosophila rolling pebbles (rols), forms a multiprotein complex
            with various postsynaptic density proteins
  JOURNAL   Eur J Neurosci 21 (2), 339-350 (2005)
   PUBMED   15673434
  REMARK    GeneRIF: Discusses cloning and expression of Rat TANC1 and
            preliminary cloning of human TANC1, which resulted in recovery of a
            partial cDNA.
            Erratum:[Eur J Neurosci. 2005 Feb;21(3):825. Usada, Nobuteru
            [corrected to Usuda, Nobuteru]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC037329.1, AK128859.1, AC009307.4, BC150597.1, BX648327.1 and
            AL833258.1.
            
            On Mar 21, 2009 this sequence version replaced NP_203752.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.84494.1,
                                           SRR1660805.205801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263635.8/ ENSP00000263635.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..1861
                     /product="protein TANC1 isoform 1"
                     /note="rolling pebbles homolog B; TPR domain,
                     ankyrin-repeat and coiled-coil-containing; protein TANC1;
                     tetratricopeptide repeat, ankyrin repeat and coiled-coil
                     domain-containing protein 1"
                     /calculated_mol_wt=202089
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          63..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          206..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          257..311
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          439..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          <521..>822
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          896..928
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          934..963
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          939..965
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(940..941,944..946,948..949,953,956,965,967,969,
                     973..974,977..979,981..982,986,989,998,1000,1002,
                     1006..1007,1010..1012,1014..1015,1019)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          948..>1205
                     /region_name="PHA03100"
                     /note="ankyrin repeat protein; Provisional; cl39094"
                     /db_xref="CDD:476869"
     Region          967..998
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          967..996
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1000..1029
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1040..1069
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1078..1107
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1079..1285
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          1079..1109
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1111..1140
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1115..1142
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1144..1173
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1145..1175
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(1146,1150..1151,1154..1156,1158..1159,1163,1166,
                     1175,1177,1179,1183..1184,1187..1189,1191..1192,1196,1199,
                     1208,1210,1212,1216..1217,1220..1222,1224..1225,1229,1232,
                     1241)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          1177..1208
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1177..1206
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1210..1241
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1210..1239
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1243..1272
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1243..1268
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          1273..>1410
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          1289..1322
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1292..1317
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1293..1294,1297..1298,1300,1337,1340..1341,
                     1344..1345,1347..1348,1371,1374..1375,1378..1379,1382)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1335..1365
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1336..1369
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1370..1398
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1371..1403
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1421..1485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6F6B3; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Region          1636..1696
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0VGY8; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     Site            1677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0VGY8; propagated from
                     UniProtKB/Swiss-Prot (Q9C0D5.3)"
     CDS             1..1861
                     /gene="TANC1"
                     /gene_synonym="ROLSB; TANC"
                     /coded_by="NM_033394.3:269..5854"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42766.1"
                     /db_xref="GeneID:85461"
                     /db_xref="HGNC:HGNC:29364"
                     /db_xref="MIM:611397"
ORIGIN      
        1 mlkavlkksr eggkggkkea gsdfgpetsp vlhldhsads pvsslptaed tyrvslakgv
       61 smslpsspll prqshlvqsr vnkkspgpvr kpkyvesprv pgdavimpfr evakptepde
      121 heakadneps cspaaqellt rlgfllgegi psathitied knetmctals qgispcstlt
      181 sstaspstds pcstlnscvs ktaankspce tisspsstle skdsgiiati tsssenddrs
      241 gsslewnkdg nlrlgvqkgv lhdrradncs pvaeeettgs aestlpkaes sagdgpvpys
      301 qgssslimpr pnsvaatsst kledlsyldg qrnaplrtsi rlpwhntagg raqevkarfa
      361 pykpqdillk pllfevpsit tdsvfvgrdw lfhqieenlr ntelaenrga vvvgnvgfgk
      421 taiisklval schgsrmrqi asnspgsspk tsdptqdlhf tpllspssst sasstaktpl
      481 gsisaenqrp redavkylas kvvayhycqa dntytclvpe fvhsiaallc rshqlaayrd
      541 llikepqlqs mlslrscvqd pvaafkrgvl epltnlrneq kipeeeyiil idglneaefh
      601 kpdygdtlss fitkiiskfp awlklivtvr anfqeiisal pfvklslddf pdnkdihsdl
      661 hayvqhrvhs sqdilsnisl ngkadatlig kvsshlvlrs lgsylylklt ldlfqrghlv
      721 iksasykvvp vslselyllq cnmkfmtqsa feralpilnv alaslhpmtd eqifqainag
      781 hiqgeqgwed fqqrmdalsc flikrrdktr mfchpsfrew lvwradgent aflceprngh
      841 allafmfsrq egklnrqqtm elghhilkah ifkglskktg issshlqalw igysteglsa
      901 alaslrnlyt pnvkvsrlli lgganvnyrt evlnnapilc vqshlgheev vtlllefgac
      961 ldgtsengmt alcyaaaagh mklvclltkk gvrvdhldkk gqcalvhsal rghgdilqyl
     1021 ltcewspgpp qpgtlrksha lqqaltaaas mghssvvqcl lgmekeheve vngtdtlwge
     1081 taltaaagrg klevcelllg hgaavsrtnr rgvpplfcaa rqghwqivrl llergcdvnl
     1141 sdkqgrtplm vaaceghlst vefllskgaa lssldkegls alswaclkgh ravvqylvee
     1201 gaaidqtdkn grtpldlaaf ygdaetvlyl vekgaviehv dhsgmrpldr aigcrntsvv
     1261 vallrkgakl gnaawamats kpdiliillq klmeegnvmy kkgkmkeaaq ryqyalrkfp
     1321 regfgedmrp fnelrvslyl nlsrcrrktn dfgmaeefas kalelkpksy eafyararak
     1381 rnsrqfvaal adlqeavklc ptnqevkrll arveeeckql qrsqqqkqqg plpaplndse
     1441 needtptpgl sdhfhseete eeetspqees vsptprsqps ssvpssyirn lqeglqskgr
     1501 pvspqsragi gkslrepvaq pglllqpskq aqivktsqhl gsgqsavrng smkvqissqn
     1561 pppspmpgri aatpagsrtq hlegtgtftt ragcghfgdr lgpsqnvrlq cgengpahpl
     1621 psktktterl lshssvavda appnqgglat csdvrhpasl tssgssgsps ssikmsssts
     1681 sltssssfsd gfkvqgpdtr ikdkvvthvq sgtaehrprn tpfmgimdkt arfqqqsnpp
     1741 srswhcpape glltntssaa glqsantekp slmqvggynn qaktcsvstl sasvhngaqv
     1801 keleeskcqi pvhsqenrit ktvshlyqes iskqqphisn eahrshltaa kpkrsfiesn
     1861 v
//
LOCUS       NP_001032402             211 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 112 kDa isoform b [Homo sapiens].
ACCESSION   NP_001032402
VERSION     NP_001032402.1
DBSOURCE    REFSEQ: accession NM_001037325.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Zhang,X., Huang,G., Jiang,T., Meng,L., Li,T., Zhang,G., Wu,N.,
            Chen,X., Zhao,B., Li,N., Wu,S., Guo,J., Zheng,R., Ji,Z., Xu,Z.,
            Wang,Z., Deng,D., Tan,Y. and Xu,W.
  TITLE     CEP112 coordinates translational regulation of essential fertility
            genes during spermiogenesis through phase separation in humans and
            mice
  JOURNAL   Nat Commun 15 (1), 8465 (2024)
   PUBMED   39349455
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Sha,Y., Wang,X., Yuan,J., Zhu,X., Su,Z., Zhang,X., Xu,X. and Wei,X.
  TITLE     Loss-of-function mutations in centrosomal protein 112 is associated
            with human acephalic spermatozoa phenotype
  JOURNAL   Clin Genet 97 (2), 321-328 (2020)
   PUBMED   31654588
  REMARK    GeneRIF: Loss-of-function mutations in centrosomal protein 112 is
            associated with human acephalic spermatozoa phenotype.
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Gopalakrishnan,C., Kamaraj,B. and Purohit,R.
  TITLE     Mutations in microRNA binding sites of CEP genes involved in cancer
  JOURNAL   Cell Biochem Biophys 70 (3), 1933-1942 (2014)
   PUBMED   25115610
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Liu,X., Zheng,Y., Zhang,W., Zhang,X., Lioyd-Jones,D.M.,
            Baccarelli,A.A., Ning,H., Fornage,M., He,K., Liu,K. and Hou,L.
  TITLE     Blood methylomics in response to arsenic exposure in a low-exposed
            US population
  JOURNAL   J Expo Sci Environ Epidemiol 24 (2), 145-149 (2014)
   PUBMED   24368509
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Kumar,A., Rajendran,V., Sethumadhavan,R. and Purohit,R.
  TITLE     CEP proteins: the knights of centrosome dynasty
  JOURNAL   Protoplasma 250 (5), 965-983 (2013)
   PUBMED   23456457
  REMARK    Review article
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Smith,K.R., Oliver,P.L., Lumb,M.J., Arancibia-Carcamo,I.L.,
            Revilla-Sanchez,R., Brandon,N.J., Moss,S.J. and Kittler,J.T.
  TITLE     Identification and characterisation of a Maf1/Macoco protein
            complex that interacts with GABAA receptors in neurons
  JOURNAL   Mol Cell Neurosci 44 (4), 330-341 (2010)
   PUBMED   20417281
  REMARK    GeneRIF: We report that Maf1 interacts with a novel coiled-coil
            domain containing protein that we have called Macoco.
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Sombekke,M.H., Arteta,D., van de Wiel,M.A., Crusius,J.B.,
            Tejedor,D., Killestein,J., Martinez,A., Pena,A.S., Polman,C.H. and
            Uitdehaag,B.M.
  TITLE     Analysis of multiple candidate genes in association with phenotypes
            of multiple sclerosis
  JOURNAL   Mult Scler 16 (6), 652-659 (2010)
   PUBMED   20378664
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Mult Scler. 2010 Jun;16(6):765]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029524.1, BG531260.1,
            AA723963.1 and AC004805.1.
            
            Summary: This gene encodes a coiled-coil domain containing protein
            that belongs to the cell division control protein 42 effector
            protein family. In neurons, it localizes to the cytoplasm of
            dendrites and is also enriched in the nucleus where it interacts
            with the RNA polymerase III transcriptional repressor Maf1 to
            regulate gamma-aminobutyric acid A receptor surface expression. In
            addition, the protein has been identified as a component of the
            human centrosome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2014].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.258787.1,
                                           SRR5189667.44641.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.1"
     Protein         1..211
                     /product="centrosomal protein of 112 kDa isoform b"
                     /note="centrosomal protein of 112 kDa; coiled-coil
                     domain-containing protein 46; centrosomal protein 112kDa"
                     /calculated_mol_wt=24407
     Region          <34..>211
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     CDS             1..211
                     /gene="CEP112"
                     /gene_synonym="CCDC46; MACOCO; SPGF44"
                     /coded_by="NM_001037325.3:153..788"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32711.1"
                     /db_xref="GeneID:201134"
                     /db_xref="HGNC:HGNC:28514"
                     /db_xref="MIM:618980"
ORIGIN      
        1 mwaslsldhp sakenqalrl iemreengnv pkteqagslk plrdtgksnl kekkansklk
       61 qiekeytqkl akssqiiael qttisslkee nsqqqlaaer rlqdvrqkfe dekkqlirdn
      121 dqaikvlqde lenrsnqvrc aekklqhkel esqeqityir qeyetklkgl mpaslrqele
      181 dtisslksqv nflqkrasil qeelttyqgr r
//
LOCUS       NP_476502                382 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_476502
VERSION     NP_476502.1
DBSOURCE    REFSEQ: accession NM_057161.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Liu,Y., Luo,Y., Yan,S., Lian,Y.F., Wu,S., Xu,M., Feng,L., Zhang,X.,
            Li,R., Zhang,X., Feng,Q.S., Zeng,Y.X. and Zhang,H.
  TITLE     CRL2KLHDC3 mediates p14ARF N-terminal ubiquitylation degradation to
            promote non-small cell lung carcinoma progression
  JOURNAL   Oncogene 41 (22), 3104-3117 (2022)
   PUBMED   35468939
  REMARK    GeneRIF: CRL2(KLHDC3) mediates p14ARF N-terminal ubiquitylation
            degradation to promote non-small cell lung carcinoma progression.
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Zhang,P., Gao,K., Zhang,L., Sun,H., Zhao,X., Liu,Y., Lv,Z., Shi,Q.,
            Chen,Y., Jiao,D., Li,Y., Gu,W. and Wang,C.
  TITLE     CRL2-KLHDC3 E3 ubiquitin ligase complex suppresses ferroptosis
            through promoting p14ARF degradation
  JOURNAL   Cell Death Differ 29 (4), 758-771 (2022)
   PUBMED   34743205
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Koren,I., Timms,R.T., Kula,T., Xu,Q., Li,M.Z. and Elledge,S.J.
  TITLE     The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting
            C-Terminal Degrons
  JOURNAL   Cell 173 (7), 1622-1635 (2018)
   PUBMED   29779948
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Ohinata,Y., Sutou,S. and Mitsui,Y.
  TITLE     Peas-Mea1-Ppp2r5d overlapping gene complex: a transposon
            mediated-gene formation in mammals
  JOURNAL   DNA Res 10 (2), 79-84 (2003)
   PUBMED   12755172
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Hermey,G., Keat,S.J., Madsen,P., Jacobsen,C., Petersen,C.M. and
            Gliemann,J.
  TITLE     Characterization of sorCS1, an alternatively spliced receptor with
            completely different cytoplasmic domains that mediate different
            trafficking in cells
  JOURNAL   J Biol Chem 278 (9), 7390-7396 (2003)
   PUBMED   12482870
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Ohinata,Y., Sutou,S. and Mitsui,Y.
  TITLE     A novel testis-specific RAG2-like protein, Peas: its expression in
            pachytene spermatocyte cytoplasm and meiotic chromatin
  JOURNAL   FEBS Lett 537 (1-3), 1-5 (2003)
   PUBMED   12606021
  REMARK    GeneRIF: cloned human and mouse Peas cDNAs (hPEAS/mPeas) and
            analyzed their tissue and stage-specific expressions; may be
            involved in meiotic recombination process
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Ohinata,Y., Sutou,S., Kondo,M., Takahashi,T. and Mitsui,Y.
  TITLE     Male-enhanced antigen-1 gene flanked by two overlapping genes is
            expressed in late spermatogenesis
  JOURNAL   Biol Reprod 67 (6), 1824-1831 (2002)
   PUBMED   12444059
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC395338.1 and BC001789.1.
            
            Summary: The protein encoded by this gene contains six repeated
            kelch motifs that are structurally similar to recombination
            activating gene 2, a protein involved in the activation of the
            V(D)J recombination. In mouse, this gene is found to be expressed
            specifically in testis. Its expression in pachytene spermatocytes
            is localized to cytoplasma and meiotic chromatin, suggesting that
            this gene may be involved in meiotic recombination. [provided by
            RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1302.1, SRR1163655.6325.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326974.9/ ENSP00000313995.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..382
                     /product="kelch domain-containing protein 3"
                     /note="testis intracellular mediator protein"
                     /calculated_mol_wt=42957
     Region          14..308
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          14..62
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          25..77
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ90.1)"
     Region          77..122
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          88..138
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ90.1)"
     Region          128..173
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          139..189
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ90.1)"
     Region          180..236
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          191..249
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ90.1)"
     Region          239..283
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          251..301
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ90.1)"
     CDS             1..382
                     /gene="KLHDC3"
                     /gene_synonym="dJ20C7.3; PEAS"
                     /coded_by="NM_057161.4:160..1308"
                     /db_xref="CCDS:CCDS4880.1"
                     /db_xref="GeneID:116138"
                     /db_xref="HGNC:HGNC:20704"
                     /db_xref="MIM:611248"
ORIGIN      
        1 mlrwtvhleg gprrvnhaav avghrvysfg gycsgedyet lrqidvhifn avslrwtklp
       61 pvksairgqa pvvpymrygh stvliddtvl lwggrndteg acnvlyafdv nthkwftprv
      121 sgtvpgardg hsacvlgkim yifggyeqqa dcfsndihkl dtstmtwtli ctkgsparwr
      181 dfhsatmlgs hmyvfggrad rfgpfhsnne iycnrirvfd trteawldcp ptpvlpegrr
      241 shsafgynge lyifggynar lnrhfhdlwk fnpvsftwkk iepkgkgpcp rrrqcccivg
      301 dkivlfggts pspeeglgde fdlidhsdlh ildfspslkt lcklaviqyn ldqsclphdi
      361 rwelnamttn snisrpivss hg
//
LOCUS       NP_001336352             600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_001336352 XP_005247613
VERSION     NP_001336352.1
DBSOURCE    REFSEQ: accession NM_001349423.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_005247613.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (12), as well as variants 7-11 and
            13-15, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.42643.1,
                                           SRR1660803.151713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349423.1:233..2035"
                     /note="isoform b is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001337605             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337605 XP_005250722
VERSION     NP_001337605.1
DBSOURCE    REFSEQ: accession NM_001350676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 21, 2017 this sequence version replaced XP_005250722.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (13), as well as variants 1-4,
            9-12, and 14-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.152231.1,
                                           SRR1803612.31790.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350676.1:579..2789"
                     /note="isoform 1 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001737                592 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform d precursor [Homo sapiens].
ACCESSION   NP_001737
VERSION     NP_001737.1
DBSOURCE    REFSEQ: accession NM_001746.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2 and BC003552.1.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.181014.1,
                                           SRR1660805.126186.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247461.9/ ENSP00000247461.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..592
                     /product="calnexin isoform d precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65396
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     mat_peptide     21..592
                     /product="calnexin isoform d"
                     /calculated_mol_wt=65396
     Region          71..440
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27824.2)"
     Region          260..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          276..409
                     /region_name="P domain (Extended arm).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          278..345
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          326..359
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          348..405
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          503..592
                     /region_name="Sufficient to mediate interaction with
                     SGIP1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          511..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK3.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     CDS             1..592
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001746.4:140..1918"
                     /note="isoform d precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4447.1"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 megkwllcml lvlgtaivea hdghdddvid ieddlddvie evedskpdtt appsspkvty
       61 kapvptgevy fadsfdrgtl sgwilskakk ddtddeiaky dgkweveemk esklpgdkgl
      121 vlmsrakhha isaklnkpfl fdtkplivqy evnfqngiec ggayvkllsk tpelnldqfh
      181 dktpytimfg pdkcgedykl hfifrhknpk tgiyeekhak rpdadlktyf tdkkthlytl
      241 ilnpdnsfei lvdqsvvnsg nllndmtppv npsreiedpe drkpedwder pkipdpeavk
      301 pddwdedapa kipdeeatkp egwlddepey vpdpdaekpe dwdedmdgew eapqianprc
      361 esapgcgvwq rpvidnpnyk gkwkppmidn psyqgiwkpr kipnpdffed lepfrmtpfs
      421 aiglelwsmt sdiffdnfii cadrrivddw andgwglkka adgaaepgvv gqmieaaeer
      481 pwlwvvyilt valpvflvil fccsgkkqts gmeykktdap qpdvkeeeee keeekdkgde
      541 eeegeeklee kqksdaeedg gtvsqeeedr kpkaeedeil nrsprnrkpr re
//
LOCUS       NP_001317008             277 aa            linear   PRI 20-NOV-2025
DEFINITION  neurexin-1 isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001317008
VERSION     NP_001317008.1
DBSOURCE    REFSEQ: accession NM_001330079.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Transcript Variant: This variant (6) lacks multiple 3' coding exons
            and contains an alternate 3' terminal exon compared to variant
            alpha2. The encoded isoform (6) is much shorter than isoform
            alpha2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK124726.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..277
                     /product="neurexin-1 isoform 6 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=27163
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     CDS             1..277
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330079.2:1074..1907"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS86838.1"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqdnn veglahlmmg dqgkskd
//
LOCUS       NP_001303865             293 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform b [Homo sapiens].
ACCESSION   NP_001303865
VERSION     NP_001303865.1
DBSOURCE    REFSEQ: accession NM_001316936.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB127388.1, AC008752.6, AA524458.1 and AK000195.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) uses an alternate splice
            junction and lacks an alternate exon compared to variant 1. The
            resulting isoform (b) has the same N- and C-termini but is shorter
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AA524458.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..293
                     /product="F-box/LRR-repeat protein 12 isoform b"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=32593
     Region          4..>22
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Region          71..92
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          88..>193
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          120..144
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          145..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          171..196
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          197..220
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          251..286
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..293
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_001316936.2:267..1148"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 matlvelpds vlleifsylp mrpkvmwhll rrymasrlhs lrmggylfsg sqapqlspal
       61 lralgqkcpn lkrlclhvad lsmvpitslp stlrtlelhs ceismawlhk qqdptvlpll
      121 ecivldrvpa frdehlqglt rfralrslvl ggtyrvtetg ldaglqelsy lqrlevlgct
      181 lsadstllai srhlrdvrki rltvrglsap glavlegmpa leslclqgpl vtpempspte
      241 ilsscltmpk lrvlelqglg wegqeaekil ckglphcmvi vracpkesmd wwm
//
LOCUS       NP_542173                241 aa            linear   PRI 20-NOV-2025
DEFINITION  class E basic helix-loop-helix protein 23 [Homo sapiens].
ACCESSION   NP_542173
VERSION     NP_542173.2
DBSOURCE    REFSEQ: accession NM_080606.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Yin,Y., Morgunova,E., Jolma,A., Kaasinen,E., Sahu,B.,
            Khund-Sayeed,S., Das,P.K., Kivioja,T., Dave,K., Zhong,F.,
            Nitta,K.R., Taipale,M., Popov,A., Ginno,P.A., Domcke,S., Yan,J.,
            Schubeler,D., Vinson,C. and Taipale,J.
  TITLE     Impact of cytosine methylation on DNA binding specificities of
            human transcription factors
  JOURNAL   Science 356 (6337) (2017)
   PUBMED   28473536
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Liu,A., Wang,Y., Zhang,D., Wang,X., Song,H., Dang,C., Yao,Q. and
            Chen,K.
  TITLE     Classification and evolutionary analysis of the basic
            helix-loop-helix gene family in the green anole lizard, Anolis
            carolinensis
  JOURNAL   Mol Genet Genomics 288 (7-8), 365-380 (2013)
   PUBMED   23756994
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Stevens,J.D., Roalson,E.H. and Skinner,M.K.
  TITLE     Phylogenetic and expression analysis of the basic helix-loop-helix
            transcription factor gene family: genomic approach to cellular
            differentiation
  JOURNAL   Differentiation 76 (9), 1006-1022 (2008)
   PUBMED   18557763
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Bramblett,D.E., Pennesi,M.E., Wu,S.M. and Tsai,M.J.
  TITLE     The transcription factor Bhlhb4 is required for rod bipolar cell
            maturation
  JOURNAL   Neuron 43 (6), 779-793 (2004)
   PUBMED   15363390
  REMARK    GeneRIF: Knockout mouse retinal dysfunction resembles human
            congenital stationary night blindness.
REFERENCE   9  (residues 1 to 241)
  AUTHORS   McLellan,A.S., Langlands,K. and Kealey,T.
  TITLE     Exhaustive identification of human class II basic helix-loop-helix
            proteins by virtual library screening
  JOURNAL   Mech Dev 119 Suppl 1, S285-S291 (2002)
   PUBMED   14516699
REFERENCE   10 (residues 1 to 241)
  AUTHORS   Bramblett,D.E., Copeland,N.G., Jenkins,N.A. and Tsai,M.J.
  TITLE     BHLHB4 is a bHLH transcriptional regulator in pancreas and brain
            that marks the dimesencephalic boundary
  JOURNAL   Genomics 79 (3), 402-412 (2002)
   PUBMED   11863370
  REMARK    GeneRIF: Mouse Bhlhe23 can function as a transcriptional repressor.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC137288.1 and AL121673.41.
            
            On May 21, 2013 this sequence version replaced NP_542173.1.
            
            Summary: This gene encodes a member of the basic helix-loop-helix
            transcription factor family. Members of this family contain two
            highly conserved and functionally distinct domains: the basic
            domain targets sequence-specific DNA binding, while the
            helix-loop-helix domain facilitates protein interaction. Studies of
            a related gene in mouse suggest that the encoded protein may
            function as a transcriptional repressor in the pancreas and brain,
            and that it is required for normal retinal function. [provided by
            RefSeq, May 2013].
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC137288.1, BK000274.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000612929.2/ ENSP00000480998.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..241
                     /product="class E basic helix-loop-helix protein 23"
                     /note="basic helix-loop-helix domain containing, class B,
                     4; class B basic helix-loop-helix protein 4"
                     /calculated_mol_wt=25036
     Region          111..191
                     /region_name="bHLH_SF"
                     /note="basic Helix Loop Helix (bHLH) domain superfamily;
                     cl00081"
                     /db_xref="CDD:469605"
     Site            order(125..126,128,133,155..156)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381392"
     Site            order(131..132,135..136,138..139,143,156..157,160..161,
                     164,166..167,170..171)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381392"
     CDS             1..241
                     /gene="BHLHE23"
                     /gene_synonym="bA305P22.3; Beta3b; BETA4; BHLHB4"
                     /coded_by="NM_080606.4:191..916"
                     /db_xref="CCDS:CCDS33507.2"
                     /db_xref="GeneID:128408"
                     /db_xref="HGNC:HGNC:16093"
                     /db_xref="MIM:609331"
ORIGIN      
        1 msirppgepp spggaamael kslsgdayla lshgyaaaaa glaygaarep eaargygtpg
       61 pggdlpaapa prapaqaaes sgeqsgdedd afeqrrrrrg pgsaadgrrr preqrslrls
      121 inarerrrmh dlndaldglr avipyahsps vrklskiatl llaknyilmq aqaldemrrl
      181 vaflnqgqgl aapvnaaplt pfgqatvcpf sagaalgpcp dkcaafsgtp salckhchek
      241 p
//
LOCUS       NP_006206                427 aa            linear   PRI 20-NOV-2025
DEFINITION  kallistatin isoform 2 precursor [Homo sapiens].
ACCESSION   NP_006206
VERSION     NP_006206.2
DBSOURCE    REFSEQ: accession NM_006215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Kim,H., Suh,G.J., Kwon,W.Y., Kim,K.S., Jung,Y.S., Kim,T. and
            Park,H.
  TITLE     Kallistatin deficiency exacerbates neuronal damage after cardiac
            arrest
  JOURNAL   Sci Rep 14 (1), 4279 (2024)
   PUBMED   38383562
  REMARK    GeneRIF: Kallistatin deficiency exacerbates neuronal damage after
            cardiac arrest.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Wang,Y., Chen,X.Y., Shang,K., Xu,Q., Li,Y.X., DU,Y. and Zhuan,L.
  TITLE     [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism]
  JOURNAL   Zhonghua Nan Ke Xue 28 (11), 976-984 (2022)
   PUBMED   37846113
  REMARK    GeneRIF: [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism].
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Cho,I., Lee,K.N., Joo,E., Kim,Y.M., Kim,T.E. and Park,K.H.
  TITLE     Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes
  JOURNAL   Am J Reprod Immunol 88 (3), e13584 (2022)
   PUBMED   35772987
  REMARK    GeneRIF: Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Krishna,S.M., Li,J., Wang,Y., Moran,C.S., Trollope,A., Huynh,P.,
            Jose,R., Biros,E., Ma,J. and Golledge,J.
  TITLE     Kallistatin limits abdominal aortic aneurysm by attenuating
            generation of reactive oxygen species and apoptosis
  JOURNAL   Sci Rep 11 (1), 17451 (2021)
   PUBMED   34465809
  REMARK    GeneRIF: Kallistatin limits abdominal aortic aneurysm by
            attenuating generation of reactive oxygen species and apoptosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Chen,L.M., Song,Q., Chao,L. and Chao,J.
  TITLE     Cellular localization of tissue kallikrein and kallistatin mRNAs in
            human kidney
  JOURNAL   Kidney Int 48 (3), 690-697 (1995)
   PUBMED   7474653
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Chai,K.X., Ward,D.C., Chao,J. and Chao,L.
  TITLE     Molecular cloning, sequence analysis, and chromosomal localization
            of the human protease inhibitor 4 (kallistatin) gene (PI4)
  JOURNAL   Genomics 23 (2), 370-378 (1994)
   PUBMED   7835886
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Chai,K.X., Chen,L.M., Chao,J. and Chao,L.
  TITLE     Kallistatin: a novel human serine proteinase inhibitor. Molecular
            cloning, tissue distribution, and expression in Escherichia coli
  JOURNAL   J Biol Chem 268 (32), 24498-24505 (1993)
   PUBMED   8227002
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Zhou,G.X., Chao,L. and Chao,J.
  TITLE     Kallistatin: a novel human tissue kallikrein inhibitor.
            Purification, characterization, and reactive center sequence
  JOURNAL   J Biol Chem 267 (36), 25873-25880 (1992)
   PUBMED   1334488
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Wang,M.Y., Day,J., Chao,L. and Chao,J.
  TITLE     Human kallistatin, a new tissue kallikrein-binding protein:
            purification and characterization
  JOURNAL   Adv Exp Med Biol 247B, 1-8 (1989)
   PUBMED   2558505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA036536.1, BX248760.1 and BC014992.1.
            
            On Jun 10, 2002 this sequence version replaced NP_006206.1.
            
            Transcript Variant: This variant (3) has an alternate splice site
            in the 5' region, which results in translation initiation at a
            downstream AUG codon, compared to variant 1. The resulting isoform
            (2) has a shorter N-terminus, compared to isoform 1. Both variants
            2 and 3 encode the same isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.66086.1,
                                           SRR5189664.71496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000557004.6/ ENSP00000450838.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..427
                     /product="kallistatin isoform 2 precursor"
                     /note="protease inhibitor 4 (kallistatin); serine (or
                     cysteine) proteinase inhibitor, clade A (alpha-1
                     antiproteinase, antitrypsin), member 4; serpin A4;
                     kallikrein inhibitor; peptidase inhibitor 4; serpin
                     peptidase inhibitor, clade A (alpha-1 antiproteinase,
                     antitrypsin), member 4; testicular secretory protein Li
                     22; sserpin family A member 4"
                     /calculated_mol_wt=46355
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2205
     mat_peptide     21..427
                     /product="Kallistatin. /id=PRO_0000032425"
                     /note="propagated from UniProtKB/Swiss-Prot (P29622.3)"
                     /calculated_mol_wt=46355
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Region          44..426
                     /region_name="serpinA4_KST"
                     /note="serpin family A member 4, kallistatin; cd19552"
                     /db_xref="CDD:381020"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            order(374..385,387..402)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381020"
     Site            388..389
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P29622.3)"
     CDS             1..427
                     /gene="SERPINA4"
                     /gene_synonym="KAL; kallistatin; KLST; KST; PI-4; PI4"
                     /coded_by="NM_006215.4:71..1354"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS9927.1"
                     /db_xref="GeneID:5267"
                     /db_xref="HGNC:HGNC:8948"
                     /db_xref="MIM:147935"
ORIGIN      
        1 mhlidyllll lvgllalshg qlhvehdges csnsshqqil etgegspslk iapanadfaf
       61 rfyyliaset pgkniffspl sisaayamls lgacshsrsq ileglgfnlt elsesdvhrg
      121 fqhllhtlnl pghgletrvg salflshnlk flakflndtm avyeaklfht nfydtvgtiq
      181 lindhvkket rgkivdlvse lkkdvlmvlv nyiyfkalwe kpfissrttp kdfyvdentt
      241 vrvpmmlqdq ehhwylhdry lpcsvlrmdy kgdatvffil pnqgkmreie evltpemlmr
      301 wnnllrkrnf ykklelhlpk fsisgsyvld qilprlgftd lfskwadlsg itkqqkleas
      361 ksfhkatldv deagteaaaa tsfaikffsa qtnrhilrfn rpflvvifst stqsvlflgk
      421 vvdptkp
//
LOCUS       NP_001171659             476 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase component PIGT isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001171659
VERSION     NP_001171659.1
DBSOURCE    REFSEQ: accession NM_001184730.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Ben Ayed,I., Jallouli,O., Murakami,Y., Souissi,A., Mallouli,S.,
            Bouzid,A., Kamoun,F., Elloumi,I., Frikha,F., Tlili,A.,
            Weckhuysen,S., Kinoshita,T., Triki,C.C. and Masmoudi,S.
  TITLE     Case report: Functional analysis of the p.Arg507Trp variant of the
            PIGT gene supporting the moderate epilepsy phenotype of mutations
            in the C-terminal region
  JOURNAL   Front Neurol 14, 1092887 (2023)
   PUBMED   36970549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Ohishi,K., Nagamune,K., Maeda,Y. and Kinoshita,T.
  TITLE     Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and
            PIG-T, form a functionally important intermolecular disulfide
            bridge
  JOURNAL   J Biol Chem 278 (16), 13959-13967 (2003)
   PUBMED   12582175
  REMARK    GeneRIF: GPI8 and PIG-T form a functionally important
            intermolecular disulfide bridge
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Vainauskas,S., Maeda,Y., Kurniawan,H., Kinoshita,T. and Menon,A.K.
  TITLE     Structural requirements for the recruitment of Gaa1 into a
            functional glycosylphosphatidylinositol transamidase complex
  JOURNAL   J Biol Chem 277 (34), 30535-30542 (2002)
   PUBMED   12052837
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Ohishi,K., Inoue,N. and Kinoshita,T.
  TITLE     PIG-S and PIG-T, essential for GPI anchor attachment to proteins,
            form a complex with GAA1 and GPI8
  JOURNAL   EMBO J 20 (15), 4088-4098 (2001)
   PUBMED   11483512
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Fossey,S.C., Mychaleckyj,J.C., Pendleton,J.K., Snyder,J.R.,
            Bensen,J.T., Hirakawa,S., Rich,S.S., Freedman,B.I. and Bowden,D.W.
  TITLE     A high-resolution 6.0-megabase transcript map of the type 2
            diabetes susceptibility region on human chromosome 20
  JOURNAL   Genomics 76 (1-3), 45-57 (2001)
   PUBMED   11549316
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302093.1 and AL121742.1.
            
            Summary: This gene encodes a protein that is involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid found on many blood cells and serves to
            anchor proteins to the cell surface. This protein is an essential
            component of the multisubunit enzyme, GPI transamidase. GPI
            transamidase mediates GPI anchoring in the endoplasmic reticulum,
            by catalyzing the transfer of fully assembled GPI units to
            proteins. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (4) lacks two consecutive exons in
            the 5' coding region, but maintains the reading frame, compared to
            variant 1. The encoded isoform (4) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.208196.1,
                                           DRR138524.599183.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..476
                     /product="GPI-anchor transamidase component PIGT isoform 4
                     precursor"
                     /note="neurotrophin-regulated neuronal
                     development-associated protein; GPI transamidase subunit;
                     GPI transamidase component PIG-T; GPI-anchor transamidase
                     component PIGT; phosphatidylinositol-glycan biosynthesis
                     class T protein"
                     /calculated_mol_wt=52026
     sig_peptide     1..21
                     /calculated_mol_wt=2111
     mat_peptide     22..476
                     /product="GPI-anchor transamidase component PIGT isoform
                     4"
                     /calculated_mol_wt=52026
     Region          <63..449
                     /region_name="Gpi16"
                     /note="Gpi16 subunit, GPI transamidase component;
                     pfam04113"
                     /db_xref="CDD:461180"
     CDS             1..476
                     /gene="PIGT"
                     /gene_synonym="CGI-06; MCAHS3; NDAP; PIG-T; PNH2"
                     /coded_by="NM_001184730.3:17..1447"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS54466.1"
                     /db_xref="GeneID:51604"
                     /db_xref="HGNC:HGNC:14938"
                     /db_xref="MIM:610272"
ORIGIN      
        1 maaamplall vllllgpggw claepprdsl reelvitplp sgdvaatfqf rtrwdselqr
       61 egdtdhyflr yavlprevvc tenltpwkkl lpcsskagls vllkadrlfh tsyhsqavhi
      121 rpvcrnarct siswelrqtl svvfdafitg qgkkdwslfr mfsrtltepc plasesrvyv
      181 dittynqdne tlevhppptt tyqdvilgtr ktyaiydlld taminnsrnl niqlkwkrpp
      241 eneappvpfl haqryvsgyg lqkgelstll ynthpyrafp vllldtvpwy lrlyvhtlti
      301 tskgkenkps yihyqpaqdr lqphllemli qlpansvtkv siqferallk wteytpdpnh
      361 gfyvspsvls alvpsmvaak pvdweesplf nslfpvsdgs nyfvrlytep llvnlptpdf
      421 smpynviclt ctvvavcygs fynlltrtfh ieeprtggla krlanlirra rgvppl
//
LOCUS       NP_001244900             333 aa            linear   PRI 20-NOV-2025
DEFINITION  procathepsin L isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001244900
VERSION     NP_001244900.1
DBSOURCE    REFSEQ: accession NM_001257971.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Bestle,D., Bittel,L., Werner,A.D., Kamper,L., Dolnik,O.,
            Krahling,V., Steinmetzer,T. and Bottcher-Friebertshauser,E.
  TITLE     Novel proteolytic activation of Ebolavirus glycoprotein GP by
            TMPRSS2 and cathepsin L at an uncharted position can compensate for
            furin cleavage
  JOURNAL   Virus Res 347, 199430 (2024)
   PUBMED   38964470
  REMARK    GeneRIF: Novel proteolytic activation of Ebolavirus glycoprotein GP
            by TMPRSS2 and cathepsin L at an uncharted position can compensate
            for furin cleavage.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Wu,Y., Jiang,D., Liu,Q., Yan,S., Liu,X., Wu,T., Sun,W. and Li,G.
  TITLE     Cathepsin L induces cellular senescence by upregulating CUX1 and
            p16INK4a
  JOURNAL   Aging (Albany NY) 16 (13), 10749-10764 (2024)
   PUBMED   38944813
  REMARK    GeneRIF: Cathepsin L induces cellular senescence by upregulating
            CUX1 and p16[INK4a].
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Xu,J., Xu,W., Choi,J., Brhane,Y., Christiani,D.C., Kothari,J.,
            McKay,J., Field,J.K., Davies,M.P.A., Liu,G., Amos,C.I., Hung,R.J.
            and Briollais,L.
  TITLE     Large-scale whole exome sequencing studies identify two genes,CTSL
            and APOE, associated with lung cancer
  JOURNAL   PLoS Genet 19 (9), e1010902 (2023)
   PUBMED   37738239
  REMARK    GeneRIF: Large-scale whole exome sequencing studies identify two
            genes,CTSL and APOE, associated with lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Liu,P., Ju,M., Zheng,X., Jiang,Y., Yu,X., Pan,B., Luo,R., Jia,W.
            and Zheng,M.
  TITLE     Methyltransferase-like 3 promotes cervical cancer metastasis by
            enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner
  JOURNAL   Cancer Sci 114 (3), 837-854 (2023)
   PUBMED   36382580
  REMARK    GeneRIF: Methyltransferase-like 3 promotes cervical cancer
            metastasis by enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Goretzki,L., Schmitt,M., Mann,K., Calvete,J., Chucholowski,N.,
            Kramer,M., Gunzler,W.A., Janicke,F. and Graeff,H.
  TITLE     Effective activation of the proenzyme form of the urokinase-type
            plasminogen activator (pro-uPA) by the cysteine protease cathepsin
            L
  JOURNAL   FEBS Lett 297 (1-2), 112-118 (1992)
   PUBMED   1551416
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Cataldo,A.M., Paskevich,P.A., Kominami,E. and Nixon,R.A.
  TITLE     Lysosomal hydrolases of different classes are abnormally
            distributed in brains of patients with Alzheimer disease
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 10998-11002 (1991)
   PUBMED   1837142
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Mar 15;89(6):2509]
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Dunn,A.D., Crutchfield,H.E. and Dunn,J.T.
  TITLE     Thyroglobulin processing by thyroidal proteases. Major sites of
            cleavage by cathepsins B, D, and L
  JOURNAL   J Biol Chem 266 (30), 20198-20204 (1991)
   PUBMED   1939080
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Stearns,N.A., Dong,J.M., Pan,J.X., Brenner,D.A. and Sahagian,G.G.
  TITLE     Comparison of cathepsin L synthesized by normal and transformed
            cells at the gene, message, protein, and oligosaccharide levels
  JOURNAL   Arch Biochem Biophys 283 (2), 447-457 (1990)
   PUBMED   2275556
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Smith,C.G., Smith,M.T., Besch,N.F., Smith,R.G. and Asch,R.H.
  TITLE     Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive
            function
  JOURNAL   Adv Biosci 22-23, 449-467 (1978)
   PUBMED   116880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647435.1, BM680778.1 and
            CB963086.1.
            
            Summary: The protein encoded by this gene is a lysosomal cysteine
            proteinase that plays a major role in intracellular protein
            catabolism. Its substrates include collagen and elastin, as well as
            alpha-1 protease inhibitor, a major controlling element of
            neutrophil elastase activity. The encoded protein has been
            implicated in several pathologic processes, including myofibril
            necrosis in myopathies and in myocardial ischemia, and in the renal
            tubular response to proteinuria. This protein, which is a member of
            the peptidase C1 family, is a dimer composed of disulfide-linked
            heavy and light chains, both produced from a single protein
            precursor. Additionally, this protein cleaves the S1 subunit of the
            SARS-CoV-2 spike protein, which is necessary for entry of the virus
            into the cell. [provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (3) has an alternate splice site
            in the 5' UTR, compared to variant 1. Variants 1-4 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647435.1, BX649140.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in SARS-CoV-2 infection
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..333
                     /product="procathepsin L isoform 1 preproprotein"
                     /EC_number="3.4.22.15"
                     /note="major excreted protein; cathepsin L1; procathepsin
                     L"
                     /calculated_mol_wt=35876
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1706
     proprotein      18..333
                     /product="cathepsin L1 proprotein"
                     /calculated_mol_wt=35876
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Site            106..107
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            107..108
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            112..113
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            113..114
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Region          114..332
                     /region_name="Peptidase_C1"
                     /note="Papain family cysteine protease; pfam00112"
                     /db_xref="CDD:425470"
     mat_peptide     114..288
                     /product="cathepsin L1 heavy chain"
                     /calculated_mol_wt=19080
     Site            order(132,138,276,300)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            order(182..183,248,274,277,327)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     Site            221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P07711.2)"
     mat_peptide     292..333
                     /product="cathepsin L1 light chain"
                     /calculated_mol_wt=4776
     CDS             1..333
                     /gene="CTSL"
                     /gene_synonym="CATL; CTSL1; MEP"
                     /coded_by="NM_001257971.2:201..1202"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS6675.1"
                     /db_xref="GeneID:1514"
                     /db_xref="HGNC:HGNC:2537"
                     /db_xref="MIM:116880"
ORIGIN      
        1 mnptlilaaf clgiasatlt fdhsleaqwt kwkamhnrly gmneegwrra vweknmkmie
       61 lhnqeyregk hsftmamnaf gdmtseefrq vmngfqnrkp rkgkvfqepl fyeaprsvdw
      121 rekgyvtpvk nqgqcgscwa fsatgalegq mfrktgrlis lseqnlvdcs gpqgnegcng
      181 glmdyafqyv qdnggldsee sypyeatees ckynpkysva ndtgfvdipk qekalmkava
      241 tvgpisvaid aghesflfyk egiyfepdcs sedmdhgvlv vgygfestes dnnkywlvkn
      301 swgeewgmgg yvkmakdrrn hcgiasaasy ptv
//
LOCUS       NP_001354623             784 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform eee [Homo sapiens].
ACCESSION   NP_001354623
VERSION     NP_001354623.1
DBSOURCE    REFSEQ: accession NM_001367694.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 784)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 784)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 784)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 784)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 784)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 784)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 784)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 784)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 784)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 784)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.131810.1,
                                           SRR1660803.29642.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..784
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..784
                     /product="SUN domain-containing protein 1 isoform eee"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=86908
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <364..>588
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          416..469
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(416,419..420,423,426..427,430..431,433..434,
                     437..438,440..441,444..445,447..448,451,454..455,458,
                     461..462,465..466,468..469)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          546..604
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          647..782
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..784
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367694.1:52..2406"
                     /note="isoform eee is encoded by transcript variant 57"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllglslrgq gnffsflpvl nwasmhrtqr vddpqdvfkp ttsrlkqplq gdseafpwhw
      361 msgveqqvas lsgqchhhge nlrelttllq klqarvdqme ggaagpsasv rdavgqppre
      421 tdfmafhqeh evrmshledi lgklreksea iqkeleqtkq ktisavgeql lptvehlqle
      481 ldqlkselss wrhvktgcet vdavqervdv qvremvkllf sedqqggsle qllqrfssqf
      541 vskgdlqtml rdlqlqilrn vthhvsvtkq lptseavvsa vseagasgit eaqaraivns
      601 alklysqdkt gmvdfalesg ggsilstrcs etyetktalm slfgiplwyf sqsprvviqp
      661 diypgncwaf kgsqgylvvr lsmmihpaaf tlehipktls ptgnissapk dfavyglene
      721 yqeegqllgq ftydqdgesl qmfqalkrpd dtafqivelr ifsnwghpey tclyrfrvhg
      781 epvk
//
LOCUS       NP_004591                538 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein RO60 isoform 2 [Homo sapiens].
ACCESSION   NP_004591
VERSION     NP_004591.2
DBSOURCE    REFSEQ: accession NM_004600.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Song,Y., Wei,F., Liu,Y., Han,F., Ma,L., Zhuang,Y., Pan,C., Jia,Z.
            and Gong,A.
  TITLE     IL-33/ST2 Activation Is involved in Ro60-Regulated Photosensitivity
            in Cutaneous Lupus Erythematosus
  JOURNAL   Mediators Inflamm 2022, 4955761 (2022)
   PUBMED   35909659
  REMARK    GeneRIF: IL-33/ST2 Activation Is involved in Ro60-Regulated
            Photosensitivity in Cutaneous Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Lee,A.Y.S., Beroukas,D., Brown,L., Lucchesi,C., Kaur,A., Gyedu,L.,
            Hughes,N., Ng,Y.H., Saran,O., Gordon,T.P. and Wang,J.J.
  TITLE     Identification of a unique anti-Ro60 subset with restricted
            serological and molecular profiles
  JOURNAL   Clin Exp Immunol 203 (1), 13-21 (2021)
   PUBMED   32852779
  REMARK    GeneRIF: Identification of a unique anti-Ro60 subset with
            restricted serological and molecular profiles.
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Leng,Y., Sim,S., Magidson,V. and Wolin,S.L.
  TITLE     Noncoding Y RNAs regulate the levels, subcellular distribution and
            protein interactions of their Ro60 autoantigen partner
  JOURNAL   Nucleic Acids Res 48 (12), 6919-6930 (2020)
   PUBMED   32469055
  REMARK    GeneRIF: Noncoding Y RNAs regulate the levels, subcellular
            distribution and protein interactions of their Ro60 autoantigen
            partner.
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Barcellos,K.S., Nonogaki,S., Enokihara,M.M., Teixeira,M.S. and
            Andrade,L.E.
  TITLE     Differential expression of Ro/SSA 60 kDa and La/SSB, but not Ro/SSA
            52 kDa, mRNA and protein in minor salivary glands from patients
            with primary Sjogren's syndrome
  JOURNAL   J Rheumatol 34 (6), 1283-1292 (2007)
   PUBMED   17552056
  REMARK    GeneRIF: Increased Ro/SSA 60 and La/SSB mRNA expression in minor
            salivary glands in primary Sjogren's syndrome (pSS) suggest that
            these 2 autoantigens, but not Ro/SSA 52, are involved in
            tissue-specific autoimmune response in pSS.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Pruijn,G.J., Slobbe,R.L. and van Venrooij,W.J.
  TITLE     Analysis of protein--RNA interactions within Ro ribonucleoprotein
            complexes
  JOURNAL   Nucleic Acids Res 19 (19), 5173-5180 (1991)
   PUBMED   1833722
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Jitsukawa,T., Nakajima,S., Usui,J. and Watanabe,H.
  TITLE     Detection of anti-nuclear antibodies from patients with systemic
            rheumatic diseases by ELISA using HEp-2 cell nuclei
  JOURNAL   J Clin Lab Anal 5 (1), 49-53 (1991)
   PUBMED   1999763
REFERENCE   8  (residues 1 to 538)
  AUTHORS   James,J.A., Dickey,W.D., Fujisaku,A., O'Brien,C.A., Deutscher,S.L.,
            Keene,J.D. and Harley,J.B.
  TITLE     Antigenicity of a recombinant Ro (SS-A) fusion protein
  JOURNAL   Arthritis Rheum 33 (1), 102-106 (1990)
   PUBMED   1689160
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Ben-Chetrit,E., Gandy,B.J., Tan,E.M. and Sullivan,K.F.
  TITLE     Isolation and characterization of a cDNA clone encoding the 60-kD
            component of the human SS-A/Ro ribonucleoprotein autoantigen
  JOURNAL   J Clin Invest 83 (4), 1284-1292 (1989)
   PUBMED   2649513
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Deutscher,S.L., Harley,J.B. and Keene,J.D.
  TITLE     Molecular analysis of the 60-kDa human Ro ribonucleoprotein
  JOURNAL   Proc Natl Acad Sci U S A 85 (24), 9479-9483 (1988)
   PUBMED   3200833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX761715.1, BC036658.2 and AL136370.4.
            
            On Jun 4, 2003 this sequence version replaced NP_004591.1.
            
            Transcript Variant: This variant (2) differs in the 3' coding
            region and 3' UTR, compared to variant 1. The resulting isoform (2)
            has a distinct C-terminus and is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036658.2, SRR1660805.91438.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.2"
     Protein         1..538
                     /product="RNA-binding protein RO60 isoform 2"
                     /note="Sjogren syndrome antigen A2 (60kD,
                     ribonucleoprotein autoantigen SS-A/Ro); gastric cancer
                     multi-drug resistance protein; TROVE domain family member
                     2; 60 kDa ribonucleoprotein Ro; sjoegren syndrome type A
                     antigen; Ro/SSA 60kDa; ro60 autoantigen; RNA-binding
                     protein RO60"
                     /calculated_mol_wt=60540
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          17..369
                     /region_name="TROVE"
                     /note="TROVE domain; pfam05731"
                     /db_xref="CDD:461724"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          120..284
                     /region_name="RNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          361..538
                     /region_name="VWFA-like domain. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Region          <363..489
                     /region_name="ViaA"
                     /note="Uncharacterized conserved protein, contains a von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG2425"
                     /db_xref="CDD:441973"
     CDS             1..538
                     /gene="RO60"
                     /gene_synonym="RORNP; SSA2; TROVE2"
                     /coded_by="NM_004600.5:371..1987"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1379.1"
                     /db_xref="GeneID:6738"
                     /db_xref="HGNC:HGNC:11313"
                     /db_xref="MIM:600063"
ORIGIN      
        1 meesvnqmqp lnekqiansq dgyvwqvtdm nrlhrflcfg seggtyyike qklglenaea
       61 lirliedgrg ceviqeiksf sqegrttkqe pmlfalaics qcsdistkqa afkavsevcr
      121 ipthlftfiq fkkdlkesmk cgmwgralrk aiadwynekg gmalalavtk ykqrngwshk
      181 dllrlshlkp sseglaivtk yitkgwkevh elykekalsv etekllkyle avekvkrtrd
      241 elevihliee hrlvrehllt nhlkskevwk allqemplta llrnlgkmta nsvlepgnse
      301 vslvceklcn ekllkkarih pfhilialet yktghglrgk lkwrpdeeil kaldaafykt
      361 fktveptgkr fllavdvsas mnqrvlgsil nastvaaamc mvvtrtekds yvvafsdemv
      421 pcpvttdmtl qqvlmamsqi paggtdcslp miwaqktntp advfivftdn etfaggvhpa
      481 ialreyrkkm dipaklivcg mtsngftiad pddrgmldmc gfdtgaldvi rnftldmi
//
LOCUS       NP_001337610             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337610
VERSION     NP_001337610.1
DBSOURCE    REFSEQ: accession NM_001350681.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (17), as well as variants 1-4,
            9-16, and 18-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.1530.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350681.1:945..3155"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_065749                477 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane and coiled-coil domain protein 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_065749
VERSION     NP_065749.3
DBSOURCE    REFSEQ: accession NM_020698.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 477)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 477)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 477)
  AUTHORS   Wang,Y.H., Chan,Y.T., Hung,T.H., Hung,J.T., Kuo,M.W., Wang,S.H.,
            Huang,Y., Lin,Y.J., Chen,S.C., Yu,J.C., Wu,J.C., Yu,J. and Yu,A.L.
  TITLE     Transmembrane and coiled-coil domain family 3 (TMCC3) regulates
            breast cancer stem cell and AKT activation
  JOURNAL   Oncogene 40 (16), 2858-2871 (2021)
   PUBMED   33742122
  REMARK    GeneRIF: Transmembrane and coiled-coil domain family 3 (TMCC3)
            regulates breast cancer stem cell and AKT activation.
REFERENCE   4  (residues 1 to 477)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 477)
  AUTHORS   Wisesa,S., Yamamoto,Y. and Sakisaka,T.
  TITLE     TMCC3 localizes at the three-way junctions for the proper tubular
            network of the endoplasmic reticulum
  JOURNAL   Biochem J 476 (21), 3241-3260 (2019)
   PUBMED   31696206
  REMARK    GeneRIF: A TMCC3 mutant lacking the N-terminal coiled-coil domain
            abolished localization to tubular network of the endoplasmic
            reticulum, suggesting that TMCC3 localized independently of binding
            to atlastins.
REFERENCE   6  (residues 1 to 477)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 477)
  AUTHORS   Sohn,W.J., Kim,J.Y., Kim,D., Park,J.A., Lee,Y. and Kwon,H.J.
  TITLE     Expression and characterization of transmembrane and coiled-coil
            domain family 3
  JOURNAL   BMB Rep 49 (11), 629-634 (2016)
   PUBMED   27697108
  REMARK    GeneRIF: TMCC3 proteins are localized in endoplasmic reticulum
            through transmembrane domains and polymerized with other TMCC3
            protein an 1-3-3 proteins.
REFERENCE   8  (residues 1 to 477)
  AUTHORS   Zhang,C., Kho,Y.S., Wang,Z., Chiang,Y.T., Ng,G.K., Shaw,P.C.,
            Wang,Y. and Qi,R.Z.
  TITLE     Transmembrane and coiled-coil domain family 1 is a novel protein of
            the endoplasmic reticulum
  JOURNAL   PLoS One 9 (1), e85206 (2014)
   PUBMED   24454821
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 477)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026672.44.
            
            On Nov 23, 2018 this sequence version replaced NP_065749.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.221159.1,
                                           SRR1660805.4038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261226.9/ ENSP00000261226.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..477
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q22"
     Protein         1..477
                     /product="transmembrane and coiled-coil domain protein 3
                     isoform 1"
                     /note="transmembrane and coiled-coil domains 3;
                     transmembrane and coiled-coil domains protein 3;
                     transmembrane and coiled-coil domain protein 3"
                     /calculated_mol_wt=53654
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R310; propagated from
                     UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Region          64..463
                     /region_name="Tmemb_cc2"
                     /note="Predicted transmembrane and coiled-coil 2 protein;
                     pfam10267"
                     /db_xref="CDD:463036"
     Region          168..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Region          249..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R310; propagated from
                     UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     Site            450..470
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULS5.3)"
     CDS             1..477
                     /gene="TMCC3"
                     /coded_by="NM_020698.4:128..1561"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31877.1"
                     /db_xref="GeneID:57458"
                     /db_xref="HGNC:HGNC:29199"
                     /db_xref="MIM:617459"
ORIGIN      
        1 mpgsdtaltv drtysypgrh hrcksrverh dmntlslpln irrggsdtnl nfdvpdgild
       61 fhkvkltads lkqkilkvte qikieqtsrd gnvaeylklv nnadkqqagr ikqvfekknq
      121 ksahsiaqlq kkleqyhrkl reieqngasr sskdiskdhl kdihrslkda hvksrtaphc
      181 messksgmpg vsltppvfvf nksrefanli rnkfgsadni ahlknsleef rpeasarayg
      241 gsativnkpk ygsddecssg tsgsadsngn qsfgaggast ldsqgklavi leelreikdt
      301 qaqlaediea lkvqfkreyg fisqtlqeer yryerledql hdltdlhqhe tanlkqelas
      361 ieekvayqay ersrdiqeal escqtriskl elhqqeqqal qtdtvnakvl lgrcinvila
      421 fmtvilvcvs tiakfvspmm ksrchilgtf favtllaifc knwdhilcai ermiipr
//
LOCUS       NP_001186185             292 aa            linear   PRI 20-NOV-2025
DEFINITION  shugoshin 1 isoform 1KL [Homo sapiens].
ACCESSION   NP_001186185
VERSION     NP_001186185.1
DBSOURCE    REFSEQ: accession NM_001199256.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 292)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494477.1, AB193065.1 and
            AB187578.1.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (Sgo1K, PMID:15737064; also known
            as sSGO1, PMID:18331714) lacks an alternate in-frame exon in its
            central coding region, and contains an alternate 3' terminal
            segment compared to variant 1, resulting in a novel 3' coding
            region and distinct 3' UTR. It encodes isoform 1KL which is
            shorter, has a distinct internal amino acid, and has a distinct
            C-terminus, compared to isoform 1. Both variants Sgo1K and Sgo1L
            encode the same isoform (1KL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB193065.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..292
                     /product="shugoshin 1 isoform 1KL"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=33370
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          205..226
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     CDS             1..292
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001199256.3:267..1145"
                     /note="isoform 1KL is encoded by transcript variant Sgo1K"
                     /db_xref="CCDS:CCDS2635.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqieat ppetqqsphl slkditnvsl
      181 ypvvkirrls lspkknkasp avalpkrrct asvnykeptl asklrrgdpf tdlcflnspi
      241 fkqkkdlrrs kkralevspa keaifilyyv refvsrfpdc rkcklethic lr
//
LOCUS       NP_001349855            1072 aa            linear   PRI 20-NOV-2025
DEFINITION  arf-GAP with SH3 domain, ANK repeat and PH domain-containing
            protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001349855 XP_016868958
VERSION     NP_001349855.1
DBSOURCE    REFSEQ: accession NM_001362926.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1072)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1072)
  AUTHORS   Zhang,Y., Bai,H., Zhang,W., Gao,J., Gao,C., Deng,T., Liu,X.,
            Sun,X., Liu,Y., Wang,N. and Wu,Y.
  TITLE     miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1
  JOURNAL   Exp Cell Res 433 (2), 113828 (2023)
   PUBMED   37875175
  REMARK    GeneRIF: miR-212/132 attenuates OVA-induced airway inflammation by
            inhibiting mast cells activation through MRGPRX2 and ASAP1.
REFERENCE   3  (residues 1 to 1072)
  AUTHORS   Park,H., Son,H., Cha,H., Song,K., Bang,S., Jee,S., Kim,H.,
            Myung,J., Shin,S.J., Cha,C., Chung,M.S. and Paik,S.
  TITLE     ASAP1 Expression in Invasive Breast Cancer and Its Prognostic Role
  JOURNAL   Int J Mol Sci 24 (18), 14355 (2023)
   PUBMED   37762658
  REMARK    GeneRIF: ASAP1 Expression in Invasive Breast Cancer and Its
            Prognostic Role.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1072)
  AUTHORS   Barbagallo,C., Stella,M., Di Mauro,S., Scamporrino,A.,
            Filippello,A., Scionti,F., Di Martino,M.T., Purrello,M., Ragusa,M.,
            Purrello,F. and Piro,S.
  TITLE     An Uncharacterised lncRNA Coded by the ASAP1 Locus Is Downregulated
            in Serum of Type 2 Diabetes Mellitus Patients
  JOURNAL   Int J Mol Sci 24 (17), 13485 (2023)
   PUBMED   37686290
  REMARK    GeneRIF: An Uncharacterised lncRNA Coded by the ASAP1 Locus Is
            Downregulated in Serum of Type 2 Diabetes Mellitus Patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1072)
  AUTHORS   Xie,W., Han,Z., Zuo,Z., Xin,D., Chen,H., Huang,J., Zhu,S., Lou,H.,
            Yu,Z., Chen,C., Chen,S., Hu,Y., Huang,J., Zhang,F., Ni,Z., Shen,X.,
            Xue,X. and Lin,K.
  TITLE     ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer
  JOURNAL   Cell Death Dis 14 (2), 124 (2023)
   PUBMED   36792578
  REMARK    GeneRIF: ASAP1 activates the IQGAP1/CDC42 pathway to promote tumor
            progression and chemotherapy resistance in gastric cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1072)
  AUTHORS   Oshiro,T., Koyama,S., Sugiyama,S., Kondo,A., Onodera,Y.,
            Asahara,T., Sabe,H. and Kikuchi,A.
  TITLE     Interaction of POB1, a downstream molecule of small G protein Ral,
            with PAG2, a paxillin-binding protein, is involved in cell
            migration
  JOURNAL   J Biol Chem 277 (41), 38618-38626 (2002)
   PUBMED   12149250
  REMARK    GeneRIF: These results suggest that POB1 interacts with PAG2
            through its proline-rich motif, thereby regulating cell migration
            (PAG2).
REFERENCE   7  (residues 1 to 1072)
  AUTHORS   Scott,M.P., Zappacosta,F., Kim,E.Y., Annan,R.S. and Miller,W.T.
  TITLE     Identification of novel SH3 domain ligands for the Src family
            kinase Hck. Wiskott-Aldrich syndrome protein (WASP),
            WASP-interacting protein (WIP), and ELMO1
  JOURNAL   J Biol Chem 277 (31), 28238-28246 (2002)
   PUBMED   12029088
REFERENCE   8  (residues 1 to 1072)
  AUTHORS   Liu,Y., Loijens,J.C., Martin,K.H., Karginov,A.V. and Parsons,J.T.
  TITLE     The association of ASAP1, an ADP ribosylation factor-GTPase
            activating protein, with focal adhesion kinase contributes to the
            process of focal adhesion assembly
  JOURNAL   Mol Biol Cell 13 (6), 2147-2156 (2002)
   PUBMED   12058076
REFERENCE   9  (residues 1 to 1072)
  AUTHORS   Furman,C., Short,S.M., Subramanian,R.R., Zetter,B.R. and
            Roberts,T.M.
  TITLE     DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that
            enhances cell motility through a GAP-dependent mechanism
  JOURNAL   J Biol Chem 277 (10), 7962-7969 (2002)
   PUBMED   11773070
  REMARK    GeneRIF: DEF-1 alters cell motility through the deactivation of
            ARF1. In contrast, the inhibition of cell spreading by DEF-1 was
            not dependent on GAP activity, indicating that spreading and
            motility are altered by DEF-1 through different pathways.
REFERENCE   10 (residues 1 to 1072)
  AUTHORS   Brown,M.T., Andrade,J., Radhakrishna,H., Donaldson,J.G.,
            Cooper,J.A. and Randazzo,P.A.
  TITLE     ASAP1, a phospholipid-dependent arf GTPase-activating protein that
            associates with and is phosphorylated by Src
  JOURNAL   Mol Cell Biol 18 (12), 7038-7051 (1998)
   PUBMED   9819391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP005856.2, DA319233.1,
            BC144493.1, BG118567.1, DA416332.1, DA315979.1, BG748866.1,
            AB033075.1 and AI494058.1.
            
            On May 3, 2018 this sequence version replaced XP_016868958.1.
            
            Summary: This gene encodes an ADP-ribosylation factor (ARF)
            GTPase-activating protein. The GTPase-activating activity is
            stimulated by phosphatidylinositol 4,5-biphosphate (PIP2), and is
            greater towards ARF1 and ARF5, and lesser for ARF6. This gene maybe
            involved in regulation of membrane trafficking and cytoskeleton
            remodeling. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.220437.1,
                                           SRR7346977.2852774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1072
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21-q24.22"
     Protein         1..1072
                     /product="arf-GAP with SH3 domain, ANK repeat and PH
                     domain-containing protein 1 isoform 5"
                     /note="centaurin, beta 4; arf-GAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1; DEF-1;
                     PIP2-dependent ARF1 GAP; ARF GTPase-activating protein 1;
                     development and differentiation-enhancing factor 1;
                     ADP-ribosylation factor-directed GTPase-activating protein
                     1; 130 kDa phosphatidylinositol 4,5-biphosphate-dependent
                     ARF1 GTPase-activating protein; 130 kDa
                     phosphatidylinositol 4,5-bisphosphate-dependent ARF1
                     GTPase-activating protein"
                     /calculated_mol_wt=119605
     Region          54..268
                     /region_name="BAR_ASAP1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of ArfGAP with
                     SH3 domain, ANK repeat and PH domain containing protein 1;
                     cd07641"
                     /db_xref="CDD:153325"
     Site            order(63,66..67,71,73..74,77..78,80..81,91..92,94..95,
                     98..99,101..102,105,121,124..125,226,229..230,232,234,
                     237..238,240..241,247..248,251..252,254..255,258..259,
                     261..262)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153325"
     Region          316..422
                     /region_name="PH_ASAP"
                     /note="ArfGAP with SH3 domain, ankyrin repeat and PH
                     domain Pleckstrin homology (PH) domain; cd13251"
                     /db_xref="CDD:270071"
     Region          437..558
                     /region_name="ArfGap_ASAP1"
                     /note="ArfGAP domain of ASAP1 (ArfGAP with SH3 domain, ANK
                     repeat and PH domain-containing protein 1); cd08848"
                     /db_xref="CDD:350073"
     Site            order(440..441,444,467..469,490,498..502,504..506,
                     508..510,514..515,518..519,550,553..554)
                     /site_type="other"
                     /note="putative ANK repeat binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350073"
     Site            order(454,457,474,477,539)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:350073"
     Site            order(454,457,474,477,482)
                     /site_type="other"
                     /note="arginine finger"
                     /db_xref="CDD:350073"
     Site            order(479,482..483)
                     /site_type="other"
                     /note="putative GTP binding site [chemical binding]"
                     /db_xref="CDD:350073"
     Region          <582..693
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          601..634
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(602,606..607,610..612,617..618,622,625,634,636,638,
                     642..643,646..648,650..651,655,658,667,669,671,675..676,
                     679..681,683..684,688)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          636..667
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <727..1003
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1014..1070
                     /region_name="SH3_ASAP1"
                     /note="Src homology 3 domain of ArfGAP with SH3 domain,
                     ankyrin repeat and PH domain containing protein 1;
                     cd11965"
                     /db_xref="CDD:212898"
     Site            order(1019,1021,1024,1028,1046..1047,1063,1065..1066)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212898"
     CDS             1..1072
                     /gene="ASAP1"
                     /gene_synonym="AMAP1; CENTB4; DDEF1; PAG2; PAP; ZG14P"
                     /coded_by="NM_001362926.2:243..3461"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:50807"
                     /db_xref="HGNC:HGNC:2720"
                     /db_xref="MIM:605953"
ORIGIN      
        1 mrssasrlss fssrdslwnr mpdqisvsef iaettedyns pttssfttrl hncrntvtll
       61 eealdqdrta lqkvkksvka iynsgqdhvq neenyaqvld kfgsnflsrd npdlgtafvk
      121 fstltkelst llknllqgls hnviftldsl lkgdlkgvkg dlkkpfdkaw kdyetkftki
      181 ekekrehakq hgmirteitg aeiaeemeke rrlfqlqmce ylikvneikt kkgvdllqnl
      241 ikyyhaqcnf fqdglktadk lkqyieklaa dlynikqtqd eekkqltalr dliksslqld
      301 qkedsqsrqg gysmhqlqgn keygsekkgy llkksdgirk vwqrrkcsvk ngiltishat
      361 snrqpaklnl ltcqvkpnae dkksfdlish nrtyhfqaed eqdyvawisv ltnskeealt
      421 mafrgeqsag ensledltka iiedvqrlpg ndiccdcgss eptwlstnlg iltciecsgi
      481 hremgvhisr iqsleldklg tselllaknv gnnsfndime anlpspspkp tpssdmtvrk
      541 eyitakyvdh rfsrktcsts saklnellea iksrdllali qvyaegvelm epllepgqel
      601 getalhlavr tadqtslhlv dflvqncgnl dkqtalgntv lhycsmyskp eclklllrsk
      661 ptvdivnqag etaldiakrl katqcedlls qaksgkfnph vhveyewnlr qeeidesddd
      721 lddkpspikk ersprpqsfc hsssispqdk lalpgfstpr dkqrlsygaf tnqifvstst
      781 dsptspttea pplpprnagk gndggpssss kttnkfegls qqsstssakt algprvlpkl
      841 pqkvalrktd hlsldkatip peifqkssql aelpqkpppg dlppkptela pkpqigdlpp
      901 kpgelppkpq lgdlppkpql sdlppkpqmk dlppkpqlgd llaksqtgdv spkaqqpsev
      961 tlkshpldls pnvqsrdaiq kqasedsndl tptlpetpvp lprkintgkn kvrrvktiyd
     1021 cqadnddelt fiegeviivt geedqewwig hiegqperkg vfpvsfvhil sd
//
LOCUS       NP_061181                548 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptic vesicle 2-related protein [Homo sapiens].
ACCESSION   NP_061181
VERSION     NP_061181.1
DBSOURCE    REFSEQ: accession NM_018711.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Jeanguenin,L., Lara-Nunez,A., Rodionov,D.A., Osterman,A.L.,
            Komarova,N.Y., Rentsch,D., Gregory,J.F. 3rd and Hanson,A.D.
  TITLE     Comparative genomics and functional analysis of the NiaP family
            uncover nicotinate transporters from bacteria, plants, and mammals
  JOURNAL   Funct Integr Genomics 12 (1), 25-34 (2012)
   PUBMED   21953179
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Yao,J. and Bajjalieh,S.M.
  TITLE     SVOP is a nucleotide binding protein
  JOURNAL   PLoS One 4 (4), e5315 (2009)
   PUBMED   19390693
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Jacobsson,J.A., Haitina,T., Lindblom,J. and Fredriksson,R.
  TITLE     Identification of six putative human transporters with structural
            similarity to the drug transporter SLC22 family
  JOURNAL   Genomics 90 (5), 595-609 (2007)
   PUBMED   17714910
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Janz,R., Hofmann,K. and Sudhof,T.C.
  TITLE     SVOP, an evolutionarily conserved synaptic vesicle protein,
            suggests novel transport functions of synaptic vesicles
  JOURNAL   J Neurosci 18 (22), 9269-9281 (1998)
   PUBMED   9801366
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA793417.1, BC033587.1, AC087893.15, BC094722.1, BC037811.1 and
            DB297770.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.60343.1,
                                           SRR1803615.265571.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000610966.5/ ENSP00000479104.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..548
                     /product="synaptic vesicle 2-related protein"
                     /note="SV2 related protein homolog; solute carrier family
                     22 member B4"
                     /calculated_mol_wt=60638
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFT9; propagated from
                     UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFT9; propagated from
                     UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Region          87..509
                     /region_name="MFS_SVOP"
                     /note="Synaptic vesicle 2-related protein (SVOP) of the
                     Major Facilitator Superfamily; cd17441"
                     /db_xref="CDD:340999"
     Site            88..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            order(97..98,101..102,105,137,187..188,190..192,195,214,
                     217..218,221,324,327..328,331..333,336,383,387,436..437,
                     441,445,461,464..465,468..469,472)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340999"
     Site            123..143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            157..177
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            181..201
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            210..230
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            317..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            374..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            402..422
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            425..445
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            458..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            490..510
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4V2.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFT9; propagated from
                     UniProtKB/Swiss-Prot (Q8N4V2.1)"
     CDS             1..548
                     /gene="SVOP"
                     /gene_synonym="SLC22B4"
                     /coded_by="NM_018711.5:201..1847"
                     /db_xref="CCDS:CCDS73520.1"
                     /db_xref="GeneID:55530"
                     /db_xref="HGNC:HGNC:25417"
                     /db_xref="MIM:611699"
ORIGIN      
        1 meedlfqlrq lpvvkfrrtg esarseddta sgehevqieg vhvgleavel ddgaavpkef
       61 anptddtfmv edaveaigfg kfqwklsvlt glawmadame mmilsilapq lhcewrlpsw
      121 qvalltsvvf vgmmssstlw gnisdqygrk tglkisvlwt lyygilsafa pvyswilvlr
      181 glvgfgiggv pqsvtlyaef lpmkarakci llievfwaig tvfevvlavf vmpslgwrwl
      241 lilsavplll favlcfwlpe sarydvlsgn qekaiatlkr iatengapmp lgkliisrqe
      301 drgkmrdlft phfrwttlll wfiwfsnafs yyglvlltte lfqagdvcgi ssrkkaveak
      361 cslaceylse edymdllwtt lsefpgvlvt lwiidrlgrk ktmalcfvif sfcslllfic
      421 vgrnvltlll fiarafisgg fqaayvytpe vyptatralg lgtcsgmarv galitpfiaq
      481 vmlessvylt lavysgccll aalascflpi etkgrglqes shrewgqemv grgmhgagvt
      541 rsnsgsqe
//
LOCUS       NP_001306221             153 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-decapping enzyme 1B isoform 2 [Homo sapiens].
ACCESSION   NP_001306221
VERSION     NP_001306221.1
DBSOURCE    REFSEQ: accession NM_001319292.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Na,Z., Luo,Y., Schofield,J.A., Smelyansky,S., Khitun,A.,
            Muthukumar,S., Valkov,E., Simon,M.D. and Slavoff,S.A.
  TITLE     The NBDY Microprotein Regulates Cellular RNA Decapping
  JOURNAL   Biochemistry 59 (42), 4131-4142 (2020)
   PUBMED   33059440
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Tritschler,F., Braun,J.E., Motz,C., Igreja,C., Haas,G.,
            Truffault,V., Izaurralde,E. and Weichenrieder,O.
  TITLE     DCP1 forms asymmetric trimers to assemble into active mRNA
            decapping complexes in metazoa
  JOURNAL   Proc Natl Acad Sci U S A 106 (51), 21591-21596 (2009)
   PUBMED   19966221
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 153)
  AUTHORS   Cougot,N., Babajko,S. and Seraphin,B.
  TITLE     Cytoplasmic foci are sites of mRNA decay in human cells
  JOURNAL   J Cell Biol 165 (1), 31-40 (2004)
   PUBMED   15067023
REFERENCE   10 (residues 1 to 153)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC425587.1, AK301109.1,
            BM544996.1, BU930253.1, AC005342.1 and BQ773904.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function in removing the 5' cap from mRNAs, which is a step in
            regulated mRNA decay. This protein localizes to cytoplasmic foci
            which are the site of mRNA breakdown and turnover. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Transcript Variant: This variant (2) lacks multiple 3' coding exons
            and extends past a splice site used in variant 1, resulting in a
            different 3' coding region and 3' UTR. The encoded isoform (2) has
            a distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1055845.1,
                                           SRR1660803.211490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..153
                     /product="mRNA-decapping enzyme 1B isoform 2"
                     /EC_number="3.6.1.62"
                     /note="decapping enzyme hDcp1b; mRNA-decapping enzyme 1B;
                     DCP1 decapping enzyme homolog B"
                     /calculated_mol_wt=16979
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          16..108
                     /region_name="Dcp1"
                     /note="mRNA decapping enzyme 1 (Dcp1); cd09804"
                     /db_xref="CDD:197362"
     Site            order(17,19..20,23..24,34,36,58,75..77,80,82)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:197362"
     CDS             1..153
                     /gene="DCP1B"
                     /gene_synonym="DCP1"
                     /coded_by="NM_001319292.2:27..488"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81651.1"
                     /db_xref="GeneID:196513"
                     /db_xref="HGNC:HGNC:24451"
                     /db_xref="MIM:609843"
ORIGIN      
        1 maavaagglv gkgrdislaa lqrhdpyinr ivdvasqval ytfghranew ektdvegtlf
       61 vytrsaspkh gftimnrlsm enrtepitkd ldfqlqdpfl lyrnarcesf llqwvvlllk
      121 fgqvfkivqc lplclhlvsv amggvsiltn vnv
//
LOCUS       NP_065434                573 aa            linear   PRI 20-NOV-2025
DEFINITION  anti-Muellerian hormone type-2 receptor isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_065434
VERSION     NP_065434.1
DBSOURCE    REFSEQ: accession NM_020547.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Colaco,S., Achrekar,S., Patil,A., Sawant,U., Desai,S., Mangoli,V.,
            Jirge,P.R., Modi,D. and Mahale,S.D.
  TITLE     Association of AMH and AMHR2 gene polymorphisms with ovarian
            response and pregnancy outcomes in Indian women
  JOURNAL   J Assist Reprod Genet 39 (7), 1633-1642 (2022)
   PUBMED   35713750
  REMARK    GeneRIF: Association of AMH and AMHR2 gene polymorphisms with
            ovarian response and pregnancy outcomes in Indian women.
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Liu,Y., Wang,S., Lan,R. and Yang,J.
  TITLE     Identification of AMH and AMHR2 Variants Led to the Diagnosis of
            Persistent Mullerian Duct Syndrome in Three Cases
  JOURNAL   Genes (Basel) 13 (1), 159 (2022)
   PUBMED   35052499
  REMARK    GeneRIF: Identification of AMH and AMHR2 Variants Led to the
            Diagnosis of Persistent Mullerian Duct Syndrome in Three Cases.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Brunello,F.G. and Rey,R.A.
  TITLE     AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development
  JOURNAL   Sex Dev 16 (2-3), 138-146 (2022)
   PUBMED   34515230
  REMARK    GeneRIF: AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development.
            Review article
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Fang,J., Gao,G., Liu,J., Cai,L., Cui,Y. and Yang,X.
  TITLE     A novel mutation of AMHR2 in two brothers with persistent Mullerian
            duct syndrome and their intracytoplasmic sperm injection outcome
  JOURNAL   Mol Genet Genomic Med 9 (10), e1801 (2021)
   PUBMED   34480531
  REMARK    GeneRIF: A novel mutation of AMHR2 in two brothers with persistent
            Mullerian duct syndrome and their intracytoplasmic sperm injection
            outcome.
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Faure,E., Gouedard,L., Imbeaud,S., Cate,R., Picard,J.Y., Josso,N.
            and di Clemente,N.
  TITLE     Mutant isoforms of the anti-Mullerian hormone type II receptor are
            not expressed at the cell membrane
  JOURNAL   J Biol Chem 271 (48), 30571-30575 (1996)
   PUBMED   8940028
REFERENCE   7  (residues 1 to 573)
  AUTHORS   Imbeaud,S., Belville,C., Messika-Zeitoun,L., Rey,R., di
            Clemente,N., Josso,N. and Picard,J.Y.
  TITLE     A 27 base-pair deletion of the anti-mullerian type II receptor gene
            is the most common cause of the persistent mullerian duct syndrome
  JOURNAL   Hum Mol Genet 5 (9), 1269-1277 (1996)
   PUBMED   8872466
REFERENCE   8  (residues 1 to 573)
  AUTHORS   Teixeira,J. and Donahoe,P.K.
  TITLE     Molecular biology of MIS and its receptors
  JOURNAL   J Androl 17 (4), 336-341 (1996)
   PUBMED   8889695
  REMARK    Review article
REFERENCE   9  (residues 1 to 573)
  AUTHORS   Imbeaud,S., Faure,E., Lamarre,I., Mattei,M.G., di Clemente,N.,
            Tizard,R., Carre-Eusebe,D., Belville,C., Tragethon,L., Tonkin,C.,
            Nelson,J., McAuliffe,M., Bidart,J.M., Lababidi,A., Josso,N.,
            Cate,R.L. and Picard,J.Y.
  TITLE     Insensitivity to anti-mullerian hormone due to a mutation in the
            human anti-mullerian hormone receptor
  JOURNAL   Nat Genet 11 (4), 382-388 (1995)
   PUBMED   7493017
REFERENCE   10 (residues 1 to 573)
  AUTHORS   Visser,J.A., McLuskey,A., van Beers,T., Weghuis,D.O., van
            Kessel,A.G., Grootegoed,J.A. and Themmen,A.P.
  TITLE     Structure and chromosomal localization of the human anti-mullerian
            hormone type II receptor gene
  JOURNAL   Biochem Biophys Res Commun 215 (3), 1029-1036 (1995)
   PUBMED   7488027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB020573.1, AF172932.1,
            AC068889.35 and AJ572328.1.
            
            Summary: This gene encodes the receptor for the anti-Mullerian
            hormone (AMH) which, in addition to testosterone, results in male
            sex differentiation. AMH and testosterone are produced in the
            testes by different cells and have different effects. Testosterone
            promotes the development of male genitalia while the binding of AMH
            to the encoded receptor prevents the development of the mullerian
            ducts into uterus and Fallopian tubes. Mutations in this gene are
            associated with persistent Mullerian duct syndrome type II.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF172932.1, BC126316.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257863.9/ ENSP00000257863.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..573
                     /product="anti-Muellerian hormone type-2 receptor isoform
                     1 precursor"
                     /EC_number="2.7.11.30"
                     /note="Mullerian inhibiting substance type II receptor;
                     MIS type II receptor; AMH type II receptor;
                     anti-Muellerian hormone type II receptor; Muellerian
                     inhibiting substance type II receptor; anti-Mullerian
                     hormone receptor, type II"
                     /calculated_mol_wt=61026
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1742
     mat_peptide     18..573
                     /product="Anti-Muellerian hormone type-2 receptor.
                     /id=PRO_0000024408"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16671.1)"
                     /calculated_mol_wt=61026
     Region          22..121
                     /region_name="TFP_LU_ECD_AMHR2"
                     /note="extracellular domain (ECD) found in anti-Muellerian
                     hormone type-2 receptor (AMHR2) and similar proteins;
                     cd23616"
                     /db_xref="CDD:467136"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16671.1)"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16671.1)"
     Site            150..170
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16671.1)"
     Region          207..508
                     /region_name="STKc_BMPR2_AMHR2"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     Bone Morphogenetic Protein and Anti-Muellerian Hormone
                     Type II Receptors; cd14054"
                     /db_xref="CDD:270956"
     Site            order(209..213,217,228,230,258,279..282,286,288,333,335,
                     337..338,340,351,354,382..385)
                     /site_type="active"
                     /db_xref="CDD:270956"
     Site            order(209..215,217,228,230,279..280,282,286,337..338,340,
                     351)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270956"
     Site            order(213,286,288,333,335,337,354,382..385)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270956"
     Site            order(350..360,373..385)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270956"
     CDS             1..573
                     /gene="AMHR2"
                     /gene_synonym="AMHR; MISR2; MISRII; MRII"
                     /coded_by="NM_020547.3:81..1802"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8858.1"
                     /db_xref="GeneID:269"
                     /db_xref="HGNC:HGNC:465"
                     /db_xref="MIM:600956"
ORIGIN      
        1 mlgslglwal lptaveappn rrtcvffeap gvrgstktlg elldtgtelp rairclysrc
       61 cfgiwnltqd raqvemqgcr dsdepgcesl hcdpsprahp spgstlftcs cgtdfcnany
      121 shlpppgspg tpgsqgpqaa pgesiwmalv llglflllll llgsiilall qrknyrvrge
      181 pvpeprpdsg rdwsvelqel pelcfsqvir egghavvwag qlqgklvaik afpprsvaqf
      241 qaeralyelp glqhdhivrf itasrggpgr llsgpllvle lhpkgslchy ltqytsdwgs
      301 slrmalslaq glaflheerw qngqykpgia hrdlssqnvl iredgscaig dlglalvlpg
      361 ltqppawtpt qpqgpaaime agtqrymape lldktldlqd wgmalrradi yslalllwei
      421 lsrcpdlrpd sspppfqlay eaelgntpts delwalavqe rrrpyipstw rcfatdpdgl
      481 relledcwda dpearltaec vqqrlaalah pqeshpfpes cprgcpplcp edctsipapt
      541 ilpcrpqrsa chfsvqqgpc srnpqpactl spv
//
LOCUS       NP_001164977             146 aa            linear   PRI 20-NOV-2025
DEFINITION  multiple coagulation factor deficiency protein 2 isoform A
            precursor [Homo sapiens].
ACCESSION   NP_001164977
VERSION     NP_001164977.1
DBSOURCE    REFSEQ: accession NM_001171506.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Zhang,Y., Liu,Z. and Zhang,B.
  TITLE     Separate roles of LMAN1 and MCFD2 in ER-to-Golgi trafficking of FV
            and FVIII
  JOURNAL   Blood Adv 7 (7), 1286-1296 (2023)
   PUBMED   36490287
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Zhang,Y., Zhu,M., Zheng,C., Wei,W., Emmer,B.T. and Zhang,B.
  TITLE     LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi transport
            of alpha1-antitrypsin
  JOURNAL   Biochem J 479 (7), 839-855 (2022)
   PUBMED   35322856
  REMARK    GeneRIF: LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi
            transport of alpha1-antitrypsin.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Guy,J.E., Wigren,E., Svard,M., Hard,T. and Lindqvist,Y.
  TITLE     New insights into multiple coagulation factor deficiency from the
            solution structure of human MCFD2
  JOURNAL   J Mol Biol 381 (4), 941-955 (2008)
   PUBMED   18590741
  REMARK    GeneRIF: These results provide an explanation for the previously
            observed calcium dependence of the MCFD2-ERGIC-53 interaction.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Mohanty,D., Ghosh,K., Shetty,S., Spreafico,M., Garagiola,I. and
            Peyvandi,F.
  TITLE     Mutations in the MCFD2 gene and a novel mutation in the LMAN1 gene
            in Indian families with combined deficiency of factor V and VIII
  JOURNAL   Am J Hematol 79 (4), 262-266 (2005)
   PUBMED   16044454
  REMARK    GeneRIF: Mutations in (LMAN1) and (MCFD2), have been found to be
            responsible for the dual deficiency of FV and FVIII.
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Zhang,B., Cunningham,M.A., Nichols,W.C., Bernat,J.A., Seligsohn,U.,
            Pipe,S.W., McVey,J.H., Schulte-Overberg,U., de Bosch,N.B.,
            Ruiz-Saez,A., White,G.C., Tuddenham,E.G., Kaufman,R.J. and
            Ginsburg,D.
  TITLE     Bleeding due to disruption of a cargo-specific ER-to-Golgi
            transport complex
  JOURNAL   Nat Genet 34 (2), 220-225 (2003)
   PUBMED   12717434
  REMARK    GeneRIF: inactivating mutations in MCFD2 cause combined deficiency
            of factor V and factor VIII with a phenotype indistinguishable from
            that caused by mutations in LMAN1
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Nichols,W.C., Terry,V.H., Wheatley,M.A., Yang,A., Zivelin,A.,
            Ciavarella,N., Stefanile,C., Matsushita,T., Saito,H., de
            Bosch,N.B., Ruiz-Saez,A., Torres,A., Thompson,A.R., Feinstein,D.I.,
            White,G.C., Negrier,C., Vinciguerra,C., Aktan,M., Kaufman,R.J.,
            Ginsburg,D. and Seligsohn,U.
  TITLE     ERGIC-53 gene structure and mutation analysis in 19 combined
            factors V and VIII deficiency families
  JOURNAL   Blood 93 (7), 2261-2266 (1999)
   PUBMED   10090935
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Neerman-Arbez,M., Johnson,K.M., Morris,M.A., McVey,J.H.,
            Peyvandi,F., Nichols,W.C., Ginsburg,D., Rossier,C.,
            Antonarakis,S.E. and Tuddenham,E.G.
  TITLE     Molecular analysis of the ERGIC-53 gene in 35 families with
            combined factor V-factor VIII deficiency
  JOURNAL   Blood 93 (7), 2253-2260 (1999)
   PUBMED   10090934
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Deka,N., Wong,E., Matera,A.G., Kraft,R., Leinwand,L.A. and
            Schmid,C.W.
  TITLE     Repetitive nucleotide sequence insertions into a novel
            calmodulin-related gene and its processed pseudogene
  JOURNAL   Gene 71 (1), 123-134 (1988)
   PUBMED   2463956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA324623.1, DA330030.1,
            CF994192.1, AF537214.1 and AI371370.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a soluble luminal protein with two
            calmodulin-like EF-hand motifs at its C-terminus. This protein
            forms a complex with LMAN1 (lectin mannose binding protein 1; also
            known as ERGIC-53) that facilitates the transport of coagulation
            factors V (FV) and VIII (FVIII) from the endoplasmic reticulum to
            the Golgi apparatus via an endoplasmic reticulum Golgi intermediate
            compartment (ERGIC). Mutations in this gene cause combined
            deficiency of FV and FVIII (F5F8D); a rare autosomal recessive
            bleeding disorder characterized by mild to moderate bleeding and
            coordinate reduction in plasma FV and FVIII levels. This protein
            has also been shown to maintain stem cell potential in adult
            central nervous system and is a marker for testicular germ cell
            tumors. The 3' UTR of this gene contains a transposon-like human
            repeat element named 'THE 1'. A processed RNA pseudogene of this
            gene is on chromosome 6p22.1. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms. [provided
            by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, 3 and 4 encode the same
            isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.118096.1,
                                           SRR1660803.241586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..146
                     /product="multiple coagulation factor deficiency protein 2
                     isoform A precursor"
                     /note="neural stem cell-derived neuronal survival protein"
                     /calculated_mol_wt=13525
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2884
     Region          77..143
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K5B3; propagated from
                     UniProtKB/Swiss-Prot (Q8NI22.1)"
     CDS             1..146
                     /gene="MCFD2"
                     /gene_synonym="F5F8D; F5F8D2; LMAN1IP; SDNSF"
                     /coded_by="NM_001171506.2:247..687"
                     /note="isoform A precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS33192.1"
                     /db_xref="GeneID:90411"
                     /db_xref="HGNC:HGNC:18451"
                     /db_xref="MIM:607788"
ORIGIN      
        1 mtmrsllrtp flcgllwafc apgaraeepa asfsqpgsmg ldkntvhdqe himehlegvi
       61 nkpeaemspq elqlhyfkmh dydgnnlldg lelstaithv hkeegseqap lmsedelini
      121 idgvlrdddk nndgyidyae fakslq
//
LOCUS       NP_001229430             222 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 4 [Homo sapiens].
ACCESSION   NP_001229430
VERSION     NP_001229430.1
DBSOURCE    REFSEQ: accession NM_001242501.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CA488406.1 and BC033759.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (4), as well as variants 7-10,
            encodes isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CA488406.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2161836,
                                           SAMN03267777 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..222
                     /product="MIF4G domain-containing protein isoform 4"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=25292
     Region          8..179
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..222
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001242501.1:61..729"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS56044.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqaeskqa gqsvfrrgll nrlqqeyqar eqlrarslqg wvcyvtficn ifdylrvnnm
      121 pmmalvnpvy dclfrlaqpd slskeeevdc lvlqlhrvge qlekmngqrm delfvlirdg
      181 fllptglssl aqlllleiie fraagwkttp aahkyyysev sd
//
LOCUS       NP_001306609             538 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-1 isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001306609 XP_011537038
VERSION     NP_001306609.1
DBSOURCE    REFSEQ: accession NM_001319680.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Xu,X., Gao,F., Wang,J., Long,C., Tao,L., Ding,L. and Ji,Y.
  TITLE     microRNA-216a-5p inhibits the development of gastric cancer through
            target combination with TCTN1
  JOURNAL   Minerva Med 114 (3), 323-331 (2023)
   PUBMED   32486612
  REMARK    GeneRIF: microRNA-216a-5p inhibits the development of gastric
            cancer through target combination with TCTN1.
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Bai,G., Wei,N., Li,F., Zhao,P., Meng,Z., Zou,B., Liu,Y., Xu,K.,
            Li,K., Yao,C. and Yang,P.
  TITLE     Function and transcriptional regulation of TCTN1 in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 47 (2) (2022)
   PUBMED   34859261
  REMARK    GeneRIF: Function and transcriptional regulation of TCTN1 in oral
            squamous cell carcinoma.
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Wang,H., Jiang,W., Dai,M., Xiao,B., Xu,Y., Sun,Y., Liu,Y., Ying,X.,
            Sun,Y., Wei,W. and Ji,X.
  TITLE     [Diagnosis of two cases from one family with Joubert syndrome
            caused by novel mutations of TCTN1 gene by whole exome sequencing]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 36 (7), 686-689 (2019)
   PUBMED   31302911
  REMARK    GeneRIF: Two novel TCTN1 mutations were identified in a family with
            Joubert syndrome
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Alazami,A.M., Alshammari,M.J., Salih,M.A., Alzahrani,F., Hijazi,H.,
            Seidahmed,M.Z., Abu Safieh,L., Aldosary,M., Khan,A.O. and
            Alkuraya,F.S.
  TITLE     Molecular characterization of Joubert syndrome in Saudi Arabia
  JOURNAL   Hum Mutat 33 (10), 1423-1428 (2012)
   PUBMED   22693042
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    GeneRIF: Mutations in Tctn1 is associated with ciliopathies.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002350.1 and AC144522.12.
            
            On Feb 4, 2016 this sequence version replaced XP_011537038.1.
            
            Summary: This gene encodes a member of a family of secreted and
            transmembrane proteins. The orthologous gene in mouse functions
            downstream of smoothened and rab23 to modulate hedgehog signal
            transduction. This protein is a component of the tectonic-like
            complex, which forms a barrier between the ciliary axoneme and the
            basal body. A mutation in this gene was found in a family with
            Joubert syndrome-13. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (6) lacks an in-frame exon and
            uses two alternate in-frame splice sites in the 3' coding region
            compared to variant 1. The resulting isoform (6) is shorter than
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.360485.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..538
                     /product="tectonic-1 isoform 6 precursor"
                     /calculated_mol_wt=55854
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2336
     Region          78..387
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..538
                     /gene="TCTN1"
                     /gene_synonym="JBTS13; TECT1"
                     /coded_by="NM_001319680.2:55..1671"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS91749.1"
                     /db_xref="GeneID:79600"
                     /db_xref="HGNC:HGNC:26113"
                     /db_xref="MIM:609863"
ORIGIN      
        1 mrprglppll vvllgcwasv saqtdatpav tteglnstea alatfgtfps trppgtprap
       61 gpssgprptp vtdvavlcvc dlspaqcdin cccdpdcssv dfsvfsacsv pvvtgdsqfc
      121 sqkaviysln ftanppqrvf elvdqinpsi fcihitnykp alsfinpevp dennfdtlmk
      181 tsdgftlnae syvsfttkld iptaakyeyg vplqtsdsfl rfpssltssl ctdnnpaafl
      241 vnqavkctrk inleqceeie alsmafyssp eilrvpdsrk kvpitvqsiv iqslnktltr
      301 redtdvlqpt lvnaghfslc vnvvlevkys ltytdagevt kadlsfvlgt vssvvvplqq
      361 kfeihflqen tqpvplsgnp gyvvglplaa gfqphkggal pcqlvaqkvk sllwgqgfpd
      421 yvapfgnsqa qdmldwvpih fitqsfnrkd scqlpgalvi evkwtkygsl lnpqakivnv
      481 tanlisssfp eansgnerti listavtfvd vsapaeagfr appainarlp fnfffpfv
//
LOCUS       NP_003204                434 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional enhancer factor TEF-3 isoform 1 [Homo sapiens].
ACCESSION   NP_003204
VERSION     NP_003204.2
DBSOURCE    REFSEQ: accession NM_003213.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Li,F., Wang,X., Zhang,J., Zhang,J., Jing,X., Jiang,Q., Zhou,J.,
            Cao,L., Peng,H., Tong,D. and Huang,C.
  TITLE     RBM8A, a new target of TEAD4, promotes breast cancer progression by
            regulating IGF1R and IRS-2
  JOURNAL   J Transl Med 22 (1), 823 (2024)
   PUBMED   39232805
  REMARK    GeneRIF: RBM8A, a new target of TEAD4, promotes breast cancer
            progression by regulating IGF1R and IRS-2.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Tan,K., Wang,J., Su,X., Zheng,Y. and Li,W.
  TITLE     KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by regulating
            the RANKL/OPG ratio on the compression side during orthodontic
            tooth movement
  JOURNAL   Prog Orthod 25 (1), 29 (2024)
   PUBMED   39129034
  REMARK    GeneRIF: KAT6A/YAP/TEAD4 pathway modulates osteoclastogenesis by
            regulating the RANKL/OPG ratio on the compression side during
            orthodontic tooth movement.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Chan,S.W., Lim,C.J., Huang,C., Chong,Y.F., Gunaratne,H.J.,
            Hogue,K.A., Blackstock,W.P., Harvey,K.F. and Hong,W.
  TITLE     WW domain-mediated interaction with Wbp2 is important for the
            oncogenic property of TAZ
  JOURNAL   Oncogene 30 (5), 600-610 (2011)
   PUBMED   20972459
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Appukuttan,B., McFarland,T.J., Davies,M.H., Atchaneeyasakul,L.O.,
            Zhang,Y., Babra,B., Pan,Y., Rosenbaum,J.T., Acott,T., Powers,M.R.
            and Stout,J.T.
  TITLE     Identification of novel alternatively spliced isoforms of RTEF-1
            within human ocular vascular endothelial cells and murine retina
  JOURNAL   Invest Ophthalmol Vis Sci 48 (8), 3775-3782 (2007)
   PUBMED   17652751
  REMARK    GeneRIF: Novel RTEF-1 transcripts are present within human ocular
            vascular endothelial cells and mouse neural retina during normal
            and retinopathy of prematurity development, and alternatively
            spliced products are produced under hyperoxic and hypoxic
            conditions
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Vassilev,A., Kaneko,K.J., Shu,H., Zhao,Y. and DePamphilis,M.L.
  TITLE     TEAD/TEF transcription factors utilize the activation domain of
            YAP65, a Src/Yes-associated protein localized in the cytoplasm
  JOURNAL   Genes Dev 15 (10), 1229-1241 (2001)
   PUBMED   11358867
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Jacquemin,P., Depetris,D., Mattei,M.G., Martial,J.A. and
            Davidson,I.
  TITLE     Localization of human transcription factor TEF-4 and TEF-5 (TEAD2,
            TEAD3) genes to chromosomes 19q13.3 and 6p21.2 using fluorescence
            in situ hybridization and radiation hybrid analysis
  JOURNAL   Genomics 55 (1), 127-129 (1999)
   PUBMED   9889009
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Stewart,A.F., Richard,C.W. 3rd, Suzow,J., Stephan,D.,
            Weremowicz,S., Morton,C.C. and Adra,C.N.
  TITLE     Cloning of human RTEF-1, a transcriptional enhancer
            factor-1-related gene preferentially expressed in skeletal muscle:
            evidence for an ancient multigene family
  JOURNAL   Genomics 37 (1), 68-76 (1996)
   PUBMED   8921372
  REMARK    GeneRIF: The paper described several reasons to designate the
            putative translation initiation codon as the leucine (TTG) codon,
            which is 7 codons upstream from the isoleucine (ATT) codon.
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Jacquemin,P., Hwang,J.J., Martial,J.A., Dolle,P. and Davidson,I.
  TITLE     A novel family of developmentally regulated mammalian transcription
            factors containing the TEA/ATTS DNA binding domain
  JOURNAL   J Biol Chem 271 (36), 21775-21785 (1996)
   PUBMED   8702974
  REMARK    GeneRIF: The paper described that the ORF of TEF-3 initiates with
            an ATT codon encoding isoleucine.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA210894.1, BC015497.1 and
            U63824.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 20, 2004 this sequence version replaced NP_003204.1.
            
            Summary: This gene product is a member of the transcriptional
            enhancer factor (TEF) family of transcription factors, which
            contain the TEA/ATTS DNA-binding domain. It is preferentially
            expressed in the skeletal muscle, and binds to the M-CAT regulatory
            element found in promoters of muscle-specific genes to direct their
            gene expression. Alternatively spliced transcripts encoding
            distinct isoforms, some of which are translated through the use of
            a non-AUG (UUG) initiation codon, have been described for this
            gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1), and initiates translation from a non-AUG (UUG) codon.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U63824.1, BC015497.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match       :: ENST00000359864.8/ ENSP00000352926.3
            non-AUG initiation codon :: PMID: 8921372
            RefSeq Select criteria   :: based on conservation, expression,
                                        longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..434
                     /product="transcriptional enhancer factor TEF-3 isoform 1"
                     /note="transcriptional enhancer factor 3; transcription
                     factor 13-like 1; related transcription enhancer factor
                     1B; transcriptional enhancer factor TEF-3; transcriptional
                     enhancer factor 1-related; transcription factor RTEF-1;
                     TEA domain family member 4"
                     /calculated_mol_wt=48198
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15561.3)"
     Region          38..105
                     /region_name="TEA"
                     /note="TEA domain; smart00426"
                     /db_xref="CDD:128703"
     Region          188..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15561.3)"
     Region          222..431
                     /region_name="YBD"
                     /note="YAP binding domain; pfam17725"
                     /db_xref="CDD:435993"
     CDS             1..434
                     /gene="TEAD4"
                     /gene_synonym="EFTR-2; hRTEF-1B; RTEF1; TCF13L1; TEF-3;
                     TEF3; TEFR-1"
                     /coded_by="NM_003213.4:208..1512"
                     /note="isoform 1 is encoded by transcript variant 1;
                     non-AUG (UUG) translation initiation codon"
                     /db_xref="CCDS:CCDS31729.1"
                     /db_xref="GeneID:7004"
                     /db_xref="HGNC:HGNC:11717"
                     /db_xref="MIM:601714"
ORIGIN      
        1 megtagtits newssptspe gstasggsqa ldkpidndae gvwspdieqs fqealaiypp
       61 cgrrkiilsd egkmygrnel iaryiklrtg ktrtrkqvss hiqvlarrka reiqaklkdq
      121 aakdkalqsm aamssaqiis atafhssmal argpgrpavs gfwqgalpgq agtshdvkpf
      181 sqqtyavqpp lplpgfespa gpapspsapp appwqgrsva ssklwmlefs afleqqqdpd
      241 tynkhlfvhi gqsspsysdp yleavdirqi ydkfpekkgg lkdlfergps nafflvkfwa
      301 dlntniedeg ssfygvssqy espenmiitc stkvcsfgkq vvekveteya ryenghysyr
      361 ihrsplceym infihklkhl pekymmnsvl enftilqvvt nrdtqetllc iayvfevsas
      421 ehgaqhhiyr lvke
//
LOCUS       NP_001356515             648 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform z [Homo sapiens].
ACCESSION   NP_001356515
VERSION     NP_001356515.1
DBSOURCE    REFSEQ: accession NM_001369586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 648)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 648)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 648)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 648)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 648)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 648)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 648)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 648)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 648)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 648)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.187179.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..648
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..648
                     /product="transcription factor 4 isoform z"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=69054
     Region          539..623
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(547,551,553..555,557,562,583..584)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(560..561,564..565,567..568,571,575,585,588,592,595,
                     598..603)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..648
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369586.1:516..2462"
                     /note="isoform z is encoded by transcript variant 46"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsgtgtavws rnggqasssp nyegplhslq
      361 sriedrlerl ddaihvlrnh avgpstampg ghgdmhgiig pshngamggl gsgygtglls
      421 anrhslmvgt hredgvalrg shsllpnqvp vpqlpvqsat spdlnppqdp yrgmppglqg
      481 qsvssgssei ksddegdenl qdtkssedkk ldddkkdiks itrsrssnnd dedltpeqka
      541 erekerrman narerlrvrd ineafkelgr mvqlhlksdk pqtkllilhq avavilsleq
      601 qvrernlnpk aaclkrreee kvssepppls lagphpgmgd asnhmgqm
//
LOCUS       NP_001354846             614 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholinesterase isoform E4-E6 precursor [Homo sapiens].
ACCESSION   NP_001354846 XP_024302538
VERSION     NP_001354846.1
DBSOURCE    REFSEQ: accession NM_001367917.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   Kongkaew,N., Hengphasatporn,K., Shigeta,Y., Rungrotmongkol,T. and
            Harada,R.
  TITLE     Preferential Door for Ligand Binding and Unbinding Pathways in
            Inhibited Human Acetylcholinesterase
  JOURNAL   J Phys Chem Lett 15 (21), 5696-5704 (2024)
   PUBMED   38768263
  REMARK    GeneRIF: Preferential Door for Ligand Binding and Unbinding
            Pathways in Inhibited Human Acetylcholinesterase.
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Chen,M., Zhang,C., Li,H., Zheng,S., Li,Y., Yuan,M., Chen,Y., Wu,J.
            and Sun,Q.
  TITLE     PLA2G4A and ACHE modulate lipid profiles via glycerophospholipid
            metabolism in platinum-resistant gastric cancer
  JOURNAL   J Transl Med 22 (1), 249 (2024)
   PUBMED   38454407
  REMARK    GeneRIF: PLA2G4A and ACHE modulate lipid profiles via
            glycerophospholipid metabolism in platinum-resistant gastric
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 614)
  AUTHORS   Joda,M., Waters,K.A. and Machaalani,R.
  TITLE     Choline-acetyltransferase (ChAT) and acetylcholinesterase (AChE) in
            the human infant dorsal motor nucleus of the Vagus (DMNV), and
            alterations according to sudden infant death syndrome (SIDS)
            category
  JOURNAL   Neurobiol Dis 188, 106319 (2023)
   PUBMED   37813167
  REMARK    GeneRIF: Choline-acetyltransferase (ChAT) and acetylcholinesterase
            (AChE) in the human infant dorsal motor nucleus of the Vagus
            (DMNV), and alterations according to sudden infant death syndrome
            (SIDS) category.
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Budhbhatti,U., Chauhan,A., Bhatt,D., Parmar,C., Damani,V., Patel,A.
            and Joshi,C.
  TITLE     Association of NOTCH4 and ACHE gene polymorphism in Alzheimer's
            disease of Gujarat cohort
  JOURNAL   Neurosci Lett 814, 137428 (2023)
   PUBMED   37544578
  REMARK    GeneRIF: Association of NOTCH4 and ACHE gene polymorphism in
            Alzheimer's disease of Gujarat cohort.
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Ohno,K., Brengman,J., Tsujino,A. and Engel,A.G.
  TITLE     Human endplate acetylcholinesterase deficiency caused by mutations
            in the collagen-like tail subunit (ColQ) of the asymmetric enzyme
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9654-9659 (1998)
   PUBMED   9689136
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Bartels,C.F., Zelinski,T. and Lockridge,O.
  TITLE     Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene
            accounts for YT blood group polymorphism
  JOURNAL   Am J Hum Genet 52 (5), 928-936 (1993)
   PUBMED   8488842
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Spring,F.A., Gardner,B. and Anstee,D.J.
  TITLE     Evidence that the antigens of the Yt blood group system are located
            on human erythrocyte acetylcholinesterase
  JOURNAL   Blood 80 (8), 2136-2141 (1992)
   PUBMED   1391965
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Shafferman,A., Kronman,C., Flashner,Y., Leitner,M., Grosfeld,H.,
            Ordentlich,A., Gozes,Y., Cohen,S., Ariel,N., Barak,D. et al.
  TITLE     Mutagenesis of human acetylcholinesterase. Identification of
            residues involved in catalytic activity and in polypeptide folding
  JOURNAL   J Biol Chem 267 (25), 17640-17648 (1992)
   PUBMED   1517212
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Ehrlich,G., Viegas-Pequignot,E., Ginzberg,D., Sindel,L., Soreq,H.
            and Zakut,H.
  TITLE     Mapping the human acetylcholinesterase gene to chromosome 7q22 by
            fluorescent in situ hybridization coupled with selective PCR
            amplification from a somatic hybrid cell panel and
            chromosome-sorted DNA libraries
  JOURNAL   Genomics 13 (4), 1192-1197 (1992)
   PUBMED   1380483
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Getman,D.K., Eubanks,J.H., Camp,S., Evans,G.A. and Taylor,P.
  TITLE     The human gene encoding acetylcholinesterase is located on the long
            arm of chromosome 7
  JOURNAL   Am J Hum Genet 51 (1), 170-177 (1992)
   PUBMED   1609795
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011895.4.
            
            On Dec 29, 2018 this sequence version replaced XP_024302538.1.
            
            Summary: Acetylcholinesterase hydrolyzes the neurotransmitter,
            acetylcholine at neuromuscular junctions and brain cholinergic
            synapses, and thus terminates signal transmission. It is also found
            on the red blood cell membranes, where it constitutes the Yt blood
            group antigen. Acetylcholinesterase exists in multiple molecular
            forms which possess similar catalytic properties, but differ in
            their oligomeric assembly and mode of cell attachment to the cell
            surface. It is encoded by the single ACHE gene, and the structural
            diversity in the gene products arises from alternative mRNA
            splicing, and post-translational associations of catalytic and
            structural subunits. The major form of acetylcholinesterase found
            in brain, muscle and other tissues is the hydrophilic species,
            which forms disulfide-linked oligomers with collagenous, or
            lipid-containing structural subunits. The other, alternatively
            spliced form, expressed primarily in the erythroid tissues, differs
            at the C-terminal end, and contains a cleavable hydrophobic peptide
            with a GPI-anchor site. It associates with the membranes through
            the phosphoinositide (PI) moieties added post-translationally. AChE
            activity may constitute a sensitive biomarker of RBC ageing in
            vivo, and thus, may be of aid in understanding the effects of
            transfusion[provided by RefSeq, Sep 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1042626.1,
                                           SRR14372080.1299628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..614
                     /product="acetylcholinesterase isoform E4-E6 precursor"
                     /EC_number="3.1.1.7"
                     /note="Yt blood group; apoptosis-related
                     acetylcholinesterase; acetylcholinesterase (Cartwright
                     blood group)"
                     /calculated_mol_wt=64576
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3238
     Region          37..563
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(151..153,233..235,238,393,397..398,433,479,482)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(234,365,478)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Region          578..611
                     /region_name="AChE_tetra"
                     /note="Acetylcholinesterase tetramerization domain;
                     pfam08674"
                     /db_xref="CDD:430146"
     CDS             1..614
                     /gene="ACHE"
                     /gene_synonym="ACEE; ARACHE; N-ACHE; YT"
                     /coded_by="NM_001367917.1:95..1939"
                     /note="isoform E4-E6 precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS5709.1"
                     /db_xref="GeneID:43"
                     /db_xref="HGNC:HGNC:108"
                     /db_xref="MIM:100740"
ORIGIN      
        1 mrppqcllht pslaspllll llwllgggvg aegredaell vtvrggrlrg irlktpggpv
       61 saflgipfae ppmgprrflp pepkqpwsgv vdattfqsvc yqyvdtlypg fegtemwnpn
      121 relsedclyl nvwtpyprpt sptpvlvwiy gggfysgass ldvydgrflv qaertvlvsm
      181 nyrvgafgfl alpgsreapg nvglldqrla lqwvqenvaa fggdptsvtl fgesagaasv
      241 gmhllsppsr glfhravlqs gapngpwatv gmgearrrat qlahlvgcpp ggtggndtel
      301 vaclrtrpaq vlvnhewhvl pqesvfrfsf vpvvdgdfls dtpealinag dfhglqvlvg
      361 vvkdegsyfl vygapgfskd neslisraef lagvrvgvpq vsdlaaeavv lhytdwlhpe
      421 dparlreals dvvgdhnvvc pvaqlagrla aqgarvyayv fehrastlsw plwmgvphgy
      481 eiefifgipl dpsrnytaee kifaqrlmry wanfartgdp neprdpkapq wppytagaqq
      541 yvsldlrple vrrglraqac afwnrflpkl lsatdtldea erqwkaefhr wssymvhwkn
      601 qfdhyskqdr csdl
//
LOCUS       NP_001231                726 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-T1 isoform a [Homo sapiens].
ACCESSION   NP_001231
VERSION     NP_001231.2
DBSOURCE    REFSEQ: accession NM_001240.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Gao,G., Wu,X., Zhou,J., He,M., He,J.J. and Guo,D.
  TITLE     Inhibition of HIV-1 transcription and replication by a newly
            identified cyclin T1 splice variant
  JOURNAL   J Biol Chem 288 (20), 14297-14309 (2013)
   PUBMED   23569210
  REMARK    GeneRIF: CYCT1b is a newly identified cyclin T1 splice variant
            whose expression leads to direct inhibition of TAT-transactivated
            transcription of the HIV-1 LTR promoter
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Urano,E., Miyauchi,K., Ichikawa,R., Futahashi,Y. and Komano,J.
  TITLE     Regulation of cyclin T1 expression and function by an alternative
            splice variant that skips exon 7 and contains a premature
            termination codon
  JOURNAL   Gene 505 (1), 1-8 (2012)
   PUBMED   22692005
REFERENCE   5  (residues 1 to 726)
  AUTHORS   De Luca,A., De Falco,M., Baldi,A. and Paggi,M.G.
  TITLE     Cyclin T: three forms for different roles in physiological and
            pathological functions
  JOURNAL   J Cell Physiol 194 (2), 101-107 (2003)
   PUBMED   12494448
  REMARK    Review article
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Martin-Serrano,J., Li,K. and Bieniasz,P.D.
  TITLE     Cyclin T1 expression is mediated by a complex and constitutively
            active promoter and does not limit human immunodeficiency virus
            type 1 Tat function in unstimulated primary lymphocytes
  JOURNAL   J Virol 76 (1), 208-219 (2002)
   PUBMED   11739686
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Liu,H. and Rice,A.P.
  TITLE     Isolation and characterization of the human cyclin T1 promoter
  JOURNAL   Gene 252 (1-2), 39-49 (2000)
   PUBMED   10903436
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Wei,P., Garber,M.E., Fang,S.M., Fischer,W.H. and Jones,K.A.
  TITLE     A novel CDK9-associated C-type cyclin interacts directly with HIV-1
            Tat and mediates its high-affinity, loop-specific binding to TAR
            RNA
  JOURNAL   Cell 92 (4), 451-462 (1998)
   PUBMED   9491887
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Yang,X., Herrmann,C.H. and Rice,A.P.
  TITLE     The human immunodeficiency virus Tat proteins specifically
            associate with TAK in vivo and require the carboxyl-terminal domain
            of RNA polymerase II for function
  JOURNAL   J Virol 70 (7), 4576-4584 (1996)
   PUBMED   8676484
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Herrmann,C.H. and Rice,A.P.
  TITLE     Lentivirus Tat proteins specifically associate with a cellular
            protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal
            domain of the large subunit of RNA polymerase II: candidate for a
            Tat cofactor
  JOURNAL   J Virol 69 (3), 1612-1620 (1995)
   PUBMED   7853496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079951.35, AF045161.1 and
            BX098766.1.
            
            On Dec 26, 2001 this sequence version replaced NP_001231.1.
            
            Summary: This gene encodes a member of the highly conserved cyclin
            C subfamily. The encoded protein tightly associates with
            cyclin-dependent kinase 9, and is a major subunit of positive
            transcription elongation factor b (p-TEFb). In humans, there are
            multiple forms of positive transcription elongation factor b, which
            may include one of several different cyclins along with
            cyclin-dependent kinase 9. The complex containing the encoded
            cyclin and cyclin-dependent kinase 9 acts as a cofactor of human
            immunodeficiency virus type 1 (HIV-1) Tat protein, and is both
            necessary and sufficient for full activation of viral
            transcription. This cyclin and its kinase partner are also involved
            in triggering transcript elongation through phosphorylation of the
            carboxy-terminal domain of the largest RNA polymerase II subunit.
            Overexpression of this gene is implicated in tumor growth.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2013].
            
            Transcript Variant: This variant (a, also known as FL and CycT1a)
            encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.147406.1,
                                           SRR1803612.103340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261900.8/ ENSP00000261900.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11-q13.12"
     Protein         1..726
                     /product="cyclin-T1 isoform a"
                     /note="human immunodeficiency virus type 1 (HIV-1)
                     expression (elevated) 1; cyclin C-related protein;
                     CDK9-associated C-type protein; MLLT10/CCNT1 fusion"
                     /calculated_mol_wt=80554
     Region          10..147
                     /region_name="CYCLIN_CCNT1_rpt1"
                     /note="first cyclin box found in cyclin-T1 (CCNT1);
                     cd20595"
                     /db_xref="CDD:410298"
     Site            order(11..12,72..73,89..90,93,96,99..102,130,134,137,
                     141..143,145..146)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410298"
     Site            order(39..40,43..44,46..47,49..51,53..54,56..57,59,81,
                     95..97,111..112)
                     /site_type="other"
                     /note="HIV-1 Tat binding site [polypeptide binding]"
                     /db_xref="CDD:410298"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          151..259
                     /region_name="CYCLIN_CCNT1_rpt2"
                     /note="second cyclin box found in cyclin-T1 (CCNT1);
                     cd20597"
                     /db_xref="CDD:410300"
     Site            order(155,158,171..172,175..176,179..180,183..184,
                     248..250)
                     /site_type="other"
                     /note="HIV-1 Tat binding site [polypeptide binding]"
                     /db_xref="CDD:410300"
     Site            order(163..165,169..170,172..173,202,206..211,213,
                     215..217,221,224,235,238..239,242..243,245..246,250,
                     252..253,256)
                     /site_type="other"
                     /note="AF4 family member binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410300"
     Region          253..270
                     /region_name="Nuclear localization signal, and interaction
                     with Tat-TAR RNA. /evidence=ECO:0000305|PubMed:9491887"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Site            261
                     /site_type="other"
                     /note="Essential for interacting with HIV-1 Tat;
                     propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          360..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Site            390
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          480..550
                     /region_name="Histidine-rich domain (HRD).
                     /evidence=ECO:0000269|PubMed:29849146,
                     ECO:0000269|PubMed:35393539"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Region          487..650
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:29849146"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Site            495
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          527..570
                     /region_name="Required for interaction with ZMYND8.
                     /evidence=ECO:0000269|PubMed:30134174"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Site            577
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60563.1)"
     Region          688..726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60563.1)"
     CDS             1..726
                     /gene="CCNT1"
                     /gene_synonym="CCNT; CYCT1; HIVE1"
                     /coded_by="NM_001240.4:33..2213"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS8766.1"
                     /db_xref="GeneID:904"
                     /db_xref="HGNC:HGNC:1599"
                     /db_xref="MIM:143055"
ORIGIN      
        1 megerknnnk rwyftreqle nspsrrfgvd pdkelsyrqq aanllqdmgq rlnvsqltin
       61 taivymhrfy miqsftqfpg nsvapaalfl aakveeqpkk lehvikvaht clhpqeslpd
      121 trseaylqqv qdlvilesii lqtlgfelti dhphthvvkc tqlvraskdl aqtsyfmatn
      181 slhlttfslq ytppvvacvc ihlackwsnw eipvstdgkh wweyvdatvt lelldelthe
      241 flqilektpn rlkriwnwra ceaakktkad drgtdektse qtilnmisqs ssdttiaglm
      301 smststtsav pslpvseess snltsvemlp gkrwlssqps fkleptqghr tsenlaltgv
      361 dhslpqdgsn afisqkqnsk svpsakvslk eyrakhaeel aaqkrqlenm eanvksqyay
      421 aaqnllshhd shssvilkmp iegsenperp flekadktal kmripvaggd kaasskpeei
      481 kmrikvhaaa dkhnsvedsv tksrehkekh kthpsnhhhh hnhhshkhsh sqlpvgtgnk
      541 rpgdpkhssq tsnlahktys lsssfsssss trkrgpseet ggavfdhpak iakstksssl
      601 nfsfpslptm gqmpghssdt sglsfsqpsc ktrvphskld kgptganghn ttqtidyqdt
      661 vnmlhsllsa qgvqptqpta fefvrpysdy lnprsggiss rsgntdkprp pplpsepppp
      721 lpplpk
//
LOCUS       NP_001353149             874 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 13 [Homo sapiens].
ACCESSION   NP_001353149 XP_016861304
VERSION     NP_001353149.1
DBSOURCE    REFSEQ: accession NM_001366220.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 874)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 874)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 874)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 874)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 874)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 874)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 874)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861304.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2191049.1,
                                           SRR14038196.2639480.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..874
                     /product="disks large homolog 1 isoform 13"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=97773
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..172
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          171..259
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(182..188,205,208,238,242,245..246)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          268..352
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(277..283,300,303,333,337,340..341)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          353..414
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          412..502
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(424..430,441,444,474,478,481..482)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          531..597
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(536,558..559,580)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(539,541,544,553,571..572,591,593..594)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          683..861
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..874
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366220.1:495..3119"
                     /note="isoform 13 is encoded by transcript variant 26"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kvngtdadye yeeitlergn
      181 sglgfsiagg tdnphigdds sifitkiitg gaaaqdgrlr vndcilrvne vdvrdvthsk
      241 avealkeags ivrlyvkrrk pvsekimeik likgpkglgf siaggvgnqh ipgdnsiyvt
      301 kiieggaahk dgklqigdkl lavnnvclee vtheeavtal kntsdfvylk vakptsmymn
      361 dgyappditn sssqpvdnhv spssflgqtp asparyspvs kavlgddeit reprkvvlhr
      421 gstglgfniv ggedgegifi sfilaggpad lsgelrkgdr iisvnsvdlr aasheqaaaa
      481 lknagqavti vaqyrpeeys rfeakihdlr eqmmnssiss gsgslrtsqk rslyvralfd
      541 ydktkdsglp sqglnfkfgd ilhvinasdd ewwqarqvtp dgesdevgvi pskrrvekke
      601 rarlktvkfn sktrdkgsfn dkrkknlfsr kfpfyknkdq seqetsdadq hvtsnasdse
      661 ssyrgqeeyv lsyepvnqqe vnytrpviil gpmkdrindd lisefpdkfg scvphttrpk
      721 rdyevdgrdy hfvtsreqme kdiqehkfie agqynnhlyg tsvqsvreva ekgkhcildv
      781 sgnaikrlqi aqlypisifi kpksmenime mnkrlteeqa rktferamkl eqeftehfta
      841 ivqgdtledi ynqvkqiiee qsgsyiwvpa kekl
//
LOCUS       NP_002758                369 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_002758
VERSION     NP_002758.1
DBSOURCE    REFSEQ: accession NM_002767.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC424578.1, BC106050.1,
            AC107982.6, AI955172.1 and AI379788.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.257405.1,
                                           SRR3476690.1117878.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268835.7/ ENSP00000268835.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..369
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 1"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=40795
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Region          20..138
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          179..363
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60256.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     CDS             1..369
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_002767.4:260..1369"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11200.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mfcvtppele tkmnitkggl vlfsansnss cmelskkiae rlgvemgkvq vyqepnretr
       61 vqiqesvrgk dvfiiqtvsk dvnttimell imvyacktsc aksiigvipy fpyskqckmr
      121 krgsivskll asmmckaglt hlitmdlhqk eiqgffnipv dnlraspfll qyiqeeipdy
      181 rnavivaksp asakraqsfa erlrlgiavi hgeaqdaesd lvdgrhsppm vrsvaaihps
      241 leipmlipke kppitvvgdv ggriaiivdd iiddvdsfla aaetlkerga ykifvmathg
      301 llssdaprri eesaidevvv tntiphevqk lqcpkiktvd ismilseair rihngesmsy
      361 lfrnigldd
//
LOCUS       NP_064507                381 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase KCMF1 [Homo sapiens].
ACCESSION   NP_064507 XP_947223
VERSION     NP_064507.3
DBSOURCE    REFSEQ: accession NM_020122.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Haakonsen,D.L., Heider,M., Ingersoll,A.J., Vodehnal,K., Witus,S.R.,
            Uenaka,T., Wernig,M. and Rape,M.
  TITLE     Stress response silencing by an E3 ligase mutated in
            neurodegeneration
  JOURNAL   Nature 626 (8000), 874-880 (2024)
   PUBMED   38297121
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Varland,S., Silva,R.D., Kjosas,I., Faustino,A., Bogaert,A.,
            Billmann,M., Boukhatmi,H., Kellen,B., Costanzo,M., Drazic,A.,
            Osberg,C., Chan,K., Zhang,X., Tong,A.H.Y., Andreazza,S., Lee,J.J.,
            Nedyalkova,L., Usaj,M., Whitworth,A.J., Andrews,B.J., Moffat,J.,
            Myers,C.L., Gevaert,K., Boone,C., Martinho,R.G. and Arnesen,T.
  TITLE     N-terminal acetylation shields proteins from degradation and
            promotes age-dependent motility and longevity
  JOURNAL   Nat Commun 14 (1), 6774 (2023)
   PUBMED   37891180
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Singh,A., Choudhury,S.D., Singh,P., Singh,V.V., Singh,S.N. and
            Sharma,A.
  TITLE     KCMF1 regulates autophagy and ion channels' function in renal cell
            carcinoma: a future therapeutic target
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 5617-5626 (2023)
   PUBMED   36515749
  REMARK    GeneRIF: KCMF1 regulates autophagy and ion channels' function in
            renal cell carcinoma: a future therapeutic target.
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Wang,W., Liu,J. and Pan,E.
  TITLE     CircHIPK3 contributes to human villous trophoblast growth,
            migration and invasion via modulating the pathway of miR-346/KCMF1
  JOURNAL   Placenta 118, 46-54 (2022)
   PUBMED   35032791
  REMARK    GeneRIF: CircHIPK3 contributes to human villous trophoblast growth,
            migration and invasion via modulating the pathway of miR-346/KCMF1.
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Kreppel,M., Aryee,D.N., Schaefer,K.L., Amann,G., Kofler,R.,
            Poremba,C. and Kovar,H.
  TITLE     Suppression of KCMF1 by constitutive high CD99 expression is
            involved in the migratory ability of Ewing's sarcoma cells
  JOURNAL   Oncogene 25 (19), 2795-2800 (2006)
   PUBMED   16314831
  REMARK    GeneRIF: Suppression of KCMF1 by constitutive high CD99 expression
            levels contribute to the malignant properties of Ewing's sarcoma by
            promoting growth and migration of tumor cells
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Mikami,S., Masutani,M., Sonenberg,N., Yokoyama,S. and Imataka,H.
  TITLE     An efficient mammalian cell-free translation system supplemented
            with translation factors
  JOURNAL   Protein Expr Purif 46 (2), 348-357 (2006)
   PUBMED   16289705
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Jang,J.H.
  TITLE     FIGC, a novel FGF-induced ubiquitin-protein ligase in gastric
            cancers
  JOURNAL   FEBS Lett 578 (1-2), 21-25 (2004)
   PUBMED   15581609
  REMARK    GeneRIF: Data indicate that FIGC upregulation in response to basic
            fibroblast growth factor in gastric cancer might be implicated in
            carcinogenesis through dysregulation of growth modulator.
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Li,Z., Stuart,R.O., Eraly,S.A., Gittes,G., Beier,D.R. and
            Nigam,S.K.
  TITLE     Debt91, a putative zinc finger protein differentially expressed
            during epithelial morphogenesis
  JOURNAL   Biochem Biophys Res Commun 306 (3), 623-628 (2003)
   PUBMED   12810064
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CT004343.1, AK023403.1, AC078974.4 and AW466865.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947223.1, NP_064507.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.182792.1,
                                           SRR1803615.119853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409785.9/ ENSP00000386738.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..381
                     /product="E3 ubiquitin-protein ligase KCMF1"
                     /EC_number="2.3.2.27"
                     /note="FGF-induced ubiquitin-protein ligase in gastric
                     cancers; differentially expressed in branching
                     tubulogenesis 91; zinc finger, ZZ domain containing 1;
                     FGF-induced in gastric cancer; ZZ-type zinc
                     finger-containing protein 1; RING-type E3 ubiquitin
                     transferase KCMF1"
                     /calculated_mol_wt=41814
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Region          7..55
                     /region_name="ZZ_PCMF_like"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     potassium channel modulatory factor (PCMF) 1 and related
                     proteins. The ZZ motif coordinates two zinc ions and most
                     likely participates in ligand binding or molecular
                     scaffolding. Human potassium channel...; cd02338"
                     /db_xref="CDD:239078"
     Site            order(9,12,24,27,33,36,46,50)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239078"
     Site            order(9,12,33,36)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239078"
     Site            order(10,21,23,29,31)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239078"
     Site            order(22,37,52,55)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239078"
     Site            order(24,27,46,50)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239078"
     Region          76..137
                     /region_name="zf-Di19"
                     /note="Drought induced 19 protein (Di19), zinc-binding;
                     pfam05605"
                     /db_xref="CDD:428539"
     Region          154..193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Region          294..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J7.2)"
     CDS             1..381
                     /gene="KCMF1"
                     /gene_synonym="DEBT91; FIGC; PCMF; ZZZ1"
                     /coded_by="NM_020122.5:292..1437"
                     /db_xref="CCDS:CCDS46350.1"
                     /db_xref="GeneID:56888"
                     /db_xref="HGNC:HGNC:20589"
                     /db_xref="MIM:614719"
ORIGIN      
        1 msrhegvscd aclkgnfrgr rykclicydy dlcascyesg atttrhttdh pmqciltrvd
       61 fdlyyggeaf sveqpqsftc pycgkmgyte tslqehvtse haetstevic picaalpggd
      121 pnhvtddfaa hltlehrapr dldessgvrh vrrmfhpgrg lggprarrsn mhftssstgg
      181 lsssqssysp snreamdpia ellsqlsgvr rsaggqlnss gpsasqlqql qmqlqlerqh
      241 aqaarqqlet arnatrrtnt ssvtttitqs tattniante ssqqtlqnsq flltrlndpk
      301 mseterqsme seradrslfv qelllstlvr eessssdedd rgemadfgam gcvdimpldv
      361 alenlnlkes nkgneppppp l
//
LOCUS       NP_001159829             483 aa            linear   PRI 20-NOV-2025
DEFINITION  serine hydroxymethyltransferase, mitochondrial isoform 3 [Homo
            sapiens].
ACCESSION   NP_001159829
VERSION     NP_001159829.1
DBSOURCE    REFSEQ: accession NM_001166357.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Qiao,Z., Li,Y., Li,S., Liu,S. and Cheng,Y.
  TITLE     Hypoxia-induced SHMT2 protein lactylation facilitates glycolysis
            and stemness of esophageal cancer cells
  JOURNAL   Mol Cell Biochem 479 (11), 3063-3076 (2024)
   PUBMED   38175377
  REMARK    GeneRIF: Hypoxia-induced SHMT2 protein lactylation facilitates
            glycolysis and stemness of esophageal cancer cells.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Han,T., Wang,Y., Cheng,M., Hu,Q., Wan,X., Huang,M., Liu,Y., Xun,W.,
            Xu,J., Wang,L., Luo,R., Yuan,Y., Wang,K. and Wang,J.
  TITLE     Phosphorylated SHMT2 Regulates Oncogenesis Through m6A Modification
            in Lung Adenocarcinoma
  JOURNAL   Adv Sci (Weinh) 11 (18), e2307834 (2024)
   PUBMED   38460155
  REMARK    GeneRIF: Phosphorylated SHMT2 Regulates Oncogenesis Through m[6]A
            Modification in Lung Adenocarcinoma.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Malatesta,M., Fornasier,E., Di Salvo,M.L., Tramonti,A.,
            Zangelmi,E., Peracchi,A., Secchi,A., Polverini,E., Giachin,G.,
            Battistutta,R., Contestabile,R. and Percudani,R.
  TITLE     One substrate many enzymes virtual screening uncovers missing genes
            of carnitine biosynthesis in human and mouse
  JOURNAL   Nat Commun 15 (1), 3199 (2024)
   PUBMED   38615009
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Shan,Y., Liu,D., Li,Y., Wu,C. and Ye,Y.
  TITLE     The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer
  JOURNAL   PeerJ 12, e16594 (2024)
   PUBMED   38188143
  REMARK    GeneRIF: The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Bennett,F.I. and Jackson,A.A.
  TITLE     Glycine is not formed through the amino transferase reaction in
            human or rat placenta
  JOURNAL   Placenta 19 (4), 329-331 (1998)
   PUBMED   9639330
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Girgis,S., Nasrallah,I.M., Suh,J.R., Oppenheim,E., Zanetti,K.A.,
            Mastri,M.G. and Stover,P.J.
  TITLE     Molecular cloning, characterization and alternative splicing of the
            human cytoplasmic serine hydroxymethyltransferase gene
  JOURNAL   Gene 210 (2), 315-324 (1998)
   PUBMED   9573390
  REMARK    GeneRIF: This paper compares the mitochondrial and cytoplasmic
            forms of this enzyme and suggests that the two genes are a result
            of a single gene duplication.
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Trakatellis,A., Dimitriadou,A. and Trakatelli,M.
  TITLE     Pyridoxine deficiency: new approaches in immunosuppression and
            chemotherapy
  JOURNAL   Postgrad Med J 73 (864), 617-622 (1997)
   PUBMED   9497969
  REMARK    Review article
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Stover,P.J., Chen,L.H., Suh,J.R., Stover,D.M., Keyomarsi,K. and
            Shane,B.
  TITLE     Molecular cloning, characterization, and regulation of the human
            mitochondrial serine hydroxymethyltransferase gene
  JOURNAL   J Biol Chem 272 (3), 1842-1848 (1997)
   PUBMED   8999870
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Garrow,T.A., Brenner,A.A., Whitehead,V.M., Chen,X.N., Duncan,R.G.,
            Korenberg,J.R. and Shane,B.
  TITLE     Cloning of human cDNAs encoding mitochondrial and cytosolic serine
            hydroxymethyltransferases and chromosomal localization
  JOURNAL   J Biol Chem 268 (16), 11910-11916 (1993)
   PUBMED   8505317
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Waziri,R., Baruah,S. and Sherman,A.D.
  TITLE     Abnormal serine-glycine metabolism in the brains of schizophrenics
  JOURNAL   Schizophr Res 8 (3), 233-243 (1993)
   PUBMED   8435385
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC339924.1, AK315916.1 and
            BC091501.1.
            
            Summary: This gene encodes the mitochondrial form of a pyridoxal
            phosphate-dependent enzyme that catalyzes the reversible reaction
            of serine and tetrahydrofolate to glycine and 5,10-methylene
            tetrahydrofolate. The encoded product is primarily responsible for
            glycine synthesis. The activity of the encoded protein has been
            suggested to be the primary source of intracellular glycine. The
            gene which encodes the cytosolic form of this enzyme is located on
            chromosome 17. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (3) is the longest transcript. It
            differs in the 5' UTR, lacks a portion of the 5' coding region, and
            initiates translation at a downstream start codon, compared to
            variant 1. The encoded isoform (3) has a shorter N-terminus,
            compared to isoform 1. Variants 3, 4, and 5 encode the same isoform
            3. Translation efficiency is uncertain from this alternative start
            codon, and there is rapid turnover of the mitochondrial protein in
            the cytoplasm prior to mitochondrial import due to its shortened
            import presequence (PMID 8999870).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315916.1, SRR18074969.3099260.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..483
                     /product="serine hydroxymethyltransferase, mitochondrial
                     isoform 3"
                     /EC_number="2.1.2.1"
                     /note="glycine hydroxymethyltransferase; serine aldolase;
                     serine hydroxymethylase; threonine aldolase; GLY A+;
                     glycine auxotroph A, human complement for hamster; serine
                     methylase; epididymis secretory sperm binding protein Li
                     51e; serine hydroxymethyltransferase 2 (mitochondrial);
                     mitochondrial serine hydroxymethyltransferase"
                     /calculated_mol_wt=53324
     Region          24..481
                     /region_name="PLN03226"
                     /note="serine hydroxymethyltransferase; Provisional"
                     /db_xref="CDD:215639"
     Site            order(32,34,41..42,51,56,74,92..93,101,120,127,167..168,
                     307,325)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(55,75,85,122..123,150,205,230,233,258..259,265,404)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(55,150,259,404)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(77,84,145,149,151,299,389)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
     CDS             1..483
                     /gene="SHMT2"
                     /gene_synonym="GLYA; HEL-S-51e; mSHMT; NEDCASB; SHMT"
                     /coded_by="NM_001166357.1:332..1783"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53805.1"
                     /db_xref="GeneID:6472"
                     /db_xref="HGNC:HGNC:10852"
                     /db_xref="MIM:138450"
ORIGIN      
        1 mairaqhsna aqtqtgeanr gwtgqeslsd sdpemwellq rekdrqcrgl eliasenfcs
       61 raalealgsc lnnkysegyp gkryyggaev vdeiellcqr raleafdldp aqwgvnvqpy
      121 sgspanlavy tallqphdri mgldlpdggh lthgymsdvk risatsiffe smpyklnpkt
      181 glidynqlal tarlfrprli iagtsayarl idyarmrevc devkahllad mahisglvaa
      241 kvipspfkha divtttthkt lrgarsglif yrkgvkavdp ktgreipytf edrinfavfp
      301 slqggphnha iaavavalkq actpmfreys lqvlknaram adallergys lvsggtdnhl
      361 vlvdlrpkgl dgaraervle lvsitanknt cpgdrsaitp gglrlgapal tsrqfreddf
      421 rrvvdfideg vniglevksk taklqdfksf llkdsetsqr lanlrqrveq farafpmpgf
      481 deh
//
LOCUS       NP_001164637            1197 aa            linear   PRI 20-NOV-2025
DEFINITION  calmodulin-binding transcription activator 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001164637
VERSION     NP_001164637.1
DBSOURCE    REFSEQ: accession NM_001171166.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1197)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 1197)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1197)
  AUTHORS   Monies,D., Abou Al-Shaar,H., Goljan,E.A., Al-Younes,B.,
            Al-Breacan,M.M.A., Al-Saif,M.M., Wakil,S.M., Meyer,B.F.,
            Khabar,K.S.A. and Bohlega,S.
  TITLE     Identification of a novel genetic locus underlying tremor and
            dystonia
  JOURNAL   Hum Genomics 11 (1), 25 (2017)
   PUBMED   29110692
  REMARK    GeneRIF: Mutation of CAMTA2 resulting in post-transcriptional
            inhibition of its own gene activity likely underlies a novel
            syndromic tremulous dystonia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1197)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1197)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   6  (residues 1 to 1197)
  AUTHORS   Finkler,A., Ashery-Padan,R. and Fromm,H.
  TITLE     CAMTAs: calmodulin-binding transcription activators from plants to
            human
  JOURNAL   FEBS Lett 581 (21), 3893-3898 (2007)
   PUBMED   17689537
  REMARK    Review article
REFERENCE   7  (residues 1 to 1197)
  AUTHORS   Liu,N. and Olson,E.N.
  TITLE     Coactivator control of cardiovascular growth and remodeling
  JOURNAL   Curr Opin Cell Biol 18 (6), 715-722 (2006)
   PUBMED   17046230
  REMARK    Review article
REFERENCE   8  (residues 1 to 1197)
  AUTHORS   Song,K., Backs,J., McAnally,J., Qi,X., Gerard,R.D.,
            Richardson,J.A., Hill,J.A., Bassel-Duby,R. and Olson,E.N.
  TITLE     The transcriptional coactivator CAMTA2 stimulates cardiac growth by
            opposing class II histone deacetylases
  JOURNAL   Cell 125 (3), 453-466 (2006)
   PUBMED   16678093
REFERENCE   9  (residues 1 to 1197)
  AUTHORS   Schwartz,R.J. and Schneider,M.D.
  TITLE     CAMTA in cardiac hypertrophy
  JOURNAL   Cell 125 (3), 427-429 (2006)
   PUBMED   16678087
  REMARK    Review article
REFERENCE   10 (residues 1 to 1197)
  AUTHORS   Bouche,N., Scharlat,A., Snedden,W., Bouchez,D. and Fromm,H.
  TITLE     A novel family of calmodulin-binding transcription activators in
            multicellular organisms
  JOURNAL   J Biol Chem 277 (24), 21851-21861 (2002)
   PUBMED   11925432
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004771.1, DB275145.1, AL833974.1 and BC010050.2.
            
            Summary: The protein encoded by this gene is a member of the
            calmodulin-binding transcription activator protein family. Members
            of this family share a common domain structure that consists of a
            transcription activation domain, a DNA-binding domain, and a
            calmodulin-binding domain. The encoded protein may be a
            transcriptional coactivator of genes involved in cardiac growth.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, has
            multiple differences in the coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL833974.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..1197
                     /product="calmodulin-binding transcription activator 2
                     isoform 2"
                     /calculated_mol_wt=130566
     Region          36..152
                     /region_name="CG-1"
                     /note="CG-1 domains are highly conserved domains of about
                     130 amino-acid residues; smart01076"
                     /db_xref="CDD:198144"
     Region          536..616
                     /region_name="TIG"
                     /note="IPT/TIG domain; pfam01833"
                     /db_xref="CDD:460355"
     Region          <712..813
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(712,714,718..719,722..724,726..727,731,746,755,757,
                     759,763..764,767..769,771..772,776,779,789,791,793,
                     797..798,801..803,805..806,810)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          712..755
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          757..789
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..1197
                     /gene="CAMTA2"
                     /coded_by="NM_001171166.2:47..3640"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54073.1"
                     /db_xref="GeneID:23125"
                     /db_xref="HGNC:HGNC:18807"
                     /db_xref="MIM:611508"
ORIGIN      
        1 maaaavtrgt pgenshhlki flpkkllecl prcpllpper lrwntneeia sylitfekhd
       61 ewlscapktr pqngsiilyn rkkvkyrkdg ylwkkrkdgk ttredhmklk vqgmeclygc
      121 yvhssivptf hrrcywllqn pdivlvhyln vpaledcgkg cspifcsiss drrewlkwsr
      181 eellgqlkpm fhgikwscgn gteefsvehl vqqildthpt kpaprthacl csgglgsgsl
      241 thkcsstkhr iispkvepra ltltsiphah ppepppliap lppelpkaht spssssssss
      301 sgfaepleir pspptsrggs srggtailll tgleqraggl tptrhlapqa dprpsmslav
      361 vvgtepsapp appspafdpd rflnspqrgq tygggqgvsp dfpeaeaaht pcsalepaaa
      421 lepqaaargp ppqsvaggrr gncffiqddd sgeelkghga appipsppps pppspaplep
      481 ssrvgrgeal fggpvgasel epfslssfpd lmgelisdea psipaptpql spalstitdf
      541 spewsypegg vkvlitgpwt eaaehyscvf dhiavpaslv qpgvlrcycp ahevglvslq
      601 vagregplsa svlfeyrarr flslpstqld wlslddnqfr msilerleqm ekrmaeiaaa
      661 gqvpcqgpda ppvqdegqgp gfearvvvlv esmiprstwk gperlahgsp frgmsllhla
      721 aaqgyarlie tlsqwrsvet gsldleqevd plnvdhfsct plmwacalgh leaavllfrw
      781 nrqalsipds lgrlplsvah srghvrlarc leelqrqeps veppfalspp ssspdtglss
      841 vsspselsdg tfsvtsayss apdgspppap lpasemtmed mapgqlssgv peaplllmdy
      901 eatnskgpls slpalppasd dgaapedads pqavdvipvd mislakqiie atperikred
      961 fvglpeagas mrertgavgl setmswlasy lenvdhfpss tppselpfer grlavpsaps
     1021 waeflsasts gkmesdfall tlsdheqrel yeaarviqta frkykgrrlk eqqevaaavi
     1081 qrcyrkykqf alykkmtqaa iliqskfrsy yeqkrfqqsr raavliqqhy rsyrrrpgpp
     1141 hrtsatlpar nkgsfltkkq dqaarkimrf lrrcrhrmre lkqnqelegl pqpglat
//
LOCUS       NP_079034                352 aa            linear   PRI 20-NOV-2025
DEFINITION  guanidino acid hydrolase, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_079034
VERSION     NP_079034.3
DBSOURCE    REFSEQ: accession NM_024758.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Xie,Y., Zhang,Y., Liu,X., Cao,L., Han,M., Wang,C., Chen,J. and
            Zhang,X.
  TITLE     miR-151a-5p promotes the proliferation and metastasis of colorectal
            carcinoma cells by targeting AGMAT
  JOURNAL   Oncol Rep 49 (3) (2023)
   PUBMED   36704851
  REMARK    GeneRIF: miR151a5p promotes the proliferation and metastasis of
            colorectal carcinoma cells by targeting AGMAT.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Sinn,M., Stanoppi,M., Hauth,F., Fleming,J.R., Funck,D., Mayans,O.
            and Hartig,J.S.
  TITLE     Guanidino acid hydrolysis by the human enzyme annotated as
            agmatinase
  JOURNAL   Sci Rep 12 (1), 22088 (2022)
   PUBMED   36543883
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Dallmann,K., Junker,H., Balabanov,S., Zimmermann,U., Giebel,J. and
            Walther,R.
  TITLE     Human agmatinase is diminished in the clear cell type of renal cell
            carcinoma
  JOURNAL   Int J Cancer 108 (3), 342-347 (2004)
   PUBMED   14648699
  REMARK    GeneRIF: Agmatinase is down-regulated in the clear cell type of
            renal cell carcinoma
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Morris,S.M. Jr.
  TITLE     Vertebrate agmatinases: what role do they play in agmatine
            catabolism?
  JOURNAL   Ann N Y Acad Sci 1009, 30-33 (2003)
   PUBMED   15028567
  REMARK    Review article
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Iyer,R.K., Kim,H.K., Tsoa,R.W., Grody,W.W. and Cederbaum,S.D.
  TITLE     Cloning and characterization of human agmatinase
  JOURNAL   Mol Genet Metab 75 (3), 209-218 (2002)
   PUBMED   11914032
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Mistry,S.K., Burwell,T.J., Chambers,R.M., Rudolph-Owen,L.,
            Spaltmann,F., Cook,W.J. and Morris,S.M. Jr.
  TITLE     Cloning of human agmatinase. An alternate path for polyamine
            synthesis induced in liver by hepatitis B virus
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 282 (2), G375-G381 (2002)
   PUBMED   11804860
  REMARK    GeneRIF: an alternative to ornithine decarboxylase for polyamine
            biosynthesis
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Chen,F.W., Davies,J.P. and Ioannou,Y.A.
  TITLE     Differential gene expression in apoptosis: identification of
            ribosomal protein 23K, a cell proliferation inhibitor
  JOURNAL   Mol Genet Metab 64 (4), 271-282 (1998)
   PUBMED   9758718
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN996958.1, BC005090.1 and AL121992.24.
            
            On Oct 7, 2003 this sequence version replaced NP_079034.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.3467.1,
                                           SRR1163657.264987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375826.4/ ENSP00000364986.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.21"
     Protein         1..352
                     /product="guanidino acid hydrolase, mitochondrial
                     precursor"
                     /EC_number="3.5.3.1"
                     /EC_number="3.5.3.7"
                     /EC_number="3.5.3.17"
                     /note="agmatinase, mitochondrial; AUH; agmatine
                     ureohydrolase (agmatinase); arginase, mitochondrial;
                     guanidinobutyrase, mitochondrial; guanidinopropionase,
                     mitochondrial; guanidino acid hydrolase, mitochondrial"
                     /calculated_mol_wt=34079
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BSE5.2)"
                     /calculated_mol_wt=3599
     Region          11..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE5.2)"
     mat_peptide     36..352
                     /product="Guanidino acid hydrolase, mitochondrial.
                     /id=PRO_0000002089"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSE5.2)"
                     /calculated_mol_wt=34079
     Region          55..343
                     /region_name="Agmatinase_PAH"
                     /note="Agmatinase-like family includes proclavaminic acid
                     amidinohydrolase; cd11592"
                     /db_xref="CDD:212538"
     Site            order(79,82,91..92,95,98,123,126..127,286,290,294,
                     298..299,330,333..334,337,341)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:212538"
     Site            order(162,185,187..189,201..202,276,278,320)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:212538"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:A2AS89; propagated from
                     UniProtKB/Swiss-Prot (Q9BSE5.2)"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:A2AS89; propagated from
                     UniProtKB/Swiss-Prot (Q9BSE5.2)"
     CDS             1..352
                     /gene="AGMAT"
                     /coded_by="NM_024758.5:85..1143"
                     /db_xref="CCDS:CCDS160.1"
                     /db_xref="GeneID:79814"
                     /db_xref="HGNC:HGNC:18407"
                     /db_xref="MIM:617887"
ORIGIN      
        1 mlrllasgca rgpgpgvgar paaglfhpgr rqsrqasdap rnqppspefv arpvgvcsmm
       61 rlpvqtspeg ldaafigvpl dtgtsnrpga rfgprriree svmlgtvnps tgalpfqslm
      121 vadlgdvnvn lynlqdscrr iqeayekiva agcipltlgg dhtitypilq amakkhgpvg
      181 llhvdahtdt tdkalgekly hgapfrrcvd eglldckrvv qigirgsstt ldpyrynrsq
      241 gfrvvlaedc wmkslvplmg evrqqmggkp iyisfdidal dpayapgtgt peiagltpsq
      301 aleiirgcqg lnvmgcdlve vsppydlsgn tallaanllf emlcalpkvt tv
//
LOCUS       NP_004441                104 aa            linear   PRI 20-NOV-2025
DEFINITION  enhancer of rudimentary homolog [Homo sapiens].
ACCESSION   NP_004441 XP_001130537
VERSION     NP_004441.1
DBSOURCE    REFSEQ: accession NM_004450.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Tsai,Y.M., Wu,K.L., Huang,Y.C., Wu,Y.Y., Chang,C.Y., Chang,Y.Y.,
            Chiang,H.H., Liu,L.X. and Hung,J.Y.
  TITLE     Upregulated enhancer of rudimentary homolog promotes
            epithelial-mesenchymal transition and cancer cell migration in lung
            adenocarcinoma
  JOURNAL   Mol Med Rep 29 (1) (2024)
   PUBMED   37997813
  REMARK    GeneRIF: Upregulated enhancer of rudimentary homolog promotes
            epithelial-mesenchymal transition and cancer cell migration in lung
            adenocarcinoma.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Pacheco-Fiallos,B., Vorlander,M.K., Riabov-Bassat,D., Fin,L.,
            O'Reilly,F.J., Ayala,F.I., Schellhaas,U., Rappsilber,J. and
            Plaschka,C.
  TITLE     mRNA recognition and packaging by the human transcription-export
            complex
  JOURNAL   Nature 616 (7958), 828-835 (2023)
   PUBMED   37020021
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Graille,M.
  TITLE     ERH: a plug-and-play protein important for gene silencing and cell
            cycle progression
  JOURNAL   FEBS J 290 (3), 688-691 (2023)
   PUBMED   36334004
  REMARK    GeneRIF: ERH: a plug-and-play protein important for gene silencing
            and cell cycle progression.
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Wang,X., Xie,H., Zhu,Z., Zhang,J. and Xu,C.
  TITLE     Molecular basis for the recognition of CIZ1 by ERH
  JOURNAL   FEBS J 290 (3), 712-723 (2023)
   PUBMED   36047590
  REMARK    GeneRIF: Molecular basis for the recognition of CIZ1 by ERH.
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Amente,S., Napolitano,G., Licciardo,P., Monti,M., Pucci,P.,
            Lania,L. and Majello,B.
  TITLE     Identification of proteins interacting with the RNAPII FCP1
            phosphatase: FCP1 forms a complex with arginine methyltransferase
            PRMT5 and it is a substrate for PRMT5-mediated methylation
  JOURNAL   FEBS Lett 579 (3), 683-689 (2005)
   PUBMED   15670829
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Skop,A.R., Liu,H., Yates,J. 3rd, Meyer,B.J. and Heald,R.
  TITLE     Dissection of the mammalian midbody proteome reveals conserved
            cytokinesis mechanisms
  JOURNAL   Science 305 (5680), 61-66 (2004)
   PUBMED   15166316
REFERENCE   9  (residues 1 to 104)
  AUTHORS   Gelsthorpe,M., Pulumati,M., McCallum,C., Dang-Vu,K. and
            Tsubota,S.I.
  TITLE     The putative cell cycle gene, enhancer of rudimentary, encodes a
            highly conserved protein found in plants and animals
  JOURNAL   Gene 186 (2), 189-195 (1997)
   PUBMED   9074495
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Isomura,M., Okui,K., Fujiwara,T., Shin,S. and Nakamura,Y.
  TITLE     Cloning and mapping of a novel human cDNA homologous to DROER, the
            enhancer of the Drosophila melanogaster rudimentary gene
  JOURNAL   Genomics 32 (1), 125-127 (1996)
   PUBMED   8786099
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            U66871.1 and AK130850.1.
            
            On Sep 20, 2006 this sequence version replaced XP_001130537.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.587541.1,
                                           SRR1163655.620782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000557016.6/ ENSP00000451080.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..104
                     /product="enhancer of rudimentary homolog"
                     /calculated_mol_wt=12128
     Region          2..99
                     /region_name="ER"
                     /note="Enhancer of rudimentary; pfam01133"
                     /db_xref="CDD:460078"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P84090.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P84090.1)"
     CDS             1..104
                     /gene="ERH"
                     /gene_synonym="DROER"
                     /coded_by="NM_004450.3:67..381"
                     /db_xref="CCDS:CCDS9794.1"
                     /db_xref="GeneID:2079"
                     /db_xref="HGNC:HGNC:3447"
                     /db_xref="MIM:601191"
ORIGIN      
        1 mshtillvqp tkrpegrtya dyesvnecme gvckmyeehl krmnpnspsi tydisqlfdf
       61 iddladlscl vyradtqtyq pynkdwikek iyvllrrqaq qagk
//
LOCUS       NP_689932                448 aa            linear   PRI 20-NOV-2025
DEFINITION  protein chibby homolog 2 isoform 1 [Homo sapiens].
ACCESSION   NP_689932
VERSION     NP_689932.1
DBSOURCE    REFSEQ: accession NM_152719.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Feige,E., Chen,A. and Motro,B.
  TITLE     Nurit, a novel leucine-zipper protein, expressed uniquely in the
            spermatid flower-like structure
  JOURNAL   Mech Dev 117 (1-2), 369-377 (2002)
   PUBMED   12204287
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY017873.1, AK093129.1 and BC027609.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB031134.1, AK093129.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310521.6/ ENSP00000309189.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.13"
     Protein         1..448
                     /product="protein chibby homolog 2 isoform 1"
                     /note="novel leucine zipper testicular protein; spermatid
                     flower-like structure protein; testis-specific leucine
                     zipper protein nurit; spermatid-associated protein;
                     spermatid associated; protein chibby homolog 2; testicular
                     tissue protein Li 182"
                     /calculated_mol_wt=51440
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Region          77..192
                     /region_name="Cby_like"
                     /note="Chibby, a nuclear inhibitor of Wnt/beta-catenin
                     mediated transcription, and similar proteins; cd07429"
                     /db_xref="CDD:143631"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Region          <168..>405
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Region          270..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6AXV6; propagated from
                     UniProtKB/Swiss-Prot (Q8NA61.1)"
     CDS             1..448
                     /gene="CBY2"
                     /gene_synonym="NURIT; SPERT"
                     /coded_by="NM_152719.3:72..1418"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9399.1"
                     /db_xref="GeneID:220082"
                     /db_xref="HGNC:HGNC:30720"
                     /db_xref="MIM:618614"
ORIGIN      
        1 msplecsecf gdqllhrtyt wqltlhsrpn ytrkrdtrse sleipisvvl pqrgtaepfp
       61 rlhnlystpr caqqaalprl srrmasqhsy plnrfssvpl dpmerpmsqa dleldynppr
      121 vqlsdemfvf qdgrwvnenc rlqspyfsps asfhhklhhk rlakecmlqe enkslreenk
      181 alreenrmls kenkilqvfw eehkaslgre esrapspllh kdsaslevvk kdhvalqvpr
      241 gkedstlqll reenralqql leqkqaywaq aedtaapaee skpapsphee pcspgllqdq
      301 gsglssrfee pkgpparqed skelralrkm vsnmsgpsge eeakvgpglp dgcqplqllr
      361 emrqalqall kenrllqeen rtlqvlraeh rgfqeenkal wennklklqq klvidtvtev
      421 tarmemliee lyafmparsq dpkkpsrv
//
LOCUS       NP_001309120             999 aa            linear   PRI 20-NOV-2025
DEFINITION  contactin-associated protein-like 4 isoform 11 [Homo sapiens].
ACCESSION   NP_001309120 XP_011521706
VERSION     NP_001309120.1
DBSOURCE    REFSEQ: accession NM_001322191.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 999)
  AUTHORS   Hu,W., Wang,M., Sun,G., Zhang,L. and Lu,H.
  TITLE     Early B Cell Factor 3 (EBF3) attenuates Parkinson's disease through
            directly regulating contactin-associated protein-like 4 (CNTNAP4)
            transcription: An experimental study
  JOURNAL   Cell Signal 118, 111139 (2024)
   PUBMED   38479556
  REMARK    GeneRIF: Early B Cell Factor 3 (EBF3) attenuates Parkinson's
            disease through directly regulating contactin-associated
            protein-like 4 (CNTNAP4) transcription: An experimental study.
REFERENCE   2  (residues 1 to 999)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 999)
  AUTHORS   Zhang,W., Zhou,M., Lu,W., Gong,J., Gao,F., Li,Y., Xu,X., Lin,Y.,
            Zhang,X., Ding,L., Zhang,Z., Li,G., Chen,X., Sun,X., Zhu,X., Xu,P.
            and Zhang,Y.
  TITLE     CNTNAP4 deficiency in dopaminergic neurons initiates parkinsonian
            phenotypes
  JOURNAL   Theranostics 10 (7), 3000-3021 (2020)
   PUBMED   32194851
  REMARK    GeneRIF: CNTNAP4 deficiency in dopaminergic neurons initiates
            parkinsonian phenotypes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 999)
  AUTHORS   Shangguan,Y., Xu,X., Ganbat,B., Li,Y., Wang,W., Yang,Y., Lu,X.,
            Du,C., Tian,X. and Wang,X.
  TITLE     CNTNAP4 Impacts Epilepsy Through GABAA Receptors Regulation:
            Evidence From Temporal Lobe Epilepsy Patients and Mouse Models
  JOURNAL   Cereb Cortex 28 (10), 3491-3504 (2018)
   PUBMED   28968899
  REMARK    GeneRIF: we demonstrated that the expression of
            contactin-associated protein-like 4 (CNTNAP4) was decreased in the
            temporal neocortex of epileptic patients
REFERENCE   5  (residues 1 to 999)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Haralambieva,I.H., Lambert,N.D.,
            Pankratz,V.S. and Poland,G.A.
  TITLE     Genome-wide SNP associations with rubella-specific cytokine
            responses in measles-mumps-rubella vaccine recipients
  JOURNAL   Immunogenetics 66 (7-8), 493-499 (2014)
   PUBMED   24811271
REFERENCE   6  (residues 1 to 999)
  AUTHORS   Dastani,Z., Pajukanta,P., Marcil,M., Rudzicz,N., Ruel,I.,
            Bailey,S.D., Lee,J.C., Lemire,M., Faith,J., Platko,J., Rioux,J.,
            Hudson,T.J., Gaudet,D., Engert,J.C. and Genest,J.
  TITLE     Fine mapping and association studies of a high-density lipoprotein
            cholesterol linkage region on chromosome 16 in French-Canadian
            subjects
  JOURNAL   Eur J Hum Genet 18 (3), 342-347 (2010)
   PUBMED   19844255
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 999)
  AUTHORS   Nordgard,S.H., Johansen,F.E., Alnaes,G.I., Bucher,E., Syvanen,A.C.,
            Naume,B., Borresen-Dale,A.L. and Kristensen,V.N.
  TITLE     Genome-wide analysis identifies 16q deletion associated with
            survival, molecular subtypes, mRNA expression, and germline
            haplotypes in breast cancer patients
  JOURNAL   Genes Chromosomes Cancer 47 (8), 680-696 (2008)
   PUBMED   18398821
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 999)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   9  (residues 1 to 999)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 999)
  AUTHORS   Spiegel,I., Salomon,D., Erne,B., Schaeren-Wiemers,N. and Peles,E.
  TITLE     Caspr3 and caspr4, two novel members of the caspr family are
            expressed in the nervous system and interact with PDZ domains
  JOURNAL   Mol Cell Neurosci 20 (2), 283-297 (2002)
   PUBMED   12093160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FO681478.1, AC010528.8,
            AC106741.3 and AC108125.4.
            
            On Apr 7, 2016 this sequence version replaced XP_011521706.1.
            
            Summary: This gene encodes a member of the neurexin protein family.
            Members of this family function in the vertebrate nervous system as
            cell adhesion molecules and receptors. This protein contains
            epidermal growth factor repeats and laminin G domains. In addition,
            it includes an F5/8 type C domain, discoidin/neuropilin- and
            fibrinogen-like domains, and thrombospondin N-terminal-like
            domains. This protein may also play a role in proper
            neurotransmission in the dopaminergic and GABAergic systems and
            mutations in this gene may be associated with certain psychiatric
            illnesses. A polymorphism in an intron of this gene may be
            associated with longevity. [provided by RefSeq, Apr 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.257096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..999
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..999
                     /product="contactin-associated protein-like 4 isoform 11"
                     /note="cell recognition molecule Caspr4; contactin
                     associated protein like 4"
                     /calculated_mol_wt=110331
     Region          89..215
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          244..275
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          284..325
                     /region_name="GGGWT_bact"
                     /note="fibrinogen-like bacterial YCDxxxxGGGW domain;
                     NF040941"
                     /db_xref="CDD:468872"
     Region          295..>378
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; cl02436"
                     /db_xref="CDD:470578"
     Region          512..630
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          653..687
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          737..867
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     CDS             1..999
                     /gene="CNTNAP4"
                     /gene_synonym="CASPR4"
                     /coded_by="NM_001322191.2:991..3990"
                     /note="isoform 11 is encoded by transcript variant 13"
                     /db_xref="GeneID:85445"
                     /db_xref="HGNC:HGNC:18747"
                     /db_xref="MIM:610518"
ORIGIN      
        1 msfggipapg ksvsfphrnf hgclenlyyn gvdiidlakq qkpqiiamgn vsfscsqpqs
       61 mpvtflssrs ylalpdfsge eevsatfqfr twnkaglllf selqlisggi llflsdgklk
      121 snlyqpgklp sditagveln dgqwhsvsls akknhlsvav dgqmasaapl lgpeqiysgg
      181 tyyfggcpdk sfgskckspl ggfqgcmrli sisgkvvdli svqqgslgnf sdlqidscgi
      241 sdrclpnyce hggecsqsws tfhcnctntg yrgatchnsi yeqsceaykh rgntsgfyyi
      301 dsdgsgplep fllycnmtet awtiiqhngs dltrvrntnp enpyagffey vasmeqlqat
      361 inraehceqe ftyyckksrl vnkqdgtpls wwvgrtnetq tywggsspdl qkctcglegn
      421 cidsqyycnc dadrnewtnd tgllaykehl pvtkivitdt grlhseaayk lgpllcqgdr
      481 sfwnsasfdt easylhfptf hgelsadvsf ffkttassgv flenlgiadf irielrsptv
      541 vtfsfdvgng pfeisvqspt hfndnqwhhv rvernmkeas lqvdqltpkt qpapadghvl
      601 lqlnsqlfvg gtatrqrgfl gcirslqlng mtldleeraq vtpevqpgcr ghcssygklc
      661 rnggkcrerp igffcdctfs aytgpfcsne isayfgsgss viynfqenyl lsknssshaa
      721 sfhgdmklsr emikfsfrtt rtpslllfvs sfykeylsvi iakngslqir yklnkyqepd
      781 vvnfdfknma dgqlhhimin reegvvfiei ddnrrrqvhl ssgtefsavk slvlgrileh
      841 sdvdqdtala gaqgftgcls avqlshvapl kaalhpshpd pvtvtghvte sscmaqpgtd
      901 atsrerthsf adhsgtiddr eplanaiksd saviggliav vifillcita iavriyqqkr
      961 lykrseakrs envdsaeavl kselniqnav nenqkeyff
//
LOCUS       NP_001129203             153 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger matrin-type protein 4 isoform b [Homo sapiens].
ACCESSION   NP_001129203
VERSION     NP_001129203.1
DBSOURCE    REFSEQ: accession NM_001135731.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 153)
  AUTHORS   Cheong,K.X., Yong,R.Y.Y., Tan,M.M.H., Tey,F.L.K. and Ang,B.C.H.
  TITLE     Association of VIPR2 and ZMAT4 with high myopia
  JOURNAL   Ophthalmic Genet 41 (1), 41-48 (2020)
   PUBMED   32166996
  REMARK    GeneRIF: Association of VIPR2 and ZMAT4 with high myopia.
REFERENCE   3  (residues 1 to 153)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 153)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 153)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 153)
  AUTHORS   Verhoeven,V.J., Hysi,P.G., Wojciechowski,R., Fan,Q.,
            Guggenheim,J.A., Hohn,R., MacGregor,S., Hewitt,A.W., Nag,A.,
            Cheng,C.Y., Yonova-Doing,E., Zhou,X., Ikram,M.K., Buitendijk,G.H.,
            McMahon,G., Kemp,J.P., Pourcain,B.S., Simpson,C.L., Makela,K.M.,
            Lehtimaki,T., Kahonen,M., Paterson,A.D., Hosseini,S.M., Wong,H.S.,
            Xu,L., Jonas,J.B., Parssinen,O., Wedenoja,J., Yip,S.P., Ho,D.W.,
            Pang,C.P., Chen,L.J., Burdon,K.P., Craig,J.E., Klein,B.E.,
            Klein,R., Haller,T., Metspalu,A., Khor,C.C., Tai,E.S., Aung,T.,
            Vithana,E., Tay,W.T., Barathi,V.A., Chen,P., Li,R., Liao,J.,
            Zheng,Y., Ong,R.T., Doring,A., Evans,D.M., Timpson,N.J.,
            Verkerk,A.J., Meitinger,T., Raitakari,O., Hawthorne,F.,
            Spector,T.D., Karssen,L.C., Pirastu,M., Murgia,F., Ang,W.,
            Mishra,A., Montgomery,G.W., Pennell,C.E., Cumberland,P.M.,
            Cotlarciuc,I., Mitchell,P., Wang,J.J., Schache,M.,
            Janmahasatian,S., Igo,R.P. Jr., Lass,J.H., Chew,E., Iyengar,S.K.,
            Gorgels,T.G., Rudan,I., Hayward,C., Wright,A.F., Polasek,O.,
            Vatavuk,Z., Wilson,J.F., Fleck,B., Zeller,T., Mirshahi,A.,
            Muller,C., Uitterlinden,A.G., Rivadeneira,F., Vingerling,J.R.,
            Hofman,A., Oostra,B.A., Amin,N., Bergen,A.A., Teo,Y.Y., Rahi,J.S.,
            Vitart,V., Williams,C., Baird,P.N., Wong,T.Y., Oexle,K.,
            Pfeiffer,N., Mackey,D.A., Young,T.L., van Duijn,C.M., Saw,S.M.,
            Bailey-Wilson,J.E., Stambolian,D., Klaver,C.C. and Hammond,C.J.
  CONSRTM   Consortium for Refractive Error and Myopia (CREAM); Diabetes
            Control and Complications Trial/Epidemiology of Diabetes
            Interventions and Complications (DCCT/EDIC) Research Group;
            Wellcome Trust Case Control Consortium 2 (WTCCC2); Fuchs' Genetics
            Multi-Center Study Group
  TITLE     Genome-wide meta-analyses of multiancestry cohorts identify
            multiple new susceptibility loci for refractive error and myopia
  JOURNAL   Nat Genet 45 (3), 314-318 (2013)
   PUBMED   23396134
  REMARK    Erratum:[Nat Genet. 2013 Jun;45(2):712. Janmahasathian, Sarayut
            [corrected to Sarayut Janmahasatian]]
REFERENCE   7  (residues 1 to 153)
  AUTHORS   Wan,J., Gao,Y., Zhao,X., Wu,Q., Fu,X., Shao,Y., Yang,H., Guan,M.,
            Yu,B. and Zhang,W.
  TITLE     The association between the copy-number variations of ZMAT4 and
            hematological malignancy
  JOURNAL   Hematology 16 (1), 20-23 (2011)
   PUBMED   21269563
  REMARK    GeneRIF: Examines the expression of ZMAT4 mRNA in the samples with
            1 or 2 copies of DNA, and observed a weak yet positive correlation
            between the relative expression level and gene dosage.
REFERENCE   8  (residues 1 to 153)
  AUTHORS   Meigs,J.B., Manning,A.K., Fox,C.S., Florez,J.C., Liu,C.,
            Cupples,L.A. and Dupuis,J.
  TITLE     Genome-wide association with diabetes-related traits in the
            Framingham Heart Study
  JOURNAL   BMC Med Genet 8 Suppl 1 (Suppl 1), S16 (2007)
   PUBMED   17903298
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC048387.16, AK023904.1 and BC019598.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.183270.1,
                                           SRR1803615.112342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..153
                     /product="zinc finger matrin-type protein 4 isoform b"
                     /note="zinc finger matrin-type protein 4"
                     /calculated_mol_wt=17209
     Region          15..38
                     /region_name="zf-met"
                     /note="Zinc-finger of C2H2 type; pfam12874"
                     /db_xref="CDD:463736"
     Region          16..38
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Region          72..106
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          77..99
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(84..86,88..89,93,98,129,132..136,138..139)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <122..>153
                     /region_name="TUTase"
                     /note="TUTase nucleotidyltransferase domain; pfam19088"
                     /db_xref="CDD:465974"
     Region          124..146
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..153
                     /gene="ZMAT4"
                     /coded_by="NM_001135731.2:149..610"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47848.1"
                     /db_xref="GeneID:79698"
                     /db_xref="HGNC:HGNC:25844"
ORIGIN      
        1 mkssdidqdl ftdsyckvcs aqlisesqrv ahyesrkhas kvrlyymlhp rdggcpakrl
       61 rsengsdadm vdknkcctlc nmsftsavva dshyqgkiha krlklllgek tplkttglrr
      121 nyrcticsvs lnsieqyhah lkgskhqtnl knk
//
LOCUS       NP_001138840             868 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001138840
VERSION     NP_001138840.1
DBSOURCE    REFSEQ: accession NM_001145368.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Masuda,S., Onishi,H., Iwamoto,N., Imaizumi,A., Koga,S., Nagao,S.,
            Sakanashi,K., Itoyama,S., Fujimura,A., Komune,N., Kogo,R.,
            Umebayashi,M., Morisaki,T. and Nakagawa,T.
  TITLE     Inhibition of PTPN3 Expressed in Activated Lymphocytes Enhances the
            Antitumor Effects of Anti-PD-1 Therapy in Head and Neck Cancer,
            Especially in Hypoxic Environments
  JOURNAL   J Immunother 47 (3), 89-97 (2024)
   PUBMED   38297883
  REMARK    GeneRIF: Inhibition of PTPN3 Expressed in Activated Lymphocytes
            Enhances the Antitumor Effects of Anti-PD-1 Therapy in Head and
            Neck Cancer, Especially in Hypoxic Environments.
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Zhou,Z., Lin,Z., Wang,M., Wang,L., Ji,Y., Yang,J., Yang,Y., Zhu,G.
            and Liu,T.
  TITLE     Identification and verification of PTPN3 as a novel biomarker in
            predicting cancer prognosis, immunity, and immunotherapeutic
            efficacy
  JOURNAL   Eur J Med Res 29 (1), 12 (2024)
   PUBMED   38173048
  REMARK    GeneRIF: Identification and verification of PTPN3 as a novel
            biomarker in predicting cancer prognosis, immunity, and
            immunotherapeutic efficacy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and
            Tonks,N.K.
  TITLE     Serine phosphorylation-dependent association of the band
            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta
            protein
  JOURNAL   J Biol Chem 272 (43), 27281-27287 (1997)
   PUBMED   9341175
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and
            Yachi,A.
  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase
            PTPH1 mRNA in human hepatocellular carcinoma
  JOURNAL   J Gastroenterol 29 (6), 727-732 (1994)
   PUBMED   7874267
REFERENCE   8  (residues 1 to 868)
  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,
            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.
  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a
            cytosolic protein tyrosine phosphatase homologous to
            cytoskeletal-associated proteins
  JOURNAL   Int J Cancer 55 (6), 947-951 (1993)
   PUBMED   8253532
REFERENCE   9  (residues 1 to 868)
  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,
            Adachi,M., Imai,K. and Yachi,A.
  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human
            colon
  JOURNAL   Tumour Biol 13 (3), 180-186 (1992)
   PUBMED   1626183
REFERENCE   10 (residues 1 to 868)
  AUTHORS   Yang,Q. and Tonks,N.K.
  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine
            phosphatase with homology to the cytoskeletal-associated proteins
            band 4.1, ezrin, and talin
  JOURNAL   Proc Natl Acad Sci U S A 88 (14), 5949-5953 (1991)
   PUBMED   1648725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316066.1, BC126117.1,
            BC033716.1, DB173093.1, AK096975.1 and AL359963.29.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This protein contains a C-terminal PTP
            domain and an N-terminal domain homologous to the band 4.1
            superfamily of cytoskeletal-associated proteins. P97, a cell cycle
            regulator involved in a variety of membrane related functions, has
            been shown to be a substrate of this PTP. This PTP was also found
            to interact with, and be regulated by adaptor protein 14-3-3 beta.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (2) is missing an in-frame coding
            exon compared to transcript variant 1, resulting in a shorter
            isoform (2) lacking an internal protein segment compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.86099.1,
                                           SRR1803613.132429.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..868
                     /product="tyrosine-protein phosphatase non-receptor type 3
                     isoform 2"
                     /EC_number="3.1.3.48"
                     /note="cytoskeletal-associated protein tyrosine
                     phosphatase; protein-tyrosine phosphatase H1"
                     /calculated_mol_wt=98767
     Region          31..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..309
                     /region_name="FERM_C_PTPN4_PTPN3_like"
                     /note="FERM domain C-lobe of Protein tyrosine phosphatase
                     non-receptor proteins 3 and 4 (PTPN4 and PTPN3); cd13189"
                     /db_xref="CDD:270010"
     Site            order(226,243,245,251)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270010"
     Site            order(255,260..263,298,302,305..306)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Site            298..309
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Region          461..550
                     /region_name="PDZ_PTPN3-4-like"
                     /note="PDZ domain of tyrosine-protein phosphatase
                     non-receptor type 3 (PTPN3), tyrosine-protein phosphatase
                     non-receptor type 4 (PTNP4), and related domains; cd06706"
                     /db_xref="CDD:467190"
     Site            order(475..481,493,496,527,531,534..535)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467190"
     Region          586..859
                     /region_name="PTPc-N3"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 3; cd14600"
                     /db_xref="CDD:350448"
     CDS             1..868
                     /gene="PTPN3"
                     /gene_synonym="PTP-H1; PTPH1"
                     /coded_by="NM_001145368.2:107..2713"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:5774"
                     /db_xref="HGNC:HGNC:9655"
                     /db_xref="MIM:176877"
ORIGIN      
        1 mtsrlralgg rinnirtsel pkektrsevi csihfldgvv qtfkvtkqdt gqvlldmvhn
       61 hlgvtekeyf glqhdddsvd sprwleaska irkqlkggfp ctlhfrvrff ipdpntlqqe
      121 qtrhlyflql kmdicegrlt cplnsavvla syavqshfgd ynssihhpgy lsdshfipdq
      181 nedfltkves lheqhsglkq seaescyini artldfygve lhsgrdlhnl dlmigiasag
      241 vavyrkyict sfypwvnilk isfkrkkffi hqrqkqaesr ehivafnmln yrscknlwks
      301 cvehhtffqa kkllpqeknv lsqywtmgsr ntkkrsprlr heirkprhss adnlanemty
      361 itetedvfyt ykgslapqds dsevsqnrsp hqeslsennp aqsyltqkss ssvspssnap
      421 gscspdgvdq qllddfhrvt kggstedasq yycdkndngd sylvliritp dedgkfgfnl
      481 kggvdqkmpl vvsrinpesp adtcipklne gdqivlingr disehthdqv vmfikasres
      541 hsrelalvir rravrsfadf ksedelnqlf peaifpmcpe ggdtlegsma qlkkglesgt
      601 vliqfeqlyr kkpglaitfa klpqnldknr ykdvlpydtt rvllqgnedy inasyvnmei
      661 paanlvnkyi atqgplphtc aqfwqvvwdq klslivmltt ltergrtkch qywpdppdvm
      721 nhggfhiqcq sedctiayvs remlvtntqt geehtvthlq yvawpdhgvp ddssdflefv
      781 nyvrslrvds epvlvhcsag igrtgvlvtm etamcltern lpiypldivr kmrdqrammv
      841 qtssqykfvc eailrvyeeg lvqmldps
//
LOCUS       NP_997637                381 aa            linear   PRI 20-NOV-2025
DEFINITION  cAMP-dependent protein kinase type I-alpha regulatory subunit
            isoform a [Homo sapiens].
ACCESSION   NP_997637
VERSION     NP_997637.1
DBSOURCE    REFSEQ: accession NM_212472.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Calvo,S.E., Pagliarini,D.J. and Mootha,V.K.
  TITLE     Upstream open reading frames cause widespread reduction of protein
            expression and are polymorphic among humans
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7507-7512 (2009)
   PUBMED   19372376
  REMARK    GeneRIF: Includes the study of a disease-related upstream ORF in
            this gene, and shows that it functions to reduce protein levels by
            ~95%.
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Gupte,R.S., Pozarowski,P., Grabarek,J., Traganos,F.,
            Darzynkiewicz,Z. and Lee,M.Y.
  TITLE     RIalpha influences cellular proliferation in cancer cells by
            transporting RFC40 into the nucleus
  JOURNAL   Cancer Biol Ther 4 (4), 429-437 (2005)
   PUBMED   15846072
  REMARK    GeneRIF: A nonconventional nuclear localization sequence (NLS) has
            been found for PRKAR1A. This suggests a new function for PRKAR1A as
            a nuclear transport protein for the second subunit of RFC40.
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Bossis,I. and Stratakis,C.A.
  TITLE     Minireview: PRKAR1A: normal and abnormal functions
  JOURNAL   Endocrinology 145 (12), 5452-5458 (2004)
   PUBMED   15331577
  REMARK    GeneRIF: PRKAR1A might function as a tumor suppressor gene
            Review article
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Stergiopoulos,S.G. and Stratakis,C.A.
  TITLE     Human tumors associated with Carney complex and germline PRKAR1A
            mutations: a protein kinase A disease!
  JOURNAL   FEBS Lett 546 (1), 59-64 (2003)
   PUBMED   12829237
  REMARK    Review article
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Stratakis,C.A.
  TITLE     Carney Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301463
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Jones,K.W., Shapero,M.H., Chevrette,M. and Fournier,R.E.
  TITLE     Subtractive hybridization cloning of a tissue-specific
            extinguisher: TSE1 encodes a regulatory subunit of protein kinase A
  JOURNAL   Cell 66 (5), 861-872 (1991)
   PUBMED   1889088
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Boshart,M., Weih,F., Nichols,M. and Schutz,G.
  TITLE     The tissue-specific extinguisher locus TSE1 encodes a regulatory
            subunit of cAMP-dependent protein kinase
  JOURNAL   Cell 66 (5), 849-859 (1991)
   PUBMED   1832337
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Sandberg,M., Skalhegg,B. and Jahnsen,T.
  TITLE     The two mRNA forms for the type I alpha regulatory subunit of
            cAMP-dependent protein kinase from human testis are due to the use
            of different polyadenylation site signals
  JOURNAL   Biochem Biophys Res Commun 167 (1), 323-330 (1990)
   PUBMED   2310396
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Sandberg,M., Tasken,K., Oyen,O., Hansson,V. and Jahnsen,T.
  TITLE     Molecular cloning, cDNA structure and deduced amino acid sequence
            for a type I regulatory subunit of cAMP-dependent protein kinase
            from human testis
  JOURNAL   Biochem Biophys Res Commun 149 (3), 939-945 (1987)
   PUBMED   3426618
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Geahlen,R.L., Carmichael,D.F., Hashimoto,E. and Krebs,E.G.
  TITLE     Phosphorylation of cAMP-dependent protein kinase subunits
  JOURNAL   Adv Enzyme Regul 20, 195-209 (1982)
   PUBMED   6287816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA219203.1, AL535889.3,
            BC093042.1, AC079210.12 and AY007115.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: cAMP is a signaling molecule important for a variety of
            cellular functions. cAMP exerts its effects by activating the
            cAMP-dependent protein kinase, which transduces the signal through
            phosphorylation of different target proteins. The inactive kinase
            holoenzyme is a tetramer composed of two regulatory and two
            catalytic subunits. cAMP causes the dissociation of the inactive
            holoenzyme into a dimer of regulatory subunits bound to four cAMP
            and two free monomeric catalytic subunits. Four different
            regulatory subunits and three catalytic subunits have been
            identified in humans. This gene encodes one of the regulatory
            subunits. This protein was found to be a tissue-specific
            extinguisher that down-regulates the expression of seven liver
            genes in hepatoma x fibroblast hybrids. Mutations in this gene
            cause Carney complex (CNC). This gene can fuse to the RET
            protooncogene by gene rearrangement and form the thyroid
            tumor-specific chimeric oncogene known as PTC2. A nonconventional
            nuclear localization sequence (NLS) has been found for this protein
            which suggests a role in DNA replication via the protein serving as
            a nuclear transport protein for the second subunit of the
            Replication Factor C (RFC40). Several alternatively spliced
            transcript variants encoding two different isoforms have been
            observed. [provided by RefSeq, Jan 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.168473.1,
                                           SRR1660807.161153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..381
                     /product="cAMP-dependent protein kinase type I-alpha
                     regulatory subunit isoform a"
                     /EC_number="2.7.11.1"
                     /note="tissue-specific extinguisher 1; cAMP-dependent
                     protein kinase type I-alpha regulatory chain;
                     cAMP-dependent protein kinase regulatory subunit RIalpha;
                     protein kinase A type 1a regulatory subunit; epididymis
                     secretory sperm binding protein; protein kinase,
                     cAMP-dependent, regulatory, type I, alpha; Carney complex
                     type 1; protein kinase, cAMP-dependent, regulatory subunit
                     type I alpha"
                     /calculated_mol_wt=42851
     Region          1..136
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          14..63
                     /region_name="DD_RIalpha_PKA"
                     /note="dimerization/docking (D/D) domain of the Type I
                     alpha Regulatory subunit of cAMP-dependent protein kinase;
                     cd12101"
                     /db_xref="CDD:438522"
     Site            order(15,18..19,28..29,31..32,35..36)
                     /site_type="other"
                     /note="AKAP interaction site [polypeptide binding]"
                     /db_xref="CDD:438522"
     Site            order(18,21..22,27,30..31,34..35,38..39,43,45..48,50..51,
                     54..55,58)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438522"
     Region          64..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          96..100
                     /region_name="Pseudophosphorylation motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBC7; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          137..246
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(201..202,211..213)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(233..235,239..241)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          255..370
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            order(325..326,335..337)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(357..359,363..365)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     CDS             1..381
                     /gene="PRKAR1A"
                     /gene_synonym="ACRDYS1; ADOHR; CAR; CNC; CNC1; PKR1;
                     PPNAD1; PRKAR1; Prkar1alpha; TSE1"
                     /coded_by="NM_212472.2:208..1353"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11678.1"
                     /db_xref="GeneID:5573"
                     /db_xref="HGNC:HGNC:9388"
                     /db_xref="MIM:188830"
ORIGIN      
        1 mesgstaase earslrecel yvqkhniqal lkdsivqlct arperpmafl reyferleke
       61 eakqiqnlqk agtrtdsred eisppppnpv vkgrrrrgai saevyteeda asyvrkvipk
      121 dyktmaalak aieknvlfsh lddnersdif damfsvsfia getviqqgde gdnfyvidqg
      181 etdvyvnnew atsvgeggsf gelaliygtp raatvkaktn vklwgidrds yrrilmgstl
      241 rkrkmyeefl skvsilesld kwerltvada lepvqfedgq kivvqgepgd effiilegsa
      301 avlqrrsene efvevgrlgp sdyfgeiall mnrpraatvv argplkcvkl drprfervlg
      361 pcsdilkrni qqynsfvsls v
//
LOCUS       NP_872625                276 aa            linear   PRI 20-NOV-2025
DEFINITION  uroplakin-3b isoform b precursor [Homo sapiens].
ACCESSION   NP_872625
VERSION     NP_872625.1
DBSOURCE    REFSEQ: accession NM_182684.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Moayyeri,A., Hsu,Y.H., Karasik,D., Estrada,K., Xiao,S.M.,
            Nielson,C., Srikanth,P., Giroux,S., Wilson,S.G., Zheng,H.F.,
            Smith,A.V., Pye,S.R., Leo,P.J., Teumer,A., Hwang,J.Y., Ohlsson,C.,
            McGuigan,F., Minster,R.L., Hayward,C., Olmos,J.M.,
            Lyytikainen,L.P., Lewis,J.R., Swart,K.M., Masi,L., Oldmeadow,C.,
            Holliday,E.G., Cheng,S., van Schoor,N.M., Harvey,N.C., Kruk,M., del
            Greco,M. F, Igl,W., Trummer,O., Grigoriou,E., Luben,R., Liu,C.T.,
            Zhou,Y., Oei,L., Medina-Gomez,C., Zmuda,J., Tranah,G., Brown,S.J.,
            Williams,F.M., Soranzo,N., Jakobsdottir,J., Siggeirsdottir,K.,
            Holliday,K.L., Hannemann,A., Go,M.J., Garcia,M., Polasek,O.,
            Laaksonen,M., Zhu,K., Enneman,A.W., McEvoy,M., Peel,R., Sham,P.C.,
            Jaworski,M., Johansson,A., Hicks,A.A., Pludowski,P., Scott,R.,
            Dhonukshe-Rutten,R.A., van der Velde,N., Kahonen,M., Viikari,J.S.,
            Sievanen,H., Raitakari,O.T., Gonzalez-Macias,J., Hernandez,J.L.,
            Mellstrom,D., Ljunggren,O., Cho,Y.S., Volker,U., Nauck,M.,
            Homuth,G., Volzke,H., Haring,R., Brown,M.A., McCloskey,E.,
            Nicholson,G.C., Eastell,R., Eisman,J.A., Jones,G., Reid,I.R.,
            Dennison,E.M., Wark,J., Boonen,S., Vanderschueren,D., Wu,F.C.,
            Aspelund,T., Richards,J.B., Bauer,D., Hofman,A., Khaw,K.T.,
            Dedoussis,G., Obermayer-Pietsch,B., Gyllensten,U.,
            Pramstaller,P.P., Lorenc,R.S., Cooper,C., Kung,A.W., Lips,P.,
            Alen,M., Attia,J., Brandi,M.L., de Groot,L.C., Lehtimaki,T.,
            Riancho,J.A., Campbell,H., Liu,Y., Harris,T.B., Akesson,K.,
            Karlsson,M., Lee,J.Y., Wallaschofski,H., Duncan,E.L., O'Neill,T.W.,
            Gudnason,V., Spector,T.D., Rousseau,F., Orwoll,E., Cummings,S.R.,
            Wareham,N.J., Rivadeneira,F., Uitterlinden,A.G., Prince,R.L.,
            Kiel,D.P., Reeve,J. and Kaptoge,S.K.
  TITLE     Genetic determinants of heel bone properties: genome-wide
            association meta-analysis and replication in the GEFOS/GENOMOS
            consortium
  JOURNAL   Hum Mol Genet 23 (11), 3054-3068 (2014)
   PUBMED   24430505
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Kanamori-Katayama,M., Kaiho,A., Ishizu,Y., Okamura-Oho,Y., Hino,O.,
            Abe,M., Kishimoto,T., Sekihara,H., Nakamura,Y., Suzuki,H.,
            Forrest,A.R. and Hayashizaki,Y.
  TITLE     LRRN4 and UPK3B are markers of primary mesothelial cells
  JOURNAL   PLoS One 6 (10), e25391 (2011)
   PUBMED   21984916
  REMARK    GeneRIF: LRRN4 was only detected in primary mesothelial cells, but
            MSLN and UPK3B were also detected in other cell types.
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Garcia-Espana,A., Chung,P.J., Zhao,X., Lee,A., Pellicer,A., Yu,J.,
            Sun,T.T. and Desalle,R.
  TITLE     Origin of the tetraspanin uroplakins and their co-evolution with
            associated proteins: implications for uroplakin structure and
            function
  JOURNAL   Mol Phylogenet Evol 41 (2), 355-367 (2006)
   PUBMED   16814572
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Deng,F.M., Liang,F.X., Tu,L., Resing,K.A., Hu,P., Supino,M.,
            Hu,C.C., Zhou,G., Ding,M., Kreibich,G. and Sun,T.T.
  TITLE     Uroplakin IIIb, a urothelial differentiation marker, dimerizes with
            uroplakin Ib as an early step of urothelial plaque assembly
  JOURNAL   J Cell Biol 159 (4), 685-694 (2002)
   PUBMED   12446744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BE615406.1, BU150542.1, BP352210.1 and AY233462.1.
            
            On Sep 20, 2006 this sequence version replaced XP_001130836.1.
            
            Summary: UPK3B is a minor component of the apical plaques of
            mammalian urothelium that binds and dimerizes with uroplakin-1b
            (UPK1B; MIM 602380), one of the major conserved urothelium membrane
            proteins. The other major conserved integral membrane proteins of
            urothelial plaques are UPK1A (MIM 611557), UPK2 (MIM 611558), and
            UPK3A (MIM 611559) (Deng et al., 2002 [PubMed 12446744]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) is alternatively spliced at
            the 5' end and contains an additional internal exon, which causes a
            frame-shift compared to variant 1. The resulting isoform (b) lacks
            a protein segment in the N-terminal region and has a distinct
            C-terminus compared to isoform a. This variant is annotated on the
            ALT_REF_LOCI_1 alternate haplotype of the GRCh38 human reference
            genome assembly.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY233462.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142363,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..276
                     /product="uroplakin-3b isoform b precursor"
                     /note="uroplakin-3b; uroplakin IIIb"
                     /calculated_mol_wt=26781
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2960
     Region          29..202
                     /region_name="UP_IIIb"
                     /note="Uroplakin IIIb; cd09969"
                     /db_xref="CDD:197378"
     CDS             1..276
                     /gene="UPK3B"
                     /gene_synonym="P35; UP3B; UPIIIB"
                     /coded_by="NM_182684.2:231..1061"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:105375355"
                     /db_xref="HGNC:HGNC:21444"
                     /db_xref="MIM:611887"
ORIGIN      
        1 mglpwgqphl glqmlllaln clrpslslel vpytpqitaw dlegkvtatt fsleqprcvf
       61 dglasasdtv wlvvafsnas rgfqnpetla dipaspqllt dghymtlpls pdqlpcgdpm
      121 agsggapvlr vghdhgchqq pfcnaplpgp gpyrvkfllm dtrgspraet kwsdpitlhq
      181 gktpgsidtw pgrrsgsmiv itsilsslag llllaflaas tmrfsslwwp eeapeqlrig
      241 sfmgkrymth hippseaatl pvgckpgldp lpslsp
//
LOCUS       NP_056128               1544 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 12 isoform 1 [Homo sapiens].
ACCESSION   NP_056128 NP_061007
VERSION     NP_056128.1
DBSOURCE    REFSEQ: accession NM_015313.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1544)
  AUTHORS   Yang,Y., Wang,S., Cai,J., Liang,J., Zhang,Y., Xie,Y., Luo,F.,
            Tang,J., Gao,Y., Shen,S., Feng,H. and Li,Y.
  TITLE     Targeting ARHGEF12 promotes neuroblastoma differentiation, MYCN
            degradation, and reduces tumorigenicity
  JOURNAL   Cell Oncol (Dordr) 46 (1), 133-143 (2023)
   PUBMED   36520365
  REMARK    GeneRIF: Targeting ARHGEF12 promotes neuroblastoma differentiation,
            MYCN degradation, and reduces tumorigenicity.
            Erratum:[Cell Oncol (Dordr). 2023 Dec;46(6):1871-1872. doi:
            10.1007/s13402-023-00890-x. PMID: 37843798]
REFERENCE   2  (residues 1 to 1544)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1544)
  AUTHORS   Khan,A., Ni,W., Baltazar,T., Lopez-Giraldez,F., Pober,J.S. and
            Pierce,R.W.
  TITLE     ArhGEF12 activates Rap1A and not RhoA in human dermal microvascular
            endothelial cells to reduce tumor necrosis factor-induced leak
  JOURNAL   FASEB J 36 (4), e22254 (2022)
   PUBMED   35294066
  REMARK    GeneRIF: ArhGEF12 activates Rap1A and not RhoA in human dermal
            microvascular endothelial cells to reduce tumor necrosis
            factor-induced leak.
REFERENCE   4  (residues 1 to 1544)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1544)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   6  (residues 1 to 1544)
  AUTHORS   Harrington,A.W., Kim,J.Y. and Yoon,S.O.
  TITLE     Activation of Rac GTPase by p75 is necessary for c-jun N-terminal
            kinase-mediated apoptosis
  JOURNAL   J Neurosci 22 (1), 156-166 (2002)
   PUBMED   11756498
REFERENCE   7  (residues 1 to 1544)
  AUTHORS   Taya,S., Inagaki,N., Sengiku,H., Makino,H., Iwamatsu,A.,
            Urakawa,I., Nagao,K., Kataoka,S. and Kaibuchi,K.
  TITLE     Direct interaction of insulin-like growth factor-1 receptor with
            leukemia-associated RhoGEF
  JOURNAL   J Cell Biol 155 (5), 809-820 (2001)
   PUBMED   11724822
REFERENCE   8  (residues 1 to 1544)
  AUTHORS   Reuther,G.W., Lambert,Q.T., Booden,M.A., Wennerberg,K.,
            Becknell,B., Marcucci,G., Sondek,J., Caligiuri,M.A. and Der,C.J.
  TITLE     Leukemia-associated Rho guanine nucleotide exchange factor, a Dbl
            family protein found mutated in leukemia, causes transformation by
            activation of RhoA
  JOURNAL   J Biol Chem 276 (29), 27145-27151 (2001)
   PUBMED   11373293
REFERENCE   9  (residues 1 to 1544)
  AUTHORS   Fukuhara,S., Chikumi,H. and Gutkind,J.S.
  TITLE     Leukemia-associated Rho guanine nucleotide exchange factor (LARG)
            links heterotrimeric G proteins of the G(12) family to Rho
  JOURNAL   FEBS Lett 485 (2-3), 183-188 (2000)
   PUBMED   11094164
REFERENCE   10 (residues 1 to 1544)
  AUTHORS   Kourlas,P.J., Strout,M.P., Becknell,B., Veronese,M.L., Croce,C.M.,
            Theil,K.S., Krahe,R., Ruutu,T., Knuutila,S., Bloomfield,C.D. and
            Caligiuri,M.A.
  TITLE     Identification of a gene at 11q23 encoding a guanine nucleotide
            exchange factor: evidence for its fusion with MLL in acute myeloid
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 97 (5), 2145-2150 (2000)
   PUBMED   10681437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001150.5, BC063117.1,
            AF180681.1, AK304316.1 and AP000758.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 8, 2003 this sequence version replaced NP_061007.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli working
            through G protein-coupled receptors. The encoded protein may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein has been observed to form a myeloid/lymphoid fusion partner
            in acute myeloid leukemia. Three transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF180681.1, SRR7346977.2307447.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397843.7/ ENSP00000380942.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..1544
                     /product="rho guanine nucleotide exchange factor 12
                     isoform 1"
                     /note="leukemia-associated rho guanine nucleotide exchange
                     factor; leukemia-associated RhoGEF; Rho guanine nucleotide
                     exchange factor (GEF) 12; KMT2A/ARHGEF12 fusion protein"
                     /calculated_mol_wt=173102
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     Phosphoserine. /evidence=ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Region          70..145
                     /region_name="PDZ_ARHGEF11-12-like"
                     /note="PDZ domain of ARHGEF11, ARHGEF12, and related
                     domains; cd23069"
                     /db_xref="CDD:467282"
     Site            order(81..87,95,98,127,131,134..135)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467282"
     Region          247..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            308..309
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-ARHGEF12 oncogene; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Region          349..570
                     /region_name="RGS_LARG"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the leukemia-associated Rho guanine nucleotide exchange
                     factor (RhoGEF) protein (LARG); cd08754"
                     /db_xref="CDD:188708"
     Site            order(392..396,486,488..491,493..495,498)
                     /site_type="other"
                     /note="putative G-alpha-13 interaction site"
                     /db_xref="CDD:188708"
     Region          570..706
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Region          791..976
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; smart00325"
                     /db_xref="CDD:214619"
     Site            order(794,798,899,927..928,931..932,934..935,938..939,
                     942..943,946,971,975)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          995..1132
                     /region_name="PH_LARG"
                     /note="Leukemia-associated Rho guanine nucleotide exchange
                     factor Pleckstrin homology (PH) domain; cd13390"
                     /db_xref="CDD:275425"
     Site            order(1023,1025,1039,1117..1118)
                     /site_type="other"
                     /note="RhoA binding site [polypeptide binding]"
                     /db_xref="CDD:275425"
     Region          1138..1179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            1288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            1327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            1457
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     Site            1541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN5.1)"
     CDS             1..1544
                     /gene="ARHGEF12"
                     /gene_synonym="LARG; PRO2792"
                     /coded_by="NM_015313.3:832..5466"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41727.1"
                     /db_xref="GeneID:23365"
                     /db_xref="HGNC:HGNC:14193"
                     /db_xref="MIM:604763"
ORIGIN      
        1 msgtqstitd rfplkkpirh gsilnrespt dkkqkveria shdfdptdss skktksssee
       61 srseiyglvq rcviiqkddn gfgltvsgdn pvfvqsvked gaamragvqt gdriikvngt
      121 lvthsnhlev vkliksgsyv altvqgrppg spqipladse vepsvighms pimtsphspg
      181 asgnmerits pvlmgeennv vhnqkveilr kmlqkeqerl qllqedynrt paqrllkeiq
      241 eakkhipqlq eqlskatgsa qdgavvtpsr plgdtltvse aetdpgdvlg rtdcssgdas
      301 rpssdnadsp ksgpkeriyl eenpekseti qdtdtqslvg spstriaphi igaedddfgt
      361 eheqingqcs cfqsiellks rpahlavflh hvvsqfdpat llcylysdly khtnsketrr
      421 iflefhqffl drsahlkvsv pdemsadlek rrpelipedl hrhyiqtmqe rvhpevqrhl
      481 edfrqkrsmg ltlaeseltk ldaerdkdrl tlekertcae qivakieevl mtaqaveedk
      541 sstmqyvilm ymkhlgvkvk eprnlehkrg rigflpkikq smkkdkegee kgkrrgfpsi
      601 lgpprrpsrh dnsaigrame lqkarhpkhl stpssvspep qdsaklrqsg lanegtdagy
      661 lpansmssva sgasfsqegg kendtgskqv getsapgdtl dgtprtlntv fdfppppldq
      721 vqeeecever vtehgtpkpf rkfdsvafge sqsedeqfen dletdppnwq qlvsrevllg
      781 lkpceikrqe vinelfyter ahvrtlkvld qvfyqrvsre gilspselrk ifsnledilq
      841 lhiglneqmk avrkrnetsv idqigedllt wfsgpgeekl khaaatfcsn qpfalemiks
      901 rqkkdsrfqt fvqdaesnpl crrlqlkdii ptqmqrltky pllldniaky tewpterekv
      961 kkaadhcrqi lnyvnqavke aenkqrledy qrrldtsslk lseypnveel rnldltkrkm
     1021 ihegplvwkv nrdktidlyt llledilvll qkqddrlvlr chskilasta dskhtfspvi
     1081 klstvlvrqv atdnkalfvi smsdngaqiy elvaqtvsek tvwqdlicrm aasvkeqstk
     1141 piplpqstpg egdndeedps klkeeqhgis vtglqspdrd lglestliss kpqshslsts
     1201 gksevrdlfv aerqfakeqh tdgtlkevge dyqiaipdsh lpvseerwal dalrnlgllk
     1261 qllvqqlglt eksvqedwqh fpryrtasqg pqtdsviqns enikayhsge ghmpfrtgtg
     1321 diatcysprt stesfaprds vglapqdsqa snilvmdhmi mtpemptmep egglddsgeh
     1381 ffdareahsd enpsegdgav nkeekdvnlr isgnylildg ydpvqesstd eevassltlq
     1441 pmtgipaves thqqqhspqn thsdgaispf tpeflvqqrw gameyscfei qspsscadsq
     1501 sqimeyihki eadlehlkkv eesytilcqr lagsaltdkh sdks
//
LOCUS       NP_001276092             809 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 7 isoform b [Homo sapiens].
ACCESSION   NP_001276092 XP_005256260
VERSION     NP_001276092.1
DBSOURCE    REFSEQ: accession NM_001289163.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 809)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 809)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 809)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 809)
  AUTHORS   Dowling,J.K., Becker,C.E., Bourke,N.M., Corr,S.C., Connolly,D.J.,
            Quinn,S.R., Pandolfi,P.P., Mansell,A. and O'Neill,L.A.J.
  TITLE     Promyelocytic leukemia protein interacts with the
            apoptosis-associated speck-like protein to limit inflammasome
            activation
  JOURNAL   J Biol Chem 289 (10), 6429-6437 (2014)
   PUBMED   24407287
REFERENCE   5  (residues 1 to 809)
  AUTHORS   Zhang,D. and Aravind,L.
  TITLE     Novel transglutaminase-like peptidase and C2 domains elucidate the
            structure, biogenesis and evolution of the ciliary compartment
  JOURNAL   Cell Cycle 11 (20), 3861-3875 (2012)
   PUBMED   22983010
REFERENCE   6  (residues 1 to 809)
  AUTHORS   Yang,Y., Cochran,D.A., Gargano,M.D., King,I., Samhat,N.K.,
            Burger,B.P., Sabourin,K.R., Hou,Y., Awata,J., Parry,D.A.,
            Marshall,W.F., Witman,G.B. and Lu,X.
  TITLE     Regulation of flagellar motility by the conserved flagellar protein
            CG34110/Ccdc135/FAP50
  JOURNAL   Mol Biol Cell 22 (7), 976-987 (2011)
   PUBMED   21289096
REFERENCE   7  (residues 1 to 809)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB093780.1, AK093035.1, BC036667.1 and AC018552.6.
            
            On Jan 16, 2014 this sequence version replaced XP_005256260.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an in-frame exon in the central coding region, compared to
            variant 1. The encoded isoform (b) is shorter, compared to isoform
            a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..809
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..809
                     /product="dynein regulatory complex subunit 7 isoform b"
                     /note="coiled-coil domain-containing protein 135;
                     coiled-coil domain-containing protein lobo homolog;
                     coiled-coil domain containing 135"
                     /calculated_mol_wt=96169
     CDS             1..809
                     /gene="DRC7"
                     /gene_synonym="C16orf50; CCDC135; CFAP50; FAP50"
                     /coded_by="NM_001289163.2:85..2514"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73894.1"
                     /db_xref="GeneID:84229"
                     /db_xref="HGNC:HGNC:25289"
                     /db_xref="MIM:618769"
ORIGIN      
        1 mevlrekvee eeeaereeaa ewaewarmek mmrpvevrke eitlkqetlr dlekklseiq
       61 itvsaelpaf tkdtidiskl pisyktntpk eehllqvadn fsrqyshlcp drvplflhpl
      121 necevpkfvs ttlrptlmpy pelynwdsca qfvsdfltmv plpdplkpti kkeekvlpkk
      181 ytikpprdlc srfeqeqevk kqqeiraqek krlreeeerl meaekakpda lhglrvhswv
      241 lvlsgkrevp enffidpftg hsystqdehf lgieslwnhk nywinmqdcw ncckdlifdl
      301 gdpvrweyml lgtdksqlsl teeddsgind eddvenlgke dedksfdmph swveqieisp
      361 eafetrcpng kkviqykrak lekwapylns nglvsrltty edlqctnile ikewyqnred
      421 mlelkhinkt tdlktdyfkp ghpqalrvhs yksmqpemdr viefyetarv dglmkreetp
      481 rtmteyyqgr pdflsyrhas fgprvkkltl ssaesnprpi vkiterffrn pakpaeedva
      541 ervflvaeer iqlryhcred hitaskrefl rrtevdskgn kiimtpdmci sfevepmeht
      601 kkllyqyeam mhlkreekls rhqvwesele vleilklree eeaahtltis iydtkrneks
      661 keyreamerm mheehlrqve tqldylapfl aqlppgeklt cwqavrlkde clsdfkqrli
      721 nkanliqarf eketqelqkk qqwyqenqvt ltpededlyl sycsqamfri rileqrlnrh
      781 kelaplkyla leeklykdpr lgelqkifa
//
LOCUS       NP_006724                756 aa            linear   PRI 20-NOV-2025
DEFINITION  centromere protein I isoform 1 [Homo sapiens].
ACCESSION   NP_006724
VERSION     NP_006724.2
DBSOURCE    REFSEQ: accession NM_006733.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Feng,Z., Cui,G., Tan,J., Liu,P., Chen,Y., Jiang,Z., Han,Y.,
            Zeng,S., Shen,H. and Cai,C.
  TITLE     Immune infiltration related CENPI associates with the malignant
            features and drug resistance of lung adenocarcinoma
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (3), 167017 (2024)
   PUBMED   38232915
  REMARK    GeneRIF: Immune infiltration related CENPI associates with the
            malignant features and drug resistance of lung adenocarcinoma.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Wang,J., Liu,X., Chu,H.J., Li,N., Huang,L.Y. and Chen,J.
  TITLE     Centromere Protein I (CENP-I) Is Upregulated in Gastric Cancer,
            Predicts Poor Prognosis, and Promotes Tumor Cell Proliferation and
            Migration
  JOURNAL   Technol Cancer Res Treat 20, 15330338211045510 (2021)
   PUBMED   34617858
  REMARK    GeneRIF: Centromere Protein I (CENP-I) Is Upregulated in Gastric
            Cancer, Predicts Poor Prognosis, and Promotes Tumor Cell
            Proliferation and Migration.
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   6  (residues 1 to 756)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Liu,S.T., Hittle,J.C., Jablonski,S.A., Campbell,M.S., Yoda,K. and
            Yen,T.J.
  TITLE     Human CENP-I specifies localization of CENP-F, MAD1 and MAD2 to
            kinetochores and is essential for mitosis
  JOURNAL   Nat Cell Biol 5 (4), 341-345 (2003)
   PUBMED   12640463
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Roberts,R.G., Kendall,E., Vetrie,D. and Bobrow,M.
  TITLE     Sequence and chromosomal location of a human homologue of LRPR1, an
            FSH primary response gene
  JOURNAL   Genomics 37 (1), 122-124 (1996)
   PUBMED   8921378
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Slegtenhorst-Eegdeman,K.E., Post,M., Baarends,W.M., Themmen,A.P.
            and Grootegoed,J.A.
  TITLE     Regulation of gene expression in Sertoli cells by
            follicle-stimulating hormone (FSH): cloning and characterization of
            LRPR1, a primary response gene encoding a leucine-rich protein
  JOURNAL   Mol Cell Endocrinol 108 (1-2), 115-124 (1995)
   PUBMED   7758824
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109963.4, X97249.1 and
            BF204027.1.
            
            On Jan 28, 2004 this sequence version replaced NP_006724.1.
            
            Summary: This gene encodes a centromere protein that is a component
            of the CENPA-NAC (nucleosome-associated) complex. This complex is
            critical for accurate chromosome alignment and segregation and it
            ensures proper mitotic progression. This protein regulates the
            recruitment of kinetochore-associated proteins that are required to
            generate the spindle checkpoint signal. The product of this gene is
            involved in the response of gonadal tissues to follicle-stimulating
            hormone. Mutations in this gene may be involved in human X-linked
            disorders of gonadal development and gametogenesis. Alternate
            splicing results in multiple transcript variants. A pseudogene of
            this gene is found on chromosome 13. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X97249.1, SRR14038191.708136.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..756
                     /product="centromere protein I isoform 1"
                     /note="follicle-stimulating hormone primary response
                     protein; leucine-rich primary response protein 1; FSH
                     primary response 1; interphase centromere complex protein
                     19"
                     /calculated_mol_wt=86590
     Region          1..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92674.2)"
     Region          9..521
                     /region_name="CENP-I"
                     /note="Mis6; pfam07778"
                     /db_xref="CDD:429654"
     Site            order(141,145,149,179..180,183,186..187,190,193..196,
                     215..217,221,224,227..232,254)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:439352"
     CDS             1..756
                     /gene="CENPI"
                     /gene_synonym="CENP-I; FSHPRH1; LRPR1"
                     /coded_by="NM_006733.3:271..2541"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14479.1"
                     /db_xref="GeneID:2491"
                     /db_xref="HGNC:HGNC:3968"
                     /db_xref="MIM:300065"
ORIGIN      
        1 mspqkrvknv qaqnrtsqgs ssfqttlsaw kvkqdpsnsk niskhgqnnp vgdyehaddq
       61 aeedalqmav gyfekgpika sqnkdktlek hlktvenvaw knglaseeid illnialsgk
      121 fgnavntril kcmipatvis edsvvkavsw lcvgkcsgst kvlfyrwlva mfdfidrkeq
      181 inllygfffa slqddalcpy vchllylltk kenvkpfrvr klldlqakmg mqphlqalls
      241 lykffapali svslpvrkki yfknsenlwk tallavkqrn rgpspeplkl mlgpanvrpl
      301 krkwnslsvi pvlnsssytk ecgkkemsls dclnrsgsfp leqlqsfpql lqnihclelp
      361 sqmgsvlnns lllhyincvr depvllrfyy wlsqtlqeec iwykvnnyeh gkeftnfldt
      421 iiraecflqe gfysceafly kslplwdglc crsqflqlvs wipfssfsev kpllfdhlaq
      481 lfftstiyfk csvlqslkel lqnwllwlsm dihmkpvtns plettlggsm nsvsklihyv
      541 gwlsttamrl esnntfllhf ildfyekvcd iyinynlplv vlfppgifys allsldtsil
      601 nqlcfimhry rknltaakkn elvqktksef nfssktyqef nhyltsmvgc lwtskpfgkg
      661 iyidpeilek tgvaeyknsl nvvhhpsfls yavsfllqes peertvnvss irgkkwswyl
      721 dylfsqglqg lklfirssvh hssipraegi ncnnqy
//
LOCUS       NP_001350455             479 aa            linear   PRI 20-NOV-2025
DEFINITION  interferon gamma receptor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001350455 XP_016866316
VERSION     NP_001350455.1
DBSOURCE    REFSEQ: accession NM_001363526.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Dhiman,N.S., Saini,V. and Kumar,V.
  TITLE     Single nucleotide polymorphism rs2234711 of interferon gamma
            receptor 1 is associated with pulmonary tuberculosis in the
            population of North India
  JOURNAL   Cytokine 169, 156274 (2023)
   PUBMED   37327531
  REMARK    GeneRIF: Single nucleotide polymorphism rs2234711 of interferon
            gamma receptor 1 is associated with pulmonary tuberculosis in the
            population of North India.
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Tsai,K.D., Lee,Y.C., Chen,B.Y., Wu,L.S., Liang,S.Y., Liu,M.Y.,
            Hung,Y.W., Hsu,H.L., Chen,P.Q., Shieh,J.C., Lee,Y.J. and Lin,T.H.
  TITLE     Recombinant Klotho attenuates IFNgamma receptor signaling and
            SAMHD1 expression through blocking NF-kappaB translocation in
            glomerular mesangial cells
  JOURNAL   Int J Med Sci 20 (6), 810-817 (2023)
   PUBMED   37213666
  REMARK    GeneRIF: Recombinant Klotho attenuates IFNgamma receptor signaling
            and SAMHD1 expression through blocking NF-kappaB translocation in
            glomerular mesangial cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Wu,S.Q., Ding,X.J., Yang,Q.L., Wang,M.G. and He,J.Q.
  TITLE     IFNG and IFNGR1 polymorphisms are associated with tuberculosis: a
            case-control study
  JOURNAL   Eur Rev Med Pharmacol Sci 26 (23), 8777-8787 (2022)
   PUBMED   36524496
  REMARK    GeneRIF: IFNG and IFNGR1 polymorphisms are associated with
            tuberculosis: a case-control study.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Varahram,M., Besharati,S., Farnia,P., Ghanavi,J., Saif,S.,
            Nia,J.H., Madani,M.R., Farnia,P. and Velayati,A.A.
  TITLE     Correlation of single-nucleotide polymorphism at interferon-gamma
            R1 (at Position - 56) in positive purified protein derivative
            health workers with COVID-19 infection
  JOURNAL   Int J Mycobacteriol 11 (3), 318-322 (2022)
   PUBMED   36260452
  REMARK    GeneRIF: Correlation of single-nucleotide polymorphism at
            interferon-gamma R1 (at Position - 56) in positive purified protein
            derivative health workers with COVID-19 infection.
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Szente,B.E., Subramaniam,P.S. and Johnson,H.M.
  TITLE     Identification of IFN-gamma receptor binding sites for JAK2 and
            enhancement of binding by IFN-gamma and its C-terminal peptide
            IFN-gamma(95-133)
  JOURNAL   J Immunol 155 (12), 5617-5622 (1995)
   PUBMED   7499845
REFERENCE   7  (residues 1 to 479)
  AUTHORS   van Loon,A.P., Ozmen,L., Fountoulakis,M., Kania,M., Haiker,M. and
            Garotta,G.
  TITLE     High-affinity receptor for interferon-gamma (IFN-gamma), a
            ubiquitous protein occurring in different molecular forms on human
            cells: blood monocytes and eleven different cell lines have the
            same IFN-gamma receptor protein
  JOURNAL   J Leukoc Biol 49 (5), 462-473 (1991)
   PUBMED   1826725
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Le Coniat,M., Alcaide-Loridan,C., Fellous,M. and Berger,R.
  TITLE     Human interferon gamma receptor 1 (IFNGR1) gene maps to chromosome
            region 6q23-6q24
  JOURNAL   Hum Genet 84 (1), 92-94 (1989)
   PUBMED   2532616
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Aguet,M., Dembic,Z. and Merlin,G.
  TITLE     Molecular cloning and expression of the human interferon-gamma
            receptor
  JOURNAL   Cell 55 (2), 273-280 (1988)
   PUBMED   2971451
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Novick,D., Orchansky,P., Revel,M. and Rubinstein,M.
  TITLE     The human interferon-gamma receptor. Purification,
            characterization, and preparation of antibodies
  JOURNAL   J Biol Chem 262 (18), 8483-8487 (1987)
   PUBMED   2954953
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL050337.6.
            
            On May 21, 2018 this sequence version replaced XP_016866316.1.
            
            Summary: This gene (IFNGR1) encodes the ligand-binding chain
            (alpha) of the gamma interferon receptor. Human interferon-gamma
            receptor is a heterodimer of IFNGR1 and IFNGR2. A genetic variation
            in IFNGR1 is associated with susceptibility to Helicobacter pylori
            infection. In addition, defects in IFNGR1 are a cause of mendelian
            susceptibility to mycobacterial disease, also known as familial
            disseminated atypical mycobacterial infection. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.256522.1,
                                           SRR14372079.3388095.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..479
                     /product="interferon gamma receptor 1 isoform 2"
                     /note="antiviral protein, type 2; CD119 antigen; AVP, type
                     2; interferon-gamma receptor alpha chain; immune
                     interferon receptor 1; IFN-gamma-R-alpha; CDw119;
                     IFN-gamma-R1; IFN-gamma receptor 1"
                     /calculated_mol_wt=53512
     Region          13..103
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     Region          151..307
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; cl46366"
                     /db_xref="CDD:480706"
     CDS             1..479
                     /gene="IFNGR1"
                     /gene_synonym="CD119; IFNGR; IMD27A; IMD27B"
                     /coded_by="NM_001363526.1:270..1709"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87446.1"
                     /db_xref="GeneID:3459"
                     /db_xref="HGNC:HGNC:5439"
                     /db_xref="MIM:107470"
ORIGIN      
        1 mllkspensl lqfqfkygvp tptnvtiesy nmnpivywey qimpqvpvft vevknygvkn
       61 sewidacini shhycnisdh vgdpsnslwv rvkarvgqke sayakseefa vcrdgkigpp
      121 kldirkeekq imidifhpsv fvngdeqevd ydpettcyir vynvyvrmng seiqykiltq
      181 keddcdeiqc qlaipvssln sqycvsaegv lhvwgvttek skevcitifn ssikgslwip
      241 vvaalllflv lslvficfyi kkinplkeks iilpkslisv vrsatletkp eskyvslits
      301 yqpfslekev vceeplspat vpgmhtednp gkvehteels sitevvttee nipdvvpgsh
      361 ltpieresss plssnqsepg sialnsyhsr ncsesdhsrn gfdtdsscle shsslsdsef
      421 ppnnkgeikt egqelitvik aptsfgydkp hvlvdllvdd sgkesligyr ptedskefs
//
LOCUS       NP_001265508             513 aa            linear   PRI 20-NOV-2025
DEFINITION  activin receptor type-2A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001265508
VERSION     NP_001265508.1
DBSOURCE    REFSEQ: accession NM_001278579.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Fei,D., Wang,F., Wang,Y., Chen,J., Chen,S., Fan,L., Yang,L.,
            Ren,Q., Duangmano,S., Du,F., Liu,H., Zhou,J., Sheng,J., Zhao,Y.,
            Wu,X., Li,M., Xiao,Z., Zhang,Z. and Jiang,X.
  TITLE     Circular RNA ACVR2A promotes the progression of hepatocellular
            carcinoma through mir-511-5p targeting PI3K-Akt signaling pathway
  JOURNAL   Mol Cancer 23 (1), 159 (2024)
   PUBMED   39107843
  REMARK    GeneRIF: Circular RNA ACVR2A promotes the progression of
            hepatocellular carcinoma through mir-511-5p targeting PI3K-Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Zhang,H., Ruan,Q., Chen,C., Yu,H., Guan,S., Hu,D., Yang,C., Lin,R.
            and Zhuo,C.
  TITLE     Activin A/ACVR2A axis inhibits epithelial-to-mesenchymal transition
            in colon cancer by activating SMAD2
  JOURNAL   Mol Carcinog 62 (10), 1585-1598 (2023)
   PUBMED   37378449
  REMARK    GeneRIF: Activin A/ACVR2A axis inhibits epithelial-to-mesenchymal
            transition in colon cancer by activating SMAD2.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Sugii,H., Albougha,M.S., Adachi,O., Tomita,H., Tomokiyo,A.,
            Hamano,S., Hasegawa,D., Yoshida,S., Itoyama,T. and Maeda,H.
  TITLE     Activin A Promotes Osteoblastic Differentiation of Human
            Preosteoblasts through the ALK1-Smad1/5/9 Pathway
  JOURNAL   Int J Mol Sci 22 (24), 13491 (2021)
   PUBMED   34948289
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Yuza,K., Nagahashi,M., Ichikawa,H., Hanyu,T., Nakajima,M.,
            Shimada,Y., Ishikawa,T., Sakata,J., Takeuchi,S., Okuda,S.,
            Matsuda,Y., Abe,M., Sakimura,K., Takabe,K. and Wakai,T.
  TITLE     Activin a Receptor Type 2A Mutation Affects the Tumor Biology of
            Microsatellite Instability-High Gastric Cancer
  JOURNAL   J Gastrointest Surg 25 (9), 2231-2241 (2021)
   PUBMED   33420656
  REMARK    GeneRIF: Activin a Receptor Type 2A Mutation Affects the Tumor
            Biology of Microsatellite Instability-High Gastric Cancer.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Xu,J., McKeehan,K., Matsuzaki,K. and McKeehan,W.L.
  TITLE     Inhibin antagonizes inhibition of liver cell growth by activin by a
            dominant-negative mechanism
  JOURNAL   J Biol Chem 270 (11), 6308-6313 (1995)
   PUBMED   7890768
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Attisano,L., Carcamo,J., Ventura,F., Weis,F.M., Massague,J. and
            Wrana,J.L.
  TITLE     Identification of human activin and TGF beta type I receptors that
            form heteromeric kinase complexes with type II receptors
  JOURNAL   Cell 75 (4), 671-680 (1993)
   PUBMED   8242742
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Donaldson,C.J., Mathews,L.S. and Vale,W.W.
  TITLE     Molecular cloning and binding properties of the human type II
            activin receptor
  JOURNAL   Biochem Biophys Res Commun 184 (1), 310-316 (1992)
   PUBMED   1314589
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Matzuk,M.M. and Bradley,A.
  TITLE     Cloning of the human activin receptor cDNA reveals high
            evolutionary conservation
  JOURNAL   Biochim Biophys Acta 1130 (1), 105-108 (1992)
   PUBMED   1311955
  REMARK    Erratum:[Biochim Biophys Acta 1992 Jun 15;1131(2):243]
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Mathews,L.S. and Vale,W.W.
  TITLE     Expression cloning of an activin receptor, a predicted
            transmembrane serine kinase
  JOURNAL   Cell 65 (6), 973-982 (1991)
   PUBMED   1646080
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301629.1, M93415.1,
            DA531622.1, BG616903.1, AW162986.1, BM503220.1, W03601.1,
            DN918410.1, T07746.1 and BU676046.1.
            
            Summary: This gene encodes a receptor that mediates the functions
            of activins, which are members of the transforming growth
            factor-beta (TGF-beta) superfamily involved in diverse biological
            processes. The encoded protein is a transmembrane serine-threonine
            kinase receptor which mediates signaling by forming heterodimeric
            complexes with various combinations of type I and type II receptors
            and ligands in a cell-specific manner. The encoded type II receptor
            is primarily involved in ligand-binding and includes an
            extracellular ligand-binding domain, a transmembrane domain and a
            cytoplasmic serine-threonine kinase domain. This gene may be
            associated with susceptibility to preeclampsia, a pregnancy-related
            disease which can result in maternal and fetal morbidity and
            mortality. Alternative splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M93415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q22.3-q23.1"
     Protein         1..513
                     /product="activin receptor type-2A isoform 1 precursor"
                     /EC_number="2.7.11.30"
                     /note="activin receptor type-2A; activin A receptor, type
                     IIA"
                     /calculated_mol_wt=56022
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
                     /calculated_mol_wt=1844
     mat_peptide     20..513
                     /product="Activin receptor type-2A. /id=PRO_0000024398"
                     /note="propagated from UniProtKB/Swiss-Prot (P27037.1)"
                     /calculated_mol_wt=56022
     Region          25..119
                     /region_name="TFP_LU_ECD_ACVR2A"
                     /note="extracellular domain (ECD) found in activin
                     receptor type-2A (ACTR-IIA) and similar proteins; cd23631"
                     /db_xref="CDD:467151"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P27037.1)"
     Site            136..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27037.1)"
     Region          196..485
                     /region_name="STKc_ACVR2a"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Activin Type IIA Receptor; cd14141"
                     /db_xref="CDD:271043"
     Site            order(198..202,206,217,219,247,267..270,274,276,322,324,
                     326..327,329,340,343,361..364)
                     /site_type="active"
                     /db_xref="CDD:271043"
     Site            order(198..204,206,217,219,267..268,270,274,326..327,329,
                     340)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271043"
     Site            order(202,274,276,322,324,326,343,361..364)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271043"
     Site            339..364
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271043"
     CDS             1..513
                     /gene="ACVR2A"
                     /gene_synonym="ACTRII; ACVR2"
                     /coded_by="NM_001278579.2:270..1811"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33301.1"
                     /db_xref="GeneID:92"
                     /db_xref="HGNC:HGNC:173"
                     /db_xref="MIM:102581"
ORIGIN      
        1 mgaaaklafa vfliscssga ilgrsetqec lffnanwekd rtnqtgvepc ygdkdkrrhc
       61 fatwknisgs ieivkqgcwl ddincydrtd cvekkdspev yfcccegnmc nekfsyfpem
      121 evtqptsnpv tpkppyynil lyslvplmli agivicafwv yrhhkmaypp vlvptqdpgp
      181 pppspllglk plqllevkar grfgcvwkaq llneyvavki fpiqdkqswq neyevyslpg
      241 mkhenilqfi gaekrgtsvd vdlwlitafh ekgslsdflk anvvswnelc hiaetmargl
      301 aylhedipgl kdghkpaish rdiksknvll knnltaciad fglalkfeag ksagdthgqv
      361 gtrrymapev legainfqrd aflridmyam glvlwelasr ctaadgpvde ymlpfeeeig
      421 qhpsledmqe vvvhkkkrpv lrdywqkhag mamlcetiee cwdhdaearl sagcvgerit
      481 qmqrltniit tedivtvvtm vtnvdfppke ssl
//
LOCUS       NP_001353527             820 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001353527
VERSION     NP_001353527.1
DBSOURCE    REFSEQ: accession NM_001366598.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.245422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..820
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 9"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92398
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <522..>656
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..820
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366598.1:2163..4625"
                     /note="isoform 9 is encoded by transcript variant 46"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprg rrrrspsppp trrrrspspa
      481 ppprrrrtpt ppprrrtpsp pprrrspspr rysppiqrry spspppkrrt aspppppkrr
      541 aspspppkrr vshspppkqr sspvtkrrsp slsskhrkgs spsrstrear spqpnkrhsp
      601 sprprapqts sspppvrrga ssspqrrqsp spstrpirrv srtpepkkik kaaspspqsv
      661 rrvsssrsvs gspepaakkp pappspvqsq spstnwspav pvkkaksptp spspprnsdq
      721 egggkkkkkk kdkkhkkdkk hkkhkkhkke kavaaaaaaa vtpaaiaaat ttlaqeepva
      781 apepkketes eaednlddle khlrekalrs mrkaqvspqs
//
LOCUS       NP_996740                205 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase inhibitor 2 family member B [Homo sapiens].
ACCESSION   NP_996740 XP_018216
VERSION     NP_996740.2
DBSOURCE    REFSEQ: accession NM_206858.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Korrodi-Gregorio,L., Abrantes,J., Muller,T., Melo-Ferreira,J.,
            Marcus,K., da Cruz e Silva,O.A., Fardilha,M. and Esteves,P.J.
  TITLE     Not so pseudo: the evolutionary history of protein phosphatase 1
            regulatory subunit 2 and related pseudogenes
  JOURNAL   BMC Evol Biol 13, 242 (2013)
   PUBMED   24195737
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Korrodi-Gregorio,L., Ferreira,M., Vintem,A.P., Wu,W., Muller,T.,
            Marcus,K., Vijayaraghavan,S., Brautigan,D.L., da Cruz E Silva,O.A.,
            Fardilha,M. and da Cruz E Silva,E.F.
  TITLE     Identification and characterization of two distinct PPP1R2 isoforms
            in human spermatozoa
  JOURNAL   BMC Cell Biol 14, 15 (2013)
   PUBMED   23506001
  REMARK    GeneRIF: PPP1R2P3 protein binds directly to PPP1CC and that this
            inhibitor cannot be phosphorylated by GSK3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Fardilha,M., Esteves,S.L., Korrodi-Gregorio,L., Vintem,A.P.,
            Domingues,S.C., Rebelo,S., Morrice,N., Cohen,P.T., da Cruz e
            Silva,O.A. and da Cruz e Silva,E.F.
  TITLE     Identification of the human testis protein phosphatase 1
            interactome
  JOURNAL   Biochem Pharmacol 82 (10), 1403-1415 (2011)
   PUBMED   21382349
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Ceulemans,H., Stalmans,W. and Bollen,M.
  TITLE     Regulator-driven functional diversification of protein
            phosphatase-1 in eukaryotic evolution
  JOURNAL   Bioessays 24 (4), 371-381 (2002)
   PUBMED   11948623
  REMARK    Review article
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Sanseau,P., Jackson,A., Alderton,R.P., Beck,S., Senger,G.,
            Sheer,D., Kelly,A. and Trowsdale,J.
  TITLE     Cloning and characterization of human phosphatase inhibitor-2
            (IPP-2) sequences
  JOURNAL   Mamm Genome 5 (8), 490-496 (1994)
   PUBMED   7949733
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011414.4 and BC066922.1.
            
            On Apr 27, 2017 this sequence version replaced NP_996740.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC066922.1, SRR6380201.76080.9
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000522232.3/ ENSP00000490297.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..205
                     /product="protein phosphatase inhibitor 2 family member B"
                     /note="protein phosphatase 1, regulatory subunit 2
                     pseudogene 3; protein phosphatase inhibitor 2-like protein
                     3; protein phosphatase 1 regulatory inhibitor subunit 2
                     pseudogene 3"
                     /calculated_mol_wt=22975
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P11845; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          12..17
                     /region_name="Required for binding PPP1CC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          43..55
                     /region_name="Required for binding PPP1CC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41236; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          45..164
                     /region_name="IPP-2"
                     /note="Protein phosphatase inhibitor 2 (IPP-2); pfam04979"
                     /db_xref="CDD:461504"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P41236; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P41236; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          111..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23506001; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50411; propagated from
                     UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          147..150
                     /region_name="Required for binding PPP1CC catalytic
                     center, displacing metal ions and inhibition of PPP1CC
                     catalytic activity. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     Region          163..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXS1.2)"
     CDS             1..205
                     /gene="PPP1R2B"
                     /gene_synonym="PPP1R2P3"
                     /coded_by="NM_206858.3:269..886"
                     /db_xref="CCDS:CCDS87340.1"
                     /db_xref="GeneID:153743"
                     /db_xref="HGNC:HGNC:16318"
ORIGIN      
        1 maastashrp ikgilknkts ttssmvasae qprrsvdeel skksqkwdei nilatyhpad
       61 kgyglmkide psppyhsmmg ddedacrdte tteamapdil akklaaaegl epkyriqeqe
      121 ssgeedsdls peerekkrqf emrrklhyne glniklarql iskdlhddde deemletadg
      181 esmnteesnq gstpsdqqqn klrss
//
LOCUS       NP_001354679             284 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform h [Homo sapiens].
ACCESSION   NP_001354679
VERSION     NP_001354679.1
DBSOURCE    REFSEQ: accession NM_001367750.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (34), as well as variants 33 and
            35, encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.401990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..284
                     /product="rab5 GDP/GTP exchange factor isoform h"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=32557
     Region          63..163
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..284
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367750.1:254..1108"
                     /note="isoform h is encoded by transcript variant 34"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mdqiekyimt rlykyvfcpe ttddekkdla iqkriralrw vtpqmlcvpv nedipevsdm
       61 vvkaitdiie mdskrvprdk lacitkcskh ifnaikitkn epasaddflp tliyivlkgn
      121 pprlqsniqy itrfcnpsrl mtgedgyyft nlccavafie kldaqslnls qedfdrymsg
      181 qtsprkqeae swspdaclgv kqmyknldll sqlnerqeri mneakklekd lidwtdgiar
      241 evqdivekyp leikppnqpl aaidsenven dklppplqpq vyag
//
LOCUS       NP_758954                292 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 16 isoform 1 [Homo sapiens].
ACCESSION   NP_758954 XP_005273478
VERSION     NP_758954.1
DBSOURCE    REFSEQ: accession NM_172366.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Zhang,Z., Liu,X., Chu,C., Zhang,Y., Li,W., Yu,X., Han,Q., Sun,H.,
            Zhang,Y., Zhu,X., Chen,L., Wei,R., Fan,N., Zhou,M. and Li,X.
  TITLE     MIR937 amplification potentiates ovarian cancer progression by
            attenuating FBXO16 inhibition on ULK1-mediated autophagy
  JOURNAL   Cell Death Dis 15 (10), 735 (2024)
   PUBMED   39384743
  REMARK    GeneRIF: MIR937 amplification potentiates ovarian cancer
            progression by attenuating FBXO16 inhibition on ULK1-mediated
            autophagy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Ji,M., Zhao,Z., Li,Y., Xu,P., Shi,J., Li,Z., Wang,K., Huang,X.,
            Ji,J., Liu,W. and Liu,B.
  TITLE     FBXO16-mediated hnRNPL ubiquitination and degradation plays a tumor
            suppressor role in ovarian cancer
  JOURNAL   Cell Death Dis 12 (8), 758 (2021)
   PUBMED   34333526
  REMARK    GeneRIF: FBXO16-mediated hnRNPL ubiquitination and degradation
            plays a tumor suppressor role in ovarian cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Paul,D., Islam,S., Manne,R.K., Dinesh,U.S., Malonia,S.K., Maity,B.,
            Boppana,R., Rapole,S., Shetty,P.K. and Santra,M.K.
  TITLE     F-box protein FBXO16 functions as a tumor suppressor by attenuating
            nuclear beta-catenin function
  JOURNAL   J Pathol 248 (3), 266-279 (2019)
   PUBMED   30714168
  REMARK    GeneRIF: that FBXO16 functions as a putative tumor suppressor by
            forming an SCF(FBXO16) complex that targets nuclear beta-catenin in
            a unique manner for ubiquitination and subsequent proteasomal
            degradation to prevent malignancy
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Khan,M., Muzumdar,D. and Shiras,A.
  TITLE     Attenuation of Tumor Suppressive Function of FBXO16 Ubiquitin
            Ligase Activates Wnt Signaling In Glioblastoma
  JOURNAL   Neoplasia 21 (1), 106-116 (2019)
   PUBMED   30530053
  REMARK    GeneRIF: we show that due to low expression of FBXO16, the
            beta-catenin is not targeted in glioma cells leading to its nuclear
            accumulation resulting in active Wnt signaling. Activated Wnt
            signaling potentiates the glioma cells toward a highly
            proliferative and malignant state.
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Cheng,H., Ma,Y., Ni,X., Jiang,M., Guo,L., Jin,W., Xu,W., Cao,G.,
            Ji,C., Yin,K., Gu,S., Ma,Y., Xie,Y. and Mao,Y.
  TITLE     cDNA cloning and expression analysis of a novel human F-box only
            protein
  JOURNAL   Mol Cells 14 (1), 56-59 (2002)
   PUBMED   12243353
  REMARK    GeneRIF: FBXO16 was localized to the human chromosome 8p12. The
            FBXO16 gene consisted of 9 exons that spanned 67,816 bp of human
            genomic DNA
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB134505.1, AF453435.1 and
            AC025871.8.
            
            On Aug 31, 2013 this sequence version replaced XP_005273478.1.
            
            Summary: This gene encodes a member of the F-box protein family,
            members of which are characterized by an approximately 40 amino
            acid motif, the F-box. The F-box proteins constitute one of the
            four subunits of ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into three classes:
            Fbws containing WD-40 domains, Fbls containing leucine-rich
            repeats, and Fbxs containing either different protein-protein
            interaction modules or no recognizable motifs. The protein encoded
            by this gene belongs to the Fbx class. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF453435.1, SRR1803612.184585.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380254.7/ ENSP00000369604.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1"
     Protein         1..292
                     /product="F-box only protein 16 isoform 1"
                     /note="F-box only protein 16"
                     /calculated_mol_wt=34457
     Region          84..138
                     /region_name="F-box_FBXO16"
                     /note="F-box domain found in F-box only protein 16
                     (FBXO16) and similar proteins; cd22172"
                     /db_xref="CDD:438943"
     Site            order(92,96,99..100,103..104,108,110..111,115..117,119)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438943"
     Region          188..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IX29.1)"
     Region          238..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IX29.1)"
     CDS             1..292
                     /gene="FBXO16"
                     /gene_synonym="FBX16"
                     /coded_by="NM_172366.4:61..939"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6068.1"
                     /db_xref="GeneID:157574"
                     /db_xref="HGNC:HGNC:13618"
                     /db_xref="MIM:608519"
ORIGIN      
        1 mmafappknt dgpkmqtkms twtplnhqll ndrvfeerra llgkwfdkwt dsqrrriltg
       61 llercslsqq kfccrklqek ipaealdftt klprvlslyi fsfldprslc rcaqvcwhwk
      121 nlaeldqlwm lkclrfnwyi nfsptpfeqg iwkkhyiqmv kelhitkpkt ppkdgfviad
      181 vqlvtsnspe ekqsplsafr sssslrkknn sgekalppwr ssdkhptdii rfnyldnrdp
      241 metvqqgrrk rnqmtpdfsr qshdkknklq drtrlrkaqs mmsrrnpfpl cp
//
LOCUS       NP_116258                583 aa            linear   PRI 20-NOV-2025
DEFINITION  nudC domain-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_116258
VERSION     NP_116258.2
DBSOURCE    REFSEQ: accession NM_032869.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 583)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 583)
  AUTHORS   Han,B., He,J., Chen,Q., Yuan,M., Zeng,X., Li,Y., Zeng,Y., He,M.,
            Feng,D. and Ma,D.
  TITLE     Identifying the role of NUDCD1 in human tumors from clinical and
            molecular mechanisms: a study based on comprehensive bioinformatics
            and experimental validation
  JOURNAL   Aging (Albany NY) 15 (12), 5611-5649 (2023)
   PUBMED   37338527
  REMARK    GeneRIF: Identifying the role of NUDCD1 in human tumors from
            clinical and molecular mechanisms: a study based on comprehensive
            bioinformatics and experimental validation.
REFERENCE   3  (residues 1 to 583)
  AUTHORS   Feng,W.M., Gong,H., Wang,Y.C., Wang,Y., Xue,T., Zhang,T. and Cui,G.
  TITLE     NudCD1 as a prognostic marker in colorectal cancer and its role in
            the upregulation of cellular spindle assembly checkpoint genes and
            LIS1 pathways
  JOURNAL   BMC Cancer 22 (1), 981 (2022)
   PUBMED   36104662
  REMARK    GeneRIF: NudCD1 as a prognostic marker in colorectal cancer and its
            role in the upregulation of cellular spindle assembly checkpoint
            genes and LIS1 pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 583)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 583)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 583)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   7  (residues 1 to 583)
  AUTHORS   Wang,Q., Li,M., Wang,Y., Zhang,Y., Jin,S., Xie,G., Liu,Z., Wang,S.,
            Zhang,H., Shen,L. and Ge,H.
  TITLE     RNA interference targeting CML66, a novel tumor antigen, inhibits
            proliferation, invasion and metastasis of HeLa cells
  JOURNAL   Cancer Lett 269 (1), 127-138 (2008)
   PUBMED   18534745
  REMARK    GeneRIF: CML66 may play an oncogenic role in ways of favoring tumor
            cells proliferation, invasion and metastasis-associated with
            multiple pathways.
REFERENCE   8  (residues 1 to 583)
  AUTHORS   Jin,S., Wang,Y., Zhang,Y., Zhang,H.Z., Wang,S.J., Tang,J.Q.,
            Chen,H.J. and Ge,H.L.
  TITLE     Humoral immune responses against tumor-associated antigen OVA66
            originally defined by serological analysis of recombinant cDNA
            expression libraries and its potentiality in cellular immunity
  JOURNAL   Cancer Sci 99 (8), 1670-1678 (2008)
   PUBMED   18754882
  REMARK    GeneRIF: study identified a novel gene, OVA66, which was expressed
            significantly higher in cancer patients than normal controls; IgG
            level against OVA66 was significantly elevated in the serum of
            cancer patients from different histological types of cancer [OVA66]
REFERENCE   9  (residues 1 to 583)
  AUTHORS   Yan,Y., Phan,L., Yang,F., Talpaz,M., Yang,Y., Xiong,Z., Ng,B.,
            Timchenko,N.A., Wu,C.J., Ritz,J., Wang,H. and Yang,X.F.
  TITLE     A novel mechanism of alternative promoter and splicing regulates
            the epitope generation of tumor antigen CML66-L
  JOURNAL   J Immunol 172 (1), 651-660 (2004)
   PUBMED   14688378
  REMARK    GeneRIF: An alternative promoter (CML66-S short isoform) has been
            identified in combination with alternative splicing as a novel
            mechanism for regulation of the epitope generation of a self-tumor
            antigen.
REFERENCE   10 (residues 1 to 583)
  AUTHORS   Yang,X.F., Wu,C.J., McLaughlin,S., Chillemi,A., Wang,K.S.,
            Canning,C., Alyea,E.P., Kantoff,P., Soiffer,R.J., Dranoff,G. and
            Ritz,J.
  TITLE     CML66, a broadly immunogenic tumor antigen, elicits a humoral
            immune response associated with remission of chronic myelogenous
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7492-7497 (2001)
   PUBMED   11416219
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF283301.1, AK307663.1, AC021237.5 and BC043406.1.
            
            On Jun 10, 2008 this sequence version replaced NP_116258.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.42673.1,
                                           SRR1803615.106059.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000239690.9/ ENSP00000239690.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..583
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q23.1"
     Protein         1..583
                     /product="nudC domain-containing protein 1 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="chronic myelogenous leukemia tumor antigen 66; nudC
                     domain-containing protein 1; tumor antigen CML66"
                     /calculated_mol_wt=66625
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96RS6.2)"
     Region          278..361
                     /region_name="p23_NUDCD1_like"
                     /note="p23_NUDCD1: p23-like NUD (nuclear distribution)
                     C-like domain found in human NUD (nuclear distribution) C
                     domain-containing protein 1, NUDCD1 (also known as CML66),
                     and similar proteins. NUDCD1/CML66 is a broadly
                     immunogenic tumor associated antigen; cd06493"
                     /db_xref="CDD:107242"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96RS6.2)"
     CDS             1..583
                     /gene="NUDCD1"
                     /gene_synonym="CML66; OVA66"
                     /coded_by="NM_032869.4:78..1829"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6312.1"
                     /db_xref="GeneID:84955"
                     /db_xref="HGNC:HGNC:24306"
                     /db_xref="MIM:606109"
ORIGIN      
        1 mevaancslr vkrplldprf egyklslepl pcyqleldaa vaevklrddq ytlehmhafg
       61 mynylhcdsw yqdsvyyidt lgrimnltvm ldtalgkpre vfrlptdlta cdnrlcasih
      121 fssstwvtls dgtgrlyvig tgergnsase kweimfneel gdpfiiihsi sllnaeehsi
      181 atlllrieke eldmkgsgfy vslewvtisk knqdnkkyei ikrdilrgks vphyaaiepd
      241 gnglmivsyk sltfvqagqd leenmdedis ekikeplyyw qqteddltvt irlpedstke
      301 diqiqflpdh inivlkdhqf legklyssid hesstwiike snsleislik knegltwpel
      361 vigdkqgeli rdsaqcaaia erlmhltsee lnpnpdkekp pcnaqeleec diffeesssl
      421 crfdgntlkt thvvnlgsnq ylfsvivdpk empcfclrhd vdallwqphs skqddmwehi
      481 atfnalgyvq askrdkkffa capnysyaal ceclrrvfiy rqpapmstvl ynrkegrqvg
      541 qvakqqvasl etndpilgfq atnerlfvlt tknlflikvn ten
//
LOCUS       NP_001035202            1945 aa            linear   PRI 20-NOV-2025
DEFINITION  myosin-11 isoform SM2B [Homo sapiens].
ACCESSION   NP_001035202
VERSION     NP_001035202.1
DBSOURCE    REFSEQ: accession NM_001040113.2
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1945)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1945)
  AUTHORS   Wei,X., Ma,Y., Xie,B., Gui,C., Shi,M., Wei,X., Huang,Y., Fan,X.,
            Wei,Q., Huang,Q., Deng,L., Zhang,C., Deng,X., Gui,B. and Chen,Y.
  TITLE     Complex genotype-phenotype correlation of MYH11: new insights from
            monozygotic twins with highly variable expressivity and outcomes
  JOURNAL   BMC Med Genomics 17 (1), 135 (2024)
   PUBMED   38773466
  REMARK    GeneRIF: Complex genotype-phenotype correlation of MYH11: new
            insights from monozygotic twins with highly variable expressivity
            and outcomes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1945)
  AUTHORS   Billon,C., Piccoli,G.B., de Sainte Agathe,J.M., Stoeva,R.,
            Derive,N., Heidet,L., Berrebi,D., Bruneval,P., Jeunemaitre,X. and
            Hureaux,M.
  TITLE     Genome-wide analysis identifies MYH11 compound heterozygous
            variants leading to visceral myopathy corresponding to late-onset
            form of megacystis-microcolon-intestinal hypoperistalsis syndrome
  JOURNAL   Mol Genet Genomics 299 (1), 44 (2024)
   PUBMED   38625590
  REMARK    GeneRIF: Genome-wide analysis identifies MYH11 compound
            heterozygous variants leading to visceral myopathy corresponding to
            late-onset form of megacystis-microcolon-intestinal hypoperistalsis
            syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1945)
  AUTHORS   Pan,M., Tan,X., Sun,T., Zhu,W., Liu,H., Liu,Q. and Dong,H.
  TITLE     A harmful MYH11 variant detected in a family with thoracic aortic
            dissection and patent ductus arteriosus
  JOURNAL   Forensic Sci Med Pathol 20 (1), 212-218 (2024)
   PUBMED   37306888
  REMARK    GeneRIF: A harmful MYH11 variant detected in a family with thoracic
            aortic dissection and patent ductus arteriosus.
REFERENCE   5  (residues 1 to 1945)
  AUTHORS   Aikawa,M., Sivam,P.N., Kuro-o,M., Kimura,K., Nakahara,K.,
            Takewaki,S., Ueda,M., Yamaguchi,H., Yazaki,Y., Periasamy,M. et al.
  TITLE     Human smooth muscle myosin heavy chain isoforms as molecular
            markers for vascular development and atherosclerosis
  JOURNAL   Circ Res 73 (6), 1000-1012 (1993)
   PUBMED   7916668
REFERENCE   6  (residues 1 to 1945)
  AUTHORS   van der Reijden,B.A., Dauwerse,J.G., Wessels,J.W., Beverstock,G.C.,
            Hagemeijer,A., van Ommen,G.J. and Breuning,M.H.
  TITLE     A gene for a myosin peptide is disrupted by the inv(16)(p13q22) in
            acute nonlymphocytic leukemia M4Eo
  JOURNAL   Blood 82 (10), 2948-2952 (1993)
   PUBMED   8219185
REFERENCE   7  (residues 1 to 1945)
  AUTHORS   Deng,Z., Liu,P., Marlton,P., Claxton,D.F., Lane,S., Callen,D.F.,
            Collins,F.S. and Siciliano,M.J.
  TITLE     Smooth muscle myosin heavy chain locus (MYH11) maps to
            16p13.13-p13.12 and establishes a new region of conserved synteny
            between human 16p and mouse 16
  JOURNAL   Genomics 18 (1), 156-159 (1993)
   PUBMED   8276405
REFERENCE   8  (residues 1 to 1945)
  AUTHORS   Matsuoka,R., Yoshida,M.C., Furutani,Y., Imamura,S., Kanda,N.,
            Yanagisawa,M., Masaki,T. and Takao,A.
  TITLE     Human smooth muscle myosin heavy chain gene mapped to chromosomal
            region 16q12
  JOURNAL   Am J Med Genet 46 (1), 61-67 (1993)
   PUBMED   7684189
REFERENCE   9  (residues 1 to 1945)
  AUTHORS   Ambartsumyan,L.
  TITLE     Megacystis-Microcolon-Intestinal Hypoperistalsis Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31070878
REFERENCE   10 (residues 1 to 1945)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX489788.1, AY520817.1,
            BC104906.1 and AA552189.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a smooth muscle myosin
            belonging to the myosin heavy chain family. The gene product is a
            subunit of a hexameric protein that consists of two heavy chain
            subunits and two pairs of non-identical light chain subunits. It
            functions as a major contractile protein, converting chemical
            energy into mechanical energy through the hydrolysis of ATP. A
            chromosomal rearrangement involving this gene is associated with
            acute myeloid leukemia of the M4Eo subtype. Mutations in this gene
            are associated with visceral myopathy,
            megacystis-microcolon-intestinal hypoperistalsis syndrome 2, and
            familial thoracic aortic aneurysm 4. [provided by RefSeq, May
            2022].
            
            Transcript Variant: This variant (SM2B) represents the longer
            transcript. It encodes the isoform SM2B.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY520817.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000452625.7/ ENSP00000407821.2
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1945
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1945
                     /product="myosin-11 isoform SM2B"
                     /note="myosin, heavy polypeptide 11, smooth muscle;
                     myosin, heavy chain 11, smooth muscle; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=224198
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          31..76
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          99..778
                     /region_name="MYSc_class_II"
                     /note="class II myosins, motor domain; cd01377"
                     /db_xref="CDD:276951"
     Site            order(126..134,178..185,238..248,466..471)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276951"
     Site            126..134
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276951"
     Site            129
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            178..185
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276951"
     Site            238..248
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276951"
     Site            466..471
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276951"
     Site            495..518
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276951"
     Region          668..690
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            710..719
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276951"
     Site            order(722..738,767..778)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276951"
     Region          769..783
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Region          855..1935
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Region          865..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            1184
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          1751..1807
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     CDS             1..1945
                     /gene="MYH11"
                     /gene_synonym="AAT4; FAA4; SMHC; SMMHC; SMMS-1; VSCM2"
                     /coded_by="NM_001040113.2:106..5943"
                     /note="isoform SM2B is encoded by transcript variant SM2B"
                     /db_xref="CCDS:CCDS45424.1"
                     /db_xref="GeneID:4629"
                     /db_xref="HGNC:HGNC:7569"
                     /db_xref="MIM:160745"
ORIGIN      
        1 maqkgqlsdd ekflfvdknf inspvaqadw aakrlvwvps ekqgfeaasi keekgdevvv
       61 elvengkkvt vgkddiqkmn ppkfskvedm aeltclneas vlhnlreryf sgliytysgl
      121 fcvvvnpykh lpiysekivd mykgkkrhem pphiyaiadt ayrsmlqdre dqsilctges
      181 gagktentkk viqylavvas shkgkkdtsi tqgpsfayge lekqllqanp ileafgnakt
      241 vkndnssrfg kfirinfdvt gyivganiet ylleksrair qardertfhi fyymiagake
      301 kmrsdllleg fnnytflsng fvpipaaqdd emfqetveam aimgfseeeq lsilkvvssv
      361 lqlgnivfkk erntdqasmp dntaaqkvch lmginvtdft rsiltprikv grdvvqkaqt
      421 keqadfavea lakatyerlf rwiltrvnka ldkthrqgas flgildiagf eifevnsfeq
      481 lcinytnekl qqlfnhtmfi leqeeyqreg iewnfidfgl dlqpcielie rpnnppgvla
      541 lldeecwfpk atdksfvekl cteqgshpkf qkpkqlkdkt efsiihyagk vdynasawlt
      601 knmdplndnv tsllnassdk fvadlwkdvd rivgldqmak mtesslpsas ktkkgmfrtv
      661 gqlykeqlgk lmttlrnttp nfvrciipnh ekrsgkldaf lvleqlrcng vlegiricrq
      721 gfpnrivfqe frqryeilaa naipkgfmdg kqacilmika leldpnlyri gqskiffrtg
      781 vlahleeerd lkitdvimaf qamcrgylar kafakrqqql tamkviqrnc aaylklrnwq
      841 wwrlftkvkp llqvtrqeee mqakedelqk tkerqqkaen elkeleqkhs qlteeknllq
      901 eqlqaetely aeaeemrvrl aakkqeleei lhemearlee eedrgqqlqa erkkmaqqml
      961 dleeqleeee aarqklqlek vtaeakikkl edeilvmddq nnklskerkl leerisdltt
     1021 nlaeeeekak nltklknkhe smiselevrl kkeeksrqel eklkrklegd asdfheqiad
     1081 lqaqiaelkm qlakkeeelq aalarlddei aqknnalkki releghisdl qedldseraa
     1141 rnkaekqkrd lgeelealkt eledtldsta tqqelrakre qevtvlkkal deetrsheaq
     1201 vqemrqkhaq aveelteqle qfkrakanld knkqtleken adlagelrvl gqakqevehk
     1261 kkkleaqvqe lqskcsdger araelndkvh klqnevesvt gmlneaegka iklakdvasl
     1321 ssqlqdtqel lqeetrqkln vstklrqlee ernslqdqld eemeakqnle rhistlniql
     1381 sdskkklqdf astvealeeg kkrfqkeien ltqqyeekaa aydklektkn rlqqelddlv
     1441 vdldnqrqlv snlekkqrkf dqllaeekni sskyaderdr aeaeareket kalslarale
     1501 ealeakeele rtnkmlkaem edlvsskddv gknvheleks kraletqmee mktqleeled
     1561 elqatedakl rlevnmqalk gqferdlqar deqneekrrq lqrqlheyet elederkqra
     1621 laaaakkkle gdlkdlelqa dsaikgreea ikqlrklqaq mkdfqreled arasrdeifa
     1681 takenekkak sleadlmqlq edlaaaerar kqadlekeel aeelasslsg rnalqdekrr
     1741 leariaqlee eleeeqgnme amsdrvrkat qqaeqlsnel aterstaqkn esarqqlerq
     1801 nkelrsklhe megavkskfk stiaaleaki aqleeqveqe arekqaatks lkqkdkklke
     1861 illqvederk maeqykeqae kgnarvkqlk rqleeaeees qrinanrrkl qreldeates
     1921 neamgrevna lksklrgppp qetsq
//
LOCUS       NP_001166217             749 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec23B isoform 2 [Homo sapiens].
ACCESSION   NP_001166217
VERSION     NP_001166217.1
DBSOURCE    REFSEQ: accession NM_001172746.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 749)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 749)
  AUTHORS   Saptarshi,A.N., More,T.A., Dongerdiye,R. and Kedar,P.
  TITLE     Congenital Dyserythropoietic Anemia Type II: High Prevalence of
            c.1385A>G, (p.Tyr462Cys) Mutation in the Indian Population
  JOURNAL   Indian J Pediatr 90 (8), 840 (2023)
   PUBMED   37204595
  REMARK    GeneRIF: Congenital Dyserythropoietic Anemia Type II: High
            Prevalence of c.1385A>G, (p.Tyr462Cys) Mutation in the Indian
            Population.
REFERENCE   3  (residues 1 to 749)
  AUTHORS   Musri,M.M., Venturi,V., Ferrer-Cortes,X., Romero-Cortadellas,L.,
            Hernandez,G., Leoz,P., Ricard Andres,M.P., Morado,M., Fernandez
            Valle,M.D.C., Beneitez Pastor,D., Ortuno Cabrero,A., Moreno
            Gamiz,M., Senent Peris,L., Perez-Valencia,A.I., Perez-Montero,S.,
            Tornador,C. and Sanchez,M.
  TITLE     New Cases and Mutations in SEC23B Gene Causing Congenital
            Dyserythropoietic Anemia Type II
  JOURNAL   Int J Mol Sci 24 (12), 9935 (2023)
   PUBMED   37373084
  REMARK    GeneRIF: New Cases and Mutations in SEC23B Gene Causing Congenital
            Dyserythropoietic Anemia Type II.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 749)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 749)
  AUTHORS   Rosato,B.E., Marra,R., D'Onofrio,V., Del Giudice,F., Della
            Monica,S., Iolascon,A., Andolfo,I. and Russo,R.
  TITLE     SEC23B Loss-of-Function Suppresses Hepcidin Expression by Impairing
            Glycosylation Pathway in Human Hepatic Cells
  JOURNAL   Int J Mol Sci 23 (3), 1304 (2022)
   PUBMED   35163229
  REMARK    GeneRIF: SEC23B Loss-of-Function Suppresses Hepcidin Expression by
            Impairing Glycosylation Pathway in Human Hepatic Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 749)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   7  (residues 1 to 749)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   8  (residues 1 to 749)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
REFERENCE   9  (residues 1 to 749)
  AUTHORS   Gasparini,P., Miraglia del Giudice,E., Delaunay,J., Totaro,A.,
            Granatiero,M., Melchionda,S., Zelante,L. and Iolascon,A.
  TITLE     Localization of the congenital dyserythropoietic anemia II locus to
            chromosome 20q11.2 by genomewide search
  JOURNAL   Am J Hum Genet 61 (5), 1112-1116 (1997)
   PUBMED   9345103
REFERENCE   10 (residues 1 to 749)
  AUTHORS   Paccaud,J.P., Reith,W., Carpentier,J.L., Ravazzola,M., Amherdt,M.,
            Schekman,R. and Orci,L.
  TITLE     Cloning and functional characterization of mammalian homologues of
            the COPII component Sec23
  JOURNAL   Mol Biol Cell 7 (10), 1535-1546 (1996)
   PUBMED   8898360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296270.1, BC005032.1 and
            AL121900.26.
            
            Summary: The protein encoded by this gene is a member of the SEC23
            subfamily of the SEC23/SEC24 family, which is involved in vesicle
            trafficking. The encoded protein has similarity to yeast Sec23p
            component of COPII. COPII is the coat protein complex responsible
            for vesicle budding from the ER. The function of this gene product
            has been implicated in cargo selection and concentration. Multiple
            alternatively spliced transcript variants have been identified in
            this gene. [provided by RefSeq, Feb 2010].
            
            Transcript Variant: This variant (5) uses an alternative splice
            site and lacks an in-frame segment in the 5' CDS, as compared to
            variant 2. The resulting isoform (2) lacks an internal segment, as
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.171792.1, AK296270.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..749
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..749
                     /product="protein transport protein Sec23B isoform 2"
                     /note="SEC23-like protein B; SEC23 homolog B, coat complex
                     II component; SEC23-related protein B; protein transport
                     protein Sec23B; transport protein SEC23B; SEC23 homolog B,
                     COPII coat complex component"
                     /calculated_mol_wt=84342
     Region          12..747
                     /region_name="PLN00162"
                     /note="transport protein sec23; Provisional"
                     /db_xref="CDD:215083"
     CDS             1..749
                     /gene="SEC23B"
                     /gene_synonym="CDA-II; CDAII; CDAN2; CWS7; HEMPAS;
                     hSec23B"
                     /coded_by="NM_001172746.3:66..2315"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS86935.1"
                     /db_xref="GeneID:10483"
                     /db_xref="HGNC:HGNC:10702"
                     /db_xref="MIM:610512"
ORIGIN      
        1 matylefiqq neerdgvrfs wnvwpssrle atrmvvplac lltplkerpd lppvqyepvl
       61 csrptckavl nplcqvdyra klwacnfcfq rnqfppaygg isevnqpael mpqfstieyv
      121 iqeddlqalk eslqmslsll ppdalvglit fgrmvqvhel scegisksyv frgtkdltak
      181 qiqdmlgltk pampmqqarp aqpqehpfas srflqpvhki dmnltdllge lqrdpwpvtq
      241 gkrplrstgv alsiavglle gtfpntgari mlftggpptq gpgmvvgdel kipirswhdi
      301 ekdnarfmkk atkhyemlan rtaanghcid iyacaldqtg llemkccanl tggymvmgds
      361 fntslfkqtf qriftkdfng dfrmafgatl dvktsrelki agaigpcvsl nvkgpcvsen
      421 elgvggtsqw kicgldptst lgiyfevvnq hntpipqggr gaiqfvthyq hsstqrrirv
      481 ttiarnwadv qsqlrhieaa fdqeaaavlm arlgvfraes eegpdvlrwl drqlirlcqk
      541 fgqynkedpt sfrlsdsfsl ypqfmfhlrr spflqvfnns pdessyyrhh farqdltqsl
      601 imiqpilysy sfhgppepvl ldsssiladr illmdtffqi viylgetiaq wrkagyqdmp
      661 eyenfkhllq aplddaqeil qarfpmpryi ntehggsqar fllskvnpsq thnnlyawgq
      721 etgapiltdd vslqvfmdhl kklavssac
//
LOCUS       NP_612493                292 aa            linear   PRI 20-NOV-2025
DEFINITION  shugoshin 1 isoform 1KL [Homo sapiens].
ACCESSION   NP_612493
VERSION     NP_612493.1
DBSOURCE    REFSEQ: accession NM_138484.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 292)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494477.1, AB193066.1 and
            AB187578.1.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (Sgo1L, PMID:15737064; also known
            as sSGO1, PMID:18331714 or C2) differs in the 5' UTR, lacks an
            alternate in-frame exon in its central coding region, and contains
            an alternate 3' terminal segment compared to variant 1, resulting
            in a novel 3' coding region and distinct 3' UTR. It encodes isoform
            1KL which is shorter, has a distinct internal amino acid, and has a
            distinct C-terminus, compared to isoform 1. Both variants Sgo1K and
            Sgo1L encode the same isoform (1KL).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB187582.1, BC017867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..292
                     /product="shugoshin 1 isoform 1KL"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=33370
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          205..226
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     CDS             1..292
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_138484.5:156..1034"
                     /note="isoform 1KL is encoded by transcript variant Sgo1L"
                     /db_xref="CCDS:CCDS2635.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqieat ppetqqsphl slkditnvsl
      181 ypvvkirrls lspkknkasp avalpkrrct asvnykeptl asklrrgdpf tdlcflnspi
      241 fkqkkdlrrs kkralevspa keaifilyyv refvsrfpdc rkcklethic lr
//
LOCUS       NP_006436               2335 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-processing-splicing factor 8 [Homo sapiens].
ACCESSION   NP_006436 XP_005256471
VERSION     NP_006436.3
DBSOURCE    REFSEQ: accession NM_006445.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2335)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2335)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2335)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2335)
  AUTHORS   Atkinson,R., Georgiou,M., Yang,C., Szymanska,K., Lahat,A.,
            Vasconcelos,E.J.R., Ji,Y., Moya Molina,M., Collin,J., Queen,R.,
            Dorgau,B., Watson,A., Kurzawa-Akanbi,M., Laws,R., Saxena,A., Shyan
            Beh,C., Siachisumo,C., Goertler,F., Karwatka,M., Davey,T.,
            Inglehearn,C.F., McKibbin,M., Luhrmann,R., Steel,D.H.,
            Elliott,D.J., Armstrong,L., Urlaub,H., Ali,R.R., Grellscheid,S.N.,
            Johnson,C.A., Mozaffari-Jovin,S. and Lako,M.
  TITLE     PRPF8-mediated dysregulation of hBrr2 helicase disrupts human
            spliceosome kinetics and 5 -splice-site selection causing
            tissue-specific defects
  JOURNAL   Nat Commun 15 (1), 3138 (2024)
   PUBMED   38605034
  REMARK    GeneRIF: PRPF8-mediated dysregulation of hBrr2 helicase disrupts
            human spliceosome kinetics and 5 -splice-site selection causing
            tissue-specific defects.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2335)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 2335)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   7  (residues 1 to 2335)
  AUTHORS   Garcia-Blanco,M.A., Anderson,G.J., Beggs,J. and Sharp,P.A.
  TITLE     A mammalian protein of 220 kDa binds pre-mRNAs in the spliceosome:
            a potential homologue of the yeast PRP8 protein
  JOURNAL   Proc Natl Acad Sci U S A 87 (8), 3082-3086 (1990)
   PUBMED   2139226
REFERENCE   8  (residues 1 to 2335)
  AUTHORS   Anderson,G.J., Bach,M., Luhrmann,R. and Beggs,J.D.
  TITLE     Conservation between yeast and man of a protein associated with U5
            small nuclear ribonucleoprotein
  JOURNAL   Nature 342 (6251), 819-821 (1989)
   PUBMED   2532307
REFERENCE   9  (residues 1 to 2335)
  AUTHORS   Pinto,A.L. and Steitz,J.A.
  TITLE     The mammalian analogue of the yeast PRP8 splicing protein is
            present in the U4/5/6 small nuclear ribonucleoprotein particle and
            the spliceosome
  JOURNAL   Proc Natl Acad Sci U S A 86 (22), 8742-8746 (1989)
   PUBMED   2479028
REFERENCE   10 (residues 1 to 2335)
  AUTHORS   Bach,M., Winkelmann,G. and Luhrmann,R.
  TITLE     20S small nuclear ribonucleoprotein U5 shows a surprisingly complex
            protein composition
  JOURNAL   Proc Natl Acad Sci U S A 86 (16), 6038-6042 (1989)
   PUBMED   2527369
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD698473.1, DB081408.1 and
            BC064370.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005256471.1, NP_006436.2.
            
            Summary: Pre-mRNA splicing occurs in 2 sequential
            transesterification steps. The protein encoded by this gene is a
            component of both U2- and U12-dependent spliceosomes, and found to
            be essential for the catalytic step II in pre-mRNA splicing
            process. It contains several WD repeats, which function in
            protein-protein interactions. This protein has a sequence
            similarity to yeast Prp8 protein. This gene is a candidate gene for
            autosomal dominant retinitis pigmentosa. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064370.1, SRR1803615.266153.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304992.11/ ENSP00000304350.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..2335
                     /product="pre-mRNA-processing-splicing factor 8"
                     /note="U5 snRNP-specific protein (220 kD), ortholog of S.
                     cerevisiae Prp8p; precursor mRNA processing protein;
                     splicing factor Prp8; apoptosis-regulated protein 2;
                     apoptosis-regulated protein 1; p220; PRP8 homolog; 220 kDa
                     U5 snRNP-specific protein; PRP8 pre-mRNA processing factor
                     8 homolog"
                     /calculated_mol_wt=273471
     Region          1..2335
                     /region_name="PRP8"
                     /note="U5 snRNP spliceosome subunit [RNA processing and
                     modification]; COG5178"
                     /db_xref="CDD:227505"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.4,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          812..1303
                     /region_name="Reverse transcriptase homology domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Site            859
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          1304..1577
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Site            1358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Site            1425
                     /site_type="methylation"
                     /note="N6,N6-dimethyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Site            1463
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          1513..1526
                     /region_name="Important for branch point selection.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          1581..1752
                     /region_name="Restriction endonuclease homology domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          1669..2034
                     /region_name="Involved in interaction with pre-mRNA 5'
                     splice site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          1767..2020
                     /region_name="RNase H homology domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     Region          2301..2335
                     /region_name="Required for interaction with EFTUD2 and
                     SNRNP200. /evidence=ECO:0000269|PubMed:17317632"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2Q9.2)"
     CDS             1..2335
                     /gene="PRPF8"
                     /gene_synonym="HPRP8; PRP8; PRPC8; RP13; SNRNP220"
                     /coded_by="NM_006445.4:100..7107"
                     /db_xref="CCDS:CCDS11010.1"
                     /db_xref="GeneID:10594"
                     /db_xref="HGNC:HGNC:17340"
                     /db_xref="MIM:607300"
ORIGIN      
        1 magvfpyrgp gnpvpgplap lpdymseekl qekarkwqql qakryaekrk fgfvdaqked
       61 mppehvrkii rdhgdmtnrk frhdkrvylg alkymphavl kllenmpmpw eqirdvpvly
      121 hitgaisfvn eipwviepvy isqwgsmwim mrrekrdrrh fkrmrfppfd deeppldyad
      181 nildveplea iqleldpeed apvldwfydh qplrdsrkyv ngstyqrwqf tlpmmstlyr
      241 lanqlltdlv ddnyfylfdl kafftskaln maipggpkfe plvrdinlqd edwnefndin
      301 kiiirqpirt eykiafpyly nnlphhvhlt wyhtpnvvfi ktedpdlpaf yfdplinpis
      361 hrhsvksqep lpdddeefel pefvepflkd tplytdntan giallwaprp fnlrsgrtrr
      421 aldiplvknw yrehcpagqp vkvrvsyqkl lkyyvlnalk hrppkaqkkr ylfrsfkatk
      481 ffqstkldwv evglqvcrqg ynmlnllihr knlnylhldy nfnlkpvktl ttkerkksrf
      541 gnafhlcrev lrltklvvds hvqyrlgnvd afqladglqy ifahvgqltg myrykyklmr
      601 qirmckdlkh liyyrfntgp vgkgpgcgfw aagwrvwlff mrgitpller wlgnllarqf
      661 egrhskgvak tvtkqrvesh fdlelraavm hdildmmpeg ikqnkartil qhlseawrcw
      721 kanipwkvpg lptpienmil ryvkakadww tntahynrer irrgatvdkt vckknlgrlt
      781 rlylkaeqer qhnylkdgpy itaeeavavy tttvhwlesr rfspipfppl sykhdtklli
      841 lalerlkeay svksrlnqsq reelglieqa ydnphealsr ikrhlltqra fkevgiefmd
      901 lyshlvpvyd veplekitda yldqylwyea dkrrlfppwi kpadtepppl lvykwcqgin
      961 nlqdvwetse gecnvmlesr fekmyekidl tllnrllrli vdhniadymt aknnvvinyk
     1021 dmnhtnsygi irglqfasfi vqyyglvmdl lvlglhrase magppqmpnd flsfqdiate
     1081 aahpirlfcr yidrihiffr ftadeardli qryltehpdp nnenivgynn kkcwprdarm
     1141 rlmkhdvnlg ravfwdiknr lprsvttvqw ensfvsvysk dnpnllfnmc gfecrilpkc
     1201 rtsyeefthk dgvwnlqnev tkertaqcfl rvddesmqrf hnrvrqilma sgsttftkiv
     1261 nkwntaligl mtyfreavvn tqelldllvk cenkiqtrik iglnskmpsr fppvvfytpk
     1321 elgglgmlsm ghvlipqsdl rwskqtdvgi thfrsgmshe edqlipnlyr yiqpwesefi
     1381 dsqrvwaeya lkrqeaiaqn rrltledled swdrgiprin tlfqkdrhtl aydkgwrvrt
     1441 dfkqyqvlkq npfwwthqrh dgklwnlnny rtdmiqalgg vegilehtlf kgtyfptweg
     1501 lfwekasgfe esmkwkkltn aqrsglnqip nrrftlwwsp tinranvyvg fqvqldltgi
     1561 fmhgkiptlk isliqifrah lwqkihesiv mdlcqvfdqe ldaleietvq ketihprksy
     1621 kmnsscadil lfasykwnvs rpslladskd vmdstttqky widiqlrwgd ydshdierya
     1681 rakfldyttd nmsiypsptg vliaidlayn lhsaygnwfp gskpliqqam akimkanpal
     1741 yvlrerirkg lqlyssepte pylssqnyge lfsnqiiwfv ddtnvyrvti hktfegnltt
     1801 kpingaifif nprtgqlflk iihtsvwagq krlgqlakwk taeevaalir slpveeqpkq
     1861 iivtrkgmld plevhlldfp nivikgselq lpfqaclkve kfgdlilkat epqmvlfnly
     1921 ddwlktissy tafsrlilil ralhvnndra kvilkpdktt itephhiwpt ltdeewikve
     1981 vqlkdlilad ygkknnvnva sltqseirdi ilgmeisaps qqrqqiaeie kqtkeqsqlt
     2041 atqtrtvnkh gdeiitstts nyetqtfssk tewrvraisa anlhlrtnhi yvssddiket
     2101 gytyilpknv lkkficisdl raqiagylyg vsppdnpqvk eircivmvpq wgthqtvhlp
     2161 gqlpqheylk emeplgwiht qpnespqlsp qdvtthakim adnpswdgek tiiitcsftp
     2221 gsctltaykl tpsgyewgrq ntdkgnnpkg ylpshyervq mllsdrflgf fmvpaqsswn
     2281 ynfmgvrhdp nmkyelqlan pkefyhevhr pshflnfall qegevysadr edlya
//
LOCUS       NP_001164979             146 aa            linear   PRI 20-NOV-2025
DEFINITION  multiple coagulation factor deficiency protein 2 isoform A
            precursor [Homo sapiens].
ACCESSION   NP_001164979
VERSION     NP_001164979.1
DBSOURCE    REFSEQ: accession NM_001171508.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Zhang,Y., Liu,Z. and Zhang,B.
  TITLE     Separate roles of LMAN1 and MCFD2 in ER-to-Golgi trafficking of FV
            and FVIII
  JOURNAL   Blood Adv 7 (7), 1286-1296 (2023)
   PUBMED   36490287
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Zhang,Y., Zhu,M., Zheng,C., Wei,W., Emmer,B.T. and Zhang,B.
  TITLE     LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi transport
            of alpha1-antitrypsin
  JOURNAL   Biochem J 479 (7), 839-855 (2022)
   PUBMED   35322856
  REMARK    GeneRIF: LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi
            transport of alpha1-antitrypsin.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Guy,J.E., Wigren,E., Svard,M., Hard,T. and Lindqvist,Y.
  TITLE     New insights into multiple coagulation factor deficiency from the
            solution structure of human MCFD2
  JOURNAL   J Mol Biol 381 (4), 941-955 (2008)
   PUBMED   18590741
  REMARK    GeneRIF: These results provide an explanation for the previously
            observed calcium dependence of the MCFD2-ERGIC-53 interaction.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Mohanty,D., Ghosh,K., Shetty,S., Spreafico,M., Garagiola,I. and
            Peyvandi,F.
  TITLE     Mutations in the MCFD2 gene and a novel mutation in the LMAN1 gene
            in Indian families with combined deficiency of factor V and VIII
  JOURNAL   Am J Hematol 79 (4), 262-266 (2005)
   PUBMED   16044454
  REMARK    GeneRIF: Mutations in (LMAN1) and (MCFD2), have been found to be
            responsible for the dual deficiency of FV and FVIII.
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Zhang,B., Cunningham,M.A., Nichols,W.C., Bernat,J.A., Seligsohn,U.,
            Pipe,S.W., McVey,J.H., Schulte-Overberg,U., de Bosch,N.B.,
            Ruiz-Saez,A., White,G.C., Tuddenham,E.G., Kaufman,R.J. and
            Ginsburg,D.
  TITLE     Bleeding due to disruption of a cargo-specific ER-to-Golgi
            transport complex
  JOURNAL   Nat Genet 34 (2), 220-225 (2003)
   PUBMED   12717434
  REMARK    GeneRIF: inactivating mutations in MCFD2 cause combined deficiency
            of factor V and factor VIII with a phenotype indistinguishable from
            that caused by mutations in LMAN1
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Nichols,W.C., Terry,V.H., Wheatley,M.A., Yang,A., Zivelin,A.,
            Ciavarella,N., Stefanile,C., Matsushita,T., Saito,H., de
            Bosch,N.B., Ruiz-Saez,A., Torres,A., Thompson,A.R., Feinstein,D.I.,
            White,G.C., Negrier,C., Vinciguerra,C., Aktan,M., Kaufman,R.J.,
            Ginsburg,D. and Seligsohn,U.
  TITLE     ERGIC-53 gene structure and mutation analysis in 19 combined
            factors V and VIII deficiency families
  JOURNAL   Blood 93 (7), 2261-2266 (1999)
   PUBMED   10090935
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Neerman-Arbez,M., Johnson,K.M., Morris,M.A., McVey,J.H.,
            Peyvandi,F., Nichols,W.C., Ginsburg,D., Rossier,C.,
            Antonarakis,S.E. and Tuddenham,E.G.
  TITLE     Molecular analysis of the ERGIC-53 gene in 35 families with
            combined factor V-factor VIII deficiency
  JOURNAL   Blood 93 (7), 2253-2260 (1999)
   PUBMED   10090934
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Deka,N., Wong,E., Matera,A.G., Kraft,R., Leinwand,L.A. and
            Schmid,C.W.
  TITLE     Repetitive nucleotide sequence insertions into a novel
            calmodulin-related gene and its processed pseudogene
  JOURNAL   Gene 71 (1), 123-134 (1988)
   PUBMED   2463956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC332658.1, DC321899.1,
            AK292127.1, AF537214.1 and AI371370.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a soluble luminal protein with two
            calmodulin-like EF-hand motifs at its C-terminus. This protein
            forms a complex with LMAN1 (lectin mannose binding protein 1; also
            known as ERGIC-53) that facilitates the transport of coagulation
            factors V (FV) and VIII (FVIII) from the endoplasmic reticulum to
            the Golgi apparatus via an endoplasmic reticulum Golgi intermediate
            compartment (ERGIC). Mutations in this gene cause combined
            deficiency of FV and FVIII (F5F8D); a rare autosomal recessive
            bleeding disorder characterized by mild to moderate bleeding and
            coordinate reduction in plasma FV and FVIII levels. This protein
            has also been shown to maintain stem cell potential in adult
            central nervous system and is a marker for testicular germ cell
            tumors. The 3' UTR of this gene contains a transposon-like human
            repeat element named 'THE 1'. A processed RNA pseudogene of this
            gene is on chromosome 6p22.1. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms. [provided
            by RefSeq, Apr 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, 3 and 4 encode the same
            isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.215534.1,
                                           SRR1803617.276733.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p21"
     Protein         1..146
                     /product="multiple coagulation factor deficiency protein 2
                     isoform A precursor"
                     /note="neural stem cell-derived neuronal survival protein"
                     /calculated_mol_wt=13525
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2884
     Region          77..143
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K5B3; propagated from
                     UniProtKB/Swiss-Prot (Q8NI22.1)"
     CDS             1..146
                     /gene="MCFD2"
                     /gene_synonym="F5F8D; F5F8D2; LMAN1IP; SDNSF"
                     /coded_by="NM_001171508.2:291..731"
                     /note="isoform A precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS33192.1"
                     /db_xref="GeneID:90411"
                     /db_xref="HGNC:HGNC:18451"
                     /db_xref="MIM:607788"
ORIGIN      
        1 mtmrsllrtp flcgllwafc apgaraeepa asfsqpgsmg ldkntvhdqe himehlegvi
       61 nkpeaemspq elqlhyfkmh dydgnnlldg lelstaithv hkeegseqap lmsedelini
      121 idgvlrdddk nndgyidyae fakslq
//
LOCUS       NP_056138                794 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 UFM1-protein ligase 1 [Homo sapiens].
ACCESSION   NP_056138
VERSION     NP_056138.1
DBSOURCE    REFSEQ: accession NM_015323.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 794)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 794)
  AUTHORS   He,C., Xing,X., Chen,H.Y., Gao,M., Shi,J., Xiang,B., Xiao,X.,
            Sun,Y., Yu,H., Xu,G., Yao,Y., Xie,Z., Xing,Y., Budiarto,B.R.,
            Chen,S.Y., Gao,Y., Lee,Y.R. and Zhang,J.
  TITLE     UFL1 ablation in T cells suppresses PD-1 UFMylation to enhance
            anti-tumor immunity
  JOURNAL   Mol Cell 84 (6), 1120-1138 (2024)
   PUBMED   38377992
REFERENCE   3  (residues 1 to 794)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   4  (residues 1 to 794)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   5  (residues 1 to 794)
  AUTHORS   Luo,H., Jiao,Q.B., Shen,C.B., Gong,W.Y., Yuan,J.H., Liu,Y.Y.,
            Chen,Z., Liu,J., Xu,X.L., Cong,Y.S. and Zhang,X.W.
  TITLE     UFMylation of HRD1 regulates endoplasmic reticulum homeostasis
  JOURNAL   FASEB J 37 (11), e23221 (2023)
   PUBMED   37795761
REFERENCE   6  (residues 1 to 794)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 794)
  AUTHORS   Lee,J.H. and Paull,T.T.
  TITLE     Direct activation of the ATM protein kinase by the Mre11/Rad50/Nbs1
            complex
  JOURNAL   Science 304 (5667), 93-96 (2004)
   PUBMED   15064416
REFERENCE   8  (residues 1 to 794)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 794)
  AUTHORS   Gatei,M., Young,D., Cerosaletti,K.M., Desai-Mehta,A., Spring,K.,
            Kozlov,S., Lavin,M.F., Gatti,R.A., Concannon,P. and Khanna,K.
  TITLE     ATM-dependent phosphorylation of nibrin in response to radiation
            exposure
  JOURNAL   Nat Genet 25 (1), 115-119 (2000)
   PUBMED   10802669
REFERENCE   10 (residues 1 to 794)
  AUTHORS   Shirabe,K., Yubisui,T., Borgese,N., Tang,C.Y., Hultquist,D.E. and
            Takeshita,M.
  TITLE     Enzymatic instability of NADH-cytochrome b5 reductase as a cause of
            hereditary methemoglobinemia type I (red cell type)
  JOURNAL   J Biol Chem 267 (28), 20416-20421 (1992)
   PUBMED   1400360
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL590404.5, BP337693.1, AB018319.1 and BC028608.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036379.2, SRR1660803.203761.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369278.5/ ENSP00000358283.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..794
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..794
                     /product="E3 UFM1-protein ligase 1"
                     /note="novel LZAP-binding protein; Regulator of CDK5RAP3
                     and DDRGK1; regulator of C53/LZAP and DDRGK1; E3
                     UFM1-protein transferase 1; multiple alpha-helix protein
                     located at ER"
                     /calculated_mol_wt=89464
     Region          2..212
                     /region_name="Required for E3 UFM1-protein ligase
                     activity. /evidence=ECO:0000269|PubMed:20018847"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Region          2..200
                     /region_name="Mediates interaction with DDRGK1.
                     /evidence=ECO:0000269|PubMed:25219498"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O94874.2)"
     Region          7..284
                     /region_name="E3_UFM1_ligase"
                     /note="E3 UFM1-protein ligase 1; pfam09743"
                     /db_xref="CDD:462874"
     Region          121..250
                     /region_name="Involved in CDK5RAP3-binding.
                     /evidence=ECO:0000269|PubMed:20164180"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Region          200..400
                     /region_name="Mediates interaction with TRIP4.
                     /evidence=ECO:0000269|PubMed:25219498"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Region          407..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Site            433
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8CCJ3; propagated from
                     UniProtKB/Swiss-Prot (O94874.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:30886146; propagated from
                     UniProtKB/Swiss-Prot (O94874.2)"
     Region          490..684
                     /region_name="Mediates interaction with CDK5RAP3.
                     /evidence=ECO:0000250|UniProtKB:B2GV24"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000269|PubMed:38377992; propagated from
                     UniProtKB/Swiss-Prot (O94874.2)"
     Region          745..770
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94874.2)"
     CDS             1..794
                     /gene="UFL1"
                     /gene_synonym="KIAA0776; Maxer; NLBP; RCAD"
                     /coded_by="NM_015323.5:69..2453"
                     /db_xref="CCDS:CCDS5034.1"
                     /db_xref="GeneID:23376"
                     /db_xref="HGNC:HGNC:23039"
                     /db_xref="MIM:613372"
ORIGIN      
        1 madaweeirr laadfqraqf aeatqrlser ncieivnkli aqkqlevvht ldgkeyitpa
       61 qiskemrdel hvrggrvniv dlqqvinvdl ihienrigdi iksekhvqlv lgqlidenyl
      121 drlaeevndk lqesgqvtis elcktydlpg nfltqaltqr lgriisghid ldnrgvifte
      181 afvarhkari rglfsaitrp tavnslisky gfqeqllysv leelvnsgrl rgtvvggrqd
      241 kavfvpdiys rtqstwvdsf frqngylefd alsrlgipda vsyikkrykt tqllflkaac
      301 vgqglvdqve asveeaissg twvdiapllp tslsvedaai llqqvmrafs kqastvvfsd
      361 tvvvsekfin dctelfrelm hqkaekemkn npvhliteed lkqistlesv stskkdkkde
      421 rrrkategsg smrgggggna reykikkvkk kgrkdddsdd esqsshtgkk kpeisfmfqd
      481 eiedflrkhi qdapeefise laeylikpln ktylevvrsv fmssttsasg tgrkrtikdl
      541 qeevsnlynn irlfekgmkf faddtqaalt khllksvctd itnlifnfla sdlmmavddp
      601 aaitseirkk ilsklseetk valtklhnsl neksiedfis cldsaaeacd imvkrgdkkr
      661 erqilfqhrq alaeqlkvte dpalilhlts vllfqfsths mlhapgrcvp qiiaflnski
      721 pedqhallvk yqglvvkqlv sqskktgqgd yplnneldke qedvasttrk elqelsssik
      781 dlvlksrkss vtee
//
LOCUS       NP_060231                139 aa            linear   PRI 20-NOV-2025
DEFINITION  proline-rich nuclear receptor coactivator 2 [Homo sapiens].
ACCESSION   NP_060231 XP_001713933
VERSION     NP_060231.1
DBSOURCE    REFSEQ: accession NM_017761.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Nicholson,P., Gkratsou,A., Josi,C., Colombo,M. and Muhlemann,O.
  TITLE     Dissecting the functions of SMG5, SMG7, and PNRC2 in
            nonsense-mediated mRNA decay of human cells
  JOURNAL   RNA 24 (4), 557-573 (2018)
   PUBMED   29348139
  REMARK    GeneRIF: UPF1 interacts with PNRC2 and that it triggers 5'-3'
            exonucleolytic decay of reporter transcripts in tethering assays.
            PNRC2 is probably an important mRNA decapping factor but that it
            does not appear to be required for nonsense-mediated mRNA decay.
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Lai,T., Cho,H., Liu,Z., Bowler,M.W., Piao,S., Parker,R., Kim,Y.K.
            and Song,H.
  TITLE     Structural basis of the PNRC2-mediated link between mrna
            surveillance and decapping
  JOURNAL   Structure 20 (12), 2025-2037 (2012)
   PUBMED   23085078
  REMARK    GeneRIF: PNRC2 acts in synergy with Dcp1a to stimulate the
            decapping activity of Dcp2 by bridging the interaction between
            Dcp1a and Dcp2.
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Cho,H., Kim,K.M. and Kim,Y.K.
  TITLE     Human proline-rich nuclear receptor coregulatory protein 2 mediates
            an interaction between mRNA surveillance machinery and decapping
            complex
  JOURNAL   Mol Cell 33 (1), 75-86 (2009)
   PUBMED   19150429
  REMARK    GeneRIF: PNRC2 plays an essential role in mammalian
            Nonsense-mediated mRNA decay (NMD), mediating the interaction
            between the NMD machinery and the decapping complex.
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Hentschke,M. and Borgmeyer,U.
  TITLE     Identification of PNRC2 and TLE1 as activation function-1 cofactors
            of the orphan nuclear receptor ERRgamma
  JOURNAL   Biochem Biophys Res Commun 312 (4), 975-982 (2003)
   PUBMED   14651967
  REMARK    GeneRIF: Not only PNRC2 but also the corepressor TLE1 functioned as
            ERRgamma coactivator in a reporter gene analysis.
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Zhou,D. and Chen,S.
  TITLE     PNRC2 is a 16 kDa coactivator that interacts with nuclear receptors
            through an SH3-binding motif
  JOURNAL   Nucleic Acids Res 29 (19), 3939-3948 (2001)
   PUBMED   11574675
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Zhou,D., Quach,K.M., Yang,C., Lee,S.Y., Pohajdak,B. and Chen,S.
  TITLE     PNRC: a proline-rich nuclear receptor coregulatory protein that
            modulates transcriptional activation of multiple nuclear receptors
            including orphan receptors SF1 (steroidogenic factor 1) and
            ERRalpha1 (estrogen related receptor alpha-1)
  JOURNAL   Mol Endocrinol 14 (7), 986-998 (2000)
   PUBMED   10894149
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA043474.1, BC078177.1, BC001959.1 and AK311305.1.
            
            On Jul 8, 2009 this sequence version replaced XP_001713933.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.32589.1,
                                           SRR1660803.47214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334351.8/ ENSP00000334840.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..139
                     /product="proline-rich nuclear receptor coactivator 2"
                     /calculated_mol_wt=15459
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ4.1)"
     Region          61..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ4.1)"
     Region          89..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ4.1)"
     Region          93..111
                     /region_name="PNRC"
                     /note="Proline-rich nuclear receptor coactivator motif;
                     pfam15365"
                     /db_xref="CDD:464675"
     Region          99..105
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPJ4.1)"
     CDS             1..139
                     /gene="PNRC2"
                     /coded_by="NM_017761.4:396..815"
                     /db_xref="CCDS:CCDS246.1"
                     /db_xref="GeneID:55629"
                     /db_xref="HGNC:HGNC:23158"
                     /db_xref="MIM:611882"
ORIGIN      
        1 mgggerynip apqsrnvskn qqqlnrqktk eqnsqmkivh kkkerghgyn ssaaawqamq
       61 nggknknfpn nqswnsslsg prllfksqan qnyagakfse ppspsvlpkp pshwvpvsfn
      121 psdkeimtfq lktllkvqv
//
LOCUS       NP_002303                911 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA ligase 4 isoform 1 [Homo sapiens].
ACCESSION   NP_002303
VERSION     NP_002303.2
DBSOURCE    REFSEQ: accession NM_002312.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 911)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 911)
  AUTHORS   Bayat,L., Abbasi,S., Balasuriya,N. and Schild-Poulter,C.
  TITLE     Critical residues in the Ku70 von Willebrand A domain mediate Ku
            interaction with the LigIV-XRCC4 complex in non-homologous
            end-joining
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (7), 119815 (2024)
   PUBMED   39151475
  REMARK    GeneRIF: Critical residues in the Ku70 von Willebrand A domain
            mediate Ku interaction with the LigIV-XRCC4 complex in
            non-homologous end-joining.
REFERENCE   3  (residues 1 to 911)
  AUTHORS   Nicolle,R., Boutaud,L., Loeuillet,L., Talhi,N., Grotto,S.,
            Bourgon,N., Feresin,A., Coussement,A., Barrois,M., Beaujard,M.P.,
            Rambaud,T., Razavi,F. and Attie-Bitach,T.
  TITLE     Expanding the phenotypic spectrum of LIG4 pathogenic variations:
            neuro-histopathological description of 4 fetuses with stenosis of
            the aqueduct
  JOURNAL   Eur J Hum Genet 32 (5), 545-549 (2024)
   PUBMED   38351293
  REMARK    GeneRIF: Expanding the phenotypic spectrum of LIG4 pathogenic
            variations: neuro-histopathological description of 4 fetuses with
            stenosis of the aqueduct.
REFERENCE   4  (residues 1 to 911)
  AUTHORS   Deng,Y., Ke,T.W., Yueh,T.C., Chin,Y.T., Wang,Y.C., Hung,Y.C.,
            Mong,M.C., Yang,Y.C., Wu,W.T., Chang,W.S., Gu,J., Bau,D.T. and
            Tsai,C.W.
  TITLE     The Contribution of DNA Ligase 4 Polymorphisms to Colorectal Cancer
  JOURNAL   In Vivo 38 (1), 127-133 (2024)
   PUBMED   38148049
  REMARK    GeneRIF: The Contribution of DNA Ligase 4 Polymorphisms to
            Colorectal Cancer.
REFERENCE   5  (residues 1 to 911)
  AUTHORS   Kumari,N., Antil,H., Kumari,S. and Raghavan,S.C.
  TITLE     Deficiency of ligase IV leads to reduced NHEJ, accumulation of DNA
            damage, and can sensitize cells to cancer therapeutics
  JOURNAL   Genomics 115 (6), 110731 (2023)
   PUBMED   37871849
  REMARK    GeneRIF: Deficiency of ligase IV leads to reduced NHEJ,
            accumulation of DNA damage, and can sensitize cells to cancer
            therapeutics.
REFERENCE   6  (residues 1 to 911)
  AUTHORS   Leon,D.A., Chenet,L., Shkolnikov,V.M., Zakharov,S., Shapiro,J.,
            Rakhmanova,G., Vassin,S. and McKee,M.
  TITLE     Huge variation in Russian mortality rates 1984-94: artefact,
            alcohol, or what?
  JOURNAL   Lancet 350 (9075), 383-388 (1997)
   PUBMED   9259651
REFERENCE   7  (residues 1 to 911)
  AUTHORS   Critchlow,S.E., Bowater,R.P. and Jackson,S.P.
  TITLE     Mammalian DNA double-strand break repair protein XRCC4 interacts
            with DNA ligase IV
  JOURNAL   Curr Biol 7 (8), 588-598 (1997)
   PUBMED   9259561
REFERENCE   8  (residues 1 to 911)
  AUTHORS   Grawunder,U., Wilm,M., Wu,X., Kulesza,P., Wilson,T.E., Mann,M. and
            Lieber,M.R.
  TITLE     Activity of DNA ligase IV stimulated by complex formation with
            XRCC4 protein in mammalian cells
  JOURNAL   Nature 388 (6641), 492-495 (1997)
   PUBMED   9242410
REFERENCE   9  (residues 1 to 911)
  AUTHORS   Robins,P. and Lindahl,T.
  TITLE     DNA ligase IV from HeLa cell nuclei
  JOURNAL   J Biol Chem 271 (39), 24257-24261 (1996)
   PUBMED   8798671
REFERENCE   10 (residues 1 to 911)
  AUTHORS   Wei,Y.F., Robins,P., Carter,K., Caldecott,K., Pappin,D.J., Yu,G.L.,
            Wang,R.P., Shell,B.K., Nash,R.A., Schar,P. et al.
  TITLE     Molecular cloning and expression of human cDNAs encoding a novel
            DNA ligase IV and DNA ligase III, an enzyme active in DNA repair
            and recombination
  JOURNAL   Mol Cell Biol 15 (6), 3206-3216 (1995)
   PUBMED   7760816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X83441.1, BC037491.2,
            CD102896.1 and AI809944.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 19, 2002 this sequence version replaced NP_002303.1.
            
            Summary: The protein encoded by this gene is a DNA ligase that
            joins single-strand breaks in a double-stranded polydeoxynucleotide
            in an ATP-dependent reaction. This protein is essential for V(D)J
            recombination and DNA double-strand break (DSB) repair through
            nonhomologous end joining (NHEJ). This protein forms a complex with
            the X-ray repair cross complementing protein 4 (XRCC4), and further
            interacts with the DNA-dependent protein kinase (DNA-PK). Both
            XRCC4 and DNA-PK are known to be required for NHEJ. The crystal
            structure of the complex formed by this protein and XRCC4 has been
            resolved. Defects in this gene are the cause of LIG4 syndrome.
            Alternatively spliced transcript variants encoding the same protein
            have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1), as well as variants 2, 3, and
            5-10, encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X83441.1, SRR1660807.214250.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..911
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.3"
     Protein         1..911
                     /product="DNA ligase 4 isoform 1"
                     /EC_number="6.5.1.1"
                     /note="polynucleotide ligase; ligase IV, DNA,
                     ATP-dependent; DNA repair enzyme; DNA joinase;
                     polydeoxyribonucleotide synthase [ATP] 4; sealase; DNA
                     ligase IV"
                     /calculated_mol_wt=103840
     Region          81..602
                     /region_name="dnl1"
                     /note="DNA ligase I, ATP-dependent (dnl1); TIGR00574"
                     /db_xref="CDD:273147"
     Region          610..620
                     /region_name="Required for catalytic activity.
                     /evidence=ECO:0000269|PubMed:23523427"
                     /note="propagated from UniProtKB/Swiss-Prot (P49917.2)"
     Region          658..745
                     /region_name="BRCT_DNA_ligase_IV_rpt1"
                     /note="first BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17722"
                     /db_xref="CDD:349354"
     Region          750..783
                     /region_name="DNA_ligase_IV"
                     /note="DNA ligase IV; pfam11411"
                     /db_xref="CDD:463272"
     Region          813..900
                     /region_name="BRCT_DNA_ligase_IV_rpt2"
                     /note="second BRCT domain of DNA ligase 4 (LIG4) and
                     similar proteins; cd17717"
                     /db_xref="CDD:349349"
     Site            order(814,835..837,839..840,843..844,846..847,895,
                     898..899)
                     /site_type="other"
                     /note="XRCC4 interaction site [polypeptide binding]"
                     /db_xref="CDD:349349"
     CDS             1..911
                     /gene="LIG4"
                     /gene_synonym="LIG4S"
                     /coded_by="NM_002312.3:274..3009"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9508.1"
                     /db_xref="GeneID:3981"
                     /db_xref="HGNC:HGNC:6601"
                     /db_xref="MIM:601837"
ORIGIN      
        1 maasqtsqtv ashvpfadlc stleriqksk graekirhfr efldswrkfh dalhknhkdv
       61 tdsfypamrl ilpqlererm aygiketmla klyiellnlp rdgkdalkll nyrtptgthg
      121 dagdfamiay fvlkprclqk gsltiqqvnd lldsiasnns akrkdlikks llqlitqssa
      181 leqkwlirmi ikdlklgvsq qtifsvfhnd aaelhnvttd lekvcrqlhd psvglsdisi
      241 tlfsafkpml aaiadiehie kdmkhqsfyi etkldgermq mhkdgdvyky fsrngynytd
      301 qfgasptegs ltpfihnafk adiqicildg emmaynpntq tfmqkgtkfd ikrmvedsdl
      361 qtcycvfdvl mvnnkklghe tlrkryeils siftpipgri eivqktqaht knevidalne
      421 aidkreegim vkqplsiykp dkrgegwlki kpeyvsglmd eldilivggy wgkgsrggmm
      481 shflcavaek pppgekpsvf htlsrvgsgc tmkelydlgl klakywkpfh rkappssilc
      541 gtekpevyie pcnsvivqik aaeivpsdmy ktgctlrfpr iekirddkew hecmtlddle
      601 qlrgkasgkl askhlyiggd depqekkrka apkmkkvigi iehlkapnlt nvnkisnife
      661 dvefcvmsgt dsqpkpdlen riaefggyiv qnpgpdtycv iagsenirvk niilsnkhdv
      721 vkpawllecf ktksfvpwqp rfmihmcpst kehfareydc ygdsyfidtd lnqlkevfsg
      781 iknsneqtpe emasliadle yryswdcspl smfrrhtvyl dsyavindls tknegtrlai
      841 kalelrfhga kvvsclaegv shviigedhs rvadfkafrr tfkrkfkilk eswvtdsidk
      901 celqeenqyl i
//
LOCUS       NP_004851                673 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein FXR2 [Homo sapiens].
ACCESSION   NP_004851
VERSION     NP_004851.2
DBSOURCE    REFSEQ: accession NM_004860.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Li,M., Hou,Y., Zhou,Y., Yang,Z., Zhao,H., Jian,T., Yu,Q., Zeng,F.,
            Liu,X., Zhang,Z. and Zhao,Y.G.
  TITLE     LLPS of FXR proteins drives replication organelle clustering for
            beta-coronaviral proliferation
  JOURNAL   J Cell Biol 223 (6) (2024)
   PUBMED   38587486
  REMARK    GeneRIF: LLPS of FXR proteins drives replication organelle
            clustering for beta-coronaviral proliferation.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Tamanini,F., Bontekoe,C., Bakker,C.E., van Unen,L., Anar,B.,
            Willemsen,R., Yoshida,M., Galjaard,H., Oostra,B.A. and
            Hoogeveen,A.T.
  TITLE     Different targets for the fragile X-related proteins revealed by
            their distinct nuclear localizations
  JOURNAL   Hum Mol Genet 8 (5), 863-869 (1999)
   PUBMED   10196376
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Joseph,D.R.
  TITLE     The rat androgen-binding protein (ABP/SHBG) gene contains triplet
            repeats similar to unstable triplets: evidence that the ABP/SHBG
            and the fragile X-related 2 genes overlap
  JOURNAL   Steroids 63 (1), 2-4 (1998)
   PUBMED   9437788
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Tamanini,F., Willemsen,R., van Unen,L., Bontekoe,C., Galjaard,H.,
            Oostra,B.A. and Hoogeveen,A.T.
  TITLE     Differential expression of FMR1, FXR1 and FXR2 proteins in human
            brain and testis
  JOURNAL   Hum Mol Genet 6 (8), 1315-1322 (1997)
   PUBMED   9259278
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Siomi,M.C., Zhang,Y., Siomi,H. and Dreyfuss,G.
  TITLE     Specific sequences in the fragile X syndrome protein FMR1 and the
            FXR proteins mediate their binding to 60S ribosomal subunits and
            the interactions among them
  JOURNAL   Mol Cell Biol 16 (7), 3825-3832 (1996)
   PUBMED   8668200
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Zhang,Y., O'Connor,J.P., Siomi,M.C., Srinivasan,S., Dutra,A.,
            Nussbaum,R.L. and Dreyfuss,G.
  TITLE     The fragile X mental retardation syndrome protein interacts with
            novel homologs FXR1 and FXR2
  JOURNAL   EMBO J 14 (21), 5358-5366 (1995)
   PUBMED   7489725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA114906.1, BC020090.1 and
            AA593676.1.
            
            On Sep 22, 2009 this sequence version replaced NP_004851.1.
            
            Summary: The protein encoded by this gene is a RNA binding protein
            containing two KH domains and one RCG box, which is similar to FMRP
            and FXR1. It associates with polyribosomes, predominantly with 60S
            large ribosomal subunits. This encoded protein may self-associate
            or interact with FMRP and FXR1. It may have a role in the
            development of fragile X cognitive disability syndrome. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067272.1, U31501.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000250113.12/ ENSP00000250113.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..673
                     /product="RNA-binding protein FXR2"
                     /calculated_mol_wt=74092
     Region          13..67
                     /region_name="Tudor_Agenet_FXR2_rpt1"
                     /note="first Tudor-like Agenet domain found in fragile X
                     mental retardation syndrome-related protein 2 (FXR2) and
                     similar proteins; cd20473"
                     /db_xref="CDD:410544"
     Site            order(20,24,26,42,46,48)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410544"
     Region          69..136
                     /region_name="Tudor_Agenet_FXR2_rpt2"
                     /note="second Tudor-like Agenet domain found in fragile X
                     mental retardation syndrome-related protein 2 (FXR2) and
                     similar proteins; cd20476"
                     /db_xref="CDD:410547"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61584; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            order(79,88,90,106,111,113)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:410547"
     Region          133..209
                     /region_name="KH_I_FXR2_rpt1"
                     /note="first type I K homology (KH) RNA-binding domain
                     found in fragile X mental retardation syndrome-related
                     protein 2 (FXR2) and similar proteins; cd22505"
                     /db_xref="CDD:411933"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Region          228..290
                     /region_name="KH_I_FXR2_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in fragile X mental retardation syndrome-related
                     protein 2 (FXR2) and similar proteins; cd22508"
                     /db_xref="CDD:411936"
     Site            order(238,240..242,244..248,251..252,255..256,262..265)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411936"
     Region          291..368
                     /region_name="KH_I_FXR2_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in fragile X mental retardation syndrome-related
                     protein 2 (FXR2) and similar proteins; cd22511"
                     /db_xref="CDD:411939"
     Site            order(301,303..305,307..311,314..315,318..319,325..328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411939"
     Region          364..478
                     /region_name="FXMRP1_C_core"
                     /note="Fragile X-related 1 protein core C terminal;
                     pfam12235"
                     /db_xref="CDD:463501"
     Region          389..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51116.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61584; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Region          502..577
                     /region_name="FXR_C1"
                     /note="Fragile X-related 1 protein C-terminal region 2;
                     pfam16096"
                     /db_xref="CDD:465019"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51116.2)"
     Site            580
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51116.2)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51116.2)"
     CDS             1..673
                     /gene="FXR2"
                     /gene_synonym="FMR1L2; FXR2P"
                     /coded_by="NM_004860.4:366..2387"
                     /db_xref="CCDS:CCDS45604.1"
                     /db_xref="GeneID:9513"
                     /db_xref="HGNC:HGNC:4024"
                     /db_xref="MIM:605339"
ORIGIN      
        1 mgglasggdv epglpvevrg sngafykgfv kdvhedsvti ffennwqser qipfgdvrlp
       61 ppadynkeit egdevevysr aneqepcgww larvrmmkgd fyvieyaacd atyneivtle
      121 rlrpvnpnpl atkgsffkvt mavpedlrea csnenvhkef kkalgancif lnitnselfi
      181 lstteapvkr asllgdmhfr slrtklllms rneeatkhle tskqlaaafq eeftvredlm
      241 glaigthgan iqqarkvpgv taielgeetc tfriygetpe acrqarsyle fsedsvqvpr
      301 nlvgkvigkn gkviqeivdk sgvvrvrveg dndkknpree gmvpfifvgt renisnaqal
      361 leyhlsylqe veqlrlerlq ideqlrqigl gfrppgsgrg sggsdkagys tdessssslh
      421 atrtyggsyg grgrgrrtgg paygpssdvs tasetesekr eepnragpgd rdpptrgees
      481 rrrptggrgr gpppaprpts rynsssissv lkdpdsnpys lldtsepepp vdsepgeppp
      541 asarrrrsrr rrtdedrtvm dgglesdgpn mtengledes rpqrrnrsrr rrnrgnrtdg
      601 sisgdrqpvt vadyisraes qsrqrppler tkpsedslsg qkgdsvsklp kgpsengels
      661 aplelgsmvn gvs
//
LOCUS       NP_689985                519 aa            linear   PRI 20-NOV-2025
DEFINITION  T-complex protein 11-like protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_689985
VERSION     NP_689985.1
DBSOURCE    REFSEQ: accession NM_152772.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Scharf,J.M., Yu,D., Mathews,C.A., Neale,B.M., Stewart,S.E.,
            Fagerness,J.A., Evans,P., Gamazon,E., Edlund,C.K., Service,S.K.,
            Tikhomirov,A., Osiecki,L., Illmann,C., Pluzhnikov,A.,
            Konkashbaev,A., Davis,L.K., Han,B., Crane,J., Moorjani,P.,
            Crenshaw,A.T., Parkin,M.A., Reus,V.I., Lowe,T.L., Rangel-Lugo,M.,
            Chouinard,S., Dion,Y., Girard,S., Cath,D.C., Smit,J.H., King,R.A.,
            Fernandez,T.V., Leckman,J.F., Kidd,K.K., Kidd,J.R., Pakstis,A.J.,
            State,M.W., Herrera,L.D., Romero,R., Fournier,E., Sandor,P.,
            Barr,C.L., Phan,N., Gross-Tsur,V., Benarroch,F., Pollak,Y.,
            Budman,C.L., Bruun,R.D., Erenberg,G., Naarden,A.L., Lee,P.C.,
            Weiss,N., Kremeyer,B., Berrio,G.B., Campbell,D.D., Cardona
            Silgado,J.C., Ochoa,W.C., Mesa Restrepo,S.C., Muller,H., Valencia
            Duarte,A.V., Lyon,G.J., Leppert,M., Morgan,J., Weiss,R.,
            Grados,M.A., Anderson,K., Davarya,S., Singer,H., Walkup,J.,
            Jankovic,J., Tischfield,J.A., Heiman,G.A., Gilbert,D.L.,
            Hoekstra,P.J., Robertson,M.M., Kurlan,R., Liu,C., Gibbs,J.R.,
            Singleton,A., Hardy,J., Strengman,E., Ophoff,R.A., Wagner,M.,
            Moessner,R., Mirel,D.B., Posthuma,D., Sabatti,C., Eskin,E.,
            Conti,D.V., Knowles,J.A., Ruiz-Linares,A., Rouleau,G.A.,
            Purcell,S., Heutink,P., Oostra,B.A., McMahon,W.M., Freimer,N.B.,
            Cox,N.J. and Pauls,D.L.
  CONSRTM   North American Brain Expression Consortium; UK Human Brain
            Expression Database
  TITLE     Genome-wide association study of Tourette's syndrome
  JOURNAL   Mol Psychiatry 18 (6), 721-728 (2013)
   PUBMED   22889924
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079174.20, BC033617.1 and AC080012.20.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033617.1, SRR1660803.118370.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000299045.8/ ENSP00000299045.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..519
                     /product="T-complex protein 11-like protein 2 isoform 1"
                     /note="T-complex protein 11-like protein 2; t-complex 11,
                     testis-specific-like 2"
                     /calculated_mol_wt=57960
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N4U5.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q568Z0; propagated from
                     UniProtKB/Swiss-Prot (Q8N4U5.1)"
     Region          77..500
                     /region_name="Tcp11"
                     /note="T-complex protein 11; pfam05794"
                     /db_xref="CDD:461743"
     CDS             1..519
                     /gene="TCP11L2"
                     /coded_by="NM_152772.3:245..1804"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9104.1"
                     /db_xref="GeneID:255394"
                     /db_xref="HGNC:HGNC:28627"
                     /db_xref="MIM:619889"
ORIGIN      
        1 mpfngekqcv gedqpsdsds srfsesmasl sdyecsrqsf asdsssksss pastspprvv
       61 tfdevmatar nlsnltlahe iavnenfqlk qealpeksla grvkhivhqa fwdvldseln
      121 adppefehai klfeeireil lsfltpggnr lrnqicevld tdlirqqaeh savdiqglan
      181 yvistmgklc apvrdndire lkatgnivev lrqifhvldl mqmdmanfti mslrphlqrq
      241 lveyertkfq eileetpsal dqttewikes vneelfslse saltpgaent skpslsptlv
      301 lnnsylkllq wdyqkkelpe tlmtdgarlq elteklnqlk iiaclslitn nmvgaitggl
      361 pelasrltri savllegmnk etfnlkevln sigiqtcvev nktlmerglp tlnaeiqanl
      421 igqfssieee dnpiwslidk riklymrrll clpspqkcmp pmpgglaviq qelealgsqy
      481 anivnlnkqv ygpfyanilr kllfneeamg kvdaspptn
//
LOCUS       NP_001239160             613 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec24A isoform 2 [Homo sapiens].
ACCESSION   NP_001239160
VERSION     NP_001239160.1
DBSOURCE    REFSEQ: accession NM_001252231.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 613)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 613)
  AUTHORS   Gomez-Navarro,N., Maldutyte,J., Poljak,K., Peak-Chew,S.Y., Orme,J.,
            Bisnett,B.J., Lamb,C.H., Boyce,M., Gianni,D. and Miller,E.A.
  TITLE     Selective inhibition of protein secretion by abrogating
            receptor-coat interactions during ER export
  JOURNAL   Proc Natl Acad Sci U S A 119 (31), e2202080119 (2022)
   PUBMED   35901214
  REMARK    GeneRIF: Selective inhibition of protein secretion by abrogating
            receptor-coat interactions during ER export.
REFERENCE   3  (residues 1 to 613)
  AUTHORS   Zhang,Z., Yang,B., Zhou,S. and Wu,J.
  TITLE     CircRNA circ_SEC24A upregulates DNMT3A expression by sponging
            miR-26b-5p to aggravate osteoarthritis progression
  JOURNAL   Int Immunopharmacol 99, 107957 (2021)
   PUBMED   34325283
  REMARK    GeneRIF: CircRNA circ_SEC24A upregulates DNMT3A expression by
            sponging miR-26b-5p to aggravate osteoarthritis progression.
REFERENCE   4  (residues 1 to 613)
  AUTHORS   Chen,X., Zhang,J., Liu,P., Wei,Y., Wang,X., Xiao,J., Wang,C.C. and
            Wang,L.
  TITLE     Proteolytic processing of secretory pathway kinase Fam20C by site-1
            protease promotes biomineralization
  JOURNAL   Proc Natl Acad Sci U S A 118 (32) (2021)
   PUBMED   34349020
REFERENCE   5  (residues 1 to 613)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 613)
  AUTHORS   Tomarev,S.I., Wistow,G., Raymond,V., Dubois,S. and Malyukova,I.
  TITLE     Gene expression profile of the human trabecular meshwork: NEIBank
            sequence tag analysis
  JOURNAL   Invest Ophthalmol Vis Sci 44 (6), 2588-2596 (2003)
   PUBMED   12766061
REFERENCE   7  (residues 1 to 613)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   8  (residues 1 to 613)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   9  (residues 1 to 613)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   10 (residues 1 to 613)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK304060.1 and BC019341.1.
            
            Summary: The protein encoded by this gene belongs to a family of
            proteins that are homologous to yeast Sec24. This protein is a
            component of coat protein II (COPII)-coated vesicles that mediate
            protein transport from the endoplasmic reticulum. COPII acts in the
            cytoplasm to promote the transport of secretory, plasma membrane,
            and vacuolar proteins from the endoplasmic reticulum to the golgi
            complex. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (2) lacks several exons from the
            3' end, and contains an alternate 3' terminal exon compared to
            variant 1. This results in a shorter isoform (2) with a distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019341.1, SRR1803617.274817.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..613
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..613
                     /product="protein transport protein Sec24A isoform 2"
                     /note="protein transport protein Sec24A; SEC24-related
                     protein A; SEC24 related gene family, member A; SEC24
                     family, member A; SEC24 homolog A, COPII coat complex
                     component"
                     /calculated_mol_wt=65879
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          60..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          189..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          255..>592
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Region          294..328
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     Region          431..455
                     /region_name="Zinc finger-like"
                     /note="propagated from UniProtKB/Swiss-Prot (O95486.2)"
     CDS             1..613
                     /gene="SEC24A"
                     /coded_by="NM_001252231.2:293..2134"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58967.1"
                     /db_xref="GeneID:10802"
                     /db_xref="HGNC:HGNC:10703"
                     /db_xref="MIM:607183"
ORIGIN      
        1 msqpgipasg gapaslqaqn gaalasgspy tngpvqnall ssqesvsqgy nfqlpgsyph
       61 pipaktlnpv sgqsnyggsq gsgqtlnrpp vasnpvtpsl hsgpaprmpl pasqnpattp
      121 mpsssflpea nlppplnwqy nypstasqtn hcprassqpt vsgntslttn hqyvssgyps
      181 lqnsfiksgp svpplvnppl pttfqpgaph gpppaggppp vraltpltss yrdvpqplfn
      241 savnqegits ntnngsmvvh ssydeieggg llatpqltnk npkmsrsvgy sypslppgyq
      301 nttppgatgv ppsslnypsg pqaftqtplg anhlttsmsg lslqpeglrv vnllqernml
      361 pstplkppvp nlhediqkln cnpelfrctl tsipqtqall nkaklplgll lhpfkdlvql
      421 pvvtsstivr crscrtyinp fvsfldqrrw kcnlcyrvnd vpeeflynpl trvygephrr
      481 pevqnatief mapseymlrp pqppvylfvf dvshnavetg ylnsvcqsll dnldllpgnt
      541 rtkigfitfd stihfyglqe slsqpqmliv sdiedvfipm penllvnlne skesvigvss
      601 eetlitclei amr
//
LOCUS       NP_997464                320 aa            linear   PRI 20-NOV-2025
DEFINITION  dual oxidase maturation factor 2 [Homo sapiens].
ACCESSION   NP_997464
VERSION     NP_997464.2
DBSOURCE    REFSEQ: accession NM_207581.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Kohda,A., Kamakura,S., Hayase,J. and Sumimoto,H.
  TITLE     The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical plasma
            membrane in epithelial cells via their respective maturation
            factors DUOXA1 and DUOXA2
  JOURNAL   Genes Cells 29 (10), 921-930 (2024)
   PUBMED   39126279
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Wang,F., Zang,Y., Li,M., Liu,W., Wang,Y., Yu,X., Li,H., Wang,F. and
            Liu,S.
  TITLE     DUOX2 and DUOXA2 Variants Confer Susceptibility to Thyroid
            Dysgenesis and Gland-in-situ With Congenital Hypothyroidism
  JOURNAL   Front Endocrinol (Lausanne) 11, 237 (2020)
   PUBMED   32425884
  REMARK    GeneRIF: DUOX2 and DUOXA2 Variants Confer Susceptibility to Thyroid
            Dysgenesis and Gland-in-situ With Congenital Hypothyroidism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Poncelet,L., Dumont,J.E., Miot,F. and De Deken,X.
  TITLE     The Dual Oxidase Duox2 stabilized with DuoxA2 in an enzymatic
            complex at the surface of the cell produces extracellular H2O2 able
            to induce DNA damage in an inducible cellular model
  JOURNAL   Exp Cell Res 384 (1), 111620 (2019)
   PUBMED   31513783
  REMARK    GeneRIF: H2O2 produced by the Duox2/DuoxA2 cell surface enzymatic
            complex could provoke potential mutagenic DNA damage.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Peters,C., Nicholas,A.K., Schoenmakers,E., Lyons,G., Langham,S.,
            Serra,E.G., Sebire,N.J., Muzza,M., Fugazzola,L. and Schoenmakers,N.
  TITLE     DUOX2/DUOXA2 Mutations Frequently Cause Congenital Hypothyroidism
            that Evades Detection on Newborn Screening in the United Kingdom
  JOURNAL   Thyroid 29 (6), 790-801 (2019)
   PUBMED   31044655
  REMARK    GeneRIF: DUOX2/DUOXA2 Mutations Frequently Cause Congenital
            Hypothyroidism that Evades Detection on Newborn Screening in the
            United Kingdom.
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Wu,Y., Antony,S., Juhasz,A., Lu,J., Ge,Y., Jiang,G., Roy,K. and
            Doroshow,J.H.
  TITLE     Up-regulation and sustained activation of Stat1 are essential for
            interferon-gamma (IFN-gamma)-induced dual oxidase 2 (Duox2) and
            dual oxidase A2 (DuoxA2) expression in human pancreatic cancer cell
            lines
  JOURNAL   J Biol Chem 286 (14), 12245-12256 (2011)
   PUBMED   21321110
  REMARK    GeneRIF: Up-regulation and sustained activation of Stat1 are
            essential for interferon-gamma (IFN-gamma)-induced dual oxidase 2
            (Duox2) and dual oxidase A2 (DuoxA2) expression in human pancreatic
            cancer cell lines.
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Luxen,S., Noack,D., Frausto,M., Davanture,S., Torbett,B.E. and
            Knaus,U.G.
  TITLE     Heterodimerization controls localization of Duox-DuoxA NADPH
            oxidases in airway cells
  JOURNAL   J Cell Sci 122 (Pt 8), 1238-1247 (2009)
   PUBMED   19339556
  REMARK    GeneRIF: Heterodimerization controls localization of Duox-DuoxA
            NADPH oxidases in airway cells.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Eriksson,A., Flach,C.F., Lindgren,A., Kvifors,E. and Lange,S.
  TITLE     Five mucosal transcripts of interest in ulcerative colitis
            identified by quantitative real-time PCR: a prospective study
  JOURNAL   BMC Gastroenterol 8, 34 (2008)
   PUBMED   18700007
  REMARK    GeneRIF: The five gene transcripts (aldolase B, elafin, MST-1,
            simNIPhom and SLC6A14) were changed in patients with ulcerative
            colitis, and were related to the disease activity.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Zamproni,I., Grasberger,H., Cortinovis,F., Vigone,M.C.,
            Chiumello,G., Mora,S., Onigata,K., Fugazzola,L., Refetoff,S.,
            Persani,L. and Weber,G.
  TITLE     Biallelic inactivation of the dual oxidase maturation factor 2
            (DUOXA2) gene as a novel cause of congenital hypothyroidism
  JOURNAL   J Clin Endocrinol Metab 93 (2), 605-610 (2008)
   PUBMED   18042646
  REMARK    GeneRIF: Results provide evidence for the critical role of DUOXA2
            in thyroid hormonogenesis. Biallelic DUOXA2 mutations are a novel
            genetic event in permanent congenital hypothroidism.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Grasberger,H., De Deken,X., Miot,F., Pohlenz,J. and Refetoff,S.
  TITLE     Missense mutations of dual oxidase 2 (DUOX2) implicated in
            congenital hypothyroidism have impaired trafficking in cells
            reconstituted with DUOX2 maturation factor
  JOURNAL   Mol Endocrinol 21 (6), 1408-1421 (2007)
   PUBMED   17374849
  REMARK    GeneRIF: DUOXA2 allows rapid ER exit of folded DUOX2 or enhanced
            degradation of mutant DUOX2 proteins not competent for ER exit.
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Grasberger,H. and Refetoff,S.
  TITLE     Identification of the maturation factor for dual oxidase. Evolution
            of an eukaryotic operon equivalent
  JOURNAL   J Biol Chem 281 (27), 18269-18272 (2006)
   PUBMED   16651268
  REMARK    GeneRIF: co-expression of DUOXA2, an ER-resident transmembrane
            protein, allows ER-to-Golgi transition, maturation, and
            translocation to the plasma membrane of functional DUOX2 in a
            heterologous system
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC393748.1, BC137465.1,
            BM987789.1 and AC091117.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 19, 2006 this sequence version replaced NP_997464.1.
            
            Summary: This gene encodes an endoplasmic reticulum protein that is
            necessary for proper cellular localization and maturation of
            functional dual oxidase 2. Mutations in this gene have been
            associated with thyroid dyshormonogenesis 5.[provided by RefSeq,
            Feb 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC137465.1, DQ489734.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323030.6/ ENSP00000319705.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..320
                     /product="dual oxidase maturation factor 2"
                     /calculated_mol_wt=34656
     Region          10..285
                     /region_name="DuoxA"
                     /note="Dual oxidase maturation factor; pfam10204"
                     /db_xref="CDD:462995"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            84
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            207..227
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HG44.2)"
     Site            248..268
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q1HG44.2)"
     CDS             1..320
                     /gene="DUOXA2"
                     /gene_synonym="SIMNIPHOM; TDH5"
                     /coded_by="NM_207581.4:281..1243"
                     /db_xref="CCDS:CCDS10118.2"
                     /db_xref="GeneID:405753"
                     /db_xref="HGNC:HGNC:32698"
                     /db_xref="MIM:612772"
ORIGIN      
        1 mtlwngvlpf ypqprhaagf svpllivilv flalaasfll ilpgirghsr wfwlvrvlls
       61 lfigaeivav hfsaewfvgt vntntsykaf saarvtarvr llvglegini tltgtpvhql
      121 netidyneqf twrlkenyaa eyanalekgl pdpvlylaek ftpsspcgly hqyhlaghya
      181 satlwvafcf wllsnvllst paplygglal lttgafalfg vfalasissv plcplrlgss
      241 alttqygaaf wvtlatgvlc lflggavvsl qyvrpsalrt lldqsakdcs qerggsplil
      301 gdplhkqaal pdlkcittnl
//
LOCUS       NP_065098                452 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit gamma isoform 1 [Homo
            sapiens].
ACCESSION   NP_065098
VERSION     NP_065098.1
DBSOURCE    REFSEQ: accession NM_020365.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Lee,Y.R., Kim,S.H., Ben-Mahmoud,A., Kim,O.H., Choi,T.I., Lee,K.H.,
            Ku,B., Eum,J., Kee,Y., Lee,S., Cha,J., Won,D., Lee,S.T., Choi,J.R.,
            Lee,J.S., Kim,H.D., Kim,H.G., Bonkowsky,J.L., Kang,H.C. and
            Kim,C.H.
  TITLE     Eif2b3 mutants recapitulate phenotypes of vanishing white matter
            disease and validate novel disease alleles in zebrafish
  JOURNAL   Hum Mol Genet 30 (5), 331-342 (2021)
   PUBMED   33517449
  REMARK    GeneRIF: Eif2b3 mutants recapitulate phenotypes of vanishing white
            matter disease and validate novel disease alleles in zebrafish.
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Zyryanova,A.F., Weis,F., Faille,A., Alard,A.A.,
            Crespillo-Casado,A., Sekine,Y., Harding,H.P., Allen,F., Parts,L.,
            Fromont,C., Fischer,P.M., Warren,A.J. and Ron,D.
  TITLE     Binding of ISRIB reveals a regulatory site in the nucleotide
            exchange factor eIF2B
  JOURNAL   Science 359 (6383), 1533-1536 (2018)
   PUBMED   29599245
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Tsai,J.C., Miller-Vedam,L.E., Anand,A.A., Jaishankar,P.,
            Nguyen,H.C., Renslo,A.R., Frost,A. and Walter,P.
  TITLE     Structure of the nucleotide exchange factor eIF2B reveals mechanism
            of memory-enhancing molecule
  JOURNAL   Science 359 (6383) (2018)
   PUBMED   29599213
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Kruger,M., Beger,C., Li,Q.X., Welch,P.J., Tritz,R., Leavitt,M.,
            Barber,J.R. and Wong-Staal,F.
  TITLE     Identification of eIF2Bgamma and eIF2gamma as cofactors of
            hepatitis C virus internal ribosome entry site-mediated translation
            using a functional genomics approach
  JOURNAL   Proc Natl Acad Sci U S A 97 (15), 8566-8571 (2000)
   PUBMED   10900014
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Anthony,T.G., Fabian,J.R., Kimball,S.R. and Jefferson,L.S.
  TITLE     Identification of domains within the epsilon-subunit of the
            translation initiation factor eIF2B that are necessary for guanine
            nucleotide exchange activity and eIF2B holoprotein formation
  JOURNAL   Biochim Biophys Acta 1492 (1), 56-62 (2000)
   PUBMED   10858531
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Gomez,E. and Pavitt,G.D.
  TITLE     Identification of domains and residues within the epsilon subunit
            of eukaryotic translation initiation factor 2B (eIF2Bepsilon)
            required for guanine nucleotide exchange reveals a novel activation
            function promoted by eIF2B complex formation
  JOURNAL   Mol Cell Biol 20 (11), 3965-3976 (2000)
   PUBMED   10805739
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 452)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from DA162797.1, AK024006.1, AK022399.1, BC018728.1,
            BF879213.1 and W21485.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is one of the subunits of
            initiation factor eIF2B, which catalyzes the exchange of eukaryotic
            initiation factor 2-bound GDP for GTP. It has also been found to
            function as a cofactor of hepatitis C virus internal ribosome entry
            site-mediated translation. Mutations in this gene have been
            associated with leukodystrophy with vanishing white matter.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314668.1, AK024006.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360403.7/ ENSP00000353575.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..452
                     /product="translation initiation factor eIF2B subunit
                     gamma isoform 1"
                     /note="translation initiation factor eIF-2B subunit gamma;
                     eIF-2B GDP-GTP exchange factor subunit gamma; eukaryotic
                     translation initiation factor 2B, subunit 3 gamma, 58kDa;
                     eIF2B GDP-GTP exchange factor subunit gamma; translation
                     initiation factor eIF2B subunit gamma"
                     /calculated_mol_wt=50109
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9NR50.1)"
     Region          3..212
                     /region_name="eIF-2B_gamma_N"
                     /note="The N-terminal domain of gamma subunit of the
                     eIF-2B is a subfamily of glycosyltransferase 2; cd04198"
                     /db_xref="CDD:133041"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NR50.1)"
     Region          357..437
                     /region_name="LbH_eIF2B_gamma_C"
                     /note="eIF-2B gamma subunit, C-terminal Left-handed
                     parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic
                     translation initiator, a guanine nucleotide exchange
                     factor (GEF) composed of five different subunits (alpha,
                     beta, gamma, delta and epsilon). eIF2B is...; cd04652"
                     /db_xref="CDD:100057"
     CDS             1..452
                     /gene="EIF2B3"
                     /gene_synonym="EIF-2B; EIF2Bgamma; VWM3"
                     /coded_by="NM_020365.5:113..1471"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS517.1"
                     /db_xref="GeneID:8891"
                     /db_xref="HGNC:HGNC:3259"
                     /db_xref="MIM:606273"
ORIGIN      
        1 mefqavvmav gggsrmtdlt ssipkpllpv gnkpliwypl nllervgfee vivvttrdvq
       61 kalcaefkmk mkpdivcipd dadmgtadsl ryiypklktd vlvlscdlit dvalhevvdl
      121 fraydaslam lmrkgqdsie pvpgqkgkkk aveqrdfigv dstgkrllfm aneadldeel
      181 vikgsilqkh prirfhtglv dahlyclkky ivdflmengs itsirselip ylvrkqfssa
      241 ssqqgqeeke edlkkkelks ldiysfikea ntlnlapyda cwnacrgdrw edlsrsqvrc
      301 yvhimkeglc srvstlglym eanrqvpkll salcpeeppv hssaqivskh lvgvdsligp
      361 etqigekssi krsvigsscl ikdrvtitnc llmnsvtvee gsniqgsvic nnaviekgad
      421 ikdcligsgq rieakakrvn evivgndqlm ei
//
LOCUS       NP_001305323             514 aa            linear   PRI 20-NOV-2025
DEFINITION  plasma kallikrein isoform 2 [Homo sapiens].
ACCESSION   NP_001305323
VERSION     NP_001305323.1
DBSOURCE    REFSEQ: accession NM_001318394.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Longhurst,H.J., Lindsay,K., Petersen,R.S., Fijen,L.M., Gurugama,P.,
            Maag,D., Butler,J.S., Shah,M.Y., Golden,A., Xu,Y., Boiselle,C.,
            Vogel,J.D., Abdelhady,A.M., Maitland,M.L., McKee,M.D., Seitzer,J.,
            Han,B.W., Soukamneuth,S., Leonard,J., Sepp-Lorenzino,L.,
            Clark,E.D., Lebwohl,D. and Cohn,D.M.
  TITLE     CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary Angioedema
  JOURNAL   N Engl J Med 390 (5), 432-441 (2024)
   PUBMED   38294975
  REMARK    GeneRIF: CRISPR-Cas9 In Vivo Gene Editing of KLKB1 for Hereditary
            Angioedema.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Schachtl-Riess,J.F., Schonherr,S., Lamina,C., Forer,L., Coassin,S.,
            Streiter,G., Kheirkhah,A., Li,Y., Meiselbach,H., Di Maio,S.,
            Eckardt,K.U., Kottgen,A. and Kronenberg,F.
  CONSRTM   GCKD investigators
  TITLE     KLKB1 and CLSTN2 are associated with HDL-mediated cholesterol
            efflux capacity in a genome-wide association study
  JOURNAL   Atherosclerosis 368, 1-11 (2023)
   PUBMED   36812656
  REMARK    GeneRIF: KLKB1 and CLSTN2 are associated with HDL-mediated
            cholesterol efflux capacity in a genome-wide association study.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Feng,L., Liu,Y., Chen,M. and Hu,Y.
  TITLE     [Matrix metalloproteinase 14 and plasma kallikrein 1 may be
            potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis]
  JOURNAL   Zhonghua Wei Zhong Bing Ji Jiu Yi Xue 34 (7), 676-681 (2022)
   PUBMED   36100402
  REMARK    GeneRIF: [Matrix metalloproteinase 14 and plasma kallikrein 1 may
            be potential biomarkers in the diagnosis and treatment of sepsis: a
            proteomics and bioinformatics analysis].
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Wan,J., Vadaq,N., Konings,J., Jaeger,M., Kumar,V., de Laat,B.,
            Joosten,L., Netea,M.G., van der Ven,A.J., de Groot,P.G., de Mast,Q.
            and Roest,M.
  TITLE     Kallikrein augments the anticoagulant function of the protein C
            system in thrombin generation
  JOURNAL   J Thromb Haemost 20 (1), 48-57 (2022)
   PUBMED   34532976
  REMARK    GeneRIF: Kallikrein augments the anticoagulant function of the
            protein C system in thrombin generation.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Beaubien,G., Rosinski-Chupin,I., Mattei,M.G., Mbikay,M.,
            Chretien,M. and Seidah,N.G.
  TITLE     Gene structure and chromosomal localization of plasma kallikrein
  JOURNAL   Biochemistry 30 (6), 1628-1635 (1991)
   PUBMED   1993180
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Chung,D.W., Fujikawa,K., McMullen,B.A. and Davie,E.W.
  TITLE     Human plasma prekallikrein, a zymogen to a serine protease that
            contains four tandem repeats
  JOURNAL   Biochemistry 25 (9), 2410-2417 (1986)
   PUBMED   3521732
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Thompson,R.E., Mandle,R. Jr. and Kaplan,A.P.
  TITLE     Studies of binding of prekallikrein and Factor XI to high molecular
            weight kininogen and its light chain
  JOURNAL   Proc Natl Acad Sci U S A 76 (10), 4862-4866 (1979)
   PUBMED   291905
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Mandle,R.J. Jr. and Kaplan,A.P.
  TITLE     Hageman-factor-dependent fibrinolysis: generation of fibrinolytic
            activity by the interaction of human activated factor XI and
            plasminogen
  JOURNAL   Blood 54 (4), 850-862 (1979)
   PUBMED   89876
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Aznar,J.A., Espana,F., Aznar,J., Tascon,A. and Jimenez,C.
  TITLE     Fletcher factor deficiency: report of a new family
  JOURNAL   Scand J Haematol 21 (2), 94-98 (1978)
   PUBMED   694428
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Meier,H.L., Pierce,J.V., Colman,R.W. and Kaplan,A.P.
  TITLE     Activation and function of human Hageman factor. The role of high
            molecular weight kininogen and prekallikrein
  JOURNAL   J Clin Invest 60 (1), 18-31 (1977)
   PUBMED   874082
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292624.1, AK297672.1,
            AC110771.3 and AW182528.1.
            
            Summary: This gene encodes a glycoprotein that participates in the
            surface-dependent activation of blood coagulation, fibrinolysis,
            kinin generation and inflammation. The encoded preproprotein
            present in plasma as a non-covalent complex with high molecular
            weight kininogen undergoes proteolytic processing mediated by
            activated coagulation factor XII to generate a disulfide-linked,
            heterodimeric serine protease comprised of heavy and light chains.
            Certain mutations in this gene cause prekallikrein deficiency.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) has multiple differences,
            compared to variant 1. These differences result in a distinct 5'
            UTR and cause translation initiation at a downstream start codon,
            compared to variant 1. The encoded protein (isoform 2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297672.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465408, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.2"
     Protein         1..514
                     /product="plasma kallikrein isoform 2"
                     /EC_number="3.4.21.34"
                     /note="kallikrein B, plasma (Fletcher factor) 1;
                     kininogenin; plasma prekallikrein; plasma kallikrein"
                     /calculated_mol_wt=57512
     Region          <1..66
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Region          73..156
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(89,91,102)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          163..246
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(179,181,192)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          254..337
                     /region_name="APPLE"
                     /note="APPLE domain; smart00223"
                     /db_xref="CDD:128519"
     Site            order(270,272,283)
                     /site_type="active"
                     /note="putative binding site [active]"
                     /db_xref="CDD:238533"
     Region          353..>500
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            353
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     CDS             1..514
                     /gene="KLKB1"
                     /gene_synonym="KLK3; PKK; PKKD; PPK"
                     /coded_by="NM_001318394.2:266..1810"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82982.1"
                     /db_xref="GeneID:3818"
                     /db_xref="HGNC:HGNC:6371"
                     /db_xref="MIM:229000"
ORIGIN      
        1 mytpnaqycq mrctfhprcl lfsflpassi ndmekrfgcf lkdsvtgtlp kvhrtgavsg
       61 hslkqcghqi sachrdiykg vdmrgvnfnv skvssveecq krctsnircq ffsyatqtfh
      121 kaeyrnncll kyspggtpta ikvlsnvesg fslkpcalse igchmnifqh lafsdvdvar
      181 vltpdafvcr tictyhpncl fftfytnvwk iesqrnvcll ktsesgtpss stpqentisg
      241 yslltckrtl pepchskiyp gvdfggeeln vtfvkgvnvc qetctkmirc qfftysllpe
      301 dckeekckcf lrlsmdgspt riaygtqgss gyslrlcntg dnsvcttkts trivggtnss
      361 wgewpwqvsl qvkltaqrhl cggslighqw vltaahcfdg lplqdvwriy sgilnlsdit
      421 kdtpfsqike iiihqnykvs egnhdialik lqaplnytef qkpiclpskg dtstiytncw
      481 vtgwgfskek grfrwslslq tqwnvafggh hqlg
//
LOCUS       NP_001271455             345 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 3 [Homo sapiens].
ACCESSION   NP_001271455 XP_005256910
VERSION     NP_001271455.1
DBSOURCE    REFSEQ: accession NM_001284526.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 345)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 345)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 345)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 345)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 345)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 345)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 345)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 345)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 345)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 345)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC013300.2 and BC009751.2.
            
            On Oct 2, 2013 this sequence version replaced XP_005256910.1.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            acceptor splice site in the mid-coding region compared to variant
            1. The resulting isoform (3) is one amino acid longer than isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013300.2, SRR1163655.397278.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..345
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..345
                     /product="aurora kinase B isoform 3"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=39336
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Region          71..340
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(84..87,90,92,105,107,139,155..158,201,205..206,208,
                     218..219)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:26829474; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14722118,
                     ECO:0000269|PubMed:26829474; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     CDS             1..345
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_001284526.2:72..1109"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS67162.1"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 maqkensypw pygrqtapsg lstlpqrvlr kepvtpsalv lmsrsnvqpt aapgqkvmen
       61 ssgtpdiltr rhftiddfei grplgkgkfg nvylarekks hfivalkvlf ksqiekegve
      121 hqlrreieiq ahlhhpnilr lynyfydrrr iylileyapr gelykelqks ctfdeqrtat
      181 imeeladalm ychgkkvihr dikpenlllg lkgelkiadf gwsvhapslr rktmcgtldy
      241 lppemiegrm hnekvdlwci gvlcyellvg nppfesashn etyrrivkvd lkfpasvpmg
      301 aqdliskllr hnpserlpla qvsahpwvra nsrrvlppsa lqsva
//
LOCUS       NP_001349908             137 aa            linear   PRI 20-NOV-2025
DEFINITION  golgin subfamily A member 7 isoform a [Homo sapiens].
ACCESSION   NP_001349908 XP_024302942
VERSION     NP_001349908.1
DBSOURCE    REFSEQ: accession NM_001362979.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 137)
  AUTHORS   Yang,A., Liu,S., Zhang,Y., Chen,J., Fan,Y., Wang,F., Zou,Y.,
            Feng,S., Wu,J. and Hu,Q.
  TITLE     Regulation of RAS palmitoyltransferases by accessory proteins and
            palmitoylation
  JOURNAL   Nat Struct Mol Biol 31 (3), 436-446 (2024)
   PUBMED   38182928
REFERENCE   2  (residues 1 to 137)
  AUTHORS   Zeng,X.T., Yu,X.X. and Cheng,W.
  TITLE     Correction to: The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2
            spike (S) protein and their effects on S protein's subcellular
            localization, palmitoylation and pseudovirus entry
  JOURNAL   Virol J 19 (1), 25 (2022)
   PUBMED   35115020
  REMARK    Correction to:[Virol J. 2021 Dec 27;18(1):257. doi:
            10.1186/s12985-021-01722-w. PMID: 34961524]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 137)
  AUTHORS   Zeng,X.T., Yu,X.X. and Cheng,W.
  TITLE     The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2 spike (S) protein
            and their effects on S protein's subcellular localization,
            palmitoylation and pseudovirus entry
  JOURNAL   Virol J 18 (1), 257 (2021)
   PUBMED   34961524
  REMARK    GeneRIF: The interactions of ZDHHC5/GOLGA7 with SARS-CoV-2 spike
            (S) protein and their effects on S protein's subcellular
            localization, palmitoylation and pseudovirus entry.
            Erratum:[Virol J. 2022 Feb 3;19(1):25. doi:
            10.1186/s12985-022-01750-0. PMID: 35115020]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 137)
  AUTHORS   Wu,Z., Zhang,Z., Wang,X., Zhang,J., Ren,C., Li,Y., Gao,L.,
            Liang,X., Wang,P. and Ma,C.
  TITLE     Palmitoylation of SARS-CoV-2 S protein is essential for viral
            infectivity
  JOURNAL   Signal Transduct Target Ther 6 (1), 231 (2021)
   PUBMED   34117209
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 137)
  AUTHORS   Stukalov,A., Girault,V., Grass,V., Karayel,O., Bergant,V.,
            Urban,C., Haas,D.A., Huang,Y., Oubraham,L., Wang,A., Hamad,M.S.,
            Piras,A., Hansen,F.M., Tanzer,M.C., Paron,I., Zinzula,L.,
            Engleitner,T., Reinecke,M., Lavacca,T.M., Ehmann,R., Wolfel,R.,
            Jores,J., Kuster,B., Protzer,U., Rad,R., Ziebuhr,J., Thiel,V.,
            Scaturro,P., Mann,M. and Pichlmair,A.
  TITLE     Multilevel proteomics reveals host perturbations by SARS-CoV-2 and
            SARS-CoV
  JOURNAL   Nature 594 (7862), 246-252 (2021)
   PUBMED   33845483
REFERENCE   6  (residues 1 to 137)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 137)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 137)
  AUTHORS   Swarthout,J.T., Lobo,S., Farh,L., Croke,M.R., Greentree,W.K.,
            Deschenes,R.J. and Linder,M.E.
  TITLE     DHHC9 and GCP16 constitute a human protein fatty acyltransferase
            with specificity for H- and N-Ras
  JOURNAL   J Biol Chem 280 (35), 31141-31148 (2005)
   PUBMED   16000296
  REMARK    GeneRIF: Data show that H- and N-Ras are palmitoylated by a human
            protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes.
REFERENCE   9  (residues 1 to 137)
  AUTHORS   Ohta,E., Misumi,Y., Sohda,M., Fujiwara,T., Yano,A. and Ikehara,Y.
  TITLE     Identification and characterization of GCP16, a novel acylated
            Golgi protein that interacts with GCP170
  JOURNAL   J Biol Chem 278 (51), 51957-51967 (2003)
   PUBMED   14522980
  REMARK    GeneRIF: results indicate that GCP16 is the acylated membrane
            protein, associated with GCP170, and possibly involved in vesicular
            transport from the Golgi to the cell surface
REFERENCE   10 (residues 1 to 137)
  AUTHORS   Jia,L., Young,M.F., Powell,J., Yang,L., Ho,N.C., Hotchkiss,R.,
            Robey,P.G. and Francomano,C.A.
  TITLE     Gene expression profile of human bone marrow stromal cells:
            high-throughput expressed sequence tag sequencing analysis
  JOURNAL   Genomics 79 (1), 7-17 (2002)
   PUBMED   11827452
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI546026.1, BC001227.2, AF068291.1, AV650886.1, AF125102.1 and
            BG939345.1.
            
            On May 4, 2018 this sequence version replaced XP_024302942.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.22583.1,
                                           SRR1660807.220545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..137
                     /product="golgin subfamily A member 7 isoform a"
                     /note="Golgi complex-associated protein of 16kDa; golgi
                     autoantigen, golgin subfamily a, 7; golgin subfamily A
                     member 7; golgi complex-associated protein of 16 kDa"
                     /calculated_mol_wt=15693
     Region          11..124
                     /region_name="Erf4"
                     /note="Golgin subfamily A member 7/ERF4 family; pfam10256"
                     /db_xref="CDD:463029"
     CDS             1..137
                     /gene="GOLGA7"
                     /gene_synonym="GCP16; GOLGA3AP1; GOLGA7A; HSPC041"
                     /coded_by="NM_001362979.1:194..607"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS34887.1"
                     /db_xref="GeneID:51125"
                     /db_xref="HGNC:HGNC:24876"
                     /db_xref="MIM:609453"
ORIGIN      
        1 mrpqqapvsg kvfiqrdyss gtrcqfqtkf paelenridr qqfeetvrtl nnlyaeaekl
       61 ggqsylegcl acltaytifl cmethyekvl kkvskyiqeq nekiyapqgl lltdpiergl
      121 rvieitiyed rgmssgr
//
LOCUS       NP_004260                311 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 27 isoform 1
            [Homo sapiens].
ACCESSION   NP_004260
VERSION     NP_004260.2
DBSOURCE    REFSEQ: accession NM_004269.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Maroofian,R., Kaiyrzhanov,R., Cali,E., Zamani,M., Zaki,M.S.,
            Ferla,M., Tortora,D., Sadeghian,S., Saadi,S.M., Abdullah,U.,
            Karimiani,E.G., Efthymiou,S., Yesil,G., Alavi,S., Al Shamsi,A.M.,
            Tajsharghi,H., Abdel-Hamid,M.S., Saadi,N.W., Al Mutairi,F.,
            Alabdi,L., Beetz,C., Ali,Z., Toosi,M.B., Rudnik-Schoneborn,S.,
            Babaei,M., Isohanni,P., Muhammad,J., Khan,S., Al Shalan,M.,
            Hickey,S.E., Marom,D., Elhanan,E., Kurian,M.A., Marafi,D.,
            Saberi,A., Hamid,M., Spaull,R., Meng,L., Lalani,S., Maqbool,S.,
            Rahman,F., Seeger,J., Palculict,T.B., Lau,T., Murphy,D.,
            Mencacci,N.E., Steindl,K., Begemann,A., Rauch,A., Akbas,S.,
            Aslanger,A.D., Salpietro,V., Yousaf,H., Ben-Shachar,S., Ejeskar,K.,
            Al Aqeel,A.I., High,F.A., Armstrong-Javors,A.E., Zahraei,S.M.,
            Seifi,T., Zeighami,J., Shariati,G., Sedaghat,A., Asl,S.N.,
            Shahrooei,M., Zifarelli,G., Burglen,L., Ravelli,C., Zschocke,J.,
            Schatz,U.A., Ghavideldarestani,M., Kamel,W.A., Van Esch,H.,
            Hackenberg,A., Taylor,J.C., Al-Gazali,L., Bauer,P., Gleeson,J.J.,
            Alkuraya,F.S., Lupski,J.R., Galehdari,H., Azizimalamiri,R.,
            Chung,W.K., Baig,S.M., Houlden,H. and Severino,M.
  TITLE     Biallelic MED27 variants lead to variable ponto-cerebello-lental
            degeneration with movement disorders
  JOURNAL   Brain 146 (12), 5031-5043 (2023)
   PUBMED   37517035
  REMARK    GeneRIF: Biallelic MED27 variants lead to variable
            ponto-cerebello-lental degeneration with movement disorders.
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Wang,R., Yu,W., Zhu,T., Lin,F., Hua,C., Ru,L., Guo,P., Wan,X.,
            Xue,G., Guo,Z., Han,S., Lv,K., Zhang,G., Ge,H., Guo,W., Xu,L. and
            Deng,W.
  TITLE     MED27 plays a tumor-promoting role in breast cancer progression by
            targeting KLF4
  JOURNAL   Cancer Sci 114 (6), 2277-2292 (2023)
   PUBMED   36786527
  REMARK    GeneRIF: MED27 plays a tumor-promoting role in breast cancer
            progression by targeting KLF4.
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Han,X., Liu,H., Tang,X. and Zhao,Y.
  TITLE     Knockdown of mediator complex subunit 27 suppresses gastric cancer
            cell metastasis and angiogenesis via Wnt/beta-catenin pathway
  JOURNAL   Tissue Cell 79, 101973 (2022)
   PUBMED   36371844
  REMARK    GeneRIF: Knockdown of mediator complex subunit 27 suppresses
            gastric cancer cell metastasis and angiogenesis via
            Wnt/beta-catenin pathway.
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Malik,S., Gu,W., Wu,W., Qin,J. and Roeder,R.G.
  TITLE     The USA-derived transcriptional coactivator PC2 is a submodule of
            TRAP/SMCC and acts synergistically with other PCs
  JOURNAL   Mol Cell 5 (4), 753-760 (2000)
   PUBMED   10882111
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Ryu,S., Zhou,S., Ladurner,A.G. and Tjian,R.
  TITLE     The transcriptional cofactor complex CRSP is required for activity
            of the enhancer-binding protein Sp1
  JOURNAL   Nature 397 (6718), 446-450 (1999)
   PUBMED   9989412
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Gress,T.M., Muller-Pillasch,F., Geng,M., Zimmerhackl,F.,
            Zehetner,G., Friess,H., Buchler,M., Adler,G. and Lehrach,H.
  TITLE     A pancreatic cancer-specific expression profile
  JOURNAL   Oncogene 13 (8), 1819-1830 (1996)
   PUBMED   8895530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP255072.1 and BC064608.1.
            
            On Feb 25, 2003 this sequence version replaced NP_004260.1.
            
            Summary: The activation of gene transcription is a multistep
            process that is triggered by factors that recognize transcriptional
            enhancer sites in DNA. These factors work with co-activators to
            direct transcriptional initiation by the RNA polymerase II
            apparatus. The protein encoded by this gene is a subunit of the
            CRSP (cofactor required for SP1 activation) complex, which, along
            with TFIID, is required for efficient activation by SP1. This
            protein is also a component of other multisubunit complexes e.g.
            thyroid hormone receptor-(TR-) associated proteins which interact
            with TR and facilitate TR function on DNA templates in conjunction
            with initiation factors and cofactors. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene, and a pseudogene of this gene is located on the long
            arm of chromosome 5. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064608.1, SRR11853565.29448.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292035.10/ ENSP00000292035.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..311
                     /product="mediator of RNA polymerase II transcription
                     subunit 27 isoform 1"
                     /note="cofactor required for Sp1 transcriptional
                     activation, subunit 8, 34kDa; p37 TRAP/SMCC/PC2 subunit;
                     mediator of RNA polymerase II transcription subunit 27;
                     CRSP complex subunit 8; transcriptional coactivator
                     CRSP34; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=35301
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2C8.1)"
     Site            134
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6P2C8.1)"
     Region          228..309
                     /region_name="Med27"
                     /note="Mediator complex subunit 27; pfam11571"
                     /db_xref="CDD:463298"
     CDS             1..311
                     /gene="MED27"
                     /gene_synonym="CRAP34; CRSP34; CRSP8; MED3; NEDSCAC;
                     TRAP37"
                     /coded_by="NM_004269.4:24..959"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6945.1"
                     /db_xref="GeneID:9442"
                     /db_xref="HGNC:HGNC:2377"
                     /db_xref="MIM:605044"
ORIGIN      
        1 madvinvsvn leafsqaisa iqalrssvsr vfdclkdgmr nketlegrek afiahfqdnl
       61 hsvnrdlnel erlsnlvgkp senhplhnsg llsldpvqdk tplysqllqa ykwsnklqyh
      121 aglasgllnq qslkrsanqm gvsakrrpka qpttlvlppq yvddvisrid rmfpemsihl
      181 srpngtsaml lvtlgkvlkv ivvmrslfid rtivkgynen vytedgkldi wsksnyqvfq
      241 kvtdhattal lhyqlpqmpd vvvrsfmtwl rsyiklfqap cqrcgkflqd glpptwrdfr
      301 tleafhdtcr q
//
LOCUS       NP_001305874             310 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26A isoform 4 [Homo
            sapiens].
ACCESSION   NP_001305874
VERSION     NP_001305874.1
DBSOURCE    REFSEQ: accession NM_001318945.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Hou,J., Wu,H., Xu,B., Shang,J., Xu,X., Li,G., Zhang,H., Zhang,W.,
            Deng,Y., Hong,X., Hu,T., Zhang,M. and Zhan,Y.
  TITLE     The Prognostic Value and the Oncogenic and Immunological Roles of
            Vacuolar Protein Sorting Associated Protein 26 A in Pancreatic
            Adenocarcinoma
  JOURNAL   Int J Mol Sci 24 (4), 3486 (2023)
   PUBMED   36834898
  REMARK    GeneRIF: The Prognostic Value and the Oncogenic and Immunological
            Roles of Vacuolar Protein Sorting Associated Protein 26 A in
            Pancreatic Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Arighi,C.N., Hartnell,L.M., Aguilar,R.C., Haft,C.R. and
            Bonifacino,J.S.
  TITLE     Role of the mammalian retromer in sorting of the cation-independent
            mannose 6-phosphate receptor
  JOURNAL   J Cell Biol 165 (1), 123-133 (2004)
   PUBMED   15078903
REFERENCE   7  (residues 1 to 310)
  AUTHORS   Seaman,M.N.
  TITLE     Cargo-selective endosomal sorting for retrieval to the Golgi
            requires retromer
  JOURNAL   J Cell Biol 165 (1), 111-122 (2004)
   PUBMED   15078902
REFERENCE   8  (residues 1 to 310)
  AUTHORS   Reddy,J.V. and Seaman,M.N.
  TITLE     Vps26p, a component of retromer, directs the interactions of Vps35p
            in endosome-to-Golgi retrieval
  JOURNAL   Mol Biol Cell 12 (10), 3242-3256 (2001)
   PUBMED   11598206
REFERENCE   9  (residues 1 to 310)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   10 (residues 1 to 310)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA498726.1, AK297142.1,
            BX647725.1 and AL596223.3.
            
            Summary: This gene belongs to a group of vacuolar protein sorting
            (VPS) genes. The encoded protein is a component of a large
            multimeric complex, termed the retromer complex, involved in
            retrograde transport of proteins from endosomes to the trans-Golgi
            network. The close structural similarity between the yeast and
            human proteins that make up this complex suggests a similarity in
            function. Expression studies in yeast and mammalian cells indicate
            that this protein interacts directly with VPS35, which serves as
            the core of the retromer complex. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) includes an additional exon in
            the 5' region, and it thus differs in its 5' UTR and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (4) has a shorter and distinct N-terminus, compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297142.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142363,
                                           SAMEA2142853 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..310
                     /product="vacuolar protein sorting-associated protein 26A
                     isoform 4"
                     /note="vacuolar protein sorting-associated protein 26A;
                     vesicle protein sorting 26A; vacuolar protein sorting 26
                     homolog A; VPS26 retromer complex comonent A"
                     /calculated_mol_wt=36456
     Region          34..266
                     /region_name="Vps26"
                     /note="Vacuolar protein sorting-associated protein 26;
                     pfam03643"
                     /db_xref="CDD:397622"
     CDS             1..310
                     /gene="VPS26A"
                     /gene_synonym="HB58; Hbeta58; PEP8A; VPS26"
                     /coded_by="NM_001318945.2:228..1160"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:9559"
                     /db_xref="HGNC:HGNC:12711"
                     /db_xref="MIM:605506"
ORIGIN      
        1 mtenpfqery svedlstfgm clcmvryvyd afykvnlafk qpgkrlehqg iriefvgqie
       61 lfndksnthe fvnlvkelal pgeltqsrsy dfefmqvekp yesyiganvr lryflkvtiv
      121 rrltdlvkey dlivhqlaty pdvnnsikme vgiedclhie feynkskyhl kdvivgkiyf
      181 llvrikiqhm elqlikkeit gigpstttet etiakyeimd gapvkgesip irlflagydp
      241 tptmrdvnkk fsvryflnlv lvdeedrryf kqqeiilwrk apeklrkqrt nfhqrfespe
      301 sqasaeqpem
//
LOCUS       NP_689986                142 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein light chain Tctex-type protein 2B isoform 2 [Homo sapiens].
ACCESSION   NP_689986 XP_941477
VERSION     NP_689986.2
DBSOURCE    REFSEQ: accession NM_152773.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Vuolo,L., Stevenson,N.L., Mukhopadhyay,A.G., Roberts,A.J. and
            Stephens,D.J.
  TITLE     Cytoplasmic dynein-2 at a glance
  JOURNAL   J Cell Sci 133 (6) (2020)
   PUBMED   32229580
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Schmidts,M., Hou,Y., Cortes,C.R., Mans,D.A., Huber,C., Boldt,K.,
            Patel,M., van Reeuwijk,J., Plaza,J.M., van Beersum,S.E., Yap,Z.M.,
            Letteboer,S.J., Taylor,S.P., Herridge,W., Johnson,C.A.,
            Scambler,P.J., Ueffing,M., Kayserili,H., Krakow,D., King,S.M.,
            Beales,P.L., Al-Gazali,L., Wicking,C., Cormier-Daire,V.,
            Roepman,R., Mitchison,H.M. and Witman,G.B.
  CONSRTM   UK10K
  TITLE     TCTEX1D2 mutations underlie Jeune asphyxiating thoracic dystrophy
            with impaired retrograde intraflagellar transport
  JOURNAL   Nat Commun 6, 7074 (2015)
   PUBMED   26044572
  REMARK    GeneRIF: integral component of the evolutionarily conserved
            retrograde intraflagellar transport machinery
            Erratum:[Nat Commun. 2016 Mar 29;7:11270. doi: 10.1038/ncomms11270.
            PMID: 27021811]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Gholkar,A.A., Senese,S., Lo,Y.C., Capri,J., Deardorff,W.J.,
            Dharmarajan,H., Contreras,E., Hodara,E., Whitelegge,J.P.,
            Jackson,P.K. and Torres,J.Z.
  TITLE     Tctex1d2 associates with short-rib polydactyly syndrome proteins
            and is required for ciliogenesis
  JOURNAL   Cell Cycle 14 (7), 1116-1125 (2015)
   PUBMED   25830415
  REMARK    GeneRIF: Tctex1d2 is a novel dynein light chain important for
            trafficking to the cilium and potentially retrograde intraflagellar
            transport.
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Asante,D., Stevenson,N.L. and Stephens,D.J.
  TITLE     Subunit composition of the human cytoplasmic dynein-2 complex
  JOURNAL   J Cell Sci 127 (Pt 21), 4774-4787 (2014)
   PUBMED   25205765
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC021177.2, BM548106.1 and
            BM983853.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 1, 2009 this sequence version replaced NP_689986.1.
            
            Summary: Dyneins are a group of microtubule-activated ATPases that
            function as molecular motors. They are divided into two subgroups
            of axonemal and cytoplasmic dyneins. The cytoplasmic dyneins
            function in intracellular motility, including retrograde axonal
            transport, protein sorting, organelle movement, and spindle
            dynamics. Molecules of conventional cytoplasmic dynein are
            comprised of 2 heavy chain polypeptides and a number of
            intermediate and light chains. This gene encodes a subunit of the
            human cytoplasmic dynein-2 complex. Mutations in this gene are
            associated with short-rib thoracic dysplasia 17 with or without
            polydactyly. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, May 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.542246.1,
                                           SRR1163657.100823.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325318.10/ ENSP00000324323.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..142
                     /product="dynein light chain Tctex-type protein 2B isoform
                     2"
                     /note="tctex1 domain-containing protein 2; Tctex1 domain
                     containing 2; dynein light chain Tctex-type protein 2B"
                     /calculated_mol_wt=15991
     Region          38..141
                     /region_name="DLC-like_TCTEX1D2"
                     /note="dynein light chain (DLC)-like domain found in
                     Tctex1 domain-containing protein 2 (TCTEX1D2) and similar
                     proteins; cd21459"
                     /db_xref="CDD:412007"
     CDS             1..142
                     /gene="DYNLT2B"
                     /gene_synonym="SRTD17; TCTEX1D2"
                     /coded_by="NM_152773.5:89..517"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33929.1"
                     /db_xref="GeneID:255758"
                     /db_xref="HGNC:HGNC:28482"
                     /db_xref="MIM:617353"
ORIGIN      
        1 matsigvsfs vgdgvpeaek nagepentyi lrpvfqqrfr psvvkdciha vlkeelanae
       61 yspeempqlt khlsenikdk lkemgfdryk mvvqvvigeq rgegvfmasr cfwdadtdny
      121 thdvfmndsl fcvvaafgcf yy
//
LOCUS       NP_002788                263 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-5 isoform 1 [Homo sapiens].
ACCESSION   NP_002788
VERSION     NP_002788.1
DBSOURCE    REFSEQ: accession NM_002797.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Wang,H., Bai,C., Dang,X. and Wang,H.
  TITLE     MiR-383 sensitizes osteosarcoma cells to bortezomib treatment via
            down-regulating PSMB5
  JOURNAL   Mol Biol Rep 51 (1), 170 (2024)
   PUBMED   38252234
  REMARK    GeneRIF: MiR-383 sensitizes osteosarcoma cells to bortezomib
            treatment via down-regulating PSMB5.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Liu,J., Mi,J., Liu,S., Chen,H. and Jiang,L.
  TITLE     PSMB5 overexpression is correlated with tumor proliferation and
            poor prognosis in hepatocellular carcinoma
  JOURNAL   FEBS Open Bio 12 (11), 2025-2041 (2022)
   PUBMED   36062301
  REMARK    GeneRIF: PSMB5 overexpression is correlated with tumor
            proliferation and poor prognosis in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 207 (3), 1059 (1995)
   PUBMED   7864893
  REMARK    Correction to:[Biochem Biophys Res Commun. 1994 Dec
            30;205(3):1785-9. doi: 10.1006/bbrc.1994.2876. PMID: 7811265]
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Belich,M.P., Glynne,R.J., Senger,G., Sheer,D. and Trowsdale,J.
  TITLE     Proteasome components with reciprocal expression to that of the
            MHC-encoded LMP proteins
  JOURNAL   Curr Biol 4 (9), 769-776 (1994)
   PUBMED   7820546
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Akiyama,K., Yokota,K., Kagawa,S., Shimbara,N., Tamura,T.,
            Akioka,H., Nothwang,H.G., Noda,C., Tanaka,K. and Ichihara,A.
  TITLE     cDNA cloning and interferon gamma down-regulation of proteasomal
            subunits X and Y
  JOURNAL   Science 265 (5176), 1231-1234 (1994)
   PUBMED   8066462
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Lee,L.W., Moomaw,C.R., Orth,K., McGuire,M.J., DeMartino,G.N. and
            Slaughter,C.A.
  TITLE     Relationships among the subunits of the high molecular weight
            proteinase, macropain (proteasome)
  JOURNAL   Biochim Biophys Acta 1037 (2), 178-185 (1990)
   PUBMED   2306472
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC057840.1 and BC107720.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit in the proteasome. This
            catalytic subunit is not present in the immunoproteasome and is
            replaced by catalytic subunit 3i (proteasome beta 8 subunit).
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.30993.1,
                                           SRR5189661.45886.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361611.11/ ENSP00000355325.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..263
                     /product="proteasome subunit beta type-5 isoform 1"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit MB1; beta-5; PSX large
                     multifunctional protease X; proteasome epsilon chain;
                     macropain epsilon chain; multicatalytic endopeptidase
                     complex epsilon chain; proteasome chain 6; proteasome
                     catalytic subunit 3; proteasome subunit, beta type, 5;
                     proteasome subunit X; proteasome beta 5 subunit;
                     proteasome (prosome, macropain) subunit, beta type, 5;
                     testicular tissue protein Li 153; proteasome subunit beta
                     5"
                     /calculated_mol_wt=28349
     Region          60..247
                     /region_name="proteasome_beta_type_5"
                     /note="proteasome beta type-5 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03761"
                     /db_xref="CDD:239730"
     Site            order(60,76,78,92,189,226,229..230)
                     /site_type="active"
                     /db_xref="CDD:239730"
     Site            order(78,81,83..88,108,110,125,137,140..141,143..144,147,
                     150,174,176,178..181,184,192..193,195..196,199..201,217,
                     224..227,230..231)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239730"
     CDS             1..263
                     /gene="PSMB5"
                     /gene_synonym="LMPX; MB1"
                     /coded_by="NM_002797.5:20..811"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9584.1"
                     /db_xref="GeneID:5693"
                     /db_xref="HGNC:HGNC:9542"
                     /db_xref="MIM:600306"
ORIGIN      
        1 malasvlerp lpvnqrgffg lggradlldl gpgslsdgls laapgwgvpe epgiemlhgt
       61 ttlafkfrhg vivaadsrat agayiasqtv kkvieinpyl lgtmaggaad csfwerllar
      121 qcriyelrnk erisvaaask llanmvyqyk gmglsmgtmi cgwdkrgpgl yyvdsegnri
      181 sgatfsvgsg svyaygvmdr gysydleveq aydlarraiy qatyrdaysg gavnlyhvre
      241 dgwirvssdn vadlhekysg stp
//
LOCUS       NP_277041                580 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 24 isoform 1 [Homo sapiens].
ACCESSION   NP_277041
VERSION     NP_277041.1
DBSOURCE    REFSEQ: accession NM_033506.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Zhang,Z., Liu,X., Chu,C., Zhang,Y., Li,W., Yu,X., Han,Q., Sun,H.,
            Zhang,Y., Zhu,X., Chen,L., Wei,R., Fan,N., Zhou,M. and Li,X.
  TITLE     MIR937 amplification potentiates ovarian cancer progression by
            attenuating FBXO16 inhibition on ULK1-mediated autophagy
  JOURNAL   Cell Death Dis 15 (10), 735 (2024)
   PUBMED   39384743
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 580)
  AUTHORS   El-Mergawy,R., Chafin,L., Ovando-Ricardez,J.A., Rosas,L., Tsai,M.,
            Rojas,M., Mora,A.L. and Mallampalli,R.K.
  TITLE     FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for ubiquitin
            mediated degradation modulates mitochondrial respiration
  JOURNAL   J Biol Chem 300 (6), 107359 (2024)
   PUBMED   38735474
  REMARK    GeneRIF: FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for
            ubiquitin mediated degradation modulates mitochondrial respiration.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Li,Z., Liu,X., Zhang,Y., Li,Y., Zhou,L. and Yuan,S.
  TITLE     FBXO24 modulates mRNA alternative splicing and MIWI degradation and
            is required for normal sperm formation and male fertility
  JOURNAL   Elife 12, 91666 (2024)
   PUBMED   38470475
  REMARK    GeneRIF: FBXO24 modulates mRNA alternative splicing and MIWI
            degradation and is required for normal sperm formation and male
            fertility.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Dong,B., Song,X., Wang,X., Dai,T., Wang,J., Yu,Z., Deng,J.,
            Evers,B.M. and Wu,Y.
  TITLE     FBXO24 Suppresses Breast Cancer Tumorigenesis by Targeting LSD1 for
            Ubiquitination
  JOURNAL   Mol Cancer Res 21 (12), 1303-1316 (2023)
   PUBMED   37540490
  REMARK    GeneRIF: FBXO24 Suppresses Breast Cancer Tumorigenesis by Targeting
            LSD1 for Ubiquitination.
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Chen,W., Xiong,S., Li,J., Li,X., Liu,Y., Zou,C. and
            Mallampalli,R.K.
  TITLE     The ubiquitin E3 ligase SCF-FBXO24 recognizes deacetylated
            nucleoside diphosphate kinase A to enhance its degradation
  JOURNAL   Mol Cell Biol 35 (6), 1001-1013 (2015)
   PUBMED   25582197
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Taipale,M., Krykbaeva,I., Koeva,M., Kayatekin,C., Westover,K.D.,
            Karras,G.I. and Lindquist,S.
  TITLE     Quantitative analysis of HSP90-client interactions reveals
            principles of substrate recognition
  JOURNAL   Cell 150 (5), 987-1001 (2012)
   PUBMED   22939624
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069281.6, BU656991.1 and
            BC067293.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067293.1, AL136811.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241071.11/ ENSP00000241071.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..580
                     /product="F-box only protein 24 isoform 1"
                     /note="F-box protein Fbx24; F-box only protein 24"
                     /calculated_mol_wt=64758
     Region          38..84
                     /region_name="F-box_FBXO24"
                     /note="F-box domain found in F-box only protein 24
                     (FBXO24) and similar proteins; cd22098"
                     /db_xref="CDD:438870"
     Site            order(42,46,49..50,53..54,58,60..61,65..67,69)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438870"
     Region          <363..>425
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          376..425
                     /region_name="RCC1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75426.2)"
     CDS             1..580
                     /gene="FBXO24"
                     /gene_synonym="FBX24"
                     /coded_by="NM_033506.3:299..2041"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5698.1"
                     /db_xref="GeneID:26261"
                     /db_xref="HGNC:HGNC:13595"
                     /db_xref="MIM:609097"
ORIGIN      
        1 mgekavpllr rrrvkrscps cgselgveek rgkgnpisiq lfppelvehi isflpvrdlv
       61 algqtcryfh evcdgegvwr ricrrlsprl qdqgsgvrpw kraailnytk glyfqafggr
      121 rrclsksvap llahgyrrfl ptkdhvfild yvgtlfflkn alvstlgqmq wkracryvvl
      181 crgakdfasd prcdtvyrky lyvlatrepq evvgttssra cdcvevylqs sgqrvfkmtf
      241 hhsmtfkqiv lvgqetqral lllteegkiy slvvnetqld qprsytvqla lrkvshylph
      301 lrvacmtsnq sstlyvtdqg gvyfevhtpg vyrdlfgtlq afdpldqqmp lalslpakil
      361 fcalgynhlg lvdefgrifm qgnnrygqlg tgdkmdrgep tqvcylqrpi tlwcglnhsl
      421 vlsqssefsk ellgcgcgag grlpgwpkgs asfvklqvkv plcacalcat reclyilssh
      481 dieqhapyrh lpasrvvgtp epslgarapq dpggmaqace eylsqihscq tlqdrtekmk
      541 eivgwmplma aqkdffweal dmlqraeggg ggvgppapet
//
LOCUS       NP_057021                578 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase component PIGT isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_057021
VERSION     NP_057021.2
DBSOURCE    REFSEQ: accession NM_015937.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Ben Ayed,I., Jallouli,O., Murakami,Y., Souissi,A., Mallouli,S.,
            Bouzid,A., Kamoun,F., Elloumi,I., Frikha,F., Tlili,A.,
            Weckhuysen,S., Kinoshita,T., Triki,C.C. and Masmoudi,S.
  TITLE     Case report: Functional analysis of the p.Arg507Trp variant of the
            PIGT gene supporting the moderate epilepsy phenotype of mutations
            in the C-terminal region
  JOURNAL   Front Neurol 14, 1092887 (2023)
   PUBMED   36970549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Ohishi,K., Nagamune,K., Maeda,Y. and Kinoshita,T.
  TITLE     Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and
            PIG-T, form a functionally important intermolecular disulfide
            bridge
  JOURNAL   J Biol Chem 278 (16), 13959-13967 (2003)
   PUBMED   12582175
  REMARK    GeneRIF: GPI8 and PIG-T form a functionally important
            intermolecular disulfide bridge
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Vainauskas,S., Maeda,Y., Kurniawan,H., Kinoshita,T. and Menon,A.K.
  TITLE     Structural requirements for the recruitment of Gaa1 into a
            functional glycosylphosphatidylinositol transamidase complex
  JOURNAL   J Biol Chem 277 (34), 30535-30542 (2002)
   PUBMED   12052837
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Ohishi,K., Inoue,N. and Kinoshita,T.
  TITLE     PIG-S and PIG-T, essential for GPI anchor attachment to proteins,
            form a complex with GAA1 and GPI8
  JOURNAL   EMBO J 20 (15), 4088-4098 (2001)
   PUBMED   11483512
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Fossey,S.C., Mychaleckyj,J.C., Pendleton,J.K., Snyder,J.R.,
            Bensen,J.T., Hirakawa,S., Rich,S.S., Freedman,B.I. and Bowden,D.W.
  TITLE     A high-resolution 6.0-megabase transcript map of the type 2
            diabetes susceptibility region on human chromosome 20
  JOURNAL   Genomics 76 (1-3), 45-57 (2001)
   PUBMED   11549316
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC136827.1 and AL121742.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2002 this sequence version replaced NP_057021.1.
            
            Summary: This gene encodes a protein that is involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid found on many blood cells and serves to
            anchor proteins to the cell surface. This protein is an essential
            component of the multisubunit enzyme, GPI transamidase. GPI
            transamidase mediates GPI anchoring in the endoplasmic reticulum,
            by catalyzing the transfer of fully assembled GPI units to
            proteins. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015022.1, SRR3476690.222865.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279036.12/ ENSP00000279036.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..578
                     /product="GPI-anchor transamidase component PIGT isoform 1
                     precursor"
                     /note="neurotrophin-regulated neuronal
                     development-associated protein; GPI transamidase subunit;
                     GPI transamidase component PIG-T; GPI-anchor transamidase
                     component PIGT; phosphatidylinositol-glycan biosynthesis
                     class T protein"
                     /calculated_mol_wt=63607
     sig_peptide     1..21
                     /note="/evidence=ECO:0000269|PubMed:11483512; propagated
                     from UniProtKB/Swiss-Prot (Q969N2.1)"
                     /calculated_mol_wt=2111
     mat_peptide     22..578
                     /product="GPI-anchor transamidase component PIGT.
                     /id=PRO_0000024107"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969N2.1)"
                     /calculated_mol_wt=63607
     Region          32..551
                     /region_name="Gpi16"
                     /note="Gpi16 subunit, GPI transamidase component;
                     pfam04113"
                     /db_xref="CDD:461180"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q969N2.1)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q969N2.1)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:35551457,
                     ECO:0000269|PubMed:37684232, ECO:0007744|PDB:7WLD,
                     ECO:0007744|PDB:8IMX, ECO:0007744|PDB:8IMY; propagated
                     from UniProtKB/Swiss-Prot (Q969N2.1)"
     Site            526..548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969N2.1)"
     CDS             1..578
                     /gene="PIGT"
                     /gene_synonym="CGI-06; MCAHS3; NDAP; PIG-T; PNH2"
                     /coded_by="NM_015937.6:17..1753"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13353.1"
                     /db_xref="GeneID:51604"
                     /db_xref="HGNC:HGNC:14938"
                     /db_xref="MIM:610272"
ORIGIN      
        1 maaamplall vllllgpggw claepprdsl reelvitplp sgdvaatfqf rtrwdselqr
       61 egvshyrlfp kalgqlisky slrelhlsft qgfwrtrywg ppflqapsga elwvwfqdtv
      121 tdvdkswkel snvlsgifca slnfidstnt vtptasfkpl glandtdhyf lryavlprev
      181 vctenltpwk kllpcsskag lsvllkadrl fhtsyhsqav hirpvcrnar ctsiswelrq
      241 tlsvvfdafi tgqgkkdwsl frmfsrtlte pcplasesrv yvdittynqd netlevhppp
      301 tttyqdvilg trktyaiydl ldtaminnsr nlniqlkwkr ppeneappvp flhaqryvsg
      361 yglqkgelst llynthpyra fpvllldtvp wylrlyvhtl titskgkenk psyihyqpaq
      421 drlqphllem liqlpansvt kvsiqferal lkwteytpdp nhgfyvspsv lsalvpsmva
      481 akpvdweesp lfnslfpvsd gsnyfvrlyt epllvnlptp dfsmpynvic ltctvvavcy
      541 gsfynlltrt fhieeprtgg lakrlanlir rargvppl
//
LOCUS       NP_001070818             569 aa            linear   PRI 20-NOV-2025
DEFINITION  GATOR1 complex protein NPRL3 isoform 1 [Homo sapiens].
ACCESSION   NP_001070818
VERSION     NP_001070818.1
DBSOURCE    REFSEQ: accession NM_001077350.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Yang,D., Wang,J., Qin,Z., Feng,J., Mao,C., Chen,Y., Huang,X. and
            Ruan,Y.
  TITLE     Phenotypic and genotypic characterization of NPRL3-related
            epilepsy: Two case reports and literature review
  JOURNAL   Epilepsia Open 9 (1), 33-40 (2024)
   PUBMED   37902097
  REMARK    GeneRIF: Phenotypic and genotypic characterization of NPRL3-related
            epilepsy: Two case reports and literature review.
            Review article
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Dainelli,A., Iacomino,M., Rossato,S., Bugin,S., Traverso,M.,
            Severino,M., Gustincich,S., Capra,V., Di Duca,M., Zara,F., Scala,M.
            and Striano,P.
  TITLE     Refining the electroclinical spectrum of NPRL3-related epilepsy: A
            novel multiplex family and literature review
  JOURNAL   Epilepsia Open 8 (4), 1314-1330 (2023)
   PUBMED   37491868
  REMARK    GeneRIF: Refining the electroclinical spectrum of NPRL3-related
            epilepsy: A novel multiplex family and literature review.
            Review article
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Wang,H., Liu,W., Zhang,Y., Liu,Q., Cai,L. and Jiang,Y.
  TITLE     Seizure features and outcomes in 50 children with GATOR1 variants:
            A retrospective study, more favorable for epilepsy surgery
  JOURNAL   Epilepsia Open 8 (3), 969-979 (2023)
   PUBMED   37259768
  REMARK    GeneRIF: Seizure features and outcomes in 50 children with GATOR1
            variants: A retrospective study, more favorable for epilepsy
            surgery.
            Review article
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Wang,Y., Yu,P., Zhu,G., Wu,X., Ding,D. and Hong,Z.
  TITLE     The clinical features of familial focal epilepsy with variable foci
            and NPRL3 gene variant
  JOURNAL   PLoS One 18 (4), e0284924 (2023)
   PUBMED   37099548
  REMARK    GeneRIF: The clinical features of familial focal epilepsy with
            variable foci and NPRL3 gene variant.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Neklesa,T.K. and Davis,R.W.
  TITLE     A genome-wide screen for regulators of TORC1 in response to amino
            acid starvation reveals a conserved Npr2/3 complex
  JOURNAL   PLoS Genet 5 (6), e1000515 (2009)
   PUBMED   19521502
REFERENCE   7  (residues 1 to 569)
  AUTHORS   De Gobbi,M., Viprakasit,V., Hughes,J.R., Fisher,C., Buckle,V.J.,
            Ayyub,H., Gibbons,R.J., Vernimmen,D., Yoshinaga,Y., de Jong,P.,
            Cheng,J.F., Rubin,E.M., Wood,W.G., Bowden,D. and Higgs,D.R.
  TITLE     A regulatory SNP causes a human genetic disease by creating a new
            transcriptional promoter
  JOURNAL   Science 312 (5777), 1215-1217 (2006)
   PUBMED   16728641
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Vyas,P., Vickers,M.A., Picketts,D.J. and Higgs,D.R.
  TITLE     Conservation of position and sequence of a novel, widely expressed
            gene containing the major human alpha-globin regulatory element
  JOURNAL   Genomics 29 (3), 679-689 (1995)
   PUBMED   8575760
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z69666.1, DA258664.1,
            AK090717.1 and Z69720.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.75559.1, SRR1660803.100275.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000611875.5/ ENSP00000478273.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..569
                     /product="GATOR1 complex protein NPRL3 isoform 1"
                     /note="conserved gene telomeric to alpha globin cluster;
                     -14 gene protein; alpha-globin regulatory
                     element-containing gene protein; GATOR complex protein
                     NPRL3; GATOR1 complex protein NPRL3"
                     /calculated_mol_wt=63474
     Region          27..60
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12980.1)"
     Region          64..416
                     /region_name="NPR3"
                     /note="Nitrogen Permease regulator of amino acid transport
                     activity 3; cl24021"
                     /db_xref="CDD:451662"
     Region          416..477
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12980.1)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12980.1)"
     CDS             1..569
                     /gene="NPRL3"
                     /gene_synonym="C16orf35; CGTHBA; FFEVF3; HS-40; MARE;
                     NPR3; RMD11"
                     /coded_by="NM_001077350.3:100..1809"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73795.1"
                     /db_xref="GeneID:8131"
                     /db_xref="HGNC:HGNC:14124"
                     /db_xref="MIM:600928"
ORIGIN      
        1 mrdntspisv ilvssgsrgn kllfrypfqr sqehpasqts kprsryaasn tgdhadeqdg
       61 dsrfsdvila tilatksemc gqkfelkidn vrfvghptll qhalgqiskt dpspkreapt
      121 milfnvvfal ranadpsvin clhnlsrria tvlqheerrc qyltreakli lalqdevsam
      181 adgnegpqsp fhhilpkckl ardlkeayds lctsgvvrlh inswlevsfc lphkihyaas
      241 slippeaier slkairpyha llllsdeksl lgelpidcsp alvrviktts avknlqqlaq
      301 dadlallqvf qlaahlvywg kaiiiyplce nnvymlspna svclysplae qfshqfpshd
      361 lpsvlakfsl pvslsefrnp lapavqetql iqmvvwmlqr rlliqlhtyv clmaspseee
      421 prpreddvpf tarvggrsls tpnalsfgsp tssddmtlts psmdnssael lpsgdsplnq
      481 rmtenllasl seheraails vpaaqnpedl rmfarllhyf rgrhhleeim ynentrrsql
      541 lmlfdkfrsv lvvtthedpv iavfqallp
//
LOCUS       NP_004760                531 aa            linear   PRI 20-NOV-2025
DEFINITION  acid-sensing ion channel 3 isoform a [Homo sapiens].
ACCESSION   NP_004760
VERSION     NP_004760.1
DBSOURCE    REFSEQ: accession NM_004769.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Balboni,A., D'Angelo,C., Collura,N., Brusco,S., Di Berardino,C.,
            Targa,A., Massoti,B., Mastrangelo,E., Milani,M., Seneci,P.,
            Broccoli,V., Muzio,L., Galli,R. and Menegon,A.
  TITLE     Acid-sensing ion channel 3 is a new potential therapeutic target
            for the control of glioblastoma cancer stem cells growth
  JOURNAL   Sci Rep 14 (1), 20421 (2024)
   PUBMED   39227705
  REMARK    GeneRIF: Acid-sensing ion channel 3 is a new potential therapeutic
            target for the control of glioblastoma cancer stem cells growth.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Jacquot,F., Khoury,S., Labrum,B., Delanoe,K., Pidoux,L.,
            Barbier,J., Delay,L., Bayle,A., Aissouni,Y., Barriere,D.A.,
            Kultima,K., Freyhult,E., Hugo,A., Kosek,E., Ahmed,A.S., Jurczak,A.,
            Lingueglia,E., Svensson,C.I., Breuil,V., Ferreira,T., Marchand,F.
            and Deval,E.
  TITLE     Lysophosphatidylcholine 16:0 mediates chronic joint pain associated
            to rheumatic diseases through acid-sensing ion channel 3
  JOURNAL   Pain 163 (10), 1999-2013 (2022)
   PUBMED   35086123
  REMARK    GeneRIF: Lysophosphatidylcholine 16:0 mediates chronic joint pain
            associated to rheumatic diseases through acid-sensing ion channel
            3.
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Han,X., Zhang,Y., Lee,A., Li,Z., Gao,J., Wu,X., Zhao,J., Wang,H.,
            Chen,D., Zou,D. and Owyang,C.
  TITLE     Upregulation of acid sensing ion channels is associated with
            esophageal hypersensitivity in GERD
  JOURNAL   FASEB J 36 (1), e22083 (2022)
   PUBMED   34918385
  REMARK    GeneRIF: Upregulation of acid sensing ion channels is associated
            with esophageal hypersensitivity in GERD.
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Lottering,B. and Lin,Y.W.
  TITLE     TRPV1 Responses in the Cerebellum Lobules VI, VII, VIII Using
            Electroacupuncture Treatment for Chronic Pain and Depression
            Comorbidity in a Murine Model
  JOURNAL   Int J Mol Sci 22 (9), 5028 (2021)
   PUBMED   34068557
  REMARK    GeneRIF: TRPV1 Responses in the Cerebellum Lobules VI, VII, VIII
            Using Electroacupuncture Treatment for Chronic Pain and Depression
            Comorbidity in a Murine Model.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Catarsi,S., Babinski,K. and Seguela,P.
  TITLE     Selective modulation of heteromeric ASIC proton-gated channels by
            neuropeptide FF
  JOURNAL   Neuropharmacology 41 (5), 592-600 (2001)
   PUBMED   11587714
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Babinski,K., Catarsi,S., Biagini,G. and Seguela,P.
  TITLE     Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric
            proton-gated channels sensitive to Gd3+
  JOURNAL   J Biol Chem 275 (37), 28519-28525 (2000)
   PUBMED   10842183
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Babinski,K., Le,K.T. and Seguela,P.
  TITLE     Molecular cloning and regional distribution of a human proton
            receptor subunit with biphasic functional properties
  JOURNAL   J Neurochem 72 (1), 51-57 (1999)
   PUBMED   9886053
REFERENCE   9  (residues 1 to 531)
  AUTHORS   de Weille,J.R., Bassilana,F., Lazdunski,M. and Waldmann,R.
  TITLE     Identification, functional expression and chromosomal localisation
            of a sustained human proton-gated cation channel
  JOURNAL   FEBS Lett 433 (3), 257-260 (1998)
   PUBMED   9744806
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Ishibashi,K. and Marumo,F.
  TITLE     Molecular cloning of a DEG/ENaC sodium channel cDNA from human
            testis
  JOURNAL   Biochem Biophys Res Commun 245 (2), 589-593 (1998)
   PUBMED   9571199
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313926.1 and AF095897.1.
            
            Summary: This gene encodes a member of the degenerin/epithelial
            sodium channel (DEG/ENaC) superfamily. The members of this family
            are amiloride-sensitive sodium channels that contain intracellular
            N and C termini, two hydrophobic transmembrane regions, and a large
            extracellular loop, which has many cysteine residues with conserved
            spacing. The member encoded by this gene is an acid sensor and may
            play an important role in the detection of lasting pH changes. In
            addition, a heteromeric association between this member and
            acid-sensing (proton-gated) ion channel 2 has been observed as
            proton-gated channels sensitive to gadolinium. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Feb 2012].
            
            Transcript Variant: This variant (1) uses an alternate splice site
            in the 3' coding region, compared to variant 2. The resulting
            protein (isoform a) has a shorter and distinct C-terminus, compared
            to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF095897.1, AB010575.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349064.10/ ENSP00000344838.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..531
                     /product="acid-sensing ion channel 3 isoform a"
                     /note="testis sodium channel 1; proton-gated cation
                     channel subunit; modulatory subunit of ASIC2a;
                     amiloride-sensitive cation channel 3, testis; acid-sensing
                     ion channel 3; neuronal amiloride-sensitive cation channel
                     3; acid sensing (proton gated) ion channel 3"
                     /calculated_mol_wt=58774
     Region          20..514
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            44..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Region          285..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            442..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Region          447..449
                     /region_name="GAS motif, ion selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P78348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Region          528..531
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000269|PubMed:15317815"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     CDS             1..531
                     /gene="ASIC3"
                     /gene_synonym="ACCN3; DRASIC; SLNAC1; TNaC1"
                     /coded_by="NM_004769.4:356..1951"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5916.1"
                     /db_xref="GeneID:9311"
                     /db_xref="HGNC:HGNC:101"
                     /db_xref="MIM:611741"
ORIGIN      
        1 mkptsgpeea rrpasdirvf asncsmhglg hvfgpgslsl rrgmwaaavv lsvatflyqv
       61 aervryyref hhqtaldere shrlifpavt lcninplrrs rltpndlhwa gsallgldpa
      121 ehaaflralg rppappgfmp sptfdmaqly araghslddm lldcrfrgqp cgpenfttif
      181 trmgkcytfn sgadgaellt ttrggmgngl dimldvqqee ylpvwrdnee tpfevgirvq
      241 ihsqeeppii dqlglgvspg yqtfvscqqq qlsflpppwg dcssaslnpn yepepsdplg
      301 spspspsppy tlmgcrlace tryvarkcgc rmvympgdvp vcspqqyknc ahpaidamlr
      361 kdscacpnpc astryakels mvripsraaa rflarklnrs eayiaenvla ldiffealny
      421 etveqkkaye msellgdigg qmglfigasl ltileildyl cevfrdkvlg yfwnrqhsqr
      481 hsstnllqeg lgshrtqvph lslgprpptp pcavtktlsa shrtcylvtq l
//
LOCUS       NP_001186759             485 aa            linear   PRI 20-NOV-2025
DEFINITION  heparanase isoform 3 preproprotein [Homo sapiens].
ACCESSION   NP_001186759
VERSION     NP_001186759.1
DBSOURCE    REFSEQ: accession NM_001199830.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Lee,C.S., Shang,R., Wang,F., Khayambashi,P., Wang,H., Araujo,G.,
            Puri,K., Vlodavsky,I., Hussein,B. and Rodrigues,B.
  TITLE     Heparanase Stimulation of Physiologic Cardiac Hypertrophy Is
            Suppressed After Chronic Diabetes, Resulting in Cardiac Remodeling
            and Dysfunction
  JOURNAL   Diabetes 73 (8), 1300-1316 (2024)
   PUBMED   38771953
  REMARK    GeneRIF: Heparanase Stimulation of Physiologic Cardiac Hypertrophy
            Is Suppressed After Chronic Diabetes, Resulting in Cardiac
            Remodeling and Dysfunction.
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Martinez,H.A., Koliesnik,I., Kaber,G., Reid,J.K., Nagy,N.,
            Barlow,G., Falk,B.A., Medina,C.O., Hargil,A., Zihsler,S.,
            Vlodavsky,I., Li,J.P., Perez-Cruz,M., Tang,S.W., Meyer,E.H.,
            Wrenshall,L.E., Lord,J.D., Garcia,K.C., Palmer,T.D., Steinman,L.,
            Nepom,G.T., Wight,T.N., Bollyky,P.L. and Kuipers,H.F.
  TITLE     Regulatory T cells use heparanase to access IL-2 bound to
            extracellular matrix in inflamed tissue
  JOURNAL   Nat Commun 15 (1), 1564 (2024)
   PUBMED   38378682
  REMARK    GeneRIF: Regulatory T cells use heparanase to access IL-2 bound to
            extracellular matrix in inflamed tissue.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Wang,C., Huang,Y., Jia,B., Huang,Y. and Chen,J.
  TITLE     Heparanase promotes malignant phenotypes of human oral squamous
            carcinoma cells by regulating the epithelial-mesenchymal
            transition-related molecules and infiltrated levels of natural
            killer cells
  JOURNAL   Arch Oral Biol 154, 105775 (2023)
   PUBMED   37481997
  REMARK    GeneRIF: Heparanase promotes malignant phenotypes of human oral
            squamous carcinoma cells by regulating the epithelial-mesenchymal
            transition-related molecules and infiltrated levels of natural
            killer cells.
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Ostrovsky,O., Beider,K., Magen,H., Leiba,M., Sanderson,R.D.,
            Vlodavsky,I. and Nagler,A.
  TITLE     Effect of HPSE and HPSE2 SNPs on the Risk of Developing Primary
            Paraskeletal Multiple Myeloma
  JOURNAL   Cells 12 (6), 913 (2023)
   PUBMED   36980254
  REMARK    GeneRIF: Effect of HPSE and HPSE2 SNPs on the Risk of Developing
            Primary Paraskeletal Multiple Myeloma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 485)
  AUTHORS   van der Velden,A.I.M., van den Berg,B.M., van den Born,B.J.,
            Galenkamp,H., Ijpelaar,D.H.T. and Rabelink,T.J.
  TITLE     Ethnic differences in urinary monocyte chemoattractant protein-1
            and heparanase-1 levels in individuals with type 2 diabetes: the
            HELIUS study
  JOURNAL   BMJ Open Diabetes Res Care 10 (6) (2022)
   PUBMED   36564084
  REMARK    GeneRIF: Ethnic differences in urinary monocyte chemoattractant
            protein-1 and heparanase-1 levels in individuals with type 2
            diabetes: the HELIUS study.
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Nasser,N.J., Avivi,A., Shushy,M., Vlodavsky,I. and Nevo,E.
  TITLE     Cloning, expression, and characterization of an alternatively
            spliced variant of human heparanase
  JOURNAL   Biochem Biophys Res Commun 354 (1), 33-38 (2007)
   PUBMED   17208203
  REMARK    GeneRIF: Splice 5 escaped proteolytic cleavage, was devoid of HS
            degradation activity and exhibited diffused rather than granular
            cellular localization.
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Kussie,P.H., Hulmes,J.D., Ludwig,D.L., Patel,S., Navarro,E.C.,
            Seddon,A.P., Giorgio,N.A. and Bohlen,P.
  TITLE     Cloning and functional expression of a human heparanase gene
  JOURNAL   Biochem Biophys Res Commun 261 (1), 183-187 (1999)
   PUBMED   10405343
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Hulett,M.D., Freeman,C., Hamdorf,B.J., Baker,R.T., Harris,M.J. and
            Parish,C.R.
  TITLE     Cloning of mammalian heparanase, an important enzyme in tumor
            invasion and metastasis
  JOURNAL   Nat Med 5 (7), 803-809 (1999)
   PUBMED   10395326
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Vlodavsky,I., Friedmann,Y., Elkin,M., Aingorn,H., Atzmon,R.,
            Ishai-Michaeli,R., Bitan,M., Pappo,O., Peretz,T., Michal,I.,
            Spector,L. and Pecker,I.
  TITLE     Mammalian heparanase: gene cloning, expression and function in
            tumor progression and metastasis
  JOURNAL   Nat Med 5 (7), 793-802 (1999)
   PUBMED   10395325
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Pikas,D.S., Li,J.P., Vlodavsky,I. and Lindahl,U.
  TITLE     Substrate specificity of heparanases from human hepatoma and
            platelets
  JOURNAL   J Biol Chem 273 (30), 18770-18777 (1998)
   PUBMED   9668050
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114781.2, AM419200.1 and
            AW293069.1.
            
            Summary: Heparan sulfate proteoglycans are major components of the
            basement membrane and extracellular matrix. The protein encoded by
            this gene is an enzyme that cleaves heparan sulfate proteoglycans
            to permit cell movement through remodeling of the extracellular
            matrix. In addition, this cleavage can release bioactive molecules
            from the extracellular matrix. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            5' coding region compared to variant 1. The resulting protein
            (isoform 3) is shorter but has the identical N- and C- termini
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AM419200.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.23"
     Protein         1..485
                     /product="heparanase isoform 3 preproprotein"
                     /EC_number="3.2.1.166"
                     /note="heparanase-1; endo-glucoronidase"
                     /calculated_mol_wt=51154
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3598
     proprotein      36..485
                     /product="heparanase isoform 3 proprotein"
                     /calculated_mol_wt=51154
     mat_peptide     36..109
                     /product="heparanase 8 kDa subunit"
                     /calculated_mol_wt=8265
     mat_peptide     158..485
                     /product="heparanase 50 kDa subunit isoform 3"
                     /calculated_mol_wt=36965
     Region          <179..312
                     /region_name="Glyco_hydro_79n"
                     /note="Glycosyl hydrolase family 79, N-terminal domain;
                     pfam03662"
                     /db_xref="CDD:461010"
     CDS             1..485
                     /gene="HPSE"
                     /gene_synonym="HPA; HPA1; HPR1; HPSE1; HSE1"
                     /coded_by="NM_001199830.1:32..1489"
                     /note="isoform 3 preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS56337.1"
                     /db_xref="GeneID:10855"
                     /db_xref="HGNC:HGNC:5164"
                     /db_xref="MIM:604724"
ORIGIN      
        1 mllrskpalp pplmllllgp lgplspgalp rpaqaqdvvd ldfftqeplh lvspsflsvt
       61 idanlatdpr flillgspkl rtlarglspa ylrfggtktd flifdpkkes tfeersywqs
      121 qvnqdickyg sippdveekl rlewpyqeql llrehyqkkf knstyskpns flkkadifin
      181 gsqlgedfiq lhkllrkstf knaklygpdv gqprrktakm lksflkagge vidsvtwhhy
      241 ylngrtatke dflnpdvldi fissvqkvfq vvestrpgkk vwlgetssay gggapllsdt
      301 faagfmwldk lglsarmgie vvmrqvffga gnyhlvdenf dplpdywlsl lfkklvgtkv
      361 lmasvqgskr rklrvylhct ntdnprykeg dltlyainlh nvtkylrlpy pfsnkqvdky
      421 llrplgphgl lsksvqlngl tlkmvddqtl pplmekplrp gsslglpafs ysffvirnak
      481 vaaci
//
LOCUS       NP_116147                110 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD finger-like domain-containing protein 5A [Homo sapiens].
ACCESSION   NP_116147
VERSION     NP_116147.1
DBSOURCE    REFSEQ: accession NM_032758.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Chang,Z., Jia,Y., Gao,M., Song,L., Zhang,W., Zhao,R., Yu,D.,
            Liu,X., Li,J. and Qin,Y.
  TITLE     PHF5A promotes esophageal squamous cell carcinoma progression via
            stabilizing VEGFA
  JOURNAL   Biol Direct 19 (1), 19 (2024)
   PUBMED   38429756
  REMARK    GeneRIF: PHF5A promotes esophageal squamous cell carcinoma
            progression via stabilizing VEGFA.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Ding,N., Li,M. and Zhao,X.
  TITLE     PHF5A is a potential diagnostic, prognostic, and immunological
            biomarker in pan-cancer
  JOURNAL   Sci Rep 13 (1), 17521 (2023)
   PUBMED   37845358
  REMARK    GeneRIF: PHF5A is a potential diagnostic, prognostic, and
            immunological biomarker in pan-cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   9  (residues 1 to 110)
  AUTHORS   Trappe,R., Ahmed,M., Glaser,B., Vogel,C., Tascou,S., Burfeind,P.
            and Engel,W.
  TITLE     Identification and characterization of a novel murine multigene
            family containing a PHD-finger-like motif
  JOURNAL   Biochem Biophys Res Commun 293 (2), 816-826 (2002)
   PUBMED   12054543
  REMARK    GeneRIF: The molecular and genetic research in this paper is
            performed on mouse but the paper identifies and discusses
            homologues found in human genomic sequence databases.
REFERENCE   10 (residues 1 to 110)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU584712.1, AL008582.11 and
            BC007321.2.
            
            Summary: This gene encodes a subunit of the splicing factor 3b
            protein complex. Splicing factor 3b, together with splicing factor
            3a and a 12S RNA unit, forms the U2 small nuclear
            ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a
            complex binds pre-mRNA upstream of the intron's branch site in a
            sequence-independent manner and may anchor the U2 snRNP to the
            pre-mRNA. The protein encoded by this gene contains a
            PHD-finger-like domain that is flanked by highly basic N- and
            C-termini. This protein belongs to the PHD-finger superfamily and
            may act as a chromatin-associated protein. This gene has several
            pseudogenes on different chromosomes. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.132999.1,
                                           SRR1163658.184099.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467150 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216252.4/ ENSP00000216252.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..110
                     /product="PHD finger-like domain-containing protein 5A"
                     /note="PHD-finger 5a; PHD finger-like domain protein 5A;
                     splicing factor 3B associated 14 kDa protein; splicing
                     factor 3b, subunit 7"
                     /calculated_mol_wt=12274
     Region          1..104
                     /region_name="PHF5"
                     /note="PHF5-like protein; pfam03660"
                     /db_xref="CDD:461008"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P83870; propagated from
                     UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Site            17
                     /site_type="other"
                     /note="Interaction with SF3B3.
                     /evidence=ECO:0000269|PubMed:27720643; propagated from
                     UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Region          35..51
                     /region_name="Interaction with SF3B1 and SF3B3.
                     /evidence=ECO:0000269|PubMed:27720643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Region          79..82
                     /region_name="Interaction with SF3B3.
                     /evidence=ECO:0000269|PubMed:27720643"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7RTV0.1)"
     Site            100
                     /site_type="other"
                     /note="Interaction with RNA.
                     /evidence=ECO:0000269|PubMed:27720643; propagated from
                     UniProtKB/Swiss-Prot (Q7RTV0.1)"
     CDS             1..110
                     /gene="PHF5A"
                     /gene_synonym="bK223H9.2; INI; Rds3; SAP14b; SF3b14b;
                     SF3B7"
                     /coded_by="NM_032758.4:40..372"
                     /db_xref="CCDS:CCDS14016.1"
                     /db_xref="GeneID:84844"
                     /db_xref="HGNC:HGNC:18000"
                     /db_xref="MIM:617846"
ORIGIN      
        1 makhhpdlif crkqagvaig rlcekcdgkc vicdsyvrpc tlvricdecn ygsyqgrcvi
       61 cggpgvsday yckectiqek drdgcpkivn lgssktdlfy erkkygfkkr
//
LOCUS       NP_689945                276 aa            linear   PRI 20-NOV-2025
DEFINITION  radial spoke head protein 9 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_689945
VERSION     NP_689945.2
DBSOURCE    REFSEQ: accession NM_152732.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Hwang,J.Y., Chai,P., Nawaz,S., Choi,J., Lopez-Giraldez,F.,
            Hussain,S., Bilguvar,K., Mane,S., Lifton,R.P., Ahmad,W., Zhang,K.
            and Chung,J.J.
  TITLE     LRRC23 truncation impairs radial spoke 3 head assembly and sperm
            motility underlying male infertility
  JOURNAL   Elife 12, 90095 (2023)
   PUBMED   38091523
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Zhu,L., Liu,H., Chen,Y., Yan,X. and Zhu,X.
  TITLE     Rsph9 is critical for ciliary radial spoke assembly and central
            pair microtubule stability
  JOURNAL   Biol Cell 111 (2), 29-38 (2019)
   PUBMED   30383886
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Zietkiewicz,E., Bukowy-Bieryllo,Z., Voelkel,K., Klimek,B.,
            Dmenska,H., Pogorzelski,A., Sulikowska-Rowinska,A., Rutkiewicz,E.
            and Witt,M.
  TITLE     Mutations in radial spoke head genes and ultrastructural cilia
            defects in East-European cohort of primary ciliary dyskinesia
            patients
  JOURNAL   PLoS One 7 (3), e33667 (2012)
   PUBMED   22448264
  REMARK    GeneRIF: Mutations in RSPH9 leads to ultrastructural cilia defects
            and ciliary dyskinesia.
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Reish,O., Slatkin,M., Chapman-Shimshoni,D., Elizur,A., Chioza,B.,
            Castleman,V. and Mitchison,H.M.
  TITLE     Founder mutation(s) in the RSPH9 gene leading to primary ciliary
            dyskinesia in two inbred Bedouin families
  JOURNAL   Ann Hum Genet 74 (2), 117-125 (2010)
   PUBMED   20070851
  REMARK    GeneRIF: Study focused on an extended 5 generation Bedouin family,
            analysed mutation segregation, and calculated the age of the
            mutated allele in 2 families based on haplotypes and
            haplotype+microsatellite in an attempt to define the source of the
            mutation.
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Castleman,V.H., Romio,L., Chodhari,R., Hirst,R.A., de Castro,S.C.,
            Parker,K.A., Ybot-Gonzalez,P., Emes,R.D., Wilson,S.W., Wallis,C.,
            Johnson,C.A., Herrera,R.J., Rutman,A., Dixon,M., Shoemark,A.,
            Bush,A., Hogg,C., Gardiner,R.M., Reish,O., Greene,N.D.,
            O'Callaghan,C., Purton,S., Chung,E.M. and Mitchison,H.M.
  TITLE     Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause
            primary ciliary dyskinesia with central-microtubular-pair
            abnormalities
  JOURNAL   Am J Hum Genet 84 (2), 197-209 (2009)
   PUBMED   19200523
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA486918.1, BC029519.1 and
            AL136131.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 18, 2003 this sequence version replaced NP_689945.1.
            
            Summary: This gene encodes a protein thought to be a component of
            the radial spoke head in motile cilia and flagella. Mutations in
            this gene are associated with primary ciliary dyskinesia 12.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291399.1, SRR5189667.286777.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372163.5/ ENSP00000361236.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..276
                     /product="radial spoke head protein 9 homolog isoform 1"
                     /note="radial spoke head protein 9 homolog; radial spoke
                     head 9 homolog"
                     /calculated_mol_wt=31161
     Region          <17..269
                     /region_name="Radial_spoke"
                     /note="Radial spokehead-like protein; pfam04712"
                     /db_xref="CDD:461405"
     CDS             1..276
                     /gene="RSPH9"
                     /gene_synonym="C6orf206; CILD12; MRPS18AL1"
                     /coded_by="NM_152732.5:64..894"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4905.1"
                     /db_xref="GeneID:221421"
                     /db_xref="HGNC:HGNC:21057"
                     /db_xref="MIM:612648"
ORIGIN      
        1 mdadslllsl elasgsgqgl spdrrasllt slmlvkrdyr ydrvlfwgri lglvadyyia
       61 qglsedqlap rktlyslnct ewsllppate emvaqssvvk grfmgdpsye yehtelqkvn
      121 egekvfeeei vvqikeetrl vsvidqidka vaiiprgalf ktpfgpthvn rtfeglslse
      181 akklssyfhf repvelknkt llekadldps ldfmdslehd ipkgswsiqm ergnalvvlr
      241 sllwpgltfy haprtknygy vyvgtgeknm dlpfml
//
LOCUS       NP_001138440             967 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4-like isoform 4 [Homo sapiens].
ACCESSION   NP_001138440
VERSION     NP_001138440.1
DBSOURCE    REFSEQ: accession NM_001144968.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 967)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 967)
  AUTHORS   Chen,G., Pei,Y., Ye,Q., Xie,Z., Gyawali,L. and Liang,X.
  TITLE     NEDD4L-mediated RASGRP2 suppresses high-glucose and oxLDL-induced
            vascular endothelial cell dysfunctions by activating Rap1 and R-Ras
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119844 (2024)
   PUBMED   39260747
  REMARK    GeneRIF: NEDD4L-mediated RASGRP2 suppresses high-glucose and
            oxLDL-induced vascular endothelial cell dysfunctions by activating
            Rap1 and R-Ras.
REFERENCE   3  (residues 1 to 967)
  AUTHORS   Wang,R., Wang,R., Zhou,S., Liu,T., Dang,J., Chen,Q., Chen,J. and
            Wang,Z.
  TITLE     Ubiquitination of angiotensin-converting enzyme 2 contributes to
            the development of pulmonary arterial hypertension mediated by
            neural precursor cell-expressed developmentally down-regulated gene
            4-Like
  JOURNAL   Respir Res 25 (1), 326 (2024)
   PUBMED   39210401
  REMARK    GeneRIF: Ubiquitination of angiotensin-converting enzyme 2
            contributes to the development of pulmonary arterial hypertension
            mediated by neural precursor cell-expressed developmentally
            down-regulated gene 4-Like.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 967)
  AUTHORS   Yang,B. and Kumar,S.
  TITLE     Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with
            distinct physiological functions
  JOURNAL   Cell Death Differ 17 (1), 68-77 (2010)
   PUBMED   19557014
  REMARK    Review article
REFERENCE   5  (residues 1 to 967)
  AUTHORS   Russo,C.J., Melista,E., Cui,J., DeStefano,A.L., Bakris,G.L.,
            Manolis,A.J., Gavras,H. and Baldwin,C.T.
  TITLE     Association of NEDD4L ubiquitin ligase with essential hypertension
  JOURNAL   Hypertension 46 (3), 488-491 (2005)
   PUBMED   16103266
  REMARK    GeneRIF: Significant association between several SNPs and
            hypertension in US whites, Greek whites, and African-Americans.
            Genetic variation in NEDD4L may play role in development or
            progression of some forms of hypertension.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 967)
  AUTHORS   Qi,H., Grenier,J., Fournier,A. and Labrie,C.
  TITLE     Androgens differentially regulate the expression of NEDD4L
            transcripts in LNCaP human prostate cancer cells
  JOURNAL   Mol Cell Endocrinol 210 (1-2), 51-62 (2003)
   PUBMED   14615060
  REMARK    GeneRIF: Results describe the isolation of three new NEDD4L
            transcripts designated NEDD4Lf, NEDD4Lg and NEDD4Lh, which encode
            different forms of the NEDD4L protein.
REFERENCE   7  (residues 1 to 967)
  AUTHORS   Itani,O.A., Campbell,J.R., Herrero,J., Snyder,P.M. and Thomas,C.P.
  TITLE     Alternate promoters and variable splicing lead to hNedd4-2 isoforms
            with a C2 domain and varying number of WW domains
  JOURNAL   Am J Physiol Renal Physiol 285 (5), F916-F929 (2003)
   PUBMED   12876068
  REMARK    GeneRIF: Alternate transcripts of Nedd4-2 may interact with ENaC
            differently. hNedd4-2 has role in regulation of ENaC. Protein
            domains are important for Nedd4-2 function.
            GeneRIF: Identification of multiple splice forms and 5' variants of
            Nedd4l.  5' variants inhibit ENaC-mediated Na+ transport when
            reconstituted in FRT epithelia.  Other splice forms encode Nedd4L
            isoforms with 2 to 4 WW domains having varying affinity for ENaC.
REFERENCE   8  (residues 1 to 967)
  AUTHORS   Chen,H., Ross,C.A., Wang,N., Huo,Y., MacKinnon,D.F., Potash,J.B.,
            Simpson,S.G., McMahon,F.J., DePaulo,J.R. Jr. and McInnis,M.G.
  TITLE     NEDD4L on human chromosome 18q21 has multiple forms of transcripts
            and is a homologue of the mouse Nedd4-2 gene
  JOURNAL   Eur J Hum Genet 9 (12), 922-930 (2001)
   PUBMED   11840194
  REMARK    GeneRIF: Candidate gene for autosomal dominant orthostatic
            hypotensive disorder.
REFERENCE   9  (residues 1 to 967)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   10 (residues 1 to 967)
  AUTHORS   Nuber,U., Schwarz,S., Kaiser,P., Schneider,R. and Scheffner,M.
  TITLE     Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7
            (E2-F1) and characterization of their interaction with E6-AP and
            RSP5
  JOURNAL   J Biol Chem 271 (5), 2795-2800 (1996)
   PUBMED   8576257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107896.7, AY112984.2,
            BC032597.2 and AC090236.4.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein mediates the ubiquitination of
            multiple target substrates and plays a critical role in epithelial
            sodium transport by regulating the cell surface expression of the
            epithelial sodium channel, ENaC. Single nucleotide polymorphisms in
            this gene may be associated with essential hypertension.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Mar
            2012].
            
            Transcript Variant: This variant (g) uses an alternate first exon,
            compared to variant j, which results in the use of a different
            start codon and a protein (isoform 4) with a shorter and distinct
            N-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript was derived from the reference
            genome assembly. The genomic coordinates were determined from
            alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY112984.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..967
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..967
                     /product="E3 ubiquitin-protein ligase NEDD4-like isoform
                     4"
                     /EC_number="2.3.2.26"
                     /EC_number="2.3.2.36"
                     /note="ubiquitin-protein ligase Rsp5; HECT-type E3
                     ubiquitin transferase NED4L; neural precursor cell
                     expressed, developmentally down-regulated 4-like, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=111184
     Region          13..145
                     /region_name="C2_NEDD4_NEDD4L"
                     /note="C2 domain present in the Human neural precursor
                     cell-expressed, developmentally down-regulated 4 (NEDD4)
                     and NEDD4-like (NEDD4L/NEDD42); cd04033"
                     /db_xref="CDD:175999"
     Site            order(34,87,89,94)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175999"
     Region          190..216
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          <311..494
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          379..408
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          492..522
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(506,517)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          541..573
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(557,568)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(616,647,658,720,893,928..929,932..936,956,963)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          634..963
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(748,751..752,754..755,758,763,765,769..770,772,777,
                     782,799,803)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..967
                     /gene="NEDD4L"
                     /gene_synonym="hNEDD4-2; NEDD4-2; NEDD4.2; PVNH7; RSP5"
                     /coded_by="NM_001144968.2:217..3120"
                     /note="isoform 4 is encoded by transcript variant g"
                     /db_xref="CCDS:CCDS45874.1"
                     /db_xref="GeneID:23327"
                     /db_xref="HGNC:HGNC:7728"
                     /db_xref="MIM:606384"
ORIGIN      
        1 mrrlafeqge srilrvkvvs gidlakkdif gasdpyvkls lyvadenrel alvqtktikk
       61 tlnpkwneef yfrvnpsnhr llfevfdenr ltrddflgqv dvplshlpte dptmerpytf
      121 kdfllrprsh ksrvkgflrl kmaympkngg qdeensdqrd dmehgwevvd sndsasqhqe
      181 elpppplppg weekvdnlgr tyyvnhnnrt tqwhrpslmd vssesdnnir qinqeaahrr
      241 frsrrhised lepepseggd vpepwetise evniagdslg lalppppasp gsrtspqels
      301 eelsrrlqit pdsngeqfss liqrepssrl rscsvtdava eqghlpppsa pagrarsstv
      361 tggeeptpsv ayvhttpglp sgweerkdak grtyyvnhnn rtttwtrpim qlaedgasgs
      421 atnsnnhlie pqirrprsls sptvtlsapl egakdspvrr avkdtlsnpq spqpspynsp
      481 kpqhkvtqsf lppgwemria pngrpffidh ntktttwedp rlkfpvhmrs ktslnpndlg
      541 plppgweeri hldgrtfyid hnskitqwed prlqnpaitg pavpysrefk qkydyfrkkl
      601 kkpadipnrf emklhrnnif eesyrrimsv krpdvlkarl wiefesekgl dyggvarewf
      661 fllskemfnp yyglfeysat dnytlqinpn sglcnedhls yftfigrvag lavfhgklld
      721 gffirpfykm mlgkqitlnd mesvdseyyn slkwilendp teldlmfcid eenfgqtyqv
      781 dlkpngseim vtnenkreyi dlviqwrfvn rvqkqmnafl egftellpid likifdenel
      841 ellmcglgdv dvndwrqhsi ykngycpnhp viqwfwkavl lmdaekrirl lqfvtgtsrv
      901 pmngfaelyg sngpqlftie qwgspeklpr ahtcfnrldl ppyetfedlr ekllmavena
      961 qgfegvd
//
LOCUS       NP_001147135             158 aa            linear   PRI 20-NOV-2025
DEFINITION  short coiled-coil protein isoform 2 [Homo sapiens].
ACCESSION   NP_001147135
VERSION     NP_001147135.1
DBSOURCE    REFSEQ: accession NM_001153663.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Wirth,M., Mouilleron,S., Zhang,W., Sjottem,E., Princely Abudu,Y.,
            Jain,A., Lauritz Olsvik,H., Bruun,J.A., Razi,M., Jefferies,H.B.J.,
            Lee,R., Joshi,D., O'Reilly,N., Johansen,T. and Tooze,S.A.
  TITLE     Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding
            Affinity and Specificity
  JOURNAL   J Mol Biol 433 (13), 166987 (2021)
   PUBMED   33845085
  REMARK    GeneRIF: Phosphorylation of the LIR Domain of SCOC Modulates ATG8
            Binding Affinity and Specificity.
            Erratum:[J Mol Biol. 2021 Jul 23;433(15):167049. doi:
            10.1016/j.jmb.2021.167049. PMID: 34052024]
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Stringer,S., Minica,C.C., Verweij,K.J., Mbarek,H., Bernard,M.,
            Derringer,J., van Eijk,K.R., Isen,J.D., Loukola,A.,
            Maciejewski,D.F., Mihailov,E., van der Most,P.J., Sanchez-Mora,C.,
            Roos,L., Sherva,R., Walters,R., Ware,J.J., Abdellaoui,A.,
            Bigdeli,T.B., Branje,S.J., Brown,S.A., Bruinenberg,M., Casas,M.,
            Esko,T., Garcia-Martinez,I., Gordon,S.D., Harris,J.M.,
            Hartman,C.A., Henders,A.K., Heath,A.C., Hickie,I.B., Hickman,M.,
            Hopfer,C.J., Hottenga,J.J., Huizink,A.C., Irons,D.E., Kahn,R.S.,
            Korhonen,T., Kranzler,H.R., Krauter,K., van Lier,P.A., Lubke,G.H.,
            Madden,P.A., Magi,R., McGue,M.K., Medland,S.E., Meeus,W.H.,
            Miller,M.B., Montgomery,G.W., Nivard,M.G., Nolte,I.M.,
            Oldehinkel,A.J., Pausova,Z., Qaiser,B., Quaye,L.,
            Ramos-Quiroga,J.A., Richarte,V., Rose,R.J., Shin,J.,
            Stallings,M.C., Stiby,A.I., Wall,T.L., Wright,M.J., Koot,H.M.,
            Paus,T., Hewitt,J.K., Ribases,M., Kaprio,J., Boks,M.P., Snieder,H.,
            Spector,T., Munafo,M.R., Metspalu,A., Gelernter,J., Boomsma,D.I.,
            Iacono,W.G., Martin,N.G., Gillespie,N.A., Derks,E.M. and Vink,J.M.
  TITLE     Genome-wide association study of lifetime cannabis use based on a
            large meta-analytic sample of 32 330 subjects from the
            International Cannabis Consortium
  JOURNAL   Transl Psychiatry 6 (3), e769 (2016)
   PUBMED   27023175
  REMARK    GeneRIF: SCOC SNPs were associated with lifetime cannabis use, but
            the association did not reach genome-wide significance.
            [Meta-Analysis]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Alborghetti,M.R., Furlan Ada,S., da Silva,J.C., Sforca,M.L.,
            Honorato,R.V., Granato,D.C., dos Santos Migueleti,D.L., Neves,J.L.,
            de Oliveira,P.S., Paes-Leme,A.F., Zeri,A.C., de Torriani,I.C. and
            Kobarg,J.
  TITLE     Structural analysis of intermolecular interactions in the kinesin
            adaptor complex fasciculation and elongation protein zeta 1/ short
            coiled-coil protein (FEZ1/SCOCO)
  JOURNAL   PLoS One 8 (10), e76602 (2013)
   PUBMED   24116125
  REMARK    GeneRIF: Studies indicate that FEZ1 (fasciculation and elongation
            protein zeta 1), SCOCO (short coiled-coil protein) and kinesins
            (kinesin heavy chain) are involved in biological transport process.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Behrens,C., Binotti,B., Schmidt,C., Robinson,C.V., Chua,J.J. and
            Kuhnel,K.
  TITLE     Crystal structure of the human short coiled coil protein and
            insights into SCOC-FEZ1 complex formation
  JOURNAL   PLoS One 8 (10), e76355 (2013)
   PUBMED   24098481
  REMARK    GeneRIF: SCOC forms a stable homogeneous complex with the coiled
            coil domain of FEZ1. SCOC dimerization and the SCOC surface residue
            R117 are important for this interaction.
            Erratum:[PLoS One. 2013;8(10).
            doi:10.1371/annotation/cb60d973-58aa-45e0-bbb3-1c7f5a42a8d2]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 158)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
  REMARK    GeneRIF: The identification of SCOC and WAC as novel regulatory
            proteins with diverse functions in autophagy contributes towards a
            fuller understanding of autophagosome formation.
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Van Valkenburgh,H., Shern,J.F., Sharer,J.D., Zhu,X. and Kahn,R.A.
  TITLE     ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
            specific and shared effectors: characterizing ARL1-binding proteins
  JOURNAL   J Biol Chem 276 (25), 22826-22837 (2001)
   PUBMED   11303027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN367654.1, DB465370.1,
            BC016511.1 and AA213765.1.
            
            Summary: This gene encodes a short coiled-coiled domain-containing
            protein that localizes to the Golgi apparatus. The encoded protein
            interacts with ADP-ribosylation factor-like proteins. Pseudogenes
            of this gene are found on chromosomes 1 and 14. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region compared to variant 1. The encoded
            isoform (2) is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.188063.1,
                                           SRR1660809.177920.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..158
                     /product="short coiled-coil protein isoform 2"
                     /calculated_mol_wt=17843
     Region          79..149
                     /region_name="DUF2205"
                     /note="Short coiled-coil protein; pfam10224"
                     /db_xref="CDD:431150"
     CDS             1..158
                     /gene="SCOC"
                     /gene_synonym="HRIHFB2072; SCOCO; UNC-69"
                     /coded_by="NM_001153663.1:28..504"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:60592"
                     /db_xref="HGNC:HGNC:20335"
ORIGIN      
        1 mrrrvfssqd wrasgwdgmg ffsrrtfcgr sgrscrgqlv qvsrpevsag slllpapqae
       61 dhssrilypr pksllpkmmn admdvdaenq veleektrli nqvlelqhtl edlsarvdav
      121 keenlklkse nqvlgqyien lmsassvfqt tdtkskrk
//
LOCUS       NP_808821                455 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1A isoform 3 [Homo sapiens].
ACCESSION   NP_808821
VERSION     NP_808821.2
DBSOURCE    REFSEQ: accession NM_177952.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Cheng,P., Wang,Y., Wu,Q., Zhang,H., Fang,W. and Feng,F.
  TITLE     Role of TRIM59 in regulating PPM1A in the pathogenesis of silicosis
            and the intervention effect of tanshinone IIA
  JOURNAL   Biomed Pharmacother 177, 117014 (2024)
   PUBMED   38908195
  REMARK    GeneRIF: Role of TRIM59 in regulating PPM1A in the pathogenesis of
            silicosis and the intervention effect of tanshinone IIA.
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Weon,S., Jo,S., Nam,B., Choi,S.H., Park,Y.S., Kim,Y.G. and Kim,T.H.
  TITLE     Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway
  JOURNAL   J Cell Mol Med 27 (5), 650-658 (2023)
   PUBMED   36756789
  REMARK    GeneRIF: Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Feng,D., Zhou,J., Liu,H., Wu,X., Li,F., Zhao,J., Zhang,Y., Wang,L.,
            Chao,M., Wang,Q., Qin,H., Ge,S., Liu,Q., Zhang,J. and Qu,Y.
  TITLE     Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain barrier
            disruption after subarachnoid hemorrhage
  JOURNAL   Sci Adv 8 (39), eabq2423 (2022)
   PUBMED   36179025
  REMARK    GeneRIF: Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain
            barrier disruption after subarachnoid hemorrhage.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Liu,C., Sun,W., Yang,K. and Xia,B.
  TITLE     Knockdown of TRIM65 suppressed the proliferation and invasiveness
            of gastric cancer cells by restricting the ubiquitin degradation of
            PPM1A
  JOURNAL   Exp Cell Res 416 (2), 113154 (2022)
   PUBMED   35421368
  REMARK    GeneRIF: Knockdown of TRIM65 suppressed the proliferation and
            invasiveness of gastric cancer cells by restricting the ubiquitin
            degradation of PPM1A.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Fjeld,C.C. and Denu,J.M.
  TITLE     Kinetic analysis of human serine/threonine protein phosphatase
            2Calpha
  JOURNAL   J Biol Chem 274 (29), 20336-20343 (1999)
   PUBMED   10400656
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Takekawa,M., Maeda,T. and Saito,H.
  TITLE     Protein phosphatase 2Calpha inhibits the human stress-responsive
            p38 and JNK MAPK pathways
  JOURNAL   EMBO J 17 (16), 4744-4752 (1998)
   PUBMED   9707433
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Das,A.K., Helps,N.R., Cohen,P.T. and Barford,D.
  TITLE     Crystal structure of the protein serine/threonine phosphatase 2C at
            2.0 A resolution
  JOURNAL   EMBO J 15 (24), 6798-6809 (1996)
   PUBMED   9003755
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Redpath,N.T., Price,N.T., Severinov,K.V. and Proud,C.G.
  TITLE     Regulation of elongation factor-2 by multisite phosphorylation
  JOURNAL   Eur J Biochem 213 (2), 689-699 (1993)
   PUBMED   8386634
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Mann,D.J., Campbell,D.G., McGowan,C.H. and Cohen,P.T.
  TITLE     Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and
            comparative analysis of amino acid sequences
  JOURNAL   Biochim Biophys Acta 1130 (1), 100-104 (1992)
   PUBMED   1311954
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157756.3, AK097843.1,
            AK313337.1, BC063243.1, AL132778.6 and AI076736.1.
            
            On Jun 29, 2008 this sequence version replaced NP_808821.1.
            
            Summary: The protein encoded by this gene is a member of the PP2C
            family of Ser/Thr protein phosphatases. PP2C family members are
            known to be negative regulators of cell stress response pathways.
            This phosphatase dephosphorylates, and negatively regulates the
            activities of, MAP kinases and MAP kinase kinases. It has been
            shown to inhibit the activation of p38 and JNK kinase cascades
            induced by environmental stresses. This phosphatase can also
            dephosphorylate cyclin-dependent kinases, and thus may be involved
            in cell cycle control. Overexpression of this phosphatase is
            reported to activate the expression of the tumor suppressor gene
            TP53/p53, which leads to G2/M cell cycle arrest and apoptosis.
            Three alternatively spliced transcript variants encoding distinct
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) has an alternate 5' exon, as
            compared to variant 1. It encodes isoform 3, which has a distinct
            and longer N-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097843.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..455
                     /product="protein phosphatase 1A isoform 3"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 1A"
                     /calculated_mol_wt=51235
     Region          96..364
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(106,110..111,133..135,312,355)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Region          358..436
                     /region_name="PP2C_C"
                     /note="Protein serine/threonine phosphatase 2C, C-terminal
                     domain; pfam07830"
                     /db_xref="CDD:429684"
     CDS             1..455
                     /gene="PPM1A"
                     /gene_synonym="PP2C-ALPHA; PP2CA; PP2Calpha"
                     /coded_by="NM_177952.3:99..1466"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45120.1"
                     /db_xref="GeneID:5494"
                     /db_xref="HGNC:HGNC:9275"
                     /db_xref="MIM:606108"
ORIGIN      
        1 mfcsgrkwva eatictklmk rekrrmgkrr akkakreekk kggerrrnek rgnqmkrmce
       61 rkkyetdled qdimgafldk pkmekhnaqg qgnglrygls smqgwrveme dahtaviglp
      121 sgleswsffa vydghagsqv akyccehlld hitnnqdfkg sagapsvenv kngirtgfle
      181 idehmrvmse kkhgadrsgs tavgvlispq htyfincgds rgllcrnrkv hfftqdhkps
      241 nplekeriqn aggsvmiqrv ngslavsral gdfdykcvhg kgpteqlvsp epevhdiers
      301 eeddqfiila cdgiwdvmgn eelcdfvrsr levtddlekv cnevvdtcly kgsrdnmsvi
      361 licfpnapkv speavkkeae ldkylecrve eiikkqgegv pdlvhvmrtl asenipslpp
      421 ggelaskrnv ieavynrlnp yknddtdsts tddmw
//
LOCUS       NP_001335701             238 aa            linear   PRI 20-NOV-2025
DEFINITION  meiotic recombination protein REC114 isoform 2 [Homo sapiens].
ACCESSION   NP_001335701
VERSION     NP_001335701.1
DBSOURCE    REFSEQ: accession NM_001348772.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Xu,S., Zhao,J., Gao,F., Zhang,Y., Luo,J., Zhang,C., Tian,R.,
            Zhi,E., Zhang,J., Bai,F., Sun,H., Zhao,F., Huang,Y., Li,P.,
            Jiang,L., Li,Z., Yao,C. and Zhou,Z.
  TITLE     A bi-allelic REC114 loss-of-function variant causes meiotic arrest
            and nonobstructive azoospermia
  JOURNAL   Clin Genet 105 (4), 440-445 (2024)
   PUBMED   38148155
  REMARK    GeneRIF: A bi-allelic REC114 loss-of-function variant causes
            meiotic arrest and nonobstructive azoospermia.
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Wang,W., Dong,J., Chen,B., Du,J., Kuang,Y., Sun,X., Fu,J., Li,B.,
            Mu,J., Zhang,Z., Zhou,Z., Lin,Z., Wu,L., Yan,Z., Mao,X., Li,Q.,
            He,L., Wang,L. and Sang,Q.
  TITLE     Homozygous mutations in REC114 cause female infertility
            characterised by multiple pronuclei formation and early embryonic
            arrest
  JOURNAL   J Med Genet 57 (3), 187-194 (2020)
   PUBMED   31704776
  REMARK    GeneRIF: Homozygous mutations in REC114 cause female infertility
            characterised by multiple pronuclei formation and early embryonic
            arrest.
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Ueta,M., Sawai,H., Shingaki,R., Kawai,Y., Sotozono,C., Kojima,K.,
            Yoon,K.C., Kim,M.K., Seo,K.Y., Joo,C.K., Nagasaki,M., Kinoshita,S.
            and Tokunaga,K.
  TITLE     Genome-wide association study using the ethnicity-specific Japonica
            array: identification of new susceptibility loci for cold
            medicine-related Stevens-Johnson syndrome with severe ocular
            complications
  JOURNAL   J Hum Genet 62 (4), 485-489 (2017)
   PUBMED   28100913
  REMARK    GeneRIF: In Japanese individuals, combined genotyping for the
            associated variants thus far identified; that is, HLA-A*02:06, TLR3
            rs3775296 T/T and Rec114 rs16957893 CG, may help to predict the
            risk for cold medicine-related Stevens-Johnson syndrome /TEN with
            severe ocular complications
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Stanzione,M., Baumann,M., Papanikos,F., Dereli,I., Lange,J.,
            Ramlal,A., Trankner,D., Shibuya,H., de Massy,B., Watanabe,Y.,
            Jasin,M., Keeney,S. and Toth,A.
  TITLE     Meiotic DNA break formation requires the unsynapsed chromosome
            axis-binding protein IHO1 (CCDC36) in mice
  JOURNAL   Nat Cell Biol 18 (11), 1208-1220 (2016)
   PUBMED   27723721
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Kumar,R., Bourbon,H.M. and de Massy,B.
  TITLE     Functional conservation of Mei4 for meiotic DNA double-strand break
            formation from yeasts to mice
  JOURNAL   Genes Dev 24 (12), 1266-1280 (2010)
   PUBMED   20551173
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK131030.1 and BX113903.1.
            
            Summary: The protein encoded by this gene is orthologous to the
            mouse meiotic recombination protein REC114, which is involved in
            DNA double-strand break formation during meiosis. The encoded
            protein is conserved in most eukaryotes and was first discovered
            and characterized in yeast. [provided by RefSeq, Feb 2017].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131030.1, SRR5189667.338973.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..238
                     /product="meiotic recombination protein REC114 isoform 2"
                     /note="meiotic recombination protein REC114-like"
                     /calculated_mol_wt=25846
     Region          21..233
                     /region_name="REC114-like"
                     /note="Meiotic recombination protein REC114-like;
                     pfam15165"
                     /db_xref="CDD:464541"
     CDS             1..238
                     /gene="REC114"
                     /gene_synonym="C15orf60; CT147; OOMD10; OZEMA10"
                     /coded_by="NM_001348772.2:23..739"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86474.1"
                     /db_xref="GeneID:283677"
                     /db_xref="HGNC:HGNC:25065"
                     /db_xref="MIM:618421"
ORIGIN      
        1 maeagkvpls lgltggeaae wplqryarci psntrdppgp cleagtapcp twkvfdsnee
       61 sgylvltivi sghffifqgq tlldksrlfr vqfsgeskeq alehccscvq klaqyitvqv
      121 pdgniqelql ipgpprates qgkdsaksvp rqpgshqhse qqqvcvtagt gapdgrtslt
      181 qlaqtllase elphvyeqsa wgaeelgpfl rlclmdqnfp afveevekel kklaglrn
//
LOCUS       NP_001280133             833 aa            linear   PRI 20-NOV-2025
DEFINITION  major vault protein isoform 2 [Homo sapiens].
ACCESSION   NP_001280133
VERSION     NP_001280133.1
DBSOURCE    REFSEQ: accession NM_001293204.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Li,C., Gao,M., Zha,N. and Guo,G.
  TITLE     The prognostic value and immunological role of MVP in pan-cancer
            study
  JOURNAL   Aging (Albany NY) 16 (10), 8497-8510 (2024)
   PUBMED   38713157
  REMARK    GeneRIF: The prognostic value and immunological role of MVP in
            pan-cancer study.
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Taube,M., Lisiak,N., Toton,E. and Rubis,B.
  TITLE     Human Vault RNAs: Exploring Their Potential Role in Cellular
            Metabolism
  JOURNAL   Int J Mol Sci 25 (7), 4072 (2024)
   PUBMED   38612882
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Yu,C., Zhu,Q., Ma,C., Luo,C., Nie,L., Cai,H., Wang,Q., Wang,F.,
            Ren,H., Yan,H., Xu,K., Zhou,L., Zhang,C., Lu,G., Lu,Z., Zhu,Y. and
            Liu,S.
  TITLE     Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6
  JOURNAL   Front Immunol 14, 1289795 (2024)
   PUBMED   38264642
  REMARK    GeneRIF: Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Holzmann,K., Ambrosch,I., Elbling,L., Micksche,M. and Berger,W.
  TITLE     A small upstream open reading frame causes inhibition of human
            major vault protein expression from a ubiquitous mRNA splice
            variant
  JOURNAL   FEBS Lett 494 (1-2), 99-104 (2001)
   PUBMED   11297743
  REMARK    GeneRIF: MVP gene expression regulated by alternative splicing due
            to generation of an upstream open reading frame
REFERENCE   6  (residues 1 to 833)
  AUTHORS   Dingemans,A.M., van Ark-Otte,J., van der Valk,P., Apolinario,R.M.,
            Scheper,R.J., Postmus,P.E. and Giaccone,G.
  TITLE     Expression of the human major vault protein LRP in human lung
            cancer samples and normal lung tissues
  JOURNAL   Ann Oncol 7 (6), 625-630 (1996)
   PUBMED   8879378
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Schroeijers,A.B., van
            der Valk,P. and Scheper,R.J.
  TITLE     Major vault protein LRP-related multidrug resistance
  JOURNAL   Eur J Cancer 32A (6), 979-984 (1996)
   PUBMED   8763338
  REMARK    Review article
REFERENCE   8  (residues 1 to 833)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Giaccone,G.,
            Broxterman,H.J., Meijer,C.J., van der Valk,P. and Scheper,R.J.
  TITLE     Broad distribution of the multidrug resistance-related vault lung
            resistance protein in normal human tissues and tumors
  JOURNAL   Am J Pathol 148 (3), 877-887 (1996)
   PUBMED   8774142
REFERENCE   9  (residues 1 to 833)
  AUTHORS   Slovak,M.L., Ho,J.P., Cole,S.P., Deeley,R.G., Greenberger,L., de
            Vries,E.G., Broxterman,H.J., Scheffer,G.L. and Scheper,R.J.
  TITLE     The LRP gene encoding a major vault protein associated with drug
            resistance maps proximal to MRP on chromosome 16: evidence that
            chromosome breakage plays a key role in MRP or LRP gene
            amplification
  JOURNAL   Cancer Res 55 (19), 4214-4219 (1995)
   PUBMED   7671223
REFERENCE   10 (residues 1 to 833)
  AUTHORS   Scheffer,G.L., Wijngaard,P.L., Flens,M.J., Izquierdo,M.A.,
            Slovak,M.L., Pinedo,H.M., Meijer,C.J., Clevers,H.C. and
            Scheper,R.J.
  TITLE     The drug resistance-related protein LRP is the human major vault
            protein
  JOURNAL   Nat Med 1 (6), 578-582 (1995)
   PUBMED   7585126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ291366.1, KJ534886.1 and
            BM999583.1.
            
            Summary: This gene encodes the major component of the vault
            complex. Vaults are multi-subunit ribonucleoprotein structures that
            may be involved in nucleo-cytoplasmic transport. The encoded
            protein may play a role in multiple cellular processes by
            regulating the MAP kinase, JAK/STAT and phosphoinositide
            3-kinase/Akt signaling pathways. The encoded protein also plays a
            role in multidrug resistance, and expression of this gene may be a
            prognostic marker for several types of cancer. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (3) has an alternate in-frame
            splice junction in the 3' coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KJ534886.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..833
                     /product="major vault protein isoform 2"
                     /note="lung resistance-related protein; testicular
                     secretory protein Li 30"
                     /calculated_mol_wt=92418
     Region          4..790
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     CDS             1..833
                     /gene="MVP"
                     /gene_synonym="LRP; VAULT1"
                     /coded_by="NM_001293204.1:36..2537"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:9961"
                     /db_xref="HGNC:HGNC:7531"
                     /db_xref="MIM:605088"
ORIGIN      
        1 mateefiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapmrm vtvpprhyct
       61 vanpvsrdaq glvlfdvtgq vrlrhadlei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkdgdkvvag dewlfegpgt yiprkevevv eiiqatiirq nqalrlrark
      181 ecwdrdgker vtgeewlvtt vgaylpavfe evldlvdavi ltektalhlr arrnfrdfrg
      241 vsrrtgeewl vtvqdteahv pdvheevlgv vpittlgphn ycvildpvgp dgknqlgqkr
      301 vvkgeksffl qpgeqleqgi qdvyvlseqq glllralqpl eegedeekvs hqagdhwlir
      361 gpleyvpsak vevveerqai pldenegiyv qdvktgkvra vigstymltq devlwekelp
      421 pgveellnkg qdpladrgek dtakslqpla prnktrvvsy rvphnaavqv ydyrekrarv
      481 vfgpelvslg peeqftvlsl sagrpkrpha rralclllgp dfftdvitie tadharlqlq
      541 laynwhfevn drkdpqetak lfsvpdfvgd ackaiasrvr gavasvtfdd fhknsariir
      601 tavfgfetse akgpdgmalp rprdqavfpq nglvvssvdv qsvepvdqrt rdalqrsvql
      661 aieittnsqe aaakheaqrl eqeargrler qkildqseae karkellele alsmavestg
      721 takaeaesra eaariegegs vlqantirdl avagpemqvk llqslglkst litdgstpin
      781 lfntafgllg mgpegqplgr rvasgpspge gispqsaqap qapgdnhvvp vlr
//
LOCUS       NP_001352601            1128 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001352601
VERSION     NP_001352601.1
DBSOURCE    REFSEQ: accession NM_001365672.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1128)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1128)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1128)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1128)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1128)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1128)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1128)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.151553.1,
                                           SRR1660803.161661.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652658.2/ ENSP00000498242.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1128
                     /product="cordon-bleu protein-like 1 isoform 4"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=123737
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          60..126
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          144..222
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          249..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          291..296
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          325..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          360..365
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          454..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          780..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          <789..1026
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          882..964
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          995..1081
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1077..1102
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1081..1082,1084..1086,1088..1090,1098..1101)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1098..1101
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     Region          1103..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     CDS             1..1128
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001365672.2:165..3551"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS63045.1"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mdgrtprpqd aparrkpkak aplppaetky tdvssaadsv estafimeqk enmidkdvel
       61 svvlpgdiik sttvhgskpm mdlliflcaq yhlnpssyti dllsaeqnhi kfkpntpigm
      121 levekvilkp kmldkkkptp iipektvrvv infkktqkti vrvsphaslq elapiicskc
      181 efdplhtlll kdyqsqepld ltkslndlgl relyamdvnr escqisqnld imkekenkgf
      241 fsffqrskkk rdqtasapat plvnkhrptf trsntiskpy isntlpsdap kkrraplppm
      301 pasqsvpqdl ahiqerpasc ivksmsvdet dkspceagrv ragslqlssm sagnsslrrt
      361 krkapsppsk ipphqsdens rvtalqpvdg vppdsasean speelsspag issdysleei
      421 dekeelsevp kveaenispk sqdipfvstd iintlkndpd salgngsgef sqnsmeekqe
      481 tkstdgqeph svvydtsngk kvvdsirnlk slgpnqenvv qneiivypen tednmkngvk
      541 kteinvegva knnnidmeve rpsnseahet dtaisykenh laassvpdqk lnqpsaektk
      601 daaiqttpsc nsfdgkhqdh nlsdskveec vqtsnnnist qhsclssqds vntsrefrsq
      661 gtliihsedp ltvkdpicah gnddllppvd ridknstasy lknyplyrqd ynpkpkpsne
      721 itreyipkig mttykivppk sleiskdwqs etieykddqd mhalgkkhth envketaiqt
      781 edsaisespe eplpnlkpkp nlrtehqvps svsspddamv splkpapkmt rdtgtapfap
      841 nleeinnile skfksrasna qakpssfflq mqkrvsghyv tsaaaksvha apnpapkelt
      901 nkeaerdmlp speqtlspls kmphsvpqpl vektdddvig qapaeasppp iapkpvtipa
      961 sqvstqnlkt lktfgaprpy sssgpspfal avvkrsqsfs kertespsas alvqppante
     1021 egkthsvnkf vdipqlgvsd kennsahneq nsqiptptdg psftvmrqss ltfqssdpeq
     1081 mrqslltair sgeaaaklkr vtipsntisv ngrsrlshsm spdaqdgh
//
LOCUS       NP_002706                309 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A catalytic subunit alpha
            isoform isoform 1 [Homo sapiens].
ACCESSION   NP_002706
VERSION     NP_002706.1
DBSOURCE    REFSEQ: accession NM_002715.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Mao,H., Ye,R., Tang,G., Tao,S., Wei,K., Wu,Y., Pang,S., Wang,J.,
            Shi,J., Ji,Y., Xiao,Y., Geng,C., Wang,W., Chen,C. and Yang,Q.
  TITLE     Drug-resistant exosome miR-99b-3p induces macrophage polarization
            and confers chemoresistance on sensitive cells by targeting PPP2CA
  JOURNAL   Int Immunopharmacol 142 (Pt B), 113168 (2024)
   PUBMED   39298813
  REMARK    GeneRIF: Drug-resistant exosome miR-99b-3p induces macrophage
            polarization and confers chemoresistance on sensitive cells by
            targeting PPP2CA.
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Liang,X., Zhang,H., Shang,W., Wang,M., Li,J., Zhao,Y. and Fang,C.
  TITLE     PPP2CA Inhibition Promotes Ferroptosis Sensitivity Through
            AMPK/SCD1 Pathway in Colorectal Cancer
  JOURNAL   Dig Dis Sci 69 (6), 2083-2095 (2024)
   PUBMED   38637456
  REMARK    GeneRIF: PPP2CA Inhibition Promotes Ferroptosis Sensitivity Through
            AMPK/SCD1 Pathway in Colorectal Cancer.
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Goedert,M., Cohen,E.S., Jakes,R. and Cohen,P.
  TITLE     p42 MAP kinase phosphorylation sites in microtubule-associated
            protein tau are dephosphorylated by protein phosphatase 2A1.
            Implications for Alzheimer's disease [corrected]
  JOURNAL   FEBS Lett 312 (1), 95-99 (1992)
   PUBMED   1330687
  REMARK    Erratum:[FEBS Lett 1992 Nov 23;313(2):203]
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Ruediger,R., Roeckel,D., Fait,J., Bergqvist,A., Magnusson,G. and
            Walter,G.
  TITLE     Identification of binding sites on the regulatory A subunit of
            protein phosphatase 2A for the catalytic C subunit and for tumor
            antigens of simian virus 40 and polyomavirus
  JOURNAL   Mol Cell Biol 12 (11), 4872-4882 (1992)
   PUBMED   1328865
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Kamibayashi,C., Lickteig,R.L., Estes,R., Walter,G. and Mumby,M.C.
  TITLE     Expression of the A subunit of protein phosphatase 2A and
            characterization of its interactions with the catalytic and
            regulatory subunits
  JOURNAL   J Biol Chem 267 (30), 21864-21872 (1992)
   PUBMED   1328247
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Scheidtmann,K.H., Virshup,D.M. and Kelly,T.J.
  TITLE     Protein phosphatase 2A dephosphorylates simian virus 40 large T
            antigen specifically at residues involved in regulation of
            DNA-binding activity
  JOURNAL   J Virol 65 (4), 2098-2101 (1991)
   PUBMED   1848320
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Khew-Goodall,Y., Mayer,R.E., Maurer,F., Stone,S.R. and
            Hemmings,B.A.
  TITLE     Structure and transcriptional regulation of protein phosphatase 2A
            catalytic subunit genes
  JOURNAL   Biochemistry 30 (1), 89-97 (1991)
   PUBMED   1846293
  REMARK    Erratum:[Biochemistry 1991 May 28;30(21):5328]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104109.3 and AK097599.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the phosphatase 2A catalytic subunit.
            Protein phosphatase 2A is one of the four major Ser/Thr
            phosphatases, and it is implicated in the negative control of cell
            growth and division. It consists of a common heteromeric core
            enzyme, which is composed of a catalytic subunit and a constant
            regulatory subunit, that associates with a variety of regulatory
            subunits. This gene encodes an alpha isoform of the catalytic
            subunit. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.26971.1,
                                           SRR11853559.26465.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267764 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000481195.6/ ENSP00000418447.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..309
                     /product="serine/threonine-protein phosphatase 2A
                     catalytic subunit alpha isoform isoform 1"
                     /EC_number="3.1.3.16"
                     /note="PP2A-alpha; replication protein C; protein
                     phosphatase 2, catalytic subunit, alpha isozyme"
                     /calculated_mol_wt=35463
     Region          9..293
                     /region_name="MPP_PP2A_PP4_PP6"
                     /note="PP2A, PP4, and PP6 phosphoprotein phosphatases,
                     metallophosphatase domain; cd07415"
                     /db_xref="CDD:277360"
     Site            order(51,67,70..71,73..74,76,78..79,91,106..110,121..122,
                     125..126,130..131,134..135,143,268,277,287,293)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:277360"
     Site            order(57,59,85,89,117..118,122..123,127,167,189..191,200,
                     213..215,241,243,267..269)
                     /site_type="active"
                     /db_xref="CDD:277360"
     Site            order(57,59,85,117,167,241)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277360"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P67774; propagated from
                     UniProtKB/Swiss-Prot (P67775.1)"
     Site            309
                     /site_type="methylation"
                     /note="Leucine methyl ester.
                     /evidence=ECO:0000269|PubMed:38123684,
                     ECO:0000269|PubMed:8206937, ECO:0007744|PDB:8SO0,
                     ECO:0007744|PDB:8TTB; propagated from UniProtKB/Swiss-Prot
                     (P67775.1)"
     CDS             1..309
                     /gene="PPP2CA"
                     /gene_synonym="HJS3; NEDLBA; PP2Ac; PP2CA; PP2Calpha;
                     RP-C"
                     /coded_by="NM_002715.4:213..1142"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4173.1"
                     /db_xref="GeneID:5515"
                     /db_xref="HGNC:HGNC:9299"
                     /db_xref="MIM:176915"
ORIGIN      
        1 mdekvftkel dqwieqlnec kqlsesqvks lcekakeilt kesnvqevrc pvtvcgdvhg
       61 qfhdlmelfr iggkspdtny lfmgdyvdrg yysvetvtll valkvryrer itilrgnhes
      121 rqitqvygfy declrkygna nvwkyftdlf dylpltalvd gqifclhggl spsidtldhi
      181 raldrlqevp hegpmcdllw sdpddrggwg isprgagytf gqdisetfnh angltlvsra
      241 hqlvmegynw chdrnvvtif sapnycyrcg nqaaimeldd tlkysflqfd paprrgephv
      301 trrtpdyfl
//
LOCUS       NP_054722               1227 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16 [Homo
            sapiens].
ACCESSION   NP_054722
VERSION     NP_054722.2
DBSOURCE    REFSEQ: accession NM_014003.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1227)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1227)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1227)
  AUTHORS   Mi,K., Zeng,L., Chen,Y., Ning,J., Zhang,S., Zhao,P. and Yang,S.
  TITLE     DHX38 enhances proliferation, metastasis, and EMT progression in
            NSCLC through the G3BP1-mediated MAPK pathway
  JOURNAL   Cell Signal 113, 110962 (2024)
   PUBMED   37931691
  REMARK    GeneRIF: DHX38 enhances proliferation, metastasis, and EMT
            progression in NSCLC through the G3BP1-mediated MAPK pathway.
REFERENCE   4  (residues 1 to 1227)
  AUTHORS   Li,Z., Qin,C., Zhao,B., Wang,Y., Li,T., Zhao,Y. and Wang,W.
  TITLE     DHX38 restricts chemoresistance by regulating the alternative
            pre-mRNA splicing of RELL2 in pancreatic ductal adenocarcinoma
  JOURNAL   PLoS Genet 19 (7), e1010847 (2023)
   PUBMED   37506056
  REMARK    GeneRIF: DHX38 restricts chemoresistance by regulating the
            alternative pre-mRNA splicing of RELL2 in pancreatic ductal
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1227)
  AUTHORS   Obuca,M., Cvackova,Z., Kubovciak,J., Kolar,M. and Stanek,D.
  TITLE     Retinitis pigmentosa-linked mutation in DHX38 modulates its
            splicing activity
  JOURNAL   PLoS One 17 (4), e0265742 (2022)
   PUBMED   35385551
  REMARK    GeneRIF: Retinitis pigmentosa-linked mutation in DHX38 modulates
            its splicing activity.
            Erratum:[PLoS One. 2023 Jan 20;18(1):e0280904. doi:
            10.1371/journal.pone.0280904. PMID: 36662708]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1227)
  AUTHORS   Wang,Y. and Guthrie,C.
  TITLE     PRP16, a DEAH-box RNA helicase, is recruited to the spliceosome
            primarily via its nonconserved N-terminal domain
  JOURNAL   RNA 4 (10), 1216-1229 (1998)
   PUBMED   9769096
REFERENCE   7  (residues 1 to 1227)
  AUTHORS   Zhou,Z. and Reed,R.
  TITLE     Human homologs of yeast prp16 and prp17 reveal conservation of the
            mechanism for catalytic step II of pre-mRNA splicing
  JOURNAL   EMBO J 17 (7), 2095-2106 (1998)
   PUBMED   9524131
REFERENCE   8  (residues 1 to 1227)
  AUTHORS   Gee,S., Krauss,S.W., Miller,E., Aoyagi,K., Arenas,J. and
            Conboy,J.G.
  TITLE     Cloning of mDEAH9, a putative RNA helicase and mammalian homologue
            of Saccharomyces cerevisiae splicing factor Prp43
  JOURNAL   Proc Natl Acad Sci U S A 94 (22), 11803-11807 (1997)
   PUBMED   9342318
REFERENCE   9  (residues 1 to 1227)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 1227)
  AUTHORS   Schwer,B. and Guthrie,C.
  TITLE     PRP16 is an RNA-dependent ATPase that interacts transiently with
            the spliceosome
  JOURNAL   Nature 349 (6309), 494-499 (1991)
   PUBMED   1825134
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG719187.1, BM473438.1,
            BC008340.1 and AA126451.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 30, 2001 this sequence version replaced NP_054722.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. The protein encoded by this gene is a
            member of the DEAD/H box family of splicing factors. This protein
            resembles yeast Prp16 more closely than other DEAD/H family
            members. It is an ATPase and essential for the catalytic step II in
            pre-mRNA splicing process. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.261139.1,
                                           SRR1660809.36002.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268482.8/ ENSP00000268482.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.2"
     Protein         1..1227
                     /product="pre-mRNA-splicing factor ATP-dependent RNA
                     helicase PRP16"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 38;
                     PRP16 homolog of S.cerevisiae; DEAH box protein 38;
                     ATP-dependent RNA helicase DHX38; DEAH (Asp-Glu-Ala-His)
                     box polypeptide 38; pre-mRNA processing factor 16"
                     /calculated_mol_wt=140372
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Region          60..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92620.2)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     Region          532..>1146
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          652..655
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92620.2)"
     Region          1155..1227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92620.2)"
     Site            1194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92620.2)"
     CDS             1..1227
                     /gene="DHX38"
                     /gene_synonym="DDX38; PRP16; PRPF16; RP84"
                     /coded_by="NM_014003.4:225..3908"
                     /db_xref="CCDS:CCDS10907.1"
                     /db_xref="GeneID:9785"
                     /db_xref="HGNC:HGNC:17211"
                     /db_xref="MIM:605584"
ORIGIN      
        1 mgdtsedasi hrlegtdldc qvgglicksk saaseqhvfk apaprpsllg ldllaslkrr
       61 ereekddged kkkskvssyk dweeskddqk daeeeggdqa gqnirkdrhy rsarvetpsh
      121 pggvseefwe rsrqrererr ehgvyasske ekdwkkeksr drdydrkrdr derdrsrhss
      181 rserdggser ssrrnepesp rhrpkdaatp srstweeeds gygssrrsqw espsptpsyr
      241 dsershrlst rdrdrsvrgk ysddtplptp sykynewadd rrhlgstprl srgrgrreeg
      301 eegisfdtee erqqweddqr qadrdwymmd egydefhnpl ayssedyvrr reqhlhkqkq
      361 krisaqrrqi nednerwetn rmltsgvvhr levdedfeed naakvhlmvh nlvppfldgr
      421 ivftkqpepv ipvkdatsdl aiiarkgsqt vrkhreqker kkaqhkhwel agtklgdimg
      481 vkkeeepdka vtedgkvdyr teqkfadhmk rkseassefa kkksileqrq ylpifavqqe
      541 lltiirdnsi vivvgetgsg kttqltqylh edgytdygmi gctqprrvaa msvakrvsee
      601 mggnlgeevg yairfedcts entlikymtd gillreslre adldhysaii mdeahersln
      661 tdvlfgllre vvarrsdlkl ivtsatmdae kfaaffgnvp ifhipgrtfp vdilfsktpq
      721 edyveaavkq slqvhlsgap gdilifmpgq edievtsdqi vehleelena palavlpiys
      781 qlpsdlqaki fqkapdgvrk civatniaet sltvdgimfv idsgycklkv fnprigmdal
      841 qiypisqana nqrsgragrt gpgqcfrlyt qsayknellt ttvpeiqrtn lanvvlllks
      901 lgvqdllqfh fmdpppednm lnsmyqlwil galdntgglt stgrlmvefp ldpalskmli
      961 vscdmgcsse illivsmlsv paifyrpkgr eeesdqirek favpesdhlt ylnvylqwkn
     1021 nnystiwcnd hfihakamrk vrevraqlkd imvqqrmsla scgtdwdivr kcicaayfhq
     1081 aaklkgigey vnirtgmpch lhptsslfgm gytpdyivyh elvmttkeym qcvtavdgew
     1141 laelgpmfys vkqagksrqe nrrrakeeas ameeemalae eqlrarrqeq ekrsplgsvr
     1201 stkiytpgrk eqgepmtprr tparfgl
//
LOCUS       NP_000738                501 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholine receptor subunit beta precursor [Homo sapiens].
ACCESSION   NP_000738
VERSION     NP_000738.2
DBSOURCE    REFSEQ: accession NM_000747.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Chia,R., Saez-Atienzar,S., Drachman,D.B. and Traynor,B.J.
  TITLE     Reply to Zhu et al.: Implications of CHRNB1 and ERBB2 in the
            pathobiology of myasthenia gravis
  JOURNAL   Proc Natl Acad Sci U S A 119 (36), e2209096119 (2022)
   PUBMED   35969799
  REMARK    GeneRIF: Reply to Zhu et al.: Implications of CHRNB1 and ERBB2 in
            the pathobiology of myasthenia gravis.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Freed,A.S., Schwarz,A.C., Brei,B.K., Clowes Candadai,S.V.,
            Thies,J., Mah,J.K., Chabra,S., Wang,L., Innes,A.M. and Bennett,J.T.
  TITLE     CHRNB1-associated congenital myasthenia syndrome: Expanding the
            clinical spectrum
  JOURNAL   Am J Med Genet A 185 (3), 827-835 (2021)
   PUBMED   33296147
  REMARK    GeneRIF: CHRNB1-associated congenital myasthenia syndrome:
            Expanding the clinical spectrum.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Aishah,A., Hinton,T. and Machaalani,R.
  TITLE     Cellular protein and mRNA expression of beta1 nicotinic
            acetylcholine receptor (nAChR) subunit in brain, skeletal muscle
            and placenta
  JOURNAL   Int J Dev Neurosci 58, 9-16 (2017)
   PUBMED   28153524
  REMARK    GeneRIF: This study reports on the presence of the CHRNB1 at the
            cellular level in human skeletal muscle and placenta and that mRNA
            expression mirrors that of protein within cell types.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Shen,X.M., Okuno,T., Milone,M., Otsuka,K., Takahashi,K., Komaki,H.,
            Giles,E., Ohno,K. and Engel,A.G.
  TITLE     Mutations Causing Slow-Channel Myasthenia Reveal That a Valine Ring
            in the Channel Pore of Muscle AChR is Optimized for Stabilizing
            Channel Gating
  JOURNAL   Hum Mutat 37 (10), 1051-1059 (2016)
   PUBMED   27375219
  REMARK    GeneRIF: Study traced the cause of congenital myasthenia syndrome
            in unrelated patients with dominant missense mutations in the M2
            domain of AChR. A valine residue is replaced by a smaller alanine
            either in the epsilon subunit or an equivalent position in the beta
            one. Also, each valine in the valine ring was found to contribute
            to channel kinetics equally, and the valine ring has bee optimized
            during evolution to govern channe...
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Ohno,K., Hutchinson,D.O., Milone,M., Brengman,J.M., Bouzat,C.,
            Sine,S.M. and Engel,A.G.
  TITLE     Congenital myasthenic syndrome caused by prolonged acetylcholine
            receptor channel openings due to a mutation in the M2 domain of the
            epsilon subunit
  JOURNAL   Proc Natl Acad Sci U S A 92 (3), 758-762 (1995)
   PUBMED   7531341
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Beeson,D., Jeremiah,S., West,L.F., Povey,S. and Newsom-Davis,J.
  TITLE     Assignment of the human nicotinic acetylcholine receptor genes: the
            alpha and delta subunit genes to chromosome 2 and the beta subunit
            gene to chromosome 17
  JOURNAL   Ann Hum Genet 54 (3), 199-208 (1990)
   PUBMED   2221824
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Beeson,D., Brydson,M. and Newsom-Davis,J.
  TITLE     Nucleotide sequence of human muscle acetylcholine receptor
            beta-subunit
  JOURNAL   Nucleic Acids Res 17 (11), 4391 (1989)
   PUBMED   2740233
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Kraus,H.
  TITLE     Research methods in the biomechanics of sports
  JOURNAL   Orthop Clin North Am 8 (3), 549-562 (1977)
   PUBMED   887246
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113189.11, BC023553.2 and
            BC011371.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 26, 2004 this sequence version replaced NP_000738.1.
            
            Summary: The muscle acetylcholine receptor is composed of five
            subunits: two alpha subunits and one beta, one gamma, and one delta
            subunit. This gene encodes the beta subunit of the acetylcholine
            receptor. The acetylcholine receptor changes conformation upon
            acetylcholine binding leading to the opening of an ion-conducting
            channel across the plasma membrane. Mutations in this gene are
            associated with slow-channel congenital myasthenic syndrome.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023553.2, AK308106.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306071.7/ ENSP00000304290.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..501
                     /product="acetylcholine receptor subunit beta precursor"
                     /note="cholinergic receptor, nicotinic, beta polypeptide 1
                     (muscle); cholinergic receptor, nicotinic beta 1;
                     acetylcholine receptor subunit beta; acetylcholine
                     receptor, nicotinic, beta 1 (muscle); cholinergic
                     receptor, nicotinic, beta 1 (muscle)"
                     /calculated_mol_wt=54540
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2177
     mat_peptide     24..501
                     /product="acetylcholine receptor subunit beta"
                     /calculated_mol_wt=54540
     Region          27..245
                     /region_name="LGIC_ECD_nAChR_B1"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit beta 1 (CHRNB1); cd19024"
                     /db_xref="CDD:349825"
     Site            order(62,64,70..71,78,100,102,111..112,114,116..117,121,
                     123..124,128..130,132,142,144,146,150,172,244)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349825"
     Region          151..165
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349825"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P11230.3)"
     Site            245..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11230.3)"
     Region          252..487
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            277..295
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11230.3)"
     Site            311..332
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11230.3)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by Tyr-kinases.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P11230.3)"
     Site            470..488
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11230.3)"
     CDS             1..501
                     /gene="CHRNB1"
                     /gene_synonym="ACHRB; CHRNB; CMS1D; CMS2A; CMS2C; SCCMS"
                     /coded_by="NM_000747.3:68..1573"
                     /db_xref="CCDS:CCDS11106.1"
                     /db_xref="GeneID:1140"
                     /db_xref="HGNC:HGNC:1961"
                     /db_xref="MIM:100710"
ORIGIN      
        1 mtpgallmll galgaplapg vrgseaegrl reklfsgyds svrparevgd rvrvsvglil
       61 aqlislnekd eemstkvyld lewtdyrlsw dpaehdgids lritaesvwl pdvvllnnnd
      121 gnfdvaldis vvvssdgsvr wqppgiyrss csiqvtyfpf dwqnctmvfs sysydssevs
      181 lqtglgpdgq ghqeihiheg tfiengqwei ihkpsrliqp pgdprggreg qrqevifyli
      241 irrkplfylv nviapcilit llaifvfylp pdagekmgls ifalltltvf lllladkvpe
      301 tslsvpiiik ylmftmvlvt fsvilsvvvl nlhhrsphth qmplwvrqif ihklplylrl
      361 krpkperdlm pepphcsspg sgwgrgtdey firkppsdfl fpkpnrfqpe lsapdlrrfi
      421 dgpnravall pelrevvssi syiarqlqeq edhdalkedw qfvamvvdrl flwtfiifts
      481 vgtlviflda tyhlpppdpf p
//
LOCUS       NP_005518                641 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock 70 kDa protein 1-like [Homo sapiens].
ACCESSION   NP_005518
VERSION     NP_005518.3
DBSOURCE    REFSEQ: accession NM_005527.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Ochoa-Ramirez,L.A., Diaz-Camacho,S.P., Mellado-Corrales,S.N.,
            Munoz-Estrada,V.F., Rios-Tostado,J.J., Sanchez-Zazueta,J.G. and
            Velarde-Felix,J.S.
  TITLE     Analysis of the heat shock protein 70 (HSP70) genetic variants in
            nonsegmental vitiligo patients
  JOURNAL   Int J Dermatol 62 (2), 225-230 (2023)
   PUBMED   36345598
  REMARK    GeneRIF: Analysis of the heat shock protein 70 (HSP70) genetic
            variants in nonsegmental vitiligo patients.
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Liu,X., Teng,Z., Wang,Z., Zhu,P., Song,Z. and Liu,F.
  TITLE     Expressions of HSPA1L and HSPA9 are associated with poor sperm
            quality of low-motility spermatozoa in fertile men
  JOURNAL   Andrologia 54 (2), e14321 (2022)
   PUBMED   34796524
  REMARK    GeneRIF: Expressions of HSPA1L and HSPA9 are associated with poor
            sperm quality of low-motility spermatozoa in fertile men.
REFERENCE   4  (residues 1 to 641)
  AUTHORS   Huusko,J.M., Tiensuu,H., Haapalainen,A.M., Pasanen,A.,
            Tissarinen,P., Karjalainen,M.K., Zhang,G., Christensen,K.,
            Ryckman,K.K., Jacobsson,B., Murray,J.C., Kingsmore,S.F.,
            Hallman,M., Muglia,L.J. and Ramet,M.
  TITLE     Integrative genetic, genomic and transcriptomic analysis of heat
            shock protein and nuclear hormone receptor gene associations with
            spontaneous preterm birth
  JOURNAL   Sci Rep 11 (1), 17115 (2021)
   PUBMED   34429451
  REMARK    GeneRIF: Integrative genetic, genomic and transcriptomic analysis
            of heat shock protein and nuclear hormone receptor gene
            associations with spontaneous preterm birth.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 641)
  AUTHORS   Nakatsuka,A., Yamaguchi,S., Eguchi,J., Kakuta,S., Iwakura,Y.,
            Sugiyama,H. and Wada,J.
  TITLE     A Vaspin-HSPA1L complex protects proximal tubular cells from
            organelle stress in diabetic kidney disease
  JOURNAL   Commun Biol 4 (1), 373 (2021)
   PUBMED   33742129
  REMARK    GeneRIF: A Vaspin-HSPA1L complex protects proximal tubular cells
            from organelle stress in diabetic kidney disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 641)
  AUTHORS   Milner,C.M. and Campbell,R.D.
  TITLE     Polymorphic analysis of the three MHC-linked HSP70 genes
  JOURNAL   Immunogenetics 36 (6), 357-362 (1992)
   PUBMED   1356099
REFERENCE   7  (residues 1 to 641)
  AUTHORS   Milner,C.M. and Campbell,R.D.
  TITLE     Structure and expression of the three MHC-linked HSP70 genes
  JOURNAL   Immunogenetics 32 (4), 242-251 (1990)
   PUBMED   1700760
REFERENCE   8  (residues 1 to 641)
  AUTHORS   Sargent,C.A., Dunham,I., Trowsdale,J. and Campbell,R.D.
  TITLE     Human major histocompatibility complex contains genes for the major
            heat shock protein HSP70
  JOURNAL   Proc Natl Acad Sci U S A 86 (6), 1968-1972 (1989)
   PUBMED   2538825
REFERENCE   9  (residues 1 to 641)
  AUTHORS   Harrison,G.S., Drabkin,H.A., Kao,F.T., Hartz,J., Hart,I.M.,
            Chu,E.H., Wu,B.J. and Morimoto,R.I.
  TITLE     Chromosomal location of human genes encoding major heat-shock
            protein HSP70
  JOURNAL   Somat Cell Mol Genet 13 (2), 119-130 (1987)
   PUBMED   3470951
REFERENCE   10 (residues 1 to 641)
  AUTHORS   Goate,A.M., Cooper,D.N., Hall,C., Leung,T.K., Solomon,E. and Lim,L.
  TITLE     Localization of a human heat-shock HSP 70 gene sequence to
            chromosome 6 and detection of two other loci by somatic-cell hybrid
            and restriction fragment length polymorphism analysis
  JOURNAL   Hum Genet 75 (2), 123-128 (1987)
   PUBMED   2880793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL671762.10, BG717447.1,
            D85730.1, BC034483.1, M59829.1, CA443193.1 and BX115051.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 29, 2007 this sequence version replaced NP_005518.2.
            
            Summary: This gene encodes a 70kDa heat shock protein. In
            conjunction with other heat shock proteins, this protein stabilizes
            existing proteins against aggregation and mediates the folding of
            newly translated proteins in the cytosol and in organelles. The
            gene is located in the major histocompatibility complex class III
            region, in a cluster with two closely related genes which also
            encode isoforms of the 70kDa heat shock protein. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295416.1, SRR1803615.268463.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            MANE Ensembl match               :: ENST00000375654.5/
                                                ENSP00000364805.4
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..641
                     /product="heat shock 70 kDa protein 1-like"
                     /note="heat shock 70kD protein-like 1; heat shock 10kDa
                     protein 1-like; epididymis secretory sperm binding
                     protein; heat shock 70 kDa protein 1L; heat shock 70 kDa
                     protein 1-Hom; heat shock 70kDa protein 1-like; heat shock
                     protein family A member 1L"
                     /calculated_mol_wt=70244
     Region          3..388
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P34931.2)"
     Region          4..641
                     /region_name="PTZ00009"
                     /note="heat shock 70 kDa protein; Provisional"
                     /db_xref="CDD:240227"
     Region          396..511
                     /region_name="Substrate-binding domain (SBD).
                     /evidence=ECO:0000250|UniProtKB:P11142"
                     /note="propagated from UniProtKB/Swiss-Prot (P34931.2)"
     CDS             1..641
                     /gene="HSPA1L"
                     /gene_synonym="HSP70-1L; HSP70-HOM; HSP70T; hum70t"
                     /coded_by="NM_005527.4:409..2334"
                     /db_xref="CCDS:CCDS34413.1"
                     /db_xref="GeneID:3305"
                     /db_xref="HGNC:HGNC:5234"
                     /db_xref="MIM:140559"
ORIGIN      
        1 matakgiaig idlgttyscv gvfqhgkvei iandqgnrtt psyvaftdte rligdaaknq
       61 vamnpqntvf dakrligrkf ndpvvqadmk lwpfqvineg gkpkvlvsyk genkafypee
      121 issmvltklk etaeaflghp vtnavitvpa yfndsqrqat kdagviagln vlriinepta
      181 aaiaygldkg gqgerhvlif dlgggtfdvs iltiddgife vkatagdthl ggedfdnrlv
      241 shfveefkrk hkkdisqnkr avrrlrtace rakrtlssst qanleidsly egidfytsit
      301 rarfeelcad lfrgtlepve kalrdakmdk akihdivlvg gstripkvqr llqdyfngrd
      361 lnksinpdea vaygaavqaa ilmgdksekv qdlllldvap lslgletagg vmtalikrns
      421 tiptkqtqif ttysdnqpgv liqvyegera mtkdnnllgr fdltgippap rgvpqievtf
      481 didangilnv tatdkstgkv nkititndkg rlskeeierm vldaekykae devqrekiaa
      541 knalesyafn mksvvsdegl kgkisesdkn kildkcnell swlevnqlae kdefdhkrke
      601 leqmcnpiit klyqggctgp acgtgyvpgr patgptieev d
//
LOCUS       NP_001229885             401 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-7 isoform 3 [Homo sapiens].
ACCESSION   NP_001229885
VERSION     NP_001229885.1
DBSOURCE    REFSEQ: accession NM_001242956.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Cavini,I.A., Winter,A.J., D'Muniz Pereira,H., Woolfson,D.N.,
            Crump,M.P. and Garratt,R.C.
  TITLE     X-ray structure of the metastable SEPT14-SEPT7 coiled coil reveals
            a hendecad region crucial for heterodimerization
  JOURNAL   Acta Crystallogr D Struct Biol 79 (Pt 10), 881-894 (2023)
   PUBMED   37712436
  REMARK    GeneRIF: X-ray structure of the metastable SEPT14-SEPT7 coiled coil
            reveals a hendecad region crucial for heterodimerization.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Fischer,M., Frank,D., Rosler,R., Johnsson,N. and Gronemeyer,T.
  TITLE     Biochemical Characterization of a Human Septin Octamer
  JOURNAL   Front Cell Dev Biol 10, 771388 (2022)
   PUBMED   35309913
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Zhu,M., Wang,F., Yan,F., Yao,P.Y., Du,J., Gao,X., Wang,X., Wu,Q.,
            Ward,T., Li,J., Kioko,S., Hu,R., Xie,W., Ding,X. and Yao,X.
  TITLE     Septin 7 interacts with centromere-associated protein E and is
            required for its kinetochore localization
  JOURNAL   J Biol Chem 283 (27), 18916-18925 (2008)
   PUBMED   18460473
  REMARK    GeneRIF: SEPT7 forms a link between kinetochore distribution of
            CENP-E and the mitotic spindle checkpoint.
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Surka,M.C., Tsang,C.W. and Trimble,W.S.
  TITLE     The mammalian septin MSF localizes with microtubules and is
            required for completion of cytokinesis
  JOURNAL   Mol Biol Cell 13 (10), 3532-3545 (2002)
   PUBMED   12388755
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Joberty,G., Perlungher,R.R., Sheffield,P.J., Kinoshita,M., Noda,M.,
            Haystead,T. and Macara,I.G.
  TITLE     Borg proteins control septin organization and are negatively
            regulated by Cdc42
  JOURNAL   Nat Cell Biol 3 (10), 861-866 (2001)
   PUBMED   11584266
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Oegema,K., Savoian,M.S., Mitchison,T.J. and Field,C.M.
  TITLE     Functional analysis of a human homologue of the Drosophila actin
            binding protein anillin suggests a role in cytokinesis
  JOURNAL   J Cell Biol 150 (3), 539-552 (2000)
   PUBMED   10931866
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Hsu,S.C., Hazuka,C.D., Roth,R., Foletti,D.L., Heuser,J. and
            Scheller,R.H.
  TITLE     Subunit composition, protein interactions, and structures of the
            mammalian brain sec6/8 complex and septin filaments
  JOURNAL   Neuron 20 (6), 1111-1122 (1998)
   PUBMED   9655500
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Nakatsuru,S., Sudo,K. and Nakamura,Y.
  TITLE     Molecular cloning of a novel human cDNA homologous to CDC10 in
            Saccharomyces cerevisiae
  JOURNAL   Biochem Biophys Res Commun 202 (1), 82-87 (1994)
   PUBMED   8037772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC414394.1, AC007551.1,
            AK297883.1, AC087072.2 and AI651908.1.
            
            Summary: This gene encodes a protein that is highly similar to the
            CDC10 protein of Saccharomyces cerevisiae. The protein also shares
            similarity with Diff 6 of Drosophila and with H5 of mouse. Each of
            these similar proteins, including the yeast CDC10, contains a
            GTP-binding motif. The yeast CDC10 protein is a structural
            component of the 10 nm filament which lies inside the cytoplasmic
            membrane and is essential for cytokinesis. This human protein
            functions in gliomagenesis and in the suppression of glioma cell
            growth, and it is required for the association of
            centromere-associated protein E with the kinetochore. Alternative
            splicing results in multiple transcript variants. Several related
            pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11,
            14, 17 and 19. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (3) lacks an in-frame segment in
            the 5' coding region, compared to variant 1, resulting in an
            isoform (3) that is 36 aa shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.65774.1,
                                           SRR1803612.191628.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.2"
     Protein         1..401
                     /product="septin-7 isoform 3"
                     /note="CDC10 (cell division cycle 10, S. cerevisiae,
                     homolog); CDC10 protein homolog"
                     /calculated_mol_wt=46435
     Region          21..281
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            21..28
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(23..29,77,80,158..159,161,214..215)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            52..60
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            54
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Site            77..80
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(79..114,115..124)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            158..161
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            214..216
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Region          301..>397
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     CDS             1..401
                     /gene="SEPTIN7"
                     /gene_synonym="CDC10; CDC3; NBLA02942; SEPT7; SEPT7A;
                     Septin-7"
                     /coded_by="NM_001242956.1:225..1430"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75582.1"
                     /db_xref="GeneID:989"
                     /db_xref="HGNC:HGNC:1717"
                     /db_xref="MIM:603151"
ORIGIN      
        1 msvsarsaaa eersvnsstm gesglgkstl inslfltdly speypgpshr ikktvqveqs
       61 kvlikeggvq llltivdtpg fgdavdnsnc wqpvidyids kfedylnaes rvnrrqmpdn
      121 rvqcclyfia psghglkpld iefmkrlhek vniipliaka dtltpeecqq fkkqimkeiq
      181 ehkikiyefp etddeeenkl vkkikdrlpl avvgsntiie vngkrvrgrq ypwgvaeven
      241 gehcdftilr nmlirthmqd lkdvtnnvhy enyrsrklaa vtyngvdnnk nkgqltkspl
      301 aqmeeerreh vakmkkmeme meqvfemkvk ekvqklkdse aelqrrheqm kknleaqhke
      361 leekrrqfed ekanweaqqr ileqqnssrt leknkkkgki f
//
LOCUS       NP_001128526             410 aa            linear   PRI 20-NOV-2025
DEFINITION  single Ig IL-1-related receptor [Homo sapiens].
ACCESSION   NP_001128526
VERSION     NP_001128526.1
DBSOURCE    REFSEQ: accession NM_001135054.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Mariotti,F.R., Supino,D., Landolina,N., Garlanda,C., Mantovani,A.,
            Moretta,L. and Maggi,E.
  TITLE     IL-1R8: A molecular brake of anti-tumor and anti-viral activity of
            NK cells and ILC
  JOURNAL   Semin Immunol 66, 101712 (2023)
   PUBMED   36753974
  REMARK    GeneRIF: IL-1R8: A molecular brake of anti-tumor and anti-viral
            activity of NK cells and ILC.
            Review article
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yu,W., Haque,I., Venkatraman,A., Menden,H.L., Mabry,S.M., Roy,B.C.,
            Xia,S., Prokop,J.W., Umar,S., Geurts,A.M. and Sampath,V.
  TITLE     SIGIRR Mutation in Human Necrotizing Enterocolitis (NEC) Disrupts
            STAT3-Dependent microRNA Expression in Neonatal Gut
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (2), 425-440 (2022)
   PUBMED   34563711
  REMARK    GeneRIF: SIGIRR Mutation in Human Necrotizing Enterocolitis (NEC)
            Disrupts STAT3-Dependent microRNA Expression in Neonatal Gut.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Jia,C., Zhuge,Y., Zhang,S., Ni,C., Wang,L., Wu,R., Niu,C., Wen,Z.,
            Rong,X., Qiu,H. and Chu,M.
  TITLE     IL-37b alleviates endothelial cell apoptosis and inflammation in
            Kawasaki disease through IL-1R8 pathway
  JOURNAL   Cell Death Dis 12 (6), 575 (2021)
   PUBMED   34083516
  REMARK    GeneRIF: IL-37b alleviates endothelial cell apoptosis and
            inflammation in Kawasaki disease through IL-1R8 pathway.
            Erratum:[Cell Death Dis. 2021 Aug 2;12(8):759. doi:
            10.1038/s41419-021-04044-5. PMID: 34341339]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Yang,X., Zhang,M., Xu,S., Pan,H., Leng,R. and Shuai,Z.
  TITLE     Single Immunoglobulin IL-1-Related Receptor (SIGIRR) Gene rs7396562
            Polymorphism and Expression Level in Rheumatoid Arthritis
  JOURNAL   Biomed Res Int 2021, 6683148 (2021)
   PUBMED   34036103
  REMARK    GeneRIF: Single Immunoglobulin IL-1-Related Receptor (SIGIRR) Gene
            rs7396562 Polymorphism and Expression Level in Rheumatoid
            Arthritis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Cavalli,G., Tengesdal,I.W., Gresnigt,M., Nemkov,T., Arts,R.J.W.,
            Dominguez-Andres,J., Molteni,R., Stefanoni,D., Cantoni,E.,
            Cassina,L., Giugliano,S., Schraa,K., Mills,T.S., Pietras,E.M.,
            Eisenmensser,E.Z., Dagna,L., Boletta,A., D'Alessandro,A.,
            Joosten,L.A.B., Netea,M.G. and Dinarello,C.A.
  TITLE     The anti-inflammatory cytokine interleukin-37 is an inhibitor of
            trained immunity
  JOURNAL   Cell Rep 35 (1), 108955 (2021)
   PUBMED   33826894
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Polentarutti,N., Rol,G.P., Muzio,M., Bosisio,D., Camnasio,M.,
            Riva,F., Zoja,C., Benigni,A., Tomasoni,S., Vecchi,A., Garlanda,C.
            and Mantovani,A.
  TITLE     Unique pattern of expression and inhibition of IL-1 signaling by
            the IL-1 receptor family member TIR8/SIGIRR
  JOURNAL   Eur Cytokine Netw 14 (4), 211-218 (2003)
   PUBMED   14715412
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Wald,D., Qin,J., Zhao,Z., Qian,Y., Naramura,M., Tian,L., Towne,J.,
            Sims,J.E., Stark,G.R. and Li,X.
  TITLE     SIGIRR, a negative regulator of Toll-like receptor-interleukin 1
            receptor signaling
  JOURNAL   Nat Immunol 4 (9), 920-927 (2003)
   PUBMED   12925853
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Du,X., Poltorak,A., Wei,Y. and Beutler,B.
  TITLE     Three novel mammalian toll-like receptors: gene structure,
            expression, and evolution
  JOURNAL   Eur Cytokine Netw 11 (3), 362-371 (2000)
   PUBMED   11022119
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Thomassen,E., Renshaw,B.R. and Sims,J.E.
  TITLE     Identification and characterization of SIGIRR, a molecule
            representing a novel subtype of the IL-1R superfamily
  JOURNAL   Cytokine 11 (6), 389-399 (1999)
   PUBMED   10346978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB112269.1, AK172830.1, BX369506.2 and AK025099.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC106007.1, SRR14038196.2424677.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431843.7/ ENSP00000403104.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..410
                     /product="single Ig IL-1-related receptor"
                     /note="single Ig IL-1R-related molecule; single
                     immunoglobulin domain IL1R1 related; toll/interleukin-1
                     receptor 8; single immunoglobulin domain-containing
                     IL1R-related protein; single immunoglobulin and
                     toll-interleukin 1 receptor (TIR) domain"
                     /calculated_mol_wt=45548
     Region          9..>66
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          28..32
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          46..50
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          80..87
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          95..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          168..311
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          340..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IA17.3)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     CDS             1..410
                     /gene="SIGIRR"
                     /gene_synonym="IL-1R8; TIR8"
                     /coded_by="NM_001135054.2:331..1563"
                     /db_xref="CCDS:CCDS31325.1"
                     /db_xref="GeneID:59307"
                     /db_xref="HGNC:HGNC:30575"
                     /db_xref="MIM:605478"
ORIGIN      
        1 mpgvcdrapd flspsedqvl rpalgssval nctawvvsgp hcslpsvqwl kdglplgigg
       61 hyslheyswv kanlsevlvs svlgvnvtst evygaftcsi qnisfssftl qragptshva
      121 avlasllvll alllaallyv kcrlnvllwy qdaygevein dgklydayvs ysdcpedrkf
      181 vnfilkpqle rrrgyklfld drdllpraep sadllvnlsr crrlivvlsd aflsrawcsh
      241 sfreglcrll eltrrpifit fegqrrdpah palrllrqhr hlvtlllwrp gsvtpssdfw
      301 kevqlalprk vqyrpvegdp qtqlqddkdp mlilrgrvpe graldsevdp dpegdlgvrg
      361 pvfgepsapp htsgvslges rssevdvsdl gsrnysartd fyclvskddm
//
LOCUS       NP_060383                337 aa            linear   PRI 20-NOV-2025
DEFINITION  hsp90 co-chaperone Cdc37-like 1 [Homo sapiens].
ACCESSION   NP_060383
VERSION     NP_060383.2
DBSOURCE    REFSEQ: accession NM_017913.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Peak,S.L., Gracia,L., Lora,G. and Jinwal,U.K.
  TITLE     Hsp90-interacting Co-chaperones and their Family Proteins in Tau
            Regulation: Introducing a Novel Role for Cdc37L1
  JOURNAL   Neuroscience 453, 312-323 (2021)
   PUBMED   33246057
  REMARK    Review article
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Cartledge,K., Elsegood,C., Roiniotis,J., Hamilton,J.A. and
            Scholz,G.M.
  TITLE     Importance of the C-terminal domain of Harc for binding to Hsp70
            and Hop as well as its response to heat shock
  JOURNAL   Biochemistry 46 (51), 15144-15152 (2007)
   PUBMED   18052042
  REMARK    GeneRIF: C-terminal domain of Harc is a key determinant of its
            cochaperone functions
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Roiniotis,J., Masendycz,P., Ho,S. and Scholz,G.M.
  TITLE     Domain-mediated dimerization of the Hsp90 cochaperones Harc and
            Cdc37
  JOURNAL   Biochemistry 44 (17), 6662-6669 (2005)
   PUBMED   15850399
  REMARK    GeneRIF: Harc forms dimers in vitro. The structural similarities
            between Harc and Cdc37 suggest that Harc may function to regulate
            the Hsp90-mediated folding of Cdc37-dependent protein kinases into
            functional conformations via dimerization with Cdc37.
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Scholz,G.M., Cartledge,K. and Hall,N.E.
  TITLE     Identification and characterization of Harc, a novel
            Hsp90-associating relative of Cdc37
  JOURNAL   J Biol Chem 276 (33), 30971-30979 (2001)
   PUBMED   11413142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA180237.1, BC014133.2 and AL136231.12.
            
            On May 27, 2005 this sequence version replaced NP_060383.1.
            
            Summary: CDC37L1 is a cytoplasmic phosphoprotein that exists in
            complex with HSP90 (HSPCA; MIM 140571) as well as several other
            proteins involved in HSP90-mediated protein folding (Scholz et al.,
            2001 [PubMed 11413142]).[supplied by OMIM, Mar 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.420111.1,
                                           SRR1660803.3552.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381854.4/ ENSP00000371278.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.1"
     Protein         1..337
                     /product="hsp90 co-chaperone Cdc37-like 1"
                     /note="CDC37 cell division cycle 37 homolog-like 1;
                     Hsp90-associating relative of Cdc37; cell division cycle
                     37 like 1"
                     /calculated_mol_wt=38704
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Region          2..171
                     /region_name="Self-association"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Region          <71..139
                     /region_name="CDC37_N"
                     /note="Cdc37 N terminal kinase binding; cl03951"
                     /db_xref="CDD:446243"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Region          138..282
                     /region_name="CDC37_M"
                     /note="Cdc37 Hsp90 binding domain; smart01070"
                     /db_xref="CDD:215010"
     Region          147..277
                     /region_name="Self-association and interaction with Hsp90"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Region          267..337
                     /region_name="Interaction with Hsp70"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L3B6.1)"
     Region          278..337
                     /region_name="Required for interaction with STIP1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L3B6.1)"
     CDS             1..337
                     /gene="CDC37L1"
                     /gene_synonym="CDC37B; HARC"
                     /coded_by="NM_017913.4:200..1213"
                     /db_xref="CCDS:CCDS6454.1"
                     /db_xref="GeneID:55664"
                     /db_xref="HGNC:HGNC:17179"
                     /db_xref="MIM:610346"
ORIGIN      
        1 meqpwpppgp wslpraegea eeesdfdvfp ssprcpqlpg ggaqmyshgi elacqkqkef
       61 vkssvackwn laeaqqklgs lalhnsesld qehakaqtav selrqreeew rqkeealvqr
      121 ekmclwstda iskdvfnksf inqdkrkdte dedksesfmq kyeqkirhfg mlsrwddsqr
      181 flsdhpylvc eetakylilw cfhleaekkg almeqiahqa vvmqfimema kncnvdprgc
      241 frlffqkaka eeegyfeafk neleafksrv rlysqsqsfq pmtvqnhvph sgvgsiglle
      301 slpqnpdylq ysistalcsl nsvvhkedde pkmmdtv
//
LOCUS       NP_001166289             580 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoglucomutase-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001166289
VERSION     NP_001166289.1
DBSOURCE    REFSEQ: accession NM_001172818.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Liu,S., Deng,Y., Yu,Y. and Xia,X.
  TITLE     Knock-down of PGM1 inhibits cell viability, glycolysis, and
            oxidative phosphorylation in glioma under low glucose condition via
            the Myc signaling pathway
  JOURNAL   Biochem Biophys Res Commun 656, 38-45 (2023)
   PUBMED   36947965
  REMARK    GeneRIF: Knock-down of PGM1 inhibits cell viability, glycolysis,
            and oxidative phosphorylation in glioma under low glucose condition
            via the Myc signaling pathway.
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Stiers,K.M., Owuocha,L.F. and Beamer,L.J.
  TITLE     Effects of the T337M and G391V disease-related variants on human
            phosphoglucomutase 1: structural disruptions large and small
  JOURNAL   Acta Crystallogr F Struct Biol Commun 78 (Pt 5), 200-209 (2022)
   PUBMED   35506765
  REMARK    GeneRIF: Effects of the T337M and G391V disease-related variants on
            human phosphoglucomutase 1: structural disruptions large and small.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Beamer,L.J.
  TITLE     Enzyme dysfunction at atomic resolution: Disease-associated
            variants of human phosphoglucomutase-1
  JOURNAL   Biochimie 183, 44-48 (2021)
   PUBMED   32898648
  REMARK    GeneRIF: Enzyme dysfunction at atomic resolution:
            Disease-associated variants of human phosphoglucomutase-1.
            Review article
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Conte,F., Morava,E., Bakar,N.A., Wortmann,S.B., Poerink,A.J.,
            Grunewald,S., Crushell,E., Al-Gazali,L., de Vries,M.C., Morkrid,L.,
            Hertecant,J., Brocke Holmefjord,K.S., Kronn,D., Feigenbaum,A.,
            Fingerhut,R., Wong,S.Y., van Scherpenzeel,M., Voermans,N.C. and
            Lefeber,D.J.
  TITLE     Phosphoglucomutase-1 deficiency: Early presentation, metabolic
            management and detection in neonatal blood spots
  JOURNAL   Mol Genet Metab 131 (1-2), 135-146 (2020)
   PUBMED   33342467
  REMARK    GeneRIF: Phosphoglucomutase-1 deficiency: Early presentation,
            metabolic management and detection in neonatal blood spots.
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Backe,P.H., Laerdahl,J.K., Kittelsen,L.S., Dalhus,B., Morkrid,L.
            and Bjoras,M.
  TITLE     Structural basis for substrate and product recognition in human
            phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily
  JOURNAL   Sci Rep 10 (1), 5656 (2020)
   PUBMED   32221390
  REMARK    GeneRIF: Structural basis for substrate and product recognition in
            human phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Whitehouse,D.B., Putt,W., Lovegrove,J.U., Morrison,K.,
            Hollyoake,M., Fox,M.F., Hopkinson,D.A. and Edwards,Y.H.
  TITLE     Phosphoglucomutase 1: complete human and rabbit mRNA sequences and
            direct mapping of this highly polymorphic marker on human
            chromosome 1
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 411-415 (1992)
   PUBMED   1530890
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Drago,G.A., Hopkinson,D.A., Westwood,S.A. and Whitehouse,D.B.
  TITLE     Antigenic analysis of the major human phosphoglucomutase isozymes:
            PGM1, PGM2, PGM3 and PGM4
  JOURNAL   Ann Hum Genet 55 (4), 263-271 (1991)
   PUBMED   1840235
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Herbich,J., Szilvassy,J. and Schnedl,W.
  TITLE     Gene localisation of the PGM1 enzyme system and the Duffy blood
            groups on chromosome No. 1 by means of a new fragile site at 1p31
  JOURNAL   Hum Genet 70 (2), 178-180 (1985)
   PUBMED   3159642
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC373587.1, AK300100.1 and
            BC019920.1.
            
            Summary: The protein encoded by this gene is an isozyme of
            phosphoglucomutase (PGM) and belongs to the phosphohexose mutase
            family. There are several PGM isozymes, which are encoded by
            different genes and catalyze the transfer of phosphate between the
            1 and 6 positions of glucose. In most cell types, this PGM isozyme
            is predominant, representing about 90% of total PGM activity. In
            red cells, PGM2 is a major isozyme. This gene is highly
            polymorphic. Mutations in this gene cause glycogen storage disease
            type 14. Alternativley spliced transcript variants encoding
            different isoforms have been identified in this gene.[provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2) has an alternate 5' exon, as
            compared to variant 1. The resulting isoform (2) has a longer and
            different N-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.99027.1, AK300100.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..580
                     /product="phosphoglucomutase-1 isoform 2"
                     /EC_number="5.4.2.2"
                     /note="PGM 1; glucose phosphomutase 1"
                     /calculated_mol_wt=63660
     Region          24..580
                     /region_name="PGM1"
                     /note="Phosphoglucomutase 1 (PGM1) catalyzes the
                     bidirectional interconversion of glucose-1-phosphate
                     (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose
                     1,6-diphosphate intermediate, an important metabolic step
                     in prokaryotes and eukaryotes. In one direction; cd03085"
                     /db_xref="CDD:100087"
     Site            order(38,135,311,354,375,377,394,396,398,521,523..525,533)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100087"
     Site            order(65..66,71..72,125,151..153,385)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:100087"
     Site            order(135..137,306,308,310..311,377,407,521,523..525,533)
                     /site_type="active"
                     /db_xref="CDD:100087"
     Site            order(135,306,308,310)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100087"
     CDS             1..580
                     /gene="PGM1"
                     /gene_synonym="CDG1T; GSD14"
                     /coded_by="NM_001172818.1:246..1988"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53323.1"
                     /db_xref="GeneID:5236"
                     /db_xref="HGNC:HGNC:8905"
                     /db_xref="MIM:171900"
ORIGIN      
        1 msdfeewisg tyrkmeegpl plltfatapy hdqkpgtsgl rkktyyfeek pcylenfiqs
       61 iffsidlkdr qgsslvvggd gryfnksaie tivqmaaang igrlvigqng ilstpavsci
      121 irkikaiggi iltashnpgg pngdfgikfn isnggpapea itdkifqisk tieeyavcpd
      181 lkvdlgvlgk qqfdlenkfk pftveivdsv eayatmlrsi fdfsalkell sgpnrlkiri
      241 damhgvvgpy vkkilceelg apansavncv pledfgghhp dpnltyaadl vetmksgehd
      301 fgaafdgdgd rnmilgkhgf fvnpsdsvav iaanifsipy fqqtgvrgfa rsmptsgald
      361 rvasatkial yetptgwkff gnlmdaskls lcgeesfgtg sdhirekdgl wavlawlsil
      421 atrkqsvedi lkdhwqkygr nfftrydyee veaegankmm kdlealmfdr sfvgkqfsan
      481 dkvytvekad nfeysdpvdg sisrnqglrl iftdgsrivf rlsgtgsaga tirlyidsye
      541 kdvakinqdp qvmlaplisi alkvsqlqer tgrtaptvit
//
LOCUS       NP_001340539             309 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform m [Homo sapiens].
ACCESSION   NP_001340539 XP_016877033
VERSION     NP_001340539.1
DBSOURCE    REFSEQ: accession NM_001353610.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877033.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.245485.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..309
                     /product="lysosomal cobalamin transporter ABCD4 isoform m"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=33466
     Region          <1..239
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     Region          124..>218
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            158..165
                     /site_type="other"
                     /note="Walker A/P-loop"
                     /db_xref="CDD:213190"
     Site            195..198
                     /site_type="other"
                     /note="Q-loop/lid"
                     /db_xref="CDD:213190"
     CDS             1..309
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353610.2:717..1646"
                     /note="isoform m is encoded by transcript variant 25"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mrslllstvg intfdylgsi lsyvviaipi fsgvygdlsp aelstlvskn afvciylisc
       61 ftqlidlstt lsdvagythr igqlretlld mslksqdcei lgesewgldt ppgwpaaepa
      121 dtafllervs isapssdkpl ikdlslkise gqsllitgnt gtgktsllrv lgglwtstrg
      181 svqmltdfgp hgvlflpqkp fftdgtlreq viyplkevyp dsgsadderi lrflelaglv
      241 sgerdpqdps ppgstsyspt wwqgqrawts rwtgtgmmfc prgrcngspl pdsstcsrst
      301 qclmkppvp
//
LOCUS       NP_002361                146 aa            linear   PRI 20-NOV-2025
DEFINITION  protein mago nashi homolog [Homo sapiens].
ACCESSION   NP_002361
VERSION     NP_002361.1
DBSOURCE    REFSEQ: accession NM_002370.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Yu,S., Chen,C., Chen,M., Liang,J., Jiang,K., Lou,B., Lu,J., Zhu,X.
            and Zhou,D.
  TITLE     MAGOH promotes gastric cancer progression via hnRNPA1 expression
            inhibition-mediated RONDelta160/PI3K/AKT signaling pathway
            activation
  JOURNAL   J Exp Clin Cancer Res 43 (1), 32 (2024)
   PUBMED   38268030
  REMARK    GeneRIF: MAGOH promotes gastric cancer progression via hnRNPA1
            expression inhibition-mediated RONDelta160/PI3K/AKT signaling
            pathway activation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Xiao,F., Long,Z., Guo,Y., Zhu,H., Zhang,Z., Xiao,Y., Hu,G.,
            Yang,Q., Huang,K. and Guo,H.
  TITLE     MAGOH is correlated with poor prognosis and is essential for cell
            proliferation in lower-grade glioma
  JOURNAL   Aging (Albany NY) 15 (12), 5713-5733 (2023)
   PUBMED   37390121
  REMARK    GeneRIF: MAGOH is correlated with poor prognosis and is essential
            for cell proliferation in lower-grade glioma.
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Pacheco-Fiallos,B., Vorlander,M.K., Riabov-Bassat,D., Fin,L.,
            O'Reilly,F.J., Ayala,F.I., Schellhaas,U., Rappsilber,J. and
            Plaschka,C.
  TITLE     mRNA recognition and packaging by the human transcription-export
            complex
  JOURNAL   Nature 616 (7958), 828-835 (2023)
   PUBMED   37020021
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Soederberg,A., Meissgeier,T., Bosserhoff,A.K. and Linck-Paulus,L.
  TITLE     MAGOH and MAGOHB Knockdown in Melanoma Cells Decreases
            Nonsense-Mediated Decay Activity and Promotes Apoptosis via
            Upregulation of GADD45A
  JOURNAL   Cells 11 (23), 3859 (2022)
   PUBMED   36497117
  REMARK    GeneRIF: MAGOH and MAGOHB Knockdown in Melanoma Cells Decreases
            Nonsense-Mediated Decay Activity and Promotes Apoptosis via
            Upregulation of GADD45A.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Le Hir,H., Gatfield,D., Izaurralde,E. and Moore,M.J.
  TITLE     The exon-exon junction complex provides a binding platform for
            factors involved in mRNA export and nonsense-mediated mRNA decay
  JOURNAL   EMBO J 20 (17), 4987-4997 (2001)
   PUBMED   11532962
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Mingot,J.M., Kostka,S., Kraft,R., Hartmann,E. and Gorlich,D.
  TITLE     Importin 13: a novel mediator of nuclear import and export
  JOURNAL   EMBO J 20 (14), 3685-3694 (2001)
   PUBMED   11447110
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Zhao,X.F., Nowak,N.J., Shows,T.B. and Aplan,P.D.
  TITLE     MAGOH interacts with a novel RNA-binding protein
  JOURNAL   Genomics 63 (1), 145-148 (2000)
   PUBMED   10662555
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Zhao,X.F., Colaizzo-Anas,T., Nowak,N.J., Shows,T.B., Elliott,R.W.
            and Aplan,P.D.
  TITLE     The mammalian homologue of mago nashi encodes a serum-inducible
            protein
  JOURNAL   Genomics 47 (2), 319-322 (1998)
   PUBMED   9479507
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Newmark,P.A., Mohr,S.E., Gong,L. and Boswell,R.E.
  TITLE     mago nashi mediates the posterior follicle cell-to-oocyte signal to
            organize axis formation in Drosophila
  JOURNAL   Development 124 (16), 3197-3207 (1997)
   PUBMED   9272960
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF067173.1 and AF035940.1.
            
            Summary: Drosophila that have mutations in their mago nashi
            (grandchildless) gene produce progeny with defects in germplasm
            assembly and germline development. This gene encodes the mammalian
            mago nashi homolog. In mammals, mRNA expression is not limited to
            the germ plasm, but is expressed ubiquitously in adult tissues and
            can be induced by serum stimulation of quiescent fibroblasts.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279835.4540.1, BU533022.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371470.8/ ENSP00000360525.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..146
                     /product="protein mago nashi homolog"
                     /note="mago-nashi homolog, proliferation-associated; mago
                     homolog, exon junction complex core component"
                     /calculated_mol_wt=17033
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P61326.1)"
     Region          4..146
                     /region_name="Mago_nashi"
                     /note="Mago nashi proteins, integral members of the exon
                     junction complex; cd11295"
                     /db_xref="CDD:199917"
     Site            order(11..13,17,20..21,34,36..38,40..44,46,48,83,103,
                     105..107,123,127,130..131,134,142..146)
                     /site_type="other"
                     /note="eIF4AIII interface [polypeptide binding]"
                     /db_xref="CDD:199917"
     Site            order(11..17,20..21,29,34,36..38,40..44,46,48,51..53,
                     55..56,59,62..63,103,105..107,123..124,127..128,130..132,
                     134..136,139..145)
                     /site_type="other"
                     /note="exon junction core complex interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:199917"
     Site            order(13..17,40..41,82..83,103)
                     /site_type="other"
                     /note="Barentsz interface [polypeptide binding]"
                     /db_xref="CDD:199917"
     Site            order(14,45,47..49,59,62,68,71,75,95,141)
                     /site_type="other"
                     /note="Imp13 interface [polypeptide binding]"
                     /db_xref="CDD:199917"
     Site            order(29,51..53,55..56,59,62..63,124,127..128,131..132,
                     135..136,139..142)
                     /site_type="other"
                     /note="Y14 interface [polypeptide binding]"
                     /db_xref="CDD:199917"
     Site            order(66,68,107)
                     /site_type="other"
                     /note="Upf3b interface [polypeptide binding]"
                     /db_xref="CDD:199917"
     CDS             1..146
                     /gene="MAGOH"
                     /gene_synonym="MAGOH1; MAGOHA"
                     /coded_by="NM_002370.4:71..511"
                     /db_xref="CCDS:CCDS577.1"
                     /db_xref="GeneID:4116"
                     /db_xref="HGNC:HGNC:6815"
                     /db_xref="MIM:602603"
ORIGIN      
        1 mesdfylryy vghkgkfghe flefefrpdg klryannsny kndvmirkea yvhksvmeel
       61 kriiddseit keddalwppp drvgrqelei vigdehisft tskigslidv nqskdpeglr
      121 vfyylvqdlk clvfsliglh fkikpi
//
LOCUS       NP_001351612             248 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.5cy [Homo sapiens].
ACCESSION   NP_001351612
VERSION     NP_001351612.1
DBSOURCE    REFSEQ: accession NM_001364683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 248)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 248)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 248)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590431.11.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.242840.1,
                                           SRR1163658.418535.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..248
                     /product="tropomyosin alpha-3 chain isoform Tpm3.5cy"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=28791
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001364683.1:100..846"
                     /note="isoform Tpm3.5cy is encoded by transcript variant
                     17"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 magittieav krkiqvlqqq addaeeraer lqrevegerr areqaeaeva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienralk deekmelqei qlkeakhiae
      121 eadrkyeeva rklviiegdl erteeraela esrcremdeq irlmdqnlkc lsaaeekysq
      181 kedkyeeeik iltdklkeae traefaersv aklektiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_002046                432 aa            linear   PRI 20-NOV-2025
DEFINITION  glial fibrillary acidic protein isoform 1 [Homo sapiens].
ACCESSION   NP_002046
VERSION     NP_002046.1
DBSOURCE    REFSEQ: accession NM_002055.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Shetty,D., Brahmbhatt,S., Desai,A., Bathla,G., Mohan,S., Gupta,V.,
            Soni,N., Vibhute,P. and Agarwal,A.
  TITLE     Glial Fibrillary Acidic Protein Astrocytopathy: Review of
            Pathogenesis, Imaging Features, and Radiographic Mimics
  JOURNAL   AJNR Am J Neuroradiol 45 (10), 1394-1402 (2024)
   PUBMED   38844367
  REMARK    GeneRIF: Glial Fibrillary Acidic Protein Astrocytopathy: Review of
            Pathogenesis, Imaging Features, and Radiographic Mimics.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Lin,N.H., Jian,W.S., Snider,N. and Perng,M.D.
  TITLE     Glial fibrillary acidic protein is pathologically modified in
            Alexander disease
  JOURNAL   J Biol Chem 300 (7), 107402 (2024)
   PUBMED   38782207
  REMARK    GeneRIF: Glial fibrillary acidic protein is pathologically modified
            in Alexander disease.
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Chiperi,L.E. and Hutanu,A.
  TITLE     Glial Fibrillary Acidic Protein: Diagnostic and Prognostic Role in
            Psychomotor Development Dynamics in Patients with Congenital Heart
            Defects after Cardiovascular Surgery
  JOURNAL   Balkan Med J 41 (2), 151-152 (2024)
   PUBMED   38173149
  REMARK    GeneRIF: Glial Fibrillary Acidic Protein: Diagnostic and Prognostic
            Role in Psychomotor Development Dynamics in Patients with
            Congenital Heart Defects after Cardiovascular Surgery.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Yin,P., Niu,X., Guan,C., Zhang,Z., Liu,Y., Li,J., Cui,G., Zan,K.
            and Xu,C.
  TITLE     Relationship between increased serum neurofilament light chain and
            glial fibrillary acidic protein levels with non-motor symptoms in
            patients with Parkinson's disease
  JOURNAL   Psychogeriatrics 24 (2), 415-425 (2024)
   PUBMED   38339819
  REMARK    GeneRIF: Relationship between increased serum neurofilament light
            chain and glial fibrillary acidic protein levels with non-motor
            symptoms in patients with Parkinson's disease.
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Srivastava,S., Waldman,A. and Naidu,S.
  TITLE     Alexander Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301351
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Hatzfeld,M., Dodemont,H., Plessmann,U. and Weber,K.
  TITLE     Truncation of recombinant vimentin by ompT. Identification of a
            short motif in the head domain necessary for assembly of type III
            intermediate filament proteins
  JOURNAL   FEBS Lett 302 (3), 239-242 (1992)
   PUBMED   1601131
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Kumanishi,T., Usui,H., Ichikawa,T., Nishiyama,A., Katagiri,T.,
            Abe,S., Yoshida,Y., Washiyama,K., Kuwano,R., Sakimura,K. et al.
  TITLE     Human glial fibrillary acidic protein (GFAP): molecular cloning of
            the complete cDNA sequence and chromosomal localization (chromosome
            17) of the GFAP gene
  JOURNAL   Acta Neuropathol 83 (6), 569-578 (1992)
   PUBMED   1636374
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Bongcam-Rudloff,E., Nister,M., Betsholtz,C., Wang,J.L., Stenman,G.,
            Huebner,K., Croce,C.M. and Westermark,B.
  TITLE     Human glial fibrillary acidic protein: complementary DNA cloning,
            chromosome localization, and messenger RNA expression in human
            glioma cell lines of various phenotypes
  JOURNAL   Cancer Res 51 (5), 1553-1560 (1991)
   PUBMED   1847665
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA254392.1, BC013596.1,
            J04569.1, AC015936.14 and BF341765.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of the major intermediate filament
            proteins of mature astrocytes. It is used as a marker to
            distinguish astrocytes from other glial cells during development.
            Mutations in this gene cause Alexander disease, a rare disorder of
            astrocytes in the central nervous system. Alternative splicing
            results in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes a predominant isoform (1, also known as
            alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.105676.1,
                                           SRR1660807.9743.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000588735.3/ ENSP00000466598.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..432
                     /product="glial fibrillary acidic protein isoform 1"
                     /calculated_mol_wt=49749
     Region          1..72
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          4..66
                     /region_name="Filament_head"
                     /note="Intermediate filament head (DNA binding) region;
                     pfam04732"
                     /db_xref="CDD:461414"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P03995; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB and ROCK1.
                     /evidence=ECO:0000269|PubMed:12686604,
                     ECO:0000269|PubMed:9099667; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          68..376
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Region          73..104
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          105..115
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          116..214
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          215..230
                     /region_name="Linker 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          231..252
                     /region_name="Coil 2A"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          253..256
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Region          257..377
                     /region_name="Coil 2B"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Region          378..432
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P14136.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     Site            385
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P47819; propagated from
                     UniProtKB/Swiss-Prot (P14136.1)"
     CDS             1..432
                     /gene="GFAP"
                     /gene_synonym="ALXDRD"
                     /coded_by="NM_002055.5:15..1313"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11491.1"
                     /db_xref="GeneID:2670"
                     /db_xref="HGNC:HGNC:4235"
                     /db_xref="MIM:137780"
ORIGIN      
        1 merrritsaa rrsyvssgem mvgglapgrr lgpgtrlsla rmppplptrv dfslagalna
       61 gfketraser aemmelndrf asyiekvrfl eqqnkalaae lnqlrakept kladvyqael
      121 relrlrldql tansarleve rdnlaqdlat vrqklqdetn lrleaennla ayrqeadeat
      181 larldlerki esleeeirfl rkiheeevre lqeqlarqqv hveldvakpd ltaalkeirt
      241 qyeamassnm heaeewyrsk fadltdaaar naellrqakh eandyrrqlq sltcdleslr
      301 gtneslerqm reqeerhvre aasyqealar leeegqslkd emarhlqeyq dllnvklald
      361 ieiatyrkll egeenritip vqtfsnlqir etsldtksvs eghlkrnivv ktvemrdgev
      421 ikeskqehkd vm
//
LOCUS       NP_055722               1578 aa            linear   PRI 20-NOV-2025
DEFINITION  FERM and PDZ domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_055722
VERSION     NP_055722.2
DBSOURCE    REFSEQ: accession NM_014907.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1578)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1578)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1578)
  AUTHORS   Johnson,E.O., Hancock,D.B., Gaddis,N.C., Levy,J.L., Page,G.,
            Novak,S.P., Glasheen,C., Saccone,N.L., Rice,J.P., Moreau,M.P.,
            Doheny,K.F., Romm,J.M., Brooks,A.I., Aouizerat,B.E., Bierut,L.J.
            and Kral,A.H.
  TITLE     Novel genetic locus implicated for HIV-1 acquisition with putative
            regulatory links to HIV replication and infectivity: a genome-wide
            association study
  JOURNAL   PLoS One 10 (3), e0118149 (2015)
   PUBMED   25786224
  REMARK    GeneRIF: G allele at rs4878712 in FRMPD1 was associated with lower
            HIV-1 acquisition. G allele at this SNP was also associated with
            reduced FBXO10 and increased BCL2 expression levels, whereas higher
            BCL2 levels are known to reduce HIV replication and infectivity.
            Erratum:[PLoS One. 2015 May 29;10(5):e0129671. doi:
            10.1371/journal.pone.0129671. PMID: 26023777]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1578)
  AUTHORS   Pan,Z., Shang,Y., Jia,M., Zhang,L., Xia,C., Zhang,M., Wang,W. and
            Wen,W.
  TITLE     Structural and biochemical characterization of the interaction
            between LGN and Frmpd1
  JOURNAL   J Mol Biol 425 (6), 1039-1049 (2013)
   PUBMED   23318951
  REMARK    GeneRIF: LGN-TPR motifs are versatile and capable of recognizing
            multiple targets via diverse binding modes.
REFERENCE   5  (residues 1 to 1578)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   6  (residues 1 to 1578)
  AUTHORS   An,N., Blumer,J.B., Bernard,M.L. and Lanier,S.M.
  TITLE     The PDZ and band 4.1 containing protein Frmpd1 regulates the
            subcellular location of activator of G-protein signaling 3 and its
            interaction with G-proteins
  JOURNAL   J Biol Chem 283 (36), 24718-24728 (2008)
   PUBMED   18566450
  REMARK    GeneRIF: The PDZ and band 4.1 containing protein Frmpd1 regulates
            the subcellular location of activator of G-protein signaling 3 and
            its interaction with G-proteins.
REFERENCE   7  (residues 1 to 1578)
  AUTHORS   Samuelson,D.J., Hesselson,S.E., Aperavich,B.A., Zan,Y., Haag,J.D.,
            Trentham-Dietz,A., Hampton,J.M., Mau,B., Chen,K.S., Baynes,C.,
            Khaw,K.T., Luben,R., Perkins,B., Shah,M., Pharoah,P.D.,
            Dunning,A.M., Easton,D.F., Ponder,B.A. and Gould,M.N.
  TITLE     Rat Mcs5a is a compound quantitative trait locus with orthologous
            human loci that associate with breast cancer risk
  JOURNAL   Proc Natl Acad Sci U S A 104 (15), 6299-6304 (2007)
   PUBMED   17404222
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL513165.12, AB023184.1, AL591470.12 and BX648967.1.
            
            On Jun 9, 2009 this sequence version replaced NP_055722.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB023184.1, SRR1660809.73286.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377765.8/ ENSP00000366995.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..1578
                     /product="FERM and PDZ domain-containing protein 1"
                     /note="FERM domain-containing protein 2"
                     /calculated_mol_wt=173306
     Region          57..132
                     /region_name="PDZ_FRMPD1_3_4-like"
                     /note="PDZ domain of FERM and PDZ domain-containing
                     protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains;
                     cd06769"
                     /db_xref="CDD:467250"
     Site            order(68..74,82,85,113,117,120..121)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467250"
     Region          179..268
                     /region_name="FERM_F1_FRMPD1"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in FERM and PDZ
                     domain-containing protein 1 (FRMPD1); cd17168"
                     /db_xref="CDD:340688"
     Region          182..401
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          397..501
                     /region_name="FERM_C_FRMPD1_FRMPD3_FRMPD4"
                     /note="FERM domain C-lobe of FERM and PDZ domain
                     containing proteins 1, 3, and 4 (FRMPD1, 3, 4); cd13183"
                     /db_xref="CDD:270004"
     Site            order(405,426,428,436)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270004"
     Site            order(440,446..449,482,486,489..490)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Site            482..493
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Region          555..>827
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          555..616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          720..743
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          759..831
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          901..938
                     /region_name="LGNbd_FRMPD1"
                     /note="LGN tetratricopeptide repeat-binding domain found
                     in FERM and PDZ domain-containing protein 1; cd21942"
                     /db_xref="CDD:409273"
     Site            920..933
                     /site_type="other"
                     /note="TPR binding site [polypeptide binding]"
                     /db_xref="CDD:409273"
     Region          924..931
                     /region_name="Important for interaction with GPSM2.
                     /evidence=ECO:0000269|PubMed:23318951"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          950..1030
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          1070..1194
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     Region          1347..1374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SYB0.1)"
     CDS             1..1578
                     /gene="FRMPD1"
                     /gene_synonym="FRMD2"
                     /coded_by="NM_014907.3:146..4882"
                     /db_xref="CCDS:CCDS6612.1"
                     /db_xref="GeneID:22844"
                     /db_xref="HGNC:HGNC:29159"
                     /db_xref="MIM:616919"
ORIGIN      
        1 meeletslfq trkahrieqm varwlrrsrd ssarakvaaa dgparnptqt lipvrhtvki
       61 dkdtllqdyg fhiseslplt vvavtaggsa hgklfpgdqi lqmnnepaed lsweravdil
      121 reaedslsit vvrctsgvpk ssflteekra rlktnpvkvh faeevlisgh sqgnsllcmp
      181 nvlklyleng qtkafkfean ttvkdiiltv keklsirsie yfalaleeqy sisrlhllhe
      241 eeliqqvver eeshdyrclf rvcfvpkdpl dllkedpvaf eylylqscsd vlqerfavem
      301 kcssalrlaa lhiqeriyac aqpqkislky iekdwgienf isptllrnmk gkdikkaisf
      361 hmkrnqnlle prqkqlisaa qlrlnylqil gelktyggri fnatlmlqdr esyiallvga
      421 kygisqvins klnimstlae fanisrvelt eesekvsvvk vylqdvkvlt lllesnsakd
      481 lacliagyyr llvdpvtsif lwpgnkqqah rvsaeegyes racsdseess evdcvlepls
      541 drrlvklapc rslikeeqpp gnsptpevar rgpstcgass ttdsaeseas dsantesrgy
      601 rtsgssesmd aleeddldtc sssrstffhf gspglaesid sdsqeersgi etsgflclld
      661 laqranpqcq ktefsesaal etfgwapels tvrldprlye gshadyyslc ssvspasyls
      721 dssestasrq ggappawgqq gwteaqpssm leplalhppl afedgssdee yydaadkltp
      781 pgppsgprdv staepsatsl qnkastsspe nslpcgpdgr qpsrrggvkk yaktlrkrrs
      841 flqtdytsqv sfplvpsasl esvddvcyyd repylalgap sptvsslqdm qgepglletk
      901 algllaplre tkstnpasrv memepetmet ksvidsrvss isairfridp nnkensgvvp
      961 aasssastph csnpgssgpd taqarpsqil plsqdldgia pkeptiehgd ssfslssgdp
     1021 npdraclasn pglnnvsqgd tlelqlephv qlemglesfc tnhiqetapk ytepllsprd
     1081 eprsdecgin pgekiasipt keepqgqlsl erdrevtnkn gtnvfqeesr kdsgdspgdv
     1141 snnvsqtldi sspagkivts lsldapvtgt eqipphpprd pqgqsreppg qgcqaqeqkl
     1201 fveldldpdf flgkqtvspa vppegikaea pnhvtgqdia prdspewvcf npepslpepl
     1261 pcpqedphle tsnhcllseg ksdsssicls aeksflcfap eshpevsasl rvatslgfag
     1321 mnemvaprig mdqcscqfsy atcfrgpqpe teeedrdlea hpmapltspp sagspvvlpw
     1381 rparahsctt aplsrkshiw peycsralrq lkatpastpe gfiqlmesll elqdiletsw
     1441 gvgnkhppek ctwhftesrs rlcmgsqkll sscrhvirmd qspeemqgav rdtfqhlvql
     1501 aglcfqftdc srcsarhrea agnlrdvvyt yhqfieaaks tcergyhdls vkllarqcta
     1561 ltaavfcltq kfrastal
//
LOCUS       NP_001291491             205 aa            linear   PRI 20-NOV-2025
DEFINITION  INO80 complex subunit E isoform 2 [Homo sapiens].
ACCESSION   NP_001291491 XP_005255321
VERSION     NP_001291491.1
DBSOURCE    REFSEQ: accession NM_001304562.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Cox,E., Hwang,W., Uzoma,I., Hu,J., Guzzo,C.M., Jeong,J.,
            Matunis,M.J., Qian,J., Zhu,H. and Blackshaw,S.
  TITLE     Global Analysis of SUMO-Binding Proteins Identifies SUMOylation as
            a Key Regulator of the INO80 Chromatin Remodeling Complex
  JOURNAL   Mol Cell Proteomics 16 (5), 812-823 (2017)
   PUBMED   28254775
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Vassileva,I., Yanakieva,I., Peycheva,M., Gospodinov,A. and
            Anachkova,B.
  TITLE     The mammalian INO80 chromatin remodeling complex is required for
            replication stress recovery
  JOURNAL   Nucleic Acids Res 42 (14), 9074-9086 (2014)
   PUBMED   25016522
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL525020.3, BI093312.1, BC047712.2 and AC093512.2.
            
            On Feb 4, 2015 this sequence version replaced XP_005255321.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.604066.1,
                                           SRR7410570.604061.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..205
                     /product="INO80 complex subunit E isoform 2"
                     /note="coiled-coil domain containing 95; coiled-coil
                     domain-containing protein 95"
                     /calculated_mol_wt=21766
     CDS             1..205
                     /gene="INO80E"
                     /gene_synonym="CCDC95"
                     /coded_by="NM_001304562.2:71..688"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76853.1"
                     /db_xref="GeneID:283899"
                     /db_xref="HGNC:HGNC:26905"
ORIGIN      
        1 mngpadgevd ykkkyrnlkr klkfliyehe cfqeelrkaq rkllkvsrdk sflldrllqy
       61 envdedssds datassdnse tegtpklsdt papkrkrspp lggapspssl slppstgfpl
      121 qasgvpspyl ssmavgppdc pvggpltfpg rgsgagvgtt ltplpppkmp pptilstvpr
      181 qmfsdagsgd daldgdddlv idipe
//
LOCUS       NP_006822                425 aa            linear   PRI 20-NOV-2025
DEFINITION  polyribonucleotide 5'-hydroxyl-kinase Clp1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006822
VERSION     NP_006822.1
DBSOURCE    REFSEQ: accession NM_006831.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Sekulovski,S., Devant,P., Panizza,S., Gogakos,T., Pitiriciu,A.,
            Heitmeier,K., Ramsay,E.P., Barth,M., Schmidt,C., Tuschl,T.,
            Baas,F., Weitzer,S., Martinez,J. and Trowitzsch,S.
  TITLE     Assembly defects of human tRNA splicing endonuclease contribute to
            impaired pre-tRNA processing in pontocerebellar hypoplasia
  JOURNAL   Nat Commun 12 (1), 5610 (2021)
   PUBMED   34584079
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Morisaki,I., Shiraishi,H., Fujinami,H., Shimizu,N., Hikida,T.,
            Arai,Y., Kobayashi,T., Hanada,R., Penninger,J.M., Fujiki,M. and
            Hanada,T.
  TITLE     Modeling a human CLP1 mutation in mouse identifies an accumulation
            of tyrosine pre-tRNA fragments causing pontocerebellar hypoplasia
            type 10
  JOURNAL   Biochem Biophys Res Commun 570, 60-66 (2021)
   PUBMED   34273619
  REMARK    GeneRIF: Modeling a human CLP1 mutation in mouse identifies an
            accumulation of tyrosine pre-tRNA fragments causing pontocerebellar
            hypoplasia type 10.
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Ramirez,A., Shuman,S. and Schwer,B.
  TITLE     Human RNA 5'-kinase (hClp1) can function as a tRNA splicing enzyme
            in vivo
  JOURNAL   RNA 14 (9), 1737-1745 (2008)
   PUBMED   18648070
  REMARK    GeneRIF: Expression of hClp1 in budding yeast can complement
            conditional and lethal mutations in the essential 5'-OH RNA kinase
            module of yeast or plant tRNA ligases.
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Weitzer,S. and Martinez,J.
  TITLE     The human RNA kinase hClp1 is active on 3' transfer RNA exons and
            short interfering RNAs
  JOURNAL   Nature 447 (7141), 222-226 (2007)
   PUBMED   17495927
  REMARK    GeneRIF: the kinase hClp1 phosphorylates and licenses synthetic
            siRNAs to become assembled into RISC for subsequent target RNA
            cleavage
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Paushkin,S.V., Patel,M., Furia,B.S., Peltz,S.W. and Trotta,C.R.
  TITLE     Identification of a human endonuclease complex reveals a link
            between tRNA splicing and pre-mRNA 3' end formation
  JOURNAL   Cell 117 (3), 311-321 (2004)
   PUBMED   15109492
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   9  (residues 1 to 425)
  AUTHORS   de Vries,H., Ruegsegger,U., Hubner,W., Friedlein,A., Langen,H. and
            Keller,W.
  TITLE     Human pre-mRNA cleavage factor II(m) contains homologs of yeast
            proteins and bridges two other cleavage factors
  JOURNAL   EMBO J 19 (21), 5895-5904 (2000)
   PUBMED   11060040
  REMARK    GeneRIF: HEAB is a pre-mRNA 3'-end processing factor, which bridges
            two other pre-mRNA processing factors (CF Im and CPSF) and is
            involved in cleavage of the pre-mRNA. It can be UV-crosslinked to
            GTP.
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Tanabe,S., Bohlander,S.K., Vignon,C.V., Espinosa,R. 3rd, Zhao,N.,
            Strissel,P.L., Zeleznik-Le,N.J. and Rowley,J.D.
  TITLE     AF10 is split by MLL and HEAB, a human homolog to a putative
            Caenorhabditis elegans ATP/GTP-binding protein in an
            invins(10;11)(p12;q23q12)
  JOURNAL   Blood 88 (9), 3535-3545 (1996)
   PUBMED   8896421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA922553.1 and BC000446.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Clp1 family. The encoded
            protein is a multifunctional kinase which is a component of the
            tRNA splicing endonuclease complex and a component of the pre-mRNA
            cleavage complex II. This protein is implicated in tRNA, mRNA, and
            siRNA maturation. Mutations in this gene are associated with
            pontocerebellar hypoplasia type 10 (PCH10). Alternatively splice
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Sep 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes a longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U73524.1, SRR1803612.125930.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000533682.2/ ENSP00000434995.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..425
                     /product="polyribonucleotide 5'-hydroxyl-kinase Clp1
                     isoform 1"
                     /EC_number="2.7.1.78"
                     /note="homolog of yeast CFIA subunit Clp1p;
                     ATP/GTP-binding protein; polyribonucleotide
                     5'-hydroxyl-kinase Clp1; polynucleotide kinase Clp1;
                     pre-mRNA cleavage complex II protein Clp1; polyadenylation
                     factor Clp1; cleavage and polyadenylation factor I subunit
                     1"
                     /calculated_mol_wt=47515
     Region          14..423
                     /region_name="CLP1"
                     /note="Predicted GTPase subunit of the pre-mRNA cleavage
                     complex [Translation, ribosomal structure and biogenesis];
                     COG5623"
                     /db_xref="CDD:227910"
     Region          121..306
                     /region_name="CLP1_P"
                     /note="mRNA cleavage and polyadenylation factor CLP1
                     P-loop; pfam16575"
                     /db_xref="CDD:406878"
     CDS             1..425
                     /gene="CLP1"
                     /gene_synonym="hClp1; HEAB"
                     /coded_by="NM_006831.3:122..1399"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7964.1"
                     /db_xref="GeneID:10978"
                     /db_xref="HGNC:HGNC:16999"
                     /db_xref="MIM:608757"
ORIGIN      
        1 mgeeanddkk pttkfelere telrfeveas qsvqlelltg maeifgtelt rnkkftfdag
       61 akvavftwhg csvqlsgrte vayvskdtpm llylnthtal eqmrrqaeke eergprvmvv
      121 gptdvgkstv crlllnyavr lgrrptyvel dvgqgsvsip gtmgalyier padveegfsi
      181 qaplvyhfgs ttpgtnikly nkitsrladv fnqrcevnrr asvsgcvint cgwvkgsgyq
      241 alvhaasafe vdvvvvldqe rlynelkrdl phfvrtvllp ksggvversk dfrrecrder
      301 ireyfygfrg cfyphafnvk fsdvkiykvg aptipdsclp lgmsqednql klvpvtpgrd
      361 mvhhllsvst aegteenlse tsvagfivvt svdlehqvft vlspaprplp knfllimdir
      421 fmdlk
//
LOCUS       NP_001655                193 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming protein RhoA isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001655
VERSION     NP_001655.1
DBSOURCE    REFSEQ: accession NM_001664.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Piao,J., Su,Z., He,J., Zhu,T., Fan,F., Wang,X., Yang,Z., Zhan,H.
            and Luo,D.
  TITLE     SphK1 deficiency ameliorates the development of atherosclerosis by
            inhibiting the S1P/S1PR3/Rhoa/ROCK pathway
  JOURNAL   Cell Signal 121, 111252 (2024)
   PUBMED   38852936
  REMARK    GeneRIF: SphK1 deficiency ameliorates the development of
            atherosclerosis by inhibiting the S1P/S1PR3/Rhoa/ROCK pathway.
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Hutchins,C.M. and Gorfe,A.A.
  TITLE     Intrinsically Disordered Membrane Anchors of Rheb, RhoA, and DiRas3
            Small GTPases: Molecular Dynamics, Membrane Organization, and
            Interactions
  JOURNAL   J Phys Chem B 128 (27), 6518-6528 (2024)
   PUBMED   38942776
  REMARK    GeneRIF: Intrinsically Disordered Membrane Anchors of Rheb, RhoA,
            and DiRas3 Small GTPases: Molecular Dynamics, Membrane
            Organization, and Interactions.
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Choi,J.H., Jeong,J., Kim,J., You,E., Keum,S., Song,S., Hwang,Y.E.,
            Ji,M., Park,K.S. and Rhee,S.
  TITLE     Genetic disruption of ATAT1 causes RhoA downregulation through
            abnormal truncation of C/EBPbeta
  JOURNAL   BMB Rep 57 (6), 293-298 (2024)
   PUBMED   38835115
  REMARK    GeneRIF: Genetic disruption of ATAT1 causes RhoA downregulation
            through abnormal truncation of C/EBPbeta.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Fagan,K.P., Oliveira,L. and Pittler,S.J.
  TITLE     Sequence of rho small GTP-binding protein cDNAs from human retina
            and identification of novel 5' end cloning artifacts
  JOURNAL   Exp Eye Res 59 (2), 235-237 (1994)
   PUBMED   7835413
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Moscow,J.A., Morrow,C.S., He,R., Mullenbach,G.T. and Cowan,K.H.
  TITLE     Structure and function of the 5'-flanking sequence of the human
            cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)
  JOURNAL   J Biol Chem 267 (9), 5949-5958 (1992)
   PUBMED   1556108
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Cannizzaro,L.A., Madaule,P., Hecht,F., Axel,R., Croce,C.M. and
            Huebner,K.
  TITLE     Chromosome localization of human ARH genes, a ras-related gene
            family
  JOURNAL   Genomics 6 (2), 197-203 (1990)
   PUBMED   2407642
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Yeramian,P., Chardin,P., Madaule,P. and Tavitian,A.
  TITLE     Nucleotide sequence of human rho cDNA clone 12
  JOURNAL   Nucleic Acids Res 15 (4), 1869 (1987)
   PUBMED   3822842
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK130066.1 and BC000946.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Rho family of small
            GTPases, which cycle between inactive GDP-bound and active
            GTP-bound states and function as molecular switches in signal
            transduction cascades. Rho proteins promote reorganization of the
            actin cytoskeleton and regulate cell shape, attachment, and
            motility. Overexpression of this gene is associated with tumor cell
            proliferation and metastasis. Multiple alternatively spliced
            variants have been identified. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.87781.1,
                                           SRR1803611.176573.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000418115.6/ ENSP00000400175.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..193
                     /product="transforming protein RhoA isoform 1 precursor"
                     /EC_number="3.6.5.2"
                     /note="transforming protein RhoA; oncogene RHO H12;
                     Aplysia ras-related homolog 12; small GTP binding protein
                     RhoA; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=21637
     mat_peptide     1..190
                     /product="Transforming protein RhoA. /id=PRO_0000030411"
                     /note="propagated from UniProtKB/Swiss-Prot (P61586.1)"
                     /calculated_mol_wt=21443
     Region          5..179
                     /region_name="RhoA_like"
                     /note="Ras homology family A (RhoA)-like includes RhoA,
                     RhoB and RhoC; cd01870"
                     /db_xref="CDD:206662"
     Site            order(5,34,37..38,41,43,45,54,58..59,61..63,66,68,72)
                     /site_type="other"
                     /note="GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206662"
     Site            order(15..20,34..35,37,59..60,118,120,161..162)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206662"
     Site            order(23,25..29,42..43,45..47,52..54,163..164,168..169,
                     172)
                     /site_type="active"
                     /note="PKN/PRK1 effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(34,36,38..39,63..66,69,72,94)
                     /site_type="other"
                     /note="GAP (GTPase-activating protein) interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            34..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206662"
     Site            34
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-linked (GlcNAc) tyrosine,
                     by Photorhabdus PAU_02230, alternate.
                     /evidence=ECO:0000269|PubMed:24141704; propagated from
                     UniProtKB/Swiss-Prot (P61586.1)"
     Site            order(37..38,61,66,68..69,71..72,75,105..106,108)
                     /site_type="other"
                     /note="GDI (guanine nucleotide dissociation inhibitor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            37
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-alpha-linked (GlcNAc)
                     threonine, by C.novyi toxin TcdA, alternate.
                     /evidence=ECO:0000269|PubMed:8810274; (Microbial
                     infection) O-linked (Glc) threonine, by C.difficile toxins
                     TcdA and TcdB, alternate.
                     /evidence=ECO:0000269|PubMed:24905543,
                     ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059;
                     propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206662"
     Site            order(39,65..69,72,97,101,105)
                     /site_type="active"
                     /note="Mdia effector interaction site [active]"
                     /db_xref="CDD:206662"
     Site            order(39..40,65..66,68..69,72)
                     /site_type="other"
                     /note="Rho kinase (ROCK) effector interaction site
                     [polypeptide binding]"
                     /db_xref="CDD:206662"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206662"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     isoform 2 binding. /evidence=ECO:0000269|PubMed:30190425,
                     ECO:0007744|PDB:5ZHX"
                     /note="propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            62..79
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206662"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206662"
     Site            160..162
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206662"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG1.
                     /evidence=ECO:0000269|PubMed:11162591; propagated from
                     UniProtKB/Swiss-Prot (P61586.1)"
     Site            189..190
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by yopT.
                     /evidence=ECO:0000269|PubMed:12062101,
                     ECO:0000269|PubMed:12538863; propagated from
                     UniProtKB/Swiss-Prot (P61586.1)"
     Site            190
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000250|UniProtKB:P61585; propagated from
                     UniProtKB/Swiss-Prot (P61586.1)"
     CDS             1..193
                     /gene="RHOA"
                     /gene_synonym="ARH12; ARHA; EDFAOB; RHO12; RHOH12"
                     /coded_by="NM_001664.4:160..741"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2795.1"
                     /db_xref="GeneID:387"
                     /db_xref="HGNC:HGNC:667"
                     /db_xref="MIM:165390"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqepvk peegrdmanr igafgymecs aktkdgvrev fematraalq
      181 arrgkkksgc lvl
//
LOCUS       NP_001352706             287 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 14 [Homo sapiens].
ACCESSION   NP_001352706 XP_005254695
VERSION     NP_001352706.1
DBSOURCE    REFSEQ: accession NM_001365777.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On Sep 12, 2018 this sequence version replaced XP_005254695.3.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.62654.1,
                                           SRR5189655.14358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..287
                     /product="tropomyosin alpha-1 chain isoform 14"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32821
     Region          48..259
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..287
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365777.1:84..947"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledkf lcftspktps sswmshlsel ciclfss
//
LOCUS       NP_001138776            1367 aa            linear   PRI 20-NOV-2025
DEFINITION  IQ domain-containing protein N isoform a [Homo sapiens].
ACCESSION   NP_001138776
VERSION     NP_001138776.1
DBSOURCE    REFSEQ: accession NM_001145304.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1367)
  AUTHORS   Li,Q., Wang,Y., Zheng,W., Guo,J., Zhang,S., Gong,F., Lu,G.X.,
            Lin,G. and Dai,J.
  TITLE     Biallelic variants in IQCN cause sperm flagellar assembly defects
            and male infertility
  JOURNAL   Hum Reprod 38 (7), 1390-1398 (2023)
   PUBMED   37140151
  REMARK    GeneRIF: Biallelic variants in IQCN cause sperm flagellar assembly
            defects and male infertility.
REFERENCE   2  (residues 1 to 1367)
  AUTHORS   Wang,Y., Chen,G., Tang,Z., Mei,X., Lin,C., Kang,J., Lian,J., Lu,J.,
            Liu,Y., Lan,F., Huang,W. and Zhang,D.
  TITLE     Loss-of-function mutations in IQCN cause male infertility in humans
            and mice owing to total fertilization failure
  JOURNAL   Mol Hum Reprod 29 (7) (2023)
   PUBMED   37184908
  REMARK    GeneRIF: Loss-of-function mutations in IQCN cause male infertility
            in humans and mice owing to total fertilization failure.
REFERENCE   3  (residues 1 to 1367)
  AUTHORS   Dai,J., Li,Q., Zhou,Q., Zhang,S., Chen,J., Wang,Y., Guo,J., Gu,Y.,
            Gong,F., Tan,Y., Lu,G., Zheng,W. and Lin,G.
  TITLE     IQCN disruption causes fertilization failure and male infertility
            due to manchette assembly defect
  JOURNAL   EMBO Mol Med 14 (12), e16501 (2022)
   PUBMED   36321563
REFERENCE   4  (residues 1 to 1367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1367)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1367)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 1367)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1367)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC403083.1, AC008397.7, BC112932.1 and AL136867.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112932.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392413.5/ ENSP00000376213.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1367
                     /product="IQ domain-containing protein N isoform a"
                     /note="IQ domain-containing protein N"
                     /calculated_mol_wt=147136
     Region          34..78
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0B3.1)"
     Region          97..131
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <276..558
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          283..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0B3.1)"
     Region          <351..862
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          476..496
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0B3.1)"
     Region          786..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0B3.1)"
     Region          1116..1134
                     /region_name="IQ"
                     /note="IQ calmodulin-binding motif; pfam00612"
                     /db_xref="CDD:459869"
     Region          <1137..>1158
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <1161..>1181
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1367
                     /gene="IQCN"
                     /gene_synonym="KIAA1683; SPGF78"
                     /coded_by="NM_001145304.2:160..4263"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46017.1"
                     /db_xref="GeneID:80726"
                     /db_xref="HGNC:HGNC:29350"
                     /db_xref="MIM:620160"
ORIGIN      
        1 mtlqgradls gnqgnaagrl atvhepvvtq wavhppapah pslldkmeka ppqpqheglk
       61 skehlpqqpa egktasrrvp rlravvesqa fknilvdemd mmharaatli qanwrgywlr
      121 qklisqmmaa kaiqeawrrf nkrhilhssk slvkktraee gdipyhapqq vrfqhpeenr
      181 llsppimvnk etqfpscdnl vlcrpqsspl lqppaaqgtp epcvqgphaa rvrglaflph
      241 qtvtirfpcp vsldakcqpc lltrtirstc lvhiegdsvk tkrvsartnk arapetplsr
      301 rydqavtrps raqtqgpvka etpkapfqic pgpmitktll qtypvvsvtl pqtypastmt
      361 ttppktspvp kvtiiktpaq mypgptvtkt aphtcpmptm tkiqvhptas rtgtprqtcp
      421 atitaknrpq vsllasimks lpqvcpgpam aktppqmhpv ttpaknplqt clsatmskts
      481 sqrspvgvtk pspqtrlpam itktpaqlrs vatilktlcl asptvanvka ppqvavaagt
      541 pntsgsihen ppkakatvnv kqaakvvkas spsylaegki rclaqphpgt gvpraaaelp
      601 leaekiktgt qkqaktdmaf ktsvavemag apswtkvaee gdkpphvyvp vdmavtlprg
      661 qlaapltnas sqrhppclsq rplaapltka ssqghlptel tktpslahld tclskmhsqt
      721 hlatgavkvq sqaplatclt ktqsrgqpit dittclipah qaadlssnth sqvlltgskv
      781 snhacqrlgg lsappwakpe drqtqpqphg hvpgkttqgg pcpaacevqg mlvppmaptg
      841 hstcnveswg dngatraqps mpgqavpcqe dtvgsllasl caevagvlas qedlrtllak
      901 alsqgevwaa lnqalskevl gatvtkalpq smlsmalvka lswselrltl sralsrgelr
      961 aeltkvmqgk laevlskalt eeewvalsqa lcqgelgall sqswcrvalr tgtilpkaas
     1021 kstgsgvtkt palvkvacrr spsaawgpsl gpvrpqtskg padagvvggq swnrawepar
     1081 gaaswdtwrn kavvpprrsg epmvsmqaae eirilaviti qagvrgylar rrirlwhrga
     1141 mviqatwrgy rvrrnlahlc ratttiqsaw rgystrrdqa rhwqmlhpvt wvelgsragv
     1201 msdrswfqdg rartvsdhrc fqscqahacs vchslssrig sppsvvmlvg ssprtchtcg
     1261 rtqptrvvqg mgqgtegpga vswasayqla alsprqphrq dkaataiqsa wrgfkirqqm
     1321 rqqqmaakiv qatwrghhtr sclknteall gpadpsassr hmhwpgi
//
LOCUS       NP_001340176             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340176 XP_016869029
VERSION     NP_001340176.1
DBSOURCE    REFSEQ: accession NM_001353247.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869029.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.44181.1,
                                           SRR1803613.352017.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353247.1:327..1301"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001310870             920 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001310870
VERSION     NP_001310870.1
DBSOURCE    REFSEQ: accession NM_001323941.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.28200.1,
                                           SRR1803611.181681.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..920
                     /product="DIS3-like exonuclease 1 isoform 3"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=104881
     Region          <1..54
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          104..732
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          747..822
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..920
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323941.2:825..3587"
                     /note="isoform 3 is encoded by transcript variant 8"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mekwqtrsiy naavwyyhhc qdrmpivmvt edeeaiqqyg setegvfvit fknyldnfwp
       61 dlkaahelcd silqsrrere nesqeshgke ypehlplevl eagiksgryi qgilnvnkhr
      121 aqieafvrlq gasskdsdlv sdilihgmka rnrsihgdvv vvellpknew kgrtvalcen
      181 dcddkasges psepmptgrv vgilqknwrd yvvtfpskee vqsqgknaqk ilvtpwdyri
      241 pkiristqqa etlqdfrvvv ridswestsv ypnghfvrvl grigdlegei atilvensis
      301 vipfseaqmc empvntpesp wkvspeeeqk rkdlrkshlv fsidpkgced vddtlsvrtl
      361 nngnlelgvh iadvthfvap nsyidieart rattyyladr rydmlpsvls adlcsllggv
      421 dryavsimwe ldkasyeikk vwygrtiirs ayklfyeaaq elldgnlsvv ddipefkdld
      481 eksrqaklee lvwaigkltd iarhvrakrd gcgalelegv evcvqlddkk nihdlipkqp
      541 levhetvaec milanhwvak kiwesfphqa llrqhppphq effselreca kakgffidtr
      601 snktladsld nandphdpiv nrllrsmatq amsnalyfst gscaeeefhh yglaldkyth
      661 ftspirrysd ivvhrllmaa iskdkkmeik gnlfsnkdle elcrhinnrn qaaqhsqkqs
      721 telfqcmyfk dkdpateerc isdgviysir tngvllfipr fgikgaaylk nkdglviscg
      781 pdscsewkpg slqrfqnkit stttdgesvt fhlfdhvtvr isiqasrchs dtirleiisn
      841 kpykipntel ihqsspllks elvkevtksv eeaqlaqevk vniiqeeyqe yrqtkgrsly
      901 tlleeirdla lldvsnnygi
//
LOCUS       NP_001104547             586 aa            linear   PRI 20-NOV-2025
DEFINITION  ezrin [Homo sapiens].
ACCESSION   NP_001104547
VERSION     NP_001104547.1
DBSOURCE    REFSEQ: accession NM_001111077.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Zhou,N., He,M., Zhou,G., Fan,Q. and Qi,Y.
  TITLE     Variant in EZR leads to defects in lens development
  JOURNAL   Ophthalmic Genet 45 (4), 363-371 (2024)
   PUBMED   38563525
  REMARK    GeneRIF: Variant in EZR leads to defects in lens development.
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Lou,J., Jin,M., Zhou,C., Fan,Y., Ni,L., Mao,Y., Shen,H., Li,J.,
            Zhang,H., Fu,C., Mao,X., Chen,Y., Zhong,J., Zhou,K., Wang,L. and
            Wu,J.
  TITLE     Ezrin inhibition alleviates oxidative stress and pyroptosis via
            regulating TRPML1-calcineurin axis mediated enhancement of
            autophagy in spinal cord injury
  JOURNAL   Free Radic Biol Med 212, 133-148 (2024)
   PUBMED   38142951
  REMARK    GeneRIF: Ezrin inhibition alleviates oxidative stress and
            pyroptosis via regulating TRPML1-calcineurin axis mediated
            enhancement of autophagy in spinal cord injury.
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Deng,D.X., Li,C.Y., Zheng,Z.Y., Wen,B., Liao,L.D., Zhang,X.J.,
            Li,E.M. and Xu,L.Y.
  TITLE     Prenylated PALM2 Promotes the Migration of Esophageal Squamous Cell
            Carcinoma Cells Through Activating Ezrin
  JOURNAL   Mol Cell Proteomics 22 (8), 100593 (2023)
   PUBMED   37328063
  REMARK    GeneRIF: Prenylated PALM2 Promotes the Migration of Esophageal
            Squamous Cell Carcinoma Cells Through Activating Ezrin.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Buenaventura,R.G.M., Merlino,G. and Yu,Y.
  TITLE     Ez-Metastasizing: The Crucial Roles of Ezrin in Metastasis
  JOURNAL   Cells 12 (12), 1620 (2023)
   PUBMED   37371090
  REMARK    GeneRIF: Ez-Metastasizing: The Crucial Roles of Ezrin in
            Metastasis.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Krieg,J. and Hunter,T.
  TITLE     Identification of the two major epidermal growth factor-induced
            tyrosine phosphorylation sites in the microvillar core protein
            ezrin
  JOURNAL   J Biol Chem 267 (27), 19258-19265 (1992)
   PUBMED   1382070
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Egerton,M., Burgess,W.H., Chen,D., Druker,B.J., Bretscher,A. and
            Samelson,L.E.
  TITLE     Identification of ezrin as an 81-kDa tyrosine-phosphorylated
            protein in T cells
  JOURNAL   J Immunol 149 (6), 1847-1852 (1992)
   PUBMED   1381389
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Lankes,W.T. and Furthmayr,H.
  TITLE     Moesin: a member of the protein 4.1-talin-ezrin family of proteins
  JOURNAL   Proc Natl Acad Sci U S A 88 (19), 8297-8301 (1991)
   PUBMED   1924289
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Gould,K.L., Bretscher,A., Esch,F.S. and Hunter,T.
  TITLE     cDNA cloning and sequencing of the protein-tyrosine kinase
            substrate, ezrin, reveals homology to band 4.1
  JOURNAL   EMBO J 8 (13), 4133-4142 (1989)
   PUBMED   2591371
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Pakkanen,R. and Vaheri,A.
  TITLE     Cytovillin and other microvillar proteins of human choriocarcinoma
            cells
  JOURNAL   J Cell Biochem 41 (1), 1-12 (1989)
   PUBMED   2592436
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA754543.1 and BC013903.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The cytoplasmic peripheral membrane protein encoded by
            this gene functions as a protein-tyrosine kinase substrate in
            microvilli. As a member of the ERM protein family, this protein
            serves as an intermediate between the plasma membrane and the actin
            cytoskeleton. This protein plays a key role in cell surface
            structure adhesion, migration and organization, and it has been
            implicated in various human cancers. A pseudogene located on
            chromosome 3 has been identified for this gene. Alternatively
            spliced variants have also been described for this gene. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.119614.1,
                                           SRR1803614.29937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMEA2467150
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367075.4/ ENSP00000356042.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..586
                     /product="ezrin"
                     /note="cytovillin 2; villin 2 (ezrin); p81; epididymis
                     secretory protein Li 105"
                     /calculated_mol_wt=69282
     Region          7..206
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            60
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Region          115..120
                     /region_name="[IL]-x-C-x-x-[DE] motif.
                     /evidence=ECO:0000305|PubMed:25417112"
                     /note="propagated from UniProtKB/Swiss-Prot (P15311.4)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PDGFR.
                     /evidence=ECO:0000269|PubMed:1382070,
                     ECO:0000269|PubMed:18046454; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Region          200..296
                     /region_name="FERM_C_ERM"
                     /note="FERM domain C-lobe/F3 of the ERM family; cd13194"
                     /db_xref="CDD:270015"
     Site            order(242..243,245..251,260,281,284..285,288)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:270015"
     Site            order(242,245..252,260,281,284..285,288)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          244..586
                     /region_name="Interaction with SCYL3.
                     /evidence=ECO:0000269|PubMed:12651155"
                     /note="propagated from UniProtKB/Swiss-Prot (P15311.4)"
     Site            order(278,282)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:270015"
     Site            281..296
                     /site_type="other"
                     /note="actin binding site 2 [polypeptide binding]"
                     /db_xref="CDD:270015"
     Region          306..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15311.4)"
     Region          337..456
                     /region_name="ERM_helical"
                     /note="Ezrin/radixin/moesin, alpha-helical domain;
                     pfam20492"
                     /db_xref="CDD:466641"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by PDGFR.
                     /evidence=ECO:0000269|PubMed:1382070; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:18046454; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Region          485..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15311.4)"
     Region          510..586
                     /region_name="ERM_C"
                     /note="Ezrin/radixin/moesin family C terminal; pfam00769"
                     /db_xref="CDD:459932"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26040; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ROCK2 and PKC/PRKCI.
                     /evidence=ECO:0000305|PubMed:18270268; propagated from
                     UniProtKB/Swiss-Prot (P15311.4)"
     CDS             1..586
                     /gene="EZR"
                     /gene_synonym="CVIL; CVL; HEL-S-105; VIL2"
                     /coded_by="NM_001111077.2:126..1886"
                     /db_xref="CCDS:CCDS5258.1"
                     /db_xref="GeneID:7430"
                     /db_xref="HGNC:HGNC:12691"
                     /db_xref="MIM:123900"
ORIGIN      
        1 mpkpinvrvt tmdaelefai qpnttgkqlf dqvvktiglr evwyfglhyv dnkgfptwlk
       61 ldkkvsaqev rkenplqfkf rakfypedva eeliqditqk lfflqvkegi lsdeiycppe
      121 tavllgsyav qakfgdynke vhksgylsse rlipqrvmdq hkltrdqwed riqvwhaehr
      181 gmlkdnamle ylkiaqdlem yginyfeikn kkgtdlwlgv dalglniyek ddkltpkigf
      241 pwseirnisf ndkkfvikpi dkkapdfvfy aprlrinkri lqlcmgnhel ymrrrkpdti
      301 evqqmkaqar eekhqkqler qqletekkrr etverekeqm mrekeelmlr lqdyeektkk
      361 aerelseqiq ralqleeerk raqeeaerle adrmaalrak eelerqavdq iksqeqlaae
      421 laeytakial leearrrked eveewqhrak eaqddlvktk eelhlvmtap ppppppvyep
      481 vsyhvqeslq degaeptgys aelssegird drneekrite aeknervqrq lltlsselsq
      541 ardenkrthn diihnenmrq grdkyktlrq irqgntkqri defeal
//
LOCUS       NP_695002                644 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 34 [Homo sapiens].
ACCESSION   NP_695002
VERSION     NP_695002.1
DBSOURCE    REFSEQ: accession NM_153270.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Ross,M.T., Grafham,D.V., Coffey,A.J., Scherer,S., McLay,K.,
            Muzny,D., Platzer,M., Howell,G.R., Burrows,C., Bird,C.P.,
            Frankish,A., Lovell,F.L., Howe,K.L., Ashurst,J.L., Fulton,R.S.,
            Sudbrak,R., Wen,G., Jones,M.C., Hurles,M.E., Andrews,T.D.,
            Scott,C.E., Searle,S., Ramser,J., Whittaker,A., Deadman,R.,
            Carter,N.P., Hunt,S.E., Chen,R., Cree,A., Gunaratne,P., Havlak,P.,
            Hodgson,A., Metzker,M.L., Richards,S., Scott,G., Steffen,D.,
            Sodergren,E., Wheeler,D.A., Worley,K.C., Ainscough,R.,
            Ambrose,K.D., Ansari-Lari,M.A., Aradhya,S., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Ballabio,A., Banerjee,R., Barker,G.E.,
            Barlow,K.F., Barrett,I.P., Bates,K.N., Beare,D.M., Beasley,H.,
            Beasley,O., Beck,A., Bethel,G., Blechschmidt,K., Brady,N.,
            Bray-Allen,S., Bridgeman,A.M., Brown,A.J., Brown,M.J., Bonnin,D.,
            Bruford,E.A., Buhay,C., Burch,P., Burford,D., Burgess,J.,
            Burrill,W., Burton,J., Bye,J.M., Carder,C., Carrel,L., Chako,J.,
            Chapman,J.C., Chavez,D., Chen,E., Chen,G., Chen,Y., Chen,Z.,
            Chinault,C., Ciccodicola,A., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S., Clerc-Blankenburg,K., Clifford,K., Cobley,V., Cole,C.G.,
            Conquer,J.S., Corby,N., Connor,R.E., David,R., Davies,J., Davis,C.,
            Davis,J., Delgado,O., Deshazo,D., Dhami,P., Ding,Y., Dinh,H.,
            Dodsworth,S., Draper,H., Dugan-Rocha,S., Dunham,A., Dunn,M.,
            Durbin,K.J., Dutta,I., Eades,T., Ellwood,M., Emery-Cohen,A.,
            Errington,H., Evans,K.L., Faulkner,L., Francis,F., Frankland,J.,
            Fraser,A.E., Galgoczy,P., Gilbert,J., Gill,R., Glockner,G.,
            Gregory,S.G., Gribble,S., Griffiths,C., Grocock,R., Gu,Y.,
            Gwilliam,R., Hamilton,C., Hart,E.A., Hawes,A., Heath,P.D.,
            Heitmann,K., Hennig,S., Hernandez,J., Hinzmann,B., Ho,S., Hoffs,M.,
            Howden,P.J., Huckle,E.J., Hume,J., Hunt,P.J., Hunt,A.R.,
            Isherwood,J., Jacob,L., Johnson,D., Jones,S., de Jong,P.J.,
            Joseph,S.S., Keenan,S., Kelly,S., Kershaw,J.K., Khan,Z.,
            Kioschis,P., Klages,S., Knights,A.J., Kosiura,A., Kovar-Smith,C.,
            Laird,G.K., Langford,C., Lawlor,S., Leversha,M., Lewis,L., Liu,W.,
            Lloyd,C., Lloyd,D.M., Loulseged,H., Loveland,J.E., Lovell,J.D.,
            Lozado,R., Lu,J., Lyne,R., Ma,J., Maheshwari,M., Matthews,L.H.,
            McDowall,J., McLaren,S., McMurray,A., Meidl,P., Meitinger,T.,
            Milne,S., Miner,G., Mistry,S.L., Morgan,M., Morris,S., Muller,I.,
            Mullikin,J.C., Nguyen,N., Nordsiek,G., Nyakatura,G., O'Dell,C.N.,
            Okwuonu,G., Palmer,S., Pandian,R., Parker,D., Parrish,J.,
            Pasternak,S., Patel,D., Pearce,A.V., Pearson,D.M., Pelan,S.E.,
            Perez,L., Porter,K.M., Ramsey,Y., Reichwald,K., Rhodes,S.,
            Ridler,K.A., Schlessinger,D., Schueler,M.G., Sehra,H.K.,
            Shaw-Smith,C., Shen,H., Sheridan,E.M., Shownkeen,R., Skuce,C.D.,
            Smith,M.L., Sotheran,E.C., Steingruber,H.E., Steward,C.A.,
            Storey,R., Swann,R.M., Swarbreck,D., Tabor,P.E., Taudien,S.,
            Taylor,T., Teague,B., Thomas,K., Thorpe,A., Timms,K., Tracey,A.,
            Trevanion,S., Tromans,A.C., d'Urso,M., Verduzco,D., Villasana,D.,
            Waldron,L., Wall,M., Wang,Q., Warren,J., Warry,G.L., Wei,X.,
            West,A., Whitehead,S.L., Whiteley,M.N., Wilkinson,J.E.,
            Willey,D.L., Williams,G., Williams,L., Williamson,A.,
            Williamson,H., Wilming,L., Woodmansey,R.L., Wray,P.W., Yen,J.,
            Zhang,J., Zhou,J., Zoghbi,H., Zorilla,S., Buck,D., Reinhardt,R.,
            Poustka,A., Rosenthal,A., Lehrach,H., Meindl,A., Minx,P.J.,
            Hillier,L.W., Willard,H.F., Wilson,R.K., Waterston,R.H., Rice,C.M.,
            Vaudin,M., Coulson,A., Nelson,D.L., Weinstock,G., Sulston,J.E.,
            Durbin,R., Hubbard,T., Gibbs,R.A., Beck,S., Rogers,J. and
            Bentley,D.R.
  TITLE     The DNA sequence of the human X chromosome
  JOURNAL   Nature 434 (7031), 325-337 (2005)
   PUBMED   15772651
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA395149.1, BC109031.2, AI792176.1 and AL772392.4.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK092279.1, BC109031.2 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379499.3/ ENSP00000368813.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..644
                     /product="kelch-like protein 34"
                     /note="kelch-like 34; RP11-450P7.3"
                     /calculated_mol_wt=70481
     Region          1..136
                     /region_name="BTB_POZ_KLHL34"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 34 (KLHL34); cd18264"
                     /db_xref="CDD:349573"
     Region          126..233
                     /region_name="BACK_KLHL34"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 34 (KLHL34); cd18473"
                     /db_xref="CDD:350548"
     Region          304..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          320..366
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          333..578
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          358..411
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          367..425
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          415..513
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          426..473
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          475..526
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          516..559
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          528..571
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     Region          561..606
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          573..623
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N239.1)"
     CDS             1..644
                     /gene="KLHL34"
                     /coded_by="NM_153270.3:543..2477"
                     /db_xref="CCDS:CCDS14199.1"
                     /db_xref="GeneID:257240"
                     /db_xref="HGNC:HGNC:26634"
ORIGIN      
        1 msyflsycka hggalltgyq alraegflcd vtletegsef pahrsllacs sdyfralfks
       61 htqesrarvi hlhvpsaagl qrlldfiyta wlslsmdtve dtleaasylq vtealglcgr
      121 ylerqlapen ccfaanvaar fglahtldaa ercivshlqe llargagpag llelnptslr
      181 avlgapdvar vpearllgla lawlrqeptt erlahctell ervrfglvpa dvlrrvysgs
      241 glvlparvkg liiqalnyht tpsrqplmqg eqtsirspqt rillvggrra revvieevaa
      301 pqraargqva apepeeeeee leeeeeeeew eltqnvvafd vynhrwrslt qlptpllghs
      361 vctagnflfv lggespsgsa sspladdsrv vtaqvhrydp rfhawtevpa mrearahfwc
      421 gavgerllav gglgaggevl asvemydlrr drwtaagalp ralhghagav gdrgvvyisg
      481 gkagrgegga sslrdlyvlg peeqvwskka pmgtarfghh mavlrgavfa flgryepfse
      541 ierydpgadq wtrlrplpyd rfcyglavve etalllgglk wrdsrqvptr nvvgydldld
      601 rwedigcalp wawsglrcav lqlaeggdde regevgeald lvlg
//
LOCUS       NP_001337621             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337621
VERSION     NP_001337621.1
DBSOURCE    REFSEQ: accession NM_001350692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (28), as well as variants 1-4,
            9-27, and 29-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.10071.1,
                                           SRR7346977.2146672.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350692.1:825..3035"
                     /note="isoform 1 is encoded by transcript variant 28"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001317658             774 aa            linear   PRI 20-NOV-2025
DEFINITION  catenin beta-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001317658
VERSION     NP_001317658.1
DBSOURCE    REFSEQ: accession NM_001330729.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 774)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 774)
  AUTHORS   Serafin,D.S., Harris,N.R., Balint,L., Douglas,E.S. and Caron,K.M.
  TITLE     Proximity interactome of lymphatic VE-cadherin reveals mechanisms
            of junctional remodeling and reelin secretion
  JOURNAL   Nat Commun 15 (1), 7734 (2024)
   PUBMED   39232006
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 774)
  AUTHORS   Li,Y., Chen,X., Xiong,Y., Xu,X., Xie,C., Min,M., Liang,D., Chen,C.
            and Mao,H.
  TITLE     BRCC36 regulates beta-catenin ubiquitination to alleviate vascular
            calcification in chronic kidney disease
  JOURNAL   J Transl Med 22 (1), 820 (2024)
   PUBMED   39227917
  REMARK    GeneRIF: BRCC36 regulates beta-catenin ubiquitination to alleviate
            vascular calcification in chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 774)
  AUTHORS   Zhao,W., Wang,X., Han,L., Zhang,C., Wang,C., Kong,D., Zhang,M.,
            Xu,T., Li,G., Hu,G., Luo,J., Yee,S.W., Yang,J., Stahl,A., Chen,X.
            and Zhang,Y.
  TITLE     SLC13A3 is a major effector downstream of activated beta-catenin in
            liver cancer pathogenesis
  JOURNAL   Nat Commun 15 (1), 7522 (2024)
   PUBMED   39215042
  REMARK    GeneRIF: SLC13A3 is a major effector downstream of activated
            beta-catenin in liver cancer pathogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 774)
  AUTHORS   Bai,Y., Li,R., Hao,J.F., Chen,L.W., Liu,S.T., Zhang,X.L.,
            Lip,G.Y.H., Yang,J.K., Zou,Y.X. and Wang,H.
  TITLE     Accumulated beta-catenin is associated with human atrial fibrosis
            and atrial fibrillation
  JOURNAL   J Transl Med 22 (1), 734 (2024)
   PUBMED   39103891
  REMARK    GeneRIF: Accumulated beta-catenin is associated with human atrial
            fibrosis and atrial fibrillation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 774)
  AUTHORS   Sacco,P.A., McGranahan,T.M., Wheelock,M.J. and Johnson,K.R.
  TITLE     Identification of plakoglobin domains required for association with
            N-cadherin and alpha-catenin
  JOURNAL   J Biol Chem 270 (34), 20201-20206 (1995)
   PUBMED   7650039
REFERENCE   7  (residues 1 to 774)
  AUTHORS   Brady-Kalnay,S.M., Rimm,D.L. and Tonks,N.K.
  TITLE     Receptor protein tyrosine phosphatase PTPmu associates with
            cadherins and catenins in vivo
  JOURNAL   J Cell Biol 130 (4), 977-986 (1995)
   PUBMED   7642713
REFERENCE   8  (residues 1 to 774)
  AUTHORS   Kanai,Y., Ochiai,A., Shibata,T., Oyama,T., Ushijima,S., Akimoto,S.
            and Hirohashi,S.
  TITLE     c-erbB-2 gene product directly associates with beta-catenin and
            plakoglobin
  JOURNAL   Biochem Biophys Res Commun 208 (3), 1067-1072 (1995)
   PUBMED   7702605
REFERENCE   9  (residues 1 to 774)
  AUTHORS   Aberle,H., Butz,S., Stappert,J., Weissig,H., Kemler,R. and
            Hoschuetzky,H.
  TITLE     Assembly of the cadherin-catenin complex in vitro with recombinant
            proteins
  JOURNAL   J Cell Sci 107 (Pt 12), 3655-3663 (1994)
   PUBMED   7706414
REFERENCE   10 (residues 1 to 774)
  AUTHORS   Ho,S.K.L., Tsang,M.H.Y., Lee,M., Cheng,S.S.W., Luk,H.M., Lo,I.F.M.
            and Chung,B.H.Y.
  TITLE     CTNNB1 Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35593792
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294778.1, AC104307.2 and
            CA944934.1.
            
            Summary: The protein encoded by this gene is part of a complex of
            proteins that constitute adherens junctions (AJs). AJs are
            necessary for the creation and maintenance of epithelial cell
            layers by regulating cell growth and adhesion between cells. The
            encoded protein also anchors the actin cytoskeleton and may be
            responsible for transmitting the contact inhibition signal that
            causes cells to stop dividing once the epithelial sheet is
            complete. Finally, this protein binds to the product of the APC
            gene, which is mutated in adenomatous polyposis of the colon.
            Mutations in this gene are a cause of colorectal cancer (CRC),
            pilomatrixoma (PTR), medulloblastoma (MDB), and ovarian cancer.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (4) differs in the 5' and 3' UTRs
            and the 5' coding region and initiates translation at a downstream
            start codon, compared to variant 1. It encodes isoform 2, which has
            a shorter N-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.234062.1,
                                           SRR1803612.59779.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..774
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..774
                     /product="catenin beta-1 isoform 2"
                     /note="catenin (cadherin-associated protein), beta 1,
                     88kDa"
                     /calculated_mol_wt=84635
     Region          71..144
                     /region_name="CTNNAbd_CTNNB1"
                     /note="alpha-catenin binding domain found in catenin
                     beta-1 (CTNNB1) and similar proteins; cd21724"
                     /db_xref="CDD:439241"
     Site            order(76..79,83..84,86..88,91..92,95,113..115,117..118,
                     121..122,125,128..136)
                     /site_type="other"
                     /note="CNTTA binding site [polypeptide binding]"
                     /db_xref="CDD:439241"
     Region          135..>424
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          146..171
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          181..214
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          223..255
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          223..255
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Site            order(246,250,254,288,292,296,331,335,339)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          263..299
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          305..340
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          343..383
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          347..382
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          395..420
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(411,415,419,455,459,463,501,505,509)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          424..466
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          428..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          475..510
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          517..575
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          576..615
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          580..614
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          622..655
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..774
                     /gene="CTNNB1"
                     /gene_synonym="armadillo; CTNNB; EVR7; MRD19; NEDSDV"
                     /coded_by="NM_001330729.2:368..2692"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS87067.1"
                     /db_xref="GeneID:1499"
                     /db_xref="HGNC:HGNC:2514"
                     /db_xref="MIM:116806"
ORIGIN      
        1 meldmamepd rkaavshwqq qsyldsgihs gatttapsls gkgnpeeedv dtsqvlyewe
       61 qgfsqsftqe qvadidgqya mtraqrvraa mfpetldegm qipstqfdaa hptnvqrlae
      121 psqmlkhavv nlinyqddae latraipelt kllndedqvv vnkaavmvhq lskkeasrha
      181 imrspqmvsa ivrtmqntnd vetarctagt lhnlshhreg llaifksggi palvkmlgsp
      241 vdsvlfyait tlhnlllhqe gakmavrlag glqkmvalln ktnvkflait tdclqilayg
      301 nqeskliila sggpqalvni mrtytyekll wttsrvlkvl svcssnkpai veaggmqalg
      361 lhltdpsqrl vqnclwtlrn lsdaatkqeg megllgtlvq llgsddinvv tcaagilsnl
      421 tcnnyknkmm vcqvggieal vrtvlragdr editepaica lrhltsrhqe aemaqnavrl
      481 hyglpvvvkl lhppshwpli katvglirnl alcpanhapl reqgaiprlv qllvrahqdt
      541 qrrtsmggtq qqfvegvrme eivegctgal hilardvhnr ivirglntip lfvqllyspi
      601 eniqrvaagv lcelaqdkea aeaieaegat apltellhsr negvatyaaa vlfrmsedkp
      661 qdykkrlsve ltsslfrtep mawnetadlg ldigaqgepl gyrqddpsyr sfhsggygqd
      721 algmdpmmeh emgghhpgad ypvdglpdlg haqdlmdglp pgdsnqlawf dtdl
//
LOCUS       NP_113642                669 aa            linear   PRI 20-NOV-2025
DEFINITION  protein adenylyltransferase SelO, mitochondrial [Homo sapiens].
ACCESSION   NP_113642
VERSION     NP_113642.1
DBSOURCE    REFSEQ: accession NM_031454.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Sreelatha,A., Yee,S.S., Lopez,V.A., Park,B.C., Kinch,L.N.,
            Pilch,S., Servage,K.A., Zhang,J., Jiou,J., Karasiewicz-Urbanska,M.,
            Lobocka,M., Grishin,N.V., Orth,K., Kucharczyk,R., Pawlowski,K.,
            Tomchick,D.R. and Tagliabracci,V.S.
  TITLE     Protein AMPylation by an Evolutionarily Conserved Pseudokinase
  JOURNAL   Cell 175 (3), 809-821 (2018)
   PUBMED   30270044
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Gladyshev,V.N., Arner,E.S., Berry,M.J., Brigelius-Flohe,R.,
            Bruford,E.A., Burk,R.F., Carlson,B.A., Castellano,S., Chavatte,L.,
            Conrad,M., Copeland,P.R., Diamond,A.M., Driscoll,D.M., Ferreiro,A.,
            Flohe,L., Green,F.R., Guigo,R., Handy,D.E., Hatfield,D.L.,
            Hesketh,J., Hoffmann,P.R., Holmgren,A., Hondal,R.J., Howard,M.T.,
            Huang,K., Kim,H.Y., Kim,I.Y., Kohrle,J., Krol,A., Kryukov,G.V.,
            Lee,B.J., Lee,B.C., Lei,X.G., Liu,Q., Lescure,A., Lobanov,A.V.,
            Loscalzo,J., Maiorino,M., Mariotti,M., Sandeep Prabhu,K.,
            Rayman,M.P., Rozovsky,S., Salinas,G., Schmidt,E.E., Schomburg,L.,
            Schweizer,U., Simonovic,M., Sunde,R.A., Tsuji,P.A., Tweedie,S.,
            Ursini,F., Whanger,P.D. and Zhang,Y.
  TITLE     Selenoprotein Gene Nomenclature
  JOURNAL   J Biol Chem 291 (46), 24036-24040 (2016)
   PUBMED   27645994
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Han,S.J., Lee,B.C., Yim,S.H., Gladyshev,V.N. and Lee,S.R.
  TITLE     Characterization of mammalian selenoprotein o: a redox-active
            mitochondrial protein
  JOURNAL   PLoS One 9 (4), e95518 (2014)
   PUBMED   24751718
  REMARK    GeneRIF: SelO is a redox-active mitochondrial selenoprotein.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Kryukov,G.V., Castellano,S., Novoselov,S.V., Lobanov,A.V.,
            Zehtab,O., Guigo,R. and Gladyshev,V.N.
  TITLE     Characterization of mammalian selenoproteomes
  JOURNAL   Science 300 (5624), 1439-1443 (2003)
   PUBMED   12775843
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Mabuchi,H., Tatami,R., Ueda,K., Ueda,R., Haba,T., Kametani,T.,
            Watanabe,A., Wakasugi,T., Ito,S., Koizumi,J., Ohta,M., Miyamoto,S.
            and Takeda,R.
  TITLE     Serum lipid and lipoprotein levels in Japanese patients with
            familial hypercholesterolemia
  JOURNAL   Atherosclerosis 32 (4), 435-444 (1979)
   PUBMED   223596
  REMARK    GeneRIF: The SELO protein has a protein domain with significant
            albeit remote sequence similarity to protein kinase-like proteins.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY324823.1.
            
            Summary: This gene encodes a selenoprotein that is localized to the
            mitochondria. It is the largest mammalian selenoprotein, containing
            the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA
            codon, which normally signals translation termination. The 3' UTRs
            of selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. The exact function of this selenoprotein is not
            known, but it is thought to have redox activity. [provided by
            RefSeq, Dec 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110866.1, AY324823.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 24751718
            MANE Ensembl match                 :: ENST00000380903.7/
                                                  ENSP00000370288.2
            protein contains selenocysteine    :: PMID: 12775843
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..669
                     /product="protein adenylyltransferase SelO, mitochondrial"
                     /EC_number="2.7.7.108"
                     /calculated_mol_wt=73358
     Region          45..669
                     /region_name="SelO"
                     /note="Protein adenylyltransferase (AMPylase) SelO/YdiU
                     (selenoprotein O) [Posttranslational modification, protein
                     turnover, chaperones]; COG0397"
                     /db_xref="CDD:440166"
     Region          634..654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVL4.3)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BVL4.3)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BVL4.3)"
     Site            667
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..669
                     /gene="SELENOO"
                     /gene_synonym="SELO"
                     /coded_by="NM_031454.2:27..2036"
                     /note="UGA stop codon recoded as selenocysteine"
                     /db_xref="CCDS:CCDS43034.1"
                     /db_xref="GeneID:83642"
                     /db_xref="HGNC:HGNC:30395"
                     /db_xref="MIM:607917"
ORIGIN      
        1 mavyraalga slaaarllpl grcspspapr stlsgaamep aprwlaglrf dnralralpv
       61 eapppgpega psaprpvpga cftrvqptpl rqprlvalse palallglga ppareaeaea
      121 alffsgnall pgaepaahcy cghqfgqfag qlgdgaamyl gevctatger welqlkgagp
      181 tpfsrqadgr kvlrssiref lcseamfhlg vpttragacv tsestvvrdv fydgnpkyeq
      241 ctvvlrvast firfgsfeif ksadehtgra gpsvgrndir vqlldyviss fypeiqaaha
      301 sdsvqrnaaf frevtrrtar mvaewqcvgf chgvlntdnm silgltidyg pfgfldrydp
      361 dhvcnasdnt gryayskqpe vcrwnlrkla ealqpelple lgeailaeef daefqrhylq
      421 kmrrklglvq veleedgalv sklletmhlt gadftntfyl lssfpveles pglaeflarl
      481 meqcasleel rlafrpqmdp rqlsmmlmla qsnpqlfalm gtragiarel erveqqsrle
      541 qlsaaelqsr nqghwadwlq ayrarldkdl egagdaaawq aehvrvmhan npkyvlrnyi
      601 aqnaieaaer gdfsevrrvl klletpyhce agaatdaeat eadgadgrqr sysskpplwa
      661 aelcvtuss
//
LOCUS       NP_075394                446 aa            linear   PRI 20-NOV-2025
DEFINITION  NAD kinase isoform 1 [Homo sapiens].
ACCESSION   NP_075394
VERSION     NP_075394.3
DBSOURCE    REFSEQ: accession NM_023018.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Praharaj,P.P., Li,Y., Mary,C., Soflaee,M.H., Ryu,K., Kim,D.,
            Tran,D.H., Dey,T., Tom,H.J., Rion,H., Gelin,M., Lemoff,A.,
            Zacharias,L.G., Patricio,J.S., Mathews,T.P., Chen,Z., Lionne,C.,
            Hoxhaj,G. and Labesse,G.
  TITLE     Cryo-EM structure and regulation of human NAD kinase
  JOURNAL   Sci Adv 11 (4), eads2664 (2025)
   PUBMED   39854463
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Meng,X., Peng,F., Yu,S., Chi,X., Wang,W. and Shao,S.
  TITLE     Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1 axis
  JOURNAL   J Cancer Res Clin Oncol 150 (5), 228 (2024)
   PUBMED   38700533
  REMARK    GeneRIF: Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1
            axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wu,T., Ding,K., Wang,C., Lin,G., Xie,C., Chen,X., Li,Q., Yu,F.,
            Mao,Y., Hong,W., Lu,L. and Li,S.
  TITLE     G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation
  JOURNAL   FASEB J 38 (3), e23449 (2024)
   PUBMED   38315451
  REMARK    GeneRIF: G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Magni,G., Amici,A., Emanuelli,M., Orsomando,G., Raffaelli,N. and
            Ruggieri,S.
  TITLE     Enzymology of NAD+ homeostasis in man
  JOURNAL   Cell Mol Life Sci 61 (1), 19-34 (2004)
   PUBMED   14704851
  REMARK    Review article
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Lerner,F., Niere,M., Ludwig,A. and Ziegler,M.
  TITLE     Structural and functional characterization of human NAD kinase
  JOURNAL   Biochem Biophys Res Commun 288 (1), 69-74 (2001)
   PUBMED   11594753
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023114.1, BC001709.1, AL031282.1 and BM842058.1.
            
            On Nov 15, 2004 this sequence version replaced NP_075394.2.
            
            Summary: NADK catalyzes the transfer of a phosphate group from ATP
            to NAD to generate NADP, which in its reduced form acts as an
            electron donor for biosynthetic reactions (Lerner et al., 2001
            [PubMed 11594753]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes variant 1 isoform (1).
            Variants 1, 2 and 5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023114.1, SRR7346977.1267052.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341426.9/ ENSP00000341679.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..446
                     /product="NAD kinase isoform 1"
                     /EC_number="2.7.1.23"
                     /note="poly(P)/ATP NAD kinase"
                     /calculated_mol_wt=49097
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Region          <96..433
                     /region_name="pnk"
                     /note="bifunctional NADP phosphatase/NAD kinase; cl28462"
                     /db_xref="CDD:333282"
     CDS             1..446
                     /gene="NADK"
                     /gene_synonym="dJ283E3.1; NADK1"
                     /coded_by="NM_023018.5:223..1563"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30565.1"
                     /db_xref="GeneID:65220"
                     /db_xref="HGNC:HGNC:29831"
                     /db_xref="MIM:611616"
ORIGIN      
        1 memeqekmtm nkelspdaaa yccsachgde twsynhpirg raksrslsas palgstkefr
       61 rtrslhgpcp vttfgpkacv lqnpqtimhi qdpasqrltw nkspksvlvi kkmrdasllq
      121 pfkelcthlm eenmivyvek kvledpaias desfgavkkk fctfredydd isnqidfiic
      181 lggdgtllya sslfqgsvpp vmafhlgslg fltpfsfenf qsqvtqvieg naavvlrsrl
      241 kvrvvkelrg kktavhnglg engsqaagld mdvgkqamqy qvlnevvidr gpssylsnvd
      301 vyldghlitt vqgdgvivst ptgstayaaa agasmihpnv paimitpicp hslsfrpivv
      361 pagvelkiml spearntawv sfdgrkrqei rhgdsisitt scyplpsicv rdpvsdwfes
      421 laqclhwnvr kkqahfeeee eeeeeg
//
LOCUS       NP_001354618             772 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform zz [Homo sapiens].
ACCESSION   NP_001354618
VERSION     NP_001354618.1
DBSOURCE    REFSEQ: accession NM_001367689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 772)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 772)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 772)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 772)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 772)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 772)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 772)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 772)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 772)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 772)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.120212.1,
                                           SRR1660805.46433.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..772
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..772
                     /product="SUN domain-containing protein 1 isoform zz"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=85267
     Region          12..278
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <352..>576
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          404..457
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(404,407..408,411,414..415,418..419,421..422,
                     425..426,428..429,432..433,435..436,439,442..443,446,
                     449..450,453..454,456..457)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          534..592
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          635..770
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..772
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367689.1:105..2423"
                     /note="isoform zz is encoded by transcript variant 52"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld
      181 ahtaahsqsp rlpgragtlw hiwacagyfl lqilrrigav gqavsrtaws alwlavvapg
      241 kaasgvfwwl gigwyqfvtl iswlnvfllt rclrnickfl vlliplflll aglslrgqgn
      301 ffsflpvlnw asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls
      361 gqchhhgenl relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev
      421 rmshledilg klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr
      481 hvktgcetvd avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd
      541 lqlqilrnvt hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm
      601 vdfalesggg silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg
      661 sqgylvvrls mmihpaaftl ehipktlspt gnissapkdf avygleneyq eegqllgqft
      721 ydqdgeslqm fqalkrpddt afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_001271168             167 aa            linear   PRI 20-NOV-2025
DEFINITION  store-operated calcium entry-associated regulatory factor isoform 2
            [Homo sapiens].
ACCESSION   NP_001271168 XP_005273586
VERSION     NP_001271168.1
DBSOURCE    REFSEQ: accession NM_001284239.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Dai,Y., Xu,Y., Shen,J., Hu,C., Li,X., Chen,Y., Liu,Y. and Hu,D.
  TITLE     MiR-30a-5p isoform -1|1 promotes the progression of gastric cancer
            by inhibiting TMEM66 and reducing intratumoral cytotoxic T cells
  JOURNAL   Exp Cell Res 439 (2), 114099 (2024)
   PUBMED   38802035
  REMARK    GeneRIF: MiR-30a-5p isoform -1|1 promotes the progression of
            gastric cancer by inhibiting TMEM66 and reducing intratumoral
            cytotoxic T cells.
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Rosado,J.A.
  TITLE     Reduced Ca2+ mobilization in neonatal human platelets involves
            SARAF and pannexin-1
  JOURNAL   Br J Haematol 204 (3), 755-756 (2024)
   PUBMED   38073055
  REMARK    GeneRIF: Reduced Ca[2+] mobilization in neonatal human platelets
            involves SARAF and pannexin-1.
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Zomot,E., Achildiev Cohen,H., Dagan,I., Militsin,R. and Palty,R.
  TITLE     Bidirectional regulation of calcium release-activated calcium
            (CRAC) channel by SARAF
  JOURNAL   J Cell Biol 220 (12) (2021)
   PUBMED   34705029
  REMARK    GeneRIF: Bidirectional regulation of calcium release-activated
            calcium (CRAC) channel by SARAF.
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Palty,R., Raveh,A., Kaminsky,I., Meller,R. and Reuveny,E.
  TITLE     SARAF inactivates the store operated calcium entry machinery to
            prevent excess calcium refilling
  JOURNAL   Cell 149 (2), 425-438 (2012)
   PUBMED   22464749
  REMARK    GeneRIF: Study shows that SARAF is an endoplasmic reticulum
            resident protein, which responds to cytosolic Ca2+ elevation after
            ER Ca2+ refilling by promoting a slow inactivation process of
            STIM2-dependent basal SOCE activity, as well as STIM1-mediated SOCE
            activity.
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Lodola,F., Laforenza,U., Bonetti,E., Lim,D., Dragoni,S.,
            Bottino,C., Ong,H.L., Guerra,G., Ganini,C., Massa,M., Manzoni,M.,
            Ambudkar,I.S., Genazzani,A.A., Rosti,V., Pedrazzoli,P., Tanzi,F.,
            Moccia,F. and Porta,C.
  TITLE     Store-operated Ca2+ entry is remodelled and controls in vitro
            angiogenesis in endothelial progenitor cells isolated from tumoral
            patients
  JOURNAL   PLoS One 7 (9), e42541 (2012)
   PUBMED   23049731
  REMARK    GeneRIF: Store-operated Ca2+ entry is remodelled and controls in
            vitro angiogenesis in endothelial progenitor cells isolated from
            tumoral patients.
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Chen,J., Sun,M., Lee,S., Zhou,G., Rowley,J.D. and Wang,S.M.
  TITLE     Identifying novel transcripts and novel genes in the human genome
            by using novel SAGE tags
  JOURNAL   Proc Natl Acad Sci U S A 99 (19), 12257-12262 (2002)
   PUBMED   12213963
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC359554.1, AK315956.1, AC044849.12 and BM280420.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005273586.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and 5'
            coding region which results in the use of a downstream start codon
            compared to variant 1. The encoded isoform (2) has a shorter
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.208631.1,
                                           SRR1660809.133803.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..167
                     /product="store-operated calcium entry-associated
                     regulatory factor isoform 2"
                     /note="HBV XAg-transactivated protein 3; HBV
                     X-transactivated gene 3 protein; SOCE-associated
                     regulatory factor; transmembrane protein 66; testicular
                     secretory protein Li 59"
                     /calculated_mol_wt=17745
     Region          <1..167
                     /region_name="SARAF"
                     /note="SOCE-associated regulatory factor of calcium
                     homoeostasis; pfam06682"
                     /db_xref="CDD:461985"
     CDS             1..167
                     /gene="SARAF"
                     /gene_synonym="FOAP-7; HSPC035; TMEM66; XTP3"
                     /coded_by="NM_001284239.1:597..1100"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64866.1"
                     /db_xref="GeneID:51669"
                     /db_xref="HGNC:HGNC:28789"
                     /db_xref="MIM:614768"
ORIGIN      
        1 msglitivvl lgiafvvykl flsdgqyspp pyseyppfsh ryqrftnsag ppppgfksef
       61 tgpqntghga tsgfgsaftg qqgyensgpg fwtglgtggi lgylfgsnra atpfsdswyy
      121 psyppsypgt wnraysplhg gsgsysvcsn sdtktrtasg yggtrrr
//
LOCUS       NP_963291                933 aa            linear   PRI 20-NOV-2025
DEFINITION  diacylglycerol kinase zeta isoform 3 [Homo sapiens].
ACCESSION   NP_963291
VERSION     NP_963291.2
DBSOURCE    REFSEQ: accession NM_201533.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Harris,R.A., Bush,A.H., Eagar,T.N., Qian,J., Greenwood,M.P.,
            Opekun,A.R., Baldassano,R., Guthery,S.L., Noe,J.D., Otley,A.,
            Rosh,J.R., Kugathasan,S. and Kellermayer,R.
  TITLE     Exome Sequencing Implicates DGKZ, ESRRA, and GXYLT1 for Modulating
            Granuloma Formation in Crohn Disease
  JOURNAL   J Pediatr Gastroenterol Nutr 77 (3), 354-357 (2023)
   PUBMED   37347142
  REMARK    GeneRIF: Exome Sequencing Implicates DGKZ , ESRRA , and GXYLT1 for
            Modulating Granuloma Formation in Crohn Disease.
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Liu,X.F., Zhao,S.W., Cui,J.J., Gu,Y.W., Fan,J.W., Fu,Y.F.,
            Zhang,Y.H., Yin,H., Chen,K. and Cui,L.B.
  TITLE     Differential expression of diacylglycerol kinase zeta is involved
            in inferior parietal lobule-related dysfunction in schizophrenia
            with cognitive impairments
  JOURNAL   BMC Psychiatry 23 (1), 526 (2023)
   PUBMED   37479996
  REMARK    GeneRIF: Differential expression of diacylglycerol kinase zeta is
            involved in inferior parietal lobule-related dysfunction in
            schizophrenia with cognitive impairments.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Furuta,M., Murakami,C., Numagami,Y., Suzuki,R. and Sakane,F.
  TITLE     Diacylglycerol kinase zeta interacts with sphingomyelin synthase 1
            and sphingomyelin synthase-related protein via different regions
  JOURNAL   FEBS Open Bio 13 (7), 1333-1345 (2023)
   PUBMED   37166445
  REMARK    GeneRIF: Diacylglycerol kinase zeta interacts with sphingomyelin
            synthase 1 and sphingomyelin synthase-related protein via different
            regions.
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Yamazaki,A., Kawashima,A., Honda,T., Kohama,T., Murakami,C.,
            Sakane,F., Murayama,T. and Nakamura,H.
  TITLE     Identification and characterization of diacylglycerol kinase zeta
            as a novel enzyme producing ceramide-1-phosphate
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1868 (6), 159307 (2023)
   PUBMED   36906254
  REMARK    GeneRIF: Identification and characterization of diacylglycerol
            kinase zeta as a novel enzyme producing ceramide-1-phosphate.
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Topham,M.K. and Prescott,S.M.
  TITLE     Diacylglycerol kinase zeta regulates Ras activation by a novel
            mechanism
  JOURNAL   J Cell Biol 152 (6), 1135-1143 (2001)
   PUBMED   11257115
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Liu,Z., Chang,G.Q. and Leibowitz,S.F.
  TITLE     Diacylglycerol kinase zeta in hypothalamus interacts with long form
            leptin receptor. Relation to dietary fat and body weight regulation
  JOURNAL   J Biol Chem 276 (8), 5900-5907 (2001)
   PUBMED   11078732
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Topham,M.K., Bunting,M., Zimmerman,G.A., McIntyre,T.M.,
            Blackshear,P.J. and Prescott,S.M.
  TITLE     Protein kinase C regulates the nuclear localization of
            diacylglycerol kinase-zeta
  JOURNAL   Nature 394 (6694), 697-700 (1998)
   PUBMED   9716136
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Ding,L., Bunting,M., Topham,M.K., McIntyre,T.M., Zimmerman,G.A. and
            Prescott,S.M.
  TITLE     Alternative splicing of the human diacylglycerol kinase zeta gene
            in muscle
  JOURNAL   Proc Natl Acad Sci U S A 94 (11), 5519-5524 (1997)
   PUBMED   9159104
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Bunting,M., Tang,W., Zimmerman,G.A., McIntyre,T.M. and
            Prescott,S.M.
  TITLE     Molecular cloning and characterization of a novel human
            diacylglycerol kinase zeta
  JOURNAL   J Biol Chem 271 (17), 10230-10236 (1996)
   PUBMED   8626588
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC416889.1, AK300577.1 and
            U51477.1.
            
            On Dec 1, 2010 this sequence version replaced NP_963291.1.
            
            Summary: The protein encoded by this gene belongs to the eukaryotic
            diacylglycerol kinase family. It may attenuate protein kinase C
            activity by regulating diacylglycerol levels in intracellular
            signaling cascade and signal transduction. Alternative splicing
            occurs at this locus and multiple transcript variants encoding
            distinct isoforms have been identified. [provided by RefSeq, Nov
            2010].
            
            Transcript Variant: This variant (3) has an alternate 5' sequence
            including the coding region, lacks nts GAG at an alternate splice
            site and has extra nts CAG at another alternate splice sites in the
            CDS, compared to variant 4. The resulting isoform (3) has a shorter
            and distinct N-terminus, lacks an internal aa in one region and has
            an additional aa in another region, compared to isoform 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300577.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..933
                     /product="diacylglycerol kinase zeta isoform 3"
                     /EC_number="2.7.1.107"
                     /EC_number="2.7.1.93"
                     /note="diacylglycerol kinase, zeta 104kDa; DAG kinase
                     zeta; diglyceride kinase zeta"
                     /calculated_mol_wt=104166
     Region          93..165
                     /region_name="C1_DGKzeta_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase zeta (DAG kinase
                     zeta) and similar proteins; cd20849"
                     /db_xref="CDD:410399"
     Region          175..249
                     /region_name="C1_DGKzeta_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in diacylglycerol kinase zeta (DAG kinase
                     zeta) and similar proteins; cd20895"
                     /db_xref="CDD:410445"
     Region          302..423
                     /region_name="DAGKc"
                     /note="Diacylglycerol kinase catalytic domain (presumed);
                     smart00046"
                     /db_xref="CDD:214487"
     Region          451..608
                     /region_name="DAGKa"
                     /note="Diacylglycerol kinase accessory domain (presumed);
                     smart00045"
                     /db_xref="CDD:214486"
     Region          <799..>915
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          799..825
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(800..801,804..806,808..809,813,816,825,827,829,
                     833..834,837..839,841..842,846,849,860,862,864,868..869,
                     872..874,876..877,881,884)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          827..860
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          862..887
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..933
                     /gene="DGKZ"
                     /gene_synonym="DAGK5; DAGK6; DGK-ZETA; hDGKzeta"
                     /coded_by="NM_201533.3:144..2945"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS44579.2"
                     /db_xref="GeneID:8525"
                     /db_xref="HGNC:HGNC:2857"
                     /db_xref="MIM:601441"
ORIGIN      
        1 msapgaghsa ggscnessal gpvealgtee gerpgslrqm wryrswdvpq ipseapqtqk
       61 aitksglqhl apppptpgap cseserqirs tvdwssatyg ehiwfetnvs gdfcyvgeqy
      121 cvarmlqksv srrkcaacki vvhtpcieql ekinfrckps fresgsrnvr eptfvrhhwv
      181 hrrrqdgkcr hcgkgfqqkf tfhskeivai scswckqayh skvscfmlqq ieepcslgvh
      241 aavvipptwi lrarrpqntl kaskkkkras fkrksskkgp eegrwrpfii rptpsplmkp
      301 llvfvnpksg gnqgakiiqs flwylnprqv fdlsqggpke alemyrkvhn lrilacggdg
      361 tvgwilstld qlrlkppppv ailplgtgnd lartlnwggg ytdepvskil shveegnvvq
      421 ldrwdlhaep npeagpedrd egatdrlpld vfnnyfslgf dahvtlefhe sreanpekfn
      481 srfrnkmfya gtafsdflmg sskdlakhir vvcdgmdltp kiqdlkpqcv vflnipryca
      541 gtmpwghpge hhdfepqrhd dgylevigft mtslaalqvg ghgerltqcr evvlttskai
      601 pvqvdgepck laasririal rnqatmvqka krrsaaplhs dqqpvpeqlr iqvsrvsmhd
      661 yealhydkeq lkeasvplgt vvvpgdsdle lcrahierlq qepdgagaks ptcqklspkw
      721 cfldattasr fyridraqeh lnyvteiaqd eiyildpell gasarpdlpt ptsplptspc
      781 sptprslqgd aappqgeeli eaakrndfck lqelhraggd lmhrdeqsrt llhhavstgs
      841 kdvvrylldh appeildave engetclhqa aalgqrtich yiveagaslm ktdqqgdtpr
      901 qraekaqdte laaylenrqh yqmiqredqe tav
//
LOCUS       NP_001305290             709 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-4 isoform d [Homo sapiens].
ACCESSION   NP_001305290 XP_005274438
VERSION     NP_001305290.1
DBSOURCE    REFSEQ: accession NM_001318361.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Wu,S., Jin,J., Huang,J., Chen,G. and Chen,Y.
  TITLE     Comprehensive analysis of the RSK gene family in acute myeloid
            leukemia determines a prognostic signature for the prediction of
            clinical prognosis and treatment responses
  JOURNAL   Hematology 28 (1), 2235833 (2023)
   PUBMED   37462338
  REMARK    GeneRIF: Comprehensive analysis of the RSK gene family in acute
            myeloid leukemia determines a prognostic signature for the
            prediction of clinical prognosis and treatment responses.
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Qiu,M., Lin,Q., Liu,Y., Chen,P., Zhou,Y., Jiang,Y., Zhou,Z.,
            Wen,Q., Zhou,X., Liang,X., Gan,H. and Yu,H.
  TITLE     Potentially functional genetic variants in RPS6KA4 and MAP2K5 in
            the MAPK signaling pathway predict HBV-related hepatocellular
            carcinoma survival
  JOURNAL   Mol Carcinog 62 (9), 1378-1387 (2023)
   PUBMED   37278562
  REMARK    GeneRIF: Potentially functional genetic variants in RPS6KA4 and
            MAP2K5 in the MAPK signaling pathway predict HBV-related
            hepatocellular carcinoma survival.
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Sattarifard,H., Safaei,A., Khazeeva,E., Rastegar,M. and Davie,J.R.
  TITLE     Mitogen- and stress-activated protein kinase (MSK1/2) regulated
            gene expression in normal and disease states
  JOURNAL   Biochem Cell Biol 101 (3), 204-219 (2023)
   PUBMED   36812480
  REMARK    GeneRIF: Mitogen- and stress-activated protein kinase (MSK1/2)
            regulated gene expression in normal and disease states.
            Review article
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Akbar,N., Forteath,C., Hussain,M.S., Reyskens,K., Belch,J.J.F.,
            Lang,C.C., Mordi,I.R., Bhalraam,U., Arthur,J.S.C. and Khan,F.
  TITLE     Mitogen and Stress-Activated Kinases 1 and 2 Mediate Endothelial
            Dysfunction
  JOURNAL   Int J Mol Sci 22 (16), 8655 (2021)
   PUBMED   34445361
  REMARK    GeneRIF: Mitogen and Stress-Activated Kinases 1 and 2 Mediate
            Endothelial Dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Du,K. and Montminy,M.
  TITLE     CREB is a regulatory target for the protein kinase Akt/PKB
  JOURNAL   J Biol Chem 273 (49), 32377-32379 (1998)
   PUBMED   9829964
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Zhu,S. and Gerhard,D.S.
  TITLE     A transcript map of an 800-kb region on human chromosome 11q13,
            part of the candidate region for SCA5 and BBS1
  JOURNAL   Hum Genet 103 (6), 674-680 (1998)
   PUBMED   9921902
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Pierrat,B., Correia,J.S., Mary,J.L., Tomas-Zuber,M. and
            Lesslauer,W.
  TITLE     RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase
            under dominant control of p38alpha mitogen-activated protein kinase
            (p38alphaMAPK)
  JOURNAL   J Biol Chem 273 (45), 29661-29671 (1998)
   PUBMED   9792677
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Deak,M., Clifton,A.D., Lucocq,L.M. and Alessi,D.R.
  TITLE     Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
            activated by MAPK and SAPK2/p38, and may mediate activation of CREB
  JOURNAL   EMBO J 17 (15), 4426-4441 (1998)
   PUBMED   9687510
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Xing,J., Ginty,D.D. and Greenberg,M.E.
  TITLE     Coupling of the RAS-MAPK pathway to gene activation by RSK2, a
            growth factor-regulated CREB kinase
  JOURNAL   Science 273 (5277), 959-963 (1996)
   PUBMED   8688081
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI253655.1, AK298507.1,
            AP003774.4 and AJ010119.1.
            
            On Jan 5, 2016 this sequence version replaced XP_005274438.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            non-identical kinase catalytic domains and phosphorylates various
            substrates, including CREB1 and ATF1. The encoded protein can also
            phosphorylate histone H3 to regulate certain inflammatory genes.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (4) uses an alternate splice
            junction in the 5' end compared to variant 1. The resulting isoform
            (d) is shorter at the N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298507.1, SRR9304718.196908.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..709
                     /product="ribosomal protein S6 kinase alpha-4 isoform d"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein kinase B; mitogen- and
                     stress-activated protein kinase 2; ribosomal protein S6
                     kinase, 90kDa, polypeptide 4; ribosomal protein S6 kinase
                     alpha-4; 90 kDa ribosomal protein S6 kinase 4; nuclear
                     mitogen- and stress-activated protein kinase 2"
                     /calculated_mol_wt=78695
     Region          1..301
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          341..651
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(354..357,360,362,375,377,404,420..423,467,471..472,
                     474,487..488)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271082"
     CDS             1..709
                     /gene="RPS6KA4"
                     /gene_synonym="MSK2; RSK-B; S6K-alpha-4"
                     /coded_by="NM_001318361.2:218..2347"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:8986"
                     /db_xref="HGNC:HGNC:10433"
                     /db_xref="MIM:603606"
ORIGIN      
        1 mkvlrkaalv qraktqehtr tersvlelvr qapflvtlhy afqtdaklhl ildyvsggem
       61 fthlyqrqyf keaevrvygg eivlalehlh klgiiyrdlk lenvlldseg hivltdfgls
      121 keflteeker tfsfcgtiey mapeiirskt ghgkavdwws lgillfellt gaspftlege
      181 rntqaevsrr ilkcsppfpp rigpvaqdll qrllckdpkk rlgagpqgaq evrnhpffqg
      241 ldwvalaark ipapfrpqir seldvgnfae eftrlepvys ppgspppgdp rifqgysfva
      301 psilfdhnna vmtdgleapg agdrpgraav arsammqdsp ffqqyeldlr epalgqgsfs
      361 vcrrcrqrqs gqefavkils rrleantqre vaalrlcqsh pnvvnlhevh hdqlhtylvl
      421 ellrggelle hirkkrhfse seasqilrsl vsavsfmhee agvvhrdlkp enilyaddtp
      481 gapvkiidfg farlrpqspg vpmqtpcftl qyaapellaq qgydescdlw slgvilymml
      541 sgqvpfqgas gqggqsqaae imckiregrf sldgeawqgv seeakelvrg lltvdpakrl
      601 kleglrgssw lqdgsarssp plrtpdvles sgpavrsgln atfmafnrgk regfflksve
      661 naplakrrkq klrsatasrr gspapanpgr apvaskgapr rangplpps
//
LOCUS       NP_001355002            1363 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFX7 isoform 2 [Homo sapiens].
ACCESSION   NP_001355002
VERSION     NP_001355002.1
DBSOURCE    REFSEQ: accession NM_001368073.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1363)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1363)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   3  (residues 1 to 1363)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1363)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 1363)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   6  (residues 1 to 1363)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1363)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1363)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1363)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1363)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068726.5, AC084783.2 and KF456052.1.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC112936.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1363
                     /product="DNA-binding protein RFX7 isoform 2"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=146765
     Region          8..86
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          <161..471
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          371..>648
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..1363
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_001368073.2:695..4786"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS92003.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 msssraqqmh afswirntle ehpetslpkq evydeyksyc dnlgyhplsa adfgkimknv
       61 fpnmkarrlg trgkskycys glrkkafvhm ptlpnldfhk tgdglegaep sgqlqnidee
      121 vissacrlvc ewaqkvlsqp fdtvlelarf lvkshyigtk smaaltvmaa apagmkgitq
      181 psafiptaes nsfqpqvktl pspidakqql qrkiqkkqqe qklqsplpge saakksesat
      241 sngvtnlpng npsilspqpi givvaavpsp ipvqrtrqlv tspspmsssd gkvlplnvqv
      301 vtqhmqsvkq apktpqnvpa spggdrsarh rypqilpkpa ntsaltirsp ttvlftsspi
      361 ktavvpashm sslnvvkmtt isltpsnsnt plkhsasvss atgtteesrs vpqikngsvv
      421 slqspgsrss saggtsavev kvepetssde hpvqcqensd eakapqtpsa llgqksntdg
      481 alqkpsnegv ieikatkvcd qrtkcksrcn emlpgtstgn nqstitlsva sqnltftsss
      541 sppngdsink dpklctkspr krlsstlqet qvppvkkpiv eqlsaatieg qkqgsvkkdq
      601 kvphsgkteg stagaqipsk vsvnvsshig anqplnssal visdsaleqq ttpssspdik
      661 vklegsvfll dsdsksvgsf npngwqqitk dsefisasce qqqdisvmti pehsdindle
      721 ksvwelegmp qdtysqqlhs qiqesslnqi qahssdqlpl qselkefeps vsqtnesyfp
      781 fddeltqdsi veelvlmeqq msmnnshsyg nclgmtlqsq svtpgapmss htssthfyhp
      841 ihsngtpiht ptptptptpt ptptptptse miagsqslsr espcsrlaqt tpvdsalgss
      901 rhtpigtphs ncsssvppsp vecrnpfaft pisssmayhd asivssspvk pmqrpmathp
      961 dktklewmnn gysgvgnssv sghgilpsyq elvedrfrkp hafavpgqsy qsqsrhhdth
     1021 fgrltpvspv qhqgatvnnt nkqegfavpa pldnkgtnss assnfrcrsv spavhrqrnl
     1081 sgstlypvsn iprsnvtpfg spvtpevhvf tnvhtdacan niaqrsqsvp ltvmmqtafp
     1141 nalqkqansk kitnvllskl dsdnddavrg lgmnnlpsny tarmnltqil epstvfpsan
     1201 pqnmidssts vyefqtpsyl tksnstgqin fspgdnqaqs eigeqqldfn stvkdllsgd
     1261 slqtnqqlvg qgasdltnta sdfssdirls selsgsindl ntldpnllfd pgrqqgqdde
     1321 atleelkndp lfqqicsesm nsmtssgfew ieskdhptve mlg
//
LOCUS       NP_001357490            1460 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFX7 isoform 1 [Homo sapiens].
ACCESSION   NP_001357490
VERSION     NP_001357490.1
DBSOURCE    REFSEQ: accession NM_001370561.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068726.5, AC084783.2 and KF456052.1.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.239107.1, SRR1803611.169829.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1460
                     /product="DNA-binding protein RFX7 isoform 1"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=157221
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          43..100
                     /region_name="RFX5_N"
                     /note="RFX5 N-terminal domain; pfam18326"
                     /db_xref="CDD:375753"
     Region          105..183
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          188..193
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and RFXANK. /evidence=ECO:0000269|PubMed:25752541,
                     ECO:0000312|PDB:6MEW"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          <258..568
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          308..352
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          404..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          468..>745
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     Region          481..585
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          632..715
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            704
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Region          917..1015
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            988
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q2KHR2.2)"
     CDS             1..1460
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_001370561.1:575..4957"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92005.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 maeeqqqppp qqpdahqqlp psapnsgval palvpglpgt easalqhkik nsicktvqsk
       61 vdcilqevek ftdleklyly lqlpsglsng eksdqnamss sraqqmhafs wirntleehp
      121 etslpkqevy deyksycdnl gyhplsaadf gkimknvfpn mkarrlgtrg kskycysglr
      181 kkafvhmptl pnldfhktgd glegaepsgq lqnideevis sacrlvcewa qkvlsqpfdt
      241 vlelarflvk shyigtksma altvmaaapa gmkgitqpsa fiptaesnsf qpqvktlpsp
      301 idakqqlqrk iqkkqqeqkl qsplpgesaa kksesatsng vtnlpngnps ilspqpigiv
      361 vaavpspipv qrtrqlvtsp spmsssdgkv lplnvqvvtq hmqsvkqapk tpqnvpaspg
      421 gdrsarhryp qilpkpants altirspttv lftsspikta vvpashmssl nvvkmttisl
      481 tpsnsntplk hsasvssatg tteesrsvpq ikngsvvslq spgsrsssag gtsavevkve
      541 petssdehpv qcqensdeak apqtpsallg qksntdgalq kpsnegviei katkvcdqrt
      601 kcksrcneml pgtstgnnqs titlsvasqn ltftsssspp ngdsinkdpk lctksprkrl
      661 sstlqetqvp pvkkpiveql saatiegqkq gsvkkdqkvp hsgktegsta gaqipskvsv
      721 nvsshiganq plnssalvis dsaleqqttp ssspdikvkl egsvflldsd sksvgsfnpn
      781 gwqqitkdse fisasceqqq disvmtipeh sdindleksv welegmpqdt ysqqlhsqiq
      841 esslnqiqah ssdqlplqse lkefepsvsq tnesyfpfdd eltqdsivee lvlmeqqmsm
      901 nnshsygncl gmtlqsqsvt pgapmsshts sthfyhpihs ngtpihtptp tptptptptp
      961 tptptsemia gsqslsresp csrlaqttpv dsalgssrht pigtphsncs ssvppspvec
     1021 rnpfaftpis ssmayhdasi vssspvkpmq rpmathpdkt klewmnngys gvgnssvsgh
     1081 gilpsyqelv edrfrkphaf avpgqsyqsq srhhdthfgr ltpvspvqhq gatvnntnkq
     1141 egfavpapld nkgtnssass nfrcrsvspa vhrqrnlsgs tlypvsnipr snvtpfgspv
     1201 tpevhvftnv htdacannia qrsqsvpltv mmqtafpnal qkqanskkit nvllskldsd
     1261 nddavrglgm nnlpsnytar mnltqileps tvfpsanpqn midsstsvye fqtpsyltks
     1321 nstgqinfsp gdnqaqseig eqqldfnstv kdllsgdslq tnqqlvgqga sdltntasdf
     1381 ssdirlssel sgsindlntl dpnllfdpgr qqgqddeatl eelkndplfq qicsesmnsm
     1441 tssgfewies kdhptvemlg
//
LOCUS       NP_001001342              99 aa            linear   PRI 20-NOV-2025
DEFINITION  biogenesis of lysosome-related organelles complex 1 subunit 2
            isoform 2 [Homo sapiens].
ACCESSION   NP_001001342
VERSION     NP_001001342.1
DBSOURCE    REFSEQ: accession NM_001001342.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Yordanov,T.E., Hipolito,V.E.B., Liebscher,G., Vogel,G.F.,
            Stasyk,T., Herrmann,C., Geley,S., Teis,D., Botelho,R.J., Hess,M.W.
            and Huber,L.A.
  TITLE     Biogenesis of lysosome-related organelles complex-1 (BORC)
            regulates late endosomal/lysosomal size through PIKfyve-dependent
            phosphatidylinositol-3,5-bisphosphate
  JOURNAL   Traffic 20 (9), 674-696 (2019)
   PUBMED   31314175
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Wang,Z., Wei,H., Yu,Y., Sun,J., Yang,Y., Xing,G., Wu,S., Zhou,Y.,
            Zhu,Y., Zhang,C., Zhou,T., Zhao,X., Sun,Q. and He,F.
  TITLE     Characterization of Ceap-11 and Ceap-16, two novel
            splicing-variant-proteins, associated with centrosome, microtubule
            aggregation and cell proliferation
  JOURNAL   J Mol Biol 343 (1), 71-82 (2004)
   PUBMED   15381421
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
  REMARK    GeneRIF: Biogenesis of lysosome-related organelles complex-1
            (BLOC-1) subunit 2 (BLOS2).BLOC-1 is required for the biogenesis of
            melanosomes and platelet dense granules.
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Li,W., Zhang,Q., Oiso,N., Novak,E.K., Gautam,R., O'Brien,E.P.,
            Tinsley,C.L., Blake,D.J., Spritz,R.A., Copeland,N.G., Jenkins,N.A.,
            Amato,D., Roe,B.A., Starcevic,M., Dell'Angelica,E.C., Elliott,R.W.,
            Mishra,V., Kingsmore,S.F., Paylor,R.E. and Swank,R.T.
  TITLE     Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
            dysbindin, a member of the biogenesis of lysosome-related
            organelles complex 1 (BLOC-1)
  JOURNAL   Nat Genet 35 (1), 84-89 (2003)
   PUBMED   12923531
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Ciciotte,S.L., Gwynn,B., Moriyama,K., Huizing,M., Gahl,W.A.,
            Bonifacino,J.S. and Peters,L.L.
  TITLE     Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a
            novel protein that is part of the pallidin-muted complex (BLOC-1)
  JOURNAL   Blood 101 (11), 4402-4407 (2003)
   PUBMED   12576321
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Moriyama,K. and Bonifacino,J.S.
  TITLE     Pallidin is a component of a multi-protein complex involved in the
            biogenesis of lysosome-related organelles
  JOURNAL   Traffic 3 (9), 666-677 (2002)
   PUBMED   12191018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY107885.1, AK054697.1, AL138921.14 and BX112121.1.
            
            Summary: This gene encodes a protein with multiple functions. The
            encoded protein has been found in association with the centrosome,
            shown to co-localize with gamma-tubulin, and also found to be one
            of the proteins in the BLOC-1 complex which functions in the
            formation of lysosome-related organelles. A pseudogene of this gene
            is located on the X chromosome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (2) uses an alternate 5' exon
            structure and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG and result in an isoform (2) with a
            shorter N-terminus, compared to isoform 1. Variants 2, 4, and 5
            encode the same isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK054697.1, BC020494.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2148093 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..99
                     /product="biogenesis of lysosome-related organelles
                     complex 1 subunit 2 isoform 2"
                     /note="centrosome protein oncogene; biogenesis of
                     lysosome-related organelles complex 1 subunit 2;
                     centrosomal 10 kDa protein; BLOC-1 subunit 2; 11 kDa
                     centrosome associated protein"
                     /calculated_mol_wt=11358
     Region          1..94
                     /region_name="BLOC1_2"
                     /note="Biogenesis of lysosome-related organelles complex-1
                     subunit 2; pfam10046"
                     /db_xref="CDD:462951"
     CDS             1..99
                     /gene="BLOC1S2"
                     /gene_synonym="BLOS2; BORCS2; CEAP; CEAP11"
                     /coded_by="NM_001001342.2:226..525"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:282991"
                     /db_xref="HGNC:HGNC:20984"
                     /db_xref="MIM:609768"
ORIGIN      
        1 mfskmatylt geltatsedy kllenmnklt slkylemkdi ainisrnlkd lnqkyaglqp
       61 yldqinviee qvaaleqaay kldayskkle akykklekr
//
LOCUS       NP_071448                207 aa            linear   PRI 20-NOV-2025
DEFINITION  protein lin-7 homolog B isoform 1 [Homo sapiens].
ACCESSION   NP_071448
VERSION     NP_071448.1
DBSOURCE    REFSEQ: accession NM_022165.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 207)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 207)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 207)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 207)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 207)
  AUTHORS   Mizuno,M., Matsumoto,A., Hamada,N., Ito,H., Miyauchi,A.,
            Jimbo,E.F., Momoi,M.Y., Tabata,H., Yamagata,T. and Nagata,K.
  TITLE     Role of an adaptor protein Lin-7B in brain development: possible
            involvement in autism spectrum disorders
  JOURNAL   J Neurochem 132 (1), 61-69 (2015)
   PUBMED   25196215
  REMARK    GeneRIF: functional deficiency in Lin-7B could be implicated in
            clinical phenotypes in some autism spectrum disorders patients
            through bringing about abnormal cortical architecture
REFERENCE   6  (residues 1 to 207)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 207)
  AUTHORS   Coussen,F., Normand,E., Marchal,C., Costet,P., Choquet,D.,
            Lambert,M., Mege,R.M. and Mulle,C.
  TITLE     Recruitment of the kainate receptor subunit glutamate receptor 6 by
            cadherin/catenin complexes
  JOURNAL   J Neurosci 22 (15), 6426-6436 (2002)
   PUBMED   12151522
REFERENCE   8  (residues 1 to 207)
  AUTHORS   Olsen,O., Liu,H., Wade,J.B., Merot,J. and Welling,P.A.
  TITLE     Basolateral membrane expression of the Kir 2.3 channel is
            coordinated by PDZ interaction with Lin-7/CASK complex
  JOURNAL   Am J Physiol Cell Physiol 282 (1), C183-C195 (2002)
   PUBMED   11742811
REFERENCE   9  (residues 1 to 207)
  AUTHORS   Jo,K., Derin,R., Li,M. and Bredt,D.S.
  TITLE     Characterization of MALS/Velis-1, -2, and -3: a family of mammalian
            LIN-7 homologs enriched at brain synapses in association with the
            postsynaptic density-95/NMDA receptor postsynaptic complex
  JOURNAL   J Neurosci 19 (11), 4189-4199 (1999)
   PUBMED   10341223
REFERENCE   10 (residues 1 to 207)
  AUTHORS   Butz,S., Okamoto,M. and Sudhof,T.C.
  TITLE     A tripartite protein complex with the potential to couple synaptic
            vesicle exocytosis to cell adhesion in brain
  JOURNAL   Cell 94 (6), 773-782 (1998)
   PUBMED   9753324
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY358744.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358744.1, SRR5189661.15876.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221459.7/ ENSP00000221459.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..207
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..207
                     /product="protein lin-7 homolog B isoform 1"
                     /note="protein lin-7 homolog B; hLin7B; hVeli2; veli-2;
                     vertebrate lin-7 homolog 2; mammalian lin-seven protein 2;
                     lin-7 homolog B, crumbs cell polarity complex component;
                     mammalian LIN-7 2; vertebrate LIN7 homolog 2"
                     /calculated_mol_wt=22765
     Region          1..13
                     /region_name="Kinase interacting site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAP6.1)"
     Region          14..66
                     /region_name="L27"
                     /note="L27 domain; pfam02828"
                     /db_xref="CDD:460717"
     Region          90..175
                     /region_name="PDZ_Lin-7-like"
                     /note="PDZ domain of protein Lin-7 and related domains;
                     cd06796"
                     /db_xref="CDD:467258"
     Site            order(102..108,120,123,153,157,160..161)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467258"
     Region          187..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAP6.1)"
     CDS             1..207
                     /gene="LIN7B"
                     /gene_synonym="LIN-7B; MALS-2; MALS2; VELI2"
                     /coded_by="NM_022165.3:36..659"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12757.1"
                     /db_xref="GeneID:64130"
                     /db_xref="HGNC:HGNC:17788"
                     /db_xref="MIM:612331"
ORIGIN      
        1 maalveplgl erdvsravel lerlqrsgel ppqklqalqr vlqsrfcsai revyeqlydt
       61 lditgsaeir ahatakatva aftaseghah prvvelpktd eglgfnimgg keqnspiyis
      121 rvipggvadr hgglkrgdql lsvngvsveg eqhekavell kaaqgsvklv vrytprvlee
      181 mearfekmrs arrrqqhqsy sslesrg
//
LOCUS       NP_003395                246 aa            linear   PRI 20-NOV-2025
DEFINITION  14-3-3 protein beta/alpha [Homo sapiens].
ACCESSION   NP_003395 NP_054771
VERSION     NP_003395.1
DBSOURCE    REFSEQ: accession NM_003404.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Nan,L., Kaisi,F., Mengzhen,Z., Yang,Y., Jiaming,Y., Huirong,Y.,
            Xinwei,H., Chen,W., Liucheng,Y. and Kai,W.
  TITLE     miR-375-3p targets YWHAB to attenuate intestine injury in neonatal
            necrotizing enterocolitis
  JOURNAL   Pediatr Surg Int 40 (1), 63 (2024)
   PUBMED   38431920
  REMARK    GeneRIF: miR-375-3p targets YWHAB to attenuate intestine injury in
            neonatal necrotizing enterocolitis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Iglesias-Martinez,L.F., Rauch,N., Wynne,K., McCann,B., Kolch,W. and
            Rauch,J.
  TITLE     Interactome dynamics of RAF1-BRAF kinase monomers and dimers
  JOURNAL   Sci Data 10 (1), 203 (2023)
   PUBMED   37045861
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Conklin,D.S., Galaktionov,K. and Beach,D.
  TITLE     14-3-3 proteins associate with cdc25 phosphatases
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7892-7896 (1995)
   PUBMED   7644510
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Aitken,A., Howell,S., Jones,D., Madrazo,J. and Patel,Y.
  TITLE     14-3-3 alpha and delta are the phosphorylated forms of
            raf-activating 14-3-3 beta and zeta. In vivo stoichiometric
            phosphorylation in brain at a Ser-Pro-Glu-Lys MOTIF
  JOURNAL   J Biol Chem 270 (11), 5706-5709 (1995)
   PUBMED   7890696
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Li,S., Janosch,P., Tanji,M., Rosenfeld,G.C., Waymire,J.C.,
            Mischak,H., Kolch,W. and Sedivy,J.M.
  TITLE     Regulation of Raf-1 kinase activity by the 14-3-3 family of
            proteins
  JOURNAL   EMBO J 14 (4), 685-696 (1995)
   PUBMED   7882972
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Fantl,W.J., Muslin,A.J., Kikuchi,A., Martin,J.A., MacNicol,A.M.,
            Gross,R.W. and Williams,L.T.
  TITLE     Activation of Raf-1 by 14-3-3 proteins
  JOURNAL   Nature 371 (6498), 612-614 (1994)
   PUBMED   7935795
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Roth,D., Morgan,A., Martin,H., Jones,D., Martens,G.J., Aitken,A.
            and Burgoyne,R.D.
  TITLE     Characterization of 14-3-3 proteins in adrenal chromaffin cells and
            demonstration of isoform-specific phospholipid binding
  JOURNAL   Biochem J 301 (Pt 1) (Pt 1), 305-310 (1994)
   PUBMED   8037685
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB443535.1, AK292717.1,
            AL008725.1 and AA845374.1.
            
            On Jun 6, 2003 this sequence version replaced NP_054771.1.
            
            Summary: This gene encodes a protein belonging to the 14-3-3 family
            of proteins, members of which mediate signal transduction by
            binding to phosphoserine-containing proteins. This highly conserved
            protein family is found in both plants and mammals. The encoded
            protein has been shown to interact with RAF1 and CDC25
            phosphatases, suggesting that it may play a role in linking
            mitogenic signaling and the cell cycle machinery. Two transcript
            variants, which encode the same protein, have been identified for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.46162.1, EU794580.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..246
                     /product="14-3-3 protein beta/alpha"
                     /note="tyrosine 3-monooxygenase/tryptophan 5-monooxygenase
                     activation protein, alpha polypeptide; 14-3-3 alpha;
                     protein kinase C inhibitor protein-1; protein 1054;
                     tyrosine 3-monooxygenase/tryptophan 5-monooxygenase
                     activation protein, beta polypeptide; epididymis secretory
                     protein Li 1"
                     /calculated_mol_wt=27951
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; N-acetylmethionine,
                     in 14-3-3 protein beta/alpha, alternate.
                     /evidence=ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P31946.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in 14-3-3 protein beta/alpha,
                     N-terminally processed.
                     /evidence=ECO:0000269|PubMed:25489052, ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Region          4..232
                     /region_name="14-3-3_beta_zeta"
                     /note="14-3-3 beta and zeta isoforms of 14-3-3 protein;
                     cd10022"
                     /db_xref="CDD:206758"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P27348; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            order(7,10..11,14..15,17..18,20,23,60,63,67,77,80..81,84,
                     87..88,91)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            order(43..44,47..48,51,119,122,129..130,167,171,174..175,
                     178,211..215,218..219,222,226)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            51
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P27348; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            58
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CQV8; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            117
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            129
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P68251; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P31946.3)"
     CDS             1..246
                     /gene="YWHAB"
                     /gene_synonym="GW128; HEL-S-1; HS1; KCIP-1; YWHAA"
                     /coded_by="NM_003404.5:281..1021"
                     /db_xref="CCDS:CCDS13339.1"
                     /db_xref="GeneID:7529"
                     /db_xref="HGNC:HGNC:12849"
                     /db_xref="MIM:601289"
ORIGIN      
        1 mtmdkselvq kaklaeqaer yddmaaamka vteqghelsn eernllsvay knvvgarrss
       61 wrvissieqk ternekkqqm gkeyrekiea elqdicndvl elldkylipn atqpeskvfy
      121 lkmkgdyfry lsevasgdnk qttvsnsqqa yqeafeiskk emqpthpirl glalnfsvfy
      181 yeilnspeka cslaktafde aiaeldtlne esykdstlim qllrdnltlw tsenqgdegd
      241 agegen
//
LOCUS       NP_001353583             573 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 3 [Homo sapiens].
ACCESSION   NP_001353583
VERSION     NP_001353583.1
DBSOURCE    REFSEQ: accession NM_001366654.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 573)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 573)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 573)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 573)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 573)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 573)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 573)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 573)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 573)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 573)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091928.3, AC011363.6 and AC008456.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295081.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142586,
                                           SAMEA2144335 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..573
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..573
                     /product="phospholipid-transporting ATPase VB isoform 3"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=66519
     Region          112..>499
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Region          473..>539
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     CDS             1..573
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001366654.2:405..2126"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 mrnyhflhmd tkmrtintet skrregergt rleiylsdlr lllemalsvd sswhrwqwrv
       61 rdgfphcpse ttpllspekg rqsynltqqr vvfpnnsifh qdweevsrry pgnrtcttky
      121 tlftflprnl feqfhrwanl yflflvilnw mpsmevfhre itmlplaivl fvimikdgme
      181 dfkrhrfdka incsniriye rkeqtyvqkc wkdvrvgdfi qmkcneivpa dilllfssdp
      241 ngichletas ldgetnlkqr cvvkgfsqqe vqfepelfhn tivcekpnnh lnkfkgymeh
      301 pdqtrtgfgc eslllrgcti rntemavgiv iyaghetkam lnnsgprykr skierrmnid
      361 iffcigilil mcligavghs iwngtfeehp pfdvpdangs flpsalggfy mfltmiillq
      421 vlipislyvs ielvklgqvf flsndldlyd eetdlsiqcr alniaedlgq iqyifsdktg
      481 tltenkmvfr rctimgseys hqengieapk gsiplskrky pallrneeik dillalleav
      541 whfhkllpvs lwsslsqira vpitcklsfv ykg
//
LOCUS       NP_004315                218 aa            linear   PRI 20-NOV-2025
DEFINITION  apoptosis regulator BAX isoform beta [Homo sapiens].
ACCESSION   NP_004315
VERSION     NP_004315.1
DBSOURCE    REFSEQ: accession NM_004324.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Dadsena,S., Cuevas Arenas,R., Vieira,G., Brodesser,S., Melo,M.N.
            and Garcia-Saez,A.J.
  TITLE     Lipid unsaturation promotes BAX and BAK pore activity during
            apoptosis
  JOURNAL   Nat Commun 15 (1), 4700 (2024)
   PUBMED   38830851
  REMARK    GeneRIF: Lipid unsaturation promotes BAX and BAK pore activity
            during apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Schweighofer,S.V., Jans,D.C., Keller-Findeisen,J., Folmeg,A.,
            Ilgen,P., Bates,M. and Jakobs,S.
  TITLE     Endogenous BAX and BAK form mosaic rings of variable size and
            composition on apoptotic mitochondria
  JOURNAL   Cell Death Differ 31 (4), 469-478 (2024)
   PUBMED   38503846
  REMARK    GeneRIF: Endogenous BAX and BAK form mosaic rings of variable size
            and composition on apoptotic mitochondria.
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Liu,X., Zhang,J., Wang,Z., Yan,M., Xu,M., Li,G., Shender,V.,
            Wei,J.J., Li,J., Shao,C., Zhang,S., Kong,B., Song,K. and Liu,Z.
  TITLE     Splicing Factor PQBP1 Curtails BAX Expression to Promote Ovarian
            Cancer Progression
  JOURNAL   Adv Sci (Weinh) 11 (15), e2306229 (2024)
   PUBMED   38342602
  REMARK    GeneRIF: Splicing Factor PQBP1 Curtails BAX Expression to Promote
            Ovarian Cancer Progression.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Chen,Y., Li,S., Yang,Z., Wang,T., Yin,F., Zhao,X. and Zhang,Y.
  TITLE     Value of Bax and Bcl2 expression in peripheral blood mononuclear
            cells for clinical prognosis of patients with chronic heart failure
  JOURNAL   Medicine (Baltimore) 103 (3), e36943 (2024)
   PUBMED   38241555
  REMARK    GeneRIF: Value of Bax and Bcl2 expression in peripheral blood
            mononuclear cells for clinical prognosis of patients with chronic
            heart failure.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Salomons,G.S., Buitenhuis,C.K., Martinez Munoz,C.,
            Verwijs-Jassen,M., Behrendt,H., Zsiros,J. and Smets,L.A.
  TITLE     Mutational analysis of Bax and Bcl-2 in childhood acute
            lymphoblastic leukaemia
  JOURNAL   Int J Cancer 79 (3), 273-277 (1998)
   PUBMED   9645350
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Apte,S.S., Mattei,M.G. and Olsen,B.R.
  TITLE     Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and
            isolation of a novel alternatively spliced transcript, BAX delta
  JOURNAL   Genomics 26 (3), 592-594 (1995)
   PUBMED   7607685
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Miyashita,T. and Reed,J.C.
  TITLE     Tumor suppressor p53 is a direct transcriptional activator of the
            human bax gene
  JOURNAL   Cell 80 (2), 293-299 (1995)
   PUBMED   7834749
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Krieger,N.S., Sessler,N.E. and Bushinsky,D.A.
  TITLE     Acidosis inhibits osteoblastic and stimulates osteoclastic activity
            in vitro
  JOURNAL   Am J Physiol 262 (3 Pt 2), F442-F448 (1992)
   PUBMED   1558161
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE396495.1, BC014175.2,
            T29044.1, BM706954.1 and AC026803.7.
            
            Summary: The protein encoded by this gene belongs to the BCL2
            protein family. BCL2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. This protein forms a
            heterodimer with BCL2, and functions as an apoptotic activator. The
            association and the ratio of BAX to BCL2 also determines survival
            or death of a cell following an apoptotic stimulus. This protein is
            reported to interact with, and increase the opening of, the
            mitochondrial voltage-dependent anion channel (VDAC), which leads
            to the loss in membrane potential and the release of cytochrome c.
            The expression of this gene is regulated by the tumor suppressor
            P53 and has been shown to be involved in P53-mediated apoptosis.
            Multiple alternatively spliced transcript variants, which encode
            different isoforms, have been reported for this gene. [provided by
            RefSeq, Dec 2019].
            
            Transcript Variant: This variant (beta) differs in the 3' coding
            region and 3' UTR, compared to variant 1. The resulting isoform
            (beta) has a shorter and distinct C-terminus, compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.213970.1,
                                           SRR3476690.335621.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..218
                     /product="apoptosis regulator BAX isoform beta"
                     /note="apoptosis regulator BAX; bcl2-L-4; bcl-2-like
                     protein 4; BCL2-associated X protein omega; Baxdelta2G9;
                     BCL2 associated X protein; Baxdelta2omega;
                     Baxdelta2G9omega; Baxdelta2(G8)-RFS protein"
                     /calculated_mol_wt=24089
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q07812.1)"
     Region          5..172
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          59..73
                     /region_name="BH3. /evidence=ECO:0000269|PubMed:8521816"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     Site            63..71
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(66..67,69..70,76,79..80,90..91,94..95,98..99,106,
                     108..109,111..112,116,120)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          98..118
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07812.1)"
     Site            order(98..100,105..117)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Site            150..163
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     CDS             1..218
                     /gene="BAX"
                     /gene_synonym="BCL2L4"
                     /coded_by="NM_004324.4:55..711"
                     /note="isoform beta is encoded by transcript variant beta"
                     /db_xref="CCDS:CCDS12744.1"
                     /db_xref="GeneID:581"
                     /db_xref="HGNC:HGNC:959"
                     /db_xref="MIM:600040"
ORIGIN      
        1 mdgsgeqprg ggptsseqim ktgalllqgf iqdragrmgg eapelaldpv pqdastkkls
       61 eclkrigdel dsnmelqrmi aavdtdspre vffrvaadmf sdgnfnwgrv valfyfaskl
      121 vlkalctkvp elirtimgwt ldflrerllg wiqdqggwvr llkpphphhr alttapapps
      181 lppatplgpw afwsrsqwcp lpifrssdvv ynafslrv
//
LOCUS       NP_001472                478 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 4 isoform a [Homo sapiens].
ACCESSION   NP_001472
VERSION     NP_001472.1
DBSOURCE    REFSEQ: accession NM_001481.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Wu,X., Jiang,T., Huang,R. and Xiao,X.
  TITLE     LncRNA GAS8-AS1 downregulates lncRNA NEAT1 to inhibit glioblastoma
            cell proliferation
  JOURNAL   Brain Behav 11 (6), e02128 (2021)
   PUBMED   33942556
  REMARK    GeneRIF: LncRNA GAS8-AS1 downregulates lncRNA NEAT1 to inhibit
            glioblastoma cell proliferation.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Ralston,K.S. and Hill,K.L.
  TITLE     Trypanin, a component of the flagellar Dynein regulatory complex,
            is essential in bloodstream form African trypanosomes
  JOURNAL   PLoS Pathog 2 (9), e101 (2006)
   PUBMED   17009870
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Colantonio,J.R., Bekker,J.M., Kim,S.J., Morrissey,K.M.,
            Crosbie,R.H. and Hill,K.L.
  TITLE     Expanding the role of the dynein regulatory complex to non-axonemal
            functions: association of GAS11 with the Golgi apparatus
  JOURNAL   Traffic 7 (5), 538-548 (2006)
   PUBMED   16643277
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Yeh,S.D., Chen,Y.J., Chang,A.C., Ray,R., She,B.R., Lee,W.S.,
            Chiang,H.S., Cohen,S.N. and Lin-Chao,S.
  TITLE     Isolation and properties of Gas8, a growth arrest-specific gene
            regulated during male gametogenesis to produce a protein associated
            with the sperm motility apparatus
  JOURNAL   J Biol Chem 277 (8), 6311-6317 (2002)
   PUBMED   11751847
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Hill,K.L., Hutchings,N.R., Grandgenett,P.M. and Donelson,J.E.
  TITLE     T lymphocyte-triggering factor of african trypanosomes is
            associated with the flagellar fraction of the cytoskeleton and
            represents a new family of proteins that are present in several
            divergent eukaryotes
  JOURNAL   J Biol Chem 275 (50), 39369-39378 (2000)
   PUBMED   10969087
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Whitmore,S.A., Settasatian,C., Crawford,J., Lower,K.M.,
            McCallum,B., Seshadri,R., Cornelisse,C.J., Moerland,E.W.,
            Cleton-Jansen,A.M., Tipping,A.J., Mathew,C.G., Savnio,M.,
            Savoia,A., Verlander,P., Auerbach,A.D., Van Berkel,C., Pronk,J.C.,
            Doggett,N.A. and Callen,D.F.
  TITLE     Characterization and screening for mutations of the growth
            arrest-specific 11 (GAS11) and C16orf3 genes at 16q24.3 in breast
            cancer
  JOURNAL   Genomics 52 (3), 325-331 (1998)
   PUBMED   9790751
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC104785.1, AF050079.1 and
            BX647947.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene includes 11 exons spanning 25 kb and maps to a
            region of chromosome 16 that is sometimes deleted in breast and
            prostrate cancer. The second intron contains an apparently
            intronless gene, C16orf3, that is transcribed in the opposite
            orientation. This gene is a putative tumor suppressor gene. Several
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Oct 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.260046.1, GQ891399.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268699.9/ ENSP00000268699.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..478
                     /product="dynein regulatory complex subunit 4 isoform a"
                     /note="growth arrest-specific protein 8; GAS-11; growth
                     arrest-specific protein 11; epididymis secretory sperm
                     binding protein; growth arrest specific 8"
                     /calculated_mol_wt=56225
     Region          1..114
                     /region_name="Regulates microtubule-binding.
                     /evidence=ECO:0000250|UniProtKB:Q60779"
                     /note="propagated from UniProtKB/Swiss-Prot (O95995.1)"
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95995.1)"
     Region          <54..>378
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          115..258
                     /region_name="Microtubule-binding.
                     /evidence=ECO:0000250|UniProtKB:Q60779"
                     /note="propagated from UniProtKB/Swiss-Prot (O95995.1)"
     Region          221..420
                     /region_name="GAS"
                     /note="Growth-arrest specific micro-tubule binding;
                     pfam13851"
                     /db_xref="CDD:464001"
     Region          357..478
                     /region_name="Interaction with SMO.
                     /evidence=ECO:0000269|PubMed:21659505"
                     /note="propagated from UniProtKB/Swiss-Prot (O95995.1)"
     CDS             1..478
                     /gene="DRC4"
                     /gene_synonym="CILD33; GAS11; GAS8"
                     /coded_by="NM_001481.3:43..1479"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10992.1"
                     /db_xref="GeneID:2622"
                     /db_xref="HGNC:HGNC:4166"
                     /db_xref="MIM:605178"
ORIGIN      
        1 mapkkkgkkg kakgtpivdg lapedmskeq veehvsrire eldrereern yfqlerdkih
       61 tfweitrrql eekkaelrnk dremeeaeer hqveikvykq kvkhllyehq nnltemkaeg
      121 tvvmklaqke hriqesvlrk dmralkvelk eqelasevvv knlrlkhtee itrmrndfer
      181 qvreieakyd kkmkmlrdel dlrrktelhe veerkngqih tlmqrheeaf tdiknyyndi
      241 tlnnlalins lkeqmedmrk kedhlerema evsgqnkrla dplqkareem semqkqlany
      301 erdkqillct karlkvreke lkdlqwehev leqrftkvqq erdelyrkft aaiqevqqkt
      361 gfknlvlerk lqalsaavek kevqfnevla asnldpaalt lvsrkledvl esknstikdl
      421 qyelaqvcka hndllrtyea kllafgipld nvgfkpleta vigqtlgqgp aglvgtpt
//
LOCUS       NP_001287828            1262 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-VI isoform 2 [Homo sapiens].
ACCESSION   NP_001287828 XP_005248782
VERSION     NP_001287828.1
DBSOURCE    REFSEQ: accession NM_001300899.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1262)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1262)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1262)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   4  (residues 1 to 1262)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1262)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1262)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 1262)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 1262)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 1262)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 1262)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB088907.1, U90236.2,
            AL136093.8 and AL392166.19.
            
            On Jul 16, 2014 this sequence version replaced XP_005248782.1.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) lacks two in-frame exons in
            the 3' coding region, compared to variant 1. It encodes isoform 2
            which has a shorter C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.265807.1,
                                           SRR1803614.175128.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..1262
                     /product="unconventional myosin-VI isoform 2"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=145918
     Region          71..759
                     /region_name="MYSc_Myo6"
                     /note="class VI myosin, motor domain; cd01382"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107,151..158,195..205,456..461)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276833"
     Site            151..158
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276833"
     Site            195..205
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276833"
     Site            456..461
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276833"
     Site            order(485..496,499..508)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276833"
     Site            693..703
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276833"
     Site            705..759
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276833"
     Region          770..917
                     /region_name="CBD_MYO6-like"
                     /note="calmodulin binding domain found in unconventional
                     myosin-VI and similar proteins; cd21759"
                     /db_xref="CDD:409646"
     Site            order(786,789..790,792..810,812..813,816..831,833,
                     836..837,840..841,886)
                     /site_type="other"
                     /note="calmodulin binding site [polypeptide binding]"
                     /db_xref="CDD:409646"
     Site            820..830
                     /site_type="other"
                     /note="IQ motif"
                     /db_xref="CDD:409646"
     Region          999..1067
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cd22294"
                     /db_xref="CDD:412090"
     Site            999..1024
                     /site_type="other"
                     /note="MIU motif"
                     /db_xref="CDD:412090"
     Region          1050..1090
                     /region_name="MyUb_Myo6"
                     /note="myosin VI ubiquitin-binding domain (MyUb) found in
                     unconventional myosin-VI and similar proteins; cd21958"
                     /db_xref="CDD:439319"
     Site            order(1055..1056,1058..1059,1085..1086,1088..1089)
                     /site_type="other"
                     /note="clathrin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Site            order(1058..1060,1063..1064,1066..1070,1072,1075..1076,
                     1079,1082..1083)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Region          1145..1235
                     /region_name="Myosin-VI_CBD"
                     /note="Myosin VI cargo binding domain; pfam16521"
                     /db_xref="CDD:465157"
     CDS             1..1262
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_001300899.2:233..4021"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75481.1"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveanplle afgnaktvrn nnssrfgkfv eihfnekssv vggfvshyll eksricvqgk
      241 eernyhifyr lcagasedir eklhlsspdn frylnrgctr yfanketdkq ilqnrkspey
      301 lkagsmkdpl lddhgdfirm ctamkkigld deekldlfrv vagvlhlgni dfeeagstsg
      361 gcnlknksaq sleycaellg ldqddlrvsl ttrvmlttag gtkgtvikvp lkveqannar
      421 dalaktvysh lfdhvvnrvn qcfpfetssy figvldiagf eyfehnsfeq fcinycnekl
      481 qqffnerilk eeqelyqkeg lgvnevhyvd nqdcidliea klvgildild eenrlpqpsd
      541 qhftsavhqk hkdhfrltip rksklavhrn irddegfiir hfagavcyet tqfveknnda
      601 lhmsleslic esrdkfirel fesstnnnkd tkqkagklsf isvgnkfktq lnllldklrs
      661 tgasfircik pnlkmtshhf egaqilsqlq csgmvsvldl mqggypsras fhelynmykk
      721 ympdklarld prlfckalfk alglnendyk fgltkvffrp gkfaefdqim ksdpdhlael
      781 vkrvnhwltc srwkkvqwcs lsviklknki kyraeacikm qktirmwlck rrhkpridgl
      841 vkvgtlkkrl dkfnevvsvl kdgkpemnkq iknleisidt lmakikstmm tqeqiqkeyd
      901 alvksseell salqkkkqqe eeaerlrriq eemekerkrr eedekrrrke eeerrmklem
      961 eakrkqeeee rkkreddekr iqaeveaqla rqkeeesqqq avleqerrdr elalriaqse
     1021 aelisdeaqa dlalrrgpav latkaaagtk kydlskwkya elrdtintsc diellaacre
     1081 efhrrlkvyh awksknkkrn teteqrapks vtdydfapfl nnspqqnpaa qiparqreie
     1141 mnrqqrffri pfirpadqyk dpqskkkgww yahfdgpwia rqmelhpdkp pillvagkdd
     1201 memcelnlee tgltrkrgae ilprqfeeiw ercggiqylq naiesrqarp tyatamlqsl
     1261 lk
//
LOCUS       NP_001164189             870 aa            linear   PRI 20-NOV-2025
DEFINITION  breast cancer anti-estrogen resistance protein 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001164189
VERSION     NP_001164189.1
DBSOURCE    REFSEQ: accession NM_001170718.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Delage,L., Lambert,M., Bardel,E., Kundlacz,C., Chartoire,D.,
            Conchon,A., Peugnet,A.L., Gorka,L., Auberger,P., Jacquel,A.,
            Soussain,C., Destaing,O., Delecluse,H.J., Delecluse,S., Merabet,S.,
            Traverse-Glehen,A., Salles,G., Bachy,E., Billaud,M.,
            Ghesquieres,H., Genestier,L., Rouault,J.P. and Sujobert,P.
  TITLE     BTG1 inactivation drives lymphomagenesis and promotes lymphoma
            dissemination through activation of BCAR1
  JOURNAL   Blood 141 (10), 1209-1220 (2023)
   PUBMED   36375119
  REMARK    GeneRIF: BTG1 inactivation drives lymphomagenesis and promotes
            lymphoma dissemination through activation of BCAR1.
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Li,H., Li,L., Qiu,X., Zhang,J. and Hua,Z.
  TITLE     The interaction of CFLAR with p130Cas promotes cell migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (2), 119390 (2023)
   PUBMED   36400248
  REMARK    GeneRIF: The interaction of CFLAR with p130Cas promotes cell
            migration.
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Camacho Leal Mdel,P., Sciortino,M., Tornillo,G., Colombo,S.,
            Defilippi,P. and Cabodi,S.
  TITLE     p130Cas/BCAR1 scaffold protein in tissue homeostasis and
            pathogenesis
  JOURNAL   Gene 562 (1), 1-7 (2015)
   PUBMED   25727852
  REMARK    GeneRIF: BCAR1 has a pivotal role in the regulation of tissue
            homeostasis in pathological conditions such as cancer. (Review)
            Review article
REFERENCE   5  (residues 1 to 870)
  AUTHORS   Nikonova,A.S., Gaponova,A.V., Kudinov,A.E. and Golemis,E.A.
  TITLE     CAS proteins in health and disease: an update
  JOURNAL   IUBMB Life 66 (6), 387-395 (2014)
   PUBMED   24962474
  REMARK    Review article
REFERENCE   6  (residues 1 to 870)
  AUTHORS   Barrett,A., Pellet-Many,C., Zachary,I.C., Evans,I.M. and Frankel,P.
  TITLE     p130Cas: a key signalling node in health and disease
  JOURNAL   Cell Signal 25 (4), 766-777 (2013)
   PUBMED   23277200
  REMARK    Review article
REFERENCE   7  (residues 1 to 870)
  AUTHORS   Brinkman,A., van der Flier,S., Kok,E.M. and Dorssers,L.C.
  TITLE     BCAR1, a human homologue of the adapter protein p130Cas, and
            antiestrogen resistance in breast cancer cells
  JOURNAL   J Natl Cancer Inst 92 (2), 112-120 (2000)
   PUBMED   10639512
REFERENCE   8  (residues 1 to 870)
  AUTHORS   Vuori,K., Hirai,H., Aizawa,S. and Ruoslahti,E.
  TITLE     Introduction of p130cas signaling complex formation upon
            integrin-mediated cell adhesion: a role for Src family kinases
  JOURNAL   Mol Cell Biol 16 (6), 2606-2613 (1996)
   PUBMED   8649368
REFERENCE   9  (residues 1 to 870)
  AUTHORS   Sakai,R., Iwamatsu,A., Hirano,N., Ogawa,S., Tanaka,T., Mano,H.,
            Yazaki,Y. and Hirai,H.
  TITLE     A novel signaling molecule, p130, forms stable complexes in vivo
            with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
  JOURNAL   EMBO J 13 (16), 3748-3756 (1994)
   PUBMED   8070403
REFERENCE   10 (residues 1 to 870)
  AUTHORS   Dorssers,L.C., van Agthoven,T., Dekker,A., van Agthoven,T.L. and
            Kok,E.M.
  TITLE     Induction of antiestrogen resistance in human breast cancer cells
            by random insertional mutagenesis using defective retroviruses:
            identification of bcar-1, a common integration site
  JOURNAL   Mol Endocrinol 7 (7), 870-878 (1993)
   PUBMED   8413311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027608.1, AK295809.1,
            AB040024.1, BU730553.1, AC009078.6 and BQ016861.1.
            
            Summary: The protein encoded by this gene is a member of the
            Crk-associated substrate (CAS) family of scaffold proteins,
            characterized by the presence of multiple protein-protein
            interaction domains and many serine and tyrosine phosphorylation
            sites. The encoded protein contains a Src-homology 3 (SH3) domain,
            a proline-rich domain, a substrate domain which contains 15 repeat
            of the YxxP consensus phosphorylation motif for Src family kinases,
            a serine-rich domain, and a bipartite Src-binding domain, which can
            bind both SH2 and SH3 domains. This adaptor protein functions in
            multiple cellular pathways, including in cell motility, apoptosis
            and cell cycle control. Dysregulation of this gene can have a wide
            range of effects, affecting different pathways, including cardiac
            development, vascular smooth muscle cells, liver and kidney
            function, endothelial migration, and cancer. [provided by RefSeq,
            Sep 2017].
            
            Transcript Variant: This variant (5) lacks an exon in the 5'
            region, resulting in an alternate AUG start codon, as compared to
            variant 1. The resulting isoform (5) is shorter and has a different
            N-terminus, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027608.1, SRR14038192.681559.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..870
                     /product="breast cancer anti-estrogen resistance protein 1
                     isoform 5"
                     /note="Cas scaffolding protein family member 1;
                     Crk-associated substrate p130Cas; breast cancer
                     anti-estrogen resistance protein 1; BCAR1, Cas family
                     scaffolding protein; BCAR1, Cas family scaffold protein"
                     /calculated_mol_wt=93160
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.7;
                     propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Region          5..71
                     /region_name="SH3_BCAR1"
                     /note="Src homology 3 domain of the CAS (Crk-Associated
                     Substrate) scaffolding protein family member, Breast
                     Cancer Anti-estrogen Resistance 1; cd12001"
                     /db_xref="CDD:212934"
     Site            order(12,14,17,21,42..43,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212934"
     Region          70..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Region          <91..483
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          115..416
                     /region_name="Substrate for kinases.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:22710723; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19454314,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61140; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000250|UniProtKB:Q63767; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61140; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61140; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61140; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Region          411..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19454314; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Region          454..610
                     /region_name="Serine_rich_CAS"
                     /note="Serine rich Four helix bundle domain of CAS
                     (Crk-Associated Substrate) scaffolding proteins; a protein
                     interaction module; cl07433"
                     /db_xref="CDD:471673"
     Region          609..658
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Region          635..643
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:19454314,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P56945.2)"
     Region          654..864
                     /region_name="CAS_C"
                     /note="Crk-Associated Substrate C-terminal domain;
                     pfam12026"
                     /db_xref="CDD:463437"
     Region          715..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     Region          746..796
                     /region_name="Divergent helix-loop-helix motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P56945.2)"
     CDS             1..870
                     /gene="BCAR1"
                     /gene_synonym="CAS; CAS1; CASS1; CRKAS; P130Cas"
                     /coded_by="NM_001170718.3:172..2784"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS54041.1"
                     /db_xref="GeneID:9564"
                     /db_xref="HGNC:HGNC:971"
                     /db_xref="MIM:602941"
ORIGIN      
        1 msvpnvlaka lydnvaespd elsfrkgdim tvleqdtqgl dgwwlcslhg rqgivpgnrl
       61 kilvgmydkk pagpgpgppa tpaqpqpglh apappasqyt pmlpntyqpq pdsvylvptp
      121 skaqqglyqv pgpspqfqsp pakqtstfsk qtphhpfpsp atdlyqvppg pggpaqdiyq
      181 vppsagmghd iyqvppsmdt rswegtkppa kvvvptrvgq gyvyeaaqpe qdeydiprhl
      241 lapgpqdiyd vppvrgllps qygqevydtp pmavkgpngr dpllevydvp psvekglpps
      301 nhhavydvpp svskdvpdgp llreetydvp pafakakpfd partplvlaa pppdsppaed
      361 vydvpppapd lydvppglrr pgpgtlydvp rervlppeva dggvvdsgvy avpppaerea
      421 paegkrlsas stgstrssqs asslevagpg replelevav ealarlqqgv satvahlldl
      481 agsagatgsw rspsepqepl vqdlqaavaa vqsavhelle farsavgnaa htsdralhak
      541 lsrqlqkmed vhqtlvahgq aldagrggsg atledldrlv acsravpeda kqlasflhgn
      601 asllfrrtka tapgpegggt lhpnptdkts siqsrplpsp pkftsqdspd gqyenseggw
      661 medydyvhlq gkeefektqk ellekgsitr qgksqlelqq lkqferleqe vsrpidhdla
      721 nwtpaqplap grtgglgpsd rqlllfyleq ceanlttltn avdafftava tnqppkifva
      781 hskfvilsah klvfigdtls rqakaadvrs qvthysnllc dllrgivatt kaaalqypsp
      841 saaqdmverv kelghstqqf rrvlgqlaaa
//
LOCUS       NP_060762                528 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial [Homo
            sapiens].
ACCESSION   NP_060762
VERSION     NP_060762.3
DBSOURCE    REFSEQ: accession NM_018292.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Kamps,R., Szklarczyk,R., Theunissen,T.E., Hellebrekers,D.M.E.I.,
            Sallevelt,S.C.E.H., Boesten,I.B., de Koning,B., van den Bosch,B.J.,
            Salomons,G.S., Simas-Mendes,M., Verdijk,R., Schoonderwoerd,K., de
            Coo,I.F.M., Vanoevelen,J.M. and Smeets,H.J.M.
  TITLE     Genetic defects in mtDNA-encoded protein translation cause
            pediatric, mitochondrial cardiomyopathy with early-onset brain
            disease
  JOURNAL   Eur J Hum Genet 26 (4), 537-551 (2018)
   PUBMED   29440775
  REMARK    GeneRIF: Homozygous intronic variant (c.850-3A > G) in the QRSL1
            was identified in a child with cardiomyopathy with early-onset
            brain disease.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Nagao,A., Suzuki,T., Katoh,T., Sakaguchi,Y. and Suzuki,T.
  TITLE     Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
  JOURNAL   Proc Natl Acad Sci U S A 106 (38), 16209-16214 (2009)
   PUBMED   19805282
  REMARK    GeneRIF: Studies showed in vitro Gln-tRNA(Gln) formation catalyzed
            by the recombinant mtGluRS and hGatCAB.
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA819470.1, BC014389.2 and AL390074.17.
            
            On Feb 6, 2009 this sequence version replaced NP_060762.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136679.1, SRR1803613.278831.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000369046.8/
                                                  ENSP00000358042.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..528
                     /product="glutamyl-tRNA(Gln) amidotransferase subunit A,
                     mitochondrial"
                     /EC_number="6.3.5.7"
                     /note="glutamyl-tRNA(Gln) amidotransferase subunit A
                     homolog; glutaminyl-tRNA synthase-like protein 1; glu-AdT
                     subunit A; glutamyl-tRNA(Gln) amidotransferase, subunit A;
                     QRSL1, glutaminyl-tRNA amidotransferase subunit A;
                     glutaminyl-tRNA synthase (glutamine-hydrolyzing)-like 1"
                     /calculated_mol_wt=57330
     Region          1..496
                     /region_name="GatA"
                     /note="Asp-tRNAAsn/Glu-tRNAGln amidotransferase A subunit
                     or related amidase [Translation, ribosomal structure and
                     biogenesis]; COG0154"
                     /db_xref="CDD:439924"
     Region          148..167
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0R6.2)"
     CDS             1..528
                     /gene="QRSL1"
                     /gene_synonym="COXPD40; GatA"
                     /coded_by="NM_018292.5:105..1691"
                     /db_xref="CCDS:CCDS5057.1"
                     /db_xref="GeneID:55278"
                     /db_xref="HGNC:HGNC:21020"
                     /db_xref="MIM:617209"
ORIGIN      
        1 mlgrslrevs aalkqgqitp telcqkclsl ikktkflnay itvseevalk qaeesekryk
       61 ngqslgdldg ipiavkdnfs tsgiettcas nmlkgyippy natvvqklld qgallmgktn
      121 ldefamgsgs tdgvfgpvkn pwsyskqyre krkqnphsen edsdwlitgg ssggsaaavs
      181 aftcyaalgs dtggstrnpa ahcglvgfkp syglvsrhgl iplvnsmdvp giltrcvdda
      241 aivlgalagp dprdsttvhe pinkpfmlps ladvsklcig ipkeylvpel ssevqslwsk
      301 aadlfesega kvievslpht sysivcyhvl ctsevasnma rfdglqyghr cdidvsteam
      361 yaatrregfn dvvrgrilsg nffllkenye nyfvkaqkvr rliandfvna fnsgvdvllt
      421 pttlseavpy lefikednrt rsaqddiftq avnmaglpav sipvalsnqg lpiglqfigr
      481 afcdqqlltv akwfekqvqf pviqlqelmd dcsavlenek lasvslkq
//
LOCUS       NP_001193768            1448 aa            linear   PRI 20-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase zeta isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001193768
VERSION     NP_001193768.1
DBSOURCE    REFSEQ: accession NM_001206839.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1448)
  AUTHORS   Wang,Y., Suo,J., Wang,Z., Ran,K., Tian,Y., Han,W., Liu,Y. and
            Peng,X.
  TITLE     The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells modulates
            tumor-associated macrophage polarization
  JOURNAL   Cell Signal 120, 111191 (2024)
   PUBMED   38685521
  REMARK    GeneRIF: The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells
            modulates tumor-associated macrophage polarization.
REFERENCE   2  (residues 1 to 1448)
  AUTHORS   Nagai,K., Muto,Y., Miura,S., Takahashi,K., Naruse,Y., Hiruta,R.,
            Hashimoto,Y., Uzuki,M., Haga,Y., Fujii,R., Ueda,K., Kawaguchi,Y.,
            Fujii,M. and Kitazume,S.
  TITLE     Brain-specific glycosylation enzyme GnT-IX maintains levels of
            protein tyrosine phosphatase receptor PTPRZ, thereby mediating
            glioma growth
  JOURNAL   J Biol Chem 299 (9), 105128 (2023)
   PUBMED   37543361
  REMARK    GeneRIF: Brain-specific glycosylation enzyme GnT-IX maintains
            levels of protein tyrosine phosphatase receptor PTPRZ, thereby
            mediating glioma growth.
REFERENCE   3  (residues 1 to 1448)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1448)
  AUTHORS   Lacore,M.G., Delmas,C., Nicaise,Y., Kowalski-Chauvel,A.,
            Cohen-Jonathan-Moyal,E. and Seva,C.
  TITLE     The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells
  JOURNAL   Cells 11 (14), 2128 (2022)
   PUBMED   35883571
  REMARK    GeneRIF: The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1448)
  AUTHORS   Nagai,K., Fujii,M. and Kitazume,S.
  TITLE     Protein Tyrosine Phosphatase Receptor Type Z in Central Nervous
            System Disease
  JOURNAL   Int J Mol Sci 23 (8), 4414 (2022)
   PUBMED   35457233
  REMARK    GeneRIF: Protein Tyrosine Phosphatase Receptor Type Z in Central
            Nervous System Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1448)
  AUTHORS   Ariyama,T., Hasegawa,K., Inazawa,J., Mizuno,K., Ogimoto,M.,
            Katagiri,T. and Yakura,H.
  TITLE     Assignment of the human protein tyrosine phosphatase,
            receptor-type, zeta (PTPRZ) gene to chromosome band 7q31.3
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 52-54 (1995)
   PUBMED   7736789
REFERENCE   7  (residues 1 to 1448)
  AUTHORS   Levy,J.B., Canoll,P.D., Silvennoinen,O., Barnea,G., Morse,B.,
            Honegger,A.M., Huang,J.T., Cannizzaro,L.A., Park,S.H., Druck,T. et
            al.
  TITLE     The cloning of a receptor-type protein tyrosine phosphatase
            expressed in the central nervous system
  JOURNAL   J Biol Chem 268 (14), 10573-10581 (1993)
   PUBMED   8387522
REFERENCE   8  (residues 1 to 1448)
  AUTHORS   Krueger,N.X. and Saito,H.
  TITLE     A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is
            expressed in brain and has an N-terminal receptor domain homologous
            to carbonic anhydrases
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7417-7421 (1992)
   PUBMED   1323835
REFERENCE   9  (residues 1 to 1448)
  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.
  TITLE     Structural diversity and evolution of human receptor-like protein
            tyrosine phosphatases
  JOURNAL   EMBO J 9 (10), 3241-3252 (1990)
   PUBMED   2170109
REFERENCE   10 (residues 1 to 1448)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA454064.1, U88967.1, M93426.1
            and BC131736.1.
            
            Summary: This gene encodes a member of the receptor protein
            tyrosine phosphatase family. Expression of this gene is restricted
            to the central nervous system (CNS), and it may be involved in the
            regulation of specific developmental processes in the CNS.
            Alternatively spliced transcript variants encoding different
            isoforms have been described for this gene. [provided by RefSeq,
            May 2011].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            donor splice site at an internal coding exon, and is lacking
            another in-frame coding exon compared to variant 1. This results in
            a shorter isoform (2) missing two internal protein segments
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.103536.1,
                                           SRR1803617.131152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.32"
     Protein         1..1448
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 3 precursor"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor-type, zeta
                     polypeptide 1; protein tyrosine phosphatase,
                     receptor-type, Z polypeptide 1; receptor-type tyrosine
                     phosphatase beta/zeta; protein-tyrosine phosphatase
                     receptor type Z polypeptide 2"
                     /calculated_mol_wt=159845
     sig_peptide     1..24
                     /calculated_mol_wt=2837
     mat_peptide     25..1448
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 3"
                     /calculated_mol_wt=159845
     Region          45..298
                     /region_name="alpha_CARP_receptor_like"
                     /note="Carbonic anhydrase alpha related protein,
                     receptor_like subfamily. Carbonic anhydrase related
                     proteins (CARPs) are sequence similar to carbonic
                     anhydrases. Carbonic anhydrases are zinc-containing
                     enzymes that catalyze the reversible hydration of
                     carbon...; cd03122"
                     /db_xref="CDD:239396"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            232
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          313..401
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            order(397..398,400..401)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          442..462
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Region          477..507
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            501
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            552
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            587
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            602
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          628..650
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23471.4)"
     Site            629
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            637
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine,
                     alternate. /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q62656; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62656; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Site            677
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23471.4)"
     Region          857..1127
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          1210..1413
                     /region_name="R-PTP-Z-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase Z, repeat 2; cd17669"
                     /db_xref="CDD:350507"
     CDS             1..1448
                     /gene="PTPRZ1"
                     /gene_synonym="HPTPZ; HPTPzeta; phosphacan; PTP-ZETA;
                     PTP18; PTPRZ; PTPZ; R-PTP-zeta-2; RPTPB; RPTPbeta"
                     /coded_by="NM_001206839.2:340..4686"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS56505.1"
                     /db_xref="GeneID:5803"
                     /db_xref="HGNC:HGNC:9685"
                     /db_xref="MIM:176891"
ORIGIN      
        1 mrilkrflac iqllcvcrld wangyyrqqr klveeigwsy tgalnqknwg kkyptcnspk
       61 qspinidedl tqvnvnlkkl kfqgwdktsl entfihntgk tveinltndy rvsggvsemv
      121 fkaskitfhw gkcnmssdgs ehslegqkfp lemqiycfda drfssfeeav kgkgklrals
      181 ilfevgteen ldfkaiidgv esvsrfgkqa aldpfillnl lpnstdkyyi yngsltsppc
      241 tdtvdwivfk dtvsisesql avfcevltmq qsgyvmlmdy lqnnfreqqy kfsrqvfssy
      301 tgkeeiheav cssepenvqa dpenytsllv twerprvvyd tmiekfavly qqldgedqtk
      361 hefltdgyqd lgailnnllp nmsyvlqiva ictnglygky sdqlivdmpt dnpeldlfpe
      421 ligteeiike eeegkdieeg aivnpgrdsa tnqirkkepq isttthynri gtkyneaktn
      481 rsptrgsefs gkgdvpntsl nstsqpvtkl atekdislts qtvtelppht vegtsaslnd
      541 gsktvlrsph mnlsgtaesl ntvsiteyee eslltsfkld tgaedssgss patsaipfis
      601 enisqgyifs senpetityd vlipesarna sedstssgse eslkdpsmeg nvwfpsstdi
      661 taqpdvgsgr esflqtnyte irvdesektt ksfsagpvms qgpsvtdlem phystfayfp
      721 tevtphaftp ssrqqdlvst vnvvysqttq pvyneasnss hesriglaeg lesekkavip
      781 lvivsaltfi clvvlvgili ywrkcfqtah fyledstspr vistpptpif pisddvgaip
      841 ikhfpkhvad lhassgftee feevqsctvd lgitadssnh pdnkhknryi nivaydhsrv
      901 klaqlaekdg kltdyinany vdgynrpkay iaaqgplkst aedfwrmiwe hnvevivmit
      961 nlvekgrrkc dqywpadgse eygnflvtqk svqvlayytv rnftlrntki kkgsqkgrps
     1021 grvvtqyhyt qwpdmgvpey slpvltfvrk aayakrhavg pvvvhcsagv grtgtyivld
     1081 smlqqiqheg tvnifgflkh irsqrnylvq teeqyvfihd tlveailske tevldshiha
     1141 yvnallipgp agktklekqf qllsqsniqq sdysaalkqc nreknrtssi ipversrvgi
     1201 sslsgegtdy inasyimgyy qsnefiitqh pllhtikdfw rmiwdhnaql vvmipdgqnm
     1261 aedefvywpn kdepincesf kvtlmaeehk clsneeklii qdfileatqd dyvlevrhfq
     1321 cpkwpnpdsp isktfelisv ikeeaanrdg pmivhdehgg vtagtfcalt tlmhqleken
     1381 svdvyqvakm inlmrpgvfa dieqyqflyk vilslvstrq eenpstslds ngaalpdgni
     1441 aesleslv
//
LOCUS       NP_006351                374 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit M isoform 1
            [Homo sapiens].
ACCESSION   NP_006351
VERSION     NP_006351.2
DBSOURCE    REFSEQ: accession NM_006360.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Hinnebusch,A.G.
  TITLE     eIF3: a versatile scaffold for translation initiation complexes
  JOURNAL   Trends Biochem Sci 31 (10), 553-562 (2006)
   PUBMED   16920360
  REMARK    Review article
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Perez-Romero,P. and Fuller,A.O.
  TITLE     The C terminus of the B5 receptor for herpes simplex virus contains
            a functional region important for infection
  JOURNAL   J Virol 79 (12), 7431-7437 (2005)
   PUBMED   15919899
  REMARK    GeneRIF: Concluded that the C terminus of B5 contains a functional
            region that is important for the B5 receptor to mediate events in
            HSV entry.
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Perez,A., Li,Q.X., Perez-Romero,P., Delassus,G., Lopez,S.R.,
            Sutter,S., McLaren,N. and Fuller,A.O.
  TITLE     A new class of receptor for herpes simplex virus has heptad repeat
            motifs that are common to membrane fusion proteins
  JOURNAL   J Virol 79 (12), 7419-7430 (2005)
   PUBMED   15919898
  REMARK    GeneRIF: Cloned a previously uncharacterized human gene, designated
            hfl-B5, and showed that it encodes a type II cell surface membrane
            protein that can serve as a receptor for entry of HSV.
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB479224.1, BC019103.2, AK304378.1, BE935691.1, CK002866.1 and
            AL078477.5.
            
            On Oct 1, 2002 this sequence version replaced NP_006351.1.
            
            Summary: This gene encodes a protein that is part of the
            eurkaryotic translation initiation factor 3 complete (eIF-3)
            required for protein synthesis. Elevated levels of the encoded
            protein are present in cancer cell lines. Inactivation of the
            encoded protein has been shown to interfere with translation of
            herpes virus mRNAs by preventing the association of mRNAs with the
            ribosomes. A pseudogene of this gene is located on the X
            chromosome. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.234014.1,
                                           SRR1803611.13609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000531120.6/ ENSP00000436049.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..374
                     /product="eukaryotic translation initiation factor 3
                     subunit M isoform 1"
                     /EC_number="3.6.5.3"
                     /note="dendritic cell protein; PCI domain containing 1
                     (herpesvirus entry mediator); fetal lung protein B5; B5
                     receptor; PCI domain-containing protein 1; transport and
                     golgi organization 7 homolog"
                     /calculated_mol_wt=42372
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03012,
                     ECO:0000269|PubMed:17322308, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            254
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Region          269..357
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          344..374
                     /region_name="Interaction with HSV-1 and HSV-2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L2H7.1)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L2H7.1)"
     CDS             1..374
                     /gene="EIF3M"
                     /gene_synonym="B5; GA17; hfl-B5; PCID1; TANGO7"
                     /coded_by="NM_006360.6:58..1182"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7880.1"
                     /db_xref="GeneID:10480"
                     /db_xref="HGNC:HGNC:24460"
                     /db_xref="MIM:609641"
ORIGIN      
        1 msvpafidis eedqaaelra ylkskgaeis eensegglhv dlaqiieacd vclkeddkdv
       61 esvmnsvvsl llilepdkqe alieslcekl vkfregerps lrlqllsnlf hgmdkntpvr
      121 ytvycslikv aascgaiqyi pteldqvrkw isdwnlttek khtllrllye alvdckksda
      181 askvmvellg sytednasqa rvdahrcivr alkdpnaflf dhlltlkpvk flegelihdl
      241 ltifvsakla syvkfyqnnk dfidslgllh eqnmakmrll tfmgmavenk eisfdtmqqe
      301 lqigaddvea fvidavrtkm vyckidqtqr kvvvshsthr tfgkqqwqql ydtlnawkqn
      361 lnkvknslls lsdt
//
LOCUS       NP_898888                140 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 107 isoform 2 [Homo sapiens].
ACCESSION   NP_898888
VERSION     NP_898888.1
DBSOURCE    REFSEQ: accession NM_183065.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Dubaic,M., Peskova,L., Hampl,M., Weissova,K., Celiker,C.,
            Shylo,N.A., Hruba,E., Kavkova,M., Zikmund,T., Weatherbee,S.D.,
            Kaiser,J., Barta,T. and Buchtova,M.
  TITLE     Role of ciliopathy protein TMEM107 in eye development: insights
            from a mouse model and retinal organoid
  JOURNAL   Life Sci Alliance 6 (12), e202302073 (2023)
   PUBMED   37863656
  REMARK    GeneRIF: Role of ciliopathy protein TMEM107 in eye development:
            insights from a mouse model and retinal organoid.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Bruel,A.L., Franco,B., Duffourd,Y., Thevenon,J., Jego,L., Lopez,E.,
            Deleuze,J.F., Doummar,D., Giles,R.H., Johnson,C.A., Huynen,M.A.,
            Chevrier,V., Burglen,L., Morleo,M., Desguerres,I., Pierquin,G.,
            Doray,B., Gilbert-Dussardier,B., Reversade,B.,
            Steichen-Gersdorf,E., Baumann,C., Panigrahi,I.,
            Fargeot-Espaliat,A., Dieux,A., David,A., Goldenberg,A., Bongers,E.,
            Gaillard,D., Argente,J., Aral,B., Gigot,N., St-Onge,J.,
            Birnbaum,D., Phadke,S.R., Cormier-Daire,V., Eguether,T.,
            Pazour,G.J., Herranz-Perez,V., Goldstein,J.S., Pasquier,L.,
            Loget,P., Saunier,S., Megarbane,A., Rosnet,O., Leroux,M.R.,
            Wallingford,J.B., Blacque,O.E., Nachury,M.V., Attie-Bitach,T.,
            Riviere,J.B., Faivre,L. and Thauvin-Robinet,C.
  TITLE     Fifteen years of research on oral-facial-digital syndromes: from 1
            to 16 causal genes
  JOURNAL   J Med Genet 54 (6), 371-380 (2017)
   PUBMED   28289185
  REMARK    Review article
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Shylo,N.A., Christopher,K.J., Iglesias,A., Daluiski,A. and
            Weatherbee,S.D.
  TITLE     TMEM107 Is a Critical Regulator of Ciliary Protein Composition and
            Is Mutated in Orofaciodigital Syndrome
  JOURNAL   Hum Mutat 37 (2), 155-159 (2016)
   PUBMED   26518474
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Lambacher,N.J., Bruel,A.L., van Dam,T.J., Szymanska,K.,
            Slaats,G.G., Kuhns,S., McManus,G.J., Kennedy,J.E., Gaff,K.,
            Wu,K.M., van der Lee,R., Burglen,L., Doummar,D., Riviere,J.B.,
            Faivre,L., Attie-Bitach,T., Saunier,S., Curd,A., Peckham,M.,
            Giles,R.H., Johnson,C.A., Huynen,M.A., Thauvin-Robinet,C. and
            Blacque,O.E.
  TITLE     TMEM107 recruits ciliopathy proteins to subdomains of the ciliary
            transition zone and causes Joubert syndrome
  JOURNAL   Nat Cell Biol 18 (1), 122-131 (2016)
   PUBMED   26595381
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Christopher,K.J., Wang,B., Kong,Y. and Weatherbee,S.D.
  TITLE     Forward genetics uncovers Transmembrane protein 107 as a novel
            factor required for ciliogenesis and Sonic hedgehog signaling
  JOURNAL   Dev Biol 368 (2), 382-392 (2012)
   PUBMED   22698544
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Geisert,E.E., Lu,L., Freeman-Anderson,N.E., Templeton,J.P.,
            Nassr,M., Wang,X., Gu,W., Jiao,Y. and Williams,R.W.
  TITLE     Gene expression in the mouse eye: an online resource for genetics
            using 103 strains of mice
  JOURNAL   Mol Vis 15, 1730-1763 (2009)
   PUBMED   19727342
  REMARK    GeneRIF: TMEM107 (2810049P21Rik) is a strong candidate gene for
            central areolar choroidal dystrophy, CACD (human 17p13). Conclusion
            is based on a massive expression data set for mouse (103 strains in
            GeneNetwork.org) and joint analysis of RetNet database.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF311338.1, BC127649.1 and
            AC129492.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a transmembrane protein and component of
            the primary cilia transition zone. The encoded protein regulates
            ciliogenesis and ciliary protein composition. Human fibroblasts
            expressing a mutant allele of this gene exhibit reduced numbers of
            cilia, altered cilia length, and impaired sonic hedgehog signaling.
            In human patients, different mutations in this gene cause different
            ciliopathies, including Meckel-Gruber syndrome and orofaciodigital
            syndrome. [provided by RefSeq, May 2017].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.163327.1,
                                           SRR1803611.201010.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000437139.7/ ENSP00000402732.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..140
                     /product="transmembrane protein 107 isoform 2"
                     /calculated_mol_wt=15372
     Region          7..129
                     /region_name="TMEM107"
                     /note="Transmembrane protein; pfam14995"
                     /db_xref="CDD:464430"
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX40.1)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX40.1)"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UX40.1)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX40.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX40.1)"
     CDS             1..140
                     /gene="TMEM107"
                     /gene_synonym="GRVS638; JBTS29; MKS13; PRO1268"
                     /coded_by="NM_183065.4:95..517"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45607.1"
                     /db_xref="GeneID:84314"
                     /db_xref="HGNC:HGNC:28128"
                     /db_xref="MIM:616183"
ORIGIN      
        1 mgrvsglvps rfltllahlv vvitlfwsrd sniqaclplt ftpeeydkqd iqlvaalsvt
       61 lglfavelag flsgvsmfns tqslisigah csasvalsff iferwectty wyifvfcsal
      121 pavtemalfv tvfglkkkpf
//
LOCUS       NP_001354622             819 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ddd [Homo sapiens].
ACCESSION   NP_001354622
VERSION     NP_001354622.1
DBSOURCE    REFSEQ: accession NM_001367693.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2151741,
                              SAMEA2154361 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..819
                     /product="SUN domain-containing protein 1 isoform ddd"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=90561
     Region          62..356
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          482..535
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(482,485..486,489,492..493,496..497,499..500,
                     503..504,506..507,510..511,513..514,517,520..521,524,
                     527..528,531..532,534..535)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          494..>627
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          612..670
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          713..817
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..819
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367693.1:52..2511"
                     /note="isoform ddd is encoded by transcript variant 56"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv revlredghl
      241 svngealcdd ckgkrhldah taahsqsprl pgragtlwhi wacagyfllq ilrrigavgq
      301 avsrtawsal wlavvapgka asgvfwwlgi gwyqfvtlis wlnvflltrc lrnickflvl
      361 liplflllag lslrgqgnff sflpvlnwas mhrtqrvddp qdvfkpttsr lkqplqgdse
      421 afpwhwmsgv eqqvaslsgq chhhgenlre lttllqklqa rvdqmeggaa gpsasvrdav
      481 gqppretdfm afhqehevrm shledilgkl rekseaiqke leqtkqktis avgeqllptv
      541 ehlqleldql kselsswrhv ktgcetvdav qervdvqvre mvkllfsedq qggsleqllq
      601 rfssqfvskg dlqtmlrdlq lqilrnvthh vsvtkqlpts eavvsavsea gasgiteaqa
      661 raivnsalkl ysqdktgmvd falesgggsi lstrcsetye tktalmslfg iplwyfsqsp
      721 rvviqpdiyp gncwafkgsq gylvvrlsmm ihpaaftleh ipktlsptgn issapkdfav
      781 ykrpddtafq ivelrifsnw ghpeytclyr frvhgepvk
//
LOCUS       NP_003155                355 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-5 isoform 1 [Homo sapiens].
ACCESSION   NP_003155 XP_943433
VERSION     NP_003155.2
DBSOURCE    REFSEQ: accession NM_003164.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Hom Choudhury,S., Bhattacharjee,S., Mukherjee,K. and
            Bhattacharyya,S.N.
  TITLE     Human antigen R transfers miRNA to Syntaxin 5 to synergize miRNA
            export from activated macrophages
  JOURNAL   J Biol Chem 300 (4), 107170 (2024)
   PUBMED   38492777
  REMARK    GeneRIF: Human antigen R transfers miRNA to Syntaxin 5 to synergize
            miRNA export from activated macrophages.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Kat,M., Karampini,E., Hoogendijk,A.J., Burgisser,P.E., Mulder,A.A.,
            Van Alphen,F.P.J., Olins,J., Geerts,D., Van den Biggelaar,M.,
            Margadant,C., Voorberg,J. and Bierings,R.
  TITLE     Syntaxin 5 determines Weibel-Palade body size and von Willebrand
            factor secretion by controlling Golgi architecture
  JOURNAL   Haematologica 107 (8), 1827-1839 (2022)
   PUBMED   35081689
  REMARK    GeneRIF: Syntaxin 5 determines Weibel-Palade body size and von
            Willebrand factor secretion by controlling Golgi architecture.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Nabeta,M., Abe,Y., Takaoka,Y., Kusanagi,Y. and Ito,M.
  TITLE     Identification of anti-syntaxin 5 autoantibody as a novel serum
            marker of endometriosis
  JOURNAL   J Reprod Immunol 91 (1-2), 48-55 (2011)
   PUBMED   21715015
  REMARK    GeneRIF: serum anti-STX5 autoantibody, which was discovered by a
            proteomic approach, is a potential new serum marker for the
            diagnosis of endometriosis.
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Hay,J.C., Klumperman,J., Oorschot,V., Steegmaier,M., Kuo,C.S. and
            Scheller,R.H.
  TITLE     Localization, dynamics, and protein interactions reveal distinct
            roles for ER and Golgi SNAREs
  JOURNAL   J Cell Biol 141 (7), 1489-1502 (1998)
   PUBMED   9647643
  REMARK    Erratum:[J Cell Biol 1998 Aug 10;142(3):following 881]
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Rabouille,C., Kondo,H., Newman,R., Hui,N., Freemont,P. and
            Warren,G.
  TITLE     Syntaxin 5 is a common component of the NSF- and p97-mediated
            reassembly pathways of Golgi cisternae from mitotic Golgi fragments
            in vitro
  JOURNAL   Cell 92 (5), 603-610 (1998)
   PUBMED   9506515
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Tang,B.L., Low,D.Y., Lee,S.S., Tan,A.E. and Hong,W.
  TITLE     Molecular cloning and localization of human syntaxin 16, a member
            of the syntaxin family of SNARE proteins
  JOURNAL   Biochem Biophys Res Commun 242 (3), 673-679 (1998)
   PUBMED   9464276
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Hay,J.C., Chao,D.S., Kuo,C.S. and Scheller,R.H.
  TITLE     Protein interactions regulating vesicle transport between the
            endoplasmic reticulum and Golgi apparatus in mammalian cells
  JOURNAL   Cell 89 (1), 149-158 (1997)
   PUBMED   9094723
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Ravichandran,V. and Roche,P.A.
  TITLE     Cloning and identification of human syntaxin 5 as a
            synaptobrevin/VAMP binding protein
  JOURNAL   J Mol Neurosci 8 (2), 159-161 (1997)
   PUBMED   9188044
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB155395.1, U26648.1 and
            BE409085.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 28, 2006 this sequence version replaced NP_003155.1.
            
            Summary: This gene encodes a member of the syntaxin or t-SNARE
            (target-SNAP receptor) family. These proteins are found on cell
            membranes and serve as the targets for v-SNAREs (vesicle-SNAP
            receptors), permitting specific synaptic vesicle docking and
            fusion. The encoded protein regulates endoplasmic reticulum to
            Golgi transport and plays a critical role in autophagy.
            Autoantibodies targeting the encoded protein may be a diagnostic
            marker for endometriosis. Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene.
            [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.472156.1,
                                           SRR3476690.304092.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294179.8/ ENSP00000294179.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..355
                     /product="syntaxin-5 isoform 1"
                     /note="syntaxin 5A"
                     /calculated_mol_wt=39542
     Region          28..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13190.2)"
     Region          53..74
                     /region_name="Syntaxin-5_N"
                     /note="Syntaxin-5 N-terminal, Sly1p-binding domain;
                     pfam11416"
                     /db_xref="CDD:463276"
     Region          <182..324
                     /region_name="COG5325"
                     /note="t-SNARE complex subunit, syntaxin [Intracellular
                     trafficking and secretion]"
                     /db_xref="CDD:227635"
     Region          245..247
                     /region_name="IxM motif, signal for cargo packaging into
                     COPII-coated vesicles.
                     /evidence=ECO:0000269|PubMed:18843296"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13190.2)"
     Region          266..338
                     /region_name="SNARE_syntaxin5"
                     /note="SNARE motif of syntaxin 5; cd15844"
                     /db_xref="CDD:277197"
     Site            order(267,269..270,272..277,279..281,283..284,286..288,
                     290..291,293..295,297..298,300..305,307..312,314..319,
                     321..323)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277197"
     Site            297
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277197"
     Site            334..354
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13190.2)"
     CDS             1..355
                     /gene="STX5"
                     /gene_synonym="CDG2AA; SED5; STX5A"
                     /coded_by="NM_003164.5:118..1185"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8038.2"
                     /db_xref="GeneID:6811"
                     /db_xref="HGNC:HGNC:11440"
                     /db_xref="MIM:603189"
ORIGIN      
        1 miprkrygsk ntdqgvylgl sktqvlspat agssssdiap lpppvtlvpp ppdtmscrdr
       61 tqeflsacks lqtrqngiqt nkpalravrq rseftlmakr igkdlsntfa klekltilak
      121 rkslfddkav eieeltyiik qdinslnkqi aqlqdfvrak gsqsgrhlqt hsntivvslq
      181 sklasmsndf ksvlevrten lkqqrsrreq fsrapvsalp lapnhlggga vvlgaeshas
      241 kdvaidmmds rtsqqlqlid eqdsyiqsra dtmqniesti velgsifqql ahmvkeqeet
      301 iqridenvlg aqldveaahs eilkyfqsvt snrwlmvkif lilivffiif vvfla
//
LOCUS       NP_002820                913 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002820
VERSION     NP_002820.3
DBSOURCE    REFSEQ: accession NM_002829.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Masuda,S., Onishi,H., Iwamoto,N., Imaizumi,A., Koga,S., Nagao,S.,
            Sakanashi,K., Itoyama,S., Fujimura,A., Komune,N., Kogo,R.,
            Umebayashi,M., Morisaki,T. and Nakagawa,T.
  TITLE     Inhibition of PTPN3 Expressed in Activated Lymphocytes Enhances the
            Antitumor Effects of Anti-PD-1 Therapy in Head and Neck Cancer,
            Especially in Hypoxic Environments
  JOURNAL   J Immunother 47 (3), 89-97 (2024)
   PUBMED   38297883
  REMARK    GeneRIF: Inhibition of PTPN3 Expressed in Activated Lymphocytes
            Enhances the Antitumor Effects of Anti-PD-1 Therapy in Head and
            Neck Cancer, Especially in Hypoxic Environments.
REFERENCE   4  (residues 1 to 913)
  AUTHORS   Zhou,Z., Lin,Z., Wang,M., Wang,L., Ji,Y., Yang,J., Yang,Y., Zhu,G.
            and Liu,T.
  TITLE     Identification and verification of PTPN3 as a novel biomarker in
            predicting cancer prognosis, immunity, and immunotherapeutic
            efficacy
  JOURNAL   Eur J Med Res 29 (1), 12 (2024)
   PUBMED   38173048
  REMARK    GeneRIF: Identification and verification of PTPN3 as a novel
            biomarker in predicting cancer prognosis, immunity, and
            immunotherapeutic efficacy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and
            Tonks,N.K.
  TITLE     Serine phosphorylation-dependent association of the band
            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta
            protein
  JOURNAL   J Biol Chem 272 (43), 27281-27287 (1997)
   PUBMED   9341175
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and
            Yachi,A.
  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase
            PTPH1 mRNA in human hepatocellular carcinoma
  JOURNAL   J Gastroenterol 29 (6), 727-732 (1994)
   PUBMED   7874267
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,
            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.
  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a
            cytosolic protein tyrosine phosphatase homologous to
            cytoskeletal-associated proteins
  JOURNAL   Int J Cancer 55 (6), 947-951 (1993)
   PUBMED   8253532
REFERENCE   9  (residues 1 to 913)
  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,
            Adachi,M., Imai,K. and Yachi,A.
  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human
            colon
  JOURNAL   Tumour Biol 13 (3), 180-186 (1992)
   PUBMED   1626183
REFERENCE   10 (residues 1 to 913)
  AUTHORS   Yang,Q. and Tonks,N.K.
  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine
            phosphatase with homology to the cytoskeletal-associated proteins
            band 4.1, ezrin, and talin
  JOURNAL   Proc Natl Acad Sci U S A 88 (14), 5949-5953 (1991)
   PUBMED   1648725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316066.1, BC126117.1,
            BC033716.1, DB173093.1, AK096975.1 and AL359963.29.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 21, 2009 this sequence version replaced NP_002820.2.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This protein contains a C-terminal PTP
            domain and an N-terminal domain homologous to the band 4.1
            superfamily of cytoskeletal-associated proteins. P97, a cell cycle
            regulator involved in a variety of membrane related functions, has
            been shown to be a substrate of this PTP. This PTP was also found
            to interact with, and be regulated by adaptor protein 14-3-3 beta.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.75211.1,
                                           SRR7346977.2885267.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374541.4/ ENSP00000363667.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..913
                     /product="tyrosine-protein phosphatase non-receptor type 3
                     isoform 1"
                     /EC_number="3.1.3.48"
                     /note="cytoskeletal-associated protein tyrosine
                     phosphatase; protein-tyrosine phosphatase H1"
                     /calculated_mol_wt=103859
     Region          31..222
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          216..309
                     /region_name="FERM_C_PTPN4_PTPN3_like"
                     /note="FERM domain C-lobe of Protein tyrosine phosphatase
                     non-receptor proteins 3 and 4 (PTPN4 and PTPN3); cd13189"
                     /db_xref="CDD:270010"
     Site            order(226,243,245,251)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270010"
     Site            order(255,260..263,298,302,305..306)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Site            298..309
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270010"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Region          363..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26045.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Region          420..475
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P26045.2)"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P26045.2)"
     Region          506..595
                     /region_name="PDZ_PTPN3-4-like"
                     /note="PDZ domain of tyrosine-protein phosphatase
                     non-receptor type 3 (PTPN3), tyrosine-protein phosphatase
                     non-receptor type 4 (PTNP4), and related domains; cd06706"
                     /db_xref="CDD:467190"
     Site            order(520..526,538,541,572,576,579..580)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467190"
     Region          631..904
                     /region_name="PTPc-N3"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 3; cd14600"
                     /db_xref="CDD:350448"
     CDS             1..913
                     /gene="PTPN3"
                     /gene_synonym="PTP-H1; PTPH1"
                     /coded_by="NM_002829.4:107..2848"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6776.1"
                     /db_xref="GeneID:5774"
                     /db_xref="HGNC:HGNC:9655"
                     /db_xref="MIM:176877"
ORIGIN      
        1 mtsrlralgg rinnirtsel pkektrsevi csihfldgvv qtfkvtkqdt gqvlldmvhn
       61 hlgvtekeyf glqhdddsvd sprwleaska irkqlkggfp ctlhfrvrff ipdpntlqqe
      121 qtrhlyflql kmdicegrlt cplnsavvla syavqshfgd ynssihhpgy lsdshfipdq
      181 nedfltkves lheqhsglkq seaescyini artldfygve lhsgrdlhnl dlmigiasag
      241 vavyrkyict sfypwvnilk isfkrkkffi hqrqkqaesr ehivafnmln yrscknlwks
      301 cvehhtffqa kkllpqeknv lsqywtmgsr ntkksvnnqy ckkviggmvw npamrrslsv
      361 ehletkslps rsppitpnwr sprlrheirk prhssadnla nemtyitete dvfytykgsl
      421 apqdsdsevs qnrsphqesl sennpaqsyl tqkssssvsp ssnapgscsp dgvdqqlldd
      481 fhrvtkggst edasqyycdk ndngdsylvl iritpdedgk fgfnlkggvd qkmplvvsri
      541 npespadtci pklnegdqiv lingrdiseh thdqvvmfik asreshsrel alvirrravr
      601 sfadfksede lnqlfpeaif pmcpeggdtl egsmaqlkkg lesgtvliqf eqlyrkkpgl
      661 aitfaklpqn ldknrykdvl pydttrvllq gnedyinasy vnmeipaanl vnkyiatqgp
      721 lphtcaqfwq vvwdqklsli vmlttlterg rtkchqywpd ppdvmnhggf hiqcqsedct
      781 iayvsremlv tntqtgeeht vthlqyvawp dhgvpddssd flefvnyvrs lrvdsepvlv
      841 hcsagigrtg vlvtmetamc lternlpiyp ldivrkmrdq rammvqtssq ykfvceailr
      901 vyeeglvqml dps
//
LOCUS       NP_001333370            1230 aa            linear   PRI 20-NOV-2025
DEFINITION  protein cordon-bleu isoform d [Homo sapiens].
ACCESSION   NP_001333370 XP_016867388
VERSION     NP_001333370.1
DBSOURCE    REFSEQ: accession NM_001346441.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1230)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1230)
  AUTHORS   Abdul Majeed,S., Dunzendorfer,H., Weiner,J., Heiker,J.T., Kiess,W.,
            Korner,A. and Landgraf,K.
  TITLE     COBL, MKX and MYOC Are Potential Regulators of Brown Adipose Tissue
            Development Associated with Obesity-Related Metabolic Dysfunction
            in Children
  JOURNAL   Int J Mol Sci 24 (4), 3085 (2023)
   PUBMED   36834493
  REMARK    GeneRIF: COBL, MKX and MYOC Are Potential Regulators of Brown
            Adipose Tissue Development Associated with Obesity-Related
            Metabolic Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1230)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1230)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1230)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 1230)
  AUTHORS   Husson,C., Renault,L., Didry,D., Pantaloni,D. and Carlier,M.F.
  TITLE     Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
            filament assembly
  JOURNAL   Mol Cell 43 (3), 464-477 (2011)
   PUBMED   21816349
  REMARK    GeneRIF: Cordon-Bleu works as a dynamizer of actin assembly by
            combining many properties of profilin with weak filament nucleating
            and powerful filament severing activities and sequestration of
            ADP-actin, which generate oscillatory polymerization kinetics.
REFERENCE   7  (residues 1 to 1230)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1230)
  AUTHORS   de Krom,M., Staal,W.G., Ophoff,R.A., Hendriks,J., Buitelaar,J.,
            Franke,B., de Jonge,M.V., Bolton,P., Collier,D., Curran,S., van
            Engeland,H. and van Ree,J.M.
  TITLE     A common variant in DRD3 receptor is associated with autism
            spectrum disorder
  JOURNAL   Biol Psychiatry 65 (7), 625-630 (2009)
   PUBMED   19058789
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1230)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
REFERENCE   10 (residues 1 to 1230)
  AUTHORS   Gasca,S., Hill,D.P., Klingensmith,J. and Rossant,J.
  TITLE     Characterization of a gene trap insertion into a novel gene,
            cordon-bleu, expressed in axial structures of the gastrulating
            mouse embryo
  JOURNAL   Dev Genet 17 (2), 141-154 (1995)
   PUBMED   7586755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005535.2, AC012372.4,
            AC004414.1 and BC045771.1.
            
            On Oct 13, 2016 this sequence version replaced XP_016867388.1.
            
            Summary: This gene encodes a protein that contains WH2 domains
            (WASP, Wiskott-Aldrich syndrome protein, homology domain-2) that
            interact with actin. The encoded actin regulator protein is
            required for growth and assembly of brush border microvilli that
            play a role in maintaining intestinal homeostasis. A similar
            protein in mouse functions in midbrain neural tube closure. A
            pseudogene of this gene is located on chromosome X. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. The encoded
            isoform (d) is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.30356.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.1"
     Protein         1..1230
                     /product="protein cordon-bleu isoform d"
                     /note="protein cordon-bleu"
                     /calculated_mol_wt=132321
     Region          152..230
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          1156..1188
                     /region_name="WH2_Wa_Cobl"
                     /note="first Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wa) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21799"
                     /db_xref="CDD:409197"
     Site            order(1167,1169..1171,1173..1175,1177,1181,1183..1187)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409197"
     Region          1183..1186
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409197"
     Region          1202..>1229
                     /region_name="WH2_Wb_Cobl"
                     /note="second Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wb) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21800"
                     /db_xref="CDD:409198"
     Region          1223..1226
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409198"
     CDS             1..1230
                     /gene="COBL"
                     /coded_by="NM_001346441.2:177..3869"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:23242"
                     /db_xref="HGNC:HGNC:22199"
                     /db_xref="MIM:610317"
ORIGIN      
        1 mdaprasaak pptgrkmkar appppgkaat lhvhsdqkpp hdgalgsqqn lvrmkealra
       61 stmdvtvvlp sglekrsvln gshammdllv elclqnhlnp shhaleirss etqqplsfkp
      121 ntligtlnvh tvflkekvpe ekvkpgppkv peksvrlvvn ylrtqkavvr vspevplqni
      181 lpvicakcev spehvvllrd niageelels kslnelgike lyawdnrret frksslgnde
      241 tdkekkkflg ffkvnkrsns kgclttpnsp smhsrsltlg pslslgsisg vsvksemkkr
      301 rappppgsgp pvqdkasekv slgsqidlqk kkrrapappp pqppppspli pnrtedkeen
      361 rkstmgggrq vpqkpprgta rgppqlvlpp pppypppdtd vveplsfpge gagseasdpi
      421 pklslplgsg shcspdgapq vlseaeetvs vgscfasedt tedsgvmssp sdivsldsqq
      481 dsmkykdkwa tdqedcsdqd lagtpdlgpq ksplwekngs enshlrteka vtasndeedl
      541 liagefrktl aeldedleem edsyetdtss ltssihgasn hcpqdamiph gdtdaipvtf
      601 igevsddpvd sglfsnrnnn agsfdsegva srrdslaplq aehsqpheka reevpalhpa
      661 shdvgkgirv alsniskdgn lmetaprvts fasnlhtdnl nakvkdkvyg cadgertqat
      721 ervnsqpvne kdsndknaal aptswhqrgq npgksyrlkh glttykiipp ksemrcydrd
      781 vslstgaiki delgnlvsph atgiriisls ssvpeaesqp igkvrefwrc nsvekhlgrp
      841 sessargpps tpvptqtqnp esrlqadpkp ispqqksahh egrnplgegr nqpptmgmgh
      901 vrvpaahtte vtflkpqrrt ssqyvasaia krigapkvha dvvrphgyae kgyagkapvl
      961 aappvtvkdd rtssphsetq gwkdgaqwpc vtppnnhged lavgapprge vigphrklst
     1021 qdrpaaihrs scfslvqssq rdrvsvgqsc gfsgkqstss qeassasepr rapdgtdppp
     1081 phtsdtqacs relvngsvra pghgepshpp ggsgteshil lereekpsvf stdgnetdsi
     1141 wppsifgpkk kfkpvvqrpv pkdtslhsal meaihsaggk drlrktaeht gegrpaklsy
     1201 teaegersal laairghsgt cslrkvpllv
//
LOCUS       NP_001265247             289 aa            linear   PRI 20-NOV-2025
DEFINITION  leukocyte immunoglobulin-like receptor subfamily A member 1 isoform
            2 precursor [Homo sapiens].
ACCESSION   NP_001265247
VERSION     NP_001265247.1
DBSOURCE    REFSEQ: accession NM_001278318.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Wang,K.S., Liu,X., Aragam,N., Mullersman,J.E., Jian,X., Pan,Y. and
            Liu,Y.
  TITLE     Polymorphisms in ABLIM1 are associated with personality traits and
            alcohol dependence
  JOURNAL   J Mol Neurosci 46 (2), 265-271 (2012)
   PUBMED   21547531
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Ryu,M., Chen,Y., Qi,J., Liu,J., Fan,Z., Nam,G., Shi,Y., Cheng,H.
            and Gao,G.F.
  TITLE     LILRA3 binds both classical and non-classical HLA class I molecules
            but with reduced affinities compared to LILRB1/LILRB2: structural
            evidence
  JOURNAL   PLoS One 6 (4), e19245 (2011)
   PUBMED   21559424
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Tedla,N., An,H., Borges,L., Vollmer-Conna,U., Bryant,K., Geczy,C.
            and McNeil,H.P.
  TITLE     Expression of activating and inhibitory leukocyte
            immunoglobulin-like receptors in rheumatoid synovium: correlations
            to disease activity
  JOURNAL   Tissue Antigens 77 (4), 305-316 (2011)
   PUBMED   21388353
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Jones,D.C., Kosmoliaptsis,V., Apps,R., Lapaque,N., Smith,I.,
            Kono,A., Chang,C., Boyle,L.H., Taylor,C.J., Trowsdale,J. and
            Allen,R.L.
  TITLE     HLA class I allelic sequence and conformation regulate leukocyte
            Ig-like receptor binding
  JOURNAL   J Immunol 186 (5), 2990-2997 (2011)
   PUBMED   21270408
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Brown,D., Trowsdale,J. and Allen,R.
  TITLE     The LILR family: modulators of innate and adaptive immune pathways
            in health and disease
  JOURNAL   Tissue Antigens 64 (3), 215-225 (2004)
   PUBMED   15304001
  REMARK    Review article
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Allen,R.L., Raine,T., Haude,A., Trowsdale,J. and Wilson,M.J.
  TITLE     Leukocyte receptor complex-encoded immunomodulatory receptors show
            differing specificity for alternative HLA-B27 structures
  JOURNAL   J Immunol 167 (10), 5543-5547 (2001)
   PUBMED   11698424
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Liu,W.R., Kim,J., Nwankwo,C., Ashworth,L.K. and Arm,J.P.
  TITLE     Genomic organization of the human leukocyte immunoglobulin-like
            receptors within the leukocyte receptor complex on chromosome
            19q13.4
  JOURNAL   Immunogenetics 51 (8-9), 659-669 (2000)
   PUBMED   10941837
REFERENCE   9  (residues 1 to 289)
  AUTHORS   Wilson,M.J., Torkar,M., Haude,A., Milne,S., Jones,T., Sheer,D.,
            Beck,S. and Trowsdale,J.
  TITLE     Plasticity in the organization and sequences of human KIR/ILT gene
            families
  JOURNAL   Proc Natl Acad Sci U S A 97 (9), 4778-4783 (2000)
   PUBMED   10781084
REFERENCE   10 (residues 1 to 289)
  AUTHORS   Borges,L., Hsu,M.L., Fanger,N., Kubin,M. and Cosman,D.
  TITLE     A family of human lymphoid and myeloid Ig-like receptors, some of
            which bind to MHC class I molecules
  JOURNAL   J Immunol 159 (11), 5192-5196 (1997)
   PUBMED   9548455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA999265.1, AF025530.1 and
            AC245036.3.
            
            Summary: This gene encodes an activating member of the leukocyte
            immunoglobulin-like receptor (LIR) family, which is found in a gene
            cluster at chromosomal region 19q13.4. The encoded protein is
            predominantly expressed in B cells, interacts with major
            histocompatibility complex class I ligands, and contributes to the
            regulation of immune responses. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (2, also known as LIR6b) lacks two
            consecutive in-frame exons in the coding region, compared to
            variant 1. The encoded isoform (2) is shorter, compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF025529.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155751 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal (PMID:9548455)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..289
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     A member 1 isoform 2 precursor"
                     /note="leukocyte immunoglobulin-like receptor 6; CD85
                     antigen-like family member I; leukocyte
                     immunoglobulin-like receptor, subfamily A (with TM
                     domain), member 1; leucocyte Ig-like receptor A1;
                     leukocyte immunoglobulin-like receptor subfamily A member
                     1"
                     /calculated_mol_wt=29223
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2519
     Region          28..118
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,107)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          111..118
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          124..219
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          153..157
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          180..184
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          212..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..289
                     /gene="LILRA1"
                     /gene_synonym="CD85I; LIR-6; LIR6"
                     /coded_by="NM_001278318.2:199..1068"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS62802.1"
                     /db_xref="GeneID:11024"
                     /db_xref="HGNC:HGNC:6602"
                     /db_xref="MIM:604810"
ORIGIN      
        1 mtpivtvlic lrlslgprth vqagtlpkpt lwaepgsvit qgspvtlwcq giletqeyrl
       61 yrekktapwi tripqeivkk gqfpipsitw ehtgryrcfy gshtagwsep sdplelvvtg
      121 ayikptlsal pspvvtsggn vtlhcvsqva fgsfilckeg edehpqclns qprthgwsra
      181 ifsvgpvsps rrwsyrcyay dsnsphvwsl psdllellvl gaaetlsppq nksdskagaa
      241 ntlspsqnkt ashpqdytve nlirmgiagl vlvvlgillf eaqhsqrsl
//
LOCUS       NP_009140                123 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL29 [Homo sapiens].
ACCESSION   NP_009140
VERSION     NP_009140.1
DBSOURCE    REFSEQ: accession NM_007209.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Liu,P.Y., Tee,A.E., Milazzo,G., Hannan,K.M., Maag,J., Mondal,S.,
            Atmadibrata,B., Bartonicek,N., Peng,H., Ho,N., Mayoh,C.,
            Ciaccio,R., Sun,Y., Henderson,M.J., Gao,J., Everaert,C.,
            Hulme,A.J., Wong,M., Lan,Q., Cheung,B.B., Shi,L., Wang,J.Y.,
            Simon,T., Fischer,M., Zhang,X.D., Marshall,G.M., Norris,M.D.,
            Haber,M., Vandesompele,J., Li,J., Mestdagh,P., Hannan,R.D.,
            Dinger,M.E., Perini,G. and Liu,T.
  TITLE     The long noncoding RNA lncNB1 promotes tumorigenesis by interacting
            with ribosomal protein RPL35
  JOURNAL   Nat Commun 10 (1), 5026 (2019)
   PUBMED   31690716
  REMARK    GeneRIF: This study therefore identifies lncNB1 and its binding
            protein RPL35 as key factors for promoting E2F1 protein synthesis,
            N-Myc protein stability and N-Myc-driven oncogenesis, and as
            therapeutic targets.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Mazumder,B., Sampath,P., Seshadri,V., Maitra,R.K., DiCorleto,P.E.
            and Fox,P.L.
  TITLE     Regulated release of L13a from the 60S ribosomal subunit as a
            mechanism of transcript-specific translational control
  JOURNAL   Cell 115 (2), 187-198 (2003)
   PUBMED   14567916
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BM854016.1, U12465.1 and CR996819.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L29P family of ribosomal proteins. It is located in the
            cytoplasm. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV759294.1, BM740758.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000348462.6/ ENSP00000259469.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..123
                     /product="large ribosomal subunit protein uL29"
                     /note="60S ribosomal protein L35"
                     /calculated_mol_wt=14420
     Region          8..63
                     /region_name="Ribosomal_L29"
                     /note="Ribosomal L29 protein; pfam00831"
                     /db_xref="CDD:459954"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P42766.2)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42766.2)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P42766.2)"
     Region          86..123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42766.2)"
     CDS             1..123
                     /gene="RPL35"
                     /gene_synonym="DBA19; L35; uL29"
                     /coded_by="NM_007209.4:46..417"
                     /db_xref="CCDS:CCDS6858.1"
                     /db_xref="GeneID:11224"
                     /db_xref="HGNC:HGNC:10344"
                     /db_xref="MIM:618315"
ORIGIN      
        1 makikardlr gkkkeellkq lddlkvelsq lrvakvtgga asklskirvv rksiarvltv
       61 inqtqkenlr kfykgkkykp ldlrpkktra mrrrlnkhee nlktkkqqrk erlyplrkya
      121 vka
//
LOCUS       NP_758952               1137 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-4 [Homo
            sapiens].
ACCESSION   NP_758952
VERSION     NP_758952.4
DBSOURCE    REFSEQ: accession NM_172364.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1137)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1137)
  AUTHORS   Schlegel,D.K., Glasauer,S.M.K., Mateos,J.M., Barmettler,G.,
            Ziegler,U. and Neuhauss,S.C.F.
  TITLE     A New Zebrafish Model for CACNA2D4-Dysfunction
  JOURNAL   Invest Ophthalmol Vis Sci 60 (15), 5124-5135 (2019)
   PUBMED   31834350
  REMARK    GeneRIF: We find that increasing the expression of Cav at the
            synaptic membrane is an evolutionarily conserved function of
            Cacna2d4b. Yet, since both paralogs participate in cone synaptic
            transmission, we propose partial subfunctionalization in zebrafish.
            Similar to human patients, our double KO zebrafish model shows mild
            cone dysfunction, which was not associated with signs of retinal
            degeneration.
REFERENCE   3  (residues 1 to 1137)
  AUTHORS   Chiang,J.P., Luo,H., Duan,J., Ekstein,J. and Hirsch,Y.
  TITLE     Founder Ashkenazi Jewish mutations of large deletion in the
            inherited retinal dystrophy genes
  JOURNAL   Ophthalmic Genet 39 (1), 135-136 (2018)
   PUBMED   28726569
  REMARK    GeneRIF: We have confirmed the TRPM1 36,445 bp deletion is a
            founder mutation in the Ashkenazi-Jewish (AJ) population with a
            carrier rate of 1 in 50. We have also confirmed the 35,741 bp
            deletion in the CACNA2D4 gene is a founder mutation in the AJ
            population with a carrier rate of 1 in 56.
REFERENCE   4  (residues 1 to 1137)
  AUTHORS   Dolphin,A.C.
  TITLE     Voltage-gated calcium channels and their auxiliary subunits:
            physiology and pathophysiology and pharmacology
  JOURNAL   J Physiol 594 (19), 5369-5390 (2016)
   PUBMED   27273705
  REMARK    Review article
REFERENCE   5  (residues 1 to 1137)
  AUTHORS   Ba-Abbad,R., Arno,G., Carss,K., Stirrups,K., Penkett,C.J.,
            Moore,A.T., Michaelides,M., Raymond,F.L., Webster,A.R. and
            Holder,G.E.
  TITLE     Mutations in CACNA2D4 Cause Distinctive Retinal Dysfunction in
            Humans
  JOURNAL   Ophthalmology 123 (3), 668-71 (2016)
   PUBMED   26560832
  REMARK    GeneRIF: This report describes a distinctive ERG phenotype,
            predominantly involving the cone pathways, in 2 unrelated patients
            from different ethnic backgrounds with homozygous mutations in
            CACNA2D4 and normal retinal imaging
REFERENCE   6  (residues 1 to 1137)
  AUTHORS   McGue,M., Zhang,Y., Miller,M.B., Basu,S., Vrieze,S., Hicks,B.,
            Malone,S., Oetting,W.S. and Iacono,W.G.
  TITLE     A genome-wide association study of behavioral disinhibition
  JOURNAL   Behav Genet 43 (5), 363-373 (2013)
   PUBMED   23942779
REFERENCE   7  (residues 1 to 1137)
  AUTHORS   Bannister,R.A. and Beam,K.G.
  TITLE     Ca(V)1.1: The atypical prototypical voltage-gated Ca(2) channel
  JOURNAL   Biochim Biophys Acta 1828 (7), 1587-1597 (2013)
   PUBMED   22982493
  REMARK    Review article
REFERENCE   8  (residues 1 to 1137)
  AUTHORS   Van Den Bossche,M.J., Strazisar,M., De Bruyne,S., Bervoets,C.,
            Lenaerts,A.S., De Zutter,S., Nordin,A., Norrback,K.F., Goossens,D.,
            De Rijk,P., Green,E.K., Grozeva,D., Mendlewicz,J., Craddock,N.,
            Sabbe,B.G., Adolfsson,R., Souery,D. and Del-Favero,J.
  TITLE     Identification of a CACNA2D4 deletion in late onset bipolar
            disorder patients and implications for the involvement of
            voltage-dependent calcium channels in psychiatric disorders
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 159B (4), 465-475 (2012)
   PUBMED   22488967
  REMARK    GeneRIF: A rare, partial deletion of 35.7 kb in CACNA2D4 in two
            unrelated late onset bipolar I patients and in one control
            individual, were identified.
REFERENCE   9  (residues 1 to 1137)
  AUTHORS   Wycisk,K.A., Zeitz,C., Feil,S., Wittmer,M., Forster,U.,
            Neidhardt,J., Wissinger,B., Zrenner,E., Wilke,R., Kohl,S. and
            Berger,W.
  TITLE     Mutation in the auxiliary calcium-channel subunit CACNA2D4 causes
            autosomal recessive cone dystrophy
  JOURNAL   Am J Hum Genet 79 (5), 973-977 (2006)
   PUBMED   17033974
REFERENCE   10 (residues 1 to 1137)
  AUTHORS   Qin,N., Yagel,S., Momplaisir,M.L., Codd,E.E. and D'Andrea,M.R.
  TITLE     Molecular cloning and characterization of the human voltage-gated
            calcium channel alpha(2)delta-4 subunit
  JOURNAL   Mol Pharmacol 62 (3), 485-496 (2002)
   PUBMED   12181424
  REMARK    GeneRIF: Calcium channel alpha(2)delta-4 subunit has limited
            distribution in special cell types of the pituitary, adrenal gland,
            colon, and fetal liver.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF516695.1, AC005342.1,
            BX537437.1 and AC005343.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 15, 2007 this sequence version replaced NP_758952.3.
            
            Summary: This gene encodes a member of the alpha-2/delta subunit
            family, a protein in the voltage-dependent calcium channel complex.
            Calcium channels mediate the influx of calcium ions into the cell
            upon membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. Research on a
            highly similar protein in rabbit suggests the protein described in
            this record is cleaved into alpha-2 and delta subunits. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537437.1, AF516695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382722.10/ ENSP00000372169.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1137
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..1137
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-4"
                     /note="voltage-gated calcium channel alpha(2)delta-4
                     subunit; calcium channel, voltage-dependent, alpha 2/delta
                     subunit 4; voltage-gated calcium channel subunit
                     alpha-2/delta-4; alpha2delta-4"
                     /calculated_mol_wt=127808
     Region          148..264
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3S7.2)"
     Region          277..460
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(297,299,301,371,405)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          297..301
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3S7.2)"
     Region          <484..537
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Region          539..654
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Region          661..1110
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            664
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3S7.2)"
     Site            1116..1136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3S7.2)"
     CDS             1..1137
                     /gene="CACNA2D4"
                     /gene_synonym="RCD4"
                     /coded_by="NM_172364.5:180..3593"
                     /db_xref="CCDS:CCDS44785.1"
                     /db_xref="GeneID:93589"
                     /db_xref="HGNC:HGNC:20202"
                     /db_xref="MIM:608171"
ORIGIN      
        1 mvcgcsallp lpnprptmpa tpnflanpss ssrwiplqpm pvawafvqkt sallwllllg
       61 tslspawgqa kipletvklw adtfggdlyn tvtkysgsll lqkkykdves slkieevdgl
      121 elvrkfsedm enmlrrkvea vqnlveaaee adlnhefnes lvfdyynsvl inerdekgnf
      181 velgaeflle snahfsnlpv ntsissvqlp tnvynkdpdi lngvymseal navfvenfqr
      241 dptltwqyfg satgffriyp gikwtpdeng vitfdcrnrg wyiqaatspk divilvdvsg
      301 smkglrmtia khtittildt lgendfinii ayndyvhyie pcfkgilvqa drdnrehfkl
      361 lveelmvkgv gvvdqalrea fqilkqfqea kqgslcnqai mlisdgaved yepvfekynw
      421 pdckvrvfty ligrevsfad rmkwiacnnk gyytqistla dtqenvmeyl hvlsrpmvin
      481 hdhdiiwtea ymdskllssq aqsltllttv ampvfskkne trshgillgv vgsdvalrel
      541 mklapryklg vhgyaflntn ngyilshpdl rplyregkkl kpkpnynsvd lsevewedqa
      601 eslrtaminr etgtlsmdvk vpmdkgkrvl fltndyfftd isdtpfslgv vlsrghgeyi
      661 llgntsveeg lhdllhpdla lagdwiycit didpdhrkls qleamirflt rkdpdlecde
      721 elvrevlfda vvtapmeayw talalnmsee sehvvdmafl gtragllrss lfvgsekvsd
      781 rkfltpedea svftldrfpl wyrqasehpa gsfvfnlrwa egpesagepm vvtastavav
      841 tvdkrtaiaa aagvqmklef lqrkfwaatr qcstvdgpct qscedsdldc fvidnngfil
      901 iskrsretgr flgevdgavl tqllsmgvfs qvtmydyqam ckpsshhhsa aqplvspisa
      961 fltatrwllq elvlfllews vwgswydrga eaksvfhhsh khkkqdplqp cdteypvfvy
     1021 qpaireangi vecgpcqkvf vvqqipnsnl lllvtdptcd csifppvlqe atevkynasv
     1081 kcdrmrsqkl rrrpdschaf hpeenaqdcg gasdtsaspp llllpvcawg llpqllr
//
LOCUS       NP_000519               1011 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal alpha-mannosidase isoform 1 precursor [Homo sapiens].
ACCESSION   NP_000519
VERSION     NP_000519.2
DBSOURCE    REFSEQ: accession NM_000528.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1011)
  AUTHORS   Lehalle,D., Colombo,R., O'Grady,M., Heron,B., Houcinat,N.,
            Kuentz,P., Moutton,S., Sorlin,A., Thevenon,J., Delanne,J., Gay,S.,
            Racine,C., Garde,A., Tran Mau-Them,F., Philippe,C., Vitobello,A.,
            Nambot,S., Huet,F., Duffourd,Y., Feillet,F., Thauvin-Robinet,C.,
            Marlin,S. and Faivre,L.
  TITLE     Hearing impairment as an early sign of alpha-mannosidosis in
            children with a mild phenotype: Report of seven new cases
  JOURNAL   Am J Med Genet A 179 (9), 1756-1763 (2019)
   PUBMED   31241255
  REMARK    GeneRIF: A diagnosis can be established by measuring the activity
            of lysosomal alpha-mannosidase in leucocytes and screening for
            abnormal urinary excretion of mannose-rich oligosaccharides.
            Genetic confirmation is obtained with the identification of MAN2B1
            mutations.
REFERENCE   2  (residues 1 to 1011)
  AUTHORS   Yu,P., Cui,Y., Cai,W., Wu,H., Xiao,X., Shao,Q., Ma,L., Guo,S.,
            Wu,N., Jin,Z.B., Wang,Y., Cai,T., Sun,Z.S. and Qu,J.
  TITLE     Lysosomal storage disease in the brain: mutations of the
            beta-mannosidase gene identified in autosomal dominant nystagmus
  JOURNAL   Genet Med 17 (12), 971-979 (2015)
   PUBMED   25741867
  REMARK    GeneRIF: A novel heterozygous mutation (c.2013G>A; p.R638H) of
            MANBA was identified in patients with autosomal-dominant nystagmus.
            An additional mutation (c.2346T>A; p.L749H) in MANBA was found by
            screening patients with sporadic nystagmus.
REFERENCE   3  (residues 1 to 1011)
  AUTHORS   Borgwardt,L., Stensland,H.M., Olsen,K.J., Wibrand,F., Klenow,H.B.,
            Beck,M., Amraoui,Y., Arash,L., Fogh,J., Nilssen,O., Dali,C.I. and
            Lund,A.M.
  TITLE     Alpha-mannosidosis: correlation between phenotype, genotype and
            mutant MAN2B1 subcellular localisation
  JOURNAL   Orphanet J Rare Dis 10, 70 (2015)
   PUBMED   26048034
  REMARK    GeneRIF: Our results indicate a correlation between the MAN2B1
            genotypes and the cognitive function, upper limb coordination,
            balance, FVC% and the storage of oligosaccharides in CSF.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1011)
  AUTHORS   Thaysen-Andersen,M., Venkatakrishnan,V., Loke,I., Laurini,C.,
            Diestel,S., Parker,B.L. and Packer,N.H.
  TITLE     Human neutrophils secrete bioactive paucimannosidic proteins from
            azurophilic granules into pathogen-infected sputum
  JOURNAL   J Biol Chem 290 (14), 8789-8802 (2015)
   PUBMED   25645918
REFERENCE   5  (residues 1 to 1011)
  AUTHORS   Manichaikul,A., Hoffman,E.A., Smolonska,J., Gao,W., Cho,M.H.,
            Baumhauer,H., Budoff,M., Austin,J.H., Washko,G.R., Carr,J.J.,
            Kaufman,J.D., Pottinger,T., Powell,C.A., Wijmenga,C., Zanen,P.,
            Groen,H.J., Postma,D.S., Wanner,A., Rouhani,F.N., Brantly,M.L.,
            Powell,R., Smith,B.M., Rabinowitz,D., Raffel,L.J., Hinckley
            Stukovsky,K.D., Crapo,J.D., Beaty,T.H., Hokanson,J.E.,
            Silverman,E.K., Dupuis,J., O'Connor,G.T., Boezen,H.M., Rich,S.S.
            and Barr,R.G.
  TITLE     Genome-wide study of percent emphysema on computed tomography in
            the general population. The Multi-Ethnic Study of Atherosclerosis
            Lung/SNP Health Association Resource Study
  JOURNAL   Am J Respir Crit Care Med 189 (4), 408-418 (2014)
   PUBMED   24383474
REFERENCE   6  (residues 1 to 1011)
  AUTHORS   Emiliani,C., Martino,S., Stirling,J.L., Maras,B. and Orlacchio,A.
  TITLE     Partial sequence of the purified protein confirms the identity of
            cDNA coding for human lysosomal alpha-mannosidase B
  JOURNAL   Biochem J 305 (Pt 2) (Pt 2), 363-366 (1995)
   PUBMED   7832746
REFERENCE   7  (residues 1 to 1011)
  AUTHORS   Ficicioglu,C. and Stepien,K.M.
  TITLE     Alpha-Mannosidosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301570
REFERENCE   8  (residues 1 to 1011)
  AUTHORS   Kaneda,Y., Hayes,H., Uchida,T., Yoshida,M.C. and Okada,Y.
  TITLE     Regional assignment of five genes on human chromosome 19
  JOURNAL   Chromosoma 95 (1), 8-12 (1987)
   PUBMED   3034518
REFERENCE   9  (residues 1 to 1011)
  AUTHORS   Champion,M.J. and Shows,T.B.
  TITLE     Electrophoretic abnormalities of lysosomal enzymes in mucolipidosis
            fibroblast lines
  JOURNAL   Am J Hum Genet 29 (2), 149-163 (1977)
   PUBMED   848490
REFERENCE   10 (residues 1 to 1011)
  AUTHORS   Phillips,N.C., Robinson,D. and Winchester,B.G.
  TITLE     Characterization of human liver alpha-D-mannosidase purified by
            affinity chromatography
  JOURNAL   Biochem J 153 (3), 579-587 (1976)
   PUBMED   821469
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB237901.1 and BC000736.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 3, 2004 this sequence version replaced NP_000519.1.
            
            Summary: This gene encodes an enzyme that hydrolyzes terminal,
            non-reducing alpha-D-mannose residues in alpha-D-mannosides. Its
            activity is necessary for the catabolism of N-linked carbohydrates
            released during glycoprotein turnover and it is member of family 38
            of glycosyl hydrolases. The full length protein is processed in two
            steps. First, a 49 aa leader sequence is cleaved off and the
            remainder of the protein is processed into 3 peptides of 70 kDa, 42
            kDa (D) and 13/15 kDa (E). Next, the 70 kDa peptide is further
            processed into three peptides (A, B and C). The A, B and C peptides
            are disulfide-linked. Defects in this gene have been associated
            with lysosomal alpha-mannosidosis. Alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291572.1, SRR1803612.260285.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000456935.7/ ENSP00000395473.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1011
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..1011
                     /product="lysosomal alpha-mannosidase isoform 1 precursor"
                     /EC_number="3.2.1.24"
                     /note="mannosidase, alpha B, lysosomal; lysosomal acid
                     alpha-mannosidase; lysosomal alpha-mannosidase;
                     mannosidase alpha-B"
                     /calculated_mol_wt=108714
     sig_peptide     1..49
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5049
     mat_peptide     50..1011
                     /product="lysosomal alpha-mannosidase isoform 1"
                     /calculated_mol_wt=108714
     mat_peptide     50..345
                     /product="lysosomal alpha-mannosidase A peptide"
                     /calculated_mol_wt=34257
     Region          63..1000
                     /region_name="PLN02701"
                     /note="alpha-mannosidase"
                     /db_xref="CDD:178304"
     Region          63..341
                     /region_name="GH38N_AMII_LAM_like"
                     /note="N-terminal catalytic domain of lysosomal
                     alpha-mannosidase and similar proteins; glycoside
                     hydrolase family 38 (GH38); cd10810"
                     /db_xref="CDD:212121"
     Site            order(72,74,77,196,198,220,319)
                     /site_type="active"
                     /db_xref="CDD:212121"
     Site            order(74..80,155..171,173..174,196,198..203,207,220..225,
                     241..243)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:212121"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            310
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     346..429
                     /product="lysosomal alpha-mannosidase B peptide"
                     /calculated_mol_wt=9578
     Site            367
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     430..601
                     /product="lysosomal alpha-mannosidase C peptide"
                     /calculated_mol_wt=18886
     Site            497
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     602..882
                     /product="lysosomal alpha-mannosidase D peptide"
                     /calculated_mol_wt=31575
     Site            645
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            651
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            692
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            766
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            832
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     mat_peptide     883..1011
                     /product="lysosomal alpha-mannosidase E peptide"
                     /calculated_mol_wt=14491
     Site            930
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     Site            989
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00754.3)"
     CDS             1..1011
                     /gene="MAN2B1"
                     /gene_synonym="LAMAN; MANB"
                     /coded_by="NM_000528.4:42..3077"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS32919.1"
                     /db_xref="GeneID:4125"
                     /db_xref="HGNC:HGNC:6826"
                     /db_xref="MIM:609458"
ORIGIN      
        1 mgayarasgv cargcldsag pwtmsralrp plpplcffll llaaagarag gyetcptvqp
       61 nmlnvhllph thddvgwlkt vdqyfygikn diqhagvqyi ldsvisalla dptrrfiyve
      121 iaffsrwwhq qtnatqevvr dlvrqgrlef anggwvmnde aathygaivd qmtlglrfle
      181 dtfgndgrpr vawhidpfgh sreqaslfaq mgfdgfffgr ldyqdkwvrm qklemeqvwr
      241 astslkppta dlftgvlpng ynpprnlcwd vlcvdqplve dprspeynak elvdyflnva
      301 taqgryyrtn htvmtmgsdf qyenanmwfk nldklirlvn aqqakgssvh vlystpacyl
      361 welnkanltw svkhddffpy adgphqfwtg yfssrpalkr yerlsynflq vcnqlealvg
      421 laanvgpygs gdsaplneam avlqhhdavs gtsrqhvand yarqlaagwg pcevllsnal
      481 arlrgfkdhf tfcqqlnisi cplsqtaarf qvivynplgr kvnwmvrlpv segvfvvkdp
      541 ngrtvpsdvv ifpssdsqah ppellfsasl palgfstysv aqvprwkpqa rapqpiprrs
      601 wspaltiene hiratfdpdt gllmeimnmn qqlllpvrqt ffwynasigd nesdqasgay
      661 ifrpnqqkpl pvsrwaqihl vktplvqevh qnfsawcsqv vrlypgqrhl elewsvgpip
      721 vgdtwgkevi srfdtpletk grfytdsngr eilerrrdyr ptwklnqtep vagnyypvnt
      781 riyitdgnmq ltvltdrsqg gsslrdgsle lmvhrrllkd dgrgvseplm engsgawvrg
      841 rhlvlldtaq aaaaghrlla eqevlapqvv lapgggaayn lgapprtqfs glrrdlppsv
      901 hlltlaswgp emvllrlehq favgedsgrn lsapvtlnlr dlfstftitr lqettlvanq
      961 lreaasrlkw ttntgptphq tpyqldpani tlepmeirtf lasvqwkevd g
//
LOCUS       NP_005405                684 aa            linear   PRI 20-NOV-2025
DEFINITION  ski-like protein isoform 1 [Homo sapiens].
ACCESSION   NP_005405
VERSION     NP_005405.2
DBSOURCE    REFSEQ: accession NM_005414.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Chi,C., Liang,X., Cui,T., Gao,X., Liu,R. and Yin,C.
  TITLE     SKIL/SnoN attenuates TGF-beta1/SMAD signaling-dependent collagen
            synthesis in hepatic fibrosis
  JOURNAL   Biomol Biomed 23 (6), 1014-1025 (2023)
   PUBMED   37389959
  REMARK    GeneRIF: SKIL/SnoN attenuates TGF-beta1/SMAD signaling-dependent
            collagen synthesis in hepatic fibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Lu,Z., Zhang,Y., Yan,H., Su,Y., Guo,L., Liao,Y., Lu,T., Yu,H.,
            Wang,L., Li,J., Li,W., Yang,Y., Xiao,X., Lv,L., Tan,Y., Zhang,D.
            and Yue,W.
  TITLE     ATAD3B and SKIL polymorphisms associated with antipsychotic-induced
            QTc interval change in patients with schizophrenia: a genome-wide
            association study
  JOURNAL   Transl Psychiatry 12 (1), 56 (2022)
   PUBMED   35136033
  REMARK    GeneRIF: ATAD3B and SKIL polymorphisms associated with
            antipsychotic-induced QTc interval change in patients with
            schizophrenia: a genome-wide association study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Ma,F., Ding,M.G., Lei,Y.Y., Luo,L.H., Jiang,S., Feng,Y.H. and
            Liu,X.L.
  TITLE     SKIL facilitates tumorigenesis and immune escape of NSCLC via
            upregulating TAZ/autophagy axis
  JOURNAL   Cell Death Dis 11 (12), 1028 (2020)
   PUBMED   33268765
  REMARK    GeneRIF: SKIL facilitates tumorigenesis and immune escape of NSCLC
            via upregulating TAZ/autophagy axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Cohen,S.B., Zheng,G., Heyman,H.C. and Stavnezer,E.
  TITLE     Heterodimers of the SnoN and Ski oncoproteins form preferentially
            over homodimers and are more potent transforming agents
  JOURNAL   Nucleic Acids Res 27 (4), 1006-1014 (1999)
   PUBMED   9927733
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Pearson-White,S. and Crittenden,R.
  TITLE     Proto-oncogene Sno expression, alternative isoforms and immediate
            early serum response
  JOURNAL   Nucleic Acids Res 25 (14), 2930-2937 (1997)
   PUBMED   9207045
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Pearson-White,S.
  TITLE     SnoI, a novel alternatively spliced isoform of the ski
            protooncogene homolog, sno
  JOURNAL   Nucleic Acids Res 21 (19), 4632-4638 (1993)
   PUBMED   8233802
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Nagase,T., Nomura,N. and Ishii,S.
  TITLE     Complex formation between proteins encoded by the ski gene family
  JOURNAL   J Biol Chem 268 (18), 13710-13716 (1993)
   PUBMED   8514802
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Nomura,N., Sasamoto,S., Ishii,S., Date,T., Matsui,M. and
            Ishizaki,R.
  TITLE     Isolation of human cDNA clones of ski and the ski-related gene, sno
  JOURNAL   Nucleic Acids Res 17 (14), 5489-5500 (1989)
   PUBMED   2762147
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA464211.1, AC073288.27,
            BC059386.1, X15219.1 and AI245308.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 10, 2009 this sequence version replaced NP_005405.1.
            
            Summary: The protein encoded by this gene is a component of the
            SMAD pathway, which regulates cell growth and differentiation
            through transforming growth factor-beta (TGFB). In the absence of
            ligand, the encoded protein binds to the promoter region of
            TGFB-responsive genes and recruits a nuclear repressor complex.
            TGFB signaling causes SMAD3 to enter the nucleus and degrade this
            protein, allowing these genes to be activated. Four transcript
            variants encoding three different isoforms have been found for this
            gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1, also known as snoN).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.112482.1,
                                           SRR1660809.15608.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259119.9/ ENSP00000259119.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..684
                     /product="ski-like protein isoform 1"
                     /note="ski-like protein; ski-related oncogene snoN;
                     SKI-like oncogene"
                     /calculated_mol_wt=76845
     Region          137..236
                     /region_name="DHD_Sno"
                     /note="Dachshund-homology domain found in Ski-like protein
                     (Sno) and similar proteins; cd21084"
                     /db_xref="CDD:410787"
     Region          261..356
                     /region_name="c-SKI_SMAD_bind"
                     /note="c-SKI Smad4 binding domain; smart01046"
                     /db_xref="CDD:198114"
     Region          355..>684
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          420..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12757.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12757.2)"
     Region          <536..>684
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..684
                     /gene="SKIL"
                     /gene_synonym="SNO; SnoA; SnoI; SnoN"
                     /coded_by="NM_005414.5:683..2737"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33890.1"
                     /db_xref="GeneID:6498"
                     /db_xref="HGNC:HGNC:10897"
                     /db_xref="MIM:165340"
ORIGIN      
        1 menlqtnfsl vqgstkklng mgddgsppak kmitdihang ktinkvptvk kehlddygea
       61 pvetdgehvk rtctsvpetl hlnpslkhtl aqfhlssqss lggpaafsar hsqesmsptv
      121 flplpspqvl pgpllipsds steltqtvle gesiscfqvg gekrlclpqv lnsvlreftl
      181 qqintvcdel yiycsrctsd qlhilkvlgi lpfnapscgl itltdaqrlc nallrprtfp
      241 qngsvlpaks slaqlketgs afeveheclg kcqglfapqf yvqpdapciq cleccgmfap
      301 qtfvmhshrs pdkrtchwgf esakwhcylh vnqkylgtpe ekklkiilee mkekfsmrsg
      361 krnqsktdap sgmelqswyp vikqegdhvs qthsflhpsy ylymcdkvva pnvsltsavs
      421 qskeltktea sksisrqsek ahssgklqkt vsypdvslee qekmdlktsr elcsrldasi
      481 snnstskrks esatcnlvrd inkvgiglva aasspllvkd viceddkgki meevmrtylk
      541 qqeklnlilq kkqqlqmevk mlsssksmke lteeqqnlqk eleslqneha qrmeefyveq
      601 kdlekkleqi mkqkctcdsn lekdkeaeya gqlaelrqrl dhaeadrqel qdelrqerea
      661 rqklemmike lklqilkssk take
//
LOCUS       NP_068809                127 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC2 isoform
            1 [Homo sapiens].
ACCESSION   NP_068809
VERSION     NP_068809.1
DBSOURCE    REFSEQ: accession NM_021974.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 127)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 127)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 127)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 127)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 127)
  AUTHORS   Pusch,C., Wang,Z., Roe,B. and Blin,N.
  TITLE     Genomic structure of the RNA polymerase II small subunit (hRPB14.4)
            locus (POLRF) and mapping to 22q13.1 by sequence identity
  JOURNAL   Genomics 34 (3), 440-442 (1996)
   PUBMED   8786150
REFERENCE   6  (residues 1 to 127)
  AUTHORS   Acker,J., Wintzerith,M., Vigneron,M. and Kedinger,C.
  TITLE     A 14.4 KDa acidic subunit of human RNA polymerase II with a
            putative leucine-zipper
  JOURNAL   DNA Seq 4 (5), 329-331 (1994)
   PUBMED   7803819
REFERENCE   7  (residues 1 to 127)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   8  (residues 1 to 127)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 127)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 127)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA372532.1 and AL031587.3.
            
            Summary: This gene encodes the sixth largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. In yeast, this polymerase subunit, in
            combination with at least two other subunits, forms a structure
            that stabilizes the transcribing polymerase on the DNA template.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no quality transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.493439.1,
                                           SRR3476690.250556.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442738.7/ ENSP00000403852.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..127
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..127
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC2 isoform 1"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC2; RNA Polymerase II subunit 14.4 kD; DNA-directed
                     RNA polymerase II subunit F; RNA polymerases I, II, and
                     III subunit ABC2; DNA-directed RNA polymerases I, II, and
                     III 14.4 kDa polypeptide; polymerase (RNA) II (DNA
                     directed) polypeptide F; polymerase (RNA) II subunit F"
                     /calculated_mol_wt=14347
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61218.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P61218.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000250|UniProtKB:O88828; propagated from
                     UniProtKB/Swiss-Prot (P61218.1)"
     Region          <26..127
                     /region_name="PLN00152"
                     /note="DNA-directed RNA polymerase; Provisional"
                     /db_xref="CDD:177755"
     CDS             1..127
                     /gene="POLR2F"
                     /gene_synonym="HRBP14.4; POLRF; RPABC14.4; RPABC2;
                     RPB14.4; RPB6; RPC15"
                     /coded_by="NM_021974.5:90..473"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13963.1"
                     /db_xref="GeneID:5435"
                     /db_xref="HGNC:HGNC:9193"
                     /db_xref="MIM:604414"
ORIGIN      
        1 msdnednfdg ddfddveede glddlenaee egqenveilp sgerpqanqk rittpymtky
       61 erarvlgtra lqiamcapvm velegetdpl liamkelkar kipiiirryl pdgsyedwgv
      121 deliitd
//
LOCUS       NP_001357483            1281 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFX7 isoform 3 [Homo sapiens].
ACCESSION   NP_001357483
VERSION     NP_001357483.1
DBSOURCE    REFSEQ: accession NM_001370554.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1281)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   3  (residues 1 to 1281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1281)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 1281)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   6  (residues 1 to 1281)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1281)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1281)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1281)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1281)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084783.2 and KF456052.1.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK128045.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1281
                     /product="DNA-binding protein RFX7 isoform 3"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=137738
     Region          8..86
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          <161..471
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          371..>648
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..1281
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_001370554.1:229..4074"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92004.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 msssraqqmh afswirntle ehpetslpkq evydeyksyc dnlgyhplsa adfgkimknv
       61 fpnmkarrlg trgkskycys glrkkafvhm ptlpnldfhk tgdglegaep sgqlqnidee
      121 vissacrlvc ewaqkvlsqp fdtvlelarf lvkshyigtk smaaltvmaa apagmkgitq
      181 psafiptaes nsfqpqvktl pspidakqql qrkiqkkqqe qklqsplpge saakksesat
      241 sngvtnlpng npsilspqpi givvaavpsp ipvqrtrqlv tspspmsssd gkvlplnvqv
      301 vtqhmqsvkq apktpqnvpa spggdrsarh rypqilpkpa ntsaltirsp ttvlftsspi
      361 ktavvpashm sslnvvkmtt isltpsnsnt plkhsasvss atgtteesrs vpqikngsvv
      421 slqspgsrss saggtsavev kvepetssde hpvqcqensd eakapqtpsa llgqksntdg
      481 alqkpsnegv ieikatkvcd qrtkcksrcn emlpgtstgn nqstitlsva sqnltftsss
      541 sppngdsink dpklctkspr krlsstlqet qvppvkkpiv eqlsaatieg qkqgsvkkdq
      601 kvphsgkteg stagaqipsk vsvnvsshig anqplnssal visdsaleqq ttpssspdik
      661 vklegsvfll dsdsksvgsf npngwqqitk dsefisasce qqqdisvmti pehsdindle
      721 ksvwelegmp qdtysqqlhs qiqesslnqi qahssdqlpl qselkefeps vsqtnesyfp
      781 fddeltqdsi veelvlmeqq msmnnshsyg nclgmtlqsq svtpgapmss htssthfyhp
      841 ihsngtpiht ptptptptpt ptptptptse miagsqslsr espcsrlaqt tpvdsalgss
      901 rhtpigtphs ncsssvppsp vecrnpfaft pisssmayhd asivssspvk pmqrpmathp
      961 dktklewmnn gysgvgnssv sghgilpsyq elvedrfrkp hafavpgqsy qsqsrhhdth
     1021 fgrltpvspv qhqgatvnnt nkqegfavpa pldnkgtnss assnfrcrsv spavhrqrnl
     1081 sgstlypvsn iprsnvtpfg spvtpevhvf tnvhtdacan niaqrsqsvp ltvmmqtafp
     1141 nalqkqansk kitnvllskl dsdnddavrg lgmnnlpsny tarmnltqil epstvfpsan
     1201 pqnmidssts vyefqtpsyl tksnstgqin fspgdnqaqs eigeqqldfn stvkdllsgd
     1261 slqtnqqlcs cpssllagmq m
//
LOCUS       NP_001351809             385 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001351809 XP_016861836
VERSION     NP_001351809.1
DBSOURCE    REFSEQ: accession NM_001364880.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008249.14 and AC108747.5.
            
            On Jul 13, 2018 this sequence version replaced XP_016861836.1.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.276746.1,
                                           SRR1803611.272165.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..385
                     /product="interleukin-1 receptor accessory protein isoform
                     4 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=41944
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     CDS             1..385
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_001364880.2:137..1294"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 8"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk efpsccpgws
      361 tvarsrlsat stswvqmill pqppe
//
LOCUS       NP_001035830             321 aa            linear   PRI 20-NOV-2025
DEFINITION  glycerol-3-phosphate phosphatase [Homo sapiens].
ACCESSION   NP_001035830 NP_077023 XP_001130630 XP_001130859
VERSION     NP_001035830.1
DBSOURCE    REFSEQ: accession NM_001042371.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Mora Lagares,L., Perez-Castillo,Y. and Novic,M.
  TITLE     Exploring the dynamics of the ABCB1 membrane transporter
            P-glycoprotein in the presence of ATP and active/non-active
            compounds through molecular dynamics simulations
  JOURNAL   Toxicology 502, 153732 (2024)
   PUBMED   38272384
  REMARK    GeneRIF: Exploring the dynamics of the ABCB1 membrane transporter
            P-glycoprotein in the presence of ATP and active/non-active
            compounds through molecular dynamics simulations.
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Torres,G.G., Nygaard,M., Caliebe,A., Blanche,H., Chantalat,S.,
            Galan,P., Lieb,W., Christiansen,L., Deleuze,J.F., Christensen,K.,
            Strauch,K., Muller-Nurasyid,M., Peters,A., Nothen,M.M.,
            Hoffmann,P., Flachsbart,F., Schreiber,S., Ellinghaus,D., Franke,A.,
            Dose,J. and Nebel,A.
  TITLE     Exome-Wide Association Study Identifies FN3KRP and PGP as New
            Candidate Longevity Genes
  JOURNAL   J Gerontol A Biol Sci Med Sci 76 (5), 786-795 (2021)
   PUBMED   33491046
  REMARK    GeneRIF: Exome-Wide Association Study Identifies FN3KRP and PGP as
            New Candidate Longevity Genes.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Segerer,G., Engelmann,D., Kaestner,A., Trotzmuller,M., Kofeler,H.,
            Stigloher,C., Thiele,C., Jeanclos,E. and Gohla,A.
  TITLE     A phosphoglycolate phosphatase/AUM-dependent link between
            triacylglycerol turnover and epidermal growth factor signaling
  JOURNAL   Biochim Biophys Acta Mol Cell Biol Lipids 1863 (6), 584-594 (2018)
   PUBMED   29524543
  REMARK    GeneRIF: data explain how PGP exerts control over EGF-induced
            cellular protein tyrosine phosphorylation, and reveal an unexpected
            influence of triacylglycerol turnover on growth factor signaling.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Beaudoin,G.A. and Hanson,A.D.
  TITLE     A Guardian Angel Phosphatase for Mainline Carbon Metabolism
  JOURNAL   Trends Biochem Sci 41 (11), 893-894 (2016)
   PUBMED   27544441
  REMARK    GeneRIF: Phosphoglycolate phosphatase rescues central carbon
            metabolism from toxic secondary metabolites in humans and yeast.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Collard,F., Baldin,F., Gerin,I., Bolsee,J., Noel,G., Graff,J.,
            Veiga-da-Cunha,M., Stroobant,V., Vertommen,D., Houddane,A.,
            Rider,M.H., Linster,C.L., Van Schaftingen,E. and Bommer,G.T.
  TITLE     A conserved phosphatase destroys toxic glycolytic side products in
            mammals and yeast
  JOURNAL   Nat Chem Biol 12 (8), 601-607 (2016)
   PUBMED   27294321
REFERENCE   6  (residues 1 to 321)
  AUTHORS   de Leon,J., Susce,M.T., Pan,R.M., Koch,W.H. and Wedlund,P.J.
  TITLE     Polymorphic variations in GSTM1, GSTT1, PgP, CYP2D6, CYP3A5, and
            dopamine D2 and D3 receptors and their association with tardive
            dyskinesia in severe mental illness
  JOURNAL   J Clin Psychopharmacol 25 (5), 448-456 (2005)
   PUBMED   16160620
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Turzanski,J., Grundy,M., Shang,S., Russell,N. and Pallis,M.
  TITLE     P-glycoprotein is implicated in the inhibition of ceramide-induced
            apoptosis in TF-1 acute myeloid leukemia cells by modulation of the
            glucosylceramide synthase pathway
  JOURNAL   Exp Hematol 33 (1), 62-72 (2005)
   PUBMED   15661399
  REMARK    GeneRIF: cerp-gp confers resistance to ceramide-induced apoptosis,
            with modulation of the ceramide-glucosylceramide pathway GCS making
            a marked contribution to this resistance
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Zhou,S., Chan,E., Pan,S.Q., Huang,M. and Lee,E.J.
  TITLE     Pharmacokinetic interactions of drugs with St John's wort
  JOURNAL   J Psychopharmacol 18 (2), 262-276 (2004)
   PUBMED   15260917
  REMARK    GeneRIF: 'The available data indicate that St. John's wort is a
            potent induced of CYP 3A4 and P-glycoprotein (PgP), although it may
            inhibit or induce other CYPs...' See page 262.
            Review article
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Mulley,J.C., Barton,N. and Callen,D.F.
  TITLE     Localisation of human PGP and HAGH genes to 16p13.3
  JOURNAL   Cytogenet Cell Genet 53 (2-3), 175-176 (1990)
   PUBMED   2164460
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Koeffler,H.P., Sparkes,R.S., Stang,H. and Mohandas,T.
  TITLE     Regional assignment of genes for human alpha-globin and
            phosphoglycollate phosphatase to the short arm of chromosome 16
  JOURNAL   Proc Natl Acad Sci U S A 78 (11), 7015-7018 (1981)
   PUBMED   6273902
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009065.8, AW161386.1, BC035985.1, DA336356.1 and AK026146.1.
            
            On or before Jul 31, 2014 this sequence version replaced
            NP_077023.1, XP_001130859.1, XP_001130630.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.10732.1,
                                           SRR1803616.239423.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333503.8/ ENSP00000330918.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..321
                     /product="glycerol-3-phosphate phosphatase"
                     /EC_number="3.1.3.48"
                     /EC_number="3.1.3.21"
                     /note="aspartate-based ubiquitous Mg(2+)-dependent
                     phosphatase"
                     /calculated_mol_wt=33875
     Region          28..319
                     /region_name="HAD_Pase_UmpH-like"
                     /note="UmpH/NagD family phosphatase, similar to human PGP
                     phosphoglycolate phosphatase and Schizosaccharomyces pombe
                     PHO2 p-nitrophenylphosphatase; cd07510"
                     /db_xref="CDD:319813"
     Site            order(34..38,66..69,172,201,204,235,259..261,264..265)
                     /site_type="active"
                     /db_xref="CDD:319813"
     Site            204
                     /site_type="other"
                     /note="Important for substrate specificity.
                     /evidence=ECO:0000250|UniProtKB:Q8CHP8; propagated from
                     UniProtKB/Swiss-Prot (A6NDG6.1)"
     CDS             1..321
                     /gene="PGP"
                     /gene_synonym="AUM; G3PP; PGPase"
                     /coded_by="NM_001042371.3:64..1029"
                     /db_xref="CCDS:CCDS42104.1"
                     /db_xref="GeneID:283871"
                     /db_xref="HGNC:HGNC:8909"
                     /db_xref="MIM:172280"
ORIGIN      
        1 maaaeaggdd arcvrlsaer aqalladvdt llfdcdgvlw rgetavpgap ealralrarg
       61 krlgfitnns sktraayaek lrrlgfggpa gpgaslevfg tayctalylr qrlagapapk
      121 ayvlgspala aeleavgvas vgvgpeplqg egpgdwlhap lepdvravvv gfdphfsymk
      181 ltkalrylqq pgcllvgtnm dnrlplengr fiagtgclvr avemaaqrqa diigkpsrfi
      241 fdcvsqeygi npertvmvgd rldtdillga tcglktiltl tgvstlgdvk nnqesdcvsk
      301 kkmvpdfyvd siadllpalq g
//
LOCUS       NP_001161402             356 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001161402
VERSION     NP_001161402.1
DBSOURCE    REFSEQ: accession NM_001167930.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA024801.1, AF538732.1 and
            AC008249.14.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Transcript Variant: This variant (5) has multiple differences,
            compared to variant 1. It encodes the soluble isoform (2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF538732.1, SRR1660803.90182.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..356
                     /product="interleukin-1 receptor accessory protein isoform
                     2 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=38714
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     CDS             1..356
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_001167930.2:137..1207"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS46982.1"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk gnrcgq
//
LOCUS       NP_001335589              93 aa            linear   PRI 20-NOV-2025
DEFINITION  UPF0547 protein C16orf87 isoform 2 [Homo sapiens].
ACCESSION   NP_001335589
VERSION     NP_001335589.1
DBSOURCE    REFSEQ: accession NM_001348660.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007225.2.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647945.1, SRR5189667.104649.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267771 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q11.2"
     Protein         1..93
                     /product="UPF0547 protein C16orf87 isoform 2"
                     /note="UPF0547 protein C16orf87"
                     /calculated_mol_wt=10300
     Region          14..38
                     /region_name="UPF0547"
                     /note="Uncharacterized protein family UPF0547; pfam10571"
                     /db_xref="CDD:402278"
     CDS             1..93
                     /gene="C16orf87"
                     /coded_by="NM_001348660.2:32..313"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86522.1"
                     /db_xref="GeneID:388272"
                     /db_xref="HGNC:HGNC:33754"
ORIGIN      
        1 msatrakkvk matkscpecd qqvpvacksc pcgyifisrk llnakhseks ppstekqeke
       61 idiyanlsde kafvfsvala einrkiinqr lil
//
LOCUS       NP_001316675              63 aa            linear   PRI 20-NOV-2025
DEFINITION  protein DPCD isoform 6 [Homo sapiens].
ACCESSION   NP_001316675
VERSION     NP_001316675.1
DBSOURCE    REFSEQ: accession NM_001329746.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 63)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 63)
  AUTHORS   Dos Santos Morais,R., Santo,P.E., Ley,M., Schelcher,C., Abel,Y.,
            Plassart,L., Desligniere,E., Chagot,M.E., Quinternet,M.,
            Paiva,A.C.F., Hessmann,S., Morellet,N., M F Sousa,P.,
            Vandermoere,F., Bertrand,E., Charpentier,B., Bandeiras,T.M.,
            Plisson-Chastang,C., Verheggen,C., Cianferani,S. and Manival,X.
  TITLE     Deciphering cellular and molecular determinants of human DPCD
            protein in complex with RUVBL1/RUVBL2 AAA-ATPases
  JOURNAL   J Mol Biol 434 (19), 167760 (2022)
   PUBMED   35901867
  REMARK    GeneRIF: Deciphering cellular and molecular determinants of human
            DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases.
REFERENCE   3  (residues 1 to 63)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 63)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 63)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 63)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 63)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 63)
  AUTHORS   Zariwala,M., O'Neal,W.K., Noone,P.G., Leigh,M.W., Knowles,M.R. and
            Ostrowski,L.E.
  TITLE     Investigation of the possible role of a novel gene, DPCD, in
            primary ciliary dyskinesia
  JOURNAL   Am J Respir Cell Mol Biol 30 (4), 428-434 (2004)
   PUBMED   14630615
  REMARK    GeneRIF: a novel candidate gene for primary ciliary dyskinesia
            GeneRIF: The mouse homolog of this gene (named Dpcd, for Deleted in
            a mouse model of Primary Ciliary Dyskinesia) appears to be
            responsible for an inner arm defect in cilia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627424.8.
            
            Summary: This gene in mouse encodes a protein that may be involved
            in the generation and maintenance of ciliated cells. In mouse,
            expression of this gene increases during ciliated cell
            differentiation, and disruption of this gene has been linked to
            primary ciliary dyskinesia. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.395373.1,
                                           SRR5189652.116996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..63
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..63
                     /product="protein DPCD isoform 6"
                     /note="protein DPCD; deleted in a mouse model of primary
                     ciliary dyskinesia; RP11-529I10.4"
                     /calculated_mol_wt=7141
     Region          6..>50
                     /region_name="DPCD"
                     /note="DPCD protein family; pfam14913"
                     /db_xref="CDD:464369"
     CDS             1..63
                     /gene="DPCD"
                     /coded_by="NM_001329746.2:17..208"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:25911"
                     /db_xref="HGNC:HGNC:24542"
                     /db_xref="MIM:616467"
ORIGIN      
        1 mavtgwlesl rtaqktallq dgrrkvhylf pdgkemaeey dektseller pecglmgrqe
       61 dlt
//
LOCUS       NP_003265               1259 aa            linear   PRI 20-NOV-2025
DEFINITION  trafficking protein particle complex subunit 10 isoform a [Homo
            sapiens].
ACCESSION   NP_003265
VERSION     NP_003265.3
DBSOURCE    REFSEQ: accession NM_003274.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1259)
  AUTHORS   Rawlins,L.E., Almousa,H., Khan,S., Collins,S.C., Milev,M.P.,
            Leslie,J., Saint-Dic,D., Khan,V., Hincapie,A.M., Day,J.O.,
            McGavin,L., Rowley,C., Harlalka,G.V., Vancollie,V.E., Ahmad,W.,
            Lelliott,C.J., Gul,A., Yalcin,B., Crosby,A.H., Sacher,M. and
            Baple,E.L.
  TITLE     Biallelic variants in TRAPPC10 cause a microcephalic TRAPPopathy
            disorder in humans and mice
  JOURNAL   PLoS Genet 18 (3), e1010114 (2022)
   PUBMED   35298461
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1259)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1259)
  AUTHORS   Cuenca,A., Insinna,C., Zhao,H., John,P., Weiss,M.A., Lu,Q.,
            Walia,V., Specht,S., Manivannan,S., Stauffer,J., Peden,A.A. and
            Westlake,C.J.
  TITLE     The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8
            for preciliary vesicle tethering at the mother centriole during
            ciliogenesis
  JOURNAL   J Biol Chem 294 (42), 15418-15434 (2019)
   PUBMED   31467083
REFERENCE   5  (residues 1 to 1259)
  AUTHORS   Lafreniere,R.G., Kibar,Z., Rochefort,D.L., Han,F.Y., Fon,E.A.,
            Dube,M.P., Kang,X., Baird,S., Korneluk,R.G., Rommens,J.M. and
            Rouleau,G.A.
  TITLE     Genomic structure of the human GT334 (EHOC-1) gene mapping to
            21q22.3
  JOURNAL   Gene 198 (1-2), 313-321 (1997)
   PUBMED   9370297
REFERENCE   6  (residues 1 to 1259)
  AUTHORS   Nagamine,K., Kudoh,J., Minoshima,S., Kawasaki,K., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Genomic organization and complete nucleotide sequence of the human
            PWP2 gene on chromosome 21
  JOURNAL   Genomics 42 (3), 528-531 (1997)
   PUBMED   9205129
REFERENCE   7  (residues 1 to 1259)
  AUTHORS   Nagamine,K., Kudoh,J., Kawasaki,K., Minoshima,S., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Genomic organization and complete nucleotide sequence of the TMEM1
            gene on human chromosome 21q22.3
  JOURNAL   Biochem Biophys Res Commun 235 (1), 185-190 (1997)
   PUBMED   9196060
REFERENCE   8  (residues 1 to 1259)
  AUTHORS   Nagamine,K., Kudoh,J., Minoshima,S., Kawasaki,K., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Isolation of cDNA for a novel human protein KNP-I that is
            homologous to the E. coli SCRP-27A protein from the autoimmune
            polyglandular disease type I (APECED) region of chromosome 21q22.3
  JOURNAL   Biochem Biophys Res Commun 225 (2), 608-616 (1996)
   PUBMED   8753807
REFERENCE   9  (residues 1 to 1259)
  AUTHORS   Yamakawa,K., Mitchell,S., Hubert,R., Chen,X.N., Colbern,S.,
            Huo,Y.K., Gadomski,C., Kim,U.J. and Korenberg,J.R.
  TITLE     Isolation and characterization of a candidate gene for progressive
            myoclonus epilepsy on 21q22.3
  JOURNAL   Hum Mol Genet 4 (4), 709-716 (1995)
   PUBMED   7633421
REFERENCE   10 (residues 1 to 1259)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB001523.1, AL559301.3,
            BC101728.1 and AB001517.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 18, 2004 this sequence version replaced NP_003265.2.
            
            Summary: The protein encoded by this gene is a transmembrane
            protein found in the cis-Golgi complex. The encoded protein is part
            of the multisubunit transport protein particle (TRAPP) complex and
            may be involved in vesicular transport from the endoplasmic
            reticulum to the Golgi. Mutations in this gene could be responsible
            for the Unverricht-Lundborg type of progressive myoclonus epilepsy,
            or for autoimmune polyglandular disease type 1. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U61500.1, U19252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291574.9/ ENSP00000291574.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1259
                     /product="trafficking protein particle complex subunit 10
                     isoform a"
                     /note="transmembrane protein 1; TRAPP 130 kDa subunit;
                     trafficking protein particle complex subunit 130; epilepsy
                     holoprosencephaly candidate-1 protein; trafficking protein
                     particle complex 10; transport protein particle subunit
                     TMEM1; TRAPP subunit TMEM1; trafficking protein particle
                     complex subunit TMEM1"
                     /calculated_mol_wt=142059
     Region          1069..1246
                     /region_name="TRAPPC10"
                     /note="Trafficking protein particle complex subunit 10,
                     TRAPPC10; pfam12584"
                     /db_xref="CDD:403698"
     CDS             1..1259
                     /gene="TRAPPC10"
                     /gene_synonym="EHOC-1; EHOC1; GT334; NEDMISS; TMEM1;
                     TRS130; TRS30"
                     /coded_by="NM_003274.5:186..3965"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13704.1"
                     /db_xref="GeneID:7109"
                     /db_xref="HGNC:HGNC:11868"
                     /db_xref="MIM:602103"
ORIGIN      
        1 mdaseeplpp viytmenkpi vtcagdqnlf tsvyptlsqq lprepmewrr sygrapkmih
       61 lesnfvqfke ellpkegnka lltfpflhiy wteccdtevy katvkddltk wqnvlkahss
      121 vdwliviven dakkknktni lprtsivdki rndfcnkqsd rcvvlsdplk dssrtqeswn
      181 afltklrtll lmsftknlgk feddmrtlre krtepgwsfc eyfmvqeela fvfemlqqfe
      241 dalvqydeld alfsqyvvnf gagdganwlt ffcqpvkswn glilrkpidm ekresiqrre
      301 atlldlrsyl fsrqctlllf lqrpwevaqr alellhncvq elkllevsvp pgaldcwvfl
      361 sclevlqrie gccdraqids niahtvglws yateklkslg ylcglvsekg pnsedlnrtv
      421 dllaglgaer petantaqsp ykklkealss veafekhyld lshatiemyt sigrirsakf
      481 vgkdlaefym rkkapqkaei ylqgalknyl aegwalpith trkqlaecqk hlgqienylq
      541 tssllasdhh lteeerkhfc qeildfasqp sdspghkivl pmhsfaqlrd lhfdpsnavv
      601 hvggvlcvei tmysqmpvpv hveqivvnvh fsieknsyrk taewltkhkt sngiinfppe
      661 tapfpvsqns lpalelyemf erspsdnsln ttgiicrnvh mllrrqesss slempsgval
      721 eegahvlrcs hvtlepganq itfrtqakep gtytlrqlca svgsvwfvlp hiypivqydv
      781 ysqepqlhve pladsllagi pqrvkftvtt ghytikngds lqlsnaeaml ilcqaesrav
      841 vysntreqss eaalriqssd kvtsislpva payhviefel evlslpsapa lggesdmlgm
      901 aephrkhkdk qrtgrcmvtt dhkvsidcpw siystvialt fsvpfrtths llssgtrkyv
      961 qvcvqnlsel dfqlsdsylv dtgdstdlql vplntqsqqp iyskqsvffv welkwteepp
     1021 pslhcrfsvg fspaseeqls islkpytyef kvenfftlyn vkaeifppsg meycrtgslc
     1081 slevlitrls dllevdkdea ltesdehfst klmyevvdns snwavcgksc gvismpvaar
     1141 athrvhmevm plfagylplp dvrlfkylph hsahssqlda dswiendsls vdkhgddqpd
     1201 ssslksrgsv hsacssehkg lpmprlqalp agqvfnsssg tqvlvipsqd dhvlevsvt
//
LOCUS       NP_001349839             302 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin recognition factor in ER-associated degradation protein 1
            isoform C [Homo sapiens].
ACCESSION   NP_001349839 XP_011528663
VERSION     NP_001349839.1
DBSOURCE    REFSEQ: accession NM_001362910.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Bekkari,H., Benmakhlouf,Y., Nourouti,N.G., Barakat,A. and
            Mechita,M.B.
  TITLE     Study of Clinical Characteristics of Intellectual Disability in
            Morocco
  JOURNAL   Innov Clin Neurosci 21 (7-9), 10-14 (2024)
   PUBMED   39329031
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Nguyen,T.Q., My Le,L.T., Kim,D.H., Ko,K.S., Lee,H.T., Kim
            Nguyen,Y.T., Kim,H.S., Han,B.W., Kang,W. and Yang,J.K.
  TITLE     Structural basis for the interaction between human Npl4 and
            Npl4-binding motif of human Ufd1
  JOURNAL   Structure 30 (11), 1530-1537 (2022)
   PUBMED   36087575
  REMARK    GeneRIF: Structural basis for the interaction between human Npl4
            and Npl4-binding motif of human Ufd1.
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Fujisawa,R., Polo Rivera,C. and Labib,K.P.M.
  TITLE     Multiple UBX proteins reduce the ubiquitin threshold of the
            mammalian p97-UFD1-NPL4 unfoldase
  JOURNAL   Elife 11, e76763 (2022)
   PUBMED   35920641
  REMARK    GeneRIF: Multiple UBX proteins reduce the ubiquitin threshold of
            the mammalian p97-UFD1-NPL4 unfoldase.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Amati,F., Condo,I., Conti,E., Sangiuolo,F., Dallapiccola,B.,
            Testi,R. and Novelli,G.
  TITLE     Analysis of intracellular distribution and apoptosis involvement of
            the Ufd1l gene product by over-expression studies
  JOURNAL   Cell Biochem Funct 21 (3), 263-267 (2003)
   PUBMED   12910480
  REMARK    GeneRIF: Ufd1l is localized around the nucleus and it does not
            interfere with Fas-and ceramide-mediated apoptosis.
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Amati,F., Conti,E., Botta,A., Amicucci,P., Dallapiccola,B. and
            Novelli,G.
  TITLE     Functional characterization of the 5' flanking region of human
            ubiquitin fusion degradation 1 like gene (UFD1L)
  JOURNAL   Cell Biochem Funct 20 (2), 163-170 (2002)
   PUBMED   11979512
  REMARK    GeneRIF: a functional analysis of its 5' regulatory region
REFERENCE   7  (residues 1 to 302)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   8  (residues 1 to 302)
  AUTHORS   Yamagishi,H., Garg,V., Matsuoka,R., Thomas,T. and Srivastava,D.
  TITLE     A molecular pathway revealing a genetic basis for human cardiac and
            craniofacial defects
  JOURNAL   Science 283 (5405), 1158-1161 (1999)
   PUBMED   10024240
REFERENCE   9  (residues 1 to 302)
  AUTHORS   Novelli,G., Mari,A., Amati,F., Colosimo,A., Sangiuolo,F.,
            Bengala,M., Conti,E., Ratti,A., Bordoni,R., Pizzuti,A., Baldini,A.,
            Crinelli,R., Pandolfi,F., Magnani,M. and Dallapiccola,B.
  TITLE     Structure and expression of the human ubiquitin fusion-degradation
            gene (UFD1L)
  JOURNAL   Biochim Biophys Acta 1396 (2), 158-162 (1998)
   PUBMED   9540831
REFERENCE   10 (residues 1 to 302)
  AUTHORS   Pizzuti,A., Novelli,G., Ratti,A., Amati,F., Mari,A., Calabrese,G.,
            Nicolis,S., Silani,V., Marino,B., Scarlato,G., Ottolenghi,S. and
            Dallapiccola,B.
  TITLE     UFD1L, a developmentally expressed ubiquitination gene, is deleted
            in CATCH 22 syndrome
  JOURNAL   Hum Mol Genet 6 (2), 259-265 (1997)
   PUBMED   9063746
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000087.2 and AC000068.2.
            
            On May 3, 2018 this sequence version replaced XP_011528663.1.
            
            Summary: The protein encoded by this gene forms a complex with two
            other proteins, nuclear protein localization-4 and
            valosin-containing protein, and this complex is necessary for the
            degradation of ubiquitinated proteins. In addition, this complex
            controls the disassembly of the mitotic spindle and the formation
            of a closed nuclear envelope after mitosis. Mutations in this gene
            have been associated with Catch 22 syndrome as well as cardiac and
            craniofacial defects. Alternative splicing results in multiple
            transcript variants encoding different isoforms. A related
            pseudogene has been identified on chromosome 18. [provided by
            RefSeq, Jun 2009].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 5' region and is predicted to use a downstream start codon
            compared to variant 1. The encoded isoform (C) has a shorter
            N-terminus compared to isoform A.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.684417.1,
                                           SRR5189658.27447.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..302
                     /product="ubiquitin recognition factor in ER-associated
                     degradation protein 1 isoform C"
                     /note="UB fusion protein 1; ubiquitin fusion degradation
                     protein 1 homolog; ubiquitin fusion degradation 1 like;
                     ubiquitin recognition factor in ER-associated degradation
                     protein 1"
                     /calculated_mol_wt=33743
     Region          14..187
                     /region_name="UFD1"
                     /note="Ubiquitin fusion degradation protein UFD1;
                     pfam03152"
                     /db_xref="CDD:460828"
     CDS             1..302
                     /gene="UFD1"
                     /gene_synonym="UFD1L"
                     /coded_by="NM_001362910.2:382..1290"
                     /note="isoform C is encoded by transcript variant 3"
                     /db_xref="GeneID:7353"
                     /db_xref="HGNC:HGNC:12520"
                     /db_xref="MIM:601754"
ORIGIN      
        1 mfdhpiprvf qnrfstqyrc fsvsmlagpn drsdvekggk iimppsaldq lsrlnitypm
       61 lfkltnknsd rmthcgvlef vadegicylp hwmmqnllle egglvqvesv nlqvatyskf
      121 qpqspdfldi tnpkavlena lrnfaclttg dviainynek iyelrvmetk pdkavsiiec
      181 dmnvdfdapl gykeperqvq heestegead hsgyagelgf rafsgsgnrl dgkkkgveps
      241 pspikpgdik rgipnyefkl gkitfirnsr plvkkveede aggrfvafsg egqslrkkgr
      301 kp
//
LOCUS       NP_001290357             478 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 3
            [Homo sapiens].
ACCESSION   NP_001290357 XP_005271347
VERSION     NP_001290357.1
DBSOURCE    REFSEQ: accession NM_001303428.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX537388.1, AK302049.1 and
            CR749649.1.
            
            On Jan 1, 2015 this sequence version replaced XP_005271347.1.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (4) contains an alternate exon and
            uses an alternate splice site in the 5' coding region. These
            differences cause translation initiation at an upstream start codon
            compared to variant 1. The encoded isoform (3) has a longer
            N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537388.1, SRR14038191.1700571.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..478
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 3"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=55962
     Region          76..184
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(89,107,129,131)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(130,157)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          189..349
                     /region_name="iSH2_PIK3R3"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunit 3, PIK3R3,
                     also called p55gamma; cd12925"
                     /db_xref="CDD:214018"
     Site            order(212,219,230..232,234..236,238..239,242..243,
                     245..246,249..250,253,269,272..273,276,280,283,309..310,
                     313,316)
                     /site_type="other"
                     /note="putative heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:214018"
     Region          368..471
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(382,400,402..403,420,422)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(421,432,454,457,461)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..478
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_001303428.1:51..1487"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 mpavpppgav gwrlsgamyn tvwsmdrdda dwrevmmpys telifyiemd ppalppkppk
       61 pmtsavpngm kdssvslqda ewywgdisre evndklrdmp dgtflvrdas tkmqgdytlt
      121 lrkggnnkli kiyhrdgkyg fsdpltfnsv velinhyhhe slaqynpkld vklmypvsry
      181 qqdqlvkedn idavgkklqe yhsqyqeksk eydrlyeeyt rtsqeiqmkr taieafneti
      241 kifeeqchtq eqhskeyier frregnekei erimmnydkl ksrlgeihds kmrleqdlkn
      301 qaldnreidk kmnsikpdli qlrkirdqhl vwlnhkgvrq krlnvwlgik nedadenyfi
      361 needenlphy dektwfvedi nrvqaedlly gkpdgaflir esskkgcyac svvadgevkh
      421 cviystargy gfaepynlys slkelvlhyq qtslvqhnds lnvrlaypvh aqmpslcr
//
LOCUS       NP_001289979             281 aa            linear   PRI 20-NOV-2025
DEFINITION  microtubule-associated protein RP/EB family member 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_001289979
VERSION     NP_001289979.1
DBSOURCE    REFSEQ: accession NM_001303050.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zhang,Y., Liu,F., Zheng,J., Jiang,K., Ai,H., Liu,L. and Mao,D.
  TITLE     MAPRE3 as an epigenetic target of EZH2 restricts ovarian cancer
            proliferation in vitro and in vivo
  JOURNAL   Exp Cell Res 435 (1), 113913 (2024)
   PUBMED   38199479
  REMARK    GeneRIF: MAPRE3 as an epigenetic target of EZH2 restricts ovarian
            cancer proliferation in vitro and in vivo.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Bu,W. and Su,L.K.
  TITLE     Characterization of functional domains of human EB1 family proteins
  JOURNAL   J Biol Chem 278 (50), 49721-49731 (2003)
   PUBMED   14514668
  REMARK    GeneRIF: neither APC nor p150glued binding domain is necessary for
            EB1 or EBF3 to induce microtubule bundling
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Su,L.K. and Qi,Y.
  TITLE     Characterization of human MAPRE genes and their proteins
  JOURNAL   Genomics 71 (2), 142-149 (2001)
   PUBMED   11161807
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Nakagawa,H., Koyama,K., Murata,Y., Morito,M., Akiyama,T. and
            Nakamura,Y.
  TITLE     EB3, a novel member of the EB1 family preferentially expressed in
            the central nervous system, binds to a CNS-specific APC homologue
  JOURNAL   Oncogene 19 (2), 210-216 (2000)
   PUBMED   10644998
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Juwana,J.P., Henderikx,P., Mischo,A., Wadle,A., Fadle,N.,
            Gerlach,K., Arends,J.W., Hoogenboom,H., Pfreundschuh,M. and
            Renner,C.
  TITLE     EB/RP gene family encodes tubulin binding proteins
  JOURNAL   Int J Cancer 81 (2), 275-284 (1999)
   PUBMED   10188731
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Renner,C., Pfitzenmeier,J.P., Gerlach,K., Held,G., Ohnesorge,S.,
            Sahin,U., Bauer,S. and Pfreundschuh,M.
  TITLE     RP1, a new member of the adenomatous polyposis coli-binding
            EB1-like gene family, is differentially expressed in activated T
            cells
  JOURNAL   J Immunol 159 (3), 1276-1283 (1997)
   PUBMED   9233623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY011071.1, BM560331.1,
            AC013472.8, BC011557.1 and AB025186.1.
            
            Summary:  The protein encoded by this gene is a member of the RP/EB
            family of genes.  The protein localizes to the cytoplasmic
            microtubule network and binds APCL, a homolog of the adenomatous
            polyposis coli tumor suppressor gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.274947.1,
                                           SRR5189667.29465.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..281
                     /product="microtubule-associated protein RP/EB family
                     member 3 isoform 1"
                     /note="APC binding protein; end-binding protein 3; EB1
                     protein family member 3"
                     /calculated_mol_wt=31851
     Region          16..279
                     /region_name="BIM1"
                     /note="Microtubule-binding protein involved in cell cycle
                     control [Cell division and chromosome partitioning /
                     Cytoskeleton]; COG5217"
                     /db_xref="CDD:227542"
     Region          157..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PER3; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          217..281
                     /region_name="DCTN1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          217..260
                     /region_name="APC-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          261..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     CDS             1..281
                     /gene="MAPRE3"
                     /gene_synonym="EB3; EBF3; EBF3-S; RP3"
                     /coded_by="NM_001303050.2:239..1084"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1731.1"
                     /db_xref="GeneID:22924"
                     /db_xref="HGNC:HGNC:6892"
                     /db_xref="MIM:605788"
ORIGIN      
        1 mavnvystsv tsenlsrhdm lawvndslhl nytkieqlcs gaaycqfmdm lfpgcvhlrk
       61 vkfqaklehe yihnfkvlqa afkkmgvdki ipveklvkgk fqdnfefiqw fkkffdanyd
      121 gkdynpllar qgqdvapppn pgdqifnksk kligtavpqr tsptgpknmq tsgrlsnvap
      181 pcilrknpps arngghetda qilelnqqlv dlkltvdgle kerdfyfskl rdielicqeh
      241 esenspvisg iigilyatee gfappeddei eehqqedqde y
//
LOCUS       NP_001158887             274 aa            linear   PRI 20-NOV-2025
DEFINITION  L-lactate dehydrogenase A chain isoform 4 [Homo sapiens].
ACCESSION   NP_001158887
VERSION     NP_001158887.1
DBSOURCE    REFSEQ: accession NM_001165415.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 274)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 274)
  AUTHORS   Hu,C., Zhang,W., Jia,Y., Zhao,J., Chen,Q., Hao,C. and Yu,Y.
  TITLE     USP4 promotes PTC progression by stabilizing LDHA and activating
            the MAPK and AKT signaling pathway
  JOURNAL   Aging (Albany NY) 16 (19), 12850-12865 (2024)
   PUBMED   39393052
  REMARK    GeneRIF: USP4 promotes PTC progression by stabilizing LDHA and
            activating the MAPK and AKT signaling pathway.
REFERENCE   3  (residues 1 to 274)
  AUTHORS   Zhuo,Z., Wang,Y. and Xu,Y.
  TITLE     Advancements in research on lactate dehydrogenase A in urinary
            system tumors
  JOURNAL   BMC Urol 24 (1), 187 (2024)
   PUBMED   39215270
  REMARK    GeneRIF: Advancements in research on lactate dehydrogenase A in
            urinary system tumors.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 274)
  AUTHORS   Vats,P., Singh,J., Srivastava,S.K., Kumar,A. and Nema,R.
  TITLE     LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by Sponging
            miR-383-5p to Trigger the LDHA Axis
  JOURNAL   Asian Pac J Cancer Prev 25 (8), 2929-2944 (2024)
   PUBMED   39205592
  REMARK    GeneRIF: LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by
            Sponging miR-383-5p to Trigger the LDHA Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 274)
  AUTHORS   Papulino,C., Chianese,U., Ali,A., Favale,G., Tuccillo,C.,
            Ciardiello,F., Di Mauro,A., Mignogna,C., Ferrara,G., Budillon,A.,
            Megchelenbrink,W.L., Del Gaudio,N., Conte,M., Merciai,F.,
            Campiglia,P., Altucci,L., Carafa,V., Sommella,E. and Benedetti,R.
  TITLE     Inverse FASN and LDHA correlation drives metabolic resistance in
            breast cancer
  JOURNAL   J Transl Med 22 (1), 676 (2024)
   PUBMED   39044184
  REMARK    GeneRIF: Inverse FASN and LDHA correlation drives metabolic
            resistance in breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 274)
  AUTHORS   Miyajima,H., Shimizu,T. and Kaneko,E.
  TITLE     [Gene expression in lactate dehydrogenase-A subunit deficiency]
  JOURNAL   Rinsho Shinkeigaku 32 (10), 1087-1092 (1992)
   PUBMED   1297552
REFERENCE   7  (residues 1 to 274)
  AUTHORS   Sudo,K., Maekawa,M., Shioya,M., Ikeda,K., Takahashi,N., Isogai,Y.,
            Li,S.S., Kanno,T., Machida,K. and Toriumi,J.
  TITLE     Molecular analysis of genetic mutation in electrophoretic variant
            of human lactate dehydrogenase-A(M) subunit
  JOURNAL   Biochem Int 27 (6), 1051-1057 (1992)
   PUBMED   1445373
REFERENCE   8  (residues 1 to 274)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Genotypic analysis of families with lactate dehydrogenase A (M)
            deficiency by selective DNA amplification
  JOURNAL   Hum Genet 88 (1), 34-38 (1991)
   PUBMED   1959923
REFERENCE   9  (residues 1 to 274)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Analysis of genetic mutations in human lactate dehydrogenase-A(M)
            deficiency using DNA conformation polymorphism in combination with
            polyacrylamide gradient gel and silver staining
  JOURNAL   Biochem Biophys Res Commun 180 (2), 1083-1090 (1991)
   PUBMED   1953713
REFERENCE   10 (residues 1 to 274)
  AUTHORS   LeVan,K.M. and Goldberg,E.
  TITLE     Properties of human testis-specific lactate dehydrogenase expressed
            from Escherichia coli
  JOURNAL   Biochem J 273 (Pt 3) (Pt 3), 587-592 (1991)
   PUBMED   1996957
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK130587.1, AK307477.1,
            AC084117.6 and BM995301.1.
            
            Summary: This gene encodes the A subunit of lactate dehydrogenase
            enzyme which catalyzes the reversible conversion of pyruvate to
            lactate with the concomitant oxidation of NADH to NAD in anaerobic
            glycolysis. The protein is found predominantly in skeletal muscle
            and belongs to the lactate dehydrogenase family. Mutations in this
            gene have been linked to exertional myoglobinuria. The human genome
            contains several non-transcribed pseudogenes of this gene.
            [provided by RefSeq, Sep 2023].
            
            Transcript Variant: This variant (4) differs in the 3' UTR and has
            multiple differences in the 3' coding region, compared to variant
            1, one of which results in a frameshift. The resulting isoform (4)
            lacks a segment of the LDH domain and has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130587.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..274
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..274
                     /product="L-lactate dehydrogenase A chain isoform 4"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase A chain; lactate
                     dehydrogenase M; LDH muscle subunit; renal carcinoma
                     antigen NY-REN-59; proliferation-inducing gene 19; LDH-A;
                     LDH-M; cell proliferation-inducing gene 19 protein;
                     epididymis secretory sperm binding protein Li 133P"
                     /calculated_mol_wt=29926
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P00338.2)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Region          19..>229
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(29..31,52,54,57,95..99,136,138,161,165,193)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06151; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     CDS             1..274
                     /gene="LDHA"
                     /gene_synonym="GSD11; HEL-S-133P; LDHM; PIG19"
                     /coded_by="NM_001165415.2:99..923"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53610.1"
                     /db_xref="GeneID:3939"
                     /db_xref="HGNC:HGNC:6535"
                     /db_xref="MIM:150000"
ORIGIN      
        1 matlkdqliy nllkeeqtpq nkitvvgvga vgmacaisil mkdladelal vdviedklkg
       61 emmdlqhgsl flrtpkivsg kdynvtansk lviitagarq qegesrlnlv qrnvnifkfi
      121 ipnvvkyspn ckllivsnpv diltyvawki sgfpknrvig sgcnldsarf rylmgerlgv
      181 hplschgwvl gehgdssvpv wsgmnvagvs lktlhpdlgt dkdkeqwkec rytlgdpkga
      241 ailkssdvis fhclgynril gggcaccpfy licd
//
LOCUS       NP_001138356             376 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 7 [Homo sapiens].
ACCESSION   NP_001138356
VERSION     NP_001138356.1
DBSOURCE    REFSEQ: accession NM_001144884.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Yu,W., Gui,S., Xie,J., Peng,L., Xiao,J., Luo,H., Tao,Z. and
            Cheng,Z.
  TITLE     Investigation of cuproptosis regulator-mediated modification
            patterns and SLC30A7 function in GBM
  JOURNAL   Aging (Albany NY) 16 (4), 3554-3582 (2024)
   PUBMED   38393693
  REMARK    GeneRIF: Investigation of cuproptosis regulator-mediated
            modification patterns and SLC30A7 function in GBM.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Bui,H.B., Watanabe,S., Nomura,N., Liu,K., Uemura,T., Inoue,M.,
            Tsutsumi,A., Fujita,H., Kinoshita,K., Kato,Y., Iwata,S., Kikkawa,M.
            and Inaba,K.
  TITLE     Cryo-EM structures of human zinc transporter ZnT7 reveal the
            mechanism of Zn2+ uptake into the Golgi apparatus
  JOURNAL   Nat Commun 14 (1), 4770 (2023)
   PUBMED   37553324
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Huang,L., Yang,Z., Kirschke,C.P., Prouteau,C., Copin,M.C.,
            Bonneau,D., Pellier,I., Coutant,R., Miot,C. and Ziegler,A.
  TITLE     Identification of novel compound heterozygous variants in the
            SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure
  JOURNAL   Hum Mol Genet 32 (12), 2016-2031 (2023)
   PUBMED   36821639
  REMARK    GeneRIF: Identification of novel compound heterozygous variants in
            the SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Penon-Portmann,M., Eldomery,M.K., Potocki,L., Marafi,D.,
            Posey,J.E., Coban-Akdemir,Z., Harel,T., Grochowski,C.M., Loucks,H.,
            Devine,W.P., Van Ziffle,J., Doherty,D., Lupski,J.R. and Shieh,J.T.
  TITLE     De novo heterozygous variants in SLC30A7 are a candidate cause for
            Joubert syndrome
  JOURNAL   Am J Med Genet A 188 (8), 2360-2366 (2022)
   PUBMED   35751429
  REMARK    GeneRIF: De novo heterozygous variants in SLC30A7 are a candidate
            cause for Joubert syndrome.
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Li,W., Yang,S., Chen,G. and He,S.
  TITLE     MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in diabetic
            retinopathy
  JOURNAL   Hum Exp Toxicol 41, 9603271221099589 (2022)
   PUBMED   35607288
  REMARK    GeneRIF: MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in
            diabetic retinopathy.
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Matsuura,W., Kohda,A.,
            Okumura,K., Nagao,M., Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Zinc transporters, ZnT5 and ZnT7, are required for the activation
            of alkaline phosphatases, zinc-requiring enzymes that are
            glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
  JOURNAL   J Biol Chem 280 (1), 637-643 (2005)
   PUBMED   15525635
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Devergnas,S., Chimienti,F., Naud,N., Pennequin,A., Coquerel,Y.,
            Chantegrel,J., Favier,A. and Seve,M.
  TITLE     Differential regulation of zinc efflux transporters ZnT-1, ZnT-5
            and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
  JOURNAL   Biochem Pharmacol 68 (4), 699-709 (2004)
   PUBMED   15276077
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Kirschke,C.P. and Huang,L.
  TITLE     ZnT7, a novel mammalian zinc transporter, accumulates zinc in the
            Golgi apparatus
  JOURNAL   J Biol Chem 278 (6), 4096-4102 (2003)
   PUBMED   12446736
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX537375.1, AL732465.6 and BX648884.1.
            
            Summary: Zinc functions as a cofactor for numerous enzymes, nuclear
            factors, and hormones and as an intra- and intercellular signal
            ion. Members of the zinc transporter (ZNT)/SLC30 subfamily of the
            cation diffusion facilitator family, such as SLC30A7, permit
            cellular efflux of zinc (Seve et al., 2004 [PubMed
            15154973]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) lacks a segment in the 3' UTR,
            as compared to variant 1. Both variants 1 and 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR936806.1, BX537375.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..376
                     /product="zinc transporter 7"
                     /note="zinc transporter like 2; zinc transporter ZnT-7;
                     znt-like transporter 2; solute carrier family 30 (zinc
                     transporter), member 7"
                     /calculated_mol_wt=41495
     Region          31..354
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          161..218
                     /region_name="His-rich loop"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          <182..219
                     /region_name="ureE"
                     /note="urease accessory protein UreE; Provisional;
                     PRK13263"
                     /db_xref="CDD:237323"
     Region          194..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     CDS             1..376
                     /gene="SLC30A7"
                     /gene_synonym="ZHS; ZnT-7; ZNT7; ZnTL2"
                     /coded_by="NM_001144884.2:174..1304"
                     /db_xref="CCDS:CCDS776.1"
                     /db_xref="GeneID:148867"
                     /db_xref="HGNC:HGNC:19306"
                     /db_xref="MIM:611149"
ORIGIN      
        1 mlplsikdde ykppkfnlfg kisgwfrsil sdktsrnlff flclnlsfaf vellygiwsn
       61 clglisdsfh mffdstaila glaasviskw rdndafsygy vraevlagfv nglfliftaf
      121 fifsegvera lappdvhher lllvsilgfv vnligifvfk hgghghshgs ghghshslfn
      181 galdqahghv dhchshevkh gaahshdhah ghghfhshdg pslkettgps rqilqgvflh
      241 iladtlgsig viasaimmqn fglmiadpic siliailivv svipllresv gilmqrtppl
      301 lenslpqcyq rvqqlqgvys lqeqhfwtlc sdvyvgtlkl ivapdadarw ilsqthnift
      361 qagvrqlyvq idfaam
//
LOCUS       NP_149162               1418 aa            linear   PRI 20-NOV-2025
DEFINITION  collagen alpha-1(II) chain isoform 2 precursor [Homo sapiens].
ACCESSION   NP_149162
VERSION     NP_149162.2
DBSOURCE    REFSEQ: accession NM_033150.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1418)
  AUTHORS   Viakhireva,I., Bychkov,I., Markova,T., Shatokhina,O.,
            Karandasheva,K., Udalova,V., Bekhtereva,Y., Ryzhkova,O. and
            Skoblov,M.
  TITLE     The molecular complexity of COL2A1 splicing variants and their
            significance in phenotype severity
  JOURNAL   Bone 181, 117013 (2024)
   PUBMED   38246255
  REMARK    GeneRIF: The molecular complexity of COL2A1 splicing variants and
            their significance in phenotype severity.
REFERENCE   2  (residues 1 to 1418)
  AUTHORS   Ma,J., Zhang,Y., Ding,X., Liang,Z., Yang,C., Deng,Z., He,H.,
            Guan,Z., Zeng,C., Lin,Y. and Luo,X.
  TITLE     Co-occurrence of Spondyloepiphyseal Dysplasia and X-Linked
            Hypophosphatemia in a Three-Generation Chinese Family
  JOURNAL   Calcif Tissue Int 113 (3), 266-275 (2023)
   PUBMED   37278761
  REMARK    GeneRIF: Co-occurrence of Spondyloepiphyseal Dysplasia and X-Linked
            Hypophosphatemia in a Three-Generation Chinese Family.
REFERENCE   3  (residues 1 to 1418)
  AUTHORS   Jacobson,A., Besirli,C.G. and Bohnsack,B.L.
  TITLE     Characteristics of a Three-Generation Family with Stickler Syndrome
            Type I Carrying Two Different COL2A1 Mutations
  JOURNAL   Genes (Basel) 14 (4), 847 (2023)
   PUBMED   37107605
  REMARK    GeneRIF: Characteristics of a Three-Generation Family with Stickler
            Syndrome Type I Carrying Two Different COL2A1 Mutations.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1418)
  AUTHORS   Tuysuz,B., Kasap,B., Saritas,M., Alkaya,D.U., Bozlak,S., Kiykim,A.,
            Durmaz,A., Yildirim,T., Akpinar,E., Apak,H. and Vural,M.
  TITLE     Natural history and genetic spectrum of the Turkish metaphyseal
            dysplasia cohort, including rare types caused by biallelic COL10A1,
            COL2A1, and LBR variants
  JOURNAL   Bone 167, 116614 (2023)
   PUBMED   36400164
  REMARK    GeneRIF: Natural history and genetic spectrum of the Turkish
            metaphyseal dysplasia cohort, including rare types caused by
            biallelic COL10A1, COL2A1, and LBR variants.
REFERENCE   5  (residues 1 to 1418)
  AUTHORS   England,J. and Campeau,P.M.
  TITLE     Spondylometaphyseal Dysplasia, Corner Fracture Type
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32200603
REFERENCE   6  (residues 1 to 1418)
  AUTHORS   Gregersen,P.A. and Savarirayan,R.
  TITLE     Type II Collagen Disorders Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31021589
REFERENCE   7  (residues 1 to 1418)
  AUTHORS   Mortier,G.
  TITLE     Stickler Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301479
REFERENCE   8  (residues 1 to 1418)
  AUTHORS   Bogaert,R., Tiller,G.E., Weis,M.A., Gruber,H.E., Rimoin,D.L.,
            Cohn,D.H. and Eyre,D.R.
  TITLE     An amino acid substitution (Gly853-->Glu) in the collagen alpha
            1(II) chain produces hypochondrogenesis
  JOURNAL   J Biol Chem 267 (31), 22522-22526 (1992)
   PUBMED   1429602
REFERENCE   9  (residues 1 to 1418)
  AUTHORS   Kirsch,T. and Pfaffle,M.
  TITLE     Selective binding of anchorin CII (annexin V) to type II and X
            collagen and to chondrocalcin (C-propeptide of type II collagen).
            Implications for anchoring function between matrix vesicles and
            matrix proteins
  JOURNAL   FEBS Lett 310 (2), 143-147 (1992)
   PUBMED   1397263
REFERENCE   10 (residues 1 to 1418)
  AUTHORS   Horton,W.A., Machado,M.A., Ellard,J., Campbell,D., Bartley,J.,
            Ramirez,F., Vitale,E. and Lee,B.
  TITLE     Characterization of a type II collagen gene (COL2A1) mutation
            identified in cultured chondrocytes from human hypochondrogenesis
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4583-4587 (1992)
   PUBMED   1374906
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004801.2.
            
            On Aug 2, 2006 this sequence version replaced NP_149162.1.
            
            Summary: This gene encodes the alpha-1 chain of type II collagen, a
            fibrillar collagen found in cartilage and the vitreous humor of the
            eye. Mutations in this gene are associated with achondrogenesis,
            chondrodysplasia, early onset familial osteoarthritis, SED
            congenita, Langer-Saldino achondrogenesis, Kniest dysplasia,
            Stickler syndrome type I, and spondyloepimetaphyseal dysplasia
            Strudwick type. In addition, defects in processing chondrocalcin, a
            calcium binding protein that is the C-propeptide of this collagen
            molecule, are also associated with chondrodysplasia. There are two
            transcripts identified for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in a
            shorter protein. The resulting protein (isoform 2) lacks the von
            Willebrand factor type C (VWC) domain, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X16468.1, SRR14038194.2122564.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..1418
                     /product="collagen alpha-1(II) chain isoform 2 precursor"
                     /note="collagen II, alpha-1 polypeptide; cartilage
                     collagen; chondrocalcin; collagen alpha-1(II) chain;
                     alpha-1 type II collagen; arthroophthalmopathy,
                     progressive (Stickler syndrome); collagen, type II, alpha
                     1"
                     /calculated_mol_wt=131757
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2650
     mat_peptide     26..1418
                     /product="collagen alpha-1(II) chain isoform 2"
                     /calculated_mol_wt=131757
     Region          <144..>357
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <305..>568
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <581..>808
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <732..>942
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <870..>1065
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1017..>1126
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1182..1417
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; pfam01410"
                     /db_xref="CDD:460199"
     CDS             1..1418
                     /gene="COL2A1"
                     /gene_synonym="ACG2; ANFH; ANFH1; AOM; COL11A3; EDMMD;
                     LCPD; OSCDP; PLSDT; SEDC; SEDSTN; SEMDSTWK; SMDALG; STL1;
                     VPED"
                     /coded_by="NM_033150.3:156..4412"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS8759.1"
                     /db_xref="GeneID:1280"
                     /db_xref="HGNC:HGNC:2200"
                     /db_xref="MIM:120140"
ORIGIN      
        1 mirlgapqtl vlltllvaav lrcqgqdvrq pgpkgqkgep gdikdivgpk gppgpqgpag
       61 eqgprgdrgd kgekgapgpr grdgepgtpg npgppgppgp pgppglggnf aaqmaggfde
      121 kaggaqlgvm qgpmgpmgpr gppgpagapg pqgfqgnpge pgepgvsgpm gprgppgppg
      181 kpgddgeagk pgkagergpp gpqgargfpg tpglpgvkgh rgypgldgak geagapgvkg
      241 esgspgengs pgpmgprglp gergrtgpag aagargndgq pgpagppgpv gpaggpgfpg
      301 apgakgeagp tgargpegaq gprgepgtpg spgpagasgn pgtdgipgak gsagapgiag
      361 apgfpgprgp pgpqgatgpl gpkgqtgepg iagfkgeqgp kgepgpagpq gapgpageeg
      421 krgargepgg vgpigppger gapgnrgfpg qdglagpkga pgergpsgla gpkgangdpg
      481 rpgepglpga rgltgrpgda gpqgkvgpsg apgedgrpgp pgpqgargqp gvmgfpgpkg
      541 angepgkage kglpgapglr glpgkdgetg aagppgpagp agergeqgap gpsgfqglpg
      601 ppgppgeggk pgdqgvpgea gapglvgprg ergfpgergs pgaqglqgpr glpgtpgtdg
      661 pkgasgpagp pgaqgppglq gmpgergaag iagpkgdrgd vgekgpegap gkdggrgltg
      721 pigppgpaga ngekgevgpp gpagsagarg apgergetgp pgpagfagpp gadgqpgakg
      781 eqgeagqkgd agapgpqgps gapgpqgptg vtgpkgarga qgppgatgfp gaagrvgppg
      841 sngnpgppgp pgpsgkdgpk gargdsgppg ragepglqgp agppgekgep gddgpsgaeg
      901 ppgpqglagq rgivglpgqr gergfpglpg psgepgkqga pgasgdrgpp gpvgppgltg
      961 pagepgregs pgadgppgrd gaagvkgdrg etgavgapga pgppgspgpa gptgkqgdrg
     1021 eagaqgpmgp sgpagargiq gpqgprgdkg eagepgergl kghrgftglq glpgppgpsg
     1081 dqgasgpagp sgprgppgpv gpsgkdgang ipgpigppgp rgrsgetgpa gppgnpgppg
     1141 ppgppgpgid msafaglgpr ekgpdplqym radqaagglr qhdaevdatl kslnnqiesi
     1201 rspegsrknp artcrdlklc hpewksgdyw idpnqgctld amkvfcnmet getcvypnpa
     1261 nvpkknwwss kskekkhiwf getinggfhf sygddnlapn tanvqmtflr llstegsqni
     1321 tyhcknsiay ldeaagnlkk alliqgsndv eiraegnsrf tytalkdgct khtgkwgktv
     1381 ieyrsqktsr lpiidiapmd iggpeqefgv digpvcfl
//
LOCUS       NP_064617                264 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome assembly chaperone 2 isoform 1 [Homo sapiens].
ACCESSION   NP_064617
VERSION     NP_064617.2
DBSOURCE    REFSEQ: accession NM_020232.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Todd,J.A., Walker,N.M., Cooper,J.D., Smyth,D.J., Downes,K.,
            Plagnol,V., Bailey,R., Nejentsev,S., Field,S.F., Payne,F.,
            Lowe,C.E., Szeszko,J.S., Hafler,J.P., Zeitels,L., Yang,J.H.,
            Vella,A., Nutland,S., Stevens,H.E., Schuilenburg,H., Coleman,G.,
            Maisuria,M., Meadows,W., Smink,L.J., Healy,B., Burren,O.S.,
            Lam,A.A., Ovington,N.R., Allen,J., Adlem,E., Leung,H.T.,
            Wallace,C., Howson,J.M., Guja,C., Ionescu-Tirgoviste,C.,
            Simmonds,M.J., Heward,J.M., Gough,S.C., Dunger,D.B., Wicker,L.S.
            and Clayton,D.G.
  CONSRTM   Genetics of Type 1 Diabetes in Finland; Wellcome Trust Case Control
            Consortium
  TITLE     Robust associations of four new chromosome regions from genome-wide
            analyses of type 1 diabetes
  JOURNAL   Nat Genet 39 (7), 857-864 (2007)
   PUBMED   17554260
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Hirano,Y., Hayashi,H., Iemura,S., Hendil,K.B., Niwa,S.,
            Kishimoto,T., Kasahara,M., Natsume,T., Tanaka,K. and Murata,S.
  TITLE     Cooperation of multiple chaperones required for the assembly of
            mammalian 20S proteasomes
  JOURNAL   Mol Cell 24 (6), 977-984 (2006)
   PUBMED   17189198
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Hirano,Y., Hendil,K.B., Yashiroda,H., Iemura,S., Nagane,R.,
            Hioki,Y., Natsume,T., Tanaka,K. and Murata,S.
  TITLE     A heterodimeric complex that promotes the assembly of mammalian 20S
            proteasomes
  JOURNAL   Nature 437 (7063), 1381-1385 (2005)
   PUBMED   16251969
  REMARK    GeneRIF: two chaperones, designated proteasome assembling
            chaperone-1 (PAC1) and PAC2, form a heterodimer and are involved in
            the maturation of mammalian 20S proteasomes
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Bahar,R., O-Wang,J., Kawamura,K., Seimiya,M., Wang,Y., Hatano,M.,
            Okada,S., Tokuhisa,T., Watanabe,T. and Tagawa,M.
  TITLE     Growth retardation, polyploidy, and multinucleation induced by
            Clast3, a novel cell cycle-regulated protein
  JOURNAL   J Biol Chem 277 (42), 40012-40019 (2002)
   PUBMED   12147697
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Wang,Z.X., Hu,G.F., Wang,H.Y. and Wu,M.C.
  TITLE     Expression of liver cancer associated gene HCCA3
  JOURNAL   World J Gastroenterol 7 (6), 821-825 (2001)
   PUBMED   11854909
  REMARK    GeneRIF: A novel full-length cDNA was cloned and differentiated,
            which was highly expressed in liver cancer tissues. (HCCA3)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF668035.1, AK057005.1 and BC013356.2.
            
            On Sep 5, 2002 this sequence version replaced NP_064617.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.538402.1,
                                           SRR5189655.8384.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317615.11/ ENSP00000325919.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..264
                     /product="proteasome assembly chaperone 2 isoform 1"
                     /note="hepatocellular carcinoma susceptibility protein;
                     CD40 ligand-activated specific transcript 3; likely
                     ortholog of mouse CD40 ligand-activated specific
                     transcript 3 (Clast3); HDCMC29P; HSPC260; x 003 protein;
                     proteasome assembling chaperone 2; PAC-2; hepatocellular
                     carcinoma-susceptibility protein 3; proteasome (prosome,
                     macropain) assembly chaperone 2; tumor necrosis factor
                     superfamily member 5-induced protein 1"
                     /calculated_mol_wt=29265
     Region          17..>123
                     /region_name="PAC2"
                     /note="PAC2 family; pfam09754"
                     /db_xref="CDD:462883"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q969U7.1)"
     CDS             1..264
                     /gene="PSMG2"
                     /gene_synonym="CLAST3; HCCA3; HsT1707; MDS003; PAC2;
                     PRAAS4; TNFSF5IP1"
                     /coded_by="NM_020232.5:67..861"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11862.1"
                     /db_xref="GeneID:56984"
                     /db_xref="HGNC:HGNC:24929"
                     /db_xref="MIM:609702"
ORIGIN      
        1 mfvpcgesap dlagftllmp avsvgnvgql amdliistln mskigyfytd clvpmvgnnp
       61 yattegnste lsinaevysl psrklvalql rsifikyksk pfcekllswv kssgcarviv
      121 lssshsyqrn dlqlrstpfr ylltpsmqks vqnkikslnw eemeksrcip eiddsefcir
      181 ipgggitktl ydescskeiq mavllkfvse gdnipdalgl veylnewlqi lkplsddptv
      241 sasrwkipss wrllfgsglp palf
//
LOCUS       NP_113640                118 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA guanine-N7 methyltransferase activating subunit [Homo sapiens].
ACCESSION   NP_113640
VERSION     NP_113640.1
DBSOURCE    REFSEQ: accession NM_031452.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Bueren-Calabuig,J.A., G Bage,M., Cowling,V.H. and Pisliakov,A.V.
  TITLE     Mechanism of allosteric activation of human mRNA cap
            methyltransferase (RNMT) by RAM: insights from accelerated
            molecular dynamics simulations
  JOURNAL   Nucleic Acids Res 47 (16), 8675-8692 (2019)
   PUBMED   31329932
  REMARK    GeneRIF: Mechanism of allosteric activation of human RNMT by RAM
            has been reported.
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Dunn,S., Lombardi,O. and Cowling,V.H.
  TITLE     c-Myc co-ordinates mRNA cap methylation and ribosomal RNA
            production
  JOURNAL   Biochem J 474 (3), 377-384 (2017)
   PUBMED   27934633
  REMARK    GeneRIF: RNMT-RAM complex coordinates mRNA processing with ribosome
            production.
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Varshney,D., Petit,A.P., Bueren-Calabuig,J.A., Jansen,C.,
            Fletcher,D.A., Peggie,M., Weidlich,S., Scullion,P., Pisliakov,A.V.
            and Cowling,V.H.
  TITLE     Molecular basis of RNA guanine-7 methyltransferase (RNMT)
            activation by RAM
  JOURNAL   Nucleic Acids Res 44 (21), 10423-10436 (2016)
   PUBMED   27422871
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Gonatopoulos-Pournatzis,T. and Cowling,V.H.
  TITLE     RAM function is dependent on Kapbeta2-mediated nuclear entry
  JOURNAL   Biochem J 457 (3), 473-484 (2014)
   PUBMED   24200467
  REMARK    GeneRIF: Data suggest that RAM/FAM103A1 has three domains:
            N-terminal activation domain (RAD); central RNA-binding domain (NR
            domain); and C-terminal nuclear localization domain (QYP) which
            contains two nuclear localization signal sequences.
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Gonatopoulos-Pournatzis,T., Dunn,S., Bounds,R. and Cowling,V.H.
  TITLE     RAM/Fam103a1 is required for mRNA cap methylation
  JOURNAL   Mol Cell 44 (4), 585-596 (2011)
   PUBMED   22099306
  REMARK    GeneRIF: RAM is an essential component of the core gene expression
            machinery
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022558.9, BC112329.1 and BQ002618.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.138270.1,
                                           SRR1660809.60487.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304191.4/ ENSP00000307181.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.2"
     Protein         1..118
                     /product="RNA guanine-N7 methyltransferase activating
                     subunit"
                     /note="protein FAM103A1; RNMT-activating mini protein;
                     family with sequence similarity 103 member A1; RNMT
                     activating mRNA cap methyltransferase subunit"
                     /calculated_mol_wt=14250
     Region          2..55
                     /region_name="Interaction with RNMT.
                     /evidence=ECO:0000269|PubMed:22099306"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Region          10..87
                     /region_name="RAM"
                     /note="mRNA cap methylation, RNMT-activating mini protein;
                     pfam15320"
                     /db_xref="CDD:464643"
     Region          29..118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Region          36..42
                     /region_name="RNMT-activating domain.
                     /evidence=ECO:0000269|PubMed:27422871"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Region          56..118
                     /region_name="RNA-binding.
                     /evidence=ECO:0000269|PubMed:22099306"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Site            85
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9BTL3.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BTL3.1)"
     CDS             1..118
                     /gene="RAMAC"
                     /gene_synonym="C15orf18; FAM103A1; HsT19360; RAM; RAMMET"
                     /coded_by="NM_031452.4:219..575"
                     /db_xref="CCDS:CCDS10321.1"
                     /db_xref="GeneID:83640"
                     /db_xref="HGNC:HGNC:31022"
                     /db_xref="MIM:614547"
ORIGIN      
        1 mtdtaeavpk feemfasrft endkeyqeyl krppesppiv eewnsraggn qrnrgnrlqd
       61 nrqfrgrdnr wgwpsdnrsn qwhgrswgnn ypqhrqepyy pqqyghygyn qrppygyy
//
LOCUS       NP_001164185             916 aa            linear   PRI 20-NOV-2025
DEFINITION  breast cancer anti-estrogen resistance protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001164185
VERSION     NP_001164185.1
DBSOURCE    REFSEQ: accession NM_001170714.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Delage,L., Lambert,M., Bardel,E., Kundlacz,C., Chartoire,D.,
            Conchon,A., Peugnet,A.L., Gorka,L., Auberger,P., Jacquel,A.,
            Soussain,C., Destaing,O., Delecluse,H.J., Delecluse,S., Merabet,S.,
            Traverse-Glehen,A., Salles,G., Bachy,E., Billaud,M.,
            Ghesquieres,H., Genestier,L., Rouault,J.P. and Sujobert,P.
  TITLE     BTG1 inactivation drives lymphomagenesis and promotes lymphoma
            dissemination through activation of BCAR1
  JOURNAL   Blood 141 (10), 1209-1220 (2023)
   PUBMED   36375119
  REMARK    GeneRIF: BTG1 inactivation drives lymphomagenesis and promotes
            lymphoma dissemination through activation of BCAR1.
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Li,H., Li,L., Qiu,X., Zhang,J. and Hua,Z.
  TITLE     The interaction of CFLAR with p130Cas promotes cell migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (2), 119390 (2023)
   PUBMED   36400248
  REMARK    GeneRIF: The interaction of CFLAR with p130Cas promotes cell
            migration.
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Camacho Leal Mdel,P., Sciortino,M., Tornillo,G., Colombo,S.,
            Defilippi,P. and Cabodi,S.
  TITLE     p130Cas/BCAR1 scaffold protein in tissue homeostasis and
            pathogenesis
  JOURNAL   Gene 562 (1), 1-7 (2015)
   PUBMED   25727852
  REMARK    GeneRIF: BCAR1 has a pivotal role in the regulation of tissue
            homeostasis in pathological conditions such as cancer. (Review)
            Review article
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Nikonova,A.S., Gaponova,A.V., Kudinov,A.E. and Golemis,E.A.
  TITLE     CAS proteins in health and disease: an update
  JOURNAL   IUBMB Life 66 (6), 387-395 (2014)
   PUBMED   24962474
  REMARK    Review article
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Barrett,A., Pellet-Many,C., Zachary,I.C., Evans,I.M. and Frankel,P.
  TITLE     p130Cas: a key signalling node in health and disease
  JOURNAL   Cell Signal 25 (4), 766-777 (2013)
   PUBMED   23277200
  REMARK    Review article
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Brinkman,A., van der Flier,S., Kok,E.M. and Dorssers,L.C.
  TITLE     BCAR1, a human homologue of the adapter protein p130Cas, and
            antiestrogen resistance in breast cancer cells
  JOURNAL   J Natl Cancer Inst 92 (2), 112-120 (2000)
   PUBMED   10639512
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Vuori,K., Hirai,H., Aizawa,S. and Ruoslahti,E.
  TITLE     Introduction of p130cas signaling complex formation upon
            integrin-mediated cell adhesion: a role for Src family kinases
  JOURNAL   Mol Cell Biol 16 (6), 2606-2613 (1996)
   PUBMED   8649368
REFERENCE   9  (residues 1 to 916)
  AUTHORS   Sakai,R., Iwamatsu,A., Hirano,N., Ogawa,S., Tanaka,T., Mano,H.,
            Yazaki,Y. and Hirai,H.
  TITLE     A novel signaling molecule, p130, forms stable complexes in vivo
            with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
  JOURNAL   EMBO J 13 (16), 3748-3756 (1994)
   PUBMED   8070403
REFERENCE   10 (residues 1 to 916)
  AUTHORS   Dorssers,L.C., van Agthoven,T., Dekker,A., van Agthoven,T.L. and
            Kok,E.M.
  TITLE     Induction of antiestrogen resistance in human breast cancer cells
            by random insertional mutagenesis using defective retroviruses:
            identification of bcar-1, a common integration site
  JOURNAL   Mol Endocrinol 7 (7), 870-878 (1993)
   PUBMED   8413311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK293808.1, AK295809.1,
            AB040024.1, BU730553.1, AC009078.6 and BQ016861.1.
            
            Summary: The protein encoded by this gene is a member of the
            Crk-associated substrate (CAS) family of scaffold proteins,
            characterized by the presence of multiple protein-protein
            interaction domains and many serine and tyrosine phosphorylation
            sites. The encoded protein contains a Src-homology 3 (SH3) domain,
            a proline-rich domain, a substrate domain which contains 15 repeat
            of the YxxP consensus phosphorylation motif for Src family kinases,
            a serine-rich domain, and a bipartite Src-binding domain, which can
            bind both SH2 and SH3 domains. This adaptor protein functions in
            multiple cellular pathways, including in cell motility, apoptosis
            and cell cycle control. Dysregulation of this gene can have a wide
            range of effects, affecting different pathways, including cardiac
            development, vascular smooth muscle cells, liver and kidney
            function, endothelial migration, and cancer. [provided by RefSeq,
            Sep 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293808.1, SRR14038197.862048.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..916
                     /product="breast cancer anti-estrogen resistance protein 1
                     isoform 1"
                     /note="Cas scaffolding protein family member 1;
                     Crk-associated substrate p130Cas; breast cancer
                     anti-estrogen resistance protein 1; BCAR1, Cas family
                     scaffolding protein; BCAR1, Cas family scaffold protein"
                     /calculated_mol_wt=97746
     Region          51..117
                     /region_name="SH3_BCAR1"
                     /note="Src homology 3 domain of the CAS (Crk-Associated
                     Substrate) scaffolding protein family member, Breast
                     Cancer Anti-estrogen Resistance 1; cd12001"
                     /db_xref="CDD:212934"
     Site            order(58,60,63,67,88..89,102,104..105)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212934"
     Region          <137..529
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          500..656
                     /region_name="Serine_rich_BCAR1"
                     /note="Serine rich Four helix bundle domain of CAS
                     (Crk-Associated Substrate) scaffolding protein, Breast
                     Cancer Anti-estrogen Resistance 1; a protein interaction
                     module; cd11552"
                     /db_xref="CDD:211406"
     Site            534..540
                     /site_type="other"
                     /note="putative 14-3-3 binding site [polypeptide binding]"
                     /db_xref="CDD:211406"
     Region          700..910
                     /region_name="CAS_C"
                     /note="Crk-Associated Substrate C-terminal domain;
                     pfam12026"
                     /db_xref="CDD:463437"
     CDS             1..916
                     /gene="BCAR1"
                     /gene_synonym="CAS; CAS1; CASS1; CRKAS; P130Cas"
                     /coded_by="NM_001170714.3:285..3035"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54040.1"
                     /db_xref="GeneID:9564"
                     /db_xref="HGNC:HGNC:971"
                     /db_xref="MIM:602941"
ORIGIN      
        1 mpakpflssv llswkvldfs gpgpqgtgqp cscghwaegq ggppepaggp nvlakalydn
       61 vaespdelsf rkgdimtvle qdtqgldgww lcslhgrqgi vpgnrlkilv gmydkkpagp
      121 gpgppatpaq pqpglhapap pasqytpmlp ntyqpqpdsv ylvptpskaq qglyqvpgps
      181 pqfqsppakq tstfskqtph hpfpspatdl yqvppgpggp aqdiyqvpps agmghdiyqv
      241 ppsmdtrswe gtkppakvvv ptrvgqgyvy eaaqpeqdey diprhllapg pqdiydvppv
      301 rgllpsqygq evydtppmav kgpngrdpll evydvppsve kglppsnhha vydvppsvsk
      361 dvpdgpllre etydvppafa kakpfdpart plvlaapppd sppaedvydv pppapdlydv
      421 ppglrrpgpg tlydvprerv lppevadggv vdsgvyavpp paereapaeg krlsasstgs
      481 trssqsassl evagpgrepl elevaveala rlqqgvsatv ahlldlagsa gatgswrsps
      541 epqeplvqdl qaavaavqsa vhellefars avgnaahtsd ralhaklsrq lqkmedvhqt
      601 lvahgqalda grggsgatle dldrlvacsr avpedakqla sflhgnasll frrtkatapg
      661 pegggtlhpn ptdktssiqs rplpsppkft sqdspdgqye nseggwmedy dyvhlqgkee
      721 fektqkelle kgsitrqgks qlelqqlkqf erleqevsrp idhdlanwtp aqplapgrtg
      781 glgpsdrqll lfyleqcean lttltnavda fftavatnqp pkifvahskf vilsahklvf
      841 igdtlsrqak aadvrsqvth ysnllcdllr givattkaaa lqypspsaaq dmvervkelg
      901 hstqqfrrvl gqlaaa
//
LOCUS       NP_001807                349 aa            linear   PRI 20-NOV-2025
DEFINITION  cell adhesion molecule CEACAM8 precursor [Homo sapiens].
ACCESSION   NP_001807
VERSION     NP_001807.2
DBSOURCE    REFSEQ: accession NM_001816.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Kovaleva,O.V., Podlesnaya,P.A., Mochalnikova,V.V., Kushlinskii,N.E.
            and Gratchev,A.N.
  TITLE     Clinical Significance of CD66b Expression in Non-Small Cell Lung
            Cancer
  JOURNAL   Bull Exp Biol Med 174 (6), 779-783 (2023)
   PUBMED   37162631
  REMARK    GeneRIF: Clinical Significance of CD66b Expression in Non-Small
            Cell Lung Cancer.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Horzum,U., Yoyen-Ermis,D., Taskiran,E.Z., Yilmaz,K.B.,
            Hamaloglu,E., Karakoc,D. and Esendagli,G.
  TITLE     CD66b+ monocytes represent a proinflammatory myeloid subpopulation
            in cancer
  JOURNAL   Cancer Immunol Immunother 70 (1), 75-87 (2021)
   PUBMED   32632664
  REMARK    GeneRIF: CD66b(+) monocytes represent a proinflammatory myeloid
            subpopulation in cancer.
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Iwabuchi,E., Miki,Y., Onodera,Y., Shibahara,Y., Takagi,K.,
            Suzuki,T., Ishida,T. and Sasano,H.
  TITLE     Co-expression of carcinoembryonic antigen-related cell adhesion
            molecule 6 and 8 inhibits proliferation and invasiveness of breast
            carcinoma cells
  JOURNAL   Clin Exp Metastasis 36 (5), 423-432 (2019)
   PUBMED   31222613
  REMARK    GeneRIF: High CEACAM8 expression is associated with metastases in
            breast carcinoma.
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Yamanaka,T., Kuroki,M., Kinugasa,T., Matsuo,Y. and Matsuoka,Y.
  TITLE     Preparation and characterization of two human carcinoembryonic
            antigen family proteins of neutrophils, CD66b and c, in silkworm
            larvae
  JOURNAL   Protein Expr Purif 7 (4), 438-446 (1996)
   PUBMED   8776764
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Khan,W.N., Frangsmyr,L., Teglund,S., Israelsson,A., Bremer,K. and
            Hammarstrom,S.
  TITLE     Identification of three new genes and estimation of the size of the
            carcinoembryonic antigen family
  JOURNAL   Genomics 14 (2), 384-390 (1992)
   PUBMED   1427854
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Oikawa,S., Inuzuka,C., Kuroki,M., Arakawa,F., Matsuoka,Y.,
            Kosaki,G. and Nakazato,H.
  TITLE     A specific heterotypic cell adhesion activity between members of
            carcinoembryonic antigen family, W272 and NCA, is mediated by
            N-domains
  JOURNAL   J Biol Chem 266 (13), 7995-8001 (1991)
   PUBMED   2022629
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Berling,B., Kolbinger,F., Grunert,F., Thompson,J.A., Brombacher,F.,
            Buchegger,F., von Kleist,S. and Zimmermann,W.
  TITLE     Cloning of a carcinoembryonic antigen gene family member expressed
            in leukocytes of chronic myeloid leukemia patients and bone marrow
  JOURNAL   Cancer Res 50 (20), 6534-6539 (1990)
   PUBMED   2208113
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Arakawa,F., Kuroki,M., Misumi,Y., Oikawa,S., Nakazato,H. and
            Matsuoka,Y.
  TITLE     Characterization of a cDNA clone encoding a new species of the
            nonspecific cross-reacting antigen (NCA), a member of the CEA gene
            family
  JOURNAL   Biochem Biophys Res Commun 166 (3), 1063-1071 (1990)
   PUBMED   2306228
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA464901.1, BC026263.1 and AK297012.1.
            
            On Jun 3, 2002 this sequence version replaced NP_001807.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026263.1, D90064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244336.10/ ENSP00000244336.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..349
                     /product="cell adhesion molecule CEACAM8 precursor"
                     /note="carcinoembryonic antigen gene family member 6; CD67
                     antigen; carcinoembryonic antigen related cell adhesion
                     molecule 8; carcinoembryonic antigen CGM6; non-specific
                     cross-reacting antigen NCA-95; cell adhesion molecule
                     CEACAM8"
                     /calculated_mol_wt=34355
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3818
     mat_peptide     35..320
                     /product="Cell adhesion molecule CEACAM8.
                     /id=PRO_0000014572"
                     /note="propagated from UniProtKB/Swiss-Prot (P31997.2)"
                     /calculated_mol_wt=31521
     Region          36..140
                     /region_name="IgV_CEACAM_D1"
                     /note="First immunoglobulin (Ig)-like domain of
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM); cd05774"
                     /db_xref="CDD:409430"
     Region          37..55
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          37..39
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409430"
     Region          44..46
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409430"
     Region          49..56
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409430"
     Region          56..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          64..68
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409430"
     Region          70..91
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409430"
     Region          78..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          88..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..124
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          98..103
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409430"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          105..109
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409430"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          119..124
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409430"
     Region          125..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..140
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409430"
     Region          133..139
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409430"
     Region          146..234
                     /region_name="IgI_hCEACAM_2_4_6_like"
                     /note="Immunoglobulin (Ig)-like domain of human
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule (CEACAM) domains 2, 4, and 6, and similar
                     domains; cd05740"
                     /db_xref="CDD:409402"
     Region          146..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409402"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          153..158
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409402"
     Region          163..169
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409402"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          176..181
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409402"
     Region          183..186
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409402"
     Region          190..194
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409402"
     Region          197..202
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409402"
     Site            197
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          212..220
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409402"
     Region          224..233
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409402"
     Site            224
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          243..318
                     /region_name="IgC2_CEACAM5-like"
                     /note="Fifth immunoglobulin (Ig)-like domain of the
                     carcinoembryonic antigen (CEA) related cell adhesion
                     molecule 5 (CEACAM5) and similar domains; member of the
                     C2-set IgSF domains; cd20948"
                     /db_xref="CDD:409540"
     Region          243..249
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409540"
     Region          254..261
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409540"
     Site            256
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          267..273
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409540"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     Region          276..281
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409540"
     Region          284..290
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409540"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498,
                     ECO:0000269|PubMed:16740002; propagated from
                     UniProtKB/Swiss-Prot (P31997.2)"
     Region          293..304
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409540"
     Region          307..318
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409540"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (P31997.2)"
     CDS             1..349
                     /gene="CEACAM8"
                     /gene_synonym="CD66b; CD67; CGM6; NCA-95"
                     /coded_by="NM_001816.4:97..1146"
                     /db_xref="CCDS:CCDS12610.1"
                     /db_xref="GeneID:1088"
                     /db_xref="HGNC:HGNC:1820"
                     /db_xref="MIM:615747"
ORIGIN      
        1 mgpisapscr wripwqglll taslftfwnp pttaqltiea vpsnaaegke vlllvhnlpq
       61 dprgynwykg etvdanrrii gyvisnqqit pgpaysnret iypnasllmr nvtrndtgsy
      121 tlqviklnlm seevtgqfsv hpetpkpsis snnsnpvedk davaftcepe tqnttylwwv
      181 ngqslpvspr lqlsngnrtl tllsvtrndv gpyeceiqnp asanfsdpvt lnvlygpdap
      241 tispsdtyyh agvnlnlsch aasnppsqys wsvngtfqqy tqklfipnit tknsgsyach
      301 ttnsatgrnr ttvrmitvsd alvqgsspgl saratvsimi gvlarvali
//
LOCUS       NP_001308441             450 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-10 isoform 18 [Homo sapiens].
ACCESSION   NP_001308441
VERSION     NP_001308441.1
DBSOURCE    REFSEQ: accession NM_001321512.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.88279.1,
                                           SRR1660803.73724.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..450
                     /product="septin-10 isoform 18"
                     /calculated_mol_wt=52015
     Region          63..331
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          73..80
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0V9.2)"
     Site            73..80
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(75..81,125,128,208..209,211,263..264)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Region          125..128
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0V9.2)"
     Site            125..128
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(127..165,167..174)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          208..211
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0V9.2)"
     Site            208..211
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            263..265
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..450
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321512.2:140..1492"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS82496.1"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 massevarhl lfqshmatkt tcmssqgsdd eqikrenirs ltmsghvgfe slpdqlvnrs
       61 iqqgfcfnil cvgetgigks tlidtlfntn fedyesshfc pnvklkaqty elqesnvqlk
      121 ltivntvgfg dqinkeesyq pivdyidaqf eaylqeelki krslftyhds rihvclyfis
      181 ptghslktld lltmknldsk vniipviaka dtvsktelqk fkiklmselv sngvqiyqfp
      241 tdddtiakvn aamngqlpfa vvgsmdevkv gnkmvkarqy pwgvvqvene nhcdfvklre
      301 mlictnmedl reqthtrhye lyrrckleem gftdvgpenk pvsvqetyea krhefhgerq
      361 rkeeemkqmf vqrvkekeai lkeaerelqa kfehlkrlhq eermkleekr rlleeeiiaf
      421 skkkatseif hsqsflatgs nlrkdkdrkk
//
LOCUS       NP_001317585             737 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform e
            [Homo sapiens].
ACCESSION   NP_001317585 XP_005248158
VERSION     NP_001317585.1
DBSOURCE    REFSEQ: accession NM_001330656.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 737)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 737)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB236935.1, DB078521.1,
            BC027946.1, AC093804.3, BC088372.1, AC131953.1 and AL080130.1.
            
            On Aug 31, 2016 this sequence version replaced XP_005248158.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (9) uses an alternate in-frame
            splice site and lacks an alternate in-frame exon in the central
            coding region, compared to variant 1, resulting in an isoform (e)
            that is shorter than isoform a. Variants 8 and 9 encode the same
            isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.256450.1,
                                           SRR1803615.175805.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..737
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform e"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=80857
     Region          292..320
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          395..532
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(410,478,495)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(477..482,495,517,521)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Region          561..687
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(572,646,665)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(583,585,633..634,636..643,645,653,659,669,671,674,
                     678,681..682,684..685)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..737
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001330656.2:555..2768"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS82918.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 msevlpadsg vdtlavfmas sgttdvtnrn spatppntln lrsshnelln aeikhtetkn
       61 stppkcrkky altniqaamg lsdpaaqpll gngsaniklv kngenqlrka aeqgqqdpnk
      121 nlsptavini tseklegkep hpqdssscei lpsqprrtks flnyyadlet sareleqnrg
      181 nhhgtaeeks qpvqgqasti igngdlllqk pnrpqssped gqvatvsssp etkkdhpktg
      241 aktdcalhri qnlapsdees swttlsqdsa spsspdetdi wsdhsfqtdp dlppgwkrvs
      301 diagtyywhi ptgttqwerp vsipadlqgs rkgslssvtp sptpenedlh aatvnpdpsl
      361 kefegatlry aslklrnaph pddddscsin sdpeakcfav rslgwvemae edlapgkssv
      421 avnncirqls yckndirdtv giwgegkdmy lilendmlsl vdpmdrsvlh sqpivsirvw
      481 gvgrdngrdf ayvardkdtr ilkchvfrcd tpakaiatsl heicskimae rknakalacs
      541 slqeranvnl dvplqvdfpt pktelvqkfh vqylgmlpvd kpvgmdilns aienlmtssn
      601 kedwlsvnmn vadatvtvis ekneeevlve crvrflsfmg vgkdvhtfaf imdtgnqrfe
      661 chvfwcepna gnvseavqaa cmlryqkclv arppsqkvrp ppppadsvtr rvttnvkrgv
      721 lslidtlkqk rpvtemp
//
LOCUS       NP_055191               1253 aa            linear   PRI 20-NOV-2025
DEFINITION  cytoplasmic FMR1-interacting protein 2 isoform a [Homo sapiens].
ACCESSION   NP_055191 NP_110405
VERSION     NP_055191.2
DBSOURCE    REFSEQ: accession NM_014376.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1253)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1253)
  AUTHORS   Peng,X., Wellard,N., Ghosh,A., Troakes,C. and Giese,K.P.
  TITLE     Different dysregulations of CYFIP1 and CYFIP2 in distinct types of
            dementia
  JOURNAL   Brain Res Bull 206, 110849 (2024)
   PUBMED   38128786
  REMARK    GeneRIF: Different dysregulations of CYFIP1 and CYFIP2 in distinct
            types of dementia.
REFERENCE   3  (residues 1 to 1253)
  AUTHORS   Peng,Q., Ren,B., Xin,K., Liu,W., Alam,M.S., Yang,Y., Gu,X., Zhu,Y.
            and Tian,Y.
  TITLE     CYFIP2 serves as a prognostic biomarker and correlates with tumor
            immune microenvironment in human cancers
  JOURNAL   Eur J Med Res 28 (1), 364 (2023)
   PUBMED   37735711
  REMARK    GeneRIF: CYFIP2 serves as a prognostic biomarker and correlates
            with tumor immune microenvironment in human cancers.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1253)
  AUTHORS   Biembengut,I.V., Shigunov,P., Frota,N.F., Lourenzoni,M.R. and de
            Souza,T.A.C.B.
  TITLE     Molecular Dynamics of CYFIP2 Protein and Its R87C Variant Related
            to Early Infantile Epileptic Encephalopathy
  JOURNAL   Int J Mol Sci 23 (15), 8708 (2022)
   PUBMED   35955843
  REMARK    GeneRIF: Molecular Dynamics of CYFIP2 Protein and Its R87C Variant
            Related to Early Infantile Epileptic Encephalopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1253)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1253)
  AUTHORS   Eden,S., Rohatgi,R., Podtelejnikov,A.V., Mann,M. and Kirschner,M.W.
  TITLE     Mechanism of regulation of WAVE1-induced actin nucleation by Rac1
            and Nck
  JOURNAL   Nature 418 (6899), 790-793 (2002)
   PUBMED   12181570
REFERENCE   7  (residues 1 to 1253)
  AUTHORS   Schenck,A., Bardoni,B., Moro,A., Bagni,C. and Mandel,J.L.
  TITLE     A highly conserved protein family interacting with the fragile X
            mental retardation protein (FMRP) and displaying selective
            interactions with FMRP-related proteins FXR1P and FXR2P
  JOURNAL   Proc Natl Acad Sci U S A 98 (15), 8844-8849 (2001)
   PUBMED   11438699
REFERENCE   8  (residues 1 to 1253)
  AUTHORS   Saller,E., Tom,E., Brunori,M., Otter,M., Estreicher,A., Mack,D.H.
            and Iggo,R.
  TITLE     Increased apoptosis induction by 121F mutant p53
  JOURNAL   EMBO J 18 (16), 4424-4437 (1999)
   PUBMED   10449408
REFERENCE   9  (residues 1 to 1253)
  AUTHORS   Witke,W., Podtelejnikov,A.V., Di Nardo,A., Sutherland,J.D.,
            Gurniak,C.B., Dotti,C. and Mann,M.
  TITLE     In mouse brain profilin I and profilin II associate with regulators
            of the endocytic pathway and actin assembly
  JOURNAL   EMBO J 17 (4), 967-976 (1998)
   PUBMED   9463375
REFERENCE   10 (residues 1 to 1253)
  AUTHORS   Kitamura,T., Kitamura,Y., Yonezawa,K., Totty,N.F., Gout,I.,
            Hara,K., Waterfield,M.D., Sakaue,M., Ogawa,W. and Kasuga,M.
  TITLE     Molecular cloning of p125Nap1, a protein that associates with an
            SH3 domain of Nck
  JOURNAL   Biochem Biophys Res Commun 219 (2), 509-514 (1996)
   PUBMED   8605018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009185.6, BC011762.1, AL136549.1 and AC008676.6.
            
            On Nov 23, 2005 this sequence version replaced NP_055191.1.
            
            Transcript Variant: This variant (3) contains an alternate exon in
            the 5' UTR, compared to variant 1. Variants 1 and 2 encode the same
            isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021008.1, SRR1660807.185041.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..1253
                     /product="cytoplasmic FMR1-interacting protein 2 isoform
                     a"
                     /note="p53-inducible protein 121"
                     /calculated_mol_wt=145543
     Region          388..1221
                     /region_name="FragX_IP"
                     /note="Cytoplasmic Fragile-X interacting family;
                     pfam05994"
                     /db_xref="CDD:461799"
     Site            1037
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96F07.2)"
     CDS             1..1253
                     /gene="CYFIP2"
                     /gene_synonym="DEE65; EIEE65; PIR121"
                     /coded_by="NM_014376.4:284..4045"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75364.1"
                     /db_xref="GeneID:26999"
                     /db_xref="HGNC:HGNC:13760"
                     /db_xref="MIM:606323"
ORIGIN      
        1 mtthvtleda lsnvdlleel plpdqqpcie pppssimyqa nfdtnfedrn afvtgiaryi
       61 eqatvhssmn emleegheya vmlytwrscs raipqvkcne qpnrveiyek tvevlepevt
      121 klmkfmyfqr kaierfcsev krlchaerrk dfvseayllt lgkfinmfav ldelknmkcs
      181 vkndhsaykr aaqflrkmad pqsiqesqnl smflanhnri tqclhqqlev ipgyeellad
      241 ivnicvdyye nkmyltpsek hmllkvmgfg lylmdgnvsn iykldakkri nlskidkffk
      301 qlqvvplfgd mqielaryik tsahyeenks kwtctqssis pqyniceqmv qirddhirfi
      361 selarysnse vvtgsgldsq ksdeeyrelf dlalrglqll skwsahvmev yswklvhptd
      421 kfcnkdcpgt aeeyeratry nytseekfaf veviamikgl qvlmgrmesv fnqairntiy
      481 aalqdfaqvt lreplrqavr kkknvlisvl qairkticdw eggreppndp clrgekdpkg
      541 gfdikvprra vgpsstqlym vrtmleslia dksgskktlr ssldgpivla iedfhkqsff
      601 fthllnisea lqqccdlsql wfrefflelt mgrriqfpie msmpwiltdh iletkepsmm
      661 eyvlypldly ndsayyaltk fkkqflydei eaevnlcfdq fvykladqif ayykamagsv
      721 lldkrfraec knygviipyp psnryetllk qrhvqllgrs idlnrlitqr isaamyksld
      781 qaisrfesed ltsivelewl leinrlthrl lckhmtldsf damfreanhn vsapygritl
      841 hvfwelnfdf lpnycyngst nrfvrtaipf tqepqrdkpa nvqpyylygs kplniayshi
      901 yssyrnfvgp phfkticrll gyqgiavvme ellkivksll qgtilqyvkt lievmpkicr
      961 lprheygspg ileffhhqlk diieyaelkt dvfqslrevg nailfcllie qalsqeevcd
     1021 llhaapfqni lprvyikege rlevrmkrle akyaplhlvp lierlgtpqq iaiaregdll
     1081 tkerlccgls mfeviltrir sylqdpiwrg ppptngvmhv decvefhrlw samqfvycip
     1141 vgtneftaeq cfgdglnwag csiivllgqq rrfdlfdfcy hllkvqrqdg kdeiiknvpl
     1201 kkmadrirky qilnnevfai lnkymksvet dsstvehvrc fqppihqsla ttc
//
LOCUS       NP_859062                395 aa            linear   PRI 20-NOV-2025
DEFINITION  protein TAMALIN isoform 1 [Homo sapiens].
ACCESSION   NP_859062
VERSION     NP_859062.1
DBSOURCE    REFSEQ: accession NM_181711.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Caillet-Saguy,C. and Wolff,N.
  TITLE     PDZ-Containing Proteins Targeted by the ACE2 Receptor
  JOURNAL   Viruses 13 (11), 2281 (2021)
   PUBMED   34835087
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Pandey,S., Ramsakha,N., Sharma,R., Gulia,R., Ojha,P., Lu,W. and
            Bhattacharyya,S.
  TITLE     The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors
  JOURNAL   J Biol Chem 295 (25), 8575-8588 (2020)
   PUBMED   32376687
  REMARK    GeneRIF: The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Matosin,N., Fernandez-Enright,F., Lum,J.S., Andrews,J.L., Engel,M.,
            Huang,X.F. and Newell,K.A.
  TITLE     Metabotropic glutamate receptor 5, and its trafficking molecules
            Norbin and Tamalin, are increased in the CA1 hippocampal region of
            subjects with schizophrenia
  JOURNAL   Schizophr Res 166 (1-3), 212-218 (2015)
   PUBMED   26048293
  REMARK    GeneRIF: Schizophrenia subjects compared to controls showed a
            marked increase in CA1 hippocampal Norbin, and Tamalin proteins
            (47% and 34% respectively), which are endogenous regulators of
            mGluR5 signalling and trafficking
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Fransen,E., Bonneux,S., Corneveaux,J.J., Schrauwen,I., Di
            Berardino,F., White,C.H., Ohmen,J.D., Van de Heyning,P.,
            Ambrosetti,U., Huentelman,M.J., Van Camp,G. and Friedman,R.A.
  TITLE     Genome-wide association analysis demonstrates the highly polygenic
            character of age-related hearing impairment
  JOURNAL   Eur J Hum Genet 23 (1), 110-115 (2015)
   PUBMED   24939585
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Sugi,T., Oyama,T., Muto,T., Nakanishi,S., Morikawa,K. and
            Jingami,H.
  TITLE     Crystal structures of autoinhibitory PDZ domain of Tamalin:
            implications for metabotropic glutamate receptor trafficking
            regulation
  JOURNAL   EMBO J 26 (8), 2192-2205 (2007)
   PUBMED   17396155
  REMARK    GeneRIF: The crystal structures of the autoinhibitory PDZ domain of
            Tamalin has implications for the regulation of metabotropic
            glutamate receptor trafficking.
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Kitano,J., Yamazaki,Y., Kimura,K., Masukado,T., Nakajima,Y. and
            Nakanishi,S.
  TITLE     Tamalin is a scaffold protein that interacts with multiple neuronal
            proteins in distinct modes of protein-protein association
  JOURNAL   J Biol Chem 278 (17), 14762-14768 (2003)
   PUBMED   12586822
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Kitano,J., Kimura,K., Yamazaki,Y., Soda,T., Shigemoto,R.,
            Nakajima,Y. and Nakanishi,S.
  TITLE     Tamalin, a PDZ domain-containing protein, links a protein complex
            formation of group 1 metabotropic glutamate receptors and the
            guanine nucleotide exchange factor cytohesins
  JOURNAL   J Neurosci 22 (4), 1280-1289 (2002)
   PUBMED   11850456
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Nevrivy,D.J., Peterson,V.J., Avram,D., Ishmael,J.E., Hansen,S.G.,
            Dowell,P., Hruby,D.E., Dawson,M.I. and Leid,M.
  TITLE     Interaction of GRASP, a protein encoded by a novel retinoic
            acid-induced gene, with members of the cytohesin family of guanine
            nucleotide exchange factors
  JOURNAL   J Biol Chem 275 (22), 16827-16836 (2000)
   PUBMED   10828067
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Dominguez,O., Ashhab,Y., Sabater,L., Belloso,E., Caro,P. and
            Pujol-Borrell,R.
  TITLE     Cloning of ARE-containing genes by AU-motif-directed display
  JOURNAL   Genomics 54 (2), 278-286 (1998)
   PUBMED   9828130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY052304.1, BC053666.1 and
            BC052967.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that functions as a molecular
            scaffold, linking receptors, including group 1 metabotropic
            glutamate receptors, to neuronal proteins. The encoded protein
            contains conserved domains, including a leucine zipper sequence,
            PDZ domain and a C-terminal PDZ-binding motif. Alternately spliced
            transcript variants have been observed for this gene.[provided by
            RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279868.3230.1, BC053666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293662.9/ ENSP00000293662.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..395
                     /product="protein TAMALIN isoform 1"
                     /note="general receptor for phosphoinositides 1 associated
                     scaffold protein; GRP1 (general receptor for
                     phosphoinositides 1)-associated scaffold protein; protein
                     TAMALIN"
                     /calculated_mol_wt=42492
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R4T5; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Region          97..187
                     /region_name="PDZ_tamalin_CYTIP-like"
                     /note="PDZ domain of tamalin, cytohesin-1-interacting
                     protein (CYTIP), and related domains; cd06713"
                     /db_xref="CDD:467197"
     Site            order(111..117,136,139,168,172,175..176)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467197"
     Region          181..258
                     /region_name="Interaction with PSCD3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            270
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Region          293..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJA9; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6J2.1)"
     CDS             1..395
                     /gene="TAMALIN"
                     /gene_synonym="GRASP"
                     /coded_by="NM_181711.4:75..1262"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8817.1"
                     /db_xref="GeneID:160622"
                     /db_xref="HGNC:HGNC:18707"
                     /db_xref="MIM:612027"
ORIGIN      
        1 mtlrrlrklq qkeeaaatpd paartpdsev apaapvptpg ppaaaatpgp padelyaale
       61 dyhpaelyra lavsggtlpr rkgsgfrwkn lsqspeqqrk vltlekednq tfgfeiqtyg
      121 lhhreeqrve mvtfvcrvhe sspaqlaglt pgdtiasvng lnvegirhre ivdiikasgn
      181 vlrletlygt sirkaelear lqylkqtlye kwgeyrslmv qeqrlvhglv vkdpsiydtl
      241 esvrsclyga gllpgslpfg pllavpgrpr ggarrargda ddavyhtcff gdseppalpp
      301 pppparafgp gpaetpavgp gpgpraalsr sasvrcagpg ggggggapga lwteareqal
      361 cgpglrktky rsfrrrllkf ipglnrslee eesql
//
LOCUS       NP_001354620             865 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform bbb [Homo sapiens].
ACCESSION   NP_001354620
VERSION     NP_001354620.1
DBSOURCE    REFSEQ: accession NM_001367691.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 865)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 865)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 865)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 865)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 865)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.57992.1,
                                           SRR1660807.144071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..865
                     /product="SUN domain-containing protein 1 isoform bbb"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=96015
     Region          12..372
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          497..550
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(497,500..501,504,507..508,511..512,514..515,
                     518..519,521..522,525..526,528..529,532,535..536,539,
                     542..543,546..547,549..550)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          509..>642
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          627..685
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          728..863
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..865
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367691.1:105..2702"
                     /note="isoform bbb is encoded by transcript variant 54"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy
      241 ygrmnvrevl redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca
      301 gyfllqilrr igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv
      361 flltrclrni ckflvllipl flllglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk
      421 pttsrlkqpl qgdseafpwh wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm
      481 eggaagpsas vrdavgqppr etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk
      541 qktisavgeq llptvehlql eldqlksels swrhvktgce tvdavqervd vqvremvkll
      601 fsedqqggsl eqllqrfssq fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs
      661 avseagasgi teaqaraivn salklysqdk tgmvdfales gggsilstrc setyetktal
      721 mslfgiplwy fsqsprvviq pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl
      781 sptgnissap kdfavyglen eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel
      841 rifsnwghpe ytclyrfrvh gepvk
//
LOCUS       NP_055719                512 aa            linear   PRI 20-NOV-2025
DEFINITION  rab11 family-interacting protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055719
VERSION     NP_055719.1
DBSOURCE    REFSEQ: accession NM_014904.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Cullis,D.N., Philip,B., Baleja,J.D. and Feig,L.A.
  TITLE     Rab11-FIP2, an adaptor protein connecting cellular components
            involved in internalization and recycling of epidermal growth
            factor receptors
  JOURNAL   J Biol Chem 277 (51), 49158-49166 (2002)
   PUBMED   12364336
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Lindsay,A.J. and McCaffrey,M.W.
  TITLE     Rab11-FIP2 functions in transferrin recycling and associates with
            endosomal membranes via its COOH-terminal domain
  JOURNAL   J Biol Chem 277 (30), 27193-27199 (2002)
   PUBMED   11994279
  REMARK    GeneRIF: Rab11-FIP2 functions downstream of Rab11 in endosomal
            trafficking.
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Wallace,D.M., Lindsay,A.J., Hendrick,A.G. and McCaffrey,M.W.
  TITLE     The novel Rab11-FIP/Rip/RCP family of proteins displays extensive
            homo- and hetero-interacting abilities
  JOURNAL   Biochem Biophys Res Commun 292 (4), 909-915 (2002)
   PUBMED   11944901
REFERENCE   9  (residues 1 to 512)
  AUTHORS   Hales,C.M., Griner,R., Hobdy-Henderson,K.C., Dorn,M.C., Hardy,D.,
            Kumar,R., Navarre,J., Chan,E.K., Lapierre,L.A. and Goldenring,J.R.
  TITLE     Identification and characterization of a family of
            Rab11-interacting proteins
  JOURNAL   J Biol Chem 276 (42), 39067-39075 (2001)
   PUBMED   11495908
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Prekeris,R., Davies,J.M. and Scheller,R.H.
  TITLE     Identification of a novel Rab11/25 binding domain present in Eferin
            and Rip proteins
  JOURNAL   J Biol Chem 276 (42), 38966-38970 (2001)
   PUBMED   11481332
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC022395.4, AB023158.1 and BM975322.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.101601.1,
                                           SRR1660805.220069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148, SAMEA2467150
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355624.8/ ENSP00000347839.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.11"
     Protein         1..512
                     /product="rab11 family-interacting protein 2 isoform 1"
                     /note="rab11 family-interacting protein 2; RAB11 family
                     interacting protein 2 (class I)"
                     /calculated_mol_wt=58148
     Region          15..141
                     /region_name="C2_Rab11-FIP_classI"
                     /note="C2 domain found in Rab11-family interacting
                     proteins (FIP) class I; cd08682"
                     /db_xref="CDD:176064"
     Region          15..102
                     /region_name="Necessary for its cellular translocation to
                     the plasma membrane"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          169..239
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MARK2.
                     /evidence=ECO:0000269|PubMed:16775013,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          262..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          323..325
                     /region_name="NPF 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          361..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          406..408
                     /region_name="NPF 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          440..442
                     /region_name="NPF 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     Region          452..499
                     /region_name="RBD-FIP"
                     /note="FIP domain; pfam09457"
                     /db_xref="CDD:462805"
     Region          465..512
                     /region_name="Necessary for interaction with AP2A1,
                     RAB11A, subcellular location, endocytosis activity and
                     homooligomerization.
                     /evidence=ECO:0000269|PubMed:12364336"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L804.1)"
     CDS             1..512
                     /gene="RAB11FIP2"
                     /gene_synonym="nRip11; Rab11-FIP2"
                     /coded_by="NM_014904.3:779..2317"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7602.1"
                     /db_xref="GeneID:22841"
                     /db_xref="HGNC:HGNC:29152"
                     /db_xref="MIM:608599"
ORIGIN      
        1 mmlseqaqkw fpthvqvtvl qakdlkpkgk sgtndtytii qlgkekysts vaektlepvw
       61 keeasfelpg lliqgspeky ilflivmhrs lvgldkflgq vainlndife dkqrrktewf
      121 rleskqgkri knrgeikvni qfmrnnmtas mfdlsmkdkt rspfaklkdk mkgrkndgtf
      181 sdtssaiips thmpdansef ssgeiqmksk pkkpfllgpq rlssahsmsd lsgshmssek
      241 lkagtigqth llghqldsfg tvpesgslks phrrtlsfdt skmnqpdsiv degelcfgrq
      301 ndpftnvtas lpqkfatlpr kknpfeesse twdssmnlfs kpieirkenk rekrekvslf
      361 ervtgkkdsr rsdklnnggs dspcdlkspn afsenrqdyf dyestnpfta kfrasnimps
      421 ssfhmsptsn edlrkipdsn pfdatagyrs ltyeevlqel vkhkellrrk dthireledy
      481 idnllvrvme etpsilrvpy epsrkagkfs ns
//
LOCUS       NP_001300881             304 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 4 [Homo sapiens].
ACCESSION   NP_001300881
VERSION     NP_001300881.1
DBSOURCE    REFSEQ: accession NM_001313952.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP225027.1, BM905813.1 and
            BC009751.2.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (6) lacks an exon in the 5' coding
            region and uses two alternate acceptor splice sites in the
            mid-region compared to variant 1. The encoded isoform (4),
            resulting from use of an in-frame downstream start codon, has a
            shorter N-terminus and and an extra amino acid in the mid-region
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed/partial sample support SAMEA1965299,
                              SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..304
                     /product="aurora kinase B isoform 4"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=34785
     Region          30..299
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(43..46,49,51,64,66,98,114..117,160,164..165,167,
                     177..178)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..304
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_001313952.2:183..1097"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 msrsnvqpta apgqkvmens sgtpdiltrr hftiddfeig rplgkgkfgn vylarekksh
       61 fivalkvlfk sqiekegveh qlrreieiqa hlhhpnilrl ynyfydrrri ylileyaprg
      121 elykelqksc tfdeqrtati meeladalmy chgkkvihrd ikpenlllgl kgelkiadfg
      181 wsvhapslrr ktmcgtldyl ppemiegrmh nekvdlwcig vlcyellvgn ppfesashne
      241 tyrrivkvdl kfpasvpmga qdliskllrh npserlplaq vsahpwvran srrvlppsal
      301 qsva
//
LOCUS       NP_056323                657 aa            linear   PRI 20-NOV-2025
DEFINITION  protein mono-ADP-ribosyltransferase TIPARP [Homo sapiens].
ACCESSION   NP_056323
VERSION     NP_056323.2
DBSOURCE    REFSEQ: accession NM_015508.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Manetsch,P., Bohi,F., Nowak,K., Leslie Pedrioli,D.M. and
            Hottiger,M.O.
  TITLE     PARP7-mediated ADP-ribosylation of FRA1 promotes cancer cell growth
            by repressing IRF1- and IRF3-dependent apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 120 (49), e2309047120 (2023)
   PUBMED   38011562
  REMARK    GeneRIF: PARP7-mediated ADP-ribosylation of FRA1 promotes cancer
            cell growth by repressing IRF1- and IRF3-dependent apoptosis.
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Jiao,H., Yan,Z., Zhai,X., Yang,Y., Wang,N., Li,X., Jiang,Z. and
            Su,S.
  TITLE     Transcriptome screening identifies TIPARP as an antiviral host
            factor against the Getah virus
  JOURNAL   J Virol 97 (10), e0059123 (2023)
   PUBMED   37768084
  REMARK    GeneRIF: Transcriptome screening identifies TIPARP as an antiviral
            host factor against the Getah virus.
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Yang,C., Wierbilowicz,K., Dworak,N.M., Bae,S.Y., Tengse,S.B.,
            Abianeh,N., Drake,J.M., Abbas,T., Ratan,A., Wotton,D. and
            Paschal,B.M.
  TITLE     Induction of PARP7 Creates a Vulnerability for Growth Inhibition by
            RBN2397 in Prostate Cancer Cells
  JOURNAL   Cancer Res Commun 3 (4), 592-606 (2023)
   PUBMED   37077937
  REMARK    GeneRIF: Induction of PARP7 Creates a Vulnerability for Growth
            Inhibition by RBN2397 in Prostate Cancer Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Zhang,Y., Song,M., Bi,Y., Lei,Y., Sun,X. and Chen,Y.
  TITLE     TIPARP is involved in the regulation of intraocular pressure
  JOURNAL   Commun Biol 5 (1), 1386 (2022)
   PUBMED   36536086
  REMARK    GeneRIF: TIPARP is involved in the regulation of intraocular
            pressure.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Gozgit,J.M., Vasbinder,M.M., Abo,R.P., Kunii,K., Kuplast-Barr,K.G.,
            Gui,B., Lu,A.Z., Molina,J.R., Minissale,E., Swinger,K.K.,
            Wigle,T.J., Blackwell,D.J., Majer,C.R., Ren,Y., Niepel,M.,
            Varsamis,Z.A., Nayak,S.P., Bamberg,E., Mo,J.R., Church,W.D.,
            Mady,A.S.A., Song,J., Utley,L., Rao,P.E., Mitchison,T.J.,
            Kuntz,K.W., Richon,V.M. and Keilhack,H.
  TITLE     PARP7 negatively regulates the type I interferon response in cancer
            cells and its inhibition triggers antitumor immunity
  JOURNAL   Cancer Cell 39 (9), 1214-1226 (2021)
   PUBMED   34375612
  REMARK    GeneRIF: PARP7 negatively regulates the type I interferon response
            in cancer cells and its inhibition triggers antitumor immunity.
REFERENCE   6  (residues 1 to 657)
  AUTHORS   de Waard,P.W., Peijnenburg,A.A., Baykus,H., Aarts,J.M.,
            Hoogenboom,R.L., van Schooten,F.J. and de Kok,T.M.
  TITLE     A human intervention study with foods containing natural
            Ah-receptor agonists does not significantly show AhR-mediated
            effects as measured in blood cells and urine
  JOURNAL   Chem Biol Interact 176 (1), 19-29 (2008)
   PUBMED   18762178
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Otto,H., Reche,P.A., Bazan,F., Dittmar,K., Haag,F. and
            Koch-Nolte,F.
  TITLE     In silico characterization of the family of PARP-like
            poly(ADP-ribosyl)transferases (pARTs)
  JOURNAL   BMC Genomics 6, 139 (2005)
   PUBMED   16202152
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 657)
  AUTHORS   Ame,J.C., Spenlehauer,C. and de Murcia,G.
  TITLE     The PARP superfamily
  JOURNAL   Bioessays 26 (8), 882-893 (2004)
   PUBMED   15273990
  REMARK    Review article
REFERENCE   9  (residues 1 to 657)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of human TIPARP gene within the
            CCNL amplicon at human chromosome 3q25.31
  JOURNAL   Int J Oncol 23 (2), 541-547 (2003)
   PUBMED   12851707
  REMARK    GeneRIF: TIPARP (DKFZp434J214) gene is amplified in HNSCC.  TIPARP,
            FLJ22693 and ZAP proteins with TPH, WW and PARP-like domains
            constitute the TIPARP family.
REFERENCE   10 (residues 1 to 657)
  AUTHORS   Ma,Q., Baldwin,K.T., Renzelli,A.J., McDaniel,A. and Dong,L.
  TITLE     TCDD-inducible poly(ADP-ribose) polymerase: a novel response to
            2,3,7,8-tetrachlorodibenzo-p-dioxin
  JOURNAL   Biochem Biophys Res Commun 289 (2), 499-506 (2001)
   PUBMED   11716501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX537965.1, AC092927.5 and
            BC050350.1.
            
            On Nov 26, 2003 this sequence version replaced NP_056323.1.
            
            Summary: This gene encodes a member of the poly(ADP-ribose)
            polymerase superfamily. Studies of the mouse ortholog have shown
            that the encoded protein catalyzes histone poly(ADP-ribosyl)ation
            and may be involved in T-cell function. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.73394.1,
                                           SRR1660803.174701.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295924.12/ ENSP00000295924.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..657
                     /product="protein mono-ADP-ribosyltransferase TIPARP"
                     /EC_number="2.4.2.30"
                     /note="poly [ADP-ribose] polymerase 7;
                     ADP-ribosyltransferase diphtheria toxin-like 14"
                     /calculated_mol_wt=76097
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3E1.1)"
     Region          41..47
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:30373764"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3E1.1)"
     Region          346..401
                     /region_name="WWE"
                     /note="WWE domain; pfam02825"
                     /db_xref="CDD:460715"
     Region          529..648
                     /region_name="TCCD_inducible_PARP_like"
                     /note="Poly(ADP-ribose) polymerases catalyse the covalent
                     attachment of ADP-ribose units from NAD+ to itself and to
                     a limited number of other DNA binding proteins, which
                     decreases their affinity for DNA. Poly(ADP-ribose)
                     polymerase is a regulatory component...; cd01439"
                     /db_xref="CDD:238719"
     Site            order(531..535,538,542,546..548,550,563..565,575,631)
                     /site_type="other"
                     /note="nad+ binding pocket [chemical binding]"
                     /db_xref="CDD:238719"
     CDS             1..657
                     /gene="TIPARP"
                     /gene_synonym="ARTD14; PARP7; pART14"
                     /coded_by="NM_015508.5:249..2222"
                     /db_xref="CCDS:CCDS3177.1"
                     /db_xref="GeneID:25976"
                     /db_xref="HGNC:HGNC:23696"
                     /db_xref="MIM:612480"
ORIGIN      
        1 memettepep dcvvqppspp ddfscqmrls ekitplktcf kkkdqkrlgt gtlrslrpil
       61 ntllesgsld gvfrsrnqst denslhepmm kkameinssc ppaennmsvl ipdrtnvgdq
      121 ipeahpstea pervvpiqdh sfpsetlsgt vadstpahfq tdllhpvssd vptspdcldk
      181 vidyvpgifq ensftiqyil dtsdklstel fqdkseeasl dlvfelvnql qyhthqengi
      241 eicmdflqgt ciygrdclkh htvlpyhwqi krtttqkwqs vfndsqehle rfycnpendr
      301 mrmkyggqef wadlnamnvy ettefdqlrr lstppssnvn siyhtvwkff crdhfgwrey
      361 pesvirliee ansrglkevr fmmwnnhyil hnsffrreik rrplfrscfi llpylqtlgg
      421 vptqappple atsssqiicp dgvtsanfyp etwvymhpsq dfiqvpvsae dksyriiynl
      481 fhktvpefky rilqilrvqn qflwekykrk keymnrkmfg rdriinerhl fhgtsqdvvd
      541 gickhnfdpr vcgkhatmfg qgsyfakkas yshnfskkss kgvhfmflak vltgrytmgs
      601 hgmrrpppvn pgsvtsdlyd scvdnffepq ifvifnddqs ypyfviqyee vsntvsi
//
LOCUS       NP_001334970             908 aa            linear   PRI 20-NOV-2025
DEFINITION  protein PTHB1 isoform 9 [Homo sapiens].
ACCESSION   NP_001334970 XP_011513566
VERSION     NP_001334970.1
DBSOURCE    REFSEQ: accession NM_001348041.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 908)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 908)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 908)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 908)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 908)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 908)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 908)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 908)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 908)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 908)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074338.1, AC007312.1,
            AC087070.2, AC006195.1, AC078833.5, AC018664.11 and AW119001.1.
            
            On Jan 4, 2017 this sequence version replaced XP_011513566.1.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (10) represents the allele encoded
            by the GRCh38 reference genome and encodes isoform (9).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.208506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..908
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..908
                     /product="protein PTHB1 isoform 9"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=101689
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          1..407
                     /region_name="Seven-bladed beta-propeller.
                     /evidence=ECO:0000269|PubMed:26085087"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Site            141
                     /site_type="other"
                     /note="Critical for protein stability.
                     /evidence=ECO:0000269|PubMed:26085087; propagated from
                     UniProtKB/Swiss-Prot (Q3SYG4.1)"
     Region          441..819
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     Region          685..765
                     /region_name="Interaction with LZTL1.
                     /evidence=ECO:0000269|PubMed:22072986"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SYG4.1)"
     CDS             1..908
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001348041.4:490..3216"
                     /note="isoform 9 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS94079.1"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmtpd
      481 ltrtvsfsvy lkrsytpsel egnavvsysr ptdrnpdgip rviqckfrlp lkliclpgqp
      541 sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf hflggaritv lasktsqryr
      601 iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi plqeyfelid hhfelringe
      661 kleellsera vqfraiqrrl larfkdktpa plqhldtlld gtykqviala daveenqgnl
      721 fqsftrlksa thlvillial wqklsadqva ileaaflplq edtqelgwee tvdaaishll
      781 ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls kggrlclstd aaapqtmvmp
      841 ggcttipesd leersveqds telftnhrhl taetprpdpr tgqrieawtl riphslsqhl
      901 qlmegpks
//
LOCUS       NP_001356020             360 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356020 XP_011538144
VERSION     NP_001356020.1
DBSOURCE    REFSEQ: accession NM_001369091.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_011538144.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.124506.1,
                                           SRR1803611.175034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..360
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 6"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40919
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..360
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369091.1:209..1291"
                     /note="isoform 6 is encoded by transcript variant 12"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitvv
//
LOCUS       NP_001356512             643 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform m [Homo sapiens].
ACCESSION   NP_001356512 XP_016881425
VERSION     NP_001356512.1
DBSOURCE    REFSEQ: accession NM_001369583.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881425.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3814993.1,
                                           ERR4352443.612877.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..643
                     /product="transcription factor 4 isoform m"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68480
     Region          534..618
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(542,546,548..550,552,557,578..579)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(555..556,559..560,562..563,566,570,580,583,587,590,
                     593..598)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..643
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369583.1:156..2087"
                     /note="isoform m is encoded by transcript variant 43"
                     /db_xref="CCDS:CCDS77192.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsagtavwsr nggqassspn yegplhslqs
      361 riedrlerld daihvlrnha vgpstampgg hgdmhgiigp shngamgglg sgygtgllsa
      421 nrhslmvgth redgvalrgs hsllpnqvpv pqlpvqsats pdlnppqdpy rgmppglqgq
      481 svssgsseik sddegdenlq dtkssedkkl dddkkdiksi tsnnddedlt peqkaereke
      541 rrmannarer lrvrdineaf kelgrmvqlh lksdkpqtkl lilhqavavi lsleqqvrer
      601 nlnpkaaclk rreeekvsse ppplslagph pgmgdasnhm gqm
//
LOCUS       NP_001171720            1244 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog isoform 8 [Homo sapiens].
ACCESSION   NP_001171720
VERSION     NP_001171720.1
DBSOURCE    REFSEQ: accession NM_001184791.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1244)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1244)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1244)
  AUTHORS   Zhang,J., Shi,Y., Ding,K., Yu,W., He,J. and Sun,B.
  TITLE     DCAF1 interacts with PARD3 to promote hepatocellular carcinoma
            progression and metastasis by activating the Akt signaling pathway
  JOURNAL   J Exp Clin Cancer Res 43 (1), 136 (2024)
   PUBMED   38711082
  REMARK    GeneRIF: DCAF1 interacts with PARD3 to promote hepatocellular
            carcinoma progression and metastasis by activating the Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1244)
  AUTHORS   Wu,J., Tan,H.Y., Chan,Y.T., Lu,Y., Feng,Z., Yuan,H., Zhang,C.,
            Feng,Y. and Wang,N.
  TITLE     PARD3 drives tumorigenesis through activating Sonic Hedgehog
            signalling in tumour-initiating cells in liver cancer
  JOURNAL   J Exp Clin Cancer Res 43 (1), 42 (2024)
   PUBMED   38317186
  REMARK    GeneRIF: PARD3 drives tumorigenesis through activating Sonic
            Hedgehog signalling in tumour-initiating cells in liver cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1244)
  AUTHORS   Gunji,D., Narumi,R., Muraoka,S., Isoyama,J., Ikemoto,N., Ishida,M.,
            Tomonaga,T., Sakai,Y., Obama,K. and Adachi,J.
  TITLE     Integrative analysis of cancer dependency data and comprehensive
            phosphoproteomics data revealed the EPHA2-PARD3 axis as a cancer
            vulnerability in KRAS-mutant colorectal cancer
  JOURNAL   Mol Omics 19 (8), 624-639 (2023)
   PUBMED   37232035
  REMARK    GeneRIF: Integrative analysis of cancer dependency data and
            comprehensive phosphoproteomics data revealed the EPHA2-PARD3 axis
            as a cancer vulnerability in KRAS-mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1244)
  AUTHORS   Ebnet,K., Suzuki,A., Horikoshi,Y., Hirose,T., Meyer Zu
            Brickwedde,M.K., Ohno,S. and Vestweber,D.
  TITLE     The cell polarity protein ASIP/PAR-3 directly associates with
            junctional adhesion molecule (JAM)
  JOURNAL   EMBO J 20 (14), 3738-3748 (2001)
   PUBMED   11447115
REFERENCE   7  (residues 1 to 1244)
  AUTHORS   Suzuki,A., Yamanaka,T., Hirose,T., Manabe,N., Mizuno,K.,
            Shimizu,M., Akimoto,K., Izumi,Y., Ohnishi,T. and Ohno,S.
  TITLE     Atypical protein kinase C is involved in the evolutionarily
            conserved par protein complex and plays a critical role in
            establishing epithelia-specific junctional structures
  JOURNAL   J Cell Biol 152 (6), 1183-1196 (2001)
   PUBMED   11257119
REFERENCE   8  (residues 1 to 1244)
  AUTHORS   Noda,Y., Takeya,R., Ohno,S., Naito,S., Ito,T. and Sumimoto,H.
  TITLE     Human homologues of the Caenorhabditis elegans cell polarity
            protein PAR6 as an adaptor that links the small GTPases Rac and
            Cdc42 to atypical protein kinase C
  JOURNAL   Genes Cells 6 (2), 107-119 (2001)
   PUBMED   11260256
REFERENCE   9  (residues 1 to 1244)
  AUTHORS   Johansson,A., Driessens,M. and Aspenstrom,P.
  TITLE     The mammalian homologue of the Caenorhabditis elegans polarity
            protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
            Rac1
  JOURNAL   J Cell Sci 113 (Pt 18), 3267-3275 (2000)
   PUBMED   10954424
REFERENCE   10 (residues 1 to 1244)
  AUTHORS   Joberty,G., Petersen,C., Gao,L. and Macara,I.G.
  TITLE     The cell-polarity protein Par6 links Par3 and atypical protein
            kinase C to Cdc42
  JOURNAL   Nat Cell Biol 2 (8), 531-539 (2000)
   PUBMED   10934474
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450337.24, AL138768.23,
            AL360233.21, AL392123.12, AL390766.16 and AL160409.12.
            
            Summary: This gene encodes a member of the PARD protein family.
            PARD family members interact with other PARD family members and
            other proteins; they affect asymmetrical cell division and direct
            polarized cell growth. Multiple alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Oct 2011].
            
            Transcript Variant: This variant (8) lacks four alternate, in-frame
            segments and uses a different splice site, in the coding region,
            compared to variant 1. The resulting protein (isoform 8) is shorter
            when it is compared to isoform 1. This variant has also been called
            'variant e'.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB073671.1, AF467005.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.22-p11.21"
     Protein         1..1244
                     /product="partitioning defective 3 homolog isoform 8"
                     /note="partitioning defective 3 homolog; atypical PKC
                     isotype-specific interacting protein; PAR3-alpha; CTCL
                     tumor antigen se2-5; bazooka; par-3 partitioning defective
                     3 homolog; par-3 family cell polarity regulator alpha;
                     protein phosphatase 1, regulatory subunit 118"
                     /calculated_mol_wt=138201
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          224..320
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(239..245,260,263,293,297,300..301)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          411..503
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(426..432,447,450,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          527..626
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(543..549,565,568,598,602,605..606)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     CDS             1..1244
                     /gene="PARD3"
                     /gene_synonym="ASIP; Baz; PAR3; PAR3alpha; PARD-3; PARD3A;
                     PPP1R118; SE2-5L16; SE2-5LT1; SE2-5T2"
                     /coded_by="NM_001184791.2:302..4036"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS53509.1"
                     /db_xref="GeneID:56288"
                     /db_xref="HGNC:HGNC:16051"
                     /db_xref="MIM:606745"
ORIGIN      
        1 mkvtvcfgrt rvvvpcgdgh mkvfsliqqa vtryrkaiak dpnywiqvhr lehgdggild
       61 lddilcdvad dkdrlvavfd eqdphhggdg tsasstgtqs peifgselgt nnvsafqpyq
      121 atseievtps vlranmplhv rrssdpalig lstsvsdsnf sseepsrknp trwsttagfl
      181 kqntagspkt cdrkdedgte ednsrvepvg hadtglehip nfslddmvkl vevpndggpl
      241 gihvvpfsar ggrtlgllvk rlekggkaeh enlfrendci vrindgdlrn rrfeqaqhmf
      301 rqamrtpiiw fhvvpaanke qyeqlsqsek nnyyssrfsp dsqyidnrsv nsaglhtvqr
      361 aprlnhppeq idshsrlphs ahpsgkppsa pasapqnvfs ttvssgyntk kigkrlniql
      421 kkgteglgfs itsrdvtigg sapiyvknil prgaaiqdgr lkagdrliev ngvdlvgksq
      481 eevvsllrst kmegtvsllv frqedafhpr elkaedediv ltpdgtrefl tfevplndsg
      541 saglgvsvkg nrskenhadl gifvksiing gaaskdgrlr vndqliavng esllgktnqd
      601 ametlrrsms tegnkrgmiq livarriskc nelkspgspp gpelpietal ddrerrishs
      661 lysgieglde spsrnaalsr imgkyqlspt vnmpqddtvi ieddrlpvlp phlsdqssss
      721 shddvgfvta dagtwakaai sdsadcslsp dvdpvlafqr egfgrqsmse krtkqfsdas
      781 qldfvktrks ksmdlgssps rdvgpslglk ksssleslqt avaevtlngd ipfhrprpri
      841 irgrgcnesf raaidksydk pavddddegm etleedtees srsgresvst asdqpshsle
      901 rqmngnqekg dktdrkkdkt gkekkkdrdk ekdkmkakkg mlkglgdmfr iqaktrefre
      961 rqarerdyae iqdfhrtfgc ddelmyggvs syegsmalna rpqspreghm mdalyaqvkk
     1021 prnskpspvd snrstpsnhd riqrlrqefq qakqdedved rrrtysfeqp wpnarpatqs
     1081 grhsvsvevq mqrqrqeere ssqqaqrqys slprqsrkna ssvsqdsweq nyspgegfqs
     1141 akenpryssy qgsrngylgg hgfnarvmle tqellrqeqr rkeqqmkkqp psegpsnyds
     1201 ykkvqdpsya ppkgpfrqdv ppspsqvarl nrlqtpekgr pfys
//
LOCUS       NP_006487                354 aa            linear   PRI 20-NOV-2025
DEFINITION  guanine nucleotide-binding protein G(i) subunit alpha-3 [Homo
            sapiens].
ACCESSION   NP_006487
VERSION     NP_006487.1
DBSOURCE    REFSEQ: accession NM_006496.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Guo,L., Sun,H. and Pu,J.
  TITLE     GNAI3 mediated by Lin28A regulates lipopolysaccharide-induced
            inflammation and osteogenic differentiation in periodontal stem
            cells by mediating the NF-kappaB/NLRP3 inflammasome pathway
  JOURNAL   Arch Oral Biol 163, 105974 (2024)
   PUBMED   38636252
  REMARK    GeneRIF: GNAI3 mediated by Lin28A regulates
            lipopolysaccharide-induced inflammation and osteogenic
            differentiation in periodontal stem cells by mediating the
            NF-kappaB/NLRP3 inflammasome pathway.
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Duranti,C., Iorio,J., Bagni,G., Chioccioli Altadonna,G.,
            Fillion,T., Lulli,M., D'Alessandro,F.N., Montalbano,A.,
            Lastraioli,E., Fanelli,D., Coppola,S., Schmidt,T., Piazza,F.,
            Becchetti,A. and Arcangeli,A.
  TITLE     Integrins regulate hERG1 dynamics by girdin-dependent Galphai3:
            signaling and modeling in cancer cells
  JOURNAL   Life Sci Alliance 7 (1), e202302135 (2023)
   PUBMED   37923359
  REMARK    GeneRIF: Integrins regulate hERG1 dynamics by girdin-dependent
            Galphai3: signaling and modeling in cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Li,Y., Chai,J.L., Shi,X., Feng,Y., Li,J.J., Zhou,L.N., Cao,C. and
            Li,K.R.
  TITLE     Galphai1/3 mediate Netrin-1-CD146-activated signaling and
            angiogenesis
  JOURNAL   Theranostics 13 (7), 2319-2336 (2023)
   PUBMED   37153740
  REMARK    GeneRIF: Galphai1/3 mediate Netrin-1-CD146-activated signaling and
            angiogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Jiang,M., Pandey,S., Tran,V.T. and Fong,H.K.
  TITLE     Guanine nucleotide-binding regulatory proteins in retinal pigment
            epithelial cells
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3907-3911 (1991)
   PUBMED   1902575
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Carty,D.J., Padrell,E., Codina,J., Birnbaumer,L., Hildebrandt,J.D.
            and Iyengar,R.
  TITLE     Distinct guanine nucleotide binding and release properties of the
            three Gi proteins
  JOURNAL   J Biol Chem 265 (11), 6268-6273 (1990)
   PUBMED   2108158
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Codina,J., Olate,J., Abramowitz,J., Mattera,R., Cook,R.G. and
            Birnbaumer,L.
  TITLE     Alpha i-3 cDNA encodes the alpha subunit of Gk, the stimulatory G
            protein of receptor-regulated K+ channels
  JOURNAL   J Biol Chem 263 (14), 6746-6750 (1988)
   PUBMED   2452165
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Suki,W.N., Abramowitz,J., Mattera,R., Codina,J. and Birnbaumer,L.
  TITLE     The human genome encodes at least three non-allellic G proteins
            with alpha i-type subunits
  JOURNAL   FEBS Lett 220 (1), 187-192 (1987)
   PUBMED   2440724
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355310.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Guanine nucleotide-binding proteins (G proteins) are
            involved as modulators or transducers in various transmembrane
            signaling pathways. G proteins are composed of 3 units: alpha, beta
            and gamma. This gene encodes an alpha subunit and belongs to the
            G-alpha family. Mutation in this gene, resulting in a gly40-to-arg
            substitution, is associated with auriculocondylar syndrome, and
            shown to affect downstream targets in the G protein-coupled
            endothelin receptor pathway. [provided by RefSeq, Jun 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.156507.1,
                                           SRR1803617.43796.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369851.7/ ENSP00000358867.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..354
                     /product="guanine nucleotide-binding protein G(i) subunit
                     alpha-3"
                     /note="guanine nucleotide-binding protein G(k) subunit
                     alpha; g(i) alpha-3; guanine nucleotide binding protein (G
                     protein), alpha inhibiting activity polypeptide 3; guanine
                     nucleotide-binding protein G(i) subunit alpha;
                     heterotrimeric guanine nucleotide-binding protein 1A"
                     /calculated_mol_wt=40401
     Region          34..348
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          35..48
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P08754.3)"
     Site            order(40,45..47,181,200,203,269..270,272,325..326)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            40..47
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(41..43,71,75,79,82,85..86,104,107,149,178,203,211,
                     215)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          173..181
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P08754.3)"
     Site            176..184
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            181
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(182,184,186,197,199,203..205,207,210..211,213..216)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(184,209,212..213,216)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          196..205
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P08754.3)"
     Site            200..203
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            201..217
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          265..272
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P08754.3)"
     Site            269..272
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(317..328,330..333)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          324..329
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P08754.3)"
     Site            325..327
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..354
                     /gene="GNAI3"
                     /gene_synonym="87U6; ARCND1; ARCODS; HG1A"
                     /coded_by="NM_006496.4:107..1171"
                     /db_xref="CCDS:CCDS802.1"
                     /db_xref="GeneID:2773"
                     /db_xref="HGNC:HGNC:4387"
                     /db_xref="MIM:139370"
ORIGIN      
        1 mgctlsaedk aaverskmid rnlredgeka akevkllllg agesgkstiv kqmkiihedg
       61 ysedeckqyk vvvysntiqs iiaiiramgr lkidfgeaar addarqlfvl agsaeegvmt
      121 pelagvikrl wrdggvqacf srsreyqlnd sasyylndld risqsnyipt qqdvlrtrvk
      181 ttgivethft fkdlyfkmfd vggqrserkk wihcfegvta iifcvalsdy dlvlaedeem
      241 nrmhesmklf dsicnnkwft etsiilflnk kdlfeekikr splticypey tgsntyeeaa
      301 ayiqcqfedl nrrkdtkeiy thftcatdtk nvqfvfdavt dviiknnlke cgly
//
LOCUS       NP_054887                209 aa            linear   PRI 20-NOV-2025
DEFINITION  rRNA N(6)-adenosine-methyltransferase METTL5 [Homo sapiens].
ACCESSION   NP_054887
VERSION     NP_054887.2
DBSOURCE    REFSEQ: accession NM_014168.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Luo,M., Luo,X., Sun,J., Ao,X., Han,H. and Yang,X.
  TITLE     METTL5 enhances the mRNA stability of TPRKB through m6A
            modification to facilitate the aggressive phenotypes of
            hepatocellular carcinoma cell
  JOURNAL   Exp Cell Res 442 (1), 114219 (2024)
   PUBMED   39182664
  REMARK    GeneRIF: METTL5 enhances the mRNA stability of TPRKB through m[6]A
            modification to facilitate the aggressive phenotypes of
            hepatocellular carcinoma cell.
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Gong,S., Liu,H., Gou,H. and Sun,W.
  TITLE     METTL5: A Potential Biomarker for Nonsmall Cell Lung Cancer That
            Promotes Cancer Cell Proliferation by Interacting with IGF2BP3
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 311-321 (2024)
   PUBMED   39023781
  REMARK    GeneRIF: METTL5: A Potential Biomarker for Nonsmall Cell Lung
            Cancer That Promotes Cancer Cell Proliferation by Interacting with
            IGF2BP3.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Wu,J., Wang,L., Xi,S., Ma,C., Zou,F., Fang,G., Liu,F., Wang,X. and
            Qu,L.
  TITLE     Biological significance of METTL5 in atherosclerosis: comprehensive
            analysis of single-cell and bulk RNA sequencing data
  JOURNAL   Aging (Albany NY) 16 (8), 7267-7276 (2024)
   PUBMED   38663914
  REMARK    GeneRIF: Biological significance of METTL5 in atherosclerosis:
            comprehensive analysis of single-cell and bulk RNA sequencing data.
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Wang,Q., Huang,Y., Zhu,Y., Zhang,W., Wang,B., Du,X., Dai,Q.,
            Zhang,F. and Fang,Z.
  TITLE     The m6A methyltransferase METTL5 promotes neutrophil extracellular
            trap network release to regulate hepatocellular carcinoma
            progression
  JOURNAL   Cancer Med 13 (7), e7165 (2024)
   PUBMED   38613157
  REMARK    GeneRIF: The m6A methyltransferase METTL5 promotes neutrophil
            extracellular trap network release to regulate hepatocellular
            carcinoma progression.
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Xia,P., Zhang,H., Lu,H., Xu,K., Jiang,X., Jiang,Y., Gongye,X.,
            Chen,Z., Liu,J., Chen,X., Ma,W., Zhang,Z. and Yuan,Y.
  TITLE     METTL5 stabilizes c-Myc by facilitating USP5 translation to
            reprogram glucose metabolism and promote hepatocellular carcinoma
            progression
  JOURNAL   Cancer Commun (Lond) 43 (3), 338-364 (2023)
   PUBMED   36602428
  REMARK    GeneRIF: METTL5 stabilizes c-Myc by facilitating USP5 translation
            to reprogram glucose metabolism and promote hepatocellular
            carcinoma progression.
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Ignatova,V.V., Stolz,P., Kaiser,S., Gustafsson,T.H., Lastres,P.R.,
            Sanz-Moreno,A., Cho,Y.L., Amarie,O.V., Aguilar-Pimentel,A.,
            Klein-Rodewald,T., Calzada-Wack,J., Becker,L., Marschall,S.,
            Kraiger,M., Garrett,L., Seisenberger,C., Holter,S.M., Borland,K.,
            Van De Logt,E., Jansen,P.W.T.C., Baltissen,M.P., Valenta,M.,
            Vermeulen,M., Wurst,W., Gailus-Durner,V., Fuchs,H., Hrabe de
            Angelis,M., Rando,O.J., Kellner,S.M., Bultmann,S. and Schneider,R.
  TITLE     The rRNA m6A methyltransferase METTL5 is involved in pluripotency
            and developmental programs
  JOURNAL   Genes Dev 34 (9-10), 715-729 (2020)
   PUBMED   32217665
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Richard,E.M., Polla,D.L., Assir,M.Z., Contreras,M., Shahzad,M.,
            Khan,A.A., Razzaq,A., Akram,J., Tarar,M.N., Blanpied,T.A.,
            Ahmed,Z.M., Abou Jamra,R., Wieczorek,D., van Bokhoven,H.,
            Riazuddin,S. and Riazuddin,S.
  TITLE     Bi-allelic Variants in METTL5 Cause Autosomal-Recessive
            Intellectual Disability and Microcephaly
  JOURNAL   Am J Hum Genet 105 (4), 869-878 (2019)
   PUBMED   31564433
REFERENCE   9  (residues 1 to 209)
  AUTHORS   van Tran,N., Ernst,F.G.M., Hawley,B.R., Zorbas,C., Ulryck,N.,
            Hackert,P., Bohnsack,K.E., Bohnsack,M.T., Jaffrey,S.R., Graille,M.
            and Lafontaine,D.L.J.
  TITLE     The human 18S rRNA m6A methyltransferase METTL5 is stabilized by
            TRMT112
  JOURNAL   Nucleic Acids Res 47 (15), 7719-7733 (2019)
   PUBMED   31328227
  REMARK    GeneRIF: METTL5-TRMT112 partners act by extruding the adenosine to
            be modified from a double-stranded nucleic acid.
REFERENCE   10 (residues 1 to 209)
  AUTHORS   Mantz,J., De Brux,J.L., Pansard,Y., Barbier-Bohm,G., Desmonts,J.M.,
            Pernot,C. and Langlois,J.
  TITLE     [Syndrome of vagal hypertonia in a newborn infant manifested during
            the surgical repair of aortic coarctation associated with banding
            of the pulmonary artery]
  JOURNAL   Arch Mal Coeur Vaiss 80 (12), 1819-1822 (1987)
   PUBMED   3128227
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CA337169.1, AL523293.3 and BC000921.2.
            
            On Apr 19, 2006 this sequence version replaced NP_054887.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000921.2, SRR1803613.201062.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267766 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260953.10/ ENSP00000260953.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..209
                     /product="rRNA N(6)-adenosine-methyltransferase METTL5"
                     /note="methyltransferase-like protein 5; rRNA
                     N6-adenosine-methyltransferase METTL5; methyltransferase
                     like 5"
                     /calculated_mol_wt=23588
     Region          7..208
                     /region_name="COG2263"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:441864"
     CDS             1..209
                     /gene="METTL5"
                     /gene_synonym="HSPC133; MRT72"
                     /coded_by="NM_014168.4:309..938"
                     /db_xref="CCDS:CCDS33320.1"
                     /db_xref="GeneID:29081"
                     /db_xref="HGNC:HGNC:25006"
                     /db_xref="MIM:618628"
ORIGIN      
        1 mkkvrlkele srlqqvdgfe kpkllleqyp trphiaacml ytihntyddi enkvvadlgc
       61 gcgvlsigta mlgaglcvgf didedaleif nrnaeefelt nidmvqcdvc llsnrmsksf
      121 dtvimnppfg tknnkgtdma flktalemar tavyslhkss trehvqkkaa ewkikidiia
      181 elrydlpasy kfhkkksvdi evdlirfsf
//
LOCUS       NP_001035552             500 aa            linear   PRI 20-NOV-2025
DEFINITION  butyrophilin-like protein 8 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001035552
VERSION     NP_001035552.1
DBSOURCE    REFSEQ: accession NM_001040462.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Bobyn,A., Zarrei,M., Zhu,Y., Hoffman,M., Brenner,D., Resnick,A.C.,
            Scherer,S.W. and Gallo,M.
  TITLE     Ancestry and frequency of genetic variants in the general
            population are confounders in the characterization of germline
            variants linked to cancer
  JOURNAL   BMC Med Genet 21 (1), 92 (2020)
   PUBMED   32375678
  REMARK    GeneRIF: analysis of genomic information from multiple non-cancer
            cohorts showed that both the NEGR1 promoter deletion and the
            BTNL3-8 deletion were CNVs occurring at high frequencies in the
            general population. Intriguingly, the upstream NEGR1 CNV deletion
            was homozygous in ~ 40% of individuals in the non-cancer
            population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Vantourout,P., Laing,A., Woodward,M.J., Zlatareva,I., Apolonia,L.,
            Jones,A.W., Snijders,A.P., Malim,M.H. and Hayday,A.C.
  TITLE     Heteromeric interactions regulate butyrophilin (BTN) and BTN-like
            molecules governing gammadelta T cell biology
  JOURNAL   Proc Natl Acad Sci U S A 115 (5), 1039-1044 (2018)
   PUBMED   29339503
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Di Marco Barros,R., Roberts,N.A., Dart,R.J., Vantourout,P.,
            Jandke,A., Nussbaumer,O., Deban,L., Cipolat,S., Hart,R.,
            Iannitto,M.L., Laing,A., Spencer-Dene,B., East,P., Gibbons,D.,
            Irving,P.M., Pereira,P., Steinhoff,U. and Hayday,A.
  TITLE     Epithelia Use Butyrophilin-like Molecules to Shape Organ-Specific
            gammadelta T Cell Compartments
  JOURNAL   Cell 167 (1), 203-218 (2016)
   PUBMED   27641500
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Chapoval,A.I., Smithson,G., Brunick,L., Mesri,M., Boldog,F.L.,
            Andrew,D., Khramtsov,N.V., Feshchenko,E.A., Starling,G.C. and
            Mezes,P.S.
  TITLE     BTNL8, a butyrophilin-like molecule that costimulates the primary
            immune response
  JOURNAL   Mol Immunol 56 (4), 819-828 (2013)
   PUBMED   24036152
  REMARK    GeneRIF: Data suggest that butyrophilin-like molecule BTNL8 may
            play an essential role in priming of naive T lymphocytes.
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Ramani,S.R., Tom,I., Lewin-Koh,N., Wranik,B., Depalatis,L.,
            Zhang,J., Eaton,D. and Gonzalez,L.C.
  TITLE     A secreted protein microarray platform for extracellular protein
            interaction discovery
  JOURNAL   Anal Biochem 420 (2), 127-138 (2012)
   PUBMED   21982860
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY358523.1 and AK025111.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the middle portion of the coding region compared to variant 1,
            that results in a frameshift. It encodes isoform 2, previously
            known as the long form, which is longer and has a distinct
            C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358523.1, ERR279826.3309.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340184.9/ ENSP00000342197.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..500
                     /product="butyrophilin-like protein 8 isoform 2 precursor"
                     /note="butyrophilin-like protein 8; B7-H5 costimulatory
                     molecule"
                     /calculated_mol_wt=55020
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1746
     mat_peptide     18..500
                     /product="Butyrophilin-like protein 8. /id=PRO_0000014541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX41.1)"
                     /calculated_mol_wt=55020
     Region          19..132
                     /region_name="IgV_MOG_like"
                     /note="Immunoglobulin (Ig)-like domain of myelin
                     oligodendrocyte glycoprotein (MOG); cd05713"
                     /db_xref="CDD:409378"
     Region          19..42
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409378"
     Region          20..24
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409378"
     Region          27..31
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409378"
     Region          34..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409378"
     Region          43..51
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409378"
     Site            order(49..50,69,80,117..118,120..121,123..124)
                     /site_type="other"
                     /note="Fab binding site [polypeptide binding]"
                     /db_xref="CDD:409378"
     Region          51..56
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409378"
     Region          52..56
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          57..75
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409378"
     Region          61..69
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409378"
     Region          77..117
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          84..89
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409378"
     Region          95..103
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409378"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UX41.1)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409378"
     Region          118..120
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409378"
     Region          120..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409378"
     Region          121..132
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409378"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX41.1)"
     Region          289..460
                     /region_name="SPRY_PRY_C-I_1"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     (TRIM) proteins, including TRIM5, TRIM6, TRIM7, TRIM10,
                     TRIM11, TRIM17, TRIM20, TRIM21, TRIM27, TRIM35, TRIM38,
                     TRIM41, TRIM50, TRIM58, TRIM60, TRIM62, TRIM69, TRIM72,
                     NF7 and bloodthirsty; cd13733"
                     /db_xref="CDD:293968"
     Region          470..500
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UX41.1)"
     CDS             1..500
                     /gene="BTNL8"
                     /gene_synonym="BTN9.2"
                     /coded_by="NM_001040462.3:153..1655"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS43413.1"
                     /db_xref="GeneID:79908"
                     /db_xref="HGNC:HGNC:26131"
                     /db_xref="MIM:615606"
ORIGIN      
        1 malmlslvls llklgsgqwq vfgpdkpvqa lvgedaafsc flspktnaea mevrffrgqf
       61 ssvvhlyrdg kdqpfmqmpq yqgrtklvkd siaegrislr lenitvldag lygcrissqs
      121 yyqkaiwelq vsalgsvpli sitgyvdrdi qllcqssgwf prptakwkgp qgqdlstdsr
      181 tnrdmhglfd veisltvqen agsiscsmrh ahlsrevesr vqigdtffep iswhlatkvl
      241 gilccglffg ivglkiffsk fqwkiqaeld wrrkhgqael rdarkhavev tldpetahpk
      301 lcvsdlktvt hrkapqevph sekrftrksv vasqsfqagk hywevdgghn krwrvgvcrd
      361 dvdrrkeyvt lspdhgywvl rlngehlyft lnprfisvfp rtpptkigvf ldyecgtisf
      421 fnindqsliy tltcrfegll rpyieypsyn eqngtpivic pvtqesekea swqrasaipe
      481 tsnsesssqa ttpflprgem
//
LOCUS       NP_001307148            1028 aa            linear   PRI 20-NOV-2025
DEFINITION  U2 snRNP-associated SURP motif-containing protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001307148 XP_005247303
VERSION     NP_001307148.1
DBSOURCE    REFSEQ: accession NM_001320219.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Deng,L., Liao,L., Zhang,Y.L., Hu,S.Y., Yang,S.Y., Ma,X.Y.,
            Huang,M.Y., Zhang,F.L. and Li,D.Q.
  TITLE     MYC-driven U2SURP regulates alternative splicing of SAT1 to promote
            triple-negative breast cancer progression
  JOURNAL   Cancer Lett 560, 216124 (2023)
   PUBMED   36907504
  REMARK    GeneRIF: MYC-driven U2SURP regulates alternative splicing of SAT1
            to promote triple-negative breast cancer progression.
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   Wang,Q., Wang,Y., Liu,Y., Zhang,C., Luo,Y., Guo,R., Zhan,Z.,
            Wei,N., Xie,Z., Shen,L., Wu,G., Wu,W. and Feng,Y.
  TITLE     U2-related proteins CHERP and SR140 contribute to colorectal
            tumorigenesis via alternative splicing regulation
  JOURNAL   Int J Cancer 145 (10), 2728-2739 (2019)
   PUBMED   30977118
  REMARK    GeneRIF: Study observed that CHERP and its binding partner SR140
            are significantly upregulated in human clinical colorectal cancer
            tissues (CRC) and clarified how CHERP/SR140 exert an oncogenic role
            in CRC development partially through regulating expression of UPF3A
            variants.
REFERENCE   6  (residues 1 to 1028)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   7  (residues 1 to 1028)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 1028)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   9  (residues 1 to 1028)
  AUTHORS   Gilmore-Hebert,M., Ramabhadran,R. and Stern,D.F.
  TITLE     Interactions of ErbB4 and Kap1 connect the growth factor and DNA
            damage response pathways
  JOURNAL   Mol Cancer Res 8 (10), 1388-1398 (2010)
   PUBMED   20858735
REFERENCE   10 (residues 1 to 1028)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC111692.1, BC006474.1 and AC018450.26.
            
            On Feb 17, 2016 this sequence version replaced XP_005247303.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (2)
            has the same N- and C-termini but is 1 aa shorter compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2477496.1,
                                           SRR1803615.205647.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q23"
     Protein         1..1028
                     /product="U2 snRNP-associated SURP motif-containing
                     protein isoform 2"
                     /note="Ser/Arg-rich domain protein, 140 kDa; functional
                     spliceosome-associated protein a; U2-associated protein
                     SR140; U2-associated SR140 protein; U2 snRNP-associated
                     SURP motif-containing protein; 140 kDa Ser/Arg-rich domain
                     protein"
                     /calculated_mol_wt=118104
     Region          1..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Region          272..355
                     /region_name="RRM_SR140"
                     /note="RNA recognition motif (RRM) found in U2-associated
                     protein SR140 and similar proteins; cd12223"
                     /db_xref="CDD:409670"
     Region          428..479
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          429..472
                     /region_name="SURP motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Region          540..675
                     /region_name="RPR"
                     /note="domain present in proteins, which are involved in
                     regulation of nuclear pre-mRNA; smart00582"
                     /db_xref="CDD:214731"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            759
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Region          777..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Region          835..883
                     /region_name="cwf21_SR140"
                     /note="cwf21 domain found in U2-associated protein SR140
                     and similar proteins; cd21370"
                     /db_xref="CDD:410597"
     Region          854..1028
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15042.2)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15042.2)"
     CDS             1..1028
                     /gene="U2SURP"
                     /gene_synonym="fSAPa; SR140"
                     /coded_by="NM_001320219.2:60..3146"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23350"
                     /db_xref="HGNC:HGNC:30855"
                     /db_xref="MIM:617849"
ORIGIN      
        1 madktpggsq kassktrssd vhssgssdah mdasgpsdsd mpsrtrpksp rkhnyrnesa
       61 reslcdsphq nlsrpllenk lkafsigkms takrtlskke qeelkkkede kaaaeiyeef
      121 laafegsdgn kvktfvrggv vnaakeehet dekrgkiykp ssrfadqknp pnqssnerpp
      181 sllvietkkp plkkgekekk ksnlelfkee lkqiqeerde rhktkgrlsr feppqsdsdg
      241 qrrsmdapsr rnrssvlddy apgshdvgdp sttnlylgni npqmneemlc qefgrfgpla
      301 svkimwprtd eerarerncg fvafmnrrda eralknlngk mimsfemklg wgkavpipph
      361 piyippsmme htlppppsgl pfnaqprerl knpnapmlpp pknkedfekt lsqaivkvvi
      421 pternllali hrmiefvvre gpmfeamimn reinnpmfrf lfenqtpahv yyrwklysil
      481 qgdsptkwrt edfrmfkngs fwrppplnpy lhgmseeqet eafveepskk galkeeqrdk
      541 leeilrgltp rkndigdamv fclnnaeaae eivdcitesl silktplpkk iarlylvsdv
      601 lynssakvan asyyrkffet klcqifsdln atyrtiqghl qsenfkqrvm tcfrawedwa
      661 iypepflikl qniflglvni ieeketedvp ddldgapiee eldgapledv dgipidatpi
      721 ddldgvpiks ldddldgvpl datedskkne pifkvapskw eavdeselea qavttskwel
      781 fdqheeseee enqnqeeese deedtqssks eehhlysnpi keemteskfs kysemseekr
      841 aklreielkv mkfqdelesg krpkkpgqsf qeqvehyrdk llqrekekel erererdkkd
      901 keklesrskd kkekdectpt rkerkrrhst spspsrsssg rrvkspspks ersersersh
      961 kessrsrssh kdsprdvskk akrspsgsrt pkrsrrsrsr spkksgkksr sqsrsphrsh
     1021 kkskknkh
//
LOCUS       NP_003040                349 aa            linear   PRI 20-NOV-2025
DEFINITION  hepatic sodium/bile acid cotransporter [Homo sapiens].
ACCESSION   NP_003040
VERSION     NP_003040.1
DBSOURCE    REFSEQ: accession NM_003049.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Ibrahim,M.K., Liu,C.-D., Zhang,L., Yu,X., Kim,E.S., Liu,Z., Jo,S.,
            Liu,Y., Huang,Y., Gao,S.-J. and Guo,H.
  TITLE     The loss of hepatitis B virus receptor NTCP/SLC10A1 in human liver
            cancer cells is due to epigenetic silencing
  JOURNAL   J Virol 98 (10), e0118724 (2024)
   PUBMED   39297647
  REMARK    GeneRIF: The loss of hepatitis B virus receptor NTCP/SLC10A1 in
            human liver cancer cells is due to epigenetic silencing.
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Ko,Y.L., Tuan,W.L., Teng,M.S., Su,W.C., Wang,C.C., Er,L.K., Wu,S.
            and Hsu,L.A.
  TITLE     SLC10A1 rs2296651 variant (S267F mutation) predicts biochemical
            traits, hepatitis B virus infection susceptibility and the risk of
            gallstone disease
  JOURNAL   Mol Genet Genomics 299 (1), 62 (2024)
   PUBMED   38869622
  REMARK    GeneRIF: SLC10A1 rs2296651 variant (S267F mutation) predicts
            biochemical traits, hepatitis B virus infection susceptibility and
            the risk of gallstone disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Xu,Z.M., Gnouamozi,G.E., Rueger,S., Shea,P.R., Buti,M., Chan,H.L.,
            Marcellin,P., Lawless,D., Naret,O., Zeller,M., Schneuing,A.,
            Scheck,A., Junier,T., Moradpour,D., Podlaha,O., Suri,V., Gaggar,A.,
            Subramanian,M., Correia,B., Gfeller,D., Urban,S. and Fellay,J.
  TITLE     Joint host-pathogen genomic analysis identifies hepatitis B virus
            mutations associated with human NTCP and HLA class I variation
  JOURNAL   Am J Hum Genet 111 (6), 1018-1034 (2024)
   PUBMED   38749427
  REMARK    GeneRIF: Joint host-pathogen genomic analysis identifies hepatitis
            B virus mutations associated with human NTCP and HLA class I
            variation.
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Jung,D., Hagenbuch,B., Fried,M., Meier,P.J. and Kullak-Ublick,G.A.
  TITLE     Role of liver-enriched transcription factors and nuclear receptors
            in regulating the human, mouse, and rat NTCP gene
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 286 (5), G752-G761 (2004)
   PUBMED   14701722
  REMARK    GeneRIF: Conserved NTCP/Ntcp 5'-regulatory region transcription
            regulation differs among species and is not directly regulated by
            small heterodimer partner. Bile acids may regulate NTCP/Ntcp
            indirectly by modulating nuclear factor regulation of gene
            expression.
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Ho,R.H., Leake,B.F., Roberts,R.L., Lee,W. and Kim,R.B.
  TITLE     Ethnicity-dependent polymorphism in Na+-taurocholate cotransporting
            polypeptide (SLC10A1) reveals a domain critical for bile acid
            substrate recognition
  JOURNAL   J Biol Chem 279 (8), 7213-7222 (2004)
   PUBMED   14660639
  REMARK    GeneRIF: a domain critical for bile acid substrate recognition of
            SLC10A1 has an ethnicity-dependent polymorphism
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Trauner,M. and Boyer,J.L.
  TITLE     Bile salt transporters: molecular characterization, function, and
            regulation
  JOURNAL   Physiol Rev 83 (2), 633-671 (2003)
   PUBMED   12663868
  REMARK    Review article
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Hallen,S., Mareninova,O., Branden,M. and Sachs,G.
  TITLE     Organization of the membrane domain of the human liver sodium/bile
            acid cotransporter
  JOURNAL   Biochemistry 41 (23), 7253-7266 (2002)
   PUBMED   12044156
  REMARK    GeneRIF: Translation/insertion scanning, alanine insertion, and
            glycosylation site mutagenesis studies of liver sodium/bile acid
            cotransporter support a topography with nine membrane-spanning or
            membrane-associated segments.
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Shiao,T., Iwahashi,M., Fortune,J., Quattrochi,L., Bowman,S.,
            Wick,M., Qadri,I. and Simon,F.R.
  TITLE     Structural and functional characterization of liver cell-specific
            activity of the human sodium/taurocholate cotransporter
  JOURNAL   Genomics 69 (2), 203-213 (2000)
   PUBMED   11031103
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Hagenbuch,B. and Meier,P.J.
  TITLE     Molecular cloning, chromosomal localization, and functional
            characterization of a human liver Na+/bile acid cotransporter
  JOURNAL   J Clin Invest 93 (3), 1326-1331 (1994)
   PUBMED   8132774
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314028.1, BC069799.1,
            L21893.1 and AL157789.6.
            
            Summary: The protein encoded by this gene belongs to the
            sodium/bile acid cotransporter family, which are integral membrane
            glycoproteins that participate in the enterohepatic circulation of
            bile acids. Two homologous transporters are involved in the
            reabsorption of bile acids; the ileal sodium/bile acid
            cotransporter with an apical cell localization that absorbs bile
            acids from the intestinal lumen, bile duct and kidney, and the
            liver-specific sodium/bile acid cotransporter, represented by this
            protein, that is found in the basolateral membranes of hepatocytes.
            Bile acids are the catabolic product of cholesterol metabolism,
            hence this protein is important for cholesterol homeostasis.
            [provided by RefSeq, Oct 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.103981.1,
                                           SRR5189664.104510.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216540.5/ ENSP00000216540.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..349
                     /product="hepatic sodium/bile acid cotransporter"
                     /note="sodium/taurocholate cotransporter; Na/taurocholate
                     cotransporting polypeptide; growth-inhibiting protein 29;
                     sodium/bile acid cotransporter; cell growth-inhibiting
                     gene 29 protein; sodium/taurocholate cotransporting
                     polypeptide; Na(+)/bile acid cotransporter;
                     Na(+)/taurocholate transport protein; solute carrier
                     family 10 (sodium/bile acid cotransporter), member 1;
                     solute carrier family 10 (sodium/bile acid cotransporter
                     family), member 1"
                     /calculated_mol_wt=37988
     Site            5
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14973.1)"
     Site            11
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14973.1)"
     Region          22..311
                     /region_name="bass"
                     /note="bile acid transporter; TIGR00841"
                     /db_xref="CDD:188087"
     Site            23..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            48..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            87..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            116..142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            157..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            184..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            220..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            248..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     Site            281..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14973.1)"
     CDS             1..349
                     /gene="SLC10A1"
                     /gene_synonym="FHCA2; NTCP"
                     /coded_by="NM_003049.4:87..1136"
                     /db_xref="CCDS:CCDS9797.1"
                     /db_xref="GeneID:6554"
                     /db_xref="HGNC:HGNC:10905"
                     /db_xref="MIM:182396"
ORIGIN      
        1 meahnasapf nftlppnfgk rptdlalsvi lvfmlffiml slgctmefsk ikahlwkpkg
       61 laialvaqyg impltafvlg kvfrlkniea lailvcgcsp ggnlsnvfsl amkgdmnlsi
      121 vmttcstfca lgmmplllyi ysrgiydgdl kdkvpykgiv islvlvlipc tigivlkskr
      181 pqymryvikg gmiiillcsv avtvlsainv gksimfamtp lliatsslmp figfllgyvl
      241 salfclngrc rrtvsmetgc qnvqlcstil nvafppevig plfffpllym ifqlgeglll
      301 iaifwcyekf ktpkdktkmi ytaatteeti pgalgngtyk gedcspcta
//
LOCUS       NP_061141                944 aa            linear   PRI 20-NOV-2025
DEFINITION  protein unc-45 homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_061141
VERSION     NP_061141.2
DBSOURCE    REFSEQ: accession NM_018671.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 944)
  AUTHORS   Waich,S., Kreidl,K., Vodopiutz,J., Demir,A.M., Pollio,A.R.,
            Dostal,V., Pfaller,K., Parlato,M., Cerf-Bensussan,N., Adam,R.,
            Vogel,G.F., Uhlig,H.H., Ruemmele,F.M., Muller,T., Hess,M.W.,
            Janecke,A.R., Huber,L.A. and Valovka,T.
  TITLE     Altered chaperone-nonmuscle myosin II interactions drive
            pathogenicity of the UNC45A c.710T>C variant in
            osteo-oto-hepato-enteric syndrome
  JOURNAL   JCI Insight 10 (6), e185508 (2025)
   PUBMED   40125554
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 944)
  AUTHORS   Almaas,R., Atneosen-Asegg,M., Ytre-Arne,M.E., Melheim,M.,
            Sorte,H.S., Cizkova,D., Reims,H.M., Bezrouk,A., Harrison,S.P.,
            Strand,J., Hermansen,J.U., Andersen,S.S., Eiklid,K.L., Mokry,J.,
            Sullivan,G.J. and Stray-Pedersen,A.
  TITLE     Aagenaes syndrome/lymphedema cholestasis syndrome 1 is caused by a
            founder variant in the 5'-untranslated region of UNC45A
  JOURNAL   J Hepatol 79 (4), 945-954 (2023)
   PUBMED   37328071
  REMARK    GeneRIF: Aagenaes syndrome/lymphedema cholestasis syndrome 1 is
            caused by a founder variant in the 5'-untranslated region of
            UNC45A.
REFERENCE   3  (residues 1 to 944)
  AUTHORS   Duclaux-Loras,R., Lebreton,C., Berthelet,J., Charbit-Henrion,F.,
            Nicolle,O., Revenu des Courtils,C., Waich,S., Valovka,T., Khiat,A.,
            Rabant,M., Racine,C., Guerrera,I.C., Baptista,J., Mahe,M.M.,
            Hess,M.W., Durel,B., Lefort,N., Banal,C., Parisot,M., Talbotec,C.,
            Lacaille,F., Ecochard-Dugelay,E., Demir,A.M., Vogel,G.F.,
            Faivre,L., Rodrigues,A., Fowler,D., Janecke,A.R., Muller,T.,
            Huber,L.A., Rodrigues-Lima,F., Ruemmele,F.M., Uhlig,H.H., Del
            Bene,F., Michaux,G., Cerf-Bensussan,N. and Parlato,M.
  TITLE     UNC45A deficiency causes microvillus inclusion disease-like
            phenotype by impairing myosin VB-dependent apical trafficking
  JOURNAL   J Clin Invest 132 (10) (2022)
   PUBMED   35575086
  REMARK    GeneRIF: UNC45A deficiency causes microvillus inclusion
            disease-like phenotype by impairing myosin VB-dependent apical
            trafficking.
REFERENCE   4  (residues 1 to 944)
  AUTHORS   Lechuga,S., Cartagena-Rivera,A.X., Khan,A., Crawford,B.I.,
            Narayanan,V., Conway,D.E., Lehtimaki,J., Lappalainen,P., Rieder,F.,
            Longworth,M.S. and Ivanov,A.I.
  TITLE     A myosin chaperone, UNC-45A, is a novel regulator of intestinal
            epithelial barrier integrity and repair
  JOURNAL   FASEB J 36 (5), e22290 (2022)
   PUBMED   35344227
  REMARK    GeneRIF: A myosin chaperone, UNC-45A, is a novel regulator of
            intestinal epithelial barrier integrity and repair.
REFERENCE   5  (residues 1 to 944)
  AUTHORS   Li,Q., Zhou,Z., Sun,Y., Sun,C., Klappe,K. and van IJzendoorn,S.C.D.
  TITLE     A Functional Relationship Between UNC45A and MYO5B Connects Two
            Rare Diseases With Shared Enteropathy
  JOURNAL   Cell Mol Gastroenterol Hepatol 14 (2), 295-310 (2022)
   PUBMED   35421597
  REMARK    GeneRIF: A Functional Relationship Between UNC45A and MYO5B
            Connects Two Rare Diseases With Shared Enteropathy.
REFERENCE   6  (residues 1 to 944)
  AUTHORS   Chadli,A., Felts,S.J. and Toft,D.O.
  TITLE     GCUNC45 is the first Hsp90 co-chaperone to show alpha/beta isoform
            specificity
  JOURNAL   J Biol Chem 283 (15), 9509-9512 (2008)
   PUBMED   18285346
  REMARK    GeneRIF: GCUNC45 is required for the normal cellular distribution
            of Hsp90beta, but not Hsp90alpha.
REFERENCE   7  (residues 1 to 944)
  AUTHORS   Bazzaro,M., Santillan,A., Lin,Z., Tang,T., Lee,M.K., Bristow,R.E.,
            Shih,Ie.M. and Roden,R.B.
  TITLE     Myosin II co-chaperone general cell UNC-45 overexpression is
            associated with ovarian cancer, rapid proliferation, and motility
  JOURNAL   Am J Pathol 171 (5), 1640-1649 (2007)
   PUBMED   17872978
  REMARK    GeneRIF: elevated GC UNC-45 protein expression in ovarian carcinoma
            proliferation and metastasis.
REFERENCE   8  (residues 1 to 944)
  AUTHORS   Chadli,A., Graham,J.D., Abel,M.G., Jackson,T.A., Gordon,D.F.,
            Wood,W.M., Felts,S.J., Horwitz,K.B. and Toft,D.
  TITLE     GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
            chaperoning pathway
  JOURNAL   Mol Cell Biol 26 (5), 1722-1730 (2006)
   PUBMED   16478993
  REMARK    GeneRIF: GCUNC-45 is a novel modulator of progesterone receptor
            chaperoning by hsp90.
REFERENCE   9  (residues 1 to 944)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   10 (residues 1 to 944)
  AUTHORS   Price,M.G., Landsverk,M.L., Barral,J.M. and Epstein,H.F.
  TITLE     Two mammalian UNC-45 isoforms are related to distinct cytoskeletal
            and muscle-specific functions
  JOURNAL   J Cell Sci 115 (Pt 21), 4013-4023 (2002)
   PUBMED   12356907
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC382051.1, AB014736.1 and
            BC006214.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 10, 2003 this sequence version replaced NP_061141.1.
            
            Summary: This gene encodes a regulatory component of the
            progesterone receptor/heat shock protein 90 chaperoning complex,
            which functions in the assembly and folding of the progesterone
            receptor. The encoded protein is thought to be essential for normal
            cell proliferation, and for the accumulation of myosin during
            development of muscle cells. [provided by RefSeq, Sep 2018].
            
            Transcript Variant: This variant (2) encodes the longer isoform
            (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.58861.1, BC006214.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000418476.2/ ENSP00000407487.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..944
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..944
                     /product="protein unc-45 homolog A isoform 2"
                     /note="general cell UNC45; protein unc-45 homolog A;
                     smooth muscle cell associated protein-1"
                     /calculated_mol_wt=102946
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Region          21..54
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Region          21..49
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(22,25..26,29..30,32,59,62..63,66..67,69..70,93,
                     96..97,100..101,104)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          <28..>125
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          57..87
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          58..91
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Region          92..125
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Region          92..120
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          363..505
                     /region_name="UNC45-central"
                     /note="Myosin-binding striated muscle assembly central;
                     pfam11701"
                     /db_xref="CDD:432011"
     Site            483
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H3U1.1)"
     Site            order(751,755,759,793,797,801,836,840)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          768..803
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          806..842
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..944
                     /gene="UNC45A"
                     /gene_synonym="GC-UNC45; GCUNC-45; GCUNC45; IRO039700;
                     OOHE; SMAP-1; SMAP1; UNC-45A"
                     /coded_by="NM_018671.5:41..2875"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10367.1"
                     /db_xref="GeneID:55898"
                     /db_xref="HGNC:HGNC:30594"
                     /db_xref="MIM:611219"
ORIGIN      
        1 mtvsgpgtpe prpatpgass veqlrkegne lfkcgdygga laaytqalgl datpqdqavl
       61 hrnraachlk ledydkaete askaiekdgg dvkalyrrsq aleklgrldq avldlqrcvs
      121 lepknkvfqe alrniggqiq ekvrymsstd akveqmfqil ldpeekgtek kqkasqnlvv
      181 laredagaek ifrsngvqll qrlldmgetd lmlaalrtlv gicsehqsrt vatlsilgtr
      241 rvvsilgves qavslaachl lqvmfdalke gvkkgfrgke gaiivdpare lkvlisnlld
      301 lltevgvsgq grdnaltlli kavprkslkd pnnsltlwvi dqglkkilev ggslqdppge
      361 lavtansrms asillsklfd dlkcdaeren fhrlcenyik swfegqglag klraiqtvsc
      421 llqgpcdagn ralelsgvme svialcaseq eeeqlvavea lihaagkakr asfitangvs
      481 llkdlykcse kdsiriralv glcklgsagg tdfsmkqfae gstlklakqc rkwlcndqid
      541 agtrrwaveg layltfdadv keefvedaaa lkalfqlsrl eersvlfava salvnctnsy
      601 dyeepdpkmv elakyakqhv peqhpkdkps fvrarvkkll aagvvsamvc mvktespvlt
      661 sscrellsrv flalveeved rgtvvaqggg raliplaleg tdvgqtkaaq alakltitsn
      721 pemtfpgeri yevvrplvsl lhlncsglqn fealmaltnl agiserlrqk ilkekavpmi
      781 egymfeehem irraatecmc nlamskevqd lfeaqgndrl kllvlysged dellqraaag
      841 glamltsmrp tlcsripqvt thwleilqal llssnqelqh rgavvvlnmv easreiastl
      901 mesemmeils vlakgdhspv traaaacldk aveygliqpn qdge
//
LOCUS       NP_001005408            1560 aa            linear   PRI 20-NOV-2025
DEFINITION  neuralized-like protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001005408
VERSION     NP_001005408.1
DBSOURCE    REFSEQ: accession NM_001005408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1560)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1560)
  AUTHORS   Cardamone,M.D., Gao,Y., Kwan,J., Hayashi,V., Sheeran,M., Xu,J.,
            English,J., Orofino,J., Emili,A. and Perissi,V.
  TITLE     Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of
            mitochondrial proteins
  JOURNAL   J Cell Biol 221 (3) (2022)
   PUBMED   35157000
  REMARK    GeneRIF: Neuralized-like protein 4 (NEURL4) mediates
            ADP-ribosylation of mitochondrial proteins.
REFERENCE   3  (residues 1 to 1560)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1560)
  AUTHORS   Loukil,A., Tormanen,K. and Sutterlin,C.
  TITLE     The daughter centriole controls ciliogenesis by regulating Neurl-4
            localization at the centrosome
  JOURNAL   J Cell Biol 216 (5), 1287-1300 (2017)
   PUBMED   28385950
  REMARK    GeneRIF: The data support a model in which the daughter centriole
            promotes ciliogenesis through Neurl-4-dependent regulation of CP110
            levels at the mother centriole.
REFERENCE   5  (residues 1 to 1560)
  AUTHORS   Li,J., Kim,S., Kobayashi,T., Liang,F.X., Korzeniewski,N.,
            Duensing,S. and Dynlacht,B.D.
  TITLE     Neurl4, a novel daughter centriole protein, prevents formation of
            ectopic microtubule organizing centres
  JOURNAL   EMBO Rep 13 (6), 547-553 (2012)
   PUBMED   22441691
  REMARK    GeneRIF: Neurl4 counteracts accumulation of CP110, thereby
            maintaining normal centriolar homeostasis and preventing formation
            of ectopic microtubular organizing centres
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1560)
  AUTHORS   Al-Hakim,A.K., Bashkurov,M., Gingras,A.C., Durocher,D. and
            Pelletier,L.
  TITLE     Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2
            as novel modulators of centrosome architecture
  JOURNAL   Mol Cell Proteomics 11 (6), M111.014233 (2012)
   PUBMED   22261722
  REMARK    GeneRIF: the NEURL4-HERC2 complex participates in the
            ubiquitin-dependent regulation of centrosome architecture
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026954.14, AB058690.1 and AL136870.1.
            
            Summary: The protein encoded by this gene is predicted and it
            includes two isoforms resulting from two alternatively spliced
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame 6-nt segment
            in the coding region, as compared to variant 1. The encoded isoform
            2 is thus slightly shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1560
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1560
                     /product="neuralized-like protein 4 isoform 2"
                     /note="neuralized-like protein 4; neuralized homolog 4"
                     /calculated_mol_wt=166591
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          43..205
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          207..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          320..482
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          523..684
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          691..716
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          718..880
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          913..1082
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          1084..1121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          1131..1290
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     CDS             1..1560
                     /gene="NEURL4"
                     /coded_by="NM_001005408.2:24..4706"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42252.1"
                     /db_xref="GeneID:84461"
                     /db_xref="HGNC:HGNC:34410"
                     /db_xref="MIM:615865"
ORIGIN      
        1 maagsggsgg sgggpgpgpg ggggpsgsgs gpgsngglgs ggelhprtgr lvslsacgrt
       61 arrqqpgqef nhglvlsrep lrdgrvftvr idrkvnswsg sieigvtald psvldfpssa
      121 tglkggswvv sgcsvlrdgr svleeygqdl dqlgegdrvg vertvagelr lwvngrdcgv
      181 aatglpprvw avvdlygkct qitvlppepg fspptpiptp pleplapted salaeqgtsa
      241 deafmvspaq arpetfpnsl eshndfanme lsevvsntil saynggllnv nlssppageg
      301 lgssgaatsp iltsndallf hekcgtlikl snnnktaerr rpldefnngv vmtnrplrdn
      361 emfeiridkl vdkwsgsiei gvtthnpnsl eypatmtnlq sgtimmsgcg iltngkgtrr
      421 eycefsldel qegdhigltr ksnsalhffi ngidqgvatp ltppvvygvv dlygmavkvt
      481 ivhnnnhsdr lrrnnailra lspegalrra apaaqaeper llfhpncgqk aaithegrta
      541 lrphatddfn hgvvlssral rdgevfqvri dkmvdkwags ieigvtthnp aylqlpstmt
      601 nlrsgtwmmt gngvmhngtt ildeyghnld rlkagdtvgv vrredgtlhf fvngmtqgpa
      661 awnvppgvya vvdlygqaaq ativddveva pvpeplpegn nqvspsspss gaggsdlrfh
      721 qlhgsnavit nggrtalrhn crsefndaiv isnralrdge lfeiviqkmv drwsgsieag
      781 vtairpedle fpntmtdidy dtwmlsgtai mqdgntmrnn ygcdldalgt garigmmrta
      841 kgdlhyfing qdqgaacsgl ppevyavvdl ygqcvqvsit natgpmdnsl atsntateks
      901 fplhspvagv ahrfhstcgk nvtleedgtr avraagyahg lvfstkelra eevfevkvee
      961 ldekwagslr lglttlapge mgpgaggggp glppslpelr tkttwmvssc evrrdgqlqr
     1021 mnygrnlerl gvgsrvgvrr gaddtmhilv dgedmgpaat giaknvwavl dlygpvrgvs
     1081 ivsstrlees egtqppspss dtgsegeedd egeehglggq nevgiipttl eflenhgkni
     1141 llsngnrtat rvasynqgiv vinqplvpql lvqvridfln rqwtsslvlg vitcaperln
     1201 fpasacalkr aawllrgrgv fhnglkicek fgpnldtcpe gtilglrlds sgglhlhvng
     1261 vdqgvavpdv pqpchalvdl ygqceqvtiv npepgaasgk sagtqgdmek admvdgikes
     1321 vcwgpppaas plksceyhal csrfqellll pedyfmpppk rslcycescr klrgdeahrr
     1381 rgeppreyal pfgwcrfnlr vnprleagtl tkkwhmayhg snvaavrrvl drgelgagta
     1441 silscrplkg epgvgfeepg encappreeq pppvllspsl qyagaetlas kvqfrdpksq
     1501 rthqaqvafq vcvrpgsytp gppsaalgep pdphfspael ewvtkekgat llcallvrve
//
LOCUS       NP_001287751             114 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger CCHC domain-containing protein 10 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001287751 XP_005272084
VERSION     NP_001287751.1
DBSOURCE    REFSEQ: accession NM_001300822.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Ohira,T., Kojima,H., Kuroda,Y., Aoki,S., Inaoka,D., Osaki,M.,
            Wanibuchi,H., Okada,F., Oshimura,M. and Kugoh,H.
  TITLE     PITX1 protein interacts with ZCCHC10 to regulate hTERT mRNA
            transcription
  JOURNAL   PLoS One 14 (8), e0217605 (2019)
   PUBMED   31404068
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Ning,Y., Hui,N., Qing,B., Zhuo,Y., Sun,W., Du,Y., Liu,S., Liu,K.
            and Zhou,J.
  TITLE     ZCCHC10 suppresses lung cancer progression and cisplatin resistance
            by attenuating MDM2-mediated p53 ubiquitination and degradation
  JOURNAL   Cell Death Dis 10 (6), 414 (2019)
   PUBMED   31138778
  REMARK    GeneRIF: ZCCHC10 exerts its tumor-suppressive effects by
            stabilizing the p53 protein and can be used a potential prognostic
            marker and therapeutic target in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Yu,X., Noll,R.R., Romero Duenas,B.P., Allgood,S.C., Barker,K.,
            Caplan,J.L., Machner,M.P., LaBaer,J., Qiu,J. and Neunuebel,M.R.
  TITLE     Legionella effector AnkX interacts with host nuclear protein
            PLEKHN1
  JOURNAL   BMC Microbiol 18 (1), 5 (2018)
   PUBMED   29433439
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK300543.1, CB112418.1, BC022443.1 and AK000101.1.
            
            On Jul 15, 2014 this sequence version replaced XP_005272084.1.
            
            Transcript Variant: This variant (6) uses an alternate splice site
            that results in a frameshift in the 3' coding region, compared to
            variant 1, resulting in an isoform (6) that has a distinct
            C-terminus and is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380200.20363.11,
                                           SRR1660809.164457.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..114
                     /product="zinc finger CCHC domain-containing protein 10
                     isoform 6"
                     /note="zinc finger CCHC domain-containing protein 10; zinc
                     finger, CCHC domain containing 10"
                     /calculated_mol_wt=13672
     Region          39..76
                     /region_name="zf-CCHC_3"
                     /note="Zinc knuckle; pfam13917"
                     /db_xref="CDD:404753"
     CDS             1..114
                     /gene="ZCCHC10"
                     /coded_by="NM_001300822.3:13..357"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS75302.1"
                     /db_xref="GeneID:54819"
                     /db_xref="HGNC:HGNC:25954"
ORIGIN      
        1 matpmhrlia rrqafdtelq pvktfwiliq psiviseank qhvrcqkcle fghwtyectg
       61 krkylhrpsr taelkkalke kenrlllqqr sffpprvyqh wrnqcrkkgq ekkv
//
LOCUS       NP_775816                511 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin and PNK-like factor [Homo sapiens].
ACCESSION   NP_775816
VERSION     NP_775816.1
DBSOURCE    REFSEQ: accession NM_173545.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 511)
  AUTHORS   London,R.E.
  TITLE     XRCC1 - Strategies for coordinating and assembling a versatile DNA
            damage response
  JOURNAL   DNA Repair (Amst) 93, 102917 (2020)
   PUBMED   33087283
  REMARK    Review article
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Richter,C., Marquardt,S., Li,F., Spitschak,A., Murr,N.,
            Edelhauser,B.A.H., Iliakis,G., Putzer,B.M. and Logotheti,S.
  TITLE     Rewiring E2F1 with classical NHEJ via APLF suppression promotes
            bladder cancer invasiveness
  JOURNAL   J Exp Clin Cancer Res 38 (1), 292 (2019)
   PUBMED   31287003
  REMARK    GeneRIF: MIR888-dependent inhibition of APLF by E2F1 was
            demonstrated using overexpression and knockdown experiments, in
            combination with luciferase assays.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Nemoz,C., Ropars,V., Frit,P., Gontier,A., Drevet,P., Yu,J.,
            Guerois,R., Pitois,A., Comte,A., Delteil,C., Barboule,N.,
            Legrand,P., Baconnais,S., Yin,Y., Tadi,S., Barbet-Massin,E.,
            Berger,I., Le Cam,E., Modesti,M., Rothenberg,E., Calsou,P. and
            Charbonnier,J.B.
  TITLE     XLF and APLF bind Ku80 at two remote sites to ensure DNA repair by
            non-homologous end joining
  JOURNAL   Nat Struct Mol Biol 25 (10), 971-980 (2018)
   PUBMED   30291363
  REMARK    GeneRIF: The crystal structures of the Ku-binding motifs (KBM) of
            the non-homologous end joining (NHEJ) proteins APLF (A-KBM) and XLF
            (X-KBM) bound to a Ku-DNA complex are discussed.
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Macrae,C.J., McCulloch,R.D., Ylanko,J., Durocher,D. and Koch,C.A.
  TITLE     APLF (C2orf13) facilitates nonhomologous end-joining and undergoes
            ATM-dependent hyperphosphorylation following ionizing radiation
  JOURNAL   DNA Repair (Amst) 7 (2), 292-302 (2008)
   PUBMED   18077224
  REMARK    GeneRIF: APLF is an ATM target that is involved in nonhomologous
            end-joining and facilitates double-strand break repair, likely via
            interactions with Ku and XRCC4-DNA ligase IV.
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Ahel,I., Ahel,D., Matsusaka,T., Clark,A.J., Pines,J., Boulton,S.J.
            and West,S.C.
  TITLE     Poly(ADP-ribose)-binding zinc finger motifs in DNA
            repair/checkpoint proteins
  JOURNAL   Nature 451 (7174), 81-85 (2008)
   PUBMED   18172500
  REMARK    GeneRIF: interaction of poly(ADP-ribose) with a PBZ motif in two
            representative human proteins, APLF (aprataxin PNK-like factor) and
            CHFR (checkpoint protein with FHA and RING domains)
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Bekker-Jensen,S., Fugger,K., Danielsen,J.R., Gromova,I.,
            Sehested,M., Celis,J., Bartek,J., Lukas,J. and Mailand,N.
  TITLE     Human Xip1 (C2orf13) is a novel regulator of cellular responses to
            DNA strand breaks
  JOURNAL   J Biol Chem 282 (27), 19638-19643 (2007)
   PUBMED   17507382
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Iles,N., Rulten,S., El-Khamisy,S.F. and Caldecott,K.W.
  TITLE     APLF (C2orf13) is a novel human protein involved in the cellular
            response to chromosomal DNA strand breaks
  JOURNAL   Mol Cell Biol 27 (10), 3793-3803 (2007)
   PUBMED   17353262
  REMARK    GeneRIF: These data identify APLF as a novel component of the
            cellular response to DNA strand breaks in human cells.
            Erratum:[Mol Cell Biol. 2008 May;28(10):3561]
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Kanno,S., Kuzuoka,H., Sasao,S., Hong,Z., Lan,L., Nakajima,S. and
            Yasui,A.
  TITLE     A novel human AP endonuclease with conserved zinc-finger-like
            motifs involved in DNA strand break responses
  JOURNAL   EMBO J 26 (8), 2094-2103 (2007)
   PUBMED   17396150
  REMARK    GeneRIF: PALF is novel human AP endonuclease with conserved
            zinc-finger-like motifs involved in DNA strand break responses.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA641644.1 and BC041144.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041144.1, SRR1660809.68342.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303795.9/ ENSP00000307004.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..511
                     /product="aprataxin and PNK-like factor"
                     /EC_number="4.2.99.18"
                     /note="aprataxin- and PNK-like factor; XRCC1-interacting
                     protein 1; PNK and APTX-like FHA protein;
                     apurinic-apyrimidinic endonuclease APLF; PNK and APTX-like
                     FHA domain-containing protein; zinc finger, CX5CX6HX5H
                     motif containing 1"
                     /calculated_mol_wt=56825
     Region          4..101
                     /region_name="FHA_APLF"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and PNK-like factor (APLF) and similar proteins; cd22717"
                     /db_xref="CDD:438769"
     Site            order(27..29,33..34,36..40,58..60)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438769"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:17507382; propagated from
                     UniProtKB/Swiss-Prot (Q8IW19.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D842; propagated from
                     UniProtKB/Swiss-Prot (Q8IW19.1)"
     Region          182..191
                     /region_name="KBM. /evidence=ECO:0000269|PubMed:23689425,
                     ECO:0000269|PubMed:27063109"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW19.1)"
     Region          223..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW19.1)"
     Region          376..400
                     /region_name="zf-CCHH"
                     /note="PBZ domain; pfam10283"
                     /db_xref="CDD:463043"
     Region          406..416
                     /region_name="Flexible linker.
                     /evidence=ECO:0000305|PubMed:20439749"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW19.1)"
     Region          418..442
                     /region_name="zf-CCHH"
                     /note="PBZ domain; pfam10283"
                     /db_xref="CDD:463043"
     Region          449..497
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:21211722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW19.1)"
     Region          476..500
                     /region_name="NAP1L motif.
                     /evidence=ECO:0000269|PubMed:21211722"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IW19.1)"
     CDS             1..511
                     /gene="APLF"
                     /gene_synonym="APFL; C2orf13; PALF; Xip1; ZCCHH1"
                     /coded_by="NM_173545.3:148..1683"
                     /db_xref="CCDS:CCDS1888.1"
                     /db_xref="GeneID:200558"
                     /db_xref="HGNC:HGNC:28724"
                     /db_xref="MIM:611035"
ORIGIN      
        1 msggfelqpr dggprvalap getvigrgpl lgitdkrvsr rhailevagg qlrikpihtn
       61 pcfyqsseks qllplkpnlw cylnpgdsfs llvdkyifri lsipsevemq ctlrnsqvld
      121 ednilnetpk spvinlphet tgasqlegst eiaktqmtpt nsvsflgenr dcnkqqpila
      181 erkrilptwm laehlsdqnl svpaisggnv iqgsgkeeic kdksqlnttq qgrrqlissg
      241 ssentsaeqd tgeeckntdq eestisskem pqsfsaitls ntemnniktn aqrnklpiee
      301 lgkvskhkia tkrtphkede amscsencss aqgdslqdes qgshsesssn psnpetlhak
      361 atdsvlqgse gnkvkrtscm ygancyrknp vhfqhfshpg dsdyggvqiv gqdetddrpe
      421 cpygpscyrk npqhkieyrh ntlpvrnvld edndnvgqpn eydlndsfld deeedyeptd
      481 edsdwepgke deekedveel lkeakrfmkr k
//
LOCUS       NP_001162002             252 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SOCS box protein 9 isoform 3 [Homo sapiens].
ACCESSION   NP_001162002
VERSION     NP_001162002.1
DBSOURCE    REFSEQ: accession NM_001168530.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Li,N., Zhou,Q., Yi,Z., Zhang,H. and Zhou,D.
  TITLE     Ubiquitin protein E3 ligase ASB9 suppresses proliferation and
            promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation
  JOURNAL   Biol Res 56 (1), 4 (2023)
   PUBMED   36683111
  REMARK    GeneRIF: Ubiquitin protein E3 ligase ASB9 suppresses proliferation
            and promotes apoptosis in human spermatogonial stem cell line by
            inducing HIF1AN degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Lumpkin,R.J., Ahmad,A.S., Blake,R., Condon,C.J. and Komives,E.A.
  TITLE     The Mechanism of NEDD8 Activation of CUL5 Ubiquitin E3 Ligases
  JOURNAL   Mol Cell Proteomics 20, 100019 (2021)
   PUBMED   33268465
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Fei,X., Zhang,Y., Gu,X., Qiu,R., Mao,Y. and Ji,C.
  TITLE     Crystallization and preliminary X-ray analysis of the splice
            variant of human ankyrin repeat and suppressor of cytokine
            signaling box protein 9 (hASB9-2)
  JOURNAL   Protein Pept Lett 15 (6), 647-649 (2008)
   PUBMED   18680464
  REMARK    GeneRIF: The splice variant of hASB9, hASB9-2 protein, was cloned,
            overexpressed, and crystallized and the data showed that the cubic
            hASB9-2 crystal belongs to space group P4(3)32 with unit-cell
            parameters.
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Debrincat,M.A., Zhang,J.G., Willson,T.A., Silke,J., Connolly,L.M.,
            Simpson,R.J., Alexander,W.S., Nicola,N.A., Kile,B.T. and
            Hilton,D.J.
  TITLE     Ankyrin repeat and suppressors of cytokine signaling box protein
            asb-9 targets creatine kinase B for degradation
  JOURNAL   J Biol Chem 282 (7), 4728-4737 (2007)
   PUBMED   17148442
REFERENCE   9  (residues 1 to 252)
  AUTHORS   Kohroki,J., Nishiyama,T., Nakamura,T. and Masuho,Y.
  TITLE     ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin
            ligase complexes
  JOURNAL   FEBS Lett 579 (30), 6796-6802 (2005)
   PUBMED   16325183
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA943920.1 and BC001244.1.
            
            Summary: This gene encodes a member of the ankyrin repeat and
            suppressor of cytokine signaling (SOCS) box protein family. Members
            of this family can interact with the elongin B-C adapter complex
            via their SOCS box domain and further complex with the cullin and
            ring box proteins to form E3 ubiquitin ligase complexes. They may
            function to mediate the substrate-recognition of the E3 ubiquitin
            ligases. A transcribed pseudogene of this gene has been identified
            on chromosome 15. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Dec
            2009].
            
            Transcript Variant: This variant (3) uses two alternate splice
            sites in the coding region, one of which results in a frameshift,
            compared to variant 1. The resulting protein (isoform 3) has a
            distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001244.1, SRR5189658.192948.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..252
                     /product="ankyrin repeat and SOCS box protein 9 isoform 3"
                     /note="ankyrin repeat and SOCS box protein 9; ankyrin
                     repeat and suppressor of cytokine signaling box protein 9;
                     ASB-9; testis tissue sperm-binding protein Li 57p"
                     /calculated_mol_wt=26718
     Site            order(35,37,41..42,45..47,49..50,54,57,66,68,70,74..75,
                     78..80,82..83,87,90,99,101,103,107..108,111..113,115..116,
                     120,123)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          35..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          <36..251
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          68..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          101..131
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..186
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          188..219
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..252
                     /gene="ASB9"
                     /coded_by="NM_001168530.2:210..968"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55372.1"
                     /db_xref="GeneID:140462"
                     /db_xref="HGNC:HGNC:17184"
                     /db_xref="MIM:300890"
ORIGIN      
        1 mdgkqggmdg skpagprdfp girllsnplm gdavsdwspm heaaihghql slrnlisqgw
       61 avniitadhv splheaclgg hlscvkillk hgaqvngvta dwhtplfnac vsgswdcvnl
      121 llqhgasvqp esdlaspihe aarrayggni dhkishlgtp lylacenqqr acvkkllesg
      181 advnqgkgqd splhavarta seelacllmd fgadtqakna egkrpvelvp pesplaqlfl
      241 eregaslpkp kp
//
LOCUS       NP_001278030            1076 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-2 isoform d
            [Homo sapiens].
ACCESSION   NP_001278030
VERSION     NP_001278030.1
DBSOURCE    REFSEQ: accession NM_001291101.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Dolphin,A.C.
  TITLE     Voltage-gated calcium channels and their auxiliary subunits:
            physiology and pathophysiology and pharmacology
  JOURNAL   J Physiol 594 (19), 5369-5390 (2016)
   PUBMED   27273705
  REMARK    Review article
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Warnier,M., Roudbaraki,M., Derouiche,S., Delcourt,P., Bokhobza,A.,
            Prevarskaya,N. and Mariot,P.
  TITLE     CACNA2D2 promotes tumorigenesis by stimulating cell proliferation
            and angiogenesis
  JOURNAL   Oncogene 34 (42), 5383-5394 (2015)
   PUBMED   25619833
  REMARK    GeneRIF: show that the action of alpha2delta2 on tumor development
            occurs not only through a stimulation of proliferation
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Pippucci,T., Parmeggiani,A., Palombo,F., Maresca,A., Angius,A.,
            Crisponi,L., Cucca,F., Liguori,R., Valentino,M.L., Seri,M. and
            Carelli,V.
  TITLE     A novel null homozygous mutation confirms CACNA2D2 as a gene
            mutated in epileptic encephalopathy
  JOURNAL   PLoS One 8 (12), e82154 (2013)
   PUBMED   24358150
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Rhodin,A., Gronbladh,A., Ginya,H., Nilsson,K.W., Rosenblad,A.,
            Zhou,Q., Enlund,M., Hallberg,M., Gordh,T. and Nyberg,F.
  TITLE     Combined analysis of circulating beta-endorphin with gene
            polymorphisms in OPRM1, CACNAD2 and ABCB1 reveals correlation with
            pain, opioid sensitivity and opioid-related side effects
  JOURNAL   Mol Brain 6, 8 (2013)
   PUBMED   23402298
  REMARK    GeneRIF: The investigation of single nucleotide polymorphisms in
            three genes that have a functional impact on the opioid response:
            OPRM1, ABCB1 and the calcium channel complex subunit CACNA2D2, is
            reported.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Edvardson,S., Oz,S., Abulhijaa,F.A., Taher,F.B., Shaag,A.,
            Zenvirt,S., Dascal,N. and Elpeleg,O.
  TITLE     Early infantile epileptic encephalopathy associated with a high
            voltage gated calcium channelopathy
  JOURNAL   J Med Genet 50 (2), 118-123 (2013)
   PUBMED   23339110
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Angeloni,D., Duh,F.M., Wei,M.F., Johnson,B.E. and Lerman,M.I.
  TITLE     A G-to-A single nucleotide polymorphism in intron 2 of the human
            CACNA2D2 gene that maps at 3p21.3
  JOURNAL   Mol Cell Probes 15 (2), 125-127 (2001)
   PUBMED   11292331
REFERENCE   8  (residues 1 to 1076)
  AUTHORS   Lerman,M.I. and Minna,J.D.
  TITLE     The 630-kb lung cancer homozygous deletion region on human
            chromosome 3p21.3: identification and evaluation of the resident
            candidate tumor suppressor genes. The International Lung Cancer
            Chromosome 3p21.3 Tumor Suppressor Gene Consortium
  JOURNAL   Cancer Res 60 (21), 6116-6133 (2000)
   PUBMED   11085536
REFERENCE   9  (residues 1 to 1076)
  AUTHORS   Gao,B., Sekido,Y., Maximov,A., Saad,M., Forgacs,E., Latif,F.,
            Wei,M.H., Lerman,M., Lee,J.H., Perez-Reyes,E., Bezprozvanny,I. and
            Minna,J.D.
  TITLE     Functional properties of a new voltage-dependent calcium channel
            alpha(2)delta auxiliary subunit gene (CACNA2D2)
  JOURNAL   J Biol Chem 275 (16), 12237-12242 (2000)
   PUBMED   10766861
REFERENCE   10 (residues 1 to 1076)
  AUTHORS   Hobom,M., Dai,S., Marais,E., Lacinova,L., Hofmann,F. and
            Klugbauer,N.
  TITLE     Neuronal distribution and functional characterization of the
            calcium channel alpha2delta-2 subunit
  JOURNAL   Eur J Neurosci 12 (4), 1217-1226 (2000)
   PUBMED   10762351
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF042793.1, Z84492.2 and
            BF373910.1.
            
            Summary: Calcium channels mediate the entry of calcium ions into
            the cell upon membrane polarization. This gene encodes the
            alpha-2/delta subunit of the voltage-dependent calcium channel
            complex. The complex consists of the main channel-forming subunit
            alpha-1, and auxiliary subunits alpha-2/delta, beta, and gamma. The
            auxiliary subunits function in the assembly and membrane
            localization of the complex, and modulate calcium currents and
            channel activation/inactivation kinetics. The subunit encoded by
            this gene undergoes post-translational cleavage to yield the
            extracellular alpha2 peptide and a membrane-anchored delta
            polypeptide. This subunit is a receptor for the antiepileptic drug,
            gabapentin. Mutations in this gene are associated with early
            infantile epileptic encephalopathy. Single nucleotide polymorphisms
            in this gene are correlated with increased sensitivity to opioid
            drugs. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (4) has a different 5' structure,
            lacks an in-frame exon in the central coding region and uses an
            alternate in-frame splice site in the 3' coding region, resulting
            in the use of a downstream start codon compared to variant 3. The
            encoded isoform (d) has a shorter N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF042793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1076
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-2 isoform d"
                     /note="gene 26; alpha 2 delta calcium channel subunit;
                     voltage-gated calcium channel subunit alpha-2/delta-2;
                     calcium channel, voltage-dependent, alpha 2/delta subunit
                     2; alpha2delta-2"
                     /calculated_mol_wt=121987
     Region          72..196
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Region          208..387
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(228,230,232,300,332)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          <379..462
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Region          464..573
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Region          593..1037
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     CDS             1..1076
                     /gene="CACNA2D2"
                     /gene_synonym="CACNA2D; CASVDD"
                     /coded_by="NM_001291101.1:178..3408"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS77748.1"
                     /db_xref="GeneID:9254"
                     /db_xref="HGNC:HGNC:1400"
                     /db_xref="MIM:607082"
ORIGIN      
        1 mqhwarrleq evdgvmrifg gvqqlreiyk dnrnlfevqe nepqklvekv agdieslldr
       61 kvqalkrlad aaenfqkahr wqdnikeedi vyydakadae lddpesedve rgskastlrl
      121 dfiedpnfkn kvnysyaavq iptdiykgst vilnelnwte alenvfmenr rqdptllwqv
      181 fgsatgvtry ypatpwrapk kidlydvrrr pwyiqgassp kdmviivdvs gsvsgltlkl
      241 mktsvcemld tlsdddyvnv asfnekaqpv scfthlvqan vrnkkvfkea vqgmvakgtt
      301 gykagfeyaf dqlqnsnitr ancnkmimmf tdggedrvqd vfekynwpnr tvrvftfsvg
      361 qhnydvtplq wmacankgyy feipsigair intqeyldvl grpmvlagke akqvqwtnvy
      421 edalglglvv tgtlpvfnlt qdgpgekknq lilgvmgidv alndikrltp nytlgangyv
      481 faidlngyvl lhpnlkpqtt nfrepvtldf ldaeledenk eeirrsmidg nkghkqirtl
      541 vkslderyid evtrnytwvp irstnyslgl vlppystfyl qanlsdqilq vkyfefllps
      601 sfeseghvfi apreyckdln asdnnteflk nfielmekvt pdskqcnnfl lhnlildtgi
      661 tqqlvervwr dqdlntysll avfaatdggi trvfpnkaae dwtenpepfn asfyrrsldn
      721 hgyvfkpphq dallrplele ndtvgilvst avelslgrrt lrpavvgvkl dleawaekfk
      781 vlasnrthqd qpqkcgpnsh cemdcevnne dllcvliddg gflvlsnqnh qwdqvgrffs
      841 evdanlmlal ynnsfytrke sydyqaacap qppgnlgaap rgvfvptvad flnlawwtsa
      901 aawslfqqll ygliyhswfq adpaeaegsp etresscvmk qtqyyfgsvn asynaiidcg
      961 ncsrlfhaqr ltntnllfvv aekplcsqce agrllqketh cpadgpeqce lvqrpryrrg
     1021 phicfdynat edtsdcgrga sfppslgvlv slqlllllgl pprpqpqvlv hasrrl
//
LOCUS       NP_001229392             262 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 32 isoform 3 [Homo sapiens].
ACCESSION   NP_001229392
VERSION     NP_001229392.1
DBSOURCE    REFSEQ: accession NM_001242463.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 262)
  AUTHORS   Li,F., Yu,H., Zhang,Y., Ma,Y., Chen,X., Zhang,J., Sun,L., Guo,R.,
            Wu,Y., Zheng,P., Wang,X., Bie,P., He,F., Zhang,L., Xie,C. and
            Xiong,H.
  TITLE     F-box protein FBXO32 ubiquitinates and stabilizes D-type cyclins to
            drive cancer progression
  JOURNAL   Nat Commun 16 (1), 4060 (2025)
   PUBMED   40307251
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 262)
  AUTHORS   Su,D., Wang,R., Chen,G., Ding,C., Liu,Y., Tao,J., Wang,Y., Qiu,J.,
            Luo,W., Weng,G., Yang,G. and Zhang,T.
  TITLE     FBXO32 Stimulates Protein Synthesis to Drive Pancreatic Cancer
            Progression and Metastasis
  JOURNAL   Cancer Res 84 (16), 2607-2625 (2024)
   PUBMED   38775804
  REMARK    GeneRIF: FBXO32 Stimulates Protein Synthesis to Drive Pancreatic
            Cancer Progression and Metastasis.
REFERENCE   3  (residues 1 to 262)
  AUTHORS   Wu,J., Wen,T., Marzio,A., Song,D., Chen,S., Yang,C., Zhao,F.,
            Zhang,B., Zhao,G., Ferri,A., Cheng,H., Ma,J., Ren,H., Chen,Q.Y.,
            Yang,Y. and Qin,S.
  TITLE     FBXO32-mediated degradation of PTEN promotes lung adenocarcinoma
            progression
  JOURNAL   Cell Death Dis 15 (4), 282 (2024)
   PUBMED   38643215
  REMARK    GeneRIF: FBXO32-mediated degradation of PTEN promotes lung
            adenocarcinoma progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 262)
  AUTHORS   Lu,Y., Huang,P., Li,Y., Liu,W., Li,J., Zhao,R., Feng,H., Shi,C. and
            Cao,G.
  TITLE     The FBXO32/ATR/ATM axis acts as a molecular switch to control the
            sensitivity of osteosarcoma cells to irradiation through its
            regulation of EXO1 expression
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (5), 842-852 (2023)
   PUBMED   37227155
  REMARK    GeneRIF: The FBXO32/ATR/ATM axis acts as a molecular switch to
            control the sensitivity of osteosarcoma cells to irradiation
            through its regulation of EXO1 expression.
REFERENCE   5  (residues 1 to 262)
  AUTHORS   Xu,K., Liu,Q., Huang,W., Chu,Y., Fan,W., Liu,J., He,Y. and Huang,F.
  TITLE     Promotive Effect of FBXO32 on the Odontoblastic Differentiation of
            Human Dental Pulp Stem Cells
  JOURNAL   Int J Mol Sci 24 (9), 7708 (2023)
   PUBMED   37175415
  REMARK    GeneRIF: Promotive Effect of FBXO32 on the Odontoblastic
            Differentiation of Human Dental Pulp Stem Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 262)
  AUTHORS   Doucet,M., Russell,A.P., Leger,B., Debigare,R., Joanisse,D.R.,
            Caron,M.A., LeBlanc,P. and Maltais,F.
  TITLE     Muscle atrophy and hypertrophy signaling in patients with chronic
            obstructive pulmonary disease
  JOURNAL   Am J Respir Crit Care Med 176 (3), 261-269 (2007)
   PUBMED   17478621
  REMARK    GeneRIF: Atrogin-1 mRNA expression was significantly increased in
            quadriceps of patients with COPD; transcriptional regulation of
            atrogin-1 and MuRF1 may occur via FoxO-1, but independently of AKT
REFERENCE   7  (residues 1 to 262)
  AUTHORS   Ogawa,T., Furochi,H., Mameoka,M., Hirasaka,K., Onishi,Y., Suzue,N.,
            Oarada,M., Akamatsu,M., Akima,H., Fukunaga,T., Kishi,K., Yasui,N.,
            Ishidoh,K., Fukuoka,H. and Nikawa,T.
  TITLE     Ubiquitin ligase gene expression in healthy volunteers with 20-day
            bedrest
  JOURNAL   Muscle Nerve 34 (4), 463-469 (2006)
   PUBMED   16868939
  REMARK    GeneRIF: results suggest that Cbl-b- or atrogin-1-mediated
            ubiquitination plays an important role in unloading-induced muscle
            atrophy, and that unloading stress may preferentially inhibit
            transcriptional responses in skeletal muscle
REFERENCE   8  (residues 1 to 262)
  AUTHORS   Leger,B., Vergani,L., Soraru,G., Hespel,P., Derave,W., Gobelet,C.,
            D'Ascenzio,C., Angelini,C. and Russell,A.P.
  TITLE     Human skeletal muscle atrophy in amyotrophic lateral sclerosis
            reveals a reduction in Akt and an increase in atrogin-1
  JOURNAL   FASEB J 20 (3), 583-585 (2006)
   PUBMED   16507768
  REMARK    GeneRIF: Human skeletal muscle atrophy in the amyotrophic lateral
            sclerosis shows an increase in atrogin-1 & a decrease in Akt. The
            transcriptional regulation of human atrogin-1 may be controlled by
            an Akt-mediated transcription factor other than FKHR.
REFERENCE   9  (residues 1 to 262)
  AUTHORS   Gomes,M.D., Lecker,S.H., Jagoe,R.T., Navon,A. and Goldberg,A.L.
  TITLE     Atrogin-1, a muscle-specific F-box protein highly expressed during
            muscle atrophy
  JOURNAL   Proc Natl Acad Sci U S A 98 (25), 14440-14445 (2001)
   PUBMED   11717410
REFERENCE   10 (residues 1 to 262)
  AUTHORS   Bodine,S.C., Latres,E., Baumhueter,S., Lai,V.K., Nunez,L.,
            Clarke,B.A., Poueymirou,W.T., Panaro,F.J., Na,E., Dharmarajan,K.,
            Pan,Z.Q., Valenzuela,D.M., DeChiara,T.M., Stitt,T.N.,
            Yancopoulos,G.D. and Glass,D.J.
  TITLE     Identification of ubiquitin ligases required for skeletal muscle
            atrophy
  JOURNAL   Science 294 (5547), 1704-1708 (2001)
   PUBMED   11679633
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from EF143260.1, AC090193.7,
            AK125888.1 and AI077844.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class and contains an F-box domain. This
            protein is highly expressed during muscle atrophy, whereas mice
            deficient in this gene were found to be resistant to atrophy. This
            protein is thus a potential drug target for the treatment of muscle
            atrophy. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Jun
            2011].
            
            Transcript Variant: This variant (3) lacks two in-frame exons in
            the coding region, compared to variant 1. This encodes a shorter
            protein (isoform 3), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2790727.1,
                                           SRR7346977.2774335.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..262
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..262
                     /product="F-box only protein 32 isoform 3"
                     /note="F-box only protein 32; muscle atrophy F-box
                     protein; atrogin 1"
                     /calculated_mol_wt=30673
     Region          62..67
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:22249105"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969P5.1)"
     Region          130..177
                     /region_name="F-box_FBXO32"
                     /note="F-box domain found in F-box only protein 32
                     (FBXO32) and similar proteins; cd22103"
                     /db_xref="CDD:438875"
     Site            order(135,139,142..143,146..147,152,154..155,159..161,163)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438875"
     Region          <172..>209
                     /region_name="Elongin_A"
                     /note="RNA polymerase II transcription factor SIII
                     (Elongin) subunit A; pfam06881"
                     /db_xref="CDD:462026"
     CDS             1..262
                     /gene="FBXO32"
                     /gene_synonym="Fbx32; MAFbx"
                     /coded_by="NM_001242463.2:193..981"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS56553.1"
                     /db_xref="GeneID:114907"
                     /db_xref="HGNC:HGNC:16731"
                     /db_xref="MIM:606604"
ORIGIN      
        1 mpflgqdwrs pgqnwvktad gwkrfldeks gsfvsdlssy cnkevynken lfnslnydva
       61 akkrkkdmln sktktqyfhq ekwiyvhkgs tkerhgyctl geafnrldfs taildsrrfn
      121 yvvrpafkgl tftdlplclq lnimqrlsdg rdlvslgqaa pdlhvlsedr llwkklcqyh
      181 fserqirkrl ilsdkgqldw kkmyfklvrc yprkeqygdt lqlckhchil swkgtdhpct
      241 annpescsvs lspqdfinlf kf
//
LOCUS       NP_003770                393 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 3 [Homo sapiens].
ACCESSION   NP_003770
VERSION     NP_003770.1
DBSOURCE    REFSEQ: accession NM_003779.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Bi,C., Shan,J., Li,M., Zhang,Q., Li,C., Tong,J. and Huang,Q.
  TITLE     Long noncoding RNA differentiation antagonizing nonprotein coding
            RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p
  JOURNAL   Neuroreport 32 (12), 965-974 (2021)
   PUBMED   34050113
  REMARK    GeneRIF: Long noncoding RNA differentiation antagonizing nonprotein
            coding RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Binieda,K., Rzepnikowska,W., Kolakowski,D., Kaminska,J.,
            Szczepankiewicz,A.A., Nieznanska,H., Kochanski,A. and Kabzinska,D.
  TITLE     Mutations in GDAP1 Influence Structure and Function of the
            Trans-Golgi Network
  JOURNAL   Int J Mol Sci 22 (2), 914 (2021)
   PUBMED   33477664
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Wu,T., Li,Y. and Chen,B.
  TITLE     B4GALT3 promotes cell proliferation and invasion in glioblastoma
  JOURNAL   Neurol Res 42 (6), 463-470 (2020)
   PUBMED   32202233
  REMARK    GeneRIF: B4GALT3 promotes cell proliferation and invasion in
            glioblastoma.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Tange,R., Tomatsu,T. and Sato,T.
  TITLE     Transcription of human beta4-galactosyltransferase 3 is regulated
            by differential DNA binding of Sp1/Sp3 in SH-SY5Y human
            neuroblastoma and A549 human lung cancer cell lines
  JOURNAL   Glycobiology 29 (3), 211-221 (2019)
   PUBMED   30561605
  REMARK    GeneRIF: These findings suggest that the transcription of the
            b4GalT3 gene is regulated by differential DNA binding of Sp3 and
            Sp1 in neuroblastoma and lung cancer. The increased expression of
            b4GalT3 in neuroblastoma may be ascribed to the enhanced expression
            of Sp3, which is observed for various cancers.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Liu,H., Chen,D., Bi,J., Han,J., Yang,M., Dong,W., Lin,T. and
            Huang,J.
  TITLE     Circular RNA circUBXN7 represses cell growth and invasion by
            sponging miR-1247-3p to enhance B4GALT3 expression in bladder
            cancer
  JOURNAL   Aging (Albany NY) 10 (10), 2606-2623 (2018)
   PUBMED   30312173
  REMARK    GeneRIF: In bladder tumor cells circUBXN7 serves as a competitive
            endogenous RNA of miR-1247-3p to elevate B4GALT3 expression,
            consequently inhibiting cell viability and invasion.
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Davidsson,J., Andersson,A., Paulsson,K., Heidenblad,M.,
            Isaksson,M., Borg,A., Heldrup,J., Behrendtz,M., Panagopoulos,I.,
            Fioretos,T. and Johansson,B.
  TITLE     Tiling resolution array comparative genomic hybridization,
            expression and methylation analyses of dup(1q) in Burkitt lymphomas
            and pediatric high hyperdiploid acute lymphoblastic leukemias
            reveal clustered near-centromeric breakpoints and overexpression of
            genes in 1q22-32.3
  JOURNAL   Hum Mol Genet 16 (18), 2215-2225 (2007)
   PUBMED   17613536
  REMARK    GeneRIF: B4GALT3, DAP3, RGS16, TMEM183A and UCK2--were
            significantly overexpressed in dup(1q)-positive ALLs compared with
            high hyperdiploid ALLs without dup(1q).
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC339671.1, AK291455.1 and
            BC006099.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene
            encodes an enzyme that may be mainly involved in the synthesis of
            the first N-acetyllactosamine unit of poly-N-acetyllactosamine
            chains. Multiple alternatively spliced transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) lacks an internal segment in
            the 5' UTR, and encodes the same protein, as compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.181823.1,
                                           SRR3476690.701043.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319769.10/ ENSP00000320965.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..393
                     /product="beta-1,4-galactosyltransferase 3"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /EC_number="2.4.1.275"
                     /note="beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 3; b4Gal-T3;
                     beta-1,4-GalTase 3; epididymis secretory sperm binding
                     protein; nal synthase; N-acetyllactosamine synthase;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 3; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase, polypeptide 3;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase; neolactotriaosylceramide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=43797
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          122..341
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(130,132,134,169,195..197)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Site            order(195,197,291)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          339..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     CDS             1..393
                     /gene="B4GALT3"
                     /gene_synonym="beta4Gal-T3"
                     /coded_by="NM_003779.4:246..1427"
                     /db_xref="CCDS:CCDS1222.1"
                     /db_xref="GeneID:8703"
                     /db_xref="HGNC:HGNC:926"
                     /db_xref="MIM:604014"
ORIGIN      
        1 mlrrllerpc tlallvgsql avmmylslgg frslsalfgr dqgptfdysh prdvysnlsh
       61 lpgapggppa pqglpycper spllvgpvsv sfspvpslae ivernprvep ggryrpagce
      121 prsrtaiivp hrarehhlrl llyhlhpflq rqqlaygiyv ihqagngtfn rakllnvgvr
      181 ealrdeewdc lflhdvdllp endhnlyvcd prgprhvava mnkfgyslpy pqyfggvsal
      241 tpdqylkmng fpneywgwgg edddiatrvr lagmkisrpp tsvghykmvk hrgdkgneen
      301 phrfdllvrt qnswtqdgmn sltyqllare lgplytnita digtdprgpr apsgpryppg
      361 ssqafrqeml qrrpparpgp lstanhtalr gsh
//
LOCUS       NP_001353501             820 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001353501 XP_016855516
VERSION     NP_001353501.1
DBSOURCE    REFSEQ: accession NM_001366572.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 820)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 820)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 820)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 820)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 820)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 820)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 820)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 820)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 820)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855516.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.73674.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..820
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..820
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 9"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92398
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <522..>656
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..820
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366572.1:2055..4517"
                     /note="isoform 9 is encoded by transcript variant 12"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprg rrrrspsppp trrrrspspa
      481 ppprrrrtpt ppprrrtpsp pprrrspspr rysppiqrry spspppkrrt aspppppkrr
      541 aspspppkrr vshspppkqr sspvtkrrsp slsskhrkgs spsrstrear spqpnkrhsp
      601 sprprapqts sspppvrrga ssspqrrqsp spstrpirrv srtpepkkik kaaspspqsv
      661 rrvsssrsvs gspepaakkp pappspvqsq spstnwspav pvkkaksptp spspprnsdq
      721 egggkkkkkk kdkkhkkdkk hkkhkkhkke kavaaaaaaa vtpaaiaaat ttlaqeepva
      781 apepkketes eaednlddle khlrekalrs mrkaqvspqs
//
LOCUS       NP_036205                541 aa            linear   PRI 20-NOV-2025
DEFINITION  T-complex protein 1 subunit epsilon isoform a [Homo sapiens].
ACCESSION   NP_036205
VERSION     NP_036205.1
DBSOURCE    REFSEQ: accession NM_012073.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Wu,S. and Peng,L.
  TITLE     Increased CCT5 expression is a potential unfavourable factor
            promoting the growth of nasopharyngeal carcinoma
  JOURNAL   J Int Med Res 52 (9), 3000605241271754 (2024)
   PUBMED   39286844
  REMARK    GeneRIF: Increased CCT5 expression is a potential unfavourable
            factor promoting the growth of nasopharyngeal carcinoma.
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Scalia,F., Lo Bosco,G., Paladino,L., Vitale,A.M., Noori,L., Conway
            de Macario,E., Macario,A.J.L., Bucchieri,F., Cappello,F. and Lo
            Celso,F.
  TITLE     Structural and Dynamic Disturbances Revealed by Molecular Dynamics
            Simulations Predict the Impact on Function of CCT5 Chaperonin
            Mutations Associated with Rare Severe Distal Neuropathies
  JOURNAL   Int J Mol Sci 24 (3), 2018 (2023)
   PUBMED   36768350
  REMARK    GeneRIF: Structural and Dynamic Disturbances Revealed by Molecular
            Dynamics Simulations Predict the Impact on Function of CCT5
            Chaperonin Mutations Associated with Rare Severe Distal
            Neuropathies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Sergeeva,O.A., Tran,M.T., Haase-Pettingell,C. and King,J.A.
  TITLE     Biochemical characterization of mutants in chaperonin proteins CCT4
            and CCT5 associated with hereditary sensory neuropathy
  JOURNAL   J Biol Chem 289 (40), 27470-27480 (2014)
   PUBMED   25124038
  REMARK    GeneRIF: H147R CCT5 was not as efficient in chaperoning these
            substrates as wild type CCT5.
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Bouhouche,A., Benomar,A., Bouslam,N., Chkili,T. and Yahyaoui,M.
  TITLE     Mutation in the epsilon subunit of the cytosolic
            chaperonin-containing t-complex peptide-1 (Cct5) gene causes
            autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia
  JOURNAL   J Med Genet 43 (5), 441-443 (2006)
   PUBMED   16399879
  REMARK    GeneRIF: A missense mutation within the CCT5 gene is associated
            with autosomal recessive mutilating sensory neuropathy with spastic
            paraplegia.
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Roperch,J.P., Lethrone,F., Prieur,S., Piouffre,L., Israeli,D.,
            Tuynder,M., Nemani,M., Pasturaud,P., Gendron,M.C., Dausset,J.,
            Oren,M., Amson,R.B. and Telerman,A.
  TITLE     SIAH-1 promotes apoptosis and tumor suppression through a network
            involving the regulation of protein folding, unfolding, and
            trafficking: identification of common effectors with p53 and
            p21(Waf1)
  JOURNAL   Proc Natl Acad Sci U S A 96 (14), 8070-8073 (1999)
   PUBMED   10393949
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Liou,A.K. and Willison,K.R.
  TITLE     Elucidation of the subunit orientation in CCT (chaperonin
            containing TCP1) from the subunit composition of CCT
            micro-complexes
  JOURNAL   EMBO J 16 (14), 4311-4316 (1997)
   PUBMED   9250675
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Roobol,A., Holmes,F.E., Hayes,N.V., Baines,A.J. and Carden,M.J.
  TITLE     Cytoplasmic chaperonin complexes enter neurites developing in vitro
            and differ in subunit composition within single cells
  JOURNAL   J Cell Sci 108 (Pt 4), 1477-1488 (1995)
   PUBMED   7615668
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Kubota,H., Hynes,G., Carne,A., Ashworth,A. and Willison,K.
  TITLE     Identification of six Tcp-1-related genes encoding divergent
            subunits of the TCP-1-containing chaperonin
  JOURNAL   Curr Biol 4 (2), 89-99 (1994)
   PUBMED   7953530
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from FJ224303.1.
            
            Summary: The protein encoded by this gene is a molecular chaperone
            that is a member of the chaperonin containing TCP1 complex (CCT),
            also known as the TCP1 ring complex (TRiC). This complex consists
            of two identical stacked rings, each containing eight different
            proteins. Unfolded polypeptides enter the central cavity of the
            complex and are folded in an ATP-dependent manner. The complex
            folds various proteins, including actin and tubulin. Mutations in
            this gene cause hereditary sensory and autonomic neuropathy with
            spastic paraplegia (HSNSP). Alternative splicing results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 5 and 13. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ224303.1, SRR1803615.113869.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280326.9/ ENSP00000280326.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..541
                     /product="T-complex protein 1 subunit epsilon isoform a"
                     /note="T-complex protein 1 subunit epsilon; epididymis
                     secretory protein Li 69; chaperonin containing TCP1,
                     subunit 5 (epsilon); chaperonin containing T-complex
                     polypeptide 1 subunit 5"
                     /calculated_mol_wt=59540
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Region          10..535
                     /region_name="TCP1_epsilon"
                     /note="TCP-1 (CTT or eukaryotic type II) chaperonin
                     family, epsilon subunit. Chaperonins are involved in
                     productive folding of proteins. They share a common
                     general morphology, a double toroid of 2 stacked rings. In
                     contrast to bacterial group I chaperonins...; cd03339"
                     /db_xref="CDD:239455"
     Site            order(25,29,57..60,62,80,82,86,90,93,392,529..535)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239455"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Site            order(52..54,104,108,171,404,422,462,506,508)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239455"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     Site            order(442,460,469,471..472,475)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239455"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48643.1)"
     CDS             1..541
                     /gene="CCT5"
                     /gene_synonym="CCT-epsilon; CCTE; HEL-S-69; HSNSP;
                     PNAS-102; TCP-1-epsilon"
                     /coded_by="NM_012073.5:62..1687"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3877.1"
                     /db_xref="GeneID:22948"
                     /db_xref="HGNC:HGNC:1618"
                     /db_xref="MIM:610150"
ORIGIN      
        1 masmgtlafd eygrpfliik dqdrksrlmg lealkshima akavantmrt slgpngldkm
       61 mvdkdgdvtv tndgatilsm mdvdhqiakl mvelsksqdd eigdgttgvv vlagalleea
      121 eqlldrgihp iriadgyeqa arvaiehldk isdsvlvdik dtepliqtak ttlgskvvns
      181 chrqmaeiav navltvadme rrdvdfelik vegkvggrle dtklikgviv dkdfshpqmp
      241 kkvedakiai ltcpfeppkp ktkhkldvts vedykalqky ekekfeemiq qiketganla
      301 icqwgfddea nhlllqnnlp avrwvggpei eliaiatggr ivprfselta eklgfaglvq
      361 eisfgttkdk mlvieqckns ravtifirgg nkmiieeakr slhdalcvir nlirdnrvvy
      421 gggaaeisca lavsqeadkc ptleqyamra fadalevipm alsensgmnp iqtmtevrar
      481 qvkemnpalg idclhkgtnd mkqqhvietl igkkqqisla tqmvrmilki ddirkpgese
      541 e
//
LOCUS       NP_076972                449 aa            linear   PRI 20-NOV-2025
DEFINITION  integrator complex subunit 15 isoform 1 [Homo sapiens].
ACCESSION   NP_076972
VERSION     NP_076972.2
DBSOURCE    REFSEQ: accession NM_024067.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Azuma,N., Yokoi,T., Tanaka,T., Matsuzaka,E., Saida,Y., Nishina,S.,
            Terao,M., Takada,S., Fukami,M., Okamura,K., Maehara,K.,
            Yamasaki,T., Hirayama,J., Nishina,H., Handa,H. and Yamaguchi,Y.
  TITLE     Integrator complex subunit 15 controls mRNA splicing and is
            critical for eye development
  JOURNAL   Hum Mol Genet 32 (12), 2032-2045 (2023)
   PUBMED   36851842
  REMARK    GeneRIF: Integrator complex subunit 15 controls mRNA splicing and
            is critical for eye development.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Drew,K., Wallingford,J.B. and Marcotte,E.M.
  TITLE     hu.MAP 2.0: integration of over 15,000 proteomic experiments builds
            a global compendium of human multiprotein assemblies
  JOURNAL   Mol Syst Biol 17 (5), e10016 (2021)
   PUBMED   33973408
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Pfleiderer,M.M. and Galej,W.P.
  TITLE     Structure of the catalytic core of the Integrator complex
  JOURNAL   Mol Cell 81 (6), 1246-1259 (2021)
   PUBMED   33548203
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Beckedorff,F., Blumenthal,E., daSilva,L.F., Aoi,Y., Cingaram,P.R.,
            Yue,J., Zhang,A., Dokaneheifard,S., Valencia,M.G., Gaidosh,G.,
            Shilatifard,A. and Shiekhattar,R.
  TITLE     The Human Integrator Complex Facilitates Transcriptional Elongation
            by Endonucleolytic Cleavage of Nascent Transcripts
  JOURNAL   Cell Rep 32 (3), 107917 (2020)
   PUBMED   32697989
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Sabath,K., Staubli,M.L., Marti,S., Leitner,A., Moes,M. and Jonas,S.
  TITLE     INTS10-INTS13-INTS14 form a functional module of Integrator that
            binds nucleic acids and the cleavage module
  JOURNAL   Nat Commun 11 (1), 3422 (2020)
   PUBMED   32647223
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI599533.1, AK056149.1, CA454040.1 and BM977018.1.
            
            On Jun 10, 2002 this sequence version replaced NP_076972.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.330641.1,
                                           SRR3476690.782506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000344417.10/ ENSP00000340220.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..449
                     /product="integrator complex subunit 15 isoform 1"
                     /note="uncharacterized protein C7orf26"
                     /calculated_mol_wt=49916
     Region          2..381
                     /region_name="DUF4507"
                     /note="Domain of unknown function (DUF4507); pfam14964"
                     /db_xref="CDD:464409"
     CDS             1..449
                     /gene="INTS15"
                     /gene_synonym="C7orf26"
                     /coded_by="NM_024067.4:264..1613"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5353.1"
                     /db_xref="GeneID:79034"
                     /db_xref="HGNC:HGNC:21702"
                     /db_xref="MIM:621239"
ORIGIN      
        1 msdirhsllr rdalsaakev lyhldiyfss qlqsaplpiv dkgpvellee fvfqvpkers
       61 aqpkrlnslq elqlleimcn yfqeqtkdsv rqiifsslfs pqgnkaddsr msllgklvsm
      121 avavcripvl ecaaswlqrt pvvycvrlak alvddycclv pgsiqtlkqi fsasprfccq
      181 fitsvtalyd lssddlippm dllemivtwi fedprlilit flntpiaanl pigfleltpl
      241 vglirwcvka playkrkkkp plsnghvsnk vtkdpgvgmd rdshllyskl hlsvlqvlmt
      301 lqlhlteknl ygrlglilfd hmvplveein rladelnpln asqeielsld rlaqalqvam
      361 asgallctrd dlrtlcsrlp hnnllqlvis gpvqqsphaa lppgfyphih tpplgygavp
      421 ahpaahpalp thpghtfisg vtfpfrpir
//
LOCUS       NP_060289                403 aa            linear   PRI 20-NOV-2025
DEFINITION  tRNA methyltransferase 10 homolog C precursor [Homo sapiens].
ACCESSION   NP_060289
VERSION     NP_060289.2
DBSOURCE    REFSEQ: accession NM_017819.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Valentin Gese,G. and Hallberg,B.M.
  TITLE     Structural basis of 3'-tRNA maturation by the human mitochondrial
            RNase Z complex
  JOURNAL   EMBO J 43 (24), 6573-6590 (2024)
   PUBMED   39516281
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Meynier,V., Hardwick,S.W., Catala,M., Roske,J.J., Oerum,S.,
            Chirgadze,D.Y., Barraud,P., Yue,W.W., Luisi,B.F. and Tisne,C.
  TITLE     Structural basis for human mitochondrial tRNA maturation
  JOURNAL   Nat Commun 15 (1), 4683 (2024)
   PUBMED   38824131
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Bhatta,A., Dienemann,C., Cramer,P. and Hillen,H.S.
  TITLE     Structural basis of RNA processing by human mitochondrial RNase P
  JOURNAL   Nat Struct Mol Biol 28 (9), 713-723 (2021)
   PUBMED   34489609
  REMARK    GeneRIF: Structural basis of RNA processing by human mitochondrial
            RNase P.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Sanchez,M.I., Mercer,T.R., Davies,S.M., Shearwood,A.M.,
            Nygard,K.K., Richman,T.R., Mattick,J.S., Rackham,O. and
            Filipovska,A.
  TITLE     RNA processing in human mitochondria
  JOURNAL   Cell Cycle 10 (17), 2904-2916 (2011)
   PUBMED   21857155
  REMARK    GeneRIF: MRPP1 is essential for transcript processing, RNA
            modification, translation and mitochondrial respiration.
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Brzezniak,L.K., Bijata,M., Szczesny,R.J. and Stepien,P.P.
  TITLE     Involvement of human ELAC2 gene product in 3' end processing of
            mitochondrial tRNAs
  JOURNAL   RNA Biol 8 (4), 616-626 (2011)
   PUBMED   21593607
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Holzmann,J., Frank,P., Loffler,E., Bennett,K.L., Gerner,C. and
            Rossmanith,W.
  TITLE     RNase P without RNA: identification and functional reconstitution
            of the human mitochondrial tRNA processing enzyme
  JOURNAL   Cell 135 (3), 462-474 (2008)
   PUBMED   18984158
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC035967.1 and BU619586.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 9, 2006 this sequence version replaced NP_060289.1.
            
            Summary: This gene encodes the precursor of a subunit of the
            mitochondrial ribonuclease P, which is involved in 5' processing of
            mitochondrial tRNAs. The encoded protein may confer RNA-binding
            capacity to mitochondrial ribonuclease P and may be essential for
            transcript processing, RNA modification, translation and
            mitochondrial respiration. [provided by RefSeq, Nov 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF226052.1, BC035967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000309922.7/
                                                  ENSP00000312356.6
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q12.3"
     Protein         1..403
                     /product="tRNA methyltransferase 10 homolog C precursor"
                     /EC_number="2.1.1.218"
                     /EC_number="2.1.1.221"
                     /note="mitochondrial ribonuclease P protein 1; renal
                     carcinoma antigen NY-REN-49; HBV pre-S2 trans-regulated
                     protein 2; RNA (guanine-9-) methyltransferase domain
                     containing 1; mitochondrial RNase P subunit 1; tRNA
                     methyltransferase 10 homolog C; tRNA
                     (adenine(9)-N(1))-methyltransferase; tRNA
                     (guanine(9)-N(1))-methyltransferase; mRNA
                     methyladenosine-N(1)-methyltransferase"
                     /calculated_mol_wt=42603
     transit_peptide 1..39
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q7L0Y3.2)"
                     /calculated_mol_wt=4762
     mat_peptide     40..403
                     /product="tRNA methyltransferase 10 homolog C.
                     /id=PRO_0000311309"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L0Y3.2)"
                     /calculated_mol_wt=42603
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UFY8; propagated from
                     UniProtKB/Swiss-Prot (Q7L0Y3.2)"
     Region          203..380
                     /region_name="Trm10_MRRP1"
                     /note="Mitochondrial ribonuclease P protein 1; cd18102"
                     /db_xref="CDD:349975"
     Site            order(290..292,309..310,312,314,335..336,338,350..351,353,
                     356)
                     /site_type="other"
                     /note="SAM binding site [chemical binding]"
                     /db_xref="CDD:349975"
     CDS             1..403
                     /gene="TRMT10C"
                     /gene_synonym="COXPD30; HNYA; MRPP1; RG9MTD1"
                     /coded_by="NM_017819.4:149..1360"
                     /db_xref="CCDS:CCDS43122.1"
                     /db_xref="GeneID:54931"
                     /db_xref="HGNC:HGNC:26022"
                     /db_xref="MIM:615423"
ORIGIN      
        1 maaflkmsvs vnffrpftrf lvpftlhrkr nnltilqrym sskipavtyp knestppsee
       61 leldkwkttm kssvqeecvs tissskdedp laatrefiem wrllgrevpe hiteeelktl
      121 mecvsntakk kylkylytke kvkkarqikk emkaaareea knikllette edkqknflfl
      181 rlwdrnmdia mgwkgaqamq fgqplvfdma yenymkrkel qntvsqlles egwnrrnvdp
      241 fhiyfcnlki dgalhrelvk ryqekwdkll ltstekshvd lfpkdsiiyl tadspnvmtt
      301 frhdkvyvig sfvdksmqpg tslakakrln lateclpldk ylqweignkn ltldqmiril
      361 lclknngnwq ealqfvpkrk htgfleisqh sqefinrlkk akt
//
LOCUS       NP_683704                719 aa            linear   PRI 20-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform b [Homo
            sapiens].
ACCESSION   NP_683704
VERSION     NP_683704.2
DBSOURCE    REFSEQ: accession NM_148906.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 719)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB081133.1, AY178997.1,
            AL050343.17 and EL953716.1.
            
            On Oct 5, 2010 this sequence version replaced NP_683704.1.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and 5'
            coding region, uses an alternate start codon, and includes an
            alternate in-frame exon in the central coding region, compared to
            variant 1. The encoded isoform (b) has a longer and distinct
            N-terminus, compared to isoform a. Isoform b contains both a
            pleckstrin homology domain and a sterol-binding domain.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. This
            transcript contains a uAUG that would result in an 18 aa N-terminal
            extension, but it has a weak Kozak signal, is not supported by the
            vast majority of human and homologous transcripts, and dAUG use is
            supported by data in PMID:19413330, which selectively purifies
            acetylated protein N-termini and shows that Ala-2 is acetylated
            following cleavage of Met-1 as encoded by the dAUG.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY178997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2162568
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:19413330)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..719
                     /product="oxysterol-binding protein-related protein 9
                     isoform b"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=81035
     Region          5..89
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          360..706
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..719
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_148906.3:20..2179"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS41333.2"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 masimegpls kwtnvmkgwq yrwfvldyna gllsyytgav igiddeddst ftitvdqktf
       61 hfqardader ekwihaleet ilrhtlqlqg ldsgfvpsvq dfdkkltead aylqilieql
      121 klfddklqnc kedeqrkkie tlkettnsmv esikhcivll qiakdqsnae khadgmisti
      181 npvdaiyqps plepvistmp sqtvlppepv qlckseqrps slpvgpvlat lghhqtptpn
      241 stgsghspps ssltspshvn lspntvpefs ysssedefyd adefhqsgss pkrlidssgs
      301 asvlthsssg nslkrpdtte slnsslsngt sdadlfdshd drdddaeags veehksvimh
      361 llsqvrlgmd ltkvvlptfi lerrsllemy adffahpdlf vsisdqkdpk drmvqvvkwy
      421 lsafhagrkg svakkpynpi lgeifqchwt lpndteente lvsegpvpwv sknsvtfvae
      481 qvshhppisa fyaecfnkki qfnahiwtks kflgmsigvh nigqgcvscl dydehyiltf
      541 pngygrsilt vpwvelggec nincsktgys aniifhtkpf yggkkhrita eifspndkks
      601 fcsiegewng vmyakyatge ntvfvdtkkl piikkkvrkl edqneyesrs lwkdvtfnlk
      661 irdidaatea khrleerqra earerkekei qwetrlfhed gecwvydepl lkrlgaakh
//
LOCUS       NP_598344                444 aa            linear   PRI 20-NOV-2025
DEFINITION  synapsin-3 isoform IIIc [Homo sapiens].
ACCESSION   NP_598344
VERSION     NP_598344.2
DBSOURCE    REFSEQ: accession NM_133633.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Baris,R.O., Sahin,N., Bilgic,A.D., Ozdemir,C. and Edgunlu,T.G.
  TITLE     Molecular and in silico analyses of SYN III gene variants in autism
            spectrum disorder
  JOURNAL   Ir J Med Sci 192 (6), 2887-2895 (2023)
   PUBMED   37166614
  REMARK    GeneRIF: Molecular and in silico analyses of SYN III gene variants
            in autism spectrum disorder.
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Bolat,H., Unsel-Bolat,G., Ozgul,S., Pariltay,E., Tahillioglu,A.,
            Rohde,L.A., Akin,H. and Ercan,E.S.
  TITLE     Investigation of possible associations of the BDNF, SNAP-25 and SYN
            III genes with the neurocognitive measures: BDNF and SNAP-25 genes
            might be involved in attention domain, SYN III gene in executive
            function
  JOURNAL   Nord J Psychiatry 76 (8), 610-615 (2022)
   PUBMED   35077325
  REMARK    GeneRIF: Investigation of possible associations of the BDNF,
            SNAP-25 and SYN III genes with the neurocognitive measures: BDNF
            and SNAP-25 genes might be involved in attention domain, SYN III
            gene in executive function.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Longhena,F., Faustini,G., Varanita,T., Zaltieri,M., Porrini,V.,
            Tessari,I., Poliani,P.L., Missale,C., Borroni,B., Padovani,A.,
            Bubacco,L., Pizzi,M., Spano,P. and Bellucci,A.
  TITLE     Synapsin III is a key component of alpha-synuclein fibrils in Lewy
            bodies of PD brains
  JOURNAL   Brain Pathol 28 (6), 875-888 (2018)
   PUBMED   29330884
  REMARK    GeneRIF: Synapsin III is a crucial alpha-synuclein interactant and
            a key component of Lewy bodies fibrils in the brain of patients
            affected by Parkinson's disease.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Porton,B., Ferreira,A., DeLisi,L.E. and Kao,H.T.
  TITLE     A rare polymorphism affects a mitogen-activated protein kinase site
            in synapsin III: possible relationship to schizophrenia
  JOURNAL   Biol Psychiatry 55 (2), 118-125 (2004)
   PUBMED   14732590
  REMARK    GeneRIF: A missense polymorphism, S470N, was identified in the
            synapsin III gene and appeared more frequently in individuals with
            schizophrenia. The site affected by the polymorphism, Ser470, was
            determined to be a substrate for mitogen-activated protein kinase.
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Tsai,M.T., Hung,C.C., Tsai,C.Y., Liu,M.Y., Su,Y.C., Chen,Y.H.,
            Hsiao,K.J. and Chen,C.H.
  TITLE     Mutation analysis of synapsin III gene in schizophrenia
  JOURNAL   Am J Med Genet 114 (1), 79-83 (2002)
   PUBMED   11840510
  REMARK    GeneRIF: Evidence is not in favor of a large effect of synapsin III
            gene in the pathogenesis of schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Kao,H.T., Porton,B., Hilfiker,S., Stefani,G., Pieribone,V.A.,
            DeSalle,R. and Greengard,P.
  TITLE     Molecular evolution of the synapsin gene family
  JOURNAL   J Exp Zool 285 (4), 360-377 (1999)
   PUBMED   10578110
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Porton,B., Kao,H.T. and Greengard,P.
  TITLE     Characterization of transcripts from the synapsin III gene locus
  JOURNAL   J Neurochem 73 (6), 2266-2271 (1999)
   PUBMED   10582583
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Kao,H.T., Porton,B., Czernik,A.J., Feng,J., Yiu,G., Haring,M.,
            Benfenati,F. and Greengard,P.
  TITLE     A third member of the synapsin gene family
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4667-4672 (1998)
   PUBMED   9539796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83846.1, Z98256.1, Z82246.2,
            Z80902.2, Z82181.2 and Z71183.2.
            
            On Oct 11, 2008 this sequence version replaced NP_598344.1.
            
            Summary: This gene is a member of the synapsin gene family.
            Synapsins encode neuronal phosphoproteins which associate with the
            cytoplasmic surface of synaptic vesicles. Family members are
            characterized by common protein domains, and they are implicated in
            synaptogenesis and the modulation of neurotransmitter release,
            suggesting a potential role in several neuropsychiatric diseases.
            The protein encoded by this gene shares the synapsin family domain
            model, with domains A, C, and E exhibiting the highest degree of
            conservation. The protein contains a unique domain J, located
            between domains C and E. Based on this gene's localization to
            22q12.3, a possible schizophrenia susceptibility locus, and the
            established neurobiological roles of the synapsins, this family
            member may represent a candidate gene for schizophrenia. The TIMP3
            gene is located within an intron of this gene and is transcribed in
            the opposite direction. Alternative splicing of this gene results
            in multiple splice variants that encode different isoforms.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1968540
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..444
                     /product="synapsin-3 isoform IIIc"
                     /note="synapsin-3; cN28H9.2 (synapsin III)"
                     /calculated_mol_wt=48856
     Region          1..29
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and CaMK1.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          19..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          28..90
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          91..399
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          92..191
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          193..395
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     CDS             1..444
                     /gene="SYN3"
                     /coded_by="NM_133633.3:160..1494"
                     /note="isoform IIIc is encoded by transcript variant IIIc"
                     /db_xref="GeneID:8224"
                     /db_xref="HGNC:HGNC:11496"
                     /db_xref="MIM:602705"
ORIGIN      
        1 mnflrrrlsd ssfmanlpng ymtdlqrpds stsspaspam errhpqplaa sfsspgsslf
       61 sslssamkqa pqatsglmep pgpstpivqr prillvidda htdwskyfhg kkvngeieir
      121 veqaefseln laayvtggcm vdmqvvrngt kvvsrsfkpd filvrqhays malgedyrsl
      181 viglqygglp avnslysvyn fcskpwvfsq likifhslgp ekfplveqtf fpnhkpmvta
      241 phfpvvvklg hahagmgkik venqldfqdi tsvvamakty atteafidsk ydiriqkigs
      301 nykaymrtsi sgnwkantgs amleqvamte ryrlwvdscs emfggldica vkavhskdgr
      361 dyiievmdss mpligehvee drqlmadlvv skmsqlpmpg gtapsplrpw apqiksaksp
      421 gqaqlgpqlg qpqprpppqa nlsp
//
LOCUS       NP_001008214             577 aa            linear   PRI 20-NOV-2025
DEFINITION  optineurin [Homo sapiens].
ACCESSION   NP_001008214
VERSION     NP_001008214.1
DBSOURCE    REFSEQ: accession NM_001008213.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Nan,H., Kim,Y.J., Chu,M., Li,D., Li,J., Jiang,D., Wu,Y., Ohtsuka,T.
            and Wu,L.
  TITLE     Genetic and clinical landscape of Chinese frontotemporal dementia:
            dominance of TBK1 and OPTN mutations
  JOURNAL   Alzheimers Res Ther 16 (1), 127 (2024)
   PUBMED   38872230
  REMARK    GeneRIF: Genetic and clinical landscape of Chinese frontotemporal
            dementia: dominance of TBK1 and OPTN mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Jin,J., Huang,R., Chang,Y. and Yi,X.
  TITLE     Roles and mechanisms of optineurin in bone metabolism
  JOURNAL   Biomed Pharmacother 172, 116258 (2024)
   PUBMED   38350370
  REMARK    GeneRIF: Roles and mechanisms of optineurin in bone metabolism.
            Review article
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Yamano,K., Sawada,M., Kikuchi,R., Nagataki,K., Kojima,W., Endo,R.,
            Kinefuchi,H., Sugihara,A., Fujino,T., Watanabe,A., Tanaka,K.,
            Hayashi,G., Murakami,H. and Matsuda,N.
  TITLE     Optineurin provides a mitophagy contact site for TBK1 activation
  JOURNAL   EMBO J 43 (5), 754-779 (2024)
   PUBMED   38287189
  REMARK    GeneRIF: Optineurin provides a mitophagy contact site for TBK1
            activation.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   D'Urso,B., Weil,R. and Genin,P.
  TITLE     [Optineurin and mitochondrial dysfunction in neurodegeneration]
  JOURNAL   Med Sci (Paris) 40 (2), 167-175 (2024)
   PUBMED   38411425
  REMARK    GeneRIF: [Optineurin and mitochondrial dysfunction in
            neurodegeneration].
            Review article
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Fong,K.S. and de Couet,H.G.
  TITLE     Novel proteins interacting with the leucine-rich repeat domain of
            human flightless-I identified by the yeast two-hybrid system
  JOURNAL   Genomics 58 (2), 146-157 (1999)
   PUBMED   10366446
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Sarfarazi,M., Child,A., Stoilova,D., Brice,G., Desai,T.,
            Trifan,O.C., Poinoosawmy,D. and Crick,R.P.
  TITLE     Localization of the fourth locus (GLC1E) for adult-onset primary
            open-angle glaucoma to the 10p15-p14 region
  JOURNAL   Am J Hum Genet 62 (3), 641-652 (1998)
   PUBMED   9497264
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Li,Y., Kang,J. and Horwitz,M.S.
  TITLE     Interaction of an adenovirus E3 14.7-kilodalton protein with a
            novel tumor necrosis factor alpha-inducible cellular protein
            containing leucine zipper domains
  JOURNAL   Mol Cell Biol 18 (3), 1601-1610 (1998)
   PUBMED   9488477
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552635.1, AF420371.1,
            BC032762.1 and AF070533.1.
            
            Summary: This gene encodes the coiled-coil containing protein
            optineurin. Optineurin may play a role in normal-tension glaucoma
            and adult-onset primary open angle glaucoma. Optineurin interacts
            with adenovirus E3-14.7K protein and may utilize tumor necrosis
            factor-alpha or Fas-ligand pathways to mediate apoptosis,
            inflammation or vasoconstriction. Optineurin may also function in
            cellular morphogenesis and membrane trafficking, vesicle
            trafficking, and transcription activation through its interactions
            with the RAB8, huntingtin, and transcription factor IIIA proteins.
            Alternative splicing results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.139115.1,
                                           SRR1660805.115899.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..577
                     /product="optineurin"
                     /note="nemo-related protein; tumor necrosis factor
                     alpha-inducible cellular protein containing leucine zipper
                     domains; transcrption factor IIIA-interacting protein;
                     Huntingtin interacting protein L; FIP-2; HIP-7; huntingtin
                     yeast partner L; E3-14.7K-interacting protein;
                     huntingtin-interacting protein 7; huntingtin-interacting
                     protein L; optic neuropathy-inducing protein;
                     transcription factor IIIA-interacting protein"
                     /calculated_mol_wt=65791
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          37..103
                     /region_name="NEMO"
                     /note="NF-kappa-B essential modulator NEMO; pfam11577"
                     /db_xref="CDD:431942"
     Region          58..209
                     /region_name="Interaction with Rab8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          101..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          176..181
                     /region_name="LIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21617041,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          186..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          245..>520
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          261..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          408..507
                     /region_name="CC2-LZ"
                     /note="Leucine zipper of domain CC2 of NEMO, NF-kappa-B
                     essential modulator; pfam16516"
                     /db_xref="CDD:465155"
     Region          411..577
                     /region_name="Interaction with HD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          412..520
                     /region_name="Interaction with MYO6.
                     /evidence=ECO:0000269|PubMed:15837803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          474..479
                     /region_name="UBAN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          551..576
                     /region_name="zf_C2H2_10"
                     /note="C2H2 type zinc-finger; pfam18414"
                     /db_xref="CDD:436483"
     CDS             1..577
                     /gene="OPTN"
                     /gene_synonym="ALS12; FIP2; GLC1E; HIP7; HYPL; NRP;
                     TFIIIA-INTP"
                     /coded_by="NM_001008213.1:439..2172"
                     /db_xref="CCDS:CCDS7094.1"
                     /db_xref="GeneID:10133"
                     /db_xref="HGNC:HGNC:17142"
                     /db_xref="MIM:602432"
ORIGIN      
        1 mshqplsclt ekedspsest gngpphlahp nldtftpeel lqqmkellte nhqlkeamkl
       61 nnqamkgrfe elsawtekqk eerqffeiqs keakerlmal sheneklkee lgklkgkser
      121 ssedptddsr lpraeaeqek dqlrtqvvrl qaekadllgi vselqlklns sgssedsfve
      181 irmaegeaeg svkeikhspg ptrtvstgta lskyrsrsad gaknyfehee ltvsqlllcl
      241 regnqkverl evalkeaker vsdfekktsn rseietqteg stekendeek gpetvgseve
      301 alnlqvtslf kelqeahtkl seaelmkkrl qekcqalerk nsaipselne kqelvytnkk
      361 lelqvesmls eikmeqakte dekskltvlq mthnkllqeh nnalktieel trkesekvdr
      421 avlkelsekl elaekalask qlqmdemkqt iakqeedlet mtilraqmev ycsdfhaera
      481 arekiheeke qlalqlavll kendafedgg rqslmemqsr hgartsdsdq qaylvqrgae
      541 drdwrqqrni pihscpkcge vlpdidtlqi hvmdcii
//
LOCUS       NP_009144                178 aa            linear   PRI 20-NOV-2025
DEFINITION  PRA1 family protein 2 [Homo sapiens].
ACCESSION   NP_009144
VERSION     NP_009144.1
DBSOURCE    REFSEQ: accession NM_007213.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Da Silva,E., Scott,M.G.H., Enslen,H. and Marullo,S.
  TITLE     Control of CCR5 Cell-Surface Targeting by the PRAF2 Gatekeeper
  JOURNAL   Int J Mol Sci 24 (24), 17438 (2023)
   PUBMED   38139265
  REMARK    GeneRIF: Control of CCR5 Cell-Surface Targeting by the PRAF2
            Gatekeeper.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Qian,Z., Wei,B., Zhou,Y., Wang,Q., Wang,J., Sun,Y., Gao,Y. and
            Chen,X.
  TITLE     PRAF2 overexpression predicts poor prognosis and promotes
            tumorigenesis in esophageal squamous cell carcinoma
  JOURNAL   BMC Cancer 19 (1), 585 (2019)
   PUBMED   31200670
  REMARK    GeneRIF: PRAF2 could be used as a potential prognostic biomarker
            and represent a potential therapeutic target for ESCC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Koomoa,D.L., Go,R.C., Wester,K. and Bachmann,A.S.
  TITLE     Expression profile of PRAF2 in the human brain and enrichment in
            synaptic vesicles
  JOURNAL   Neurosci Lett 436 (2), 171-176 (2008)
   PUBMED   18395978
  REMARK    GeneRIF: The expression of PRAF2 in specific regions of the brain
            including SVs suggest an important physiological function for this
            novel protein, possibly by participating in multiple aspects of SV
            maturation, transport, and signal transmission.
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Geerts,D., Wallick,C.J., Koomoa,D.L., Koster,J., Versteeg,R.,
            Go,R.C. and Bachmann,A.S.
  TITLE     Expression of prenylated Rab acceptor 1 domain family, member 2
            (PRAF2) in neuroblastoma: correlation with clinical features,
            cellular localization, and cerulenin-mediated apoptosis regulation
  JOURNAL   Clin Cancer Res 13 (21), 6312-6319 (2007)
   PUBMED   17975142
  REMARK    GeneRIF: PRAF2 has a role in progression of neuroblastoma
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Fo,C.S., Coleman,C.S., Wallick,C.J., Vine,A.L. and Bachmann,A.S.
  TITLE     Genomic organization, expression profile, and characterization of
            the new protein PRA1 domain family, member 2 (PRAF2)
  JOURNAL   Gene 371 (1), 154-165 (2006)
   PUBMED   16481131
  REMARK    GeneRIF: CCR5-interacting PRAF2 protein is expressed in several
            human tissues with a possible function in ER/Golgi transport and
            vesicular traffic.
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Schweneker,M., Bachmann,A.S. and Moelling,K.
  TITLE     JM4 is a four-transmembrane protein binding to the CCR5 receptor
  JOURNAL   FEBS Lett 579 (7), 1751-1758 (2005)
   PUBMED   15757671
  REMARK    GeneRIF: PRAF2 (JM4) is CCR5-interacting protein, which is
            suggested to function in trafficking and membrane localisation of
            the receptor.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AJ005896.1 and AC231657.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ005896.1, SRR1660807.243742.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000553851.3/ ENSP00000451962.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..178
                     /product="PRA1 family protein 2"
                     /note="Jena-Muenchen 4"
                     /calculated_mol_wt=19127
     Region          4..148
                     /region_name="PRA1"
                     /note="PRA1 family protein; pfam03208"
                     /db_xref="CDD:460846"
     Site            42..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60831.1)"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60831.1)"
     Site            97..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60831.1)"
     Site            123..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60831.1)"
     CDS             1..178
                     /gene="PRAF2"
                     /gene_synonym="JM4; Yip6a"
                     /coded_by="NM_007213.3:16..552"
                     /db_xref="CCDS:CCDS14317.1"
                     /db_xref="GeneID:11230"
                     /db_xref="HGNC:HGNC:28911"
                     /db_xref="MIM:300840"
ORIGIN      
        1 msevrlpplr alddfvlgsa rlaapdpcdp qrwchrvinn llyyqtnyll cfgiglalag
       61 yvrplhtlls alvvavalgv lvwaaetraa vrrcrrshpa aclaavlavg llvlwvagga
      121 ctflfsiagp vllilvhasl rlrnlknkie nkiesiglkr tpmgllleal gqeqeags
//
LOCUS       NP_001352507             474 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein 45 isoform 1 [Homo sapiens].
ACCESSION   NP_001352507 XP_016858811
VERSION     NP_001352507.1
DBSOURCE    REFSEQ: accession NM_001365578.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Wang,C., Chen,Z., Yi,Y., Ding,Y., Xu,F., Kang,H., Lin,K., Shu,X.,
            Zhong,Z., Zhang,Z., Liu,J., Xu,Z., Liu,L., He,X., Chang,Y. and
            Zhao,Q.
  TITLE     RBM45 reprograms lipid metabolism promoting hepatocellular
            carcinoma via Rictor and ACSL1/ACSL4
  JOURNAL   Oncogene 43 (5), 328-340 (2024)
   PUBMED   38040804
  REMARK    GeneRIF: RBM45 reprograms lipid metabolism promoting hepatocellular
            carcinoma via Rictor and ACSL1/ACSL4.
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Wang,R., Sun,H., Chen,W., Zhao,B. and Chen,L.
  TITLE     Molecular basis of ssDNA recognition by RBM45 protein of
            neurodegenerative disease from multiple molecular dynamics
            simulations and energy predictions
  JOURNAL   J Mol Graph Model 118, 108377 (2023)
   PUBMED   36435031
  REMARK    GeneRIF: Molecular basis of ssDNA recognition by RBM45 protein of
            neurodegenerative disease from multiple molecular dynamics
            simulations and energy predictions.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   van der Zee,J., Dillen,L., Baradaran-Heravi,Y., Gossye,H.,
            Kocoglu,C., Cuyt,I., Dermaut,B., Sieben,A., Baets,J., De Jonghe,P.,
            Vandenberghe,R., De Deyn,P., Cras,P., Engelborghs,S. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU Consortium
  TITLE     Family-based exome sequencing identifies RBM45 as a possible
            candidate gene for frontotemporal dementia and amyotrophic lateral
            sclerosis
  JOURNAL   Neurobiol Dis 156, 105421 (2021)
   PUBMED   34118419
  REMARK    GeneRIF: Family-based exome sequencing identifies RBM45 as a
            possible candidate gene for frontotemporal dementia and amyotrophic
            lateral sclerosis.
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Collins,M., Riascos,D., Kovalik,T., An,J., Krupa,K., Krupa,K.,
            Hood,B.L., Conrads,T.P., Renton,A.E., Traynor,B.J. and Bowser,R.
  TITLE     The RNA-binding motif 45 (RBM45) protein accumulates in inclusion
            bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal
            lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients
  JOURNAL   Acta Neuropathol 124 (5), 717-732 (2012)
   PUBMED   22993125
  REMARK    GeneRIF: This study demonistrated that RBM45 protein accumulates in
            inclusion bodies in amyotrophic lateral sclerosis (ALS) and
            frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP)
            patients.
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Chu,X., Pan,C.M., Zhao,S.X., Liang,J., Gao,G.Q., Zhang,X.M.,
            Yuan,G.Y., Li,C.G., Xue,L.Q., Shen,M., Liu,W., Xie,F., Yang,S.Y.,
            Wang,H.F., Shi,J.Y., Sun,W.W., Du,W.H., Zuo,C.L., Shi,J.X.,
            Liu,B.L., Guo,C.C., Zhan,M., Gu,Z.H., Zhang,X.N., Sun,F.,
            Wang,Z.Q., Song,Z.Y., Zou,C.Y., Sun,W.H., Guo,T., Cao,H.M.,
            Ma,J.H., Han,B., Li,P., Jiang,H., Huang,Q.H., Liang,L., Liu,L.B.,
            Chen,G., Su,Q., Peng,Y.D., Zhao,J.J., Ning,G., Chen,Z., Chen,J.L.,
            Chen,S.J., Huang,W. and Song,H.D.
  CONSRTM   China Consortium for Genetics of Autoimmune Thyroid Disease
  TITLE     A genome-wide association study identifies two new risk loci for
            Graves' disease
  JOURNAL   Nat Genet 43 (9), 897-901 (2011)
   PUBMED   21841780
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Tamada,H., Sakashita,E., Shimazaki,K., Ueno,E., Hamamoto,T.,
            Kagawa,Y. and Endo,H.
  TITLE     cDNA cloning and characterization of Drb1, a new member of RRM-type
            neural RNA-binding protein
  JOURNAL   Biochem Biophys Res Commun 297 (1), 96-104 (2002)
   PUBMED   12220514
  REMARK    GeneRIF: a new member of RRM-type neural RNA-binding protein
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI763677.1, BC066549.1 and
            AC011238.8.
            
            On Sep 3, 2018 this sequence version replaced XP_016858811.1.
            
            Summary: This gene encodes a member of the RNA recognition motif
            (RRM)-type RNA-binding family of proteins. This protein exhibits
            preferential binding to poly(C) RNA. Initial cloning of this gene
            found that the rat ortholog was dynamically expressed in the
            developing rat brain. This protein has been localized to inclusion
            bodies in the brain and spinal cord of amyotrophic lateral
            sclerosis and Alzheimer's patients. A pseudogene has been
            identified on chromosome 8. [provided by RefSeq, Feb 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.246807.1,
                                           SRR1803616.61860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.2"
     Protein         1..474
                     /product="RNA-binding protein 45 isoform 1"
                     /note="RNA-binding protein 45; putative RNA binding
                     protein RB-1; developmentally regulated RNA-binding
                     protein 1"
                     /calculated_mol_wt=53215
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUH3.1)"
     Region          23..104
                     /region_name="RRM1_RBM45"
                     /note="RNA recognition motif 1 (RRM1) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12366"
                     /db_xref="CDD:409801"
     Region          120..193
                     /region_name="RRM2_RBM45"
                     /note="RNA recognition motif 2 (RRM2) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12367"
                     /db_xref="CDD:409802"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHN5; propagated from
                     UniProtKB/Swiss-Prot (Q8IUH3.1)"
     Region          246..318
                     /region_name="RRM3_RBM45"
                     /note="RNA recognition motif 3 (RRM3) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12368"
                     /db_xref="CDD:409803"
     Region          391..458
                     /region_name="RRM4_RBM45"
                     /note="RNA recognition motif 4 (RRM4) found in RNA-binding
                     protein 45 (RBM45) and similar proteins; cd12369"
                     /db_xref="CDD:409804"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUH3.1)"
     CDS             1..474
                     /gene="RBM45"
                     /gene_synonym="DRB1; RB-1"
                     /coded_by="NM_001365578.1:111..1535"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33335.1"
                     /db_xref="GeneID:129831"
                     /db_xref="HGNC:HGNC:24468"
                     /db_xref="MIM:608888"
ORIGIN      
        1 mdeagssasg ggfrpgvdsl deppnsrifl viskytpesv lrerfspfgd iqdiwvvrdk
       61 htkeskgiaf vkfarssqac rameemhgqc lgpndtkpik vfiaqsrssg shrdvedeel
      121 trifvmipks yteedlrekf kvygdieycs iiknkvtges kglgyvrylk psqaaqaien
      181 cdrsfraila epknkasess eqdyysnmrq ealgheprvn mfpfeqqsef ssfdkndsrg
      241 qeaiskrlsv vsrvpfteeq lfsifdivpg leycevqrdp ysnyghgvvq yfnvasaiya
      301 kyklhgfqyp pgnrigvsfi ddgsnatdll rkmatqmvaa qlasmvwnnp sqqqfmqfgg
      361 ssgsqlpqiq tdvvlpsckk kapaetpvke rlfivfnphp lpldvledif crfgnlievy
      421 lvsgknvgya kyadrisand aiatlhgkil ngvrlkvmla dspreesnkr qrty
//
LOCUS       NP_060009               4116 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein axonemal heavy chain 3 isoform 1 [Homo sapiens].
ACCESSION   NP_060009
VERSION     NP_060009.1
DBSOURCE    REFSEQ: accession NM_017539.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4116)
  AUTHORS   Wang,X., Shen,G., Yang,Y., Jiang,C., Ruan,T., Yang,X., Zhuo,L.,
            Zhang,Y., Ou,Y., Zhao,X., Long,S., Tang,X., Lin,T. and Shen,Y.
  TITLE     DNAH3 deficiency causes flagellar inner dynein arm loss and male
            infertility in humans and mice
  JOURNAL   Elife 13, 96755 (2024)
   PUBMED   39503742
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4116)
  AUTHORS   Li,S., Zhang,Z., Xie,L., Zhao,Y., Chen,H., Zhang,S., Cai,Y.,
            Ren,B., Liu,W., Tang,S. and Sha,Y.
  TITLE     Novel bi-allelic DNAH3 variants cause oligoasthenoteratozoospermia
  JOURNAL   Front Endocrinol (Lausanne) 15, 1462509 (2024)
   PUBMED   39588341
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4116)
  AUTHORS   Meng,G.Q., Wang,Y., Luo,C., Tan,Y.M., Li,Y., Tan,C., Tu,C.,
            Zhang,Q.J., Hu,L., Zhang,H., Meng,L.L., Liu,C.Y., Deng,L., Lu,G.X.,
            Lin,G., Du,J., Tan,Y.Q., Sha,Y., Wang,L. and He,W.B.
  TITLE     Bi-allelic variants in DNAH3 cause male infertility with
            asthenoteratozoospermia in humans and mice
  JOURNAL   Hum Reprod Open 2024 (1), hoae003 (2024)
   PUBMED   38312775
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 4116)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   5  (residues 1 to 4116)
  AUTHORS   Maiti,A.K., Mattei,M.G., Jorissen,M., Volz,A., Zeigler,A. and
            Bouvagnet,P.
  TITLE     Identification, tissue specific expression, and chromosomal
            localisation of several human dynein heavy chain genes
  JOURNAL   Eur J Hum Genet 8 (12), 923-932 (2000)
   PUBMED   11175280
REFERENCE   6  (residues 1 to 4116)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   7  (residues 1 to 4116)
  AUTHORS   Milisav,I.
  TITLE     Dynein and dynein-related genes
  JOURNAL   Cell Motil Cytoskeleton 39 (4), 261-272 (1998)
   PUBMED   9556328
  REMARK    Review article
REFERENCE   8  (residues 1 to 4116)
  AUTHORS   Neesen,J., Koehler,M.R., Kirschner,R., Steinlein,C.,
            Kreutzberger,J., Engel,W. and Schmid,M.
  TITLE     Identification of dynein heavy chain genes expressed in human and
            mouse testis: chromosomal localization of an axonemal dynein gene
  JOURNAL   Gene 200 (1-2), 193-202 (1997)
   PUBMED   9373155
REFERENCE   9  (residues 1 to 4116)
  AUTHORS   Chapelin,C., Duriez,B., Magnino,F., Goossens,M., Escudier,E. and
            Amselem,S.
  TITLE     Isolation of several human axonemal dynein heavy chain genes:
            genomic structure of the catalytic site, phylogenetic analysis and
            chromosomal assignment
  JOURNAL   FEBS Lett 412 (2), 325-330 (1997)
   PUBMED   9256245
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF494040.1, AC105410.1 and
            AL096732.1.
            
            Summary: This gene belongs to the dynein family, whose members
            encode large proteins that are constituents of the
            microtubule-associated motor protein complex. This complex is
            composed of dynein heavy, intermediate and light chains, which can
            be axonemal or cytoplasmic. This protein is an axonemal dynein
            heavy chain. It is involved in producing force for ciliary beating
            by using energy from ATP hydrolysis. Alternative splicing results
            in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Dec 2016].
            
            Transcript Variant: Thos variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF494040.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..4116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..4116
                     /product="dynein axonemal heavy chain 3 isoform 1"
                     /note="dynein, axonemal, heavy polypeptide 3; dynein heavy
                     chain 3, axonemal; axonemal dynein, heavy chain; ciliary
                     dynein heavy chain 3; axonemal beta dynein heavy chain 3;
                     epididymis luminal protein 36"
                     /calculated_mol_wt=470643
     Region          1..1390
                     /region_name="Stem. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          137..172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          859..1262
                     /region_name="DHC_N2"
                     /note="Dynein heavy chain, N-terminal region 2; pfam08393"
                     /db_xref="CDD:462462"
     Region          1062..3743
                     /region_name="DYN1"
                     /note="Dynein, heavy chain [Cytoskeleton]; COG5245"
                     /db_xref="CDD:227570"
     Region          1391..1717
                     /region_name="AAA_6"
                     /note="Hydrolytic ATP binding site of dynein motor region;
                     pfam12774"
                     /db_xref="CDD:463697"
     Region          1391..1612
                     /region_name="AAA 1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          1672..1903
                     /region_name="AAA 2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          2036..2284
                     /region_name="AAA 3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          2395..2646
                     /region_name="AAA 4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          2404..2664
                     /region_name="AAA_8"
                     /note="P-loop containing dynein motor region D4;
                     pfam12780"
                     /db_xref="CDD:463701"
     Region          2661..2960
                     /region_name="Stalk. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          3045..3275
                     /region_name="AAA 5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          3052..3273
                     /region_name="AAA_9"
                     /note="ATP-binding dynein motor region; pfam12781"
                     /db_xref="CDD:463702"
     Region          3488..3712
                     /region_name="AAA 6. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TD57.1)"
     Region          3811..4112
                     /region_name="Dynein_C"
                     /note="Dynein heavy chain C-terminal domain; pfam18199"
                     /db_xref="CDD:465677"
     CDS             1..4116
                     /gene="DNAH3"
                     /gene_synonym="DNAHC3-B; DNAHC3B; HDHC8; HEL-36; HSADHC3"
                     /coded_by="NM_017539.2:1..12351"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10594.1"
                     /db_xref="GeneID:55567"
                     /db_xref="HGNC:HGNC:2949"
                     /db_xref="MIM:603334"
ORIGIN      
        1 mgatgrlelt laapphpgpa fqrskaretq geeegsemqi aksdsihhms hsqgqpelpp
       61 lpasaneeps glyqtvmshs fypplmqrts wtlaapfkeq hhhrgpsdsi annyslmaqd
      121 lklkdllkvy qpatisvprd rtgqglpssg nrsssepmrk ktkfssrnke dstriklafk
      181 tsifspmkke vktsltfpgs rpmspeqqld vmlqqememe skekkpsesd leryyyyltn
      241 girkdmiape egevmvrisk lisntlltsp fleplmvvlv qekendyycs lmksivdyil
      301 mdpmerkrlf iesiprlfpq rvirapvpwh svyrsakkwn eehlhtvnpm mlrlkelwfa
      361 efrdlrfvrt aeilagklpl qpqefwdviq khcleahqtl lnkwiptcaq lftsrkehwi
      421 hfapksnyds srnieeyfas vasfmslqlr elviksledl vslfmihkdg ndfkepyqem
      481 kffipqlimi klevsepiiv fnpsfdgcwe lirdsfleii knsngipklk yiplkfsfta
      541 aaadrqcvka aepgepsmha aatamaelkg ynlllgtvna eeklvsdfli qtfkvfqknq
      601 vgpckylnvy kkyvdlldnt aeqniaaflk enhdiddfvt kinaikkrrn eiasmnitvp
      661 lamfcldata lnhdlceraq nlkdhliqfq vdvnrdtnts icnqyshiad kvsevpantk
      721 elvslieflk kssavtvfkl rrqlrdaser leflmdyadl pyqiedifdn srnlllhkrd
      781 qaemdlikrc sefelrlegy hrelesfrkr evmtteemkh nveklnelsk nlnrafaefe
      841 linkeeelle kekstypllq amlknkvpye qlwstayefs ikseewmngp lfllnaeqia
      901 eeignmwrtt ykliktlsdv paprrlaenv kikidkfkqy ipilsiscnp gmkdrhwqqi
      961 seivgyeikp tettclsnml efgfgkfvek lepigaaask eysleknldr mkldwvnvtf
     1021 sfvkyrdtdt nilcaiddiq mllddhvikt qtmcgspfik pieaecrkwe ekliriqdnl
     1081 dawlkcqatw lylepifsse diiaqmpeeg rkfgivdsyw kslmsqavkd nrilvaadqp
     1141 rmaeklqean fllediqkgl ndylekkrlf fprffflsnd elleilsetk dplrvqphlk
     1201 kcfegiakle ftdnleivgm isseketvpf iqkiypanak gmvekwlqqv eqmmlasmre
     1261 viglgieayv kvprnhwvlq wpgqvvicvs sifwtqevsq alaentlldf lkksndqiaq
     1321 ivqlvrgkls sgarltlgal tvidvhardv vaklsedrvs dlndfqwisq lryywvakdv
     1381 qvqiitteal ygyeylgnsp rlvitpltdr cyrtlmgalk lnlggapegp agtgktettk
     1441 dlakalakqc vvfncsdgld ykamgkffkg laqagawacf defnrievev lsvvaqqils
     1501 iqqaiirklk tfifegtels lnptcavfit mnpgyagrae lpdnlkalfr tvammvpdya
     1561 ligeislysm gfldsrslaq kivatyrlcs eqlssqhhyd ygmravksvl taagnlklky
     1621 peenesvlll ralldvnlak flaqdvplfq giisdlfpgv vlpkpdyevf lkvlndnikk
     1681 mklqpvpwfi gkiiqiyemm lvrhgymivg dpmggktsay kvlaaalgdl haanqmeefa
     1741 veykiinpka itmgqlygcf dqvshewmdg vlanafreqa sslsddrkwi ifdgpvdaiw
     1801 ienmntvldd nkklclmsge iiqmnskmsl ifepadleqa spatvsrcgm iymephqlgw
     1861 kplkdsymdt lpssltkehk elvndmfmwl vqpclefgrl hckfvvqtsp ihlafsmmrl
     1921 ysslldeira veeeemelge glssqqiflw lqglflfslv wtvagtinad srkkfdvffr
     1981 nlimgmddnh prpksvkltk nnifpergsi ydfyfikqas ghwetwtqyi tkeeekvpag
     2041 akvseliipt metarqsffl ktyldheipm lfvgptgtgk saitnnfllh lpkntylpnc
     2101 infsartsan qtqdiimskl drrrkglfgp pigkkavvfv ddlnmpakev ygaqppiell
     2161 rqwidhgywf dkkdttrldi vdmllvtamg ppgggrndit grftrhlnii sinafeddil
     2221 tkifssivdw hfgkgfdvmf lrygkmlvqa tktiyrdave nflptpsksh yvfnlrdfsr
     2281 viqgvllcph thlqdvekci rlwihevyrv fydrlidked rqvffnmvke ttsncfkqti
     2341 ekvlihlspt gkivddnirs lffgdyfkpe sdqkiydeit dlkqltvvme hyleefnnis
     2401 kapmslvmfr faiehisric rvlkqdkghl llvgiggsgr qsaaklstfm nayelyqiei
     2461 tknyagndwr edlkkiilqv gvatkstvfl fadnqikdes fvedinmlln tgdvpnifpa
     2521 dekadivekm qtaartqgek vevtplsmyn ffiervinki sfslamspig dafrnrlrmf
     2581 pslincctid wfqswptdal elvankfled velddnirve vvsmckyfqe svkklsldyy
     2641 nklrrhnyvt ptsylelilt fktllnskrq evammrnryl tglqkldfaa sqvavmqrel
     2701 talqpqlilt seetakmmvk ieaetreadg kkllvqadek eanvaaaiaq giknecegdl
     2761 aeampaleaa laaldtlnpa dislvksmqn ppgpvklvme sicimkgmkp erkpdpsgsg
     2821 kmiedywgvs kkilgdlkfl eslktydkdn ippltmkrir erfinhpefq paviknvssa
     2881 ceglckwvra mevydrvakv vapkrerlre aegklaaqmq klnqkraelk lvvdrlqaln
     2941 ddfeemntkk kdleenieic sqklvraekl isglggekdr wteaarqlgi rytnltgdvl
     3001 lssgtvaylg aftvdyrvqc qnqwlaeckd kvipgfsdfs lshtlgdpik irawqiaglp
     3061 vdsfsidngi ivsnsrrwal midphgqank wiknmekank lavikfsdsn ymrmlenalq
     3121 lgtpvlieni geeldasiep illkatfkqq gveymrlgen iieysrdfkl yittrlrnph
     3181 ylpevavkvc llnfmitplg lqdqllgiva akekpeleek knqlivesak nkkhlkeied
     3241 kilevlsmsk gniledetai kvlssskvls eeisekqkva smtetqidet rmgykpvavh
     3301 satiffcisd laniepmyqy sltwfinlym hslthstkse elnlrikyii dhftlsiynn
     3361 vcrslfekdk llfsllltig imkqkkeite evwyflltgg ialdnpypnp apqwlsekaw
     3421 aeivrasalp klhglmehle qnlgewkliy dsawpheeql pgswkfsqgl ekmvilrclr
     3481 pdkmvpavre fiaehmgkly ieaptfdlqg syndssccap lifvlspsad pmagllkfad
     3541 dlgmggtrtq tislgqgqgp iaakminnai kdgtwvvlqn chlaaswmpt lekiceeviv
     3601 pestnarfrl wltsypsekf pvsilqngik mtneppkglr anllrsylnd pisdpvffqs
     3661 cakavmwqkm lfglcffhav vqerrnfgpl gwnipyefne sdlrismwqi qmflndykev
     3721 pfdaltyltg ecnyggrvtd dkdrrlllsl lsmfyckeie edyyslapgd tyyipphgsy
     3781 qsyidylrnl pitahpevfg lhenaditkd nqetnqlfeg vlltlprqsg gsgkspqevv
     3841 eelaqdilsk lprdfdleev mklypvvyee smntvlrqel irfnrltkvv rrslinlgra
     3901 ikgqvlmsse leevfnsmlv gkvpamwaak sypslkplgg yvadllarlt ffqewidkgp
     3961 pvvfwisgfy ftqsfltgvs qnyarkytip idhigfefev tpqetvmenn pedgayikgl
     4021 flegarwdrk tmqigeslpk ilydplpiiw lkpgesamfl hqdiyvcpvy ktsarrgtls
     4081 ttghstnyvl sielptdmpq khwinrgvas lcqldn
//
LOCUS       NP_001356619             196 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin-like growth factor-binding protein 3 receptor isoform 3
            precursor [Homo sapiens].
ACCESSION   NP_001356619
VERSION     NP_001356619.1
DBSOURCE    REFSEQ: accession NM_001369690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Xu,W., Chao,R., Xie,X., Mao,Y., Chen,X., Chen,X. and Zhang,S.
  TITLE     IL13Ralpha2 as a crucial receptor for Chi3l1 in osteoclast
            differentiation and bone resorption through the MAPK/AKT pathway
  JOURNAL   Cell Commun Signal 22 (1), 81 (2024)
   PUBMED   38291404
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 196)
  AUTHORS   D'Addio,F., Assi,E., Maestroni,A., Rossi,G., Usuelli,V.,
            Petrazzuolo,A., Nardini,M., Loretelli,C., Ben Nasr,M. and
            Fiorina,P.
  TITLE     TMEM219 regulates the transcription factor expression and
            proliferation of beta cells
  JOURNAL   Front Endocrinol (Lausanne) 15, 1306127 (2024)
   PUBMED   38318298
  REMARK    GeneRIF: TMEM219 regulates the transcription factor expression and
            proliferation of beta cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Knudson,K.M., Hwang,S., McCann,M.S., Joshi,B.H., Husain,S.R. and
            Puri,R.K.
  TITLE     Recent Advances in IL-13Ralpha2-Directed Cancer Immunotherapy
  JOURNAL   Front Immunol 13, 878365 (2022)
   PUBMED   35464460
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   D'Addio,F., Maestroni,A., Assi,E., Ben Nasr,M., Amabile,G.,
            Usuelli,V., Loretelli,C., Bertuzzi,F., Antonioli,B., Cardarelli,F.,
            El Essawy,B., Solini,A., Gerling,I.C., Bianchi,C., Becchi,G.,
            Mazzucchelli,S., Corradi,D., Fadini,G.P., Foschi,D., Markmann,J.F.,
            Orsi,E., Skrha,J. Jr., Camboni,M.G., Abdi,R., James Shapiro,A.M.,
            Folli,F., Ludvigsson,J., Del Prato,S., Zuccotti,G. and Fiorina,P.
  TITLE     The IGFBP3/TMEM219 pathway regulates beta cell homeostasis
  JOURNAL   Nat Commun 13 (1), 684 (2022)
   PUBMED   35115561
  REMARK    GeneRIF: The IGFBP3/TMEM219 pathway regulates beta cell
            homeostasis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Joyce,S. and Nour,A.M.
  TITLE     Blocking transmembrane219 protein signaling inhibits autophagy and
            restores normal cell death
  JOURNAL   PLoS One 14 (6), e0218091 (2019)
   PUBMED   31220095
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 196)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   7  (residues 1 to 196)
  AUTHORS   He,C.H., Lee,C.G., Dela Cruz,C.S., Lee,C.M., Zhou,Y., Ahangari,F.,
            Ma,B., Herzog,E.L., Rosenberg,S.A., Li,Y., Nour,A.M., Parikh,C.R.,
            Schmidt,I., Modis,Y., Cantley,L. and Elias,J.A.
  TITLE     Chitinase 3-like 1 regulates cellular and tissue responses via
            IL-13 receptor alpha2
  JOURNAL   Cell Rep 4 (4), 830-841 (2013)
   PUBMED   23972995
  REMARK    Erratum:[Cell Rep. 2013 Nov 27;5(4):1156]
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Baxter,R.C.
  TITLE     Insulin-like growth factor binding protein-3 (IGFBP-3): Novel
            ligands mediate unexpected functions
  JOURNAL   J Cell Commun Signal 7 (3), 179-189 (2013)
   PUBMED   23700234
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Ingermann,A.R., Yang,Y.F., Han,J., Mikami,A., Garza,A.E.,
            Mohanraj,L., Fan,L., Idowu,M., Ware,J.L., Kim,H.S., Lee,D.Y. and
            Oh,Y.
  TITLE     Identification of a novel cell death receptor mediating
            IGFBP-3-induced anti-tumor effects in breast and prostate cancer
  JOURNAL   J Biol Chem 285 (39), 30233-30246 (2010)
   PUBMED   20353938
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Wood,N., Whitters,M.J., Jacobson,B.A., Witek,J., Sypek,J.P.,
            Kasaian,M., Eppihimer,M.J., Unger,M., Tanaka,T., Goldman,S.J.,
            Collins,M., Donaldson,D.D. and Grusby,M.J.
  TITLE     Enhanced interleukin (IL)-13 responses in mice lacking IL-13
            receptor alpha 2
  JOURNAL   J Exp Med 197 (6), 703-709 (2003)
   PUBMED   12642602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC120114.2 and AC093512.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2147975,
                              SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..196
                     /product="insulin-like growth factor-binding protein 3
                     receptor isoform 3 precursor"
                     /note="insulin-like growth factor-binding protein 3
                     receptor; testicular tissue protein Li 203"
                     /calculated_mol_wt=16848
     sig_peptide     1..38
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
                     /calculated_mol_wt=3872
     Region          48..169
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     CDS             1..196
                     /gene="TMEM219"
                     /gene_synonym="IGFBP-3R; IGFBP3R"
                     /coded_by="NM_001369690.1:89..679"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 5"
                     /db_xref="GeneID:124446"
                     /db_xref="HGNC:HGNC:25201"
                     /db_xref="MIM:620290"
ORIGIN      
        1 mgncqaghnl hlclahhppl vcatlillll glsglglgsf llthrtglrs pdipqdwvsf
       61 lrsfgqltlc prngtvtgkw rgshvvgllt tlnfgdgpdr nktrtfqatv lgsqmglkgs
      121 sagqlvlita rvttertagt clyfsavpgi lpssqppisc seegagnatl sprmgeecvs
      181 vwsheglvlt klltsv
//
LOCUS       NP_001010867             356 aa            linear   PRI 20-NOV-2025
DEFINITION  iron-sulfur cluster assembly factor IBA57, mitochondrial isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001010867 XP_114152
VERSION     NP_001010867.1
DBSOURCE    REFSEQ: accession NM_001010867.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Bargagna,B., Staderini,T., Lang,S.H., Banci,L. and Camponeschi,F.
  TITLE     Defects in the Maturation of Mitochondrial Iron-Sulfur Proteins:
            Biophysical Investigation of the MMDS3 Causing Gly104Cys Variant of
            IBA57
  JOURNAL   Int J Mol Sci 25 (19), 10466 (2024)
   PUBMED   39408793
  REMARK    GeneRIF: Defects in the Maturation of Mitochondrial Iron-Sulfur
            Proteins: Biophysical Investigation of the MMDS3 Causing Gly104Cys
            Variant of IBA57.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Nasta,V., Da Vela,S., Gourdoupis,S., Ciofi-Baffoni,S., Svergun,D.I.
            and Banci,L.
  TITLE     Structural properties of [2Fe-2S] ISCA2-IBA57: a complex of the
            mitochondrial iron-sulfur cluster assembly machinery
  JOURNAL   Sci Rep 9 (1), 18986 (2019)
   PUBMED   31831856
  REMARK    GeneRIF: Structural properties of [2Fe-2S] ISCA2-IBA57: a complex
            of the mitochondrial iron-sulfur cluster assembly machinery.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Sheftel,A.D., Wilbrecht,C., Stehling,O., Niggemeyer,B.,
            Elsasser,H.P., Muhlenhoff,U. and Lill,R.
  TITLE     The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are
            required for [4Fe-4S] protein maturation
  JOURNAL   Mol Biol Cell 23 (7), 1157-1166 (2012)
   PUBMED   22323289
  REMARK    GeneRIF: ISCA1, ISCA2, and IBA57 were depleted by RNA interference.
            Depleted cells contained massively swollen and enlarged
            mitochondria that were virtually devoid of cristae membranes,
            demonstrating the importance of these proteins for mitochondrial
            biogenesis.
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Nilsson,R., Schultz,I.J., Pierce,E.L., Soltis,K.A.,
            Naranuntarat,A., Ward,D.M., Baughman,J.M., Paradkar,P.N.,
            Kingsley,P.D., Culotta,V.C., Kaplan,J., Palis,J., Paw,B.H. and
            Mootha,V.K.
  TITLE     Discovery of genes essential for heme biosynthesis through
            large-scale gene expression analysis
  JOURNAL   Cell Metab 10 (2), 119-130 (2009)
   PUBMED   19656490
  REMARK    GeneRIF: Required for functional heme biosynthesis in erythroid
            cells.
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359510.24, HY081013.1 and
            BI820993.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 27, 2005 this sequence version replaced XP_114152.2.
            
            Summary: The protein encoded by this gene localizes to the
            mitochondrion and is part of the iron-sulfur cluster assembly
            pathway. The encoded protein functions late in the biosynthesis of
            mitochondrial 4Fe-4S proteins. Defects in this gene have been
            associated with autosomal recessive spastic paraplegia-74 and with
            multiple mitochondrial dysfunctions syndrome-3. Two transcript
            variants encoding different isoforms have been found for this gene.
            The smaller isoform is not likely to be localized to the
            mitochondrion since it lacks the amino-terminal transit peptide.
            [provided by RefSeq, Jul 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.402822.1,
                                           SRR1163655.527695.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000366711.4/
                                                  ENSP00000355672.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..356
                     /product="iron-sulfur cluster assembly factor IBA57,
                     mitochondrial isoform 1 precursor"
                     /note="iron-sulfur cluster assembly factor for biotin
                     synthase- and aconitase-like mitochondrial proteins, with
                     a mass of 57kDa; putative transferase C1orf69,
                     mitochondrial; putative transferase CAF17, mitochondrial;
                     IBA57, iron-sulfur cluster assembly homolog; IBA57
                     homolog, iron-sulfur cluster assembly; iron-sulfur cluster
                     assembly factor IBA57, mitochondrial"
                     /calculated_mol_wt=38024
     Region          49..344
                     /region_name="YgfZ"
                     /note="Folate-binding protein YgfZ, synthesis and repair
                     of Fe-S clusters [Posttranslational modification, protein
                     turnover, chaperones]; COG0354"
                     /db_xref="CDD:440123"
     CDS             1..356
                     /gene="IBA57"
                     /gene_synonym="C1orf69; MMDS3; SPG74"
                     /coded_by="NM_001010867.4:14..1084"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31046.1"
                     /db_xref="GeneID:200205"
                     /db_xref="HGNC:HGNC:27302"
                     /db_xref="MIM:615316"
ORIGIN      
        1 mataallrga tpgrggpvwr wrlraaprcr lahsscspgg dptagaawac frldgrtllr
       61 vrgpdaapfl lglltnelpl pspaaagapp aaragyahfl nvqgrtlydv ilyglqehse
      121 vsgfllecds svqgalqkhl alyrirrkvt vephpelrvw avlpsspeac gaaslqerag
      181 aaailirdpr tarmgwrllt qdegpalvpg grlgdlwdyh qhrylqgvpe gvrdlppgva
      241 lplesnlafm ngvsftkgcy igqeltarth hmgvirkrlf pvrfldplpt sgitpgatvl
      301 tasgqtvgkf ragqgnvgla llwsekikgp lhirasegaq valaasvpdw wptvsk
//
LOCUS       NP_001356509             646 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform 28 [Homo sapiens].
ACCESSION   NP_001356509 XP_024307008
VERSION     NP_001356509.1
DBSOURCE    REFSEQ: accession NM_001369580.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_024307008.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.142861.1,
                                           SRR14372080.98192.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..646
                     /product="transcription factor 4 isoform 28"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68896
     Region          537..621
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(545,549,551..553,555,560,581..582)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(558..559,562..563,565..566,569,573,583,586,590,593,
                     596..601)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..646
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369580.1:151..2091"
                     /note="isoform 28 is encoded by transcript variant 40"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsgtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit rsrssnndde dltpeqkaer
      541 ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv
      601 rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_055248                348 aa            linear   PRI 20-NOV-2025
DEFINITION  radial spoke head 14 homolog [Homo sapiens].
ACCESSION   NP_055248
VERSION     NP_055248.1
DBSOURCE    REFSEQ: accession NM_014433.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Ma,K., Peng,J., Rong,H., Jiang,Y., Zhang,H., Zhu,J., Xiao,B.,
            Tang,P., He,J. and Yu,Z.
  TITLE     RSPH14 regulates the proliferation, cell cycle progression, and
            apoptosis of non-small cell lung cancer cells
  JOURNAL   FEBS Open Bio 11 (10), 2715-2726 (2021)
   PUBMED   34351079
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Estrada,K., Styrkarsdottir,U., Evangelou,E., Hsu,Y.H., Duncan,E.L.,
            Ntzani,E.E., Oei,L., Albagha,O.M., Amin,N., Kemp,J.P., Koller,D.L.,
            Li,G., Liu,C.T., Minster,R.L., Moayyeri,A., Vandenput,L.,
            Willner,D., Xiao,S.M., Yerges-Armstrong,L.M., Zheng,H.F.,
            Alonso,N., Eriksson,J., Kammerer,C.M., Kaptoge,S.K., Leo,P.J.,
            Thorleifsson,G., Wilson,S.G., Wilson,J.F., Aalto,V., Alen,M.,
            Aragaki,A.K., Aspelund,T., Center,J.R., Dailiana,Z., Duggan,D.J.,
            Garcia,M., Garcia-Giralt,N., Giroux,S., Hallmans,G., Hocking,L.J.,
            Husted,L.B., Jameson,K.A., Khusainova,R., Kim,G.S., Kooperberg,C.,
            Koromila,T., Kruk,M., Laaksonen,M., Lacroix,A.Z., Lee,S.H.,
            Leung,P.C., Lewis,J.R., Masi,L., Mencej-Bedrac,S., Nguyen,T.V.,
            Nogues,X., Patel,M.S., Prezelj,J., Rose,L.M., Scollen,S.,
            Siggeirsdottir,K., Smith,A.V., Svensson,O., Trompet,S., Trummer,O.,
            van Schoor,N.M., Woo,J., Zhu,K., Balcells,S., Brandi,M.L.,
            Buckley,B.M., Cheng,S., Christiansen,C., Cooper,C., Dedoussis,G.,
            Ford,I., Frost,M., Goltzman,D., Gonzalez-Macias,J., Kahonen,M.,
            Karlsson,M., Khusnutdinova,E., Koh,J.M., Kollia,P., Langdahl,B.L.,
            Leslie,W.D., Lips,P., Ljunggren,O., Lorenc,R.S., Marc,J.,
            Mellstrom,D., Obermayer-Pietsch,B., Olmos,J.M.,
            Pettersson-Kymmer,U., Reid,D.M., Riancho,J.A., Ridker,P.M.,
            Rousseau,F., Slagboom,P.E., Tang,N.L., Urreizti,R., Van Hul,W.,
            Viikari,J., Zarrabeitia,M.T., Aulchenko,Y.S.,
            Castano-Betancourt,M., Grundberg,E., Herrera,L., Ingvarsson,T.,
            Johannsdottir,H., Kwan,T., Li,R., Luben,R., Medina-Gomez,C.,
            Palsson,S.T., Reppe,S., Rotter,J.I., Sigurdsson,G., van Meurs,J.B.,
            Verlaan,D., Williams,F.M., Wood,A.R., Zhou,Y., Gautvik,K.M.,
            Pastinen,T., Raychaudhuri,S., Cauley,J.A., Chasman,D.I.,
            Clark,G.R., Cummings,S.R., Danoy,P., Dennison,E.M., Eastell,R.,
            Eisman,J.A., Gudnason,V., Hofman,A., Jackson,R.D., Jones,G.,
            Jukema,J.W., Khaw,K.T., Lehtimaki,T., Liu,Y., Lorentzon,M.,
            McCloskey,E., Mitchell,B.D., Nandakumar,K., Nicholson,G.C.,
            Oostra,B.A., Peacock,M., Pols,H.A., Prince,R.L., Raitakari,O.,
            Reid,I.R., Robbins,J., Sambrook,P.N., Sham,P.C., Shuldiner,A.R.,
            Tylavsky,F.A., van Duijn,C.M., Wareham,N.J., Cupples,L.A.,
            Econs,M.J., Evans,D.M., Harris,T.B., Kung,A.W., Psaty,B.M.,
            Reeve,J., Spector,T.D., Streeten,E.A., Zillikens,M.C.,
            Thorsteinsdottir,U., Ohlsson,C., Karasik,D., Richards,J.B.,
            Brown,M.A., Stefansson,K., Uitterlinden,A.G., Ralston,S.H.,
            Ioannidis,J.P., Kiel,D.P. and Rivadeneira,F.
  TITLE     Genome-wide meta-analysis identifies 56 bone mineral density loci
            and reveals 14 loci associated with risk of fracture
  JOURNAL   Nat Genet 44 (5), 491-501 (2012)
   PUBMED   22504420
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Zhou,J., Fogelgren,B., Wang,Z., Roe,B.A. and Biegel,J.A.
  TITLE     Isolation of genes from the rhabdoid tumor deletion region in
            chromosome band 22q11.2
  JOURNAL   Gene 241 (1), 133-141 (2000)
   PUBMED   10607907
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000029.17 and AC245054.3.
            
            Summary: This gene encodes a protein with no known function but
            with slight similarity to a yeast vacuolar protein. The gene is
            located in a region deleted in pediatric rhabdoid tumors of the
            brain, kidney and soft tissues, but mutations in this gene have not
            been associated with the disease. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF133587.1, BC008986.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158188 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216036.9/ ENSP00000216036.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.22-q11.23"
     Protein         1..348
                     /product="radial spoke head 14 homolog"
                     /note="rhabdoid tumor deletion region protein 1; rhabdoid
                     tumor deletion region gene 1"
                     /calculated_mol_wt=38461
     Region          16..55
                     /region_name="ARM 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          27..55
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          57..96
                     /region_name="ARM 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          65..97
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          99..137
                     /region_name="ARM 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          107..134
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          139..179
                     /region_name="ARM 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          180..219
                     /region_name="ARM 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          183..>303
                     /region_name="HEAT"
                     /note="HEAT repeat [General function prediction only];
                     COG1413"
                     /db_xref="CDD:441023"
     Region          220..255
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          221..260
                     /region_name="ARM 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          224..259
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          262..301
                     /region_name="ARM 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     Region          265..296
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          303..346
                     /region_name="ARM 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHP6.1)"
     CDS             1..348
                     /gene="RSPH14"
                     /gene_synonym="RTDR1"
                     /coded_by="NM_014433.3:95..1141"
                     /db_xref="CCDS:CCDS13803.1"
                     /db_xref="GeneID:27156"
                     /db_xref="HGNC:HGNC:13437"
                     /db_xref="MIM:605663"
ORIGIN      
        1 mahsqnslel pininatqit tayghralpk lkeelqsedl qtrqkalmal cdlmhdpeci
       61 ykamnigcme nlkallkdsn smvrikttev lhitashsvg ryaflehdiv lalsfllndp
      121 spvcrgnlyk aymqlvqvpr gaqeiiskgl isslvwklqv eveeeefqef ildtlvlclq
      181 edatealgsn vvlvlkqkll sanqnirska arallnvsis regkkqvchf dvipilvhll
      241 kdpvehvksn aagalmfatv itegkyaale aqaiglllel lhspmtiarl natkaltmla
      301 eapegrkalq thvptframe vetyekpqva ealqraaria isviefkp
//
LOCUS       NP_001354477             574 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 41 [Homo sapiens].
ACCESSION   NP_001354477
VERSION     NP_001354477.1
DBSOURCE    REFSEQ: accession NM_001367548.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 574)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 574)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 574)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 574)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 574)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 574)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 574)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 574)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 574)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 574)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..574
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..574
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 41"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63690
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          442..569
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..574
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367548.1:95..1819"
                     /note="isoform 41 is encoded by transcript variant 41"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lepqttvvhn atdgikgste scnttteded lkaaplrtgn gssvpegrss
      421 rdrtapsagm qpqpslcssa mrkqeiikit eqlieainng dfeaytkicd pgltsfepea
      481 lgnlvegmdf hkfyfenlls knskpihtti lnphvhvige daaciayirl tqyidgqgrp
      541 rtsqseetrv whrrdgkwln vhyhcsgapa aplq
//
LOCUS       NP_078989                304 aa            linear   PRI 20-NOV-2025
DEFINITION  KATNB1-like protein 1 [Homo sapiens].
ACCESSION   NP_078989
VERSION     NP_078989.1
DBSOURCE    REFSEQ: accession NM_024713.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Kovacs,I.A., Luck,K., Spirohn,K., Wang,Y., Pollis,C., Schlabach,S.,
            Bian,W., Kim,D.K., Kishore,N., Hao,T., Calderwood,M.A., Vidal,M.
            and Barabasi,A.L.
  TITLE     Network-based prediction of protein interactions
  JOURNAL   Nat Commun 10 (1), 1240 (2019)
   PUBMED   30886144
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Sanders,A.A., de Vrieze,E., Alazami,A.M., Alzahrani,F.,
            Malarkey,E.B., Sorusch,N., Tebbe,L., Kuhns,S., van Dam,T.J.,
            Alhashem,A., Tabarki,B., Lu,Q., Lambacher,N.J., Kennedy,J.E.,
            Bowie,R.V., Hetterschijt,L., van Beersum,S., van Reeuwijk,J.,
            Boldt,K., Kremer,H., Kesterson,R.A., Monies,D., Abouelhoda,M.,
            Roepman,R., Huynen,M.H., Ueffing,M., Russell,R.B., Wolfrum,U.,
            Yoder,B.K., van Wijk,E., Alkuraya,F.S. and Blacque,O.E.
  TITLE     KIAA0556 is a novel ciliary basal body component mutated in Joubert
            syndrome
  JOURNAL   Genome Biol 16, 293 (2015)
   PUBMED   26714646
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   8  (residues 1 to 304)
  AUTHORS   McNally,K.P. and McNally,F.J.
  TITLE     The spindle assembly function of Caenorhabditis elegans katanin
            does not require microtubule-severing activity
  JOURNAL   Mol Biol Cell 22 (9), 1550-1560 (2011)
   PUBMED   21372175
  REMARK    Erratum:[Mol Biol Cell. 2012 Nov;23(22):4472]
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK311338.1, AL136908.1, BX389537.2, BC026234.1 and BM831547.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136908.1, SRR1660805.49837.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256544.8/ ENSP00000256544.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..304
                     /product="KATNB1-like protein 1"
                     /note="katanin p80 subunit B-like 1"
                     /calculated_mol_wt=34636
     Region          26..33
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H079.1)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H079.1)"
     Region          72..79
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H079.1)"
     Region          149..300
                     /region_name="Katanin_con80"
                     /note="con80 domain of Katanin; pfam13925"
                     /db_xref="CDD:464044"
     CDS             1..304
                     /gene="KATNBL1"
                     /gene_synonym="C15orf29"
                     /coded_by="NM_024713.3:161..1075"
                     /db_xref="CCDS:CCDS10034.1"
                     /db_xref="GeneID:79768"
                     /db_xref="HGNC:HGNC:26199"
                     /db_xref="MIM:616235"
ORIGIN      
        1 masethnvkk rnfcnkiedh fidlprkkis nftnknmkev kkspkqlaay inrtvgqtvk
       61 spdklrkviy rrkkvhhpfp npcyrkkqsp gsggcdmank enelacaghl peklhhdsrt
      121 ylvnssdsgs sqtespssky sgffsevsqd hetmaqvlfs rnmrlnvalt fwrkrsisel
      181 vayllriedl gvvvdclpvl tnclqeekqy islgccvdll plvksllksk feeyvivgln
      241 wlqavikrww selsskteii ndgniqilkq qlsglweqen hltlvpgytg niakdvdayl
      301 lqlh
//
LOCUS       NP_872624                265 aa            linear   PRI 20-NOV-2025
DEFINITION  uroplakin-3b isoform c precursor [Homo sapiens].
ACCESSION   NP_872624
VERSION     NP_872624.1
DBSOURCE    REFSEQ: accession NM_182683.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Moayyeri,A., Hsu,Y.H., Karasik,D., Estrada,K., Xiao,S.M.,
            Nielson,C., Srikanth,P., Giroux,S., Wilson,S.G., Zheng,H.F.,
            Smith,A.V., Pye,S.R., Leo,P.J., Teumer,A., Hwang,J.Y., Ohlsson,C.,
            McGuigan,F., Minster,R.L., Hayward,C., Olmos,J.M.,
            Lyytikainen,L.P., Lewis,J.R., Swart,K.M., Masi,L., Oldmeadow,C.,
            Holliday,E.G., Cheng,S., van Schoor,N.M., Harvey,N.C., Kruk,M., del
            Greco,M. F, Igl,W., Trummer,O., Grigoriou,E., Luben,R., Liu,C.T.,
            Zhou,Y., Oei,L., Medina-Gomez,C., Zmuda,J., Tranah,G., Brown,S.J.,
            Williams,F.M., Soranzo,N., Jakobsdottir,J., Siggeirsdottir,K.,
            Holliday,K.L., Hannemann,A., Go,M.J., Garcia,M., Polasek,O.,
            Laaksonen,M., Zhu,K., Enneman,A.W., McEvoy,M., Peel,R., Sham,P.C.,
            Jaworski,M., Johansson,A., Hicks,A.A., Pludowski,P., Scott,R.,
            Dhonukshe-Rutten,R.A., van der Velde,N., Kahonen,M., Viikari,J.S.,
            Sievanen,H., Raitakari,O.T., Gonzalez-Macias,J., Hernandez,J.L.,
            Mellstrom,D., Ljunggren,O., Cho,Y.S., Volker,U., Nauck,M.,
            Homuth,G., Volzke,H., Haring,R., Brown,M.A., McCloskey,E.,
            Nicholson,G.C., Eastell,R., Eisman,J.A., Jones,G., Reid,I.R.,
            Dennison,E.M., Wark,J., Boonen,S., Vanderschueren,D., Wu,F.C.,
            Aspelund,T., Richards,J.B., Bauer,D., Hofman,A., Khaw,K.T.,
            Dedoussis,G., Obermayer-Pietsch,B., Gyllensten,U.,
            Pramstaller,P.P., Lorenc,R.S., Cooper,C., Kung,A.W., Lips,P.,
            Alen,M., Attia,J., Brandi,M.L., de Groot,L.C., Lehtimaki,T.,
            Riancho,J.A., Campbell,H., Liu,Y., Harris,T.B., Akesson,K.,
            Karlsson,M., Lee,J.Y., Wallaschofski,H., Duncan,E.L., O'Neill,T.W.,
            Gudnason,V., Spector,T.D., Rousseau,F., Orwoll,E., Cummings,S.R.,
            Wareham,N.J., Rivadeneira,F., Uitterlinden,A.G., Prince,R.L.,
            Kiel,D.P., Reeve,J. and Kaptoge,S.K.
  TITLE     Genetic determinants of heel bone properties: genome-wide
            association meta-analysis and replication in the GEFOS/GENOMOS
            consortium
  JOURNAL   Hum Mol Genet 23 (11), 3054-3068 (2014)
   PUBMED   24430505
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Kanamori-Katayama,M., Kaiho,A., Ishizu,Y., Okamura-Oho,Y., Hino,O.,
            Abe,M., Kishimoto,T., Sekihara,H., Nakamura,Y., Suzuki,H.,
            Forrest,A.R. and Hayashizaki,Y.
  TITLE     LRRN4 and UPK3B are markers of primary mesothelial cells
  JOURNAL   PLoS One 6 (10), e25391 (2011)
   PUBMED   21984916
  REMARK    GeneRIF: LRRN4 was only detected in primary mesothelial cells, but
            MSLN and UPK3B were also detected in other cell types.
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Foot,N.J., Dalton,H.E., Shearwin-Whyatt,L.M., Dorstyn,L., Tan,S.S.,
            Yang,B. and Kumar,S.
  TITLE     Regulation of the divalent metal ion transporter DMT1 and iron
            homeostasis by a ubiquitin-dependent mechanism involving Ndfips and
            WWP2
  JOURNAL   Blood 112 (10), 4268-4275 (2008)
   PUBMED   18776082
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Garcia-Espana,A., Chung,P.J., Zhao,X., Lee,A., Pellicer,A., Yu,J.,
            Sun,T.T. and Desalle,R.
  TITLE     Origin of the tetraspanin uroplakins and their co-evolution with
            associated proteins: implications for uroplakin structure and
            function
  JOURNAL   Mol Phylogenet Evol 41 (2), 355-367 (2006)
   PUBMED   16814572
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Deng,F.M., Liang,F.X., Tu,L., Resing,K.A., Hu,P., Supino,M.,
            Hu,C.C., Zhou,G., Ding,M., Kreibich,G. and Sun,T.T.
  TITLE     Uroplakin IIIb, a urothelial differentiation marker, dimerizes with
            uroplakin Ib as an early step of urothelial plaque assembly
  JOURNAL   J Cell Biol 159 (4), 685-694 (2002)
   PUBMED   12446744
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BE615406.1, BU150542.1, BP352210.1 and AY233462.1.
            
            On Mar 4, 2006 this sequence version replaced XP_944772.1.
            
            Summary: UPK3B is a minor component of the apical plaques of
            mammalian urothelium that binds and dimerizes with uroplakin-1b
            (UPK1B; MIM 602380), one of the major conserved urothelium membrane
            proteins. The other major conserved integral membrane proteins of
            urothelial plaques are UPK1A (MIM 611557), UPK2 (MIM 611558), and
            UPK3A (MIM 611559) (Deng et al., 2002 [PubMed 12446744]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) is alternatively spliced at
            the 5' end compared to variant 1, which results in a shorter
            isoform (c) lacking a protein segment in the N-terminal region
            compared to isoform a. This variant is annotated on the
            ALT_REF_LOCI_1 alternate haplotype of the GRCh38 human reference
            genome assembly.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056760.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1968968,
                                           SAMEA2142363 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..265
                     /product="uroplakin-3b isoform c precursor"
                     /note="uroplakin-3b; uroplakin IIIb"
                     /calculated_mol_wt=25565
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2960
     Region          29..>154
                     /region_name="UP_III_II"
                     /note="Uroplakin IIIb, IIIa and II; cl06408"
                     /db_xref="CDD:471435"
     CDS             1..265
                     /gene="UPK3B"
                     /gene_synonym="P35; UP3B; UPIIIB"
                     /coded_by="NM_182683.2:231..1028"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="GeneID:105375355"
                     /db_xref="HGNC:HGNC:21444"
                     /db_xref="MIM:611887"
ORIGIN      
        1 mglpwgqphl glqmlllaln clrpslslel vpytpqitaw dlegkvtatt fsleqprcvf
       61 dglasasdtv wlvvafsnas rgfqnpetla dipaspqllt dghymtlpls pdqlpcgdpm
      121 agsggapvlr vghdhgchqq pfcnaplpgp gpyredprih rhlaraakwq hdrhylhplf
      181 sgrpptlgll gslyhallqp vvagggpgaa adrllhgqal hdpphptqrg rhtagglqaw
      241 pgpppqpqpl awplcmglge mgrre
//
LOCUS       NP_054727                627 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 22 [Homo sapiens].
ACCESSION   NP_054727
VERSION     NP_054727.1
DBSOURCE    REFSEQ: accession NM_014008.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 627)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 627)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 627)
  AUTHORS   Boesch,D.J., Singla,A., Han,Y., Kramer,D.A., Liu,Q., Suzuki,K.,
            Juneja,P., Zhao,X., Long,X., Medlyn,M.J., Billadeau,D.D., Chen,Z.,
            Chen,B. and Burstein,E.
  TITLE     Structural organization of the retriever-CCC endosomal recycling
            complex
  JOURNAL   Nat Struct Mol Biol 31 (6), 910-924 (2024)
   PUBMED   38062209
REFERENCE   4  (residues 1 to 627)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   5  (residues 1 to 627)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
  REMARK    GeneRIF: CCDC22 participates in NF-kappaB activation and its
            deficiency leads to decreased IkappaB turnover
REFERENCE   6  (residues 1 to 627)
  AUTHORS   Voineagu,I., Huang,L., Winden,K., Lazaro,M., Haan,E., Nelson,J.,
            McGaughran,J., Nguyen,L.S., Friend,K., Hackett,A., Field,M.,
            Gecz,J. and Geschwind,D.
  TITLE     CCDC22: a novel candidate gene for syndromic X-linked intellectual
            disability
  JOURNAL   Mol Psychiatry 17 (1), 4-7 (2012)
   PUBMED   21826058
  REMARK    GeneRIF: This study demonistrated that CCDC22 is a novel candidate
            gene for syndromic X-linked intellectual disability.
REFERENCE   7  (residues 1 to 627)
  AUTHORS   Suttner,K., Depner,M., Wetzke,M., Klopp,N., von Mutius,E.,
            Illig,T., Sparwasser,T. and Kabesch,M.
  TITLE     Genetic variants harbored in the forkhead box protein 3 locus
            increase hay fever risk
  JOURNAL   J Allergy Clin Immunol 125 (6), 1395-1399 (2010)
   PUBMED   20398921
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 627)
  AUTHORS   Mulder,J., Wernerus,H., Shi,T.J., Ponten,F., Hober,S., Uhlen,M. and
            Hokfelt,T.
  TITLE     Systematically generated antibodies against human gene products:
            high throughput screening on sections from the rat nervous system
  JOURNAL   Neuroscience 146 (4), 1689-1703 (2007)
   PUBMED   17478047
REFERENCE   9  (residues 1 to 627)
  AUTHORS   Tomsig,J.L., Snyder,S.L. and Creutz,C.E.
  TITLE     Identification of targets for calcium signaling through the copine
            family of proteins. Characterization of a coiled-coil
            copine-binding motif
  JOURNAL   J Biol Chem 278 (12), 10048-10054 (2003)
   PUBMED   12522145
  REMARK    GeneRIF: Identifies the homologous mouse protein as a
            copine-binding protein.
REFERENCE   10 (residues 1 to 627)
  AUTHORS   Elliott,A.M. and Chudley,A.
  TITLE     Ritscher-Schinzel Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31971710
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC340647.1, AJ005890.1 and
            BC000972.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein containing a coiled-coil
            domain. The encoded protein functions in the regulation of NF-kB
            (nuclear factor kappa-light-chain-enhancer of activated B cells) by
            interacting with COMMD (copper metabolism Murr1 domain-containing)
            proteins. The mouse orthologous protein has been shown to bind
            copines, which are calcium-dependent, membrane-binding proteins
            that may function in calcium signaling. This human gene has been
            identified as a novel candidate gene for syndromic X-linked
            intellectual disability. [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.584118.1,
                                           SRR1803614.180387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376227.4/ ENSP00000365401.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..627
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..627
                     /product="coiled-coil domain-containing protein 22"
                     /note="coiled-coil domain containing 22"
                     /calculated_mol_wt=70625
     Region          1..597
                     /region_name="CCDC22"
                     /note="Coiled-coil domain-containing protein 22;
                     pfam05667"
                     /db_xref="CDD:461708"
     Region          1..447
                     /region_name="Sufficicient and required for interaction
                     with CCDC93. /evidence=ECO:0000269|PubMed:25355947"
                     /note="propagated from UniProtKB/Swiss-Prot (O60826.1)"
     Region          1..321
                     /region_name="Sufficient for interaction with COMMD1.
                     /evidence=ECO:0000269|PubMed:25355947"
                     /note="propagated from UniProtKB/Swiss-Prot (O60826.1)"
     Region          218..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60826.1)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (O60826.1)"
     CDS             1..627
                     /gene="CCDC22"
                     /gene_synonym="CXorf37; JM1; RTSC2"
                     /coded_by="NM_014008.5:168..2051"
                     /db_xref="CCDS:CCDS14322.1"
                     /db_xref="GeneID:28952"
                     /db_xref="HGNC:HGNC:28909"
                     /db_xref="MIM:300859"
ORIGIN      
        1 meeadrilih slrqagtavp pdvqtlraft telvveavvr clrvinpavg sglspllpla
       61 msarfrlams laqacmdlgy plelgyqnfl ypsepdlrdl llflaerlpt dasedadqpa
      121 gdsaillrai gsqirdqlal pwvpphlrtp klqhlqgsal qkpfhasrlv vpelssrgep
      181 refqasplll pvptqvpqpv grvasllehh alqlcqqtgr drpgdedwvh rtsrlppqed
      241 traqrqrlqk qltehlrqsw gllgapiqar dlgellqawg agaktgapkg srfthsekft
      301 fhlepqaqat qvsdvpatsr rpeqvtwaaq eqeleslreq legvnrsiee veadmktlgv
      361 sfvqaesecr hsklstaere qalrlksrav ellpdgtanl aklqlvvens aqrvihlagq
      421 wekhrvplla eyrhlrklqd crelessrrl aeiqelhqsv raaaeearrk eevykqlmse
      481 letlprdvsr laytqrilei vgnirkqkee itkilsdtke lqkeinslsg kldrtfavtd
      541 elvfkdakkd davrkaykyl aalhencsql iqtiedtgti mrevrdleeq ietelgkktl
      601 snlekiredy ralrqenagl lgrvrea
//
LOCUS       NP_001269                745 aa            linear   PRI 20-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit alpha isoform 1
            [Homo sapiens].
ACCESSION   NP_001269
VERSION     NP_001269.3
DBSOURCE    REFSEQ: accession NM_001278.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Chen,X., Wu,W., Jeong,J.H., Rokavec,M., Wei,R., Feng,S.,
            Schroth,W., Brauch,H., Zhong,S. and Luo,J.L.
  TITLE     Cytokines-activated nuclear IKKalpha-FAT10 pathway induces breast
            cancer tamoxifen-resistance
  JOURNAL   Sci China Life Sci 67 (7), 1413-1426 (2024)
   PUBMED   38565741
  REMARK    GeneRIF: Cytokines-activated nuclear IKKalpha-FAT10 pathway induces
            breast cancer tamoxifen-resistance.
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   4  (residues 1 to 745)
  AUTHORS   McIntosh,K., Khalaf,Y.H., Craig,R., West,C., McCulloch,A.,
            Waghmare,A., Lawson,C., Chan,E.Y.W., Mackay,S., Paul,A. and
            Plevin,R.
  TITLE     IL-1beta stimulates a novel, IKKalpha -dependent, NIK -independent
            activation of non-canonical NFkappaB signalling
  JOURNAL   Cell Signal 107, 110684 (2023)
   PUBMED   37080443
  REMARK    GeneRIF: IL-1beta stimulates a novel, IKKalpha -dependent, NIK
            -independent activation of non-canonical NFkappaB signalling.
REFERENCE   5  (residues 1 to 745)
  AUTHORS   Yang,H., Espada,C.E., Phillips,S., Martinez,N., Kenney,A.D.,
            Yount,J.S., Xiong,Y. and Wu,L.
  TITLE     The host antiviral protein SAMHD1 suppresses NF-kappaB activation
            by interacting with the IKK complex during inflammatory responses
            and viral infection
  JOURNAL   J Biol Chem 299 (6), 104750 (2023)
   PUBMED   37100289
  REMARK    GeneRIF: The host antiviral protein SAMHD1 suppresses NF-kappaB
            activation by interacting with the IKK complex during inflammatory
            responses and viral infection.
REFERENCE   6  (residues 1 to 745)
  AUTHORS   Scherer,D.C., Brockman,J.A., Chen,Z., Maniatis,T. and Ballard,D.W.
  TITLE     Signal-induced degradation of I kappa B alpha requires
            site-specific ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 92 (24), 11259-11263 (1995)
   PUBMED   7479976
REFERENCE   7  (residues 1 to 745)
  AUTHORS   Mock,B.A., Connelly,M.A., McBride,O.W., Kozak,C.A. and Marcu,K.B.
  TITLE     CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human
            chromosome 10 and mouse chromosome 19
  JOURNAL   Genomics 27 (2), 348-351 (1995)
   PUBMED   7558004
REFERENCE   8  (residues 1 to 745)
  AUTHORS   Connelly,M.A. and Marcu,K.B.
  TITLE     CHUK, a new member of the helix-loop-helix and leucine zipper
            families of interacting proteins, contains a serine-threonine
            kinase catalytic domain
  JOURNAL   Cell Mol Biol Res 41 (6), 537-549 (1995)
   PUBMED   8777433
REFERENCE   9  (residues 1 to 745)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     A novel NF-kappa B complex containing p65 homodimers: implications
            for transcriptional control at the level of subunit dimerization
  JOURNAL   Mol Cell Biol 13 (12), 7826-7835 (1993)
   PUBMED   8246997
REFERENCE   10 (residues 1 to 745)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA405845.1, AF080157.1,
            BM800404.1, BC034796.1 and AI829429.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 6, 2005 this sequence version replaced NP_001269.2.
            
            Summary: This gene encodes a member of the serine/threonine protein
            kinase family. The encoded protein, a component of a
            cytokine-activated protein complex that is an inhibitor of the
            essential transcription factor NF-kappa-B complex, phosphorylates
            sites that trigger the degradation of the inhibitor via the
            ubiquination pathway, thereby activating the transcription factor.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC092514.1, AF080157.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370397.8/ ENSP00000359424.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..745
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit alpha isoform 1"
                     /EC_number="2.7.11.10"
                     /note="I-kappa-B kinase-alpha; I-kappa-B kinase 1; Nuclear
                     factor NFkappaB inhibitor kinase alpha; IKK-a kinase; IkB
                     kinase alpha subunit; inhibitor of nuclear factor kappa-B
                     kinase subunit alpha; conserved helix-loop-helix
                     ubiquitous kinase; transcription factor 16"
                     /calculated_mol_wt=84509
     Region          21..309
                     /region_name="STKc_IKK_alpha"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha;
                     cd14039"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,104,144,146,148..149,
                     151,165,168,183..186)
                     /site_type="active"
                     /db_xref="CDD:270941"
     Site            order(21..25,29,42,44,74,95..98,102,144,146,148..149,151,
                     165)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270941"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and SGK1.
                     /evidence=ECO:0000269|PubMed:10485710,
                     ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            order(25,102,104,144,146,148,168,183..186)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270941"
     Site            order(108,110,114,117,218,223,251..252,254,260..263)
                     /site_type="other"
                     /note="putative SDD interface [polypeptide binding]"
                     /db_xref="CDD:270941"
     Site            164..186
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270941"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:9520446; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Site            179
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylthreonine, by
                     Yersinia YopJ. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Site            180
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by SGK1.
                     /evidence=ECO:0000269|PubMed:19088076; propagated from
                     UniProtKB/Swiss-Prot (O15111.2)"
     Region          311..387
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          386..659
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          455..476
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (O15111.2)"
     Region          707..743
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     Region          738..743
                     /region_name="NEMO-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15111.2)"
     CDS             1..745
                     /gene="CHUK"
                     /gene_synonym="BPS2; IKBKA; IKK-1; IKK-alpha; IKK1; IKKA;
                     NFKBIKA; TCF16"
                     /coded_by="NM_001278.5:65..2302"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7488.1"
                     /db_xref="GeneID:1147"
                     /db_xref="HGNC:HGNC:1974"
                     /db_xref="MIM:600664"
ORIGIN      
        1 merppglrpg aggpwemrer lgtggfgnvc lyqhreldlk iaikscrlel stknrerwch
       61 eiqimkklnh anvvkacdvp eelnilihdv pllameycsg gdlrkllnkp enccglkesq
      121 ilsllsdigs girylhenki ihrdlkpeni vlqdvggkii hkiidlgyak dvdqgslcts
      181 fvgtlqylap elfenkpyta tvdywsfgtm vfeciagyrp flhhlqpftw hekikkkdpk
      241 cifaceemsg evrfsshlpq pnslcslvve pmenwlqlml nwdpqqrggp vdltlkqprc
      301 fvlmdhilnl kivhilnmts akiisfllpp deslhslqsr ieretgintg sqellsetgi
      361 sldprkpasq cvldgvrgcd symvylfdks ktvyegpfas rslsdcvnyi vqdskiqlpi
      421 iqlrkvwaea vhyvsglked ysrlfqgqra amlsllryna nltkmkntli sasqqlkakl
      481 effhksiqld leryseqmty gissekmlka wkemeekaih yaevgvigyl edqimslhae
      541 imelqkspyg rrqgdlmesl eqraidlykq lkhrpsdhsy sdstemvkii vhtvqsqdrv
      601 lkelfghlsk llgckqkiid llpkvevals nikeadntvm fmqgkrqkei whllkiactq
      661 ssarslvgss legavtpqts awlpptsaeh dhslscvvtp qdgetsaqmi eenlnclghl
      721 stiiheanee qgnsmmnldw swlte
//
LOCUS       NP_877398               1173 aa            linear   PRI 20-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
            isoform b [Homo sapiens].
ACCESSION   NP_877398
VERSION     NP_877398.1
DBSOURCE    REFSEQ: accession NM_182734.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Dai,S., Wang,Q., Lyu,Y., Chen,Z., Liu,X., Zhao,G. and Zhang,H.
  TITLE     LncRNA AC100826.1 regulated PLCB1 to promote progression in
            non-small cell lung cancer
  JOURNAL   Thorac Cancer 15 (19), 1477-1489 (2024)
   PUBMED   38778543
  REMARK    GeneRIF: LncRNA AC100826.1 regulated PLCB1 to promote progression
            in non-small cell lung cancer.
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Chang,M., Cui,X., Sun,Q., Wang,Y., Liu,J., Sun,Z., Ren,J., Sun,Y.,
            Han,L. and Li,W.
  TITLE     Lnc-PLCB1 is stabilized by METTL14 induced m6A modification and
            inhibits Helicobacter pylori mediated gastric cancer by
            destabilizing DDX21
  JOURNAL   Cancer Lett 588, 216746 (2024)
   PUBMED   38387756
  REMARK    GeneRIF: Lnc-PLCB1 is stabilized by METTL14 induced m6A
            modification and inhibits Helicobacter pylori mediated gastric
            cancer by destabilizing DDX21.
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Wang,Y., Tu,Z., Zhao,W., Wang,L., Jiang,J., Gu,L., Li,M., Jiang,L.,
            Wang,Y. and Bi,Y.
  TITLE     PLCB1 Enhances Cell Migration and Invasion in Gastric Cancer Via
            Regulating Actin Cytoskeletal Remodeling and Epithelial-Mesenchymal
            Transition
  JOURNAL   Biochem Genet 61 (6), 2618-2632 (2023)
   PUBMED   37208557
  REMARK    GeneRIF: PLCB1 Enhances Cell Migration and Invasion in Gastric
            Cancer Via Regulating Actin Cytoskeletal Remodeling and
            Epithelial-Mesenchymal Transition.
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Wang,S.H., Cheng,J.Y., Tsai,H.H., Lo,T.C., Hung,J.T., Lin,C.C.,
            Lee,C.W., Ho,Y.H., Kuo,H.H., Yu,A.L. and Yu,J.
  TITLE     Conformational alteration in glycan induces phospholipase Cbeta1
            activation and angiogenesis
  JOURNAL   J Biomed Sci 29 (1), 105 (2022)
   PUBMED   36517806
  REMARK    GeneRIF: Conformational alteration in glycan induces phospholipase
            Cbeta1 activation and angiogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Hwang,S.C., Park,K.H., Ha,M.J., Noh,I.S., Park,T.B. and Lee,Y.H.
  TITLE     Distribution of phospholipase C isozymes in normal human lung
            tissue and their immunohistochemical localization
  JOURNAL   J Korean Med Sci 11 (4), 305-313 (1996)
   PUBMED   8878798
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Zini,N., Sabatelli,P., Faenza,I., Ognibene,A. and Maraldi,N.M.
  TITLE     Interleukin-1 alpha induces variations of the intranuclear amount
            of phosphatidylinositol 4,5-bisphosphate and phospholipase C beta 1
            in human osteosarcoma Saos-2 cells
  JOURNAL   Histochem J 28 (7), 495-504 (1996)
   PUBMED   8872139
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   9  (residues 1 to 1173)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1173)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB011153.3, AJ278314.1,
            AL049593.10 and BQ184058.1.
            
            Summary: The protein encoded by this gene catalyzes the formation
            of inositol 1,4,5-trisphosphate and diacylglycerol from
            phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium
            as a cofactor and plays an important role in the intracellular
            transduction of many extracellular signals. This gene is activated
            by two G-protein alpha subunits, alpha-q and alpha-11. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) includes an alternate exon in
            the 3' end compared to variant 1. This exon contains an in-frame
            stop codon, and the resulting isoform (b) is shorter and has a
            distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.139741.1,
                                           SRR1803615.262237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3"
     Protein         1..1173
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-1 isoform b"
                     /EC_number="3.1.4.11"
                     /note="triphosphoinositide phosphodiesterase;
                     phosphoinositidase C; monophosphatidylinositol
                     phosphodiesterase;
                     1-phosphatidyl-D-myo-inositol-4,5-bisphosphate;
                     inositoltrisphosphohydrolase; phospholipase C-I;
                     1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
                     beta-1; phospholipase C, beta 1
                     (phosphoinositide-specific); phosphoinositide
                     phospholipase C"
                     /calculated_mol_wt=133573
     Region          22..148
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(27,29,40,57,122)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(30,32,37,39,41,56..57)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          153..303
                     /region_name="EFh_PI-PLCbeta1"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 1 (PI-PLC-beta1); cd16208"
                     /db_xref="CDD:320038"
     Region          153..182
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          186..215
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          224..253
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          270..303
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          316..643
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Site            order(331..332,361,363,378,412,479,481,569,596,598)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(331,378)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(332,361,363,412)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          469..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          677..796
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(694,720,751,753,755,757)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          834..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P10894; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          903..939
                     /region_name="DUF1154"
                     /note="Protein of unknown function (DUF1154); pfam06631"
                     /db_xref="CDD:461969"
     Region          963..994
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          1003..>1141
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     Region          1071..1095
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     CDS             1..1173
                     /gene="PLCB1"
                     /gene_synonym="DEE12; EIEE12; PI-PLC; PLC-154; PLC-beta-1;
                     PLC-I; PLC154; PLCB1A; PLCB1B"
                     /coded_by="NM_182734.3:387..3908"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13103.1"
                     /db_xref="GeneID:23236"
                     /db_xref="HGNC:HGNC:15917"
                     /db_xref="MIM:607120"
ORIGIN      
        1 magaqpgvha lqlkpvcvsd slkkgtkfvk wdddstivtp iilrtdpqgf ffywtdqnke
       61 telldlslvk darcgrhaka pkdpklrell dvgnigrleq rmitvvygpd lvnishlnlv
      121 afqeevakew tnevfslatn llaqnmsrda flekaytklk lqvtpegrip lkniyrlfsa
      181 drkrvetale acslpssrnd sipqedftpe vyrvflnnlc prpeidnifs efgakskpyl
      241 tvdqmmdfin lkqrdprlne ilypplkqeq vqvliekyep nnslarkgqi svdgfmryls
      301 geengvvspe kldlnedmsq plshyfinss hntyltagql agnssvemyr qvllsgcrcv
      361 eldcwkgrta eeepvithgf tmtteisfke vieaiaecaf ktspfpills fenhvdspkq
      421 qakmaeycrl ifgdallmep lekyplesgv plpspmdlmy kilvknkkks hkssegsgkk
      481 klseqasnty sdsssmfeps spgageadte sddddddddc kkssmdegta gseamateem
      541 snlvnyiqpv kfesfeiskk rnksfemssf vetkgleqlt kspvefveyn kmqlsriypk
      601 gtrvdssnym pqlfwnagcq mvalnfqtmd lamqinmgmy eyngksgyrl kpefmrrpdk
      661 hfdpftegiv dgivantlsv kiisgqflsd kkvgtyvevd mfglpvdtrr kafktktsqg
      721 navnpvweee pivfkkvvlp tlaclriavy eeggkfighr ilpvqairpg yhyiclrner
      781 nqpltlpavf vyievkdyvp dtyadvieal snpiryvnlm eqrakqlaal tledeeevkk
      841 eadpgetpse apsearttpa engvnhtttl tpkppsqalh sqpapgsvka paktedliqs
      901 vlteveaqti eelkqqksfv klqkkhykem kdlvkrhhkk ttdlikehtt kyneiqndyl
      961 rrraaleksa kkdskkksep sspdhgssti eqdlaaldae mtqklidlkd kqqqqllnlr
     1021 qeqyysekyq krehiklliq kltdvaeecq nnqlkklkei cekekkelkk kmdkkrqeki
     1081 teakskdksq meeektemir syiqevvqyi krleeaqskr qeklvekhke irqqildekp
     1141 kgegsssfls etchedpsvs pnftppnpqa lkw
//
LOCUS       NP_001135822             296 aa            linear   PRI 20-NOV-2025
DEFINITION  THO complex subunit 6 isoform 2 [Homo sapiens].
ACCESSION   NP_001135822
VERSION     NP_001135822.1
DBSOURCE    REFSEQ: accession NM_001142350.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Ruaud,L., Roux,N., Boutaud,L., Bessieres,B., Ageorges,F.,
            Achaiaa,A., Bole,C., Nitschke,P., Masson,C., Vekemans,M.,
            Verloes,A. and Attie-Bitach,T.
  TITLE     Biallelic THOC6 pathogenic variants: Prenatal phenotype and review
            of the literature
  JOURNAL   Birth Defects Res 114 (10), 499-504 (2022)
   PUBMED   35426486
  REMARK    GeneRIF: Biallelic THOC6 pathogenic variants: Prenatal phenotype
            and review of the literature.
            Review article
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Amos,J.S., Huang,L., Thevenon,J., Kariminedjad,A., Beaulieu,C.L.,
            Masurel-Paulet,A., Najmabadi,H., Fattahi,Z., Beheshtian,M.,
            Tonekaboni,S.H., Tang,S., Helbig,K.L., Alcaraz,W., Riviere,J.B.,
            Faivre,L., Innes,A.M., Lebel,R.R. and Boycott,K.M.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Autosomal recessive mutations in THOC6 cause intellectual
            disability: syndrome delineation requiring forward and reverse
            phenotyping
  JOURNAL   Clin Genet 91 (1), 92-99 (2017)
   PUBMED   27102954
  REMARK    GeneRIF: Results indicate three unrelated patients with bi-allelic
            mutations in THOC6 associated with intellectual disability and
            additional clinical features.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Anazi,S., Alshammari,M., Moneis,D., Abouelhoda,M., Ibrahim,N. and
            Alkuraya,F.S.
  TITLE     Confirming the candidacy of THOC6 in the etiology of intellectual
            disability
  JOURNAL   Am J Med Genet A 170A (5), 1367-1369 (2016)
   PUBMED   26739162
  REMARK    GeneRIF: In addition to confirming the morbid nature of THOC6 by
            providing an independent homozygous apparently loss of function
            allele in a patient with a compatible phenotype, our data also
            expand THOC6-related phenotype to include previously unreported
            imperforate anus and undescended testicles.
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Beaulieu,C.L., Huang,L., Innes,A.M., Akimenko,M.A.,
            Puffenberger,E.G., Schwartz,C., Jerry,P., Ober,C., Hegele,R.A.,
            McLeod,D.R., Schwartzentruber,J., Majewski,J., Bulman,D.E.,
            Parboosingh,J.S. and Boycott,K.M.
  CONSRTM   FORGE Canada Consortium
  TITLE     Intellectual disability associated with a homozygous missense
            mutation in THOC6
  JOURNAL   Orphanet J Rare Dis 8, 62 (2013)
   PUBMED   23621916
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Boyne,J.R., Colgan,K.J. and Whitehouse,A.
  TITLE     Recruitment of the complete hTREX complex is required for Kaposi's
            sarcoma-associated herpesvirus intronless mRNA nuclear export and
            virus replication
  JOURNAL   PLoS Pathog 4 (10), e1000194 (2008)
   PUBMED   18974867
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Cheng,H., Dufu,K., Lee,C.S., Hsu,J.L., Dias,A. and Reed,R.
  TITLE     Human mRNA export machinery recruited to the 5' end of mRNA
  JOURNAL   Cell 127 (7), 1389-1400 (2006)
   PUBMED   17190602
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Masuda,S., Das,R., Cheng,H., Hurt,E., Dorman,N. and Reed,R.
  TITLE     Recruitment of the human TREX complex to mRNA during splicing
  JOURNAL   Genes Dev 19 (13), 1512-1517 (2005)
   PUBMED   15998806
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Guo,S., Hakimi,M.A., Baillat,D., Chen,X., Farber,M.J.,
            Klein-Szanto,A.J., Cooch,N.S., Godwin,A.K. and Shiekhattar,R.
  TITLE     Linking transcriptional elongation and messenger RNA export to
            metastatic breast cancers
  JOURNAL   Cancer Res 65 (8), 3011-3016 (2005)
   PUBMED   15833825
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Lemire,G., Innes,A.M. and Boycott,K.M.
  TITLE     THOC6 Intellectual Disability Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32790266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX425088.2, AK075330.1,
            AC108134.3 and BM457458.1.
            
            Summary: This gene encodes a subunit of the multi-protein THO
            complex, which is involved in coordination between transcription
            and mRNA processing. The THO complex is a component of the TREX
            (transcription/export) complex, which is involved in transcription
            and export of mRNAs. A missense mutation in this gene is associated
            with a neurodevelopmental disorder called Beaulieu-Boycott-Innes
            syndrome. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The encoded isoform (2) has the same N-
            and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075330.1, ERR3218372.319837.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..296
                     /product="THO complex subunit 6 isoform 2"
                     /note="WD repeat domain 58; functional
                     spliceosome-associated protein 35; THO complex subunit 6
                     homolog; WD repeat-containing protein 58; THO complex 6"
                     /calculated_mol_wt=32760
     Region          7..>256
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          28..74
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          79..115
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          130..165
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..210
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          218..260
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..296
                     /gene="THOC6"
                     /gene_synonym="fSAP35; MMRFCGU; WDR58"
                     /coded_by="NM_001142350.3:293..1183"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45392.1"
                     /db_xref="GeneID:79228"
                     /db_xref="HGNC:HGNC:28369"
                     /db_xref="MIM:615403"
ORIGIN      
        1 meravplavp lgqtevfqal qrlhmtifsq svspcgkfla agnnygqiai fslssalsse
       61 akeeskkpvv tfqahdgpvy smvstdrhll sagdgevkaw lwaemlkkgc kelwrrqppy
      121 rtslevpein alllvpkens lilaggdcql htmdletgtf trvlrghtdy ihclalrers
      181 pevlsggedg avrlwdlrta kevqtievyk heecsrphng rwigclatds dwmvcgggpa
      241 ltlwhlrsst pttifpirap qkhvtfyqdl vltaagnscr vdvftnlgyr afslsf
//
LOCUS       NP_001257411             422 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 11 [Homo sapiens].
ACCESSION   NP_001257411
VERSION     NP_001257411.1
DBSOURCE    REFSEQ: accession NM_001270482.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Deb,W., Rosenfelt,C., Vignard,V., Papendorf,J.J., Moller,S.,
            Wendlandt,M., Studencka-Turski,M., Cogne,B., Besnard,T.,
            Ruffier,L., Toutain,B., Poirier,L., Cuinat,S., Kritzer,A.,
            Crunk,A., diMonda,J., Vengoechea,J., Mercier,S., Kleinendorst,L.,
            van Haelst,M.M., Zuurbier,L., Sulem,T., Katrinardottir,H.,
            Friethriksdottir,R., Sulem,P., Stefansson,K., Jonsdottir,B.,
            Zeidler,S., Sinnema,M., Stegmann,A.P.A., Naveh,N., Skraban,C.M.,
            Gray,C., Murrell,J.R., Isikay,S., Pehlivan,D., Calame,D.G.,
            Posey,J.E., Nizon,M., McWalter,K., Lupski,J.R., Isidor,B.,
            Bolduc,F.V., Bezieau,S., Kruger,E., Kury,S. and Ebstein,F.
  TITLE     PSMD11 loss-of-function variants correlate with a neurobehavioral
            phenotype, obesity, and increased interferon response
  JOURNAL   Am J Hum Genet 111 (7), 1352-1369 (2024)
   PUBMED   38866022
  REMARK    GeneRIF: PSMD11 loss-of-function variants correlate with a
            neurobehavioral phenotype, obesity, and increased interferon
            response.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Cal-Kayitmazbatir,S., Francey,L.J., Lee,Y., Liu,A.C. and
            Hogenesch,J.B.
  TITLE     PSMD11 modulates circadian clock function through PER and CRY
            nuclear translocation
  JOURNAL   PLoS One 18 (3), e0283463 (2023)
   PUBMED   36961772
  REMARK    GeneRIF: PSMD11 modulates circadian clock function through PER and
            CRY nuclear translocation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Saito,A., Watanabe,T.K., Shimada,Y., Fujiwara,T., Slaughter,C.A.,
            DeMartino,G.N., Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p44.5 and p55, two
            regulatory subunits of the 26S proteasome
  JOURNAL   Gene 203 (2), 241-250 (1997)
   PUBMED   9426256
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Hoffman,L. and Rechsteiner,M.
  TITLE     Molecular cloning and expression of subunit 9 of the 26S proteasome
  JOURNAL   FEBS Lett 404 (2-3), 179-184 (1997)
   PUBMED   9119060
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Kanayama,H.O., Tamura,T., Ugai,S., Kagawa,S., Tanahashi,N.,
            Yoshimura,T., Tanaka,K. and Ichihara,A.
  TITLE     Demonstration that a human 26S proteolytic complex consists of a
            proteasome and multiple associated protein components and
            hydrolyzes ATP and ubiquitin-ligated proteins by closely linked
            mechanisms
  JOURNAL   Eur J Biochem 206 (2), 567-578 (1992)
   PUBMED   1317798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290602.1, AC079336.5 and
            BQ006240.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. This
            gene encodes a member of the proteasome subunit S9 family that
            functions as a non-ATPase subunit of the 19S regulator and is
            phosphorylated by AMP-activated protein kinase. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.228002.1,
                                           SRR1163655.77714.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..422
                     /product="26S proteasome non-ATPase regulatory subunit 11"
                     /note="26S proteasome regulatory subunit 9; 26S proteasome
                     regulatory subunit S9; 26S proteasome regulatory subunit
                     p44.5; 26S proteasome regulatory subunit RPN6; proteasome
                     (prosome, macropain) 26S subunit, non-ATPase, 11"
                     /calculated_mol_wt=47333
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00231.3)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17323924,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00231.3)"
     Region          17..421
                     /region_name="RPN6"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5159"
                     /db_xref="CDD:227488"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00231.3)"
     CDS             1..422
                     /gene="PSMD11"
                     /gene_synonym="p44.5; Rpn6; S9"
                     /coded_by="NM_001270482.2:15..1283"
                     /db_xref="CCDS:CCDS11272.1"
                     /db_xref="GeneID:5717"
                     /db_xref="HGNC:HGNC:9556"
                     /db_xref="MIM:604449"
ORIGIN      
        1 maaaavvefq raqsllstdr easidilhsi vkrdiqende eavqvkeqsi lelgsllakt
       61 gqaaelggll kyvrpflnsi skakaarlvr slldlfldme aatgqevelc leciewakse
      121 krtflrqale arlvslyfdt kryqealhlg sqllrelkkm ddkallvevq llesktyhal
      181 snlpkaraal tsarttanai ycppklqatl dmqsgiihaa eekdwktays yfyeafegyd
      241 sidspkaits lkymllckim lntpedvqal vsgklalrya grqtealkcv aqasknrsla
      301 dfekaltdyr aelrddpiis thlaklydnl leqnlirvie pfsrvqiehi ssliklskad
      361 verklsqmil dkkfhgildq gegvliifde ppvdktyeaa letiqnmskv vdslynkakk
      421 lt
//
LOCUS       NP_001278845              78 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein Sm D1 isoform 2 [Homo sapiens].
ACCESSION   NP_001278845
VERSION     NP_001278845.1
DBSOURCE    REFSEQ: accession NM_001291916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Polverini,E., Squeri,P. and Gherardi,V.
  TITLE     Effect of E134K pathogenic mutation of SMN protein on SMN-SmD1
            interaction, with implication in spinal muscular atrophy: A
            molecular dynamics study
  JOURNAL   Int J Biol Macromol 275 (Pt 2), 133663 (2024)
   PUBMED   38969036
  REMARK    GeneRIF: Effect of E134K pathogenic mutation of SMN protein on
            SMN-SmD1 interaction, with implication in spinal muscular atrophy:
            A molecular dynamics study.
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Sun,D., Ou,Y.C. and Hoch,S.O.
  TITLE     Analysis of genes for human snRNP Sm-D1 protein and identification
            of the promoter sequence which shows segmental homology to the
            promoters of Sm-E and U1 snRNA genes
  JOURNAL   Gene 189 (2), 245-254 (1997)
   PUBMED   9168134
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Lehmeier,T., Raker,V., Hermann,H. and Luhrmann,R.
  TITLE     cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
            ribonucleoproteins: evidence for a direct D1-D2 interaction
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12317-12321 (1994)
   PUBMED   7527560
REFERENCE   8  (residues 1 to 78)
  AUTHORS   Lehmeier,T., Foulaki,K. and Luhrmann,R.
  TITLE     Evidence for three distinct D proteins, which react differentially
            with anti-Sm autoantibodies, in the cores of the major snRNPs U1,
            U2, U4/U6 and U5
  JOURNAL   Nucleic Acids Res 18 (22), 6475-6484 (1990)
   PUBMED   1701240
REFERENCE   9  (residues 1 to 78)
  AUTHORS   Renz,M., Heim,C., Braunling,O., Czichos,A., Wieland,C. and
            Seelig,H.P.
  TITLE     Expression of the major human ribonucleoprotein (RNP) autoantigens
            in Escherichia coli and their use in an EIA for screening sera from
            patients with autoimmune diseases
  JOURNAL   Clin Chem 35 (9), 1861-1863 (1989)
   PUBMED   2528429
REFERENCE   10 (residues 1 to 78)
  AUTHORS   Rokeach,L.A., Haselby,J.A. and Hoch,S.O.
  TITLE     Molecular cloning of a cDNA encoding the human Sm-D autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 85 (13), 4832-4836 (1988)
   PUBMED   3260384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY043971.1, CN354758.1,
            J03798.1 and AC106037.9.
            
            Summary: This gene encodes a small nuclear ribonucleoprotein that
            belongs to the SNRNP core protein family. The protein may act as a
            charged protein scaffold to promote SNRNP assembly or strengthen
            SNRNP-SNRNP interactions through nonspecific electrostatic contacts
            with RNA. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice junction at the 5' end of an exon compared to variant 1. The
            resulting isoform (2) has the same N- and C-termini but is shorter
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.101562.1,
                                           SRR5189658.134007.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..78
                     /product="small nuclear ribonucleoprotein Sm D1 isoform 2"
                     /note="snRNP core protein D1; Sm-D autoantigen; small
                     nuclear ribonucleoprotein Sm D1; small nuclear
                     ribonucleoprotein D1 polypeptide 16kDa pseudogene"
                     /calculated_mol_wt=8471
     Region          2..52
                     /region_name="Sm_like"
                     /note="Sm and related proteins; cl00259"
                     /db_xref="CDD:469694"
     CDS             1..78
                     /gene="SNRPD1"
                     /gene_synonym="HsT2456; Sm-D1; SMD1; SNRPD"
                     /coded_by="NM_001291916.2:117..353"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6632"
                     /db_xref="HGNC:HGNC:11158"
                     /db_xref="MIM:601063"
ORIGIN      
        1 mklvrflmkl shetvtielk ngtqvhgtit dslpldtllv dvepkvkskk reavagrgrg
       61 rgrgrgrgrg rgrggprr
//
LOCUS       NP_000802                453 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-6 precursor [Homo
            sapiens].
ACCESSION   NP_000802
VERSION     NP_000802.2
DBSOURCE    REFSEQ: accession NM_000811.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Sente,A., Desai,R., Naydenova,K., Malinauskas,T., Jounaidi,Y.,
            Miehling,J., Zhou,X., Masiulis,S., Hardwick,S.W., Chirgadze,D.Y.,
            Miller,K.W. and Aricescu,A.R.
  TITLE     Differential assembly diversifies GABAA receptor structures and
            signalling
  JOURNAL   Nature 604 (7904), 190-194 (2022)
   PUBMED   35355020
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Riaz,M., Abbasi,M.H., Sheikh,N., Saleem,T. and Virk,A.O.
  TITLE     GABRA1 and GABRA6 gene mutations in idiopathic generalized epilepsy
            patients
  JOURNAL   Seizure 93, 88-94 (2021)
   PUBMED   34740144
  REMARK    GeneRIF: GABRA1 and GABRA6 gene mutations in idiopathic generalized
            epilepsy patients.
REFERENCE   3  (residues 1 to 453)
  AUTHORS   Ghit,A., Assal,D., Al-Shami,A.S. and Hussein,D.E.E.
  TITLE     GABAA receptors: structure, function, pharmacology, and related
            disorders
  JOURNAL   J Genet Eng Biotechnol 19 (1), 123 (2021)
   PUBMED   34417930
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 453)
  AUTHORS   Gonda,X., Sarginson,J., Eszlari,N., Petschner,P., Toth,Z.G.,
            Baksa,D., Hullam,G., Anderson,I.M., Deakin,J.F.W., Juhasz,G. and
            Bagdy,G.
  TITLE     A new stress sensor and risk factor for suicide: the T allele of
            the functional genetic variant in the GABRA6 gene
  JOURNAL   Sci Rep 7 (1), 12887 (2017)
   PUBMED   29018204
  REMARK    GeneRIF: stress-associated suicide risk is elevated in carriers of
            the GABRA6 rs3219151 T allele with several independent markers and
            predictors of suicidal behaviours converging to this increased
            risk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 453)
  AUTHORS   Chua,H.C. and Chebib,M.
  TITLE     GABAA Receptors and the Diversity in their Structure and
            Pharmacology
  JOURNAL   Adv Pharmacol 79, 1-34 (2017)
   PUBMED   28528665
  REMARK    Review article
REFERENCE   6  (residues 1 to 453)
  AUTHORS   Comings,D.E., Gade-Andavolu,R., Gonzalez,N., Wu,S., Muhleman,D.,
            Blake,H., Mann,M.B., Dietz,G., Saucier,G. and MacMurray,J.P.
  TITLE     A multivariate analysis of 59 candidate genes in personality
            traits: the temperament and character inventory
  JOURNAL   Clin Genet 58 (5), 375-385 (2000)
   PUBMED   11140838
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 453)
  AUTHORS   Russek,S.J.
  TITLE     Evolution of GABA(A) receptor diversity in the human genome
  JOURNAL   Gene 227 (2), 213-222 (1999)
   PUBMED   10023064
REFERENCE   8  (residues 1 to 453)
  AUTHORS   Hadingham,K.L., Garrett,E.M., Wafford,K.A., Bain,C., Heavens,R.P.,
            Sirinathsinghji,D.J. and Whiting,P.J.
  TITLE     Cloning of cDNAs encoding the human gamma-aminobutyric acid type A
            receptor alpha 6 subunit and characterization of the pharmacology
            of alpha 6-containing receptors
  JOURNAL   Mol Pharmacol 49 (2), 253-259 (1996)
   PUBMED   8632757
REFERENCE   9  (residues 1 to 453)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
REFERENCE   10 (residues 1 to 453)
  AUTHORS   Hicks,A.A., Bailey,M.E., Riley,B.P., Kamphuis,W., Siciliano,M.J.,
            Johnson,K.J. and Darlison,M.G.
  TITLE     Further evidence for clustering of human GABAA receptor subunit
            genes: localization of the alpha 6-subunit gene (GABRA6) to distal
            chromosome 5q by linkage analysis
  JOURNAL   Genomics 20 (2), 285-288 (1994)
   PUBMED   8020978
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA068807.1, BC096241.3 and
            AC091944.2.
            
            On Sep 20, 2007 this sequence version replaced NP_000802.1.
            
            Summary: GABA is the major inhibitory neurotransmitter in the
            mammalian brain where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. Chloride conductance of these
            channels can be modulated by agents such as benzodiazepines that
            bind to the GABA-A receptor. At least 16 distinct subunits of
            GABA-A receptors have been identified. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.258927.1,
                                           SRR1660803.145888.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274545.10/ ENSP00000274545.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..453
                     /product="gamma-aminobutyric acid receptor subunit alpha-6
                     precursor"
                     /note="gamma-aminobutyric acid receptor subunit alpha-6;
                     GABA subunit A receptor alpha 6; GABA(A) receptor subunit
                     alpha-6; GABA(A) receptor, alpha 6; gamma-aminobutyric
                     acid (GABA) A receptor, alpha 6; gamma-aminobutyric acid
                     type A receptor alpha6 subunit; GABAAR subunit alpha-6"
                     /calculated_mol_wt=48912
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2131
     Region          5..440
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     20..453
                     /product="gamma-aminobutyric acid receptor subunit
                     alpha-6"
                     /calculated_mol_wt=48912
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16445.2)"
     Region          42..239
                     /region_name="LGIC_ECD_GABAAR_A6"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-6 (GABAAR-A6 or GABRA6); cd19039"
                     /db_xref="CDD:349840"
     Site            order(54,82)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349840"
     Site            order(66,68..69,74..75,82,84..85,102,104..105,114..119,
                     122,124,126..127,133..135,137,147..149,177,239)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349840"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16445.2)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q16445.2)"
     Region          156..170
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349840"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16445.2)"
     Site            271..290
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16445.2)"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16445.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P30191; propagated from
                     UniProtKB/Swiss-Prot (Q16445.2)"
     Site            423..443
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16445.2)"
     CDS             1..453
                     /gene="GABRA6"
                     /coded_by="NM_000811.3:270..1631"
                     /db_xref="CCDS:CCDS4356.1"
                     /db_xref="GeneID:2559"
                     /db_xref="HGNC:HGNC:4080"
                     /db_xref="MIM:137143"
ORIGIN      
        1 masslpwlci ilwlenalgk levegnfyse nvsrildnll egydnrlrpg fggavtevkt
       61 diyvtsfgpv sdvemeytmd vffrqtwtde rlkfggptei lslnnlmvsk iwtpdtffrn
      121 gkksiahnmt tpnklfrimq ngtilytmrl tinadcpmrl vnfpmdghac plkfgsyayp
      181 kseiiytwkk gplysvevpe esssllqydl igqtvsseti ksntgeyvim tvyfhlqrkm
      241 gyfmiqiytp cimtvilsqv sfwinkesvp artvfgittv ltmttlsisa rhslpkvsya
      301 tamdwfiavc fafvfsalie faavnyftnl qtqkakrkaq faapptvtis katepleaei
      361 vlhpdskyhl kkritslslp ivssseankv ltrapilqst pvtppplspa fggtskidqy
      421 srilfpvafa gfnlvywvvy lskdtmevss sve
//
LOCUS       NP_001269237             332 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 25 isoform 3 [Homo sapiens].
ACCESSION   NP_001269237 XP_005247043
VERSION     NP_001269237.1
DBSOURCE    REFSEQ: accession NM_001282308.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Chen,K.Q., Lei,G.L., Ke,B.Y., Chen,L., Wang,Z.B. and Wang,S.Z.
  TITLE     STK25: a viable therapeutic target for cancer treatments?
  JOURNAL   Anticancer Drugs 34 (9), 995-1001 (2023)
   PUBMED   36728989
  REMARK    GeneRIF: STK25: a viable therapeutic target for cancer treatments?
            Review article
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Zhang,X., Wang,B.Z., Kim,M., Nash,T.R., Liu,B., Rao,J., Lock,R.,
            Tamargo,M., Soni,R.K., Belov,J., Li,E., Vunjak-Novakovic,G. and
            Fine,B.
  TITLE     STK25 inhibits PKA signaling by phosphorylating PRKAR1A
  JOURNAL   Cell Rep 40 (7), 111203 (2022)
   PUBMED   35977512
  REMARK    GeneRIF: STK25 inhibits PKA signaling by phosphorylating PRKAR1A.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Chen,J., Gao,P., Peng,L., Liu,T., Wu,F., Xu,K., Chen,L., Tan,F.,
            Xing,P., Wang,Z., Di,J., Jiang,B. and Su,X.
  TITLE     Downregulation of STK25 promotes autophagy via the Janus kinase
            2/signal transducer and activator of transcription 3 pathway in
            colorectal cancer
  JOURNAL   Mol Carcinog 61 (6), 572-586 (2022)
   PUBMED   35349179
  REMARK    GeneRIF: Downregulation of STK25 promotes autophagy via the Janus
            kinase 2/signal transducer and activator of transcription 3 pathway
            in colorectal cancer.
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Findlay,G.M., Yan,L., Procter,J., Mieulet,V. and Lamb,R.F.
  TITLE     A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of
            mTOR signalling
  JOURNAL   Biochem J 403 (1), 13-20 (2007)
   PUBMED   17253963
  REMARK    GeneRIF: Ste20 family member (MAP4K3) that is required for maximal
            S6K (S6 kinase)/4E-BP1 [eIF4E (eukaryotic initiation factor 4E)
            that is required for maximal S6K (S6 kinase).
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Preisinger,C., Short,B., De Corte,V., Bruyneel,E., Haas,A.,
            Kopajtich,R., Gettemans,J. and Barr,F.A.
  TITLE     YSK1 is activated by the Golgi matrix protein GM130 and plays a
            role in cell migration through its substrate 14-3-3zeta
  JOURNAL   J Cell Biol 164 (7), 1009-1020 (2004)
   PUBMED   15037601
  REMARK    GeneRIF: 14-3-3zeta is a specific substrate for YSK1 that localizes
            to the Golgi apparatus, and potentially links YSK1 signaling at the
            Golgi apparatus with protein transport.
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Osada,S., Izawa,M., Saito,R., Mizuno,K., Suzuki,A., Hirai,S. and
            Ohno,S.
  TITLE     YSK1, a novel mammalian protein kinase structurally related to
            Ste20 and SPS1, but is not involved in the known MAPK pathways
  JOURNAL   Oncogene 14 (17), 2047-2057 (1997)
   PUBMED   9160885
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Pombo,C.M., Bonventre,J.V., Molnar,A., Kyriakis,J. and Force,T.
  TITLE     Activation of a human Ste20-like kinase by oxidant stress defines a
            novel stress response pathway
  JOURNAL   EMBO J 15 (17), 4537-4546 (1996)
   PUBMED   8887545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315966.1, CB250694.1,
            HY315908.1 and AC110299.3.
            
            On Aug 29, 2013 this sequence version replaced XP_005247043.1.
            
            Summary: This gene encodes a member of the germinal centre kinase
            III (GCK III) subfamily of the sterile 20 superfamily of kinases.
            The encoded enzyme plays a role in serine-threonine liver kinase B1
            (LKB1) signaling pathway to regulate neuronal polarization and
            morphology of the Golgi apparatus. The protein is translocated from
            the Golgi apparatus to the nucleus in response to chemical anoxia
            and plays a role in regulation of cell death. A pseudogene
            associated with this gene is located on chromosome 18. Multiple
            alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (7) lacks an exon which contains a
            portion of the 5' UTR and 5' coding region including the start
            codon, compared to variant 1. These differences cause translation
            initiation at a downstream start codon and result in an isoform (3)
            with a shorter N-terminus, compared to isoform 1. Variants 2, 6,
            and 7 encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1914114.1, AK315966.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..332
                     /product="serine/threonine-protein kinase 25 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 25; Ste20, yeast
                     homolog; ste20-like kinase; ste20/oxidant stress response
                     kinase 1; sterile 20/oxidant stress-response kinase 1"
                     /calculated_mol_wt=37166
     Region          <1..197
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..332
                     /gene="STK25"
                     /gene_synonym="SOK1; YSK1"
                     /coded_by="NM_001282308.2:333..1331"
                     /note="isoform 3 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS63199.1"
                     /db_xref="GeneID:10494"
                     /db_xref="HGNC:HGNC:11404"
                     /db_xref="MIM:602255"
ORIGIN      
        1 meylgggsal dllkpgplee tyiatilrei lkgldylhse rkihrdikaa nvllseqgdv
       61 kladfgvagq ltdtqikrnt fvgtpfwmap evikqsaydf kadiwslgit aielakgepp
      121 nsdlhpmrvl flipknsppt legqhskpfk efveaclnkd prfrptakel lkhkfitryt
      181 kktsflteli drykrwkseg hgeessseds didgeaedge qgpiwtfppt irpsphsklh
      241 kgtalhssqk paepvkrqpr sqclstlvrp vfgelkekhk qsggsvgale elenafslae
      301 escpgisdkl mvhlvervqr fshnrnhlts tr
//
LOCUS       NP_001012412             309 aa            linear   PRI 20-NOV-2025
DEFINITION  shugoshin 1 isoform 1GH [Homo sapiens].
ACCESSION   NP_001012412
VERSION     NP_001012412.1
DBSOURCE    REFSEQ: accession NM_001012412.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 309)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494477.1, AB193063.1 and
            AB187578.1.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (Sgo1H, PMID:15737064, also known
            as B2) differs in its 5' UTR, uses an alternate in-frame splice
            site in its central coding region, and contains an alternate 3'
            terminal segment compared to variant 1, resulting in a novel 3'
            coding region and distinct 3' UTR. It encodes isoform 1GH which is
            shorter, has a distinct internal amino acid, and has a distinct
            C-terminus, compared to isoform 1. Both variants Sgo1G and Sgo1H
            encode the same isoform (1GH).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB187580.1, AB193063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..309
                     /product="shugoshin 1 isoform 1GH"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=35213
     Region          1..176
                     /region_name="Necessary for interaction with PPP2CA and
                     PPP2R1A. /evidence=ECO:0000269|PubMed:16580887"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          222..243
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     CDS             1..309
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001012412.5:156..1085"
                     /note="isoform 1GH is encoded by transcript variant Sgo1H"
                     /db_xref="CCDS:CCDS46771.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqiedq iptipqdtlg vdfdsatppe
      181 tqqsphlslk ditnvslypv vkirrlslsp kknkaspava lpkrrctasv nykeptlask
      241 lrrgdpftdl cflnspifkq kkdlrrskkr alevspakea ifilyyvref vsrfpdcrkc
      301 klethiclr
//
LOCUS       NP_001355003            1363 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFX7 isoform 2 [Homo sapiens].
ACCESSION   NP_001355003
VERSION     NP_001355003.1
DBSOURCE    REFSEQ: accession NM_001368074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1363)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1363)
  AUTHORS   Coronel,L., Riege,K., Schwab,K., Forste,S., Hackes,D., Semerau,L.,
            Bernhart,S.H., Siebert,R., Hoffmann,S. and Fischer,M.
  TITLE     Transcription factor RFX7 governs a tumor suppressor network in
            response to p53 and stress
  JOURNAL   Nucleic Acids Res 49 (13), 7437-7456 (2021)
   PUBMED   34197623
  REMARK    GeneRIF: Transcription factor RFX7 governs a tumor suppressor
            network in response to p53 and stress.
REFERENCE   3  (residues 1 to 1363)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1363)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 1363)
  AUTHORS   Castro,W., Chelbi,S.T., Niogret,C., Ramon-Barros,C., Welten,S.P.M.,
            Osterheld,K., Wang,H., Rota,G., Morgado,L., Vivier,E., Raeber,M.E.,
            Boyman,O., Delorenzi,M., Barras,D., Ho,P.C., Oxenius,A. and
            Guarda,G.
  TITLE     The transcription factor Rfx7 limits metabolism of NK cells and
            promotes their maintenance and immunity
  JOURNAL   Nat Immunol 19 (8), 809-820 (2018)
   PUBMED   29967452
REFERENCE   6  (residues 1 to 1363)
  AUTHORS   Berndt,S.I., Skibola,C.F., Joseph,V., Camp,N.J., Nieters,A.,
            Wang,Z., Cozen,W., Monnereau,A., Wang,S.S., Kelly,R.S., Lan,Q.,
            Teras,L.R., Chatterjee,N., Chung,C.C., Yeager,M.,
            Brooks-Wilson,A.R., Hartge,P., Purdue,M.P., Birmann,B.M.,
            Armstrong,B.K., Cocco,P., Zhang,Y., Severi,G.,
            Zeleniuch-Jacquotte,A., Lawrence,C., Burdette,L., Yuenger,J.,
            Hutchinson,A., Jacobs,K.B., Call,T.G., Shanafelt,T.D., Novak,A.J.,
            Kay,N.E., Liebow,M., Wang,A.H., Smedby,K.E., Adami,H.O., Melbye,M.,
            Glimelius,B., Chang,E.T., Glenn,M., Curtin,K.,
            Cannon-Albright,L.A., Jones,B., Diver,W.R., Link,B.K., Weiner,G.J.,
            Conde,L., Bracci,P.M., Riby,J., Holly,E.A., Smith,M.T.,
            Jackson,R.D., Tinker,L.F., Benavente,Y., Becker,N., Boffetta,P.,
            Brennan,P., Foretova,L., Maynadie,M., McKay,J., Staines,A.,
            Rabe,K.G., Achenbach,S.J., Vachon,C.M., Goldin,L.R., Strom,S.S.,
            Lanasa,M.C., Spector,L.G., Leis,J.F., Cunningham,J.M.,
            Weinberg,J.B., Morrison,V.A., Caporaso,N.E., Norman,A.D.,
            Linet,M.S., De Roos,A.J., Morton,L.M., Severson,R.K., Riboli,E.,
            Vineis,P., Kaaks,R., Trichopoulos,D., Masala,G., Weiderpass,E.,
            Chirlaque,M.D., Vermeulen,R.C., Travis,R.C., Giles,G.G.,
            Albanes,D., Virtamo,J., Weinstein,S., Clavel,J., Zheng,T.,
            Holford,T.R., Offit,K., Zelenetz,A., Klein,R.J., Spinelli,J.J.,
            Bertrand,K.A., Laden,F., Giovannucci,E., Kraft,P., Kricker,A.,
            Turner,J., Vajdic,C.M., Ennas,M.G., Ferri,G.M., Miligi,L.,
            Liang,L., Sampson,J., Crouch,S., Park,J.H., North,K.E., Cox,A.,
            Snowden,J.A., Wright,J., Carracedo,A., Lopez-Otin,C., Bea,S.,
            Salaverria,I., Martin-Garcia,D., Campo,E., Fraumeni,J.F. Jr., de
            Sanjose,S., Hjalgrim,H., Cerhan,J.R., Chanock,S.J., Rothman,N. and
            Slager,S.L.
  TITLE     Genome-wide association study identifies multiple risk loci for
            chronic lymphocytic leukemia
  JOURNAL   Nat Genet 45 (8), 868-876 (2013)
   PUBMED   23770605
REFERENCE   7  (residues 1 to 1363)
  AUTHORS   Crowther-Swanepoel,D., Broderick,P., Di Bernardo,M.C.,
            Dobbins,S.E., Torres,M., Mansouri,M., Ruiz-Ponte,C., Enjuanes,A.,
            Rosenquist,R., Carracedo,A., Jurlander,J., Campo,E., Juliusson,G.,
            Montserrat,E., Smedby,K.E., Dyer,M.J., Matutes,E., Dearden,C.,
            Sunter,N.J., Hall,A.G., Mainou-Fowler,T., Jackson,G.H.,
            Summerfield,G., Harris,R.J., Pettitt,A.R., Allsup,D.J.,
            Bailey,J.R., Pratt,G., Pepper,C., Fegan,C., Parker,A., Oscier,D.,
            Allan,J.M., Catovsky,D. and Houlston,R.S.
  TITLE     Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence
            chronic lymphocytic leukemia risk
  JOURNAL   Nat Genet 42 (2), 132-136 (2010)
   PUBMED   20062064
REFERENCE   8  (residues 1 to 1363)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   9  (residues 1 to 1363)
  AUTHORS   Aftab,S., Semenec,L., Chu,J.S. and Chen,N.
  TITLE     Identification and characterization of novel human tissue-specific
            RFX transcription factors
  JOURNAL   BMC Evol Biol 8, 226 (2008)
   PUBMED   18673564
  REMARK    GeneRIF: RFX7 is a winged helix transcription factor expressed
            ubiquitously in all tissues examined, especially brain tissue.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1363)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084783.2 and KF456052.1.
            
            Summary: RFX7 is a member of the regulatory factor X (RFX) family
            of transcription factors (see RFX1, MIM 600006) (Aftab et al., 2008
            [PubMed 18673564]).[supplied by OMIM, Mar 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC112936.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1363
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1363
                     /product="DNA-binding protein RFX7 isoform 2"
                     /note="regulatory factor X domain containing 2;
                     DNA-binding protein RFX7; regulatory factor X
                     domain-containing protein 2; regulatory factor X, 7"
                     /calculated_mol_wt=146765
     Region          8..86
                     /region_name="RFX_DNA_binding"
                     /note="RFX DNA-binding domain; pfam02257"
                     /db_xref="CDD:460512"
     Region          <161..471
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          371..>648
                     /region_name="MSCRAMM_ClfA"
                     /note="MSCRAMM family adhesin clumping factor ClfA;
                     NF033609"
                     /db_xref="CDD:468110"
     CDS             1..1363
                     /gene="RFX7"
                     /gene_synonym="MRD71; RFXDC2"
                     /coded_by="NM_001368074.1:229..4320"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92003.1"
                     /db_xref="GeneID:64864"
                     /db_xref="HGNC:HGNC:25777"
                     /db_xref="MIM:612660"
ORIGIN      
        1 msssraqqmh afswirntle ehpetslpkq evydeyksyc dnlgyhplsa adfgkimknv
       61 fpnmkarrlg trgkskycys glrkkafvhm ptlpnldfhk tgdglegaep sgqlqnidee
      121 vissacrlvc ewaqkvlsqp fdtvlelarf lvkshyigtk smaaltvmaa apagmkgitq
      181 psafiptaes nsfqpqvktl pspidakqql qrkiqkkqqe qklqsplpge saakksesat
      241 sngvtnlpng npsilspqpi givvaavpsp ipvqrtrqlv tspspmsssd gkvlplnvqv
      301 vtqhmqsvkq apktpqnvpa spggdrsarh rypqilpkpa ntsaltirsp ttvlftsspi
      361 ktavvpashm sslnvvkmtt isltpsnsnt plkhsasvss atgtteesrs vpqikngsvv
      421 slqspgsrss saggtsavev kvepetssde hpvqcqensd eakapqtpsa llgqksntdg
      481 alqkpsnegv ieikatkvcd qrtkcksrcn emlpgtstgn nqstitlsva sqnltftsss
      541 sppngdsink dpklctkspr krlsstlqet qvppvkkpiv eqlsaatieg qkqgsvkkdq
      601 kvphsgkteg stagaqipsk vsvnvsshig anqplnssal visdsaleqq ttpssspdik
      661 vklegsvfll dsdsksvgsf npngwqqitk dsefisasce qqqdisvmti pehsdindle
      721 ksvwelegmp qdtysqqlhs qiqesslnqi qahssdqlpl qselkefeps vsqtnesyfp
      781 fddeltqdsi veelvlmeqq msmnnshsyg nclgmtlqsq svtpgapmss htssthfyhp
      841 ihsngtpiht ptptptptpt ptptptptse miagsqslsr espcsrlaqt tpvdsalgss
      901 rhtpigtphs ncsssvppsp vecrnpfaft pisssmayhd asivssspvk pmqrpmathp
      961 dktklewmnn gysgvgnssv sghgilpsyq elvedrfrkp hafavpgqsy qsqsrhhdth
     1021 fgrltpvspv qhqgatvnnt nkqegfavpa pldnkgtnss assnfrcrsv spavhrqrnl
     1081 sgstlypvsn iprsnvtpfg spvtpevhvf tnvhtdacan niaqrsqsvp ltvmmqtafp
     1141 nalqkqansk kitnvllskl dsdnddavrg lgmnnlpsny tarmnltqil epstvfpsan
     1201 pqnmidssts vyefqtpsyl tksnstgqin fspgdnqaqs eigeqqldfn stvkdllsgd
     1261 slqtnqqlvg qgasdltnta sdfssdirls selsgsindl ntldpnllfd pgrqqgqdde
     1321 atleelkndp lfqqicsesm nsmtssgfew ieskdhptve mlg
//
LOCUS       NP_079513                213 aa            linear   PRI 20-NOV-2025
DEFINITION  sclerostin precursor [Homo sapiens].
ACCESSION   NP_079513
VERSION     NP_079513.1
DBSOURCE    REFSEQ: accession NM_025237.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 213)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 213)
  AUTHORS   McKean,D.M., Zhang,Q., Narayan,P., Morton,S.U., Strohmenger,V.,
            Tang,V.T., McAllister,S., Sharma,A., Quiat,D., Reichart,D.,
            DeLaughter,D.M., Wakimoto,H., Gorham,J.M., Brown,K., McDonough,B.,
            Willcox,J.A., Jang,M.Y., DePalma,S.R., Ward,T., Kim,R.,
            Cleveland,J.D., Seidman,J.G. and Seidman,C.E.
  CONSRTM   Pediatric Cardiac Genomics Consortium Investigators
  TITLE     Increased endothelial sclerostin caused by elevated DSCAM mediates
            multiple trisomy 21 phenotypes
  JOURNAL   J Clin Invest 134 (11), e167811 (2024)
   PUBMED   38828726
  REMARK    GeneRIF: Increased endothelial sclerostin caused by elevated DSCAM
            mediates multiple trisomy 21 phenotypes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 213)
  AUTHORS   Liu,Y., Yuan,M., He,J., Cai,L. and Leng,A.
  TITLE     The Impact of Non-alcohol Fatty Liver Disease on Bone Mineral
            Density is Mediated by Sclerostin by Mendelian Randomization Study
  JOURNAL   Calcif Tissue Int 114 (5), 502-512 (2024)
   PUBMED   38555554
  REMARK    GeneRIF: The Impact of Non-alcohol Fatty Liver Disease on Bone
            Mineral Density is Mediated by Sclerostin by Mendelian
            Randomization Study.
REFERENCE   4  (residues 1 to 213)
  AUTHORS   Alramah,T., Cherian,P., Al-Khairi,I., Abu-Farha,M., Thanaraj,T.A.,
            Albatineh,A.N., Safadi,F., Ali,H., Abdul-Ghani,M., Tuomilehto,J.,
            Koistinen,H.A., Al-Mulla,F. and Abubaker,J.
  TITLE     Evaluating the correlation of sclerostin levels with obesity and
            type 2 diabetes in a multiethnic population living in Kuwait
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392675 (2024)
   PUBMED   38711986
  REMARK    GeneRIF: Evaluating the correlation of sclerostin levels with
            obesity and type 2 diabetes in a multiethnic population living in
            Kuwait.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 213)
  AUTHORS   Jarjees,Z. and Sarhat,E.
  TITLE     ASSESSMENT OF OSTEOPONTIN, SCLEROSTIN, AND OSTEOCALCIN LEVELS IN
            PATIENTS WITH HYPOTHYROIDISM ON MEDICAL THERAPY
  JOURNAL   Georgian Med News (347), 131-135 (2024)
   PUBMED   38609129
  REMARK    GeneRIF: ASSESSMENT OF OSTEOPONTIN, SCLEROSTIN, AND OSTEOCALCIN
            LEVELS IN PATIENTS WITH HYPOTHYROIDISM ON MEDICAL THERAPY.
REFERENCE   6  (residues 1 to 213)
  AUTHORS   Staehling-Hampton,K., Proll,S., Paeper,B.W., Zhao,L., Charmley,P.,
            Brown,A., Gardner,J.C., Galas,D., Schatzman,R.C., Beighton,P.,
            Papapoulos,S., Hamersma,H. and Brunkow,M.E.
  TITLE     A 52-kb deletion in the SOST-MEOX1 intergenic region on 17q12-q21
            is associated with van Buchem disease in the Dutch population
  JOURNAL   Am J Med Genet 110 (2), 144-152 (2002)
   PUBMED   12116252
REFERENCE   7  (residues 1 to 213)
  AUTHORS   Balemans,W., Patel,N., Ebeling,M., Van Hul,E., Wuyts,W., Lacza,C.,
            Dioszegi,M., Dikkers,F.G., Hildering,P., Willems,P.J.,
            Verheij,J.B., Lindpaintner,K., Vickery,B., Foernzler,D. and Van
            Hul,W.
  TITLE     Identification of a 52 kb deletion downstream of the SOST gene in
            patients with van Buchem disease
  JOURNAL   J Med Genet 39 (2), 91-97 (2002)
   PUBMED   11836356
  REMARK    GeneRIF: A 52 kb deletion has been identified downstream of the
            SOST gene in patients with van Buchem disease.
REFERENCE   8  (residues 1 to 213)
  AUTHORS   Balemans,W., Ebeling,M., Patel,N., Van Hul,E., Olson,P.,
            Dioszegi,M., Lacza,C., Wuyts,W., Van Den Ende,J., Willems,P.,
            Paes-Alves,A.F., Hill,S., Bueno,M., Ramos,F.J., Tacconi,P.,
            Dikkers,F.G., Stratakis,C., Lindpaintner,K., Vickery,B.,
            Foernzler,D. and Van Hul,W.
  TITLE     Increased bone density in sclerosteosis is due to the deficiency of
            a novel secreted protein (SOST)
  JOURNAL   Hum Mol Genet 10 (5), 537-543 (2001)
   PUBMED   11181578
REFERENCE   9  (residues 1 to 213)
  AUTHORS   Brunkow,M.E., Gardner,J.C., Van Ness,J., Paeper,B.W.,
            Kovacevich,B.R., Proll,S., Skonier,J.E., Zhao,L., Sabo,P.J., Fu,Y.,
            Alisch,R.S., Gillett,L., Colbert,T., Tacconi,P., Galas,D.,
            Hamersma,H., Beighton,P. and Mulligan,J.
  TITLE     Bone dysplasia sclerosteosis results from loss of the SOST gene
            product, a novel cystine knot-containing protein
  JOURNAL   Am J Hum Genet 68 (3), 577-589 (2001)
   PUBMED   11179006
REFERENCE   10 (residues 1 to 213)
  AUTHORS   Appelman-Dijkstra,N., Van Lierop,A. and Papapoulos,S.
  TITLE     SOST-Related Sclerosing Bone Dysplasias
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36508511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055813.9 and AF326739.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Sclerostin is a secreted glycoprotein with a C-terminal
            cysteine knot-like (CTCK) domain and sequence similarity to the DAN
            (differential screening-selected gene aberrative in neuroblastoma)
            family of bone morphogenetic protein (BMP) antagonists.
            Loss-of-function mutations in this gene are associated with an
            autosomal-recessive disorder, sclerosteosis, which causes
            progressive bone overgrowth. A deletion downstream of this gene,
            which causes reduced sclerostin expression, is associated with a
            milder form of the disorder called van Buchem disease. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF331844.1, AF326739.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301691.3/ ENSP00000301691.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..213
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..213
                     /product="sclerostin precursor"
                     /calculated_mol_wt=21522
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2526
     mat_peptide     24..213
                     /product="sclerostin"
                     /calculated_mol_wt=21522
     Region          28..210
                     /region_name="GHB_like"
                     /note="Glycoprotein hormone beta chain homologues;
                     cl21545"
                     /db_xref="CDD:473907"
     Region          41..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQB4.1)"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BQB4.1)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9BQB4.1)"
     Region          178..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQB4.1)"
     CDS             1..213
                     /gene="SOST"
                     /gene_synonym="CDD; DAND6; SOST1; VBCH"
                     /coded_by="NM_025237.3:51..692"
                     /db_xref="CCDS:CCDS11468.1"
                     /db_xref="GeneID:50964"
                     /db_xref="HGNC:HGNC:13771"
                     /db_xref="MIM:605740"
ORIGIN      
        1 mqlplalclv cllvhtafrv vegqgwqafk ndateiipel geypepppel ennktmnrae
       61 nggrpphhpf etkdvseysc relhftryvt dgpcrsakpv telvcsgqcg parllpnaig
      121 rgkwwrpsgp dfrcipdryr aqrvqllcpg geaprarkvr lvasckckrl trfhnqselk
      181 dfgteaarpq kgrkprprar sakanqaele nay
//
LOCUS       NP_004577                740 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-3 isoform 1 [Homo sapiens].
ACCESSION   NP_004577 XP_944432 XP_949205
VERSION     NP_004577.1
DBSOURCE    REFSEQ: accession NM_004586.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Schaeffer,S., Gupta,B., Calatayud,A.L., Calderaro,J., Caruso,S.,
            Hirsch,T.Z., Pelletier,L., Zucman-Rossi,J. and Rebouissou,S.
  TITLE     RSK2 inactivation cooperates with AXIN1 inactivation or
            beta-catenin activation to promote hepatocarcinogenesis
  JOURNAL   J Hepatol 79 (3), 704-716 (2023)
   PUBMED   37201672
  REMARK    GeneRIF: RSK2 inactivation cooperates with AXIN1 inactivation or
            beta-catenin activation to promote hepatocarcinogenesis.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Pan,J., Liu,M., Duan,X. and Wang,D.
  TITLE     A short peptide LINC00665_18aa encoded by lncRNA LINC00665
            suppresses the proliferation and migration of osteosarcoma cells
            through the regulation of the CREB1/RPS6KA3 interaction
  JOURNAL   PLoS One 18 (6), e0286422 (2023)
   PUBMED   37285335
  REMARK    GeneRIF: A short peptide LINC00665_18aa encoded by lncRNA LINC00665
            suppresses the proliferation and migration of osteosarcoma cells
            through the regulation of the CREB1/RPS6KA3 interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Lopez,J., Bonsor,D.A., Sale,M.J., Urisman,A., Mehalko,J.L.,
            Cabanski-Dunning,M., Castel,P., Simanshu,D.K. and McCormick,F.
  TITLE     The ribosomal S6 kinase 2 (RSK2)-SPRED2 complex regulates the
            phosphorylation of RSK substrates and MAPK signaling
  JOURNAL   J Biol Chem 299 (6), 104789 (2023)
   PUBMED   37149146
  REMARK    GeneRIF: The ribosomal S6 kinase 2 (RSK2)-SPRED2 complex regulates
            the phosphorylation of RSK substrates and MAPK signaling.
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Zhao,Y., Bjorbaek,C., Weremowicz,S., Morton,C.C. and Moller,D.E.
  TITLE     RSK3 encodes a novel pp90rsk isoform with a unique N-terminal
            sequence: growth factor-stimulated kinase function and nuclear
            translocation
  JOURNAL   Mol Cell Biol 15 (8), 4353-4363 (1995)
   PUBMED   7623830
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Ku,N.O. and Omary,M.B.
  TITLE     Identification of the major physiologic phosphorylation site of
            human keratin 18: potential kinases and a role in filament
            reorganization
  JOURNAL   J Cell Biol 127 (1), 161-171 (1994)
   PUBMED   7523419
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Rogers,R.C. and Abidi,F.E.
  TITLE     RPS6KA3-Related Intellectual Disability
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301520
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807772.12, U08316.1,
            AB102662.1, BC015451.1, BU618685.1, W00439.1, AV684171.1,
            CK905714.1, CA843526.1, CA843287.1, AA317826.1, AL732366.7,
            BQ427696.1, AK022869.1 and AA858312.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_949205.1, XP_944432.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            non-identical kinase catalytic domains and phosphorylates various
            substrates, including members of the mitogen-activated kinase
            (MAPK) signalling pathway. The activity of this protein has been
            implicated in controlling cell growth and differentiation.
            Mutations in this gene have been associated with Coffin-Lowry
            syndrome (CLS). [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2687120.1, AK313932.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379565.9/ ENSP00000368884.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..740
                     /product="ribosomal protein S6 kinase alpha-3 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="insulin-stimulated protein kinase 1; ribosomal
                     protein S6 kinase alpha-3; RSK-2; p90-RSK 3; MAPKAPK-1b;
                     S6K-alpha-3; MAPKAP kinase 1b; ribosomal S6 kinase 2;
                     MAPK-activated protein kinase 1b; MAP kinase-activated
                     protein kinase 1b; ribosomal protein S6 kinase, 90kDa,
                     polypeptide 3; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=83605
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Region          72..388
                     /region_name="STKc_RSK_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, 90 kDa ribosomal protein S6 kinase; cd05582"
                     /db_xref="CDD:270734"
     Site            order(74..78,82,98,100,131,147..148,150,154,156,193,195,
                     197..198,200,210..211,214,228..233,260,266,269)
                     /site_type="active"
                     /db_xref="CDD:270734"
     Site            order(74..78,82,98,100,131,148..150,154,193,195,197..198,
                     200,210..211)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270734"
     Site            order(78,154,156,193,195,197,214,228..233,260,266,269)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270734"
     Site            order(210..221,223..233)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270734"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P18654, ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51812.1)"
     Site            369
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270734"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195;
                     propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Site            382..387
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270734"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis and MAPKAPK2.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Region          402..740
                     /region_name="STKc_RSK2_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal
                     protein S6 kinase 3 or Ribosomal protein S6 kinase
                     alpha-3); cd14176"
                     /db_xref="CDD:271078"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P51812.1)"
     Site            order(428..432,434,436,449,451,477,493..496,499..500,502,
                     538..539,541,543..544,546,560..561,564,579..583,585)
                     /site_type="active"
                     /db_xref="CDD:271078"
     Site            order(428..431,434,436,449,451,477,493..496,499..500,
                     543..544,546,560..561)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271078"
     Site            order(432,500,502,538..539,541,543,564,579..583,585)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271078"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FGFR3.
                     /evidence=ECO:0000250|UniProtKB:P18654; propagated from
                     UniProtKB/Swiss-Prot (P51812.1)"
     Site            556
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P51812.1)"
     Site            560..583
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271078"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51812.1)"
     CDS             1..740
                     /gene="RPS6KA3"
                     /gene_synonym="CLS; HU-3; ISPK-1; MAPKAPK1B; MRX19;
                     p90-RSK2; pp90RSK2; RSK; RSK2; S6K-alpha3; XLID19"
                     /coded_by="NM_004586.3:278..2500"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14197.1"
                     /db_xref="GeneID:6197"
                     /db_xref="HGNC:HGNC:10432"
                     /db_xref="MIM:300075"
ORIGIN      
        1 mplaqladpw qkmavespsd saengqqimd epmgeeeinp qteevsikei aithhvkegh
       61 ekadpsqfel lkvlgqgsfg kvflvkkisg sdarqlyamk vlkkatlkvr drvrtkmerd
      121 ilvevnhpfi vklhyafqte gklylildfl rggdlftrls kevmfteedv kfylaelala
      181 ldhlhslgii yrdlkpenil ldeeghiklt dfglskesid hekkaysfcg tveymapevv
      241 nrrghtqsad wwsfgvlmfe mltgtlpfqg kdrketmtmi lkaklgmpqf lspeaqsllr
      301 mlfkrnpanr lgagpdgvee ikrhsffsti dwnklyrrei hppfkpatgr pedtfyfdpe
      361 ftaktpkdsp gippsanahq lfrgfsfvai tsddesqamq tvgvhsivqq lhrnsiqftd
      421 gyevkedigv gsysvckrci hkatnmefav kiidkskrdp teeieillry gqhpniitlk
      481 dvyddgkyvy vvtelmkgge lldkilrqkf fsereasavl ftitktveyl haqgvvhrdl
      541 kpsnilyvde sgnpesiric dfgfakqlra engllmtpcy tanfvapevl krqgydaacd
      601 iwslgvllyt mltgytpfan gpddtpeeil arigsgkfsl sggywnsvsd takdlvskml
      661 hvdphqrlta alvlrhpwiv hwdqlpqyql nrqdaphlvk gamaatysal nrnqspvlep
      721 vgrstlaqrr gikkitstal
//
LOCUS       NP_001268382             291 aa            linear   PRI 20-NOV-2025
DEFINITION  methyl-CpG-binding domain protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001268382
VERSION     NP_001268382.1
DBSOURCE    REFSEQ: accession NM_001281453.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Leighton,G.O., Irvin,E.M., Kaur,P., Liu,M., You,C., Bhattaram,D.,
            Piehler,J., Riehn,R., Wang,H., Pan,H. and Williams,D.C. Jr.
  TITLE     Densely methylated DNA traps Methyl-CpG-binding domain protein 2
            but permits free diffusion by Methyl-CpG-binding domain protein 3
  JOURNAL   J Biol Chem 298 (10), 102428 (2022)
   PUBMED   36037972
  REMARK    GeneRIF: Densely methylated DNA traps Methyl-CpG-binding domain
            protein 2 but permits free diffusion by Methyl-CpG-binding domain
            protein 3.
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Yan,W., Han,Q., Gong,L., Zhan,X., Li,W., Guo,Z., Zhao,J., Li,T.,
            Bai,Z., Wu,J., Huang,Y., Lv,L., Zhao,H., Cai,H., Huang,S., Diao,X.,
            Chen,Y., Gong,W., Xia,Q., Man,J., Chen,L., Dai,G. and Zhou,T.
  TITLE     MBD3 promotes hepatocellular carcinoma progression and metastasis
            through negative regulation of tumour suppressor TFPI2
  JOURNAL   Br J Cancer 127 (4), 612-623 (2022)
   PUBMED   35501390
  REMARK    GeneRIF: MBD3 promotes hepatocellular carcinoma progression and
            metastasis through negative regulation of tumour suppressor TFPI2.
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Hendrich,B., Abbott,C., McQueen,H., Chambers,D., Cross,S. and
            Bird,A.
  TITLE     Genomic structure and chromosomal mapping of the murine and human
            Mbd1, Mbd2, Mbd3, and Mbd4 genes
  JOURNAL   Mamm Genome 10 (9), 906-912 (1999)
   PUBMED   10441743
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Hendrich,B. and Bird,A.
  TITLE     Identification and characterization of a family of mammalian
            methyl-CpG binding proteins
  JOURNAL   Mol Cell Biol 18 (11), 6538-6547 (1998)
   PUBMED   9774669
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Tong,J.K., Hassig,C.A., Schnitzler,G.R., Kingston,R.E. and
            Schreiber,S.L.
  TITLE     Chromatin deacetylation by an ATP-dependent nucleosome remodelling
            complex
  JOURNAL   Nature 395 (6705), 917-921 (1998)
   PUBMED   9804427
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Zhang,Y., LeRoy,G., Seelig,H.P., Lane,W.S. and Reinberg,D.
  TITLE     The dermatomyositis-specific autoantigen Mi2 is a component of a
            complex containing histone deacetylase and nucleosome remodeling
            activities
  JOURNAL   Cell 95 (2), 279-289 (1998)
   PUBMED   9790534
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005943.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: DNA methylation is the major modification of eukaryotic
            genomes and plays an essential role in mammalian development. This
            gene belongs to a family of nuclear proteins which are
            characterized by the presence of a methyl-CpG binding domain (MBD).
            The encoded protein is a subunit of the NuRD, a multisubunit
            complex containing nucleosome remodeling and histone deacetylase
            activities. Unlike the other family members, the encoded protein is
            not capable of binding to methylated DNA. The protein mediates the
            association of metastasis-associated protein 2 with the core
            histone deacetylase complex. Alternative splicing results in
            multiple transcript variants of this gene. [provided by RefSeq, Jul
            2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1880464.1, AF072247.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000434436.8/ ENSP00000412302.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..291
                     /product="methyl-CpG-binding domain protein 3 isoform 1"
                     /calculated_mol_wt=32713
     Region          1..80
                     /region_name="Required for interaction with MBD2.
                     /evidence=ECO:0000269|PubMed:15701600"
                     /note="propagated from UniProtKB/Swiss-Prot (O95983.1)"
     Region          5..79
                     /region_name="MeCP2_MBD"
                     /note="MeCP2, MBD1, MBD2, MBD3, and MBD4 are members of a
                     protein family that share the methyl-CpG-binding domain
                     (MBD). The MBD, consists of about 70 residues and is
                     defined as the minimal region required for binding to
                     methylated DNA by a methyl-CpG-binding...; cd01396"
                     /db_xref="CDD:238690"
     Site            order(18,20,22,30,32,41,44,48)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238690"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95983.1)"
     Region          60..80
                     /region_name="Required for interaction with MBD3L2.
                     /evidence=ECO:0000269|PubMed:15701600"
                     /note="propagated from UniProtKB/Swiss-Prot (O95983.1)"
     Region          82..148
                     /region_name="MBDa"
                     /note="p55-binding region of Methyl-CpG-binding domain
                     proteins MBD; pfam16564"
                     /db_xref="CDD:465179"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95983.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95983.1)"
     Region          152..243
                     /region_name="MBD_C"
                     /note="C-terminal domain of methyl-CpG binding protein 2
                     and 3; pfam14048"
                     /db_xref="CDD:464072"
     Region          254..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95983.1)"
     CDS             1..291
                     /gene="MBD3"
                     /coded_by="NM_001281453.2:235..1110"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12072.1"
                     /db_xref="GeneID:53615"
                     /db_xref="HGNC:HGNC:6918"
                     /db_xref="MIM:603573"
ORIGIN      
        1 merkrwecpa lpqgwereev prrsglsagh rdvfyyspsg kkfrskpqla rylggsmdls
       61 tfdfrtgkml mskmnksrqr vrydssnqvk gkpdlntalp vrqtasifkq pvtkitnhps
      121 nkvksdpqka vdqprqlfwe kklsglnafd iaeelvktmd lpkglqgvgp gctdetllsa
      181 iasalhtstm pitgqlsaav eknpgvwlnt tqplckafmv tdedirkqee lvqqvrkrle
      241 ealmadmlah veelardgea pldkacaedd deedeeeeee epdpdpemeh v
//
LOCUS       NP_001351407             354 aa            linear   PRI 20-NOV-2025
DEFINITION  spliceosome-associated protein CWC27 homolog isoform 5 [Homo
            sapiens].
ACCESSION   NP_001351407 XP_016864432
VERSION     NP_001351407.1
DBSOURCE    REFSEQ: accession NM_001364478.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Yassin,S.H., Henderson,R., Lenberg,J., Murillo,V., Murdock,D.R.,
            Friedman,J., Jones,M.C., Wigby,K. and Borooah,S.
  TITLE     Further delineation of the CWC27-associated spliceosomeopathy: Case
            report and review of the literature
  JOURNAL   Am J Med Genet A 191 (5), 1378-1383 (2023)
   PUBMED   36718996
  REMARK    GeneRIF: Further delineation of the CWC27-associated
            spliceosomeopathy: Case report and review of the literature.
            Review article
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Busetto,V., Barbosa,I., Basquin,J., Marquenet,E., Hocq,R.,
            Hennion,M., Paternina,J.A., Namane,A., Conti,E., Bensaude,O. and Le
            Hir,H.
  TITLE     Structural and functional insights into CWC27/CWC22 heterodimer
            linking the exon junction complex to spliceosomes
  JOURNAL   Nucleic Acids Res 48 (10), 5670-5683 (2020)
   PUBMED   32329775
  REMARK    GeneRIF: Structural and functional insights into CWC27/CWC22
            heterodimer linking the exon junction complex to spliceosomes.
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Wang,M., Li,Z., Chu,H., Lv,Q., Ye,D., Ding,Q., Xu,C., Guo,J.,
            Du,M., Chen,J., Song,Z., Yin,C., Qin,C., Gu,C., Zhu,Y., Xia,G.,
            Liu,F., Zhang,Z., Yuan,L., Fu,G., Hu,Z., Tong,N., Shen,J., Liu,K.,
            Sun,J., Sun,Y., Li,J., Li,X., Shen,H., Xu,J., Shi,Y. and Zhang,Z.
  TITLE     Genome-Wide Association Study of Bladder Cancer in a Chinese Cohort
            Reveals a New Susceptibility Locus at 5q12.3
  JOURNAL   Cancer Res 76 (11), 3277-3284 (2016)
   PUBMED   27206850
  REMARK    GeneRIF: CWC27 overexpression is associated with Bladder Cancer.
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Ulrich,A. and Wahl,M.C.
  TITLE     Structure and evolution of the spliceosomal peptidyl-prolyl
            cis-trans isomerase Cwc27
  JOURNAL   Acta Crystallogr D Biol Crystallogr 70 (Pt 12), 3110-3123 (2014)
   PUBMED   25478830
  REMARK    GeneRIF: The crystal structure of a relatively protease-resistant
            N-terminal fragment of human Cwc27 containing the cyclophilin-type
            peptidyl-prolyl cis-trans isomerase domain was determined at 2.0 A
            resolution.
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Davis,T.L., Walker,J.R., Campagna-Slater,V., Finerty,P.J.,
            Paramanathan,R., Bernstein,G., MacKenzie,F., Tempel,W., Ouyang,H.,
            Lee,W.H., Eisenmesser,E.Z. and Dhe-Paganon,S.
  TITLE     Structural and biochemical characterization of the human
            cyclophilin family of peptidyl-prolyl isomerases
  JOURNAL   PLoS Biol 8 (7), e1000439 (2010)
   PUBMED   20676357
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Fabrizio,P., Dannenberg,J., Dube,P., Kastner,B., Stark,H.,
            Urlaub,H. and Luhrmann,R.
  TITLE     The evolutionarily conserved core design of the catalytic
            activation step of the yeast spliceosome
  JOURNAL   Mol Cell 36 (4), 593-608 (2009)
   PUBMED   19941820
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008898.6 and AC109465.3.
            
            On Jun 20, 2018 this sequence version replaced XP_016864432.1.
            
            Transcript Variant: This variant (5) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (5)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.182453.1,
                                           SRR1803612.397737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..354
                     /product="spliceosome-associated protein CWC27 homolog
                     isoform 5"
                     /EC_number="5.2.1.8"
                     /note="serologically defined colon cancer antigen 10;
                     peptidyl-prolyl cis-trans isomerase SDCCAG10;
                     peptidyl-prolyl cis-trans isomerase CWC27 homolog; PPIase
                     SDCCAG10; antigen NY-CO-10; PPIase CWC27; probable
                     inactive peptidyl-prolyl cis-trans isomerase CWC27
                     homolog; spliceosome-associated protein CWC27 homolog;
                     CWC27 spliceosome associated protein homolog"
                     /calculated_mol_wt=39608
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          8..178
                     /region_name="cyclophilin_CeCYP16-like"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerase) (PPIase) domain similar to Caenorhabditis
                     elegans cyclophilin 16. C. elegans CeCYP-16, compared to
                     the archetypal cyclophilin Human cyclophilin A has, a
                     reduced peptidylprolyl cis- trans isomerase...; cd01925"
                     /db_xref="CDD:238906"
     Site            order(55..56,61,112,114,122)
                     /site_type="active"
                     /db_xref="CDD:238906"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Site            201
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     Region          <239..348
                     /region_name="NOP7"
                     /note="Protein required for biogenesis of the 60S
                     ribosomal subunit [Translation, ribosomal structure and
                     biogenesis]; COG5163"
                     /db_xref="CDD:227492"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5XIB2; propagated from
                     UniProtKB/Swiss-Prot (Q6UX04.1)"
     CDS             1..354
                     /gene="CWC27"
                     /gene_synonym="NY-CO-10; RPSKA; SDCCAG-10; SDCCAG10"
                     /coded_by="NM_001364478.1:218..1282"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS93719.1"
                     /db_xref="GeneID:10283"
                     /db_xref="HGNC:HGNC:10664"
                     /db_xref="MIM:617170"
ORIGIN      
        1 msniyiqepp tngkvllktt agdidielws keapkacrnf iqlcleayyd ntifhrvvpg
       61 fivqggdptg tgsggesiyg apfkdefhsr lrfnrrglva managshdng sqffftlgra
      121 delnnkhtif gkvtgdtvyn mlrlsevdid dderphnphk ikscevlfnp fddiipreik
      181 rlkkekpeee vkklkpkgtk nfsllsfgee aeeeeeevnr vsqsmkgksk sshdllkddp
      241 hlssvpvves ekgdapdlvd dgedesaehd eyidgdeknl mreriakklk kdtsanvksa
      301 gegevekksv srseelrkea rqlkrellaa kqkkvenaak qaekrsedgi spcc
//
LOCUS       NP_001265570             150 aa            linear   PRI 20-NOV-2025
DEFINITION  ran-specific GTPase-activating protein isoform 4 [Homo sapiens].
ACCESSION   NP_001265570
VERSION     NP_001265570.1
DBSOURCE    REFSEQ: accession NM_001278641.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Kodiha,M., Azad,N., Chu,S., Crampton,N. and Stochaj,U.
  TITLE     Oxidative stress and signaling through EGFR and PKA pathways
            converge on the nuclear transport factor RanBP1
  JOURNAL   Eur J Cell Biol 103 (1), 151376 (2024)
   PUBMED   38011756
  REMARK    GeneRIF: Oxidative stress and signaling through EGFR and PKA
            pathways converge on the nuclear transport factor RanBP1.
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Kahm,Y.J., Kim,I.G. and Kim,R.K.
  TITLE     RanBP1: A Potential Therapeutic Target for Cancer Stem Cells in
            Lung Cancer and Glioma
  JOURNAL   Int J Mol Sci 24 (7), 6855 (2023)
   PUBMED   37047826
  REMARK    GeneRIF: RanBP1: A Potential Therapeutic Target for Cancer Stem
            Cells in Lung Cancer and Glioma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Nan,G., Zhao,S.H., Wang,T., Chao,D., Tian,R.F., Wang,W.J., Fu,X.,
            Lin,P., Guo,T., Wang,B., Sun,X.X., Chen,X., Chen,Z.N., Wang,S.J.
            and Cui,H.Y.
  TITLE     CD147 supports paclitaxel resistance via interacting with RanBP1
  JOURNAL   Oncogene 41 (7), 983-996 (2022)
   PUBMED   34974521
  REMARK    GeneRIF: CD147 supports paclitaxel resistance via interacting with
            RanBP1.
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Chi,N.C., Adam,E.J. and Adam,S.A.
  TITLE     Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear
            import factor p97
  JOURNAL   J Biol Chem 272 (10), 6818-6822 (1997)
   PUBMED   9045717
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Chi,N.C., Adam,E.J., Visser,G.D. and Adam,S.A.
  TITLE     RanBP1 stabilizes the interaction of Ran with p97 nuclear protein
            import
  JOURNAL   J Cell Biol 135 (3), 559-569 (1996)
   PUBMED   8909533
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Hayashi,N., Yokoyama,N., Seki,T., Azuma,Y., Ohba,T. and
            Nishimoto,T.
  TITLE     RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
            RCC1 via Ran/TC4
  JOURNAL   Mol Gen Genet 247 (6), 661-669 (1995)
   PUBMED   7616957
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Ren,M., Villamarin,A., Shih,A., Coutavas,E., Moore,M.S.,
            LoCurcio,M., Clarke,V., Oppenheim,J.D., D'Eustachio,P. and
            Rush,M.G.
  TITLE     Separate domains of the Ran GTPase interact with different factors
            to regulate nuclear protein import and RNA processing
  JOURNAL   Mol Cell Biol 15 (4), 2117-2124 (1995)
   PUBMED   7891706
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Bischoff,F.R., Krebber,H., Smirnova,E., Dong,W. and Ponstingl,H.
  TITLE     Co-activation of RanGTPase and inhibition of GTP dissociation by
            Ran-GTP binding protein RanBP1
  JOURNAL   EMBO J 14 (4), 705-715 (1995)
   PUBMED   7882974
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Coutavas,E., Ren,M., Oppenheim,J.D., D'Eustachio,P. and Rush,M.G.
  TITLE     Characterization of proteins that interact with the cell-cycle
            regulatory protein Ran/TC4
  JOURNAL   Nature 366 (6455), 585-587 (1993)
   PUBMED   8255297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006547.9, BI916757.1,
            BG717186.1, AW404614.1 and HY229989.1.
            
            Summary: This gene encodes a protein that forms a complex with
            Ras-related nuclear protein (Ran) and metabolizes guanoside
            triphosphate (GTP). This complex participates in the regulation of
            the cell cycle by controlling transport of proteins and nucleic
            acids into the nucleus. There are multiple pseudogenes for this
            gene on chromosomes 9, 12, 17, and X. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (4) contains multiple differences,
            compared to variant 1. It initiates translation at a downstream
            in-frame start codon. The encoded isoform (4) is shorter and has a
            distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1066923.1,
                                           SRR3476690.674704.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..150
                     /product="ran-specific GTPase-activating protein isoform
                     4"
                     /note="ran-specific GTPase-activating protein; HpaII tiny
                     fragments locus 9A; testis secretory sperm-binding protein
                     Li 221n"
                     /calculated_mol_wt=17355
     Region          1..110
                     /region_name="RanBD_RanBP1"
                     /note="Ran-binding domain; cd13179"
                     /db_xref="CDD:270000"
     Site            order(4,6,8,17..20,37,39,41..42,44..48,51..53,61..64,71,
                     73,78,81,83,87,91)
                     /site_type="other"
                     /note="Ran#RanBP1#RanGAP complex [polypeptide binding]"
                     /db_xref="CDD:270000"
     Site            order(6,8,15..20,24,35,37,39,41..48,51..53,61..64,67..69,
                     71,73,78,85,87,89,91)
                     /site_type="other"
                     /note="CRM1-RanBP1-RanGTP complex [polypeptide binding]"
                     /db_xref="CDD:270000"
     CDS             1..150
                     /gene="RANBP1"
                     /gene_synonym="HTF9A"
                     /coded_by="NM_001278641.2:705..1157"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5902"
                     /db_xref="HGNC:HGNC:9847"
                     /db_xref="MIM:601180"
ORIGIN      
        1 mraklfrfas endlpewker gtgdvkllkh kekgairllm rrdktlkica nhyitpmmel
       61 kpnagsdraw vwnthadfad ecpkpellai rflnaenaqk fktkfeecrk eieerekkgs
      121 gkndhaekva eklealsvke etkedaeekq
//
LOCUS       NP_789788                136 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial [Homo
            sapiens].
ACCESSION   NP_789788 XP_495934
VERSION     NP_789788.1
DBSOURCE    REFSEQ: accession NM_176818.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Echevarria,L., Clemente,P., Hernandez-Sierra,R., Gallardo,M.E.,
            Fernandez-Moreno,M.A. and Garesse,R.
  TITLE     Glutamyl-tRNAGln amidotransferase is essential for mammalian
            mitochondrial translation in vivo
  JOURNAL   Biochem J 460 (1), 91-101 (2014)
   PUBMED   24579914
  REMARK    GeneRIF: The mitochondrial defective phenotype provoked by the
            absence of gatA in human cells is confirmed by means of a deficient
            ability to grow when galactose is used as a carbon source.
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Nagao,A., Suzuki,T., Katoh,T., Sakaguchi,Y. and Suzuki,T.
  TITLE     Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
  JOURNAL   Proc Natl Acad Sci U S A 106 (38), 16209-16214 (2009)
   PUBMED   19805282
  REMARK    GeneRIF: Studies showed in vitro Gln-tRNA(Gln) formation catalyzed
            by the recombinant mtGluRS and hGatCAB.
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Scherer,S.E., Muzny,D.M., Buhay,C.J., Chen,R., Cree,A., Ding,Y.,
            Dugan-Rocha,S., Gill,R., Gunaratne,P., Harris,R.A., Hawes,A.C.,
            Hernandez,J., Hodgson,A.V., Hume,J., Jackson,A., Khan,Z.M.,
            Kovar-Smith,C., Lewis,L.R., Lozado,R.J., Metzker,M.L.,
            Milosavljevic,A., Miner,G.R., Montgomery,K.T., Morgan,M.B.,
            Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z., Steffen,D.,
            Lovering,R.C., Wheeler,D.A., Worley,K.C., Yuan,Y., Zhang,Z.,
            Adams,C.Q., Ansari-Lari,M.A., Ayele,M., Brown,M.J., Chen,G.,
            Chen,Z., Clerc-Blankenburg,K.P., Davis,C., Delgado,O., Dinh,H.H.,
            Draper,H., Gonzalez-Garay,M.L., Havlak,P., Jackson,L.R.,
            Jacob,L.S., Kelly,S.H., Li,L., Li,Z., Liu,J., Liu,W., Lu,J.,
            Maheshwari,M., Nguyen,B.V., Okwuonu,G.O., Pasternak,S., Perez,L.M.,
            Plopper,F.J., Santibanez,J., Shen,H., Tabor,P.E., Verduzco,D.,
            Waldron,L., Wang,Q., Williams,G.A., Zhang,J., Zhou,J., Allen,C.C.,
            Amin,A.G., Anyalebechi,V., Bailey,M., Barbaria,J.A., Bimage,K.E.,
            Bryant,N.P., Burch,P.E., Burkett,C.E., Burrell,K.L., Calderon,E.,
            Cardenas,V., Carter,K., Casias,K., Cavazos,I., Cavazos,S.R.,
            Ceasar,H., Chacko,J., Chan,S.N., Chavez,D., Christopoulos,C.,
            Chu,J., Cockrell,R., Cox,C.D., Dang,M., Dathorne,S.R., David,R.,
            Davis,C.M., Davy-Carroll,L., Deshazo,D.R., Donlin,J.E., D'Souza,L.,
            Eaves,K.A., Simons,R., Emery-Cohen,A.J., Escotto,M., Flagg,N.,
            Forbes,L.D., Gabisi,A.M., Garza,M., Hamilton,C., Henderson,N.,
            Hernandez,O., Hines,S., Hogues,M.E., Huang,M., Idlebird,D.G.,
            Johnson,R., Jolivet,A., Jones,S., Kagan,R., King,L.M., Leal,B.,
            Lebow,H., Lee,S., LeVan,J.M., Lewis,L.C., London,P.,
            Lorensuhewa,L.M., Loulseged,H., Lovett,D.A., Lucier,A.,
            Lucier,R.L., Ma,J., Madu,R.C., Mapua,P., Martindale,A.D.,
            Martinez,E., Massey,E., Mawhiney,S., Meador,M.G., Mendez,S.,
            Mercado,C., Mercado,I.C., Merritt,C.E., Miner,Z.L., Minja,E.,
            Mitchell,T., Mohabbat,F., Mohabbat,K., Montgomery,B., Moore,N.,
            Morris,S., Munidasa,M., Ngo,R.N., Nguyen,N.B., Nickerson,E.,
            Nwaokelemeh,O.O., Nwokenkwo,S., Obregon,M., Oguh,M., Oragunye,N.,
            Oviedo,R.J., Parish,B.J., Parker,D.N., Parrish,J., Parks,K.L.,
            Paul,H.A., Payton,B.A., Perez,A., Perrin,W., Pickens,A.,
            Primus,E.L., Pu,L.L., Puazo,M., Quiles,M.M., Quiroz,J.B.,
            Rabata,D., Reeves,K., Ruiz,S.J., Shao,H., Sisson,I., Sonaike,T.,
            Sorelle,R.P., Sutton,A.E., Svatek,A.F., Svetz,L.A., Tamerisa,K.S.,
            Taylor,T.R., Teague,B., Thomas,N., Thorn,R.D., Trejos,Z.Y.,
            Trevino,B.K., Ukegbu,O.N., Urban,J.B., Vasquez,L.I., Vera,V.A.,
            Villasana,D.M., Wang,L., Ward-Moore,S., Warren,J.T., Wei,X.,
            White,F., Williamson,A.L., Wleczyk,R., Wooden,H.S., Wooden,S.H.,
            Yen,J., Yoon,L., Yoon,V., Zorrilla,S.E., Nelson,D.,
            Kucherlapati,R., Weinstock,G. and Gibbs,R.A.
  CONSRTM   Baylor College of Medicine Human Genome Sequencing Center Sequence
            Production Team
  TITLE     The finished DNA sequence of human chromosome 12
  JOURNAL   Nature 440 (7082), 346-351 (2006)
   PUBMED   16541075
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL021546.1 and BC107145.1.
            
            On Aug 30, 2004 this sequence version replaced XP_495934.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094319.1, SRR1660809.103286.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000551765.6/ ENSP00000446872.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..136
                     /product="glutamyl-tRNA(Gln) amidotransferase subunit C,
                     mitochondrial"
                     /note="glu-AdT subunit C; glutamyl-tRNA(Gln)
                     amidotransferase, subunit C homolog"
                     /calculated_mol_wt=14955
     Region          31..118
                     /region_name="gatC"
                     /note="Asp-tRNA(Asn)/Glu-tRNA(Gln) amidotransferase
                     subunit GatC; PRK00034"
                     /db_xref="CDD:178810"
     CDS             1..136
                     /gene="GATC"
                     /gene_synonym="15E1.2; COXPD42"
                     /coded_by="NM_176818.3:38..448"
                     /db_xref="CCDS:CCDS31911.1"
                     /db_xref="GeneID:283459"
                     /db_xref="HGNC:HGNC:25068"
                     /db_xref="MIM:617210"
ORIGIN      
        1 mwsrlvwlgl raplggrqgf tskadpqgsg ritaaviehl erlalvdfgs reavarleka
       61 iafadrlrav dtdgvepmes vledrclylr sdnvvegnca dellqnshrv veeyfvappg
      121 nislpkldeq epfphs
//
LOCUS       NP_112202                129 aa            linear   PRI 20-NOV-2025
DEFINITION  iron-sulfur cluster assembly 1 homolog, mitochondrial precursor
            [Homo sapiens].
ACCESSION   NP_112202
VERSION     NP_112202.2
DBSOURCE    REFSEQ: accession NM_030940.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Du,J., Huang,Z., Li,Y., Ren,X., Zhou,C., Liu,R., Zhang,P., Lei,G.,
            Lyu,J., Li,J. and Tan,G.
  TITLE     Copper exerts cytotoxicity through inhibition of iron-sulfur
            cluster biogenesis on ISCA1/ISCA2/ISCU assembly proteins
  JOURNAL   Free Radic Biol Med 204, 359-373 (2023)
   PUBMED   37225108
  REMARK    GeneRIF: Copper exerts cytotoxicity through inhibition of
            iron-sulfur cluster biogenesis on ISCA1/ISCA2/ISCU assembly
            proteins.
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Zhou,R., Peng,N. and Li,W.
  TITLE     Identification of ISCA1 as novel immunological and prognostic
            biomarker for bladder cancer
  JOURNAL   Front Immunol 13, 975503 (2022)
   PUBMED   36072584
  REMARK    GeneRIF: Identification of ISCA1 as novel immunological and
            prognostic biomarker for bladder cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Song,D., Tu,Z. and Lee,F.S.
  TITLE     Human ISCA1 interacts with IOP1/NARFL and functions in both
            cytosolic and mitochondrial iron-sulfur protein biogenesis
  JOURNAL   J Biol Chem 284 (51), 35297-35307 (2009)
   PUBMED   19864422
  REMARK    GeneRIF: human IscA1 plays an important role in both mitochondrial
            and cytosolic iron-sulfur cluster biogenesis, and a notable
            component of the latter is the interaction between IscA1 and IOP1.
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Nilsson,R., Schultz,I.J., Pierce,E.L., Soltis,K.A.,
            Naranuntarat,A., Ward,D.M., Baughman,J.M., Paradkar,P.N.,
            Kingsley,P.D., Culotta,V.C., Kaplan,J., Palis,J., Paw,B.H. and
            Mootha,V.K.
  TITLE     Discovery of genes essential for heme biosynthesis through
            large-scale gene expression analysis
  JOURNAL   Cell Metab 10 (2), 119-130 (2009)
   PUBMED   19656490
  REMARK    GeneRIF: Required for functional heme biosynthesis in erythroid
            cells.
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Cozar-Castellano,I., del Valle Machargo,M., Trujillo,E.,
            Arteaga,M.F., Gonzalez,T., Martin-Vasallo,P. and Avila,J.
  TITLE     hIscA: a protein implicated in the biogenesis of iron-sulfur
            clusters
  JOURNAL   Biochim Biophys Acta 1700 (2), 179-188 (2004)
   PUBMED   15262227
  REMARK    GeneRIF: screening a human brain cDNA expression library with serum
            from a patient suffering from the autoimmune Sjogren's syndrome
            yielded a gene product called hIscA implicated in iron-sulfur
            cluster biogenesis
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Shukla,A., Narayanan,D.L., Kaur,P. and Girisha,K.M.
  TITLE     ISCA1-Related Multiple Mitochondrial Dysfunctions Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31580634
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG772866.1, BC002675.2, BC071621.1, AI436792.1 and AA745613.1.
            
            On Sep 22, 2004 this sequence version replaced NP_112202.1.
            
            Summary: ISCA1 is a mitochondrial protein involved in the
            biogenesis and assembly of iron-sulfur clusters, which play a role
            in electron-transfer reactions (Cozar-Castellano et al., 2004
            [PubMed 15262227]).[supplied by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225937.1, SRR3476690.915749.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000375991.9/
                                                  ENSP00000365159.4
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..129
                     /product="iron-sulfur cluster assembly 1 homolog,
                     mitochondrial precursor"
                     /EC_number="2.7.7.52"
                     /note="HESB like domain containing 2; iron-sulfur cluster
                     assembly 1 homolog, mitochondrial; HESB-like
                     domain-containing protein 2; iron-sulfur assembly protein
                     IscA"
                     /calculated_mol_wt=12936
     transit_peptide 1..12
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BUE6.1)"
                     /calculated_mol_wt=1262
     mat_peptide     13..129
                     /product="Iron-sulfur cluster assembly 1 homolog,
                     mitochondrial. /id=PRO_0000042734"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUE6.1)"
                     /calculated_mol_wt=12936
     Region          24..129
                     /region_name="IscA"
                     /note="Fe-S cluster assembly iron-binding protein IscA
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG0316"
                     /db_xref="CDD:440085"
     CDS             1..129
                     /gene="ISCA1"
                     /gene_synonym="HBLD2; hIscA; hIscA1; ISA1; MMDS5"
                     /coded_by="NM_030940.4:81..470"
                     /db_xref="CCDS:CCDS35056.1"
                     /db_xref="GeneID:81689"
                     /db_xref="HGNC:HGNC:28660"
                     /db_xref="MIM:611006"
ORIGIN      
        1 msaslvratv ravskrklqp traaltltps avnkikqllk dkpehvgvkv gvrtrgcngl
       61 sytleytktk gdsdeeviqd gvrvfiekka qltllgtemd yvedklssef vfnnpnikgt
      121 cgcgesfni
//
LOCUS       NP_001350489             721 aa            linear   PRI 20-NOV-2025
DEFINITION  ras and Rab interactor 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001350489 XP_011543702
VERSION     NP_001350489.1
DBSOURCE    REFSEQ: accession NM_001363560.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Osei Saahene,R., Barnes,P., Yeboah,F.A., Agbo,E., Asante,D.B. and
            Arhin,S.K.
  TITLE     Expression of RAS and RAB interactor 1 (RIN1) in head and neck
            tumors at selected hospital in Ghana
  JOURNAL   PLoS One 19 (4), e0301295 (2024)
   PUBMED   38635569
  REMARK    GeneRIF: Expression of RAS and RAB interactor 1 (RIN1) in head and
            neck tumors at selected hospital in Ghana.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Afar,D.E., Han,L., McLaughlin,J., Wong,S., Dhaka,A., Parmar,K.,
            Rosenberg,N., Witte,O.N. and Colicelli,J.
  TITLE     Regulation of the oncogenic activity of BCR-ABL by a tightly bound
            substrate protein RIN1
  JOURNAL   Immunity 6 (6), 773-782 (1997)
   PUBMED   9208849
REFERENCE   7  (residues 1 to 721)
  AUTHORS   Han,L., Wong,D., Dhaka,A., Afar,D., White,M., Xie,W., Herschman,H.,
            Witte,O. and Colicelli,J.
  TITLE     Protein binding and signaling properties of RIN1 suggest a unique
            effector function
  JOURNAL   Proc Natl Acad Sci U S A 94 (10), 4954-4959 (1997)
   PUBMED   9144171
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Han,L. and Colicelli,J.
  TITLE     A human protein selected for interference with Ras function
            interacts directly with Ras and competes with Raf1
  JOURNAL   Mol Cell Biol 15 (3), 1318-1323 (1995)
   PUBMED   7862125
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Colicelli,J., Nicolette,C., Birchmeier,C., Rodgers,L., Riggs,M. and
            Wigler,M.
  TITLE     Expression of three mammalian cDNAs that interfere with RAS
            function in Saccharomyces cerevisiae
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2913-2917 (1991)
   PUBMED   1849280
REFERENCE   10 (residues 1 to 721)
  AUTHORS   Trowbridge,I.S., Lesley,J., Trotter,J. and Hyman,R.
  TITLE     Thymocyte subpopulation enriched for progenitors with an
            unrearranged T-cell receptor beta-chain gene
  JOURNAL   Nature 315 (6021), 666-669 (1985)
   PUBMED   3874369
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001107.5.
            
            On May 24, 2018 this sequence version replaced XP_011543702.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KU178482.1, DRR138507.19879.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..721
                     /product="ras and Rab interactor 1 isoform 3"
                     /note="ras inhibitor 1; ras inhibitor RIN1; ras inhibitor
                     JC99; ras interaction/interference protein 1"
                     /calculated_mol_wt=77369
     Region          58..158
                     /region_name="SH2_RIN1"
                     /note="Src homology 2 (SH2) domain found in Ras and Rab
                     interactor 1 (RIN1)-like proteins; cd10393"
                     /db_xref="CDD:198256"
     Site            order(76,94,119,121)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198256"
     Site            order(120,148)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198256"
     Region          429..545
                     /region_name="VPS9"
                     /note="Domain present in VPS9; smart00167"
                     /db_xref="CDD:128469"
     Region          563..643
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     CDS             1..721
                     /gene="RIN1"
                     /coded_by="NM_001363560.2:33..2198"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9610"
                     /db_xref="HGNC:HGNC:18749"
                     /db_xref="MIM:605965"
ORIGIN      
        1 mespgesgag spgapspssf ttghlarekp aqdplydvpn asggqaggpq rpgrvvslre
       61 rllltrpvwl qlqanaaaal hmlrteppgt flvrksntrq cqalcmrlpe asgpsfvssh
      121 yilespggvs legselmfpd lvqlicaych trdilllplq lpraihhaat hkeleaishl
      181 giefwsssln ikaqrgpagg pvlpqlkars pqeldqgtga alcffnplfp gdlgptkrek
      241 fkrsfkvrvs tetssplspp avppppvpvl pgavpsqter lppcqllrre ssvgyrvpag
      301 sgpslppmps lqevdcgsps sseeegvpgs rgspatsphl grrrpllrsm saafcsllap
      361 erqvgraaaa lmqdrhtaag qlvqdlltqv ragpepqelq girqalsrar amlsaelgpe
      421 kllspkrlel eqvrqkllql lrtyspsaqv krllqackll ymalrtqege gagadeflpl
      481 lslvlahcdl pellleaeym sellepsllt geggyyltsl saslallsgl gqahtlplsp
      541 vqelrrslsl weqrrlpath cfqhllrvay qdpssgctsk tlavppeasi atlnqlcatk
      601 frvtqpntfg lflykeqgyh rlppgalahr lpttgylvyr raewpetqga vteeegsgqs
      661 earsrgeeqg cqgdgdagvk asprdireqs ettaeggqgq aqegpaqpge peaegsraae
      721 e
//
LOCUS       NP_001308736             722 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform j [Homo sapiens].
ACCESSION   NP_001308736
VERSION     NP_001308736.1
DBSOURCE    REFSEQ: accession NM_001321807.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 14 and 15 encode the same isoform (j).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.136685.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..722
                     /product="E3 ubiquitin-protein ligase CBL-B isoform j"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=79175
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          671..711
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(673..674,676..678,680..681,686,690)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..722
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321807.2:1216..3384"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikctgpl anslsektrd pveedddeyk ipsshpvsln sqpshchnvk ppvrscdngh
      481 cmlngthgps sekksnipdl siylkgdvfd sasdpvplpp arpptrdnpk hgsslnrtps
      541 dydllipplg edafdalpps lpppppparh sliehskppg sssrpssgqd lfllpsdpfv
      601 dlasgqvplp parrlpgenv ktnrtsqdyd qlpscsdgsq aparppkprp rrtapeihhr
      661 kphgpeaale nvdakiaklm gegyafeevk raleiaqnnv evarsilref afpppvsprl
      721 nl
//
LOCUS       NP_000631                380 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-13 receptor subunit alpha-2 precursor [Homo sapiens].
ACCESSION   NP_000631
VERSION     NP_000631.1
DBSOURCE    REFSEQ: accession NM_000640.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Xu,W., Chao,R., Xie,X., Mao,Y., Chen,X., Chen,X. and Zhang,S.
  TITLE     IL13Ralpha2 as a crucial receptor for Chi3l1 in osteoclast
            differentiation and bone resorption through the MAPK/AKT pathway
  JOURNAL   Cell Commun Signal 22 (1), 81 (2024)
   PUBMED   38291404
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Chao,H., Zheng,L., Hsu,P., He,J., Wu,R., Xu,S., Zeng,R., Zhou,Y.,
            Ma,H., Liu,H. and Tang,Q.
  TITLE     IL-13RA2 downregulation in fibroblasts promotes keloid fibrosis via
            JAK/STAT6 activation
  JOURNAL   JCI Insight 8 (6), e157091 (2023)
   PUBMED   36757802
  REMARK    GeneRIF: IL-13RA2 downregulation in fibroblasts promotes keloid
            fibrosis via JAK/STAT6 activation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Nagai,T., Terada,N., Fujii,M., Nagata,Y., Nakahara,K., Mukai,S.,
            Okasho,K., Kamiyama,Y., Akamatsu,S., Kobayashi,T., Iida,K.,
            Denawa,M., Hagiwara,M., Inoue,T., Ogawa,O. and Kamoto,T.
  TITLE     Identification of the alpha2 chain of interleukin-13 receptor as a
            potential biomarker for predicting castration resistance of
            prostate cancer using patient-derived xenograft models
  JOURNAL   Cancer Rep (Hoboken) 6 (2), e1701 (2023)
   PUBMED   36806727
  REMARK    GeneRIF: Identification of the alpha2 chain of interleukin-13
            receptor as a potential biomarker for predicting castration
            resistance of prostate cancer using patient-derived xenograft
            models.
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Knudson,K.M., Hwang,S., McCann,M.S., Joshi,B.H., Husain,S.R. and
            Puri,R.K.
  TITLE     Recent Advances in IL-13Ralpha2-Directed Cancer Immunotherapy
  JOURNAL   Front Immunol 13, 878365 (2022)
   PUBMED   35464460
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Marquez-Ortiz,R.A., Contreras-Zarate,M.J., Tesic,V.,
            Alvarez-Eraso,K.L.F., Kwak,G., Littrell,Z., Costello,J.C.,
            Sreekanth,V., Ormond,D.R., Karam,S.D., Kabos,P. and Cittelly,D.M.
  TITLE     IL13Ralpha2 Promotes Proliferation and Outgrowth of Breast Cancer
            Brain Metastases
  JOURNAL   Clin Cancer Res 27 (22), 6209-6221 (2021)
   PUBMED   34544797
  REMARK    GeneRIF: IL13Ralpha2 Promotes Proliferation and Outgrowth of Breast
            Cancer Brain Metastases.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Donaldson,D.D., Whitters,M.J., Fitz,L.J., Neben,T.Y., Finnerty,H.,
            Henderson,S.L., O'Hara,R.M. Jr., Beier,D.R., Turner,K.J., Wood,C.R.
            and Collins,M.
  TITLE     The murine IL-13 receptor alpha 2: molecular cloning,
            characterization, and comparison with murine IL-13 receptor alpha 1
  JOURNAL   J Immunol 161 (5), 2317-2324 (1998)
   PUBMED   9725226
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Guo,J., Apiou,F., Mellerin,M.P., Lebeau,B., Jacques,Y. and
            Minvielle,S.
  TITLE     Chromosome mapping and expression of the human interleukin-13
            receptor
  JOURNAL   Genomics 42 (1), 141-145 (1997)
   PUBMED   9177784
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Zhang,J.G., Hilton,D.J., Willson,T.A., McFarlane,C., Roberts,B.A.,
            Moritz,R.L., Simpson,R.J., Alexander,W.S., Metcalf,D. and
            Nicola,N.A.
  TITLE     Identification, purification, and characterization of a soluble
            interleukin (IL)-13-binding protein. Evidence that it is distinct
            from the cloned Il-13 receptor and Il-4 receptor alpha-chains
  JOURNAL   J Biol Chem 272 (14), 9474-9480 (1997)
   PUBMED   9083087
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Gauchat,J.F., Schlagenhauf,E., Feng,N.P., Moser,R., Yamage,M.,
            Jeannin,P., Alouani,S., Elson,G., Notarangelo,L.D., Wells,T.,
            Eugster,H.P. and Bonnefoy,J.Y.
  TITLE     A novel 4-kb interleukin-13 receptor alpha mRNA expressed in human
            B, T, and endothelial cells encoding an alternate type-II
            interleukin-4/interleukin-13 receptor
  JOURNAL   Eur J Immunol 27 (4), 971-978 (1997)
   PUBMED   9130652
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Caput,D., Laurent,P., Kaghad,M., Lelias,J.M., Lefort,S., Vita,N.
            and Ferrara,P.
  TITLE     Cloning and characterization of a specific interleukin (IL)-13
            binding protein structurally related to the IL-5 receptor alpha
            chain
  JOURNAL   J Biol Chem 271 (28), 16921-16926 (1996)
   PUBMED   8663118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y08768.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is closely related to
            Il13RA1, a subuint of the interleukin 13 receptor complex. This
            protein binds IL13 with high affinity, but lacks cytoplasmic
            domain, and does not appear to function as a signal mediator. It is
            reported to play a role in the internalization of IL13. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291957.1, Y08768.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000243213.2/ ENSP00000243213.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..380
                     /product="interleukin-13 receptor subunit alpha-2
                     precursor"
                     /note="cancer/testis antigen 19; interleukin 13 binding
                     protein; interleukin 13 receptor alpha 2 chain; IL-13RA2;
                     IL-13R-alpha-2; IL-13R subunit alpha-2; IL-13 receptor
                     subunit alpha-2; interleukin 13 receptor, alpha 2"
                     /calculated_mol_wt=41457
     sig_peptide     1..26
                     /calculated_mol_wt=2737
     mat_peptide     27..380
                     /product="interleukin-13 receptor subunit alpha-2"
                     /calculated_mol_wt=41457
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Region          142..235
                     /region_name="IL6Ra-bind"
                     /note="Interleukin-6 receptor alpha chain, binding;
                     pfam09240"
                     /db_xref="CDD:401252"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20223216; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Site            290
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14627.1)"
     Region          322..326
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14627.1)"
     Site            344..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14627.1)"
     CDS             1..380
                     /gene="IL13RA2"
                     /gene_synonym="CD213A2; CT19; IL-13R; IL13BP"
                     /coded_by="NM_000640.3:98..1240"
                     /db_xref="CCDS:CCDS14565.1"
                     /db_xref="GeneID:3598"
                     /db_xref="HGNC:HGNC:5975"
                     /db_xref="MIM:300130"
ORIGIN      
        1 mafvclaigc lytflisttf gctsssdtei kvnppqdfei vdpgylgyly lqwqpplsld
       61 hfkectveye lkyrnigset wktiitknlh ykdgfdlnkg ieakihtllp wqctngsevq
      121 sswaettywi spqgipetkv qdmdcvyynw qyllcswkpg igvlldtnyn lfywyegldh
      181 alqcvdyika dgqnigcrfp yleasdykdf yicvngssen kpirssyftf qlqnivkplp
      241 pvyltftres sceiklkwsi plgpiparcf dyeieiredd ttlvtatven etytlkttne
      301 trqlcfvvrs kvniycsddg iwsewsdkqc wegedlskkt llrfwlpfgf ililvifvtg
      361 lllrkpntyp kmipeffcdt
//
LOCUS       NP_002800                534 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 3 [Homo sapiens].
ACCESSION   NP_002800
VERSION     NP_002800.2
DBSOURCE    REFSEQ: accession NM_002809.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Chen,J., Lian,P., Zhao,X., Li,J., Yu,X., Huang,X., Chen,S. and
            Lu,L.
  TITLE     PSMD3 gene mutations cause pathological myopia
  JOURNAL   J Med Genet 60 (9), 918-924 (2023)
   PUBMED   36948574
  REMARK    GeneRIF: PSMD3 gene mutations cause pathological myopia.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Zhang,J., Ma,Q., Yu,Q., Xiao,F., Zhang,Z., Feng,H. and Liang,C.
  TITLE     PSMD3-ILF3 signaling cascade drives lung cancer cell proliferation
            and migration
  JOURNAL   Biol Direct 18 (1), 33 (2023)
   PUBMED   37337223
  REMARK    GeneRIF: PSMD3-ILF3 signaling cascade drives lung cancer cell
            proliferation and migration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Kominami,K., Okura,N., Kawamura,M., DeMartino,G.N., Slaughter,C.A.,
            Shimbara,N., Chung,C.H., Fujimuro,M., Yokosawa,H., Shimizu,Y.,
            Tanahashi,N., Tanaka,K. and Toh-e,A.
  TITLE     Yeast counterparts of subunits S5a and p58 (S3) of the human 26S
            proteasome are encoded by two multicopy suppressors of nin1-1
  JOURNAL   Mol Biol Cell 8 (1), 171-187 (1997)
   PUBMED   9017604
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY034626.1, D67025.1 and
            AA143716.1.
            
            On Nov 27, 2002 this sequence version replaced NP_002800.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. This
            gene encodes a member of the proteasome subunit S3 family that
            functions as one of the non-ATPase subunits of the 19S regulator
            lid. Single nucleotide polymorphisms in this gene are associated
            with neutrophil count. [provided by RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK054611.1, SRR3476690.333839.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264639.9/ ENSP00000264639.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.1"
     Protein         1..534
                     /product="26S proteasome non-ATPase regulatory subunit 3"
                     /note="tissue specific transplantation antigen 2; 26S
                     proteasome regulatory subunit S3; proteasome subunit p58;
                     26S proteasome regulatory subunit RPN3; proteasome
                     (prosome, macropain) 26S subunit, non-ATPase, 3"
                     /calculated_mol_wt=60847
     Region          1..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43242.2)"
     Region          358..462
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43242.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43242.2)"
     Region          465..523
                     /region_name="Rpn3_C"
                     /note="Proteasome regulatory subunit C-terminal;
                     pfam08375"
                     /db_xref="CDD:462452"
     Region          500..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43242.2)"
     CDS             1..534
                     /gene="PSMD3"
                     /gene_synonym="P58; RPN3; S3; TSTA2"
                     /coded_by="NM_002809.4:165..1769"
                     /db_xref="CCDS:CCDS11356.1"
                     /db_xref="GeneID:5709"
                     /db_xref="HGNC:HGNC:9560"
                     /db_xref="MIM:617676"
ORIGIN      
        1 mkqegsarrr gadkakpppg ggeqeppppp apqdvemkee aatgggstge adgktaaaaa
       61 ehsqreldtv tledikehvk qlekavsgke prfvlralrm lpstsrrlnh yvlykavqgf
      121 ftsnnatrdf llpfleepmd teadlqfrpr tgkaastpll peveaylqll vvifmmnskr
      181 ykeaqkisdd lmqkistqnr raldlvaakc yyyharvyef ldkldvvrsf lharlrtatl
      241 rhdadgqatl lnlllrnylh yslydqaekl vsksvfpeqa nnnewaryly ytgrikaiql
      301 eysearrtmt nalrkapqht avgfkqtvhk llivvelllg eipdrlqfrq pslkrslmpy
      361 flltqavrtg nlakfnqvld qfgekfqadg tytliirlrh nviktgvrmi slsysrisla
      421 diaqklqlds pedaefivak airdgvieas inhekgyvqs kemidiystr epqlafhqri
      481 sfcldihnms vkamrfppks ynkdlesaee rrereqqdle fakemaeddd dsfp
//
LOCUS       NP_060948                259 aa            linear   PRI 20-NOV-2025
DEFINITION  dysbindin domain-containing protein 2 isoform e [Homo sapiens].
ACCESSION   NP_060948
VERSION     NP_060948.3
DBSOURCE    REFSEQ: accession NM_018478.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Elsholz,L., Wasser,Y., Ziegler,P., Habib,P. and Voigt,A.
  TITLE     CK1BP Reduces alpha-Synuclein Oligomerization and Aggregation
            Independent of Serine 129 Phosphorylation
  JOURNAL   Cells 10 (11), 2830 (2021)
   PUBMED   34831053
  REMARK    GeneRIF: CK1BP Reduces alpha-Synuclein Oligomerization and
            Aggregation Independent of Serine 129 Phosphorylation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Yin,H., Laguna,K.A., Li,G. and Kuret,J.
  TITLE     Dysbindin structural homologue CK1BP is an isoform-selective
            binding partner of human casein kinase-1
  JOURNAL   Biochemistry 45 (16), 5297-5308 (2006)
   PUBMED   16618118
  REMARK    GeneRIF: CK1BP is an isoform-selective binding partner of human
            casein kinase-1
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Lucas,T., Pratscher,B., Fink,D., Wolschek,M., Samorapoompichit,P.,
            Schofer,C., Pehamberger,H., Muller,M., Sorensen,P. and Jansen,B.
  TITLE     The human orthologue of a novel apoptosis response gene induced
            during rat myelomonocytic stem cell apoptosis maps to 20q13.12
  JOURNAL   Stem Cells Dev 14 (5), 556-563 (2005)
   PUBMED   16305340
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF220191.1, AL021578.4 and AW516035.1.
            
            On Oct 7, 2010 this sequence version replaced NP_060948.2.
            
            Transcript Variant: This variant (9) differs in the 5' UTR and 5'
            coding region, and uses an alternate start codon, compared to
            variant 1. The encoded isoform (e) has a distinct and longer
            N-terminus, compared to isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF220191.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..259
                     /product="dysbindin domain-containing protein 2 isoform e"
                     /note="SCF apoptosis response protein 1; casein kinase-1
                     binding protein; dysbindin (dystrobrevin binding protein
                     1) domain containing 2"
                     /calculated_mol_wt=27540
     Region          27..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQY9.3)"
     Region          103..255
                     /region_name="Dysbindin"
                     /note="Dysbindin (Dystrobrevin binding protein 1);
                     pfam04440"
                     /db_xref="CDD:461312"
     Region          174..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQY9.3)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRD4; propagated from
                     UniProtKB/Swiss-Prot (Q9BQY9.3)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRD4; propagated from
                     UniProtKB/Swiss-Prot (Q9BQY9.3)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRD4; propagated from
                     UniProtKB/Swiss-Prot (Q9BQY9.3)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CRD4; propagated from
                     UniProtKB/Swiss-Prot (Q9BQY9.3)"
     CDS             1..259
                     /gene="DBNDD2"
                     /gene_synonym="C20orf35; CK1BP; HSMNP1"
                     /coded_by="NM_018478.3:232..1011"
                     /note="isoform e is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS56193.1"
                     /db_xref="GeneID:55861"
                     /db_xref="HGNC:HGNC:15881"
                     /db_xref="MIM:611453"
ORIGIN      
        1 mgagnfltal evpvaalaga asdrrascer vspppplphf rlpplprsrl pgpvsrpepg
       61 apllgcwlqw gapspgplcl lfrlcsctcf aplpagadmd pnpraalerq qlrlrerqkf
      121 fedilqpete fvfplshlhl esqrppigsi ssmevnvdtl eqvelidlgd pdaadvflpc
      181 edppptpqss gmdnhleels lpvptsdrtt srtssssssd sstnlhspnp sddgadtpla
      241 qsdeeeergd ggaepgacs
//
LOCUS       NP_001317937            1149 aa            linear   PRI 20-NOV-2025
DEFINITION  intersectin-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001317937 XP_016883928
VERSION     NP_001317937.1
DBSOURCE    REFSEQ: accession NM_001331008.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1149)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1149)
  AUTHORS   Lan,C., Zhang,H., Wang,K., Liu,X., Zhao,Y., Guo,Z., Zhang,N.,
            Zhou,Y., Gao,M., Gu,F. and Ma,Y.
  TITLE     The alternative splicing of intersectin 1 regulated by PTBP1
            promotes human glioma progression
  JOURNAL   Cell Death Dis 13 (9), 835 (2022)
   PUBMED   36171198
  REMARK    GeneRIF: The alternative splicing of intersectin 1 regulated by
            PTBP1 promotes human glioma progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1149)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1149)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1149)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1149)
  AUTHORS   Sengar,A.S., Wang,W., Bishay,J., Cohen,S. and Egan,S.E.
  TITLE     The EH and SH3 domain Ese proteins regulate endocytosis by linking
            to dynamin and Eps15
  JOURNAL   EMBO J 18 (5), 1159-1171 (1999)
   PUBMED   10064583
REFERENCE   7  (residues 1 to 1149)
  AUTHORS   Yamabhai,M., Hoffman,N.G., Hardison,N.L., McPherson,P.S.,
            Castagnoli,L., Cesareni,G. and Kay,B.K.
  TITLE     Intersectin, a novel adaptor protein with two Eps15 homology and
            five Src homology 3 domains
  JOURNAL   J Biol Chem 273 (47), 31401-31407 (1998)
   PUBMED   9813051
REFERENCE   8  (residues 1 to 1149)
  AUTHORS   Guipponi,M., Scott,H.S., Chen,H., Schebesta,A., Rossier,C. and
            Antonarakis,S.E.
  TITLE     Two isoforms of a human intersectin (ITSN) protein are produced by
            brain-specific alternative splicing in a stop codon
  JOURNAL   Genomics 53 (3), 369-376 (1998)
   PUBMED   9799604
REFERENCE   9  (residues 1 to 1149)
  AUTHORS   Chen,H. and Antonarakis,S.E.
  TITLE     The SH3D1A gene maps to human chromosome 21q22.1-->q22.2
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 213-215 (1997)
   PUBMED   9465890
REFERENCE   10 (residues 1 to 1149)
  AUTHORS   Sparks,A.B., Hoffman,N.G., McConnell,S.J., Fowlkes,D.M. and
            Kay,B.K.
  TITLE     Cloning of ligand targets: systematic isolation of SH3
            domain-containing proteins
  JOURNAL   Nat Biotechnol 14 (6), 741-744 (1996)
   PUBMED   9630982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027846.1, AP000308.1,
            AP000311.1, KF511399.1, AP000312.2 and CX163355.1.
            
            On Sep 3, 2016 this sequence version replaced XP_016883928.1.
            
            Summary: The protein encoded by this gene is a cytoplasmic
            membrane-associated protein that indirectly coordinates endocytic
            membrane traffic with the actin assembly machinery. In addition,
            the encoded protein may regulate the formation of clathrin-coated
            vesicles and could be involved in synaptic vesicle recycling. This
            protein has been shown to interact with dynamin, CDC42, SNAP23,
            SNAP25, SPIN90, EPS15, EPN1, EPN2, and STN2. Multiple transcript
            variants encoding different isoforms have been found for this gene,
            but the full-length nature of only two of them have been
            characterized so far. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.91155.1, DQ679755.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..1149
                     /product="intersectin-1 isoform 3"
                     /note="human intersectin-SH3 domain-containing protein
                     SH3P17; Src homology 3 domain-containing protein; SH3
                     domain-containing protein 1A; intersectin 1 (SH3 domain
                     protein)"
                     /calculated_mol_wt=129885
     Region          14..108
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          214..309
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <363..>684
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          744..803
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(749,751,754,758,783..784,797,799..800)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          803..917
                     /region_name="INTAP"
                     /note="Intersectin and clathrin adaptor AP2 binding
                     region; pfam16617"
                     /db_xref="CDD:435467"
     Region          917..968
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(922,924,927,931,948..949,962,964..965)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1006..1067
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(1012,1014,1017,1021,1039..1040,1058,1060..1061)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1087..1140
                     /region_name="SH3_Intersectin1_5"
                     /note="Fifth Src homology 3 domain (or SH3E) of
                     Intersectin-1; cd11995"
                     /db_xref="CDD:212928"
     Site            order(1093,1095,1098,1102,1120..1121,1134,1136..1137)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212928"
     CDS             1..1149
                     /gene="ITSN1"
                     /gene_synonym="ITSN; SH3D1A; SH3P17"
                     /coded_by="NM_001331008.2:246..3695"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82661.1"
                     /db_xref="GeneID:6453"
                     /db_xref="HGNC:HGNC:6183"
                     /db_xref="MIM:602442"
ORIGIN      
        1 maqfptpfgg sldiwaitve erakhdqqfh slkpisgfit gdqarnfffq sglpqpvlaq
       61 iwaladmnnd grmdqvefsi amkliklklq gyqlpsalpp vmkqqpvais sapafgmggi
      121 asmppltava pvpmgsipvv gmsptlvssv ptaavpplan gappviqplp afahpaatlp
      181 ksssfsrsgp gsqlntklqk aqsfdvasvp pvaewavpqs srlkyrqlfn shdktmsghl
      241 tgpqartilm qsslpqaqla siwnlsdidq dgkltaeefi lamhlidvam sgqplppvlp
      301 peyippsfrr vrsgsgisvi sstsvdqrlp eepvledeqq qlekklpvtf edkkrenfer
      361 gnlelekrrq alleqqrkeq erlaqlerae qerkererqe qerkrqlele kqlekqrele
      421 rqreeerrke ierreaakre lerqrqlewe rnrrqellnq rnkeqedivv lkakkktlef
      481 elealndkkh qlegklqdir crlttqrqei estnksrelr iaeithlqqq lqesqqmlgr
      541 lipekqilnd qlkqvqqnsl hrdslvtlkr aleakelarq hlrdqldeve ketrsklqei
      601 difnnqlkel reihnkqqlq kqksmeaerl kqkeqerkii elekqkeeaq rraqerdkqw
      661 lehvqqedeh qrprklheee klkreesvkk kdgeekgkqe aqdklgrlfh qhqepakpav
      721 qapwstaekg pltisaqenv kvvyyralyp fesrshdeit iqpgdivmvk gewvdesqtg
      781 epgwlggelk gktgwfpany aekipenevp apvkpvtdst sapapklalr etpaplavts
      841 sepsttpnnw adfsstwpts tnekpetdnw dawaaqpslt vpsagqlrqr saftpatatg
      901 sspspvlgqg ekveglqaqa lypwrakkdn hlnfnkndvi tvleqqdmww fgevqgqkgw
      961 fpksyvklis gpirkstsmd sgssespasl krvaspaakp vvsgeeiaqv iasytatgpe
     1021 qltlapgqli lirkknpggw wegelqargk krqigwfpan yvkllspgts kitpteppks
     1081 talaavcqvi gmydytaqnd delafnkgqi invlnkedpd wwkgevngqv glfpsnyvkl
     1141 ttdmdpsqq
//
LOCUS       NP_940999               1094 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec24C [Homo sapiens].
ACCESSION   NP_940999
VERSION     NP_940999.1
DBSOURCE    REFSEQ: accession NM_198597.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1094)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1094)
  AUTHORS   Rebensburg,S.V., Wei,G., Larue,R.C., Lindenberger,J., Francis,A.C.,
            Annamalai,A.S., Morrison,J., Shkriabai,N., Huang,S.W.,
            KewalRamani,V., Poeschla,E.M., Melikyan,G.B. and Kvaratskhelia,M.
  TITLE     Sec24C is an HIV-1 host dependency factor crucial for virus
            replication
  JOURNAL   Nat Microbiol 6 (4), 435-444 (2021)
   PUBMED   33649557
  REMARK    GeneRIF: Sec24C is an HIV-1 host dependency factor crucial for
            virus replication.
REFERENCE   6  (residues 1 to 1094)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   7  (residues 1 to 1094)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   8  (residues 1 to 1094)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   9  (residues 1 to 1094)
  AUTHORS   Tani,K., Oyama,Y., Hatsuzawa,K. and Tagaya,M.
  TITLE     Hypothetical protein KIAA0079 is a mammalian homologue of yeast
            Sec24p
  JOURNAL   FEBS Lett 447 (2-3), 247-250 (1999)
   PUBMED   10214955
REFERENCE   10 (residues 1 to 1094)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022400.9, AL596994.1,
            BC018928.2, D38555.1 and CA419040.1.
            
            Summary: The protein encoded by this gene is a member of the SEC24
            subfamily of the SEC23/SEC24 family, which is involved in vesicle
            trafficking. The encoded protein has similarity to yeast Sec24p
            component of COPII. COPII is the coat protein complex responsible
            for vesicle budding from the ER. The product of this gene may play
            a role in shaping the vesicle, as well as in cargo selection and
            concentration. Alternatively spliced transcript variants encoding
            the same protein have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks a segment in the 5' UTR
            region, compared to variant 1. Both variants 1 and 2 encode the
            same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.4989.1,
                                           SRR1803614.201498.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345254.9/ ENSP00000321845.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..1094
                     /product="protein transport protein Sec24C"
                     /note="SEC24 family, member C; SEC24-related protein C;
                     SEC24 related gene family, member C; SEC24 homolog C,
                     COPII coat complex component"
                     /calculated_mol_wt=118194
     Region          1..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     Region          <4..329
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          181..1090
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P53992.3)"
     Region          425..450
                     /region_name="Zinc finger-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     Region          962..1034
                     /region_name="Gelsolin-like. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     CDS             1..1094
                     /gene="SEC24C"
                     /coded_by="NM_198597.3:95..3379"
                     /db_xref="CCDS:CCDS7332.1"
                     /db_xref="GeneID:9632"
                     /db_xref="HGNC:HGNC:10705"
                     /db_xref="MIM:607185"
ORIGIN      
        1 mnvnqsvppv ppfgqpqpiy pgyhqssygg qsgstapaip ygayngpvpg yqqtppqgms
       61 rappssgapp astaqapcgq aaygqfgqgd vqngpsstvq mqrlpgsqpf gsplapvgnq
      121 ppvlqpygpp ptsaqvatql sgmqisgava pappssglgf gpptslasas gsfpnsglyg
      181 sypqgqappl sqaqghpgiq tpqrsapsqa ssftppasgg prlpsmtgpl lpgqsfggps
      241 vsqpnhvssp pqalppgtqm tgplgplppm hspqqpgyqp qqngsfgpar gpqsnyggpy
      301 paaptfgsqp gppqplppkr ldpdaipspi qvieddrnnr gtepfvtgvr gqvpplvttn
      361 flvkdqgnas pryirctsyn ipctsdmakq aqvplaavik plarlppeea spyvvdhges
      421 gplrcnrcka ymcpfmqfie ggrrfqccfc scindvppqy fqhldhtgkr vdaydrpels
      481 lgsyeflatv dycknnkfps ppafifmidv synairtglv rllceelksl ldflpregga
      541 eesairvgfv tynkvlhfyn vksslaqpqm mvvsdvadmf vplldgflvn vnesravits
      601 lldqipemfa dtretetvfv pviqagmeal kaaecagklf lfhtslpiae apgklknrdd
      661 rklintdkek tlfqpqtgay qtlakecvaq gccvdlflfp nqyvdvatls vvpqltggsv
      721 ykyasfqven dqerflsdlr rdvqkvvgfd avmrvrtstg iravdffgaf ymsnttdvel
      781 agldgdktvt vefkhddrln eesgallqca llytscagqr rlrihnlaln cctqladlyr
      841 ncetdtliny makfayrgvl nspvkavrdt litqcaqila cyrkncasps sagqlilpec
      901 mkllpvylnc vlksdvlqpg aevttddray vrqlvtsmdv tetnvffypr llpltkspve
      961 stteppavra seerlsngdi yllenglnlf lwvgasvqqg vvqslfsvss fsqitsglsv
     1021 lpvldnplsk kvrglidslr aqrsrymklt vvkqedkmem lfkhflvedk slsggasyvd
     1081 flchmhkeir qlls
//
LOCUS       NP_001290554             214 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL16 isoform a [Homo sapiens].
ACCESSION   NP_001290554
VERSION     NP_001290554.1
DBSOURCE    REFSEQ: accession NM_001303625.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Wang,K., Chen,S., Wu,Y., Wang,Y., Lu,Y., Sun,Y. and Chen,Y.
  TITLE     The ufmylation modification of ribosomal protein L10 in the
            development of pancreatic adenocarcinoma
  JOURNAL   Cell Death Dis 14 (6), 350 (2023)
   PUBMED   37280198
  REMARK    GeneRIF: The ufmylation modification of ribosomal protein L10 in
            the development of pancreatic adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Farmer,A.A., Johnsen,J.I., Loftus,T.M., Smith,K.P. and
            Stanbridge,E.J.
  TITLE     Isolation and characterization of the QM promoter
  JOURNAL   Nucleic Acids Res 24 (11), 2158-2165 (1996)
   PUBMED   8668549
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Farmer,A.A., Loftus,T.M., Mills,A.A., Sato,K.Y., Neill,J.D.,
            Tron,T., Yang,M., Trumpower,B.L. and Stanbridge,E.J.
  TITLE     Extreme evolutionary conservation of QM, a novel c-Jun associated
            transcription factor
  JOURNAL   Hum Mol Genet 3 (5), 723-728 (1994)
   PUBMED   8081358
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Kaneko,K., Kobayashi,H., Onodera,O., Miyatake,T. and Tsuji,S.
  TITLE     Genomic organization of a cDNA (QM) demonstrating an altered mRNA
            level in nontumorigenic Wilms' microcell hybrid cells and its
            localization to Xq28
  JOURNAL   Hum Mol Genet 1 (7), 529-533 (1992)
   PUBMED   1339145
REFERENCE   7  (residues 1 to 214)
  AUTHORS   van den Ouweland,A.M., Verdijk,M., Mannens,M.M. and van Oost,B.A.
  TITLE     The QM gene is X-linked and therefore not involved in suppression
            of tumorigenesis in Wilms' tumor
  JOURNAL   Hum Genet 90 (1-2), 144-146 (1992)
   PUBMED   1330878
REFERENCE   8  (residues 1 to 214)
  AUTHORS   van den Ouweland,A.M., Kioschis,P., Verdijk,M., Tamanini,F.,
            Toniolo,D., Poustka,A. and van Oost,B.A.
  TITLE     Identification and characterization of a new gene in the human Xq28
            region
  JOURNAL   Hum Mol Genet 1 (4), 269-273 (1992)
   PUBMED   1303197
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Bignon,C., Roux-Dosseto,M., Zeigler,M.E., Wicha,M.S. and
            Martin,P.M.
  TITLE     cDNA cloning and genomic analysis of a new multigene family sharing
            common phylogenetic and expression profiles with the laminin
            receptor gene
  JOURNAL   Biochem Biophys Res Commun 184 (3), 1165-1172 (1992)
   PUBMED   1534224
REFERENCE   10 (residues 1 to 214)
  AUTHORS   Dowdy,S.F., Lai,K.M., Weissman,B.E., Matsui,Y., Hogan,B.L. and
            Stanbridge,E.J.
  TITLE     The isolation and characterization of a novel cDNA demonstrating an
            altered mRNA level in nontumorigenic Wilms' microcell hybrid cells
  JOURNAL   Nucleic Acids Res 19 (20), 5763-5769 (1991)
   PUBMED   1658743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA589764.1, BM761549.1,
            BC003358.1 and AC245140.2.
            
            Summary: This gene encodes a ribosomal protein that is a component
            of the 60S ribosome subunit. The related protein in chicken can
            bind to c-Jun and can repress c-Jun-mediated transcriptional
            activation. Some studies have detected an association between
            variation in this gene and autism spectrum disorders, though others
            do not detect this relationship. There are multiple pseudogenes of
            this gene dispersed throughout the genome. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2015].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1, 4, and 5 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD248160.1, CD248767.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..214
                     /product="large ribosomal subunit protein uL16 isoform a"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10; tumor suppressor QM;
                     Wilms tumor-related protein; laminin receptor homolog;
                     large ribosomal subunit protein uL16"
                     /calculated_mol_wt=24446
     Region          1..209
                     /region_name="PTZ00173"
                     /note="60S ribosomal protein L10; Provisional"
                     /db_xref="CDD:185498"
     Site            order(41,43..44,47,63..64,67,70,74,77,88..90,92,94,98..99,
                     115..119,133,153..154,157..158)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            56..57
                     /site_type="other"
                     /note="5S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            order(68..70,73..74)
                     /site_type="other"
                     /note="putative antibiotic binding site [chemical
                     binding]"
                     /db_xref="CDD:238714"
     Site            order(77,85..86,88,139)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     Site            order(113..114,117..118)
                     /site_type="other"
                     /note="L27 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     CDS             1..214
                     /gene="RPL10"
                     /gene_synonym="AUTSX5; DXS648; DXS648E; L10; MRXS35; NOV;
                     QM; uL16"
                     /coded_by="NM_001303625.1:358..1002"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS14746.1"
                     /db_xref="GeneID:6134"
                     /db_xref="HGNC:HGNC:10298"
                     /db_xref="MIM:312173"
ORIGIN      
        1 mgrrparcyr ycknkpypks rfcrgvpdak irifdlgrkk akvdefplcg hmvsdeyeql
       61 ssealeaari cankymvksc gkdgfhirvr lhpfhvirin kmlscagadr lqtgmrgafg
      121 kpqgtvarvh igqvimsirt klqnkehvie alrrakfkfp grqkihiskk wgftkfnade
      181 fedmvaekrl ipdgcgvkyi psrgpldkwr alhs
//
LOCUS       NP_003782               1052 aa            linear   PRI 20-NOV-2025
DEFINITION  membrane-bound transcription factor site-1 protease preproprotein
            [Homo sapiens].
ACCESSION   NP_003782
VERSION     NP_003782.1
DBSOURCE    REFSEQ: accession NM_003791.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1052)
  AUTHORS   Chen,J., Zhou,Y., Liu,Z., Lu,Y., Jiang,Y., Cao,K., Zhou,N.,
            Wang,D., Zhang,C., Zhou,N., Shi,K., Zhang,L., Zhou,L., Wang,Z.,
            Zhang,H., Tang,K., Ma,J., Lv,J. and Huang,B.
  TITLE     Hepatic glycogenesis antagonizes lipogenesis by blocking S1P via
            UDPG
  JOURNAL   Science 383 (6684), eadi3332 (2024)
   PUBMED   38359126
  REMARK    GeneRIF: Hepatic glycogenesis antagonizes lipogenesis by blocking
            S1P via UDPG.
REFERENCE   2  (residues 1 to 1052)
  AUTHORS   Santinelli,R., Benz,N., Guellec,J., Quinquis,F., Kocas,E.,
            Thomas,J., Montier,T., Ka,C., Luczka-Majerus,E., Sage,E., Ferec,C.,
            Coraux,C. and Trouve,P.
  TITLE     The Inhibition of the Membrane-Bound Transcription Factor Site-1
            Protease (MBTP1) Alleviates the p.Phe508del-Cystic Fibrosis
            Transmembrane Conductance Regulator (CFTR) Defects in Cystic
            Fibrosis Cells
  JOURNAL   Cells 13 (2), 185 (2024)
   PUBMED   38247876
  REMARK    GeneRIF: The Inhibition of the Membrane-Bound Transcription Factor
            Site-1 Protease (MBTP1) Alleviates the p.Phe508del-Cystic Fibrosis
            Transmembrane Conductance Regulator (CFTR) Defects in Cystic
            Fibrosis Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1052)
  AUTHORS   Liu,X.T., Huang,Y., Liu,D., Jiang,Y.C., Zhao,M., Chung,L.H.,
            Han,X.D., Zhao,Y., Chen,J., Coleman,P., Ting,K.K., Tran,C., Su,Y.,
            Dennis,C.V., Bhatnagar,A., Liu,K., Don,A.S., Vadas,M.A.,
            Gorrell,M.D., Zhang,S., Murray,M., Kavurma,M.M., McCaughan,G.W.,
            Gamble,J.R. and Qi,Y.
  TITLE     Targeting the SphK1/S1P/PFKFB3 axis suppresses hepatocellular
            carcinoma progression by disrupting glycolytic energy supply that
            drives tumor angiogenesis
  JOURNAL   J Transl Med 22 (1), 43 (2024)
   PUBMED   38200582
  REMARK    GeneRIF: Targeting the SphK1/S1P/PFKFB3 axis suppresses
            hepatocellular carcinoma progression by disrupting glycolytic
            energy supply that drives tumor angiogenesis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1052)
  AUTHORS   Fang,C., Ren,P., Bian,G., Wang,J., Bai,J., Huang,J., Ding,Y.,
            Li,X., Li,M. and Hou,Z.
  TITLE     Enhancing Spns2/S1P in macrophages alleviates hyperinflammation and
            prevents immunosuppression in sepsis
  JOURNAL   EMBO Rep 24 (8), e56635 (2023)
   PUBMED   37358015
  REMARK    GeneRIF: Enhancing Spns2/S1P in macrophages alleviates
            hyperinflammation and prevents immunosuppression in sepsis.
REFERENCE   5  (residues 1 to 1052)
  AUTHORS   Li,F., Zhang,Y., Lin,Z., Yan,L., Liu,Q., Li,Y., Pei,X., Feng,Y.,
            Han,X., Yang,J., Zheng,F., Li,T., Zhang,Y., Fu,Z., Shao,D., Yu,J.
            and Li,C.
  TITLE     Targeting SPHK1/S1PR3-regulated S-1-P metabolic disorder triggers
            autophagic cell death in pulmonary lymphangiomyomatosis (LAM)
  JOURNAL   Cell Death Dis 13 (12), 1065 (2022)
   PUBMED   36543771
  REMARK    GeneRIF: Targeting SPHK1/S1PR3-regulated S-1-P metabolic disorder
            triggers autophagic cell death in pulmonary lymphangiomyomatosis
            (LAM).
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1052)
  AUTHORS   Seidah,N.G., Mowla,S.J., Hamelin,J., Mamarbachi,A.M., Benjannet,S.,
            Toure,B.B., Basak,A., Munzer,J.S., Marcinkiewicz,J., Zhong,M.,
            Barale,J.C., Lazure,C., Murphy,R.A., Chretien,M. and
            Marcinkiewicz,M.
  TITLE     Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed
            proprotein convertase with a unique cleavage specificity and
            cellular localization
  JOURNAL   Proc Natl Acad Sci U S A 96 (4), 1321-1326 (1999)
   PUBMED   9990022
REFERENCE   7  (residues 1 to 1052)
  AUTHORS   Sakai,J., Rawson,R.B., Espenshade,P.J., Cheng,D., Seegmiller,A.C.,
            Goldstein,J.L. and Brown,M.S.
  TITLE     Molecular identification of the sterol-regulated luminal protease
            that cleaves SREBPs and controls lipid composition of animal cells
  JOURNAL   Mol Cell 2 (4), 505-514 (1998)
   PUBMED   9809072
REFERENCE   8  (residues 1 to 1052)
  AUTHORS   Duncan,E.A., Brown,M.S., Goldstein,J.L. and Sakai,J.
  TITLE     Cleavage site for sterol-regulated protease localized to a leu-Ser
            bond in the lumenal loop of sterol regulatory element-binding
            protein-2
  JOURNAL   J Biol Chem 272 (19), 12778-12785 (1997)
   PUBMED   9139737
REFERENCE   9  (residues 1 to 1052)
  AUTHORS   Siezen,R.J. and Leunissen,J.A.
  TITLE     Subtilases: the superfamily of subtilisin-like serine proteases
  JOURNAL   Protein Sci 6 (3), 501-523 (1997)
   PUBMED   9070434
  REMARK    Review article
REFERENCE   10 (residues 1 to 1052)
  AUTHORS   Wang,H., Wierenga,A., Prabhu,S. and Wierenga,K.
  TITLE     MBTPS1-Related Spondyloepimetaphyseal Dysplasia with Elevated
            Lysosomal Enzymes
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38048414
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP364386.1, D42053.1,
            BC114555.1 and BM680126.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the subtilisin-like
            proprotein convertase family, which includes proteases that process
            protein and peptide precursors trafficking through regulated or
            constitutive branches of the secretory pathway. The encoded protein
            undergoes an initial autocatalytic processing event in the ER to
            generate a heterodimer which exits the ER and sorts to the
            cis/medial-Golgi where a second autocatalytic event takes place and
            the catalytic activity is acquired. It encodes a type 1 membrane
            bound protease which is ubiquitously expressed and regulates
            cholesterol or lipid homeostasis via cleavage of substrates at
            non-basic residues. Mutations in this gene may be associated with
            lysosomal dysfunction. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D42053.1, BC114555.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343411.8/ ENSP00000344223.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1052
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.3-q24.1"
     Protein         1..1052
                     /product="membrane-bound transcription factor site-1
                     protease preproprotein"
                     /EC_number="3.4.21.112"
                     /note="site-1 protease; subtilisin/kexin isozyme-1;
                     membrane-bound transcription factor site-1 protease;
                     endopeptidase S1P; proprotein convertase subtilisin/kexin
                     type 8"
                     /calculated_mol_wt=115827
     sig_peptide     1..17
                     /note="propagated from UniProtKB/Swiss-Prot (Q14703.1)"
                     /calculated_mol_wt=1941
     proprotein      18..1052
                     /product="membrane-bound transcription factor site-1
                     protease proprotein"
                     /calculated_mol_wt=115827
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Site            186..187
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:10644685; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     mat_peptide     187..1052
                     /product="Membrane-bound transcription factor site-1
                     protease. /id=PRO_0000027052"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14703.1)"
                     /calculated_mol_wt=96430
     Region          203..455
                     /region_name="Peptidases_S8_SKI-1_like"
                     /note="Peptidase S8 family domain in SKI-1-like proteins;
                     cd07479"
                     /db_xref="CDD:173805"
     Site            order(218,249,289,308,338,414)
                     /site_type="active"
                     /db_xref="CDD:173805"
     Site            order(218,249,414)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:173805"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Site            305
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Region          651..>726
                     /region_name="DUF4350"
                     /note="Domain of unknown function (DUF4350); pfam14258"
                     /db_xref="CDD:464118"
     Site            728
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Region          877..899
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14703.1)"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14703.1)"
     Site            999..1021
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14703.1)"
     Region          1027..1052
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14703.1)"
     CDS             1..1052
                     /gene="MBTPS1"
                     /gene_synonym="CAOP; PCSK8; S1P; SEDKF; SKI-1"
                     /coded_by="NM_003791.4:533..3691"
                     /db_xref="CCDS:CCDS10941.1"
                     /db_xref="GeneID:8720"
                     /db_xref="HGNC:HGNC:15456"
                     /db_xref="MIM:603355"
ORIGIN      
        1 mklvniwlll lvvllcgkkh lgdrlekksf ekapcpgcsh ltlkvefsst vveyeyivaf
       61 ngyftakarn sfissalkss evdnwriipr nnpssdypsd feviqikekq kaglltledh
      121 pnikrvtpqr kvfrslkyae sdptvpcnet rwsqkwqssr plrraslslg sgfwhatgrh
      181 ssrrllraip rqvaqtlqad vlwqmgytga nvrvavfdtg lsekhphfkn vkertnwtne
      241 rtlddglghg tfvagviasm recqgfapda elhifrvftn nqvsytswfl dafnyailkk
      301 idvlnlsigg pdfmdhpfvd kvweltannv imvsaigndg plygtlnnpa dqmdvigvgg
      361 idfedniarf ssrgmttwel pggygrmkpd ivtygagvrg sgvkggcral sgtsvaspvv
      421 agavtllvst vqkrelvnpa smkqaliasa rrlpgvnmfe qghgkldllr ayqilnsykp
      481 qaslspsyid ltecpymwpy csqpiyyggm ptvvnvtiln gmgvtgrivd kpdwqpylpq
      541 ngdnievafs yssvlwpwsg ylaisisvtk kaaswegiaq ghvmitvasp aeteskngae
      601 qtstvklpik vkiiptpprs krvlwdqyhn lryppgyfpr dnlrmkndpl dwngdhihtn
      661 frdmyqhlrs mgyfvevlga pftcfdasqy gtllmvdsee eyfpeeiakl rrdvdnglsl
      721 vifsdwynts vmrkvkfyde ntrqwwmpdt gganipalne llsvwnmgfs dglyegeftl
      781 anhdmyyasg csiakfpedg vvitqtfkdq glevlkqeta vvenvpilgl yqipaegggr
      841 ivlygdsncl ddshrqkdcf wlldallqyt sygvtppsls hsgnrqrpps gagsvtperm
      901 egnhlhrysk vleahlgdpk prplpacprl swakpqplne tapsnlwkhq kllsidldkv
      961 vlpnfrsnrp qvrplspges gawdipggim pgrynqevgq tipvfaflga mvvlaffvvq
     1021 inkaksrpkr rkprvkrpql mqqvhppktp sv
//
LOCUS       NP_001357403             462 aa            linear   PRI 20-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 6 isoform 3 [Homo sapiens].
ACCESSION   NP_001357403 XP_016865159
VERSION     NP_001357403.1
DBSOURCE    REFSEQ: accession NM_001370474.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Chen,Y., Khazina,E., Izaurralde,E. and Weichenrieder,O.
  TITLE     Crystal structure and functional properties of the human CCR4-CAF1
            deadenylase complex
  JOURNAL   Nucleic Acids Res 49 (11), 6489-6510 (2021)
   PUBMED   34038562
  REMARK    GeneRIF: Crystal structure and functional properties of the human
            CCR4-CAF1 deadenylase complex.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Raisch,T., Chang,C.T., Levdansky,Y., Muthukumar,S., Raunser,S. and
            Valkov,E.
  TITLE     Reconstitution of recombinant human CCR4-NOT reveals molecular
            insights into regulated deadenylation
  JOURNAL   Nat Commun 10 (1), 3173 (2019)
   PUBMED   31320642
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Morita,M., Siddiqui,N., Katsumura,S., Rouya,C., Larsson,O.,
            Nagashima,T., Hekmatnejad,B., Takahashi,A., Kiyonari,H., Zang,M.,
            St-Arnaud,R., Oike,Y., Giguere,V., Topisirovic,I.,
            Okada-Hatakeyama,M., Yamamoto,T. and Sonenberg,N.
  TITLE     Hepatic posttranscriptional network comprised of CCR4-NOT
            deadenylase and FGF21 maintains systemic metabolic homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 116 (16), 7973-7981 (2019)
   PUBMED   30926667
  REMARK    GeneRIF: Studied hepatic role in metabolic homeostasis of
            fibroblast growth factor 21(FGF21) and the 'CCR4-NOT complex' (a
            multisubunit protein complex composed of 'CCR4-NOT transcription
            complex subunit 6 like' (CNOT6L) and 'CCR4-NOT transcription
            complex subunit 6' (CNOT6). Results show CNOT6L plays a major role
            in regulation FGF21 levels.
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Morel,A.P., Sentis,S., Bianchin,C., Le Romancer,M., Jonard,L.,
            Rostan,M.C., Rimokh,R. and Corbo,L.
  TITLE     BTG2 antiproliferative protein interacts with the human CCR4
            complex existing in vivo in three cell-cycle-regulated forms
  JOURNAL   J Cell Sci 116 (Pt 14), 2929-2936 (2003)
   PUBMED   12771185
  REMARK    GeneRIF: CCR4 and BTG2 interact and have a role in cell-cycle
            regulation
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Chen,J., Chiang,Y.C. and Denis,C.L.
  TITLE     CCR4, a 3'-5' poly(A) RNA and ssDNA exonuclease, is the catalytic
            component of the cytoplasmic deadenylase
  JOURNAL   EMBO J 21 (6), 1414-1426 (2002)
   PUBMED   11889047
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Dupressoir,A., Morel,A.P., Barbot,W., Loireau,M.P., Corbo,L. and
            Heidmann,T.
  TITLE     Identification of four families of yCCR4- and Mg2+-dependent
            endonuclease-related proteins in higher eukaryotes, and
            characterization of orthologs of yCCR4 with a conserved
            leucine-rich repeat essential for hCAF1/hPOP2 binding
  JOURNAL   BMC Genomics 2, 9 (2001)
   PUBMED   11747467
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Okubo,K., Itoh,K., Fukushima,A., Yoshii,J. and Matsubara,K.
  TITLE     Monitoring cell physiology by expression profiles and discovering
            cell type-specific genes by compiled expression profiles
  JOURNAL   Genomics 30 (2), 178-186 (1995)
   PUBMED   8586417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC122714.2.
            
            On May 8, 2019 this sequence version replaced XP_016865159.1.
            
            Summary: This gene encodes the catalytic component of the CCR4-NOT
            core transcriptional regulation complex. The encoded protein has a
            3'-5' RNase activity and prefers polyadenylated substrates. The
            CCR4-NOT complex plays a role in many cellular processes, including
            miRNA-mediated repression, mRNA degradation, and transcriptional
            regulation. [provided by RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.85036.1,
                                           SRR1803617.253307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..462
                     /product="CCR4-NOT transcription complex subunit 6 isoform
                     3"
                     /EC_number="3.1.13.4"
                     /note="carbon catabolite repression 4 protein; cytoplasmic
                     deadenylase; carbon catabolite repressor protein 4
                     homolog"
                     /calculated_mol_wt=52550
     Region          <1..>38
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          4..26
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          96..445
                     /region_name="Deadenylase_CCR4a"
                     /note="C-terminal deadenylase domain of CCR4a, also known
                     as CCR4-NOT transcription complex subunit 6; cd10313"
                     /db_xref="CDD:197340"
     Site            order(100,145,266,269,271,277,317,319,321,386,391,
                     395..396,436)
                     /site_type="active"
                     /db_xref="CDD:197340"
     Site            order(100,145,266,269,271,277,317,319,321,386,391,395,436)
                     /site_type="other"
                     /note="poly(A) RNA binding site [nucleotide binding]"
                     /db_xref="CDD:197340"
     Site            order(100,145,266,317,319,396,435..436)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197340"
     Site            order(100,145,435)
                     /site_type="other"
                     /note="Mg binding site A [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(266,319,436)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(317,319,436)
                     /site_type="other"
                     /note="Mg binding site B [ion binding]"
                     /db_xref="CDD:197340"
     CDS             1..462
                     /gene="CNOT6"
                     /gene_synonym="CCR4; Ccr4a"
                     /coded_by="NM_001370474.1:529..1917"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:57472"
                     /db_xref="HGNC:HGNC:14099"
                     /db_xref="MIM:608951"
ORIGIN      
        1 mvslrelhln nnllrvlpfe lgklfqlqtl glkgnpltqd ilnlyqepdg trrllnylld
       61 nlsgtakrit teqppprswi mlqepdrtrp talfsvmcyn vlcdkyatrq lygycpswal
      121 nwdyrkkaii qeilscnadi vslqeveteq yysfflvelk ergyngffsp ksrartmseq
      181 erkhvdgcai ffktekftlv qkhtvefnql amansegsea mlnrvmtkdn igvavllelr
      241 kesiempsgk phlgtekqli lvanahmhwd peysdvklvq tmmflsevkn iidkasrnlk
      301 ssvlgefgti plvlcadlns lpdsgvveyl stggvetnhk dfkelrynes ltnfschgkn
      361 gttngrithg fklqsayesg lmpytnytfd fkgiidyify skpqlntlgi lgpldhhwlv
      421 ennisgcphp lipsdhfslf aqlelllpfl pqvngihlpg rr
//
LOCUS       NP_003137                709 aa            linear   PRI 20-NOV-2025
DEFINITION  FACT complex subunit SSRP1 [Homo sapiens].
ACCESSION   NP_003137
VERSION     NP_003137.1
DBSOURCE    REFSEQ: accession NM_003146.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Lyu,Y., Yang,Y., Talwar,V., Lu,H., Chen,C., Salman,S., Wicks,E.E.,
            Huang,T.Y., Drehmer,D., Wang,Y., Zuo,Q., Datan,E., Jackson,W. 3rd,
            Dordai,D., Wang,R. and Semenza,G.L.
  TITLE     Hypoxia-inducible factor 1 recruits FACT and RNF20/40 to mediate
            histone ubiquitination and transcriptional activation of target
            genes
  JOURNAL   Cell Rep 43 (4), 113972 (2024)
   PUBMED   38517892
  REMARK    GeneRIF: Hypoxia-inducible factor 1 recruits FACT and RNF20/40 to
            mediate histone ubiquitination and transcriptional activation of
            target genes.
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Chen,X., Li,M., Wang,D., Wang,Q., Wei,X., Liu,X., Yang,J.,
            Kalvakolanu,D.V., Guo,B. and Zhang,L.
  TITLE     Histone chaperone SSRP1 is required for apoptosis inhibition and
            mitochondrial function in HCC via transcriptional promotion of
            TRAP1
  JOURNAL   Biochem Cell Biol 101 (4), 361-376 (2023)
   PUBMED   37084412
  REMARK    GeneRIF: Histone chaperone SSRP1 is required for apoptosis
            inhibition and mitochondrial function in HCC via transcriptional
            promotion of TRAP1.
REFERENCE   4  (residues 1 to 709)
  AUTHORS   McCauley,M.J., Morse,M., Becker,N., Hu,Q., Botuyan,M.V.,
            Navarrete,E., Huo,R., Muthurajan,U.M., Rouzina,I., Luger,K.,
            Mer,G., Maher,L.J. 3rd and Williams,M.C.
  TITLE     Human FACT subunits coordinate to catalyze both disassembly and
            reassembly of nucleosomes
  JOURNAL   Cell Rep 41 (13), 111858 (2022)
   PUBMED   36577379
  REMARK    GeneRIF: Human FACT subunits coordinate to catalyze both
            disassembly and reassembly of nucleosomes.
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Dyer,M.A., Hayes,P.J. and Baron,M.H.
  TITLE     The HMG domain protein SSRP1/PREIIBF is involved in activation of
            the human embryonic beta-like globin gene
  JOURNAL   Mol Cell Biol 18 (5), 2617-2628 (1998)
   PUBMED   9566881
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Orphanides,G., LeRoy,G., Chang,C.H., Luse,D.S. and Reinberg,D.
  TITLE     FACT, a factor that facilitates transcript elongation through
            nucleosomes
  JOURNAL   Cell 92 (1), 105-116 (1998)
   PUBMED   9489704
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Nagulapalli,S., Pongubala,J.M. and Atchison,M.L.
  TITLE     Multiple proteins physically interact with PU.1. Transcriptional
            synergy with NF-IL6 beta (C/EBP delta, CRP3)
  JOURNAL   J Immunol 155 (9), 4330-4338 (1995)
   PUBMED   7594592
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Bruhn,S.L., Pil,P.M., Essigmann,J.M., Housman,D.E. and Lippard,S.J.
  TITLE     Isolation and characterization of human cDNA clones encoding a high
            mobility group box protein that recognizes structural distortions
            to DNA caused by binding of the anticancer agent cisplatin
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2307-2311 (1992)
   PUBMED   1372440
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Toney,J.H., Donahue,B.A., Kellett,P.J., Bruhn,S.L., Essigmann,J.M.
            and Lippard,S.J.
  TITLE     Isolation of cDNAs encoding a human protein that binds selectively
            to DNA modified by the anticancer drug
            cis-diamminedichloroplatinum(II)
  JOURNAL   Proc Natl Acad Sci U S A 86 (21), 8328-8332 (1989)
   PUBMED   2530581
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1990 Feb;87(4):1625]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000781.6.
            
            Summary: The protein encoded by this gene is a subunit of a
            heterodimer that, along with SUPT16H, forms chromatin
            transcriptional elongation factor FACT. FACT interacts specifically
            with histones H2A/H2B to effect nucleosome disassembly and
            transcription elongation. FACT and cisplatin-damaged DNA may be
            crucial to the anticancer mechanism of cisplatin. This encoded
            protein contains a high mobility group box which most likely
            constitutes the structure recognition element for
            cisplatin-modified DNA. This protein also functions as a
            co-activator of the transcriptional activator p63. An alternatively
            spliced transcript variant of this gene has been described, but its
            full-length nature is not known. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.5331.1,
                                           SRR11853560.5239.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278412.7/ ENSP00000278412.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..709
                     /product="FACT complex subunit SSRP1"
                     /note="chromatin-specific transcription elongation factor
                     80 kDa subunit; high mobility group box; facilitates
                     chromatin remodeling 80 kDa subunit; cisplatin-DNA SSRP;
                     hSSRP1; FACTp80; FACT 80 kDa subunit; recombination signal
                     sequence recognition protein 1; facilitates chromatin
                     transcription complex subunit SSRP1; facilitates chromatin
                     transcription complex 80 kDa subunit"
                     /calculated_mol_wt=80944
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.3,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          21..480
                     /region_name="POB3"
                     /note="Nucleosome-binding factor SPN, POB3 subunit
                     [Transcription / DNA replication, recombination, and
                     repair / Chromatin structure and dynamics]; COG5165"
                     /db_xref="CDD:227494"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            413
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            450..451
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and/or caspase-7; propagated
                     from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          458..709
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000305|PubMed:15659405; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            542
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q08943; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Region          549..615
                     /region_name="HMG-box_SSRP1-like"
                     /note="high mobility group (HMG)-box found in
                     structure-specific recognition protein 1 (SSRP1) and
                     similar proteins; cd21994"
                     /db_xref="CDD:438810"
     Site            order(549,551..552,554..555,558..559,562,566,574..575,
                     578..579,582,585..586,607,611,615)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438810"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15659405,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            659
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q08945.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000305|PubMed:15659405; propagated from
                     UniProtKB/Swiss-Prot (Q08945.1)"
     CDS             1..709
                     /gene="SSRP1"
                     /gene_synonym="FACT; FACT80; T160"
                     /coded_by="NM_003146.3:283..2412"
                     /db_xref="CCDS:CCDS7952.1"
                     /db_xref="GeneID:6749"
                     /db_xref="HGNC:HGNC:11327"
                     /db_xref="MIM:604328"
ORIGIN      
        1 maetlefndv yqevkgsmnd grlrlsrqgi ifknsktgkv dniqagelte giwrrvalgh
       61 glklltkngh vykydgfres efeklsdffk thyrlelmek dlcvkgwnwg tvkfggqlls
      121 fdigdqpvfe iplsnvsqct tgknevtlef hqnddaevsl mevrfyvppt qedgvdpvea
      181 faqnvlskad viqatgdaic ifrelqcltp rgrydiriyp tflhlhgktf dykipyttvl
      241 rlfllphkdq rqmffvisld ppikqgqtry hflillfskd edisltlnmn eeevekrfeg
      301 rltknmsgsl yemvsrvmka lvnrkitvpg nfqghsgaqc itcsykassg llyplergfi
      361 yvhkppvhir fdeisfvnfa rgttttrsfd feietkqgtq ytfssieree ygklfdfvna
      421 kklniknrgl kegmnpsyde yadsdedqhd aylermkeeg kireenands sddsgeetde
      481 sfnpgeeeed vaeefdsnas assssnegds drdekkrkql kkakmakdrk srkkpvevkk
      541 gkdpnapkrp msaymlwlna srekiksdhp gisitdlskk ageiwkgmsk ekkeewdrka
      601 edarrdyeka mkeyeggrge sskrdkskkk kkvkvkmekk stpsrgsssk sssrqlsesf
      661 kskefvssde sssgenkskk krrrsedsee eelastppss edsasgsde
//
LOCUS       NP_001165438             242 aa            linear   PRI 20-NOV-2025
DEFINITION  putative ribosome-binding factor A, mitochondrial isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_001165438
VERSION     NP_001165438.1
DBSOURCE    REFSEQ: accession NM_001171967.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Zhou,W., Liu,X., Lv,M., Shi,Y. and Zhang,L.
  TITLE     The recognition mode between hsRBFA and mitoribosome 12S rRNA
            during mitoribosomal biogenesis
  JOURNAL   Nucleic Acids Res 51 (3), 1353-1363 (2023)
   PUBMED   36620886
  REMARK    GeneRIF: The recognition mode between hsRBFA and mitoribosome 12S
            rRNA during mitoribosomal biogenesis.
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Kuwasako,K., Suzuki,S., Nameki,N., Takizawa,M., Takahashi,M.,
            Tsuda,K., Nagata,T., Watanabe,S., Tanaka,A., Kobayashi,N.,
            Kigawa,T., Guntert,P., Shirouzu,M., Yokoyama,S. and Muto,Y.
  TITLE     1H, 13C, and 15N resonance assignments and solution structures of
            the KH domain of human ribosome binding factor A, mtRbfA, involved
            in mitochondrial ribosome biogenesis
  JOURNAL   Biomol NMR Assign 16 (2), 297-303 (2022)
   PUBMED   35666428
  REMARK    GeneRIF: (1)H, (13)C, and (15)N resonance assignments and solution
            structures of the KH domain of human ribosome binding factor A,
            mtRbfA, involved in mitochondrial ribosome biogenesis.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Itoh,Y., Khawaja,A., Laptev,I., Cipullo,M., Atanassov,I.,
            Sergiev,P., Rorbach,J. and Amunts,A.
  TITLE     Mechanism of mitoribosomal small subunit biogenesis and
            preinitiation
  JOURNAL   Nature 606 (7914), 603-608 (2022)
   PUBMED   35676484
REFERENCE   4  (residues 1 to 242)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Rozanska,A., Richter-Dennerlein,R., Rorbach,J., Gao,F., Lewis,R.J.,
            Chrzanowska-Lightowlers,Z.M. and Lightowlers,R.N.
  TITLE     The human RNA-binding protein RBFA promotes the maturation of the
            mitochondrial ribosome
  JOURNAL   Biochem J 474 (13), 2145-2158 (2017)
   PUBMED   28512204
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK307212.1, AF439745.2 and AC090360.9.
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (2) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF439745.2, SRR5189652.10148.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..242
                     /product="putative ribosome-binding factor A,
                     mitochondrial isoform 2 precursor"
                     /note="putative ribosome-binding factor A, mitochondrial;
                     ribosome binding factor A (putative)"
                     /calculated_mol_wt=22672
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8N0V3.3)"
                     /calculated_mol_wt=4408
     Region          92..>160
                     /region_name="RBFA"
                     /note="Ribosome-binding factor A; pfam02033"
                     /db_xref="CDD:460422"
     CDS             1..242
                     /gene="RBFA"
                     /gene_synonym="C18orf22; HsT169"
                     /coded_by="NM_001171967.2:63..791"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS54194.1"
                     /db_xref="GeneID:79863"
                     /db_xref="HGNC:HGNC:26120"
                     /db_xref="MIM:620768"
ORIGIN      
        1 mwaaagglwr sraglralfr srdaalfpgc erglhcsavs cknwlkkfas ktkkkvwyes
       61 pslgshstyk pskleflmrs tskktrkedh arlralngll ykaltdllct pevsqelydl
      121 nvelskvslt pdfsacrayw kttlsaeqna hmeavlqrsa ahmslisywq sqtldpgmke
      181 ttlykmisgt lmphnpaapq srpqapvcvg simrrstsrl wstkggkikg sgawcgrgrw
      241 ls
//
LOCUS       NP_001337622             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337622
VERSION     NP_001337622.1
DBSOURCE    REFSEQ: accession NM_001350693.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (29), as well as variants 1-4,
            9-28, and 30-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.132377.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350693.1:712..2922"
                     /note="isoform 1 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001354671             530 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform e [Homo sapiens].
ACCESSION   NP_001354671
VERSION     NP_001354671.1
DBSOURCE    REFSEQ: accession NM_001367742.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (26), as well as variant 25,
            encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.53890.1,
                                           SRR1803612.218976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..530
                     /product="rab5 GDP/GTP exchange factor isoform e"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=60718
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..259
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          309..409
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..530
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367742.1:78..1670"
                     /note="isoform e is encoded by transcript variant 26"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgker rfhhvgqagl elltsgdppa sasqsagntg vepphpavpp
      241 ervekimdqi ekyimtrlyk yvfcpettdd ekkdlaiqkr iralrwvtpq mlcvpvnedi
      301 pevsdmvvka itdiiemdsk rvprdklaci tkcskhifna ikitknepas addflptliy
      361 ivlkgnpprl qsniqyitrf cnpsrlmtge dgyyftnlcc avafieklda qslnlsqedf
      421 drymsgqtsp rkqeaeswsp daclgvkqmy knldllsqln erqerimnea kklekdlidw
      481 tdgiarevqd ivekypleik ppnqplaaid senvendklp pplqpqvyag
//
LOCUS       NP_068815                577 aa            linear   PRI 20-NOV-2025
DEFINITION  optineurin [Homo sapiens].
ACCESSION   NP_068815
VERSION     NP_068815.2
DBSOURCE    REFSEQ: accession NM_021980.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Nan,H., Kim,Y.J., Chu,M., Li,D., Li,J., Jiang,D., Wu,Y., Ohtsuka,T.
            and Wu,L.
  TITLE     Genetic and clinical landscape of Chinese frontotemporal dementia:
            dominance of TBK1 and OPTN mutations
  JOURNAL   Alzheimers Res Ther 16 (1), 127 (2024)
   PUBMED   38872230
  REMARK    GeneRIF: Genetic and clinical landscape of Chinese frontotemporal
            dementia: dominance of TBK1 and OPTN mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Jin,J., Huang,R., Chang,Y. and Yi,X.
  TITLE     Roles and mechanisms of optineurin in bone metabolism
  JOURNAL   Biomed Pharmacother 172, 116258 (2024)
   PUBMED   38350370
  REMARK    GeneRIF: Roles and mechanisms of optineurin in bone metabolism.
            Review article
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Yamano,K., Sawada,M., Kikuchi,R., Nagataki,K., Kojima,W., Endo,R.,
            Kinefuchi,H., Sugihara,A., Fujino,T., Watanabe,A., Tanaka,K.,
            Hayashi,G., Murakami,H. and Matsuda,N.
  TITLE     Optineurin provides a mitophagy contact site for TBK1 activation
  JOURNAL   EMBO J 43 (5), 754-779 (2024)
   PUBMED   38287189
  REMARK    GeneRIF: Optineurin provides a mitophagy contact site for TBK1
            activation.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   D'Urso,B., Weil,R. and Genin,P.
  TITLE     [Optineurin and mitochondrial dysfunction in neurodegeneration]
  JOURNAL   Med Sci (Paris) 40 (2), 167-175 (2024)
   PUBMED   38411425
  REMARK    GeneRIF: [Optineurin and mitochondrial dysfunction in
            neurodegeneration].
            Review article
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Fong,K.S. and de Couet,H.G.
  TITLE     Novel proteins interacting with the leucine-rich repeat domain of
            human flightless-I identified by the yeast two-hybrid system
  JOURNAL   Genomics 58 (2), 146-157 (1999)
   PUBMED   10366446
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Sarfarazi,M., Child,A., Stoilova,D., Brice,G., Desai,T.,
            Trifan,O.C., Poinoosawmy,D. and Crick,R.P.
  TITLE     Localization of the fourth locus (GLC1E) for adult-onset primary
            open-angle glaucoma to the 10p15-p14 region
  JOURNAL   Am J Hum Genet 62 (3), 641-652 (1998)
   PUBMED   9497264
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Li,Y., Kang,J. and Horwitz,M.S.
  TITLE     Interaction of an adenovirus E3 14.7-kilodalton protein with a
            novel tumor necrosis factor alpha-inducible cellular protein
            containing leucine zipper domains
  JOURNAL   Mol Cell Biol 18 (3), 1601-1610 (1998)
   PUBMED   9488477
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552635.1, AF420372.1,
            BC032762.1, AF420371.1 and AF070533.1.
            
            On Apr 15, 2002 this sequence version replaced NP_068815.1.
            
            Summary: This gene encodes the coiled-coil containing protein
            optineurin. Optineurin may play a role in normal-tension glaucoma
            and adult-onset primary open angle glaucoma. Optineurin interacts
            with adenovirus E3-14.7K protein and may utilize tumor necrosis
            factor-alpha or Fas-ligand pathways to mediate apoptosis,
            inflammation or vasoconstriction. Optineurin may also function in
            cellular morphogenesis and membrane trafficking, vesicle
            trafficking, and transcription activation through its interactions
            with the RAB8, huntingtin, and transcription factor IIIA proteins.
            Alternative splicing results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.186430.1,
                                           SRR1660809.216864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..577
                     /product="optineurin"
                     /note="nemo-related protein; tumor necrosis factor
                     alpha-inducible cellular protein containing leucine zipper
                     domains; transcrption factor IIIA-interacting protein;
                     Huntingtin interacting protein L; FIP-2; HIP-7; huntingtin
                     yeast partner L; E3-14.7K-interacting protein;
                     huntingtin-interacting protein 7; huntingtin-interacting
                     protein L; optic neuropathy-inducing protein;
                     transcription factor IIIA-interacting protein"
                     /calculated_mol_wt=65791
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          37..103
                     /region_name="NEMO"
                     /note="NF-kappa-B essential modulator NEMO; pfam11577"
                     /db_xref="CDD:431942"
     Region          58..209
                     /region_name="Interaction with Rab8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          101..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          176..181
                     /region_name="LIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21617041,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          186..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          245..>520
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          261..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          408..507
                     /region_name="CC2-LZ"
                     /note="Leucine zipper of domain CC2 of NEMO, NF-kappa-B
                     essential modulator; pfam16516"
                     /db_xref="CDD:465155"
     Region          411..577
                     /region_name="Interaction with HD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          412..520
                     /region_name="Interaction with MYO6.
                     /evidence=ECO:0000269|PubMed:15837803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          474..479
                     /region_name="UBAN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          551..576
                     /region_name="zf_C2H2_10"
                     /note="C2H2 type zinc-finger; pfam18414"
                     /db_xref="CDD:436483"
     CDS             1..577
                     /gene="OPTN"
                     /gene_synonym="ALS12; FIP2; GLC1E; HIP7; HYPL; NRP;
                     TFIIIA-INTP"
                     /coded_by="NM_021980.4:233..1966"
                     /db_xref="CCDS:CCDS7094.1"
                     /db_xref="GeneID:10133"
                     /db_xref="HGNC:HGNC:17142"
                     /db_xref="MIM:602432"
ORIGIN      
        1 mshqplsclt ekedspsest gngpphlahp nldtftpeel lqqmkellte nhqlkeamkl
       61 nnqamkgrfe elsawtekqk eerqffeiqs keakerlmal sheneklkee lgklkgkser
      121 ssedptddsr lpraeaeqek dqlrtqvvrl qaekadllgi vselqlklns sgssedsfve
      181 irmaegeaeg svkeikhspg ptrtvstgta lskyrsrsad gaknyfehee ltvsqlllcl
      241 regnqkverl evalkeaker vsdfekktsn rseietqteg stekendeek gpetvgseve
      301 alnlqvtslf kelqeahtkl seaelmkkrl qekcqalerk nsaipselne kqelvytnkk
      361 lelqvesmls eikmeqakte dekskltvlq mthnkllqeh nnalktieel trkesekvdr
      421 avlkelsekl elaekalask qlqmdemkqt iakqeedlet mtilraqmev ycsdfhaera
      481 arekiheeke qlalqlavll kendafedgg rqslmemqsr hgartsdsdq qaylvqrgae
      541 drdwrqqrni pihscpkcge vlpdidtlqi hvmdcii
//
LOCUS       NP_115677                458 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/WD repeat-containing protein 9 [Homo sapiens].
ACCESSION   NP_115677
VERSION     NP_115677.2
DBSOURCE    REFSEQ: accession NM_032301.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Yu,S., Liang,Z., Fan,Z., Cao,B., Wang,N., Wu,R. and Sun,H.
  TITLE     A Comprehensive Analysis Revealing FBXW9 as a Potential Prognostic
            and Immunological Biomarker in Breast Cancer
  JOURNAL   Int J Mol Sci 24 (6), 5262 (2023)
   PUBMED   36982338
  REMARK    GeneRIF: A Comprehensive Analysis Revealing FBXW9 as a Potential
            Prognostic and Immunological Biomarker in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Sun,Y., Hu,Z., Goeb,Y. and Dreier,L.
  TITLE     The F-box protein MEC-15 (FBXW9) promotes synaptic transmission in
            GABAergic motor neurons in C. elegans
  JOURNAL   PLoS One 8 (3), e59132 (2013)
   PUBMED   23527112
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Lievens,S., Vanderroost,N., Van der Heyden,J., Gesellchen,V.,
            Vidal,M. and Tavernier,J.
  TITLE     Array MAPPIT: high-throughput interactome analysis in mammalian
            cells
  JOURNAL   J Proteome Res 8 (2), 877-886 (2009)
   PUBMED   19159283
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA079240.1, AK123037.1 and AW083348.1.
            
            On Jan 27, 2007 this sequence version replaced NP_115677.1.
            
            Summary: Members of the F-box protein family, such as FBXW9, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603034), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004290.1, AK123037.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393261.8/ ENSP00000376945.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..458
                     /product="F-box/WD repeat-containing protein 9"
                     /note="F-box and WD-40 domain protein 9; specificity
                     factor for SCF ubiquitin ligase; F-box and WD-40 repeat
                     containing protein 9; F-box and WD-40 domain-containing
                     protein 9"
                     /calculated_mol_wt=50629
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          42..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          <89..120
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Site            order(89..90,93..94,98,100..101,106..108,110)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438907"
     Region          <170..457
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          171..210
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          177..222
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..261
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          227..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          264..301
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          270..301
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          305..344
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          305..342
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          344..381
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          350..385
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          387..424
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     Region          392..413
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          427..458
                     /region_name="WD 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX1.3)"
     CDS             1..458
                     /gene="FBXW9"
                     /gene_synonym="Fbw9; MEC-15"
                     /coded_by="NM_032301.3:51..1427"
                     /db_xref="CCDS:CCDS12278.2"
                     /db_xref="GeneID:84261"
                     /db_xref="HGNC:HGNC:28136"
                     /db_xref="MIM:609074"
ORIGIN      
        1 melplgrcdd srtwdddsdp esetdpdaqa kayvarvlsp pksglafsrp sqlstpaasp
       61 sasepraasr vsavsepgll slppelllei csyldarlvl hvlsrvchal rdlvsdhvtw
      121 rlralrrvra pypvveeknf dwpaaciale qhlsrwaedg rwveyfclae ghvasvdsvl
      181 llqggslcls gsrdrnvnlw dlrqlgtesn qvliktlgtk rnsthegwvw slaaqdhrvc
      241 sgswdstvkl wdmaadgqqf geikassavl clsylpdilv tgtydkkvti ydpragpall
      301 khqqlhsrpv ltlladdrhi isgsedhtlv vvdrransvl qrlqldsyll cmsyqepqlw
      361 agdnqgllhv fanrngcfql irsfdvghsf pitgiqysvg alyttstdkt irvhvptdpp
      421 rtictrrhdn glnrvcaegn lvvagsgdls levwrlqa
//
LOCUS       NP_573570               1023 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator 1-beta
            isoform 1 [Homo sapiens].
ACCESSION   NP_573570
VERSION     NP_573570.3
DBSOURCE    REFSEQ: accession NM_133263.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1023)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1023)
  AUTHORS   Huang,M., Prasad,R.B., Coral,D.E., Hjort,L., Minja,D.T.R.,
            Mulder,H., Franks,P.W. and Kalamajski,S.
  TITLE     Human Genetic Variation at rs10071329 Correlates With
            Adiposity-Related Traits, Modulates PPARGC1B Expression, and Alters
            Brown Adipocyte Function
  JOURNAL   Diabetes 73 (4), 637-645 (2024)
   PUBMED   38190589
  REMARK    GeneRIF: Human Genetic Variation at rs10071329 Correlates With
            Adiposity-Related Traits, Modulates PPARGC1B Expression, and Alters
            Brown Adipocyte Function.
REFERENCE   3  (residues 1 to 1023)
  AUTHORS   Shimoda,F., Naito,T., Kakuta,Y., Kawai,Y., Tokunaga,K.,
            Shimoyama,Y., Moroi,R., Shiga,H., Nagasaki,M., Kinouchi,Y. and
            Masamune,A.
  CONSRTM   NCBN Controls WGS Consortium
  TITLE     HLA-DQA1*05 and upstream variants of PPARGC1B are associated with
            infliximab persistence in Japanese Crohn's disease patients
  JOURNAL   Pharmacogenomics J 23 (6), 141-148 (2023)
   PUBMED   37460671
  REMARK    GeneRIF: HLA-DQA1*05 and upstream variants of PPARGC1B are
            associated with infliximab persistence in Japanese Crohn's disease
            patients.
REFERENCE   4  (residues 1 to 1023)
  AUTHORS   Torres,H.M., Yeo,D. and Westendorf,J.J.
  TITLE     Pulling rank with RNA: RANKL promotes the association of
            PGC-1beta/RNA complexes with NCoR/HDAC3 to activate gene expression
            in osteoclasts
  JOURNAL   Mol Cell 83 (19), 3397-3399 (2023)
   PUBMED   37802020
  REMARK    GeneRIF: Pulling rank with RNA: RANKL promotes the association of
            PGC-1beta/RNA complexes with NCoR/HDAC3 to activate gene expression
            in osteoclasts.
REFERENCE   5  (residues 1 to 1023)
  AUTHORS   Chen,S., Zhang,P., Feng,J., Li,R., Chen,J., Zheng,W.V., Zhang,H.
            and Yao,P.
  TITLE     LMP1 mediates tumorigenesis through persistent epigenetic
            modifications and PGC1beta upregulation
  JOURNAL   Oncol Rep 49 (3) (2023)
   PUBMED   36734290
  REMARK    GeneRIF: LMP1 mediates tumorigenesis through persistent epigenetic
            modifications and PGC1beta upregulation.
REFERENCE   6  (residues 1 to 1023)
  AUTHORS   Meirhaeghe,A., Crowley,V., Lenaghan,C., Lelliott,C., Green,K.,
            Stewart,A., Hart,K., Schinner,S., Sethi,J.K., Yeo,G., Brand,M.D.,
            Cortright,R.N., O'Rahilly,S., Montague,C. and Vidal-Puig,A.J.
  TITLE     Characterization of the human, mouse and rat PGC1 beta
            (peroxisome-proliferator-activated receptor-gamma co-activator 1
            beta) gene in vitro and in vivo
  JOURNAL   Biochem J 373 (Pt 1), 155-165 (2003)
   PUBMED   12678921
REFERENCE   7  (residues 1 to 1023)
  AUTHORS   Lin,J., Puigserver,P., Donovan,J., Tarr,P. and Spiegelman,B.M.
  TITLE     Peroxisome proliferator-activated receptor gamma coactivator 1beta
            (PGC-1beta), a novel PGC-1-related transcription coactivator
            associated with host cell factor
  JOURNAL   J Biol Chem 277 (3), 1645-1648 (2002)
   PUBMED   11733490
REFERENCE   8  (residues 1 to 1023)
  AUTHORS   Ek,J., Andersen,G., Urhammer,S.A., Gaede,P.H., Drivsholm,T.,
            Borch-Johnsen,K., Hansen,T. and Pedersen,O.
  TITLE     Mutation analysis of peroxisome proliferator-activated
            receptor-gamma coactivator-1 (PGC-1) and relationships of
            identified amino acid polymorphisms to Type II diabetes mellitus
  JOURNAL   Diabetologia 44 (12), 2220-2226 (2001)
   PUBMED   11793024
REFERENCE   9  (residues 1 to 1023)
  AUTHORS   Knutti,D., Kaul,A. and Kralli,A.
  TITLE     A tissue-specific coactivator of steroid receptors, identified in a
            functional genetic screen
  JOURNAL   Mol Cell Biol 20 (7), 2411-2422 (2000)
   PUBMED   10713165
REFERENCE   10 (residues 1 to 1023)
  AUTHORS   Esterbauer,H., Oberkofler,H., Krempler,F. and Patsch,W.
  TITLE     Human peroxisome proliferator activated receptor gamma coactivator
            1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
            localization, and tissue expression
  JOURNAL   Genomics 62 (1), 98-102 (1999)
   PUBMED   10585775
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC132971.1, AC008545.3 and
            CA435617.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 25, 2010 this sequence version replaced NP_573570.2.
            
            Summary: The protein encoded by this gene stimulates the activity
            of several transcription factors and nuclear receptors, including
            estrogen receptor alpha, nuclear respiratory factor 1, and
            glucocorticoid receptor. The encoded protein may be involved in fat
            oxidation, non-oxidative glucose metabolism, and the regulation of
            energy expenditure. This protein is downregulated in prediabetic
            and type 2 diabetes mellitus patients. Certain allelic variations
            in this gene increase the risk of the development of obesity. Three
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY188947.1, AK095391.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309241.10/ ENSP00000312649.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1023
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..1023
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-beta isoform 1"
                     /note="PGC-1-related estrogen receptor alpha coactivator;
                     PPARGC-1-beta; PPAR-gamma coactivator 1-beta; peroxisome
                     proliferator-activated receptor gamma, coactivator 1 beta;
                     PPARgamma coactivator 1 beta; PPARAGCIbeta"
                     /calculated_mol_wt=113092
     Region          1..91
                     /region_name="Abolishes DNA transcriptional activity when
                     missing"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          122..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          156..160
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          165..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          237..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          302..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          343..347
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          369..463
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          520..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          601..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          636..683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          691..694
                     /region_name="HCFC1-binding-motif (HBM)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          717..758
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          779..867
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YN6.2)"
     Region          895..991
                     /region_name="RRM_PPARGC1B"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-beta
                     (PGC-1-beta) and similar proteins; cd12356"
                     /db_xref="CDD:409792"
     CDS             1..1023
                     /gene="PPARGC1B"
                     /gene_synonym="ERRL1; PERC; PGC-1(beta); PGC1B"
                     /coded_by="NM_133263.4:34..3105"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4298.1"
                     /db_xref="GeneID:133522"
                     /db_xref="HGNC:HGNC:30022"
                     /db_xref="MIM:608886"
ORIGIN      
        1 magndcgall deelssffln yladtqgggs geeqlyadfp eldlsqldas dfdsatcfge
       61 lqwcpenset epnqyspdds elfqidsene allaeltktl ddipeddvgl aafpaldggd
      121 alsctsaspa pssappspap ekpsapapev delsllqkll latsyptsss dtqkegtawr
      181 qaglrsksqr pcvkadstqd kkapmmqsqs rsctelhkhl tsaqcclqdr glqppclqsp
      241 rlpakedkep gedcpspqpa pasprdslal gradpgapvs qedmqamvql irymhtyclp
      301 qrklppqtpe plpkacsnps qqvrsrpwsr hhskaswaef silrellaqd vlcdvskpyr
      361 latpvyaslt prsrprppkd sqaspgrpss veevriaasp kstgprpslr plrlevkrev
      421 rrparlqqqe eedeeeeeee eeeekeeeee wgrkrpgrgl pwtklgrkle ssvcpvrrsr
      481 rlnpelgpwl tfadeplvps epqgalpslc lapkaydver elgsptdeds gqdqqllrgp
      541 qipalespce sgcgdmdedp scpqlpprds prclmlalsq sdptfgkksf eqtltvelcg
      601 tagltppttp pykpteedpf kpdikhslgk eialslpspe glslkatpga ahklpkkhpe
      661 rsellshlrh ataqpasqag qkrpfscsfg dhdycqvlrp egvlqrkvlr swepsgvhle
      721 dwpqqgapwa eaqapgreed rscdagappk dstllrdhei rasltkhfgl letaleeedl
      781 asckspeydt vfedsssssg essflpeeee eegeeeeedd eeedsgvspt csdhcpyqsp
      841 pskanrqlcs rsrsssgssp chswspatrr nfrcesrgpc sdrtpsirha rkrrekaige
      901 grvvyiqnls sdmssrelkr rfevfgeiee cevltrnrrg ekygfityrc sehaalsltk
      961 gaalrkrnep sfqlsygglr hfcwprytdy dsnseealpa sgkskyeamd fdsllkeaqq
     1021 slh
//
LOCUS       NP_001353469             499 aa            linear   PRI 20-NOV-2025
DEFINITION  inositol 1,4,5-triphosphate receptor associated 2 isoform a [Homo
            sapiens].
ACCESSION   NP_001353469
VERSION     NP_001353469.1
DBSOURCE    REFSEQ: accession NM_001366540.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Okumura,W., Tadahira,K., Kozono,T., Tamura-Nakano,M., Sato,H.,
            Matsui,H., Dohi,T., Rohrer,J., Tonozuka,T. and Nishikawa,A.
  TITLE     Jaw1/LRMP is associated with the maintenance of Golgi ribbon
            structure
  JOURNAL   J Biochem 173 (5), 383-392 (2023)
   PUBMED   36689741
  REMARK    GeneRIF: Jaw1/LRMP is associated with the maintenance of Golgi
            ribbon structure.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Okumura,W., Kozono,T., Sato,H., Matsui,H., Takagi,T., Tonozuka,T.
            and Nishikawa,A.
  TITLE     Jaw1/LRMP increases Ca2+ influx upon GPCR stimulation with
            heterogeneous effect on the activity of each ITPR subtype
  JOURNAL   Sci Rep 12 (1), 9476 (2022)
   PUBMED   35676525
  REMARK    GeneRIF: Jaw1/LRMP increases Ca(2+) influx upon GPCR stimulation
            with heterogeneous effect on the activity of each ITPR subtype.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Cruz,V.E., Esra Demircioglu,F. and Schwartz,T.U.
  TITLE     Structural Analysis of Different LINC Complexes Reveals Distinct
            Binding Modes
  JOURNAL   J Mol Biol 432 (23), 6028-6041 (2020)
   PUBMED   33058875
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Bataille,P., Michaud,V., Robert,M.P., Bekel,L., Leclerc-Mercier,S.,
            Harroche,A., Celerier,C., Lasseaux,E., Borgel,D.,
            Bremond-Gignac,D., Bodemer,C., Arveiler,B. and Hadj-Rabia,S.
  TITLE     Clinical variability and probable founder effect in oculocutaneous
            albinism type 7
  JOURNAL   Clin Genet 97 (3), 527-528 (2020)
   PUBMED   31694064
  REMARK    GeneRIF: Clinical variability and probable founder effect in
            oculocutaneous albinism type 7.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Kohno,T., Kunitoh,H., Suzuki,K., Yamamoto,S., Kuchiba,A.,
            Matsuno,Y., Yanagitani,N. and Yokota,J.
  TITLE     Association of KRAS polymorphisms with risk for lung adenocarcinoma
            accompanied by atypical adenomatous hyperplasias
  JOURNAL   Carcinogenesis 29 (5), 957-963 (2008)
   PUBMED   18299280
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Manenti,G., Galbiati,F., Pettinicchio,A., Spinola,M., Piconese,S.,
            Leoni,V.P., Conti,B., Ravagnani,F., Incarbone,M., Pastorino,U. and
            Dragani,T.A.
  TITLE     A V141L polymorphism of the human LRMP gene is associated with
            survival of lung cancer patients
  JOURNAL   Carcinogenesis 27 (7), 1386-1390 (2006)
   PUBMED   16410263
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Snyder,H.L., Bacik,I., Bennink,J.R., Kearns,G., Behrens,T.W.,
            Bachi,T., Orlowski,M. and Yewdell,J.W.
  TITLE     Two novel routes of transporter associated with antigen processing
            (TAP)-independent major histocompatibility complex class I antigen
            processing
  JOURNAL   J Exp Med 186 (7), 1087-1098 (1997)
   PUBMED   9314557
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Behrens,T.W., Kearns,G.M., Rivard,J.J., Bernstein,H.D.,
            Yewdell,J.W. and Staudt,L.M.
  TITLE     Carboxyl-terminal targeting and novel post-translational processing
            of JAW1, a lymphoid protein of the endoplasmic reticulum
  JOURNAL   J Biol Chem 271 (38), 23528-23534 (1996)
   PUBMED   8798562
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Behrens,T.W., Jagadeesh,J., Scherle,P., Kearns,G., Yewdell,J. and
            Staudt,L.M.
  TITLE     Jaw1, A lymphoid-restricted membrane protein localized to the
            endoplasmic reticulum
  JOURNAL   J Immunol 153 (2), 682-690 (1994)
   PUBMED   8021504
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC023510.16.
            
            Summary: The protein encode dby this gene is expressed in a
            developmentally regulated manner in lymphoid cell lines and
            tissues. The protein is localized to the cytoplasmic face of the
            endoplasmic reticulum. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.222479.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p12.1"
     Protein         1..499
                     /product="inositol 1,4,5-triphosphate receptor associated
                     2 isoform a"
                     /note="protein Jaw1; lymphoid restricted membrane protein"
                     /calculated_mol_wt=56082
     Region          4..499
                     /region_name="MRVI1"
                     /note="MRVI1 protein; pfam05781"
                     /db_xref="CDD:461738"
     CDS             1..499
                     /gene="IRAG2"
                     /gene_synonym="JAW1; LRMP"
                     /coded_by="NM_001366540.1:670..2169"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS8701.1"
                     /db_xref="GeneID:4033"
                     /db_xref="HGNC:HGNC:6690"
                     /db_xref="MIM:602003"
ORIGIN      
        1 mnddpsmeen gvervcpesl lqsreysslp lprhtsstdg titssdpgle ilnmascdld
       61 rnslckkeed trsasptiea qgtspahdni afqdstskdk tilnleakee petieehkke
      121 hasgdsvvsp lpvttvksvn lrqsentsan ekeveaeflr lslgfkcdwf tlekrvklee
      181 rsrdlaeenl kkeitnclkl lesltplced dnqaqeiikk leksikflsq caarvasrae
      241 mlgainqesr vskavevmiq hvenlkrmya kehaeleelk qvllqnersf npleddddcq
      301 ikkrsaslns kpsslrrvti aslprnigna gmvagmennd rfsrrssswr ilgskqsehr
      361 pslprfisty swadaeeekc elktkddsep sgeetvertr kpslsekknn pskwdvssvy
      421 dtiaswatnl kssirkanka lwlsiafivl faalmsfltg qlfqksvdaa ptqqedswts
      481 lehilwpftr lrhngpppv
//
LOCUS       NP_001303871             273 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform c [Homo sapiens].
ACCESSION   NP_001303871 XP_011526412
VERSION     NP_001303871.1
DBSOURCE    REFSEQ: accession NM_001316942.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB127388.1, AC008752.6, BI760557.1 and AK000195.1.
            
            On Nov 4, 2015 this sequence version replaced XP_011526412.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (8) uses an alternate splice
            junction, contains an alternate exon, and uses a downstream AUG
            start codon compared to variant 1. The resulting isoform (c) is
            shorter at the N-terminus compared to isoform a. Variants 3, 4, 5,
            6, 7, and 8 all encode the same isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI760557.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2144333,
                                           SAMEA2145245 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..273
                     /product="F-box/LRR-repeat protein 12 isoform c"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=30360
     Region          51..72
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          68..>173
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          100..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <114..238
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          125..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          151..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          231..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..273
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_001316942.2:498..1319"
                     /note="isoform c is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS82287.1"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 mrpkvmwhll rrymasrlhs lrmggylfsg sqapqlspal lralgqkcpn lkrlclhvad
       61 lsmvpitslp stlrtlelhs ceismawlhk qqdptvlpll ecivldrvpa frdehlqglt
      121 rfralrslvl ggtyrvtetg ldaglqelsy lqrlevlgct lsadstllai srhlrdvrki
      181 rltvrglsap glavlegmpa leslclqgpl vtpempspte ilsscltmpk lrvlelqglg
      241 wegqeaekil ckglphcmvi vracpkesmd wwm
//
LOCUS       NP_001091872            1066 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger and BTB domain-containing protein 21 isoform L [Homo
            sapiens].
ACCESSION   NP_001091872
VERSION     NP_001091872.1
DBSOURCE    REFSEQ: accession NM_001098402.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1066)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1066)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1066)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1066)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1066)
  AUTHORS   Heckerman,D., Traynor,B.J., Picca,A., Calvani,R., Marzetti,E.,
            Hernandez,D., Nalls,M., Arepali,S., Ferrucci,L. and Landi,F.
  TITLE     Genetic variants associated with physical performance and
            anthropometry in old age: a genome-wide association study in the
            ilSIRENTE cohort
  JOURNAL   Sci Rep 7 (1), 15879 (2017)
   PUBMED   29158487
  REMARK    GeneRIF: Genotyping was accomplished on Infinium Human610-QUAD
            version 1. In the ilSIRENTE population, genetic variants in ZNF295
            and C2CD2 (rs928874 and rs1788355) on chromosome 21q22.3, were
            significantly associated with the 4-meter gait speed
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1066)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   7  (residues 1 to 1066)
  AUTHORS   Wang,J., Kudoh,J., Takayanagi,A. and Shimizu,N.
  TITLE     Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is
            directly associated with ZFP161
  JOURNAL   Biochem Biophys Res Commun 327 (2), 615-627 (2005)
   PUBMED   15629158
  REMARK    GeneRIF: ZNF295 may be involved in the bi-directional control of
            gene expression in concert with ZFP161
REFERENCE   8  (residues 1 to 1066)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 1066)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 1066)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP230048.1 and AB041014.1.
            
            Transcript Variant: This variant (1) contains an alternate exon in
            the 5' UTR compared to variant 5. Variants 1, 2, and 5 encode the
            longer isoform (L).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB041014.1, DB095107.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2153427,
                                           SAMN03267780 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310826.10/ ENSP00000308759.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1066
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1066
                     /product="zinc finger and BTB domain-containing protein 21
                     isoform L"
                     /note="zinc finger and BTB domain-containing protein 21;
                     zinc finger protein 295"
                     /calculated_mol_wt=118740
     Region          12..123
                     /region_name="BTB_POZ_ZBTB21_ZNF295"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 21 (ZBTB21); cd18209"
                     /db_xref="CDD:349518"
     Region          30..96
                     /region_name="Mediates homodimerization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          154..196
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          388..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          454..485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          498..525
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          545..>598
                     /region_name="SUF4-like"
                     /note="N-terminal domain of Oryza sativa transcription
                     factor SUPPRESSOR OF FRI 4 (OsSUF4), Arabidopsis thaliana
                     SUF4 (AtSUF4), and similar proteins; cd20908"
                     /db_xref="CDD:411020"
     Region          548..569
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Region          548..569
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(553,559,566,568,576,583)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411020"
     Region          577..598
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:411020"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          670..692
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          672..692
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          746..773
                     /region_name="zf_C2H2_6"
                     /note="Zinc Finger domain; pfam18450"
                     /db_xref="CDD:408245"
     Region          806..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          879..906
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Region          911..931
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(916,918,920,922..923,926..927,930,944,946..948,
                     954..955,959)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          939..960
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          963..1014
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9ULJ3.2)"
     CDS             1..1066
                     /gene="ZBTB21"
                     /gene_synonym="ZNF295"
                     /coded_by="NM_001098402.2:188..3388"
                     /note="isoform L is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13678.1"
                     /db_xref="GeneID:49854"
                     /db_xref="HGNC:HGNC:13083"
                     /db_xref="MIM:616485"
ORIGIN      
        1 megllhyinp ahaisllsal neerlkgqlc dvllivgdqk frahknvlaa sseyfqslft
       61 nkenesqtvf qldfcepdaf dnvlnyiyss slfvekssla avqelgyslg isfltnivsk
      121 tpqapfptcp nrkkvfvedd enssqkrsvi vcqsrneaqg ktvsqnqpdv shtsrpspsi
      181 avkantnkph vpkpieplhn lsltekswpk dssvvyaksl ehsgslddpn rislvkrnav
      241 lpskplqdre amddkpgvsg qlpkgkalel alkrprppvl svcsssetpy llketnkgng
      301 qgedrnllyy sklglvipss gsgsgnqsid rsgplvksll rrslsmdsqv pvyspsidlk
      361 ssqgsssvss dapgnvlcal sqksslkdcs ektalddrpq vlqphrlrsf sasqstdreg
      421 aspvtevrik tepssplsdp sdiirvtvgd aattaaasss svtrdlslkt eddqkdmsrl
      481 pakrrfqadr rlpfkklkvn ehgspvsedn feegssptll dadfpdsdln kdefgelegt
      541 rpnkkfkckh clkifrstag lhrhvnmyhn pekpyacdic hkrfhtnfkv wthcqtqhgi
      601 vknpspasss havldekfqr klidivrere ikkaliiklr rgkpgfqgqs ssqaqqvikr
      661 nlrsrakgay ictycgkayr flsqfkqhik mhpgekplgv nkvakpkeha plaspvenke
      721 vyqcrlcnak lsslleqgsh erlcrnaavc pycslrffsp elkqeheskc eykkltclec
      781 mrtfkssfsi wrhqvevhnq nnmaptenfs lpvldhngdv tgssrpqsqp epnkvnhivt
      841 tkddnvfsds seqvnfdsed ssclpedlsl skqlkiqvke epveeaeeea peastapkea
      901 gpskeaslwp cekcgkmftv hkqlerhqel lcsvkpfich vcnkafrtnf rlwshfqshm
      961 sqaseesahk esevcpvptn spsppplppp pplpkiqple pdsptglsen ptpateklfv
     1021 pqesdtlfyh applsaitfk rqfmcklchr tfktafslws heqthn
//
LOCUS       NP_001005417             372 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 2 isoform b [Homo sapiens].
ACCESSION   NP_001005417
VERSION     NP_001005417.1
DBSOURCE    REFSEQ: accession NM_001005417.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Pallet,N., Belleville-Rolland,T., Savalle,A., Lejeune,M., Mauge,L.,
            Bertil,S., Loriot,M.A. and Gaussem,P.
  TITLE     Beta-1,4-galactosyltransferase 2 c.909C>T gene variant is
            predictive of on-clopidogrel platelet reactivity
  JOURNAL   Pharmacogenomics 19 (12), 937-945 (2018)
   PUBMED   30020015
  REMARK    GeneRIF: In individuals under dual antiplatelet therapy, B4GALT2
            c.909C>T is an independent genetic predictor of on-treatment
            platelet reactivity.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Dekkers,G., Plomp,R., Koeleman,C.A., Visser,R., von Horsten,H.H.,
            Sandig,V., Rispens,T., Wuhrer,M. and Vidarsson,G.
  TITLE     Multi-level glyco-engineering techniques to generate IgG with
            defined Fc-glycans
  JOURNAL   Sci Rep 6, 36964 (2016)
   PUBMED   27872474
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Venkitachalam,S., Revoredo,L., Varadan,V., Fecteau,R.E., Ravi,L.,
            Lutterbaugh,J., Markowitz,S.D., Willis,J.E., Gerken,T.A. and
            Guda,K.
  TITLE     Biochemical and functional characterization of
            glycosylation-associated mutational landscapes in colon cancer
  JOURNAL   Sci Rep 6, 23642 (2016)
   PUBMED   27004849
  REMARK    GeneRIF: Study provides evidence that mutations in B3GNT2, B4GALT2,
            and ST6GALNAC2 underlie aberrant glycosylation, and contribute to
            the pathogenesis of molecular subsets of colon and other
            gastrointestinal malignancies.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Brockhausen,I., Dowler,T. and Paulsen,H.
  TITLE     Site directed processing: role of amino acid sequences and
            glycosylation of acceptor glycopeptides in the assembly of extended
            mucin type O-glycan core 2
  JOURNAL   Biochim Biophys Acta 1790 (10), 1244-1257 (2009)
   PUBMED   19524017
  REMARK    GeneRIF: Data show that Beta4-Gal-transferase (beta4GalT) extends
            core 2 and forms the backbone structure for biologically important
            epitopes.
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD675528.1, AK095873.1,
            BC096821.1 and AI702508.1.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. The enzyme
            encoded by this gene synthesizes N-acetyllactosamine in glycolipids
            and glycoproteins. Its substrate specificity is affected by
            alpha-lactalbumin but it is not expressed in lactating mammary
            tissue. Three transcript variants encoding two different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK095873.1, SRR9304719.205659.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..372
                     /product="beta-1,4-galactosyltransferase 2 isoform b"
                     /EC_number="2.4.1.22"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /note="beta-4-GalT2; beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase 2; UDP-Gal:betaGlcNAc beta
                     1,4-galactosyltransferase, polypeptide 2; beta-1,4-GalTase
                     2; UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 2; nal synthase; lactose
                     synthase A protein; N-acetyllactosamine synthase;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=41841
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60909.1)"
     Region          56..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60909.1)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     Region          145..361
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(150,152,154,189,216..218)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            order(216,218,311)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            357
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60909.1)"
     CDS             1..372
                     /gene="B4GALT2"
                     /gene_synonym="B4Gal-T2; B4Gal-T3; beta4Gal-T2"
                     /coded_by="NM_001005417.2:163..1281"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS506.1"
                     /db_xref="GeneID:8704"
                     /db_xref="HGNC:HGNC:925"
                     /db_xref="MIM:604013"
ORIGIN      
        1 msrllggtle rvckavlllc llhflvavil yfdvyaqhla ffsrfsargp ahalhpaass
       61 sssssncsrp natasssglp evpsalpgpt aptlppcpds ppglvgrlli eftspmpler
      121 vqrenpgvlm ggrytppdct paqtvaviip frhrehhlry wlhylhpilr rqrlrygvyv
      181 inqhgedtfn rakllnvgfl ealkedaayd cfifsdvdlv pmddrnlyrc gdqprhfaia
      241 mdkfgfrlpy agyfggvsgl skaqflring fpneywgwgg edddifnris ltgmkisrpd
      301 irigryrmik hdrdkhnepn pqrftkiqnt kltmkrdgig svryqvlevs rqplftnitv
      361 digrppswpp rg
//
LOCUS       NP_001019820             592 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform d precursor [Homo sapiens].
ACCESSION   NP_001019820
VERSION     NP_001019820.1
DBSOURCE    REFSEQ: accession NM_001024649.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2 and BC042843.1.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042843.1, SRR1660809.10008.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..592
                     /product="calnexin isoform d precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65396
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     mat_peptide     21..592
                     /product="calnexin isoform d"
                     /calculated_mol_wt=65396
     Region          71..440
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27824.2)"
     Region          260..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          276..409
                     /region_name="P domain (Extended arm).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          278..345
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          326..359
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          348..405
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          503..592
                     /region_name="Sufficient to mediate interaction with
                     SGIP1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          511..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK3.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     CDS             1..592
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001024649.2:87..1865"
                     /note="isoform d precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS4447.1"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 megkwllcml lvlgtaivea hdghdddvid ieddlddvie evedskpdtt appsspkvty
       61 kapvptgevy fadsfdrgtl sgwilskakk ddtddeiaky dgkweveemk esklpgdkgl
      121 vlmsrakhha isaklnkpfl fdtkplivqy evnfqngiec ggayvkllsk tpelnldqfh
      181 dktpytimfg pdkcgedykl hfifrhknpk tgiyeekhak rpdadlktyf tdkkthlytl
      241 ilnpdnsfei lvdqsvvnsg nllndmtppv npsreiedpe drkpedwder pkipdpeavk
      301 pddwdedapa kipdeeatkp egwlddepey vpdpdaekpe dwdedmdgew eapqianprc
      361 esapgcgvwq rpvidnpnyk gkwkppmidn psyqgiwkpr kipnpdffed lepfrmtpfs
      421 aiglelwsmt sdiffdnfii cadrrivddw andgwglkka adgaaepgvv gqmieaaeer
      481 pwlwvvyilt valpvflvil fccsgkkqts gmeykktdap qpdvkeeeee keeekdkgde
      541 eeegeeklee kqksdaeedg gtvsqeeedr kpkaeedeil nrsprnrkpr re
//
LOCUS       NP_003842                220 aa            linear   PRI 20-NOV-2025
DEFINITION  protein CREG1 precursor [Homo sapiens].
ACCESSION   NP_003842
VERSION     NP_003842.1
DBSOURCE    REFSEQ: accession NM_003851.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Song,H., Tian,X., He,L., Liu,D., Li,J., Mei,Z., Zhou,T., Liu,C.,
            He,J., Jia,X., Yang,Z., Yan,C. and Han,Y.
  TITLE     CREG1 deficiency impaired myoblast differentiation and skeletal
            muscle regeneration
  JOURNAL   J Cachexia Sarcopenia Muscle 15 (2), 587-602 (2024)
   PUBMED   38272853
  REMARK    GeneRIF: CREG1 deficiency impaired myoblast differentiation and
            skeletal muscle regeneration.
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Song,H., Li,J., Peng,C., Liu,D., Mei,Z., Yang,Z., Tian,X.,
            Zhang,X., Jing,Q., Yan,C. and Han,Y.
  TITLE     The role of CREG1 in megakaryocyte maturation and
            thrombocytopoiesis
  JOURNAL   Int J Biol Sci 19 (11), 3614-3627 (2023)
   PUBMED   37496998
  REMARK    GeneRIF: The role of CREG1 in megakaryocyte maturation and
            thrombocytopoiesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Liu,J., Qi,Y., Chao,J., Sathuvalli,P., Y Lee,L. and Li,S.
  TITLE     CREG1 promotes lysosomal biogenesis and function
  JOURNAL   Autophagy 17 (12), 4249-4265 (2021)
   PUBMED   33966596
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Liu,Y., Tian,X., Liu,S., Liu,D., Li,Y., Liu,M., Zhang,X., Yan,C.
            and Han,Y.
  TITLE     DNA hypermethylation: A novel mechanism of CREG gene suppression
            and atherosclerogenic endothelial dysfunction
  JOURNAL   Redox Biol 32, 101444 (2020)
   PUBMED   32067910
  REMARK    GeneRIF: DNA hypermethylation: A novel mechanism of CREG gene
            suppression and atherosclerogenic endothelial dysfunction.
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Tian,X., Yan,C. and Han,Y.
  TITLE     Cellular Repressor of E1A-stimulated Genes, A New Potential
            Therapeutic Target for Atherosclerosis
  JOURNAL   Curr Drug Targets 18 (15), 1800-1804 (2017)
   PUBMED   27784214
  REMARK    GeneRIF: Studies demonstrated that CREG may modulate homeostasis of
            vascular wall cells and inhibit inflammation of vascular tissue
            cells and macrophages. Mechanistically, CREG behaves like a typical
            soluble lysosomal protein that regulates the formation and
            maturation of lysosomes by modulating the small GTPase protein
            Rab7, to mediate autophagy in vascular vascular tissue cells.
            [review]
            Review article
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Di Bacco,A. and Gill,G.
  TITLE     The secreted glycoprotein CREG inhibits cell growth dependent on
            the mannose-6-phosphate/insulin-like growth factor II receptor
  JOURNAL   Oncogene 22 (35), 5436-5445 (2003)
   PUBMED   12934103
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Jiang,L.Q., Wen,S.J., Wang,H.Y. and Chen,L.Y.
  TITLE     Screening the proteins that interact with calpain in a human heart
            cDNA library using a yeast two-hybrid system
  JOURNAL   Hypertens Res 25 (4), 647-652 (2002)
   PUBMED   12358155
REFERENCE   9  (residues 1 to 220)
  AUTHORS   Veal,E., Groisman,R., Eisenstein,M. and Gill,G.
  TITLE     The secreted glycoprotein CREG enhances differentiation of NTERA-2
            human embryonal carcinoma cells
  JOURNAL   Oncogene 19 (17), 2120-2128 (2000)
   PUBMED   10815803
REFERENCE   10 (residues 1 to 220)
  AUTHORS   Veal,E., Eisenstein,M., Tseng,Z.H. and Gill,G.
  TITLE     A cellular repressor of E1A-stimulated genes that inhibits
            activation by E2F
  JOURNAL   Mol Cell Biol 18 (9), 5032-5041 (1998)
   PUBMED   9710587
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF084523.1 and BC006786.1.
            
            Summary: The adenovirus E1A protein both activates and represses
            gene expression to promote cellular proliferation and inhibit
            differentiation. The protein encoded by this gene antagonizes
            transcriptional activation and cellular transformation by E1A. This
            protein shares limited sequence similarity with E1A and binds both
            the general transcription factor TBP and the tumor suppressor pRb
            in vitro. This gene may contribute to the transcriptional control
            of cell growth and differentiation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006786.1, AF084523.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370509.5/ ENSP00000359540.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..220
                     /product="protein CREG1 precursor"
                     /note="protein CREG1"
                     /calculated_mol_wt=21071
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3022
     Region          50..216
                     /region_name="Pyrid_oxidase_2"
                     /note="Pyridoxamine 5'-phosphate oxidase; pfam13883"
                     /db_xref="CDD:404723"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O75629.1)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O75629.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O75629.1)"
     CDS             1..220
                     /gene="CREG1"
                     /gene_synonym="CREG"
                     /coded_by="NM_003851.3:22..684"
                     /db_xref="CCDS:CCDS1262.1"
                     /db_xref="GeneID:8804"
                     /db_xref="HGNC:HGNC:2351"
                     /db_xref="MIM:618055"
ORIGIN      
        1 maglsrgsar allaallast llallvspar grggrdhgdw deasrlpplp predaarvar
       61 fvthvsdwga latistleav rgrpfadvls lsdgppgags gvpyfylspl qlsvsnlqen
      121 pyatltmtla qtnfckkhgf dpqsplcvhi mlsgtvtkvn etemdiakhs lfirhpemkt
      181 wpsshnwffa klnitniwvl dyfggpkivt peeyynvtvq
//
LOCUS       NP_116249                475 aa            linear   PRI 20-NOV-2025
DEFINITION  protein LTV1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_116249
VERSION     NP_116249.2
DBSOURCE    REFSEQ: accession NM_032860.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Han,J.H., Ryan,G., Guy,A., Liu,L., Quinodoz,M., Helbling,I.,
            Lai-Cheong,J.E., Barwell,J., Folcher,M., McGrath,J.A., Moss,C. and
            Rivolta,C.
  CONSRTM   Genomics England Research Consortium
  TITLE     Mutations in the ribosome biogenesis factor gene LTV1 are linked to
            LIPHAK syndrome, a novel poikiloderma-like disorder
  JOURNAL   Hum Mol Genet 31 (12), 1970-1978 (2022)
   PUBMED   34999892
  REMARK    GeneRIF: Mutations in the ribosome biogenesis factor gene LTV1 are
            linked to LIPHAK syndrome, a novel poikiloderma-like disorder.
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Collins,J.C., Ghalei,H., Doherty,J.R., Huang,H., Culver,R.N. and
            Karbstein,K.
  TITLE     Ribosome biogenesis factor Ltv1 chaperones the assembly of the
            small subunit head
  JOURNAL   J Cell Biol 217 (12), 4141-4154 (2018)
   PUBMED   30348748
  REMARK    GeneRIF: Ribosome biogenesis factor Ltv1 chaperones the assembly of
            the small subunit head.
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Ghalei,H., Schaub,F.X., Doherty,J.R., Noguchi,Y., Roush,W.R.,
            Cleveland,J.L., Stroupe,M.E. and Karbstein,K.
  TITLE     Hrr25/CK1delta-directed release of Ltv1 from pre-40S ribosomes is
            necessary for ribosome assembly and cell growth
  JOURNAL   J Cell Biol 208 (6), 745-759 (2015)
   PUBMED   25778921
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Zhang,M., Han,G., Wang,C., Cheng,K., Li,R., Liu,H., Wei,X., Ye,M.
            and Zou,H.
  TITLE     A bead-based approach for large-scale identification of in vitro
            kinase substrates
  JOURNAL   Proteomics 11 (24), 4632-4637 (2011)
   PUBMED   22113938
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA885378.1, BC009855.2 and AA453435.1.
            
            On Jun 10, 2002 this sequence version replaced NP_116249.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1144452.1,
                                           SRR1803614.9919.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367576.6/ ENSP00000356548.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..475
                     /product="protein LTV1 homolog isoform 1"
                     /note="protein LTV1 homolog"
                     /calculated_mol_wt=54724
     Region          15..363
                     /region_name="LTV"
                     /note="Low temperature viability protein; pfam04180"
                     /db_xref="CDD:461211"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GA3.1)"
     Region          23..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GA3.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GA3.1)"
     Region          74..99
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GA3.1)"
     Region          169..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GA3.1)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NSQ7; propagated from
                     UniProtKB/Swiss-Prot (Q96GA3.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96GA3.1)"
     Region          405..447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GA3.1)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GA3.1)"
     CDS             1..475
                     /gene="LTV1"
                     /gene_synonym="C6orf93; dJ468K18.4; IPHAK"
                     /coded_by="NM_032860.5:141..1568"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5201.1"
                     /db_xref="GeneID:84946"
                     /db_xref="HGNC:HGNC:21173"
                     /db_xref="MIM:620074"
ORIGIN      
        1 mphrkkkpfi ekkkavsfhl vhrsqrdpla adesapqrvl lptqkidnee rraeqrkygv
       61 ffdddydylq hlkepsgpse lipsstfsah nrreekeetl vipstgiklp ssvfasefee
      121 dvgllnkaap vsgprldfdp divaaldddf dfddpdnlle ddfilqanka tgeeegmdiq
      181 kseneddsew edvddekgds nddydsagll sdedcmsvpg kthraiadhl fwseetksrf
      241 teysmtssvm rrneqltlhd erfekfyeqy dddeigaldn aelegsiqvd snrlqevlnd
      301 yykekaencv klntlepled qdlpmnelde seeeemitvv leeakekwdc esicstysnl
      361 ynhpqlikyq pkpkqiriss ktgiplnvlp kkgltakqte riqmingsdl pkvstqprsk
      421 neskedkrar kqaikeerke rrvekkankl afklekrrqe kellnlkknv eglkl
//
LOCUS       NP_001003937             410 aa            linear   PRI 20-NOV-2025
DEFINITION  testis-specific Y-encoded-like protein 6 [Homo sapiens].
ACCESSION   NP_001003937 XP_371494
VERSION     NP_001003937.2
DBSOURCE    REFSEQ: accession NM_001003937.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Liang,Y., Zhang,R., Zhang,S., Ji,G., Shi,P., Yang,T., Liu,F.,
            Feng,J., Li,C., Guo,D. and Chen,M.
  TITLE     Association of ACYP2 and TSPYL6 Genetic Polymorphisms with Risk of
            Ischemic Stroke in Han Chinese Population
  JOURNAL   Mol Neurobiol 54 (8), 5988-5995 (2017)
   PUBMED   27686078
  REMARK    GeneRIF: genetic polymorphisms of ACYP2 and TSPYL6 are associated
            with increased risk of developing ischemic stroke
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Liu,M., Li,B., Guo,W., Zhang,X., Chen,Z., Li,J., Yan,M., Chen,C.
            and Jin,T.
  TITLE     Association between single nucleotide polymorphisms in the TSPYL6
            gene and breast cancer susceptibility in the Han Chinese population
  JOURNAL   Oncotarget 7 (34), 54771-54781 (2016)
   PUBMED   27458158
  REMARK    GeneRIF: Findings indicate a significant association between single
            nucleotide polymorphisms (SNPs) in the testis-specific
            Y-encoded-like protein 6 (TSPYL6) gene and breast cancer (BC) risk
            in a Han Chinese population.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB073493.1, AK097417.1 and BC068576.1.
            
            On May 2, 2007 this sequence version replaced NP_001003937.1.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK097417.1, BC068576.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317802.9/ ENSP00000417919.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.2"
     Protein         1..410
                     /product="testis-specific Y-encoded-like protein 6"
                     /note="TSPY-like protein 6; testicular tissue protein Li
                     211"
                     /calculated_mol_wt=45743
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N831.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N831.1)"
     Region          46..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N831.1)"
     Region          210..382
                     /region_name="PTZ00007"
                     /note="(NAP-L) nucleosome assembly protein -L;
                     Provisional; cl08298"
                     /db_xref="CDD:471807"
     CDS             1..410
                     /gene="TSPYL6"
                     /coded_by="NM_001003937.3:79..1311"
                     /db_xref="CCDS:CCDS42682.1"
                     /db_xref="GeneID:388951"
                     /db_xref="HGNC:HGNC:14521"
ORIGIN      
        1 mslpesphsp atldyaledp hqgqrsreks katevmadmf dgrlepivfp pprlpeegva
       61 pqdpadgght fhilvdagrs hgaikagqev tpppaeglea asaslttdgs lkngfpgeet
      121 hglggekale tcgagrsese viaegkaedv kpeecamfsa pvdekpggee mdvaeenrai
      181 devnreagpg pgpgplnvgl hlnplesiql eldsvnaead rallqverrf gqiheyyleq
      241 rndiirnipg fwvtafrhhp qlsamirgqd aemlsyltnl evkelrhprt gckfkfffqr
      301 npyfrnkliv kvyevrsfgq vvsfstlimw rrghgpqsfi hrnrhvicsf ftwfsdhslp
      361 esdriaqiik edlwsnplqy yllgedahra rrrlvrepve iprpfgfqcg
//
LOCUS       NP_808808                502 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane prolyl 4-hydroxylase isoform a [Homo sapiens].
ACCESSION   NP_808808 XP_001133929 XP_001133930
VERSION     NP_808808.1
DBSOURCE    REFSEQ: accession NM_177939.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Gulcu Ustun,N.S.
  TITLE     A pathogenic P4HTM gene variant in two brothers with autism
            spectrum disorder
  JOURNAL   Psychiatr Genet 34 (2), 68-69 (2024)
   PUBMED   38441145
  REMARK    GeneRIF: A pathogenic P4HTM gene variant in two brothers with
            autism spectrum disorder.
REFERENCE   2  (residues 1 to 502)
  AUTHORS   Saeed,S., Ning,L., Badreddine,A., Mirza,M.U., Boissel,M.,
            Khanam,R., Manzoor,J., Janjua,Q.M., Khan,W.I., Toussaint,B.,
            Vaillant,E., Amanzougarene,S., Derhourhi,M., Trant,J.F.,
            Siegert,A.M., Lam,B.Y.H., Yeo,G.S.H., Chabraoui,L., Touzani,A.,
            Kulkarni,A., Farooqi,I.S., Bonnefond,A., Arslan,M. and Froguel,P.
  TITLE     Biallelic Mutations in P4HTM Cause Syndromic Obesity
  JOURNAL   Diabetes 72 (9), 1228-1234 (2023)
   PUBMED   37083980
  REMARK    GeneRIF: Biallelic Mutations in P4HTM Cause Syndromic Obesity.
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Myllykoski,M., Sutinen,A., Koski,M.K., Kallio,J.P., Raasakka,A.,
            Myllyharju,J., Wierenga,R.K. and Koivunen,P.
  TITLE     Structure of transmembrane prolyl 4-hydroxylase reveals unique
            organization of EF and dioxygenase domains
  JOURNAL   J Biol Chem 296, 100197 (2021)
   PUBMED   33334883
  REMARK    GeneRIF: Structure of transmembrane prolyl 4-hydroxylase reveals
            unique organization of EF and dioxygenase domains.
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Maddirevula,S., Ben-Omran,T., AlMureikhi,M., Eyaid,W., Arabi,H.,
            Alkuraya,H., Alfaifi,A., Alfalah,A.H., Alsaif,H.S., Abdulwahab,F.,
            Alfadhel,M. and Alkuraya,F.S.
  TITLE     Further delineation of HIDEA syndrome
  JOURNAL   Am J Med Genet A 182 (12), 2999-3006 (2020)
   PUBMED   32965080
  REMARK    GeneRIF: Further delineation of HIDEA syndrome.
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Seo,K., Seo,S., Ki,S.H. and Shin,S.M.
  TITLE     Sestrin2 inhibits hypoxia-inducible factor-1alpha accumulation via
            AMPK-mediated prolyl hydroxylase regulation
  JOURNAL   Free Radic Biol Med 101, 511-523 (2016)
   PUBMED   27840318
  REMARK    GeneRIF: The results suggest that SESN2 increases degradation of
            HIF-1A via AMPK-PHD regulation that contributes to inhibition of in
            vitro and in vivo tumorigenesis.
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Koivunen,P., Tiainen,P., Hyvarinen,J., Williams,K.E., Sormunen,R.,
            Klaus,S.J., Kivirikko,K.I. and Myllyharju,J.
  TITLE     An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is
            induced by hypoxia and acts on hypoxia-inducible factor alpha
  JOURNAL   J Biol Chem 282 (42), 30544-30552 (2007)
   PUBMED   17726031
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Hirota,K. and Semenza,G.L.
  TITLE     Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl
            hydroxylases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 610-616 (2005)
   PUBMED   16154531
  REMARK    GeneRIF: This review summarizes recent progress in elucidating the
            molecular mechanisms of hypoxia-inducible factor (HIF)-1
            activation, focusing on the role of oxygen-dependent asparaginyl
            hydroxylase in hypoxia signal transduction.
            Review article
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Pekkala,M., Hieta,R., Bergmann,U., Kivirikko,K.I., Wierenga,R.K.
            and Myllyharju,J.
  TITLE     The peptide-substrate-binding domain of collagen prolyl
            4-hydroxylases is a tetratricopeptide repeat domain with functional
            aromatic residues
  JOURNAL   J Biol Chem 279 (50), 52255-52261 (2004)
   PUBMED   15456751
  REMARK    GeneRIF: crystal structure of the peptide-substrate-binding domain
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Hirsila,M., Koivunen,P., Gunzler,V., Kivirikko,K.I. and
            Myllyharju,J.
  TITLE     Characterization of the human prolyl 4-hydroxylases that modify the
            hypoxia-inducible factor
  JOURNAL   J Biol Chem 278 (33), 30772-30780 (2003)
   PUBMED   12788921
  REMARK    GeneRIF: the longest and shortest isoenzymes have major transcripts
            encoding inactive polypeptides, which suggest novel regulation by
            alternative splicing.
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Oehme,F., Ellinghaus,P., Kolkhof,P., Smith,T.J., Ramakrishnan,S.,
            Hutter,J., Schramm,M. and Flamme,I.
  TITLE     Overexpression of PH-4, a novel putative proline 4-hydroxylase,
            modulates activity of hypoxia-inducible transcription factors
  JOURNAL   Biochem Biophys Res Commun 296 (2), 343-349 (2002)
   PUBMED   12163023
  REMARK    GeneRIF: Data suggest that PH-4 is a novel hypoxia-inducible
            factor-prolyl hydroxylase that may be involved in the degradation
            of hypoxia-inducible transcription factors under normoxia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC047566.1, BC011710.2,
            BC000580.1, AW072069.1 and AC137630.9.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_001133930.1, XP_001133929.1.
            
            Summary: The product of this gene belongs to the family of prolyl
            4-hydroxylases. This protein is a prolyl hydroxylase that may be
            involved in the degradation of hypoxia-inducible transcription
            factors under normoxia. It plays a role in adaptation to hypoxia
            and may be related to cellular oxygen sensing. Alternatively
            spliced variants encoding different isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.80976.1,
                                           SRR3476690.955576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000383729.9/ ENSP00000373235.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..502
                     /product="transmembrane prolyl 4-hydroxylase isoform a"
                     /EC_number="1.14.11.29"
                     /note="P4H with transmembrane domain; Prolyl hydroxlase
                     domain-containing 4; hypoxia-inducible factor prolyl
                     4-hydroxylase; proline 4-hydroxylase; transmembrane prolyl
                     4-hydroxylase; HPH-4; HIF-PH4; HIF-prolyl hydroxylase 4;
                     hypoxia-inducible factor prolyl hydroxylase 4; prolyl
                     4-hydroxylase, transmembrane (endoplasmic reticulum)"
                     /calculated_mol_wt=56530
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Region          89..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Region          192..252
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          246..458
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG6.2)"
     CDS             1..502
                     /gene="P4HTM"
                     /gene_synonym="EGLN4; HIDEA; HIFPH4; P4H-TM; PH-4; PH4;
                     PHD4"
                     /coded_by="NM_177939.3:17..1525"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43089.1"
                     /db_xref="GeneID:54681"
                     /db_xref="HGNC:HGNC:28858"
                     /db_xref="MIM:614584"
ORIGIN      
        1 maaaavtgqr petaaaeeas rpqwappdhc qaqaaaglgd gedapvrplc kprgicsray
       61 flvlmvfvhl ylgnvlalll fvhysngdes sdpgpqhraq gpgpeptlgp ltrlegikvg
      121 herkvqlvtd rdhfirtlsl kpllfeipgf ltdeecrlii hlaqmkglqr sqilpteeye
      181 eamstmqvsq ldlfrlldqn rdghlqlrev laqtrlgngw wmtpesiqem yaaikadpdg
      241 dgvlslqefs nmdlrdfhky mrshkaesse lvrnshhtwl yqgegahhim rairqrvlrl
      301 trlspeivel seplqvvryg egghyhahvd sgpvypetic shtklvanes vpfetscrym
      361 tvlfylnnvt gggetvfpva dnrtydemsl iqddvdlrdt rrhcdkgnlr vkpqqgtavf
      421 wynylpdgqg wvgdvddysl hggclvtrgt kwiannwinv dpsrarqalf qqemarlare
      481 ggtdsqpewa ldrayrdarv el
//
LOCUS       NP_001306133             267 aa            linear   PRI 20-NOV-2025
DEFINITION  pro-opiomelanocortin preproprotein [Homo sapiens].
ACCESSION   NP_001306133
VERSION     NP_001306133.1
DBSOURCE    REFSEQ: accession NM_001319204.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Santana,C.V.N., Magno,L.A.V., Ramos,A.V., Rios,M.A., Sandrim,V.C.,
            De Marco,L.A., de Miranda,D.M. and Romano-Silva,M.A.
  TITLE     Genetic Variations in AMPK, FOXO3A, and POMC Increase the Risk of
            Extreme Obesity
  JOURNAL   J Obes 2024, 3813621 (2024)
   PUBMED   39484290
  REMARK    GeneRIF: Genetic Variations in AMPK, FOXO3A, and POMC Increase the
            Risk of Extreme Obesity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Bando,H., Yamamoto,M., Urai,S., Motomura,Y., Sasaki,Y., Ohmachi,Y.,
            Kobatake,M., Tsujimoto,Y., Oi-Yo,Y., Suzuki,M., Yamamoto,N.,
            Takahashi,M., Fukuoka,H., Iguchi,G. and Ogawa,W.
  TITLE     Fluctuations in plasma adrenocorticotropic hormone concentration
            may predict the onset of immune checkpoint inhibitor-related
            hypophysitis
  JOURNAL   J Immunother Cancer 12 (2), e008634 (2024)
   PUBMED   38418395
  REMARK    GeneRIF: Fluctuations in serum adrenocorticotropic hormone
            concentration may predict the onset of immune checkpoint
            inhibitor-related hypophysitis.
            Erratum:[J Immunother Cancer. 2024 Mar 29;12(3):e008634corr1. doi:
            10.1136/jitc-2023-008634corr1. PMID: 38553010]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Singh,M. and Mukhopadhyay,K.
  TITLE     Alpha-melanocyte stimulating hormone: an emerging anti-inflammatory
            antimicrobial peptide
  JOURNAL   Biomed Res Int 2014, 874610 (2014)
   PUBMED   25140322
  REMARK    Review article
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Pritchard,L.E. and White,A.
  TITLE     Neuropeptide processing and its impact on melanocortin pathways
  JOURNAL   Endocrinology 148 (9), 4201-4207 (2007)
   PUBMED   17584964
  REMARK    Review article
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Raffin-Sanson,M.L., de Keyzer,Y. and Bertagna,X.
  TITLE     Proopiomelanocortin, a polypeptide precursor with multiple
            functions: from physiology to pathological conditions
  JOURNAL   Eur J Endocrinol 149 (2), 79-90 (2003)
   PUBMED   12887283
  REMARK    GeneRIF: POMC has become a paradigmatic polypeptide precursor model
            illustrating the variable roles of a single gene and its various
            products in different localities--review
            Review article
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Challis,B.G. and Millington,G.W.M.
  TITLE     Proopiomelanocortin Deficiency - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354022
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Mountjoy,K.G., Robbins,L.S., Mortrud,M.T. and Cone,R.D.
  TITLE     The cloning of a family of genes that encode the melanocortin
            receptors
  JOURNAL   Science 257 (5074), 1248-1251 (1992)
   PUBMED   1325670
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Takahashi,H., Hakamata,Y., Watanabe,Y., Kikuno,R., Miyata,T. and
            Numa,S.
  TITLE     Complete nucleotide sequence of the human
            corticotropin-beta-lipotropin precursor gene
  JOURNAL   Nucleic Acids Res 11 (19), 6847-6858 (1983)
   PUBMED   6314261
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Dragon,N., Seidah,N.G., Lis,M., Routhier,R. and Chretien,M.
  TITLE     Primary structure and morphine-like activity of human
            beta-endorphin
  JOURNAL   Can J Biochem 55 (6), 666-670 (1977)
   PUBMED   195688
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Li,C.H. and Chung,D.
  TITLE     Primary structure of human beta-lipotropin
  JOURNAL   Nature 260 (5552), 622-624 (1976)
   PUBMED   1264228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY050419.1, CD106051.1,
            BC065832.1 and T29537.1.
            
            Summary: This gene encodes a preproprotein that undergoes
            extensive, tissue-specific, post-translational processing via
            cleavage by subtilisin-like enzymes known as prohormone
            convertases. There are eight potential cleavage sites within the
            preproprotein and, depending on tissue type and the available
            convertases, processing may yield as many as ten biologically
            active peptides involved in diverse cellular functions. The encoded
            protein is synthesized mainly in corticotroph cells of the anterior
            pituitary where four cleavage sites are used; adrenocorticotrophin,
            essential for normal steroidogenesis and the maintenance of normal
            adrenal weight, and lipotropin beta are the major end products. In
            other tissues, including the hypothalamus, placenta, and
            epithelium, all cleavage sites may be used, giving rise to peptides
            with roles in pain and energy homeostasis, melanocyte stimulation,
            and immune modulation. These include several distinct
            melanotropins, lipotropins, and endorphins that are contained
            within the adrenocorticotrophin and beta-lipotropin peptides. The
            antimicrobial melanotropin alpha peptide exhibits antibacterial and
            antifungal activity. Mutations in this gene have been associated
            with early onset obesity, adrenal insufficiency, and red hair
            pigmentation. Alternatively spliced transcript variants encoding
            the same protein have been described. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (3) represents the longest
            transcript. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD106051.1, CD513745.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 25140322
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..267
                     /product="pro-opiomelanocortin preproprotein"
                     /note="met-enkephalin; melanotropin gamma; gamma-MSH;
                     adrenocorticotropic hormone; melanotropin alpha;
                     alpha-MSH; corticotropin-like intermediary peptide;
                     lipotropin beta; beta-LPH; lipotropin gamma; gamma-LPH;
                     melanotropin beta; beta-MSH; beta-endorphin;
                     alpha-melanocyte-stimulating hormone; pro-ACTH-endorphin;
                     beta-melanocyte-stimulating hormone; adrenocorticotropin;
                     proopiomelanocortin preproprotein;
                     corticotropin-lipotropin; opiomelanocortin prepropeptide"
                     /calculated_mol_wt=26679
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2763
     mat_peptide     27..102
                     /product="NPP. /id=PRO_0000024966"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=8469
     Region          28..70
                     /region_name="NPP"
                     /note="Pro-opiomelanocortin, N-terminal region; pfam08384"
                     /db_xref="CDD:429962"
     Site            71
                     /site_type="glycosylation"
                     /note="O-linked (HexNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:6267033; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Region          74..91
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     mat_peptide     77..87
                     /product="Melanotropin gamma.
                     /evidence=ECO:0000269|PubMed:2839146. /id=PRO_0000024967"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=1514
     Site            87
                     /site_type="amidation"
                     /note="Phenylalanine amide. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P01189.2)"
     Region          88..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     105..134
                     /product="Potential peptide. /id=PRO_0000024968"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=3006
     Site            134
                     /site_type="amidation"
                     /note="Glutamic acid 1-amide.
                     /evidence=ECO:0000269|PubMed:6272808; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Region          136..154
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     mat_peptide     138..176
                     /product="Corticotropin. /id=PRO_0000024969"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=4541
     mat_peptide     138..150
                     /product="Melanotropin alpha"
                     /experiment="DESCRIPTION:antimicrobial
                     peptide[PMID:25140322]"
                     /exception="alternative processing"
                     /note="occurs in cells other than corticotroph cells of
                     the anterior pituitary"
                     /calculated_mol_wt=1624
     Site            138
                     /site_type="acetylation"
                     /note="N-acetylserine, in Corticotropin.
                     /evidence=ECO:0000250|UniProtKB:P01191; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Site            150
                     /site_type="amidation"
                     /note="Valine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     156..176
                     /product="Corticotropin-like intermediary peptide.
                     /id=PRO_0000024971"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=2310
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     179..267
                     /product="Lipotropin beta. /id=PRO_0000024972"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=9806
     mat_peptide     179..234
                     /product="Lipotropin gamma. /id=PRO_0000024973"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=6075
     Region          181..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     217..234
                     /product="Melanocyte-stimulating hormone beta.
                     /id=PRO_0000024974"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=2204
     Region          218..236
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     Region          222..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     237..267
                     /product="Beta-endorphin. /id=PRO_0000024975"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=3465
     Region          237..264
                     /region_name="Op_neuropeptide"
                     /note="Opioids neuropeptide; pfam08035"
                     /db_xref="CDD:462343"
     mat_peptide     237..241
                     /product="Met-enkephalin. /id=PRO_0000024976"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=574
     CDS             1..267
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /coded_by="NM_001319204.2:184..987"
                     /db_xref="CCDS:CCDS1717.1"
                     /db_xref="GeneID:5443"
                     /db_xref="HGNC:HGNC:9201"
                     /db_xref="MIM:176830"
ORIGIN      
        1 mprsccsrsg alllalllqa smevrgwcle ssqcqdltte snllecirac kpdlsaetpm
       61 fpgngdeqpl tenprkyvmg hfrwdrfgrr nssssgssga gqkredvsag edcgplpegg
      121 peprsdgakp gpregkrsys mehfrwgkpv gkkrrpvkvy pngaedesae afplefkrel
      181 tgqrlregdg pdgpaddgag aqadlehsll vaaekkdegp yrmehfrwgs ppkdkryggf
      241 mtseksqtpl vtlfknaiik naykkge
//
LOCUS       NP_057457                414 aa            linear   PRI 20-NOV-2025
DEFINITION  WW domain-containing oxidoreductase isoform 1 [Homo sapiens].
ACCESSION   NP_057457 NP_004907
VERSION     NP_057457.1
DBSOURCE    REFSEQ: accession NM_016373.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Cheng,L., Chang,Y., Xia,Z., Liu,Y., Liu,X., Xiong,L., Liu,C.,
            Zhu,X., Wang,M. and Qiu,L.
  TITLE     Remote modulation of WWOX by an intronic variant associated with
            survival of Chinese gastric cancer patients
  JOURNAL   Int J Cancer 154 (2), 307-319 (2024)
   PUBMED   37615513
  REMARK    GeneRIF: Remote modulation of WWOX by an intronic variant
            associated with survival of Chinese gastric cancer patients.
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Shin,M.J., Kim,H.S., Lee,P., Yang,N.G., Kim,J.Y., Eun,Y.S., Lee,W.,
            Kim,D., Lee,Y., Jung,K.E., Hong,D., Shin,J.M., Lee,S.H., Lee,S.Y.,
            Kim,C.D. and Kim,J.E.
  TITLE     Mechanistic Investigation of WWOX Function in NF-kB-Induced Skin
            Inflammation in Psoriasis
  JOURNAL   Int J Mol Sci 25 (1), 167 (2023)
   PUBMED   38203337
  REMARK    GeneRIF: Mechanistic Investigation of WWOX Function in
            NF-kB-Induced Skin Inflammation in Psoriasis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 414)
  AUTHORS   Dong,X.S., Wen,X.J., Zhang,S., Wang,D.G., Xiong,Y. and Li,Z.M.
  TITLE     Identification of compound heterozygous deletion of the WWOX gene
            in WOREE syndrome
  JOURNAL   BMC Med Genomics 16 (1), 291 (2023)
   PUBMED   37974179
  REMARK    GeneRIF: Identification of compound heterozygous deletion of the
            WWOX gene in WOREE syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Cheng,H.C., Huang,P.H., Lai,F.J., Jan,M.S., Chen,Y.L., Chen,S.Y.,
            Chen,W.L., Hsu,C.K., Huang,W. and Hsu,L.J.
  TITLE     Loss of fragile WWOX gene leads to senescence escape and genome
            instability
  JOURNAL   Cell Mol Life Sci 80 (11), 338 (2023)
   PUBMED   37897534
  REMARK    GeneRIF: Loss of fragile WWOX gene leads to senescence escape and
            genome instability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Bednarek,A.K., Keck-Waggoner,C.L., Daniel,R.L., Laflin,K.J.,
            Bergsagel,P.L., Kiguchi,K., Brenner,A.J. and Aldaz,C.M.
  TITLE     WWOX, the FRA16D gene, behaves as a suppressor of tumor growth
  JOURNAL   Cancer Res 61 (22), 8068-8073 (2001)
   PUBMED   11719429
  REMARK    GeneRIF: WWOX, the FRA16D gene, behaves as a suppressor of tumor
            growth.
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Paige,A.J., Taylor,K.J., Taylor,C., Hillier,S.G., Farrington,S.,
            Scott,D., Porteous,D.J., Smyth,J.F., Gabra,H. and Watson,J.E.
  TITLE     WWOX: a candidate tumor suppressor gene involved in multiple tumor
            types
  JOURNAL   Proc Natl Acad Sci U S A 98 (20), 11417-11422 (2001)
   PUBMED   11572989
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Chang,N.S., Pratt,N., Heath,J., Schultz,L., Sleve,D., Carey,G.B.
            and Zevotek,N.
  TITLE     Hyaluronidase induction of a WW domain-containing oxidoreductase
            that enhances tumor necrosis factor cytotoxicity
  JOURNAL   J Biol Chem 276 (5), 3361-3370 (2001)
   PUBMED   11058590
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Ried,K., Finnis,M., Hobson,L., Mangelsdorf,M., Dayan,S.,
            Nancarrow,J.K., Woollatt,E., Kremmidiotis,G., Gardner,A.,
            Venter,D., Baker,E. and Richards,R.I.
  TITLE     Common chromosomal fragile site FRA16D sequence: identification of
            the FOR gene spanning FRA16D and homozygous deletions and
            translocation breakpoints in cancer cells
  JOURNAL   Hum Mol Genet 9 (11), 1651-1663 (2000)
   PUBMED   10861292
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Bednarek,A.K., Laflin,K.J., Daniel,R.L., Liao,Q., Hawkins,K.A. and
            Aldaz,C.M.
  TITLE     WWOX, a novel WW domain-containing protein mapping to human
            chromosome 16q23.3-24.1, a region frequently affected in breast
            cancer
  JOURNAL   Cancer Res 60 (8), 2140-2145 (2000)
   PUBMED   10786676
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF211943.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 25, 2001 this sequence version replaced NP_004907.1.
            
            Summary: This gene encodes a member of the short-chain
            dehydrogenases/reductases (SDR) protein family. This gene spans the
            FRA16D common chromosomal fragile site and appears to function as a
            tumor suppressor gene. Expression of the encoded protein is able to
            induce apoptosis, while defects in this gene are associated with
            multiple types of cancer. Disruption of this gene is also
            associated with autosomal recessive spinocerebellar ataxia 12.
            Disruption of a similar gene in mouse results in impaired
            steroidogenesis, additionally suggesting a metabolic function for
            the protein. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF211943.1, SRR1803614.118508.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000566780.6/ ENSP00000457230.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1-q23.2"
     Protein         1..414
                     /product="WW domain-containing oxidoreductase isoform 1"
                     /EC_number="1.1.1.-"
                     /note="WW domain-containing protein WWOX; fragile site
                     FRA16D oxidoreductase; short chain dehydrogenase/reductase
                     family 41C member 1"
                     /calculated_mol_wt=46546
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Region          18..47
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:15070730,
                     ECO:0000269|PubMed:19366691; propagated from
                     UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Region          50..55
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Region          60..90
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(74,85)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          124..407
                     /region_name="human_WWOX_like_SDR_c-like"
                     /note="human WWOX (WW domain-containing
                     oxidoreductase)-like, classical (c)-like SDRs; cd09809"
                     /db_xref="CDD:187669"
     Region          125..414
                     /region_name="Interaction with MAPT.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Site            order(131,133..136,155..157,182..184,210..212,231,
                     264..266,293,297,323..326,328..329)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187669"
     Region          209..273
                     /region_name="Mediates targeting to the mitochondria.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZC7.1)"
     Site            order(232,266,293,297)
                     /site_type="active"
                     /db_xref="CDD:187669"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by TNK2.
                     /evidence=ECO:0000269|PubMed:16288044; propagated from
                     UniProtKB/Swiss-Prot (Q9NZC7.1)"
     CDS             1..414
                     /gene="WWOX"
                     /gene_synonym="D16S432E; DEE28; EIEE28; FOR; FRA16D;
                     HHCMA56; PRO0128; SCAR12; SDR41C1; WOX1"
                     /coded_by="NM_016373.4:126..1370"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42196.1"
                     /db_xref="GeneID:51741"
                     /db_xref="HGNC:HGNC:12799"
                     /db_xref="MIM:605131"
ORIGIN      
        1 maalryagld dtdsedelpp gweerttkdg wvyyanhtee ktqwehpktg krkrvagdlp
       61 ygweqetden gqvffvdhin krttyldprl aftvddnptk pttrqrydgs ttameilqgr
      121 dftgkvvvvt gansgigfet aksfalhgah vilacrnmar aseavsrile ewhkakveam
      181 tldlallrsv qhfaeafkak nvplhvlvcn aatfalpwsl tkdglettfq vnhlghfylv
      241 qllqdvlcrs aparvivvss eshrftdind slgkldfsrl sptkndywam laynrsklcn
      301 ilfsnelhrr lsprgvtsna vhpgnmmysn ihrswwvytl lftlarpftk smqqgaattv
      361 ycaavpeleg lggmyfnncc rcmpspeaqs eetartlwal serliqerlg sqsg
//
LOCUS       NP_001293106             622 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 6 isoform 2 [Homo sapiens].
ACCESSION   NP_001293106 XP_005262558
VERSION     NP_001293106.1
DBSOURCE    REFSEQ: accession NM_001306177.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Zheng,T., Zhou,H., Zheng,Z., Guo,Y., Liu,J., Zhang,J. and Li,S.
  TITLE     The pathological significance and potential mechanism of ARHGEF6 in
            lung adenocarcinoma
  JOURNAL   Comput Biol Med 158, 106894 (2023)
   PUBMED   37058762
  REMARK    GeneRIF: The pathological significance and potential mechanism of
            ARHGEF6 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Li,K., Wang,H., Yang,C., Li,C., Xue,B. and Zhou,J.
  TITLE     Clinical implication and potential function of ARHGEF6 in acute
            myeloid leukemia: An in vitro study
  JOURNAL   PLoS One 18 (4), e0283934 (2023)
   PUBMED   37027440
  REMARK    GeneRIF: Clinical implication and potential function of ARHGEF6 in
            acute myeloid leukemia: An in vitro study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Klambt,V., Buerger,F., Wang,C., Naert,T., Richter,K., Nauth,T.,
            Weiss,A.C., Sieckmann,T., Lai,E., Connaughton,D.M., Seltzsam,S.,
            Mann,N., Majmundar,A.J., Wu,C.W., Onuchic-Whitford,A.C., Shril,S.,
            Schneider,S., Schierbaum,L., Dai,R., Bekheirnia,M.R., Joosten,M.,
            Shlomovitz,O., Vivante,A., Banne,E., Mane,S., Lifton,R.P.,
            Kirschner,K.M., Kispert,A., Rosenberger,G., Fischer,K.D.,
            Lienkamp,S.S., Zegers,M.M.P. and Hildebrandt,F.
  TITLE     Genetic Variants in ARHGEF6 Cause Congenital Anomalies of the
            Kidneys and Urinary Tract in Humans, Mice, and Frogs
  JOURNAL   J Am Soc Nephrol 34 (2), 273-290 (2023)
   PUBMED   36414417
  REMARK    GeneRIF: Genetic Variants in ARHGEF6 Cause Congenital Anomalies of
            the Kidneys and Urinary Tract in Humans, Mice, and Frogs.
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Wang,N., Li,Y., Zhou,X., Wang,X. and Yang,G.
  TITLE     Comprehensive analysis identifies ARHGEF6 as a potential prognostic
            and immunological biomarker in lung adenocarcinoma
  JOURNAL   Comput Biol Med 153, 106448 (2023)
   PUBMED   36586227
  REMARK    GeneRIF: Comprehensive analysis identifies ARHGEF6 as a potential
            prognostic and immunological biomarker in lung adenocarcinoma.
REFERENCE   6  (residues 1 to 622)
  AUTHORS   Yoshii,S., Tanaka,M., Otsuki,Y., Wang,D.Y., Guo,R.J., Zhu,Y.,
            Takeda,R., Hanai,H., Kaneko,E. and Sugimura,H.
  TITLE     alphaPIX nucleotide exchange factor is activated by interaction
            with phosphatidylinositol 3-kinase
  JOURNAL   Oncogene 18 (41), 5680-5690 (1999)
   PUBMED   10523848
REFERENCE   7  (residues 1 to 622)
  AUTHORS   Yntema,H.G., Hamel,B.C., Smits,A.P., van Roosmalen,T., van den
            Helm,B., Kremer,H., Ropers,H.H., Smeets,D.F. and van Bokhoven,H.
  TITLE     Localisation of a gene for non-specific X linked mental retardation
            (MRX46) to Xq25-q26
  JOURNAL   J Med Genet 35 (10), 801-805 (1998)
   PUBMED   9783701
REFERENCE   8  (residues 1 to 622)
  AUTHORS   Ebinu,J.O., Bottorff,D.A., Chan,E.Y., Stang,S.L., Dunn,R.J. and
            Stone,J.C.
  TITLE     RasGRP, a Ras guanyl nucleotide- releasing protein with calcium-
            and diacylglycerol-binding motifs
  JOURNAL   Science 280 (5366), 1082-1086 (1998)
   PUBMED   9582122
REFERENCE   9  (residues 1 to 622)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 622)
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1 (supplement)
  JOURNAL   DNA Res 1 (5), 251-262 (1994)
   PUBMED   7584048
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135783.6, AK295709.1,
            AK294929.1 and BC033768.1.
            
            On Apr 16, 2015 this sequence version replaced XP_005262558.1.
            
            Summary: Rho GTPases play a fundamental role in numerous cellular
            processes that are initiated by extracellular stimuli that work
            through G protein coupled receptors. The encoded protein belongs to
            a family of cytoplasmic proteins that activate the Ras-like family
            of Rho proteins by exchanging bound GDP for GTP. It may form a
            complex with G proteins and stimulate Rho-dependent signals. This
            protein is activated by PI3-kinase. Mutations in this gene can
            cause X-chromosomal non-specific cognitive disability. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks two 5' exons and
            contains an alternate 5' terminal exon, compared to variant 1.
            These differences cause translation initiation at a downstream AUG
            and result in an isoform (2) with a shorter N-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.87045.1,
                                           SRR1803615.106646.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.3"
     Protein         1..622
                     /product="rho guanine nucleotide exchange factor 6 isoform
                     2"
                     /note="Rac/Cdc42 guanine exchange factor (GEF) 6; rho
                     guanine nucleotide exchange factor 6; PAK-interacting
                     exchange factor, alpha; Rac/Cdc42 guanine nucleotide
                     exchange factor (GEF) 6"
                     /calculated_mol_wt=70660
     Region          8..65
                     /region_name="SH3_alphaPIX"
                     /note="Src Homology 3 domain of alpha-Pak Interactive
                     eXchange factor; cd12060"
                     /db_xref="CDD:212993"
     Site            order(15,17,20,23..24,39,41..43,54,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212993"
     Region          88..265
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(94,98,192,216..217,220..221,223..224,227..228,
                     231..232,235,261,265)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          296..393
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          422..520
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          531..615
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..622
                     /gene="ARHGEF6"
                     /gene_synonym="alpha-PIX; alphaPIX; Cool-2; COOL2; MRX46;
                     PIXA"
                     /coded_by="NM_001306177.2:886..2754"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS78509.1"
                     /db_xref="GeneID:9459"
                     /db_xref="HGNC:HGNC:685"
                     /db_xref="MIM:300267"
ORIGIN      
        1 mtengshqli vkarfnfkqt nedelsvckg diiyvtrvee ggwwegtlng rtgwfpsnyv
       61 reiksserpl spkavkgfet apltknyytv vlqnildtek eyakelqsll vtylrplqsn
      121 nnlstvevts llgnfeevct fqqtlcqale ecskfpenqh kvggcllslm phfksmylay
      181 canhpsavnv ltqhsdeleq fmenqgassp gililttnls kpfmrlekyv tllqelerhm
      241 edthpdhqdi lkaivafktl mgqcqdlrkr kqlelqilse piqawegedi knlgnvifms
      301 qvmvqygace ekeerylmlf snvlimlsas prmsgfiyqg kipiagtvvt rldeiegndc
      361 tfeitgntve rivvhcnnnq dfqewleqln rlirgpascs slsktssssc sahssfsstg
      421 qprgpleppq iikpwslscl rpapplrpsa algykermsy ilkesskspk tmkkflhkrk
      481 terkpseeey virkstaale edaqilkvie ayctsanfqq ghgsstrkds ipqvllpeee
      541 kliieetrsn gqtimeeksl vdtvyalkde vrelkqenkr mkqcleeelk srrdleklvr
      601 rllkqtdeci rgesssktsi lp
//
LOCUS       NP_001245325             242 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein axonemal assembly factor 19 isoform 1 [Homo sapiens].
ACCESSION   NP_001245325
VERSION     NP_001245325.1
DBSOURCE    REFSEQ: accession NM_001258396.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Zubair,M., Khan,R., Ma,A., Hameed,U., Khan,M., Abbas,T., Ahmad,R.,
            Zhou,J.T., Shah,W., Hussain,A., Ahmed,N., Khan,I., Khan,K.,
            Zhang,Y.W., Zhang,H., Wu,L.M. and Shi,Q.H.
  TITLE     A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms
  JOURNAL   Asian J Androl 24 (3), 255-259 (2022)
   PUBMED   35259782
  REMARK    GeneRIF: A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 242)
  AUTHORS   King,S.M. and Patel-King,R.S.
  TITLE     The outer dynein arm assembly factor CCDC103 forms molecular
            scaffolds through multiple self-interaction sites
  JOURNAL   Cytoskeleton (Hoboken) 77 (1-2), 25-35 (2020)
   PUBMED   31858719
  REMARK    GeneRIF: The outer dynein arm assembly factor CCDC103 forms
            molecular scaffolds through multiple self-interaction sites.
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Shoemark,A., Moya,E., Hirst,R.A., Patel,M.P., Robson,E.A.,
            Hayward,J., Scully,J., Fassad,M.R., Lamb,W., Schmidts,M., Dixon,M.,
            Patel-King,R.S., Rogers,A.V., Rutman,A., Jackson,C.L., Goggin,P.,
            Rubbo,B., Ollosson,S., Carr,S., Walker,W., Adler,B.,
            Loebinger,M.R., Wilson,R., Bush,A., Williams,H., Boustred,C.,
            Jenkins,L., Sheridan,E., Chung,E.M.K., Watson,C.M., Cullup,T.,
            Lucas,J.S., Kenia,P., O'Callaghan,C., King,S.M., Hogg,C. and
            Mitchison,H.M.
  TITLE     High prevalence of CCDC103 p.His154Pro mutation causing primary
            ciliary dyskinesia disrupts protein oligomerisation and is
            associated with normal diagnostic investigations
  JOURNAL   Thorax 73 (2), 157-166 (2018)
   PUBMED   28790179
  REMARK    GeneRIF: The CCDC103 p.His154Pro mutation is more prevalent than
            previously thought in the South Asian community in the UK and
            causes primary ciliary dyskinesia that can be difficult to diagnose
            using pathology-based clinical tests.
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Casey,J.P., Goggin,P., McDaid,J., White,M., Ennis,S., Betts,D.R.,
            Lucas,J.S., Elnazir,B. and Lynch,S.A.
  TITLE     A case report of primary ciliary dyskinesia, laterality defects and
            developmental delay caused by the co-existence of a single gene and
            chromosome disorder
  JOURNAL   BMC Med Genet 16, 45 (2015)
   PUBMED   26123568
  REMARK    GeneRIF: A variable and complex phenotype caused by the
            co-inheritance of a single gene mutation in CCDC103 and a
            microduplication at 17q12, both on chromosome 17.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Tarkar,A., Loges,N.T., Slagle,C.E., Francis,R., Dougherty,G.W.,
            Tamayo,J.V., Shook,B., Cantino,M., Schwartz,D., Jahnke,C.,
            Olbrich,H., Werner,C., Raidt,J., Pennekamp,P., Abouhamed,M.,
            Hjeij,R., Kohler,G., Griese,M., Li,Y., Lemke,K., Klena,N., Liu,X.,
            Gabriel,G., Tobita,K., Jaspers,M., Morgan,L.C., Shapiro,A.J.,
            Letteboer,S.J., Mans,D.A., Carson,J.L., Leigh,M.W., Wolf,W.E.,
            Chen,S., Lucas,J.S., Onoufriadis,A., Plagnol,V., Schmidts,M.,
            Boldt,K., Roepman,R., Zariwala,M.A., Lo,C.W., Mitchison,H.M.,
            Knowles,M.R., Burdine,R.D., Loturco,J.J. and Omran,H.
  CONSRTM   UK10K
  TITLE     DYX1C1 is required for axonemal dynein assembly and ciliary
            motility
  JOURNAL   Nat Genet 45 (9), 995-1003 (2013)
   PUBMED   23872636
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Panizzi,J.R., Becker-Heck,A., Castleman,V.H., Al-Mutairi,D.A.,
            Liu,Y., Loges,N.T., Pathak,N., Austin-Tse,C., Sheridan,E.,
            Schmidts,M., Olbrich,H., Werner,C., Haffner,K., Hellman,N.,
            Chodhari,R., Gupta,A., Kramer-Zucker,A., Olale,F., Burdine,R.D.,
            Schier,A.F., O'Callaghan,C., Chung,E.M., Reinhardt,R.,
            Mitchison,H.M., King,S.M., Omran,H. and Drummond,I.A.
  TITLE     CCDC103 mutations cause primary ciliary dyskinesia by disrupting
            assembly of ciliary dynein arms
  JOURNAL   Nat Genet 44 (6), 714-719 (2012)
   PUBMED   22581229
  REMARK    GeneRIF: These results identify Ccdc103 as a dynein arm attachment
            factor that causes primary ciliary dyskinesia when mutated.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB085134.1, AC015936.14 and
            BQ448043.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.210853.1,
                                           SRR1803611.261887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..242
                     /product="dynein axonemal assembly factor 19 isoform 1"
                     /note="coiled-coil domain-containing protein 103;
                     coiled-coil domain containing 103"
                     /calculated_mol_wt=27032
     Region          7..74
                     /region_name="Dynein_attach_N"
                     /note="Dynein attachment factor N-terminus; pfam15867"
                     /db_xref="CDD:464912"
     Region          99..188
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..242
                     /gene="DNAAF19"
                     /gene_synonym="CCDC103; CILD17; PR46b; SMH"
                     /coded_by="NM_001258396.2:125..853"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11490.1"
                     /db_xref="GeneID:388389"
                     /db_xref="HGNC:HGNC:32700"
                     /db_xref="MIM:614677"
ORIGIN      
        1 merndiinfk alekelqaal tadekykren aaklraveqr vasyeefrgi vlashlkple
       61 rkdkmggkrt vpwnchtiqg rtfqdvatei spekaplqpe tsadfyrdwr rhlpsgpery
      121 qallqlggpr lgclfqtdvg fgllgellva ladhvgpadr aavlgilcsl astgrftlnl
      181 sllsraeres ckglfqklqa mgnprsvkeg lsweeqglee qsgglqeeer llqellelyq
      241 vd
//
LOCUS       NP_001091059             283 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p38 [Homo sapiens].
ACCESSION   NP_001091059
VERSION     NP_001091059.1
DBSOURCE    REFSEQ: accession NM_001097590.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Oshima,K., Kakiuchi,Y., Tanaka,Y., Ueda,T., Nakashima,T., Kimura,M.
            and Yao,M.
  TITLE     Structural basis for recognition of a kink-turn motif by an
            archaeal homologue of human RNase P protein Rpp38
  JOURNAL   Biochem Biophys Res Commun 474 (3), 541-546 (2016)
   PUBMED   27114305
  REMARK    GeneRIF: A pull-down assay further suggested the presence of a
            second K-turn in SL12. Based on the present results, together with
            available data, we discuss a structural basis for recognition of
            K-turn motifs in PhopRNA by PhoRpp38.
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Welting,T.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Mutual interactions between subunits of the human RNase MRP
            ribonucleoprotein complex
  JOURNAL   Nucleic Acids Res 32 (7), 2138-2146 (2004)
   PUBMED   15096576
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Jiang,T., Guerrier-Takada,C. and Altman,S.
  TITLE     Protein-RNA interactions in the subunits of human nuclear RNase P
  JOURNAL   RNA 7 (7), 937-941 (2001)
   PUBMED   11455963
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Jarrous,N., Wolenski,J.S., Wesolowski,D., Lee,C. and Altman,S.
  TITLE     Localization in the nucleolus and coiled bodies of protein subunits
            of the ribonucleoprotein ribonuclease P
  JOURNAL   J Cell Biol 146 (3), 559-572 (1999)
   PUBMED   10444065
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Jarrous,N., Eder,P.S., Guerrier-Takada,C., Hoog,C. and Altman,S.
  TITLE     Autoantigenic properties of some protein subunits of catalytically
            active complexes of human ribonuclease P
  JOURNAL   RNA 4 (4), 407-417 (1998)
   PUBMED   9630247
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Eder,P.S., Kekuda,R., Stolc,V. and Altman,S.
  TITLE     Characterization of two scleroderma autoimmune antigens that
            copurify with human ribonuclease P
  JOURNAL   Proc Natl Acad Sci U S A 94 (4), 1101-1106 (1997)
   PUBMED   9037013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX872398.1, BC029494.1 and AW292674.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.217714.1,
                                           SRR1163658.471773.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..283
                     /product="ribonuclease P protein subunit p38"
                     /EC_number="3.1.26.5"
                     /note="RNaseP protein p38; ribonuclease P/MRP 38kDa
                     subunit"
                     /calculated_mol_wt=31703
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Region          107..185
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     cl00600"
                     /db_xref="CDD:469835"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P78345.2)"
     CDS             1..283
                     /gene="RPP38"
                     /coded_by="NM_001097590.3:185..1036"
                     /db_xref="CCDS:CCDS7108.1"
                     /db_xref="GeneID:10557"
                     /db_xref="HGNC:HGNC:30329"
                     /db_xref="MIM:606116"
ORIGIN      
        1 maaapqapgr gslrktrplv vktslnnpyi irwsalesed mhfilqtled rlkaiglqki
       61 edkkkknktp flkkesrekc siavdisenl kekktdakqq vsgwtpahvr kqlaigvnev
      121 tralerrell lvlvcksvkp amitshliql slsrsvpacq vprlseriap viglkcvlal
      181 afkknttdfv devraiiprv pslsvpwlqd riedsgenle teplesqdre lldtsfedls
      241 kpkrkladgr qasvtlqplk ikklipnpnk irkppkskka tpk
//
LOCUS       NP_064633                 81 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-catenin-interacting protein 1 [Homo sapiens].
ACCESSION   NP_064633 XP_001128063
VERSION     NP_064633.1
DBSOURCE    REFSEQ: accession NM_020248.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Zhang,T., Zhang,Y., Xu,H., Lan,J., Feng,Z., Huang,R., Geng,J.,
            Chi,H. and Bai,X.
  TITLE     LINC00355 Mediates CTNNBIP1 Promoter Methylation and Promotes
            Endoplasmic Reticulum Stress-Induced Podocyte Injury in Diabetic
            Nephropathy
  JOURNAL   Antioxid Redox Signal 39 (4-6), 225-240 (2023)
   PUBMED   36738224
  REMARK    GeneRIF: LINC00355 Mediates CTNNBIP1 Promoter Methylation and
            Promotes Endoplasmic Reticulum Stress-Induced Podocyte Injury in
            Diabetic Nephropathy.
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Wang,Z., Hu,J., Chen,J., Zhang,J., Li,W., Tian,Y., Liu,H. and
            Yang,X.
  TITLE     ICAT promotes colorectal cancer metastasis via binding to JUP and
            activating the NF-kappaB signaling pathway
  JOURNAL   J Clin Lab Anal 36 (10), e24678 (2022)
   PUBMED   36036768
  REMARK    GeneRIF: ICAT promotes colorectal cancer metastasis via binding to
            JUP and activating the NF-kappaB signaling pathway.
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Han,H., Zhu,B., Xie,J., Huang,Y., Geng,Y., Chen,K. and Wang,W.
  TITLE     Expression level and prognostic potential of
            beta-catenin-interacting protein in acute myeloid leukemia
  JOURNAL   Medicine (Baltimore) 101 (33), e30022 (2022)
   PUBMED   35984200
  REMARK    GeneRIF: Expression level and prognostic potential of
            beta-catenin-interacting protein in acute myeloid leukemia.
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Hu,J., Wang,Z., Chen,J., Yu,Z., Zhang,J., Li,W., Lin,M., Yang,X.
            and Liu,H.
  TITLE     Overexpression of ICAT Inhibits the Progression of Colorectal
            Cancer by Binding with beta-Catenin in the Cytoplasm
  JOURNAL   Technol Cancer Res Treat 20, 15330338211041253 (2021)
   PUBMED   34569368
  REMARK    GeneRIF: Overexpression of ICAT Inhibits the Progression of
            Colorectal Cancer by Binding with beta-Catenin in the Cytoplasm.
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Reifenberger,J., Knobbe,C.B., Wolter,M., Blaschke,B., Schulte,K.W.,
            Pietsch,T., Ruzicka,T. and Reifenberger,G.
  TITLE     Molecular genetic analysis of malignant melanomas for aberrations
            of the WNT signaling pathway genes CTNNB1, APC, ICAT and BTRC
  JOURNAL   Int J Cancer 100 (5), 549-556 (2002)
   PUBMED   12124804
  REMARK    GeneRIF: Molecular genetic analysis of malignant melanomas for
            aberrations of the WNT signaling pathway genes CTNNB1, APC, ICAT
            and BTRC.
REFERENCE   7  (residues 1 to 81)
  AUTHORS   von Koch,C.S., Gulati,M., Aldape,K. and Berger,M.S.
  TITLE     Familial medulloblastoma: case report of one family and review of
            the literature
  JOURNAL   Neurosurgery 51 (1), 227-33 (2002)
   PUBMED   12182422
  REMARK    GeneRIF: presentation of medulloblastoma in two siblings (one of
            each sex) and their great-uncle; immunostaining for gene products
            in medulloblastoma differed in the two siblings for beta-catenin
            and was similar with staining for gli.
            Review article
REFERENCE   8  (residues 1 to 81)
  AUTHORS   Ashihara,K., Saito,T., Mizumoto,H., Adachi,K., Tanaka,R.,
            Nishimura,M., Ito,E. and Kudo,R.
  TITLE     Loss of gamma-Catenin expression in squamous differentiation in
            endometrial carcinomas
  JOURNAL   Int J Gynecol Pathol 21 (3), 246-254 (2002)
   PUBMED   12068170
  REMARK    GeneRIF: stimulation of beta-catenin and suppression of
            gamma-catenin expression, occur within endometrial carcinomas with
            squamous differentiation
REFERENCE   9  (residues 1 to 81)
  AUTHORS   Tutter,A.V., Fryer,C.J. and Jones,K.A.
  TITLE     Chromatin-specific regulation of LEF-1-beta-catenin transcription
            activation and inhibition in vitro
  JOURNAL   Genes Dev 15 (24), 3342-3354 (2001)
   PUBMED   11751639
REFERENCE   10 (residues 1 to 81)
  AUTHORS   Tago,K., Nakamura,T., Nishita,M., Hyodo,J., Nagai,S., Murata,Y.,
            Adachi,S., Ohwada,S., Morishita,Y., Shibuya,H. and Akiyama,T.
  TITLE     Inhibition of Wnt signaling by ICAT, a novel
            beta-catenin-interacting protein
  JOURNAL   Genes Dev 14 (14), 1741-1749 (2000)
   PUBMED   10898789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357140.33, CB995652.1 and
            BI226022.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 20, 2006 this sequence version replaced XP_001128063.1.
            
            Summary: The protein encoded by this gene binds CTNNB1 and prevents
            interaction between CTNNB1 and TCF family members. The encoded
            protein is a negative regulator of the Wnt signaling pathway. Two
            transcript variants encoding the same protein have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB021262.1, ERR279858.1749.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377263.6/ ENSP00000366474.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..81
                     /product="beta-catenin-interacting protein 1"
                     /note="beta-catenin-interacting protein ICAT; inhibitor of
                     beta-catenin and Tcf-4"
                     /calculated_mol_wt=9039
     Region          1..79
                     /region_name="ICAT"
                     /note="Beta-catenin-interacting protein ICAT; pfam06384"
                     /db_xref="CDD:399405"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJN6; propagated from
                     UniProtKB/Swiss-Prot (Q9NSA3.1)"
     CDS             1..81
                     /gene="CTNNBIP1"
                     /gene_synonym="ICAT"
                     /coded_by="NM_020248.3:319..564"
                     /db_xref="CCDS:CCDS106.1"
                     /db_xref="GeneID:56998"
                     /db_xref="HGNC:HGNC:16913"
                     /db_xref="MIM:607758"
ORIGIN      
        1 mnregapgks peemyiqqkv rvllmlrkmg snltaseeef lrtyagvvns qlsqlpphsi
       61 dqgaedvvma fsrsetedrr q
//
LOCUS       NP_689476                285 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.12st [Homo sapiens].
ACCESSION   NP_689476
VERSION     NP_689476.2
DBSOURCE    REFSEQ: accession NM_152263.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 285)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 285)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 285)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 285)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 285)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008425.1, AL590431.11,
            BC050470.1 and AJ573307.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 7, 2006 this sequence version replaced NP_689476.1.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (Tpm3.12, also known as variant 1)
            differs in the 5' and 3' UTRs and contains multiple differences in
            the coding region, compared to variant Tpm3.1. It represents use of
            an alternate promoter and initiates translation at an alternate
            start codon. The encoded isoform (Tpm3.12st, also known as Tm sk
            alpha-slow, alpha s Tm1, or isoform 1) is longer and has distinct
            N- and C- termini, compared to isoform Tpm3.1cy. Expression of the
            encoded isoform is enriched in slow-twitch skeletal muscle.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008425.1, X04201.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000651641.1/ ENSP00000498577.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..285
                     /product="tropomyosin alpha-3 chain isoform Tpm3.12st"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=32819
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000305;
                     N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:P58776; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Region          16..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P06753.2)"
     Region          49..283
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07951; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58774; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07951; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P07951; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58775; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            253
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07951; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P58775; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21107; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P07951; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21107; propagated from
                     UniProtKB/Swiss-Prot (P06753.2)"
     CDS             1..285
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_152263.4:83..940"
                     /note="isoform Tpm3.12st is encoded by transcript variant
                     Tpm3.12"
                     /db_xref="CCDS:CCDS41403.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 mmeaikkkmq mlkldkenal draeqaeaeq kqaeerskql edelaamqkk lkgtedeldk
       61 ysealkdaqe klelaekkaa daeaevasln rriqlveeel draqerlata lqkleeaeka
      121 adesergmkv ienralkdee kmelqeiqlk eakhiaeead rkyeevarkl viiegdlert
      181 eeraelaesk cseleeelkn vtnnlkslea qaekysqked kyeeeikilt dklkeaetra
      241 efaersvakl ektiddlede lyaqklkyka iseeldhaln dmtsi
//
LOCUS       NP_001229862             557 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-1 isoform d [Homo sapiens].
ACCESSION   NP_001229862
VERSION     NP_001229862.1
DBSOURCE    REFSEQ: accession NM_001242933.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Garcia Delgado,L., Derome,A., Longpre,S., Giroux-Dansereau,M.,
            Basbous,G., Lavoie,C., Saucier,C. and Denault,J.B.
  TITLE     Spatiotemporal regulation of the hepatocyte growth factor receptor
            MET activity by sorting nexins 1/2 in HCT116 colorectal cancer
            cells
  JOURNAL   Biosci Rep 44 (6) (2024)
   PUBMED   38836326
  REMARK    GeneRIF: Spatiotemporal regulation of the hepatocyte growth factor
            receptor MET activity by sorting nexins 1/2 in HCT116 colorectal
            cancer cells.
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Lopez-Robles,C., Scaramuzza,S., Astorga-Simon,E.N., Ishida,M.,
            Williamson,C.D., Banos-Mateos,S., Gil-Carton,D., Romero-Durana,M.,
            Vidaurrazaga,A., Fernandez-Recio,J., Rojas,A.L., Bonifacino,J.S.,
            Castano-Diez,D. and Hierro,A.
  TITLE     Architecture of the ESCPE-1 membrane coat
  JOURNAL   Nat Struct Mol Biol 30 (7), 958-969 (2023)
   PUBMED   37322239
REFERENCE   3  (residues 1 to 557)
  AUTHORS   Sugatha,J., Priya,A., Raj,P., Jaimon,E., Swaminathan,U., Jose,A.,
            Pucadyil,T.J. and Datta,S.
  TITLE     Insights into cargo sorting by SNX32 and its role in neurite
            outgrowth
  JOURNAL   Elife 12, e84396 (2023)
   PUBMED   37158588
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Carlton,J., Bujny,M., Peter,B.J., Oorschot,V.M., Rutherford,A.,
            Mellor,H., Klumperman,J., McMahon,H.T. and Cullen,P.J.
  TITLE     Sorting nexin-1 mediates tubular endosome-to-TGN transport through
            coincidence sensing of high- curvature membranes and
            3-phosphoinositides
  JOURNAL   Curr Biol 14 (20), 1791-1800 (2004)
   PUBMED   15498486
  REMARK    GeneRIF: SNX1 associates with a microdomain of the early endosome
            where it regulates tubular-based endosome-to-trans Golgi network
            retrieval of the cation-independent mannose-6-phosphate receptor.
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Shank,B.B., Wiley,H.S. and Kurten,R.C.
  TITLE     Structural and functional characterization of the human gene for
            sorting nexin 1 (SNX1)
  JOURNAL   DNA Cell Biol 20 (5), 287-296 (2001)
   PUBMED   11410165
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Kurten,R.C., Eddington,A.D., Chowdhury,P., Smith,R.D.,
            Davidson,A.D. and Shank,B.B.
  TITLE     Self-assembly and binding of a sorting nexin to sorting endosomes
  JOURNAL   J Cell Sci 114 (Pt 9), 1743-1756 (2001)
   PUBMED   11309204
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Chin,L.S., Raynor,M.C., Wei,X., Chen,H.Q. and Li,L.
  TITLE     Hrs interacts with sorting nexin 1 and regulates degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 276 (10), 7069-7078 (2001)
   PUBMED   11110793
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Barr,V.A., Haft,D.H. and
            Taylor,S.I.
  TITLE     Identification of a family of sorting nexin molecules and
            characterization of their association with receptors
  JOURNAL   Mol Cell Biol 18 (12), 7278-7287 (1998)
   PUBMED   9819414
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Kurten,R.C., Cadena,D.L. and Gill,G.N.
  TITLE     Enhanced degradation of EGF receptors by a sorting nexin, SNX1
  JOURNAL   Science 272 (5264), 1008-1010 (1996)
   PUBMED   8638121
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455188.1, AK128179.1,
            AC100840.2 and BX108623.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This endosomal protein regulates the cell-surface
            expression of epidermal growth factor receptor. This protein also
            has a role in sorting protease-activated receptor-1 from early
            endosomes to lysosomes. This protein may form oligomeric complexes
            with family members. This gene results in three transcript variants
            encoding distinct isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            that causes a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (d) has a distinct and longer
            C-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK128179.1, SRR1803616.97635.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..557
                     /product="sorting nexin-1 isoform d"
                     /note="sorting nexin 1A"
                     /calculated_mol_wt=62951
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          11..90
                     /region_name="Sorting_nexin"
                     /note="Sorting nexin, N-terminal domain; pfam03700"
                     /db_xref="CDD:461016"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV80; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV80; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Region          115..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          145..268
                     /region_name="PX_SNX1"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 1; cd07281"
                     /db_xref="CDD:132814"
     Site            order(186..188,238)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132814"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Site            237
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Region          281..298
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000303|PubMed:19816406"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          286..506
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(315,318..319,323,325..326,329..330,332..333,
                     343..344,346..347,350..351,353..354,357,370,373..374,479,
                     482..483,485,490,493..494,496..497,500..501,504..505)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153271"
     CDS             1..557
                     /gene="SNX1"
                     /gene_synonym="HsT17379; VPS5"
                     /coded_by="NM_001242933.2:33..1706"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58371.1"
                     /db_xref="GeneID:6642"
                     /db_xref="HGNC:HGNC:11172"
                     /db_xref="MIM:601272"
ORIGIN      
        1 masggggcsa serlpppfpg lepesegaag gsepeagdsd tegediftga avvskhqspk
       61 ittsllpinn gskengihee qdqepqdlfa datvelslds tqnnqkkvla ktlislppqe
      121 atnsskpqpt yeeleeeeqe dqfdltvgit dpekigdgmn ayvaykvttq tslplfrskq
      181 favkrrfsdf lglyeklsek hsqngfivpp ppeksligmt kvkvgkedss saeflekrra
      241 alerylqriv nhptmlqdpd vreflekeel pravgtqtls gagllkmfnk atdavskmti
      301 kmnesdiwfe eklqevecee qrlrklhavv etlvnhrkel alntaqfaks lamlgssedn
      361 talsralsql aeveekieql hqeqanndff llaellsdyi rllaivraaf dqrmktwqrw
      421 qdaqatlqkk reaearllwa nkpdklqqak deilewesrv tqyerdferi stvvrkevir
      481 fekekskdfk nhvikyletl lysqqqageq lgirsgillt kklpryskff stvhkfcaaa
      541 slwkwgffls aylsylf
//
LOCUS       NP_000208                495 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium voltage-gated channel subfamily A member 1 [Homo
            sapiens].
ACCESSION   NP_000208 XP_001133050
VERSION     NP_000208.2
DBSOURCE    REFSEQ: accession NM_000217.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Sun,W.B., Fu,J.X., Chen,Y.L., Li,H.F., Wu,Z.Y. and Chen,D.F.
  TITLE     Both gain- and loss-of-function variants of KCNA1 are associated
            with paroxysmal kinesigenic dyskinesia
  JOURNAL   J Genet Genomics 51 (8), 801-810 (2024)
   PUBMED   38570113
  REMARK    GeneRIF: Both gain- and loss-of-function variants of KCNA1 are
            associated with paroxysmal kinesigenic dyskinesia.
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Zhao,J., Petitjean,D., Haddad,G.A., Batulan,Z. and Blunck,R.
  TITLE     A Common Kinetic Property of Mutations Linked to Episodic Ataxia
            Type 1 Studied in the Shaker Kv Channel
  JOURNAL   Int J Mol Sci 21 (20), 7602 (2020)
   PUBMED   33066705
  REMARK    GeneRIF: A Common Kinetic Property of Mutations Linked to Episodic
            Ataxia Type 1 Studied in the Shaker Kv Channel.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Uhan,S., Zidar,N., Tomazic,A. and Hauptman,N.
  TITLE     Hypermethylated promoters of genes UNC5D and KCNA1 as potential
            novel diagnostic biomarkers in colorectal cancer
  JOURNAL   Epigenomics 12 (19), 1677-1688 (2020)
   PUBMED   33078631
  REMARK    GeneRIF: Hypermethylated promoters of genes UNC5D and KCNA1 as
            potential novel diagnostic biomarkers in colorectal cancer.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Browne,D.L., Gancher,S.T., Nutt,J.G., Brunt,E.R., Smith,E.A.,
            Kramer,P. and Litt,M.
  TITLE     Episodic ataxia/myokymia syndrome is associated with point
            mutations in the human potassium channel gene, KCNA1
  JOURNAL   Nat Genet 8 (2), 136-140 (1994)
   PUBMED   7842011
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Hasan,S.M. and D'Adamo,M.C.
  TITLE     Episodic Ataxia Type 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301785
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Curran,M.E., Landes,G.M. and Keating,M.T.
  TITLE     Molecular cloning, characterization, and genomic localization of a
            human potassium channel gene
  JOURNAL   Genomics 12 (4), 729-737 (1992)
   PUBMED   1349297
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Freeman,S.N., Conley,E.C., Brennand,J.C., Russell,N.J. and
            Brammar,W.J.
  TITLE     Cloning and characterization of a cDNA encoding a human brain
            potassium channel
  JOURNAL   Biochem Soc Trans 18 (5), 891-892 (1990)
   PUBMED   2128063
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA336089.1, DA236475.1 and
            AC006063.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Dec 16, 2006 this sequence version replaced
            XP_001133050.1, NP_000208.1.
            
            Summary: This gene encodes a voltage-gated delayed potassium
            channel that is phylogenetically related to the Drosophila Shaker
            channel. The encoded protein has six putative transmembrane
            segments (S1-S6), and the loop between S5 and S6 forms the pore and
            contains the conserved selectivity filter motif (GYGD). The
            functional channel is a homotetramer. The N-terminus of the channel
            is associated with beta subunits that can modify the inactivation
            properties of the channel as well as affect expression levels. The
            C-terminus of the channel is complexed to a PDZ domain protein that
            is responsible for channel targeting. Mutations in this gene have
            been associated with myokymia with periodic ataxia (AEMK).
            [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.830717.1,
                                           SRR1803621.9971.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382545.5/ ENSP00000371985.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.32"
     Protein         1..495
                     /product="potassium voltage-gated channel subfamily A
                     member 1"
                     /note="voltage-gated potassium channel subunit Kv1.1;
                     voltage-gated K(+) channel HuKI; voltage-gated potassium
                     channel HBK1; potassium voltage-gated channel,
                     shaker-related subfamily, member 1 (episodic ataxia with
                     myokymia); potassium channel, voltage gated shaker related
                     subfamily A, member 1"
                     /calculated_mol_wt=56335
     Region          1..128
                     /region_name="Tetramerization domain.
                     /evidence=ECO:0000250|UniProtKB:P10499"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10499; propagated from
                     UniProtKB/Swiss-Prot (Q09470.2)"
     Region          37..163
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Site            165..186
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Region          166..418
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q09470.2)"
     Site            221..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Region          310..323
                     /region_name="S4-S5 linker.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            324..345
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Region          372..377
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            387..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10499; propagated from
                     UniProtKB/Swiss-Prot (Q09470.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P10499; propagated from
                     UniProtKB/Swiss-Prot (Q09470.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000305|PubMed:23774215; propagated from
                     UniProtKB/Swiss-Prot (Q09470.2)"
     Region          493..495
                     /region_name="PDZ-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09470.2)"
     CDS             1..495
                     /gene="KCNA1"
                     /gene_synonym="AEMK; EA1; HBK1; HUK1; KV1.1; MBK1; MK1;
                     RBK1"
                     /coded_by="NM_000217.3:1108..2595"
                     /db_xref="CCDS:CCDS8535.1"
                     /db_xref="GeneID:3736"
                     /db_xref="HGNC:HGNC:6218"
                     /db_xref="MIM:176260"
ORIGIN      
        1 mtvmsgenvd easaapghpq dgsyprqadh ddheccervv inisglrfet qlktlaqfpn
       61 tllgnpkkrm ryfdplrney ffdrnrpsfd ailyyyqsgg rlrrpvnvpl dmfseeikfy
      121 elgeeamekf redegfikee erplpekeyq rqvwllfeyp essgparvia ivsvmvilis
      181 ivifcletlp elkddkdftg tvhridnttv iynsniftdp ffivetlcii wfsfelvvrf
      241 facpsktdff knimnfidiv aiipyfitlg teiaeqegnq kgeqatslai lrvirlvrvf
      301 rifklsrhsk glqilgqtlk asmrelglli fflfigvilf ssavyfaeae eaeshfssip
      361 dafwwavvsm ttvgygdmyp vtiggkivgs lcaiagvlti alpvpvivsn fnyfyhrete
      421 geeqaqllhv sspnlasdsd lsrrssstms kseymeieed mnnsiahyrq vnirtanctt
      481 anqncvnksk lltdv
//
LOCUS       NP_001180237             562 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001180237
VERSION     NP_001180237.1
DBSOURCE    REFSEQ: accession NM_001193308.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Wang,J., Luo,J., Wu,X. and Li,Z.
  TITLE     WTAP enhances the instability of SYTL1 mRNA caused by YTHDF2 in
            bladder cancer
  JOURNAL   Histol Histopathol 39 (5), 633-646 (2024)
   PUBMED   37933909
  REMARK    GeneRIF: WTAP enhances the instability of SYTL1 mRNA caused by
            YTHDF2 in bladder cancer.
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Wang,J., Luo,J., Wu,X. and Li,Z.
  TITLE     ELK1 suppresses SYTL1 expression by recruiting HDAC2 in bladder
            cancer progression
  JOURNAL   Hum Cell 35 (6), 1961-1975 (2022)
   PUBMED   36107384
  REMARK    GeneRIF: ELK1 suppresses SYTL1 expression by recruiting HDAC2 in
            bladder cancer progression.
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Holt,O., Kanno,E., Bossi,G., Booth,S., Daniele,T., Santoro,A.,
            Arico,M., Saegusa,C., Fukuda,M. and Griffiths,G.M.
  TITLE     Slp1 and Slp2-a localize to the plasma membrane of CTL and
            contribute to secretion from the immunological synapse
  JOURNAL   Traffic 9 (4), 446-457 (2008)
   PUBMED   18266782
  REMARK    GeneRIF: These results suggest that both Slp1 and Slp2-a may form
            part of a docking complex, capturing secretory lysosomes at the
            immunological synapse.
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Johnson,J.L., Ellis,B.A., Noack,D., Seabra,M.C. and Catz,S.D.
  TITLE     The Rab27a-binding protein, JFC1, regulates androgen-dependent
            secretion of prostate-specific antigen and prostatic-specific acid
            phosphatase
  JOURNAL   Biochem J 391 (Pt 3), 699-710 (2005)
   PUBMED   16004602
  REMARK    GeneRIF: evidence that JFC1 differentially regulates the secretion
            of PSAP and PSA, and that Rab27a and PI3K play a central role in
            the exocytosis of prostate-specific markers
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Catz,S.D., Babior,B.M. and Johnson,J.L.
  TITLE     JFC1 is transcriptionally activated by nuclear factor-kappaB and
            up-regulated by tumour necrosis factor alpha in prostate carcinoma
            cells
  JOURNAL   Biochem J 367 (Pt 3), 791-799 (2002)
   PUBMED   12137562
  REMARK    GeneRIF: transcriptional activation of JFC1 by the
            TNFalpha/NF-kappaB pathway is significant in prostate carcinoma
            cell lines
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Jfc1/synaptotagmin-like protein 1 (Slp1) contains an
            N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD of
            Slp1/Jfc1 specifically and directly binds the GTP-bound form of
            Rab27A (J. Biol. Chem. 277, (2002) 9212-9218; PMID: 11773082).
REFERENCE   10 (residues 1 to 562)
  AUTHORS   McAdara Berkowitz,J.K., Catz,S.D., Johnson,J.L., Ruedi,J.M.,
            Thon,V. and Babior,B.M.
  TITLE     JFC1, a novel tandem C2 domain-containing protein associated with
            the leukocyte NADPH oxidase
  JOURNAL   J Biol Chem 276 (22), 18855-18862 (2001)
   PUBMED   11278853
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA948740.1 and BC035725.1.
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035725.1, SRR3476690.279672.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616558.5/ ENSP00000481032.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..562
                     /product="synaptotagmin-like protein 1 isoform 1"
                     /note="NADPH oxidase-related, C2 domain-containing
                     protein; exophilin-7; synaptotagmin-like protein 1"
                     /calculated_mol_wt=61726
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYJ3.1)"
     Region          35..>99
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          62..>229
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Region          94..255
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYJ3.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYJ3.1)"
     Region          267..386
                     /region_name="C2A_SLP-1_2"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 1 and 2; cd08393"
                     /db_xref="CDD:176039"
     Region          399..555
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..562
                     /gene="SYTL1"
                     /gene_synonym="JFC1; SLP1"
                     /coded_by="NM_001193308.2:168..1856"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53286.1"
                     /db_xref="GeneID:84958"
                     /db_xref="HGNC:HGNC:15584"
                     /db_xref="MIM:608042"
ORIGIN      
        1 mpqrghpsqe glwalpslpm ahgpkpeteg lldlsfltee eqeaiagvlq rdarlrqlee
       61 grvsklrasv adpgqlkilt gdwfqearsq rhhnahfgsd lvrasmrrkk strgdqapgh
      121 dreaeaavke keegpeprlt ideapqerlr etegpdfpsp svplkasdpe easqaqedpg
      181 qgdqqvcaee adpelepasg geqeprpqqa qtkaasqile ngeeapgpdp sldrmlssss
      241 svsslnsstl sgsqmslsgd aeavqvrgsv hfalhyepga aelrvhviqc qglaaarrrr
      301 sdpyvksyll pdkqskrkta vkkrnlnpvf netlrysvpq aelqgrvlsl svwhreslgr
      361 niflgevevp ldtwdwgsep twlplqprvp pspddlpsrg llalslkyvp agsegaglpp
      421 sgelhfwvke ardllplrag sldtyvqcfv lpddsqasrq rtrvvrrsls pvfnhtmvyd
      481 gfgpadlrqa caelslwdhg alanrqlggt rlslgtgssy glqvpwmdst peekqlwqal
      541 leqpcewvdg llplrtnlap rt
//
LOCUS       NP_002802                324 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 7 [Homo sapiens].
ACCESSION   NP_002802
VERSION     NP_002802.2
DBSOURCE    REFSEQ: accession NM_002811.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Wang,J., Wang,T., Feng,Y.K., Liu,Y., Fu,B., Liu,X.T. and Wu,Q.Z.
  TITLE     Deubiquitinating enzyme PSMD7 promotes bladder cancer development:
            Involvement of RAB1A stabilization
  JOURNAL   Cell Signal 114, 110996 (2024)
   PUBMED   38040402
  REMARK    GeneRIF: Deubiquitinating enzyme PSMD7 promotes bladder cancer
            development: Involvement of RAB1A stabilization.
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Tsurumi,C., DeMartino,G.N., Slaughter,C.A., Shimbara,N. and
            Tanaka,K.
  TITLE     cDNA cloning of p40, a regulatory subunit of the human 26S
            proteasome, and a homolog of the Mov-34 gene product
  JOURNAL   Biochem Biophys Res Commun 210 (2), 600-608 (1995)
   PUBMED   7755639
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Gridley,T., Gray,D.A., Orr-Weaver,T., Soriano,P., Barton,D.E.,
            Francke,U. and Jaenisch,R.
  TITLE     Molecular analysis of the Mov 34 mutation: transcript disrupted by
            proviral integration in mice is conserved in Drosophila
  JOURNAL   Development 109 (1), 235-242 (1990)
   PUBMED   2209467
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Winkelmann,D.A. and Kahan,L.
  TITLE     Immunochemical accessibility of ribosomal protein S4 in the 30 S
            ribosome. The interaction of S4 with S5 and S12
  JOURNAL   J Mol Biol 165 (2), 357-374 (1983)
   PUBMED   6188845
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000338.2, BC012606.1 and
            CA429667.1.
            
            On Nov 27, 2002 this sequence version replaced NP_002802.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. A pseudogene has been
            identified on chromosome 17. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1146516.1,
                                           SRR3476690.1155915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219313.9/ ENSP00000219313.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..324
                     /product="26S proteasome non-ATPase regulatory subunit 7"
                     /note="Mov34 homolog; proteasome (prosome, macropain) 26S
                     subunit, non-ATPase, 7 (Mov34 homolog); proteasome subunit
                     p40; 26S proteasome regulatory subunit S12; Moloney
                     leukemia virus-34 proviral integration; 26S proteasome
                     regulatory subunit rpn8"
                     /calculated_mol_wt=36894
     Region          7..285
                     /region_name="MPN_RPN7_8"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains without
                     catalytic isopeptidase activity, found in 19S proteasomal
                     subunits Rpn7 and Rpn8; cd08062"
                     /db_xref="CDD:163693"
     Site            204
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51665.2)"
     Site            214
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51665.2)"
     Region          281..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51665.2)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P26516; propagated from
                     UniProtKB/Swiss-Prot (P51665.2)"
     Site            317
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P26516; propagated from
                     UniProtKB/Swiss-Prot (P51665.2)"
     CDS             1..324
                     /gene="PSMD7"
                     /gene_synonym="MOV34; P40; Rpn8; S12"
                     /coded_by="NM_002811.5:102..1076"
                     /db_xref="CCDS:CCDS10910.1"
                     /db_xref="GeneID:5713"
                     /db_xref="HGNC:HGNC:9565"
                     /db_xref="MIM:157970"
ORIGIN      
        1 mpelavqkvv vhplvllsvv dhfnrigkvg nqkrvvgvll gswqkkvldv snsfavpfde
       61 ddkddsvwfl dhdylenmyg mfkkvnarer ivgwyhtgpk lhkndiaine lmkrycpnsv
      121 lviidvkpkd lglpteayis veevhddgtp tsktfehvts eigaeeaeev gvehllrdik
      181 dttvgtlsqr itnqvhglkg lnsklldirs ylekvatgkl pinhqiiyql qdvfnllpdv
      241 slqefvkafy lktndqmvvv ylaslirsvv alhnlinnki anrdaekkeg qekeeskkdr
      301 kedkekdkdk eksdvkkeek kekk
//
LOCUS       NP_001308136             716 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb protein SUZ12 isoform 2 [Homo sapiens].
ACCESSION   NP_001308136 XP_005258011
VERSION     NP_001308136.1
DBSOURCE    REFSEQ: accession NM_001321207.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Hu,X., Hu,C. and Zhong,P.
  TITLE     The expression and role of SUZ12 in lung adenocarcinoma
  JOURNAL   Cancer Med 13 (19), e70190 (2024)
   PUBMED   39400513
  REMARK    GeneRIF: The expression and role of SUZ12 in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Li,L., Li,C., Cao,S., Zhou,G., Jiang,Y. and Feng,J.
  TITLE     Circ-SUZ12 Protects Cardiomyocytes from Hypoxia-Induced Dysfunction
            Through Upregulating SUZ12 Expression to Activate Wnt/beta-catenin
            Signaling Pathway
  JOURNAL   Int Heart J 64 (6), 1113-1124 (2023)
   PUBMED   37967992
  REMARK    GeneRIF: Circ-SUZ12 Protects Cardiomyocytes from Hypoxia-Induced
            Dysfunction Through Upregulating SUZ12 Expression to Activate
            Wnt/beta-catenin Signaling Pathway.
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Matsui,Y., Djekidel,M.N., Lindsay,K., Samir,P., Connolly,N., Wu,G.,
            Yang,X., Fan,Y., Xu,B. and Peng,J.C.
  TITLE     SNIP1 and PRC2 coordinate cell fates of neural progenitors during
            brain development
  JOURNAL   Nat Commun 14 (1), 4754 (2023)
   PUBMED   37553330
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Yuksel Ulker,A., Uludag Alkaya,D., Caglayan,A.O., Usluer,E.,
            Aykut,A., Aslanger,A., Vural,M. and Tuysuz,B.
  TITLE     An investigation of the etiology and follow-up findings in 35
            children with overgrowth syndromes, including biallelic SUZ12
            variant
  JOURNAL   Am J Med Genet A 191 (6), 1530-1545 (2023)
   PUBMED   36919607
  REMARK    GeneRIF: An investigation of the etiology and follow-up findings in
            35 children with overgrowth syndromes, including biallelic SUZ12
            variant.
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Kuzmichev,A., Nishioka,K., Erdjument-Bromage,H., Tempst,P. and
            Reinberg,D.
  TITLE     Histone methyltransferase activity associated with a human
            multiprotein complex containing the Enhancer of Zeste protein
  JOURNAL   Genes Dev 16 (22), 2893-2905 (2002)
   PUBMED   12435631
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Cao,R., Wang,L., Wang,H., Xia,L., Erdjument-Bromage,H., Tempst,P.,
            Jones,R.S. and Zhang,Y.
  TITLE     Role of histone H3 lysine 27 methylation in Polycomb-group
            silencing
  JOURNAL   Science 298 (5595), 1039-1043 (2002)
   PUBMED   12351676
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Weinmann,A.S., Bartley,S.M., Zhang,T., Zhang,M.Q. and Farnham,P.J.
  TITLE     Use of chromatin immunoprecipitation to clone novel E2F target
            promoters
  JOURNAL   Mol Cell Biol 21 (20), 6820-6832 (2001)
   PUBMED   11564866
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Birve,A., Sengupta,A.K., Beuchle,D., Larsson,J., Kennison,J.A.,
            Rasmuson-Lestander,A. and Muller,J.
  TITLE     Su(z)12, a novel Drosophila Polycomb group gene that is conserved
            in vertebrates and plants
  JOURNAL   Development 128 (17), 3371-3379 (2001)
   PUBMED   11546753
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Koontz,J.I., Soreng,A.L., Nucci,M., Kuo,F.C., Pauwels,P., van Den
            Berghe,H., Dal Cin,P., Fletcher,J.A. and Sklar,J.
  TITLE     Frequent fusion of the JAZF1 and JJAZ1 genes in endometrial stromal
            tumors
  JOURNAL   Proc Natl Acad Sci U S A 98 (11), 6348-6353 (2001)
   PUBMED   11371647
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC129917.6, BI668506.1,
            DR000680.1, BC018583.1 and BM975130.1.
            
            On Mar 18, 2016 this sequence version replaced XP_005258011.1.
            
            Summary: This zinc finger gene has been identified at the
            breakpoints of a recurrent chromosomal translocation reported in
            endometrial stromal sarcoma. Recombination of these breakpoints
            results in the fusion of this gene and JAZF1. The protein encoded
            by this gene contains a zinc finger domain in the C terminus of the
            coding region. [provided by RefSeq, Jul 2009].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. It encodes
            isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018583.1, DRR138512.398435.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..716
                     /product="polycomb protein SUZ12 isoform 2"
                     /note="polycomb protein SUZ12; chET 9 protein; joined to
                     JAZF1 protein; suppressor of zeste 12 protein homolog;
                     chromatin precipitated E2F target 9 protein"
                     /calculated_mol_wt=80191
     Region          82..>110
                     /region_name="ZnB-Zn_SUZ12-like"
                     /note="zinc finger-binding (ZnB) and C2H2-type zinc finger
                     (Zn) domain found in suppressor of zeste 12 protein
                     (SUZ12), and similar proteins; cl45905"
                     /db_xref="CDD:459250"
     Region          132..339
                     /region_name="C2_II_SUZ12"
                     /note="type II C2 domain found in suppressor of zeste 12
                     protein (SUZ12) and similar proteins; cd21740"
                     /db_xref="CDD:467848"
     Site            order(170..173,220..221,276,286..295)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:467848"
     Region          <400..473
                     /region_name="ZnB-Zn_SUZ12"
                     /note="zinc finger-binding (ZnB) and C2H2-type zinc finger
                     (Zn) domain found in suppressor of zeste 12 protein
                     (SUZ12) and similar proteins; cd21750"
                     /db_xref="CDD:439246"
     Region          540..661
                     /region_name="VEFS-box_SUZ12"
                     /note="VEFS (VRN2-EMF2-FIS2-Su(z)12) box found in
                     suppressor of zeste 12 protein (SUZ12) and similar
                     proteins; cd21551"
                     /db_xref="CDD:439216"
     Site            order(540..548,552,554..556,558..559,566..569,571,573,576,
                     580,582,585..587,591,594..595,598,603..609,628..632,
                     634..636,638..646,648,651..652,656,659)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:439216"
     CDS             1..716
                     /gene="SUZ12"
                     /gene_synonym="CHET9; IMMAS; JJAZ1"
                     /coded_by="NM_001321207.2:241..2391"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82101.1"
                     /db_xref="GeneID:23512"
                     /db_xref="HGNC:HGNC:17101"
                     /db_xref="MIM:606245"
ORIGIN      
        1 mapqkhgggg gggsgpsags ggggfggsaa vaaatasggk sgggscgggg sysasssssa
       61 aaaagaavlp vkkpkmehvq adhelflqaf ekptqiyrfl rtrnliapif lhrtltymsh
      121 rnsrtniksl sahlqltftg ffhkndkpsp nseneqnsvt levllvkvch kkrkdvscpi
      181 rqvptgkkqv plnpdlnqtk pgnfpslavs snefepsnsh mvksysllfr vtrpgrrefn
      241 gmingetnen idvneelpar rkrnredgek tfvaqmtvfd knrrlqlldg eyevamqeme
      301 ecpiskkrat wetildgkrl ppfetfsqgp tlqftlrwtg etndkstapi akplatrnse
      361 slhqenkpgs vkptqtiavk eslttdlqtr kekdtpnenr qklrifyqfl ynnntrqqte
      421 arddlhcpwc tlncrklysl lkhlklchsr fifnyvyhpk garidvsine cydgsyagnp
      481 qdihrqpgfa fsrngpvkrt pithilvcrp krtkasmsef lesedgeveq qrtyssghnr
      541 lyfhsdtclp lrpqemevds edekdpewlr ektitqieef sdvnegekev mklwnlhvmk
      601 hgfiadnqmn hacmlfveny gqkiikknlc rnfmlhlvsm hdfnlisims idkavtklre
      661 mqqklekges aspaneeite eqngtangfs einskekale tdsvsgvskq skkqkl
//
LOCUS       NP_001340029             283 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            4 [Homo sapiens].
ACCESSION   NP_001340029 XP_016880361
VERSION     NP_001340029.1
DBSOURCE    REFSEQ: accession NM_001353100.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            On Jun 29, 2017 this sequence version replaced XP_016880361.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.262848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..283
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 4"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=31191
     Region          <1..52
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          93..277
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..283
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353100.2:601..1452"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS58527.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mellimvyac ktscaksiig vipyfpyskq ckmrkrgsiv skllasmmck aglthlitmd
       61 lhqkeiqgff nipvdnlras pfllqyiqee ipdyrnaviv akspasakra qsfaerlrlg
      121 iavihgeaqd aesdlvdgrh sppmvrsvaa ihpsleipml ipkekppitv vgdvggriai
      181 ivddiiddvd sflaaaetlk ergaykifvm athgllssda prrieesaid evvvtntiph
      241 evqklqcpki ktvdismils eairrihnge smsylfrnig ldd
//
LOCUS       NP_057663                282 aa            linear   PRI 20-NOV-2025
DEFINITION  CD320 antigen isoform 1 precursor [Homo sapiens].
ACCESSION   NP_057663
VERSION     NP_057663.1
DBSOURCE    REFSEQ: accession NM_016579.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   McCaddon,A., Carr,D.F., Peter,H., Moat,S.J. and Quadros,E.V.
  TITLE     Transcobalamin receptor gene polymorphisms and mutation in an
            elderly population
  JOURNAL   Clin Nutr ESPEN 55, 425-427 (2023)
   PUBMED   37202078
  REMARK    GeneRIF: Transcobalamin receptor gene polymorphisms and mutation in
            an elderly population.
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Pangilinan,F., Watkins,D., Bernard,D., Chen,Y., Dong,N., Wu,Q.,
            Ozel-Abaan,H., Kaur,M., Caggana,M., Morrissey,M., Browne,M.L.,
            Mills,J.L., Van Ryzin,C., Shchelochkov,O., Sloan,J., Venditti,C.P.,
            Sarafoglou,K., Rosenblatt,D.S., Kay,D.M. and Brody,L.C.
  TITLE     Probing the functional consequence and clinical relevance of CD320
            p.E88del, a variant in the transcobalamin receptor gene
  JOURNAL   Am J Med Genet A 188 (4), 1124-1141 (2022)
   PUBMED   35107211
  REMARK    GeneRIF: Probing the functional consequence and clinical relevance
            of CD320 p.E88del, a variant in the transcobalamin receptor gene.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Boachie,J., Adaikalakoteswari,A., Goljan,I., Samavat,J.,
            Cagampang,F.R. and Saravanan,P.
  TITLE     Intracellular and Tissue Levels of Vitamin B12 in Hepatocytes Are
            Modulated by CD320 Receptor and TCN2 Transporter
  JOURNAL   Int J Mol Sci 22 (6), 3089 (2021)
   PUBMED   33803025
  REMARK    GeneRIF: Intracellular and Tissue Levels of Vitamin B12 in
            Hepatocytes Are Modulated by CD320 Receptor and TCN2 Transporter.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Gick,G.G., Arora,K., Sequeira,J.M., Nakayama,Y., Lai,S.C. and
            Quadros,E.V.
  TITLE     Cellular uptake of vitamin B12: Role and fate of TCblR/CD320, the
            transcobalamin receptor
  JOURNAL   Exp Cell Res 396 (1), 112256 (2020)
   PUBMED   32898552
  REMARK    GeneRIF: Cellular uptake of vitamin B12: Role and fate of
            TCblR/CD320, the transcobalamin receptor.
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Zhang,X., Li,L., Jung,J., Xiang,S., Hollmann,C. and Choi,Y.S.
  TITLE     The distinct roles of T cell-derived cytokines and a novel
            follicular dendritic cell-signaling molecule 8D6 in germinal
            center-B cell differentiation
  JOURNAL   J Immunol 167 (1), 49-56 (2001)
   PUBMED   11418631
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Acierno,J.S. Jr., Kennedy,J.C., Falardeau,J.L., Leyne,M.,
            Bromley,M.C., Colman,M.W., Sun,M., Bove,C., Ashworth,L.K.,
            Chadwick,L.H., Schiripo,T., Ma,S., Goldin,E., Schiffmann,R. and
            Slaugenhaupt,S.A.
  TITLE     A physical and transcript map of the MCOLN1 gene region on human
            chromosome 19p13.3-p13.2
  JOURNAL   Genomics 73 (2), 203-210 (2001)
   PUBMED   11318610
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Li,L., Zhang,X., Kovacic,S., Long,A.J., Bourque,K., Wood,C.R. and
            Choi,Y.S.
  TITLE     Identification of a human follicular dendritic cell molecule that
            stimulates germinal center B cell growth
  JOURNAL   J Exp Med 191 (6), 1077-1084 (2000)
   PUBMED   10727470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010323.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the transcobalamin receptor that is
            expressed at the cell surface. It mediates the cellular uptake of
            transcobalamin bound cobalamin (vitamin B12), and is involved in
            B-cell proliferation and immunoglobulin secretion. Mutations in
            this gene are associated with methylmalonic aciduria. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.167666.1, AF161254.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301458.10/ ENSP00000301458.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..282
                     /product="CD320 antigen isoform 1 precursor"
                     /note="8D6 antigen; CD320 antigen; FDC-SM-8D6;
                     transcobalamin receptor; FDC-signaling molecule 8D6;
                     transcobalamin 2 receptor; soluble CD320"
                     /calculated_mol_wt=25570
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3439
     mat_peptide     31..282
                     /product="CD320 antigen isoform 1"
                     /calculated_mol_wt=26026
     Region          54..89
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(59,68,79..80)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(72,75,79,85..86)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            82..86
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     Region          132..167
                     /region_name="LDLa"
                     /note="Low Density Lipoprotein Receptor Class A domain, a
                     cysteine-rich repeat that plays a central role in
                     mammalian cholesterol metabolism; the receptor protein
                     binds LDL and transports it into cells by endocytosis; 7
                     successive cysteine-rich repeats of about...; cd00112"
                     /db_xref="CDD:238060"
     Site            order(137,146,157..158)
                     /site_type="active"
                     /note="putative binding surface [active]"
                     /db_xref="CDD:238060"
     Site            order(150,153,157,163..164)
                     /site_type="other"
                     /note="calcium-binding site [ion binding]"
                     /db_xref="CDD:238060"
     Site            160..164
                     /site_type="other"
                     /note="D-X-S-D-E motif"
                     /db_xref="CDD:238060"
     CDS             1..282
                     /gene="CD320"
                     /gene_synonym="8D6; 8D6A; sCD320; TCBLR; TCII-R; TCN2R"
                     /coded_by="NM_016579.4:69..917"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12198.1"
                     /db_xref="GeneID:51293"
                     /db_xref="HGNC:HGNC:16692"
                     /db_xref="MIM:606475"
ORIGIN      
        1 msggwmaqvg awrtgalgla lllllglglg leaaasplst ptsaqaagps sgscpptkfq
       61 crtsglcvpl twrcdrdldc sdgsdeeecr iepctqkgqc ppppglpcpc tgvsdcsggt
      121 dkklrncsrl aclagelrct lsddcipltw rcdghpdcpd ssdelgcgtn eilpegdatt
      181 mgppvtlesv tslrnattmg ppvtlesvps vgnatsssag dqsgsptayg viaaaavlsa
      241 slvtatllll swlraqerlr plgllvamke slllseqkts lp
//
LOCUS       NP_001269339             280 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1 regulatory subunit 7 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001269339 XP_005247089
VERSION     NP_001269339.1
DBSOURCE    REFSEQ: accession NM_001282410.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Jiang,Y., Scott,K.L., Kwak,S.J., Chen,R. and Mardon,G.
  TITLE     Sds22/PP1 links epithelial integrity and tumor suppression via
            regulation of myosin II and JNK signaling
  JOURNAL   Oncogene 30 (29), 3248-3260 (2011)
   PUBMED   21399659
  REMARK    GeneRIF: human Sds22 is focally deleted and downregulated in
            multiple carcinomas, and this downregulation correlates with tumor
            progression, suggesting that sds22 inactivation may contribute to
            tumorigenesis and metastatic potential
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Posch,M., Khoudoli,G.A., Swift,S., King,E.M., Deluca,J.G. and
            Swedlow,J.R.
  TITLE     Sds22 regulates aurora B activity and microtubule-kinetochore
            interactions at mitosis
  JOURNAL   J Cell Biol 191 (1), 61-74 (2010)
   PUBMED   20921135
  REMARK    GeneRIF: Sds22 specifically defines protein phosphatase 1 function
            and localization in mitosis.
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Lesage,B., Beullens,M., Pedelini,L., Garcia-Gimeno,M.A.,
            Waelkens,E., Sanz,P. and Bollen,M.
  TITLE     A complex of catalytically inactive protein phosphatase-1
            sandwiched between Sds22 and inhibitor-3
  JOURNAL   Biochemistry 46 (31), 8909-8919 (2007)
   PUBMED   17630778
  REMARK    GeneRIF: Sds22 and Inhibitor-3 form a heterotrimeric complex with
            PP1, both in cell lysates and after purification. A pool of PP1 is
            complexly controlled by both Sds22 and Inhibitor-3.
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Ceulemans,H., Vulsteke,V., De Maeyer,M., Tatchell,K., Stalmans,W.
            and Bollen,M.
  TITLE     Binding of the concave surface of the Sds22 superhelix to the alpha
            4/alpha 5/alpha 6-triangle of protein phosphatase-1
  JOURNAL   J Biol Chem 277 (49), 47331-47337 (2002)
   PUBMED   12226088
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Ceulemans,H., Van Eynde,A., Perez-Callejon,E., Beullens,M.,
            Stalmans,W. and Bollen,M.
  TITLE     Structure and splice products of the human gene encoding sds22, a
            putative mitotic regulator of protein phosphatase-1
  JOURNAL   Eur J Biochem 262 (1), 36-42 (1999)
   PUBMED   10231361
REFERENCE   9  (residues 1 to 280)
  AUTHORS   Renouf,S., Beullens,M., Wera,S., Van Eynde,A., Sikela,J.,
            Stalmans,W. and Bollen,M.
  TITLE     Molecular cloning of a human polypeptide related to yeast sds22, a
            regulator of protein phosphatase-1
  JOURNAL   FEBS Lett 375 (1-2), 75-78 (1995)
   PUBMED   7498485
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Berry,R., Stevens,T.J., Walter,N.A., Wilcox,A.S., Rubano,T.,
            Hopkins,J.A., Weber,J., Goold,R., Soares,M.B. and Sikela,J.M.
  TITLE     Gene-based sequence-tagged-sites (STSs) as the basis for a human
            gene map
  JOURNAL   Nat Genet 10 (4), 415-423 (1995)
   PUBMED   7670491
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051689.1, AC005237.2 and
            BC013001.2.
            
            On Sep 7, 2013 this sequence version replaced XP_005247089.1.
            
            Summary: This gene encodes a protein subunit that regulates the
            activity of the serine/threonine phosphatase, protein
            phosphatase-1. The encoded protein is required for completion of
            the mitotic cycle and for targeting protein phosphatase-1 to
            mitotic kinetochores. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (3) differs in the 3' structure
            resulting in a novel 3' coding region and 3' UTR compared to
            variant 1. The encoded protein (isoform 3, also known as
            sds22beta1) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013001.2, SRR1163655.279429.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..280
                     /product="protein phosphatase 1 regulatory subunit 7
                     isoform 3"
                     /note="protein phosphatase 1 regulatory subunit 22;
                     protein phosphatase 1, regulatory (inhibitor) subunit 7;
                     testis secretory sperm-binding protein Li 210a"
                     /calculated_mol_wt=31922
     Region          1..64
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q15435.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15435.1)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15435.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15435.1)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15435.1)"
     Region          77..98
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          97..>272
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          99..120
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          100..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          121..142
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          122..143
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          143..164
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          144..165
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          165..186
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          166..187
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          187..208
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          188..209
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          209..230
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          210..231
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          231..252
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15435.1)"
     Region          232..253
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..280
                     /gene="PPP1R7"
                     /gene_synonym="SDS22"
                     /coded_by="NM_001282410.1:839..1681"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS63192.1"
                     /db_xref="GeneID:5510"
                     /db_xref="HGNC:HGNC:9295"
                     /db_xref="MIM:602877"
ORIGIN      
        1 maaergagqq qsqemmevdr rveseesgde egkkhssgiv adlseqslkd geergeedpe
       61 eehelpvdme tinldrdaed vdlnhyrigk iegfevlkkv ktlclrqnli kcienleelq
      121 slreldlydn qikkienlea lteleildis fnllrniegv dkltrlkklf lvnnkiskie
      181 nlsnlhqlqm lelgsnrira ienidtltnl eslflgknki tklqnldalt nltvlsmqsn
      241 rltkieglqn lvnlrelyls hngieviegl ennvqdslty
//
LOCUS       NP_116277               1860 aa            linear   PRI 20-NOV-2025
DEFINITION  collagen alpha-1(XXVII) chain preproprotein [Homo sapiens].
ACCESSION   NP_116277
VERSION     NP_116277.2
DBSOURCE    REFSEQ: accession NM_032888.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1860)
  AUTHORS   Satoh,C., Kondoh,T., Shimizu,H., Kinoshita,A., Mishima,H.,
            Nishimura,G., Miyazaki,M., Okano,K., Kumai,Y. and Yoshiura,K.I.
  TITLE     Brothers with novel compound heterozygous mutations in COL27A1
            causing dental and genital abnormalities
  JOURNAL   Eur J Med Genet 64 (2), 104125 (2021)
   PUBMED   33359165
  REMARK    GeneRIF: Brothers with novel compound heterozygous mutations in
            COL27A1 causing dental and genital abnormalities.
REFERENCE   2  (residues 1 to 1860)
  AUTHORS   Gonzaga-Jauregui,C., Yesil,G., Nistala,H., Gezdirici,A., Bayram,Y.,
            Nannuru,K.C., Pehlivan,D., Yuan,B., Jimenez,J., Sahin,Y.,
            Paine,I.S., Akdemir,Z.C., Rajamani,S., Staples,J., Dronzek,J.,
            Howell,K., Fatih,J.M., Smaldone,S., Schlesinger,A.E., Ramirez,N.,
            Cornier,A.S., Kelly,M.A., Haber,R., Chim,S.M., Nieman,K., Wu,N.,
            Walls,J., Poueymirou,W., Siao,C.J., Sutton,V.R., Williams,M.S.,
            Posey,J.E., Gibbs,R.A., Carlo,S., Tegay,D.H., Economides,A.N. and
            Lupski,J.R.
  CONSRTM   Baylor-Hopkins Center for Mendelian Genetics, Regeneron Genetics
            Center
  TITLE     Functional biology of the Steel syndrome founder allele and
            evidence for clan genomics derivation of COL27A1 pathogenic alleles
            worldwide
  JOURNAL   Eur J Hum Genet 28 (9), 1243-1264 (2020)
   PUBMED   32376988
  REMARK    GeneRIF: Functional biology of the Steel syndrome founder allele
            and evidence for clan genomics derivation of COL27A1 pathogenic
            alleles worldwide.
REFERENCE   3  (residues 1 to 1860)
  AUTHORS   Evie,Kritioti., Athina,Theodosiou., Nayia,Nicolaou.,
            Angelos,Alexandrou., Ioannis,Papaevripidou., Elisavet,Efstathiou.,
            Violetta,Christophidou.-Anastasiadou., Carolina,Sismani. and
            Tanteles,G.A.
  TITLE     First reported case of Steel syndrome in the European population: A
            novel homozygous mutation in COL27A1 and review of the literature
  JOURNAL   Eur J Med Genet 63 (7), 103939 (2020)
   PUBMED   32360765
  REMARK    GeneRIF: First reported case of Steel syndrome in the European
            population: A novel homozygous mutation in COL27A1 and review of
            the literature.
            Review article
REFERENCE   4  (residues 1 to 1860)
  AUTHORS   Amlie-Wolf,L., Moyer-Harasink,S., Carr,A.M., Giampietro,P.,
            Schneider,A. and Simon,M.
  TITLE     Three new patients with Steel syndrome and a Puerto Rican specific
            COL27A1 mutation
  JOURNAL   Am J Med Genet A 182 (4), 798-803 (2020)
   PUBMED   31903681
  REMARK    GeneRIF: Three new patients with Steel syndrome and a Puerto Rican
            specific COL27A1 mutation.
REFERENCE   5  (residues 1 to 1860)
  AUTHORS   Meng,W., Adams,M.J., Palmer,C.N.A., Shi,J., Auton,A., Ryan,K.A.,
            Jordan,J.M., Mitchell,B.D., Jackson,R.D., Yau,M.S., McIntosh,A.M.
            and Smith,B.H.
  CONSRTM   23andMe Research Team
  TITLE     Genome-wide association study of knee pain identifies associations
            with GDF5 and COL27A1 in UK Biobank
  JOURNAL   Commun Biol 2, 321 (2019)
   PUBMED   31482140
  REMARK    GeneRIF: two loci in or near GDF5 and COL27A1 that are associated
            with knee pain, were identified.
            Erratum:[Commun Biol. 2020 Mar 26;3(1):149. doi:
            10.1038/s42003-020-0880-x. PMID: 32218487]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1860)
  AUTHORS   Vieira,A.R., McHenry,T.G., Daack-Hirsch,S., Murray,J.C. and
            Marazita,M.L.
  TITLE     Candidate gene/loci studies in cleft lip/palate and dental
            anomalies finds novel susceptibility genes for clefts
  JOURNAL   Genet Med 10 (9), 668-674 (2008)
   PUBMED   18978678
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1860)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   8  (residues 1 to 1860)
  AUTHORS   Jenkins,E., Moss,J.B., Pace,J.M. and Bridgewater,L.C.
  TITLE     The new collagen gene COL27A1 contains SOX9-responsive enhancer
            elements
  JOURNAL   Matrix Biol 24 (3), 177-184 (2005)
   PUBMED   15922909
  REMARK    GeneRIF: SOX9 may play an important role in the transcriptional
            activation of the newest collagen gene, COL27A1.
REFERENCE   9  (residues 1 to 1860)
  AUTHORS   Boot-Handford,R.P., Tuckwell,D.S., Plumb,D.A., Rock,C.F. and
            Poulsom,R.
  TITLE     A novel and highly conserved collagen (pro(alpha)1(XXVII)) with a
            unique expression pattern and unusual molecular characteristics
            establishes a new clade within the vertebrate fibrillar collagen
            family
  JOURNAL   J Biol Chem 278 (33), 31067-31077 (2003)
   PUBMED   12766169
  REMARK    GeneRIF: type XXVII collagen has unusual molecular features such as
            no minor helical domain, a major helical domain that is short and
            interrupted, and a short chain selection sequence within the NC1
            domain
REFERENCE   10 (residues 1 to 1860)
  AUTHORS   Pace,J.M., Corrado,M., Missero,C. and Byers,P.H.
  TITLE     Identification, characterization and expression analysis of a new
            fibrillar collagen gene, COL27A1
  JOURNAL   Matrix Biol 22 (1), 3-14 (2003)
   PUBMED   12714037
  REMARK    GeneRIF: molecular cloning
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445543.20, BU076480.1,
            BC035728.1, AY149237.1, AL356796.16 and AI808820.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 22, 2003 this sequence version replaced NP_116277.1.
            
            Summary: This gene encodes a member of the fibrillar collagen
            family, and plays a role during the calcification of cartilage and
            the transition of cartilage to bone. The encoded protein product is
            a preproprotein. It includes an N-terminal signal peptide, which is
            followed by an N-terminal propetide, mature peptide and a
            C-terminal propeptide. The N-terminal propeptide contains
            thrombospondin N-terminal-like and laminin G-like domains. The
            mature peptide is a major triple-helical region. The C-terminal
            propeptide, also known as COLFI domain, plays crucial roles in
            tissue growth and repair. Mutations in this gene cause Steel
            syndrome. Alternatively spliced transcript variants have been
            found, but the full-length nature of some variants has not been
            determined. [provided by RefSeq, Sep 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY149237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356083.8/ ENSP00000348385.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1860
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..1860
                     /product="collagen alpha-1(XXVII) chain preproprotein"
                     /note="collagen alpha-1(XXVII) chain; collagen, type
                     XXVII, alpha 1"
                     /calculated_mol_wt=182957
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3955
     proprotein      42..1860
                     /product="collagen alpha-1(XXVII) chain proprotein"
                     /calculated_mol_wt=182957
     Region          45..220
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cl22861"
                     /db_xref="CDD:473984"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <274..605
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          278..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     mat_peptide     625..1621
                     /product="Collagen alpha-1(XXVII) chain.
                     /id=PRO_5000089163"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
                     /calculated_mol_wt=94791
     Region          625..1618
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          625..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <709..>989
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          851..1625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZC6.1)"
     Region          <974..>1249
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1183..>1449
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1369..>1598
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1661..1859
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; cl02436"
                     /db_xref="CDD:470578"
     Site            1769
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZC6.1)"
     CDS             1..1860
                     /gene="COL27A1"
                     /gene_synonym="STLS"
                     /coded_by="NM_032888.4:415..5997"
                     /db_xref="CCDS:CCDS6802.1"
                     /db_xref="GeneID:85301"
                     /db_xref="HGNC:HGNC:22986"
                     /db_xref="MIM:608461"
ORIGIN      
        1 mgagsargar gtaaaaaarg ggflfswilv sfachlastq gapedvdilq rlglswtkag
       61 spappgvipf qsgfiftqra rlqaptgtvi paalgtelal vlslcshrvn haflfavrsq
      121 krklqlglqf lpgktvvhlg srrsvafdld mhdgrwhhla lelrgrtvtl vtacgqrrvp
      181 vllpfhrdpa ldpggsflfg kmnphavqfe galcqfsiyp vtqvahnyct hlrkqcgqad
      241 tyqsplgplf sqdsgrpftf qsdlallgle nlttatpalg slpagrgprg tvapatptkp
      301 qrtsptnphq hmavggpaqt pllpaklsas naldpmlpas vggstrtprp aaaqpsqkit
      361 atkipkslpt kpsapstsiv piksphptqk tapssftksa lptqkqvppt srpvparvsr
      421 paekpiqrnp gmprppppst rplppttsss kkpiptlart eakitshask pasartsthk
      481 pppftalsss paptpgstrs trppatmvpp tsgtstprta pavptpgsap tgskkpigse
      541 askkagpkss prkpvplrpg kaardvplsd lttrpsprqp qpsqqttpal vlapaqflss
      601 sprptssgys ifhlagstpf pllmgppgpk gdcglpgppg lpglpgipga rgprgppgpy
      661 gnpglpgppg akgqkgdpgl spgkahdgak gdmglpglsg npgppgrkgh kgypgpaghp
      721 geqgqpgpeg spgakgypgr qglpgpvgdp gpkgsrgyig lpglfglpgs dgerglpgvp
      781 gkrgkmgmpg fpgvfgergp pgldgnpgel glpgppgvpg ligdlgvlgp igypgpkgmk
      841 glmgsvgepg lkgdkgeqgv pgvsgdpgfq gdkgsqglpg fpgargkpgp lgkvgdkgsi
      901 gfpgppgpeg fpgdigppgd ngpegmkgkp garglpgprg qlgpegdegp mgppgapgle
      961 gqpgrkgfpg rpgldgvkge pgdpgrpgpv geqgfmgfig lvgepgivge kgdrgmmgpp
     1021 gvpgpkgsmg hpgmpggmgt pgepgpqgpp gsrgppgmrg akgrrgprgp dgpageqgsr
     1081 glkgppgpqg rpgrpgqqgv agerghlgsr gfpgipgpsg ppgtkglpge pgpqgpqgpi
     1141 gppgemgpkg ppgavgepgl pgeagmkgdl gplgtpgeqg ligqrgepgl egdsgpmgpd
     1201 glkgdrgdpg pdgehgekgq eglmgedgpp gppgvtgvrg pegksgkqge kgrtgakgak
     1261 gyqgqlgemg vpgdpgppgt pgpkgsrgsl gptgapgrmg aqgepglagy dghkgivgpl
     1321 gppgpkgekg eqgedgkaeg ppgppgdrgp vgdrgdrgep gdpgypgqeg vqglrgkpgq
     1381 qgqpghpgpr gwpgpkgskg aegpkgkqgk agapgrrgvq glqglpgprg vvgrqglegi
     1441 agpdglpgrd gqagqqgeqg ddgdpgpmgp agkrgnpgva glpgaqgppg fkgesglpgq
     1501 lgppgkrgte grtglpgnqg epgskgqpgd sgemgfpgma glfgpkgppg digfkgiqgp
     1561 rgppglmgke givgplgilg psglpgpkgd kgsrgdwglq gprgppgprg rpgppgppgg
     1621 piqlqqddlg aafqtwmdts galrpesysy pdrlvldqgg eifktlhyls nliqsiktpl
     1681 gtkenparvc rdlmdceqkm vdgtywvdpn lgcssdtiev scnfthggqt clkpitaskv
     1741 efaisrvqmn flhllssevt qhitihclnm tvwqegtgqt pakqavrfra wngqifeagg
     1801 qfrpevsmdg ckvqdgrwhq tlftfrtqdp qqlpiisvdn lppassgkqy rlevgpacfl
//
LOCUS       NP_004512                963 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-1 heavy chain [Homo sapiens].
ACCESSION   NP_004512
VERSION     NP_004512.1
DBSOURCE    REFSEQ: accession NM_004521.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Marom,R., Zhang,B., Washington,M.E., Song,I.W., Burrage,L.C.,
            Rossi,V.C., Berrier,A.S., Lindsey,A., Lesinski,J., Nonet,M.L.,
            Chen,J., Baldridge,D., Silverman,G.A., Sutton,V.R., Rosenfeld,J.A.,
            Tran,A.A., Hicks,M.J., Murdock,D.R., Dai,H., Weis,M.,
            Jhangiani,S.N., Muzny,D.M., Gibbs,R.A., Caswell,R., Pottinger,C.,
            Cilliers,D., Stals,K., Eyre,D., Krakow,D., Schedl,T., Pak,S.C. and
            Lee,B.H.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Dominant negative variants in KIF5B cause osteogenesis imperfecta
            via down regulation of mTOR signaling
  JOURNAL   PLoS Genet 19 (11), e1011005 (2023)
   PUBMED   37934770
  REMARK    GeneRIF: Dominant negative variants in KIF5B cause osteogenesis
            imperfecta via down regulation of mTOR signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Tunganuntarat,J., Kanjanasirirat,P., Khumpanied,T.,
            Benjaskulluecha,S., Wongprom,B., Palaga,T., Siregar,T.A.P.,
            Borwornpinyo,S., Chaiprasert,A., Palittapongarnpim,P. and
            Ponpuak,M.
  TITLE     BORC complex specific components and Kinesin-1 mediate autophagy
            evasion by the autophagy-resistant Mycobacterium tuberculosis
            Beijing strain
  JOURNAL   Sci Rep 13 (1), 1663 (2023)
   PUBMED   36717601
  REMARK    GeneRIF: BORC complex specific components and Kinesin-1 mediate
            autophagy evasion by the autophagy-resistant Mycobacterium
            tuberculosis Beijing strain.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Tanaka,Y., Kanai,Y., Okada,Y., Nonaka,S., Takeda,S., Harada,A. and
            Hirokawa,N.
  TITLE     Targeted disruption of mouse conventional kinesin heavy chain,
            kif5B, results in abnormal perinuclear clustering of mitochondria
  JOURNAL   Cell 93 (7), 1147-1158 (1998)
   PUBMED   9657148
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Rahman,A., Friedman,D.S. and Goldstein,L.S.
  TITLE     Two kinesin light chain genes in mice. Identification and
            characterization of the encoded proteins
  JOURNAL   J Biol Chem 273 (25), 15395-15403 (1998)
   PUBMED   9624122
  REMARK    Erratum:[J Biol Chem 1998 Sep 11;273(37):24280]
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Kull,F.J., Sablin,E.P., Lau,R., Fletterick,R.J. and Vale,R.D.
  TITLE     Crystal structure of the kinesin motor domain reveals a structural
            similarity to myosin
  JOURNAL   Nature 380 (6574), 550-555 (1996)
   PUBMED   8606779
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Niclas,J., Navone,F., Hom-Booher,N. and Vale,R.D.
  TITLE     Cloning and localization of a conventional kinesin motor expressed
            exclusively in neurons
  JOURNAL   Neuron 12 (5), 1059-1072 (1994)
   PUBMED   7514426
REFERENCE   10 (residues 1 to 963)
  AUTHORS   Navone,F., Niclas,J., Hom-Booher,N., Sparks,L., Bernstein,H.D.,
            McCaffrey,G. and Vale,R.D.
  TITLE     Cloning and expression of a human kinesin heavy chain gene:
            interaction of the COOH-terminal domain with cytoplasmic
            microtubules in transfected CV-1 cells
  JOURNAL   J Cell Biol 117 (6), 1263-1275 (1992)
   PUBMED   1607388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP361225.1, DC399931.1, BC065267.1, X65873.1, AL161932.15 and
            BU633712.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.674711.1,
                                           SRR14038193.375442.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302418.5/ ENSP00000307078.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.22"
     Protein         1..963
                     /product="kinesin-1 heavy chain"
                     /note="kinesin 1 (110-120kD); kinesin heavy chain;
                     ubiquitous kinesin heavy chain; conventional kinesin heavy
                     chain; epididymis secretory protein Li 61"
                     /calculated_mol_wt=109554
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P33176.1)"
     Region          6..325
                     /region_name="KISc_KHC_KIF5"
                     /note="Kinesin motor domain, kinesin heavy chain (KHC) or
                     KIF5-like subgroup; cd01369"
                     /db_xref="CDD:276820"
     Site            order(16,85,88,90..93,231)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276820"
     Site            order(156..158,161,274,278..279)
                     /site_type="other"
                     /note="beta tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Site            order(157..159,161,237..239,248,252,256,274,279)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276820"
     Site            order(235,237..238,252,255..256,259)
                     /site_type="other"
                     /note="alpha tubulin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:276820"
     Region          <414..803
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          834..903
                     /region_name="Khc_CBD_cc"
                     /note="cargo binding coiled-coil domain found in kinesin
                     heavy chains; cd23649"
                     /db_xref="CDD:467880"
     Region          908..963
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P33176.1)"
     Region          915..963
                     /region_name="Globular"
                     /note="propagated from UniProtKB/Swiss-Prot (P33176.1)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P33176.1)"
     Site            956
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P33176.1)"
     CDS             1..963
                     /gene="KIF5B"
                     /gene_synonym="HEL-S-61; KINH; KNS; KNS1; UKHC"
                     /coded_by="NM_004521.3:453..3344"
                     /db_xref="CCDS:CCDS7171.1"
                     /db_xref="GeneID:3799"
                     /db_xref="HGNC:HGNC:6324"
                     /db_xref="MIM:602809"
ORIGIN      
        1 madlaecnik vmcrfrplne sevnrgdkyi akfqgedtvv iaskpyafdr vfqsstsqeq
       61 vyndcakkiv kdvlegyngt ifaygqtssg kthtmegklh dpegmgiipr ivqdifnyiy
      121 smdenlefhi kvsyfeiyld kirdlldvsk tnlsvhedkn rvpyvkgcte rfvcspdevm
      181 dtidegksnr hvavtnmneh ssrshsifli nvkqentqte qklsgklylv dlagsekvsk
      241 tgaegavlde akninkslsa lgnvisalae gstyvpyrds kmtrilqdsl ggncrttivi
      301 ccspssynes etkstllfgq raktikntvc vnveltaeqw kkkyekekek nkilrntiqw
      361 lenelnrwrn getvpideqf dkekanleaf tvdkditltn dkpataigvi gnftdaerrk
      421 ceeeiaklyk qlddkdeein qqsqlveklk tqmldqeell astrrdqdnm qaelnrlqae
      481 ndaskeevke vlqaleelav nydqksqeve dktkeyells delnqksatl asidaelqkl
      541 kemtnhqkkr aaemmasllk dlaeigiavg nndvkqpegt gmideeftva rlyiskmkse
      601 vktmvkrckq lestqtesnk kmeenekela acqlrisqhe akikslteyl qnveqkkrql
      661 eesvdalsee lvqlraqekv hemekehlnk vqtanevkqa veqqiqshre thqkqisslr
      721 deveakakli tdlqdqnqkm mleqerlrve heklkatdqe ksrklheltv mqdrreqarq
      781 dlkgleetva kelqtlhnlr klfvqdlatr vkksaeidsd dtggsaaqkq kisflennle
      841 qltkvhkqlv rdnadlrcel pklekrlrat aervkalesa lkeakenasr drkryqqevd
      901 rikeavrskn marrghsaqi akpirpgqhp aaspthpsai rgggafvqns qpvavrgggg
      961 kqv
//
LOCUS       NP_004730                668 aa            linear   PRI 20-NOV-2025
DEFINITION  metastasis-associated protein MTA2 isoform 1 [Homo sapiens].
ACCESSION   NP_004730
VERSION     NP_004730.2
DBSOURCE    REFSEQ: accession NM_004739.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Morgenstern,E., Molthof,C., Schwartz,U., Graf,J., Bruckmann,A.,
            Hombach,S. and Kretz,M.
  TITLE     lncRNA LINC00941 modulates MTA2/NuRD occupancy to suppress
            premature human epidermal differentiation
  JOURNAL   Life Sci Alliance 7 (7), e202302475 (2024)
   PUBMED   38649186
  REMARK    GeneRIF: lncRNA LINC00941 modulates MTA2/NuRD occupancy to suppress
            premature human epidermal differentiation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Xie,G., Lei,B., Yin,Z., Xu,F. and Liu,X.
  TITLE     CircMTA2 Drives Gastric Cancer Progression through Suppressing MTA2
            Degradation via Interacting with UCHL3
  JOURNAL   Int J Mol Sci 25 (5), 2817 (2024)
   PUBMED   38474064
  REMARK    GeneRIF: CircMTA2 Drives Gastric Cancer Progression through
            Suppressing MTA2 Degradation via Interacting with UCHL3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Huang,X., Tan,J., Chen,M., Zheng,W., Zou,S., Ye,X., Li,Y. and Wu,M.
  TITLE     Prognostic, Immunological, and Mutational Analysis of MTA2 in
            Pan-Cancer and Drug Screening for Hepatocellular Carcinoma
  JOURNAL   Biomolecules 13 (6), 883 (2023)
   PUBMED   37371463
  REMARK    GeneRIF: Prognostic, Immunological, and Mutational Analysis of MTA2
            in Pan-Cancer and Drug Screening for Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Wade,P.A., Gegonne,A., Jones,P.L., Ballestar,E., Aubry,F. and
            Wolffe,A.P.
  TITLE     Mi-2 complex couples DNA methylation to chromatin remodelling and
            histone deacetylation
  JOURNAL   Nat Genet 23 (1), 62-66 (1999)
   PUBMED   10471500
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Zhang,Y., Ng,H.H., Erdjument-Bromage,H., Tempst,P., Bird,A. and
            Reinberg,D.
  TITLE     Analysis of the NuRD subunits reveals a histone deacetylase core
            complex and a connection with DNA methylation
  JOURNAL   Genes Dev 13 (15), 1924-1935 (1999)
   PUBMED   10444591
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Futamura,M., Nishimori,H., Shiratsuchi,T., Saji,S., Nakamura,Y. and
            Tokino,T.
  TITLE     Molecular cloning, mapping, and characterization of a novel human
            gene, MTA1-L1, showing homology to a metastasis-associated gene,
            MTA1
  JOURNAL   J Hum Genet 44 (1), 52-56 (1999)
   PUBMED   9929979
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Xue,Y., Wong,J., Moreno,G.T., Young,M.K., Cote,J. and Wang,W.
  TITLE     NURD, a novel complex with both ATP-dependent chromatin-remodeling
            and histone deacetylase activities
  JOURNAL   Mol Cell 2 (6), 851-861 (1998)
   PUBMED   9885572
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Tong,J.K., Hassig,C.A., Schnitzler,G.R., Kingston,R.E. and
            Schreiber,S.L.
  TITLE     Chromatin deacetylation by an ATP-dependent nucleosome remodelling
            complex
  JOURNAL   Nature 395 (6705), 917-921 (1998)
   PUBMED   9804427
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Zhang,Y., LeRoy,G., Seelig,H.P., Lane,W.S. and Reinberg,D.
  TITLE     The dermatomyositis-specific autoantigen Mi2 is a component of a
            complex containing histone deacetylase and nucleosome remodeling
            activities
  JOURNAL   Cell 95 (2), 279-289 (1998)
   PUBMED   9790534
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001458.6, AL561056.3,
            BC053650.1, BQ574987.1 and AI380395.1.
            
            On May 17, 2001 this sequence version replaced NP_004730.1.
            
            Summary: This gene encodes a protein that has been identified as a
            component of NuRD, a nucleosome remodeling deacetylase complex
            identified in the nucleus of human cells. It shows a very broad
            expression pattern and is strongly expressed in many tissues. It
            may represent one member of a small gene family that encode
            different but related proteins involved either directly or
            indirectly in transcriptional regulation. Their indirect effects on
            transcriptional regulation may include chromatin remodeling. It is
            closely related to another member of this family, a protein that
            has been correlated with the metastatic potential of certain
            carcinomas. These two proteins are so closely related that they
            share the same types of domains. These domains include two DNA
            binding domains, a dimerization domain, and a domain commonly found
            in proteins that methylate DNA. One of the proteins known to be a
            target protein for this gene product is p53. Deacetylation of p53
            is correlated with a loss of growth inhibition in transformed cells
            supporting a connection between these gene family members and
            metastasis. [provided by RefSeq, May 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053650.1, AB016591.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278823.7/ ENSP00000278823.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..668
                     /product="metastasis-associated protein MTA2 isoform 1"
                     /note="metastasis-associated protein 2; metastasis
                     associated gene family, member 2; metastasis-associated
                     1-like 1; metastasis -associated gene 1-like 1;
                     metastasis-associated protein MTA2; MTA1-L1 protein; p53
                     target protein in deacetylase complex"
                     /calculated_mol_wt=74892
     Region          3..168
                     /region_name="BAH_MTA"
                     /note="BAH, or Bromo Adjacent Homology domain, as present
                     in MTA1 and similar proteins. The Metastasis-associated
                     protein MTA1 is part of the NURD (nucleosome remodeling
                     and deacetylating) complex and plays a role in cellular
                     transformation and metastasis. BAH...; cd04709"
                     /db_xref="CDD:240060"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Region          147..198
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            152
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Region          267..312
                     /region_name="SANT_MTA3_like"
                     /note="Myb-Like Dna-Binding Domain of MTA3 and related
                     proteins; cd11661"
                     /db_xref="CDD:212559"
     Site            order(268,298..299,301..302,304..306,308..310)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          363..414
                     /region_name="ZnF_GATA"
                     /note="zinc finger binding to DNA consensus sequence
                     [AT]GATA[AG]; smart00401"
                     /db_xref="CDD:214648"
     Region          <405..664
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          409..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94776.1)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94776.1)"
     Region          449..524
                     /region_name="MTA_R1"
                     /note="MTA R1 domain; pfam17226"
                     /db_xref="CDD:465388"
     Site            460
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9R190; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            522
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9R190; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            531
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9R190; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94776.1)"
     Region          580..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94776.1)"
     Region          647..668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94776.1)"
     CDS             1..668
                     /gene="MTA2"
                     /gene_synonym="MTA1L1; PID"
                     /coded_by="NM_004739.4:416..2422"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8022.1"
                     /db_xref="GeneID:9219"
                     /db_xref="HGNC:HGNC:7411"
                     /db_xref="MIM:603947"
ORIGIN      
        1 maanmyrvgd yvyfensssn pylvrrieel nktangnvea kvvclfrrrd issslnslad
       61 snarefeees kqpgvseqqr hqlkhrelfl srqfeslpat hirgkcsvtl lnetdilsqy
      121 lekedcffys lvfdpvqktl ladqgeirvg ckyqaeipdr lvegesdnrn qqkmemkvwd
      181 pdnpltdrqi dqflvvarav gtfaraldcs ssirqpslhm saaaasrdit lfhamdtlqr
      241 ngydlakams tlvpqggpvl crdemeewsa seamlfeeal ekygkdfndi rqdflpwksl
      301 asivqfyymw kttdryiqqk rlkaaeadsk lkqvyiptyt kpnpnqiisv gskpgmngag
      361 fqkgltcesc httqsaqwya wgppnmqcrl cascwiywkk ygglktptql egatrgttep
      421 hsrghlsrpe aqslspytts anrakllakn rqtfllqttk ltrlarrmcr dllqprraar
      481 rpyapinana ikaecsirlp kaaktplkih plvrlplati vkdlvaqapl kpktprgtkt
      541 pinrnqlsqn rglggimvkr ayetmagagv pfsangrpla sgirsssqpa akrqklnpad
      601 apnpvvfvat kdtralrkal thlemrraar rpnlplkvkp tliavrppvp lpapshpast
      661 nepivled
//
LOCUS       NP_001123312            2138 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit alpha-1C isoform
            14 [Homo sapiens].
ACCESSION   NP_001123312
VERSION     NP_001123312.1
DBSOURCE    REFSEQ: accession NM_001129840.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2138)
  AUTHORS   Zhang,X., Liang,X., Cheng,X., Chen,J., Deng,W., Zhang,Y., Cui,L.,
            Cheng,X., Li,X., Yang,C., Ye,B. and Cao,L.
  TITLE     [CACNA1C rs58619945 genotype influences the cortical thickness of
            attention network among patients with Bipolar disorder]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (9), 1045-1052 (2024)
   PUBMED   39217481
  REMARK    GeneRIF: [CACNA1C rs58619945 genotype influences the cortical
            thickness of attention network among patients with Bipolar
            disorder].
REFERENCE   2  (residues 1 to 2138)
  AUTHORS   Yang,Y., Zhu,Z., Hui,L. and Sun,P.
  TITLE     Effects of CACNA1C and ANK3 on cognitive function in patients with
            bipolar disorder
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 133, 111016 (2024)
   PUBMED   38657895
  REMARK    GeneRIF: Effects of CACNA1C and ANK3 on cognitive function in
            patients with bipolar disorder.
REFERENCE   3  (residues 1 to 2138)
  AUTHORS   Almodovar-Paya,C., Guardiola-Ripoll,M., Giralt-Lopez,M.,
            Oscoz-Irurozqui,M., Canales-Rodriguez,E.J., Madre,M.,
            Soler-Vidal,J., Ramiro,N., Callado,L.F., Arias,B., Gallego,C.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     NRN1 epistasis with BDNF and CACNA1C: mediation effects on symptom
            severity through neuroanatomical changes in schizophrenia
  JOURNAL   Brain Struct Funct 229 (5), 1299-1315 (2024)
   PUBMED   38720004
  REMARK    GeneRIF: NRN1 epistasis with BDNF and CACNA1C: mediation effects on
            symptom severity through neuroanatomical changes in schizophrenia.
REFERENCE   4  (residues 1 to 2138)
  AUTHORS   Gao,S., Yao,X., Chen,J., Huang,G., Fan,X., Xue,L., Li,Z., Wu,T.,
            Zheng,Y., Huang,J., Jin,X., Wang,Y., Wang,Z., Yu,Y., Liu,L.,
            Pan,X., Song,C. and Yan,N.
  TITLE     Structural basis for human Cav1.2 inhibition by multiple drugs and
            the neurotoxin calciseptine
  JOURNAL   Cell 186 (24), 5363-5374 (2023)
   PUBMED   37972591
  REMARK    GeneRIF: Structural basis for human Cav1.2 inhibition by multiple
            drugs and the neurotoxin calciseptine.
REFERENCE   5  (residues 1 to 2138)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   6  (residues 1 to 2138)
  AUTHORS   Napolitano,C. and Priori,S.G.
  TITLE     CACNA1C-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301577
REFERENCE   7  (residues 1 to 2138)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   8  (residues 1 to 2138)
  AUTHORS   Sun,W., McPherson,J.D., Hoang,D.Q., Wasmuth,J.J., Evans,G.A. and
            Montal,M.
  TITLE     Mapping of a human brain voltage-gated calcium channel to human
            chromosome 12p13-pter
  JOURNAL   Genomics 14 (4), 1092-1094 (1992)
   PUBMED   1335957
REFERENCE   9  (residues 1 to 2138)
  AUTHORS   Powers,P.A., Gregg,R.G. and Hogan,K.
  TITLE     Linkage mapping of the human gene for the alpha 1 subunit of the
            cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome
            12p13.2-pter using a dinucleotide repeat
  JOURNAL   Genomics 14 (1), 206-207 (1992)
   PUBMED   1330882
REFERENCE   10 (residues 1 to 2138)
  AUTHORS   Soldatov,N.M.
  TITLE     Molecular diversity of L-type Ca2+ channel transcripts in human
            fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4628-4632 (1992)
   PUBMED   1316612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005342.1, AJ224873.1 and
            AC007618.21.
            
            Summary: This gene encodes an alpha-1 subunit of a
            voltage-dependent calcium channel. Calcium channels mediate the
            influx of calcium ions into the cell upon membrane polarization.
            The alpha-1 subunit consists of 24 transmembrane segments and forms
            the pore through which ions pass into the cell. The calcium channel
            consists of a complex of alpha-1, alpha-2/delta, beta, and gamma
            subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of
            these proteins, either encoded by different genes or the result of
            alternative splicing of transcripts. The protein encoded by this
            gene binds to and is inhibited by dihydropyridine. Alternative
            splicing results in many transcript variants encoding different
            proteins. Some of the predicted proteins may not produce functional
            ion channel subunits. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (14), also referred to has
            HLCC105, lacks four alternate in-frame exons and contains an
            alternate in-frame exon, compared to variant 1, resulting in a
            shorter protein (isoform 14), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ224873.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2138
                     /product="voltage-dependent L-type calcium channel subunit
                     alpha-1C isoform 14"
                     /note="calcium channel, cardic dihydropyridine-sensitive,
                     alpha-1 subunit; DHPR, alpha-1 subunit; voltage-dependent
                     L-type Ca2+ channel alpha 1 subunit; calcium channel,
                     voltage-dependent, L type, alpha 1C subunit; CACNA1C
                     intronic transcript 2; CACNA1C intronic transcript 2
                     (non-protein coding)"
                     /calculated_mol_wt=239389
     Region          123..416
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          523..764
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          899..1176
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1218..1487
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1496..1549
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1559..1633
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1653..2088
                     /region_name="CAC1F_C"
                     /note="Voltage-gated calcium channel subunit alpha,
                     C-term; pfam16885"
                     /db_xref="CDD:465298"
     CDS             1..2138
                     /gene="CACNA1C"
                     /gene_synonym="CACH2; CACN2; CACNA1C-IT2; CACNL1A1;
                     CaV1.2; CCHL1A1; LQT8; NEDHLSS; TS; TS. LQT8"
                     /coded_by="NM_001129840.2:577..6993"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS44787.1"
                     /db_xref="GeneID:775"
                     /db_xref="HGNC:HGNC:1390"
                     /db_xref="MIM:114205"
ORIGIN      
        1 mvnentrmyi peenhqgsny gsprpahanm nanaaaglap ehiptpgaal swqaaidaar
       61 qaklmgsagn atistvsstq rkrqqygkpk kqgsttatrp prallcltlk npirracisi
      121 vewkpfeiii lltifancva laiyipfped dsnatnsnle rveylfliif tveaflkvia
      181 ygllfhpnay lrngwnlldf iivvvglfsa ileqatkadg analggkgag fdvkalrafr
      241 vlrplrlvsg vpslqvvlns iikamvpllh iallvlfvii iyaiiglelf mgkmhktcyn
      301 qegiadvpae ddpspcalet ghgrqcqngt vckpgwdgpk hgitnfdnfa famltvfqci
      361 tmegwtdvly wmqdamgyel pwvyfvslvi fgsffvlnlv lgvlsgefsk erekakargd
      421 fqklrekqql eedlkgyldw itqaedidpe nedegmdeek prnmsmptse tesvntenva
      481 ggdiegencg arlahrisks kfsrywrrwn rfcrrkcraa vksnvfywlv iflvflntlt
      541 iasehynqpn wltevqdtan kallalftae mllkmyslgl qayfvslfnr fdcfvvcggi
      601 letilvetki msplgisvlr cvrllrifki trywnslsnl vasllnsvrs iaslllllfl
      661 fiiifsllgm qlfggkfnfd emqtrrstfd nfpqslltvf qiltgedwns vmydgimayg
      721 gpsfpgmlvc iyfiilficg nyillnvfla iavdnladae sltsaqkeee eekerkklar
      781 taspekkqel vekpavgesk eekielksit adgesppatk inmddlqpne nedkspypnp
      841 ettgeedeee pempvgprpr plselhlkek avpmpeasaf fifssnnrfr lqchrivndt
      901 iftnlilffi llssislaae dpvqhtsfrn hilgnadyvf tsiftleiil kmtaygaflh
      961 kgsfcrnyfn ildllvvsvs lisfgiqssa invvkilrvl rvlrplrain rakglkhvvq
     1021 cvfvairtig nivivttllq fmfacigvql fkgklytcsd sskqteaeck gnyitykdge
     1081 vdhpiiqprs wenskfdfdn vlaammalft vstfegwpel lyrsidshte dkgpiynyrv
     1141 eisiffiiyi iiiaffmmni fvgfvivtfq eqgeqeyknc eldknqrqcv eyalkarplr
     1201 ryipknqhqy kvwyvvnsty feylmfvlil lnticlamqh ygqsclfkia mnilnmlftg
     1261 lftvemilkl iafkpkhyfc dawntfdali vvgsivdiai tevnpaehtq cspsmnaeen
     1321 srisitffrl frvmrlvkll srgegirtll wtfiksfqal pyvallivml ffiyavigmq
     1381 vfgkialndt teinrnnnfq tfpqavlllf rcatgeawqd imlacmpgkk capesepsns
     1441 tegetpcgss favfyfisfy mlcafliinl fvavimdnfd yltrdwsilg phhldefkri
     1501 waeydpeakg rikhldvvtl lrriqpplgf gklcphrvac krlvsmnmpl nsdgtvmfna
     1561 tlfalvrtal riktegnleq aneelraiik kiwkrtsmkl ldqvvppagd devtvgkfya
     1621 tfliqeyfrk fkkrkeqglv gkpsqrnals lqaglrtlhd igpeirrais gdltaeeeld
     1681 kamkeavsaa seddifrrag glfgnhvsyy qsdgrsafpq tfttqrplhi nkagssqgdt
     1741 espsheklvd stftpssyss tgsnaninna nntalgrlpr pagypstvst veghgpplsp
     1801 airvqevawk lssnrchsre sqaamagqee tsqdetyevk mnhdteacse psllstemls
     1861 yqddenrqlt lpeedkrdir qspkrgflrs aslgrrasfh leclkrqkdr ggdisqktvl
     1921 plhlvhhqal avaglspllq rshspasfpr pfatppatpg srgwppqpvp tlrlegvess
     1981 eklnssfpsi hcgswaettp ggggssaarr vrpvslmvps qagapgrqfh gsasslveav
     2041 liseglgqfa qdpkfievtt qeladacdmt ieemesaadn ilsggapqsp ngallpfvnc
     2101 rdagqdragg eedagcvrar grpseeelqd srvyvssl
//
LOCUS       NP_689601                400 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 237 isoform b [Homo sapiens].
ACCESSION   NP_689601
VERSION     NP_689601.2
DBSOURCE    REFSEQ: accession NM_152388.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 400)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 400)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   3  (residues 1 to 400)
  AUTHORS   Skiba,N.P., Cady,M.A., Molday,L., Han,J.Y.S., Lewis,T.R.,
            Spencer,W.J., Thompson,W.J., Hiles,S., Philp,N.J., Molday,R.S. and
            Arshavsky,V.Y.
  TITLE     TMEM67, TMEM237, and Embigin in Complex With Monocarboxylate
            Transporter MCT1 Are Unique Components of the Photoreceptor Outer
            Segment Plasma Membrane
  JOURNAL   Mol Cell Proteomics 20, 100088 (2021)
   PUBMED   33933680
REFERENCE   4  (residues 1 to 400)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 400)
  AUTHORS   Zuniga,F.I. and Craft,C.M.
  TITLE     Deciphering the structure and function of Als2cr4 in the mouse
            retina
  JOURNAL   Invest Ophthalmol Vis Sci 51 (9), 4407-4415 (2010)
   PUBMED   20375344
REFERENCE   6  (residues 1 to 400)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 400)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   8  (residues 1 to 400)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
REFERENCE   9  (residues 1 to 400)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 400)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007279.4, AB053301.1 and
            AC007282.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 26, 2006 this sequence version replaced NP_689601.1.
            
            Summary: The protein encoded by this gene is a tetraspanin protein
            that is thought to be involved in WNT signaling. Defects in this
            gene are a cause of Joubert syndrome-14. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.28051.1,
                                           SRR1803612.14418.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..400
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..400
                     /product="transmembrane protein 237 isoform b"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 4; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 4 protein"
                     /calculated_mol_wt=44468
     Region          132..375
                     /region_name="TMEM237"
                     /note="Transmembrane protein 237; pfam15383"
                     /db_xref="CDD:464690"
     CDS             1..400
                     /gene="TMEM237"
                     /gene_synonym="ALS2CR4; JBTS14"
                     /coded_by="NM_152388.4:45..1247"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46490.1"
                     /db_xref="GeneID:65062"
                     /db_xref="HGNC:HGNC:14432"
                     /db_xref="MIM:614423"
ORIGIN      
        1 mgknpvrppr alppvpsqdd iplsrpkkkk prtkntpasa sleglaqtag rrpsegneps
       61 tkelkehpea pvqrrqkktr lpleletsst qkksssssll rnengidaep aeeaviqkpr
      121 rktkktqpae lqyanelgve dediitdeqt tveqqsvfta ptgisqpvgk vfveksrrfq
      181 aadrselikt tenidvsmdv kpswttrdva ltvhrafrmi glfshgflag cavwnivviy
      241 vlagdqlsnl snllqqyktl aypfqsllyl llalstisaf dridfakisv airnflaldp
      301 talasflyft alilslsqqm tsdrihlytp ssvngslwea gieeqilqpw ivvnlvvall
      361 vglswlflsy rpgmdlseel mfsseveeyp dkekeikass
//
LOCUS       NP_001310481             312 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor type 1-associated DEATH domain
            protein [Homo sapiens].
ACCESSION   NP_001310481 XP_011521722
VERSION     NP_001310481.1
DBSOURCE    REFSEQ: accession NM_001323552.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   van Loo,G. and Bertrand,M.J.M.
  TITLE     Death by TNF: a road to inflammation
  JOURNAL   Nat Rev Immunol 23 (5), 289-303 (2023)
   PUBMED   36380021
  REMARK    Review article
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Chen,Y., Gu,Y., Xiong,X., Zheng,Y., Liu,X., Wang,W. and Meng,G.
  TITLE     Roles of the adaptor protein tumor necrosis factor receptor type
            1-associated death domain protein (TRADD) in human diseases
  JOURNAL   Biomed Pharmacother 153, 113467 (2022)
   PUBMED   36076575
  REMARK    GeneRIF: Roles of the adaptor protein tumor necrosis factor
            receptor type 1-associated death domain protein (TRADD) in human
            diseases.
            Review article
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Feoktistova,M., Makarov,R., Yazdi,A.S. and Panayotova-Dimitrova,D.
  TITLE     RIPK1 and TRADD Regulate TNF-Induced Signaling and Ripoptosome
            Formation
  JOURNAL   Int J Mol Sci 22 (22), 12459 (2021)
   PUBMED   34830347
  REMARK    GeneRIF: RIPK1 and TRADD Regulate TNF-Induced Signaling and
            Ripoptosome Formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Zhang,N., Kisiswa,L., Ramanujan,A., Li,Z., Sim,E.W., Tian,X.,
            Yuan,W., Ibanez,C.F. and Lin,Z.
  TITLE     Structural basis of NF-kappaB signaling by the p75 neurotrophin
            receptor interaction with adaptor protein TRADD through their
            respective death domains
  JOURNAL   J Biol Chem 297 (2), 100916 (2021)
   PUBMED   34175311
  REMARK    GeneRIF: Structural basis of NF-kappaB signaling by the p75
            neurotrophin receptor interaction with adaptor protein TRADD
            through their respective death domains.
            Erratum:[J Biol Chem. 2022 Nov;298(11):102583. doi:
            10.1016/j.jbc.2022.102583. PMID: 36257251]
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Park,A. and Baichwal,V.R.
  TITLE     Systematic mutational analysis of the death domain of the tumor
            necrosis factor receptor 1-associated protein TRADD
  JOURNAL   J Biol Chem 271 (16), 9858-9862 (1996)
   PUBMED   8621670
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hsu,H., Huang,J., Shu,H.B., Baichwal,V. and Goeddel,D.V.
  TITLE     TNF-dependent recruitment of the protein kinase RIP to the TNF
            receptor-1 signaling complex
  JOURNAL   Immunity 4 (4), 387-396 (1996)
   PUBMED   8612133
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Hsu,H., Shu,H.B., Pan,M.G. and Goeddel,D.V.
  TITLE     TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF
            receptor 1 signal transduction pathways
  JOURNAL   Cell 84 (2), 299-308 (1996)
   PUBMED   8565075
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hsu,H., Xiong,J. and Goeddel,D.V.
  TITLE     The TNF receptor 1-associated protein TRADD signals cell death and
            NF-kappa B activation
  JOURNAL   Cell 81 (4), 495-504 (1995)
   PUBMED   7758105
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Hasegawa,H.
  TITLE     [Nurses replies to expectations of the nursing profession]
  JOURNAL   Kango 27 (3), 66-80 (1975)
   PUBMED   1040062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA353575.1, AC074143.5,
            BT006934.1 and CA426418.1.
            
            On Apr 22, 2016 this sequence version replaced XP_011521722.1.
            
            Summary: The protein encoded by this gene is a death domain
            containing adaptor molecule that interacts with TNFRSF1A/TNFR1 and
            mediates programmed cell death signaling and NF-kappaB activation.
            This protein binds adaptor protein TRAF2, reduces the recruitment
            of inhibitor-of-apoptosis proteins (IAPs) by TRAF2, and thus
            suppresses TRAF2 mediated apoptosis. This protein can also interact
            with receptor TNFRSF6/FAS and adaptor protein FADD/MORT1, and is
            involved in the Fas-induced cell death pathway. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR9304713.271039.1,
                                           ERR279839.1380.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..312
                     /product="tumor necrosis factor receptor type 1-associated
                     DEATH domain protein"
                     /note="tumor necrosis factor receptor-1-associated
                     protein; TNFR1-associated death domain protein; tumor
                     necrosis factor receptor type 1 associated death domain
                     protein"
                     /calculated_mol_wt=34116
     Region          51..161
                     /region_name="TRADD_N"
                     /note="TRADD, N-terminal domain; pfam09034"
                     /db_xref="CDD:430379"
     Region          147..163
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:Q3U0V2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          170..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          215..304
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     Region          222..289
                     /region_name="Interaction with KRT14 and KRT18.
                     /evidence=ECO:0000269|PubMed:11684708"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          231..244
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q3U0V2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Site            235
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:23955153,
                     ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:32766249,
                     ECO:0007744|PDB:6AC0; propagated from UniProtKB/Swiss-Prot
                     (Q15628.2)"
     Site            245
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:32766249;
                     propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     CDS             1..312
                     /gene="TRADD"
                     /gene_synonym="Hs.89862"
                     /coded_by="NM_001323552.2:94..1032"
                     /db_xref="CCDS:CCDS10829.1"
                     /db_xref="GeneID:8717"
                     /db_xref="HGNC:HGNC:12030"
                     /db_xref="MIM:603500"
ORIGIN      
        1 maagqnghee wvgsaylfve ssldkvvlsd ayahpqqkva vyralqaala esggspdvlq
       61 mlkihrsdpq livqlrfcgr qpcgrflray regalraalq rslaaalaqh svplqlelra
      121 gaerldalla deerclscil aqqpdrlrde elaeledalr nlkcgsgarg gdgevasapl
      181 qppvpslsev kpppppppaq tflfqgqpvv nrplslkdqq tfarsvglkw rkvgrslqrg
      241 cralrdpald slayeyereg lyeqafqllr rfvqaegrra tlqrlveale eneltslaed
      301 llgltdpngg la
//
LOCUS       NP_079441                397 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA polymerase II elongation factor ELL3 [Homo sapiens].
ACCESSION   NP_079441
VERSION     NP_079441.1
DBSOURCE    REFSEQ: accession NM_025165.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 397)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 397)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 397)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 397)
  AUTHORS   Lee,J.Y., Lee,S.H., Kim,K.S., Park,K.H. and Park,K.S.
  TITLE     Ell3 functions as a critical decision maker at the crossroad
            between stem cell senescence and apoptosis
  JOURNAL   Stem Cell Res Ther 10 (1), 32 (2019)
   PUBMED   30654843
  REMARK    GeneRIF: Suppression of Ell3 expression induced senescence in stem
            cells by increasing Bcl-2 expression. Unlike the effect of Ell3
            suppression, the ectopic expression of Ell3 induces apoptosis of
            stem cells and induces apoptosis of adjacent cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 397)
  AUTHORS   Alexander,L.M.M., Watters,J., Reusch,J.A., Maurin,M.,
            Nepon-Sixt,B.S., Vrzalikova,K., Alexandrow,M.G., Murray,P.G. and
            Wright,K.L.
  TITLE     Selective expression of the transcription elongation factor ELL3 in
            B cells prior to ELL2 drives proliferation and survival
  JOURNAL   Mol Immunol 91, 8-16 (2017)
   PUBMED   28858629
  REMARK    GeneRIF: Selective expression of the transcription elongation
            factor ELL3 in B cells prior to ELL2 drives proliferation and
            survival
REFERENCE   6  (residues 1 to 397)
  AUTHORS   Hu,D., Smith,E.R., Garruss,A.S., Mohaghegh,N., Varberg,J.M.,
            Lin,C., Jackson,J., Gao,X., Saraf,A., Florens,L., Washburn,M.P.,
            Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex functions at initiation and
            elongation phases of snRNA gene transcription
  JOURNAL   Mol Cell 51 (4), 493-505 (2013)
   PUBMED   23932780
REFERENCE   7  (residues 1 to 397)
  AUTHORS   Ahn,H.J., Kim,G. and Park,K.S.
  TITLE     Ell3 stimulates proliferation, drug resistance, and cancer stem
            cell properties of breast cancer cells via a MEK/ERK-dependent
            signaling pathway
  JOURNAL   Biochem Biophys Res Commun 437 (4), 557-564 (2013)
   PUBMED   23850691
  REMARK    GeneRIF: Ell3 may play a critical role in promoting oncogenesis in
            breast cancer by regulating cell proliferation and cancer stem cell
            properties via the ERK1/2 signaling pathway
REFERENCE   8  (residues 1 to 397)
  AUTHORS   Smith,E.R., Lin,C., Garrett,A.S., Thornton,J., Mohaghegh,N., Hu,D.,
            Jackson,J., Saraf,A., Swanson,S.K., Seidel,C., Florens,L.,
            Washburn,M.P., Eissenberg,J.C. and Shilatifard,A.
  TITLE     The little elongation complex regulates small nuclear RNA
            transcription
  JOURNAL   Mol Cell 44 (6), 954-965 (2011)
   PUBMED   22195968
REFERENCE   9  (residues 1 to 397)
  AUTHORS   Takahashi,H., Parmely,T.J., Sato,S., Tomomori-Sato,C., Banks,C.A.,
            Kong,S.E., Szutorisz,H., Swanson,S.K., Martin-Brown,S.,
            Washburn,M.P., Florens,L., Seidel,C.W., Lin,C., Smith,E.R.,
            Shilatifard,A., Conaway,R.C. and Conaway,J.W.
  TITLE     Human mediator subunit MED26 functions as a docking site for
            transcription elongation factors
  JOURNAL   Cell 146 (1), 92-104 (2011)
   PUBMED   21729782
REFERENCE   10 (residues 1 to 397)
  AUTHORS   Miller,T., Williams,K., Johnstone,R.W. and Shilatifard,A.
  TITLE     Identification, cloning, expression, and biochemical
            characterization of the testis-specific RNA polymerase II
            elongation factor ELL3
  JOURNAL   J Biol Chem 275 (41), 32052-32056 (2000)
   PUBMED   10882741
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK126384.1 and AC018512.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026290.1, SRR5189667.282666.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319359.8/ ENSP00000320346.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..397
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.3"
     Protein         1..397
                     /product="RNA polymerase II elongation factor ELL3"
                     /note="elongation factor RNA polymerase II-like 3"
                     /calculated_mol_wt=45230
     Region          17..>118
                     /region_name="ELL"
                     /note="RNA polymerase II elongation factor ELL; pfam10390"
                     /db_xref="CDD:463068"
     Region          164..219
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB65.2)"
     Region          237..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HB65.2)"
     Region          291..391
                     /region_name="Occludin_ELL"
                     /note="Occludin homology domain; pfam07303"
                     /db_xref="CDD:462140"
     CDS             1..397
                     /gene="ELL3"
                     /coded_by="NM_025165.3:66..1259"
                     /db_xref="CCDS:CCDS10102.1"
                     /db_xref="GeneID:80237"
                     /db_xref="HGNC:HGNC:23113"
                     /db_xref="MIM:609885"
ORIGIN      
        1 meelqeplrg qlrlcftqaa rtsllllrln daalralqec qrqqvrpvia fqghrgylrl
       61 pgpgwsclfs fivsqccqeg aggsldlvcq rflrsgpnsl hclgslrerl iiwaamdsip
      121 apssvqghnl tedarhpesw qntggysegd avsqpqmale evsvsdplas nqgqslpgss
      181 rehmaqwevr sqthvpnrep vqalpssasr krldkkrsvp vatveleekr frtlplvpsp
      241 lqgltnqdlq egedweqede dmdprlehss svqedsesps pedipdyllq yraihsaeqq
      301 hayeqdfetd yaeyrilhar vgtasqrfie lgaeikrvrr gtpeykvled kiiqeykkfr
      361 kqypsyreek rrceylhqkl shikglilef eeknrgs
//
LOCUS       NP_996756                286 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase PP1-alpha catalytic subunit
            isoform 2 [Homo sapiens].
ACCESSION   NP_996756
VERSION     NP_996756.1
DBSOURCE    REFSEQ: accession NM_206873.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Wang,Z., Song,A., Tao,B., Miao,M., Luo,Y.Q., Wang,J., Yin,Z.,
            Xiao,R., Zhou,X., Shang,X.Y., Hu,S., Liang,K., Danko,C.G. and
            Chen,F.X.
  TITLE     The phosphatase PP1 sustains global transcription by promoting RNA
            polymerase II pause release
  JOURNAL   Mol Cell 84 (24), 4824-4842 (2024)
   PUBMED   39603240
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Kelley,J.R., Dimitrova,E., Maciuszek,M., Nguyen,H.T.,
            Szczurek,A.T., Hughes,A.L., Blackledge,N.P., Kettenbach,A.N. and
            Klose,R.J.
  TITLE     The PNUTS phosphatase complex controls transcription pause release
  JOURNAL   Mol Cell 84 (24), 4843-4861 (2024)
   PUBMED   39603239
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Chen,Z., Li,Y., He,K., Yang,J., Deng,Q., Chen,Y. and Fu,Z.
  TITLE     CircGPRC5A enhances colorectal cancer progress by stabilizing
            PPP1CA and inducing YAP dephosphorylation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 334 (2023)
   PUBMED   38057879
  REMARK    GeneRIF: CircGPRC5A enhances colorectal cancer progress by
            stabilizing PPP1CA and inducing YAP dephosphorylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Saadat,M., Mizuno,Y., Kikuchi,K. and Yoshida,M.C.
  TITLE     Comparative mapping of the gene encoding the catalytic subunit of
            protein phosphatase type 1 alpha (PPP1CA) to human, rat, and mouse
            chromosomes
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 55-57 (1995)
   PUBMED   7736790
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Durfee,T., Becherer,K., Chen,P.L., Yeh,S.H., Yang,Y., Kilburn,A.E.,
            Lee,W.H. and Elledge,S.J.
  TITLE     The retinoblastoma protein associates with the protein phosphatase
            type 1 catalytic subunit
  JOURNAL   Genes Dev 7 (4), 555-569 (1993)
   PUBMED   8384581
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Barker,H.M., Jones,T.A., da Cruz e Silva,E.F., Spurr,N.K., Sheer,D.
            and Cohen,P.T.
  TITLE     Localization of the gene encoding a type I protein phosphatase
            catalytic subunit to human chromosome band 11q13
  JOURNAL   Genomics 7 (2), 159-166 (1990)
   PUBMED   2161401
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Carrey,E.A., Campbell,D.G. and Hardie,D.G.
  TITLE     Phosphorylation and activation of hamster carbamyl phosphate
            synthetase II by cAMP-dependent protein kinase. A novel mechanism
            for regulation of pyrimidine nucleotide biosynthesis
  JOURNAL   EMBO J 4 (13B), 3735-3742 (1985)
   PUBMED   4092695
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Hemmings,H.C. Jr., Greengard,P., Tung,H.Y. and Cohen,P.
  TITLE     DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent
            inhibitor of protein phosphatase-1
  JOURNAL   Nature 310 (5977), 503-505 (1984)
   PUBMED   6087160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG480286.1, BM799599.1,
            BE278068.1 and BC008010.1.
            
            Summary: The protein encoded by this gene is one of the three
            catalytic subunits of protein phosphatase 1 (PP1). This broadly
            expressed gene encodes the alpha subunit of the PP1 complex that
            associates with over 200 regulatory proteins to form holoenzymes
            which dephosphorylate their biological targets with high
            specificity. PP1 is a serine/threonine specific protein phosphatase
            known to be involved in the regulation of a variety of cellular
            processes, such as cell division, glycogen metabolism, muscle
            contractility, protein synthesis, and HIV-1 viral transcription.
            Increased PP1 activity has been observed in the end stage of heart
            failure. Studies suggest that PP1 is an important regulator of
            cardiac function and that PP1 deregulation is implicated in
            diabetes and multiple types of cancer. Three alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2020].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1. The resulting isoform (2) lacks an internal
            region, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.71247.1,
                                           SRR5189667.128784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..286
                     /product="serine/threonine-protein phosphatase PP1-alpha
                     catalytic subunit isoform 2"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine protein phosphatase PP1-alpha 1
                     catalytic subunit; serine/threonine-protein phosphatase
                     PP1-alpha catalytic subunit; protein phosphatase 1,
                     catalytic subunit, alpha isozyme; testicular tissue
                     protein Li 155"
                     /calculated_mol_wt=32464
     Region          19..254
                     /region_name="MPP_PP1_PPKL"
                     /note="PP1, PPKL (PP1 and kelch-like) enzymes, and related
                     proteins, metallophosphatase domain; cd07414"
                     /db_xref="CDD:277359"
     Site            order(20,22,48,52,80..81,85..86,90,129,151..153,162,
                     176..178,204,228..232)
                     /site_type="active"
                     /db_xref="CDD:277359"
     Site            order(20,22,48,80,129,204)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277359"
     Site            order(52,85..86,90,151..153,162,176..178,228..232)
                     /site_type="other"
                     /note="natural toxin binding site [chemical binding]"
                     /db_xref="CDD:277359"
     Site            order(135,137,154,159,172,181,189..190,192..194,196..198,
                     213,217,244..245,247,249,251)
                     /site_type="other"
                     /note="MYPT1 binding site [polypeptide binding]"
                     /db_xref="CDD:277359"
     CDS             1..286
                     /gene="PPP1CA"
                     /gene_synonym="PP-1A; PP1A; PP1alpha; PPP1A"
                     /coded_by="NM_206873.2:77..937"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8161.1"
                     /db_xref="GeneID:5499"
                     /db_xref="HGNC:HGNC:9281"
                     /db_xref="MIM:176875"
ORIGIN      
        1 msdseklnld siigrllegd ihgqyydllr lfeyggfppe snylflgdyv drgkqsleti
       61 clllaykiky penffllrgn hecasinriy gfydeckrry niklwktftd cfnclpiaai
      121 vdekifcchg glspdlqsme qirrimrptd vpdqgllcdl lwsdpdkdvq gwgendrgvs
      181 ftfgaevvak flhkhdldli crahqvvedg yeffakrqlv tlfsapnycg efdnagamms
      241 vdetlmcsfq ilkpadknkg kygqfsglnp ggrpitpprn sakakk
//
LOCUS       NP_001353505             887 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001353505 XP_016855509
VERSION     NP_001353505.1
DBSOURCE    REFSEQ: accession NM_001366576.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 887)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 887)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 887)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 887)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 887)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 887)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 887)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 887)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 887)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 887)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855509.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.118736.1,
                                           SRR1803611.29489.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..887
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..887
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 12"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=100003
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <121..209
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <384..713
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <589..>723
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..887
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366576.1:26..2689"
                     /note="isoform 12 is encoded by transcript variant 16"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkekt pelpepsvkv kepsvqeats tsdilkvpkp epipepkeps peknskkeke
      241 kektrprsrs rsksrsrtrs rspshtrprr rhrsrsrsys prrrpsprrr psprrrtppr
      301 rmpppprhrr srspvrrrrr ssaslsgsss sssssrsrsp pkkppkrtss pprktrrlsp
      361 saspprrrhr psppatpppk trhsptpqqs nrtrksrvsv spgrtsgkvt khkgtekres
      421 pspapkprkv elsesedkgg kmaaadsvqq rrqyrrqnqq sssdsgssss sederpkrsh
      481 vkngevgrrr rhspsrsasp sprkrqkets prmqmgkrwq spvtksgrrr rspsppptrr
      541 rrspspappp rrrrtptppp rrrtpspppr rrspsprrys ppiqrrysps pppkrrtasp
      601 ppppkrrasp spppkrrvsh spppkqrssp vtkrrspsls skhrkgssps rstrearspq
      661 pnkrhspspr prapqtsssp ppvrrgasss pqrrqspsps trpirrvsrt pepkkikkaa
      721 spspqsvrrv sssrsvsgsp epaakkppap pspvqsqsps tnwspavpvk kaksptpsps
      781 pprnsdqegg gkkkkkkkdk khkkdkkhkk hkkhkkekav aaaaaaavtp aaiaaatttl
      841 aqeepvaape pkketeseae dnlddlekhl rekalrsmrk aqvspqs
//
LOCUS       NP_078911                725 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 35, NatC auxiliary subunit [Homo
            sapiens].
ACCESSION   NP_078911
VERSION     NP_078911.3
DBSOURCE    REFSEQ: accession NM_024635.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Varland,S., Silva,R.D., Kjosas,I., Faustino,A., Bogaert,A.,
            Billmann,M., Boukhatmi,H., Kellen,B., Costanzo,M., Drazic,A.,
            Osberg,C., Chan,K., Zhang,X., Tong,A.H.Y., Andreazza,S., Lee,J.J.,
            Nedyalkova,L., Usaj,M., Whitworth,A.J., Andrews,B.J., Moffat,J.,
            Myers,C.L., Gevaert,K., Boone,C., Martinho,R.G. and Arnesen,T.
  TITLE     N-terminal acetylation shields proteins from degradation and
            promotes age-dependent motility and longevity
  JOURNAL   Nat Commun 14 (1), 6774 (2023)
   PUBMED   37891180
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Lin,Y., Dong,H., Deng,W., Lin,W., Li,K., Xiong,X., Guo,Y., Zhou,F.,
            Ma,C., Chen,Y., Ren,H., Yang,H., Dai,N., Ma,L., Meltzer,S.J.,
            Yeung,S.J. and Zhang,H.
  TITLE     Evaluation of Salivary Exosomal Chimeric GOLM1-NAA35 RNA as a
            Potential Biomarker in Esophageal Carcinoma
  JOURNAL   Clin Cancer Res 25 (10), 3035-3045 (2019)
   PUBMED   30745298
  REMARK    GeneRIF: salivary exosomal GOLM1-NAA35 chimeric RNA (seG-NchiRNA)
            constitutes an effective candidate noninvasive biomarker for the
            convenient, reliable assessment of therapeutic response,
            recurrence, and early detection.
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Li,Y., Oosting,M., Deelen,P., Ricano-Ponce,I., Smeekens,S.,
            Jaeger,M., Matzaraki,V., Swertz,M.A., Xavier,R.J., Franke,L.,
            Wijmenga,C., Joosten,L.A., Kumar,V. and Netea,M.G.
  TITLE     Inter-individual variability and genetic influences on cytokine
            responses to bacteria and fungi
  JOURNAL   Nat Med 22 (8), 952-960 (2016)
   PUBMED   27376574
  REMARK    GeneRIF: A cytokine QTL at the NAA35-GOLM1 locus markedly modulated
            interleukin (IL)-6 production in response to multiple pathogens and
            was associated with susceptibility to candidemia.
            Erratum:[Nat Med. 2016 Oct 6;22(10):1192. doi:
            10.1038/nm1016-1192b. PMID: 27711068]
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Zhang,H., Lin,W., Kannan,K., Luo,L., Li,J., Chao,P.W., Wang,Y.,
            Chen,Y.P., Gu,J. and Yen,L.
  TITLE     Aberrant chimeric RNA GOLM1-MAK10 encoding a secreted fusion
            protein as a molecular signature for human esophageal squamous cell
            carcinoma
  JOURNAL   Oncotarget 4 (11), 2135-2143 (2013)
   PUBMED   24243830
  REMARK    GeneRIF: Data demonstrate that chimera GOLM1-MAK10 encodes a
            secreted fusion protein. Mechanistic studies reveal that
            GOLM1-MAK10 is likely derived from transcription
            read-through/splicing rather than being generated from a fusion
            gene.
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Starheim,K.K., Gromyko,D., Evjenth,R., Ryningen,A., Varhaug,J.E.,
            Lillehaug,J.R. and Arnesen,T.
  TITLE     Knockdown of human N alpha-terminal acetyltransferase complex C
            leads to p53-dependent apoptosis and aberrant human Arl8b
            localization
  JOURNAL   Mol Cell Biol 29 (13), 3569-3581 (2009)
   PUBMED   19398576
  REMARK    GeneRIF: Human Naa35 (MAK10) is an auxiliary subunit of the human
            NatC N-terminal acetyltransferase complex. NatC acetylates
            hydrophobic Met-starting N-termini, and NatC knockdown induces
            p53-dependent apoptosis.
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Yi,X.J., Li,X.F. and Yu,F.S.
  TITLE     A novel epithelial wound-related gene is abundantly expressed in
            developing rat cornea and skin
  JOURNAL   Curr Eye Res 20 (5), 430-440 (2000)
   PUBMED   10855038
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB023442.1, BC117427.1, CA945233.1 and AL161447.20.
            
            On Apr 13, 2007 this sequence version replaced NP_078911.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.48610.1,
                                           SRR1660805.148328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361671.10/ ENSP00000354972.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..725
                     /product="N-alpha-acetyltransferase 35, NatC auxiliary
                     subunit"
                     /note="corneal wound healing-related protein; protein
                     MAK10 homolog; embryonic growth-associated protein
                     homolog; MAK10 homolog, amino-acid N-acetyltransferase
                     subunit"
                     /calculated_mol_wt=83508
     Region          46..181
                     /region_name="Mak10"
                     /note="Mak10 subunit, NatC N(alpha)-terminal
                     acetyltransferase; pfam04112"
                     /db_xref="CDD:461179"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5VZE5.1)"
     Region          548..573
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VZE5.1)"
     CDS             1..725
                     /gene="NAA35"
                     /gene_synonym="bA379P1.1; EGAP; MAK10; MAK10P"
                     /coded_by="NM_024635.4:134..2311"
                     /db_xref="CCDS:CCDS6673.1"
                     /db_xref="GeneID:60560"
                     /db_xref="HGNC:HGNC:24340"
                     /db_xref="MIM:619438"
ORIGIN      
        1 mvmkasvddd dsgwelsmpe kmeksntnwv ditqdfeeac relklgellh dklfglfeam
       61 saiemmdpkm dagmignqvn rkvlnfeqai kdgtikikdl tlpeligimd tcfcclitwl
      121 eghslaqtvf tclyihnpdf iedpamkafa lgilkicdia rekvnkaavf eeedfqsmty
      181 gfkmansvtd lrvtgmlkdv eddmqrrvks trsrqgeerd pevelehqqc lavfsrvkft
      241 rvlltvliaf tkketsavae aqklmvqaad llsaihnslh hgiqaqndtt kgdhpimmgf
      301 eplvnqrllp ptfpryakii kreemvnyfa rlidriktvc evvnltnlhc ildffcefse
      361 qspcvlsrsl lqttflvdnk kvfgthlmqd mvkdalrsfv sppvlspkcy lynnhqakdc
      421 idsfvthcvr pfcsliqihg hnrarqrdkl ghileefatl qdeaekvdaa lhtmllkqep
      481 qrqhlaclgt wvlyhnlrim iqyllsgfel elysmheyyy iywylsefly awlmstlsra
      541 dgsqmaeeri meeqqkgrss kktkkkkkvr plsreitmsq ayqnmcagmf ktmvafdmdg
      601 kvrkpkfeld seqvryehrf apfnsvmtpp pvhylqfkem sdlnkysppp qspelyvaas
      661 khfqqakmil enipnpdhev nrilkvakpn fvvmkllagg hkkeskvppe fdfsahkyfp
      721 vvklv
//
LOCUS       NP_001340821             647 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3 domain-containing kinase-binding protein 1 isoform f [Homo
            sapiens].
ACCESSION   NP_001340821 XP_016884951
VERSION     NP_001340821.1
DBSOURCE    REFSEQ: accession NM_001353892.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Ahmed,S.F., Buetow,L., Gabrielsen,M., Lilla,S., Sibbet,G.J.,
            Sumpton,D., Zanivan,S., Hedley,A., Clark,W. and Huang,D.T.
  TITLE     E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis
  JOURNAL   Oncogene 40 (12), 2149-2164 (2021)
   PUBMED   33627783
  REMARK    GeneRIF: E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    GeneRIF: Cbl-CIN85-endophilin complex mediates ligand-induced
            downregulation of EGF receptors
            Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Narita,T., Amano,F., Yoshizaki,K., Nishimoto,N., Nishimura,T.,
            Tajima,T., Namiki,H. and Taniyama,T.
  TITLE     Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 133-134 (2001)
   PUBMED   11474197
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Watanabe,S., Take,H., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Characterization of the CIN85 adaptor protein and identification of
            components involved in CIN85 complexes
  JOURNAL   Biochem Biophys Res Commun 278 (1), 167-174 (2000)
   PUBMED   11071869
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Gout,I., Middleton,G., Adu,J., Ninkina,N.N., Drobot,L.B.,
            Filonenko,V., Matsuka,G., Davies,A.M., Waterfield,M. and
            Buchman,V.L.
  TITLE     Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein
  JOURNAL   EMBO J 19 (15), 4015-4025 (2000)
   PUBMED   10921882
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Take,H., Watanabe,S., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Cloning and characterization of a novel adaptor protein, CIN85,
            that interacts with c-Cbl
  JOURNAL   Biochem Biophys Res Commun 268 (2), 321-328 (2000)
   PUBMED   10679202
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Salvatore,P., Hanash,C.R., Kido,Y., Imai,Y. and Accili,D.
  TITLE     Identification of sirm, a novel insulin-regulated SH3 binding
            protein that associates with Grb-2 and FYN
  JOURNAL   J Biol Chem 273 (12), 6989-6997 (1998)
   PUBMED   9507006
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL772197.12, AL732325.6,
            AL732327.6 and AL732423.12.
            
            On Jul 28, 2017 this sequence version replaced XP_016884951.1.
            
            Summary: This gene encodes an adapter protein that contains one or
            more N-terminal Src homology domains, a proline rich region and a
            C-terminal coiled-coil domain. The encoded protein facilitates
            protein-protein interactions and has been implicated in numerous
            cellular processes including apoptosis, cytoskeletal rearrangement,
            cell adhesion and in the regulation of clathrin-dependent
            endocytosis. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.236622.1,
                                           SRR1660803.123327.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..647
                     /product="SH3 domain-containing kinase-binding protein 1
                     isoform f"
                     /note="Src family kinase-binding protein 1; src-related
                     kinase binding protein-1; CD2-binding protein 3;
                     migration-inducing gene 18; c-Cbl-interacting protein;
                     cbl-interacting protein of 85 kDa; SH3-domain kinase
                     binding protein 1; human Src family kinase-binding protein
                     1"
                     /calculated_mol_wt=71326
     Region          3..55
                     /region_name="SH3_CIN85_1"
                     /note="First Src Homology 3 domain (SH3A) of
                     Cbl-interacting protein of 85 kDa; cd12052"
                     /db_xref="CDD:212985"
     Site            order(7..13,17,21..22,34..36,46..47,49,51..52)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212985"
     Site            order(8,10,13..14,16..17,34,36,47,51..52,54)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212985"
     Region          102..154
                     /region_name="SH3_CIN85_2"
                     /note="Second Src Homology 3 domain (SH3B) of
                     Cbl-interacting protein of 85 kDa; cd12055"
                     /db_xref="CDD:212988"
     Site            order(106..112,116,120..121,133..135,145..146,148,
                     150..151)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Site            order(107,109,112,116,133..135,146,148,150..151)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Region          296..351
                     /region_name="SH3_CIN85_3"
                     /note="Third Src Homology 3 domain (SH3C) of
                     Cbl-interacting protein of 85 kDa; cd12057"
                     /db_xref="CDD:212990"
     Site            order(300..307,309..310,314..315,328..331,341..342,344,
                     346..347,349)
                     /site_type="other"
                     /note="ubiquitin interaction site [polypeptide binding]"
                     /db_xref="CDD:212990"
     Site            order(301,303,306,310,329..331,342,344,346..347)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212990"
     CDS             1..647
                     /gene="SH3KBP1"
                     /gene_synonym="AGMX2; CD2BP3; CIN85; GIG10; HSB-1; HSB1;
                     IMD61; MIG18"
                     /coded_by="NM_001353892.2:291..2234"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS94572.1"
                     /db_xref="GeneID:30011"
                     /db_xref="HGNC:HGNC:13867"
                     /db_xref="MIM:300374"
ORIGIN      
        1 mveaivefdy qaqhddelti svgeiitnir kedggwwegq ingrrglfpd nfvreikkem
       61 kkdpltnkap ekplhevpsg nsllssetil rtnkrgerrr rrcqvafsyl pqnddelelk
      121 vgdiievvge veegwwegvl ngktgmfpsn fikelsgesd elgisqdeql sksrkttfeg
      181 tilyraapgk teghrryysl rettgsesdg gdssstkseg angtvataai qpkkvkgvgf
      241 gdifkdkpik lrprsieven dflpvektig kklpattatp dssktemdsr tkskdyckvi
      301 fpyeaqndde ltikegdivt linkdcidvg wwegelngrr gvfpdnfvkl lppdfekegn
      361 rpkkppppsa pvikqgagtt erkheikkip perpemlpnr teekerpere pkldlqkpsv
      421 paippkkprp pktnslsrpg alpprrperp vgplthtrgd spkidlagss lsgildkdls
      481 drsndidleg fdsvvsstek lshpttsrpk atgrrppsqs ltsvsdnkas lppkpgtmaa
      541 ggggpaplss aapsplsssl gtaghransp slfgtegkpk mepaassqaa veelrtqvre
      601 lrsiietmkd qqkreikqll seldeekkir lrlqmevndi kkalqsk
//
LOCUS       NP_001020095             894 aa            linear   PRI 20-NOV-2025
DEFINITION  exocyst complex component 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001020095
VERSION     NP_001020095.1
DBSOURCE    REFSEQ: accession NM_001024924.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 894)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 894)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 894)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 894)
  AUTHORS   Qian,X., Zhou,X., Shentu,P., Yao,Y., Jiao,D., Chen,Q., Zhou,J. and
            Xu,Y.
  TITLE     Sec3 knockdown inhibits TGF-beta induced epithelial-mesenchymal
            transition through the down-regulation of Akt phosphorylation in
            A549 cells
  JOURNAL   Biochem Biophys Res Commun 519 (2), 253-260 (2019)
   PUBMED   31495494
  REMARK    GeneRIF: study provides evidence that Sec3 is involved in TGF-beta
            induced cell migration and epithelial-mesenchymal transition
            processes, presumably through the regulation of PI3K/Akt signaling
            activation in A549 cancer cells
REFERENCE   5  (residues 1 to 894)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 894)
  AUTHORS   Hsu,S.C., TerBush,D., Abraham,M. and Guo,W.
  TITLE     The exocyst complex in polarized exocytosis
  JOURNAL   Int Rev Cytol 233, 243-265 (2004)
   PUBMED   15037366
  REMARK    Review article
REFERENCE   7  (residues 1 to 894)
  AUTHORS   Moskalenko,S., Tong,C., Rosse,C., Mirey,G., Formstecher,E.,
            Daviet,L., Camonis,J. and White,M.A.
  TITLE     Ral GTPases regulate exocyst assembly through dual subunit
            interactions
  JOURNAL   J Biol Chem 278 (51), 51743-51748 (2003)
   PUBMED   14525976
REFERENCE   8  (residues 1 to 894)
  AUTHORS   Inoue,M., Chang,L., Hwang,J., Chiang,S.H. and Saltiel,A.R.
  TITLE     The exocyst complex is required for targeting of Glut4 to the
            plasma membrane by insulin
  JOURNAL   Nature 422 (6932), 629-633 (2003)
   PUBMED   12687004
REFERENCE   9  (residues 1 to 894)
  AUTHORS   Matern,H.T., Yeaman,C., Nelson,W.J. and Scheller,R.H.
  TITLE     The Sec6/8 complex in mammalian cells: characterization of
            mammalian Sec3, subunit interactions, and expression of subunits in
            polarized cells
  JOURNAL   Proc Natl Acad Sci U S A 98 (17), 9648-9653 (2001)
   PUBMED   11493706
REFERENCE   10 (residues 1 to 894)
  AUTHORS   Brymora,A., Valova,V.A., Larsen,M.R., Roufogalis,B.D. and
            Robinson,P.J.
  TITLE     The brain exocyst complex interacts with RalA in a GTP-dependent
            manner: identification of a novel mammalian Sec3 gene and a second
            Sec15 gene
  JOURNAL   J Biol Chem 276 (32), 29792-29797 (2001)
   PUBMED   11406615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC110611.3, BC094751.1,
            BM468054.1 and AW589689.1.
            
            Summary: The protein encoded by this gene is a component of the
            exocyst complex, a multiple protein complex essential for targeting
            exocytic vesicles to specific docking sites on the plasma membrane.
            Though best characterized in yeast, the component proteins and
            functions of the exocyst complex have been demonstrated to be
            highly conserved in higher eukaryotes. At least eight components of
            the exocyst complex, including this protein, are found to interact
            with the actin cytoskeletal remodeling and vesicle transport
            machinery. Alternatively spliced transcript variants encoding
            distinct isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 5' UTR, as compared to variant 1. Variants 1 and 3 encode
            the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094751.1, SRR1803614.231929.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381295.7/ ENSP00000370695.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..894
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..894
                     /product="exocyst complex component 1 isoform 1"
                     /note="exocyst complex component Sec3; SEC3-like 1"
                     /calculated_mol_wt=101851
     Region          3..120
                     /region_name="PH-EXOC1"
                     /note="PH-like domain of Exocyst complex component 1;
                     cd14683"
                     /db_xref="CDD:270202"
     Region          184..871
                     /region_name="Sec3_C"
                     /note="Exocyst complex component Sec3; pfam09763"
                     /db_xref="CDD:401638"
     Region          439..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NV70.4)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NV70.4)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NV70.4)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NV70.4)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NV70.4)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NV70.4)"
     CDS             1..894
                     /gene="EXOC1"
                     /gene_synonym="BM-102; SEC3; SEC3L1; SEC3P"
                     /coded_by="NM_001024924.2:317..3001"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS3502.1"
                     /db_xref="GeneID:55763"
                     /db_xref="HGNC:HGNC:30380"
                     /db_xref="MIM:607879"
ORIGIN      
        1 mtaikhalqr diftpnderl lsivnvckag kkkkncflca tvtterpvqv kvvkvkksdk
       61 gdfykrqiaw alrdlavvda kdaikenpef dlhfekiykw vasstaekna fisciwklnq
      121 rylrkkidfv nvssqllees vpsgenqsvt ggdeevvdey qelnareeqd ieimmegcey
      181 aisnaeafae klsrelqvld ganiqsimas ekqvnilmkl ldealkevdq ielklssyee
      241 mlqsvkeqmd qisesnhlih lsntnnvkll seieflvnhm dlakghikal qegdlassrg
      301 ieactnaada llqcmnvalr pghdlllavk qqqqrfsdlr elfarrlash lnnvfvqqgh
      361 dqsstlaqhs veltlpnhhp fhrdllryak lmewlkstdy gkyegltkny mdylsrlyer
      421 eikdffevak ikmtgttkes kkfatlprke savkqetesl hgssgkltgs tsslnklsvq
      481 ssgnrrsqss slldmgnmsa sdldvadrtk fdkifeqvls eleplclaeq dfiskffklq
      541 qhqsmpgtma eaedldggtl srqhncgtpl pvssekdmir qmmikifrci epelnnlial
      601 gdkidsfnsl ymlvkmshhv wtaqnvdpas flsttlgnvl vtvkrnfdkc isnqirqmee
      661 vkiskkskvg ilpfvaefee faglaesifk naerrgdldk aytklirgvf vnvekvanes
      721 qktprdvvmm enfhhifatl srlkisclea ekkeakqkyt dhlqsyviys lgqpleklnh
      781 ffegvearva qgireeevsy qlafnkqelr kvikeypgke vkkgldnlyk kvdkhlceee
      841 nllqvvwhsm qdefirqykh fegliarcyp gsgvtmefti qdildycssi aqsh
//
LOCUS       NP_003312                455 aa            linear   PRI 20-NOV-2025
DEFINITION  elongation factor Tu, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_003312
VERSION     NP_003312.3
DBSOURCE    REFSEQ: accession NM_003321.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Zhang,J., Zhou,X.Y., Wang,A., Lai,Y.H., Zhang,X.F., Liu,X.T.,
            Wang,Z., Liu,Y.D., Tang,S.Y. and Chen,S.L.
  TITLE     Novel Tu translation elongation factor, mitochondrial (TUFM)
            homozygous variant in a consanguineous family with premature
            ovarian insufficiency
  JOURNAL   Clin Genet 104 (5), 516-527 (2023)
   PUBMED   37461298
  REMARK    GeneRIF: Novel Tu translation elongation factor, mitochondrial
            (TUFM) homozygous variant in a consanguineous family with premature
            ovarian insufficiency.
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Cipullo,M., Gese,G.V., Khawaja,A., Hallberg,B.M. and Rorbach,J.
  TITLE     Structural basis for late maturation steps of the human
            mitoribosomal large subunit
  JOURNAL   Nat Commun 12 (1), 3673 (2021)
   PUBMED   34135318
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Zhong,B.R., Zhou,G.F., Song,L., Wen,Q.X., Deng,X.J., Ma,Y.L.,
            Hu,L.T. and Chen,G.J.
  TITLE     TUFM is involved in Alzheimer's disease-like pathologies that are
            associated with ROS
  JOURNAL   FASEB J 35 (5), e21445 (2021)
   PUBMED   33774866
  REMARK    GeneRIF: TUFM is involved in Alzheimer's disease-like pathologies
            that are associated with ROS.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Girodat,D., Blanchard,S.C., Wieden,H.J. and Sanbonmatsu,K.Y.
  TITLE     Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA
            Selection
  JOURNAL   J Mol Biol 432 (9), 3064-3077 (2020)
   PUBMED   32061931
  REMARK    GeneRIF: Elongation Factor Tu Switch I Element is a Gate for
            Aminoacyl-tRNA Selection.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Chang,S.Y., Park,S.G., Kim,S. and Kang,C.Y.
  TITLE     Interaction of the C-terminal domain of p43 and the alpha subunit
            of ATP synthase. Its functional implication in endothelial cell
            proliferation
  JOURNAL   J Biol Chem 277 (10), 8388-8394 (2002)
   PUBMED   11741979
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Shah,Z.H., Migliosi,V., Miller,S.C., Wang,A., Friedman,T.B. and
            Jacobs,H.T.
  TITLE     Chromosomal locations of three human nuclear genes (RPSM12, TUFM,
            and AFG3L1) specifying putative components of the mitochondrial
            gene expression apparatus
  JOURNAL   Genomics 48 (3), 384-388 (1998)
   PUBMED   9545647
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Ling,M., Merante,F., Chen,H.S., Duff,C., Duncan,A.M. and
            Robinson,B.H.
  TITLE     The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA
            sequence, genomic localization, genomic structure, and
            identification of a pseudogene
  JOURNAL   Gene 197 (1-2), 325-336 (1997)
   PUBMED   9332382
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Woriax,V.L., Burkhart,W. and Spremulli,L.L.
  TITLE     Cloning, sequence analysis and expression of mammalian
            mitochondrial protein synthesis elongation factor Tu
  JOURNAL   Biochim Biophys Acta 1264 (3), 347-356 (1995)
   PUBMED   8547323
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Wells,J., Henkler,F., Leversha,M. and Koshy,R.
  TITLE     A mitochondrial elongation factor-like protein is over-expressed in
            tumours and differentially expressed in normal tissues
  JOURNAL   FEBS Lett 358 (2), 119-125 (1995)
   PUBMED   7828719
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133550.2, BC010041.2 and
            CA420396.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 25, 2003 this sequence version replaced NP_003312.2.
            
            Summary: This gene encodes a protein which participates in protein
            translation in mitochondria. Mutations in this gene have been
            associated with combined oxidative phosphorylation deficiency
            resulting in lactic acidosis and fatal encephalopathy. A pseudogene
            has been identified on chromosome 17. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.291522.1,
                                           SRR1803613.251890.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000313511.8/
                                                  ENSP00000322439.3
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..455
                     /product="elongation factor Tu, mitochondrial isoform 1
                     precursor"
                     /EC_number="3.6.5.3"
                     /note="elongation factor Tu, mitochondrial; EF-Tu;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=45045
     transit_peptide 1..46
                     /calculated_mol_wt=4848
     mat_peptide     47..455
                     /product="elongation factor Tu, mitochondrial isoform 1"
                     /calculated_mol_wt=45045
     Region          50..444
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
     Region          67..74
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P49411.3)"
     Site            82
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Region          108..112
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P49411.3)"
     Region          129..132
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P49411.3)"
     Region          184..187
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P49411.3)"
     Region          222..224
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P49411.3)"
     Site            259
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFR5; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BFR5; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     Site            421
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49411.3)"
     CDS             1..455
                     /gene="TUFM"
                     /gene_synonym="COXPD4; EF-TuMT; EFTU; P43"
                     /coded_by="NM_003321.5:80..1447"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10642.1"
                     /db_xref="GeneID:7284"
                     /db_xref="HGNC:HGNC:12420"
                     /db_xref="MIM:602389"
ORIGIN      
        1 mttmaaatll ratphfsgla agrtfllqgl lrllkapalp llcrglavea kktyvrdkph
       61 vnvgtighvd hgkttltaai tkilaeggga kfkkyeeidn apeerargit inaahveyst
      121 aarhyahtdc pghadyvknm itgtapldgc ilvvaandgp mpqtrehlll arqigvehvv
      181 vyvnkadavq dsemvelvel eirelltefg ykgeetpviv gsalcalegr dpelglksvq
      241 klldavdtyi pvpardlekp fllpveavys vpgrgtvvtg tlergilkkg decellghsk
      301 nirtvvtgie mfhkslerae agdnlgalvr glkredlrrg lvmvkpgsik phqkveaqvy
      361 ilskeeggrh kpfvshfmpv mfsltwdmac riilppekel ampgedlkfn lilrqpmile
      421 kgqrftlrdg nrtigtglvt ntlamteeek nikwg
//
LOCUS       NP_001304310             870 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock 70 kDa protein 4L isoform 2 [Homo sapiens].
ACCESSION   NP_001304310
VERSION     NP_001304310.1
DBSOURCE    REFSEQ: accession NM_001317381.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 870)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 870)
  AUTHORS   Zhu,M., Huang,Y., Tang,J., Shao,S., Zhang,L., Zhou,Y., He,S. and
            Wang,Y.
  TITLE     Role of Apg-1 in HSF1 activation and bortezomib sensitivity in
            myeloma cells
  JOURNAL   Exp Hematol 81, 50-59 (2020)
   PUBMED   31899217
  REMARK    GeneRIF: Apg-1 knockdown sensitized myeloma cells to bortezomib
            treatment, which may provide a new approach in multiple myeloma
            treatment.
REFERENCE   3  (residues 1 to 870)
  AUTHORS   Liu,X., Wang,X. and Liu,F.
  TITLE     Decreased expression of heat shock protein A4L in spermatozoa is
            positively related to poor human sperm quality
  JOURNAL   Mol Reprod Dev 86 (4), 379-386 (2019)
   PUBMED   30637842
  REMARK    GeneRIF: decreased expression of HSPA4L in immature and
            asthenozoospermic spermatozoa was validated by western blot
            analysis. Functional analysis revealed a correlation between HSPA4L
            and sperm motility by Spearman correlation analysis and its
            involvement in sperm-oocyte penetration by the human sperm-hamster
            egg penetration test.
REFERENCE   4  (residues 1 to 870)
  AUTHORS   Wang,S., Mo,Y., Midorikawa,K., Zhang,Z., Huang,G., Ma,N., Zhao,W.,
            Hiraku,Y., Oikawa,S. and Murata,M.
  TITLE     The potent tumor suppressor miR-497 inhibits cancer phenotypes in
            nasopharyngeal carcinoma by targeting ANLN and HSPA4L
  JOURNAL   Oncotarget 6 (34), 35893-35907 (2015)
   PUBMED   26486082
  REMARK    GeneRIF: Findings indicate that miR-497 is a potent tumor
            suppressor that inhibits cancer phenotypes by targeting ANLN and
            HSPA4L in NPC.
REFERENCE   5  (residues 1 to 870)
  AUTHORS   Kuo,Y., Ren,S., Lao,U., Edgar,B.A. and Wang,T.
  TITLE     Suppression of polyglutamine protein toxicity by co-expression of a
            heat-shock protein 40 and a heat-shock protein 110
  JOURNAL   Cell Death Dis 4 (10), e833 (2013)
   PUBMED   24091676
  REMARK    GeneRIF: HSP40 and HSP110 function together in protein homeostasis
            control.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 870)
  AUTHORS   Mala,J.G. and Takeuchi,S.
  TITLE     Molecular cloning of OSP94: A significant biomarker protein of
            hypertensive human heart and a member of HSP110 family
  JOURNAL   Mol Biotechnol 42 (2), 175-194 (2009)
   PUBMED   19169850
REFERENCE   7  (residues 1 to 870)
  AUTHORS   Takahashi,H., Furukawa,T., Yano,T., Sato,N., Takizawa,J.,
            Kurasaki,T., Abe,T., Narita,M., Masuko,M., Koyama,S., Toba,K.,
            Takahashi,M. and Aizawa,Y.
  TITLE     Identification of an overexpressed gene, HSPA4L, the product of
            which can provoke prevalent humoral immune responses in leukemia
            patients
  JOURNAL   Exp Hematol 35 (7), 1091-1099 (2007)
   PUBMED   17588478
REFERENCE   8  (residues 1 to 870)
  AUTHORS   Colgan,S.P., Pitman,R.S., Nagaishi,T., Mizoguchi,A., Mizoguchi,E.,
            Mayer,L.F., Shao,L., Sartor,R.B., Subjeck,J.R. and Blumberg,R.S.
  TITLE     Intestinal heat shock protein 110 regulates expression of CD1d on
            intestinal epithelial cells
  JOURNAL   J Clin Invest 112 (5), 745-754 (2003)
   PUBMED   12952923
  REMARK    GeneRIF: a novel autocrine pathway of CD1d regulation by Hsp110.
REFERENCE   9  (residues 1 to 870)
  AUTHORS   Nonoguchi,K., Tokuchi,H., Okuno,H., Watanabe,H., Egawa,H.,
            Saito,K., Ogawa,O. and Fujita,J.
  TITLE     Expression of Apg-1, a member of the Hsp110 family, in the human
            testis and sperm
  JOURNAL   Int J Urol 8 (6), 308-314 (2001)
   PUBMED   11389747
REFERENCE   10 (residues 1 to 870)
  AUTHORS   Nonoguchi,K., Itoh,K., Xue,J.H., Tokuchi,H., Nishiyama,H.,
            Kaneko,Y., Tatsumi,K., Okuno,H., Tomiwa,K. and Fujita,J.
  TITLE     Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110
            family, and chromosomal assignment of their genes
  JOURNAL   Gene 237 (1), 21-28 (1999)
   PUBMED   10524232
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093591.3, AK303053.1,
            BC040560.1 and BM679019.1.
            
            Summary: The protein encoded by this gene is heat shock inducible
            and may act as a chaperone. The encoded protein can protect the
            heat-shocked cell against the harmful effects of aggregated
            proteins. This gene is highly expressed in leukemia cells and may
            be a good target for therapeutic intervention. Several transcripts
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            longer at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303053.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..870
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28.1"
     Protein         1..870
                     /product="heat shock 70 kDa protein 4L isoform 2"
                     /note="heat shock protein (hsp110 family); heat shock 70
                     kDa protein 4L; testis tissue sperm-binding protein Li
                     64n; heat shock 70 kDa protein 4-like protein; osmotic
                     stress protein 94; heat shock 70-related protein APG-1;
                     heat shock 70kDa protein 4-like; HSPA4-like protein;
                     heat-shock protein family A member 4-like protein; heat
                     shock protein family H member 3"
                     /calculated_mol_wt=97528
     Region          33..415
                     /region_name="ASKHA_NBD_HSP70_HSPA4L"
                     /note="nucleotide-binding domain (NBD) of heat shock 70
                     kDa protein 4L (HSPA4L) and similar proteins; cd11738"
                     /db_xref="CDD:466844"
     CDS             1..870
                     /gene="HSPA4L"
                     /gene_synonym="APG-1; APG1; HSPH3; Osp94"
                     /coded_by="NM_001317381.2:265..2877"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:22824"
                     /db_xref="HGNC:HGNC:17041"
                     /db_xref="MIM:619077"
ORIGIN      
        1 msrnpssnsp eedtvpvpkg svpaarpsrg gmsvvgidlg flncyiavar sggietiane
       61 ysdrctpaci slgsrtraig naaksqivtn vrntihgfkk lhgrsfddpi vqterirlpy
      121 elqkmpngsa gvkvryleee rpfaieqvtg mllaklkets enalkkpvad cvisipsfft
      181 daerrsvmaa aqvaglnclr lmnettaval aygiykqdlp pldekprnvv fidmghsayq
      241 vlvcafnkgk lkvlattfdp ylggrnfdea lvdyfcdefk tkykinvken srallrlyqe
      301 ceklkklmsa nasdlplnie cfmndldvss kmnraqfeql casllarvep plkavmeqan
      361 lqredissie ivggatripa vkeqitkffl kdisttlnad eavargcalq cailspafkv
      421 refsitdlvp ysitlrwkts fedgsgecev fcknhpapfs kvitfhkkep feleafytnl
      481 hevpypdari gsftiqnvfp qsdgdsskvk vkvrvnihgi fsvasasvie kqnlegdhsd
      541 apmetetsfk nenkdnmdkm qvdqeeghqk chaehtpeee idhtgaktks avsdkqdrln
      601 qtlkkgkvks idlpiqsslc rqlgqdllns yienegkmim qdklekernd aknaveeyvy
      661 dfrdrlgtvy ekfitpedls klsavledte nwlyedgedq pkqvyvdklq elkkygqpiq
      721 mkymeheerp kalndlgkki qlvmkvieay rnkderydhl dptemekvek cisdamswln
      781 skmnaqnkls ltqdpvvkvs eivakskeld nfcnpiiykp kpkaevpedk pkansehngp
      841 mdgqsgtetk sdstkdssqh tkssgemevd
//
LOCUS       NP_065917                748 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_065917
VERSION     NP_065917.1
DBSOURCE    REFSEQ: accession NM_020866.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Sood,R.F., Westenberg,R.F., Winograd,J.M., Eberlin,K.R. and
            Chen,N.C.
  TITLE     Genetic Risk of Trigger Finger: Results of a Genomewide Association
            Study
  JOURNAL   Plast Reconstr Surg 146 (2), 165e-176e (2020)
   PUBMED   32740585
  REMARK    GeneRIF: Genetic Risk of Trigger Finger: Results of a Genomewide
            Association Study.
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Mena,E.L., Kjolby,R.A.S., Saxton,R.A., Werner,A., Lew,B.G.,
            Boyle,J.M., Harland,R. and Rape,M.
  TITLE     Dimerization quality control ensures neuronal development and
            survival
  JOURNAL   Science 362 (6411) (2018)
   PUBMED   30190310
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   6  (residues 1 to 748)
  AUTHORS   Aromolaran,K.A., Benzow,K.A., Cribbs,L.L., Koob,M.D. and
            Piedras-Renteria,E.S.
  TITLE     T-type current modulation by the actin-binding protein Kelch-like 1
  JOURNAL   Am J Physiol Cell Physiol 298 (6), C1353-C1362 (2010)
   PUBMED   20147652
  REMARK    GeneRIF: KLHL1 interacts with Cav3.2 and modulates T-type calcium
            currents by increasing current deactivation kinetics and current
            density and calcium influx.
REFERENCE   7  (residues 1 to 748)
  AUTHORS   Chen,W.L., Lin,J.W., Huang,H.J., Wang,S.M., Su,M.T., Lee-Chen,G.J.,
            Chen,C.M. and Hsieh-Li,H.M.
  TITLE     SCA8 mRNA expression suggests an antisense regulation of KLHL1 and
            correlates to SCA8 pathology
  JOURNAL   Brain Res 1233, 176-184 (2008)
   PUBMED   18708037
  REMARK    GeneRIF: KLHL1 was expressed in human brain and kidney, but was
            also in other tissues, such as prostate gland, small intestine,
            colon, testis (but not the ovaries), liver and pancreas.
REFERENCE   8  (residues 1 to 748)
  AUTHORS   Aromolaran,K.A., Benzow,K.A., Koob,M.D. and Piedras-Renteria,E.S.
  TITLE     The Kelch-like protein 1 modulates P/Q-type calcium current density
  JOURNAL   Neuroscience 145 (3), 841-850 (2007)
   PUBMED   17289272
  REMARK    GeneRIF: modulatory effect of KLHL1 on the P/Q-type calcium channel
            function, suggesting a possible novel role for KLHL1 in cellular
            excitability.
REFERENCE   9  (residues 1 to 748)
  AUTHORS   Seng,S., Avraham,H.K., Jiang,S., Venkatesh,S. and Avraham,S.
  TITLE     KLHL1/MRP2 mediates neurite outgrowth in a glycogen synthase kinase
            3beta-dependent manner
  JOURNAL   Mol Cell Biol 26 (22), 8371-8384 (2006)
   PUBMED   16982692
  REMARK    GeneRIF: This study provides, for the first time, insights into the
            involvement of MRP2 in neurite outgrowth, which occurs in a
            GSK3beta-dependent manner.
REFERENCE   10 (residues 1 to 748)
  AUTHORS   Nemes,J.P., Benzow,K.A., Moseley,M.L., Ranum,L.P. and Koob,M.D.
  TITLE     The SCA8 transcript is an antisense RNA to a brain-specific
            transcript encoding a novel actin-binding protein (KLHL1)
  JOURNAL   Hum Mol Genet 9 (10), 1543-1551 (2000)
   PUBMED   10888605
  REMARK    Erratum:[Hum Mol Genet 2000 Nov 1;9(18):2777]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK291435.1, AF252283.1 and BC022460.1.
            
            Summary: The KLHL1 protein belongs to a family of actin-organizing
            proteins related to Drosophila Kelch (Nemes et al., 2000 [PubMed
            10888605]).[supplied by OMIM, Feb 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022460.1, AB040923.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465404
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377844.9/ ENSP00000367075.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q21.33"
     Protein         1..748
                     /product="kelch-like protein 1 isoform 1"
                     /note="Mayven-related protein 2; Kelch-like protein 1"
                     /calculated_mol_wt=82549
     Region          22..93
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          151..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          206..728
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          460..506
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          496..539
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          507..553
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          543..587
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          555..600
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          590..633
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          601..647
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          637..687
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          649..700
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     Region          690..734
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          701..747
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR64.1)"
     CDS             1..748
                     /gene="KLHL1"
                     /gene_synonym="MRP2"
                     /coded_by="NM_020866.3:754..3000"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9445.1"
                     /db_xref="GeneID:57626"
                     /db_xref="HGNC:HGNC:6352"
                     /db_xref="MIM:605332"
ORIGIN      
        1 msgsgrkdfd vkhilrlrwk lfshpspstg gpagggclqq dgsgsfehwg psqsrllksq
       61 ersgvstfwk kpssssssss spssssssfn plngtllpva trlqqgapgq gtqqpartlf
      121 yvesleeevv pgmdfpgphe kglvlqelkv epdnssqatg egcghrlsst ghsmtpqsdl
      181 dsssseefyq avhhaeqtfr kmesylkqqq lcdvilivgn rkipahrlvl ssvsdyfaam
      241 ftsdvceakq eeikmegidp nalwdlvqfa ytgclelked tienllaaac llqlpqvvev
      301 cchflmkllh psnclgiraf adaqgcielm kvahsytmen imevirnqef lllpaeelhk
      361 llasddvnvp deetifhalm mwvkydmqsr cndlsmllaf irlpllppqi ladlenhalf
      421 kndlecqkli leamkyhllp errtlmqspr tkprkstvgt lyavggmdnn kgattiekyd
      481 lrtnlwiqag mmngrrlqfg vaviddklfv iggrdglktl ntvecynpkt ktwtvlppms
      541 thrhglgvtv legpiyavgg hdgwsylntv erwdpqsqqw tfvasmsiar stvgvaalng
      601 klysvggrdg ssclssmeyy dphtnkwnmc apmckrrggv gvatcdgfly avgghdapas
      661 nhcsrlldyv erydpktdtw tmvaplsmpr davgvcllgd rlyavggydg qtylntmesy
      721 dpqtnewtqm aslnigraga cvvvikqp
//
LOCUS       NP_001309171             233 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_001309171 XP_011527265
VERSION     NP_001309171.1
DBSOURCE    REFSEQ: accession NM_001322242.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL160175.5 and BC019307.1.
            
            On Apr 8, 2016 this sequence version replaced XP_011527265.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380199.51148.3,
                                           SRR6380199.94416.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_001322242.2:197..898"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     9"
                     /db_xref="CCDS:CCDS13189.1"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001271137             326 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 5 isoform 4 [Homo sapiens].
ACCESSION   NP_001271137
VERSION     NP_001271137.1
DBSOURCE    REFSEQ: accession NM_001284208.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Radko-Juettner,S., Yue,H., Myers,J.A., Carter,R.D., Robertson,A.N.,
            Mittal,P., Zhu,Z., Hansen,B.S., Donovan,K.A., Hunkeler,M.,
            Rosikiewicz,W., Wu,Z., McReynolds,M.G., Roy Burman,S.S.,
            Schmoker,A.M., Mageed,N., Brown,S.A., Mobley,R.J., Partridge,J.F.,
            Stewart,E.A., Pruett-Miller,S.M., Nabet,B., Peng,J., Gray,N.S.,
            Fischer,E.S. and Roberts,C.W.M.
  TITLE     Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing
            SWI/SNF
  JOURNAL   Nature 628 (8007), 442-449 (2024)
   PUBMED   38538798
  REMARK    GeneRIF: Targeting DCAF5 suppresses SMARCB1-mutant cancer by
            stabilizing SWI/SNF.
            Erratum:[Nature. 2024 May;629(8012):E12. doi:
            10.1038/s41586-024-07402-3. PMID: 38684813]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Zhang,C., Leng,F., Saxena,L., Hoang,N., Yu,J., Alejo,S., Lee,L.,
            Qi,D., Lu,F., Sun,H. and Zhang,H.
  TITLE     Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and
            CRL4DCAF5 ubiquitin ligase
  JOURNAL   J Biol Chem 294 (2), 476-489 (2019)
   PUBMED   30442713
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Leng,F., Yu,J., Zhang,C., Alejo,S., Hoang,N., Sun,H., Lu,F. and
            Zhang,H.
  TITLE     Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3
            and CRL4DCAF5 ubiquitin ligase
  JOURNAL   Nat Commun 9 (1), 1641 (2018)
   PUBMED   29691401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Lynch,R.A., Piper,M., Bankier,A., Bhugra,B., Surti,U., Liu,J.,
            Buckler,A., Dear,P.H. and Menon,A.G.
  TITLE     Genomic and functional map of the chromosome 14 t(12;14) breakpoint
            cluster region in uterine leiomyoma
  JOURNAL   Genomics 52 (1), 17-26 (1998)
   PUBMED   9740667
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK094283.1, BC022967.1 and DB507867.1.
            
            Transcript Variant: This variant (4) lacks multiple 3' exons and
            contains an alternate 3' exon, resulting in a distinct 3' coding
            region and 3' UTR, compared to variant 1. The encoded isoform (4)
            is shorter and has a distinct C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022967.1, SRR1660809.149094.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..326
                     /product="DDB1- and CUL4-associated factor 5 isoform 4"
                     /note="breakpoint cluster region protein, uterine
                     leiomyoma, 2; WD repeat-containing protein 22"
                     /calculated_mol_wt=36459
     Region          <49..250
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          51..91
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          57..98
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          99..139
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          104..139
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          140..180
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          146..187
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          185..225
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          191..228
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..326
                     /gene="DCAF5"
                     /gene_synonym="BCRG2; BCRP2; D14S1461E; WDR22"
                     /coded_by="NM_001284208.2:142..1122"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS73646.1"
                     /db_xref="GeneID:8816"
                     /db_xref="HGNC:HGNC:20224"
                     /db_xref="MIM:603812"
ORIGIN      
        1 mkrraglggs mrsvvgflsq rglhgdpllt qdfqrrrlrg crnlykkdll ghfgcvnaie
       61 fsnnggqwlv sggddrrvll whmeqaihsr vkpiqlkgeh hsnifclafn sgntkvfsgg
      121 ndeqvilhdv essetldvfa hedavyglsv spvndnifas ssddgrvliw diresphgep
      181 fclanypsaf hsvmfnpvep rllatanske gvglwdirkp qssllryggn lslqsamsvr
      241 fnsngtqlla lrrrlppvly dihsrlpvfq fdnqgyfnsc tmksccfagd rdqhhnwkwr
      301 aqavsfqpfl sltrngdadv dlklav
//
LOCUS       NP_001247                824 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001247
VERSION     NP_001247.3
DBSOURCE    REFSEQ: accession NM_001256.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY023336.1, S78234.1,
            AC002558.2 and AA927469.1.
            
            On Feb 8, 2008 this sequence version replaced NP_001247.2.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (2) that is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853558.10627.1,
                                           SRR14038193.4312364.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000066544.8/ ENSP00000066544.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..824
                     /product="cell division cycle protein 27 homolog isoform
                     2"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=91737
     Region          6..35
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          17..92
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          38..65
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          67..99
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          115..145
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Region          287..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          448..>671
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          465..495
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          499..528
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          501..527
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          533..563
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          561..>731
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          567..598
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          567..595
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(568,571..572,575..576,578,602,605..606,609..610,
                     612..613,636,639..640,643..644,647)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          600..630
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          601..631
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          635..667
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          635..663
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <665..804
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          669..696
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          670..702
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          703..731
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          704..734
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          737..768
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          737..765
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          781..824
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22139841; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     CDS             1..824
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001256.6:124..2598"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11509.1"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mtvlqepvqa aiwqalnhya yrdavflaer lyaevhseea lfllatcyyr sgkaykayrl
       61 lkghscttpq ckyllakccv dlsklaegeq ilsggvfnkq kshddivtef gdsacftlsl
      121 lghvycktdr lakgsecyqk slslnpflws pfeslceige kpdpdqtfkf tslqnfsncl
      181 pnscttqvpn hslshrqpet vltetpqdti elnrlnless nskyslntds svsyidsavi
      241 spdtvplgtg tsilskqvqn kpktgrsllg gpaalspltp sfgilpletp spgdgsylqn
      301 ytntppvidv pstgapskks varigqtgtk svfsqsgnsr evtpilaqtq ssgpqtsttp
      361 qvlsptitsp pnalprrssr lftsdssttk enskklkmkf ppkipnrktk sktnkggitq
      421 pnindsleit kldssiiseg kistitpqiq afnlqkaaae glmsllremg kgylalcsyn
      481 ckeainilsh lpshhyntgw vlcqigrayf elseymqaer ifsevrrien yrvegmeiys
      541 ttlwhlqkdv alsvlskdlt dmdknspeaw caagncfslq rehdiaikff qraiqvdpny
      601 ayaytllghe fvlteeldka lacfrnairv nprhynawyg lgmiyykqek fslaemhfqk
      661 aldinpqssv llchigvvqh alkksekald tlnkaividp knplckfhra svlfanekyk
      721 salqeleelk qivpkeslvy fligkvykkl gqthlalmnf swamdldpkg annqikeaid
      781 krylpddeep itqeeqimgt desqessmtd addtqlhaae sdef
//
LOCUS       NP_079187                541 aa            linear   PRI 20-NOV-2025
DEFINITION  protein wntless homolog isoform 1 [Homo sapiens].
ACCESSION   NP_079187
VERSION     NP_079187.3
DBSOURCE    REFSEQ: accession NM_024911.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Abdel-Salam,G.M.H., Afifi,H.H., Abdel-Hamid,M.S., Ahmed,N.E.B.,
            Taher,M.B., El-Kamah,G., Thiele,H., Nurnberg,P.N. and Bolz,H.J.
  TITLE     Expanding the phenotypic spectrum and clinical severity associated
            with WLS gene
  JOURNAL   J Hum Genet 68 (9), 607-613 (2023)
   PUBMED   37106064
  REMARK    GeneRIF: Expanding the phenotypic spectrum and clinical severity
            associated with WLS gene.
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Yu,C., Wang,C., Zhou,W., Zhang,A., Jia,Z., Zheng,B. and Ding,G.
  TITLE     Compound heterozygous variants in WLS gene causes Zaki syndrome
  JOURNAL   Clin Genet 104 (2), 226-229 (2023)
   PUBMED   37005218
  REMARK    GeneRIF: Compound heterozygous variants in WLS gene causes Zaki
            syndrome.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Kantaputra,P., Tripuwabhrut,K., Jatooratthawichot,P.,
            Adisornkanj,P., Hatsadaloi,A., Porntrakoolsaree,N., Kaewgaya,M.,
            Olsen,B., Tongsima,S., Ngamphiw,C. and Ketudat Cairns,J.R.
  TITLE     Mutations in the WLS are associated with dental anomalies, torus
            palatinus, and torus mandibularis
  JOURNAL   Eur J Orthod 45 (3), 317-323 (2023)
   PUBMED   36374649
  REMARK    GeneRIF: Mutations in the WLS are associated with dental anomalies,
            torus palatinus, and torus mandibularis.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Wolf,L. and Boutros,M.
  TITLE     The role of Evi/Wntless in exporting Wnt proteins
  JOURNAL   Development 150 (3) (2023)
   PUBMED   36763105
  REMARK    GeneRIF: The role of Evi/Wntless in exporting Wnt proteins.
            Review article
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Belenkaya,T.Y., Wu,Y., Tang,X., Zhou,B., Cheng,L., Sharma,Y.V.,
            Yan,D., Selva,E.M. and Lin,X.
  TITLE     The retromer complex influences Wnt secretion by recycling wntless
            from endosomes to the trans-Golgi network
  JOURNAL   Dev Cell 14 (1), 120-131 (2008)
   PUBMED   18160348
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Binnerts,M.E., Kim,K.A., Bright,J.M., Patel,S.M., Tran,K., Zhou,M.,
            Leung,J.M., Liu,Y., Lomas,W.E. 3rd, Dixon,M., Hazell,S.A.,
            Wagle,M., Nie,W.S., Tomasevic,N., Williams,J., Zhan,X., Levy,M.D.,
            Funk,W.D. and Abo,A.
  TITLE     R-Spondin1 regulates Wnt signaling by inhibiting internalization of
            LRP6
  JOURNAL   Proc Natl Acad Sci U S A 104 (37), 14700-14705 (2007)
   PUBMED   17804805
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Bartscherer,K., Pelte,N., Ingelfinger,D. and Boutros,M.
  TITLE     Secretion of Wnt ligands requires Evi, a conserved transmembrane
            protein
  JOURNAL   Cell 125 (3), 523-533 (2006)
   PUBMED   16678096
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Banziger,C., Soldini,D., Schutt,C., Zipperlen,P., Hausmann,G. and
            Basler,K.
  TITLE     Wntless, a conserved membrane protein dedicated to the secretion of
            Wnt proteins from signaling cells
  JOURNAL   Cell 125 (3), 509-522 (2006)
   PUBMED   16678095
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DQ323735.1 and AW137622.1.
            
            On Jun 9, 2003 this sequence version replaced NP_079187.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074984.1, DQ323735.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262348.9/ ENSP00000262348.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..541
                     /product="protein wntless homolog isoform 1"
                     /note="G protein-coupled receptor 177; integral membrane
                     protein GPR177; putative NFkB activating protein 373;
                     protein evenness interrupted homolog; putative
                     NF-kappa-B-activating protein 373; wntless Wnt ligand
                     secretion mediator"
                     /calculated_mol_wt=62122
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Region          101..232
                     /region_name="Interaction with Wnt proteins.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Region          178..496
                     /region_name="MIG-14_Wnt-bd"
                     /note="Wnt-binding factor required for Wnt secretion;
                     pfam06664"
                     /db_xref="CDD:461980"
     Site            233..253
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            269..289
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            304..324
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            332..352
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            432..452
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     Site            472..492
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5T9L3.2)"
     CDS             1..541
                     /gene="WLS"
                     /gene_synonym="C1orf139; EVI; GPR177; mig-14; MRP; ZKS"
                     /coded_by="NM_024911.7:225..1850"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS642.1"
                     /db_xref="GeneID:79971"
                     /db_xref="HGNC:HGNC:30238"
                     /db_xref="MIM:611514"
ORIGIN      
        1 magaiienms tkklcivggi llvfqiiafl vggliapgpt tavsymsvkc vdarknhhkt
       61 kwfvpwgpnh cdkirdieea ipreieandi vfsvhiplph memspwfqfm lfilqldiaf
      121 klnnqirena evsmdvslay rddafaewte mahervprkl kctftspktp ehegryyecd
      181 vlpfmeigsv ahkfyllnir lpvnekkkin vgigeikdir lvgihqnggf tkvwfamktf
      241 ltpsifiimv wywrritmms rppvllekvi falgismtfi nipvewfsig fdwtwmllfg
      301 dirqgifyam llsfwiifcg ehmmdqhern hiagywkqvg piavgsfclf ifdmcergvq
      361 ltnpfysiwt tdigtelama fiivagiclc lyflflcfmv fqvfrnisgk qsslpamskv
      421 rrlhyeglif rfkflmlitl acaamtviff ivsqvteghw kwggvtvqvn safftgiygm
      481 wnlyvfalmf lyapshknyg edqsngdlgv hsgeelqltt tithvdgpte iykltrkeaq
      541 e
//
LOCUS       NP_001339879             651 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 20 [Homo sapiens].
ACCESSION   NP_001339879 XP_016868773
VERSION     NP_001339879.1
DBSOURCE    REFSEQ: accession NM_001352950.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868773.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.277764.1,
                                           SRR1803614.30404.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..651
                     /product="DNA repair-scaffolding protein isoform 20"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=71712
     Region          <11..205
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          357..>650
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..651
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352950.1:410..2365"
                     /note="isoform 20 is encoded by transcript variant 25"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mkirhflsyr epssieiley ssdsekeddl envllidses phkyhvqfas darqimerli
       61 dprtksteti lhtpqkptak fprtpensak kkllrgglae rlnglqnrer saislwrhqc
      121 isyqktlsgr ksgvltvkil elheecamqv amceqllgsp atsssqsvap rpgaglkvlf
      181 tketagylrg rpqdtvrifp pwqkliipsg scpvilntyf cekvvakeds ektcevycpd
      241 iplprrsisl aqmfvikglt nnspeiqvvc sgvattgtaw thghkeakqr iptstplrds
      301 lldvvesqga aswpgagvrv vvqrvyslps rdstrgqqga ssghtdpagt racllvqdac
      361 gmfgevhlef tmskarqleg kscslvgmkv lqkvtrgrta gifslidtlw ppaiplktpg
      421 rdqpceeikt hlpppalcyi ltahpnlgqi diidedpiyk lyqppvtrcl rdilqmndlg
      481 trcsfyatvi yqkpqlksll lleqreiwll vtdvtlqtke erdprlpktl lvyvaplcvl
      541 gsevlealag aaphslffkd alrdqgrivc aertvlllqk pllsvvsgas scelpgpvml
      601 dsldsatpvn sicsvqgtvv gvdestafsw pvcdmcgngr leqrpedrat k
//
LOCUS       NP_003496                647 aa            linear   PRI 20-NOV-2025
DEFINITION  frizzled-1 [Homo sapiens].
ACCESSION   NP_003496
VERSION     NP_003496.1
DBSOURCE    REFSEQ: accession NM_003505.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Palomer,E., Martin-Flores,N., Jolly,S., Pascual-Vargas,P.,
            Benvegnu,S., Podpolny,M., Teo,S., Vaher,K., Saito,T., Saido,T.C.,
            Whiting,P. and Salinas,P.C.
  TITLE     Epigenetic repression of Wnt receptors in AD: a role for
            Sirtuin2-induced H4K16ac deacetylation of Frizzled1 and Frizzled7
            promoters
  JOURNAL   Mol Psychiatry 27 (7), 3024-3033 (2022)
   PUBMED   35296808
  REMARK    GeneRIF: Epigenetic repression of Wnt receptors in AD: a role for
            Sirtuin2-induced H4K16ac deacetylation of Frizzled1 and Frizzled7
            promoters.
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Zhang,Y.P., Gao,D. and Wu,P.
  TITLE     [RBM38 Mediates the Proliferation of Acute Myeloid Leukemia Cells
            HL-60 by Regulating FZD1 mRNA Stability]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 29 (6), 1775-1779 (2021)
   PUBMED   34893109
  REMARK    GeneRIF: [RBM38 Mediates the Proliferation of Acute Myeloid
            Leukemia Cells HL-60 by Regulating FZD1 mRNA Stability].
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Huang,Y., He,P. and Ding,J.
  TITLE     Protein disulfide isomerase family 6 promotes the
            imatinib-resistance of renal cell carcinoma by regulation of
            Wnt3a-Frizzled1 axis
  JOURNAL   Bioengineered 12 (2), 12157-12166 (2021)
   PUBMED   34781823
  REMARK    GeneRIF: Protein disulfide isomerase family 6 promotes the
            imatinib-resistance of renal cell carcinoma by regulation of
            Wnt3a-Frizzled1 axis.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Wang,R., Wang,X., Zhang,J. and Liu,Y.
  TITLE     LINC00942 Promotes Tumor Proliferation and Metastasis in Lung
            Adenocarcinoma via FZD1 Upregulation
  JOURNAL   Technol Cancer Res Treat 20, 1533033820977526 (2021)
   PUBMED   34253104
  REMARK    GeneRIF: LINC00942 Promotes Tumor Proliferation and Metastasis in
            Lung Adenocarcinoma via FZD1 Upregulation.
REFERENCE   6  (residues 1 to 647)
  AUTHORS   DeCostanzo,A.J., Huang,X.P., Wang,H.Y. and Malbon,C.C.
  TITLE     The Frizzled-1/(beta(2))-adrenergic receptor chimera:
            pharmacological properties of a unique G protein-linked receptor
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 365 (5), 341-348 (2002)
   PUBMED   12012019
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Bafico,A., Liu,G., Yaniv,A., Gazit,A. and Aaronson,S.A.
  TITLE     Novel mechanism of Wnt signalling inhibition mediated by Dickkopf-1
            interaction with LRP6/Arrow
  JOURNAL   Nat Cell Biol 3 (7), 683-686 (2001)
   PUBMED   11433302
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Gazit,A., Yaniv,A., Bafico,A., Pramila,T., Igarashi,M.,
            Kitajewski,J. and Aaronson,S.A.
  TITLE     Human frizzled 1 interacts with transforming Wnts to transduce a
            TCF dependent transcriptional response
  JOURNAL   Oncogene 18 (44), 5959-5966 (1999)
   PUBMED   10557084
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Sagara,N., Toda,G., Hirai,M., Terada,M. and Katoh,M.
  TITLE     Molecular cloning, differential expression, and chromosomal
            localization of human frizzled-1, frizzled-2, and frizzled-7
  JOURNAL   Biochem Biophys Res Commun 252 (1), 117-122 (1998)
   PUBMED   9813155
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Tanaka,S., Akiyoshi,T., Mori,M., Wands,J.R. and Sugimachi,K.
  TITLE     A novel frizzled gene identified in human esophageal carcinoma
            mediates APC/beta-catenin signals
  JOURNAL   Proc Natl Acad Sci U S A 95 (17), 10164-10169 (1998)
   PUBMED   9707618
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC084381.6 and AB017363.1.
            
            Summary:  Members of the 'frizzled' gene family encode
            7-transmembrane domain proteins that are receptors for Wnt
            signaling proteins.  The FZD1 protein contains a signal peptide, a
            cysteine-rich domain in the N-terminal extracellular region, 7
            transmembrane domains, and a C-terminal PDZ domain-binding motif.
            The FZD1 transcript is expressed in various tissues. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AB017363.1, BC051271.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287934.4/ ENSP00000287934.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.13"
     Protein         1..647
                     /product="frizzled-1"
                     /note="Wnt receptor; frizzled 1, seven transmembrane
                     spanning receptor; frizzled family receptor 1; frizzled,
                     Drosophila, homolog of, 1; fz-1; fzE1; hFz1; frizzled
                     homolog 1"
                     /calculated_mol_wt=71028
     Region          112..238
                     /region_name="CRD_FZ1"
                     /note="Cysteine-rich Wnt-binding domain (CRD) of the
                     frizzled 1 (Fz1) receptor; cd07465"
                     /db_xref="CDD:143574"
     Site            order(123,125..127,129..131)
                     /site_type="other"
                     /note="putative Wnt binding site [polypeptide binding]"
                     /db_xref="CDD:143574"
     Region          299..646
                     /region_name="7tmF_FZD1"
                     /note="class F mammalian frizzled subfamily 1, member of
                     7-transmembrane G protein-coupled receptors; cd15247"
                     /db_xref="CDD:320375"
     Site            order(310,319,369,389,471,476,478,481..482,487,562,
                     565..566,598,603,606..607)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320375"
     Region          318..343
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320375"
     Region          352..373
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320375"
     Region          403..429
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320375"
     Region          446..462
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320375"
     Region          484..513
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320375"
     Region          533..560
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320375"
     Region          596..621
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320375"
     CDS             1..647
                     /gene="FZD1"
                     /coded_by="NM_003505.2:449..2392"
                     /db_xref="CCDS:CCDS5620.1"
                     /db_xref="GeneID:8321"
                     /db_xref="HGNC:HGNC:4038"
                     /db_xref="MIM:603408"
ORIGIN      
        1 maeeeapkks raagggaswe lcagalsarl aeegsgdagg rrrppvdprr larqlllllw
       61 lleaplllgv raqaagqgpg qgpgpgqqpp pppqqqqsgq qyngergisv pdhgycqpis
      121 iplctdiayn qtimpnllgh tnqedaglev hqfyplvkvq csaelkfflc smyapvctvl
      181 eqalppcrsl cerarqgcea lmnkfgfqwp dtlkcekfpv hgagelcvgq ntsdkgtptp
      241 sllpefwtsn pqhgggghrg gfpggagase rgkfscpral kvpsylnyhf lgekdcgapc
      301 eptkvyglmy fgpeelrfsr twigiwsvlc castlftvlt ylvdmrrfsy perpiiflsg
      361 cytavavayi agflledrvv cndkfaedga rtvaqgtkke gctilfmmly ffsmassiww
      421 vilsltwfla agmkwgheai eansqyfhla awavpaikti tilalgqvdg dvlsgvcfvg
      481 lnnvdalrgf vlaplfvylf igtsfllagf vslfrirtim khdgtktekl eklmvrigvf
      541 svlytvpati viacyfyeqa frdqwerswv aqscksyaip cphlqaggga pphppmspdf
      601 tvfmikylmt livgitsgfw iwsgktlnsw rkfytrltns kqgettv
//
LOCUS       NP_003602               1012 aa            linear   PRI 20-NOV-2025
DEFINITION  centriole and centriolar satellite protein OFD1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_003602
VERSION     NP_003602.1
DBSOURCE    REFSEQ: accession NM_003611.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Kim,N.H., Lee,C.H. and Lee,A.Y.
  TITLE     Extraciliary OFD1 Is Involved in Melanocyte Survival through Cell
            Adhesion to ECM via Paxillin
  JOURNAL   Int J Mol Sci 24 (24), 17528 (2023)
   PUBMED   38139355
  REMARK    GeneRIF: Extraciliary OFD1 Is Involved in Melanocyte Survival
            through Cell Adhesion to ECM via Paxillin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Alitalo,T., Francis,F., Kere,J., Lehrach,H., Schlessinger,D. and
            Willard,H.F.
  TITLE     A 6-Mb YAC contig in Xp22.1-p22.2 spanning the DXS69E, XE59, GLRA2,
            PIGA, GRPR, CALB3, and PHKA2 genes
  JOURNAL   Genomics 25 (3), 691-700 (1995)
   PUBMED   7759104
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   8  (residues 1 to 1012)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
REFERENCE   9  (residues 1 to 1012)
  AUTHORS   Franco,B., Bruel,A.L. and Thauvin-Robinet,C.
  TITLE     Oral-Facial-Digital Syndrome Type I
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301367
REFERENCE   10 (residues 1 to 1012)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC003037.1, Y15164.1 and
            CB134304.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is located on the X chromosome and encodes a
            centrosomal protein. A knockout mouse model has been used to study
            the effect of mutations in this gene. The mouse gene is also
            located on the X chromosome, however, unlike the human gene it is
            not subject to X inactivation. Mutations in this gene are
            associated with oral-facial-digital syndrome type I and
            Simpson-Golabi-Behmel syndrome type 2. Many pseudogenes have been
            identified; a single pseudogene is found on chromosome 5 while as
            many as fifteen have been found on the Y chromosome. [provided by
            RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.272710.1, Y15164.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000340096.11/ ENSP00000344314.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..1012
                     /product="centriole and centriolar satellite protein OFD1
                     isoform 1"
                     /note="oral-facial-digital syndrome 1 protein; protein
                     71-7A; Joubert syndrome type 10; centriole and centriolar
                     satellite protein OFD1"
                     /calculated_mol_wt=116541
     Region          75..101
                     /region_name="LisH_2"
                     /note="pfam16045"
                     /db_xref="CDD:464992"
     Region          <273..>556
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          609..665
                     /region_name="Mediates homooligomerization"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     Region          615..1012
                     /region_name="Mediates the interaction with SDCCAG8.
                     /evidence=ECO:0000269|PubMed:20835237"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     Site            663
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Region          719..744
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:33934390; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            745
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Region          757..794
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     Site            774
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75665.1)"
     Region          824..904
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     Region          963..1012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75665.1)"
     CDS             1..1012
                     /gene="OFD1"
                     /gene_synonym="71-7A; CXorf5; JBTS10; RP23; SGBS2"
                     /coded_by="NM_003611.3:325..3363"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14157.1"
                     /db_xref="GeneID:8481"
                     /db_xref="HGNC:HGNC:2567"
                     /db_xref="MIM:300170"
ORIGIN      
        1 mmaqsnmftv advlsqdelr kklyqtfkdr gildtlktql rnqlihelmh pvlsgelqpr
       61 sisvegssll igasnslvad hlqrcgyeys lsvffpesgl akekvftmqd llqlikinpt
      121 sslykslvsg sdkenqkgfl mhflkelaey hqakescnme tqtsstfnrd slaeklqlid
      181 dqfadaypqr ikfesleikl neykreieeq lraemcqklk ffkdteiaki kmeakkkyek
      241 eltmfqndfe kacqakseal vlrekstler ihkhqeietk eiyaqrqlll kdmdllrgre
      301 aelkqrveaf elnqklqeek hksitealrr qeqniksfee tydrklknel lkyqlelkdd
      361 yiirtnrlie derknkekav hlqeeliain skkeelnqsv nrvkelelel esvkaqslai
      421 tkqnhmlnek vkemsdysll keeklellaq nkllkqqlee srnenlrlln rlaqpapela
      481 vfqkelrkae kaivveheef escrqalhkq lqdeiehsaq lkaqilgyka svkslttqva
      541 dlklqlkqtq talenevycn pkqsvidrsv nglingnvvp cngeisgdfl nnpfkqenvl
      601 armvasritn yptawvegss pdsdlefvan tkarvkelqq eaerlekafr syhrrvikns
      661 aksplaaksp pslhlleafk nitsssperh ifgedrvvse qpqvgtleer ndvvealtgs
      721 aasrlrggts srrlsstplp kakrslesem yleglgrshi aspspcpdrm plpsptesrh
      781 slsippvssp peqkvglyrr qtelqdksef sdvdklafkd neefessfes agnmprqlem
      841 gglspagdms hvdaaaaavp lsyqhpsvdq kqieeqkeee kireqqvker rqreerrqsn
      901 lqevlererr eleklyqerk mieeslkiki kkelemenel emsnqeikdk sahsenplek
      961 ymkiiqqeqd qesadksskk mvqegslvdt lqssdkvesl tgfsheeldd sw
//
LOCUS       NP_037404                710 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 3A1 isoform
            1 [Homo sapiens].
ACCESSION   NP_037404 XP_946154 XP_950051 XP_950052
VERSION     NP_037404.2
DBSOURCE    REFSEQ: accession NM_013272.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Surrer,D.B., Schusser,S., Konig,J., Fromm,M.F. and Gessner,A.
  TITLE     Transport of aromatic amino acids l-tryptophan, l-tyrosine, and
            l-phenylalanine by the organic anion transporting polypeptide
            (OATP) 3A1
  JOURNAL   FEBS J 291 (21), 4732-4743 (2024)
   PUBMED   39206635
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Bakos,E., Nemet,O., Kucsma,N., Tokesi,N., Stieger,B., Rushing,E.,
            Tokes,A.M., Kele,P., Tusnady,G.E. and Ozvegy-Laczka,C.
  TITLE     Cloning and characterization of a novel functional organic anion
            transporting polypeptide 3A1 isoform highly expressed in the human
            brain and testis
  JOURNAL   Front Pharmacol 13, 958023 (2022)
   PUBMED   36120371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Li,M., Wang,W., Cheng,Y., Zhang,X., Zhao,N., Tan,Y., Xie,Q.,
            Chai,J. and Pan,Q.
  TITLE     Tumor necrosis factor alpha upregulates the bile acid efflux
            transporter OATP3A1 via multiple signaling pathways in cholestasis
  JOURNAL   J Biol Chem 298 (2), 101543 (2022)
   PUBMED   34971708
  REMARK    GeneRIF: Tumor necrosis factor alpha upregulates the bile acid
            efflux transporter OATP3A1 via multiple signaling pathways in
            cholestasis.
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Hagenbuch,B. and Meier,P.J.
  TITLE     Organic anion transporting polypeptides of the OATP/ SLC21 family:
            phylogenetic classification as OATP/ SLCO superfamily, new
            nomenclature and molecular/functional properties
  JOURNAL   Pflugers Arch 447 (5), 653-665 (2004)
   PUBMED   14579113
  REMARK    Review article
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Adachi,H., Suzuki,T., Abe,M., Asano,N., Mizutamari,H., Tanemoto,M.,
            Nishio,T., Onogawa,T., Toyohara,T., Kasai,S., Satoh,F., Suzuki,M.,
            Tokui,T., Unno,M., Shimosegawa,T., Matsuno,S., Ito,S. and Abe,T.
  TITLE     Molecular characterization of human and rat organic anion
            transporter OATP-D
  JOURNAL   Am J Physiol Renal Physiol 285 (6), F1188-F1197 (2003)
   PUBMED   14631946
  REMARK    GeneRIF: OATP-D plays an important role in translocating
            prostaglandins in specialized tissues and cells.
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Schiffer,R., Neis,M., Holler,D., Rodriguez,F., Geier,A.,
            Gartung,C., Lammert,F., Dreuw,A., Zwadlo-Klarwasser,G., Merk,H.,
            Jugert,F. and Baron,J.M.
  TITLE     Active influx transport is mediated by members of the organic anion
            transporting polypeptide family in human epidermal keratinocytes
  JOURNAL   J Invest Dermatol 120 (2), 285-291 (2003)
   PUBMED   12542534
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Patel,P., Weerasekera,N., Hitchins,M., Boyd,C.A., Johnston,D.G. and
            Williamson,C.
  TITLE     Semi quantitative expression analysis of MDR3, FIC1, BSEP, OATP-A,
            OATP-C,OATP-D, OATP-E and NTCP gene transcripts in 1st and 3rd
            trimester human placenta
  JOURNAL   Placenta 24 (1), 39-44 (2003)
   PUBMED   12495658
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Tamai,I., Nezu,J., Uchino,H., Sai,Y., Oku,A., Shimane,M. and
            Tsuji,A.
  TITLE     Molecular identification and characterization of novel members of
            the human organic anion transporter (OATP) family
  JOURNAL   Biochem Biophys Res Commun 273 (1), 251-260 (2000)
   PUBMED   10873595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104020.10, AF205074.1, AC113190.8 and AC116903.3.
            
            On Feb 6, 2009 this sequence version replaced NP_037404.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF205074.1, AB031050.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318445.11/ ENSP00000320634.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..710
                     /product="solute carrier organic anion transporter family
                     member 3A1 isoform 1"
                     /note="solute carrier family 21 (organic anion
                     transporter), member 11; PGE1 transporter; solute carrier
                     family 21 member 11; organic anion-transporting
                     polypeptide D; sodium-independent organic anion
                     transporter D; organic anion transporter
                     polypeptide-related protein 3"
                     /calculated_mol_wt=76422
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:25732826; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Region          39..563
                     /region_name="MFS_SLCO3_OATP3"
                     /note="Solute carrier organic anion transporter 3 family
                     of the Major Facilitator Superfamily of transporters;
                     cd17402"
                     /db_xref="CDD:340960"
     Site            41..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            order(53..54,57..58,61,93,191..192,194..196,199,219,
                     222..223,226,358,361..362,365..367,370,399,403,444..445,
                     449,453,506,509..510,513..514,517)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340960"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            107..131
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            169
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            175..203
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            262..286
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            345..366
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            387..410
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            415..438
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            457
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            502
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            505
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            519
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            540..562
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            572..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     Site            631..648
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UIG8.3)"
     CDS             1..710
                     /gene="SLCO3A1"
                     /gene_synonym="OATP-D; OATP-RP3; OATP3A1; OATPD; OATPRP3;
                     SLC21A11"
                     /coded_by="NM_013272.4:202..2334"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10371.1"
                     /db_xref="GeneID:28232"
                     /db_xref="HGNC:HGNC:10952"
                     /db_xref="MIM:612435"
ORIGIN      
        1 mqgkkpggss gggrsgelqg deaqrnkkkk kkvscfsnik iflvsecalm laqgtvgayl
       61 vsvlttlerr fnlqsadvgv iassfeignl alilfvsyfg arghrprlig cggivmalga
      121 llsalpeflt hqykyeagei rwgaegrdvc aangsggdeg pdpdlicrnr tatnmmylll
      181 igaqvllgig atpvqplgvs yiddhvrrkd sslyigilft mlvfgpacgf ilgsfctkiy
      241 vdavfidtsn lditpddprw igawwggfll cgallffssl lmfgfpqslp phsepamese
      301 qamlsereye rpkpsngvlr hplepdssas cfqqlrvipk vtkhllsnpv ftciilaacm
      361 eiavvagfaa flgkyleqqf nlttssanql lgmtaipcac lgiflggllv kklslsalga
      421 irmamlvnlv stacyvsflf lgcdtgpvag vtvpygnsta pgsaldpysp cnnncecqtd
      481 sftpvcgadg itylsacfag cnstnltgca clttvpaena tvvpgkcpsp gcqeafltfl
      541 cvmcicslig amaqtpsvii lirtvspelk syalgvlfll lrllgfippp lifgagidst
      601 clfwstfcge qgacvlydnv vyrylyvsia ialksfafil ytttwqclrk nykryiknhe
      661 gglstseffa stltldnlgr dpvpanqthr tkfiynledh ewcenmesvl
//
LOCUS       NP_001310339             263 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome inhibitor PI31 subunit isoform 6 [Homo sapiens].
ACCESSION   NP_001310339
VERSION     NP_001310339.1
DBSOURCE    REFSEQ: accession NM_001323410.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Yang,S., Tang,D., Zhao,Y.C., Liu,H., Luo,S., Stinchcombe,T.E.,
            Glass,C., Su,L., Shen,S., Christiani,D.C., Wang,Q. and Wei,Q.
  TITLE     Potentially functional variants of ERAP1, PSMF1 and NCF2 in the
            MHC-I-related pathway predict non-small cell lung cancer survival
  JOURNAL   Cancer Immunol Immunother 70 (10), 2819-2833 (2021)
   PUBMED   33651148
  REMARK    GeneRIF: Potentially functional variants of ERAP1, PSMF1 and NCF2
            in the MHC-I-related pathway predict non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 263)
  AUTHORS   McCutchen-Maloney,S.L., Matsuda,K., Shimbara,N., Binns,D.D.,
            Tanaka,K., Slaughter,C.A. and DeMartino,G.N.
  TITLE     cDNA cloning, expression, and functional characterization of PI31,
            a proline-rich inhibitor of the proteasome
  JOURNAL   J Biol Chem 275 (24), 18557-18565 (2000)
   PUBMED   10764772
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Tanahashi,N., Kawahara,H., Murakami,Y. and Tanaka,K.
  TITLE     The proteasome-dependent proteolytic system
  JOURNAL   Mol Biol Rep 26 (1-2), 3-9 (1999)
   PUBMED   10363639
  REMARK    Review article
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC398668.1, AL031665.19 and
            AA699495.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            protein that inhibits the activation of the proteasome by the 11S
            and 19S regulators. Alternative transcript variants have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.128928.1,
                                           SRR1803615.258009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..263
                     /product="proteasome inhibitor PI31 subunit isoform 6"
                     /note="proteasome inhibitor PI31 subunit; proteasome
                     (prosome, macropain) inhibitor subunit 1 (PI31)"
                     /calculated_mol_wt=28751
     Region          2..150
                     /region_name="Important for homodimerization and
                     interaction with FBXO7.
                     /evidence=ECO:0000269|PubMed:18495667"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          11..148
                     /region_name="PI31_Prot_N"
                     /note="PI31 proteasome regulator N-terminal; pfam11566"
                     /db_xref="CDD:463296"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Region          182..248
                     /region_name="PI31_Prot_C"
                     /note="PI31 proteasome regulator; pfam08577"
                     /db_xref="CDD:430086"
     Site            205
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            219
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHL8; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            231
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92530.2)"
     CDS             1..263
                     /gene="PSMF1"
                     /gene_synonym="PI31"
                     /coded_by="NM_001323410.2:173..964"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9491"
                     /db_xref="HGNC:HGNC:9571"
                     /db_xref="MIM:617858"
ORIGIN      
        1 maglevlfas aapaitcrqd alvcflhwev vthgyfglgv gdqpgpndkk sellpagwnn
       61 nkdlyvlrye ykdgsrkllv kaitvessmi lnvleygsqq vadltlnldd yidaehlgdf
      121 hrtyknseel rsrivsgiit piheqwekan vssphrefpp atarevdplr ipphhphtsr
      181 qppwcdplgp fvvggedldp fgprrggmiv dplrsgfpra lidpssglpn rlppgavppg
      241 arfdpfgpig tsppgyvvtq pea
//
LOCUS       NP_001138408             678 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger translocation-associated protein [Homo sapiens].
ACCESSION   NP_001138408 XP_001715442 XP_938632 XP_949622
VERSION     NP_001138408.1
DBSOURCE    REFSEQ: accession NM_001144936.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Dorwal,P., White,C., Goh,A.F., Kumar,A., McEniery,J., Walker,R. and
            Robertson,T.
  TITLE     Ependymoma-like tumor with mesenchymal differentiation (ELTMD) with
            ZFTA:NCOA1 fusion: A diagnostic challenge
  JOURNAL   Neuropathology 44 (3), 216-221 (2024)
   PUBMED   37931917
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Tauziede-Espariat,A., Nicaise,Y., Sievers,P., Sahm,F., von
            Deimling,A., Guillemot,D., Pierron,G., Duchesne,M., Edjlali,M.,
            Dangouloff-Ros,V., Boddaert,N., Roux,A., Dezamis,E., Hasty,L.,
            Lhermitte,B., Hirsch,E., Hirsch,M.P.V., Ardellier,F.D.,
            Karnoub,M.A., Csanyi,M., Maurage,C.A., Mokhtari,K., Bielle,F.,
            Rigau,V., Roujeau,T., Abad,M., Klein,S., Bernier,M., Horodyckid,C.,
            Adam,C., Brandal,P., Niehusmann,P., Vannod-Michel,Q., Provost,C.,
            de Champfleur,N.M., Nichelli,L., Metais,A., Mariet,C., Chretien,F.,
            Blauwblomme,T., Beccaria,K., Pallud,J., Puget,S., Uro-Coste,E. and
            Varlet,P.
  CONSRTM   RENOCLIP-LOC
  TITLE     CNS tumors with PLAGL1-fusion: beyond ZFTA and YAP1 in the genetic
            spectrum of supratentorial ependymomas
  JOURNAL   Acta Neuropathol Commun 12 (1), 55 (2024)
   PUBMED   38581034
  REMARK    GeneRIF: CNS tumors with PLAGL1-fusion: beyond ZFTA and YAP1 in the
            genetic spectrum of supratentorial ependymomas.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Herranz-Perez,V., Nakatani,J., Ishii,M., Katada,T.,
            Garcia-Verdugo,J.M. and Ohata,S.
  TITLE     Ependymoma associated protein Zfta is expressed in immature
            ependymal cells but is not essential for ependymal development in
            mice
  JOURNAL   Sci Rep 12 (1), 1493 (2022)
   PUBMED   35087169
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Tomomasa,R., Arai,Y., Kawabata-Iwakawa,R., Fukuoka,K., Nakano,Y.,
            Hama,N., Nakata,S., Suzuki,N., Ishi,Y., Tanaka,S., Takahashi,J.A.,
            Yuba,Y., Shiota,M., Natsume,A., Kurimoto,M., Shiba,Y., Aoki,M.,
            Nabeshima,K., Enomoto,T., Inoue,T., Fujimura,J., Kondo,A., Yao,T.,
            Okura,N., Hirose,T., Sasaki,A., Nishiyama,M., Ichimura,K.,
            Shibata,T., Hirato,J., Yokoo,H. and Nobusawa,S.
  TITLE     Ependymoma-like tumor with mesenchymal differentiation harboring
            C11orf95-NCOA1/2 or -RELA fusion: A hitherto unclassified tumor
            related to ependymoma
  JOURNAL   Brain Pathol 31 (3), e12943 (2021)
   PUBMED   33576087
  REMARK    GeneRIF: Ependymoma-like tumor with mesenchymal differentiation
            harboring C11orf95-NCOA1/2 or -RELA fusion: A hitherto unclassified
            tumor related to ependymoma.
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Ozawa,T., Kaneko,S., Szulzewsky,F., Qiao,Z., Takadera,M.,
            Narita,Y., Kondo,T., Holland,E.C., Hamamoto,R. and Ichimura,K.
  TITLE     C11orf95-RELA fusion drives aberrant gene expression through the
            unique epigenetic regulation for ependymoma formation
  JOURNAL   Acta Neuropathol Commun 9 (1), 36 (2021)
   PUBMED   33685520
  REMARK    GeneRIF: C11orf95-RELA fusion drives aberrant gene expression
            through the unique epigenetic regulation for ependymoma formation.
            Erratum:[Acta Neuropathol Commun. 2021 May 27;9(1):100. doi:
            10.1186/s40478-021-01157-y. PMID: 34044883]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Pietsch,T., Wohlers,I., Goschzik,T., Dreschmann,V., Denkhaus,D.,
            Dorner,E., Rahmann,S. and Klein-Hitpass,L.
  TITLE     Supratentorial ependymomas of childhood carry C11orf95-RELA fusions
            leading to pathological activation of the NF-kappaB signaling
            pathway
  JOURNAL   Acta Neuropathol 127 (4), 609-611 (2014)
   PUBMED   24562983
  REMARK    GeneRIF: C11orf95-RELA fusions represent a unique novel mechanism
            leading to pathological activation of NF-kappaB signaling in
            supratentorial ependymomas.
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Parker,M., Mohankumar,K.M., Punchihewa,C., Weinlich,R.,
            Dalton,J.D., Li,Y., Lee,R., Tatevossian,R.G., Phoenix,T.N.,
            Thiruvenkatam,R., White,E., Tang,B., Orisme,W., Gupta,K., Rusch,M.,
            Chen,X., Li,Y., Nagahawhatte,P., Hedlund,E., Finkelstein,D., Wu,G.,
            Shurtleff,S., Easton,J., Boggs,K., Yergeau,D., Vadodaria,B.,
            Mulder,H.L., Becksfort,J., Gupta,P., Huether,R., Ma,J., Song,G.,
            Gajjar,A., Merchant,T., Boop,F., Smith,A.A., Ding,L., Lu,C.,
            Ochoa,K., Zhao,D., Fulton,R.S., Fulton,L.L., Mardis,E.R.,
            Wilson,R.K., Downing,J.R., Green,D.R., Zhang,J., Ellison,D.W. and
            Gilbertson,R.J.
  TITLE     C11orf95-RELA fusions drive oncogenic NF-kappaB signalling in
            ependymoma
  JOURNAL   Nature 506 (7489), 451-455 (2014)
   PUBMED   24553141
  REMARK    Erratum:[Nature. 2014 Apr 24;508(7497):554. Becksford, Jared
            [corrected to Becksfort, Jared]]
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Flucke,U., Tops,B.B., de Saint Aubain Somerhausen,N., Bras,J.,
            Creytens,D.H., Kusters,B., Groenen,P.J., Verdijk,M.A.,
            Suurmeijer,A.J. and Mentzel,T.
  TITLE     Presence of C11orf95-MKL2 fusion is a consistent finding in
            chondroid lipomas: a study of eight cases
  JOURNAL   Histopathology 62 (6), 925-930 (2013)
   PUBMED   23672313
  REMARK    GeneRIF: Based on a recurrent translocation t(11;16)(q13;p13), the
            C11orf95-MKL2 fusion gene has been found in eight further cases of
            chondroid lipomas.
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Nishio,J.
  TITLE     Contributions of cytogenetics and molecular cytogenetics to the
            diagnosis of adipocytic tumors
  JOURNAL   J Biomed Biotechnol 2011, 524067 (2011)
   PUBMED   21274402
  REMARK    Review article
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Huang,D., Sumegi,J., Dal Cin,P., Reith,J.D., Yasuda,T., Nelson,M.,
            Muirhead,D. and Bridge,J.A.
  TITLE     C11orf95-MKL2 is the resulting fusion oncogene of t(11;16)(q13;p13)
            in chondroid lipoma
  JOURNAL   Genes Chromosomes Cancer 49 (9), 810-818 (2010)
   PUBMED   20607705
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP006289.2.
            
            On or before Jan 31, 2009 this sequence version replaced
            XP_938632.2, XP_949622.2, XP_001715442.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. There are no full-length human transcripts
            supporting this exon combination; it is predicted based on partial
            transcript alignments and on homologous alignments from mouse
            GeneID:108899.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1970526 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000433688.2/ ENSP00000482180.1
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..678
                     /product="zinc finger translocation-associated protein"
                     /note="uncharacterized protein C11orf95"
                     /calculated_mol_wt=73067
     Region          1..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (C9JLR9.1)"
     Region          106..169
                     /region_name="zf-C2H2_12"
                     /note="Spin-doc zinc-finger; pfam18658"
                     /db_xref="CDD:465831"
     Site            138
                     /site_type="other"
                     /note="Breakpoint for translocation to form ZFTA-MLK2
                     fusion protein; propagated from UniProtKB/Swiss-Prot
                     (C9JLR9.1)"
     Region          182..250
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (C9JLR9.1)"
     Region          265..326
                     /region_name="zf-C2H2_12"
                     /note="Spin-doc zinc-finger; pfam18658"
                     /db_xref="CDD:465831"
     Region          329..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (C9JLR9.1)"
     Region          419..482
                     /region_name="zf-C2H2_12"
                     /note="Spin-doc zinc-finger; pfam18658"
                     /db_xref="CDD:465831"
     Region          490..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (C9JLR9.1)"
     Region          582..645
                     /region_name="zf-C2H2_12"
                     /note="Spin-doc zinc-finger; pfam18658"
                     /db_xref="CDD:465831"
     CDS             1..678
                     /gene="ZFTA"
                     /gene_synonym="C11orf95"
                     /coded_by="NM_001144936.2:154..2190"
                     /db_xref="CCDS:CCDS44636.1"
                     /db_xref="GeneID:65998"
                     /db_xref="HGNC:HGNC:28449"
                     /db_xref="MIM:615699"
ORIGIN      
        1 mepggdhrsr ssggrggpgp avasargrrl ppagssgsae peedeggqdl qleggalgsw
       61 gsaplpssra rgpassgrky sdhcearasr pgksripgrd hrryyhdhwr leylmdfnpa
      121 rhgmvcmvcg sslatlklst ikrhirqkhp yslhwsprek evisnswdah lglgacgeae
      181 glgvqgaeee eeeeeeeeee gagvpacppk gpgkapaggg crrqrrggpv aprarrlrls
      241 asrraggsrg lgarrlerrl keslqnwfra eclmdydprg nrlvcmacgr alpslhlddi
      301 rahvlevhpg slglsgpqrs allqawggqp ealseltqsp pgddlapqdl tgksrdsasa
      361 agapssqdls ppdvkeeagw vperpgpaee eeeleegege ragvpgrspr grahrrhpqe
      421 rwrleylmel dggrrglvcg vcggalaslk mstierhirr rhpgstrlgg pvqaliarew
      481 sekaahllal gpprpespqg pippgtaaas degggdeeee peeeeeewgd vplspgaple
      541 rpaeeeedee dgqepgglal pppppppppp pprsreqrrn yqprwrgeyl mdydgsrrgl
      601 vcmvcggala tlkvstikrh ilqvhpfsmd ftpeerqtil eayeeaalrc yghegfgppa
      661 paprdggadl ksgavcra
//
LOCUS       NP_001026913             622 aa            linear   PRI 20-NOV-2025
DEFINITION  cilia- and flagella-associated protein 206 [Homo sapiens].
ACCESSION   NP_001026913
VERSION     NP_001026913.1
DBSOURCE    REFSEQ: accession NM_001031743.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Shen,Q., Martinez,G., Liu,H., Beurois,J., Wu,H., Amiri-Yekta,A.,
            Liang,D., Kherraf,Z.E., Bidart,M., Cazin,C., Celse,T., Satre,V.,
            Thierry-Mieg,N., Whitfield,M., Toure,A., Song,B., Lv,M., Li,K.,
            Liu,C., Tao,F., He,X., Zhang,F., Arnoult,C., Ray,P.F., Cao,Y. and
            Coutton,C.
  TITLE     Bi-allelic truncating variants in CFAP206 cause male infertility in
            human and mouse
  JOURNAL   Hum Genet 140 (9), 1367-1377 (2021)
   PUBMED   34255152
  REMARK    GeneRIF: Bi-allelic truncating variants in CFAP206 cause male
            infertility in human and mouse.
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 622)
  AUTHORS   Gupta,A., Diener,D.R., Sivadas,P., Rosenbaum,J.L. and Yang,P.
  TITLE     The versatile molecular complex component LC8 promotes several
            distinct steps of flagellar assembly
  JOURNAL   J Cell Biol 198 (1), 115-126 (2012)
   PUBMED   22753897
REFERENCE   7  (residues 1 to 622)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 622)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL049697.9.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.389050.1,
                                           SRR1803617.108958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369562.9/ ENSP00000358575.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..622
                     /product="cilia- and flagella-associated protein 206"
                     /note="UPF0704 protein C6orf165"
                     /calculated_mol_wt=71062
     Region          214..491
                     /region_name="FAP206"
                     /note="Domain of unknown function; pfam12018"
                     /db_xref="CDD:463432"
     Region          570..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYR0.2)"
     CDS             1..622
                     /gene="CFAP206"
                     /gene_synonym="C6orf165; dJ382I10.1; SPGF102"
                     /coded_by="NM_001031743.3:124..1992"
                     /db_xref="CCDS:CCDS34498.1"
                     /db_xref="GeneID:154313"
                     /db_xref="HGNC:HGNC:21405"
                     /db_xref="MIM:621376"
ORIGIN      
        1 mpptqaesvi rsiireigqe caahgeivse tliafmvkav vldpsngfnm drtlmksdvq
       61 nlvklcmtrl ldtknpsldt ikmqvyfdmn ytnrveflee hhrvlesrlg svtreitdnr
      121 acakeelesl yrkiisyvll rsglgsptdi ktvrevtaal qsvfpqaelg tfltlskkdk
      181 erqlkeltmi vtgirlfnrd cgkggegidd lpavlhvaip atmqhidyql etarsqvyry
      241 tailekaand plmraelqpy mlkealynir qyevflqiil sdiitgaqev emmtkqlgah
      301 leqlkmtiks kiavptsqvf pifialstlw tslqdetivv gvlsnlfthi qpflgahely
      361 fpervmqchl ngatvktdvc rmkehmedrv nvadfrklew lfpettanfd klliqyrgfc
      421 aytfaatdgl llpgnpaigi lkykekyytf nskdaaysfa enpehyidiv rekakkntel
      481 iqllelhqqf etfipysqmr dadkhyikpi tkcesstqtn thilpptivr syewnewelr
      541 rkaiklanlr qkvthsvqtd lshlrrencs qvyppkdtst qsmredstgv prpqiylagl
      601 rggkseitde vkvnltrdvd et
//
LOCUS       NP_055506               1485 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA helicase aquarius [Homo sapiens].
ACCESSION   NP_055506 XP_029045
VERSION     NP_055506.1
DBSOURCE    REFSEQ: accession NM_014691.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1485)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1485)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1485)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 1485)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1485)
  AUTHORS   Zhang,X., Zhan,X., Yan,C., Zhang,W., Liu,D., Lei,J. and Shi,Y.
  TITLE     Structures of the human spliceosomes before and after release of
            the ligated exon
  JOURNAL   Cell Res 29 (4), 274-285 (2019)
   PUBMED   30728453
REFERENCE   6  (residues 1 to 1485)
  AUTHORS   Silva,L.K., Blanton,R.E., Parrado,A.R., Melo,P.S., Morato,V.G.,
            Reis,E.A., Dias,J.P., Castro,J.M., Vasconcelos,P.F., Goddard,K.A.,
            Barreto,M.L., Reis,M.G. and Teixeira,M.G.
  TITLE     Dengue hemorrhagic fever is associated with polymorphisms in JAK1
  JOURNAL   Eur J Hum Genet 18 (11), 1221-1227 (2010)
   PUBMED   20588308
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1485)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 1485)
  AUTHORS   Hirose,T., Ideue,T., Nagai,M., Hagiwara,M., Shu,M.D. and
            Steitz,J.A.
  TITLE     A spliceosomal intron binding protein, IBP160, links
            position-dependent assembly of intron-encoded box C/D snoRNP to
            pre-mRNA splicing
  JOURNAL   Mol Cell 23 (5), 673-684 (2006)
   PUBMED   16949364
REFERENCE   9  (residues 1 to 1485)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 1485)
  AUTHORS   Sam,M., Wurst,W., Kluppel,M., Jin,O., Heng,H. and Bernstein,A.
  TITLE     Aquarius, a novel gene isolated by gene trapping with an
            RNA-dependent RNA polymerase motif
  JOURNAL   Dev Dyn 212 (2), 304-317 (1998)
   PUBMED   9626505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018868.4.
            
            On Dec 18, 2003 this sequence version replaced XP_029045.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.51066.1,
                                           SRR1660807.30390.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000156471.10/ ENSP00000156471.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..1485
                     /product="RNA helicase aquarius"
                     /EC_number="3.6.4.13"
                     /note="functional spliceosome-associated protein 164;
                     intron-binding protein aquarius; intron-binding protein of
                     160 kDa; aquarius homolog"
                     /calculated_mol_wt=171165
     Region          1..416
                     /region_name="Helical region with structural similarity to
                     ARM repeat domains. /evidence=ECO:0000269|PubMed:25599396"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     Region          18..802
                     /region_name="Aquarius_N"
                     /note="Intron-binding protein aquarius N-terminus;
                     pfam16399"
                     /db_xref="CDD:435319"
     Region          417..1485
                     /region_name="Required for assembly of the IB complex.
                     /evidence=ECO:0000269|PubMed:25599396"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     Region          797..1152
                     /region_name="EEXXQc_AQR"
                     /note="EEXXQ-box helicase domain of AQR; cd17935"
                     /db_xref="CDD:350693"
     Site            order(800..803,806,825..831,861,1137..1138)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350693"
     Site            1051
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60306.4)"
     Region          1140..1323
                     /region_name="SF1_C_Upf1"
                     /note="C-terminal helicase domain of Upf1-like family
                     helicases; cd18808"
                     /db_xref="CDD:350195"
     Site            order(1229..1231,1259,1261..1262,1277)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350195"
     Site            order(1265,1267,1296)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350195"
     Region          1419..1485
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60306.4)"
     CDS             1..1485
                     /gene="AQR"
                     /gene_synonym="fSAP164; IBP160"
                     /coded_by="NM_014691.3:130..4587"
                     /db_xref="CCDS:CCDS42013.1"
                     /db_xref="GeneID:9716"
                     /db_xref="HGNC:HGNC:29513"
                     /db_xref="MIM:610548"
ORIGIN      
        1 maapaqpkki vaptvsqina efvtqlacky waphikkksp fdikviediy ekeivksrfa
       61 irkimllefs qylenylwmn yspevsskay lmsiccmvne kfrenvpawe ifkkkpdhfp
      121 fffkhilkaa laetdgefsl heqtvlllfl dhcfnslevd lirsqvqqli slpmwmglql
      181 arlelelkkt pklrkfwnli kkndekmdpe areqayqerr flsqliqkfi svlksvplse
      241 pvtmdkvhyc erfielmidl eallptrrwf ntilddshll vhcylsnlvr reedghlfsq
      301 lldmlkfytg feindqtgna ltenemttih ydritslqra afahfpelyd falsnvaevd
      361 treslvkffg plssntlhqv asylcllptl pknedttfdk efllellvsr herrisqiqq
      421 lnqmplypte kiiwdenivp teyysgegcl alpklnlqfl tlhdyllrnf nlfrlestye
      481 irqdiedsvs rmkpwqseyg gvvfggwarm aqpivaftvv evakpnigen wptrvradvt
      541 inlnvrdhik deweglrkhd vcflitvrpt kpygtkfdrr rpfieqvglv yvrgceiqgm
      601 lddkgrvied gpeprpnlrg esrtfrvfld pnqyqqdmtn tiqngaedvy etfniimrrk
      661 pkennfkavl etirnlmntd cvvpdwlhdi ilgygdpssa hyskmpnqia tldfndtfls
      721 iehlkasfpg hnvkvtvedp alqippfrit fpvrsgkgkk rkdadveded teeaktlive
      781 phvipnrgpy pynqpkrnti qfthtqieai ragmqpgltm vvgppgtgkt dvavqiisni
      841 yhnfpeqrtl ivthsnqaln qlfekimald iderhllrlg hgeeeletek dfsrygrvny
      901 vlarrielle evkrlqkslg vpgdasytce tagyfflyqv msrweeyisk vknkgstlpd
      961 vtevstffpf heyfanapqp ifkgrsyeed meiaegcfrh ikkiftqlee frasellrsg
     1021 ldrskyllvk eakiiamtct haalkrhdlv klgfkydnil meeaaqilei etfiplllqn
     1081 pqdgfsrlkr wimigdhhql ppviknmafq kysnmeqslf trfvrvgvpt vdldaqgrar
     1141 aslcnlynwr yknlgnlphv qllpefstan agllydfqli nvedfqgvge sepnpyfyqn
     1201 lgeaeyvval fmymcllgyp adkisiltty ngqkhlirdi inrrcgnnpl igrpnkvttv
     1261 drfqgqqndy illslvrtra vghlrdvrrl vvamsrarlg lyifarvslf qncfeltpaf
     1321 sqltarplhl hiiptepfpt trkngerpsh evqiiknmpq manfvynmym hliqtthhyh
     1381 qtllqlppam veegeevqnq eteleteeea mtvqadiips ptdtscrqet pafqtdttps
     1441 etgatstpea ipalsettpt vvgavsapae antpqdatsa peetk
//
LOCUS       NP_001034673             415 aa            linear   PRI 20-NOV-2025
DEFINITION  PRKCA-binding protein [Homo sapiens].
ACCESSION   NP_001034673
VERSION     NP_001034673.1
DBSOURCE    REFSEQ: accession NM_001039584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Fadahunsi,N., Petersen,J., Metz,S., Jakobsen,A., Vad Mathiesen,C.,
            Silke Buch-Rasmussen,A., Kurgan,N., Kjaergaard Larsen,J.,
            Andersen,R.C., Topilko,T., Svendsen,C., Apuschkin,M., Skovbjerg,G.,
            Hendrik Schmidt,J., Houser,G., Elgaard Jager,S., Bach,A.,
            Deshmukh,A.S., Kilpelainen,T.O., Stromgaard,K., Madsen,K.L. and
            Clemmensen,C.
  TITLE     Targeting postsynaptic glutamate receptor scaffolding proteins
            PSD-95 and PICK1 for obesity treatment
  JOURNAL   Sci Adv 10 (9), eadg2636 (2024)
   PUBMED   38427737
  REMARK    GeneRIF: Targeting postsynaptic glutamate receptor scaffolding
            proteins PSD-95 and PICK1 for obesity treatment.
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Jin,J., Li,K., Du,Y., Gao,F., Wang,Z. and Li,W.
  TITLE     Multi-omics study identifies that PICK1 deficiency causes male
            infertility by inhibiting vesicle trafficking in Sertoli cells
  JOURNAL   Reprod Biol Endocrinol 21 (1), 114 (2023)
   PUBMED   38001535
  REMARK    GeneRIF: Multi-omics study identifies that PICK1 deficiency causes
            male infertility by inhibiting vesicle trafficking in Sertoli
            cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Sorensen,A.T., Rombach,J., Gether,U. and Madsen,K.L.
  TITLE     The Scaffold Protein PICK1 as a Target in Chronic Pain
  JOURNAL   Cells 11 (8), 1255 (2022)
   PUBMED   35455935
  REMARK    GeneRIF: The Scaffold Protein PICK1 as a Target in Chronic Pain.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Takeya,R., Takeshige,K. and Sumimoto,H.
  TITLE     Interaction of the PDZ domain of human PICK1 with class I
            ADP-ribosylation factors
  JOURNAL   Biochem Biophys Res Commun 267 (1), 149-155 (2000)
   PUBMED   10623590
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Dev,K.K., Nishimune,A., Henley,J.M. and Nakanishi,S.
  TITLE     The protein kinase C alpha binding protein PICK1 interacts with
            short but not long form alternative splice variants of AMPA
            receptor subunits
  JOURNAL   Neuropharmacology 38 (5), 635-644 (1999)
   PUBMED   10340301
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Torres,R., Firestein,B.L., Dong,H., Staudinger,J., Olson,E.N.,
            Huganir,R.L., Bredt,D.S., Gale,N.W. and Yancopoulos,G.D.
  TITLE     PDZ proteins bind, cluster, and synaptically colocalize with Eph
            receptors and their ephrin ligands
  JOURNAL   Neuron 21 (6), 1453-1463 (1998)
   PUBMED   9883737
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Staudinger,J., Lu,J. and Olson,E.N.
  TITLE     Specific interaction of the PDZ domain protein PICK1 with the COOH
            terminus of protein kinase C-alpha
  JOURNAL   J Biol Chem 272 (51), 32019-32024 (1997)
   PUBMED   9405395
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Staudinger,J., Zhou,J., Burgess,R., Elledge,S.J. and Olson,E.N.
  TITLE     PICK1: a perinuclear binding protein and substrate for protein
            kinase C isolated by the yeast two-hybrid system
  JOURNAL   J Cell Biol 128 (3), 263-271 (1995)
   PUBMED   7844141
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK092818.1 and BC017561.2.
            
            Summary: The protein encoded by this gene contains a PDZ domain,
            through which it interacts with protein kinase C, alpha (PRKCA).
            This protein may function as an adaptor that binds to and organizes
            the subcellular localization of a variety of membrane proteins. It
            has been shown to interact with multiple glutamate receptor
            subtypes, monoamine plasma membrane transporters, as well as
            non-voltage gated sodium channels, and may target PRKCA to these
            membrane proteins and thus regulate their distribution and
            function. This protein has also been found to act as an anchoring
            protein that specifically targets PRKCA to mitochondria in a
            ligand-specific manner. Three transcript variants encoding the same
            protein have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.919539.1,
                                           SRR1803614.196902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..415
                     /product="PRKCA-binding protein"
                     /note="protein interacting with C kinase 1; protein kinase
                     C-alpha-binding protein"
                     /calculated_mol_wt=46469
     Region          21..104
                     /region_name="PDZ_PICK1-like"
                     /note="PDZ domain of PICK1 (protein interacting with
                     C-kinase 1) and similar domains; cd06722"
                     /db_xref="CDD:467205"
     Site            order(32..38,50,53,83,87,90..91)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467205"
     Site            order(44..46,79,81,83)
                     /site_type="lipid-binding"
                     /note="lipid binding site [chemical binding]"
                     /db_xref="CDD:467205"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:20403402; propagated from
                     UniProtKB/Swiss-Prot (Q9NRD5.2)"
     Region          146..360
                     /region_name="BAR_PICK1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Protein
                     Interacting with C Kinase 1; cd07659"
                     /db_xref="CDD:153343"
     Site            order(162..163,169,173,176,179..180,183,186..187,191,
                     193..194,197,200..201,206..207,209..210,213,217,326,
                     330..331,334..335,337..338,345..346,348..349)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153343"
     Site            order(168,171,174..175,178..179,181..183,185..186,222,225,
                     229,232..233)
                     /site_type="active"
                     /note="putative Rac binding site [active]"
                     /db_xref="CDD:153343"
     Region          376..415
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRD5.2)"
     CDS             1..415
                     /gene="PICK1"
                     /gene_synonym="PICK; PRKCABP"
                     /coded_by="NM_001039584.1:240..1487"
                     /db_xref="CCDS:CCDS13965.1"
                     /db_xref="GeneID:9463"
                     /db_xref="HGNC:HGNC:9394"
                     /db_xref="MIM:605926"
ORIGIN      
        1 mfadldydie edklgiptvp gkvtlqkdaq nligisiggg aqycpclyiv qvfdntpaal
       61 dgtvaagdei tgvngrsikg ktkvevakmi qevkgevtih ynklqadpkq gmsldivlkk
      121 vkhrlvenms sgtadalgls railcndglv krleelerta elykgmteht knllrafyel
      181 sqthrafgdv fsvigvrepq paaseafvkf adahrsiekf girllktikp mltdlntyln
      241 kaipdtrlti kkyldvkfey lsyclkvkem ddeeyscial geplyrvstg nyeyrlilrc
      301 rqeararfsq mrkdvlekme lldqkhvqdi vfqlqrlvst mskyyndcya vlrdadvfpi
      361 evdlahttla yglnqeeftd geeeeeeedt aagepsrdtr gaagpldkgg swcds
//
LOCUS       NP_001354596             741 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform dd [Homo sapiens].
ACCESSION   NP_001354596
VERSION     NP_001354596.1
DBSOURCE    REFSEQ: accession NM_001367667.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 741)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 741)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 741)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 741)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2153307 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..741
                     /product="SUN domain-containing protein 1 isoform dd"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=81703
     Region          12..278
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <352..>576
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          404..457
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(404,407..408,411,414..415,418..419,421..422,
                     425..426,428..429,432..433,435..436,439,442..443,446,
                     449..450,453..454,456..457)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          534..592
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          635..739
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..741
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367667.1:105..2330"
                     /note="isoform dd is encoded by transcript variant 30"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld
      181 ahtaahsqsp rlpgragtlw hiwacagyfl lqilrrigav gqavsrtaws alwlavvapg
      241 kaasgvfwwl gigwyqfvtl iswlnvfllt rclrnickfl vlliplflll aglslrgqgn
      301 ffsflpvlnw asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls
      361 gqchhhgenl relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev
      421 rmshledilg klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr
      481 hvktgcetvd avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd
      541 lqlqilrnvt hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm
      601 vdfalesggg silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg
      661 sqgylvvrls mmihpaaftl ehipktlspt gnissapkdf avykrpddta fqivelrifs
      721 nwghpeytcl yrfrvhgepv k
//
LOCUS       NP_003158                285 aa            linear   PRI 20-NOV-2025
DEFINITION  sulfotransferase 2A1 [Homo sapiens].
ACCESSION   NP_003158
VERSION     NP_003158.2
DBSOURCE    REFSEQ: accession NM_003167.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Yang,J., Zhao,T., Fan,J., Zou,H., Lan,G., Guo,F., Shi,Y., Ke,H.,
            Yu,H., Yue,Z., Wang,X., Bai,Y., Li,S., Liu,Y., Wang,X., Chen,Y.,
            Li,Y. and Lei,X.
  TITLE     Structure-guided discovery of bile acid derivatives for treating
            liver diseases without causing itch
  JOURNAL   Cell 187 (25), 7164-7182 (2024)
   PUBMED   39476841
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Peng,H., Feng,K., Jia,W., Li,Y., Lv,Q. and Zhang,Y.
  TITLE     An integrated investigation of sulfotransferases (SULTs) in
            hepatocellular carcinoma and identification of the role of SULT2A1
            on stemness
  JOURNAL   Apoptosis 29 (5-6), 898-919 (2024)
   PUBMED   38411862
  REMARK    GeneRIF: An integrated investigation of sulfotransferases (SULTs)
            in hepatocellular carcinoma and identification of the role of
            SULT2A1 on stemness.
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Yoshimura,Y., Togashi,M., Ogawa,S. and Higashi,T.
  TITLE     3-Epi-25-hydroxyvitamin D3 is a poor substrate for SULT2A1:
            Analysis of its 3-sulfate in cord plasma and recombinant human
            SULT2A1 incubate
  JOURNAL   Steroids 162, 108695 (2020)
   PUBMED   32649998
  REMARK    GeneRIF: 3-Epi-25-hydroxyvitamin D3 is a poor substrate for
            SULT2A1: Analysis of its 3-sulfate in cord plasma and recombinant
            human SULT2A1 incubate.
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Mueller,J.W., Idkowiak,J., Gesteira,T.F., Vallet,C., Hardman,R.,
            van den Boom,J., Dhir,V., Knauer,S.K., Rosta,E. and Arlt,W.
  TITLE     Human DHEA sulfation requires direct interaction between PAPS
            synthase 2 and DHEA sulfotransferase SULT2A1
  JOURNAL   J Biol Chem 293 (25), 9724-9735 (2018)
   PUBMED   29743239
  REMARK    GeneRIF: Energy-dependent scoring of docking solutions identified
            the interaction as specific for the PAPSS2 and SULT2A1 isoforms
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Forbes,K.J., Hagen,M., Glatt,H., Hume,R. and Coughtrie,M.W.
  TITLE     Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning,
            stable expression in V79 cells and functional characterisation of
            the expressed enzyme
  JOURNAL   Mol Cell Endocrinol 112 (1), 53-60 (1995)
   PUBMED   7589785
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Kong,A.N., Yang,L., Ma,M., Tao,D. and Bjornsson,T.D.
  TITLE     Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of
            sulfotransferase from human liver
  JOURNAL   Biochem Biophys Res Commun 187 (1), 448-454 (1992)
   PUBMED   1520333
REFERENCE   8  (residues 1 to 285)
  AUTHORS   Otterness,D.M., Wieben,E.D., Wood,T.C., Watson,W.G., Madden,B.J.,
            McCormick,D.J. and Weinshilboum,R.M.
  TITLE     Human liver dehydroepiandrosterone sulfotransferase: molecular
            cloning and expression of cDNA
  JOURNAL   Mol Pharmacol 41 (5), 865-872 (1992)
   PUBMED   1588921
REFERENCE   9  (residues 1 to 285)
  AUTHORS   Comer,K.A. and Falany,C.N.
  TITLE     Immunological characterization of dehydroepiandrosterone
            sulfotransferase from human liver and adrenal
  JOURNAL   Mol Pharmacol 41 (4), 645-651 (1992)
   PUBMED   1569919
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Radominska,A., Comer,K.A., Zimniak,P., Falany,J., Iscan,M. and
            Falany,C.N.
  TITLE     Human liver steroid sulphotransferase sulphates bile acids
  JOURNAL   Biochem J 272 (3), 597-604 (1990)
   PUBMED   2268288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX509490.1, BC020755.1 and
            AC024582.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2003 this sequence version replaced NP_003158.1.
            
            Summary: This gene encodes a member of the sulfotransferase family.
            Sulfotransferases aid in the metabolism of drugs and endogenous
            compounds by converting these substances into more hydrophilic
            water-soluble sulfate conjugates that can be easily excreted. This
            protein catalyzes the sulfation of steroids and bile acids in the
            liver and adrenal glands, and may have a role in the inherited
            adrenal androgen excess in women with polycystic ovary syndrome.
            [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020755.1, SRR5189664.117161.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155590, SAMN03267753
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222002.4/ ENSP00000222002.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..285
                     /product="sulfotransferase 2A1"
                     /EC_number="2.8.2.2"
                     /EC_number="2.8.2.14"
                     /note="alcohol/hydroxysteroid sulfotransferase; bile-salt
                     sulfotranasferase 2A1; sulfotransferase family, cytosolic,
                     2A, dehydroepiandrosterone (DHEA)-preferring, member 1"
                     /calculated_mol_wt=33649
     Region          34..278
                     /region_name="Sulfotransfer_1"
                     /note="Sulfotransferase domain; pfam00685"
                     /db_xref="CDD:425820"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06520.3)"
     CDS             1..285
                     /gene="SULT2A1"
                     /gene_synonym="DHEA-ST; DHEA-ST8; DHEAS; HST; hSTa; ST2;
                     ST2A1; ST2A3; STD; SULT2A3"
                     /coded_by="NM_003167.4:59..916"
                     /db_xref="CCDS:CCDS12707.1"
                     /db_xref="GeneID:6822"
                     /db_xref="HGNC:HGNC:11458"
                     /db_xref="MIM:125263"
ORIGIN      
        1 msddflwfeg iafptmgfrs etlrkvrdef virdedviil typksgtnwl aeilclmhsk
       61 gdakwiqsvp iwerspwves eigytalset esprlfsshl piqlfpksff sskakviylm
      121 rnprdvlvsg yffwknmkfi kkpksweeyf ewfcqgtvly gswfdhihgw mpmreeknfl
      181 llsyeelkqd tgrtiekicq flgktlepee lnlilknssf qsmkenkmsn ysllsvdyvv
      241 dkaqllrkgv sgdwknhftv aqaedfdklf qekmadlpre lfpwe
//
LOCUS       NP_001356021             360 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356021
VERSION     NP_001356021.1
DBSOURCE    REFSEQ: accession NM_001369092.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.71952.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..360
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 6"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40919
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..360
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369092.1:214..1296"
                     /note="isoform 6 is encoded by transcript variant 13"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitvv
//
LOCUS       NP_000284               1093 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphorylase b kinase regulatory subunit beta isoform a [Homo
            sapiens].
ACCESSION   NP_000284
VERSION     NP_000284.1
DBSOURCE    REFSEQ: accession NM_000293.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1093)
  AUTHORS   Yang,X., Zhu,M., Lu,X., Wang,Y. and Xiao,J.
  TITLE     Architecture and activation of human muscle phosphorylase kinase
  JOURNAL   Nat Commun 15 (1), 2719 (2024)
   PUBMED   38548794
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1093)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1093)
  AUTHORS   Yang,W., Zhang,C., Li,Y., Jin,A., Sun,Y., Yang,X., Wang,B. and
            Guo,W.
  TITLE     Phosphorylase Kinase beta Represents a Novel Prognostic Biomarker
            and Inhibits Malignant Phenotypes of Liver Cancer Cell
  JOURNAL   Int J Biol Sci 15 (12), 2596-2606 (2019)
   PUBMED   31754332
  REMARK    GeneRIF: PHKB acts as a novel prognostic indicator for HCC, which
            exerts its suppression function via inactivating AKT and STAT3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1093)
  AUTHORS   Wang,G., Shen,W., Liu,C.Y., Liu,Y., Wu,T., Cui,X., Yu,T., Zhu,Y.,
            Song,J., Du,P. and Cui,L.
  TITLE     Phosphorylase kinase beta affects colorectal cancer cell growth and
            represents a novel prognostic biomarker
  JOURNAL   J Cancer Res Clin Oncol 143 (6), 971-980 (2017)
   PUBMED   28275865
  REMARK    GeneRIF: PHKb affects colorectal cancer cell growth and represents
            a novel prognostic biomarker.
REFERENCE   5  (residues 1 to 1093)
  AUTHORS   Terashima,M., Fujita,Y., Togashi,Y., Sakai,K., De Velasco,M.A.,
            Tomida,S. and Nishio,K.
  TITLE     KIAA1199 interacts with glycogen phosphorylase kinase beta-subunit
            (PHKB) to promote glycogen breakdown and cancer cell survival
  JOURNAL   Oncotarget 5 (16), 7040-7050 (2014)
   PUBMED   25051373
  REMARK    GeneRIF: Analysis showed that the glycogen phosphorylase kinase
            beta-subunit (PHKB) interacted with the C-terminal region of
            KIAA1199 protein.
REFERENCE   6  (residues 1 to 1093)
  AUTHORS   van den Berg,I.E., van Beurden,E.A., de Klerk,J.B., van
            Diggelen,O.P., Malingre,H.E., Boer,M.M. and Berger,R.
  TITLE     Autosomal recessive phosphorylase kinase deficiency in liver,
            caused by mutations in the gene encoding the beta subunit (PHKB)
  JOURNAL   Am J Hum Genet 61 (3), 539-546 (1997)
   PUBMED   9326319
REFERENCE   7  (residues 1 to 1093)
  AUTHORS   Burwinkel,B., Maichele,A.J., Aagenaes,O., Bakker,H.D., Lerner,A.,
            Shin,Y.S., Strachan,J.A. and Kilimann,M.W.
  TITLE     Autosomal glycogenosis of liver and muscle due to phosphorylase
            kinase deficiency is caused by mutations in the phosphorylase
            kinase beta subunit (PHKB)
  JOURNAL   Hum Mol Genet 6 (7), 1109-1115 (1997)
   PUBMED   9215682
REFERENCE   8  (residues 1 to 1093)
  AUTHORS   Wullrich-Schmoll,A. and Kilimann,M.W.
  TITLE     Structure of the human gene encoding the phosphorylase kinase beta
            subunit (PHKB)
  JOURNAL   Eur J Biochem 238 (2), 374-380 (1996)
   PUBMED   8681948
REFERENCE   9  (residues 1 to 1093)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   10 (residues 1 to 1093)
  AUTHORS   Francke,U., Darras,B.T., Zander,N.F. and Kilimann,M.W.
  TITLE     Assignment of human genes for phosphorylase kinase subunits alpha
            (PHKA) to Xq12-q13 and beta (PHKB) to 16q12-q13
  JOURNAL   Am J Hum Genet 45 (2), 276-282 (1989)
   PUBMED   2757032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X84908.1 and AC092374.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, encoded by two different
            genes. The beta subunit is the same in both the muscle and hepatic
            isoforms, encoded by this gene, which is a member of the
            phosphorylase b kinase regulatory subunit family. The gamma subunit
            also includes the skeletal muscle and hepatic isoforms, encoded by
            two different genes. The delta subunit is a calmodulin and can be
            encoded by three different genes. The gamma subunits contain the
            active site of the enzyme, whereas the alpha and beta subunits have
            regulatory functions controlled by phosphorylation. The delta
            subunit mediates the dependence of the enzyme on calcium
            concentration. Mutations in this gene cause glycogen storage
            disease type 9B, also known as phosphorylase kinase deficiency of
            liver and muscle. Alternatively spliced transcript variants
            encoding different isoforms have been identified in this gene. Two
            pseudogenes have been found on chromosomes 14 and 20,
            respectively.[provided by RefSeq, Feb 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X84908.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323584.10/ ENSP00000313504.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1093
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.1"
     Protein         1..1093
                     /product="phosphorylase b kinase regulatory subunit beta
                     isoform a"
                     /EC_number="2.7.11.19"
                     /note="phosphorylase b kinase regulatory subunit beta;
                     phosphorylase kinase beta-subunit; phosphorylase kinase
                     subunit beta; phosphorylase kinase, beta"
                     /calculated_mol_wt=124754
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:P12798; N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q93100.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q93100.3)"
     Region          7..29
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93100.3)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P12798; propagated from
                     UniProtKB/Swiss-Prot (Q93100.3)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q93100.3)"
     Region          49..>470
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          689..716
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93100.3)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P12798; propagated from
                     UniProtKB/Swiss-Prot (Q93100.3)"
     Region          <751..878
                     /region_name="Bac_rhamnosid6H"
                     /note="Bacterial alpha-L-rhamnosidase 6 hairpin
                     glycosidase domain; cl46875"
                     /db_xref="CDD:481215"
     Region          768..795
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93100.3)"
     Region          898..1077
                     /region_name="KPBB_C"
                     /note="Phosphorylase b kinase C-terminal domain;
                     pfam19292"
                     /db_xref="CDD:437124"
     Region          920..951
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q93100.3)"
     CDS             1..1093
                     /gene="PHKB"
                     /coded_by="NM_000293.3:21..3302"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10729.1"
                     /db_xref="GeneID:5257"
                     /db_xref="HGNC:HGNC:8927"
                     /db_xref="MIM:172490"
ORIGIN      
        1 magaagltae vswkvlerra rtkrsgsvye plksinlprp dnetlwdkld hyyrivkstl
       61 llyqspttgl fptktcggdq kakiqdslyc aagawalala yrridddkgr thelehsaik
      121 cmrgilycym rqadkvqqfk qdprpttclh svfnvhtgde llsyeeyghl qinavslyll
      181 ylvemissgl qiiyntdevs fiqnlvfcve rvyrvpdfgv wergskynng stelhsssvg
      241 lakaaleain gfnlfgnqgc swsvifvdld ahnrnrqtlc sllpresrsh ntdaallpci
      301 sypafaldde vlfsqtldkv vrklkgkygf krflrdgyrt sledpnrcyy kpaeiklfdg
      361 iecefpiffl ymmidgvfrg npkqvqeyqd lltpvlhhtt egypvvpkyy yvpadfveye
      421 knnpgsqkrf psncgrdgkl flwgqalyii aklladelis pkdidpvqry vplkdqrnvs
      481 mrfsnqgple ndlvvhvali aesqrlqvfl ntygiqtqtp qqvepiqiwp qqelvkaylq
      541 lgineklgls grpdrpigcl gtskiyrilg ktvvcypiif dlsdfymsqd vflliddikn
      601 alqfikqywk mhgrplflvl irednirgsr fnpildmlaa lkkgiiggvk vhvdrlqtli
      661 sgavveqldf lrisdteelp efksfeelep pkhskvkrqs stpsapelgq qpdvnisewk
      721 dkptheilqk lndcsclasq aillgillkr egpnfitkeg tvsdhiervy rragsqklwl
      781 avrygaaftq kfsssiaphi ttflvhgkqv tlgafgheee visnplsprv iqniiyykcn
      841 thdereaviq qelvihigwi isnnpelfsg mlkirigwii hameyelqir ggdkpaldly
      901 qlspsevkql lldilqpqqn grcwlnrrqi dgslnrtptg fydrvwqile rtpngiivag
      961 khlpqqptls dmtmyemnfs llvedtlgni dqpqyrqivv ellmvvsivl ernpelefqd
     1021 kvdldrlvke afnefqkdqs rlkeiekqdd mtsfyntppl gkrgtcsylt kavmnllleg
     1081 evkpnnddpc lis
//
LOCUS       NP_001341825            2861 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform c [Homo sapiens].
ACCESSION   NP_001341825
VERSION     NP_001341825.1
DBSOURCE    REFSEQ: accession NM_001354896.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2861)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2861)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2861)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2861)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2861)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2861)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2861)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2861)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2861)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2861)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.53642.1,
                                           SRR1660807.179835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2861
                     /product="adenomatous polyposis coli protein isoform c"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=313343
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Region          <8..272
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          239..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          340..392
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          393..466
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          490..526
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          523..565
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          530..571
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          534..571
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          566..609
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          581..613
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(604,608,612,651,655,659,696,700,704)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          610..656
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          621..662
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          657..701
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          667..707
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          671..705
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          702..743
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          709..749
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          713..749
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          744..785
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          750..1037
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          846..896
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            926
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          941..961
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          976..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          978..1355
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1038..1187
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1054..1153
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1056
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1117..1187
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1208..1262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1275..>1292
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1301..1386
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1309..1719
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1329..1394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1421..1493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1456
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1544..1587
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1601..1629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1655..1678
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1680..1733
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1682..1735
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1734..1755
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1747..1854
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1764..1857
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1881
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1882
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1884..1911
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1891..1965
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1899..1968
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1983..2029
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1989
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2051..2070
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2053..2077
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2061..2090
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2165..2653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2185..2692
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2241..2586
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2491
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2493..2861
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2685..2732
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2688..2861
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2692..2861
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2697
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2747..2861
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2821..2824
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2859..2861
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2861
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354896.2:60..8645"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr irqllqsqat
      241 eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas vlssssthsa
      301 prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs gclplliqll
      361 hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll eqiraycetc
      421 wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg rkatrgissq
      481 elgqglsggl qaiaellqvd cemygltndh ysitlrryag maltnltfgd vankatlcsm
      541 kgcmralvaq lksesedlqq viasvlrnls wradvnskkt lrevgsvkal mecalevkke
      601 stlksvlsal wnlsahcten kadicavdga laflvgtlty rsqtntlaii esgggilrnv
      661 ssliatnedh rqilrenncl qtllqhlksh sltivsnacg tlwnlsarnp kdqealwdmg
      721 avsmlknlih skhkmiamgs aaalrnlman rpakykdani mspgsslpsl hvrkqkalea
      781 eldaqhlset fdnidnlspk ashrskqrhk qslygdyvfd tnrhddnrsd nfntgnmtvl
      841 spylnttvlp sssssrgsld ssrsekdrsl erergiglgn yhpatenpgt sskrglqist
      901 taaqiakvme evsaihtsqe drssgsttel hcvtdernal rrssaahths ntynftksen
      961 snrtcsmpya kleykrssnd slnsvsssdg ygkrgqmkps iesyseddes kfcsygqypa
     1021 dlahkihsan hmddndgeld tpinyslkys deqlnsgrqs psqnerwarp khiiedeikq
     1081 seqrqsrnqs ttypvytest ddkhlkfqph fgqqecvspy rsrgangset nrvgsnhgin
     1141 qnvsqslcqe ddyeddkptn yseryseeeq heeeerptny sikyneekrh vdqpidyslk
     1201 yatdipssqk qsfsfsksss gqssktehms sssentstps snakrqnqlh pssaqsrsgq
     1261 pqkaatckvs sinqetiqty cvedtpicfs rcsslsslss aedeigcnqt tqeadsantl
     1321 qiaeikekig trsaedpvse vpavsqhprt kssrlqgssl ssesarhkav efssgaksps
     1381 ksgaqtpksp pehyvqetpl mfsrctsvss ldsfesrsia ssvqsepcsg mvsgiispsd
     1441 lpdspgqtmp psrsktpppp pqtaqtkrev pknkaptaek resgpkqaav naavqrvqvl
     1501 pdadtllhfa testpdgfsc ssslsalsld epfiqkdvel rimppvqend ngneteseqp
     1561 kesnenqeke aektidsekd llddsddddi eileeciisa mptkssrkak kpaqtasklp
     1621 ppvarkpsql pvykllpsqn rlqpqkhvsf tpgddmprvy cvegtpinfs tatslsdlti
     1681 esppnelaag egvrggaqsg efekrdtipt egrstdeaqg gktssvtipe lddnkaeegd
     1741 ilaecinsam pkgkshkpfr vkkimdqvqq asasssapnk nqldgkkkkp tspvkpipqn
     1801 teyrtrvrkn adsknnlnae rvfsdnkdsk kqnlknnskv fndklpnned rvrgsfafds
     1861 phhytpiegt pycfsrndsl ssldfddddv dlsrekaelr kakenkesea kvtshtelts
     1921 nqqsanktqa iakqpinrgq pkpilqkqst fpqsskdipd rgaatdeklq nfaientpvc
     1981 fshnsslssl sdidqennnk enepiketep pdsqgepskp qasgyapksf hvedtpvcfs
     2041 rnsslsslsi dseddllqec issampkkkk psrlkgdnek hsprnmggil gedltldlkd
     2101 iqrpdsehgl spdsenfdwk aiqegansiv sslhqaaaaa clsrqassds dsilslksgi
     2161 slgspfhltp dqeekpftsn kgprilkpge kstletkkie seskgikggk kvykslitgk
     2221 vrsnseisgq mkqplqanmp sisrgrtmih ipgvrnssss tspvskkgpp lktpasksps
     2281 egqtattspr gakpsvksel spvarqtsqi ggsskapsrs gsrdstpsrp aqqplsrpiq
     2341 spgrnsispg rngisppnkl sqlprtssps tastkssgsg kmsytspgrq msqqnltkqt
     2401 glsknassip rsesaskgln qmnngngank kvelsrmsst kssgsesdrs erpvlvrqst
     2461 fikeapsptl rrkleesasf eslspssrpa sptrsqaqtp vlspslpdms lsthssvqag
     2521 gwrklppnls ptieyndgrp akrhdiarsh sespsrlpin rsgtwkrehs khssslprvs
     2581 twrrtgssss ilsassesse kaksedekhv nsisgtkqsk enqvsakgtw rkikenefsp
     2641 tnstsqtvss gatngaeskt liyqmapavs ktedvwvrie dcpinnprsg rsptgntppv
     2701 idsvsekanp nikdskdnqa kqnvgngsvp mrtvglenrl nsfiqvdapd qkgteikpgq
     2761 nnpvpvsetn essivertpf sssssskhss psgtvaarvt pfnynpsprk ssadstsarp
     2821 sqiptpvnnn tkkrdsktds tessgtqspk rhsgsylvts v
//
LOCUS       NP_001278772             334 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform Ik-8 [Homo sapiens].
ACCESSION   NP_001278772
VERSION     NP_001278772.1
DBSOURCE    REFSEQ: accession NM_001291843.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U40462.1 and JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (Ik-8) lacks three consecutive
            in-frame exons in the central coding region, compared to variant 1.
            The encoded isoform (Ik-8) is shorter than isoform 1. This isoform
            contains no N-terminal zinc finger motifs, and represents a
            non-DNA-binding, dominant-negative isoform (PMID:9892693).
            
            Sequence Note: The 5' UTR of this variant is incomplete because
            there are no full-length transcripts supporting this variant, and
            there is splicing ambiguity in the 5' UTR.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 12937159
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..334
                     /product="DNA-binding protein Ikaros isoform Ik-8"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=36930
     CDS             1..334
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291843.1:15..1019"
                     /note="isoform Ik-8 is encoded by transcript variant Ik-8"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvikeetn
       61 hsemaedlck igserslvld rlasnvakrk ssmpqkflgd kglsdtpyds sasyekenem
      121 mkshvmdqai nnainylgae slrplvqtpp ggsevvpvis pmyqlhkpla egtprsnhsa
      181 qdsavenlll lskaklvpse reaspsnscq dstdtesnne eqrsgliylt nhiapharng
      241 lslkeehray dllraasens qdalrvvsts geqmkvykce hcrvlfldhv mytihmgchg
      301 frdpfecnmc gyhsqdryef sshitrgehr fhms
//
LOCUS       NP_542408                 89 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein light chain 2, cytoplasmic [Homo sapiens].
ACCESSION   NP_542408
VERSION     NP_542408.1
DBSOURCE    REFSEQ: accession NM_080677.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 89)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Day,C.L., Puthalakath,H., Skea,G., Strasser,A., Barsukov,I.,
            Lian,L.Y., Huang,D.C. and Hinds,M.G.
  TITLE     Localization of dynein light chains 1 and 2 and their pro-apoptotic
            ligands
  JOURNAL   Biochem J 377 (Pt 3), 597-605 (2004)
   PUBMED   14561217
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Lei,K. and Davis,R.J.
  TITLE     JNK phosphorylation of Bim-related members of the Bcl2 family
            induces Bax-dependent apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 100 (5), 2432-2437 (2003)
   PUBMED   12591950
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Fuhrmann,J.C., Kins,S., Rostaing,P., El Far,O., Kirsch,J.,
            Sheng,M., Triller,A., Betz,H. and Kneussel,M.
  TITLE     Gephyrin interacts with Dynein light chains 1 and 2, components of
            motor protein complexes
  JOURNAL   J Neurosci 22 (13), 5393-5402 (2002)
   PUBMED   12097491
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Puthalakath,H., Villunger,A., O'Reilly,L.A., Beaumont,J.G.,
            Coultas,L., Cheney,R.E., Huang,D.C. and Strasser,A.
  TITLE     Bmf: a proapoptotic BH3-only protein regulated by interaction with
            the myosin V actin motor complex, activated by anoikis
  JOURNAL   Science 293 (5536), 1829-1832 (2001)
   PUBMED   11546872
  REMARK    Erratum:[Science 2002 Aug 16;297(5584):1122]
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Naisbitt,S., Valtschanoff,J., Allison,D.W., Sala,C., Kim,E.,
            Craig,A.M., Weinberg,R.J. and Sheng,M.
  TITLE     Interaction of the postsynaptic density-95/guanylate kinase
            domain-associated protein complex with a light chain of myosin-V
            and dynein
  JOURNAL   J Neurosci 20 (12), 4524-4534 (2000)
   PUBMED   10844022
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA140058.1, BF528423.1, BC010744.1, DB022843.1, CN280282.1 and
            AC015813.12.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA140058.1, SRR3476690.1025326.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000579991.3/ ENSP00000477310.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..89
                     /product="dynein light chain 2, cytoplasmic"
                     /note="radial spoke 22 homolog; DLC8b; 8 kDa dynein light
                     chain b"
                     /calculated_mol_wt=10219
     Region          5..88
                     /region_name="DLC-like_DYNLL1_DYNLL2"
                     /note="dynein light chain (DLC)-like domain found in the
                     cytoplasmic dynein light chain 1 (DYNLL1) family; cd21452"
                     /db_xref="CDD:412000"
     Site            41
                     /site_type="other"
                     /note="Interaction with myosin V motor complex.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q96FJ2.1)"
     CDS             1..89
                     /gene="DYNLL2"
                     /gene_synonym="Dlc2; DNCL1B; RSPH22"
                     /coded_by="NM_080677.3:275..544"
                     /db_xref="CCDS:CCDS11601.1"
                     /db_xref="GeneID:140735"
                     /db_xref="HGNC:HGNC:24596"
                     /db_xref="MIM:608942"
ORIGIN      
        1 msdrkavikn admsedmqqd avdcatqame kyniekdiaa yikkefdkky nptwhcivgr
       61 nfgsyvthet khfiyfylgq vaillfksg
//
LOCUS       NP_001309864             858 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit isoform c [Homo sapiens].
ACCESSION   NP_001309864
VERSION     NP_001309864.1
DBSOURCE    REFSEQ: accession NM_001322935.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 858)
  AUTHORS   De Paolis,V., Troisi,V., Bordin,A., Pagano,F., Caputo,V. and
            Parisi,C.
  TITLE     Unconventional p65/p52 NF-kappaB module regulates key tumor
            microenvironment-related genes in breast tumor-associated
            macrophages (TAMs)
  JOURNAL   Life Sci 357, 123059 (2024)
   PUBMED   39278618
  REMARK    GeneRIF: Unconventional p65/p52 NF-kappaB module regulates key
            tumor microenvironment-related genes in breast tumor-associated
            macrophages (TAMs).
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Vallabhapurapu,S. and Karin,M.
  TITLE     Regulation and function of NF-kappaB transcription factors in the
            immune system
  JOURNAL   Annu Rev Immunol 27, 693-733 (2009)
   PUBMED   19302050
  REMARK    Review article
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Heusch,M., Lin,L., Geleziunas,R. and Greene,W.C.
  TITLE     The generation of nfkb2 p52: mechanism and efficiency
  JOURNAL   Oncogene 18 (46), 6201-6208 (1999)
   PUBMED   10597218
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Lombardi,L., Ciana,P., Cappellini,C., Trecca,D., Guerrini,L.,
            Migliazza,A., Maiolo,A.T. and Neri,A.
  TITLE     Structural and functional characterization of the promoter regions
            of the NFKB2 gene
  JOURNAL   Nucleic Acids Res 23 (12), 2328-2336 (1995)
   PUBMED   7541912
REFERENCE   6  (residues 1 to 858)
  AUTHORS   Liptay,S., Schmid,R.M., Nabel,E.G. and Nabel,G.J.
  TITLE     Transcriptional regulation of NF-kappa B2: evidence for kappa
            B-mediated positive and negative autoregulation
  JOURNAL   Mol Cell Biol 14 (12), 7695-7703 (1994)
   PUBMED   7969113
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Bours,V., Burd,P.R., Brown,K., Villalobos,J., Park,S., Ryseck,R.P.,
            Bravo,R., Kelly,K. and Siebenlist,U.
  TITLE     A novel mitogen-inducible gene product related to p50/p105-NF-kappa
            B participates in transactivation through a kappa B site
  JOURNAL   Mol Cell Biol 12 (2), 685-695 (1992)
   PUBMED   1531086
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Schreck,R., Albermann,K. and Baeuerle,P.A.
  TITLE     Nuclear factor kappa B: an oxidative stress-responsive
            transcription factor of eukaryotic cells (a review)
  JOURNAL   Free Radic Res Commun 17 (4), 221-237 (1992)
   PUBMED   1473734
  REMARK    Review article
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Schmid,R.M., Perkins,N.D., Duckett,C.S., Andrews,P.C. and
            Nabel,G.J.
  TITLE     Cloning of an NF-kappa B subunit which stimulates HIV transcription
            in synergy with p65
  JOURNAL   Nature 352 (6337), 733-736 (1991)
   PUBMED   1876189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121928.13 and BC002844.2.
            
            Summary: This gene encodes a subunit of the transcription factor
            complex nuclear factor-kappa-B (NFkB). The NFkB complex is
            expressed in numerous cell types and functions as a central
            activator of genes involved in inflammation and immune function.
            The protein encoded by this gene can function as both a
            transcriptional activator or repressor depending on its
            dimerization partner. The p100 full-length protein is
            co-translationally processed into a p52 active form. Chromosomal
            rearrangements and translocations of this locus have been observed
            in B cell lymphomas, some of which may result in the formation of
            fusion proteins. There is a pseudogene for this gene on chromosome
            18. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..858
                     /product="nuclear factor NF-kappa-B p100 subunit isoform
                     c"
                     /note="nuclear factor NF-kappa-B p100 subunit; oncogene
                     Lyt-10; DNA-binding factor KBF2; lymphocyte translocation
                     chromosome 10 protein; transcription factor NFKB2; NFKB,
                     p52/p100 subunit; nuclear factor Kappa-B, subunit 2;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells 2 (p49/p100); nuclear factor of Kappa light chain
                     gene enhancer in B cells 2; nuclear factor NF-kappa-B p52
                     subunit"
                     /calculated_mol_wt=92558
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          396..664
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(445,447,451..452,455..457,459..460,464,467,482,484,
                     486,490..491,494..496,498..499,503,506,515,517,519,
                     523..524,529..531,533..534,538,541)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          445..482
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          484..515
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          517..544
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(557,559,563..564,567..569,571..572,576,579,588,591,
                     593,597..598,601..603,605..606,610,613,623,625,627,
                     631..632,635..637,639..640,644,647,656)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          557..588
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          591..623
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          625..656
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          732..807
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     CDS             1..858
                     /gene="NFKB2"
                     /gene_synonym="CVID10; H2TF1; LYT-10; LYT10; NF-kB2; p100;
                     p49/p100; p52"
                     /coded_by="NM_001322935.1:564..3140"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:4791"
                     /db_xref="HGNC:HGNC:7795"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve ggslgffpss layspyqsga gpmgcypggg
      361 ggaqmaatvp srdsgeeaae psapsrtpqc epqapemlqr areynarlfg laqrsarall
      421 dygvtadara llagqrhllt aqdengdtpl hlaiihgqts vieqivyvih haqdlgvvnl
      481 tnhlhqtplh lavitgqtsv vsfllrvgad palldrhgds amhlalraga gapellrall
      541 qsgapavpql lhmpdfegly pvhlavrars pecldllvds gaeveaterq ggrtalhlat
      601 emeelglvth lvtklranvn artfagntpl hlaaglgypt ltrlllkaga dihaeneepl
      661 cplpspptsd sdsdsegpek dtrssfrght pldltcstkv ktlllnaaqn tmeppltpps
      721 pagpglslgd talqnleqll dgpeaqgswa elaerlglrs lvdtyrqtts psgsllrsye
      781 laggdlagll ealsdmglee gvrllrgpet rdklpstaev kedsaygsqs veqeaeklgp
      841 ppeppgglch ghpqpqvh
//
LOCUS       NP_001354770            1251 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin-like and fibronectin type III domain-containing
            protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001354770
VERSION     NP_001354770.1
DBSOURCE    REFSEQ: accession NM_001367841.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1251)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1251)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 1251)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1251)
  AUTHORS   Verma,S.P. and Das,P.
  TITLE     Novel splicing in IGFN1 intron 15 and role of stable G-quadruplex
            in the regulation of splicing in renal cell carcinoma
  JOURNAL   PLoS One 13 (10), e0205660 (2018)
   PUBMED   30335789
  REMARK    GeneRIF: Study results in UOK146 renal cell carcinoma cell line
            provide evidence of novel splicing in intron 15 of IGFN1 leading to
            the formation of two more alternative spliced isoforms. Potential
            G-quadruplex forming sequence (PQS) in this intron forms a stable
            G-quadruplex which is involved in the alternative splicing and
            regulates splicing efficiency.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1251)
  AUTHORS   Wen,X., Liu,Y., Yan,Q., Liang,M., Tang,M., Liu,R., Pan,J., Liu,Q.,
            Chen,T., Guo,S., Liang,J., Lu,L., Ding,X., Chen,W. and Wei,L.
  TITLE     Association of IGFN1 variant with polypoidal choroidal vasculopathy
  JOURNAL   J Gene Med 20 (2-3), e3007 (2018)
   PUBMED   29323771
  REMARK    GeneRIF: A novel variant, c.6196A>G in the IGFN1 gene, was
            significantly associated with only Polypoidal choroidal
            vasculopathy (combined p = 7.1 x 10(-11) , odds ratio = 9.44), but
            not with neovascular age-related macular degeneration(combined p =
            0.683, odds ratio = 1.30).
REFERENCE   6  (residues 1 to 1251)
  AUTHORS   Mansilla,F., Dominguez,C.A., Yeadon,J.E., Corydon,T.J., Burden,S.J.
            and Knudsen,C.R.
  TITLE     Translation elongation factor eEF1A binds to a novel myosin binding
            protein-C-like protein
  JOURNAL   J Cell Biochem 105 (3), 847-858 (2008)
   PUBMED   18756455
  REMARK    GeneRIF: a model in which this increased expression of IGFN1 serves
            to down-regulate protein synthesis via interaction with eEF1A
            during denervation.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC103925.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
FEATURES             Location/Qualifiers
     source          1..1251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..1251
                     /product="immunoglobulin-like and fibronectin type III
                     domain-containing protein 1 isoform 2"
                     /note="immunoglobulin-like and fibronectin type III
                     domain-containing protein 1; eEF1A2 binding protein;
                     EEF1A2-binding protein 1; KY-interacting protein 1"
                     /calculated_mol_wt=137633
     Region          29..120
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          46..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          59..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          61..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VF2.2)"
     Region          86..90
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          100..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          113..116
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          166..199
                     /region_name="THB"
                     /note="Tri-helix bundle domain; pfam18362"
                     /db_xref="CDD:465725"
     Region          309..395
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          403..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VF2.2)"
     Region          457..540
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          473..477
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..489
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          510..514
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          524..529
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          533..536
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          558..640
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          566..570
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          579..583
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          606..610
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          620..625
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          633..636
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          644..736
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(644,711,726)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <709..>946
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            order(727..728,730..731)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          958..1037
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          966..970
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          979..983
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1002..1006
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1016..1021
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1029..1033
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1041..1130
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1041,1106,1121)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1122..1123,1125..1126)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1157..1246
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1174..1178
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1187..1191
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1212..1216
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1226..1231
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1239..1242
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1251
                     /gene="IGFN1"
                     /gene_synonym="EEF1A2BP1"
                     /coded_by="NM_001367841.1:132..3887"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS91141.1"
                     /db_xref="GeneID:91156"
                     /db_xref="HGNC:HGNC:24607"
                     /db_xref="MIM:617309"
ORIGIN      
        1 magklrkshi pgvsiwqlve eipegcstpd feqkpvtsal pegknavfra vvcgeprpev
       61 rwqnskgdls dsskykisss pgskehvlqi nkltgedtdl yrctavnayg eaacsvrltv
      121 ievgfrknrk rhrepqedlr kelmdfrkll kkrappapkk kmdleqiwql lmtadrkdye
      181 kiclkygivd yrgmlrrlqe mkkeqedkma qyintisslr hirvtkdgna kfdleldlkd
      241 sqskiylykd gemipygfnn qtkhclrrlg kryefqiqdl rpedsgiyqv kvedavvfst
      301 eleasaippr vvvplaethc eeqgdavfec tlsspcpsaa whfrhrllhp sdkyevyvsp
      361 dglthrlvvr garfsdmgpy slgtglytss awlvveagkd kdlqstsadh klqsrrsgkd
      421 grldiygerr datrsstsry kpgtgsfskd aqgpmghfsq gladmevqpg eaatlsctlt
      481 sdlgpgtwfk dgvklttqdg vifkqdglvh slfithvqgt qagrytfvag dqqseatltv
      541 qdsptiapdv teklreplvv kagkpvivki pfqshlpiqa awrkdgaevv gssdreaqvd
      601 lgdgytrlcl psagrkdcgq ysvtlrsegg svqaeltlqv idkpdppqgp mevqdchrag
      661 vclrwrpprd nggrtvecyv verrqagrst wlkvgeapad sttftdahve pgrkytfrvr
      721 avtsegagea leseeilvap ealpkapsap ailsassqgi tltwtaprgp gsahilgyli
      781 errkkgsntw tavndqpvpe rrwtvadvrq gcqyefrvta vapsgpgepg ppsdavfard
      841 pmrppglvrn lqvtdrsnts itlswagpdt qegdeaqgyv velcssdslq wlpchvgtvp
      901 vttytakglr pgegyfvrvt avneggqsqp saldtlvqam pvtvcpkflv dsstkdlltv
      961 kvgdtvrvpv sfeampmpev twlkdglplp krsvtvtkdg ltqllipvag lsdsglytvv
     1021 lrtlqgkeva hsfrirvaac pqapgpihlq envpgtvtae wepspdeaqd vplhyavftr
     1081 ssahgpwhea adrihtnrft llgilpghey hfrvvaknel gaskpsdtsq pwciprqrdr
     1141 ftvkapcyre pdlsqkprfl vglrshllpq gceccmscav qgsprphvtw fkndrslegn
     1201 pavystdllg vcsltipsvs pkdsgeykav aentlgqavs tatlivieps t
//
LOCUS       NP_003789                734 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-catulin isoform a [Homo sapiens].
ACCESSION   NP_003789
VERSION     NP_003789.1
DBSOURCE    REFSEQ: accession NM_003798.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Wu,D., Zhu,J., Yang,F., Li,R., Liu,L., Liu,D., Liu,C., Qu,X.,
            Liu,H., Ji,M., Qin,X., Hua,L. and Xiang,Y.
  TITLE     CTNNAL1 deficiency suppresses CFTR expression in HDM-induced asthma
            mouse model through ROCK1-CAL signaling pathway
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1618-1629 (2023)
   PUBMED   37715489
  REMARK    GeneRIF: CTNNAL1 deficiency suppresses CFTR expression in
            HDM-induced asthma mouse model through ROCK1-CAL signaling pathway.
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Tung,C.H., Huang,M.F., Liang,C.H., Wu,Y.Y., Wu,J.E., Hsu,C.L.,
            Chen,Y.L. and Hong,T.M.
  TITLE     alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer
  JOURNAL   Theranostics 12 (3), 1173-1186 (2022)
   PUBMED   35154481
  REMARK    GeneRIF: alpha-Catulin promotes cancer stemness by antagonizing
            WWP1-mediated KLF5 degradation in lung cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Surpili,M.J., Delben,T.M. and Kobarg,J.
  TITLE     Identification of proteins that interact with the central
            coiled-coil region of the human protein kinase NEK1
  JOURNAL   Biochemistry 42 (51), 15369-15376 (2003)
   PUBMED   14690447
REFERENCE   7  (residues 1 to 734)
  AUTHORS   Shieh,Y.S., Chang,L.C., Chiu,K.C., Wu,C.W. and Lee,H.S.
  TITLE     Cadherin and catenin expression in mucoepidermoid carcinoma:
            correlation with histopathologic grade, clinical stage, and patient
            outcome
  JOURNAL   J Oral Pathol Med 32 (5), 297-304 (2003)
   PUBMED   12694354
  REMARK    GeneRIF: Abnormal expression of alpha-catenin was seen in
            mucoepidermoid carcinoma.
REFERENCE   8  (residues 1 to 734)
  AUTHORS   Park,B., Nguyen,N.T., Dutt,P., Merdek,K.D., Bashar,M.,
            Sterpetti,P., Tosolini,A., Testa,J.R. and Toksoz,D.
  TITLE     Association of Lbc Rho guanine nucleotide exchange factor with
            alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports
            serum response factor activation
  JOURNAL   J Biol Chem 277 (47), 45361-45370 (2002)
   PUBMED   12270917
  REMARK    GeneRIF: Results show that alpha-catulin co-expression leads to
            increased Lbc-induced serum response factor activation and may
            modulate Rho pathway signaling in vivo by providing a scaffold for
            the Lbc Rho guanine nucleotide exchange factor.
REFERENCE   9  (residues 1 to 734)
  AUTHORS   Janssens,B., Staes,K. and van Roy,F.
  TITLE     Human alpha-catulin, a novel alpha-catenin-like molecule with
            conserved genomic structure, but deviating alternative splicing
  JOURNAL   Biochim Biophys Acta 1447 (2-3), 341-347 (1999)
   PUBMED   10542337
REFERENCE   10 (residues 1 to 734)
  AUTHORS   Zhang,J.S., Nelson,M., Wang,L., Liu,W., Qian,C.P., Shridhar,V.,
            Urrutia,R. and Smith,D.I.
  TITLE     Identification and chromosomal localization of CTNNAL1, a novel
            protein homologous to alpha-catenin
  JOURNAL   Genomics 54 (1), 149-154 (1998)
   PUBMED   9806841
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022926.1 and AF030233.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022926.1, AK223230.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325551.9/ ENSP00000320434.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..734
                     /product="alpha-catulin isoform a"
                     /note="alpha-catulin; alpha2-catulin; catenin alpha-like
                     protein 1; alpha-catenin-related protein; catenin
                     (cadherin-associated protein), alpha-like 1"
                     /calculated_mol_wt=81766
     Region          31..675
                     /region_name="Vinculin"
                     /note="Vinculin family; pfam01044"
                     /db_xref="CDD:460040"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88327; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     Site            538
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBT7.2)"
     CDS             1..734
                     /gene="CTNNAL1"
                     /gene_synonym="ACRP; alpha-CATU; CLLP"
                     /coded_by="NM_003798.4:58..2262"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6775.1"
                     /db_xref="GeneID:8727"
                     /db_xref="HGNC:HGNC:2512"
                     /db_xref="MIM:604785"
ORIGIN      
        1 maaspgpagv ggagavygsg ssgfaldsgl eiktrsveqt llplvsqitt linhkdntkk
       61 sdktlqaiqr vgqavnlavg rfvkvgeaia nenwdlkeei niacieakqa getiaaltdi
      121 tnlnhlesdg qitiftdktg vikaarllls svtkvlllad rvvikqiits rnkvlatmer
      181 lekvnsfqef vqifsqfgne mvefahlsgd rqndlkdekk kakmaaarav lekctmmllt
      241 asktclrhpn cesahknkeg vfdrmkvald kvieivtdck pngetdissi siftgikefk
      301 mniealrenl yfqskenlsv tlevilerme dftdsaytsh ehrerilels tqarmelqql
      361 isvwiqaqsk ktksiaeele lsilkishsl nelkkelhst atqlaadllk yhadhvvlka
      421 lkltgvegnl ealaeyackl seqkeqlvet crllrhisgt epleitciha eetfqvtgqq
      481 iisaaetltl hpsskiaken ldvfceawes qisdmstllr eindvfegrr gekygylslp
      541 kpmknnanlk slkpdkpdse eqakiaklgl klglltsdad ceiekwedqe neivqygrnm
      601 ssmayslylf trgegplkts qdlihqlevf aaeglkltss vqafskqlkd ddklmlllei
      661 nkliplchql qtvtktslqn kvflkvdkci tktrsmmall vqllslcykl lkklqmenng
      721 wvsvtnkdtm dskt
//
LOCUS       NP_006847                483 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-7 isoform 2 [Homo
            sapiens].
ACCESSION   NP_006847
VERSION     NP_006847.1
DBSOURCE    REFSEQ: accession NM_006856.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Zhang,J., Liu,D., Deng,G., Wang,Q., Li,L., Zhang,J. and Wu,H.
  TITLE     lncRNA prostate cancer-associated transcript 18 upregulates
            activating transcription factor 7 to prevent metastasis of
            triple-negative breast cancer via sponging miR-103a-3p
  JOURNAL   Bioengineered 12 (2), 12070-12086 (2021)
   PUBMED   34787047
  REMARK    GeneRIF: lncRNA prostate cancer-associated transcript 18
            upregulates activating transcription factor 7 to prevent metastasis
            of triple-negative breast cancer via sponging miR-103a-3p.
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Newman,S.P., Bates,N.P., Vernimmen,D., Parker,M.G. and Hurst,H.C.
  TITLE     Cofactor competition between the ligand-bound oestrogen receptor
            and an intron 1 enhancer leads to oestrogen repression of ERBB2
            expression in breast cancer
  JOURNAL   Oncogene 19 (4), 490-497 (2000)
   PUBMED   10698518
REFERENCE   6  (residues 1 to 483)
  AUTHORS   De Graeve,F., Bahr,A., Sabapathy,K.T., Hauss,C., Wagner,E.F.,
            Kedinger,C. and Chatton,B.
  TITLE     Role of the ATFa/JNK2 complex in Jun activation
  JOURNAL   Oncogene 18 (23), 3491-3500 (1999)
   PUBMED   10376527
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Goetz,J., Chatton,B., Mattei,M.G. and Kedinger,C.
  TITLE     Structure and expression of the ATFa gene
  JOURNAL   J Biol Chem 271 (47), 29589-29598 (1996)
   PUBMED   8939888
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Bocco,J.L., Bahr,A., Goetz,J., Hauss,C., Kallunki,T., Kedinger,C.
            and Chatton,B.
  TITLE     In vivo association of ATFa with JNK/SAP kinase activities
  JOURNAL   Oncogene 12 (9), 1971-1980 (1996)
   PUBMED   8649858
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Pescini,R., Kaszubska,W., Whelan,J., DeLamarter,J.F. and Hooft van
            Huijsduijnen,R.
  TITLE     ATF-a0, a novel variant of the ATF/CREB transcription factor
            family, forms a dominant transcription inhibitor in ATF-a
            heterodimers
  JOURNAL   J Biol Chem 269 (2), 1159-1165 (1994)
   PUBMED   8288576
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Gaire,M., Chatton,B. and Kedinger,C.
  TITLE     Isolation and characterization of two novel, closely related ATF
            cDNA clones from HeLa cells
  JOURNAL   Nucleic Acids Res 18 (12), 3467-3473 (1990)
   PUBMED   1694576
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB047160.1, X52943.1, BP312300.1, BP279417.1, AC023509.42 and
            BQ184780.1.
            
            Transcript Variant: This variant (2), as well as variants 8 and 9,
            encodes isoform 2 (also known as ATFa2).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1494684.1,
                                           SRR11853564.6774.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000420353.7/ ENSP00000399465.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..483
                     /product="cyclic AMP-dependent transcription factor ATF-7
                     isoform 2"
                     /note="cyclic AMP-dependent transcription factor ATF-7;
                     transcription factor ATF-A"
                     /calculated_mol_wt=51626
     Region          1..285
                     /region_name="Transactivation domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Region          9..31
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          47..84
                     /region_name="GCN4_cent"
                     /note="GCN4 central activation domain-like acidic
                     activation domain; cd12192"
                     /db_xref="CDD:213399"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK11.
                     /evidence=ECO:0000269|PubMed:18950637; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18950637; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Site            order(58..59,61..62,70..71,73..75,77..78,82..84)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:213399"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18950637; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Region          110..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Region          299..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Region          325..483
                     /region_name="Essential for binding adenovirus 2 E1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Region          334..394
                     /region_name="bZIP_ATF2"
                     /note="Basic leucine zipper (bZIP) domain of Activating
                     Transcription Factor-2 (ATF-2) and similar proteins: a
                     DNA-binding and dimerization domain; cd14687"
                     /db_xref="CDD:269835"
     Region          334..394
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269835"
     Region          334..354
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Site            order(335,339,341..343,346,348..350,352..354)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269835"
     Site            order(353,360..361,363..364,367..368,371,374..375,378,
                     381..382,384..385,388..389,392..393)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269835"
     Region          360..388
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Region          407..439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P17544.3)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     CDS             1..483
                     /gene="ATF7"
                     /gene_synonym="ATFA"
                     /coded_by="NM_006856.3:126..1577"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44906.1"
                     /db_xref="GeneID:11016"
                     /db_xref="HGNC:HGNC:792"
                     /db_xref="MIM:606371"
ORIGIN      
        1 mgddrpfvcn apgcgqrftn edhlavhkhk hemtlkfgpa rtdsviiadq tptptrflkn
       61 ceevglfnel assfehefkk aadedekkaa agpldmslps tpdikikeee pvevdssppd
      121 spasspcspp lkekevtpkp vlistptpti vrpgslplhl gydplhptlp sptsvitqap
      181 psnrqmgspt gslplvmhla ngqtmpvlpg ppvqmpsvis larpvsmvpn ipgipgppvn
      241 ssgsispsgh pipseakmrl katlthqvss inggcgmvvg tastmvtarp eqsqiliqhp
      301 dapspaqpqv spaqptpstg grrrrtvded pderrqrfle rnraaasrcr qkrklwvssl
      361 ekkaeeltsq niqlsnevtl lrnevaqlkq lllahkdcpv talqkktqgy lespkessep
      421 tgspapviqh ssatapsngl svrsaaeava tsvltqmasq rtelsmpiqs hvimtpqsqs
      481 agr
//
LOCUS       NP_001351611             285 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform 13 [Homo sapiens].
ACCESSION   NP_001351611
VERSION     NP_001351611.1
DBSOURCE    REFSEQ: accession NM_001364682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 285)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 285)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 285)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 285)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 285)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 285)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 285)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 285)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 285)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 285)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 285)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 285)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 285)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590431.11.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.143201.1,
                                           SRR5189655.173586.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..285
                     /product="tropomyosin alpha-3 chain isoform 13"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=32981
     Region          49..283
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..285
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001364682.1:83..940"
                     /note="isoform 13 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS91061.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 mmeaikkkmq mlkldkenal draeqaeaeq kqaeerskql edelaamqkk lkgtedeldk
       61 ysealkdaqe klelaekkaa daeaevasln rriqlveeel draqerlata lqkleeaeka
      121 adesergmkv ienralkdee kmelqeiqlk eakhiaeead rkyeevarkl viiegdlert
      181 eeraelaesr cremdeqirl mdqnlkclsa aeekysqked kyeeeikilt dklkeaetra
      241 efaersvakl ektiddlede lyaqklkyka iseeldhaln dmtsi
//
LOCUS       NP_001991                287 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin alpha Fc receptor isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001991
VERSION     NP_001991.1
DBSOURCE    REFSEQ: accession NM_002000.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Liu,Q. and Stadtmueller,B.M.
  TITLE     SIgA structures bound to Streptococcus pyogenes M4 and human CD89
            provide insights into host-pathogen interactions
  JOURNAL   Nat Commun 14 (1), 6726 (2023)
   PUBMED   37872175
  REMARK    GeneRIF: SIgA structures bound to Streptococcus pyogenes M4 and
            human CD89 provide insights into host-pathogen interactions.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wu,H., Wang,X., Yang,Z., Zhao,Q., Wen,Y., Li,X., Zhang,W. and
            Gao,R.
  TITLE     Serum Soluble CD89-IgA Complexes Are Elevated in IgA Nephropathy
            without Immunosuppressant History
  JOURNAL   Dis Markers 2020, 8393075 (2020)
   PUBMED   32076466
  REMARK    GeneRIF: Serum Soluble CD89-IgA Complexes Are Elevated in IgA
            Nephropathy without Immunosuppressant History.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Pleass,R.J., Andrews,P.D., Kerr,M.A. and Woof,J.M.
  TITLE     Alternative splicing of the human IgA Fc receptor CD89 in
            neutrophils and eosinophils
  JOURNAL   Biochem J 318 (Pt 3) (Pt 3), 771-777 (1996)
   PUBMED   8836118
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Patry,C., Sibille,Y., Lehuen,A. and Monteiro,R.C.
  TITLE     Identification of Fc alpha receptor (CD89) isoforms generated by
            alternative splicing that are differentially expressed between
            blood monocytes and alveolar macrophages
  JOURNAL   J Immunol 156 (11), 4442-4448 (1996)
   PUBMED   8666819
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Morton,H.C., Schiel,A.E., Janssen,S.W. and van de Winkel,J.G.
  TITLE     Alternatively spliced forms of the human myeloid Fc alpha receptor
            (CD89) in neutrophils
  JOURNAL   Immunogenetics 43 (4), 246-247 (1996)
   PUBMED   8575829
REFERENCE   7  (residues 1 to 287)
  AUTHORS   de Wit,T.P., Morton,H.C., Capel,P.J. and van de Winkel,J.G.
  TITLE     Structure of the gene for the human myeloid IgA Fc receptor (CD89)
  JOURNAL   J Immunol 155 (3), 1203-1209 (1995)
   PUBMED   7636188
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Kremer,E.J., Kalatzis,V., Baker,E., Callen,D.F., Sutherland,G.R.
            and Maliszewski,C.R.
  TITLE     The gene for the human IgA Fc receptor maps to 19q13.4
  JOURNAL   Hum Genet 89 (1), 107-108 (1992)
   PUBMED   1577457
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Maliszewski,C.R., March,C.J., Schoenborn,M.A., Gimpel,S. and
            Shen,L.
  TITLE     Expression cloning of a human Fc receptor for IgA
  JOURNAL   J Exp Med 172 (6), 1665-1672 (1990)
   PUBMED   2258698
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Kimata,H. and Saxon,A.
  TITLE     Subset of natural killer cells is induced by immune complexes to
            display Fc receptors for IgE and IgA and demonstrates isotype
            regulatory function
  JOURNAL   J Clin Invest 82 (1), 160-167 (1988)
   PUBMED   2455732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290922.1, BC027953.1 and
            AC245128.3.
            
            Summary: This gene is a member of the immunoglobulin gene
            superfamily and encodes a receptor for the Fc region of IgA. The
            receptor is a transmembrane glycoprotein present on the surface of
            myeloid lineage cells such as neutrophils, monocytes, macrophages,
            and eosinophils, where it mediates immunologic responses to
            pathogens. It interacts with IgA-opsonized targets and triggers
            several immunologic defense processes, including phagocytosis,
            antibody-dependent cell-mediated cytotoxicity, and stimulation of
            the release of inflammatory mediators. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1, also known as a.1) represents
            the longest transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290922.1, SRR1803617.280490.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355524.8/ ENSP00000347714.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..287
                     /product="immunoglobulin alpha Fc receptor isoform a
                     precursor"
                     /note="immunoglobulin alpha Fc receptor; Fc fragment of
                     IgA, receptor for; Fc fragment of IgA receptor"
                     /calculated_mol_wt=29938
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2345
     mat_peptide     22..287
                     /product="Immunoglobulin alpha Fc receptor.
                     /id=PRO_0000015138"
                     /note="propagated from UniProtKB/Swiss-Prot (P24071.1)"
                     /calculated_mol_wt=29938
     Region          28..119
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,101,108)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P24071.1)"
     Region          72..75
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P24071.1)"
     Region          84..88
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          96..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          112..119
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          125..215
                     /region_name="IgC2_D2_LILR_KIR_like"
                     /note="Second immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors, Natural killer inhibitory
                     receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05711"
                     /db_xref="CDD:409376"
     Region          126..130
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409376"
     Region          134..137
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409376"
     Region          140..147
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409376"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12768205; propagated from
                     UniProtKB/Swiss-Prot (P24071.1)"
     Region          155..160
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409376"
     Region          170..172
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409376"
     Region          177..181
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409376"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12768205; propagated from
                     UniProtKB/Swiss-Prot (P24071.1)"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P24071.1)"
     Region          189..195
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409376"
     Region          208..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409376"
     Site            228..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P24071.1)"
     CDS             1..287
                     /gene="FCAR"
                     /gene_synonym="CD89; CTB-61M7.2; FcalphaR; FcalphaRI"
                     /coded_by="NM_002000.4:56..919"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12907.1"
                     /db_xref="GeneID:2204"
                     /db_xref="HGNC:HGNC:3608"
                     /db_xref="MIM:147045"
ORIGIN      
        1 mdpkqttllc lvlclgqriq aqegdfpmpf isaksspvip ldgsvkiqcq aireayltql
       61 miiknstyre igrrlkfwne tdpefvidhm dankagryqc qyrighyrfr ysdtlelvvt
      121 glygkpflsa drglvlmpge nisltcssah ipfdrfslak egelslpqhq sgehpanfsl
      181 gpvdlnvsgi yrcygwynrs pylwsfpsna lelvvtdsih qdyttqnlir mavaglvlva
      241 llailvenwh shtalnkeas advaepswsq qmcqpgltfa rtpsvck
//
LOCUS       NP_004302                182 aa            linear   PRI 20-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 3 [Homo sapiens].
ACCESSION   NP_004302
VERSION     NP_004302.1
DBSOURCE    REFSEQ: accession NM_004311.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Zhang,X., Yao,S., Zhang,L., Yang,L., Yang,M., Guo,Q., Li,Y.,
            Wang,Z., Lei,B. and Jin,X.
  TITLE     Mechanisms underlying morphological and functional changes of cilia
            in fibroblasts derived from patients bearing ARL3T31A and
            ARL3T31A/C118F mutations
  JOURNAL   FASEB J 38 (5), e23519 (2024)
   PUBMED   38457249
  REMARK    GeneRIF: Mechanisms underlying morphological and functional changes
            of cilia in fibroblasts derived from patients bearing ARL3[T31A]
            and ARL3[T31A/C118F] mutations.
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Travis,A.M. and Pearring,J.N.
  TITLE     Human Mutations in Arl3, a Small GTPase Involved in Lipidated Cargo
            Delivery to the Cilia, Cause Retinal Dystrophy
  JOURNAL   Adv Exp Med Biol 1415, 283-288 (2023)
   PUBMED   37440046
  REMARK    GeneRIF: Human Mutations in Arl3, a Small GTPase Involved in
            Lipidated Cargo Delivery to the Cilia, Cause Retinal Dystrophy.
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Khrenova,M.G., Bulavko,E.S., Mulashkin,F.D. and Nemukhin,A.V.
  TITLE     Mechanism of Guanosine Triphosphate Hydrolysis by the Visual
            Proteins Arl3-RP2: Free Energy Reaction Profiles Computed with Ab
            Initio Type QM/MM Potentials
  JOURNAL   Molecules 26 (13), 3998 (2021)
   PUBMED   34208932
  REMARK    GeneRIF: Mechanism of Guanosine Triphosphate Hydrolysis by the
            Visual Proteins Arl3-RP2: Free Energy Reaction Profiles Computed
            with Ab Initio Type QM/MM Potentials.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Linari,M., Hanzal-Bayer,M. and Becker,J.
  TITLE     The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE
            delta, interacts with the Arf-like protein Arl3 in a GTP specific
            manner
  JOURNAL   FEBS Lett 458 (1), 55-59 (1999)
   PUBMED   10518933
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Kim,H.S.
  TITLE     Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene
            to chromosome 10 band q23.3 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 83 (3-4), 246 (1998)
   PUBMED   10072593
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Cavenagh,M.M., Breiner,M., Schurmann,A., Rosenwald,A.G., Terui,T.,
            Zhang,C., Randazzo,P.A., Adams,M., Joost,H.G. and Kahn,R.A.
  TITLE     ADP-ribosylation factor (ARF)-like 3, a new member of the ARF
            family of GTP-binding proteins cloned from human and rat tissues
  JOURNAL   J Biol Chem 269 (29), 18937-18942 (1994)
   PUBMED   8034651
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL391121.29.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1149522.1,
                                           SRR3476690.185947.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260746.6/ ENSP00000260746.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..182
                     /product="ADP-ribosylation factor-like protein 3"
                     /note="ARF-like 3; ADP ribosylation factor like GTPase 3;
                     ADP-ribosylation factor-like 3"
                     /calculated_mol_wt=20324
     Region          3..176
                     /region_name="Arl3"
                     /note="Arf-like 3 (Arl3) GTPase; cd04155"
                     /db_xref="CDD:206721"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P36405.2)"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206721"
     Site            order(26..27,31,35,47..54,76,81)
                     /site_type="other"
                     /note="putative GAP interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206721"
     Site            order(27..32,126..127,129..130,159..161)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206721"
     Site            36..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206721"
     Site            order(48..52,57,67,71,77,79..81)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206721"
     Site            48
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206721"
     Site            order(49..56,66,77,80..81)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206721"
     Site            order(52..58,61..66)
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206721"
     Site            67..84
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206721"
     Site            67..70
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206721"
     Site            126..129
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206721"
     Site            159..161
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206721"
     CDS             1..182
                     /gene="ARL3"
                     /gene_synonym="ARFL3; JBTS35; RP83"
                     /coded_by="NM_004311.4:123..671"
                     /db_xref="CCDS:CCDS7538.1"
                     /db_xref="GeneID:403"
                     /db_xref="HGNC:HGNC:694"
                     /db_xref="MIM:604695"
ORIGIN      
        1 mgllsilrkl ksapdqevri lllgldnagk ttllkqlase dishitptqg fniksvqsqg
       61 fklnvwdigg qrkirpywkn yfentdiliy vidsadrkrf eetgqelael leeeklscvp
      121 vlifankqdl ltaapaseia eglnlhtird rvwqiqscsa ltgegvqdgm nwvcknvnak
      181 kk
//
LOCUS       NP_001354463             588 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 27 [Homo sapiens].
ACCESSION   NP_001354463 XP_006718056
VERSION     NP_001354463.1
DBSOURCE    REFSEQ: accession NM_001367534.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 5, 2018 this sequence version replaced XP_006718056.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.779364.1,
                                           SRR1803611.17573.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000423381.6/ ENSP00000410298.3
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..588
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 27"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=65111
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          456..583
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..588
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367534.1:95..1861"
                     /note="isoform 27 is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS91269.1"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lvspaqepap lqtamepqtt vvhnatdgik gstescnttt ededlkaapl
      421 rtgngssvpe grssrdrtap sagmqpqpsl cssamrkqei ikiteqliea inngdfeayt
      481 kicdpgltsf epealgnlve gmdfhkfyfe nllsknskpi httilnphvh vigedaacia
      541 yirltqyidg qgrprtsqse etrvwhrrdg kwlnvhyhcs gapaaplq
//
LOCUS       NP_078862                736 aa            linear   PRI 20-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform e [Homo
            sapiens].
ACCESSION   NP_078862
VERSION     NP_078862.4
DBSOURCE    REFSEQ: accession NM_024586.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 736)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB081133.1, AF392445.1,
            AL050343.17 and EL953716.1.
            
            On Oct 5, 2010 this sequence version replaced NP_078862.3.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and 5'
            coding region, uses an alternate start codon, and includes an
            additional in-frame exon in its central coding region, compared to
            variant 1. The encoded isoform (e) has a longer and distinct
            N-terminus, and contains an additional internal segment, compared
            to isoform a. Isoform e contains both a pleckstrin homology domain
            and a sterol-binding domain.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. This
            transcript contains a uAUG that would result in an 18 aa N-terminal
            extension, but it has a weak Kozak signal, is not supported by the
            vast majority of human and homologous transcripts, and dAUG use is
            supported by data in PMID:19413330, which selectively purifies
            acetylated protein N-termini and shows that Ala-2 is acetylated
            following cleavage of Met-1 as encoded by the dAUG.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.19453.1,
                                           SRR1660805.123569.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:19413330)
            MANE Ensembl match               :: ENST00000428468.6/
                                                ENSP00000407168.1
            RefSeq Select criteria           :: based on conservation,
                                                expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..736
                     /product="oxysterol-binding protein-related protein 9
                     isoform e"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=83054
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Region          5..106
                     /region_name="PH_ORP9"
                     /note="Human Oxysterol binding protein related protein 9
                     Pleckstrin homology (PH) domain; cd13290"
                     /db_xref="CDD:241444"
     Region          231..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96SU4.2)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     Region          377..723
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96SU4.2)"
     CDS             1..736
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_024586.6:20..2230"
                     /note="isoform e is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS41332.3"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 masimegpls kwtnvmkgwq yrwfvldyna gllsyytskd kmmrgsrrgc vrlrgavigi
       61 ddeddstfti tvdqktfhfq ardaderekw ihaleetilr htlqlqglds gfvpsvqdfd
      121 kklteadayl qilieqlklf ddklqncked eqrkkietlk ettnsmvesi khcivllqia
      181 kdqsnaekha dgmistinpv daiyqpsple pvistmpsqt vlppepvqlc kseqrpsslp
      241 vgpvlatlgh hqtptpnstg sghsppsssl tspshvnlsp ntvpefsyss sedefydade
      301 fhqsgsspkr lidssgsasv lthsssgnsl krpdttesln sslsngtsda dlfdshddrd
      361 ddaeagsvee hksvimhlls qvrlgmdltk vvlptfiler rsllemyadf fahpdlfvsi
      421 sdqkdpkdrm vqvvkwylsa fhagrkgsva kkpynpilge ifqchwtlpn dteentelvs
      481 egpvpwvskn svtfvaeqvs hhppisafya ecfnkkiqfn ahiwtkskfl gmsigvhnig
      541 qgcvscldyd ehyiltfpng ygrsiltvpw velggecnin csktgysani ifhtkpfygg
      601 kkhritaeif spndkksfcs iegewngvmy akyatgentv fvdtkklpii kkkvrkledq
      661 neyesrslwk dvtfnlkird idaateakhr leerqraear erkekeiqwe trlfhedgec
      721 wvydepllkr lgaakh
//
LOCUS       NP_001308501             512 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 12 [Homo sapiens].
ACCESSION   NP_001308501
VERSION     NP_001308501.1
DBSOURCE    REFSEQ: accession NM_001321572.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 512)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (13) encodes isoform (12, also
            known as delta 5).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.39686.1,
                                           SRR1660803.193350.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..512
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 12"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57618
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          380..507
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..512
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321572.2:671..2209"
                     /note="isoform 12 is encoded by transcript variant 13"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpalep qttvihnpdg
      361 nkestessnt tiededvkar kqeiikvteq lieainngdf eaytkicdpg ltafepealg
      421 nlvegmdfhr fyfenalsks nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt
      481 mqseetrvwh rrdgkwqnvh fhrsgsptvp in
//
LOCUS       NP_076424                314 aa            linear   PRI 20-NOV-2025
DEFINITION  DDRGK domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_076424
VERSION     NP_076424.1
DBSOURCE    REFSEQ: accession NM_023935.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Makhlouf,L., Peter,J.J., Magnussen,H.M., Thakur,R., Millrine,D.,
            Minshull,T.C., Harrison,G., Varghese,J., Lamoliatte,F.,
            Foglizzo,M., Macartney,T., Calabrese,A.N., Zeqiraj,E. and
            Kulathu,Y.
  TITLE     The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER
            translocons
  JOURNAL   Nature 627 (8003), 437-444 (2024)
   PUBMED   38383789
REFERENCE   3  (residues 1 to 314)
  AUTHORS   DaRosa,P.A., Penchev,I., Gumbin,S.C., Scavone,F., Wachalska,M.,
            Paulo,J.A., Ordureau,A., Peter,J.J., Kulathu,Y., Harper,J.W.,
            Becker,T., Beckmann,R. and Kopito,R.R.
  TITLE     UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from
            the ER
  JOURNAL   Nature 627 (8003), 445-452 (2024)
   PUBMED   38383785
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Luo,H., Jiao,Q.B., Shen,C.B., Gong,W.Y., Yuan,J.H., Liu,Y.Y.,
            Chen,Z., Liu,J., Xu,X.L., Cong,Y.S. and Zhang,X.W.
  TITLE     UFMylation of HRD1 regulates endoplasmic reticulum homeostasis
  JOURNAL   FASEB J 37 (11), e23221 (2023)
   PUBMED   37795761
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Ishimura,R., Ito,S., Mao,G., Komatsu-Hirota,S., Inada,T., Noda,N.N.
            and Komatsu,M.
  TITLE     Mechanistic insights into the roles of the UFM1 E3 ligase complex
            in ufmylation and ribosome-associated protein quality control
  JOURNAL   Sci Adv 9 (33), eadh3635 (2023)
   PUBMED   37595036
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Ochi,H., Maekawa,T., Abe,H., Hayashida,Y., Nakano,R., Kubo,M.,
            Tsunoda,T., Hayes,C.N., Kumada,H., Nakamura,Y. and Chayama,K.
  TITLE     ITPA polymorphism affects ribavirin-induced anemia and outcomes of
            therapy--a genome-wide study of Japanese HCV virus patients
  JOURNAL   Gastroenterology 139 (4), 1190-1197 (2010)
   PUBMED   20637204
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Wu,J., Lei,G., Mei,M., Tang,Y. and Li,H.
  TITLE     A novel C53/LZAP-interacting protein regulates stability of
            C53/LZAP and DDRGK domain-containing Protein 1 (DDRGK1) and
            modulates NF-kappaB signaling
  JOURNAL   J Biol Chem 285 (20), 15126-15136 (2010)
   PUBMED   20228063
  REMARK    GeneRIF: found that C53/LZAP and DDRGK1 became more susceptible to
            the proteasome-mediated degradation in RCAD knockdown cells,
            whereas their ubiquitination was significantly attenuated by RCAD
            overexpression
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Neziri,D., Ilhan,A., Maj,M., Majdic,O., Baumgartner-Parzer,S.,
            Cohen,G., Base,W. and Wagner,L.
  TITLE     Cloning and molecular characterization of Dashurin encoded by
            C20orf116, a PCI-domain containing protein
  JOURNAL   Biochim Biophys Acta 1800 (4), 430-438 (2010)
   PUBMED   20036718
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Tatsumi,K., Sou,Y.S., Tada,N., Nakamura,E., Iemura,S., Natsume,T.,
            Kang,S.H., Chung,C.H., Kasahara,M., Kominami,E., Yamamoto,M.,
            Tanaka,K. and Komatsu,M.
  TITLE     A novel type of E3 ligase for the Ufm1 conjugation system
  JOURNAL   J Biol Chem 285 (8), 5417-5427 (2010)
   PUBMED   20018847
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Shirabe,K., Yubisui,T., Borgese,N., Tang,C.Y., Hultquist,D.E. and
            Takeshita,M.
  TITLE     Enzymatic instability of NADH-cytochrome b5 reductase as a cause of
            hereditary methemoglobinemia type I (red cell type)
  JOURNAL   J Biol Chem 267 (28), 20416-20421 (1992)
   PUBMED   1400360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY128886.1, BC000643.1 and
            CB305409.1.
            
            Summary: The protein encoded by this gene interacts with components
            of the ubiquitin fold modifier 1 conjugation pathway and helps
            prevent apoptosis in ER-stressed secretory tissues. In addition,
            the encoded protein regulates nuclear factor-&#954;B activity.
            [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.5657.1,
                                           SRR1660803.217942.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354488.8/ ENSP00000346483.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..314
                     /product="DDRGK domain-containing protein 1"
                     /note="UFM1-binding protein 1 containing a PCI domain;
                     Dashurin; UFM1-binding and PCI domain-containing protein
                     1"
                     /calculated_mol_wt=35480
     Region          115..302
                     /region_name="DDRGK"
                     /note="DDRGK domain; pfam09756"
                     /db_xref="CDD:370664"
     CDS             1..314
                     /gene="DDRGK1"
                     /gene_synonym="C20orf116; dJ1187M17.3; SEMDSH; UFBP1"
                     /coded_by="NM_023935.3:56..1000"
                     /db_xref="CCDS:CCDS13050.1"
                     /db_xref="GeneID:65992"
                     /db_xref="HGNC:HGNC:16110"
                     /db_xref="MIM:616177"
ORIGIN      
        1 mvapvwylva aallvgfilf ltrsrgraas agqeplhnee lagagrvaqp gplepeepra
       61 ggrprrrrdl gsrlqaqrra qrvawaeade neeeavilaq eeegvekpae thlsgkigak
      121 klrkleekqa rkaqreaeea ereerkrles qreaewkkee erlrleeeqk eeeerkaree
      181 qaqreheeyl klkeafvvee egvgetmtee qsqsfltefi nyikqskvvl ledlasqvgl
      241 rtqdtinriq dllaegtitg viddrgkfiy itpeelaava nfirqrgrvs iaelaqasns
      301 liawgrespa qapa
//
LOCUS       NP_001341023             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341023 XP_016879191
VERSION     NP_001341023.1
DBSOURCE    REFSEQ: accession NM_001354094.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 4, 2017 this sequence version replaced XP_016879191.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.432486.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354094.2:374..1138"
                     /note="isoform a is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001356032             320 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001356032
VERSION     NP_001356032.1
DBSOURCE    REFSEQ: accession NM_001369103.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.226673.1,
                                           SRR1803612.228129.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..320
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 11"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36568
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..281
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..320
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369103.1:104..1066"
                     /note="isoform 11 is encoded by transcript variant 24"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefikl qelvdrvler fqasglivke wnsvklhatv
      241 mntlfrkdpn aegrynlyta egkyifkere sfdgrnilks fallprleyn daisahcnlc
      301 lpgssdspas asqvagitvv
//
LOCUS       NP_056975                579 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-processing factor 17 [Homo sapiens].
ACCESSION   NP_056975
VERSION     NP_056975.1
DBSOURCE    REFSEQ: accession NM_015891.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Chai,G., Webb,A., Li,C., Antaki,D., Lee,S., Breuss,M.W., Lang,N.,
            Stanley,V., Anzenberg,P., Yang,X., Marshall,T., Gaffney,P.,
            Wierenga,K.J., Chung,B.H., Tsang,M.H., Pais,L.S., Lovgren,A.K.,
            VanNoy,G.E., Rehm,H.L., Mirzaa,G., Leon,E., Diaz,J., Neumann,A.,
            Kalverda,A.P., Manfield,I.W., Parry,D.A., Logan,C.V., Johnson,C.A.,
            Bonthron,D.T., Valleley,E.M.A., Issa,M.Y., Abdel-Ghafar,S.F.,
            Abdel-Hamid,M.S., Jennings,P., Zaki,M.S., Sheridan,E. and
            Gleeson,J.G.
  TITLE     Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause
            Neurodegenerative Pontocerebellar Hypoplasia with Microcephaly
  JOURNAL   Neuron 109 (2), 241-256 (2021)
   PUBMED   33220177
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Zhang,X., Zhan,X., Yan,C., Zhang,W., Liu,D., Lei,J. and Shi,Y.
  TITLE     Structures of the human spliceosomes before and after release of
            the ligated exon
  JOURNAL   Cell Res 29 (4), 274-285 (2019)
   PUBMED   30728453
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Lindsey,L.A. and Garcia-Blanco,M.A.
  TITLE     Functional conservation of the human homolog of the yeast pre-mRNA
            splicing factor Prp17p
  JOURNAL   J Biol Chem 273 (49), 32771-32775 (1998)
   PUBMED   9830021
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Ben Yehuda,S., Dix,I., Russell,C.S., Levy,S., Beggs,J.D. and
            Kupiec,M.
  TITLE     Identification and functional analysis of hPRP17, the human
            homologue of the PRP17/CDC40 yeast gene involved in splicing and
            cell cycle control
  JOURNAL   RNA 4 (10), 1304-1312 (1998)
   PUBMED   9769104
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Zhou,Z. and Reed,R.
  TITLE     Human homologs of yeast prp16 and prp17 reveal conservation of the
            mechanism for catalytic step II of pre-mRNA splicing
  JOURNAL   EMBO J 17 (7), 2095-2106 (1998)
   PUBMED   9524131
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Salcini,A.E., Confalonieri,S., Doria,M., Santolini,E., Tassi,E.,
            Minenkova,O., Cesareni,G., Pelicci,P.G. and Di Fiore,P.P.
  TITLE     Binding specificity and in vivo targets of the EH domain, a novel
            protein-protein interaction module
  JOURNAL   Genes Dev 11 (17), 2239-2249 (1997)
   PUBMED   9303539
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Wong,W.T., Schumacher,C., Salcini,A.E., Romano,A., Castagnino,P.,
            Pelicci,P.G. and Di Fiore,P.P.
  TITLE     A protein-binding domain, EH, identified in the receptor tyrosine
            kinase substrate Eps15 and conserved in evolution
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9530-9534 (1995)
   PUBMED   7568168
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF038392.1, AK001426.1,
            CB242479.1 and AL671518.3.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is
            found to be essential for the catalytic step II in pre-mRNA
            splicing process. It is found in the spliceosome, and contains
            seven WD repeats, which function in protein-protein interactions.
            This protein has a sequence similarity to yeast Prp17 protein,
            which functions in two different cellular processes: pre-mRNA
            splicing and cell cycle progression. It suggests that this protein
            may play a role in cell cycle progression. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.242774.1,
                                           SRR1660809.250792.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307731.2/ ENSP00000304370.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..579
                     /product="pre-mRNA-processing factor 17"
                     /note="pre-mRNA splicing factor 17; EH-binding protein 3;
                     hPRP17; PRP17 homolog; cell division cycle 40 homolog"
                     /calculated_mol_wt=65390
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60508.1)"
     Region          204..237
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          281..579
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          286..326
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Site            order(287,306,310,316..317,330..331,349,353,359..360,372,
                     392,397,403..404,417,435,439,445..446,461..462,478,482,
                     488..489,504..505,524,529,535..536,548..549,568,572,
                     578..579)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          292..330
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..369
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          335..371
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          371..413
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          377..415
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          416..455
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          421..503
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          459..498
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          504..545
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          511..547
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          548..578
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O60508.1)"
     Region          553..578
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..579
                     /gene="CDC40"
                     /gene_synonym="EHB3; PCH15; PRP17; PRPF17"
                     /coded_by="NM_015891.3:19..1758"
                     /db_xref="CCDS:CCDS5081.1"
                     /db_xref="GeneID:51362"
                     /db_xref="HGNC:HGNC:17350"
                     /db_xref="MIM:605585"
ORIGIN      
        1 msaaiaalaa sygsgsgses dsdsessrcp lpaadslmhl tkspsskpsl avavdsapev
       61 avkedletgv hldpavkevq ynptyetmfa pefgpenpfr tqqmaaprnm lsgyaepahi
      121 ndfmfeqqrr tfatygyald psldnhqvsa kyigsveeae knqgltvfet gqkktekrkk
      181 fkendasnid gflgpwakyv dekdvakpse eeqkeldeit akrqkkgkqe eekpgeekti
      241 lhvkemydyq grsylhipqd vgvnlrstmp pekcylpkkq ihvwsghtkg vsavrlfpls
      301 ghlllscsmd ckiklwevyg errclrtfig hskavrdicf ntagtqflsa aydrylklwd
      361 tetgqcisrf tnrkvpycvk fnpdedkqnl fvagmsdkki vqwdirsgei vqeydrhlga
      421 vntivfvden rrfvstsddk slrvwewdip vdfkyiaeps mhsmpavtls pngkwlacqs
      481 mdnqilifga qnrfrlnkkk ifkghmvagy acqvdfspdm syvisgdgng klniwdwktt
      541 klysrfkahd kvcigavwhp hetskvitcg wdgliklwd
//
LOCUS       NP_002781                241 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-5 isoform 1 [Homo sapiens].
ACCESSION   NP_002781
VERSION     NP_002781.2
DBSOURCE    REFSEQ: accession NM_002790.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 241)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 241)
  AUTHORS   Xie,S., Li,X., Yan,J., Yu,H., Chen,S. and Chen,K.
  TITLE     Knockdown of liver cancer cell-secreted exosomal PSMA5 controls
            macrophage polarization to restrain cancer progression by blocking
            JAK2/STAT3 signaling
  JOURNAL   Immun Inflamm Dis 12 (2), e1146 (2024)
   PUBMED   38415977
  REMARK    GeneRIF: Knockdown of liver cancer cell-secreted exosomal PSMA5
            controls macrophage polarization to restrain cancer progression by
            blocking JAK2/STAT3 signaling.
REFERENCE   3  (residues 1 to 241)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 241)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 241)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 241)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   7  (residues 1 to 241)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   8  (residues 1 to 241)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   9  (residues 1 to 241)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 241)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313351.1, AK225990.1,
            AL390252.9 and H08369.1.
            
            On Sep 18, 2002 this sequence version replaced NP_002781.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. Multiple alternatively spliced transcript variants
            encoding two distinct isoforms have been found for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) is the predominant transcript
            and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2400113.1,
                                           SRR11853562.1578.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000271308.9/ ENSP00000271308.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..241
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..241
                     /product="proteasome subunit alpha type-5 isoform 1"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit zeta; proteasome subunit zeta;
                     proteasome zeta chain; macropain zeta chain;
                     multicatalytic endopeptidase complex zeta chain;
                     proteasome component 5; proteasome subunit alpha type-5;
                     proteasome alpha 5 subunit; alpha-5; proteasome (prosome,
                     macropain) subunit, alpha type, 5; epididymis tissue sperm
                     binding protein Li 11n; proteasome subunit alpha 5"
                     /calculated_mol_wt=26280
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2U1; propagated from
                     UniProtKB/Swiss-Prot (P28066.3)"
     Region          8..220
                     /region_name="proteasome_alpha_type_5"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03753"
                     /db_xref="CDD:239722"
     Site            order(10..13,15..16,18..19,23,26,29..30,33,41,56,58..59,
                     82..84,86..87,118,121,124..125,133..137,154,159..160,162,
                     164..165,167)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239722"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28066.3)"
     Site            order(35,51,53,66,172)
                     /site_type="active"
                     /db_xref="CDD:239722"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P28066.3)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28066.3)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28066.3)"
     Site            198
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P28066.3)"
     CDS             1..241
                     /gene="PSMA5"
                     /gene_synonym="PSC5; ZETA"
                     /coded_by="NM_002790.4:119..844"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS799.1"
                     /db_xref="GeneID:5686"
                     /db_xref="HGNC:HGNC:9534"
                     /db_xref="MIM:176844"
ORIGIN      
        1 mfltrseydr gvntfspegr lfqveyaiea iklgstaigi qtsegvclav ekritsplme
       61 pssiekivei dahigcamsg liadaktlid karvetqnhw ftynetmtve svtqavsnla
      121 lqfgeedadp gamsrpfgva llfggvdekg pqlfhmdpsg tfvqcdarai gsasegaqss
      181 lqevyhksmt lkeaikssli ilkqvmeekl natnielatv qpgqnfhmft keeleevikd
      241 i
//
LOCUS       NP_001341826            2853 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform d [Homo sapiens].
ACCESSION   NP_001341826
VERSION     NP_001341826.1
DBSOURCE    REFSEQ: accession NM_001354897.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2853)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2853)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2853)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2853)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2853)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2853)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2853)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2853)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2853)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2853)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: LC085428.1, SRR1660807.253264.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2853
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2853
                     /product="adenomatous polyposis coli protein isoform d"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=311963
     Region          137..217
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          350..402
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          403..476
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          475..518
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(509,513,517,552,556,560,596,600,604)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          522..563
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          526..563
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          570..605
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          613..654
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          659..699
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          663..697
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          701..741
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          705..741
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          742..1029
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          1046..1145
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1267..>1284
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1293..1378
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1301..1711
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1647..1670
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1672..1725
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1726..1747
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1756..1849
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1883..1957
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          2043..2062
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2233..2578
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2680..2853
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2853
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354897.2:221..8782"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 myaslgsgpv aplpasvpps vlgswstggs rscvrqetks pggartsghw asvwqevlkq
       61 lqgsiedeam assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec
      121 spvpmgsfpr rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid
      181 slpltenfsl qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr
      241 irqllqsqat eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas
      301 vlssssthsa prrltshlgt kvemvyslls mlgthdkddm srtllamsss qdscismrqs
      361 gclplliqll hgndkdsvll gnsrgskear arasaalhni ihsqpddkrg rreirvlhll
      421 eqiraycetc wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde ehrhamnelg
      481 glqaiaellq vdcemygltn dhysitlrry agmaltnltf gdvankatlc smkgcmralv
      541 aqlksesedl qqviasvlrn lswradvnsk ktlrevgsvk almecalevk kestlksvls
      601 alwnlsahct enkadicavd galaflvgtl tyrsqtntla iiesgggilr nvssliatne
      661 dhrqilrenn clqtllqhlk shsltivsna cgtlwnlsar npkdqealwd mgavsmlknl
      721 ihskhkmiam gsaaalrnlm anrpakykda nimspgsslp slhvrkqkal eaeldaqhls
      781 etfdnidnls pkashrskqr hkqslygdyv fdtnrhddnr sdnfntgnmt vlspylnttv
      841 lpsssssrgs ldssrsekdr slerergigl gnyhpatenp gtsskrglqi sttaaqiakv
      901 meevsaihts qedrssgstt elhcvtdern alrrssaaht hsntynftks ensnrtcsmp
      961 yakleykrss ndslnsvsss dgygkrgqmk psiesysedd eskfcsygqy padlahkihs
     1021 anhmddndge ldtpinyslk ysdeqlnsgr qspsqnerwa rpkhiiedei kqseqrqsrn
     1081 qsttypvyte stddkhlkfq phfgqqecvs pyrsrgangs etnrvgsnhg inqnvsqslc
     1141 qeddyeddkp tnyserysee eqheeeerpt nysikyneek rhvdqpidys lkyatdipss
     1201 qkqsfsfsks ssgqsskteh mssssentst pssnakrqnq lhpssaqsrs gqpqkaatck
     1261 vssinqetiq tycvedtpic fsrcsslssl ssaedeigcn qttqeadsan tlqiaeikek
     1321 igtrsaedpv sevpavsqhp rtkssrlqgs slssesarhk avefssgaks psksgaqtpk
     1381 sppehyvqet plmfsrctsv ssldsfesrs iassvqsepc sgmvsgiisp sdlpdspgqt
     1441 mppsrsktpp pppqtaqtkr evpknkapta ekresgpkqa avnaavqrvq vlpdadtllh
     1501 fatestpdgf scssslsals ldepfiqkdv elrimppvqe ndngnetese qpkesnenqe
     1561 keaektidse kdllddsddd dieileecii samptkssrk akkpaqtask lpppvarkps
     1621 qlpvykllps qnrlqpqkhv sftpgddmpr vycvegtpin fstatslsdl tiesppnela
     1681 agegvrggaq sgefekrdti ptegrstdea qggktssvti pelddnkaee gdilaecins
     1741 ampkgkshkp frvkkimdqv qqasasssap nknqldgkkk kptspvkpip qnteyrtrvr
     1801 knadsknnln aervfsdnkd skkqnlknns kvfndklpnn edrvrgsfaf dsphhytpie
     1861 gtpycfsrnd slssldfddd dvdlsrekae lrkakenkes eakvtshtel tsnqqsankt
     1921 qaiakqpinr gqpkpilqkq stfpqsskdi pdrgaatdek lqnfaientp vcfshnssls
     1981 slsdidqenn nkenepiket eppdsqgeps kpqasgyapk sfhvedtpvc fsrnsslssl
     2041 sidseddllq ecissampkk kkpsrlkgdn ekhsprnmgg ilgedltldl kdiqrpdseh
     2101 glspdsenfd wkaiqegans ivsslhqaaa aaclsrqass dsdsilslks gislgspfhl
     2161 tpdqeekpft snkgprilkp gekstletkk ieseskgikg gkkvykslit gkvrsnseis
     2221 gqmkqplqan mpsisrgrtm ihipgvrnss sstspvskkg pplktpasks psegqtatts
     2281 prgakpsvks elspvarqts qiggsskaps rsgsrdstps rpaqqplsrp iqspgrnsis
     2341 pgrngisppn klsqlprtss pstastkssg sgkmsytspg rqmsqqnltk qtglsknass
     2401 iprsesaskg lnqmnngnga nkkvelsrms stkssgsesd rserpvlvrq stfikeapsp
     2461 tlrrkleesa sfeslspssr pasptrsqaq tpvlspslpd mslsthssvq aggwrklppn
     2521 lsptieyndg rpakrhdiar shsespsrlp inrsgtwkre hskhssslpr vstwrrtgss
     2581 ssilsasses sekaksedek hvnsisgtkq skenqvsakg twrkikenef sptnstsqtv
     2641 ssgatngaes ktliyqmapa vsktedvwvr iedcpinnpr sgrsptgntp pvidsvseka
     2701 npnikdskdn qakqnvgngs vpmrtvglen rlnsfiqvda pdqkgteikp gqnnpvpvse
     2761 tnessivert pfsssssskh sspsgtvaar vtpfnynpsp rkssadstsa rpsqiptpvn
     2821 nntkkrdskt dstessgtqs pkrhsgsylv tsv
//
LOCUS       NP_001186180             527 aa            linear   PRI 20-NOV-2025
DEFINITION  shugoshin 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001186180
VERSION     NP_001186180.1
DBSOURCE    REFSEQ: accession NM_001199251.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 527)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 527)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 527)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK308095.1, AB190994.1,
            AF308299.1, BC032696.1, BX648516.1 and AC099057.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and A1 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB190994.1, SRR9304714.96190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267758, SAMN03267770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412997.6/ ENSP00000410458.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..527
                     /product="shugoshin 1 isoform 1"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=59991
     Region          1..176
                     /region_name="Necessary for interaction with PPP2CA and
                     PPP2R1A. /evidence=ECO:0000269|PubMed:16580887"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          192..200
                     /region_name="D-box 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          260..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          310..312
                     /region_name="KEN box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          348..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          438..446
                     /region_name="D-box 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          451..455
                     /region_name="PXVXL/I motif.
                     /evidence=ECO:0000305|PubMed:21346195"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          457..465
                     /region_name="D-box 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          474..495
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     CDS             1..527
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001199251.3:267..1850"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46773.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqiedq iptipqdtlg vdfdsgeaks
      181 tdnvlprtvs vrsslkkhcn sicqfdsldd fetshlagks fefervgfld plvnmhipen
      241 vqhnacqwsk dqvnlspkli qpgtftktke dileskseqt kskqrdtqer kreekrkanr
      301 rkskrmskyk enksenkktv pqkkmhksvs sndaynfnle egvhltpfrq kvsndsnree
      361 nnesevslce ssgsgddsdd lylptckyiq nptsnsdrpv trplakralk ytdeketegs
      421 kptktptttp petqqsphls lkditnvsly pvvkirrlsl spkknkaspa valpkrrcta
      481 svnykeptla sklrrgdpft dlcflnspif kqkkdlrrsk ksmkqiq
//
LOCUS       NP_001293136             643 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform m [Homo sapiens].
ACCESSION   NP_001293136 XP_005266803
VERSION     NP_001293136.1
DBSOURCE    REFSEQ: accession NM_001306207.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 643)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 643)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 643)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 643)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 643)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 643)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 643)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 643)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 643)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 643)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP293388.1, AK301144.1 and
            AC091103.4.
            
            On Apr 16, 2015 this sequence version replaced XP_005266803.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (13) differs in the 5' UTR and
            coding sequence, and uses an alternate in-frame splice site in the
            3' coding region, compared to variant 3. The encoded isoform (m)
            has a shorter N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301144.1, SRR1660807.106999.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..643
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..643
                     /product="transcription factor 4 isoform m"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68480
     Region          534..618
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(542,546,548..550,552,557,578..579)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(555..556,559..560,562..563,566,570,580,583,587,590,
                     593..598)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..643
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001306207.1:310..2241"
                     /note="isoform m is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS77192.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsagtavwsr nggqassspn yegplhslqs
      361 riedrlerld daihvlrnha vgpstampgg hgdmhgiigp shngamgglg sgygtgllsa
      421 nrhslmvgth redgvalrgs hsllpnqvpv pqlpvqsats pdlnppqdpy rgmppglqgq
      481 svssgsseik sddegdenlq dtkssedkkl dddkkdiksi tsnnddedlt peqkaereke
      541 rrmannarer lrvrdineaf kelgrmvqlh lksdkpqtkl lilhqavavi lsleqqvrer
      601 nlnpkaaclk rreeekvsse ppplslagph pgmgdasnhm gqm
//
LOCUS       NP_001352705             281 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform Tpm1.10br [Homo sapiens].
ACCESSION   NP_001352705 XP_005254702
VERSION     NP_001352705.1
DBSOURCE    REFSEQ: accession NM_001365776.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11.
            
            On Sep 12, 2018 this sequence version replaced XP_005254702.3.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.114741.1,
                                           SRR1660807.43259.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..281
                     /product="tropomyosin alpha-1 chain isoform Tpm1.10br"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32383
     Region          48..280
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..281
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365776.1:84..929"
                     /note="isoform Tpm1.10br is encoded by transcript variant
                     TmBr1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledql yqqleqnrrl tnelklalne d
//
LOCUS       NP_001291870            1424 aa            linear   PRI 20-NOV-2025
DEFINITION  G patch domain-containing protein 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001291870
VERSION     NP_001291870.1
DBSOURCE    REFSEQ: accession NM_001304941.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1424)
  AUTHORS   Benbarche,S., Pineda,J.M.B., Galvis,L.B., Biswas,J., Liu,B.,
            Wang,E., Zhang,Q., Hogg,S.J., Lyttle,K., Dahi,A., Lewis,A.M.,
            Sarchi,M., Rahman,J., Fox,N., Ai,Y., Mehta,S., Garippa,R.,
            Ortiz-Pacheco,J., Li,Z., Monetti,M., Stanley,R.F., Doulatov,S.,
            Bradley,R.K. and Abdel-Wahab,O.
  TITLE     GPATCH8 modulates mutant SF3B1 mis-splicing and pathogenicity in
            hematologic malignancies
  JOURNAL   Mol Cell 84 (10), 1886-1903 (2024)
   PUBMED   38688280
  REMARK    GeneRIF: GPATCH8 modulates mutant SF3B1 mis-splicing and
            pathogenicity in hematologic malignancies.
REFERENCE   3  (residues 1 to 1424)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1424)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 1424)
  AUTHORS   Kaneko,H., Kitoh,H., Matsuura,T., Masuda,A., Ito,M., Mottes,M.,
            Rauch,F., Ishiguro,N. and Ohno,K.
  TITLE     Hyperuricemia cosegregating with osteogenesis imperfecta is
            associated with a mutation in GPATCH8
  JOURNAL   Hum Genet 130 (5), 671-683 (2011)
   PUBMED   21594610
  REMARK    GeneRIF: Two missense single-nucleotide variants in ZPBP2 and
            GPATCH8 on chromosome 17 were identified that cosegregated with
            hyperuricemia in the Japanese family.
REFERENCE   6  (residues 1 to 1424)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 1424)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1424)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 1424)
  AUTHORS   Thornton,M.A., Poncz,M., Korostishevsky,M., Yakobson,E., Usher,S.,
            Seligsohn,U. and Peretz,H.
  TITLE     The human platelet alphaIIb gene is not closely linked to its
            integrin partner beta3
  JOURNAL   Blood 94 (6), 2039-2047 (1999)
   PUBMED   10477733
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY048299.1, BC136629.1 and
            BC024147.2.
            
            Summary: The protein encoded by this gene contains an
            RNA-processing domain, a zinc finger domain, a lysine-rich region
            and a serine-rich region. A mutation in the serine-rich region of
            the protein is thought to be associated with hyperuricemia (PMID:
            21594610). Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Feb
            2015].
            
            Transcript Variant: This variant (4) contains an alternate exon in
            the 5' region compared to variant 1. This variant represents
            translation initiation at an in-frame downstream start codon
            compared to variant 1; the 5'-most initiation codon, as used in
            variant 1, is associated with a truncated ORF that would render the
            transcript a candidate for nonsense-mediated decay (NMD). Leaky
            scanning may allow translation initiation at the downstream start
            codon to encode an isoform (3) that has a shorter N-terminus,
            compared to isoform 1. Variants 3, 4, 5 and 6 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144323.1, SRR1803613.16566.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..1424
                     /product="G patch domain-containing protein 8 isoform 3"
                     /note="g patch domain-containing protein 8"
                     /calculated_mol_wt=155063
     Region          <4..>129
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          58..85
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     CDS             1..1424
                     /gene="GPATCH8"
                     /gene_synonym="GPATC8; KIAA0553"
                     /coded_by="NM_001304941.2:289..4563"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:23131"
                     /db_xref="HGNC:HGNC:29066"
                     /db_xref="MIM:614396"
ORIGIN      
        1 mgmgrmemel dyaedaterr rvlevekedt eelrqkykdy vdkekaiaka ledlranfyc
       61 elcdkqyqkh qefdnhinsy dhahkqrlkd lkqrefarnv ssrsrkdekk qekalrrlhe
      121 laeqrkqaec apgsgpmfkp ttvavdeegg eddkdesatn sgtgatascg lgsefstdkg
      181 gpftavqitn ttglaqapgl asqgisfgik nnlgtplqkl gvsfsfakka pvklesiasv
      241 fkdhaeegts edgtkpdeks sdqglqkvgd sdgssnldgk kededpqdgg slastlsklk
      301 rmkreegaga tepeyyhyip pahckvkpnf pfllfmrase qmdgdntthp knapeskkgs
      361 spkpkscika aasqgaektv sevseqpket smtepsepgs kaeakkalgg dvsdqslesh
      421 sqkvsetqmc esnssketsl atpagkesqe gpkhptgpff pvlskdesta lqwpsellif
      481 tkaepsisys cnplyfdfkl srnkdartkg tekpkdigss skdhlqgldp gepnkskevg
      541 gekivrssgg rmdapasgsa csglnkqepg gshgsetedt grslpskker sgkshrhkkk
      601 kkhkksskhk rkhkadteek sskaesgeks kkrkkrkrkk nkssapadse rgpkpeppgs
      661 gspapprrrr raqddsqrrs lpaeegssgk kdeggggsss qdhggrkhkg elppsscqrr
      721 agtkrssrss hrsqpssgde dsddasshrl hqkspsqyse eeeeedsgse hsrsrsrsgr
      781 rhsshrssrr syssssdass dqscysrqrs ysddsysdys drsrrhskrs hdsddsdyas
      841 skhrskrhky sssdddysls csqsrsrsrs htrersrsrg rsrssscsrs rskrrsrstt
      901 ahswqrsrsy srdrsrstrs psqrsgsrkr swghespeer hsgrrdfirs kiyrsqsphy
      961 frsgrgegpg kkddgrgdds katgppsqns nigtgrgseg dcspedknsv taklllekiq
     1021 srkverkpsv seevqatpnk agpklkdppq gyfgpklpps lgnkpvlpli gklpatrkpn
     1081 kkceesgler geeqeqsete egppgssdal fghqfpseet tgplldpppe esksgeatad
     1141 hpvaplgtpa hsdcypgdpt ishnylpdps dgdtleslds ssqpgpvess llpiapdleh
     1201 fpsyappsgd psiestdgae daslaplesq pitftpeeme kysklqqaaq qhiqqqllak
     1261 qvkafpasaa lapatpalqp ihiqqpatas atsittvqha ilqhhaaaaa aaigihphph
     1321 pqplaqvhhi pqphltpisl shlthsiipg hpatflashp ihiipasaih pgpftfhpvp
     1381 haalyptlla prpaaaaata lhlhpllhpi fsgqdlqhpp shgt
//
LOCUS       NP_001338575             931 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            8 [Homo sapiens].
ACCESSION   NP_001338575
VERSION     NP_001338575.1
DBSOURCE    REFSEQ: accession NM_001351646.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 931)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 931)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 931)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 931)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 931)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 931)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 931)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 931)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 931)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 931)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, AL954743.9,
            AL671545.13 and AL096767.14.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.240761.1,
                                           DRR138524.1064149.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..931
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..931
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 8"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=100987
     Region          128..531
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          <675..926
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..931
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001351646.2:372..3167"
                     /note="isoform 8 is encoded by transcript variant 10"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkailtt igvleeplgn arlhgarlma allhtntpsi
      361 nqelcrlntm dllldlffky twnnflhfqv elciaailsh aareerteas gsesrvepph
      421 engnrsletp qpaaslpdnt mvthlfqkcc lvqrileawe andhtqaagg mrrgnmghlt
      481 rianavvqnl ergpvqthis evirglpadc rgrwesfvee tltetnrrnt vdlafsdyqi
      541 qqmtanfvdq fgfndeefad qddninapfd riaeinfnid adedspsaal feaccsdriq
      601 pfdddededi wedsdtrcaa rvmarprfga phasescskn gperggqdgk asleahrdap
      661 gagappapgk keappvegds egamwtavfd epanstptap gvvrdvgssv waagtsapee
      721 kgwakftdfq pfccsesgpr csspvdtecs haegsrsqgp ekafspaspc awnvcvtrka
      781 pllasdssss ggshsedgdq kaasamdavs rgpgreappl ptvarteeav grvgcadsrl
      841 lspacpapke vtaapavavp peatvaitta lskagpaipt pavssalava vplgpimavt
      901 aapamvatlg tvtkdgktda ppegaalngp v
//
LOCUS       NP_003896                534 aa            linear   PRI 20-NOV-2025
DEFINITION  NEDD8-activating enzyme E1 regulatory subunit isoform a [Homo
            sapiens].
ACCESSION   NP_003896
VERSION     NP_003896.1
DBSOURCE    REFSEQ: accession NM_003905.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Muffels,I.J.J., Schene,I.F., Rehmann,H., Massink,M.P.G., van der
            Wal,M.M., Bauder,C., Labeur,M., Armando,N.G., Lequin,M.H.,
            Houben,M.L., Giltay,J.C., Haitjema,S., Huisman,A., Vansenne,F.,
            Bluvstein,J., Pappas,J., Shailee,L.V., Zarate,Y.A., Mokry,M., van
            Haaften,G.W., Nieuwenhuis,E.E.S., Refojo,D., van Wijk,F.,
            Fuchs,S.A. and van Hasselt,P.M.
  TITLE     Bi-allelic variants in NAE1 cause intellectual disability,
            ischiopubic hypoplasia, stress-mediated lymphopenia and
            neurodegeneration
  JOURNAL   Am J Hum Genet 110 (1), 146-160 (2023)
   PUBMED   36608681
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Chen,Y., McPhie,D.L., Hirschberg,J. and Neve,R.L.
  TITLE     The amyloid precursor protein-binding protein APP-BP1 drives the
            cell cycle through the S-M checkpoint and causes apoptosis in
            neurons
  JOURNAL   J Biol Chem 275 (12), 8929-8935 (2000)
   PUBMED   10722740
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Hori,T., Osaka,F., Chiba,T., Miyamoto,C., Okabayashi,K.,
            Shimbara,N., Kato,S. and Tanaka,K.
  TITLE     Covalent modification of all members of human cullin family
            proteins by NEDD8
  JOURNAL   Oncogene 18 (48), 6829-6834 (1999)
   PUBMED   10597293
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Gong,L. and Yeh,E.T.
  TITLE     Identification of the activating and conjugating enzymes of the
            NEDD8 conjugation pathway
  JOURNAL   J Biol Chem 274 (17), 12036-12042 (1999)
   PUBMED   10207026
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Chow,N., Korenberg,J.R., Chen,X.N. and Neve,R.L.
  TITLE     APP-BP1, a novel protein that binds to the carboxyl-terminal region
            of the amyloid precursor protein
  JOURNAL   J Biol Chem 271 (19), 11339-11346 (1996)
   PUBMED   8626687
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM785899.1 and BC000480.2.
            
            Summary: The protein encoded by this gene binds to the beta-amyloid
            precursor protein. Beta-amyloid precursor protein is a cell surface
            protein with signal-transducing properties, and it is thought to
            play a role in the pathogenesis of Alzheimer's disease. In
            addition, the encoded protein can form a heterodimer with UBE1C and
            bind and activate NEDD8, a ubiquitin-like protein. This protein is
            required for cell cycle progression through the S/M checkpoint.
            Three transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.483875.1,
                                           SRR3476690.780082.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290810.8/ ENSP00000290810.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..534
                     /product="NEDD8-activating enzyme E1 regulatory subunit
                     isoform a"
                     /note="amyloid beta precursor protein-binding protein 1,
                     59kD; amyloid beta precursor protein binding protein 1,
                     59kDa; NEDD8-activating enzyme E1 subunit; amyloid
                     protein-binding protein 1; NEDD8-activating enzyme E1
                     regulatory subunit; protooncogene protein 1; APP-BP1;
                     proto-oncogene protein 1; amyloid beta precursor
                     protein-binding protein 1, 59 kDa"
                     /calculated_mol_wt=60115
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13564.1)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13564.1)"
     Region          11..532
                     /region_name="APPBP1_RUB"
                     /note="Ubiquitin activating enzyme (E1) subunit APPBP1.
                     APPBP1 is part of the heterodimeric activating enzyme
                     (E1), specific for the Rub family of ubiquitin-like
                     proteins (Ubls). E1 enzymes are part of a conjugation
                     cascade to attach Ub or Ubls, covalently to...; cd01493"
                     /db_xref="CDD:238770"
     Site            order(11..12,14..20,22,44,47..48,51,67..68,70..72,74,81,
                     92,95..96,158,495,499,503,525)
                     /site_type="other"
                     /note="dimer interaction [polypeptide binding]"
                     /db_xref="CDD:238770"
     Site            211
                     /site_type="other"
                     /note="Interaction with UBA3; propagated from
                     UniProtKB/Swiss-Prot (Q13564.1)"
     Region          331..344
                     /region_name="Interaction with UBA3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13564.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8VBW6; propagated from
                     UniProtKB/Swiss-Prot (Q13564.1)"
     CDS             1..534
                     /gene="NAE1"
                     /gene_synonym="A-116A10.1; APPBP1; HPP1; NEDFIH; ula-1"
                     /coded_by="NM_003905.4:78..1682"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10820.1"
                     /db_xref="GeneID:8883"
                     /db_xref="HGNC:HGNC:621"
                     /db_xref="MIM:603385"
ORIGIN      
        1 maqlgkllke qkydrqlrlw gdhgqeales ahvclinata tgteilknlv lpgigsftii
       61 dgnqvsgeda gnnfflqrss igknraeaam eflqelnsdv sgsfveespe nlldndpsff
      121 crftvvvatq lpestslrla dvlwnsqipl licrtyglvg ymriiikehp vieshpdnal
      181 edlrldkpfp elrehfqsyd ldhmekkdhs htpwiviiak ylaqwysetn gripktykek
      241 edfrdlirqg ilknengape deenfeeaik nvntalnttq ipssiedifn ddrcinitkq
      301 tpsfwilara lkefvakegq gnlpvrgtip dmiadsgkyi klqnvyreka kkdaaavgnh
      361 vakllqsigq apesisekel kllcsnsafl rvvrcrslae eygldtinkd eiissmdnpd
      421 neivlylmlr avdrfhkqqg rypgvsnyqv eedigklksc ltgflqeygl svmvkddyvh
      481 efcrygaaep htiaaflgga aaqevikiit kqfvifnnty iysgmsqtsa tfql
//
LOCUS       NP_055872               4678 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase MYCBP2 [Homo sapiens].
ACCESSION   NP_055872
VERSION     NP_055872.4
DBSOURCE    REFSEQ: accession NM_015057.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4678)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 4678)
  AUTHORS   Chang,C., Banerjee,S.L., Park,S.S., Zhang,X.L., Cotnoir-White,D.,
            Opperman,K.J., Desbois,M., Grill,B. and Kania,A.
  TITLE     Ubiquitin ligase and signalling hub MYCBP2 is required for
            efficient EPHB2 tyrosine kinase receptor function
  JOURNAL   Elife 12, 89176 (2024)
   PUBMED   38289221
  REMARK    GeneRIF: Ubiquitin ligase and signalling hub MYCBP2 is required for
            efficient EPHB2 tyrosine kinase receptor function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 4678)
  AUTHORS   AlAbdi,L., Desbois,M., Rusnac,D.V., Sulaiman,R.A., Rosenfeld,J.A.,
            Lalani,S., Murdock,D.R., Burrage,L.C., Billie Au,P.Y., Towner,S.,
            Wilson,W.G., Wong,L., Brunet,T., Strobl-Wildemann,G., Burton,J.E.,
            Hoganson,G., McWalter,K., Begtrup,A., Zarate,Y.A.,
            Christensen,E.L., Opperman,K.J., Giles,A.C., Helaby,R., Kania,A.,
            Zheng,N., Grill,B. and Alkuraya,F.S.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Loss-of-function variants in MYCBP2 cause neurobehavioural
            phenotypes and corpus callosum defects
  JOURNAL   Brain 146 (4), 1373-1387 (2023)
   PUBMED   36200388
  REMARK    GeneRIF: Loss-of-function variants in MYCBP2 cause neurobehavioural
            phenotypes and corpus callosum defects.
REFERENCE   4  (residues 1 to 4678)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 4678)
  AUTHORS   Wang,G., Miao,C., Mo,L., Kahlert,U.D., Wu,J., Ou,M., Huang,R.,
            Feng,R., Pang,W. and Shi,W.
  TITLE     MYCBP2 expression correlated with inflammatory cell infiltration
            and prognosis immunotherapy in thyroid cancer patients
  JOURNAL   Front Immunol 13, 1048503 (2022)
   PUBMED   36582246
  REMARK    GeneRIF: MYCBP2 expression correlated with inflammatory cell
            infiltration and prognosis immunotherapy in thyroid cancer
            patients.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 4678)
  AUTHORS   Grill,B., Murphey,R.K. and Borgen,M.A.
  TITLE     The PHR proteins: intracellular signaling hubs in neuronal
            development and axon degeneration
  JOURNAL   Neural Dev 11, 8 (2016)
   PUBMED   27008623
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 4678)
  AUTHORS   Pierre,S.C., Hausler,J., Birod,K., Geisslinger,G. and Scholich,K.
  TITLE     PAM mediates sustained inhibition of cAMP signaling by
            sphingosine-1-phosphate
  JOURNAL   EMBO J 23 (15), 3031-3040 (2004)
   PUBMED   15257286
  REMARK    GeneRIF: PAM the longest lasting nontranscriptional regulator of
            adenylyl cyclase activity known to date and presents a novel
            mechanism for the temporal regulation of cAMP signaling
REFERENCE   8  (residues 1 to 4678)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 4678)
  AUTHORS   Murthy,V., Han,S., Beauchamp,R.L., Smith,N., Haddad,L.A., Ito,N.
            and Ramesh,V.
  TITLE     Pam and its ortholog highwire interact with and may negatively
            regulate the TSC1.TSC2 complex
  JOURNAL   J Biol Chem 279 (2), 1351-1358 (2004)
   PUBMED   14559897
  REMARK    GeneRIF: Pam, through its interaction with tuberin, could regulate
            the ubiquitination and proteasomal degradation of the
            tuberin-hamartin complex particularly in the CNS
REFERENCE   10 (residues 1 to 4678)
  AUTHORS   Guo,Q., Xie,J., Dang,C.V., Liu,E.T. and Bishop,J.M.
  TITLE     Identification of a large Myc-binding protein that contains
            RCC1-like repeats
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9172-9177 (1998)
   PUBMED   9689053
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL159158.12, AF075587.1,
            AL159154.16, AL359257.9 and AC001226.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 18, 2010 this sequence version replaced NP_055872.3.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase and
            member of the PHR (Phr1/MYCBP2, highwire and RPM-1) family of
            proteins. The encoded protein plays a role in axon guidance and
            synapse formation in the developing nervous system. In mammalian
            cells, this protein regulates the cAMP and mTOR signaling pathways,
            and may additionally regulate autophagy. Reduced expression of this
            gene has been observed in acute lymphoblastic leukemia patients and
            a mutation in this gene has been identified in patients with a rare
            inherited vision defect. [provided by RefSeq, Mar 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000544440.7/ ENSP00000444596.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..4678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q22.3"
     Protein         1..4678
                     /product="E3 ubiquitin-protein ligase MYCBP2"
                     /EC_number="2.3.2.33"
                     /note="protein associated with Myc; myc-binding protein 2;
                     Highwire; RING-type E3 ubiquitin transferase MYCBP2;
                     PAM/Highwire/RPM-1 protein 1; MYC binding protein 2, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=513508
     Region          87..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          172..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          <534..717
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          600..655
                     /region_name="RCC1 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          609..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          699..755
                     /region_name="RCC1 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          898..928
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          907..957
                     /region_name="RCC1 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          <941..1025
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     Region          958..1008
                     /region_name="RCC1 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          1010..1066
                     /region_name="RCC1 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          1235..1386
                     /region_name="PHR domain 1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          1235..1385
                     /region_name="PHR"
                     /note="PHR domain; pfam08005"
                     /db_xref="CDD:462339"
     Site            1624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          1726..1884
                     /region_name="PHR domain 2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          1726..1883
                     /region_name="PHR"
                     /note="PHR domain; pfam08005"
                     /db_xref="CDD:462339"
     Region          1993..2012
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          2022..2550
                     /region_name="RAE1 binding.
                     /evidence=ECO:0000269|PubMed:22357847"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          2321..2340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          <2394..2445
                     /region_name="IG_FLMN"
                     /note="Filamin-type immunoglobulin domains; smart00557"
                     /db_xref="CDD:214720"
     Region          2477..2539
                     /region_name="SH3_3"
                     /note="Bacterial SH3 domain; pfam08239"
                     /db_xref="CDD:462405"
     Site            2683
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          2709..2931
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            2769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          <2799..3007
                     /region_name="PHA03309"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:165564"
     Site            2833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPH6; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            2920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          2943..2963
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          2979..3020
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            2985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          3066..3085
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            3090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            3478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            3505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          3605..3631
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Region          3748..>3840
                     /region_name="APC10-like"
                     /note="APC10-like DOC1 domains in E3 ubiquitin ligases
                     that mediate substrate ubiquitination; cl02148"
                     /db_xref="CDD:382862"
     Site            order(3768,3798,3805,3807)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:176482"
     Region          3915..3934
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            3921
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPH6; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            3931
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            3932
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Region          4259..4307
                     /region_name="Bbox2_MYCBP2"
                     /note="B-box-type 2 zinc finger found in Myc-binding
                     protein 2 (MYCBP2) and similar proteins; cd19799"
                     /db_xref="CDD:380857"
     Region          4425..4479
                     /region_name="RING-H2_PHR"
                     /note="RING finger, H2 subclass, found in the PHR
                     (Pam/Highwire/RPM-1) protein family; cd16463"
                     /db_xref="CDD:438126"
     Region          4539..4676
                     /region_name="Tandem cysteine domain.
                     /evidence=ECO:0000305|PubMed:29643511"
                     /note="propagated from UniProtKB/Swiss-Prot (O75592.4)"
     Site            4611
                     /site_type="other"
                     /note="Important for catalysis.
                     /evidence=ECO:0000269|PubMed:29643511; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            4616
                     /site_type="other"
                     /note="Important for catalysis.
                     /evidence=ECO:0000269|PubMed:29643511; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     Site            4624
                     /site_type="other"
                     /note="Important for catalysis.
                     /evidence=ECO:0000269|PubMed:29643511; propagated from
                     UniProtKB/Swiss-Prot (O75592.4)"
     CDS             1..4678
                     /gene="MYCBP2"
                     /gene_synonym="Myc-bp2; PAM; Phr; PHR1"
                     /coded_by="NM_015057.5:320..14356"
                     /db_xref="GeneID:23077"
                     /db_xref="HGNC:HGNC:23386"
                     /db_xref="MIM:610392"
ORIGIN      
        1 mmmcaatasp aaassglggd gfypaatfss spapgalfmp vpdgsvaaag lglglpaads
       61 rghyqlllsg raladryrri ytaalndrdq gggsaghpas rnkkilnkkk lkrkqksksk
      121 vktrsksenl entviipdik lhsnpsafni ycnvrhcvle wqkkeislaa asknsvqsge
      181 sdsdeeeesk eppiklpkii evglcevfel iketrfshps lclrslqall nvlqgqqpeg
      241 lqseppevle slfqllleit vrstgmndst gqsltalsca clfslvaswg etgrtlqais
      301 ailtnngsha cqtiqvptil nslqrsvqav lvgkiqiqdw fsngikkaal mhkwplkeis
      361 vdeddqcllq ndgfflyllc kdglykigsg ysgtvrghiy nstsrirnrk ekkswlgyaq
      421 gyllyrdvnn hsmtairisp etleqdgtvm lpdchtegqn ilftdgeyin qiaasrddgf
      481 vvrifatste pvlqqelqlk larkclhacg islfdlekdl hiistgfdee sailgagref
      541 almktangki yytgkyqslg ikqggpsagk wvelpitksp kivhfsvghd gshallvaed
      601 gsifftgsas kgedgestks rrqskpykpk kiikmegkiv vytacnngss sviskdgely
      661 mfgkdaiysd ssslvtdlkg hfvtqvamgk ahtcvlmkng evwtfgvnnk gqcgrdtgam
      721 nqggkgfgve nmatamdedl eeeldekdek smmcppgmhk wkleqcmvct vcgdctgyga
      781 scvssgrpdr vpggicgcgs gesgcavcgc ckacareldg qearqrgild avkemipldl
      841 llavpvpgvn ieehlqlrqe ekrqrvirrh rleegrgplv fagpifmnhr eqalarlrsh
      901 paqlkhkrdk hkdgsgerge kdaskittyp pgsvrfdcel ravqvscgfh hsvvlmengd
      961 vytfgygqhg qlghgdvnsr gcptlvqalp gpstqvtags nhtavllmdg qvftfgsfsk
     1021 gqlgrpildv pywnakpapm pnigskygrk atwigasgdq tflrideali nshvlatsei
     1081 faskhiiglv pasisepppf kcllinkvdg scktfndseq edlqgfgvcl dpvydviwrf
     1141 rpntrelwcy navvadarlp saadmqsrcs ilspelalpt gsralttrsh aalhilgcld
     1201 tlaamqdlkm gvasteeetq avmkvysked ysvvnrfesh gggwgysahs veairfsadt
     1261 dillgglglf ggrgeytaki klfelgpdgg dhetdgdlla etdvlaydca arekyammfd
     1321 epvllqagww yvawarvsgp ssdcgshgqa sittddgvvf qfksskksnn gtdvnagqip
     1381 qllyrlptsd gsaskgkqqt sepvhilkrs fartvsvecf esllsilhws wttlvlgvee
     1441 lrglkgfqft atlldlerlr fvgtcclrll rvytceiypv satgkavvee tsklaecigk
     1501 trtllrkils egvdhcmvkl dndpqgylsq plslleavlq echntftacf hsfyptpalq
     1561 waclcdllnc ldqdiqeanf ktsssrllaa vmsalchtsv kltsifpiay dgevllrsiv
     1621 kqvstendst lvhrfpllva hmeklsqsee nisgmtsfre vlekmlvivv lpvrnslrre
     1681 nelfsshlvs ntcgllasiv seltasalgs evdglnslhs vkasanrftk tsqgrswntg
     1741 ngspdaicfs vdkpgivvvg fsvyggggih eyelevlvdd sehagdsths hrwtslelvk
     1801 gtyttddsps diaeirldkv vplkenvkya vrlrnygsrt angdggmttv qcpdgvtftf
     1861 stcslssngt nqtrgqipqi lyyrsefdgd lqsqllskan eedkncsral svvstvvras
     1921 kdllhralav daddipells ssslfsmllp liiayigpva aaipkvavev fglvqqllps
     1981 vailnqkyap pafnpnqstd sttgnqpeqg lsacttsshy aviesehpyk pacvmhykvt
     2041 fpecvrwmti efdpqcgtaq sedvlrllip vrtvqnsgyg pkltsvhenl nswielkkfs
     2101 gssgwptmvl vlpgnealfs letasdyvkd dkasfygfkc faigyefspg pdegviqlek
     2161 elanlggvca aalmkkdlal pigneleedl eileeaalqv ckthsgilgk glalshspti
     2221 lealegnlpl qiqsneqsfl ddfiacvpgs sggrlarwlq pdsyadpqkt slilnkddir
     2281 cgwpttitvq tkdqygdvvh vpnmkvevka vpvsqkkmsl qqdqakkpqr ipgspavtaa
     2341 ssntdmtygg laspkldvsy epmivkeary iaitmmkvye nysfeelrfa sptpkrpsen
     2401 mlirvnndgt ycanwtpgai glytlhvtid gieidaglev kvkdppkgmi ppgtqlvkpk
     2461 sepqpnkvrk fvakdsaglr irshpslqse qigivkvngt itfideihnd dgvwlrlnde
     2521 tikkyvpnmn gyteawclsf nqhlgksllv pvdesktntd dffkdinscc pqeatmqeqd
     2581 mpflrggpgm ykvvktgpsg hnirscpnlr gipigmlvlg nkvkavgevt nsegtwvqld
     2641 qnsmvefces degeawslar drggnqylrh edeqalldqn sqtpppspfs vqafnkgasc
     2701 saqgfdyglg nskgdrgnis tsskpastsg kselsskhsr slkpdgrmsr ttadqkkprg
     2761 teslsasesl ilksdaaklr sdshsrslsp nhntlqtlks dgrmpsssra espgpgsrls
     2821 spkpktlpan rsspsgassp rsssphdknl pqkstapvkt kldpprersk sdsytldpdt
     2881 lrkkkmplte plrgrstspk pksvpkdstd spgsenraps phvvqenlhs evvevctsst
     2941 lktnsltdst cddssefksv degsnkvhfs igkaplkdeq emraspkisr kcanrhtrpk
     3001 kekssflfkg dgskplepak qamspsvaec aravfasflw hegivhdama cssflkfhpe
     3061 lskehapirs slnsqqptee ketklknrhs leissalnmf niaphgpdis kmgsinknkv
     3121 lsmlkepplh ekcedgktet tfemsmhntm ksksplpltl qhlvafwedi slatikaasq
     3181 nmifpspgsc avlkkkecek enkkskkekk kkekaevrpr gnlfgemaql avggpekdti
     3241 celcgeshpy pvtyhmrqah pgcgryaggq gynsighfcg gwagncgdgg iggstwylvc
     3301 drcrekylre kqaaarekvk qsrrkpmqvk tpralptmea hqvikanalf llslssaaep
     3361 silcyhpakp fqsqlpsvke gisedlpvkm pclylqtlar hhhenfvgyq ddnlfqdemr
     3421 ylrstsvpap yisvtpdasp nvfeepesnm ksmppslets pitdtdlakr tvfqrsysvv
     3481 aseydkqhsi lparvkaipr rrvnsgdtev gssllrhpsp elsrlisahs slskgernfq
     3541 wpvlafviqh hdlegleiam kqalrksacr vfameafnwl lcnviqttsl hdilwhfvas
     3601 ltpapvepee eedeenktsk enseqekdtr vcehplsdiv iageaahplp htfhrllqti
     3661 sdlmmslpsg sslqqmalrc wslkfkqsdh qflhqsnvfh hinnilsksd dgdseesfsi
     3721 siqsgfeams qelcivmclk dltsivdikt ssrpamigsl tdgstetfwe sgdedknktk
     3781 nitincvkgi naryvsvhvd nsrdlgnkvt smtfltgkav edlcrikqvd ldsrhigwvt
     3841 selpggdnhi ikielkgpen tlrvrqvkvl gwkdgestki agqisasvaq qrnceaetlr
     3901 vfrlitsqvf gklisgdaep tpeqeekall sspegeekvy natsdadlke hmvgiifsrs
     3961 kltnlqkqvc ahivqairme atrvreeweh aisskenans qpndedassd aycfellsmv
     4021 lalsgsnvgr qylaqqltll qdlfsllhta sprvqrqvts llrrvlpevt psrlasiigv
     4081 kslppadisd iihstekgdw nklgildmfl gciakaltvq lkakgttitg tagttvgkgv
     4141 ttvtlpmifn ssylrrgesh wwmkgstptq iseiiiklik dmaaghlsea wsrvtknaia
     4201 etiialtkme eefrspvrci attrlwlala slcvldqdhv drlssgrwmg kdgqqkqmpm
     4261 cdnhddgeta aiilcnvcgn lctdcdrflh lhrrtkthqr qvfkeeeeai kvdlhegcgr
     4321 tklfwlmala dsktmkamve frehtgkptt ssseacrfcg srsgtelsav gsvcsdadcq
     4381 eyakiacskt hpcghpcggv kneehclpcl hgcdksatsl kqdaddmcmi cftealsaap
     4441 aiqldcshif hlqccrrvle nrwlgpritf gfiscpickn kinhivlkdl ldpikelyed
     4501 vrrkalmrle yeglhkseai ttpgvrfynd pagyamnrya yyvcykcrka yfggearcda
     4561 eagrgddydp relicgacsd vsraqmcpkh gtdfleykcr yccsvavffc fgtthfcnac
     4621 hddfqrmtsi pkeelphcpa gpkgkqlegt ecplhvvhpp tgeefalgcg vcrnahtf
//
LOCUS       NP_001336350             600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_001336350
VERSION     NP_001336350.1
DBSOURCE    REFSEQ: accession NM_001349421.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (10), as well as variants 7-9 and
            11-15, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.11462.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349421.1:222..2024"
                     /note="isoform b is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001005413             230 aa            linear   PRI 20-NOV-2025
DEFINITION  outer kinetochore KNL1 complex subunit ZWINT isoform b [Homo
            sapiens].
ACCESSION   NP_001005413
VERSION     NP_001005413.1
DBSOURCE    REFSEQ: accession NM_001005413.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Ma,Z., Cai,Y. and Tian,C.
  TITLE     ZWINT promotes the proliferation, migration, and invasion of
            cervical cancer cells by regulating the p53/p21 signaling pathway
  JOURNAL   Chin J Physiol 66 (5), 372-378 (2023)
   PUBMED   37929349
  REMARK    GeneRIF: ZWINT promotes the proliferation, migration, and invasion
            of cervical cancer cells by regulating the p53/p21 signaling
            pathway.
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Nygaard,M., Dowsett,J., McGue,M., Christensen,K., Christiansen,L.,
            Tan,Q. and Mengel-From,J.
  TITLE     Genome-wide association analysis of cognitive function in Danish
            long-lived individuals
  JOURNAL   Mech Ageing Dev 195, 111463 (2021)
   PUBMED   33607172
  REMARK    GeneRIF: Genome-wide association analysis of cognitive function in
            Danish long-lived individuals.
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Wang,H., Hu,X., Ding,X., Dou,Z., Yang,Z., Shaw,A.W., Teng,M.,
            Cleveland,D.W., Goldberg,M.L., Niu,L. and Yao,X.
  TITLE     Human Zwint-1 specifies localization of Zeste White 10 to
            kinetochores and is essential for mitotic checkpoint signaling
  JOURNAL   J Biol Chem 279 (52), 54590-54598 (2004)
   PUBMED   15485811
  REMARK    GeneRIF: show that ZW10 interacting protein-1(Zwint-1) is required
            and is sufficient for kinetochore localization of Zeste White 10
            (ZW10) in HeLa cells
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Obuse,C., Iwasaki,O., Kiyomitsu,T., Goshima,G., Toyoda,Y. and
            Yanagida,M.
  TITLE     A conserved Mis12 centromere complex is linked to heterochromatic
            HP1 and outer kinetochore protein Zwint-1
  JOURNAL   Nat Cell Biol 6 (11), 1135-1141 (2004)
   PUBMED   15502821
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Musio,A., Mariani,T., Montagna,C., Zambroni,D., Ascoli,C., Ried,T.
            and Vezzoni,P.
  TITLE     Recapitulation of the Roberts syndrome cellular phenotype by
            inhibition of INCENP, ZWINT-1 and ZW10 genes
  JOURNAL   Gene 331, 33-40 (2004)
   PUBMED   15094189
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Van Hooser,A.A., Ouspenski,I.I., Gregson,H.C., Starr,D.A.,
            Yen,T.J., Goldberg,M.L., Yokomori,K., Earnshaw,W.C., Sullivan,K.F.
            and Brinkley,B.R.
  TITLE     Specification of kinetochore-forming chromatin by the histone H3
            variant CENP-A
  JOURNAL   J Cell Sci 114 (Pt 19), 3529-3542 (2001)
   PUBMED   11682612
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Starr,D.A., Saffery,R., Li,Z., Simpson,A.E., Choo,K.H., Yen,T.J.
            and Goldberg,M.L.
  TITLE     HZwint-1, a novel human kinetochore component that interacts with
            HZW10
  JOURNAL   J Cell Sci 113 (Pt 11), 1939-1950 (2000)
   PUBMED   10806105
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG615304.1, BM724168.1,
            BC020979.1 and BC016357.2.
            
            Summary: This gene encodes a protein that is clearly involved in
            kinetochore function although an exact role is not known. It
            interacts with ZW10, another kinetochore protein, possibly
            regulating the association between ZW10 and kinetochores. The
            encoded protein localizes to prophase kinetochores before ZW10 does
            and it remains detectable on the kinetochore until late anaphase.
            It has a uniform distribution in the cytoplasm of interphase cells.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            segment compared to variant 1. The resulting isoform (b) has the
            same N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.581548.1,
                                           SRR1163658.199937.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150385, SAMEA2161836
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.1"
     Protein         1..230
                     /product="outer kinetochore KNL1 complex subunit ZWINT
                     isoform b"
                     /note="human ZW10 interacting protein-1; zwint-1; ZW10
                     interactor, kinetochore protein; SNAP25 interacting
                     protein of 30 kDa; outer kinetochore KNL1 complex subunit
                     ZWINT"
                     /calculated_mol_wt=25413
     Region          29..230
                     /region_name="Zwint"
                     /note="ZW10 interactor; pfam15556"
                     /db_xref="CDD:464766"
     CDS             1..230
                     /gene="ZWINT"
                     /gene_synonym="HZwint-1; KNTC2AP; SIP30; ZWINT1"
                     /coded_by="NM_001005413.1:38..730"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS31205.1"
                     /db_xref="GeneID:11130"
                     /db_xref="HGNC:HGNC:13195"
                     /db_xref="MIM:609177"
ORIGIN      
        1 meaaeteaea aalevlaeva gilepvglqe eaelpakilv efvvdsqkkd kllcsqlqva
       61 dflqnilaqe dtakgldpla sedtsrqkai aakeqwkelk atyrehveai kigltkaltq
      121 meeaqrkrtq lreafeqlqa kkqmamekrr avqnqwqlqq ekhlqhlaev saegkllfpe
      181 aeaeaenlpd dkpqqptrpq eqstgdtmgr dpgvsfkavg lqpagdvnlp
//
LOCUS       NP_001288060             105 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC2 isoform
            4 [Homo sapiens].
ACCESSION   NP_001288060
VERSION     NP_001288060.1
DBSOURCE    REFSEQ: accession NM_001301131.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 105)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 105)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 105)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 105)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 105)
  AUTHORS   Pusch,C., Wang,Z., Roe,B. and Blin,N.
  TITLE     Genomic structure of the RNA polymerase II small subunit (hRPB14.4)
            locus (POLRF) and mapping to 22q13.1 by sequence identity
  JOURNAL   Genomics 34 (3), 440-442 (1996)
   PUBMED   8786150
REFERENCE   6  (residues 1 to 105)
  AUTHORS   Acker,J., Wintzerith,M., Vigneron,M. and Kedinger,C.
  TITLE     A 14.4 KDa acidic subunit of human RNA polymerase II with a
            putative leucine-zipper
  JOURNAL   DNA Seq 4 (5), 329-331 (1994)
   PUBMED   7803819
REFERENCE   7  (residues 1 to 105)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   8  (residues 1 to 105)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 105)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 105)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN989996.1 and AK026327.1.
            
            Summary: This gene encodes the sixth largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. In yeast, this polymerase subunit, in
            combination with at least two other subunits, forms a structure
            that stabilizes the transcribing polymerase on the DNA template.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (4) contains an alternate 3' exon
            structure, resulting in a different 3' coding region and 3' UTR,
            compared to variant 1. The encoded isoform (4) has a distinct
            C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1081828.1,
                                           SRR3476690.129483.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..105
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..105
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC2 isoform 4"
                     /EC_number="2.7.7.6"
                     /note="DNA-directed RNA polymerases I, II, and III subunit
                     RPABC2; RNA Polymerase II subunit 14.4 kD; DNA-directed
                     RNA polymerase II subunit F; RNA polymerases I, II, and
                     III subunit ABC2; DNA-directed RNA polymerases I, II, and
                     III 14.4 kDa polypeptide; polymerase (RNA) II (DNA
                     directed) polypeptide F; polymerase (RNA) II subunit F"
                     /calculated_mol_wt=11943
     Region          <26..102
                     /region_name="RNA_pol_Rpb6"
                     /note="RNA polymerase Rpb6; cl14651"
                     /db_xref="CDD:449344"
     CDS             1..105
                     /gene="POLR2F"
                     /gene_synonym="HRBP14.4; POLRF; RPABC14.4; RPABC2;
                     RPB14.4; RPB6; RPC15"
                     /coded_by="NM_001301131.2:90..407"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:5435"
                     /db_xref="HGNC:HGNC:9193"
                     /db_xref="MIM:604414"
ORIGIN      
        1 msdnednfdg ddfddveede glddlenaee egqenveilp sgerpqanqk rittpymtky
       61 erarvlgtra lqiamcapvm velegetdpl liamkelkrr rlree
//
LOCUS       NP_009196                644 aa            linear   PRI 20-NOV-2025
DEFINITION  protein ecdysoneless homolog isoform 1 [Homo sapiens].
ACCESSION   NP_009196 XP_944280
VERSION     NP_009196.1
DBSOURCE    REFSEQ: accession NM_007265.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 644)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 644)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 644)
  AUTHORS   Mohapatra,B.C., Mirza,S., Bele,A., Gurumurthy,C.B., Raza,M.,
            Saleem,I., Storck,M.D., Sarkar,A., Kollala,S.S., Shukla,S.K.,
            Southekal,S., Wagner,K.U., Qiu,F., Lele,S.M., Alsaleem,M.A.,
            Rakha,E.A., Guda,C., Singh,P.K., Cardiff,R.D., Band,H. and Band,V.
  TITLE     Ecdysoneless Overexpression Drives Mammary Tumorigenesis through
            Upregulation of C-MYC and Glucose Metabolism
  JOURNAL   Mol Cancer Res 20 (9), 1391-1404 (2022)
   PUBMED   35675041
  REMARK    GeneRIF: Ecdysoneless Overexpression Drives Mammary Tumorigenesis
            through Upregulation of C-MYC and Glucose Metabolism.
REFERENCE   4  (residues 1 to 644)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 644)
  AUTHORS   Klimesova,K., Vojackova,J., Radivojevic,N., Vandermoere,F.,
            Bertrand,E., Verheggen,C. and Stanek,D.
  TITLE     TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation
  JOURNAL   Nat Commun 12 (1), 3646 (2021)
   PUBMED   34131137
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 644)
  AUTHORS   Zhang,M., Boter,M., Li,K., Kadota,Y., Panaretou,B., Prodromou,C.,
            Shirasu,K. and Pearl,L.H.
  TITLE     Structural and functional coupling of Hsp90- and Sgt1-centred
            multi-protein complexes
  JOURNAL   EMBO J 27 (20), 2789-2798 (2008)
   PUBMED   18818696
REFERENCE   7  (residues 1 to 644)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 644)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 644)
  AUTHORS   Gaziova,I., Bonnette,P.C., Henrich,V.C. and Jindra,M.
  TITLE     Cell-autonomous roles of the ecdysoneless gene in Drosophila
            development and oogenesis
  JOURNAL   Development 131 (11), 2715-2725 (2004)
   PUBMED   15128659
REFERENCE   10 (residues 1 to 644)
  AUTHORS   Sato,T., Jigami,Y., Suzuki,T. and Uemura,H.
  TITLE     A human gene, hSGT1, can substitute for GCR2, which encodes a
            general regulatory factor of glycolytic gene expression in
            Saccharomyces cerevisiae
  JOURNAL   Mol Gen Genet 260 (6), 535-540 (1999)
   PUBMED   9928932
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D88208.1, BC103720.1 and AC016394.13.
            
            On Mar 4, 2006 this sequence version replaced XP_944280.1.
            
            Transcript Variant: This variant (1) represents a more abundant
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1338526.1,
                                           SRR1660803.56480.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372979.9/ ENSP00000362070.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..644
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..644
                     /product="protein ecdysoneless homolog isoform 1"
                     /note="suppressor of S. cerevisiae gcr2; ecdysoneless
                     homolog; protein SGT1; human suppressor of GCR two;
                     suppressor of GCR2; protein ecdysoneless homolog"
                     /calculated_mol_wt=72627
     Region          14..597
                     /region_name="SGT1"
                     /note="SGT1 protein; pfam07093"
                     /db_xref="CDD:462089"
     Region          430..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Region          439..644
                     /region_name="Transcription activation.
                     /evidence=ECO:0000269|PubMed:19919181"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Region          481..497
                     /region_name="Involved in nuclear export.
                     /evidence=ECO:0000269|PubMed:19919181"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Region          496..537
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Region          502..532
                     /region_name="Acidic region required for transactivation
                     activity. /evidence=ECO:0000269|PubMed:19919181"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O95905.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O95905.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O95905.1)"
     Region          567..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     Region          623..644
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95905.1)"
     CDS             1..644
                     /gene="ECD"
                     /gene_synonym="GCR2; HSGT1; SGT1"
                     /coded_by="NM_007265.3:157..2091"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7321.1"
                     /db_xref="GeneID:11319"
                     /db_xref="HGNC:HGNC:17029"
                     /db_xref="MIM:616464"
ORIGIN      
        1 meetmklatm edtveyclfl ipdesrdsdk hkeilqkyie riitrfapml vpyiwqnqpf
       61 nlkykpgkgg vpahmfgvtk fgdniedewf ivyvikqitk efpelvarie dndgefllie
      121 aadflpkwld penstnrvff chgelciipa prksgaeswl pttpptipqa lniitahsek
      181 ilasesiraa vnrrirgype kiqaslhrah cflpagivav lkqrprlvaa avqafylrdp
      241 idlracrvfk tflpetrimt svtftkclya qlvqqrfvpd rrsgyrlppp sdpqyrahel
      301 gmklahgfei lcskcsphfs dckkslvtas plwasflesl kkndyfkgli egsaqyrerl
      361 emaenyfqls vdwpesslam spgeeiltll qtipfdiedl kkeaanlppe dddqwldlsp
      421 dqldqllqea vgkkesesvs keekeqnydl tevsesmkaf iskvsthkga elprepseap
      481 itfdadsfln yfdkilgprp nesdsddldd edfecldsdd dldfethepg eeaslkgtld
      541 nlksymaqmd qelahtcisk sfttrnqvep vsqttdnnsd eedsgtgesv mapvdvdlnl
      601 vsnilesyss qaglagpasn llqsmgvqlp dntdhrptsk ptkn
//
LOCUS       NP_001166216             767 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec23B isoform 1 [Homo sapiens].
ACCESSION   NP_001166216
VERSION     NP_001166216.1
DBSOURCE    REFSEQ: accession NM_001172745.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Saptarshi,A.N., More,T.A., Dongerdiye,R. and Kedar,P.
  TITLE     Congenital Dyserythropoietic Anemia Type II: High Prevalence of
            c.1385A>G, (p.Tyr462Cys) Mutation in the Indian Population
  JOURNAL   Indian J Pediatr 90 (8), 840 (2023)
   PUBMED   37204595
  REMARK    GeneRIF: Congenital Dyserythropoietic Anemia Type II: High
            Prevalence of c.1385A>G, (p.Tyr462Cys) Mutation in the Indian
            Population.
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Musri,M.M., Venturi,V., Ferrer-Cortes,X., Romero-Cortadellas,L.,
            Hernandez,G., Leoz,P., Ricard Andres,M.P., Morado,M., Fernandez
            Valle,M.D.C., Beneitez Pastor,D., Ortuno Cabrero,A., Moreno
            Gamiz,M., Senent Peris,L., Perez-Valencia,A.I., Perez-Montero,S.,
            Tornador,C. and Sanchez,M.
  TITLE     New Cases and Mutations in SEC23B Gene Causing Congenital
            Dyserythropoietic Anemia Type II
  JOURNAL   Int J Mol Sci 24 (12), 9935 (2023)
   PUBMED   37373084
  REMARK    GeneRIF: New Cases and Mutations in SEC23B Gene Causing Congenital
            Dyserythropoietic Anemia Type II.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 767)
  AUTHORS   Rosato,B.E., Marra,R., D'Onofrio,V., Del Giudice,F., Della
            Monica,S., Iolascon,A., Andolfo,I. and Russo,R.
  TITLE     SEC23B Loss-of-Function Suppresses Hepcidin Expression by Impairing
            Glycosylation Pathway in Human Hepatic Cells
  JOURNAL   Int J Mol Sci 23 (3), 1304 (2022)
   PUBMED   35163229
  REMARK    GeneRIF: SEC23B Loss-of-Function Suppresses Hepcidin Expression by
            Impairing Glycosylation Pathway in Human Hepatic Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   8  (residues 1 to 767)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
REFERENCE   9  (residues 1 to 767)
  AUTHORS   Gasparini,P., Miraglia del Giudice,E., Delaunay,J., Totaro,A.,
            Granatiero,M., Melchionda,S., Zelante,L. and Iolascon,A.
  TITLE     Localization of the congenital dyserythropoietic anemia II locus to
            chromosome 20q11.2 by genomewide search
  JOURNAL   Am J Hum Genet 61 (5), 1112-1116 (1997)
   PUBMED   9345103
REFERENCE   10 (residues 1 to 767)
  AUTHORS   Paccaud,J.P., Reith,W., Carpentier,J.L., Ravazzola,M., Amherdt,M.,
            Schekman,R. and Orci,L.
  TITLE     Cloning and functional characterization of mammalian homologues of
            the COPII component Sec23
  JOURNAL   Mol Biol Cell 7 (10), 1535-1546 (1996)
   PUBMED   8898360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121893.21, DC351945.1,
            BC005404.1, BC005032.1 and AL121900.26.
            
            Summary: The protein encoded by this gene is a member of the SEC23
            subfamily of the SEC23/SEC24 family, which is involved in vesicle
            trafficking. The encoded protein has similarity to yeast Sec23p
            component of COPII. COPII is the coat protein complex responsible
            for vesicle budding from the ER. The function of this gene product
            has been implicated in cargo selection and concentration. Multiple
            alternatively spliced transcript variants have been identified in
            this gene. [provided by RefSeq, Feb 2010].
            
            Transcript Variant: This variant (4) has an alternate 5' UTR exon,
            as compared to variant 2. Variants 1, 2, 3 and 4 encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.86032.1,
                                           SRR1803614.14035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.23"
     Protein         1..767
                     /product="protein transport protein Sec23B isoform 1"
                     /note="SEC23-like protein B; SEC23 homolog B, coat complex
                     II component; SEC23-related protein B; protein transport
                     protein Sec23B; transport protein SEC23B; SEC23 homolog B,
                     COPII coat complex component"
                     /calculated_mol_wt=86348
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15437.2)"
     Region          12..765
                     /region_name="PLN00162"
                     /note="transport protein sec23; Provisional"
                     /db_xref="CDD:215083"
     Site            564
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D662; propagated from
                     UniProtKB/Swiss-Prot (Q15437.2)"
     Region          634..720
                     /region_name="Gelsolin-like. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15437.2)"
     CDS             1..767
                     /gene="SEC23B"
                     /gene_synonym="CDA-II; CDAII; CDAN2; CWS7; HEMPAS;
                     hSec23B"
                     /coded_by="NM_001172745.3:373..2676"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13137.1"
                     /db_xref="GeneID:10483"
                     /db_xref="HGNC:HGNC:10702"
                     /db_xref="MIM:610512"
ORIGIN      
        1 matylefiqq neerdgvrfs wnvwpssrle atrmvvplac lltplkerpd lppvqyepvl
       61 csrptckavl nplcqvdyra klwacnfcfq rnqfppaygg isevnqpael mpqfstieyv
      121 iqrgaqspli flyvvdtcle eddlqalkes lqmslsllpp dalvglitfg rmvqvhelsc
      181 egisksyvfr gtkdltakqi qdmlgltkpa mpmqqarpaq pqehpfassr flqpvhkidm
      241 nltdllgelq rdpwpvtqgk rplrstgval siavgllegt fpntgariml ftggpptqgp
      301 gmvvgdelki pirswhdiek dnarfmkkat khyemlanrt aanghcidiy acaldqtgll
      361 emkccanltg gymvmgdsfn tslfkqtfqr iftkdfngdf rmafgatldv ktsrelkiag
      421 aigpcvslnv kgpcvsenel gvggtsqwki cgldptstlg iyfevvnqhn tpipqggrga
      481 iqfvthyqhs stqrrirvtt iarnwadvqs qlrhieaafd qeaaavlmar lgvfraesee
      541 gpdvlrwldr qlirlcqkfg qynkedptsf rlsdsfslyp qfmfhlrrsp flqvfnnspd
      601 essyyrhhfa rqdltqslim iqpilysysf hgppepvlld sssiladril lmdtffqivi
      661 ylgetiaqwr kagyqdmpey enfkhllqap lddaqeilqa rfpmpryint ehggsqarfl
      721 lskvnpsqth nnlyawgqet gapiltddvs lqvfmdhlkk lavssac
//
LOCUS       NP_001317419            1332 aa            linear   PRI 20-NOV-2025
DEFINITION  claspin isoform 3 [Homo sapiens].
ACCESSION   NP_001317419 XP_011540241
VERSION     NP_001317419.1
DBSOURCE    REFSEQ: accession NM_001330490.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1332)
  AUTHORS   Hsieh,M.J., Lo,Y.S., Ho,H.Y., Lin,C.C., Chuang,Y.C. and Chen,M.K.
  TITLE     The Interaction between CLSPN Gene Polymorphisms and Alcohol
            Consumption Contributes to Oral Cancer Progression
  JOURNAL   Int J Mol Sci 25 (2), 1098 (2024)
   PUBMED   38256171
  REMARK    GeneRIF: The Interaction between CLSPN Gene Polymorphisms and
            Alcohol Consumption Contributes to Oral Cancer Progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1332)
  AUTHORS   Jia,Y., Cheng,X., Liang,W., Lin,S., Li,P., Yan,Z., Zhang,M., Ma,W.,
            Hu,C., Wang,B. and Liu,Z.
  TITLE     CLSPN is a potential biomarker associated with poor prognosis in
            low-grade gliomas based on a multi-database analysis
  JOURNAL   Curr Res Transl Med 70 (4), 103345 (2022)
   PUBMED   35487167
  REMARK    GeneRIF: CLSPN is a potential biomarker associated with poor
            prognosis in low-grade gliomas based on a multi-database analysis.
REFERENCE   4  (residues 1 to 1332)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1332)
  AUTHORS   Hu,T., Lei,D., Zhou,J. and Zhang,B.O.
  TITLE     circRNA derived from CLSPN (circCLSPN) is an oncogene in human
            glioblastoma multiforme by regulating cell growth, migration and
            invasion via ceRNA pathway
  JOURNAL   J Biosci 46 (2021)
   PUBMED   34269180
  REMARK    GeneRIF: circRNA derived from CLSPN (circCLSPN) is an oncogene in
            human glioblastoma multiforme by regulating cell growth, migration
            and invasion via ceRNA pathway.
REFERENCE   6  (residues 1 to 1332)
  AUTHORS   Lin,S.Y., Li,K., Stewart,G.S. and Elledge,S.J.
  TITLE     Human Claspin works with BRCA1 to both positively and negatively
            regulate cell proliferation
  JOURNAL   Proc Natl Acad Sci U S A 101 (17), 6484-6489 (2004)
   PUBMED   15096610
  REMARK    GeneRIF: determination of properties of both a tumor suppressor and
            an oncogene
REFERENCE   7  (residues 1 to 1332)
  AUTHORS   Chini,C.C. and Chen,J.
  TITLE     Human claspin is required for replication checkpoint control
  JOURNAL   J Biol Chem 278 (32), 30057-30062 (2003)
   PUBMED   12766152
  REMARK    GeneRIF: Claspin has a potentially critical role in replication
            checkpoint control in mammalian cells
REFERENCE   8  (residues 1 to 1332)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
REFERENCE   9  (residues 1 to 1332)
  AUTHORS   Kumagai,A. and Dunphy,W.G.
  TITLE     Claspin, a novel protein required for the activation of Chk1 during
            a DNA replication checkpoint response in Xenopus egg extracts
  JOURNAL   Mol Cell 6 (4), 839-849 (2000)
   PUBMED   11090622
REFERENCE   10 (residues 1 to 1332)
  AUTHORS   Calderari,G.
  TITLE     [Inlays in the prosthetic rehabilitation of the periodontal
            patient]
  JOURNAL   Dent Cadmos 34 (11), 1509-1537 (1966)
   PUBMED   5226314
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354864.16.
            
            On Aug 29, 2016 this sequence version replaced XP_011540241.1.
            
            Summary: The product of this gene is an essential upstream
            regulator of checkpoint kinase 1 and triggers a checkpoint arrest
            of the cell cycle in response to replicative stress or DNA damage.
            The protein is also required for efficient DNA replication during a
            normal S phase. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (3) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (3)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..1332
                     /product="claspin isoform 3"
                     /note="claspin homolog"
                     /calculated_mol_wt=150238
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YR7; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          136..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          243..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          311..318
                     /region_name="PCNA-interacting protein (PIP).
                     /evidence=ECO:0000269|PubMed:27401717"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          336..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          618..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          730..774
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            744
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            839
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            891
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          910..919
                     /region_name="CKB motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            916
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CHEK1.
                     /evidence=ECO:0000269|PubMed:16963448; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          939..948
                     /region_name="CKB motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          946..973
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            950
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            954
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          976..985
                     /region_name="CKB motif 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          985..1075
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Region          988..1086
                     /region_name="Acidic patch.
                     /evidence=ECO:0000269|PubMed:27401717"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1012
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1018
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1072..1073
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-7.
                     /evidence=ECO:0000269|PubMed:16123041; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HAW4.3)"
     Site            1289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HAW4.3)"
     CDS             1..1332
                     /gene="CLSPN"
                     /coded_by="NM_001330490.2:109..4107"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81299.1"
                     /db_xref="GeneID:63967"
                     /db_xref="HGNC:HGNC:19715"
                     /db_xref="MIM:605434"
ORIGIN      
        1 mtgevgsevh leindpnvis qeeadspsds gqgsyetigp lsegdsdeei fvskklknrk
       61 vlqdsdsete dtnaspektt ydsaeeenke nlyagkntki kriyktvads desymeksly
      121 qenleaqvkp clelslqsgn stdfttdrks skkhihdkeg tagkakvksk rrlekeerkm
      181 ekirqlkkke tknqeddveq pfndsgcllv dkdlfetgle dennsplede eslesiraav
      241 knkvkkhkkk epslesgvhs feegselskg ttrkerkaar lskealkqlh setqrlires
      301 alnlpyhmpe nktihdffkr kprptchgna mallksskyq sshhkeiidt anttemnsdh
      361 hskgseqttg aenevetnal pvvsketqii tgsdescrkd lvkneeleiq ekqkqsdirp
      421 spgdssvlqq esnflgnnhs eecqvgglva fephalegeg pqnpeetdek veepeqqnks
      481 savgppekvr rftldrlkql gvdvsikprl gadedsfvil epetnrelea lkqrfwkhan
      541 paakpragqt vnvnvivkdm gtdgkeelka dvvpvtlapk kldgashtkp geklqvlkak
      601 lqeamklrrf eerqkrqalf kldnedgfee eeeeeeemtd eseedgeekv ekeekeeele
      661 eeeekeeeee eegnqetaef llsseeietk dekemdkenn dgsseigkav gflsvpksls
      721 sdstlllfkd ssskmgyfpt eeksetdens gkqpsklded dscslltkes shnssfelig
      781 stipsyqpcn rqtgrgtsff ptaggfrsps pglfraslvs saskssgkls epslpiedsq
      841 dlynaspepk tlflgagdfq fcleddtqsq lldadgflnv rnhrnqyqal kprlplasmd
      901 enamdanmde lldlctgkft sqaekhlprk sdkkenmeel lnlcsgkfts qdastpasse
      961 lnkqekessm gdpmeealal csgsfptdke eedeeeefgd frlvsndnef dsdedehsds
     1021 gndlaledhe dddeeellkr seklkrqmrl rkyledeaev sgsdvgsede ydgeeideye
     1081 edvidevlps deelqsqikk ihmktmlddd krqlrlyqer yladgdlhsd gpgrmrkfrw
     1141 kniddasqmd lfhrdsdddq teeqldesea rwrkeriere qwlrdmaqqg kitaeeeeei
     1201 gedsqfmila kkvtakalqk nasrpmviqe sksllrnpfe airpgsaqqv ktgsllnqpk
     1261 avlqklaals dhnpsaprns rnfvfhtlsp vkaeaakess ksqkipekds dwltwsgapi
     1321 pgffrlsfdp hg
//
LOCUS       NP_001135921             454 aa            linear   PRI 20-NOV-2025
DEFINITION  protein spinster homolog 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001135921
VERSION     NP_001135921.1
DBSOURCE    REFSEQ: accession NM_001142449.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   He,M., Kuk,A.C.Y., Ding,M., Chin,C.F., Galam,D.L.A., Nah,J.M.,
            Tan,B.C., Yeo,H.L., Chua,G.L., Benke,P.I., Wenk,M.R., Ho,L.,
            Torta,F. and Silver,D.L.
  TITLE     Spns1 is a lysophospholipid transporter mediating lysosomal
            phospholipid salvage
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2210353119 (2022)
   PUBMED   36161949
  REMARK    GeneRIF: Spns1 is a lysosomal proton-dependent
            lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine
            (LPE) transporter mediating phospholipid salvage pathway
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Fang,Z., Cao,B., Liao,J.M., Deng,J., Plummer,K.D., Liao,P., Liu,T.,
            Zhang,W., Zhang,K., Li,L., Margolin,D., Zeng,S.X., Xiong,J. and
            Lu,H.
  TITLE     SPIN1 promotes tumorigenesis by blocking the uL18 (universal large
            ribosomal subunit protein 18)-MDM2-p53 pathway in human cancer
  JOURNAL   Elife 7, e31275 (2018)
   PUBMED   29547122
  REMARK    GeneRIF: Spindlin 1 (SPIN1) sequesters ribosomal protein uL18 in
            the nucleolus, preventing it from interacting with c-mdm2
            Proto-oncogene protein (MDM2), and alleviating uL18-mediated
            inhibition of MDM2 ubiquitin ligase activity toward p53 tumor
            suppressor protein (p53).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 454)
  AUTHORS   Yanagisawa,H., Ishii,T., Endo,K., Kawakami,E., Nagao,K.,
            Miyashita,T., Akiyama,K., Watabe,K., Komatsu,M., Yamamoto,D. and
            Eto,Y.
  TITLE     L-leucine and SPNS1 coordinately ameliorate dysfunction of
            autophagy in mouse and human Niemann-Pick type C disease
  JOURNAL   Sci Rep 7 (1), 15944 (2017)
   PUBMED   29162837
  REMARK    GeneRIF: SPNS1-dependent L-leucine export across the lysosomal
            membrane is a key step for triggering autophagy, and that this
            mechanism is impaired in Niemann-Pick type C disease-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Chang,J., Lee,S. and Blackstone,C.
  TITLE     Spastic paraplegia proteins spastizin and spatacsin mediate
            autophagic lysosome reformation
  JOURNAL   J Clin Invest 124 (12), 5249-5262 (2014)
   PUBMED   25365221
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Rietveld,C.A., Esko,T., Davies,G., Pers,T.H., Turley,P.,
            Benyamin,B., Chabris,C.F., Emilsson,V., Johnson,A.D., Lee,J.J., de
            Leeuw,C., Marioni,R.E., Medland,S.E., Miller,M.B., Rostapshova,O.,
            van der Lee,S.J., Vinkhuyzen,A.A., Amin,N., Conley,D.,
            Derringer,J., van Duijn,C.M., Fehrmann,R., Franke,L., Glaeser,E.L.,
            Hansell,N.K., Hayward,C., Iacono,W.G., Ibrahim-Verbaas,C.,
            Jaddoe,V., Karjalainen,J., Laibson,D., Lichtenstein,P.,
            Liewald,D.C., Magnusson,P.K., Martin,N.G., McGue,M., McMahon,G.,
            Pedersen,N.L., Pinker,S., Porteous,D.J., Posthuma,D.,
            Rivadeneira,F., Smith,B.H., Starr,J.M., Tiemeier,H., Timpson,N.J.,
            Trzaskowski,M., Uitterlinden,A.G., Verhulst,F.C., Ward,M.E.,
            Wright,M.J., Davey Smith,G., Deary,I.J., Johannesson,M., Plomin,R.,
            Visscher,P.M., Benjamin,D.J., Cesarini,D. and Koellinger,P.D.
  TITLE     Common genetic variants associated with cognitive performance
            identified using the proxy-phenotype method
  JOURNAL   Proc Natl Acad Sci U S A 111 (38), 13790-13794 (2014)
   PUBMED   25201988
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2015 Jan 27;112(4):E380. doi:
            10.1073/pnas.1424631112. PMID: 25572966]
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Vastermark,A., Jacobsson,J.A., Johansson,A., Fredriksson,R.,
            Gyllensten,U. and Schioth,H.B.
  TITLE     Polymorphisms in sh2b1 and spns1 loci are associated with
            triglyceride levels in a healthy population in northern Sweden
  JOURNAL   J Genet 91 (2), 237-240 (2012)
   PUBMED   22942098
  REMARK    GeneRIF: A single nucleotide polymorphism located within the spns1
            gene is associated with plasma triglyceride levels.
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Yanagisawa,H., Miyashita,T., Nakano,Y. and Yamamoto,D.
  TITLE     HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL,
            induces a caspase-independent autophagic cell death
  JOURNAL   Cell Death Differ 10 (7), 798-807 (2003)
   PUBMED   12815463
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Nakano,Y., Fujitani,K., Kurihara,J., Ragan,J., Usui-Aoki,K.,
            Shimoda,L., Lukacsovich,T., Suzuki,K., Sezaki,M., Sano,Y., Ueda,R.,
            Awano,W., Kaneda,M., Umeda,M. and Yamamoto,D.
  TITLE     Mutations in the novel membrane protein spinster interfere with
            programmed cell death and cause neural degeneration in Drosophila
            melanogaster
  JOURNAL   Mol Cell Biol 21 (11), 3775-3788 (2001)
   PUBMED   11340170
  REMARK    GeneRIF: Spinster protein interferes with programmed cell death in
            Drosophila melanogaster and has orthologs in nematode, mouse, and
            human.
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG771918.1, AL390215.1 and CD368853.1.
            
            Transcript Variant: This variant (5) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL390215.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400289 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..454
                     /product="protein spinster homolog 1 isoform 4"
                     /note="sphingolipid transporter 1 (putative); solute
                     carrier family 63 member 1; protein spinster homolog 1;
                     spinster-like protein 1; SPNS sphingolipid transporter 1
                     (putative)"
                     /calculated_mol_wt=48882
     Region          62..405
                     /region_name="MFS_spinster_like"
                     /note="Protein spinster and spinster homologs of the Major
                     Facilitator Superfamily of transporters; cd17328"
                     /db_xref="CDD:340886"
     Site            order(72..73,76..77,80,90,142..143,145..147,150,170,
                     173..174,177,259,263,316..317,321,325,345,348..349,
                     352..353,356)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340886"
     CDS             1..454
                     /gene="SPNS1"
                     /gene_synonym="HSpin1; LAT; nrs; PP2030; SLC62A1; SLC63A1;
                     SPIN1; SPINL"
                     /coded_by="NM_001142449.2:375..1739"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS45453.1"
                     /db_xref="GeneID:83985"
                     /db_xref="HGNC:HGNC:30621"
                     /db_xref="MIM:612583"
ORIGIN      
        1 magsdtapfl sqaddpddgp vpgtpglpgs tgnpkseepe vpdqeglqri tglspgrsal
       61 ivavlcyinl lnymdrftva vfissymvla pvfgylgdry nrkylmcggi afwslvtlgs
      121 sfipgehfwl llltrglvgv geasystiap tliadlfvad qrsrmlsify faipvgsglg
      181 yiagskvkdm agdwhwalrv tpglgvvavl llflvvrepp rgaverhsdl pplnptswwa
      241 dlralarnli fglitcltgv lgvglgveis rrlrhsnpra dplvcatgll gsapflflsl
      301 acargsivat yififigetl lsmnwaivad illyvviptr rstaeafqiv lshllgdags
      361 pyliglisdr lrrnwppsfl sefralqfsl mlcafvgalg gaaflgtaif ieadrrraql
      421 hvqgllheag stddrivvpq rgrstrvpva svli
//
LOCUS       NP_060767                654 aa            linear   PRI 20-NOV-2025
DEFINITION  peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase isoform
            1 [Homo sapiens].
ACCESSION   NP_060767
VERSION     NP_060767.2
DBSOURCE    REFSEQ: accession NM_018297.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Satoh,T., Yagi-Utsumi,M., Ishii,N., Mizushima,T., Yagi,H., Kato,R.,
            Tachida,Y., Tateno,H., Matsuo,I., Kato,K., Suzuki,T. and Yoshida,Y.
  TITLE     Structural basis of sugar recognition by SCFFBS2 ubiquitin ligase
            involved in NGLY1 deficiency
  JOURNAL   FEBS Lett 598 (18), 2259-2268 (2024)
   PUBMED   39171510
  REMARK    GeneRIF: Structural basis of sugar recognition by SCF[FBS2]
            ubiquitin ligase involved in NGLY1 deficiency.
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Frater,C.H., Ruzhnikov,M.R.Z., Beres,S., Alcorn,D., Shue,A. and
            Levy,R.J.
  TITLE     Ocular features of NGLY1 deficiency from a prospective longitudinal
            cohort
  JOURNAL   J AAPOS 28 (3), 103925 (2024)
   PUBMED   38697387
  REMARK    GeneRIF: Ocular features of NGLY1 deficiency from a prospective
            longitudinal cohort.
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Manole,A., Wong,T., Rhee,A., Novak,S., Chin,S.M., Tsimring,K.,
            Paucar,A., Williams,A., Newmeyer,T.F., Schafer,S.T., Rosh,I.,
            Kaushik,S., Hoffman,R., Chen,S., Wang,G., Snyder,M., Cuervo,A.M.,
            Andrade,L., Manor,U., Lee,K., Jones,J.R., Stern,S., Marchetto,M.C.
            and Gage,F.H.
  TITLE     NGLY1 mutations cause protein aggregation in human neurons
  JOURNAL   Cell Rep 42 (12), 113466 (2023)
   PUBMED   38039131
  REMARK    GeneRIF: NGLY1 mutations cause protein aggregation in human
            neurons.
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Stanclift,C.R., Dwight,S.S., Lee,K., Eijkenboom,Q.L., Wilsey,M.,
            Wilsey,K., Kobayashi,E.S., Tong,S. and Bainbridge,M.N.
  TITLE     NGLY1 deficiency: estimated incidence, clinical features, and
            genotypic spectrum from the NGLY1 Registry
  JOURNAL   Orphanet J Rare Dis 17 (1), 440 (2022)
   PUBMED   36528660
  REMARK    GeneRIF: NGLY1 deficiency: estimated incidence, clinical features,
            and genotypic spectrum from the NGLY1 Registry.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Katiyar,S., Joshi,S. and Lennarz,W.J.
  TITLE     The retrotranslocation protein Derlin-1 binds peptide:N-glycanase
            to the endoplasmic reticulum
  JOURNAL   Mol Biol Cell 16 (10), 4584-4594 (2005)
   PUBMED   16055502
REFERENCE   7  (residues 1 to 654)
  AUTHORS   Misaghi,S., Pacold,M.E., Blom,D., Ploegh,H.L. and Korbel,G.A.
  TITLE     Using a small molecule inhibitor of peptide: N-glycanase to probe
            its role in glycoprotein turnover
  JOURNAL   Chem Biol 11 (12), 1677-1687 (2004)
   PUBMED   15610852
REFERENCE   8  (residues 1 to 654)
  AUTHORS   Katiyar,S., Li,G. and Lennarz,W.J.
  TITLE     A complex between peptide:N-glycanase and two proteasome-linked
            proteins suggests a mechanism for the degradation of misfolded
            glycoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (38), 13774-13779 (2004)
   PUBMED   15358861
REFERENCE   9  (residues 1 to 654)
  AUTHORS   Suzuki,T., Park,H., Hollingsworth,N.M., Sternglanz,R. and
            Lennarz,W.J.
  TITLE     PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase
  JOURNAL   J Cell Biol 149 (5), 1039-1052 (2000)
   PUBMED   10831608
  REMARK    GeneRIF: Describes the function of Yeast PNG1 and identifies
            similar proteins in mouse, human, D. melanogaster, C. elegans, and
            S. pombe.
REFERENCE   10 (residues 1 to 654)
  AUTHORS   Lam,C., Wolfe,L., Need,A., Shashi,V. and Enns,G.
  TITLE     NGLY1-Related Congenital Disorder of Deglycosylation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29419975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092798.3, BC007226.1 and
            BQ017148.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 3, 2002 this sequence version replaced NP_060767.1.
            
            Summary: This gene encodes an enzyme that catalyzes hydrolysis of
            an N(4)-(acetyl-beta-D-glucosaminyl) asparagine residue to
            N-acetyl-beta-D-glucosaminylamine and a peptide containing an
            aspartate residue. The encoded enzyme may play a role in the
            proteasome-mediated degradation of misfolded glycoproteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.667160.1,
                                           SRR1660803.2103.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280700.10/ ENSP00000280700.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..654
                     /product="peptide-N(4)-(N-acetyl-beta-
                     glucosaminyl)asparagine amidase isoform 1"
                     /EC_number="3.5.1.52"
                     /note="peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
                     amidase; hPNGase; peptide:N-glycanase"
                     /calculated_mol_wt=74259
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96IV0.1)"
     Region          19..109
                     /region_name="PUB_PNGase"
                     /note="PNGase/UBA or UBX (PUB) domain of the P97 adaptor
                     protein Peptide:N-glycanase (PNGase); cd10459"
                     /db_xref="CDD:198417"
     Site            order(34,37..38,41,50..51,53..55,58,60,64)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:198417"
     Region          112..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96IV0.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96IV0.1)"
     Region          275..354
                     /region_name="Transglut_core"
                     /note="Transglutaminase-like superfamily; pfam01841"
                     /db_xref="CDD:376628"
     Region          <338..>392
                     /region_name="Rad4"
                     /note="Rad4 transglutaminase-like domain; pfam03835"
                     /db_xref="CDD:427539"
     Region          457..651
                     /region_name="PAW"
                     /note="PNGase C-terminal domain, mannose-binding module
                     PAW; pfam04721"
                     /db_xref="CDD:461409"
     CDS             1..654
                     /gene="NGLY1"
                     /gene_synonym="CDDG; CDG1V; PNG-1; PNG1; PNGase"
                     /coded_by="NM_018297.4:54..2018"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33719.1"
                     /db_xref="GeneID:55768"
                     /db_xref="HGNC:HGNC:17646"
                     /db_xref="MIM:610661"
ORIGIN      
        1 maaaalgsss gsaspavael cqntpetfle askllltyad nilrnpndek yrsirignta
       61 fstrllpvrg aveclfemgf eegethlifp kkasveqlqk irdliaiers srldgsnksh
      121 kvkssqqpaa stqlpttpss npsglnqhtr nrqgqssdpp sastvaadsa ilevlqsniq
      181 hvlvyenpal qekalacipv qelkrksqek lsrarkldkg inisdedfll lellhwfkee
      241 ffhwvnnvlc skcggqtrsr drsllpsdde lkwgakeved hycdacqfsn rfprynnpek
      301 lletrcgrcg ewancftlcc ravgfearyv wdytdhvwte vyspsqqrwl hcdacedvcd
      361 kpllyeigwg kklsyviafs kdevvdvtwr ysckheevia rrtkvkeall rdtinglnkq
      421 rqlflsenrr kellqriive lvefispktp kpgelggris gsvawrvarg emglqrketl
      481 fipcenekis kqlhlcyniv kdryvrvsnn nqtisgweng vwkmesifrk vetdwhmvyl
      541 arkegssfay iswkfecgsv glkvdsisir tssqtfqtgt vewklrsdta qveltgdnsl
      601 hsyadfsgat evileaelsr gdgdvawqht qlfrqslndh eencleiiik fsdl
//
LOCUS       NP_001357086             142 aa            linear   PRI 20-NOV-2025
DEFINITION  DPY30 domain-containing protein 1 isoform b [Homo sapiens].
ACCESSION   NP_001357086
VERSION     NP_001357086.1
DBSOURCE    REFSEQ: accession NM_001370157.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Li,S., Qiao,Y., Di,Q., Le,X., Zhang,L., Zhang,X., Zhang,C.,
            Cheng,J., Zong,S., Koide,S.S., Miao,S. and Wang,L.
  TITLE     Interaction of SH3P13 and DYDC1 protein: a germ cell component that
            regulates acrosome biogenesis during spermiogenesis
  JOURNAL   Eur J Cell Biol 88 (9), 509-520 (2009)
   PUBMED   19545932
  REMARK    Erratum:[Eur J Cell Biol. 2019 Jan;98(1):51-52. doi:
            10.1016/j.ejcb.2018.11.002. PMID: 30497823]
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL359195.24.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. The encoded protein is involved in
            acrosome formation during spermatid development. This gene locus
            overlaps with a closely related gene on the opposite strand.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon compared to variant 3. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.143470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..142
                     /product="DPY30 domain-containing protein 1 isoform b"
                     /note="DPY30 domain-containing protein 1"
                     /calculated_mol_wt=16923
     Region          2..43
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..142
                     /gene="DYDC1"
                     /gene_synonym="DPY30D1"
                     /coded_by="NM_001370157.1:413..841"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:143241"
                     /db_xref="HGNC:HGNC:23460"
                     /db_xref="MIM:615154"
ORIGIN      
        1 mesiylqkhl gacltqglae varvrpvdpi eylalwiyky kenvtmeqlr qkemaklere
       61 relalmeqem merlkaeell lqqqqlalql elemqekerq riqelqraqe qlgkemrmnm
      121 enlvrnedil hseialnidq dl
//
LOCUS       NP_004588                118 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein Sm D2 isoform 1 [Homo sapiens].
ACCESSION   NP_004588 XP_005259237
VERSION     NP_004588.1
DBSOURCE    REFSEQ: accession NM_004597.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Chang,C., Li,L., Su,L., Yang,F., Zha,Q., Sun,M., Tao,L., Wang,M.,
            Song,K., Jiang,L., Gao,H., Liang,Y., Xu,C., Yong,C., Wang,M.,
            Huang,J., Liu,J., Jin,W., Lv,W., Dong,H., Li,Q., Bu,F., Yan,S.,
            Qi,H., Zhao,S., Zhu,Y., Wang,Y., Shi,J., Qiao,Y., Xu,J., Chabot,B.
            and Chen,J.
  TITLE     Intron Retention of DDX39A Driven by SNRPD2 is a Crucial Splicing
            Axis for Oncogenic MYC/Spliceosome Program in Hepatocellular
            Carcinoma
  JOURNAL   Adv Sci (Weinh) 11 (35), e2403387 (2024)
   PUBMED   39018261
  REMARK    GeneRIF: Intron Retention of DDX39A Driven by SNRPD2 is a Crucial
            Splicing Axis for Oncogenic MYC/Spliceosome Program in
            Hepatocellular Carcinoma.
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Kambach,C., Walke,S., Young,R., Avis,J.M., de la Fortelle,E.,
            Raker,V.A., Luhrmann,R., Li,J. and Nagai,K.
  TITLE     Crystal structures of two Sm protein complexes and their
            implications for the assembly of the spliceosomal snRNPs
  JOURNAL   Cell 96 (3), 375-387 (1999)
   PUBMED   10025403
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Lehmeier,T., Raker,V., Hermann,H. and Luhrmann,R.
  TITLE     cDNA cloning of the Sm proteins D2 and D3 from human small nuclear
            ribonucleoproteins: evidence for a direct D1-D2 interaction
  JOURNAL   Proc Natl Acad Sci U S A 91 (25), 12317-12321 (1994)
   PUBMED   7527560
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Lehmeier,T., Foulaki,K. and Luhrmann,R.
  TITLE     Evidence for three distinct D proteins, which react differentially
            with anti-Sm autoantibodies, in the cores of the major snRNPs U1,
            U2, U4/U6 and U5
  JOURNAL   Nucleic Acids Res 18 (22), 6475-6484 (1990)
   PUBMED   1701240
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Rokeach,L.A., Haselby,J.A. and Hoch,S.O.
  TITLE     Molecular cloning of a cDNA encoding the human Sm-D autoantigen
  JOURNAL   Proc Natl Acad Sci U S A 85 (13), 4832-4836 (1988)
   PUBMED   3260384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF130080.1, AC007191.1 and
            AJ707552.1.
            
            On Mar 18, 2016 this sequence version replaced XP_005259237.1.
            
            Summary: The protein encoded by this gene belongs to the small
            nuclear ribonucleoprotein core protein family. It is required for
            pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, May 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CF130080.1, SRR1163655.367543.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..118
                     /product="small nuclear ribonucleoprotein Sm D2 isoform 1"
                     /note="snRNP core protein D2; small nuclear
                     ribonucleoprotein Sm D2; small nuclear ribonucleoprotein
                     D2 polypeptide 16.5kDa"
                     /calculated_mol_wt=13396
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62316.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P62316.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62316.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62316.1)"
     Region          24..113
                     /region_name="Sm_D2"
                     /note="Sm protein D2; cd01720"
                     /db_xref="CDD:212467"
     Site            order(25,28..29,47..49,61..62,64,102,104)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212467"
     Site            order(31,39,45..49,56..57,60..64,68..69,72..73,92..94,96,
                     98..104,106..112)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212467"
     Site            order(42..48,50..62,64..68)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212467"
     Site            98..109
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212467"
     CDS             1..118
                     /gene="SNRPD2"
                     /gene_synonym="Sm-D2; SMD2; SNRPD1"
                     /coded_by="NM_004597.6:256..612"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33053.1"
                     /db_xref="GeneID:6633"
                     /db_xref="HGNC:HGNC:11159"
                     /db_xref="MIM:601061"
ORIGIN      
        1 msllnkpkse mtpeelqkre eeefntgpls vltqsvknnt qvlincrnnk kllgrvkafd
       61 rhcnmvlenv kemwtevpks gkgkkkskpv nkdryiskmf lrgdsvivvl rnpliagk
//
LOCUS       NP_001776                146 aa            linear   PRI 20-NOV-2025
DEFINITION  cytidine deaminase [Homo sapiens].
ACCESSION   NP_001776
VERSION     NP_001776.1
DBSOURCE    REFSEQ: accession NM_001785.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Lumeau,A., Bery,N., Frances,A., Gayral,M., Labrousse,G.,
            Ribeyre,C., Lopez,C., Nevot,A., El Kaoutari,A., Hanoun,N.,
            Sarot,E., Perrier,M., Pont,F., Cerapio,J.P., Fournie,J.J.,
            Lopez,F., Madrid-Mencia,M., Pancaldi,V., Pillaire,M.J.,
            Bergoglio,V., Torrisani,J., Dusetti,N., Hoffmann,J.S., Buscail,L.,
            Lutzmann,M. and Cordelier,P.
  TITLE     Cytidine Deaminase Resolves Replicative Stress and Protects
            Pancreatic Cancer from DNA-Targeting Drugs
  JOURNAL   Cancer Res 84 (7), 1013-1028 (2024)
   PUBMED   38294491
  REMARK    GeneRIF: Cytidine Deaminase Resolves Replicative Stress and
            Protects Pancreatic Cancer from DNA-Targeting Drugs.
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Hong,K.U., Tagnedji,A.H., Doll,M.A., Walls,K.M. and Hein,D.W.
  TITLE     Upregulation of cytidine deaminase in NAT1 knockout breast cancer
            cells
  JOURNAL   J Cancer Res Clin Oncol 149 (8), 5047-5060 (2023)
   PUBMED   36329350
  REMARK    GeneRIF: Upregulation of cytidine deaminase in NAT1 knockout breast
            cancer cells.
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Kurup,H.M., Kvach,M.V., Harjes,S., Jameson,G.B., Harjes,E. and
            Filichev,V.V.
  TITLE     Seven-membered ring nucleobases as inhibitors of human cytidine
            deaminase and APOBEC3A
  JOURNAL   Org Biomol Chem 21 (24), 5117-5128 (2023)
   PUBMED   37282621
  REMARK    GeneRIF: Seven-membered ring nucleobases as inhibitors of human
            cytidine deaminase and APOBEC3A.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Silveira,S.C., Buhagiar-Labarchede,G., Onclercq-Delic,R.,
            Gemble,S., Bou Samra,E., Mameri,H., Duchambon,P., Machon,C.,
            Guitton,J. and Amor-Gueret,M.
  TITLE     A decrease in NAMPT activity impairs basal PARP-1 activity in
            cytidine deaminase deficient-cells, independently of NAD
  JOURNAL   Sci Rep 10 (1), 13907 (2020)
   PUBMED   32807821
  REMARK    GeneRIF: A decrease in NAMPT activity impairs basal PARP-1 activity
            in cytidine deaminase deficient-cells, independently of NAD(.)
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Vincenzetti,S., Cambi,A., Neuhard,J., Garattini,E. and Vita,A.
  TITLE     Recombinant human cytidine deaminase: expression, purification, and
            characterization
  JOURNAL   Protein Expr Purif 8 (2), 247-253 (1996)
   PUBMED   8812871
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Laliberte,J. and Momparler,R.L.
  TITLE     Human cytidine deaminase: purification of enzyme, cloning, and
            expression of its complementary DNA
  JOURNAL   Cancer Res 54 (20), 5401-5407 (1994)
   PUBMED   7923172
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Saccone,S., Besati,C., Andreozzi,L., Della Valle,G., Garattini,E.
            and Terao,M.
  TITLE     Assignment of the human cytidine deaminase (CDA) gene to chromosome
            1 band p35-p36.2
  JOURNAL   Genomics 22 (3), 661-662 (1994)
   PUBMED   8001985
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Kuhn,K., Bertling,W.M. and Emmrich,F.
  TITLE     Cloning of a functional cDNA for human cytidine deaminase (CDD) and
            its use as a marker of monocyte/macrophage differentiation
  JOURNAL   Biochem Biophys Res Commun 190 (1), 1-7 (1993)
   PUBMED   8422236
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Wentworth,D.F. and Wolfenden,R.
  TITLE     On the interaction of 3,4,5,6-tetrahydrouridine with human liver
            cytidine deaminase
  JOURNAL   Biochemistry 14 (23), 5099-5105 (1975)
   PUBMED   53069
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD675458.1 and BC054036.1.
            
            Summary: This gene encodes an enzyme involved in pyrimidine
            salvaging. The encoded protein forms a homotetramer that catalyzes
            the irreversible hydrolytic deamination of cytidine and
            deoxycytidine to uridine and deoxyuridine, respectively. It is one
            of several deaminases responsible for maintaining the cellular
            pyrimidine pool. Mutations in this gene are associated with
            decreased sensitivity to the cytosine nucleoside analogue cytosine
            arabinoside used in the treatment of certain childhood leukemias.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L27943.1, BC054036.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375071.4/ ENSP00000364212.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..146
                     /product="cytidine deaminase"
                     /EC_number="3.5.4.5"
                     /note="cytidine aminohydrolase; cytosine nucleoside
                     deaminase; small cytidine deaminase"
                     /calculated_mol_wt=16054
     Region          16..142
                     /region_name="cyt_deam_tetra"
                     /note="cytidine deaminase, homotetrameric; TIGR01354"
                     /db_xref="CDD:273572"
     CDS             1..146
                     /gene="CDA"
                     /gene_synonym="CDD"
                     /coded_by="NM_001785.3:34..474"
                     /db_xref="CCDS:CCDS210.1"
                     /db_xref="GeneID:978"
                     /db_xref="HGNC:HGNC:1712"
                     /db_xref="MIM:123920"
ORIGIN      
        1 maqkrpactl kpecvqqllv csqeakksay cpyshfpvga alltqegrif kgcnienacy
       61 plgicaerta iqkavsegyk dfraiaiasd mqddfispcg acrqvmrefg tnwpvymtkp
      121 dgtyivmtvq ellpssfgpe dlqktq
//
LOCUS       NP_001106205             494 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger and SCAN domain-containing protein 30 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001106205 XP_001720123 XP_001722432 XP_001723287
VERSION     NP_001106205.1
DBSOURCE    REFSEQ: accession NM_001112734.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Ivarsson,Y., Arnold,R., McLaughlin,M., Nim,S., Joshi,R., Ray,D.,
            Liu,B., Teyra,J., Pawson,T., Moffat,J., Li,S.S., Sidhu,S.S. and
            Kim,P.M.
  TITLE     Large-scale interaction profiling of PDZ domains through proteomic
            peptide-phage display using human and viral phage peptidomes
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2542-2547 (2014)
   PUBMED   24550280
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC414102.1, AY234408.1, AL832180.1, AK001503.1 and AA988135.1.
            
            On or before Mar 29, 2008 this sequence version replaced
            XP_001722432.1, XP_001720123.1, XP_001723287.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.35095.1,
                                           SRR1660805.181887.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000333206.10/ ENSP00000329738.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..494
                     /product="zinc finger and SCAN domain-containing protein
                     30 isoform 1"
                     /note="zinc finger protein 397 opposite strand; ZNF397
                     opposite strand; zinc finger and SCAN domain-containing
                     protein 30; zinc finger protein 397OS"
                     /calculated_mol_wt=56233
     Region          44..154
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          281..>360
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          303..323
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          <328..479
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          331..351
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(336,338,340,342..343,346..347,350,364,366,370..371,
                     374..375,378,392,394,396,398..399,402..403,406)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          359..379
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          387..407
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          415..435
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(420,422,424,426..427,430..431,434,448,450,454..455,
                     458..459,462,476,478,480,482..483,486..487,490)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          443..463
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          469..491
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..494
                     /gene="ZSCAN30"
                     /gene_synonym="ZNF-WYM; ZNF397OS; ZNF917"
                     /coded_by="NM_001112734.4:250..1734"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42427.1"
                     /db_xref="GeneID:100101467"
                     /db_xref="HGNC:HGNC:33517"
ORIGIN      
        1 msgeatvlay hapeeqegll vvkveeenyv ldqdfglqen pwsqevfrqk frqfsysdst
       61 gprealsrlr elccqwlrpe vhskeqilel lmleqflail peelqawlre hrpengeeav
      121 tmleelekel eeprqqdtth gqemfwqemt stgalkslsl nspvqplenq cktetqesqa
      181 fqerdgrmva gkvlmakqei vecvasaami spgklpgeth sqriaeealg gldnskkqkg
      241 naagnkisql psqdrhfsla tfnrripteh svlesheseg sfsmnsndit qqsvdtrekl
      301 yecfdcgkaf cqssklirhq rihtgerpya ckecgkafsl ssdlvrhqri hsgekpyecc
      361 ecgkafrgss elirhrriht gekpyecgec gkafsrssal iqhkkihtgd ksyeciacgk
      421 afgrssilie hqrihtgekp yecnecgksf nqssaltqhq rihtgekpye csecrktfrh
      481 rsglmqhqrt htrv
//
LOCUS       NP_001340534             343 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform k [Homo sapiens].
ACCESSION   NP_001340534 XP_016877024
VERSION     NP_001340534.1
DBSOURCE    REFSEQ: accession NM_001353605.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 343)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 343)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 343)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 343)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 343)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 343)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 343)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 343)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877024.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (20), as well as variants 17-19,
            encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.6064.1, SRR1803611.4786.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..343
                     /product="lysosomal cobalamin transporter ABCD4 isoform k"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=37800
     Region          <1..319
                     /region_name="SunT"
                     /note="ABC-type bacteriocin/lantibiotic exporters, contain
                     an N-terminal double-glycine peptidase domain [Defense
                     mechanisms]; COG2274"
                     /db_xref="CDD:441875"
     Region          124..335
                     /region_name="ABCD_peroxisomal_ALDP"
                     /note="ATP-binding cassette domain of peroxisomal
                     transporter, subfamily D; cd03223"
                     /db_xref="CDD:213190"
     CDS             1..343
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353605.2:717..1748"
                     /note="isoform k is encoded by transcript variant 20"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mrslllstvg intfdylgsi lsyvviaipi fsgvygdlsp aelstlvskn afvciylisc
       61 ftqlidlstt lsdvagythr igqlretlld mslksqdcei lgesewgldt ppgwpaaepa
      121 dtafllervs isapssdkpl ikdlslkise gqsllitgnt gtgktsllrv lgglwtstrg
      181 svqmltdfgp hgvlflpqkp fftdgtlreq viyplkevyp dsgsadderi lrflelagls
      241 nlvartegld qqvdwnwydv lspgemqrls farlfylqpk yavldeatsa lteevesely
      301 rigqqlgmtf isvghrqsle kfhslvlklc gggrwelmri kve
//
LOCUS       NP_005862                238 aa            linear   PRI 20-NOV-2025
DEFINITION  survival of motor neuron-related-splicing factor 30 [Homo sapiens].
ACCESSION   NP_005862
VERSION     NP_005862.1
DBSOURCE    REFSEQ: accession NM_005871.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Belleville,A.E., Thomas,J.D., Tonnies,J., Gabel,A.M., Borrero
            Rossi,A., Singh,P., Queitsch,C. and Bradley,R.K.
  TITLE     An autoregulatory poison exon in Smndc1 is conserved across
            kingdoms and influences organism growth
  JOURNAL   PLoS Genet 20 (8), e1011363 (2024)
   PUBMED   39150991
  REMARK    GeneRIF: An autoregulatory poison exon in Smndc1 is conserved
            across kingdoms and influences organism growth.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Casteels,T., Bajew,S., Reinis,J., Enders,L., Schuster,M.,
            Fontaine,F., Muller,A.C., Wagner,B.K., Bock,C. and Kubicek,S.
  TITLE     SMNDC1 links chromatin remodeling and splicing to regulate
            pancreatic hormone expression
  JOURNAL   Cell Rep 40 (9), 111288 (2022)
   PUBMED   36044849
  REMARK    GeneRIF: SMNDC1 links chromatin remodeling and splicing to regulate
            pancreatic hormone expression.
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Narayanan,U., Achsel,T., Luhrmann,R. and Matera,A.G.
  TITLE     Coupled in vitro import of U snRNPs and SMN, the spinal muscular
            atrophy protein
  JOURNAL   Mol Cell 16 (2), 223-234 (2004)
   PUBMED   15494309
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Rappsilber,J., Ajuh,P., Lamond,A.I. and Mann,M.
  TITLE     SPF30 is an essential human splicing factor required for assembly
            of the U4/U5/U6 tri-small nuclear ribonucleoprotein into the
            spliceosome
  JOURNAL   J Biol Chem 276 (33), 31142-31150 (2001)
   PUBMED   11331295
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Meister,G., Hannus,S., Plottner,O., Baars,T., Hartmann,E.,
            Fakan,S., Laggerbauer,B. and Fischer,U.
  TITLE     SMNrp is an essential pre-mRNA splicing factor required for the
            formation of the mature spliceosome
  JOURNAL   EMBO J 20 (9), 2304-2314 (2001)
   PUBMED   11331595
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Talbot,K., Miguel-Aliaga,I., Mohaghegh,P., Ponting,C.P. and
            Davies,K.E.
  TITLE     Characterization of a gene encoding survival motor neuron
            (SMN)-related protein, a constituent of the spliceosome complex
  JOURNAL   Hum Mol Genet 7 (13), 2149-2156 (1998)
   PUBMED   9817934
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ694303.1, BC011234.1 and
            AL360182.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a paralog of SMN1 gene, which encodes the
            survival motor neuron protein, mutations in which are cause of
            autosomal recessive proximal spinal muscular atrophy. The protein
            encoded by this gene is a nuclear protein that has been identified
            as a constituent of the spliceosome complex. This gene is
            differentially expressed, with abundant levels in skeletal muscle,
            and may share similar cellular function as the SMN1 gene. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1550391.1,
                                           SRR14038193.2094364.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369603.10/ ENSP00000358616.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.2"
     Protein         1..238
                     /product="survival of motor neuron-related-splicing factor
                     30"
                     /note="splicing factor 30, survival of motor
                     neuron-related; SMN-related protein; 30 kDa splicing
                     factor SMNrp; survival motor neuron domain-containing
                     protein 1; tudor domain containing 16C"
                     /calculated_mol_wt=26580
     Region          73..128
                     /region_name="Tudor_SPF30"
                     /note="Tudor domain found in survival of motor
                     neuron-related-splicing factor 30 (SPF30) and similar
                     proteins; cd20399"
                     /db_xref="CDD:410470"
     Site            order(83,88,90,108,111,113)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:410470"
     Region          142..160
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O75940.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75940.1)"
     Site            219
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75940.1)"
     CDS             1..238
                     /gene="SMNDC1"
                     /gene_synonym="SMNR; SPF30; TDRD16C"
                     /coded_by="NM_005871.4:174..890"
                     /db_xref="CCDS:CCDS7565.1"
                     /db_xref="GeneID:10285"
                     /db_xref="HGNC:HGNC:16900"
                     /db_xref="MIM:603519"
ORIGIN      
        1 msedlakqla sykaqlqqve aalsgngene dllklkkdlq evieltkdll stqpsetlas
       61 sdsfastqpt hswkvgdkcm avwsedgqcy eaeieeidee ngtaaitfag ygnaevtpll
      121 nlkpveegrk akedsgnkpm skkemiaqqr eykkkkalkk aqrikeleqe redqkvkwqq
      181 fnnraysknk kgqvkrsifa spesvtgkvg vgtcgiadkp mtqyqdtsky nvrhlmpq
//
LOCUS       NP_001191040              75 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 16 [Homo sapiens].
ACCESSION   NP_001191040
VERSION     NP_001191040.1
DBSOURCE    REFSEQ: accession NM_001204111.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 75)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 75)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 75)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 75)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 75)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 75)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 75)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 75)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 75)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 75)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            DQ849201.1 and AI268146.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (16) lacks an in-frame segment in
            the 5' coding region, and lacks an exon in the 3' coding region
            which results in a frameshift, compared to variant 1. The resulting
            isoform (16) is shorter and has a distinct C-terminus, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: DQ849201.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..75
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..75
                     /product="bcl-2-like protein 11 isoform 16"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=8083
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     CDS             1..75
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_001204111.2:289..516"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qdrspapmsc dkstqtpspp
       61 cqafnhylsa mgife
//
LOCUS       NP_002173                570 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_002173
VERSION     NP_002173.1
DBSOURCE    REFSEQ: accession NM_002182.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA024801.1, AB006537.1,
            BM194193.1 and BM973472.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Transcript Variant: This variant (1) encodes the membrane-bound
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB006537.1, SRR1660803.224601.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000447382.6/ ENSP00000390541.1
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..570
                     /product="interleukin-1 receptor accessory protein isoform
                     1 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=63114
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     mat_peptide     21..570
                     /product="Interleukin-1 receptor accessory protein.
                     /id=PRO_0000015450"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
                     /calculated_mol_wt=63114
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          405..552
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          549..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     CDS             1..570
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_002182.4:224..1936"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3298.1"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk vpaprytvel
      361 acgfgatvll vvilivvyhv ywlemvlfyr ahfgtdetil dgkeydiyvs yarnaeeeef
      421 vlltlrgvle nefgyklcif drdslpggiv tdetlsfiqk srrllvvlsp nyvlqgtqal
      481 lelkaglenm asrgninvil vqykavketk vkelkraktv ltvikwkgek skypqgrfwk
      541 qlqvampvkk sprrsssdeq glsysslknv
//
LOCUS       NP_001253970             642 aa            linear   PRI 20-NOV-2025
DEFINITION  armadillo repeat-containing protein 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001253970
VERSION     NP_001253970.1
DBSOURCE    REFSEQ: accession NM_001267041.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Zhan,T., Chen,M., Liu,W., Han,Z., Zhu,Q., Liu,M., Tan,J., Liu,J.,
            Chen,X., Tian,X. and Huang,X.
  TITLE     MiR-455-3p inhibits gastric cancer progression by repressing
            Wnt/beta-catenin signaling through binding to ARMC8
  JOURNAL   BMC Med Genomics 16 (1), 155 (2023)
   PUBMED   37400847
  REMARK    GeneRIF: MiR-455-3p inhibits gastric cancer progression by
            repressing Wnt/beta-catenin signaling through binding to ARMC8.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Li,X., Zhang,C., Yuan,Y., Wang,Y., Lu,S., Zhou,Z., Zhen,P. and
            Zhou,M.
  TITLE     Downregulation of ARMC8 promotes tumorigenesis through activating
            Wnt/beta-catenin pathway and EMT in cutaneous squamous cell
            carcinomas
  JOURNAL   J Dermatol Sci 102 (3), 184-192 (2021)
   PUBMED   34016486
  REMARK    GeneRIF: Downregulation of ARMC8 promotes tumorigenesis through
            activating Wnt/beta-catenin pathway and EMT in cutaneous squamous
            cell carcinomas.
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Jiang,G., Zhang,Y., Zhang,X., Fan,C., Wang,L., Xu,H., Yu,J. and
            Wang,E.
  TITLE     ARMc8 indicates aggressive colon cancers and promotes invasiveness
            and migration of colon cancer cells
  JOURNAL   Tumour Biol 36 (11), 9005-9013 (2015)
   PUBMED   26081621
  REMARK    GeneRIF: invasiveness and migration capacity of HT29 cells
            transfected with ARMc8 were significantly greater than those of
            control cells (p < 0.001), while ARMc8 siRNA treatment
            significantly reduced cell invasion and migration in LoVo cells
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Jiang,G., Yang,D., Wang,L., Zhang,X., Xu,H., Miao,Y., Wang,E. and
            Zhang,Y.
  TITLE     A novel biomarker ARMc8 promotes the malignant progression of
            ovarian cancer
  JOURNAL   Hum Pathol 46 (10), 1471-1479 (2015)
   PUBMED   26232863
  REMARK    GeneRIF: ARMc8 may enhance the invasion and metastasis of ovarian
            cancer cells
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Fan,C., Zhao,Y., Mao,X., Miao,Y., Lin,X., Jiang,G., Zhang,X.,
            Han,Q., Luan,L. and Wang,E.
  TITLE     Armc8 expression was elevated during atypia-to-carcinoma
            progression and associated with cancer development of breast
            carcinoma
  JOURNAL   Tumour Biol 35 (11), 11337-11343 (2014)
   PUBMED   25119601
  REMARK    GeneRIF: Armc8 expression was elevated during atypia-to-carcinoma
            progression and associated with cancer development of breast
            carcinoma.
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Xie,C., Jiang,G., Fan,C., Zhang,X., Zhang,Y., Miao,Y., Lin,X.,
            Wu,J., Wang,L., Liu,Y., Yu,J., Yang,L., Zhang,D., Xu,K. and Wang,E.
  TITLE     ARMC8alpha promotes proliferation and invasion of non-small cell
            lung cancer cells by activating the canonical Wnt signaling pathway
  JOURNAL   Tumour Biol 35 (9), 8903-8911 (2014)
   PUBMED   24894675
  REMARK    GeneRIF: Data suggest that armadillo repeat containing protein 8
            (ARMC8) might serve as a therapeutic target in non-small cell lung
            cancer (NSCLC).
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY004298.1, AK296837.1, AK299769.1, AL096748.1 and BQ014283.1.
            
            Transcript Variant: This variant (4) differs in the 5' and 3' UTRs
            and has multiple differences in the coding region, including the
            use of an alternate start codon, compared to variant 1. The encoded
            isoform (3) is longer and has distinct N- and C-termini, compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296837.1, SRR1163657.119266.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..642
                     /product="armadillo repeat-containing protein 8 isoform 3"
                     /note="armadillo repeat-containing protein 8; GID complex
                     subunit 5, VID28 homolog"
                     /calculated_mol_wt=71768
     Region          <22..181
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          57..90
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(81,85,89,123,127,131,175,179,183)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          98..134
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          150..184
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          <343..576
                     /region_name="COG5369"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:227663"
     Site            order(413,417,421,455,459,463,498,502,506)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          430..466
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          472..507
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          522..552
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..642
                     /gene="ARMC8"
                     /gene_synonym="GID5; HSPC056; S863-2; VID28"
                     /coded_by="NM_001267041.2:308..2236"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58854.1"
                     /db_xref="GeneID:25852"
                     /db_xref="HGNC:HGNC:24999"
                     /db_xref="MIM:618521"
ORIGIN      
        1 maclletpir msvlsevtas srhyvdrlfd pdpqkvlqgv idmknavign nkqkanlivl
       61 gavprllyll qqetsstelk tecavvlgsl amgtennvks lldchiipal lqgllspdlk
      121 fieaclrclr tiftspvtpe ellytgpdhq tilfnhgavq niahlltsls ykvrmqalkc
      181 fsvlafenpq vsmtlvnvlv dgellpqifv kmlqrdkpie mqltsakclt ymcragairt
      241 ddncivlktl pclvrmcske rlleervega etlayliepd velqriasit dhliamlady
      301 fkypssvsai tdikrldhdl khahelrqaa fklyaslgan dedirkkiie tenmmdrivt
      361 glsessvkvr laavrclhsl srsvqqlrts fqdhavwkpl mkvlqnapde ilvvassmlc
      421 nlllefspsk epilesgave llcgltqsen palrvngiwa lmnmafqaeq kikadilrsl
      481 steqlfrlls dsdlnvlmkt lgllrnllst rphidkimst hgkqimqavt lilegehnie
      541 vkeqtlcila niadgttakd limtnddilq kikyymghsh vklqlaamfc isnliwneee
      601 gsqerqdklr dmgivdilhk lsqspdsnlc dkakmalqqy la
//
LOCUS       NP_002044                592 aa            linear   PRI 20-NOV-2025
DEFINITION  guanylate-binding protein 1 [Homo sapiens].
ACCESSION   NP_002044
VERSION     NP_002044.2
DBSOURCE    REFSEQ: accession NM_002053.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Gu,T., Qu,S., Zhang,J., Ying,Q., Zhang,X., Lv,Y., Liu,R., Feng,Y.,
            Wang,F. and Wu,X.
  TITLE     Guanylate-binding protein 1 inhibits Hantaan virus infection by
            restricting virus entry
  JOURNAL   J Med Virol 96 (6), e29730 (2024)
   PUBMED   38860570
  REMARK    GeneRIF: Guanylate-binding protein 1 inhibits Hantaan virus
            infection by restricting virus entry.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Yu,S., Li,Y., Feng,W., Zeng,J., Cui,X., Zhou,S. and Zhang,P.
  TITLE     GBP1 promotes cutaneous squamous cell carcinoma proliferation and
            invasion through activation of STAT3 by SP1
  JOURNAL   Exp Dermatol 33 (6), e15112 (2024)
   PUBMED   38840385
  REMARK    GeneRIF: GBP1 promotes cutaneous squamous cell carcinoma
            proliferation and invasion through activation of STAT3 by SP1.
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Xu,M., Lin,M.C. and Li,Z.H.
  TITLE     Interferon-gamma-induced GBP1 is an inhibitor of human
            papillomavirus 18
  JOURNAL   BMC Womens Health 24 (1), 240 (2024)
   PUBMED   38622605
  REMARK    GeneRIF: Interferon-gamma-induced GBP1 is an inhibitor of human
            papillomavirus 18.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Bender,D., Koulouri,A., Wen,X., Glitscher,M., Schollmeier,A.,
            Fernandes da Costa,L., Murra,R.O., Carra,G.P., Haberger,V.,
            Praefcke,G.J.K. and Hildt,E.
  TITLE     Guanylate-binding protein 1 acts as a pro-viral factor for the life
            cycle of hepatitis C virus
  JOURNAL   PLoS Pathog 20 (2), e1011976 (2024)
   PUBMED   38315728
  REMARK    GeneRIF: Guanylate-binding protein 1 acts as a pro-viral factor for
            the life cycle of hepatitis C virus.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Saunders,N.A., Smith,R.J. and Jetten,A.M.
  TITLE     Regulation of guanylate-binding protein expression in
            interferon-gamma-treated human epidermal keratinocytes and squamous
            cell carcinoma cells
  JOURNAL   J Invest Dermatol 112 (6), 977-983 (1999)
   PUBMED   10383748
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Nantais,D.E., Schwemmle,M., Stickney,J.T., Vestal,D.J. and
            Buss,J.E.
  TITLE     Prenylation of an interferon-gamma-induced GTP-binding protein: the
            human guanylate binding protein, huGBP1
  JOURNAL   J Leukoc Biol 60 (3), 423-431 (1996)
   PUBMED   8830800
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Strehlow,I., Lohmann-Matthes,M.L. and Decker,T.
  TITLE     The interferon-inducible GBP1 gene: structure and mapping to human
            chromosome 1
  JOURNAL   Gene 144 (2), 295-299 (1994)
   PUBMED   7518790
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Schwemmle,M. and Staeheli,P.
  TITLE     The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is
            a GTPase that converts GTP to GMP
  JOURNAL   J Biol Chem 269 (15), 11299-11305 (1994)
   PUBMED   7512561
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Cheng,Y.S., Patterson,C.E. and Staeheli,P.
  TITLE     Interferon-induced guanylate-binding proteins lack an N(T)KXD
            consensus motif and bind GMP in addition to GDP and GTP
  JOURNAL   Mol Cell Biol 11 (9), 4717-4725 (1991)
   PUBMED   1715024
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK291783.1, CB164272.1, BF058809.1 and CD676970.1.
            
            On Feb 1, 2008 this sequence version replaced NP_002044.1.
            
            Summary: Guanylate binding protein expression is induced by
            interferon. Guanylate binding proteins are characterized by their
            ability to specifically bind guanine nucleotides (GMP, GDP, and
            GTP) and are distinguished from the GTP-binding proteins by the
            presence of 2 binding motifs rather than 3. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M55542.1, AK291783.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370473.5/ ENSP00000359504.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.2"
     Protein         1..592
                     /product="guanylate-binding protein 1"
                     /note="guanylate binding protein 1, interferon-inducible,
                     67kDa; interferon-induced guanylate-binding protein 1;
                     GBP-1; huGBP-1; GTP-binding protein 1; guanine
                     nucleotide-binding protein 1"
                     /calculated_mol_wt=67800
     mat_peptide     1..589
                     /product="Guanylate-binding protein 1. /id=PRO_0000190963"
                     /note="propagated from UniProtKB/Swiss-Prot (P32455.2)"
                     /calculated_mol_wt=67630
     Region          1..311
                     /region_name="GTPase domain (Globular).
                     /evidence=ECO:0000305|PubMed:10676968"
                     /note="propagated from UniProtKB/Swiss-Prot (P32455.2)"
     Region          18..282
                     /region_name="GBP"
                     /note="Guanylate-binding protein, N-terminal domain;
                     pfam02263"
                     /db_xref="CDD:460516"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PIM1.
                     /evidence=ECO:0000269|PubMed:37797010; propagated from
                     UniProtKB/Swiss-Prot (P32455.2)"
     Region          284..580
                     /region_name="GBP_C"
                     /note="Guanylate-binding protein, C-terminal domain;
                     pfam02841"
                     /db_xref="CDD:460721"
     Site            589
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000305|PubMed:8830800; propagated from
                     UniProtKB/Swiss-Prot (P32455.2)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PIM1.
                     /evidence=ECO:0000269|PubMed:37797010; propagated from
                     UniProtKB/Swiss-Prot (P32455.2)"
     CDS             1..592
                     /gene="GBP1"
                     /gene_synonym="hGBP1"
                     /coded_by="NM_002053.3:69..1847"
                     /db_xref="CCDS:CCDS718.1"
                     /db_xref="GeneID:2633"
                     /db_xref="HGNC:HGNC:4182"
                     /db_xref="MIM:600411"
ORIGIN      
        1 maseihmtgp mclientngr lmanpealki lsaitqpmvv vaivglyrtg ksylmnklag
       61 kkkgfslgst vqshtkgiwm wcvphpkkpg hilvlldteg lgdvekgdnq ndswifalav
      121 llsstfvyns igtinqqamd qlyyvtelth rirsksspde nenevedsad fvsffpdfvw
      181 tlrdfsldle adgqpltpde yltyslklkk gtsqkdetfn lprlcirkff pkkkcfvfdr
      241 pvhrrklaql eklqdeeldp efvqqvadfc syifsnsktk tlsggiqvng prleslvlty
      301 vnaissgdlp cmenavlala qiensaavqk aiahyeqqmg qkvqlptetl qelldlhrds
      361 ereaievfir ssfkdvdhlf qkelaaqlek krddfckqnq eassdrcsal lqvifsplee
      421 evkagiyskp ggyrlfvqkl qdlkkkyyee prkgiqaeei lqtylkskes mtdailqtdq
      481 tltekekeie vervkaesaq asakmlqemq rkneqmmeqk ersyqehlkq ltekmendrv
      541 qllkeqertl alklqeqeql lkegfqkesr imkneiqdlq tkmrrrkact is
//
LOCUS       NP_055787                676 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosome quality control complex subunit TCF25 [Homo sapiens].
ACCESSION   NP_055787
VERSION     NP_055787.1
DBSOURCE    REFSEQ: accession NM_014972.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Dos Santos,O.A.L., Carneiro,R.L., Requiao,R.D., Ribeiro-Alves,M.,
            Domitrovic,T. and Palhano,F.L.
  TITLE     Transcriptional profile of ribosome-associated quality control
            components and their associated phenotypes in mammalian cells
  JOURNAL   Sci Rep 14 (1), 1439 (2024)
   PUBMED   38228636
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Filbeck,S., Cerullo,F., Pfeffer,S. and Joazeiro,C.A.P.
  TITLE     Ribosome-associated quality-control mechanisms from bacteria to
            humans
  JOURNAL   Mol Cell 82 (8), 1451-1466 (2022)
   PUBMED   35452614
  REMARK    Review article
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Steen,H. and Lindholm,D.
  TITLE     Nuclear localized protein-1 (Nulp1) increases cell death of human
            osteosarcoma cells and binds the X-linked inhibitor of apoptosis
            protein
  JOURNAL   Biochem Biophys Res Commun 366 (2), 432-437 (2008)
   PUBMED   18068114
  REMARK    GeneRIF: These results indicate that Nulp1 plays a role in cell
            death control and may influence tumor growth.
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Cai,Z., Wang,Y., Yu,W., Xiao,J., Li,Y., Liu,L., Zhu,C., Tan,K.,
            Deng,Y., Yuan,W., Liu,M. and Wu,X.
  TITLE     hnulp1, a basic helix-loop-helix protein with a novel
            transcriptional repressive domain, inhibits transcriptional
            activity of serum response factor
  JOURNAL   Biochem Biophys Res Commun 343 (3), 973-981 (2006)
   PUBMED   16574069
  REMARK    GeneRIF: hnulp1 may act as a novel transcriptional repressor in
            serum response factor signaling pathways.
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Olsson,M., Durbeej,M., Ekblom,P. and Hjalt,T.
  TITLE     Nulp1, a novel basic helix-loop-helix protein expressed broadly
            during early embryonic organogenesis and prominently in developing
            dorsal root ganglia
  JOURNAL   Cell Tissue Res 308 (3), 361-370 (2002)
   PUBMED   12107429
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI913551.1 and BC011884.2.
            
            Summary: TCF25 is a member of the basic helix-loop-helix (bHLH)
            family of transcription factors that are important in embryonic
            development (Steen and Lindholm, 2008 [PubMed 18068114]).[supplied
            by OMIM, Sep 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1091791.1,
                                           SRR1660809.32437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263346.13/ ENSP00000263346.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..676
                     /product="ribosome quality control complex subunit TCF25"
                     /note="TCF-25; nuclear localized protein 1; transcription
                     factor 25 (basic helix-loop-helix)"
                     /calculated_mol_wt=76536
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ70.1)"
     Region          85..147
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQ70.1)"
     Region          248..588
                     /region_name="Tcf25"
                     /note="Transcriptional repressor TCF25; pfam04910"
                     /db_xref="CDD:461476"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BQ70.1)"
     CDS             1..676
                     /gene="TCF25"
                     /gene_synonym="FKSG26; hKIAA1049; Hulp1; NULP1; PRO2620"
                     /coded_by="NM_014972.3:77..2107"
                     /db_xref="CCDS:CCDS10987.1"
                     /db_xref="GeneID:22980"
                     /db_xref="HGNC:HGNC:29181"
                     /db_xref="MIM:612326"
ORIGIN      
        1 msrralrrlr geqrgqeplg pgalhfdlrd dddaeeegpk relgvrrpgg agkegvrvnn
       61 rfeliniddl eddpvvnger sgcaltdava pgnkgrgqrg ntesktdgdd tetvpseqsh
      121 asgklrkkkk kqknkksstg easengledi drilerieds tglnrpgpap lssrkhvlyv
      181 ehrhlnpdte lkryfgarai lgeqrprqrq rvypkctwlt tpkstwprys kpglsmrlle
      241 skkglsffaf ehseeyqqaq hkflvavesm epnnivvllq tspyhvdsll qlsdacrfqe
      301 dqemardlve ralysmecaf hplfsltsga crldyrrpen rsfylalykq msflekrgcp
      361 rtaleyckli lslepdedpl cmlllidhla lrarnyeyli rlfqeweahr nlsqlpnfaf
      421 svplayflls qqtdlpeceq ssarqkasll iqqaltmfpg vllpllescs vrpdasvssh
      481 rffgpnaeis qppalsqlvn lylgrshflw kepatmswle envhevlqav dagdpaveac
      541 enrrkvlyqr aprnihrhvi lseikeavaa lppdvttqsv mgfdplppsd tiysyvrper
      601 lspishgnti alffrsllpn ytmegerpee gvagglnrnq glnrlmlavr dmmanfhlnd
      661 leapheddae gegewd
//
LOCUS       NP_001356513             642 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform u [Homo sapiens].
ACCESSION   NP_001356513 XP_016881437
VERSION     NP_001356513.1
DBSOURCE    REFSEQ: accession NM_001369584.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 642)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 642)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 642)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 642)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 642)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 642)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 642)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 642)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 642)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 642)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881437.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.1049467.1,
                                           SRR1660807.26423.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..642
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..642
                     /product="transcription factor 4 isoform u"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68352
     Region          533..617
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(541,545,547..549,551,556,577..578)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(554..555,558..559,561..562,565,569,579,582,586,589,
                     592..597)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..642
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369584.1:516..2444"
                     /note="isoform u is encoded by transcript variant 44"
                     /db_xref="CCDS:CCDS86672.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqs llggdmdmgn pgtlsptkpg
      121 sqyyqyssnn prrrplhssa mevqtkkvrk vppglpssvy apsastadyn rdspgypssk
      181 patstfpssf fmqdghhssd pwssssgmnq pgyagmlgns shipqsssyc slhpherlsy
      241 pshssadins slppmstfhr sgtnhystss ctppangtds imanrgsgaa gssqtgdalg
      301 kalasiyspd htnnsfssnp stpvgsppsl sagtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit snnddedltp eqkaereker
      541 rmannarerl rvrdineafk elgrmvqlhl ksdkpqtkll ilhqavavil sleqqvrern
      601 lnpkaaclkr reeekvssep pplslagphp gmgdasnhmg qm
//
LOCUS       NP_003962               1307 aa            linear   PRI 20-NOV-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 4 isoform 3 [Homo
            sapiens].
ACCESSION   NP_003962
VERSION     NP_003962.3
DBSOURCE    REFSEQ: accession NM_003971.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1307)
  AUTHORS   Bassey-Archibong,B.I., Rajendra Chokshi,C., Aghaei,N.,
            Kieliszek,A.M., Tatari,N., McKenna,D., Singh,M., Kalpana
            Subapanditha,M., Parmar,A., Mobilio,D., Savage,N., Lam,F.,
            Tokar,T., Provias,J., Lu,Y., Chafe,S.C., Swanton,C., Hynds,R.E.,
            Venugopal,C. and Singh,S.K.
  TITLE     An HLA-G/SPAG9/STAT3 axis promotes brain metastases
  JOURNAL   Proc Natl Acad Sci U S A 120 (8), e2205247120 (2023)
   PUBMED   36780531
  REMARK    GeneRIF: An HLA-G/SPAG9/STAT3 axis promotes brain metastases.
REFERENCE   2  (residues 1 to 1307)
  AUTHORS   Ramadan,R.A., Morsy,H., Samir,M., Shamseya,M., Shalaby,M. and
            El-Attar,E.A.
  TITLE     Significance of cancer testis-associated antigens (SPAG9 and
            FBXO39) in colon cancer
  JOURNAL   Indian J Cancer 59 (3), 394-401 (2022)
   PUBMED   34380828
  REMARK    GeneRIF: Significance of cancer testis-associated antigens (SPAG9
            and FBXO39) in colon cancer.
REFERENCE   3  (residues 1 to 1307)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1307)
  AUTHORS   Del Sarto,J., Gerlt,V., Friedrich,M.E., Anhlan,D., Wixler,V.,
            Teixeira,M.M., Boergeling,Y. and Ludwig,S.
  TITLE     Phosphorylation of JIP4 at S730 Presents Antiviral Properties
            against Influenza A Virus Infection
  JOURNAL   J Virol 95 (20), e0067221 (2021)
   PUBMED   34319782
  REMARK    GeneRIF: Phosphorylation of JIP4 at S730 Presents Antiviral
            Properties against Influenza A Virus Infection.
REFERENCE   5  (residues 1 to 1307)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1307)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   7  (residues 1 to 1307)
  AUTHORS   Yasuoka,H., Ihn,H., Medsger,T.A. Jr., Hirakata,M., Kawakami,Y.,
            Ikeda,Y. and Kuwana,M.
  TITLE     A novel protein highly expressed in testis is overexpressed in
            systemic sclerosis fibroblasts and targeted by autoantibodies
  JOURNAL   J Immunol 171 (12), 6883-6890 (2003)
   PUBMED   14662895
  REMARK    GeneRIF: Testicular antigen PHET is an auutoantigen recognized by
            sera from systemic sclerosis (SSc) patients with extensive fibrotic
            changes; the autoantibody response to PHET is induced by ectopic
            overexpression of PHET in dermal fibroblasts of SSc patients.
REFERENCE   8  (residues 1 to 1307)
  AUTHORS   Lee,C.M., Onesime,D., Reddy,C.D., Dhanasekaran,N. and Reddy,E.P.
  TITLE     JLP: A scaffolding protein that tethers JNK/p38MAPK signaling
            modules and transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14189-14194 (2002)
   PUBMED   12391307
REFERENCE   9  (residues 1 to 1307)
  AUTHORS   Ichijo,H.
  TITLE     From receptors to stress-activated MAP kinases
  JOURNAL   Oncogene 18 (45), 6087-6093 (1999)
   PUBMED   10557099
  REMARK    Review article
REFERENCE   10 (residues 1 to 1307)
  AUTHORS   Shankar,S., Mohapatra,B. and Suri,A.
  TITLE     Cloning of a novel human testis mRNA specifically expressed in
            testicular haploid germ cells, having unique palindromic sequences
            and encoding a leucine zipper dimerization motif
  JOURNAL   Biochem Biophys Res Commun 243 (2), 561-565 (1998)
   PUBMED   9480848
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005839.1, AK091921.1,
            AY850123.1 and AC005920.1.
            
            On Dec 31, 2002 this sequence version replaced NP_003962.2.
            
            Summary: This gene encodes a member of the cancer testis antigen
            gene family. The encoded protein functions as a scaffold protein
            that structurally organizes mitogen-activated protein kinases and
            mediates c-Jun-terminal kinase signaling. This protein also binds
            to kinesin-1 and may be involved in microtubule-based membrane
            transport. This protein may play a role in tumor growth and
            development. Alternate splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3) lacks an in-frame coding exon
            in the coding region, compared to variant 1. The resulting isoform
            (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY850123.1, SRR9304718.211368.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.33"
     Protein         1..1307
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     4 isoform 3"
                     /note="sperm surface protein; cancer/testis antigen 89;
                     JNK/SAPK-associated protein; JNK interacting protein;
                     c-Jun NH2-terminal kinase-associated leucine zipper
                     protein; Max-binding protein; C-Jun-amino-terminal
                     kinase-interacting protein 4; proliferation-inducing gene
                     6; lung cancer oncogene 4; sunday driver 1; protein highly
                     expressed in testis; human lung cancer oncogene 6 protein;
                     mitogen-activated protein kinase 8-interacting protein 4;
                     C-Jun N-terminal kinase protein-associated leucine-zipper
                     protein"
                     /calculated_mol_wt=144551
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          24..178
                     /region_name="Jnk-SapK_ap_N"
                     /note="JNK_SAPK-associated protein-1; pfam09744"
                     /db_xref="CDD:462875"
     Region          66..349
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            238
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q58A65; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q58A65; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          392..>447
                     /region_name="JIP_LZII"
                     /note="JNK-interacting protein leucine zipper II;
                     pfam16471"
                     /db_xref="CDD:465127"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          <435..>628
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          459..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          549..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            714
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          840..892
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Region          938..>1292
                     /region_name="WD40_2"
                     /note="WD40 repeated domain; pfam19056"
                     /db_xref="CDD:465964"
     Site            1174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     Region          1225..1252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60271.4)"
     Site            1250
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60271.4)"
     CDS             1..1307
                     /gene="SPAG9"
                     /gene_synonym="CT89; HLC-6; HLC4; HLC6; JIP-4; JIP4; JLP;
                     PHET; PIG6"
                     /coded_by="NM_003971.6:213..4136"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11577.1"
                     /db_xref="GeneID:9043"
                     /db_xref="HGNC:HGNC:14524"
                     /db_xref="MIM:605430"
ORIGIN      
        1 meledgvvyq eepggsgavm servsglags iyreferlig rydeevvkel mplvvavlen
       61 ldsvfaqdqe hqvelellrd dneqlitqye rekalrkhae ekfiefedsq eqekkdlqtr
      121 veslesqtrq lelkaknyad qisrleerea elkkeynalh qrhtemihny mehlertklh
      181 qlsgsdqles tahsrirker pislgifplp agdglltpda qkggetpgse qwkfqelsqp
      241 rshtslkdel sdvsqggska ttpastansd vatiptdtpl keenegfvkv tdapnkseis
      301 khievqvaqe trnvstgsae neeksevqai iestpeldmd kdlsgykgss tptkgienka
      361 fdrnteslfe elssagsgli gdvdegadll gmgrevenli lentqlletk nalnivkndl
      421 iakvdeltce kdvlqgelea vkqaklklee knreleeelr karaeaedar qkakddddsd
      481 iptaqrkrft rvemarvlme rnqykerlme lqeavrwtem irasrenpam qekkrssiwq
      541 ffsrlfssss nttkkpeppv nlkynaptsh vtpsvkkrss tlsqlpgdks kafdflseet
      601 easlasrreq kreqyrqvka hvqkedgrvq afgwslpqky kqvtngqgen kmknlpvpvy
      661 lrpldekdts mklwcavgvn lsggktrdgg svvgasvfyk dvagldtegs kqrsasqssl
      721 dkldqelkeq qkelknqeel sslvwictst hsatkvliid avqpgnilds ftvcnshvlc
      781 iasvpgaret dypagedlse sgqvdkaslc gsmtsnssae tdsllggitv vgcsaegvtg
      841 aatspstnga spvmdkppem eaensevden vptaeeatea tegnagsaed tvdisqtgvy
      901 tehvftdplg vqipedlspv yqssndsday kdqisvlpne qdlvreeaqk mssllptmwl
      961 gaqngclyvh ssvaqwrkcl hsiklkdsil sivhvkgivl valadgtlai fhrgvdgqwd
     1021 lsnyhlldlg rphhsircmt vvhdkvwcgy rnkiyvvqpk amkieksfda hprkesqvrq
     1081 lawvgdgvwv sirldstlrl yhahtyqhlq dvdiepyvsk mlgtgklgfs fvritalmvs
     1141 cnrlwvgtgn gviisiplte tnktsgvpgn rpgsvirvyg densdkvtpg tfipycsmah
     1201 aqlcfhghrd avkffvavpg qvispqssss gtdltgdkag psaqepgsqt plksmlvisg
     1261 gegyidfrmg deggesellg edlplepsvt kaershlivw qvmygne
//
LOCUS       NP_001121362             281 aa            linear   PRI 20-NOV-2025
DEFINITION  maspardin isoform b [Homo sapiens].
ACCESSION   NP_001121362
VERSION     NP_001121362.1
DBSOURCE    REFSEQ: accession NM_001127890.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zhou,P., Yao,W., Liu,L., Yan,Q., Chen,X., Wei,X., Ding,S., Lv,Z.
            and Zhu,F.
  TITLE     SPG21, a potential oncogene targeted by miR-128-3p, amplifies
            HBx-induced carcinogenesis and chemoresistance via activation of
            TRPM7-mediated JNK pathway in hepatocellular carcinoma
  JOURNAL   Cell Oncol (Dordr) 47 (5), 1757-1778 (2024)
   PUBMED   38753154
  REMARK    GeneRIF: SPG21, a potential oncogene targeted by miR-128-3p,
            amplifies HBx-induced carcinogenesis and chemoresistance via
            activation of TRPM7-mediated JNK pathway in hepatocellular
            carcinoma.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Hanna,M.C. and Blackstone,C.
  TITLE     Interaction of the SPG21 protein ACP33/maspardin with the aldehyde
            dehydrogenase ALDH16A1
  JOURNAL   Neurogenetics 10 (3), 217-228 (2009)
   PUBMED   19184135
  REMARK    GeneRIF: Data report that maspardin localizes prominently to
            cytoplasm as well as to membranes, possibly at trans-Golgi
            network/late endosomal compartments, and that maspardin interacts
            with the aldehyde dehydrogenase ALDH16A1.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Simpson,M.A., Cross,H., Proukakis,C., Pryde,A., Hershberger,R.,
            Chatonnet,A., Patton,M.A. and Crosby,A.H.
  TITLE     Maspardin is mutated in mast syndrome, a complicated form of
            hereditary spastic paraplegia associated with dementia
  JOURNAL   Am J Hum Genet 73 (5), 1147-1156 (2003)
   PUBMED   14564668
  REMARK    GeneRIF: frameshift results in the premature termination of the
            encoded product, which is designated 'maspardin' (Mast syndrome,
            spastic paraplegia, autosomal recessive with dementia)
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Zeitlmann,L., Sirim,P., Kremmer,E. and Kolanus,W.
  TITLE     Cloning of ACP33 as a novel intracellular ligand of CD4
  JOURNAL   J Biol Chem 276 (12), 9123-9132 (2001)
   PUBMED   11113139
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Cross,H.E. and McKusick,V.A.
  TITLE     The mast syndrome. A recessively inherited form of presenile
            dementia with motor disturbances
  JOURNAL   Arch Neurol 16 (1), 1-13 (1967)
   PUBMED   6024251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP268459.1, AK301362.1,
            BC000244.1, BI259651.1 and AI161152.1.
            
            Summary: The protein encoded by this gene binds to the hydrophobic
            C-terminal amino acids of CD4 which are involved in repression of T
            cell activation. The interaction with CD4 is mediated by the
            noncatalytic alpha/beta hydrolase fold domain of this protein. It
            is thus proposed that this gene product modulates the stimulatory
            activity of CD4. Mutations in this gene are associated with
            autosomal recessive spastic paraplegia 21 (SPG21), also known as
            mast syndrome. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The resulting
            isoform (b) lacks an internal segment and is shorter, compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301362.1, SRR7346977.98287.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..281
                     /product="maspardin isoform b"
                     /note="acid cluster protein 33; spastic paraplegia 21
                     (autosomal recessive, Mast syndrome); maspardin; SPG21,
                     maspardin"
                     /calculated_mol_wt=31454
     Region          <59..>138
                     /region_name="alpha/beta hydrolases"
                     /note="A functionally diverse superfamily containing
                     proteases, lipases, peroxidases, esterases, epoxide
                     hydrolases and dehalogenases. The catalytic apparatus
                     typically involves three residues (catalytic triad): a
                     serine, a glutamate or aspartate and a...; cl21494"
                     /db_xref="CDD:473884"
     CDS             1..281
                     /gene="SPG21"
                     /gene_synonym="ABHD21; ACP33; BM-019; GL010; MAST"
                     /coded_by="NM_001127890.5:275..1120"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45279.1"
                     /db_xref="GeneID:51324"
                     /db_xref="HGNC:HGNC:20373"
                     /db_xref="MIM:608181"
ORIGIN      
        1 mgeikvspdy nwfrgtvplk kiivddddsk iwslydagpr sircpliflp pvsgtadvff
       61 rqilaltgwg yrviavhlfg aslggflaqk faeythkspr vhslilcnsf sdtsifnqtw
      121 tansfwlmpa fmlkkivlgn fssgpvdpmm adaidfmvdr leslgqsela srltlncqns
      181 yvephkirdi pvtimdvfdq salsteakee myklypnarr ahlktggnfp ylcrsaevnl
      241 yvqihllqfh gtkyaaidps mvsaeelevq kgslgisqee q
//
LOCUS       NP_115664                318 aa            linear   PRI 20-NOV-2025
DEFINITION  UAP56-interacting factor isoform 1 [Homo sapiens].
ACCESSION   NP_115664
VERSION     NP_115664.2
DBSOURCE    REFSEQ: accession NM_032288.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Tunnicliffe,R.B., Tian,X., Storer,J., Sandri-Goldin,R.M. and
            Golovanov,A.P.
  TITLE     Overlapping motifs on the herpes viral proteins ICP27 and ORF57
            mediate interactions with the mRNA export adaptors ALYREF and UIF
  JOURNAL   Sci Rep 8 (1), 15005 (2018)
   PUBMED   30301920
  REMARK    GeneRIF: In both ORF57 and ICP27 the interaction sites for ALYREF
            and UIF partially overlap, suggestive of mutually exclusive
            binding. The data provide a map of the binding sites responsible
            for promoting herpes virus mRNA export, enabling future studies to
            accurately probe these interactions and reveal the functional
            consequences for UIF and ALYREF redundancy
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Jackson,B.R., Boyne,J.R., Noerenberg,M., Taylor,A.,
            Hautbergue,G.M., Walsh,M.J., Wheat,R., Blackbourn,D.J., Wilson,S.A.
            and Whitehouse,A.
  TITLE     An interaction between KSHV ORF57 and UIF provides mRNA-adaptor
            redundancy in herpesvirus intronless mRNA export
  JOURNAL   PLoS Pathog 7 (7), e1002138 (2011)
   PUBMED   21814512
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Hautbergue,G.M., Hung,M.L., Walsh,M.J., Snijders,A.P., Chang,C.T.,
            Jones,R., Ponting,C.P., Dickman,M.J. and Wilson,S.A.
  TITLE     UIF, a New mRNA export adaptor that works together with REF/ALY,
            requires FACT for recruitment to mRNA
  JOURNAL   Curr Biol 19 (22), 1918-1924 (2009)
   PUBMED   19836239
  REMARK    GeneRIF: FYTTD1 was named UIF for UAP56 Interacting Factor. UIF is
            an mRNA export adaptor, recruited to mRNA by SSRP1 of the FACT
            complex. It also binds mRNA and NXF1. It is required for efficient
            nuclear export of mRNA in vertebrates and other animals.
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Pope,S.N. and Lee,I.R.
  TITLE     Yeast two-hybrid identification of prostatic proteins interacting
            with human sex hormone-binding globulin
  JOURNAL   J Steroid Biochem Mol Biol 94 (1-3), 203-208 (2005)
   PUBMED   15862967
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC035006.2, AJ344094.1, H97483.1 and AC055764.23.
            
            On Feb 20, 2004 this sequence version replaced NP_115664.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.114493.1,
                                           SRR1803616.249868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241502.9/ ENSP00000241502.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..318
                     /product="UAP56-interacting factor isoform 1"
                     /note="UAP56-interacting factor; protein 40-2-3;
                     forty-two-three domain-containing protein 1"
                     /calculated_mol_wt=35687
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QD9.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     Region          10..318
                     /region_name="FYTT"
                     /note="Forty-two-three protein; pfam07078"
                     /db_xref="CDD:462082"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91Z49; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     Region          26..44
                     /region_name="UAP56-binding motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QD9.3)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     Region          79..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QD9.3)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QD9.3)"
     CDS             1..318
                     /gene="FYTTD1"
                     /gene_synonym="UIF"
                     /coded_by="NM_032288.7:90..1046"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3329.1"
                     /db_xref="GeneID:84248"
                     /db_xref="HGNC:HGNC:25407"
                     /db_xref="MIM:616933"
ORIGIN      
        1 mnrfgtrlvg atatsspppk arsnenldki dmslddiikl nrkegkkqnf prlnrrllqq
       61 sgaqqfrmrv rwgiqqnsgf gktslnrrgr vmpgkrrpng vitglaarkt tgirkgispm
      121 nrpplsdkni eqyfpvlkrk anllrqnegq rkpvavlkrp sqlsrknnip anftrsgnkl
      181 nhqkdtrqat flfrrglkvq aqlnteqlld dvvakrtrqw rtsttnggil tvsidnpgav
      241 qcpvtqkprl trtavpsflt kreqsdvkkv pkgvplqfdi nsvgkqtgmt lnerfgilke
      301 qratltynkg gsrfvtvg
//
LOCUS       NP_612452                278 aa            linear   PRI 20-NOV-2025
DEFINITION  HAUS augmin-like complex subunit 1 [Homo sapiens].
ACCESSION   NP_612452 XP_943224
VERSION     NP_612452.1
DBSOURCE    REFSEQ: accession NM_138443.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Liu,S., Yu,Y., Xu,J., Wang,Y. and Li,D.
  TITLE     Single-cell and bulk RNA-sequencing reveals mitosis-involved gene
            HAUS1 is a promising indicator for predicting prognosis and immune
            responses in prostate adenocarcinoma (PRAD)
  JOURNAL   Cell Biol Int 48 (8), 1169-1184 (2024)
   PUBMED   38818762
  REMARK    GeneRIF: Single-cell and bulk RNA-sequencing reveals
            mitosis-involved gene HAUS1 is a promising indicator for predicting
            prognosis and immune responses in prostate adenocarcinoma (PRAD).
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Lawo,S., Bashkurov,M., Mullin,M., Ferreria,M.G., Kittler,R.,
            Habermann,B., Tagliaferro,A., Poser,I., Hutchins,J.R., Hegemann,B.,
            Pinchev,D., Buchholz,F., Peters,J.M., Hyman,A.A., Gingras,A.C. and
            Pelletier,L.
  TITLE     HAUS, the 8-subunit human Augmin complex, regulates centrosome and
            spindle integrity
  JOURNAL   Curr Biol 19 (10), 816-826 (2009)
   PUBMED   19427217
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Uehara,R., Nozawa,R.S., Tomioka,A., Petry,S., Vale,R.D., Obuse,C.
            and Goshima,G.
  TITLE     The augmin complex plays a critical role in spindle microtubule
            generation for mitotic progression and cytokinesis in human cells
  JOURNAL   Proc Natl Acad Sci U S A 106 (17), 6998-7003 (2009)
   PUBMED   19369198
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Goshima,G., Mayer,M., Zhang,N., Stuurman,N. and Vale,R.D.
  TITLE     Augmin: a protein complex required for centrosome-independent
            microtubule generation within the spindle
  JOURNAL   J Cell Biol 181 (3), 421-429 (2008)
   PUBMED   18443220
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Einarson,M.B., Cukierman,E., Compton,D.A. and Golemis,E.A.
  TITLE     Human enhancer of invasion-cluster, a coiled-coil protein required
            for passage through mitosis
  JOURNAL   Mol Cell Biol 24 (9), 3957-3971 (2004)
   PUBMED   15082789
  REMARK    GeneRIF: These results place human enhancer of invasion-cluster as
            a novel regulator of spindle function and integrity during the
            metaphase-anaphase transition.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC014003.2.
            
            On Mar 4, 2006 this sequence version replaced XP_943224.1.
            
            Summary: HAUS1 is 1 of 8 subunits of the 390-kD human augmin
            complex, or HAUS complex. The augmin complex was first identified
            in Drosophila, and its name comes from the Latin verb 'augmentare,'
            meaning 'to increase.' The augmin complex is a microtubule-binding
            complex involved in microtubule generation within the mitotic
            spindle and is vital to mitotic spindle assembly (Goshima et al.,
            2008 [PubMed 18443220]; Uehara et al., 2009 [PubMed
            19369198]).[supplied by OMIM, Jun 2010].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and is protein-coding.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014003.2, SRR1163658.312301.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282058.11/ ENSP00000282058.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..278
                     /product="HAUS augmin-like complex subunit 1"
                     /note="coiled-coil domain containing 5 (spindle
                     associated); enhancer of invasion-cluster; coiled-coil
                     domain-containing protein 5"
                     /calculated_mol_wt=31732
     CDS             1..278
                     /gene="HAUS1"
                     /gene_synonym="CCDC5; HEI-C; HEIC; HsT1461"
                     /coded_by="NM_138443.4:28..864"
                     /db_xref="CCDS:CCDS11928.1"
                     /db_xref="GeneID:115106"
                     /db_xref="HGNC:HGNC:25174"
                     /db_xref="MIM:608775"
ORIGIN      
        1 mepqeeretq vaawlkkifg dhpipqyevn prtteilhhl sernrvrdrd vylviedlkq
       61 kaseyeseak ylqdllmesv nfspanlsst gsrylnalvd savaletkdt slasfipavn
      121 dltsdlfrtk skseeikiel ekleknltat lvlekclqed vkkaelhlst erakvdnrrq
      181 nmdflkakse efrfgikaae eqlsargmda slshqslval seklarlkqq tiplkkkles
      241 yldlmpnpsl aqvkieeakr eldsieaelt rrvdmmel
//
LOCUS       NP_001268366             368 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasomal ubiquitin receptor ADRM1 isoform 2 [Homo sapiens].
ACCESSION   NP_001268366
VERSION     NP_001268366.1
DBSOURCE    REFSEQ: accession NM_001281437.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Shao,Z., Wang,Y., He,Y., Zhang,C., Zhao,Y., Zhang,M., Li,Q. and
            Wang,J.
  TITLE     The high expression of ADRM1 in hepatocellular carcinoma is closely
            related to tumor immune infiltration and is regulated by
            miR-891a-5p
  JOURNAL   Sci Rep 14 (1), 14002 (2024)
   PUBMED   38890391
  REMARK    GeneRIF: The high expression of ADRM1 in hepatocellular carcinoma
            is closely related to tumor immune infiltration and is regulated by
            miR-891a-5p.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Osei-Amponsa,V., Chandravanshi,M., Lu,X., Magidson,V., Das,S.,
            Andresson,T., Dyba,M., Sabbasani,V.R., Swenson,R.E., Fromont,C.,
            Shrestha,B., Zhao,Y., Clapp,M.E., Chari,R. and Walters,K.J.
  TITLE     hRpn13 shapes the proteome and transcriptome through epigenetic
            factors HDAC8, PADI4, and transcription factor NF-kappaB p50
  JOURNAL   Mol Cell 84 (3), 522-537 (2024)
   PUBMED   38151017
  REMARK    GeneRIF: hRpn13 shapes the proteome and transcriptome through
            epigenetic factors HDAC8, PADI4, and transcription factor NF-kappaB
            p50.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Zhu,D. and Zhong,Q.
  TITLE     Potential of adhesion-regulating molecule 1 (ADRM1) as a biomarker
            for patients with renal clear-cell carcinoma or papillary-cell
            carcinoma
  JOURNAL   Asian J Surg 46 (10), 4666-4668 (2023)
   PUBMED   37268471
  REMARK    GeneRIF: Potential of adhesion-regulating molecule 1 (ADRM1) as a
            biomarker for patients with renal clear-cell carcinoma or
            papillary-cell carcinoma.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Xiao,J., Xie,Y., Duan,Q., Liu,T., Ye,R., Duan,X., Le,Z., Deng,N.
            and Liu,F.
  TITLE     LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models
  JOURNAL   Int Heart J 64 (4), 750-758 (2023)
   PUBMED   37518356
  REMARK    GeneRIF: LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models.
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Jorgensen,J.P., Lauridsen,A.M., Kristensen,P., Dissing,K.,
            Johnsen,A.H., Hendil,K.B. and Hartmann-Petersen,R.
  TITLE     Adrm1, a putative cell adhesion regulating protein, is a novel
            proteasome-associated factor
  JOURNAL   J Mol Biol 360 (5), 1043-1052 (2006)
   PUBMED   16815440
  REMARK    GeneRIF: Adrm1 has a specialised role in proteasome function.
            Identified Adrm1 as a novel component of the regulatory ATPase
            complex of the 26 S proteasome
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Lamerant,N. and Kieda,C.
  TITLE     Adhesion properties of adhesion-regulating molecule 1 protein on
            endothelial cells
  JOURNAL   FEBS J 272 (8), 1833-1844 (2005)
   PUBMED   15819879
  REMARK    GeneRIF: ARM-1 is a cytosolic protein associated with the plasma
            membrane. However, no cell surface expression of the protein was
            observed. These results suggest an indirect role of ARM-1 in
            adhesion rather than a direct role as an adhesion molecule
            itself.[ARM-1]
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Cascio,P., Call,M., Petre,B.M., Walz,T. and Goldberg,A.L.
  TITLE     Properties of the hybrid form of the 26S proteasome containing both
            19S and PA28 complexes
  JOURNAL   EMBO J 21 (11), 2636-2645 (2002)
   PUBMED   12032076
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Simins,A.B., Weighardt,H., Weidner,K.M., Weidle,U.H. and
            Holzmann,B.
  TITLE     Functional cloning of ARM-1, an adhesion-regulating molecule
            upregulated in metastatic tumor cells
  JOURNAL   Clin Exp Metastasis 17 (8), 641-648 (1999)
   PUBMED   10919708
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Shimada,S., Ogawa,M., Takahashi,M., Schlom,J. and Greiner,J.W.
  TITLE     Molecular cloning and characterization of the complementary DNA of
            an M(r) 110,000 antigen expressed by human gastric carcinoma cells
            and upregulated by gamma-interferon
  JOURNAL   Cancer Res 54 (14), 3831-3836 (1994)
   PUBMED   8033103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY029018.1, HY178253.1,
            BR000321.1 and BC017245.2.
            
            Summary: This gene encodes a member of the adhesion regulating
            molecule 1 protein family. The encoded protein is a component of
            the proteasome where it acts as a ubiquitin receptor and recruits
            the deubiquitinating enzyme, ubiquitin carboxyl-terminal hydrolase
            L5. Increased levels of the encoded protein are associated with
            increased cell adhesion, which is likely an indirect effect of this
            intracellular protein. Dysregulation of this gene has been
            implicated in carcinogenesis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an in-frame exon in the 5' coding region, compared to variant
            1. The encoded isoform (2) is shorter, compared to isoform 1.
            Variants 3 and 4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR5189664.384.1, SRR5189661.21066.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..368
                     /product="proteasomal ubiquitin receptor ADRM1 isoform 2"
                     /note="110 kDa cell membrane glycoprotein; M(r) 110,000
                     surface antigen; proteasomal ubiquitin receptor ADRM1;
                     rpn13 homolog; proteasome regulatory particle non-ATPase
                     13; proteasome ubiquitin receptor; adhesion regulating
                     molecule 1"
                     /calculated_mol_wt=37374
     Region          24..89
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          235..342
                     /region_name="RPN13_C"
                     /note="UCH-binding domain; pfam16550"
                     /db_xref="CDD:465170"
     CDS             1..368
                     /gene="ADRM1"
                     /gene_synonym="ARM-1; ARM1; GP110; PSMD16"
                     /coded_by="NM_001281437.1:152..1258"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS74747.1"
                     /db_xref="GeneID:11047"
                     /db_xref="HGNC:HGNC:15759"
                     /db_xref="MIM:610650"
ORIGIN      
        1 mttsgalfps lvpgsrgasn kylvefragk mslkgttvtp dkrkglvyiq qtddslihfc
       61 wkdrtsgnve depktdqdee hcrkvneyln nppmpgalga sgssghelsa lggegglqsl
      121 lgnmshsqlm qligpaglgg lgglgaltgp glasllgssg ppgsssssss rsqsaavtps
      181 sttsstratp apsapaaasa tspspapssg ngastaaspt qpiqlsdlqs ilatmnvpag
      241 paggqqvdla svltpeimap ilanadvqer llpylpsges lpqtadeiqn tltspqfqqa
      301 lgmfsaalas gqlgplmcqf glpaeaveaa nkgdveafak amqnnakpeq kegdtkdkkd
      361 eeedmsld
//
LOCUS       NP_009143                336 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RING2 [Homo sapiens].
ACCESSION   NP_009143
VERSION     NP_009143.1
DBSOURCE    REFSEQ: accession NM_007212.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Araujo-Abad,S., Rizzuti,B., Soto-Conde,L., Vidal,M., Abian,O.,
            Velazquez-Campoy,A., Neira,J.L. and de Juan Romero,C.
  TITLE     Citrullinating enzyme PADI4 and transcriptional repressor RING1B
            bind in cancer cells
  JOURNAL   Int J Biol Macromol 274 (Pt 1), 133163 (2024)
   PUBMED   38878927
  REMARK    GeneRIF: Citrullinating enzyme PADI4 and transcriptional repressor
            RING1B bind in cancer cells.
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Sera,Y., Imanaka,T. and Yamaguchi,M.
  TITLE     M phase-specific interaction between SBDS and RNF2 at the mitotic
            spindles regulates mitotic progression
  JOURNAL   Biochem Biophys Res Commun 682, 118-123 (2023)
   PUBMED   37806249
  REMARK    GeneRIF: M phase-specific interaction between SBDS and RNF2 at the
            mitotic spindles regulates mitotic progression.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Seo,D.Y., Kim,D., Nguyen,K.T., Oh,J., Lee,J.S. and Hwang,C.S.
  TITLE     N-Terminally arginylated ubiquitin is attached to histone H2A by
            RING1B E3 ligase in human cells
  JOURNAL   Biochem Biophys Res Commun 666, 186-194 (2023)
   PUBMED   36932026
  REMARK    GeneRIF: N-Terminally arginylated ubiquitin is attached to histone
            H2A by RING1B E3 ligase in human cells.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Yao,L., Li,J., Jiang,B., Zhang,Z., Li,X., Ouyang,X., Xiao,Y.,
            Liu,G., Wang,Z. and Zhang,G.
  TITLE     RNF2 inhibits E-Cadherin transcription to promote hepatocellular
            carcinoma metastasis via inducing histone mono-ubiquitination
  JOURNAL   Cell Death Dis 14 (4), 261 (2023)
   PUBMED   37037816
  REMARK    GeneRIF: RNF2 inhibits E-Cadherin transcription to promote
            hepatocellular carcinoma metastasis via inducing histone
            mono-ubiquitination.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Suzuki,M., Mizutani-Koseki,Y., Fujimura,Y., Miyagishima,H.,
            Kaneko,T., Takada,Y., Akasaka,T., Tanzawa,H., Takihara,Y.,
            Nakano,M., Masumoto,H., Vidal,M., Isono,K. and Koseki,H.
  TITLE     Involvement of the Polycomb-group gene Ring1B in the specification
            of the anterior-posterior axis in mice
  JOURNAL   Development 129 (18), 4171-4183 (2002)
   PUBMED   12183370
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Tuckfield,A., Clouston,D.R., Wilanowski,T.M., Zhao,L.L.,
            Cunningham,J.M. and Jane,S.M.
  TITLE     Binding of the RING polycomb proteins to specific target genes in
            complex with the grainyhead-like family of developmental
            transcription factors
  JOURNAL   Mol Cell Biol 22 (6), 1936-1946 (2002)
   PUBMED   11865070
  REMARK    GeneRIF: The human PcG protein dinG interacts with CP2, a mammalian
            member of the grainyhead-like family of transcription factors, in
            vitro and in vivo. The functional consequence of this interaction
            is repression of CP2-dependent transcription.
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Lee,S.J., Choi,J.Y., Sung,Y.M., Park,H., Rhim,H. and Kang,S.
  TITLE     E3 ligase activity of RING finger proteins that interact with
            Hip-2, a human ubiquitin-conjugating enzyme
  JOURNAL   FEBS Lett 503 (1), 61-64 (2001)
   PUBMED   11513855
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Garcia,E., Marcos-Gutierrez,C., del Mar Lorente,M., Moreno,J.C. and
            Vidal,M.
  TITLE     RYBP, a new repressor protein that interacts with components of the
            mammalian Polycomb complex, and with the transcription factor YY1
  JOURNAL   EMBO J 18 (12), 3404-3418 (1999)
   PUBMED   10369680
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF141327.1 and AL109865.36.
            
            Summary: Polycomb group (PcG) of proteins form the multiprotein
            complexes that are important for the transcription repression of
            various genes involved in development and cell proliferation. The
            protein encoded by this gene is one of the PcG proteins. It has
            been shown to interact with, and suppress the activity of,
            transcription factor CP2 (TFCP2/CP2). Studies of the mouse
            counterpart suggested the involvement of this gene in the
            specification of anterior-posterior axis, as well as in cell
            proliferation in early development. This protein was also found to
            interact with huntingtin interacting protein 2 (HIP2), an
            ubiquitin-conjugating enzyme, and possess ubiquitin ligase
            activity. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012583.1, AF141327.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367510.8/ ENSP00000356480.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.3"
     Protein         1..336
                     /product="E3 ubiquitin-protein ligase RING2"
                     /EC_number="2.3.2.27"
                     /note="RING finger protein 1B; RING finger protein BAP-1;
                     HIP2-interacting protein 3; huntingtin-interacting protein
                     2-interacting protein 3; protein DinG; RING-type E3
                     ubiquitin transferase RING2"
                     /calculated_mol_wt=37524
     Region          2..179
                     /region_name="Interaction with HIP2.
                     /evidence=ECO:0000269|PubMed:11513855"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99496.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q99496.1)"
     Region          37..113
                     /region_name="RING-HC_RING2"
                     /note="RING finger, HC subclass, found in really
                     interesting new gene 2 protein (RING2) and similar
                     proteins; cd16740"
                     /db_xref="CDD:438398"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:25519132; propagated from
                     UniProtKB/Swiss-Prot (Q99496.1)"
     Site            order(48..49,63,65..66,68,70,77,81,85,93,95..98,101..103,
                     105..106,108..109,112..113)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438398"
     Region          93..98
                     /region_name="Interaction with nucleosomes via an acidic
                     patch on histone H2A and histone H2B.
                     /evidence=ECO:0000269|PubMed:25355358"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99496.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99496.1)"
     Region          157..208
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99496.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:25519132,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99496.1)"
     Region          225..330
                     /region_name="RAWUL_RING2"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in really interesting new gene 2
                     protein (RING2); cd17167"
                     /db_xref="CDD:340687"
     Site            order(227..229,247..250,254,257..259,261..262,265..266,
                     322..324)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340687"
     CDS             1..336
                     /gene="RNF2"
                     /gene_synonym="BAP-1; BAP1; DING; HIPI3; LUSYAM; RING1B;
                     RING2"
                     /coded_by="NM_007212.4:95..1105"
                     /db_xref="CCDS:CCDS1365.1"
                     /db_xref="GeneID:6045"
                     /db_xref="HGNC:HGNC:10061"
                     /db_xref="MIM:608985"
ORIGIN      
        1 msqavqtngt qplsktwels lyelqrtpqe aitdgleivv sprslhselm cpicldmlkn
       61 tmttkeclhr fcadciital rsgnkecptc rkklvskrsl rpdpnfdali skiypsrdey
      121 eahqervlar inkhnnqqal shsieeglki qamnrlqrgk kqqiengsga edngdsshcs
      181 nasthsnqea gpsnkrtkts ddsgleldnn naamaidpvm dgaseielvf rphptlmekd
      241 dsaqtryikt sgnatvdhls kylavrlale elrskgesnq mnldtasekq ytiyiatasg
      301 qftvlngsfs lelvsekywk vnkpmelyya ptkehk
//
LOCUS       NP_001356029             332 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001356029
VERSION     NP_001356029.1
DBSOURCE    REFSEQ: accession NM_001369100.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.53119.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..332
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 9"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=37747
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..281
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..332
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369100.1:104..1102"
                     /note="isoform 9 is encoded by transcript variant 21"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefikl qelvdrvler fqasglivke wnsvklhatv
      241 mntlfrkdpn aegrynlyta egkyifkere sfdgrnilks fallprleyn daisahcnlc
      301 lpgssdspas asqvagitgv sdaysqslpg ks
//
LOCUS       NP_001354580             923 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform u [Homo sapiens].
ACCESSION   NP_001354580
VERSION     NP_001354580.1
DBSOURCE    REFSEQ: accession NM_001367651.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 923)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 923)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 923)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 923)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 923)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 923)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..923
                     /product="SUN domain-containing protein 1 isoform u"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=102245
     Region          135..429
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          555..608
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(555,558..559,562,565..566,569..570,572..573,
                     576..577,579..580,583..584,586..587,590,593..594,597,
                     600..601,604..605,607..608)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          567..>700
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          685..743
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          786..921
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..923
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367651.1:76..2847"
                     /note="isoform u is encoded by transcript variant 21"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 meqltylfrl deeayeglnm pggrmrgpsa ahtalwppan srthtalwpp vnshthtalw
       61 ppvnshthta lwppansrth valwprmnsc tgffrsvvss syssdaldfe tehkldpvfd
      121 sprmsrrslr lattactlgd geavgadsgt ssavslknra arttkqrrst nksafsinhv
      181 srqvtssgvs hggtvslqda vtrrppvlde swireqttvd hfwgldddgd lkggnkaaiq
      241 gngdvgaaaa tahngfscsn csmlserkdv ltahpaapgp vsrvysrdrn qkshasyygr
      301 mnvrevlred ghlsvngeal cddckgkrhl dahtaahsqs prlpgragtl whiwacagyf
      361 llqilrriga vgqavsrtaw salwlavvap gkaasgvfww lgigwyqfvt liswlnvfll
      421 trclrnickf lvlliplfll laglslrgqg nffsflpvln wasmhrtqrv ddpqdvfkpt
      481 tsrlkqplqg dseafpwhwm sgveqqvasl sgqchhhgen lrelttllqk lqarvdqmeg
      541 gaagpsasvr davgqppret dfmafhqehe vrmshledil gklrekseai qkeleqtkqk
      601 tisavgeqll ptvehlqlel dqlkselssw rhvktgcetv davqervdvq vremvkllfs
      661 edqqggsleq llqrfssqfv skgdlqtmlr dlqlqilrnv thhvsvtkql ptseavvsav
      721 seagasgite aqaraivnsa lklysqdktg mvdfalesgg gsilstrcse tyetktalms
      781 lfgiplwyfs qsprvviqpd iypgncwafk gsqgylvvrl smmihpaaft lehipktlsp
      841 tgnissapkd favygleney qeegqllgqf tydqdgeslq mfqalkrpdd tafqivelri
      901 fsnwghpeyt clyrfrvhge pvk
//
LOCUS       NP_005601                425 aa            linear   PRI 20-NOV-2025
DEFINITION  histone-binding protein RBBP4 isoform a [Homo sapiens].
ACCESSION   NP_005601
VERSION     NP_005601.1
DBSOURCE    REFSEQ: accession NM_005610.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Zhan,Y., Zhang,Z., Yin,A., Su,X., Tang,N., Chen,Y., Zhang,Z.,
            Chen,W., Wang,J. and Wang,W.
  TITLE     RBBP4: A novel diagnostic and prognostic biomarker for
            non-small-cell lung cancer correlated with autophagic cell death
  JOURNAL   Cancer Med 13 (15), e70090 (2024)
   PUBMED   39109577
  REMARK    GeneRIF: RBBP4: A novel diagnostic and prognostic biomarker for
            non-small-cell lung cancer correlated with autophagic cell death.
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Zhan,Y., Yin,A., Su,X., Tang,N., Zhang,Z., Chen,Y., Wang,W. and
            Wang,J.
  TITLE     Interpreting the molecular mechanisms of RBBP4/7 and their roles in
            human diseases (Review)
  JOURNAL   Int J Mol Med 53 (5) (2024)
   PUBMED   38577935
  REMARK    GeneRIF: Interpreting the molecular mechanisms of RBBP4/7 and their
            roles in human diseases (Review).
            Review article
REFERENCE   4  (residues 1 to 425)
  AUTHORS   Li,J., Song,C., Gu,J., Li,C., Zang,W., Shi,L., Chen,L., Zhu,L.,
            Zhou,M., Wang,T., Li,H., Qi,S. and Lu,Y.
  TITLE     RBBP4 regulates the expression of the Mre11-Rad50-NBS1 (MRN)
            complex and promotes DNA double-strand break repair to mediate
            glioblastoma chemoradiotherapy resistance
  JOURNAL   Cancer Lett 557, 216078 (2023)
   PUBMED   36736531
  REMARK    GeneRIF: RBBP4 regulates the expression of the Mre11-Rad50-NBS1
            (MRN) complex and promotes DNA double-strand break repair to
            mediate glioblastoma chemoradiotherapy resistance.
REFERENCE   5  (residues 1 to 425)
  AUTHORS   Zhu,X., Luo,X., Long,X., Jiang,S., Xie,X., Zhang,Q. and Wang,H.
  TITLE     CircAGO2 promotes colorectal cancer progression by inhibiting heat
            shock protein family B (small) member 8 via miR-1-3p/retinoblastoma
            binding protein 4 axis
  JOURNAL   Funct Integr Genomics 23 (2), 78 (2023)
   PUBMED   36881338
  REMARK    GeneRIF: CircAGO2 promotes colorectal cancer progression by
            inhibiting heat shock protein family B (small) member 8 via
            miR-1-3p/retinoblastoma binding protein 4 axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 425)
  AUTHORS   Taunton,J., Hassig,C.A. and Schreiber,S.L.
  TITLE     A mammalian histone deacetylase related to the yeast
            transcriptional regulator Rpd3p
  JOURNAL   Science 272 (5260), 408-411 (1996)
   PUBMED   8602529
REFERENCE   7  (residues 1 to 425)
  AUTHORS   Qian,Y.W. and Lee,E.Y.
  TITLE     Dual retinoblastoma-binding proteins with properties related to a
            negative regulator of ras in yeast
  JOURNAL   J Biol Chem 270 (43), 25507-25513 (1995)
   PUBMED   7503932
REFERENCE   8  (residues 1 to 425)
  AUTHORS   Qian,Y.W., Wang,Y.C., Hollingsworth,R.E. Jr., Jones,D., Ling,N. and
            Lee,E.Y.
  TITLE     A retinoblastoma-binding protein related to a negative regulator of
            Ras in yeast
  JOURNAL   Nature 364 (6438), 648-652 (1993)
   PUBMED   8350924
REFERENCE   9  (residues 1 to 425)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 425)
  AUTHORS   Bauw,G., Rasmussen,H.H., van den Bulcke,M., van Damme,J., Puype,M.,
            Gesser,B., Celis,J.E. and Vandekerckhove,J.
  TITLE     Two-dimensional gel electrophoresis, protein electroblotting and
            microsequencing: a direct link between proteins and genes
  JOURNAL   Electrophoresis 11 (7), 528-536 (1990)
   PUBMED   1699755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC315298.1, AK312571.1 and
            AC114489.2.
            
            Summary: This gene encodes a ubiquitously expressed nuclear protein
            which belongs to a highly conserved subfamily of WD-repeat
            proteins. It is present in protein complexes involved in histone
            acetylation and chromatin assembly. It is part of the Mi-2 complex
            which has been implicated in chromatin remodeling and
            transcriptional repression associated with histone deacetylation.
            This encoded protein is also part of co-repressor complexes, which
            is an integral component of transcriptional silencing. It is found
            among several cellular proteins that bind directly to
            retinoblastoma protein to regulate cell proliferation. This protein
            also seems to be involved in transcriptional repression of
            E2F-responsive genes. Three transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.35501.1,
                                           SRR3476690.340079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373493.10/ ENSP00000362592.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..425
                     /product="histone-binding protein RBBP4 isoform a"
                     /note="MSI1 protein homolog; retinoblastoma-binding
                     protein 4; chromatin assembly factor/CAF-1 p48 subunit;
                     retinoblastoma-binding protein p48; histone-binding
                     protein RBBP4; RBBP-4; CAF-I p48; CAF-1 subunit C; CAF-I
                     48 kDa subunit; chromatin assembly factor 1 subunit C;
                     chromatin assembly factor I p48 subunit;
                     nucleosome-remodeling factor subunit RBAP48"
                     /calculated_mol_wt=47525
     Region          2..132
                     /region_name="Interaction with ARMC12.
                     /evidence=ECO:0000269|PubMed:30026490"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q09028.3)"
     Site            4
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q09028.3)"
     Region          19..88
                     /region_name="CAF1C_H4-bd"
                     /note="Histone-binding protein RBBP4 or subunit C of CAF1
                     complex; pfam12265"
                     /db_xref="CDD:463513"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q09028.3)"
     Region          122..403
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Site            order(122..123,141,148,152..153,175..176,199,205..206,226,
                     245,249,255..256,271..272,291,295,301..302,315..316,334,
                     339,345..346,372..373,392,396,402..403)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          126..175
                     /region_name="WD 2. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          128..175
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            160
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q60972; propagated from
                     UniProtKB/Swiss-Prot (Q09028.3)"
     Region          176..223
                     /region_name="WD 3. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          180..224
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          225..270
                     /region_name="WD 4. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          231..270
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          271..314
                     /region_name="WD 5. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          276..314
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          315..371
                     /region_name="WD 6. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          320..371
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q09028.3)"
     Region          372..404
                     /region_name="WD 7. /evidence=ECO:0000269|PubMed:39460621,
                     ECO:0007744|PDB:8TX8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q09028.3)"
     Region          377..402
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..425
                     /gene="RBBP4"
                     /gene_synonym="lin-53; NURF55; RBAP48"
                     /coded_by="NM_005610.3:100..1377"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS366.1"
                     /db_xref="GeneID:5928"
                     /db_xref="HGNC:HGNC:9887"
                     /db_xref="MIM:602923"
ORIGIN      
        1 madkeaafdd aveervinee ykiwkkntpf lydlvmthal ewpsltaqwl pdvtrpegkd
       61 fsihrlvlgt htsdeqnhlv iasvqlpndd aqfdashyds ekgefggfgs vsgkieieik
      121 inhegevnra rympqnpcii atktpssdvl vfdytkhpsk pdpsgecnpd lrlrghqkeg
      181 yglswnpnls ghllsasddh ticlwdisav pkegkvvdak tiftghtavv edvswhllhe
      241 slfgsvaddq klmiwdtrsn ntskpshsvd ahtaevncls fnpysefila tgsadktval
      301 wdlrnlklkl hsfeshkdei fqvqwsphne tilassgtdr rlnvwdlski geeqspedae
      361 dgppellfih gghtakisdf swnpnepwvi csvsednimq vwqmaeniyn dedpegsvdp
      421 egqgs
//
LOCUS       NP_078929                184 aa            linear   PRI 20-NOV-2025
DEFINITION  PRKR-interacting protein 1 [Homo sapiens].
ACCESSION   NP_078929
VERSION     NP_078929.1
DBSOURCE    REFSEQ: accession NM_024653.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Ozato,Y., Masuda,T., Kobayashi,Y., Takao,S., Hisamatu,Y.,
            Toshima,T., Yonemura,Y., Uemura,M., Eguchi,H., Doki,Y., Mori,M. and
            Mimori,K.
  TITLE     PRKRIP1, A Splicing Complex Factor, Is a Marker of Poor Prognosis
            in Colorectal Cancer
  JOURNAL   Anticancer Res 42 (10), 4701-4706 (2022)
   PUBMED   36192001
  REMARK    GeneRIF: PRKRIP1, A Splicing Complex Factor, Is a Marker of Poor
            Prognosis in Colorectal Cancer.
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Zhang,X., Zhan,X., Yan,C., Zhang,W., Liu,D., Lei,J. and Shi,Y.
  TITLE     Structures of the human spliceosomes before and after release of
            the ligated exon
  JOURNAL   Cell Res 29 (4), 274-285 (2019)
   PUBMED   30728453
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Butte,A.J., Sigdel,T.K., Wadia,P.P., Miklos,D.B. and Sarwal,M.M.
  TITLE     Protein microarrays discover angiotensinogen and PRKRIP1 as novel
            targets for autoantibodies in chronic renal disease
  JOURNAL   Mol Cell Proteomics 10 (3), M110.000497 (2011)
   PUBMED   21183621
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Yin,Z., Haynie,J., Williams,B.R. and Yang,Y.C.
  TITLE     C114 is a novel IL-11-inducible nuclear double-stranded RNA-binding
            protein that inhibits protein kinase R
  JOURNAL   J Biol Chem 278 (25), 22838-22845 (2003)
   PUBMED   12679338
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC073517.6.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014298.2, AK023964.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397912.3/ ENSP00000381010.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..184
                     /product="PRKR-interacting protein 1"
                     /note="likely ortholog of mouse C114 dsRNA-binding
                     protein; KRAB box domain containing 3; PRKR interacting
                     protein 1 (IL11 inducible)"
                     /calculated_mol_wt=20866
     Region          1..50
                     /region_name="Interaction with EIF2AK2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     Region          37..76
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     Region          42..>125
                     /region_name="DUF1168"
                     /note="Protein of unknown function (DUF1168); pfam06658"
                     /db_xref="CDD:461977"
     Region          51..143
                     /region_name="Required for RNA-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     Region          120..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     Region          126..138
                     /region_name="Required for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H875.1)"
     CDS             1..184
                     /gene="PRKRIP1"
                     /gene_synonym="C114; KRBOX3"
                     /coded_by="NM_024653.4:50..604"
                     /db_xref="CCDS:CCDS34714.1"
                     /db_xref="GeneID:79706"
                     /db_xref="HGNC:HGNC:21894"
                     /db_xref="MIM:617458"
ORIGIN      
        1 maspaassvr pprpkkepqt lvipknaaee qklklerlmk npdkavpipe kmsewaprpp
       61 pefvrdvmgs sagagsgefh vyrhlrrrey qrqdymdama ekqkldaefq krleknkiaa
      121 eeqtakrrkk rqklkekkll akkmkleqkk qegpgqpkeq gssssaeasg teeeeevpsf
      181 tmgr
//
LOCUS       NP_647595                506 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_647595
VERSION     NP_647595.1
DBSOURCE    REFSEQ: accession NM_139345.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF594020.1, AF043899.1,
            AC012508.10, AF070576.1 and BM711160.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) lacks three in-frame exons in
            the coding region, compared to variant 1. Isoform 3, also called
            IIc1, is shorter than isoform 1 and binds dynamin and synaptojanin.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043899.1, SRR1803617.154908.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..506
                     /product="myc box-dependent-interacting protein 1 isoform
                     3"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=55044
     Region          31..272
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,228,231..232,234,239..240,242..243,246..247,
                     249..250,253..254,256..257,261,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <270..>390
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          434..505
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(445..451,470,472..475,498,500..501)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..506
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_139345.3:212..1732"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2140.1"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakpvsllek
      181 aapqwcqgkl qahlvaqtnl lrnqaeeeli kaqkvfeemn vdlqeelpsl wnsrvgfyvn
      241 tfqsiaglee nfhkemskln qnlndvlvgl ekqhgsntft vkaqpsdnap akgnkspspp
      301 dgspaatpei rvnhepepag gatpgatlpk spsqptespa gslpsgepsa aegtfavswp
      361 sqtaepgpaq paeasevagg tqpaagaqep getaaseaas sslpavvvet fpatvngtve
      421 ggsgagrldl ppgfmfkvqa qhdytatdtd elqlkagdvv lvipfqnpee qdegwlmgvk
      481 esdwnqhkel ekcrgvfpen ftervp
//
LOCUS       NP_001124488             898 aa            linear   PRI 20-NOV-2025
DEFINITION  cip1-interacting zinc finger protein isoform 1 [Homo sapiens].
ACCESSION   NP_001124488
VERSION     NP_001124488.1
DBSOURCE    REFSEQ: accession NM_001131016.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Chen,Y.R., Wu,Y.S., Wang,W.S., Zhang,J.S. and Wu,Q.G.
  TITLE     Upregulation of lncRNA DANCR functions as an oncogenic role in
            non-small lung cancer by regulating miR-214-5p/CIZ1 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2539-2547 (2020)
   PUBMED   32196604
  REMARK    GeneRIF: Upregulation of lncRNA DANCR functions as an oncogenic
            role in non-small lung cancer by regulating miR-214-5p/CIZ1 axis.
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Chen,X., Wang,P., Wang,S., Li,J., Ou,T. and Zeng,X.
  TITLE     CIZ1 knockdown suppresses the proliferation of bladder cancer cells
            by inducing apoptosis
  JOURNAL   Gene 719, 143946 (2019)
   PUBMED   31252164
  REMARK    GeneRIF: silencing of CIZ1 suppressed bladder cancer cell
            proliferation through inducing apoptosis and reducing cell cycle
            progression
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Coverley,D., Marr,J. and Ainscough,J.
  TITLE     Ciz1 promotes mammalian DNA replication
  JOURNAL   J Cell Sci 118 (Pt 1), 101-112 (2005)
   PUBMED   15585571
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Warder,D.E. and Keherly,M.J.
  TITLE     Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus
            DNA sequence ARYSR(0-2)YYAC
  JOURNAL   J Biomed Sci 10 (4), 406-417 (2003)
   PUBMED   12824700
  REMARK    GeneRIF: data indicate that Ciz1 is localized in the nucleus and is
            expressed in a wide range of tissues, especially the pancreas and
            the brain; formulated a consensus DNA sequence, ARYSR(0-2)YYAC,
            recognized by Ciz1
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Mitsui,K., Matsumoto,A., Ohtsuka,S., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
            zinc finger protein, ciz1
  JOURNAL   Biochem Biophys Res Commun 264 (2), 457-464 (1999)
   PUBMED   10529385
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292713.1, AK303636.1 and
            BC021163.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a zinc finger DNA
            binding protein that interacts with CIP1, part of a complex with
            cyclin E. The encoded protein may regulate the cellular
            localization of CIP1. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (5) has an alternate exon in place
            of the first exon and lacks an alternate in-frame exon compared to
            variant 6. The resulting isoform (1) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform 5.
            Variants 1 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292713.1, AB030835.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372938.10/ ENSP00000362029.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..898
                     /product="cip1-interacting zinc finger protein isoform 1"
                     /note="zinc finger protein 356; nuclear protein NP94;
                     Cip1-interacting zinc finger protein"
                     /calculated_mol_wt=99915
     Region          48..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          <129..482
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          157..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          318..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          562..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          592..621
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          656..676
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(663..665,666,670,675,692,695..699,701..702)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <666..>717
                     /region_name="UFD2"
                     /note="U1-like Zn-finger-containing protein [General
                     function prediction only]; COG5112"
                     /db_xref="CDD:227443"
     Region          686..710
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          687..709
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          859..898
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     CDS             1..898
                     /gene="CIZ1"
                     /gene_synonym="LSFR1; NP94; ZNF356"
                     /coded_by="NM_001131016.2:147..2843"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS6894.1"
                     /db_xref="GeneID:25792"
                     /db_xref="HGNC:HGNC:16744"
                     /db_xref="MIM:611420"
ORIGIN      
        1 mfsqqqqqql qqqqqqlqql qqqqlqqqql qqqqllqlqq llqqsppqap lpmavsrglp
       61 pqqpqqplln lqgtnsasll ngsmlqrall lqqlqgldqf amppatydta gltmptatlg
      121 nlrgygmasp glaapsltpp qlatpnlqqf fpqatrqsll gpppvgvpmn psqfnlsgrn
      181 pqkqartsss ttpnrkdsss qtmpvedksd ppegseeaae prmdtpedqd lppcpediak
      241 ekrtpapepe pceaselpak rlrsseepte keppgqlqvk aqpqarmtvp kqtqtpdllp
      301 ealeaqvlpr fqprvlqvqa qvqsqtqpri pstdtqvqpk lqkqaqtqts pehlvlqqkq
      361 vqpqlqqeae pqkqvqpqvq pqahsqgprq vqlqqeaepl kqvqpqvqpq ahsqpprqvq
      421 lqlqkqvqtq typqvhtqaq psvqpqehpp aqvsvqppeq theqphtqpq vsllapeqtp
      481 vvvhvcglem ppdaveaggg mektlpepvg tqvsmeeiqn esacgldvge cenrarempg
      541 vwgaggslkv tilqssdsra fstvpltpvp rpsdsvsstp aatstpskqa lqffcyicka
      601 scssqqefqd hmsepqhqqr lgeiqhmsqa cllsllpvpr dvletedeep pprrwcntcq
      661 lyymgdliqh rrtqdhkiak qslrpfctvc nryfktprkf vehvksqghk dkakelksle
      721 keiagqdedh fitvdavgcf egdeeeeedd edeeeievee elckqvrsrd isreewkgse
      781 tyspntaygv dflvpvmgyi crichkfyhs nsgaqlshck slghfenlqk ykaaknpspt
      841 trpvsrrcai narnaltalf tssgrppsqp ntqdktpskv tarpsqpplp rrstrlkt
//
LOCUS       NP_001307499             717 aa            linear   PRI 20-NOV-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 10
            isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001307499 XP_005254174
VERSION     NP_001307499.1
DBSOURCE    REFSEQ: accession NM_001320570.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Dolla,G., Nicolas,S., Dos Santos,L.R., Bourgeois,A.,
            Pardossi-Piquard,R., Bihl,F., Zaghrini,C., Justino,J., Payre,C.,
            Mansuelle,P., Garbers,C., Ronco,P., Checler,F., Lambeau,G. and
            Petit-Paitel,A.
  TITLE     Ectodomain shedding of PLA2R1 is mediated by the metalloproteases
            ADAM10 and ADAM17
  JOURNAL   J Biol Chem 300 (7), 107480 (2024)
   PUBMED   38897568
  REMARK    GeneRIF: Ectodomain shedding of PLA2R1 is mediated by the
            metalloproteases ADAM10 and ADAM17.
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Piwkowska,A., Rachubik,P., Typiak,M., Kulesza,T., Audzeyenka,I.,
            Saleem,M.A., Gruba,N., Wysocka,M., Lesner,A. and Rogacka,D.
  TITLE     ADAM10 as a major activator of reactive oxygen species production
            and klotho shedding in podocytes under diabetic conditions
  JOURNAL   Biochem Pharmacol 225, 116328 (2024)
   PUBMED   38815628
  REMARK    GeneRIF: ADAM10 as a major activator of reactive oxygen species
            production and klotho shedding in podocytes under diabetic
            conditions.
REFERENCE   4  (residues 1 to 717)
  AUTHORS   Babendreyer,A., Kieselhorst,J., Rinkens,C., Lyashenko,A.M.,
            Dusterhoft,S., Jahr,H., Craveiro,R.B., Wolf,M. and Ludwig,A.
  TITLE     Downregulation of the metalloproteinases ADAM10 or ADAM17 promotes
            osteoclast differentiation
  JOURNAL   Cell Commun Signal 22 (1), 322 (2024)
   PUBMED   38863060
  REMARK    GeneRIF: Downregulation of the metalloproteinases ADAM10 or ADAM17
            promotes osteoclast differentiation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Gao,J.H., He,A.D., Liu,L.M., Zhou,Y.J., Guo,Y.W., Lu,M., Zeng,X.B.,
            Gong,X., Lu,Y.J., Liang,H.F., Zhang,B.X., Ma,R., Zhang,R.Y. and
            Ming,Z.Y.
  TITLE     Direct interaction of platelet with tumor cell aggravates
            hepatocellular carcinoma metastasis by activating
            TLR4/ADAM10/CX3CL1 axis
  JOURNAL   Cancer Lett 585, 216674 (2024)
   PUBMED   38280480
  REMARK    GeneRIF: Direct interaction of platelet with tumor cell aggravates
            hepatocellular carcinoma metastasis by activating
            TLR4/ADAM10/CX3CL1 axis.
REFERENCE   6  (residues 1 to 717)
  AUTHORS   Lammich,S., Buell,D., Zilow,S., Ludwig,A.K., Nuscher,B.,
            Lichtenthaler,S.F., Prinzen,C., Fahrenholz,F. and Haass,C.
  TITLE     Expression of the anti-amyloidogenic secretase ADAM10 is suppressed
            by its 5'-untranslated region
  JOURNAL   J Biol Chem 285 (21), 15753-15760 (2010)
   PUBMED   20348102
  REMARK    GeneRIF: the 5'-UTR of ADAM10 may have an important role for
            post-transcriptional regulation of ADAM10 expression and
            consequently Abeta production.
REFERENCE   7  (residues 1 to 717)
  AUTHORS   McKie,N., Edwards,T., Dallas,D.J., Houghton,A., Stringer,B.,
            Graham,R., Russell,G. and Croucher,P.I.
  TITLE     Expression of members of a novel membrane linked metalloproteinase
            family (ADAM) in human articular chondrocytes
  JOURNAL   Biochem Biophys Res Commun 230 (2), 335-339 (1997)
   PUBMED   9016778
REFERENCE   8  (residues 1 to 717)
  AUTHORS   Howard,L., Lu,X., Mitchell,S., Griffiths,S. and Glynn,P.
  TITLE     Molecular cloning of MADM: a catalytically active mammalian
            disintegrin-metalloprotease expressed in various cell types
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 45-50 (1996)
   PUBMED   8694785
REFERENCE   9  (residues 1 to 717)
  AUTHORS   Wolfsberg,T.G., Primakoff,P., Myles,D.G. and White,J.M.
  TITLE     ADAM, a novel family of membrane proteins containing A Disintegrin
            And Metalloprotease domain: multipotential functions in cell-cell
            and cell-matrix interactions
  JOURNAL   J Cell Biol 131 (2), 275-278 (1995)
   PUBMED   7593158
  REMARK    Review article
REFERENCE   10 (residues 1 to 717)
  AUTHORS   O'Bryan,J.P., Fridell,Y.W., Koski,R., Varnum,B. and Liu,E.T.
  TITLE     The transforming receptor tyrosine kinase, Axl, is
            post-translationally regulated by proteolytic cleavage
  JOURNAL   J Biol Chem 270 (2), 551-557 (1995)
   PUBMED   7822279
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091046.2 and AC018904.6.
            
            On Mar 1, 2016 this sequence version replaced XP_005254174.1.
            
            Summary: Members of the ADAM family are cell surface proteins with
            a unique structure possessing both potential adhesion and protease
            domains. This gene encodes and ADAM family member that cleaves many
            proteins including TNF-alpha and E-cadherin. Alternate splicing
            results in multiple transcript variants encoding different proteins
            that may undergo similar processing. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (2) lacks an in-frame exon
            compared to variant 1. The encoded isoform (2) is shorter than
            isoform 1. This isoform (2) may undergo proteolytic processing
            similar to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1562705.1,
                                           SRR14038196.1459340.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..717
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 10 isoform 2 precursor"
                     /EC_number="3.4.24.81"
                     /note="a disintegrin and metalloprotease domain 10;
                     disintegrin and metalloproteinase domain-containing
                     protein 10; kuzbanian protein homolog; mammalian
                     disintegrin-metalloprotease"
                     /calculated_mol_wt=78567
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2014
     Region          46..156
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          220..428
                     /region_name="ZnMc_TACE_like"
                     /note="Zinc-dependent metalloprotease; TACE_like
                     subfamily. TACE, the tumor-necrosis factor-alpha
                     converting enzyme, releases soluble TNF-alpha from
                     transmembrane pro-TNF-alpha; cd04270"
                     /db_xref="CDD:239798"
     Site            order(352..353,356,362)
                     /site_type="active"
                     /db_xref="CDD:239798"
     Region          435..514
                     /region_name="DISIN"
                     /note="Homologues of snake disintegrins; smart00050"
                     /db_xref="CDD:214490"
     CDS             1..717
                     /gene="ADAM10"
                     /gene_synonym="AD10; AD18; CD156c; CDw156; HsT18717; kuz;
                     MADM; RAK"
                     /coded_by="NM_001320570.2:174..2327"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:102"
                     /db_xref="HGNC:HGNC:188"
                     /db_xref="MIM:602192"
ORIGIN      
        1 mvllrvlill lswaagmggq ygnplnkyir hyeglsynvd slhqkhqrak ravshedqfl
       61 rldfhahgrh fnlrmkrdts lfsdefkvet snkvldydts hiytghiyge egsfshgsvi
      121 dgrfegfiqt rggtfyvepa eryikdrtlp fhsviyhedd inyphkygpq ggcadhsvfe
      181 rmrkyqmtgv eevtqipqee haangpellr kkrttsaekn tcqlyiqtdh lffkyygtre
      241 aviaqintta dekdptnpfr fpnigvekfl elnseqnhdd yclayvftdr dfddgvlgla
      301 wvgapsgssg giceksklys dgkkkslntg iitvqnygsh vppkvshitf ahevghnfgs
      361 phdsgtectp gesknlgqke ngnyimyara tsgdklnnnk fslcsirnis qvlekkrnnc
      421 fvesgqpicg ngmveqgeec dcgysdqckd eccfdanqpe grkcklkpgk qcspsqgpcc
      481 taqcafksks ekcrddsdca regicngfta lcpasdpkpn ftdcnrhtqv cingqcagsi
      541 cekygleect cassdgkddk elchvccmkk mdpstcastg svqwsrhfsg rtitlqpgsp
      601 cndfrgycdv fmrcrlvdad gplarlkkai fspelyenia ewivahwwav llmgialiml
      661 magfikicsv htpssnpklp ppkplpgtlk rrrppqpiqq pqrqrpresy qmghmrr
//
LOCUS       NP_001354663             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354663
VERSION     NP_001354663.1
DBSOURCE    REFSEQ: accession NM_001367734.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (18), as well as variants 3, 4,
            9-17, 19, and 20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.42550.1,
                                           DRR138512.206555.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144835, SAMN03465409
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367734.1:68..1543"
                     /note="isoform c is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001335051             434 aa            linear   PRI 20-NOV-2025
DEFINITION  tripartite motif-containing protein 16 isoform b [Homo sapiens].
ACCESSION   NP_001335051
VERSION     NP_001335051.1
DBSOURCE    REFSEQ: accession NM_001348122.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Guo,D., Zhang,M., Wei,T., Zhang,X., Shi,X., Tang,H., Ding,M.,
            Li,J., Zhang,S. and Guo,W.
  TITLE     NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16
  JOURNAL   Cell Mol Life Sci 81 (1), 167 (2024)
   PUBMED   38581570
  REMARK    GeneRIF: NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Li,S., Wang,J., Chen,H., Hou,J., Shen,T., Li,J., Zhou,B., Zhang,B.,
            Liu,H. and Jiang,D.K.
  TITLE     TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin pathway
  JOURNAL   Mol Carcinog 62 (11), 1686-1699 (2023)
   PUBMED   37477507
  REMARK    GeneRIF: TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin
            pathway.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Roshanazadeh,M.R., Adelipour,M., Sanaei,A., Chenane,H. and
            Rashidi,M.
  TITLE     TRIM3 and TRIM16 as potential tumor suppressors in breast cancer
            patients
  JOURNAL   BMC Res Notes 15 (1), 312 (2022)
   PUBMED   36180926
  REMARK    GeneRIF: TRIM3 and TRIM16 as potential tumor suppressors in breast
            cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,Y., Wu,Y. and Xie,S.
  TITLE     CircPTK2 inhibits cell cisplatin (CDDP) resistance by targeting
            miR-942/TRIM16 axis in non-small cell lung cancer (NSCLC)
  JOURNAL   Bioengineered 13 (2), 3651-3664 (2022)
   PUBMED   35230201
  REMARK    GeneRIF: CircPTK2 inhibits cell cisplatin (CDDP) resistance by
            targeting miR-942/TRIM16 axis in non-small cell lung cancer
            (NSCLC).
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Gwinn,M.R., Whipkey,D.L., Tennant,L.B. and Weston,A.
  TITLE     Differential gene expression in normal human mammary epithelial
            cells treated with malathion monitored by DNA microarrays
  JOURNAL   Environ Health Perspect 113 (8), 1046-1051 (2005)
   PUBMED   16079077
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Beer,H.D., Munding,C., Dubois,N., Mamie,C., Hohl,D. and Werner,S.
  TITLE     The estrogen-responsive B box protein: a novel regulator of
            keratinocyte differentiation
  JOURNAL   J Biol Chem 277 (23), 20740-20749 (2002)
   PUBMED   11919186
  REMARK    GeneRIF: role in regulating keratinocyte differentiation
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Liu,H.L., Golder-Novoselsky,E., Seto,M.H., Webster,L., McClary,J.
            and Zajchowski,D.A.
  TITLE     The novel estrogen-responsive B-box protein (EBBP) gene is
            tamoxifen-regulated in cells expressing an estrogen receptor
            DNA-binding domain mutant
  JOURNAL   Mol Endocrinol 12 (11), 1733-1748 (1998)
   PUBMED   9817599
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005324.1.
            
            Summary: The protein encoded by this gene is a tripartite motif
            (TRIM) family member that contains two B box domains and a
            coiled-coiled region that are characteristic of the B box zinc
            finger protein family. While it lacks a RING domain found in other
            TRIM proteins, the encoded protein can homodimerize or
            heterodimerize with other TRIM proteins and has E3 ubiquitin ligase
            activity. This gene is also a tumor suppressor and is involved in
            secretory autophagy. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (5), as well as variant 4, encodes
            isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2431204.1,
                                           SRR14372080.2169731.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..434
                     /product="tripartite motif-containing protein 16 isoform
                     b"
                     /EC_number="2.3.2.27"
                     /note="estrogen-responsive B box protein; tripartite
                     motif-containing protein 16; E3 ubiquitin-protein ligase
                     TRIM16"
                     /calculated_mol_wt=49899
     Region          235..416
                     /region_name="SPRY_PRY_TRIM16"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 16 (TRIM16); cd12890"
                     /db_xref="CDD:293948"
     CDS             1..434
                     /gene="TRIM16"
                     /gene_synonym="EBBP"
                     /coded_by="NM_001348122.1:199..1503"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS86579.1"
                     /db_xref="GeneID:10626"
                     /db_xref="HGNC:HGNC:17241"
                     /db_xref="MIM:609505"
ORIGIN      
        1 mimedwtckl qnrvlpsedp alsqkgylkk enmaalcrta esqaelqctq ldlerklkln
       61 enaisrlqan qksvlvsvse vkavaemqfg ellaavrkaq anvmlfleek eqaalsqang
      121 ikahleyrsa emekskqele rmaaisntvq fleeyckfkn teditfpsvy vglkdklsgi
      181 rkvitestvh liqllenykk klqefskeee ydirtqvsav vqrkywtskp epstreqflq
      241 yayditfdpd tahkylrlqe enrkvtnttp wehpypdlps rflhwrqvls qqslylhryy
      301 feveifgagt yvgltckgid rkgeernsci sgnnfswslq wngkeftawy sdmetplkag
      361 pfrrlgvyid fpggilsfyg veydtmtlvh kfackfsepv yaafwlskke nairivdlge
      421 epekpapslv gtap
//
LOCUS       NP_001355926             342 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform a [Homo sapiens].
ACCESSION   NP_001355926 XP_024303343
VERSION     NP_001355926.1
DBSOURCE    REFSEQ: accession NM_001368997.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303343.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.87638.1,
                                           SRR1803617.231403.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..342
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=38973
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          283..342
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..342
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368997.1:322..1350"
                     /note="isoform a is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS47956.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qaviemvqea
      301 grvtvrdgmp ellklplrch ecqqllpsip qlkehlrkhw tq
//
LOCUS       NP_001357163             238 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFXANK isoform c [Homo sapiens].
ACCESSION   NP_001357163 XP_016882905
VERSION     NP_001357163.1
DBSOURCE    REFSEQ: accession NM_001370234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 238)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 238)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   3  (residues 1 to 238)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 238)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 238)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 238)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 238)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 238)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 238)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 238)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002126.1 and AC003110.1.
            
            On May 2, 2019 this sequence version replaced XP_016882905.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.1517.1,
                                           SRR5189658.165288.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..238
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..238
                     /product="DNA-binding protein RFXANK isoform c"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=25520
     Region          <95..227
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(101,103,107..108,111..113,115..116,120,123,132,134,
                     136,140..141,144..146,148..149,153,156,165,167,169,
                     173..174,177..179,181..182,186,189)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          101..132
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          134..165
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          167..195
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..238
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_001370234.1:175..891"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS62611.1"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqagsslkhs ttltnrqrgn evsalpatld cdnlvnkpde rgftpliwas afgeietvrf
      121 llewgadphi lakeresals lastggytdi vglllerdvd iniydwnggt pllyavrgnh
      181 vkcveallar gadltteads gytpmdlava lgyrkvqqvi enhilklfqs nlvpadpe
//
LOCUS       NP_001190194             688 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor C isoform 6 precursor [Homo sapiens].
ACCESSION   NP_001190194
VERSION     NP_001190194.2
DBSOURCE    REFSEQ: accession NM_001203265.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Arikan,S., Ozturk,O., Duygulu,S., Atalay,E.O. and Atalay,A.
  TITLE     Associations of IL-17 and IL-17 receptor polymorphisms with
            Behcet's disease in Denizli Province of Turkey
  JOURNAL   Immunol Res 71 (4), 600-608 (2023)
   PUBMED   36701075
  REMARK    GeneRIF: Associations of IL-17 and IL-17 receptor polymorphisms
            with Behcet's disease in Denizli Province of Turkey.
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Kang,J.H., Park,S., Rho,J., Hong,E.J., Cho,Y.E., Won,Y.S. and
            Kwon,H.J.
  TITLE     IL-17A promotes Helicobacter pylori-induced gastric carcinogenesis
            via interactions with IL-17RC
  JOURNAL   Gastric Cancer 26 (1), 82-94 (2023)
   PUBMED   36125689
  REMARK    GeneRIF: IL-17A promotes Helicobacter pylori-induced gastric
            carcinogenesis via interactions with IL-17RC.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Goepfert,A., Barske,C., Lehmann,S., Wirth,E., Willemsen,J.,
            Gudjonsson,J.E., Ward,N.L., Sarkar,M.K., Hemmig,R., Kolbinger,F.
            and Rondeau,J.M.
  TITLE     IL-17-induced dimerization of IL-17RA drives the formation of the
            IL-17 signalosome to potentiate signaling
  JOURNAL   Cell Rep 41 (3), 111489 (2022)
   PUBMED   36260993
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Huang,X., Li,Z., Shen,X., Nie,N. and Shen,Y.
  TITLE     IL-17 upregulates MCP-1 expression via Act1 / TRAF6 / TAK1 in
            experimental autoimmune myocarditis
  JOURNAL   Cytokine 152, 155823 (2022)
   PUBMED   35183823
  REMARK    Erratum:[Cytokine. 2022 Jun;154:155879. doi:
            10.1016/j.cyto.2022.155879. PMID: 35413623]
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Schmidt,T., Luebbe,J., Kilian,C., Riedel,J.H., Hiekmann,S.,
            Asada,N., Ginsberg,P., Robben,L., Song,N., Kaffke,A., Peters,A.,
            Borchers,A., Flavell,R.A., Gagliani,N., Pelzcar,P., Huber,S.,
            Huber,T.B., Turner,J.E., Paust,H.J., Krebs,C.F. and Panzer,U.
  TITLE     IL-17 Receptor C Signaling Controls CD4+ TH17 Immune Responses and
            Tissue Injury in Immune-Mediated Kidney Diseases
  JOURNAL   J Am Soc Nephrol 32 (12), 3081-3098 (2021)
   PUBMED   35167487
  REMARK    GeneRIF: IL-17 Receptor C Signaling Controls CD4(+) TH17 Immune
            Responses and Tissue Injury in Immune-Mediated Kidney Diseases.
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Haudenschild,D.R., Curtiss,S.B., Moseley,T.A. and Reddi,A.H.
  TITLE     Generation of interleukin-17 receptor-like protein (IL-17RL) in
            prostate by alternative splicing of RNA
  JOURNAL   Prostate 66 (12), 1268-1274 (2006)
   PUBMED   16688746
  REMARK    GeneRIF: IL-17RL exists as multiple isoforms due to extensive
            alternative splicing. Changes in RNA IL-17RL splicing occur in
            advanced cancers.
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Gerritsen,M.E., Tomlinson,J.E., Zlot,C., Ziman,M. and Hwang,S.
  TITLE     Using gene expression profiling to identify the molecular basis of
            the synergistic actions of hepatocyte growth factor and vascular
            endothelial growth factor in human endothelial cells
  JOURNAL   Br J Pharmacol 140 (4), 595-610 (2003)
   PUBMED   14504135
  REMARK    Review article
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Haudenschild,D., Moseley,T., Rose,L. and Reddi,A.H.
  TITLE     Soluble and transmembrane isoforms of novel interleukin-17
            receptor-like protein by RNA splicing and expression in prostate
            cancer
  JOURNAL   J Biol Chem 277 (6), 4309-4316 (2002)
   PUBMED   11706037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018809.5.
            
            On May 31, 2019 this sequence version replaced NP_001190194.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that shares similarity with the interleukin-17 receptor (IL-17RA).
            Unlike IL-17RA, which is predominantly expressed in hemopoietic
            cells, and binds with high affinity to only IL-17A, this protein is
            expressed in nonhemopoietic tissues, and binds both IL-17A and
            IL-17F with similar affinities. The proinflammatory cytokines,
            IL-17A and IL-17F, have been implicated in the progression of
            inflammatory and autoimmune diseases. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            detected for this gene, and it has been proposed that soluble,
            secreted proteins lacking transmembrane and intracellular domains
            may function as extracellular antagonists to cytokine signaling.
            [provided by RefSeq, Feb 2011].
            
            Transcript Variant: This variant (6) lacks 2 in-frame coding exons
            (exons 7 and 12) compared to variant 1, resulting in a shorter
            isoform (6, also known as IL-17RCdelta7,12) missing 2 internal
            protein segments compared to isoform 1. It has been reported that
            isoforms lacking exon 12 lose the ability to bind cytokines, IL-17A
            and IL-17F (PMID:17911633).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF676032.1, SRR1660805.132671.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..688
                     /product="interleukin-17 receptor C isoform 6 precursor"
                     /note="IL17F receptor; IL-17RL; IL17Rhom; zcytoR14; IL-17
                     receptor C; interleukin-17 receptor homolog;
                     interleukin-17 receptor-like protein"
                     /calculated_mol_wt=72861
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     mat_peptide     21..688
                     /product="interleukin-17 receptor C isoform 6"
                     /calculated_mol_wt=72861
     Region          71..427
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          487..634
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..688
                     /gene="IL17RC"
                     /gene_synonym="CANDF9; IL17-RL; IL17RL"
                     /coded_by="NM_001203265.2:219..2285"
                     /note="isoform 6 precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS56241.1"
                     /db_xref="GeneID:84818"
                     /db_xref="HGNC:HGNC:18358"
                     /db_xref="MIM:610925"
ORIGIN      
        1 mpvpwfllsl algrspvvls lerlvgpqda thcspglscr lwdsdilclp gdivpapgpv
       61 lapthlqtel vlrcqketdc dlclrvavhl avhghweepe deekfggaad sgveeprnas
      121 lqaqvvlsfq ayptarcvll evqvpaalvq fgqsvgsvvy dcfeaalgse vriwsytqpr
      181 yekelnhtqq lpalpwlnvs adgdnvhlvl nvseeqhfgl slywnqvqgp pkprwhknlt
      241 gpqiitlnht dlvpclciqv wplepdsvrt nicpfredpr ahqnlwqaar lqlltlqswl
      301 ldapcslpae aalcwrapgg dpcqplvppl swenvtvdvn sseklqlqec lwadslgplk
      361 ddvllletrg pqdnrslcal epsgctslps kastraarlg eyllqdlqsg qclqlwdddl
      421 galwacpmdk yihkrwalvw lacllfaaal slilllkkdh akgwlrllkq dvrsgaaarg
      481 raalllysad dsgferlvga lasalcqlpl rvavdlwsrr elsaqgpvaw fhaqrrqtlq
      541 eggvvvllfs pgavalcsew lqdgvsgpga hgphdafras lscvlpdflq grapgsyvga
      601 cfdrllhpda vpalfrtvpv ftlpsqlpdf lgalqqprap rsgrlqerae qvsralqpal
      661 dsyfhppgtp apgrgvgpga gpgagdgt
//
LOCUS       NP_001308740             673 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform l [Homo sapiens].
ACCESSION   NP_001308740
VERSION     NP_001308740.1
DBSOURCE    REFSEQ: accession NM_001321811.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 17 and 18 encode the same isoform (l).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.120726.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..673
                     /product="E3 ubiquitin-protein ligase CBL-B isoform l"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=73781
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          622..662
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(624..625,627..629,631..632,637,641)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..673
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321811.2:915..2936"
                     /note="isoform l is encoded by transcript variant 17"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikscdng hcmlngthgp ssekksnipd lsiylkgdvf dsasdpvplp parpptrdnp
      481 khgsslnrtp sdydllippl gedafdalpp slppppppar hsliehskpp gsssrpssgq
      541 dlfllpsdpf vdlasgqvpl pparrlpgen vktnrtsqdy dqlpscsdgs qaparppkpr
      601 prrtapeihh rkphgpeaal envdakiakl mgegyafeev kraleiaqnn vevarsilre
      661 fafpppvspr lnl
//
LOCUS       NP_003036                629 aa            linear   PRI 20-NOV-2025
DEFINITION  high affinity cationic amino acid transporter 1 [Homo sapiens].
ACCESSION   NP_003036
VERSION     NP_003036.1
DBSOURCE    REFSEQ: accession NM_003045.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Gai,X., Liu,Y., Lan,X., Chen,L., Yuan,T., Xu,J., Li,Y., Zheng,Y.,
            Yan,Y., Yang,L., Fu,Y., Tang,S., Cao,S., Dai,X., Zhu,H., Geng,M.,
            Ding,J., Pu,C. and Huang,M.
  TITLE     Oncogenic KRAS Induces Arginine Auxotrophy and Confers a
            Therapeutic Vulnerability to SLC7A1 Inhibition in Non-Small Cell
            Lung Cancer
  JOURNAL   Cancer Res 84 (12), 1963-1977 (2024)
   PUBMED   38502865
  REMARK    GeneRIF: Oncogenic KRAS Induces Arginine Auxotrophy and Confers a
            Therapeutic Vulnerability to SLC7A1 Inhibition in Non-Small Cell
            Lung Cancer.
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Kurtyka,M., Wessely,F., Bau,S., Ifie,E., He,L., de Wit,N.M.,
            Pedersen,A.B.V., Keller,M., Webber,C., de Vries,H.E., Ansorge,O.,
            Betsholtz,C., De Bock,M., Chaves,C., Brodin,B., Nielsen,M.S.,
            Neuhaus,W., Bell,R.D., Letoha,T., Meyer,A.H., Leparc,G., Lenter,M.,
            Lesuisse,D., Cader,Z.M., Buckley,S.T., Loryan,I. and Pietrzik,C.U.
  TITLE     The solute carrier SLC7A1 may act as a protein transporter at the
            blood-brain barrier
  JOURNAL   Eur J Cell Biol 103 (2), 151406 (2024)
   PUBMED   38547677
  REMARK    GeneRIF: The solute carrier SLC7A1 may act as a protein transporter
            at the blood-brain barrier.
REFERENCE   5  (residues 1 to 629)
  AUTHORS   You,S., Han,X., Xu,Y., Sui,L., Song,K. and Yao,Q.
  TITLE     High expression of SLC7A1 in high-grade serous ovarian cancer
            promotes tumor progression and is involved in MAPK/ERK pathway and
            EMT
  JOURNAL   Cancer Med 13 (10), e7217 (2024)
   PUBMED   38752472
  REMARK    GeneRIF: High expression of SLC7A1 in high-grade serous ovarian
            cancer promotes tumor progression and is involved in MAPK/ERK
            pathway and EMT.
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Vekony,N., Wolf,S., Boissel,J.P., Gnauert,K. and Closs,E.I.
  TITLE     Human cationic amino acid transporter hCAT-3 is preferentially
            expressed in peripheral tissues
  JOURNAL   Biochemistry 40 (41), 12387-12394 (2001)
   PUBMED   11591158
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Kamath,S.G., Furesz,T.C., Way,B.A. and Smith,C.H.
  TITLE     Identification of three cationic amino acid transporters in
            placental trophoblast: cloning, expression, and characterization of
            hCAT-1
  JOURNAL   J Membr Biol 171 (1), 55-62 (1999)
   PUBMED   10485994
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Closs,E.I., Graf,P., Habermeier,A., Cunningham,J.M. and
            Forstermann,U.
  TITLE     Human cationic amino acid transporters hCAT-1, hCAT-2A, and
            hCAT-2B: three related carriers with distinct transport properties
  JOURNAL   Biochemistry 36 (21), 6462-6468 (1997)
   PUBMED   9174363
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Albritton,L.M., Bowcock,A.M., Eddy,R.L., Morton,C.C., Tseng,L.,
            Farrer,L.A., Cavalli-Sforza,L.L., Shows,T.B. and Cunningham,J.M.
  TITLE     The human cationic amino acid transporter (ATRC1): physical and
            genetic mapping to 13q12-q14
  JOURNAL   Genomics 12 (3), 430-434 (1992)
   PUBMED   1348489
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Yoshimoto,T., Yoshimoto,E. and Meruelo,D.
  TITLE     Molecular cloning and characterization of a novel human gene
            homologous to the murine ecotropic retroviral receptor
  JOURNAL   Virology 185 (1), 10-17 (1991)
   PUBMED   1718082
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL596114.10.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB105377.1, SRR14038191.1238336.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380752.10/ ENSP00000370128.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..629
                     /product="high affinity cationic amino acid transporter 1"
                     /note="ecotropic retroviral receptor; amino acid
                     transporter, cationic 1; CAT1; ecotropic retrovirus
                     receptor homolog; system Y+ basic amino acid transporter;
                     ecotropic retroviral leukemia receptor homolog; solute
                     carrier family 7 (cationic amino acid transporter, y+
                     system), member 1"
                     /calculated_mol_wt=67508
     Region          4..610
                     /region_name="2A0303"
                     /note="cationic amino acid transport permease; TIGR00906"
                     /db_xref="CDD:273330"
     Site            36..57
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            192..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P30825.1)"
     Site            235
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P30825.1)"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            288..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            338..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            385..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            409..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            493..513
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            527..551
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            560..580
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     Site            585..605
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P30825.1)"
     CDS             1..629
                     /gene="SLC7A1"
                     /gene_synonym="ATRC1; CAT-1; ERR; HCAT1; REC1L"
                     /coded_by="NM_003045.5:388..2277"
                     /db_xref="CCDS:CCDS9333.1"
                     /db_xref="GeneID:6541"
                     /db_xref="HGNC:HGNC:11057"
                     /db_xref="MIM:104615"
ORIGIN      
        1 mgckvllnig qqmlrrkvvd csreetrlsr clntfdlval gvgstlgagv yvlagavare
       61 nagpaivisf liaalasvla glcygefgar vpktgsayly syvtvgelwa fitgwnlils
      121 yiigtssvar awsatfdeli grpigefsrt hmtlnapgvl aenpdifavi iililtgllt
      181 lgvkesamvn kiftcinvlv lgfimvsgfv kgsvknwqlt eedfgntsgr lclnndtkeg
      241 kpgvggfmpf gfsgvlsgaa tcfyafvgfd ciattgeevk npqkaipvgi vasllicfia
      301 yfgvsaaltl mmpyfcldnn splpdafkhv gwegakyava vgslcalsas llgsmfpmpr
      361 viyamaedgl lfkflanvnd rtktpiiatl asgavaavma flfdlkdlvd lmsigtllay
      421 slvaacvlvl ryqpeqpnlv yqmastsdel dpadqnelas tndsqlgflp eaemfslkti
      481 lspknmepsk isglivnist sliavliitf civtvlgrea ltkgalwavf llagsallca
      541 vvtgviwrqp esktklsfkv pflpvlpils ifvnvylmmq ldqgtwvrfa vwmligfiiy
      601 fgyglwhsee asldadqart pdgnldqck
//
LOCUS       NP_001180442             501 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001180442
VERSION     NP_001180442.1
DBSOURCE    REFSEQ: accession NM_001193513.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Song,C.C., Liu,T., Hogstrand,C., Zhong,C.C., Zheng,H., Sun,L.H. and
            Luo,Z.
  TITLE     SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved
            in the regulation of zinc metabolism in Golgi apparatus
  JOURNAL   Cell Mol Life Sci 81 (1), 422 (2024)
   PUBMED   39367979
  REMARK    GeneRIF: SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409
            involved in the regulation of zinc metabolism in Golgi apparatus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Aktay,I., Billur,D., Tuncay,E. and Turan,B.
  TITLE     An Overexpression of SLC30A6 Gene Contributes to Cardiomyocyte
            Dysfunction via Affecting Mitochondria and Inducing Activations in
            K-Acetylation and Epigenetic Proteins
  JOURNAL   Biochem Genet 62 (4), 3198-3214 (2024)
   PUBMED   38091184
  REMARK    GeneRIF: An Overexpression of SLC30A6 Gene Contributes to
            Cardiomyocyte Dysfunction via Affecting Mitochondria and Inducing
            Activations in K-Acetylation and Epigenetic Proteins.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Zhu,B., Huo,R., Zhi,Q., Zhan,M., Chen,X. and Hua,Z.C.
  TITLE     Increased expression of zinc transporter ZIP4, ZIP11, ZnT1, and
            ZnT6 predicts poor prognosis in pancreatic cancer
  JOURNAL   J Trace Elem Med Biol 65, 126734 (2021)
   PUBMED   33631610
  REMARK    GeneRIF: Increased expression of zinc transporter ZIP4, ZIP11,
            ZnT1, and ZnT6 predicts poor prognosis in pancreatic cancer.
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Smith,J.L., Xiong,S., Markesbery,W.R. and Lovell,M.A.
  TITLE     Altered expression of zinc transporters-4 and -6 in mild cognitive
            impairment, early and late Alzheimer's disease brain
  JOURNAL   Neuroscience 140 (3), 879-888 (2006)
   PUBMED   16580781
  REMARK    GeneRIF: Our results show that Zn transporter-4 and Zn
            transporter-6 are significantly (P<0.05) increased in
            hippocampus/parahippocampal gyrus of early Alzheimer's disease and
            Alzheimer's disease subjects.
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Huang,L., Kirschke,C.P. and Gitschier,J.
  TITLE     Functional characterization of a novel mammalian zinc transporter,
            ZnT6
  JOURNAL   J Biol Chem 277 (29), 26389-26395 (2002)
   PUBMED   11997387
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB469378.1, BC066903.1,
            AK055663.1, BC032525.1, BG527678.1 and AA594503.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function as zinc transporters. This protein can regulate
            subcellular levels of zinc in the Golgi and vesicles. Expression of
            this gene is altered in the Alzheimer's disease brain plaques.
            [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066903.1, SRR1803616.35545.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..501
                     /product="zinc transporter 6 isoform 1"
                     /note="zinc transporter 6; solute carrier family 30 (zinc
                     transporter), member 6"
                     /calculated_mol_wt=55664
     Region          113..371
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     CDS             1..501
                     /gene="SLC30A6"
                     /gene_synonym="MST103; MSTP103; ZNT6"
                     /coded_by="NM_001193513.3:38..1543"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54341.1"
                     /db_xref="GeneID:55676"
                     /db_xref="HGNC:HGNC:19305"
                     /db_xref="MIM:611148"
ORIGIN      
        1 mgtihlfrkp qrsffgkllr efrlvaadrr swkillfgvi nlictgfllm wcsstnsial
       61 taytyltifd lfrdgvspfw lgwsqtpdlk wsthlglpkc wdnrrelpcl snslmtclis
      121 ywvtlrkpsp vysfgferle vlavfastvl aqlgalfilk esaerfleqp eihtgrllvg
      181 tfvalcfnlf tmlsirnkpf ayvseaasts wlqehvadls rslcgiipgl ssiflprmnp
      241 fvlidlagaf alcitymlie innyfavdta saiaialmtf gtmypmsvys gkvllqttpp
      301 hvigqldkli revstldgvl evrnehfwtl gfgslagsvh vrirrdaneq mvlahvtnrl
      361 ytlvstltvq ifkddwirpa llsgpvaanv lnfsdhhvip mpllkgtddl npvtstpakp
      421 sspppefsfn tpgknvnpvi llntqtrpyg fglnhghtpy ssmlnqglgv pgigatqglr
      481 tgftnipsry gtnnrigqpr p
//
LOCUS       NP_001351754             409 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 12 [Homo sapiens].
ACCESSION   NP_001351754 XP_005269019
VERSION     NP_001351754.1
DBSOURCE    REFSEQ: accession NM_001364825.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079684.16 and AC079601.25.
            
            On Jul 12, 2018 this sequence version replaced XP_005269019.1.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380201.19485.7, AK299951.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..409
                     /product="periphilin-1 isoform 12"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=46704
     Region          211..>267
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Region          <360..>395
                     /region_name="HERV-K_REC"
                     /note="Rec (regulator of expression encoded by corf) of
                     HERV-K-113; pfam15695"
                     /db_xref="CDD:292323"
     CDS             1..409
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001364825.2:84..1313"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdesgyr wtrddhsasr qpeyrdmrdg frrksfyssh
       61 yarerspykr dntffrespv grkdsphsrs gssvssrsys persksysfh qsqhrnkerp
      121 vqslktsrdt spssgsavss skvldkpsrl tekelaeaas kwaaekleks desnlpeise
      181 yeagstaplf tdqpeepesn tthgielfed sqlttrskai asktkeieqv yrqdcetfgm
      241 vvkmliekdp sleksiqfal rqnlheiesa gqtwqqvppv rntemdhdgt penegeetaq
      301 shdasnhtiv glgpnqvpem kettlqapqp pqapqplqpr kkrvrrttql rrttgapdit
      361 wgmlkkttqe aerillrtqt pftpenlfla mlsvvhcnsr kdvkpenkq
//
LOCUS       NP_694947                164 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich single-pass membrane protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_694947
VERSION     NP_694947.1
DBSOURCE    REFSEQ: accession NM_153215.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC028000.1 and U90094.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028000.1, SRR5189655.45685.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316436.4/ ENSP00000315081.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..164
                     /product="leucine-rich single-pass membrane protein 2
                     isoform 1"
                     /calculated_mol_wt=17737
     Region          13..162
                     /region_name="DUF4714"
                     /note="Domain of unknown function (DUF4714); pfam15833"
                     /db_xref="CDD:464901"
     Site            97..117
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N112.1)"
     CDS             1..164
                     /gene="LSMEM2"
                     /gene_synonym="C3orf45"
                     /coded_by="NM_153215.3:28..522"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2814.1"
                     /db_xref="GeneID:132228"
                     /db_xref="HGNC:HGNC:26781"
                     /db_xref="MIM:621358"
ORIGIN      
        1 mpslapdcpl lampeetqed svapmmpsqr srgplapnhv hevclhqves isdlhsgagt
       61 lrpylteear pwdellgvlp pslcaqagcs pvyrrggfll llallvltcl vlallavyls
      121 vlqseslril ahtlrtqeet llklrlasls qlrrlnssea qaps
//
LOCUS       NP_036471                294 aa            linear   PRI 20-NOV-2025
DEFINITION  tetraspanin-15 isoform 1 [Homo sapiens].
ACCESSION   NP_036471
VERSION     NP_036471.1
DBSOURCE    REFSEQ: accession NM_012339.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 294)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 294)
  AUTHORS   Lipper,C.H., Gabriel,K.H., Seegar,T.C.M., Durr,K.L., Tomlinson,M.G.
            and Blacklow,S.C.
  TITLE     Crystal structure of the Tspan15 LEL domain reveals a conserved
            ADAM10 binding site
  JOURNAL   Structure 30 (2), 206-214 (2022)
   PUBMED   34739841
  REMARK    GeneRIF: Crystal structure of the Tspan15 LEL domain reveals a
            conserved ADAM10 binding site.
REFERENCE   3  (residues 1 to 294)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 294)
  AUTHORS   Koo,C.Z., Harrison,N., Noy,P.J., Szyroka,J., Matthews,A.L.,
            Hsia,H.E., Muller,S.A., Tushaus,J., Goulding,J., Willis,K.,
            Apicella,C., Cragoe,B., Davis,E., Keles,M., Malinova,A.,
            McFarlane,T.A., Morrison,P.R., Nguyen,H.T.H., Sykes,M.C., Ahmed,H.,
            Di Maio,A., Seipold,L., Saftig,P., Cull,E., Pliotas,C.,
            Rubinstein,E., Poulter,N.S., Briddon,S.J., Holliday,N.D.,
            Lichtenthaler,S.F. and Tomlinson,M.G.
  TITLE     The tetraspanin Tspan15 is an essential subunit of an ADAM10
            scissor complex
  JOURNAL   J Biol Chem 295 (36), 12822-12839 (2020)
   PUBMED   32111735
  REMARK    GeneRIF: The tetraspanin Tspan15 is an essential subunit of an
            ADAM10 scissor complex.
REFERENCE   5  (residues 1 to 294)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 294)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 294)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 294)
  AUTHORS   Semplici,F., Meggio,F., Pinna,L.A. and Oliviero,S.
  TITLE     CK2-dependent phosphorylation of the E2 ubiquitin conjugating
            enzyme UBC3B induces its interaction with beta-TrCP and enhances
            beta-catenin degradation
  JOURNAL   Oncogene 21 (25), 3978-3987 (2002)
   PUBMED   12037680
REFERENCE   9  (residues 1 to 294)
  AUTHORS   Berditchevski,F.
  TITLE     Complexes of tetraspanins with integrins: more than meets the eye
  JOURNAL   J Cell Sci 114 (Pt 23), 4143-4151 (2001)
   PUBMED   11739647
  REMARK    Review article
REFERENCE   10 (residues 1 to 294)
  AUTHORS   Serru,V., Dessen,P., Boucheix,C. and Rubinstein,E.
  TITLE     Sequence and expression of seven new tetraspans
  JOURNAL   Biochim Biophys Acta 1478 (1), 159-163 (2000)
   PUBMED   10719184
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016821.9, DR158973.1,
            BC003157.1, CA454790.1, BM972680.1 and AI612860.1.
            
            Summary: The protein encoded by this gene is a member of the
            transmembrane 4 superfamily, also known as the tetraspanin family.
            Most of these members are cell-surface proteins that are
            characterized by the presence of four hydrophobic domains. The
            proteins mediate signal transduction events that play a role in the
            regulation of cell development, activation, growth and motility.
            The use of alternate polyadenylation sites has been found for this
            gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.346384.1,
                                           SRR3476690.1138911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373290.7/ ENSP00000362387.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..294
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..294
                     /product="tetraspanin-15 isoform 1"
                     /note="transmembrane 4 superfamily member tetraspan NET-7;
                     transmembrane 4 superfamily member 15; tspan-15"
                     /calculated_mol_wt=33034
     Region          20..>157
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            24..44
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95858.1)"
     Site            63..83
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95858.1)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95858.1)"
     Region          114..231
                     /region_name="penumbra_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), penumbra_like family.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03158"
                     /db_xref="CDD:239411"
     Site            order(115,120,124,126..127,130,144,147..148,151..152)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239411"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95858.1)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255, ECO:0000269|PubMed:34739841;
                     propagated from UniProtKB/Swiss-Prot (O95858.1)"
     Site            230
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95858.1)"
     Site            236..256
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95858.1)"
     CDS             1..294
                     /gene="TSPAN15"
                     /gene_synonym="2700063A19Rik; NET-7; NET7; TM4SF15"
                     /coded_by="NM_012339.5:131..1015"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7294.1"
                     /db_xref="GeneID:23555"
                     /db_xref="HGNC:HGNC:23298"
                     /db_xref="MIM:613140"
ORIGIN      
        1 mprgdseqvr ycarfsylwl kfsliiystv fwligalvls vgiyaeverq kyktlesafl
       61 apaiilillg vvmfmvsfig vlaslrdnly llqafmyilg iclimeligg vvaltfrnqt
      121 idflndnirr gienyyddld fknimdfvqk kfkccggedy rdwsknqyhd csapgplacg
      181 vpytccirnt tevvntmcgy ktidkerfsv qdviyvrgct naviiwfmdn ytimagillg
      241 illpqflgvl ltllyitrve diimehsvtd gllgpgakps veaagtgccl cypn
//
LOCUS       NP_001886                391 aa            linear   PRI 20-NOV-2025
DEFINITION  casein kinase II subunit alpha isoform a [Homo sapiens].
ACCESSION   NP_001886
VERSION     NP_001886.1
DBSOURCE    REFSEQ: accession NM_001895.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Goel,H. and O'Donnell,S.
  TITLE     Inherited loss of function variant in CSNK2A1: the oldest reported
            cases of Okur-Chung syndrome in a single family
  JOURNAL   Clin Dysmorphol 33 (3), 121-124 (2024)
   PUBMED   38818820
  REMARK    GeneRIF: Inherited loss of function variant in CSNK2A1: the oldest
            reported cases of Okur-Chung syndrome in a single family.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Ampofo,E., Pack,M., Wrublewsky,S., Boewe,A.S., Spigelman,A.F.,
            Koch,H., MacDonald,P.E., Laschke,M.W., Montenarh,M. and Gotz,C.
  TITLE     CK2 activity is crucial for proper glucagon expression
  JOURNAL   Diabetologia 67 (7), 1368-1385 (2024)
   PUBMED   38503901
  REMARK    GeneRIF: CK2 activity is crucial for proper glucagon expression.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Liu,Z.D., Shi,Y.H., Xu,Q.C., Zhao,G.Y., Zhu,Y.Q., Li,F.X., Ma,M.J.,
            Ye,J.Y., Huang,X.T., Wang,X.Y., Xu,X., Wang,J.Q., Zhao,W. and
            Yin,X.Y.
  TITLE     CSNK2A1 confers gemcitabine resistance to pancreatic ductal
            adenocarcinoma via inducing autophagy
  JOURNAL   Cancer Lett 585, 216640 (2024)
   PUBMED   38290659
  REMARK    GeneRIF: CSNK2A1 confers gemcitabine resistance to pancreatic
            ductal adenocarcinoma via inducing autophagy.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Nan,H., Chu,M., Zhang,J., Jiang,D., Wang,Y. and Wu,L.
  TITLE     Okur-Chung neurodevelopmental syndrome: Implications for phenotype
            and genotype expansion
  JOURNAL   Mol Genet Genomic Med 12 (3), e2398 (2024)
   PUBMED   38444259
  REMARK    GeneRIF: Okur-Chung neurodevelopmental syndrome: Implications for
            phenotype and genotype expansion.
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Chung,W. and Okur,V.
  TITLE     Okur-Chung Neurodevelopmental Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35679446
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Russo,G.L., Vandenberg,M.T., Yu,I.J., Bae,Y.S., Franza,B.R. Jr. and
            Marshak,D.R.
  TITLE     Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the
            HeLa cell division cycle
  JOURNAL   J Biol Chem 267 (28), 20317-20325 (1992)
   PUBMED   1400350
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Lin,A., Frost,J., Deng,T., Smeal,T., al-Alawi,N., Kikkawa,U.,
            Hunter,T., Brenner,D. and Karin,M.
  TITLE     Casein kinase II is a negative regulator of c-Jun DNA binding and
            AP-1 activity
  JOURNAL   Cell 70 (5), 777-789 (1992)
   PUBMED   1516134
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1423636]
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Sacks,D.B., Davis,H.W., Crimmins,D.L. and McDonald,J.M.
  TITLE     Insulin-stimulated phosphorylation of calmodulin
  JOURNAL   Biochem J 286 (Pt 1) (Pt 1), 211-216 (1992)
   PUBMED   1520270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU133318.1, M55265.1,
            BC053532.1 and AL049761.11.
            
            Summary: Casein kinase II is a serine/threonine protein kinase that
            phosphorylates acidic proteins such as casein. It is involved in
            various cellular processes, including cell cycle control,
            apoptosis, and circadian rhythm. The kinase exists as a tetramer
            and is composed of an alpha, an alpha-prime, and two beta subunits.
            The alpha subunits contain the catalytic activity while the beta
            subunits undergo autophosphorylation. The protein encoded by this
            gene represents the alpha subunit. Multiple transcript variants
            encoding different protein isoforms have been found for this gene.
            [provided by RefSeq, Apr 2018].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 4 and 5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1706663.1,
                                           SRR1803615.248400.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..391
                     /product="casein kinase II subunit alpha isoform a"
                     /EC_number="2.7.11.1"
                     /note="CK2 catalytic subunit alpha; protein kinase CK2;
                     casein kinase II alpha 1 subunit; casein kinase II alpha 1
                     polypeptide pseudogene; casein kinase 2, alpha 1
                     polypeptide"
                     /calculated_mol_wt=45013
     Region          20..325
                     /region_name="STKc_CK2_alpha"
                     /note="Catalytic subunit (alpha) of the Serine/Threonine
                     Kinase, Casein Kinase 2; cd14132"
                     /db_xref="CDD:271034"
     Site            order(36,39..41,67,69,101,103..104,110)
                     /site_type="other"
                     /note="allosteric inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..42,50,54,103)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..41,57,59,103)
                     /site_type="other"
                     /note="CK2 beta interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Region          36..41
                     /region_name="Interaction with beta subunit.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P68400.1)"
     Site            order(45..49,53,66,68,80,95,113..116,120,122..123,156,158,
                     160..161,163,175,178,189,191..194,196,235)
                     /site_type="active"
                     /db_xref="CDD:271034"
     Site            order(47..48,50..51,53,66,68,95,113..114,116,160..161,163,
                     174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271034"
     Site            order(80,122,156,158,178,189,191..194,196,235)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(174..184,189..196)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271034"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     CDS             1..391
                     /gene="CSNK2A1"
                     /gene_synonym="CK2A1; Cka1; Cka2; CKII; OCNDS"
                     /coded_by="NM_001895.4:229..1404"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13003.1"
                     /db_xref="GeneID:1457"
                     /db_xref="HGNC:HGNC:2457"
                     /db_xref="MIM:115440"
ORIGIN      
        1 msgpvpsrar vytdvnthrp reywdyeshv vewgnqddyq lvrklgrgky sevfeainit
       61 nnekvvvkil kpvkkkkikr eikilenlrg gpniitladi vkdpvsrtpa lvfehvnntd
      121 fkqlyqtltd ydirfymyei lkaldychsm gimhrdvkph nvmidhehrk lrlidwglae
      181 fyhpgqeynv rvasryfkgp ellvdyqmyd ysldmwslgc mlasmifrke pffhghdnyd
      241 qlvriakvlg tedlydyidk ynieldprfn dilgrhsrkr werfvhsenq hlvspealdf
      301 ldkllrydhq srltareame hpyfytvvkd qarmgsssmp ggstpvssan mmsgissvpt
      361 psplgplags pviaaanplg mpvpaaagaq q
//
LOCUS       NP_004254                770 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4F isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004254 NP_060994
VERSION     NP_004254.2
DBSOURCE    REFSEQ: accession NM_004263.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Fan,Q., Barathi,V.A., Cheng,C.Y., Zhou,X., Meguro,A., Nakata,I.,
            Khor,C.C., Goh,L.K., Li,Y.J., Lim,W., Ho,C.E., Hawthorne,F.,
            Zheng,Y., Chua,D., Inoko,H., Yamashiro,K., Ohno-Matsui,K.,
            Matsuo,K., Matsuda,F., Vithana,E., Seielstad,M., Mizuki,N.,
            Beuerman,R.W., Tai,E.S., Yoshimura,N., Aung,T., Young,T.L.,
            Wong,T.Y., Teo,Y.Y. and Saw,S.M.
  TITLE     Genetic variants on chromosome 1q41 influence ocular axial length
            and high myopia
  JOURNAL   PLoS Genet 8 (6), e1002753 (2012)
   PUBMED   22685421
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Parrinello,S., Noon,L.A., Harrisingh,M.C., Wingfield Digby,P.,
            Rosenberg,L.H., Cremona,C.A., Echave,P., Flanagan,A.M., Parada,L.F.
            and Lloyd,A.C.
  TITLE     NF1 loss disrupts Schwann cell-axonal interactions: a novel role
            for semaphorin 4F
  JOURNAL   Genes Dev 22 (23), 3335-3348 (2008)
   PUBMED   19056885
  REMARK    GeneRIF: Sema4F levels were strongly reduced in a panel of human
            neurofibromas, confirming the relevance of these findings to the
            human disease.
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Ayala,G.E., Dai,H., Powell,M., Li,R., Ding,Y., Wheeler,T.M.,
            Shine,D., Kadmon,D., Thompson,T., Miles,B.J., Ittmann,M.M. and
            Rowley,D.
  TITLE     Cancer-related axonogenesis and neurogenesis in prostate cancer
  JOURNAL   Clin Cancer Res 14 (23), 7593-7603 (2008)
   PUBMED   19047084
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Park,Y.D., Park,D., Bhak,J. and Yang,J.M.
  TITLE     Proteomic approaches to the analysis of atopic dermatitis and new
            insights from interactomics
  JOURNAL   Proteomics Clin Appl 2 (3), 290-300 (2008)
   PUBMED   21136834
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Francks,C., Fisher,S.E., Olson,R.K., Pennington,B.F., Smith,S.D.,
            DeFries,J.C. and Monaco,A.P.
  TITLE     Fine mapping of the chromosome 2p12-16 dyslexia susceptibility
            locus: quantitative association analysis and positional candidate
            genes SEMA4F and OTX1
  JOURNAL   Psychiatr Genet 12 (1), 35-41 (2002)
   PUBMED   11901358
  REMARK    GeneRIF: Fine mapping of the chromosome 2p12-16 dyslexia
            susceptibility candidate gene
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Schultze,W., Eulenburg,V., Lessmann,V., Herrmann,L., Dittmar,T.,
            Gundelfinger,E.D., Heumann,R. and Erdmann,K.S.
  TITLE     Semaphorin4F interacts with the synapse-associated protein
            SAP90/PSD-95
  JOURNAL   J Neurochem 78 (3), 482-489 (2001)
   PUBMED   11483650
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Encinas,J.A., Kikuchi,K., Chedotal,A., de Castro,F., Goodman,C.S.
            and Kimura,T.
  TITLE     Cloning, expression, and genetic mapping of Sema W, a member of the
            semaphorin family
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2491-2496 (1999)
   PUBMED   10051670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC306380.1, AL136552.1,
            AC007387.4 and CK905501.1.
            
            On Apr 4, 2002 this sequence version replaced NP_004254.1.
            
            Summary: This gene encodes a transmembrane class IV semaphorin
            family protein, which plays a role in neural development. This gene
            may be involved in neurogenesis in prostate cancer, the development
            of neurofibromas, and breast cancer tumorigenesis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.241466.1,
                                           SRR1660807.58907.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357877.7/ ENSP00000350547.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..770
                     /product="semaphorin-4F isoform 1 precursor"
                     /note="semaphorin M; semaphorin-4F; semaphorin-W; sema
                     domain immunoglobulin domain transmembrane domain (TM) and
                     short cytoplasmic domain (semaphorin) 4F; sema domain,
                     immunoglobulin domain (Ig), transmembrane domain (TM) and
                     short cytoplasmic domain, (semaphorin) 4F"
                     /calculated_mol_wt=80219
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3311
     mat_peptide     35..770
                     /product="Semaphorin-4F. /id=PRO_0000032330"
                     /note="propagated from UniProtKB/Swiss-Prot (O95754.2)"
                     /calculated_mol_wt=80219
     Region          52..511
                     /region_name="Sema_4F"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4F (Sema4F); cd11261"
                     /db_xref="CDD:200522"
     Site            64
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(114..116,172,193,195..196,198,214,217,219,224,256,
                     280..284,286,365..366,402,406,409)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            133
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            order(257..258,260,263..265,299,302..304,306,308,332..334,
                     338..339,415,430)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200522"
     Site            509
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Region          512..563
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          576..770
                     /region_name="Sema4F_C"
                     /note="Semaphorin 4F C-terminal; pfam19428"
                     /db_xref="CDD:437260"
     Site            660..680
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95754.2)"
     Region          696..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95754.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z123; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z123; propagated from
                     UniProtKB/Swiss-Prot (O95754.2)"
     Region          768..770
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:Q9Z123"
                     /note="propagated from UniProtKB/Swiss-Prot (O95754.2)"
     CDS             1..770
                     /gene="SEMA4F"
                     /gene_synonym="M-SEMA; m-Sema-M; PRO2353; S4F; SEMAM;
                     SEMAW"
                     /coded_by="NM_004263.5:131..2443"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1955.1"
                     /db_xref="GeneID:10505"
                     /db_xref="HGNC:HGNC:10734"
                     /db_xref="MIM:603706"
ORIGIN      
        1 mpasaarprp gpgqptaspf pllllavlsg pvsgrvprsv prtslpisea dscltrfavp
       61 htynysvllv dpashtlyvg ardtifalsl pfsgerprri dwmvpeahrq ncrkkgkked
      121 echnfvqila ianashlltc gtfafdpkcg vidvsrfqqv erlesgrgkc pfepaqrsaa
      181 vmaggvlyaa tvknylgtep iitravgrae dwirtdtlps wlnapafvaa valspaewgd
      241 edgddeiyff ftetsrafds yerikvprva rvcagdlggr ktlqqrwttf lkadllcpgp
      301 ehgrassvlq dvavlrpelg agtpifygif ssqwegatis avcafrpqdi rtvlngpfre
      361 lkhdcnrglp vvdndvpqpr pgecitnnmk lrhfgsslsl pdrvltfird hplmdrpvfp
      421 adghpllvtt dtaylrvvah rvtslsgkey dvlylgtedg hlhravriga qlsvledlal
      481 fpepqpvenm klyhswllvg srtevtqvnt tncgrlqscs ecilaqdpvc awsfrldecv
      541 ahagehrglv qdiesadvss lcpkepgerp vvfevpvata ahvvlpcsps sawascvwhq
      601 psgvtaltpr rdglevvvtp gamgayacec qeggaahvva ayslvwgsqr dapsrahtvg
      661 aglagfflgi laasltlili grrqqrrrqr ellardkvgl dlgappsgtt sysqdppsps
      721 pederlplal akrgsgfggf sppflldpcp spahirltga platcdetsi
//
LOCUS       NP_057520               1012 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD finger protein 20 [Homo sapiens].
ACCESSION   NP_057520
VERSION     NP_057520.2
DBSOURCE    REFSEQ: accession NM_016436.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1012)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1012)
  AUTHORS   Zhang,Z., Wang,L., Zhao,L., Wang,Q., Yang,C., Zhang,M., Wang,B.,
            Jiang,K., Ye,Y., Wang,S. and Shen,Z.
  TITLE     N6-methyladenosine demethylase ALKBH5 suppresses colorectal cancer
            progression potentially by decreasing PHF20 mRNA methylation
  JOURNAL   Clin Transl Med 12 (8), e940 (2022)
   PUBMED   35979628
  REMARK    GeneRIF: N6-methyladenosine demethylase ALKBH5 suppresses
            colorectal cancer progression potentially by decreasing PHF20 mRNA
            methylation.
REFERENCE   3  (residues 1 to 1012)
  AUTHORS   Liu,X., Zhang,Z., Kan,S., Lv,Z., Zhou,S., Liu,X., Jing,P. and Xu,W.
  TITLE     PHF20 inhibition promotes apoptosis and cisplatin chemosensitivity
            via the OCT4-p-STAT3-MCL1 signaling pathway in hypopharyngeal
            squamous cell carcinoma
  JOURNAL   Int J Oncol 59 (1) (2021)
   PUBMED   33982773
  REMARK    GeneRIF: PHF20 inhibition promotes apoptosis and cisplatin
            chemosensitivity via the OCT4pSTAT3MCL1 signaling pathway in
            hypopharyngeal squamous cell carcinoma.
REFERENCE   4  (residues 1 to 1012)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1012)
  AUTHORS   Long,W., Zhao,W., Ning,B., Huang,J., Chu,J., Li,L., Ma,Q., Xing,C.,
            Wang,H.Y., Liu,Q. and Wang,R.F.
  TITLE     PHF20 collaborates with PARP1 to promote stemness and
            aggressiveness of neuroblastoma cells through activation of SOX2
            and OCT4
  JOURNAL   J Mol Cell Biol 10 (2), 147-160 (2018)
   PUBMED   29452418
  REMARK    GeneRIF: PHF20 interacts with poly(ADP-ribose) polymerase 1 (PARP1)
            and directly binds to promoter regions of octamer-binding
            transcription factor 4 (OCT4) and sex determining region Y-box 2
            (SOX2) to modulate a histone mark associated with active
            transcription, trimethylation of lysine 4 on histone H3 protein
            subunit (H3K4me3).
REFERENCE   6  (residues 1 to 1012)
  AUTHORS   Pallasch,C.P., Struss,A.K., Munnia,A., Konig,J., Steudel,W.I.,
            Fischer,U. and Meese,E.
  TITLE     Autoantibodies against GLEA2 and PHF3 in glioblastoma:
            tumor-associated autoantibodies correlated with prolonged survival
  JOURNAL   Int J Cancer 117 (3), 456-459 (2005)
   PUBMED   15906353
  REMARK    GeneRIF: Survival of patients with GLEA2 antibodies was increased
            to 17.4 months and for patients with PHF3 antibodies to 14.7
            months, as compared to 7.2 months for patients without GLEA2 or
            PHF3 antibodies in glioblastoma.
REFERENCE   7  (residues 1 to 1012)
  AUTHORS   Behrends,U., Schneider,I., Rossler,S., Frauenknecht,H., Golbeck,A.,
            Lechner,B., Eigenstetter,G., Zobywalski,C., Muller-Weihrich,S.,
            Graubner,U., Schmid,I., Sackerer,D., Spath,M., Goetz,C., Prantl,F.,
            Asmuss,H.P., Bise,K. and Mautner,J.
  TITLE     Novel tumor antigens identified by autologous antibody screening of
            childhood medulloblastoma cDNA libraries
  JOURNAL   Int J Cancer 106 (2), 244-251 (2003)
   PUBMED   12800201
REFERENCE   8  (residues 1 to 1012)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   9  (residues 1 to 1012)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 1012)
  AUTHORS   Fischer,U., Struss,A.K., Hemmer,D., Pallasch,C.P., Steudel,W.I. and
            Meese,E.
  TITLE     Glioma-expressed antigen 2 (GLEA2): a novel protein that can elicit
            immune responses in glioblastoma patients and some controls
  JOURNAL   Clin Exp Immunol 126 (2), 206-213 (2001)
   PUBMED   11703362
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC093405.1, AY027523.1, AL137330.1 and AL109965.34.
            
            On Jan 2, 2002 this sequence version replaced NP_057520.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150178.1, SRR1660803.41886.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374012.8/ ENSP00000363124.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22-q11.23"
     Protein         1..1012
                     /product="PHD finger protein 20"
                     /note="glioma-expressed antigen 2; hepatocellular
                     carcinoma-associated antigen 58; transcription factor TZP;
                     novel zinc finger protein; tudor domain containing 20A"
                     /calculated_mol_wt=115255
     Region          13..69
                     /region_name="MBT_PHF20L1-like"
                     /note="malignant brain tumor (MBT) repeat found in PHD
                     finger protein 20-like protein 1 (PHF20L1) and similar
                     domains; cd20104"
                     /db_xref="CDD:439094"
     Site            order(23,26..27,29,47,50,54)
                     /site_type="other"
                     /note="putative methyllysine peptide binding site
                     [polypeptide binding]"
                     /db_xref="CDD:439094"
     Region          87..139
                     /region_name="Tudor_PHF20"
                     /note="Tudor domain found in PHD finger protein 20 (PHF20)
                     and similar proteins; cd20453"
                     /db_xref="CDD:410524"
     Region          142..336
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Region          176..280
                     /region_name="DUF3776"
                     /note="Protein of unknown function (DUF3776); pfam12618"
                     /db_xref="CDD:463645"
     Region          481..611
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Region          654..697
                     /region_name="PHD_PHF20"
                     /note="PHD finger found in PHD finger protein 20 (PHF20);
                     cd15634"
                     /db_xref="CDD:277104"
     Site            order(654,665..669,673,692)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277104"
     Site            843
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Region          866..912
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Site            878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BVI0.2)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BVI0.2)"
     CDS             1..1012
                     /gene="PHF20"
                     /gene_synonym="C20orf104; GLEA2; HCA58; NZF; TDRD20A; TZP"
                     /coded_by="NM_016436.5:98..3136"
                     /db_xref="CCDS:CCDS13268.1"
                     /db_xref="GeneID:51230"
                     /db_xref="HGNC:HGNC:16098"
                     /db_xref="MIM:610335"
ORIGIN      
        1 mtkhppnrrg isfevgaqle ardrlknwyp ahiedidyee gkvlihfkrw nhrydewfcw
       61 dspylrplek iqlrkeglhe edgssefqin eqvlacwsdc rfypakvtav nkdgtytvkf
      121 ydgvvqtvkh ihvkafskdq nivgnarpke tdhkslsssp dkrekfkeqr katvnvkkdk
      181 edkplktekr pkqpdkegkl icsekgkvse kslpkneked kenisendre ysgdaqvdkk
      241 pendivkspq enlrepkrkr grppsiapta vdsnsqtlqp itlelrrrki skgcevplkr
      301 prldknssqe ksknysentd kdlsrrrssr lstngtheil dpdlvvsdlv dtdplqdtls
      361 stkeseegql ksaleagqvs saltchsfgd gsgaagleln cpsmgentmk teptsplvel
      421 qeistvevtn tfkktddfgs snapavdldh kfrckvvdcl kffrkakllh yhmkyfhgme
      481 kslepeespg krhvqtrgps asdkpsqetl trkrvsassp ttkdkeknke kkfkefvrvk
      541 pkkkkkkkkk tkpecpcsee isdtsqepsp pkafavtrcg sshkpgvhms pqlhgpesgh
      601 hkgkvkalee dnlsessses flwsddeygq dvdvttnpde eldgddrydf evvrcicevq
      661 eendfmiqce ecqcwqhgvc mglleenvpe kytcyvcqdp pgqrpgfkyw ydkewlsrgh
      721 mhglafleen yshqnakkiv athqllgdvq rvievlhglq lkmsilqsre hpdlplwcqp
      781 wkqhsgegrs hfrnipvtdt rskeeapsyr tlngavekpr plalplprsv eesyitsehc
      841 yqkprayypa veqklvvetr gsalddavnp lhengddsls prlgwpldqd rskgdsdpkp
      901 gspkvkeyvs kkalpeeapa rklldrggeg llssqhqwqf nllthveslq devthrmdsi
      961 ekeldvlesw ldytgelepp eplarlpqlk hcikqllmdl gkvqqialcc st
//
LOCUS       NP_055746                881 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 1 [Homo
            sapiens].
ACCESSION   NP_055746 XP_375651
VERSION     NP_055746.3
DBSOURCE    REFSEQ: accession NM_014931.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 881)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 881)
  AUTHORS   Han,K.J., Mikalayeva,V., Gerber,S.A., Kettenbach,A.N.,
            Skeberdis,V.A. and Prekeris,R.
  TITLE     Rab40c regulates focal adhesions and PP6 activity by controlling
            ANKRD28 ubiquitylation
  JOURNAL   Life Sci Alliance 5 (9), e202101346 (2022)
   PUBMED   35512830
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 881)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 881)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 881)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 881)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   7  (residues 1 to 881)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   8  (residues 1 to 881)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
REFERENCE   9  (residues 1 to 881)
  AUTHORS   Nasu-Nishimura,Y., Hayashi,T., Ohishi,T., Okabe,T., Ohwada,S.,
            Hasegawa,Y., Senda,T., Toyoshima,C., Nakamura,T. and Akiyama,T.
  TITLE     Role of the Rho GTPase-activating protein RICS in neurite outgrowth
  JOURNAL   Genes Cells 11 (6), 607-614 (2006)
   PUBMED   16716191
REFERENCE   10 (residues 1 to 881)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116342.2, AL544921.3, BG772019.1, BC002799.2 and AC010327.8.
            
            On Jul 5, 2007 this sequence version replaced NP_055746.2.
            
            Summary: Protein phosphatase regulatory subunits, such as SAPS1,
            modulate the activity of protein phosphatase catalytic subunits by
            restricting substrate specificity, recruiting substrates, and
            determining the intracellular localization of the holoenzyme. SAPS1
            is a regulatory subunit for the protein phosphatase-6 catalytic
            subunit (PPP6C; MIM 612725) (Stefansson and Brautigan, 2006 [PubMed
            16769727]).[supplied by OMIM, Nov 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094753.1, AB029038.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000412770.7/ ENSP00000414202.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..881
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..881
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 1"
                     /note="SAPS domain family, member 1"
                     /calculated_mol_wt=96593
     Region          10..403
                     /region_name="Interaction with PPP6C"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Region          128..519
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSI3; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Region          621..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Region          <688..879
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q9UPN7.5)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TSI3; propagated from
                     UniProtKB/Swiss-Prot (Q9UPN7.5)"
     CDS             1..881
                     /gene="PPP6R1"
                     /gene_synonym="KIAA1115; PP6R1; SAP190; SAPS1"
                     /coded_by="NM_014931.4:590..3235"
                     /db_xref="CCDS:CCDS46186.1"
                     /db_xref="GeneID:22870"
                     /db_xref="HGNC:HGNC:29195"
                     /db_xref="MIM:610875"
ORIGIN      
        1 mfwkfdlhts shldtllere dlslpellde edvlqeckvv nrklldfllq pphlqamvaw
       61 vtqeppdsge erlrykypsv aceiltsdvp qindalgade sllnrlygfl qstgslnpll
      121 asffskvmgi linrktdqlv sflrkkddfv dlllqhigts aimdlllrll tcverpqlrq
      181 dvvnwlneek ivqrlieqih pskdenqhsn asqslcdiir lsreqmiqvq dspepdqlla
      241 tlekqetieq llsnmfegeq sqsvivsgiq vlltlleprr prsesvtvns ffssvdgqle
      301 llaqgalest vssvgalhal rprlscfhql lleppklepl qmtwgmlapp lgntrlhvvk
      361 llasalsand aalthellal dvpntmldlf fhyvfnnflh aqvegcvstm lslgpppdss
      421 petpiqnpvv khllqqcrlv eriltsween drvqcaggpr kgymghltrv agalvqntek
      481 gpnaeqlrql lkelpseqqe qweafvsgpl aetnkknmvd lvnthhlhss sddeddrlke
      541 fnfpeeavlq qafmdfqmqr mtsafidhfg fndeefgeqe esvnapfdkt anitfslnad
      601 denpnanlle icykdriqqf dddeeeedee eaqgsgesdg edgawqgsql argarlgqpp
      661 gvrsggstds edeeeedeee eedeegigca arggatplsy pspgpqppgp swtatfdpvp
      721 tdaptsprvs geeelhtgpp apqgplsvpq glptqslasp pardalqlrs qdptppsapq
      781 eategskvte psapcqalvs igdlqatfhg irsapsssds atrdpstsvp asgahqppqt
      841 tegekspepl glpqsqsaqa ltpppipngs apegpaspgs q
//
LOCUS       NP_001075144             581 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 38 [Homo sapiens].
ACCESSION   NP_001075144 XP_005250958
VERSION     NP_001075144.2
DBSOURCE    REFSEQ: accession NM_001081675.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Xu,Y., Wang,C., Jiang,X., Zhang,Y., Su,H., Jiang,J., Ren,H. and
            Qiu,X.
  TITLE     KLHL38 involvement in non-small cell lung cancer progression via
            activation of the Akt signaling pathway
  JOURNAL   Cell Death Dis 12 (6), 556 (2021)
   PUBMED   34050138
  REMARK    GeneRIF: KLHL38 involvement in non-small cell lung cancer
            progression via activation of the Akt signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Sano,M., Kamitsuji,S., Kamatani,N., Hong,K.W., Han,B.G., Kim,Y.,
            Kim,J.W., Aizawa,Y. and Fukuda,K.
  CONSRTM   Japan Pharmacogenomics Data Science Consortium (JPDSC)
  TITLE     Genome-wide association study of electrocardiographic parameters
            identifies a new association for PR interval and confirms
            previously reported associations
  JOURNAL   Hum Mol Genet 23 (24), 6668-6676 (2014)
   PUBMED   25055868
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Taipale,M., Krykbaeva,I., Koeva,M., Kayatekin,C., Westover,K.D.,
            Karras,G.I. and Lindquist,S.
  TITLE     Quantitative analysis of HSP90-client interactions reveals
            principles of substrate recognition
  JOURNAL   Cell 150 (5), 987-1001 (2012)
   PUBMED   22939624
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135166.8.
            
            On or before Sep 20, 2018 this sequence version replaced
            XP_005250958.1, NP_001075144.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.57505.1,
                                           SRR1803614.257648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000684634.1/ ENSP00000508228.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..581
                     /product="kelch-like protein 38"
                     /note="kelch-like 38"
                     /calculated_mol_wt=65410
     Region          11..139
                     /region_name="BTB_POZ_KLHL38"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 38 (KLHL38); cd18268"
                     /db_xref="CDD:349577"
     Region          131..229
                     /region_name="BACK_KLHL38"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 38 (KLHL38); cd18476"
                     /db_xref="CDD:350551"
     Region          285..332
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     Region          287..528
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          325..369
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          334..383
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     Region          373..417
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          384..431
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     Region          421..508
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          433..479
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     Region          480..521
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     Region          510..560
                     /region_name="Kelch_1"
                     /note="Kelch motif; pfam01344"
                     /db_xref="CDD:396078"
     Region          511..561
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          523..573
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2WGJ6.3)"
     CDS             1..581
                     /gene="KLHL38"
                     /gene_synonym="C8ORFK36"
                     /coded_by="NM_001081675.3:218..1963"
                     /db_xref="CCDS:CCDS43766.1"
                     /db_xref="GeneID:340359"
                     /db_xref="HGNC:HGNC:34435"
ORIGIN      
        1 mdeesldgll fkdhdfssdl lrqlnslrqs riltdvsica gareipchrn vlassspyfr
       61 amfcssfrek seakvqlkgi dpptldqivs yvytgeahia tdnvlpvmea asmlqfpklf
      121 eacssylqsq lapsnclgmi rlseilscet lkkkareval tsfpevaasa dlkelcalel
      181 rdylgddglc geeekvfeal mvwikhdlqa rkrymqelfk qvrlqyihpa ffhhfianda
      241 llqsspacqi iletakrqmf slcgttvpdc klllhvpprn syqdflillg grkdsqqttr
      301 dvllyskqtg qwqslaklpt rlykasaitl hrsiyvlggm avssgrslvs hnvyifslkl
      361 nqwrlgepml varyshrsta hknfifsigg igegqelmgs merydsicnv wesmasmpvg
      421 vlhpavavkd qrlylfgged imqnpvrliq vyhisrnswf kmetrmiknv capavvlger
      481 ivivggytrr ilaydpqsnk fvkcadmkdr rmhhgatvmg nklyvtggrr lttdcnieds
      541 asfdcydpet dtwtsqgqlp hklfdhaclt lqciprtsgl p
//
LOCUS       NP_001340031             369 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001340031
VERSION     NP_001340031.1
DBSOURCE    REFSEQ: accession NM_001353102.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.177825.1,
                                           SRR1803615.221902.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..369
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 1"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=40795
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Region          20..138
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          179..363
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60256.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     CDS             1..369
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353102.2:218..1327"
                     /note="isoform 1 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS11200.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mfcvtppele tkmnitkggl vlfsansnss cmelskkiae rlgvemgkvq vyqepnretr
       61 vqiqesvrgk dvfiiqtvsk dvnttimell imvyacktsc aksiigvipy fpyskqckmr
      121 krgsivskll asmmckaglt hlitmdlhqk eiqgffnipv dnlraspfll qyiqeeipdy
      181 rnavivaksp asakraqsfa erlrlgiavi hgeaqdaesd lvdgrhsppm vrsvaaihps
      241 leipmlipke kppitvvgdv ggriaiivdd iiddvdsfla aaetlkerga ykifvmathg
      301 llssdaprri eesaidevvv tntiphevqk lqcpkiktvd ismilseair rihngesmsy
      361 lfrnigldd
//
LOCUS       NP_001339868             751 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 12 [Homo sapiens].
ACCESSION   NP_001339868
VERSION     NP_001339868.1
DBSOURCE    REFSEQ: accession NM_001352939.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 751)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 751)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 751)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 751)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 751)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 751)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Transcript Variant: This variant (14), as well as variants 13 and
            15, encodes isoform 12.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.144256.1,
                                           SRR1803614.13247.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..751
                     /product="DNA repair-scaffolding protein isoform 12"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=82442
     Region          <11..205
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          357..741
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..751
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352939.1:343..2598"
                     /note="isoform 12 is encoded by transcript variant 14"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mkirhflsyr epssieiley ssdsekeddl envllidses phkyhvqfas darqimerli
       61 dprtksteti lhtpqkptak fprtpensak kkllrgglae rlnglqnrer saislwrhqc
      121 isyqktlsgr ksgvltvkil elheecamqv amceqllgsp atsssqsvap rpgaglkvlf
      181 tketagylrg rpqdtvrifp pwqkliipsg scpvilntyf cekvvakeds ektcevycpd
      241 iplprrsisl aqmfvikglt nnspeiqvvc sgvattgtaw thghkeakqr iptstplrds
      301 lldvvesqga aswpgagvrv vvqrvyslps rdstrgqqga ssghtdpagt racllvqdac
      361 gmfgevhlef tmskarqleg kscslvgmkv lqkvtrgrta gifslidtlw ppaiplktpg
      421 rdqpceeikt hlpppalcyi ltahpnlgqi diidedpiyk lyqppvtrcl rdilqmndlg
      481 trcsfyatvi yqkpqlksll lleqreiwll vtdvtlqtke erdprlpktl lvyvaplcvl
      541 gsevlealag aaphslffkd alrdqgrivc aertvlllqk pllsvvsgas scelpgpvml
      601 dsldsatpvn sicsvqgtvv gvdestafsw pvcdmcgngr leqrpedrga fscgdcsrvv
      661 tspvlkrhlq vfldcrsrpq crvkvkllqr sissllrfaa gedgsyevks vlgkevglln
      721 cfvqsvtahp tscigleeie llsaggasae h
//
LOCUS       NP_001341007             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341007
VERSION     NP_001341007.1
DBSOURCE    REFSEQ: accession NM_001354078.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.163395.1,
                                           SRR1803615.87118.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354078.1:102..866"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001317598             536 aa            linear   PRI 20-NOV-2025
DEFINITION  serine--tRNA ligase, cytoplasmic isoform b [Homo sapiens].
ACCESSION   NP_001317598 XP_006710876
VERSION     NP_001317598.1
DBSOURCE    REFSEQ: accession NM_001330669.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Throll,P., G Dolce,L., Rico-Lastres,P., Arnold,K., Tengo,L.,
            Basu,S., Kaiser,S., Schneider,R. and Kowalinski,E.
  TITLE     Structural basis of tRNA recognition by the m3C RNA
            methyltransferase METTL6 in complex with SerRS seryl-tRNA
            synthetase
  JOURNAL   Nat Struct Mol Biol 31 (10), 1614-1624 (2024)
   PUBMED   38918637
  REMARK    Erratum:[Nat Struct Mol Biol. 2025 Feb;32(2):405. doi:
            10.1038/s41594-025-01508-6. PMID: 39905155]
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Liu,Z., Wang,J., Shi,Y., Yee,B.A., Terrey,M., Zhang,Q., Lee,J.C.,
            Lin,K.I., Wang,A.H., Ackerman,S.L., Yeo,G.W., Cui,H. and Yang,X.L.
  TITLE     Seryl-tRNA synthetase promotes translational readthrough by mRNA
            binding and involvement of the selenocysteine incorporation
            machinery
  JOURNAL   Nucleic Acids Res 51 (19), 10768-10781 (2023)
   PUBMED   37739431
  REMARK    GeneRIF: Seryl-tRNA synthetase promotes translational readthrough
            by mRNA binding and involvement of the selenocysteine incorporation
            machinery.
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Verdura,E., Senger,B., Raspall-Chaure,M., Schluter,A., Launay,N.,
            Ruiz,M., Casasnovas,C., Rodriguez-Palmero,A., Macaya,A.,
            Becker,H.D. and Pujol,A.
  TITLE     Loss of seryl-tRNA synthetase (SARS1) causes complex spastic
            paraplegia and cellular senescence
  JOURNAL   J Med Genet 59 (12), 1227-1233 (2022)
   PUBMED   36041817
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Bogershausen,N., Krawczyk,H.E., Jamra,R.A., Lin,S.J., Yigit,G.,
            Huning,I., Polo,A.M., Vona,B., Huang,K., Schmidt,J., Altmuller,J.,
            Luppe,J., Platzer,K., Dorgeloh,B.B., Busche,A., Biskup,S.,
            Mendes,M.I., Smith,D.E.C., Salomons,G.S., Zibat,A., Bultmann,E.,
            Nurnberg,P., Spielmann,M., Lemke,J.R., Li,Y., Zenker,M.,
            Varshney,G.K., Hillen,H.S., Kratz,C.P. and Wollnik,B.
  TITLE     WARS1 and SARS1: Two tRNA synthetases implicated in autosomal
            recessive microcephaly
  JOURNAL   Hum Mutat 43 (10), 1454-1471 (2022)
   PUBMED   35790048
  REMARK    GeneRIF: WARS1 and SARS1: Two tRNA synthetases implicated in
            autosomal recessive microcephaly.
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Ravel,J.M., Dreumont,N., Mosca,P., Smith,D.E.C., Mendes,M.I.,
            Wiedemann,A., Coelho,D., Schmitt,E., Riviere,J.B., Tran
            Mau-Them,F., Thevenon,J., Kuentz,P., Polivka,M., Fuchs,S.A.,
            Kok,G., Thauvin-Robinet,C., Gueant,J.L., Salomons,G.S., Faivre,L.
            and Feillet,F.
  TITLE     A bi-allelic loss-of-function SARS1 variant in children with
            neurodevelopmental delay, deafness, cardiomyopathy, and
            decompensation during fever
  JOURNAL   Hum Mutat 42 (12), 1576-1583 (2021)
   PUBMED   34570399
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Shimada,N., Suzuki,T. and Watanabe,K.
  TITLE     Dual mode recognition of two isoacceptor tRNAs by mammalian
            mitochondrial seryl-tRNA synthetase
  JOURNAL   J Biol Chem 276 (50), 46770-46778 (2001)
   PUBMED   11577083
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Shah,Z.H., Toompuu,M., Hakkinen,T., Rovio,A.T., van Ravenswaay,C.,
            De Leenheer,E.M., Smith,R.J., Cremers,F.P., Cremers,C.W. and
            Jacobs,H.T.
  TITLE     Novel coding-region polymorphisms in mitochondrial seryl-tRNA
            synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in
            DFNA4 autosomal dominant deafness families
  JOURNAL   Hum Mutat 17 (5), 433-434 (2001)
   PUBMED   11317363
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Heckl,M., Busch,K. and Gross,H.J.
  TITLE     Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA
            synthetase: contribution of tRNA domains to serylation and tertiary
            structure
  JOURNAL   FEBS Lett 427 (3), 315-319 (1998)
   PUBMED   9637248
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Vincent,C., Tarbouriech,N. and Hartlein,M.
  TITLE     Genomic organization, cDNA sequence, bacterial expression, and
            purification of human seryl-tRNA synthase
  JOURNAL   Eur J Biochem 250 (1), 77-84 (1997)
   PUBMED   9431993
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Hartlein,M. and Cusack,S.
  TITLE     Structure, function and evolution of seryl-tRNA synthetases:
            implications for the evolution of aminoacyl-tRNA synthetases and
            the genetic code
  JOURNAL   J Mol Evol 40 (5), 519-530 (1995)
   PUBMED   7540217
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356389.20.
            
            On Sep 1, 2016 this sequence version replaced XP_006710876.1.
            
            Summary: This gene belongs to the class II amino-acyl tRNA family.
            The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser)
            and is related to bacterial and yeast counterparts. Multiple
            alternatively spliced transcript variants have been described but
            the biological validity of all variants is unknown. [provided by
            RefSeq, Jul 2010].
            
            Transcript Variant: This variant (3) encodes the longer isoform
            (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.244787.1,
                                           SRR1803612.255120.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..536
                     /product="serine--tRNA ligase, cytoplasmic isoform b"
                     /EC_number="6.1.1.11"
                     /note="serine tRNA ligase 1, cytoplasmic; seryl-tRNA
                     synthetase, cytoplasmic; seryl-tRNA(Ser/Sec) synthetase;
                     serine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=61182
     Region          3..508
                     /region_name="PLN02678"
                     /note="seryl-tRNA synthetase"
                     /db_xref="CDD:215364"
     CDS             1..536
                     /gene="SARS1"
                     /gene_synonym="NEDMAS; SARS; SERRS; SERS"
                     /coded_by="NM_001330669.1:101..1711"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81356.1"
                     /db_xref="GeneID:6301"
                     /db_xref="HGNC:HGNC:10537"
                     /db_xref="MIM:607529"
ORIGIN      
        1 mvldldlfrv dkggdpalir etqekrfkdp glvdqlvkad sewrrcrfra dnlnklknlc
       61 sktigekmkk kepvgddesv penvlsfddl tadalanlkv sqikkvrlli deailkcdae
      121 rikleaerfe nlreignllh psvpisnded vdnkveriwg dctvrkkysh vdlvvmvdgf
      181 egekgavvag srgyflkgvl vfleqaliqy alrtlgsrgy ipiytpffmr kevmqevaql
      241 sqfdeelykv igkgseksdd nsydekylia tseqpiaalh rdewlrpedl pikyaglstc
      301 frqevgshgr dtrgifrvhq fekieqfvys sphdnkswem feemittaee fyqslgipyh
      361 ivnivsgsln haaskkldle awfpgsgafr elvscsnctd yqarrlriry gqtkkmmdkr
      421 knnlhlstqn kleaslfspk kvefvhmlna tmcattrtic ailenyqtek gitvpeklke
      481 fmppglqeli pfvkpapieq epskkqkkqh egskkkaaar dvtlenrlqn mevtda
//
LOCUS       NP_061335                617 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 9 [Homo sapiens].
ACCESSION   NP_061335
VERSION     NP_061335.1
DBSOURCE    REFSEQ: accession NM_018847.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Mena,E.L., Kjolby,R.A.S., Saxton,R.A., Werner,A., Lew,B.G.,
            Boyle,J.M., Harland,R. and Rape,M.
  TITLE     Dimerization quality control ensures neuronal development and
            survival
  JOURNAL   Science 362 (6411) (2018)
   PUBMED   30190310
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Cirak,S., von Deimling,F., Sachdev,S., Errington,W.J., Herrmann,R.,
            Bonnemann,C., Brockmann,K., Hinderlich,S., Lindner,T.H.,
            Steinbrecher,A., Hoffmann,K., Prive,G.G., Hannink,M., Nurnberg,P.
            and Voit,T.
  TITLE     Kelch-like homologue 9 mutation is associated with an early onset
            autosomal dominant distal myopathy
  JOURNAL   Brain 133 (Pt 7), 2123-2135 (2010)
   PUBMED   20554658
  REMARK    GeneRIF: A unique form of early onset autosomal dominant distal
            myopathy is associated with a kelch-like homologue 9 mutation and
            interferes with normal skeletal muscle through a novel pathogenetic
            mechanism.
            Erratum:[Brain. 2020 Jun 1;143(6):e52. doi: 10.1093/brain/awaa065.
            PMID: 32163547]
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Maerki,S., Olma,M.H., Staubli,T., Steigemann,P., Gerlich,D.W.,
            Quadroni,M., Sumara,I. and Peter,M.
  TITLE     The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
            microtubules in anaphase and is required for cytokinesis
  JOURNAL   J Cell Biol 187 (6), 791-800 (2009)
   PUBMED   19995937
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Sumara,I., Quadroni,M., Frei,C., Olma,M.H., Sumara,G., Ricci,R. and
            Peter,M.
  TITLE     A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
            regulating mitotic progression and completion of cytokinesis in
            human cells
  JOURNAL   Dev Cell 12 (6), 887-900 (2007)
   PUBMED   17543862
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Kim,Y.C., Jung,Y.C., Xuan,Z., Dong,H., Zhang,M.Q. and Wang,S.M.
  TITLE     Pan-genome isolation of low abundance transcripts using SAGE tag
  JOURNAL   FEBS Lett 580 (28-29), 6721-6729 (2006)
   PUBMED   17113583
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB237245.1, AB037775.1,
            BC052776.1 and AL162420.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that belongs to the kelch
            repeat-containing family, and contains an N-terminal BTB/POZ
            domain, a BACK domain and six C-terminal kelch repeats. The encoded
            protein is a component of a complex with cullin 3-based E3 ligase,
            which plays a role in mitosis. This protein complex is a cell cycle
            regulator, and functions in the organization and integrity of the
            spindle midzone in anaphase and the completion of cytokinesis. The
            complex is required for the removal of the chromosomal passenger
            protein aurora B from mitotic chromosomes. [provided by RefSeq, Jul
            2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1803614.109379.1, SRR1803616.49521.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359039.5/ ENSP00000351933.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.3"
     Protein         1..617
                     /product="kelch-like protein 9"
                     /calculated_mol_wt=69298
     Region          27..154
                     /region_name="BTB_POZ_KLHL9_13"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     proteins KLHL9 and KLHL13; cd18239"
                     /db_xref="CDD:349548"
     Region          50..593
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          300..347
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          337..385
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          348..399
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          389..433
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          400..446
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          436..481
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..493
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          483..532
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          495..545
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          535..582
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          546..595
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     Region          595..617
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2J3.2)"
     CDS             1..617
                     /gene="KLHL9"
                     /coded_by="NM_018847.4:546..2399"
                     /db_xref="CCDS:CCDS6503.1"
                     /db_xref="GeneID:55958"
                     /db_xref="HGNC:HGNC:18732"
                     /db_xref="MIM:611201"
ORIGIN      
        1 mkvslgngem gvsahlqpck agttrfftsn thssvvlqgf dqlriegllc dvtlvpgdgd
       61 eifpvhramm asasdyfkam ftggmkeqdl mciklhgvnk vglkkiidfi ytaklslnmd
      121 nlqdtleaas flqilpvldf ckvflisgvs ldncvevgri antynlievd kyvnnfilkn
      181 fpallstgef lklpferlaf vlssnslkhc telelfkaac rwlrledprm dyaaklmkni
      241 rfplmtpqdl inyvqtvdfm rtdntcvnll leasnyqmmp ymqpvmqsdr tairsdsthl
      301 vtlggvlrqq lvvskelrmy deraqewrsl apmdapryqh giavignfly vvggqsnydt
      361 kgktavdtvf rfdprynkwm qvaslnekrt ffhlsalkgh lyavggrsaa gelatvecyn
      421 prmnewsyva kmsephygha gtvygglmyi sggithdtfq nelmcfdpdt dkwmqkapmt
      481 tvrglhcmct vgdklyvigg nhfrgtsdyd dvlsceyysp tldqwtpiaa mlrgqsdvgv
      541 avfenkiyvv ggyswnnrcm veivqkydpe kdewhkvfdl peslggirac tltvfppeen
      601 pgspsrespl sapsdhs
//
LOCUS       NP_001035960            1091 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 12 member 6 isoform c [Homo sapiens].
ACCESSION   NP_001035960
VERSION     NP_001035960.1
DBSOURCE    REFSEQ: accession NM_001042495.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Loseth,S., Hoyer,H., Le,K.M., Delpire,E., Kinge,E., Lande,A.,
            Hilmarsen,H.T., Fagerheim,T., Nilssen,O. and Braathen,G.J.
  TITLE     Late-onset sensory-motor axonal neuropathy, a novel SLC12A6-related
            phenotype
  JOURNAL   Brain 146 (3), 912-922 (2023)
   PUBMED   36542484
  REMARK    GeneRIF: Late-onset sensory-motor axonal neuropathy, a novel
            SLC12A6-related phenotype.
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Ando,M., Higuchi,Y., Yuan,J., Yoshimura,A., Taniguchi,T., Takei,J.,
            Takeuchi,M., Hiramatsu,Y., Shimizu,F., Kubota,M., Takeshima,A.,
            Ueda,T., Koh,K., Nagaoka,U., Tokashiki,T., Sawai,S., Sakiyama,Y.,
            Hashiguchi,A., Sato,R., Kanda,T., Okamoto,Y. and Takashima,H.
  TITLE     Novel heterozygous variants of SLC12A6 in Japanese families with
            Charcot-Marie-Tooth disease
  JOURNAL   Ann Clin Transl Neurol 9 (7), 902-911 (2022)
   PUBMED   35733399
  REMARK    GeneRIF: Novel heterozygous variants of SLC12A6 in Japanese
            families with Charcot-Marie-Tooth disease.
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Bogdanova-Mihaylova,P., McNamara,P., Burton-Jones,S. and
            Murphy,S.M.
  TITLE     Expanding the phenotype of SLC12A6-associated sensorimotor
            neuropathy
  JOURNAL   BMJ Case Rep 14 (10), e244641 (2021)
   PUBMED   34706912
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Chi,G., Ebenhoch,R., Man,H., Tang,H., Tremblay,L.E., Reggiano,G.,
            Qiu,X., Bohstedt,T., Liko,I., Almeida,F.G., Garneau,A.P., Wang,D.,
            McKinley,G., Moreau,C.P., Bountra,K.D., Abrusci,P.,
            Mukhopadhyay,S.M.M., Fernandez-Cid,A., Slimani,S., Lavoie,J.L.,
            Burgess-Brown,N.A., Tehan,B., DiMaio,F., Jazayeri,A., Isenring,P.,
            Robinson,C.V. and Durr,K.L.
  TITLE     Phospho-regulation, nucleotide binding and ion access control in
            potassium-chloride cotransporters
  JOURNAL   EMBO J 40 (14), e107294 (2021)
   PUBMED   34031912
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
            Chernova,M.N., Brugnara,C. and Alper,S.L.
  TITLE     A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
            and C-terminal cytoplasmic domains are required for K-Cl
            cotransport activity
  JOURNAL   J Biol Chem 276 (45), 41870-41878 (2001)
   PUBMED   11551954
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Race,J.E., Makhlouf,F.N., Logue,P.J., Wilson,F.H., Dunham,P.B. and
            Holtzman,E.J.
  TITLE     Molecular cloning and functional characterization of KCC3, a new
            K-Cl cotransporter
  JOURNAL   Am J Physiol 277 (6), C1210-C1219 (1999)
   PUBMED   10600773
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
            and Gamba,G.
  TITLE     Cloning and characterization of KCC3 and KCC4, new members of the
            cation-chloride cotransporter gene family
  JOURNAL   J Biol Chem 274 (23), 16355-16362 (1999)
   PUBMED   10347194
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Hiki,K., D'Andrea,R.J., Furze,J., Crawford,J., Woollatt,E.,
            Sutherland,G.R., Vadas,M.A. and Gamble,J.R.
  TITLE     Cloning, characterization, and chromosomal location of a novel
            human K+-Cl- cotransporter
  JOURNAL   J Biol Chem 274 (15), 10661-10667 (1999)
   PUBMED   10187864
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Gauvreau,C., Brisson,J.D. and Dupre,N.
  TITLE     Hereditary Motor and Sensory Neuropathy with Agenesis of the Corpus
            Callosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070107.1 and AC079203.9.
            
            Summary: This gene is a member of the K-Cl cotransporter (KCC)
            family. K-Cl cotransporters are integral membrane proteins that
            lower intracellular chloride concentrations below the
            electrochemical equilibrium potential. The proteins encoded by this
            gene are activated by cell swelling induced by hypotonic
            conditions. Alternate splicing results in multiple transcript
            variants encoding different isoforms. Mutations in this gene are
            associated with agenesis of the corpus callosum with peripheral
            neuropathy. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) has an additional exon in its
            5' UTR and uses an alternate in-frame splice site in the first
            protein coding exon, compared to variant 1. The encoded protein
            (isoform c) uses a downstream start codon, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070107.1, AF531260.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..1091
                     /product="solute carrier family 12 member 6 isoform c"
                     /note="potassium chloride cotransporter 3; potassium
                     chloride cotransporter KCC3a-S3; potassium-chloride
                     transporter-3a; potassium-chloride transporter-3b; K-Cl
                     cotransporter 3; electroneutral potassium-chloride
                     cotransporter 3; solute carrier family 12
                     (potassium/chloride transporters), member 6; solute
                     carrier family 12 (potassium/chloride transporter), member
                     6"
                     /calculated_mol_wt=120994
     Region          50..1091
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     CDS             1..1091
                     /gene="SLC12A6"
                     /gene_synonym="ACCPN; CMT2II; KCC3; KCC3A; KCC3B"
                     /coded_by="NM_001042495.2:196..3471"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS42012.1"
                     /db_xref="GeneID:9990"
                     /db_xref="HGNC:HGNC:10914"
                     /db_xref="MIM:604878"
ORIGIN      
        1 msemsgatts latvaldpps drtshpqdvi edlsqnsitg ehsqllddgh kkarnaylnn
       61 snyeegdeyf dknlalfeee mdtrpkvssl lnrmanytnl tqgakeheea enitegkkkp
      121 tktpqmgtfm gvylpclqni fgvilflrlt wvvgtagvlq afaivliccc ctmltaisms
      181 aiatngvvpa ggsyfmisra lgpefggavg lcfylgttfa aamyilgaie iflvyivpra
      241 aifhsddalk esaamlnnmr vygtaflvlm vlvvfigvry vnkfaslfla cvivsilaiy
      301 agaikssfap phfpvcmlgn rtlssrhidv csktkeinnm tvpsklwgff cnssqffnat
      361 cdeyfvhnnv tsiqgipgla sgiitenlws nylpkgeiie kpsakssdvl gslnheyvlv
      421 dittsftllv giffpsvtgi magsnrsgdl kdaqksipig tilailttsf vylsnvvlfg
      481 aciegvvlrd kfgdavkgnl vvgtlswpsp wvivigsffs tcgaglqslt gaprllqaia
      541 kdniipflrv fghskangep twallltaai aelgiliasl dlvapilsmf flmcylfvnl
      601 acalqtllrt pnwrprfryy hwalsfmgms iclalmfiss wyyaivamvi agmiykyiey
      661 qgaekewgdg irglslsaar fallrleegp phtknwrpql lvllkldedl hvkhprlltf
      721 asqlkagkgl tivgsvivgn flenygeala aeqtikhlme aekvkgfcql vvaaklregi
      781 shliqscglg gmkhntvvmg wpngwrqsed arawktfigt vrvttaahla llvaknisff
      841 psnveqfseg nidvwwivhd ggmlmllpfl lkqhkvwrkc siriftvaql ednsiqmkkd
      901 latflyhlri eaevevvemh dsdisaytye rtlmmeqrsq mlrhmrlskt erdreaqlvk
      961 drnsmlrlts igsdedeete tyqekvhmtw tkdkymasrg qkaksmegfq dllnmrpdqs
     1021 nvrrmhtavk lnevivnksh eaklvllnmp gpprnpegde nymeflevlt eglervllvr
     1081 gggsevitiy s
//
LOCUS       NP_001903                333 aa            linear   PRI 20-NOV-2025
DEFINITION  procathepsin L isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001903
VERSION     NP_001903.1
DBSOURCE    REFSEQ: accession NM_001912.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Bestle,D., Bittel,L., Werner,A.D., Kamper,L., Dolnik,O.,
            Krahling,V., Steinmetzer,T. and Bottcher-Friebertshauser,E.
  TITLE     Novel proteolytic activation of Ebolavirus glycoprotein GP by
            TMPRSS2 and cathepsin L at an uncharted position can compensate for
            furin cleavage
  JOURNAL   Virus Res 347, 199430 (2024)
   PUBMED   38964470
  REMARK    GeneRIF: Novel proteolytic activation of Ebolavirus glycoprotein GP
            by TMPRSS2 and cathepsin L at an uncharted position can compensate
            for furin cleavage.
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Wu,Y., Jiang,D., Liu,Q., Yan,S., Liu,X., Wu,T., Sun,W. and Li,G.
  TITLE     Cathepsin L induces cellular senescence by upregulating CUX1 and
            p16INK4a
  JOURNAL   Aging (Albany NY) 16 (13), 10749-10764 (2024)
   PUBMED   38944813
  REMARK    GeneRIF: Cathepsin L induces cellular senescence by upregulating
            CUX1 and p16[INK4a].
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Xu,J., Xu,W., Choi,J., Brhane,Y., Christiani,D.C., Kothari,J.,
            McKay,J., Field,J.K., Davies,M.P.A., Liu,G., Amos,C.I., Hung,R.J.
            and Briollais,L.
  TITLE     Large-scale whole exome sequencing studies identify two genes,CTSL
            and APOE, associated with lung cancer
  JOURNAL   PLoS Genet 19 (9), e1010902 (2023)
   PUBMED   37738239
  REMARK    GeneRIF: Large-scale whole exome sequencing studies identify two
            genes,CTSL and APOE, associated with lung cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Liu,P., Ju,M., Zheng,X., Jiang,Y., Yu,X., Pan,B., Luo,R., Jia,W.
            and Zheng,M.
  TITLE     Methyltransferase-like 3 promotes cervical cancer metastasis by
            enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner
  JOURNAL   Cancer Sci 114 (3), 837-854 (2023)
   PUBMED   36382580
  REMARK    GeneRIF: Methyltransferase-like 3 promotes cervical cancer
            metastasis by enhancing cathepsin L mRNA stability in an
            N6-methyladenosine-dependent manner.
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Goretzki,L., Schmitt,M., Mann,K., Calvete,J., Chucholowski,N.,
            Kramer,M., Gunzler,W.A., Janicke,F. and Graeff,H.
  TITLE     Effective activation of the proenzyme form of the urokinase-type
            plasminogen activator (pro-uPA) by the cysteine protease cathepsin
            L
  JOURNAL   FEBS Lett 297 (1-2), 112-118 (1992)
   PUBMED   1551416
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Cataldo,A.M., Paskevich,P.A., Kominami,E. and Nixon,R.A.
  TITLE     Lysosomal hydrolases of different classes are abnormally
            distributed in brains of patients with Alzheimer disease
  JOURNAL   Proc Natl Acad Sci U S A 88 (24), 10998-11002 (1991)
   PUBMED   1837142
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Mar 15;89(6):2509]
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Dunn,A.D., Crutchfield,H.E. and Dunn,J.T.
  TITLE     Thyroglobulin processing by thyroidal proteases. Major sites of
            cleavage by cathepsins B, D, and L
  JOURNAL   J Biol Chem 266 (30), 20198-20204 (1991)
   PUBMED   1939080
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Stearns,N.A., Dong,J.M., Pan,J.X., Brenner,D.A. and Sahagian,G.G.
  TITLE     Comparison of cathepsin L synthesized by normal and transformed
            cells at the gene, message, protein, and oligosaccharide levels
  JOURNAL   Arch Biochem Biophys 283 (2), 447-457 (1990)
   PUBMED   2275556
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Smith,C.G., Smith,M.T., Besch,N.F., Smith,R.G. and Asch,R.H.
  TITLE     Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive
            function
  JOURNAL   Adv Biosci 22-23, 449-467 (1978)
   PUBMED   116880
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN993009.1, AL832167.1,
            BM680778.1 and AL160279.21.
            
            Summary: The protein encoded by this gene is a lysosomal cysteine
            proteinase that plays a major role in intracellular protein
            catabolism. Its substrates include collagen and elastin, as well as
            alpha-1 protease inhibitor, a major controlling element of
            neutrophil elastase activity. The encoded protein has been
            implicated in several pathologic processes, including myofibril
            necrosis in myopathies and in myocardial ischemia, and in the renal
            tubular response to proteinuria. This protein, which is a member of
            the peptidase C1 family, is a dimer composed of disulfide-linked
            heavy and light chains, both produced from a single protein
            precursor. Additionally, this protein cleaves the S1 subunit of the
            SARS-CoV-2 spike protein, which is necessary for entry of the virus
            into the cell. [provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-4 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X12451.1, SRR3476690.922332.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in SARS-CoV-2 infection
            MANE Ensembl match     :: ENST00000343150.10/ ENSP00000345344.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.33"
     Protein         1..333
                     /product="procathepsin L isoform 1 preproprotein"
                     /EC_number="3.4.22.15"
                     /note="major excreted protein; cathepsin L1; procathepsin
                     L"
                     /calculated_mol_wt=35876
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1706
     proprotein      18..333
                     /product="cathepsin L1 proprotein"
                     /calculated_mol_wt=35876
     Region          29..87
                     /region_name="Inhibitor_I29"
                     /note="Cathepsin propeptide inhibitor domain (I29);
                     smart00848"
                     /db_xref="CDD:214853"
     Site            106..107
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            107..108
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            112..113
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Site            113..114
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:9468501; propagated from
                     UniProtKB/Swiss-Prot (P07711.2)"
     Region          114..332
                     /region_name="Peptidase_C1"
                     /note="Papain family cysteine protease; pfam00112"
                     /db_xref="CDD:425470"
     mat_peptide     114..288
                     /product="cathepsin L1 heavy chain"
                     /calculated_mol_wt=19080
     Site            order(132,138,276,300)
                     /site_type="active"
                     /db_xref="CDD:239068"
     Site            order(182..183,248,274,277,327)
                     /site_type="active"
                     /note="S2 subsite [active]"
                     /db_xref="CDD:239068"
     Site            221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P07711.2)"
     mat_peptide     292..333
                     /product="cathepsin L1 light chain"
                     /calculated_mol_wt=4776
     CDS             1..333
                     /gene="CTSL"
                     /gene_synonym="CATL; CTSL1; MEP"
                     /coded_by="NM_001912.5:291..1292"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6675.1"
                     /db_xref="GeneID:1514"
                     /db_xref="HGNC:HGNC:2537"
                     /db_xref="MIM:116880"
ORIGIN      
        1 mnptlilaaf clgiasatlt fdhsleaqwt kwkamhnrly gmneegwrra vweknmkmie
       61 lhnqeyregk hsftmamnaf gdmtseefrq vmngfqnrkp rkgkvfqepl fyeaprsvdw
      121 rekgyvtpvk nqgqcgscwa fsatgalegq mfrktgrlis lseqnlvdcs gpqgnegcng
      181 glmdyafqyv qdnggldsee sypyeatees ckynpkysva ndtgfvdipk qekalmkava
      241 tvgpisvaid aghesflfyk egiyfepdcs sedmdhgvlv vgygfestes dnnkywlvkn
      301 swgeewgmgg yvkmakdrrn hcgiasaasy ptv
//
LOCUS       NP_001265048             578 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001265048
VERSION     NP_001265048.1
DBSOURCE    REFSEQ: accession NM_001278119.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Lee,P.L., Gelbart,T., West,C., Adams,M., Blackstone,R. and
            Beutler,E.
  TITLE     Three genes encoding zinc finger proteins on human chromosome
            6p21.3: members of a new subclass of the Kruppel gene family
            containing the conserved SCAN box domain
  JOURNAL   Genomics 43 (2), 191-201 (1997)
   PUBMED   9244436
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Beutler,E., Gelbart,T., West,C., Kuhl,W. and Lee,P.
  TITLE     A strategy for cloning the hereditary hemochromatosis gene
  JOURNAL   Blood Cells Mol Dis 21 (3), 207-216 (1995)
   PUBMED   8673473
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL358933.15, AB208793.1, BC096282.3 and BM664529.1.
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longer isoform (1). Both variants 1 and 2 encode the
            same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC096282.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..578
                     /product="zinc finger protein with KRAB and SCAN domains 8
                     isoform 1"
                     /note="zinc finger protein with KRAB and SCAN domains 8;
                     zinc finger protein 192"
                     /calculated_mol_wt=65685
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15776.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15776.2)"
     Region          47..159
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          158..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15776.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17029; propagated from
                     UniProtKB/Swiss-Prot (Q15776.2)"
     Region          221..>262
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <315..564
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(441,443,445,447..448,451..452,455,469,471,475..476,
                     479..480,483,497,499,501,503..504,507..508,511)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          464..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(464,467,480,484)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(520,523,536,540)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..578
                     /gene="ZKSCAN8"
                     /gene_synonym="LD5-1; ZNF192; ZSCAN40"
                     /coded_by="NM_001278119.2:334..2070"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4645.1"
                     /db_xref="GeneID:7745"
                     /db_xref="HGNC:HGNC:12983"
                     /db_xref="MIM:602240"
ORIGIN      
        1 maeesrkpsa psppdqtpee dlvivkveed hgwdqesslh esnplgqevf rlrfrqlryq
       61 etlgpreali qlralchqwl rpdlntkeqi lellvleqfl tilpeelqtl vkehqlenge
      121 evvtlledle rqidilgrpv sarvhghrvl weevvhsasa peppntqlqs eatqhkspvp
      181 qesqeramst sqsptrsqkg ssgdqemtat lltagfqtle kiedmavsli reewlldpsq
      241 kdlcrdnrpe nfrnmfslgg etrsenrela skqvistgiq phgetaakcn gdvirglehe
      301 eardllgrle rqrgnptqer rhkcdecgks faqssglvrh wrihtgekpy qcnvcgkafs
      361 yrsallshqd ihnkvkryhc kecgkafsqn tglilhqrih tgekpyqcnq cgkafsqsag
      421 lilhqrihsg erpyecnecg kafshsshli ghqrihtgek pyecdecgkt frrsshligh
      481 qrshtgekpy kcnecgrafs qksgliehqr ihtgerpykc kecgkafngn tgliqhlrih
      541 tgekpyqcne cgkafiqrss lirhqrihsg eksesisv
//
LOCUS       NP_001308509             519 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 20 [Homo sapiens].
ACCESSION   NP_001308509
VERSION     NP_001308509.1
DBSOURCE    REFSEQ: accession NM_001321580.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 519)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (21) encodes isoform (20, also
            known as delta 4).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.244715.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..519
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 20"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=58341
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          366..493
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..519
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321580.2:671..2230"
                     /note="isoform 20 is encoded by transcript variant 21"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkin nkanvvtspk eniptpales tessnttied
      361 edvkarkqei ikvteqliea inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe
      421 nalsksnkpi htiilnphvh lvgddaacia yirltqymdg sgmpktmqse etrvwhrrdg
      481 kwqnvhfhrs gsptvpikpp cipngkenfs ggtslwqni
//
LOCUS       NP_001353355            1468 aa            linear   PRI 20-NOV-2025
DEFINITION  neurexin 3 isoform 7 [Homo sapiens].
ACCESSION   NP_001353355 XP_016877292
VERSION     NP_001353355.1
DBSOURCE    REFSEQ: accession NM_001366426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1468)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1468)
  AUTHORS   Gulec,G., Cosan,D.T., Sahin,F.M., Calis,I.U., Sonkurt,M.D.,
            Kosger,F. and Essizoglu,A.
  TITLE     Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms
  JOURNAL   Turk Psikiyatri Derg 32 (3), 160-166 (2021)
   PUBMED   34647286
  REMARK    GeneRIF: Association of Nicotine Use Disorder with Neurexin 3 Gene
            Polymorphisms.', trans 'Nikotin Kullanim Bozuklugunun Neurexin 3
            Gen Polimorfizmi ile Iliskisi.
REFERENCE   3  (residues 1 to 1468)
  AUTHORS   Hishimoto,A., Liu,Q.R., Drgon,T., Pletnikova,O., Walther,D.,
            Zhu,X.G., Troncoso,J.C. and Uhl,G.R.
  TITLE     Neurexin 3 polymorphisms are associated with alcohol dependence and
            altered expression of specific isoforms
  JOURNAL   Hum Mol Genet 16 (23), 2880-2891 (2007)
   PUBMED   17804423
  REMARK    GeneRIF: details of NRXN3's gene structure and variants, and
            association of NRXN3 SNPs with alcohol dependence
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   4  (residues 1 to 1468)
  AUTHORS   Occhi,G., Rampazzo,A., Beffagna,G. and Antonio Danieli,G.
  TITLE     Identification and characterization of heart-specific splicing of
            human neurexin 3 mRNA (NRXN3)
  JOURNAL   Biochem Biophys Res Commun 298 (1), 151-155 (2002)
   PUBMED   12379233
  REMARK    GeneRIF: Identification and characterization of heart-specific
            splicing of neurexin 3 mRNA
REFERENCE   5  (residues 1 to 1468)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   6  (residues 1 to 1468)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   7  (residues 1 to 1468)
  AUTHORS   Missler,M., Hammer,R.E. and Sudhof,T.C.
  TITLE     Neurexophilin binding to alpha-neurexins. A single LNS domain
            functions as an independently folding ligand-binding unit
  JOURNAL   J Biol Chem 273 (52), 34716-34723 (1998)
   PUBMED   9856994
  REMARK    GeneRIF: N-terminal sequencing of rat neurexin III alpha provides
            evidence for signal peptide
REFERENCE   8  (residues 1 to 1468)
  AUTHORS   Missler,M. and Sudhof,T.C.
  TITLE     Neurexins: three genes and 1001 products
  JOURNAL   Trends Genet 14 (1), 20-26 (1998)
   PUBMED   9448462
  REMARK    Review article
REFERENCE   9  (residues 1 to 1468)
  AUTHORS   Ichtchenko,K., Nguyen,T. and Sudhof,T.C.
  TITLE     Structures, alternative splicing, and neurexin binding of multiple
            neuroligins
  JOURNAL   J Biol Chem 271 (5), 2676-2682 (1996)
   PUBMED   8576240
REFERENCE   10 (residues 1 to 1468)
  AUTHORS   Ushkaryov,Y.A., Hata,Y., Ichtchenko,K., Moomaw,C., Afendis,S.,
            Slaughter,C.A. and Sudhof,T.C.
  TITLE     Conserved domain structure of beta-neurexins. Unusual cleaved
            signal sequences in receptor-like neuronal cell-surface proteins
  JOURNAL   J Biol Chem 269 (16), 11987-11992 (1994)
   PUBMED   8163501
  REMARK    GeneRIF: N-terminal sequencing of cow neurexin III beta provides
            evidence for signal peptide
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007955.4, AF099810.1,
            AC008045.5, AC009396.5, AC026888.6, AC012099.4, AC008056.6 and
            AF123462.1.
            
            On Oct 5, 2018 this sequence version replaced XP_016877292.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function in the nervous system as receptors and cell adhesion
            molecules. Extensive alternative splicing and the use of
            alternative promoters results in multiple transcript variants and
            protein isoforms for this gene, but the full-length nature of many
            of these variants has not been determined. Transcripts that
            initiate from an upstream promoter encode alpha isoforms, which
            contain epidermal growth factor-like (EGF-like) sequences and
            laminin G domains. Transcripts initiating from the downstream
            promoter encode beta isoforms, which lack EGF-like sequences.
            Genetic variation at this locus has been associated with a range of
            behavioral phenotypes, including alcohol dependence and autism
            spectrum disorder. [provided by RefSeq, Dec 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3-q31.1"
     Protein         1..1468
                     /product="neurexin 3 isoform 7"
                     /note="neurexin III; neurexin-3-alpha"
                     /calculated_mol_wt=162196
     Region          35..181
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          202..232
                     /region_name="EGF"
                     /note="EGF-like domain; pfam00008"
                     /db_xref="CDD:394967"
     Region          286..417
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          474..623
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          651..684
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          712..846
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          903..1031
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1095..1274
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          1394..1450
                     /region_name="Syndecan"
                     /note="Syndecan domain; pfam01034"
                     /db_xref="CDD:460035"
     Region          1414..1432
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1468
                     /gene="NRXN3"
                     /gene_synonym="C14orf60"
                     /coded_by="NM_001366426.1:1006..5412"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS91913.1"
                     /db_xref="GeneID:9369"
                     /db_xref="HGNC:HGNC:8010"
                     /db_xref="MIM:600567"
ORIGIN      
        1 msstlhsvff tlkvsillgs llglclglef mglpnqwary lrwdastrsd lsfqfktnvs
       61 tglllylddg gvcdflclsl vdgrvqlrfs mdcaetavls nkqvndsswh flmvsrdrlr
      121 tvlmldgegq sgelqpqrpy mdvvsdlflg gvptdirpsa ltldgvqamp gfkglildlk
      181 ygnseprllg srgvqmdaeg pcgerpceng gicflldghp tcdcsttgyg gklcsedvsq
      241 dpglshlmms eqgrskaree nvatfrgsey lcydlsqnpi qsssdeitls fktwqrngli
      301 lhtgksadyv nlalkdgavs lvinlgsgaf eaivepvngk fndnawhdvk vtrnlrqvti
      361 svdgiltttg ytqedytmlg sddffyvggs pstadlpgsp vsnnfmgclk evvyknndir
      421 lelsrlaria dtkmkiygev vfkcenvatl dpinfetpea yislpkwntk rmgsisfdfr
      481 ttepnglilf thgkpqerkd arsqkntkvd ffavelldgn lyllldmgsg tikvkatqkk
      541 andgewyhvd iqrdgrsgti svnsrrtpft asgeseildl egdmylgglp enraglilpt
      601 elwtamlnyg yvgcirdlfi dgrsknirql aemqnaagvk sscsrmsakq cdsypcknna
      661 vckdgwnrfi cdctgtgywg rtcereasil sydgsmymki impmvmhtea edvsfrfmsq
      721 raygllvatt srdsadtlrl eldggrvklm vnldcirinc nsskgpetly agqklndnew
      781 htvrvvrrgk slkltvdddv aegtmvgdht rlefhnietg imtekryisv vpssfighlq
      841 slmfngllyi dlckngdidy celkarfglr niiadpvtfk tkssylslat lqaytsmhlf
      901 fqfkttspdg filfnsgdgn dfiavelvkg yihyvfdlgn gpnvikgnsd rplndnqwhn
      961 vvitrdnsnt hslkvdtkvv tqvingaknl dlkgdlymag laqgmysnlp klvasrdgfq
     1021 gclasvdlng rlpdlindal hrsgqiergc egpsttcqed scanqgvcmq qwegftcdcs
     1081 mtsysgnqcn dpgatyifgk sgglilytwp andrpstrsd rlavgfsttv kdgilvrids
     1141 apglgdflql hieqgkigvv fnigtvdisi keertpvndg kyhvvrftrn ggnatlqvdn
     1201 wpvnehyptg ntdnerfqmv kqkipfkynr pveewlqekg rqltifntqa qiaiggkdkg
     1261 rlfqgqlsgl yydglkvlnm aaennpniki ngsvrlvgev psilgttqtt smppemsttv
     1321 mettttmatt ttrknrstas iqptsddlvs saecssdded fvecepstan ptepgirrvp
     1381 gaseviress sttgmvvgiv aaaalcilil lyamykyrnr degsyqvdet rnyisnsaqs
     1441 ngtlmkekqq ssksghkkqk nkdreyyv
//
LOCUS       NP_001406                472 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 2 subunit 3 [Homo
            sapiens].
ACCESSION   NP_001406
VERSION     NP_001406.1
DBSOURCE    REFSEQ: accession NM_001415.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Cardenal Peralta,C., Vandroux,P., Neumann-Arnold,L., Panvert,M.,
            Fagart,J., Seufert,W., Mechulam,Y. and Schmitt,E.
  TITLE     Binding of human Cdc123 to eIF2gamma
  JOURNAL   J Struct Biol 215 (3), 108006 (2023)
   PUBMED   37507029
  REMARK    GeneRIF: Binding of human Cdc123 to eIF2gamma.
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Ivanova,N., Serzhanova,V., Demina,N., Guseva,D. and Skoblov,M.
  TITLE     mRNA analysis revealed a novel pathogenic EIF2S3 variant causing
            MEHMO syndrome
  JOURNAL   Eur J Med Genet 65 (2), 104421 (2022)
   PUBMED   34999262
  REMARK    GeneRIF: mRNA analysis revealed a novel pathogenic EIF2S3 variant
            causing MEHMO syndrome.
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Lu,J., Chen,S., Tan,H., Huang,Z., Li,B., Liu,L., Chen,Y., Zeng,X.,
            Zou,Y. and Xu,L.
  TITLE     Eukaryotic initiation factor-2, gamma subunit, suppresses
            proliferation and regulates the cell cycle via the MAPK/ERK
            signaling pathway in acute myeloid leukemia
  JOURNAL   J Cancer Res Clin Oncol 147 (11), 3157-3168 (2021)
   PUBMED   34232382
  REMARK    GeneRIF: Eukaryotic initiation factor-2, gamma subunit, suppresses
            proliferation and regulates the cell cycle via the MAPK/ERK
            signaling pathway in acute myeloid leukemia.
REFERENCE   6  (residues 1 to 472)
  AUTHORS   Ehrmann,I.E., Ellis,P.S., Mazeyrat,S., Duthie,S., Brockdorff,N.,
            Mattei,M.G., Gavin,M.A., Affara,N.A., Brown,G.M., Simpson,E.,
            Mitchell,M.J. and Scott,D.M.
  TITLE     Characterization of genes encoding translation initiation factor
            eIF-2gamma in mouse and human: sex chromosome localization, escape
            from X-inactivation and evolution
  JOURNAL   Hum Mol Genet 7 (11), 1725-1737 (1998)
   PUBMED   9736774
REFERENCE   7  (residues 1 to 472)
  AUTHORS   Brand,S.R., Kobayashi,R. and Mathews,M.B.
  TITLE     The Tat protein of human immunodeficiency virus type 1 is a
            substrate and inhibitor of the interferon-induced, virally
            activated protein kinase, PKR
  JOURNAL   J Biol Chem 272 (13), 8388-8395 (1997)
   PUBMED   9079663
REFERENCE   8  (residues 1 to 472)
  AUTHORS   Gaspar,N.J., Kinzy,T.G., Scherer,B.J., Humbelin,M., Hershey,J.W.
            and Merrick,W.C.
  TITLE     Translation initiation factor eIF-2. Cloning and expression of the
            human cDNA encoding the gamma-subunit
  JOURNAL   J Biol Chem 269 (5), 3415-3422 (1994)
   PUBMED   8106381
REFERENCE   9  (residues 1 to 472)
  AUTHORS   Ray,M.K., Chakraborty,A., Datta,B., Chattopadhyay,A., Saha,D.,
            Bose,A., Kinzy,T.G., Wu,S., Hileman,R.E., Merrick,W.C. et al.
  TITLE     Characteristics of the eukaryotic initiation factor 2 associated
            67-kDa polypeptide
  JOURNAL   Biochemistry 32 (19), 5151-5159 (1993)
   PUBMED   8098621
REFERENCE   10 (residues 1 to 472)
  AUTHORS   Safer,B., Adams,S.L., Anderson,W.F. and Merrick,W.C.
  TITLE     Binding of MET-TRNAf and GTP to homogeneous initiation factor MP
  JOURNAL   J Biol Chem 250 (23), 9076-9082 (1975)
   PUBMED   1104615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC019906.1, BC011945.1, AI133612.1, BF435665.1 and
            CB150474.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the largest subunit of
            a heterotrimeric GTP-binding protein involved in the recruitment of
            methionyl-tRNA(i) to the 40 S ribosomal subunit. [provided by
            RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.218577.1,
                                           SRR1660807.237157.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253039.9/ ENSP00000253039.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.11"
     Protein         1..472
                     /product="eukaryotic translation initiation factor 2
                     subunit 3"
                     /EC_number="3.6.5.3"
                     /note="eukaryotic translation initiation factor 2G;
                     eIF-2gX; eIF2-gamma X; eIF-2-gamma X; eukaryotic
                     translation initiation factor 2 subunit gamma X;
                     eukaryotic translation initiation factor 2, subunit 3
                     gamma, 52kDa; mental retardation, epileptic seizures,
                     hypogonadism and -genitalism, microcephaly and obesity
                     syndrome"
                     /calculated_mol_wt=50979
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine, partial.
                     /evidence=ECO:0000269|Ref.8; propagated from
                     UniProtKB/Swiss-Prot (P41091.3)"
     Region          13..466
                     /region_name="PTZ00327"
                     /note="eukaryotic translation initiation factor 2 gamma
                     subunit; Provisional"
                     /db_xref="CDD:240362"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0N1; propagated from
                     UniProtKB/Swiss-Prot (P41091.3)"
     Region          48..55
                     /region_name="G1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          76..80
                     /region_name="G2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          134..137
                     /region_name="G3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          190..193
                     /region_name="G4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          225..227
                     /region_name="G5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01059"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     Region          457..469
                     /region_name="Interacts with CDC123.
                     /evidence=ECO:0000305|PubMed:35031321"
                     /note="propagated from UniProtKB/Swiss-Prot (P41091.3)"
     CDS             1..472
                     /gene="EIF2S3"
                     /gene_synonym="eIF-2gA; EIF2; EIF2G; EIF2gamma; eIF2gX;
                     MEHMO; MRXSBRK"
                     /coded_by="NM_001415.4:14..1432"
                     /db_xref="CCDS:CCDS14210.1"
                     /db_xref="GeneID:1968"
                     /db_xref="HGNC:HGNC:3267"
                     /db_xref="MIM:300161"
ORIGIN      
        1 maggeagvtl gqphlsrqdl ttldvtkltp lshevisrqa tinigtighv ahgkstvvka
       61 isgvhtvrfk nelernitik lgyanakiyk lddpscprpe cyrscgsstp defptdipgt
      121 kgnfklvrhv sfvdcpghdi lmatmlngaa vmdaalllia gnescpqpqt sehlaaieim
      181 klkhililqn kidlvkesqa keqyeqilaf vqgtvaegap iipisaqlky nievvceyiv
      241 kkipvpprdf tseprlivir sfdvnkpgce vddlkggvag gsilkgvlkv gqeievrpgi
      301 vskdsegklm ckpifskivs lfaehndlqy aapggligvg tkidptlcra drmvgqvlga
      361 vgalpeifte leisyfllrr llgvrtegdk kaakvqklsk nevlmvnigs lstggrvsav
      421 kadlgkivlt npvctevgek ialsrrvekh wrligwgqir rgvtikptvd dd
//
LOCUS       NP_001354653             299 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform a [Homo sapiens].
ACCESSION   NP_001354653
VERSION     NP_001354653.1
DBSOURCE    REFSEQ: accession NM_001367724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (8), as well as variants 1, 6, and
            7, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.26144.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..299
                     /product="rab5 GDP/GTP exchange factor isoform a"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=34307
     Region          <9..28
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          78..178
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..299
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367724.1:682..1581"
                     /note="isoform a is encoded by transcript variant 8"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mqtrgkvppe rvekimdqie kyimtrlyky vfcpettdde kkdlaiqkri ralrwvtpqm
       61 lcvpvnedip evsdmvvkai tdiiemdskr vprdklacit kcskhifnai kitknepasa
      121 ddflptliyi vlkgnpprlq sniqyitrfc npsrlmtged gyyftnlcca vafiekldaq
      181 slnlsqedfd rymsgqtspr kqeaeswspd aclgvkqmyk nldllsqlne rqerimneak
      241 klekdlidwt dgiarevqdi vekypleikp pnqplaaids envendklpp plqpqvyag
//
LOCUS       NP_808820                324 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1A isoform 2 [Homo sapiens].
ACCESSION   NP_808820
VERSION     NP_808820.1
DBSOURCE    REFSEQ: accession NM_177951.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Cheng,P., Wang,Y., Wu,Q., Zhang,H., Fang,W. and Feng,F.
  TITLE     Role of TRIM59 in regulating PPM1A in the pathogenesis of silicosis
            and the intervention effect of tanshinone IIA
  JOURNAL   Biomed Pharmacother 177, 117014 (2024)
   PUBMED   38908195
  REMARK    GeneRIF: Role of TRIM59 in regulating PPM1A in the pathogenesis of
            silicosis and the intervention effect of tanshinone IIA.
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Weon,S., Jo,S., Nam,B., Choi,S.H., Park,Y.S., Kim,Y.G. and Kim,T.H.
  TITLE     Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway
  JOURNAL   J Cell Mol Med 27 (5), 650-658 (2023)
   PUBMED   36756789
  REMARK    GeneRIF: Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Feng,D., Zhou,J., Liu,H., Wu,X., Li,F., Zhao,J., Zhang,Y., Wang,L.,
            Chao,M., Wang,Q., Qin,H., Ge,S., Liu,Q., Zhang,J. and Qu,Y.
  TITLE     Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain barrier
            disruption after subarachnoid hemorrhage
  JOURNAL   Sci Adv 8 (39), eabq2423 (2022)
   PUBMED   36179025
  REMARK    GeneRIF: Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain
            barrier disruption after subarachnoid hemorrhage.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Liu,C., Sun,W., Yang,K. and Xia,B.
  TITLE     Knockdown of TRIM65 suppressed the proliferation and invasiveness
            of gastric cancer cells by restricting the ubiquitin degradation of
            PPM1A
  JOURNAL   Exp Cell Res 416 (2), 113154 (2022)
   PUBMED   35421368
  REMARK    GeneRIF: Knockdown of TRIM65 suppressed the proliferation and
            invasiveness of gastric cancer cells by restricting the ubiquitin
            degradation of PPM1A.
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Fjeld,C.C. and Denu,J.M.
  TITLE     Kinetic analysis of human serine/threonine protein phosphatase
            2Calpha
  JOURNAL   J Biol Chem 274 (29), 20336-20343 (1999)
   PUBMED   10400656
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Takekawa,M., Maeda,T. and Saito,H.
  TITLE     Protein phosphatase 2Calpha inhibits the human stress-responsive
            p38 and JNK MAPK pathways
  JOURNAL   EMBO J 17 (16), 4744-4752 (1998)
   PUBMED   9707433
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Das,A.K., Helps,N.R., Cohen,P.T. and Barford,D.
  TITLE     Crystal structure of the protein serine/threonine phosphatase 2C at
            2.0 A resolution
  JOURNAL   EMBO J 15 (24), 6798-6809 (1996)
   PUBMED   9003755
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Redpath,N.T., Price,N.T., Severinov,K.V. and Proud,C.G.
  TITLE     Regulation of elongation factor-2 by multisite phosphorylation
  JOURNAL   Eur J Biochem 213 (2), 689-699 (1993)
   PUBMED   8386634
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Mann,D.J., Campbell,D.G., McGowan,C.H. and Cohen,P.T.
  TITLE     Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and
            comparative analysis of amino acid sequences
  JOURNAL   Biochim Biophys Acta 1130 (1), 100-104 (1992)
   PUBMED   1311954
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157756.3, DA439296.1,
            AF070670.1 and CB156710.1.
            
            Summary: The protein encoded by this gene is a member of the PP2C
            family of Ser/Thr protein phosphatases. PP2C family members are
            known to be negative regulators of cell stress response pathways.
            This phosphatase dephosphorylates, and negatively regulates the
            activities of, MAP kinases and MAP kinase kinases. It has been
            shown to inhibit the activation of p38 and JNK kinase cascades
            induced by environmental stresses. This phosphatase can also
            dephosphorylate cyclin-dependent kinases, and thus may be involved
            in cell cycle control. Overexpression of this phosphatase is
            reported to activate the expression of the tumor suppressor gene
            TP53/p53, which leads to G2/M cell cycle arrest and apoptosis.
            Three alternatively spliced transcript variants encoding distinct
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) has an additional exon within
            the 5' UTR and lacks a few of 3' exons but has an alternate 3'
            segment, as compared to variant 1. The resulting isoform (2) has a
            distinct and shorter C-terminus, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF070670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..324
                     /product="protein phosphatase 1A isoform 2"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 1A"
                     /calculated_mol_wt=35827
     Region          23..291
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(33,37..38,60..62,239,282)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Region          285..>317
                     /region_name="PP2C_C"
                     /note="Protein serine/threonine phosphatase 2C, C-terminal
                     domain; pfam07830"
                     /db_xref="CDD:429684"
     CDS             1..324
                     /gene="PPM1A"
                     /gene_synonym="PP2C-ALPHA; PP2CA; PP2Calpha"
                     /coded_by="NM_177951.3:580..1554"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9745.1"
                     /db_xref="GeneID:5494"
                     /db_xref="HGNC:HGNC:9275"
                     /db_xref="MIM:606108"
ORIGIN      
        1 mgafldkpkm ekhnaqgqgn glryglssmq gwrvemedah taviglpsgl eswsffavyd
       61 ghagsqvaky ccehlldhit nnqdfkgsag apsvenvkng irtgfleide hmrvmsekkh
      121 gadrsgstav gvlispqhty fincgdsrgl lcrnrkvhff tqdhkpsnpl ekeriqnagg
      181 svmiqrvngs lavsralgdf dykcvhgkgp teqlvspepe vhdierseed dqfiilacdg
      241 iwdvmgneel cdfvrsrlev tddlekvcne vvdtclykgs rdnmsvilic fpnapkvspe
      301 avkkeaeldk ylecrveggs fnkk
//
LOCUS       NP_001139550             239 aa            linear   PRI 20-NOV-2025
DEFINITION  claudin-14 [Homo sapiens].
ACCESSION   NP_001139550
VERSION     NP_001139550.1
DBSOURCE    REFSEQ: accession NM_001146078.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Mohanty,S., White,J.K., Scheffschick,A., Fischer,B., Pathak,A.,
            Tovi,J., Ostenson,C.G., Aspenstrom,P., Brauner,H. and Brauner,A.
  TITLE     Diabetes compromises tight junction protein claudin 14 in the
            urinary bladder
  JOURNAL   Cell Tissue Res 398 (1), 27-33 (2024)
   PUBMED   39162877
  REMARK    GeneRIF: Diabetes compromises tight junction protein claudin 14 in
            the urinary bladder.
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Mizukami,Y., Ito,A., Hashimoto,S., Ando,T., Ishikawa,Y., Eguchi,H.,
            Yoshino,Y., Matsunaga,T. and Ikari,A.
  TITLE     Downregulation of chemoresistance by claudin-14 silencing in human
            colorectal cancer cells
  JOURNAL   Arch Biochem Biophys 758, 110075 (2024)
   PUBMED   38942107
  REMARK    GeneRIF: Downregulation of chemoresistance by claudin-14 silencing
            in human colorectal cancer cells.
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Khatami,F., Gorji,A., Khoshchehreh,M., Mashhadi,R., Pishkuhi,M.A.,
            Khajavi,A., Shabestari,A.N. and Aghamir,S.M.K.
  TITLE     The correlation between promoter hypermethylation of VDR, CLDN, and
            CasR genes and recurrent stone formation
  JOURNAL   BMC Med Genomics 15 (1), 109 (2022)
   PUBMED   35546405
  REMARK    GeneRIF: The correlation between promoter hypermethylation of VDR,
            CLDN, and CasR genes and recurrent stone formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Tsukita,S., Furuse,M. and Itoh,M.
  TITLE     Multifunctional strands in tight junctions
  JOURNAL   Nat Rev Mol Cell Biol 2 (4), 285-293 (2001)
   PUBMED   11283726
  REMARK    Review article
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Heiskala,M., Peterson,P.A. and Yang,Y.
  TITLE     The roles of claudin superfamily proteins in paracellular transport
  JOURNAL   Traffic 2 (2), 93-98 (2001)
   PUBMED   11247307
  REMARK    Review article
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Wilcox,E.R., Burton,Q.L., Naz,S., Riazuddin,S., Smith,T.N.,
            Ploplis,B., Belyantseva,I., Ben-Yosef,T., Liburd,N.A., Morell,R.J.,
            Kachar,B., Wu,D.K., Griffith,A.J., Riazuddin,S. and Friedman,T.B.
  TITLE     Mutations in the gene encoding tight junction claudin-14 cause
            autosomal recessive deafness DFNB29
  JOURNAL   Cell 104 (1), 165-172 (2001)
   PUBMED   11163249
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Kniesel,U. and Wolburg,H.
  TITLE     Tight junctions of the blood-brain barrier
  JOURNAL   Cell Mol Neurobiol 20 (1), 57-76 (2000)
   PUBMED   10690502
  REMARK    Review article
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI655909.1, AJ566765.1 and
            BC012126.1.
            
            Summary: Tight junctions represent one mode of cell-to-cell
            adhesion in epithelial or endothelial cell sheets, forming
            continuous seals around cells and serving as a physical barrier to
            prevent solutes and water from passing freely through the
            paracellular space. These junctions are comprised of sets of
            continuous networking strands in the outwardly facing cytoplasmic
            leaflet, with complementary grooves in the inwardly facing
            extracytoplasmic leaflet. The protein encoded by this gene, a
            member of the claudin family, is an integral membrane protein and a
            component of tight junction strands. The encoded protein also binds
            specifically to the WW domain of Yes-associated protein. Defects in
            this gene are the cause of an autosomal recessive form of
            nonsyndromic sensorineural deafness. It is also reported that four
            synonymous variants in this gene are associated with kidney stones
            and reduced bone mineral density. Several transcript variants
            encoding the same protein have been found for this gene. [provided
            by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (gamma) differs in the 5' UTR
            compared to variant 1. All five variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ566765.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145774 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..239
                     /product="claudin-14"
                     /calculated_mol_wt=25568
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Region          23..181
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Region          196..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     CDS             1..239
                     /gene="CLDN14"
                     /gene_synonym="DFNB29"
                     /coded_by="NM_001146078.3:440..1159"
                     /db_xref="CCDS:CCDS13645.1"
                     /db_xref="GeneID:23562"
                     /db_xref="HGNC:HGNC:2035"
                     /db_xref="MIM:605608"
ORIGIN      
        1 mastavqllg fllsflgmvg tlittilphw rrtahvgtni ltavsylkgl wmecvwhstg
       61 iyqcqiyrsl lalpqdlqaa ralmviscll sgiacacavi gmkctrcakg tpakttfail
      121 ggtlfilagl lcmvavswtt ndvvqnfynp llpsgmkfei gqalylgfis sslsliggtl
      181 lclscqdeap yrpyqappra ttttantapa yqppaaykdn rapsvtsath sgyrlndyv
//
LOCUS       NP_065178                418 aa            linear   PRI 20-NOV-2025
DEFINITION  actin-related protein 3B isoform 1 [Homo sapiens].
ACCESSION   NP_065178 XP_942767
VERSION     NP_065178.1
DBSOURCE    REFSEQ: accession NM_020445.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Abella,J.V., Galloni,C., Pernier,J., Barry,D.J., Kjaer,S.,
            Carlier,M.F. and Way,M.
  TITLE     Isoform diversity in the Arp2/3 complex determines actin filament
            dynamics
  JOURNAL   Nat Cell Biol 18 (1), 76-86 (2016)
   PUBMED   26655834
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Shin,J.H., Gulesserian,T., Weitzdoerfer,R., Fountoulakis,M. and
            Lubec,G.
  TITLE     Derangement of hypothetical proteins in fetal Down's syndrome brain
  JOURNAL   Neurochem Res 29 (6), 1307-1316 (2004)
   PUBMED   15176487
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Shindo-Okada,N. and Iigo,M.
  TITLE     Expression of the Arp11 gene suppresses the tumorigenicity of PC-14
            human lung adenocarcinoma cells
  JOURNAL   Biochem Biophys Res Commun 312 (4), 889-896 (2003)
   PUBMED   14651955
  REMARK    GeneRIF: Thus, overexpression of Arp11 may suppress tumorigenicity
            in nude mice.
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Eckley,D.M. and Schroer,T.A.
  TITLE     Interactions between the evolutionarily conserved, actin-related
            protein, Arp11, actin, and Arp1
  JOURNAL   Mol Biol Cell 14 (7), 2645-2654 (2003)
   PUBMED   12857853
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Shindo-Okada,N. and Shimizu,K.
  TITLE     Isolation of a novel actin-related gene expressed in low-metastatic
            PC-14 human lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 280 (1), 61-67 (2001)
   PUBMED   11162478
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Jay,P., Berge-Lefranc,J.L., Massacrier,A., Roessler,E., Wallis,D.,
            Muenke,M., Gastaldi,M., Taviaux,S., Cau,P. and Berta,P.
  TITLE     ARP3beta, the gene encoding a new human actin-related protein, is
            alternatively spliced and predominantly expressed in brain neuronal
            cells
  JOURNAL   Eur J Biochem 267 (10), 2921-2928 (2000)
   PUBMED   10806390
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Machesky,L.M. and Gould,K.L.
  TITLE     The Arp2/3 complex: a multifunctional actin organizer
  JOURNAL   Curr Opin Cell Biol 11 (1), 117-121 (1999)
   PUBMED   10047519
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN601600.1, AK315534.1,
            AB209174.1 and AA559050.1.
            
            On Mar 4, 2006 this sequence version replaced XP_942767.1.
            
            Summary: This gene encodes a member of the actin-related proteins
            (ARP), which form multiprotein complexes and share 35-55% amino
            acid identity with conventional actin. The protein encoded by this
            gene may have a regulatory role in the actin cytoskeleton and
            induce cell-shape change and motility. Pseudogenes of this gene are
            located on chromosomes 2, 4, 10, 16, 22 and Y. Alternative splicing
            results in multiple transcript variants and protein isoforms.
            [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.247181.1,
                                           SRR1660803.17233.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256001.13/ ENSP00000256001.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1-q36.2"
     Protein         1..418
                     /product="actin-related protein 3B isoform 1"
                     /note="actin-related protein 3-beta; actin-related protein
                     Arp11; ARP3-beta; actin-like protein 3B; actin-related
                     protein ARP4; ARP3 actin related protein 3 homolog B"
                     /calculated_mol_wt=47477
     Region          7..410
                     /region_name="ASKHA_NBD_Arp3-like"
                     /note="nucleotide-binding domain (NBD) of actin-related
                     protein3 (Arp3) and similar proteins; cd10221"
                     /db_xref="CDD:466822"
     CDS             1..418
                     /gene="ACTR3B"
                     /gene_synonym="ARP11; ARP3BETA"
                     /coded_by="NM_020445.6:132..1388"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5934.1"
                     /db_xref="GeneID:57180"
                     /db_xref="HGNC:HGNC:17256"
ORIGIN      
        1 magslppcvv dcgtgytklg yagntepqfi ipsciaires akvvdqaqrr vlrgvddldf
       61 figdeaidkp tyatkwpirh giiedwdlme rfmeqvvfky lraepedhyf lmtepplntp
      121 enreylaeim fesfnvpgly iavqavlala aswtsrqvge rtltgivids gdgvthvipv
      181 aegyvigsci khipiagrdi tyfiqqllre revgippeqs letakaikek ycyicpdivk
      241 efakydvdpr kwikqytgin ainqkkfvid vgyerflgpe iffhpefanp dfmesisdvv
      301 deviqncpid vrrplyknvv lsggstmfrd fgrrlqrdlk rvvdarlrls eelsggrikp
      361 kpvevqvvth hmqryavwfg gsmlastpef fqvchtkkdy eeygpsicrh npvfgvms
//
LOCUS       NP_003321                551 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin reductase 1, cytoplasmic isoform 2 [Homo sapiens].
ACCESSION   NP_003321
VERSION     NP_003321.3
DBSOURCE    REFSEQ: accession NM_003330.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Hsieh,M.S., Ling,H.H., Setiawan,S.A., Hardianti,M.S., Fong,I.H.,
            Yeh,C.T. and Chen,J.H.
  TITLE     Therapeutic targeting of thioredoxin reductase 1 causes ferroptosis
            while potentiating anti-PD-1 efficacy in head and neck cancer
  JOURNAL   Chem Biol Interact 395, 111004 (2024)
   PUBMED   38636790
  REMARK    GeneRIF: Therapeutic targeting of thioredoxin reductase 1 causes
            ferroptosis while potentiating anti-PD-1 efficacy in head and neck
            cancer.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Shen,X., Xia,Y., Lu,H., Zheng,P., Wang,J., Chen,Y., Xu,C., Qiu,C.,
            Zhang,Y., Xiao,Z., Zou,P., Cui,R. and Ni,D.
  TITLE     Synergistic targeting of TrxR1 and ATM/AKT pathway in human colon
            cancer cells
  JOURNAL   Biomed Pharmacother 174, 116507 (2024)
   PUBMED   38565059
  REMARK    GeneRIF: Synergistic targeting of TrxR1 and ATM/AKT pathway in
            human colon cancer cells.
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Nalvarte,I., Damdimopoulos,A.E., Ruegg,J. and Spyrou,G.
  TITLE     The expression and activity of thioredoxin reductase 1 splice
            variants v1 and v2 regulate the expression of genes associated with
            differentiation and adhesion
  JOURNAL   Biosci Rep 35 (6), e00269 (2015)
   PUBMED   26464515
  REMARK    GeneRIF: TXNRD1_v1 and TXNRD1_v2 have distinct roles in
            differentiation, possibly by altering the expression of the genes
            associated with differentiation, and further emphasize the
            importance in distinguishing each unique action of different TrxR1
            splice forms
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Dammeyer,P., Damdimopoulos,A.E., Nordman,T., Jimenez,A.,
            Miranda-Vizuete,A. and Arner,E.S.
  TITLE     Induction of cell membrane protrusions by the N-terminal
            glutaredoxin domain of a rare splice variant of human thioredoxin
            reductase 1
  JOURNAL   J Biol Chem 283 (5), 2814-2821 (2008)
   PUBMED   18042542
  REMARK    GeneRIF: the Grx domain of TXNRD1_v3 localizes first in the
            emerging cell membrane protrusion and is then followed into the
            protrusions by actin and subsequently by tubulin
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Gladyshev,V.N., Jeang,K.T. and Stadtman,T.C.
  TITLE     Selenocysteine, identified as the penultimate C-terminal residue in
            human T-cell thioredoxin reductase, corresponds to TGA in the human
            placental gene
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 6146-6151 (1996)
   PUBMED   8650234
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Tamura,T. and Stadtman,T.C.
  TITLE     A new selenoprotein from human lung adenocarcinoma cells:
            purification, properties, and thioredoxin reductase activity
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1006-1011 (1996)
   PUBMED   8577704
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-linked peroxidase from human red blood cell: evidence
            for the existence of thioredoxin and thioredoxin reductase in human
            red blood cell
  JOURNAL   Biochem Biophys Res Commun 217 (3), 900-907 (1995)
   PUBMED   8554614
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Gasdaska,P.Y., Gasdaska,J.R., Cochran,S. and Powis,G.
  TITLE     Cloning and sequencing of a human thioredoxin reductase
  JOURNAL   FEBS Lett 373 (1), 5-9 (1995)
   PUBMED   7589432
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Schallreuter,K.U., Grebe,T., Pittelkow,M.R. and Wood,J.M.
  TITLE     [3H]-13-cis-retinoic acid covalently binds to thioredoxin reductase
            in human keratinocytes
  JOURNAL   Skin Pharmacol 4 (1), 14-20 (1991)
   PUBMED   2064786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC351122.1, AK226071.1,
            BC018122.1 and AI097548.1.
            
            On May 23, 2007 this sequence version replaced NP_003321.2.
            
            Summary: The protein encoded by this gene belongs to the pyridine
            nucleotide-disulfide oxidoreductase family, and is a member of the
            thioredoxin (Trx) system. Three thioredoxin reductase (TrxR)
            isozymes are found in mammals. TrxRs are selenocysteine-containing
            flavoenzymes, which reduce thioredoxins, as well as other
            substrates, and play a key role in redox homoeostasis. This gene
            encodes an ubiquitously expressed, cytosolic form of TrxR, which
            functions as a homodimer containing FAD, and selenocysteine (Sec)
            at the active site. Sec is encoded by UGA codon that normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, the Sec insertion sequence
            (SECIS) element, which is necessary for the recognition of UGA as a
            Sec codon rather than as a stop signal. Alternative splicing,
            primarily at the 5' end, results in transcript variants encoding
            same or different isoforms, including a glutaredoxin-containing
            isoform that is predominantly expressed in testis. [provided by
            RefSeq, May 2017].
            
            Transcript Variant: This variant (4) uses an alternate donor splice
            site at the 5' terminal exon, which results in translation
            initiation from an in-frame upstream start codon compared to
            variant 1. The encoded isoform (2, also known as TXNRD1_v2) has a
            longer and distinct N-terminus, and is thought to differentially
            regulate genes associated with differentiation and adhesion
            compared to isoform 1 (PMID:26464515).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.200117.1,
                                           SRR1803611.274629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: PMID: 7589432, 8650234
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..551
                     /product="thioredoxin reductase 1, cytoplasmic isoform 2"
                     /EC_number="1.8.1.9"
                     /EC_number="1.11.1.2"
                     /note="KM-102-derived reductase-like factor; thioredoxin
                     reductase GRIM-12; thioredoxin reductase 1, cytoplasmic;
                     oxidoreductase; thioredoxin reductase TR1; gene associated
                     with retinoic and IFN-induced mortality 12 protein;
                     selenoprotein TXNRD1; gene associated with retinoic and
                     interferon-induced mortality 12 protein; testis tissue
                     sperm-binding protein Li 46a; peroxidase TXNRD1"
                     /calculated_mol_wt=60288
     Region          <4..50
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Region          63..551
                     /region_name="TGR"
                     /note="thioredoxin and glutathione reductase
                     selenoprotein; TIGR01438"
                     /db_xref="CDD:273624"
     Site            550
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..551
                     /gene="TXNRD1"
                     /gene_synonym="GRIM-12; TR; TR1; TRXR1; TXNR; TXNR1"
                     /coded_by="NM_003330.4:306..1961"
                     /note="UGA stop codon recoded as selenocysteine; isoform 2
                     is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53821.1"
                     /db_xref="GeneID:7296"
                     /db_xref="HGNC:HGNC:12437"
                     /db_xref="MIM:601112"
ORIGIN      
        1 mscedgrale gtlselaaet dlpvvfvkqr kigghgptlk ayqegrlqkl lkmngpedlp
       61 ksydydliii gggsgglaaa keaaqygkkv mvldfvtptp lgtrwglggt cvnvgcipkk
      121 lmhqaallgq alqdsrnygw kveetvkhdw drmieavqnh igslnwgyrv alrekkvvye
      181 naygqfigph rikatnnkgk ekiysaerfl iatgerpryl gipgdkeyci ssddlfslpy
      241 cpgktlvvga syvalecagf lagigldvtv mvrsillrgf dqdmankige hmeehgikfi
      301 rqfvpikveq ieagtpgrlr vvaqstnsee iiegeyntvm laigrdactr kigletvgvk
      361 inektgkipv tdeeqtnvpy iyaigdiled kveltpvaiq agrllaqrly agstvkcdye
      421 nvpttvftpl eygacglsee kavekfgeen ievyhsyfwp lewtipsrdn nkcyakiicn
      481 tkdnervvgf hvlgpnagev tqgfaaalkc gltkkqldst igihpvcaev fttlsvtkrs
      541 gasilqagcu g
//
LOCUS       NP_001341229            1439 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 3 [Homo sapiens].
ACCESSION   NP_001341229 XP_006717107
VERSION     NP_001341229.1
DBSOURCE    REFSEQ: accession NM_001354300.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1439)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1439)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1439)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1439)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1439)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1439)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1439)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1439)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1439)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1439)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On Aug 10, 2017 this sequence version replaced XP_006717107.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.113729.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1439
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1439
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 3"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=160476
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Region          1224..1287
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1335..1436
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1439
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001354300.2:216..4535"
                     /note="isoform 3 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS65130.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgpsn rsnsvssldl egesvselga gpsgsngvea lqlleheqat
      601 tqdnlddklr kfeirdmmgl tddrdisetv setwstdvlg sdfdpnided rlqeiagaaa
      661 enmlgsllcl pgsgsvlldp ctgstisett seawsvevlp sdseapdlkq eerlqelesc
      721 sglgstsddt dvrevssrps tpglsvvsgi satsedipnk iedlrsecss dfggkdsvts
      781 pdmdeithga hqltsppsqs esllamfdpl sshegasavv rpkvhyarps hpppdppile
      841 gavggnearl pnfgshvltp aemeafkqrh syperlvrsr ssdivssvrr pmsdpswnrr
      901 pgneerelpp aaaigatslv aaphsssssp skdssrgete erkdsddeks drnrpwwrkr
      961 fvsampkapi pfrkkekqek dkddlgpdrf stltddpspr lsaqaqvaed ildkyrnaik
     1021 rtspsdgama nyestevmgd gesahdsprd ealqnisadd lpdsasqaah pqdsafsyrd
     1081 akkklrlalc sadsvafpvl thstrnglpd htdpedneiv cflkvqiaea inlqdknlma
     1141 qlqetmrcvc rfdnrtcrkl lasiaedyrk rapyiayltr crqglqttqa hlerllqrvl
     1201 rdkevanryf ttvcvrllle skekkirefi qdfqkltaad dktaqvedfl qflygamaqd
     1261 viwqnaseeq lqdaqlaier svmnrifkla fypnqdgdil rdqvlhehiq rlskvvtanh
     1321 ralqipevyl reapwpsaqs eirtisaykt prdkvqcilr mcstimnlls lanedsvpga
     1381 ddfvpvlvfv likanppcll stvqyissfy asclsgeesy wwmqftaave fiktiddrk
//
LOCUS       NP_001338779            1922 aa            linear   PRI 20-NOV-2025
DEFINITION  trinucleotide repeat-containing gene 6A protein isoform 3 [Homo
            sapiens].
ACCESSION   NP_001338779
VERSION     NP_001338779.1
DBSOURCE    REFSEQ: accession NM_001351850.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1922)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1922)
  AUTHORS   Li,M., Zhai,P., Mu,X., Song,J., Zhang,H. and Su,J.
  TITLE     Hypoxic BMSC-derived exosomal miR-652-3p promotes proliferation and
            metastasis of hepatocarcinoma cancer cells via targeting TNRC6A
  JOURNAL   Aging (Albany NY) 15 (22), 12780-12793 (2023)
   PUBMED   37976119
  REMARK    GeneRIF: Hypoxic BMSC-derived exosomal miR-652-3p promotes
            proliferation and metastasis of hepatocarcinoma cancer cells via
            targeting TNRC6A.
REFERENCE   3  (residues 1 to 1922)
  AUTHORS   Majerciak,V., Zhou,T., Kruhlak,M.J. and Zheng,Z.M.
  TITLE     RNA helicase DDX6 and scaffold protein GW182 in P-bodies promote
            biogenesis of stress granules
  JOURNAL   Nucleic Acids Res 51 (17), 9337-9355 (2023)
   PUBMED   37427791
  REMARK    GeneRIF: RNA helicase DDX6 and scaffold protein GW182 in P-bodies
            promote biogenesis of stress granules.
REFERENCE   4  (residues 1 to 1922)
  AUTHORS   Yang,R., Han,J. and Zhao,S.
  TITLE     LINC01082 Inhibits Non-Small Cell Lung Cancer by Targeting the
            miR-543/TNRC6A Axis
  JOURNAL   Biochem Genet 61 (4), 1585-1605 (2023)
   PUBMED   36719626
  REMARK    GeneRIF: LINC01082 Inhibits Non-Small Cell Lung Cancer by Targeting
            the miR-543/TNRC6A Axis.
REFERENCE   5  (residues 1 to 1922)
  AUTHORS   Chen,W., Ru,J., Wu,T., Man,D., Wu,J., Wu,L., Sun,Y., Yu,H., Li,M.,
            Zhang,G., Zhu,X., Tong,R., Xiao,H., Li,Y. and Yang,B.
  TITLE     MiR-652-3p promotes malignancy and metastasis of cancer cells via
            inhibiting TNRC6A in hepatocellular carcinoma
  JOURNAL   Biochem Biophys Res Commun 640, 1-11 (2023)
   PUBMED   36495604
  REMARK    GeneRIF: MiR-652-3p promotes malignancy and metastasis of cancer
            cells via inhibiting TNRC6A in hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 1922)
  AUTHORS   Eystathioy,T., Jakymiw,A., Chan,E.K., Seraphin,B., Cougot,N. and
            Fritzler,M.J.
  TITLE     The GW182 protein colocalizes with mRNA degradation associated
            proteins hDcp1 and hLSm4 in cytoplasmic GW bodies
  JOURNAL   RNA 9 (10), 1171-1173 (2003)
   PUBMED   13130130
REFERENCE   7  (residues 1 to 1922)
  AUTHORS   Eystathioy,T., Chan,E.K., Mahler,M., Luft,L.M., Fritzler,M.L. and
            Fritzler,M.J.
  TITLE     A panel of monoclonal antibodies to cytoplasmic GW bodies and the
            mRNA binding protein GW182
  JOURNAL   Hybrid Hybridomics 22 (2), 79-86 (2003)
   PUBMED   12831532
REFERENCE   8  (residues 1 to 1922)
  AUTHORS   Eystathioy,T., Chan,E.K., Tenenbaum,S.A., Keene,J.D., Griffith,K.
            and Fritzler,M.J.
  TITLE     A phosphorylated cytoplasmic autoantigen, GW182, associates with a
            unique population of human mRNAs within novel cytoplasmic speckles
  JOURNAL   Mol Biol Cell 13 (4), 1338-1351 (2002)
   PUBMED   11950943
  REMARK    GeneRIF: GW ribonucleoprotein complex is involved in the
            posttranscriptional regulation of gene expression
REFERENCE   9  (residues 1 to 1922)
  AUTHORS   Margolis,R.L., Abraham,M.R., Gatchell,S.B., Li,S.H., Kidwai,A.S.,
            Breschel,T.S., Stine,O.C., Callahan,C., McInnis,M.G. and Ross,C.A.
  TITLE     cDNAs with long CAG trinucleotide repeats from human brain
  JOURNAL   Hum Genet 100 (1), 114-122 (1997)
   PUBMED   9225980
REFERENCE   10 (residues 1 to 1922)
  AUTHORS   Yamagata,K., Takeda,J., Menzel,S., Chen,X., Eng,S., Lim,L.R.,
            Concannon,P., Hanis,C.L., Spielman,R.S., Cox,N.J. and Bell,G.I.
  TITLE     Searching for NIDDM susceptibility genes: studies of genes with
            triplet repeats expressed in skeletal muscle
  JOURNAL   Diabetologia 39 (6), 725-730 (1996)
   PUBMED   8781769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010321.8 and AC008731.8.
            
            Summary: This gene encodes a member of the trinucleotide repeat
            containing 6 protein family. The protein functions in
            post-transcriptional gene silencing through the RNA interference
            (RNAi) and microRNA pathways. The protein associates with messenger
            RNAs and Argonaute proteins in cytoplasmic bodies known as
            GW-bodies or P-bodies. Inhibiting expression of this gene
            delocalizes other GW-body proteins and impairs RNAi and
            microRNA-induced gene silencing. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.156185.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1922
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..1922
                     /product="trinucleotide repeat-containing gene 6A protein
                     isoform 3"
                     /note="CAG repeat protein 26; glycine-tryptophan protein
                     of 182 kDa; trinucleotide repeat-containing gene 6A
                     protein; EDIE; GW182 autoantigen; EMSY interactor protein;
                     CTD-2540M10.1; trinucleotide repeat containing 6A"
                     /calculated_mol_wt=205897
     Region          <414..>702
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          <631..>869
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          1084..1211
                     /region_name="Ago_hook"
                     /note="Argonaute hook; pfam10427"
                     /db_xref="CDD:463088"
     Region          <1289..1441
                     /region_name="M_domain"
                     /note="M domain of GW182; pfam12938"
                     /db_xref="CDD:432890"
     Region          1466..1727
                     /region_name="TNRC6-PABC_bdg"
                     /note="TNRC6-PABC binding domain; pfam16608"
                     /db_xref="CDD:465195"
     Region          1735..1826
                     /region_name="RRM_TNRC6A"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     GW182 autoantigen; cd12711"
                     /db_xref="CDD:410110"
     CDS             1..1922
                     /gene="TNRC6A"
                     /gene_synonym="CAGH26; FAME6; GW1; GW182; TNRC6"
                     /coded_by="NM_001351850.2:327..6095"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:27327"
                     /db_xref="HGNC:HGNC:11969"
                     /db_xref="MIM:610739"
ORIGIN      
        1 mqlvaepgld arcpgsqdip lpeewnrdlv qeeeqlmeek kkkkddkkkk eaaqkkateq
       61 kikvpeqikp svsqpqpans nngtstatst nnnakratan nqqpqqqqqq qqpqqqqpqq
      121 qpqpqpqqqq pqqqpqalpr yprevpprfr hqehkqllkr gqhfpviaan lgsavkvlns
      181 qsessaltnq qpqnngevqn sknqsdinhs tsgshyensq rgpvsstsds stncknavvs
      241 dlsekeawps apgsdpelas ecmdadsass sesernitim asgntggekd glrnstglgs
      301 qnkfvvgsss nnvghgsstg pwgfshgaii stcqvsvdap esksessnnr mnawgtvsss
      361 sngglnpstl nsasnhgawp vlennglalk gpvgsgssgi niqcstigqm pnnqsinskv
      421 sggsthgtwg slqetcesev sgtqkvsfsg qpqnittemt gpnnttnfmt sslpnsgsvq
      481 nnelpssntg awrvstmnhp qmqapsgmng tslshlsnge sksggsygtt wgaygsnysg
      541 dkcsgpngqa ngdtvnatlm qpgvngpmgt nfqvntnkgg gvwesgaans qstswgsgng
      601 ansggsrrgw gtpaqntgtn lpsvewnklp snqhsndsan gngktftngw ksteeedqgs
      661 atsqtneqss vwaktggtve sdgstestgr leekgtgesq srdrrkidqh tllqsivnrt
      721 dldprvlsns gwgqtpikqn tawdtetspr gerktdngte awgssatqtf nsgacidkts
      781 pngndtssvs gwgdpkpalr wgdskgsncq ggweddsaat gmvksnqwgn ckeekaawnd
      841 sqknkqgwgd gqkssqgwsv sasdnwgets rnnhwgeank ksssggsdsd rsvsgwnelg
      901 ktssftwgnn inpnnssgwd esskptpsqg wgdppksnqs lgwgdsskpv sspdwnkqqd
      961 ivgswgippa tgkppgtgwl ggpipapake eeptgweeps pesirrkmei ddgtsawgdp
     1021 skynyknvnm wnknvpngns rsdqqaqvhq lltpasaisn keassgsgwg epwgepstpa
     1081 ttvdngtsaw gkpidsgpsw gepiaaasst stwgsssvgp qalsksgpks mqdgwcgddm
     1141 plpgnrptgw eeeedveigm wnsnssqeln sslnwppytk kmsskglsgk krrrergmmk
     1201 ggnkqeeawi npfvkqfsni sfsrdspeen vqsnkmdlsg gmlqdkrmei dkhslnigdy
     1261 nrtvgkgpgs rpqiskessm ernpyfdkng npsmfgvgnt aaqprgmqqp paqplsssqp
     1321 nlraqvpppl lspqvpvsll kyapnnggln plfgpqqvam lnqlsqlnql sqisqlqrll
     1381 aqqqraqsqr svpsgnrpqq dqqgrplsvq qqmmqqsrql dpnllvkqqt ppsqqqplhq
     1441 pamksfldnv mphttpelqk gpspinafsn fpiglnsnln vnmdmnsike pqsrlrkwtt
     1501 vdsisvntsl dqnsskhgai ssgfrleesp fvpydfmnss tspasppgsi gdgwpraksp
     1561 ngsssvnwpp efrpgepwkg ypnidpetdp yvtpgsvinn lsintvrevd hlrdrnsgss
     1621 sslnttlpst sawssirasn ynvplsstaq stsarnsdsk ltwspgsvtn tslahelwkv
     1681 plppknitap srpppgltgq kpplstwdns plrigggwgn sdarytpgss wgesssgrit
     1741 nwlvlknltp qidgstlrtl cmqhgplitf hlnlphgnal vrysskeevv kaqkslhmcv
     1801 lgnttilaef aseeeisrff aqsqsltpsp gwqslgssqs rlgsldcshs fssrtdlnhw
     1861 ngaglsgtnc gdlhgtslwg tphystslwg ppsssdprgi sspspinafl svdhlgggge
     1921 sm
//
LOCUS       NP_001340529             433 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform j [Homo sapiens].
ACCESSION   NP_001340529
VERSION     NP_001340529.1
DBSOURCE    REFSEQ: accession NM_001353600.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 433)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 433)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 433)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 433)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 433)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 433)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 433)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 433)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (15), as well as variants 14 and
            16, encodes isoform j.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.96670.1,
                                           SRR1803614.10146.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..433
                     /product="lysosomal cobalamin transporter ABCD4 isoform j"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=48425
     Region          <32..425
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..433
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353600.2:372..1673"
                     /note="isoform j is encoded by transcript variant 15"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 maskliispf tlvyytyqcf qstgwlgpvs ifgyfilgtv vnktlmgpiv mklvhqekle
       61 gdfrfkhmqi rvnaepaafy raghvehmrt drrlqrllqt qrelmskelw lyigintfdy
      121 lgsilsyvvi aipifsgvyg dlspaelstl vsknafvciy liscftqlid lsttlsdvag
      181 ythrigqlre tlldmslksq dceilgesew gldtppgwpa aepadtafll ervsisapss
      241 dkplikdlsl kisegqslli tgntgtgkts llrvlgglwt strgsvqmlt dfgphgvlfl
      301 pqkpfftdgt lreqviyplk evypdsgsad derilrflel aglsnlvart egldqqvdwn
      361 wydvlspgem qrlsfarlfy lqpkyavlde atsalteeve selyrigqql gmtfisvghr
      421 qslekvpvlt rma
//
LOCUS       NP_647601                409 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 10 [Homo sapiens].
ACCESSION   NP_647601
VERSION     NP_647601.1
DBSOURCE    REFSEQ: accession NM_139351.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF594020.1, AF068915.1,
            AF070576.1 and BM711160.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (10) lacks six in-frame exons in
            the coding region, compared to variant 1. Isoform 10, also called
            BIN1-10-13, is shorter than isoform 1 and is ubiquitously
            expressed.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF068915.1, SRR11853562.19632.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..409
                     /product="myc box-dependent-interacting protein 1 isoform
                     10"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=45432
     Region          31..241
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,197,200..201,203,208..209,211..212,215..216,
                     218..219,222..223,225..226,230,233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          337..408
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(348..354,373,375..378,401,403..404)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..409
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_139351.3:212..1441"
                     /note="isoform 10 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS2143.1"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakaeeelik
      181 aqkvfeemnv dlqeelpslw nsrvgfyvnt fqsiagleen fhkemsklnq nlndvlvgle
      241 kqhgsntftv kaqpsdnapa kgnkspsppd gspaatpeir vnhepepagg atpgatlpks
      301 psqsslpavv vetfpatvng tveggsgagr ldlppgfmfk vqaqhdytat dtdelqlkag
      361 dvvlvipfqn peeqdegwlm gvkesdwnqh kelekcrgvf penftervp
//
LOCUS       NP_001354662             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354662
VERSION     NP_001354662.1
DBSOURCE    REFSEQ: accession NM_001367733.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (17), as well as variants 3, 4,
            9-16, and 18-20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.177488.1,
                                           SRR1660807.106467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367733.1:192..1667"
                     /note="isoform c is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001193994              89 aa            linear   PRI 20-NOV-2025
DEFINITION  coxsackievirus and adenovirus receptor isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001193994
VERSION     NP_001193994.1
DBSOURCE    REFSEQ: accession NM_001207065.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 89)
  AUTHORS   Tan,H.J., Deng,Z.H., Zhang,C., Deng,H.W. and Xiao,H.M.
  TITLE     CXADR promote epithelial-mesenchymal transition in endometriosis by
            modulating AKT/GSK-3beta signaling
  JOURNAL   Cell Cycle 22 (21-22), 2436-2448 (2023)
   PUBMED   38146657
  REMARK    GeneRIF: CXADR promote epithelial-mesenchymal transition in
            endometriosis by modulating AKT/GSK-3beta signaling.
REFERENCE   2  (residues 1 to 89)
  AUTHORS   Oliviero,F., Klement,W., Mary,L., Dauwe,Y., Lippi,Y., Naylies,C.,
            Gayrard,V., Marchi,N. and Mselli-Lakhal,L.
  TITLE     CAR Protects Females from Diet-Induced Steatosis and Associated
            Metabolic Disorders
  JOURNAL   Cells 12 (18), 2218 (2023)
   PUBMED   37759441
  REMARK    GeneRIF: CAR Protects Females from Diet-Induced Steatosis and
            Associated Metabolic Disorders.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 89)
  AUTHORS   Nilchian,A., Plant,E., Parniewska,M.M., Santiago,A., Rossignoli,A.,
            Skogsberg,J., Hedin,U., Matic,L. and Fuxe,J.
  TITLE     Induction of the Coxsackievirus and Adenovirus Receptor in
            Macrophages During the Formation of Atherosclerotic Plaques
  JOURNAL   J Infect Dis 222 (12), 2041-2051 (2020)
   PUBMED   32852032
  REMARK    GeneRIF: Induction of the Coxsackievirus and Adenovirus Receptor in
            Macrophages During the Formation of Atherosclerotic Plaques.
REFERENCE   4  (residues 1 to 89)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 89)
  AUTHORS   Herrmann,L., Filip,A., Lapuente,D., Tenbusch,M., Niehaus,K.,
            Rudolph,V. and Farr,M.
  TITLE     Naturally occurring variants in the transmembrane and cytoplasmic
            domains of the human Coxsackie- and adenovirus receptor have no
            impact on virus internalisation
  JOURNAL   Biochem Biophys Res Commun 527 (2), 401-405 (2020)
   PUBMED   32334832
  REMARK    GeneRIF: Naturally occurring variants in the transmembrane and
            cytoplasmic domains of the human Coxsackie- and adenovirus receptor
            have no impact on virus internalisation.
REFERENCE   6  (residues 1 to 89)
  AUTHORS   Fechner,H., Haack,A., Wang,H., Wang,X., Eizema,K., Pauschinger,M.,
            Schoemaker,R., Veghel,R., Houtsmuller,A., Schultheiss,H.P.,
            Lamers,J. and Poller,W.
  TITLE     Expression of coxsackie adenovirus receptor and alphav-integrin
            does not correlate with adenovector targeting in vivo indicating
            anatomical vector barriers
  JOURNAL   Gene Ther 6 (9), 1520-1535 (1999)
   PUBMED   10490761
REFERENCE   7  (residues 1 to 89)
  AUTHORS   Bergelson,J.M., Krithivas,A., Celi,L., Droguett,G., Horwitz,M.S.,
            Wickham,T., Crowell,R.L. and Finberg,R.W.
  TITLE     The murine CAR homolog is a receptor for coxsackie B viruses and
            adenoviruses
  JOURNAL   J Virol 72 (1), 415-419 (1998)
   PUBMED   9420240
REFERENCE   8  (residues 1 to 89)
  AUTHORS   Carson,S.D., Chapman,N.N. and Tracy,S.M.
  TITLE     Purification of the putative coxsackievirus B receptor from HeLa
            cells
  JOURNAL   Biochem Biophys Res Commun 233 (2), 325-328 (1997)
   PUBMED   9144533
REFERENCE   9  (residues 1 to 89)
  AUTHORS   Tomko,R.P., Xu,R. and Philipson,L.
  TITLE     HCAR and MCAR: the human and mouse cellular receptors for subgroup
            C adenoviruses and group B coxsackieviruses
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3352-3356 (1997)
   PUBMED   9096397
REFERENCE   10 (residues 1 to 89)
  AUTHORS   Bergelson,J.M., Cunningham,J.A., Droguett,G., Kurt-Jones,E.A.,
            Krithivas,A., Hong,J.S., Horwitz,M.S., Crowell,R.L. and
            Finberg,R.W.
  TITLE     Isolation of a common receptor for Coxsackie B viruses and
            adenoviruses 2 and 5
  JOURNAL   Science 275 (5304), 1320-1323 (1997)
   PUBMED   9036860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CV570985.1, AY072910.1 and
            AP000967.2.
            
            Summary: The protein encoded by this gene is a type I membrane
            receptor for group B coxsackieviruses and subgroup C adenoviruses.
            Several transcript variants encoding different isoforms have been
            found for this gene. Pseudogenes of this gene are found on
            chromosomes 15, 18, and 21. [provided by RefSeq, May 2011].
            
            Transcript Variant: This variant (4, alternatively referred to as
            delta or CAR2/7) lacks four consecutive alternate coding exons
            compared to variant 1, that causes a frameshift. The resulting
            isoform (4) has a shorter and distinct C-terminus compared to
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY072910.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163623 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..89
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.1"
     Protein         1..89
                     /product="coxsackievirus and adenovirus receptor isoform 4
                     precursor"
                     /note="46 kD coxsackievirus and adenovirus receptor (CAR)
                     protein; HCVADR; CVB3-binding protein; coxsackievirus
                     B-adenovirus receptor; coxsackie virus and adenovirus
                     receptor; CXADR Ig-like cell adhesion molecule"
                     /calculated_mol_wt=7914
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2071
     mat_peptide     20..89
                     /product="coxsackievirus and adenovirus receptor isoform
                     4"
                     /calculated_mol_wt=7914
     Region          20..>70
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          54..58
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..89
                     /gene="CXADR"
                     /gene_synonym="CAR; CAR4/6; HCAR"
                     /coded_by="NM_001207065.2:88..357"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS56207.1"
                     /db_xref="GeneID:1525"
                     /db_xref="HGNC:HGNC:2559"
                     /db_xref="MIM:602621"
ORIGIN      
        1 malllcfvll cgvvdfarsl sittpeemie kakgetaylp ckftlspedq gpldiewlis
       61 padnqkvdqv grcatskepy vhcqklhrq
//
LOCUS       NP_001230215             366 aa            linear   PRI 20-NOV-2025
DEFINITION  nectin-3 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001230215
VERSION     NP_001230215.1
DBSOURCE    REFSEQ: accession NM_001243286.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Lachke,S.A., Higgins,A.W., Inagaki,M., Saadi,I., Xi,Q., Long,M.,
            Quade,B.J., Talkowski,M.E., Gusella,J.F., Fujimoto,A.,
            Robinson,M.L., Yang,Y., Duong,Q.T., Shapira,I., Motro,B.,
            Miyoshi,J., Takai,Y., Morton,C.C. and Maas,R.L.
  TITLE     The cell adhesion gene PVRL3 is associated with congenital ocular
            defects
  JOURNAL   Hum Genet 131 (2), 235-250 (2012)
   PUBMED   21769484
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Reymond,N., Fabre,S., Lecocq,E., Adelaide,J., Dubreuil,P. and
            Lopez,M.
  TITLE     Nectin4/PRR4, a new afadin-associated member of the nectin family
            that trans-interacts with nectin1/PRR1 through V domain interaction
  JOURNAL   J Biol Chem 276 (46), 43205-43215 (2001)
   PUBMED   11544254
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Reymond,N., Borg,J.P., Lecocq,E., Adelaide,J., Campadelli-Fiume,G.,
            Dubreuil,P. and Lopez,M.
  TITLE     Human nectin3/PRR3: a novel member of the PVR/PRR/nectin family
            that interacts with afadin
  JOURNAL   Gene 255 (2), 347-355 (2000)
   PUBMED   11024295
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Satoh-Horikawa,K., Nakanishi,H., Takahashi,K., Miyahara,M.,
            Nishimura,M., Tachibana,K., Mizoguchi,A. and Takai,Y.
  TITLE     Nectin-3, a new member of immunoglobulin-like cell adhesion
            molecules that shows homophilic and heterophilic cell-cell adhesion
            activities
  JOURNAL   J Biol Chem 275 (14), 10291-10299 (2000)
   PUBMED   10744716
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Takahashi,K., Nakanishi,H., Miyahara,M., Mandai,K., Satoh,K.,
            Satoh,A., Nishioka,H., Aoki,J., Nomoto,A., Mizoguchi,A. and
            Takai,Y.
  TITLE     Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited
            to cadherin-based adherens junctions through interaction with
            Afadin, a PDZ domain-containing protein
  JOURNAL   J Cell Biol 145 (3), 539-549 (1999)
   PUBMED   10225955
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Lopez,M., Aoubala,M., Jordier,F., Isnardon,D., Gomez,S. and
            Dubreuil,P.
  TITLE     The human poliovirus receptor related 2 protein is a new
            hematopoietic/endothelial homophilic adhesion molecule
  JOURNAL   Blood 92 (12), 4602-4611 (1998)
   PUBMED   9845526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI464010.1, BC067808.1,
            AC133477.2, AC137833.3 and AA555086.1.
            
            Summary: This gene encodes a member of the nectin family of
            proteins, which function as adhesion molecules at adherens
            junctions. This family member interacts with other nectin-like
            proteins and with afadin, a filamentous actin-binding protein
            involved in the regulation of directional motility, cell
            proliferation and survival. This gene plays a role in ocular
            development involving the ciliary body. Mutations in this gene are
            believed to result in congenital ocular defects. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            that results in a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (2) has a distinct and shorter
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.137772.1, BC067808.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13"
     Protein         1..366
                     /product="nectin-3 isoform 2 precursor"
                     /note="nectin 3; poliovirus receptor-related protein 3;
                     poliovirus receptor-related 3"
                     /calculated_mol_wt=33890
     sig_peptide     1..57
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
                     /calculated_mol_wt=5820
     Region          58..167
                     /region_name="IgV_1_Nectin-3_like"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-3 (also known as poliovirus receptor related
                     protein 3), and similar domains; cd05887"
                     /db_xref="CDD:409470"
     Region          58..81
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409470"
     Region          58..62
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409470"
     Region          64..68
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409470"
     Site            order(72..79,86..94,101..113,131..137,142..156,159..167)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409470"
     Region          73..81
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409470"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          82..86
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409470"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          87..93
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          88..93
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409470"
     Region          94..113
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409470"
     Region          103..108
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          110..114
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409470"
     Region          114..152
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          121..125
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409470"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          130..137
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409470"
     Region          144..152
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409470"
     Region          153..156
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409470"
     Region          156..166
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409470"
     Region          157..167
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409470"
     Region          170..265
                     /region_name="IgC1_2_Nectin-3-4_like"
                     /note="Second immunoglobulin (Ig) domain of nectin-3 and
                     nectin-4 (poliovirus receptor related protein 4), and
                     similar domains; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd07704"
                     /db_xref="CDD:409501"
     Region          170..176
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409501"
     Site            186
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          189..196
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409501"
     Region          201..207
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409501"
     Region          209..211
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409501"
     Region          213..220
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409501"
     Site            222
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          225..233
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409501"
     Region          243..250
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409501"
     Region          256..262
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409501"
     Region          269..355
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          287..291
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          301..305
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          320..325
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:22902367; propagated from
                     UniProtKB/Swiss-Prot (Q9NQS3.1)"
     Region          335..340
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          350..353
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..366
                     /gene="NECTIN3"
                     /gene_synonym="CD113; CDW113; NECTIN-3; PPR3; PRR3; PVRL3;
                     PVRR3"
                     /coded_by="NM_001243286.2:203..1303"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS58842.1"
                     /db_xref="GeneID:25945"
                     /db_xref="HGNC:HGNC:17664"
                     /db_xref="MIM:607147"
ORIGIN      
        1 martlrpspl cpgggkaqls sasllgagll lqpptpppll lllfplllfs rlcgalagpi
       61 ivephvtavw gknvslkcli evnetitqis wekihgkssq tvavhhpqyg fsvqgeyqgr
      121 vlfknyslnd atitlhnigf sdsgkyicka vtfplgnaqs sttvtvlvep tvslikgpds
      181 lidggnetva aiciaatgkp vahidwegdl gemestttsf pnetatiisq yklfptrfar
      241 grritcvvkh palekdirys fildiqyape vsvtgydgnw fvgrkgvnlk cnadanpppf
      301 ksvwsrldgq wpdgllasdn tlhfvhpltf nysgvyickv tnslgqrsdq kviyisayns
      361 vaslnc
//
LOCUS       NP_001317702             868 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001317702
VERSION     NP_001317702.1
DBSOURCE    REFSEQ: accession NM_001330773.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 868)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 868)
  AUTHORS   Ito,H. and Nagata,K.I.
  TITLE     Functions of CNKSR2 and Its Association with Neurodevelopmental
            Disorders
  JOURNAL   Cells 11 (2), 303 (2022)
   PUBMED   35053419
  REMARK    GeneRIF: Functions of CNKSR2 and Its Association with
            Neurodevelopmental Disorders.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 868)
  AUTHORS   Toraman,B., Bilginer,S.C., Hesapcioglu,S.T., Goker,Z., Soykam,H.O.,
            Erguner,B., Dincer,T., Yildiz,G., Unsal,S., Kasap,B.K., Kandil,S.
            and Kalay,E.
  TITLE     Finding underlying genetic mechanisms of two patients with autism
            spectrum disorder carrying familial apparently balanced chromosomal
            translocations
  JOURNAL   J Gene Med 23 (4), e3322 (2021)
   PUBMED   33591602
  REMARK    GeneRIF: Finding underlying genetic mechanisms of two patients with
            autism spectrum disorder carrying familial apparently balanced
            chromosomal translocations.
REFERENCE   4  (residues 1 to 868)
  AUTHORS   Zhang,Y., Yu,T., Li,N., Wang,J., Wang,J., Ge,Y. and Yao,R.
  TITLE     Psychomotor development and attention problems caused by a splicing
            variant of CNKSR2
  JOURNAL   BMC Med Genomics 13 (1), 182 (2020)
   PUBMED   33298018
  REMARK    GeneRIF: Psychomotor development and attention problems caused by a
            splicing variant of CNKSR2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 868)
  AUTHORS   Daoqi,M., Guohong,C., Yuan,W., Zhixiao,Y., Kaili,X. and Shiyue,M.
  TITLE     Exons deletion of CNKSR2 gene identified in X-linked syndromic
            intellectual disability
  JOURNAL   BMC Med Genet 21 (1), 69 (2020)
   PUBMED   32245427
  REMARK    GeneRIF: This study enhances our knowledge of the CNKSR2 gene
            mutation spectrum and provides further information about the
            phenotypic characteristics of X-linked syndromic intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 868)
  AUTHORS   Wang,X., Patel,R. and Studzinski,G.P.
  TITLE     hKSR-2, a vitamin D-regulated gene, inhibits apoptosis in
            arabinocytosine-treated HL60 leukemia cells
  JOURNAL   Mol Cancer Ther 7 (9), 2798-2806 (2008)
   PUBMED   18790760
REFERENCE   7  (residues 1 to 868)
  AUTHORS   Rajakulendran,T., Sahmi,M., Kurinov,I., Tyers,M., Therrien,M. and
            Sicheri,F.
  TITLE     CNK and HYP form a discrete dimer by their SAM domains to mediate
            RAF kinase signaling
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 2836-2841 (2008)
   PUBMED   18287031
  REMARK    GeneRIF: CNK and HYP form a discrete dimer by their SAM domains to
            mediate RAF kinase signaling.
REFERENCE   8  (residues 1 to 868)
  AUTHORS   Bumeister,R., Rosse,C., Anselmo,A., Camonis,J. and White,M.A.
  TITLE     CNK2 couples NGF signal propagation to multiple regulatory cascades
            driving cell differentiation
  JOURNAL   Curr Biol 14 (5), 439-445 (2004)
   PUBMED   15028221
REFERENCE   9  (residues 1 to 868)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
  REMARK    GeneRIF: CNK2 through interaction with Raf and Rlf may function as
            a regulator of Ras signaling.
REFERENCE   10 (residues 1 to 868)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807781.6, AL928874.3 and
            AL772392.4.
            
            Summary: This gene encodes a multidomain protein that functions as
            a scaffold protein to mediate the mitogen-activated protein kinase
            pathways downstream from Ras. This gene product is induced by
            vitamin D and inhibits apoptosis in certain cancer cells. It may
            also play a role in ternary complex assembly of synaptic proteins
            at the postsynaptic membrane and coupling of signal transduction to
            membrane/cytoskeletal remodeling. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.132045.1,
                                           SRR1660805.9253.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..868
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..868
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 8"
                     /note="connector enhancer of KSR2; membrane-associated
                     guanylate kinase-interacting protein; CNK homolog protein
                     2"
                     /calculated_mol_wt=98123
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          339..>457
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Region          529..642
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     CDS             1..868
                     /gene="CNKSR2"
                     /gene_synonym="CNK2; KSR2; MAGUIN; MRXSHG"
                     /coded_by="NM_001330773.2:481..3087"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS87728.1"
                     /db_xref="GeneID:22866"
                     /db_xref="HGNC:HGNC:19701"
                     /db_xref="MIM:300724"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv vgwqlknlvn alredpsgvi ltlkkrpqsm
      301 ltsapallkn mrwkplalqp liprsptssv atpsstistp tkrdssalqd lyippppaep
      361 yiprdekgnl pcedlrghmv gkpvhkgses pnsfldqeyr krfniveedt vlycyeyekg
      421 rsssqgrres tptyensllr ymsnekiaqe eymfqrnskk dtgkkskkkg dksnspthys
      481 llpslqmdal rqdimgtpvp ettlyhtfqq sslqhkskkk nkgpiagksk rrisckdlgr
      541 gdcegwlwkk kdaksyfsqk wkkywfvlkd aslywyinee dekaegfisl pefkidrase
      601 crkkyafkac hpkiksfyfa aehlddmnrw lnrinmltag yaererikqe qdywsesdke
      661 eadtpstpkq dsppppydty prppsmscas pyveakhsrl sstetsqsqs sheefrqevt
      721 gssavspirk tasqrrswqd lietpltssg lhylqtlple dsvfsdsaai spehrrqstl
      781 ptqkchlqdh ygpyplaese rmqvlngngg kprsftlprd sgfnhcclna pvsacdpqdd
      841 vqppeveeee eeeeeegeaa genigeks
//
LOCUS       NP_808228                255 aa            linear   PRI 20-NOV-2025
DEFINITION  casein kinase II subunit alpha isoform b [Homo sapiens].
ACCESSION   NP_808228
VERSION     NP_808228.1
DBSOURCE    REFSEQ: accession NM_177560.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Goel,H. and O'Donnell,S.
  TITLE     Inherited loss of function variant in CSNK2A1: the oldest reported
            cases of Okur-Chung syndrome in a single family
  JOURNAL   Clin Dysmorphol 33 (3), 121-124 (2024)
   PUBMED   38818820
  REMARK    GeneRIF: Inherited loss of function variant in CSNK2A1: the oldest
            reported cases of Okur-Chung syndrome in a single family.
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Ampofo,E., Pack,M., Wrublewsky,S., Boewe,A.S., Spigelman,A.F.,
            Koch,H., MacDonald,P.E., Laschke,M.W., Montenarh,M. and Gotz,C.
  TITLE     CK2 activity is crucial for proper glucagon expression
  JOURNAL   Diabetologia 67 (7), 1368-1385 (2024)
   PUBMED   38503901
  REMARK    GeneRIF: CK2 activity is crucial for proper glucagon expression.
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Liu,Z.D., Shi,Y.H., Xu,Q.C., Zhao,G.Y., Zhu,Y.Q., Li,F.X., Ma,M.J.,
            Ye,J.Y., Huang,X.T., Wang,X.Y., Xu,X., Wang,J.Q., Zhao,W. and
            Yin,X.Y.
  TITLE     CSNK2A1 confers gemcitabine resistance to pancreatic ductal
            adenocarcinoma via inducing autophagy
  JOURNAL   Cancer Lett 585, 216640 (2024)
   PUBMED   38290659
  REMARK    GeneRIF: CSNK2A1 confers gemcitabine resistance to pancreatic
            ductal adenocarcinoma via inducing autophagy.
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Nan,H., Chu,M., Zhang,J., Jiang,D., Wang,Y. and Wu,L.
  TITLE     Okur-Chung neurodevelopmental syndrome: Implications for phenotype
            and genotype expansion
  JOURNAL   Mol Genet Genomic Med 12 (3), e2398 (2024)
   PUBMED   38444259
  REMARK    GeneRIF: Okur-Chung neurodevelopmental syndrome: Implications for
            phenotype and genotype expansion.
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Chung,W. and Okur,V.
  TITLE     Okur-Chung Neurodevelopmental Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35679446
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Russo,G.L., Vandenberg,M.T., Yu,I.J., Bae,Y.S., Franza,B.R. Jr. and
            Marshak,D.R.
  TITLE     Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the
            HeLa cell division cycle
  JOURNAL   J Biol Chem 267 (28), 20317-20325 (1992)
   PUBMED   1400350
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Lin,A., Frost,J., Deng,T., Smeal,T., al-Alawi,N., Kikkawa,U.,
            Hunter,T., Brenner,D. and Karin,M.
  TITLE     Casein kinase II is a negative regulator of c-Jun DNA binding and
            AP-1 activity
  JOURNAL   Cell 70 (5), 777-789 (1992)
   PUBMED   1516134
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1423636]
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Sacks,D.B., Davis,H.W., Crimmins,D.L. and McDonald,J.M.
  TITLE     Insulin-stimulated phosphorylation of calmodulin
  JOURNAL   Biochem J 286 (Pt 1) (Pt 1), 211-216 (1992)
   PUBMED   1520270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132198.1, AY735339.1,
            M55265.1, BC053532.1 and AL049761.11.
            
            Summary: Casein kinase II is a serine/threonine protein kinase that
            phosphorylates acidic proteins such as casein. It is involved in
            various cellular processes, including cell cycle control,
            apoptosis, and circadian rhythm. The kinase exists as a tetramer
            and is composed of an alpha, an alpha-prime, and two beta subunits.
            The alpha subunits contain the catalytic activity while the beta
            subunits undergo autophosphorylation. The protein encoded by this
            gene represents the alpha subunit. Multiple transcript variants
            encoding different protein isoforms have been found for this gene.
            [provided by RefSeq, Apr 2018].
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            5' UTR as well as the first coding exon compared to variant 1,
            resulting in an isoform (b) which is shorter at the N-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.196518.1,
                                           SRR1660805.133194.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..255
                     /product="casein kinase II subunit alpha isoform b"
                     /EC_number="2.7.11.1"
                     /note="CK2 catalytic subunit alpha; protein kinase CK2;
                     casein kinase II alpha 1 subunit; casein kinase II alpha 1
                     polypeptide pseudogene; casein kinase 2, alpha 1
                     polypeptide"
                     /calculated_mol_wt=29050
     Region          <1..189
                     /region_name="STKc_CK2_alpha"
                     /note="Catalytic subunit (alpha) of the Serine/Threonine
                     Kinase, Casein Kinase 2; cd14132"
                     /db_xref="CDD:271034"
     Site            order(20,22,42,53,55..58,60,99)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(38..48,53..60)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271034"
     CDS             1..255
                     /gene="CSNK2A1"
                     /gene_synonym="CK2A1; Cka1; Cka2; CKII; OCNDS"
                     /coded_by="NM_177560.3:427..1194"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13004.1"
                     /db_xref="GeneID:1457"
                     /db_xref="HGNC:HGNC:2457"
                     /db_xref="MIM:115440"
ORIGIN      
        1 myeilkaldy chsmgimhrd vkphnvmidh ehrklrlidw glaefyhpgq eynvrvasry
       61 fkgpellvdy qmydysldmw slgcmlasmi frkepffhgh dnydqlvria kvlgtedlyd
      121 yidkynield prfndilgrh srkrwerfvh senqhlvspe aldfldkllr ydhqsrltar
      181 eamehpyfyt vvkdqarmgs ssmpggstpv ssanmmsgis svptpsplgp lagspviaaa
      241 nplgmpvpaa agaqq
//
LOCUS       NP_003178                264 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription initiation factor TFIID subunit 9 [Homo sapiens].
ACCESSION   NP_003178
VERSION     NP_003178.1
DBSOURCE    REFSEQ: accession NM_003187.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Hsieh,A.H., Kuo,C.F., Chou,I.J., Tseng,W.Y., Chen,Y.F., Yu,K.H. and
            Luo,S.F.
  TITLE     Human cytomegalovirus pp65 peptide-induced autoantibodies
            cross-reacts with TAF9 protein and induces lupus-like autoimmunity
            in BALB/c mice
  JOURNAL   Sci Rep 10 (1), 9662 (2020)
   PUBMED   32541894
  REMARK    GeneRIF: Human cytomegalovirus pp65 peptide-induced autoantibodies
            cross-reacts with TAF9 protein and induces lupus-like autoimmunity
            in BALB/c mice.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Zeng,P., Wang,Y., Zheng,Y., Song,X. and Yin,Y.
  TITLE     Cancer-testis antigen HCA587/MAGEC2 interacts with the general
            transcription coactivator TAF9 in cancer cells
  JOURNAL   Mol Med Rep 17 (2), 3226-3231 (2018)
   PUBMED   29257297
  REMARK    GeneRIF: TAF9 directly binds HCA587/MAGEC2 through its CR domain,
            suggesting that HCA587/MAGEC2 may involve in TAF9 binding with DNA
            to regulate certain genes transcription.
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Hisatake,K., Ohta,T., Takada,R., Guermah,M., Horikoshi,M.,
            Nakatani,Y. and Roeder,R.G.
  TITLE     Evolutionary conservation of human
            TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and
            interactions of TAFII80 with other TAFs and with general
            transcription factors
  JOURNAL   Proc Natl Acad Sci U S A 92 (18), 8195-8199 (1995)
   PUBMED   7667268
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Klemm,R.D., Goodrich,J.A., Zhou,S. and Tjian,R.
  TITLE     Molecular cloning and expression of the 32-kDa subunit of human
            TFIID reveals interactions with VP16 and TFIIB that mediate
            transcriptional activation
  JOURNAL   Proc Natl Acad Sci U S A 92 (13), 5788-5792 (1995)
   PUBMED   7597030
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Lu,H. and Levine,A.J.
  TITLE     Human TAFII31 protein is a transcriptional coactivator of the p53
            protein
  JOURNAL   Proc Natl Acad Sci U S A 92 (11), 5154-5158 (1995)
   PUBMED   7761466
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG490028.1, BG720149.1, BC003400.1 and AC145132.2.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes one of the smaller
            subunits of TFIID that binds to the basal transcription factor
            GTF2B as well as to several transcriptional activators such as p53
            and VP16. In human, TAF9 and AK6 (GeneID: 102157402) are two
            distinct genes that share 5' exons. A similar but distinct gene
            (TAF9L) has been found on the X chromosome and a pseudogene has
            been identified on chromosome 19. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 4. Both variants 4 and 1 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.140457.1,
                                           SRR5189658.144879.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217893.10/ ENSP00000217893.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..264
                     /product="transcription initiation factor TFIID subunit 9"
                     /EC_number="2.7.4.3"
                     /note="transcription initiation factor TFIID 31 kD
                     subunit; RNA polymerase II TBP-associated factor subunit
                     G; transcription initiation factor TFIID 31 kDa subunit;
                     transcription initiation factor TFIID 32 kDa subunit; TAF9
                     RNA polymerase II, TATA box binding protein
                     (TBP)-associated factor, 32kDa"
                     /calculated_mol_wt=28843
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Region          9..130
                     /region_name="TFIID-31kDa"
                     /note="Transcription initiation factor IID, 31kD subunit;
                     pfam02291"
                     /db_xref="CDD:460525"
     Region          149..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16594.1)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16594.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VI33; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16594.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16594.1)"
     Region          232..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16594.1)"
     CDS             1..264
                     /gene="TAF9"
                     /gene_synonym="MGC:5067; STAF31/32; TAF2G; TAFII-31;
                     TAFII-32; TAFII31; TAFII32; TAFIID32"
                     /coded_by="NM_003187.5:169..963"
                     /db_xref="CCDS:CCDS4002.1"
                     /db_xref="GeneID:6880"
                     /db_xref="HGNC:HGNC:11542"
                     /db_xref="MIM:600822"
ORIGIN      
        1 mesgktaspk smpkdaqmma qilkdmgite yeprvinqml efafryvtti lddakiyssh
       61 akkatvdadd vrlaiqcrad qsftsppprd flldiarqrn qtplplikpy sgprlppdry
      121 cltapnyrlk slqkkastsa gritvprlsv gsvtsrpstp tlgtptpqtm svstkvgtpm
      181 sltgqrftvq mptsqspavk asipatsavq nvlinpslig sknilittnm mssqntanes
      241 snalkrkred dddddddddd ydnl
//
LOCUS       NP_000443                348 aa            linear   PRI 20-NOV-2025
DEFINITION  ileal sodium/bile acid cotransporter [Homo sapiens].
ACCESSION   NP_000443
VERSION     NP_000443.2
DBSOURCE    REFSEQ: accession NM_000452.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Meadows,V., Marakovits,C., Ekser,B., Kundu,D., Zhou,T., Kyritsi,K.,
            Pham,L., Chen,L., Kennedy,L., Ceci,L., Wu,N., Carpino,G., Zhang,W.,
            Isidan,A., Meyer,A., Owen,T., Gaudio,E., Onori,P., Alpini,G. and
            Francis,H.
  TITLE     Loss of apical sodium bile acid transporter alters bile acid
            circulation and reduces biliary damage in cholangitis
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 324 (1), G60-G77 (2023)
   PUBMED   36410025
  REMARK    GeneRIF: Loss of apical sodium bile acid transporter alters bile
            acid circulation and reduces biliary damage in cholangitis.
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Ontsouka,E., Epstein,A., Kallol,S., Zaugg,J., Baumann,M.,
            Schneider,H. and Albrecht,C.
  TITLE     Placental Expression of Bile Acid Transporters in Intrahepatic
            Cholestasis of Pregnancy
  JOURNAL   Int J Mol Sci 22 (19), 10434 (2021)
   PUBMED   34638773
  REMARK    GeneRIF: Placental Expression of Bile Acid Transporters in
            Intrahepatic Cholestasis of Pregnancy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Zhu,Q., Komori,H., Imamura,R. and Tamai,I.
  TITLE     A Novel Fluorescence-Based Method to Evaluate Ileal Apical
            Sodium-Dependent Bile Acid Transporter ASBT
  JOURNAL   J Pharm Sci 110 (3), 1392-1400 (2021)
   PUBMED   33278408
  REMARK    GeneRIF: A Novel Fluorescence-Based Method to Evaluate Ileal Apical
            Sodium-Dependent Bile Acid Transporter ASBT.
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Shneider,B.L.
  TITLE     Intestinal bile acid transport: biology, physiology, and
            pathophysiology
  JOURNAL   J Pediatr Gastroenterol Nutr 32 (4), 407-417 (2001)
   PUBMED   11396803
  REMARK    Review article
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Craddock,A.L., Love,M.W., Daniel,R.W., Kirby,L.C., Walters,H.C.,
            Wong,M.H. and Dawson,P.A.
  TITLE     Expression and transport properties of the human ileal and renal
            sodium-dependent bile acid transporter
  JOURNAL   Am J Physiol 274 (1), G157-G169 (1998)
   PUBMED   9458785
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Oelkers,P., Kirby,L.C., Heubi,J.E. and Dawson,P.A.
  TITLE     Primary bile acid malabsorption caused by mutations in the ileal
            sodium-dependent bile acid transporter gene (SLC10A2)
  JOURNAL   J Clin Invest 99 (8), 1880-1887 (1997)
   PUBMED   9109432
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Wong,M.H., Rao,P.N., Pettenati,M.J. and Dawson,P.A.
  TITLE     Localization of the ileal sodium-bile acid cotransporter gene
            (SLC10A2) to human chromosome 13q33
  JOURNAL   Genomics 33 (3), 538-540 (1996)
   PUBMED   8661017
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Wong,M.H., Oelkers,P. and Dawson,P.A.
  TITLE     Identification of a mutation in the ileal sodium-dependent bile
            acid transporter gene that abolishes transport activity
  JOURNAL   J Biol Chem 270 (45), 27228-27234 (1995)
   PUBMED   7592981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161771.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 17, 2019 this sequence version replaced NP_000443.1.
            
            Summary: This gene encodes a sodium/bile acid cotransporter. This
            transporter is the primary mechanism for uptake of intestinal bile
            acids by apical cells in the distal ileum. Bile acids are the
            catabolic product of cholesterol metabolism, so this protein is
            also critical for cholesterol homeostasis. Mutations in this gene
            cause primary bile acid malabsorption (PBAM); muatations in this
            gene may also be associated with other diseases of the liver and
            intestines, such as familial hypertriglyceridemia (FHTG). [provided
            by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U10417.1, BC130523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267780 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245312.5/ ENSP00000245312.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.1"
     Protein         1..348
                     /product="ileal sodium/bile acid cotransporter"
                     /note="ileal apical sodium-dependent bile acid
                     transporter; ileal sodium-dependent bile acid transporter;
                     Na(+)-dependent ileal bile acid transporter;
                     sodium/taurocholate cotransporting polypeptide, ileal;
                     solute carrier family 10 (sodium/bile acid cotransporter
                     family), member 2; solute carrier family 10 (sodium/bile
                     acid cotransporter), member 2; Na+/taurocholate
                     cotransporting polypeptide 2"
                     /calculated_mol_wt=37583
     Site            10
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15350125; propagated from
                     UniProtKB/Swiss-Prot (Q12908.2)"
     Region          29..315
                     /region_name="bass"
                     /note="bile acid transporter; TIGR00841"
                     /db_xref="CDD:188087"
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            83..103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            127..147
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            196..216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            225..245
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Region          320..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12908.2)"
     Site            328
                     /site_type="other"
                     /note="Not glycosylated; propagated from
                     UniProtKB/Swiss-Prot (Q12908.2)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70172; propagated from
                     UniProtKB/Swiss-Prot (Q12908.2)"
     CDS             1..348
                     /gene="SLC10A2"
                     /gene_synonym="ASBT; IBAT; ISBT; NTCP2; PBAM; PBAM1"
                     /coded_by="NM_000452.3:169..1215"
                     /db_xref="CCDS:CCDS9506.1"
                     /db_xref="GeneID:6555"
                     /db_xref="HGNC:HGNC:10906"
                     /db_xref="MIM:601295"
ORIGIN      
        1 mndpnscvdn atvcsgascv vpesnfnnil svvlstvlti llalvmfsmg cnveikkflg
       61 hikrpwgicv gflcqfgimp ltgfilsvaf dilplqavvv liigccpggt asnilaywvd
      121 gdmdlsvsmt tcstllalgm mplclliytk mwvdsgsivi pydnigtslv slvvpvsigm
      181 fvnhkwpqka kiilkigsia gailivliav vggilyqsaw iiapklwiig tifpvagysl
      241 gfllariagl pwyrcrtvaf etgmqntqlc stivqlsftp eelnvvftfp liysifqlaf
      301 aaiflgfyva ykkchgknka eipeskengt epessfykan ggfqpdek
//
LOCUS       NP_001072989            1357 aa            linear   PRI 20-NOV-2025
DEFINITION  kinectin isoform a [Homo sapiens].
ACCESSION   NP_001072989
VERSION     NP_001072989.1
DBSOURCE    REFSEQ: accession NM_001079521.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1357)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1357)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1357)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1357)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1357)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1357)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1357)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1357)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1357)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA769269.1, Z22551.1,
            AL138499.4, AY536375.1 and BQ014936.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.138589.1,
                                           SRR1803612.12872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395314.8/ ENSP00000378725.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1357
                     /product="kinectin isoform a"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=156145
     Site            7..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          48..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          103..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          448..1270
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            904
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1055
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1084
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1088
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Region          <1190..>1357
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            1263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1313
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     Site            1329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86UP2.1)"
     CDS             1..1357
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001079521.2:179..4252"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41957.1"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktske rqqqveavel eakevlkklf
     1081 pkvsvpsnls ygewlhgfek kakecmagts gseevkvleh klkeademht llqlecekyk
     1141 svlaetegil qklqrsveqe enkwkvkvde shktikqmqs sftsseqele rlrsenkdie
     1201 nlrrerehle melekaemer styvtevrel kdlltelqkk lddsyseavr qneelnllka
     1261 qlnetltklr teqnerqkva gdlhkaqqsl eliqskivka agdttviens dvspetesse
     1321 ketmsvslnq tvtqlqqllq avnqqltkek ehyqvle
//
LOCUS       NP_001351447             586 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SLU7 isoform b [Homo sapiens].
ACCESSION   NP_001351447
VERSION     NP_001351447.1
DBSOURCE    REFSEQ: accession NM_001364518.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Rojo,C., Fernandez-Barrena,M.G.,
            Avila,M.A., Arechederra,M. and Berasain,C.
  TITLE     SLU7: A New Hub of Gene Expression Regulation-From Epigenetics to
            Protein Stability in Health and Disease
  JOURNAL   Int J Mol Sci 23 (21), 13411 (2022)
   PUBMED   36362191
  REMARK    GeneRIF: SLU7: A New Hub of Gene Expression Regulation-From
            Epigenetics to Protein Stability in Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Jimenez,M., Elizalde,M., Azkona,M.,
            Uriarte,I., Latasa,M.U., Urtasun,R., Bilbao,I., Sangro,B.,
            Garcia-Ruiz,C., Fernandez-Checa,J.C., Corrales,F.J., Esquivel,A.,
            Pineda-Lucena,A., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     Splicing Factor SLU7 Prevents Oxidative Stress-Mediated Hepatocyte
            Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage
  JOURNAL   Hepatology 74 (5), 2791-2807 (2021)
   PUBMED   34170569
  REMARK    GeneRIF: Splicing Factor SLU7 Prevents Oxidative Stress-Mediated
            Hepatocyte Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Recalde,M., Garate-Rascon,M., Elizalde,M., Azkona,M., Latasa,M.U.,
            Barcena-Varela,M., Sangro,B., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     The splicing regulator SLU7 is required to preserve DNMT1 protein
            stability and DNA methylation
  JOURNAL   Nucleic Acids Res 49 (15), 8592-8609 (2021)
   PUBMED   34331453
  REMARK    GeneRIF: The splicing regulator SLU7 is required to preserve DNMT1
            protein stability and DNA methylation.
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Shomron,N., Reznik,M. and Ast,G.
  TITLE     Splicing factor hSlu7 contains a unique functional domain required
            to retain the protein within the nucleus
  JOURNAL   Mol Biol Cell 15 (8), 3782-3795 (2004)
   PUBMED   15181151
  REMARK    GeneRIF: The zinc-knuckle motif of hSlu7 determines the cellular
            localization of the protein through a nucleocytoplasmic-sensitive
            shuttling balance.
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     An upstream AG determines whether a downstream AG is selected
            during catalytic step II of splicing
  JOURNAL   Mol Cell Biol 21 (5), 1509-1514 (2001)
   PUBMED   11238888
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     The RNA splicing factor hSlu7 is required for correct 3'
            splice-site choice
  JOURNAL   Nature 402 (6758), 207-210 (1999)
   PUBMED   10647016
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     Human step II splicing factor hSlu7 functions in restructuring the
            spliceosome between the catalytic steps of splicing
  JOURNAL   Genes Dev 13 (7), 841-850 (1999)
   PUBMED   10197984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091842.3.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is a
            splicing factor that has been found to be essential during the
            second catalytic step in the pre-mRNA splicing process. It
            associates with the spliceosome and contains a zinc knuckle motif
            that is found in other splicing factors and is involved in
            protein-nucleic acid and protein-protein interactions. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3), as well as variants 2, 4, and
            5, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803612.176674.1, SRR1803611.171033.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..586
                     /product="pre-mRNA-splicing factor SLU7 isoform b"
                     /note="step II splicing factor SLU7; zinc knuckle motif
                     containing; pre-mRNA-splicing factor SLU7; SLU7 splicing
                     factor homolog; SLU7 homolog, splicing factor"
                     /calculated_mol_wt=68256
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          77..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          129..169
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          161..434
                     /region_name="Slu7"
                     /note="Pre-mRNA splicing Prp18-interacting factor;
                     pfam11708"
                     /db_xref="CDD:463326"
     Region          206..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          496..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     CDS             1..586
                     /gene="SLU7"
                     /gene_synonym="9G8; hSlu7"
                     /coded_by="NM_001364518.2:501..2261"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS4352.1"
                     /db_xref="GeneID:10569"
                     /db_xref="HGNC:HGNC:16939"
                     /db_xref="MIM:605974"
ORIGIN      
        1 msatvvdavn aaplsgskem sleepkkmtr edwrkkkele eqrklgnapa evdeegkdin
       61 phipqyissv pwyidpskrp tlkhqrpqpe kqkqfsssge wykrgvkens iitkyrkgac
      121 encgamthkk kdcferprrv gakftgtnia pdehvqpqlm fdydgkrdrw ngynpeehmk
      181 iveeyakvdl akrtlkaqkl qeelasgklv eqanspkhqw geeepnsqme kdhnsedede
      241 dkyaddidmp gqnfdskrri tvrnlrired iakylrnldp nsayydpktr amrenpyana
      301 gknpdevsya gdnfvrytgd tismaqtqlf aweaydkgse vhlqadptkl ellyksfkvk
      361 kedfkeqqke silekyggqe hldappaell laqtedyvey srhgtvikgq eravacskye
      421 edvkihnhth iwgsywkegr wgykcchsff kysyctgeag keivnseeci ineitgeesv
      481 kkpqtlmelh qeklkeekkk kkkkkkkhrk sssdsddeek kheklkkaln aeearllhvk
      541 etmqiderkr pynsmyetre pteeemeayr mkrqrpddpm asflgq
//
LOCUS       NP_065854                620 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_065854
VERSION     NP_065854.3
DBSOURCE    REFSEQ: accession NM_020803.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Mena,E.L., Kjolby,R.A.S., Saxton,R.A., Werner,A., Lew,B.G.,
            Boyle,J.M., Harland,R. and Rape,M.
  TITLE     Dimerization quality control ensures neuronal development and
            survival
  JOURNAL   Science 362 (6411) (2018)
   PUBMED   30190310
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092658.2, CN290430.1, BX640727.1, BX647454.1, BX538173.1,
            BX640744.1 and AA878129.1.
            
            On Aug 22, 2003 this sequence version replaced NP_065854.2.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.259598.1,
                                           SRR1660803.9680.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273963.10/ ENSP00000273963.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..620
                     /product="kelch-like protein 8 isoform 1"
                     /note="kelch-like protein 8; kelch-like 8"
                     /calculated_mol_wt=68671
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          52..171
                     /region_name="BTB_POZ_KLHL8"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 8 (KLHL8); cd18238"
                     /db_xref="CDD:349547"
     Region          60..535
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          319..366
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          356..399
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          367..413
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          403..447
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          415..460
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          450..495
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          462..507
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          497..542
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          508..554
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     Region          544..586
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          555..599
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          556..601
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2G9.4)"
     CDS             1..620
                     /gene="KLHL8"
                     /coded_by="NM_020803.5:353..2215"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3617.1"
                     /db_xref="GeneID:57563"
                     /db_xref="HGNC:HGNC:18644"
                     /db_xref="MIM:611967"
ORIGIN      
        1 masdsmsskq arnhitkgkr qqqhqqiknr ssisdgdged sfifeaneaw kdfhgsllrf
       61 yengelcdvt lkvgsklisc hklvlacvip yframflsem aeakqtliei rdfdgdaied
      121 lvkfvyssrl tltvdnvqpl lyaacilqve lvaracceym klhfhpsncl avrafaeshn
      181 ridlmdmadq yacdhftevv ecedfvsvsp qhlhkllsss dlnienekqv ynaaikwlla
      241 npqhhskwld etlaqvrlpl lpvdflmgvv akeqivkqnl kcrdlldear nyhlhlssra
      301 vpdfeysirt tprkhtagvl fcvggrggsg dpfrsiecys inknswffgp emnsrrrhvg
      361 visvegkvya vgghdgnehl gsmemfdplt nkwmmkasmn tkrrgialas lggpiyaigg
      421 lddntcfndv erydiesdqw stvapmntpr ggvgsvalvn hvyavggndg maslssvery
      481 dphldkwiev kemgqrragn gvsklhgcly vvggfddnsp lssverydpr snkwdyvaal
      541 ttprggvgia tvmgkifavg ghngnaylnt veafdpvlnr welvgsvshc ragagvavcs
      601 cltsqirdvg hgsnnvvdcm
//
LOCUS       NP_001153895             438 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin-like growth factor 2 mRNA-binding protein 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001153895
VERSION     NP_001153895.1
DBSOURCE    REFSEQ: accession NM_001160423.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Luo,J., Yang,C., Xu,S., Ji,Z., Zhang,Y., Bai,H., Deng,Z., Liang,J.,
            Huang,Y., Zhi,E., Tian,R., Li,P., Zhao,F., Zhou,Z., Li,Z. and
            Yao,C.
  TITLE     RNA-binding protein IGF2BP1 is required for spermatogenesis in an
            age-dependent manner
  JOURNAL   Commun Biol 7 (1), 1362 (2024)
   PUBMED   39433965
  REMARK    GeneRIF: RNA-binding protein IGF2BP1 is required for
            spermatogenesis in an age-dependent manner.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Hornegger,H., Anisimova,A.S., Muratovic,A., Bourgeois,B.,
            Spinetti,E., Niedermoser,I., Covino,R., Madl,T. and Karagoz,G.E.
  TITLE     IGF2BP1 phosphorylation in the disordered linkers regulates
            ribonucleoprotein condensate formation and RNA metabolism
  JOURNAL   Nat Commun 15 (1), 9054 (2024)
   PUBMED   39426983
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Bai,W., Xiao,G., Xie,G., Chen,Z., Xu,X., Zeng,J. and Xie,J.
  TITLE     METTL3/IGF2BP1 influences the development of non-small-cell lung
            cancer by mediating m6A methylation modification of TRPV1
  JOURNAL   Thorac Cancer 15 (26), 1871-1881 (2024)
   PUBMED   39090761
  REMARK    GeneRIF: METTL3/IGF2BP1 influences the development of
            non-small-cell lung cancer by mediating m6A methylation
            modification of TRPV1.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Leclair,N.K., Lucas,C.G., Mirchia,K., McCortney,K., Horbinski,C.M.,
            Raleigh,D.R. and Anczukow,O.
  TITLE     The RNA-binding protein IGF2BP1 regulates stability of mRNA
            transcribed from FOXM1 target genes in hypermitotic meningiomas
  JOURNAL   Acta Neuropathol 148 (1), 28 (2024)
   PUBMED   39179895
  REMARK    GeneRIF: The RNA-binding protein IGF2BP1 regulates stability of
            mRNA transcribed from FOXM1 target genes in hypermitotic
            meningiomas.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Xiao,B., Li,Y., Yang,Y., Chen,C., Gong,S., Li,H., Yao,Q. and
            Wang,L.
  TITLE     METTL3 and IGF2BP1-Mediated m6A Modification of ZHX2 Promotes Tumor
            Property of Renal Cell Carcinoma
  JOURNAL   Kidney Blood Press Res 49 (1), 787-798 (2024)
   PUBMED   39159608
  REMARK    GeneRIF: METTL3 and IGF2BP1-Mediated m6A Modification of ZHX2
            Promotes Tumor Property of Renal Cell Carcinoma.
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Runge,S., Nielsen,F.C., Nielsen,J., Lykke-Andersen,J., Wewer,U.M.
            and Christiansen,J.
  TITLE     H19 RNA binds four molecules of insulin-like growth factor II
            mRNA-binding protein
  JOURNAL   J Biol Chem 275 (38), 29562-29569 (2000)
   PUBMED   10875929
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Doyle,G.A., Bourdeau-Heller,J.M., Coulthard,S., Meisner,L.F. and
            Ross,J.
  TITLE     Amplification in human breast cancer of a gene encoding a c-myc
            mRNA-binding protein
  JOURNAL   Cancer Res 60 (11), 2756-2759 (2000)
   PUBMED   10850408
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Nielsen,J., Christiansen,J., Lykke-Andersen,J., Johnsen,A.H.,
            Wewer,U.M. and Nielsen,F.C.
  TITLE     A family of insulin-like growth factor II mRNA-binding proteins
            represses translation in late development
  JOURNAL   Mol Cell Biol 19 (2), 1262-1270 (1999)
   PUBMED   9891060
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Doyle,G.A., Betz,N.A., Leeds,P.F., Fleisig,A.J., Prokipcak,R.D. and
            Ross,J.
  TITLE     The c-myc coding region determinant-binding protein: a member of a
            family of KH domain RNA-binding proteins
  JOURNAL   Nucleic Acids Res 26 (22), 5036-5044 (1998)
   PUBMED   9801297
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Prokipcak,R.D., Herrick,D.J. and Ross,J.
  TITLE     Purification and properties of a protein that binds to the
            C-terminal coding region of human c-myc mRNA
  JOURNAL   J Biol Chem 269 (12), 9261-9269 (1994)
   PUBMED   8132663
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091133.11, DA758608.1,
            DQ227344.1 and AC105030.11.
            
            Summary: This gene encodes a member of the insulin-like growth
            factor 2 mRNA-binding protein family. The protein encoded by this
            gene contains four K homology domains and two RNA recognition
            motifs. It functions by binding to the mRNAs of certain genes,
            including insulin-like growth factor 2, beta-actin and
            beta-transducin repeat-containing protein, and regulating their
            translation. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, May 2009].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (2) is shorter
            than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2481808.1,
                                           SRR14038191.3645283.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMN03267763
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..438
                     /product="insulin-like growth factor 2 mRNA-binding
                     protein 1 isoform 2"
                     /note="coding region determinant-binding protein;
                     zipcode-binding protein 1; VICKZ family member 1; IGF2
                     mRNA-binding protein 1; ZBP-1; IGF-II mRNA-binding protein
                     1; insulin-like growth factor 2 mRNA binding protein 1
                     deltaN CRDBP"
                     /calculated_mol_wt=48467
     Region          1..77
                     /region_name="RRM1_IGF2BP1"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     insulin-like growth factor 2 mRNA-binding protein 1
                     (IGF2BP1); cd12625"
                     /db_xref="CDD:241069"
     Region          81..>135
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          135..230
                     /region_name="KH-I_IGF2BP1_rpt2"
                     /note="second type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22493"
                     /db_xref="CDD:411921"
     Site            order(147,149..151,153..157,160..161,164..165,170..173)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411921"
     Region          265..340
                     /region_name="KH-I_IGF2BP1_rpt3"
                     /note="third type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22496"
                     /db_xref="CDD:411924"
     Site            order(278..280,282..286,289..290,300..304,313)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411924"
     Region          348..423
                     /region_name="KH-I_IGF2BP1_rpt4"
                     /note="fourth type I K homology (KH) RNA-binding domain
                     found in insulin-like growth factor 2 mRNA-binding protein
                     1 (IGF2BP1) and similar proteins; cd22499"
                     /db_xref="CDD:411927"
     Site            order(361..362,364..368,371,382..388)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:411927"
     CDS             1..438
                     /gene="IGF2BP1"
                     /gene_synonym="CRD-BP; CRDBP; IMP-1; IMP1; VICKZ1; ZBP1"
                     /coded_by="NM_001160423.2:362..1678"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54138.1"
                     /db_xref="GeneID:10642"
                     /db_xref="HGNC:HGNC:28866"
                     /db_xref="MIM:608288"
ORIGIN      
        1 mnklyignln esvtpadlek vfaehkisys gqflvksgya fvdcpdehwa mkaietfsgk
       61 velqgkrlei ehsvpkkqrs rkiqirnipp qlrwevldsl laqygtvenc eqvnteseta
      121 vvnvtysnre qtrqadevpl kilahnnfvg rligkegrnl kkveqdtetk itisslqdlt
      181 lynpertitv kgaienccra eqeimkkvre ayendvaams lqshlipgln laavglfpas
      241 ssavppppss vtgaapyssf mqapeqemvq vfipaqavga iigkkgqhik qlsrfasasi
      301 kiappetpds kvrmviitgp peaqfkaqgr iygklkeenf fgpkeevkle thirvpasaa
      361 grvigkggkt vnelqnltaa evvvprdqtp dendqvivki ighfyasqma qrkirdilaq
      421 vkqqhqkgqs nqaqarrk
//
LOCUS       NP_001158163             478 aa            linear   PRI 20-NOV-2025
DEFINITION  anti-Muellerian hormone type-2 receptor isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001158163
VERSION     NP_001158163.1
DBSOURCE    REFSEQ: accession NM_001164691.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Colaco,S., Achrekar,S., Patil,A., Sawant,U., Desai,S., Mangoli,V.,
            Jirge,P.R., Modi,D. and Mahale,S.D.
  TITLE     Association of AMH and AMHR2 gene polymorphisms with ovarian
            response and pregnancy outcomes in Indian women
  JOURNAL   J Assist Reprod Genet 39 (7), 1633-1642 (2022)
   PUBMED   35713750
  REMARK    GeneRIF: Association of AMH and AMHR2 gene polymorphisms with
            ovarian response and pregnancy outcomes in Indian women.
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Liu,Y., Wang,S., Lan,R. and Yang,J.
  TITLE     Identification of AMH and AMHR2 Variants Led to the Diagnosis of
            Persistent Mullerian Duct Syndrome in Three Cases
  JOURNAL   Genes (Basel) 13 (1), 159 (2022)
   PUBMED   35052499
  REMARK    GeneRIF: Identification of AMH and AMHR2 Variants Led to the
            Diagnosis of Persistent Mullerian Duct Syndrome in Three Cases.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Brunello,F.G. and Rey,R.A.
  TITLE     AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development
  JOURNAL   Sex Dev 16 (2-3), 138-146 (2022)
   PUBMED   34515230
  REMARK    GeneRIF: AMH and AMHR2 Involvement in Congenital Disorders of Sex
            Development.
            Review article
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Fang,J., Gao,G., Liu,J., Cai,L., Cui,Y. and Yang,X.
  TITLE     A novel mutation of AMHR2 in two brothers with persistent Mullerian
            duct syndrome and their intracytoplasmic sperm injection outcome
  JOURNAL   Mol Genet Genomic Med 9 (10), e1801 (2021)
   PUBMED   34480531
  REMARK    GeneRIF: A novel mutation of AMHR2 in two brothers with persistent
            Mullerian duct syndrome and their intracytoplasmic sperm injection
            outcome.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Faure,E., Gouedard,L., Imbeaud,S., Cate,R., Picard,J.Y., Josso,N.
            and di Clemente,N.
  TITLE     Mutant isoforms of the anti-Mullerian hormone type II receptor are
            not expressed at the cell membrane
  JOURNAL   J Biol Chem 271 (48), 30571-30575 (1996)
   PUBMED   8940028
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Imbeaud,S., Belville,C., Messika-Zeitoun,L., Rey,R., di
            Clemente,N., Josso,N. and Picard,J.Y.
  TITLE     A 27 base-pair deletion of the anti-mullerian type II receptor gene
            is the most common cause of the persistent mullerian duct syndrome
  JOURNAL   Hum Mol Genet 5 (9), 1269-1277 (1996)
   PUBMED   8872466
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Teixeira,J. and Donahoe,P.K.
  TITLE     Molecular biology of MIS and its receptors
  JOURNAL   J Androl 17 (4), 336-341 (1996)
   PUBMED   8889695
  REMARK    Review article
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Imbeaud,S., Faure,E., Lamarre,I., Mattei,M.G., di Clemente,N.,
            Tizard,R., Carre-Eusebe,D., Belville,C., Tragethon,L., Tonkin,C.,
            Nelson,J., McAuliffe,M., Bidart,J.M., Lababidi,A., Josso,N.,
            Cate,R.L. and Picard,J.Y.
  TITLE     Insensitivity to anti-mullerian hormone due to a mutation in the
            human anti-mullerian hormone receptor
  JOURNAL   Nat Genet 11 (4), 382-388 (1995)
   PUBMED   7493017
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Visser,J.A., McLuskey,A., van Beers,T., Weghuis,D.O., van
            Kessel,A.G., Grootegoed,J.A. and Themmen,A.P.
  TITLE     Structure and chromosomal localization of the human anti-mullerian
            hormone type II receptor gene
  JOURNAL   Biochem Biophys Res Commun 215 (3), 1029-1036 (1995)
   PUBMED   7488027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB020573.1, AY714878.1,
            BC126316.1 and AJ572328.1.
            
            Summary: This gene encodes the receptor for the anti-Mullerian
            hormone (AMH) which, in addition to testosterone, results in male
            sex differentiation. AMH and testosterone are produced in the
            testes by different cells and have different effects. Testosterone
            promotes the development of male genitalia while the binding of AMH
            to the encoded receptor prevents the development of the mullerian
            ducts into uterus and Fallopian tubes. Mutations in this gene are
            associated with persistent Mullerian duct syndrome type II.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (3) lacks two exons in the 3'
            coding region compared to variant 1. The resulting protein (isoform
            3) is shorter compared to isoform 1. Variants 2 and 3 encode
            isoforms that are the same length, but have distinct protein
            sequences.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.95746.1, AY714878.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..478
                     /product="anti-Muellerian hormone type-2 receptor isoform
                     3 precursor"
                     /EC_number="2.7.11.30"
                     /note="Mullerian inhibiting substance type II receptor;
                     MIS type II receptor; AMH type II receptor;
                     anti-Muellerian hormone type II receptor; Muellerian
                     inhibiting substance type II receptor; anti-Mullerian
                     hormone receptor, type II"
                     /calculated_mol_wt=50104
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1742
     Region          22..121
                     /region_name="TFP_LU_ECD_AMHR2"
                     /note="extracellular domain (ECD) found in anti-Muellerian
                     hormone type-2 receptor (AMHR2) and similar proteins;
                     cd23616"
                     /db_xref="CDD:467136"
     Region          207..413
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(209..212,215,217,228,230,258,279..282,333,337..338,
                     340,350..351)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..478
                     /gene="AMHR2"
                     /gene_synonym="AMHR; MISR2; MISRII; MRII"
                     /coded_by="NM_001164691.2:81..1517"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS53798.1"
                     /db_xref="GeneID:269"
                     /db_xref="HGNC:HGNC:465"
                     /db_xref="MIM:600956"
ORIGIN      
        1 mlgslglwal lptaveappn rrtcvffeap gvrgstktlg elldtgtelp rairclysrc
       61 cfgiwnltqd raqvemqgcr dsdepgcesl hcdpsprahp spgstlftcs cgtdfcnany
      121 shlpppgspg tpgsqgpqaa pgesiwmalv llglflllll llgsiilall qrknyrvrge
      181 pvpeprpdsg rdwsvelqel pelcfsqvir egghavvwag qlqgklvaik afpprsvaqf
      241 qaeralyelp glqhdhivrf itasrggpgr llsgpllvle lhpkgslchy ltqytsdwgs
      301 slrmalslaq glaflheerw qngqykpgia hrdlssqnvl iredgscaig dlglalvlpg
      361 ltqppawtpt qpqgpaaime dpdglrelle dcwdadpear ltaecvqqrl aalahpqesh
      421 pfpescprgc pplcpedcts ipaptilpcr pqrsachfsv qqgpcsrnpq pactlspv
//
LOCUS       NP_001339191             419 aa            linear   PRI 20-NOV-2025
DEFINITION  protein fuzzy homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001339191 XP_011525641
VERSION     NP_001339191.1
DBSOURCE    REFSEQ: accession NM_001352262.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Singh,S., Nampoothiri,S., Narayanan,D.L., Chaudhry,C., Salvankar,S.
            and Girisha,K.M.
  TITLE     Biallelic loss of function variants in FUZ result in an
            orofaciodigital syndrome
  JOURNAL   Eur J Hum Genet 32 (8), 1022-1026 (2024)
   PUBMED   38702430
  REMARK    GeneRIF: Biallelic loss of function variants in FUZ result in an
            orofaciodigital syndrome.
REFERENCE   3  (residues 1 to 419)
  AUTHORS   Langousis,G., Cavadini,S., Boegholm,N., Lorentzen,E., Kempf,G. and
            Matthias,P.
  TITLE     Structure of the ciliogenesis-associated CPLANE complex
  JOURNAL   Sci Adv 8 (15), eabn0832 (2022)
   PUBMED   35427153
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Seo,J.H., Zilber,Y., Babayeva,S., Liu,J., Kyriakopoulos,P., De
            Marco,P., Merello,E., Capra,V., Gros,P. and Torban,E.
  TITLE     Mutations in the planar cell polarity gene, Fuzzy, are associated
            with neural tube defects in humans
  JOURNAL   Hum Mol Genet 20 (22), 4324-4333 (2011)
   PUBMED   21840926
  REMARK    GeneRIF: Data propose that mutations in Fuzzy may account for a
            subset of neural tube defects in humans.
            Erratum:[Hum Mol Genet. 2015 Jul 1;24(13):3893. doi:
            10.1093/hmg/ddv131. PMID: 25954026]
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Heydeck,W. and Liu,A.
  TITLE     PCP effector proteins inturned and fuzzy play nonredundant roles in
            the patterning but not convergent extension of mammalian neural
            tube
  JOURNAL   Dev Dyn 240 (8), 1938-1948 (2011)
   PUBMED   21761479
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 419)
  AUTHORS   Park,T.J., Haigo,S.L. and Wallingford,J.B.
  TITLE     Ciliogenesis defects in embryos lacking inturned or fuzzy function
            are associated with failure of planar cell polarity and Hedgehog
            signaling
  JOURNAL   Nat Genet 38 (3), 303-311 (2006)
   PUBMED   16493421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB152506.1, AK315445.1,
            BU685207.1 and BU073247.1.
            
            On Jun 14, 2017 this sequence version replaced XP_011525641.1.
            
            Summary: This gene encodes a planar cell polarity protein that is
            involved in ciliogenesis and directional cell movement. Knockout
            studies in mice exhibit neural tube defects and defective cilia,
            and mutations in this gene are associated with neural tube defects
            in humans. Alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. The
            encoded isoform has the same N- and C-termini, but is one aa longer
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.3469220.1,
                                           SRR18074968.4064205.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..419
                     /product="protein fuzzy homolog isoform 3"
                     /note="protein fuzzy homolog; ciliogenesis and planar
                     polarity effector 3; ciliogenesis and planar polarity
                     effector complex subunit 3"
                     /calculated_mol_wt=45619
     Region          12..417
                     /region_name="Fuzzy"
                     /note="protein fuzzy and homologs; cd21091"
                     /db_xref="CDD:411043"
     CDS             1..419
                     /gene="FUZ"
                     /gene_synonym="CPLANE3; FY; NTD"
                     /coded_by="NM_001352262.2:187..1446"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:80199"
                     /db_xref="HGNC:HGNC:26219"
                     /db_xref="MIM:610622"
ORIGIN      
        1 mgeegtggtv hllclaassg vplfcrssrg gaparqqlpf svigslngvh mfgqnlevql
       61 ssartenttv vwksfhdsit livlssevgi selrlerllq mvfgamvllv gleeltnirn
      121 verlkkdlra syclidsflg dseligdltq cvdcvippeg sllqealsgf aeaagttfvs
      181 lvvsgrvvaa tegwwrlgtp eavllpwlvg slppqtardy pvylphgspt vphrlltltl
      241 lpslelcllc gpspplsqly pqllerwwqp lldplraclp lgpralpsgf plhtdilgll
      301 llhlelkrcl ftveplgdka epspeqrrrl lrnfytlvts thfppepgpp ektedevyqa
      361 qlpracylvl gteepgtgvr lvalqlglrr lllllspqsp thglrslath tlhaltpll
//
LOCUS       NP_003667                323 aa            linear   PRI 20-NOV-2025
DEFINITION  sphingolipid delta(4)-desaturase DES1 isoform 1 [Homo sapiens].
ACCESSION   NP_003667
VERSION     NP_003667.1
DBSOURCE    REFSEQ: accession NM_003676.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Dei Cas,M., Montavoci,L., Pasini,C., Caretti,A., Penati,S.,
            Martinelli,C., Gianelli,U., Casati,S., Nardecchia,F., Torella,A.,
            Brunetti-Pierri,N. and Trinchera,M.
  TITLE     Loss of function and reduced levels of sphingolipid desaturase
            DEGS1 variants are both relevant in disease mechanism
  JOURNAL   J Lipid Res 65 (3), 100517 (2024)
   PUBMED   38342436
  REMARK    GeneRIF: Loss of function and reduced levels of sphingolipid
            desaturase DEGS1 variants are both relevant in disease mechanism.
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Hulsmeier,A.J., Toelle,S.P., Bellstedt,P., Wentzel,C., Bahr,A.,
            Kolokotronis,K. and Hornemann,T.
  TITLE     The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker for DEGS1
            related hypomyelinating leukodystrophy
  JOURNAL   J Lipid Res 64 (12), 100464 (2023)
   PUBMED   37890668
  REMARK    GeneRIF: The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker
            for DEGS1 related hypomyelinating leukodystrophy.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Planas-Serra,L., Launay,N., Goicoechea,L., Heron,B., Jou,C.,
            Julia-Palacios,N., Ruiz,M., Fourcade,S., Casasnovas,C., De La
            Torre,C., Gelot,A., Marsal,M., Loza-Alvarez,P., Garcia-Cazorla,A.,
            Fatemi,A., Ferrer,I., Portero-Otin,M., Area-Gomez,E. and Pujol,A.
  TITLE     Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity
  JOURNAL   J Clin Invest 133 (10), e162957 (2023)
   PUBMED   36951944
  REMARK    GeneRIF: Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Hayashi,Y., Matsuda,K., Tanigawa,K., Tanikawa,T., Maeda,K. and
            Tsuchiya,K.
  TITLE     Dihydroceramide Delta4-Desaturase 1 Is Not Involved in SARS-CoV-2
            Infection
  JOURNAL   Biol Pharm Bull 45 (10), 1559-1563 (2022)
   PUBMED   36184516
  REMARK    GeneRIF: Dihydroceramide Delta4-Desaturase 1 Is Not Involved in
            SARS-CoV-2 Infection.
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Devlin,C.M., Lahm,T., Hubbard,W.C., Van Demark,M., Wang,K.C.,
            Wu,X., Bielawska,A., Obeid,L.M., Ivan,M. and Petrache,I.
  TITLE     Dihydroceramide-based response to hypoxia
  JOURNAL   J Biol Chem 286 (44), 38069-38078 (2011)
   PUBMED   21914808
  REMARK    GeneRIF: overexpression of DEGS1 or DEGS2 attenuates the DHC
            accumulation and increased cell proliferation during hypoxia
            Erratum:[J Biol Chem. 2012 May 18;287(21):17425]
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Idkowiak-Baldys,J., Apraiz,A., Li,L., Rahmaniyan,M., Clarke,C.J.,
            Kraveka,J.M., Asumendi,A. and Hannun,Y.A.
  TITLE     Dihydroceramide desaturase activity is modulated by oxidative
            stress
  JOURNAL   Biochem J 427 (2), 265-274 (2010)
   PUBMED   20105137
  REMARK    GeneRIF: oxidative stress leads to potent inhibition of
            dihydroceramide desaturase resulting in significant elevation in
            dihydroceramide levels in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Kraveka,J.M., Li,L., Szulc,Z.M., Bielawski,J., Ogretmen,B.,
            Hannun,Y.A., Obeid,L.M. and Bielawska,A.
  TITLE     Involvement of dihydroceramide desaturase in cell cycle progression
            in human neuroblastoma cells
  JOURNAL   J Biol Chem 282 (23), 16718-16728 (2007)
   PUBMED   17283068
  REMARK    GeneRIF: partial loss of DEGS-1 inhibited cell growth, with cell
            cycle arrest at G(0)/G(1). This was accompanied by a significant
            decrease in the amount of phosphorylated retinoblastoma protein
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Inuzuka,M., Hayakawa,M. and Ingi,T.
  TITLE     Serinc, an activity-regulated protein family, incorporates serine
            into membrane lipid synthesis
  JOURNAL   J Biol Chem 280 (42), 35776-35783 (2005)
   PUBMED   16120614
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Ternes,P., Franke,S., Zahringer,U., Sperling,P. and Heinz,E.
  TITLE     Identification and characterization of a sphingolipid delta
            4-desaturase family
  JOURNAL   J Biol Chem 277 (28), 25512-25518 (2002)
   PUBMED   11937514
  REMARK    GeneRIF: identification of sphingolipid delta 4-desaturase family
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Cadena,D.L., Kurten,R.C. and Gill,G.N.
  TITLE     The product of the MLD gene is a member of the membrane fatty acid
            desaturase family: overexpression of MLD inhibits EGF receptor
            biosynthesis
  JOURNAL   Biochemistry 36 (23), 6960-6967 (1997)
   PUBMED   9188692
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000961.2 and AY423730.1.
            
            Summary: This gene encodes a member of the membrane fatty acid
            desaturase family which is responsible for inserting double bonds
            into specific positions in fatty acids. This protein contains three
            His-containing consensus motifs that are characteristic of a group
            of membrane fatty acid desaturases. It is predicted to be a
            multiple membrane-spanning protein localized to the endoplasmic
            reticulum. Overexpression of this gene inhibited biosynthesis of
            the EGF receptor, suggesting a possible role of a fatty acid
            desaturase in regulating biosynthetic processing of the EGF
            receptor. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000961.2, SRR3476690.245725.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323699.9/ ENSP00000316476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.11"
     Protein         1..323
                     /product="sphingolipid delta(4)-desaturase DES1 isoform 1"
                     /EC_number="1.14.19.17"
                     /note="membrane fatty acid (lipid) desaturase;
                     sphingolipid delta 4 desaturase; migration-inducing gene
                     15 protein; membrane lipid desaturase; cell
                     migration-inducing gene 15 protein; degenerative
                     spermatocyte homolog 1, lipid desaturase; sphingolipid
                     delta(4)-desaturase 1; dihydroceramide desaturase 1;
                     degenerative spermatocyte homolog, lipid desaturase;
                     retinol isomerase"
                     /calculated_mol_wt=37735
     Region          6..42
                     /region_name="Lipid_DES"
                     /note="Sphingolipid Delta4-desaturase (DES); pfam08557"
                     /db_xref="CDD:462517"
     Region          26..315
                     /region_name="Delta4-sphingolipid-FADS-like"
                     /note="The Delta4-sphingolipid Fatty Acid Desaturase
                     (Delta4-sphingolipid-FADS)-like CD includes the
                     integral-membrane enzymes, dihydroceramide Delta-4
                     desaturase, involved in the synthesis of sphingosine; and
                     the human membrane fatty acid (lipid) desaturase...;
                     cd03508"
                     /db_xref="CDD:239585"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            order(89,93,128,131..132,259,262..263)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239585"
     Region          89..93
                     /region_name="Histidine box-1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          128..132
                     /region_name="Histidine box-2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          259..263
                     /region_name="Histidine box-3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15121.1)"
     CDS             1..323
                     /gene="DEGS1"
                     /gene_synonym="DEGS; DEGS-1; Des-1; DES1; FADS7; HLD18;
                     MIG15; MLD"
                     /coded_by="NM_003676.4:98..1069"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1540.1"
                     /db_xref="GeneID:8560"
                     /db_xref="HGNC:HGNC:13709"
                     /db_xref="MIM:615843"
ORIGIN      
        1 mgsrvsredf ewvytdqpha drrreilaky peikslmkpd pnliwiiimm vltqlgafyi
       61 vkdldwkwvi fgayafgsci nhsmtlaihe iahnaafgnc kamwnrwfgm fanlpigipy
      121 sisfkryhmd hhrylgadgv dvdiptdfeg wffctafrkf iwvilqplfy afrplfinpk
      181 pitylevint vaqvtfdili yyflgikslv ymlaasllgl glhpisghfi aehymflkgh
      241 etysyygpln lltfnvgyhn ehhdfpnipg kslplvrkia aeyydnlphy nswikvlydf
      301 vmddtispys rmkrhqkgem vle
//
LOCUS       NP_001291381             470 aa            linear   PRI 20-NOV-2025
DEFINITION  6-phosphogluconate dehydrogenase, decarboxylating isoform 3 [Homo
            sapiens].
ACCESSION   NP_001291381
VERSION     NP_001291381.1
DBSOURCE    REFSEQ: accession NM_001304452.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Wu,J., Chen,Y., Zou,H., Xu,K., Hou,J., Wang,M., Tian,S., Gao,M.,
            Ren,Q., Sun,C., Lu,S., Wang,Q., Shu,Y., Wang,S. and Wang,X.
  TITLE     6-Phosphogluconate dehydrogenase promotes glycolysis and fatty acid
            synthesis by inhibiting the AMPK pathway in lung adenocarcinoma
            cells
  JOURNAL   Cancer Lett 601, 217177 (2024)
   PUBMED   39179096
  REMARK    GeneRIF: 6-Phosphogluconate dehydrogenase promotes glycolysis and
            fatty acid synthesis by inhibiting the AMPK pathway in lung
            adenocarcinoma cells.
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Qiao,R., Wei,M., Chen,H., Zhang,X., Zhang,J., Gao,L., Ma,H.,
            Wang,Y. and Li,L.
  TITLE     Critical Role of 6-Phosphogluconate Dehydrogenase in TAp73-Mediated
            Cancer Cell Proliferation
  JOURNAL   Mol Cancer Res 21 (8), 825-835 (2023)
   PUBMED   37071129
  REMARK    GeneRIF: Critical Role of 6-Phosphogluconate Dehydrogenase in
            TAp73-Mediated Cancer Cell Proliferation.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Cao,J., Sun,X., Zhang,X. and Chen,D.
  TITLE     6PGD Upregulation is Associated with Chemo- and Immuno-Resistance
            of Renal Cell Carcinoma via AMPK Signaling-Dependent NADPH-Mediated
            Metabolic Reprograming
  JOURNAL   Am J Med Sci 360 (3), 279-286 (2020)
   PUBMED   32829780
  REMARK    GeneRIF: 6PGD Upregulation is Associated with Chemo- and
            Immuno-Resistance of Renal Cell Carcinoma via AMPK
            Signaling-Dependent NADPH-Mediated Metabolic Reprograming.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Xu,K., He,Z., Chen,M., Wang,N., Zhang,D., Yang,L., Xu,Z. and Xu,H.
  TITLE     HIF-1alpha regulates cellular metabolism, and Imatinib resistance
            by targeting phosphogluconate dehydrogenase in gastrointestinal
            stromal tumors
  JOURNAL   Cell Death Dis 11 (7), 586 (2020)
   PUBMED   32719331
  REMARK    GeneRIF: HIF-1alpha regulates cellular metabolism, and Imatinib
            resistance by targeting phosphogluconate dehydrogenase in
            gastrointestinal stromal tumors.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Gao,X., Zhao,L., Liu,S., Li,Y., Xia,S., Chen,D., Wang,M., Wu,S.,
            Dai,Q., Vu,H., Zacharias,L., DeBerardinis,R., Lim,E., Metallo,C.,
            Boggon,T.J., Lonial,S., Lin,R., Mao,H., Pan,Y., Shan,C. and Chen,J.
  TITLE     gamma-6-Phosphogluconolactone, a Byproduct of the Oxidative Pentose
            Phosphate Pathway, Contributes to AMPK Activation through
            Inhibition of PP2A
  JOURNAL   Mol Cell 76 (6), 857-871 (2019)
   PUBMED   31586547
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Komatsu,N., Kido,A., Kimura,Y. and Oya,M.
  TITLE     PGD phenotyping in bloodstains, organ tissues, dental pulps and
            hair roots by isoelectric focusing
  JOURNAL   Forensic Sci Int 48 (2), 185-194 (1990)
   PUBMED   2283141
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Beutler,E. and Kuhl,W.
  TITLE     Limiting role of 6-phosphogluconolactonase in erythrocyte hexose
            monophosphate pathway metabolism
  JOURNAL   J Lab Clin Med 106 (5), 573-577 (1985)
   PUBMED   3932573
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Beutler,E., Kuhl,W. and Gelbart,T.
  TITLE     6-Phosphogluconolactonase deficiency, a hereditary erythrocyte
            enzyme deficiency: possible interaction with glucose-6-phosphate
            dehydrogenase deficiency
  JOURNAL   Proc Natl Acad Sci U S A 82 (11), 3876-3878 (1985)
   PUBMED   3858849
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Povey,S., Morton,N.E. and Sherman,S.L.
  TITLE     Report of the Committee on the Genetic Constitution of Chromosomes
            1 and 2
  JOURNAL   Cytogenet Cell Genet 40 (1-4), 67-106 (1985)
   PUBMED   3864603
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Douglas,G.R., McAlpine,P.J. and Hamerton,J.L.
  TITLE     Regional localization of loci for human PGM and 6PGD on human
            chromosome one by use of hybrids of Chinese hamster-human somatic
            cells
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2737-2740 (1973)
   PUBMED   4517931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139424.21, AK298830.1,
            BC000368.2 and HY245069.1.
            
            Summary: 6-phosphogluconate dehydrogenase is the second
            dehydrogenase in the pentose phosphate shunt. Deficiency of this
            enzyme is generally asymptomatic, and the inheritance of this
            disorder is autosomal dominant. Hemolysis results from combined
            deficiency of 6-phosphogluconate dehydrogenase and
            6-phosphogluconolactonase suggesting a synergism of the two
            enzymopathies. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jan
            2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298830.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161674 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..470
                     /product="6-phosphogluconate dehydrogenase,
                     decarboxylating isoform 3"
                     /EC_number="1.1.1.44"
                     /note="6-phosphogluconate dehydrogenase, decarboxylating"
                     /calculated_mol_wt=51742
     Region          1..456
                     /region_name="Gnd"
                     /note="6-phosphogluconate dehydrogenase [Carbohydrate
                     transport and metabolism]; COG0362"
                     /db_xref="CDD:440131"
     CDS             1..470
                     /gene="PGD"
                     /gene_synonym="6PGD"
                     /coded_by="NM_001304452.2:299..1711"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5226"
                     /db_xref="HGNC:HGNC:8891"
                     /db_xref="MIM:172200"
ORIGIN      
        1 mgqnlilnmn dhgfvvcafn rtvskvddfl aneakgtkvv gaqslkemvs klkkprriil
       61 lvkagqavdd fieklvplld tgdiiidggn seyrdttrrc rdlkakgilf vgsgvsggee
      121 garygpslmp ggnkeawphi ktifqgiaak vgtgepccdw vgdegaghfv kmvhngieyg
      181 dmqliceayh lmkdvlgmaq demaqafedw nkteldsfli eitanilkfq dtdgkhllpk
      241 irdsagqkgt gkwtaisale ygvpvtlige avfarclssl kderiqaskk lkgpqkfqfd
      301 gdkksfledi rkalyaskii syaqgfmllr qaatefgwtl nyggialmwr ggciirsvfl
      361 gkikdafdrn pelqnllldd ffksavencq dswrravstg vqagipmpcf ttalsfydgy
      421 rhemlpasli qaqrdyfgah tyellakpgq fihtnwtghg gtvssssyna
//
LOCUS       NP_055393                210 aa            linear   PRI 20-NOV-2025
DEFINITION  rho-related GTP-binding protein RhoD isoform 1 [Homo sapiens].
ACCESSION   NP_055393
VERSION     NP_055393.1
DBSOURCE    REFSEQ: accession NM_014578.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Kazmi,N., Robinson,T., Zheng,J., Kar,S., Martin,R.M. and
            Ridley,A.J.
  TITLE     Rho GTPase gene expression and breast cancer risk: a Mendelian
            randomization analysis
  JOURNAL   Sci Rep 12 (1), 1463 (2022)
   PUBMED   35087170
  REMARK    GeneRIF: Rho GTPase gene expression and breast cancer risk: a
            Mendelian randomization analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 210)
  AUTHORS   King,V.L., Leclair,N.K., Coulter,A.M. and Campellone,K.G.
  TITLE     The actin nucleation factors JMY and WHAMM enable a rapid Arp2/3
            complex-mediated intrinsic pathway of apoptosis
  JOURNAL   PLoS Genet 17 (4), e1009512 (2021)
   PUBMED   33872315
  REMARK    GeneRIF: The actin nucleation factors JMY and WHAMM enable a rapid
            Arp2/3 complex-mediated intrinsic pathway of apoptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Blom,M., Reis,K. and Aspenstrom,P.
  TITLE     RhoD localization and function is dependent on its GTP/GDP-bound
            state and unique N-terminal motif
  JOURNAL   Eur J Cell Biol 97 (6), 393-401 (2018)
   PUBMED   29776664
  REMARK    GeneRIF: The GTPase deficient atypical Rho GTPases, which have a
            stalled GTPase activity, RhoD has an elevated intrinsic GDP/GTP
            exchange activity, rendering the protein constitutively active.
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Zanata,S.M., Hovatta,I., Rohm,B. and Puschel,A.W.
  TITLE     Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor
            activity in Semaphorin 3A-induced cytoskeletal collapse
  JOURNAL   J Neurosci 22 (2), 471-477 (2002)
   PUBMED   11784792
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Murphy,C., Saffrich,R., Olivo-Marin,J.C., Giner,A., Ansorge,W.,
            Fotsis,T. and Zerial,M.
  TITLE     Dual function of rhoD in vesicular movement and cell motility
  JOURNAL   Eur J Cell Biol 80 (6), 391-398 (2001)
   PUBMED   11484930
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Ridley,A.J.
  TITLE     Rho proteins: linking signaling with membrane trafficking
  JOURNAL   Traffic 2 (5), 303-310 (2001)
   PUBMED   11350626
  REMARK    Review article
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Kim,H.S., Choi,J.Y., Jung,A.R., Jang,K.L., Lee,W.H., Choi,W.C.,
            Crow,T.J. and Hyun,B.H.
  TITLE     Assignment of the human RhoHP1 gene (ARHD) to chromosome 11q14.3 by
            radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 53 (2000)
   PUBMED   10894936
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Shimizu,F., Watanabe,T.K., Okuno,S., Omori,Y., Fujiwara,T.,
            Takahashi,E. and Nakamura,Y.
  TITLE     Isolation of a novel human cDNA (rhoHP1) homologous to rho genes
  JOURNAL   Biochim Biophys Acta 1351 (1-2), 13-16 (1997)
   PUBMED   9116026
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM761362.1, BC001338.1 and
            CA433897.1.
            
            Summary: Ras homolog, or Rho, proteins interact with protein
            kinases and may serve as targets for activated GTPase. They play a
            critical role in muscle differentiation. The protein encoded by
            this gene binds GTP and is a member of the small GTPase
            superfamily. It is involved in endosome dynamics and reorganization
            of the actin cytoskeleton, and it may coordinate membrane transport
            with the function of the cytoskeleton. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.69415.1,
                                           SRR1163658.550091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308831.7/ ENSP00000308576.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..210
                     /product="rho-related GTP-binding protein RhoD isoform 1"
                     /note="ras homolog gene family, member A; Rho-related
                     protein HP1; Rho-related GTP-binding protein RhoD; ras
                     homolog D; ras homolog gene family, member D"
                     /calculated_mol_wt=23335
     Region          16..210
                     /region_name="Rho4_like"
                     /note="Ras homology family 4 (Rho4) of small guanosine
                     triphosphatases (GTPases)-like; cd04132"
                     /db_xref="CDD:206704"
     Site            order(19,49..50,53..54,56,58,66,70..71,73..75,81,84)
                     /site_type="other"
                     /note="putative GEF (guanine nucleotide exchange factor)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206704"
     Site            24..31
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206704"
     Site            order(27..32,71..72,74,130,132,173..174)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206704"
     Site            48..54
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206704"
     Site            49
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206704"
     Site            order(50,73,81,83)
                     /site_type="active"
                     /note="putative GDI (guanine nucleotide dissociation
                     inhibitor) interaction [active]"
                     /db_xref="CDD:206704"
     Site            order(50..51,75,81)
                     /site_type="other"
                     /note="putative GAP (GTPase-activating protein)
                     interaction site [polypeptide binding]"
                     /db_xref="CDD:206704"
     Site            order(51..52,81,84)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206704"
     Site            71..74
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206704"
     Site            order(74..75,81..84,89..91)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206704"
     Site            129..132
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206704"
     Site            172..174
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206704"
     Site            207..210
                     /site_type="other"
                     /note="putative lipid modification site [posttranslational
                     modification]"
                     /db_xref="CDD:206704"
     CDS             1..210
                     /gene="RHOD"
                     /gene_synonym="ARHD; Rho; RHOHP1; RHOM"
                     /coded_by="NM_014578.4:57..689"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8155.1"
                     /db_xref="GeneID:29984"
                     /db_xref="HGNC:HGNC:670"
                     /db_xref="MIM:605781"
ORIGIN      
        1 mtaaqaagee appgvrsvkv vlvgdggcgk tsllmvfadg afpesytptv ferymvnlqv
       61 kgkpvhlhiw dtagqddydr lrplfypdas vlllcfdvts pnsfdnifnr wypevnhfck
      121 kvpiivvgck tdlrkdkslv nklrrnglep vtyhrgqema rsvgavayle csarlhdnvh
      181 avfqeaaeva lssrgrnfwr ritqgfcvvt
//
LOCUS       NP_004746                802 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-5 isoform a [Homo sapiens].
ACCESSION   NP_004746
VERSION     NP_004746.2
DBSOURCE    REFSEQ: accession NM_004755.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 802)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 802)
  AUTHORS   Xu,P., Tao,Y., Zhang,H., Jin,M., Xu,H., Zou,S., Deng,F., Huang,L.,
            Zhang,H., Wang,X., Tang,X., Wang,Y., Yin,L. and Sun,X.
  TITLE     Associations of MSK1 Methylation and Executive Function With
            Suicidal Ideation in Adolescents With Major Depressive Disorder: A
            Prospective Cohort Study
  JOURNAL   J Clin Psychiatry 85 (1) (2024)
   PUBMED   38385994
  REMARK    GeneRIF: Associations of MSK1 Methylation and Executive Function
            With Suicidal Ideation in Adolescents With Major Depressive
            Disorder: A Prospective Cohort Study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 802)
  AUTHORS   Sattarifard,H., Safaei,A., Khazeeva,E., Rastegar,M. and Davie,J.R.
  TITLE     Mitogen- and stress-activated protein kinase (MSK1/2) regulated
            gene expression in normal and disease states
  JOURNAL   Biochem Cell Biol 101 (3), 204-219 (2023)
   PUBMED   36812480
  REMARK    GeneRIF: Mitogen- and stress-activated protein kinase (MSK1/2)
            regulated gene expression in normal and disease states.
            Review article
REFERENCE   4  (residues 1 to 802)
  AUTHORS   Akbar,N., Forteath,C., Hussain,M.S., Reyskens,K., Belch,J.J.F.,
            Lang,C.C., Mordi,I.R., Bhalraam,U., Arthur,J.S.C. and Khan,F.
  TITLE     Mitogen and Stress-Activated Kinases 1 and 2 Mediate Endothelial
            Dysfunction
  JOURNAL   Int J Mol Sci 22 (16), 8655 (2021)
   PUBMED   34445361
  REMARK    GeneRIF: Mitogen and Stress-Activated Kinases 1 and 2 Mediate
            Endothelial Dysfunction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 802)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 802)
  AUTHORS   Thomson,S., Clayton,A.L., Hazzalin,C.A., Rose,S., Barratt,M.J. and
            Mahadevan,L.C.
  TITLE     The nucleosomal response associated with immediate-early gene
            induction is mediated via alternative MAP kinase cascades: MSK1 as
            a potential histone H3/HMG-14 kinase
  JOURNAL   EMBO J 18 (17), 4779-4793 (1999)
   PUBMED   10469656
REFERENCE   7  (residues 1 to 802)
  AUTHORS   New,L., Zhao,M., Li,Y., Bassett,W.W., Feng,Y., Ludwig,S.,
            Padova,F.D., Gram,H. and Han,J.
  TITLE     Cloning and characterization of RLPK, a novel RSK-related protein
            kinase
  JOURNAL   J Biol Chem 274 (2), 1026-1032 (1999)
   PUBMED   9873047
REFERENCE   8  (residues 1 to 802)
  AUTHORS   Jain,N., Zhang,T., Fong,S.L., Lim,C.P. and Cao,X.
  TITLE     Repression of Stat3 activity by activation of mitogen-activated
            protein kinase (MAPK)
  JOURNAL   Oncogene 17 (24), 3157-3167 (1998)
   PUBMED   9872331
REFERENCE   9  (residues 1 to 802)
  AUTHORS   Deak,M., Clifton,A.D., Lucocq,L.M. and Alessi,D.R.
  TITLE     Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
            activated by MAPK and SAPK2/p38, and may mediate activation of CREB
  JOURNAL   EMBO J 17 (15), 4426-4441 (1998)
   PUBMED   9687510
REFERENCE   10 (residues 1 to 802)
  AUTHORS   Chung,J., Uchida,E., Grammer,T.C. and Blenis,J.
  TITLE     STAT3 serine phosphorylation by ERK-dependent and -independent
            pathways negatively modulates its tyrosine phosphorylation
  JOURNAL   Mol Cell Biol 17 (11), 6508-6516 (1997)
   PUBMED   9343414
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121784.5, AL133454.6 and AL159191.4.
            
            On Jul 11, 2003 this sequence version replaced NP_004746.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.8221.1,
                                           SRR1660807.30363.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000614987.5/ ENSP00000479667.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..802
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.11"
     Protein         1..802
                     /product="ribosomal protein S6 kinase alpha-5 isoform a"
                     /EC_number="2.7.11.1"
                     /note="RSK-like protein kinase; nuclear mitogen- and
                     stress-activated protein kinase 1; ribosomal protein S6
                     kinase alpha-5; RSKL; S6K-alpha-5; 90 kDa ribosomal
                     protein S6 kinase 5; ribosomal protein S6 kinase, 90kDa,
                     polypeptide 5"
                     /calculated_mol_wt=89735
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75582.1)"
     Region          48..337
                     /region_name="STKc_MSK1_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, Mitogen and stress-activated kinase 1; cd05613"
                     /db_xref="CDD:270764"
     Site            order(55..59,63,79,81,115,131..132,134,138,140,177,179,
                     181..182,184,194..195,198,213..218,247,253,256)
                     /site_type="active"
                     /db_xref="CDD:270764"
     Site            order(55..59,63,79,81,115,132..134,138,177,179,181..182,
                     184,194..195)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270764"
     Site            order(59,138,140,177,179,181,198,213..218,247,253,256)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270764"
     Site            order(194..204,207..218)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270764"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Region          320..379
                     /region_name="S_TK_X"
                     /note="Extension to Ser/Thr-type protein kinases;
                     smart00133"
                     /db_xref="CDD:214529"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (O75582.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Region          418..727
                     /region_name="STKc_MSK1_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Mitogen and stress-activated kinase 1; cd14179"
                     /db_xref="CDD:271081"
     Site            order(432..436,440,453,455,482,498..501,505,507,543..544,
                     546,548..549,551,564..565,568,583..587,589,716)
                     /site_type="active"
                     /db_xref="CDD:271081"
     Site            order(432..434,453,498..501,505,548..549,551,564,716)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271081"
     Site            order(436,505,507,543..544,546,548,568,583..587,589)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271081"
     Site            564..587
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271081"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17117922; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17117922; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C050; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:17117922; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000269|PubMed:17117922; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Region          741..802
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75582.1)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15568999; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     Site            798
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8C050; propagated from
                     UniProtKB/Swiss-Prot (O75582.1)"
     CDS             1..802
                     /gene="RPS6KA5"
                     /gene_synonym="MSK1; MSPK1; RLPK"
                     /coded_by="NM_004755.4:208..2616"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9893.1"
                     /db_xref="GeneID:9252"
                     /db_xref="HGNC:HGNC:10434"
                     /db_xref="MIM:603607"
ORIGIN      
        1 meeeggssgg aagtsadggd ggeqlltvkh elrtanltgh aekvgienfe llkvlgtgay
       61 gkvflvrkis ghdtgklyam kvlkkativq kakttehtrt erqvlehirq spflvtlhya
      121 fqtetklhli ldyinggelf thlsqrerft ehevqiyvge ivlalehlhk lgiiyrdikl
      181 enilldsngh vvltdfglsk efvadetera ysfcgtieym apdivrggds ghdkavdwws
      241 lgvlmyellt gaspftvdge knsqaeisrr ilkseppypq emsalakdli qrllmkdpkk
      301 rlgcgprdad eikehlffqk inwddlaakk vpapfkpvir deldvsnfae eftemdptys
      361 paalpqssek lfqgysfvap silfkrnaav idplqfhmgv erpgvtnvar sammkdspfy
      421 qhydldlkdk plgegsfsic rkcvhkksnq afavkiiskr meantqkeit alklceghpn
      481 ivklhevfhd qlhtflvmel lnggelferi kkkkhfsete asyimrklvs avshmhdvgv
      541 vhrdlkpenl lftdendnle ikiidfgfar lkppdnqplk tpcftlhyaa pellnqngyd
      601 escdlwslgv ilytmlsgqv pfqshdrslt ctsaveimkk ikkgdfsfeg eawknvsqea
      661 kdliqglltv dpnkrlkmsg lrynewlqdg sqlssnplmt pdilgssgaa vhtcvkatfh
      721 afnkykregf clqnvdkapl akrrkmkkts tstetrssss esshsssshs hgkttptktl
      781 qpsnpadsnn petlfqfsds va
//
LOCUS       NP_733776                470 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox protein Meis2 isoform d [Homo sapiens].
ACCESSION   NP_733776
VERSION     NP_733776.1
DBSOURCE    REFSEQ: accession NM_170676.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Xiao,Y., Liu,Y., Sun,Y., Huang,C. and Zhong,S.
  TITLE     MEIS2 suppresses breast cancer development by downregulating IL10
  JOURNAL   Cancer Rep (Hoboken) 7 (5), e2064 (2024)
   PUBMED   38711262
  REMARK    GeneRIF: MEIS2 suppresses breast cancer development by
            downregulating IL10.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Li,D. and Hu,A.
  TITLE     LINC-PINT suppresses breast cancer cell proliferation and migration
            via MEIS2/PPP3CC/NF-kappaB pathway by sponging miR-576-5p
  JOURNAL   Am J Med Sci 367 (3), 201-211 (2024)
   PUBMED   37660994
  REMARK    GeneRIF: LINC-PINT suppresses breast cancer cell proliferation and
            migration via MEIS2/PPP3CC/NF-kappaB pathway by sponging
            miR-576-5p.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Arunachalam,V., Lea,R., Hoy,W., Lee,S., Mott,S., Savige,J.,
            Mathews,J.D., McMorran,B.J. and Nagaraj,S.H.
  TITLE     Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study
  JOURNAL   Genome Med 16 (1), 29 (2024)
   PUBMED   38347632
  REMARK    GeneRIF: Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Xu,H., Chen,S., Li,J., Weng,S., Ren,Y., Zhang,Y., Wang,L., Liu,L.,
            Guo,C., Xing,Z., Luo,P., Cheng,Q., Han,X. and Liu,Z.
  TITLE     Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a Key
            Factor for the Aggressive Progression and Prognosis in Stage II/III
            Colorectal Cancer
  JOURNAL   J Proteome Res 23 (2), 760-774 (2024)
   PUBMED   38153233
  REMARK    GeneRIF: Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a
            Key Factor for the Aggressive Progression and Prognosis in Stage
            II/III Colorectal Cancer.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Fujino,T., Yamazaki,Y., Largaespada,D.A., Jenkins,N.A.,
            Copeland,N.G., Hirokawa,K. and Nakamura,T.
  TITLE     Inhibition of myeloid differentiation by Hoxa9, Hoxb8, and Meis
            homeobox genes
  JOURNAL   Exp Hematol 29 (7), 856-863 (2001)
   PUBMED   11438208
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Liu,Y., MacDonald,R.J. and Swift,G.H.
  TITLE     DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b
            trimer and cooperation with a pancreas-specific basic
            helix-loop-helix complex
  JOURNAL   J Biol Chem 276 (21), 17985-17993 (2001)
   PUBMED   11279116
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Yang,Y., Hwang,C.K., D'Souza,U.M., Lee,S.H., Junn,E. and
            Mouradian,M.M.
  TITLE     Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
            differentially regulate transcription
  JOURNAL   J Biol Chem 275 (27), 20734-20741 (2000)
   PUBMED   10764806
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Smith,J.E., Afonja,O., Yee,H.T., Inghirami,G. and Takeshita,K.
  TITLE     Chromosomal mapping to 15q14 and expression analysis of the human
            MEIS2 homeobox gene
  JOURNAL   Mamm Genome 8 (12), 951-952 (1997)
   PUBMED   9383298
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Steelman,S., Moskow,J.J., Muzynski,K., North,C., Druck,T.,
            Montgomery,J.C., Huebner,K., Daar,I.O. and Buchberg,A.M.
  TITLE     Identification of a conserved family of Meis1-related homeobox
            genes
  JOURNAL   Genome Res 7 (2), 142-156 (1997)
   PUBMED   9049632
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078909.7, AK056216.1,
            DA689122.1, AF179898.1, BC050431.1, BM679305.1 and AC018563.7.
            
            Summary: This gene encodes a homeobox protein belonging to the TALE
            ('three amino acid loop extension') family of
            homeodomain-containing proteins. TALE homeobox proteins are highly
            conserved transcription regulators, and several members have been
            shown to be essential contributors to developmental programs.
            Multiple transcript variants encoding distinct isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (d) uses an alternate in-frame
            splice junction at the 5' end of a coding exon and lacks the exon
            containing the stop codon compared to variant a, that causes a
            frameshift. The resulting isoform (d) lacks an alternate internal
            segment and has a longer and distinct C-terminus compared to
            isoform a. Variants d and i both encode the same isoform (d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF179898.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..470
                     /product="homeobox protein Meis2 isoform d"
                     /note="Meis homolog 2; TALE homeobox protein Meis2;
                     Meis1-related gene 1; meis1-related protein 1; Meis1,
                     myeloid ecotropic viral integration site 1 homolog 2"
                     /calculated_mol_wt=50929
     Region          71..191
                     /region_name="Required for interaction with PBX1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14770.2)"
     Region          110..194
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Region          193..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14770.2)"
     Site            order(282,325,328..329,332)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          295..333
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     Region          299..333
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000305|PubMed:26550823, ECO:0000305|Ref.16"
                     /note="propagated from UniProtKB/Swiss-Prot (O14770.2)"
     CDS             1..470
                     /gene="MEIS2"
                     /gene_synonym="CPCMR; HsT18361; MRG1"
                     /coded_by="NM_170676.5:1084..2496"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS10045.1"
                     /db_xref="GeneID:4212"
                     /db_xref="HGNC:HGNC:7001"
                     /db_xref="MIM:601740"
ORIGIN      
        1 maqrydelph yggmdgvgvp asmygdphap rpippvhhln hgpplhatqh ygahaphpnv
       61 mpasmgsavn dalkrdkdai yghplfplla lvfekcelat ctprepgvag gdvcssdsfn
      121 ediavfakqv raekplfssn peldnlmiqa iqvlrfhlle lekvhelcdn fchryisclk
      181 gkmpidlvid erdgssksdh eelsgsstnl adhnpsswrd hddatsthsa gtpgpssggh
      241 asqsgdnsse qgdgldnsva spgtgddddp dkdkkrqkkr gifpkvatni mrawlfqhlt
      301 hpypseeqkk qlaqdtglti lqvnnwfina rrrivqpmid qsnravsqga ayspegqpmg
      361 sfvldgqqhm girpaglqsm pgdyvsqggp mgmsmaqpsy tppqmtphpt qlrhgppmhs
      421 ylpshphhpa mmmhggppth pgmtmsaqsp tmlnsvdpnv ggqvmdihaq
//
LOCUS       NP_001241679             601 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell differentiation antigen CD6 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001241679
VERSION     NP_001241679.1
DBSOURCE    REFSEQ: accession NM_001254750.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 601)
  AUTHORS   Do,J.S., Arribas-Layton,D., Juan,J., Garcia,I., Saraswathy,S.,
            Qi,M., Montero,E. and Reijonen,H.
  TITLE     The CD318/CD6 axis limits type 1 diabetes islet
            autoantigen-specific human T cell activation
  JOURNAL   J Autoimmun 146, 103228 (2024)
   PUBMED   38642507
  REMARK    GeneRIF: The CD318/CD6 axis limits type 1 diabetes islet
            autoantigen-specific human T cell activation.
REFERENCE   2  (residues 1 to 601)
  AUTHORS   Wagner,M., Sobczynski,M., Wisniewski,A., Matusiak,L.,
            Kusnierczyk,P. and Jasek,M.
  TITLE     Polymorphisms in the CD6-ALCAM axis may modulate psoriasis risk and
            outcomes
  JOURNAL   Hum Immunol 85 (3), 110797 (2024)
   PUBMED   38580538
  REMARK    GeneRIF: Polymorphisms in the CD6-ALCAM axis may modulate psoriasis
            risk and outcomes.
REFERENCE   3  (residues 1 to 601)
  AUTHORS   Gurrea-Rubio,M., Wu,Q., Amin,M.A., Tsou,P.S., Campbell,P.L.,
            Amarista,C.I., Ikari,Y., Brodie,W.D., Mattichak,M.N., Muraoka,S.,
            Randon,P.M., Lind,M.E., Ruth,J.H., Mao-Draayer,Y., Ding,S.,
            Shen,X., Cooney,L.A., Lin,F. and Fox,D.A.
  TITLE     Activation of cytotoxic lymphocytes through CD6 enhances killing of
            cancer cells
  JOURNAL   Cancer Immunol Immunother 73 (2), 34 (2024)
   PUBMED   38280067
  REMARK    GeneRIF: Activation of cytotoxic lymphocytes through CD6 enhances
            killing of cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 601)
  AUTHORS   Aragon-Serrano,L., Carrillo-Serradell,L., Planells-Romeo,V.,
            Isamat,M., Velasco-de Andres,M. and Lozano,F.
  TITLE     CD6 and Its Interacting Partners: Newcomers to the Block of Cancer
            Immunotherapies
  JOURNAL   Int J Mol Sci 24 (24), 17510 (2023)
   PUBMED   38139340
  REMARK    GeneRIF: CD6 and Its Interacting Partners: Newcomers to the Block
            of Cancer Immunotherapies.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 601)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   6  (residues 1 to 601)
  AUTHORS   Robinson,W.H., Neuman de Vegvar,H.E., Prohaska,S.S., Rhee,J.W. and
            Parnes,J.R.
  TITLE     Human CD6 possesses a large, alternatively spliced cytoplasmic
            domain
  JOURNAL   Eur J Immunol 25 (10), 2765-2769 (1995)
   PUBMED   7589069
REFERENCE   7  (residues 1 to 601)
  AUTHORS   Whitney,G.S., Starling,G.C., Bowen,M.A., Modrell,B., Siadak,A.W.
            and Aruffo,A.
  TITLE     The membrane-proximal scavenger receptor cysteine-rich domain of
            CD6 contains the activated leukocyte cell adhesion molecule binding
            site
  JOURNAL   J Biol Chem 270 (31), 18187-18190 (1995)
   PUBMED   7543097
REFERENCE   8  (residues 1 to 601)
  AUTHORS   Aruffo,A., Melnick,M.B., Linsley,P.S. and Seed,B.
  TITLE     The lymphocyte glycoprotein CD6 contains a repeated domain
            structure characteristic of a new family of cell surface and
            secreted proteins
  JOURNAL   J Exp Med 174 (4), 949-952 (1991)
   PUBMED   1919444
REFERENCE   9  (residues 1 to 601)
  AUTHORS   Swack,J.A., Mier,J.W., Romain,P.L., Hull,S.R. and Rudd,C.E.
  TITLE     Biosynthesis and post-translational modification of CD6, a T cell
            signal-transducing molecule
  JOURNAL   J Biol Chem 266 (11), 7137-7143 (1991)
   PUBMED   2016320
REFERENCE   10 (residues 1 to 601)
  AUTHORS   Tsuge,I., Utsumi,K.R., Ueda,R., Takamoto,S. and Takahashi,T.
  TITLE     Assignment of gene coding human T-cell differentiation antigen,
            Tp120, to chromosome 11
  JOURNAL   Somat Cell Mol Genet 11 (3), 217-222 (1985)
   PUBMED   3923629
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003721.3, U66145.1 and AI657093.1.
            
            Summary: This gene encodes a protein found on the outer membrane of
            T-lymphocytes as well as some other immune cells. The encoded
            protein contains three scavenger receptor cysteine-rich (SRCR)
            domains and a binding site for an activated leukocyte cell adhesion
            molecule. The gene product is important for continuation of T cell
            activation. This gene may be associated with susceptibility to
            multiple sclerosis (PMID: 19525953, 21849685). Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (2) lacks two alternate in-frame
            exons in the 3' coding region compared to variant 1. The resulting
            protein (isoform 2) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U66145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..601
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.2"
     Protein         1..601
                     /product="T-cell differentiation antigen CD6 isoform 2
                     precursor"
                     /note="CD6 antigen; T-cell differentiation antigen CD6;
                     T12"
                     /calculated_mol_wt=62883
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1798
     Region          50..156
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     Region          161..260
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          270..361
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     CDS             1..601
                     /gene="CD6"
                     /gene_synonym="TP120"
                     /coded_by="NM_001254750.2:187..1992"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS58138.1"
                     /db_xref="GeneID:923"
                     /db_xref="HGNC:HGNC:1691"
                     /db_xref="MIM:186720"
ORIGIN      
        1 mwlffgitgl ltaalsghps pappdqlnts saeselwepg erlpvrltng ssscsgtvev
       61 rleaswepac galwdsraae avcralgcgg aeaasqlapp tpelppppaa gntsvaanat
      121 lagapallcs gaewrlcevv ehacrsdgrr arvtcaenra lrlvdgggac agrvemlehg
      181 ewgsvcddtw dledahvvcr qlgcgwavqa lpglhftpgr gpihrdqvnc sgaeaylwdc
      241 pglpgqhycg hkedagavcs ehqswrltgg adrcegqvev hfrgvwntvc dsewypseak
      301 vlcqslgcgt averpkglph slsgrmyysc ngeeltlsnc swrfnnsnlc sqslaarvlc
      361 sasrslhnls tpevpasvqt vtiessvtvk ienkesrelm llipsivlgi lllgslifia
      421 fillrikgky vfmlpiqvqa pppedsdsgs dsdyehydfs aqppvalttf ynsqrhrvtd
      481 eevqqsrfqm ppleegleel hashiptanp ghcitdppsl gpqyhprsns esstssgedy
      541 cnspksklpp wnpqvfsser ssfleqppnl elagtqpafs gspspqpdst dnddyddisa
      601 a
//
LOCUS       NP_060565                534 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch repeat and BTB domain-containing protein 4 isoform a [Homo
            sapiens].
ACCESSION   NP_060565
VERSION     NP_060565.4
DBSOURCE    REFSEQ: accession NM_018095.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Tsay,A. and Wang,J.C.
  TITLE     The Role of PIK3R1 in Metabolic Function and Insulin Sensitivity
  JOURNAL   Int J Mol Sci 24 (16), 12665 (2023)
   PUBMED   37628845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Chen,Z., Ioris,R.M., Richardson,S., Van Ess,A.N., Vendrell,I.,
            Kessler,B.M., Buffa,F.M., Busino,L., Clifford,S.C., Bullock,A.N.
            and D'Angiolella,V.
  TITLE     Disease-associated KBTBD4 mutations in medulloblastoma elicit
            neomorphic ubiquitylation activity to promote CoREST degradation
  JOURNAL   Cell Death Differ 29 (10), 1955-1969 (2022)
   PUBMED   35379950
  REMARK    GeneRIF: Disease-associated KBTBD4 mutations in medulloblastoma
            elicit neomorphic ubiquitylation activity to promote CoREST
            degradation.
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Uchida,E., Sasaki,A., Shirahata,M., Suzuki,T., Adachi,J.I.,
            Mishima,K., Yasuda,M., Fujimaki,T., Ichimura,K. and Nishikawa,R.
  TITLE     Role of proliferative marker index and KBTBD4 mutation in the
            pathological diagnosis of pineal parenchymal tumors
  JOURNAL   Brain Tumor Pathol 39 (3), 130-138 (2022)
   PUBMED   35000018
  REMARK    GeneRIF: Role of proliferative marker index and KBTBD4 mutation in
            the pathological diagnosis of pineal parenchymal tumors.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Leal,L.F., Cavagna,R.O., Campanella,N.C., Mancano,B., Almeida,G.C.,
            Matsushita,M., Almeida Junior,C.R., Saggioro,F., Stavale,J.N.,
            Malheiros,S.M.F., Lima,M., Hajj,G.N.M., Neder,L. and Reis,R.M.
  TITLE     Lack of KBTBD4 Mutations in Molecularly Classified Brazilian
            Medulloblastomas
  JOURNAL   J Neuropathol Exp Neurol 78 (9), 788-790 (2019)
   PUBMED   31403685
  REMARK    GeneRIF: Our findings suggest that KBTBD4 mutations are uncommon in
            Brazilian MBGRP3 and MBGRP4 medulloblastomas subgroups.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104942.5 and KF459542.1.
            
            On Oct 17, 2008 this sequence version replaced NP_060565.3.
            
            Transcript Variant: This variant (1) differs in the 5' UTR and
            coding sequence compared to variant 4. The resulting isoform (a)
            has a shorter and distinct N-terminus compared to isoform c.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.944498.1,
                                           SRR1803612.174017.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430070.7/ ENSP00000415106.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..534
                     /product="kelch repeat and BTB domain-containing protein 4
                     isoform a"
                     /note="BTB and kelch domain containing 4; kelch repeat and
                     BTB domain-containing protein 4; BTB and kelch
                     domain-containing protein 4; kelch repeat and BTB (POZ)
                     domain containing 4"
                     /calculated_mol_wt=59773
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          29..168
                     /region_name="BTB_POZ_KBTBD4"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 4 (KBTBD4); cd18272"
                     /db_xref="CDD:349581"
     Region          63..495
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          158..245
                     /region_name="BACK_KBTBD4"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 4 (KBTBD4);
                     cd18481"
                     /db_xref="CDD:350556"
     Region          255..301
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          295..330
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          302..344
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          334..381
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          347..394
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          384..430
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          396..446
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     Region          438..483
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..497
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVX7.4)"
     CDS             1..534
                     /gene="KBTBD4"
                     /gene_synonym="BKLHD4; HSPC252"
                     /coded_by="NM_018095.6:20..1624"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44594.1"
                     /db_xref="GeneID:55709"
                     /db_xref="HGNC:HGNC:23761"
                     /db_xref="MIM:617645"
ORIGIN      
        1 mkggnadswq reklasmesp eepgasmden yfvnytfkdr shsgrvaqgi mklcleeelf
       61 advtisvegr efqlhrlvls aqscffrsmf tsnlkeahnr vivlqdvses vfqllvdyiy
      121 hgtvklraee lqeiyevsdm yqltslfeec srflartvqv gnclqvmwla drhsdpelyt
      181 aakhcakthl aqlqnteefl hlphrlltdi isdgvpcsqn pteaieawin fnkeereafa
      241 eslrtslkei genvhiylig kessrthsla vslhcaedds isvsgqnslc hqitaackhg
      301 gdlyvvggsi prrmwkcnna tvdwewcapl prdrlqhtlv svpgkdaiys lggktlqdtl
      361 snaviyyrvg dnvwtettql evavsgaaga nlngiiyllg geendldfft kpsrliqcfd
      421 tetdkchvkp yvlpfagrmh aavhkdlvfi vaegdslvcy nplldsftrl clpeawssap
      481 slwkiascng siyvfrdryk kgdantykld patsavtvtr gikvlltnlq fvla
//
LOCUS       NP_079218                445 aa            linear   PRI 20-NOV-2025
DEFINITION  ATPase PAAT [Homo sapiens].
ACCESSION   NP_079218
VERSION     NP_079218.2
DBSOURCE    REFSEQ: accession NM_024942.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Yang,X., Yang,J., Li,L., Sun,L., Yi,X., Han,X., Si,W., Yan,R.,
            Chen,Z., Xie,G., Li,W., Shang,Y. and Liang,J.
  TITLE     PAAT, a novel ATPase and trans-regulator of mitochondrial ABC
            transporters, is critically involved in the maintenance of
            mitochondrial homeostasis
  JOURNAL   FASEB J 28 (11), 4821-4834 (2014)
   PUBMED   25063848
  REMARK    GeneRIF: Regulates iron transport into the mitochondria
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Kitanaka,S., Isojima,T., Takaki,M., Numakura,C., Hayasaka,K. and
            Igarashi,T.
  TITLE     Association of vitamin D-related gene polymorphisms with
            manifestation of vitamin D deficiency in children
  JOURNAL   Endocr J 59 (11), 1007-1014 (2012)
   PUBMED   22785457
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Ahn,J., Yu,K., Stolzenberg-Solomon,R., Simon,K.C., McCullough,M.L.,
            Gallicchio,L., Jacobs,E.J., Ascherio,A., Helzlsouer,K.,
            Jacobs,K.B., Li,Q., Weinstein,S.J., Purdue,M., Virtamo,J.,
            Horst,R., Wheeler,W., Chanock,S., Hunter,D.J., Hayes,R.B., Kraft,P.
            and Albanes,D.
  TITLE     Genome-wide association study of circulating vitamin D levels
  JOURNAL   Hum Mol Genet 19 (13), 2739-2745 (2010)
   PUBMED   20418485
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC032645.1, CB044034.1 and AC073585.8.
            
            On Aug 21, 2007 this sequence version replaced NP_079218.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.230873.1,
                                           SRR1803617.22055.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2146411 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000481909.2/ ENSP00000419126.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..445
                     /product="ATPase PAAT"
                     /EC_number="3.6.1.3"
                     /note="uncharacterized protein C10orf88; protein
                     associated with ABC transporters"
                     /calculated_mol_wt=49118
     Region          59..198
                     /region_name="PAAT-like"
                     /note="ATPase PAAT-like; pfam14958"
                     /db_xref="CDD:464404"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8K7.2)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8K7.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8K7.2)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8K7.2)"
     Region          426..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8K7.2)"
     CDS             1..445
                     /gene="C10orf88"
                     /gene_synonym="PAAT"
                     /coded_by="NM_024942.4:50..1387"
                     /db_xref="CCDS:CCDS7632.1"
                     /db_xref="GeneID:80007"
                     /db_xref="HGNC:HGNC:25822"
                     /db_xref="MIM:620661"
ORIGIN      
        1 metrtedggl trrptlassw dvaggalths llltraglgp gdfdweella ppapgqdlvi
       61 lkrnhnnkde npcflylrcg pdggeeiasi gilssarnme vylgeeycgt srgknvctvl
      121 ddsehekiil ykknlkless thackiklls fgerqcvfis kvvvhmrsvf ansstsspal
      181 gsridldkvq timesmgskl spgaqqlmdm vrcqqrncip igeqlqsvlg nsgykhmigl
      241 qssstlgtln kssstpfpfr tgltsgnvte nlqtyidkst qlpggenstk ldeckvmpqn
      301 hsflendlkn amasflpkkv sdnsnipnse llpflqnlcs qvnhlhvgnk tecqenitkh
      361 gerilgvgme eqsicsylek ilsknmelme kklmdyidqr ihelqehidd kiallldllq
      421 npnspptgip lrhydsgerl snger
//
LOCUS       NP_001338207             139 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 107 isoform 3 [Homo sapiens].
ACCESSION   NP_001338207
VERSION     NP_001338207.1
DBSOURCE    REFSEQ: accession NM_001351278.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Dubaic,M., Peskova,L., Hampl,M., Weissova,K., Celiker,C.,
            Shylo,N.A., Hruba,E., Kavkova,M., Zikmund,T., Weatherbee,S.D.,
            Kaiser,J., Barta,T. and Buchtova,M.
  TITLE     Role of ciliopathy protein TMEM107 in eye development: insights
            from a mouse model and retinal organoid
  JOURNAL   Life Sci Alliance 6 (12), e202302073 (2023)
   PUBMED   37863656
  REMARK    GeneRIF: Role of ciliopathy protein TMEM107 in eye development:
            insights from a mouse model and retinal organoid.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Bruel,A.L., Franco,B., Duffourd,Y., Thevenon,J., Jego,L., Lopez,E.,
            Deleuze,J.F., Doummar,D., Giles,R.H., Johnson,C.A., Huynen,M.A.,
            Chevrier,V., Burglen,L., Morleo,M., Desguerres,I., Pierquin,G.,
            Doray,B., Gilbert-Dussardier,B., Reversade,B.,
            Steichen-Gersdorf,E., Baumann,C., Panigrahi,I.,
            Fargeot-Espaliat,A., Dieux,A., David,A., Goldenberg,A., Bongers,E.,
            Gaillard,D., Argente,J., Aral,B., Gigot,N., St-Onge,J.,
            Birnbaum,D., Phadke,S.R., Cormier-Daire,V., Eguether,T.,
            Pazour,G.J., Herranz-Perez,V., Goldstein,J.S., Pasquier,L.,
            Loget,P., Saunier,S., Megarbane,A., Rosnet,O., Leroux,M.R.,
            Wallingford,J.B., Blacque,O.E., Nachury,M.V., Attie-Bitach,T.,
            Riviere,J.B., Faivre,L. and Thauvin-Robinet,C.
  TITLE     Fifteen years of research on oral-facial-digital syndromes: from 1
            to 16 causal genes
  JOURNAL   J Med Genet 54 (6), 371-380 (2017)
   PUBMED   28289185
  REMARK    Review article
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Shylo,N.A., Christopher,K.J., Iglesias,A., Daluiski,A. and
            Weatherbee,S.D.
  TITLE     TMEM107 Is a Critical Regulator of Ciliary Protein Composition and
            Is Mutated in Orofaciodigital Syndrome
  JOURNAL   Hum Mutat 37 (2), 155-159 (2016)
   PUBMED   26518474
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Lambacher,N.J., Bruel,A.L., van Dam,T.J., Szymanska,K.,
            Slaats,G.G., Kuhns,S., McManus,G.J., Kennedy,J.E., Gaff,K.,
            Wu,K.M., van der Lee,R., Burglen,L., Doummar,D., Riviere,J.B.,
            Faivre,L., Attie-Bitach,T., Saunier,S., Curd,A., Peckham,M.,
            Giles,R.H., Johnson,C.A., Huynen,M.A., Thauvin-Robinet,C. and
            Blacque,O.E.
  TITLE     TMEM107 recruits ciliopathy proteins to subdomains of the ciliary
            transition zone and causes Joubert syndrome
  JOURNAL   Nat Cell Biol 18 (1), 122-131 (2016)
   PUBMED   26595381
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Christopher,K.J., Wang,B., Kong,Y. and Weatherbee,S.D.
  TITLE     Forward genetics uncovers Transmembrane protein 107 as a novel
            factor required for ciliogenesis and Sonic hedgehog signaling
  JOURNAL   Dev Biol 368 (2), 382-392 (2012)
   PUBMED   22698544
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Geisert,E.E., Lu,L., Freeman-Anderson,N.E., Templeton,J.P.,
            Nassr,M., Wang,X., Gu,W., Jiao,Y. and Williams,R.W.
  TITLE     Gene expression in the mouse eye: an online resource for genetics
            using 103 strains of mice
  JOURNAL   Mol Vis 15, 1730-1763 (2009)
   PUBMED   19727342
  REMARK    GeneRIF: TMEM107 (2810049P21Rik) is a strong candidate gene for
            central areolar choroidal dystrophy, CACD (human 17p13). Conclusion
            is based on a massive expression data set for mouse (103 strains in
            GeneNetwork.org) and joint analysis of RetNet database.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070231.1 and AC129492.6.
            
            Summary: This gene encodes a transmembrane protein and component of
            the primary cilia transition zone. The encoded protein regulates
            ciliogenesis and ciliary protein composition. Human fibroblasts
            expressing a mutant allele of this gene exhibit reduced numbers of
            cilia, altered cilia length, and impaired sonic hedgehog signaling.
            In human patients, different mutations in this gene cause different
            ciliopathies, including Meckel-Gruber syndrome and orofaciodigital
            syndrome. [provided by RefSeq, May 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070231.1, BU852346.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..139
                     /product="transmembrane protein 107 isoform 3"
                     /calculated_mol_wt=15118
     Region          7..128
                     /region_name="TMEM107"
                     /note="Transmembrane protein; pfam14995"
                     /db_xref="CDD:464430"
     CDS             1..139
                     /gene="TMEM107"
                     /gene_synonym="GRVS638; JBTS29; MKS13; PRO1268"
                     /coded_by="NM_001351278.2:95..514"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86572.1"
                     /db_xref="GeneID:84314"
                     /db_xref="HGNC:HGNC:28128"
                     /db_xref="MIM:616183"
ORIGIN      
        1 mgrvsglvps rfltllahlv vvitlfwsrd sniqaclplt ftpeeydkqd ihplplcrlv
       61 aalsvtlglf avelagflsg vsmfnstqsl isigahcsas valsffifer wecttycalp
      121 avtemalfvt vfglkkkpf
//
LOCUS       NP_001258785             252 aa            linear   PRI 20-NOV-2025
DEFINITION  protein TAMALIN isoform 2 [Homo sapiens].
ACCESSION   NP_001258785
VERSION     NP_001258785.1
DBSOURCE    REFSEQ: accession NM_001271856.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Caillet-Saguy,C. and Wolff,N.
  TITLE     PDZ-Containing Proteins Targeted by the ACE2 Receptor
  JOURNAL   Viruses 13 (11), 2281 (2021)
   PUBMED   34835087
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Pandey,S., Ramsakha,N., Sharma,R., Gulia,R., Ojha,P., Lu,W. and
            Bhattacharyya,S.
  TITLE     The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors
  JOURNAL   J Biol Chem 295 (25), 8575-8588 (2020)
   PUBMED   32376687
  REMARK    GeneRIF: The post-synaptic scaffolding protein tamalin regulates
            ligand-mediated trafficking of metabotropic glutamate receptors.
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Matosin,N., Fernandez-Enright,F., Lum,J.S., Andrews,J.L., Engel,M.,
            Huang,X.F. and Newell,K.A.
  TITLE     Metabotropic glutamate receptor 5, and its trafficking molecules
            Norbin and Tamalin, are increased in the CA1 hippocampal region of
            subjects with schizophrenia
  JOURNAL   Schizophr Res 166 (1-3), 212-218 (2015)
   PUBMED   26048293
  REMARK    GeneRIF: Schizophrenia subjects compared to controls showed a
            marked increase in CA1 hippocampal Norbin, and Tamalin proteins
            (47% and 34% respectively), which are endogenous regulators of
            mGluR5 signalling and trafficking
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Fransen,E., Bonneux,S., Corneveaux,J.J., Schrauwen,I., Di
            Berardino,F., White,C.H., Ohmen,J.D., Van de Heyning,P.,
            Ambrosetti,U., Huentelman,M.J., Van Camp,G. and Friedman,R.A.
  TITLE     Genome-wide association analysis demonstrates the highly polygenic
            character of age-related hearing impairment
  JOURNAL   Eur J Hum Genet 23 (1), 110-115 (2015)
   PUBMED   24939585
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Sugi,T., Oyama,T., Muto,T., Nakanishi,S., Morikawa,K. and
            Jingami,H.
  TITLE     Crystal structures of autoinhibitory PDZ domain of Tamalin:
            implications for metabotropic glutamate receptor trafficking
            regulation
  JOURNAL   EMBO J 26 (8), 2192-2205 (2007)
   PUBMED   17396155
  REMARK    GeneRIF: The crystal structures of the autoinhibitory PDZ domain of
            Tamalin has implications for the regulation of metabotropic
            glutamate receptor trafficking.
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Kitano,J., Yamazaki,Y., Kimura,K., Masukado,T., Nakajima,Y. and
            Nakanishi,S.
  TITLE     Tamalin is a scaffold protein that interacts with multiple neuronal
            proteins in distinct modes of protein-protein association
  JOURNAL   J Biol Chem 278 (17), 14762-14768 (2003)
   PUBMED   12586822
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Kitano,J., Kimura,K., Yamazaki,Y., Soda,T., Shigemoto,R.,
            Nakajima,Y. and Nakanishi,S.
  TITLE     Tamalin, a PDZ domain-containing protein, links a protein complex
            formation of group 1 metabotropic glutamate receptors and the
            guanine nucleotide exchange factor cytohesins
  JOURNAL   J Neurosci 22 (4), 1280-1289 (2002)
   PUBMED   11850456
REFERENCE   9  (residues 1 to 252)
  AUTHORS   Nevrivy,D.J., Peterson,V.J., Avram,D., Ishmael,J.E., Hansen,S.G.,
            Dowell,P., Hruby,D.E., Dawson,M.I. and Leid,M.
  TITLE     Interaction of GRASP, a protein encoded by a novel retinoic
            acid-induced gene, with members of the cytohesin family of guanine
            nucleotide exchange factors
  JOURNAL   J Biol Chem 275 (22), 16827-16836 (2000)
   PUBMED   10828067
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Dominguez,O., Ashhab,Y., Sabater,L., Belloso,E., Caro,P. and
            Pujol-Borrell,R.
  TITLE     Cloning of ARE-containing genes by AU-motif-directed display
  JOURNAL   Genomics 54 (2), 278-286 (1998)
   PUBMED   9828130
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY035281.1, BC035500.2 and
            BC052967.1.
            
            Summary: This gene encodes a protein that functions as a molecular
            scaffold, linking receptors, including group 1 metabotropic
            glutamate receptors, to neuronal proteins. The encoded protein
            contains conserved domains, including a leucine zipper sequence,
            PDZ domain and a C-terminal PDZ-binding motif. Alternately spliced
            transcript variants have been observed for this gene.[provided by
            RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) has multiple differences,
            compared to variant 1. These differences result in a distinct 5'
            UTR and cause translation initiation at a downstream start codon,
            compared to variant 1. The encoded protein (isoform 2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035500.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..252
                     /product="protein TAMALIN isoform 2"
                     /note="general receptor for phosphoinositides 1 associated
                     scaffold protein; GRP1 (general receptor for
                     phosphoinositides 1)-associated scaffold protein; protein
                     TAMALIN"
                     /calculated_mol_wt=26773
     Region          <7..44
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     CDS             1..252
                     /gene="TAMALIN"
                     /gene_synonym="GRASP"
                     /coded_by="NM_001271856.2:271..1029"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS61124.1"
                     /db_xref="GeneID:160622"
                     /db_xref="HGNC:HGNC:18707"
                     /db_xref="MIM:612027"
ORIGIN      
        1 mtllpskggd tiasvnglnv egirhreivd iikasgnvlr letlygtsir kaelearlqy
       61 lkqtlyekwg eyrslmvqeq rlvhglvvkd psiydtlesv rsclygagll pgslpfgpll
      121 avpgrprgga rrargdadda vyhtcffgds eppalppppp parafgpgpa etpavgpgpg
      181 praalsrsas vrcagpgggg gggapgalwt eareqalcgp glrktkyrsf rrrllkfipg
      241 lnrsleeees ql
//
LOCUS       NP_055192                621 aa            linear   PRI 20-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055192
VERSION     NP_055192.1
DBSOURCE    REFSEQ: accession NM_014377.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Yang,F., Hu,A., Guo,Y., Wang,J., Li,D., Wang,X., Jin,S., Yuan,B.,
            Cai,S., Zhou,Y., Li,Q., Chen,G., Gao,H., Zheng,L. and Tong,Q.
  TITLE     p113 isoform encoded by CUX1 circular RNA drives tumor progression
            via facilitating ZRF1/BRD4 transactivation
  JOURNAL   Mol Cancer 20 (1), 123 (2021)
   PUBMED   34579723
  REMARK    GeneRIF: p113 isoform encoded by CUX1 circular RNA drives tumor
            progression via facilitating ZRF1/BRD4 transactivation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Liu,H., Li,J., Zhao,H., Liu,X. and Ye,X.
  TITLE     DNAJC2 is reversely regulated by miR-627-3p, promoting the
            proliferation of colorectal cancer
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165158
  REMARK    GeneRIF: DNAJC2 is reversely regulated by miR6273p, promoting the
            proliferation of colorectal cancer.
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Hundley,H.A., Walter,W., Bairstow,S. and Craig,E.A.
  TITLE     Human Mpp11 J protein: ribosome-tethered molecular chaperones are
            ubiquitous
  JOURNAL   Science 308 (5724), 1032-1034 (2005)
   PUBMED   15802566
  REMARK    GeneRIF: concluded that Mpp11, an ortholog of yeast Zuo, is a
            ribosome-associated J protein; proposed that in metazoans,
            ribosome-associated Zuo and Mpp11 orthologs recruit cytosolic Hsc70
            to short ribosome-bound nascent chains as they exit the ribosome
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Li,L., Schmitt,A.,
            Shiku,H., Dohner,H. and Schmitt,M.
  TITLE     mRNA expression of leukemia-associated antigens in patients with
            acute myeloid leukemia for the development of specific
            immunotherapies
  JOURNAL   Int J Cancer 108 (5), 704-711 (2004)
   PUBMED   14696097
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Greiner,J., Ringhoffer,M., Taniguchi,M., Hauser,T., Schmitt,A.,
            Dohner,H. and Schmitt,M.
  TITLE     Characterization of several leukemia-associated antigens inducing
            humoral immune responses in acute and chronic myeloid leukemia
  JOURNAL   Int J Cancer 106 (2), 224-231 (2003)
   PUBMED   12800198
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Resto,V.A., Caballero,O.L., Buta,M.R., Westra,W.H., Wu,L.,
            Westendorf,J.M., Jen,J., Hieter,P. and Sidransky,D.
  TITLE     A putative oncogenic role for MPP11 in head and neck squamous cell
            cancer
  JOURNAL   Cancer Res 60 (19), 5529-5535 (2000)
   PUBMED   11034098
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Matsumoto-Taniura,N., Pirollet,F., Monroe,R., Gerace,L. and
            Westendorf,J.M.
  TITLE     Identification of novel M phase phosphoproteins by expression
            cloning
  JOURNAL   Mol Biol Cell 7 (9), 1455-1469 (1996)
   PUBMED   8885239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA272314.1, DA691752.1,
            BC012376.1, AI621015.1, BC000859.1, X98260.1 and AI140595.1.
            
            Summary: This gene is a member of the M-phase phosphoprotein (MPP)
            family. The gene encodes a phosphoprotein with a J domain and a Myb
            DNA-binding domain which localizes to both the nucleus and the
            cytosol. The protein is capable of forming a heterodimeric complex
            that associates with ribosomes, acting as a molecular chaperone for
            nascent polypeptide chains as they exit the ribosome. This protein
            was identified as a leukemia-associated antigen and expression of
            the gene is upregulated in leukemic blasts. Also, chromosomal
            aberrations involving this gene are associated with primary head
            and neck squamous cell tumors. This gene has a pseudogene on
            chromosome 6. Alternatively spliced variants which encode different
            protein isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1166810.1,
                                           SRR1803614.23994.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379263.8/ ENSP00000368565.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..621
                     /product="dnaJ homolog subfamily C member 2 isoform 1"
                     /note="M-phase phosphoprotein 11; dnaJ homolog subfamily C
                     member 2; zuotin-related factor 1; DnaJ (Hsp40) homolog,
                     subfamily C, member 2"
                     /calculated_mol_wt=71866
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99543.4)"
     Region          13..49
                     /region_name="zuotin_NTD"
                     /note="N-terminal domain of fungal ribosome associated
                     J-protein zuotin and similar proteins; cd23953"
                     /db_xref="CDD:467935"
     Region          23..31
                     /region_name="Epitope (recognized by CD8(+) cytotoxic
                     T-lymphocytes)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99543.4)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99543.4)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99543.4)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q99543.4)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q99543.4)"
     Region          75..368
                     /region_name="ZUO1"
                     /note="Ribosome-associated chaperone zuotin [Translation,
                     ribosomal structure and biogenesis / Posttranslational
                     modification, protein turnover, chaperones]; COG5269"
                     /db_xref="CDD:227594"
     Region          160..250
                     /region_name="ZRF1-UBD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99543.4)"
     Region          294..315
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99543.4)"
     Region          344..420
                     /region_name="RAC_head"
                     /note="Ribosome-associated complex head domain; pfam16717"
                     /db_xref="CDD:435537"
     Region          426..453
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99543.4)"
     Region          453..506
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(454,494..495,497..498,500..502,504..506)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     Region          553..600
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cd00167"
                     /db_xref="CDD:238096"
     Site            order(554,587..588,590..591,593..595,597..599)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238096"
     CDS             1..621
                     /gene="DNAJC2"
                     /gene_synonym="MPHOSPH11; MPP11; ZRF1; ZUO1"
                     /coded_by="NM_014377.3:146..2011"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43628.1"
                     /db_xref="GeneID:27000"
                     /db_xref="HGNC:HGNC:13192"
                     /db_xref="MIM:605502"
ORIGIN      
        1 mlllpsaadg rgtaithalt sastlcqvep vgrwfeafvk rrnrnasasf qeledkkels
       61 eesedeelql eefpmlktld pkdwknqdhy avlglghvry katqrqikaa hkamvlkhhp
      121 dkrkaagepi kegdndyftc itkayemlsd pvkrrafnsv dptfdnsvps kseakdnffe
      181 vftpvferns rwsnkknvpk lgdmnssfed vdifysfwyn fdswrefsyl deeekekaec
      241 rderrwiekq nratraqrkk eemnrirtlv dnayscdpri kkfkeeekak keaekkakae
      301 akrkeqeake kqrqaeleaa rlakekeeee vrqqallakk ekdiqkkaik kerqklrnsc
      361 ktwnhfsdne aervkmmeev eklcdrlela slqclnetlt sctkevgkaa lekqieeine
      421 qirkekeeae armrqasknt ekstggggng sknwseddlq llikavnlfp agtnsrwevi
      481 anymnihsss gvkrtakdvi gkakslqkld phqkddinkk afdkfkkehg vvpqadnatp
      541 serfegpytd ftpwtteeqk lleqalktyp vntperweki aeavpgrtkk dcmkrykelv
      601 emvkakkaaq eqvlnasrak k
//
LOCUS       NP_001300952             122 aa            linear   PRI 20-NOV-2025
DEFINITION  endoribonuclease YbeY isoform 4 [Homo sapiens].
ACCESSION   NP_001300952
VERSION     NP_001300952.1
DBSOURCE    REFSEQ: accession NM_001314023.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 122)
  AUTHORS   D'Souza,A.R., Van Haute,L., Powell,C.A., Mutti,C.D., Palenikova,P.,
            Rebelo-Guiomar,P., Rorbach,J. and Minczuk,M.
  TITLE     YbeY is required for ribosome small subunit assembly and tRNA
            processing in human mitochondria
  JOURNAL   Nucleic Acids Res 49 (10), 5798-5812 (2021)
   PUBMED   34037799
  REMARK    GeneRIF: YbeY is required for ribosome small subunit assembly and
            tRNA processing in human mitochondria.
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Liao,Z., Schelcher,C. and Smirnov,A.
  TITLE     YbeY, eminence grise of ribosome biogenesis
  JOURNAL   Biochem Soc Trans 49 (2), 727-745 (2021)
   PUBMED   33929506
  REMARK    GeneRIF: YbeY, eminence grise of ribosome biogenesis.
            Review article
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Ghosal,A., Kohrer,C., Babu,V.M.P., Yamanaka,K., Davies,B.W.,
            Jacob,A.I., Ferullo,D.J., Gruber,C.C., Vercruysse,M. and
            Walker,G.C.
  TITLE     C21orf57 is a human homologue of bacterial YbeY proteins
  JOURNAL   Biochem Biophys Res Commun 484 (3), 612-617 (2017)
   PUBMED   28153719
  REMARK    GeneRIF: This observation suggests that the function of HuYbeY in
            human cells is likely regulated through specific interactions with
            partner proteins similarly to the way YbeY is regulated in
            bacteria.
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Uhlen,M., Oksvold,P., Algenas,C., Hamsten,C., Fagerberg,L.,
            Klevebring,D., Lundberg,E., Odeberg,J., Ponten,F., Kondo,T. and
            Sivertsson,A.
  TITLE     Antibody-based protein profiling of the human chromosome 21
  JOURNAL   Mol Cell Proteomics 11 (3), M111.013458 (2012)
   PUBMED   22042635
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Reymond,A., Friedli,M., Henrichsen,C.N., Chapot,F., Deutsch,S.,
            Ucla,C., Rossier,C., Lyle,R., Guipponi,M. and Antonarakis,S.E.
  TITLE     From PREDs and open reading frames to cDNA isolation: revisiting
            the human chromosome 21 transcription map
  JOURNAL   Genomics 78 (1-2), 46-54 (2001)
   PUBMED   11707072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC384882.1, AY040875.1 and
            AP000471.2.
            
            Summary: This gene encodes a highly conserved metalloprotein. A
            similar protein in bacteria acts as an endoribonuclease, and is
            thought to function in ribosomal RNA maturation and ribosome
            assembly. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 5' coding region, compared
            to variant 1. The encoded isoform (4) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY040875.1, W84414.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..122
                     /product="endoribonuclease YbeY isoform 4"
                     /note="putative metalloprotease C21orf57; rRNA maturation
                     factor homolog; putative ribonuclease; endoribonuclease
                     YbeY; ybeY metallopeptidase (putative)"
                     /calculated_mol_wt=13835
     Region          <29..104
                     /region_name="PRK13963"
                     /note="rRNA maturation RNase YbeY; cl46897"
                     /db_xref="CDD:481237"
     CDS             1..122
                     /gene="YBEY"
                     /gene_synonym="C21orf57"
                     /coded_by="NM_001314023.2:119..487"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82685.1"
                     /db_xref="GeneID:54059"
                     /db_xref="HGNC:HGNC:1299"
                     /db_xref="MIM:617461"
ORIGIN      
        1 mslvirnlqr vipirraplr skieihlkag efpqpdfpdd ynlgdiflgv eyifhqcken
       61 edyndvltvt athglchllg fthgteaewq qmfqkekavl delgrrtgtr lqpltrglfg
      121 gs
//
LOCUS       NP_004433                987 aa            linear   PRI 20-NOV-2025
DEFINITION  ephrin type-B receptor 2 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_004433
VERSION     NP_004433.2
DBSOURCE    REFSEQ: accession NM_004442.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Overman,R.C., Debreczeni,J.E., Truman,C.M., McAlister,M.S. and
            Attwood,T.K.
  TITLE     Completing the structural family portrait of the human EphB
            tyrosine kinase domains
  JOURNAL   Protein Sci 23 (5), 627-638 (2014)
   PUBMED   24677421
  REMARK    GeneRIF: Comparative crystalisation analysis of the human EphB
            family kinases has yielded new crystal forms of the human EphB2 and
            EphB4 catalytic domains.
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Badzioch,M., Eeles,R., Leblanc,G., Foulkes,W.D., Giles,G.,
            Edwards,S., Goldgar,D., Hopper,J.L., Bishop,D.T., Moller,P.,
            Heimdal,K., Easton,D. and Simard,J.
  TITLE     Suggestive evidence for a site specific prostate cancer gene on
            chromosome 1p36. The CRC/BPG UK Familial Prostate Cancer Study
            Coordinators and Collaborators. The EU Biomed Collaborators
  JOURNAL   J Med Genet 37 (12), 947-949 (2000)
   PUBMED   11186936
REFERENCE   4  (residues 1 to 987)
  AUTHORS   Gibbs,M., Stanford,J.L., McIndoe,R.A., Jarvik,G.P., Kolb,S.,
            Goode,E.L., Chakrabarti,L., Schuster,E.F., Buckley,V.A.,
            Miller,E.L., Brandzel,S., Li,S., Hood,L. and Ostrander,E.A.
  TITLE     Evidence for a rare prostate cancer-susceptibility locus at
            chromosome 1p36
  JOURNAL   Am J Hum Genet 64 (3), 776-787 (1999)
   PUBMED   10053012
REFERENCE   5  (residues 1 to 987)
  AUTHORS   Tang,X.X., Pleasure,D.E., Brodeur,G.M. and Ikegaki,N.
  TITLE     A variant transcript encoding an isoform of the human protein
            tyrosine kinase EPHB2 is generated by alternative splicing and
            alternative use of polyadenylation signals
  JOURNAL   Oncogene 17 (4), 521-526 (1998)
   PUBMED   9696046
REFERENCE   6  (residues 1 to 987)
  AUTHORS   Saito,T., Seki,N., Matsuda,Y., Kitahara,M., Murata,M., Kanda,N.,
            Nomura,N., Yamamoto,T. and Hori,T.A.
  TITLE     Identification of the human ERK gene as a putative receptor
            tyrosine kinase and its chromosomal localization to 1p36.1: a
            comparative mapping of human, mouse, and rat chromosomes
  JOURNAL   Genomics 26 (2), 382-384 (1995)
   PUBMED   7601466
REFERENCE   7  (residues 1 to 987)
  AUTHORS   Fox,G.M., Holst,P.L., Chute,H.T., Lindberg,R.A., Janssen,A.M.,
            Basu,R. and Welcher,A.A.
  TITLE     cDNA cloning and tissue distribution of five human EPH-like
            receptor protein-tyrosine kinases
  JOURNAL   Oncogene 10 (5), 897-905 (1995)
   PUBMED   7898931
REFERENCE   8  (residues 1 to 987)
  AUTHORS   Kiyokawa,E., Takai,S., Tanaka,M., Iwase,T., Suzuki,M., Xiang,Y.Y.,
            Naito,Y., Yamada,K., Sugimura,H. and Kino,I.
  TITLE     Overexpression of ERK, an EPH family receptor protein tyrosine
            kinase, in various human tumors
  JOURNAL   Cancer Res 54 (14), 3645-3650 (1994)
   PUBMED   8033077
REFERENCE   9  (residues 1 to 987)
  AUTHORS   Iwase,T., Tanaka,M., Suzuki,M., Naito,Y., Sugimura,H. and Kino,I.
  TITLE     Identification of protein-tyrosine kinase genes preferentially
            expressed in embryo stomach and gastric cancer
  JOURNAL   Biochem Biophys Res Commun 194 (2), 698-705 (1993)
   PUBMED   7688222
REFERENCE   10 (residues 1 to 987)
  AUTHORS   Chan,J. and Watt,V.M.
  TITLE     eek and erk, new members of the eph subclass of receptor
            protein-tyrosine kinases
  JOURNAL   Oncogene 6 (6), 1057-1061 (1991)
   PUBMED   1648701
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB282024.1, BC067861.1,
            L41939.2, AL035704.9 and AK025975.1.
            
            On Jun 12, 2002 this sequence version replaced NP_004433.1.
            
            Summary: This gene encodes a member of the Eph receptor family of
            receptor tyrosine kinase transmembrane glycoproteins. These
            receptors are composed of an N-terminal glycosylated ligand-binding
            domain, a transmembrane region and an intracellular kinase domain.
            They bind ligands called ephrins and are involved in diverse
            cellular processes including motility, division, and
            differentiation. A distinguishing characteristic of Eph-ephrin
            signaling is that both receptors and ligands are competent to
            transduce a signaling cascade, resulting in bidirectional
            signaling. This protein belongs to a subgroup of the Eph receptors
            called EphB. Proteins of this subgroup are distinguished from other
            members of the family by sequence homology and preferential binding
            affinity for membrane-bound ephrin-B ligands. Allelic variants are
            associated with prostate and brain cancer susceptibility.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2015].
            
            Transcript Variant: This variant (2) represents the longest
            transcript. It encodes isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L41939.2, SRR14038194.957048.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.12"
     Protein         1..987
                     /product="ephrin type-B receptor 2 isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="elk-related tyrosine kinase; ephrin type-B receptor
                     2; protein-tyrosine kinase HEK5; eph tyrosine kinase 3;
                     EPH-like kinase 5; tyrosine-protein kinase TYRO5; renal
                     carcinoma antigen NY-REN-47; tyrosine-protein kinase
                     receptor EPH-3; developmentally-regulated Eph-related
                     tyrosine kinase"
                     /calculated_mol_wt=107470
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2579
     Region          19..196
                     /region_name="EphR_LBD_B2"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 2;
                     cd10477"
                     /db_xref="CDD:198445"
     Site            order(28..30,32,44..47,49,53,55,57,60,93..95,99,101,147,
                     149..156,158..159,184,186,188)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198445"
     Site            265
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(325,400,415)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          326..421
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            336
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(416,418,420..421)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(436,500,515)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          437..520
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            482
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            order(516..517,519..520)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            535..536
                     /site_type="cleavage"
                     /note="Cleavage, by a metalloproteinase.
                     /evidence=ECO:0000250|UniProtKB:P54763; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Region          544..618
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Site            544..564
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29323.5)"
     Site            561..562
                     /site_type="cleavage"
                     /note="Cleavage, by gamma-secretase/PS1.
                     /evidence=ECO:0000250|UniProtKB:P54763; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Region          617..885
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(628..632,636,652,654,700..701,703,707,747,751..752,
                     754,765,786..790,799,833)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(628..630,632,636,652,654,700..701,703,707,752,754,
                     765)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(747,751,786..790,799,833)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            764..792
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          911..981
                     /region_name="SAM_EPH-B2"
                     /note="SAM domain of EPH-B2 subfamily of tyrosine kinase
                     receptors; cd09552"
                     /db_xref="CDD:188951"
     Site            order(913..914,916,938,944..945,953,961..964,966..967,975,
                     979)
                     /site_type="other"
                     /note="homooligomer interface [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(913,916,922,943,971,974..975)
                     /site_type="other"
                     /note="putative homodimer interface (head-to-head)
                     [polypeptide binding]"
                     /db_xref="CDD:188951"
     Site            order(931,964)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188951"
     Site            order(947..952,955,973,976,979..980)
                     /site_type="other"
                     /note="homodimer interface (tail-to-tail) [polypeptide
                     binding]"
                     /db_xref="CDD:188951"
     Site            984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     Site            985
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29323.5)"
     CDS             1..987
                     /gene="EPHB2"
                     /gene_synonym="BDPLT22; CAPB; DRT; EK5; EPHT3; ERK; Hek5;
                     PCBC; Tyro5"
                     /coded_by="NM_004442.7:146..3109"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS230.1"
                     /db_xref="GeneID:2048"
                     /db_xref="HGNC:HGNC:3393"
                     /db_xref="MIM:600997"
ORIGIN      
        1 malrrlgaal lllpllaave etlmdsttat aelgwmvhpp sgweevsgyd enmntirtyq
       61 vcnvfessqn nwlrtkfirr rgahrihvem kfsvrdcssi psvpgscket fnlyyyeadf
      121 dsatktfpnw menpwvkvdt iaadesfsqv dlggrvmkin tevrsfgpvs rsgfylafqd
      181 yggcmsliav rvfyrkcpri iqngaifqet lsgaestslv aargsciana eevdvpikly
      241 cngdgewlvp igrcmckagf eavengtvcr gcpsgtfkan qgdeacthcp insrttsega
      301 tncvcrngyy radldpldmp cttipsapqa vissvnetsl mlewtpprds ggredlvyni
      361 ickscgsgrg actrcgdnvq yaprqlglte priyisdlla htqytfeiqa vngvtdqspf
      421 spqfasvnit tnqaapsavs imhqvsrtvd sitlswsqpd qpngvildye lqyyekelse
      481 ynataikspt ntvtvqglka gaiyvfqvra rtvagygrys gkmyfqtmte aeyqtsiqek
      541 lpliigssaa glvfliavvv iaivcnrrrg feradseytd klqhytsghm tpgmkiyidp
      601 ftyedpneav refakeidis cvkieqviga gefgevcsgh lklpgkreif vaiktlksgy
      661 tekqrrdfls easimgqfdh pnvihlegvv tkstpvmiit efmengslds flrqndgqft
      721 viqlvgmlrg iaagmkylad mnyvhrdlaa rnilvnsnlv ckvsdfglsr fleddtsdpt
      781 ytsalggkip irwtapeaiq yrkftsasdv wsygivmwev msygerpywd mtnqdvinai
      841 eqdyrlpppm dcpsalhqlm ldcwqkdrnh rpkfgqivnt ldkmirnpns lkamaplssg
      901 inlplldrti pdytsfntvd ewleaikmgq ykesfanagf tsfdvvsqmm medilrvgvt
      961 laghqkkiln siqvmraqmn qiqsvev
//
LOCUS       NP_036430               1119 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-associated NEDD8-dissociated protein 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_036430 XP_371617 XP_945952
VERSION     NP_036430.1
DBSOURCE    REFSEQ: accession NM_012298.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Gorska,A.A., Sandmann,C., Riechert,E., Hofmann,C., Malovrh,E.,
            Varma,E., Kmietczyk,V., Olschlager,J., Jurgensen,L.,
            Kamuf-Schenk,V., Stroh,C., Furkel,J., Konstandin,M.H., Sticht,C.,
            Boileau,E., Dieterich,C., Frey,N., Katus,H.A., Doroudgar,S. and
            Volkers,M.
  TITLE     Muscle-specific Cand2 is translationally upregulated by mTORC1 and
            promotes adverse cardiac remodeling
  JOURNAL   EMBO Rep 22 (12), e52170 (2021)
   PUBMED   34605609
  REMARK    GeneRIF: Muscle-specific Cand2 is translationally upregulated by
            mTORC1 and promotes adverse cardiac remodeling.
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Dong,S.S., Yao,S., Chen,Y.X., Guo,Y., Zhang,Y.J., Niu,H.M.,
            Hao,R.H., Shen,H., Tian,Q., Deng,H.W. and Yang,T.L.
  TITLE     Detecting epistasis within chromatin regulatory circuitry reveals
            CAND2 as a novel susceptibility gene for obesity
  JOURNAL   Int J Obes (Lond) 43 (3), 450-456 (2019)
   PUBMED   29717274
  REMARK    GeneRIF: The work developed the tool and performed 'interaction
            analyses within chromatin regulatory circuitry' (IACRC); analysis
            found CAND2 may be a novel obesity susceptibility gene.
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Wei,T., Song,J., Xu,M., Lv,L., Liu,C., Shen,J. and Huang,Y.
  TITLE     NEURL rs6584555 and CAND2 rs4642101 contribute to postoperative
            atrial fibrillation: a prospective study among Chinese population
  JOURNAL   Oncotarget 7 (27), 42617-42624 (2016)
   PUBMED   27203392
  REMARK    GeneRIF: NEURL rs12415501 and CAND2 rs4642101 are significantly
            associated with postoperative atrial fibrillation susceptibility
            after coronary artery bypass grafting among Chinese population
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Shyy,W., Dietz,F., Dobbs,M.B., Sheffield,V.C. and Morcuende,J.A.
  TITLE     Evaluation of CAND2 and WNT7a as candidate genes for congenital
            idiopathic clubfoot
  JOURNAL   Clin Orthop Relat Res 467 (5), 1201-1205 (2009)
   PUBMED   19159115
  REMARK    GeneRIF: Based on these results it is unlikely CAND2 and WNT7a are
            the major genes that causes clubfoot.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Muzny,D.M., Scherer,S.E., Kaul,R., Wang,J., Yu,J., Sudbrak,R.,
            Buhay,C.J., Chen,R., Cree,A., Ding,Y., Dugan-Rocha,S., Gill,R.,
            Gunaratne,P., Harris,R.A., Hawes,A.C., Hernandez,J., Hodgson,A.V.,
            Hume,J., Jackson,A., Khan,Z.M., Kovar-Smith,C., Lewis,L.R.,
            Lozado,R.J., Metzker,M.L., Milosavljevic,A., Miner,G.R.,
            Morgan,M.B., Nazareth,L.V., Scott,G., Sodergren,E., Song,X.Z.,
            Steffen,D., Wei,S., Wheeler,D.A., Wright,M.W., Worley,K.C.,
            Yuan,Y., Zhang,Z., Adams,C.Q., Ansari-Lari,M.A., Ayele,M.,
            Brown,M.J., Chen,G., Chen,Z., Clendenning,J.,
            Clerc-Blankenburg,K.P., Chen,R., Chen,Z., Davis,C., Delgado,O.,
            Dinh,H.H., Dong,W., Draper,H., Ernst,S., Fu,G.,
            Gonzalez-Garay,M.L., Garcia,D.K., Gillett,W., Gu,J., Hao,B.,
            Haugen,E., Havlak,P., He,X., Hennig,S., Hu,S., Huang,W.,
            Jackson,L.R., Jacob,L.S., Kelly,S.H., Kube,M., Levy,R., Li,Z.,
            Liu,B., Liu,J., Liu,W., Lu,J., Maheshwari,M., Nguyen,B.V.,
            Okwuonu,G.O., Palmeiri,A., Pasternak,S., Perez,L.M., Phelps,K.A.,
            Plopper,F.J., Qiang,B., Raymond,C., Rodriguez,R.,
            Saenphimmachak,C., Santibanez,J., Shen,H., Shen,Y., Subramanian,S.,
            Tabor,P.E., Verduzco,D., Waldron,L., Wang,J., Wang,J., Wang,Q.,
            Williams,G.A., Wong,G.K., Yao,Z., Zhang,J., Zhang,X., Zhao,G.,
            Zhou,J., Zhou,Y., Nelson,D., Lehrach,H., Reinhardt,R., Naylor,S.L.,
            Yang,H., Olson,M., Weinstock,G. and Gibbs,R.A.
  TITLE     The DNA sequence, annotation and analysis of human chromosome 3
  JOURNAL   Nature 440 (7088), 1194-1198 (2006)
   PUBMED   16641997
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   You,J., Wang,M., Aoki,T., Tamura,T.A. and Pickart,C.M.
  TITLE     Proteolytic targeting of transcriptional regulator TIP120B by a
            HECT domain E3 ligase
  JOURNAL   J Biol Chem 278 (26), 23369-23375 (2003)
   PUBMED   12692129
  REMARK    GeneRIF: TIP120B is a specific substrate of KIAA10; both are highly
            expressed in human skeletal muscle, suggesting that KIAA10 may
            regulate TIP120B homeostasis specifically in this tissue.
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TIP120B was induced in C2C12 myoblasts when these cells
            differentiated into myotubes (TIP120B).
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Aoki,T., Okada,N., Ishida,M., Yogosawa,S., Makino,Y. and
            Tamura,T.A.
  TITLE     TIP120B: a novel TIP120-family protein that is expressed
            specifically in muscle tissues
  JOURNAL   Biochem Biophys Res Commun 261 (3), 911-916 (1999)
   PUBMED   10441524
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR001490.1, BC136592.1, BX502783.1, AB014567.1 and W44800.1.
            
            On or before Sep 20, 2006 this sequence version replaced
            XP_371617.2, XP_945952.1.
            
            Transcript Variant: This variant (2) is missing two in-frame coding
            exons, and uses an alternate in-frame acceptor splice site at one
            of the coding exons, compared to variant 1. This results in a
            shorter isoform (2) lacking two internal protein segments compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB014567.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2148093,
                                           SAMEA2148874 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.2"
     Protein         1..1119
                     /product="cullin-associated NEDD8-dissociated protein 2
                     isoform 2"
                     /note="TBP interacting protein; cullin-associated
                     NEDD8-dissociated protein 2; epididymis tissue protein Li
                     169; p120 CAND2; TBP-interacting protein 120B;
                     TBP-interacting protein of 120 kDa B; cullin-associated
                     and neddylation-dissociated protein 2; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=122533
     Region          2..39
                     /region_name="HEAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75155.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.3,
                     ECO:0000269|Ref.4; propagated from UniProtKB/Swiss-Prot
                     (O75155.3)"
     Region          8..33
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(25..26,29,32..33,66..67,70,73,100..101,104,107..108,
                     111,138..139,142,145..146,183..184,187,190..191)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          49..73
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          82..112
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          121..146
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          163..192
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          <341..864
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          701..725
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(717..718,721,724..725,748..749,752,755..756,759,
                     786..787,790,793..794,797,822..823,826,830..831,861..862,
                     865,868..869)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          768..798
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          802..831
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          841..870
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          941..1090
                     /region_name="TIP120"
                     /note="TATA-binding protein interacting (TIP20);
                     pfam08623"
                     /db_xref="CDD:430111"
     CDS             1..1119
                     /gene="CAND2"
                     /gene_synonym="TIP120B; Tp120b"
                     /coded_by="NM_012298.3:42..3401"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43053.1"
                     /db_xref="GeneID:23066"
                     /db_xref="HGNC:HGNC:30689"
                     /db_xref="MIM:610403"
ORIGIN      
        1 mstaafhiss llekmtssdk dfrfmatsdl mselqkdsiq ldedserkvv kmllrlledk
       61 ngevqnlavk wlgvplgafh asllhcllpq lssprlavrk ravgalghla aacstdlfve
      121 ladhlldrlp gprvptspta irtliqclgs vgrqaghrlg ahldrlvplv edfcnlddde
      181 lresclqafe aflrkcpkem gphvpnvtsl clqyikhdpn ynydsdedee qmetedsefs
      241 eqesedeysd dddmswkvrr aaakciaali ssrpdllpdf hctlapvlir rfkereenvk
      301 advftayivl lrqtqppkgw leameeptqt gsnlhmlrgq vplvvkalqr qlkdrsvrar
      361 qgcfslltel agvlpgslae hmpvlvsgii fsladrssss tirmdalafl qgllgtepae
      421 afhphlpill ppvmacvads fykiaaealv vlqelvralw plhrprmldp epyvgemsav
      481 tlarlratdl dqevkerais cmghlvghlg drlgddlept llllldrlrn eitrlpaika
      541 ltlvavsplq ldlqpilaea lhilasflrk nqralrlatl aaldalaqsq glslppsavq
      601 avlaelpalv nesdmhvaql avdflatvtq aqpaslvevs gpvlsellrl lrspllpagv
      661 laaaegflqa lvgtrppcvd yaklisllta pvyeqavdgg pglhkqvfhs larcvaalsa
      721 acpqeaasta srlvcdarsp hsstgvkvla flslaevgqv agpghqrelk avllealgsp
      781 sedvraaasy algrvgagsl pdflpflleq ieaeprrqyl llhslrealg aaqpdslkpy
      841 aediwallfq rcegaeegtr gvvaecigkl vlvnpsfllp rlrkqlaagr phtrstvita
      901 vkflisdqph pidpllksfi avhnkpslvr dllddilpll yqetkirrdl irevemgpfk
      961 htvddgldvr kaafecmysl lesclgqldi ceflnhvedg lkdhydirml tfimvarlat
     1021 lcpapvlqrv drlieplrat ctakvkagsv kqefekqdel krsamravaa lltipevgks
     1081 pimadfssqi rsnpelaalf esiqkdsasa pstdsmels
//
LOCUS       NP_001245145             635 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-2 isoform d precursor [Homo
            sapiens].
ACCESSION   NP_001245145
VERSION     NP_001245145.1
DBSOURCE    REFSEQ: accession NM_001258216.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Zare,M., Hesampour,F., Poordast,T., Valibeigi,M., Enayatmehri,M.,
            Ahmadi,S., Nasri,F. and Gharesi-Fard,B.
  TITLE     Association between gene polymorphisms of IL-12, IL-12 receptor and
            IL-27 and organ involvement in Iranian endometriosis patients
  JOURNAL   Int J Immunogenet 50 (1), 24-33 (2023)
   PUBMED   36328955
  REMARK    GeneRIF: Association between gene polymorphisms of IL-12, IL-12
            receptor and IL-27 and organ involvement in Iranian endometriosis
            patients.
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Fu,Y., Liu,L. and Wu,H.
  TITLE     Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic Obstructive
            Pulmonary Disease
  JOURNAL   Int J Chron Obstruct Pulmon Dis 17, 1671-1683 (2022)
   PUBMED   35923356
  REMARK    GeneRIF: Role of Genetic Polymorphisms in IL12Rbeta2 in Chronic
            Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Ye,C., Yano,H., Workman,C.J. and Vignali,D.A.A.
  TITLE     Interleukin-35: Structure, Function and Its Impact on
            Immune-Related Diseases
  JOURNAL   J Interferon Cytokine Res 41 (11), 391-406 (2021)
   PUBMED   34788131
  REMARK    Review article
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Wang,X., Zhou,S., Fan,M., Wang,P., Fang,H., Bian,F., Huang,T. and
            Du,X.
  TITLE     Expressions of IL-12 and its receptors in patients with lumbar disc
            herniation and their relationship with clinical efficacy
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 66 (7), 5-11 (2020)
   PUBMED   33287915
  REMARK    GeneRIF: Expressions of IL-12 and its receptors in patients with
            lumbar disc herniation and their relationship with clinical
            efficacy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 635)
  AUTHORS   Rogge,L., Barberis-Maino,L., Biffi,M., Passini,N., Presky,D.H.,
            Gubler,U. and Sinigaglia,F.
  TITLE     Selective expression of an interleukin-12 receptor component by
            human T helper 1 cells
  JOURNAL   J Exp Med 185 (5), 825-831 (1997)
   PUBMED   9120388
REFERENCE   7  (residues 1 to 635)
  AUTHORS   Presky,D.H., Yang,H., Minetti,L.J., Chua,A.O., Nabavi,N., Wu,C.Y.,
            Gately,M.K. and Gubler,U.
  TITLE     A functional interleukin 12 receptor complex is composed of two
            beta-type cytokine receptor subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (24), 14002-14007 (1996)
   PUBMED   8943050
REFERENCE   8  (residues 1 to 635)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   9  (residues 1 to 635)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   10 (residues 1 to 635)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB126833.1, U64198.1,
            AL389925.10, BC143250.1 and AL358512.9.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein identified as a subunit of the interleukin 12 receptor
            complex. The coexpression of this and IL12RB1 proteins was shown to
            lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. The expression of this
            gene is up-regulated by interferon gamma in Th1 cells, and plays a
            role in Th1 cell differentiation. The up-regulation of this gene is
            found to be associated with a number of infectious diseases, such
            as Crohn's disease and leprosy, which is thought to contribute to
            the inflammatory response and host defense. Several transcript
            variants encoding different isoforms and non-protein coding
            transcripts have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Transcript Variant: This variant (4) lacks two alternate coding
            exons compared to variant 1, that causes a frameshift. The
            resulting isoform (d) has a shorter and distinct C-terminus
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.56123.1,
                                           SRR1660809.51466.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..635
                     /product="interleukin-12 receptor subunit beta-2 isoform d
                     precursor"
                     /note="interleukin-12 receptor beta-2 chain; IL-12R
                     subunit beta-2; IL-12 receptor subunit beta-2; interleukin
                     12 receptor, beta 2"
                     /calculated_mol_wt=68578
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3099
     mat_peptide     24..635
                     /product="interleukin-12 receptor subunit beta-2 isoform
                     d"
                     /calculated_mol_wt=69006
     Region          28..110
                     /region_name="Lep_receptor_Ig"
                     /note="Ig-like C2-type domain; pfam06328"
                     /db_xref="CDD:461878"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          224..316
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(224,286,304)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          305..309
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(305..306,308..309)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          <368..>608
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Region          423..511
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            480
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q99665.1)"
     Site            order(507..508,510..511)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     CDS             1..635
                     /gene="IL12RB2"
                     /coded_by="NM_001258216.1:641..2548"
                     /note="isoform d precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS72805.1"
                     /db_xref="GeneID:3595"
                     /db_xref="HGNC:HGNC:5972"
                     /db_xref="MIM:601642"
ORIGIN      
        1 mahtfrgcsl afmfiitwll ikakidackr gdvtvkpshv illgstvnit cslkprqgcf
       61 hysrrnklil ykfdrrinfh hghslnsqvt glplgttlfv cklacinsde iqicgaeifv
      121 gvapeqpqnl sciqkgeqgt vactwergrd thlyteytlq lsgpknltwq kqckdiycdy
      181 ldfginltpe spesnftakv tavnslgsss slpstftfld ivrplppwdi rikfqkasvs
      241 rctlywrdeg lvllnrlryr psnsrlwnmv nvtkakgrhd lldlkpftey efqissklhl
      301 ykgswsdwse slraqtpeee ptgmldvwym krhidysrqq islfwknlsv seargkilhy
      361 qvtlqeltgg kamtqnitgh tswttviprt gnwavavsaa nskgsslptr inimnlceag
      421 llaprqvsan segmdnilvt wqpprkdpsa vqeyvvewre lhpggdtqvp lnwlrsrpyn
      481 vsalisenik syicyeirvy alsgdqggcs silgnskhka plsgphinai teekgsilis
      541 wnsipvqeqm gcllhyriyw kerdsnsqpq lceipyrvsq nshpinslqp rvtyvlwmta
      601 ltaagesshg nerefclqge dtaalgqapd rlaha
//
LOCUS       NP_005888                584 aa            linear   PRI 20-NOV-2025
DEFINITION  actin-binding protein IPP isoform 1 [Homo sapiens].
ACCESSION   NP_005888
VERSION     NP_005888.1
DBSOURCE    REFSEQ: accession NM_005897.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Nikou,S., Arbi,M., Dimitrakopoulos,F.D., Sirinian,C., Chadla,P.,
            Pappa,I., Ntaliarda,G., Stathopoulos,G.T., Papadaki,H., Zolota,V.,
            Lygerou,Z., Kalofonos,H.P. and Bravou,V.
  TITLE     Integrin-linked kinase (ILK) regulates KRAS, IPP complex and Ras
            suppressor-1 (RSU1) promoting lung adenocarcinoma progression and
            poor survival
  JOURNAL   J Mol Histol 51 (4), 385-400 (2020)
   PUBMED   32592097
  REMARK    GeneRIF: Integrin-linked kinase (ILK) regulates KRAS, IPP complex
            and Ras suppressor-1 (RSU1) promoting lung adenocarcinoma
            progression and poor survival.
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Kim,Y.C. and Cutler,M.L.
  TITLE     MicroRNA-Dependent Targeting of RSU1 and the IPP Adhesion Complex
            Regulates the PTEN/PI3K/AKT Signaling Pathway in Breast Cancer Cell
            Lines
  JOURNAL   Int J Mol Sci 21 (15), 5458 (2020)
   PUBMED   32751711
  REMARK    GeneRIF: MicroRNA-Dependent Targeting of RSU1 and the IPP Adhesion
            Complex Regulates the PTEN/PI3K/AKT Signaling Pathway in Breast
            Cancer Cell Lines.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 584)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 584)
  AUTHORS   VanHouten,J.N., Asch,H.L. and Asch,B.B.
  TITLE     Cloning and characterization of ectopically expressed transcripts
            for the actin-binding protein MIPP in mouse mammary carcinomas
  JOURNAL   Oncogene 20 (38), 5366-5372 (2001)
   PUBMED   11536049
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Kim,I.F., Mohammadi,E. and Huang,R.C.
  TITLE     Isolation and characterization of IPP, a novel human gene encoding
            an actin-binding, kelch-like protein
  JOURNAL   Gene 228 (1-2), 73-83 (1999)
   PUBMED   10072760
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Chang-Yeh,A., Jabs,E.W., Li,X., Dracopoli,N.C. and Huang,R.C.
  TITLE     The IPP gene is assigned to human chromosome 1p32-1p22
  JOURNAL   Genomics 15 (1), 239-241 (1993)
   PUBMED   8432546
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Chang-Yeh,A., Mold,D.E. and Huang,R.C.
  TITLE     Identification of a novel murine IAP-promoted placenta-expressed
            gene
  JOURNAL   Nucleic Acids Res 19 (13), 3667-3672 (1991)
   PUBMED   1906605
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Mold,D.E., Chang-Yeh,A. and Huang,R.C.
  TITLE     Cell lineage-specific expression of the MIPP gene
  JOURNAL   Biochem Biophys Res Commun 177 (3), 1062-1067 (1991)
   PUBMED   1905535
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA905423.1, AK023880.1 and
            AL604028.15.
            
            Summary: The protein encoded by this gene is a member of the kelch
            family of proteins, which is characterized by a 50 amino acid
            repeat which interacts with actin. Transcript variants have been
            described but their full-length nature has not been determined.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.179904.1,
                                           SRR1660805.199385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396478.4/ ENSP00000379739.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..584
                     /product="actin-binding protein IPP isoform 1"
                     /note="actin-binding protein IPP; kelch-like protein 27;
                     kelch-like family member 27"
                     /calculated_mol_wt=65130
     Region          17..141
                     /region_name="BTB_POZ_KLHL27_IPP"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in intracisternal
                     A particle-promoted polypeptide (IPP); cd18256"
                     /db_xref="CDD:349565"
     Region          30..575
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          289..343
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     Region          333..376
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          344..390
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     Region          380..424
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          391..437
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     Region          427..473
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          439..485
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     Region          475..520
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          487..533
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     Region          523..574
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          535..583
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y573.1)"
     CDS             1..584
                     /gene="IPP"
                     /gene_synonym="KLHL27"
                     /coded_by="NM_005897.3:108..1862"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30702.1"
                     /db_xref="GeneID:3652"
                     /db_xref="HGNC:HGNC:6108"
                     /db_xref="MIM:147485"
ORIGIN      
        1 manedcpkaa dspfssdkha qlilaqinkm rngqhfcdvq lqvgqesfka hrlvlaassp
       61 yfaalftggm kesskdvvpi lgieagifqi lldfiytgiv nigvnnvqel iiaadmlqlt
      121 evvhlccefl kgqidplnci gifqfseqia chdllefsen yihvhflevh sgeeflaltk
      181 dqlikilrse elsiedeyqv flaamqwilk dlgkrrkhvv evldpirfpl lppqrllkyi
      241 egvsdfnlrv alqtllkeyc evckspkenk fcsflqtskv rprkkarkyl yavggytrlq
      301 ggrwsdsral scverfdtfs qywttvsslh qarsglgvtv lggmvyaigg ekdsmifdct
      361 ecydpvtkqw ttvasmnhpr cglgvcvcyg aiyalggwvg aeigntierf dpdenkwevv
      421 gnmavsryyf gccemqgliy viggisnegi elrsfevydp lskrwsplpp mgtrraylgv
      481 aalndciysv ggwnetqdal htvekysfee ekwvevasmk vpragmcvva vngllyvsgg
      541 rssshdflap gtldsvevyn phsdtwteig nmitsrcegg vavl
//
LOCUS       NP_079202                554 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 56 isoform 1 [Homo sapiens].
ACCESSION   NP_079202
VERSION     NP_079202.2
DBSOURCE    REFSEQ: accession NM_024926.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 554)
  AUTHORS   David,O., Eskin-Schwartz,M., Ling,G., Dolgin,V., Kristal,E.,
            Benkowitz,E., Osyntsov,L., Gradstein,L., Birk,O.S., Loewenthal,N.
            and Yerushalmi,B.
  TITLE     Pituitary stalk interruption syndrome broadens the clinical
            spectrum of the TTC26 ciliopathy
  JOURNAL   Clin Genet 98 (3), 303-307 (2020)
   PUBMED   32617964
  REMARK    GeneRIF: Pituitary stalk interruption syndrome broadens the
            clinical spectrum of the TTC26 ciliopathy.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Shaheen,R., Alsahli,S., Ewida,N., Alzahrani,F., Shamseldin,H.E.,
            Patel,N., Al Qahtani,A., Alhebbi,H., Alhashem,A., Al-Sheddi,T.,
            Alomar,R., Alobeid,E., Abouelhoda,M., Monies,D., Al-Hussaini,A.,
            Alzouman,M.A., Shagrani,M., Faqeih,E. and Alkuraya,F.S.
  TITLE     Biallelic Mutations in Tetratricopeptide Repeat Domain 26
            (Intraflagellar Transport 56) Cause Severe Biliary Ciliopathy in
            Humans
  JOURNAL   Hepatology 71 (6), 2067-2079 (2020)
   PUBMED   31595528
  REMARK    GeneRIF: Biallelic Mutations in Tetratricopeptide Repeat Domain 26
            (Intraflagellar Transport 56) Cause Severe Biliary Ciliopathy in
            Humans.
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ishikawa,H., Ide,T., Yagi,T., Jiang,X., Hirono,M., Sasaki,H.,
            Yanagisawa,H., Wemmer,K.A., Stainier,D.Y., Qin,H., Kamiya,R. and
            Marshall,W.F.
  TITLE     TTC26/DYF13 is an intraflagellar transport protein required for
            transport of motility-related proteins into flagella
  JOURNAL   Elife 3, e01566 (2014)
   PUBMED   24596149
  REMARK    GeneRIF: TTC26 is an intraflagellar transport protein required for
            transport of motility-related proteins into flagella.
            Erratum:[Elife. 2014 Apr 01;3:e02897. doi: 10.7554/eLife.02897.
            PMID: 24692455]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP315162.1, BC126331.1, AC009220.10 and CA450032.1.
            
            On Jan 29, 2009 this sequence version replaced NP_079202.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022633.1, SRR1660803.248116.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000464848.5/ ENSP00000419279.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..554
                     /product="intraflagellar transport protein 56 isoform 1"
                     /note="tetratricopeptide repeat protein 26; TPR repeat
                     protein 26; intraflagellar transport protein 56;
                     tetratricopeptide repeat domain 26"
                     /calculated_mol_wt=64047
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AVF1.1)"
     Region          29..224
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          57..90
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AVF1.1)"
     Region          58..86
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          92..125
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AVF1.1)"
     Region          139..178
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          151..184
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AVF1.1)"
     Region          157..>331
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          184..214
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          219..247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          468..501
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (A0AVF1.1)"
     CDS             1..554
                     /gene="IFT56"
                     /gene_synonym="BRENS; dyf-13; DYF13; TTC26"
                     /coded_by="NM_024926.4:81..1745"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5852.1"
                     /db_xref="GeneID:79989"
                     /db_xref="HGNC:HGNC:21882"
                     /db_xref="MIM:617453"
ORIGIN      
        1 mmlsrakpav grgvqhtdkr kkkgrkipkl eellskrdft gaitllefkr hvgeeeedtn
       61 lwigycafhl gdykraleey enatkeencn sevwvnlact yfflgmykqa eaagfkasks
      121 rlqnrllfhl ahkfndekkl msfhqnlqdv tedqlslasi hymrshyqea idiykrilld
      181 nreylalnvy valcyykldy ydvsqevlav ylqqipdsti alnlkacnhf rlyngraaea
      241 elkslmdnas ssfefakeli rhnlvvfrgg egalqvlppl vdvipearln lviyylrqdd
      301 vqeaynlikd lepttpqeyi lkgvvnaalg qemgsrdhmk iaqqffqlvg gsasecdtip
      361 grqcmascff llkqfddvli ylnsfksyfy nddifnfnya qakaatgnts egeeaflliq
      421 sekmkndyiy lswlarcyim nkkprlawel ylkmetsges fsllqliand cykmgqfyys
      481 akafdvlerl dpnpeywegk rgacvgifqm iiagrepket lrevlhllrs tgntqveymi
      541 rimkkwaken rvsi
//
LOCUS       NP_003008                164 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine-rich splicing factor 3 [Homo sapiens].
ACCESSION   NP_003008
VERSION     NP_003008.1
DBSOURCE    REFSEQ: accession NM_003017.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Zhang,L., Zhang,H., Tang,Y., Dai,C. and Zheng,J.
  TITLE     SRSF3 suppresses RCC tumorigenesis and progression via regulating
            SP4 alternative splicing
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119841 (2024)
   PUBMED   39222664
  REMARK    GeneRIF: SRSF3 suppresses RCC tumorigenesis and progression via
            regulating SP4 alternative splicing.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Gao,H., Rocha,K.C.E., Jin,Z., Kumar,D., Zhang,D., Wang,K., Das,M.,
            Farrell,A., Truong,T., Tekin,Y., Jung,H.S., Kempf,J.,
            Webster,N.J.G. and Ying,W.
  TITLE     Restoring SRSF3 in Kupffer cells attenuates obesity-related insulin
            resistance
  JOURNAL   Hepatology 80 (2), 363-375 (2024)
   PUBMED   38456794
  REMARK    GeneRIF: Restoring SRSF3 in Kupffer cells attenuates
            obesity-related insulin resistance.
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Sue,S.H., Liu,S.T. and Huang,S.M.
  TITLE     Factors affecting the expression and stability of full-length and
            truncated SRSF3 proteins in human cancer cells
  JOURNAL   Sci Rep 14 (1), 14397 (2024)
   PUBMED   38909100
  REMARK    GeneRIF: Factors affecting the expression and stability of
            full-length and truncated SRSF3 proteins in human cancer cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 164)
  AUTHORS   More,D.A., Singh,N., Mishra,R., Muralidharan,H.P., Gopinath,K.S.,
            Gopal,C. and Kumar,A.
  TITLE     Intronic miR-6741-3p targets the oncogene SRSF3: Implications for
            oral squamous cell carcinoma pathogenesis
  JOURNAL   PLoS One 19 (5), e0296565 (2024)
   PUBMED   38781195
  REMARK    GeneRIF: Intronic miR-6741-3p targets the oncogene SRSF3:
            Implications for oral squamous cell carcinoma pathogenesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Caceres,J.F., Screaton,G.R. and Krainer,A.R.
  TITLE     A specific subset of SR proteins shuttles continuously between the
            nucleus and the cytoplasm
  JOURNAL   Genes Dev 12 (1), 55-66 (1998)
   PUBMED   9420331
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Zahler,A.M., Lane,W.S., Stolk,J.A. and Roth,M.B.
  TITLE     SR proteins: a conserved family of pre-mRNA splicing factors
  JOURNAL   Genes Dev 6 (5), 837-847 (1992)
   PUBMED   1577277
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Ayane,M., Preuss,U., Kohler,G. and Nielsen,P.J.
  TITLE     A differentially expressed murine RNA encoding a protein with
            similarities to two types of nucleic acid binding motifs
  JOURNAL   Nucleic Acids Res 19 (6), 1273-1278 (1991)
   PUBMED   2030943
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z85986.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/arginine (SR)-rich family of pre-mRNA splicing factors,
            which constitute part of the spliceosome. Each of these factors
            contains an RNA recognition motif (RRM) for binding RNA and an RS
            domain for binding other proteins. The RS domain is rich in serine
            and arginine residues and facilitates interaction between different
            SR splicing factors. In addition to being critical for mRNA
            splicing, the SR proteins have also been shown to be involved in
            mRNA export from the nucleus and in translation. Two transcript
            variants, one protein-coding and the other non-coding, have been
            found for this gene. [provided by RefSeq, Sep 2010].
            
            Transcript Variant: This variant (1) is the protein-coding variant.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.150012.1,
                                           SRR1803614.13020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373715.11/ ENSP00000362820.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31-p21.2"
     Protein         1..164
                     /product="serine/arginine-rich splicing factor 3"
                     /note="splicing factor, arginine/serine-rich 3; splicing
                     factor, arginine/serine-rich, 20-kD; pre-mRNA-splicing
                     factor SRP20; pre-mRNA splicing factor SRp20; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=19198
     Region          1..90
                     /region_name="Sufficient for interaction with NXF1 and
                     SRSP. /evidence=ECO:0000269|PubMed:12667464,
                     ECO:0000269|PubMed:17036044, ECO:0000269|PubMed:32440474"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Region          6..86
                     /region_name="RRM_SRSF3"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     serine/arginine-rich splicing factor 3 (SRSF3); cd12645"
                     /db_xref="CDD:241089"
     Site            23
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P84103.1)"
     Site            order(40,42..44,46,48,50,81,83)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:241089"
     Region          81..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     Region          119..164
                     /region_name="2 X approximate repeats, basic"
                     /note="propagated from UniProtKB/Swiss-Prot (P84103.1)"
     CDS             1..164
                     /gene="SRSF3"
                     /gene_synonym="SFRS3; SRp20"
                     /coded_by="NM_003017.5:123..617"
                     /db_xref="CCDS:CCDS4823.1"
                     /db_xref="GeneID:6428"
                     /db_xref="HGNC:HGNC:10785"
                     /db_xref="MIM:603364"
ORIGIN      
        1 mhrdscpldc kvyvgnlgnn gnkteleraf gyygplrsvw varnppgfaf vefedprdaa
       61 davreldgrt lcgcrvrvel sngekrsrnr gpppswgrrp rddyrrrspp prrrsprrrs
      121 fsrsrsrsls rdrrrersls rernhkpsrs fsrsrsrsrs nerk
//
LOCUS       NP_001357598             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001357598
VERSION     NP_001357598.1
DBSOURCE    REFSEQ: accession NM_001370669.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.163036.1,
                                           SRR1803616.74523.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001370669.1:326..1090"
                     /note="isoform j is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001315549             457 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 5
            isoform 3 [Homo sapiens].
ACCESSION   NP_001315549
VERSION     NP_001315549.1
DBSOURCE    REFSEQ: accession NM_001328620.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Song,A., Mao,Y. and Wei,H.
  TITLE     GLUT5: structure, functions, diseases and potential applications
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1519-1538 (2023)
   PUBMED   37674366
  REMARK    GeneRIF: GLUT5: structure, functions, diseases and potential
            applications.
            Review article
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Cui,Y., Liu,H., Wang,Z., Zhang,H., Tian,J., Wang,Z., Song,W.,
            Guo,H., Liu,L., Tian,R., Zuo,X., Ren,S., Zhang,F. and Niu,R.
  TITLE     Fructose promotes angiogenesis by improving vascular endothelial
            cell function and upregulating VEGF expression in cancer cells
  JOURNAL   J Exp Clin Cancer Res 42 (1), 184 (2023)
   PUBMED   37507736
  REMARK    GeneRIF: Fructose promotes angiogenesis by improving vascular
            endothelial cell function and upregulating VEGF expression in
            cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Fiorentino,T.V., De Vito,F., Suraci,E., Marasco,R., Hribal,M.L.,
            Luzza,F. and Sesti,G.
  TITLE     Obesity and overweight are linked to increased sodium-glucose
            cotransporter 1 and glucose transporter 5 levels in duodenum
  JOURNAL   Obesity (Silver Spring) 31 (3), 724-731 (2023)
   PUBMED   36746764
  REMARK    GeneRIF: Obesity and overweight are linked to increased
            sodium-glucose cotransporter 1 and glucose transporter 5 levels in
            duodenum.
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Taneva,I., Grumann,D., Schmidt,D., Taneva,E., von Arnim,U.,
            Ansorge,T. and Wex,T.
  TITLE     Gene variants of the SLC2A5 gene encoding GLUT5, the major fructose
            transporter, do not contribute to clinical presentation of acquired
            fructose malabsorption
  JOURNAL   BMC Gastroenterol 22 (1), 167 (2022)
   PUBMED   35387598
  REMARK    GeneRIF: Gene variants of the SLC2A5 gene encoding GLUT5, the major
            fructose transporter, do not contribute to clinical presentation of
            acquired fructose malabsorption.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Mahraoui,L., Takeda,J., Mesonero,J., Chantret,I., Dussaulx,E.,
            Bell,G.I. and Brot-Laroche,E.
  TITLE     Regulation of expression of the human fructose transporter (GLUT5)
            by cyclic AMP
  JOURNAL   Biochem J 301 (Pt 1) (Pt 1), 169-175 (1994)
   PUBMED   8037665
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Rand,E.B., Depaoli,A.M., Davidson,N.O., Bell,G.I. and Burant,C.F.
  TITLE     Sequence, tissue distribution, and functional characterization of
            the rat fructose transporter GLUT5
  JOURNAL   Am J Physiol 264 (6 Pt 1), G1169-G1176 (1993)
   PUBMED   8333543
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Burant,C.F., Takeda,J., Brot-Laroche,E., Bell,G.I. and
            Davidson,N.O.
  TITLE     Fructose transporter in human spermatozoa and small intestine is
            GLUT5
  JOURNAL   J Biol Chem 267 (21), 14523-14526 (1992)
   PUBMED   1634504
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Davidson,N.O., Hausman,A.M., Ifkovits,C.A., Buse,J.B., Gould,G.W.,
            Burant,C.F. and Bell,G.I.
  TITLE     Human intestinal glucose transporter expression and localization of
            GLUT5
  JOURNAL   Am J Physiol 262 (3 Pt 1), C795-C800 (1992)
   PUBMED   1550217
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Kayano,T., Burant,C.F., Fukumoto,H., Gould,G.W., Fan,Y.S.,
            Eddy,R.L., Byers,M.G., Shows,T.B., Seino,S. and Bell,G.I.
  TITLE     Human facilitative glucose transporters. Isolation, functional
            characterization, and gene localization of cDNAs encoding an
            isoform (GLUT5) expressed in small intestine, kidney, muscle, and
            adipose tissue and an unusual glucose transporter pseudogene-like
            sequence (GLUT6)
  JOURNAL   J Biol Chem 265 (22), 13276-13282 (1990)
   PUBMED   1695905
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158048.35.
            
            Summary: The protein encoded by this gene is a fructose transporter
            responsible for fructose uptake by the small intestine. The encoded
            protein also is necessary for the increase in blood pressure due to
            high dietary fructose consumption. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (4) uses an alternate splice
            junction at the 5' end of a coding exon compared to variant 1. The
            resulting isoform (3) has a shorter and distinct N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.13732.1, AK294368.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..457
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 5 isoform 3"
                     /note="glucose transporter-like protein 5; glucose
                     transporter type 5, small intestine; solute carrier family
                     2 (facilitated glucose/fructose transporter), member 5;
                     testicular tissue protein Li 81"
                     /calculated_mol_wt=50001
     Region          8..427
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(123,126..127,130,244..245,249..250,253..254,281,
                     343..344,347..348,352,375..376,379)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     CDS             1..457
                     /gene="SLC2A5"
                     /gene_synonym="GLUT-5; GLUT5"
                     /coded_by="NM_001328620.2:194..1567"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:6518"
                     /db_xref="HGNC:HGNC:11010"
                     /db_xref="MIM:138230"
ORIGIN      
        1 mgttwllstp qhwtgefmed fpltllwsvt vsmfpfggfi gsllvgplvn kfgrkgallf
       61 nnifsivpai lmgcsrvats feliiisrll vgicagvssn vvpmylgela pknlrgalgv
      121 vpqlfitvgi lvaqifglrn llanvdgwpi llgltgvpaa lqllllpffp esprylliqk
      181 kdeaaakkal qtlrgwdsvd revaeirqed eaekaagfis vlklfrmrsl rwqllsiivl
      241 mggqqlsgvn aiyyyadqiy lsagvpeehv qyvtagtgav nvvmtfcavf vvellgrrll
      301 lllgfsicli accvltaala lqdtvswmpy isivcvisyv ighalgpspi palliteifl
      361 qssrpsafmv ggsvhwlsnf tvglifpfiq eglgpysfiv faviclltti yiflivpetk
      421 aktfieinqi ftkmnkvsev ypekeelkel ppvtseq
//
LOCUS       NP_001278776              77 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 16 [Homo sapiens].
ACCESSION   NP_001278776
VERSION     NP_001278776.1
DBSOURCE    REFSEQ: accession NM_001291847.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB122945.1, BU537824.1 and
            AW337855.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (17) differs in the 5' UTR, and
            lacks five 3' exons but contains two alternate 3' exons, and it
            thus differs in its 3' coding region and 3' UTR, compared to
            variant 1. The encoded isoform (16) has a distinct C-terminus and
            is significantly shorter than isoform 1. This isoform contains no
            N-terminal zinc finger motifs and is likely non-DNA-binding. Both
            variants 16 and 17 encode isoform 16.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU537824.1, SRR1163658.401370.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..77
                     /product="DNA-binding protein Ikaros isoform 16"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=8158
     CDS             1..77
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291847.2:222..455"
                     /note="isoform 16 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS87502.1"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvtygadd
       61 frdfhaiipk sfsllel
//
LOCUS       NP_001334651             754 aa            linear   PRI 20-NOV-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 1A
            isoform 2 [Homo sapiens].
ACCESSION   NP_001334651 XP_016883774
VERSION     NP_001334651.1
DBSOURCE    REFSEQ: accession NM_001347722.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 754)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 754)
  AUTHORS   Wang,P., Sarkar,S., Zhang,M., Xiao,T., Kong,F., Zhang,Z.,
            Balasubramanian,D., Jayaram,N., Datta,S., He,R., Wu,P., Chao,P.,
            Zhang,Y., Washburn,M., Florens,L.A., Nagarkar-Jaiswal,S.,
            Jaiswal,M. and Mohan,M.
  TITLE     DYRK1A interacts with the tuberous sclerosis complex and promotes
            mTORC1 activity
  JOURNAL   Elife 12, 88318 (2024)
   PUBMED   39436397
  REMARK    GeneRIF: DYRK1A interacts with the tuberous sclerosis complex and
            promotes mTORC1 activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 754)
  AUTHORS   Pastor,F., Charles,E., Di Vona,C., Chapelle,M., Rivoire,M.,
            Passot,G., Chabot,B., de la Luna,S., Lucifora,J., Durantel,D. and
            Salvetti,A.
  TITLE     The dual-specificity kinase DYRK1A interacts with the Hepatitis B
            virus genome and regulates the production of viral RNA
  JOURNAL   PLoS One 19 (10), e0311655 (2024)
   PUBMED   39405283
  REMARK    GeneRIF: The dual-specificity kinase DYRK1A interacts with the
            Hepatitis B virus genome and regulates the production of viral RNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 754)
  AUTHORS   Guimera,J., Casas,C., Estivill,X. and Pritchard,M.
  TITLE     Human minibrain homologue (MNBH/DYRK1): characterization,
            alternative splicing, differential tissue expression, and
            overexpression in Down syndrome
  JOURNAL   Genomics 57 (3), 407-418 (1999)
   PUBMED   10329007
REFERENCE   5  (residues 1 to 754)
  AUTHORS   Wang,J., Kudoh,J., Shintani,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of two novel 5' noncoding exons in human MNB/DYRK
            gene and alternatively spliced transcripts
  JOURNAL   Biochem Biophys Res Commun 250 (3), 704-710 (1998)
   PUBMED   9784410
REFERENCE   6  (residues 1 to 754)
  AUTHORS   Song,W.J., Sternberg,L.R., Kasten-Sportes,C., Keuren,M.L.,
            Chung,S.H., Slack,A.C., Miller,D.E., Glover,T.W., Chiang,P.W.,
            Lou,L. and Kurnit,D.M.
  TITLE     Isolation of human and murine homologues of the Drosophila
            minibrain gene: human homologue maps to 21q22.2 in the Down
            syndrome 'critical region'
  JOURNAL   Genomics 38 (3), 331-339 (1996)
   PUBMED   8975710
REFERENCE   7  (residues 1 to 754)
  AUTHORS   Guimera,J., Casas,C., Pucharcos,C., Solans,A., Domenech,A.,
            Planas,A.M., Ashley,J., Lovett,M., Estivill,X. and Pritchard,M.A.
  TITLE     A human homologue of Drosophila minibrain (MNB) is expressed in the
            neuronal regions affected in Down syndrome and maps to the critical
            region
  JOURNAL   Hum Mol Genet 5 (9), 1305-1310 (1996)
   PUBMED   8872470
REFERENCE   8  (residues 1 to 754)
  AUTHORS   Shindoh,N., Kudoh,J., Maeda,H., Yamaki,A., Minoshima,S., Shimizu,Y.
            and Shimizu,N.
  TITLE     Cloning of a human homolog of the Drosophila minibrain/rat Dyrk
            gene from 'the Down syndrome critical region' of chromosome 21
  JOURNAL   Biochem Biophys Res Commun 225 (1), 92-99 (1996)
   PUBMED   8769099
REFERENCE   9  (residues 1 to 754)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
REFERENCE   10 (residues 1 to 754)
  AUTHORS   van Bon,B.W.M., Coe,B.P., de Vries,B.B.A. and Eichler,E.E.
  TITLE     DYRK1A Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26677511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001437.1, AP001428.1,
            AP001413.1, KF457264.1, AP001421.1 and KF511415.1.
            
            On Dec 10, 2016 this sequence version replaced XP_016883774.1.
            
            Summary: This gene encodes a member of the Dual-specificity
            tyrosine phosphorylation-regulated kinase (DYRK) family. This
            member contains a nuclear targeting signal sequence, a protein
            kinase domain, a leucine zipper motif, and a highly conservative
            13-consecutive-histidine repeat. It catalyzes its
            autophosphorylation on serine/threonine and tyrosine residues. It
            may play a significant role in a signaling pathway regulating cell
            proliferation and may be involved in brain development. This gene
            is a homolog of Drosophila mnb (minibrain) gene and rat Dyrk gene.
            It is localized in the Down syndrome critical region of chromosome
            21, and is considered to be a strong candidate gene for learning
            defects associated with Down syndrome. Alternative splicing of this
            gene generates several transcript variants differing from each
            other either in the 5' UTR or in the 3' coding region. These
            variants encode at least five different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.275980.1,
                                           SRR7410570.681176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..754
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..754
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 1A isoform 2"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.12.1"
                     /note="dual specificity YAK1-related kinase;
                     serine/threonine-specific protein kinase; mnb protein
                     kinase homolog hp86; serine/threonine kinase MNB; MNB/DYRK
                     protein kinase; protein kinase minibrain homolog; dual
                     specificity tyrosine-(Y)-phosphorylation regulated kinase
                     1A"
                     /calculated_mol_wt=84426
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          32..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          106..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          108..125
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          139..475
                     /region_name="PKc_DYRK1"
                     /note="Catalytic domain of the protein kinase,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinase 1; cd14226"
                     /db_xref="CDD:271128"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(156..160,164,177,179,193,213,229..232,235,237..238,
                     278,280,282..283,285,298,301,310,312..315,317,354)
                     /site_type="active"
                     /db_xref="CDD:271128"
     Site            order(156..160,164,177,179,213,229..232,235,278,280,
                     282..283,285,298)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271128"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(193,237,278,280,301,310,312..315,317,354)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271128"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63470; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            297..317
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271128"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            312
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          399..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          476..531
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61214; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          586..616
                     /region_name="Histidine-rich domain (HRD).
                     /evidence=ECO:0000269|PubMed:29849146"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          587..670
                     /region_name="Disordered.
                     /evidence=ECO:0000269|PubMed:29849146"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          735..754
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     CDS             1..754
                     /gene="DYRK1A"
                     /gene_synonym="DYRK; DYRK1; HP86; MNB; MNBH; MRD7"
                     /coded_by="NM_001347722.2:190..2454"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS13653.1"
                     /db_xref="GeneID:1859"
                     /db_xref="HGNC:HGNC:3091"
                     /db_xref="MIM:600855"
ORIGIN      
        1 mhtggetsac kpssvrlaps fsfhaaglqm agqmphshqy sdrrqpnisd qqvsalsysd
       61 qiqqpltnqr rmpqtfrdpa taplrklsvd liktykhine vyyakkkrrh qqgqgddssh
      121 kkerkvyndg ydddnydyiv kngekwmdry eidsligkgs fgqvvkaydr veqewvaiki
      181 iknkkaflnq aqievrllel mnkhdtemky yivhlkrhfm frnhlclvfe mlsynlydll
      241 rntnfrgvsl nltrkfaqqm ctallflatp elsiihcdlk penillcnpk rsaikivdfg
      301 sscqlgqriy qyiqsrfyrs pevllgmpyd laidmwslgc ilvemhtgep lfsganevdq
      361 mnkivevlgi ppahildqap karkffeklp dgtwnlkktk dgkreykppg trklhnilgv
      421 etggpggrra gesghtvady lkfkdlilrm ldydpktriq pyyalqhsff kktadegtnt
      481 snsvstspam eqsqssgtts stssssggss gtsnsgrars dpthqhrhsg ghftaavqam
      541 dcethspqvr qqfpaplgws gteaptqvtv ethpvqettf hvapqqnalh hhhgnsshhh
      601 hhhhhhhhhh gqqalgnrtr prvynsptns sstqdsmevg hshhsmtsls ssttssstss
      661 sstgnqgnqa yqnrpvaant ldfgqngamd vnltvysnpr qetgiaghpt yqfsantgpa
      721 hymteghltm rqgadreesp mtgvcvqqsp vass
//
LOCUS       NP_001230871             283 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            4 [Homo sapiens].
ACCESSION   NP_001230871
VERSION     NP_001230871.1
DBSOURCE    REFSEQ: accession NM_001243942.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA257655.1, BX648850.1,
            AC107982.6, BC106050.1, AI955172.1 and AI379788.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks
            an in-frame exon in the 5' coding region, and initiates translation
            at a downstream start codon, compared to variant 1. Variants 4 and
            5 encode the same isoform (4), which has a shorter N-terminus
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648850.1, SRR1660809.70256.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..283
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 4"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=31191
     Region          <1..52
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          93..277
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..283
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001243942.1:465..1316"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58527.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mellimvyac ktscaksiig vipyfpyskq ckmrkrgsiv skllasmmck aglthlitmd
       61 lhqkeiqgff nipvdnlras pfllqyiqee ipdyrnaviv akspasakra qsfaerlrlg
      121 iavihgeaqd aesdlvdgrh sppmvrsvaa ihpsleipml ipkekppitv vgdvggriai
      181 ivddiiddvd sflaaaetlk ergaykifvm athgllssda prrieesaid evvvtntiph
      241 evqklqcpki ktvdismils eairrihnge smsylfrnig ldd
//
LOCUS       NP_001340203             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340203
VERSION     NP_001340203.1
DBSOURCE    REFSEQ: accession NM_001353274.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.54987.1,
                                           SRR1803616.290493.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353274.1:583..1119"
                     /note="isoform 2 is encoded by transcript variant 36"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_054899                206 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22m isoform a [Homo sapiens].
ACCESSION   NP_054899
VERSION     NP_054899.2
DBSOURCE    REFSEQ: accession NM_014180.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Greber,B.J. and Ban,N.
  TITLE     Structure and Function of the Mitochondrial Ribosome
  JOURNAL   Annu Rev Biochem 85, 103-132 (2016)
   PUBMED   27023846
  REMARK    Review article
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Brown,A., Amunts,A., Bai,X.C., Sugimoto,Y., Edwards,P.C.,
            Murshudov,G., Scheres,S.H.W. and Ramakrishnan,V.
  TITLE     Structure of the large ribosomal subunit from human mitochondria
  JOURNAL   Science 346 (6210), 718-722 (2014)
   PUBMED   25278503
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   7  (residues 1 to 206)
  AUTHORS   O'Brien,T.W.
  TITLE     Evolution of a protein-rich mitochondrial ribosome: implications
            for human genetic disease
  JOURNAL   Gene 286 (1), 73-79 (2002)
   PUBMED   11943462
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Goldschmidt-Reisin,S., Kitakawa,M., Herfurth,E.,
            Wittmann-Liebold,B., Grohmann,L. and Graack,H.R.
  TITLE     Mammalian mitochondrial ribosomal proteins. N-terminal amino acid
            sequencing, characterization, and identification of corresponding
            gene sequences
  JOURNAL   J Biol Chem 273 (52), 34828-34836 (1998)
   PUBMED   9857009
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP372420.1, AK000601.1,
            AC008410.6 and CR933679.1.
            
            On May 30, 2002 this sequence version replaced NP_054899.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 39S subunit protein that belongs to
            the L22 ribosomal protein family. A pseudogene corresponding to
            this gene is found on chromosome 4q. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.267279.1,
                                           SRR1803611.38860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000523037.6/
                                                  ENSP00000431040.1
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..206
                     /product="large ribosomal subunit protein uL22m isoform a"
                     /note="39S ribosomal protein L22, mitochondrial; L25mt;
                     39S ribosomal protein L25, mitochondrial; mitochondrial
                     large ribosomal subunit protein uL22m"
                     /calculated_mol_wt=23510
     Region          69..172
                     /region_name="Ribosomal_L22"
                     /note="Ribosomal protein L22p/L17e; pfam00237"
                     /db_xref="CDD:459725"
     CDS             1..206
                     /gene="MRPL22"
                     /gene_synonym="HSPC158; L22mt; MRP-L22; MRP-L25; RPML25;
                     uL22m"
                     /coded_by="NM_014180.4:39..659"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4331.1"
                     /db_xref="GeneID:29093"
                     /db_xref="HGNC:HGNC:14480"
                     /db_xref="MIM:611835"
ORIGIN      
        1 maaavlgqlg alwihnlrsr gklalgvlpq syihtsasld isrkwekknk ivyppqlpge
       61 prrpaeiyhc rrqikyskdk mwylaklirg msidqalaql efndkkgaki ikevlleaqd
      121 mavrdhnvef rsnlyiaest sgrgqclkri ryhgrgrfgi mekvychyfv klvegppppp
      181 eppktavaha keyiqqlrsr tivhtl
//
LOCUS       NP_001161708            1161 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform f [Homo sapiens].
ACCESSION   NP_001161708
VERSION     NP_001161708.1
DBSOURCE    REFSEQ: accession NM_001168236.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1161)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1161)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1161)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1161)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1161)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1161)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1161)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1161)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1161)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1161)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512326.25, FJ542285.1,
            AL139132.16 and BQ014912.1.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (f) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant b, resulting in
            an isoform (f, also known as 1BSCTL) that is shorter than isoform
            b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ542285.1, SRR11853567.2394.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1161
                     /product="tyrosine-protein kinase ABL2 isoform f"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=126088
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          90..143
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(95,97,100..102,104,119,123..124,135,137,139..140)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(99..102,121,123)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          148..241
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(159,187,200)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15735735; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          260..522
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(273,275..277,294,296,341,343,347,395,406,424..426,
                     428,436,470,474)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(273,275,278,294,296,311,315,324,340..341,343,347,
                     395,405..406)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(288..289,319..321,325,367,399..400,518..519)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(365..366,369,454,457..458,487..488)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            405..429
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Region          406..430
                     /region_name="Kinase activation loop.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            418
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis and SRC-type
                     Tyr-kinases. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(424..426,428,436,470,474)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          590..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          633..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          637..639
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; Phosphotyrosine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          673..909
                     /region_name="F-actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          742..773
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            755
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          786..830
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          943..1003
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          999..1161
                     /region_name="F-actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          1042..1161
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1161
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_001168236.2:281..3766"
                     /note="isoform f is encoded by transcript variant f"
                     /db_xref="CCDS:CCDS53436.1"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mgqqvgrvge apglqqpqpr girgssaarp sgrrrdpagr ttetgfnift qhealhrpyg
       61 cdvepqalne airwsskenl lgatesdpnl fvalydfvas gdntlsitkg eklrvlgynq
      121 ngewsevrsk ngqgwvpsny itpvnslekh swyhgpvsrs aaeyllssli ngsflvrese
      181 sspgqlsisl ryegrvyhyr inttadgkvy vtaesrfstl aelvhhhstv adglvttlhy
      241 papkcnkptv ygvspihdkw emertditmk hklgggqyge vyvgvwkkys ltvavktlke
      301 dtmeveeflk eaavmkeikh pnlvqllgvc tleppfyivt eympygnlld ylrecnreev
      361 tavvllymat qissameyle kknfihrdla arnclvgenh vvkvadfgls rlmtgdtyta
      421 hagakfpikw tapeslaynt fsiksdvwaf gvllweiaty gmspypgidl sqvydllekg
      481 yrmeqpegcp pkvyelmrac wkwspadrps faethqafet mfhdssisee vaeelgraas
      541 sssvvpylpr lpilpsktrt lkkqvenken iegaqdaten sasslapgfi rgaqassgsp
      601 alprkqrdks psslledake tcftrdrkgg ffssfmkkrn aptppkrsss fremenqphk
      661 kyeltgnfss vaslqhadgf sftpaqqean lvppkcyggs faqrnlcndd ggggggsgta
      721 gggwsgitgf ftprlikktl glragkptas ddtskpfprs nstssmssgl peqdrmamtl
      781 prncqrsklq lertvstssq peenvdrand mlpkkseesa apsrerpkak llprgatalp
      841 lrtpsgdlai tekdppgvgv agvaaapkgk eknggarlgm agvpedgeqp gwpspakaap
      901 vlptthnhkv pvlisptlkh tpadvqligt dsqgnkfkll sehqvtssgd kdrprrvkpk
      961 capppppvmr llqhpsicsd pteeptalta gqstsetqeg gkkaalgavp isgkagrpvm
     1021 pppqvplpts sispakmang tagtkvalrk tkqaaekisa dkiskealle cadllssalt
     1081 epvpnsqlvd tghqlldycs gyvdcipqtr nkfafreavs klelslqelq vssaaagvpg
     1141 tnpvlnnlls cvqeisdvvq r
//
LOCUS       NP_001311321             405 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001311321
VERSION     NP_001311321.1
DBSOURCE    REFSEQ: accession NM_001324392.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 405)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 405)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 405)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 405)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 405)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 405)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 405)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 405)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 405)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 405)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC069242.1, AC040975.8, AC091558.7, AC108449.5 and BQ019252.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.211720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147920, SAMEA2149398
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..405
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..405
                     /product="homeobox-containing protein 1 isoform 7"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=45850
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..405
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324392.1:370..1587"
                     /note="isoform 7 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS83274.1"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr aniaailesh gidvqspggh
      361 snsddvdgnd yseqdtwqvr ngeeeegrss eggreaekve eerri
//
LOCUS       NP_006116                765 aa            linear   PRI 20-NOV-2025
DEFINITION  rho GTPase-activating protein 6 isoform 3 [Homo sapiens].
ACCESSION   NP_006116
VERSION     NP_006116.2
DBSOURCE    REFSEQ: accession NM_006125.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Chen,X., Zhu,J., Li,X., Chen,J., Zhou,Z., Fan,X., Liang,R., Liu,H.
            and Zhu,D.
  TITLE     ARHGAP6 Suppresses Breast Cancer Tumor Growth by Promoting
            Ferroptosis via RhoA-ROCK1-p38 MAPK Signaling
  JOURNAL   Front Biosci (Landmark Ed) 29 (1), 6 (2024)
   PUBMED   38287795
  REMARK    GeneRIF: ARHGAP6 Suppresses Breast Cancer Tumor Growth by Promoting
            Ferroptosis via RhoA-ROCK1-p38 MAPK Signaling.
REFERENCE   2  (residues 1 to 765)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
  REMARK    GeneRIF: RhoGAP6 interacts with COPI to regulate protein transport.
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Chen,W., Tan,M., Yu,C., Liao,G., Kong,D., Bai,J., Yang,B. and
            Gong,H.
  TITLE     ARHGAP6 inhibits bladder cancer cell viability, migration, and
            invasion via beta-catenin signaling and enhances mitomycin C
            sensitivity
  JOURNAL   Hum Cell 36 (2), 786-797 (2023)
   PUBMED   36715867
  REMARK    GeneRIF: ARHGAP6 inhibits bladder cancer cell viability, migration,
            and invasion via beta-catenin signaling and enhances mitomycin C
            sensitivity.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Liu,Z., Cui,Y., Wang,S., Wu,C., Mei,F., Han,E., Hu,Z. and Zhou,B.
  TITLE     MiR-96-5p is an oncogene in lung adenocarcinoma and facilitates
            tumor progression through ARHGAP6 downregulation
  JOURNAL   J Appl Genet 62 (4), 631-638 (2021)
   PUBMED   34338998
  REMARK    GeneRIF: MiR-96-5p is an oncogene in lung adenocarcinoma and
            facilitates tumor progression through ARHGAP6 downregulation.
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Ochocka,A.M., Grden,M., Sakowicz-Burkiewicz,M., Szutowicz,A. and
            Pawelczyk,T.
  TITLE     Regulation of phospholipase C-delta1 by ARGHAP6, a
            GTPase-activating protein for RhoA: possible role for enhanced
            activity of phospholipase C in hypertension
  JOURNAL   Int J Biochem Cell Biol 40 (10), 2264-2273 (2008)
   PUBMED   18434237
  REMARK    GeneRIF: Human ARHGAP6 protein possessing GTPase stimulating
            activity for RhoA on the catalytic properties of PLC-delta1, was
            studied.
REFERENCE   8  (residues 1 to 765)
  AUTHORS   Ochocka,A.M., Czyzewska,M. and Pawelczyk,T.
  TITLE     Expression in Escherichia coli of human ARHGAP6 gene and
            purification of His-tagged recombinant protein
  JOURNAL   Acta Biochim Pol 50 (1), 239-247 (2003)
   PUBMED   12673365
REFERENCE   9  (residues 1 to 765)
  AUTHORS   Prakash,S.K., Paylor,R., Jenna,S., Lamarche-Vane,N.,
            Armstrong,D.L., Xu,B., Mancini,M.A. and Zoghbi,H.Y.
  TITLE     Functional analysis of ARHGAP6, a novel GTPase-activating protein
            for RhoA
  JOURNAL   Hum Mol Genet 9 (4), 477-488 (2000)
   PUBMED   10699171
REFERENCE   10 (residues 1 to 765)
  AUTHORS   Schaefer,L., Prakash,S. and Zoghbi,H.Y.
  TITLE     Cloning and characterization of a novel rho-type GTPase-activating
            protein gene (ARHGAP6) from the critical region for microphthalmia
            with linear skin defects
  JOURNAL   Genomics 46 (2), 268-277 (1997)
   PUBMED   9417914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004554.1, AF012272.2 and
            AB208792.1.
            
            On May 10, 2006 this sequence version replaced NP_006116.1.
            
            Summary: This gene encodes a member of the rhoGAP family of
            proteins which play a role in the regulation of actin
            polymerization at the plasma membrane during several cellular
            processes. This protein is thought to have two independent
            functions, one as a GTPase-activating protein with specificity for
            RhoA, and another as a cytoskeletal protein that promotes actin
            remodeling. Multiple alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks the last two exons but
            has an alternate 3' segment at the 3' end, as compared to variant
            1. The encoded isoform 3 has a distinct and shorter C-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF012272.2 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..765
                     /product="rho GTPase-activating protein 6 isoform 3"
                     /note="Rho-type GTPase-activating protein RhoGAPX-1; rho
                     GTPase-activating protein 6; rho-type GTPase-activating
                     protein 6"
                     /calculated_mol_wt=83795
     Region          1..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43182.3)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O54834; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Region          <60..173
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            264
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Region          322..361
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43182.3)"
     Region          342..352
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O43182.3)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Region          402..608
                     /region_name="RhoGAP_ARHGAP6"
                     /note="RhoGAP (GTPase-activator protein [GAP] for Rho-like
                     small GTPases) domain of ArhGAP6-like proteins. ArhGAP6
                     shows GAP activity towards RhoA, but not towards Cdc42 and
                     Rac1. ArhGAP6 is often deleted in microphthalmia with
                     linear skin defects syndrome (MLS)...; cd04376"
                     /db_xref="CDD:239841"
     Site            order(433,470,474,553,556..557,588)
                     /site_type="other"
                     /note="putative GTPase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239841"
     Site            433
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00172; propagated
                     from UniProtKB/Swiss-Prot (O43182.3)"
     Site            433
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:239841"
     Region          639..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43182.3)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     Site            711
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43182.3)"
     CDS             1..765
                     /gene="ARHGAP6"
                     /gene_synonym="RHOGAP6; RHOGAPX-1"
                     /coded_by="NM_006125.3:1093..3390"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14142.1"
                     /db_xref="GeneID:395"
                     /db_xref="HGNC:HGNC:676"
                     /db_xref="MIM:300118"
ORIGIN      
        1 msaqsllhsv fscsspasss aasakgfskr klrqtrsldp aliggcgsde agaegsarga
       61 tagrlyspsl paeslgprla sssrgpppra trlpppgplc ssfstpstpq ekspsgsfhf
      121 dyevplgrgg lkksmawdlp svlagpassr sassilcssg ggpngifasp rrwlqqrkfq
      181 sppdsrghpy vvwksegdft wnsmsgrsvr lrsvpiqsls elerarlqev afyqlqqdcd
      241 lscqitipkd gqkrkkslrk kldslgkekn kdkefipqaf gmplsqvian drayklkqdl
      301 qrdeqkdasd fvasllpfgn krqnkelsss nsslsstset pnestspntp epaprarrrg
      361 amsvdsitdl ddnqsrllea lqlslpaeaq skkekardkk lslnpiyrqv prlvdsccqh
      421 lekhglqtvg ifrvgsskkr vrqlreefdr gidvsleeeh svhdvaallk eflrdmpdpl
      481 ltrelytafi ntlllepeeq lgtlqlliyl lppcncdtlh rllqflsiva rhaddniskd
      541 gqevtgnkmt slnlatifgp nllhkqkssd kefsvqssar aeestaiiav vqkmienyea
      601 lfmvppdlqn evlislletd pdvvdyllrr kasqssspdm lqsevsfsvg grhsstdsnk
      661 assgdispyd nnspvlsers llamqedaap ggseklyrvp gqfmlvghls ssksresspg
      721 prlgkgnwsl asrrwpkqat llllhvawcg alrtfssslp ylmfl
//
LOCUS       NP_001254651             610 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle subunit SRP72 isoform 2 [Homo sapiens].
ACCESSION   NP_001254651
VERSION     NP_001254651.1
DBSOURCE    REFSEQ: accession NM_001267722.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 610)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 610)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 610)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 610)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 610)
  AUTHORS   Wild,K., Juaire,K.D., Soni,K., Shanmuganathan,V., Hendricks,A.,
            Segnitz,B., Beckmann,R. and Sinning,I.
  TITLE     Reconstitution of the human SRP system and quantitative and
            systematic analysis of its ribosome interactions
  JOURNAL   Nucleic Acids Res 47 (6), 3184-3196 (2019)
   PUBMED   30649417
  REMARK    GeneRIF: e show that SRP RNA does not bind to the ribosome, while
            SRP binds with nanomolar affinity involving a two-step mechanism of
            the key-player SRP54. Ultrasensitive binding of SRP68/72 indicates
            avidity by multiple binding sites that are dominated by the
            C-terminus of SRP72
REFERENCE   6  (residues 1 to 610)
  AUTHORS   Utz,P.J., Hottelet,M., Le,T.M., Kim,S.J., Geiger,M.E., van
            Venrooij,W.J. and Anderson,P.
  TITLE     The 72-kDa component of signal recognition particle is cleaved
            during apoptosis
  JOURNAL   J Biol Chem 273 (52), 35362-35370 (1998)
   PUBMED   9857079
REFERENCE   7  (residues 1 to 610)
  AUTHORS   Larsen,N., Samuelsson,T. and Zwieb,C.
  TITLE     The Signal Recognition Particle Database (SRPDB)
  JOURNAL   Nucleic Acids Res 26 (1), 177-178 (1998)
   PUBMED   9399828
REFERENCE   8  (residues 1 to 610)
  AUTHORS   Breen,M.A. and Ashcroft,S.J.
  TITLE     A truncated isoform of Ca2+/calmodulin-dependent protein kinase II
            expressed in human islets of Langerhans may result from
            trans-splicing
  JOURNAL   FEBS Lett 409 (3), 375-379 (1997)
   PUBMED   9224693
REFERENCE   9  (residues 1 to 610)
  AUTHORS   Lutcke,H., Prehn,S., Ashford,A.J., Remus,M., Frank,R. and
            Dobberstein,B.
  TITLE     Assembly of the 68- and 72-kD proteins of signal recognition
            particle with 7S RNA
  JOURNAL   J Cell Biol 121 (5), 977-985 (1993)
   PUBMED   8388879
REFERENCE   10 (residues 1 to 610)
  AUTHORS   Siegel,V. and Walter,P.
  TITLE     Each of the activities of signal recognition particle (SRP) is
            contained within a distinct domain: analysis of biochemical mutants
            of SRP
  JOURNAL   Cell 52 (1), 39-49 (1988)
   PUBMED   2830980
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB487204.2, AF069765.1,
            BX537991.1, BM985263.1, AK023480.1 and BM985419.1.
            
            Summary: This gene encodes the 72 kDa subunit of the signal
            recognition particle (SRP), a ribonucleoprotein complex that
            mediates the targeting of secretory proteins to the endoplasmic
            reticulum (ER). The SRP complex consists of a 7S RNA and 6 protein
            subunits: SRP9, SRP14, SRP19, SRP54, SRP68, and SRP72, that are
            bound to the 7S RNA as monomers or heterodimers. SRP has at least 3
            distinct functions that can be associated with the protein
            subunits: signal recognition, translational arrest, and ER membrane
            targeting by interaction with the docking protein. Mutations in
            this gene are associated with familial bone marrow failure.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2012].
            
            Transcript Variant: This variant (2) lacks 2 consecutive in-frame
            coding exons in the 5' region compared to variant 1, which results
            in a shorter isoform (2) missing an internal protein segment
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX537991.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..610
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..610
                     /product="signal recognition particle subunit SRP72
                     isoform 2"
                     /note="signal recognition particle 72 kDa protein; signal
                     recognition particle subunit SRP72; epididymis luminal
                     protein 103; signal recognition particle 72kD; signal
                     recognition particle 72kDa"
                     /calculated_mol_wt=67749
     Site            order(19..20,22,46,49..50,53..54,56..57,80,82..83,86..87,
                     90)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          44..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          51..154
                     /region_name="SRP_TPR_like"
                     /note="Putative TPR-like repeat; pfam17004"
                     /db_xref="CDD:435703"
     Region          79..104
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          180..441
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          310..343
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          348..373
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          471..523
                     /region_name="SRP72"
                     /note="SRP72 RNA-binding domain; pfam08492"
                     /db_xref="CDD:462494"
     CDS             1..610
                     /gene="SRP72"
                     /gene_synonym="BMFF; BMFS1; HEL103"
                     /coded_by="NM_001267722.2:20..1852"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58898.1"
                     /db_xref="GeneID:6731"
                     /db_xref="HGNC:HGNC:11303"
                     /db_xref="MIM:602122"
ORIGIN      
        1 masggsggvs vpalwsevnr ygqngdftra lktvnkilqi nkddvtalhc kvvcliqngs
       61 fkealnvint htkvlannsl sfekayceyr lnrienalkt iesanqqtdk lkelygqvly
      121 rlerydecla vyrdlvrnsq ddydeerktn lsavvaaqsn wekvvpenlg lqegthelcy
      181 ntacaligqg qlnqamkilq kaedlcrrsl sedtdqnvfd skkkvkltna egvefklskk
      241 qlqaiefnka llamytnqae qcrkisaslq sqspehllpv liqaaqlcre kqhtkaiell
      301 qefsdqhpen aaeikltmaq lkisqgnisk aclilrsiee lkhkpgmvsa lvtmysheed
      361 idsaievftq aiqwyqnhqp kspahlslir eaanfklkyg rkkeaisdlq qlwkqnpkdi
      421 htlaqlisay slvdpekaka lskhlpssds mslkvdveal ensagatyir kkggkvtgds
      481 qpkeqgqgdl kkkkkkkkgk lpknydpkvt pdperwlpmr ersyyrgrkk gkkkdqigkg
      541 tqgatagass eldasktvss pptsprpgsa atvsastsni ipprhqkpag apatkkkqqq
      601 kkkkggkggw
//
LOCUS       NP_001354572             849 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform n [Homo sapiens].
ACCESSION   NP_001354572
VERSION     NP_001354572.1
DBSOURCE    REFSEQ: accession NM_001367643.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 849)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 849)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 849)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 849)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 849)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 849)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 849)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 849)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 849)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 849)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.16234.1,
                                           SRR1803613.102063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..849
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..849
                     /product="SUN domain-containing protein 1 isoform n"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=94054
     Region          62..356
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          481..534
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(481,484..485,488,491..492,495..496,498..499,
                     502..503,505..506,509..510,512..513,516,519..520,523,
                     526..527,530..531,533..534)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          493..>626
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          611..669
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          712..847
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..849
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367643.1:52..2601"
                     /note="isoform n is encoded by transcript variant 14"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv revlredghl
      241 svngealcdd ckgkrhldah taahsqsprl pgragtlwhi wacagyfllq ilrrigavgq
      301 avsrtawsal wlavvapgka asgvfwwlgi gwyqfvtlis wlnvflltrc lrnickflvl
      361 liplflllgl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl kqplqgdsea
      421 fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag psasvrdavg
      481 qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa vgeqllptve
      541 hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq ggsleqllqr
      601 fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag asgiteaqar
      661 aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi plwyfsqspr
      721 vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni ssapkdfavy
      781 gleneyqeeg qllgqftydq dgeslqmfqa lkrpddtafq ivelrifsnw ghpeytclyr
      841 frvhgepvk
//
LOCUS       NP_001288177            1086 aa            linear   PRI 20-NOV-2025
DEFINITION  ELKS/Rab6-interacting/CAST family member 1 isoform zeta [Homo
            sapiens].
ACCESSION   NP_001288177
VERSION     NP_001288177.1
DBSOURCE    REFSEQ: accession NM_001301248.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1086)
  AUTHORS   Ribolla,L.M., Sala,K., Tonoli,D., Ramella,M., Bracaglia,L.,
            Bonomo,I., Gonnelli,L., Lamarca,A., Brindisi,M., Pierattelli,R.,
            Provenzani,A. and de Curtis,I.
  TITLE     Interfering with the ERC1-LL5beta interaction disrupts plasma
            membrane-Associated platforms and affects tumor cell motility
  JOURNAL   PLoS One 18 (7), e0287670 (2023)
   PUBMED   37437062
  REMARK    GeneRIF: Interfering with the ERC1-LL5beta interaction disrupts
            plasma membrane-Associated platforms and affects tumor cell
            motility.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1086)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 1086)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1086)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1086)
  AUTHORS   Ko,J., Na,M., Kim,S., Lee,J.R. and Kim,E.
  TITLE     Interaction of the ERC family of RIM-binding proteins with the
            liprin-alpha family of multidomain proteins
  JOURNAL   J Biol Chem 278 (43), 42377-42385 (2003)
   PUBMED   12923177
  REMARK    GeneRIF: In vitro results indicate that ERC2/CAST, an active
            zone-specific isoform, interacts with all of the known isoforms of
            liprin-alpha and that liprin-alpha1 associates with both ERC2 and
            ERC1b
REFERENCE   6  (residues 1 to 1086)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 1086)
  AUTHORS   Nakata,T., Yokota,T., Emi,M. and Minami,S.
  TITLE     Differential expression of multiple isoforms of the ELKS mRNAs
            involved in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 35 (1), 30-37 (2002)
   PUBMED   12203787
  REMARK    GeneRIF: Analysis of the gene structure of four isoforms (ELKS
            beta, ELKS gamma, ELKS delta, and ELKS epsilon) in a case of
            papillary thyroid carcinoma reveal that the isoforms are produced
            by alternative splicing.
REFERENCE   8  (residues 1 to 1086)
  AUTHORS   Monier,S., Jollivet,F., Janoueix-Lerosey,I., Johannes,L. and
            Goud,B.
  TITLE     Characterization of novel Rab6-interacting proteins involved in
            endosome-to-TGN transport
  JOURNAL   Traffic 3 (4), 289-297 (2002)
   PUBMED   11929610
REFERENCE   9  (residues 1 to 1086)
  AUTHORS   Yokota,T., Nakata,T., Minami,S., Inazawa,J. and Emi,M.
  TITLE     Genomic organization and chromosomal mapping of ELKS, a gene
            rearranged in a papillary thyroid carcinoma
  JOURNAL   J Hum Genet 45 (1), 6-11 (2000)
   PUBMED   10697956
REFERENCE   10 (residues 1 to 1086)
  AUTHORS   Nakata,T., Kitamura,Y., Shimizu,K., Tanaka,S., Fujimori,M.,
            Yokoyama,S., Ito,K. and Emi,M.
  TITLE     Fusion of a novel gene, ELKS, to RET due to translocation
            t(10;12)(q11;p13) in a papillary thyroid carcinoma
  JOURNAL   Genes Chromosomes Cancer 25 (2), 97-103 (1999)
   PUBMED   10337992
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004803.11, BC144287.1,
            AC004671.1 and BM984956.1.
            
            Summary: The protein encoded by this gene is a member of a family
            of RIM-binding proteins. RIMs are active zone proteins that
            regulate neurotransmitter release. This gene has been found fused
            to the receptor-type tyrosine kinase gene RET by gene rearrangement
            due to the translocation t(10;12)(q11;p13) in thyroid papillary
            carcinoma. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (zeta) contains an additional exon
            that results in an alternate 3' coding region and 3' UTR, compared
            to variant epsilon. The encoded isoform (zeta) has a distinct
            C-terminus and is shorter than isoform epsilon. The 5' UTR of this
            variant is incomplete due to lack of full-length transcript support
            and splice site ambiguity in the 5'-most exon.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144287.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1086
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..1086
                     /product="ELKS/Rab6-interacting/CAST family member 1
                     isoform zeta"
                     /note="RAB6 interacting protein 2"
                     /calculated_mol_wt=124690
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MI1; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          154..982
                     /region_name="Cast"
                     /note="RIM-binding protein of the cytomatrix active zone;
                     pfam10174"
                     /db_xref="CDD:431111"
     Region          590..609
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            719..720
                     /site_type="other"
                     /note="Breakpoint for translocation to form ERC1-RET
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Region          814..836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1005
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811U3; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IUD2.1)"
     CDS             1..1086
                     /gene="ERC1"
                     /gene_synonym="Cast2; ELKS; ERC-1; RAB6IP2"
                     /coded_by="NM_001301248.1:157..3417"
                     /note="isoform zeta is encoded by transcript variant zeta"
                     /db_xref="CCDS:CCDS76504.1"
                     /db_xref="GeneID:23085"
                     /db_xref="HGNC:HGNC:17072"
                     /db_xref="MIM:607127"
ORIGIN      
        1 mygsarsvgk vepssqspgr sprlprsprl ghrrtnstgg ssgssvgggs gktlsmeniq
       61 slnaayatsg pmylsdhenv gsetpkstmt lgrsggrlpy gvrmtamgss pniassgvas
      121 dtiafgehhl ppvsmastvp hslrqardnt imdlqtqlke vlrendllrk dvevkeskls
      181 ssmnsiktfw spelkkeral rkdeaskiti wkeqyrvvqe enqhmqmtiq alqdelriqr
      241 dlnqlfqqds ssrtgepcva elteenfqrl haeherqake lfllrktlee melrietqkq
      301 tlnardesik kllemlqskg lsakateedh ertrrlaeae mhvhhlesll eqkekensml
      361 reemhrrfen apdsaktkal qtviemkdsk issmerglrd leeeiqmlks ngalsteere
      421 eemkqmevyr shskfmknkv eqlkeelssk eaqweelkkk aaglqaeigq vkqelsrkdt
      481 ellalqtkle tltnqfsdsk qhievlkesl takeqraail qtevdalrlr leeketmlnk
      541 ktkqiqdmae ekgtqageih dlkdmldvke rkvnvlqkki enlqeqlrdk ekqmsslker
      601 vkslqadttn tdtalttlee alaekertie rlkeqrdrde rekqeeidny kkdlkdlkek
      661 vsllqgdlse keaslldlke hasslassgl kkdsrlktle ialeqkkeec lkmesqlkka
      721 heaalearas pemsdriqhl ereitrykde sskaqaevdr lleilkeven ekndkdkkia
      781 elerqvkdqn kkvanlkhke qvekkksaqm leearrredn lndssqqlqd slrkkddrie
      841 eleealresv qitaeremvl aqeesartna ekqveellma mekvkqeles mkaklsstqq
      901 slaekethlt nlraerrkhl eevlemkqea llaaisekda niallelsss kkktqeevaa
      961 lkrekdrlvq qlkqqtqnrm klmadnyedd hfksshsnqt nhkpspdqii qplleldqnr
     1021 sklklyighl ttlchdrdpl ilrgltppas ynldddqaaw enelqkmtrg qnplhpkame
     1081 klpffm
//
LOCUS       NP_001724                705 aa            linear   PRI 20-NOV-2025
DEFINITION  complement C1r subcomponent isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001724 XP_930935 XP_935774
VERSION     NP_001724.4
DBSOURCE    REFSEQ: accession NM_001733.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Zhang,Q., Yue,Y., Wang,X., Cui,H., Liu,Y., Gao,M., Liu,T. and
            Xiao,L.
  TITLE     Tandem Mass Tag-Labeled Quantitative Proteome Analyses Identify C1R
            and A2M as Novel Serum Biomarkers in Pregnant Women with
            Obstructive Sleep Apnea
  JOURNAL   J Proteome Res 23 (4), 1232-1248 (2024)
   PUBMED   38407963
  REMARK    GeneRIF: Tandem Mass Tag-Labeled Quantitative Proteome Analyses
            Identify C1R and A2M as Novel Serum Biomarkers in Pregnant Women
            with Obstructive Sleep Apnea.
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Yadav,M.K., Maharana,J., Yadav,R., Saha,S., Sarma,P., Soni,C.,
            Singh,V., Saha,S., Ganguly,M., Li,X.X., Mohapatra,S., Mishra,S.,
            Khant,H.A., Chami,M., Woodruff,T.M., Banerjee,R., Shukla,A.K. and
            Gati,C.
  TITLE     Molecular basis of anaphylatoxin binding, activation, and signaling
            bias at complement receptors
  JOURNAL   Cell 186 (22), 4956-4973 (2023)
   PUBMED   37852260
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Nakajima,K., Suzuki,H., Yamamoto,M., Yamamoto,T., Kawai,T.,
            Nakabayashi,K., Hata,K., Kosaki,K., Nakajima,H., Sano,S. and
            Kubo,A.
  TITLE     A familial case of periodontal Ehlers-Danlos syndrome lacking skin
            extensibility and joint hypermobility with a missense mutation in
            C1R
  JOURNAL   J Dermatol 49 (7), 714-718 (2022)
   PUBMED   35365885
  REMARK    GeneRIF: A familial case of periodontal Ehlers-Danlos syndrome
            lacking skin extensibility and joint hypermobility with a missense
            mutation in C1R.
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Wang,X., Yang,G., Wang,Q., Zhao,Y., Ding,K., Ji,C., Shi,Z., Li,H.,
            Li,Y. and Li,S.
  TITLE     C1R, CCL2, and TNFRSF1A Genes in Coronavirus Disease-COVID-19
            Pathway Serve as Novel Molecular Biomarkers of GBM Prognosis and
            Immune Infiltration
  JOURNAL   Dis Markers 2022, 8602068 (2022)
   PUBMED   35726234
  REMARK    GeneRIF: C1R, CCL2, and TNFRSF1A Genes in Coronavirus
            Disease-COVID-19 Pathway Serve as Novel Molecular Biomarkers of GBM
            Prognosis and Immune Infiltration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Viiklepp,K., Nissinen,L., Ojalill,M., Riihila,P., Kallajoki,M.,
            Meri,S., Heino,J. and Kahari,V.M.
  TITLE     C1r Upregulates Production of Matrix Metalloproteinase-13 and
            Promotes Invasion of Cutaneous Squamous Cell Carcinoma
  JOURNAL   J Invest Dermatol 142 (5), 1478-1488 (2022)
   PUBMED   34756877
  REMARK    GeneRIF: C1r Upregulates Production of Matrix Metalloproteinase-13
            and Promotes Invasion of Cutaneous Squamous Cell Carcinoma.
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Kapferer-Seebacher,I., van Dijk,F.S. and Zschocke,J.
  TITLE     Periodontal Ehlers-Danlos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34324282
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Luo,C., Thielens,N.M., Gagnon,J., Gal,P., Sarvari,M., Tseng,Y.,
            Tosi,M., Zavodszky,P., Arlaud,G.J. and Schumaker,V.N.
  TITLE     Recombinant human complement subcomponent C1s lacking
            beta-hydroxyasparagine, sialic acid, and one of its two
            carbohydrate chains still reassembles with C1q and C1r to form a
            functional C1 complex
  JOURNAL   Biochemistry 31 (17), 4254-4262 (1992)
   PUBMED   1533159
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Lee,S.L., Wallace,S.L., Barone,R., Blum,L. and Chase,P.H.
  TITLE     Familial deficiency of two subunits of the first component of
            complement. C1r and C1s associated with a lupus erythematosus-like
            disease
  JOURNAL   Arthritis Rheum 21 (8), 958-967 (1978)
   PUBMED   737019
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Ziccardi,R.J. and Cooper,N.R.
  TITLE     Activation of C1r by proteolytic cleavage
  JOURNAL   J Immunol 116 (2), 504-509 (1976)
   PUBMED   1249422
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Ziccardi,R.J. and Cooper,N.R.
  TITLE     Physicochemical and functional characterization of the C1r subunit
            of the first complement component
  JOURNAL   J Immunol 116 (2), 496-503 (1976)
   PUBMED   814163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC035220.1 and M14058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2017 this sequence version replaced NP_001724.3.
            
            Summary: This gene encodes a member of the peptidase S1 protein
            family. The encoded protein is a proteolytic subunit in the
            complement system C1 complex. The complement system acts as a
            mediator in the innate immune response by ultimately triggering
            phagocytosis, inflammation, and rupturing the bacterial cell wall.
            Mutations in this gene are associated with Ehlers-Danlos Syndrome.
            [provided by RefSeq, Dec 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035220.1, SRR1803617.180836.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647956.2/ ENSP00000497341.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..705
                     /product="complement C1r subcomponent isoform 1
                     preproprotein"
                     /EC_number="3.4.21.41"
                     /note="complement component 1, r subcomponent; complement
                     C1r subcomponent"
                     /calculated_mol_wt=78269
     sig_peptide     1..17
                     /note="/evidence=ECO:0000269|PubMed:3036070; propagated
                     from UniProtKB/Swiss-Prot (P00736.2)"
                     /calculated_mol_wt=1923
     mat_peptide     18..705
                     /product="Complement C1r subcomponent. /id=PRO_0000027577"
                     /note="propagated from UniProtKB/Swiss-Prot (P00736.2)"
                     /calculated_mol_wt=78269
     mat_peptide     18..463
                     /product="Complement C1r subcomponent heavy chain.
                     /evidence=ECO:0000269|PubMed:3036070. /id=PRO_0000027578"
                     /note="propagated from UniProtKB/Swiss-Prot (P00736.2)"
                     /calculated_mol_wt=51191
     Site            order(26,28,30,57,62,104,135,137,139..140)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          27..138
                     /region_name="CUB"
                     /note="Domain first found in C1r, C1s, uEGF, and bone
                     morphogenetic protein; smart00042"
                     /db_xref="CDD:214483"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:29311313, ECO:0007744|PDB:6F1C,
                     ECO:0007744|PDB:6F1H, ECO:0007744|PDB:6F39; propagated
                     from UniProtKB/Swiss-Prot (P00736.2)"
     Region          161..189
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            167
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyasparagine.
                     /evidence=ECO:0000269|PubMed:2820791; propagated from
                     UniProtKB/Swiss-Prot (P00736.2)"
     Region          193..302
                     /region_name="CUB"
                     /note="CUB domain; pfam00431"
                     /db_xref="CDD:395345"
     Site            order(202,204,206,233,238,275,299,301,303..304)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:8635594; propagated from
                     UniProtKB/Swiss-Prot (P00736.2)"
     Site            221
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P00736.2)"
     Region          309..371
                     /region_name="Sushi"
                     /note="Sushi repeat (SCR repeat); pfam00084"
                     /db_xref="CDD:459664"
     Region          376..447
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(386,407)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          463..697
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; smart00020"
                     /db_xref="CDD:214473"
     Site            463..464
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000269|PubMed:11445589,
                     ECO:0000269|PubMed:11673533, ECO:0000269|PubMed:869924;
                     propagated from UniProtKB/Swiss-Prot (P00736.2)"
     mat_peptide     464..705
                     /product="Complement C1r subcomponent light chain.
                     /evidence=ECO:0000269|PubMed:6303394,
                     ECO:0000305|PubMed:869924. /id=PRO_0000027579"
                     /note="propagated from UniProtKB/Swiss-Prot (P00736.2)"
                     /calculated_mol_wt=27096
     Site            464
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(502,557,654)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            514
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P00736.2)"
     Site            581
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:11823416; propagated from
                     UniProtKB/Swiss-Prot (P00736.2)"
     Site            order(648,675,677)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..705
                     /gene="C1R"
                     /gene_synonym="EDS8; EDSPD1"
                     /coded_by="NM_001733.7:58..2175"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS81658.1"
                     /db_xref="GeneID:715"
                     /db_xref="HGNC:HGNC:1246"
                     /db_xref="MIM:613785"
ORIGIN      
        1 mwllyllvpa lfcraggsip ipqklfgevt splfpkpypn nfetttvitv ptgyrvklvf
       61 qqfdlepseg cfydyvkisa dkkslgrfcg qlgsplgnpp gkkefmsqgn kmlltfhtdf
      121 sneengtimf ykgflayyqa vdldecasrs ksgeedpqpq cqhlchnyvg gyfcscrpgy
      181 elqedrhscq aecsselyte asgyissley prsyppdlrc nysirvergl tlhlkflepf
      241 diddhqqvhc pydqlqiyan gknigefcgk qrppdldtss navdllfftd esgdsrgwkl
      301 rytteiikcp qpktldefti iqnlqpqyqf rdyfiatckq gyqliegnqv lhsftavcqd
      361 dgtwhrampr ckikdcgqpr nlpngdfryt ttmgvntyka riqyychepy ykmqtragsr
      421 eseqgvytct aqgiwkneqk gekiprclpv cgkpvnpveq rqriiggqka kmgnfpwqvf
      481 tnihgrggga llgdrwilta ahtlypkehe aqsnasldvf lghtnveelm klgnhpirrv
      541 svhpdyrqde synfegdial lelensvtlg pnllpiclpd ndtfydlglm gyvsgfgvme
      601 ekiahdlrfv rlpvanpqac enwlrgknrm dvfsqnmfca ghpslkqdac qgdsggvfav
      661 rdpntdrwva tgivswgigc srgygfytkv lnyvdwikke meeed
//
LOCUS       NP_001091894             904 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001091894
VERSION     NP_001091894.1
DBSOURCE    REFSEQ: accession NM_001098424.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 904)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 904)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 904)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 904)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 904)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 904)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 904)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 904)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 904)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8, U13897.1 and
            AC068302.18.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U13897.1, SRR11853561.21838.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..904
                     /product="disks large homolog 1 isoform 1"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=100324
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..223
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          162..212
                     /region_name="Interaction with SH3 domains"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Region          222..310
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Region          224..546
                     /region_name="Required for interaction with MARCHF2.
                     /evidence=ECO:0000269|PubMed:17980554"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62696; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            order(233..239,256,259,289,293,296..297)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          319..403
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(328..334,351,354,384,388,391..392)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q811D0; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          404..465
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          463..553
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(475..481,492,495,525,529,532..533)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          582..648
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(587,609..610,631)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(590,592,595,604,622..623,642,644..645)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811D0; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          662..693
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          713..891
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62696; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     CDS             1..904
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001098424.1:191..2905"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43194.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kpteavlpsp ptvpvipvlp
      181 vpaentvilp tipqanpppv lvntdsletp tyvngtdady eyeeitlerg nsglgfsiag
      241 gtdnphigdd ssifitkiit ggaaaqdgrl rvndcilrvn evdvrdvths kavealkeag
      301 sivrlyvkrr kpvsekimei klikgpkglg fsiaggvgnq hipgdnsiyv tkiieggaah
      361 kdgklqigdk llavnnvcle evtheeavta lkntsdfvyl kvakptsmym ndgyappdit
      421 nsssqpvdnh vspssflgqt pasparyspv skavlgddei treprkvvlh rgstglgfni
      481 vggedgegif isfilaggpa dlsgelrkgd riisvnsvdl raasheqaaa alknagqavt
      541 ivaqyrpeey srfeakihdl reqmmnssis sgsgslrtsq krslyvralf dydktkdsgl
      601 psqglnfkfg dilhvinasd dewwqarqvt pdgesdevgv ipskrrvekk erarlktvkf
      661 nsktrdkgei pddmgskglk hvtsnasdse ssyrgqeeyv lsyepvnqqe vnytrpviil
      721 gpmkdrindd lisefpdkfg scvphttrpk rdyevdgrdy hfvtsreqme kdiqehkfie
      781 agqynnhlyg tsvqsvreva ekgkhcildv sgnaikrlqi aqlypisifi kpksmenime
      841 mnkrlteeqa rktferamkl eqeftehfta ivqgdtledi ynqvkqiiee qsgsyiwvpa
      901 kekl
//
LOCUS       NP_066927                 25 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein eS32 [Homo sapiens].
ACCESSION   NP_066927
VERSION     NP_066927.1
DBSOURCE    REFSEQ: accession NM_021104.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 25)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 25)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 25)
  AUTHORS   Geng,W., Ren,J., Shi,H., Qin,F., Xu,X., Xiao,S., Jiao,Y. and
            Wang,A.
  TITLE     RPL41 sensitizes retinoblastoma cells to chemotherapeutic drugs via
            ATF4 degradation
  JOURNAL   J Cell Physiol 236 (3), 2214-2225 (2021)
   PUBMED   32783256
  REMARK    GeneRIF: RPL41 sensitizes retinoblastoma cells to chemotherapeutic
            drugs via ATF4 degradation.
REFERENCE   4  (residues 1 to 25)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 25)
  AUTHORS   Yang,G. and Zong,H.
  TITLE     Overexpression of PDZK1IP1, EEF1A2 and RPL41 genes in intrahepatic
            cholangiocarcinoma
  JOURNAL   Mol Med Rep 13 (6), 4786-4790 (2016)
   PUBMED   27082702
  REMARK    GeneRIF: Differential gene expression analysis demonstrated
            significant upregulation of PDZK1IP1, EEF1A2 and RPL41
            (ENSG00000279483) genes in the intrahepatic cholangiocarcinoma
            samples when compared with the matched paratumor samples.
REFERENCE   6  (residues 1 to 25)
  AUTHORS   Go,H., Miyado,K. and Taniguchi,S.
  TITLE     Genomic structure of the human ribosomal protein L41 gene
  JOURNAL   Biochem Mol Biol Int 46 (6), 1227-1231 (1998)
   PUBMED   9891856
REFERENCE   7  (residues 1 to 25)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 25)
  AUTHORS   Lee,J.H., Kim,J.M., Kim,M.S., Lee,Y.T., Marshak,D.R. and Bae,Y.S.
  TITLE     The highly basic ribosomal protein L41 interacts with the beta
            subunit of protein kinase CKII and stimulates phosphorylation of
            DNA topoisomerase IIalpha by CKII
  JOURNAL   Biochem Biophys Res Commun 238 (2), 462-467 (1997)
   PUBMED   9299532
REFERENCE   9  (residues 1 to 25)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 25)
  AUTHORS   Klaudiny,J., von der Kammer,H. and Scheit,K.H.
  TITLE     Characterization by cDNA cloning of the mRNA of a highly basic
            human protein homologous to the yeast ribosomal protein YL41
  JOURNAL   Biochem Biophys Res Commun 187 (2), 901-906 (1992)
   PUBMED   1326959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from Z12962.1 and AC034102.32.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM830448.1, BM765079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..25
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..25
                     /product="small ribosomal subunit protein eS32"
                     /note="60S ribosomal protein L41; homologue of yeast
                     ribosomal protein YL41; HG12 protein; large ribosomal
                     subunit protein eL41"
                     /calculated_mol_wt=3325
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62945.1)"
     Region          1..24
                     /region_name="Ribosomal_L41"
                     /note="Ribosomal protein L41; pfam05162"
                     /db_xref="CDD:428342"
     CDS             1..25
                     /gene="RPL41"
                     /gene_synonym="eL41; L41"
                     /coded_by="NM_021104.2:41..118"
                     /db_xref="CCDS:CCDS44919.1"
                     /db_xref="GeneID:6171"
                     /db_xref="HGNC:HGNC:10354"
                     /db_xref="MIM:613315"
ORIGIN      
        1 mrakwrkkrm rrlkrkrrkm rqrsk
//
LOCUS       NP_001339877             665 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 18 [Homo sapiens].
ACCESSION   NP_001339877 XP_005251255
VERSION     NP_001339877.1
DBSOURCE    REFSEQ: accession NM_001352948.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_005251255.1.
            
            Transcript Variant: This variant (23), as well as variants 21 and
            22, encodes isoform 18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.116369.1,
                                           SRR1660809.183345.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..665
                     /product="DNA repair-scaffolding protein isoform 18"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=72443
     Region          <5..119
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          271..655
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..665
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352948.1:581..2578"
                     /note="isoform 18 is encoded by transcript variant 23"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mrscrsfprg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt vkilelheec
       61 amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv rifppwqkli
      121 ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi kgltnnspei
      181 qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga gvrvvvqrvy
      241 slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar qlegkscslv
      301 gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa lcyiltahpn
      361 lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql kslllleqre
      421 iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl ffkdalrdqg
      481 rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq gtvvgvdest
      541 afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr srpqcrvkvk
      601 llqrsissll rfaagedgsy evksvlgkev gllncfvqsv tahptscigl eeiellsagg
      661 asaeh
//
LOCUS       NP_000980                115 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL30 [Homo sapiens].
ACCESSION   NP_000980
VERSION     NP_000980.1
DBSOURCE    REFSEQ: accession NM_000989.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Lee,J.H., Han,J.H., Kim,H., Park,S.M., Joe,E.H. and Jou,I.
  TITLE     Parkinson's disease-associated LRRK2-G2019S mutant acts through
            regulation of SERCA activity to control ER stress in astrocytes
  JOURNAL   Acta Neuropathol Commun 7 (1), 68 (2019)
   PUBMED   31046837
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Chaillou,T., Zhang,X. and McCarthy,J.J.
  TITLE     Expression of Muscle-Specific Ribosomal Protein L3-Like Impairs
            Myotube Growth
  JOURNAL   J Cell Physiol 231 (9), 1894-1902 (2016)
   PUBMED   26684695
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 115)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 115)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 115)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 115)
  AUTHORS   Feo,S., Davies,B. and Fried,M.
  TITLE     The mapping of seven intron-containing ribosomal protein genes
            shows they are unlinked in the human genome
  JOURNAL   Genomics 13 (1), 201-207 (1992)
   PUBMED   1577483
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BM785413.1 and BC095426.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L30E family of ribosomal proteins. It is located in the
            cytoplasm. This gene is co-transcribed with the U72 small nucleolar
            RNA gene, which is located in its fourth intron. As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AV761808.1, BE439872.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000287038.8/ ENSP00000287038.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..115
                     /product="large ribosomal subunit protein eL30"
                     /note="60S ribosomal protein L30"
                     /calculated_mol_wt=12653
     Region          2..107
                     /region_name="PTZ00106"
                     /note="60S ribosomal protein L30; Provisional"
                     /db_xref="CDD:185450"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     Site            26
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62888.2)"
     CDS             1..115
                     /gene="RPL30"
                     /gene_synonym="eL30; L30"
                     /coded_by="NM_000989.4:71..418"
                     /db_xref="CCDS:CCDS34928.1"
                     /db_xref="GeneID:6156"
                     /db_xref="HGNC:HGNC:10333"
                     /db_xref="MIM:180467"
ORIGIN      
        1 mvaakktkks lesinsrlql vmksgkyvlg ykqtlkmirq gkaklvilan ncpalrksei
       61 eyyamlaktg vhhysgnnie lgtacgkyyr vctlaiidpg dsdiirsmpe qtgek
//
LOCUS       NP_001354607             915 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform oo [Homo sapiens].
ACCESSION   NP_001354607
VERSION     NP_001354607.1
DBSOURCE    REFSEQ: accession NM_001367678.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 915)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 915)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 915)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 915)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 915)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 915)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 915)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 915)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 915)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 915)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.123432.1,
                                           SRR1660807.75978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..915
                     /product="SUN domain-containing protein 1 isoform oo"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=101731
     Region          62..422
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          547..600
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(547,550..551,554,557..558,561..562,564..565,
                     568..569,571..572,575..576,578..579,582,585..586,589,
                     592..593,596..597,599..600)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          559..>692
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          677..735
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          778..913
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..915
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367678.1:52..2799"
                     /note="isoform oo is encoded by transcript variant 41"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca gyfllqilrr
      361 igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv flltrclrni
      421 ckflvllipl flllglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl
      481 qgdseafpwh wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas
      541 vrdavgqppr etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq
      601 llptvehlql eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl
      661 eqllqrfssq fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi
      721 teaqaraivn salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy
      781 fsqsprvviq pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap
      841 kdfavyglen eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe
      901 ytclyrfrvh gepvk
//
LOCUS       NP_001171658             511 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase component PIGT isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001171658
VERSION     NP_001171658.1
DBSOURCE    REFSEQ: accession NM_001184729.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Ben Ayed,I., Jallouli,O., Murakami,Y., Souissi,A., Mallouli,S.,
            Bouzid,A., Kamoun,F., Elloumi,I., Frikha,F., Tlili,A.,
            Weckhuysen,S., Kinoshita,T., Triki,C.C. and Masmoudi,S.
  TITLE     Case report: Functional analysis of the p.Arg507Trp variant of the
            PIGT gene supporting the moderate epilepsy phenotype of mutations
            in the C-terminal region
  JOURNAL   Front Neurol 14, 1092887 (2023)
   PUBMED   36970549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Ohishi,K., Nagamune,K., Maeda,Y. and Kinoshita,T.
  TITLE     Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and
            PIG-T, form a functionally important intermolecular disulfide
            bridge
  JOURNAL   J Biol Chem 278 (16), 13959-13967 (2003)
   PUBMED   12582175
  REMARK    GeneRIF: GPI8 and PIG-T form a functionally important
            intermolecular disulfide bridge
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Vainauskas,S., Maeda,Y., Kurniawan,H., Kinoshita,T. and Menon,A.K.
  TITLE     Structural requirements for the recruitment of Gaa1 into a
            functional glycosylphosphatidylinositol transamidase complex
  JOURNAL   J Biol Chem 277 (34), 30535-30542 (2002)
   PUBMED   12052837
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Ohishi,K., Inoue,N. and Kinoshita,T.
  TITLE     PIG-S and PIG-T, essential for GPI anchor attachment to proteins,
            form a complex with GAA1 and GPI8
  JOURNAL   EMBO J 20 (15), 4088-4098 (2001)
   PUBMED   11483512
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Fossey,S.C., Mychaleckyj,J.C., Pendleton,J.K., Snyder,J.R.,
            Bensen,J.T., Hirakawa,S., Rich,S.S., Freedman,B.I. and Bowden,D.W.
  TITLE     A high-resolution 6.0-megabase transcript map of the type 2
            diabetes susceptibility region on human chromosome 20
  JOURNAL   Genomics 76 (1-3), 45-57 (2001)
   PUBMED   11549316
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK225517.1 and AL121742.1.
            
            Summary: This gene encodes a protein that is involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid found on many blood cells and serves to
            anchor proteins to the cell surface. This protein is an essential
            component of the multisubunit enzyme, GPI transamidase. GPI
            transamidase mediates GPI anchoring in the endoplasmic reticulum,
            by catalyzing the transfer of fully assembled GPI units to
            proteins. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (3) lacks an exon in the coding
            region, but maintains the reading frame, compared to variant 1. The
            encoded isoform (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225517.1, SRR3476690.1108432.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..511
                     /product="GPI-anchor transamidase component PIGT isoform 3
                     precursor"
                     /note="neurotrophin-regulated neuronal
                     development-associated protein; GPI transamidase subunit;
                     GPI transamidase component PIG-T; GPI-anchor transamidase
                     component PIGT; phosphatidylinositol-glycan biosynthesis
                     class T protein"
                     /calculated_mol_wt=55895
     sig_peptide     1..21
                     /calculated_mol_wt=2111
     mat_peptide     22..511
                     /product="GPI-anchor transamidase component PIGT isoform
                     3"
                     /calculated_mol_wt=55895
     Region          32..484
                     /region_name="Gpi16"
                     /note="Gpi16 subunit, GPI transamidase component;
                     pfam04113"
                     /db_xref="CDD:461180"
     Site            164
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q969N2.1)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q969N2.1)"
     Site            327
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:35551457,
                     ECO:0000269|PubMed:37684232, ECO:0007744|PDB:7WLD,
                     ECO:0007744|PDB:8IMX, ECO:0007744|PDB:8IMY; propagated
                     from UniProtKB/Swiss-Prot (Q969N2.1)"
     CDS             1..511
                     /gene="PIGT"
                     /gene_synonym="CGI-06; MCAHS3; NDAP; PIG-T; PNH2"
                     /coded_by="NM_001184729.3:17..1552"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS54465.1"
                     /db_xref="GeneID:51604"
                     /db_xref="HGNC:HGNC:14938"
                     /db_xref="MIM:610272"
ORIGIN      
        1 maaamplall vllllgpggw claepprdsl reelvitplp sgdvaatfqf rtrwdselqr
       61 egvshyrlfp kalgqlisky slrelhlsft qgfwrtrywg ppflqapsga elwvwfqdtv
      121 tdvdkswkel snvlsgifca slnfidstnt vtptasfkpl glandtdhyf lryavlprev
      181 vctenltpwk kllpcsskag lsvllkadrl fhtsyhsqav hirpvcrnar ctsiswelrq
      241 tlsvvfdafi tgqgkkdwsl frmfsrtlte pcplasesrv yvdittynqd netlevhppp
      301 tttyqdvilg trktyaiydl ldtaminnsr nlniqlkwkr ppengyihyq paqdrlqphl
      361 lemliqlpan svtkvsiqfe rallkwteyt pdpnhgfyvs psvlsalvps mvaakpvdwe
      421 esplfnslfp vsdgsnyfvr lytepllvnl ptpdfsmpyn vicltctvva vcygsfynll
      481 trtfhieepr tgglakrlan lirrargvpp l
//
LOCUS       NP_001307571             566 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 15 [Homo sapiens].
ACCESSION   NP_001307571
VERSION     NP_001307571.1
DBSOURCE    REFSEQ: accession NM_001320642.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012508.10, AL713697.1 and
            BM711160.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (15) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (15)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.202471.1,
                                           SRR1803615.225213.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..566
                     /product="myc box-dependent-interacting protein 1 isoform
                     15"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=61755
     Region          4..245
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(23,26..27,31,34,37..38,41,51..52,54..55,58..59,
                     61..62,65,73,201,204..205,207,212..213,215..216,219..220,
                     222..223,226..227,229..230,234,237)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(46,53,112,115,118..119,143)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <249..480
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          494..565
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(505..511,530,532..535,558,560..561)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..566
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_001320642.1:960..2660"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 mvlqklgkad etkdeqfeqc vqnfnkqlte gtrlqkdlrt ylasvkamhe askklneclq
       61 evyepdwpgr deankiaenn dllwmdyhqk lvdqalltmd tylgqfpdik sriakrgrkl
      121 vdydsarhhy eslqtakkkd eakiakpvsl lekaapqwcq gklqahlvaq tnllrnqaee
      181 elikaqkvfe emnvdlqeel pslwnsrvgf yvntfqsiag leenfhkems klnqnlndvl
      241 vglekqhgsn tftvkaqpsd napakgnksp sppdgspaat peirvnhepe paggatpgat
      301 lpkspsqlrk gppvppppkh tpskevkqeq ilslfedtfv peisvttpsq feapgpfseq
      361 aslldldfdp lppvtspvka ptpsgqsipw dlweptespa gslpsgepsa aegtfavswp
      421 sqtaepgpaq paeasevagg tqpaagaqep getaaseaas sslpavvvet fpatvngtve
      481 ggsgagrldl ppgfmfkvqa qhdytatdtd elqlkagdvv lvipfqnpee qdegwlmgvk
      541 esdwnqhkel ekcrgvfpen ftervp
//
LOCUS       NP_001354610             801 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform rr [Homo sapiens].
ACCESSION   NP_001354610
VERSION     NP_001354610.1
DBSOURCE    REFSEQ: accession NM_001367681.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 801)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 801)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 801)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 801)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142853 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..801
                     /product="SUN domain-containing protein 1 isoform rr"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=88910
     Region          12..307
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <381..>605
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          433..486
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(433,436..437,440,443..444,447..448,450..451,
                     454..455,457..458,461..462,464..465,468,471..472,475,
                     478..479,482..483,485..486)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          563..621
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          664..799
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..801
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367681.1:105..2510"
                     /note="isoform rr is encoded by transcript variant 44"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskgyfll
      241 qilrrigavg qavsrtawsa lwlavvapgk aasgvfwwlg igwyqfvtli swlnvflltr
      301 clrnickflv lliplfllla glslrgqgnf fsflpvlnwa smhrtqrvdd pqdvfkptts
      361 rlkqplqgds eafpwhwmsg veqqvaslsg qchhhgenlr elttllqklq arvdqmegga
      421 agpsasvrda vgqppretdf mafhqehevr mshledilgk lrekseaiqk eleqtkqkti
      481 savgeqllpt vehlqleldq lkselsswrh vktgcetvda vqervdvqvr emvkllfsed
      541 qqggsleqll qrfssqfvsk gdlqtmlrdl qlqilrnvth hvsvtkqlpt seavvsavse
      601 agasgiteaq araivnsalk lysqdktgmv dfalesgggs ilstrcsety etktalmslf
      661 giplwyfsqs prvviqpdiy pgncwafkgs qgylvvrlsm mihpaaftle hipktlsptg
      721 nissapkdfa vygleneyqe egqllgqfty dqdgeslqmf qalkrpddta fqivelrifs
      781 nwghpeytcl yrfrvhgepv k
//
LOCUS       NP_005181                283 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-C isoform a [Homo sapiens].
ACCESSION   NP_005181
VERSION     NP_005181.2
DBSOURCE    REFSEQ: accession NM_005190.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Lloyd,R.L., Urban,V., Munoz-Martinez,F., Ayestaran,I., Thomas,J.C.,
            de Renty,C., O'Connor,M.J., Forment,J.V., Galanty,Y. and
            Jackson,S.P.
  TITLE     Loss of Cyclin C or CDK8 provides ATR inhibitor resistance by
            suppressing transcription-associated replication stress
  JOURNAL   Nucleic Acids Res 49 (15), 8665-8683 (2021)
   PUBMED   34329458
  REMARK    GeneRIF: Loss of Cyclin C or CDK8 provides ATR inhibitor resistance
            by suppressing transcription-associated replication stress.
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Tang,M., Pei,G., Su,D., Wang,C., Feng,X., Srivastava,M., Chen,Z.,
            Zhao,Z. and Chen,J.
  TITLE     Genome-wide CRISPR screens reveal cyclin C as synthetic survival
            target of BRCA2
  JOURNAL   Nucleic Acids Res 49 (13), 7476-7491 (2021)
   PUBMED   34197614
  REMARK    GeneRIF: Genome-wide CRISPR screens reveal cyclin C as synthetic
            survival target of BRCA2.
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Tassan,J.P., Jaquenoud,M., Leopold,P., Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of human cyclin-dependent kinase 8, a putative
            protein kinase partner for cyclin C
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8871-8875 (1995)
   PUBMED   7568034
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Yoshizumi,M., Lee,W.S., Hsieh,C.M., Tsai,J.C., Li,J.,
            Perrella,M.A., Patterson,C., Endege,W.O., Schlegel,R. and Lee,M.E.
  TITLE     Disappearance of cyclin A correlates with permanent withdrawal of
            cardiomyocytes from the cell cycle in human and rat hearts
  JOURNAL   J Clin Invest 95 (5), 2275-2280 (1995)
   PUBMED   7738192
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Demetrick,D.J., Matsumoto,S., Hannon,G.J., Okamoto,K., Xiong,Y.,
            Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human cell cycle proteins
            cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 190-192 (1995)
   PUBMED   7698009
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Nozawa,T., Hatano,M., Yamamoto,H. and Kwan,T.
  TITLE     Magnetic circular dichroism on the reversible oxygenation of
            dimethylmesoporphyrin-IX-atopyridinecobalt (II)
  JOURNAL   Bioinorg Chem 5 (3), 267-273 (1976)
   PUBMED   1260071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC041123.1 and BC056153.1.
            
            On Mar 22, 2005 this sequence version replaced NP_005181.1.
            
            Summary: The protein encoded by this gene is a member of the cyclin
            family of proteins. The encoded protein interacts with
            cyclin-dependent kinase 8 and induces the phophorylation of the
            carboxy-terminal domain of the large subunit of RNA polymerase II.
            The level of mRNAs for this gene peaks in the G1 phase of the cell
            cycle. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.980579.1,
                                           SRR5189658.74859.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000520429.6/ ENSP00000428982.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.2"
     Protein         1..283
                     /product="cyclin-C isoform a"
                     /note="SRB11 homolog"
                     /calculated_mol_wt=33112
     Region          40..146
                     /region_name="CYCLIN_CCNC_rpt1"
                     /note="first cyclin box found in cyclin-C (CCNC) and
                     similar proteins; cd20513"
                     /db_xref="CDD:410217"
     Site            order(93,96..99,136..137,139..141,143..145)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410217"
     Region          154..245
                     /region_name="CYCLIN_CCNC_rpt2"
                     /note="second cyclin box found in cyclin-C (CCNC) and
                     similar proteins; cd20514"
                     /db_xref="CDD:410218"
     Region          252..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24863.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P24863.2)"
     CDS             1..283
                     /gene="CCNC"
                     /gene_synonym="CycC; hSRB11; SRB11"
                     /coded_by="NM_005190.4:134..985"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34502.1"
                     /db_xref="GeneID:892"
                     /db_xref="HGNC:HGNC:1581"
                     /db_xref="MIM:123838"
ORIGIN      
        1 magnfwqssh ylqwildkqd llkerqkdlk flseeeywkl qifftnviqa lgehlklrqq
       61 viatatvyfk rfyaryslks idpvlmaptc vflaskveef gvvsntrlia aatsvlktrf
      121 syafpkefpy rmnhilecef yllelmdccl ivyhpyrpll qyvqdmgqed mllplawriv
      181 ndtyrtdlcl lyppfmiala clhvacvvqq kdarqwfael svdmekilei irvilklyeq
      241 wknfderkem atilskmpkp kpppnsegeq gpngsqnssy sqs
//
LOCUS       NP_001354563             785 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001354563
VERSION     NP_001354563.1
DBSOURCE    REFSEQ: accession NM_001367634.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (72), as well as variants 1 and
            73, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN02400308
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..785
                     /product="SUN domain-containing protein 1 isoform a"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=86979
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <365..>589
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          417..470
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(417,420..421,424,427..428,431..432,434..435,
                     438..439,441..442,445..446,448..449,452,455..456,459,
                     462..463,466..467,469..470)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          547..605
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          648..783
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..785
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367634.1:392..2749"
                     /note="isoform a is encoded by transcript variant 72"
                     /db_xref="CCDS:CCDS47525.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllaglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl qgdseafpwh
      361 wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas vrdavgqppr
      421 etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq llptvehlql
      481 eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl eqllqrfssq
      541 fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi teaqaraivn
      601 salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy fsqsprvviq
      661 pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap kdfavyglen
      721 eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe ytclyrfrvh
      781 gepvk
//
LOCUS       NP_001162195             436 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 135 isoform 2 [Homo sapiens].
ACCESSION   NP_001162195
VERSION     NP_001162195.1
DBSOURCE    REFSEQ: accession NM_001168724.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Hu,D., Tan,M., Lu,D., Kleiboeker,B., Liu,X., Park,H., Kravitz,A.V.,
            Shoghi,K.I., Tseng,Y.H., Razani,B., Ikeda,A. and Lodhi,I.J.
  TITLE     TMEM135 links peroxisomes to the regulation of brown fat
            mitochondrial fission and energy homeostasis
  JOURNAL   Nat Commun 14 (1), 6099 (2023)
   PUBMED   37773161
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Wang,R., Zhang,M., Hu,Y., He,J., Lin,Q. and Peng,N.
  TITLE     MiR-100-5p inhibits osteogenic differentiation of human bone
            mesenchymal stromal cells by targeting TMEM135
  JOURNAL   Hum Cell 35 (6), 1671-1683 (2022)
   PUBMED   35947339
  REMARK    GeneRIF: MiR-100-5p inhibits osteogenic differentiation of human
            bone mesenchymal stromal cells by targeting TMEM135.
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Maharjan,Y., Lee,J.N., Kwak,S.A., Dutta,R.K., Park,C., Choe,S.K.
            and Park,R.
  TITLE     TMEM135 regulates primary ciliogenesis through modulation of
            intracellular cholesterol distribution
  JOURNAL   EMBO Rep 21 (5), e48901 (2020)
   PUBMED   32157776
  REMARK    GeneRIF: TMEM135 regulates primary ciliogenesis through modulation
            of intracellular cholesterol distribution.
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Zarsky,V. and Dolezal,P.
  TITLE     Evolution of the Tim17 protein family
  JOURNAL   Biol Direct 11 (1), 54 (2016)
   PUBMED   27760563
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Moayyeri,A., Hsu,Y.H., Karasik,D., Estrada,K., Xiao,S.M.,
            Nielson,C., Srikanth,P., Giroux,S., Wilson,S.G., Zheng,H.F.,
            Smith,A.V., Pye,S.R., Leo,P.J., Teumer,A., Hwang,J.Y., Ohlsson,C.,
            McGuigan,F., Minster,R.L., Hayward,C., Olmos,J.M.,
            Lyytikainen,L.P., Lewis,J.R., Swart,K.M., Masi,L., Oldmeadow,C.,
            Holliday,E.G., Cheng,S., van Schoor,N.M., Harvey,N.C., Kruk,M., del
            Greco,M. F, Igl,W., Trummer,O., Grigoriou,E., Luben,R., Liu,C.T.,
            Zhou,Y., Oei,L., Medina-Gomez,C., Zmuda,J., Tranah,G., Brown,S.J.,
            Williams,F.M., Soranzo,N., Jakobsdottir,J., Siggeirsdottir,K.,
            Holliday,K.L., Hannemann,A., Go,M.J., Garcia,M., Polasek,O.,
            Laaksonen,M., Zhu,K., Enneman,A.W., McEvoy,M., Peel,R., Sham,P.C.,
            Jaworski,M., Johansson,A., Hicks,A.A., Pludowski,P., Scott,R.,
            Dhonukshe-Rutten,R.A., van der Velde,N., Kahonen,M., Viikari,J.S.,
            Sievanen,H., Raitakari,O.T., Gonzalez-Macias,J., Hernandez,J.L.,
            Mellstrom,D., Ljunggren,O., Cho,Y.S., Volker,U., Nauck,M.,
            Homuth,G., Volzke,H., Haring,R., Brown,M.A., McCloskey,E.,
            Nicholson,G.C., Eastell,R., Eisman,J.A., Jones,G., Reid,I.R.,
            Dennison,E.M., Wark,J., Boonen,S., Vanderschueren,D., Wu,F.C.,
            Aspelund,T., Richards,J.B., Bauer,D., Hofman,A., Khaw,K.T.,
            Dedoussis,G., Obermayer-Pietsch,B., Gyllensten,U.,
            Pramstaller,P.P., Lorenc,R.S., Cooper,C., Kung,A.W., Lips,P.,
            Alen,M., Attia,J., Brandi,M.L., de Groot,L.C., Lehtimaki,T.,
            Riancho,J.A., Campbell,H., Liu,Y., Harris,T.B., Akesson,K.,
            Karlsson,M., Lee,J.Y., Wallaschofski,H., Duncan,E.L., O'Neill,T.W.,
            Gudnason,V., Spector,T.D., Rousseau,F., Orwoll,E., Cummings,S.R.,
            Wareham,N.J., Rivadeneira,F., Uitterlinden,A.G., Prince,R.L.,
            Kiel,D.P., Reeve,J. and Kaptoge,S.K.
  TITLE     Genetic determinants of heel bone properties: genome-wide
            association meta-analysis and replication in the GEFOS/GENOMOS
            consortium
  JOURNAL   Hum Mol Genet 23 (11), 3054-3068 (2014)
   PUBMED   24430505
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Exil,V.J., Silva Avila,D., Benedetto,A., Exil,E.A., Adams,M.R.,
            Au,C. and Aschner,M.
  TITLE     Stressed-induced TMEM135 protein is part of a conserved genetic
            network involved in fat storage and longevity regulation in
            Caenorhabditis elegans
  JOURNAL   PLoS One 5 (12), e14228 (2010)
   PUBMED   21151927
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Schrader,M. and Fahimi,H.D.
  TITLE     The peroxisome: still a mysterious organelle
  JOURNAL   Histochem Cell Biol 129 (4), 421-440 (2008)
   PUBMED   18274771
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Pei,L.
  TITLE     Pituitary tumor-transforming gene protein associates with ribosomal
            protein S10 and a novel human homologue of DnaJ in testicular cells
  JOURNAL   J Biol Chem 274 (5), 3151-3158 (1999)
   PUBMED   9915854
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX648678.1, AP000811.4 and DB325683.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            encoded isoform (2) is shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648678.1, SRR1803613.172771.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..436
                     /product="transmembrane protein 135 isoform 2"
                     /note="peroxisomal membrane protein 52; peroxisomal
                     protein 52"
                     /calculated_mol_wt=49783
     Region          9..132
                     /region_name="TMEM135_C_rich"
                     /note="N-terminal cysteine-rich region of Transmembrane
                     protein 135; pfam15982"
                     /db_xref="CDD:374269"
     Region          <277..329
                     /region_name="Tim17"
                     /note="Tim17/Tim22/Tim23/Pmp24 family; pfam02466"
                     /db_xref="CDD:460567"
     CDS             1..436
                     /gene="TMEM135"
                     /gene_synonym="PMP52"
                     /coded_by="NM_001168724.2:113..1423"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53692.1"
                     /db_xref="GeneID:65084"
                     /db_xref="HGNC:HGNC:26167"
                     /db_xref="MIM:616360"
ORIGIN      
        1 maalsksiph ncyeightwh pscrvsflqi tggaleeslk iyaplyliaa ilrkrkldyy
       61 lhkllpeilq sasfltanga lymaffcilr kilgkfyswt pgfgaalpas yvailierks
      121 rrglltiyma nlvllfcita amymfffrck dglkgftfsa lrfivgkeei pthsfspeaa
      181 yakveqkreq heekpgrmnm iglvrkfvds ickhgprhrc ckhyedncis ycikgfirmf
      241 svgyliqccl ripsafrhlf tqpsrllslf ynkenfqlga flgsfvsiyk gtscflrwir
      301 nlddelhaii agflagismm fyksttismy lasklvetmy fkgieagkvp yfphadtiiy
      361 sistaicfqa avmevqtlrp sywkfllrlt kgkfavmnrk vldvfgtgas khfqdfiprl
      421 dpryttvtpe lptefs
//
LOCUS       NP_001239004             224 aa            linear   PRI 20-NOV-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF2 isoform d [Homo
            sapiens].
ACCESSION   NP_001239004
VERSION     NP_001239004.1
DBSOURCE    REFSEQ: accession NM_001252075.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Zizak,M., Lamprecht,G., Steplock,D., Tariq,N., Shenolikar,S.,
            Donowitz,M., Yun,C.H. and Weinman,E.J.
  TITLE     cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger
            3 (NHE3) are dependent on the presence but not the phosphorylation
            of NHE regulatory factor
  JOURNAL   J Biol Chem 274 (35), 24753-24758 (1999)
   PUBMED   10455146
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Imai,K., Sarker,A.H., Akiyama,K., Ikeda,S., Yao,M., Tsutsui,K.,
            Shohmori,T. and Seki,S.
  TITLE     Genomic structure and sequence of a human homologue (NTHL1/NTH1) of
            Escherichia coli endonuclease III with those of the adjacent parts
            of TSC2 and SLC9A3R2 genes
  JOURNAL   Gene 222 (2), 287-295 (1998)
   PUBMED   9831664
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Yun,C.H., Lamprecht,G., Forster,D.V. and Sidor,A.
  TITLE     NHE3 kinase A regulatory protein E3KARP binds the epithelial brush
            border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin
  JOURNAL   J Biol Chem 273 (40), 25856-25863 (1998)
   PUBMED   9748260
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Hall,R.A., Ostedgaard,L.S., Premont,R.T., Blitzer,J.T., Rahman,N.,
            Welsh,M.J. and Lefkowitz,R.J.
  TITLE     A C-terminal motif found in the beta2-adrenergic receptor, P2Y1
            receptor and cystic fibrosis transmembrane conductance regulator
            determines binding to the Na+/H+ exchanger regulatory factor family
            of PDZ proteins
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8496-8501 (1998)
   PUBMED   9671706
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Yun,C.H., Oh,S., Zizak,M., Steplock,D., Tsao,S., Tse,C.M.,
            Weinman,E.J. and Donowitz,M.
  TITLE     cAMP-mediated inhibition of the epithelial brush border Na+/H+
            exchanger, NHE3, requires an associated regulatory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3010-3015 (1997)
   PUBMED   9096337
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1997 Sep 2;94(18):10006]
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Poulat,F., de Santa Barbara,P., Desclozeaux,M., Soullier,S.,
            Moniot,B., Bonneaud,N., Boizet,B. and Berta,P.
  TITLE     The human testis determining factor SRY binds a nuclear factor
            containing PDZ protein interaction domains
  JOURNAL   J Biol Chem 272 (11), 7167-7172 (1997)
   PUBMED   9054412
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961565.1 and AC093513.3.
            
            Summary: This gene encodes a member of the NHERF family of PDZ
            scaffolding proteins. These proteins mediate many cellular
            processes by binding to and regulating the membrane expression and
            protein-protein interactions of membrane receptors and transport
            proteins. The encoded protein plays a role in intestinal sodium
            absorption by regulating the activity of the sodium/hydrogen
            exchanger 3, and may also regulate the cystic fibrosis
            transmembrane regulator (CFTR) ion channel. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (d) is shorter and has a distinct N-terminus, compared to isoform
            a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.1253489.1,
                                           DRR138524.1185176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..224
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF2
                     isoform d"
                     /note="solute carrier family 9, subfamily A (NHE3, cation
                     proton antiporter 3), member 3 regulator 2; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF2; SRY-interacting
                     protein 1; tyrosine kinase activator protein 1; NHE3
                     kinase A regulatory protein E3KARP; NHE3 regulatory factor
                     2; SLC9A3 regulator 2; sodium/hydrogen exchanger 3 kinase
                     A regulatory protein; solute carrier family 9
                     (sodium/hydrogen exchanger), member 3 regulator 2;
                     Na(+)/H(+) exchange regulatory cofactor 2"
                     /calculated_mol_wt=24359
     Region          37..116
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(47..53,64,67,96,100,103..104)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          119..224
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     CDS             1..224
                     /gene="NHERF2"
                     /gene_synonym="E3KARP; NHE3RF2; NHERF-2; OCTS2; SIP-1;
                     SIP1; SLC9A3R2; TKA-1"
                     /coded_by="NM_001252075.2:59..733"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:9351"
                     /db_xref="HGNC:HGNC:11076"
                     /db_xref="MIM:606553"
ORIGIN      
        1 marsgsatpp arapgapprs ppqrldvsgp lrelrprlch lrkgpqgygf nlhsdksrpg
       61 qyirsvdpgs paarsglraq drlievngqn veglrhaevv asikaredea rllvvdpetd
      121 ehfkrlrvtp teehvegplp spvtngtspa qlnggsacss rsdlpgsdkd tedgsawkqd
      181 pfqesglhls ptaaeakeka ramrvnkrap qmdwnrkrei fsnf
//
LOCUS       NP_001354595             866 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform cc [Homo sapiens].
ACCESSION   NP_001354595
VERSION     NP_001354595.1
DBSOURCE    REFSEQ: accession NM_001367666.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 866)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 866)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 866)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 866)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 866)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 866)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 866)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 866)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 866)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 866)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.144380.1,
                                           SRR1660803.148636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..866
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..866
                     /product="SUN domain-containing protein 1 isoform cc"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=96086
     Region          12..372
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          498..551
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(498,501..502,505,508..509,512..513,515..516,
                     519..520,522..523,526..527,529..530,533,536..537,540,
                     543..544,547..548,550..551)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          510..>643
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          628..686
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          729..864
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..866
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367666.1:105..2705"
                     /note="isoform cc is encoded by transcript variant 29"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy
      241 ygrmnvrevl redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca
      301 gyfllqilrr igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv
      361 flltrclrni ckflvllipl flllaglslr gqgnffsflp vlnwasmhrt qrvddpqdvf
      421 kpttsrlkqp lqgdseafpw hwmsgveqqv aslsgqchhh genlrelttl lqklqarvdq
      481 meggaagpsa svrdavgqpp retdfmafhq ehevrmshle dilgklreks eaiqkeleqt
      541 kqktisavge qllptvehlq leldqlksel sswrhvktgc etvdavqerv dvqvremvkl
      601 lfsedqqggs leqllqrfss qfvskgdlqt mlrdlqlqil rnvthhvsvt kqlptseavv
      661 savseagasg iteaqaraiv nsalklysqd ktgmvdfale sgggsilstr csetyetkta
      721 lmslfgiplw yfsqsprvvi qpdiypgncw afkgsqgylv vrlsmmihpa aftlehipkt
      781 lsptgnissa pkdfavygle neyqeegqll gqftydqdge slqmfqalkr pddtafqive
      841 lrifsnwghp eytclyrfrv hgepvk
//
LOCUS       NP_006504                514 aa            linear   PRI 20-NOV-2025
DEFINITION  serine--tRNA ligase, cytoplasmic isoform a [Homo sapiens].
ACCESSION   NP_006504
VERSION     NP_006504.2
DBSOURCE    REFSEQ: accession NM_006513.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Throll,P., G Dolce,L., Rico-Lastres,P., Arnold,K., Tengo,L.,
            Basu,S., Kaiser,S., Schneider,R. and Kowalinski,E.
  TITLE     Structural basis of tRNA recognition by the m3C RNA
            methyltransferase METTL6 in complex with SerRS seryl-tRNA
            synthetase
  JOURNAL   Nat Struct Mol Biol 31 (10), 1614-1624 (2024)
   PUBMED   38918637
  REMARK    Erratum:[Nat Struct Mol Biol. 2025 Feb;32(2):405. doi:
            10.1038/s41594-025-01508-6. PMID: 39905155]
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Liu,Z., Wang,J., Shi,Y., Yee,B.A., Terrey,M., Zhang,Q., Lee,J.C.,
            Lin,K.I., Wang,A.H., Ackerman,S.L., Yeo,G.W., Cui,H. and Yang,X.L.
  TITLE     Seryl-tRNA synthetase promotes translational readthrough by mRNA
            binding and involvement of the selenocysteine incorporation
            machinery
  JOURNAL   Nucleic Acids Res 51 (19), 10768-10781 (2023)
   PUBMED   37739431
  REMARK    GeneRIF: Seryl-tRNA synthetase promotes translational readthrough
            by mRNA binding and involvement of the selenocysteine incorporation
            machinery.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Verdura,E., Senger,B., Raspall-Chaure,M., Schluter,A., Launay,N.,
            Ruiz,M., Casasnovas,C., Rodriguez-Palmero,A., Macaya,A.,
            Becker,H.D. and Pujol,A.
  TITLE     Loss of seryl-tRNA synthetase (SARS1) causes complex spastic
            paraplegia and cellular senescence
  JOURNAL   J Med Genet 59 (12), 1227-1233 (2022)
   PUBMED   36041817
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Bogershausen,N., Krawczyk,H.E., Jamra,R.A., Lin,S.J., Yigit,G.,
            Huning,I., Polo,A.M., Vona,B., Huang,K., Schmidt,J., Altmuller,J.,
            Luppe,J., Platzer,K., Dorgeloh,B.B., Busche,A., Biskup,S.,
            Mendes,M.I., Smith,D.E.C., Salomons,G.S., Zibat,A., Bultmann,E.,
            Nurnberg,P., Spielmann,M., Lemke,J.R., Li,Y., Zenker,M.,
            Varshney,G.K., Hillen,H.S., Kratz,C.P. and Wollnik,B.
  TITLE     WARS1 and SARS1: Two tRNA synthetases implicated in autosomal
            recessive microcephaly
  JOURNAL   Hum Mutat 43 (10), 1454-1471 (2022)
   PUBMED   35790048
  REMARK    GeneRIF: WARS1 and SARS1: Two tRNA synthetases implicated in
            autosomal recessive microcephaly.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Ravel,J.M., Dreumont,N., Mosca,P., Smith,D.E.C., Mendes,M.I.,
            Wiedemann,A., Coelho,D., Schmitt,E., Riviere,J.B., Tran
            Mau-Them,F., Thevenon,J., Kuentz,P., Polivka,M., Fuchs,S.A.,
            Kok,G., Thauvin-Robinet,C., Gueant,J.L., Salomons,G.S., Faivre,L.
            and Feillet,F.
  TITLE     A bi-allelic loss-of-function SARS1 variant in children with
            neurodevelopmental delay, deafness, cardiomyopathy, and
            decompensation during fever
  JOURNAL   Hum Mutat 42 (12), 1576-1583 (2021)
   PUBMED   34570399
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Shimada,N., Suzuki,T. and Watanabe,K.
  TITLE     Dual mode recognition of two isoacceptor tRNAs by mammalian
            mitochondrial seryl-tRNA synthetase
  JOURNAL   J Biol Chem 276 (50), 46770-46778 (2001)
   PUBMED   11577083
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Shah,Z.H., Toompuu,M., Hakkinen,T., Rovio,A.T., van Ravenswaay,C.,
            De Leenheer,E.M., Smith,R.J., Cremers,F.P., Cremers,C.W. and
            Jacobs,H.T.
  TITLE     Novel coding-region polymorphisms in mitochondrial seryl-tRNA
            synthetase (SARSM) and mitoribosomal protein S12 (RPMS12) genes in
            DFNA4 autosomal dominant deafness families
  JOURNAL   Hum Mutat 17 (5), 433-434 (2001)
   PUBMED   11317363
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Heckl,M., Busch,K. and Gross,H.J.
  TITLE     Minimal tRNA(Ser) and tRNA(Sec) substrates for human seryl-tRNA
            synthetase: contribution of tRNA domains to serylation and tertiary
            structure
  JOURNAL   FEBS Lett 427 (3), 315-319 (1998)
   PUBMED   9637248
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Vincent,C., Tarbouriech,N. and Hartlein,M.
  TITLE     Genomic organization, cDNA sequence, bacterial expression, and
            purification of human seryl-tRNA synthase
  JOURNAL   Eur J Biochem 250 (1), 77-84 (1997)
   PUBMED   9431993
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Hartlein,M. and Cusack,S.
  TITLE     Structure, function and evolution of seryl-tRNA synthetases:
            implications for the evolution of aminoacyl-tRNA synthetases and
            the genetic code
  JOURNAL   J Mol Evol 40 (5), 519-530 (1995)
   PUBMED   7540217
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC111398.1, BC009390.2 and
            BM666450.1.
            
            On Oct 22, 2001 this sequence version replaced NP_006504.1.
            
            Summary: This gene belongs to the class II amino-acyl tRNA family.
            The encoded enzyme catalyzes the transfer of L-serine to tRNA (Ser)
            and is related to bacterial and yeast counterparts. Multiple
            alternatively spliced transcript variants have been described but
            the biological validity of all variants is unknown. [provided by
            RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) lacks an alternate in-frame
            exon compared to variant 3. The resulting isoform (a) has the same
            N- and C-termini but is shorter compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.274910.1,
                                           SRR5189658.83431.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234677.7/ ENSP00000234677.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..514
                     /product="serine--tRNA ligase, cytoplasmic isoform a"
                     /EC_number="6.1.1.11"
                     /note="serine tRNA ligase 1, cytoplasmic; seryl-tRNA
                     synthetase, cytoplasmic; seryl-tRNA(Ser/Sec) synthetase;
                     serine--tRNA ligase, cytoplasmic"
                     /calculated_mol_wt=58646
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Region          3..486
                     /region_name="PLN02678"
                     /note="seryl-tRNA synthetase"
                     /db_xref="CDD:215364"
     Region          9..61
                     /region_name="Interaction with tRNA.
                     /evidence=ECO:0000269|PubMed:26433229"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Site            323
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Site            429
                     /site_type="other"
                     /note="Important for serine binding.
                     /evidence=ECO:0000269|PubMed:28236339; propagated from
                     UniProtKB/Swiss-Prot (P49591.3)"
     Region          473..514
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     Region          482..494
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:22353712"
                     /note="propagated from UniProtKB/Swiss-Prot (P49591.3)"
     CDS             1..514
                     /gene="SARS1"
                     /gene_synonym="NEDMAS; SARS; SERRS; SERS"
                     /coded_by="NM_006513.4:76..1620"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS795.1"
                     /db_xref="GeneID:6301"
                     /db_xref="HGNC:HGNC:10537"
                     /db_xref="MIM:607529"
ORIGIN      
        1 mvldldlfrv dkggdpalir etqekrfkdp glvdqlvkad sewrrcrfra dnlnklknlc
       61 sktigekmkk kepvgddesv penvlsfddl tadalanlkv sqikkvrlli deailkcdae
      121 rikleaerfe nlreignllh psvpisnded vdnkveriwg dctvrkkysh vdlvvmvdgf
      181 egekgavvag srgyflkgvl vfleqaliqy alrtlgsrgy ipiytpffmr kevmqevaql
      241 sqfdeelykv igkgseksdd nsydekylia tseqpiaalh rdewlrpedl pikyaglstc
      301 frqevgshgr dtrgifrvhq fekieqfvys sphdnkswem feemittaee fyqslgipyh
      361 ivnivsgsln haaskkldle awfpgsgafr elvscsnctd yqarrlriry gqtkkmmdkv
      421 efvhmlnatm cattrticai lenyqtekgi tvpeklkefm ppglqelipf vkpapieqep
      481 skkqkkqheg skkkaaardv tlenrlqnme vtda
//
LOCUS       NP_001284644             282 aa            linear   PRI 20-NOV-2025
DEFINITION  survival motor neuron protein isoform a [Homo sapiens].
ACCESSION   NP_001284644 XP_005248632 XP_005276832 XP_006714740
VERSION     NP_001284644.1
DBSOURCE    REFSEQ: accession NM_001297715.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Nurputra,D.K., Sofian,J., Iskandar,K., Triono,A., Herini,E.S.,
            Sunartini and Ulhaq,Z.S.
  TITLE     Multidisciplinary approach on divergent outcomes in spinal muscular
            atrophies: comparing DYNC1H1 and SMN1 gene mutations
  JOURNAL   Neurol Sci 45 (9), 4583-4588 (2024)
   PUBMED   38806879
  REMARK    GeneRIF: Multidisciplinary approach on divergent outcomes in spinal
            muscular atrophies: comparing DYNC1H1 and SMN1 gene mutations.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Polverini,E., Squeri,P. and Gherardi,V.
  TITLE     Effect of E134K pathogenic mutation of SMN protein on SMN-SmD1
            interaction, with implication in spinal muscular atrophy: A
            molecular dynamics study
  JOURNAL   Int J Biol Macromol 275 (Pt 2), 133663 (2024)
   PUBMED   38969036
  REMARK    GeneRIF: Effect of E134K pathogenic mutation of SMN protein on
            SMN-SmD1 interaction, with implication in spinal muscular atrophy:
            A molecular dynamics study.
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Li,L., Menezes,M.P., Smith,M., Forbes,R., Zuchner,S., Burgess,A.,
            Woodcock,I.R., Delatycki,M.B. and Yiu,E.M.
  TITLE     Rare homozygous disease-associated sequence variants in children
            with spinal muscular atrophy: a phenotypic description and review
            of the literature
  JOURNAL   Neuromuscul Disord 37, 29-35 (2024)
   PUBMED   38520993
  REMARK    GeneRIF: Rare homozygous disease-associated sequence variants in
            children with spinal muscular atrophy: a phenotypic description and
            review of the literature.
            Review article
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Valsecchi,V., Errico,F., Bassareo,V., Marino,C., Nuzzo,T.,
            Brancaccio,P., Laudati,G., Casamassa,A., Grimaldi,M., D'Amico,A.,
            Carta,M., Bertini,E., Pignataro,G., D'Ursi,A.M. and Usiello,A.
  TITLE     SMN deficiency perturbs monoamine neurotransmitter metabolism in
            spinal muscular atrophy
  JOURNAL   Commun Biol 6 (1), 1155 (2023)
   PUBMED   37957344
  REMARK    GeneRIF: SMN deficiency perturbs monoamine neurotransmitter
            metabolism in spinal muscular atrophy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Bussaglia,E., Clermont,O., Tizzano,E., Lefebvre,S., Burglen,L.,
            Cruaud,C., Urtizberea,J.A., Colomer,J., Munnich,A., Baiget,M. et
            al.
  TITLE     A frame-shift deletion in the survival motor neuron gene in Spanish
            spinal muscular atrophy patients
  JOURNAL   Nat Genet 11 (3), 335-337 (1995)
   PUBMED   7581461
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Gennarelli,M., Lucarelli,M., Capon,F., Pizzuti,A., Merlini,L.,
            Angelini,C., Novelli,G. and Dallapiccola,B.
  TITLE     Survival motor neuron gene transcript analysis in muscles from
            spinal muscular atrophy patients
  JOURNAL   Biochem Biophys Res Commun 213 (1), 342-348 (1995)
   PUBMED   7639755
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Lefebvre,S., Burglen,L., Reboullet,S., Clermont,O., Burlet,P.,
            Viollet,L., Benichou,B., Cruaud,C., Millasseau,P., Zeviani,M. et
            al.
  TITLE     Identification and characterization of a spinal muscular
            atrophy-determining gene
  JOURNAL   Cell 80 (1), 155-165 (1995)
   PUBMED   7813012
REFERENCE   9  (residues 1 to 282)
  AUTHORS   van der Steege,G., Draaijers,T.G., Grootscholten,P.M., Osinga,J.,
            Anzevino,R., Velona,I., Den Dunnen,J.T., Scheffer,H., Brahe,C., van
            Ommen,G.J. et al.
  TITLE     A provisional transcript map of the spinal muscular atrophy (SMA)
            critical region
  JOURNAL   Eur J Hum Genet 3 (2), 87-95 (1995)
   PUBMED   7552146
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Prior,T.W., Leach,M.E. and Finanger,E.L.
  TITLE     Spinal Muscular Atrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301526
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139834.2 and AC044797.5.
            
            On or before Jul 10, 2014 this sequence version replaced
            XP_006714740.1, XP_005248632.1, XP_005276832.1.
            
            Summary: This gene is part of a 500 kb inverted duplication on
            chromosome 5q13. This duplicated region contains at least four
            genes and repetitive elements which make it prone to rearrangements
            and deletions. The repetitiveness and complexity of the sequence
            have also caused difficulty in determining the organization of this
            genomic region. The telomeric and centromeric copies of this gene
            are nearly identical and encode the same protein. However,
            mutations in this gene, the telomeric copy, are associated with
            spinal muscular atrophy; mutations in the centromeric copy do not
            lead to disease. The centromeric copy may be a modifier of disease
            caused by mutation in the telomeric copy. The critical sequence
            difference between the two genes is a single nucleotide in exon 7,
            which is thought to be an exon splice enhancer. Note that the nine
            exons of both the telomeric and centromeric copies are designated
            historically as exon 1, 2a, 2b, and 3-8. It is thought that gene
            conversion events may involve the two genes, leading to varying
            copy numbers of each gene. The protein encoded by this gene
            localizes to both the cytoplasm and the nucleus. Within the
            nucleus, the protein localizes to subnuclear bodies called gems
            which are found near coiled bodies containing high concentrations
            of small ribonucleoproteins (snRNPs). This protein forms
            heteromeric complexes with proteins such as SIP1 and GEMIN4, and
            also interacts with several proteins known to be involved in the
            biogenesis of snRNPs, such as hnRNP U protein and the small
            nucleolar RNA binding protein. Multiple transcript variants
            encoding distinct isoforms have been described. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (a) lacks the penultimate exon,
            which results in an alternate translation stop codon, compared to
            variant d. The resulting isoform (a) is shorter and has a distinct
            C-terminus, compared to isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.254111.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..282
                     /product="survival motor neuron protein isoform a"
                     /note="gemin-1; component of gems 1; survival motor neuron
                     1 protein; tudor domain containing 16A"
                     /calculated_mol_wt=30319
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          26..278
                     /region_name="SMN"
                     /note="Survival motor neuron protein (SMN); pfam06003"
                     /db_xref="CDD:428716"
     Region          26..51
                     /region_name="Interacts with GEMIN2.
                     /evidence=ECO:0000269|PubMed:21816274,
                     ECO:0000269|PubMed:22607171, ECO:0000269|PubMed:26092730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          59..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            69
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          97..209
                     /region_name="Required for interaction with RPP20/POP7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Region          156..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21609790; propagated from
                     UniProtKB/Swiss-Prot (Q16637.1)"
     Region          240..267
                     /region_name="P2 (binding site for SNRPB)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16637.1)"
     CDS             1..282
                     /gene="SMN1"
                     /gene_synonym="BCD541; GEMIN1; SMA; SMA1; SMA2; SMA3;
                     SMA4; SMA@; SMN; SMNT; T-BCD541; TDRD16A"
                     /coded_by="NM_001297715.1:164..1012"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS75256.1"
                     /db_xref="GeneID:6606"
                     /db_xref="HGNC:HGNC:11117"
                     /db_xref="MIM:600354"
ORIGIN      
        1 mamssggsgg gvpeqedsvl frrgtgqsdd sdiwddtali kaydkavasf khalkngdic
       61 etsgkpkttp krkpakknks qkkntaaslq qwkvgdkcsa iwsedgciyp atiasidfkr
      121 etcvvvytgy gnreeqnlsd llspicevan nieqnaqene nesqvstdes ensrspgnks
      181 dnikpksapw nsflpppppm pgprlgpgkp glkfngpppp pppppphlls cwlppfpsgp
      241 piipppppic pdslddadal gsmliswyms gyhtgyymem la
//
LOCUS       NP_001193845             483 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit beta-3 isoform 3
            [Homo sapiens].
ACCESSION   NP_001193845
VERSION     NP_001193845.1
DBSOURCE    REFSEQ: accession NM_001206916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Chen,Z., Mondal,A., Abderemane-Ali,F., Jang,S., Niranjan,S.,
            Montano,J.L., Zaro,B.W. and Minor,D.L. Jr.
  TITLE     EMC chaperone-CaV structure reveals an ion channel assembly
            intermediate
  JOURNAL   Nature 619 (7969), 410-419 (2023)
   PUBMED   37196677
  REMARK    GeneRIF: EMC chaperone-CaV structure reveals an ion channel
            assembly intermediate.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Murakami,M., Wissenbach,U. and Flockerzi,V.
  TITLE     Gene structure of the murine calcium channel beta3 subunit, cDNA
            and characterization of alternative splicing and transcription
            products
  JOURNAL   Eur J Biochem 236 (1), 138-143 (1996)
   PUBMED   8617257
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Scott,V.E., De Waard,M., Liu,H., Gurnett,C.A., Venzke,D.P.,
            Lennon,V.A. and Campbell,K.P.
  TITLE     Beta subunit heterogeneity in N-type Ca2+ channels
  JOURNAL   J Biol Chem 271 (6), 3207-3212 (1996)
   PUBMED   8621722
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Yamada,Y., Masuda,K., Li,Q., Ihara,Y., Kubota,A., Miura,T.,
            Nakamura,K., Fujii,Y., Seino,S. and Seino,Y.
  TITLE     The structures of the human calcium channel alpha 1 subunit
            (CACNL1A2) and beta subunit (CACNLB3) genes
  JOURNAL   Genomics 27 (2), 312-319 (1995)
   PUBMED   7557998
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Collin,T., Lory,P., Taviaux,S., Courtieu,C., Guilbault,P., Berta,P.
            and Nargeot,J.
  TITLE     Cloning, chromosomal location and functional expression of the
            human voltage-dependent calcium-channel beta 3 subunit
  JOURNAL   Eur J Biochem 220 (1), 257-262 (1994)
   PUBMED   8119293
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Rosenfeld,M.R., Wong,E., Dalmau,J., Manley,G., Posner,J.B., Sher,E.
            and Furneaux,H.M.
  TITLE     Cloning and characterization of a Lambert-Eaton myasthenic syndrome
            antigen
  JOURNAL   Ann Neurol 33 (1), 113-120 (1993)
   PUBMED   8494331
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB277524.1, AK316323.1 and
            AC117498.6.
            
            Summary: This gene encodes a regulatory beta subunit of the
            voltage-dependent calcium channel. Beta subunits are composed of
            five domains, which contribute to the regulation of surface
            expression and gating of calcium channels and may also play a role
            in the regulation of transcription factors and calcium transport.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (3) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.918729.1,
                                           SRR7410570.498529.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..483
                     /product="voltage-dependent L-type calcium channel subunit
                     beta-3 isoform 3"
                     /note="voltage-dependent L-type calcium channel subunit
                     beta-3; calcium channel, voltage-dependent, beta 3
                     subunit"
                     /calculated_mol_wt=54225
     Region          15..57
                     /region_name="VGCC_beta4Aa_N"
                     /note="Voltage gated calcium channel subunit beta domain
                     4Aa N terminal; pfam12052"
                     /db_xref="CDD:463445"
     Region          57..124
                     /region_name="SH3_CACNB3"
                     /note="Src Homology 3 domain of Voltage-dependent L-type
                     calcium channel subunit beta3; cd12042"
                     /db_xref="CDD:212975"
     Site            order(67,69,72,83,101..102,118,120..121)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212975"
     Region          175..355
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..483
                     /gene="CACNB3"
                     /gene_synonym="CAB3; CACNLB3"
                     /coded_by="NM_001206916.2:114..1565"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55822.1"
                     /db_xref="GeneID:784"
                     /db_xref="HGNC:HGNC:1403"
                     /db_xref="MIM:601958"
ORIGIN      
        1 msfsdssatf llnegsadsy tsrpsldsdv sleedresar revesqaqqq lerakhkpva
       61 favrtnvsyc gvldeecpvq gsgvnfeakd flhikekysn dwwigrlvke ggdiafipsp
      121 qrlesirlkq eqkarrsgnp sslsdignrr spppslakqk qkqaehvppy dvvpsmrpvv
      181 lvgpslkgye vtdmmqkalf dflkhrfdgr isitrvtadl slakrsvlnn pgkrtiiers
      241 sarssiaevq seierifela kslqlvvlda dtinhpaqla ktslapiivf vkvsspkvlq
      301 rlirsrgksq mkhltvqmma ydklvqcppe sfdvildenq ledacehlae ylevywrath
      361 hpapgpgllg ppsaipglqn qqllgergee hsplerdslm psdeasessr qawtgssqrs
      421 srhleedyad ayqdlyqphr qhtsglpsan ghdpqdrlla qdsehnhsdr nwqrnrpwpk
      481 dsy
//
LOCUS       NP_001310188             210 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 32 isoform k [Homo sapiens].
ACCESSION   NP_001310188
VERSION     NP_001310188.1
DBSOURCE    REFSEQ: accession NM_001323259.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Simino,J., Shi,G., Bis,J.C., Chasman,D.I., Ehret,G.B., Gu,X.,
            Guo,X., Hwang,S.J., Sijbrands,E., Smith,A.V., Verwoert,G.C.,
            Bragg-Gresham,J.L., Cadby,G., Chen,P., Cheng,C.Y., Corre,T., de
            Boer,R.A., Goel,A., Johnson,T., Khor,C.C., Lluis-Ganella,C.,
            Luan,J., Lyytikainen,L.P., Nolte,I.M., Sim,X., Sober,S., van der
            Most,P.J., Verweij,N., Zhao,J.H., Amin,N., Boerwinkle,E.,
            Bouchard,C., Dehghan,A., Eiriksdottir,G., Elosua,R., Franco,O.H.,
            Gieger,C., Harris,T.B., Hercberg,S., Hofman,A., James,A.L.,
            Johnson,A.D., Kahonen,M., Khaw,K.T., Kutalik,Z., Larson,M.G.,
            Launer,L.J., Li,G., Liu,J., Liu,K., Morrison,A.C., Navis,G.,
            Ong,R.T., Papanicolau,G.J., Penninx,B.W., Psaty,B.M., Raffel,L.J.,
            Raitakari,O.T., Rice,K., Rivadeneira,F., Rose,L.M., Sanna,S.,
            Scott,R.A., Siscovick,D.S., Stolk,R.P., Uitterlinden,A.G.,
            Vaidya,D., van der Klauw,M.M., Vasan,R.S., Vithana,E.N., Volker,U.,
            Volzke,H., Watkins,H., Young,T.L., Aung,T., Bochud,M., Farrall,M.,
            Hartman,C.A., Laan,M., Lakatta,E.G., Lehtimaki,T., Loos,R.J.,
            Lucas,G., Meneton,P., Palmer,L.J., Rettig,R., Snieder,H., Tai,E.S.,
            Teo,Y.Y., van der Harst,P., Wareham,N.J., Wijmenga,C., Wong,T.Y.,
            Fornage,M., Gudnason,V., Levy,D., Palmas,W., Ridker,P.M.,
            Rotter,J.I., van Duijn,C.M., Witteman,J.C., Chakravarti,A. and
            Rao,D.C.
  CONSRTM   LifeLines Cohort Study
  TITLE     Gene-age interactions in blood pressure regulation: a large-scale
            investigation with the CHARGE, Global BPgen, and ICBP Consortia
  JOURNAL   Am J Hum Genet 95 (1), 24-38 (2014)
   PUBMED   24954895
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Leone,M.A., Barizzone,N., Esposito,F., Lucenti,A., Harbo,H.F.,
            Goris,A., Kockum,I., Oturai,A.B., Celius,E.G., Mero,I.L.,
            Dubois,B., Olsson,T., Sondergaard,H.B., Cusi,D., Lupoli,S.,
            Andreassen,B.K., Myhr,K.M., Guerini,F.R., Comi,G.,
            Martinelli-Boneschi,F. and D'Alfonso,S.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2; PROGEMUS Group; PROGRESSO Group
  TITLE     Association of genetic markers with CSF oligoclonal bands in
            multiple sclerosis patients
  JOURNAL   PLoS One 8 (6), e64408 (2013)
   PUBMED   23785401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Monda,K.L., Chen,G.K., Taylor,K.C., Palmer,C., Edwards,T.L.,
            Lange,L.A., Ng,M.C., Adeyemo,A.A., Allison,M.A., Bielak,L.F.,
            Chen,G., Graff,M., Irvin,M.R., Rhie,S.K., Li,G., Liu,Y., Liu,Y.,
            Lu,Y., Nalls,M.A., Sun,Y.V., Wojczynski,M.K., Yanek,L.R.,
            Aldrich,M.C., Ademola,A., Amos,C.I., Bandera,E.V., Bock,C.H.,
            Britton,A., Broeckel,U., Cai,Q., Caporaso,N.E., Carlson,C.S.,
            Carpten,J., Casey,G., Chen,W.M., Chen,F., Chen,Y.D., Chiang,C.W.,
            Coetzee,G.A., Demerath,E., Deming-Halverson,S.L., Driver,R.W.,
            Dubbert,P., Feitosa,M.F., Feng,Y., Freedman,B.I., Gillanders,E.M.,
            Gottesman,O., Guo,X., Haritunians,T., Harris,T., Harris,C.C.,
            Hennis,A.J., Hernandez,D.G., McNeill,L.H., Howard,T.D.,
            Howard,B.V., Howard,V.J., Johnson,K.C., Kang,S.J., Keating,B.J.,
            Kolb,S., Kuller,L.H., Kutlar,A., Langefeld,C.D., Lettre,G.,
            Lohman,K., Lotay,V., Lyon,H., Manson,J.E., Maixner,W., Meng,Y.A.,
            Monroe,K.R., Morhason-Bello,I., Murphy,A.B., Mychaleckyj,J.C.,
            Nadukuru,R., Nathanson,K.L., Nayak,U., N'diaye,A., Nemesure,B.,
            Wu,S.Y., Leske,M.C., Neslund-Dudas,C., Neuhouser,M., Nyante,S.,
            Ochs-Balcom,H., Ogunniyi,A., Ogundiran,T.O., Ojengbede,O.,
            Olopade,O.I., Palmer,J.R., Ruiz-Narvaez,E.A., Palmer,N.D.,
            Press,M.F., Rampersaud,E., Rasmussen-Torvik,L.J.,
            Rodriguez-Gil,J.L., Salako,B., Schadt,E.E., Schwartz,A.G.,
            Shriner,D.A., Siscovick,D., Smith,S.B., Wassertheil-Smoller,S.,
            Speliotes,E.K., Spitz,M.R., Sucheston,L., Taylor,H., Tayo,B.O.,
            Tucker,M.A., Van Den Berg,D.J., Edwards,D.R., Wang,Z.,
            Wiencke,J.K., Winkler,T.W., Witte,J.S., Wrensch,M., Wu,X.,
            Yang,J.J., Levin,A.M., Young,T.R., Zakai,N.A., Cushman,M.,
            Zanetti,K.A., Zhao,J.H., Zhao,W., Zheng,Y., Zhou,J., Ziegler,R.G.,
            Zmuda,J.M., Fernandes,J.K., Gilkeson,G.S., Kamen,D.L., Hunt,K.J.,
            Spruill,I.J., Ambrosone,C.B., Ambs,S., Arnett,D.K., Atwood,L.,
            Becker,D.M., Berndt,S.I., Bernstein,L., Blot,W.J., Borecki,I.B.,
            Bottinger,E.P., Bowden,D.W., Burke,G., Chanock,S.J., Cooper,R.S.,
            Ding,J., Duggan,D., Evans,M.K., Fox,C., Garvey,W.T.,
            Bradfield,J.P., Hakonarson,H., Grant,S.F., Hsing,A., Chu,L.,
            Hu,J.J., Huo,D., Ingles,S.A., John,E.M., Jordan,J.M.,
            Kabagambe,E.K., Kardia,S.L., Kittles,R.A., Goodman,P.J.,
            Klein,E.A., Kolonel,L.N., Le Marchand,L., Liu,S., McKnight,B.,
            Millikan,R.C., Mosley,T.H., Padhukasahasram,B., Williams,L.K.,
            Patel,S.R., Peters,U., Pettaway,C.A., Peyser,P.A., Psaty,B.M.,
            Redline,S., Rotimi,C.N., Rybicki,B.A., Sale,M.M., Schreiner,P.J.,
            Signorello,L.B., Singleton,A.B., Stanford,J.L., Strom,S.S.,
            Thun,M.J., Vitolins,M., Zheng,W., Moore,J.H., Williams,S.M.,
            Ketkar,S., Zhu,X., Zonderman,A.B., Kooperberg,C.,
            Papanicolaou,G.J., Henderson,B.E., Reiner,A.P., Hirschhorn,J.N.,
            Loos,R.J., North,K.E. and Haiman,C.A.
  CONSRTM   NABEC Consortium; UKBEC Consortium; BioBank Japan Project; AGEN
            Consortium
  TITLE     A meta-analysis identifies new loci associated with body mass index
            in individuals of African ancestry
  JOURNAL   Nat Genet 45 (6), 690-696 (2013)
   PUBMED   23583978
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA296671.1, AK055292.1, DA255882.1, BC071627.1 and HY334128.1.
            
            Transcript Variant: This variant (14) lacks several 3' exons, but
            it contains an alternate 3' terminal exon and it thus differs in
            the 3' coding region and 3' UTR, compared to variant 1. The encoded
            isoform (k) has a distinct C-terminus and is shorter than isoform
            a. Both variants 13 and 14 encode isoform k.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.126918.1,
                                           SRR1803612.226206.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..210
                     /product="kelch-like protein 32 isoform k"
                     /note="BTB and kelch domain containing 5; kelch-like
                     protein 32"
                     /calculated_mol_wt=23517
     Region          14..146
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          139..>210
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     CDS             1..210
                     /gene="KLHL32"
                     /gene_synonym="BKLHD5; dJ21F7.1; KIAA1900; UG0030H05"
                     /coded_by="NM_001323259.2:365..997"
                     /note="isoform k is encoded by transcript variant 14"
                     /db_xref="GeneID:114792"
                     /db_xref="HGNC:HGNC:21221"
ORIGIN      
        1 mpserclsiq emltgqrlch seshndsvla alnqqrsdgi lcditliaee qkfhahkavl
       61 aacsdyfram fslcmvesga devnlhgvts lglkqalefa ytgqillepg viqdvlaags
      121 hlqllellnl cshyliqeln sfnyldlyrl adlfnltlle kavidflvkh lsellksrpe
      181 evltlpycll qevlksdrlt slseeqiwql
//
LOCUS       NP_000987                110 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL33 [Homo sapiens].
ACCESSION   NP_000987
VERSION     NP_000987.2
DBSOURCE    REFSEQ: accession NM_000996.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Wu,H., Xia,L., Sun,L., Li,D., Liu,X., Song,H., Sheng,J., Wang,K.
            and Feng,Q.
  TITLE     RPL35A drives ovarian cancer progression by promoting the binding
            of YY1 to CTCF promoter
  JOURNAL   J Cell Mol Med 28 (6), e18115 (2024)
   PUBMED   38436544
  REMARK    GeneRIF: RPL35A drives ovarian cancer progression by promoting the
            binding of YY1 to CTCF promoter.
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Zhang,C., Wang,Y., Wu,G., Sun,N., Bai,H., Li,X., Han,S., Zhou,H.,
            Qi,R. and Zhang,J.
  TITLE     RPL35A promotes the progression of cholangiocarcinoma by mediating
            HSPA8 ubiquitination
  JOURNAL   Biol Direct 19 (1), 16 (2024)
   PUBMED   38395908
  REMARK    GeneRIF: RPL35A promotes the progression of cholangiocarcinoma by
            mediating HSPA8 ubiquitination.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Colombo,P., Read,M. and Fried,M.
  TITLE     The human L35a ribosomal protein (RPL35A) gene is located at
            chromosome band 3q29-qter
  JOURNAL   Genomics 32 (1), 148-150 (1996)
   PUBMED   8786106
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 110)
  AUTHORS   Feo,S., Davies,B. and Fried,M.
  TITLE     The mapping of seven intron-containing ribosomal protein genes
            shows they are unlinked in the human genome
  JOURNAL   Genomics 13 (1), 201-207 (1992)
   PUBMED   1577483
REFERENCE   10 (residues 1 to 110)
  AUTHORS   Herzog,H., Hofferer,L., Schneider,R. and Schweiger,M.
  TITLE     cDNA encoding the human homologue of rat ribosomal protein L35a
  JOURNAL   Nucleic Acids Res 18 (15), 4600 (1990)
   PUBMED   2388839
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC010949.1, BM972808.1 and AW575227.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 13, 2001 this sequence version replaced NP_000987.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L35AE family of ribosomal proteins. It is located in the
            cytoplasm. The rat protein has been shown to bind to both initiator
            and elongator tRNAs, and thus, it is located at the P site, or P
            and A sites, of the ribosome. Although this gene was originally
            mapped to chromosome 18, it has been established that it is located
            at 3q29-qter. Alternative splicing results in multiple transcript
            variants. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.66844.1,
                                           SRR5189658.88288.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000647248.2/ ENSP00000495672.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..110
                     /product="large ribosomal subunit protein eL33"
                     /note="60S ribosomal protein L35a; cell growth-inhibiting
                     gene 33 protein"
                     /calculated_mol_wt=12407
     Region          5..103
                     /region_name="Ribosomal_L35Ae"
                     /note="Ribosomal protein L35Ae; pfam01247"
                     /db_xref="CDD:460132"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P18077.2)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:O55142; propagated from
                     UniProtKB/Swiss-Prot (P18077.2)"
     CDS             1..110
                     /gene="RPL35A"
                     /gene_synonym="DBA5; eL33; L35A"
                     /coded_by="NM_000996.4:65..397"
                     /db_xref="CCDS:CCDS33930.1"
                     /db_xref="GeneID:6165"
                     /db_xref="HGNC:HGNC:10345"
                     /db_xref="MIM:180468"
ORIGIN      
        1 msgrlwskai fagykrglrn qrehtallki egvyardete fylgkrcayv ykaknntvtp
       61 ggkpnktrvi wgkvtrahgn sgmvrakfrs nlpakaighr irvmlypsri
//
LOCUS       NP_001138830            1273 aa            linear   PRI 20-NOV-2025
DEFINITION  paired amphipathic helix protein Sin3a [Homo sapiens].
ACCESSION   NP_001138830
VERSION     NP_001138830.1
DBSOURCE    REFSEQ: accession NM_001145358.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1273)
  AUTHORS   Coenen-van der Spek,J., Relator,R., Kerkhof,J., McConkey,H.,
            Levy,M.A., Tedder,M.L., Louie,R.J., Fletcher,R.S., Moore,H.W.,
            Childers,A., Farrelly,E.R., Champaigne,N.L., Lyons,M.J.,
            Everman,D.B., Rogers,R.C., Skinner,S.A., Renck,A., Matalon,D.R.,
            Dills,S.K., Monteleone,B., Demirdas,S., Dingemans,A.J.M., Donker
            Kaat,L., Kolk,S.M., Pfundt,R., Rump,P., Sadikovic,B., Kleefstra,T.
            and Butler,K.M.
  TITLE     DNA methylation episignature for Witteveen-Kolk syndrome due to
            SIN3A haploinsufficiency
  JOURNAL   Genet Med 25 (1), 63-75 (2023)
   PUBMED   36399132
  REMARK    GeneRIF: DNA methylation episignature for Witteveen-Kolk syndrome
            due to SIN3A haploinsufficiency.
REFERENCE   3  (residues 1 to 1273)
  AUTHORS   Soukar,I., Amarasinghe,A. and Pile,L.A.
  TITLE     Coordination of cross-talk between metabolism and epigenetic
            regulation by the SIN3 complex
  JOURNAL   Enzymes 53, 33-68 (2023)
   PUBMED   37748836
  REMARK    GeneRIF: Coordination of cross-talk between metabolism and
            epigenetic regulation by the SIN3 complex.
            Review article
REFERENCE   4  (residues 1 to 1273)
  AUTHORS   Dahiya,N.R., Leibovitch,B.A., Kadamb,R., Bansal,N. and Waxman,S.
  TITLE     The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a Second
            Repressor of Retinoic Acid Receptor Beta Expression in Breast
            Cancer Cells
  JOURNAL   Cells 11 (7), 1179 (2022)
   PUBMED   35406744
  REMARK    GeneRIF: The Sin3A/MAD1 Complex, through Its PAH2 Domain, Acts as a
            Second Repressor of Retinoic Acid Receptor Beta Expression in
            Breast Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1273)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1273)
  AUTHORS   Laherty,C.D., Yang,W.M., Sun,J.M., Davie,J.R., Seto,E. and
            Eisenman,R.N.
  TITLE     Histone deacetylases associated with the mSin3 corepressor mediate
            mad transcriptional repression
  JOURNAL   Cell 89 (3), 349-356 (1997)
   PUBMED   9150134
  REMARK    GeneRIF: mSin3A interacts with HDAC2 via the HDAC-interacting
            domain (HID) of mSin3A.
            GeneRIF: The transcriptional repressor mSin3A associates with
            histone deacetylase 1 forming a co-repressor complex. See also PMID
            (PubMed identifier) 9150133.
REFERENCE   7  (residues 1 to 1273)
  AUTHORS   Hassig,C.A., Fleischer,T.C., Billin,A.N., Schreiber,S.L. and
            Ayer,D.E.
  TITLE     Histone deacetylase activity is required for full transcriptional
            repression by mSin3A
  JOURNAL   Cell 89 (3), 341-347 (1997)
   PUBMED   9150133
REFERENCE   8  (residues 1 to 1273)
  AUTHORS   Hurlin,P.J., Queva,C., Koskinen,P.J., Steingrimsson,E., Ayer,D.E.,
            Copeland,N.G., Jenkins,N.A. and Eisenman,R.N.
  TITLE     Mad3 and Mad4: novel Max-interacting transcriptional repressors
            that suppress c-myc dependent transformation and are expressed
            during neural and epidermal differentiation
  JOURNAL   EMBO J 14 (22), 5646-5659 (1995)
   PUBMED   8521822
  REMARK    Erratum:[EMBO J. 1996 Apr 15;15(8):2030. PMID: 8617250]
REFERENCE   9  (residues 1 to 1273)
  AUTHORS   Halleck,M.S., Pownall,S., Harder,K.W., Duncan,A.M., Jirik,F.R. and
            Schlegel,R.A.
  TITLE     A widely distributed putative mammalian transcriptional regulator
            containing multiple paired amphipathic helices, with similarity to
            yeast SIN3
  JOURNAL   Genomics 26 (2), 403-406 (1995)
   PUBMED   7601471
REFERENCE   10 (residues 1 to 1273)
  AUTHORS   Ayer,D.E., Lawrence,Q.A. and Eisenman,R.N.
  TITLE     Mad-Max transcriptional repression is mediated by ternary complex
            formation with mammalian homologs of yeast repressor Sin3
  JOURNAL   Cell 80 (5), 767-776 (1995)
   PUBMED   7889570
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096477.1, AF418569.1,
            AC068338.14 and BM676304.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a transcriptional
            regulatory protein. It contains paired amphipathic helix (PAH)
            domains, which are important for protein-protein interactions and
            may mediate repression by the Mad-Max complex. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.11566.1,
                                           SRR11853562.12031.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394947.8/ ENSP00000378402.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..1273
                     /product="paired amphipathic helix protein Sin3a"
                     /note="transcriptional co-repressor Sin3A; histone
                     deacetylase complex subunit Sin3a; transcriptional
                     corepressor Sin3a; transcriptional regulator, SIN3A; SIN3
                     homolog A, transcription regulator"
                     /calculated_mol_wt=145045
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          5..1213
                     /region_name="Sin3"
                     /note="Histone deacetylase complex, regulatory component
                     SIN3 [Chromatin structure and dynamics]; COG5602"
                     /db_xref="CDD:227889"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          87..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          119..196
                     /region_name="Interaction with HCFC1.
                     /evidence=ECO:0000269|PubMed:12670868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..480
                     /region_name="Interaction with REST.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          205..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          398..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          458..525
                     /region_name="Interaction with SAP30.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            469
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          523..850
                     /region_name="Interaction with NCOR1.
                     /evidence=ECO:0000250|UniProtKB:Q60520"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          524..659
                     /region_name="Interaction with SUDS3 and SAP130.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          687..829
                     /region_name="Interaction with HDAC1 and ARID4B.
                     /evidence=ECO:0000269|PubMed:12724404"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            860
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            865
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            875
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60520; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          888..967
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:12150998"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            940
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1089
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96ST3.2)"
     Region          1136..1156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ST3.2)"
     CDS             1..1273
                     /gene="SIN3A"
                     /gene_synonym="CHR15DELq24; DEL15Q24; WITKOS"
                     /coded_by="NM_001145358.2:302..4123"
                     /db_xref="CCDS:CCDS10279.1"
                     /db_xref="GeneID:25942"
                     /db_xref="HGNC:HGNC:19353"
                     /db_xref="MIM:607776"
ORIGIN      
        1 mkrrlddqes pvyaaqqrri pgsteafphq hrvlapappv yeavsetmqs atgiqysvtp
       61 syqvsampqs sgshgpaiaa vhsshhhpta vqphggqvvq shahpappva pvqgqqqfqr
      121 lkvedalsyl dqvklqfgsq pqvyndfldi mkefksqsid tpgvisrvsq lfkghpdlim
      181 gfntflppgy kievqtndmv nvttpgqvhq ipthgiqpqp qpppqhpsqp saqsapapaq
      241 papqpppakv skpsqlqaht pasqqtpplp pyasprsppv qphtpvtisl gtapslqnnq
      301 pvefnhainy vnkiknrfqg qpdiykafle ilhtyqkeqr nakeaggnyt palteqevya
      361 qvarlfknqe dllsefgqfl pdanssvlls kttaekvdsv rndhggtvkk pqlnnkpqrp
      421 sqngcqirrh ptgttppvkk kpkllnlkds smadaskhgg gteslffdkv rkalrsaeay
      481 enflrclvif nqevisrael vqlvspflgk fpelfnwfkn flgykesvhl etypkerate
      541 giameidyas ckrlgssyra lpksyqqpkc tgrtplckev lndtwvsfps wsedstfvss
      601 kktqyeehiy rcederfeld vvletnlati rvleaiqkkl srlsaeeqak frldntlggt
      661 sevihrkalq riyadkaadi idglrknpsi avpivlkrlk mkeeewreaq rgfnkvwreq
      721 nekyylksld hqginfkqnd tkvlrsksll neiesiyder qeqateenag vpvgphlsla
      781 yedkqileda aaliihhvkr qtgiqkedky kikqimhhfi pdllfaqrgd lsdveeeeee
      841 emdvdeatga vkkhngvggs ppkskllfsn taaqklrgmd evynlfyvnn nwyifmrlhq
      901 ilclrllric sqaerqieee nrerewerev lgikrdksds paiqlrlkep mdvdvedyyp
      961 afldmvrsll dgnidssqye dslremftih ayiaftmdkl iqsivrqlqh ivsdeicvqv
     1021 tdlylaennn gatggqlntq nsrsllesty qrkaeqlmsd encfklmfiq sqgqvqltie
     1081 lldteeensd dpveaerwsd yverymnsdt tspelrehla qkpvflprnl rrirkcqrgr
     1141 eqqekegkeg nskktmenvd sldklecrfk lnsykmvyvi ksedymyrrt allrahqshe
     1201 rvskrlhqrf qawvdkwtke hvpremaaet skwlmgegle glvpctttcd tetlhfvsin
     1261 kyrvkygtvf kap
//
LOCUS       NP_003030                501 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 5
            isoform 1 [Homo sapiens].
ACCESSION   NP_003030
VERSION     NP_003030.1
DBSOURCE    REFSEQ: accession NM_003039.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Song,A., Mao,Y. and Wei,H.
  TITLE     GLUT5: structure, functions, diseases and potential applications
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1519-1538 (2023)
   PUBMED   37674366
  REMARK    GeneRIF: GLUT5: structure, functions, diseases and potential
            applications.
            Review article
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Cui,Y., Liu,H., Wang,Z., Zhang,H., Tian,J., Wang,Z., Song,W.,
            Guo,H., Liu,L., Tian,R., Zuo,X., Ren,S., Zhang,F. and Niu,R.
  TITLE     Fructose promotes angiogenesis by improving vascular endothelial
            cell function and upregulating VEGF expression in cancer cells
  JOURNAL   J Exp Clin Cancer Res 42 (1), 184 (2023)
   PUBMED   37507736
  REMARK    GeneRIF: Fructose promotes angiogenesis by improving vascular
            endothelial cell function and upregulating VEGF expression in
            cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Fiorentino,T.V., De Vito,F., Suraci,E., Marasco,R., Hribal,M.L.,
            Luzza,F. and Sesti,G.
  TITLE     Obesity and overweight are linked to increased sodium-glucose
            cotransporter 1 and glucose transporter 5 levels in duodenum
  JOURNAL   Obesity (Silver Spring) 31 (3), 724-731 (2023)
   PUBMED   36746764
  REMARK    GeneRIF: Obesity and overweight are linked to increased
            sodium-glucose cotransporter 1 and glucose transporter 5 levels in
            duodenum.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Taneva,I., Grumann,D., Schmidt,D., Taneva,E., von Arnim,U.,
            Ansorge,T. and Wex,T.
  TITLE     Gene variants of the SLC2A5 gene encoding GLUT5, the major fructose
            transporter, do not contribute to clinical presentation of acquired
            fructose malabsorption
  JOURNAL   BMC Gastroenterol 22 (1), 167 (2022)
   PUBMED   35387598
  REMARK    GeneRIF: Gene variants of the SLC2A5 gene encoding GLUT5, the major
            fructose transporter, do not contribute to clinical presentation of
            acquired fructose malabsorption.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Mahraoui,L., Takeda,J., Mesonero,J., Chantret,I., Dussaulx,E.,
            Bell,G.I. and Brot-Laroche,E.
  TITLE     Regulation of expression of the human fructose transporter (GLUT5)
            by cyclic AMP
  JOURNAL   Biochem J 301 (Pt 1) (Pt 1), 169-175 (1994)
   PUBMED   8037665
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Rand,E.B., Depaoli,A.M., Davidson,N.O., Bell,G.I. and Burant,C.F.
  TITLE     Sequence, tissue distribution, and functional characterization of
            the rat fructose transporter GLUT5
  JOURNAL   Am J Physiol 264 (6 Pt 1), G1169-G1176 (1993)
   PUBMED   8333543
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Burant,C.F., Takeda,J., Brot-Laroche,E., Bell,G.I. and
            Davidson,N.O.
  TITLE     Fructose transporter in human spermatozoa and small intestine is
            GLUT5
  JOURNAL   J Biol Chem 267 (21), 14523-14526 (1992)
   PUBMED   1634504
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Davidson,N.O., Hausman,A.M., Ifkovits,C.A., Buse,J.B., Gould,G.W.,
            Burant,C.F. and Bell,G.I.
  TITLE     Human intestinal glucose transporter expression and localization of
            GLUT5
  JOURNAL   Am J Physiol 262 (3 Pt 1), C795-C800 (1992)
   PUBMED   1550217
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Kayano,T., Burant,C.F., Fukumoto,H., Gould,G.W., Fan,Y.S.,
            Eddy,R.L., Byers,M.G., Shows,T.B., Seino,S. and Bell,G.I.
  TITLE     Human facilitative glucose transporters. Isolation, functional
            characterization, and gene localization of cDNAs encoding an
            isoform (GLUT5) expressed in small intestine, kidney, muscle, and
            adipose tissue and an unusual glucose transporter pseudogene-like
            sequence (GLUT6)
  JOURNAL   J Biol Chem 265 (22), 13276-13282 (1990)
   PUBMED   1695905
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC379829.1, M55531.1,
            CA309754.1 and AL158048.35.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a fructose transporter
            responsible for fructose uptake by the small intestine. The encoded
            protein also is necessary for the increase in blood pressure due to
            high dietary fructose consumption. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 3
            both encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.179157.1,
                                           SRR1803617.129736.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377424.9/ ENSP00000366641.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..501
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 5 isoform 1"
                     /note="glucose transporter-like protein 5; glucose
                     transporter type 5, small intestine; solute carrier family
                     2 (facilitated glucose/fructose transporter), member 5;
                     testicular tissue protein Li 81"
                     /calculated_mol_wt=54843
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22732.1)"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Region          23..471
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(32,36,167,170..171,174,288..289,293..294,297..298,
                     325,387..388,391..392,396,419..420,423)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22732.1)"
     Site            69..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            127..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            162..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            343..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            372..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            440..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     CDS             1..501
                     /gene="SLC2A5"
                     /gene_synonym="GLUT-5; GLUT5"
                     /coded_by="NM_003039.3:100..1605"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS99.1"
                     /db_xref="GeneID:6518"
                     /db_xref="HGNC:HGNC:11010"
                     /db_xref="MIM:138230"
ORIGIN      
        1 meqqdqsmke grltlvlala tliaafgssf qygynvaavn spallmqqfy netyygrtge
       61 fmedfpltll wsvtvsmfpf ggfigsllvg plvnkfgrkg allfnnifsi vpailmgcsr
      121 vatsfeliii srllvgicag vssnvvpmyl gelapknlrg algvvpqlfi tvgilvaqif
      181 glrnllanvd gwpillgltg vpaalqllll pffpespryl liqkkdeaaa kkalqtlrgw
      241 dsvdrevaei rqedeaekaa gfisvlklfr mrslrwqlls iivlmggqql sgvnaiyyya
      301 dqiylsagvp eehvqyvtag tgavnvvmtf cavfvvellg rrlllllgfs icliaccvlt
      361 aalalqdtvs wmpyisivcv isyvighalg pspipallit eiflqssrps afmvggsvhw
      421 lsnftvglif pfiqeglgpy sfivfavicl lttiyifliv petkaktfie inqiftkmnk
      481 vsevypekee lkelppvtse q
//
LOCUS       NP_061990                718 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_061990
VERSION     NP_061990.2
DBSOURCE    REFSEQ: accession NM_019117.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Choi,S.H., Cho,S.Y., Song,J. and Hur,M.W.
  TITLE     KLHL4, a novel p53 target gene, inhibits cell proliferation by
            activating p21WAF/CDKN1A
  JOURNAL   Biochem Biophys Res Commun 530 (3), 588-596 (2020)
   PUBMED   32753315
  REMARK    GeneRIF: KLHL4, a novel p53 target gene, inhibits cell
            proliferation by activating p21(WAF/CDKN1A).
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Cheroki,C., Krepischi-Santos,A.C., Szuhai,K., Brenner,V., Kim,C.A.,
            Otto,P.A. and Rosenberg,C.
  TITLE     Genomic imbalances associated with mullerian aplasia
  JOURNAL   J Med Genet 45 (4), 228-232 (2008)
   PUBMED   18039948
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Braybrook,C., Warry,G., Howell,G., Mandryko,V., Arnason,A.,
            Bjornsson,A., Ross,M.T., Moore,G.E. and Stanier,P.
  TITLE     Physical and transcriptional mapping of the X-linked cleft palate
            and ankyloglossia (CPX) critical region
  JOURNAL   Hum Genet 108 (6), 537-545 (2001)
   PUBMED   11499681
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Braybrook,C., Warry,G., Howell,G., Arnason,A., Bjornsson,A.,
            Moore,G.E., Ross,M.T. and Stanier,P.
  TITLE     Identification and characterization of KLHL4, a novel human
            homologue of the Drosophila Kelch gene that maps within the
            X-linked cleft palate and Ankyloglossia (CPX) critical region
  JOURNAL   Genomics 72 (2), 128-136 (2001)
   PUBMED   11401425
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z95400.2, AF284765.1,
            BC161675.1 and AL121884.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 20, 2001 this sequence version replaced NP_061990.1.
            
            Summary: This gene encodes a member of the kelch family of
            proteins, which are characterized by kelch repeat motifs and a
            POZ/BTB protein-binding domain. It is thought that kelch repeats
            are actin binding domains. However, the specific function of this
            protein has not been determined. Alternative splicing of this gene
            results in two transcript variants encoding different isoforms.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) uses an alternate last exon as
            compared to variant 2, resulting in a frameshift and use of a
            different stop codon. The encoded isoform (1) is 2 aa shorter than
            isoform 2 and has a distinct C-terminus.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC161675.1, SRR1660807.33341.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373119.9/ ENSP00000362211.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.31"
     Protein         1..718
                     /product="kelch-like protein 4 isoform 1"
                     /note="kelch-like protein 4"
                     /calculated_mol_wt=80115
     Region          46..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          176..698
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          430..476
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          466..509
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          477..523
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          513..557
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          525..570
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          560..603
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          571..617
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          607..658
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          619..670
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     Region          660..699
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          671..717
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0H6.2)"
     CDS             1..718
                     /gene="KLHL4"
                     /gene_synonym="DKELCHL; KHL4"
                     /coded_by="NM_019117.5:93..2249"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14457.1"
                     /db_xref="GeneID:56062"
                     /db_xref="HGNC:HGNC:6355"
                     /db_xref="MIM:300348"
ORIGIN      
        1 msvsgkkefd vkqilrlrwr wfshpfqgst ntgsclqqeg yehrgtpvqg rlkshsrdrn
       61 glkksnspvh hnilapvpgp apahqravqn lqqhnlivhf qanedtpksv peknlfkeac
      121 ekraqdlemm addniedsta rldtqhsedm natrseeqfh vinhaeqtlr kmenylkekq
      181 lcdvlliagh lripahrlvl savsdyfaam ftndvleakq eevrmegvdp nalnslvqya
      241 ytgvlqlked tiesllaaac llqltqvidv csnflikqlh psnclgirsf gdaqgctell
      301 nvahkytmeh fieviknqef lllpaneisk llcsddinvp deetifhalm qwvghdvqnr
      361 qgelgmllsy irlpllppql ladletssmf tgdlecqkll meamkyhllp errsmmqspr
      421 tkprkstvga lyavggmdam kgtttiekyd lrtnswlhig tmngrrlqfg vavidnklyv
      481 vggrdglktl ntvecfnpvg kiwtvmppms thrhglgvat legpmyavgg hdgwsylntv
      541 erwdpegrqw nyvasmstpr stvgvvalnn klyaiggrdg ssclksmeyf dphtnkwslc
      601 apmskrrggv gvatyngfly vvgghdapas nhcsrlsdcv erydpkgdsw stvaplsvpr
      661 davavcplgd klyvvggydg htylntvesy daqrnewkee vpvnigraga cvvvvklp
//
LOCUS       NP_060173                326 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform a [Homo sapiens].
ACCESSION   NP_060173
VERSION     NP_060173.1
DBSOURCE    REFSEQ: accession NM_017703.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB127388.1 and AK000195.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.139176.1,
                                           SRR3476690.723967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151358, SAMEA2156099
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247977.9/ ENSP00000247977.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..326
                     /product="F-box/LRR-repeat protein 12 isoform a"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=36895
     Region          4..45
                     /region_name="F-box_FBXL12"
                     /note="F-box domain found in F-box/LRR-repeat protein 12
                     (FBXL12) and similar proteins; cd22123"
                     /db_xref="CDD:438895"
     Site            order(7,11,14..15,18..19,23,25..26,30..32,34)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438895"
     Region          51..78
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          86..111
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          104..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          113..133
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          121..>226
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          153..177
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          161..185
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          178..203
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          186..211
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          204..229
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          212..236
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          230..253
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          237..261
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          266..291
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXK8.1)"
     Region          284..319
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..326
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_017703.3:267..1247"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12218.1"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 matlvelpds vlleifsylp vrdririsrv chrwkrlvdd rwlwrhvdlt lytmrpkvmw
       61 hllrrymasr lhslrmggyl fsgsqapqls pallralgqk cpnlkrlclh vadlsmvpit
      121 slpstlrtle lhsceismaw lhkqqdptvl pllecivldr vpafrdehlq gltrfralrs
      181 lvlggtyrvt etgldaglqe lsylqrlevl gctlsadstl laisrhlrdv rkirltvrgl
      241 sapglavleg mpaleslclq gplvtpemps pteilssclt mpklrvlelq glgwegqeae
      301 kilckglphc mvivracpke smdwwm
//
LOCUS       NP_004595                297 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-4 isoform 3 [Homo sapiens].
ACCESSION   NP_004595
VERSION     NP_004595.2
DBSOURCE    REFSEQ: accession NM_004604.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Kioumourtzoglou,D., Black,H.L., Al Tobi,M., Livingstone,R.,
            Petrie,J.R., Boyle,J.G., Gould,G.W. and Bryant,N.J.
  TITLE     Phosphorylation of Syntaxin 4 by the Insulin Receptor Drives
            Exocytic SNARE Complex Formation to Deliver GLUT4 to the Cell
            Surface
  JOURNAL   Biomolecules 13 (12), 1738 (2023)
   PUBMED   38136609
  REMARK    GeneRIF: Phosphorylation of Syntaxin 4 by the Insulin Receptor
            Drives Exocytic SNARE Complex Formation to Deliver GLUT4 to the
            Cell Surface.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Gigon,L., Fettrelet,T., Miholic,M., McLeish,K.R., Yousefi,S.,
            Stojkov,D. and Simon,H.U.
  TITLE     Syntaxin-4 and SNAP23 are involved in neutrophil degranulation, but
            not in the release of mitochondrial DNA during NET formation
  JOURNAL   Front Immunol 14, 1272699 (2023)
   PUBMED   37885878
  REMARK    GeneRIF: Syntaxin-4 and SNAP23 are involved in neutrophil
            degranulation, but not in the release of mitochondrial DNA during
            NET formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Schrauwen,I., Ghaffar,A., Bharadwaj,T., Shah,K., Rehman,S.,
            Acharya,A., Liaqat,K., Lin,N.S., Everard,J.L., Khan,A., Ahmed,Z.M.,
            Ahmad,W., Riazuddin,S. and Leal,S.M.
  TITLE     Syntaxin 4 is essential for hearing in human and zebrafish
  JOURNAL   Hum Mol Genet 32 (7), 1184-1192 (2023)
   PUBMED   36355422
  REMARK    GeneRIF: Syntaxin 4 is essential for hearing in human and
            zebrafish.
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Mandon,B., Chou,C.L., Nielsen,S. and Knepper,M.A.
  TITLE     Syntaxin-4 is localized to the apical plasma membrane of rat renal
            collecting duct cells: possible role in aquaporin-2 trafficking
  JOURNAL   J Clin Invest 98 (4), 906-913 (1996)
   PUBMED   8770861
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Jagadish,M.N., Fernandez,C.S., Hewish,D.R., Macaulay,S.L.,
            Gough,K.H., Grusovin,J., Verkuylen,A., Cosgrove,L., Alafaci,A.,
            Frenkel,M.J. and Ward,C.W.
  TITLE     Insulin-responsive tissues contain the core complex protein SNAP-25
            (synaptosomal-associated protein 25) A and B isoforms in addition
            to syntaxin 4 and synaptobrevins 1 and 2
  JOURNAL   Biochem J 317 (Pt 3) (Pt 3), 945-954 (1996)
   PUBMED   8760387
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Li,C., Ullrich,B., Zhang,J.Z., Anderson,R.G., Brose,N. and
            Sudhof,T.C.
  TITLE     Ca(2+)-dependent and -independent activities of neural and
            non-neural synaptotagmins
  JOURNAL   Nature 375 (6532), 594-599 (1995)
   PUBMED   7791877
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Li,H., Hodge,D.R., Pei,G.K. and Seth,A.
  TITLE     Isolation and sequence analysis of the human syntaxin-encoding gene
  JOURNAL   Gene 143 (2), 303-304 (1994)
   PUBMED   8206394
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Bennett,M.K., Garcia-Arraras,J.E., Elferink,L.A., Peterson,K.,
            Fleming,A.M., Hazuka,C.D. and Scheller,R.H.
  TITLE     The syntaxin family of vesicular transport receptors
  JOURNAL   Cell 74 (5), 863-873 (1993)
   PUBMED   7690687
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI755734.1 and BC002436.2.
            
            On Apr 15, 2002 this sequence version replaced NP_004595.1.
            
            Transcript Variant: This variant (3) initiates translation at an
            alternate downstream start codon and uses alternate splice sites at
            internal exons, compared to variant 1. The encoded isoform (3) has
            a distinct N-terminus and is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.285293.1,
                                           SRR3476690.1061790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313843.8/ ENSP00000317714.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..297
                     /product="syntaxin-4 isoform 3"
                     /note="syntaxin 4A (placental); renal carcinoma antigen
                     NY-REN-31"
                     /calculated_mol_wt=34049
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12846.2)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q12846.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q12846.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     Region          39..189
                     /region_name="SynN"
                     /note="Syntaxin N-terminus domain; syntaxins are nervous
                     system-specific proteins implicated in the docking of
                     synaptic vesicles with the presynaptic plasma membrane;
                     they are a family of receptors for intracellular transport
                     vesicles; each target membrane may...; cd00179"
                     /db_xref="CDD:238105"
     Site            order(42,49,121..122,125..126,129,132..133,139,142,174)
                     /site_type="active"
                     /note="nSec1 interaction sites [active]"
                     /db_xref="CDD:238105"
     Site            order(69,80,83..84,91,95,98,105,127,132,135,141,148..149,
                     152..153,155..156,159,186)
                     /site_type="active"
                     /note="interdomain interaction site [active]"
                     /db_xref="CDD:238105"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     Region          154..297
                     /region_name="Interaction with CENPF.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12846.2)"
     Site            order(166..176,185..189)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238105"
     Region          199..261
                     /region_name="SNARE_syntaxin4"
                     /note="SNARE motif of syntaxin 4; cd15883"
                     /db_xref="CDD:277236"
     Site            order(204,206..207,209..214,216..218,220..221,223..225,
                     227..228,230..232,234..235,237..242,244..249,251..256,
                     258..260)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277236"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70452; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     Site            234
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277236"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70452; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     Site            276..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12846.2)"
     Site            290
                     /site_type="other"
                     /note="Required for neurite tip localization.
                     /evidence=ECO:0000250|UniProtKB:Q08850; propagated from
                     UniProtKB/Swiss-Prot (Q12846.2)"
     CDS             1..297
                     /gene="STX4"
                     /gene_synonym="DFNB123; p35-2; STX4A"
                     /coded_by="NM_004604.5:249..1142"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10700.1"
                     /db_xref="GeneID:6810"
                     /db_xref="HGNC:HGNC:11439"
                     /db_xref="MIM:186591"
ORIGIN      
        1 mrdrthelrq gddssdeedk ervalvvhpg tarlgspdee ffhkvrtirq tivklgnkvq
       61 elekqqvtil atplpeesmk qelqnlrdei kqlgreirlq lkaiepqkee adenynsvnt
      121 rmrktqhgvl sqqfvelink cnsmqseyre knverirrql kitnagmvsd eeleqmldsg
      181 qsevfvsnil kdtqvtrqal neisarhsei qqlersirel hdiftflate vemqgeminr
      241 ieknilssad yvergqehvk talenqkkar kkkvliaicv sitvvllavi igvtvvg
//
LOCUS       NP_006224                125 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB9 [Homo sapiens].
ACCESSION   NP_006224
VERSION     NP_006224.1
DBSOURCE    REFSEQ: accession NM_006233.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Higman,B., Shugar,D.H., Stark,C.P., Ekstrom,G., Koppes,M.N.,
            Lynett,P., Dufresne,A., Haeussler,P.J., Geertsema,M., Gulick,S.,
            Mattox,A., Venditti,J.G., Walton,M.A.L., McCall,N., Mckittrick,E.,
            MacInnes,B., Bilderback,E.L., Tang,H., Willis,M.J., Richmond,B.,
            Reece,R.S., Larsen,C., Olson,B., Capra,J., Ayca,A., Bloom,C.,
            Williams,H., Bonno,D., Weiss,R., Keen,A., Skanavis,V. and Loso,M.
  TITLE     The 2015 landslide and tsunami in Taan Fiord, Alaska
  JOURNAL   Sci Rep 8 (1), 12993 (2018)
   PUBMED   30190595
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Hu,X., Malik,S., Negroiu,C.C., Hubbard,K., Velalar,C.N.,
            Hampton,B., Grosu,D., Catalano,J., Roeder,R.G. and Gnatt,A.
  TITLE     A Mediator-responsive form of metazoan RNA polymerase II
  JOURNAL   Proc Natl Acad Sci U S A 103 (25), 9506-9511 (2006)
   PUBMED   16769904
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Wu-Baer,F., Sigman,D. and Gaynor,R.B.
  TITLE     Specific binding of RNA polymerase II to the human immunodeficiency
            virus trans-activating region RNA is regulated by cellular
            cofactors and Tat
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7153-7157 (1995)
   PUBMED   7638159
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC017112.1.
            
            Summary: This gene encodes a subunit of RNA polymerase II, the
            polymerase responsible for synthesizing messenger RNA in
            eukaryotes. This subunit, in combination with two other polymerase
            subunits, forms the DNA binding domain of the polymerase, a groove
            in which the DNA template is transcribed into RNA. The product of
            this gene has two zinc finger motifs with conserved cysteines and
            the subunit does possess zinc binding activity. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017112.1, SRR1163655.549868.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221859.9/ ENSP00000221859.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..125
                     /product="DNA-directed RNA polymerase II subunit RPB9"
                     /EC_number="2.7.7.6"
                     /note="polymerase (RNA) II subunit I; RPB14.5; RNA
                     polymerase II subunit B9; DNA-directed RNA polymerase II
                     subunit I; DNA-directed RNA polymerase II 14.5 kDa
                     polypeptide; RNA polymerase II 14.5 kDa subunit;
                     polymerase (RNA) II (DNA directed) polypeptide I, 14.5kDa"
                     /calculated_mol_wt=14392
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P36954.1)"
     Region          15..68
                     /region_name="RPOL9"
                     /note="RNA polymerase subunit 9; smart00661"
                     /db_xref="CDD:197822"
     Region          74..124
                     /region_name="Zn-ribbon_RPB9"
                     /note="C-terminal zinc ribbon domain of RPB9 subunit of
                     RNA polymerase II; cd10508"
                     /db_xref="CDD:259793"
     Site            order(74,76..77,79,97..98,100,108..110)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:259793"
     Site            order(86,89,114,119)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259793"
     CDS             1..125
                     /gene="POLR2I"
                     /gene_synonym="hRPB14.5; RPB9"
                     /coded_by="NM_006233.5:20..397"
                     /db_xref="CCDS:CCDS12487.1"
                     /db_xref="GeneID:5438"
                     /db_xref="HGNC:HGNC:9196"
                     /db_xref="MIM:180662"
ORIGIN      
        1 mepdgtyepg fvgirfcqec nnmlypkedk enrillyacr ncdyqqeadn sciyvnkith
       61 evdeltqiia dvsqdptlpr tedhpcqkcg hkeavffqsh saraedamrl yyvctaphcg
      121 hrwte
//
LOCUS       NP_055418                465 aa            linear   PRI 20-NOV-2025
DEFINITION  cerebellar degeneration-related protein 2-like [Homo sapiens].
ACCESSION   NP_055418
VERSION     NP_055418.2
DBSOURCE    REFSEQ: accession NM_014603.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Erikstad,K.I., Herdlevaer,I., Peter,E., Haugen,M., Totland,C. and
            Vedeler,C.
  TITLE     A cerebellar degeneration-related protein 2-like cell-based assay
            for anti-Yo detection in patients with paraneoplastic cerebellar
            degeneration
  JOURNAL   Eur J Neurol 30 (6), 1727-1733 (2023)
   PUBMED   36912432
  REMARK    GeneRIF: A cerebellar degeneration-related protein 2-like
            cell-based assay for anti-Yo detection in patients with
            paraneoplastic cerebellar degeneration.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Herdlevaer,I., Haugen,M., Mazengia,K., Totland,C. and Vedeler,C.
  TITLE     Paraneoplastic Cerebellar Degeneration: The Importance of Including
            CDR2L as a Diagnostic Marker
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 8 (2), e963 (2021)
   PUBMED   33531379
  REMARK    GeneRIF: Paraneoplastic Cerebellar Degeneration: The Importance of
            Including CDR2L as a Diagnostic Marker.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Small,M., Treilleux,I., Couillault,C., Pissaloux,D., Picard,G.,
            Paindavoine,S., Attignon,V., Wang,Q., Rogemond,V., Lay,S.,
            Ray-Coquard,I., Pfisterer,J., Joly,F., Du Bois,A., Psimaras,D.,
            Bendriss-Vermare,N., Caux,C., Dubois,B., Honnorat,J. and
            Desestret,V.
  TITLE     Genetic alterations and tumor immune attack in Yo paraneoplastic
            cerebellar degeneration
  JOURNAL   Acta Neuropathol 135 (4), 569-579 (2018)
   PUBMED   29299667
  REMARK    GeneRIF: Paraneoplastic cerebellar degenerations with anti-Yo
            antibodies (Yo-PCD) tumors differed from the 116 control tumors by
            more abundant T and B cells infiltration occasionally organized in
            tertiary lymphoid structures harboring CDR2L protein deposits. 65%
            of Yo-PCD tumors cohort presented at least one somatic mutation in
            CDR2 and CDR2L with a predominance of missense mutations.
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Raspotnig,M., Haugen,M., Thorsteinsdottir,M., Stefansson,I.,
            Salvesen,H.B., Storstein,A. and Vedeler,C.A.
  TITLE     Cerebellar degeneration-related proteins 2 and 2-like are present
            in ovarian cancer in patients with and without Yo antibodies
  JOURNAL   Cancer Immunol Immunother 66 (11), 1463-1471 (2017)
   PUBMED   28710511
  REMARK    GeneRIF: Both cerebellar degeneration related protein 2 (CDR2) and
            cerebellar degeneration-related antigen CDR2L (CDR2L) are more
            widely expressed than previously thought, both in normal and
            cancerous tissues.
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Eichler,T.W., Totland,C., Haugen,M., Qvale,T.H., Mazengia,K.,
            Storstein,A., Haukanes,B.I. and Vedeler,C.A.
  TITLE     CDR2L Antibodies: A New Player in Paraneoplastic Cerebellar
            Degeneration
  JOURNAL   PLoS One 8 (6), e66002 (2013)
   PUBMED   23823982
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC047534.1, AC087651.19, AW239343.1 and BC013105.2.
            
            On Aug 4, 2007 this sequence version replaced NP_055418.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047534.1, L02867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337231.5/ ENSP00000336587.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..465
                     /product="cerebellar degeneration-related protein 2-like"
                     /note="paraneoplastic antigen; paraneoplastic 62 kDa
                     antigen"
                     /calculated_mol_wt=52879
     Region          <61..>233
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          282..314
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X02.2)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q86X02.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86X02.2)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86X02.2)"
     Region          382..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86X02.2)"
     CDS             1..465
                     /gene="CDR2L"
                     /gene_synonym="HUMPPA"
                     /coded_by="NM_014603.3:413..1810"
                     /db_xref="CCDS:CCDS11710.2"
                     /db_xref="GeneID:30850"
                     /db_xref="HGNC:HGNC:29999"
ORIGIN      
        1 mrraagmedf saeeeeswyd qqdleqdlhl aaelgktlle rnkelegslq qmystneeqv
       61 qeieyltkql dtlrhvneqh akvyeqldlt ardleltnhr lvleskaaqq kihgltetie
      121 rlqaqveelq aqveqlrgle qlrvlrekre rrrtihtfpc lkelctsprc kdafrlhsss
      181 lelgprpleq enerlqtlvg alrsqvsqer qrkeraerey tavlqeysel erqlcemeac
      241 rlrvqeleae llelqqmkqa ktyllgpddh laeallaplt qapeaddpqp grgddlgaqd
      301 gvsspaaspg hvvrkscsdt alnaivakdp asrhagnltl hansvrkrgm silrevdeqy
      361 hallekyeel lskcrqhgag vrhagvqtsr pisrdsswrd lrggeegqge vkagekslsq
      421 hveavdkrle qsqpeykalf keifsriqkt kadinatkvk thssk
//
LOCUS       NP_001521                826 aa            linear   PRI 20-NOV-2025
DEFINITION  hypoxia-inducible factor 1-alpha isoform 1 [Homo sapiens].
ACCESSION   NP_001521
VERSION     NP_001521.1
DBSOURCE    REFSEQ: accession NM_001530.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 826)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 826)
  AUTHORS   Nie,L., Huang,L., Zhu,Q., Yao,Q., Wu,Y., Zhao,L., Yu,L. and Fu,F.
  TITLE     HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in the
            Progression of Ovarian Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 44 (1), 47-55 (2025)
   PUBMED   39462449
  REMARK    GeneRIF: HIF-1alpha Activates Hypoxia-Induced MXRA5 Expression in
            the Progression of Ovarian Cancer.
REFERENCE   3  (residues 1 to 826)
  AUTHORS   VON Fournier,A., Wilhelm,C., Tirtey,C., Stoth,M., Kasemo,T.E.,
            Hackenberg,S. and Scherzad,A.
  TITLE     Impact of Hypoxia and the Levels of Transcription Factor HIF-1alpha
            and JMJD1A on Epithelial-Mesenchymal Transition in Head and Neck
            Squamous Cell Carcinoma Cell Lines
  JOURNAL   Cancer Genomics Proteomics 21 (6), 591-607 (2024)
   PUBMED   39467631
  REMARK    GeneRIF: Impact of Hypoxia and the Levels of Transcription Factor
            HIF-1alpha and JMJD1A on Epithelial-Mesenchymal Transition in Head
            and Neck Squamous Cell Carcinoma Cell Lines.
REFERENCE   4  (residues 1 to 826)
  AUTHORS   Kling,L., Eulenberg-Gustavus,C., Jerke,U., Rousselle,A.,
            Eckardt,K.U., Schreiber,A. and Kettritz,R.
  TITLE     beta2-integrins control HIF1alpha activation in human neutrophils
  JOURNAL   Front Immunol 15, 1406967 (2024)
   PUBMED   39469705
  REMARK    GeneRIF: beta2-integrins control HIF1alpha activation in human
            neutrophils.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 826)
  AUTHORS   Zarychta,J., Kowalczyk,A., Slowik,K., Przywara,D., Petniak,A.,
            Kondracka,A., Wojtowicz-Marzec,M., Slyk-Gulewska,P.,
            Kwasniewska,A., Kocki,J. and Gil-Kulik,P.
  TITLE     Pilot Study on the Effect of Patient Condition and Clinical
            Parameters on Hypoxia-Induced Factor Expression: HIF1A, EPAS1 and
            HIF3A in Human Colostrum Cells
  JOURNAL   Int J Mol Sci 25 (20), 11042 (2024)
   PUBMED   39456823
  REMARK    GeneRIF: Pilot Study on the Effect of Patient Condition and
            Clinical Parameters on Hypoxia-Induced Factor Expression: HIF1A,
            EPAS1 and HIF3A in Human Colostrum Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 826)
  AUTHORS   Wang,G.L., Jiang,B.H., Rue,E.A. and Semenza,G.L.
  TITLE     Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS
            heterodimer regulated by cellular O2 tension
  JOURNAL   Proc Natl Acad Sci U S A 92 (12), 5510-5514 (1995)
   PUBMED   7539918
REFERENCE   7  (residues 1 to 826)
  AUTHORS   Wang,G.L. and Semenza,G.L.
  TITLE     Purification and characterization of hypoxia-inducible factor 1
  JOURNAL   J Biol Chem 270 (3), 1230-1237 (1995)
   PUBMED   7836384
REFERENCE   8  (residues 1 to 826)
  AUTHORS   Semenza,G.L., Roth,P.H., Fang,H.M. and Wang,G.L.
  TITLE     Transcriptional regulation of genes encoding glycolytic enzymes by
            hypoxia-inducible factor 1
  JOURNAL   J Biol Chem 269 (38), 23757-23763 (1994)
   PUBMED   8089148
REFERENCE   9  (residues 1 to 826)
  AUTHORS   Wang,G.L. and Semenza,G.L.
  TITLE     General involvement of hypoxia-inducible factor 1 in
            transcriptional response to hypoxia
  JOURNAL   Proc Natl Acad Sci U S A 90 (9), 4304-4308 (1993)
   PUBMED   8387214
REFERENCE   10 (residues 1 to 826)
  AUTHORS   Semenza,G.L. and Wang,G.L.
  TITLE     A nuclear factor induced by hypoxia via de novo protein synthesis
            binds to the human erythropoietin gene enhancer at a site required
            for transcriptional activation
  JOURNAL   Mol Cell Biol 12 (12), 5447-5454 (1992)
   PUBMED   1448077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC344032.1, BC012527.2 and
            CN264295.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the alpha subunit of transcription
            factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer
            composed of an alpha and a beta subunit. HIF-1 functions as a
            master regulator of cellular and systemic homeostatic response to
            hypoxia by activating transcription of many genes, including those
            involved in energy metabolism, angiogenesis, apoptosis, and other
            genes whose protein products increase oxygen delivery or facilitate
            metabolic adaptation to hypoxia. HIF-1 thus plays an essential role
            in embryonic vascularization, tumor angiogenesis and
            pathophysiology of ischemic disease. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.144807.1,
                                           SRR1660805.134018.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337138.9/ ENSP00000338018.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..826
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..826
                     /product="hypoxia-inducible factor 1-alpha isoform 1"
                     /note="ARNT interacting protein; hypoxia inducible factor
                     1, alpha subunit (basic helix-loop-helix transcription
                     factor); member of PAS superfamily 1; hypoxia-inducible
                     factor 1-alpha; member of PAS protein 1; PAS
                     domain-containing protein 8; hypoxia inducible factor 1
                     alpha subunit; basic-helix-loop-helix-PAS protein MOP1;
                     class E basic helix-loop-helix protein 78;
                     hypoxia-inducible factor1alpha"
                     /calculated_mol_wt=92540
     Region          1..401
                     /region_name="Interaction with TSGA10.
                     /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          13..83
                     /region_name="bHLH-PAS_HIF1a_PASD8"
                     /note="basic helix-loop-helix-Per-ARNT-Sim (bHLH-PAS)
                     domain found in hypoxia-inducible factor 1-alpha (HIF1a)
                     and similar proteins; cd19727"
                     /db_xref="CDD:381570"
     Site            order(18..19,21..23,26..27,29..30,55..56)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381570"
     Site            18
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30125331;
                     propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          21..30
                     /region_name="DNA-binding.
                     /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            order(32..33,35..36,39..40,43..44,55..57,60..61,64,67..68,
                     71)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381570"
     Region          93..148
                     /region_name="PAS"
                     /note="PAS domain; smart00091"
                     /db_xref="CDD:214512"
     Region          170..191
                     /region_name="Required for heterodimer formation with
                     ARNT. /evidence=ECO:0000250|UniProtKB:Q61221"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:20699359; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          254..339
                     /region_name="PAS_3"
                     /note="PAS fold; pfam08447"
                     /db_xref="CDD:430001"
     Site            order(255,259,265,278..281,307,312)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238075"
     Site            order(275,279,287,290..291,319,321)
                     /site_type="other"
                     /note="heme pocket [chemical binding]"
                     /db_xref="CDD:238075"
     Region          380..417
                     /region_name="N-terminal VHL recognition site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          401..603
                     /region_name="ODD. /evidence=ECO:0000303|PubMed:16288748"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            402
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:11566883; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          494..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          531..575
                     /region_name="NTAD. /evidence=ECO:0000303|PubMed:10202154,
                     ECO:0000303|PubMed:9235919"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            532
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24681946; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          551..581
                     /region_name="HIF-1"
                     /note="Hypoxia-inducible factor-1; pfam11413"
                     /db_xref="CDD:463274"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          556..572
                     /region_name="C-terminal VHL recognition site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            564
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000269|PubMed:11292861,
                     ECO:0000269|PubMed:11566883, ECO:0000269|PubMed:12351678,
                     ECO:0000269|PubMed:25974097; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          576..785
                     /region_name="ID"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            589
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          642..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:20889502; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Site            709
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24681946; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     Region          718..721
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          786..826
                     /region_name="CTAD. /evidence=ECO:0000303|PubMed:10202154,
                     ECO:0000303|PubMed:9235919"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16665.1)"
     Region          789..825
                     /region_name="HIF-1a_CTAD"
                     /note="HIF-1 alpha C terminal transactivation domain;
                     pfam08778"
                     /db_xref="CDD:430212"
     Site            803
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine.
                     /evidence=ECO:0000269|PubMed:12080085; propagated from
                     UniProtKB/Swiss-Prot (Q16665.1)"
     CDS             1..826
                     /gene="HIF1A"
                     /gene_synonym="bHLHe78; HIF-1-alpha; HIF-1A; HIF-1alpha;
                     HIF1; HIF1-ALPHA; MOP1; PASD8"
                     /coded_by="NM_001530.4:293..2773"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9753.1"
                     /db_xref="GeneID:3091"
                     /db_xref="HGNC:HGNC:4910"
                     /db_xref="MIM:603348"
ORIGIN      
        1 megaggandk kkisserrke ksrdaarsrr skesevfyel ahqlplphnv sshldkasvm
       61 rltisylrvr klldagdldi eddmkaqmnc fylkaldgfv mvltddgdmi yisdnvnkym
      121 gltqfeltgh svfdfthpcd heemremlth rnglvkkgke qntqrsfflr mkctltsrgr
      181 tmniksatwk vlhctghihv ydtnsnqpqc gykkppmtcl vlicepiphp snieipldsk
      241 tflsrhsldm kfsycderit elmgyepeel lgrsiyeyyh aldsdhltkt hhdmftkgqv
      301 ttgqyrmlak rggyvwvetq atviyntkns qpqcivcvny vvsgiiqhdl ifslqqtecv
      361 lkpvessdmk mtqlftkves edtsslfdkl kkepdaltll apaagdtiis ldfgsndtet
      421 ddqqleevpl yndvmlpspn eklqninlam splptaetpk plrssadpal nqevalklep
      481 npeslelsft mpqiqdqtps psdgstrqss pepnspseyc fyvdsdmvne fklelveklf
      541 aedteaknpf stqdtdldle mlapyipmdd dfqlrsfdql splesssasp esaspqstvt
      601 vfqqtqiqep tanattttat tdelktvtkd rmedikilia spspthihke ttsatsspyr
      661 dtqsrtaspn ragkgvieqt ekshprspnv lsvalsqrtt vpeeelnpki lalqnaqrkr
      721 kmehdgslfq avgigtllqq pddhaattsl swkrvkgcks seqngmeqkt iilipsdlac
      781 rllgqsmdes glpqltsydc evnapiqgsr nllqgeellr aldqvn
//
LOCUS       NP_659433                321 aa            linear   PRI 20-NOV-2025
DEFINITION  ADP-ribosylation factor-like protein 13B isoform 2 [Homo sapiens].
ACCESSION   NP_659433
VERSION     NP_659433.2
DBSOURCE    REFSEQ: accession NM_144996.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Lin,Z., Shen,Y., Li,Y., Lu,C., Zhu,Y., He,R., Cao,Z., Yin,Z.,
            Gao,H., Guo,B., Ma,X., Cao,M. and Luo,M.
  TITLE     Novel compound heterozygous variants in ARL13B lead to Joubert
            syndrome
  JOURNAL   J Cell Physiol 239 (4), e31189 (2024)
   PUBMED   38219074
  REMARK    GeneRIF: Novel compound heterozygous variants in ARL13B lead to
            Joubert syndrome.
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Shi,P., Tian,J., Mallinger,J.C., Ling,D., Deleyrolle,L.P.,
            McIntyre,J.C., Caspary,T., Breunig,J.J. and Sarkisian,M.R.
  TITLE     Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia
  JOURNAL   Cells 12 (19), 2354 (2023)
   PUBMED   37830570
  REMARK    GeneRIF: Increasing Ciliary ARL13B Expression Drives Active and
            Inhibitor-Resistant Smoothened and GLI into Glioma Primary Cilia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Mahajan,D., Madugula,V. and Lu,L.
  TITLE     Rab8 and TNPO1 are ciliary transport adaptors for GTPase Arl13b by
            interacting with its RVEP motif containing ciliary targeting
            sequence
  JOURNAL   J Biol Chem 299 (5), 104604 (2023)
   PUBMED   36907439
  REMARK    GeneRIF: Rab8 and TNPO1 are ciliary transport adaptors for GTPase
            Arl13b by interacting with its RVEP motif containing ciliary
            targeting sequence.
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Hori,Y., Kobayashi,T., Kikko,Y., Kontani,K. and Katada,T.
  TITLE     Domain architecture of the atypical Arf-family GTPase Arl13b
            involved in cilia formation
  JOURNAL   Biochem Biophys Res Commun 373 (1), 119-124 (2008)
   PUBMED   18554500
  REMARK    GeneRIF: These findings suggest that N and C domains of Arl13b
            cooperatively regulate its ciliary localization and that N
            domain-dependent self-association of Arl13b may be important for
            its function in cilia biogenesis.
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Cantagrel,V., Silhavy,J.L., Bielas,S.L., Swistun,D., Marsh,S.E.,
            Bertrand,J.Y., Audollent,S., Attie-Bitach,T., Holden,K.R.,
            Dobyns,W.B., Traver,D., Al-Gazali,L., Ali,B.R., Lindner,T.H.,
            Caspary,T., Otto,E.A., Hildebrandt,F., Glass,I.A., Logan,C.V.,
            Johnson,C.A., Bennett,C., Brancati,F., Valente,E.M., Woods,C.G. and
            Gleeson,J.G.
  CONSRTM   International Joubert Syndrome Related Disorders Study Group
  TITLE     Mutations in the cilia gene ARL13B lead to the classical form of
            Joubert syndrome
  JOURNAL   Am J Hum Genet 83 (2), 170-179 (2008)
   PUBMED   18674751
  REMARK    GeneRIF: ARL13B has an evolutionarily conserved role mediating
            cilia function in multiple organs
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Fan,Y., Esmail,M.A., Ansley,S.J., Blacque,O.E., Boroevich,K.,
            Ross,A.J., Moore,S.J., Badano,J.L., May-Simera,H., Compton,D.S.,
            Green,J.S., Lewis,R.A., van Haelst,M.M., Parfrey,P.S.,
            Baillie,D.L., Beales,P.L., Katsanis,N., Davidson,W.S. and
            Leroux,M.R.
  TITLE     Mutations in a member of the Ras superfamily of small GTP-binding
            proteins causes Bardet-Biedl syndrome
  JOURNAL   Nat Genet 36 (9), 989-993 (2004)
   PUBMED   15314642
REFERENCE   9  (residues 1 to 321)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094725.1 and AA775026.1.
            
            On Aug 12, 2003 this sequence version replaced NP_659433.1.
            
            Summary: This gene encodes a member of the ADP-ribosylation
            factor-like family. The encoded protein is a small GTPase that
            contains both N-terminal and C-terminal guanine nucleotide-binding
            motifs. This protein is localized in the cilia and plays a role in
            cilia formation and in maintenance of cilia. Mutations in this gene
            are the cause of Joubert syndrome 8. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            lacks two in-frame exons in the coding region, compared to variant
            1. The encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094725.1, CR936753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q11.1-q11.2"
     Protein         1..321
                     /product="ADP-ribosylation factor-like protein 13B isoform
                     2"
                     /note="ADP-ribosylation factor-like 2-like 1; ARL2-like
                     protein 1; ADP ribosylation factor like GTPase 13B"
                     /calculated_mol_wt=36664
     Region          <21..82
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            23..26
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133361"
     Site            59..61
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133361"
     Region          <92..134
                     /region_name="CCDC47"
                     /note="PAT complex subunit CCDC47; cl46382"
                     /db_xref="CDD:480722"
     CDS             1..321
                     /gene="ARL13B"
                     /gene_synonym="ARL2L1; JBTS8"
                     /coded_by="NM_144996.4:270..1235"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2924.1"
                     /db_xref="GeneID:200894"
                     /db_xref="HGNC:HGNC:25419"
                     /db_xref="MIM:608922"
ORIGIN      
        1 mfslmasccg wfkrwrepvr lankqdkega lgeadviecl sleklvnehk clcqiepcsa
       61 isgygkkidk sikkglywll hviardfdal neriqkette qraleeqekq eraervrklr
      121 eerkqneqeq aeldgtsgla eldpeptnpf qpiasviien egklerekkn qkmekdsdgc
      181 hlkhkmeheq ietqgqvnhn gqknnefglv enykealtqq lknedetdrp slesangkkk
      241 tkklrmkrnh rveplniddc apesptpppp pppvgwgtpk vtrlpklepl gethhndfyr
      301 kplpplavpq rpnsdahdvi s
//
LOCUS       NP_001311312             444 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001311312 XP_006716459
VERSION     NP_001311312.1
DBSOURCE    REFSEQ: accession NM_001324383.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 444)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK290683.1, AK295320.1, BC069242.1, AC108449.5 and BQ019252.1.
            
            On May 2, 2016 this sequence version replaced XP_006716459.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.153624.1,
                                           SRR1660805.219811.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..444
                     /product="homeobox-containing protein 1 isoform 2"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=49865
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     CDS             1..444
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324383.2:342..1676"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr anieaailes hgidvqspgg
      361 hsnsddvdgn dyseqdtwqv rngeeeegrs seggreaekd dstshsdhqd pislavemaa
      421 vnhtilalar qganeiktea lddd
//
LOCUS       NP_001288075             263 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 isoform e [Homo sapiens].
ACCESSION   NP_001288075
VERSION     NP_001288075.1
DBSOURCE    REFSEQ: accession NM_001301146.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Sun,L., Chen,Y., Xia,L., Wang,J., Zhu,J., Li,J., Wang,K., Shen,K.,
            Zhang,D., Zhang,G., Shi,T. and Chen,W.
  TITLE     TRIM69 suppressed the anoikis resistance and metastasis of gastric
            cancer through ubiquitin-proteasome-mediated degradation of PRKCD
  JOURNAL   Oncogene 42 (49), 3619-3632 (2023)
   PUBMED   37864033
  REMARK    GeneRIF: TRIM69 suppressed the anoikis resistance and metastasis of
            gastric cancer through ubiquitin-proteasome-mediated degradation of
            PRKCD.
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Wang,Y., Risteski,P., Yang,Y., Chen,H., Droby,G., Walens,A.,
            Jayaprakash,D., Troester,M., Herring,L., Chernoff,J., Tolic,I.M.,
            Bowser,J. and Vaziri,C.
  TITLE     The TRIM69-MST2 signaling axis regulates centrosome dynamics and
            chromosome segregation
  JOURNAL   Nucleic Acids Res 51 (19), 10568-10589 (2023)
   PUBMED   37739411
  REMARK    GeneRIF: The TRIM69-MST2 signaling axis regulates centrosome
            dynamics and chromosome segregation.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Yuan,J., Lv,T., Yang,J., Wu,Z., Yan,L., Yang,J. and Shi,Y.
  TITLE     HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability by
            diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma
  JOURNAL   Redox Biol 58, 102546 (2022)
   PUBMED   36423520
  REMARK    GeneRIF: HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability
            by diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Song,Y., Nguyen,X.N., Kumar,A., da Silva,C., Picard,L., Etienne,L.
            and Cimarelli,A.
  TITLE     Trim69 is a microtubule regulator that acts as a pantropic viral
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 119 (43), e2211467119 (2022)
   PUBMED   36251989
  REMARK    GeneRIF: Trim69 is a microtubule regulator that acts as a pantropic
            viral inhibitor.
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
  REMARK    GeneRIF: hTRIM69 is a novel E3 ubiquitin ligase identified from
            human testis and may function to ubiquitinate its particular
            substrates during spermatogenesis.
REFERENCE   7  (residues 1 to 263)
  AUTHORS   Bahmanyar,S., Kaplan,D.D., Deluca,J.G., Giddings,T.H. Jr.,
            O'Toole,E.T., Winey,M., Salmon,E.D., Casey,P.J., Nelson,W.J. and
            Barth,A.I.
  TITLE     beta-Catenin is a Nek2 substrate involved in centrosome separation
  JOURNAL   Genes Dev 22 (1), 91-105 (2008)
   PUBMED   18086858
REFERENCE   8  (residues 1 to 263)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     Forced expression of RNF36 induces cell apoptosis
  JOURNAL   Exp Cell Res 287 (2), 301-313 (2003)
   PUBMED   12837286
REFERENCE   9  (residues 1 to 263)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     A novel member of the RBCC family, Trif, expressed specifically in
            the spermatids of mouse testis
  JOURNAL   Mech Dev 108 (1-2), 213-216 (2001)
   PUBMED   11578878
  REMARK    GeneRIF: Gene and protein analysis of the mouse counterpart.
REFERENCE   10 (residues 1 to 263)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI827618.1, BI465168.1,
            AC122108.2, AF302088.1 and DB524904.1.
            
            Summary: This gene encodes a member of the RING-B-box-coiled-coil
            (RBCC) family and encodes a protein with an N-terminal RING finger
            motif, a PRY domain and a C-terminal SPRY domain. The mouse
            ortholog of this gene is specifically expressed in germ cells at
            the round spermatid stages during spermatogenesis and, when
            overexpressed, induces apoptosis. Alternatively spliced transcript
            variants encoding distinct isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (e) lacks an alternate in-frame
            exon in both the 5' and central coding regions, compared to variant
            a, resulting in an isoform (e) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI465168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..263
                     /product="E3 ubiquitin-protein ligase TRIM69 isoform e"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 36; RFP-like domain-containing
                     protein trimless; E3 ubiquitin-protein ligase TRIM69;
                     RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=29903
     Region          74..260
                     /region_name="SPRY_PRY_TRIM69"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     69 (TRIM69), also known as RING finger protein 36 (RNF36);
                     cd15818"
                     /db_xref="CDD:293990"
     CDS             1..263
                     /gene="TRIM69"
                     /gene_synonym="HSD-34; HSD34; RNF36; Trif"
                     /coded_by="NM_001301146.2:178..969"
                     /note="isoform e is encoded by transcript variant e"
                     /db_xref="CCDS:CCDS76745.1"
                     /db_xref="GeneID:140691"
                     /db_xref="HGNC:HGNC:17857"
                     /db_xref="MIM:616017"
ORIGIN      
        1 meeelaiqqg qlettlkelq tlrnmqkeai aahkdittll hsleqgmkvl atrelisrkl
       61 nlgqykgpiq ymvwremqdt lcpglspltl dpktahpnlv lsksqtsvwh gdikkimpdd
      121 perfdssvav lgsrgftsgk wywevevakk tkwtvgvvre siirkgscpl tpeqgfwllr
      181 lrnqtdlkal dlpsfsltlt nnldkvgiyl dyeggqlsfy naktmthiyt fsntfmekly
      241 pyfcpclndg genkeplhil hpq
//
LOCUS       NP_001290378             877 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001290378
VERSION     NP_001290378.1
DBSOURCE    REFSEQ: accession NM_001303449.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 877)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 877)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 877)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 877)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 877)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 877)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 877)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 877)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 877)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 877)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK307419.1, DC353932.1, AK302498.1, AF419855.1, AW958761.1,
            AA744578.1, CX782666.1 and BG178896.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..877
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..877
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 3"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=99133
     Region          7..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <579..>713
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..877
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001303449.1:271..2904"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mskvnlevik pwitkrvtei lgfeddvvie fifnqlevkn pdskmmqinl tgflngknar
       61 efmgelwpll lsaqeniagi psaflelkke eikqrqieqe klasmkkqde dkdkrdkeek
      121 essrekrers rsprrrksrs psprrrsspv rrerkrshsr sprhrtksrs pspapekkek
      181 tpelpepsvk vkepsvqeat stsdilkvpk pepipepkep speknskkek ekektrprsr
      241 srsksrsrtr srspshtrpr rrhrsrsrsy sprrrpsprr rpsprrrtpp rrmpppprhr
      301 rsrspvrrrr rssaslsgss ssssssrsrs ppkkppkrts spprktrrls psaspprrrh
      361 rpsppatppp ktrhsptpqq snrtrksrvs vspgrtsvtk hkgtekresp spapkprkve
      421 lseseedkgg kmaaadsvqq rrqyrrqnqq sssdsgssss sederpkrsh vkngevgrrr
      481 rhspsrsasp sprkrqkets prmqmgkrwq spvtksgrrr rspsppptrr rrspspappp
      541 rrrrtptppp rrrtpspppr rrspsprrys ppiqrrysps pppkrrtasp ppppkrrasp
      601 spppkrrvsh spppkqrssp vtkrrspsls skhrkgssps rstrearspq pnkrhspspr
      661 prapqtsssp ppvrrgasss pqrrqspsps trpirrvsrt pepkkikkaa spspqsvrrv
      721 sssrsvsgsp epaakkppap pspvqsqsps tnwspavpvk kaksptpsps pprnsdqegg
      781 gkkkkkkkdk khkkdkkhkk hkkhkkekav aaaaaaavtp aaiaaatttl aqeepvaape
      841 pkketeseae dnlddlekhl rekalrsmrk aqvspqs
//
LOCUS       NP_001310866             928 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001310866
VERSION     NP_001310866.1
DBSOURCE    REFSEQ: accession NM_001323937.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 928)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 928)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 928)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 928)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 928)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 928)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 928)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 928)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 928)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 928)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.279618.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..928
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..928
                     /product="DIS3-like exonuclease 1 isoform 5"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=105673
     Region          <11..62
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          112..740
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          755..830
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..928
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323937.2:170..2956"
                     /note="isoform 5 is encoded by transcript variant 4"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mqtacqavqh qrgrrsiyna avwyyhhcqd rmpivmvted eeaiqqygse tegvfvitfk
       61 nyldnfwpdl kaahelcdsi lqsrrerene sqeshgkeyp ehlplevlea giksgryiqg
      121 ilnvnkhraq ieafvrlqga sskdsdlvsd ilihgmkarn rsihgdvvvv ellpknewkg
      181 rtvalcendc ddkasgesps epmptgrvvg ilqknwrdyv vtfpskeevq sqgknaqkil
      241 vtpwdyripk iristqqaet lqdfrvvvri dswestsvyp nghfvrvlgr igdlegeiat
      301 ilvensisvi pfseaqmcem pvntpespwk vspeeeqkrk dlrkshlvfs idpkgcedvd
      361 dtlsvrtlnn gnlelgvhia dvthfvapns yidieartra ttyyladrry dmlpsvlsad
      421 lcsllggvdr yavsimweld kasyeikkvw ygrtiirsay klfyeaaqel ldgnlsvvdd
      481 ipefkdldek srqakleelv waigkltdia rhvrakrdgc galelegvev cvqlddkkni
      541 hdlipkqple vhetvaecmi lanhwvakki wesfphqall rqhppphqef fselrecaka
      601 kgffidtrsn ktladsldna ndphdpivnr llrsmatqam snalyfstgs caeeefhhyg
      661 laldkythft spirrysdiv vhrllmaais kdkkmeikgn lfsnkdleel crhinnrnqa
      721 aqhsqkqste lfqcmyfkdk dpateercis dgviysirtn gvllfiprfg ikgaaylknk
      781 dglviscgpd scsewkpgsl qrfqnkitst ttdgesvtfh lfdhvtvris iqasrchsdt
      841 irleiisnkp ykipntelih qsspllksel vkevtksvee aqlaqevkvn iiqeeyqeyr
      901 qtkgrslytl leeirdlall dvsnnygi
//
LOCUS       NP_008912                626 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor subfamily 4 group A member 3 isoform a [Homo
            sapiens].
ACCESSION   NP_008912
VERSION     NP_008912.2
DBSOURCE    REFSEQ: accession NM_006981.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Wu,Y., Jing,H., Li,Y., Li,M., Zheng,Y., Lin,Y., Ma,G., Cao,H. and
            Yang,H.
  TITLE     NOR1 promotes the osteoblastic differentiation of human periodontal
            ligament stem cells via TGF-beta signaling pathway
  JOURNAL   Cell Mol Life Sci 81 (1), 338 (2024)
   PUBMED   39120703
  REMARK    GeneRIF: NOR1 promotes the osteoblastic differentiation of human
            periodontal ligament stem cells via TGF-beta signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 626)
  AUTHORS   He,S., Jiang,W., Jiang,B., Yu,C., Zhao,G., Li,Y., Qi,L., Zhang,J.
            and Wang,D.
  TITLE     Potential Roles of Nr4a3-Mediated Inflammation in Immunological and
            Neurological Diseases
  JOURNAL   Mol Neurobiol 61 (8), 5958-5973 (2024)
   PUBMED   38261254
  REMARK    GeneRIF: Potential Roles of Nr4a3-Mediated Inflammation in
            Immunological and Neurological Diseases.
            Review article
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Ma,W., Jia,K., Cheng,H., Xu,H., Li,Z., Zhang,H., Xie,H., Sun,H.,
            Yi,L., Chen,Z., Duan,S., Sano,M., Fukuda,K., Lu,L., Gao,F.,
            Zhang,R. and Yan,X.
  TITLE     Orphan Nuclear Receptor NR4A3 Promotes Vascular Calcification via
            Histone Lactylation
  JOURNAL   Circ Res 134 (11), 1427-1447 (2024)
   PUBMED   38629274
  REMARK    GeneRIF: Orphan Nuclear Receptor NR4A3 Promotes Vascular
            Calcification via Histone Lactylation.
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Phelan,D.E., Reddan,B., Shigemura,M., Sznajder,J.I., Crean,D. and
            Cummins,E.P.
  TITLE     Orphan Nuclear Receptor Family 4A (NR4A) Members NR4A2 and NR4A3
            Selectively Modulate Elements of the Monocyte Response to Buffered
            Hypercapnia
  JOURNAL   Int J Mol Sci 25 (5), 2852 (2024)
   PUBMED   38474099
  REMARK    GeneRIF: Orphan Nuclear Receptor Family 4A (NR4A) Members NR4A2 and
            NR4A3 Selectively Modulate Elements of the Monocyte Response to
            Buffered Hypercapnia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Wang,J., Chen,S., Xiang,W., Zhu,Q. and Ren,N.
  TITLE     NRF1 Alleviated Oxidative Stress of Glioblastoma Cells by
            Regulating NOR1
  JOURNAL   Folia Biol (Praha) 69 (1), 13-21 (2023)
   PUBMED   37962027
  REMARK    GeneRIF: NRF1 Alleviated Oxidative Stress of Glioblastoma Cells by
            Regulating NOR1.
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Labelle,Y., Bussieres,J., Courjal,F. and Goldring,M.B.
  TITLE     The EWS/TEC fusion protein encoded by the t(9;22) chromosomal
            translocation in human chondrosarcomas is a highly potent
            transcriptional activator
  JOURNAL   Oncogene 18 (21), 3303-3308 (1999)
   PUBMED   10359536
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Ohkura,N., Ito,M., Tsukada,T., Sasaki,K., Yamaguchi,K. and Miki,K.
  TITLE     Alternative splicing generates isoforms of human neuron-derived
            orphan receptor-1 (NOR-1) mRNA
  JOURNAL   Gene 211 (1), 79-85 (1998)
   PUBMED   9573341
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Ohkura,N., Ito,M., Tsukada,T., Sasaki,K., Yamaguchi,K. and Miki,K.
  TITLE     Structure, mapping and expression of a human NOR-1 gene, the third
            member of the Nur77/NGFI-B family
  JOURNAL   Biochim Biophys Acta 1308 (3), 205-214 (1996)
   PUBMED   8809112
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Hedvat,C.V. and Irving,S.G.
  TITLE     The isolation and characterization of MINOR, a novel
            mitogen-inducible nuclear orphan receptor
  JOURNAL   Mol Endocrinol 9 (12), 1692-1700 (1995)
   PUBMED   8614405
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Ohkura,N., Hijikuro,M., Yamamoto,A. and Miki,K.
  TITLE     Molecular cloning of a novel thyroid/steroid receptor superfamily
            gene from cultured rat neuronal cells
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1959-1965 (1994)
   PUBMED   7811288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK226108.1, S81243.1,
            AL358937.16 and U12767.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 24, 2003 this sequence version replaced NP_008912.1.
            
            Summary: This gene encodes a member of the steroid-thyroid
            hormone-retinoid receptor superfamily. The encoded protein may act
            as a transcriptional activator. The protein can efficiently bind
            the NGFI-B Response Element (NBRE). Three different versions of
            extraskeletal myxoid chondrosarcomas (EMCs) are the result of
            reciprocal translocations between this gene and other genes. The
            translocation breakpoints are associated with Nuclear Receptor
            Subfamily 4, Group A, Member 3 (on chromosome 9) and either Ewing
            Sarcome Breakpoint Region 1 (on chromosome 22), RNA Polymerase II,
            TATA Box-Binding Protein-Associated Factor, 68-KD (on chromosome
            17), or Transcription factor 12 (on chromosome 15). Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) lacks the exon containing the
            translational start site compared to variant 3. The resulting
            isoform (a) is shorter at the N-terminus compared to isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK226108.1, D78579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395097.7/ ENSP00000378531.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..626
                     /product="nuclear receptor subfamily 4 group A member 3
                     isoform a"
                     /note="chondrosarcoma, extraskeletal myxoid, fused to EWS;
                     translocated in extraskeletal chondrosarcoma; nuclear
                     hormone receptor NOR-1; neuron-derived orphan receptor 1;
                     mitogen-induced nuclear orphan receptor"
                     /calculated_mol_wt=68099
     Region          290..364
                     /region_name="NR_DBD_NGFI-B"
                     /note="DNA-binding domain of the orphan nuclear receptor,
                     nerve growth factor-induced-B; cd06969"
                     /db_xref="CDD:143527"
     Site            order(292,295,309,312,328,334,344,347)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143527"
     Site            order(301..304,310..311,313,315,317..318,341..342,345,348,
                     361..363)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143527"
     Region          396..626
                     /region_name="NR_LBD"
                     /note="The ligand binding domain of nuclear receptors, a
                     family of ligand-activated transcription regulators;
                     cl11397"
                     /db_xref="CDD:472173"
     Site            order(437..438,441,444..445,474..475,478..479,482,485,517)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132726"
     Site            order(446,449,453,458,463..464,466..467,470..471)
                     /site_type="active"
                     /note="coregulator recognition site [active]"
                     /db_xref="CDD:132726"
     CDS             1..626
                     /gene="NR4A3"
                     /gene_synonym="CHN; CSMF; MINOR; NOR1"
                     /coded_by="NM_006981.4:700..2580"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6743.1"
                     /db_xref="GeneID:8013"
                     /db_xref="HGNC:HGNC:7982"
                     /db_xref="MIM:600542"
ORIGIN      
        1 mpcvqaqysp sppgssyaaq tysseyttei mnpdytkltm dlgsteitat attslpsist
       61 fvegyssnye lkpscvyqmq rplikveegr apsyhhhhhh hhhhhhhhqq qhqqpsippa
      121 sspedevlps tsmyfkqspp stpttpafpp qagalwdeal psapgciapg plldppmkav
      181 ptvagarfpl fhfkpspphp papspagghh lgydptaaaa lslplgaaaa agsqaaales
      241 hpyglplakr aaplafpplg ltpsptassl lgespslpsp psrssssgeg tcavcgdnaa
      301 cqhygvrtce gckgffkrtv qknakyvcla nkncpvdkrr rnrcqycrfq kclsvgmvke
      361 vvrtdslkgr rgrlpskpks plqqepsqps ppsppicmmn alvraltdst prdldysryc
      421 ptdqaaagtd aehvqqfynl ltasidvsrs waekipgftd lpkedqtlli esaflelfvl
      481 rlsirsntae dkfvfcnglv lhrlqclrgf gewldsikdf slnlqslnld iqalaclsal
      541 smiterhglk epkrveelcn kitsslkdhq skgqalepte skvlgalvel rkictlglqr
      601 ifylkledlv sppsiidklf ldtlpf
//
LOCUS       NP_001289980             606 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 12 isoform 1 [Homo sapiens].
ACCESSION   NP_001289980
VERSION     NP_001289980.1
DBSOURCE    REFSEQ: accession NM_001303051.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Rondou,P., Haegeman,G., Vanhoenacker,P. and Van Craenenbroeck,K.
  TITLE     BTB Protein KLHL12 targets the dopamine D4 receptor for
            ubiquitination by a Cul3-based E3 ligase
  JOURNAL   J Biol Chem 283 (17), 11083-11096 (2008)
   PUBMED   18303015
  REMARK    GeneRIF: KLHL12 specifically interacts with the D4 polymorphism,
            thereby building up a Cul3-E3 ligase complex with substrate
            specificity toward the D4 receptor
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Sumara,I., Quadroni,M., Frei,C., Olma,M.H., Sumara,G., Ricci,R. and
            Peter,M.
  TITLE     A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
            regulating mitotic progression and completion of cytokinesis in
            human cells
  JOURNAL   Dev Cell 12 (6), 887-900 (2007)
   PUBMED   17543862
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Angers,S., Thorpe,C.J., Biechele,T.L., Goldenberg,S.J., Zheng,N.,
            MacCoss,M.J. and Moon,R.T.
  TITLE     The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the
            Wnt-beta-catenin pathway by targeting Dishevelled for degradation
  JOURNAL   Nat Cell Biol 8 (4), 348-357 (2006)
   PUBMED   16547521
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Uchida,K., Akita,Y., Matsuo,K., Fujiwara,S., Nakagawa,A.,
            Kazaoka,Y., Hachiya,H., Naganawa,Y., Oh-Iwa,I., Ohura,K., Saga,S.,
            Kawai,T., Matsumoto,Y., Shimozato,K. and Kozaki,K.
  TITLE     Identification of specific autoantigens in Sjogren's syndrome by
            SEREX
  JOURNAL   Immunology 116 (1), 53-63 (2005)
   PUBMED   16108817
REFERENCE   10 (residues 1 to 606)
  AUTHORS   Mai,A., Jung,S.K. and Yonehara,S.
  TITLE     hDKIR, a human homologue of the Drosophila kelch protein, involved
            in a ring-like structure
  JOURNAL   Exp Cell Res 300 (1), 72-83 (2004)
   PUBMED   15383316
  REMARK    GeneRIF: molecular cloning and characterization of a novel gene,
            encoded a human kelch protein containing 568 amino acid residues,
            termed hDKIR.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301791.1, AK027656.1 and
            AK024412.1.
            
            Summary: This gene encodes a member of the KLHL (Kelch-like) family
            of proteins. This protein has been identified as an autoantigen in
            the autoimmune disease Sjogren's syndrome and as a potential
            biomarker in primary biliary cirrhosis. This protein may act as a
            substrate adaptor of the Cullin-3 ubiquitin ligase complex to
            promote substrate-specific ubiquitylation. Ubiquitylation by this
            complex has been shown to regulate the Wnt signaling pathway as
            well as COPII vesicle coat size. A pseudogene has been identified
            on chromosome 22. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301791.1, SRR5189667.218743.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..606
                     /product="kelch-like protein 12 isoform 1"
                     /note="kelch-like protein C3IP1; CUL3-interacting protein
                     1; DKIR homolog"
                     /calculated_mol_wt=67596
     Region          50..173
                     /region_name="BTB_POZ_KLHL12_C3IP1_DKIR"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 12 (KLHL12); cd18242"
                     /db_xref="CDD:349551"
     Region          168..303
                     /region_name="BACK_KLHL12"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 12 (KLHL12); cd18452"
                     /db_xref="CDD:350527"
     Region          312..353
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          320..367
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          346..603
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          357..403
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          407..450
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          454..497
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          501..545
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          548..593
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..606
                     /gene="KLHL12"
                     /gene_synonym="C3IP1; DKIR"
                     /coded_by="NM_001303051.2:51..1871"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:59349"
                     /db_xref="HGNC:HGNC:19360"
                     /db_xref="MIM:614522"
ORIGIN      
        1 mdvnkfeasv gfldvkkfls twklqnprth fvlsphcfmg gimapkdimt nthaksilns
       61 mnslrksntl cdvtlrveqk dfpahrivla acsdyfcamf tselsekgkp yvdiqgltas
      121 tmeilldfvy tetvhvtven vqellpaacl lqlkgvkqac ceflesqldp snclgirdfa
      181 ethncvdlmq aaevfsqkhf pevvqheefi llsqgevekl ikcdeiqvds eepvfeavin
      241 wvkhakkere eslpnllqyv rmplltpryi tdvidaepfi rcslqcrdlv deakkfhlrp
      301 elrsqmqgpr trarlganev llvvggfgsq qspidvveky dpktqewsfl psitrkrryv
      361 asvslhdriy viggydgrsr lssvecldyt adedgvwysv apmnvrrgla gattlgdmiy
      421 vsggfdgsrr htsmerydpn idqwsmlgdm qtaregaglv vasgviyclg gydglnilns
      481 vekydphtgh wtnvtpmatk rsgagvalln dhiyvvggfd gtahlssvea ynirtdswtt
      541 vtsmttprcy vgatvlrgrl yaiagydgns llssiecydp iidswevvts mgtqrcdagv
      601 cvlrek
//
LOCUS       NP_612815                233 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 1 isoform Bcl-X(L) [Homo sapiens].
ACCESSION   NP_612815
VERSION     NP_612815.1
DBSOURCE    REFSEQ: accession NM_138578.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Nguyen,T.T., Torrini,C., Shang,E., Shu,C., Mun,J.Y., Gao,Q.,
            Humala,N., Akman,H.O., Zhang,G., Westhoff,M.A., Karpel-Massler,G.,
            Bruce,J.N., Canoll,P. and Siegelin,M.D.
  TITLE     OGDH and Bcl-xL loss causes synthetic lethality in glioblastoma
  JOURNAL   JCI Insight 9 (8), e172565 (2024)
   PUBMED   38483541
  REMARK    GeneRIF: OGDH and Bcl-xL loss causes synthetic lethality in
            glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Li,S., Wang,Y., Chen,Y., Zhang,H., Shen,K. and Guan,H.
  TITLE     PTEN hinders the formation of scars by regulating the levels of
            proteins in the extracellular matrix and promoting the apoptosis of
            dermal fibroblasts through Bcl-xL
  JOURNAL   Arch Biochem Biophys 753, 109912 (2024)
   PUBMED   38325773
  REMARK    GeneRIF: PTEN hinders the formation of scars by regulating the
            levels of proteins in the extracellular matrix and promoting the
            apoptosis of dermal fibroblasts through Bcl-xL.
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Dou,Z., Lei,H., Su,W., Zhang,T., Chen,X., Yu,B., Zhen,X., Si,J.,
            Sun,C., Zhang,H. and Di,C.
  TITLE     Modification of BCLX pre-mRNA splicing has antitumor efficacy alone
            or in combination with radiotherapy in human glioblastoma cells
  JOURNAL   Cell Death Dis 15 (2), 160 (2024)
   PUBMED   38383492
  REMARK    GeneRIF: Modification of BCLX pre-mRNA splicing has antitumor
            efficacy alone or in combination with radiotherapy in human
            glioblastoma cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Yin,L., Hu,X., Pei,G., Tang,M., Zhou,Y., Zhang,H., Huang,M., Li,S.,
            Zhang,J., Citu,C., Zhao,Z., Debeb,B.G., Feng,X. and Chen,J.
  TITLE     Genome-wide CRISPR screen reveals the synthetic lethality between
            BCL2L1 inhibition and radiotherapy
  JOURNAL   Life Sci Alliance 7 (4), e202302353 (2024)
   PUBMED   38316463
  REMARK    GeneRIF: Genome-wide CRISPR screen reveals the synthetic lethality
            between BCL2L1 inhibition and radiotherapy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Broome,H.E., Dargan,C.M., Krajewski,S. and Reed,J.C.
  TITLE     Expression of Bcl-2, Bcl-x, and Bax after T cell activation and
            IL-2 withdrawal
  JOURNAL   J Immunol 155 (5), 2311-2317 (1995)
   PUBMED   7650367
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Sedlak,T.W., Oltvai,Z.N., Yang,E., Wang,K., Boise,L.H.,
            Thompson,C.B. and Korsmeyer,S.J.
  TITLE     Multiple Bcl-2 family members demonstrate selective dimerizations
            with Bax
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7834-7838 (1995)
   PUBMED   7644501
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Jaattela,M., Benedict,M., Tewari,M., Shayman,J.A. and Dixit,V.M.
  TITLE     Bcl-x and Bcl-2 inhibit TNF and Fas-induced apoptosis and
            activation of phospholipase A2 in breast carcinoma cells
  JOURNAL   Oncogene 10 (12), 2297-2305 (1995)
   PUBMED   7540278
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Boise,L.H., Gonzalez-Garcia,M., Postema,C.E., Ding,L., Lindsten,T.,
            Turka,L.A., Mao,X., Nunez,G. and Thompson,C.B.
  TITLE     bcl-x, a bcl-2-related gene that functions as a dominant regulator
            of apoptotic cell death
  JOURNAL   Cell 74 (4), 597-608 (1993)
   PUBMED   8358789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU845775.1 and BC019307.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The proteins encoded by this
            gene are located at the outer mitochondrial membrane, and have been
            shown to regulate outer mitochondrial membrane channel (VDAC)
            opening. VDAC regulates mitochondrial membrane potential, and thus
            controls the production of reactive oxygen species and release of
            cytochrome C by mitochondria, both of which are the potent inducers
            of cell apoptosis. Alternative splicing results in multiple
            transcript variants encoding two different isoforms. The longer
            isoform acts as an apoptotic inhibitor and the shorter isoform acts
            as an apoptotic activator. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (Bcl-X(L), also known as
            Bcl-xL). Variants 1, 3, 4 and 5 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.276060.1,
                                           SRR3476690.942208.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000307677.5/
                                                  ENSP00000302564.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
     Protein         1..233
                     /product="bcl-2-like protein 1 isoform Bcl-X(L)"
                     /note="bcl-2-like protein 1; apoptosis regulator Bcl-X;
                     protein phosphatase 1, regulatory subunit 52"
                     /calculated_mol_wt=25918
     Region          1..233
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Region          4..24
                     /region_name="BH4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Region          28..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PLK3.
                     /evidence=ECO:0000269|PubMed:21840391; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            61..62
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-1; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:19917720; propagated from
                     UniProtKB/Swiss-Prot (Q07817.1)"
     Region          86..100
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            90..98
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(93..94,96..97,101,104..105,121..122,125..126,
                     129..130,136,138..139,141..142,146,150,194)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          129..148
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            order(129..131,135..147)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          180..195
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     Site            180..194
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            210..226
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07817.1)"
     CDS             1..233
                     /gene="BCL2L1"
                     /gene_synonym="Bcl-X; BCL-XL/S; BCL2L; BCLX; PPP1R52"
                     /coded_by="NM_138578.3:382..1083"
                     /note="isoform Bcl-X(L) is encoded by transcript variant
                     1"
                     /db_xref="CCDS:CCDS13189.1"
                     /db_xref="GeneID:598"
                     /db_xref="HGNC:HGNC:992"
                     /db_xref="MIM:600039"
ORIGIN      
        1 msqsnrelvv dflsyklsqk gyswsqfsdv eenrteapeg tesemetpsa ingnpswhla
       61 dspavngatg hsssldarev ipmaavkqal reagdefelr yrrafsdlts qlhitpgtay
      121 qsfeqvvnel frdgvnwgri vaffsfggal cvesvdkemq vlvsriaawm atylndhlep
      181 wiqenggwdt fvelygnnaa aesrkgqerf nrwfltgmtv agvvllgslf srk
//
LOCUS       NP_001265151             322 aa            linear   PRI 20-NOV-2025
DEFINITION  centriolar satellite-associated tubulin polyglutamylase complex
            regulator 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001265151
VERSION     NP_001265151.1
DBSOURCE    REFSEQ: accession NM_001278222.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 322)
  AUTHORS   Wang,L., Paudyal,S.C., Kang,Y., Owa,M., Liang,F.X., Spektor,A.,
            Knaut,H., Sanchez,I. and Dynlacht,B.D.
  TITLE     Regulators of tubulin polyglutamylation control nuclear shape and
            cilium disassembly by balancing microtubule and actin assembly
  JOURNAL   Cell Res 32 (2), 190-209 (2022)
   PUBMED   34782749
REFERENCE   2  (residues 1 to 322)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 322)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 322)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 322)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   6  (residues 1 to 322)
  AUTHORS   He,L., Wu,W.J., Yang,J.K., Cheng,H., Zuo,X.B., Lai,W., Gao,T.W.,
            Ma,C.L., Luo,N., Huang,J.Q., Lu,F.Y., Liu,Y.Q., Huang,Y.J.,
            Lu,Q.J., Zhang,H.L., Wang,L., Wang,W.Z., Wang,M.M., Xiao,S.X.,
            Sun,Q., Li,C.Y., Bai,Y.P., Li,H., Zhou,Z.C., Zhou,F.S., Chen,G.,
            Liang,B., Qi,J., Yang,X.Y., Yang,T., Zheng,X., Sun,L.D., Zhang,X.J.
            and Zhang,Y.P.
  TITLE     Two new susceptibility loci 1q24.2 and 11p11.2 confer risk to
            severe acne
  JOURNAL   Nat Commun 5, 2870 (2014)
   PUBMED   24399259
REFERENCE   7  (residues 1 to 322)
  AUTHORS   Smith,N.L., Huffman,J.E., Strachan,D.P., Huang,J., Dehghan,A.,
            Trompet,S., Lopez,L.M., Shin,S.Y., Baumert,J., Vitart,V., Bis,J.C.,
            Wild,S.H., Rumley,A., Yang,Q., Uitterlinden,A.G., Stott,D.J.,
            Davies,G., Carter,A.M., Thorand,B., Polasek,O., McKnight,B.,
            Campbell,H., Rudnicka,A.R., Chen,M.H., Buckley,B.M., Harris,S.E.,
            Peters,A., Pulanic,D., Lumley,T., de Craen,A.J., Liewald,D.C.,
            Gieger,C., Campbell,S., Ford,I., Gow,A.J., Luciano,M.,
            Porteous,D.J., Guo,X., Sattar,N., Tenesa,A., Cushman,M.,
            Slagboom,P.E., Visscher,P.M., Spector,T.D., Illig,T., Rudan,I.,
            Bovill,E.G., Wright,A.F., McArdle,W.L., Tofler,G., Hofman,A.,
            Westendorp,R.G., Starr,J.M., Grant,P.J., Karakas,M., Hastie,N.D.,
            Psaty,B.M., Wilson,J.F., Lowe,G.D., O'Donnell,C.J., Witteman,J.C.,
            Jukema,J.W., Deary,I.J., Soranzo,N., Koenig,W. and Hayward,C.
  TITLE     Genetic predictors of fibrin D-dimer levels in healthy adults
  JOURNAL   Circulation 123 (17), 1864-1872 (2011)
   PUBMED   21502573
REFERENCE   8  (residues 1 to 322)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 322)
  AUTHORS   Kitazawa,H., Iida,J., Uchida,A., Haino-Fukushima,K., Itoh,T.J.,
            Hotani,H., Ookata,K., Murofushi,H., Bulinski,J.C., Kishimoto,T. and
            Hisanaga,S.
  TITLE     Ser787 in the proline-rich region of human MAP4 is a critical
            phosphorylation site that reduces its activity to promote tubulin
            polymerization
  JOURNAL   Cell Struct Funct 25 (1), 33-39 (2000)
   PUBMED   10791892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA487960.1, AK300813.1 and BI763384.1.
            
            Transcript Variant: This variant (5) lacks an exon in the 5' coding
            region which results in an upstream start codon, and has an
            alternate splice site in the 3' coding region, compared to variant
            2. The resulting isoform (5) has a distinct N-terminus and lacks an
            internal segment in the C-terminal region, compared to isoform 2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.170478.1, AK300813.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..322
                     /product="centriolar satellite-associated tubulin
                     polyglutamylase complex regulator 1 isoform 5"
                     /note="UPF0705 protein C11orf49; centriolar
                     satellite-associated tubulin polyglutamylation protein 1"
                     /calculated_mol_wt=35315
     Region          <42..59
                     /region_name="DD_R_PKA_DPY30-like"
                     /note="dimerization/docking (D/D) domains found in the
                     cAMP-dependent protein kinase regulatory subunit (PRKAR)
                     and the DPY30/SDC1-like family; cl02594"
                     /db_xref="CDD:445844"
     CDS             1..322
                     /gene="CSTPP1"
                     /gene_synonym="C11orf49"
                     /coded_by="NM_001278222.1:42..1010"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:79096"
                     /db_xref="HGNC:HGNC:28720"
                     /db_xref="MIM:620479"
ORIGIN      
        1 materdgnlg sgsrragalk pprskdaesg apsptglrvs gfnsvcqgth ilfrefsfvq
       61 atphnrvsfl rafwrcfrtv gkngdlltmk eyhcllqllc pdfpleltqk aarivlmdda
      121 mdclmsfsdf lfafqiqfyy sefldsvaai yedllsgknp ntvivptsss gqhrqrpalg
      181 gagtlegvea slfyqclenl cdrhkyscpp palvkealsn vqrltfygfl malskhrgin
      241 qalgalpdkg dlmhdpamde elerllaqvp glvnsvtasp easclpsrtp prvgspwrpl
      301 hhsrkvdges dgsteetdes et
//
LOCUS       NP_001012329              81 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-catenin-interacting protein 1 [Homo sapiens].
ACCESSION   NP_001012329
VERSION     NP_001012329.1
DBSOURCE    REFSEQ: accession NM_001012329.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Zhang,T., Zhang,Y., Xu,H., Lan,J., Feng,Z., Huang,R., Geng,J.,
            Chi,H. and Bai,X.
  TITLE     LINC00355 Mediates CTNNBIP1 Promoter Methylation and Promotes
            Endoplasmic Reticulum Stress-Induced Podocyte Injury in Diabetic
            Nephropathy
  JOURNAL   Antioxid Redox Signal 39 (4-6), 225-240 (2023)
   PUBMED   36738224
  REMARK    GeneRIF: LINC00355 Mediates CTNNBIP1 Promoter Methylation and
            Promotes Endoplasmic Reticulum Stress-Induced Podocyte Injury in
            Diabetic Nephropathy.
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Wang,Z., Hu,J., Chen,J., Zhang,J., Li,W., Tian,Y., Liu,H. and
            Yang,X.
  TITLE     ICAT promotes colorectal cancer metastasis via binding to JUP and
            activating the NF-kappaB signaling pathway
  JOURNAL   J Clin Lab Anal 36 (10), e24678 (2022)
   PUBMED   36036768
  REMARK    GeneRIF: ICAT promotes colorectal cancer metastasis via binding to
            JUP and activating the NF-kappaB signaling pathway.
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Han,H., Zhu,B., Xie,J., Huang,Y., Geng,Y., Chen,K. and Wang,W.
  TITLE     Expression level and prognostic potential of
            beta-catenin-interacting protein in acute myeloid leukemia
  JOURNAL   Medicine (Baltimore) 101 (33), e30022 (2022)
   PUBMED   35984200
  REMARK    GeneRIF: Expression level and prognostic potential of
            beta-catenin-interacting protein in acute myeloid leukemia.
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Hu,J., Wang,Z., Chen,J., Yu,Z., Zhang,J., Li,W., Lin,M., Yang,X.
            and Liu,H.
  TITLE     Overexpression of ICAT Inhibits the Progression of Colorectal
            Cancer by Binding with beta-Catenin in the Cytoplasm
  JOURNAL   Technol Cancer Res Treat 20, 15330338211041253 (2021)
   PUBMED   34569368
  REMARK    GeneRIF: Overexpression of ICAT Inhibits the Progression of
            Colorectal Cancer by Binding with beta-Catenin in the Cytoplasm.
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Reifenberger,J., Knobbe,C.B., Wolter,M., Blaschke,B., Schulte,K.W.,
            Pietsch,T., Ruzicka,T. and Reifenberger,G.
  TITLE     Molecular genetic analysis of malignant melanomas for aberrations
            of the WNT signaling pathway genes CTNNB1, APC, ICAT and BTRC
  JOURNAL   Int J Cancer 100 (5), 549-556 (2002)
   PUBMED   12124804
  REMARK    GeneRIF: Molecular genetic analysis of malignant melanomas for
            aberrations of the WNT signaling pathway genes CTNNB1, APC, ICAT
            and BTRC.
REFERENCE   7  (residues 1 to 81)
  AUTHORS   von Koch,C.S., Gulati,M., Aldape,K. and Berger,M.S.
  TITLE     Familial medulloblastoma: case report of one family and review of
            the literature
  JOURNAL   Neurosurgery 51 (1), 227-33 (2002)
   PUBMED   12182422
  REMARK    GeneRIF: presentation of medulloblastoma in two siblings (one of
            each sex) and their great-uncle; immunostaining for gene products
            in medulloblastoma differed in the two siblings for beta-catenin
            and was similar with staining for gli.
            Review article
REFERENCE   8  (residues 1 to 81)
  AUTHORS   Ashihara,K., Saito,T., Mizumoto,H., Adachi,K., Tanaka,R.,
            Nishimura,M., Ito,E. and Kudo,R.
  TITLE     Loss of gamma-Catenin expression in squamous differentiation in
            endometrial carcinomas
  JOURNAL   Int J Gynecol Pathol 21 (3), 246-254 (2002)
   PUBMED   12068170
  REMARK    GeneRIF: stimulation of beta-catenin and suppression of
            gamma-catenin expression, occur within endometrial carcinomas with
            squamous differentiation
REFERENCE   9  (residues 1 to 81)
  AUTHORS   Tutter,A.V., Fryer,C.J. and Jones,K.A.
  TITLE     Chromatin-specific regulation of LEF-1-beta-catenin transcription
            activation and inhibition in vitro
  JOURNAL   Genes Dev 15 (24), 3342-3354 (2001)
   PUBMED   11751639
REFERENCE   10 (residues 1 to 81)
  AUTHORS   Tago,K., Nakamura,T., Nishita,M., Hyodo,J., Nagai,S., Murata,Y.,
            Adachi,S., Ohwada,S., Morishita,Y., Shibuya,H. and Akiyama,T.
  TITLE     Inhibition of Wnt signaling by ICAT, a novel
            beta-catenin-interacting protein
  JOURNAL   Genes Dev 14 (14), 1741-1749 (2000)
   PUBMED   10898789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357140.33 and CB995652.1.
            
            Summary: The protein encoded by this gene binds CTNNB1 and prevents
            interaction between CTNNB1 and TCF family members. The encoded
            protein is a negative regulator of the Wnt signaling pathway. Two
            transcript variants encoding the same protein have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.854634.1,
                                           DRR138524.297196.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..81
                     /product="beta-catenin-interacting protein 1"
                     /note="beta-catenin-interacting protein ICAT; inhibitor of
                     beta-catenin and Tcf-4"
                     /calculated_mol_wt=9039
     Region          1..79
                     /region_name="ICAT"
                     /note="Beta-catenin-interacting protein ICAT; pfam06384"
                     /db_xref="CDD:399405"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJN6; propagated from
                     UniProtKB/Swiss-Prot (Q9NSA3.1)"
     CDS             1..81
                     /gene="CTNNBIP1"
                     /gene_synonym="ICAT"
                     /coded_by="NM_001012329.2:285..530"
                     /db_xref="CCDS:CCDS106.1"
                     /db_xref="GeneID:56998"
                     /db_xref="HGNC:HGNC:16913"
                     /db_xref="MIM:607758"
ORIGIN      
        1 mnregapgks peemyiqqkv rvllmlrkmg snltaseeef lrtyagvvns qlsqlpphsi
       61 dqgaedvvma fsrsetedrr q
//
LOCUS       NP_001269519             228 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 7 isoform d precursor [Homo sapiens].
ACCESSION   NP_001269519 XP_005245445
VERSION     NP_001269519.1
DBSOURCE    REFSEQ: accession NM_001282590.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Chu,E., Wu,J., Kang,S.S. and Kang,Y.
  TITLE     SLAMF7 as a Promising Immunotherapeutic Target in Multiple Myeloma
            Treatments
  JOURNAL   Curr Oncol 30 (9), 7891-7903 (2023)
   PUBMED   37754488
  REMARK    GeneRIF: SLAMF7 as a Promising Immunotherapeutic Target in Multiple
            Myeloma Treatments.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Choe,U., Pham,Q., Kim,Y.S., Yu,L. and Wang,T.T.Y.
  TITLE     Identification and elucidation of cross talk between SLAM Family
            Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages
  JOURNAL   Sci Rep 13 (1), 11007 (2023)
   PUBMED   37420084
  REMARK    GeneRIF: Identification and elucidation of cross talk between SLAM
            Family Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 228)
  AUTHORS   O'Connell,P., Blake,M.K., Godbehere,S., Amalfitano,A. and
            Aldhamen,Y.A.
  TITLE     SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity
  JOURNAL   J Neuroinflammation 19 (1), 241 (2022)
   PUBMED   36199066
  REMARK    GeneRIF: SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Simmons,D.P., Nguyen,H.N., Gomez-Rivas,E., Jeong,Y., Jonsson,A.H.,
            Chen,A.F., Lange,J.K., Dyer,G.S., Blazar,P., Earp,B.E.,
            Coblyn,J.S., Massarotti,E.M., Sparks,J.A., Todd,D.J., Rao,D.A.,
            Kim,E.Y. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership (AMP) RA/SLE Network
  TITLE     SLAMF7 engagement superactivates macrophages in acute and chronic
            inflammation
  JOURNAL   Sci Immunol 7 (68), eabf2846 (2022)
   PUBMED   35148199
  REMARK    GeneRIF: SLAMF7 engagement superactivates macrophages in acute and
            chronic inflammation.
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Lee,J.K., Boles,K.S. and Mathew,P.A.
  TITLE     Molecular and functional characterization of a CS1 (CRACC) splice
            variant expressed in human NK cells that does not contain
            immunoreceptor tyrosine-based switch motifs
  JOURNAL   Eur J Immunol 34 (10), 2791-2799 (2004)
   PUBMED   15368295
  REMARK    GeneRIF: CS1-L and CS1-S may differentially regulate human NK cell
            functions
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Tovar,V., del Valle,J., Zapater,N., Martin,M., Romero,X.,
            Pizcueta,P., Bosch,J., Terhorst,C. and Engel,P.
  TITLE     Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family
            of leukocyte cell-surface receptors
  JOURNAL   Immunogenetics 54 (6), 394-402 (2002)
   PUBMED   12242590
REFERENCE   8  (residues 1 to 228)
  AUTHORS   Murphy,J.J., Hobby,P., Vilarino-Varela,J., Bishop,B.,
            Iordanidou,P., Sutton,B.J. and Norton,J.D.
  TITLE     A novel immunoglobulin superfamily receptor (19A) related to CD2 is
            expressed on activated lymphocytes and promotes homotypic B-cell
            adhesion
  JOURNAL   Biochem J 361 (Pt 3), 431-436 (2002)
   PUBMED   11802771
REFERENCE   9  (residues 1 to 228)
  AUTHORS   Bouchon,A., Cella,M., Grierson,H.L., Cohen,J.I. and Colonna,M.
  TITLE     Activation of NK cell-mediated cytotoxicity by a SAP-independent
            receptor of the CD2 family
  JOURNAL   J Immunol 167 (10), 5517-5521 (2001)
   PUBMED   11698418
REFERENCE   10 (residues 1 to 228)
  AUTHORS   Boles,K.S. and Mathew,P.A.
  TITLE     Molecular cloning of CS1, a novel human natural killer cell
            receptor belonging to the CD2 subset of the immunoglobulin
            superfamily
  JOURNAL   Immunogenetics 52 (3-4), 302-307 (2001)
   PUBMED   11220635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388332.1, AL834424.1, AL121985.13 and BQ000581.1.
            
            On Sep 14, 2013 this sequence version replaced XP_005245445.1.
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (d) that is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL834424.1, SRR1163657.21906.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..228
                     /product="SLAM family member 7 isoform d precursor"
                     /note="CD2-like receptor activating cytotoxic cells; 19A24
                     protein; novel LY9 (lymphocyte antigen 9) like protein;
                     protein 19A; CD2 subset 1; membrane protein FOAP-12"
                     /calculated_mol_wt=22673
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3176
     CDS             1..228
                     /gene="SLAMF7"
                     /gene_synonym="19A; CD319; CRACC; CS1"
                     /coded_by="NM_001282590.2:56..742"
                     /note="isoform d precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS60324.1"
                     /db_xref="GeneID:57823"
                     /db_xref="HGNC:HGNC:21394"
                     /db_xref="MIM:606625"
ORIGIN      
        1 magsptcltl iyilwqlteh lskpkvtmgl qsnkngtcvt nltccmehge edviytwkal
       61 gqaaneshng silpiswrwg esdmtficva rnpvsrnfss pilarklceg aaddpdssmv
      121 llclllvpll lslfvlglfl wflkrerqee yieekkrvdi cretpnicph sgenteydti
      181 phtnrtilke dpantvystv eipkkmenph slltmpdtpr lfayenvi
//
LOCUS       NP_001271268            1303 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4 isoform 4 [Homo sapiens].
ACCESSION   NP_001271268 XP_005254464
VERSION     NP_001271268.1
DBSOURCE    REFSEQ: accession NM_001284339.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1303)
  AUTHORS   Kliche,J., Simonetti,L., Krystkowiak,I., Kuss,H., Diallo,M.,
            Rask,E., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Proteome-scale characterisation of motif-based interactome rewiring
            by disease mutations
  JOURNAL   Mol Syst Biol 20 (9), 1025-1048 (2024)
   PUBMED   39009827
REFERENCE   3  (residues 1 to 1303)
  AUTHORS   Ling,X., Xu,W., Tang,J., Cao,Q., Luo,G., Chen,X., Yang,S.,
            Reinach,P.S. and Yan,D.
  TITLE     The Role of Ubiquitination and the E3 Ligase Nedd4 in Regulating
            Corneal Epithelial Wound Healing
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 29 (2024)
   PUBMED   38888282
  REMARK    GeneRIF: The Role of Ubiquitination and the E3 Ligase Nedd4 in
            Regulating Corneal Epithelial Wound Healing.
REFERENCE   4  (residues 1 to 1303)
  AUTHORS   He,J., Yi,J., Ji,L., Dai,L., Chen,Y. and Xue,W.
  TITLE     ECHDC2 inhibits the proliferation of gastric cancer cells by
            binding with NEDD4 to degrade MCCC2 and reduce aerobic glycolysis
  JOURNAL   Mol Med 30 (1), 69 (2024)
   PUBMED   38783226
  REMARK    GeneRIF: ECHDC2 inhibits the proliferation of gastric cancer cells
            by binding with NEDD4 to degrade MCCC2 and reduce aerobic
            glycolysis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1303)
  AUTHORS   Lv,B., Fu,P., Wang,M., Cui,L., Bao,L., Wang,X., Yu,L., Zhou,C.,
            Zhu,M., Wang,F., Pang,Y., Qi,S., Zhang,Z. and Cui,G.
  TITLE     DMT1 ubiquitination by Nedd4 protects against ferroptosis after
            intracerebral hemorrhage
  JOURNAL   CNS Neurosci Ther 30 (4), e14685 (2024)
   PUBMED   38634270
  REMARK    GeneRIF: DMT1 ubiquitination by Nedd4 protects against ferroptosis
            after intracerebral hemorrhage.
REFERENCE   6  (residues 1 to 1303)
  AUTHORS   Staub,O., Gautschi,I., Ishikawa,T., Breitschopf,K., Ciechanover,A.,
            Schild,L. and Rotin,D.
  TITLE     Regulation of stability and function of the epithelial Na+ channel
            (ENaC) by ubiquitination
  JOURNAL   EMBO J 16 (21), 6325-6336 (1997)
   PUBMED   9351815
REFERENCE   7  (residues 1 to 1303)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   8  (residues 1 to 1303)
  AUTHORS   Hatakeyama,S., Jensen,J.P. and Weissman,A.M.
  TITLE     Subcellular localization and ubiquitin-conjugating enzyme (E2)
            interactions of mammalian HECT family ubiquitin protein ligases
  JOURNAL   J Biol Chem 272 (24), 15085-15092 (1997)
   PUBMED   9182527
REFERENCE   9  (residues 1 to 1303)
  AUTHORS   Kumar,S., Harvey,K.F., Kinoshita,M., Copeland,N.G., Noda,M. and
            Jenkins,N.A.
  TITLE     cDNA cloning, expression analysis, and mapping of the mouse Nedd4
            gene
  JOURNAL   Genomics 40 (3), 435-443 (1997)
   PUBMED   9073511
  REMARK    Erratum:[Genomics 1997 Aug 15;44(1):156]
REFERENCE   10 (residues 1 to 1303)
  AUTHORS   Imhof,M.O. and McDonnell,D.P.
  TITLE     Yeast RSP5 and its human homolog hRPF1 potentiate hormone-dependent
            activation of transcription by human progesterone and
            glucocorticoid receptors
  JOURNAL   Mol Cell Biol 16 (6), 2594-2605 (1996)
   PUBMED   8649367
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL832063.1, BC144285.1,
            BC136605.1 and AC009997.7.
            
            On Sep 28, 2013 this sequence version replaced XP_005254464.1.
            
            Summary: This gene is the founding member of the NEDD4 family of
            HECT ubiquitin ligases that function in the ubiquitin proteasome
            system of protein degradation. The encoded protein contains an
            N-terminal calcium and phospholipid binding C2 domain followed by
            multiple tryptophan-rich WW domains and, a C-terminal HECT
            ubiquitin ligase catalytic domain. It plays critical role in the
            regulation of a number of membrane receptors, endocytic machinery
            components and the tumor suppressor PTEN. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (4) contains three alternate
            in-frame exons and uses an alternate in-frame splice site, compared
            to variant 2. The encoded isoform (4) is longer than isoform 2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144285.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..1303
                     /product="E3 ubiquitin-protein ligase NEDD4 isoform 4"
                     /EC_number="2.3.2.26"
                     /note="receptor-potentiating factor 1; cell
                     proliferation-inducing gene 53 protein; neural precursor
                     cell expressed, developmentally down-regulated 4, E3
                     ubiquitin protein ligase; HECT-type E3 ubiquitin
                     transferase NEDD4"
                     /calculated_mol_wt=147253
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Region          204..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46934.4)"
     Region          <517..570
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62940; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Region          595..627
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(611,622)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P46935; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Site            654
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P46935; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Region          700..710
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000269|PubMed:11342538"
                     /note="propagated from UniProtKB/Swiss-Prot (P46934.4)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P46934.4)"
     Region          739..764
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46934.4)"
     Region          753..782
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          780..818
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46934.4)"
     Region          826..855
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          877..909
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(893,904)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(952,983,994,1056,1229,1264..1265,1268..1272,1292,
                     1299)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          970..1299
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(1084,1087..1088,1090..1091,1094,1099,1101,
                     1105..1106,1107,1113,1118,1135,1139)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..1303
                     /gene="NEDD4"
                     /gene_synonym="NEDD4-1; RPF1"
                     /coded_by="NM_001284339.1:301..4212"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61643.1"
                     /db_xref="GeneID:4734"
                     /db_xref="HGNC:HGNC:7727"
                     /db_xref="MIM:602278"
ORIGIN      
        1 maqslrlhfa arrsntypls etsgddldsh vhmcfkrptr istsnvvqmk ltprqtalap
       61 likenvqsqe rssvpssenv nkkssclqis lqptrysgyl qssnvladsd dasftcilkd
      121 giyssavvdn elnavndghl vsspaicsgs lsnfstsdng syssngsdfg scasitsggs
      181 ytnsvisdss sytfppsddt flggnlpsds tsnrsvpnrn ttpceifsrs tstdpfvqdd
      241 lehgleimkl pvsrntkipl krysslvifp rspsttrpts ptslctllsk gsyqtshqfi
      301 ispseiahne dgtsakgfls tavnglrlsk tictpgevrd irplhrkgsl qkkivlsnnt
      361 prqtvcekss egyscvsvhf tqrkaatldc ettngdckpe mseiklnsds eyiklmhrts
      421 aclpssqnvd cqiningele rphsqmnknh gilrrsislg gaypniscls slkhncskgg
      481 psqllikfas gnegkvdnls rdsnrdctne lsnscktrdd flgqvdvply plptenprle
      541 rpytfkdfvl hprshksrvk gylrlkmtyl pktsgseddn aeqaeeleqq qepsplppgw
      601 eerqdilgrt yyvnhesrrt qwkrptpqdn ltdaengniq lqaqrafttr rqiseetesv
      661 dnressenwe iiredeatmy snqafpsppp ssnldvpthl aeelnarlti fgnsavsqpa
      721 sssnhssrrg slqaytfeeq ptlpvllpts sglppgweek qdergrsyyv dhnsrtttwt
      781 kptvqatvet sqltssqssa gpqsqastsd sgqqvtqpse ieqgflpkgw evrhapngrp
      841 ffidhntktt twedprlkip ahlrgktsld tsndlgplpp gweerthtdg rifyinhnik
      901 rtqwedprle nvaitgpavp ysrdykrkye ffrrklkkqn dipnkfemkl rratvledsy
      961 rrimgvkrad flkarlwief dgekgldygg varewfflis kemfnpyygl feysatdnyt
     1021 lqinpnsglc nedhlsyfkf igrvagmavy hgklldgffi rpfykmmlhk pitlhdmesv
     1081 dseyynslrw ilendpteld lrfiideelf gqthqhelkn ggseivvtnk nkkeyiylvi
     1141 qwrfvnriqk qmaafkegff elipqdliki fdenelellm cglgdvdvnd wrehtkykng
     1201 ysanhqviqw fwkavlmmds ekrirllqfv tgtsrvpmng faelygsngp qsftveqwgt
     1261 peklprahtc fnrldlppye sfeelwdklq maientqgfd gvd
//
LOCUS       NP_056210               1165 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonin beta-propeller repeat-containing protein 1 [Homo sapiens].
ACCESSION   NP_056210
VERSION     NP_056210.1
DBSOURCE    REFSEQ: accession NM_015395.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Kaur,N., de la Ballina,L.R., Haukaas,H.S., Torgersen,M.L.,
            Radulovic,M., Munson,M.J., Sabirsh,A., Stenmark,H., Simonsen,A.,
            Carlsson,S.R. and Lystad,A.H.
  TITLE     TECPR1 is activated by damage-induced sphingomyelin exposure to
            mediate noncanonical autophagy
  JOURNAL   EMBO J 42 (17), e113105 (2023)
   PUBMED   37409525
  REMARK    GeneRIF: TECPR1 is activated by damage-induced sphingomyelin
            exposure to mediate noncanonical autophagy.
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Cao,L. and Lin,F.
  TITLE     TECPR1 Induces Apoptosis in Non-Small Cell Lung Carcinoma via ATG5
            Upregulation-Induced Autophagy Promotion
  JOURNAL   Ann Clin Lab Sci 52 (4), 580-592 (2022)
   PUBMED   36197771
  REMARK    GeneRIF: TECPR1 Induces Apoptosis in Non-Small Cell Lung Carcinoma
            via ATG5 Upregulation-Induced Autophagy Promotion.
REFERENCE   4  (residues 1 to 1165)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1165)
  AUTHORS   Kim,J.H., Hong,S.B., Lee,J.K., Han,S., Roh,K.H., Lee,K.E.,
            Kim,Y.K., Choi,E.J. and Song,H.K.
  TITLE     Insights into autophagosome maturation revealed by the structures
            of ATG5 with its interacting partners
  JOURNAL   Autophagy 11 (1), 75-87 (2015)
   PUBMED   25484072
REFERENCE   7  (residues 1 to 1165)
  AUTHORS   Chen,D., Fan,W., Lu,Y., Ding,X., Chen,S. and Zhong,Q.
  TITLE     A mammalian autophagosome maturation mechanism mediated by TECPR1
            and the Atg12-Atg5 conjugate
  JOURNAL   Mol Cell 45 (5), 629-641 (2012)
   PUBMED   22342342
  REMARK    GeneRIF: The concerted interactions among TECPR1, Atg12-Atg5, and
            PtdIns(3)P provide the fusion specificity between autophagosomes
            and lysosomes and that the assembly of this complex initiates the
            autophagosome maturation process.
REFERENCE   8  (residues 1 to 1165)
  AUTHORS   Ogawa,M. and Sasakawa,C.
  TITLE     The role of Tecpr1 in selective autophagy as a cargo receptor
  JOURNAL   Autophagy 7 (11), 1389-1391 (2011)
   PUBMED   21795850
REFERENCE   9  (residues 1 to 1165)
  AUTHORS   Ogawa,M., Yoshikawa,Y., Kobayashi,T., Mimuro,H., Fukumatsu,M.,
            Kiga,K., Piao,Z., Ashida,H., Yoshida,M., Kakuta,S., Koyama,T.,
            Goto,Y., Nagatake,T., Nagai,S., Kiyono,H., Kawalec,M.,
            Reichhart,J.M. and Sasakawa,C.
  TITLE     A Tecpr1-dependent selective autophagy pathway targets bacterial
            pathogens
  JOURNAL   Cell Host Microbe 9 (5), 376-389 (2011)
   PUBMED   21575909
REFERENCE   10 (residues 1 to 1165)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091654.4.
            
            Summary: This gene encodes a tethering factor involved in
            autophagy. The encoded protein is found at autolysosomes, and is
            involved in targeting protein aggregates, damaged mitochondria, and
            bacterial pathogens for autophagy [provided by RefSeq, Nov 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053591.1, AK292996.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000447648.7/ ENSP00000404923.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..1165
                     /product="tectonin beta-propeller repeat-containing
                     protein 1"
                     /calculated_mol_wt=129566
     Region          64..125
                     /region_name="DysFN"
                     /note="Dysferlin domain, N-terminal region; smart00693"
                     /db_xref="CDD:214777"
     Region          206..375
                     /region_name="Tectonin"
                     /note="Tectonin domain; pfam19193"
                     /db_xref="CDD:465992"
     Region          209..240
                     /region_name="TECPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          254..285
                     /region_name="TECPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          301..332
                     /region_name="TECPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          344..376
                     /region_name="TECPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          404..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80VP0; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          604..724
                     /region_name="PH1_TECPR1"
                     /note="Tectonin beta-propeller repeat-containing protein 1
                     Pleckstrin homology (PH) domain, repeat 1; cd13300"
                     /db_xref="CDD:270112"
     Region          729..756
                     /region_name="TECPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          761..794
                     /region_name="TECPR"
                     /note="Beta propeller repeats in Physarum polycephalum
                     tectonins, Limulus lectin L-6 and animal hypothetical
                     proteins; smart00706"
                     /db_xref="CDD:214782"
     Region          816..877
                     /region_name="DysFN"
                     /note="Dysferlin domain, N-terminal region; smart00693"
                     /db_xref="CDD:214777"
     Region          888..921
                     /region_name="DysFC"
                     /note="Dysferlin domain, C-terminal region; smart00694"
                     /db_xref="CDD:128935"
     Region          922..1136
                     /region_name="Tectonin"
                     /note="Tectonin domain; pfam19193"
                     /db_xref="CDD:465992"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Site            949
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          953..984
                     /region_name="TECPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          998..1029
                     /region_name="TECPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          1044..1075
                     /region_name="TECPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          1087..1127
                     /region_name="TECPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     Region          1140..1165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6L1.1)"
     CDS             1..1165
                     /gene="TECPR1"
                     /coded_by="NM_015395.3:282..3779"
                     /db_xref="CCDS:CCDS47648.1"
                     /db_xref="GeneID:25851"
                     /db_xref="HGNC:HGNC:22214"
                     /db_xref="MIM:614781"
ORIGIN      
        1 mpnsvlwavd lfgrvytlst agqywemckd sqlefkrvsa ttqccwgiac dnqvyvyvca
       61 sdvpirrree ayenqrwnpm ggfcekllls drwgwsdvsg lqhrpldrva lpsphwewes
      121 dwyvdenfgg eptekggwty aidfpatytk dkkwnscvrr rkwiryrryk srdiwakips
      181 kddpkelpdp fndlsvggwe iteepvgrls vwavslqgkv wyredvshsn pegsswslld
      241 tpgevvqisc gphdllwatl wegqalvreg inrsnpkgss wsiveppgse ngvmhisvgv
      301 svvwavtkdw kvwfrrgvns hnpcgtswie mvgemtmvnv gmndqvwgig cedravyfrq
      361 gvtpselsgk twkaiiaare cdrshsgsss sllsagcffg devrgsgesa psdtdassev
      421 erpgpgqilp aeplddskna tgnsasglga grtaedtved acpaegsrea rpnthpgpap
      481 tpaelpwtni dlkeakkvps hsaagfpett slsslgllpl gleepygvdd hplwawvsgg
      541 gcvveacamp rwftvqagls ssvhmlslsi tpaqtaawrk qifqqltert krelenfrhy
      601 eqaveqsvwv ktgalqwwcd wkphkwvdvr laleqftghd gvrdsilfiy yvvheekkyi
      661 hiflnevval vpvlnetkhs falytpertr qrwpvrlaaa teqdmndwla llslsccesr
      721 kvqgrpspqa iwsitckgdi fvsepspdle ahehplpcdq mfwrqmgghl rmveansrgv
      781 vwgigydhta wvytggyggg cfqglassts niytqsdvkc vhiyenqrwn pvtgytsrgl
      841 ptdrymwsda sglqectkag tkppslqwaw vsdwfvdfsv pggtdqegwq yasdfpasyh
      901 gsktmkdfvr rrcwarkckl vtsgpwlevp pialrdvsii pespgaegsg hsialwavsd
      961 kgdvlcrlgv selnpagssw lhvgtdqpfa sisigacyqv wavardgsaf yrgsvypsqp
     1021 agdcwyhips pprqrlkqvs agqtsvyald engnlwyrqg itpsypqgss wehvsnnvcr
     1081 vsvgpldqvw viankvqgsh slsrgtvchr tgvqphepkg hgwdygiggg wdhisvrana
     1141 traprsssqe qepsappeah gpvcc
//
LOCUS       NP_065910               1996 aa            linear   PRI 20-NOV-2025
DEFINITION  protein Shroom3 [Homo sapiens].
ACCESSION   NP_065910
VERSION     NP_065910.3
DBSOURCE    REFSEQ: accession NM_020859.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1996)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1996)
  AUTHORS   Deshwar,A.R., Martin,N., Shannon,P. and Chitayat,D.
  TITLE     A homozygous pathogenic variant in SHROOM3 associated with
            anencephaly and cleft lip and palate
  JOURNAL   Clin Genet 98 (3), 299-302 (2020)
   PUBMED   32621286
  REMARK    GeneRIF: A homozygous pathogenic variant in SHROOM3 associated with
            anencephaly and cleft lip and palate.
REFERENCE   3  (residues 1 to 1996)
  AUTHORS   Corredor,Z., da Silva Filho,M.I., Rodriguez-Ribera,L., Catalano,C.,
            Hemminki,K., Coll,E., Silva,I., Diaz,J.M., Ballarin,J.A.,
            Henandez,A., Forsti,A., Marcos,R. and Pastor,S.
  TITLE     Loci associated with genomic damage levels in chronic kidney
            disease patients and controls
  JOURNAL   Mutat Res Genet Toxicol Environ Mutagen 852, 503167 (2020)
   PUBMED   32265040
  REMARK    GeneRIF: The three genes associated with chronic kidney disease
            (AGT, GLO1, and SHROOM3) showed associations with both the high
            levels of oxidatively damaged DNA and genomic instability.
REFERENCE   4  (residues 1 to 1996)
  AUTHORS   Wei,C., Banu,K., Garzon,F., Basgen,J.M., Philippe,N., Yi,Z.,
            Liu,R., Choudhuri,J., Fribourg,M., Liu,T., Cumpelik,A., Wong,J.,
            Khan,M., Das,B., Keung,K., Salem,F., Campbell,K.N., Kaufman,L.,
            Cravedi,P., Zhang,W., O'Connell,P.J., He,J.C., Murphy,B. and
            Menon,M.C.
  TITLE     SHROOM3-FYN Interaction Regulates Nephrin Phosphorylation and
            Affects Albuminuria in Allografts
  JOURNAL   J Am Soc Nephrol 29 (11), 2641-2657 (2018)
   PUBMED   30341149
  REMARK    GeneRIF: We confirmed the interaction of endogenous SHROOM3 with
            FYN in podocytes via a critical Src homology 3-binding domain,
            distinct from its ROCK-binding domain. Shroom3-Fyn interaction was
            required in vitro and in vivo for activation of Fyn kinase and
            downstream nephrin phosphorylation in podocytes.
REFERENCE   5  (residues 1 to 1996)
  AUTHORS   Prokop,J.W., Yeo,N.C., Ottmann,C., Chhetri,S.B., Florus,K.L.,
            Ross,E.J., Sosonkina,N., Link,B.A., Freedman,B.I., Coppola,C.J.,
            McDermott-Roe,C., Leysen,S., Milroy,L.G., Meijer,F.A., Geurts,A.M.,
            Rauscher,F.J. 3rd, Ramaker,R., Flister,M.J., Jacob,H.J.,
            Mendenhall,E.M. and Lazar,J.
  TITLE     Characterization of Coding/Noncoding Variants for SHROOM3 in
            Patients with CKD
  JOURNAL   J Am Soc Nephrol 29 (5), 1525-1535 (2018)
   PUBMED   29476007
  REMARK    GeneRIF: We determined that coding variant P1244L attenuates the
            interaction of SHROOM3 with 14-3-3, suggesting alterations to the
            Hippo pathway, a known mediator of CKD.
REFERENCE   6  (residues 1 to 1996)
  AUTHORS   Rothenberg,M.E., Spergel,J.M., Sherrill,J.D., Annaiah,K.,
            Martin,L.J., Cianferoni,A., Gober,L., Kim,C., Glessner,J.,
            Frackelton,E., Thomas,K., Blanchard,C., Liacouras,C., Verma,R.,
            Aceves,S., Collins,M.H., Brown-Whitehorn,T., Putnam,P.E.,
            Franciosi,J.P., Chiavacci,R.M., Grant,S.F., Abonia,J.P.,
            Sleiman,P.M. and Hakonarson,H.
  TITLE     Common variants at 5q22 associate with pediatric eosinophilic
            esophagitis
  JOURNAL   Nat Genet 42 (4), 289-291 (2010)
   PUBMED   20208534
REFERENCE   7  (residues 1 to 1996)
  AUTHORS   Kottgen,A., Glazer,N.L., Dehghan,A., Hwang,S.J., Katz,R., Li,M.,
            Yang,Q., Gudnason,V., Launer,L.J., Harris,T.B., Smith,A.V.,
            Arking,D.E., Astor,B.C., Boerwinkle,E., Ehret,G.B., Ruczinski,I.,
            Scharpf,R.B., Chen,Y.D., de Boer,I.H., Haritunians,T., Lumley,T.,
            Sarnak,M., Siscovick,D., Benjamin,E.J., Levy,D., Upadhyay,A.,
            Aulchenko,Y.S., Hofman,A., Rivadeneira,F., Uitterlinden,A.G., van
            Duijn,C.M., Chasman,D.I., Pare,G., Ridker,P.M., Kao,W.H.,
            Witteman,J.C., Coresh,J., Shlipak,M.G. and Fox,C.S.
  TITLE     Multiple loci associated with indices of renal function and chronic
            kidney disease
  JOURNAL   Nat Genet 41 (6), 712-717 (2009)
   PUBMED   19430482
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1996)
  AUTHORS   Hagens,O., Ballabio,A., Kalscheuer,V., Kraehenbuhl,J.P.,
            Schiaffino,M.V., Smith,P., Staub,O., Hildebrand,J. and
            Wallingford,J.B.
  TITLE     A new standard nomenclature for proteins related to Apx and Shroom
  JOURNAL   BMC Cell Biol 7, 18 (2006)
   PUBMED   16615870
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1996)
  AUTHORS   Navarro-Lerida,I., Martinez Moreno,M., Roncal,F., Gavilanes,F.,
            Albar,J.P. and Rodriguez-Crespo,I.
  TITLE     Proteomic identification of brain proteins that interact with
            dynein light chain LC8
  JOURNAL   Proteomics 4 (2), 339-346 (2004)
   PUBMED   14760703
REFERENCE   10 (residues 1 to 1996)
  AUTHORS   Hildebrand,J.D. and Soriano,P.
  TITLE     Shroom, a PDZ domain-containing actin-binding protein, is required
            for neural tube morphogenesis in mice
  JOURNAL   Cell 99 (5), 485-497 (1999)
   PUBMED   10589677
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB055660.1, AK127929.1,
            AC107072.3, AK128677.1 and AW025141.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 17, 2008 this sequence version replaced NP_065910.2.
            
            Summary: This gene encodes a PDZ-domain-containing protein that
            belongs to a family of Shroom-related proteins. This protein may be
            involved in regulating cell shape in certain tissues. A similar
            protein in mice is required for proper neurulation. [provided by
            RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB055660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2163459
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296043.7/ ENSP00000296043.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1996
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.1"
     Protein         1..1996
                     /product="protein Shroom3"
                     /note="F-actin-binding protein; shroom-related protein"
                     /calculated_mol_wt=216727
     Region          27..108
                     /region_name="PDZ_shroom2_3_4-like"
                     /note="PDZ domain of shroom2, shroom3, shroom4, and
                     related domains; cd06750"
                     /db_xref="CDD:467232"
     Site            order(37..43,55,58,88,92,95..96)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467232"
     Region          150..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXN0; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          340..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          437..468
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          568..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          673..772
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          788..1053
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          884..1066
                     /region_name="ASD1"
                     /note="Apx/Shroom domain ASD1; pfam08688"
                     /db_xref="CDD:462562"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          <959..1521
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXN0; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            1072
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QXN0; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          1093..1115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          1137..1223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            1221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          1315..1573
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Site            1441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          1627..1665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF72.2)"
     Region          1670..1956
                     /region_name="ASD2"
                     /note="Apx/Shroom domain ASD2; pfam08687"
                     /db_xref="CDD:462561"
     CDS             1..1996
                     /gene="SHROOM3"
                     /gene_synonym="APXL3; MSTP013; SHRM; ShrmL"
                     /coded_by="NM_020859.4:825..6815"
                     /db_xref="CCDS:CCDS3579.2"
                     /db_xref="GeneID:57619"
                     /db_xref="HGNC:HGNC:30422"
                     /db_xref="MIM:604570"
ORIGIN      
        1 mmrttedfhk psatlnsnta tkgryiylea fleggapwgf tlkgglehge pliiskveeg
       61 gkadtlsskl qagdevvhin evtlsssrke avslvkgsyk tlrlvvrrdv ctdpghadtg
      121 asnfvspehl tsgpqhrkaa wsggvklrlk hrrsepagrp hswhttksge kqpdasmmqi
      181 sqgmigppwh qsyhssssts dlsnydhayl rrspdqcssq gsmeslepsg ayppchlspa
      241 kstgsidqls hfhnkrdsay ssfstsssil eyphpgisgr ersgsmdnts arggllegmr
      301 qadiryvktv ydtrrgvsae yevnssalll qgrearasan gqgydkwsni prgkgvppps
      361 wsqqcpssle tatdnlppkv gaplpparsd syaafrhrer psswssldqk rlcrpqansl
      421 gslkspfiee qlhtvleksp ensppvkpkh nytqkaqpgq pllptsiypv pslephfaqv
      481 pqpsvssngm lypalakesg yiapqgacnk matidengnq ngsgrpgfaf cqplehdlls
      541 pvekkpeata kyvpskvhfc svpeneedas lkrhltppqg nsphsnerks thsnkpsshp
      601 hslkcpqaqa wqagedkrss rlsepwegdf qedhnanlwr rlereglgqs lsgnfgktks
      661 afsslqnipe slrrhsslel grgtqegypg grptcavntk aedpgrkaap dlgshldrqv
      721 syprpegrtg asasfnstdp speeppapsh phtsslgrrg pgpgsasalq gfqygkphcs
      781 vlekvskfeq reqgsqrpsv ggsgfghnyr phrtvstsst sgndfeetka hirfsesaep
      841 lgngeqhfkn gelkleeasr qpcgqqlsgg asdsgrgpqr pdarllrsqs tfqlsseper
      901 epewrdrpgs pesplldapf srayrnsikd aqsrvlgats frrrdlelga pvasrswrpr
      961 pssahvglrs peasasasph tprerhsvtp aegdlarpvp paarrgarrr ltpeqkkrsy
     1021 sepekmnevg iveeaepapl gpqrngmrfp essvadrrrl ferdgkacst lslsgpelkq
     1081 fqqsaladyi qrktgkrpts aagcslqepg plreraqsay lqpgpaaleg sglasassls
     1141 slrepslqpr reatllpatv aetqqaprdr sssfaggrrl gerrrgdlls ganggtrgtq
     1201 rgdetpreps swgaragksm saedllersd vlagpvhvrs rsspatadkr qdvllgqdsg
     1261 fglvkdpcyl agpgsrslsc sergqeemlp lfhhltprwg gsgckaigds svpsecpgtl
     1321 dhqrqasrtp cprpplagtq glvtdtraap ltpigtplps aipsgycsqd gqtgrqplpp
     1381 ytpammhrsn ghtltqppgp rgcegdgpeh gveegtrkrv slpqwpppsr akwahaared
     1441 slpeessapd fanlkhyqkq qslpslcsts dpdtplgaps tpgrislris esvlrdsppp
     1501 hedyedevfv rdphpkatss ptfeplpppp ppppsqetpv ysmddfpppp phtvceaqld
     1561 sedpegprps fnklskvtia rerhmpgaah vvgsqtlasr lqtsikgsea estppsfmsv
     1621 haqlagslgg qpapiqtqsl shdpvsgtqg lekkvspdpq kssedirtea lakeivhqdk
     1681 sladildpds rlkttmdlme glfprdvnll kensvkrkai qrtvsssgce gkrnedkeav
     1741 smlvncpayy svsapkaell nkikempaev neeeeqadvn ekkaeligsl thkletlqea
     1801 kgslltdikl nnalgeevea liselckpne fdkyrmfigd ldkvvnllls lsgrlarven
     1861 vlsglgedas neersslyek rkilagqhed arelkenldr rervvlgila nylseeqlqd
     1921 yqhfvkmkst llieqrkldd kiklgqeqvk clleslpsdf ipkagalalp pnltsepipa
     1981 ggctfsgifp tltspl
//
LOCUS       NP_001034612             482 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholine receptor subunit alpha isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001034612
VERSION     NP_001034612.1
DBSOURCE    REFSEQ: accession NM_001039523.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Rodriguez Cruz,P.M., Ravenscroft,G., Natera,D., Carr,A., Manzur,A.,
            Liu,W.W., Vella,N.R., Jerico,I., Gonzalez-Quereda,L., Gallano,P.,
            Montalto,S.A., Davis,M.R., Lamont,P.J., Laing,N.G., Bourque,P.,
            Nascimento,A., Muntoni,F., Polavarapu,K., Lochmuller,H., Palace,J.
            and Beeson,D.
  TITLE     A novel phenotype of AChR-deficiency syndrome with predominant
            facial and distal weakness resulting from the inclusion of an
            evolutionary alternatively-spliced exon in CHRNA1
  JOURNAL   Neuromuscul Disord 33 (2), 161-168 (2023)
   PUBMED   36634413
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Lin,J.B., Kang,M.Q., Huang,L.P., Zhuo,Y., Li,X. and Lai,F.C.
  TITLE     CHRNA1 promotes the pathogenesis of primary focal hyperhidrosis
  JOURNAL   Mol Cell Neurosci 111, 103598 (2021)
   PUBMED   33476802
  REMARK    GeneRIF: CHRNA1 promotes the pathogenesis of primary focal
            hyperhidrosis.
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Kudryavtsev,D., Isaeva,A., Barkova,D., Spirova,E., Mukhutdinova,R.,
            Kasheverov,I. and Tsetlin,V.
  TITLE     Point Mutations of Nicotinic Receptor alpha1 Subunit Reveal New
            Molecular Features of G153S Slow-Channel Myasthenia
  JOURNAL   Molecules 26 (5), 1278 (2021)
   PUBMED   33652901
  REMARK    GeneRIF: Point Mutations of Nicotinic Receptor alpha1 Subunit
            Reveal New Molecular Features of G153S Slow-Channel Myasthenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Uzawa,A., Ozawa,Y., Yasuda,M., Oda,F., Kojima,Y., Kawaguchi,N.,
            Kanai,T., Himuro,K. and Kuwabara,S.
  TITLE     Increased serum acetylcholine receptor alpha1 subunit protein in
            anti-acetylcholine receptor antibody-positive myasthenia gravis
  JOURNAL   J Neuroimmunol 339, 577125 (2020)
   PUBMED   31855720
  REMARK    GeneRIF: Serum AChR alpha1 subunit protein concentrations were
            higher in patients with ant-AChR antibody-positive myasthenia
            gravis than those in controls.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Wang,M., Liu,D., Schwender,H., Wang,H., Wang,P., Zhou,Z., Li,J.,
            Wu,T., Zhu,H. and Beaty,T.H.
  TITLE     Evaluating the effect of nicotinic cholinergic receptor genes on
            the risk of nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Oral Dis 24 (6), 1068-1072 (2018)
   PUBMED   29688589
  REMARK    GeneRIF: In our analysis, we found one pair of SNPs in CHRNA1 and
            CHRNA7, plus one pair of SNPs in CHRNA2 and CHRNA3 reached
            corrected significance in tests for GxG interaction. Our study
            suggested evidence of interactions between CHRNs in controlling the
            risk of NSCL/P.
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Yu,X.M. and Hall,Z.W.
  TITLE     Extracellular domains mediating epsilon subunit interactions of
            muscle acetylcholine receptor
  JOURNAL   Nature 352 (6330), 64-67 (1991)
   PUBMED   1712080
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Beeson,D., Jeremiah,S., West,L.F., Povey,S. and Newsom-Davis,J.
  TITLE     Assignment of the human nicotinic acetylcholine receptor genes: the
            alpha and delta subunit genes to chromosome 2 and the beta subunit
            gene to chromosome 17
  JOURNAL   Ann Hum Genet 54 (3), 199-208 (1990)
   PUBMED   2221824
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Beeson,D., Morris,A., Vincent,A. and Newsom-Davis,J.
  TITLE     The human muscle nicotinic acetylcholine receptor alpha-subunit
            exist as two isoforms: a novel exon
  JOURNAL   EMBO J 9 (7), 2101-2106 (1990)
   PUBMED   1694127
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Hohlfeld,R., Toyka,K.V., Miner,L.L., Walgrave,S.L. and
            Conti-Tronconi,B.M.
  TITLE     Amphipathic segment of the nicotinic receptor alpha subunit
            contains epitopes recognized by T lymphocytes in myasthenia gravis
  JOURNAL   J Clin Invest 81 (3), 657-660 (1988)
   PUBMED   2449458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315312.1, CD013889.1 and
            BC043196.2.
            
            Summary: The muscle acetylcholine receptor consiststs of 5 subunits
            of 4 different types: 2 alpha subunits and 1 each of the beta,
            gamma, and delta subunits. This gene encodes an alpha subunit that
            plays a role in acetlycholine binding/channel gating. Alternatively
            spliced transcript variants encoding different isoforms have been
            identified. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.102475.1, AK299445.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162946, SAMN03267754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..482
                     /product="acetylcholine receptor subunit alpha isoform a
                     precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     1 (muscle); cholinergic receptor, nicotinic alpha 1;
                     nicotinic cholinergic receptor alpha 1; acetylcholine
                     receptor subunit alpha; nicotinic acetylcholine receptor
                     alpha subunit; muscle nicotinic acetylcholine receptor;
                     acetylcholine receptor, nicotinic, alpha 1 (muscle);
                     cholinergic receptor, nicotinic, alpha 1 (muscle)"
                     /calculated_mol_wt=52404
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2160
     mat_peptide     21..482
                     /product="acetylcholine receptor subunit alpha isoform a"
                     /calculated_mol_wt=52404
     Region          22..256
                     /region_name="LGIC_ECD_nAChR_A1"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit alpha 1 (CHRNA1); cd19014"
                     /db_xref="CDD:349815"
     Site            order(59,61,67..68,75,122,124,133..134,136,138..139,143,
                     145..146,150..152,154,164,166,168,172,194,255)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349815"
     Region          173..187
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349815"
     Region          263..471
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     CDS             1..482
                     /gene="CHRNA1"
                     /gene_synonym="ACHRA; ACHRD; CHRNA; CMS1A; CMS1B; CMS2A;
                     FCCMS; SCCMS"
                     /coded_by="NM_001039523.3:79..1527"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33331.1"
                     /db_xref="GeneID:1134"
                     /db_xref="HGNC:HGNC:1955"
                     /db_xref="MIM:100690"
ORIGIN      
        1 mepwpllllf slcsaglvlg sehetrlvak lfkdyssvvr pvedhrqvve vtvglqliql
       61 invdevnqiv ttnvrlkqgd mvdlprpscv tlgvplfshl qneqwvdynl kwnpddyggv
      121 kkihipseki wrpdlvlynn adgdfaivkf tkvllqytgh itwtppaifk syceiivthf
      181 pfdeqncsmk lgtwtydgsv vainpesdqp dlsnfmesge wvikesrgwk hsvtysccpd
      241 tpyldityhf vmqrlplyfi vnviipcllf sfltglvfyl ptdsgekmtl sisvllsltv
      301 fllvivelip stssavplig kymlftmvfv iasiiitviv inthhrspst hvmpnwvrkv
      361 fidtipnimf fstmkrpsre kqdkkifted idisdisgkp gpppmgfhsp likhpevksa
      421 iegikyiaet mksdqesnna aaewkyvamv mdhillgvfm lvciigtlav fagrlielnq
      481 qg
//
LOCUS       NP_085148                393 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3 domain-binding protein 5-like isoform 1 [Homo sapiens].
ACCESSION   NP_085148
VERSION     NP_085148.1
DBSOURCE    REFSEQ: accession NM_030645.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Jenkins,M.L., Margaria,J.P., Stariha,J.T.B., Hoffmann,R.M.,
            McPhail,J.A., Hamelin,D.J., Boulanger,M.J., Hirsch,E. and
            Burke,J.E.
  TITLE     Structural determinants of Rab11 activation by the guanine
            nucleotide exchange factor SH3BP5
  JOURNAL   Nat Commun 9 (1), 3772 (2018)
   PUBMED   30217979
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK056382.1 and AL136569.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056382.1, AK125138.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157511 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366472.6/ ENSP00000355428.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..393
                     /product="SH3 domain-binding protein 5-like isoform 1"
                     /note="SH3 domain-binding protein 5-like; SH3BP-5-like"
                     /calculated_mol_wt=43368
     Region          1..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99LH9; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Region          54..283
                     /region_name="SH3BP5"
                     /note="SH3 domain-binding protein 5 (SH3BP5); pfam05276"
                     /db_xref="CDD:461608"
     Region          273..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Region          362..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7L8J4.1)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99LH9; propagated from
                     UniProtKB/Swiss-Prot (Q7L8J4.1)"
     CDS             1..393
                     /gene="SH3BP5L"
                     /coded_by="NM_030645.3:513..1694"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31126.1"
                     /db_xref="GeneID:80851"
                     /db_xref="HGNC:HGNC:29360"
                     /db_xref="MIM:620652"
ORIGIN      
        1 maelrqvpgg retpqgelrp evvedevprs pvaeepgggg sssseaklsp reeeeldpri
       61 qeelehlnqa seeinqvelq ldearttyrr ilqesarkln tqgshlgsci ekarpyyear
      121 rlakeaqqet qkaalryera vsmhnaarem vfvaeqgvma dknrldptwq emlnhatckv
      181 neaeeerlrg erehqrvtrl cqqaearvqa lqktlrraig ksrpyfelka qfsqileehk
      241 akvteleqqv aqaktrysva lrnleqiseq iharrrgglp phplgprrss pvgaeagped
      301 medgdsgieg aegagleegs slgpgpapdt dtlsllslrt vasdlqkcds vehlrglsdh
      361 vsldgqelgt rsggrrgsdg garggrhqrs vsl
//
LOCUS       NP_001355930             288 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform h [Homo sapiens].
ACCESSION   NP_001355930 XP_024303348
VERSION     NP_001355930.1
DBSOURCE    REFSEQ: accession NM_001369001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303348.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.179317.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..288
                     /product="aprataxin isoform h"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=32994
     Region          3..>44
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Region          110..211
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(204,206,208..210)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            206
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          229..288
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..288
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369001.1:103..969"
                     /note="isoform h is encoded by transcript variant 22"
                     /db_xref="CCDS:CCDS75827.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqefeeea knpglethrk
       61 rkrsgnsdsi erdaaqeaea gtglepgsns gqcsvplkkg kdapikkesl ghwsqglkis
      121 mqdpkmqvyk deqvvvikdk ypkaryhwlv lpwtsisslk avarehlell khmhtvgekv
      181 ivdfagsskl rfrlgyhaip smshvhlhvi sqdfdspclk nkkhwnsfnt eyflesqavi
      241 emvqeagrvt vrdgmpellk lplrchecqq llpsipqlke hlrkhwtq
//
LOCUS       NP_076960                118 aa            linear   PRI 20-NOV-2025
DEFINITION  proton-coupled zinc antiporter SLC30A5 isoform 2 [Homo sapiens].
ACCESSION   NP_076960
VERSION     NP_076960.1
DBSOURCE    REFSEQ: accession NM_024055.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Wagatsuma,T., Shimotsuma,K., Sogo,A., Sato,R., Kubo,N., Ueda,S.,
            Uchida,Y., Kinoshita,M. and Kambe,T.
  TITLE     Zinc transport via ZNT5-6 and ZNT7 is critical for cell surface
            glycosylphosphatidylinositol-anchored protein expression
  JOURNAL   J Biol Chem 298 (6), 102011 (2022)
   PUBMED   35525268
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 118)
  AUTHORS   Lieberwirth,J.K., Joset,P., Heinze,A., Hentschel,J., Stein,A.,
            Iannaccone,A., Steindl,K., Kuechler,A. and Abou Jamra,R.
  TITLE     Bi-allelic loss of function variants in SLC30A5 as cause of
            perinatal lethal cardiomyopathy
  JOURNAL   Eur J Hum Genet 29 (5), 808-815 (2021)
   PUBMED   33547425
  REMARK    GeneRIF: Bi-allelic loss of function variants in SLC30A5 as cause
            of perinatal lethal cardiomyopathy.
            Erratum:[Eur J Hum Genet. 2021 May;29(5):887. doi:
            10.1038/s41431-021-00843-8. PMID: 33750920]
REFERENCE   5  (residues 1 to 118)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   6  (residues 1 to 118)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   7  (residues 1 to 118)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Matsuura,W., Kohda,A.,
            Okumura,K., Nagao,M., Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Zinc transporters, ZnT5 and ZnT7, are required for the activation
            of alkaline phosphatases, zinc-requiring enzymes that are
            glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
  JOURNAL   J Biol Chem 280 (1), 637-643 (2005)
   PUBMED   15525635
REFERENCE   8  (residues 1 to 118)
  AUTHORS   Devergnas,S., Chimienti,F., Naud,N., Pennequin,A., Coquerel,Y.,
            Chantegrel,J., Favier,A. and Seve,M.
  TITLE     Differential regulation of zinc efflux transporters ZnT-1, ZnT-5
            and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
  JOURNAL   Biochem Pharmacol 68 (4), 699-709 (2004)
   PUBMED   15276077
REFERENCE   9  (residues 1 to 118)
  AUTHORS   Cragg,R.A., Christie,G.R., Phillips,S.R., Russi,R.M., Kury,S.,
            Mathers,J.C., Taylor,P.M. and Ford,D.
  TITLE     A novel zinc-regulated human zinc transporter, hZTL1, is localized
            to the enterocyte apical membrane
  JOURNAL   J Biol Chem 277 (25), 22789-22797 (2002)
   PUBMED   11937503
  REMARK    GeneRIF: A novel zinc-regulated human zinc transporter, hZTL1, is
            localized to the enterocyte apical membrane
REFERENCE   10 (residues 1 to 118)
  AUTHORS   Kambe,T., Narita,H., Yamaguchi-Iwai,Y., Hirose,J., Amano,T.,
            Sugiura,N., Sasaki,R., Mori,K., Iwanaga,T. and Nagao,M.
  TITLE     Cloning and characterization of a novel mammalian zinc transporter,
            zinc transporter 5, abundantly expressed in pancreatic beta cells
  JOURNAL   J Biol Chem 277 (21), 19049-19055 (2002)
   PUBMED   11904301
  REMARK    GeneRIF: cloning and characterization of ZnT-5 which is expressed
            in pancreatic beta cells
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB090660.1 and BC017441.1.
            
            Summary: This gene encodes a member of the SLC30A/ZnT family of
            zinc transporter proteins. ZnT proteins mediate both cellular zinc
            efflux and zinc sequestration into membrane-bound organelles. The
            encoded protein plays a role in the early secretory pathway as a
            heterodimer with zinc transporter 6, and may also regulate zinc
            sequestration into secretory granules of pancreatic beta cells.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the long arm of chromosome 19. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            lacks a large portion of the coding region, compared to variant 1.
            The encoded isoform (2) is significantly shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017441.1, SRR1163655.77850.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.1-q13.2"
     Protein         1..118
                     /product="proton-coupled zinc antiporter SLC30A5 isoform
                     2"
                     /note="zinc transporter ZTL1; znT-like transporter 1;
                     solute carrier family 30 (zinc transporter), member 5;
                     proton-coupled zinc antiporter SLC30A5"
                     /calculated_mol_wt=12813
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8TAD4.1)"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAD4.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAD4.1)"
     CDS             1..118
                     /gene="SLC30A5"
                     /gene_synonym="ZnT-5; ZNT5; ZNTL1; ZTL1"
                     /coded_by="NM_024055.5:243..599"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34173.1"
                     /db_xref="GeneID:64924"
                     /db_xref="HGNC:HGNC:19089"
                     /db_xref="MIM:607819"
ORIGIN      
        1 meekyggdvl agpggggglg pvdvpsarlt kyivllcftk flkavglfes ydllkavhiv
       61 qfifilklgt affmvlfqkp fssgktitkh qiigslkipg rkefkdkkln dprklvgn
//
LOCUS       NP_001354451             571 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 15 [Homo sapiens].
ACCESSION   NP_001354451 XP_016872214
VERSION     NP_001354451.1
DBSOURCE    REFSEQ: accession NM_001367522.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872214.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.227357.1,
                                           SRR1803614.265811.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..571
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 15"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63369
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          412..>467
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..571
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367522.1:95..1810"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mepqttvvhn atdgikgste
      361 scnttteded lkaaplrtgn gssvpegrss rdrtapsagm qpqpslcssa mrkqeiikit
      421 eqlieainng dfeaytkicd pgltsfepea lgnlvegmdf hkfyfenrew vraadillpa
      481 plplclclll tfssqlptfp lfdlraalll cmlvplcpdg crqaplkall lsskchsfcs
      541 cfvavpvtti kltyflpgav ayacnpntlg g
//
LOCUS       NP_001353524             918 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 24 [Homo
            sapiens].
ACCESSION   NP_001353524 XP_005245774
VERSION     NP_001353524.1
DBSOURCE    REFSEQ: accession NM_001366595.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 918)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 918)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 918)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 918)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 918)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 918)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 918)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 918)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 918)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 918)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14, KU178513.1 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_005245774.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.265693.1,
                                           SRR1803614.36103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..918
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..918
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 24"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=103850
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            452
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            478
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <620..>754
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            811
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            888
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..918
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366595.1:26..2782"
                     /note="isoform 24 is encoded by transcript variant 42"
                     /db_xref="CCDS:CCDS90884.1"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsgkvt khkgtekres pspapkprkv elseseedkg gkmaaadsvq
      481 qrrqyrrqnq qsssdsgsss ssederpkrs hvkngevgrr rrhspsrsas psprkrqket
      541 sprmqmgkrw qspvtksgrr rrspsppptr rrrspspapp prrrrtptpp prrrtpsppp
      601 rrrspsprry sppiqrrysp spppkrrtas pppppkrras pspppkrrvs hspppkqrss
      661 pvtkrrspsl sskhrkgssp srstrearsp qpnkrhspsp rprapqtsss pppvrrgass
      721 spqrrqspsp strpirrvsr tpepkkikka aspspqsvrr vsssrsvsgs pepaakkppa
      781 ppspvqsqsp stnwspavpv kkaksptpsp spprnsdqeg ggkkkkkkkd kkhkkdkkhk
      841 khkkhkkeka vaaaaaaavt paaiaaattt laqeepvaap epkketesea ednlddlekh
      901 lrekalrsmr kaqvspqs
//
LOCUS       NP_001356019             360 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001356019 XP_011538143
VERSION     NP_001356019.1
DBSOURCE    REFSEQ: accession NM_001369090.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_011538143.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.204542.1,
                                           SRR7346977.1051767.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..360
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 6"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40919
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..360
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369090.1:104..1186"
                     /note="isoform 6 is encoded by transcript variant 11"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitvv
//
LOCUS       NP_659438                166 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 32A isoform 2 [Homo sapiens].
ACCESSION   NP_659438
VERSION     NP_659438.1
DBSOURCE    REFSEQ: accession NM_145001.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Takamitsu,E., Fukunaga,K., Iio,Y., Moriya,K. and Utsumi,T.
  TITLE     Cell-free identification of novel N-myristoylated proteins from
            complementary DNA resources using bioorthogonal myristic acid
            analogues
  JOURNAL   Anal Biochem 464, 83-93 (2014)
   PUBMED   25043870
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Koskinen,L.L., Einarsdottir,E., Korponay-Szabo,I.R., Kurppa,K.,
            Kaukinen,K., Sistonen,P., Pocsai,Z., Szeles,G., Adany,R., Maki,M.,
            Kere,J. and Saavalainen,P.
  TITLE     Fine mapping of the CELIAC2 locus on chromosome 5q31-q33 in the
            Finnish and Hungarian populations
  JOURNAL   Tissue Antigens 74 (5), 408-416 (2009)
   PUBMED   19845895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011338.8 and AC009189.6.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 3. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021666.1, BU156055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..166
                     /product="serine/threonine-protein kinase 32A isoform 2"
                     /EC_number="2.7.11.1"
                     /note="A930015B13Rik; serine/threonine-protein kinase 32A;
                     yet another novel kinase 1; CTB-108O6.2"
                     /calculated_mol_wt=19661
     Region          22..>157
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(29..32,35,37,50,52,84,100..103,146,150..151,153)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270730"
     CDS             1..166
                     /gene="STK32A"
                     /gene_synonym="YANK1"
                     /coded_by="NM_145001.4:271..771"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54931.1"
                     /db_xref="GeneID:202374"
                     /db_xref="HGNC:HGNC:28317"
                     /db_xref="MIM:621310"
ORIGIN      
        1 mgantsrkpp vfdenedvnf dhfeilraig kgsfgkvciv qkndtkkmya mkymnkqkcv
       61 ernevrnvfk elqimqgleh pflvnlwysf qdeedmfmvv dlllggdlry hlqqnvhfke
      121 etvklficel vmaldylqnq riihrdmkpd nilldehdtw lsyksh
//
LOCUS       NP_066951                 67 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC5 [Homo
            sapiens].
ACCESSION   NP_066951
VERSION     NP_066951.1
DBSOURCE    REFSEQ: accession NM_021128.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 67)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 67)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 67)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   4  (residues 1 to 67)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 67)
  AUTHORS   Acker,J., Murroni,O., Mattei,M.G., Kedinger,C. and Vigneron,M.
  TITLE     The gene (POLR2L) encoding the hRPB7.6 subunit of human RNA
            polymerase
  JOURNAL   Genomics 32 (1), 86-90 (1996)
   PUBMED   8786124
REFERENCE   6  (residues 1 to 67)
  AUTHORS   McKune,K., Moore,P.A., Hull,M.W. and Woychik,N.A.
  TITLE     Six human RNA polymerase subunits functionally substitute for their
            yeast counterparts
  JOURNAL   Mol Cell Biol 15 (12), 6895-6900 (1995)
   PUBMED   8524256
REFERENCE   7  (residues 1 to 67)
  AUTHORS   Shpakovski,G.V., Acker,J., Wintzerith,M., Lacroix,J.F., Thuriaux,P.
            and Vigneron,M.
  TITLE     Four subunits that are shared by the three classes of RNA
            polymerase are functionally interchangeable between Homo sapiens
            and Saccharomyces cerevisiae
  JOURNAL   Mol Cell Biol 15 (9), 4702-4710 (1995)
   PUBMED   7651387
REFERENCE   8  (residues 1 to 67)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   9  (residues 1 to 67)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   10 (residues 1 to 67)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005903.1, BC018649.2,
            BQ435190.1 and BU679804.1.
            
            Summary: This gene encodes a subunit of RNA polymerase II, the
            polymerase responsible for synthesizing messenger RNA in
            eukaryotes. The product of this gene contains four conserved
            cysteines characteristic of an atypical zinc-binding domain. Like
            its counterpart in yeast, this subunit may be shared by the other
            two DNA-directed RNA polymerases. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.295353.1,
                                           SRR5189667.157673.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322028.5/ ENSP00000324124.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..67
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..67
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC5"
                     /EC_number="2.7.7.6"
                     /note="RPB10 homolog; RNA polymerase II 7.6 kDa subunit;
                     RNA polymerase II subunit L; polymerase (RNA) II subunit
                     L; DNA-directed RNA polymerase III subunit L; RNA
                     polymerases I, II, and III subunit ABC5; polymerase (RNA)
                     II (DNA directed) polypeptide L, 7.6kDa"
                     /calculated_mol_wt=7514
     Region          1..67
                     /region_name="PLN00032"
                     /note="DNA-directed RNA polymerase; Provisional"
                     /db_xref="CDD:215034"
     CDS             1..67
                     /gene="POLR2L"
                     /gene_synonym="hRPB7.6; RBP10; RPABC5; RPB10; RPB10beta;
                     RPB7.6"
                     /coded_by="NM_021128.5:22..225"
                     /db_xref="CCDS:CCDS7720.1"
                     /db_xref="GeneID:5441"
                     /db_xref="HGNC:HGNC:9199"
                     /db_xref="MIM:601189"
ORIGIN      
        1 miipvrcftc gkivgnkwea ylgllqaeyt egdaldalgl kryccrrmll ahvdliekll
       61 nyaplek
//
LOCUS       NP_001244905             797 aa            linear   PRI 20-NOV-2025
DEFINITION  cip1-interacting zinc finger protein isoform 6 [Homo sapiens].
ACCESSION   NP_001244905
VERSION     NP_001244905.1
DBSOURCE    REFSEQ: accession NM_001257976.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 797)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 797)
  AUTHORS   Chen,Y.R., Wu,Y.S., Wang,W.S., Zhang,J.S. and Wu,Q.G.
  TITLE     Upregulation of lncRNA DANCR functions as an oncogenic role in
            non-small lung cancer by regulating miR-214-5p/CIZ1 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2539-2547 (2020)
   PUBMED   32196604
  REMARK    GeneRIF: Upregulation of lncRNA DANCR functions as an oncogenic
            role in non-small lung cancer by regulating miR-214-5p/CIZ1 axis.
REFERENCE   5  (residues 1 to 797)
  AUTHORS   Chen,X., Wang,P., Wang,S., Li,J., Ou,T. and Zeng,X.
  TITLE     CIZ1 knockdown suppresses the proliferation of bladder cancer cells
            by inducing apoptosis
  JOURNAL   Gene 719, 143946 (2019)
   PUBMED   31252164
  REMARK    GeneRIF: silencing of CIZ1 suppressed bladder cancer cell
            proliferation through inducing apoptosis and reducing cell cycle
            progression
REFERENCE   6  (residues 1 to 797)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 797)
  AUTHORS   Coverley,D., Marr,J. and Ainscough,J.
  TITLE     Ciz1 promotes mammalian DNA replication
  JOURNAL   J Cell Sci 118 (Pt 1), 101-112 (2005)
   PUBMED   15585571
REFERENCE   8  (residues 1 to 797)
  AUTHORS   Warder,D.E. and Keherly,M.J.
  TITLE     Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus
            DNA sequence ARYSR(0-2)YYAC
  JOURNAL   J Biomed Sci 10 (4), 406-417 (2003)
   PUBMED   12824700
  REMARK    GeneRIF: data indicate that Ciz1 is localized in the nucleus and is
            expressed in a wide range of tissues, especially the pancreas and
            the brain; formulated a consensus DNA sequence, ARYSR(0-2)YYAC,
            recognized by Ciz1
REFERENCE   9  (residues 1 to 797)
  AUTHORS   Mitsui,K., Matsumoto,A., Ohtsuka,S., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
            zinc finger protein, ciz1
  JOURNAL   Biochem Biophys Res Commun 264 (2), 457-464 (1999)
   PUBMED   10529385
REFERENCE   10 (residues 1 to 797)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303636.1, AL590708.18 and
            BC021163.2.
            
            Summary: The protein encoded by this gene is a zinc finger DNA
            binding protein that interacts with CIP1, part of a complex with
            cyclin E. The encoded protein may regulate the cellular
            localization of CIP1. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (7) has an alternate exon in place
            of the first exon, lacks an alternate in-frame exon, and lacks
            another alternate exon compared to variant 6, that causes a
            frameshift. The resulting isoform (6) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform 5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303636.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..797
                     /product="cip1-interacting zinc finger protein isoform 6"
                     /note="zinc finger protein 356; nuclear protein NP94;
                     Cip1-interacting zinc finger protein"
                     /calculated_mol_wt=88389
     Region          <28..381
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          491..520
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          555..575
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(562..564,565,569,574,591,594..598,600..601)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <565..>616
                     /region_name="UFD2"
                     /note="U1-like Zn-finger-containing protein [General
                     function prediction only]; COG5112"
                     /db_xref="CDD:227443"
     Region          585..609
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          586..608
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..797
                     /gene="CIZ1"
                     /gene_synonym="LSFR1; NP94; ZNF356"
                     /coded_by="NM_001257976.2:334..2727"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS59147.1"
                     /db_xref="GeneID:25792"
                     /db_xref="HGNC:HGNC:16744"
                     /db_xref="MIM:611420"
ORIGIN      
        1 mppatydtag ltmptatlgn lrgygmaspg laapsltppq latpnlqqff pqatrqsllg
       61 pppvgvpmnp sqfnlsgrnp qkqartssst tpnrkdsssq tmpvedksdp pegseeaaep
      121 rmdtpedqdl ppcpediake krtpapepep ceaselpakr lrsseeptek eppgqlqvka
      181 qpqarmtvpk qtqtpdllpe aleaqvlprf qprvlqvqaq vqsqtqprip stdtqvqpkl
      241 qkqaqtqtsp ehlvlqqkqv qpqlqqeaep qkqvqpqvqp qahsqgprqv qlqqeaeplk
      301 qvqpqvqpqa hsqpprqvql qlqkqvqtqt ypqvhtqaqp svqpqehppa qvsvqppeqt
      361 heqphtqpqv sllapeqtpv vvhvcglemp pdaveagggm ektlpepvgt qvsmeeiqne
      421 sacgldvgec enrarempgv wgaggslkvt ilqssdsraf stvpltpvpr psdsvsstpa
      481 atstpskqal qffcyickas cssqqefqdh msepqhqqrl geiqhmsqac llsllpvprd
      541 vletedeepp prrwcntcql yymgdliqhr rtqdhkiakq slrpfctvcn ryfktprkfv
      601 ehvksqghkd kakelkslek eiagqdedhf itvdavgcfe gdeeeeedde deeeieveee
      661 lckqvrsrdi sreewkgset yspntaygvd flvpvmgyic richkfyhsn sgaqlshcks
      721 lghfenlqky kaaknpsptt rpvsrrcain arnaltalft ssgrppsqpn tqdktpskvt
      781 arpsqpplpr rstrlkt
//
LOCUS       NP_060366                228 aa            linear   PRI 20-NOV-2025
DEFINITION  glucose-induced degradation protein 8 homolog [Homo sapiens].
ACCESSION   NP_060366 XP_005260277
VERSION     NP_060366.1
DBSOURCE    REFSEQ: accession NM_017896.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Han,Y., Pu,Y., Liu,X., Liu,Z., Chen,Y., Tang,L., Zhou,J., Song,Q.
            and Ji,Q.
  TITLE     YTHDF1 regulates GID8-mediated glutamine metabolism to promote
            colorectal cancer progression in m6A-dependent manner
  JOURNAL   Cancer Lett 601, 217186 (2024)
   PUBMED   39151722
  REMARK    GeneRIF: YTHDF1 regulates GID8-mediated glutamine metabolism to
            promote colorectal cancer progression in m6A-dependent manner.
REFERENCE   3  (residues 1 to 228)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 228)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 228)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 228)
  AUTHORS   Francis,O., Han,F. and Adams,J.C.
  TITLE     Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in
            eukaryotic cells and dominated by homologous components, the
            muskelin/RanBPM/CTLH complex
  JOURNAL   PLoS One 8 (10), e75217 (2013)
   PUBMED   24143168
  REMARK    Erratum:[PLoS One. 2013 Nov 8;8(11). doi:
            10.1371/annotation/1e464689-3c86-4399-b229-1e00d65593a5. PMID:
            29161723]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 228)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
REFERENCE   8  (residues 1 to 228)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
REFERENCE   9  (residues 1 to 228)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 228)
  AUTHORS   Umeda,M., Nishitani,H. and Nishimoto,T.
  TITLE     A novel nuclear protein, Twa1, and Muskelin comprise a complex with
            RanBPM
  JOURNAL   Gene 303, 47-54 (2003)
   PUBMED   12559565
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD676269.1, AK000609.1, BC032120.2, BQ931571.1, BQ935273.1,
            AK025775.1 and BC031819.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005260277.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.251224.1,
                                           SRR1803611.275507.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266069.5/ ENSP00000266069.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..228
                     /product="glucose-induced degradation protein 8 homolog"
                     /note="protein C20orf11; two hybrid associated protein No.
                     1 with RanBPM; two hybrid-associated protein 1 with
                     RanBPM"
                     /calculated_mol_wt=26618
     Region          28..52
                     /region_name="LisH"
                     /note="pfam08513"
                     /db_xref="CDD:462501"
     Region          63..207
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Region          116..212
                     /region_name="Interaction with CTNNB1.
                     /evidence=ECO:0000269|PubMed:28829046"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWU2.1)"
     CDS             1..228
                     /gene="GID8"
                     /gene_synonym="C20orf11; TWA1"
                     /coded_by="NM_017896.3:120..806"
                     /db_xref="CCDS:CCDS13510.1"
                     /db_xref="GeneID:54994"
                     /db_xref="HGNC:HGNC:15857"
                     /db_xref="MIM:611625"
ORIGIN      
        1 msyaekpdei tkdewmekln nlhvqradmn rlimnylvte gfkeaaekfr mesgiepsvd
       61 letlderiki remilkgqiq eaialinslh pelldtnryl yfhlqqqhli elirqretea
      121 alefaqtqla eqgeesrecl temertlall afdspeespf gdllhtmqrq kvwsevnqav
      181 ldyenrestp klakllklll waqneldqkk vkypkmtdls kgvieepk
//
LOCUS       NP_003745                357 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit F [Homo
            sapiens].
ACCESSION   NP_003745
VERSION     NP_003745.1
DBSOURCE    REFSEQ: accession NM_003754.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Pan,Q., Yu,F., Jin,H., Zhang,P., Huang,X., Peng,J., Xie,X., Li,X.,
            Ma,N., Wei,Y., Wen,W., Zhang,J., Zhang,B., Yu,H., Xiao,Y.,
            Liu,R.Y., Liu,Q., Meng,X. and Lee,M.H.
  TITLE     eIF3f Mediates SGOC Pathway Reprogramming by Enhancing
            Deubiquitinating Activity in Colorectal Cancer
  JOURNAL   Adv Sci (Weinh) 10 (27), e2300759 (2023)
   PUBMED   37544925
  REMARK    GeneRIF: eIF3f Mediates SGOC Pathway Reprogramming by Enhancing
            Deubiquitinating Activity in Colorectal Cancer.
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Huffmeier,U., Kraus,C., Reuter,M.S., Uebe,S., Abbott,M.A.,
            Ahmed,S.A., Rawson,K.L., Barr,E., Li,H., Bruel,A.L., Faivre,L.,
            Tran Mau-Them,F., Botti,C., Brooks,S., Burns,K., Ward,D.I.,
            Dutra-Clarke,M., Martinez-Agosto,J.A., Lee,H., Nelson,S.F.,
            Zacher,P., Abou Jamra,R., Klockner,C., McGaughran,J., Kohlhase,J.,
            Schuhmann,S., Moran,E., Pappas,J., Raas-Rothschild,A.,
            Sacoto,M.J.G., Henderson,L.B., Palculict,T.B., Mullegama,S.V.,
            Zghal Elloumi,H., Reich,A., Schrier Vergano,S.A., Wahl,E., Reis,A.
            and Zweier,C.
  CONSRTM   UCLA California Center for Rare Disease
  TITLE     EIF3F-related neurodevelopmental disorder: refining the phenotypic
            and expanding the molecular spectrum
  JOURNAL   Orphanet J Rare Dis 16 (1), 136 (2021)
   PUBMED   33736665
  REMARK    GeneRIF: EIF3F-related neurodevelopmental disorder: refining the
            phenotypic and expanding the molecular spectrum.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Block,K.L., Vornlocher,H.P. and Hershey,J.W.
  TITLE     Characterization of cDNAs encoding the p44 and p35 subunits of
            human translation initiation factor eIF3
  JOURNAL   J Biol Chem 273 (48), 31901-31908 (1998)
   PUBMED   9822659
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Asano,K., Vornlocher,H.P., Richter-Cook,N.J., Merrick,W.C.,
            Hinnebusch,A.G. and Hershey,J.W.
  TITLE     Structure of cDNAs encoding human eukaryotic initiation factor 3
            subunits. Possible roles in RNA binding and macromolecular assembly
  JOURNAL   J Biol Chem 272 (43), 27042-27052 (1997)
   PUBMED   9341143
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Asano,K., Kinzy,T.G., Merrick,W.C. and Hershey,J.W.
  TITLE     Conservation and diversity of eukaryotic translation initiation
            factor eIF3
  JOURNAL   J Biol Chem 272 (2), 1101-1109 (1997)
   PUBMED   8995409
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from CB141463.1, U94855.1, CD050033.1, BC000490.2 and
            AC116456.12.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.246689.1,
                                           SRR1660805.149226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000651655.1/ ENSP00000499218.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..357
                     /product="eukaryotic translation initiation factor 3
                     subunit F"
                     /EC_number="3.4.19.12"
                     /note="eukaryotic translation initiation factor 3, subunit
                     5 (epsilon, 47kD); eukaryotic translation initiation
                     factor 3, subunit 5 epsilon, 47kDa; eIF3-epsilon;
                     eIF-3-epsilon; deubiquitinating enzyme eIF3f"
                     /calculated_mol_wt=37433
     Region          1..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00303.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03005,
                     ECO:0000269|PubMed:17322308; propagated from
                     UniProtKB/Swiss-Prot (O00303.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK11, in vitro.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03005,
                     ECO:0000269|PubMed:12446680; propagated from
                     UniProtKB/Swiss-Prot (O00303.1)"
     Region          92..354
                     /region_name="MPN_eIF3f"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains without
                     catalytic isopeptidase activity, found in eIF3f; cd08064"
                     /db_xref="CDD:163695"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00303.1)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03005,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00303.1)"
     CDS             1..357
                     /gene="EIF3F"
                     /gene_synonym="eIF3-p47; EIF3S5; MRT67"
                     /coded_by="NM_003754.3:17..1090"
                     /db_xref="CCDS:CCDS7785.1"
                     /db_xref="GeneID:8665"
                     /db_xref="HGNC:HGNC:3275"
                     /db_xref="MIM:603914"
ORIGIN      
        1 matpavpvsa ppatptpvpa aapasvpapt papaaapvpa aapasssdpa aaaaataapg
       61 qtpasaqapa qtpapalpgp alpgpfpggr vvrlhpvila sivdsyerrn egaarvigtl
      121 lgtvdkhsve vtncfsvphn esedevavdm efaknmyelh kkvspnelil gwyatghdit
      181 ehsvliheyy sreapnpihl tvdtslqngr msikayvstl mgvpgrtmgv mftpltvkya
      241 yydterigvd limktcfspn rviglssdlq qvggasariq dalstvlqya edvlsgkvsa
      301 dntvgrflms lvnqvpkivp ddfetmlnsn indllmvtyl anltqsqial neklvnl
//
LOCUS       NP_003087                 76 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein G isoform a [Homo sapiens].
ACCESSION   NP_003087
VERSION     NP_003087.1
DBSOURCE    REFSEQ: accession NM_003096.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Plessel,G., Luhrmann,R. and Kastner,B.
  TITLE     Electron microscopy of assembly intermediates of the snRNP core:
            morphological similarities between the RNA-free (E.F.G) protein
            heteromer and the intact snRNP core
  JOURNAL   J Mol Biol 265 (2), 87-94 (1997)
   PUBMED   9020971
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Hermann,H., Fabrizio,P., Raker,V.A., Foulaki,K., Hornig,H.,
            Brahms,H. and Luhrmann,R.
  TITLE     snRNP Sm proteins share two evolutionarily conserved sequence
            motifs which are involved in Sm protein-protein interactions
  JOURNAL   EMBO J 14 (9), 2076-2088 (1995)
   PUBMED   7744013
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Heinrichs,V., Hackl,W. and Luhrmann,R.
  TITLE     Direct binding of small nuclear ribonucleoprotein G to the Sm site
            of small nuclear RNA. Ultraviolet light cross-linking of protein G
            to the AAU stretch within the Sm site (AAUUUGUGG) of U1 small
            nuclear ribonucleoprotein reconstituted in vitro
  JOURNAL   J Mol Biol 227 (1), 15-28 (1992)
   PUBMED   1387914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DW428820.1, BC106055.1 and
            AI742299.1.
            
            Summary: The protein encoded by this gene is a component of the U1,
            U2, U4, and U5 small nuclear ribonucleoprotein complexes,
            precursors of the spliceosome. The encoded protein may also be a
            part of the U7 small nuclear ribonucleoprotein complex, which
            participates in the processing of the 3' end of histone
            transcripts. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (1) encodes the highly conserved
            isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG772605.1, HX785413.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272348.7/ ENSP00000272348.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..76
                     /product="small nuclear ribonucleoprotein G isoform a"
                     /EC_number="1.8.1.4"
                     /note="small nuclear ribonucleoprotein G; snRNP-G; sm
                     protein G"
                     /calculated_mol_wt=8365
     Region          5..74
                     /region_name="Sm_G"
                     /note="Sm protein G; cd01719"
                     /db_xref="CDD:212466"
     Site            order(8,12,20,25,38,59,61..62,64,67..71,73)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212466"
     Site            order(17..23,25..37,39..43)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212466"
     Site            order(37,39,63,65)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212466"
     Site            59..70
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212466"
     CDS             1..76
                     /gene="SNRPG"
                     /gene_synonym="Sm-G; SMG"
                     /coded_by="NM_003096.4:92..322"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1903.1"
                     /db_xref="GeneID:6637"
                     /db_xref="HGNC:HGNC:11163"
                     /db_xref="MIM:603542"
ORIGIN      
        1 mskahppelk kfmdkklslk lnggrhvqgi lrgfdpfmnl videcvemat sgqqnnigmv
       61 virgnsiiml ealerv
//
LOCUS       NP_588616                971 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 2 [Homo sapiens].
ACCESSION   NP_588616
VERSION     NP_588616.1
DBSOURCE    REFSEQ: accession NM_133375.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 971)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 971)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 971)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 971)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 971)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 971)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 971)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 971)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 971)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 971)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Transcript Variant: This variant (2) represents an alternate first
            exon and the transcript has a smaller open reading frame compared
            to variant 1. The resulting protein isoform (2) has a shorter
            N-terminus than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022089.2, SRR1803616.59524.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..971
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..971
                     /product="DIS3-like exonuclease 1 isoform 2"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=110988
     Region          <1..105
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          155..783
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          798..873
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..971
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_133375.5:170..3085"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10214.1"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mqtacqavqh qrgrrqynkl rnllkdarhd cilfanefqq ccylprerge smekwqtrsi
       61 ynaavwyyhh cqdrmpivmv tedeeaiqqy gsetegvfvi tfknyldnfw pdlkaahelc
      121 dsilqsrrer enesqeshgk eypehlplev leagiksgry iqgilnvnkh raqieafvrl
      181 qgasskdsdl vsdilihgmk arnrsihgdv vvvellpkne wkgrtvalce ndcddkasge
      241 spsepmptgr vvgilqknwr dyvvtfpske evqsqgknaq kilvtpwdyr ipkiristqq
      301 aetlqdfrvv vridswests vypnghfvrv lgrigdlege iatilvensi svipfseaqm
      361 cempvntpes pwkvspeeeq krkdlrkshl vfsidpkgce dvddtlsvrt lnngnlelgv
      421 hiadvthfva pnsyidiear trattyylad rrydmlpsvl sadlcsllgg vdryavsimw
      481 eldkasyeik kvwygrtiir sayklfyeaa qelldgnlsv vddipefkdl deksrqakle
      541 elvwaigklt diarhvrakr dgcgaleleg vevcvqlddk knihdlipkq plevhetvae
      601 cmilanhwva kkiwesfphq allrqhppph qeffselrec akakgffidt rsnktladsl
      661 dnandphdpi vnrllrsmat qamsnalyfs tgscaeeefh hyglaldkyt hftspirrys
      721 divvhrllma aiskdkkmei kgnlfsnkdl eelcrhinnr nqaaqhsqkq stelfqcmyf
      781 kdkdpateer cisdgviysi rtngvllfip rfgikgaayl knkdglvisc gpdscsewkp
      841 gslqrfqnki tstttdgesv tfhlfdhvtv risiqasrch sdtirleiis nkpykipnte
      901 lihqsspllk selvkevtks veeaqlaqev kvniiqeeyq eyrqtkgrsl ytlleeirdl
      961 alldvsnnyg i
//
LOCUS       NP_001180263             450 aa            linear   PRI 20-NOV-2025
DEFINITION  protein wntless homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001180263
VERSION     NP_001180263.1
DBSOURCE    REFSEQ: accession NM_001193334.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Abdel-Salam,G.M.H., Afifi,H.H., Abdel-Hamid,M.S., Ahmed,N.E.B.,
            Taher,M.B., El-Kamah,G., Thiele,H., Nurnberg,P.N. and Bolz,H.J.
  TITLE     Expanding the phenotypic spectrum and clinical severity associated
            with WLS gene
  JOURNAL   J Hum Genet 68 (9), 607-613 (2023)
   PUBMED   37106064
  REMARK    GeneRIF: Expanding the phenotypic spectrum and clinical severity
            associated with WLS gene.
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Yu,C., Wang,C., Zhou,W., Zhang,A., Jia,Z., Zheng,B. and Ding,G.
  TITLE     Compound heterozygous variants in WLS gene causes Zaki syndrome
  JOURNAL   Clin Genet 104 (2), 226-229 (2023)
   PUBMED   37005218
  REMARK    GeneRIF: Compound heterozygous variants in WLS gene causes Zaki
            syndrome.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Kantaputra,P., Tripuwabhrut,K., Jatooratthawichot,P.,
            Adisornkanj,P., Hatsadaloi,A., Porntrakoolsaree,N., Kaewgaya,M.,
            Olsen,B., Tongsima,S., Ngamphiw,C. and Ketudat Cairns,J.R.
  TITLE     Mutations in the WLS are associated with dental anomalies, torus
            palatinus, and torus mandibularis
  JOURNAL   Eur J Orthod 45 (3), 317-323 (2023)
   PUBMED   36374649
  REMARK    GeneRIF: Mutations in the WLS are associated with dental anomalies,
            torus palatinus, and torus mandibularis.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Wolf,L. and Boutros,M.
  TITLE     The role of Evi/Wntless in exporting Wnt proteins
  JOURNAL   Development 150 (3) (2023)
   PUBMED   36763105
  REMARK    GeneRIF: The role of Evi/Wntless in exporting Wnt proteins.
            Review article
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Belenkaya,T.Y., Wu,Y., Tang,X., Zhou,B., Cheng,L., Sharma,Y.V.,
            Yan,D., Selva,E.M. and Lin,X.
  TITLE     The retromer complex influences Wnt secretion by recycling wntless
            from endosomes to the trans-Golgi network
  JOURNAL   Dev Cell 14 (1), 120-131 (2008)
   PUBMED   18160348
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Binnerts,M.E., Kim,K.A., Bright,J.M., Patel,S.M., Tran,K., Zhou,M.,
            Leung,J.M., Liu,Y., Lomas,W.E. 3rd, Dixon,M., Hazell,S.A.,
            Wagle,M., Nie,W.S., Tomasevic,N., Williams,J., Zhan,X., Levy,M.D.,
            Funk,W.D. and Abo,A.
  TITLE     R-Spondin1 regulates Wnt signaling by inhibiting internalization of
            LRP6
  JOURNAL   Proc Natl Acad Sci U S A 104 (37), 14700-14705 (2007)
   PUBMED   17804805
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Bartscherer,K., Pelte,N., Ingelfinger,D. and Boutros,M.
  TITLE     Secretion of Wnt ligands requires Evi, a conserved transmembrane
            protein
  JOURNAL   Cell 125 (3), 523-533 (2006)
   PUBMED   16678096
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Banziger,C., Soldini,D., Schutt,C., Zipperlen,P., Hausmann,G. and
            Basler,K.
  TITLE     Wntless, a conserved membrane protein dedicated to the secretion of
            Wnt proteins from signaling cells
  JOURNAL   Cell 125 (3), 509-522 (2006)
   PUBMED   16678095
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA753300.1, DB478499.1, BX648748.1, AL513284.12 and AW137622.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an alternate in-frame exon in the 5' coding region, compared
            to variant 1, resulting in an isoform (3) that is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX648748.1, SRR14038195.1480134.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..450
                     /product="protein wntless homolog isoform 3"
                     /note="G protein-coupled receptor 177; integral membrane
                     protein GPR177; putative NFkB activating protein 373;
                     protein evenness interrupted homolog; putative
                     NF-kappa-B-activating protein 373; wntless Wnt ligand
                     secretion mediator"
                     /calculated_mol_wt=51440
     Region          87..405
                     /region_name="MIG-14_Wnt-bd"
                     /note="Wnt-binding factor required for Wnt secretion;
                     pfam06664"
                     /db_xref="CDD:461980"
     CDS             1..450
                     /gene="WLS"
                     /gene_synonym="C1orf139; EVI; GPR177; mig-14; MRP; ZKS"
                     /coded_by="NM_001193334.1:248..1600"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53331.1"
                     /db_xref="GeneID:79971"
                     /db_xref="HGNC:HGNC:30238"
                     /db_xref="MIM:611514"
ORIGIN      
        1 magaiienms tkklcivggi llvfqiiafl vggligenae vsmdvslayr ddafaewtem
       61 ahervprklk ctftspktpe hegryyecdv lpfmeigsva hkfyllnirl pvnekkkinv
      121 gigeikdirl vgihqnggft kvwfamktfl tpsifiimvw ywrritmmsr ppvllekvif
      181 algismtfin ipvewfsigf dwtwmllfgd irqgifyaml lsfwiifcge hmmdqhernh
      241 iagywkqvgp iavgsfclfi fdmcergvql tnpfysiwtt digtelamaf iivagiclcl
      301 yflflcfmvf qvfrnisgkq sslpamskvr rlhyeglifr fkflmlitla caamtviffi
      361 vsqvteghwk wggvtvqvns afftgiygmw nlyvfalmfl yapshknyge dqsngdlgvh
      421 sgeelqlttt ithvdgptei ykltrkeaqe
//
LOCUS       NP_001135771             356 aa            linear   PRI 20-NOV-2025
DEFINITION  sequestosome-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001135771
VERSION     NP_001135771.1
DBSOURCE    REFSEQ: accession NM_001142299.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 356)
  AUTHORS   Kramer,N., Mato,U.G., Krauter,S., Buscher,N., Afifi,A., Herhaus,L.,
            Florin,L., Plachter,B. and Zimmermann,C.
  TITLE     The Autophagy Receptor SQSTM1/p62 Is a Restriction Factor of HCMV
            Infection
  JOURNAL   Viruses 16 (9), 1440 (2024)
   PUBMED   39339916
  REMARK    GeneRIF: The Autophagy Receptor SQSTM1/p62 Is a Restriction Factor
            of HCMV Infection.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 356)
  AUTHORS   Dasgupta,N., Lei,X., Shi,C.H., Arnold,R., Teneche,M.G.,
            Miller,K.N., Rajesh,A., Davis,A., Anschau,V., Campos,A.R.,
            Gilson,R., Havas,A., Yin,S., Chua,Z.M., Liu,T., Proulx,J.,
            Alcaraz,M., Rather,M.I., Baeza,J., Schultz,D.C., Yip,K.Y.,
            Berger,S.L. and Adams,P.D.
  TITLE     Histone chaperone HIRA, promyelocytic leukemia protein, and
            p62/SQSTM1 coordinate to regulate inflammation during cell
            senescence
  JOURNAL   Mol Cell 84 (17), 3271-3287 (2024)
   PUBMED   39178863
  REMARK    GeneRIF: Histone chaperone HIRA, promyelocytic leukemia protein,
            and p62/SQSTM1 coordinate to regulate inflammation during cell
            senescence.
REFERENCE   3  (residues 1 to 356)
  AUTHORS   Martin,S., Scorzoni,S., Cordone,S., Mazzagatti,A.,
            Beznoussenko,G.V., Gunn,A.L., Di Bona,M., Eliezer,Y., Leor,G.,
            Ben-Yishay,T., Loffreda,A., Cancila,V., Rainone,M.C.,
            Ippolito,M.R., Martis,V., Bedin,F., Garre,M., Vaites,L.P.,
            Vasapolli,P., Polo,S., Parazzoli,D., Tripodo,C., Mironov,A.A.,
            Cuomo,A., Ben-David,U., Bakhoum,S.F., Hatch,E.M., Ly,P. and
            Santaguida,S.
  TITLE     A p62-dependent rheostat dictates micronuclei catastrophe and
            chromosome rearrangements
  JOURNAL   Science 385 (6712), eadj7446 (2024)
   PUBMED   39208097
  REMARK    GeneRIF: A p62-dependent rheostat dictates micronuclei catastrophe
            and chromosome rearrangements.
REFERENCE   4  (residues 1 to 356)
  AUTHORS   Wang,Y., Lyu,L., Vu,T. and McCarty,N.
  TITLE     TRIM44 enhances autophagy via SQSTM1 oligomerization in response to
            oxidative stress
  JOURNAL   Sci Rep 14 (1), 18974 (2024)
   PUBMED   39152142
  REMARK    GeneRIF: TRIM44 enhances autophagy via SQSTM1 oligomerization in
            response to oxidative stress.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 356)
  AUTHORS   Vadlamudi,R.K., Joung,I., Strominger,J.L. and Shin,J.
  TITLE     p62, a phosphotyrosine-independent ligand of the SH2 domain of
            p56lck, belongs to a new class of ubiquitin-binding proteins
  JOURNAL   J Biol Chem 271 (34), 20235-20237 (1996)
   PUBMED   8702753
REFERENCE   6  (residues 1 to 356)
  AUTHORS   Joung,I., Strominger,J.L. and Shin,J.
  TITLE     Molecular cloning of a phosphotyrosine-independent ligand of the
            p56lck SH2 domain
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 5991-5995 (1996)
   PUBMED   8650207
REFERENCE   7  (residues 1 to 356)
  AUTHORS   Devergne,O., Hummel,M., Koeppen,H., Le Beau,M.M., Nathanson,E.C.,
            Kieff,E. and Birkenbach,M.
  TITLE     A novel interleukin-12 p40-related protein induced by latent
            Epstein-Barr virus infection in B lymphocytes
  JOURNAL   J Virol 70 (2), 1143-1153 (1996)
   PUBMED   8551575
  REMARK    Erratum:[J Virol 1996 Apr;70(4):2678]
REFERENCE   8  (residues 1 to 356)
  AUTHORS   Park,I., Chung,J., Walsh,C.T., Yun,Y., Strominger,J.L. and Shin,J.
  TITLE     Phosphotyrosine-independent binding of a 62-kDa protein to the src
            homology 2 (SH2) domain of p56lck and its regulation by
            phosphorylation of Ser-59 in the lck unique N-terminal region
  JOURNAL   Proc Natl Acad Sci U S A 92 (26), 12338-12342 (1995)
   PUBMED   8618896
REFERENCE   9  (residues 1 to 356)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   10 (residues 1 to 356)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA541885.1, BC000951.2,
            BC017222.1 and BU625974.1.
            
            Summary: This gene encodes a multifunctional protein that binds
            ubiquitin and regulates activation of the nuclear factor kappa-B
            (NF-kB) signaling pathway. The protein functions as a
            scaffolding/adaptor protein in concert with TNF receptor-associated
            factor 6 to mediate activation of NF-kB in response to upstream
            signals. Alternatively spliced transcript variants encoding either
            the same or different isoforms have been identified for this gene.
            Mutations in this gene result in sporadic and familial Paget
            disease of bone. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation from an
            in-frame downstream start codon compared to variant 1. This results
            in an isoform (2) with a shorter N-terminus compared to isoform 1.
            Variants 2 and 3 differ in the 5' UTR, but encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.159731.1,
                                           SRR1803617.15086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..356
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..356
                     /product="sequestosome-1 isoform 2"
                     /note="oxidative stress induced like; ubiquitin-binding
                     protein p62; EBI3-associated protein p60; phosphotyrosine
                     independent ligand for the Lck SH2 domain p62;
                     EBI3-associated protein of 60 kDa;
                     phosphotyrosine-independent ligand for the Lck SH2 domain
                     of 62 kDa; autophagy receptor p62"
                     /calculated_mol_wt=38498
     Region          <1..18
                     /region_name="PB1"
                     /note="The PB1 domain is a modular domain mediating
                     specific protein-protein interactions which play a role in
                     many critical cell processes, such as osteoclastogenesis,
                     angiogenesis, early cardiovascular development, and cell
                     polarity. A canonical PB1-PB1...; cl02720"
                     /db_xref="CDD:413452"
     Region          42..84
                     /region_name="ZZ_NBR1_like"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     Drosophila ref(2)P, NBR1, Human sequestosome 1 and related
                     proteins. The ZZ motif coordinates two zinc ions and most
                     likely participates in ligand binding or molecular
                     scaffolding. Drosophila ref(2)P appears...; cd02340"
                     /db_xref="CDD:239080"
     Site            order(44,47,58,61,67,70,76,79)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239080"
     Site            order(44,47,67,70)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239080"
     Site            order(45,55,57,63,65)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239080"
     Site            order(56,81,84)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239080"
     Site            order(58,61,76,79)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239080"
     Region          295..356
                     /region_name="UBA_5"
                     /note="UBA domain; pfam16577"
                     /db_xref="CDD:318725"
     Site            order(320..322,325..328,331..332,335,346..348)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270505"
     CDS             1..356
                     /gene="SQSTM1"
                     /gene_synonym="A170; DMRV; EBIAP; FTDALS3; NADGP; OSIL;
                     p60; p62; p62B; PDB3; ZIP3"
                     /coded_by="NM_001142299.2:272..1342"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47355.1"
                     /db_xref="GeneID:8878"
                     /db_xref="HGNC:HGNC:11280"
                     /db_xref="MIM:601530"
ORIGIN      
        1 mamsyvkddi friyikekke crrdhrppca qeaprnmvhp nvicdgcngp vvgtrykcsv
       61 cpdydlcsvc egkglhrght klafpspfgh lsegfshsrw lrkvkhghfg wpgwemgppg
      121 nwsprpprag earpgptaes asgpsedpsv nflknvgesv aaalsplgie vdidvehggk
      181 rsrltpvspe sssteeksss qpssccsdps kpggnvegat qslaeqmrki alesegrpee
      241 qmesdncsgg dddwthlssk evdpstgelq slqmpesegp ssldpsqegp tglkeaalyp
      301 hlppeadprl ieslsqmlsm gfsdeggwlt rllqtknydi gaaldtiqys khpppl
//
LOCUS       NP_002730                697 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C gamma type isoform 2 [Homo sapiens].
ACCESSION   NP_002730
VERSION     NP_002730.1
DBSOURCE    REFSEQ: accession NM_002739.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 697)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 697)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 697)
  AUTHORS   Xu,Z., Li,Q. and Shen,X.
  TITLE     AZU1 (HBP/CAP37) and PRKCG (PKC-gamma) may be candidate genes
            affecting the severity of acute mountain sickness
  JOURNAL   BMC Med Genomics 16 (1), 28 (2023)
   PUBMED   36803152
  REMARK    GeneRIF: AZU1 (HBP/CAP37) and PRKCG (PKC-gamma) may be candidate
            genes affecting the severity of acute mountain sickness.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 697)
  AUTHORS   Gan,Y., Long,J., Zeng,Y., Zhang,Y. and Tao,Y.
  TITLE     lncRNA IL-17RA-1 Attenuates LPS-Induced Sepsis via
            miR-7847-3p/PRKCG-Mediated MAPK Signaling Pathway
  JOURNAL   Mediators Inflamm 2022, 9923204 (2022)
   PUBMED   36274974
  REMARK    GeneRIF: lncRNA IL-17RA-1 Attenuates LPS-Induced Sepsis via
            miR-7847-3p/PRKCG-Mediated MAPK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 697)
  AUTHORS   Chen,D.H., Bird,T.D. and Raskind,W.H.
  TITLE     Spinocerebellar Ataxia Type 14
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301573
REFERENCE   6  (residues 1 to 697)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 697)
  AUTHORS   McSwine-Kennick,R.L., McKeegan,E.M., Johnson,M.D. and Morin,M.J.
  TITLE     Phorbol diester-induced alterations in the expression of protein
            kinase C isozymes and their mRNAs. Analysis in wild-type and
            phorbol diester-resistant HL-60 cell clones
  JOURNAL   J Biol Chem 266 (23), 15135-15143 (1991)
   PUBMED   1714454
REFERENCE   8  (residues 1 to 697)
  AUTHORS   Jakobovits,A., Rosenthal,A. and Capon,D.J.
  TITLE     Trans-activation of HIV-1 LTR-directed gene expression by tat
            requires protein kinase C
  JOURNAL   EMBO J 9 (4), 1165-1170 (1990)
   PUBMED   2182321
  REMARK    Erratum:[EMBO J 1990 Oct;9(10):3413]
REFERENCE   9  (residues 1 to 697)
  AUTHORS   Saunders,A.M. and Seldin,M.F.
  TITLE     The syntenic relationship of proximal mouse chromosome 7 and the
            myotonic dystrophy gene region on human chromosome 19q
  JOURNAL   Genomics 6 (2), 324-332 (1990)
   PUBMED   2307474
REFERENCE   10 (residues 1 to 697)
  AUTHORS   Johnson,K.J., Jones,P.J., Spurr,N., Nimmo,E., Davies,J., Creed,H.,
            Weiss,M. and Williamson,R.
  TITLE     Linkage relationships of the protein kinase C gamma gene which
            exclude it as a candidate for myotonic dystrophy
  JOURNAL   Cytogenet Cell Genet 48 (1), 13-15 (1988)
   PUBMED   2460293
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC318717.1, BC047876.1 and
            AC008440.9.
            
            Summary: Protein kinase C (PKC) is a family of serine- and
            threonine-specific protein kinases that can be activated by calcium
            and second messenger diacylglycerol. PKC family members
            phosphorylate a wide variety of protein targets and are known to be
            involved in diverse cellular signaling pathways. PKC also serve as
            major receptors for phorbol esters, a class of tumor promoters.
            Each member of the PKC family has a specific expression profile and
            is believed to play distinct roles in cells. The protein encoded by
            this gene is one of the PKC family members. This protein kinase is
            expressed solely in the brain and spinal cord and its localization
            is restricted to neurons. It has been demonstrated that several
            neuronal functions, including long term potentiation (LTP) and long
            term depression (LTD), specifically require this kinase. Knockout
            studies in mice also suggest that this kinase may be involved in
            neuropathic pain development. Defects in this protein have been
            associated with neurodegenerative disorder spinocerebellar
            ataxia-14 (SCA14). Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2015].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.912204.1,
                                           SRR3476690.862624.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263431.4/ ENSP00000263431.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..697
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..697
                     /product="protein kinase C gamma type isoform 2"
                     /EC_number="2.7.11.13"
                     /note="protein kinase C gamma type"
                     /calculated_mol_wt=78317
     Region          34..91
                     /region_name="C1_cPKC_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in the classical (or conventional) protein
                     kinase C (cPKC) family; cd20833"
                     /db_xref="CDD:410383"
     Site            order(41..47,55..59,62)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410383"
     Region          101..154
                     /region_name="C1_cPKC_rpt2"
                     /note="second protein kinase C conserved region 1 (C1
                     domain) found in the classical (or conventional) protein
                     kinase C (cPKC) family; cd20836"
                     /db_xref="CDD:410386"
     Site            order(106..112,120..124,127)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410386"
     Region          158..289
                     /region_name="C2_PKC_alpha_gamma"
                     /note="C2 domain in Protein Kinase C (PKC) alpha and
                     gamma; cd04026"
                     /db_xref="CDD:175992"
     Site            order(187,193,246,248,254)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175992"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Region          354..677
                     /region_name="STKc_cPKC"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Classical (or Conventional) Protein Kinase C; cd05587"
                     /db_xref="CDD:270739"
     Site            order(357..361,365,378,380,418,434..435,437,441,443,480,
                     482,484..485,487,497..498,501,515..520,547,553,556)
                     /site_type="active"
                     /db_xref="CDD:270739"
     Site            order(357..361,365,378,380,418,435..437,441,480,482,
                     484..485,487,497..498)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270739"
     Site            order(361,441,443,480,482,484,501,515..520,547,553,556)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270739"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            497..520
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270739"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PDPK1.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            655
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270739"
     Site            670..675
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270739"
     Site            674
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P63318; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SYK. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P05129.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63319; propagated from
                     UniProtKB/Swiss-Prot (P05129.3)"
     CDS             1..697
                     /gene="PRKCG"
                     /gene_synonym="PKC-gamma; PKCC; PKCG; PKCgamma; PKCI(3);
                     SCA14"
                     /coded_by="NM_002739.5:299..2392"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12867.1"
                     /db_xref="GeneID:5582"
                     /db_xref="HGNC:HGNC:9402"
                     /db_xref="MIM:176980"
ORIGIN      
        1 maglgpgvgd seggprplfc rkgalrqkvv hevkshkfta rffkqptfcs hctdfiwgig
       61 kqglqcqvcs fvvhrrchef vtfecpgagk gpqtddprnk hkfrlhsyss ptfcdhcgsl
      121 lyglvhqgmk csccemnvhr rcvrsvpslc gvdhterrgr lqleirapta deihvtvgea
      181 rnlipmdpng lsdpyvklkl ipdprnltkq ktrtvkatln pvwnetfvfn lkpgdverrl
      241 svevwdwdrt srndfmgams fgvsellkap vdgwykllnq eegeyynvpv adadncsllq
      301 kfeacnyple lyervrmgps sspipspsps ptdpkrcffg aspgrlhisd fsflmvlgkg
      361 sfgkvmlaer rgsdelyaik ilkkdvivqd ddvdctlvek rvlalggrgp ggrphfltql
      421 hstfqtpdrl yfvmeyvtgg dlmyhiqqlg kfkephaafy aaeiaiglff lhnqgiiyrd
      481 lkldnvmlda eghikitdfg mckenvfpgt ttrtfcgtpd yiapeiiayq pygksvdwws
      541 fgvllyemla gqppfdgede eelfqaimeq tvtypkslsr eavaickgfl tkhpgkrlgs
      601 gpdgeptira hgffrwidwe rlerleippp frprpcgrsg enfdkfftra apaltppdrl
      661 vlasidqadf qgftyvnpdf vhpdarspts pvpvpvm
//
LOCUS       NP_699181                479 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 16 [Homo sapiens].
ACCESSION   NP_699181
VERSION     NP_699181.2
DBSOURCE    REFSEQ: accession NM_153350.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Yao,L.P., Wang,Z.K., Jiang,X.Q., Jiang,B., Chen,S.J., Hua,Z.D.,
            Gao,D.D., Zheng,Q., Zhu,S.M., Qian,M.X., Zhang,F., Xu,L.F.,
            Chen,C.S. and Lu,F.
  TITLE     MiR-1307-5p enhances fibroblast transdifferentiation to exacerbate
            chronic obstructive pulmonary disease through regulating
            FBXL16/HIF1alpha axis
  JOURNAL   Respir Res 25 (1), 376 (2024)
   PUBMED   39420370
  REMARK    GeneRIF: MiR-1307-5p enhances fibroblast transdifferentiation to
            exacerbate chronic obstructive pulmonary disease through regulating
            FBXL16/HIF1alpha axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Liu,H., Han,L., Zhong,L., Zhuang,X. and Peng,Y.
  TITLE     FBXL16 Promotes Endometrial Progesterone Resistance via
            PP2AB55alpha /Cyclin D1 Axis in Ishikawa
  JOURNAL   J Immunol Res 2022, 7372202 (2022)
   PUBMED   36106050
  REMARK    GeneRIF: FBXL16 Promotes Endometrial Progesterone Resistance via
            PP2A(B55alpha) /Cyclin D1 Axis in Ishikawa.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Kim,Y.J., Zhao,Y., Myung,J.K., Yi,J.M., Kim,M.J. and Lee,S.J.
  TITLE     Suppression of breast cancer progression by FBXL16 via
            oxygen-independent regulation of HIF1alpha stability
  JOURNAL   Cell Rep 37 (8), 109996 (2021)
   PUBMED   34818544
  REMARK    GeneRIF: Suppression of breast cancer progression by FBXL16 via
            oxygen-independent regulation of HIF1alpha stability.
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Yang,M. and Jing,F.
  TITLE     FBXL16 modulates the proliferation and autophagy in breast cancer
            cells via activating SRC-3-AKT signaling pathway
  JOURNAL   Reprod Biol 21 (3), 100538 (2021)
   PUBMED   34333223
  REMARK    GeneRIF: FBXL16 modulates the proliferation and autophagy in breast
            cancer cells via activating SRC-3-AKT signaling pathway.
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Sato,K., Kusama,Y., Tategu,M. and Yoshida,K.
  TITLE     FBXL16 is a novel E2F1-regulated gene commonly upregulated in
            p16INK4A- and p14ARF-silenced HeLa cells
  JOURNAL   Int J Oncol 36 (2), 479-490 (2010)
   PUBMED   20043084
  REMARK    GeneRIF: the expression of FBXL16 reproducibly upregulated in
            p16INK4A and p14ARF knockdown HeLa cells
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Martin,J., Han,C., Gordon,L.A., Terry,A., Prabhakar,S., She,X.,
            Xie,G., Hellsten,U., Chan,Y.M., Altherr,M., Couronne,O., Aerts,A.,
            Bajorek,E., Black,S., Blumer,H., Branscomb,E., Brown,N.C.,
            Bruno,W.J., Buckingham,J.M., Callen,D.F., Campbell,C.S.,
            Campbell,M.L., Campbell,E.W., Caoile,C., Challacombe,J.F.,
            Chasteen,L.A., Chertkov,O., Chi,H.C., Christensen,M., Clark,L.M.,
            Cohn,J.D., Denys,M., Detter,J.C., Dickson,M.,
            Dimitrijevic-Bussod,M., Escobar,J., Fawcett,J.J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Goodwin,L.A., Grady,D.L., Grigoriev,I., Groza,M., Hammon,N.,
            Hawkins,T., Haydu,L., Hildebrand,C.E., Huang,W., Israni,S.,
            Jett,J., Jewett,P.B., Kadner,K., Kimball,H., Kobayashi,A.,
            Krawczyk,M.C., Leyba,T., Longmire,J.L., Lopez,F., Lou,Y., Lowry,S.,
            Ludeman,T., Manohar,C.F., Mark,G.A., McMurray,K.L., Meincke,L.J.,
            Morgan,J., Moyzis,R.K., Mundt,M.O., Munk,A.C., Nandkeshwar,R.D.,
            Pitluck,S., Pollard,M., Predki,P., Parson-Quintana,B., Ramirez,L.,
            Rash,S., Retterer,J., Ricke,D.O., Robinson,D.L., Rodriguez,A.,
            Salamov,A., Saunders,E.H., Scott,D., Shough,T., Stallings,R.L.,
            Stalvey,M., Sutherland,R.D., Tapia,R., Tesmer,J.G., Thayer,N.,
            Thompson,L.S., Tice,H., Torney,D.C., Tran-Gyamfi,M., Tsai,M.,
            Ulanovsky,L.E., Ustaszewska,A., Vo,N., White,P.S., Williams,A.L.,
            Wills,P.L., Wu,J.R., Wu,K., Yang,J., Dejong,P., Bruce,D.,
            Doggett,N.A., Deaven,L., Schmutz,J., Grimwood,J., Richardson,P.,
            Rokhsar,D.S., Eichler,E.E., Gilna,P., Lucas,S.M., Myers,R.M.,
            Rubin,E.M. and Pennacchio,L.A.
  TITLE     The sequence and analysis of duplication-rich human chromosome 16
  JOURNAL   Nature 432 (7020), 988-994 (2004)
   PUBMED   15616553
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            Z97653.14 and Z92544.1.
            
            On Feb 27, 2010 this sequence version replaced NP_699181.1.
            
            Summary: Members of the F-box protein family, such as FBXL16, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC036680.2 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397621.6/ ENSP00000380746.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..479
                     /product="F-box/LRR-repeat protein 16"
                     /calculated_mol_wt=51527
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Site            92
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2RT62; propagated from
                     UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          95..136
                     /region_name="F-box_FBXL16"
                     /note="F-box domain found in F-box/LRR-repeat protein 16
                     (FBXL16) and similar proteins; cd22127"
                     /db_xref="CDD:438899"
     Site            order(97,101,104..105,108..109,113,115..116,120..122,124)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438899"
     Region          201..413
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          220..243
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          244..269
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          244..266
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          267..290
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          270..295
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          296..321
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          319..343
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          322..347
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          345..369
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          348..373
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          371..395
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          374..398
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          396..420
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     Region          446..470
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N461.2)"
     CDS             1..479
                     /gene="FBXL16"
                     /gene_synonym="C16orf22; c380A1.1; Fbl16"
                     /coded_by="NM_153350.4:305..1744"
                     /db_xref="CCDS:CCDS10421.1"
                     /db_xref="GeneID:146330"
                     /db_xref="HGNC:HGNC:14150"
                     /db_xref="MIM:609082"
ORIGIN      
        1 msspgidgdp kppclprngl vklpgqpngl gaasitkgtp atknrpcqpp ppptlpppsl
       61 aaplsraala ggpctpaggp asalapghpa erpplatdek ilnglfwyfs acekcvlaqv
      121 ckawrrvlyq pkfwagltpv lhakelynvl pggekefvnl qgfaargfeg fclvgvsdld
      181 icefidnyal skkgvkamsl krstitdagl evmleqmqgv vrlelsgcnd fteaglwssl
      241 saritslsvs dcinvaddai aaisqllpnl aelslqayhv tdtalayfta rqghsthtlr
      301 llscweitnh gvvnvvhslp nltalslsgc skvtddgvel vaenlrklrs ldlswcprit
      361 dmaleyvacd lhrleelvld rcvritdtgl sylstmsslr slylrwccqv qdfglkhlla
      421 lgslrllsla gcplltttgl sglvqlqele eleltncpga tpelfkyfsq hlprclvie
//
LOCUS       NP_002431                936 aa            linear   PRI 20-NOV-2025
DEFINITION  mutS protein homolog 4 [Homo sapiens].
ACCESSION   NP_002431
VERSION     NP_002431.2
DBSOURCE    REFSEQ: accession NM_002440.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 936)
  AUTHORS   Chen,L. and Weir,J.R.
  TITLE     The molecular machinery of meiotic recombination
  JOURNAL   Biochem Soc Trans 52 (1), 379-393 (2024)
   PUBMED   38348856
  REMARK    Review article
REFERENCE   2  (residues 1 to 936)
  AUTHORS   Hashemi Sheikhshabani,S., Ghafouri-Fard,S., Hosseini,E. and
            Omrani,M.D.
  TITLE     A novel homozygote nonsense variant of MSH4 leads to primary
            ovarian insufficiency and non-obstructive azoospermia
  JOURNAL   Mol Biol Rep 51 (1), 68 (2024)
   PUBMED   38175272
  REMARK    GeneRIF: A novel homozygote nonsense variant of MSH4 leads to
            primary ovarian insufficiency and non-obstructive azoospermia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 936)
  AUTHORS   Wan,Y., Hong,Z., Ma,B., He,X., Ma,L., Wang,M. and Zhang,Y.
  TITLE     Identification of compound heterozygous variants in MSH4 as a novel
            genetic cause of diminished ovarian reserve
  JOURNAL   Reprod Biol Endocrinol 21 (1), 76 (2023)
   PUBMED   37620942
  REMARK    GeneRIF: Identification of compound heterozygous variants in MSH4
            as a novel genetic cause of diminished ovarian reserve.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 936)
  AUTHORS   Li,P., Ji,Z., Zhi,E., Zhang,Y., Han,S., Zhao,L., Tian,R., Chen,H.,
            Huang,Y., Zhang,J., Chen,H., Zhao,F., Zhou,Z., Li,Z. and Yao,C.
  TITLE     Novel bi-allelic MSH4 variants causes meiotic arrest and
            non-obstructive azoospermia
  JOURNAL   Reprod Biol Endocrinol 20 (1), 21 (2022)
   PUBMED   35090489
  REMARK    GeneRIF: Novel bi-allelic MSH4 variants causes meiotic arrest and
            non-obstructive azoospermia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 936)
  AUTHORS   Wyrwoll,M.J., van Walree,E.S., Hamer,G., Rotte,N., Motazacker,M.M.,
            Meijers-Heijboer,H., Alders,M., Meissner,A., Kaminsky,E., Woste,M.,
            Krallmann,C., Kliesch,S., Hunt,T.J., Clark,A.T., Silber,S.,
            Stallmeyer,B., Friedrich,C., van Pelt,A.M.M., Mathijssen,I.B. and
            Tuttelmann,F.
  TITLE     Bi-allelic variants in DNA mismatch repair proteins MutS Homolog
            MSH4 and MSH5 cause infertility in both sexes
  JOURNAL   Hum Reprod 37 (1), 178-189 (2021)
   PUBMED   34755185
  REMARK    GeneRIF: Bi-allelic variants in DNA mismatch repair proteins MutS
            Homolog MSH4 and MSH5 cause infertility in both sexes.
REFERENCE   6  (residues 1 to 936)
  AUTHORS   Santucci-Darmanin,S., Walpita,D., Lespinasse,F., Desnuelle,C.,
            Ashley,T. and Paquis-Flucklinger,V.
  TITLE     MSH4 acts in conjunction with MLH1 during mammalian meiosis
  JOURNAL   FASEB J 14 (11), 1539-1547 (2000)
   PUBMED   10928988
REFERENCE   7  (residues 1 to 936)
  AUTHORS   Kneitz,B., Cohen,P.E., Avdievich,E., Zhu,L., Kane,M.F., Hou,H. Jr.,
            Kolodner,R.D., Kucherlapati,R., Pollard,J.W. and Edelmann,W.
  TITLE     MutS homolog 4 localization to meiotic chromosomes is required for
            chromosome pairing during meiosis in male and female mice
  JOURNAL   Genes Dev 14 (9), 1085-1097 (2000)
   PUBMED   10809667
REFERENCE   8  (residues 1 to 936)
  AUTHORS   Bocker,T., Barusevicius,A., Snowden,T., Rasio,D., Guerrette,S.,
            Robbins,D., Schmidt,C., Burczak,J., Croce,C.M., Copeland,T.,
            Kovatich,A.J. and Fishel,R.
  TITLE     hMSH5: a human MutS homologue that forms a novel heterodimer with
            hMSH4 and is expressed during spermatogenesis
  JOURNAL   Cancer Res 59 (4), 816-822 (1999)
   PUBMED   10029069
REFERENCE   9  (residues 1 to 936)
  AUTHORS   Winand,N.J., Panzer,J.A. and Kolodner,R.D.
  TITLE     Cloning and characterization of the human and Caenorhabditis
            elegans homologs of the Saccharomyces cerevisiae MSH5 gene
  JOURNAL   Genomics 53 (1), 69-80 (1998)
   PUBMED   9787078
REFERENCE   10 (residues 1 to 936)
  AUTHORS   Paquis-Flucklinger,V., Santucci-Darmanin,S., Paul,R., Saunieres,A.,
            Turc-Carel,C. and Desnuelle,C.
  TITLE     Cloning and expression analysis of a meiosis-specific MutS homolog:
            the human MSH4 gene
  JOURNAL   Genomics 44 (2), 188-194 (1997)
   PUBMED   9299235
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB077677.1, AF104243.1,
            BC033030.1 and AL445464.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 29, 2003 this sequence version replaced NP_002431.1.
            
            Summary: This gene encodes a member of the DNA mismatch repair mutS
            family. This member is a meiosis-specific protein that is not
            involved in DNA mismatch correction, but is required for reciprocal
            recombination and proper segregation of homologous chromosomes at
            meiosis I. This protein and MSH5 form a heterodimer which binds
            uniquely to a Holliday Junction and its developmental progenitor,
            thus provoking ADP-ATP exchange, and stabilizing the interaction
            between parental chromosomes during meiosis double-stranded break
            repair. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033030.1, U89293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263187.4/ ENSP00000263187.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..936
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..936
                     /product="mutS protein homolog 4"
                     /note="hMSH4"
                     /calculated_mol_wt=104625
     Region          1..83
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15457.2)"
     Region          103..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15457.2)"
     Region          157..864
                     /region_name="MutS"
                     /note="DNA mismatch repair ATPase MutS [Replication,
                     recombination and repair]; COG0249"
                     /db_xref="CDD:440019"
     CDS             1..936
                     /gene="MSH4"
                     /gene_synonym="ASG; POF20; SPGF2"
                     /coded_by="NM_002440.4:105..2915"
                     /db_xref="CCDS:CCDS670.1"
                     /db_xref="GeneID:4438"
                     /db_xref="HGNC:HGNC:7327"
                     /db_xref="MIM:602105"
ORIGIN      
        1 mlrpeissts psapavspss getrspqgpr ynfglqetpq srpsvqvvsa stcpgtsgaa
       61 gdrssssssl pcpapnsrpa qgsyfgnkra yaentvasnf tfgassssar dtnypqtlkt
      121 plstgnpqrs gykswtpqvg ysassssais ahspsvivav vegrglarge igmasidlkn
      181 pqiilsqfad nttyakvitk lkilspleii msntacavgn stklftlite nfknvnftti
      241 qrkyfnetkg leyieqlcia efstvlmevq skyyclaava allkyvefiq nsvyapkslk
      301 icfqgseqta midsssaqnl ellinnqdyr nnhtlfgvln ytktpggsrr lrsnileplv
      361 dietinmrld cvqellqdee lffglqsvis rfldteqlls vlvqipkqdt vnaaeskitn
      421 liylkhtlel vdplkiamkn cntpllrayy gsledkrfgi ilekiktvin ddarymkgcl
      481 nmrtqkcyav rsninefldi arrtyteivd diagmisqlg ekyslplrts fssargffiq
      541 mttdcialps dqlpsefiki skvknsysft sadlikmner cqeslreiyh mtymivckll
      601 seiyehihcl yklsdtvsml dmllsfahac tlsdyvrpef tdtlaikqgw hpilekisae
      661 kpianntyvt egsnfliitg pnmsgkstyl kqialcqima qigsyvpaey ssfriakqif
      721 tristdddie tnsstfmkem keiayilhna ndkslilide lgrgtnteeg igicyavcey
      781 llslkaftlf athflelchi dalypnvenm hfevqhvknt srnkeailyt yklskgltee
      841 knyglkaaev sslppsivld akeittqitr qilqnqrstp emerqravyh latrlvqtar
      901 nsqldpdslr iylsnlkkky kedfprteqv pektee
//
LOCUS       NP_001353581            1461 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 1 [Homo sapiens].
ACCESSION   NP_001353581 XP_006714896
VERSION     NP_001353581.1
DBSOURCE    REFSEQ: accession NM_001366652.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1461)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1461)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 1461)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 1461)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 1461)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 1461)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 1461)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 1461)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 1461)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 1461)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091928.3, AC011363.6, AC008456.6 and AC008388.7.
            
            On Oct 13, 2018 this sequence version replaced XP_006714896.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.163130.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..1461
                     /product="phospholipid-transporting ATPase VB isoform 1"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=165260
     Region          68..1213
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            83..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            111..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            317..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            369..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            order(433..435,766,790..792,868,915..917,1029,1032,1035,
                     1055,1058)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            433..439
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319770"
     Site            433
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319770"
     Region          496..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          640..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1112..1132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1145..1164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1195..1216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1224..1246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1253..1273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1292..1316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          1346..1397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     CDS             1..1461
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001366652.1:486..4871"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43394.1"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 malsvdsswh rwqwrvrdgf phcpsettpl lspekgrqsy nltqqrvvfp nnsifhqdwe
       61 evsrrypgnr tcttkytlft flprnlfeqf hrwanlyflf lvilnwmpsm evfhreitml
      121 plaivlfvim ikdgmedfkr hrfdkaincs niriyerkeq tyvqkcwkdv rvgdfiqmkc
      181 neivpadill lfssdpngic hletasldge tnlkqrcvvk gfsqqevqfe pelfhntivc
      241 ekpnnhlnkf kgymehpdqt rtgfgcesll lrgctirnte mavgiviyag hetkamlnns
      301 gprykrskie rrmnidiffc igililmcli gavghsiwng tfeehppfdv pdangsflps
      361 alggfymflt miillqvlip islyvsielv klgqvfflsn dldlydeetd lsiqcralni
      421 aedlgqiqyi fsdktgtlte nkmvfrrcti mgseyshqen akrletpkel dsdgeewtqy
      481 qclsfsarwa qdpatmrsqk gaqplrrsqs arvpiqghyr qrsmghress qppvafsssi
      541 ekdvtpdknl ltkvrdaalw letlsdsrpa kaslsttssi adfflaltic nsvmvsttte
      601 prqrvtikps skalgtslek iqqlfqklkl lslsqsfsst apsdtdlges lganvattds
      661 derddasvcs ggdstddggy rssmwdqgdi lesgsgtsle ealeapatdl arpefcyeae
      721 spdeaalvha ahaysftlvs rtpeqvtvrl pqgtcltfsl lctlgfdsvr krmsvvvrhp
      781 ltgeivvytk gadsvimdll edpacvpdin mekklrkira rtqkhldlya rdglrtlcia
      841 kkvvseedfr rwasfrreae asldnrdell metaqhlenq ltllgatgie drlqegvpdt
      901 iatlreagiq lwvltgdkqe tavniahscr llnqtdtvyt intenqetce silncaleel
      961 kqfrelqkpd rklfgfrlps ktpsitseav vpeaglvidg ktlnaifqgk lekkfleltq
     1021 ycrsvlccrs tplqksmivk lvrdklrvmt lsigdgandv smiqaadigi gisgqegmqa
     1081 vmssdfaitr fkhlkklllv hghwcysrla rmvvyylykn vcyvnllfwy qffcgfssst
     1141 midywqmiff nlfftslppl vfgvldkdis aetllalpel yksgqnsecy nlstfwismv
     1201 dafyqslicf fipylaykgs didvftfgtp intislttil lhqamemktw tifhgvvllg
     1261 sflmyflvsl lynatcvicn sptnpywvme gqlsnptfyl vcfltpvval lpryfflslq
     1321 gtcgkslisk aqkidklppd krnleiqswr srqrpapvpe varpthhpvs sitgqdfsas
     1381 tpkssnppkr khveesvlhe qrcgtecmrd dscsgdssaq lssgehllgp nrimaysrgq
     1441 tdmcrcskrs shrrsqsslt i
//
LOCUS       NP_000824               1464 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate receptor ionotropic, NMDA 2A isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_000824
VERSION     NP_000824.1
DBSOURCE    REFSEQ: accession NM_000833.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Korinek,M., Candelas Serra,M., Abdel Rahman,F., Dobrovolski,M.,
            Kuchtiak,V., Abramova,V., Fili,K., Tomovic,E., Hrcka Krausova,B.,
            Krusek,J., Cerny,J., Vyklicky,L., Balik,A. and Smejkalova,T.
  TITLE     Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B genes:
            Insights into NMDA Receptor Structure, Function, and
            Pathophysiology
  JOURNAL   Physiol Res 73 (Suppl 1), S413-S434 (2024)
   PUBMED   38836461
  REMARK    GeneRIF: Disease-Associated Variants in GRIN1, GRIN2A and GRIN2B
            genes: Insights into NMDA Receptor Structure, Function, and
            Pathophysiology.
            Review article
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Raich,I., Lillo,J., Rebassa,J.B., Capo,T., Cordomi,A.,
            Reyes-Resina,I., Pallas,M. and Navarro,G.
  TITLE     Dual Role of NMDAR Containing NR2A and NR2B Subunits in Alzheimer's
            Disease
  JOURNAL   Int J Mol Sci 25 (9), 4757 (2024)
   PUBMED   38731978
  REMARK    GeneRIF: Dual Role of NMDAR Containing NR2A and NR2B Subunits in
            Alzheimer's Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Xu,Y., Song,R., Perszyk,R.E., Chen,W., Kim,S., Park,K.L.,
            Allen,J.P., Nocilla,K.A., Zhang,J., XiangWei,W., Tankovic,A.,
            McDaniels,E.D., Sheikh,R., Mizu,R.K., Karamchandani,M.M., Hu,C.,
            Kusumoto,H., Pecha,J., Cappuccio,G., Gaitanis,J., Sullivan,J.,
            Shashi,V., Petrovski,S., Jauss,R.T., Lee,H.K., Bozarth,X.,
            Lynch,D.R., Helbig,I., Pierson,T.M., Boerkoel,C.F., Myers,S.J.,
            Lemke,J.R., Benke,T.A., Yuan,H. and Traynelis,S.F.
  TITLE     De novo GRIN variants in M3 helix associated with neurological
            disorders control channel gating of NMDA receptor
  JOURNAL   Cell Mol Life Sci 81 (1), 153 (2024)
   PUBMED   38538865
  REMARK    GeneRIF: De novo GRIN variants in M3 helix associated with
            neurological disorders control channel gating of NMDA receptor.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Lu,W., Yang,X., Zhong,W., Chen,G., Guo,X., Ye,Q., Xu,Y., Qi,Z.,
            Ye,Y., Zhang,J., Wang,Y., Wang,X., Wang,S., Zhao,Q., Zeng,W.,
            Huang,J., Ma,H. and Xie,J.
  TITLE     METTL14-mediated m6A epitranscriptomic modification contributes to
            chemotherapy-induced neuropathic pain by stabilizing GluN2A
            expression via IGF2BP2
  JOURNAL   J Clin Invest 134 (6), e174847 (2024)
   PUBMED   38319733
  REMARK    GeneRIF: METTL14-mediated m6A epitranscriptomic modification
            contributes to chemotherapy-induced neuropathic pain by stabilizing
            GluN2A expression via IGF2BP2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Shepard,N., Baez-Nieto,D., Iqbal,S., Kurganov,E., Budnik,N.,
            Campbell,A.J., Pan,J.Q., Sheng,M. and Farsi,Z.
  TITLE     Differential functional consequences of GRIN2A mutations associated
            with schizophrenia and neurodevelopmental disorders
  JOURNAL   Sci Rep 14 (1), 2798 (2024)
   PUBMED   38307912
  REMARK    GeneRIF: Differential functional consequences of GRIN2A mutations
            associated with schizophrenia and neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Magnuson,D.S., Knudsen,B.E., Geiger,J.D., Brownstone,R.M. and
            Nath,A.
  TITLE     Human immunodeficiency virus type 1 tat activates
            non-N-methyl-D-aspartate excitatory amino acid receptors and causes
            neurotoxicity
  JOURNAL   Ann Neurol 37 (3), 373-380 (1995)
   PUBMED   7695237
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Sokolov,B.P. and Prockop,D.J.
  TITLE     A rapid and simple PCR-based method for isolation of cDNAs from
            differentially expressed genes
  JOURNAL   Nucleic Acids Res 22 (19), 4009-4015 (1994)
   PUBMED   7524031
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Strehlow,V., Myers,K.A., Morgan,A.T., Scheffer,I.E. and Lemke,J.R.
  TITLE     GRIN2A-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27683935
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Monyer,H., Sprengel,R., Schoepfer,R., Herb,A., Higuchi,M.,
            Lomeli,H., Burnashev,N., Sakmann,B. and Seeburg,P.H.
  TITLE     Heteromeric NMDA receptors: molecular and functional distinction of
            subtypes
  JOURNAL   Science 256 (5060), 1217-1221 (1992)
   PUBMED   1350383
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022168.6, U90277.1, U09002.1,
            AC006531.1 and AC007218.6.
            
            Summary: This gene encodes a member of the glutamate-gated ion
            channel protein family. The encoded protein is an
            N-methyl-D-aspartate (NMDA) receptor subunit. NMDA receptors are
            both ligand-gated and voltage-dependent, and are involved in
            long-term potentiation, an activity-dependent increase in the
            efficiency of synaptic transmission thought to underlie certain
            kinds of memory and learning. These receptors are permeable to
            calcium ions, and activation results in a calcium influx into
            post-synaptic cells, which results in the activation of several
            signaling cascades. Disruption of this gene is associated with
            focal epilepsy and speech disorder with or without cognitive
            disability. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Transcript variants 1 and 2 encode the same
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U90277.1, SRR14038192.2603991.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.2"
     Protein         1..1464
                     /product="glutamate receptor ionotropic, NMDA 2A isoform 1
                     precursor"
                     /note="N-methyl-D-aspartate receptor channel, subunit
                     epsilon-1; N-methyl-D-aspartate receptor subunit 2A;
                     N-methyl D-aspartate receptor subtype 2A; glutamate
                     receptor, ionotropic, N-methyl D-aspartate 2A; glutamate
                     receptor ionotropic, NMDA 2A; glutamate ionotropic
                     receptor NMDA 2A"
                     /calculated_mol_wt=162435
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2866
     Region          32..387
                     /region_name="PBP1_iGluR_NMDA_NR2"
                     /note="N-terminal leucine-isoleucine-valine-binding
                     protein (LIVBP)-like domain of the NR2 subunit of NMDA
                     receptor family; cd06378"
                     /db_xref="CDD:380601"
     Site            order(32,78..80,115,136,176,178,193,208..209,310..311)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Site            order(76..81,83..84,119..120,176,180,207,209,310..316,
                     320..322,333)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:380601"
     Region          403..802
                     /region_name="PBP2_iGluR_NMDA_Nr2"
                     /note="The ligand-binding domain of the NR2 subunit of
                     ionotropic NMDA (N-methyl-D-aspartate) glutamate
                     receptors, a member of the type 2 periplasmic binding fold
                     protein superfamily; cd13718"
                     /db_xref="CDD:270436"
     Site            order(511..514,516,518..520,666,688..689,693,731,756..758,
                     761,767,783..786,789)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:270436"
     Site            order(511..513,518,688..690,730..731)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270436"
     Region          839..1464
                     /region_name="NMDAR2_C"
                     /note="N-methyl D-aspartate receptor 2B3 C-terminus;
                     pfam10565"
                     /db_xref="CDD:463148"
     CDS             1..1464
                     /gene="GRIN2A"
                     /gene_synonym="EPND; FESD; GluN2A; LKS; NMDAR2A; NR2A"
                     /coded_by="NM_000833.5:465..4859"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS10539.1"
                     /db_xref="GeneID:2903"
                     /db_xref="HGNC:HGNC:4585"
                     /db_xref="MIM:138253"
ORIGIN      
        1 mgrvgywtll vlpallvwrg papsaaaekg ppalniavml ghshdvtere lrtlwgpeqa
       61 aglpldvnvv allmnrtdpk slithvcdlm sgarihglvf gddtdqeava qmldfissht
      121 fvpilgihgg asmimadkdp tstffqfgas iqqqatvmlk imqdydwhvf slvttifpgy
      181 refisfvktt vdnsfvgwdm qnvitldtsf edaktqvqlk kihssvilly cskdeavlil
      241 searslgltg ydffwivpsl vsgntelipk efpsglisvs yddwdyslea rvrdgigilt
      301 taassmlekf syipeakasc ygqmerpevp mhtlhpfmvn vtwdgkdlsf teegyqvhpr
      361 lvvivlnkdr ewekvgkwen htlslrhavw pryksfsdce pddnhlsivt leeapfvive
      421 didpltetcv rntvpcrkfv kinnstnegm nvkkcckgfc idilkklsrt vkftydlylv
      481 tngkhgkkvn nvwngmigev vyqravmavg sltineerse vvdfsvpfve tgisvmvsrs
      541 ngtvspsafl epfsasvwvm mfvmllivsa iavfvfeyfs pvgynrnlak gkaphgpsft
      601 igkaiwllwg lvfnnsvpvq npkgttskim vsvwaffavi flasytanla afmiqeefvd
      661 qvtglsdkkf qrphdysppf rfgtvpngst ernirnnypy mhqymtkfnq kgvedalvsl
      721 ktgkldafiy daavlnykag rdegcklvti gsgyifattg ygialqkgsp wkrqidlall
      781 qfvgdgemee letlwltgic hneknevmss qldidnmagv fymlaaamal slitfiwehl
      841 fywklrfcft gvcsdrpgll fsisrgiysc ihgvhieekk kspdfnltgs qsnmlkllrs
      901 aknissmsnm nssrmdspkr aadfiqrgsl imdmvsdkgn lmysdnrsfq gkesifgdnm
      961 nelqtfvanr qkdnlnnyvf qgqhpltlne snpntvevav steskansrp rqlwkksvds
     1021 irqdslsqnp vsqrdeatae nrthslkspr ylpeemahsd isetsnratc hrepdnsknh
     1081 ktkdnfkrsv askypkdcse vertylktks ssprdkiyti dgekepgfhl dppqfvenvt
     1141 lpenvdfpdp yqdpsenfrk gdstlpmnrn plhneeglsn ndqyklyskh ftlkdkgsph
     1201 setseryrqn sthcrsclsn mptysghftm rspfkcdacl rmgnlydide dqmlqetgnp
     1261 atgeqvyqqd waqnnalqlq knklrisrqh sydnivdkpr eldlsrpsrs islkdrerll
     1321 egnfygslfs vpssklsgkk sslfpqgled skrsksllpd htsdnpflhs hrddqrlvig
     1381 rcpsdpykhs lpsqavndsy lrsslrstas ycsrdsrghn dvyisehvmp yaanknnmys
     1441 tprvlnscsn rrvykkmpsi esdv
//
LOCUS       NP_003090                522 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-1 isoform a [Homo sapiens].
ACCESSION   NP_003090
VERSION     NP_003090.2
DBSOURCE    REFSEQ: accession NM_003099.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Garcia Delgado,L., Derome,A., Longpre,S., Giroux-Dansereau,M.,
            Basbous,G., Lavoie,C., Saucier,C. and Denault,J.B.
  TITLE     Spatiotemporal regulation of the hepatocyte growth factor receptor
            MET activity by sorting nexins 1/2 in HCT116 colorectal cancer
            cells
  JOURNAL   Biosci Rep 44 (6) (2024)
   PUBMED   38836326
  REMARK    GeneRIF: Spatiotemporal regulation of the hepatocyte growth factor
            receptor MET activity by sorting nexins 1/2 in HCT116 colorectal
            cancer cells.
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Lopez-Robles,C., Scaramuzza,S., Astorga-Simon,E.N., Ishida,M.,
            Williamson,C.D., Banos-Mateos,S., Gil-Carton,D., Romero-Durana,M.,
            Vidaurrazaga,A., Fernandez-Recio,J., Rojas,A.L., Bonifacino,J.S.,
            Castano-Diez,D. and Hierro,A.
  TITLE     Architecture of the ESCPE-1 membrane coat
  JOURNAL   Nat Struct Mol Biol 30 (7), 958-969 (2023)
   PUBMED   37322239
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Sugatha,J., Priya,A., Raj,P., Jaimon,E., Swaminathan,U., Jose,A.,
            Pucadyil,T.J. and Datta,S.
  TITLE     Insights into cargo sorting by SNX32 and its role in neurite
            outgrowth
  JOURNAL   Elife 12, e84396 (2023)
   PUBMED   37158588
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Carlton,J., Bujny,M., Peter,B.J., Oorschot,V.M., Rutherford,A.,
            Mellor,H., Klumperman,J., McMahon,H.T. and Cullen,P.J.
  TITLE     Sorting nexin-1 mediates tubular endosome-to-TGN transport through
            coincidence sensing of high- curvature membranes and
            3-phosphoinositides
  JOURNAL   Curr Biol 14 (20), 1791-1800 (2004)
   PUBMED   15498486
  REMARK    GeneRIF: SNX1 associates with a microdomain of the early endosome
            where it regulates tubular-based endosome-to-trans Golgi network
            retrieval of the cation-independent mannose-6-phosphate receptor.
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Shank,B.B., Wiley,H.S. and Kurten,R.C.
  TITLE     Structural and functional characterization of the human gene for
            sorting nexin 1 (SNX1)
  JOURNAL   DNA Cell Biol 20 (5), 287-296 (2001)
   PUBMED   11410165
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Kurten,R.C., Eddington,A.D., Chowdhury,P., Smith,R.D.,
            Davidson,A.D. and Shank,B.B.
  TITLE     Self-assembly and binding of a sorting nexin to sorting endosomes
  JOURNAL   J Cell Sci 114 (Pt 9), 1743-1756 (2001)
   PUBMED   11309204
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Chin,L.S., Raynor,M.C., Wei,X., Chen,H.Q. and Li,L.
  TITLE     Hrs interacts with sorting nexin 1 and regulates degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 276 (10), 7069-7078 (2001)
   PUBMED   11110793
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Barr,V.A., Haft,D.H. and
            Taylor,S.I.
  TITLE     Identification of a family of sorting nexin molecules and
            characterization of their association with receptors
  JOURNAL   Mol Cell Biol 18 (12), 7278-7287 (1998)
   PUBMED   9819414
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Kurten,R.C., Cadena,D.L. and Gill,G.N.
  TITLE     Enhanced degradation of EGF receptors by a sorting nexin, SNX1
  JOURNAL   Science 272 (5264), 1008-1010 (1996)
   PUBMED   8638121
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455188.1, AK291752.1,
            AC100840.2 and BX108623.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 18, 2002 this sequence version replaced NP_003090.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This endosomal protein regulates the cell-surface
            expression of epidermal growth factor receptor. This protein also
            has a role in sorting protease-activated receptor-1 from early
            endosomes to lysosomes. This protein may form oligomeric complexes
            with family members. This gene results in three transcript variants
            encoding distinct isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.160542.1,
                                           SRR1803614.174871.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000559844.6/ ENSP00000453785.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..522
                     /product="sorting nexin-1 isoform a"
                     /note="sorting nexin 1A"
                     /calculated_mol_wt=58939
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          11..90
                     /region_name="Sorting_nexin"
                     /note="Sorting nexin, N-terminal domain; pfam03700"
                     /db_xref="CDD:461016"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV80; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV80; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Region          115..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          145..268
                     /region_name="PX_SNX1"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 1; cd07281"
                     /db_xref="CDD:132814"
     Site            order(186..188,238)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132814"
     Site            188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Site            237
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13596.3)"
     Region          281..298
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000303|PubMed:19816406"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13596.3)"
     Region          286..519
                     /region_name="BAR_SNX1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 1; cd07665"
                     /db_xref="CDD:153349"
     Site            order(315,318..319,322..323,325..326,329,332..333,336,
                     343..344,346..347,350,353..354,357..358,374,479,482..483,
                     485..487,490,493..494,496..498,500..501,504..505,507..508,
                     511..512,514..515)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153349"
     CDS             1..522
                     /gene="SNX1"
                     /gene_synonym="HsT17379; VPS5"
                     /coded_by="NM_003099.5:33..1601"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32266.1"
                     /db_xref="GeneID:6642"
                     /db_xref="HGNC:HGNC:11172"
                     /db_xref="MIM:601272"
ORIGIN      
        1 masggggcsa serlpppfpg lepesegaag gsepeagdsd tegediftga avvskhqspk
       61 ittsllpinn gskengihee qdqepqdlfa datvelslds tqnnqkkvla ktlislppqe
      121 atnsskpqpt yeeleeeeqe dqfdltvgit dpekigdgmn ayvaykvttq tslplfrskq
      181 favkrrfsdf lglyeklsek hsqngfivpp ppeksligmt kvkvgkedss saeflekrra
      241 alerylqriv nhptmlqdpd vreflekeel pravgtqtls gagllkmfnk atdavskmti
      301 kmnesdiwfe eklqevecee qrlrklhavv etlvnhrkel alntaqfaks lamlgssedn
      361 talsralsql aeveekieql hqeqanndff llaellsdyi rllaivraaf dqrmktwqrw
      421 qdaqatlqkk reaearllwa nkpdklqqak deilewesrv tqyerdferi stvvrkevir
      481 fekekskdfk nhvikyletl lysqqqlaky weaflpeaka is
//
LOCUS       NP_001291411            1510 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 23 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001291411 XP_005265090
VERSION     NP_001291411.1
DBSOURCE    REFSEQ: accession NM_001304482.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1510)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1510)
  AUTHORS   Niu,S., Ma,J., Li,Y., Yue,X., Shi,K., Pan,M., Song,L., Tan,Y.,
            Gu,L., Liu,S. and Chang,J.
  TITLE     PTPN23[Thr] variant reduces susceptibility and tumorigenesis in
            esophageal squamous cell carcinoma through dephosphorylation of
            EGFR
  JOURNAL   Cancer Lett 592, 216936 (2024)
   PUBMED   38704135
  REMARK    GeneRIF: PTPN23[Thr] variant reduces susceptibility and
            tumorigenesis in esophageal squamous cell carcinoma through
            dephosphorylation of EGFR.
REFERENCE   3  (residues 1 to 1510)
  AUTHORS   Singh,S., Yeat,N.Y., Wang,Y.T., Lin,S.Y., Kuo,I.Y., Wu,K.P.,
            Wang,W.J., Wang,W.C., Su,W.C., Wang,Y.C. and Chen,R.H.
  TITLE     PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET degradation
            to define a lung cancer therapeutic target
  JOURNAL   Cell Death Dis 14 (10), 671 (2023)
   PUBMED   37821451
  REMARK    GeneRIF: PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET
            degradation to define a lung cancer therapeutic target.
            Erratum:[Cell Death Dis. 2024 Jul 2;15(7):468. doi:
            10.1038/s41419-024-06747-x. PMID: 38956428]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1510)
  AUTHORS   Pashkova,N., Yu,L., Schnicker,N.J., Tseng,C.C., Gakhar,L.,
            Katzmann,D.J. and Piper,R.C.
  TITLE     Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP
            reveals role for regulation of Vps4 ATPase
  JOURNAL   Mol Biol Cell 32 (22), ar42 (2021)
   PUBMED   34586919
  REMARK    GeneRIF: Interactions of ubiquitin and CHMP5 with the V domain of
            HD-PTP reveals role for regulation of Vps4 ATPase.
REFERENCE   5  (residues 1 to 1510)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1510)
  AUTHORS   Castiglioni,S., Maier,J.A. and Mariotti,M.
  TITLE     The tyrosine phosphatase HD-PTP: A novel player in endothelial
            migration
  JOURNAL   Biochem Biophys Res Commun 364 (3), 534-539 (2007)
   PUBMED   17959146
  REMARK    GeneRIF: We suggest that HD-PTP contributes to the regulation of
            endothelial motility by modulating the tyrosine phosphorylation of
            FAK.
REFERENCE   7  (residues 1 to 1510)
  AUTHORS   Ichioka,F., Takaya,E., Suzuki,H., Kajigaya,S., Buchman,V.L.,
            Shibata,H. and Maki,M.
  TITLE     HD-PTP and Alix share some membrane-traffic related proteins that
            interact with their Bro1 domains or proline-rich regions
  JOURNAL   Arch Biochem Biophys 457 (2), 142-149 (2007)
   PUBMED   17174262
REFERENCE   8  (residues 1 to 1510)
  AUTHORS   Mariotti,M., Castiglioni,S., Beguinot,L. and Maier,J.A.
  TITLE     The tyrosine phosphatase HD-PTP is regulated by FGF-2 through
            proteasome degradation
  JOURNAL   Front Biosci 11, 2138-2143 (2006)
   PUBMED   16720300
  REMARK    GeneRIF: data suggest that HD-PTP might participate in modulating
            endothelial response to angiogenic factors and play a role in
            regulating the complex events leading to the formation of new
            vessels
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1510)
  AUTHORS   Mariotti,M., Castiglioni,S. and Maier,J.A.
  TITLE     Expression analysis and modulation by HIV-Tat of the tyrosine
            phosphatase HD-PTP
  JOURNAL   J Cell Biochem 98 (2), 301-308 (2006)
   PUBMED   16408268
  REMARK    GeneRIF: These results suggest that HD-PTP amounts might be
            regulated both at the transcriptional and post-transcriptional
            levels.
REFERENCE   10 (residues 1 to 1510)
  AUTHORS   Toyooka,S., Ouchida,M., Jitsumori,Y., Tsukuda,K., Sakai,A.,
            Nakamura,A., Shimizu,N. and Shimizu,K.
  TITLE     HD-PTP: A novel protein tyrosine phosphatase gene on human
            chromosome 3p21.3
  JOURNAL   Biochem Biophys Res Commun 278 (3), 671-678 (2000)
   PUBMED   11095967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299906.1, AF290614.1 and
            BU173747.1.
            
            On Jan 29, 2015 this sequence version replaced XP_005265090.1.
            
            Summary: This gene encodes a member of the non-receptor type
            protein-tyrosine phosphatase family. The encoded protein may be
            involved in the regulation of small nuclear ribonucleo protein
            assembly and pre-mRNA splicing by modifying the survival motor
            neuron (SMN) complex. The encoded protein additionally plays a role
            in ciliogenesis and is part of endosomal sorting complex required
            for transport (ESCRT) pathways. This gene may serve a tumor
            suppressor function. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) lacks an alternate exon in its
            5' UTR and uses a downstream start codon compared to variant 1. It
            encodes isoform 2 which has a shorter N-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299906.1, SRR14038192.3269991.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1510
                     /product="tyrosine-protein phosphatase non-receptor type
                     23 isoform 2"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase TD14; his
                     domain-containing protein tyrosine phosphatase"
                     /calculated_mol_wt=164437
     Region          <1..231
                     /region_name="BRO1_Alix_like"
                     /note="Protein-interacting Bro1-like domain of mammalian
                     Alix and related domains; cl14649"
                     /db_xref="CDD:472700"
     Site            order(2,15,18..19,63,66..67,76,79..80,210,212,214,216)
                     /site_type="other"
                     /note="putative ESCRT-III binding site"
                     /db_xref="CDD:185761"
     Region          236..574
                     /region_name="V_HD-PTP_like"
                     /note="Protein-interacting V-domain of mammalian
                     His-Domain type N23 protein tyrosine phosphatase and
                     related domains; cd09234"
                     /db_xref="CDD:185747"
     Site            order(319,378,382,385..386,545,548..549,552,555)
                     /site_type="other"
                     /note="putative YPXnL-motif binding site"
                     /db_xref="CDD:185747"
     Region          <601..957
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1117..1321
                     /region_name="PTP-N23"
                     /note="PTP-like domain of tyrosine-protein phosphatase
                     non-receptor type 23; cd14539"
                     /db_xref="CDD:350387"
     CDS             1..1510
                     /gene="PTPN23"
                     /gene_synonym="HD-PTP; HDPTP; NEDBASS; PTP-TD14"
                     /coded_by="NM_001304482.2:327..4859"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25930"
                     /db_xref="HGNC:HGNC:14406"
                     /db_xref="MIM:606584"
ORIGIN      
        1 mlgamdkrvs eegmkvscth fqcaagafay lrehfpqays vdmsrqiltl nvnlmlgqaq
       61 eclleksmld nrksflvari saqvvdyyke acralenpdt asllgriqkd wkklvqmkiy
      121 yfaavahlhm gkqaeeqqkf gervayfqsa ldklneaikl akgqpdtvqd alrftmdvig
      181 gkynsakkdn dfiyheavpa ldtlqpvkga plvkplpvnp tdpavtgpdi faklvpmaah
      241 easslyseek akllremmak iedknevldq fmdsmqldpe tvdnldaysh ippqlmekca
      301 alsvrpdtvr nlvqsmqvls gvftdveasl kdirdlleed elleqkfqea vgqagaisit
      361 skaelaevrr ewakymevhe kasftnselh ramnlhvgnl rllsgpldqv raalptpals
      421 pedkavlqnl krilakvqem rdqrvsleqq lreliqkddi taslvttdhs emkklfeeql
      481 kkydqlkvyl eqnlaaqdrv lcalteanvq yaavrrvlsd ldqkwnstlq tlvasyeaye
      541 dlmkksqegr dfyadleskv aallertqst cqareaarqq lldrelkkkp pprptapkpl
      601 lprreeseav eagdppeelr slppdmvagp rlpdtflgsa tplhfppspf psstgpgphy
      661 lsgplppgty sgptqliqpr apgphampva pgpalypapa ytpelglvpr sspqhgvvss
      721 pyvgvgpapp vaglpsappp qfsgpelama vrpatttvds iqapipshta prpnptpapp
      781 ppcfpvpppq plptpytypa gakqpipaqh hfssgipagf paprigpqpq phpqphpsqa
      841 fgpqppqqpl plqhphlfpp qapgllppqs pypyapqpgv lgqpppplht qlypgpaqdp
      901 lpahsgalpf pspgppqpph pplaygpaps trpmgpqaap ltirgpssag qstpsphlvp
      961 spapspgpgp vpprppaaep ppclrrgaaa adllssspes qhggtqspgg gqpllqptkv
     1021 daaegrrpqa lrlierdpye hperlrqlqq eleafrgqlg dvgaldtvwr elqdaqehda
     1081 rgrsiaiarc yslknrhqdv mpydsnrvvl rsgkddyina scveglspyc pplvatqapl
     1141 pgtaadfwlm vheqkvsviv mlvseaemek qkvaryfpte rgqpmvhgal slalssvrst
     1201 ethvervlsl qfrdqslkrs lvhlhfptwp elglpdspsn llrfiqevha hylhqrplht
     1261 piivhcssgv grtgafally aavqeveagn gipelpqlvr rmrqqrkhml qeklhlrfcy
     1321 eavvrhveqv lqrhgvpppc kplasasisq knhlpqdsqd lvlggdvpis siqatiakls
     1381 irppgglesp vaslpgpaep pglppaslpe stpipssspp plssplpeap qpkeeppvpe
     1441 apssgppsss lellasltpe afsldsslrg kqrmskhnfl qahngqglra trpsddplsl
     1501 ldplwtlnkt
//
LOCUS       NP_005991                448 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin alpha-4A chain isoform 1 [Homo sapiens].
ACCESSION   NP_005991
VERSION     NP_005991.1
DBSOURCE    REFSEQ: accession NM_006000.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Wan,Y., Zhou,C., Chang,X., Wu,L., Zheng,Y., Yu,J., Bai,L., Luan,M.,
            Yu,M., Wang,Q., Zhang,W., Yuan,Y., Deng,J. and Wang,Z.
  TITLE     Novel TUBA4A variant causes congenital myopathy with focal
            myofibrillar disorganisation
  JOURNAL   J Med Genet 61 (7), 626-632 (2024)
   PUBMED   38413182
  REMARK    GeneRIF: Novel TUBA4A variant causes congenital myopathy with focal
            myofibrillar disorganisation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Torella,A., Ricca,I., Piluso,G., Galatolo,D., De Michele,G.,
            Zanobio,M., Trovato,R., De Michele,G., Zeuli,R., Pane,C.,
            Cocozza,S., Sacca,F., Santorelli,F.M., Nigro,V. and Filla,A.
  TITLE     A new genetic cause of spastic ataxia: the p.Glu415Lys variant in
            TUBA4A
  JOURNAL   J Neurol 270 (10), 5057-5063 (2023)
   PUBMED   37418012
  REMARK    GeneRIF: A new genetic cause of spastic ataxia: the p.Glu415Lys
            variant in TUBA4A.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Ganne,A., Balasubramaniam,M., Ayyadevara,H., Kiaei,L., Shmookler
            Reis,R.J., Varughese,K.I. and Kiaei,M.
  TITLE     In silico analysis of TUBA4A mutations in Amyotrophic Lateral
            Sclerosis to define mechanisms of microtubule disintegration
  JOURNAL   Sci Rep 13 (1), 2096 (2023)
   PUBMED   36747013
  REMARK    GeneRIF: In silico analysis of TUBA4A mutations in Amyotrophic
            Lateral Sclerosis to define mechanisms of microtubule
            disintegration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Kirsch,J., Langosch,D., Prior,P., Littauer,U.Z., Schmitt,B. and
            Betz,H.
  TITLE     The 93-kDa glycine receptor-associated protein binds to tubulin
  JOURNAL   J Biol Chem 266 (33), 22242-22245 (1991)
   PUBMED   1657993
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Dobner,P.R., Kislauskis,E., Wentworth,B.M. and Villa-Komaroff,L.
  TITLE     Alternative 5' exons either provide or deny an initiator methionine
            codon to the same alpha-tubulin coding region
  JOURNAL   Nucleic Acids Res 15 (1), 199-218 (1987)
   PUBMED   3029670
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Villasante,A., Wang,D., Dobner,P., Dolph,P., Lewis,S.A. and
            Cowan,N.J.
  TITLE     Six mouse alpha-tubulin mRNAs encode five distinct isotypes:
            testis-specific expression of two sister genes
  JOURNAL   Mol Cell Biol 6 (7), 2409-2419 (1986)
   PUBMED   3785200
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Hall,J.L. and Cowan,N.J.
  TITLE     Structural features and restricted expression of a human
            alpha-tubulin gene
  JOURNAL   Nucleic Acids Res 13 (1), 207-223 (1985)
   PUBMED   3839072
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP346611.1, AK054731.1 and
            AC068946.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Microtubules of the eukaryotic cytoskeleton perform
            essential and diverse functions and are composed of a heterodimer
            of alpha and beta tubulin. The genes encoding these microtubule
            constituents are part of the tubulin superfamily, which is composed
            of six distinct families. Genes from the alpha, beta and gamma
            tubulin families are found in all eukaryotes. The alpha and beta
            tubulins represent the major components of microtubules, while
            gamma tubulin plays a critical role in the nucleation of
            microtubule assembly. There are multiple alpha and beta tubulin
            genes and they are highly conserved among and between species. This
            gene encodes an alpha tubulin that is a highly conserved homolog of
            a rat testis-specific alpha tubulin. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.148068.1,
                                           SRR3476690.544408.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248437.9/ ENSP00000248437.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..448
                     /product="tubulin alpha-4A chain isoform 1"
                     /note="tubulin, alpha 1 (testis specific); tubulin alpha-1
                     chain; tubulin H2-alpha"
                     /calculated_mol_wt=49793
     Region          1..448
                     /region_name="PTZ00335"
                     /note="tubulin alpha chain; Provisional"
                     /db_xref="CDD:185562"
     Region          1..4
                     /region_name="MREC motif.
                     /evidence=ECO:0000250|UniProtKB:P68363"
                     /note="propagated from UniProtKB/Swiss-Prot (P68366.1)"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:24906155; propagated from
                     UniProtKB/Swiss-Prot (P68366.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P68366.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9BQE3; propagated from
                     UniProtKB/Swiss-Prot (P68366.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5XIF6; propagated from
                     UniProtKB/Swiss-Prot (P68366.1)"
     CDS             1..448
                     /gene="TUBA4A"
                     /gene_synonym="ALS22; CMYO26; FTDALS9; H2-ALPHA; OZEMA23;
                     SPAX11; TUBA1"
                     /coded_by="NM_006000.3:61..1407"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2438.1"
                     /db_xref="GeneID:7277"
                     /db_xref="HGNC:HGNC:12407"
                     /db_xref="MIM:191110"
ORIGIN      
        1 mrecisvhvg qagvqmgnac welyclehgi qpdgqmpsdk tigggddsft tffcetgagk
       61 hvpravfvdl eptvideirn gpyrqlfhpe qlitgkedaa nnyarghyti gkeiidpvld
      121 rirklsdqct glqgflvfhs fgggtgsgft sllmerlsvd ygkksklefs iypapqvsta
      181 vvepynsilt thttlehsdc afmvdneaiy dicrrnldie rptytnlnrl isqivssita
      241 slrfdgalnv dltefqtnlv pyprihfpla tyapvisaek ayheqlsvae itnacfepan
      301 qmvkcdprhg kymaccllyr gdvvpkdvna aiaaiktkrs iqfvdwcptg fkvginyqpp
      361 tvvpggdlak vqravcmlsn ttaiaeawar ldhkfdlmya krafvhwyvg egmeegefse
      421 aredmaalek dyeevgidsy ededegee
//
LOCUS       NP_940916                726 aa            linear   PRI 20-NOV-2025
DEFINITION  NHL repeat-containing protein 2 [Homo sapiens].
ACCESSION   NP_940916 NP_060157 XP_350804
VERSION     NP_940916.2
DBSOURCE    REFSEQ: accession NM_198514.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Sczakiel,H.L., Zhao,M., Wollert-Wulf,B., Danyel,M., Ehmke,N.,
            Stoltenburg,C., Damseh,N., Al-Ashhab,M., Balci,T.B., Osmond,M.,
            Andrade,A., Schallner,J., Porrmann,J., McDonald,K., Liao,M.,
            Oppermann,H., Platzer,K., Dierksen,N., Mojarrad,M., Eslahi,A.,
            Bakaeean,B., Calame,D.G., Lupski,J.R., Firoozfar,Z.,
            Seyedhassani,S.M., Mohammadi,S.A., Anwaar,N., Rahman,F., Seelow,D.,
            Janz,M., Horn,D., Maroofian,R. and Boschann,F.
  TITLE     Broadening the phenotypic and molecular spectrum of FINCA syndrome:
            Biallelic NHLRC2 variants in 15 novel individuals
  JOURNAL   Eur J Hum Genet 31 (8), 905-917 (2023)
   PUBMED   37188825
  REMARK    GeneRIF: Broadening the phenotypic and molecular spectrum of FINCA
            syndrome: Biallelic NHLRC2 variants in 15 novel individuals.
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Kreus,M., Lehtonen,S., Hinttala,R., Salonen,J., Porvari,K. and
            Kaarteenaho,R.
  TITLE     NHLRC2 expression is increased in idiopathic pulmonary fibrosis
  JOURNAL   Respir Res 23 (1), 206 (2022)
   PUBMED   35964085
  REMARK    GeneRIF: NHLRC2 expression is increased in idiopathic pulmonary
            fibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Brodsky,N.N., Boyarchuk,O., Kovalchuk,T., Hariyan,T., Rice,A.,
            Ji,W., Khokha,M., Lakhani,S. and Lucas,C.L.
  TITLE     Novel compound heterozygous variants in NHLRC2 in a patient with
            FINCA syndrome
  JOURNAL   J Hum Genet 65 (10), 911-915 (2020)
   PUBMED   32435055
  REMARK    GeneRIF: Novel compound heterozygous variants in NHLRC2 in a
            patient with FINCA syndrome.
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Paakkola,T., Salokas,K., Miinalainen,I., Lehtonen,S., Manninen,A.,
            Kaakinen,M., Ruddock,L.W., Varjosalo,M., Kaarteenaho,R., Uusimaa,J.
            and Hinttala,R.
  TITLE     Biallelic mutations in human NHLRC2 enhance myofibroblast
            differentiation in FINCA disease
  JOURNAL   Hum Mol Genet 27 (24), 4288-4302 (2018)
   PUBMED   30239752
  REMARK    GeneRIF: We conclude that compound heterozygous p.Asp148Tyr and
            p.Arg201GlyfsTer6 mutations in NHLRC2 lead to severe tissue
            fibrosis in humans by enhancing the differentiation of fibroblasts
            to myofibroblasts.
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Biterova,E., Ignatyev,A., Uusimaa,J., Hinttala,R. and Ruddock,L.W.
  TITLE     Structural analysis of human NHLRC2, mutations of which are
            associated with FINCA disease
  JOURNAL   PLoS One 13 (8), e0202391 (2018)
   PUBMED   30138417
  REMARK    GeneRIF: Bioinformatics analysis discovers homologs across a range
            of eukaryotic and prokaryotic species and conserved residues map
            mostly to the adjacent surfaces of the Trx-like and beta-propeller
            domains that form the cleft, suggesting both that this forms the
            potential functional site of NHLRC2 and that the function is
            conserved across species.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Uusimaa,J., Kaarteenaho,R., Paakkola,T., Tuominen,H.,
            Karjalainen,M.K., Nadaf,J., Varilo,T., Uusi-Makela,M.,
            Suo-Palosaari,M., Pietila,I., Hiltunen,A.E., Ruddock,L., Alanen,H.,
            Biterova,E., Miinalainen,I., Salminen,A., Soininen,R., Manninen,A.,
            Sormunen,R., Kaakinen,M., Vuolteenaho,R., Herva,R., Vieira,P.,
            Dunder,T., Kokkonen,H., Moilanen,J.S., Rantala,H., Nogee,L.M.,
            Majewski,J., Ramet,M., Hallman,M. and Hinttala,R.
  TITLE     NHLRC2 variants identified in patients with fibrosis,
            neurodegeneration, and cerebral angiomatosis (FINCA):
            characterisation of a novel cerebropulmonary disease
  JOURNAL   Acta Neuropathol 135 (5), 727-742 (2018)
   PUBMED   29423877
  REMARK    GeneRIF: Study identified a novel cerebropulmonary and multi-organ
            disease characterised by a unique combination of tissue fibrosis,
            neurodegeneration and cerebral angiomatosis, and identified
            identical compound heterozygous NHLRC2 variants in three affected
            children from two unrelated families. Also created a KO mouse model
            and zebrafish morphants to investigate the consequences of absent
            or decreased Nhlrc2 expression.
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Nishi,K., Iwaihara,Y., Tsunoda,T., Doi,K., Sakata,T., Shirasawa,S.
            and Ishikura,S.
  TITLE     ROS-induced cleavage of NHLRC2 by caspase-8 leads to apoptotic cell
            death in the HCT116 human colon cancer cell line
  JOURNAL   Cell Death Dis 8 (12), 3218 (2017)
   PUBMED   29242562
  REMARK    GeneRIF: Reactive oxygen species-induced cleavage of NHLRC2 by
            caspase-8 leads to apoptotic cell death in the HCT116 human colon
            cancer cells.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK090631.1, AK098487.1, AL832090.1, BX538287.1 and AL162407.14.
            
            On or before Feb 21, 2004 this sequence version replaced
            NP_060157.2, NP_940916.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK090631.1, SRR1660803.237092.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369301.3/ ENSP00000358307.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.3"
     Protein         1..726
                     /product="NHL repeat-containing protein 2"
                     /note="1200003G01Rik; novel NHL repeat domain containing
                     protein"
                     /calculated_mol_wt=79313
     Region          <30..708
                     /region_name="PLN02919"
                     /note="haloacid dehalogenase-like hydrolase family
                     protein"
                     /db_xref="CDD:215497"
     Region          212..254
                     /region_name="NHL 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     Region          265..307
                     /region_name="NHL 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     Region          335..369
                     /region_name="NHL 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     Region          409..439
                     /region_name="NHL 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     Region          461..505
                     /region_name="NHL 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     Region          518..562
                     /region_name="NHL 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBF2.1)"
     CDS             1..726
                     /gene="NHLRC2"
                     /gene_synonym="FINCA"
                     /coded_by="NM_198514.4:213..2393"
                     /db_xref="CCDS:CCDS7585.1"
                     /db_xref="GeneID:374354"
                     /db_xref="HGNC:HGNC:24731"
                     /db_xref="MIM:618277"
ORIGIN      
        1 maapggrgrs lsgllpaqts leyalldavt qqekdslvyq ylqkvdgweq dlsvpefpeg
       61 lewlnteepi svykdlcgki vvldfftycc incihllpdl halehtysdk dglliigvhs
      121 akfpnekvld niksavlryn ithpmvndad aslwqelevs cwptlvilgp rgnmlfslig
      181 eghkdklfly tsialkyykd rgqirdnkig iklykdslpp spllfpgkvt vdqvtdrlvi
      241 adtghhrilv vwkngqiqys iggpnpgrkd gifsestfns pqgvaimnni iyvadtenhl
      301 irkidleaek vstvagigiq gtdkeggakg eqqpisspwd vvfgtsgsev qrgdilwiam
      361 agthqiwall ldsgklpkkn eltkgtclrf agsgneenrn nayphkagfa qpsglslase
      421 dpwsclfvad sesstvrtvs lkdgavkhlv ggerdpmnlf afgdvdgvgi naklqhplgv
      481 twdkkrnlly vadsynhkik vvdpktknct tlagtgdtnn vtsssftest fnepgglcig
      541 engellyvad tnnhqikvmd letkmvsvlp ifrsenavvd gpflvekqkt lpklpksaps
      601 irlspvtaca gqtlqfklrl dlpsgsklte gvsscwflta egnewllqgq iaagdienis
      661 sqptislqip ddclsleaiv svsvflyycs adssacmmka ilfsqplqit dtqqgciapv
      721 elryvf
//
LOCUS       NP_001230870             283 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            4 [Homo sapiens].
ACCESSION   NP_001230870
VERSION     NP_001230870.1
DBSOURCE    REFSEQ: accession NM_001243941.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC424578.1, AK304544.1,
            BC106050.1, AI955172.1 and AI379788.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks
            an in-frame exon in the 5' coding region, and initiates translation
            at a downstream start codon, compared to variant 1. Variants 4 and
            5 encode the same isoform (4), which has a shorter N-terminus
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304544.1, SRR7410570.630720.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..283
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 4"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=31191
     Region          <1..52
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          93..277
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..283
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001243941.1:432..1283"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58527.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mellimvyac ktscaksiig vipyfpyskq ckmrkrgsiv skllasmmck aglthlitmd
       61 lhqkeiqgff nipvdnlras pfllqyiqee ipdyrnaviv akspasakra qsfaerlrlg
      121 iavihgeaqd aesdlvdgrh sppmvrsvaa ihpsleipml ipkekppitv vgdvggriai
      181 ivddiiddvd sflaaaetlk ergaykifvm athgllssda prrieesaid evvvtntiph
      241 evqklqcpki ktvdismils eairrihnge smsylfrnig ldd
//
LOCUS       NP_001356837             580 aa            linear   PRI 20-NOV-2025
DEFINITION  synapsin-3 isoform IIIa [Homo sapiens].
ACCESSION   NP_001356837 XP_011528709
VERSION     NP_001356837.1
DBSOURCE    REFSEQ: accession NM_001369908.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Baris,R.O., Sahin,N., Bilgic,A.D., Ozdemir,C. and Edgunlu,T.G.
  TITLE     Molecular and in silico analyses of SYN III gene variants in autism
            spectrum disorder
  JOURNAL   Ir J Med Sci 192 (6), 2887-2895 (2023)
   PUBMED   37166614
  REMARK    GeneRIF: Molecular and in silico analyses of SYN III gene variants
            in autism spectrum disorder.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Bolat,H., Unsel-Bolat,G., Ozgul,S., Pariltay,E., Tahillioglu,A.,
            Rohde,L.A., Akin,H. and Ercan,E.S.
  TITLE     Investigation of possible associations of the BDNF, SNAP-25 and SYN
            III genes with the neurocognitive measures: BDNF and SNAP-25 genes
            might be involved in attention domain, SYN III gene in executive
            function
  JOURNAL   Nord J Psychiatry 76 (8), 610-615 (2022)
   PUBMED   35077325
  REMARK    GeneRIF: Investigation of possible associations of the BDNF,
            SNAP-25 and SYN III genes with the neurocognitive measures: BDNF
            and SNAP-25 genes might be involved in attention domain, SYN III
            gene in executive function.
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Longhena,F., Faustini,G., Varanita,T., Zaltieri,M., Porrini,V.,
            Tessari,I., Poliani,P.L., Missale,C., Borroni,B., Padovani,A.,
            Bubacco,L., Pizzi,M., Spano,P. and Bellucci,A.
  TITLE     Synapsin III is a key component of alpha-synuclein fibrils in Lewy
            bodies of PD brains
  JOURNAL   Brain Pathol 28 (6), 875-888 (2018)
   PUBMED   29330884
  REMARK    GeneRIF: Synapsin III is a crucial alpha-synuclein interactant and
            a key component of Lewy bodies fibrils in the brain of patients
            affected by Parkinson's disease.
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Porton,B., Ferreira,A., DeLisi,L.E. and Kao,H.T.
  TITLE     A rare polymorphism affects a mitogen-activated protein kinase site
            in synapsin III: possible relationship to schizophrenia
  JOURNAL   Biol Psychiatry 55 (2), 118-125 (2004)
   PUBMED   14732590
  REMARK    GeneRIF: A missense polymorphism, S470N, was identified in the
            synapsin III gene and appeared more frequently in individuals with
            schizophrenia. The site affected by the polymorphism, Ser470, was
            determined to be a substrate for mitogen-activated protein kinase.
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Tsai,M.T., Hung,C.C., Tsai,C.Y., Liu,M.Y., Su,Y.C., Chen,Y.H.,
            Hsiao,K.J. and Chen,C.H.
  TITLE     Mutation analysis of synapsin III gene in schizophrenia
  JOURNAL   Am J Med Genet 114 (1), 79-83 (2002)
   PUBMED   11840510
  REMARK    GeneRIF: Evidence is not in favor of a large effect of synapsin III
            gene in the pathogenesis of schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Hilfiker,S., Stefani,G., Pieribone,V.A.,
            DeSalle,R. and Greengard,P.
  TITLE     Molecular evolution of the synapsin gene family
  JOURNAL   J Exp Zool 285 (4), 360-377 (1999)
   PUBMED   10578110
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Porton,B., Kao,H.T. and Greengard,P.
  TITLE     Characterization of transcripts from the synapsin III gene locus
  JOURNAL   J Neurochem 73 (6), 2266-2271 (1999)
   PUBMED   10582583
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Czernik,A.J., Feng,J., Yiu,G., Haring,M.,
            Benfenati,F. and Greengard,P.
  TITLE     A third member of the synapsin gene family
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4667-4672 (1998)
   PUBMED   9539796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83846.1, Z98256.1, Z82246.2,
            Z80902.2, Z82181.2 and Z71183.2.
            
            On Apr 24, 2019 this sequence version replaced XP_011528709.1.
            
            Summary: This gene is a member of the synapsin gene family.
            Synapsins encode neuronal phosphoproteins which associate with the
            cytoplasmic surface of synaptic vesicles. Family members are
            characterized by common protein domains, and they are implicated in
            synaptogenesis and the modulation of neurotransmitter release,
            suggesting a potential role in several neuropsychiatric diseases.
            The protein encoded by this gene shares the synapsin family domain
            model, with domains A, C, and E exhibiting the highest degree of
            conservation. The protein contains a unique domain J, located
            between domains C and E. Based on this gene's localization to
            22q12.3, a possible schizophrenia susceptibility locus, and the
            established neurobiological roles of the synapsins, this family
            member may represent a candidate gene for schizophrenia. The TIMP3
            gene is located within an intron of this gene and is transcribed in
            the opposite direction. Alternative splicing of this gene results
            in multiple splice variants that encode different isoforms.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF046873.1, BC143874.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..580
                     /product="synapsin-3 isoform IIIa"
                     /note="synapsin-3; cN28H9.2 (synapsin III)"
                     /calculated_mol_wt=63172
     Region          1..29
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and CaMK1.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          19..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          28..90
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          91..399
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          92..191
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          193..395
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Region          <394..536
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          395..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          400..531
                     /region_name="J, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and MAPK.
                     /evidence=ECO:0000269|PubMed:14732590; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70441; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          532..580
                     /region_name="E"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     CDS             1..580
                     /gene="SYN3"
                     /coded_by="NM_001369908.1:483..2225"
                     /note="isoform IIIa is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS13908.1"
                     /db_xref="GeneID:8224"
                     /db_xref="HGNC:HGNC:11496"
                     /db_xref="MIM:602705"
ORIGIN      
        1 mnflrrrlsd ssfmanlpng ymtdlqrpds stsspaspam errhpqplaa sfsspgsslf
       61 sslssamkqa pqatsglmep pgpstpivqr prillvidda htdwskyfhg kkvngeieir
      121 veqaefseln laayvtggcm vdmqvvrngt kvvsrsfkpd filvrqhays malgedyrsl
      181 viglqygglp avnslysvyn fcskpwvfsq likifhslgp ekfplveqtf fpnhkpmvta
      241 phfpvvvklg hahagmgkik venqldfqdi tsvvamakty atteafidsk ydiriqkigs
      301 nykaymrtsi sgnwkantgs amleqvamte ryrlwvdscs emfggldica vkavhskdgr
      361 dyiievmdss mpligehvee drqlmadlvv skmsqlpmpg gtapsplrpw apqiksaksp
      421 gqaqlgpqlg qpqprpppqg gprqaqspqp qrsgspsqqr lspqgqqpls pqsgspqqqr
      481 spgspqlsra ssgsspnqas kpgatlasqp rppvqgrsts qqgeeskkpa pphphlnksq
      541 sltnslstsd tsqrgtpsed eakaetirnl rksfaslfsd
//
LOCUS       NP_057346                475 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin epsilon chain [Homo sapiens].
ACCESSION   NP_057346
VERSION     NP_057346.1
DBSOURCE    REFSEQ: accession NM_016262.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Pitsava,G., Feldkamp,M.L., Pankratz,N., Lane,J., Kay,D.M.,
            Conway,K.M., Shaw,G.M., Reefhuis,J., Jenkins,M.M., Almli,L.M.,
            Olshan,A.F., Pangilinan,F., Brody,L.C., Sicko,R.J., Hobbs,C.A.,
            Bamshad,M., McGoldrick,D., Nickerson,D.A., Finnell,R.H.,
            Mullikin,J., Romitti,P.A. and Mills,J.L.
  CONSRTM   University of Washington Center for Mendelian Genomics, NISC
            Comparative Sequencing Program and the National Birth Defects
            Prevention Study
  TITLE     Exome sequencing of child-parent trios with bladder exstrophy:
            Findings in 26 children
  JOURNAL   Am J Med Genet A 185 (10), 3028-3041 (2021)
   PUBMED   34355505
  REMARK    GeneRIF: Exome sequencing of child-parent trios with bladder
            exstrophy: Findings in 26 children.
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Wang,J.T., Kong,D., Hoerner,C.R., Loncarek,J. and Stearns,T.
  TITLE     Centriole triplet microtubules are required for stable centriole
            formation and inheritance in human cells
  JOURNAL   Elife 6, e29061 (2017)
   PUBMED   28906251
  REMARK    GeneRIF: Here, the authors report that centrioles in delta-tubulin
            and epsilon-tubulin null mutant human cells lack triplet
            microtubules and fail to undergo centriole maturation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Zanic,M., Stear,J.H., Hyman,A.A. and Howard,J.
  TITLE     EB1 recognizes the nucleotide state of tubulin in the microtubule
            lattice
  JOURNAL   PLoS One 4 (10), e7585 (2009)
   PUBMED   19851462
  REMARK    GeneRIF: EB1 recognizes the nucleotide state of tubulin in the
            microtubule lattice
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Chang,P., Giddings,T.H. Jr., Winey,M. and Stearns,T.
  TITLE     Epsilon-tubulin is required for centriole duplication and
            microtubule organization
  JOURNAL   Nat Cell Biol 5 (1), 71-76 (2003)
   PUBMED   12510196
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Chang,P. and Stearns,T.
  TITLE     Delta-tubulin and epsilon-tubulin: two new human centrosomal
            tubulins reveal new aspects of centrosome structure and function
  JOURNAL   Nat Cell Biol 2 (1), 30-35 (2000)
   PUBMED   10620804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK026242.1, BC025405.2 and
            CA411886.1.
            
            Summary: This gene encodes a member of the tubulin superfamily.
            This protein localizes to the centriolar sub-distal appendages that
            are associated with the older of the two centrioles after
            centrosome duplication. This protein plays a central role in
            organization of the microtubules during centriole duplication. A
            pseudogene of this gene is found on chromosome 5.[provided by
            RefSeq, Jan 2009].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025405.2, AK026242.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368662.10/ ENSP00000357651.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..475
                     /product="tubulin epsilon chain"
                     /note="epsilon-tubulin"
                     /calculated_mol_wt=52801
     Region          2..457
                     /region_name="epsilon_tubulin"
                     /note="The epsilon-tubulin family; cd02190"
                     /db_xref="CDD:276959"
     Site            order(10..12,15..16,75..77,80,105..107,146..149,151..152,
                     177,179..180,188,211,255,258..259,262)
                     /site_type="other"
                     /note="putative nucleotide binding site [chemical
                     binding]"
                     /db_xref="CDD:276959"
     CDS             1..475
                     /gene="TUBE1"
                     /gene_synonym="dJ142L7.2; TUBE"
                     /coded_by="NM_016262.5:49..1476"
                     /db_xref="CCDS:CCDS5100.1"
                     /db_xref="GeneID:51175"
                     /db_xref="HGNC:HGNC:20775"
                     /db_xref="MIM:607345"
ORIGIN      
        1 mtqsvvvqvg qcgnqigccf wdlalrehaa vnqkgiydea issffrnvdt rvvgdggsis
       61 kgkicslkar avlidmeegv vneilqgplr dvfdtkqlit disgsgnnwa vghkvfgsly
      121 qdqilekfrk saehcdclqc ffiihsmggg tgsglgtfll kvledefpev yrfvtsiyps
      181 geddvitspy nsilamkeln ehadcvlpid nqslfdiisk idlmvnsgkl gttvkpkslv
      241 tsssgalkkq hkkpfdamnn ivanlllnlt ssarfegsln mdlneismnl vpfpqlhylv
      301 ssltplytlt dvnipprrld qmfsdafskd hqllradpkh slylacalmv rgnvqisdlr
      361 rnierlkpsl qfvswnqegw ktslcsvppv ghshsllala nntcvkptfm elkerfmrly
      421 kkkahlhhyl qvegmeescf teavsslsal iqeydqldat knmpvqdlpr lsiam
//
LOCUS       NP_001357269             215 aa            linear   PRI 20-NOV-2025
DEFINITION  high mobility group protein B1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357269 XP_024305108
VERSION     NP_001357269.1
DBSOURCE    REFSEQ: accession NM_001370340.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 215)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138681.17 and AL353648.27.
            
            On May 7, 2019 this sequence version replaced XP_024305108.1.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.205139.1,
                                           SRR1803615.25694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2155974
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..215
                     /product="high mobility group protein B1 isoform 1"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=24763
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..163
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156,159,162..163)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          150..183
                     /region_name="Binding to AGER/RAGE.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          161..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          178..184
                     /region_name="Nuclear localization signal (NLS) 2.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            184
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..215
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001370340.1:387..1034"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS9335.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekdia ayrakgkpda akkgvvkaek
      181 skkkkeeeed eedeedeeee edeededeee dddde
//
LOCUS       NP_001305254             916 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear pore complex protein Nup214 isoform 4 [Homo sapiens].
ACCESSION   NP_001305254
VERSION     NP_001305254.1
DBSOURCE    REFSEQ: accession NM_001318325.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Choi,Y.J., Min,Y.K., Lee,S.T., Choi,J.R. and Shin,S.
  TITLE     NUP214 Rearrangements in Leukemia Patients: A Case Series From a
            Single Institution
  JOURNAL   Ann Lab Med 44 (4), 335-342 (2024)
   PUBMED   38145892
  REMARK    GeneRIF: NUP214 Rearrangements in Leukemia Patients: A Case Series
            From a Single Institution.
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Wang,J., Zhan,Q.R., Lu,X.X., Zhang,L.J., Wang,X.X. and Zhang,H.Y.
  TITLE     The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review
  JOURNAL   Medicine (Baltimore) 101 (30), e29294 (2022)
   PUBMED   35905214
  REMARK    GeneRIF: The characteristics and prognostic significance of the
            SET-CAN/NUP214 fusion gene in hematological malignancies: A
            systematic review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Zheng,Y.Z., Wen,J.J., Wang,L.Y., Zheng,H., Hua,X.L., Li,J. and
            Hu,J.D.
  TITLE     [SET-NUP214-positive pediatric acute myeloid leukemia: a report of
            two cases]
  JOURNAL   Zhonghua Xue Ye Xue Za Zhi 42 (9), 769 (2021)
   PUBMED   34753234
  REMARK    GeneRIF: [SET-NUP214-positive pediatric acute myeloid leukemia: a
            report of two cases].
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Napetschnig,J., Blobel,G. and Hoelz,A.
  TITLE     Crystal structure of the N-terminal domain of the human
            protooncogene Nup214/CAN
  JOURNAL   Proc Natl Acad Sci U S A 104 (6), 1783-1788 (2007)
   PUBMED   17264208
  REMARK    GeneRIF: A mechanism is proposed by which the C-terminal peptide
            extension is involved in nuclear pore complex assembly.
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Pilz,A., Woodward,K., Povey,S. and Abbott,C.
  TITLE     Comparative mapping of 50 human chromosome 9 loci in the laboratory
            mouse
  JOURNAL   Genomics 25 (1), 139-149 (1995)
   PUBMED   7774911
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Kraemer,D., Wozniak,R.W., Blobel,G. and Radu,A.
  TITLE     The human CAN protein, a putative oncogene product associated with
            myeloid leukemogenesis, is a nuclear pore complex protein that
            faces the cytoplasm
  JOURNAL   Proc Natl Acad Sci U S A 91 (4), 1519-1523 (1994)
   PUBMED   8108440
REFERENCE   9  (residues 1 to 916)
  AUTHORS   von Lindern,M., Fornerod,M., van Baal,S., Jaegle,M., de Wit,T.,
            Buijs,A. and Grosveld,G.
  TITLE     The translocation (6;9), associated with a specific subtype of
            acute myeloid leukemia, results in the fusion of two genes, dek and
            can, and the expression of a chimeric, leukemia-specific dek-can
            mRNA
  JOURNAL   Mol Cell Biol 12 (4), 1687-1697 (1992)
   PUBMED   1549122
REFERENCE   10 (residues 1 to 916)
  AUTHORS   von Lindern,M., Poustka,A., Lerach,H. and Grosveld,G.
  TITLE     The (6;9) chromosome translocation, associated with a specific
            subtype of acute nonlymphocytic leukemia, leads to aberrant
            transcription of a target gene on 9q34
  JOURNAL   Mol Cell Biol 10 (8), 4016-4026 (1990)
   PUBMED   2370860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316417.1, AL157938.22 and
            BC105998.1.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. This gene is a member of the
            FG-repeat-containing nucleoporins. The protein encoded by this gene
            is localized to the cytoplasmic face of the nuclear pore complex
            where it is required for proper cell cycle progression and
            nucleocytoplasmic transport. The 3' portion of this gene forms a
            fusion gene with the DEK gene on chromosome 6 in a t(6,9)
            translocation associated with acute myeloid leukemia and
            myelodysplastic syndrome. Alternative splicing of this gene results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (4) lacks several exons and
            contains an alternate 5' terminal exon resulting in a distinct 5'
            UTR and 5' coding region, compared to variant 2. It encodes isoform
            4, which is shorter and has a distinct N-terminus, compared to
            isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316417.1, AK302676.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.13"
     Protein         1..916
                     /product="nuclear pore complex protein Nup214 isoform 4"
                     /note="CAN protein, putative oncogene; nuclear pore
                     complex protein Nup214; nucleoporin 214kDa"
                     /calculated_mol_wt=87842
     Region          <88..517
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          <347..>525
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Region          <411..>913
                     /region_name="FhaB"
                     /note="Large exoprotein involved in heme utilization or
                     adhesion [Intracellular trafficking, secretion, and
                     vesicular transport]; COG3210"
                     /db_xref="CDD:442443"
     Region          742..803
                     /region_name="Nup214_FG"
                     /note="Nucleoporin Nup214 phenylalanine-glycine (FG)
                     domain; pfam18617"
                     /db_xref="CDD:408399"
     CDS             1..916
                     /gene="NUP214"
                     /gene_synonym="CAIN; CAN; IIAE9"
                     /coded_by="NM_001318325.2:291..3041"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS83430.1"
                     /db_xref="GeneID:8021"
                     /db_xref="HGNC:HGNC:8064"
                     /db_xref="MIM:114350"
ORIGIN      
        1 mksslllrgv hfcfhlpgta kietavtstp sasgqfskpf sfspsgtgfn fgiitptpss
       61 nftaaqgatp stkessqpda fssgggskps yeaipesspp sgitsasntt pgepaasssr
      121 pvapsgtals ttsskletpp sklgellfps slagetlgsf sglrvgqadd stkptnkass
      181 tsltstqptk tsgvpsgfnf tappvlgkht eppvtssatt tsvappaats tsstavfgsl
      241 pvtsagssgv isfggtslsa gktsfsfgsq qtnstvppsa pppttaatpl ptsfptlsfg
      301 sllssattps lpmsagrste eatssalpek pgdsevsasa aslleeqqsa qlpqappqts
      361 dsvkkepvla qpavsnsgta asstslvals aeatpattgv pdarteavpp assfsvpgqt
      421 avtaaaissa gpvavetsst piassttsiv apgpsaeaaa fgtvtsgssv faqppaasss
      481 safnqltnnt atapsatpvf gqvaastaps lfgqqtgsta staaatpqvs ssgfsspafg
      541 ttapgvfgqt tfgqasvfgq sassaasvfs fsqpgfssvp afgqpasstp tstsgsvfga
      601 asstsssssf sfgqsspntg gglfgqsnap afgqspgfgq ggsvfggtsa atttaatsgf
      661 sfcqasgfgs sntgsvfgqa astggivfgq qsssssgsvf gsgntgrggg ffsglggkps
      721 qdaanknpfs sasggfgsta tsntsnlfgn sgaktfggfa sssfgeqkpt gtfssgggsv
      781 asqgfgfssp nktggfgaap vfgspptfgg spgfggvpaf gsapaftspl gstggkvfge
      841 gtaaasaggf gfgsssntts fgtlasqnap tfgslsqqts gfgtqssgfs gfgsgtggfs
      901 fgsnnssvqg fggwrs
//
LOCUS       NP_036569                136 aa            linear   PRI 20-NOV-2025
DEFINITION  SNARE-associated protein Snapin [Homo sapiens].
ACCESSION   NP_036569
VERSION     NP_036569.1
DBSOURCE    REFSEQ: accession NM_012437.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Jeong,S., Rhee,J.S. and Lee,J.H.
  TITLE     Snapin Specifically Up-Regulates Cav1.3 Ca2+ Channel Variant with a
            Long Carboxyl Terminus
  JOURNAL   Int J Mol Sci 22 (20), 11268 (2021)
   PUBMED   34681928
  REMARK    GeneRIF: Snapin Specifically Up-Regulates Cav1.3 Ca(2+) Channel
            Variant with a Long Carboxyl Terminus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Jiang,M., Kuang,Z., He,Y., Cao,Y., Yu,T., Cheng,J., Liu,W. and
            Wang,W.
  TITLE     SNAPIN Regulates Cell Cycle Progression to Promote Pancreatic beta
            Cell Growth
  JOURNAL   Front Endocrinol (Lausanne) 12, 624309 (2021)
   PUBMED   34194388
  REMARK    GeneRIF: SNAPIN Regulates Cell Cycle Progression to Promote
            Pancreatic beta Cell Growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Hunt,R.A., Edris,W., Chanda,P.K., Nieuwenhuijsen,B. and Young,K.H.
  TITLE     Snapin interacts with the N-terminus of regulator of G protein
            signaling 7
  JOURNAL   Biochem Biophys Res Commun 303 (2), 594-599 (2003)
   PUBMED   12659861
  REMARK    GeneRIF: results suggest that RGS7 could play a role in synaptic
            vesicle exocytosis through its interaction with snapin
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Chheda,M.G., Ashery,U., Thakur,P., Rettig,J. and Sheng,Z.H.
  TITLE     Phosphorylation of Snapin by PKA modulates its interaction with the
            SNARE complex
  JOURNAL   Nat Cell Biol 3 (4), 331-338 (2001)
   PUBMED   11283605
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Ilardi,J.M., Mochida,S. and Sheng,Z.H.
  TITLE     Snapin: a SNARE-associated protein implicated in synaptic
            transmission
  JOURNAL   Nat Neurosci 2 (2), 119-124 (1999)
   PUBMED   10195194
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI117540.1, BC000761.2 and
            AI018675.1.
            
            Summary: The protein encoded by this gene is a coiled-coil-forming
            protein that associates with the SNARE (soluble
            N-ethylmaleimide-sensitive fusion protein attachment protein
            receptor) complex of proteins and the BLOC-1 (biogenesis of
            lysosome-related organelles) complex. Biochemical studies have
            identified additional binding partners. As part of the SNARE
            complex, it is required for vesicle docking and fusion and
            regulates neurotransmitter release. The BLOC-1 complex is required
            for the biogenesis of specialized organelles such as melanosomes
            and platelet dense granules. Mutations in gene products that form
            the BLOC-1 complex have been identified in mouse strains that are
            models of Hermansky-Pudlak syndrome. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK024555.1, BC000761.2 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368685.6/ ENSP00000357674.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..136
                     /product="SNARE-associated protein Snapin"
                     /note="SNARE associated protein snapin; SNAP-25-binding
                     protein; synaptosomal-associated protein 25-binding
                     protein; biogenesis of lysosomal organelles complex-1,
                     subunit 7; BLOC-1 subunit 7; biogenesis of
                     lysosome-related organelles complex 1 subunit 7; BLOC-1
                     related complex subunit 3"
                     /calculated_mol_wt=14743
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O95295.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     Region          23..110
                     /region_name="Snapin_Pallidin"
                     /note="Snapin/Pallidin; pfam14712"
                     /db_xref="CDD:464275"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:Q9Z266; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     Region          83..136
                     /region_name="Interaction with TOR1A"
                     /note="propagated from UniProtKB/Swiss-Prot (O95295.1)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95295.1)"
     CDS             1..136
                     /gene="SNAPIN"
                     /gene_synonym="BLOC1S7; BLOS7; BORCS3; NEDBAC; SNAPAP"
                     /coded_by="NM_012437.6:42..452"
                     /db_xref="CCDS:CCDS1049.1"
                     /db_xref="GeneID:23557"
                     /db_xref="HGNC:HGNC:17145"
                     /db_xref="MIM:607007"
ORIGIN      
        1 magagsaavs gagtpvagpt grdlfaegll eflrpavqql dshvhavres qvelreqidn
       61 latelcrine dqkvaldldp yvkkllnarr rvvlvnnilq naqerlrrln hsvaketarr
      121 ramldsgiyp pgspgk
//
LOCUS       NP_001356628             338 aa            linear   PRI 20-NOV-2025
DEFINITION  NF-kappa-B inhibitor beta isoform 3 [Homo sapiens].
ACCESSION   NP_001356628
VERSION     NP_001356628.1
DBSOURCE    REFSEQ: accession NM_001369699.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Suyang,H., Phillips,R., Douglas,I. and Ghosh,S.
  TITLE     Role of unphosphorylated, newly synthesized I kappa B beta in
            persistent activation of NF-kappa B
  JOURNAL   Mol Cell Biol 16 (10), 5444-5449 (1996)
   PUBMED   8816457
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Beauparlant,P., Kwon,H., Clarke,M., Lin,R., Sonenberg,N.,
            Wainberg,M. and Hiscott,J.
  TITLE     Transdominant mutants of I kappa B alpha block Tat-tumor necrosis
            factor synergistic activation of human immunodeficiency virus type
            1 gene expression and virus multiplication
  JOURNAL   J Virol 70 (9), 5777-5785 (1996)
   PUBMED   8709193
REFERENCE   8  (residues 1 to 338)
  AUTHORS   DiDonato,J., Mercurio,F., Rosette,C., Wu-Li,J., Suyang,H., Ghosh,S.
            and Karin,M.
  TITLE     Mapping of the inducible IkappaB phosphorylation sites that signal
            its ubiquitination and degradation
  JOURNAL   Mol Cell Biol 16 (4), 1295-1304 (1996)
   PUBMED   8657102
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Harhaj,E., Blaney,J., Millhouse,S. and Sun,S.C.
  TITLE     Differential effects of I kappa B molecules on Tat-mediated
            transactivation of HIV-1 LTR
  JOURNAL   Virology 216 (1), 284-287 (1996)
   PUBMED   8615004
REFERENCE   10 (residues 1 to 338)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209784.1 and AC011455.6.
            
            Summary: The protein encoded by this gene belongs to the NF-kappa-B
            inhibitor family, which inhibit NF-kappa-B by complexing with, and
            trapping it in the cytoplasm. Phosphorylation of serine residues on
            these proteins by kinases marks them for destruction via the
            ubiquitination pathway, thereby allowing activation of the
            NF-kappa-B, which translocates to the nucleus to function as a
            transcription factor. Alternatively spliced transcript variants
            have been found for this gene.[provided by RefSeq, Jul 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.75279.1, AB209784.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..338
                     /product="NF-kappa-B inhibitor beta isoform 3"
                     /note="NF-kappa-B inhibitor beta; ikB-B; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells
                     inhibitor, beta; TRIP-9; ikB-beta; ikappaBbeta;
                     NF-kappa-BIB; I-kappa-B-beta; TR-interacting protein 9;
                     thyroid receptor-interacting protein 9"
                     /calculated_mol_wt=35399
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:8657102; propagated from
                     UniProtKB/Swiss-Prot (Q15653.2)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by RPS6KA1.
                     /evidence=ECO:0000269|PubMed:8657102; propagated from
                     UniProtKB/Swiss-Prot (Q15653.2)"
     Region          56..298
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(57,59,63..64,67..69,71..72,76,79,91,93,95,99..100,
                     103..105,107..108,112,115,124,126,128,132..133,136..138,
                     140..141,145,148)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          57..91
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          57..86
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          93..124
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          93..122
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          126..155
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          149..193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15653.2)"
     Site            order(206,208,212..213,216..218,220..221,225,228,237,239,
                     242,246..247,250..252,254..255,259,262,271,273,275,
                     279..280,283..285,287..288,292,295)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          206..237
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          206..235
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          239..271
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          240..269
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          273..302
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15653.2)"
     Region          273..298
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:8887627; propagated from
                     UniProtKB/Swiss-Prot (Q15653.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:8887627; propagated from
                     UniProtKB/Swiss-Prot (Q15653.2)"
     CDS             1..338
                     /gene="NFKBIB"
                     /gene_synonym="IKBB; TRIP9"
                     /coded_by="NM_001369699.1:65..1081"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92612.1"
                     /db_xref="GeneID:4793"
                     /db_xref="HGNC:HGNC:7798"
                     /db_xref="MIM:604495"
ORIGIN      
        1 magvaclgka adadewcdsg lgslgpdaaa pggpglgael gpglswaplv fgyvtedgdt
       61 alhlavihqh epfldfllgf sagteymdlq ndlgqtalhl aailgetstv eklyaagagl
      121 cvaerrghta lhlacrvgah acarallqpr prrpreapdt ylaqgpdrtp dtnhtpvaly
      181 pdsdlekeee eseedwklql eaenyeghtp lhvavihkdv emvrllrdag adldkpeptc
      241 grsplhlave aqaadvlell lraganpaar myggrtplgs amlrpnpila rllrahgape
      301 pegedeksgp cssssdsdsg degvsqeerq gspaggsg
//
LOCUS       NP_036303                332 aa            linear   PRI 20-NOV-2025
DEFINITION  tetraspanin-17 isoform a [Homo sapiens].
ACCESSION   NP_036303
VERSION     NP_036303.1
DBSOURCE    REFSEQ: accession NM_012171.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Guo,X.B., Zhang,X.C., Chen,P., Ma,L.M. and Shen,Z.Q.
  TITLE     miR-378a-3p inhibits cellular proliferation and migration in
            glioblastoma multiforme by targeting tetraspanin 17
  JOURNAL   Oncol Rep 42 (5), 1957-1971 (2019)
   PUBMED   31432186
  REMARK    GeneRIF: Data suggested that increased miR378a3p and decreased
            TSPAN17 levels were associated with improved survival in
            glioblastoma multiforme (GBM). Additionally, high levels of TSPAN17
            were linked to the poor prognosis of patients with GBM aged 5060,
            larger tumor sizes and an advanced World Health Organization stage.
            TSPAN17 was identified and confirmed as a direct target of miR378a.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Reyat,J.S., Chimen,M., Noy,P.J., Szyroka,J., Rainger,G.E. and
            Tomlinson,M.G.
  TITLE     ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate
            VE-Cadherin Expression and Promote T Lymphocyte Transmigration
  JOURNAL   J Immunol 199 (2), 666-676 (2017)
   PUBMED   28600292
  REMARK    GeneRIF: Endothelial Tspan5- and Tspan17-ADAM10 complexes may
            regulate inflammation by maintaining normal VE-cadherin expression
            and promoting T lymphocyte transmigration.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Dornier,E., Coumailleau,F., Ottavi,J.F., Moretti,J., Boucheix,C.,
            Mauduit,P., Schweisguth,F. and Rubinstein,E.
  TITLE     TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and
            promote Notch activation in flies and mammals
  JOURNAL   J Cell Biol 199 (3), 481-496 (2012)
   PUBMED   23091066
  REMARK    Erratum:[J Cell Biol. 2016 May 23;213(4):495-6. doi:
            10.1083/jcb.20120113304262016c. PMID: 27185832]
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091934.2.
            
            Summary: This gene encodes a member of the transmembrane 4
            superfamily. It is characterized by four tetraspanin transmembrane
            segments. The function of this gene has not yet been determined.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.102915.1,
                                           SRR1803616.270529.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..332
                     /product="tetraspanin-17 isoform a"
                     /EC_number="3.6.5.3"
                     /note="F-box only protein 23, transmembrane 4 superfamily
                     member 17; tetraspan protein SB134"
                     /calculated_mol_wt=36924
     Region          18..263
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Region          115..238
                     /region_name="TM4SF9_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF9_like subfamily.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03159"
                     /db_xref="CDD:239412"
     Site            order(116,121,125,127..128,131,145,148..149,152..153)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239412"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     CDS             1..332
                     /gene="TSPAN17"
                     /gene_synonym="FBX23; FBXO23; TM4SF17"
                     /coded_by="NM_012171.3:133..1131"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34298.1"
                     /db_xref="GeneID:26262"
                     /db_xref="HGNC:HGNC:13594"
                     /db_xref="MIM:620446"
ORIGIN      
        1 mpgkhqhfqe pevgccgkyf lfgfnivfwv lgalflaigl wawgekgvls nisaltdlgg
       61 ldpvwlfvvv ggvmsvlgfa gcigalrent fllkffsvfl glifflelat gilafvfkdw
      121 irdqlnlfin nnvkayrddi dlqnlidfaq eywsccgarg pndwnlniyf nctdlnpsre
      181 rcgvpfsccv rdpaedvlnt qcgydvrlkl vrgeleqqgf ihtkgcvgqf ekwlqdnliv
      241 vagvfmgial lqifgiclaq nlvsdikavk anwskwnddf enhwltptis evlstagpqq
      301 nsltgapgpa ppsrhvffgl gglypeptfk nw
//
LOCUS       NP_001354669             492 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform d [Homo sapiens].
ACCESSION   NP_001354669
VERSION     NP_001354669.1
DBSOURCE    REFSEQ: accession NM_001367740.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (24), as well as variants 21-23,
            encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.195546.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..492
                     /product="rab5 GDP/GTP exchange factor isoform d"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56831
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          159..221
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          271..371
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..492
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367740.1:942..2420"
                     /note="isoform d is encoded by transcript variant 24"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkaeiqe
      121 akapspsinr qtsietdrvs kefieflktf hktgqeiykq tklflegmhy krdlsieeqs
      181 ecaqdfyhnv aermqtrgkv ppervekimd qiekyimtrl ykyvfcpett ddekkdlaiq
      241 kriralrwvt pqmlcvpvne dipevsdmvv kaitdiiemd skrvprdkla citkcskhif
      301 naikitknep asaddflptl iyivlkgnpp rlqsniqyit rfcnpsrlmt gedgyyftnl
      361 ccavafiekl daqslnlsqe dfdrymsgqt sprkqeaesw spdaclgvkq myknldllsq
      421 lnerqerimn eakklekdli dwtdgiarev qdivekyple ikppnqplaa idsenvendk
      481 lppplqpqvy ag
//
LOCUS       NP_001515                131 aa            linear   PRI 20-NOV-2025
DEFINITION  hypocretin neuropeptide precursor precursor [Homo sapiens].
ACCESSION   NP_001515
VERSION     NP_001515.1
DBSOURCE    REFSEQ: accession NM_001524.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 131)
  AUTHORS   Nigro,E., D'Arco,D., Moscatelli,F., Pisani,A., Amicone,M.,
            Riccio,E., Capuano,I., Argentino,F., Monda,M., Messina,G.,
            Daniele,A. and Polito,R.
  TITLE     Increased Expression of Orexin-A in Patients Affected by Polycystic
            Kidney Disease
  JOURNAL   Int J Mol Sci 25 (11), 6243 (2024)
   PUBMED   38892431
  REMARK    GeneRIF: Increased Expression of Orexin-A in Patients Affected by
            Polycystic Kidney Disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 131)
  AUTHORS   Huan,R., Zhang,J., Yue,J., Yang,S., Han,G., Cheng,Y. and Tan,Y.
  TITLE     Orexin-A mediates glioblastoma proliferation inhibition by
            increasing ferroptosis triggered by unstable iron pools and GPX4
            depletion
  JOURNAL   J Cell Mol Med 28 (9), e18318 (2024)
   PUBMED   38685674
  REMARK    GeneRIF: Orexin-A mediates glioblastoma proliferation inhibition by
            increasing ferroptosis triggered by unstable iron pools and GPX4
            depletion.
REFERENCE   3  (residues 1 to 131)
  AUTHORS   Hakami,W., Thabet,F., Alhashem,A., Alghamdi,A., Alshahwan,S.,
            Alkuraya,F.S. and Tabarki,B.
  TITLE     Bi-allelic variants in HCRT cause autosomal recessive narcolepsy
  JOURNAL   Neurogenetics 25 (2), 79-83 (2024)
   PUBMED   38240911
  REMARK    GeneRIF: Bi-allelic variants in HCRT cause autosomal recessive
            narcolepsy.
REFERENCE   4  (residues 1 to 131)
  AUTHORS   Sandikci,S.C., Gultuna,S., Ozisler,C. and Aydin,F.N.
  TITLE     The role of orexin in fatigue and sleep quality in patients with
            primary Sjogren's syndrome
  JOURNAL   Z Rheumatol 83 (Suppl 1), 242-247 (2024)
   PUBMED   38108866
  REMARK    GeneRIF: The role of orexin in fatigue and sleep quality in
            patients with primary Sjogren's syndrome.
REFERENCE   5  (residues 1 to 131)
  AUTHORS   Soejima,Y., Iwata,N., Nishioka,R., Honda,M., Nakano,Y.,
            Yamamoto,K., Suyama,A. and Otsuka,F.
  TITLE     Interaction of Orexin and Bone Morphogenetic Proteins in
            Steroidogenesis by Human Adrenocortical Cells
  JOURNAL   Int J Mol Sci 24 (16), 12559 (2023)
   PUBMED   37628739
  REMARK    GeneRIF: Interaction of Orexin and Bone Morphogenetic Proteins in
            Steroidogenesis by Human Adrenocortical Cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 131)
  AUTHORS   van den Pol,A.N., Gao,X.B., Obrietan,K., Kilduff,T.S. and
            Belousov,A.B.
  TITLE     Presynaptic and postsynaptic actions and modulation of
            neuroendocrine neurons by a new hypothalamic peptide,
            hypocretin/orexin
  JOURNAL   J Neurosci 18 (19), 7962-7971 (1998)
   PUBMED   9742163
REFERENCE   7  (residues 1 to 131)
  AUTHORS   Sakurai,T., Amemiya,A., Ishii,M., Matsuzaki,I., Chemelli,R.M.,
            Tanaka,H., Williams,S.C., Richarson,J.A., Kozlowski,G.P.,
            Wilson,S., Arch,J.R., Buckingham,R.E., Haynes,A.C., Carr,S.A.,
            Annan,R.S., McNulty,D.E., Liu,W.S., Terrett,J.A., Elshourbagy,N.A.,
            Bergsma,D.J. and Yanagisawa,M.
  TITLE     Orexins and orexin receptors: a family of hypothalamic
            neuropeptides and G protein-coupled receptors that regulate feeding
            behavior
  JOURNAL   Cell 92 (5), 1pagefollowing696 (1998)
   PUBMED   9527442
REFERENCE   8  (residues 1 to 131)
  AUTHORS   Sakurai,T., Amemiya,A., Ishii,M., Matsuzaki,I., Chemelli,R.M.,
            Tanaka,H., Williams,S.C., Richardson,J.A., Kozlowski,G.P.,
            Wilson,S., Arch,J.R., Buckingham,R.E., Haynes,A.C., Carr,S.A.,
            Annan,R.S., McNulty,D.E., Liu,W.S., Terrett,J.A., Elshourbagy,N.A.,
            Bergsma,D.J. and Yanagisawa,M.
  TITLE     Orexins and orexin receptors: a family of hypothalamic
            neuropeptides and G protein-coupled receptors that regulate feeding
            behavior
  JOURNAL   Cell 92 (4), 573-585 (1998)
   PUBMED   9491897
REFERENCE   9  (residues 1 to 131)
  AUTHORS   Flier,J.S. and Maratos-Flier,E.
  TITLE     Obesity and the hypothalamus: novel peptides for new pathways
  JOURNAL   Cell 92 (4), 437-440 (1998)
   PUBMED   9491885
  REMARK    Review article
REFERENCE   10 (residues 1 to 131)
  AUTHORS   de Lecea,L., Kilduff,T.S., Peyron,C., Gao,X., Foye,P.E.,
            Danielson,P.E., Fukuhara,C., Battenberg,E.L., Gautvik,V.T.,
            Bartlett,F.S. 2nd, Frankel,W.N., van den Pol,A.N., Bloom,F.E.,
            Gautvik,K.M. and Sutcliffe,J.G.
  TITLE     The hypocretins: hypothalamus-specific peptides with
            neuroexcitatory activity
  JOURNAL   Proc Natl Acad Sci U S A 95 (1), 322-327 (1998)
   PUBMED   9419374
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF041240.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a hypothalamic neuropeptide precursor
            protein that gives rise to two mature neuropeptides, orexin A and
            orexin B, by proteolytic processing. Orexin A and orexin B, which
            bind to orphan G-protein coupled receptors HCRTR1 and HCRTR2,
            function in the regulation of sleep and arousal. This neuropeptide
            arrangement may also play a role in feeding behavior, metabolism,
            and homeostasis. [provided by RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF041240.1, AW163085.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293330.1/ ENSP00000293330.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..131
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..131
                     /product="hypocretin neuropeptide precursor precursor"
                     /note="orexin; prepro-orexin; hypocretin (orexin)
                     neuropeptide; preprohypocretin"
                     /calculated_mol_wt=10035
     Region          1..130
                     /region_name="Orexin"
                     /note="Prepro-orexin; pfam02072"
                     /db_xref="CDD:460436"
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3346
     mat_peptide     33..66
                     /product="orexin A"
                     /calculated_mol_wt=3654
     Site            34
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:O55232; propagated from
                     UniProtKB/Swiss-Prot (O43612.1)"
     Site            66
                     /site_type="amidation"
                     /note="Leucine amide.
                     /evidence=ECO:0000250|UniProtKB:O55232; propagated from
                     UniProtKB/Swiss-Prot (O43612.1)"
     mat_peptide     69..96
                     /product="orexin B"
                     /calculated_mol_wt=2925
     Site            97
                     /site_type="amidation"
                     /note="Methionine amide.
                     /evidence=ECO:0000250|UniProtKB:O55232; propagated from
                     UniProtKB/Swiss-Prot (O43612.1)"
     CDS             1..131
                     /gene="HCRT"
                     /gene_synonym="NRCLP1; OX; PPOX"
                     /coded_by="NM_001524.1:88..483"
                     /db_xref="CCDS:CCDS11421.1"
                     /db_xref="GeneID:3060"
                     /db_xref="HGNC:HGNC:4847"
                     /db_xref="MIM:602358"
ORIGIN      
        1 mnlpstkvsw aavtllllll llppallssg aaaqplpdcc rqktcscrly ellhgagnha
       61 agiltlgkrr sgppglqgrl qrllqasgnh aagiltmgrr agaepaprpc lgrrcsapaa
      121 asvapggqsg i
//
LOCUS       NP_001138881             471 aa            linear   PRI 20-NOV-2025
DEFINITION  non-POU domain-containing octamer-binding protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_001138881
VERSION     NP_001138881.1
DBSOURCE    REFSEQ: accession NM_001145409.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Trifault,B., Mamontova,V., Cossa,G., Ganskih,S., Wei,Y.,
            Hofstetter,J., Bhandare,P., Baluapuri,A., Nieto,B., Solvie,D.,
            Ade,C.P., Gallant,P., Wolf,E., Larsen,D.H., Munschauer,M. and
            Burger,K.
  TITLE     Nucleolar detention of NONO shields DNA double-strand breaks from
            aberrant transcripts
  JOURNAL   Nucleic Acids Res 52 (6), 3050-3068 (2024)
   PUBMED   38224452
  REMARK    GeneRIF: Nucleolar detention of NONO shields DNA double-strand
            breaks from aberrant transcripts.
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Clark,J., Lu,Y.J., Sidhar,S.K., Parker,C., Gill,S., Smedley,D.,
            Hamoudi,R., Linehan,W.M., Shipley,J. and Cooper,C.S.
  TITLE     Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
            gene in papillary renal cell carcinoma
  JOURNAL   Oncogene 15 (18), 2233-2239 (1997)
   PUBMED   9393982
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Peters,U., Haberhausen,G., Kostrzewa,M., Nolte,D. and Muller,U.
  TITLE     AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as
            candidate genes of X-linked dystonia parkinsonism
  JOURNAL   Hum Genet 100 (5-6), 569-572 (1997)
   PUBMED   9341872
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Traish,A.M., Huang,Y.H., Ashba,J., Pronovost,M., Pavao,M.,
            McAneny,D.B. and Moreland,R.B.
  TITLE     Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen
            receptor-negative human breast cancer
  JOURNAL   Diagn Mol Pathol 6 (4), 209-221 (1997)
   PUBMED   9360842
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Hallier,M., Tavitian,A. and Moreau-Gachelin,F.
  TITLE     The transcription factor Spi-1/PU.1 binds RNA and interferes with
            the RNA-binding protein p54nrb
  JOURNAL   J Biol Chem 271 (19), 11177-11181 (1996)
   PUBMED   8626664
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Dong,B., Horowitz,D.S., Kobayashi,R. and Krainer,A.R.
  TITLE     Purification and cDNA cloning of HeLa cell p54nrb, a nuclear
            protein with two RNA recognition motifs and extensive homology to
            human splicing factor PSF and Drosophila NONA/BJ6
  JOURNAL   Nucleic Acids Res 21 (17), 4085-4092 (1993)
   PUBMED   8371983
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Zhang,W.W., Zhang,L.X., Busch,R.K., Farres,J. and Busch,H.
  TITLE     Purification and characterization of a DNA-binding heterodimer of
            52 and 100 kDa from HeLa cells
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 267-272 (1993)
   PUBMED   8439294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA116840.1, BC012141.1 and
            BC002364.1.
            
            Summary: This gene encodes an RNA-binding protein which plays
            various roles in the nucleus, including transcriptional regulation
            and RNA splicing. A rearrangement between this gene and the
            transcription factor E3 gene has been observed in papillary renal
            cell carcinoma. Alternatively spliced transcript variants have been
            described. Pseudogenes exist on Chromosomes 2 and 16. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein (isoform
            1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012141.1, SRR1803614.153868.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..471
                     /product="non-POU domain-containing octamer-binding
                     protein isoform 1"
                     /note="non-POU domain-containing octamer (ATGCAAAT)
                     binding protein; 54 kDa nuclear RNA- and DNA-binding
                     protein; p54(nrb); 55 kDa nuclear protein; DNA-binding
                     p52/p100 complex, 52 kDa subunit; protein phosphatase 1,
                     regulatory subunit 114"
                     /calculated_mol_wt=54101
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          54..373
                     /region_name="DBHS"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Region          73..143
                     /region_name="RRM1_p54nrb"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     54 kDa nuclear RNA- and DNA-binding protein (p54nrb);
                     cd12588"
                     /db_xref="CDD:410001"
     Site            order(119..120,123..124,126..128)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410001"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          149..228
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          219..311
                     /region_name="NOPS_p54nrb_PSF_PSPC1"
                     /note="NOPS domain, including C-terminal coiled-coil
                     region, in p54nrb/PSF/PSPC1 family proteins; cd12946"
                     /db_xref="CDD:240581"
     Site            order(219..221,223,263..264,266..268,270..272,274..275,
                     277..278,281..282,285..286,288..289,292..293,296..297,
                     299..300,303..304,307)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:240581"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            371
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            377..378
                     /site_type="other"
                     /note="Breakpoint for translocation to form NONO-TFE3;
                     propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          443..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            456
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     CDS             1..471
                     /gene="NONO"
                     /gene_synonym="MRXS34; NMT55; NRB54; P54; P54NRB;
                     PPP1R114"
                     /coded_by="NM_001145409.2:97..1512"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14410.1"
                     /db_xref="GeneID:4841"
                     /db_xref="HGNC:HGNC:7871"
                     /db_xref="MIM:300084"
ORIGIN      
        1 mqsnktfnle kqnhtprkhh qhhhqqqhhq qqqqqppppp ipangqqass qnegltidlk
       61 nfrkpgektf tqrsrlfvgn lppditeeem rklfekygka gevfihkdkg fgfirletrt
      121 laeiakveld nmplrgkqlr vrfachsasl tvrnlpqyvs nelleeafsv fgqveravvi
      181 vddrgrpsgk givefsgkpa arkaldrcse gsfllttfpr pvtvepmdql ddeeglpekl
      241 viknqqfhke reqpprfaqp gsfeyeyamr wkaliemekq qqdqvdrnik eareklemem
      301 eaarhehqvm lmrqdlmrrq eelrrmeelh nqevqkrkql elrqeeerrr reeemrrqqe
      361 emmrrqqegf kgtfpdareq eirmgqmamg gamginnrga mppapvpagt pappgpatmm
      421 pdgtlgltpp tterfgqaat megigaiggt ppafnraapg aefapnkrrr y
//
LOCUS       NP_689478                158 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor BTF3 homolog 4 isoform 1 [Homo sapiens].
ACCESSION   NP_689478 XP_371577 XP_496364
VERSION     NP_689478.1
DBSOURCE    REFSEQ: accession NM_152265.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Lu,B., Lu,T., Shi,J., Sun,P., Zhang,X., Yang,L., Wang,Z. and
            Huang,J.
  TITLE     Basic Transcription Factor 3 Like 4 Enhances Malignant Phenotypes
            through Modulating Tumor Cell Function and Immune Microenvironment
            in Glioma
  JOURNAL   Am J Pathol 194 (5), 772-784 (2024)
   PUBMED   38320629
  REMARK    GeneRIF: Basic Transcription Factor 3 Like 4 Enhances Malignant
            Phenotypes through Modulating Tumor Cell Function and Immune
            Microenvironment in Glioma.
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Ji,Y.H., Ji,J.L., Sun,F.Y., Zeng,Y.Y., He,X.H., Zhao,J.X., Yu,Y.,
            Yu,S.H. and Wu,W.
  TITLE     Quantitative proteomics analysis of chondrogenic differentiation of
            C3H10T1/2 mesenchymal stem cells by iTRAQ labeling coupled with
            on-line two-dimensional LC/MS/MS
  JOURNAL   Mol Cell Proteomics 9 (3), 550-564 (2010)
   PUBMED   20008835
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC070378.1 and AL139156.11.
            
            On or before Mar 11, 2005 this sequence version replaced
            XP_371577.1, XP_496364.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.26945.1,
                                           SRR1803611.61306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313334.13/ ENSP00000360664.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..158
                     /product="transcription factor BTF3 homolog 4 isoform 1"
                     /note="transcription factor BTF3 homolog 4"
                     /calculated_mol_wt=17139
     Region          4..120
                     /region_name="NAC_BTF3"
                     /note="basal transcription factor BTF3; cd22055"
                     /db_xref="CDD:409234"
     Site            5
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000250|UniProtKB:P20290; propagated from
                     UniProtKB/Swiss-Prot (Q96K17.1)"
     Site            22..26
                     /site_type="other"
                     /note="ribosome binding motif"
                     /db_xref="CDD:409234"
     Site            order(52..62,67,69,81..87,89,103..105)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:409234"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P20290; propagated from
                     UniProtKB/Swiss-Prot (Q96K17.1)"
     Region          122..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K17.1)"
     CDS             1..158
                     /gene="BTF3L4"
                     /coded_by="NM_152265.5:99..575"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30713.1"
                     /db_xref="GeneID:91408"
                     /db_xref="HGNC:HGNC:30547"
ORIGIN      
        1 mnqeklaklq aqvriggkgt arrkkkvvhr tataddkklq sslkklavnn iagieevnmi
       61 kddgtvihfn npkvqaslsa ntfaitghae akpitemlpg ilsqlgadsl tslrklaeqf
      121 prqvldskap kpedideedd dvpdlvenfd easknean
//
LOCUS       NP_001275712             276 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 8 isoform F [Homo sapiens].
ACCESSION   NP_001275712 XP_005267395
VERSION     NP_001275712.1
DBSOURCE    REFSEQ: accession NM_001288783.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Ullah,A., Umair,M., Yousaf,M., Khan,S.A., Nazim-Ud-Din,M., Shah,K.,
            Ahmad,F., Azeem,Z., Ali,G., Alhaddad,B., Rafique,A., Jan,A.,
            Haack,T.B., Strom,T.M., Meitinger,T., Ghous,T. and Ahmad,W.
  TITLE     Sequence variants in four genes underlying Bardet-Biedl syndrome in
            consanguineous families
  JOURNAL   Mol Vis 23, 482-494 (2017)
   PUBMED   28761321
  REMARK    GeneRIF: Two novel mutations and three previously reported
            variants, identified in the present study, further extend the body
            of evidence implicating BBS6, BBS7, BBS8, and BBS10 in causing
            Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
  REMARK    GeneRIF: A homozygous null BBS8 mutation leads to Bardet-Biedl
            syndrome with randomization of left-right body axis symmetry, a
            known defect of the nodal cilium
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX247959.1, AK093891.1,
            AY366523.1 and BU738965.1.
            
            On Jan 4, 2014 this sequence version replaced XP_005267395.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is involved in the formation of cilia. A
            mutation in this gene has also been implicated in nonsyndromic
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (6) differs in its 5' UTR and uses
            a downstream start codon, compared to variant 1. The encoded
            isoform (F) has a shorter N-terminus, compared to isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK093891.1, SRR1660803.297300.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..276
                     /product="tetratricopeptide repeat protein 8 isoform F"
                     /note="Bardet-Biedl syndrome type 8; TPR repeat protein 8"
                     /calculated_mol_wt=31348
     Region          2..272
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          19..47
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(20,23..24,27..28,30,54,57..58,61..62,64..65,88,
                     91..92,95..96,99)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          52..82
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          87..115
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(122,125..126,129..130,132,159,162..163,166..167,
                     169..170,193,196..197,200..201,204)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          122..149
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          154..187
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          192..218
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          226..251
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..276
                     /gene="TTC8"
                     /gene_synonym="BBS8; RP51"
                     /coded_by="NM_001288783.1:854..1684"
                     /note="isoform F is encoded by transcript variant 6"
                     /db_xref="GeneID:123016"
                     /db_xref="HGNC:HGNC:20087"
                     /db_xref="MIM:608132"
ORIGIN      
        1 myreaekqfk salkqqemvd tflylakvyv sldqpvtaln lfkqgldkfp gevtllcgia
       61 riyeemnnms saaeyykevl kqdnthveai acigsnhfys dqpeialrfy rrllqmgiyn
      121 gqlfnnlglc cfyaqqydmt ltsferalsl aeneeeaadv wynlghvavg igdtnlahqc
      181 frlalvnnnn haeaynnlav lemrkghveq arallqtass laphmyephf nfatisdkig
      241 dlqrsyvaaq kseaafpdhv dtqhlikqlr qhfaml
//
LOCUS       NP_060613                708 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 11 precursor [Homo sapiens].
ACCESSION   NP_060613
VERSION     NP_060613.1
DBSOURCE    REFSEQ: accession NM_018143.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Dubey,D., Wilson,M.R., Clarkson,B., Giannini,C., Gandhi,M.,
            Cheville,J., Lennon,V.A., Eggers,S., Devine,M.F., Mandel-Brehm,C.,
            Kryzer,T., Hinson,S.R., Khazaie,K., Hales,C., Kattah,J.,
            Pavelko,K.D., Andrews,P., Eaton,J.E., Jitprapaikulsan,J.,
            Mills,J.R., Flanagan,E.P., Zekeridou,A., Leibovich,B., Fryer,J.,
            Torre,M., Kaufman,C., Thoreson,J.B., Sagen,J., Linnoila,J.J.,
            DeRisi,J.L., Howe,C.L., McKeon,A. and Pittock,S.J.
  TITLE     Expanded Clinical Phenotype, Oncological Associations, and
            Immunopathologic Insights of Paraneoplastic Kelch-like Protein-11
            Encephalitis
  JOURNAL   JAMA Neurol 77 (11), 1420-1429 (2020)
   PUBMED   32744608
  REMARK    GeneRIF: Expanded Clinical Phenotype, Oncological Associations, and
            Immunopathologic Insights of Paraneoplastic Kelch-like Protein-11
            Encephalitis.
            Erratum:[JAMA Neurol. 2020 Nov 1;77(11):1453. doi:
            10.1001/jamaneurol.2020.3470. PMID: 32926076]
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Canning,P., Cooper,C.D.O., Krojer,T., Murray,J.W., Pike,A.C.W.,
            Chaikuad,A., Keates,T., Thangaratnarajah,C., Hojzan,V.,
            Marsden,B.D., Gileadi,O., Knapp,S., von Delft,F. and Bullock,A.N.
  TITLE     Structural basis for Cul3 protein assembly with the BTB-Kelch
            family of E3 ubiquitin ligases
  JOURNAL   J Biol Chem 288 (11), 7803-7814 (2013)
   PUBMED   23349464
  REMARK    GeneRIF: analysis of crystal structures of the BTB-BACK domains of
            KLHL11 both alone and in complex with Cul3
            Erratum:[J Biol Chem. 2013 Sep 27;388(39):28304. Ayinampudi, Vikram
            [added]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI463857.1, AK001434.1 and AC125257.4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.72019.1,
                                           SRR1660805.47769.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319121.4/ ENSP00000314608.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..708
                     /product="kelch-like protein 11 precursor"
                     /note="kelch-like protein 11"
                     /calculated_mol_wt=78994
     sig_peptide     1..15
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NVR0.1)"
                     /calculated_mol_wt=1172
     mat_peptide     16..708
                     /product="Kelch-like protein 11. /id=PRO_0000243918"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
                     /calculated_mol_wt=78994
     Region          47..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          71..205
                     /region_name="BTB_POZ_KLHL11"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 11 (KLHL11); cd18241"
                     /db_xref="CDD:349550"
     Site            order(71..73,76..81,83..84,87,92..93,111..114,116..118,
                     160..170,187,191,195,198..199)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349550"
     Region          90..553
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Site            order(120..121,124..125,129..132,139..142,170,173..174,
                     181..182,184,196,204)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349550"
     Region          200..287
                     /region_name="BACK_KLHL11"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 11 (KLHL11); cd18451"
                     /db_xref="CDD:350526"
     Site            order(204,207..208,210..211,213..216,245..246,284)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:350526"
     Region          360..407
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          399..439
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..453
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          443..488
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          455..501
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          491..541
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          503..556
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          567..649
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          610..661
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVR0.1)"
     Region          611..657
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..708
                     /gene="KLHL11"
                     /coded_by="NM_018143.3:54..2180"
                     /db_xref="CCDS:CCDS11411.1"
                     /db_xref="GeneID:55175"
                     /db_xref="HGNC:HGNC:19008"
                     /db_xref="MIM:619078"
ORIGIN      
        1 maaaavaaaa aaaaaaslqv lemesmetaa agsaglaaev rgsgtvdfgp gpgisameas
       61 ggdpgpeaed fecsshcsel swrqneqrrq glfcditlcf ggaggrefra hrsvlaaate
      121 yftpllsgqf sesrsgrvem rkwssepgpe pdtveaviey mytgrirvst gsvhevlela
      181 drfllirlke fcgeflkkkl hlsncvaihs lahmytlsql alkaadmirr nfhkviqdee
      241 fytlpfhlir dwlsdleitv dseevlfetv lkwvqrnaee reryfeelfk llrlsqmkpt
      301 yltrhvkper lvannevcvk lvadaverha lraeniqsgt cqhptshvsl lprygqnmdv
      361 imviggvseg gdylsecvgy fvdedrwvnl phihnhldgh avavtesyvy vagsmepgfa
      421 ktverynpnl ntwehvcslm trkhsfglte vkgklysigg hgnfspgfkd vtvynpeldk
      481 whnlesapki lrdvkalaie drfvyiaart pvdrdtedgl kavitcydte trqwqdvesl
      541 plidnycffq msvvnsnfyq tasccpksyc leneeavrki asqvsdeile slppevlsie
      601 gaaicyykdd vfiiggwkns ddidkqyrke ayrycaerkr wmllppmpqp rcratachvr
      661 ipyrylhgtq rypmpqnlmw qkdrirqmqe ihrhalnmrr vpssqiec
//
LOCUS       NP_068712                473 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit beta-3 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_068712 XP_942347
VERSION     NP_068712.1
DBSOURCE    REFSEQ: accession NM_021912.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 473)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 473)
  AUTHORS   Bundy,J., Shaw,J., Hammel,M., Nguyen,J., Robbins,C., Mercier,I. and
            Suryanarayanan,A.
  TITLE     Role of beta3 subunit of the GABA type A receptor in triple
            negative breast cancer proliferation, migration, and cell cycle
            progression
  JOURNAL   Cell Cycle 23 (4), 448-465 (2024)
   PUBMED   38623967
  REMARK    GeneRIF: Role of beta3 subunit of the GABA type A receptor in
            triple negative breast cancer proliferation, migration, and cell
            cycle progression.
REFERENCE   3  (residues 1 to 473)
  AUTHORS   Chen,J.Y., Chang,C.F., Huang,S.P., Huang,C.Y., Yu,C.C., Lin,V.C.,
            Geng,J.H., Li,C.Y., Lu,T.L. and Bao,B.Y.
  TITLE     Integrated analysis identifies GABRB3 as a biomarker in prostate
            cancer
  JOURNAL   BMC Med Genomics 17 (1), 41 (2024)
   PUBMED   38287309
  REMARK    GeneRIF: Integrated analysis identifies GABRB3 as a biomarker in
            prostate cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 473)
  AUTHORS   Lin,S.X.N., Ahring,P.K., Keramidas,A., Liao,V.W.Y., Moller,R.S.,
            Chebib,M. and Absalom,N.L.
  TITLE     Correlations of receptor desensitization of gain-of-function GABRB3
            variants with clinical severity
  JOURNAL   Brain 147 (1), 224-239 (2024)
   PUBMED   37647766
  REMARK    GeneRIF: Correlations of receptor desensitization of
            gain-of-function GABRB3 variants with clinical severity.
REFERENCE   5  (residues 1 to 473)
  AUTHORS   Togel,M., Mossier,B., Fuchs,K. and Sieghart,W.
  TITLE     gamma-Aminobutyric acidA receptors displaying association of gamma
            3-subunits with beta 2/3 and different alpha-subunits exhibit
            unique pharmacological properties
  JOURNAL   J Biol Chem 269 (17), 12993-12998 (1994)
   PUBMED   8175718
REFERENCE   6  (residues 1 to 473)
  AUTHORS   Knoll,J.H., Cheng,S.D. and Lalande,M.
  TITLE     Allele specificity of DNA replication timing in the
            Angelman/Prader-Willi syndrome imprinted chromosomal region
  JOURNAL   Nat Genet 6 (1), 41-46 (1994)
   PUBMED   8136833
REFERENCE   7  (residues 1 to 473)
  AUTHORS   Kirkness,E.F. and Fraser,C.M.
  TITLE     A strong promoter element is located between alternative exons of a
            gene encoding the human gamma-aminobutyric acid-type A receptor
            beta 3 subunit (GABRB3)
  JOURNAL   J Biol Chem 268 (6), 4420-4428 (1993)
   PUBMED   8382702
REFERENCE   8  (residues 1 to 473)
  AUTHORS   Saitoh,S., Kubota,T., Ohta,T., Jinno,Y., Niikawa,N., Sugimoto,T.,
            Wagstaff,J. and Lalande,M.
  TITLE     Familial Angelman syndrome caused by imprinted submicroscopic
            deletion encompassing GABAA receptor beta 3-subunit gene
  JOURNAL   Lancet 339 (8789), 366-367 (1992)
   PUBMED   1346439
REFERENCE   9  (residues 1 to 473)
  AUTHORS   Wagstaff,J., Chaillet,J.R. and Lalande,M.
  TITLE     The GABAA receptor beta 3 subunit gene: characterization of a human
            cDNA from chromosome 15q11q13 and mapping to a region of conserved
            synteny on mouse chromosome 7
  JOURNAL   Genomics 11 (4), 1071-1078 (1991)
   PUBMED   1664410
REFERENCE   10 (residues 1 to 473)
  AUTHORS   Wagstaff,J., Knoll,J.H., Fleming,J., Kirkness,E.F.,
            Martin-Gallardo,A., Greenberg,F., Graham,J.M. Jr., Menninger,J.,
            Ward,D., Venter,J.C. et al.
  TITLE     Localization of the gene encoding the GABAA receptor beta 3 subunit
            to the Angelman/Prader-Willi region of human chromosome 15
  JOURNAL   Am J Hum Genet 49 (2), 330-337 (1991)
   PUBMED   1714232
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315311.1, CD652458.1,
            BC010641.1 and AC009878.9.
            
            On Mar 4, 2006 this sequence version replaced XP_942347.1.
            
            Summary: This gene encodes a member of the ligand-gated ionic
            channel family. The encoded protein is one the subunits of a
            multi-subunit chloride channel that serves as the receptor for
            gamma-aminobutyric acid, a major inhibitory neurotransmitter of the
            mammalian nervous system. This gene is located on the long arm of
            chromosome 15 in a cluster with two other genes encoding related
            subunits of the family. This gene may be associated with the
            pathogenesis of several disorders including Angelman syndrome,
            Prader-Willi syndrome, nonsyndromic orofacial clefts, epilepsy and
            autism. Alternatively spliced transcript variants encoding distinct
            isoforms have been described. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) uses an alternate 5' terminal
            exon compared to variant 1. It encodes isoform 2, which is of the
            same length, but has a distinct N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2841439.1,
                                           SRR14038192.3922900.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..473
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q12"
     Protein         1..473
                     /product="gamma-aminobutyric acid receptor subunit beta-3
                     isoform 2 precursor"
                     /note="gamma-aminobutyric acid type A receptor beta3
                     subunit; gamma-aminobutyric acid A receptor beta 3;
                     GABA-alpha receptor beta-2 subunit; GABAA receptor beta-3
                     subunit; gamma-aminobutyric acid (GABA) A receptor, beta
                     3; gamma-aminobutyric acid type A receptor subunit beta 3;
                     GABAAR subunit beta-3"
                     /calculated_mol_wt=51937
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2460
     mat_peptide     23..473
                     /product="gamma-aminobutyric acid receptor subunit beta-3
                     isoform 2"
                     /calculated_mol_wt=51937
     Region          23..471
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     CDS             1..473
                     /gene="GABRB3"
                     /gene_synonym="DEE43; ECA5; EIEE43"
                     /coded_by="NM_021912.5:40..1461"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS10018.1"
                     /db_xref="GeneID:2562"
                     /db_xref="HGNC:HGNC:4083"
                     /db_xref="MIM:137192"
ORIGIN      
        1 mcsgllelll piwlswtlgt rgseprsvnd pgnmsfvket vdkllkgydi rlrpdfggpp
       61 vcvgmnidia sidmvsevnm dytltmyfqq ywrdkrlays giplnltldn rvadqlwvpd
      121 tyflndkksf vhgvtvknrm irlhpdgtvl yglritttaa cmmdlrrypl deqnctleie
      181 sygyttddie fywrggdkav tgverielpq fsivehrlvs rnvvfatgay prlslsfrlk
      241 rnigyfilqt ympsilitil swvsfwinyd asaarvalgi ttvltmttin thlretlpki
      301 pyvkaidmyl mgcfvfvfla lleyafvnyi ffgrgpqrqk klaektakak ndrsksesnr
      361 vdahgnillt slevhnemne vsggigdtrn saisfdnsgi qyrkqsmpre ghgrflgdrs
      421 lphkkthlrr rssqlkikip dltdvnaidr wsrivfpftf slfnlvywly yvn
//
LOCUS       NP_001357521             222 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 4 [Homo sapiens].
ACCESSION   NP_001357521 XP_005257589
VERSION     NP_001357521.1
DBSOURCE    REFSEQ: accession NM_001370592.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5, AF225422.1 and
            BP308696.1.
            
            On May 14, 2019 this sequence version replaced XP_005257589.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.30332.1,
                                           SRR5189658.26544.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2161836 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325102.13/ ENSP00000321625.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..222
                     /product="MIF4G domain-containing protein isoform 4"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=25292
     Region          8..179
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..222
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001370592.1:139..807"
                     /note="isoform 4 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS56044.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqaeskqa gqsvfrrgll nrlqqeyqar eqlrarslqg wvcyvtficn ifdylrvnnm
      121 pmmalvnpvy dclfrlaqpd slskeeevdc lvlqlhrvge qlekmngqrm delfvlirdg
      181 fllptglssl aqlllleiie fraagwkttp aahkyyysev sd
//
LOCUS       NP_003835                468 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 10A [Homo
            sapiens].
ACCESSION   NP_003835
VERSION     NP_003835.3
DBSOURCE    REFSEQ: accession NM_003844.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Kiraly,P., Zupan,A., Matjasic,A. and Mekjavic,P.J.
  TITLE     Associations of Single-Nucleotide Polymorphisms in Slovenian
            Patients with Acute Central Serous Chorioretinopathy
  JOURNAL   Genes (Basel) 13 (1), 55 (2021)
   PUBMED   35052395
  REMARK    GeneRIF: Associations of Single-Nucleotide Polymorphisms in
            Slovenian Patients with Acute Central Serous Chorioretinopathy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Greenlee,J.D., Lopez-Cavestany,M., Ortiz-Otero,N., Liu,K.,
            Subramanian,T., Cagir,B. and King,M.R.
  TITLE     Oxaliplatin resistance in colorectal cancer enhances TRAIL
            sensitivity via death receptor 4 upregulation and lipid raft
            localization
  JOURNAL   Elife 10, e67750 (2021)
   PUBMED   34342264
  REMARK    GeneRIF: Oxaliplatin resistance in colorectal cancer enhances TRAIL
            sensitivity via death receptor 4 upregulation and lipid raft
            localization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Watanabe,A., Miyake,K., Akahane,K., Goi,K., Kagami,K., Yagita,H.
            and Inukai,T.
  TITLE     Epigenetic Modification of Death Receptor Genes for TRAIL and TRAIL
            Resistance in Childhood B-Cell Precursor Acute Lymphoblastic
            Leukemia
  JOURNAL   Genes (Basel) 12 (6), 864 (2021)
   PUBMED   34198757
  REMARK    GeneRIF: Epigenetic Modification of Death Receptor Genes for TRAIL
            and TRAIL Resistance in Childhood B-Cell Precursor Acute
            Lymphoblastic Leukemia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Khorshied,M., Soliman,N., Khorshid,O. and Bakr,S.
  TITLE     Genetic variations in tumor ecrosis factor related
            apoptosis-inducing ligand receptor-1 (TRAIL-R1) gene and the
            susceptibility to b-cell non-hodgkin lymphoma (B-NHL) in Egypt
  JOURNAL   Cancer Biomark 32 (4), 451-458 (2021)
   PUBMED   34275891
  REMARK    GeneRIF: Genetic variations in tumor ecrosis factor related
            apoptosis-inducing ligand receptor-1 (TRAIL-R1) gene and the
            susceptibility to b-cell non-hodgkin lymphoma (B-NHL) in Egypt.
            Erratum:[Cancer Biomark. 2022;33(2):275. doi: 10.3233/CBM-209786.
            PMID: 35068443]
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Schneider,P., Bodmer,J.L., Thome,M., Hofmann,K., Holler,N. and
            Tschopp,J.
  TITLE     Characterization of two receptors for TRAIL
  JOURNAL   FEBS Lett 416 (3), 329-334 (1997)
   PUBMED   9373179
REFERENCE   7  (residues 1 to 468)
  AUTHORS   MacFarlane,M., Ahmad,M., Srinivasula,S.M., Fernandes-Alnemri,T.,
            Cohen,G.M. and Alnemri,E.S.
  TITLE     Identification and molecular cloning of two novel receptors for the
            cytotoxic ligand TRAIL
  JOURNAL   J Biol Chem 272 (41), 25417-25420 (1997)
   PUBMED   9325248
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Walczak,H., Degli-Esposti,M.A., Johnson,R.S., Smolak,P.J.,
            Waugh,J.Y., Boiani,N., Timour,M.S., Gerhart,M.J., Schooley,K.A.,
            Smith,C.A., Goodwin,R.G. and Rauch,C.T.
  TITLE     TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL
  JOURNAL   EMBO J 16 (17), 5386-5397 (1997)
   PUBMED   9311998
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Pan,G., O'Rourke,K., Chinnaiyan,A.M., Gentz,R., Ebner,R., Ni,J. and
            Dixit,V.M.
  TITLE     The receptor for the cytotoxic ligand TRAIL
  JOURNAL   Science 276 (5309), 111-113 (1997)
   PUBMED   9082980
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Fleury,S., Thibodeau,J., Croteau,G., Labrecque,N., Aronson,H.E.,
            Cantin,C., Long,E.O. and Sekaly,R.P.
  TITLE     HLA-DR polymorphism affects the interaction with CD4
  JOURNAL   J Exp Med 182 (3), 733-741 (1995)
   PUBMED   7650480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012866.1, CN423254.1 and
            AC100861.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 28, 2009 this sequence version replaced NP_003835.2.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor is activated by tumor
            necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL),
            and thus transduces cell death signal and induces cell apoptosis.
            Studies with FADD-deficient mice suggested that FADD, a death
            domain containing adaptor protein, is required for the apoptosis
            mediated by this protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.404726.1,
                                           SRR6380201.98557.17 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221132.8/ ENSP00000221132.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..468
                     /product="tumor necrosis factor receptor superfamily
                     member 10A"
                     /note="death receptor 4; cytotoxic TRAIL receptor;
                     TRAIL-R1; TRAIL receptor 1; TNF-related apoptosis-inducing
                     ligand receptor 1; tumor necrosis factor receptor
                     superfamily, member 10a"
                     /calculated_mol_wt=49958
     Region          17..82
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00220.3)"
     Site            52
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O00220.3)"
     Region          107..145
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00220.3)"
     Region          129..230
                     /region_name="TNFRSF10"
                     /note="Tumor necrosis factor receptor superfamily member
                     10 (TNFRSF10), includes TNFRSF10A (DR4), TNFRSF10B (DR5),
                     TNFRSF10C (DcR1) and TNFRSF10D (DcR2); cd10580"
                     /db_xref="CDD:276906"
     Site            order(129..131,138,140,157..158,160..163,165..166,205,226)
                     /site_type="other"
                     /note="Antibody binding [polypeptide binding]"
                     /db_xref="CDD:276906"
     Region          129..145
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276906"
     Region          147..188
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00220.3)"
     Region          148..188
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276906"
     Site            156
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00220.3)"
     Site            order(163,166,171,202..206)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276906"
     Region          189..229
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00220.3)"
     Region          190..229
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276906"
     Site            240..262
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00220.3)"
     Region          367..454
                     /region_name="Death_TRAILR_DR4_DR5"
                     /note="Death domain of Tumor necrosis factor-Related
                     Apoptosis-Inducing Ligand Receptors; cd08315"
                     /db_xref="CDD:260027"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00220.3)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00220.3)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00220.3)"
     CDS             1..468
                     /gene="TNFRSF10A"
                     /gene_synonym="APO2; CD261; DR4; TRAILR-1; TRAILR1"
                     /coded_by="NM_003844.4:42..1448"
                     /db_xref="CCDS:CCDS6039.1"
                     /db_xref="GeneID:8797"
                     /db_xref="HGNC:HGNC:11904"
                     /db_xref="MIM:603611"
ORIGIN      
        1 mappparvhl gaflavtpnp gsaasgteaa aatpskvwgs sagrieprgg grgalptsmg
       61 qhgpsarara grapgprpar easprlrvhk tfkfvvvgvl lqvvpssaat iklhdqsigt
      121 qqwehsplge lcppgshrse hpgacnrcte gvgytnasnn lfaclpctac ksdeeerspc
      181 tttrntacqc kpgtfrndns aemcrkcsrg cprgmvkvkd ctpwsdiecv hkesgnghni
      241 wvilvvtlvv plllvavliv cccigsgcgg dpkcmdrvcf wrlgllrgpg aednahneil
      301 snadslstfv seqqmesqep adltgvtvqs pgeaqcllgp aeaegsqrrr llvpangadp
      361 tetlmlffdk fanivpfdsw dqlmrqldlt kneidvvrag tagpgdalya mlmkwvnktg
      421 rnasihtlld alermeerha rekiqdllvd sgkfiyledg tgsavsle
//
LOCUS       NP_742024                478 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and BTB/POZ domain-containing protein 1 isoform 2
            [Homo sapiens].
ACCESSION   NP_742024
VERSION     NP_742024.1
DBSOURCE    REFSEQ: accession NM_172027.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Kitamura,H., Ozono,E., Iwanaga,R., Bradford,A.P., Okuno,J.,
            Shimizu,E., Kurayoshi,K., Kugawa,K., Toh,H. and Ohtani,K.
  TITLE     Identification of novel target genes specifically activated by
            deregulated E2F in human normal fibroblasts
  JOURNAL   Genes Cells 20 (9), 739-757 (2015)
   PUBMED   26201719
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Koiwai,K., Maezawa,S., Hayano,T., Iitsuka,M. and Koiwai,O.
  TITLE     BPOZ-2 directly binds to eEF1A1 to promote eEF1A1 ubiquitylation
            and degradation and prevent translation
  JOURNAL   Genes Cells 13 (6), 593-607 (2008)
   PUBMED   18459963
  REMARK    GeneRIF: BPOZ-2 promoted eEF1A1 ubiquitylation and degradation,
            suggesting that eEF1A1 is a substrate of BPOZ-2.
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Maezawa,S., Hayano,T., Koiwai,K., Fukushima,R., Kouda,K., Kubota,T.
            and Koiwai,O.
  TITLE     Bood POZ containing gene type 2 is a human counterpart of yeast
            Btb3p and promotes the degradation of terminal
            deoxynucleotidyltransferase
  JOURNAL   Genes Cells 13 (5), 439-457 (2008)
   PUBMED   18429817
  REMARK    GeneRIF: Study showed that BPOZ-2 is a human counterpart of yeast
            Btb3p, which is a putative adaptor for Pcu3p-based ubiquitin
            ligase; BPOZ-2 bound to E3 ligase CUL3 in vitro and in vivo.
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Unoki,M. and Nakamura,Y.
  TITLE     Growth-suppressive effects of BPOZ and EGR2, two genes involved in
            the PTEN signaling pathway
  JOURNAL   Oncogene 20 (33), 4457-4465 (2001)
   PUBMED   11494141
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Dai,K.S., Wei,W. and Liew,C.C.
  TITLE     Molecular cloning and characterization of a novel human gene
            containing ankyrin repeat and double BTB/POZ domain
  JOURNAL   Biochem Biophys Res Commun 273 (3), 991-996 (2000)
   PUBMED   10891360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF664138.1, AB053325.1,
            AI337369.1 and BM671027.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with an ankyrin repeat region
            and two BTB/POZ domains, which are thought to be involved in
            protein-protein interactions. Expression of this gene is activated
            by the phosphatase and tensin homolog, a tumor suppressor.
            Alternate splicing results in three transcript variants. [provided
            by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2, also known as BPOZ type 2)
            encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1171313.1,
                                           SRR3476690.727347.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000232744.13/ ENSP00000232744.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
     Protein         1..478
                     /product="ankyrin repeat and BTB/POZ domain-containing
                     protein 1 isoform 2"
                     /note="elongation factor 1A-binding protein; ankyrin
                     repeat and BTB (POZ) domain containing 1"
                     /calculated_mol_wt=53848
     Region          1..31
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969K4.1)"
     Region          <6..118
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          35..66
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          35..64
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969K4.1)"
     Region          97..214
                     /region_name="BTB1_POZ_ABTB1_BPOZ1"
                     /note="first BTB (Broad-Complex, Tramtrack and Bric a
                     brac)/POZ (poxvirus and zinc finger) domain found in
                     Ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18295"
                     /db_xref="CDD:349604"
     Region          254..377
                     /region_name="BTB2_POZ_ABTB1_BPOZ1"
                     /note="second BTB (Broad-Complex, Tramtrack and Bric a
                     brac)/POZ (poxvirus and zinc finger) domain found in
                     Ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18296"
                     /db_xref="CDD:349605"
     Region          376..447
                     /region_name="BACK_ABTB1_BPOZ"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     ankyrin repeat and BTB/POZ domain-containing protein 1
                     (ABTB1); cd18497"
                     /db_xref="CDD:350572"
     CDS             1..478
                     /gene="ABTB1"
                     /gene_synonym="BPOZ; BPOZ-2; BTB3; BTBD21; EF1ABP; PP2259"
                     /coded_by="NM_172027.3:75..1511"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3045.1"
                     /db_xref="GeneID:80325"
                     /db_xref="HGNC:HGNC:18275"
                     /db_xref="MIM:608308"
ORIGIN      
        1 mdtsdlfasc rkgdvgrvry lleqrdvevn vrdkwdstpl yyaclcghee lvlyllanga
       61 rceantfdge rclygalsdp irralrdykq vtascrrrdy yddflqrlle qgihsdvvfv
      121 vhgkpfrvhr cvlgarsayf anmldtkwkg ksvvvlrhpl inpvafgall qylytgrldi
      181 gvehvsdcer lakqcqlwdl lsdleakcek vsefvaskpg tcvkvltiep ppadprlred
      241 malladcalp pelrgdlwel pfpcpdgfns cpdicfrvag csflchkaff cgrsdyfral
      301 lddhfresee patsggppav tlhgispdvf thvlyymysd htelspeaay dvlsvadmyl
      361 lpglkrlcgr slaqmldedt vvgvwrvakl frlarledqc teymakviek lveredfvea
      421 vkeeaaavaa rqetdsiplv ddirfhvast vqtysaieea qqrlraledl lvsigldc
//
LOCUS       NP_001357526            1190 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase ID isoform e [Homo sapiens].
ACCESSION   NP_001357526
VERSION     NP_001357526.1
DBSOURCE    REFSEQ: accession NM_001370597.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1190)
  AUTHORS   Honsho,M., Mawatari,S. and Fujiki,Y.
  TITLE     ATP8B2-Mediated Asymmetric Distribution of Plasmalogens Regulates
            Plasmalogen Homeostasis and Plays a Role in Intracellular Signaling
  JOURNAL   Front Mol Biosci 9, 915457 (2022)
   PUBMED   35832735
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1190)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1190)
  AUTHORS   Takatsu,H., Tanaka,G., Segawa,K., Suzuki,J., Nagata,S., Nakayama,K.
            and Shin,H.W.
  TITLE     Phospholipid flippase activities and substrate specificities of
            human type IV P-type ATPases localized to the plasma membrane
  JOURNAL   J Biol Chem 289 (48), 33543-33556 (2014)
   PUBMED   25315773
  REMARK    Erratum:[J Biol Chem. 2016 Oct 7;291(41):21421. doi:
            10.1074/jbc.A114.593012. PMID: 27825076]
REFERENCE   4  (residues 1 to 1190)
  AUTHORS   Bryde,S., Hennrich,H., Verhulst,P.M., Devaux,P.F., Lenoir,G. and
            Holthuis,J.C.
  TITLE     CDC50 proteins are critical components of the human class-1
            P4-ATPase transport machinery
  JOURNAL   J Biol Chem 285 (52), 40562-40572 (2010)
   PUBMED   20961850
REFERENCE   5  (residues 1 to 1190)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   6  (residues 1 to 1190)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   7  (residues 1 to 1190)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   8  (residues 1 to 1190)
  AUTHORS   Harris,M.J. and Arias,I.M.
  TITLE     FIC1, a P-type ATPase linked to cholestatic liver disease, has
            homologues (ATP8B2 and ATP8B3) expressed throughout the body
  JOURNAL   Biochim Biophys Acta 1633 (2), 127-131 (2003)
   PUBMED   12880872
REFERENCE   9  (residues 1 to 1190)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1190)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162591.16.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.46644.1,
                                           SRR1803615.166442.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368489.6/ ENSP00000357475.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1190
                     /product="phospholipid-transporting ATPase ID isoform e"
                     /EC_number="7.6.2.1"
                     /note="phospholipid-transporting ATPase ID; probable
                     phospholipid-transporting ATPase ID; ATPase, class I, type
                     8B, member 2; P4-ATPase flippase complex alpha subunit
                     ATP8B2; 36/8-9 fusion protein with epitope for anti-lectin
                     antibody; ATPase, aminophospholipid transporter, class I,
                     type 8B, member 2"
                     /calculated_mol_wt=135041
     Region          31..972
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            order(392..394,537,560..562,627,674..676,788,791,794,814,
                     817)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     CDS             1..1190
                     /gene="ATP8B2"
                     /gene_synonym="ATPID"
                     /coded_by="NM_001370597.1:216..3788"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS1066.2"
                     /db_xref="GeneID:57198"
                     /db_xref="HGNC:HGNC:13534"
                     /db_xref="MIM:605867"
ORIGIN      
        1 mavcakkrpp eeerrarand reynekfqya snciktskyn iltflpvnlf eqfqevanty
       61 flfllilqli pqisslswft tivplvlvlt itavkdatdd yfrhksdnqv nnrqsqvlin
      121 gilqqeqwmn vcvgdiikle nnqfvaadll llsssephgl cyietaeldg etnmkvrqai
      181 pvtselgdis klakfdgevi ceppnnkldk fsgtlywken kfplsnqnml lrgcvlrnte
      241 wcfglvifag pdtklmqnsg rtkfkrtsid rlmntlvlwi fgflvcmgvi laignaiweh
      301 evgmrfqvyl pwdeavdsaf fsgflsfwsy iiilntvvpi slyvsvevir lghsyfinwd
      361 kkmfcmkkrt paeartttln eelgqveyif sdktgtltqn imvfnkcsin ghsygdvfdv
      421 lghkaelger pepvdfsfnp ladkkflfwd pslleavkig dphtheffrl lslchtvmse
      481 eknegelyyk aqspdegalv taarnfgfvf rsrtpktitv hemgtaityq llaildfnni
      541 rkrmsvivrn pegkirlyck gadtilldrl hhstqellnt tmdhlneyag eglrtlvlay
      601 kdldeeyyee waerrlqasl aqdsredrla siyeevennm mllgataied klqqgvpeti
      661 alltlaniki wvltgdkqet avnigysckm ltddmtevfi vtghtvlevr eelrkarekm
      721 mdssrsvgng ftyqdklsss kltsvleava geyalvingh slahaleadm elefletaca
      781 ckaviccrvt plqkaqvvel vkkykkavtl aigdgandvs miktahigvg isgqegiqav
      841 lasdysfsqf kflqrlllvh grwsylrmck flcyffyknf aftmvhfwfg ffcgfsaqtv
      901 ydqyfitlyn ivytslpvla mgvfdqdvpe qrsmeypkly epgqlnllfn krefficiaq
      961 giytsvlmff ipygvfadat rddgtqlady qsfavtvats lvivvsvqig ldtgywtain
     1021 hffiwgslav yfailfamhs nglfdmfpnq frfvgnaqnt laqptvwlti vlttvvcimp
     1081 vvafrflrln lkpdlsdtvr ytqlvrkkqk aqhrcmrrvg rtgsrrsgya fshqegfgel
     1141 imsgknmrls slalssfttr sssswieslr rkksdsassp sggadkplkg
//
LOCUS       NP_115875                182 aa            linear   PRI 20-NOV-2025
DEFINITION  dynactin subunit 5 isoform 1 [Homo sapiens].
ACCESSION   NP_115875
VERSION     NP_115875.1
DBSOURCE    REFSEQ: accession NM_032486.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Parisi,G., Fornasari,M.S. and Echave,J.
  TITLE     Dynactins p25 and p27 are predicted to adopt the LbetaH fold
  JOURNAL   FEBS Lett 562 (1-3), 1-4 (2004)
   PUBMED   15043994
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Eckley,D.M., Gill,S.R., Melkonian,K.A., Bingham,J.B., Goodson,H.V.,
            Heuser,J.E. and Schroer,T.A.
  TITLE     Analysis of dynactin subcomplexes reveals a novel actin-related
            protein associated with the arp1 minifilament pointed end
  JOURNAL   J Cell Biol 147 (2), 307-320 (1999)
   PUBMED   10525537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA310703.1, BC004191.2 and
            AC008870.8.
            
            Summary: This gene encodes a subunit of dynactin, a component of
            the cytoplasmic dynein motor machinery involved in
            minus-end-directed transport. The encoded protein is a component of
            the pointed-end subcomplex and is thought to bind membranous cargo.
            A pseudogene of this gene is located on the long arm of chromosome
            1. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.169035.1,
                                           SRR1803611.11422.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300087.7/ ENSP00000300087.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..182
                     /product="dynactin subunit 5 isoform 1"
                     /note="dynactin 4; dynactin subunit p25; dynactin 5 (p25)"
                     /calculated_mol_wt=19995
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BTE1.1)"
     Region          13..173
                     /region_name="LbH_Dynactin_5"
                     /note="Dynactin 5 (or subunit p25); Dynactin is a major
                     component of the activator complex that stimulates
                     dynein-mediated vesicle transport. Dynactin is a
                     heterocomplex of at least eight subunits, including a
                     150,000-MW protein called Glued, the actin-capping...;
                     cd03359"
                     /db_xref="CDD:100049"
     CDS             1..182
                     /gene="DCTN5"
                     /coded_by="NM_032486.4:78..626"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10615.1"
                     /db_xref="GeneID:84516"
                     /db_xref="HGNC:HGNC:24594"
                     /db_xref="MIM:612962"
ORIGIN      
        1 melgellynk seyietasgn kvsrqsvlcg sqnivlngkt ivmndciirg dlanvrvgrh
       61 cvvksrsvir ppfkkfskgv affplhigdh vfieedcvvn aaqigsyvhv gkncvigrrc
      121 vlkdcckild ntvlppetvv ppftvfsgcp glfsgelpec tqelmidvtk syyqkflplt
      181 qv
//
LOCUS       NP_001305830             391 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate dehydrogenase 1, mitochondrial isoform c [Homo sapiens].
ACCESSION   NP_001305830 XP_011537970
VERSION     NP_001305830.1
DBSOURCE    REFSEQ: accession NM_001318901.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Qin,J., Zhao,Y., Li,S., Liu,Q., Huang,S. and Yu,X.
  TITLE     GDH1 exacerbates renal fibrosis by inhibiting the transcriptional
            activity of peroxisome proliferator-activated receptor gamma
  JOURNAL   FEBS J 291 (20), 4581-4601 (2024)
   PUBMED   39136063
  REMARK    GeneRIF: GDH1 exacerbates renal fibrosis by inhibiting the
            transcriptional activity of peroxisome proliferator-activated
            receptor gamma.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Tzimagiorgis,G., Leversha,M.A., Chroniary,K., Goulielmos,G.,
            Sargent,C.A., Ferguson-Smith,M. and Moschonas,N.K.
  TITLE     Structure and expression analysis of a member of the human
            glutamate dehydrogenase (GLUD) gene family mapped to chromosome
            10p11.2
  JOURNAL   Hum Genet 91 (5), 433-438 (1993)
   PUBMED   8314555
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Gillis,D.
  TITLE     Nonsyndromic Genetic Hyperinsulinism Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301549
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Nakatani,Y., Schneider,M., Banner,C. and Freese,E.
  TITLE     Complete nucleotide sequence of human glutamate dehydrogenase cDNA
  JOURNAL   Nucleic Acids Res 16 (13), 6237 (1988)
   PUBMED   3399399
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Amuro,N., Yamaura,M., Goto,Y. and Okazaki,T.
  TITLE     Molecular cloning and nucleotide sequence of the cDNA for human
            liver glutamate dehydrogenase precursor
  JOURNAL   Biochem Biophys Res Commun 152 (3), 1395-1400 (1988)
   PUBMED   3377777
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Mavrothalassitis,G., Tzimagiorgis,G., Mitsialis,A., Zannis,V.,
            Plaitakis,A., Papamatheakis,J. and Moschonas,N.
  TITLE     Isolation and characterization of cDNA clones encoding human liver
            glutamate dehydrogenase: evidence for a small gene family
  JOURNAL   Proc Natl Acad Sci U S A 85 (10), 3494-3498 (1988)
   PUBMED   3368458
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Banner,C., Silverman,S., Thomas,J.W., Lampel,K.A., Vitkovic,L.,
            Huie,D. and Wenthold,R.J.
  TITLE     Isolation of a human brain cDNA for glutamate dehydrogenase
  JOURNAL   J Neurochem 49 (1), 246-252 (1987)
   PUBMED   3585334
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Julliard,J.H. and Smith,E.L.
  TITLE     Partial amino acid sequence of the glutamate dehydrogenase of human
            liver and a revision of the sequence of the bovine enzyme
  JOURNAL   J Biol Chem 254 (9), 3427-3438 (1979)
   PUBMED   429360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294685.1, AK122685.1,
            BC112946.1 and AF086070.2.
            
            On Jan 15, 2016 this sequence version replaced XP_011537970.1.
            
            Summary: This gene encodes glutamate dehydrogenase, which is a
            mitochondrial matrix enzyme that catalyzes the oxidative
            deamination of glutamate to alpha-ketoglutarate and ammonia. This
            enzyme has an important role in regulating amino acid-induced
            insulin secretion. It is allosterically activated by ADP and
            inhibited by GTP and ATP. Activating mutations in this gene are a
            common cause of congenital hyperinsulinism. Alternative splicing of
            this gene results in multiple transcript variants. The related
            glutamate dehydrogenase 2 gene on the human X-chromosome originated
            from this gene via retrotransposition and encodes a soluble form of
            glutamate dehydrogenase. Related pseudogenes have been identified
            on chromosomes 10, 18 and X. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) contains alternate 5' exon
            structure, and it thus differs in its 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (c) is shorter at the N-terminus,
            compared to isoform a. Variants 3, 4, 5, 6 and 7 all encode isoform
            c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122685.1, SRR14038193.1116929.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.2"
     Protein         1..391
                     /product="glutamate dehydrogenase 1, mitochondrial isoform
                     c"
                     /EC_number="1.4.1.3"
                     /note="glutamate dehydrogenase 1, mitochondrial; glutamate
                     dehydrogenase (NAD(P)+); epididymis tissue sperm binding
                     protein Li 18mP; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=42819
     Region          <1..388
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
     CDS             1..391
                     /gene="GLUD1"
                     /gene_synonym="GDH; GDH1; GLUD; hGDH1"
                     /coded_by="NM_001318901.1:565..1740"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91291.1"
                     /db_xref="GeneID:2746"
                     /db_xref="HGNC:HGNC:4335"
                     /db_xref="MIM:138130"
ORIGIN      
        1 mtykcavvdv pfggakagvk inpknytdne lekitrrftm elakkgfigp gidvpapdms
       61 tgeremswia dtyastighy dinahacvtg kpisqggihg risatgrgvf hgienfinea
      121 symsilgmtp gfgdktfvvq gfgnvglhsm rylhrfgakc iavgesdgsi wnpdgidpke
      181 ledfklqhgs ilgfpkakpy egsileadcd ilipaasekq ltksnaprvk akiiaegang
      241 pttpeadkif lernimvipd lylnaggvtv syfewlknln hvsygrltfk yerdsnyhll
      301 msvqeslerk fgkhggtipi vptaefqdri sgasekdivh sglaytmers arqimrtamk
      361 ynlgldlrta ayvnaiekvf kvyneagvtf t
//
LOCUS       NP_001004434             372 aa            linear   PRI 20-NOV-2025
DEFINITION  proton-coupled zinc antiporter SLC30A2 isoform 1 [Homo sapiens].
ACCESSION   NP_001004434
VERSION     NP_001004434.1
DBSOURCE    REFSEQ: accession NM_001004434.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Escobar,A., Styrpejko,D.J., Ali,S. and Cuajungco,M.P.
  TITLE     Transmembrane 163 (TMEM163) protein interacts with specific
            mammalian SLC30 zinc efflux transporter family members
  JOURNAL   Biochem Biophys Rep 32, 101362 (2022)
   PUBMED   36204728
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Kelleher,S.L., Alam,S., Rivera,O.C., Barber-Zucker,S., Zarivach,R.,
            Wagatsuma,T., Kambe,T., Soybel,D.I., Wright,J. and Lamendella,R.
  TITLE     Loss-of-function SLC30A2 mutants are associated with gut dysbiosis
            and alterations in intestinal gene expression in preterm infants
  JOURNAL   Gut Microbes 14 (1), 2014739 (2022)
   PUBMED   34965180
  REMARK    GeneRIF: Loss-of-function SLC30A2 mutants are associated with gut
            dysbiosis and alterations in intestinal gene expression in preterm
            infants.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Rivera,O.C., Geddes,D.T., Barber-Zucker,S., Zarivach,R., Gagnon,A.,
            Soybel,D.I. and Kelleher,S.L.
  TITLE     A common genetic variant in zinc transporter ZnT2 (Thr288Ser) is
            present in women with low milk volume and alters lysosome function
            and cell energetics
  JOURNAL   Am J Physiol Cell Physiol 318 (6), C1166-C1177 (2020)
   PUBMED   32320289
  REMARK    GeneRIF: Thr288Ser mutation in SLC30A2/ZnT2 impairs critical
            functions of mammary epithelial cells, resulting in milk volume and
            altering lysosome function and cell energetics.
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Overbeck,S., Uciechowski,P., Ackland,M.L., Ford,D. and Rink,L.
  TITLE     Intracellular zinc homeostasis in leukocyte subsets is regulated by
            different expression of zinc exporters ZnT-1 to ZnT-9
  JOURNAL   J Leukoc Biol 83 (2), 368-380 (2008)
   PUBMED   17971500
  REMARK    GeneRIF: hZnT-2 was not detectable in leukocytes.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
  REMARK    GeneRIF: ZnT2 can facilitate vesicular zinc accumulation
            independently of AP-3 function, and validate the M1 fibroblastoid
            line as a human cell culture system amenable to the study of
            vesicular zinc regulation.
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Chowanadisai,W., Lonnerdal,B. and Kelleher,S.L.
  TITLE     Identification of a mutation in SLC30A2 (ZnT-2) in women with low
            milk zinc concentration that results in transient neonatal zinc
            deficiency
  JOURNAL   J Biol Chem 281 (51), 39699-39707 (2006)
   PUBMED   17065149
  REMARK    GeneRIF: a mutation in SLC30A2 (ZnT-2) may have a role in transient
            neonatal zinc deficiency
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Palmiter,R.D., Cole,T.B. and Findley,S.D.
  TITLE     ZnT-2, a mammalian protein that confers resistance to zinc by
            facilitating vesicular sequestration
  JOURNAL   EMBO J 15 (8), 1784-1791 (1996)
   PUBMED   8617223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR004258.1, AF370409.1,
            AL391650.18 and AI161067.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a zinc transporter
            that acts as a homodimer. The encoded protein plays a role in
            secreting zinc into breast milk. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Aug 2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF370409.1, ERR279833.8297.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374276.4/ ENSP00000363394.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..372
                     /product="proton-coupled zinc antiporter SLC30A2 isoform
                     1"
                     /note="zinc transporter 2; solute carrier family 30 (zinc
                     transporter), member 2; proton-coupled zinc antiporter
                     SLC30A2"
                     /calculated_mol_wt=40433
     Region          51..54
                     /region_name="Mitochondrial localization signal.
                     /evidence=ECO:0000269|PubMed:21289295"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Region          83..357
                     /region_name="CDF"
                     /note="cation diffusion facilitator family transporter;
                     TIGR01297"
                     /db_xref="CDD:273544"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Site            250..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Region          294..295
                     /region_name="Lysosomal targeting motif.
                     /evidence=ECO:0000303|PubMed:25808614"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:25808614; propagated from
                     UniProtKB/Swiss-Prot (Q9BRI3.2)"
     Site            305..325
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRI3.2)"
     CDS             1..372
                     /gene="SLC30A2"
                     /gene_synonym="PP12488; TNZD; ZnT-2; ZNT2"
                     /coded_by="NM_001004434.3:223..1341"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30644.1"
                     /db_xref="GeneID:7780"
                     /db_xref="HGNC:HGNC:11013"
                     /db_xref="MIM:609617"
ORIGIN      
        1 meakekqhll darpairsyt gslwqegagw iplprpgldl qaielaaqsn hhchaqkgpd
       61 shcdpkkgka qrqlyvasai cllfmigevv ggylahslav mtdaahlltd fasmlislfs
      121 lwmssrpatk tmnfgwqrae ilgalvsvls iwvvtgvlvy laverlisgd yeidggtmli
      181 tsgcavavni imgltlhqsg hghshgttnq qeenpsvraa fihvigdfmq smgvlvaayi
      241 lyfkpeykyv dpictfvfsi lvlgttltil rdvilvlmeg tpkgvdftav rdlllsvegv
      301 ealhslhiwa ltvaqpvlsv hiaiaqntda qavlktassr lqgkfhfhtv tiqiedysed
      361 mkdcqacqgp sd
//
LOCUS       NP_004921                272 aa            linear   PRI 20-NOV-2025
DEFINITION  F-actin-capping protein subunit beta isoform 1 [Homo sapiens].
ACCESSION   NP_004921
VERSION     NP_004921.1
DBSOURCE    REFSEQ: accession NM_004930.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Carman,P.J., Barrie,K.R., Rebowski,G. and Dominguez,R.
  TITLE     Structures of the free and capped ends of the actin filament
  JOURNAL   Science 380 (6651), 1287-1292 (2023)
   PUBMED   37228182
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Wells,C.D., Fawcett,J.P., Traweger,A., Yamanaka,Y., Goudreault,M.,
            Elder,K., Kulkarni,S., Gish,G., Virag,C., Lim,C., Colwill,K.,
            Starostine,A., Metalnikov,P. and Pawson,T.
  TITLE     A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
            proteins in epithelial cells
  JOURNAL   Cell 125 (3), 535-548 (2006)
   PUBMED   16678097
REFERENCE   6  (residues 1 to 272)
  AUTHORS   Yang,C., Pring,M., Wear,M.A., Huang,M., Cooper,J.A., Svitkina,T.M.
            and Zigmond,S.H.
  TITLE     Mammalian CARMIL inhibits actin filament capping by capping protein
  JOURNAL   Dev Cell 9 (2), 209-221 (2005)
   PUBMED   16054028
REFERENCE   7  (residues 1 to 272)
  AUTHORS   Olavesen,M.G., Bentley,E., Mason,R.V., Stephens,R.J. and
            Ragoussis,J.
  TITLE     Fine mapping of 39 ESTs on human chromosome 6p23-p25
  JOURNAL   Genomics 46 (2), 303-306 (1997)
   PUBMED   9417921
REFERENCE   8  (residues 1 to 272)
  AUTHORS   Kuhlman,P.A. and Fowler,V.M.
  TITLE     Purification and characterization of an alpha 1 beta 2 isoform of
            CapZ from human erythrocytes: cytosolic location and inability to
            bind to Mg2+ ghosts suggest that erythrocyte actin filaments are
            capped by adducin
  JOURNAL   Biochemistry 36 (44), 13461-13472 (1997)
   PUBMED   9354614
REFERENCE   9  (residues 1 to 272)
  AUTHORS   Hart,M.C., Korshunova,Y.O. and Cooper,J.A.
  TITLE     Vertebrates have conserved capping protein alpha isoforms with
            specific expression patterns
  JOURNAL   Cell Motil Cytoskeleton 38 (2), 120-132 (1997)
   PUBMED   9331217
REFERENCE   10 (residues 1 to 272)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J Biol Chem 270 (37), 21472-21479 (1995)
   PUBMED   7665558
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY021163.1, BC107752.1,
            BC008095.1 and BQ773230.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the beta subunit of the barbed-end actin
            binding protein, which belongs to the F-actin capping protein
            family. The capping protein is a heterodimeric actin capping
            protein that blocks actin filament assembly and disassembly at the
            fast growing (barbed) filament ends and functions in regulating
            actin filament dynamics as well as in stabilizing actin filament
            lengths in muscle and nonmuscle cells. A pseudogene of this gene is
            located on the long arm of chromosome 2. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found.[provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.352082.1,
                                           SRR3476690.1160401.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264202.8/ ENSP00000264202.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..272
                     /product="F-actin-capping protein subunit beta isoform 1"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     epididymis secretory sperm binding protein; capping
                     protein (actin filament) muscle Z-line, beta; capping
                     actin protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=30498
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P47756.5)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47756.5)"
     Region          11..239
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P47756.5)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47756.5)"
     CDS             1..272
                     /gene="CAPZB"
                     /gene_synonym="CAPB; CAPPB; CAPZ"
                     /coded_by="NM_004930.5:102..920"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41277.1"
                     /db_xref="GeneID:832"
                     /db_xref="HGNC:HGNC:1491"
                     /db_xref="MIM:601572"
ORIGIN      
        1 msdqqldcal dlmrrlppqq ieknlsdlid lvpslcedll ssvdqplkia rdkvvgkdyl
       61 lcdynrdgds yrspwsnkyd ppledgamps arlrklevea nnafdqyrdl yfeggvssvy
      121 lwdldhgfag vilikkagdg skkikgcwds ihvvevqeks sgrtahyklt stvmlwlqtn
      181 ksgsgtmnlg gsltrqmekd etvsdcsphi anigrlvedm enkirstlne iyfgktkdiv
      241 nglrsvqtfa dkskqealkn dlvealkrkq qc
//
LOCUS       NP_001003674             269 aa            linear   PRI 20-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform gamma 1 [Homo sapiens].
ACCESSION   NP_001003674
VERSION     NP_001003674.1
DBSOURCE    REFSEQ: accession NM_001003674.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001010.4, AK055028.1, DA412541.1, DA391326.1, DA321390.1,
            AI878844.1, HY309264.1, AI668861.1 and AF009426.1.
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon, differs in its 5' UTR, lacks a portion of the 5'
            coding region, and initiates translation at an alternate start
            codon, compared to variant a1. The encoded isoform (gamma 1) is
            shorter and has a distinct N-terminus, compared to isoform alpha 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055028.1, SRR1660803.10505.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..269
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform gamma 1"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=29944
     CDS             1..269
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001003674.3:1242..2051"
                     /note="isoform gamma 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32795.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mssdhlnnst lkeaqfkdlf lkkaelefaq iiiivvvvtv mvvvivclln hykvstrsfi
       61 nrpnqsrrre dglpqegclw psdsaaprlg aseimhaprs rdrftapsfi qrdrfsrfqp
      121 typyvqheid lpptislsdg eepppyqgpc tlqlrdpeqq melnresvra ppnrtifdsd
      181 lidiamysgg pcppssnsgi sastcssngr megppptyse vmghhpgasf lhhqrsnahr
      241 gsrlqfqqnn aestivpikg kdrkpgnlv
//
LOCUS       NP_006074                557 aa            linear   PRI 20-NOV-2025
DEFINITION  protein Red [Homo sapiens].
ACCESSION   NP_006074 NP_004502
VERSION     NP_006074.2
DBSOURCE    REFSEQ: accession NM_006083.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 557)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 557)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 557)
  AUTHORS   von Elsner,L., Chai,G., Schneeberger,P.E., Harms,F.L., Casar,C.,
            Qi,M., Alawi,M., Abdel-Salam,G.M.H., Zaki,M.S., Arndt,F., Yang,X.,
            Stanley,V., Hempel,M., Gleeson,J.G. and Kutsche,K.
  TITLE     Biallelic FRA10AC1 variants cause a neurodevelopmental disorder
            with growth retardation
  JOURNAL   Brain 145 (4), 1551-1563 (2022)
   PUBMED   34694367
REFERENCE   4  (residues 1 to 557)
  AUTHORS   Gao,C., Han,Y., Bai,L., Wang,Y. and Xue,F.
  TITLE     IK: A novel cell mitosis regulator that contributes to
            carcinogenesis
  JOURNAL   Cell Biochem Funct 39 (7), 854-859 (2021)
   PUBMED   34250629
  REMARK    GeneRIF: IK: A novel cell mitosis regulator that contributes to
            carcinogenesis.
            Review article
REFERENCE   5  (residues 1 to 557)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 557)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 557)
  AUTHORS   Willers,J., Haffner,A., Zepter,K., Storz,M., Urosevic,M., Burg,G.
            and Dummer,R.
  TITLE     The interferon inhibiting cytokine IK is overexpressed in cutaneous
            T cell lymphoma derived tumor cells that fail to upregulate major
            histocompatibility complex class II upon interferon-gamma
            stimulation
  JOURNAL   J Invest Dermatol 116 (6), 874-879 (2001)
   PUBMED   11407974
REFERENCE   8  (residues 1 to 557)
  AUTHORS   Assier,E., Bouzinba-Segard,H., Stolzenberg,M.C., Stephens,R.,
            Bardos,J., Freemont,P., Charron,D., Trowsdale,J. and Rich,T.
  TITLE     Isolation, sequencing and expression of RED, a novel human gene
            encoding an acidic-basic dipeptide repeat
  JOURNAL   Gene 230 (2), 145-154 (1999)
   PUBMED   10216252
REFERENCE   9  (residues 1 to 557)
  AUTHORS   Cao,L.X., Le Bousse-Kerdiles,M.C., Clay,D., Oshevski,S., Jasmin,C.
            and Krief,P.
  TITLE     Implication of a new molecule IK in CD34+ hematopoietic progenitor
            cell proliferation and differentiation
  JOURNAL   Blood 89 (10), 3615-3623 (1997)
   PUBMED   9160666
REFERENCE   10 (residues 1 to 557)
  AUTHORS   Krief,P., Augery-Bourget,Y., Plaisance,S., Merck,M.F., Assier,E.,
            Tanchou,V., Billard,M., Boucheix,C., Jasmin,C. and Azzarone,B.
  TITLE     A new cytokine (IK) down-regulating HLA class II: monoclonal
            antibodies, cloning and chromosome localization
  JOURNAL   Oncogene 9 (12), 3449-3456 (1994)
   PUBMED   7970704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF182645.1, BC071964.1 and
            BC013005.2.
            
            On Feb 16, 2007 this sequence version replaced NP_006074.1.
            
            Summary: The protein encoded by this gene was identified by its RED
            repeat, a stretch of repeated arginine, glutamic acid and aspartic
            acid residues. The protein localizes to discrete dots within the
            nucleus, excluding the nucleolus. Its function is unknown. This
            gene maps to chromosome 5; however, a pseudogene may exist on
            chromosome 2. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.680642.1,
                                           SRR3476690.957447.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417647.7/ ENSP00000396301.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..557
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..557
                     /product="protein Red"
                     /note="RD element; prer protein; IK factor; IK cytokine,
                     down-regulator of HLA II; chondrosarcoma-associated
                     protein 2; cytokine IK"
                     /calculated_mol_wt=65471
     Region          1..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Region          84..295
                     /region_name="RED_N"
                     /note="RED-like protein N-terminal region; pfam07808"
                     /db_xref="CDD:462273"
     Site            98
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1M8; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          181..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          294..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Region          342..375
                     /region_name="17 X 2 AA tandem repeats of R-[ED]"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13123.3)"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Region          445..549
                     /region_name="RED_C"
                     /note="RED-like protein C-terminal region; pfam07807"
                     /db_xref="CDD:462272"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13123.3)"
     CDS             1..557
                     /gene="IK"
                     /gene_synonym="CSA2; RED; RER"
                     /coded_by="NM_006083.4:81..1754"
                     /db_xref="CCDS:CCDS47280.1"
                     /db_xref="GeneID:3550"
                     /db_xref="HGNC:HGNC:5958"
                     /db_xref="MIM:600549"
ORIGIN      
        1 mperdsepfs nplapdghdv ddphsfhqsk ltnedfrkll mtpraaptsa ppsksrhhem
       61 preynededp aarrrkkksy yaklrqqeie rerelaekyr drakerrdgv nkdyeeteli
      121 sttanyravg ptaeadksaa ekrrqliqes kflggdmeht hlvkgldfal lqkvraeias
      181 kekeeeelme kpqketkkde dpenkiefkt rlgrnvyrml fkskayerne lflpgrmayv
      241 vdlddeyadt dipttlirsk adcptmeaqt tlttndivis kltqilsylr qgtrnkklkk
      301 kdkgkleekk ppeadmnife digdyvpstt ktprdkerer yrererdrer drdrdrerer
      361 erdrererer drereeekkr hsyfekpkvd depmdvdkgp gstkeliksi nekfagsagw
      421 egteslkkpe dkkqlgdffg msnsyaecyp atmddmavds deevdyskmd qgnkkgplgr
      481 wdfdtqeeys eymnnkealp kaafqygikm segrktrrfk etndkaeldr qwkkisaiie
      541 krkkmeadgv evkrpky
//
LOCUS       NP_001350453             635 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich repeat and fibronectin type-III domain-containing
            protein 4 precursor [Homo sapiens].
ACCESSION   NP_001350453 XP_005274296
VERSION     NP_001350453.1
DBSOURCE    REFSEQ: accession NM_001363524.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 635)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 635)
  AUTHORS   Zheng,F., Zhai,X.L., Wang,W.J., Guo,K.P., Xiao,C.C. and Ni,Q.C.
  TITLE     [Expression and clinical significance of LRFN4 in colorectal cancer
            tissue]
  JOURNAL   Zhonghua Yi Xue Za Zhi 100 (22), 1745-1749 (2020)
   PUBMED   32536098
  REMARK    GeneRIF: [Expression and clinical significance of LRFN4 in
            colorectal cancer tissue].
REFERENCE   3  (residues 1 to 635)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 635)
  AUTHORS   Liu,Y., Chen,X., Chen,X., Yang,X., Song,Q. and Wu,H.
  TITLE     High SALM3 Expression in Tumor Cells and Fibroblasts Is Correlated
            with Poor Prognosis in Gastric Cancer Patients
  JOURNAL   Dis Markers 2019, 8282414 (2019)
   PUBMED   31089399
  REMARK    GeneRIF: SALM3 is overexpressed in the tumor cells and fibroblasts
            of gastric cancer patients.  High SALM3 expression is associated
            with poor prognosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 635)
  AUTHORS   Li,Y., Zhang,P., Choi,T.Y., Park,S.K., Park,H., Lee,E.J., Lee,D.,
            Roh,J.D., Mah,W., Kim,R., Kim,Y., Kwon,H., Bae,Y.C., Choi,S.Y.,
            Craig,A.M. and Kim,E.
  TITLE     Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions
            Regulate Excitatory Synapse Development and Locomotion
  JOURNAL   Cell Rep 12 (10), 1618-1630 (2015)
   PUBMED   26321637
  REMARK    GeneRIF: SALM3 regulates excitatory synapse development and
            locomotion behavior.
REFERENCE   6  (residues 1 to 635)
  CONSRTM   Psychiatric GWAS Consortium Bipolar Disorder Working Group
  TITLE     Large-scale genome-wide association analysis of bipolar disorder
            identifies a new susceptibility locus near ODZ4
  JOURNAL   Nat Genet 43 (10), 977-983 (2011)
   PUBMED   21926972
  REMARK    Erratum:[Nat Genet. 2012 Sep;44(9):1072. Fullerton, Janice M
            [added]; Hyoun, Phil L [corrected to Lee, Phil H]; Meng, Fan Guo
            [corrected to Meng, Fan]]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 635)
  AUTHORS   Konakahara,S., Saitou,M., Hori,S., Nakane,T., Murai,K., Itoh,R.,
            Shinsaka,A., Kohroki,J., Kawakami,T., Kajikawa,M. and Masuho,Y.
  TITLE     A neuronal transmembrane protein LRFN4 induces monocyte/macrophage
            migration via actin cytoskeleton reorganization
  JOURNAL   FEBS Lett 585 (14), 2377-2384 (2011)
   PUBMED   21704618
  REMARK    GeneRIF: Data indicate that LRFN4 signaling plays an important role
            in the migration of monocytes/macrophages.
REFERENCE   8  (residues 1 to 635)
  AUTHORS   Nam,J., Mah,W. and Kim,E.
  TITLE     The SALM/Lrfn family of leucine-rich repeat-containing cell
            adhesion molecules
  JOURNAL   Semin Cell Dev Biol 22 (5), 492-498 (2011)
   PUBMED   21736948
  REMARK    Review article
REFERENCE   9  (residues 1 to 635)
  AUTHORS   Morimura,N., Inoue,T., Katayama,K. and Aruga,J.
  TITLE     Comparative analysis of structure, expression and PSD95-binding
            capacity of Lrfn, a novel family of neuronal transmembrane proteins
  JOURNAL   Gene 380 (2), 72-83 (2006)
   PUBMED   16828986
REFERENCE   10 (residues 1 to 635)
  AUTHORS   Wang,C.Y., Chang,K., Petralia,R.S., Wang,Y.X., Seabold,G.K. and
            Wenthold,R.J.
  TITLE     A novel family of adhesion-like molecules that interacts with the
            NMDA receptor
  JOURNAL   J Neurosci 26 (8), 2174-2183 (2006)
   PUBMED   16495444
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003176.2.
            
            On May 24, 2018 this sequence version replaced XP_005274296.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138511.9964.1,
                                           SRR7346977.1211670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..635
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..635
                     /product="leucine-rich repeat and fibronectin type-III
                     domain-containing protein 4 precursor"
                     /note="fibronectin type III, immunoglobulin and leucine
                     rich repeat domains 6; leucine-rich repeat and fibronectin
                     type-III domain-containing protein 4"
                     /calculated_mol_wt=65357
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1522
     mat_peptide     17..635
                     /product="Leucine-rich repeat and fibronectin type-III
                     domain-containing protein 4. /id=PRO_0000014843"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
                     /calculated_mol_wt=65357
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          49..70
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          50..73
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <52..>215
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            70
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          73..94
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          74..97
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          97..118
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          98..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          121..142
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          122..146
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          146..161
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          147..170
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          170..191
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          171..194
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          194..215
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          195..213
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          234..278
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Region          281..368
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          298..302
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409421"
     Region          311..315
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409421"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          334..338
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409421"
     Region          348..353
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409421"
     Region          361..364
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409421"
     Region          373..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            376
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          409..478
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            440
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            519..539
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          555..583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJG9.1)"
     Region          632..635
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJG9.1)"
     CDS             1..635
                     /gene="LRFN4"
                     /gene_synonym="FIGLER6; SALM3; SALM3."
                     /coded_by="NM_001363524.2:244..2151"
                     /db_xref="CCDS:CCDS8153.1"
                     /db_xref="GeneID:78999"
                     /db_xref="HGNC:HGNC:28456"
                     /db_xref="MIM:612810"
ORIGIN      
        1 mappllllll asgaaacplp cvcqnlsesl stlcahrgll fvppnvdrrt velrladnfi
       61 qalgppdfrn mtglvdltls rnaitrigar afgdleslrs lhldgnrlve lgtgslrgpv
      121 nlqhlilsgn qlgriapgaf ddflesledl dlsynnlrqv pwagigampa lhtlnldhnl
      181 idalppgafa qlgqlsrldl tsnrlatlap dplfsrgrda easpaplvls fsgnplhcnc
      241 ellwlrrlar pddletcasp pglagryfwa vpegefscep pliarhtqrl wvlegqratl
      301 rcralgdpap tmhwvgpddr lvgnssrara fpngtleigv tgagdaggyt ciatnpagea
      361 tarvelrvla lphggnssae ggrpgpsdia asartaaege gtlesepavq vtevtatsgl
      421 vswgpgrpad pvwmfqiqyn ssedetliyr ivpasshhfl lkhlvpgady dlcllalspa
      481 agpsdltatr llgcahfstl pasplchalq ahvlggtltv avggvlvaal lvftvallvr
      541 grgagngrlp lklshvqsqt nggpsptpka hpprsppprp qrscsldlgd agcygyarrl
      601 ggawarrshs vhggllgagc rgvggsaerl eesvv
//
LOCUS       NP_848621                318 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial coenzyme A transporter SLC25A42 [Homo sapiens].
ACCESSION   NP_848621 XP_209204
VERSION     NP_848621.2
DBSOURCE    REFSEQ: accession NM_178526.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Liu,R., Zhang,Z., Kyaw,A.K., Grabinska,K.A., Shah,H. and Shen,H.
  TITLE     Cellular pan-chain acyl-CoA profiling reveals SLC25A42/SLC25A16 in
            mitochondrial CoA import and metabolism
  JOURNAL   Nat Metab 7 (9), 1871-1888 (2025)
   PUBMED   40925986
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Taga,K. and Takeuchi,H.
  TITLE     Novel role of host protein SLC25A42 in the HIV-1 reactivation of
            latent HIV-1 provirus
  JOURNAL   Microbiol Immunol 68 (3), 90-99 (2024)
   PUBMED   38244193
  REMARK    GeneRIF: Novel role of host protein SLC25A42 in the HIV-1
            reactivation of latent HIV-1 provirus.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Almannai,M., Alasmari,A., Alqasmi,A., Faqeih,E., Al Mutairi,F.,
            Alotaibi,M., Samman,M.M., Eyaid,W., Aljadhai,Y.I., Shamseldin,H.E.,
            Craigen,W. and Alkuraya,F.S.
  TITLE     Expanding the phenotype of SLC25A42-associated mitochondrial
            encephalomyopathy
  JOURNAL   Clin Genet 93 (5), 1097-1102 (2018)
   PUBMED   29327420
  REMARK    GeneRIF: our report confirms the link between SLC25A42 and
            mitochondrial disease in humans, and suggests that pathogenic
            variants in SLC25A42 should be interpreted with the understanding
            that the associated phenotype may be highly variable.
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Palmieri,F.
  TITLE     The mitochondrial transporter family SLC25: identification,
            properties and physiopathology
  JOURNAL   Mol Aspects Med 34 (2-3), 465-484 (2013)
   PUBMED   23266187
  REMARK    GeneRIF: Compares and contrasts all the known human SLC25A* genes
            and includes functional information.
            Review article
REFERENCE   7  (residues 1 to 318)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Fiermonte,G., Paradies,E., Todisco,S., Marobbio,C.M. and
            Palmieri,F.
  TITLE     A novel member of solute carrier family 25 (SLC25A42) is a
            transporter of coenzyme A and adenosine 3',5'-diphosphate in human
            mitochondria
  JOURNAL   J Biol Chem 284 (27), 18152-18159 (2009)
   PUBMED   19429682
  REMARK    GeneRIF: The main physiological role of SLC25A42 is to import CoA
            into mitochondria in exchange for intramitochondrial (deoxy)adenine
            nucleotides and adenosine 3',5'-diphosphate
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Haitina,T., Lindblom,J., Renstrom,T. and Fredriksson,R.
  TITLE     Fourteen novel human members of mitochondrial solute carrier family
            25 (SLC25) widely expressed in the central nervous system
  JOURNAL   Genomics 88 (6), 779-790 (2006)
   PUBMED   16949250
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC003038.1, FN356975.1,
            AF521885.1 and AI057363.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 15, 2009 this sequence version replaced NP_848621.1.
            
            Summary: This gene encodes a solute carrier family 25 protein.
            Solute carrier family 25 proteins are localized to mitochondria and
            play critical roles in the transport of molecules across the inner
            mitochondrial membrane. The encoded protein is a mitochondrial
            transporter for coenzyme A (CoA) and adenosine 3',5'-diphosphate.
            [provided by RefSeq, Feb 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FN356975.1, BC045598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000318596.8/
                                                  ENSP00000326693.6
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..318
                     /product="mitochondrial coenzyme A transporter SLC25A42"
                     /calculated_mol_wt=35278
     Region          31..117
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          34..295
                     /region_name="PTZ00169"
                     /note="ADP/ATP transporter on adenylate translocase;
                     Provisional"
                     /db_xref="CDD:240302"
     Site            89..109
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          129..214
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Region          224..312
                     /region_name="Solcar 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            230..250
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     Site            293..313
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VD7.2)"
     CDS             1..318
                     /gene="SLC25A42"
                     /gene_synonym="MECREN"
                     /coded_by="NM_178526.5:157..1113"
                     /db_xref="CCDS:CCDS32966.1"
                     /db_xref="GeneID:284439"
                     /db_xref="HGNC:HGNC:28380"
                     /db_xref="MIM:610823"
ORIGIN      
        1 mgngvkegpv rlhedaeavl sssvsskrdh rqvlssllsg alagalakta vapldrtkii
       61 fqvsskrfsa keafrvlyyt ylnegflslw rgnsatmvrv vpyaaiqfsa heeykrilgs
      121 yygfrgealp pwprlfagal agttaaslty pldlvrarma vtpkemysni fhvfirisre
      181 eglktlyhgf mptvlgvipy aglsfftyet lkslhreysg rrqpypferm ifgacaglig
      241 qsasypldvv rrrmqtagvt gyprasiart lrtivreega vrglykglsm nwvkgpiavg
      301 isfttfdlmq illrhlqs
//
LOCUS       NP_001310184             398 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 32 isoform h [Homo sapiens].
ACCESSION   NP_001310184
VERSION     NP_001310184.1
DBSOURCE    REFSEQ: accession NM_001323255.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Simino,J., Shi,G., Bis,J.C., Chasman,D.I., Ehret,G.B., Gu,X.,
            Guo,X., Hwang,S.J., Sijbrands,E., Smith,A.V., Verwoert,G.C.,
            Bragg-Gresham,J.L., Cadby,G., Chen,P., Cheng,C.Y., Corre,T., de
            Boer,R.A., Goel,A., Johnson,T., Khor,C.C., Lluis-Ganella,C.,
            Luan,J., Lyytikainen,L.P., Nolte,I.M., Sim,X., Sober,S., van der
            Most,P.J., Verweij,N., Zhao,J.H., Amin,N., Boerwinkle,E.,
            Bouchard,C., Dehghan,A., Eiriksdottir,G., Elosua,R., Franco,O.H.,
            Gieger,C., Harris,T.B., Hercberg,S., Hofman,A., James,A.L.,
            Johnson,A.D., Kahonen,M., Khaw,K.T., Kutalik,Z., Larson,M.G.,
            Launer,L.J., Li,G., Liu,J., Liu,K., Morrison,A.C., Navis,G.,
            Ong,R.T., Papanicolau,G.J., Penninx,B.W., Psaty,B.M., Raffel,L.J.,
            Raitakari,O.T., Rice,K., Rivadeneira,F., Rose,L.M., Sanna,S.,
            Scott,R.A., Siscovick,D.S., Stolk,R.P., Uitterlinden,A.G.,
            Vaidya,D., van der Klauw,M.M., Vasan,R.S., Vithana,E.N., Volker,U.,
            Volzke,H., Watkins,H., Young,T.L., Aung,T., Bochud,M., Farrall,M.,
            Hartman,C.A., Laan,M., Lakatta,E.G., Lehtimaki,T., Loos,R.J.,
            Lucas,G., Meneton,P., Palmer,L.J., Rettig,R., Snieder,H., Tai,E.S.,
            Teo,Y.Y., van der Harst,P., Wareham,N.J., Wijmenga,C., Wong,T.Y.,
            Fornage,M., Gudnason,V., Levy,D., Palmas,W., Ridker,P.M.,
            Rotter,J.I., van Duijn,C.M., Witteman,J.C., Chakravarti,A. and
            Rao,D.C.
  CONSRTM   LifeLines Cohort Study
  TITLE     Gene-age interactions in blood pressure regulation: a large-scale
            investigation with the CHARGE, Global BPgen, and ICBP Consortia
  JOURNAL   Am J Hum Genet 95 (1), 24-38 (2014)
   PUBMED   24954895
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Leone,M.A., Barizzone,N., Esposito,F., Lucenti,A., Harbo,H.F.,
            Goris,A., Kockum,I., Oturai,A.B., Celius,E.G., Mero,I.L.,
            Dubois,B., Olsson,T., Sondergaard,H.B., Cusi,D., Lupoli,S.,
            Andreassen,B.K., Myhr,K.M., Guerini,F.R., Comi,G.,
            Martinelli-Boneschi,F. and D'Alfonso,S.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2; PROGEMUS Group; PROGRESSO Group
  TITLE     Association of genetic markers with CSF oligoclonal bands in
            multiple sclerosis patients
  JOURNAL   PLoS One 8 (6), e64408 (2013)
   PUBMED   23785401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Monda,K.L., Chen,G.K., Taylor,K.C., Palmer,C., Edwards,T.L.,
            Lange,L.A., Ng,M.C., Adeyemo,A.A., Allison,M.A., Bielak,L.F.,
            Chen,G., Graff,M., Irvin,M.R., Rhie,S.K., Li,G., Liu,Y., Liu,Y.,
            Lu,Y., Nalls,M.A., Sun,Y.V., Wojczynski,M.K., Yanek,L.R.,
            Aldrich,M.C., Ademola,A., Amos,C.I., Bandera,E.V., Bock,C.H.,
            Britton,A., Broeckel,U., Cai,Q., Caporaso,N.E., Carlson,C.S.,
            Carpten,J., Casey,G., Chen,W.M., Chen,F., Chen,Y.D., Chiang,C.W.,
            Coetzee,G.A., Demerath,E., Deming-Halverson,S.L., Driver,R.W.,
            Dubbert,P., Feitosa,M.F., Feng,Y., Freedman,B.I., Gillanders,E.M.,
            Gottesman,O., Guo,X., Haritunians,T., Harris,T., Harris,C.C.,
            Hennis,A.J., Hernandez,D.G., McNeill,L.H., Howard,T.D.,
            Howard,B.V., Howard,V.J., Johnson,K.C., Kang,S.J., Keating,B.J.,
            Kolb,S., Kuller,L.H., Kutlar,A., Langefeld,C.D., Lettre,G.,
            Lohman,K., Lotay,V., Lyon,H., Manson,J.E., Maixner,W., Meng,Y.A.,
            Monroe,K.R., Morhason-Bello,I., Murphy,A.B., Mychaleckyj,J.C.,
            Nadukuru,R., Nathanson,K.L., Nayak,U., N'diaye,A., Nemesure,B.,
            Wu,S.Y., Leske,M.C., Neslund-Dudas,C., Neuhouser,M., Nyante,S.,
            Ochs-Balcom,H., Ogunniyi,A., Ogundiran,T.O., Ojengbede,O.,
            Olopade,O.I., Palmer,J.R., Ruiz-Narvaez,E.A., Palmer,N.D.,
            Press,M.F., Rampersaud,E., Rasmussen-Torvik,L.J.,
            Rodriguez-Gil,J.L., Salako,B., Schadt,E.E., Schwartz,A.G.,
            Shriner,D.A., Siscovick,D., Smith,S.B., Wassertheil-Smoller,S.,
            Speliotes,E.K., Spitz,M.R., Sucheston,L., Taylor,H., Tayo,B.O.,
            Tucker,M.A., Van Den Berg,D.J., Edwards,D.R., Wang,Z.,
            Wiencke,J.K., Winkler,T.W., Witte,J.S., Wrensch,M., Wu,X.,
            Yang,J.J., Levin,A.M., Young,T.R., Zakai,N.A., Cushman,M.,
            Zanetti,K.A., Zhao,J.H., Zhao,W., Zheng,Y., Zhou,J., Ziegler,R.G.,
            Zmuda,J.M., Fernandes,J.K., Gilkeson,G.S., Kamen,D.L., Hunt,K.J.,
            Spruill,I.J., Ambrosone,C.B., Ambs,S., Arnett,D.K., Atwood,L.,
            Becker,D.M., Berndt,S.I., Bernstein,L., Blot,W.J., Borecki,I.B.,
            Bottinger,E.P., Bowden,D.W., Burke,G., Chanock,S.J., Cooper,R.S.,
            Ding,J., Duggan,D., Evans,M.K., Fox,C., Garvey,W.T.,
            Bradfield,J.P., Hakonarson,H., Grant,S.F., Hsing,A., Chu,L.,
            Hu,J.J., Huo,D., Ingles,S.A., John,E.M., Jordan,J.M.,
            Kabagambe,E.K., Kardia,S.L., Kittles,R.A., Goodman,P.J.,
            Klein,E.A., Kolonel,L.N., Le Marchand,L., Liu,S., McKnight,B.,
            Millikan,R.C., Mosley,T.H., Padhukasahasram,B., Williams,L.K.,
            Patel,S.R., Peters,U., Pettaway,C.A., Peyser,P.A., Psaty,B.M.,
            Redline,S., Rotimi,C.N., Rybicki,B.A., Sale,M.M., Schreiner,P.J.,
            Signorello,L.B., Singleton,A.B., Stanford,J.L., Strom,S.S.,
            Thun,M.J., Vitolins,M., Zheng,W., Moore,J.H., Williams,S.M.,
            Ketkar,S., Zhu,X., Zonderman,A.B., Kooperberg,C.,
            Papanicolaou,G.J., Henderson,B.E., Reiner,A.P., Hirschhorn,J.N.,
            Loos,R.J., North,K.E. and Haiman,C.A.
  CONSRTM   NABEC Consortium; UKBEC Consortium; BioBank Japan Project; AGEN
            Consortium
  TITLE     A meta-analysis identifies new loci associated with body mass index
            in individuals of African ancestry
  JOURNAL   Nat Genet 45 (6), 690-696 (2013)
   PUBMED   23583978
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA296671.1, AK055292.1, HY131926.1, BC071627.1 and HY334128.1.
            
            Transcript Variant: This variant (10) lacks an alternate in-frame
            exon and several 3' exons, but it contains an alternate 3' terminal
            exon and it thus differs in the 3' coding region and 3' UTR,
            compared to variant 1. The encoded isoform (h) has a distinct
            C-terminus and is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.27145.1,
                                           SRR1660803.222339.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q16.1"
     Protein         1..398
                     /product="kelch-like protein 32 isoform h"
                     /note="BTB and kelch domain containing 5; kelch-like
                     protein 32"
                     /calculated_mol_wt=44815
     Region          14..146
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          <137..164
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     Region          219..274
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          252..>383
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          264..313
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          316..359
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..398
                     /gene="KLHL32"
                     /gene_synonym="BKLHD5; dJ21F7.1; KIAA1900; UG0030H05"
                     /coded_by="NM_001323255.2:365..1561"
                     /note="isoform h is encoded by transcript variant 10"
                     /db_xref="GeneID:114792"
                     /db_xref="HGNC:HGNC:21221"
ORIGIN      
        1 mpserclsiq emltgqrlch seshndsvla alnqqrsdgi lcditliaee qkfhahkavl
       61 aacsdyfram fslcmvesga devnlhgvts lglkqalefa ytgqillepg viqdvlaags
      121 hlqllellnl cshyliqlav rwlehnchyq ymdellqyir fglmdvdtlh tvalshplvq
      181 asetatalvn ealeyhqsiy aqpvwqtrrt kprfqsdtly iiggkkrevc kvkelryfnp
      241 vdqenaliaa ianwselapm pvgrshhcva vmgdflfvag gevehasgrt cavrtacryd
      301 prsnswaeia pmkncrehfv lgameeylya vggrnelrqv lptverycpk knkwtfvqsf
      361 drslschagy vadgllwisg rtylmldlsk htfivvyi
//
LOCUS       NP_003306                494 aa            linear   PRI 20-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 7 isoform 1 [Homo sapiens].
ACCESSION   NP_003306
VERSION     NP_003306.3
DBSOURCE    REFSEQ: accession NM_003315.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Wang,S., Zheng,X., Wei,Q., Lin,J., Yang,T., Xiao,Y., Jiang,Q.,
            Li,C. and Shang,H.
  TITLE     Rare DNAJC7 Variants May Play a Minor Role in Chinese Patients with
            ALS
  JOURNAL   Mol Neurobiol 61 (4), 2265-2269 (2024)
   PUBMED   37870677
  REMARK    GeneRIF: Rare DNAJC7 Variants May Play a Minor Role in Chinese
            Patients with ALS.
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Dilliott,A.A., Andary,C.M., Stoltz,M., Petropavlovskiy,A.A.,
            Farhan,S.M.K. and Duennwald,M.L.
  TITLE     DnaJC7 in Amyotrophic Lateral Sclerosis
  JOURNAL   Int J Mol Sci 23 (8), 4076 (2022)
   PUBMED   35456894
  REMARK    GeneRIF: DnaJC7 in Amyotrophic Lateral Sclerosis.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Moffatt,N.S., Bruinsma,E., Uhl,C., Obermann,W.M. and Toft,D.
  TITLE     Role of the cochaperone Tpr2 in Hsp90 chaperoning
  JOURNAL   Biochemistry 47 (31), 8203-8213 (2008)
   PUBMED   18620420
  REMARK    GeneRIF: Data show that Tpr2 associates with Hsp90 and Hsp70
            complexes, promoted the accumulation of Hsp70 in PR heterocomplexes
            in the presence of Hsp90. Thus, Tpr2 has the potential to regulate
            PR chaperoning.
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Brychzy,A., Rein,T., Winklhofer,K.F., Hartl,F.U., Young,J.C. and
            Obermann,W.M.
  TITLE     Cofactor Tpr2 combines two TPR domains and a J domain to regulate
            the Hsp70/Hsp90 chaperone system
  JOURNAL   EMBO J 22 (14), 3613-3623 (2003)
   PUBMED   12853476
  REMARK    GeneRIF: TPR2 combines two TPR domains and a J domain to regulate
            the Hsp70/Hsp90 chaperone system.
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Ohtsuka,K. and Hata,M.
  TITLE     Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a
            proposal for their classification and nomenclature
  JOURNAL   Cell Stress Chaperones 5 (2), 98-112 (2000)
   PUBMED   11147971
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Murthy,A.E., Bernards,A., Church,D., Wasmuth,J. and Gusella,J.F.
  TITLE     Identification and characterization of two novel tetratricopeptide
            repeat-containing genes
  JOURNAL   DNA Cell Biol 15 (9), 727-735 (1996)
   PUBMED   8836031
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647209.1, BC011837.2 and
            BQ445927.1.
            
            On Oct 29, 2009 this sequence version replaced NP_003306.2.
            
            Summary: This gene encodes a member of the DNAJ heat shock protein
            40 family of proteins that is characterized by two N-terminal
            tetratricopeptide repeat domains and a C-terminal DNAJ domain. This
            protein binds the chaperone proteins heat shock proteins 70 and 90
            in an ATP-dependent manner and may function as a co-chaperone.
            Pseudogenes of this gene are found on chromosomes 1 and 6.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.888846.1, BX647209.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000457167.9/ ENSP00000406463.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..494
                     /product="dnaJ homolog subfamily C member 7 isoform 1"
                     /note="tetratricopeptide repeat domain 2; dnaJ homolog
                     subfamily C member 7; TPR repeat protein 2;
                     tetratricopeptide repeat protein 2; DnaJ (Hsp40) homolog,
                     subfamily C, member 7"
                     /calculated_mol_wt=56310
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99615.2)"
     Region          27..>195
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          28..61
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          28..56
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(29,32..33,36..37,39,63,66..67,70..71,73..74,97,
                     100..101,104..105,108)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          61..91
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          62..95
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          96..129
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          96..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..175
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          145..170
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(146..147,150..151,153,177,180..181,184..185,
                     187..188,211,214..215,218..219,222)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          169..398
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          175..205
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          177..209
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          210..243
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          210..238
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          256..289
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Site            order(257,260..261,264..265,267,295,298..299,302..303,
                     305..306,329,332..333,336..337,340)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          257..284
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          289..323
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          294..327
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          328..361
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99615.2)"
     Region          328..356
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          377..>448
                     /region_name="PRK10767"
                     /note="chaperone protein DnaJ; Provisional"
                     /db_xref="CDD:236757"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99615.2)"
     CDS             1..494
                     /gene="DNAJC7"
                     /gene_synonym="DJ11; DJC7; TPR2; TTC2"
                     /coded_by="NM_003315.4:24..1508"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45677.1"
                     /db_xref="GeneID:7266"
                     /db_xref="HGNC:HGNC:12392"
                     /db_xref="MIM:601964"
ORIGIN      
        1 maaaaecdvv maatepelld dqeakreaet fkeqgnayya kkdyneayny ytkaidmcpk
       61 nasyygnraa tlmmlgrfre algdaqqsvr lddsfvrghl regkchlslg namaacrsfq
      121 raleldhkna qaqqefknan avmeyekiae tdfekrdfrk vvfcmdrale fapachrfki
      181 lkaeclamlg rypeaqsvas dilrmdstna dalyvrglcl yyedciekav qffvqalrma
      241 pdhekaciac rnakalkakk edgnkafkeg nyklayelyt ealgidpnni ktnaklycnr
      301 gtvnsklrkl ddaiedctna vklddtyika ylrraqcymd teqyeeavrd yekvyqtekt
      361 kehkqllkna qlelkkskrk dyykilgvdk nasedeikka yrkralmhhp drhsgasaev
      421 qkeeekkfke vgeaftilsd pkkktrydsg qdldeegmnm gdfdpnnifk affggpggfs
      481 feasgpgnff fqfg
//
LOCUS       NP_056345                452 aa            linear   PRI 20-NOV-2025
DEFINITION  Golgi reassembly-stacking protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_056345
VERSION     NP_056345.3
DBSOURCE    REFSEQ: accession NM_015530.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Yang,F., Chen,L., Wen,B., Wang,X., Wang,L., Ji,K. and Liu,H.
  TITLE     Golgi Reassembly Stacking Protein 2 Modulates Myometrial
            Contractility during Labor by Affecting ATP Production
  JOURNAL   Int J Mol Sci 24 (12), 10116 (2023)
   PUBMED   37373263
  REMARK    GeneRIF: Golgi Reassembly Stacking Protein 2 Modulates Myometrial
            Contractility during Labor by Affecting ATP Production.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Ahat,E., Song,Y., Xia,K., Reid,W., Li,J., Bui,S., Zhang,F.,
            Linhardt,R.J. and Wang,Y.
  TITLE     GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion
  JOURNAL   Cell Mol Life Sci 79 (4), 199 (2022)
   PUBMED   35312866
  REMARK    GeneRIF: GRASP depletion-mediated Golgi fragmentation impairs
            glycosaminoglycan synthesis, sulfation, and secretion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Duran,J.M., Kinseth,M., Bossard,C., Rose,D.W., Polishchuk,R.,
            Wu,C.C., Yates,J., Zimmerman,T. and Malhotra,V.
  TITLE     The role of GRASP55 in Golgi fragmentation and entry of cells into
            mitosis
  JOURNAL   Mol Biol Cell 19 (6), 2579-2587 (2008)
   PUBMED   18385516
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Lane,J.D., Lucocq,J., Pryde,J., Barr,F.A., Woodman,P.G., Allan,V.J.
            and Lowe,M.
  TITLE     Caspase-mediated cleavage of the stacking protein GRASP65 is
            required for Golgi fragmentation during apoptosis
  JOURNAL   J Cell Biol 156 (3), 495-509 (2002)
   PUBMED   11815631
  REMARK    GeneRIF: GRASP65 is an important structural component required for
            maintenance of Golgi apparatus integrity
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Short,B., Preisinger,C., Korner,R., Kopajtich,R., Byron,O. and
            Barr,F.A.
  TITLE     A GRASP55-rab2 effector complex linking Golgi structure to membrane
            traffic
  JOURNAL   J Cell Biol 155 (6), 877-883 (2001)
   PUBMED   11739401
  REMARK    GeneRIF: GRASP55 forms an effector complex for the small GTPase
            rab2, together with a conserved coiled-coil protein golgin-45
            (JEM-1).
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Jesch,S.A., Lewis,T.S., Ahn,N.G. and Linstedt,A.D.
  TITLE     Mitotic phosphorylation of Golgi reassembly stacking protein 55 by
            mitogen-activated protein kinase ERK2
  JOURNAL   Mol Biol Cell 12 (6), 1811-1817 (2001)
   PUBMED   11408587
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Kuo,A., Zhong,C., Lane,W.S. and Derynck,R.
  TITLE     Transmembrane transforming growth factor-alpha tethers to the PDZ
            domain-containing, Golgi membrane-associated protein p59/GRASP55
  JOURNAL   EMBO J 19 (23), 6427-6439 (2000)
   PUBMED   11101516
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010092.4, BC007770.2 and
            BQ004408.1.
            
            On Apr 14, 2003 this sequence version replaced NP_056345.2.
            
            Summary: This gene encodes a member of the Golgi reassembly
            stacking protein family. These proteins may play a role in the
            stacking of Golgi cisternae and Golgi ribbon formation, as well as
            Golgi fragmentation during apoptosis or mitosis. The encoded
            protein also plays a role in the intracellular transport of
            transforming growth factor alpha and may function as a molecular
            chaperone. A pseudogene of this gene is located on the short arm of
            chromosome 2. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1172575.1, AK023201.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234160.5/ ENSP00000234160.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..452
                     /product="Golgi reassembly-stacking protein 2 isoform 1"
                     /note="golgi phosphoprotein 6; golgi reassembly stacking
                     protein 2, 55kDa; Golgi reassembly-stacking protein 2"
                     /calculated_mol_wt=47014
     Region          <14..100
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          15..215
                     /region_name="GRASP.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01214"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            30
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q9R064; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            47
                     /site_type="methylation"
                     /note="Dimethylated arginine.
                     /evidence=ECO:0000250|UniProtKB:Q9R064; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Region          69..204
                     /region_name="GRASP55_65"
                     /note="GRASP55/65 PDZ-like domain; pfam04495"
                     /db_xref="CDD:427981"
     Region          194..199
                     /region_name="Important for membrane binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:11408587,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Region          <241..397
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          372..452
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JX3; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:21884936,
                     ECO:0000269|PubMed:27062250; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27062250,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27062250,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H8Y8.3)"
     CDS             1..452
                     /gene="GORASP2"
                     /gene_synonym="GOLPH6; GRASP55; GRS2; p59"
                     /coded_by="NM_015530.5:89..1447"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33325.1"
                     /db_xref="GeneID:26003"
                     /db_xref="HGNC:HGNC:17500"
                     /db_xref="MIM:608693"
ORIGIN      
        1 mgssqsveip gggtegyhvl rvqenspghr aglepffdfi vsingsrlnk dndtlkdllk
       61 anvekpvkml iyssktlelr etsvtpsnlw ggqgllgvsi rfcsfdgane nvwhvleves
      121 nspaalaglr phsdyiigad tvmnesedlf slietheakp lklyvyntdt dncreviitp
      181 nsawggegsl gcgigygylh riptrpfeeg kkislpgqma gtpitplkdg ftevqlssvn
      241 ppslsppgtt gieqsltgls isstppavss vlstgvptvp llppqvnqsl tsvppmnpat
      301 tlpglmplpa glpnlpnlnl nlpaphimpg vglpelvnpg lpplpsmppr nlpgiaplpl
      361 pseflpsfpl vpesssaass gellsslppt snapsdpatt takadaassl tvdvtpptak
      421 apttvedrvg dstpvsekpv saavdanase sp
//
LOCUS       NP_859064                259 aa            linear   PRI 20-NOV-2025
DEFINITION  UBX domain-containing protein 2A [Homo sapiens].
ACCESSION   NP_859064
VERSION     NP_859064.2
DBSOURCE    REFSEQ: accession NM_181713.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Sane,S., Srinivasan,R., Potts,R.A., Eikanger,M., Zagirova,D.,
            Freeling,J., Reihe,C.A., Antony,R.M., Gupta,B.K., Lynch,D.,
            Bleeker,J., Turaihi,H., Pillatzki,A., Zhou,W., Luo,X.,
            Linnebacher,M., Agany,D., Zohim,E.G., Humphrey,L.E., Black,A.R. and
            Rezvani,K.
  TITLE     UBXN2A suppresses the Rictor-mTORC2 signaling pathway, an
            established tumorigenic pathway in human colorectal cancer
  JOURNAL   Oncogene 42 (21), 1763-1776 (2023)
   PUBMED   37037900
  REMARK    GeneRIF: UBXN2A suppresses the Rictor-mTORC2 signaling pathway, an
            established tumorigenic pathway in human colorectal cancer.
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Reihe,C.
  TITLE     UBXN2A, a Ubiquitin-Like Protein, Alters Proteins in mTORC2 Pathway
  JOURNAL   S D Med 75 (10), 456-458 (2022)
   PUBMED   36889268
  REMARK    GeneRIF: UBXN2A, a Ubiquitin-Like Protein, Alters Proteins in
            mTORC2 Pathway.
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Wang,C.W. and Lee,S.C.
  TITLE     The ubiquitin-like (UBX)-domain-containing protein Ubx2/Ubxd8
            regulates lipid droplet homeostasis
  JOURNAL   J Cell Sci 125 (Pt 12), 2930-2939 (2012)
   PUBMED   22454508
  REMARK    GeneRIF: Ubx2 and Ubxd8 regulates lipid droplet homeostasis.
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Bhatnagar,P., Purvis,S., Barron-Casella,E., DeBaun,M.R.,
            Casella,J.F., Arking,D.E. and Keefer,J.R.
  TITLE     Genome-wide association study identifies genetic variants
            influencing F-cell levels in sickle-cell patients
  JOURNAL   J Hum Genet 56 (4), 316-323 (2011)
   PUBMED   21326311
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Lowe,J.K., Maller,J.B., Pe'er,I., Neale,B.M., Salit,J., Kenny,E.E.,
            Shea,J.L., Burkhardt,R., Smith,J.G., Ji,W., Noel,M., Foo,J.N.,
            Blundell,M.L., Skilling,V., Garcia,L., Sullivan,M.L., Lee,H.E.,
            Labek,A., Ferdowsian,H., Auerbach,S.B., Lifton,R.P.,
            Newton-Cheh,C., Breslow,J.L., Stoffel,M., Daly,M.J., Altshuler,D.M.
            and Friedman,J.M.
  TITLE     Genome-wide association studies in an isolated founder population
            from the Pacific Island of Kosrae
  JOURNAL   PLoS Genet 5 (2), e1000365 (2009)
   PUBMED   19197348
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC066692.3, AL832079.1 and BC016364.1.
            
            On Aug 6, 2003 this sequence version replaced NP_859064.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.59218.1,
                                           SRR1803617.137813.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309033.5/ ENSP00000312107.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..259
                     /product="UBX domain-containing protein 2A"
                     /note="UBX domain containing 4; UBX domain-containing
                     protein 4"
                     /calculated_mol_wt=29147
     Region          1..164
                     /region_name="Required for inhibition of CHRNA3
                     ubiquitination and translocation of CHRNA3 to the plasma
                     membrane resulting in an increase in acetylcholine-gated
                     nicotinic acetylcholine receptor currents.
                     /evidence=ECO:0000250|UniProtKB:Q99KJ0"
                     /note="propagated from UniProtKB/Swiss-Prot (P68543.1)"
     Region          1..151
                     /region_name="Required for interaction with CHRNA3.
                     /evidence=ECO:0000269|PubMed:26265139"
                     /note="propagated from UniProtKB/Swiss-Prot (P68543.1)"
     Region          65..138
                     /region_name="SEP"
                     /note="SEP domain; pfam08059"
                     /db_xref="CDD:462348"
     Region          167..259
                     /region_name="Required for interaction with VCP.
                     /evidence=ECO:0000269|PubMed:26265139"
                     /note="propagated from UniProtKB/Swiss-Prot (P68543.1)"
     Region          167..250
                     /region_name="UBX_UBXN2A"
                     /note="Ubiquitin regulatory domain X (UBX) found in UBX
                     domain protein 2A (UBXN2A) and similar proteins; cd17160"
                     /db_xref="CDD:340680"
     Site            order(175,177,179..180,183..184,186,220..221,223,239..242,
                     244,246)
                     /site_type="other"
                     /note="putative UBX-p97 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:340680"
     CDS             1..259
                     /gene="UBXN2A"
                     /gene_synonym="UBXD4"
                     /coded_by="NM_181713.4:201..980"
                     /db_xref="CCDS:CCDS1704.1"
                     /db_xref="GeneID:165324"
                     /db_xref="HGNC:HGNC:27265"
ORIGIN      
        1 mkdvdnlksi keewvcetgs dnqplgnnqq snceyfvdsl feeaqkvssk cvspaeqkkq
       61 vdvniklwkn gftvnddfrs ysdgasqqfl nsikkgelps elqgifdkee vdvkvedkkn
      121 eiclstkpvf qpfsgqghrl gsatpkivsk aknievenkn nlsavplnnl epitniqiwl
      181 angkrivqkf nithrvshik dfiekyqgsq rsppfslata lpvlrlldet ltleeadlqn
      241 aviiqrlqkt asfrelseh
//
LOCUS       NP_803171                626 aa            linear   PRI 20-NOV-2025
DEFINITION  protein argonaute-3 isoform b [Homo sapiens].
ACCESSION   NP_803171
VERSION     NP_803171.1
DBSOURCE    REFSEQ: accession NM_177422.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Pan,L., Xu,C., Mei,J., Chen,Y. and Wang,D.
  TITLE     Argonaute 3 (AGO3) promotes malignancy potential of cervical cancer
            via regulation of Wnt/beta-catenin signaling pathway
  JOURNAL   Reprod Biol 21 (1), 100479 (2021)
   PUBMED   33444963
  REMARK    GeneRIF: Argonaute 3 (AGO3) promotes malignancy potential of
            cervical cancer via regulation of Wnt/beta-catenin signaling
            pathway.
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Park,M.S., Sim,G., Kehling,A.C. and Nakanishi,K.
  TITLE     Human Argonaute2 and Argonaute3 are catalytically activated by
            different lengths of guide RNA
  JOURNAL   Proc Natl Acad Sci U S A 117 (46), 28576-28578 (2020)
   PUBMED   33122430
  REMARK    GeneRIF: Human Argonaute2 and Argonaute3 are catalytically
            activated by different lengths of guide RNA.
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Park,M.S., Phan,H.D., Busch,F., Hinckley,S.H., Brackbill,J.A.,
            Wysocki,V.H. and Nakanishi,K.
  TITLE     Human Argonaute3 has slicer activity
  JOURNAL   Nucleic Acids Res 45 (20), 11867-11877 (2017)
   PUBMED   29040713
  REMARK    GeneRIF: Data show that recombinant AGO3 loaded with miR-20a
            cleaves complementary target RNAs.
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Elkayam,E., Faehnle,C.R., Morales,M., Sun,J., Li,H. and
            Joshua-Tor,L.
  TITLE     Multivalent Recruitment of Human Argonaute by GW182
  JOURNAL   Mol Cell 67 (4), 646-658 (2017)
   PUBMED   28781232
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Bridge,K.S., Shah,K.M., Li,Y., Foxler,D.E., Wong,S.C.K.,
            Miller,D.C., Davidson,K.M., Foster,J.G., Rose,R., Hodgkinson,M.R.,
            Ribeiro,P.S., Aboobaker,A.A., Yashiro,K., Wang,X., Graves,P.R.,
            Plevin,M.J., Lagos,D. and Sharp,T.V.
  TITLE     Argonaute Utilization for miRNA Silencing Is Determined by
            Phosphorylation-Dependent Recruitment of LIM-Domain-Containing
            Proteins
  JOURNAL   Cell Rep 20 (1), 173-187 (2017)
   PUBMED   28683311
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Wu,L., Fan,J. and Belasco,J.G.
  TITLE     Importance of translation and nonnucleolytic ago proteins for
            on-target RNA interference
  JOURNAL   Curr Biol 18 (17), 1327-1332 (2008)
   PUBMED   18771919
  REMARK    GeneRIF: The specificity of RNA interference depends on the
            concentration of Ago1, Ago3, and Ago4 relative to Ago2.
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Meister,G., Landthaler,M., Patkaniowska,A., Dorsett,Y., Teng,G. and
            Tuschl,T.
  TITLE     Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
            siRNAs
  JOURNAL   Mol Cell 15 (2), 185-197 (2004)
   PUBMED   15260970
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Sasaki,T., Shiohama,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of eight members of the Argonaute family in the
            human genome
  JOURNAL   Genomics 82 (3), 323-330 (2003)
   PUBMED   12906857
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Doi,N., Zenno,S., Ueda,R., Ohki-Hamazaki,H., Ui-Tei,K. and Saigo,K.
  TITLE     Short-interfering-RNA-mediated gene silencing in mammalian cells
            requires Dicer and eIF2C translation initiation factors
  JOURNAL   Curr Biol 13 (1), 41-46 (2003)
   PUBMED   12526743
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF979526.1, BC025769.1,
            BX104163.1, AA251146.1 and AL138787.11.
            
            Summary: This gene encodes a member of the Argonaute family of
            proteins which play a role in RNA interference. The encoded protein
            is highly basic, contains a PAZ domain and a PIWI domain, and may
            play a role in short-interfering-RNA-mediated gene silencing. This
            gene is located on chromosome 1 in a tandem cluster of closely
            related family members including argonaute 4 and eukaryotic
            translation initiation factor 2C, 1. Two transcript variants
            encoding distinct isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) has multiple differences in
            the coding region, which causes translation initiation at a
            downstream start codon, compared to variant 1. The resulting
            protein (isoform b) has a shorter N-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025769.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..626
                     /product="protein argonaute-3 isoform b"
                     /EC_number="3.1.26.n2"
                     /note="hAgo3; argonaute 3, RISC catalytic component;
                     eukaryotic translation initiation factor 2C, 3"
                     /calculated_mol_wt=71080
     Region          1..114
                     /region_name="PAZ_argonaute_like"
                     /note="PAZ domain, argonaute_like subfamily. Argonaute is
                     part of the RNA-induced silencing complex (RISC), and is
                     an endonuclease that plays a key role in the RNA
                     interference pathway. The PAZ domain has been named after
                     the proteins Piwi,Argonaut, and Zwille; cd02846"
                     /db_xref="CDD:239212"
     Site            order(46,61,75,79,97,104,106)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239212"
     Region          159..584
                     /region_name="Piwi_ago-like"
                     /note="PIWI domain, Argonaute-like subfamily. Argonaute is
                     the central component of the RNA-induced silencing complex
                     (RISC) and related complexes. The PIWI domain is the
                     C-terminal portion of Argonaute and consists of two
                     subdomains, one of which provides the...; cd04657"
                     /db_xref="CDD:240015"
     Site            order(296,300,312..315,318,326,329,333,337)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240015"
     Site            order(364,366,436,574)
                     /site_type="active"
                     /db_xref="CDD:240015"
     CDS             1..626
                     /gene="AGO3"
                     /gene_synonym="EIF2C3"
                     /coded_by="NM_177422.3:767..2647"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS400.1"
                     /db_xref="GeneID:192669"
                     /db_xref="HGNC:HGNC:18421"
                     /db_xref="MIM:607355"
ORIGIN      
        1 mcevldihni deqprpltds hrvkftkeik glkvevthcg tmrrkyrvcn vtrrpashqt
       61 fplqlengqt vertvaqyfr ekytlqlkyp hlpclqvgqe qkhtylplev cnivagqrci
      121 kkltdnqtst mikatarsap drqeeisrlv rsanyetdpf vqefqfkvrd emahvtgrvl
      181 papmlqyggr nrtvatpshg vwdmrgkqfh tgveikmwai acfatqrqcr eeilkgftdq
      241 lrkiskdagm piqgqpcfck yaqgadsvep mfrhlkntys glqliivilp gktpvyaevk
      301 rvgdtllgma tqcvqvknvi ktspqtlsnl clkinvklgg innilvphqr psvfqqpvif
      361 lgadvthppa gdgkkpsiaa vvgsmdahps rycatvrvqr prqeiiqdla smvrelliqf
      421 ykstrfkptr iifyrdgvse gqfrqvlyye llaireacis lekdyqpgit yivvqkrhht
      481 rlfcadrter vgrsgnipag ttvdtdithp yefdfylcsh agiqgtsrps hyhvlwddnc
      541 ftadelqllt yqlchtyvrc trsvsipapa yyahlvafra ryhlvdkehd saegshvsgq
      601 sngrdpqala kavqihqdtl rtmyfa
//
LOCUS       NP_001093207             315 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat domain-containing protein 83 [Homo sapiens].
ACCESSION   NP_001093207
VERSION     NP_001093207.1
DBSOURCE    REFSEQ: accession NM_001099737.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kournoutis,A., Lamark,T., Johansen,T. and Abudu,Y.P.
  TITLE     WDR83/MORG1 inhibits RRAG GTPase-MTORC1 signaling to facilitate
            basal autophagy
  JOURNAL   Autophagy 20 (7), 1687-1688 (2024)
   PUBMED   38450633
  REMARK    GeneRIF: WDR83/MORG1 inhibits RRAG GTPase-MTORC1 signaling to
            facilitate basal autophagy.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bondeva,T. and Wolf,G.
  TITLE     Cloning of the Human MORG1 Promoter: Differential Regulation by
            Hypoxia and Prolyl-Hydroxylase Inhibitors
  JOURNAL   Genes (Basel) 13 (3), 427 (2022)
   PUBMED   35327980
  REMARK    GeneRIF: Cloning of the Human MORG1 Promoter: Differential
            Regulation by Hypoxia and Prolyl-Hydroxylase Inhibitors.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Hopfer,U., Hopfer,H., Jablonski,K., Stahl,R.A. and Wolf,G.
  TITLE     The novel WD-repeat protein Morg1 acts as a molecular scaffold for
            hypoxia-inducible factor prolyl hydroxylase 3 (PHD3)
  JOURNAL   J Biol Chem 281 (13), 8645-8655 (2006)
   PUBMED   16407229
  REMARK    GeneRIF: Functional characterization of the homologous rat gene.
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Vomastek,T., Schaeffer,H.J., Tarcsafalvi,A., Smolkin,M.E.,
            Bissonette,E.A. and Weber,M.J.
  TITLE     Modular construction of a signaling scaffold: MORG1 interacts with
            components of the ERK cascade and links ERK signaling to specific
            agonists
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 6981-6986 (2004)
   PUBMED   15118098
  REMARK    GeneRIF: Component of a modular scaffold system that participates
            in the regulation of agonist-specific ERK signaling.
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
  REMARK    GeneRIF: Includes the identification of this protein in C complex
            spliceosomes.
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z46189.1, AK314164.1 and
            BC005870.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the WD-40 protein family.
            The protein is proposed to function as a molecular scaffold for
            various multimeric protein complexes. The protein associates with
            several components of the extracellular signal-regulated kinase
            (ERK) pathway, and promotes ERK activity in response to serum or
            other signals. The protein also interacts with egl nine homolog 3
            (EGLN3, also known as PHD3) and regulates expression of
            hypoxia-inducible factor 1, and has been purified as part of the
            spliceosome. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.680912.1,
                                           SRR3476690.661101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000418543.8/ ENSP00000402653.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..315
                     /product="WD repeat domain-containing protein 83"
                     /note="mitogen-activated protein kinase organizer 1; MAPK
                     organizer 1"
                     /calculated_mol_wt=34212
     Region          18..295
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          23..62
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Site            order(24,42,46,52..53,65..66,84,88,94..95,107..108,125,
                     130,136..137,152,167,172,178..179,191,208,212,218..219,
                     231..232,251,256,262..263,275..276,294)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          30..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          65..104
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          71..107
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..146
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          112..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          151..188
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          157..187
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          190..228
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          194..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          231..272
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          238..272
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          275..313
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          279..303
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..315
                     /gene="WDR83"
                     /gene_synonym="MORG1"
                     /coded_by="NM_001099737.3:343..1290"
                     /db_xref="CCDS:CCDS12275.1"
                     /db_xref="GeneID:84292"
                     /db_xref="HGNC:HGNC:32672"
                     /db_xref="MIM:616850"
ORIGIN      
        1 mafpepkprp pelpqkrlkt ldcgqgavra vrfnvdgnyc ltcgsdktlk lwnplrgtll
       61 rtysghgyev ldaagsfdns slcsgggdka vvlwdvasgq vvrkfrghag kvntvqfnee
      121 atvilsgsid ssircwdcrs rrpepvqtld eardgvssvk vsdheilags vdgrvrrydl
      181 rmgqlfsdyv gspitctcfs rdgqctlvss ldstlrlldk dtgellgeyk ghknqeykld
      241 cclserdthv vscsedgkvf fwdlvegala lalpvgsgvv qslayhptep clltamggsv
      301 qcwreeayea edgag
//
LOCUS       NP_001306095             398 aa            linear   PRI 20-NOV-2025
DEFINITION  2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 isoform d
            [Homo sapiens].
ACCESSION   NP_001306095
VERSION     NP_001306095.1
DBSOURCE    REFSEQ: accession NM_001319166.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Utkur,K., Mayer,K., Khan,M., Manivannan,T., Schaffrath,R. and
            Brinkmann,U.
  TITLE     DPH1 and DPH2 variants that confer susceptibility to diphthamide
            deficiency syndrome in human cells and yeast models
  JOURNAL   Dis Model Mech 16 (9) (2023)
   PUBMED   37675463
  REMARK    GeneRIF: DPH1 and DPH2 variants that confer susceptibility to
            diphthamide deficiency syndrome in human cells and yeast models.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Feng,J., Shaik,S. and Wang,B.
  TITLE     Spin-Regulated Electron Transfer and Exchange-Enhanced Reactivity
            in Fe4 S4 -Mediated Redox Reaction of the Dph2 Enzyme During the
            Biosynthesis of Diphthamide
  JOURNAL   Angew Chem Int Ed Engl 60 (37), 20430-20436 (2021)
   PUBMED   34302311
  REMARK    GeneRIF: Spin-Regulated Electron Transfer and Exchange-Enhanced
            Reactivity in Fe4 S4 -Mediated Redox Reaction of the Dph2 Enzyme
            During the Biosynthesis of Diphthamide.
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Hawer,H., Mendelsohn,B.A., Mayer,K., Kung,A., Malhotra,A.,
            Tuupanen,S., Schleit,J., Brinkmann,U. and Schaffrath,R.
  TITLE     Diphthamide-deficiency syndrome: a novel human developmental
            disorder and ribosomopathy
  JOURNAL   Eur J Hum Genet 28 (11), 1497-1508 (2020)
   PUBMED   32576952
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Urreizti,R., Mayer,K., Evrony,G.D., Said,E., Castilla-Vallmanya,L.,
            Cody,N.A.L., Plasencia,G., Gelb,B.D., Grinberg,D., Brinkmann,U.,
            Webb,B.D. and Balcells,S.
  TITLE     DPH1 syndrome: two novel variants and structural and functional
            analyses of seven missense variants identified in syndromic
            patients
  JOURNAL   Eur J Hum Genet 28 (1), 64-75 (2020)
   PUBMED   30877278
  REMARK    Erratum:[Eur J Hum Genet. 2020 Jan;28(1):138. doi:
            10.1038/s41431-019-0394-5. PMID: 31477843]
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Zhang,Y., Zhu,X., Torelli,A.T., Lee,M., Dzikovski,B.,
            Koralewski,R.M., Wang,E., Freed,J., Krebs,C., Ealick,S.E. and
            Lin,H.
  TITLE     Diphthamide biosynthesis requires an organic radical generated by
            an iron-sulphur enzyme
  JOURNAL   Nature 465 (7300), 891-896 (2010)
   PUBMED   20559380
  REMARK    Erratum:[Nature. 2011 May 26;473(7348):544]
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Liu,S., Milne,G.T., Kuremsky,J.G., Fink,G.R. and Leppla,S.H.
  TITLE     Identification of the proteins required for biosynthesis of
            diphthamide, the target of bacterial ADP-ribosylating toxins on
            translation elongation factor 2
  JOURNAL   Mol Cell Biol 24 (21), 9487-9497 (2004)
   PUBMED   15485916
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Schultz,D.C., Balasara,B.R., Testa,J.R. and Godwin,A.K.
  TITLE     Cloning and localization of a human diphthamide biosynthesis-like
            protein-2 gene, DPH2L2
  JOURNAL   Genomics 52 (2), 186-191 (1998)
   PUBMED   9782084
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Foley,B.T., Moehring,J.M. and Moehring,T.J.
  TITLE     Mutations in the elongation factor 2 gene which confer resistance
            to diphtheria toxin and Pseudomonas exotoxin A. Genetic and
            biochemical analyses
  JOURNAL   J Biol Chem 270 (39), 23218-23225 (1995)
   PUBMED   7559470
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Mattheakis,L.C., Sor,F. and Collier,R.J.
  TITLE     Diphthamide synthesis in Saccharomyces cerevisiae: structure of the
            DPH2 gene
  JOURNAL   Gene 132 (1), 149-154 (1993)
   PUBMED   8406038
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG385934.1, AK315506.1,
            AK091303.1 and AA252672.1.
            
            Summary: This gene is one of two human genes similar to the yeast
            gene dph2. The yeast gene was identified by its ability to
            complement a diphthamide mutant strain, and thus probably functions
            in diphthamide biosynthesis. Diphthamide is a post-translationally
            modified histidine residue present in elongation factor 2 (EF2)
            that is the target of diphtheria toxin ADP-ribosylation. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice junction compared to variant 1. The resulting isoform (d)
            has the same N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.274621.1,
                                           SRR1803614.180040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..398
                     /product="2-(3-amino-3-carboxypropyl)histidine synthase
                     subunit 2 isoform d"
                     /EC_number="2.5.1.108"
                     /note="diphthamide biosynthesis-like protein 2; DPH2-like
                     2; diphthamide biosynthesis protein 2 homolog-like 2;
                     diptheria toxin resistance protein required for
                     diphthamide biosynthesis-like 2; diphtheria toxin
                     resistance protein 2; S-adenosyl-L-methionine:L-histidine
                     3-amino-3-carboxypropyltransferase 2; DPH2 homolog;
                     2-(3-amino-3-carboxypropyl)histidine synthase subunit 2"
                     /calculated_mol_wt=42057
     Region          32..277
                     /region_name="diphth2_R"
                     /note="diphthamide biosynthesis enzyme Dph1/Dph2 domain;
                     TIGR00322"
                     /db_xref="CDD:273013"
     CDS             1..398
                     /gene="DPH2"
                     /gene_synonym="DEDSSH2; DPH2L2"
                     /coded_by="NM_001319166.2:167..1363"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:1802"
                     /db_xref="HGNC:HGNC:3004"
                     /db_xref="MIM:603456"
ORIGIN      
        1 mesmfsspae aalqretgvp glltplpdld gvyelervag fvrdlgcerv alqfpdqllg
       61 davavaarle ettgskmfil gdtaygsccv dvlgaeqaga qalihfgpac lspparplpv
      121 afvlrqrsva lelcvkafea qnpdpkapvv llsepacaha ldtgktqdeg aragrlrarr
      181 rylverarda rvvgllagtl gvaqhreala hlrnltqaag krsyvlalgr ptpaklanfp
      241 evdvfvllac plgalapqls gsffqpilap celeaacnpa wpppglaphl thyadllpgs
      301 pfhvalpppe selwetpdvs litgdlrppp awkssndhgs laltprpqle laesspaasf
      361 lssrswqgle prlgqtpvte avsgrrgiai ayedegsg
//
LOCUS       NP_001352357             564 aa            linear   PRI 20-NOV-2025
DEFINITION  TRPM8 channel-associated factor 2 isoform E [Homo sapiens].
ACCESSION   NP_001352357
VERSION     NP_001352357.1
DBSOURCE    REFSEQ: accession NM_001365428.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Yun,D., Liang,J., Wang,X., Fan,J., Wang,X., Li,J., Ren,X., Liu,J.,
            Ren,X., Zhang,H., Shang,G., Jin,W., Chen,L., Li,T., Zhang,C., Yu,S.
            and Yang,X.
  TITLE     TCAF2 drives glioma cellular migratory/invasion properties through
            STAT3 signaling
  JOURNAL   Mol Cell Biochem 479 (7), 1801-1815 (2024)
   PUBMED   38019450
  REMARK    GeneRIF: TCAF2 drives glioma cellular migratory/invasion properties
            through STAT3 signaling.
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Li,Y., Li,J., Chen,H., Lu,B., Lu,F., Chen,H., Liu,H. and Qian,C.
  TITLE     TCAF2 is associated with the immune microenvironment, promotes
            pathogenesis, and impairs prognosis in glioma
  JOURNAL   Gene 883, 147667 (2023)
   PUBMED   37506986
  REMARK    GeneRIF: TCAF2 is associated with the immune microenvironment,
            promotes pathogenesis, and impairs prognosis in glioma.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Li,X., Qi,Q., Li,Y., Miao,Q., Yin,W., Pan,J., Zhao,Z., Chen,X.,
            Yang,F., Zhou,X., Huang,M., Wang,C., Deng,L., Huang,D., Qi,M.,
            Fan,S., Zhang,Y., Qiu,S., Deng,W., Liu,T., Chen,M., Ye,W. and
            Zhang,D.
  TITLE     TCAF2 in Pericytes Promotes Colorectal Cancer Liver Metastasis via
            Inhibiting Cold-Sensing TRPM8 Channel
  JOURNAL   Adv Sci (Weinh) 10 (30), e2302717 (2023)
   PUBMED   37635201
  REMARK    GeneRIF: TCAF2 in Pericytes Promotes Colorectal Cancer Liver
            Metastasis via Inhibiting Cold-Sensing TRPM8 Channel.
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Hsieh,P., Dang,V., Vollger,M.R., Mao,Y., Huang,T.H., Dishuck,P.C.,
            Baker,C., Cantsilieris,S., Lewis,A.P., Munson,K.M., Sorensen,M.,
            Welch,A.E., Underwood,J.G. and Eichler,E.E.
  TITLE     Evidence for opposing selective forces operating on human-specific
            duplicated TCAF genes in Neanderthals and humans
  JOURNAL   Nat Commun 12 (1), 5118 (2021)
   PUBMED   34433829
  REMARK    GeneRIF: Evidence for opposing selective forces operating on
            human-specific duplicated TCAF genes in Neanderthals and humans.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Gkika,D., Lemonnier,L., Shapovalov,G., Gordienko,D., Poux,C.,
            Bernardini,M., Bokhobza,A., Bidaux,G., Degerny,C., Verreman,K.,
            Guarmit,B., Benahmed,M., de Launoit,Y., Bindels,R.J., Fiorio Pla,A.
            and Prevarskaya,N.
  TITLE     TRP channel-associated factors are a novel protein family that
            regulates TRPM8 trafficking and activity
  JOURNAL   J Cell Biol 208 (1), 89-107 (2015)
   PUBMED   25559186
  REMARK    GeneRIF: Report novel TRP channel-associated factors that modulate
            TRPM8 activity.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK098041.1, BC113530.1 and AL832734.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.152170.1, AK098041.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35"
     Protein         1..564
                     /product="TRPM8 channel-associated factor 2 isoform E"
                     /note="family with sequence similarity 139, member A;
                     protein FAM115C; family with sequence similarity 115,
                     member C; TRP channel-associated factor 2"
                     /calculated_mol_wt=61966
     Region          241..351
                     /region_name="M60-like_N"
                     /note="N-terminal domain of M60-like peptidases;
                     pfam17291"
                     /db_xref="CDD:435844"
     Region          352..>554
                     /region_name="Peptidase_M60"
                     /note="Peptidase M60, enhancin and enhancin-like;
                     pfam13402"
                     /db_xref="CDD:433178"
     CDS             1..564
                     /gene="TCAF2"
                     /gene_synonym="FAM115C; FAM139A; GATD9; GATD9B"
                     /coded_by="NM_001365428.1:268..1962"
                     /note="isoform E is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS94223.1"
                     /db_xref="GeneID:285966"
                     /db_xref="HGNC:HGNC:26878"
                     /db_xref="MIM:616252"
ORIGIN      
        1 mgpfllnavr wlargqtgkv gvntnlkdlc pllsehglqc slephlnsdl cvycckaysd
       61 keakqlqefv aeggglligg qawwwasqnp ghcplagfpg niilncfgls ilpqtlkagc
      121 fpvptpemrs yhfrkalsqf qailnhengn leksclaklr vdgaaflqip aegvpayisl
      181 hrllrkmlrg sglpavsren pvasdsyeaa vlslatglah sgtdcsqlaq glgtwtcsss
      241 lypskhpitv einginpgnn dcwvstglyl legqnaevsl seaaasaglr vqigchtddl
      301 tkarklsrap vvthqcwmdr tersvsclwg gllyvivpkg sqlgpvpvti rgavpapyyk
      361 lgktsleewk rqmqenlapw gelatdniil tvpttnlqal kdpepvlrlw demmqavarl
      421 aaepfpfrrp erivadvqis agwmhsgypi mchlesvkei inemdmrsrg vwgpihelgh
      481 nqqrhgwefp phtteatcnl wsvyvhetvl gipraqahea lsppererri kahlgkgapl
      541 cdwnvwtale tylqvlsrns grrg
//
LOCUS       NP_031393                290 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein Raly isoform 2 [Homo sapiens].
ACCESSION   NP_031393
VERSION     NP_031393.2
DBSOURCE    REFSEQ: accession NM_007367.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Zhou,J., Li,L., Han,Y., Ge,G., Ji,Q. and Li,H.
  TITLE     RNA binding protein RALY facilitates colorectal cancer metastasis
            via enhancing exosome biogenesis in m6A dependent manner
  JOURNAL   Int J Biol Macromol 273 (Pt 2), 133112 (2024)
   PUBMED   38880454
  REMARK    GeneRIF: RNA binding protein RALY facilitates colorectal cancer
            metastasis via enhancing exosome biogenesis in m6A dependent
            manner.
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Cao,S., Wang,D., Wang,P., Liu,Y., Dong,W., Ruan,X., Liu,L., Xue,Y.,
            E,T., Lin,H. and Liu,X.
  TITLE     SUMOylation of RALY promotes vasculogenic mimicry in glioma cells
            via the FOXD1/DKK1 pathway
  JOURNAL   Cell Biol Toxicol 39 (6), 3323-3340 (2023)
   PUBMED   37906341
  REMARK    GeneRIF: SUMOylation of RALY promotes vasculogenic mimicry in
            glioma cells via the FOXD1/DKK1 pathway.
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Khrebtukova,I., Kuklin,A., Woychik,R.P. and Michaud,E.J.
  TITLE     Alternative processing of the human and mouse raly genes(1)
  JOURNAL   Biochim Biophys Acta 1447 (1), 107-112 (1999)
   PUBMED   10500250
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Rhodes,G.H., Valbracht,J.R., Nguyen,M.D. and Vaughan,J.H.
  TITLE     The p542 gene encodes an autoantigen that cross-reacts with EBNA-1
            of the Epstein Barr virus and which may be a heterogeneous nuclear
            ribonucleoprotein
  JOURNAL   J Autoimmun 10 (5), 447-454 (1997)
   PUBMED   9376072
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Vaughan,J.H., Valbracht,J.R., Nguyen,M.D., Handley,H.H.,
            Smith,R.S., Patrick,K. and Rhodes,G.H.
  TITLE     Epstein-Barr virus-induced autoimmune responses. I. Immunoglobulin
            M autoantibodies to proteins mimicking and not mimicking
            Epstein-Barr virus nuclear antigen-1
  JOURNAL   J Clin Invest 95 (3), 1306-1315 (1995)
   PUBMED   7533788
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK226085.1, AL031668.23 and
            BM680768.1.
            
            On Jun 12, 2002 this sequence version replaced NP_031393.1.
            
            Summary: This gene encodes a member of the heterogeneous nuclear
            ribonucleoprotein (hnRNP) gene family. This protein may play a role
            in pre-mRNA splicing and in embryonic development. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1. This isoform is also known as short
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.156200.1,
                                           SRR3476690.30820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..290
                     /product="RNA-binding protein Raly isoform 2"
                     /note="RNA-binding protein (autoantigenic); RNA-binding
                     protein (autoantigenic, hnRNP-associated with lethal
                     yellow); RNA binding protein, autoantigenic
                     (hnRNP-associated with lethal yellow homolog); RNA-binding
                     protein Raly; autoantigen p542; hnRNP core protein C-like
                     2; heterogeneous nuclear ribonucleoprotein C-like 2; hnRNP
                     associated with lethal yellow protein homolog"
                     /calculated_mol_wt=30233
     Region          20..95
                     /region_name="RRM_RALY"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein Raly; cd12604"
                     /db_xref="CDD:410016"
     CDS             1..290
                     /gene="RALY"
                     /gene_synonym="HNRPCL2; P542"
                     /coded_by="NM_007367.4:314..1186"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS13229.1"
                     /db_xref="GeneID:22913"
                     /db_xref="HGNC:HGNC:15921"
                     /db_xref="MIM:614663"
ORIGIN      
        1 mslklqasnv tnkndpksin srvfignlnt alvkksdvet ifskygrvag csvhkgyafv
       61 qysnerhara avlgengrvl agqtldinma gepkpdrpkg lkraasaiyr lfdyrgrlsp
      121 vpvpravpvk rprvtvplvr rvktnvpvkl farstavtts sakiklksse lqaikteltq
      181 iksnidalls rleqiaaeqk anpdgkkkgd gggagggggg ggsggggsgg gggggssrpp
      241 apqenttsea glpqgeartr ddgdeegllt hseeelehsq dtdaddgalq
//
LOCUS       NP_001291720             255 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 44 isoform 1 [Homo sapiens].
ACCESSION   NP_001291720 XP_005263595
VERSION     NP_001291720.1
DBSOURCE    REFSEQ: accession NM_001304791.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Shen,J.Z., Qiu,Z., Wu,Q., Finlay,D., Garcia,G., Sun,D., Rantala,J.,
            Barshop,W., Hope,J.L., Gimple,R.C., Sangfelt,O., Bradley,L.M.,
            Wohlschlegel,J., Rich,J.N. and Spruck,C.
  TITLE     FBXO44 promotes DNA replication-coupled repetitive element
            silencing in cancer cells
  JOURNAL   Cell 184 (2), 352-369 (2021)
   PUBMED   33357448
  REMARK    GeneRIF: FBXO44 promotes DNA replication-coupled repetitive element
            silencing in cancer cells.
REFERENCE   4  (residues 1 to 255)
  AUTHORS   McNabb,H.J., Gonzalez,S., Muli,C.S. and Sjogren,B.
  TITLE     N-Terminal Targeting of Regulator of G Protein Signaling Protein 2
            for F-Box Only Protein 44-Mediated Proteasomal Degradation
  JOURNAL   Mol Pharmacol 98 (6), 677-685 (2020)
   PUBMED   33008920
  REMARK    GeneRIF: N-Terminal Targeting of Regulator of G Protein Signaling
            Protein 2 for F-Box Only Protein 44-Mediated Proteasomal
            Degradation.
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 255)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 255)
  AUTHORS   Glenn,K.A., Nelson,R.F., Wen,H.M., Mallinger,A.J. and Paulson,H.L.
  TITLE     Diversity in tissue expression, substrate binding, and SCF complex
            formation for a lectin family of ubiquitin ligases
  JOURNAL   J Biol Chem 283 (19), 12717-12729 (2008)
   PUBMED   18203720
REFERENCE   8  (residues 1 to 255)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 255)
  AUTHORS   Ilyin,G.P., Serandour,A.L., Pigeon,C., Rialland,M., Glaise,D. and
            Guguen-Guillouzo,C.
  TITLE     A new subfamily of structurally related human F-box proteins
  JOURNAL   Gene 296 (1-2), 11-20 (2002)
   PUBMED   12383498
REFERENCE   10 (residues 1 to 255)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055344.1, BM546141.1 and
            AL031731.44.
            
            On Feb 10, 2015 this sequence version replaced XP_005263595.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. It is also a member of the NFB42 (neural
            F Box 42 kDa) family, similar to F-box only protein 2 and F-box
            only protein 6. Several alternatively spliced transcript variants
            encoding two distinct isoforms have been found for this gene.
            [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to isoform 1. Variants 1, 4, and 6 all encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.233761.1,
                                           SRR1803613.420104.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..255
                     /product="F-box only protein 44 isoform 1"
                     /note="F-box protein FBX30; F-box gene 3; F-box only
                     protein 44; F-box/G-domain protein 3"
                     /calculated_mol_wt=29616
     Region          3..85
                     /region_name="F-box_FBXO6-like"
                     /note="F-box domain found in F-box only proteins FBXO6,
                     FBXO44 and similar proteins; cd22168"
                     /db_xref="CDD:438939"
     Site            order(3,5..7,9..10,13,17,20,22,24..25,27,30..35,37..38,70)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438939"
     Region          72..250
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     CDS             1..255
                     /gene="FBXO44"
                     /gene_synonym="FBG3; FBX30; Fbx44; FBX6A; Fbxo6a"
                     /coded_by="NM_001304791.2:206..973"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS132.1"
                     /db_xref="GeneID:93611"
                     /db_xref="HGNC:HGNC:24847"
                     /db_xref="MIM:609111"
ORIGIN      
        1 mavgninelp enillelfth vparqlllnc rlvcslwrdl idlvtlwkrk clregfited
       61 wdqpvadwki fyflrslhrn llhnpcaeeg fefwsldvng gdewkvedls rdqrkefpnd
      121 qvkkyfvtsy ytclksqvvd lkaegyweel mdttrpdiev kdwfaarpdc gskyqlcvql
      181 lssahaplgt fqpdpatiqq ksdakwrevs htfsnyppgv ryiwfqhggv dthywagwyg
      241 prvtnssiti gpplp
//
LOCUS       NP_001305906             333 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            B isoform b [Homo sapiens].
ACCESSION   NP_001305906 XP_011508714
VERSION     NP_001305906.1
DBSOURCE    REFSEQ: accession NM_001318977.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Okuda,H., Kanai,A., Ito,S., Matsui,H. and Yokoyama,A.
  TITLE     AF4 uses the SL1 components of RNAP1 machinery to initiate MLL
            fusion- and AEP-dependent transcription
  JOURNAL   Nat Commun 6, 8869 (2015)
   PUBMED   26593443
  REMARK    GeneRIF: AEP coactivator complex facilitates the initiation of
            RNAP2-dependent transcription via SL1 activity by loading TBP onto
            the TATA element.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Muth,V., Nadaud,S., Grummt,I. and Voit,R.
  TITLE     Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA
            polymerase I transcription
  JOURNAL   EMBO J 20 (6), 1353-1362 (2001)
   PUBMED   11250901
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Zhai,W. and Comai,L.
  TITLE     Repression of RNA polymerase I transcription by the tumor
            suppressor p53
  JOURNAL   Mol Cell Biol 20 (16), 5930-5938 (2000)
   PUBMED   10913176
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Di Pietro,C., Rapisarda,A., Amico,V., Bonaiuto,C., Viola,A.,
            Scalia,M., Motta,S., Amato,A., Engel,H., Messina,A., Sichel,G.,
            Grzeschik,K. and Purrello,M.
  TITLE     Genomic localization of the human genes TAF1A, TAF1B and TAF1C,
            encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I
            general transcription initiation factor SL1
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 133-136 (2000)
   PUBMED   10894955
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Comai,L., Zomerdijk,J.C., Beckmann,H., Zhou,S., Admon,A. and
            Tjian,R.
  TITLE     Reconstitution of transcription factor SL1: exclusive binding of
            TBP by SL1 or TFIID subunits
  JOURNAL   Science 266 (5193), 1966-1972 (1994)
   PUBMED   7801123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA910748.1, AC010969.11,
            AK026521.1, AK308070.1 and AA746267.1.
            
            On Jan 20, 2016 this sequence version replaced XP_011508714.1.
            
            Summary: Initiation of transcription by RNA polymerase I requires
            the formation of a complex composed of the TATA-binding protein
            (TBP) and three TBP-associated factors (TAFs) specific for RNA
            polymerase I. This complex, known as SL1, binds to the core
            promoter of ribosomal RNA genes to position the polymerase properly
            and acts as a channel for regulatory signals. This gene encodes one
            of the SL1-specific TAFs. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.71386.1,
                                           SRR1803617.50333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..333
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit B isoform b"
                     /note="SL1, 63kD subunit; TBP-associated factor 1B; TATA
                     box-binding protein-associated factor 1B; transcription
                     initiation factor SL1/TIF-IB subunit B; RNA polymerase
                     I-specific TBP-associated factor 63 kDa; TATA box binding
                     protein (TBP)-associated factor, RNA polymerase I, B,
                     63kD; TATA-box binding protein associated factor, RNA
                     polymerase I, B; TATA box binding protein (TBP)-associated
                     factor, RNA polymerase I, B, 63kDa"
                     /calculated_mol_wt=39416
     CDS             1..333
                     /gene="TAF1B"
                     /gene_synonym="MGC:9349; RAF1B; RAFI63; SL1; TAFI63"
                     /coded_by="NM_001318977.1:712..1713"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:9014"
                     /db_xref="HGNC:HGNC:11533"
                     /db_xref="MIM:604904"
ORIGIN      
        1 mklygrdrgi fgieswpdye diykktievg tfldlprfpd itedcylhpn ilcmkylmev
       61 nlpdemhslt chvvkmtgmg evdfltfdpi akmaktvkyd vqavaiivvv lkllflldds
      121 fewslsnlae khneknkkdk pwfdfrkwyq imkkafdekk qkweearaky lwksekplyy
      181 sfvdkpvayk kremvvnlqk qfstlvesta tagkkspssf qfnwteedtd rtcfhghslq
      241 gvlkekgqsl ltknslywls tqkfcrcyct hvttyeesny slsyqfilnl fsfllrikts
      301 llheevslve kklfekkysv krkksrskkv rrh
//
LOCUS       NP_001271320             231 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription cofactor vestigial-like protein 4 isoform f [Homo
            sapiens].
ACCESSION   NP_001271320 XP_005265667
VERSION     NP_001271320.1
DBSOURCE    REFSEQ: accession NM_001284391.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Wang,Z., Quan,Y., Hu,M., Xu,Y., Chen,Y., Jin,P., Ma,J., Chen,X.,
            Fan,J., Fan,X., Gong,Y., Li,M. and Wang,Y.
  TITLE     VGLL4-TEAD1 promotes vascular smooth muscle cell differentiation
            from human pluripotent stem cells via TET2
  JOURNAL   J Mol Cell Cardiol 176, 21-32 (2023)
   PUBMED   36657637
  REMARK    GeneRIF: VGLL4-TEAD1 promotes vascular smooth muscle cell
            differentiation from human pluripotent stem cells via TET2.
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Geng,H., Liu,G., Hu,J., Li,J., Wang,D., Zou,S. and Xu,X.
  TITLE     HOXB13 suppresses proliferation, migration and invasion, and
            promotes apoptosis of gastric cancer cells through transcriptional
            activation of VGLL4 to inhibit the involvement of TEAD4 in the
            Hippo signaling pathway
  JOURNAL   Mol Med Rep 24 (4) (2021)
   PUBMED   34396425
  REMARK    GeneRIF: HOXB13 suppresses proliferation, migration and invasion,
            and promotes apoptosis of gastric cancer cells through
            transcriptional activation of VGLL4 to inhibit the involvement of
            TEAD4 in the Hippo signaling pathway.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Mesrouze,Y., Meyerhofer,M., Zimmermann,C., Fontana,P., Erdmann,D.
            and Chene,P.
  TITLE     Biochemical properties of VGLL4 from Homo sapiens and Tgi from
            Drosophila melanogaster and possible biological implications
  JOURNAL   Protein Sci 30 (9), 1871-1881 (2021)
   PUBMED   34075638
  REMARK    GeneRIF: Biochemical properties of VGLL4 from Homo sapiens and Tgi
            from Drosophila melanogaster and possible biological implications.
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Mickle,M., Adhikary,G., Shrestha,S., Xu,W. and Eckert,R.L.
  TITLE     VGLL4 inhibits YAP1/TEAD signaling to suppress the epidermal
            squamous cell carcinoma cancer phenotype
  JOURNAL   Mol Carcinog 60 (7), 497-507 (2021)
   PUBMED   34004031
  REMARK    GeneRIF: VGLL4 inhibits YAP1/TEAD signaling to suppress the
            epidermal squamous cell carcinoma cancer phenotype.
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Jin,H.S., Park,H.S., Shin,J.H., Kim,D.H., Jun,S.H., Lee,C.J. and
            Lee,T.H.
  TITLE     A novel inhibitor of apoptosis protein (IAP)-interacting protein,
            Vestigial-like (Vgl)-4, counteracts apoptosis-inhibitory function
            of IAPs by nuclear sequestration
  JOURNAL   Biochem Biophys Res Commun 412 (3), 454-459 (2011)
   PUBMED   21839727
  REMARK    GeneRIF: Vgl-4 may play a role in the apoptotic pathways by
            regulating translocation of IAPs between different cell
            compartments.
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Teng,A.C., Kuraitis,D., Deeke,S.A., Ahmadi,A., Dugan,S.G.,
            Cheng,B.L., Crowson,M.G., Burgon,P.G., Suuronen,E.J., Chen,H.H. and
            Stewart,A.F.
  TITLE     IRF2BP2 is a skeletal and cardiac muscle-enriched
            ischemia-inducible activator of VEGFA expression
  JOURNAL   FASEB J 24 (12), 4825-4834 (2010)
   PUBMED   20702774
  REMARK    GeneRIF: IRF2BP2 was identifies as a novel VGLL4 partner.
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Chen,H.H., Mullett,S.J. and Stewart,A.F.
  TITLE     Vgl-4, a novel member of the vestigial-like family of transcription
            cofactors, regulates alpha1-adrenergic activation of gene
            expression in cardiac myocytes
  JOURNAL   J Biol Chem 279 (29), 30800-30806 (2004)
   PUBMED   15140898
  REMARK    GeneRIF: Vgl-4 modulates the activity of TEF-1 factors and
            counteracts alpha1-adrenergic activation of gene expression in
            cardiac myocytes
            GeneRIF: A transcriptional cofactor of transcriptional enhancer
            factor-1 (TEF-1) transcription factors.  Interacts with TEF-1
            factors through 2 TDU (tondu) motifs.  Controls gene expression in
            cardiac myocytes.
            GeneRIF: This gene is named Vestigial-like 4, to distinguish it
            from 3 previously described genes Vgl-1, Vgl-2 and Vgl-3. Contains
            2 motifs, found in the Drosophila transcription cofactor Vestigial,
            that interact with the TEF-1 family of transcription factors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK300344.1, AC022001.5, DA383197.1, D50911.3, BU682809.1 and
            AI809612.1.
            
            On Oct 1, 2013 this sequence version replaced XP_005265667.1.
            
            Transcript Variant: This variant (6) contains alternate 5' exon
            structure and it thus differs in the 5' UTR and 5' coding region,
            compared to variant 1. The encoded isoform (f) has a distinct
            N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300344.1, SRR1163658.256863.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3-p25.2"
     Protein         1..231
                     /product="transcription cofactor vestigial-like protein 4
                     isoform f"
                     /note="Vestigial-like 4; transcription cofactor
                     vestigial-like protein 4; vestigial like 4"
                     /calculated_mol_wt=24440
     Region          <1..165
                     /region_name="VGLL4"
                     /note="Transcription cofactor vestigial-like protein 4;
                     pfam15245"
                     /db_xref="CDD:464585"
     Region          175..190
                     /region_name="TDU"
                     /note="Short repeats in human TONDU, fly vestigial and
                     other proteins; smart00711"
                     /db_xref="CDD:197839"
     CDS             1..231
                     /gene="VGLL4"
                     /gene_synonym="VGL-4"
                     /coded_by="NM_001284391.1:372..1067"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS68342.1"
                     /db_xref="GeneID:9686"
                     /db_xref="HGNC:HGNC:28966"
                     /db_xref="MIM:618692"
ORIGIN      
        1 mepgdedldc dndhvskmsr ifnphlnkta ngdcrrdpre rsrspierav aptmslhgsh
       61 lytslpslgl eqplaltkns ldasrpagls ptltpgerqq nrpsvitcas agarncnlsh
      121 cpiahsgcaa pgpasyrrpp saattcdpvv eehfrrslgk nykepepapn svsitgsvdd
      181 hfakalgdtw lqikaakdga ssspesasrr gqpaspsahm vshshspsvv s
//
LOCUS       NP_116023               1089 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI ethanolamine phosphate transferase 3, catalytic subunit isoform
            1 [Homo sapiens].
ACCESSION   NP_116023
VERSION     NP_116023.2
DBSOURCE    REFSEQ: accession NM_032634.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1089)
  AUTHORS   Kinoshita,T.
  TITLE     Biosynthesis and biology of mammalian GPI-anchored proteins
  JOURNAL   Open Biol 10 (3), 190290 (2020)
   PUBMED   32156170
  REMARK    Review article
REFERENCE   2  (residues 1 to 1089)
  AUTHORS   Tanigawa,J., Mimatsu,H., Mizuno,S., Okamoto,N., Fukushi,D.,
            Tominaga,K., Kidokoro,H., Muramatsu,Y., Nishi,E., Nakamura,S.,
            Motooka,D., Nomura,N., Hayasaka,K., Niihori,T., Aoki,Y.,
            Nabatame,S., Hayakawa,M., Natsume,J., Ozono,K., Kinoshita,T.,
            Wakamatsu,N. and Murakami,Y.
  TITLE     Phenotype-genotype correlations of PIGO deficiency with variable
            phenotypes from infantile lethality to mild learning difficulties
  JOURNAL   Hum Mutat 38 (7), 805-815 (2017)
   PUBMED   28337824
  REMARK    GeneRIF: PIGO deficiency shows variable phenotypes from infantile
            lethality to mild learning difficulties
REFERENCE   3  (residues 1 to 1089)
  AUTHORS   Pagnamenta,A.T., Murakami,Y., Taylor,J.M., Anzilotti,C.,
            Howard,M.F., Miller,V., Johnson,D.S., Tadros,S., Mansour,S.,
            Temple,I.K., Firth,R., Rosser,E., Harrison,R.E., Kerr,B.,
            Popitsch,N., Kinoshita,T., Taylor,J.C. and Kini,U.
  CONSRTM   DDD Study
  TITLE     Analysis of exome data for 4293 trios suggests GPI-anchor
            biogenesis defects are a rare cause of developmental disorders
  JOURNAL   Eur J Hum Genet 25 (6), 669-679 (2017)
   PUBMED   28327575
  REMARK    GeneRIF: Disease associated PIGO missense mutations resulted in
            decreased activity in vitro.
REFERENCE   4  (residues 1 to 1089)
  AUTHORS   Nakamura,K., Osaka,H., Murakami,Y., Anzai,R., Nishiyama,K.,
            Kodera,H., Nakashima,M., Tsurusaki,Y., Miyake,N., Kinoshita,T.,
            Matsumoto,N. and Saitsu,H.
  TITLE     PIGO mutations in intractable epilepsy and severe developmental
            delay with mild elevation of alkaline phosphatase levels
  JOURNAL   Epilepsia 55 (2), e13-e17 (2014)
   PUBMED   24417746
  REMARK    GeneRIF: Novel PIGO mutations expand the clinical spectrum of PIGO
            abnormalities to include epileptic encephalopathy with mild
            elevation of alkaline phosphatase (ALP).
REFERENCE   5  (residues 1 to 1089)
  AUTHORS   Kuki,I., Takahashi,Y., Okazaki,S., Kawawaki,H., Ehara,E., Inoue,N.,
            Kinoshita,T. and Murakami,Y.
  TITLE     Vitamin B6-responsive epilepsy due to inherited GPI deficiency
  JOURNAL   Neurology 81 (16), 1467-1469 (2013)
   PUBMED   24049131
  REMARK    Erratum:[Neurology. 2013 Nov 12;81(20):1803]
REFERENCE   6  (residues 1 to 1089)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   7  (residues 1 to 1089)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 1089)
  AUTHORS   Takeda,S., Kadowaki,S., Haga,T., Takaesu,H. and Mitaku,S.
  TITLE     Identification of G protein-coupled receptor genes from the human
            genome sequence
  JOURNAL   FEBS Lett 520 (1-3), 97-101 (2002)
   PUBMED   12044878
  REMARK    Erratum:[FEBS Lett 2002 Jul 17;523(1-3):257]
REFERENCE   9  (residues 1 to 1089)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   10 (residues 1 to 1089)
  AUTHORS   Hong,Y., Maeda,Y., Watanabe,R., Inoue,N., Ohishi,K. and
            Kinoshita,T.
  TITLE     Requirement of PIG-F and PIG-O for transferring phosphoethanolamine
            to the third mannose in glycosylphosphatidylinositol
  JOURNAL   J Biol Chem 275 (27), 20911-20919 (2000)
   PUBMED   10781593
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353795.13, CR985224.1,
            AY358472.1, BC029271.1, BE139632.1 and BU727886.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2002 this sequence version replaced NP_116023.1.
            
            Summary: This gene encodes a protein that is involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid which contains three mannose molecules
            in its core backbone. The GPI-anchor is found on many blood cells
            and serves to anchor proteins to the cell surface. This protein is
            involved in the transfer of ethanolaminephosphate (EtNP) to the
            third mannose in GPI. At least three alternatively spliced
            transcripts encoding two distinct isoforms have been found for this
            gene. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.144472.1, AL833956.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378617.4/ ENSP00000367880.3
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1089
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..1089
                     /product="GPI ethanolamine phosphate transferase 3,
                     catalytic subunit isoform 1"
                     /note="GPI ethanolamine phosphate transferase 3;
                     phosphatidylinositol-glycan biosynthesis class O protein;
                     GPI ethanolamine phosphate transferase 3, catalytic
                     subunit"
                     /calculated_mol_wt=118568
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Region          65..344
                     /region_name="GPI_EPT_3"
                     /note="GPI ethanolamine phosphate transferase 3, PIG-O;
                     cd16023"
                     /db_xref="CDD:293747"
     Site            order(76,131,235,277..278)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293747"
     Site            order(76,131,235,278)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293747"
     Site            268
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            457..477
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            510..530
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            575..595
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            668..688
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            701..721
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            747..767
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            830..850
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            857..877
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            944..964
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            1014..1034
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     Site            1048..1068
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEQ8.3)"
     CDS             1..1089
                     /gene="PIGO"
                     /gene_synonym="hGPCR43; HPMRS2"
                     /coded_by="NM_032634.4:439..3708"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6575.1"
                     /db_xref="GeneID:84720"
                     /db_xref="HGNC:HGNC:23215"
                     /db_xref="MIM:614730"
ORIGIN      
        1 mqkasvllfl awvcflfyag ialftsgfll trleltnhss cqeppgpgsl pwgsqgkpga
       61 cwmasrfsrv vlvlidalrf dfaqpqhshv preppvslpf lgklsslqri leiqphharl
      121 yrsqvdpptt tmqrlkaltt gslptfidag snfashaive dnlikqltsa grrvvfmgdd
      181 twkdlfpgaf skafffpsfn vrdldtvdng ilehlyptmd sgewdvliah flgvdhcghk
      241 hgphhpemak klsqmdqviq glverlendt llvvagdhgm ttngdhggds elevsaalfl
      301 ysptavfpst ppeepevipq vslvptlall lglpipfgni gevmaelfsg gedsqphssa
      361 laqasalhln aqqvsrflht ysaatqdlqa kelhqlqnlf skasadyqwl lqspkgaeat
      421 lptviaelqq flrgaramci eswarfslvr maggtallaa scficllasq waispgfpfc
      481 pllltpvawg lvgaiayagl lgtielkldl vllgavaavs sflpflwkaw agwgskrpla
      541 tlfpipgpvl llllfrlavf fsdsfvvaea ratpfllgsf illlvvqlhw egqllppkll
      601 tmprlgtsat tnpprhngay alrlgiglll ctrlaglfhr cpeetpvchs spwlsplasm
      661 vggraknlwy gacvaalval laavrlwlrr ygnlkspepp mlfvrwglpl malgtaaywa
      721 lasgadeapp rlrvlvsgas mvlpravagl aasglalllw kpvtvlvkag agaprtrtvl
      781 tpfsgpptsq adldyvvpqi yrhmqeefrg rlertksqgp ltvaayqlgs vysaamvtal
      841 tllafpllll haerislvfl llflqsflll hllaagipvt tpgpftvpwq avsawalmat
      901 qtfystghqp vfpaihwhaa fvgfpeghgs ctwlpallvg antfashllf avgcpllllw
      961 pflcesqglr krqqppgnea darvrpeeee eplmemrlrd apqhfyaall qlglkylfil
     1021 giqilacala asilrrhlmv wkvfapkfif eavgfivssv glllgialvm rvdgavsswf
     1081 rqlflaqqr
//
LOCUS       NP_001265400            1688 aa            linear   PRI 20-NOV-2025
DEFINITION  protein MON2 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001265400
VERSION     NP_001265400.1
DBSOURCE    REFSEQ: accession NM_001278471.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1688)
  AUTHORS   Li,P., Wu,Q., Yang,X.R. and Sun,T.
  TITLE     MicroRNA-133a-5p inhibiting metastatic capacity of renal clear cell
            carcinoma through regulating MON2
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (11), 5988-5995 (2020)
   PUBMED   32572912
  REMARK    GeneRIF: MicroRNA-133a-5p inhibiting metastatic capacity of renal
            clear cell carcinoma through regulating MON2.
REFERENCE   2  (residues 1 to 1688)
  AUTHORS   Mahajan,D., Tie,H.C., Chen,B. and Lu,L.
  TITLE     Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for
            membrane trafficking
  JOURNAL   Nat Commun 10 (1), 3218 (2019)
   PUBMED   31324769
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1688)
  AUTHORS   McGough,I.J., de Groot,R.E.A., Jellett,A.P., Betist,M.C.,
            Varandas,K.C., Danson,C.M., Heesom,K.J., Korswagen,H.C. and
            Cullen,P.J.
  TITLE     SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A
            complex to mediate Wntless sorting and Wnt secretion
  JOURNAL   Nat Commun 9 (1), 3737 (2018)
   PUBMED   30213940
  REMARK    GeneRIF: an evolutionary conserved MON2:DOPEY2:ATP9A complex is
            required for SNX3 retromer mediation of Wntless sorting and Wnt
            secretion
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1688)
  AUTHORS   Mahajan,D., Boh,B.K., Zhou,Y., Chen,L., Cornvik,T.C., Hong,W. and
            Lu,L.
  TITLE     Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but
            possesses no guanine nucleotide exchange activity toward Arl1
            GTPase
  JOURNAL   Sci Rep 3, 3362 (2013)
   PUBMED   24285343
  REMARK    GeneRIF: Mon2 is involved in endosome-to-Golgi trafficking as its
            depletion accelerated the delivery of furin and CI-M6PR to Golgi
            after endocytosis.
            Erratum:[Sci Rep. 2016 Sep 22;6:33619. doi: 10.1038/srep33619.
            PMID: 27654351]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1688)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   6  (residues 1 to 1688)
  AUTHORS   Tomita,Y., Noda,T., Fujii,K., Watanabe,T., Morikawa,Y. and
            Kawaoka,Y.
  TITLE     The cellular factors Vps18 and Mon2 are required for efficient
            production of infectious HIV-1 particles
  JOURNAL   J Virol 85 (11), 5618-5627 (2011)
   PUBMED   21450827
  REMARK    GeneRIF: Depletion of hVps18 or hMon2 reduced the efficient
            production of infectious HIV-1 virions in human cells.
REFERENCE   7  (residues 1 to 1688)
  AUTHORS   Singer-Kruger,B., Lasic,M., Burger,A.M., Hausser,A., Pipkorn,R. and
            Wang,Y.
  TITLE     Yeast and human Ysl2p/hMon2 interact with Gga adaptors and mediate
            their subcellular distribution
  JOURNAL   EMBO J 27 (10), 1423-1435 (2008)
   PUBMED   18418388
  REMARK    GeneRIF: Ysl2p represents an essential, evolutionarily conserved
            member of a network controlling direct binding and membrane docking
            of Ggas.
REFERENCE   8  (residues 1 to 1688)
  AUTHORS   Gillingham,A.K., Whyte,J.R., Panic,B. and Munro,S.
  TITLE     Mon2, a relative of large Arf exchange factors, recruits Dop1 to
            the Golgi apparatus
  JOURNAL   J Biol Chem 281 (4), 2273-2280 (2006)
   PUBMED   16301316
REFERENCE   9  (residues 1 to 1688)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA125763.1, BC144309.1 and AC026115.27.
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice site at the 3' end of an exon and lacks an alternate
            in-frame exon compared to variant 1. The resulting isoform (4) has
            the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..1688
                     /product="protein MON2 homolog isoform 4"
                     /note="protein MON2 homolog; MON2 homolog, regulator of
                     endosome-to-Golgi trafficking"
                     /calculated_mol_wt=187190
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          9..180
                     /region_name="DCB"
                     /note="dimerization and cyclophilin-binding domain of
                     Mon2; pfam16213"
                     /db_xref="CDD:465072"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          212..381
                     /region_name="Sec7_N"
                     /note="Guanine nucleotide exchange factor in Golgi
                     transport N-terminal; pfam12783"
                     /db_xref="CDD:463703"
     Region          511..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80TL7; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          <553..>1059
                     /region_name="PLN03076"
                     /note="ARF guanine nucleotide exchange factor (ARF-GEF);
                     Provisional"
                     /db_xref="CDD:215560"
     Region          <849..908
                     /region_name="DUF1981"
                     /note="Domain of unknown function (DUF1981); pfam09324"
                     /db_xref="CDD:462756"
     Region          911..1679
                     /region_name="Mon2_C"
                     /note="C-terminal region of Mon2 protein; pfam16206"
                     /db_xref="CDD:465066"
     CDS             1..1688
                     /gene="MON2"
                     /coded_by="NM_001278471.2:383..5449"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61175.1"
                     /db_xref="GeneID:23041"
                     /db_xref="HGNC:HGNC:29177"
                     /db_xref="MIM:616822"
ORIGIN      
        1 msgtsspeav kkllenmqsd lralsleckk kfppvkeaae sgiikvktia arnteilaal
       61 kenssevvqp flmgcgtkep kitqlclaai qrlmshevvs etaagniinm lwqlmensle
      121 elkllqtvlv llttntvvhd ealskaivlc frlhftkdni tnntaaatvr qvvtvvferm
      181 vaederhrdi ieqpvlvqgn snrrsvstlk pcakdaymlf qdlcqlvnad apywlvgmte
      241 mtrtfglell esvlndfpqv flqhqefsfl lkervcplvi klfspnikfr qgsstssspa
      301 pvekpyfpic mrllrvvsvl ikqfysllvt eceiflsllv kfldadkpqw lravavesih
      361 rfcvqpqllr sfcqsydmkq hstkvfrdiv nalgsfiqsl flvpptgnpa tsnqagnnnl
      421 ggsvsapans gmvgigggvt llpafeyrgt wipiltitvq gsakatylem ldkvepptip
      481 egyamsvafh clldlvrgit smiegelgel etecqtttee gssptqsteq qdlqstsdqm
      541 dkeivsravw eemvnacwcg llaalsllld astdeaaten ilkaeltmaa lcgrlglvts
      601 rdafitaick aysvqgqsvm mispsseshq qvvavgqpla vqpqgtvmlt skniqcmrtl
      661 lnlahchgav lgtswqlvla tlqhlvwilg lkpssggalk pgravegpst vlttavmtdl
      721 pvisnilsrl fessqylddv slhhlinalc slsleamdma ygnnkepslf avaklletgl
      781 vnmhrieilw rpltghllev cqhpnsrmre wgaealtsli kagltfnhdp plsqnqrlql
      841 lllnplkems ninhpdirlk qlecvlqilq sqgdslgpgw plvlgvmgai rndqgeslir
      901 tafqclqlvv tdflptmpct clqivvdvag sfglhnqeln isltsigllw nisdyffqrg
      961 etiekelnke eaaqqkqaee kgvvlnrpfh pappfdclwl clyaklgelc vdprpavrks
     1021 agqtlfstig ahgtllqhst whtviwkvlf hlldrvress ttadkekies gggnilihhs
     1081 rdtaekqwae twvltlagva rifntrryll qplgdfsraw dvlldhiqsa alsknnevsl
     1141 aalksfqeil qivspvrdsd kpetppvvnv pvpvligpis gmsrpfvrtd sigeklgrys
     1201 sseppivtde ledlnlwwaa wntwyrigse stkppitfdk ltfipsqpfl taliqifpal
     1261 yqhiktgfnm ddlqklgvil hsaisvpiss daspfilpsy teavltslqe avltaldvlq
     1321 kaicvgpenm qimypaifdq llafvefsck ppqygqletk hianakynqa ewvalnyvpf
     1381 aerslevvvd lyqktachka vvnekvlqni iktlrvplsl kyscpsestw klavssllrv
     1441 lsiglpvarq hassgkfdsm wpelantfed flftksippd nlsiqefqrn enidvevvql
     1501 isneilpyan fipkefvgqi mtmlnkgsih sqsssfteae idirlreefs kmcfetllqf
     1561 sfsnkvttpq egyisrmals vllkrsqdvl hryiederls gkcplprqqv teiifvlkav
     1621 stlidslkkt qpenvdgntw aqvialyptl vecitcssse vcsalkealv pfkdfmqppa
     1681 srvqnges
//
LOCUS       NP_079479                721 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat and coiled-coil-containing protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_079479
VERSION     NP_079479.1
DBSOURCE    REFSEQ: accession NM_025203.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 721)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 721)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 721)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 721)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 721)
  AUTHORS   Xu,R., Xu,Y., Huo,W., Lv,Z., Yuan,J., Ning,S., Wang,Q., Hou,M.,
            Gao,G., Ji,J., Chen,J., Guo,R. and Xu,D.
  TITLE     Mitosis-specific MRN complex promotes a mitotic signaling cascade
            to regulate spindle dynamics and chromosome segregation
  JOURNAL   Proc Natl Acad Sci U S A 115 (43), E10079-E10088 (2018)
   PUBMED   30297404
REFERENCE   6  (residues 1 to 721)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 721)
  AUTHORS   Yokoyama,N. and Miller,W.T.
  TITLE     Molecular characterization of WDCP, a novel fusion partner for the
            anaplastic lymphoma tyrosine kinase ALK
  JOURNAL   Biomed Rep 3 (1), 9-13 (2015)
   PUBMED   25469238
REFERENCE   8  (residues 1 to 721)
  AUTHORS   Lipson,D., Capelletti,M., Yelensky,R., Otto,G., Parker,A.,
            Jarosz,M., Curran,J.A., Balasubramanian,S., Bloom,T., Brennan,K.W.,
            Donahue,A., Downing,S.R., Frampton,G.M., Garcia,L., Juhn,F.,
            Mitchell,K.C., White,E., White,J., Zwirko,Z., Peretz,T.,
            Nechushtan,H., Soussan-Gutman,L., Kim,J., Sasaki,H., Kim,H.R.,
            Park,S.I., Ercan,D., Sheehan,C.E., Ross,J.S., Cronin,M.T.,
            Janne,P.A. and Stephens,P.J.
  TITLE     Identification of new ALK and RET gene fusions from colorectal and
            lung cancer biopsies
  JOURNAL   Nat Med 18 (3), 382-384 (2012)
   PUBMED   22327622
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 721)
  AUTHORS   Lowe,J.K., Maller,J.B., Pe'er,I., Neale,B.M., Salit,J., Kenny,E.E.,
            Shea,J.L., Burkhardt,R., Smith,J.G., Ji,W., Noel,M., Foo,J.N.,
            Blundell,M.L., Skilling,V., Garcia,L., Sullivan,M.L., Lee,H.E.,
            Labek,A., Ferdowsian,H., Auerbach,S.B., Lifton,R.P.,
            Newton-Cheh,C., Breslow,J.L., Stoffel,M., Daly,M.J., Altshuler,D.M.
            and Friedman,J.M.
  TITLE     Genome-wide association studies in an isolated founder population
            from the Pacific Island of Kosrae
  JOURNAL   PLoS Genet 5 (2), e1000365 (2009)
   PUBMED   19197348
REFERENCE   10 (residues 1 to 721)
  AUTHORS   Scott,M.P., Zappacosta,F., Kim,E.Y., Annan,R.S. and Miller,W.T.
  TITLE     Identification of novel SH3 domain ligands for the Src family
            kinase Hck. Wiskott-Aldrich syndrome protein (WASP),
            WASP-interacting protein (WIP), and ELMO1
  JOURNAL   J Biol Chem 277 (31), 28238-28246 (2002)
   PUBMED   12029088
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB292134.1, AK025598.1, CX756689.1 and BC035698.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.15389.1,
                                           SRR1803612.10856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267750 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295148.9/ ENSP00000295148.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..721
                     /product="WD repeat and coiled-coil-containing protein
                     isoform 1"
                     /note="WD repeat-containing protein C2orf44; WD repeat and
                     coiled-coil-containing protein C2orf44"
                     /calculated_mol_wt=79005
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Region          2..672
                     /region_name="WDCP"
                     /note="WD repeat and coiled-coil-containing protein
                     family; pfam15390"
                     /db_xref="CDD:464697"
     Region          55..98
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Region          154..194
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Region          520..553
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Region          539..545
                     /region_name="Interaction with HCK.
                     /evidence=ECO:0000269|PubMed:25469238"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H6R7.1)"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H6R7.1)"
     CDS             1..721
                     /gene="WDCP"
                     /gene_synonym="C2orf44; MMAP; PP384"
                     /coded_by="NM_025203.3:97..2262"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1705.1"
                     /db_xref="GeneID:80304"
                     /db_xref="HGNC:HGNC:26157"
                     /db_xref="MIM:616234"
ORIGIN      
        1 melgkgkllr tglnalhqav hpihglawtd gnqvvltdlr lhsgevkfgd skvigqfecv
       61 cglswappva ddtpvllavq hekhvtvwql cpspmesskw ltsqtceirg slpilpqgcv
      121 whpkcailtv ltaqdvsifp nvhsddsqvk adintqgrih cacwtqdglr lvvavgsslh
      181 syiwdsaqkt lhrcssclvf dvdshvcsit atvdsqvaia telpldkicg lnasetfnip
      241 pnskdmtpya lpvigevrsm dkeatdsetn sevsvsssyl epldlthihf nqhksegnsl
      301 iclrkkdylt gtgqdsshlv lvtfkkavtm trkvtipgil vpdliafnlk ahvvavasnt
      361 cniiliysvi pssvpniqqi rlenterpkg icfltdqlll ilvgkqkltd ttflpssksd
      421 qyaislivre imleeepsit sgesqttyst fsaplnkanr kklieslspd fchqnkglll
      481 tvntssqngr pgrtlikeiq splssicdgs ialdaepvtq paslprhsst pdhtstlepp
      541 rlpqrknlqs eketyqlske veilsrnlve mqrclseltn rlhngkksss vyplsqdlpy
      601 vhiiyqkpyy lgpvvekrav llcdgklrls tvqqtfglsl iemlhdshwi llsadsegfi
      661 pltftatqei iirdgslsrs dvfrdsfshs pgavsslkvf tglaapsldt tgccnhvdgm
      721 a
//
LOCUS       NP_001139433            1079 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 12 member 4 isoform b [Homo sapiens].
ACCESSION   NP_001139433
VERSION     NP_001139433.1
DBSOURCE    REFSEQ: accession NM_001145961.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Zhao,Y., Shen,J., Wang,Q., Ruiz Munevar,M.J., Vidossich,P., De
            Vivo,M., Zhou,M. and Cao,E.
  TITLE     Structure of the human cation-chloride cotransport KCC1 in an
            outward-open state
  JOURNAL   Proc Natl Acad Sci U S A 119 (27), e2109083119 (2022)
   PUBMED   35759661
  REMARK    GeneRIF: Structure of the human cation-chloride cotransport KCC1 in
            an outward-open state.
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Chi,G., Ebenhoch,R., Man,H., Tang,H., Tremblay,L.E., Reggiano,G.,
            Qiu,X., Bohstedt,T., Liko,I., Almeida,F.G., Garneau,A.P., Wang,D.,
            McKinley,G., Moreau,C.P., Bountra,K.D., Abrusci,P.,
            Mukhopadhyay,S.M.M., Fernandez-Cid,A., Slimani,S., Lavoie,J.L.,
            Burgess-Brown,N.A., Tehan,B., DiMaio,F., Jazayeri,A., Isenring,P.,
            Robinson,C.V. and Durr,K.L.
  TITLE     Phospho-regulation, nucleotide binding and ion access control in
            potassium-chloride cotransporters
  JOURNAL   EMBO J 40 (14), e107294 (2021)
   PUBMED   34031912
REFERENCE   4  (residues 1 to 1079)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 1079)
  AUTHORS   Zhou,G.P., Wong,C., Su,R., Crable,S.C., Anderson,K.P. and
            Gallagher,P.G.
  TITLE     Human potassium chloride cotransporter 1 (SLC12A4) promoter is
            regulated by AP-2 and contains a functional downstream promoter
            element
  JOURNAL   Blood 103 (11), 4302-4309 (2004)
   PUBMED   14976052
  REMARK    GeneRIF: the KCC1 gene promoter lacks a TATA box and is composed of
            an initiator element (InR) and a downstream promoter element (DPE)
REFERENCE   6  (residues 1 to 1079)
  AUTHORS   Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
            Chernova,M.N., Brugnara,C. and Alper,S.L.
  TITLE     A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
            and C-terminal cytoplasmic domains are required for K-Cl
            cotransport activity
  JOURNAL   J Biol Chem 276 (45), 41870-41878 (2001)
   PUBMED   11551954
REFERENCE   7  (residues 1 to 1079)
  AUTHORS   Su,W., Shmukler,B.E., Chernova,M.N., Stuart-Tilley,A.K., de
            Franceschi,L., Brugnara,C. and Alper,S.L.
  TITLE     Mouse K-Cl cotransporter KCC1: cloning, mapping, pathological
            expression, and functional regulation
  JOURNAL   Am J Physiol 277 (5), C899-C912 (1999)
   PUBMED   10564083
REFERENCE   8  (residues 1 to 1079)
  AUTHORS   Pellegrino,C.M., Rybicki,A.C., Musto,S., Nagel,R.L. and
            Schwartz,R.S.
  TITLE     Molecular identification and expression of erythroid K:Cl
            cotransporter in human and mouse erythroleukemic cells
  JOURNAL   Blood Cells Mol Dis 24 (1), 31-40 (1998)
   PUBMED   9516379
REFERENCE   9  (residues 1 to 1079)
  AUTHORS   Gillen,C.M., Brill,S., Payne,J.A. and Forbush,B. 3rd.
  TITLE     Molecular cloning and functional expression of the K-Cl
            cotransporter from rabbit, rat, and human. A new member of the
            cation-chloride cotransporter family
  JOURNAL   J Biol Chem 271 (27), 16237-16244 (1996)
   PUBMED   8663127
REFERENCE   10 (residues 1 to 1079)
  AUTHORS   Larsen,F., Solheim,J., Kristensen,T., Kolsto,A.B. and Prydz,H.
  TITLE     A tight cluster of five unrelated human genes on chromosome 16q22.1
  JOURNAL   Hum Mol Genet 2 (10), 1589-1595 (1993)
   PUBMED   8268911
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC321966.1, AK293906.1,
            BC021193.2, CF272417.1, AK310027.1 and AI368074.1.
            
            Summary: This gene encodes a member of the SLC12A transporter
            family. The encoded protein mediates the coupled movement of
            potassium and chloride ions across the plasma membrane. This gene
            is expressed ubiquitously. Multiple alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. This
            results in a shorter protein (isoform b) compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293906.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..1079
                     /product="solute carrier family 12 member 4 isoform b"
                     /note="potassium/chloride cotransporter 1; erythroid K-Cl
                     cotransporter 1; solute carrier family 12
                     (potassium/chloride transporter), member 4; solute carrier
                     family 12 (potassium/chloride transporters), member 4;
                     electroneutral potassium-chloride cotransporter 1"
                     /calculated_mol_wt=119833
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Region          42..1079
                     /region_name="2a30"
                     /note="K-Cl cotransporter; TIGR00930"
                     /db_xref="CDD:273347"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIS8; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9UHW9; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:34031912,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            120..141
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            150..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            197..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            245
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            249..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            272..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            312
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31649201,
                     ECO:0007744|PDB:6KKR, ECO:0007744|PDB:6KKT,
                     ECO:0007744|PDB:6KKU; propagated from UniProtKB/Swiss-Prot
                     (Q9UP95.2)"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            361
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:31649201; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            420..440
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            451..473
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            505..531
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            555..575
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            576..598
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            613..635
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            636..651
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Region          665..681
                     /region_name="Scissor helix.
                     /evidence=ECO:0000269|PubMed:34031912,
                     ECO:0000269|PubMed:35759661, ECO:0007744|PDB:7AIP,
                     ECO:0007744|PDB:7AIQ, ECO:0007744|PDB:7AIR,
                     ECO:0007744|PDB:7TTH"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            734
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:34031912; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            910
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:34031912; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            961
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     Site            1044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:34031912; propagated from
                     UniProtKB/Swiss-Prot (Q9UP95.2)"
     CDS             1..1079
                     /gene="SLC12A4"
                     /gene_synonym="CTC-479C5.17; hKCC1; KCC1"
                     /coded_by="NM_001145961.2:85..3324"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:6560"
                     /db_xref="HGNC:HGNC:10913"
                     /db_xref="MIM:604119"
ORIGIN      
        1 mphftvvpvd gprrgdydnl eglswvdyge raelddsdgh gnhresspfl spleasrgid
       61 yydrnlalfe eeldirpkvs sllgklvsyt nltqgakehe eaesgegtrr raaeapsmgt
      121 lmgvylpclq nifgvilflr ltwmvgtagv lqallivlic ccctlltais msaiatngvv
      181 paggsyfmis rslgpefgga vglcfylgtt faaamyilga ieilltyiap paaifypsga
      241 hdtsnatlnn mrvygtiflt fmtlvvfvgv kyvnkfaslf lacviisils iyaggiksif
      301 dppvfpvcml gnrtlsrdqf dicaktavvd netvatqlws ffchspnltt dscdpyfmln
      361 nvteipgipg aaagvlqenl wsaylekgdi vekhglpsad apslkeslpl yvvadiatsf
      421 tvlvgiffps vtgimagsnr sgdlrdaqks ipvgtilaii ttslvyfssv vlfgaciegv
      481 vlrdkygdgv srnlvvgtla wpspwvivig sffstcgagl qsltgaprll qaiakdniip
      541 flrvfghgkv ngeptwalll taliaelgil iasldmvapi lsmfflmcyl fvnlacavqt
      601 llrtpnwrpr fkyyhwalsf lgmslclalm fvsswyyalv amliagmiyk yieyqgaeke
      661 wgdgirglsl saaryallrl eegpphtknw rpqllvllkl dedlhvkypr lltfasqlka
      721 gkgltivgsv iqgsflesyg eaqaaeqtik nmmeiekvkg fcqvvvaskv reglahliqs
      781 cglggmrhns vvlgwpygwr qsedprawkt fidtvrctta ahlallvpkn iafypsnher
      841 yleghidvww ivhdggmlml lpfllrqhkv wrkcrmrift vaqmddnsiq mkkdlavfly
      901 hlrleaehns disaytyert lmmeqrsqml rqmrltkter ereaqlvkdr hsalrlesly
      961 sdeedesavg adkiqmtwtr dkymtetwdp shapdnfrel vhikpdqsnv rrmhtavkln
     1021 evivtrshda rlvllnmpgp prnsegdeny meflevlteg lervllvrgg grevitiys
//
LOCUS       NP_001356373             377 aa            linear   PRI 20-NOV-2025
DEFINITION  NIF3-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001356373 XP_011509884
VERSION     NP_001356373.1
DBSOURCE    REFSEQ: accession NM_001369444.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Reed,C.J., Hutinet,G. and de Crecy-Lagard,V.
  TITLE     Comparative Genomic Analysis of the DUF34 Protein Family Suggests
            Role as a Metal Ion Chaperone or Insertase
  JOURNAL   Biomolecules 11 (9), 1282 (2021)
   PUBMED   34572495
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Merla,G., Howald,C., Antonarakis,S.E. and Reymond,A.
  TITLE     The subcellular localization of the ChoRE-binding protein, encoded
            by the Williams-Beuren syndrome critical region gene 14, is
            regulated by 14-3-3
  JOURNAL   Hum Mol Genet 13 (14), 1505-1514 (2004)
   PUBMED   15163635
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Tascou,S., Kang,T.W., Trappe,R., Engel,W. and Burfeind,P.
  TITLE     Identification and characterization of NIF3L1 BP1, a novel
            cytoplasmic interaction partner of the NIF3L1 protein
  JOURNAL   Biochem Biophys Res Commun 309 (2), 440-448 (2003)
   PUBMED   12951069
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Akiyama,H., Fujisawa,N., Tashiro,Y., Takanabe,N., Sugiyama,A. and
            Tashiro,F.
  TITLE     The role of transcriptional corepressor Nif3l1 in early stage of
            neural differentiation via cooperation with Trip15/CSN2
  JOURNAL   J Biol Chem 278 (12), 10752-10762 (2003)
   PUBMED   12522100
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Hadano,S., Yanagisawa,Y., Skaug,J., Fichter,K., Nasir,J.,
            Martindale,D., Koop,B.F., Scherer,S.W., Nicholson,D.W.,
            Rouleau,G.A., Ikeda,J. and Hayden,M.R.
  TITLE     Cloning and characterization of three novel genes, ALS2CR1,
            ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis
            (ALS2) critical region at chromosome 2q33-q34: candidate genes for
            ALS2
  JOURNAL   Genomics 71 (2), 200-213 (2001)
   PUBMED   11161814
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Tascou,S., Uedelhoven,J., Dixkens,C., Nayernia,K., Engel,W. and
            Burfeind,P.
  TITLE     Isolation and characterization of a novel human gene, NIF3L1, and
            its mouse ortholog, Nif3l1, highly conserved from bacteria to
            mammals
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 330-336 (2000)
   PUBMED   11124544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005037.2.
            
            On Apr 9, 2019 this sequence version replaced XP_011509884.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.272873.1,
                                           SRR3476690.854103.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..377
                     /product="NIF3-like protein 1 isoform 1"
                     /EC_number="3.5.4.16"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 1; NIF3 (Ngg1 interacting
                     factor 3, S.pombe homolog)-like 1; NIF3-like protein 1;
                     NIF3 NGG1 interacting factor 3-like 1; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 1 protein;
                     GTP cyclohydrolase I; putative GTP cyclohydrolase 1 type 2
                     NIF3L1"
                     /calculated_mol_wt=41837
     Region          33..354
                     /region_name="NIF3"
                     /note="NIF3 (NGG1p interacting factor 3); pfam01784"
                     /db_xref="CDD:426431"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Region          244..377
                     /region_name="Mediates interaction with COPS2.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     CDS             1..377
                     /gene="NIF3L1"
                     /gene_synonym="ALS2CR1; CALS-7; MDS015"
                     /coded_by="NM_001369444.1:274..1407"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS46485.1"
                     /db_xref="GeneID:60491"
                     /db_xref="HGNC:HGNC:13390"
                     /db_xref="MIM:605778"
ORIGIN      
        1 mlsscvrpvp ttvrfvdsli cnssrsfmdl kallsslndf aslsfaeswd nvgllvepsp
       61 phtvntlflt ndlteevmee vlqkkadlil syhppifrpm kritwntwke rlviralenr
      121 vgiysphtay daapqgvnnw lakglgacts rpihpskapn yptegnhrve fnvnytqdld
      181 kvmsavkgid gvsvtsfsar tgneeqtrin lnctqkalmq vvdflsrnkq lyqkteilsl
      241 ekplllhtgm grlctldesv slatmidrik rhlklshirl algvgrtles qvkvvalcag
      301 sgssvlqgve adlyltgems hhdtldaasq ginvilcehs ntergflsdl rdmldshlen
      361 kiniilsetd rdplqvv
//
LOCUS       NP_003802                254 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor ligand superfamily member 9 [Homo sapiens].
ACCESSION   NP_003802
VERSION     NP_003802.1
DBSOURCE    REFSEQ: accession NM_003811.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Li,Z., Gao,T., Wang,J., Zhang,X., Zhang,Y., Zhang,L., Yang,P. and
            Liu,J.
  TITLE     Ferroptosis mediated by TNFSF9 interferes in acute ischaemic stroke
            reperfusion injury with the progression of acute ischaemic stroke
  JOURNAL   J Neurochem 168 (6), 1030-1044 (2024)
   PUBMED   38344886
  REMARK    GeneRIF: Ferroptosis mediated by TNFSF9 interferes in acute
            ischaemic stroke reperfusion injury with the progression of acute
            ischaemic stroke.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Wu,J. and Wang,Y.
  TITLE     Role of TNFSF9 bidirectional signal transduction in antitumor
            immunotherapy
  JOURNAL   Eur J Pharmacol 928, 175097 (2022)
   PUBMED   35714694
  REMARK    GeneRIF: Role of TNFSF9 bidirectional signal transduction in
            antitumor immunotherapy.
            Review article
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Nielsen,M.A., Juul-Madsen,K., Stegmayr,J., Gao,C., Mehta,A.Y.,
            Greisen,S.R., Kragstrup,T.W., Hvid,M., Vorup-Jensen,T.,
            Cummings,R.D., Leffler,H. and Deleuran,B.W.
  TITLE     Galectin-3 Decreases 4-1BBL Bioactivity by Crosslinking Soluble and
            Membrane Expressed 4-1BB
  JOURNAL   Front Immunol 13, 915890 (2022)
   PUBMED   35812455
  REMARK    GeneRIF: Galectin-3 Decreases 4-1BBL Bioactivity by Crosslinking
            Soluble and Membrane Expressed 4-1BB.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Saoulli,K., Lee,S.Y., Cannons,J.L., Yeh,W.C., Santana,A.,
            Goldstein,M.D., Bangia,N., DeBenedette,M.A., Mak,T.W., Choi,Y. and
            Watts,T.H.
  TITLE     CD28-independent, TRAF2-dependent costimulation of resting T cells
            by 4-1BB ligand
  JOURNAL   J Exp Med 187 (11), 1849-1862 (1998)
   PUBMED   9607925
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Arch,R.H. and Thompson,C.B.
  TITLE     4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve
            growth factor receptor subfamily that bind TNF receptor-associated
            factors and activate nuclear factor kappaB
  JOURNAL   Mol Cell Biol 18 (1), 558-565 (1998)
   PUBMED   9418902
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Loo,D.T., Chalupny,N.J., Bajorath,J., Shuford,W.W., Mittler,R.S.
            and Aruffo,A.
  TITLE     Analysis of 4-1BBL and laminin binding to murine 4-1BB, a member of
            the tumor necrosis factor receptor superfamily, and comparison with
            human 4-1BB
  JOURNAL   J Biol Chem 272 (10), 6448-6456 (1997)
   PUBMED   9045669
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Alderson,M.R., Smith,C.A., Tough,T.W., Davis-Smith,T.,
            Armitage,R.J., Falk,B., Roux,E., Baker,E., Sutherland,G.R. and
            Din,W.S.
  TITLE     Molecular and biological characterization of human 4-1BB and its
            ligand
  JOURNAL   Eur J Immunol 24 (9), 2219-2227 (1994)
   PUBMED   8088337
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Goodwin,R.G., Din,W.S., Davis-Smith,T., Anderson,D.M., Gimpel,S.D.,
            Sato,T.A., Maliszewski,C.R., Brannan,C.I., Copeland,N.G.,
            Jenkins,N.A. et al.
  TITLE     Molecular cloning of a ligand for the inducible T cell gene 4-1BB:
            a member of an emerging family of cytokines with homology to tumor
            necrosis factor
  JOURNAL   Eur J Immunol 23 (10), 2631-2641 (1993)
   PUBMED   8405064
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010503.8 and BX107825.1.
            
            Summary: The protein encoded by this gene is a cytokine that
            belongs to the tumor necrosis factor (TNF) ligand family. This
            transmembrane cytokine is a bidirectional signal transducer that
            acts as a ligand for TNFRSF9/4-1BB, which is a costimulatory
            receptor molecule in T lymphocytes. This cytokine and its receptor
            are involved in the antigen presentation process and in the
            generation of cytotoxic T cells. The receptor TNFRSF9/4-1BB is
            absent from resting T lymphocytes but rapidly expressed upon
            antigenic stimulation. The ligand encoded by this gene,
            TNFSF9/4-1BBL, has been shown to reactivate anergic T lymphocytes
            in addition to promoting T lymphocyte proliferation. This cytokine
            has also been shown to be required for the optimal CD8 responses in
            CD8 T cells. This cytokine is expressed in carcinoma cell lines,
            and is thought to be involved in T cell-tumor cell
            interaction.[provided by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.187091.1, U03398.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245817.5/ ENSP00000245817.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..254
                     /product="tumor necrosis factor ligand superfamily member
                     9"
                     /note="receptor 4-1BB ligand; tumor necrosis factor
                     superfamily member 9; homolog of mouse 4-1BB-L; 4-1BBL;
                     tumor necrosis factor (ligand) superfamily, member 9;
                     tumor necrosis factor ligand 5A; CD137 ligand"
                     /calculated_mol_wt=26494
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P41273.1)"
     Site            order(94,142,144,199,204,234,238)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:238108"
     Region          107..240
                     /region_name="TNF"
                     /note="Tumour necrosis factor family; smart00207"
                     /db_xref="CDD:214557"
     Site            order(110..111,116,162,169,176)
                     /site_type="active"
                     /note="receptor binding sites [active]"
                     /db_xref="CDD:238108"
     CDS             1..254
                     /gene="TNFSF9"
                     /gene_synonym="4-1BB-L; CD137L; TNLG5A"
                     /coded_by="NM_003811.4:12..776"
                     /db_xref="CCDS:CCDS12169.1"
                     /db_xref="GeneID:8744"
                     /db_xref="HGNC:HGNC:11939"
                     /db_xref="MIM:606182"
ORIGIN      
        1 meyasdasld peapwppapr aracrvlpwa lvagllllll laaacavfla cpwavsgara
       61 spgsaasprl regpelspdd paglldlrqg mfaqlvaqnv llidgplswy sdpglagvsl
      121 tgglsykedt kelvvakagv yyvffqlelr rvvagegsgs vslalhlqpl rsaagaaala
      181 ltvdlppass earnsafgfq grllhlsagq rlgvhlhtea rarhawqltq gatvlglfrv
      241 tpeipaglps prse
//
LOCUS       NP_612401                707 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3KBP1-binding protein 1 [Homo sapiens].
ACCESSION   NP_612401
VERSION     NP_612401.2
DBSOURCE    REFSEQ: accession NM_138392.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Feng,L., Wang,J.T., Jin,H., Qian,K. and Geng,J.G.
  TITLE     SH3KBP1-binding protein 1 prevents epidermal growth factor receptor
            degradation by the interruption of c-Cbl-CIN85 complex
  JOURNAL   Cell Biochem Funct 29 (7), 589-596 (2011)
   PUBMED   21830225
  REMARK    GeneRIF: SHKBP1 disturbed the translocation of CIN85 to
            EGFR-containing vesicles.
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Liu,J.P., Liu,N.S., Yuan,H.Y., Guo,Q., Lu,H. and Li,Y.Y.
  TITLE     Human homologue of SETA binding protein 1 interacts with cathepsin
            B and participates in TNF-Induced apoptosis in ovarian cancer cells
  JOURNAL   Mol Cell Biochem 292 (1-2), 189-195 (2006)
   PUBMED   16733801
  REMARK    GeneRIF: hSB1 may function as a regulator of cathepsin B-mediated
            apoptosis.
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Borinstein,S.C., Hyatt,M.A., Sykes,V.W., Straub,R.E., Lipkowitz,S.,
            Boulter,J. and Bogler,O.
  TITLE     SETA is a multifunctional adapter protein with three SH3 domains
            that binds Grb2, Cbl, and the novel SB1 proteins
  JOURNAL   Cell Signal 12 (11-12), 769-779 (2000)
   PUBMED   11152963
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB038927.1, AF258553.1 and BC007653.1.
            
            On Feb 9, 2009 this sequence version replaced NP_612401.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF258553.1, SRR1803611.185584.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291842.10/ ENSP00000291842.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..707
                     /product="SH3KBP1-binding protein 1"
                     /note="SETA-binding protein 1"
                     /calculated_mol_wt=76213
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          18..120
                     /region_name="BTB_POZ_SHKBP1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in SH3KBP1-binding
                     protein 1 (SHKBP1); cd18393"
                     /db_xref="CDD:349701"
     Region          145..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          185..225
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          226..278
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          279..318
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          319..362
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          363..420
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          421..466
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          467..518
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          519..577
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          621..626
                     /region_name="PXXXPR. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          628..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Region          681..686
                     /region_name="PXXXPW. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBC3.2)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBC3.2)"
     CDS             1..707
                     /gene="SHKBP1"
                     /gene_synonym="PP203; Sb1"
                     /coded_by="NM_138392.4:28..2151"
                     /db_xref="CCDS:CCDS12560.1"
                     /db_xref="GeneID:92799"
                     /db_xref="HGNC:HGNC:19214"
                     /db_xref="MIM:617322"
ORIGIN      
        1 maaaataaeg vpsrgppgev ihlnvggkrf stsrqtltwi pdsffsslls gristlkdet
       61 gaifidrdpt vfapilnflr tkeldprgvh gssllheaqf ygltplvrrl qlreeldrss
      121 cgnvlfngyl pppvfpvkrr nrhslvgpqq lggrpapvrr sntmppnlgn agllgrmlde
      181 ktppspsgqp eepgmvrlvc ghhnwiavay tqflvcyrlk easgwqlvfs sprldwpier
      241 laltarvhgg algehdkmva aatgseillw alqaegggse igvfhlgvpv ealffvgnql
      301 iatshtgrig vwnavtkhwq vqevqpitsy daagsflllg cnngsiyyvd vqkfplrmkd
      361 ndllvselyr dpaedgvtal svyltpktsd sgnwieiayg tssggvrviv qhpetvgsgp
      421 qlfqtftvhr spvtkimlse khlisvcadn nhvrtwsvtr frgmistqpg stplasfkil
      481 alesadghgg csagndigpy gerddqqvfi qkvvpsasql fvrlsstgqr vcsvrsvdgs
      541 pttaftvlec egsrrlgsrp rrylltgqan gslamwdltt amdglgqapa gglteqelme
      601 qlehcelapp apsapswgcl pspsprislt slhsassnts lsghrgspsp pqaearrrgg
      661 gsfvercqel vrsgpdlrrp ptpapwpssg lgtpltppkm klnetsf
//
LOCUS       NP_075565                231 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome c oxidase assembly factor 7 [Homo sapiens].
ACCESSION   NP_075565
VERSION     NP_075565.2
DBSOURCE    REFSEQ: accession NM_023077.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 231)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 231)
  AUTHORS   Higuchi,Y., Ando,M., Kojima,F., Yuan,J., Hashiguchi,A.,
            Yoshimura,A., Hiramatsu,Y., Nozuma,S., Fukumura,S., Yahikozawa,H.,
            Abe,E., Toyoshima,I., Sugawara,M., Okamoto,Y., Matsuura,E. and
            Takashima,H.
  TITLE     Dystonia and Parkinsonism in COA7-related disorders: expanding the
            phenotypic spectrum
  JOURNAL   J Neurol 271 (1), 419-430 (2024)
   PUBMED   37750949
  REMARK    GeneRIF: Dystonia and Parkinsonism in COA7-related disorders:
            expanding the phenotypic spectrum.
REFERENCE   3  (residues 1 to 231)
  AUTHORS   Formosa,L.E., Maghool,S., Sharpe,A.J., Reljic,B., Muellner-Wong,L.,
            Stroud,D.A., Ryan,M.T. and Maher,M.J.
  TITLE     Mitochondrial COA7 is a heme-binding protein with disulfide
            reductase activity, which acts in the early stages of complex IV
            assembly
  JOURNAL   Proc Natl Acad Sci U S A 119 (9) (2022)
   PUBMED   35210360
  REMARK    GeneRIF: Mitochondrial COA7 is a heme-binding protein with
            disulfide reductase activity, which acts in the early stages of
            complex IV assembly.
REFERENCE   4  (residues 1 to 231)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 231)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 231)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 231)
  AUTHORS   Mohanraj,K., Wasilewski,M., Beninca,C., Cysewski,D., Poznanski,J.,
            Sakowska,P., Bugajska,Z., Deckers,M., Dennerlein,S.,
            Fernandez-Vizarra,E., Rehling,P., Dadlez,M., Zeviani,M. and
            Chacinska,A.
  TITLE     Inhibition of proteasome rescues a pathogenic variant of
            respiratory chain assembly factor COA7
  JOURNAL   EMBO Mol Med 11 (5) (2019)
   PUBMED   30885959
  REMARK    GeneRIF: pathogenic mutant versions of COA7 are imported slower
            than the wild-type protein, and mislocalized proteins are degraded
            in the cytosol by the proteasome.
REFERENCE   8  (residues 1 to 231)
  AUTHORS   Higuchi,Y., Okunushi,R., Hara,T., Hashiguchi,A., Yuan,J.,
            Yoshimura,A., Murayama,K., Ohtake,A., Ando,M., Hiramatsu,Y.,
            Ishihara,S., Tanabe,H., Okamoto,Y., Matsuura,E., Ueda,T., Toda,T.,
            Yamashita,S., Yamada,K., Koide,T., Yaguchi,H., Mitsui,J.,
            Ishiura,H., Yoshimura,J., Doi,K., Morishita,S., Sato,K.,
            Nakagawa,M., Yamaguchi,M., Tsuji,S. and Takashima,H.
  TITLE     Mutations in COA7 cause spinocerebellar ataxia with axonal
            neuropathy
  JOURNAL   Brain 141 (6), 1622-1636 (2018)
   PUBMED   29718187
  REMARK    GeneRIF: The results of this study suggest that loss-of-function
            COA7 mutation is responsible for the phenotype of the presented
            patients, and this new entity of disease would be referred to as
            spinocerebellar ataxia with axonal neuropathy type 3.
REFERENCE   9  (residues 1 to 231)
  AUTHORS   Martinez Lyons,A., Ardissone,A., Reyes,A., Robinson,A.J.,
            Moroni,I., Ghezzi,D., Fernandez-Vizarra,E. and Zeviani,M.
  TITLE     COA7 (C1orf163/RESA1) mutations associated with mitochondrial
            leukoencephalopathy and cytochrome c oxidase deficiency
  JOURNAL   J Med Genet 53 (12), 846-849 (2016)
   PUBMED   27683825
  REMARK    GeneRIF: The first patient carrying pathogenic mutations of COA7,
            causative of isolated COX deficiency and progressive neurological
            impairment is reported. It is also shown that COA7 is a soluble
            protein localized to the matrix, rather than in the intermembrane
            space as previously suggested.
REFERENCE   10 (residues 1 to 231)
  AUTHORS   Kozjak-Pavlovic,V., Prell,F., Thiede,B., Gotz,M., Wosiek,D., Ott,C.
            and Rudel,T.
  TITLE     C1orf163/RESA1 is a novel mitochondrial intermembrane space protein
            connected to respiratory chain assembly
  JOURNAL   J Mol Biol 426 (4), 908-920 (2014)
   PUBMED   24333015
  REMARK    GeneRIF: C1orf163 is a novel factor important for the assembly of
            respiratory chain complexes in human mitochondria.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022501.1, BC015313.1 and AC099784.2.
            
            On Dec 30, 2009 this sequence version replaced NP_075565.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.7543.1,
                                           SRR1803616.55041.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371538.5/ ENSP00000360593.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..231
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..231
                     /product="cytochrome c oxidase assembly factor 7"
                     /note="hcp beta-lactamase-like protein C1orf163; sel1
                     repeat-containing protein 1; beta-lactamase hcp-like
                     protein; Sel1 repeat containing 1; respiratory chain
                     assembly 1; respiratory chain assembly factor 1;
                     epididymis secretory sperm binding protein; cytochrome c
                     oxidase assembly factor 7 (putative)"
                     /calculated_mol_wt=25578
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96BR5.2)"
     Region          <21..214
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          34..66
                     /region_name="Sel1-like 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BR5.2)"
     Region          50..80
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          68..104
                     /region_name="Sel1-like 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BR5.2)"
     Region          88..120
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          108..146
                     /region_name="Sel1-like 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BR5.2)"
     Region          130..159
                     /region_name="SLR repeat"
                     /note="SLR repeat [structural motif]"
                     /db_xref="CDD:276807"
     Region          147..183
                     /region_name="Sel1-like 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BR5.2)"
     Region          184..219
                     /region_name="Sel1-like 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BR5.2)"
     CDS             1..231
                     /gene="COA7"
                     /gene_synonym="C1orf163; RESA1; SCAN3; SELRC1"
                     /coded_by="NM_023077.3:22..717"
                     /db_xref="CCDS:CCDS570.1"
                     /db_xref="GeneID:65260"
                     /db_xref="HGNC:HGNC:25716"
                     /db_xref="MIM:615623"
ORIGIN      
        1 magmvdfqde eqvksflenm evecnyhcyh ekdpdgcyrl vdylegirkn fdeaakvlkf
       61 nceenqhsds cyklgayyvt gkggltqdlk aaarcflmac ekpgkksiaa chnvgllahd
      121 gqvnedgqpd lgkardyytr acdggytssc fnlsamflqg apgfpkdmdl ackysmkacd
      181 lghiwacana srmyklgdgv dkdeakaevl knraqqlhke qqkgvqpltf g
//
LOCUS       NP_683758                457 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-1 isoform b [Homo sapiens].
ACCESSION   NP_683758
VERSION     NP_683758.1
DBSOURCE    REFSEQ: accession NM_148955.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 457)
  AUTHORS   Garcia Delgado,L., Derome,A., Longpre,S., Giroux-Dansereau,M.,
            Basbous,G., Lavoie,C., Saucier,C. and Denault,J.B.
  TITLE     Spatiotemporal regulation of the hepatocyte growth factor receptor
            MET activity by sorting nexins 1/2 in HCT116 colorectal cancer
            cells
  JOURNAL   Biosci Rep 44 (6) (2024)
   PUBMED   38836326
  REMARK    GeneRIF: Spatiotemporal regulation of the hepatocyte growth factor
            receptor MET activity by sorting nexins 1/2 in HCT116 colorectal
            cancer cells.
REFERENCE   2  (residues 1 to 457)
  AUTHORS   Lopez-Robles,C., Scaramuzza,S., Astorga-Simon,E.N., Ishida,M.,
            Williamson,C.D., Banos-Mateos,S., Gil-Carton,D., Romero-Durana,M.,
            Vidaurrazaga,A., Fernandez-Recio,J., Rojas,A.L., Bonifacino,J.S.,
            Castano-Diez,D. and Hierro,A.
  TITLE     Architecture of the ESCPE-1 membrane coat
  JOURNAL   Nat Struct Mol Biol 30 (7), 958-969 (2023)
   PUBMED   37322239
REFERENCE   3  (residues 1 to 457)
  AUTHORS   Sugatha,J., Priya,A., Raj,P., Jaimon,E., Swaminathan,U., Jose,A.,
            Pucadyil,T.J. and Datta,S.
  TITLE     Insights into cargo sorting by SNX32 and its role in neurite
            outgrowth
  JOURNAL   Elife 12, e84396 (2023)
   PUBMED   37158588
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 457)
  AUTHORS   Carlton,J., Bujny,M., Peter,B.J., Oorschot,V.M., Rutherford,A.,
            Mellor,H., Klumperman,J., McMahon,H.T. and Cullen,P.J.
  TITLE     Sorting nexin-1 mediates tubular endosome-to-TGN transport through
            coincidence sensing of high- curvature membranes and
            3-phosphoinositides
  JOURNAL   Curr Biol 14 (20), 1791-1800 (2004)
   PUBMED   15498486
  REMARK    GeneRIF: SNX1 associates with a microdomain of the early endosome
            where it regulates tubular-based endosome-to-trans Golgi network
            retrieval of the cation-independent mannose-6-phosphate receptor.
REFERENCE   5  (residues 1 to 457)
  AUTHORS   Shank,B.B., Wiley,H.S. and Kurten,R.C.
  TITLE     Structural and functional characterization of the human gene for
            sorting nexin 1 (SNX1)
  JOURNAL   DNA Cell Biol 20 (5), 287-296 (2001)
   PUBMED   11410165
REFERENCE   6  (residues 1 to 457)
  AUTHORS   Kurten,R.C., Eddington,A.D., Chowdhury,P., Smith,R.D.,
            Davidson,A.D. and Shank,B.B.
  TITLE     Self-assembly and binding of a sorting nexin to sorting endosomes
  JOURNAL   J Cell Sci 114 (Pt 9), 1743-1756 (2001)
   PUBMED   11309204
REFERENCE   7  (residues 1 to 457)
  AUTHORS   Chin,L.S., Raynor,M.C., Wei,X., Chen,H.Q. and Li,L.
  TITLE     Hrs interacts with sorting nexin 1 and regulates degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 276 (10), 7069-7078 (2001)
   PUBMED   11110793
REFERENCE   8  (residues 1 to 457)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   9  (residues 1 to 457)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Barr,V.A., Haft,D.H. and
            Taylor,S.I.
  TITLE     Identification of a family of sorting nexin molecules and
            characterization of their association with receptors
  JOURNAL   Mol Cell Biol 18 (12), 7278-7287 (1998)
   PUBMED   9819414
REFERENCE   10 (residues 1 to 457)
  AUTHORS   Kurten,R.C., Cadena,D.L. and Gill,G.N.
  TITLE     Enhanced degradation of EGF receptors by a sorting nexin, SNX1
  JOURNAL   Science 272 (5264), 1008-1010 (1996)
   PUBMED   8638121
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455188.1, AF065484.1,
            AC100840.2 and BX108623.1.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This endosomal protein regulates the cell-surface
            expression of epidermal growth factor receptor. This protein also
            has a role in sorting protease-activated receptor-1 from early
            endosomes to lysosomes. This protein may form oligomeric complexes
            with family members. This gene results in three transcript variants
            encoding distinct isoforms. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame segment of
            the 5' coding region, compared to variant 1. It encodes a shorter
            isoform (b), also known as SNX1A, that is missing an internal
            segment compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.249750.1,
                                           SRR1803613.56466.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..457
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..457
                     /product="sorting nexin-1 isoform b"
                     /note="sorting nexin 1A"
                     /calculated_mol_wt=51682
     Region          11..90
                     /region_name="Sorting_nexin"
                     /note="Sorting nexin, N-terminal domain; pfam03700"
                     /db_xref="CDD:461016"
     Region          91..203
                     /region_name="PX_domain"
                     /note="The Phox Homology domain, a phosphoinositide
                     binding module; cl02563"
                     /db_xref="CDD:470617"
     Site            order(121..123,149..150,173)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:132768"
     Region          221..454
                     /region_name="BAR_SNX1"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 1; cd07665"
                     /db_xref="CDD:153349"
     Site            order(250,253..254,257..258,260..261,264,267..268,271,
                     278..279,281..282,285,288..289,292..293,309,414,417..418,
                     420..422,425,428..429,431..433,435..436,439..440,442..443,
                     446..447,449..450)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153349"
     CDS             1..457
                     /gene="SNX1"
                     /gene_synonym="HsT17379; VPS5"
                     /coded_by="NM_148955.4:33..1406"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32268.1"
                     /db_xref="GeneID:6642"
                     /db_xref="HGNC:HGNC:11172"
                     /db_xref="MIM:601272"
ORIGIN      
        1 masggggcsa serlpppfpg lepesegaag gsepeagdsd tegediftga avvskhqspk
       61 ittsllpinn gskengihee qdqepqdlfa gdgmnayvay kvttqtslpl frskqfavkr
      121 rfsdflglye klsekhsqng fivppppeks ligmtkvkvg kedsssaefl ekrraalery
      181 lqrivnhptm lqdpdvrefl ekeelpravg tqtlsgagll kmfnkatdav skmtikmnes
      241 diwfeeklqe veceeqrlrk lhavvetlvn hrkelalnta qfakslamlg ssedntalsr
      301 alsqlaevee kieqlhqeqa nndffllael lsdyirllai vraafdqrmk twqrwqdaqa
      361 tlqkkreaea rllwankpdk lqqakdeile wesrvtqyer dferistvvr kevirfekek
      421 skdfknhvik yletllysqq qlakyweafl peakais
//
LOCUS       NP_001278955             102 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor protein D53 isoform 5 [Homo sapiens].
ACCESSION   NP_001278955 XP_005267181
VERSION     NP_001278955.1
DBSOURCE    REFSEQ: accession NM_001292026.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Nourse,C.R., Mattei,M.G., Gunning,P. and Byrne,J.A.
  TITLE     Cloning of a third member of the D52 gene family indicates
            alternative coding sequence usage in D52-like transcripts
  JOURNAL   Biochim Biophys Acta 1443 (1-2), 155-168 (1998)
   PUBMED   9838088
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 102)
  AUTHORS   Byrne,J.A., Mattei,M.G., Basset,P. and Gunning,P.
  TITLE     Identification and in situ hybridization mapping of a mouse Tpd52l1
            (D53) orthologue to chromosome 10A4-B2
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 199-201 (1998)
   PUBMED   9730602
REFERENCE   9  (residues 1 to 102)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   10 (residues 1 to 102)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK124817.1, BP334548.1,
            U44429.1, AL121938.10 and AI222450.1.
            
            On May 16, 2014 this sequence version replaced XP_005267181.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contain coiled-coil domains and may form hetero- or homomers. The
            encoded protein is involved in cell proliferation and calcium
            signaling. It also interacts with the mitogen-activated protein
            kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates
            MAP3K5-induced apoptosis. Multiple alternatively spliced transcript
            variants have been observed. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and lacks two exons in the 3'
            coding region compared to variant 1. It initiates translation at a
            downstream start codon. The resulting isoform (5) has a shorter
            N-terminus and a distinct C-terminus, and is shorter than isoform
            1. Variants 5 and 8 encode the same isoform (5).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG677422.1, BP334548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..102
                     /product="tumor protein D53 isoform 5"
                     /note="tumor protein D53; tumor protein D52 like 1"
                     /calculated_mol_wt=11590
     Region          15..100
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..102
                     /gene="TPD52L1"
                     /gene_synonym="D53; TPD53"
                     /coded_by="NM_001292026.3:356..664"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS75514.1"
                     /db_xref="GeneID:7164"
                     /db_xref="HGNC:HGNC:12006"
                     /db_xref="MIM:604069"
ORIGIN      
        1 mlseeekeel kaelvqlede ittlrqvlsa kerhlveikq klgmnlmnel kqnfskswhd
       61 mqtttaykkt hetlshagqk ataafsnvgt aiskkfgdmr rk
//
LOCUS       NP_001243897             302 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial potassium channel isoform 2 [Homo sapiens].
ACCESSION   NP_001243897
VERSION     NP_001243897.1
DBSOURCE    REFSEQ: accession NM_001256968.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Paggio,A., Checchetto,V., Campo,A., Menabo,R., Di Marco,G., Di
            Lisa,F., Szabo,I., Rizzuto,R. and De Stefani,D.
  TITLE     Identification of an ATP-sensitive potassium channel in
            mitochondria
  JOURNAL   Nature 572 (7771), 609-613 (2019)
   PUBMED   31435016
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Wang,C. and Brennan,W.A. Jr.
  TITLE     Rat skeletal muscle, liver and brain have different fetal and adult
            forms of the glucose transporter
  JOURNAL   Biochim Biophys Acta 946 (1), 11-18 (1988)
   PUBMED   3145016
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK022498.1, AC134772.2 and BC011993.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            initiates translation at a downstream, in-frame start codon,
            compared to variant 1. Variants 3, 4, 5, 6 and 7 encode the same
            isoform (2), which has a shorter N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022498.1, SRR1163655.482570.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..302
                     /product="mitochondrial potassium channel isoform 2"
                     /note="coiled-coil domain-containing protein 51;
                     mitochondrial potassium channel"
                     /calculated_mol_wt=33526
     CDS             1..302
                     /gene="CCDC51"
                     /gene_synonym="MITOK"
                     /coded_by="NM_001256968.3:239..1147"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS58830.1"
                     /db_xref="GeneID:79714"
                     /db_xref="HGNC:HGNC:25714"
                     /db_xref="MIM:618585"
ORIGIN      
        1 mvarglvrea redlevhqak lkevrdrldr vsredsqyle latlehrmlq eekrlrtayl
       61 raedserekf slfsaavres hekertraer tknwsligsv lgaligvags tyvnrvrlqe
      121 lkallleaqk gpvslqeair eqassysrqq rdlhnlmvdl rglvhaagpg qdsgsqagsp
      181 ptrdrdvdvl saalkeqlsh srqvhscleg lreqldglek tcsqmagvvq lvksaahpgl
      241 vepadgamps flleqgsmil alsdteqrle aqvnrntiys tlvtcvtfva tlpvlymlfk
      301 as
//
LOCUS       NP_116037                163 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM167B [Homo sapiens].
ACCESSION   NP_116037
VERSION     NP_116037.2
DBSOURCE    REFSEQ: accession NM_032648.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG282224.1 and BC004269.1.
            
            On Jul 7, 2006 this sequence version replaced NP_116037.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004269.1, BU741530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373582.4/ ENSP00000362684.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..163
                     /product="protein FAM167B"
                     /note="disordered autoimmunity 2"
                     /calculated_mol_wt=18283
     Region          90..163
                     /region_name="FAM167"
                     /note="pfam11652"
                     /db_xref="CDD:463319"
     CDS             1..163
                     /gene="FAM167B"
                     /gene_synonym="C1orf90; DIORA-2"
                     /coded_by="NM_032648.3:201..692"
                     /db_xref="CCDS:CCDS358.2"
                     /db_xref="GeneID:84734"
                     /db_xref="HGNC:HGNC:28133"
ORIGIN      
        1 mslgllkfqa vgeedeedee gesldsvkal taklqlqtrr psylewtaqv qsqawrraqa
       61 kpgpggpgdi cgfdsmdsal ewlrrelrem qaqdrqlagq llrlraqlhr lkmdqachlh
      121 qelldeaele lelepgagla lapllrhlgl trmnisarrf tlc
//
LOCUS       NP_001295052             193 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 24 isoform 2 [Homo sapiens].
ACCESSION   NP_001295052 XP_005258399
VERSION     NP_001295052.1
DBSOURCE    REFSEQ: accession NM_001308123.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Meng,F., Ai,C., Yan,G. and Wang,G.
  TITLE     Tumor-suppressive zinc finger protein 24 (ZNF24) sensitizes
            colorectal cancer cells to 5-fluorouracil by inhibiting the Wnt
            pathway and activating the p53 signaling
  JOURNAL   Exp Cell Res 433 (1), 113796 (2023)
   PUBMED   37774763
  REMARK    GeneRIF: Tumor-suppressive zinc finger protein 24 (ZNF24)
            sensitizes colorectal cancer cells to 5-fluorouracil by inhibiting
            the Wnt pathway and activating the p53 signaling.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Liu,Y., Cheng,H., Cheng,C., Zheng,F., Zhao,Z., Chen,Q., Zeng,W.,
            Zhang,P., Huang,C., Jiang,W., Liu,X. and Liu,G.
  TITLE     ZNF191 alters DNA methylation and activates the PI3K-AKT pathway in
            hepatoma cells via transcriptional regulation of DNMT1
  JOURNAL   Cancer Med 11 (5), 1269-1280 (2022)
   PUBMED   35092191
  REMARK    GeneRIF: ZNF191 alters DNA methylation and activates the PI3K-AKT
            pathway in hepatoma cells via transcriptional regulation of DNMT1.
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Liu,Y., Wu,D., Cheng,H., Chen,L., Zhang,W., Zou,L., Gao,Q.,
            Zhao,Z., Chen,Q., Zeng,W., Zhang,Z., Jiang,W., Huang,C. and Liu,G.
  TITLE     Wnt8B, transcriptionally regulated by ZNF191, promotes cell
            proliferation of hepatocellular carcinoma via Wnt signaling
  JOURNAL   Cancer Sci 112 (2), 629-640 (2021)
   PUBMED   33197287
  REMARK    GeneRIF: Wnt8B, transcriptionally regulated by ZNF191, promotes
            cell proliferation of hepatocellular carcinoma via Wnt signaling.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Rousseau-Merck,M.F., Huebner,K., Berger,R. and Thiesen,H.J.
  TITLE     Chromosomal localization of two human zinc finger protein genes,
            ZNF24 (KOX17) and ZNF29 (KOX26), to 18q12 and 17p13-p12,
            respectively
  JOURNAL   Genomics 9 (1), 154-161 (1991)
   PUBMED   2004757
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG436261.1, AF542097.1, AC116447.10 and CA314100.1.
            
            On Apr 22, 2015 this sequence version replaced XP_005258399.1.
            
            Transcript Variant: This variant (2) differs in the 5' and 3'
            structures compared to variant 1. The encoded isoform (2) has a
            distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.400336.1, BG436261.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..193
                     /product="zinc finger protein 24 isoform 2"
                     /note="zinc finger protein 191; zinc finger protein 24
                     (KOX 17); zinc finger protein KOX17; retinoic acid
                     suppression protein A; zinc finger and SCAN
                     domain-containing protein 3"
                     /calculated_mol_wt=22251
     Region          48..160
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     CDS             1..193
                     /gene="ZNF24"
                     /gene_synonym="KOX17; RSG-A; Zfp191; ZNF191; ZSCAN3"
                     /coded_by="NM_001308123.2:135..716"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77175.1"
                     /db_xref="GeneID:7572"
                     /db_xref="HGNC:HGNC:13032"
                     /db_xref="MIM:194534"
ORIGIN      
        1 msaqsveeds iliiptpdee ekilrvklee dpdgeegssi pwnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailpkelqt wvrdhhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lvedmvsqee aqglpsseld avenqlkwas
      181 welhslrhcv iip
//
LOCUS       NP_001317951             270 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26C isoform 4 [Homo
            sapiens].
ACCESSION   NP_001317951 XP_005260966
VERSION     NP_001317951.1
DBSOURCE    REFSEQ: accession NM_001331022.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Koumandou,V.L., Klute,M.J., Herman,E.K., Nunez-Miguel,R.,
            Dacks,J.B. and Field,M.C.
  TITLE     Evolutionary reconstruction of the retromer complex and its
            function in Trypanosoma brucei
  JOURNAL   J Cell Sci 124 (Pt 9), 1496-1509 (2011)
   PUBMED   21502137
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Aubry,L., Guetta,D. and Klein,G.
  TITLE     The arrestin fold: variations on a theme
  JOURNAL   Curr Genomics 10 (2), 133-142 (2009)
   PUBMED   19794886
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Dahmane,N., Ghezala,G.A., Gosset,P., Chamoun,Z.,
            Dufresne-Zacharia,M.C., Lopes,C., Rabatel,N.,
            Gassanova-Maugenre,S., Chettouh,Z., Abramowski,V., Fayet,E.,
            Yaspo,M.L., Korn,B., Blouin,J.L., Lehrach,H., Poutska,A.,
            Antonarakis,S.E., Sinet,P.M., Creau,N. and Delabar,J.M.
  TITLE     Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21
            involved in Down syndrome
  JOURNAL   Genomics 48 (1), 12-23 (1998)
   PUBMED   9503011
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Nakamura,A., Hattori,M. and Sakaki,Y.
  TITLE     Isolation of a novel human gene from the Down syndrome critical
            region of chromosome 21q22.2
  JOURNAL   J Biochem 122 (4), 872-877 (1997)
   PUBMED   9399594
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001412.2, DB286372.1,
            DA311783.1, AK303624.1, AK300024.1, D87343.1 and BX648191.1.
            
            On Sep 3, 2016 this sequence version replaced XP_005260966.1.
            
            Summary: The region of chromosome 21 between genes CBR and ERG
            (CBR-ERG region), which spans 2.5 Mb on 21q22.2, has been defined
            by analysis of patients with partial trisomy 21. It contributes
            significantly to the pathogenesis of many characteristics of Down
            syndrome, including morphological features, hypotonia, and
            cognitive disability. The DSCR3 (Down syndrome critical region gene
            3) gene is found in this region and is predictated to contain eight
            exons. DSCR3 is expressed in most tissues examined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.8404.1,
                                           SRR1660809.148223.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..270
                     /product="vacuolar protein sorting-associated protein 26C
                     isoform 4"
                     /note="Down syndrome critical region protein A; Down
                     syndrome critical region protein 3; Down syndrome critical
                     region gene 3; Down syndrome critical region 3; DSCR3
                     arrestin fold containing; vacuolar protein
                     sorting-associated protein 26C"
                     /calculated_mol_wt=29754
     Region          1..256
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     cl22903"
                     /db_xref="CDD:451447"
     CDS             1..270
                     /gene="VPS26C"
                     /gene_synonym="DCRA; DSCR3; DSCRA"
                     /coded_by="NM_001331022.1:816..1628"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS82673.1"
                     /db_xref="GeneID:10311"
                     /db_xref="HGNC:HGNC:3044"
                     /db_xref="MIM:605298"
ORIGIN      
        1 mgtaldikik rankvyhage vlsgvvviss kdsvqhqgvs ltmegtvnlq lsaksvgvfe
       61 afynsvkpiq iinstiemvk pgkfpsgkte ipfefplhlk gnkvlyetyh gvfvniqpqk
      121 gkftpspvdf titpetlqnv kerallpkfl lrghlnstnc vitqpltgel vvesseaair
      181 svelqlvrve tcgcaegyar dateiqniqi adgdvcrgls vpiymvfprl ftcptlettn
      241 fkvefevniv vllhpdhlit enfplklcri
//
LOCUS       NP_001353146             883 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001353146
VERSION     NP_001353146.1
DBSOURCE    REFSEQ: accession NM_001366217.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 883)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.74132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..883
                     /product="disks large homolog 1 isoform 10"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=98183
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          692..870
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..883
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366217.1:624..3275"
                     /note="isoform 10 is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS93453.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 lilitdeygc skggqeeyvl syepvnqqev nytrpviilg pmkdrinddl isefpdkfgs
      721 cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt svqsvrevae
      781 kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar ktferamkle
      841 qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_001093161             159 aa            linear   PRI 20-NOV-2025
DEFINITION  protransforming growth factor alpha isoform 2 preproprotein [Homo
            sapiens].
ACCESSION   NP_001093161
VERSION     NP_001093161.1
DBSOURCE    REFSEQ: accession NM_001099691.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Ma,X., Zheng,J., He,K., Wang,L., Wang,Z., Wang,K., Liu,Z., San,Z.,
            Zhao,L. and Wang,L.
  TITLE     TGFA expression is associated with poor prognosis and promotes the
            development of cervical cancer
  JOURNAL   J Cell Mol Med 28 (3), e18086 (2024)
   PUBMED   38152044
  REMARK    GeneRIF: TGFA expression is associated with poor prognosis and
            promotes the development of cervical cancer.
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kamentseva,R.S., Kharchenko,M.V., Gabdrahmanova,G.V., Kotov,M.A.,
            Kosheverova,V.V. and Kornilova,E.S.
  TITLE     EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells
  JOURNAL   Int J Mol Sci 24 (17), 13408 (2023)
   PUBMED   37686213
  REMARK    GeneRIF: EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Sun,Y., Miao,X., Zhu,L., Liu,J., Lin,Y., Xiang,G., Wu,X., Wang,X.,
            Ni,Z. and Li,S.
  TITLE     Autocrine TGF-alpha is associated with Benzo(a)pyrene-induced mucus
            production and MUC5AC expression during allergic asthma
  JOURNAL   Ecotoxicol Environ Saf 241, 113833 (2022)
   PUBMED   36068759
  REMARK    GeneRIF: Autocrine TGF-alpha is associated with
            Benzo(a)pyrene-induced mucus production and MUC5AC expression
            during allergic asthma.
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Qian,J.F., Lazar-Wesley,E., Breugnot,C. and May,E.
  TITLE     Human transforming growth factor alpha: sequence analysis of the
            4.5-kb and 1.6-kb mRNA species
  JOURNAL   Gene 132 (2), 291-296 (1993)
   PUBMED   8224876
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Thomas,D.M., Nasim,M.M., Gullick,W.J. and Alison,M.R.
  TITLE     Immunoreactivity of transforming growth factor alpha in the normal
            adult gastrointestinal tract
  JOURNAL   Gut 33 (5), 628-631 (1992)
   PUBMED   1612477
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Nasim,M.M., Thomas,D.M., Alison,M.R. and Filipe,M.I.
  TITLE     Transforming growth factor alpha expression in normal gastric
            mucosa, intestinal metaplasia, dysplasia and gastric carcinoma--an
            immunohistochemical study
  JOURNAL   Histopathology 20 (4), 339-343 (1992)
   PUBMED   1577411
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Bean,M.F. and Carr,S.A.
  TITLE     Characterization of disulfide bond position in proteins and
            sequence analysis of cystine-bridged peptides by tandem mass
            spectrometry
  JOURNAL   Anal Biochem 201 (2), 216-226 (1992)
   PUBMED   1632509
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Tricoli,J.V., Nakai,H., Byers,M.G., Rall,L.B., Bell,G.I. and
            Shows,T.B.
  TITLE     The gene for human transforming growth factor alpha is on the short
            arm of chromosome 2
  JOURNAL   Cytogenet Cell Genet 42 (1-2), 94-98 (1986)
   PUBMED   3459638
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Derynck,R., Roberts,A.B., Winkler,M.E., Chen,E.Y. and Goeddel,D.V.
  TITLE     Human transforming growth factor-alpha: precursor structure and
            expression in E. coli
  JOURNAL   Cell 38 (1), 287-297 (1984)
   PUBMED   6088071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005308.1, CN274505.1,
            DA373586.1, BM453873.1, BI760767.1, X70340.1 and CD369689.1.
            
            Summary: This gene encodes a growth factor that is a ligand for the
            epidermal growth factor receptor, which activates a signaling
            pathway for cell proliferation, differentiation and development.
            This protein may act as either a transmembrane-bound ligand or a
            soluble ligand. This gene has been associated with many types of
            cancers, and it may also be involved in some cases of cleft
            lip/palate. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (2) is one amino acid shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.89353.1,
                                           SRR18074969.585494.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..159
                     /product="protransforming growth factor alpha isoform 2
                     preproprotein"
                     /note="protransforming growth factor alpha; TGF-alpha"
                     /calculated_mol_wt=14808
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2145
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01135.1)"
     mat_peptide     39..88
                     /product="Transforming growth factor alpha.
                     /id=PRO_0000007753"
                     /note="propagated from UniProtKB/Swiss-Prot (P01135.1)"
                     /calculated_mol_wt=5552
     Region          <43..82
                     /region_name="PHA02887"
                     /note="EGF-like protein; Provisional"
                     /db_xref="CDD:165214"
     Region          <46..120
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     Site            98..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01135.1)"
     CDS             1..159
                     /gene="TGFA"
                     /gene_synonym="TFGA"
                     /coded_by="NM_001099691.3:60..539"
                     /note="isoform 2 preproprotein is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS46316.1"
                     /db_xref="GeneID:7039"
                     /db_xref="HGNC:HGNC:11765"
                     /db_xref="MIM:190170"
ORIGIN      
        1 mvpsagqlal falgivlaac qalenstspl sdppvaaavv shfndcpdsh tqfcfhgtcr
       61 flvqedkpac vchsgyvgar cehadllavv aasqkkqait alvvvsival avliitcvli
      121 hccqvrkhce wcralicrhe kpsallkgrt acchsetvv
//
LOCUS       NP_056286                281 aa            linear   PRI 20-NOV-2025
DEFINITION  kinetochore-associated protein NSL1 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_056286
VERSION     NP_056286.3
DBSOURCE    REFSEQ: accession NM_015471.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Kiyomitsu,T., Iwasaki,O., Obuse,C. and Yanagida,M.
  TITLE     Inner centromere formation requires hMis14, a trident kinetochore
            protein that specifically recruits HP1 to human chromosomes
  JOURNAL   J Cell Biol 188 (6), 791-807 (2010)
   PUBMED   20231385
  REMARK    GeneRIF: The hMis14, which contains a tripartite-binding domain for
            HP1 and two other kinetochore proteins, hMis13 and blinkin, is a
            cornerstone for the assembly of the inner centromere and
            kinetochore.
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Kiyomitsu,T., Obuse,C. and Yanagida,M.
  TITLE     Human Blinkin/AF15q14 is required for chromosome alignment and the
            mitotic checkpoint through direct interaction with Bub1 and BubR1
  JOURNAL   Dev Cell 13 (5), 663-676 (2007)
   PUBMED   17981135
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Kline,S.L., Cheeseman,I.M., Hori,T., Fukagawa,T. and Desai,A.
  TITLE     The human Mis12 complex is required for kinetochore assembly and
            proper chromosome segregation
  JOURNAL   J Cell Biol 173 (1), 9-17 (2006)
   PUBMED   16585270
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Obuse,C., Iwasaki,O., Kiyomitsu,T., Goshima,G., Toyoda,Y. and
            Yanagida,M.
  TITLE     A conserved Mis12 centromere complex is linked to heterochromatic
            HP1 and outer kinetochore protein Zwint-1
  JOURNAL   Nat Cell Biol 6 (11), 1135-1141 (2004)
   PUBMED   15502821
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Cheeseman,I.M., Niessen,S., Anderson,S., Hyndman,F., Yates,J.R.
            3rd, Oegema,K. and Desai,A.
  TITLE     A conserved protein network controls assembly of the outer
            kinetochore and its ability to sustain tension
  JOURNAL   Genes Dev 18 (18), 2255-2268 (2004)
   PUBMED   15371340
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223260.1, AL591647.14 and
            AA806390.1.
            
            On Jul 14, 2006 this sequence version replaced NP_056286.2.
            
            Summary: This gene encodes a protein with two coiled-coil domains
            that localizes to kinetochores, which are chromosome-associated
            structures that attach to microtubules and mediate chromosome
            movements during cell division. The encoded protein is part of a
            conserved protein complex that includes two chromodomain-containing
            proteins and a component of the outer plate of the kinetochore.
            This protein complex is proposed to bridge centromeric
            heterochromatin with the outer kinetochore structure. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. There is a pseudogene of the 3' UTR region of this gene
            on chromosome X. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2526052.1,
                                           SRR14038191.280817.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366977.8/ ENSP00000355944.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.3"
     Protein         1..281
                     /product="kinetochore-associated protein NSL1 homolog
                     isoform 1"
                     /note="kinetochore-associated protein NSL1 homolog; NSL1,
                     MIND kinetochore complex component, homolog; NSL1, MIS12
                     kinetochore complex component"
                     /calculated_mol_wt=32031
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96IY1.3)"
     Region          82..197
                     /region_name="Mis14"
                     /note="Kinetochore protein Mis14 like; pfam08641"
                     /db_xref="CDD:430124"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96IY1.3)"
     CDS             1..281
                     /gene="NSL1"
                     /gene_synonym="C1orf48; DC8; MIS14"
                     /coded_by="NM_015471.4:15..860"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1509.1"
                     /db_xref="GeneID:25936"
                     /db_xref="HGNC:HGNC:24548"
                     /db_xref="MIM:609174"
ORIGIN      
        1 magspelvvl dppwdkelaa gtesqalvsa tpredfrvrc tskravteml qlcgrfvqkl
       61 gdalpeeire palrdaqwtf esavqenisi ngqawqeasd ncfmdsdikv ledqfdeiiv
      121 diatkrkqyp rkilecvikt ikakqeilkq yhpvvhpldl kydpdpaphm enlkcrgetv
      181 akeiseamks lpalieqgeg fsqvlrmqpv ihlqrihqev fsschrkpda kpenfitqie
      241 ttptetasrk tsdmvlkrkq tkdcpqrkwy plrpkkinld t
//
LOCUS       NP_004163                542 aa            linear   PRI 20-NOV-2025
DEFINITION  excitatory amino acid transporter 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004163
VERSION     NP_004163.3
DBSOURCE    REFSEQ: accession NM_004172.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Albury,C.L., Sutherland,H.G., Lam,A.W.Y., Tran,N.K., Lea,R.A.,
            Haupt,L.M. and Griffiths,L.R.
  TITLE     Identification of Polymorphisms in EAAT1 Glutamate Transporter Gene
            SLC1A3 Associated with Reduced Migraine Risk
  JOURNAL   Genes (Basel) 15 (6), 797 (2024)
   PUBMED   38927733
  REMARK    GeneRIF: Identification of Polymorphisms in EAAT1 Glutamate
            Transporter Gene SLC1A3 Associated with Reduced Migraine Risk.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Welby,E. and Ebert,A.D.
  TITLE     Diminished motor neuron activity driven by abnormal astrocytic
            EAAT1 glutamate transporter activity in spinal muscular atrophy is
            not fully restored after lentiviral SMN delivery
  JOURNAL   Glia 71 (5), 1311-1332 (2023)
   PUBMED   36655314
  REMARK    GeneRIF: Diminished motor neuron activity driven by abnormal
            astrocytic EAAT1 glutamate transporter activity in spinal muscular
            atrophy is not fully restored after lentiviral SMN delivery.
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Pant,S., Wu,Q., Ryan,R. and Tajkhorshid,E.
  TITLE     Microscopic Characterization of the Chloride Permeation Pathway in
            the Human Excitatory Amino Acid Transporter 1 (EAAT1)
  JOURNAL   ACS Chem Neurosci 13 (6), 776-785 (2022)
   PUBMED   35192345
  REMARK    GeneRIF: Microscopic Characterization of the Chloride Permeation
            Pathway in the Human Excitatory Amino Acid Transporter 1 (EAAT1).
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Lee,A., Anderson,A.R., Beasley,S.J., Barnett,N.L., Poronnik,P. and
            Pow,D.V.
  TITLE     A new splice variant of the glutamate-aspartate transporter:
            cloning and immunolocalization of GLAST1c in rat, pig and human
            brains
  JOURNAL   J Chem Neuroanat 43 (1), 52-63 (2012)
   PUBMED   22026960
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Vallejo-Illarramendi,A., Domercq,M. and Matute,C.
  TITLE     A novel alternative splicing form of excitatory amino acid
            transporter 1 is a negative regulator of glutamate uptake
  JOURNAL   J Neurochem 95 (2), 341-348 (2005)
   PUBMED   16042756
  REMARK    GeneRIF: EAAT1ex9skip splice variant is a negative regulator of
            full-length EAAT1 function in the human brain
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Takai,S., Yamada,K., Kawakami,H., Tanaka,K. and Nakamura,S.
  TITLE     Localization of the gene (SLC1A3) encoding human glutamate
            transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 209-210 (1995)
   PUBMED   7698014
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC320625.1, D26443.1,
            BC037310.2, AK057823.1 and AF070609.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 12, 2008 this sequence version replaced NP_004163.2.
            
            Summary: This gene encodes a member of a member of a high affinity
            glutamate transporter family. This gene functions in the
            termination of excitatory neurotransmission in central nervous
            system. Mutations are associated with episodic ataxia, Type 6.
            Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (GLAST) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.84261.1,
                                           SRR1803611.74849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265113.9/ ENSP00000265113.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..542
                     /product="excitatory amino acid transporter 1 isoform 1"
                     /note="excitatory amino acid transporter 1; GLAST-1;
                     sodium-dependent glutamate/aspartate transporter 1; solute
                     carrier family 1 (glial high affinity glutamate
                     transporter), member 3"
                     /calculated_mol_wt=59441
     Region          46..496
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            48..68
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            87..108
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            123..145
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            237..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            270..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            386..412
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            473..494
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43003.1)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43003.1)"
     CDS             1..542
                     /gene="SLC1A3"
                     /gene_synonym="EA6; EAAT1; GLAST; GLAST1"
                     /coded_by="NM_004172.5:226..1854"
                     /note="isoform 1 is encoded by transcript variant GLAST"
                     /db_xref="CCDS:CCDS3919.1"
                     /db_xref="GeneID:6507"
                     /db_xref="HGNC:HGNC:10941"
                     /db_xref="MIM:600111"
ORIGIN      
        1 mtksngeepk mggrmerfqq gvrkrtllak kkvqnitked vksylfrnaf vlltvtaviv
       61 gtilgftlrp yrmsyrevky fsfpgellmr mlqmlvlpli isslvtgmaa ldskasgkmg
      121 mravvyymtt tiiavvigii iviiihpgkg tkenmhregk ivrvtaadaf ldlirnmfpp
      181 nlveacfkqf ktnyekrsfk vpiqanetlv gavinnvsea metltritee lvpvpgsvng
      241 vnalglvvfs mcfgfvignm keqgqalref fdslneaimr lvavimwyap vgilfliagk
      301 ivemedmgvi ggqlamytvt vivgllihav ivlpllyflv trknpwvfig gllqalital
      361 gtssssatlp itfkcleenn gvdkrvtrfv lpvgatinmd gtalyealaa ifiaqvnnfe
      421 lnfgqiitis itataasiga agipqaglvt mvivltsvgl ptdditliia vdwfldrlrt
      481 ttnvlgdslg agivehlsrh elknrdvemg nsvieenemk kpyqliaqdn etekpidset
      541 km
//
LOCUS       NP_054747                334 aa            linear   PRI 20-NOV-2025
DEFINITION  osteopetrosis-associated transmembrane protein 1 precursor [Homo
            sapiens].
ACCESSION   NP_054747
VERSION     NP_054747.2
DBSOURCE    REFSEQ: accession NM_014028.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Vacher,J.
  TITLE     OSTM1 pleiotropic roles from osteopetrosis to neurodegeneration
  JOURNAL   Bone 163, 116505 (2022)
   PUBMED   35902071
  REMARK    GeneRIF: OSTM1 pleiotropic roles from osteopetrosis to
            neurodegeneration.
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Zhang,S., Liu,Y., Zhang,B., Zhou,J., Li,T., Liu,Z., Li,Y. and
            Yang,M.
  TITLE     Molecular insights into the human CLC-7/Ostm1 transporter
  JOURNAL   Sci Adv 6 (33), eabb4747 (2020)
   PUBMED   32851177
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Maranda,B., Chabot,G., Decarie,J.C., Pata,M., Azeddine,B.,
            Moreau,A. and Vacher,J.
  TITLE     Clinical and cellular manifestations of OSTM1-related infantile
            osteopetrosis
  JOURNAL   J Bone Miner Res 23 (2), 296-300 (2008)
   PUBMED   17922613
  REMARK    GeneRIF: A novel mutation affecting the OSTM1 locus responsible for
            ARO. In addition to common clinical features of osteopetrosis, the
            patient developed a unique neuronal pathology that provided
            evidence for the role of OSTM1 in normal neuronal cell development.
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Castellano Chiodo,D., DiRocco,M., Gandolfo,C., Morana,G., Buzzi,D.
            and Rossi,A.
  TITLE     Neuroimaging findings in malignant infantile osteopetrosis due to
            OSTM1 mutations
  JOURNAL   Neuropediatrics 38 (3), 154-156 (2007)
   PUBMED   17985267
  REMARK    GeneRIF: This study reports on a 12-month-old female with recessive
            OSMT1 mutations and neuroimaging findings suggesting a malignant
            infantile osteopetrosis.
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Fischer,T., De Vries,L., Meerloo,T. and Farquhar,M.G.
  TITLE     Promotion of G alpha i3 subunit down-regulation by GIPN, a putative
            E3 ubiquitin ligase that interacts with RGS-GAIP
  JOURNAL   Proc Natl Acad Sci U S A 100 (14), 8270-8275 (2003)
   PUBMED   12826607
  REMARK    GeneRIF: The human GIPN gene has 6 exons and 5 introns, and encodes
            a 334-aa protein.
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Chalhoub,N., Benachenhou,N., Rajapurohitam,V., Pata,M., Ferron,M.,
            Frattini,A., Villa,A. and Vacher,J.
  TITLE     Grey-lethal mutation induces severe malignant autosomal recessive
            osteopetrosis in mouse and human
  JOURNAL   Nat Med 9 (4), 399-406 (2003)
   PUBMED   12627228
  REMARK    GeneRIF: mutation in the human GL gene leads to severe recessive
            osteopetrosis
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Abrahams,B.S., Mak,G.M., Berry,M.L., Palmquist,D.L., Saionz,J.R.,
            Tay,A., Tan,Y.H., Brenner,S., Simpson,E.M. and Venkatesh,B.
  TITLE     Novel vertebrate genes and putative regulatory elements identified
            at kidney disease and NR2E1/fierce loci
  JOURNAL   Genomics 80 (1), 45-53 (2002)
   PUBMED   12079282
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z98200.9, BI668275.1,
            AF533891.1, AJ420489.1, AA428166.1, BQ716123.1, BE218267.1 and
            AV715475.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 19, 2003 this sequence version replaced NP_054747.1.
            
            Summary: This gene encodes a protein that may be involved in the
            degradation of G proteins via the ubiquitin-dependent proteasome
            pathway. The encoded protein binds to members of subfamily A of the
            regulator of the G-protein signaling (RGS) family through an
            N-terminal leucine-rich region. This protein also has a central
            RING finger-like domain and E3 ubiquitin ligase activity. This
            protein is highly conserved from flies to humans. Defects in this
            gene may cause the autosomal recessive, infantile malignant form of
            osteopetrosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.2510513.1,
                                           SRR11853566.24425.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000193322.8/ ENSP00000193322.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..334
                     /product="osteopetrosis-associated transmembrane protein 1
                     precursor"
                     /note="grey-lethal osteopetrosis; GAIP-interacting protein
                     N terminus; chloride channel 7 beta subunit; CLCN7
                     accessory beta subunit; osteopetrosis associated
                     transmembrane protein 1"
                     /calculated_mol_wt=33973
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3302
     Region          84..328
                     /region_name="OSTMP1"
                     /note="Osteopetrosis-associated transmembrane protein 1
                     precursor; pfam09777"
                     /db_xref="CDD:430817"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            163
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            216
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            263
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            285..305
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q86WC4.1)"
     CDS             1..334
                     /gene="OSTM1"
                     /gene_synonym="GIPN; GL; HSPC019; OPTB5"
                     /coded_by="NM_014028.4:91..1095"
                     /db_xref="CCDS:CCDS5062.1"
                     /db_xref="GeneID:28962"
                     /db_xref="HGNC:HGNC:21652"
                     /db_xref="MIM:607649"
ORIGIN      
        1 mepgptaaqr rcslppwlpl glllwsglal galpfgssph rvfhdllseq qllevedlsl
       61 sllqggglgp lslppdlpdl dpecrellld fanssaeltg clvrsarpvr lcqtcyplfq
      121 qvvskmdnis raagntsesq scarsllmad rmqivvilse ffnttwqean cancltnnse
      181 elsnstvyfl nlfnhtltcf ehnlqgnahs llqtknysev ckncreaykt lsslysemqk
      241 mnelenkaep gthlcidved amnitrklws rtfncsvpcs dtvpviavsv filflpvvfy
      301 lssflhseqk krklilpkrl ksstsfaniq ensn
//
LOCUS       NP_001353869             239 aa            linear   PRI 20-NOV-2025
DEFINITION  protein prenyltransferase alpha subunit repeat-containing protein 1
            isoform 7 [Homo sapiens].
ACCESSION   NP_001353869 XP_005252038
VERSION     NP_001353869.1
DBSOURCE    REFSEQ: accession NM_001366940.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Shirakawa,R., Goto-Ito,S., Goto,K., Wakayama,S., Kubo,H.,
            Sakata,N., Trinh,D.A., Yamagata,A., Sato,Y., Masumoto,H., Cheng,J.,
            Fujimoto,T., Fukai,S. and Horiuchi,H.
  TITLE     A SNARE geranylgeranyltransferase essential for the organization of
            the Golgi apparatus
  JOURNAL   EMBO J 39 (8), e104120 (2020)
   PUBMED   32128853
  REMARK    GeneRIF: A SNARE geranylgeranyltransferase essential for the
            organization of the Golgi apparatus.
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Kuchay,S., Wang,H., Marzio,A., Jain,K., Homer,H., Fehrenbacher,N.,
            Philips,M.R., Zheng,N. and Pagano,M.
  TITLE     GGTase3 is a newly identified geranylgeranyltransferase targeting a
            ubiquitin ligase
  JOURNAL   Nat Struct Mol Biol 26 (7), 628-636 (2019)
   PUBMED   31209342
  REMARK    GeneRIF: This study reports the identification of a previously
            unknown human prenyltransferase complex consisting of an orphan
            prenyltransferase alpha subunit, PTAR1, and the catalytic
            beta-subunit of GGTase2, RabGGTB.
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL162412.11.
            
            On Oct 26, 2018 this sequence version replaced XP_005252038.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1606014.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.12"
     Protein         1..239
                     /product="protein prenyltransferase alpha subunit
                     repeat-containing protein 1 isoform 7"
                     /note="protein prenyltransferase alpha subunit
                     repeat-containing protein 1"
                     /calculated_mol_wt=27390
     Region          88..>208
                     /region_name="PLN02789"
                     /note="farnesyltranstransferase"
                     /db_xref="CDD:215423"
     CDS             1..239
                     /gene="PTAR1"
                     /coded_by="NM_001366940.1:74..793"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:375743"
                     /db_xref="HGNC:HGNC:30449"
                     /db_xref="MIM:621024"
ORIGIN      
        1 maetseevav lvqrvvkdit nafrrnphid eiglipcpea rynrspivlv enklgveswc
       61 vkfllpyvhn klllyrtrkq wlnrdelidv tctllllnpd fttawnvrke lilsgtlnpi
      121 kdlhlgklal tkfpkspetw ihrrwvlqql iqetslpsfv tkgnlgtipt eraqrliqee
      181 mevcgeaagr ypsnynawsh riwvlqhlak ldvkaayflp saslkwlpav ssngsrwte
//
LOCUS       NP_001340202             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340202
VERSION     NP_001340202.1
DBSOURCE    REFSEQ: accession NM_001353273.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.177226.1,
                                           SRR5189661.70108.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353273.1:526..1062"
                     /note="isoform 2 is encoded by transcript variant 35"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001050                465 aa            linear   PRI 20-NOV-2025
DEFINITION  neuromedin-K receptor [Homo sapiens].
ACCESSION   NP_001050
VERSION     NP_001050.1
DBSOURCE    REFSEQ: accession NM_001059.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Nguyen,L.P., Cho,M., Nguyen,T.U., Park,H.K., Nguyen,H.T.,
            Mykhailova,K., Hurh,S., Kim,H.R., Seong,J.Y., Lee,C.S., Ham,B.J.
            and Hwang,J.I.
  TITLE     Neurokinin-2 receptor negatively modulates substance P responses by
            forming complex with Neurokinin-1 receptor
  JOURNAL   Cell Biosci 13 (1), 212 (2023)
   PUBMED   37968728
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Sun,W., Yang,F., Zhang,H., Yuan,Q., Ling,S., Wang,Y., Lv,P., Li,Z.,
            Luo,Y., Liu,D., Yin,W., Shi,P., Xu,H.E. and Tian,C.
  TITLE     Structural insights into neurokinin 3 receptor activation by
            endogenous and analogue peptide agonists
  JOURNAL   Cell Discov 9 (1), 66 (2023)
   PUBMED   37391393
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Guo,F., Fernando,T., Zhu,X. and Shi,Y.
  TITLE     The overexpression of neurokinin B-neurokinin 3 receptor system
            exerts direct effects on the ovary under PCOS-like conditions to
            interfere with mitochondrial function
  JOURNAL   Am J Reprod Immunol 89 (3), e13663 (2023)
   PUBMED   36453600
  REMARK    GeneRIF: The overexpression of neurokinin B-neurokinin 3 receptor
            system exerts direct effects on the ovary under PCOS-like
            conditions to interfere with mitochondrial function.
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Schank,J.R.
  TITLE     Neurokinin receptors in drug and alcohol addiction
  JOURNAL   Brain Res 1734, 146729 (2020)
   PUBMED   32067964
  REMARK    GeneRIF: Neurokinin receptors in drug and alcohol addiction.
            Review article
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Geng,D., Yang,X., Wang,R., Deng,S., Li,L., Hu,X., Jiang,Y. and
            Liu,R.
  TITLE     A novel stopgain mutation c.G992A (p.W331X) in TACR3 gene was
            identified in nonobstructive azoospermia by targeted
            next-generation sequencing
  JOURNAL   J Clin Lab Anal 33 (3), e22700 (2019)
   PUBMED   30390321
  REMARK    GeneRIF: Identified a newly discovered stopgain mutation in
            tachykinin receptor 3 (TACR3) in nonobstructive azoospermia
            paitents.
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Balasubramanian,R. and Crowley,W.F. Jr.
  TITLE     Isolated Gonadotropin-Releasing Hormone (GnRH) Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301509
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Xie,G.X., Miyajima,A. and Goldstein,A.
  TITLE     Expression cloning of cDNA encoding a seven-helix receptor from
            human placenta with affinity for opioid ligands
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 4124-4128 (1992)
   PUBMED   1315051
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1992 Aug 1;89(15):7287]
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Huang,R.R., Cheung,A.H., Mazina,K.E., Strader,C.D. and Fong,T.M.
  TITLE     cDNA sequence and heterologous expression of the human neurokinin-3
            receptor
  JOURNAL   Biochem Biophys Res Commun 184 (2), 966-972 (1992)
   PUBMED   1374246
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Buell,G., Schulz,M.F., Arkinstall,S.J., Maury,K., Missotten,M.,
            Adami,N., Talabot,F. and Kawashima,E.
  TITLE     Molecular characterisation, expression and localisation of human
            neurokinin-3 receptor
  JOURNAL   FEBS Lett 299 (1), 90-95 (1992)
   PUBMED   1312036
REFERENCE   10 (residues 1 to 465)
  AUTHORS   Takahashi,K., Tanaka,A., Hara,M. and Nakanishi,S.
  TITLE     The primary structure and gene organization of human substance P
            and neuromedin K receptors
  JOURNAL   Eur J Biochem 204 (3), 1025-1033 (1992)
   PUBMED   1312928
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004065.1, M89473.1 and
            AC105460.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to a family of genes that function as
            receptors for tachykinins.  Receptor affinities are specified by
            variations in the 5'-end of the sequence.  The receptors belonging
            to this family are characterized by interactions with G proteins
            and 7 hydrophobic transmembrane regions.  This gene encodes the
            receptor for the tachykinin neurokinin 3, also referred to as
            neurokinin B. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M89473.1, BC121806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304883.3/ ENSP00000303325.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..465
                     /product="neuromedin-K receptor"
                     /EC_number="2.7.11.14"
                     /note="neurokinin B receptor; neurokinin beta receptor;
                     NK-3 receptor; NK3 receptor"
                     /calculated_mol_wt=52071
     Site            23
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29371.1)"
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29371.1)"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29371.1)"
     Site            85..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          86..367
                     /region_name="7tmA_NKR_NK3R"
                     /note="neuromedin-K receptor, member of the class A family
                     of seven-transmembrane G protein-coupled receptors;
                     cd16003"
                     /db_xref="CDD:320669"
     Region          87..113
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320669"
     Site            118..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          120..146
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320669"
     Site            order(142,145..146,158..163,165..166,169,212,214..218,244,
                     247..249,251..253,255..256,312,315..316,318..319,322,
                     334..335,337..339,342,345..346)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320669"
     Region          158..188
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320669"
     Site            160..181
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          199..220
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320669"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          244..273
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320669"
     Site            246..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          292..322
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320669"
     Site            300..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          335..360
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320669"
     Site            335..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     Region          415..465
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29371.1)"
     CDS             1..465
                     /gene="TACR3"
                     /gene_synonym="HH11; NK-3R; NK3; NK3R; NKR; TAC3R; TAC3RL"
                     /coded_by="NM_001059.3:311..1708"
                     /db_xref="CCDS:CCDS3664.1"
                     /db_xref="GeneID:6870"
                     /db_xref="HGNC:HGNC:11528"
                     /db_xref="MIM:162332"
ORIGIN      
        1 matlpaaetw idggggvgad avnltaslaa gaatgavetg wlqlldqagn lssspsalgl
       61 pvaspapsqp wanltnqfvq pswrialwsl aygvvvavav lgnliviwii lahkrmrtvt
      121 nyflvnlafs dasmaafntl vnfiyalhse wyfganycrf qnffpitavf asiysmtaia
      181 vdrymaiidp lkprlsatat kivigsiwil afllafpqcl ysktkvmpgr tlcfvqwpeg
      241 pkqhftyhii viilvycfpl limgitytiv gitlwggeip gdtcdkyheq lkakrkvvkm
      301 miivvmtfai cwlpyhiyfi ltaiyqqlnr wkyiqqvyla sfwlamsstm ynpiiyccln
      361 krfragfkra frwcpfikvs sydelelktt rfhpnrqssm ytvtrmesmt vvfdpndadt
      421 trssrkkrat prdpsfngcs rrnsksasat ssfisspyts vdeys
//
LOCUS       NP_001128525             410 aa            linear   PRI 20-NOV-2025
DEFINITION  single Ig IL-1-related receptor [Homo sapiens].
ACCESSION   NP_001128525 XP_002347224 XP_003120711
VERSION     NP_001128525.1
DBSOURCE    REFSEQ: accession NM_001135053.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Mariotti,F.R., Supino,D., Landolina,N., Garlanda,C., Mantovani,A.,
            Moretta,L. and Maggi,E.
  TITLE     IL-1R8: A molecular brake of anti-tumor and anti-viral activity of
            NK cells and ILC
  JOURNAL   Semin Immunol 66, 101712 (2023)
   PUBMED   36753974
  REMARK    GeneRIF: IL-1R8: A molecular brake of anti-tumor and anti-viral
            activity of NK cells and ILC.
            Review article
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Yu,W., Haque,I., Venkatraman,A., Menden,H.L., Mabry,S.M., Roy,B.C.,
            Xia,S., Prokop,J.W., Umar,S., Geurts,A.M. and Sampath,V.
  TITLE     SIGIRR Mutation in Human Necrotizing Enterocolitis (NEC) Disrupts
            STAT3-Dependent microRNA Expression in Neonatal Gut
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (2), 425-440 (2022)
   PUBMED   34563711
  REMARK    GeneRIF: SIGIRR Mutation in Human Necrotizing Enterocolitis (NEC)
            Disrupts STAT3-Dependent microRNA Expression in Neonatal Gut.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Jia,C., Zhuge,Y., Zhang,S., Ni,C., Wang,L., Wu,R., Niu,C., Wen,Z.,
            Rong,X., Qiu,H. and Chu,M.
  TITLE     IL-37b alleviates endothelial cell apoptosis and inflammation in
            Kawasaki disease through IL-1R8 pathway
  JOURNAL   Cell Death Dis 12 (6), 575 (2021)
   PUBMED   34083516
  REMARK    GeneRIF: IL-37b alleviates endothelial cell apoptosis and
            inflammation in Kawasaki disease through IL-1R8 pathway.
            Erratum:[Cell Death Dis. 2021 Aug 2;12(8):759. doi:
            10.1038/s41419-021-04044-5. PMID: 34341339]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Yang,X., Zhang,M., Xu,S., Pan,H., Leng,R. and Shuai,Z.
  TITLE     Single Immunoglobulin IL-1-Related Receptor (SIGIRR) Gene rs7396562
            Polymorphism and Expression Level in Rheumatoid Arthritis
  JOURNAL   Biomed Res Int 2021, 6683148 (2021)
   PUBMED   34036103
  REMARK    GeneRIF: Single Immunoglobulin IL-1-Related Receptor (SIGIRR) Gene
            rs7396562 Polymorphism and Expression Level in Rheumatoid
            Arthritis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Cavalli,G., Tengesdal,I.W., Gresnigt,M., Nemkov,T., Arts,R.J.W.,
            Dominguez-Andres,J., Molteni,R., Stefanoni,D., Cantoni,E.,
            Cassina,L., Giugliano,S., Schraa,K., Mills,T.S., Pietras,E.M.,
            Eisenmensser,E.Z., Dagna,L., Boletta,A., D'Alessandro,A.,
            Joosten,L.A.B., Netea,M.G. and Dinarello,C.A.
  TITLE     The anti-inflammatory cytokine interleukin-37 is an inhibitor of
            trained immunity
  JOURNAL   Cell Rep 35 (1), 108955 (2021)
   PUBMED   33826894
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Polentarutti,N., Rol,G.P., Muzio,M., Bosisio,D., Camnasio,M.,
            Riva,F., Zoja,C., Benigni,A., Tomasoni,S., Vecchi,A., Garlanda,C.
            and Mantovani,A.
  TITLE     Unique pattern of expression and inhibition of IL-1 signaling by
            the IL-1 receptor family member TIR8/SIGIRR
  JOURNAL   Eur Cytokine Netw 14 (4), 211-218 (2003)
   PUBMED   14715412
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Wald,D., Qin,J., Zhao,Z., Qian,Y., Naramura,M., Tian,L., Towne,J.,
            Sims,J.E., Stark,G.R. and Li,X.
  TITLE     SIGIRR, a negative regulator of Toll-like receptor-interleukin 1
            receptor signaling
  JOURNAL   Nat Immunol 4 (9), 920-927 (2003)
   PUBMED   12925853
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Du,X., Poltorak,A., Wei,Y. and Beutler,B.
  TITLE     Three novel mammalian toll-like receptors: gene structure,
            expression, and evolution
  JOURNAL   Eur Cytokine Netw 11 (3), 362-371 (2000)
   PUBMED   11022119
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Thomassen,E., Renshaw,B.R. and Sims,J.E.
  TITLE     Identification and characterization of SIGIRR, a molecule
            representing a novel subtype of the IL-1R superfamily
  JOURNAL   Cytokine 11 (6), 389-399 (1999)
   PUBMED   10346978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA963481.1, AK172830.1, BX369506.2 and AK025099.1.
            
            On or before Dec 15, 2010 this sequence version replaced
            XP_003120711.1, XP_002347224.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All three variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025953.1, SRR11853565.4272.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..410
                     /product="single Ig IL-1-related receptor"
                     /note="single Ig IL-1R-related molecule; single
                     immunoglobulin domain IL1R1 related; toll/interleukin-1
                     receptor 8; single immunoglobulin domain-containing
                     IL1R-related protein; single immunoglobulin and
                     toll-interleukin 1 receptor (TIR) domain"
                     /calculated_mol_wt=45548
     Region          9..>66
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          28..32
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          46..50
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          80..87
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            86
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          95..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IA17.3)"
     Region          168..311
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          340..390
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IA17.3)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JLZ8; propagated from
                     UniProtKB/Swiss-Prot (Q6IA17.3)"
     CDS             1..410
                     /gene="SIGIRR"
                     /gene_synonym="IL-1R8; TIR8"
                     /coded_by="NM_001135053.2:258..1490"
                     /db_xref="CCDS:CCDS31325.1"
                     /db_xref="GeneID:59307"
                     /db_xref="HGNC:HGNC:30575"
                     /db_xref="MIM:605478"
ORIGIN      
        1 mpgvcdrapd flspsedqvl rpalgssval nctawvvsgp hcslpsvqwl kdglplgigg
       61 hyslheyswv kanlsevlvs svlgvnvtst evygaftcsi qnisfssftl qragptshva
      121 avlasllvll alllaallyv kcrlnvllwy qdaygevein dgklydayvs ysdcpedrkf
      181 vnfilkpqle rrrgyklfld drdllpraep sadllvnlsr crrlivvlsd aflsrawcsh
      241 sfreglcrll eltrrpifit fegqrrdpah palrllrqhr hlvtlllwrp gsvtpssdfw
      301 kevqlalprk vqyrpvegdp qtqlqddkdp mlilrgrvpe graldsevdp dpegdlgvrg
      361 pvfgepsapp htsgvslges rssevdvsdl gsrnysartd fyclvskddm
//
LOCUS       NP_001230156             647 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform d [Homo sapiens].
ACCESSION   NP_001230156
VERSION     NP_001230156.1
DBSOURCE    REFSEQ: accession NM_001243227.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299169.1 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 3. The resulting isoform (d) is
            shorter at the N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299169.1, SRR1803617.103495.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..647
                     /product="transcription factor 4 isoform d"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68967
     Region          538..622
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(546,550,552..554,556,561,582..583)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(559..560,563..564,566..567,570,574,584,587,591,594,
                     597..602)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..647
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243227.2:516..2459"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58629.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsagtavwsr nggqassspn yegplhslqs
      361 riedrlerld daihvlrnha vgpstampgg hgdmhgiigp shngamgglg sgygtgllsa
      421 nrhslmvgth redgvalrgs hsllpnqvpv pqlpvqsats pdlnppqdpy rgmppglqgq
      481 svssgsseik sddegdenlq dtkssedkkl dddkkdiksi trsrssnndd edltpeqkae
      541 rekerrmann arerlrvrdi neafkelgrm vqlhlksdkp qtkllilhqa vavilsleqq
      601 vrernlnpka aclkrreeek vsseppplsl agphpgmgda snhmgqm
//
LOCUS       NP_001308521              69 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 30 [Homo sapiens].
ACCESSION   NP_001308521
VERSION     NP_001308521.1
DBSOURCE    REFSEQ: accession NM_001321592.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 69)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 69)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 69)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 69)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 69)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 69)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 69)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 69)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 69)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 69)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU785828.1, AI829910.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..69
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..69
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 30"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=7549
     Region          12..>56
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..69
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321592.2:671..880"
                     /note="isoform 30 is encoded by transcript variant 33"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sargsqestv
       61 isqlhgyls
//
LOCUS       NP_055331                753 aa            linear   PRI 20-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_055331
VERSION     NP_055331.1
DBSOURCE    REFSEQ: accession NM_014516.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Ghashghaei,M., Liu,Y., Ettles,J., Bombaci,G., Ramkumar,N., Liu,Z.,
            Escano,L., Miko,S.S., Kim,Y., Waldron,J.A., Do,K., MacPherson,K.,
            Yuen,K.A., Taibi,T., Yue,M., Arsalan,A., Jin,Z., Edin,G.,
            Karsan,A., Morin,G.B., Kuchenbauer,F., Perna,F., Bushell,M. and
            Vu,L.P.
  TITLE     Translation efficiency driven by CNOT3 subunit of the CCR4-NOT
            complex promotes leukemogenesis
  JOURNAL   Nat Commun 15 (1), 2340 (2024)
   PUBMED   38491013
  REMARK    GeneRIF: Translation efficiency driven by CNOT3 subunit of the
            CCR4-NOT complex promotes leukemogenesis.
            Erratum:[Nat Commun. 2024 Oct 7;15(1):8674. doi:
            10.1038/s41467-024-53071-1. PMID: 39375334]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Burgess,H.M., Grande,R., Riccio,S., Dinesh,I., Winkler,G.S.,
            Depledge,D.P. and Mohr,I.
  TITLE     CCR4-NOT differentially controls host versus virus poly(a)-tail
            length and regulates HCMV infection
  JOURNAL   EMBO Rep 24 (12), e56327 (2023)
   PUBMED   37846490
  REMARK    GeneRIF: CCR4-NOT differentially controls host versus virus
            poly(a)-tail length and regulates HCMV infection.
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Zhao,P., Meng,Q., Wan,C., Lei,T., Zhang,L., Zhang,X., Tan,L.,
            Zhu,H. and He,X.
  TITLE     Clinical features of CNOT3-associated neurodevelopmental disorder
            in three Chinese patients
  JOURNAL   Neurogenetics 24 (2), 129-136 (2023)
   PUBMED   36802310
  REMARK    GeneRIF: Clinical features of CNOT3-associated neurodevelopmental
            disorder in three Chinese patients.
REFERENCE   5  (residues 1 to 753)
  AUTHORS   McLenachan,S., Zhang,D., Grainok,J., Zhang,X., Huang,Z., Chen,S.C.,
            Zaw,K., Lima,A., Jennings,L., Roshandel,D., Moon,S.Y., Heath
            Jeffery,R.C., Attia,M.S., Thompson,J.A., Lamey,T.M., McLaren,T.L.,
            De Roach,J., Fletcher,S. and Chen,F.K.
  TITLE     Determinants of Disease Penetrance in PRPF31-Associated Retinopathy
  JOURNAL   Genes (Basel) 12 (10), 1542 (2021)
   PUBMED   34680937
  REMARK    GeneRIF: Determinants of Disease Penetrance in PRPF31-Associated
            Retinopathy.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Yin,X., Warner,D.R., Roberts,E.A., Pisano,M.M. and Greene,R.M.
  TITLE     Identification of novel CBP interacting proteins in embryonic
            orofacial tissue
  JOURNAL   Biochem Biophys Res Commun 329 (3), 1010-1017 (2005)
   PUBMED   15752756
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Aoki,T., Okada,N., Wakamatsu,T. and Tamura,T.A.
  TITLE     TBP-interacting protein 120B, which is induced in relation to
            myogenesis, binds to NOT3
  JOURNAL   Biochem Biophys Res Commun 296 (5), 1097-1103 (2002)
   PUBMED   12207886
  REMARK    GeneRIF: TBP-interacting protein 120B binds to NOT3
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC245052.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016474.1, SRR3476690.377136.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221232.11/ ENSP00000221232.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..753
                     /product="CCR4-NOT transcription complex subunit 3 isoform
                     1"
                     /note="NOT3 (negative regulator of transcription 3, yeast)
                     homolog; CCR4-associated factor 3; leukocyte receptor
                     cluster member 2"
                     /calculated_mol_wt=81741
     Region          3..229
                     /region_name="Not3"
                     /note="Not1 N-terminal domain, CCR4-Not complex component;
                     pfam04065"
                     /db_xref="CDD:461155"
     Region          240..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     Region          <288..659
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Site            542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75175.1)"
     Region          620..745
                     /region_name="NOT2_3_5"
                     /note="NOT2 / NOT3 / NOT5 family; pfam04153"
                     /db_xref="CDD:461199"
     Region          661..753
                     /region_name="Repressor domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O75175.1)"
     CDS             1..753
                     /gene="CNOT3"
                     /gene_synonym="IDDSADF; LENG2; NOT3; NOT3H"
                     /coded_by="NM_014516.4:283..2544"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12880.1"
                     /db_xref="GeneID:4849"
                     /db_xref="HGNC:HGNC:7879"
                     /db_xref="MIM:604910"
ORIGIN      
        1 madkrklqge idrclkkvse gveqfediwq klhnaananq kekyeadlkk eikklqrlrd
       61 qiktwvasne ikdkrqlidn rklietqmer fkvveretkt kayskeglgl aqkvdpaqke
      121 keevgqwltn tidtlnmqvd qfesevesls vqtrkkkgdk dkqdrieglk rhiekhryhv
      181 rmletilrml dndsilvdai rkikddveyy vdssqdpdfe eneflyddld ledipqalva
      241 tsppshshme deifnqssst ptsttssspi ppspanctte nseddkkrgr stdsevsqsp
      301 akngskpvhs nqhpqspavp ptypsgpppa asalsttpgn ngvpapaapp salgpkaspa
      361 pshnsgtpap yaqavappap sgpsttqprp psvqpsgggg ggsggggsss ssnssaggga
      421 gkqngatsys svvadspaev alsssggnna ssqalgppsg phnpppstsk epsaaaptga
      481 ggvapgsgnn sggpsllvpl pvnppssptp sfsdakaaga llngppqfst apeikapepl
      541 sslksmaera aissgiedpv ptlhlterdi ilsstsappa saqpplqlse vniplslgvc
      601 plgpvpltke qlyqqameea awhhmphpsd serirqylpr npcptppyhh qmppphsdtv
      661 efyqrlstet lffifyyleg tkaqylaaka lkkqswrfht kymmwfqrhe epktitdefe
      721 qgtyiyfdye kwgqrkkegf tfeyryledr dlq
//
LOCUS       NP_149073                210 aa            linear   PRI 20-NOV-2025
DEFINITION  SAP domain-containing ribonucleoprotein [Homo sapiens].
ACCESSION   NP_149073
VERSION     NP_149073.1
DBSOURCE    REFSEQ: accession NM_033082.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Xie,Y., Gao,S., Zhang,K., Bhat,P., Clarke,B.P., Batten,K., Mei,M.,
            Gazzara,M., Shay,J.W., Lynch,K.W., Angelos,A.E., Hill,P.S.,
            Ivey,A.L., Fontoura,B.M.A. and Ren,Y.
  TITLE     Structural basis for high-order complex of SARNP and DDX39B to
            facilitate mRNP assembly
  JOURNAL   Cell Rep 42 (8), 112988 (2023)
   PUBMED   37578863
  REMARK    GeneRIF: Structural basis for high-order complex of SARNP and
            DDX39B to facilitate mRNP assembly.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Ellis,J.D., Lleres,D., Denegri,M., Lamond,A.I. and Caceres,J.F.
  TITLE     Spatial mapping of splicing factor complexes involved in exon and
            intron definition
  JOURNAL   J Cell Biol 181 (6), 921-934 (2008)
   PUBMED   18559666
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Sugiura,T., Sakurai,K. and Nagano,Y.
  TITLE     Intracellular characterization of DDX39, a novel growth-associated
            RNA helicase
  JOURNAL   Exp Cell Res 313 (4), 782-790 (2007)
   PUBMED   17196963
  REMARK    GeneRIF: CIP29 physically and functionally associates with DDX39,
            suggesting their cooperation in the RNA metabolism.
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Leaw,C.L., Ren,E.C. and Choong,M.L.
  TITLE     Hcc-1 is a novel component of the nuclear matrix with growth
            inhibitory function
  JOURNAL   Cell Mol Life Sci 61 (17), 2264-2273 (2004)
   PUBMED   15338056
  REMARK    GeneRIF: Hcc-1 plays a role in growth regulation and nucleic acids
            metabolism.
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Hashii,Y., Kim,J.Y., Sawada,A., Tokimasa,S., Hiroyuki,F., Ohta,H.,
            Makiko,K., Takihara,Y., Ozono,K. and Hara,J.
  TITLE     A novel partner gene CIP29 containing a SAP domain with MLL
            identified in infantile myelomonocytic leukemia
  JOURNAL   Leukemia 18 (9), 1546-1548 (2004)
   PUBMED   15284855
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Fukuda,S., Wu,D.W., Stark,K. and Pelus,L.M.
  TITLE     Cloning and characterization of a proliferation-associated
            cytokine-inducible protein, CIP29
  JOURNAL   Biochem Biophys Res Commun 292 (3), 593-600 (2002)
   PUBMED   11922608
  REMARK    GeneRIF: CIP29 appears to be a new cytokine regulated protein
            involved in normal and cancer cell proliferation.
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Choong,M.L., Tan,L.K., Lo,S.L., Ren,E.C., Ou,K., Ong,S.E.,
            Liang,R.C., Seow,T.K. and Chung,M.C.
  TITLE     An integrated approach in the discovery and characterization of a
            novel nuclear protein over-expressed in liver and pancreatic tumors
  JOURNAL   FEBS Lett 496 (2-3), 109-116 (2001)
   PUBMED   11356193
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI520421.1, BC007099.1 and
            AF161434.1.
            
            Summary: This gene encodes a protein that is upregulated in
            response to various cytokines. The encoded protein may play a role
            in cell cycle progression. A translocation between this gene and
            the myeloid/lymphoid leukemia gene, resulting in expression of a
            chimeric protein, has been associated with acute myelomonocytic
            leukemia. Pseudogenes exist on chromosomes 7 and 8. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.16237.1,
                                           SRR1660805.38117.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336133.8/ ENSP00000337632.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..210
                     /product="SAP domain-containing ribonucleoprotein"
                     /note="cytokine induced protein 29 kDa; hepatocellular
                     carcinoma 1; proliferation associated cytokine-inducible
                     protein CIP29; nuclear protein Hcc-1; cytokine-induced
                     protein of 29 kDa"
                     /calculated_mol_wt=23540
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P82979.3)"
     Region          7..>90
                     /region_name="PLN03124"
                     /note="poly [ADP-ribose] polymerase; Provisional"
                     /db_xref="CDD:215591"
     Region          8..42
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1J3; propagated from
                     UniProtKB/Swiss-Prot (P82979.3)"
     Region          45..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82979.3)"
     Site            142
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1J3; propagated from
                     UniProtKB/Swiss-Prot (P82979.3)"
     Region          161..210
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82979.3)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1J3; propagated from
                     UniProtKB/Swiss-Prot (P82979.3)"
     CDS             1..210
                     /gene="SARNP"
                     /gene_synonym="CIP29; HCC1; HSPC316; THO1"
                     /coded_by="NM_033082.4:24..656"
                     /db_xref="CCDS:CCDS8892.1"
                     /db_xref="GeneID:84324"
                     /db_xref="HGNC:HGNC:24432"
                     /db_xref="MIM:610049"
ORIGIN      
        1 matetvelhk lklaelkqec largletkgi kqdlihrlqa yleehaeeea needvlgdet
       61 eeeetkpiel pvkeeeppek tvdvaaekkv vkitseipqt ermqkraerf nvpvsleskk
      121 aaraarfgis svptkglssd nkpmvnldkl keraqrfgln vssisrksed deklkkrker
      181 fgivtssagt gttedteakk rkraerfgia
//
LOCUS       NP_001351834            2852 aa            linear   PRI 20-NOV-2025
DEFINITION  lipopolysaccharide-responsive and beige-like anchor protein isoform
            3 [Homo sapiens].
ACCESSION   NP_001351834 XP_005263432
VERSION     NP_001351834.1
DBSOURCE    REFSEQ: accession NM_001364905.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2852)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2852)
  AUTHORS   Szentgyorgyi,V., Lueck,L.M., Overwijn,D., Ritz,D., Zoeller,N.,
            Schmidt,A., Hondele,M., Spang,A. and Bakhtiar,S.
  TITLE     Arf1-dependent LRBA recruitment to Rab4 endosomes is required for
            endolysosome homeostasis
  JOURNAL   J Cell Biol 223 (11) (2024)
   PUBMED   39325073
  REMARK    GeneRIF: Arf1-dependent LRBA recruitment to Rab4 endosomes is
            required for endolysosome homeostasis.
REFERENCE   3  (residues 1 to 2852)
  AUTHORS   Freund,T., Baxter,S.K., Walsh,T., Golan,H., Kapelushnik,J.,
            Abramsohn-Goldenberg,M., Benor,S., Sarid,N., Ram,R., Alcalay,Y.,
            Segel,R., Renbaum,P., Stepensky,P., King,M.C., Torgerson,T.R. and
            Hagin,D.
  TITLE     Clinically Complex LRBA Deficiency Due to a Founder Allele in the
            Georgian Jewish Population
  JOURNAL   J Clin Immunol 43 (1), 151-164 (2023)
   PUBMED   36063261
  REMARK    GeneRIF: Clinically Complex LRBA Deficiency Due to a Founder Allele
            in the Georgian Jewish Population.
REFERENCE   4  (residues 1 to 2852)
  AUTHORS   Catak,M.C., Akcam,B., Bilgic Eltan,S., Babayeva,R., Karakus,I.S.,
            Akgun,G., Baser,D., Bulutoglu,A., Bayram,F., Kasap,N., Kiykim,A.,
            Hancioglu,G., Kokcu Karadag,S.I., Kendir Demirkol,Y., Ozen,S.,
            Cekic,S., Ozcan,D., Edeer Karaca,N., Sasihuseyinoglu,A.S.,
            Cansever,M., Ozek Yucel,E., Tamay,Z., Altintas,D.U., Aydogmus,C.,
            Celmeli,F., Cokugras,H., Gulez,N., Genel,F., Metin,A., Guner,S.N.,
            Kutukculer,N., Keles,S., Reisli,I., Kilic,S.S., Yildiran,A.,
            Karakoc-Aydiner,E., Lo,B., Ozen,A. and Baris,S.
  TITLE     Comparing the levels of CTLA-4-dependent biological defects in
            patients with LRBA deficiency and CTLA-4 insufficiency
  JOURNAL   Allergy 77 (10), 3108-3123 (2022)
   PUBMED   35491430
  REMARK    GeneRIF: Comparing the levels of CTLA-4-dependent biological
            defects in patients with LRBA deficiency and CTLA-4 insufficiency.
REFERENCE   5  (residues 1 to 2852)
  AUTHORS   Yao,J., Gu,H., Mou,W., Chen,Z., Ma,J., Ma,H., Li,N., Zhang,R.,
            Wang,T., Jiang,J. and Wu,R.
  TITLE     Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients
  JOURNAL   Int J Immunopathol Pharmacol 36, 3946320221125591 (2022)
   PUBMED   36074705
  REMARK    GeneRIF: Various phenotypes of LRBA gene with compound heterozygous
            variation: A case series report of pediatric cytopenia patients.
REFERENCE   6  (residues 1 to 2852)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 2852)
  AUTHORS   Gebauer,D., Li,J., Jogl,G., Shen,Y., Myszka,D.G. and Tong,L.
  TITLE     Crystal structure of the PH-BEACH domains of human LRBA/BGL
  JOURNAL   Biochemistry 43 (47), 14873-14880 (2004)
   PUBMED   15554694
  REMARK    GeneRIF: The crystal structure of the aPH-BEACH domains of LRBA
            were studied.
REFERENCE   8  (residues 1 to 2852)
  AUTHORS   Dyomin,V.G., Chaganti,S.R., Dyomina,K., Palanisamy,N., Murty,V.V.,
            Dalla-Favera,R. and Chaganti,R.S.
  TITLE     BCL8 is a novel, evolutionarily conserved human gene family
            encoding proteins with presumptive protein kinase A anchoring
            function
  JOURNAL   Genomics 80 (2), 158-165 (2002)
   PUBMED   12160729
REFERENCE   9  (residues 1 to 2852)
  AUTHORS   Wang,J.W., Howson,J., Haller,E. and Kerr,W.G.
  TITLE     Identification of a novel lipopolysaccharide-inducible gene with
            key features of both A kinase anchor proteins and chs1/beige
            proteins
  JOURNAL   J Immunol 166 (7), 4586-4595 (2001)
   PUBMED   11254716
REFERENCE   10 (residues 1 to 2852)
  AUTHORS   Feuchter,A.E., Freeman,J.D. and Mager,D.L.
  TITLE     Strategy for detecting cellular transcripts promoted by human
            endogenous long terminal repeats: identification of a novel gene
            (CDC4L) with homology to yeast CDC4
  JOURNAL   Genomics 13 (4), 1237-1246 (1992)
   PUBMED   1505956
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104796.4, AC092544.4,
            AC110813.4, AC097373.3, AC092612.3 and AC093748.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 13, 2018 this sequence version replaced XP_005263432.1.
            
            Summary: The protein encoded by this gene is a member of the
            WDL-BEACH-WD (WBW) gene family. Its expression is induced in B
            cells and macrophages by bacterial lipopolysaccharides (LPS). The
            encoded protein associates with protein kinase A and may be
            involved in leading intracellular vesicles to activated receptor
            complexes, which aids in the secretion and/or membrane deposition
            of immune effector molecules. Defects in this gene are associated
            with the disorder common variable immunodeficiency-8 with
            autoimmunity. Two transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Dec 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000651943.2/ ENSP00000498582.2
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..2852
                     /product="lipopolysaccharide-responsive and beige-like
                     anchor protein isoform 3"
                     /note="vesicle trafficking, beach and anchor containing;
                     lipopolysaccharide-responsive and beige-like anchor
                     protein; CDC4-like protein; LPS-responsive vesicle
                     trafficking, beach and anchor containing"
                     /calculated_mol_wt=317660
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          229..376
                     /region_name="Laminin_G_3"
                     /note="Concanavalin A-like lectin/glucanases superfamily;
                     pfam13385"
                     /db_xref="CDD:463865"
     Region          441..921
                     /region_name="DUF4704"
                     /note="Neurobeachin/BDCP, DUF4704 alpha solenoid region;
                     pfam15787"
                     /db_xref="CDD:464870"
     Region          969..1005
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1018..1039
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1161..1193
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1301..1343
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1531..1548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          1586..1668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1759..1789
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Site            1767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Site            1770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESE1; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          1880..2047
                     /region_name="DUF1088"
                     /note="Neurobeachin-like, DUF1088; pfam06469"
                     /db_xref="CDD:461925"
     Site            2053
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2073..2170
                     /region_name="PH_BEACH"
                     /note="PH domain associated with Beige/BEACH; pfam14844"
                     /db_xref="CDD:434260"
     Region          2201..2478
                     /region_name="Beach"
                     /note="Beige/BEACH domain; smart01026"
                     /db_xref="CDD:214982"
     Site            2485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50851.4)"
     Region          2573..2837
                     /region_name="NBCH_WD40"
                     /note="Neurobeachin beta propeller domain; pfam20426"
                     /db_xref="CDD:466575"
     Region          2580..2622
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2589..2625
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2625..2668
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2631..2684
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2684..2724
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2689..2724
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2729..2758
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2766..2805
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     Region          2771..2805
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2808..2847
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P50851.4)"
     CDS             1..2852
                     /gene="LRBA"
                     /gene_synonym="BGL; CDC4L; CVID8; LAB300; LBA; uc.147"
                     /coded_by="NM_001364905.1:303..8861"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93649.1"
                     /db_xref="GeneID:987"
                     /db_xref="HGNC:HGNC:1742"
                     /db_xref="MIM:606453"
ORIGIN      
        1 masednrvps ppptgddggg ggreetpteg galslkpglp irgirmkfav ltglvevgev
       61 snrdivetvf nllvggqfdl emnfiiqege sincmvdlle kcditcqaev wsmftailkk
      121 sirnlqvcte vglvekvlgk iekvdnmiad llvdmlgvla synltvrelk lffsklqgdk
      181 grwpphagkl lsvlkhmpqk ygpdaffnfp gksaaaialp piakwpyqng ftfhtwlrmd
      241 pvnninvdkd kpylycfrts kglgysahfv ggclivtsik skgkgfqhcv kfdfkpqkwy
      301 mvtivhiynr wknselrcyv ngelasygei twfvntsdtf dkcflgsset adanrvfcgq
      361 mtavylfsea lnaaqifaiy qlglgykgtf kfkaesdlfl aehhklllyd gklssaiaft
      421 ynpratdaql clesspkdnp sifvhsphal mlqdvkavlt hsiqsamhsi ggvqvlfplf
      481 aqldyrqyls deidlticst llafimellk nsiamqeqml ackgflvigy sleksskshv
      541 sravlelcla fskylsnlqn gmpllkqlcd hvllnpaiwi htpakvqlml ytylstefig
      601 tvniyntirr vgtvllimht lkyyywavnp qdrsgitpkg ldgprpnqke mlslrafllm
      661 fikqlvmkds gvkedelqai lnylltmhed dnlmdvlqll valmsehpns mipafdqrng
      721 lrviykllas ksegirvqal kamgyflkhl apkrkaevml ghglfsllae rlmlqtnlit
      781 mttynvlfei lieqigtqvi hkqhpdpdss vkiqnpqilk viatllrnsp qcpesmevrr
      841 aflsdmiklf nnsrenrrsl lqcsvwqewm lslcyfnpkn sdeqkitemv yaifrillyh
      901 avkyewggwr vwvdtlsith skvtfeihke nlanifreqq gkvdeeiglc sstsvqaasg
      961 irrdinvsvg sqqpdtkdsp vcphfttngn enssiektss lesasnielq ttntsyeemk
     1021 aeqenqelpd egtleetltn etrnaddlev ssdiieavai ssnsfittgk dsmtvsevta
     1081 sisspseeda sempefldks iveeeedddy velkvegspt eeanlptelq dnslspaase
     1141 agekldmfgn ddklifqegk pvtekqtdte tqdskdsgiq tmtasgssam spettvsqia
     1201 vesdlgqmle egkkatnltr etklindchg svseasseqk iakldvsnva tdterlelka
     1261 spnveapqph rhvleisrqh eqpgqgiapd avngqrrdsr stvfripefn wsqmhqrllt
     1321 dllfsietdi qmwrshstkt vmdfvnssdn vifvhntihl isqvmdnmvm acggilplls
     1381 aatsathele nieptqglsi easvtflqrl islvdvlifa sslgfteiea eksmssggil
     1441 rqclrlvcav avrnclecqq hsqlktrgdk alkpmhslip lgksaakspv divtggispv
     1501 rdldrllqdm dinrlravvf rdiedskqaq flalavvyfi svlmvskyrd ilepqnerhs
     1561 qsctetgsen envslseitp aafstlttas veesestssa rrrdsgigee tatglgshve
     1621 vtphtappgv sagpdaisev lstlslevnk spetkndrgn dldtkatpsv svsknvnvkd
     1681 ilrslvnipa dgvtvdpall ppaclgalgd lsveqpvqfr sfdrsvivaa kksavspstf
     1741 ntsiptnavs vvssvdsaqa sdmggespgs rssnaklpsv ptvdsvsqdp vsnmsiterl
     1801 ehalekaapl lreifvdfap flsrtllgsh gqelliegts lvcmkssssv velvmllcsq
     1861 ewqnsiqkna glafielvne grllsqtmkd hlvrvaneae filsrqraed ihrhaefesl
     1921 caqysadkre dekmcdhlir aakyrdhvta tqliqkiini ltdkhgawgn savsrplefw
     1981 rldyweddlr rrrrfvrnpl gsthpeatlk tavehatded ilakgkqsir sqalgnqnse
     2041 neillegddd tlssvdekdl enlagpvsls tpaqlvapsv vvkgtlsvts selyfevdee
     2101 dpnfkkidpk ilayteglhg kwlfteirsi fsrryllqnt aleifmanrv avmfnfpdpa
     2161 tvkkvvnylp rvgvgtsfgl pqtrrislas prqlfkasnm tqrwqhreis nfeylmflnt
     2221 iagrsyndln qypvfpwvit nyeseeldlt lptnfrdlsk pigalnpkra affaeryesw
     2281 eddqvpkfhy gthystasfv lawllriepf ttyflnlqgg kfdhadrtfs sisrawrnsq
     2341 rdtsdikeli pefyylpemf vnfnnynlgv mddgtvvsdv elppwaktse efvhinrlal
     2401 esefvscqlh qwidlifgyk qqgpeavral nvfyyltyeg avnlnsitdp vlreaveaqi
     2461 rsfgqtpsql liephpprgs amqvsplmft dkaqqdvimv lkfpsnspvt hvaantqpgl
     2521 atpavitvta nrlfavnkwh nlpahqgavq dqpyqlpvei dpliasntgm hrrqitdlld
     2581 qsiqvhsqcf vitsdnryil vcgfwdksfr vystdtgrli qvvfghwdvv tclarsesyi
     2641 ggncyilsgs rdatlllwyw ngkcsgigdn pgsetaapra iltghdyevt caavcaelgl
     2701 vlsgsqegpc lihsmngdll rtlegpencl kpkliqasre ghcvifyeng lfctfsvngk
     2761 lqatmetddn iraiqlsrdg qylltggdrg vvvvrqvsdl kqlfaypgcd agiramalsy
     2821 dqrciisgma sgsivlfynd fnrwhheyqt ry
//
LOCUS       NP_001278434             179 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase inhibitor 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001278434
VERSION     NP_001278434.1
DBSOURCE    REFSEQ: accession NM_001291505.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Bresch,A.M., Yerich,N., Wang,R. and Sperry,A.O.
  TITLE     The PP1 regulator PPP1R2 coordinately regulates AURKA and PP1 to
            control centrosome phosphorylation and maintain central spindle
            architecture
  JOURNAL   BMC Mol Cell Biol 21 (1), 84 (2020)
   PUBMED   33238888
  REMARK    GeneRIF: The PP1 regulator PPP1R2 coordinately regulates AURKA and
            PP1 to control centrosome phosphorylation and maintain central
            spindle architecture.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Kakinoki,Y., Somers,J. and Brautigan,D.L.
  TITLE     Multisite phosphorylation and the nuclear localization of
            phosphatase inhibitor 2-green fluorescent protein fusion protein
            during S phase of the cell growth cycle
  JOURNAL   J Biol Chem 272 (51), 32308-32314 (1997)
   PUBMED   9405437
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Permana,P.A. and Mott,D.M.
  TITLE     Genetic analysis of human type 1 protein phosphatase inhibitor 2 in
            insulin-resistant Pima Indians
  JOURNAL   Genomics 41 (1), 110-114 (1997)
   PUBMED   9126490
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Sanseau,P., Jackson,A., Alderton,R.P., Beck,S., Senger,G.,
            Sheer,D., Kelly,A. and Trowsdale,J.
  TITLE     Cloning and characterization of human phosphatase inhibitor-2
            (IPP-2) sequences
  JOURNAL   Mamm Genome 5 (8), 490-496 (1994)
   PUBMED   7949733
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Helps,N.R., Street,A.J., Elledge,S.J. and Cohen,P.T.
  TITLE     Cloning of the complete coding region for human protein phosphatase
            inhibitor 2 using the two hybrid system and expression of inhibitor
            2 in E. coli
  JOURNAL   FEBS Lett 340 (1-2), 93-98 (1994)
   PUBMED   8119416
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Park,I.K., Roach,P., Bondor,J., Fox,S.P. and DePaoli-Roach,A.A.
  TITLE     Molecular mechanism of the synergistic phosphorylation of
            phosphatase inhibitor-2. Cloning, expression, and site-directed
            mutagenesis of inhibitor-2
  JOURNAL   J Biol Chem 269 (2), 944-954 (1994)
   PUBMED   8288648
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC069213.22.
            
            Summary: Protein phosphatase-1 (PP1) is one of the main eukaryotic
            serine/threonine phosphatases. The protein encoded by this gene
            binds to the catalytic subunit of PP1, strongly inhibiting its
            activity. Ten related pseudogenes have been found throughout the
            human genome. Several splice variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon and  uses an alternate in-frame splice site, compared to
            variant 1. The encoded isoform (3) is shorter than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.185117.1,
                                           SRR1660805.48768.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..179
                     /product="protein phosphatase inhibitor 2 isoform 3"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase inhibitor 2; phosphoprotein
                     phosphatase"
                     /calculated_mol_wt=20184
     Region          45..138
                     /region_name="IPP-2"
                     /note="Protein phosphatase inhibitor 2 (IPP-2); pfam04979"
                     /db_xref="CDD:461504"
     CDS             1..179
                     /gene="PPP1R2"
                     /gene_synonym="IPP-2; IPP2; PPP1R2A"
                     /coded_by="NM_001291505.2:301..840"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:5504"
                     /db_xref="HGNC:HGNC:9288"
                     /db_xref="MIM:601792"
ORIGIN      
        1 maastashrp ikgilknkts ttssmvasae qprgnvdeel skksqkwdem nilatyhpad
       61 kdyglmkide pstpyhrlaa aeglepkyri qeqessgeed sdlspeerek krqfemkrkl
      121 hyneglnikl arqliskdlh dddedeemle tadgesmnte esnqgstpsd qqqnklrss
//
LOCUS       NP_001317189            1980 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel protein type 8 subunit alpha isoform 3 [Homo
            sapiens].
ACCESSION   NP_001317189 XP_011536952
VERSION     NP_001317189.1
DBSOURCE    REFSEQ: accession NM_001330260.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1980)
  AUTHORS   Miralles,R.M., Boscia,A.R., Kittur,S., Hanflink,J.C., Panchal,P.S.,
            Yorek,M.S., Deutsch,T.C.J., Reever,C.M., Vundela,S.R., Wengert,E.R.
            and Patel,M.K.
  TITLE     Parvalbumin interneuron impairment causes synaptic transmission
            deficits and seizures in SCN8A developmental and epileptic
            encephalopathy
  JOURNAL   JCI Insight 9 (20), e181005 (2024)
   PUBMED   39435659
  REMARK    GeneRIF: Parvalbumin interneuron impairment causes synaptic
            transmission deficits and seizures in SCN8A developmental and
            epileptic encephalopathy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1980)
  AUTHORS   Zhang,X., Qiu,S., Yang,L., Li,Y., Xu,N. and Yu,X.
  TITLE     [Clinical features and genetic analysis of five children with
            epilepsies due to variants of SCN8A gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (2), 174-180 (2024)
   PUBMED   38311555
  REMARK    GeneRIF: [Clinical features and genetic analysis of five children
            with epilepsies due to variants of SCN8A gene].
REFERENCE   3  (residues 1 to 1980)
  AUTHORS   Yuan,T., Wang,Y., Jin,Y., Yang,H., Xu,S., Zhang,H., Chen,Q., Li,N.,
            Ma,X., Song,H., Peng,C., Geng,Z., Dong,J., Duan,G., Sun,Q.,
            Yang,Y., Yang,F. and Huang,Z.
  TITLE     Coupling of Slack and NaV1.6 sensitizes Slack to quinidine blockade
            and guides anti-seizure strategy development
  JOURNAL   Elife 12, 87559 (2024)
   PUBMED   38289338
  REMARK    GeneRIF: Coupling of Slack and NaV1.6 sensitizes Slack to quinidine
            blockade and guides anti-seizure strategy development.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1980)
  AUTHORS   Hebbar,M., Al-Taweel,N., Gill,I., Boelman,C., Dean,R.A.,
            Goodchild,S.J., Mezeyova,J., Shuart,N.G., Johnson,J.P. Jr., Lee,J.,
            Michoulas,A., Huh,L.L., Armstrong,L., Connolly,M.B. and Demos,M.K.
  TITLE     Expanding the genotype-phenotype spectrum in SCN8A-related
            disorders
  JOURNAL   BMC Neurol 24 (1), 31 (2024)
   PUBMED   38233770
  REMARK    GeneRIF: Expanding the genotype-phenotype spectrum in SCN8A-related
            disorders.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1980)
  AUTHORS   Chung,K.M., Hack,J., Andrews,J., Galindo-Kelly,M., Schreiber,J.,
            Watkins,J. and Hammer,M.F.
  TITLE     Clinical severity is correlated with age at seizure onset and
            biophysical properties of recurrent gain of function variants
            associated with SCN8A-related epilepsy
  JOURNAL   Epilepsia 64 (12), 3365-3376 (2023)
   PUBMED   37585367
  REMARK    GeneRIF: Clinical severity is correlated with age at seizure onset
            and biophysical properties of recurrent gain of function variants
            associated with SCN8A-related epilepsy.
REFERENCE   6  (residues 1 to 1980)
  AUTHORS   Plummer,N.W., Galt,J., Jones,J.M., Burgess,D.L., Sprunger,L.K.,
            Kohrman,D.C. and Meisler,M.H.
  TITLE     Exon organization, coding sequence, physical mapping, and
            polymorphic intragenic markers for the human neuronal sodium
            channel gene SCN8A
  JOURNAL   Genomics 54 (2), 287-296 (1998)
   PUBMED   9828131
REFERENCE   7  (residues 1 to 1980)
  AUTHORS   Plummer,N.W., McBurney,M.W. and Meisler,M.H.
  TITLE     Alternative splicing of the sodium channel SCN8A predicts a
            truncated two-domain protein in fetal brain and non-neuronal cells
  JOURNAL   J Biol Chem 272 (38), 24008-24015 (1997)
   PUBMED   9295353
REFERENCE   8  (residues 1 to 1980)
  AUTHORS   Genini,M., Schwalbe,P., Scholl,F.A. and Schafer,B.W.
  TITLE     Isolation of genes differentially expressed in human primary
            myoblasts and embryonal rhabdomyosarcoma
  JOURNAL   Int J Cancer 66 (4), 571-577 (1996)
   PUBMED   8635876
REFERENCE   9  (residues 1 to 1980)
  AUTHORS   Burgess,D.L., Kohrman,D.C., Galt,J., Plummer,N.W., Jones,J.M.,
            Spear,B. and Meisler,M.H.
  TITLE     Mutation of a new sodium channel gene, Scn8a, in the mouse mutant
            'motor endplate disease'
  JOURNAL   Nat Genet 10 (4), 461-465 (1995)
   PUBMED   7670495
REFERENCE   10 (residues 1 to 1980)
  AUTHORS   Hammer,M.F., Xia,M. and Schreiber,J.M.
  TITLE     SCN8A-Related Epilepsy and/or Neurodevelopmental Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27559564
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025097.41, AC140060.3,
            AC013421.31 and AC068987.38.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 20, 2016 this sequence version replaced XP_011536952.1.
            
            Summary: This gene encodes a member of the sodium channel alpha
            subunit gene family. The encoded protein forms the ion pore region
            of the voltage-gated sodium channel. This protein is essential for
            the rapid membrane depolarization that occurs during the formation
            of the action potential in excitable neurons. Mutations in this
            gene are associated with cognitive disability, pancerebellar
            atrophy and ataxia. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (3) contains an alternate in-frame
            exon in the 5' coding region, compared to variant 1. Isoforms 1 and
            3 are the same length but differ in their sequence.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154665,
                              SAMN03465403 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000627620.5/ ENSP00000487583.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1980
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..1980
                     /product="sodium channel protein type 8 subunit alpha
                     isoform 3"
                     /note="sodium channel protein type 8 subunit alpha;
                     hNa6/Scn8a voltage-gated sodium channel; voltage-gated
                     sodium channel subunit alpha Nav1.6; sodium channel,
                     voltage gated, type VIII, alpha subunit; voltage-gated
                     sodium channel type VIII alpha protein"
                     /calculated_mol_wt=225137
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          28..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          114..442
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          131..421
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            133..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            159..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            194..211
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            215
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            218..234
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            254..273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:36823201,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:36696443,
                     ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:36696443,
                     ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            326
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (high mannose) asparagine.
                     /evidence=ECO:0000269|PubMed:36696443,
                     ECO:0000269|PubMed:36823201, ECO:0007744|PDB:8FHD,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            388..408
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          446..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            518
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88420; propagated from
                     UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            520
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88420; propagated from
                     UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          546..702
                     /region_name="Na_trans_cytopl"
                     /note="Cytoplasmic domain of voltage-gated Na+ ion
                     channel; pfam11933"
                     /db_xref="CDD:463401"
     Region          568..602
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          735..1007
                     /region_name="II. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          752..965
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            754..772
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            784..803
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            818..837
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            840..857
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            874..892
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            956..976
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          991..1192
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          1107..1148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1180..1495
                     /region_name="III. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1197..1473
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1200..1217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1231..1249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1264..1282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1291..1309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1327..1346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1358
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:36696443,
                     ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1372
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:36696443,
                     ECO:0000269|PubMed:36823201, ECO:0000312|PDB:8FHD,
                     ECO:0007744|PDB:8GZ1, ECO:0007744|PDB:8GZ2; propagated
                     from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1383
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1439..1460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1465..1517
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1479..1482
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Site            1497
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q15858; propagated from
                     UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1504..1801
                     /region_name="IV. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1522..1776
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1524..1541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1553..1571
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1584..1601
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1615..1631
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1651..1668
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Site            1743..1765
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     Region          1894..1915
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          1922..1980
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQD0.1)"
     CDS             1..1980
                     /gene="SCN8A"
                     /gene_synonym="BFIS5; CERIII; CIAT; DEE13; EIEE13; MED;
                     MYOCL2; NaCh6; Nav1.6; PN4"
                     /coded_by="NM_001330260.2:182..6124"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81692.1"
                     /db_xref="GeneID:6334"
                     /db_xref="HGNC:HGNC:10596"
                     /db_xref="MIM:600702"
ORIGIN      
        1 maarllappg pdsfkpftpe slanierria esklkkppka dgshredded skpkpnsdle
       61 agkslpfiyg dipqglvavp ledfdpyylt qktfvvlnrg ktlfrfsatp alyilspfnl
      121 irriaikili hsvfsmiimc tiltncvfmt fsnppdwskn veytftgiyt feslvkiiar
      181 gfcidgftfl rdpwnwldfs vimmayvtef vdlgnvsalr tfrvlralkt isvipglkti
      241 vgaliqsvkk lsdvmiltvf clsvfaligl qlfmgnlrnk cvvwpinfne sylengtkgf
      301 dweeyinnkt nfytvpgmle pllcgnssda gqcpegyqcm kagrnpnygy tsfdtfswaf
      361 lalfrlmtqd ywenlyqltl raagktymif fvlvifvgsf ylvnlilavv amayeeqnqa
      421 tleeaeqkea efkamleqlk kqqeeaqaaa matsagtvse daieeegeeg ggsprsssei
      481 sklssksake rrnrrkkrkq kelsegeekg dpekvfkses edgmrrkafr lpdnrigrkf
      541 simnqsllsi pgspflsrhn skssifsfrg pgrfrdpgse nefaddehst veesegrrds
      601 lfipirarer rssysgysgy sqgsrssrif pslrrsvkrn stvdcngvvs liggpgshig
      661 grllpeatte veikkkgpgs llvsmdqlas ygrkdrinsi msvvtntlve eleesqrkcp
      721 pcwykfantf liwechpywi klkeivnliv mdpfvdlait icivlntlfm amehhpmtpq
      781 fehvlavgnl vftgiftaem flkliamdpy yyfqegwnif dgfivslslm elsladvegl
      841 svlrsfrllr vfklakswpt lnmlikiign svgalgnltl vlaiivfifa vvgmqlfgks
      901 ykecvckinq dcelprwhmh dffhsflivf rvlcgewiet mwdcmevagq amclivfmmv
      961 mvignlvvln lflalllssf sadnlaatdd dgemnnlqis virikkgvaw tklkvhafmq
     1021 ahfkqreade vkpldelyek kancianhtg adihrngdfq kngngttsgi gssvekyiid
     1081 edhmsfinnp nltvrvpiav gesdfenlnt edvssesdpe gskdklddts ssegstidik
     1141 peveevpveq peeyldpdac ftegcvqrfk ccqvnieegl gkswwilrkt cflivehnwf
     1201 etfiifmill ssgalafedi yieqrktirt ileyadkvft yifilemllk wtaygfvkff
     1261 tnawcwldfl ivavslvsli analgyselg aikslrtlra lrplralsrf egmrvvvnal
     1321 vgaipsimnv llvclifwli fsimgvnlfa gkyhycfnet seirfeiedv nnkteceklm
     1381 egnnteirwk nvkinfdnvg agylallqva tfkgwmdimy aavdsrkpde qpkyedniym
     1441 yiyfvifiif gsfftlnlfi gviidnfnqq kkkfggqdif mteeqkkyyn amkklgskkp
     1501 qkpiprplnk iqgivfdfvt qqafdivimm liclnmvtmm vetdtqskqm enilywinlv
     1561 fvifftcecv lkmfalrhyy ftigwnifdf vvvilsivgm fladiiekyf vsptlfrvir
     1621 larigrilrl ikgakgirtl lfalmmslpa lfniglllfl vmfifsifgm snfayvkhea
     1681 giddmfnfet fgnsmiclfq ittsagwdgl llpilnrppd csldkehpgs gfkgdcgnps
     1741 vgifffvsyi iisflivvnm yiaiilenfs vateesadpl seddfetfye iwekfdpdat
     1801 qfieycklad fadalehplr vpkpntieli amdlpmvsgd rihcldilfa ftkrvlgdsg
     1861 eldilrqqme erfvasnpsk vsyepitttl rrkqeevsav vlqrayrghl arrgfickkt
     1921 tsnklenggt hrekkestps taslpsydsv tkpekekqqr aeegrrerak rqkevreskc
//
LOCUS       NP_001356836             580 aa            linear   PRI 20-NOV-2025
DEFINITION  synapsin-3 isoform IIIa [Homo sapiens].
ACCESSION   NP_001356836 XP_011528710
VERSION     NP_001356836.1
DBSOURCE    REFSEQ: accession NM_001369907.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Baris,R.O., Sahin,N., Bilgic,A.D., Ozdemir,C. and Edgunlu,T.G.
  TITLE     Molecular and in silico analyses of SYN III gene variants in autism
            spectrum disorder
  JOURNAL   Ir J Med Sci 192 (6), 2887-2895 (2023)
   PUBMED   37166614
  REMARK    GeneRIF: Molecular and in silico analyses of SYN III gene variants
            in autism spectrum disorder.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Bolat,H., Unsel-Bolat,G., Ozgul,S., Pariltay,E., Tahillioglu,A.,
            Rohde,L.A., Akin,H. and Ercan,E.S.
  TITLE     Investigation of possible associations of the BDNF, SNAP-25 and SYN
            III genes with the neurocognitive measures: BDNF and SNAP-25 genes
            might be involved in attention domain, SYN III gene in executive
            function
  JOURNAL   Nord J Psychiatry 76 (8), 610-615 (2022)
   PUBMED   35077325
  REMARK    GeneRIF: Investigation of possible associations of the BDNF,
            SNAP-25 and SYN III genes with the neurocognitive measures: BDNF
            and SNAP-25 genes might be involved in attention domain, SYN III
            gene in executive function.
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Longhena,F., Faustini,G., Varanita,T., Zaltieri,M., Porrini,V.,
            Tessari,I., Poliani,P.L., Missale,C., Borroni,B., Padovani,A.,
            Bubacco,L., Pizzi,M., Spano,P. and Bellucci,A.
  TITLE     Synapsin III is a key component of alpha-synuclein fibrils in Lewy
            bodies of PD brains
  JOURNAL   Brain Pathol 28 (6), 875-888 (2018)
   PUBMED   29330884
  REMARK    GeneRIF: Synapsin III is a crucial alpha-synuclein interactant and
            a key component of Lewy bodies fibrils in the brain of patients
            affected by Parkinson's disease.
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Porton,B., Ferreira,A., DeLisi,L.E. and Kao,H.T.
  TITLE     A rare polymorphism affects a mitogen-activated protein kinase site
            in synapsin III: possible relationship to schizophrenia
  JOURNAL   Biol Psychiatry 55 (2), 118-125 (2004)
   PUBMED   14732590
  REMARK    GeneRIF: A missense polymorphism, S470N, was identified in the
            synapsin III gene and appeared more frequently in individuals with
            schizophrenia. The site affected by the polymorphism, Ser470, was
            determined to be a substrate for mitogen-activated protein kinase.
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Tsai,M.T., Hung,C.C., Tsai,C.Y., Liu,M.Y., Su,Y.C., Chen,Y.H.,
            Hsiao,K.J. and Chen,C.H.
  TITLE     Mutation analysis of synapsin III gene in schizophrenia
  JOURNAL   Am J Med Genet 114 (1), 79-83 (2002)
   PUBMED   11840510
  REMARK    GeneRIF: Evidence is not in favor of a large effect of synapsin III
            gene in the pathogenesis of schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Hilfiker,S., Stefani,G., Pieribone,V.A.,
            DeSalle,R. and Greengard,P.
  TITLE     Molecular evolution of the synapsin gene family
  JOURNAL   J Exp Zool 285 (4), 360-377 (1999)
   PUBMED   10578110
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Porton,B., Kao,H.T. and Greengard,P.
  TITLE     Characterization of transcripts from the synapsin III gene locus
  JOURNAL   J Neurochem 73 (6), 2266-2271 (1999)
   PUBMED   10582583
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Czernik,A.J., Feng,J., Yiu,G., Haring,M.,
            Benfenati,F. and Greengard,P.
  TITLE     A third member of the synapsin gene family
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4667-4672 (1998)
   PUBMED   9539796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83846.1, Z98256.1, Z82246.2,
            Z80902.2, Z82181.2 and Z71183.2.
            
            On Apr 24, 2019 this sequence version replaced XP_011528710.1.
            
            Summary: This gene is a member of the synapsin gene family.
            Synapsins encode neuronal phosphoproteins which associate with the
            cytoplasmic surface of synaptic vesicles. Family members are
            characterized by common protein domains, and they are implicated in
            synaptogenesis and the modulation of neurotransmitter release,
            suggesting a potential role in several neuropsychiatric diseases.
            The protein encoded by this gene shares the synapsin family domain
            model, with domains A, C, and E exhibiting the highest degree of
            conservation. The protein contains a unique domain J, located
            between domains C and E. Based on this gene's localization to
            22q12.3, a possible schizophrenia susceptibility locus, and the
            established neurobiological roles of the synapsins, this family
            member may represent a candidate gene for schizophrenia. The TIMP3
            gene is located within an intron of this gene and is transcribed in
            the opposite direction. Alternative splicing of this gene results
            in multiple splice variants that encode different isoforms.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.217535.1,
                                           SRR1803613.38599.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..580
                     /product="synapsin-3 isoform IIIa"
                     /note="synapsin-3; cN28H9.2 (synapsin III)"
                     /calculated_mol_wt=63172
     Region          1..29
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and CaMK1.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          19..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          28..90
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          91..399
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          92..191
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          193..395
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Region          <394..536
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          395..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          400..531
                     /region_name="J, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and MAPK.
                     /evidence=ECO:0000269|PubMed:14732590; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70441; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          532..580
                     /region_name="E"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     CDS             1..580
                     /gene="SYN3"
                     /coded_by="NM_001369907.1:250..1992"
                     /note="isoform IIIa is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13908.1"
                     /db_xref="GeneID:8224"
                     /db_xref="HGNC:HGNC:11496"
                     /db_xref="MIM:602705"
ORIGIN      
        1 mnflrrrlsd ssfmanlpng ymtdlqrpds stsspaspam errhpqplaa sfsspgsslf
       61 sslssamkqa pqatsglmep pgpstpivqr prillvidda htdwskyfhg kkvngeieir
      121 veqaefseln laayvtggcm vdmqvvrngt kvvsrsfkpd filvrqhays malgedyrsl
      181 viglqygglp avnslysvyn fcskpwvfsq likifhslgp ekfplveqtf fpnhkpmvta
      241 phfpvvvklg hahagmgkik venqldfqdi tsvvamakty atteafidsk ydiriqkigs
      301 nykaymrtsi sgnwkantgs amleqvamte ryrlwvdscs emfggldica vkavhskdgr
      361 dyiievmdss mpligehvee drqlmadlvv skmsqlpmpg gtapsplrpw apqiksaksp
      421 gqaqlgpqlg qpqprpppqg gprqaqspqp qrsgspsqqr lspqgqqpls pqsgspqqqr
      481 spgspqlsra ssgsspnqas kpgatlasqp rppvqgrsts qqgeeskkpa pphphlnksq
      541 sltnslstsd tsqrgtpsed eakaetirnl rksfaslfsd
//
LOCUS       NP_001276679             410 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydrolipoyl dehydrogenase, mitochondrial isoform 2 [Homo
            sapiens].
ACCESSION   NP_001276679
VERSION     NP_001276679.1
DBSOURCE    REFSEQ: accession NM_001289750.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Lin,J., Wang,G., Cheng,S., Hu,Y., Li,H., Feng,W., Liu,X. and Xu,C.
  TITLE     Pan-Cancer Analysis of the Cuproptosis-Related Gene DLD
  JOURNAL   Mediators Inflamm 2023, 5533444 (2023)
   PUBMED   38077227
  REMARK    GeneRIF: Pan-Cancer Analysis of the Cuproptosis-Related Gene DLD.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Wongkittichote,P., Cuddapah,S.R., Master,S.R., Grange,D.K.,
            Dietzen,D., Roper,S.M. and Ganetzky,R.D.
  TITLE     Biochemical characterization of patients with dihydrolipoamide
            dehydrogenase deficiency
  JOURNAL   JIMD Rep 64 (5), 367-374 (2023)
   PUBMED   37701333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Babady,N.E., Pang,Y.P., Elpeleg,O. and Isaya,G.
  TITLE     Cryptic proteolytic activity of dihydrolipoamide dehydrogenase
  JOURNAL   Proc Natl Acad Sci U S A 104 (15), 6158-6163 (2007)
   PUBMED   17404228
  REMARK    GeneRIF: Certain DLD mutations can simultaneously induce the loss
            of a primary metabolic activity and the gain of a moonlighting
            proteolytic activity thus contributing to the metabolic derangement
            associated with DLD deficiency.
            GeneRIF: Human, mouse, and pig Dld has moonlighting function as a
            protease in addition to its canonical function as a a
            dehydrogenase.
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Ganetzky,R., McCormick,E.M. and Falk,M.J.
  TITLE     Primary Pyruvate Dehydrogenase Complex Deficiency Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34138529
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Quinonez,S.C. and Thoene,J.G.
  TITLE     Dihydrolipoamide Dehydrogenase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25032271
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Johanning,G.L., Morris,J.I., Madhusudhan,K.T., Samols,D. and
            Patel,M.S.
  TITLE     Characterization of the transcriptional regulatory region of the
            human dihydrolipoamide dehydrogenase gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (22), 10964-10968 (1992)
   PUBMED   1332063
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Kume,A., Koyata,H., Sakakibara,T., Ishiguro,Y., Kure,S. and
            Hiraga,K.
  TITLE     The glycine cleavage system. Molecular cloning of the chicken and
            human glycine decarboxylase cDNAs and some characteristics involved
            in the deduced protein structures
  JOURNAL   J Biol Chem 266 (5), 3323-3329 (1991)
   PUBMED   1993704
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Scherer,S.W., Otulakowski,G., Robinson,B.H. and Tsui,L.C.
  TITLE     Localization of the human dihydrolipoamide dehydrogenase gene (DLD)
            to 7q31----q32
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 176-177 (1991)
   PUBMED   2055113
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC354209.1, AK295080.1 and
            AC005046.3.
            
            Summary: This gene encodes a member of the class-I pyridine
            nucleotide-disulfide oxidoreductase family. The encoded protein has
            been identified as a moonlighting protein based on its ability to
            perform mechanistically distinct functions. In homodimeric form,
            the encoded protein functions as a dehydrogenase and is found in
            several multi-enzyme complexes that regulate energy metabolism.
            However, as a monomer, this protein can function as a protease.
            Mutations in this gene have been identified in patients with
            E3-deficient maple syrup urine disease and lipoamide dehydrogenase
            deficiency. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (2) lacks part of the 5' coding
            region, and uses a downstream start codon, compared to variant 1.
            The encoded isoform (2) has a shorter N-terminus, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.165809.1,
                                           SRR1803616.138276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142363, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            multifunctional gene product(s)    :: PMID: 17404228
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..410
                     /product="dihydrolipoyl dehydrogenase, mitochondrial
                     isoform 2"
                     /EC_number="1.8.1.4"
                     /note="E3 component of pyruvate dehydrogenase complex,
                     2-oxo-glutarate complex, branched chain keto acid
                     dehydrogenase complex; dihydrolipoyl dehydrogenase,
                     mitochondrial; glycine cleavage system protein L;
                     lipoamide reductase; lipoamide dehydrogenase; lipoyl
                     dehydrogenase; diaphorase; glycine cleavage system L
                     protein; epididymis secretory sperm binding protein;
                     pyruvate dehydrogenase complex subunit E3, 2-oxo-glutarate
                     complex, branched chain keto acid dehydrogenase complex,
                     glycine cleavage system protein L"
                     /calculated_mol_wt=43456
     Region          5..402
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
     CDS             1..410
                     /gene="DLD"
                     /gene_synonym="DLDD; DLDH; E3; GCSL; LAD; OGDC-E3; PHE3"
                     /coded_by="NM_001289750.1:293..1525"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:1738"
                     /db_xref="HGNC:HGNC:2898"
                     /db_xref="MIM:238331"
ORIGIN      
        1 mahgkdfasr giemsevrln ldkmmeqkst avkaltggia hlfkqnkvvh vngygkitgk
       61 nqvtatkadg gtqvidtkni liatgsevtp fpgitidedt ivsstgalsl kkvpekmvvi
      121 gagvigvelg svwqrlgadv taveflghvg gvgidmeisk nfqrilqkqg fkfklntkvt
      181 gatkksdgki dvsieaasgg kaevitcdvl lvcigrrpft knlgleelgi eldprgripv
      241 ntrfqtkipn iyaigdvvag pmlahkaede giicvegmag gavhidyncv psviythpev
      301 awvgkseeql keegieykvg kfpfaansra ktnadtdgmv kilgqkstdr vlgahilgpg
      361 agemvneaal aleygasced iarvchahpt lseafreanl aasfgksinf
//
LOCUS       NP_542784                214 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein uL16-like [Homo sapiens].
ACCESSION   NP_542784
VERSION     NP_542784.1
DBSOURCE    REFSEQ: accession NM_080746.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Tu,C., Meng,L., Nie,H., Yuan,S., Wang,W., Du,J., Lu,G., Lin,G. and
            Tan,Y.Q.
  TITLE     A homozygous RPL10L missense mutation associated with male factor
            infertility and severe oligozoospermia
  JOURNAL   Fertil Steril 113 (3), 561-568 (2020)
   PUBMED   32111475
  REMARK    GeneRIF: A homozygous RPL10L missense mutation associated with male
            factor infertility and severe oligozoospermia.
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Liu,J., Li,R., Liao,X. and Jiang,W.
  TITLE     Comprehensive Bioinformatic Analysis Genes Associated to the
            Prognosis of Liposarcoma
  JOURNAL   Med Sci Monit 24, 7329-7339 (2018)
   PUBMED   30317246
  REMARK    GeneRIF: The Cox regression model revealed that only NIP7, RPL10L,
            and MCM2 exhibited significant correlation with distant
            recurrence-free survival in liposarcoma in the GSE30929 dataset,
            and the regression coefficients were -0.676, -0.703, and 0.868,
            respectively
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Rohozinski,J., Anderson,M.L., Broaddus,R.E., Edwards,C.L. and
            Bishop,C.E.
  TITLE     Spermatogenesis associated retrogenes are expressed in the human
            ovary and ovarian cancers
  JOURNAL   PLoS One 4 (3), e5064 (2009)
   PUBMED   19333399
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Balasubramanian,S., Zheng,D., Liu,Y.J., Fang,G., Frankish,A.,
            Carriero,N., Robilotto,R., Cayting,P. and Gerstein,M.
  TITLE     Comparative analysis of processed ribosomal protein pseudogenes in
            four mammalian genomes
  JOURNAL   Genome Biol 10 (1), R2 (2009)
   PUBMED   19123937
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Uechi,T., Maeda,N., Tanaka,T. and Kenmochi,N.
  TITLE     Functional second genes generated by retrotransposition of the
            X-linked ribosomal protein genes
  JOURNAL   Nucleic Acids Res 30 (24), 5369-5375 (2002)
   PUBMED   12490704
REFERENCE   10 (residues 1 to 214)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Pseudogene.org. The reference sequence was
            derived from AL591768.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein sharing sequence similarity
            with ribosomal protein L10. It is not currently known whether the
            encoded protein is a functional ribosomal protein or whether it has
            evolved a function that is independent of the ribosome. This gene
            is intronless. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC066312.1, SRR5189667.193114.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298283.5/ ENSP00000298283.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.2"
     Protein         1..214
                     /product="ribosomal protein uL16-like"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10-like; large ribosomal
                     subunit protein uL16-like"
                     /calculated_mol_wt=24388
     Region          1..209
                     /region_name="PTZ00173"
                     /note="60S ribosomal protein L10; Provisional"
                     /db_xref="CDD:185498"
     Site            order(41,43..44,47,63..64,67,70,74,77,88..90,92,94,98..99,
                     115..119,133,153..154,157..158)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            56..57
                     /site_type="other"
                     /note="5S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            order(68..70,73..74)
                     /site_type="other"
                     /note="putative antibiotic binding site [chemical
                     binding]"
                     /db_xref="CDD:238714"
     Site            order(77,85..86,88,139)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     Site            order(113..114,117..118)
                     /site_type="other"
                     /note="L27 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     CDS             1..214
                     /gene="RPL10L"
                     /gene_synonym="RPL10_5_1358; SPGF63"
                     /coded_by="NM_080746.3:46..690"
                     /db_xref="CCDS:CCDS32071.1"
                     /db_xref="GeneID:140801"
                     /db_xref="HGNC:HGNC:17976"
                     /db_xref="MIM:619655"
ORIGIN      
        1 mgrrparcyr ycknkpypks rfcrgvpdak irifdlgrkk akvdefplgg hmvsdeyeql
       61 ssealeaari cankymvksc grdgfhmrvr lhpfhvirin kmlscagadr lqtgmrgafg
      121 kpqgtvarvh igqvimsirt klqneehvie alrrakfkfp grqkihiskk wgftkfnade
      181 fedmvakkcl ipdgcgvkyv pshgpldkwr vlhs
//
LOCUS       NP_054862                290 aa            linear   PRI 20-NOV-2025
DEFINITION  programmed cell death 1 ligand 1 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_054862
VERSION     NP_054862.1
DBSOURCE    REFSEQ: accession NM_014143.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Cheng,X., Veverka,V., Radhakrishnan,A., Waters,L.C., Muskett,F.W.,
            Morgan,S.H., Huo,J., Yu,C., Evans,E.J., Leslie,A.J., Griffiths,M.,
            Stubberfield,C., Griffin,R., Henry,A.J., Jansson,A., Ladbury,J.E.,
            Ikemizu,S., Carr,M.D. and Davis,S.J.
  TITLE     Structure and interactions of the human programmed cell death 1
            receptor
  JOURNAL   J Biol Chem 288 (17), 11771-11785 (2013)
   PUBMED   23417675
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Amarnath,S., Costanzo,C.M., Mariotti,J., Ullman,J.L., Telford,W.G.,
            Kapoor,V., Riley,J.L., Levine,B.L., June,C.H., Fong,T., Warner,N.L.
            and Fowler,D.H.
  TITLE     Regulatory T cells and human myeloid dendritic cells promote
            tolerance via programmed death ligand-1
  JOURNAL   PLoS Biol 8 (2), e1000302 (2010)
   PUBMED   20126379
  REMARK    GeneRIF: Human Tregs can promote immune suppression via DC
            modulation through PD-L1 up-regulation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Lin,D.Y., Tanaka,Y., Iwasaki,M., Gittis,A.G., Su,H.P., Mikami,B.,
            Okazaki,T., Honjo,T., Minato,N. and Garboczi,D.N.
  TITLE     The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of
            antibodies and T cell receptors
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 3011-3016 (2008)
   PUBMED   18287011
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Trabattoni,D., Saresella,M., Biasin,M., Boasso,A., Piacentini,L.,
            Ferrante,P., Dong,H., Maserati,R., Shearer,G.M., Chen,L. and
            Clerici,M.
  TITLE     B7-H1 is up-regulated in HIV infection and is a novel surrogate
            marker of disease progression
  JOURNAL   Blood 101 (7), 2514-2520 (2003)
   PUBMED   12468426
  REMARK    GeneRIF: up-regulation in HIV infection, relation to disease
            progression, and possible role in AIDS progression
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Brown,J.A., Dorfman,D.M., Ma,F.R., Sullivan,E.L., Munoz,O.,
            Wood,C.R., Greenfield,E.A. and Freeman,G.J.
  TITLE     Blockade of programmed death-1 ligands on dendritic cells enhances
            T cell activation and cytokine production
  JOURNAL   J Immunol 170 (3), 1257-1266 (2003)
   PUBMED   12538684
  REMARK    GeneRIF: Blockade of PD-L1 during T cell responses initiated by
            allogenic dendritic cells increases T cell proliferation and
            cytokine production, showing that PD-L1 functions to inhibit T cell
            activation.
REFERENCE   7  (residues 1 to 290)
  AUTHORS   Mazanet,M.M. and Hughes,C.C.
  TITLE     B7-H1 is expressed by human endothelial cells and suppresses T cell
            cytokine synthesis
  JOURNAL   J Immunol 169 (7), 3581-3588 (2002)
   PUBMED   12244148
  REMARK    GeneRIF: B7-H1 is inducible on human endothelial cells by IFN-gamma
            both in vitro and in vivo; blocking its interaction with its
            receptor (PD-1) on T cells augments T cell cytokine synthesis.
REFERENCE   8  (residues 1 to 290)
  AUTHORS   Dong,H., Strome,S.E., Salomao,D.R., Tamura,H., Hirano,F.,
            Flies,D.B., Roche,P.C., Lu,J., Zhu,G., Tamada,K., Lennon,V.A.,
            Celis,E. and Chen,L.
  TITLE     Tumor-associated B7-H1 promotes T-cell apoptosis: a potential
            mechanism of immune evasion
  JOURNAL   Nat Med 8 (8), 793-800 (2002)
   PUBMED   12091876
  REMARK    GeneRIF: Cancer cell-associated B7-H1 increases apoptosis of
            antigen-specific human T-cell clones in vitro
            Erratum:[Nat Med 2002 Sep;8(9):1039]
REFERENCE   9  (residues 1 to 290)
  AUTHORS   Freeman,G.J., Long,A.J., Iwai,Y., Bourque,K., Chernova,T.,
            Nishimura,H., Fitz,L.J., Malenkovich,N., Okazaki,T., Byrne,M.C.,
            Horton,H.F., Fouser,L., Carter,L., Ling,V., Bowman,M.R.,
            Carreno,B.M., Collins,M., Wood,C.R. and Honjo,T.
  TITLE     Engagement of the PD-1 immunoinhibitory receptor by a novel B7
            family member leads to negative regulation of lymphocyte activation
  JOURNAL   J Exp Med 192 (7), 1027-1034 (2000)
   PUBMED   11015443
REFERENCE   10 (residues 1 to 290)
  AUTHORS   Dong,H., Zhu,G., Tamada,K. and Chen,L.
  TITLE     B7-H1, a third member of the B7 family, co-stimulates T-cell
            proliferation and interleukin-10 secretion
  JOURNAL   Nat Med 5 (12), 1365-1369 (1999)
   PUBMED   10581077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314567.1, AL162253.17 and
            AI826502.1.
            
            Summary: This gene encodes an immune inhibitory receptor ligand
            that is expressed by hematopoietic and non-hematopoietic cells,
            such as T cells and B cells and various types of tumor cells. The
            encoded protein is a type I transmembrane protein that has
            immunoglobulin V-like and C-like domains. Interaction of this
            ligand with its receptor inhibits T-cell activation and cytokine
            production. During infection or inflammation of normal tissue, this
            interaction is important for preventing autoimmunity by maintaining
            homeostasis of the immune response. In tumor microenvironments,
            this interaction provides an immune escape for tumor cells through
            cytotoxic T-cell inactivation. Expression of this gene in tumor
            cells is considered to be prognostic in many types of human
            malignancies, including colon cancer and renal cell carcinoma.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314567.1, SRR1660803.237105.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381577.4/ ENSP00000370989.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.1"
     Protein         1..290
                     /product="programmed cell death 1 ligand 1 isoform a
                     precursor"
                     /note="CD274 antigen; programmed cell death 1 ligand 1; B7
                     homolog 1; PDCD1 ligand 1"
                     /calculated_mol_wt=31020
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2274
     mat_peptide     19..290
                     /product="programmed cell death 1 ligand 1 isoform a"
                     /calculated_mol_wt=31020
     Region          21..130
                     /region_name="IgV_PDl1"
                     /note="Immunoglobulin Variable (IgV) domain of Programmed
                     death ligand 1 (PD-L1); cd20947"
                     /db_xref="CDD:409539"
     Region          21..41
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409539"
     Region          21..24
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409539"
     Region          26..31
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409539"
     Region          33..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409539"
     Site            35
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ7.1)"
     Region          42..53
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409539"
     Region          53..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409539"
     Region          54..62
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409539"
     Region          63..74
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409539"
     Region          63..68
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409539"
     Region          70..74
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409539"
     Region          75..116
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409539"
     Region          84..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409539"
     Region          96..103
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409539"
     Region          107..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409539"
     Region          117..121
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409539"
     Region          121..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409539"
     Region          122..130
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409539"
     Region          138..211
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          151..155
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          164..173
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ7.1)"
     Region          195..199
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ7.1)"
     Region          206..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            219
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ7.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ7.1)"
     CDS             1..290
                     /gene="CD274"
                     /gene_synonym="ADMIO5; B7-H; B7H1; hPD-L1; PD-L1; PDCD1L1;
                     PDCD1LG1; PDL1"
                     /coded_by="NM_014143.4:70..942"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6464.1"
                     /db_xref="GeneID:29126"
                     /db_xref="HGNC:HGNC:17635"
                     /db_xref="MIM:605402"
ORIGIN      
        1 mrifavfifm tywhllnaft vtvpkdlyvv eygsnmtiec kfpvekqldl aalivyweme
       61 dkniiqfvhg eedlkvqhss yrqrarllkd qlslgnaalq itdvklqdag vyrcmisygg
      121 adykritvkv napynkinqr ilvvdpvtse heltcqaegy pkaeviwtss dhqvlsgktt
      181 ttnskreekl fnvtstlrin tttneifyct frrldpeenh taelvipelp lahppnerth
      241 lvilgaillc lgvaltfifr lrkgrmmdvk kcgiqdtnsk kqsdthleet
//
LOCUS       NP_001317007            1507 aa            linear   PRI 20-NOV-2025
DEFINITION  neurexin-1 isoform alpha4 precursor [Homo sapiens].
ACCESSION   NP_001317007 XP_011531473
VERSION     NP_001317007.1
DBSOURCE    REFSEQ: accession NM_001330078.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1507)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1507)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1507)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1507)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 1507)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 1507)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 1507)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 1507)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 1507)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 1507)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3, AC009234.3,
            AC007462.3, AC068725.5, AC069550.4 and AC078994.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 16, 2016 this sequence version replaced XP_011531473.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401669.7/ ENSP00000385017.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..1507
                     /product="neurexin-1 isoform alpha4 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=162368
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     Region          307..446
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          503..652
                     /region_name="LamG"
                     /note="Laminin G domain; smart00282"
                     /db_xref="CDD:214598"
     Region          680..713
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain, present in a large
                     number of membrane-bound and extracellular (mostly animal)
                     proteins. Many of these proteins require calcium for their
                     biological function and calcium-binding sites have been
                     found to be located at the...; cd00054"
                     /db_xref="CDD:238011"
     Region          746..876
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          933..1061
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1156..1304
                     /region_name="Laminin_G_2"
                     /note="Laminin G domain; pfam02210"
                     /db_xref="CDD:460494"
     Region          1452..1470
                     /region_name="4.1m"
                     /note="putative band 4.1 homologues' binding motif;
                     smart00294"
                     /db_xref="CDD:128590"
     CDS             1..1507
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330078.2:1074..5597"
                     /note="isoform alpha4 precursor is encoded by transcript
                     variant alpha4"
                     /db_xref="CCDS:CCDS82451.1"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqedn nveglahlmm gdqgkskgke eyiatfkgse yfcydlsqnp
      301 iqsssdeitl sfktlqrngl mlhtgksady vnlalkngav slvinlgsga fealvepvng
      361 kfndnawhdv kvtrnlrqhs gighamvtis vdgiltttgy tqedytmlgs ddffyvggsp
      421 stadlpgspv snnfmgclke vvyknndvrl elsrlakqgd pkmkihgvva fkcenvatld
      481 pitfetpesf islpkwnakk tgsisfdfrt tepnglilfs hgkprhqkda khpqmikvdf
      541 faiemldghl yllldmgsgt ikikallkkv ndgewyhvdf qrdgrsgtis vntlrtpyta
      601 pgeseildld delylgglpe nkaglvfpte vwtallnygy vgcirdlfid gqskdirqma
      661 evqstagvkp scsketakpc lsnpcknngm crdgwnryvc dcsgtgylgr scereatvls
      721 ydgsmfmkiq lpvvmhteae dvslrfrsqr aygilmatts rdsadtlrle ldagrvkltv
      781 nldcirincn sskgpetlfa gynlndnewh tvrvvrrgks lkltvddqqa mtgqmagdht
      841 rlefhnietg iiterrylss vpsnfighlq sltfngmayi dlckngdidy celnarfgfr
      901 niiadpvtfk tkssyvalat lqaytsmhlf fqfkttsldg lilynsgdgn dfivvelvkg
      961 ylhyvfdlgn ganlikgssn kplndnqwhn vmisrdtsnl htvkidtkit tqitagarnl
     1021 dlksdlyigg vaketykslp klvhakegfq gclasvdlng rlpdlisdal fcngqiergc
     1081 egpsttcqed scsnqgvclq qwdgfscdcs mtsfsgplcn dpgttyifsk gggqitykwp
     1141 pndrpstrad rlaigfstvq keavlvrvds ssglgdylel hihqgkigvk fnvgtddiai
     1201 eesnaiindg kyhvvrftrs ggnatlqvds wpvierypag nndnerlaia rqripyrlgr
     1261 vvdewlldkg rqltifnsqa tiiiggkeqg qpfqgqlsgl yynglkvlnm aaendaniai
     1321 vgnvrlvgev pssmttesta tamqsemsts imettttlat starrgkppt kepisqttdd
     1381 ilvasaecps ddedidpcep ssgglanptr aggrepypgs aeviressst tgmvvgivaa
     1441 aalcililly amykyrnrde gsyhvdesrn yisnsaqsng avvkekqpss akssnknkkn
     1501 kdkeyyv
//
LOCUS       NP_001121691             296 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription cofactor vestigial-like protein 4 isoform a [Homo
            sapiens].
ACCESSION   NP_001121691
VERSION     NP_001121691.1
DBSOURCE    REFSEQ: accession NM_001128219.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Wang,Z., Quan,Y., Hu,M., Xu,Y., Chen,Y., Jin,P., Ma,J., Chen,X.,
            Fan,J., Fan,X., Gong,Y., Li,M. and Wang,Y.
  TITLE     VGLL4-TEAD1 promotes vascular smooth muscle cell differentiation
            from human pluripotent stem cells via TET2
  JOURNAL   J Mol Cell Cardiol 176, 21-32 (2023)
   PUBMED   36657637
  REMARK    GeneRIF: VGLL4-TEAD1 promotes vascular smooth muscle cell
            differentiation from human pluripotent stem cells via TET2.
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Geng,H., Liu,G., Hu,J., Li,J., Wang,D., Zou,S. and Xu,X.
  TITLE     HOXB13 suppresses proliferation, migration and invasion, and
            promotes apoptosis of gastric cancer cells through transcriptional
            activation of VGLL4 to inhibit the involvement of TEAD4 in the
            Hippo signaling pathway
  JOURNAL   Mol Med Rep 24 (4) (2021)
   PUBMED   34396425
  REMARK    GeneRIF: HOXB13 suppresses proliferation, migration and invasion,
            and promotes apoptosis of gastric cancer cells through
            transcriptional activation of VGLL4 to inhibit the involvement of
            TEAD4 in the Hippo signaling pathway.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Mesrouze,Y., Meyerhofer,M., Zimmermann,C., Fontana,P., Erdmann,D.
            and Chene,P.
  TITLE     Biochemical properties of VGLL4 from Homo sapiens and Tgi from
            Drosophila melanogaster and possible biological implications
  JOURNAL   Protein Sci 30 (9), 1871-1881 (2021)
   PUBMED   34075638
  REMARK    GeneRIF: Biochemical properties of VGLL4 from Homo sapiens and Tgi
            from Drosophila melanogaster and possible biological implications.
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Mickle,M., Adhikary,G., Shrestha,S., Xu,W. and Eckert,R.L.
  TITLE     VGLL4 inhibits YAP1/TEAD signaling to suppress the epidermal
            squamous cell carcinoma cancer phenotype
  JOURNAL   Mol Carcinog 60 (7), 497-507 (2021)
   PUBMED   34004031
  REMARK    GeneRIF: VGLL4 inhibits YAP1/TEAD signaling to suppress the
            epidermal squamous cell carcinoma cancer phenotype.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Jin,H.S., Park,H.S., Shin,J.H., Kim,D.H., Jun,S.H., Lee,C.J. and
            Lee,T.H.
  TITLE     A novel inhibitor of apoptosis protein (IAP)-interacting protein,
            Vestigial-like (Vgl)-4, counteracts apoptosis-inhibitory function
            of IAPs by nuclear sequestration
  JOURNAL   Biochem Biophys Res Commun 412 (3), 454-459 (2011)
   PUBMED   21839727
  REMARK    GeneRIF: Vgl-4 may play a role in the apoptotic pathways by
            regulating translocation of IAPs between different cell
            compartments.
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Teng,A.C., Kuraitis,D., Deeke,S.A., Ahmadi,A., Dugan,S.G.,
            Cheng,B.L., Crowson,M.G., Burgon,P.G., Suuronen,E.J., Chen,H.H. and
            Stewart,A.F.
  TITLE     IRF2BP2 is a skeletal and cardiac muscle-enriched
            ischemia-inducible activator of VEGFA expression
  JOURNAL   FASEB J 24 (12), 4825-4834 (2010)
   PUBMED   20702774
  REMARK    GeneRIF: IRF2BP2 was identifies as a novel VGLL4 partner.
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Chen,H.H., Mullett,S.J. and Stewart,A.F.
  TITLE     Vgl-4, a novel member of the vestigial-like family of transcription
            cofactors, regulates alpha1-adrenergic activation of gene
            expression in cardiac myocytes
  JOURNAL   J Biol Chem 279 (29), 30800-30806 (2004)
   PUBMED   15140898
  REMARK    GeneRIF: Vgl-4 modulates the activity of TEF-1 factors and
            counteracts alpha1-adrenergic activation of gene expression in
            cardiac myocytes
            GeneRIF: A transcriptional cofactor of transcriptional enhancer
            factor-1 (TEF-1) transcription factors.  Interacts with TEF-1
            factors through 2 TDU (tondu) motifs.  Controls gene expression in
            cardiac myocytes.
            GeneRIF: This gene is named Vestigial-like 4, to distinguish it
            from 3 previously described genes Vgl-1, Vgl-2 and Vgl-3. Contains
            2 motifs, found in the Drosophila transcription cofactor Vestigial,
            that interact with the TEF-1 family of transcription factors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA386938.1, DR159250.1, DA383197.1, D50911.3 and BU682809.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.19963.1,
                                           SRR11853561.20246.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430365.7/ ENSP00000404251.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3-p25.2"
     Protein         1..296
                     /product="transcription cofactor vestigial-like protein 4
                     isoform a"
                     /note="Vestigial-like 4; transcription cofactor
                     vestigial-like protein 4; vestigial like 4"
                     /calculated_mol_wt=31734
     Region          8..230
                     /region_name="VGLL4"
                     /note="Transcription cofactor vestigial-like protein 4;
                     pfam15245"
                     /db_xref="CDD:464585"
     Region          240..255
                     /region_name="TDU"
                     /note="Short repeats in human TONDU, fly vestigial and
                     other proteins; smart00711"
                     /db_xref="CDD:197839"
     CDS             1..296
                     /gene="VGLL4"
                     /gene_synonym="VGL-4"
                     /coded_by="NM_001128219.3:398..1288"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46754.1"
                     /db_xref="GeneID:9686"
                     /db_xref="HGNC:HGNC:28966"
                     /db_xref="MIM:618692"
ORIGIN      
        1 mlfmkmdlln yqyldkmnnn igilcyegea alrgepriqt lpvasalssh rtgpppisps
       61 krkfsmepgd edldcdndhv skmsrifnph lnktangdcr rdprersrsp ieravaptms
      121 lhgshlytsl pslgleqpla ltknsldasr paglsptltp gerqqnrpsv itcasagarn
      181 cnlshcpiah sgcaapgpas yrrppsaatt cdpvveehfr rslgknykep epapnsvsit
      241 gsvddhfaka lgdtwlqika akdgassspe sasrrgqpas psahmvshsh spsvvs
//
LOCUS       NP_705931                440 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear pore complex protein Nup50 isoform a [Homo sapiens].
ACCESSION   NP_705931
VERSION     NP_705931.1
DBSOURCE    REFSEQ: accession NM_153645.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 440)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Smitherman,M., Lee,K., Swanger,J., Kapur,R. and Clurman,B.E.
  TITLE     Characterization and targeted disruption of murine Nup50, a
            p27(Kip1)-interacting component of the nuclear pore complex
  JOURNAL   Mol Cell Biol 20 (15), 5631-5642 (2000)
   PUBMED   10891500
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Guan,T., Kehlenbach,R.H., Schirmer,E.C., Kehlenbach,A., Fan,F.,
            Clurman,B.E., Arnheim,N. and Gerace,L.
  TITLE     Nup50, a nucleoplasmically oriented nucleoporin with a role in
            nuclear protein export
  JOURNAL   Mol Cell Biol 20 (15), 5619-5630 (2000)
   PUBMED   10891499
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Trichet,V., Shkolny,D., Dunham,I., Beare,D. and McDermid,H.E.
  TITLE     Mapping and complex expression pattern of the human NPAP60L
            nucleoporin gene
  JOURNAL   Cytogenet Cell Genet 85 (3-4), 221-226 (1999)
   PUBMED   10449902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z82243.1, BC028125.1 and
            AL008718.23.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. The protein encoded by this gene is a
            member of the FG-repeat containing nucleoporins that functions as a
            soluble cofactor in importin-alpha:beta-mediated nuclear protein
            import. Pseudogenes of this gene are found on chromosomes 5, 6, and
            14. Two transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region compared to variant 2. The resulting isoform (a) is
            shorter at the N-terminus compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..440
                     /product="nuclear pore complex protein Nup50 isoform a"
                     /note="nuclear pore-associated protein 60L; nuclear pore
                     complex protein Nup50; nucleoporin Nup50; 50 kDa
                     nucleoporin; nucleoporin 50kD; nucleoporin 50kDa"
                     /calculated_mol_wt=46732
     Region          <2..39
                     /region_name="NUP50"
                     /note="NUP50 (Nucleoporin 50 kDa); pfam08911"
                     /db_xref="CDD:462629"
     Region          322..438
                     /region_name="RanBD_NUP50"
                     /note="Nucleoporin 50 Ran-binding domain; cd13170"
                     /db_xref="CDD:269991"
     Site            order(336,338..340,344..348,364,366,368..369,374..376,379,
                     381,385,389,397,399,416,420)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:269991"
     CDS             1..440
                     /gene="NUP50"
                     /gene_synonym="NPAP60; NPAP60L"
                     /coded_by="NM_153645.2:373..1695"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14063.1"
                     /db_xref="GeneID:10762"
                     /db_xref="HGNC:HGNC:8065"
                     /db_xref="MIM:604646"
ORIGIN      
        1 maseevlknr aikkakrrnv gfesdtggaf kgfkglvvps gggrfsgfgs gaggkplegl
       61 sngnnitsap pfasakaaad pkvafgslaa ngpttlvdkv snpktngdsq qpsssglass
      121 kacvgnayhk qlaalncsvr dwivkhvntn plcdltpifk dyekylanie qqhgnsgrns
      181 esesnkvaae tqspslfgst klqqestflf hgnktedtpd kkmevasekk tdpsslgats
      241 asfnfgkkvd ssvlgslssv pltgfsfspg nsslfgkdtt qskpvsspfp tkplegqaeg
      301 dsgeckggde eendeppkvv vtevkeedaf yskkcklfyk kdnefkekgi gtlhlkptan
      361 qktqllvrad tnlgnillnv lippnmpctr tgknnvlivc vpnppidekn atmpvtmlir
      421 vktsedadel hkillekkda
//
LOCUS       NP_001305169            2063 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor coactivator 6 isoform 1 [Homo sapiens].
ACCESSION   NP_001305169 XP_011527027
VERSION     NP_001305169.1
DBSOURCE    REFSEQ: accession NM_001318240.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2063)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2063)
  AUTHORS   Lee,K.G., Hong,B.K., Lee,S., Lee,N., Kim,S.W., Kim,D. and Kim,W.U.
  TITLE     Nuclear receptor coactivator 6 is a critical regulator of NLRP3
            inflammasome activation and gouty arthritis
  JOURNAL   Cell Mol Immunol 21 (3), 227-244 (2024)
   PUBMED   38195836
  REMARK    GeneRIF: Nuclear receptor coactivator 6 is a critical regulator of
            NLRP3 inflammasome activation and gouty arthritis.
REFERENCE   3  (residues 1 to 2063)
  AUTHORS   Fang,Y., Xu,Y., Liao,W., Ji,T., Yu,L., Li,L., Pan,M. and Yang,D.
  TITLE     Multiomics analyses and machine learning of nuclear receptor
            coactivator 6 reveal its essential role in hepatocellular carcinoma
  JOURNAL   Cancer Sci 114 (1), 75-90 (2023)
   PUBMED   36086920
  REMARK    GeneRIF: Multiomics analyses and machine learning of nuclear
            receptor coactivator 6 reveal its essential role in hepatocellular
            carcinoma.
REFERENCE   4  (residues 1 to 2063)
  AUTHORS   Watanabe,N., Kawagoe,J., Sugiyama,A., Takehara,I., Ohta,T. and
            Nagase,S.
  TITLE     Nuclear receptor coactivator-6 is essential for the morphological
            change of human uterine stromal cell decidualization via regulating
            actin fiber reorganization
  JOURNAL   Mol Reprod Dev 89 (4), 165-174 (2022)
   PUBMED   35384116
  REMARK    GeneRIF: Nuclear receptor coactivator-6 is essential for the
            morphological change of human uterine stromal cell decidualization
            via regulating actin fiber reorganization.
REFERENCE   5  (residues 1 to 2063)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 2063)
  AUTHORS   Caira,F., Antonson,P., Pelto-Huikko,M., Treuter,E. and
            Gustafsson,J.A.
  TITLE     Cloning and characterization of RAP250, a novel nuclear receptor
            coactivator
  JOURNAL   J Biol Chem 275 (8), 5308-5317 (2000)
   PUBMED   10681503
REFERENCE   7  (residues 1 to 2063)
  AUTHORS   Lee,S.K., Anzick,S.L., Choi,J.E., Bubendorf,L., Guan,X.Y.,
            Jung,Y.K., Kallioniemi,O.P., Kononen,J., Trent,J.M., Azorsa,D.,
            Jhun,B.H., Cheong,J.H., Lee,Y.C., Meltzer,P.S. and Lee,J.W.
  TITLE     A nuclear factor, ASC-2, as a cancer-amplified transcriptional
            coactivator essential for ligand-dependent transactivation by
            nuclear receptors in vivo
  JOURNAL   J Biol Chem 274 (48), 34283-34293 (1999)
   PUBMED   10567404
REFERENCE   8  (residues 1 to 2063)
  AUTHORS   Guan,X.Y., Xu,J., Anzick,S.L., Zhang,H., Trent,J.M. and
            Meltzer,P.S.
  TITLE     Hybrid selection of transcribed sequences from microdissected DNA:
            isolation of genes within amplified region at 20q11-q13.2 in breast
            cancer
  JOURNAL   Cancer Res 56 (15), 3446-3450 (1996)
   PUBMED   8758910
REFERENCE   9  (residues 1 to 2063)
  AUTHORS   Carney,J.P., McKnight,C., VanEpps,S. and Kelley,M.R.
  TITLE     Random rapid amplification of cDNA ends (RRACE) allows for cloning
            of multiple novel human cDNA fragments containing (CAG)n repeats
  JOURNAL   Gene 155 (2), 289-292 (1995)
   PUBMED   7536696
REFERENCE   10 (residues 1 to 2063)
  AUTHORS   Estey,A., Kemp,M., Allison,S. and Lamb,C.
  TITLE     Evaluation of a patient information booklet
  JOURNAL   J Nurs Staff Dev 9 (6), 278-282 (1993)
   PUBMED   8263591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049709.18, AF208227.1 and
            AL109824.24.
            
            On Dec 30, 2015 this sequence version replaced XP_011527027.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that can interact with nuclear hormone receptors to
            enhance their transcriptional activator functions. This protein has
            been shown to be involved in the hormone-dependent coactivation of
            several receptors, including prostanoid, retinoid, vitamin D3,
            thyroid hormone, and steroid receptors. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longer isoform (1, also known as
            NCOA6-alpha). Variants 1 and 3 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF208227.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2063
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.22"
     Protein         1..2063
                     /product="nuclear receptor coactivator 6 isoform 1"
                     /note="amplified in breast cancer-3 protein; activating
                     signal cointegrator-2; nuclear receptor coactivator
                     RAP250; peroxisome proliferator-activated receptor
                     interacting protein; thyroid hormone receptor binding
                     protein; NRC RAP250; PPAR-interacting protein; amplified
                     in breast cancer protein 3; nuclear receptor-activating
                     protein, 250 kDa; cancer-amplified transcriptional
                     coactivator ASC-2"
                     /calculated_mol_wt=219015
     Region          1..1310
                     /region_name="NCOA1-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..1057
                     /region_name="CREBBP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1..928
                     /region_name="TBP/GTF2A-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          48..190
                     /region_name="Nucleic_acid_bd"
                     /note="Putative nucleic acid-binding region; pfam13820"
                     /db_xref="CDD:463988"
     Site            95
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <152..544
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          184..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          281..549
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          520..>838
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          773..927
                     /region_name="NCOA6IP-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          789..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK, in vitro.
                     /evidence=ECO:0000269|PubMed:11773444; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          887..891
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          899..1278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1047
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          <1056..1302
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1058
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1096
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1310..1353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1448..1474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1491..1495
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1641..2063
                     /region_name="EP300/CRSP3-binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1738..1820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1819
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Site            1822
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JL19; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1837..1908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Region          1995..2063
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14686.3)"
     Site            2018
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14686.3)"
     CDS             1..2063
                     /gene="NCOA6"
                     /gene_synonym="AIB3; ASC2; NRC; PRIP; RAP250; TRBP"
                     /coded_by="NM_001318240.1:2572..8763"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS13241.1"
                     /db_xref="GeneID:23054"
                     /db_xref="HGNC:HGNC:15936"
                     /db_xref="MIM:605299"
ORIGIN      
        1 mvlddlpnle diytslcsst medsemdfds gledddtksd siledstifv afkgniddkd
       61 fkwkldailk nvpnllhmes sklkvqkvep wnsvrvtfni preaaerlri laqsnnqqlr
      121 dlgilsvqie gegainlala qnrsqdvrmn gpmgagnsvr meagfpmasg pgiirmnnpa
      181 tvmippggnv sssmmapgpn pelqprtprp asqsdamdpl lsglhiqqqs hpsgslapph
      241 hpmqpvsvnr qmnpanfpql qqqqqqqqqq qqqqqqqqqq qqqqqlqarp pqqhqqqqpq
      301 girpqftapt qvpvppgwnq lpsgalqppp aqgslgtmta nqgwkkaplp gpmqqqlqar
      361 pslatvqtps hppppypfgs qqasqahtnf pqmsnpgqft apqmkslqgg psrvptplqq
      421 phltnkspas spssfqqgsp assptvnqtq qqmgprppqn nplpqgfqqp vsspgrnpmv
      481 qqgnvppnfm vmqqqppnqg pqslhpglgg mpkrlppgfs agqanpnfmq gqvpsttatt
      541 pgnsgapqlq anqnvqhagg qgagppqnqm qvshgppnmm qpslmgihgn mnnqqagtsg
      601 vpqvnlsnmq gqpqqgppsq lmgmhqqivp sqgqmvqqqg tlnpqnpmil sraqlmpqgq
      661 mmvnppsqnl gpspqrmtpp kqmlsqqgpq mmaphnqmmg pqgqvllqqn pmieqimtnq
      721 mqgnkqqfnt qnqsnvmpgp aqimrgptpn mqgnmvqftg qmsgqmlpqq gpvnnspsqv
      781 mgiqgqvlrp pgpsphmaqq hgdpattann dvslsqmmpd vsiqqtnmvp phvqamqgns
      841 asgnhfsghg msfnapfsga pngnqmscgq npgfpvnkdv tltspllvnl lqsdisaghf
      901 gvnnkqnntn ankpkkkkpp rkkknsqqdl ntpdtrpagl eeadqpplpg eqginldnsg
      961 pklpefsnrp pgypsqpveq rplqqmppql mqhvapppqp pqqqpqpqlp qqqqppppsq
     1021 pqsqqqqqqq qqmmmmlmmq qdpksvrlpv sqnvhpprgp lnpdsqrmpm qqsgsvpvmv
     1081 slqgpasvpp spdkqrmpmp vntplgsnsr kmvyqespqn psssplaema slpeasgsea
     1141 psvpggpnnm pshvvlpqnq lmmtgpkpgp splsatqgat pqqppvnslp sshghhfpnv
     1201 aaptqtsrpk tpnrasprpy ypqtpnnrpp stepseisls perlnasiag lfppqinipl
     1261 pprpnlnrgf dqqglnpttl kaigqapsnl tmnpsnfatp qthkldsvvv nsgkqsnsga
     1321 tkraspsnsr rsspgssrkt tpspgrqnsk apkltlasqt naallqnvel prnvlvsptp
     1381 lanppvpgsf pnnsglnpqn stvsvaavgg vvednkesln vpqdsdcqns qsrkeqvnie
     1441 lkavpaqevk mvvpedqskk dgqpsdpnkl psveenknlv spamreapts lsqlldnsga
     1501 pnvtikppgl tdlevtppvv sgedlkkasv iptlqdlsss kepsnslnlp hsnelcsslv
     1561 hpelsevssn vapsippvms rpvssssist plppnqitvf vtsnpittsa ntsaalpthl
     1621 qsalmstvvt mpnagskvmv segqsaaqsn arpqfitpvf insssiiqvm kgsqpstipa
     1681 aplttnsglm ppsvavvgpl hipqnikfss apvppnalss spapniqtgr plvlssratp
     1741 vqlpsppcts spvvpshppv qqvkelnpde aspqvntsad qntlpssqst tmvsplltns
     1801 pgssgnrrsp vssskgkgkv dkigqilltk ackkvtgsle kgeeqygadg etegqgldtt
     1861 apglmgteql steldsktpt ppaptllkmt sspvgpgtas agpslpggal ptsvrsivtt
     1921 lvpselisav pttksnhggi aseslagglv eekvgshpel lpsiapsqnl vsketsttal
     1981 qasvarpele vnaaivsgqs sepkeiveks kipgrrnsrt eeptvasesv enghrkrssr
     2041 pasassstkd itsavqskrr ksk
//
LOCUS       NP_001070737             503 aa            linear   PRI 20-NOV-2025
DEFINITION  WAS/WASL-interacting protein family member 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001070737
VERSION     NP_001070737.1
DBSOURCE    REFSEQ: accession NM_001077269.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 503)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 503)
  AUTHORS   Dong,Y., Jin,Q., Sun,M., Qi,D., Qu,H., Wang,X. and Quan,C.
  TITLE     CLDN6 inhibits breast cancer metastasis through WIP-dependent actin
            cytoskeleton-mediated autophagy
  JOURNAL   J Exp Clin Cancer Res 42 (1), 68 (2023)
   PUBMED   36935496
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 503)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 503)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 503)
  AUTHORS   Sokolik,C.G., Qassem,N. and Chill,J.H.
  TITLE     The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein
            Interactions: A Structural View
  JOURNAL   Biomolecules 10 (7), 1084 (2020)
   PUBMED   32708183
  REMARK    GeneRIF: The Disordered Cellular Multi-Tasker WIP and Its
            Protein-Protein Interactions: A Structural View.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 503)
  AUTHORS   Vaduva,G., Martinez-Quiles,N., Anton,I.M., Martin,N.C., Geha,R.S.,
            Hopper,A.K. and Ramesh,N.
  TITLE     The human WASP-interacting protein, WIP, activates the cell
            polarity pathway in yeast
  JOURNAL   J Biol Chem 274 (24), 17103-17108 (1999)
   PUBMED   10358064
REFERENCE   7  (residues 1 to 503)
  AUTHORS   Stewart,D.M., Tian,L. and Nelson,D.L.
  TITLE     Mutations that cause the Wiskott-Aldrich syndrome impair the
            interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP
            interacting protein
  JOURNAL   J Immunol 162 (8), 5019-5024 (1999)
   PUBMED   10202051
REFERENCE   8  (residues 1 to 503)
  AUTHORS   Ramesh,N., Anton,I.M., Martinez-Quiles,N. and Geha,R.S.
  TITLE     Waltzing with WASP
  JOURNAL   Trends Cell Biol 9 (1), 15-19 (1999)
   PUBMED   10087612
  REMARK    Review article
REFERENCE   9  (residues 1 to 503)
  AUTHORS   Anton,I.M., Lu,W., Mayer,B.J., Ramesh,N. and Geha,R.S.
  TITLE     The Wiskott-Aldrich syndrome protein-interacting protein (WIP)
            binds to the adaptor protein Nck
  JOURNAL   J Biol Chem 273 (33), 20992-20995 (1998)
   PUBMED   9694849
REFERENCE   10 (residues 1 to 503)
  AUTHORS   Ramesh,N., Anton,I.M., Hartwig,J.H. and Geha,R.S.
  TITLE     WIP, a protein associated with wiskott-aldrich syndrome protein,
            induces actin polymerization and redistribution in lymphoid cells
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14671-14676 (1997)
   PUBMED   9405671
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX640870.1, BC110288.1,
            AL529597.3, BC002914.2, AL832275.1, BM475558.1, AA903457.1 and
            BC045584.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that plays an important role
            in the organization of the actin cytoskeleton. The encoded protein
            binds to a region of Wiskott-Aldrich syndrome protein that is
            frequently mutated in Wiskott-Aldrich syndrome, an X-linked
            recessive disorder. Impairment of the interaction between these two
            proteins may contribute to the disease. Two transcript variants
            encoding the same protein have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2), as well as variants 1 and
            3-5, encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005539.1, SRR7346977.1465950.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..503
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..503
                     /product="WAS/WASL-interacting protein family member 1
                     isoform a"
                     /note="Wiskott-Aldrich syndrome protein interacting
                     protein; protein PRPL-2; WASP-interacting protein;
                     testicular tissue protein Li 226"
                     /calculated_mol_wt=51128
     Region          1..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Region          29..60
                     /region_name="WH2_WAS_WASL-1"
                     /note="Wiskott Aldrich syndrome homology region 2 (WH2
                     motif) in WAS/WASL-interacting protein family member 1;
                     cd22076"
                     /db_xref="CDD:409219"
     Site            order(29..33,35..37,39..41,44,46..60)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409219"
     Site            33
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Region          45..48
                     /region_name="Binds actin"
                     /note="propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Region          46..49
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409219"
     Site            125
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            134
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K1I7; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O43516.3)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43516.3)"
     CDS             1..503
                     /gene="WIPF1"
                     /gene_synonym="PRPL-2; WAS2; WASPIP; WIP"
                     /coded_by="NM_001077269.1:165..1676"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2260.1"
                     /db_xref="GeneID:7456"
                     /db_xref="HGNC:HGNC:12736"
                     /db_xref="MIM:602357"
ORIGIN      
        1 mpvppppapp ppptfalant ekptlnkteq agrnallsdi skgkklkktv tndrsapild
       61 kpkgagaggg gggfgggggf gggggggggg sfggggppgl gglfqagmpk lrstanrdnd
      121 sggsrppllp pggrstsakp fsppsgpgrf pvpspghrsg ppepqrnrmp pprpdvgskp
      181 dsipppvpst prpiqssphn rgsppvpggp rqpspgptpp pfpgnrgtal gggsirqspl
      241 sssspfsnrp plpptpsral ddkppppppp vgnrpsihre avpppppqnn kppvpstprp
      301 sassqapppp pppsrpgppp lppsssgnde tprlpqrnls lssstpplps pgrsgplppp
      361 pserppppvr dppgrsgplp ppppvsrngs tsralpatpq lpsrsgvdsp rsgprpplpp
      421 drpsagappp pppstsirng fqdspcedew esrfyfhpis dlpppepyvq ttksypskla
      481 rnesrsgsnr rergapplpp ipr
//
LOCUS       NP_001137435            1248 aa            linear   PRI 20-NOV-2025
DEFINITION  neural cell adhesion molecule L1 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001137435
VERSION     NP_001137435.1
DBSOURCE    REFSEQ: accession NM_001143963.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1248)
  AUTHORS   Mannan,R., Wang,X., Mahapatra,S., Wang,S., Chinnaiyan,A.K.,
            Skala,S.L., Zhang,Y., McMurry,L.M., Zelenka-Wang,S., Cao,X.,
            Sangoi,A.R., Dadhania,V., Picken,M.M., Menon,S., Al-Ahmadie,H.,
            Chinnaiyan,A.M., Dhanasekaran,S.M. and Mehra,R.
  TITLE     Expression of L1 Cell Adhesion Molecule, a Nephronal Principal Cell
            Marker, in Nephrogenic Adenoma
  JOURNAL   Mod Pathol 37 (8), 100540 (2024)
   PUBMED   38901674
  REMARK    GeneRIF: Expression of L1 Cell Adhesion Molecule, a Nephronal
            Principal Cell Marker, in Nephrogenic Adenoma.
REFERENCE   2  (residues 1 to 1248)
  AUTHORS   Hauser,S., Bickel,L., Weinspach,D., Gerg,M., Schafer,M.K.,
            Pfeifer,M., Hazin,J., Schelter,F., Weidle,U.H., Ramser,J.,
            Volkmann,J., Meindl,A., Schmitt,M., Schrotzlmair,F., Altevogt,P.
            and Kruger,A.
  TITLE     Full-length L1CAM and not its Delta2Delta27 splice variant promotes
            metastasis through induction of gelatinase expression
  JOURNAL   PLoS One 6 (4), e18989 (2011)
   PUBMED   21541352
  REMARK    GeneRIF: Metastasis formation upon up-regulation of full
            length-L1CAM correlated with increased invasive potential and
            elevated Matrix metalloproteinase (MMP)-2 and -9 expression and
            activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1248)
  AUTHORS   Pfeifer,M., Schirmer,U., Geismann,C., Schafer,H., Sebens,S. and
            Altevogt,P.
  TITLE     L1CAM expression in endometrial carcinomas is regulated by usage of
            two different promoter regions
  JOURNAL   BMC Mol Biol 11, 64 (2010)
   PUBMED   20799950
  REMARK    GeneRIF: Results suggest that the L1CAM gene has two functionally
            active promoter sites that are used in a cell-type specific manner.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1248)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   5  (residues 1 to 1248)
  AUTHORS   Stumpel,C. and Vos,Y.J.
  TITLE     L1 Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301657
REFERENCE   6  (residues 1 to 1248)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   7  (residues 1 to 1248)
  AUTHORS   Rosenthal,A., Jouet,M. and Kenwrick,S.
  TITLE     Aberrant splicing of neural cell adhesion molecule L1 mRNA in a
            family with X-linked hydrocephalus
  JOURNAL   Nat Genet 2 (2), 107-112 (1992)
   PUBMED   1303258
  REMARK    Erratum:[Nat Genet 1993 Mar;3(3):273]
REFERENCE   8  (residues 1 to 1248)
  AUTHORS   Kobayashi,M., Miura,M., Asou,H. and Uyemura,K.
  TITLE     Molecular cloning of cell adhesion molecule L1 from human nervous
            tissue: a comparison of the primary sequences of L1 molecules of
            different origin
  JOURNAL   Biochim Biophys Acta 1090 (2), 238-240 (1991)
   PUBMED   1932117
REFERENCE   9  (residues 1 to 1248)
  AUTHORS   Hlavin,M.L. and Lemmon,V.
  TITLE     Molecular structure and functional testing of human L1CAM: an
            interspecies comparison
  JOURNAL   Genomics 11 (2), 416-423 (1991)
   PUBMED   1769655
REFERENCE   10 (residues 1 to 1248)
  AUTHORS   Djabali,M., Mattei,M.G., Nguyen,C., Roux,D., Demengeot,J.,
            Denizot,F., Moos,M., Schachner,M., Goridis,C. and Jordan,B.R.
  TITLE     The gene encoding L1, a neural adhesion molecule of the
            immunoglobulin family, is located on the X chromosome in mouse and
            man
  JOURNAL   Genomics 7 (4), 587-593 (1990)
   PUBMED   2387585
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC126229.1, EF506611.1,
            BC025843.1 and AI361399.1.
            
            Summary: The protein encoded by this gene is an axonal glycoprotein
            belonging to the immunoglobulin supergene family. The ectodomain,
            consisting of several immunoglobulin-like domains and
            fibronectin-like repeats (type III), is linked via a single
            transmembrane sequence to a conserved cytoplasmic domain. This cell
            adhesion molecule plays an important role in nervous system
            development, including neuronal migration and differentiation.
            Mutations in the gene cause X-linked neurological syndromes known
            as CRASH (corpus callosum hypoplasia, retardation, aphasia, spastic
            paraplegia and hydrocephalus). Alternative splicing of this gene
            results in multiple transcript variants, some of which include an
            alternate exon that is considered to be specific to neurons.
            [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (3, also known as SV-L1CAM) lacks
            two alternate in-frame exons, one in the 5' coding region and the
            other (neuron-specific exon) in the 3' coding region, compared to
            variant 4. The resulting isoform (3) is shorter, and lacks an
            internal segment in the N-terminus and is missing a tyrosine-based
            sorting motif in the C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EF506611.1, SRR7346977.2962170.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..1248
                     /product="neural cell adhesion molecule L1 isoform 3
                     precursor"
                     /note="neural cell adhesion molecule L1; antigen
                     identified by monoclonal antibody R1"
                     /calculated_mol_wt=136737
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2190
     Region          30..125
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          48..52
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          61..65
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          88..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            95
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          106..111
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..123
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          135..225
                     /region_name="IgI_2_L1-CAM_like"
                     /note="Second immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM), and similar domains; member
                     of the I-set of Ig superfamily (IgSF) domains; cd05845"
                     /db_xref="CDD:409432"
     Region          135..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409432"
     Region          140..144
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409432"
     Region          147..155
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          162..168
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          171..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409432"
     Region          180..184
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409432"
     Region          186..190
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          201..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Region          212..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          243..325
                     /region_name="Ig3_L1-CAM"
                     /note="Third immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05876"
                     /db_xref="CDD:409460"
     Region          255..259
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409460"
     Region          268..272
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409460"
     Site            289
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          290..294
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409460"
     Region          304..309
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409460"
     Region          317..320
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409460"
     Region          329..417
                     /region_name="Ig4_L1-CAM_like"
                     /note="Fourth immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05867"
                     /db_xref="CDD:409453"
     Region          345..349
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409453"
     Region          358..362
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409453"
     Region          382..386
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409453"
     Region          396..401
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409453"
     Region          409..412
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409453"
     Region          423..509
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            428
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          439..443
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409031"
     Region          452..456
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409031"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          475..479
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409031"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          489..494
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409031"
     Site            500
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          502..505
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409031"
     Region          514..589
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          549..551
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            583
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          607..704
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(607,676,691)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <622..>832
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(692..693,695..696)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          693..720
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            721
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            772
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(807,882,897)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          819..902
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            820
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            844
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            871
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(898..899,901..902)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          913..998
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(913,980,995)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            974
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1017
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1025
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1066
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1116..1138
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Region          1139..1224
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Site            1158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000269|PubMed:8592152; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          1217..1248
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            1234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11627; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     CDS             1..1248
                     /gene="L1CAM"
                     /gene_synonym="CAML1; CD171; HSAS; HSAS1; HYCX; MASA;
                     MIC5; N-CAM-L1; N-CAML1; NCAM-L1; S10; SPG1"
                     /coded_by="NM_001143963.2:109..3855"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS48192.1"
                     /db_xref="GeneID:3897"
                     /db_xref="HGNC:HGNC:6470"
                     /db_xref="MIM:308840"
ORIGIN      
        1 mvvalryvwp lllcspclli qipeelmepp viteqsprrl vvfptddisl kceasgkpev
       61 qfrwtrdgvh fkpkeelgvt vyqsphsgsf titgnnsnfa qrfqgiyrcf asnklgtams
      121 heirlmaega pkwpketvkp veveegesvv lpcnpppsae plriywmnsk ilhikqderv
      181 tmgqngnlyf anvltsdnhs dyichahfpg trtiiqkepi dlrvkatnsm idrkprllfp
      241 tnssshlval qgqplvleci aegfptptik wlrpsgpmpa drvtyqnhnk tlqllkvgee
      301 ddgeyrclae nslgsarhay yvtveaapyw lhkpqshlyg pgetarldcq vqgrpqpevt
      361 wringipvee lakdqkyriq rgalilsnvq psdtmvtqce arnrhgllla nayiyvvqlp
      421 akiltadnqt ymavqgstay llckafgapv psvqwldedg ttvlqderff pyangtlgir
      481 dlqandtgry fclaandqnn vtimanlkvk datqitqgpr stiekkgsrv tftcqasfdp
      541 slqpsitwrg dgrdlqelgd sdkyfiedgr lvihsldysd qgnyscvast eldvvesraq
      601 llvvgspgpv prlvlsdlhl ltqsqvrvsw spaedhnapi ekydiefedk emapekwysl
      661 gkvpgnqtst tlklspyvhy tfrvtainky gpgepspvse tvvtpeaape knpvdvkgeg
      721 nettnmvitw kplrwmdwna pqvqyrvqwr pqgtrgpwqe qivsdpflvv sntstfvpye
      781 ikvqavnsqg kgpepqvtig ysgedypqai pelegieiln ssavlvkwrp vdlaqvkghl
      841 rgynvtywre gsqrkhskrh ihkdhvvvpa nttsvilsgl rpyssyhlev qafngrgsgp
      901 aseftfstpe gvpghpealh lecqsntsll lrwqpplshn gvltgyvlsy hpldeggkgq
      961 lsfnlrdpel rthnltdlsp hlryrfqlqa ttkegpgeai vreggtmals gisdfgnisa
     1021 tagenysvvs wvpkegqcnf rfhilfkalg eekggaslsp qyvsynqssy tqwdlqpdtd
     1081 yeihlfkerm frhqmavktn gtgrvrlppa gfategwfig fvsaiillll vllilcfikr
     1141 skggkysvkd kedtqvdsea rpmkdetfge ysdneekafg ssqpslngdi kplgsddsla
     1201 dyggsvdvqf nedgsfigqy sgkkekeaag gndssgatsp inpavale
//
LOCUS       NP_009186                327 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 7 [Homo sapiens].
ACCESSION   NP_009186
VERSION     NP_009186.1
DBSOURCE    REFSEQ: accession NM_007255.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Liu,C., Jia,Y., Zhao,X., Wang,Z., Zhu,X., Zhang,C., Li,X., Zhao,X.,
            Gong,T., Zhao,H., Zhang,D., Niu,Y., Dong,X., Li,G., Li,F.,
            Zhang,H., Zhang,L., Xu,J. and Yu,B.
  TITLE     Targeting B4GALT7 suppresses the proliferation, migration and
            invasion of hepatocellular carcinoma through the Cdc2/CyclinB1 and
            miR-338-3p/MMP2 pathway
  JOURNAL   PeerJ 11, e16450 (2023)
   PUBMED   38025683
  REMARK    GeneRIF: Targeting B4GALT7 suppresses the proliferation, migration
            and invasion of hepatocellular carcinoma through the Cdc2/CyclinB1
            and miR-338-3p/MMP2 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Sun,X., Mahajan,D., Chen,B., Song,Z. and Lu,L.
  TITLE     A quantitative study of the Golgi retention of glycosyltransferases
  JOURNAL   J Cell Sci 134 (20) (2021)
   PUBMED   34533190
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Caraffi,S.G., Maini,I., Ivanovski,I., Pollazzon,M., Giangiobbe,S.,
            Valli,M., Rossi,A., Sassi,S., Faccioli,S., Rocco,M.D., Magnani,C.,
            Campos-Xavier,B., Unger,S., Superti-Furga,A. and Garavelli,L.
  TITLE     Severe Peripheral Joint Laxity is a Distinctive Clinical Feature of
            Spondylodysplastic-Ehlers-Danlos Syndrome (EDS)-B4GALT7 and
            Spondylodysplastic-EDS-B3GALT6
  JOURNAL   Genes (Basel) 10 (10), 799 (2019)
   PUBMED   31614862
  REMARK    GeneRIF: Define some of the clinical features of B4GALT7 and
            B3GALT6-related conditions and underlined the extreme hypermobility
            of distal joints and the soft, doughy skin on the hands and feet as
            features that may be useful as the first clues for a correct
            diagnosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Mihalic Mosher,T., Zygmunt,D.A., Koboldt,D.C., Kelly,B.J.,
            Johnson,L.R., McKenna,D.S., Hood,B.C., Hickey,S.E., White,P.,
            Wilson,R.K., Martin,P.T. and McBride,K.L.
  TITLE     Expansion of B4GALT7 linkeropathy phenotype to include perinatal
            lethal skeletal dysplasia
  JOURNAL   Eur J Hum Genet 27 (10), 1569-1577 (2019)
   PUBMED   31278392
  REMARK    GeneRIF: The findings in this family expand the clinical phenotype
            of B4GALT7-related linkeropathies to include perinatal lethal
            skeletal dysplasia
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Okajima,T., Fukumoto,S., Furukawa,K. and Urano,T.
  TITLE     Molecular basis for the progeroid variant of Ehlers-Danlos
            syndrome. Identification and characterization of two mutations in
            galactosyltransferase I gene
  JOURNAL   J Biol Chem 274 (41), 28841-28844 (1999)
   PUBMED   10506123
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Almeida,R., Levery,S.B., Mandel,U., Kresse,H., Schwientek,T.,
            Bennett,E.P. and Clausen,H.
  TITLE     Cloning and expression of a proteoglycan UDP-galactose:beta-xylose
            beta1,4-galactosyltransferase I. A seventh member of the human
            beta4-galactosyltransferase gene family
  JOURNAL   J Biol Chem 274 (37), 26165-26171 (1999)
   PUBMED   10473568
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Okajima,T., Yoshida,K., Kondo,T. and Furukawa,K.
  TITLE     Human homolog of Caenorhabditis elegans sqv-3 gene is
            galactosyltransferase I involved in the biosynthesis of the
            glycosaminoglycan-protein linkage region of proteoglycans
  JOURNAL   J Biol Chem 274 (33), 22915-22918 (1999)
   PUBMED   10438455
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Kresse,H., Rosthoj,S., Quentin,E., Hollmann,J., Glossl,J., Okada,S.
            and Tonnesen,T.
  TITLE     Glycosaminoglycan-free small proteoglycan core protein is secreted
            by fibroblasts from a patient with a syndrome resembling progeroid
  JOURNAL   Am J Hum Genet 41 (3), 436-453 (1987)
   PUBMED   3631078
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC072403.1 and AF142675.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the
            beta-1,4-galactosyltransferase (beta4GalT) family. Family members
            encode type II membrane-bound glycoproteins that appear to have
            exclusive specificity for the donor substrate UDP-galactose. Each
            beta4GalT member has a distinct function in the biosynthesis of
            different glycoconjugates and saccharide structures. As type II
            membrane proteins, they have an N-terminal hydrophobic signal
            sequence that directs the protein to the Golgi apparatus which then
            remains uncleaved to function as a transmembrane anchor. The enzyme
            encoded by this gene attaches the first galactose in the common
            carbohydrate-protein linkage
            (GlcA-beta1,3-Gal-beta1,3-Gal-beta1,4-Xyl-beta1-O-Ser) found in
            proteoglycans. This enzyme differs from other beta4GalTs because it
            lacks the conserved Cys residues found in beta4GalT1-beta4GalT6 and
            it is located in cis-Golgi instead of trans-Golgi. Mutations in
            this gene have been associated with the progeroid form of
            Ehlers-Danlos syndrome. [provided by RefSeq, Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.310844.1,
                                           SRR1163655.38696.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000029410.10/ ENSP00000029410.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..327
                     /product="beta-1,4-galactosyltransferase 7"
                     /EC_number="2.4.1.133"
                     /note="beta-1,4-galactosyltransferase VII; beta4Gal-T7;
                     beta4GalT-VII; UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 7; galactosyltransferase I;
                     proteoglycan UDP-galactose:beta-xylose
                     beta1,4-galactosyltransferase I; beta-1,4-GalTase 7;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 7;
                     xylosylprotein 4-beta-galactosyltransferase;
                     xylosylprotein beta 1,4-galactosyltransferase, polypeptide
                     7; xylosylprotein beta-1,4-galactosyltransferase;
                     UDP-galactose:beta-xylose beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=37275
     Site            31..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBV7.1)"
     Region          63..87
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBV7.1)"
     Region          92..315
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(100,102,104,139,163..165)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBV7.1)"
     Site            order(163,165,257)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     CDS             1..327
                     /gene="B4GALT7"
                     /gene_synonym="EDSP1; EDSSLA; EDSSPD1; XGALT1; XGPT;
                     XGPT1"
                     /coded_by="NM_007255.3:80..1063"
                     /db_xref="CCDS:CCDS4429.1"
                     /db_xref="GeneID:11285"
                     /db_xref="HGNC:HGNC:930"
                     /db_xref="MIM:604327"
ORIGIN      
        1 mfpsrrkaaq lpwedgrsgl lsgglprkcs vfhlfvacls lgffsllwlq lscsgdvara
       61 vrgqgqetsg ppracppepp pehweedasw gphrlavlvp frerfeellv fvphmrrfls
      121 rkkirhhiyv lnqvdhfrfn raalinvgfl essnstdyia mhdvdllpln eeldygfpea
      181 gpfhvaspel hplyhyktyv ggilllskqh yrlcngmsnr fwgwgredde fyrrikgagl
      241 qlfrpsgitt gyktfrhlhd pawrkrdqkr iaaqkqeqfk vdregglntv kyhvasrtal
      301 svggapctvl nimldcdkta tpwctfs
//
LOCUS       NP_001034966             760 aa            linear   PRI 20-NOV-2025
DEFINITION  striatin-4 isoform 2 [Homo sapiens].
ACCESSION   NP_001034966
VERSION     NP_001034966.1
DBSOURCE    REFSEQ: accession NM_001039877.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 760)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 760)
  AUTHORS   Czauderna,C., Poplawski,A., O'Rourke,C.J., Castven,D.,
            Perez-Aguilar,B., Becker,D., Heilmann-Heimbach,S., Odenthal,M.,
            Amer,W., Schmiel,M., Drebber,U., Binder,H., Ridder,D.A.,
            Schindeldecker,M., Straub,B.K., Galle,P.R., Andersen,J.B.,
            Thorgeirsson,S.S., Park,Y.N. and Marquardt,J.U.
  TITLE     Epigenetic modifications precede molecular alterations and drive
            human hepatocarcinogenesis
  JOURNAL   JCI Insight 6 (17), e146196 (2021)
   PUBMED   34375307
  REMARK    GeneRIF: Epigenetic modifications precede molecular alterations and
            drive human hepatocarcinogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 760)
  AUTHORS   Jeong,B.C., Bae,S.J., Ni,L., Zhang,X., Bai,X.C. and Luo,X.
  TITLE     Cryo-EM structure of the Hippo signaling integrator human STRIPAK
  JOURNAL   Nat Struct Mol Biol 28 (3), 290-299 (2021)
   PUBMED   33633399
REFERENCE   4  (residues 1 to 760)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 760)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 760)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 760)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   8  (residues 1 to 760)
  AUTHORS   Di Bernardo,M.C., Crowther-Swanepoel,D., Broderick,P., Webb,E.,
            Sellick,G., Wild,R., Sullivan,K., Vijayakrishnan,J., Wang,Y.,
            Pittman,A.M., Sunter,N.J., Hall,A.G., Dyer,M.J., Matutes,E.,
            Dearden,C., Mainou-Fowler,T., Jackson,G.H., Summerfield,G.,
            Harris,R.J., Pettitt,A.R., Hillmen,P., Allsup,D.J., Bailey,J.R.,
            Pratt,G., Pepper,C., Fegan,C., Allan,J.M., Catovsky,D. and
            Houlston,R.S.
  TITLE     A genome-wide association study identifies six susceptibility loci
            for chronic lymphocytic leukemia
  JOURNAL   Nat Genet 40 (10), 1204-1210 (2008)
   PUBMED   18758461
REFERENCE   9  (residues 1 to 760)
  AUTHORS   Breitman,M., Zilberberg,A., Caspi,M. and Rosin-Arbesfeld,R.
  TITLE     The armadillo repeat domain of the APC tumor suppressor protein
            interacts with Striatin family members
  JOURNAL   Biochim Biophys Acta 1783 (10), 1792-1802 (2008)
   PUBMED   18502210
REFERENCE   10 (residues 1 to 760)
  AUTHORS   Castets,F., Rakitina,T., Gaillard,S., Moqrich,A., Mattei,M.G. and
            Monneron,A.
  TITLE     Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
            proteins principally expressed in the brain
  JOURNAL   J Biol Chem 275 (26), 19970-19977 (2000)
   PUBMED   10748158
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA510367.1, AB209003.1 and AF212940.1.
            
            Transcript Variant: This variant (2) represents the longer
            transcript and encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.282814.1,
                                           SRR18074967.1917498.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            NMD candidate :: translation inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..760
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..760
                     /product="striatin-4 isoform 2"
                     /note="striatin, calmodulin binding protein 4; protein
                     phosphatase 2 regulatory subunit B'''gamma"
                     /calculated_mol_wt=81135
     Region          10..65
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          65..189
                     /region_name="Striatin"
                     /note="Striatin family; pfam08232"
                     /db_xref="CDD:462401"
     Region          71..79
                     /region_name="Caveolin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          165..182
                     /region_name="Calmodulin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          213..232
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          271..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          363..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          437..759
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          443..482
                     /region_name="WD 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Site            order(444,462,466,472..473,496..497,515,519,525..526,
                     549..550,567,572,578..579,594,615,620,625..626,640..641,
                     661,665,671..672,684..685,702,707,713..714,726,731,749,
                     753,759)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          450..496
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          496..535
                     /region_name="WD 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          502..549
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          549..588
                     /region_name="WD 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          554..593
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          594..635
                     /region_name="WD 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          601..637
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          642..681
                     /region_name="WD 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          647..683
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          684..723
                     /region_name="WD 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          689..728
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          730..760
                     /region_name="WD 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRL3.2)"
     Region          735..759
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..760
                     /gene="STRN4"
                     /gene_synonym="PPP2R6C; ZIN; zinedin"
                     /coded_by="NM_001039877.2:21..2303"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42581.1"
                     /db_xref="GeneID:29888"
                     /db_xref="HGNC:HGNC:15721"
                     /db_xref="MIM:614767"
ORIGIN      
        1 mmeeraaaav aaaasscrpl gsgagpgptg aapvsapapg pgpagkgggg ggspgptagp
       61 eplslpgilh fiqhewarfe aekarweaer aelqaqvafl qgerkgqenl ktdlvrrikm
      121 leyalkqera kyhklkfgtd lnqgekkadv seqvsngpve svtlensplv wkegrqllrq
      181 yleevgytdt ildmrskrvr sllgrsleln gavepsegap rappgpagls ggesllvkqi
      241 eeqikrnaag kdgkerlggs vlgqipflqn cededsdedd eldsvqhkkq rvklpskalv
      301 pemededeed dsedainefd flgsgedgeg apdprrctvd gsphelesrr vklqgiladl
      361 rdvdglppkv tgpppgtpqp rphegsfgfs sdvfimdtig ggevslgdla dltvtndndl
      421 scdlsdskda fkktwnpkft lrshydgirs lafhhsqsal ltasedgtlk lwnlqkavta
      481 kknaaldvep ihafrahrgp vlavamgsns eycysggada cihswkipdl smdpydgydp
      541 svlshvlegh gdavwglafs ptsqrlascs adgtvriwdp sssspaclct fptasehgvp
      601 tsvaftstep ahivasfrsg dtvlydmevg salltlesrg ssgptqinqv vshpnqplti
      661 tahddrgirf ldnrtgkpvh smvahldavt clavdpngaf lmsgshdcsl rlwsldnktc
      721 vqeitahrkk heeaihavac hpskaliasa gadalakvfv
//
LOCUS       NP_031396                340 aa            linear   PRI 20-NOV-2025
DEFINITION  replication factor C subunit 5 isoform 1 [Homo sapiens].
ACCESSION   NP_031396
VERSION     NP_031396.1
DBSOURCE    REFSEQ: accession NM_007370.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Wang,F., He,Q., Yao,N.Y., O'Donnell,M.E. and Li,H.
  TITLE     The human ATAD5 has evolved unique structural elements to function
            exclusively as a PCNA unloader
  JOURNAL   Nat Struct Mol Biol 31 (11), 1680-1691 (2024)
   PUBMED   38871854
REFERENCE   3  (residues 1 to 340)
  AUTHORS   He,Q., Wang,F., O'Donnell,M.E. and Li,H.
  TITLE     Cryo-EM reveals a nearly complete PCNA loading process and unique
            features of the human alternative clamp loader CTF18-RFC
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2319727121 (2024)
   PUBMED   38669181
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Yao,H., Zhou,X., Zhou,A., Chen,J., Chen,G., Shi,X., Shi,B., Tai,Q.,
            Mi,X., Zhou,G., Wang,S., Sun,J., Yang,X., Yang,Y., Cao,H., Zhou,D.,
            Sun,L., Yao,Y. and He,S.
  TITLE     RFC5, regulated by circ_0038985/miR-3614-5p, functions as an
            oncogene in the progression of colorectal cancer
  JOURNAL   Mol Carcinog 62 (6), 771-785 (2023)
   PUBMED   36988339
  REMARK    GeneRIF: RFC5, regulated by circ_0038985/miR-3614-5p, functions as
            an oncogene in the progression of colorectal cancer.
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Li,W.J., Wu,D.W., Zhou,Y.F., Zhang,C.W. and Liao,X.W.
  TITLE     Prognostic biomarker replication factor C subunit 5 and its
            correlation with immune infiltrates in acute myeloid leukemia
  JOURNAL   Hematology 27 (1), 555-564 (2022)
   PUBMED   35544695
  REMARK    GeneRIF: Prognostic biomarker replication factor C subunit 5 and
            its correlation with immune infiltrates in acute myeloid leukemia.
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Wood,R.D. and Shivji,M.K.
  TITLE     Which DNA polymerases are used for DNA-repair in eukaryotes?
  JOURNAL   Carcinogenesis 18 (4), 605-610 (1997)
   PUBMED   9111189
  REMARK    Review article
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Mossi,R., Jonsson,Z.O., Allen,B.L., Hardin,S.H. and Hubscher,U.
  TITLE     Replication factor C interacts with the C-terminal side of
            proliferating cell nuclear antigen
  JOURNAL   J Biol Chem 272 (3), 1769-1776 (1997)
   PUBMED   8999859
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Uhlmann,F., Cai,J., Flores-Rozas,H., Dean,F.B., Finkelstein,J.,
            O'Donnell,M. and Hurwitz,J.
  TITLE     In vitro reconstitution of human replication factor C from its five
            subunits
  JOURNAL   Proc Natl Acad Sci U S A 93 (13), 6521-6526 (1996)
   PUBMED   8692848
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Dean,F.B., Chen,M., Pan,Z.Q.,
            Hurwitz,J., Shiratori,A., Murakami,Y., Ozawa,K. et al.
  TITLE     Assignment of the 36.5-kDa (RFC5), 37-kDa (RFC4), 38-kDa (RFC3),
            and 40-kDa (RFC2) subunit genes of human replication factor C to
            chromosome bands 12q24.2-q24.3, 3q27, 13q12.3-q13, and 7q11.23
  JOURNAL   Genomics 25 (1), 274-278 (1995)
   PUBMED   7774928
REFERENCE   10 (residues 1 to 340)
  AUTHORS   O'Donnell,M., Onrust,R., Dean,F.B., Chen,M. and Hurwitz,J.
  TITLE     Homology in accessory proteins of replicative polymerases--E. coli
            to humans
  JOURNAL   Nucleic Acids Res 21 (1), 1-3 (1993)
   PUBMED   8441605
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU121576.1 and BC001866.1.
            
            Summary: This gene encodes the smallest subunit of the replication
            factor C complex, which consists of five distinct subunits (140,
            40, 38, 37, and 36 kDa) and is required for DNA replication. This
            subunit interacts with the C-terminal region of proliferating cell
            nuclear antigen and is required to open and load proliferating cell
            nuclear antigen onto DNA during S phase. It is a member of the AAA+
            (ATPases associated with various cellular activities) ATPase family
            and forms a core complex with the 38 and 40 kDa subunits that
            possesses DNA-dependent ATPase activity. A related pseudogene has
            been identified on chromosome 9. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Nov 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001866.1, SRR1803611.126310.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000454402.7/ ENSP00000408295.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.23"
     Protein         1..340
                     /product="replication factor C subunit 5 isoform 1"
                     /note="RFC, 36.5 kD subunit; A1 36 kDa subunit;
                     replication factor C, 36-kDa subunit; replication factor C
                     (activator 1) 5, 36.5kDa; RF-C 36 kDa subunit"
                     /calculated_mol_wt=38366
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P40937.1)"
     Region          16..329
                     /region_name="rfc"
                     /note="replication factor C small subunit; Reviewed;
                     PRK00440"
                     /db_xref="CDD:234763"
     CDS             1..340
                     /gene="RFC5"
                     /gene_synonym="RFC36"
                     /coded_by="NM_007370.7:126..1148"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9185.1"
                     /db_xref="GeneID:5985"
                     /db_xref="HGNC:HGNC:9973"
                     /db_xref="MIM:600407"
ORIGIN      
        1 metsalkqqe qpaatkirnl pwvekyrpqt lndlishqdi lstiqkfine drlphlllyg
       61 ppgtgktsti lacakqlykd kefgsmvlel nasddrgidi irgpilsfas trtifkkgfk
      121 lvildeadam tqdaqnalrr viekftentr fclicnylsk iipalqsrct rfrfgpltpe
      181 lmvprlehvv eeekvdised gmkalvtlss gdmrralnil qstnmafgkv teetvytctg
      241 hplksdiani ldwmlnqdft tayrnitelk tlkglalhdi lteihlfvhr vdfpssvrih
      301 lltkmadiey rlsvgtneki qlssliaafq vtrdlivaea
//
LOCUS       NP_001308512             492 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 23 [Homo sapiens].
ACCESSION   NP_001308512 XP_011530598
VERSION     NP_001308512.1
DBSOURCE    REFSEQ: accession NM_001321583.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 492)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Mar 26, 2016 this sequence version replaced XP_011530598.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.164152.1,
                                           SRR1660807.160034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..492
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 23"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=55530
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          360..487
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..492
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321583.2:671..2149"
                     /note="isoform 23 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS93602.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkep qttvihnpdg nkestessnt tiededvkar
      361 kqeiikvteq lieainngdf eaytkicdpg ltafepealg nlvegmdfhr fyfenalsks
      421 nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt mqseetrvwh rrdgkwqnvh
      481 fhrsgsptvp ik
//
LOCUS       NP_001337212             552 aa            linear   PRI 20-NOV-2025
DEFINITION  structure-specific endonuclease subunit MUS81 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001337212
VERSION     NP_001337212.1
DBSOURCE    REFSEQ: accession NM_001350283.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Dvorak,O., Slavickova,M., Laco,J., Stepan,M., Cermakova,E. and
            Spacek,J.
  TITLE     DNA hypermethylation of tumor suppressor genes TWIST1, GATA4, MUS81
            and NTRK1 in endometrial hyperplasia
  JOURNAL   Ceska Gynekol 89 (4), 261-268 (2024)
   PUBMED   39242200
  REMARK    GeneRIF: DNA hypermethylation of tumor suppressor genes TWIST1,
            GATA4, MUS81 and NTRK1 in endometrial hyperplasia.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Dehe,P.M. and Gaillard,P.H.L.
  TITLE     Control of structure-specific endonucleases to maintain genome
            stability
  JOURNAL   Nat Rev Mol Cell Biol 18 (5), 315-330 (2017)
   PUBMED   28327556
  REMARK    Review article
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Blanco,M.G. and Matos,J.
  TITLE     Hold your horSSEs: controlling structure-selective endonucleases
            MUS81 and Yen1/GEN1
  JOURNAL   Front Genet 6, 253 (2015)
   PUBMED   26284109
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 552)
  AUTHORS   West,S.C., Blanco,M.G., Chan,Y.W., Matos,J., Sarbajna,S. and
            Wyatt,H.D.
  TITLE     Resolution of Recombination Intermediates: Mechanisms and
            Regulation
  JOURNAL   Cold Spring Harb Symp Quant Biol 80, 103-109 (2015)
   PUBMED   26370409
  REMARK    Review article
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Wyatt,H.D. and West,S.C.
  TITLE     Holliday junction resolvases
  JOURNAL   Cold Spring Harb Perspect Biol 6 (9), a023192 (2014)
   PUBMED   25183833
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Sarbajna,S. and West,S.C.
  TITLE     Holliday junction processing enzymes as guardians of genome
            stability
  JOURNAL   Trends Biochem Sci 39 (9), 409-419 (2014)
   PUBMED   25131815
  REMARK    Review article
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Constantinou,A., Chen,X.B., McGowan,C.H. and West,S.C.
  TITLE     Holliday junction resolution in human cells: two junction
            endonucleases with distinct substrate specificities
  JOURNAL   EMBO J 21 (20), 5577-5585 (2002)
   PUBMED   12374758
  REMARK    GeneRIF: Mus81-associated endonuclease may play a more direct role
            in replication fork collapse by catalysing the cleavage of stalled
            fork structures.
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Chen,X.B., Melchionna,R., Denis,C.M., Gaillard,P.H.L., Blasina,A.,
            Van de Weyer,I., Boddy,M.N., Russell,P., Vialard,J. and
            McGowan,C.H.
  TITLE     Human Mus81-associated endonuclease cleaves Holliday junctions in
            vitro
  JOURNAL   Mol Cell 8 (5), 1117-1127 (2001)
   PUBMED   11741546
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Boddy,M.N., Lopez-Girona,A., Shanahan,P., Interthal,H., Heyer,W.D.
            and Russell,P.
  TITLE     Damage tolerance protein Mus81 associates with the FHA1 domain of
            checkpoint kinase Cds1
  JOURNAL   Mol Cell Biol 20 (23), 8758-8766 (2000)
   PUBMED   11073977
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA449863.1, AK223564.1,
            BC009999.2, CR989527.1 and BI816797.1.
            
            Summary: This gene encodes a structure-specific endonuclease which
            belongs to the XPF/MUS81 endonuclease family and plays a critical
            role in the resolution of recombination intermediates during DNA
            repair after inter-strand cross-links, replication fork collapse,
            and DNA double-strand breaks. The encoded protein associates with
            one of two closely related essential meiotic endonuclease proteins
            (EME1 or EME2) to form a complex that processes DNA secondary
            structures. It contains an N-terminal DEAH helicase domain, an
            excision repair cross complementation group 4 (ERCC4) endonuclease
            domain, and two tandem C-terminal helix-hairpin-helix domains. Mice
            with a homozygous knockout of the orthologous gene have significant
            meiotic defects including the failure to repair a subset of DNA
            double strand breaks. [provided by RefSeq, Jun 2017].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.820893.1,
                                           SRR1660805.116860.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..552
                     /product="structure-specific endonuclease subunit MUS81
                     isoform 1"
                     /EC_number="3.1.22.-"
                     /note="SLX3 structure-specific endonuclease subunit
                     homolog; crossover junction endonuclease MUS81; MUS81
                     endonuclease homolog; structure-specific endonuclease
                     subunit MUS81"
                     /calculated_mol_wt=61113
     Region          84..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NY9.3)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96NY9.3)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96NY9.3)"
     Region          125..244
                     /region_name="Interaction with BLM.
                     /evidence=ECO:0000269|PubMed:15805243"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NY9.3)"
     Region          130..219
                     /region_name="WH_MUS81"
                     /note="winged helix domain found in crossover junction
                     endonuclease MUS81 and similar proteins; cd21036"
                     /db_xref="CDD:411029"
     Region          131..230
                     /region_name="Winged helix domain (WHD), critical for
                     endonuclease activity.
                     /evidence=ECO:0000269|PubMed:35290797"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NY9.3)"
     Site            184..191
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:411029"
     Region          266..420
                     /region_name="XPF_nuclease_Mus81"
                     /note="XPF-like nuclease domain of Mus81; cd20074"
                     /db_xref="CDD:410850"
     Site            order(274,277,307)
                     /site_type="other"
                     /note="Mg binding site [ion binding]"
                     /db_xref="CDD:410850"
     Site            order(331,348,351..352,355,364,366,386..387,390..391,
                     393..394,398..402,404,408,412,415..416,419..420)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410850"
     Site            order(345..346,351,384,387..388,391)
                     /site_type="other"
                     /note="nucleic acid substrate binding site [nucleotide
                     binding]"
                     /db_xref="CDD:410850"
     Region          472..546
                     /region_name="Helix-hairpin-helix (2HhH), involved in DNA
                     recognition and bending.
                     /evidence=ECO:0000269|PubMed:24733841,
                     ECO:0000269|PubMed:35290797"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NY9.3)"
     CDS             1..552
                     /gene="MUS81"
                     /gene_synonym="SLX3"
                     /coded_by="NM_001350283.2:322..1980"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:80198"
                     /db_xref="HGNC:HGNC:29814"
                     /db_xref="MIM:606591"
ORIGIN      
        1 maapvrlgrk rplpacpnpl fvrwltewrd eatrsrrrtr fvfqkalrsl rryplplrsg
       61 keakilqhfg dglcrmlder lqrhrtsggd hapdspsgen spapqgrlae vqdssmpvpa
      121 qpkaggsgsy wparhsgarv illvlyrehl npnghhfltk eellqrcaqk sprvapgsar
      181 pwpalrsllh rnlvlrthqp arysltpegl elaqklaese glsllnvgig pkeppgeeta
      241 vpgaasaela seagvqqqpl elrpgeyrvl lcvdigetrg gghrpellre lqrlhvthtv
      301 rklhvgdfvw vaqetnprdp aanpgelvld hiverkrldd lcssiidgrf reqkfrlkrc
      361 glerrvylve ehgsvhnlsl pestllqavt ntqvidgffv krtadikesa aylalltrgl
      421 qrlyqghtlr srpwgtpgnp esgamtspnp lcslltfsdf nagaiknkaq svrevfarql
      481 mqvrgvsgek aaalvdryst pasllaayda catpkeqetl lstikcgrlq rnlgpalsrt
      541 lsqlycsygp lt
//
LOCUS       NP_056171               1630 aa            linear   PRI 20-NOV-2025
DEFINITION  protein scribble homolog isoform b [Homo sapiens].
ACCESSION   NP_056171
VERSION     NP_056171.3
DBSOURCE    REFSEQ: accession NM_015356.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1630)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1630)
  AUTHORS   Edamana,S., Login,F.H., Riishede,A., Dam,V.S., Kirkegaard,T. and
            Nejsum,L.N.
  TITLE     The water channels aquaporin-1 and aquaporin-3 interact with and
            affect the cell polarity protein Scribble in 3D in vitro models of
            breast cancer
  JOURNAL   Am J Physiol Cell Physiol 327 (5), C1323-C1334 (2024)
   PUBMED   39279492
  REMARK    GeneRIF: The water channels aquaporin-1 and aquaporin-3 interact
            with and affect the cell polarity protein Scribble in 3D in vitro
            models of breast cancer.
REFERENCE   3  (residues 1 to 1630)
  AUTHORS   Lulic,L., Simic,I., Bozinovic,K., Pesut,E., Manojlovic,L., Grce,M.,
            Dediol,E., Sabol,I. and Tomaic,V.
  TITLE     Moderate SCRIB Expression Levels Correlate with Worse Prognosis in
            OPSCC Patients Regardless of HPV Status
  JOURNAL   Cells 13 (12), 1002 (2024)
   PUBMED   38920638
  REMARK    GeneRIF: Moderate SCRIB Expression Levels Correlate with Worse
            Prognosis in OPSCC Patients Regardless of HPV Status.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1630)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   5  (residues 1 to 1630)
  AUTHORS   Almeida,S.M., Ivantsiv,S., Niibori,R., Dunham,W.H., Green,B.A.,
            Zhao,L., Gingras,A.C. and Cordes,S.P.
  TITLE     An interaction between OTULIN and SCRIB uncovers roles for linear
            ubiquitination in planar cell polarity
  JOURNAL   Dis Model Mech 16 (8) (2023)
   PUBMED   37589075
  REMARK    GeneRIF: An interaction between OTULIN and SCRIB uncovers roles for
            linear ubiquitination in planar cell polarity.
REFERENCE   6  (residues 1 to 1630)
  AUTHORS   Audebert,S., Navarro,C., Nourry,C., Chasserot-Golaz,S., Lecine,P.,
            Bellaiche,Y., Dupont,J.L., Premont,R.T., Sempere,C., Strub,J.M.,
            Van Dorsselaer,A., Vitale,N. and Borg,J.P.
  TITLE     Mammalian Scribble forms a tight complex with the betaPIX exchange
            factor
  JOURNAL   Curr Biol 14 (11), 987-995 (2004)
   PUBMED   15182672
REFERENCE   7  (residues 1 to 1630)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
REFERENCE   8  (residues 1 to 1630)
  AUTHORS   Nakagawa,S., Yano,T., Nakagawa,K., Takizawa,S., Suzuki,Y.,
            Yasugi,T., Huibregtse,J.M. and Taketani,Y.
  TITLE     Analysis of the expression and localisation of a LAP protein, human
            scribble, in the normal and neoplastic epithelium of uterine cervix
  JOURNAL   Br J Cancer 90 (1), 194-199 (2004)
   PUBMED   14710229
  REMARK    GeneRIF: Degradation by human papilloma virus E6 may cause
            progressive decrease of hScrib expression during disease
            progression from low-grade squamous intraepithelial lesions (SIL)
            to high-grade SIL
REFERENCE   9  (residues 1 to 1630)
  AUTHORS   Dow,L.E., Brumby,A.M., Muratore,R., Coombe,M.L., Sedelies,K.A.,
            Trapani,J.A., Russell,S.M., Richardson,H.E. and Humbert,P.O.
  TITLE     hScrib is a functional homologue of the Drosophila tumour
            suppressor Scribble
  JOURNAL   Oncogene 22 (58), 9225-9230 (2003)
   PUBMED   14681682
  REMARK    GeneRIF: hScrib is a functional homologue of DmScrib and therefore
            predict an important role for hScrib in the suppression of
            mammalian tumorigenesis
REFERENCE   10 (residues 1 to 1630)
  AUTHORS   Nakagawa,S. and Huibregtse,J.M.
  TITLE     Human scribble (Vartul) is targeted for ubiquitin-mediated
            degradation by the high-risk papillomavirus E6 proteins and the
            E6AP ubiquitin-protein ligase
  JOURNAL   Mol Cell Biol 20 (21), 8244-8253 (2000)
   PUBMED   11027293
  REMARK    GeneRIF: KIAA0147 encodes the human homolog of Drosophila Scribble.
            hScrib is targeted for ubiquitin-mediated degradation by the HPV E6
            oncoprotein, and mutations in Dros. scrib result in loss of
            polarity and growth control of epithelial cells.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105219.6 and KF458881.1.
            
            On Nov 3, 2011 this sequence version replaced NP_056171.2.
            
            Summary: This gene encodes a protein that was identified as being
            similar to the Drosophila scribble protein. The mammalian protein
            is involved in tumor suppression pathways. As a scaffold protein
            involved in cell polarization processes, this protein binds to many
            other proteins. The encoded protein binds to papillomavirus E6
            protein via its PDZ domain and the C-terminus of E6. Two
            alternatively spliced transcript variants that encode different
            protein isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame exon
            compared to variant 1. The resulting isoform (b) has the same N-
            and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY062238.1, AF240677.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1630
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1630
                     /product="protein scribble homolog isoform b"
                     /note="protein scribble homolog; scribbled homolog;
                     scribbled planar cell polarity protein"
                     /calculated_mol_wt=174785
     Region          1..818
                     /region_name="Sufficient for targeting to adherens
                     junction and to inhibit cell proliferation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          14..37
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          36..94
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          38..60
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          87..>396
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          199..221
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          268..290
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          291..313
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          314..336
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          360..381
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          417..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          459..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          628..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          717..1229
                     /region_name="Interaction with ARHGEF7.
                     /evidence=ECO:0000269|PubMed:15182672"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          727..813
                     /region_name="PDZ1_Scribble-like"
                     /note="PDZ domain 1 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06704"
                     /db_xref="CDD:467188"
     Region          728..1194
                     /region_name="Required for interaction with VIM.
                     /evidence=ECO:0000269|PubMed:19386766"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            order(737..743,761,764,793,797,800..801)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467188"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          827..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          859..950
                     /region_name="PDZ2_Scribble-like"
                     /note="PDZ domain 2 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06703"
                     /db_xref="CDD:467187"
     Site            order(871..877,895,898,928,932,935..936)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467187"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1003..1091
                     /region_name="PDZ3_Scribble-like"
                     /note="PDZ domain 3 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06702"
                     /db_xref="CDD:467186"
     Site            order(1013..1019,1039,1042,1071,1075,1078..1079)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467186"
     Region          1095..1192
                     /region_name="PDZ4_Scribble-like"
                     /note="PDZ domain 4 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06701"
                     /db_xref="CDD:467185"
     Region          1105..1117
                     /region_name="Interaction with tick-borne encephalitis
                     virus RNA-directed RNA polymerase NS5.
                     /evidence=ECO:0000269|PubMed:18042258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            order(1110..1116,1137,1140,1170,1174,1177..1178)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467185"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1227..1246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1277..1489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1545
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1597..1630
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     CDS             1..1630
                     /gene="SCRIB"
                     /gene_synonym="CRIB1; oSCRIB; SCRB1; SCRIB1; Vartul"
                     /coded_by="NM_015356.5:402..5294"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6411.1"
                     /db_xref="GeneID:23513"
                     /db_xref="HGNC:HGNC:30377"
                     /db_xref="MIM:607733"
ORIGIN      
        1 mlkciplwrc nrhvesvdkr hcslqavpee iyrysrslee llldanqlre lpkpffrlln
       61 lrklglsdne iqrlppevan fmqlveldvs rndipeipes ikfckaleia dfsgnplsrl
      121 pdgftqlrsl ahlalndvsl qalpgdvgnl anlvtlelre nllkslpasl sflvkleqld
      181 lggndlevlp dtlgalpnlr elwldrnqls alppelgnlr rlvcldvsen rleelpaelg
      241 glvlltdlll sqnllrrlpd gigqlkqlsi lkvdqnrlce vteaigdcen lseliltenl
      301 lmalprslgk ltkltnlnvd rnhlealppe iggcvalsvl slrdnrlavl ppelahttel
      361 hvldvagnrl qslpfalthl nlkalwlaen qaqpmlrfqt eddartgekv ltcyllpqqp
      421 ppsledagqq gslsetwsda ppsrvsviqf leapigdeda eeaaaekrgl qrratphpse
      481 lkvmkrsieg rrseacpcqp dsgsplpaee ekrlsaesgl sedsrpsast vseaepegps
      541 aeaqggsqqe attaggeeda eedyqeptvh faedallpgd dreieegqpe apwtlpggrq
      601 rlirkdtphy kkhfkisklp qpeavvallq gmqpdgegpv apggwhngph apwapraqke
      661 eeeeeegspq eeeeeeeeen raeeeeaste eedkegavvs apsvkgvsfd qannlliepa
      721 rieeeeltlt ilrqtgglgi siaggkgstp ykgddegifi srvseegpaa ragvrvgdkl
      781 levngvalqg aehheaveal rgagtavqmr vwrermvepe navtitplrp eddysprerr
      841 ggglrlpllp pespgplrqr hvaclarser glgfsiaggk gstpyragda gifvsriaeg
      901 gaahragtlq vgdrvlsing vdvtearhdh avslltaasp tialllerea ggplppsplp
      961 hsspptaava ttsittatpg vpglpslaps llaaalegpy pveeirlpra ggplglsivg
     1021 gsdhsshpfg vqepgvfisk vlprglaars glrvgdrila vngqdvrdat hqeavsallr
     1081 pclelsllvr rdpappglre lciqkapger lgisirggar ghagnprdpt degifiskvs
     1141 ptgaagrdgr lrvglrllev nqqsllglth geavqllrsv gdtltvlvcd gfeastdaal
     1201 evspgvianp faagighrns lesissidre lspegpgkek elpgqtlhwg peateaagrg
     1261 lqplkldyra laavpsagsv qrvpsgaagg kmaespcsps gqqppsppsp delpanvkqa
     1321 yrafaavpts hppedapaqp ptpgpaaspe qlsfrerqky felevrvpqa egppkrvslv
     1381 gaddlrkmqe eearklqqkr aqmlreaaea gaearlaldg etlgeeeqed eqppwaspsp
     1441 tsrqspaspp plgggapvrt akaerrhqer lrvqspeppa peralspael raleaekral
     1501 wraarmksle qdalraqmvl srsqegrgtr gplerlaeap spaptpsptp vedlgpqtst
     1561 spgrlspdfa eelrslepsp spgpqeedge valvllgrps pgavgpedva lcssrrpvrp
     1621 grrglgpvps
//
LOCUS       NP_001306610             409 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-1 isoform 7 [Homo sapiens].
ACCESSION   NP_001306610 XP_005253993
VERSION     NP_001306610.1
DBSOURCE    REFSEQ: accession NM_001319681.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 409)
  AUTHORS   Xu,X., Gao,F., Wang,J., Long,C., Tao,L., Ding,L. and Ji,Y.
  TITLE     microRNA-216a-5p inhibits the development of gastric cancer through
            target combination with TCTN1
  JOURNAL   Minerva Med 114 (3), 323-331 (2023)
   PUBMED   32486612
  REMARK    GeneRIF: microRNA-216a-5p inhibits the development of gastric
            cancer through target combination with TCTN1.
REFERENCE   2  (residues 1 to 409)
  AUTHORS   Bai,G., Wei,N., Li,F., Zhao,P., Meng,Z., Zou,B., Liu,Y., Xu,K.,
            Li,K., Yao,C. and Yang,P.
  TITLE     Function and transcriptional regulation of TCTN1 in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 47 (2) (2022)
   PUBMED   34859261
  REMARK    GeneRIF: Function and transcriptional regulation of TCTN1 in oral
            squamous cell carcinoma.
REFERENCE   3  (residues 1 to 409)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 409)
  AUTHORS   Wang,H., Jiang,W., Dai,M., Xiao,B., Xu,Y., Sun,Y., Liu,Y., Ying,X.,
            Sun,Y., Wei,W. and Ji,X.
  TITLE     [Diagnosis of two cases from one family with Joubert syndrome
            caused by novel mutations of TCTN1 gene by whole exome sequencing]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 36 (7), 686-689 (2019)
   PUBMED   31302911
  REMARK    GeneRIF: Two novel TCTN1 mutations were identified in a family with
            Joubert syndrome
REFERENCE   5  (residues 1 to 409)
  AUTHORS   Alazami,A.M., Alshammari,M.J., Salih,M.A., Alzahrani,F., Hijazi,H.,
            Seidahmed,M.Z., Abu Safieh,L., Aldosary,M., Khan,A.O. and
            Alkuraya,F.S.
  TITLE     Molecular characterization of Joubert syndrome in Saudi Arabia
  JOURNAL   Hum Mutat 33 (10), 1423-1428 (2012)
   PUBMED   22693042
REFERENCE   6  (residues 1 to 409)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 409)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    GeneRIF: Mutations in Tctn1 is associated with ciliopathies.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 409)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 409)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 409)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295514.1, AK301732.1,
            CA419765.1 and AC144522.12.
            
            On Feb 4, 2016 this sequence version replaced XP_005253993.1.
            
            Summary: This gene encodes a member of a family of secreted and
            transmembrane proteins. The orthologous gene in mouse functions
            downstream of smoothened and rab23 to modulate hedgehog signal
            transduction. This protein is a component of the tectonic-like
            complex, which forms a barrier between the ciliary axoneme and the
            basal body. A mutation in this gene was found in a family with
            Joubert syndrome-13. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (7) contains an alternate exon in
            the 5' region, initiates translation at a downstream start codon,
            and uses an alternate in-frame splice site in the 3' coding region,
            compared to variant 1. The resulting isoform (7) has a shorter
            N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301732.1, SRR1803616.21712.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..409
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..409
                     /product="tectonic-1 isoform 7"
                     /calculated_mol_wt=44617
     Region          <1..209
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     CDS             1..409
                     /gene="TCTN1"
                     /gene_synonym="JBTS13; TECT1"
                     /coded_by="NM_001319681.2:762..1991"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:79600"
                     /db_xref="HGNC:HGNC:26113"
                     /db_xref="MIM:609863"
ORIGIN      
        1 mktsdgftln aesyvsfttk ldiptaakye ygvplqtsds flrfpsslts slctdnnpaa
       61 flvnqavkct rkinleqcee iealsmafys speilrvpds rkkvpitvqs iviqslnktl
      121 trredtdvlq ptlvnaghfs lcvnvvlevk ysltytdage vtkadlsfvl gtvssvvvpl
      181 qqkfeihflq entqpvplsg npgyvvglpl aagfqphkgs giiqttnryg qltilhstte
      241 qdclalegvr tpvlfgytmq sgcklrltga lpcqlvaqkv ksllwgqgfp dyvapfgnsq
      301 aqdmldwvpi hfitqsfnrk dscqlpgalv ievkwtkygs llnpqakivn vtanlisssf
      361 peansgnert ilistavtfv dvsapaeagf rappainarl pfnfffpfv
//
LOCUS       NP_001108479             528 aa            linear   PRI 20-NOV-2025
DEFINITION  protein lin-54 homolog isoform b [Homo sapiens].
ACCESSION   NP_001108479
VERSION     NP_001108479.1
DBSOURCE    REFSEQ: accession NM_001115007.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Marceau,A.H., Felthousen,J.G., Goetsch,P.D., Iness,A.N., Lee,H.W.,
            Tripathi,S.M., Strome,S., Litovchick,L. and Rubin,S.M.
  TITLE     Structural basis for LIN54 recognition of CHR elements in cell
            cycle-regulated promoters
  JOURNAL   Nat Commun 7, 12301 (2016)
   PUBMED   27465258
  REMARK    GeneRIF: the DNA-binding properties of LIN54 and the structural
            basis for recognition of a cell cycle genes homology region
            sequence, are described.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Sadasivam,S. and DeCaprio,J.A.
  TITLE     The DREAM complex: master coordinator of cell cycle-dependent gene
            expression
  JOURNAL   Nat Rev Cancer 13 (8), 585-595 (2013)
   PUBMED   23842645
  REMARK    Review article
            Erratum:[Nat Rev Cancer. 2013 Oct;13(10):752]
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Matsuo,T., Kuramoto,H., Kumazaki,T., Mitsui,Y. and Takahashi,T.
  TITLE     LIN54 harboring a mutation in CHC domain is localized to the
            cytoplasm and inhibits cell cycle progression
  JOURNAL   Cell Cycle 11 (17), 3227-3236 (2012)
   PUBMED   22895175
  REMARK    GeneRIF: LIN54 harboring a mutation in CHC domain is localized to
            the cytoplasm and inhibits cell cycle progression.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Sadasivam,S., Duan,S. and DeCaprio,J.A.
  TITLE     The MuvB complex sequentially recruits B-Myb and FoxM1 to promote
            mitotic gene expression
  JOURNAL   Genes Dev 26 (5), 474-489 (2012)
   PUBMED   22391450
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Litovchick,L., Florens,L.A., Swanson,S.K., Washburn,M.P. and
            DeCaprio,J.A.
  TITLE     DYRK1A protein kinase promotes quiescence and senescence through
            DREAM complex assembly
  JOURNAL   Genes Dev 25 (8), 801-813 (2011)
   PUBMED   21498570
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Schmit,F., Cremer,S. and Gaubatz,S.
  TITLE     LIN54 is an essential core subunit of the DREAM/LINC complex that
            binds to the cdc2 promoter in a sequence-specific manner
  JOURNAL   FEBS J 276 (19), 5703-5716 (2009)
   PUBMED   19725879
  REMARK    GeneRIF: the cysteine-rich CXC domain of LIN54 is a novel
            DNA-binding domain that binds to the cdc2 promoter in a
            sequence-specific manner
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Litovchick,L., Sadasivam,S., Florens,L., Zhu,X., Swanson,S.K.,
            Velmurugan,S., Chen,R., Washburn,M.P., Liu,X.S. and DeCaprio,J.A.
  TITLE     Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
            complex represses human cell cycle-dependent genes in quiescence
  JOURNAL   Mol Cell 26 (4), 539-551 (2007)
   PUBMED   17531812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021105.13.
            
            Summary: LIN54 is a component of the LIN, or DREAM, complex, an
            essential regulator of cell cycle genes (Schmit et al., 2009
            [PubMed 19725879]).[supplied by OMIM, Dec 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 5' coding region, compared
            to variant 1. Variants 2, 3 and 7 encode the same isoform (b) which
            is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.126016.1,
                                           SRR1803611.2919.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..528
                     /product="protein lin-54 homolog isoform b"
                     /note="protein lin-54 homolog; CXC domain-containing
                     protein 1"
                     /calculated_mol_wt=56153
     Region          <26..>245
                     /region_name="SP1-4_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Proteins (SP) 1-4; cl41773"
                     /db_xref="CDD:425404"
     Region          301..>324
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     Region          375..410
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     CDS             1..528
                     /gene="LIN54"
                     /gene_synonym="CXCDC1; JC8.6; MIP120; TCX1"
                     /coded_by="NM_001115007.3:183..1769"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47089.1"
                     /db_xref="GeneID:132660"
                     /db_xref="HGNC:HGNC:25397"
                     /db_xref="MIM:613367"
ORIGIN      
        1 mevvpaeiak kprtptsgpv itklifakpi nskavtgqtt qvsppviagr vlsqstpgtp
       61 sktitisesg vigstlnstt qtpnkiaisp lkspnkavks tvqtitvggv stsqfktiip
      121 latapnvqqi qvpgskfhyv rlvtatsass stqpvsqnps tntqplqqak pvvvnttpvr
      181 msvpivsaqa vkqvvpkpin ptsqivttsq pqqrlimpat plpqiqpnlt nlppgtvlap
      241 apgtgnvgya vlpaqyvtql qqssyvsias nstftgtsgi qtqarlpfng iipsesasrp
      301 rkpcnctksl clklycdcfa ngefcnncnc tncynnlehe nerqkaikac ldrnpeafkp
      361 kigkgkeges drrhskgcnc krsgclknyc ecyeakimcs sickcigckn feesperktl
      421 mhladaaevr vqqqtaaktk lssqisdllt rptpalnsgg gklpftfvtk evaeatcncl
      481 laqaeqadkk gkskaaaerm ileefgrclm svinsagkak sdpcamnc
//
LOCUS       NP_006363                623 aa            linear   PRI 20-NOV-2025
DEFINITION  heterogeneous nuclear ribonucleoprotein Q isoform 1 [Homo sapiens].
ACCESSION   NP_006363
VERSION     NP_006363.4
DBSOURCE    REFSEQ: accession NM_006372.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Ishtayeh,H., Galves,M., Barnatan,T.T., Berdichevsky,Y.,
            Amer-Sarsour,F., Pasmanik-Chor,M., Braverman,I., Blumen,S.C. and
            Ashkenazi,A.
  TITLE     Oculopharyngeal muscular dystrophy mutations link the RNA-binding
            protein HNRNPQ to autophagosome biogenesis
  JOURNAL   Aging Cell 22 (10), e13949 (2023)
   PUBMED   37559347
  REMARK    GeneRIF: Oculopharyngeal muscular dystrophy mutations link the
            RNA-binding protein HNRNPQ to autophagosome biogenesis.
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Semino,F., Schroter,J., Willemsen,M.H., Bast,T., Biskup,S.,
            Beck-Woedl,S., Brennenstuhl,H., Schaaf,C.P., Kolker,S.,
            Hoffmann,G.F., Haack,T.B. and Syrbe,S.
  TITLE     Further evidence for de novo variants in SYNCRIP as the cause of a
            neurodevelopmental disorder
  JOURNAL   Hum Mutat 42 (9), 1094-1100 (2021)
   PUBMED   34157790
  REMARK    GeneRIF: Further evidence for de novo variants in SYNCRIP as the
            cause of a neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 623)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 623)
  AUTHORS   Mourelatos,Z., Abel,L., Yong,J., Kataoka,N. and Dreyfuss,G.
  TITLE     SMN interacts with a novel family of hnRNP and spliceosomal
            proteins
  JOURNAL   EMBO J 20 (19), 5443-5452 (2001)
   PUBMED   11574476
REFERENCE   6  (residues 1 to 623)
  AUTHORS   Lau,P.P., Chang,B.H. and Chan,L.
  TITLE     Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a
            component of apobec-1 editosome
  JOURNAL   Biochem Biophys Res Commun 282 (4), 977-983 (2001)
   PUBMED   11352648
REFERENCE   7  (residues 1 to 623)
  AUTHORS   Blanc,V., Navaratnam,N., Henderson,J.O., Anant,S., Kennedy,S.,
            Jarmuz,A., Scott,J. and Davidson,N.O.
  TITLE     Identification of GRY-RBP as an apolipoprotein B RNA-binding
            protein that interacts with both apobec-1 and apobec-1
            complementation factor to modulate C to U editing
  JOURNAL   J Biol Chem 276 (13), 10272-10283 (2001)
   PUBMED   11134005
REFERENCE   8  (residues 1 to 623)
  AUTHORS   Grosset,C., Chen,C.Y., Xu,N., Sonenberg,N., Jacquemin-Sablon,H. and
            Shyu,A.B.
  TITLE     A mechanism for translationally coupled mRNA turnover: interaction
            between the poly(A) tail and a c-fos RNA coding determinant via a
            protein complex
  JOURNAL   Cell 103 (1), 29-40 (2000)
   PUBMED   11051545
REFERENCE   9  (residues 1 to 623)
  AUTHORS   Mizutani,A., Fukuda,M., Ibata,K., Shiraishi,Y. and Mikoshiba,K.
  TITLE     SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
            ribonucleoprotein R, interacts with ubiquitous synaptotagmin
            isoforms
  JOURNAL   J Biol Chem 275 (13), 9823-9831 (2000)
   PUBMED   10734137
REFERENCE   10 (residues 1 to 623)
  AUTHORS   Harris,C.E., Boden,R.A. and Astell,C.R.
  TITLE     A novel heterogeneous nuclear ribonucleoprotein-like protein
            interacts with NS1 of the minute virus of mice
  JOURNAL   J Virol 73 (1), 72-80 (1999)
   PUBMED   9847309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF037448.1, AL136082.22,
            DA117533.1 and DB160837.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 29, 2009 this sequence version replaced NP_006363.3.
            
            Summary: This gene encodes a member of the cellular heterogeneous
            nuclear ribonucleoprotein (hnRNP) family. hnRNPs are RNA binding
            proteins that complex with heterogeneous nuclear RNA (hnRNA) and
            regulate alternative splicing, polyadenylation, and other aspects
            of mRNA metabolism and transport. The encoded protein plays a role
            in multiple aspects of mRNA maturation and is associated with
            several multiprotein complexes including the apoB RNA
            editing-complex and survival of motor neurons (SMN) complex.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the short arm of chromosome 20. [provided by
            RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF037448.1, AK222776.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369622.8/ ENSP00000358635.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.3"
     Protein         1..623
                     /product="heterogeneous nuclear ribonucleoprotein Q
                     isoform 1"
                     /note="NS1-associated protein 1; heterogeneous nuclear
                     ribonucleoprotein Q; glycine- and tyrosine-rich
                     RNA-binding protein"
                     /calculated_mol_wt=69472
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          23..107
                     /region_name="NURR_hnRNPQ"
                     /note="NURR (N-terminal unit for RNA recognition) domain
                     found in heterogeneous nuclear ribonucleoprotein Q
                     (hnRNPQ) and similar proteins; cd21066"
                     /db_xref="CDD:410954"
     Region          103..615
                     /region_name="hnRNP-R-Q"
                     /note="heterogeneous nuclear ribonucleoprotein R, Q
                     family; TIGR01648"
                     /db_xref="CDD:273732"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            363
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:12601080; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          400..561
                     /region_name="Interaction with APOBEC1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            444
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          448..559
                     /region_name="8 X 3 AA repeats of R-G-G"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Region          460..488
                     /region_name="3 X 4 AA repeats of Y-Y-G-Y"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            496
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          497..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            510
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          518..549
                     /region_name="Interaction with SMN.
                     /evidence=ECO:0000269|PubMed:11574476"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            518
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            526
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            536
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Site            539
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:23455924; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     Region          564..578
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O60506.2)"
     Site            587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O60506.2)"
     CDS             1..623
                     /gene="SYNCRIP"
                     /gene_synonym="GRY-RBP; GRYRBP; hnRNP-Q; HNRNPQ; HNRPQ1;
                     NSAP1; PP68"
                     /coded_by="NM_006372.5:103..1974"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5005.1"
                     /db_xref="GeneID:10492"
                     /db_xref="HGNC:HGNC:16918"
                     /db_xref="MIM:616686"
ORIGIN      
        1 matehvngng teepmdttsa vihsenfqtl ldaglpqkva ekldeiyvag lvahsdlder
       61 aiealkefne dgalavlqqf kdsdlshvqn ksaflcgvmk tyrqrekqgt kvadsskgpd
      121 eakikaller tgytldvttg qrkyggpppd svysgqqpsv gteifvgkip rdlfedelvp
      181 lfekagpiwd lrlmmdpltg lnrgyafvtf ctkeaaqeav klynnheirs gkhigvcisv
      241 annrlfvgsi pksktkeqil eefskvtegl tdvilyhqpd dkkknrgfcf leyedhktaa
      301 qarrrlmsgk vkvwgnvgtv ewadpiedpd pevmakvkvl fvrnlantvt eeilekafsq
      361 fgklervkkl kdyafihfde rdgavkamee mngkdlegen ieivfakppd qkrkerkaqr
      421 qaaknqmydd yyyygpphmp pptrgrgrgg rggygyppdy ygyedyydyy gydyhnyrgg
      481 yedpyygyed fqvgargrgg rgargaapsr grgaapprgr agysqrggpg sargvrgarg
      541 gaqqqrgrgv rgarggrggn vggkrkadgy nqpdskrrqt nnqnwgsqpi aqqplqggdh
      601 sgnygyksen qefyqdtfgq qwk
//
LOCUS       NP_001269201             489 aa            linear   PRI 20-NOV-2025
DEFINITION  set1/Ash2 histone methyltransferase complex subunit ASH2 isoform d
            [Homo sapiens].
ACCESSION   NP_001269201 XP_005273741
VERSION     NP_001269201.1
DBSOURCE    REFSEQ: accession NM_001282272.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Batbayar,G., Ishimura,A., Lyu,H., Wanna-Udom,S., Meguro-Horike,M.,
            Terashima,M., Horike,S.I., Takino,T. and Suzuki,T.
  TITLE     ASH2L, a COMPASS core subunit, is involved in the cell invasion and
            migration of triple-negative breast cancer cells through the
            epigenetic control of histone H3 lysine 4 methylation
  JOURNAL   Biochem Biophys Res Commun 669, 19-29 (2023)
   PUBMED   37262949
  REMARK    GeneRIF: ASH2L, a COMPASS core subunit, is involved in the cell
            invasion and migration of triple-negative breast cancer cells
            through the epigenetic control of histone H3 lysine 4 methylation.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Lee,Y.T., Ayoub,A., Park,S.H., Sha,L., Xu,J., Mao,F., Zheng,W.,
            Zhang,Y., Cho,U.S. and Dou,Y.
  TITLE     Mechanism for DPY30 and ASH2L intrinsically disordered regions to
            modulate the MLL/SET1 activity on chromatin
  JOURNAL   Nat Commun 12 (1), 2953 (2021)
   PUBMED   34012049
  REMARK    GeneRIF: Mechanism for DPY30 and ASH2L intrinsically disordered
            regions to modulate the MLL/SET1 activity on chromatin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Li,X., Qu,M., Zhang,J., Chen,K. and Ma,X.
  TITLE     CircASH2L facilitates tumor-like biologic behaviours and
            inflammation of fibroblast-like synoviocytes via miR-129-5p/HIPK2
            axis in rheumatoid arthritis
  JOURNAL   J Orthop Surg Res 16 (1), 302 (2021)
   PUBMED   33964939
  REMARK    GeneRIF: CircASH2L facilitates tumor-like biologic behaviours and
            inflammation of fibroblast-like synoviocytes via miR-129-5p/HIPK2
            axis in rheumatoid arthritis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Hughes,C.M., Rozenblatt-Rosen,O., Milne,T.A., Copeland,T.D.,
            Levine,S.S., Lee,J.C., Hayes,D.N., Shanmugam,K.S.,
            Bhattacharjee,A., Biondi,C.A., Kay,G.F., Hayward,N.K., Hess,J.L.
            and Meyerson,M.
  TITLE     Menin associates with a trithorax family histone methyltransferase
            complex and with the hoxc8 locus
  JOURNAL   Mol Cell 13 (4), 587-597 (2004)
   PUBMED   14992727
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Wysocka,J., Myers,M.P., Laherty,C.D., Eisenman,R.N. and Herr,W.
  TITLE     Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone
            H3-K4 methyltransferase are tethered together selectively by the
            cell-proliferation factor HCF-1
  JOURNAL   Genes Dev 17 (7), 896-911 (2003)
   PUBMED   12670868
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Wang,J., Zhou,Y., Yin,B., Du,G., Huang,X., Li,G., Shen,Y., Yuan,J.
            and Qiang,B.
  TITLE     ASH2L: alternative splicing and downregulation during induced
            megakaryocytic differentiation of multipotential leukemia cell
            lines
  JOURNAL   J Mol Med (Berl) 79 (7), 399-405 (2001)
   PUBMED   11466562
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Ikegawa,S., Isomura,M., Koshizuka,Y. and Nakamura,Y.
  TITLE     Cloning and characterization of ASH2L and Ash2l, human and mouse
            homologs of the Drosophila ash2 gene
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 167-172 (1999)
   PUBMED   10393421
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC353644.1, AK298483.1 and AC084024.17.
            
            On Aug 27, 2013 this sequence version replaced XP_005273741.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (d) has a shorter N-terminus, compared to isoform
            a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.194453.1, AK298483.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.23"
     Protein         1..489
                     /product="set1/Ash2 histone methyltransferase complex
                     subunit ASH2 isoform d"
                     /note="set1/Ash2 histone methyltransferase complex subunit
                     ASH2; ASH2-like protein; ash2 (absent, small, or
                     homeotic)-like"
                     /calculated_mol_wt=55194
     Region          253..444
                     /region_name="SPRY_Ash2"
                     /note="SPRY domain in Ash2; cd12872"
                     /db_xref="CDD:293932"
     CDS             1..489
                     /gene="ASH2L"
                     /gene_synonym="ASH2; ASH2L1; ASH2L2; Bre2"
                     /coded_by="NM_001282272.1:330..1799"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS64872.1"
                     /db_xref="GeneID:9070"
                     /db_xref="HGNC:HGNC:744"
                     /db_xref="MIM:604782"
ORIGIN      
        1 mtnysfhcnv chhsgntyfl rkqanlkemc lsalanltwq srtqdehpkt mfskdkdiip
       61 fidkywecmt trqrpgkmtw pnnivktmsk erdvflvkeh pdpgskdpee dypkfglldq
      121 dlsnigpayd nqkqssavst sgnlnggiaa gssgkgrgak rkqqdggttg ttkkarsdpl
      181 fsaqrlpphg yplehpfnkd gyryilaepd phapdpekle ldcwagkpip gdlyraclye
      241 rvllalhdra pqlkisddrl tvvgekgysm vrashgvrkg awyfeitvde mppdtaarlg
      301 wsqplgnlqa plgydkfsys wrskkgtkfh qsigkhyssg ygqgdvlgfy inlpedteta
      361 kslpdtykdk alikfksyly feekdfvdka ekslkqtphs eiifykngvn qgvaykdife
      421 gvyfpaisly ksctvsinfg pcfkyppkdl tyrpmsdmgw gavvehtlad vlyhvetevd
      481 grrsppwep
//
LOCUS       NP_001026850             429 aa            linear   PRI 20-NOV-2025
DEFINITION  runt-related transcription factor 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001026850
VERSION     NP_001026850.1
DBSOURCE    REFSEQ: accession NM_001031680.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Samsa,W.E., Zhang,Z. and Gong,Z.
  TITLE     CBFbeta Regulates RUNX3 ADP-Ribosylation to Mediate Homologous
            Recombination Repair
  JOURNAL   J Cell Physiol 240 (1), e31503 (2025)
   PUBMED   39696918
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wang,J., Wang,J., Zhang,J., Gong,H., Li,J., Song,Y., Huang,Y.,
            Ma,B., Gu,W. and Yang,R.
  TITLE     Association between the methylations of RUNX3 in peripheral blood
            and lung cancer: a case-control study
  JOURNAL   Biomarkers 29 (6), 343-351 (2024)
   PUBMED   38923933
  REMARK    GeneRIF: Association between the methylations of RUNX3 in
            peripheral blood and lung cancer: a case-control study.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhao,B., Xia,Z., Yang,B., Guo,Y., Zhou,R., Gu,M., Liu,M., Li,Q.,
            Bai,W., Huang,J., Zhang,X., Zhu,C., Leung,K.T., Chen,C. and Dong,J.
  TITLE     USP7 promotes IgA class switching through stabilizing RUNX3 for
            germline transcription activation
  JOURNAL   Cell Rep 43 (5), 114194 (2024)
   PUBMED   38735043
  REMARK    GeneRIF: USP7 promotes IgA class switching through stabilizing
            RUNX3 for germline transcription activation.
            Erratum:[Cell Rep. 2024 Jun 25;43(6):114315. doi:
            10.1016/j.celrep.2024.114315. PMID: 38795349]
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Wang,N., Miao,X., Lu,W., Ji,Y., Zheng,Y., Meng,D., Liu,H. and
            Xiang,C.
  TITLE     RUNX3 exerts tumor-suppressive role through inhibiting EXOSC4
            expression
  JOURNAL   Funct Integr Genomics 24 (3), 103 (2024)
   PUBMED   38913281
  REMARK    GeneRIF: RUNX3 exerts tumor-suppressive role through inhibiting
            EXOSC4 expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Zheng,G., Ye,H., Bai,J. and Zhang,X.
  TITLE     Downregulation of lncRNA MIR17HG reduced tumorigenicity and
            Treg-mediated immune escape of non-small-cell lung cancer cells
            through targeting the miR-17-5p/RUNX3 axis
  JOURNAL   J Biochem Mol Toxicol 38 (5), e23715 (2024)
   PUBMED   38704830
  REMARK    GeneRIF: Downregulation of lncRNA MIR17HG reduced tumorigenicity
            and Treg-mediated immune escape of non-small-cell lung cancer cells
            through targeting the miR-17-5p/RUNX3 axis.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Levanon,D., Goldstein,R.E., Bernstein,Y., Tang,H., Goldenberg,D.,
            Stifani,S., Paroush,Z. and Groner,Y.
  TITLE     Transcriptional repression by AML1 and LEF-1 is mediated by the
            TLE/Groucho corepressors
  JOURNAL   Proc Natl Acad Sci U S A 95 (20), 11590-11595 (1998)
   PUBMED   9751710
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Wijmenga,C., Speck,N.A., Dracopoli,N.C., Hofker,M.H., Liu,P. and
            Collins,F.S.
  TITLE     Identification of a new murine runt domain-containing gene, Cbfa3,
            and localization of the human homolog, CBFA3, to chromosome
            1p35-pter
  JOURNAL   Genomics 26 (3), 611-614 (1995)
   PUBMED   7607690
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Levanon,D., Negreanu,V., Bernstein,Y., Bar-Am,I., Avivi,L. and
            Groner,Y.
  TITLE     AML1, AML2, and AML3, the human members of the runt domain
            gene-family: cDNA structure, expression, and chromosomal
            localization
  JOURNAL   Genomics 23 (2), 425-432 (1994)
   PUBMED   7835892
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Bae,S.C., Yamaguchi-Iwai,Y., Ogawa,E., Maruyama,M., Inuzuka,M.,
            Kagoshima,H., Shigesada,K., Satake,M. and Ito,Y.
  TITLE     Isolation of PEBP2 alpha B cDNA representing the mouse homolog of
            human acute myeloid leukemia gene, AML1
  JOURNAL   Oncogene 8 (3), 809-814 (1993)
   PUBMED   8437866
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA935726.1, BC013362.2,
            AL023096.1 and AI375031.1.
            
            Summary: This gene encodes a member of the runt domain-containing
            family of transcription factors. A heterodimer of this protein and
            a beta subunit forms a complex that binds to the core DNA sequence
            5'-PYGPYGGT-3' found in a number of enhancers and promoters, and
            can either activate or suppress transcription. It also interacts
            with other transcription factors. It functions as a tumor
            suppressor, and the gene is frequently deleted or transcriptionally
            silenced in cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1), also known as p46, represents
            the longest transcript and encodes the longer isoform (1). Variants
            1 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC013362.2 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..429
                     /product="runt-related transcription factor 3 isoform 1"
                     /note="core-binding factor, runt domain, alpha subunit 3;
                     transcription factor AML2; acute myeloid leukemia gene 2;
                     polyomavirus enhancer-binding protein 2 alpha C subunit;
                     PEA2 alpha C; PEBP2 alpha C; CBF-alpha-3; oncogene AML-2;
                     acute myeloid leukemia 2 protein; core-binding factor
                     subunit alpha-3; SL3-3 enhancer factor 1 alpha C subunit;
                     SL3/AKV core-binding factor alpha C subunit; runt related
                     transcription factor 3"
                     /calculated_mol_wt=45791
     Region          69..197
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <191..325
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          330..429
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..429
                     /gene="RUNX3"
                     /gene_synonym="AML2; CBFA3; PEBP2aC"
                     /coded_by="NM_001031680.2:440..1729"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30633.1"
                     /db_xref="GeneID:864"
                     /db_xref="HGNC:HGNC:10473"
                     /db_xref="MIM:600210"
ORIGIN      
        1 masnsifdsf ptysptfird pstsrrftpp spafpcgggg gkmgensgal saqaavgpgg
       61 rarpevrsmv dvladhagel vrtdspnflc svlpshwrcn ktlpvafkvv algdvpdgtv
      121 vtvmagnden ysaelrnasa vmknqvarfn dlrfvgrsgr gksftltitv ftnptqvaty
      181 hraikvtvdg preprrhrqk ledqtkpfpd rfgdlerlrm rvtpstpspr gslsttshfs
      241 sqpqtpiqgt selnpfsdpr qfdrsfptlp tltesrfpdp rmhypgamsa afpysatpsg
      301 tsisslsvag mpatsrfhht ylpppypgap qnqsgpfqan pspyhlyygt ssgsyqfsmv
      361 agsssggdrs ptrmlascts saasvaagnl mnpslggqsd gveadgshsn sptalstpgr
      421 mdeavwrpy
//
LOCUS       NP_000421                410 aa            linear   PRI 20-NOV-2025
DEFINITION  platelet-activating factor acetylhydrolase IB subunit beta [Homo
            sapiens].
ACCESSION   NP_000421
VERSION     NP_000421.1
DBSOURCE    REFSEQ: accession NM_000430.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Feng,W.X., Wang,X.F., Wu,Y., Li,X.M., Chen,S.H., Wang,X.H.,
            Wang,Z.H., Fang,F. and Chen,C.H.
  TITLE     Clinical analysis of PAFAH1B1 gene variants in pediatric patients
            with epilepsy
  JOURNAL   Seizure 117, 98-104 (2024)
   PUBMED   38364333
  REMARK    GeneRIF: Clinical analysis of PAFAH1B1 gene variants in pediatric
            patients with epilepsy.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Singh,K., Lau,C.K., Manigrasso,G., Gama,J.B., Gassmann,R. and
            Carter,A.P.
  TITLE     Molecular mechanism of dynein-dynactin complex assembly by LIS1
  JOURNAL   Science 383 (6690), eadk8544 (2024)
   PUBMED   38547289
  REMARK    GeneRIF: Molecular mechanism of dynein-dynactin complex assembly by
            LIS1.
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Mitevska,O., Lam,P.W., Daly,L. and Auckland,P.
  TITLE     Lis1-dynein drives corona compaction and limits erroneous
            microtubule attachment at kinetochores
  JOURNAL   J Cell Sci 136 (5) (2023)
   PUBMED   36274587
  REMARK    GeneRIF: Lis1-dynein drives corona compaction and limits erroneous
            microtubule attachment at kinetochores.
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Reimer,J.M., DeSantis,M.E., Reck-Peterson,S.L. and Leschziner,A.E.
  TITLE     Structures of human dynein in complex with the lissencephaly 1
            protein, LIS1
  JOURNAL   Elife 12, e84302 (2023)
   PUBMED   36692009
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Mizuguchi,M., Takashima,S., Kakita,A., Yamada,M. and Ikeda,K.
  TITLE     Lissencephaly gene product. Localization in the central nervous
            system and loss of immunoreactivity in Miller-Dieker syndrome
  JOURNAL   Am J Pathol 147 (4), 1142-1151 (1995)
   PUBMED   7573359
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Hattori,M., Adachi,H., Tsujimoto,M., Arai,H. and Inoue,K.
  TITLE     Miller-Dieker lissencephaly gene encodes a subunit of brain
            platelet-activating factor acetylhydrolase [corrected]
  JOURNAL   Nature 370 (6486), 216-218 (1994)
   PUBMED   8028668
  REMARK    Erratum:[Nature 1994 Aug 4;370(6488):391]
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Reiner,O., Carrozzo,R., Shen,Y., Wehnert,M., Faustinella,F.,
            Dobyns,W.B., Caskey,C.T. and Ledbetter,D.H.
  TITLE     Isolation of a Miller-Dieker lissencephaly gene containing G
            protein beta-subunit-like repeats
  JOURNAL   Nature 364 (6439), 717-721 (1993)
   PUBMED   8355785
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Brock,S., Dobyns,W.B. and Jansen,A.
  TITLE     PAFAH1B1-Related Lissencephaly / Subcortical Band Heterotopia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301752
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC015799.23 and AC005696.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This locus was identified as encoding a gene that when
            mutated or lost caused the lissencephaly associated with
            Miller-Dieker lissencephaly syndrome. This gene encodes the
            non-catalytic alpha subunit of the intracellular Ib isoform of
            platelet-activating factor acteylhydrolase, a heterotrimeric enzyme
            that specifically catalyzes the removal of the acetyl group at the
            SN-2 position of platelet-activating factor (identified as
            1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). Two other
            isoforms of intracellular platelet-activating factor
            acetylhydrolase exist: one composed of multiple subunits, the
            other, a single subunit. In addition, a single-subunit isoform of
            this enzyme is found in serum. [provided by RefSeq, Apr 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.179163.1,
                                           SRR1660809.209848.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397195.10/ ENSP00000380378.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..410
                     /product="platelet-activating factor acetylhydrolase IB
                     subunit beta"
                     /EC_number="3.1.1.47"
                     /note="lissencephaly 1 protein; platelet-activating factor
                     acetylhydrolase 1b, regulatory subunit 1 (45kDa)"
                     /calculated_mol_wt=46507
     Region          1..102
                     /region_name="Interaction with NDEL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     Region          1..66
                     /region_name="Interaction with NDE1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     Region          1..38
                     /region_name="Required for self-association and
                     interaction with PAFAH1B2 and PAFAH1B3.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     Region          7..39
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P43034.2)"
     Region          83..410
                     /region_name="Interaction with dynein and dynactin"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     Region          104..408
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(107,125,129,135..136,148..149,167,171,177..178,
                     190..191,208,213,219..220,233,250,255,261..262,274..275,
                     313,317,323..324,336..337,354,359,365..366,378..379,397,
                     401,407..408)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P43034.2)"
     Region          111..148
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          154..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          195..231
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          238..273
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          279..335
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          341..377
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          367..409
                     /region_name="Interaction with DCX.
                     /evidence=ECO:0000269|PubMed:11001923"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     Region          383..407
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          388..410
                     /region_name="Interaction with NDEL1.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03141"
                     /note="propagated from UniProtKB/Swiss-Prot (P43034.2)"
     CDS             1..410
                     /gene="PAFAH1B1"
                     /gene_synonym="LIS1; LIS2; MDCR; MDS; NudF; PAFAH"
                     /coded_by="NM_000430.4:544..1776"
                     /db_xref="CCDS:CCDS32528.1"
                     /db_xref="GeneID:5048"
                     /db_xref="HGNC:HGNC:8574"
                     /db_xref="MIM:601545"
ORIGIN      
        1 mvlsqrqrde lnraiadylr sngyeeaysv fkkeaeldvn eeldkkyagl lekkwtsvir
       61 lqkkvmeles klneakeeft sggplgqkrd pkewiprppe kyalsghrsp vtrvifhpvf
      121 svmvsaseda tikvwdyetg dfertlkght dsvqdisfdh sgkllascsa dmtiklwdfq
      181 gfecirtmhg hdhnvssvai mpngdhivsa srdktikmwe vqtgycvktf tghrewvrmv
      241 rpnqdgtlia scsndqtvrv wvvatkecka elrehehvve ciswapessy ssiseatgse
      301 tkksgkpgpf llsgsrdkti kmwdvstgmc lmtlvghdnw vrgvlfhsgg kfilscaddk
      361 tlrvwdyknk rcmktlnahe hfvtsldfhk tapyvvtgsv dqtvkvwecr
//
LOCUS       NP_002011               1298 aa            linear   PRI 20-NOV-2025
DEFINITION  vascular endothelial growth factor receptor 3 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_002011
VERSION     NP_002011.2
DBSOURCE    REFSEQ: accession NM_002020.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Zhang,Y., Dong,X., Zhang,J., Zhao,M., Wang,J., Chu,J., Yang,Z.,
            Ma,S., Lin,K., Sun,H. and Luo,Z.
  TITLE     FLT4 gene polymorphisms influence isolated ventricular septal
            defect predisposition in a Southwest China population
  JOURNAL   BMC Med Genomics 17 (1), 197 (2024)
   PUBMED   39107825
  REMARK    GeneRIF: FLT4 gene polymorphisms influence isolated ventricular
            septal defect predisposition in a Southwest China population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Schmidt,A., Hrupka,B., van Bebber,F., Sunil Kumar,S., Feng,X.,
            Tschirner,S.K., Assfalg,M., Muller,S.A., Hilger,L.S., Hofmann,L.I.,
            Pigoni,M., Jocher,G., Voytyuk,I., Self,E.L., Ito,M., Hyakkoku,K.,
            Yoshimura,A., Horiguchi,N., Feederle,R., De Strooper,B.,
            Schulte-Merker,S., Lammert,E., Moechars,D., Schmid,B. and
            Lichtenthaler,S.F.
  TITLE     The Alzheimer's disease-linked protease BACE2 cleaves VEGFR3 and
            modulates its signaling
  JOURNAL   J Clin Invest 134 (16), e170550 (2024)
   PUBMED   38888964
  REMARK    GeneRIF: The Alzheimer's disease-linked protease BACE2 cleaves
            VEGFR3 and modulates its signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Fournier,E., Dubreuil,P., Birnbaum,D. and Borg,J.P.
  TITLE     Mutation at tyrosine residue 1337 abrogates ligand-dependent
            transforming capacity of the FLT4 receptor
  JOURNAL   Oncogene 11 (5), 921-931 (1995)
   PUBMED   7675451
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Borg,J.P., deLapeyriere,O., Noguchi,T., Rottapel,R., Dubreuil,P.
            and Birnbaum,D.
  TITLE     Biochemical characterization of two isoforms of FLT4, a VEGF
            receptor-related tyrosine kinase
  JOURNAL   Oncogene 10 (5), 973-984 (1995)
   PUBMED   7898938
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Pajusola,K., Aprelikova,O., Armstrong,E., Morris,S. and Alitalo,K.
  TITLE     Two human FLT4 receptor tyrosine kinase isoforms with distinct
            carboxy terminal tails are produced by alternative processing of
            primary transcripts
  JOURNAL   Oncogene 8 (11), 2931-2937 (1993)
   PUBMED   7692369
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Galland,F., Karamysheva,A., Pebusque,M.J., Borg,J.P., Rottapel,R.,
            Dubreuil,P., Rosnet,O. and Birnbaum,D.
  TITLE     The FLT4 gene encodes a transmembrane tyrosine kinase related to
            the vascular endothelial growth factor receptor
  JOURNAL   Oncogene 8 (5), 1233-1240 (1993)
   PUBMED   8386825
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Van Zanten,M., Mansour,S., Ostergaard,P., Mortimer,P. and Gordon,K.
  TITLE     Milroy Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301417
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Pajusola,K., Aprelikova,O., Korhonen,J., Kaipainen,A.,
            Pertovaara,L., Alitalo,R. and Alitalo,K.
  TITLE     FLT4 receptor tyrosine kinase contains seven immunoglobulin-like
            loops and is expressed in multiple human tissues and cell lines
  JOURNAL   Cancer Res 52 (20), 5738-5743 (1992)
   PUBMED   1327515
  REMARK    Erratum:[Cancer Res 1993 Aug 15;53(16):3845]
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Galland,F., Karamysheva,A., Mattei,M.G., Rosnet,O., Marchetto,S.
            and Birnbaum,D.
  TITLE     Chromosomal localization of FLT4, a novel receptor-type tyrosine
            kinase gene
  JOURNAL   Genomics 13 (2), 475-478 (1992)
   PUBMED   1319394
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Aprelikova,O., Pajusola,K., Partanen,J., Armstrong,E., Alitalo,R.,
            Bailey,S.K., McMahon,J., Wasmuth,J., Huebner,K. and Alitalo,K.
  TITLE     FLT4, a novel class III receptor tyrosine kinase in chromosome
            5q33-qter
  JOURNAL   Cancer Res 52 (3), 746-748 (1992)
   PUBMED   1310071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455035.2, X68203.1,
            AY233382.1 and AC122714.2.
            
            On May 27, 2006 this sequence version replaced NP_002011.1.
            
            Summary: This gene encodes a tyrosine kinase receptor for vascular
            endothelial growth factors C and D. The protein is thought to be
            involved in lymphangiogenesis and maintenance of the lymphatic
            endothelium. Mutations in this gene cause hereditary lymphedema
            type IA. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an alternate 3'
            terminal exon compared to variant 1. This results in an isoform (2)
            with a shorter C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291679.1, AY233382.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..1298
                     /product="vascular endothelial growth factor receptor 3
                     isoform 2 precursor"
                     /EC_number="2.7.10.1"
                     /note="vascular endothelial growth factor receptor 3; VEGF
                     receptor-3; Feline McDonough Sarcoma (FMS)-like tyrosine
                     kinase 4; fms related tyrosine kinase 4; primary
                     congenital lymphedema; fms-like tyrosine kinase 4;
                     tyrosine-protein kinase receptor FLT4"
                     /calculated_mol_wt=143058
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2559
     mat_peptide     25..1298
                     /product="vascular endothelial growth factor receptor 3
                     isoform 2"
                     /calculated_mol_wt=143058
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Region          137..224
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          230..329
                     /region_name="IgI_VEGFR"
                     /note="Immunoglobulin (Ig)-like domain of vascular
                     endothelial growth factor (VEGF) receptor(R); member of
                     the I-set of IgSF domains; cd05862"
                     /db_xref="CDD:409448"
     Region          230..234
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409448"
     Region          240..244
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409448"
     Region          246..255
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409448"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          262..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409448"
     Region          270..272
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409448"
     Region          276..284
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409448"
     Region          289..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409448"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          307..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409448"
     Region          318..324
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409448"
     Region          331..418
                     /region_name="IgI_VEGFR-3"
                     /note="Immunoglobulin (Ig)-like domain of vascular
                     endothelial growth factor receptor 3 (VEGFR-3); member of
                     the I-set of Ig superfamily (IgSF) domains; cd05863"
                     /db_xref="CDD:409449"
     Region          332..337
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409449"
     Region          342..347
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409449"
     Region          349..360
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409449"
     Region          364..370
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409449"
     Region          372..375
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409449"
     Region          378..380
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409449"
     Region          382..387
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409449"
     Region          395..403
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409449"
     Region          409..418
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409449"
     Site            411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            527
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          559..655
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          678..765
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            683
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          695..699
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          708..712
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          731..735
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          745..750
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            758
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          770..804
                     /region_name="VEGFR-2_TMD"
                     /note="VEGFR-2 Transmembrane domain; pfam17988"
                     /db_xref="CDD:375470"
     Site            776..796
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35916.3)"
     Site            830
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            833
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          837..1176
                     /region_name="PTKc_VEGFR3"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Vascular Endothelial Growth Factor Receptor 3; cd05102"
                     /db_xref="CDD:270680"
     Site            order(851..855,859,877..879,896,925,927..931,933..934,
                     1028,1035,1037,1041..1042,1044,1054..1056,1073..1077,1086,
                     1121)
                     /site_type="active"
                     /db_xref="CDD:270680"
     Site            order(851..853,859,877..879,896,925,927..931,933..934,
                     1028,1035,1044,1054..1056)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270680"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            order(1037,1041,1073..1077,1086,1121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270680"
     Site            1054..1079
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270680"
     Site            1063
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis and SRC.
                     /evidence=ECO:0000269|PubMed:16076871,
                     ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16076871,
                     ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528,
                     ECO:0000269|PubMed:16076871; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528,
                     ECO:0000269|PubMed:16076871; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1265
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     CDS             1..1298
                     /gene="FLT4"
                     /gene_synonym="CHTD7; FLT-4; FLT41; LMPH1A; LMPHM1; PCL;
                     VEGFR-3; VEGFR3"
                     /coded_by="NM_002020.5:56..3952"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS43412.1"
                     /db_xref="GeneID:2324"
                     /db_xref="HGNC:HGNC:3767"
                     /db_xref="MIM:136352"
ORIGIN      
        1 mqrgaalclr lwlclglldg lvsgysmtpp tlniteeshv idtgdslsis crgqhplewa
       61 wpgaqeapat gdkdsedtgv vrdcegtdar pyckvlllhe vhandtgsyv cyykyikari
      121 egttaassyv fvrdfeqpfi nkpdtllvnr kdamwvpclv sipglnvtlr sqssvlwpdg
      181 qevvwddrrg mlvstpllhd alylqcettw gdqdflsnpf lvhitgnely diqllprksl
      241 ellvgeklvl nctvwaefns gvtfdwdypg kqaergkwvp errsqqthte lssiltihnv
      301 sqhdlgsyvc kanngiqrfr estevivhen pfisvewlkg pileatagde lvklpvklaa
      361 ypppefqwyk dgkalsgrhs phalvlkevt eastgtytla lwnsaaglrr nislelvvnv
      421 ppqihekeas spsiysrhsr qaltctaygv plplsiqwhw rpwtpckmfa qrslrrrqqq
      481 dlmpqcrdwr avttqdavnp iesldtwtef vegknktvsk lviqnanvsa mykcvvsnkv
      541 gqderliyfy vttipdgfti eskpseelle gqpvllscqa dsykyehlrw yrlnlstlhd
      601 ahgnpllldc knvhlfatpl aasleevapg arhatlslsi prvapehegh yvcevqdrrs
      661 hdkhchkkyl svqaleaprl tqnltdllvn vsdslemqcl vagahapsiv wykderllee
      721 ksgvdladsn qklsiqrvre edagrylcsv cnakgcvnss asvavegsed kgsmeivilv
      781 gtgviavffw vllllifcnm rrpahadikt gylsiimdpg evpleeqcey lsydasqwef
      841 prerlhlgrv lgygafgkvv easafgihkg sscdtvavkm lkegataseh ralmselkil
      901 ihignhlnvv nllgactkpq gplmvivefc kygnlsnflr akrdafspca ekspeqrgrf
      961 ramvelarld rrrpgssdrv lfarfskteg garraspdqe aedlwlsplt medlvcysfq
     1021 vargmeflas rkcihrdlaa rnillsesdv vkicdfglar diykdpdyvr kgsarlplkw
     1081 mapesifdkv yttqsdvwsf gvllweifsl gaspypgvqi neefcqrlrd gtrmrapela
     1141 tpairrimln cwsgdpkarp afselveilg dllqgrglqe eeevcmaprs sqsseegsfs
     1201 qvstmalhia qadaedspps lqrhslaary ynwvsfpgcl argaetrgss rmktfeefpm
     1261 tpttykgsvd nqtdsgmvla seefeqiesr hrqesgfr
//
LOCUS       NP_113661                431 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 81 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_113661
VERSION     NP_113661.2
DBSOURCE    REFSEQ: accession NM_031473.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Zhou,Z., Qiu,H., Castro-Araya,R.F., Takei,R., Nakayama,K. and
            Katoh,Y.
  TITLE     Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome
  JOURNAL   Hum Mol Genet 31 (10), 1681-1693 (2022)
   PUBMED   34888642
  REMARK    GeneRIF: Impaired cooperation between IFT74/BBS22-IFT81 and
            IFT25-IFT27/BBS19 causes Bardet-Biedl syndrome.
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Perrault,I., Halbritter,J., Porath,J.D., Gerard,X., Braun,D.A.,
            Gee,H.Y., Fathy,H.M., Saunier,S., Cormier-Daire,V., Thomas,S.,
            Attie-Bitach,T., Boddaert,N., Taschner,M., Schueler,M.,
            Lorentzen,E., Lifton,R.P., Lawson,J.A., Garfa-Traore,M., Otto,E.A.,
            Bastin,P., Caillaud,C., Kaplan,J., Rozet,J.M. and Hildebrandt,F.
  TITLE     IFT81, encoding an IFT-B core protein, as a very rare cause of a
            ciliopathy phenotype
  JOURNAL   J Med Genet 52 (10), 657-665 (2015)
   PUBMED   26275418
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Bhogaraju,S., Cajanek,L., Fort,C., Blisnick,T., Weber,K.,
            Taschner,M., Mizuno,N., Lamla,S., Bastin,P., Nigg,E.A. and
            Lorentzen,E.
  TITLE     Molecular basis of tubulin transport within the cilium by IFT74 and
            IFT81
  JOURNAL   Science 341 (6149), 1009-1012 (2013)
   PUBMED   23990561
  REMARK    GeneRIF: this study found that the two core intraflagellar
            transport proteins IFT74 and IFT81 form a tubulin-binding module
            and mapped the interaction to a calponin homology domain of IFT81
            and a highly basic domain in IFT74.
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Peng,J., Yu,L., Horiuchi,M., Zhang,P., Huang,X., Zhang,Y., Li,D.,
            Jalil,M.A. and Zhao,S.
  TITLE     Identification of human CDV-1R and mouse Cdv-1R, two novel proteins
            with putative signal peptides, especially highly expressed in
            testis and increased with the male sex maturation
  JOURNAL   Mol Biol Rep 29 (4), 353-362 (2002)
   PUBMED   12549821
  REMARK    GeneRIF: inconsistent expression levels of human CDV-1 and mouse
            Cdv-1 in heart implied that cardiac hypertrophy in human SCD might
            not be associated with the abnormal expression of CDV-1
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Higashi,M., Kobayashi,K., Iijima,M., Wakana,S., Horiuchi,M.,
            Yasuda,T., Yoshida,G., Kanmura,Y. and Saheki,T.
  TITLE     Genomic organization and mapping of mouse CDV (carnitine
            deficiency-associated gene expressed in ventricle)-1 and its
            related CDV-1R gene
  JOURNAL   Mamm Genome 11 (12), 1053-1057 (2000)
   PUBMED   11130971
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP351086.1, AF332010.1,
            BC108257.1 and AC007546.6.
            
            On Aug 25, 2003 this sequence version replaced NP_113661.1.
            
            Summary: The protein encoded by this gene, together with IFT74,
            forms a tubulin-binding module of intraflagellar transport complex
            B. This module is involved in transport of tubulin within the
            cilium, and the encoded protein is required for ciliogenesis.
            Mutations in this gene are a cause of short-rib polydactyly
            syndromes. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            Variants 2 and 4 both encode isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004536.2, SRR1660809.135951.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..431
                     /product="intraflagellar transport protein 81 homolog
                     isoform 2"
                     /note="carnitine deficiency-associated gene expressed in
                     ventricle 1; intraflagellar transport protein 81 homolog;
                     carnitine deficiency-associated protein expressed in
                     ventricle 1"
                     /calculated_mol_wt=50110
     Region          2..121
                     /region_name="CH (calponin-homology)-like region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Region          3..126
                     /region_name="IFT81_CH"
                     /note="Intraflagellar transport 81 calponin homology
                     domain; pfam18383"
                     /db_xref="CDD:465736"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (Q8WYA0.1)"
     Region          <142..>407
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..431
                     /gene="IFT81"
                     /gene_synonym="CDV-1; CDV-1R; CDV1; CDV1R; DV1; SRTD19"
                     /coded_by="NM_031473.4:527..1822"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9142.1"
                     /db_xref="GeneID:28981"
                     /db_xref="HGNC:HGNC:14313"
                     /db_xref="MIM:605489"
ORIGIN      
        1 msdqikfimd slnkepfrkn ynlitfdsle pmqllqvlsd vlaeidpkql vdireempeq
       61 takrmlsllg ilkykpsgna tdmstfrqgl vigskpviyp vlhwllqrtn elkkraylar
      121 fliklevpse flqdetvadt nkqyeelmea fktlhkeyeq lkisgfstae irkdisamee
      181 ekdqlikrve hlkkrvetaq nhqwmlkiar qlrvekeree ylaqqkqeqk nqlfhavqrl
      241 qrvqnqlksm rqaaadakpe slmkrleeei kfnlymvtek fpkelenkkk elhflqkvvs
      301 epamghsdll eleskinein teinqliekk mmrnepiegk lslyrqqasi isrkkeakae
      361 elqeakekla slereasvkr nqtrefdgte vlkgderqdl tlsprlecgg vimaycslkl
      421 lgssdpptsa s
//
LOCUS       NP_001171714            1353 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001171714
VERSION     NP_001171714.1
DBSOURCE    REFSEQ: accession NM_001184785.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1353)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1353)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1353)
  AUTHORS   Zhang,J., Shi,Y., Ding,K., Yu,W., He,J. and Sun,B.
  TITLE     DCAF1 interacts with PARD3 to promote hepatocellular carcinoma
            progression and metastasis by activating the Akt signaling pathway
  JOURNAL   J Exp Clin Cancer Res 43 (1), 136 (2024)
   PUBMED   38711082
  REMARK    GeneRIF: DCAF1 interacts with PARD3 to promote hepatocellular
            carcinoma progression and metastasis by activating the Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1353)
  AUTHORS   Wu,J., Tan,H.Y., Chan,Y.T., Lu,Y., Feng,Z., Yuan,H., Zhang,C.,
            Feng,Y. and Wang,N.
  TITLE     PARD3 drives tumorigenesis through activating Sonic Hedgehog
            signalling in tumour-initiating cells in liver cancer
  JOURNAL   J Exp Clin Cancer Res 43 (1), 42 (2024)
   PUBMED   38317186
  REMARK    GeneRIF: PARD3 drives tumorigenesis through activating Sonic
            Hedgehog signalling in tumour-initiating cells in liver cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1353)
  AUTHORS   Gunji,D., Narumi,R., Muraoka,S., Isoyama,J., Ikemoto,N., Ishida,M.,
            Tomonaga,T., Sakai,Y., Obama,K. and Adachi,J.
  TITLE     Integrative analysis of cancer dependency data and comprehensive
            phosphoproteomics data revealed the EPHA2-PARD3 axis as a cancer
            vulnerability in KRAS-mutant colorectal cancer
  JOURNAL   Mol Omics 19 (8), 624-639 (2023)
   PUBMED   37232035
  REMARK    GeneRIF: Integrative analysis of cancer dependency data and
            comprehensive phosphoproteomics data revealed the EPHA2-PARD3 axis
            as a cancer vulnerability in KRAS-mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1353)
  AUTHORS   Ebnet,K., Suzuki,A., Horikoshi,Y., Hirose,T., Meyer Zu
            Brickwedde,M.K., Ohno,S. and Vestweber,D.
  TITLE     The cell polarity protein ASIP/PAR-3 directly associates with
            junctional adhesion molecule (JAM)
  JOURNAL   EMBO J 20 (14), 3738-3748 (2001)
   PUBMED   11447115
REFERENCE   7  (residues 1 to 1353)
  AUTHORS   Suzuki,A., Yamanaka,T., Hirose,T., Manabe,N., Mizuno,K.,
            Shimizu,M., Akimoto,K., Izumi,Y., Ohnishi,T. and Ohno,S.
  TITLE     Atypical protein kinase C is involved in the evolutionarily
            conserved par protein complex and plays a critical role in
            establishing epithelia-specific junctional structures
  JOURNAL   J Cell Biol 152 (6), 1183-1196 (2001)
   PUBMED   11257119
REFERENCE   8  (residues 1 to 1353)
  AUTHORS   Noda,Y., Takeya,R., Ohno,S., Naito,S., Ito,T. and Sumimoto,H.
  TITLE     Human homologues of the Caenorhabditis elegans cell polarity
            protein PAR6 as an adaptor that links the small GTPases Rac and
            Cdc42 to atypical protein kinase C
  JOURNAL   Genes Cells 6 (2), 107-119 (2001)
   PUBMED   11260256
REFERENCE   9  (residues 1 to 1353)
  AUTHORS   Johansson,A., Driessens,M. and Aspenstrom,P.
  TITLE     The mammalian homologue of the Caenorhabditis elegans polarity
            protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
            Rac1
  JOURNAL   J Cell Sci 113 (Pt 18), 3267-3275 (2000)
   PUBMED   10954424
REFERENCE   10 (residues 1 to 1353)
  AUTHORS   Joberty,G., Petersen,C., Gao,L. and Macara,I.G.
  TITLE     The cell-polarity protein Par6 links Par3 and atypical protein
            kinase C to Cdc42
  JOURNAL   Nat Cell Biol 2 (8), 531-539 (2000)
   PUBMED   10934474
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450337.24, AL138768.23,
            AL360233.21, AL392123.12, AL390766.16 and AL160409.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the PARD protein family.
            PARD family members interact with other PARD family members and
            other proteins; they affect asymmetrical cell division and direct
            polarized cell growth. Multiple alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Oct 2011].
            
            Transcript Variant: This variant (2) uses a different splice site,
            compared to variant 1. The resulting protein (isoform 2) is shorter
            when it is compared to isoform 1. This variant has also been called
            the 'long variant' and 'variant b'.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF196185.1, AF467003.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374788.8/ ENSP00000363920.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.22-p11.21"
     Protein         1..1353
                     /product="partitioning defective 3 homolog isoform 2"
                     /note="partitioning defective 3 homolog; atypical PKC
                     isotype-specific interacting protein; PAR3-alpha; CTCL
                     tumor antigen se2-5; bazooka; par-3 partitioning defective
                     3 homolog; par-3 family cell polarity regulator alpha;
                     protein phosphatase 1, regulatory subunit 118"
                     /calculated_mol_wt=151019
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          81..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          154..262
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          268..364
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(283..289,304,307,337,341,344..345)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          408..448
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          455..547
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(470..476,491,494,524,528,531..532)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Site            489
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          584..683
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(600..606,622,625,655,659,662..663)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            831
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            848
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            849
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          862..883
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            882
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          929..1022
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          932..1353
                     /region_name="Interaction with FRMD4A.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKA.
                     /evidence=ECO:0000269|PubMed:19812038,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            968
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            1043
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Region          1126..1353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW0.2)"
     Site            1347
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99NH2; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW0.2)"
     CDS             1..1353
                     /gene="PARD3"
                     /gene_synonym="ASIP; Baz; PAR3; PAR3alpha; PARD-3; PARD3A;
                     PPP1R118; SE2-5L16; SE2-5LT1; SE2-5T2"
                     /coded_by="NM_001184785.2:302..4363"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53515.1"
                     /db_xref="GeneID:56288"
                     /db_xref="HGNC:HGNC:16051"
                     /db_xref="MIM:606745"
ORIGIN      
        1 mkvtvcfgrt rvvvpcgdgh mkvfsliqqa vtryrkaiak dpnywiqvhr lehgdggild
       61 lddilcdvad dkdrlvavfd eqdphhggdg tsasstgtqs peifgselgt nnvsafqpyq
      121 atseievtps vlranmplhv rrssdpalig lstsvsdsnf sseepsrknp trwsttagfl
      181 kqntagspkt cdrkkdenyr slprdtsnws nqfqrdnars slsashpmvg kwlekqeqde
      241 dgteednsrv epvghadtgl ehipnfsldd mvklvevpnd ggplgihvvp fsarggrtlg
      301 llvkrlekgg kaehenlfre ndcivrindg dlrnrrfeqa qhmfrqamrt piiwfhvvpa
      361 ankeqyeqls qseknnyyss rfspdsqyid nrsvnsaglh tvqraprlnh ppeqidshsr
      421 lphsahpsgk ppsapasapq nvfsttvssg yntkkigkrl niqlkkgteg lgfsitsrdv
      481 tiggsapiyv knilprgaai qdgrlkagdr lievngvdlv gksqeevvsl lrstkmegtv
      541 sllvfrqeda fhprelnaep sqmqipketk aededivltp dgtrefltfe vplndsgsag
      601 lgvsvkgnrs kenhadlgif vksiinggaa skdgrlrvnd qliavngesl lgktnqdame
      661 tlrrsmsteg nkrgmiqliv arriskcnel kspgsppgpe lpietalddr errishslys
      721 giegldesps rnaalsrimg kyqlsptvnm pqddtviied drlpvlpphl sdqssssshd
      781 dvgfvtadag twakaaisds adcslspdvd pvlafqregf grqsmsekrt kqfsdasqld
      841 fvktrksksm dlgiadetkl ntvddqkags psrdvgpslg lkkssslesl qtavaevtln
      901 gdipfhrprp riirgrgcne sfraaidksy dkpavdddde gmetleedte essrsgresv
      961 stasdqpshs lerqmngnqe kgdktdrkkd ktgkekkkdr dkekdkmkak kgmlkglgdm
     1021 frfgkhrkdd kiektgkiki qesftseeer irmkqeqeri qaktrefrer qarerdyaei
     1081 qdfhrtfgcd delmyggvss yegsmalnar pqspreghmm dalyaqvkkp rnskpspvds
     1141 nrstpsnhdr iqrlrqefqq akqdedvedr rrtysfeqpw pnarpatqsg rhsvsvevqm
     1201 qrqrqeeres sqqaqrqyss lprqsrknas svsqdsweqn yspgegfqsa kenpryssyq
     1261 gsrngylggh gfnarvmlet qellrqeqrr keqqmkkqpp segpsnydsy kkvqdpsyap
     1321 pkgpfrqdvp pspsqvarln rlqtpekgrp fys
//
LOCUS       NP_064718                543 aa            linear   PRI 20-NOV-2025
DEFINITION  acid-sensing ion channel 3 isoform c [Homo sapiens].
ACCESSION   NP_064718
VERSION     NP_064718.1
DBSOURCE    REFSEQ: accession NM_020322.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 543)
  AUTHORS   Balboni,A., D'Angelo,C., Collura,N., Brusco,S., Di Berardino,C.,
            Targa,A., Massoti,B., Mastrangelo,E., Milani,M., Seneci,P.,
            Broccoli,V., Muzio,L., Galli,R. and Menegon,A.
  TITLE     Acid-sensing ion channel 3 is a new potential therapeutic target
            for the control of glioblastoma cancer stem cells growth
  JOURNAL   Sci Rep 14 (1), 20421 (2024)
   PUBMED   39227705
  REMARK    GeneRIF: Acid-sensing ion channel 3 is a new potential therapeutic
            target for the control of glioblastoma cancer stem cells growth.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 543)
  AUTHORS   Jacquot,F., Khoury,S., Labrum,B., Delanoe,K., Pidoux,L.,
            Barbier,J., Delay,L., Bayle,A., Aissouni,Y., Barriere,D.A.,
            Kultima,K., Freyhult,E., Hugo,A., Kosek,E., Ahmed,A.S., Jurczak,A.,
            Lingueglia,E., Svensson,C.I., Breuil,V., Ferreira,T., Marchand,F.
            and Deval,E.
  TITLE     Lysophosphatidylcholine 16:0 mediates chronic joint pain associated
            to rheumatic diseases through acid-sensing ion channel 3
  JOURNAL   Pain 163 (10), 1999-2013 (2022)
   PUBMED   35086123
  REMARK    GeneRIF: Lysophosphatidylcholine 16:0 mediates chronic joint pain
            associated to rheumatic diseases through acid-sensing ion channel
            3.
REFERENCE   3  (residues 1 to 543)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 543)
  AUTHORS   Han,X., Zhang,Y., Lee,A., Li,Z., Gao,J., Wu,X., Zhao,J., Wang,H.,
            Chen,D., Zou,D. and Owyang,C.
  TITLE     Upregulation of acid sensing ion channels is associated with
            esophageal hypersensitivity in GERD
  JOURNAL   FASEB J 36 (1), e22083 (2022)
   PUBMED   34918385
  REMARK    GeneRIF: Upregulation of acid sensing ion channels is associated
            with esophageal hypersensitivity in GERD.
REFERENCE   5  (residues 1 to 543)
  AUTHORS   Lottering,B. and Lin,Y.W.
  TITLE     TRPV1 Responses in the Cerebellum Lobules VI, VII, VIII Using
            Electroacupuncture Treatment for Chronic Pain and Depression
            Comorbidity in a Murine Model
  JOURNAL   Int J Mol Sci 22 (9), 5028 (2021)
   PUBMED   34068557
  REMARK    GeneRIF: TRPV1 Responses in the Cerebellum Lobules VI, VII, VIII
            Using Electroacupuncture Treatment for Chronic Pain and Depression
            Comorbidity in a Murine Model.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 543)
  AUTHORS   Catarsi,S., Babinski,K. and Seguela,P.
  TITLE     Selective modulation of heteromeric ASIC proton-gated channels by
            neuropeptide FF
  JOURNAL   Neuropharmacology 41 (5), 592-600 (2001)
   PUBMED   11587714
REFERENCE   7  (residues 1 to 543)
  AUTHORS   Babinski,K., Catarsi,S., Biagini,G. and Seguela,P.
  TITLE     Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric
            proton-gated channels sensitive to Gd3+
  JOURNAL   J Biol Chem 275 (37), 28519-28525 (2000)
   PUBMED   10842183
REFERENCE   8  (residues 1 to 543)
  AUTHORS   Babinski,K., Le,K.T. and Seguela,P.
  TITLE     Molecular cloning and regional distribution of a human proton
            receptor subunit with biphasic functional properties
  JOURNAL   J Neurochem 72 (1), 51-57 (1999)
   PUBMED   9886053
REFERENCE   9  (residues 1 to 543)
  AUTHORS   de Weille,J.R., Bassilana,F., Lazdunski,M. and Waldmann,R.
  TITLE     Identification, functional expression and chromosomal localisation
            of a sustained human proton-gated cation channel
  JOURNAL   FEBS Lett 433 (3), 257-260 (1998)
   PUBMED   9744806
REFERENCE   10 (residues 1 to 543)
  AUTHORS   Ishibashi,K. and Marumo,F.
  TITLE     Molecular cloning of a DEG/ENaC sodium channel cDNA from human
            testis
  JOURNAL   Biochem Biophys Res Commun 245 (2), 589-593 (1998)
   PUBMED   9571199
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313926.1, AC010973.7,
            AF095897.1 and AI580095.1.
            
            Summary: This gene encodes a member of the degenerin/epithelial
            sodium channel (DEG/ENaC) superfamily. The members of this family
            are amiloride-sensitive sodium channels that contain intracellular
            N and C termini, two hydrophobic transmembrane regions, and a large
            extracellular loop, which has many cysteine residues with conserved
            spacing. The member encoded by this gene is an acid sensor and may
            play an important role in the detection of lasting pH changes. In
            addition, a heteromeric association between this member and
            acid-sensing (proton-gated) ion channel 2 has been observed as
            proton-gated channels sensitive to gadolinium. Alternatively
            spliced transcript variants have been described. [provided by
            RefSeq, Feb 2012].
            
            Transcript Variant: This variant (3) lacks an exon and uses an
            alternate splice site in the 3' coding region, compared to variant
            2. The resulting protein (isoform c) has a shorter and distinct
            C-terminus, compared to isoform b.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313926.1, AF195024.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..543
                     /product="acid-sensing ion channel 3 isoform c"
                     /note="testis sodium channel 1; proton-gated cation
                     channel subunit; modulatory subunit of ASIC2a;
                     amiloride-sensitive cation channel 3, testis; acid-sensing
                     ion channel 3; neuronal amiloride-sensitive cation channel
                     3; acid sensing (proton gated) ion channel 3"
                     /calculated_mol_wt=60201
     Region          20..523
                     /region_name="ENaC"
                     /note="sodium channel transporter; TIGR00859"
                     /db_xref="CDD:273304"
     Site            44..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            175
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Region          285..307
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Site            442..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     Region          447..449
                     /region_name="GAS motif, ion selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P78348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHC3.2)"
     CDS             1..543
                     /gene="ASIC3"
                     /gene_synonym="ACCN3; DRASIC; SLNAC1; TNaC1"
                     /coded_by="NM_020322.3:595..2226"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5914.1"
                     /db_xref="GeneID:9311"
                     /db_xref="HGNC:HGNC:101"
                     /db_xref="MIM:611741"
ORIGIN      
        1 mkptsgpeea rrpasdirvf asncsmhglg hvfgpgslsl rrgmwaaavv lsvatflyqv
       61 aervryyref hhqtaldere shrlifpavt lcninplrrs rltpndlhwa gsallgldpa
      121 ehaaflralg rppappgfmp sptfdmaqly araghslddm lldcrfrgqp cgpenfttif
      181 trmgkcytfn sgadgaellt ttrggmgngl dimldvqqee ylpvwrdnee tpfevgirvq
      241 ihsqeeppii dqlglgvspg yqtfvscqqq qlsflpppwg dcssaslnpn yepepsdplg
      301 spspspsppy tlmgcrlace tryvarkcgc rmvympgdvp vcspqqyknc ahpaidamlr
      361 kdscacpnpc astryakels mvripsraaa rflarklnrs eayiaenvla ldiffealny
      421 etveqkkaye msellgdigg qmglfigasl ltileildyl cevfrdkvlg yfwnrqhsqr
      481 hsstnltshp slcrhqdslr lpphllpcht aldllsvsse prpdildmps lhvafpsspq
      541 iks
//
LOCUS       NP_001123608             745 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin superfamily containing leucine-rich repeat protein 2
            precursor [Homo sapiens].
ACCESSION   NP_001123608
VERSION     NP_001123608.1
DBSOURCE    REFSEQ: accession NM_001130136.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Alazami,A.M., Maddirevula,S., Seidahmed,M.Z., Albhlal,L.A. and
            Alkuraya,F.S.
  TITLE     A novel ISLR2-linked autosomal recessive syndrome of congenital
            hydrocephalus, arthrogryposis and abdominal distension
  JOURNAL   Hum Genet 138 (1), 105-107 (2019)
   PUBMED   30483960
  REMARK    GeneRIF: Deletion in ISLR2 gene is associated with autosomal
            recessive syndrome of congenital hydrocephalus, arthrogryposis and
            abdominal distension.
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC152429.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All four transcripts encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC152429.1, AK092302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..745
                     /product="immunoglobulin superfamily containing
                     leucine-rich repeat protein 2 precursor"
                     /note="immunoglobulin superfamily containing leucine-rich
                     repeat protein 2; leucine-rich repeat domain and
                     immunoglobulin domain-containing axon extension protein"
                     /calculated_mol_wt=76995
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2014
     mat_peptide     19..745
                     /product="Immunoglobulin superfamily containing
                     leucine-rich repeat protein 2. /id=PRO_0000317498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
                     /calculated_mol_wt=76995
     Region          36..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <51..>183
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          53..76
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          76..97
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          100..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..169
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          154..>228
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          232..359
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          287..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          375..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            590..610
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          656..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     CDS             1..745
                     /gene="ISLR2"
                     /gene_synonym="LINX"
                     /coded_by="NM_001130136.1:770..3007"
                     /db_xref="CCDS:CCDS10259.1"
                     /db_xref="GeneID:57611"
                     /db_xref="HGNC:HGNC:29286"
                     /db_xref="MIM:614179"
ORIGIN      
        1 mfplralwlv wallgvagsc pepcacvdky ahqfadcayk elrevpeglp anvttlslsa
       61 nkitvlrrga fadvtqvtsl wlahnevrtv epgalavlsq lknldlshnf issfpwsdlr
      121 nlsalqllkm nhnrlgslpr dalgalpdlr slrinnnrlr tlapgtfdal salshlqlyh
      181 npfhcgcglv wlqawaastr vslpepdsia casppalqgv pvyrlpalpc appsvhlsae
      241 ppleapgtpl raglafvlhc iadghptprl qwqlqipggt vvleppvlsg eddgvgaeeg
      301 egegdgdllt qtqaqtptpa pawpappatp rflalangsl lvpllsakea gvytcrahne
      361 lganstsirv avaatgppkh apgaggepdg qaptserkst akgrgnsvlp skpegkikgq
      421 glakvsilge tetepeedts egeeaedqil adpaeeqrcg ngdpsryvsn hafnqsaelk
      481 phvfelgvia ldvaerearv qltplaarwg pgpggaggap rpgrrplrll ylcpagggaa
      541 vqwsrveegv naywfrglrp gtnysvclal ageachvqvv fstkkelpsl lvivavsvfl
      601 lvlatvpllg aacchllakh pgkpyrlilr pqapdpmekr iaadfdpras yleseksypa
      661 ggeaggeepe dvqgeglded aeqgdpsgdl qreeslaacs lvesqskanq eefeagseys
      721 drlplgaeav niaqeingny rqtag
//
LOCUS       NP_001139014             566 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger and SCAN domain-containing protein 18 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001139014
VERSION     NP_001139014.1
DBSOURCE    REFSEQ: accession NM_001145542.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Wang,Y., Luo,Y., Fu,S., He,L., Pan,G., Fan,D., Wen,Q. and Fan,Y.
  TITLE     Zinc finger and SCAN domain-containing protein 18 is a potential
            DNA methylation-modified tumor suppressor and biomarker in breast
            cancer
  JOURNAL   Front Endocrinol (Lausanne) 14, 1095604 (2023)
   PUBMED   37223020
  REMARK    GeneRIF: Zinc finger and SCAN domain-containing protein 18 is a
            potential DNA methylation-modified tumor suppressor and biomarker
            in breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Li,B., Ren,B., Ma,G., Cai,F., Wang,P., Zeng,Y., Liu,Y., Zhang,L.,
            Yang,Y., Liang,H., Zhang,R. and Deng,J.
  TITLE     Inactivation of ZSCAN18 by promoter hypermethylation drives the
            proliferation via attenuating TP53INP2-mediated autophagy in
            gastric cancer cells
  JOURNAL   Clin Epigenetics 15 (1), 10 (2023)
   PUBMED   36650573
  REMARK    GeneRIF: Inactivation of ZSCAN18 by promoter hypermethylation
            drives the proliferation via attenuating TP53INP2-mediated
            autophagy in gastric cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Qi,L., Zhou,L., Lu,M., Yuan,K., Li,Z., Wu,G., Huang,X., Shen,Y.,
            Zhao,M., Fu,W., Chu,B., Wang,G., Ren,F., Ma,D. and Chen,J.
  TITLE     Development of a highly specific HER2 monoclonal antibody for
            immunohistochemistry using protein microarray chips
  JOURNAL   Biochem Biophys Res Commun 484 (2), 248-254 (2017)
   PUBMED   28111342
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Vedeld,H.M., Andresen,K., Eilertsen,I.A., Nesbakken,A., Seruca,R.,
            Gladhaug,I.P., Thiis-Evensen,E., Rognum,T.O., Boberg,K.M. and
            Lind,G.E.
  TITLE     The novel colorectal cancer biomarkers CDO1, ZSCAN18 and ZNF331 are
            frequently methylated across gastrointestinal cancers
  JOURNAL   Int J Cancer 136 (4), 844-853 (2015)
   PUBMED   24948044
  REMARK    GeneRIF: A high negative correlation between promoter DNA
            methylation and gene expression was observed for CDO1, ZNF331 and
            ZSCAN18 in gastrointestinal tumors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC354023.1, AK294376.1 and BC006205.2.
            
            Transcript Variant: This variant (1) encodes the longest protein
            (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294376.1, SRR3476690.116888.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.43"
     Protein         1..566
                     /product="zinc finger and SCAN domain-containing protein
                     18 isoform 1"
                     /note="zinc finger protein 447; zinc finger and SCAN
                     domain-containing protein 18"
                     /calculated_mol_wt=60694
     Region          101..189
                     /region_name="SCAN"
                     /note="SCAN domain; pfam02023"
                     /db_xref="CDD:460417"
     Region          <284..321
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          372..>456
                     /region_name="katE"
                     /note="hydroperoxidase II; Provisional; PRK11249"
                     /db_xref="CDD:236886"
     Region          471..491
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          499..519
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..566
                     /gene="ZSCAN18"
                     /gene_synonym="ZNF447"
                     /coded_by="NM_001145542.1:31..1731"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46214.1"
                     /db_xref="GeneID:65982"
                     /db_xref="HGNC:HGNC:21037"
ORIGIN      
        1 mrrvggrade dataagslwv lappeptghl vipgtsplep pcpwldshif qcrfgkmlpl
       61 ekafasprss pappdlptpg saagvqqeep etipertpad lefsrlrfre fvyqeaagph
      121 qtlarlhelc rqwlmpears keqmlellvl eqflgilpdk vrpwvvaqyp esckkaaslv
      181 egladvleep gmllgspags ssilsdgvye rhmdplllpg elaspsqalg ageipapset
      241 pwlspdplfl eqrrvreakt eedgpanteq klksfpedpq hlgewghldp aeenlksyrk
      301 lllwgyqlsq pdaasrldte elrlverdpq gsslpeggrr qesagcacee aapagvlpel
      361 pteappgdal adppsgttee eeeqpgkapd pqdpqdaesd satgsqrqsv iqqpapdrgt
      421 aklgtkrphp edgdgqsleg vsssgdsagl eagqgpgade pglsrgkpya cgecgeafaw
      481 lshlmehhss hggrkryacq gcwktfhfsl alaehqkthe keksyalgga rgpqpstrea
      541 qagaraggpp esvegeappa ppeaqr
//
LOCUS       NP_001207697             432 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 5 [Homo sapiens].
ACCESSION   NP_001207697
VERSION     NP_001207697.1
DBSOURCE    REFSEQ: accession NM_001220768.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U40462.1 and JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (5) lacks two consecutive in-frame
            exons in the central coding region, compared to variant 1. The
            encoded isoform (5, also known as Ik-3 as described in
            PMID:12937159) is shorter than isoform 1. This isoform contains
            three N-terminal zinc finger motifs for high affinity DNA binding
            (PMID:9892693).
            
            Sequence Note: The 5' UTR of this variant is incomplete because
            there are no full-length transcripts supporting this variant, and
            there is splicing ambiguity in the 5' UTR.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 9892693, 12937159
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..432
                     /product="DNA-binding protein Ikaros isoform 5"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=47503
     Region          119..139
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(124,126,128,130..131,134..135,138,152,154,158..159,
                     162..163,166,180,182,184,186..187,190..191,194)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          132..156
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          147..167
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          159..184
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          175..195
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..432
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001220768.2:15..1313"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvasnvkve
       61 tqsdeengra cemngeecae dlrmldasge kmngshrdqg ssalsgvggi rlpngklkcd
      121 icgiicigpn vlmvhkrsht gerpfqcnqc gasftqkgnl lrhiklhsge kpfkchlcny
      181 acrrrdaltg hlrthsgdkg lsdtpydssa syekenemmk shvmdqainn ainylgaesl
      241 rplvqtppgg sevvpvispm yqlhkplaeg tprsnhsaqd savenlllls kaklvpsere
      301 aspsnscqds tdtesnneeq rsgliyltnh iapharngls lkeehraydl lraasensqd
      361 alrvvstsge qmkvykcehc rvlfldhvmy tihmgchgfr dpfecnmcgy hsqdryefss
      421 hitrgehrfh ms
//
LOCUS       NP_001271306             140 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001271306 XP_005254570
VERSION     NP_001271306.1
DBSOURCE    REFSEQ: accession NM_001284377.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK000459.1.
            
            On Oct 1, 2013 this sequence version replaced XP_005254570.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000459.1, SRR1163657.554205.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..140
                     /product="COMM domain-containing protein 4 isoform 2"
                     /note="COMM domain-containing protein 4"
                     /calculated_mol_wt=15327
     Region          25..>127
                     /region_name="Commd"
                     /note="COMM_Domain, a family of domains found at the
                     C-terminus of HCarG, the copper metabolism gene MURR1
                     product, and related proteins. Presumably all COMM_Domain
                     containing proteins are located in the nucleus and the
                     COMM domain plays a role in...; cl06336"
                     /db_xref="CDD:471425"
     CDS             1..140
                     /gene="COMMD4"
                     /coded_by="NM_001284377.2:28..450"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS66834.1"
                     /db_xref="GeneID:54939"
                     /db_xref="HGNC:HGNC:26027"
                     /db_xref="MIM:616701"
ORIGIN      
        1 mrfrfcgdld cpdwvlaeis tlakmssvkl rllcsqvlke llgqgidyek ilkltadakf
       61 esgdvkatva vlsfilssaa khsvdgesls selqqlglpk ehaaslcrcy eekqsplqkh
      121 lrvcslrklk qaqtlmsslg
//
LOCUS       NP_001335142             541 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform p [Homo sapiens].
ACCESSION   NP_001335142
VERSION     NP_001335142.1
DBSOURCE    REFSEQ: accession NM_001348213.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC358599.1, AK300612.1,
            BM011452.1 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (19) differs in the 5' UTR, lacks
            a portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 3. The resulting
            isoform (p) is shorter at the N-terminus compared to isoform c.
            Variants 16 and 19 encode the same isoform (p).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.122903.1,
                                           SRR1803615.74290.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..541
                     /product="transcription factor 4 isoform p"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=57781
     Region          432..516
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(440,444,446..448,450,455,476..477)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(453..454,457..458,460..461,464,468,478,481,485,488,
                     491..496)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..541
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348213.2:193..1818"
                     /note="isoform p is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS82255.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg ypsskpatst fpssffmqdg hhssdpwsss sgmnqpgyag mlgnsshipq
      121 sssycslhph erlsypshss adinsslppm stfhrsgtnh ystssctppa ngtdsimanr
      181 gsgaagssqt gdalgkalas iyspdhtnns fssnpstpvg sppslsagta vwsrnggqas
      241 sspnyegplh slqsriedrl erlddaihvl rnhavgpsta mpgghgdmhg iigpshngam
      301 gglgsgygtg llsanrhslm vgthredgva lrgshsllpn qvpvpqlpvq satspdlnpp
      361 qdpyrgmppg lqgqsvssgs seiksddegd enlqdtksse dkkldddkkd iksitrsrss
      421 nnddedltpe qkaerekerr mannarerlr vrdineafke lgrmvqlhlk sdkpqtklli
      481 lhqavavils leqqvrernl npkaaclkrr eeekvssepp plslagphpg mgdasnhmgq
      541 m
//
LOCUS       NP_001340526             451 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform i [Homo sapiens].
ACCESSION   NP_001340526
VERSION     NP_001340526.1
DBSOURCE    REFSEQ: accession NM_001353597.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 451)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 451)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 451)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 451)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 451)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 451)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 451)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 451)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 451)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 451)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.13947.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..451
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..451
                     /product="lysosomal cobalamin transporter ABCD4 isoform i"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=49752
     Region          <53..448
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..451
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353597.2:304..1659"
                     /note="isoform i is encoded by transcript variant 12"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mtsitrtsas artwsdsags saawpassss prspssttlt saskgwlgpv sifgyfilgt
       61 vvnktlmgpi vmklvhqekl egdfraghve hmrtdrrlqr llqtqrelms kelwlyigin
      121 tfdylgsils yvviaipifs gvygdlspae lstlvsknaf vciyliscft qlidlsttls
      181 dvagythrig qlretlldms lksqdceilg esewgldtpp gwpaaepadt afllervsis
      241 apssdkplik dlslkisegq sllitgntgt gktsllrvlg glwtstrgsv qmltdfgphg
      301 vlflpqkpff tdgtlreqvi yplkevypds gsadderilr flelaglsnl vartegldqq
      361 vdwnwydvls pgemqrlsfa rlfylqpkya vldeatsalt eeveselyri gqqlgmtfis
      421 vghrqslekf hslvlklcgg grwelmrikv e
//
LOCUS       NP_000984                125 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL31 isoform 1 [Homo sapiens].
ACCESSION   NP_000984 NP_001092048
VERSION     NP_000984.1
DBSOURCE    REFSEQ: accession NM_000993.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Sharen,G., Li,X., Sun,J., Zhang,L., Xi,W., Zhao,X., Han,F., Jia,L.,
            A,R., Cheng,H. and Hou,M.
  TITLE     Silencing eL31 suppresses the progression of colorectal cancer via
            targeting DEPDC1
  JOURNAL   J Transl Med 20 (1), 493 (2022)
   PUBMED   36309731
  REMARK    GeneRIF: Silencing eL31 suppresses the progression of colorectal
            cancer via targeting DEPDC1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Chester,K.A., Robson,L., Begent,R.H., Talbot,I.C., Pringle,J.H.,
            Primrose,L., Macpherson,A.J., Boxer,G., Southall,P. and
            Malcolm,A.D.
  TITLE     Identification of a human ribosomal protein mRNA with increased
            expression in colorectal tumours
  JOURNAL   Biochim Biophys Acta 1009 (3), 297-300 (1989)
   PUBMED   2597680
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Nobori,T., Hexdall,L.E. and Carson,D.A.
  TITLE     cDNA sequence of human ribosomal protein L31
  JOURNAL   Nucleic Acids Res 17 (17), 7105 (1989)
   PUBMED   2780320
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from DA869102.1, BC070373.1, BC017343.2 and AC016738.6.
            
            On Jul 24, 2007 this sequence version replaced NP_001092048.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L31E family of ribosomal proteins. It is located in the
            cytoplasm. Higher levels of expression of this gene in familial
            adenomatous polyps compared to matched normal tissues have been
            observed. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB106299.1, SRR1660809.181058.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264258.8/ ENSP00000264258.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..125
                     /product="large ribosomal subunit protein eL31 isoform 1"
                     /note="60S ribosomal protein L31; large ribosomal subunit
                     protein eL31"
                     /calculated_mol_wt=14332
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62899.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62900; propagated from
                     UniProtKB/Swiss-Prot (P62899.1)"
     Region          19..100
                     /region_name="Ribosomal_L31e"
                     /note="Ribosomal protein L31e; pfam01198"
                     /db_xref="CDD:460108"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62899.1)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P62899.1)"
     CDS             1..125
                     /gene="RPL31"
                     /gene_synonym="eL31; L31"
                     /coded_by="NM_000993.5:28..405"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2049.1"
                     /db_xref="GeneID:6160"
                     /db_xref="HGNC:HGNC:10334"
                     /db_xref="MIM:617415"
ORIGIN      
        1 mapakkggek kkgrsainev vtreytinih krihgvgfkk rapralkeir kfamkemgtp
       61 dvridtrlnk avwakgirnv pyrirvrlsr krnededspn klytlvtyvp vttfknlqtv
      121 nvden
//
LOCUS       NP_001191041              80 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 17 [Homo sapiens].
ACCESSION   NP_001191041
VERSION     NP_001191041.1
DBSOURCE    REFSEQ: accession NM_001204112.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 80)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 80)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 80)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 80)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 80)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 80)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 80)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 80)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 80)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 80)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            DQ849202.1 and AI268146.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (17) lacks an alternate in-frame
            segment in the 5' coding region, lacks an internal exon, and
            contains an alternate internal exon, compared to variant 1. The
            resulting isoform (17) is shorter and has a distinct C-terminus,
            compared to isoform 1. This record was created to support clinical
            studies, but the encoded isoform currently lacks experimental
            evidence.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: DQ849202.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            NMD candidate             :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..80
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..80
                     /product="bcl-2-like protein 11 isoform 17"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=8690
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     CDS             1..80
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_001204112.2:289..531"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS56131.1"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qdrspapmsc dkstqtpspp
       61 cqafnhylsa mvreieevvv
//
LOCUS       NP_001356040             292 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 14 [Homo
            sapiens].
ACCESSION   NP_001356040
VERSION     NP_001356040.1
DBSOURCE    REFSEQ: accession NM_001369111.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.3789.1,
                                           SRR1803617.157254.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267753 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..292
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 14"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=33508
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..>290
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..292
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369111.1:209..1087"
                     /note="isoform 14 is encoded by transcript variant 32"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn vv
//
LOCUS       NP_851307                570 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            delta isoform isoform 2 [Homo sapiens].
ACCESSION   NP_851307
VERSION     NP_851307.1
DBSOURCE    REFSEQ: accession NM_180976.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Oyama,N., Vaneynde,P., Reynhout,S., Pao,E.M., Timms,A., Fan,X.,
            Foss,K., Derua,R., Janssens,V., Chung,W. and Mirzaa,G.M.
  TITLE     Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis
  JOURNAL   J Med Genet 60 (5), 511-522 (2023)
   PUBMED   36216457
  REMARK    GeneRIF: Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Liu,R., Huang,Y., Li,C., Wang,P., Wang,Y. and Zhang,L.
  TITLE     A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree
  JOURNAL   Clin Neurol Neurosurg 223, 107524 (2022)
   PUBMED   36403339
  REMARK    GeneRIF: A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Anwar,M.I., Li,N., Zhou,Q., Chen,M., Hu,C., Wu,T., Chen,H., Li,Y.P.
            and Zhou,Y.
  TITLE     PPP2R5D promotes hepatitis C virus infection by binding to viral
            NS5B and enhancing viral RNA replication
  JOURNAL   Virol J 19 (1), 118 (2022)
   PUBMED   35836293
  REMARK    GeneRIF: PPP2R5D promotes hepatitis C virus infection by binding to
            viral NS5B and enhancing viral RNA replication.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   7  (residues 1 to 570)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Tanabe,O., Nagase,T., Murakami,T., Nozaki,H., Usui,H., Nishito,Y.,
            Hayashi,H., Kagamiyama,H. and Takeda,M.
  TITLE     Molecular cloning of a 74-kDa regulatory subunit (B' or delta) of
            human protein phosphatase 2A
  JOURNAL   FEBS Lett 379 (1), 107-111 (1996)
   PUBMED   8566219
REFERENCE   9  (residues 1 to 570)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Mirzaa,G., Foss,K., Sudnawa,K. and Chung,W.K.
  TITLE     PPP2R5D-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30676711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA388594.1 and BC001175.1.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a delta isoform of the regulatory subunit B56 subfamily.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            isoform (2), that is missing an internal segment compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001175.1, SRR1660805.176556.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..570
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit delta isoform isoform 2"
                     /calculated_mol_wt=66050
     Region          82..481
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..570
                     /gene="PPP2R5D"
                     /gene_synonym="B56D; B56delta; HJS1; MRD35"
                     /coded_by="NM_180976.3:109..1821"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55002.1"
                     /db_xref="GeneID:5528"
                     /db_xref="HGNC:HGNC:9312"
                     /db_xref="MIM:601646"
ORIGIN      
        1 mpyklkkeke ppkvakctak psssgkdggg enteeaqpqp qpqpqpqaqs qppssnkrps
       61 nstppptqls kikysggpqi vkkelfiqkl rqccvlfdfv sdplsdlkfk evkraglnem
      121 veyithsrdv vteaiypeav tmfsvnlfrt lppssnptga efdpeedept leaawphlql
      181 vyefflrfle spdfqpniak kyidqkfvla lldlfdsedp rerdflktil hriygkflgl
      241 rayirrqinh ifyrfiyete hhngiaelle ilgsiingfa lplkeehkmf lirvllplhk
      301 vkslsvyhpq laycvvqfle kessltepvi vgllkfwpkt hspkevmfln eleeildvie
      361 psefskvmep lfrqlakcvs sphfqvaera lyywnneyim slisdnaarv lpimfpalyr
      421 nskshwnkti hgliynalkl fmemnqklfd dctqqykaek qkgrfrmker eemwqkieel
      481 arlnpqypmf rappplppvy smetetptae diqllkrtve teavqmlkdi kkekvllrrk
      541 selpqdvyti kaleahkrae efltasqeal
//
LOCUS       NP_001004720             380 aa            linear   PRI 20-NOV-2025
DEFINITION  cytoplasmic protein NCK2 isoform A [Homo sapiens].
ACCESSION   NP_001004720
VERSION     NP_001004720.1
DBSOURCE    REFSEQ: accession NM_001004720.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 380)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 380)
  AUTHORS   Song,X., Xiao,B., Lu,J., Zhang,W., Li,J., Zhu,X., Sun,Z. and Li,L.
  TITLE     [CBL inhibits proliferation and invasion of breast cancer cells by
            ubiquitylation-mediated degradation of NCK2]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (11), 1594-1603 (2022)
   PUBMED   36504051
  REMARK    GeneRIF: [CBL inhibits proliferation and invasion of breast cancer
            cells by ubiquitylation-mediated degradation of NCK2].
REFERENCE   3  (residues 1 to 380)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 380)
  AUTHORS   Aboualizadeh,F., Yao,Z., Guan,J., Drecun,L., Pathmanathan,S.,
            Snider,J., Umapathy,G., Kotlyar,M., Jurisica,I., Palmer,R. and
            Stagljar,I.
  TITLE     Mapping the Phospho-dependent ALK Interactome to Identify Novel
            Components in ALK Signaling
  JOURNAL   J Mol Biol 433 (23), 167283 (2021)
   PUBMED   34606829
REFERENCE   5  (residues 1 to 380)
  AUTHORS   Park,S., Takeuchi,K. and Wagner,G.
  TITLE     Solution structure of the first SRC homology 3 domain of human Nck2
  JOURNAL   J Biomol NMR 34 (3), 203-208 (2006)
   PUBMED   16604428
  REMARK    GeneRIF: Molecular model of the first SRC homology 3 domain of
            Nck2.
REFERENCE   6  (residues 1 to 380)
  AUTHORS   Tu,Y., Li,F., Goicoechea,S. and Wu,C.
  TITLE     The LIM-only protein PINCH directly interacts with integrin-linked
            kinase and is recruited to integrin-rich sites in spreading cells
  JOURNAL   Mol Cell Biol 19 (3), 2425-2434 (1999)
   PUBMED   10022929
REFERENCE   7  (residues 1 to 380)
  AUTHORS   Braverman,L.E. and Quilliam,L.A.
  TITLE     Identification of Grb4/Nckbeta, a src homology 2 and 3
            domain-containing adapter protein having similar binding and
            biological properties to Nck
  JOURNAL   J Biol Chem 274 (9), 5542-5549 (1999)
   PUBMED   10026169
REFERENCE   8  (residues 1 to 380)
  AUTHORS   Tu,Y., Li,F. and Wu,C.
  TITLE     Nck-2, a novel Src homology2/3-containing adaptor protein that
            interacts with the LIM-only protein PINCH and components of growth
            factor receptor kinase-signaling pathways
  JOURNAL   Mol Biol Cell 9 (12), 3367-3382 (1998)
   PUBMED   9843575
REFERENCE   9  (residues 1 to 380)
  AUTHORS   Chen,M., She,H., Davis,E.M., Spicer,C.M., Kim,L., Ren,R., Le
            Beau,M.M. and Li,W.
  TITLE     Identification of Nck family genes, chromosomal localization,
            expression, and signaling specificity
  JOURNAL   J Biol Chem 273 (39), 25171-25178 (1998)
   PUBMED   9737977
REFERENCE   10 (residues 1 to 380)
  AUTHORS   Li,W., Hu,P., Skolnik,E.Y., Ullrich,A. and Schlessinger,J.
  TITLE     The SH2 and SH3 domain-containing Nck protein is oncogenic and a
            common target for phosphorylation by different surface receptors
  JOURNAL   Mol Cell Biol 12 (12), 5824-5833 (1992)
   PUBMED   1333047
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB456958.1, BC000103.2 and
            AC009505.3.
            
            Summary: This gene encodes a member of the NCK family of adaptor
            proteins. The protein contains three SH3 domains and one SH2
            domain. The protein has no known catalytic function but has been
            shown to bind and recruit various proteins involved in the
            regulation of receptor protein tyrosine kinases. It is through
            these regulatory activities that this protein is believed to be
            involved in cytoskeletal reorganization. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000103.2, SRR9304719.454245.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..380
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12.2"
     Protein         1..380
                     /product="cytoplasmic protein NCK2 isoform A"
                     /note="SH2/SH3 adaptor protein NCK-beta; noncatalytic
                     region of tyrosine kinase, beta; cytoplasmic protein NCK2;
                     growth factor receptor-bound protein 4"
                     /calculated_mol_wt=42784
     Region          2..59
                     /region_name="SH3_Nck2_1"
                     /note="First Src Homology 3 domain of Nck2 adaptor
                     protein; cd11899"
                     /db_xref="CDD:212832"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O43639.2)"
     Site            order(13,16..17,19..20,36..38,50,52..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212832"
     Region          79..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43639.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43639.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43639.2)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O55033; propagated from
                     UniProtKB/Swiss-Prot (O43639.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18088087; propagated from
                     UniProtKB/Swiss-Prot (O43639.2)"
     Region          114..168
                     /region_name="SH3_Nck2_2"
                     /note="Second Src Homology 3 domain of Nck2 adaptor
                     protein; cd11902"
                     /db_xref="CDD:212835"
     Site            order(120,122,125,129,147..148,161,163..164)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212835"
     Region          198..256
                     /region_name="SH3_Nck2_3"
                     /note="Third Src Homology 3 domain of Nck2 adaptor
                     protein; cd11903"
                     /db_xref="CDD:212836"
     Site            order(204,206,209,213,233..234,248,250..251)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212836"
     Site            order(235,249..250,252..254)
                     /site_type="other"
                     /note="Lim4 domain interface [polypeptide binding]"
                     /db_xref="CDD:212836"
     Region          283..380
                     /region_name="SH2_Nck2"
                     /note="Src homology 2 (SH2) domain found in Nck; cd10409"
                     /db_xref="CDD:198272"
     Site            order(292,311,313..315,321,334)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198272"
     Site            order(333,344,347,364..366)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198272"
     CDS             1..380
                     /gene="NCK2"
                     /gene_synonym="GRB4; NCKbeta"
                     /coded_by="NM_001004720.3:68..1210"
                     /note="isoform A is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33266.1"
                     /db_xref="GeneID:8440"
                     /db_xref="HGNC:HGNC:7665"
                     /db_xref="MIM:604930"
ORIGIN      
        1 mteeviviak wdytaqqdqe ldikknerlw llddsktwwr vrnaanrtgy vpsnyverkn
       61 slkkgslvkn lkdtlglgkt rrktsardas ptpstdaeyp angsgadriy dlnipafvkf
      121 ayvaeredel slvkgsrvtv mekcsdgwwr gsyngqigwf psnyvleevd eaaaespsfl
      181 slrkgaslsn gqgsrvlhvv qtlypfssvt eeelnfekge tmeviekpen dpewwkckna
      241 rgqvglvpkn yvvvlsdgpa lhpahapqis ytgpsssgrf agrewyygnv trhqaecaln
      301 ergvegdfli rdsesspsdf svslkasgkn khfkvqlvdn vycigqrrfh tmdelvehyk
      361 kapiftsehg eklylvralq
//
LOCUS       NP_002077                217 aa            linear   PRI 20-NOV-2025
DEFINITION  growth factor receptor-bound protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_002077 NP_079475
VERSION     NP_002077.1
DBSOURCE    REFSEQ: accession NM_002086.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Li,Z., Zhao,P.L., Gao,X., Li,X., Meng,Y.Q., Li,Z.Q., Zhai,K.R.,
            Wei,S.L., Feng,H.M., Huang,H.R. and Li,B.
  TITLE     DUS4L suppresses invasion and metastasis in LUAD via modulation of
            PI3K/AKT and ERK/MAPK signaling through GRB2
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113043 (2024)
   PUBMED   39216120
  REMARK    GeneRIF: DUS4L suppresses invasion and metastasis in LUAD via
            modulation of PI3K/AKT and ERK/MAPK signaling through GRB2.
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Tang,A.A.S., Macdonald,A., McPherson,M.J. and Tomlinson,D.C.
  TITLE     Targeting Grb2 SH3 Domains with Affimer Proteins Provides Novel
            Insights into Ras Signalling Modulation
  JOURNAL   Biomolecules 14 (8), 1040 (2024)
   PUBMED   39199427
  REMARK    GeneRIF: Targeting Grb2 SH3 Domains with Affimer Proteins Provides
            Novel Insights into Ras Signalling Modulation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Qiu,T., Kong,Y., Wei,G., Sun,K., Wang,R., Wang,Y., Chen,Y.,
            Wang,W., Zhang,Y., Jiang,C., Yang,P., Xie,T. and Chen,X.
  TITLE     CCDC6-RET fusion protein regulates Ras/MAPK signaling through the
            fusion- GRB2-SHC1 signal niche
  JOURNAL   Proc Natl Acad Sci U S A 121 (23), e2322359121 (2024)
   PUBMED   38805286
  REMARK    GeneRIF: CCDC6-RET fusion protein regulates Ras/MAPK signaling
            through the fusion- GRB2-SHC1 signal niche.
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Huang,L., Turck,C.W., Rao,P. and Peters,K.G.
  TITLE     GRB2 and SH-PTP2: potentially important endothelial signaling
            molecules downstream of the TEK/TIE2 receptor tyrosine kinase
  JOURNAL   Oncogene 11 (10), 2097-2103 (1995)
   PUBMED   7478529
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Meisner,H. and Czech,M.P.
  TITLE     A 115 kDa tyrosine phosphorylated protein associates with Grb-2 in
            activated Jurkat cells
  JOURNAL   Ann N Y Acad Sci 766, 204-205 (1995)
   PUBMED   7486658
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Matuoka,K., Shibata,M., Yamakawa,A. and Takenawa,T.
  TITLE     Cloning of ASH, a ubiquitous protein composed of one Src homology
            region (SH) 2 and two SH3 domains, from human and rat cDNA
            libraries
  JOURNAL   Proc Natl Acad Sci U S A 89 (19), 9015-9019 (1992)
   PUBMED   1384039
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Lowenstein,E.J., Daly,R.J., Batzer,A.G., Li,W., Margolis,B.,
            Lammers,R., Ullrich,A., Skolnik,E.Y., Bar-Sagi,D. and
            Schlessinger,J.
  TITLE     The SH2 and SH3 domain-containing protein GRB2 links receptor
            tyrosine kinases to ras signaling
  JOURNAL   Cell 70 (3), 431-442 (1992)
   PUBMED   1322798
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Jagielski,J. and Pruszynski,B.
  TITLE     [A case of adrenal adenoma diagnosed by means of adrenal
            phlebography (author's transl)]
  JOURNAL   Pol Przegl Radiol Med Nukl 41 (4), 291-292 (1977)
   PUBMED   917890
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011933.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 23, 2003 this sequence version replaced NP_079475.1.
            
            Summary: The protein encoded by this gene binds the epidermal
            growth factor receptor and contains one SH2 domain and two SH3
            domains. Its two SH3 domains direct complex formation with
            proline-rich regions of other proteins, and its SH2 domain binds
            tyrosine phosphorylated sequences. This gene is similar to the Sem5
            gene of C.elegans, which is involved in the signal transduction
            pathway. Two alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.646033.1, BC000631.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316804.10/ ENSP00000339007.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..217
                     /product="growth factor receptor-bound protein 2 isoform
                     1"
                     /note="HT027; growth factor receptor-bound protein 3;
                     epidermal growth factor receptor-binding protein GRB2;
                     abundant SRC homology; protein Ash; SH2/SH3 adapter GRB2;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=25075
     Region          1..56
                     /region_name="SH3_GRB2_N"
                     /note="N-terminal Src homology 3 domain of Growth factor
                     receptor-bound protein 2; cd11946"
                     /db_xref="CDD:212879"
     Site            order(1,37,50,53..55)
                     /site_type="other"
                     /note="C-terminal SH3 interface [polypeptide binding]"
                     /db_xref="CDD:212879"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     Site            order(6..9,12..13,15..16,31..33,35..36,49..52)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212879"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     Site            50
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     Region          56..150
                     /region_name="SH2_Grb2_like"
                     /note="Src homology 2 domain found in Growth factor
                     receptor-bound protein 2 (Grb2) and similar proteins;
                     cd09941"
                     /db_xref="CDD:199828"
     Site            order(67,86,88,96,107,109)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:199828"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     Region          160..212
                     /region_name="SH3_GRB2_C"
                     /note="C-terminal Src homology 3 domain of Growth factor
                     receptor-bound protein 2; cd11949"
                     /db_xref="CDD:212882"
     Site            order(165,167..168,170..171,192..193,206,208..209)
                     /site_type="other"
                     /note="Vav SH3 interface [polypeptide binding]"
                     /db_xref="CDD:212882"
     Site            order(165,167,170..171,174,190,192..193,204,206,208..209)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212882"
     Site            order(184..188,195,202)
                     /site_type="other"
                     /note="N-terminal SH3 interface [polypeptide binding]"
                     /db_xref="CDD:212882"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11726515; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P62993.1)"
     CDS             1..217
                     /gene="GRB2"
                     /gene_synonym="ASH; EGFRBP-GRB2; Grb3-3; MST084; MSTP084;
                     NCKAP2"
                     /coded_by="NM_002086.5:328..981"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11721.1"
                     /db_xref="GeneID:2885"
                     /db_xref="HGNC:HGNC:4566"
                     /db_xref="MIM:108355"
ORIGIN      
        1 meaiakydfk ataddelsfk rgdilkvlne ecdqnwykae lngkdgfipk nyiemkphpw
       61 ffgkipraka eemlskqrhd gaflireses apgdfslsvk fgndvqhfkv lrdgagkyfl
      121 wvvkfnslne lvdyhrstsv srnqqiflrd ieqvpqqpty vqalfdfdpq edgelgfrrg
      181 dfihvmdnsd pnwwkgachg qtgmfprnyv tpvnrnv
//
LOCUS       NP_001335072             766 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 4 isoform
            4 [Homo sapiens].
ACCESSION   NP_001335072 XP_016877019
VERSION     NP_001335072.1
DBSOURCE    REFSEQ: accession NM_001348143.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 766)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Chen,G.I., Tisayakorn,S., Jorgensen,C., D'Ambrosio,L.M.,
            Goudreault,M. and Gingras,A.C.
  TITLE     PP4R4/KIAA1622 forms a novel stable cytosolic complex with
            phosphoprotein phosphatase 4
  JOURNAL   J Biol Chem 283 (43), 29273-29284 (2008)
   PUBMED   18715871
  REMARK    GeneRIF: PP4R4 forms a novel cytosolic complex with PP4c,
            independent from the complexes containing PP4R1, PP4R2.PP4R3, and
            alpha4, and the regulatory subunits of PP4c have evolved different
            modes of interaction with the catalytic subunit
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Namciu,S.J., Friedman,R.D., Marsden,M.D., Sarausad,L.M.,
            Jasoni,C.L. and Fournier,R.E.
  TITLE     Sequence organization and matrix attachment regions of the human
            serine protease inhibitor gene cluster at 14q32.1
  JOURNAL   Mamm Genome 15 (3), 162-178 (2004)
   PUBMED   15014966
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Andrade,M.A., Petosa,C., O'Donoghue,S.I., Muller,C.W. and Bork,P.
  TITLE     Comparison of ARM and HEAT protein repeats
  JOURNAL   J Mol Biol 309 (1), 1-18 (2001)
   PUBMED   11491282
  REMARK    Review article
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Groves,M.R., Hanlon,N., Turowski,P., Hemmings,B.A. and Barford,D.
  TITLE     The structure of the protein phosphatase 2A PR65/A subunit reveals
            the conformation of its 15 tandemly repeated HEAT motifs
  JOURNAL   Cell 96 (1), 99-110 (1999)
   PUBMED   9989501
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121838.4 and AL117259.6.
            
            On Jan 11, 2017 this sequence version replaced XP_016877019.1.
            
            Summary: The protein encoded by this gene is a HEAT-like
            repeat-containing protein. The HEAT repeat is a tandemly repeated,
            37-47 amino acid long module occurring in a number of cytoplasmic
            proteins. Arrays of HEAT repeats form a rod-like helical structure
            and appear to function as protein-protein interaction surfaces. The
            repeat-containing region of this protein has some similarity to the
            constant regulatory domain of the protein phosphatase 2A PR65/A
            subunit. The encoded protein binds protein serine/threonine
            phosphatase 4c in the cytoplasm. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (4), as well as variant 5, encodes
            isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.52604.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12-q32.13"
     Protein         1..766
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 4 isoform 4"
                     /note="HEAT-like repeat-containing protein;
                     serine/threonine-protein phosphatase 4 regulatory subunit
                     4; cilia and flagella associated protein 14"
                     /calculated_mol_wt=87269
     Region          28..52
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Site            order(44..45,48,51..52,84..85,88,91..92,95,123..124,127,
                     130..131,134,162..163,166,169..170)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293787"
     Region          66..95
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          105..135
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          106..181
                     /region_name="HEAT_2"
                     /note="HEAT repeats; pfam13646"
                     /db_xref="CDD:433376"
     Region          144..170
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          289..315
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          326..353
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..766
                     /gene="PPP4R4"
                     /gene_synonym="CFAP14; KIAA1622; PP4R4"
                     /coded_by="NM_001348143.2:837..3137"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:57718"
                     /db_xref="HGNC:HGNC:23788"
                     /db_xref="MIM:616790"
ORIGIN      
        1 mqltaamsfl tilqdesvsi haythsflqv illhlehrdt gvsnawletl lsvievlpke
       61 tlrheilnpl vskaqlsqtv qsrlvsckil gkltnkfdah tikreilplv kslcqdveye
      121 vrscmcrqle niaqgigtel tksvvlpeli elsrdegssv rlaafetlvn lldifdtddr
      181 sqtilplvks fceksfkade silislsfhl gklchglygi ftpdqhlrfl efykklctlg
      241 lqqenghnen qippqileqe kkyisvrknc aynfpamivf vdpknfhmel ystffclchd
      301 pevpvrytia icfyevskll nsgvylihke litllqdesl evldalidhl peilelmstg
      361 gessvqenkl sslpdlipal taaeqraaas lkwrthekll qkyaclphvi ssdqiyyrfl
      421 qrmftimmtn nvlpvqkaas rtlciflryn rkqeqrhevi qklieqlgqg ksywnrlrfl
      481 dtcefiieif sksffckyff lpaielthdp vanvrmklcy llpkvkstlk ipadkhllqq
      541 lemcvrkllc qekdkdvlai vkrtvleldr memsmdafqk kfyekdlldq ekereellll
      601 emeqlekekq qndgrpmsdk mfekkrrdtk tptqslpkni pisvpgpssv tpstskeikk
      661 sklirsqsfn nqafhakygn lekcasksst tgyttsvsgl gktsvlslad dsfrtrnass
      721 vpssfspntp lpstsrgtgn svdpkssgsk dtqprkatlk srksnp
//
LOCUS       NP_001351452             596 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SLU7 isoform c [Homo sapiens].
ACCESSION   NP_001351452
VERSION     NP_001351452.1
DBSOURCE    REFSEQ: accession NM_001364523.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Garate-Rascon,M., Recalde,M., Rojo,C., Fernandez-Barrena,M.G.,
            Avila,M.A., Arechederra,M. and Berasain,C.
  TITLE     SLU7: A New Hub of Gene Expression Regulation-From Epigenetics to
            Protein Stability in Health and Disease
  JOURNAL   Int J Mol Sci 23 (21), 13411 (2022)
   PUBMED   36362191
  REMARK    GeneRIF: SLU7: A New Hub of Gene Expression Regulation-From
            Epigenetics to Protein Stability in Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Garate-Rascon,M., Recalde,M., Jimenez,M., Elizalde,M., Azkona,M.,
            Uriarte,I., Latasa,M.U., Urtasun,R., Bilbao,I., Sangro,B.,
            Garcia-Ruiz,C., Fernandez-Checa,J.C., Corrales,F.J., Esquivel,A.,
            Pineda-Lucena,A., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     Splicing Factor SLU7 Prevents Oxidative Stress-Mediated Hepatocyte
            Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage
  JOURNAL   Hepatology 74 (5), 2791-2807 (2021)
   PUBMED   34170569
  REMARK    GeneRIF: Splicing Factor SLU7 Prevents Oxidative Stress-Mediated
            Hepatocyte Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage.
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Recalde,M., Garate-Rascon,M., Elizalde,M., Azkona,M., Latasa,M.U.,
            Barcena-Varela,M., Sangro,B., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     The splicing regulator SLU7 is required to preserve DNMT1 protein
            stability and DNA methylation
  JOURNAL   Nucleic Acids Res 49 (15), 8592-8609 (2021)
   PUBMED   34331453
  REMARK    GeneRIF: The splicing regulator SLU7 is required to preserve DNMT1
            protein stability and DNA methylation.
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Shomron,N., Reznik,M. and Ast,G.
  TITLE     Splicing factor hSlu7 contains a unique functional domain required
            to retain the protein within the nucleus
  JOURNAL   Mol Biol Cell 15 (8), 3782-3795 (2004)
   PUBMED   15181151
  REMARK    GeneRIF: The zinc-knuckle motif of hSlu7 determines the cellular
            localization of the protein through a nucleocytoplasmic-sensitive
            shuttling balance.
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     An upstream AG determines whether a downstream AG is selected
            during catalytic step II of splicing
  JOURNAL   Mol Cell Biol 21 (5), 1509-1514 (2001)
   PUBMED   11238888
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     The RNA splicing factor hSlu7 is required for correct 3'
            splice-site choice
  JOURNAL   Nature 402 (6758), 207-210 (1999)
   PUBMED   10647016
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     Human step II splicing factor hSlu7 functions in restructuring the
            spliceosome between the catalytic steps of splicing
  JOURNAL   Genes Dev 13 (7), 841-850 (1999)
   PUBMED   10197984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091842.3.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is a
            splicing factor that has been found to be essential during the
            second catalytic step in the pre-mRNA splicing process. It
            associates with the spliceosome and contains a zinc knuckle motif
            that is found in other splicing factors and is involved in
            protein-nucleic acid and protein-protein interactions. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (7), as well as variant 6, encodes
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..596
                     /product="pre-mRNA-splicing factor SLU7 isoform c"
                     /note="step II splicing factor SLU7; zinc knuckle motif
                     containing; pre-mRNA-splicing factor SLU7; SLU7 splicing
                     factor homolog; SLU7 homolog, splicing factor"
                     /calculated_mol_wt=69273
     Region          171..444
                     /region_name="Slu7"
                     /note="Pre-mRNA splicing Prp18-interacting factor;
                     pfam11708"
                     /db_xref="CDD:463326"
     CDS             1..596
                     /gene="SLU7"
                     /gene_synonym="9G8; hSlu7"
                     /coded_by="NM_001364523.2:136..1926"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:10569"
                     /db_xref="HGNC:HGNC:16939"
                     /db_xref="MIM:605974"
ORIGIN      
        1 mktsiggqit msatvvdavn aaplsgskem sleepkkmtr edwrkkkele eqrklgnapa
       61 evdeegkdin phipqyissv pwyidpskrp tlkhqrpqpe kqkqfsssge wykrgvkens
      121 iitkyrkgac encgamthkk kdcferprrv gakftgtnia pdehvqpqlm fdydgkrdrw
      181 ngynpeehmk iveeyakvdl akrtlkaqkl qeelasgklv eqanspkhqw geeepnsqme
      241 kdhnsedede dkyaddidmp gqnfdskrri tvrnlrired iakylrnldp nsayydpktr
      301 amrenpyana gknpdevsya gdnfvrytgd tismaqtqlf aweaydkgse vhlqadptkl
      361 ellyksfkvk kedfkeqqke silekyggqe hldappaell laqtedyvey srhgtvikgq
      421 eravacskye edvkihnhth iwgsywkegr wgykcchsff kysyctgeag keivnseeci
      481 ineitgeesv kkpqtlmelh qeklkeekkk kkkkkkkhrk sssdsddeek kheklkkaln
      541 aeearllhvk etmqiderkr pynsmyetre pteeemeayr mkrqrpddpm asflgq
//
LOCUS       NP_001305288            1690 aa            linear   PRI 20-NOV-2025
DEFINITION  NEDD4-binding protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001305288 XP_006714085
VERSION     NP_001305288.1
DBSOURCE    REFSEQ: accession NM_001318359.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1690)
  AUTHORS   Nicholson-Shaw,T., Dowdle,M.E., Ajaj,Y., Perelis,M., Fulzele,A.,
            Yeo,G.W., Bennett,E.J. and Lykke-Andersen,J.
  TITLE     Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay
            factor
  JOURNAL   RNA 31 (8), 1195-1205 (2025)
   PUBMED   40441874
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1690)
  AUTHORS   Leslie,E.J., Carlson,J.C., Shaffer,J.R., Buxo,C.J., Castilla,E.E.,
            Christensen,K., Deleyiannis,F.W.B., Field,L.L., Hecht,J.T.,
            Moreno,L., Orioli,I.M., Padilla,C., Vieira,A.R., Wehby,G.L.,
            Feingold,E., Weinberg,S.M., Murray,J.C. and Marazita,M.L.
  TITLE     Association studies of low-frequency coding variants in
            nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Am J Med Genet A 173 (6), 1531-1538 (2017)
   PUBMED   28425186
  REMARK    GeneRIF: We found that a burden of low-frequency coding variants in
            N4BP2, CDSN, PRTG, and AHRR were associated with increased risk of
            Nonsyndromic cleft lip with or without cleft palate (NSCL/P) .
            Low-frequency variants in other genes were associated with
            decreased risk of NSCL/P. These results demonstrate that
            low-frequency variants contribute to the genetic etiology of NSCL/P
REFERENCE   3  (residues 1 to 1690)
  AUTHORS   Jeong,E.Y., Kim,T.G. and Ban,C.
  TITLE     Modulated nicking endonuclease function by the N-terminal extended
            region of the smr domain in human Bcl-3 binding protein
  JOURNAL   Proteins 80 (1), 327-332 (2012)
   PUBMED   22072629
  REMARK    GeneRIF: the N-terminal extended region of the Smr domain in the
            native B3bp may function as a regulatory region for the nicking
            endonuclease
REFERENCE   4  (residues 1 to 1690)
  AUTHORS   Diercks,T., AB,E., Daniels,M.A., de Jong,R.N., Besseling,R.,
            Kaptein,R. and Folkers,G.E.
  TITLE     Solution structure and characterization of the DNA-binding activity
            of the B3BP-Smr domain
  JOURNAL   J Mol Biol 383 (5), 1156-1170 (2008)
   PUBMED   18804481
  REMARK    GeneRIF: The solution structure of the functionally active Smr
            domain of the Bcl3-binding protein (also known as Nedd4-binding
            protein 2), a protein with unknown function that lacks other
            domains present in MutS proteins, is determined.
REFERENCE   5  (residues 1 to 1690)
  AUTHORS   Oshikawa,M., Sugai,Y., Usami,R., Ohtoko,K., Toyama,S. and Kato,S.
  TITLE     Fine expression profiling of full-length transcripts using a
            size-unbiased cDNA library prepared with the vector-capping method
  JOURNAL   DNA Res 15 (3), 123-136 (2008)
   PUBMED   18487259
REFERENCE   6  (residues 1 to 1690)
  AUTHORS   Zheng,M.Z., Qin,H.D., Yu,X.J., Zhang,R.H., Chen,L.Z., Feng,Q.S. and
            Zeng,Y.X.
  TITLE     Haplotype of gene Nedd4 binding protein 2 associated with sporadic
            nasopharyngeal carcinoma in the Southern Chinese population
  JOURNAL   J Transl Med 5, 36 (2007)
   PUBMED   17626640
  REMARK    GeneRIF: These data suggest that haplotype blocks ATTA and GTTG of
            N4BP2 is correlation with the risk of sporadic nasopharyngeal
            carcinoma in the Southern Chinese population.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1690)
  AUTHORS   Watanabe,N., Wachi,S. and Fujita,T.
  TITLE     Identification and characterization of BCL-3-binding protein:
            implications for transcription and DNA repair or recombination
  JOURNAL   J Biol Chem 278 (28), 26102-26110 (2003)
   PUBMED   12730195
  REMARK    GeneRIF: B3BP is a 5'-polynucleotide kinase
REFERENCE   8  (residues 1 to 1690)
  AUTHORS   Murillas,R., Simms,K.S., Hatakeyama,S., Weissman,A.M. and
            Kuehn,M.R.
  TITLE     Identification of developmentally expressed proteins that
            functionally interact with Nedd4 ubiquitin ligase
  JOURNAL   J Biol Chem 277 (4), 2897-2907 (2002)
   PUBMED   11717310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098591.4, AU129951.1,
            AB371584.1, AK001542.1, AC095057.3 and AW135590.1.
            
            On Jan 5, 2016 this sequence version replaced XP_006714085.1.
            
            Summary: This gene encodes a protein containing a polynucleotide
            kinase domain (PNK) near the N-terminal region, and a Small MutS
            Related (Smr) domain near the C-terminal region. The encoded
            protein can bind to both B-cell leukemia/lymphoma 3 (BCL-3) and
            neural precursor cell expressed, developmentally downregulated 4,
            (Nedd4) proteins. This protein binds and hydrolyzes ATP, may
            function as a 5'-polynucleotide kinase, and has the capacity to be
            a ubiquitylation substrate. This protein may play a role in
            transcription-coupled DNA repair or genetic recombination.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in its 5' UTR compared
            to variant 1. This variant represents translation initiation at a
            downstream start codon compared to variant 1; the 5'-most
            initiation codon, as used in variant 1, is associated with a
            truncated ORF that would render the transcript a candidate for
            nonsense-mediated decay (NMD). Leaky scanning may allow translation
            initiation at the downstream start codon to encode an isoform (2)
            that has a shorter N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB371584.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1690
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1690
                     /product="NEDD4-binding protein 2 isoform 2"
                     /note="BCL-3-binding protein"
                     /calculated_mol_wt=189710
     Region          369..500
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Region          1541..1602
                     /region_name="DUF1771"
                     /note="Domain of unknown function (DUF1771); pfam08590"
                     /db_xref="CDD:462528"
     Region          1608..1690
                     /region_name="SMR"
                     /note="Small MutS-related domain; smart00463"
                     /db_xref="CDD:214676"
     CDS             1..1690
                     /gene="N4BP2"
                     /gene_synonym="B3BP"
                     /coded_by="NM_001318359.2:724..5796"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55728"
                     /db_xref="HGNC:HGNC:29851"
                     /db_xref="MIM:619139"
ORIGIN      
        1 mdcllelsat dtkieesssq sfvasenqvg aaeskimekr peeesedskm dsfldmqlte
       61 dldsliqnaf eklnsspddq vysflpsqdv nsfndssefi npdssnmtpi fstqnmnlng
      121 enlensgstl slnplpshsv lneskcfikd ntlalesnyp edsllsssln vasdsiagcs
      181 slnqkqkell esecveaqfs eapvdldase pqaclnlpgl dlpgtggdqk strvsdvflp
      241 segfnfkphk hpelptkgkd vsycpvlapl plllpppppp pmwnpmipaf dlfqgnhgfv
      301 apvvttaahw rsvnytfpps vishtsptkv wrnkdgtsay qvqetpvsqv vrkktsyvgl
      361 vlvllrglpg sgksflartl qednpsgvil stddyfying qyqfdvkylg eahewnqnra
      421 keafekkisp iiidntnlqa wemkpyvals qkhkykvlfr epdtwwkfkp kelarrnihg
      481 vskekitrml ehyqrfvsvp iimsssvpek ierielcays cedrstsprd dediisekee
      541 nilslslkhl efteeknldv tketmlpenv aylsnadlnk rrkeisdmnp siqsalilet
      601 phmyfsdses klqatdksen eqiemvavkg ysktdtdssm ervspstccs ennqedcdla
      661 nsgplqneks spgeiveera tvtkkafgkq kskstlekfp rhelsnfvgd wpvdktigqr
      721 tkrnrktekt ssvqsdkkyn ypqshklvns vsvntdcvqq rgsphesved grksqcddas
      781 eplnsykyda yknidknsfn imgdwpssds laqrehrsrm pktglsepnl eigtndkmne
      841 islstaheac wgtssqklkt lgssnlgsse mllsemtces qtclskkshg qhtslpltft
      901 nsaptvsgvv epqtlaecqe qmpkrdpgke vgmctqtepq dfallwkiek nkisisdsik
      961 vltgrldgfk pkvfnintks dvqeaipyrv mydkstfvee seltsadese nlnilcklfg
     1021 sfslealkdl yercnkdiiw atsllldset klcedtefen fqkscdgsqi gpfslglnlk
     1081 eiisqrgtle nsnspvpefs hgigisnads qstcdaergn seqaemravt penhesmtsi
     1141 fpsaavglkn nndilpnsqe ellysskqsf pgilkattpk dmseteknlv vtetgdnihs
     1201 pshfsdifnf vsstsnleln eeiyftdsle ikrnenfpkd yvkfsdeeef mnedekemke
     1261 ilmagsslsa gvsgedktei lnptpamaks ltidclelal ppelafqlne lfgpvgidsg
     1321 sltvedcvvh idlnlakvih ekwkesvmer qrqeevscgk fmqdpslvgh tgldnpeqks
     1381 sqrtgkkllk tltasemlpl ldhwntqtkk vslreimsee ialqekhnlk retlmfekdc
     1441 atklkekqlf kifpainqnf lvdifkdhny slehtvqfln cvlegdpvkt vvaqefvhqn
     1501 envtshtgqk skekkpkklk eteetpsels fqdfeypdyd dyraeaflhq qkrmecyska
     1561 keayrigkkn vatfyaqqgt lheqkmkean hlaaieifek vnasllpqnv ldlhglhvde
     1621 alehlmrvle kkteefkqng gkpylsvitg rgnhsqggva rikpavikyl ishsfrfsei
     1681 kpgclkvmlk
//
LOCUS       NP_001353147             904 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001353147 XP_016861294
VERSION     NP_001353147.1
DBSOURCE    REFSEQ: accession NM_001366218.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 904)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 904)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 904)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 904)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 904)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 904)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 904)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 904)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 904)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 904)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861294.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.21834.1,
                                           SRR11853560.21666.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..904
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..904
                     /product="disks large homolog 1 isoform 1"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=100324
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..223
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          162..212
                     /region_name="Interaction with SH3 domains"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Region          222..310
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Region          224..546
                     /region_name="Required for interaction with MARCHF2.
                     /evidence=ECO:0000269|PubMed:17980554"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62696; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            order(233..239,256,259,289,293,296..297)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          319..403
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(328..334,351,354,384,388,391..392)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q811D0; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          404..465
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          463..553
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(475..481,492,495,525,529,532..533)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          582..648
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(587,609..610,631)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(590,592,595,604,622..623,642,644..645)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q811D0; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          662..693
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12959.2)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     Region          713..891
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62696; propagated from
                     UniProtKB/Swiss-Prot (Q12959.2)"
     CDS             1..904
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366218.1:624..3338"
                     /note="isoform 1 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS43194.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kpteavlpsp ptvpvipvlp
      181 vpaentvilp tipqanpppv lvntdsletp tyvngtdady eyeeitlerg nsglgfsiag
      241 gtdnphigdd ssifitkiit ggaaaqdgrl rvndcilrvn evdvrdvths kavealkeag
      301 sivrlyvkrr kpvsekimei klikgpkglg fsiaggvgnq hipgdnsiyv tkiieggaah
      361 kdgklqigdk llavnnvcle evtheeavta lkntsdfvyl kvakptsmym ndgyappdit
      421 nsssqpvdnh vspssflgqt pasparyspv skavlgddei treprkvvlh rgstglgfni
      481 vggedgegif isfilaggpa dlsgelrkgd riisvnsvdl raasheqaaa alknagqavt
      541 ivaqyrpeey srfeakihdl reqmmnssis sgsgslrtsq krslyvralf dydktkdsgl
      601 psqglnfkfg dilhvinasd dewwqarqvt pdgesdevgv ipskrrvekk erarlktvkf
      661 nsktrdkgei pddmgskglk hvtsnasdse ssyrgqeeyv lsyepvnqqe vnytrpviil
      721 gpmkdrindd lisefpdkfg scvphttrpk rdyevdgrdy hfvtsreqme kdiqehkfie
      781 agqynnhlyg tsvqsvreva ekgkhcildv sgnaikrlqi aqlypisifi kpksmenime
      841 mnkrlteeqa rktferamkl eqeftehfta ivqgdtledi ynqvkqiiee qsgsyiwvpa
      901 kekl
//
LOCUS       NP_036557                277 aa            linear   PRI 20-NOV-2025
DEFINITION  ras suppressor protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_036557
VERSION     NP_036557.1
DBSOURCE    REFSEQ: accession NM_012425.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cheng,Y., Wang,F., Guo,C., Yuan,S., Li,J. and Zhang,Y.
  TITLE     CircRSU1 alleviates LPS-induced human pulmonary microvascular
            endothelial cell injury by targeting miR-1224-5p/ITGA5 axis
  JOURNAL   Gen Physiol Biophys 43 (1), 1-11 (2024)
   PUBMED   38312030
  REMARK    GeneRIF: CircRSU1 alleviates LPS-induced human pulmonary
            microvascular endothelial cell injury by targeting
            miR-1224-5p/ITGA5 axis.
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Nikou,S., Arbi,M., Dimitrakopoulos,F.D., Kalogeropoulou,A.,
            Geramoutsou,C., Zolota,V., Kalofonos,H.P., Taraviras,S., Lygerou,Z.
            and Bravou,V.
  TITLE     Ras suppressor-1 (RSU1) exerts a tumor suppressive role with
            prognostic significance in lung adenocarcinoma
  JOURNAL   Clin Exp Med 23 (3), 871-885 (2023)
   PUBMED   35729367
  REMARK    GeneRIF: Ras suppressor-1 (RSU1) exerts a tumor suppressive role
            with prognostic significance in lung adenocarcinoma.
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Christou,C., Christodoulou,M.I., Zaravinos,A. and Gkretsi,V.
  TITLE     Ras suppressor 1 long form (RSU1L) silencing promotes apoptosis in
            invasive breast cancer cells
  JOURNAL   Cell Signal 101, 110522 (2023)
   PUBMED   36375714
  REMARK    GeneRIF: Ras suppressor 1 long form (RSU1L) silencing promotes
            apoptosis in invasive breast cancer cells.
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Geramoutsou,C., Nikou,S., Karavias,D., Arbi,M., Tavlas,P.,
            Tzelepi,V., Lygerou,Z., Maroulis,I. and Bravou,V.
  TITLE     Focal adhesion proteins in hepatocellular carcinoma: RSU1 a novel
            tumour suppressor with prognostic significance
  JOURNAL   Pathol Res Pract 235, 153950 (2022)
   PUBMED   35642986
  REMARK    GeneRIF: Focal adhesion proteins in hepatocellular carcinoma: RSU1
            a novel tumour suppressor with prognostic significance.
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Masuelli,L. and Cutler,M.L.
  TITLE     Increased expression of the Ras suppressor Rsu-1 enhances Erk-2
            activation and inhibits Jun kinase activation
  JOURNAL   Mol Cell Biol 16 (10), 5466-5476 (1996)
   PUBMED   8816460
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Tsuda,T., Marinetti,M.R., Masuelli,L. and Cutler,M.L.
  TITLE     The Ras suppressor RSU-1 localizes to 10p13 and its expression in
            the U251 glioblastoma cell line correlates with a decrease in
            growth rate and tumorigenic potential
  JOURNAL   Oncogene 11 (2), 397-403 (1995)
   PUBMED   7624154
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
   PUBMED   8076819
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Tsuda,T. and Cutler,M.L.
  TITLE     Human RSU1 is highly homologous to mouse Rsu-1 and localizes to
            human chromosome 10
  JOURNAL   Genomics 18 (2), 461-462 (1993)
   PUBMED   8288261
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Cutler,M.L., Bassin,R.H., Zanoni,L. and Talbot,N.
  TITLE     Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras
            transformation
  JOURNAL   Mol Cell Biol 12 (9), 3750-3756 (1992)
   PUBMED   1508180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG400752.1, BC005993.1,
            BX647733.1, AK055596.1 and AC073367.11.
            
            Summary: This gene encodes a protein that is involved in the Ras
            signal transduction pathway, growth inhibition, and nerve-growth
            factor induced differentiation processes, as determined in mouse
            and human cell line studies. In mouse, the encoded protein was
            initially isolated based on its ability to inhibit v-Ras
            transformation. Multiple alternatively spliced transcript variants
            for this gene have been reported; one of these variants was found
            only in glioma tumors. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.245998.1,
                                           SRR1803613.241393.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345264.10/ ENSP00000339521.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..277
                     /product="ras suppressor protein 1 isoform 1"
                     /note="rsu-1"
                     /calculated_mol_wt=31409
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15404.3)"
     Region          19..41
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <34..>205
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          41..63
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          42..64
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          64..85
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          65..87
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          87..109
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          88..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          110..133
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          111..135
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          135..156
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          136..158
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          158..179
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          159..181
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          181..202
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     Region          182..207
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          208..227
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          250..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15404.3)"
     CDS             1..277
                     /gene="RSU1"
                     /gene_synonym="RSP-1"
                     /coded_by="NM_012425.4:114..947"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7112.1"
                     /db_xref="GeneID:6251"
                     /db_xref="HGNC:HGNC:10464"
                     /db_xref="MIM:179555"
ORIGIN      
        1 mskslkklve esreknqpev dmsdrgisnm ldvnglftls hitqlvlshn kltmvppnia
       61 elknlevlnf fnnqieelpt qisslqklkh lnlgmnrlnt lprgfgslpa levldltynn
      121 lsenslpgnf fylttlraly lsdndfeilp pdigkltklq ilslrdndli slpkeigelt
      181 qlkelhiqgn rltvlppelg nldltgqkqv fkaennpwvt piadqfqlgv shvfeyirse
      241 tykylygrhm qanpeppkkn ndkskkisrk plaaknr
//
LOCUS       NP_001245149             205 aa            linear   PRI 20-NOV-2025
DEFINITION  protein MIS12 homolog [Homo sapiens].
ACCESSION   NP_001245149
VERSION     NP_001245149.1
DBSOURCE    REFSEQ: accession NM_001258220.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Wu,Z., Shi,Y., Lu,M., Song,M., Yu,Z., Wang,J., Wang,S., Ren,J.,
            Yang,Y.G., Liu,G.H., Zhang,W., Ci,W. and Qu,J.
  TITLE     METTL3 counteracts premature aging via m6A-dependent stabilization
            of MIS12 mRNA
  JOURNAL   Nucleic Acids Res 48 (19), 11083-11096 (2020)
   PUBMED   33035345
  REMARK    GeneRIF: METTL3 counteracts premature aging via m6A-dependent
            stabilization of MIS12 mRNA.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Kline,S.L., Cheeseman,I.M., Hori,T., Fukagawa,T. and Desai,A.
  TITLE     The human Mis12 complex is required for kinetochore assembly and
            proper chromosome segregation
  JOURNAL   J Cell Biol 173 (1), 9-17 (2006)
   PUBMED   16585270
  REMARK    GeneRIF: These results indicate that a four-subunit Mis12 complex
            plays an essential role in chromosome segregation in vertebrates
            and contributes to mitotic kinetochore assembly.
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Obuse,C., Iwasaki,O., Kiyomitsu,T., Goshima,G., Toyoda,Y. and
            Yanagida,M.
  TITLE     A conserved Mis12 centromere complex is linked to heterochromatic
            HP1 and outer kinetochore protein Zwint-1
  JOURNAL   Nat Cell Biol 6 (11), 1135-1141 (2004)
   PUBMED   15502821
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Cheeseman,I.M., Niessen,S., Anderson,S., Hyndman,F., Yates,J.R.
            3rd, Oegema,K. and Desai,A.
  TITLE     A conserved protein network controls assembly of the outer
            kinetochore and its ability to sustain tension
  JOURNAL   Genes Dev 18 (18), 2255-2268 (2004)
   PUBMED   15371340
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Goshima,G., Kiyomitsu,T., Yoda,K. and Yanagida,M.
  TITLE     Human centromere chromatin protein hMis12, essential for equal
            segregation, is independent of CENP-A loading pathway
  JOURNAL   J Cell Biol 160 (1), 25-39 (2003)
   PUBMED   12515822
  REMARK    GeneRIF: hMIS12 has a role in mitosis and localizes at kinetochores
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA964146.1 and AL136906.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR,
            compared to variant 1. Variants 1-5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.28323.1,
                                           SRR1803613.148987.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..205
                     /product="protein MIS12 homolog"
                     /note="homolog of yeast Mis12; MIS12 homolog; MIS12, MIND
                     kinetochore complex component, homolog"
                     /calculated_mol_wt=24009
     Region          8..140
                     /region_name="Mis12"
                     /note="Mis12 protein; pfam05859"
                     /db_xref="CDD:461761"
     CDS             1..205
                     /gene="MIS12"
                     /gene_synonym="2510025F08Rik; hMis12; KNTC2AP; MTW1"
                     /coded_by="NM_001258220.1:88..705"
                     /db_xref="CCDS:CCDS11074.1"
                     /db_xref="GeneID:79003"
                     /db_xref="HGNC:HGNC:24967"
                     /db_xref="MIM:609178"
ORIGIN      
        1 msvdpmtyea qffgftpqtc mlriyiafqd ylfevmqave qvilkkldgi pdcdispvqi
       61 rkctekflcf mkghfdnlfs kmeqlflqli lripsnillp edkcketpys eedfqhlqke
      121 ieqlqekykt elctkqalla eleeqkivqa klkqtltffd elhnvgrdhg tsdfreslvs
      181 lvqnsrklqn irdnvekesk rlkis
//
LOCUS       NP_065081                951 aa            linear   PRI 20-NOV-2025
DEFINITION  metal transporter CNNM1 isoform 1 [Homo sapiens].
ACCESSION   NP_065081
VERSION     NP_065081.2
DBSOURCE    REFSEQ: accession NM_020348.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 951)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 951)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 951)
  AUTHORS   Xie,Y., Wang,Y., Gong,R., Lin,J., Li,X., Ma,J. and Huo,L.
  TITLE     SNHG7 Facilitates Hepatocellular Carcinoma Occurrence by
            Sequestering miR-9-5p to Upregulate CNNM1 Expression
  JOURNAL   Cancer Biother Radiopharm 35 (10), 731-740 (2020)
   PUBMED   32397799
  REMARK    GeneRIF: SNHG7 Facilitates Hepatocellular Carcinoma Occurrence by
            Sequestering miR-9-5p to Upregulate CNNM1 Expression.
REFERENCE   4  (residues 1 to 951)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 951)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 951)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   7  (residues 1 to 951)
  AUTHORS   Kenny,E.E., Pe'er,I., Karban,A., Ozelius,L., Mitchell,A.A.,
            Ng,S.M., Erazo,M., Ostrer,H., Abraham,C., Abreu,M.T., Atzmon,G.,
            Barzilai,N., Brant,S.R., Bressman,S., Burns,E.R., Chowers,Y.,
            Clark,L.N., Darvasi,A., Doheny,D., Duerr,R.H., Eliakim,R.,
            Giladi,N., Gregersen,P.K., Hakonarson,H., Jones,M.R., Marder,K.,
            McGovern,D.P., Mulle,J., Orr-Urtreger,A., Proctor,D.D., Pulver,A.,
            Rotter,J.I., Silverberg,M.S., Ullman,T., Warren,S.T., Waterman,M.,
            Zhang,W., Bergman,A., Mayer,L., Katz,S., Desnick,R.J., Cho,J.H. and
            Peter,I.
  TITLE     A genome-wide scan of Ashkenazi Jewish Crohn's disease suggests
            novel susceptibility loci
  JOURNAL   PLoS Genet 8 (3), e1002559 (2012)
   PUBMED   22412388
REFERENCE   8  (residues 1 to 951)
  AUTHORS   Gomez Garcia,I., Oyenarte,I. and Martinez-Cruz,L.A.
  TITLE     Purification, crystallization and preliminary crystallographic
            analysis of the CBS pair of the human metal transporter CNNM4
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 349-353
            (2011)
   PUBMED   21393841
REFERENCE   9  (residues 1 to 951)
  AUTHORS   Wang,C.Y., Yang,P., Shi,J.D., Purohit,S., Guo,D., An,H., Gu,J.G.,
            Ling,J., Dong,Z. and She,J.X.
  TITLE     Molecular cloning and characterization of the mouse Acdp gene
            family
  JOURNAL   BMC Genomics 5 (1), 7 (2004)
   PUBMED   14723793
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 951)
  AUTHORS   Wang,C.Y., Shi,J.D., Yang,P., Kumar,P.G., Li,Q.Z., Run,Q.G.,
            Su,Y.C., Scott,H.S., Kao,K.J. and She,J.X.
  TITLE     Molecular cloning and characterization of a novel gene family of
            four ancient conserved domain proteins (ACDP)
  JOURNAL   Gene 306, 37-44 (2003)
   PUBMED   12657465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB067736.1, DA326933.1,
            DA758649.1, BC098103.1, AL391684.6, AF169226.1 and BI868774.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 21, 2007 this sequence version replaced NP_065081.1.
            
            Summary: This gene encodes a member of the ancient conserved domain
            protein family. The encoded protein may bind copper. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF169226.1, SRR1660809.236112.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356713.5/ ENSP00000349147.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..951
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..951
                     /product="metal transporter CNNM1 isoform 1"
                     /note="metal transporter CNNM1; cyclin-M1; ancient
                     conserved domain-containing protein 1"
                     /calculated_mol_wt=104220
     Site            23..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Region          46..>148
                     /region_name="KLF9_13_N-like"
                     /note="Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16,
                     and similar proteins; cl41730"
                     /db_xref="CDD:425361"
     Region          116..135
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Region          250..>554
                     /region_name="TlyC"
                     /note="Hemolysin-related protein, contains CBS domains,
                     UPF0053 family [General function prediction only];
                     COG1253"
                     /db_xref="CDD:440865"
     Site            282..302
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Site            321..341
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Region          428..553
                     /region_name="CBS_pair_CorC_HlyC_assoc"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains the majority of which are
                     associated with the CorC_HlyC domain; cd04590"
                     /db_xref="CDD:341366"
     Region          436..503
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Site            order(463,478,482..483,486,507,529..531)
                     /site_type="other"
                     /note="putative ligand binding site I [chemical binding]"
                     /db_xref="CDD:341366"
     Region          507..552
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Region          731..753
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Region          795..830
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q0GA42; propagated from
                     UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Site            824
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q0GA42; propagated from
                     UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Site            850
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q0GA42; propagated from
                     UniProtKB/Swiss-Prot (Q9NRU3.3)"
     Region          920..951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRU3.3)"
     CDS             1..951
                     /gene="CNNM1"
                     /gene_synonym="ACDP1; CLP-1; SLC70A1"
                     /coded_by="NM_020348.3:33..2888"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7478.2"
                     /db_xref="GeneID:26507"
                     /db_xref="HGNC:HGNC:102"
                     /db_xref="MIM:607802"
ORIGIN      
        1 maaaaaaaaa vgvrlrdccs rgavlllffs lsprppaaaa wllglrpedt aggrvslegg
       61 tlraaegtsf llrvyfqpgp pataapvpsp tlnsgengtg dwaprlvfie eppggggvap
      121 savptrppgp qrcreqsdwa sdvevlgplr pggvagsalv qvrvrelrkg eaerggaggg
      181 gklfslcawd grawhhhgaa ggfllrvrpr lygpggdllp pawlralgal lllalsalfs
      241 glrlsllsld pvelrvlrns gsaaeqeqar rvqavrgrgt hllctlllgq aganaalagw
      301 lytslppgfg gtgedyseeg ihfpwlpalv ctgavflgae icpysvcsrh glaiashsvc
      361 ltrllmaaaf pvcyplgrll dwalrqeist fytrekllet lraadpysdl vkeelniiqg
      421 alelrtkvve evltplgdcf mlrsdavldf atvseilrsg ytripvyegd qrhnivdilf
      481 vkdlafvdpd dctplltvtr fynrplhcvf ndtrldtvle efkkgkshla ivqrvnnege
      541 gdpfyevmgi vtlediieei ikseildetd lytdnrkkqr vpqrerkrhd fslfklsdte
      601 mrvkispqll lathrfmate vepfkslyls ekillrllkh pnviqelkfd eknkkapehy
      661 lyqrnrpvdy fvlllqgkve vevgkeglrf engaftyygv paimttacsd ndvrkvgsla
      721 gssvflnrsp srcsglnrse spnrersdfg gsntqlysss nnlympdysv hilsdvqfvk
      781 itrqqyqnal tachmdsspq spdmeaftdg dstkapttrg tpqtpkddpa itllnnrnsl
      841 pcsrsdglrs psevvylrme elaftqeemt dfeehstqql tlspaavptr aasdseccni
      901 nldtetspcs sdfeenvgkk llrtlsgqkr krspegerts ednsnltpli t
//
LOCUS       NP_001124489             837 aa            linear   PRI 20-NOV-2025
DEFINITION  cip1-interacting zinc finger protein isoform 3 [Homo sapiens].
ACCESSION   NP_001124489
VERSION     NP_001124489.1
DBSOURCE    REFSEQ: accession NM_001131017.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 837)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 837)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 837)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 837)
  AUTHORS   Chen,Y.R., Wu,Y.S., Wang,W.S., Zhang,J.S. and Wu,Q.G.
  TITLE     Upregulation of lncRNA DANCR functions as an oncogenic role in
            non-small lung cancer by regulating miR-214-5p/CIZ1 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2539-2547 (2020)
   PUBMED   32196604
  REMARK    GeneRIF: Upregulation of lncRNA DANCR functions as an oncogenic
            role in non-small lung cancer by regulating miR-214-5p/CIZ1 axis.
REFERENCE   5  (residues 1 to 837)
  AUTHORS   Chen,X., Wang,P., Wang,S., Li,J., Ou,T. and Zeng,X.
  TITLE     CIZ1 knockdown suppresses the proliferation of bladder cancer cells
            by inducing apoptosis
  JOURNAL   Gene 719, 143946 (2019)
   PUBMED   31252164
  REMARK    GeneRIF: silencing of CIZ1 suppressed bladder cancer cell
            proliferation through inducing apoptosis and reducing cell cycle
            progression
REFERENCE   6  (residues 1 to 837)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 837)
  AUTHORS   Coverley,D., Marr,J. and Ainscough,J.
  TITLE     Ciz1 promotes mammalian DNA replication
  JOURNAL   J Cell Sci 118 (Pt 1), 101-112 (2005)
   PUBMED   15585571
REFERENCE   8  (residues 1 to 837)
  AUTHORS   Warder,D.E. and Keherly,M.J.
  TITLE     Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus
            DNA sequence ARYSR(0-2)YYAC
  JOURNAL   J Biomed Sci 10 (4), 406-417 (2003)
   PUBMED   12824700
  REMARK    GeneRIF: data indicate that Ciz1 is localized in the nucleus and is
            expressed in a wide range of tissues, especially the pancreas and
            the brain; formulated a consensus DNA sequence, ARYSR(0-2)YYAC,
            recognized by Ciz1
REFERENCE   9  (residues 1 to 837)
  AUTHORS   Mitsui,K., Matsumoto,A., Ohtsuka,S., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
            zinc finger protein, ciz1
  JOURNAL   Biochem Biophys Res Commun 264 (2), 457-464 (1999)
   PUBMED   10529385
REFERENCE   10 (residues 1 to 837)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK303288.1 and BC021163.2.
            
            Summary: The protein encoded by this gene is a zinc finger DNA
            binding protein that interacts with CIP1, part of a complex with
            cyclin E. The encoded protein may regulate the cellular
            localization of CIP1. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (3) has an alternate exon in place
            of the first exon, lacks an alternate in-frame exon, and lacks an
            alternate in-frame segment compared to variant 6. The resulting
            isoform (3) is shorter at the N-terminus and lacks two alternate
            internal segments compared to isoform 5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303288.1, SRR3476690.932051.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..837
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..837
                     /product="cip1-interacting zinc finger protein isoform 3"
                     /note="zinc finger protein 356; nuclear protein NP94;
                     Cip1-interacting zinc finger protein"
                     /calculated_mol_wt=92984
     Region          <117..421
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          531..560
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          595..615
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(602..604,605,609,614,631,634..638,640..641)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <605..>656
                     /region_name="UFD2"
                     /note="U1-like Zn-finger-containing protein [General
                     function prediction only]; COG5112"
                     /db_xref="CDD:227443"
     Region          625..649
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          626..648
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..837
                     /gene="CIZ1"
                     /gene_synonym="LSFR1; NP94; ZNF356"
                     /coded_by="NM_001131017.2:147..2660"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25792"
                     /db_xref="HGNC:HGNC:16744"
                     /db_xref="MIM:611420"
ORIGIN      
        1 mfsqqqqqql qqqqqqlqql qqqqlqqqql qqqqllqlqq llqqsppqap lpmavsrglp
       61 pqqpqqplln lqgtnsasll ngsmlqrall lqqlqgldqf amppatydta gltmptatlg
      121 nlrgygmasp glaapsltpp qlatpnlqqf fpqatrqsll gpppvgvpmn psqfnlsgrn
      181 pqkqartsss ttpnrktmpv edksdppegs eeaaeprmdt pedqdlppcp ediakekrtp
      241 apepepceas elpakrlrss eeptekeppg qlqvkaqpqa rmtvpkqtqt pdllpealea
      301 qvlprfqprv lqvqaqvqsq tqpripstdt qvqpklqkqa qtqtspehlv lqqkqvqpql
      361 qqeaepqkqv qpqvhtqaqp svqpqehppa qvsvqppeqt heqphtqpqv sllapeqtpv
      421 vvhvcglemp pdaveagggm ektlpepvgt qvsmeeiqne sacgldvgec enrarempgv
      481 wgaggslkvt ilqssdsraf stvpltpvpr psdsvsstpa atstpskqal qffcyickas
      541 cssqqefqdh msepqhqqrl geiqhmsqac llsllpvprd vletedeepp prrwcntcql
      601 yymgdliqhr rtqdhkiakq slrpfctvcn ryfktprkfv ehvksqghkd kakelkslek
      661 eiagqdedhf itvdavgcfe gdeeeeedde deeeieveee lckqvrsrdi sreewkgset
      721 yspntaygvd flvpvmgyic richkfyhsn sgaqlshcks lghfenlqky kaaknpsptt
      781 rpvsrrcain arnaltalft ssgrppsqpn tqdktpskvt arpsqpplpr rstrlkt
//
LOCUS       NP_663788                782 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform b [Homo sapiens].
ACCESSION   NP_663788
VERSION     NP_663788.1
DBSOURCE    REFSEQ: accession NM_145735.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AB177848.1,
            AL834228.1, BC060776.1, BM677392.1, DB180957.1 and AK093326.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 3. The resulting protein (isoform b) is
            shorter than isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB177848.1, SRR1803614.207505.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..782
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     b"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=87640
     Region          3..115
                     /region_name="CH_betaPIX"
                     /note="calponin homology (CH) domain found in beta-Pak
                     Interactive eXchange factor; cd21266"
                     /db_xref="CDD:409115"
     Site            order(3,7,65,67..68,71..72,74,82..90,96,98..99,101..102,
                     105..106,109)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409115"
     Region          117..163
                     /region_name="RhoGEF67_u1"
                     /note="Unstructured region one on RhoGEF 6 and 7;
                     pfam16615"
                     /db_xref="CDD:465201"
     Region          167..220
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(172,174,177,180..181,196,198..200,211,213,215..216)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          251..428
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(257,261,355,379..380,383..384,386..387,390..391,
                     394..395,398,424,428)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          459..557
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          617..707
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     CDS             1..782
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_145735.3:909..3257"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32009.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mnsaeqtvtw litlgvlesp kktisdpegf lqaslkdgvv lcrllerllp gtiekvypep
       61 rseseclsni reflrgcgas lrletfdand lyqgqnfnkv lsslvtlnkv tadiglgsds
      121 vcarpsshri ksfdslgsqs lhtrtsklfq gqyrsldmtd nsnnqlvvra kfnfqqtned
      181 elsfskgdvi hvtrveeggw wegtlngrtg wfpsnyvrev kasekpvspk sgtlksppkg
      241 fdttainksy ynvvlqnile teneyskelq tvlstylrpl qtseklssan isylmgnlee
      301 icsfqqmlvq sleectklpe aqqrvggcfl nlmpqmktly ltycanhpsa vnvltehsee
      361 lgefmetkga sspgilvltt glskpfmrld kyptllkele rhmedyhtdr qdiqksmaaf
      421 knlsaqcqev rkrkelelqi lteairnweg ddiktlgnvt ymsqvliqca gseekneryl
      481 llfpnvllml sasprmsgfi yqgklpttgm titkledsen hrnafeisgs mierilvscn
      541 nqqdlqewve hlqkqtkvts vgnptikphs vpshtlpshp vtpsskhads kpapltpayh
      601 tlphpshhgt phttinwgpl eppktpkpws lsclrpappl rpsaalcyke dlskspktmk
      661 kllpkrkper kpsdeefasr kstaaleeda qilkvieayc tsaktrqtln stwqgtdlmh
      721 nhvladddqp sldslgrrss lsrlepsdls edsdydsiwt ahsyrmgsts rksccsyish
      781 qn
//
LOCUS       NP_001138886             110 aa            linear   PRI 20-NOV-2025
DEFINITION  rab proteins geranylgeranyltransferase component A 1 isoform b
            [Homo sapiens].
ACCESSION   NP_001138886
VERSION     NP_001138886.1
DBSOURCE    REFSEQ: accession NM_001145414.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Sarkar,H., Tracey-White,D., Hagag,A.M., Burgoyne,T., Nair,N.,
            Jensen,L.D., Edwards,M.M. and Moosajee,M.
  TITLE     Loss of REP1 impacts choroidal melanogenesis and vasculogenesis in
            choroideremia
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166963 (2024)
   PUBMED   37989423
  REMARK    GeneRIF: Loss of REP1 impacts choroidal melanogenesis and
            vasculogenesis in choroideremia.
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Iwagawa,T., Masumoto,H., Tabuchi,H., Tani,K., Conklin,B.R. and
            Watanabe,S.
  TITLE     Evaluation of CRISPR/Cas9 exon-skipping vector for choroideremia
            using human induced pluripotent stem cell-derived RPE
  JOURNAL   J Gene Med 25 (2), e3464 (2023)
   PUBMED   36413603
  REMARK    GeneRIF: Evaluation of CRISPR/Cas9 exon-skipping vector for
            choroideremia using human induced pluripotent stem cell-derived
            RPE.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 110)
  AUTHORS   van Bokhoven,H., van den Hurk,J.A., Bogerd,L., Philippe,C.,
            Gilgenkrantz,S., de Jong,P., Ropers,H.H. and Cremers,F.P.
  TITLE     Cloning and characterization of the human choroideremia gene
  JOURNAL   Hum Mol Genet 3 (7), 1041-1046 (1994)
   PUBMED   7981670
REFERENCE   6  (residues 1 to 110)
  AUTHORS   MacDonald,I.M., Hume,S., Zhai,Y. and Xu,M.
  TITLE     Choroideremia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301511
REFERENCE   7  (residues 1 to 110)
  AUTHORS   van den Hurk,J.A., van de Pol,T.J., Molloy,C.M., Brunsmann,F.,
            Ruther,K., Zrenner,E., Pinckers,A.J., Pawlowitzki,I.H.,
            Bleeker-Wagemakers,E.M., Wieringa,B. et al.
  TITLE     Detection and characterization of point mutations in the
            choroideremia candidate gene by PCR-SSCP analysis and direct DNA
            sequencing
  JOURNAL   Am J Hum Genet 50 (6), 1195-1202 (1992)
   PUBMED   1598901
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Sankila,E.M., Tolvanen,R., van den Hurk,J.A., Cremers,F.P. and de
            la Chapelle,A.
  TITLE     Aberrant splicing of the CHM gene is a significant cause of
            choroideremia
  JOURNAL   Nat Genet 1 (2), 109-113 (1992)
   PUBMED   1302003
REFERENCE   9  (residues 1 to 110)
  AUTHORS   Molloy,C.M., van de Pol,T.J., Brohet,R.M., Ropers,H.H. and
            Cremers,F.P.
  TITLE     Three RFLPs for pZ11 (DXS540) in the choroideremia gene at Xq21.2
  JOURNAL   Nucleic Acids Res 20 (6), 1434 (1992)
   PUBMED   1373238
REFERENCE   10 (residues 1 to 110)
  AUTHORS   Merry,D.E., Janne,P.A., Landers,J.E., Lewis,R.A. and Nussbaum,R.L.
  TITLE     Isolation of a candidate gene for choroideremia
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2135-2139 (1992)
   PUBMED   1549574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB231066.1 and BC032237.1.
            
            Summary: This gene encodes component A of the RAB geranylgeranyl
            transferase holoenzyme. In the dimeric holoenzyme, this subunit
            binds unprenylated Rab GTPases and then presents them to the
            catalytic Rab GGTase subunit for the geranylgeranyl transfer
            reaction. Rab GTPases need to be geranylgeranyled on either one or
            two cysteine residues in their C-terminus to localize to the
            correct intracellular membrane. Mutations in this gene are a cause
            of choroideremia; also known as tapetochoroidal dystrophy (TCD).
            This X-linked disease is characterized by progressive dystrophy of
            the choroid, retinal pigment epithelium and retina. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) contains a novel 3' terminal
            exon and lacks many exons at the 3' end compared to variant 1. The
            resulting isoform (b) is shorter with a distinct C-terminus
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032237.1, SRR1660803.36258.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.2"
     Protein         1..110
                     /product="rab proteins geranylgeranyltransferase component
                     A 1 isoform b"
                     /note="rab proteins geranylgeranyltransferase component A
                     1; choroideremia (Rab escort protein 1); CHM, Rab escort
                     protein 1"
                     /calculated_mol_wt=12170
     Region          5..>61
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     CDS             1..110
                     /gene="CHM"
                     /gene_synonym="DXS540; GGTA; HSD-32; REP-1; TCD"
                     /coded_by="NM_001145414.4:27..359"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48139.1"
                     /db_xref="GeneID:1121"
                     /db_xref="HGNC:HGNC:1940"
                     /db_xref="MIM:300390"
ORIGIN      
        1 madtlpsefd vivigtglpe siiaaacsrs grrvlhvdsr syyggnwasf sfsgllswlk
       61 eyqensdivs dspvwqdqil eneeaialsr kdktiqhvev fcyarstlll
//
LOCUS       NP_001290555             145 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL16 isoform d [Homo sapiens].
ACCESSION   NP_001290555
VERSION     NP_001290555.1
DBSOURCE    REFSEQ: accession NM_001303626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 145)
  AUTHORS   Wang,K., Chen,S., Wu,Y., Wang,Y., Lu,Y., Sun,Y. and Chen,Y.
  TITLE     The ufmylation modification of ribosomal protein L10 in the
            development of pancreatic adenocarcinoma
  JOURNAL   Cell Death Dis 14 (6), 350 (2023)
   PUBMED   37280198
  REMARK    GeneRIF: The ufmylation modification of ribosomal protein L10 in
            the development of pancreatic adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 145)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 145)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 145)
  AUTHORS   Farmer,A.A., Johnsen,J.I., Loftus,T.M., Smith,K.P. and
            Stanbridge,E.J.
  TITLE     Isolation and characterization of the QM promoter
  JOURNAL   Nucleic Acids Res 24 (11), 2158-2165 (1996)
   PUBMED   8668549
REFERENCE   5  (residues 1 to 145)
  AUTHORS   Farmer,A.A., Loftus,T.M., Mills,A.A., Sato,K.Y., Neill,J.D.,
            Tron,T., Yang,M., Trumpower,B.L. and Stanbridge,E.J.
  TITLE     Extreme evolutionary conservation of QM, a novel c-Jun associated
            transcription factor
  JOURNAL   Hum Mol Genet 3 (5), 723-728 (1994)
   PUBMED   8081358
REFERENCE   6  (residues 1 to 145)
  AUTHORS   Kaneko,K., Kobayashi,H., Onodera,O., Miyatake,T. and Tsuji,S.
  TITLE     Genomic organization of a cDNA (QM) demonstrating an altered mRNA
            level in nontumorigenic Wilms' microcell hybrid cells and its
            localization to Xq28
  JOURNAL   Hum Mol Genet 1 (7), 529-533 (1992)
   PUBMED   1339145
REFERENCE   7  (residues 1 to 145)
  AUTHORS   van den Ouweland,A.M., Verdijk,M., Mannens,M.M. and van Oost,B.A.
  TITLE     The QM gene is X-linked and therefore not involved in suppression
            of tumorigenesis in Wilms' tumor
  JOURNAL   Hum Genet 90 (1-2), 144-146 (1992)
   PUBMED   1330878
REFERENCE   8  (residues 1 to 145)
  AUTHORS   van den Ouweland,A.M., Kioschis,P., Verdijk,M., Tamanini,F.,
            Toniolo,D., Poustka,A. and van Oost,B.A.
  TITLE     Identification and characterization of a new gene in the human Xq28
            region
  JOURNAL   Hum Mol Genet 1 (4), 269-273 (1992)
   PUBMED   1303197
REFERENCE   9  (residues 1 to 145)
  AUTHORS   Bignon,C., Roux-Dosseto,M., Zeigler,M.E., Wicha,M.S. and
            Martin,P.M.
  TITLE     cDNA cloning and genomic analysis of a new multigene family sharing
            common phylogenetic and expression profiles with the laminin
            receptor gene
  JOURNAL   Biochem Biophys Res Commun 184 (3), 1165-1172 (1992)
   PUBMED   1534224
REFERENCE   10 (residues 1 to 145)
  AUTHORS   Dowdy,S.F., Lai,K.M., Weissman,B.E., Matsui,Y., Hogan,B.L. and
            Stanbridge,E.J.
  TITLE     The isolation and characterization of a novel cDNA demonstrating an
            altered mRNA level in nontumorigenic Wilms' microcell hybrid cells
  JOURNAL   Nucleic Acids Res 19 (20), 5763-5769 (1991)
   PUBMED   1658743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC095425.1, CA776692.1,
            BC003358.1 and AC245140.2.
            
            Summary: This gene encodes a ribosomal protein that is a component
            of the 60S ribosome subunit. The related protein in chicken can
            bind to c-Jun and can repress c-Jun-mediated transcriptional
            activation. Some studies have detected an association between
            variation in this gene and autism spectrum disorders, though others
            do not detect this relationship. There are multiple pseudogenes of
            this gene dispersed throughout the genome. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2015].
            
            Transcript Variant: This variant (6) has a shorter 5' UTR and uses
            an alternate splice site in the 3' coding region, which results in
            a frameshift, compared to variant 1. The encoded isoform (d) has a
            distinct, shorter C-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.146890.1,
                                           SRR1163655.338956.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..145
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..145
                     /product="large ribosomal subunit protein uL16 isoform d"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10; tumor suppressor QM;
                     Wilms tumor-related protein; laminin receptor homolog;
                     large ribosomal subunit protein uL16"
                     /calculated_mol_wt=16420
     Region          1..>110
                     /region_name="Ribosomal_L16_L10e"
                     /note="L16 is an essential protein in the large ribosomal
                     subunit of bacteria, mitochondria, and chloroplasts. Large
                     subunits that lack L16 are defective in peptidyl
                     transferase activity, peptidyl-tRNA hydrolysis activity,
                     association with the 30S subunit; cl00353"
                     /db_xref="CDD:469737"
     Site            56..57
                     /site_type="other"
                     /note="5S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            order(68..70,73..74)
                     /site_type="other"
                     /note="putative antibiotic binding site [chemical
                     binding]"
                     /db_xref="CDD:238714"
     Site            order(77,85..86,88)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     CDS             1..145
                     /gene="RPL10"
                     /gene_synonym="AUTSX5; DXS648; DXS648E; L10; MRXS35; NOV;
                     QM; uL16"
                     /coded_by="NM_001303626.1:24..461"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="GeneID:6134"
                     /db_xref="HGNC:HGNC:10298"
                     /db_xref="MIM:312173"
ORIGIN      
        1 mgrrparcyr ycknkpypks rfcrgvpdak irifdlgrkk akvdefplcg hmvsdeyeql
       61 ssealeaari cankymvksc gkdgfhirvr lhpfhvirin kmlscagadr harclwkapg
      121 hcgqgshwps yhvhphqaae qgacd
//
LOCUS       NP_006130                220 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell-specific surface glycoprotein CD28 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_006130
VERSION     NP_006130.1
DBSOURCE    REFSEQ: accession NM_006139.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Xiong,Y., Taleb,M., Misawa,K., Hou,Z., Banerjee,S.,
            Amador-Molina,A., Jones,D.R., Chintala,N.K. and Adusumilli,P.S.
  TITLE     c-Kit signaling potentiates CAR T cell efficacy in solid tumors by
            CD28- and IL-2-independent co-stimulation
  JOURNAL   Nat Cancer 4 (7), 1001-1015 (2023)
   PUBMED   37336986
  REMARK    GeneRIF: c-Kit signaling potentiates CAR T cell efficacy in solid
            tumors by CD28- and IL-2-independent co-stimulation.
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Pulanco,M.C., Madsen,A.T., Tanwar,A., Corrigan,D.T. and Zang,X.
  TITLE     Recent advancements in the B7/CD28 immune checkpoint families: new
            biology and clinical therapeutic strategies
  JOURNAL   Cell Mol Immunol 20 (7), 694-713 (2023)
   PUBMED   37069229
  REMARK    GeneRIF: Recent advancements in the B7/CD28 immune checkpoint
            families: new biology and clinical therapeutic strategies.
            Review article
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Mai,H.L., Degauque,N., Lorent,M., Rimbert,M., Renaudin,K.,
            Danger,R., Kerleau,C., Tilly,G., Vivet,A., Le Bot,S., Delbos,F.,
            Walencik,A., Giral,M. and Brouard,S.
  TITLE     Kidney allograft rejection is associated with an imbalance of B
            cells, regulatory T cells and differentiated CD28-CD8+ T cells:
            analysis of a cohort of 1095 graft biopsies
  JOURNAL   Front Immunol 14, 1151127 (2023)
   PUBMED   37168864
  REMARK    GeneRIF: Kidney allograft rejection is associated with an imbalance
            of B cells, regulatory T cells and differentiated CD28-CD8+ T
            cells: analysis of a cohort of 1095 graft biopsies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Gelemanovic,A., Catipovic Ardalic,T., Pribisalic,A., Hayward,C.,
            Kolcic,I. and Polasek,O.
  TITLE     Genome-Wide Meta-Analysis Identifies Multiple Novel Rare Variants
            to Predict Common Human Infectious Diseases Risk
  JOURNAL   Int J Mol Sci 24 (8), 7006 (2023)
   PUBMED   37108169
  REMARK    GeneRIF: Genome-Wide Meta-Analysis Identifies Multiple Novel Rare
            Variants to Predict Common Human Infectious Diseases Risk.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Liu,T.H., Lei,J.Y., Mai,Y.G. and Fang,J.P.
  TITLE     [Clinical Analysis of Pediatric Acute Leukemia Complicated with
            Septic Shock]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1708-1714 (2022)
   PUBMED   36476893
  REMARK    GeneRIF: [Clinical Analysis of Pediatric Acute Leukemia Complicated
            with Septic Shock].
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Fraser,J.D., Newton,M.E. and Weiss,A.
  TITLE     CD28 and T cell antigen receptor signal transduction coordinately
            regulate interleukin 2 gene expression in response to superantigen
            stimulation
  JOURNAL   J Exp Med 175 (4), 1131-1134 (1992)
   PUBMED   1313075
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Zocchi,M.R., Poggi,A., Crosti,F., Tongiani,S. and Rugarli,C.
  TITLE     Signalling in human tumour infiltrating lymphocytes: the CD28
            molecule is functional and is physically associated with the CD45R0
            molecule
  JOURNAL   Eur J Cancer 28A (4-5), 749-754 (1992)
   PUBMED   1355979
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Gimmi,C.D., Freeman,G.J., Gribben,J.G., Sugita,K., Freedman,A.S.,
            Morimoto,C. and Nadler,L.M.
  TITLE     B-cell surface antigen B7 provides a costimulatory signal that
            induces T cells to proliferate and secrete interleukin 2
  JOURNAL   Proc Natl Acad Sci U S A 88 (15), 6575-6579 (1991)
   PUBMED   1650475
REFERENCE   9  (residues 1 to 220)
  AUTHORS   Linsley,P.S., Brady,W., Grosmaire,L., Aruffo,A., Damle,N.K. and
            Ledbetter,J.A.
  TITLE     Binding of the B cell activation antigen B7 to CD28 costimulates T
            cell proliferation and interleukin 2 mRNA accumulation
  JOURNAL   J Exp Med 173 (3), 721-730 (1991)
   PUBMED   1847722
REFERENCE   10 (residues 1 to 220)
  AUTHORS   Lafage-Pochitaloff,M., Costello,R., Couez,D., Simonetti,J.,
            Mannoni,P., Mawas,C. and Olive,D.
  TITLE     Human CD28 and CTLA-4 Ig superfamily genes are located on
            chromosome 2 at bands q33-q34
  JOURNAL   Immunogenetics 31 (3), 198-201 (1990)
   PUBMED   2156778
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125238.5, AK292986.1,
            J02988.1, DA939711.1, AW241446.1, AA311148.1 and BF509568.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is essential for T-cell
            proliferation and survival, cytokine production, and T-helper
            type-2 development. Several alternatively spliced transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript, and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: J02988.1, ERR279829.6684.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324106.9/ ENSP00000324890.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..220
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 1 precursor"
                     /calculated_mol_wt=23085
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1999
     mat_peptide     19..220
                     /product="T-cell-specific surface glycoprotein CD28
                     isoform 1"
                     /calculated_mol_wt=23085
     Region          21..137
                     /region_name="IgV_CD28"
                     /note="Immunoglobulin Variable (IgV) domain Cluster of
                     Differentiation (CD) 28; cd20925"
                     /db_xref="CDD:409519"
     Region          21..42
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409519"
     Region          21..25
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409519"
     Region          27..30
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409519"
     Region          34..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409519"
     Site            37
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15696168; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Region          43..49
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409519"
     Region          50..60
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409519"
     Region          50..57
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409519"
     Region          61..80
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409519"
     Region          63..70
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409519"
     Site            71
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Region          76..80
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409519"
     Region          81..114
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409519"
     Region          85..91
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409519"
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Region          94..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409519"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15696168; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Region          108..117
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409519"
     Region          117..122
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409519"
     Site            117..122
                     /site_type="other"
                     /note="CD28/B7 interaction site"
                     /db_xref="CDD:409519"
     Region          123..137
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409519"
     Region          123..126
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409519"
     Region          129..135
                     /region_name="Ig strand G'"
                     /note="Ig strand G' [structural motif]"
                     /db_xref="CDD:409519"
     Site            129
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Site            153..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P10747.1)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by LCK.
                     /evidence=ECO:0000269|PubMed:7568038,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     Region          198..220
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10747.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (P10747.1)"
     CDS             1..220
                     /gene="CD28"
                     /gene_synonym="IMD123; Tp44"
                     /coded_by="NM_006139.4:59..721"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2361.1"
                     /db_xref="GeneID:940"
                     /db_xref="HGNC:HGNC:1653"
                     /db_xref="MIM:186760"
ORIGIN      
        1 mlrlllalnl fpsiqvtgnk ilvkqspmlv aydnavnlsc kysynlfsre fraslhkgld
       61 savevcvvyg nysqqlqvys ktgfncdgkl gnesvtfylq nlyvnqtdiy fckievmypp
      121 pyldneksng tiihvkgkhl cpsplfpgps kpfwvlvvvg gvlacysllv tvafiifwvr
      181 skrsrllhsd ymnmtprrpg ptrkhyqpya pprdfaayrs
//
LOCUS       NP_001307353             252 aa            linear   PRI 20-NOV-2025
DEFINITION  adenylosuccinate synthetase isozyme 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001307353 XP_011534717
VERSION     NP_001307353.1
DBSOURCE    REFSEQ: accession NM_001320424.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 252)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 252)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 252)
  AUTHORS   Saito,Y., Nishikawa,A., Iida,A., Mori-Yoshimura,M., Oya,Y.,
            Ishiyama,A., Komaki,H., Nakamura,S., Fujikawa,S., Kanda,T.,
            Yamadera,M., Sakiyama,H., Hayashi,S., Nonaka,I., Noguchi,S. and
            Nishino,I.
  TITLE     ADSSL1 myopathy is the most common nemaline myopathy in Japan with
            variable clinical features
  JOURNAL   Neurology 95 (11), e1500-e1511 (2020)
   PUBMED   32646962
  REMARK    GeneRIF: ADSSL1 myopathy is the most common nemaline myopathy in
            Japan with variable clinical features.
REFERENCE   4  (residues 1 to 252)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 252)
  AUTHORS   Park,H.J., Shin,H.Y., Kim,S., Kim,S.H., Lee,Y., Lee,J.H.,
            Hong,J.M., Kim,S.M., Park,K.D., Choi,B.O., Lee,J.H. and Choi,Y.C.
  TITLE     Distal myopathy with ADSSL1 mutations in Korean patients
  JOURNAL   Neuromuscul Disord 27 (5), 465-472 (2017)
   PUBMED   28268051
  REMARK    GeneRIF: Study investigated the clinical manifestation in Korean
            patients with ADSSL1 mutations. Patients with ADSSL1 mutations
            demonstrated distal muscle weakness in adolescence, followed by
            quadriceps muscle weakness in the early 30s. All patients had mild
            facial weakness and two patients complained of easy fatigue while
            eating and chewing. Muscle biopsies and whole body muscle MR
            imaging findings are discussed.
REFERENCE   6  (residues 1 to 252)
  AUTHORS   Rosenthal,S.L., Wang,X., Demirci,F.Y., Barmada,M.M., Ganguli,M.,
            Lopez,O.L. and Kamboh,M.I.
  TITLE     Beta-amyloid toxicity modifier genes and the risk of Alzheimer's
            disease
  JOURNAL   Am J Neurodegener Dis 1 (2), 191-198 (2012)
   PUBMED   22984654
REFERENCE   7  (residues 1 to 252)
  AUTHORS   Sun,H., Li,N., Wang,X., Chen,T., Shi,L., Zhang,L., Wang,J., Wan,T.
            and Cao,X.
  TITLE     Molecular cloning and characterization of a novel muscle
            adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal
            cells
  JOURNAL   Mol Cell Biochem 269 (1-2), 85-94 (2005)
   PUBMED   15786719
  REMARK    GeneRIF: A novel muscle isozyme of adenylosuccinate synthetase,
            human AdSSL1, is identified from human bone marrow stromal cells.
REFERENCE   8  (residues 1 to 252)
  AUTHORS   Iancu,C.V., Borza,T., Choe,J.Y., Fromm,H.J. and Honzatko,R.B.
  TITLE     Recombinant mouse muscle adenylosuccinate synthetase:
            overexpression, kinetics, and crystal structure
  JOURNAL   J Biol Chem 276 (45), 42146-42152 (2001)
   PUBMED   11560929
REFERENCE   9  (residues 1 to 252)
  AUTHORS   Powell,S.M., Zalkin,H. and Dixon,J.E.
  TITLE     Cloning and characterization of the cDNA encoding human
            adenylosuccinate synthetase
  JOURNAL   FEBS Lett 303 (1), 4-10 (1992)
   PUBMED   1592113
REFERENCE   10 (residues 1 to 252)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY011538.1, AK096720.1,
            BC047904.1 and AJ573490.1.
            
            On Feb 25, 2016 this sequence version replaced XP_011534717.1.
            
            Summary: This gene encodes a member of the adenylosuccinate
            synthase family of proteins. The encoded muscle-specific enzyme
            plays a role in the purine nucleotide cycle by catalyzing the first
            step in the conversion of inosine monophosphate (IMP) to adenosine
            monophosphate (AMP). Mutations in this gene may cause adolescent
            onset distal myopathy. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start site compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..252
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..252
                     /product="adenylosuccinate synthetase isozyme 1 isoform 3"
                     /EC_number="6.3.4.4"
                     /note="adenylosuccinate synthetase isozyme 1; M-type
                     adenylosuccinate synthetase; adenylosuccinate synthetase,
                     basic isozyme; adenylosuccinate synthetase, muscle
                     isozyme; adSS 1; AMPSase 1; IMP--aspartate ligase 1;
                     adenylosuccinate synthase like 1; adenylosuccinate
                     synthetase-like 1"
                     /calculated_mol_wt=27948
     Region          <6..249
                     /region_name="Adenylsucc_synt"
                     /note="Adenylosuccinate synthetase; pfam00709"
                     /db_xref="CDD:459912"
     CDS             1..252
                     /gene="ADSS1"
                     /gene_synonym="ADSSL1; MPD5"
                     /coded_by="NM_001320424.1:777..1535"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:122622"
                     /db_xref="HGNC:HGNC:20093"
                     /db_xref="MIM:612498"
ORIGIN      
        1 mfptleidie gqlkrlkgfa erirpmvrdg vyfmyealhg ppkkilvega naalldidfg
       61 typfvtssnc tvggvctglg ippqnigdvy gvvkayttrv gigafpteqi neiggllqtr
      121 ghewgvttgr krrcgwldlm ilryahmvng ftalaltkld ildvlgevkv gvsyklngkr
      181 ipyfpanqem lqkveveyet lpgwkadttg arrwedlppq aqnyirfven hvgvavkwvg
      241 vgksresmiq lf
//
LOCUS       NP_009035                217 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL1 [Homo sapiens].
ACCESSION   NP_009035
VERSION     NP_009035.3
DBSOURCE    REFSEQ: accession NM_007104.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Olvera,J. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L10a
  JOURNAL   Biochem Biophys Res Commun 220 (3), 954-957 (1996)
   PUBMED   8607874
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Fisicaro,N., Katerelos,M., Williams,J., Power,D., D'Apice,A. and
            Pearse,M.
  TITLE     Identification of genes downregulated in the thymus by
            cyclosporin-A: preliminary characterization of clone CSA-19
  JOURNAL   Mol Immunol 32 (8), 565-572 (1995)
   PUBMED   7609734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BP318268.1 and BC006791.1.
            
            On Sep 5, 2001 this sequence version replaced NP_009035.2.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L1P family of ribosomal proteins. It is located in the
            cytoplasm. The expression of this gene is downregulated in the
            thymus by cyclosporin-A (CsA), an immunosuppressive drug. Studies
            in mice have shown that the expression of the ribosomal protein
            L10a gene is downregulated in neural precursor cells during
            development. This gene previously was referred to as NEDD6 (neural
            precursor cell expressed, developmentally downregulated 6), but it
            has been renamed RPL10A (ribosomal protein 10a). As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.467930.1,
                                           SRR5189652.58832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322203.7/ ENSP00000363018.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..217
                     /product="large ribosomal subunit protein uL1"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10a; NEDD-6; neural
                     precursor cell expressed developmentally down-regulated
                     protein 6"
                     /calculated_mol_wt=24700
     Region          2..217
                     /region_name="Ribosomal_L1"
                     /note="Ribosomal protein L1. The L1 protein, located near
                     the E-site of the ribosome, forms part of the L1 stalk
                     along with 23S rRNA. In bacteria and archaea, L1 functions
                     both as a ribosomal protein that binds rRNA, and as a
                     translation repressor that binds...; cl00322"
                     /db_xref="CDD:469720"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000305|PubMed:12962325; propagated from
                     UniProtKB/Swiss-Prot (P62906.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P53026; propagated from
                     UniProtKB/Swiss-Prot (P62906.2)"
     Site            order(26..28,31,33,35,37,162,164,166,210..211,213)
                     /site_type="other"
                     /note="mRNA/rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238235"
     Site            91
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P53026; propagated from
                     UniProtKB/Swiss-Prot (P62906.2)"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62906.2)"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62906.2)"
     CDS             1..217
                     /gene="RPL10A"
                     /gene_synonym="Csa-19; CSA19; L10A; NEDD6; uL1"
                     /coded_by="NM_007104.5:35..688"
                     /db_xref="CCDS:CCDS4806.1"
                     /db_xref="GeneID:4736"
                     /db_xref="HGNC:HGNC:10299"
                     /db_xref="MIM:615660"
ORIGIN      
        1 msskvsrdtl yeavrevlhg nqrkrrkfle tvelqislkn ydpqkdkrfs gtvrlkstpr
       61 pkfsvcvlgd qqhcdeakav diphmdieal kklnknkklv kklakkydaf laseslikqi
      121 prilgpglnk agkfpsllth nenmvakvde vkstikfqmk kvlclavavg hvkmtddelv
      181 ynihlavnfl vsllkknwqn vralyikstm gkpqrly
//
LOCUS       NP_001300946             140 aa            linear   PRI 20-NOV-2025
DEFINITION  copine-5 isoform b [Homo sapiens].
ACCESSION   NP_001300946
VERSION     NP_001300946.1
DBSOURCE    REFSEQ: accession NM_001314017.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Zhu,P., Qian,T., Si,C., Liu,Y., Cui,L., Huang,W., Fu,L., Deng,C.
            and Zeng,T.
  TITLE     High expression of CPNE5 and CPNE9 predicts positive prognosis in
            multiple myeloma
  JOURNAL   Cancer Biomark 31 (1), 77-85 (2021)
   PUBMED   33780365
  REMARK    GeneRIF: High expression of CPNE5 and CPNE9 predicts positive
            prognosis in multiple myeloma.
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Umeda,S., Kanda,M., Koike,M., Tanaka,H., Miwa,T., Tanaka,C.,
            Kobayashi,D., Suenaga,M., Hayashi,M., Yamada,S., Nakayama,G. and
            Kodera,Y.
  TITLE     Copine 5 expression predicts prognosis following curative resection
            of esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 40 (6), 3772-3780 (2018)
   PUBMED   30272363
  REMARK    GeneRIF: Data revealed that CPNE5 mRNA expression was significantly
            lower in ESCC tissues and cell lines and correlated with
            significantly shorter overall survival. Multivariable analysis
            identified low CPNE5 expression to be an independent prognostic
            factor of OS. Analysis of recurrence patterns revealed that
            significantly more patients with local recurrence expressed lower
            levels of CPNE5 mRNA.
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Wang,K.S., Zuo,L., Pan,Y., Xie,C. and Luo,X.
  TITLE     Genetic variants in the CPNE5 gene are associated with alcohol
            dependence and obesity in Caucasian populations
  JOURNAL   J Psychiatr Res 71, 1-7 (2015)
   PUBMED   26522866
  REMARK    GeneRIF: Results provide the first evidence of genetic variants in
            the CPNE5 gene influencing both alcohol dependence and obesity
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 140)
  AUTHORS   den Hoed,M., Eijgelsheim,M., Esko,T., Brundel,B.J., Peal,D.S.,
            Evans,D.M., Nolte,I.M., Segre,A.V., Holm,H., Handsaker,R.E.,
            Westra,H.J., Johnson,T., Isaacs,A., Yang,J., Lundby,A., Zhao,J.H.,
            Kim,Y.J., Go,M.J., Almgren,P., Bochud,M., Boucher,G.,
            Cornelis,M.C., Gudbjartsson,D., Hadley,D., van der Harst,P.,
            Hayward,C., den Heijer,M., Igl,W., Jackson,A.U., Kutalik,Z.,
            Luan,J., Kemp,J.P., Kristiansson,K., Ladenvall,C., Lorentzon,M.,
            Montasser,M.E., Njajou,O.T., O'Reilly,P.F., Padmanabhan,S., St
            Pourcain,B., Rankinen,T., Salo,P., Tanaka,T., Timpson,N.J.,
            Vitart,V., Waite,L., Wheeler,W., Zhang,W., Draisma,H.H.,
            Feitosa,M.F., Kerr,K.F., Lind,P.A., Mihailov,E., Onland-Moret,N.C.,
            Song,C., Weedon,M.N., Xie,W., Yengo,L., Absher,D., Albert,C.M.,
            Alonso,A., Arking,D.E., de Bakker,P.I., Balkau,B., Barlassina,C.,
            Benaglio,P., Bis,J.C., Bouatia-Naji,N., Brage,S., Chanock,S.J.,
            Chines,P.S., Chung,M., Darbar,D., Dina,C., Dorr,M., Elliott,P.,
            Felix,S.B., Fischer,K., Fuchsberger,C., de Geus,E.J., Goyette,P.,
            Gudnason,V., Harris,T.B., Hartikainen,A.L., Havulinna,A.S.,
            Heckbert,S.R., Hicks,A.A., Hofman,A., Holewijn,S.,
            Hoogstra-Berends,F., Hottenga,J.J., Jensen,M.K., Johansson,A.,
            Junttila,J., Kaab,S., Kanon,B., Ketkar,S., Khaw,K.T., Knowles,J.W.,
            Kooner,A.S., Kors,J.A., Kumari,M., Milani,L., Laiho,P.,
            Lakatta,E.G., Langenberg,C., Leusink,M., Liu,Y., Luben,R.N.,
            Lunetta,K.L., Lynch,S.N., Markus,M.R., Marques-Vidal,P., Mateo
            Leach,I., McArdle,W.L., McCarroll,S.A., Medland,S.E., Miller,K.A.,
            Montgomery,G.W., Morrison,A.C., Muller-Nurasyid,M., Navarro,P.,
            Nelis,M., O'Connell,J.R., O'Donnell,C.J., Ong,K.K., Newman,A.B.,
            Peters,A., Polasek,O., Pouta,A., Pramstaller,P.P., Psaty,B.M.,
            Rao,D.C., Ring,S.M., Rossin,E.J., Rudan,D., Sanna,S., Scott,R.A.,
            Sehmi,J.S., Sharp,S., Shin,J.T., Singleton,A.B., Smith,A.V.,
            Soranzo,N., Spector,T.D., Stewart,C., Stringham,H.M., Tarasov,K.V.,
            Uitterlinden,A.G., Vandenput,L., Hwang,S.J., Whitfield,J.B.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilson,J.F., Witteman,J.C.,
            Wong,A., Wong,Q., Jamshidi,Y., Zitting,P., Boer,J.M., Boomsma,D.I.,
            Borecki,I.B., van Duijn,C.M., Ekelund,U., Forouhi,N.G., Froguel,P.,
            Hingorani,A., Ingelsson,E., Kivimaki,M., Kronmal,R.A., Kuh,D.,
            Lind,L., Martin,N.G., Oostra,B.A., Pedersen,N.L., Quertermous,T.,
            Rotter,J.I., van der Schouw,Y.T., Verschuren,W.M., Walker,M.,
            Albanes,D., Arnar,D.O., Assimes,T.L., Bandinelli,S., Boehnke,M., de
            Boer,R.A., Bouchard,C., Caulfield,W.L., Chambers,J.C., Curhan,G.,
            Cusi,D., Eriksson,J., Ferrucci,L., van Gilst,W.H., Glorioso,N., de
            Graaf,J., Groop,L., Gyllensten,U., Hsueh,W.C., Hu,F.B.,
            Huikuri,H.V., Hunter,D.J., Iribarren,C., Isomaa,B., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kiemeney,L.A., van der Klauw,M.M.,
            Kooner,J.S., Kraft,P., Iacoviello,L., Lehtimaki,T., Lokki,M.L.,
            Mitchell,B.D., Navis,G., Nieminen,M.S., Ohlsson,C., Poulter,N.R.,
            Qi,L., Raitakari,O.T., Rimm,E.B., Rioux,J.D., Rizzi,F., Rudan,I.,
            Salomaa,V., Sever,P.S., Shields,D.C., Shuldiner,A.R., Sinisalo,J.,
            Stanton,A.V., Stolk,R.P., Strachan,D.P., Tardif,J.C.,
            Thorsteinsdottir,U., Tuomilehto,J., van Veldhuisen,D.J.,
            Virtamo,J., Viikari,J., Vollenweider,P., Waeber,G., Widen,E.,
            Cho,Y.S., Olsen,J.V., Visscher,P.M., Willer,C., Franke,L.,
            Erdmann,J., Thompson,J.R., Pfeufer,A., Sotoodehnia,N.,
            Newton-Cheh,C., Ellinor,P.T., Stricker,B.H., Metspalu,A.,
            Perola,M., Beckmann,J.S., Smith,G.D., Stefansson,K., Wareham,N.J.,
            Munroe,P.B., Sibon,O.C., Milan,D.J., Snieder,H., Samani,N.J. and
            Loos,R.J.
  CONSRTM   Global BPgen Consortium; CARDIoGRAM Consortium; PR GWAS Consortium;
            QRS GWAS Consortium; QT-IGC Consortium; CHARGE-AF Consortium
  TITLE     Identification of heart rate-associated loci and their effects on
            cardiac conduction and rhythm disorders
  JOURNAL   Nat Genet 45 (6), 621-631 (2013)
   PUBMED   23583979
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Tripodis,N., Mason,R., Humphray,S.J., Davies,A.F., Herberg,J.A.,
            Trowsdale,J., Nizetic,D., Senger,G. and Ragoussis,J.
  TITLE     Physical map of human 6p21.2-6p21.3: region flanking the
            centromeric end of the major histocompatibility complex
  JOURNAL   Genome Res 8 (6), 631-643 (1998)
   PUBMED   9647638
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA265730.1, AI951562.1 and
            AA912142.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encode a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. More variants may
            exist, but their full-length natures could not be determined.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) lacks several 3' exons and
            contains an alternate 3' terminal exon compared to variant 1. This
            results in a novel 3' coding region and 3' UTR compared to variant
            1. The resulting isoform (b) has a shorter and distinct C-terminus
            compared to isoform a.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2161674
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..140
                     /product="copine-5 isoform b"
                     /note="copine V"
                     /calculated_mol_wt=15898
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH3.2)"
     Region          23..135
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(38,44,98,100,110)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZW4; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH3.2)"
     CDS             1..140
                     /gene="CPNE5"
                     /gene_synonym="COPN5; CPN5"
                     /coded_by="NM_001314017.1:68..490"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:57699"
                     /db_xref="HGNC:HGNC:2318"
                     /db_xref="MIM:604209"
ORIGIN      
        1 meqpedmasl sefdslagsi patkveitvs crnlldkdmf sksdplcvmy tqgmenkqwr
       61 efgrtevidn tlnpdfvrkf ivdyffeekq nlrfdlydvd skspdlskhd flgqafctlg
      121 eivgspgsrl ekplteklll
//
LOCUS       NP_006501                513 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein RFP [Homo sapiens].
ACCESSION   NP_006501
VERSION     NP_006501.1
DBSOURCE    REFSEQ: accession NM_006510.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Zhao,D., Qiang,L., Lei,Z., Ge,P., Lu,Z., Wang,Y., Zhang,X.,
            Qiang,Y., Li,B., Pang,Y., Zhang,L., Liu,C.H. and Wang,J.
  TITLE     TRIM27 elicits protective immunity against tuberculosis by
            activating TFEB-mediated autophagy flux
  JOURNAL   Autophagy 20 (7), 1483-1504 (2024)
   PUBMED   38390831
  REMARK    GeneRIF: TRIM27 elicits protective immunity against tuberculosis by
            activating TFEB-mediated autophagy flux.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Chen,Y., Xiang,Y., Miao,X., Kuai,L., Ding,X., Ma,T., Li,B. and
            Fan,B.
  TITLE     METTL14 promotes IL-6-induced viability, glycolysis and
            inflammation in HaCaT cells via the m6A modification of TRIM27
  JOURNAL   J Cell Mol Med 28 (3), e18085 (2024)
   PUBMED   38146129
  REMARK    GeneRIF: METTL14 promotes IL-6-induced viability, glycolysis and
            inflammation in HaCaT cells via the m6A modification of TRIM27.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Kimura,S., Suzuki,M., Nakamaru,Y., Kano,S., Watanabe,M., Honma,A.,
            Nakazono,A., Tsushima,N., Hatakeyama,S. and Homma,A.
  TITLE     TRIM27 expression is associated with poor prognosis in sinonasal
            mucosal melanoma
  JOURNAL   Rhinology 61 (3), 263-271 (2023)
   PUBMED   36891983
  REMARK    GeneRIF: TRIM27 expression is associated with poor prognosis in
            sinonasal mucosal melanoma.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Smits,D.J., Dekker,J., Schot,R., Tabarki,B., Alhashem,A.,
            Demmers,J.A.A., Dekkers,D.H.W., Romito,A., van der Spek,P.J., van
            Ham,T.J., Bertoli-Avella,A.M. and Mancini,G.M.S.
  TITLE     CLEC16A interacts with retromer and TRIM27, and its loss impairs
            endosomal trafficking and neurodevelopment
  JOURNAL   Hum Genet 142 (3), 379-397 (2023)
   PUBMED   36538041
  REMARK    GeneRIF: CLEC16A interacts with retromer and TRIM27, and its loss
            impairs endosomal trafficking and neurodevelopment.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Vernet,C., Boretto,J., Mattei,M.G., Takahashi,M., Jack,L.J.,
            Mather,I.H., Rouquier,S. and Pontarotti,P.
  TITLE     Evolutionary study of multigenic families mapping close to the
            human MHC class I region
  JOURNAL   J Mol Evol 37 (6), 600-612 (1993)
   PUBMED   8114113
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Isomura,T., Tamiya-Koizumi,K., Suzuki,M., Yoshida,S., Taniguchi,M.,
            Matsuyama,M., Ishigaki,T., Sakuma,S. and Takahashi,M.
  TITLE     RFP is a DNA binding protein associated with the nuclear matrix
  JOURNAL   Nucleic Acids Res 20 (20), 5305-5310 (1992)
   PUBMED   1437549
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Takahashi,M., Buma,Y., Iwamoto,T., Inaguma,Y., Ikeda,H. and Hiai,H.
  TITLE     Cloning and expression of the ret proto-oncogene encoding a
            tyrosine kinase with two potential transmembrane domains
  JOURNAL   Oncogene 3 (5), 571-578 (1988)
   PUBMED   3078962
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Takahashi,M., Inaguma,Y., Hiai,H. and Hirose,F.
  TITLE     Developmentally regulated expression of a human 'finger'-containing
            gene encoded by the 5' half of the ret transforming gene
  JOURNAL   Mol Cell Biol 8 (4), 1853-1856 (1988)
   PUBMED   3380101
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Takahashi,M. and Cooper,G.M.
  TITLE     ret transforming gene encodes a fusion protein homologous to
            tyrosine kinases
  JOURNAL   Mol Cell Biol 7 (4), 1378-1385 (1987)
   PUBMED   3037315
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL662871.9 and BC013580.1.
            
            Summary: This gene encodes a member of the tripartite motif (TRIM)
            family. The TRIM motif includes three zinc-binding domains, a RING,
            a B-box type 1 and a B-box type 2, and a coiled-coil region. This
            protein localizes to the nuclear matrix. It interacts with the
            enhancer of polycomb protein and represses gene transcription. It
            is also thought to be involved in the differentiation of male germ
            cells. Fusion of the N-terminus of this protein with the truncated
            C-terminus of the RET gene product has been shown to result in
            production of the ret transforming protein. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ420519.1, BC013580.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377199.4/ ENSP00000366404.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..513
                     /product="zinc finger protein RFP"
                     /EC_number="2.3.2.27"
                     /note="ret finger protein; tripartite motif protein
                     TRIM27; RFP transforming protein; RING finger protein 76;
                     tripartite motif-containing protein 27; RING-type E3
                     ubiquitin transferase TRIM27"
                     /calculated_mol_wt=58359
     Region          9..69
                     /region_name="RING-HC_TRIM7-like_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing proteins, TRIM7, TRIM11 and TRIM27, and
                     similar proteins; cd16594"
                     /db_xref="CDD:438256"
     Region          94..137
                     /region_name="Bbox2_TRIM7-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM7, TRIM27 and similar
                     proteins; cd19762"
                     /db_xref="CDD:380820"
     Region          131..>310
                     /region_name="COG1340"
                     /note="Uncharacterized coiled-coil protein, contains
                     DUF342 domain [Function unknown]"
                     /db_xref="CDD:440951"
     Region          315..491
                     /region_name="SPRY_PRY_TRIM27"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 27 (TRIM27), also known as RING finger protein 76
                     (RNF76); cd15814"
                     /db_xref="CDD:293986"
     Site            315..316
                     /site_type="other"
                     /note="Breakpoint for translocation to form the TRIM27/RET
                     oncogene; propagated from UniProtKB/Swiss-Prot (P14373.1)"
     CDS             1..513
                     /gene="TRIM27"
                     /gene_synonym="RFP; RNF76"
                     /coded_by="NM_006510.5:354..1895"
                     /db_xref="CCDS:CCDS4654.1"
                     /db_xref="GeneID:5987"
                     /db_xref="HGNC:HGNC:9975"
                     /db_xref="MIM:602165"
ORIGIN      
        1 masgsvaecl qqettcpvcl qyfaepmmld cghniccacl arcwgtaetn vscpqcretf
       61 pqrhmrpnrh lanvtqlvkq lrterpsgpg gemgvcekhr eplklyceed qmpicvvcdr
      121 srehrghsvl pleeavegfk eqiqnqldhl krvkdlkkrr raqgeqarae llsltqmere
      181 kivwefeqly hslkeheyrl larleeldla iynsingait qfscnishls sliaqleekq
      241 qqptrellqd igdtlsraer iripepwitp pdlqekihif aqkclfltes lkqftekmqs
      301 dmekiqelre aqlysvdvtl dpdtaypsli lsdnlrqvry sylqqdlpdn perfnlfpcv
      361 lgspcfiagr hywevevgdk akwtigvced svcrkggvts apqngfwavs lwygkeywal
      421 tspmtalplr tplqrvgifl dydagevsfy nvterchtft fshatfcgpv rpyfslsysg
      481 gksaapliic pmsgidgfsg hvgnhghsme tsp
//
LOCUS       NP_775889                244 aa            linear   PRI 20-NOV-2025
DEFINITION  INO80 complex subunit E isoform 1 [Homo sapiens].
ACCESSION   NP_775889
VERSION     NP_775889.1
DBSOURCE    REFSEQ: accession NM_173618.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 244)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 244)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 244)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 244)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 244)
  AUTHORS   Cox,E., Hwang,W., Uzoma,I., Hu,J., Guzzo,C.M., Jeong,J.,
            Matunis,M.J., Qian,J., Zhu,H. and Blackshaw,S.
  TITLE     Global Analysis of SUMO-Binding Proteins Identifies SUMOylation as
            a Key Regulator of the INO80 Chromatin Remodeling Complex
  JOURNAL   Mol Cell Proteomics 16 (5), 812-823 (2017)
   PUBMED   28254775
REFERENCE   6  (residues 1 to 244)
  AUTHORS   Vassileva,I., Yanakieva,I., Peycheva,M., Gospodinov,A. and
            Anachkova,B.
  TITLE     The mammalian INO80 chromatin remodeling complex is required for
            replication stress recovery
  JOURNAL   Nucleic Acids Res 42 (14), 9074-9086 (2014)
   PUBMED   25016522
REFERENCE   7  (residues 1 to 244)
  AUTHORS   Chen,L., Cai,Y., Jin,J., Florens,L., Swanson,S.K., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit organization of the human INO80 chromatin remodeling
            complex: an evolutionarily conserved core complex catalyzes
            ATP-dependent nucleosome remodeling
  JOURNAL   J Biol Chem 286 (13), 11283-11289 (2011)
   PUBMED   21303910
REFERENCE   8  (residues 1 to 244)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   9  (residues 1 to 244)
  AUTHORS   Yao,T., Song,L., Jin,J., Cai,Y., Takahashi,H., Swanson,S.K.,
            Washburn,M.P., Florens,L., Conaway,R.C., Cohen,R.E. and
            Conaway,J.W.
  TITLE     Distinct modes of regulation of the Uch37 deubiquitinating enzyme
            in the proteasome and in the Ino80 chromatin-remodeling complex
  JOURNAL   Mol Cell 31 (6), 909-917 (2008)
   PUBMED   18922472
REFERENCE   10 (residues 1 to 244)
  AUTHORS   Jin,J., Cai,Y., Yao,T., Gottschalk,A.J., Florens,L., Swanson,S.K.,
            Gutierrez,J.L., Coleman,M.K., Workman,J.L., Mushegian,A.,
            Washburn,M.P., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian chromatin remodeling complex with similarities to the
            yeast INO80 complex
  JOURNAL   J Biol Chem 280 (50), 41207-41212 (2005)
   PUBMED   16230350
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK075133.1, BC047712.2 and AC093512.2.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075133.1, AK130409.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000563197.6/ ENSP00000457016.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..244
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..244
                     /product="INO80 complex subunit E isoform 1"
                     /note="coiled-coil domain containing 95; coiled-coil
                     domain-containing protein 95"
                     /calculated_mol_wt=26347
     Region          63..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBZ0.1)"
     CDS             1..244
                     /gene="INO80E"
                     /gene_synonym="CCDC95"
                     /coded_by="NM_173618.3:71..805"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10665.1"
                     /db_xref="GeneID:283899"
                     /db_xref="HGNC:HGNC:26905"
ORIGIN      
        1 mngpadgevd ykkkyrnlkr klkfliyehe cfqeelrkaq rkllkvsrdk sflldrllqy
       61 envdedssds datassdnse tegtpklsdt papkrkrspp lggapspssl slppstgfpl
      121 qasgvpspyl sslassrypp fpsdylalql pepsplrpkr ekrprlprkl kmavgppdcp
      181 vggpltfpgr gsgagvgttl tplpppkmpp ptilstvprq mfsdagsgdd aldgdddlvi
      241 dipe
//
LOCUS       NP_001036818             247 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.4cy [Homo sapiens].
ACCESSION   NP_001036818
VERSION     NP_001036818.1
DBSOURCE    REFSEQ: accession NM_001043353.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 247)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 247)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 247)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 247)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 247)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA472065.1, BI546300.1,
            BG706843.1, BX419658.2, BM674269.1, AK123113.1, AL590431.11 and
            AA863064.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (Tpm3.4, also known as variant 5)
            lacks an exon and contains an alternate exon in the central coding
            region, and uses an alternate splice site in the 3' coding region,
            compared to variant Tpm3.1. The encoded isoform (Tpm3.4cy, also
            known as isoform 5 or Tm5NM4) is shorter and has a distinct
            C-terminus, compared to isoform Tpm3.1cy.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.28721.1,
                                           SRR1803611.114460.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..247
                     /product="tropomyosin alpha-3 chain isoform Tpm3.4cy"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=28662
     Region          12..245
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..247
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001043353.2:100..843"
                     /note="isoform Tpm3.4cy is encoded by transcript variant
                     Tpm3.4"
                     /db_xref="CCDS:CCDS41401.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 magittieav krkiqvlqqq addaeeraer lqrevegerr areqaeaeva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienralk deekmelqei qlkeakhiae
      121 eadrkyeeva rklviiegdl erteeraela eskcseleee lknvtnnlks leaqaekysq
      181 kedkyeeeik iltdklkeae traefaersv aklektiddl eerlysqler nrllsnelkl
      241 tlhdlcd
//
LOCUS       NP_078843                420 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_078843
VERSION     NP_078843.2
DBSOURCE    REFSEQ: accession NM_024567.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 420)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 420)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 420)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 420)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 420)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 420)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 420)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 420)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 420)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 420)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC069242.1, AC108449.5 and BQ019252.1.
            
            On May 6, 2004 this sequence version replaced NP_078843.1.
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1,
            2, and 3 all encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC069242.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..420
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..420
                     /product="homeobox-containing protein 1 isoform 1"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=47147
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          353..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..420
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_024567.4:401..1663"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6071.1"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr anieaailes hgidvqspgg
      361 hsnsddvdgn dyseqddsts hsdhqdpisl avemaavnht ilalarqgan eiktealddd
//
LOCUS       NP_001186703             183 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-5 isoform 2 [Homo sapiens].
ACCESSION   NP_001186703
VERSION     NP_001186703.1
DBSOURCE    REFSEQ: accession NM_001199774.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Xie,S., Li,X., Yan,J., Yu,H., Chen,S. and Chen,K.
  TITLE     Knockdown of liver cancer cell-secreted exosomal PSMA5 controls
            macrophage polarization to restrain cancer progression by blocking
            JAK2/STAT3 signaling
  JOURNAL   Immun Inflamm Dis 12 (2), e1146 (2024)
   PUBMED   38415977
  REMARK    GeneRIF: Knockdown of liver cancer cell-secreted exosomal PSMA5
            controls macrophage polarization to restrain cancer progression by
            blocking JAK2/STAT3 signaling.
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 183)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC324021.1, BM793388.1,
            AL390252.9 and H08369.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. Multiple alternatively spliced transcript variants
            encoding two distinct isoforms have been found for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (4) has an alternate 5' UTR exon,
            resulting in a downstream AUG start codon, as compared to variant
            1. The resulting isoform (2) is shorter at the N-terminus, as
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2882971.1,
                                           SRR14372079.3592557.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..183
                     /product="proteasome subunit alpha type-5 isoform 2"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit zeta; proteasome subunit zeta;
                     proteasome zeta chain; macropain zeta chain;
                     multicatalytic endopeptidase complex zeta chain;
                     proteasome component 5; proteasome subunit alpha type-5;
                     proteasome alpha 5 subunit; alpha-5; proteasome (prosome,
                     macropain) subunit, alpha type, 5; epididymis tissue sperm
                     binding protein Li 11n; proteasome subunit alpha 5"
                     /calculated_mol_wt=19904
     Region          <1..162
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     CDS             1..183
                     /gene="PSMA5"
                     /gene_synonym="PSC5; ZETA"
                     /coded_by="NM_001199774.2:175..726"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55619.1"
                     /db_xref="GeneID:5686"
                     /db_xref="HGNC:HGNC:9534"
                     /db_xref="MIM:176844"
ORIGIN      
        1 mepssiekiv eidahigcam sgliadaktl idkarvetqn hwftynetmt vesvtqavsn
       61 lalqfgeeda dpgamsrpfg vallfggvde kgpqlfhmdp sgtfvqcdar aigsasegaq
      121 sslqevyhks mtlkeaikss liilkqvmee klnatniela tvqpgqnfhm ftkeeleevi
      181 kdi
//
LOCUS       NP_001243893             411 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial potassium channel isoform 1 [Homo sapiens].
ACCESSION   NP_001243893
VERSION     NP_001243893.1
DBSOURCE    REFSEQ: accession NM_001256964.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 411)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 411)
  AUTHORS   Paggio,A., Checchetto,V., Campo,A., Menabo,R., Di Marco,G., Di
            Lisa,F., Szabo,I., Rizzuto,R. and De Stefani,D.
  TITLE     Identification of an ATP-sensitive potassium channel in
            mitochondria
  JOURNAL   Nature 572 (7771), 609-613 (2019)
   PUBMED   31435016
REFERENCE   5  (residues 1 to 411)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 411)
  AUTHORS   Wang,C. and Brennan,W.A. Jr.
  TITLE     Rat skeletal muscle, liver and brain have different fetal and adult
            forms of the glucose transporter
  JOURNAL   Biochim Biophys Acta 946 (1), 11-18 (1988)
   PUBMED   3145016
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134772.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1 and 2
            encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.356057.1,
                                           SRR3476690.900146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395694.7/ ENSP00000379047.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..411
                     /product="mitochondrial potassium channel isoform 1"
                     /note="coiled-coil domain-containing protein 51;
                     mitochondrial potassium channel"
                     /calculated_mol_wt=41892
     transit_peptide 1..35
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96ER9.2)"
                     /calculated_mol_wt=3938
     mat_peptide     36..411
                     /product="Mitochondrial potassium channel.
                     /evidence=ECO:0000255. /id=PRO_0000288868"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ER9.2)"
                     /calculated_mol_wt=41892
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96ER9.2)"
     Region          112..>201
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ER9.2)"
     Region          274..294
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ER9.2)"
     Site            387..407
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96ER9.2)"
     CDS             1..411
                     /gene="CCDC51"
                     /gene_synonym="MITOK"
                     /coded_by="NM_001256964.2:141..1376"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2766.2"
                     /db_xref="GeneID:79714"
                     /db_xref="HGNC:HGNC:25714"
                     /db_xref="MIM:618585"
ORIGIN      
        1 mmgrspgfam qhivgvphvl vrrgllgrdl fmtrtlcspg psqpgekrpe evalglhhrl
       61 palgralghs iqqratstak twwdryeefv glnevreaqg kvteaekvfm varglvrear
      121 edlevhqakl kevrdrldrv sredsqylel atlehrmlqe ekrlrtaylr aedserekfs
      181 lfsaavresh ekertraert knwsligsvl galigvagst yvnrvrlqel kallleaqkg
      241 pvslqeaire qassysrqqr dlhnlmvdlr glvhaagpgq dsgsqagspp trdrdvdvls
      301 aalkeqlshs rqvhsclegl reqldglekt csqmagvvql vksaahpglv epadgampsf
      361 lleqgsmila lsdteqrlea qvnrntiyst lvtcvtfvat lpvlymlfka s
//
LOCUS       NP_002060                354 aa            linear   PRI 20-NOV-2025
DEFINITION  guanine nucleotide-binding protein G(i) subunit alpha-1 isoform 1
            [Homo sapiens].
ACCESSION   NP_002060
VERSION     NP_002060.4
DBSOURCE    REFSEQ: accession NM_002069.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Ham,D., Shihoya,W., Nureki,O., Inoue,A. and Chung,K.Y.
  TITLE     Molecular mechanism of the endothelin receptor type B interactions
            with Gs, Gi, and Gq
  JOURNAL   Structure 32 (10), 1632-1639 (2024)
   PUBMED   39043181
  REMARK    GeneRIF: Molecular mechanism of the endothelin receptor type B
            interactions with Gs, Gi, and Gq.
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Hu,X., Chen,F., Jia,L., Long,A., Peng,Y., Li,X., Huang,J., Wei,X.,
            Fang,X., Gao,Z., Zhang,M., Liu,X., Chen,Y.G., Wang,Y., Zhang,H. and
            Wang,Y.
  TITLE     A gut-derived hormone regulates cholesterol metabolism
  JOURNAL   Cell 187 (7), 1685-1700 (2024)
   PUBMED   38503280
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Wang,W.W., Ji,S.Y., Zhang,W., Zhang,J., Cai,C., Hu,R., Zang,S.K.,
            Miao,L., Xu,H., Chen,L.N., Yang,Z., Guo,J., Qin,J., Shen,D.D.,
            Liang,P., Zhang,Y. and Zhang,Y.
  TITLE     Structure-based design of non-hypertrophic apelin receptor
            modulator
  JOURNAL   Cell 187 (6), 1460-1475 (2024)
   PUBMED   38428423
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Yin,D.P., Zhang,H., Teng,H., Zhang,D., Chen,P., Xie,L. and Liu,J.S.
  TITLE     Overexpressed Galphai1 exerts pro-tumorigenic activity in
            nasopharyngeal carcinoma
  JOURNAL   Cell Death Dis 14 (12), 792 (2023)
   PUBMED   38049415
  REMARK    GeneRIF: Overexpressed Galphai1 exerts pro-tumorigenic activity in
            nasopharyngeal carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Bonkowski,E., Fathi,E. and Mefford,H.C.
  TITLE     GNAI1-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   39083633
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Gennity,J.M. and Siess,W.
  TITLE     Thrombin inhibits the pertussis-toxin-dependent ADP-ribosylation of
            a novel soluble Gi-protein in human platelets
  JOURNAL   Biochem J 279 (Pt 3) (Pt 3), 643-650 (1991)
   PUBMED   1953657
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Jiang,M., Pandey,S., Tran,V.T. and Fong,H.K.
  TITLE     Guanine nucleotide-binding regulatory proteins in retinal pigment
            epithelial cells
  JOURNAL   Proc Natl Acad Sci U S A 88 (9), 3907-3911 (1991)
   PUBMED   1902575
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Itoh,H., Toyama,R., Kozasa,T., Tsukamoto,T., Matsuoka,M. and
            Kaziro,Y.
  TITLE     Presence of three distinct molecular species of Gi protein alpha
            subunit. Structure of rat cDNAs and human genomic DNAs
  JOURNAL   J Biol Chem 263 (14), 6656-6664 (1988)
   PUBMED   2834384
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Suki,W.N., Abramowitz,J., Mattera,R., Codina,J. and Birnbaumer,L.
  TITLE     The human genome encodes at least three non-allellic G proteins
            with alpha i-type subunits
  JOURNAL   FEBS Lett 220 (1), 187-192 (1987)
   PUBMED   2440724
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004159.1 and AC080066.6.
            
            On Aug 20, 2003 this sequence version replaced NP_002060.3.
            
            Summary: Guanine nucleotide binding proteins are heterotrimeric
            signal-transducing molecules consisting of alpha, beta, and gamma
            subunits. The alpha subunit binds guanine nucleotide, can hydrolyze
            GTP, and can interact with other proteins. The protein encoded by
            this gene represents the alpha subunit of an inhibitory complex.
            The encoded protein is part of a complex that responds to
            beta-adrenergic signals by inhibiting adenylate cyclase. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.205066.1,
                                           SRR1660803.118122.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649796.2/ ENSP00000497260.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..354
                     /product="guanine nucleotide-binding protein G(i) subunit
                     alpha-1 isoform 1"
                     /note="Gi1 protein alpha subunit; guanine
                     nucleotide-binding protein G(i) subunit alpha-1; adenylate
                     cyclase-inhibiting G alpha protein; guanine nucleotide
                     binding protein (G protein), alpha inhibiting activity
                     polypeptide 1; heterotrimeric guanine nucleotide-binding
                     protein 1B"
                     /calculated_mol_wt=40230
     Region          34..348
                     /region_name="G-alpha"
                     /note="Alpha subunit of G proteins (guanine nucleotide
                     binding); cd00066"
                     /db_xref="CDD:206639"
     Region          35..48
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63096.2)"
     Site            order(40,45..47,181,200,203,269..270,272,325..326)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206639"
     Site            40..47
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206639"
     Site            order(41..43,71,75,79,82,85..86,104,107,149,178,203,211,
                     215)
                     /site_type="active"
                     /note="GoLoco binding site [active]"
                     /db_xref="CDD:206639"
     Region          173..181
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63096.2)"
     Site            176..184
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206639"
     Site            181
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206639"
     Site            order(182,184,186,197,199,203..205,207,210..211,213..216)
                     /site_type="other"
                     /note="beta - gamma complex interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Site            order(184,209,212..213,216)
                     /site_type="other"
                     /note="adenylyl cyclase interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206639"
     Region          196..205
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63096.2)"
     Site            200..203
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206639"
     Site            201..217
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206639"
     Region          265..272
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63096.2)"
     Site            269..272
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206639"
     Site            order(317..328,330..333)
                     /site_type="active"
                     /note="putative receptor binding site [active]"
                     /db_xref="CDD:206639"
     Region          324..329
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01230"
                     /note="propagated from UniProtKB/Swiss-Prot (P63096.2)"
     Site            325..327
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206639"
     CDS             1..354
                     /gene="GNAI1"
                     /gene_synonym="Gi; HG1B; NEDHISB"
                     /coded_by="NM_002069.6:331..1395"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5595.1"
                     /db_xref="GeneID:2770"
                     /db_xref="HGNC:HGNC:4384"
                     /db_xref="MIM:139310"
ORIGIN      
        1 mgctlsaedk aaverskmid rnlredgeka arevkllllg agesgkstiv kqmkiiheag
       61 yseeeckqyk avvysntiqs iiaiiramgr lkidfgdsar addarqlfvl agaaeegfmt
      121 aelagvikrl wkdsgvqacf nrsreyqlnd saayylndld riaqpnyipt qqdvlrtrvk
      181 ttgivethft fkdlhfkmfd vggqrserkk wihcfegvta iifcvalsdy dlvlaedeem
      241 nrmhesmklf dsicnnkwft dtsiilflnk kdlfeekikk splticypey agsntyeeaa
      301 ayiqcqfedl nkrkdtkeiy thftcatdtk nvqfvfdavt dviiknnlkd cglf
//
LOCUS       NP_001340036             369 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001340036 XP_005256782
VERSION     NP_001340036.1
DBSOURCE    REFSEQ: accession NM_001353107.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            On Jun 29, 2017 this sequence version replaced XP_005256782.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.63123.1,
                                           SRR1660809.58493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..369
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 1"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=40795
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Region          20..138
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          179..363
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60256.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     CDS             1..369
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353107.2:164..1273"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS11200.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mfcvtppele tkmnitkggl vlfsansnss cmelskkiae rlgvemgkvq vyqepnretr
       61 vqiqesvrgk dvfiiqtvsk dvnttimell imvyacktsc aksiigvipy fpyskqckmr
      121 krgsivskll asmmckaglt hlitmdlhqk eiqgffnipv dnlraspfll qyiqeeipdy
      181 rnavivaksp asakraqsfa erlrlgiavi hgeaqdaesd lvdgrhsppm vrsvaaihps
      241 leipmlipke kppitvvgdv ggriaiivdd iiddvdsfla aaetlkerga ykifvmathg
      301 llssdaprri eesaidevvv tntiphevqk lqcpkiktvd ismilseair rihngesmsy
      361 lfrnigldd
//
LOCUS       NP_001308003             764 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 4 isoform 3 [Homo sapiens].
ACCESSION   NP_001308003 XP_005256546
VERSION     NP_001308003.1
DBSOURCE    REFSEQ: accession NM_001321074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Fadahunsi,N., Petersen,J., Metz,S., Jakobsen,A., Vad Mathiesen,C.,
            Silke Buch-Rasmussen,A., Kurgan,N., Kjaergaard Larsen,J.,
            Andersen,R.C., Topilko,T., Svendsen,C., Apuschkin,M., Skovbjerg,G.,
            Hendrik Schmidt,J., Houser,G., Elgaard Jager,S., Bach,A.,
            Deshmukh,A.S., Kilpelainen,T.O., Stromgaard,K., Madsen,K.L. and
            Clemmensen,C.
  TITLE     Targeting postsynaptic glutamate receptor scaffolding proteins
            PSD-95 and PICK1 for obesity treatment
  JOURNAL   Sci Adv 10 (9), eadg2636 (2024)
   PUBMED   38427737
  REMARK    GeneRIF: Targeting postsynaptic glutamate receptor scaffolding
            proteins PSD-95 and PICK1 for obesity treatment.
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Shen,Z., Sun,D., Savastano,A., Varga,S.J., Cima-Omori,M.S.,
            Becker,S., Honigmann,A. and Zweckstetter,M.
  TITLE     Multivalent Tau/PSD-95 interactions arrest in vitro condensates and
            clusters mimicking the postsynaptic density
  JOURNAL   Nat Commun 14 (1), 6839 (2023)
   PUBMED   37891164
  REMARK    GeneRIF: Multivalent Tau/PSD-95 interactions arrest in vitro
            condensates and clusters mimicking the postsynaptic density.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Shimizu,H. and Hohjoh,H.
  TITLE     FMRP, FXR1 protein and Dlg4 mRNA, which are associated with fragile
            X syndrome, are involved in the ubiquitin-proteasome system
  JOURNAL   Sci Rep 13 (1), 1956 (2023)
   PUBMED   36732356
  REMARK    GeneRIF: FMRP, FXR1 protein and Dlg4 mRNA, which are associated
            with fragile X syndrome, are involved in the ubiquitin-proteasome
            system.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Niethammer,M., Kim,E. and Sheng,M.
  TITLE     Interaction between the C terminus of NMDA receptor subunits and
            multiple members of the PSD-95 family of membrane-associated
            guanylate kinases
  JOURNAL   J Neurosci 16 (7), 2157-2163 (1996)
   PUBMED   8601796
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Kornau,H.C., Schenker,L.T., Kennedy,M.B. and Seeburg,P.H.
  TITLE     Domain interaction between NMDA receptor subunits and the
            postsynaptic density protein PSD-95
  JOURNAL   Science 269 (5231), 1737-1740 (1995)
   PUBMED   7569905
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Tumer,Z., Dye,T.J., Prada,C., White-Brown,A.M., MacKenzie,A. and
            Levy,A.M.
  TITLE     DLG4-Related Synaptopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37347881
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC120057.9, DB064366.1,
            BC136553.1, BC030203.1 and AI571947.1.
            
            On Mar 18, 2016 this sequence version replaced XP_005256546.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. It heteromultimerizes with another
            MAGUK protein, DLG2, and is recruited into NMDA receptor and
            potassium channel clusters. These two MAGUK proteins may interact
            at postsynaptic sites to form a multimeric scaffold for the
            clustering of receptors, ion channels, and associated signaling
            proteins. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..764
                     /product="disks large homolog 4 isoform 3"
                     /note="disks large homolog 4; Tax interaction protein 15;
                     post-synaptic density protein 95; synapse-associated
                     protein 90; discs large homolog 4"
                     /calculated_mol_wt=84929
     Region          <26..49
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          54..104
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          103..191
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(114..120,137,140,170,174,177..178)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          200..284
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(209..215,232,235,265,269,272..273)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          285..352
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          350..440
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(362..368,379,382,412,416,419..420)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          470..535
                     /region_name="SH3_DLG4"
                     /note="Src Homology 3 domain of Disks Large homolog 4;
                     cd12030"
                     /db_xref="CDD:212963"
     Site            order(474,496)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212963"
     Site            order(477,479,482,491,509..510,529,531..532)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212963"
     Region          573..751
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..764
                     /gene="DLG4"
                     /gene_synonym="MRD62; PSD95; SAP-90; SAP90"
                     /coded_by="NM_001321074.1:1202..3496"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92245.1"
                     /db_xref="GeneID:1742"
                     /db_xref="HGNC:HGNC:2903"
                     /db_xref="MIM:602887"
ORIGIN      
        1 msqrpraprs alwllappll rwapplltvl hsdlfqalld ildyyeasls esqkyryqde
       61 dtpplehspa hlpnqanspp vivntdtlea pgyvngtege meyeeitler gnsglgfsia
      121 ggtdnphigd dpsifitkii pggaaaqdgr lrvndsilfv nevdvrevth saavealkea
      181 gsivrlyvmr rkppaekvme iklikgpkgl gfsiaggvgn qhipgdnsiy vtkiieggaa
      241 hkdgrlqigd kilavnsvgl edvmhedava alkntydvvy lkvakpsnay lsdsyappdi
      301 ttsysqhldn eishssylgt dyptamtpts prryspvakd llgeedipre prrivihrgs
      361 tglgfnivgg edgegifisf ilaggpadls gelrkgdqil svngvdlrna sheqaaialk
      421 nagqtvtiia qykpeeysrf eakihdlreq lmnsslgsgt aslrsnpkrg fyiralfdyd
      481 ktkdcgflsq alsfrfgdvl hvidasdeew wqarrvhsds etddigfips krrverrews
      541 rlkakdwgss sgsqgredsv lsyetvtqme vhyarpiiil gptkdrandd llsefpdkfg
      601 scvphttrpk reyeidgrdy hfvssrekme kdiqahkfie agqynshlyg tsvqsvreva
      661 eqgkhcildv sanavrrlqa ahlhpiaifi rprslenvle inkriteeqa rkafdratkl
      721 eqeftecfsa ivegdsfeei yhkvkrvied lsgpyiwvpa rerl
//
LOCUS       NP_001303870             273 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform c [Homo sapiens].
ACCESSION   NP_001303870 XP_011526411
VERSION     NP_001303870.1
DBSOURCE    REFSEQ: accession NM_001316941.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB127388.1, AC008752.6, CN427140.1 and AK000195.1.
            
            On Nov 5, 2015 this sequence version replaced XP_011526411.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (7) lacks an alternate exon and
            uses a downstream AUG start codon compared to variant 1. The
            resulting isoform (c) is shorter at the N-terminus compared to
            isoform a. Variants 3, 4, 5, 6, 7, and 8 all encode the same
            isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.705631.1,
                                           SRR1163658.256478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..273
                     /product="F-box/LRR-repeat protein 12 isoform c"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=30360
     Region          51..72
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          68..>173
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          100..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <114..238
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          125..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          151..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          231..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..273
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_001316941.2:353..1174"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS82287.1"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 mrpkvmwhll rrymasrlhs lrmggylfsg sqapqlspal lralgqkcpn lkrlclhvad
       61 lsmvpitslp stlrtlelhs ceismawlhk qqdptvlpll ecivldrvpa frdehlqglt
      121 rfralrslvl ggtyrvtetg ldaglqelsy lqrlevlgct lsadstllai srhlrdvrki
      181 rltvrglsap glavlegmpa leslclqgpl vtpempspte ilsscltmpk lrvlelqglg
      241 wegqeaekil ckglphcmvi vracpkesmd wwm
//
LOCUS       NP_001354465             535 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 29 [Homo sapiens].
ACCESSION   NP_001354465
VERSION     NP_001354465.1
DBSOURCE    REFSEQ: accession NM_001367536.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 535)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 535)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 535)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 535)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 535)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 535)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 535)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 535)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 535)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 535)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..535
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..535
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 29"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=59720
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          403..530
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..535
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367536.1:95..1702"
                     /note="isoform 29 is encoded by transcript variant 29"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmpqsnnkns lvspaqepap lqtamgstes cntttededl kvrkqeiiki teqlieainn
      421 gdfeaytkic dpgltsfepe algnlvegmd fhkfyfenll sknskpihtt ilnphvhvig
      481 edaaciayir ltqyidgqgr prtsqseetr vwhrrdgkwl nvhyhcsgap aaplq
//
LOCUS       NP_001230162             537 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform i [Homo sapiens].
ACCESSION   NP_001230162
VERSION     NP_001230162.1
DBSOURCE    REFSEQ: accession NM_001243233.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK300612.1 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (9) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            3' end of an exon compared to variant 3. The resulting isoform (i)
            is shorter at the N-terminus and lacks an alternate internal
            segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300612.1, SRR14038194.1166617.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..537
                     /product="transcription factor 4 isoform i"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=57294
     Region          428..512
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(436,440,442..444,446,451,472..473)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(449..450,453..454,456..457,460,464,474,477,481,484,
                     487..492)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..537
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243233.2:205..1818"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS58626.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg ypsskpatst fpssffmqdg hhssdpwsss sgmnqpgyag mlgnsshipq
      121 sssycslhph erlsypshss adinsslppm stfhrsgtnh ystssctppa ngtdsimanr
      181 gsgaagssqt gdalgkalas iyspdhtnns fssnpstpvg sppslsagta vwsrnggqas
      241 sspnyegplh slqsriedrl erlddaihvl rnhavgpsta mpgghgdmhg iigpshngam
      301 gglgsgygtg llsanrhslm vgthredgva lrgshsllpn qvpvpqlpvq satspdlnpp
      361 qdpyrgmppg lqgqsvssgs seiksddegd enlqdtksse dkkldddkkd iksitsnndd
      421 edltpeqkae rekerrmann arerlrvrdi neafkelgrm vqlhlksdkp qtkllilhqa
      481 vavilsleqq vrernlnpka aclkrreeek vsseppplsl agphpgmgda snhmgqm
//
LOCUS       NP_003325               1058 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-like modifier-activating enzyme 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_003325
VERSION     NP_003325.2
DBSOURCE    REFSEQ: accession NM_003334.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1058)
  AUTHORS   Sirenko,M., Bernard,E., Creignou,M., Domenico,D., Farina,A., Arango
            Ossa,J.E., Kosmider,O., Hasserjian,R., Jadersten,M., Germing,U.,
            Sanz,G., van de Loosdrecht,A.A., Gurnari,C., Follo,M.Y., Thol,F.,
            Zamora,L., Pinheiro,R.F., Pellagatti,A., Elias,H.K., Haase,D.,
            Sander,B., Orna,E., Zoldan,K., Eder,L.N., Sperr,W.R.,
            Thalhammer,R., Ganster,C., Ades,L., Tobiasson,M., Palomo,L., Della
            Porta,M.G., Huberman,K., Fenaux,P., Belickova,M., Savona,M.R.,
            Klimek,V.M., Santos,F.P.S., Boultwood,J., Kotsianidis,I.,
            Santini,V., Sole,F., Platzbecker,U., Heuser,M., Valent,P.,
            Finelli,C., Voso,M.T., Shih,L.Y., Ogawa,S., Fontenay,M.,
            Jansen,J.H., Cervera,J., Ebert,B.L., Bejar,R., Greenberg,P.L.,
            Gattermann,N., Malcovati,L., Cazzola,M., Beck,D.B.,
            Hellstrom-Lindberg,E. and Papaemmanuil,E.
  TITLE     Molecular and clinical presentation of UBA1-mutated myelodysplastic
            syndromes
  JOURNAL   Blood 144 (11), 1221-1229 (2024)
   PUBMED   38687605
  REMARK    GeneRIF: Molecular and clinical presentation of UBA1-mutated
            myelodysplastic syndromes.
REFERENCE   2  (residues 1 to 1058)
  AUTHORS   Chen,C., Li,Y., Chen,Z., Shi,P., Li,Y. and Qian,S.
  TITLE     A comprehensive prognostic and immune infiltration analysis of UBA1
            in pan-cancer: A computational analysis and in vitro experiments
  JOURNAL   J Cell Mol Med 28 (16), e70037 (2024)
   PUBMED   39183260
  REMARK    GeneRIF: A comprehensive prognostic and immune infiltration
            analysis of UBA1 in pan-cancer: A computational analysis and in
            vitro experiments.
REFERENCE   3  (residues 1 to 1058)
  AUTHORS   Corty,R.W., Brogan,J., Byram,K., Springer,J., Grayson,P.C. and
            Bick,A.G.
  TITLE     VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse Individuals
            in the NIH All Of Us Cohort
  JOURNAL   Arthritis Rheumatol 76 (6), 942-948 (2024)
   PUBMED   38225170
  REMARK    GeneRIF: VEXAS-Defining UBA1 Somatic Variants in 245,368 Diverse
            Individuals in the NIH All Of Us Cohort.
REFERENCE   4  (residues 1 to 1058)
  AUTHORS   Collins,J.C., Magaziner,S.J., English,M., Hassan,B., Chen,X.,
            Balanda,N., Anderson,M., Lam,A., Fernandez-Pol,S., Kwong,B.,
            Greenberg,P.L., Terrier,B., Likhite,M.E., Kosmider,O., Wang,Y.,
            Samara,N.L., Walters,K.J., Beck,D.B. and Werner,A.
  TITLE     Shared and distinct mechanisms of UBA1 inactivation across
            different diseases
  JOURNAL   EMBO J 43 (10), 1919-1946 (2024)
   PUBMED   38360993
  REMARK    GeneRIF: Shared and distinct mechanisms of UBA1 inactivation across
            different diseases.
REFERENCE   5  (residues 1 to 1058)
  AUTHORS   Hadjadj,J. and Beck,D.
  TITLE     VEXAS Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373178
REFERENCE   6  (residues 1 to 1058)
  AUTHORS   Baumbach-Reardon,L., Hunter,J.M., Ahearn,M.E. and Pfautsch,M.
  TITLE     Spinal Muscular Atrophy, X-Linked Infantile
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301739
REFERENCE   7  (residues 1 to 1058)
  AUTHORS   Schwartz,A.L., Trausch,J.S., Ciechanover,A., Slot,J.W. and Geuze,H.
  TITLE     Immunoelectron microscopic localization of the ubiquitin-activating
            enzyme E1 in HepG2 cells
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5542-5546 (1992)
   PUBMED   1376922
REFERENCE   8  (residues 1 to 1058)
  AUTHORS   Ayusawa,D., Kaneda,S., Itoh,Y., Yasuda,H., Murakami,Y.,
            Sugasawa,K., Hanaoka,F. and Seno,T.
  TITLE     Complementation by a cloned human ubiquitin-activating enzyme E1 of
            the S-phase-arrested mouse FM3A cell mutant with thermolabile E1
  JOURNAL   Cell Struct Funct 17 (2), 113-122 (1992)
   PUBMED   1606621
REFERENCE   9  (residues 1 to 1058)
  AUTHORS   Takahashi,E., Ayusawa,D., Kaneda,S., Itoh,Y., Seno,T. and Hori,T.
  TITLE     The human ubiquitin-activating enzyme E1 gene (UBE1) mapped to band
            Xp11.3----p11.23 by fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 59 (4), 268-269 (1992)
   PUBMED   1544321
REFERENCE   10 (residues 1 to 1058)
  AUTHORS   Kudo,M., Sugasawa,K., Hori,T., Enomoto,T., Hanaoka,F. and Ui,M.
  TITLE     Human ubiquitin-activating enzyme (E1): compensation for
            heat-labile mouse E1 and its gene localization on the X chromosome
  JOURNAL   Exp Cell Res 192 (1), 110-117 (1991)
   PUBMED   1845793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI547207.1, M58028.1 and
            BC013041.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 7, 2002 this sequence version replaced NP_003325.1.
            
            Summary: The protein encoded by this gene catalyzes the first step
            in ubiquitin conjugation to mark cellular proteins for degradation.
            This gene complements an X-linked mouse temperature-sensitive
            defect in DNA synthesis, and thus may function in DNA repair. It is
            part of a gene cluster on chromosome Xp11.23. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.128662.1,
                                           SRR1660807.76023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335972.11/ ENSP00000338413.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1058
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.3"
     Protein         1..1058
                     /product="ubiquitin-like modifier-activating enzyme 1
                     isoform 1"
                     /EC_number="6.2.1.45"
                     /note="POC20 centriolar protein homolog; UBA1,
                     ubiquitin-activating enzyme E1 homolog A; A1S9T and BN75
                     temperature sensitivity complementing; testicular
                     secretory protein Li 63"
                     /calculated_mol_wt=117718
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9099746; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          5..11
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Region          49..1055
                     /region_name="Ube1"
                     /note="ubiquitin-activating enzyme E1; TIGR01408"
                     /db_xref="CDD:273603"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Region          63..611
                     /region_name="2 approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P22314.3)"
     Site            671
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            810
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q02053; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     Site            980
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P22314.3)"
     CDS             1..1058
                     /gene="UBA1"
                     /gene_synonym="A1S9; A1S9T; A1ST; AMCX1; CFAP124; GXP1;
                     POC20; SMAX2; UBA1A; UBE1; UBE1X; VEXAS"
                     /coded_by="NM_003334.4:197..3373"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14275.1"
                     /db_xref="GeneID:7317"
                     /db_xref="HGNC:HGNC:12469"
                     /db_xref="MIM:314370"
ORIGIN      
        1 msssplskkr rvsgpdpkpg sncspaqsvl sevpsvptng makngseadi deglysrqly
       61 vlgheamkrl qtssvlvsgl rglgveiakn iilggvkavt lhdqgtaqwa dlssqfylre
      121 edigknraev sqprlaelns yvpvtaytgp lvedflsgfq vvvltntple dqlrvgefch
      181 nrgiklvvad trglfgqlfc dfgeemiltd sngeqplsam vsmvtkdnpg vvtcldearh
      241 gfesgdfvsf sevqgmveln gnqpmeikvl gpytfsicdt snfsdyirgg ivsqvkvpkk
      301 isfkslvasl aepdfvvtdf akfsrpaqlh igfqalhqfc aqhgrpprpr needaaelva
      361 laqavnaral pavqqnnlde dlirklayva agdlapinaf igglaaqevm kacsgkfmpi
      421 mqwlyfdale clpedkevlt edkclqrqnr ydgqvavfgs dlqeklgkqk yflvgagaig
      481 cellknfami glgcgeggei ivtdmdtiek snlnrqflfr pwdvtklksd taaaavrqmn
      541 phirvtshqn rvgpdteriy dddffqnldg vanaldnvda rmymdrrcvy yrkpllesgt
      601 lgtkgnvqvv ipfltesyss sqdppeksip ictlknfpna iehtlqward efeglfkqpa
      661 envnqyltdp kfvertlrla gtqplevlea vqrslvlqrp qtwadcvtwa chhwhtqysn
      721 nirqllhnfp pdqltssgap fwsgpkrcph pltfdvnnpl hldyvmaaan lfaqtygltg
      781 sqdraavatf lqsvqvpeft pksgvkihvs dqelqsanas vddsrleelk atlpspdklp
      841 gfkmypidfe kdddsnfhmd fivaasnlra enydipsadr hkskliagki ipaiatttaa
      901 vvglvclely kvvqghrqld sykngflnla lpffgfsepl aaprhqyynq ewtlwdrfev
      961 qglqpngeem tlkqfldyfk tehkleitml sqgvsmlysf fmpaaklker ldqpmteivs
     1021 rvskrklgrh vralvlelcc ndesgedvev pyvrytir
//
LOCUS       NP_001308719             960 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform d [Homo sapiens].
ACCESSION   NP_001308719
VERSION     NP_001308719.1
DBSOURCE    REFSEQ: accession NM_001321790.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 960)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 960)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 960)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 960)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 960)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 960)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 960)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302533.1, AK316276.1,
            AC016138.8 and AI221219.1.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316276.1, AK302533.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..960
                     /product="E3 ubiquitin-protein ligase CBL-B isoform d"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=106963
     Region          63..189
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          193..276
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          270..366
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(288,308,310..313,318,330,332)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(333..336,349..351)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          373..448
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(384..385,388,412,431..434)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(388..390,396..399,418,421..422,425,431..432,434)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          909..949
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(911..912,914..916,918..919,924,928)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..960
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321790.2:14..2896"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 malapgpdah ahlpplielk fqmansmngr npggrggnpr kgrilgiida iqdavgppkq
       61 aaadrrtvek twklmdkvvr lcqnpklqlk nsppyildil pdtyqhlrli lskyddnqkl
      121 aqlseneyfk iyidslmkks krairlfkeg kermyeeqsq drrnltklsl ifshmlaeik
      181 aifpngqfqg dnfritkada aefwrkffgd ktivpwkvfr qclhevhqis sgleamalks
      241 tidltcndyi svfefdiftr lfqpwgsilr nwnflavthp gymafltyde vkarlqkyst
      301 kpgsyifrls ctrlgqwaig yvtgdgnilq tiphnkplfq alidgsregf ylypdgrsyn
      361 pdltglcept phdhikvtqe qyelycemgs tfqlckicae ndkdvkiepc ghlmctsclt
      421 awqesdgqgc pfcrceikgt epiivdpfdp rdegsrccsi idpfgmpmld ldddddrees
      481 lmmnrlanvr kctdrqnspv tspgssplaq rrkpqpdplq iphlslppvp prldliqkgi
      541 vrspcgsptg spksspcmvr kqdkplpapp pplrdppppp perpppippd nrlsrhihhv
      601 esvpsrdppm pleawcprdv fgtnqlvgcr llgegspkpg itassnvngr hsrvgsdpvl
      661 mrkhrrhdlp legakvfsng hlgseeydvp prlsppppvt tllpsikctg planslsekt
      721 rdpveeddde ykipsshpvs lnsqpshchn vkppvrscdn ghcmlngthg pssekksnip
      781 dlsiylkged afdalppslp ppppparhsl iehskppgss srpssgqdlf llpsdpfvdl
      841 asgqvplppa rrlpgenvkt nrtsqdydql pscsdgsqap arppkprprr tapeihhrkp
      901 hgpeaalenv dakiaklmge gyafeevkra leiaqnnvev arsilrefaf pppvsprlnl
//
LOCUS       NP_001304889            1028 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-3' exoribonuclease 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001304889 XP_011527486
VERSION     NP_001304889.1
DBSOURCE    REFSEQ: accession NM_001317960.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Reiss,M., Keegan,J., Aldrich,A., Lyons,S.M. and Flynn,R.L.
  TITLE     The exoribonuclease XRN2 mediates degradation of the long
            non-coding telomeric RNA TERRA
  JOURNAL   FEBS Lett 597 (14), 1818-1836 (2023)
   PUBMED   37191774
  REMARK    GeneRIF: The exoribonuclease XRN2 mediates degradation of the long
            non-coding telomeric RNA TERRA.
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Pieraccioli,M., Caggiano,C., Mignini,L., Zhong,C., Babini,G.,
            Lattanzio,R., Di Stasi,S., Tian,B., Sette,C. and Bielli,P.
  TITLE     The transcriptional terminator XRN2 and the RNA-binding protein
            Sam68 link alternative polyadenylation to cell cycle progression in
            prostate cancer
  JOURNAL   Nat Struct Mol Biol 29 (11), 1101-1112 (2022)
   PUBMED   36344846
  REMARK    GeneRIF: The transcriptional terminator XRN2 and the RNA-binding
            protein Sam68 link alternative polyadenylation to cell cycle
            progression in prostate cancer.
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Dang,T.T., Lerner,M., Saunders,D., Smith,N., Gulej,R., Zalles,M.,
            Towner,R.A. and Morales,J.C.
  TITLE     XRN2 Is Required for Cell Motility and Invasion in Glioblastomas
  JOURNAL   Cells 11 (9), 1481 (2022)
   PUBMED   35563787
  REMARK    GeneRIF: XRN2 Is Required for Cell Motility and Invasion in
            Glioblastomas.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   West,S., Gromak,N. and Proudfoot,N.J.
  TITLE     Human 5' --> 3' exonuclease Xrn2 promotes transcription termination
            at co-transcriptional cleavage sites
  JOURNAL   Nature 432 (7016), 522-525 (2004)
   PUBMED   15565158
  REMARK    GeneRIF: co-transcriptional cleavage acts as a precursor to
            termination by presenting a free RNA 5' end that is recognized by
            the human 5' --> 3' exonuclease Xrn2
REFERENCE   6  (residues 1 to 1028)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   7  (residues 1 to 1028)
  AUTHORS   Lejeune,F., Li,X. and Maquat,L.E.
  TITLE     Nonsense-mediated mRNA decay in mammalian cells involves decapping,
            deadenylating, and exonucleolytic activities
  JOURNAL   Mol Cell 12 (3), 675-687 (2003)
   PUBMED   14527413
REFERENCE   8  (residues 1 to 1028)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 1028)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
REFERENCE   10 (residues 1 to 1028)
  AUTHORS   Zhang,M., Yu,L., Xin,Y., Hu,P., Fu,Q., Yu,C. and Zhao,S.
  TITLE     Cloning and mapping of the XRN2 gene to human chromosome
            20p11.1-p11.2
  JOURNAL   Genomics 59 (2), 252-254 (1999)
   PUBMED   10409438
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC403143.1, AL117332.16,
            AK302846.1 and AF152169.1.
            
            On Dec 17, 2015 this sequence version replaced XP_011527486.1.
            
            Summary: This gene encodes a 5'-3' exonuclease that promotes
            transcription termination at cotranscriptional cleavage sites.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302846.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p11.22"
     Protein         1..1028
                     /product="5'-3' exoribonuclease 2 isoform 1"
                     /EC_number="3.1.13.-"
                     /note="DHP protein; DHM1-like protein"
                     /calculated_mol_wt=116676
     Region          118..865
                     /region_name="XRN1"
                     /note="5'-3' exonuclease [Replication, recombination and
                     repair]; COG5049"
                     /db_xref="CDD:227382"
     CDS             1..1028
                     /gene="XRN2"
                     /coded_by="NM_001317960.1:42..3128"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:22803"
                     /db_xref="HGNC:HGNC:12836"
                     /db_xref="MIM:608851"
ORIGIN      
        1 mgsaacprga lpelapccqp reqsqphtrw dagcgiqhpg geefrtlgga rayrvpnsqe
       61 grssptrffp apegpahcfv sspdrafwvs eevqrlllsn acqpkecngv kipvdaskpn
      121 pndvefdnly ldmngiihpc thpedkpapk nedemmvaif eyidrlfsiv rprrllymai
      181 dgvaprakmn qqrsrrfras kegmeaavek qrvreeilak ggflppeeik erfdsncitp
      241 gtefmdnlak clryyiadrl nndpgwknlt vilsdasapg egehkimdyi rrqraqpnhd
      301 pnthhclcga dadlimlgla thepnftiir eefkpnkpkp cglcnqfghe vkdceglpre
      361 kkgkhdelad slpcaegefi flrlnvlrey lereltmasl pftfdversi ddwvfmcffv
      421 gndflphlps leirenaidr lvniyknvvh ktggyltesg yvnlqrvqmi mlavgeveds
      481 ifkkrkdded sfrrrqkekr krmkrdqpaf tpsgiltpha lgsrnspgsq vasnprqaay
      541 emrmqnnssp sispntsfts dgspsplggi krkaedsdse pepednvrlw eagwkqryyk
      601 nkfdvdaade kfrrkvvqsy veglcwvlry yyqgcaswkw yypfhyapfa sdfegiadmp
      661 sdfekgtkpf kpleqlmgvf paasgnflpp swrklmsdpd ssiidfyped faidlngkky
      721 awqgvallpf vderrlraal eevypdltpe etrrnslggd vlfvgkhhpl hdfilelyqt
      781 gstepvevpp elchgiqgkf sldeeailpd qivcspvpml rdltqntvvs infkdpqfae
      841 dyifkavmlp garkpaavlk psdwekssng rqwkpqlgfn rdrrpvhldq aafrtlghvm
      901 prgsgtgiys naapppvtyq gnlyrpllrg qaqipklmsn mrpqdswrgp pplfqqqrfd
      961 rgvgaepllp wnrmlqtqna afqpnqyqml agpggypprr ddrggrqgyp regrkyplpp
     1021 psgrynwn
//
LOCUS       NP_073747                532 aa            linear   PRI 20-NOV-2025
DEFINITION  5' exonuclease Apollo isoform a [Homo sapiens].
ACCESSION   NP_073747
VERSION     NP_073747.1
DBSOURCE    REFSEQ: accession NM_022836.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 532)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 532)
  AUTHORS   Sonmez,C., Toia,B., Eickhoff,P., Matei,A.M., El Beyrouthy,M.,
            Wallner,B., Douglas,M.E., de Lange,T. and Lottersberger,F.
  TITLE     DNA-PK controls Apollo's access to leading-end telomeres
  JOURNAL   Nucleic Acids Res 52 (8), 4313-4327 (2024)
   PUBMED   38407308
  REMARK    GeneRIF: DNA-PK controls Apollo's access to leading-end telomeres.
REFERENCE   3  (residues 1 to 532)
  AUTHORS   Bories,C., Lejour,T., Adolphe,F., Kermasson,L., Couve,S.,
            Tanguy,L., Luszczewska,G., Watzky,M., Poillerat,V., Garnier,P.,
            Groisman,R., Ferlicot,S., Richard,S., Saparbaev,M., Revy,P., Gad,S.
            and Renaud,F.
  TITLE     DCLRE1B/Apollo germline mutations associated with renal cell
            carcinoma impair telomere protection
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167107 (2024)
   PUBMED   38430974
  REMARK    GeneRIF: DCLRE1B/Apollo germline mutations associated with renal
            cell carcinoma impair telomere protection.
REFERENCE   4  (residues 1 to 532)
  AUTHORS   Li,L., Wang,F., Deng,Z., Zhang,G., Zhu,L., Zhao,Z. and Liu,R.
  TITLE     DCLRE1B promotes tumor progression and predicts immunotherapy
            response through METTL3-mediated m6A modification in pancreatic
            cancer
  JOURNAL   BMC Cancer 23 (1), 1073 (2023)
   PUBMED   37936074
  REMARK    GeneRIF: DCLRE1B promotes tumor progression and predicts
            immunotherapy response through METTL3-mediated m6A modification in
            pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 532)
  AUTHORS   Yosaatmadja,Y., Baddock,H.T., Newman,J.A., Bielinski,M.,
            Gavard,A.E., Mukhopadhyay,S.M.M., Dannerfjord,A.A., Schofield,C.J.,
            McHugh,P.J. and Gileadi,O.
  TITLE     Structural and mechanistic insights into the Artemis endonuclease
            and strategies for its inhibition
  JOURNAL   Nucleic Acids Res 49 (16), 9310-9326 (2021)
   PUBMED   34387696
  REMARK    GeneRIF: Structural and mechanistic insights into the Artemis
            endonuclease and strategies for its inhibition.
REFERENCE   6  (residues 1 to 532)
  AUTHORS   Lenain,C., Bauwens,S., Amiard,S., Brunori,M., Giraud-Panis,M.J. and
            Gilson,E.
  TITLE     The Apollo 5' exonuclease functions together with TRF2 to protect
            telomeres from DNA repair
  JOURNAL   Curr Biol 16 (13), 1303-1310 (2006)
   PUBMED   16730175
  REMARK    GeneRIF: SNM1B (Apollo) protein exhibits a 5'-to-3' DNA exonuclease
            activity and functions together with TRF2 to protect telomeres from
            damage and fusion.
REFERENCE   7  (residues 1 to 532)
  AUTHORS   Freibaum,B.D. and Counter,C.M.
  TITLE     hSnm1B is a novel telomere-associated protein
  JOURNAL   J Biol Chem 281 (22), 15033-15036 (2006)
   PUBMED   16606622
  REMARK    GeneRIF: the C terminus of Snm1B was shown to interact with the TRF
            homology domain of TRF2 indicating that Snm1B is likely recruited
            to the telomere via interaction with the double-stranded
            telomere-binding protein TRF2
REFERENCE   8  (residues 1 to 532)
  AUTHORS   Ishiai,M., Kimura,M., Namikoshi,K., Yamazoe,M., Yamamoto,K.,
            Arakawa,H., Agematsu,K., Matsushita,N., Takeda,S., Buerstedde,J.M.
            and Takata,M.
  TITLE     DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
            focus formation
  JOURNAL   Mol Cell Biol 24 (24), 10733-10741 (2004)
   PUBMED   15572677
REFERENCE   9  (residues 1 to 532)
  AUTHORS   Demuth,I., Digweed,M. and Concannon,P.
  TITLE     Human SNM1B is required for normal cellular response to both DNA
            interstrand crosslink-inducing agents and ionizing radiation
  JOURNAL   Oncogene 23 (53), 8611-8618 (2004)
   PUBMED   15467758
  REMARK    GeneRIF: siRNA knockdown of hSNM1B rendered cells sensitive to
            ionizing radiation, suggesting the possibility of hSNM1B
            involvement in homologous recombination repair of double-strand
            breaks arising as intermediates of ICL repair
REFERENCE   10 (residues 1 to 532)
  AUTHORS   Dronkert,M.L., de Wit,J., Boeve,M., Vasconcelos,M.L., van Steeg,H.,
            Tan,T.L., Hoeijmakers,J.H. and Kanaar,R.
  TITLE     Disruption of mouse SNM1 causes increased sensitivity to the DNA
            interstrand cross-linking agent mitomycin C
  JOURNAL   Mol Cell Biol 20 (13), 4553-4561 (2000)
   PUBMED   10848582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR005221.1, BC029687.1 and
            AI669133.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: DNA interstrand cross-links prevent strand separation,
            thereby physically blocking transcription, replication, and
            segregation of DNA. DCLRE1B is one of several evolutionarily
            conserved genes involved in repair of interstrand cross-links
            (Dronkert et al., 2000 [PubMed 10848582]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.162258.1,
                                           SRR1803614.276786.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650450.2/ ENSP00000498042.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..532
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..532
                     /product="5' exonuclease Apollo isoform a"
                     /EC_number="3.5.2.6"
                     /note="DNA cross-link repair 1B (PSO2 homolog, S.
                     cerevisiae); 5' exonuclease Apollo; SNM1 homolog B;
                     beta-lactamase DCLRE1B"
                     /calculated_mol_wt=59871
     Region          6..151
                     /region_name="SNM1A-1C-like_MBL-fold"
                     /note="SNM1A, artemis/SNM1C, yeast Pso2p, and related
                     proteins; MBL-fold metallo-hydrolase domain; cd16273"
                     /db_xref="CDD:293831"
     Site            order(31,33,35..36,99..100,120,145)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293831"
     Region          216..299
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     Region          350..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Region          453..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Region          496..529
                     /region_name="apollo_TRF2_binding"
                     /note="TRF2-binding region of apollo and similar proteins;
                     cd11662"
                     /db_xref="CDD:212560"
     Region          496..511
                     /region_name="TBM"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H816.1)"
     Site            order(498,500..510)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212560"
     CDS             1..532
                     /gene="DCLRE1B"
                     /gene_synonym="APOLLO; DKCB8; SNM1B; SNMIB"
                     /coded_by="NM_022836.4:262..1860"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS866.1"
                     /db_xref="GeneID:64858"
                     /db_xref="HGNC:HGNC:17641"
                     /db_xref="MIM:609683"
ORIGIN      
        1 mngvliphtp iavdfwslrr agtarlffls hmhsdhtvgl sstwarplyc spitahllhr
       61 hlqvskqwiq alevgeshvl pldeigqetm tvtlldanhc pgsvmflfeg yfgtilytgd
      121 frytpsmlke paltlgkqih tlyldntncn palvlpsrqe aahqivqlir khpqhnikig
      181 lyslgkesll eqlalefqtw vvlsprrlel vqllgladvf tveekagrih avdhmeichs
      241 nmlrwnqthp tiailptsrk ihsshpdihv ipysdhssys elrafvaalk pcqvvpivsr
      301 rpcggfqdsl sprisvplip dsvqqymsss srkpsllwll errlkrprtq gvvfespees
      361 adqsqadrds kkakkeklsp wpadlekqps hhplrikkql fpdlyskewn kavpfcesqk
      421 rvtmltaplg fsvhlrstde efisqktree iglgsplvpm gdddggpeat gnqsawmghg
      481 splshsskgt pllatefrgl alkylltpvn ffqagyssrr fdqqvekyhk pc
//
LOCUS       NP_001036817             247 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.7cy [Homo sapiens].
ACCESSION   NP_001036817
VERSION     NP_001036817.1
DBSOURCE    REFSEQ: accession NM_001043352.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 247)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 247)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 247)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 247)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 247)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 247)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 247)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 247)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 247)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 247)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 247)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 247)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 247)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA472065.1, AY004867.1,
            BM674269.1, AK123113.1, AL590431.11 and AA863064.1.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (Tpm3.7, also known as variant 3)
            uses an alternate splice site in the 3' coding region, compared to
            variant Tpm3.1. The encoded isoform (Tpm3.7cy, also known as
            isoform 3, Tm5NM7, or TC22), is shorter and has a distinct
            C-terminus, compared to isoform Tpm3.1cy.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.110647.1,
                                           SRR7410570.110640.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..247
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..247
                     /product="tropomyosin alpha-3 chain isoform Tpm3.7cy"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=28824
     Region          12..245
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..247
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001043352.2:100..843"
                     /note="isoform Tpm3.7cy is encoded by transcript variant
                     Tpm3.7"
                     /db_xref="CCDS:CCDS41402.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 magittieav krkiqvlqqq addaeeraer lqrevegerr areqaeaeva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienralk deekmelqei qlkeakhiae
      121 eadrkyeeva rklviiegdl erteeraela esrcremdeq irlmdqnlkc lsaaeekysq
      181 kedkyeeeik iltdklkeae traefaersv aklektiddl eerlysqler nrllsnelkl
      241 tlhdlcd
//
LOCUS       NP_570122                372 aa            linear   PRI 20-NOV-2025
DEFINITION  inositol polyphosphate 5-phosphatase K isoform 2 [Homo sapiens].
ACCESSION   NP_570122
VERSION     NP_570122.1
DBSOURCE    REFSEQ: accession NM_130766.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Moes,B., Li,H., Molina-Ortiz,P., Radermecker,C., Rosu,A., Vande
            Catsyne,C.A., Sayyed,S.A., Fontela,J., Duque,M., Mostafa,A.,
            Azzi,A., Barata,J.T., Merino,R., Xu,C., Desmet,C.J. and
            Schurmans,S.
  TITLE     INPP5K controls the dynamic structure and signaling of wild-type
            and mutated, leukemia-associated IL-7 receptors
  JOURNAL   Blood 141 (14), 1708-1717 (2023)
   PUBMED   36599086
  REMARK    GeneRIF: INPP5K controls the dynamic structure and signaling of
            wild-type and mutated, leukemia-associated IL-7 receptors.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Sun,J., Harion,R., Naito,T. and Saheki,Y.
  TITLE     INPP5K and Atlastin-1 maintain the nonuniform distribution of
            ER-plasma membrane contacts in neurons
  JOURNAL   Life Sci Alliance 4 (11), e202101092 (2021)
   PUBMED   34556534
  REMARK    GeneRIF: INPP5K and Atlastin-1 maintain the nonuniform distribution
            of ER-plasma membrane contacts in neurons.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Hathazi,D., Cox,D., D'Amico,A., Tasca,G., Charlton,R.,
            Carlier,R.Y., Baumann,J., Kollipara,L., Zahedi,R.P., Feldmann,I.,
            Deleuze,J.F., Torella,A., Cohn,R., Robinson,E., Ricci,F.,
            Jungbluth,H., Fattori,F., Boland,A., O'Connor,E., Horvath,R.,
            Barresi,R., Lochmuller,H., Urtizberea,A., Jacquemont,M.L.,
            Nelson,I., Swan,L., Bonne,G. and Roos,A.
  TITLE     INPP5K and SIL1 associated pathologies with overlapping clinical
            phenotypes converge through dysregulation of PHGDH
  JOURNAL   Brain 144 (8), 2427-2442 (2021)
   PUBMED   33792664
  REMARK    GeneRIF: INPP5K and SIL1 associated pathologies with overlapping
            clinical phenotypes converge through dysregulation of PHGDH.
            Erratum:[Brain. 2024 Aug 1;147(8):e62. doi: 10.1093/brain/awae239.
            PMID: 39023925]
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Gurung,R., Tan,A., Ooms,L.M., McGrath,M.J., Huysmans,R.D.,
            Munday,A.D., Prescott,M., Whisstock,J.C. and Mitchell,C.A.
  TITLE     Identification of a novel domain in two mammalian
            inositol-polyphosphate 5-phosphatases that mediates membrane ruffle
            localization. The inositol 5-phosphatase skip localizes to the
            endoplasmic reticulum and translocates to membrane ruffles
            following epidermal growth factor stimulation
  JOURNAL   J Biol Chem 278 (13), 11376-11385 (2003)
   PUBMED   12536145
  REMARK    GeneRIF: identification of novel domain that mediates membrane
            ruffle localization
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Ijuin,T. and Takenawa,T.
  TITLE     SKIP negatively regulates insulin-induced GLUT4 translocation and
            membrane ruffle formation
  JOURNAL   Mol Cell Biol 23 (4), 1209-1220 (2003)
   PUBMED   12556481
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Ijuin,T., Mochizuki,Y., Fukami,K., Funaki,M., Asano,T. and
            Takenawa,T.
  TITLE     Identification and characterization of a novel inositol
            polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 275 (15), 10870-10875 (2000)
   PUBMED   10753883
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Drayer,A.L., Pesesse,X., De Smedt,F., Communi,D., Moreau,C. and
            Erneux,C.
  TITLE     The family of inositol and phosphatidylinositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 1001-1005 (1996)
   PUBMED   8968500
  REMARK    Review article
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Mitchell,C.A., Brown,S., Campbell,J.K., Munday,A.D. and Speed,C.J.
  TITLE     Regulation of second messengers by the inositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 994-1000 (1996)
   PUBMED   8968499
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100748.2, BC004362.1,
            AB036829.1 and BM510617.1.
            
            Summary: This gene encodes a protein with 5-phosphatase activity
            toward polyphosphate inositol. The protein localizes to the cytosol
            in regions lacking actin stress fibers. It is thought that this
            protein may negatively regulate the actin cytoskeleton.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (2) has an additional segment in
            its 5' end, as compared to variant 1. The resulting isoform,
            isoform 2, has a shorter N-terminus, compared to isoform 1.
            Variants 2 and 3 encode the same isoform, isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.211489.1,
                                           SRR1803614.94175.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..372
                     /product="inositol polyphosphate 5-phosphatase K isoform
                     2"
                     /EC_number="3.1.3.56"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="phosphatidylinositol-4,5-bisphosphate
                     5-phosphatase; phosphatidylinositol-3,4,5-trisphosphate
                     5-phosphatase; skeletal muscle and kidney-enriched
                     inositol phosphatase"
                     /calculated_mol_wt=42653
     Region          <1..244
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Site            order(73,118,235)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197306"
     Region          255..355
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     CDS             1..372
                     /gene="INPP5K"
                     /gene_synonym="MDCCAID; PPS; SKIP"
                     /coded_by="NM_130766.3:573..1691"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11005.1"
                     /db_xref="GeneID:51763"
                     /db_xref="HGNC:HGNC:33882"
                     /db_xref="MIM:607875"
ORIGIN      
        1 mdvlsplsfi kvshvrmqgi lllvfakyqh lpyiqilstk stptglfgyw gnkggvnicl
       61 klygyyvsii nchlpphisn nyqrlehfdr ilemqncegr dipnildhdl iiwfgdmnfr
      121 iedfglhfvr esiknrcygg lwekdqlsia kkhdpllref qegrllfppt ykfdrnsndy
      181 dtsekkrkpa wtdrilwrlk rqpcagpdtp ippashfsls lrgysshmty gisdhkpvsg
      241 tfdlelkplv saplivlmpe dlwtvendmm vsysstsdfp sspwdwigly kvglrdvndy
      301 vsyawvgdsk vscsdnlnqv yidisniptt edefllcyys nslrsvvgis rpfqippgsl
      361 redplgeaqp qi
//
LOCUS       NP_001352222             937 aa            linear   PRI 20-NOV-2025
DEFINITION  VPS35 endosomal protein-sorting factor-like isoform 3 [Homo
            sapiens].
ACCESSION   NP_001352222 XP_005255492
VERSION     NP_001352222.1
DBSOURCE    REFSEQ: accession NM_001365293.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 937)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 937)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 937)
  AUTHORS   Otsuji,S., Nishio,Y., Tsujita,M., Rio,M., Huber,C.,
            Anton-Plagaro,C., Mizuno,S., Kawano,Y., Miyatake,S., Simon,M., van
            Binsbergen,E., van Jaarsveld,R.H., Matsumoto,N., Cormier-Daire,V.,
            J Cullen,P., Saitoh,S. and Kato,K.
  TITLE     Clinical diversity and molecular mechanism of VPS35L-associated
            Ritscher-Schinzel syndrome
  JOURNAL   J Med Genet 60 (4), 359-367 (2023)
   PUBMED   36113987
  REMARK    GeneRIF: Clinical diversity and molecular mechanism of
            VPS35L-associated Ritscher-Schinzel syndrome.
REFERENCE   4  (residues 1 to 937)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 937)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 937)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 937)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 937)
  AUTHORS   Naukkarinen,J., Surakka,I., Pietilainen,K.H., Rissanen,A.,
            Salomaa,V., Ripatti,S., Yki-Jarvinen,H., van Duijn,C.M.,
            Wichmann,H.E., Kaprio,J., Taskinen,M.R. and Peltonen,L.
  CONSRTM   ENGAGE Consortium
  TITLE     Use of genome-wide expression data to mine the 'Gray Zone' of GWA
            studies leads to novel candidate obesity genes
  JOURNAL   PLoS Genet 6 (6), e1000976 (2010)
   PUBMED   20532202
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 937)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 937)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012621.8 and AC002550.1.
            
            On Aug 15, 2018 this sequence version replaced XP_005255492.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.259858.1,
                                           SRR1803615.264101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..937
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..937
                     /product="VPS35 endosomal protein-sorting factor-like
                     isoform 3"
                     /note="esophageal cancer associated protein; UPF0505
                     protein C16orf62"
                     /calculated_mol_wt=106462
     CDS             1..937
                     /gene="VPS35L"
                     /gene_synonym="C16orf62; EC97; RTSC3"
                     /coded_by="NM_001365293.2:28..2841"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:57020"
                     /db_xref="HGNC:HGNC:24641"
                     /db_xref="MIM:618981"
ORIGIN      
        1 mavfpwhsrn rnykaefasc rleavplefg dyhplkpitv tesktkkvnr kgstsstsss
       61 ssssvvdpls svldgtdpls mfaatadpaa laaamdssrr krdrddnsvv gsdfepwtnk
      121 rgeilarytt teklsinlfm gsekgkagta tlamsekvrt rleelddfee gsqkellnlt
      181 qqdyvnriee lnqslkdawa sdqkvkalki viqcskllsd tsviqfypsk fvlitdildt
      241 fgklvyerif smcvdsrsvl pdhfspenan dtaketclnw ffkiasirel iprfyveasi
      301 lkcnkflskt giseclprlt cmirgigdpl vsvyaraylc rvgmevaphl ketlnknffd
      361 flltfkqihg dtvqnqlvvq gvelpsylpl yppamdwifq cisyhapeal ltemmerckk
      421 lgnnalllns vmsafraefi atrsmdfigm ikecdesgfp khllfrslgl nlaladppes
      481 drlqilneaw kvitklknpq dyincaevwv eytckhftkr evntvladvi khmtpdrafe
      541 dsypqlqlii kkviahfhdf svlfsvekfl pfldmfqkes vrvevckcim dafikhqqep
      601 tkdpvilnal lhvcktmhds vnaltledek rmlsylingf ikmvsfgrdf eqqlsfyves
      661 rsmfcnlepv lvqlihacva ycfitipsla giftrlnlyl hsgqvalanq clsqadaffk
      721 aaislvpevp kminidgkmr psesfllefl cnffstlliv pdhpehgvlf lvrellnviq
      781 dytwednsde kiriytcvlh llsamsqety lyhidkvdsn dslyggdskf laennklcet
      841 vmaqilehlk tlakdealkr qsslglsffn silahgdlrn nklnqlsvnl whlaqrhgca
      901 dtrtmvktle yikkqskqpd mthltelalr lplqtrt
//
LOCUS       NP_002378                829 aa            linear   PRI 20-NOV-2025
DEFINITION  colorectal mutant cancer protein isoform 2 [Homo sapiens].
ACCESSION   NP_002378
VERSION     NP_002378.2
DBSOURCE    REFSEQ: accession NM_002387.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 829)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 829)
  AUTHORS   Xiao,N., Cao,X., Liu,Z. and Han,Y.
  TITLE     Two germline mutations can serve as genetic susceptibility
            screening makers for a lung adenocarcinoma family
  JOURNAL   J Cancer Res Clin Oncol 149 (9), 6541-6548 (2023)
   PUBMED   36781503
  REMARK    GeneRIF: Two germline mutations can serve as genetic susceptibility
            screening makers for a lung adenocarcinoma family.
REFERENCE   3  (residues 1 to 829)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 829)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 829)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 829)
  AUTHORS   Curtis,L.J., Bubb,V.J., Gledhill,S., Morris,R.G., Bird,C.C. and
            Wyllie,A.H.
  TITLE     Loss of heterozygosity of MCC is not associated with mutation of
            the retained allele in sporadic colorectal cancer
  JOURNAL   Hum Mol Genet 3 (3), 443-446 (1994)
   PUBMED   8012355
REFERENCE   7  (residues 1 to 829)
  AUTHORS   Lindgren,V., Bryke,C.R., Ozcelik,T., Yang-Feng,T.L. and Francke,U.
  TITLE     Phenotypic, cytogenetic, and molecular studies of three patients
            with constitutional deletions of chromosome 5 in the region of the
            gene for familial adenomatous polyposis
  JOURNAL   Am J Hum Genet 50 (5), 988-997 (1992)
   PUBMED   1315124
  REMARK    Review article
REFERENCE   8  (residues 1 to 829)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   9  (residues 1 to 829)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Vogelstein,B., Bryan,T.M., Levy,D.B.,
            Smith,K.J., Preisinger,A.C., Hamilton,S.R., Hedge,P., Markham,A. et
            al.
  TITLE     Identification of a gene located at chromosome 5q21 that is mutated
            in colorectal cancers
  JOURNAL   Science 251 (4999), 1366-1370 (1991)
   PUBMED   1848370
REFERENCE   10 (residues 1 to 829)
  AUTHORS   Hoshino,Y., Horikawa,I., Oshimura,M. and Yuasa,Y.
  TITLE     Normal human chromosome 5, on which a familial adenomatous
            polyposis gene is located, has tumor suppressive activity
  JOURNAL   Biochem Biophys Res Commun 174 (1), 298-304 (1991)
   PUBMED   1846539
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC126917.1, AC106750.3 and
            AC008536.7.
            
            On May 31, 2019 this sequence version replaced NP_002378.1.
            
            Summary: This gene is a candidate colorectal tumor suppressor gene
            that is thought to negatively regulate cell cycle progression. The
            orthologous gene in the mouse expresses a phosphoprotein associated
            with the plasma membrane and membrane organelles, and
            overexpression of the mouse protein inhibits entry into S phase.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) has a distinct 5' UTR and 5'
            coding region, compared to variant 1. The resulting isoform (2) has
            a shorter and distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.94966.1,
                                           SRR1803615.235511.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..829
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..829
                     /product="colorectal mutant cancer protein isoform 2"
                     /note="mutated in colorectal cancers; MCC, WNT signaling
                     pathway regulator"
                     /calculated_mol_wt=92897
     Region          <14..>266
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          114..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23508.2)"
     Region          282..320
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23508.2)"
     Region          402..465
                     /region_name="MCC-bdg_PDZ"
                     /note="PDZ domain of MCC-2 bdg protein for Usher syndrome;
                     pfam10506"
                     /db_xref="CDD:463122"
     Region          <609..>821
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          672..700
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23508.2)"
     Region          732..798
                     /region_name="MCC-bdg_PDZ"
                     /note="PDZ domain of MCC-2 bdg protein for Usher syndrome;
                     pfam10506"
                     /db_xref="CDD:463122"
     Region          766..782
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:24824780"
                     /note="propagated from UniProtKB/Swiss-Prot (P23508.2)"
     Region          826..829
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P23508.2)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22480440; propagated from
                     UniProtKB/Swiss-Prot (P23508.2)"
     CDS             1..829
                     /gene="MCC"
                     /gene_synonym="MCC1"
                     /coded_by="NM_002387.3:554..3043"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4111.1"
                     /db_xref="GeneID:4163"
                     /db_xref="HGNC:HGNC:6935"
                     /db_xref="MIM:159350"
ORIGIN      
        1 mnsgvamkyg ndssaelsel hsaalaslkg divelnkrlq qtererdlle kklakaqceq
       61 shlmrehedv qerttlryee ritelhsvia elnkkidrlq gttireedey selrselsqs
      121 qhevnedsrs mdqdqtsvsi penqstmvta dmdncsdlns elqrvltgle nvvcgrkkss
      181 cslsvaevdk hieqlttase hcdlaiktve eiegvlgrdl ypnlaeersr wekelaglre
      241 enesltamlc skeeelnrtk atmnaireer drlrrrvrel qtrlqsvqat gpsspgrlts
      301 tnrpinpstg elstssssnd ipiakiaerv klsktrsess ssdrpvlgse issigvsssv
      361 aehlahslqd csniqeifqt lyshgsaise skirefevet erlnsriehl ksqndlltit
      421 leecksnaer msmlvgkyes natalrlalq yseqcieaye lllalaeseq slilgqfraa
      481 gvgsspgdqs gdenitqmlk rahdcrktae naakallmkl dgscggafav agcsvqpwes
      541 lssnshtstt sstasscdte ftkedeqrlk dyiqqlkndr aavkltmlel esihidplsy
      601 dvkprgdsqr ldlenavlmq elmamkeema elkaqlylle kekkalelkl streaqeqay
      661 lvhiehlkse veeqkeqrmr slsstssgsk dkpgkecada aspalslael rttcsenela
      721 aeftnairre kklkarvqel vsalerltks seirhqqsae fvndlkrans nlvaayekak
      781 kkhqnklkkl esqmmamver hetqvrmlkq rialleeens rphtnetsl
//
LOCUS       NP_001608                726 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-adducin isoform a [Homo sapiens].
ACCESSION   NP_001608
VERSION     NP_001608.1
DBSOURCE    REFSEQ: accession NM_001617.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 726)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 726)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 726)
  AUTHORS   Yang,C., Sui,Z., Xu,T., Liu,W., Wang,X. and Zeng,X.
  TITLE     Lipid raft-associated beta-adducin participates in neutrophil
            migration
  JOURNAL   Mol Med Rep 18 (2), 1353-1360 (2018)
   PUBMED   29901076
  REMARK    GeneRIF: betaadducin was demonstrated to have a critical role in
            neutrophil migration.
REFERENCE   4  (residues 1 to 726)
  AUTHORS   Kiang,K.M. and Leung,G.K.
  TITLE     A Review on Adducin from Functional to Pathological Mechanisms:
            Future Direction in Cancer
  JOURNAL   Biomed Res Int 2018, 3465929 (2018)
   PUBMED   29862265
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 726)
  AUTHORS   Citterio,L., Tizzoni,L., Catalano,M., Zerbini,G., Bianchi,G. and
            Barlassina,C.
  TITLE     Expression analysis of the human adducin gene family and evidence
            of ADD2 beta4 multiple splicing variants
  JOURNAL   Biochem Biophys Res Commun 309 (2), 359-367 (2003)
   PUBMED   12951058
REFERENCE   6  (residues 1 to 726)
  AUTHORS   Hughes,C.A. and Bennett,V.
  TITLE     Adducin: a physical model with implications for function in
            assembly of spectrin-actin complexes
  JOURNAL   J Biol Chem 270 (32), 18990-18996 (1995)
   PUBMED   7642559
REFERENCE   7  (residues 1 to 726)
  AUTHORS   Gilligan,D.M., Lieman,J. and Bennett,V.
  TITLE     Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in
            situ hybridization
  JOURNAL   Genomics 28 (3), 610-612 (1995)
   PUBMED   7490111
REFERENCE   8  (residues 1 to 726)
  AUTHORS   Miyazaki,M., Kaibuchi,K., Shirataki,H., Kohno,H., Ueyama,T.,
            Nishikawa,J. and Takai,Y.
  TITLE     Rabphilin-3A binds to a M(r) 115,000 polypeptide in a
            phosphatidylserine- and Ca(2+)-dependent manner
  JOURNAL   Brain Res Mol Brain Res 28 (1), 29-36 (1995)
   PUBMED   7707875
REFERENCE   9  (residues 1 to 726)
  AUTHORS   Joshi,R., Gilligan,D.M., Otto,E., McLaughlin,T. and Bennett,V.
  TITLE     Primary structure and domain organization of human alpha and beta
            adducin
  JOURNAL   J Cell Biol 115 (3), 665-675 (1991)
   PUBMED   1840603
REFERENCE   10 (residues 1 to 726)
  AUTHORS   Mische,S.M., Mooseker,M.S. and Morrow,J.S.
  TITLE     Erythrocyte adducin: a calmodulin-regulated actin-bundling protein
            that stimulates spectrin-actin binding
  JOURNAL   J Cell Biol 105 (6 Pt 1), 2837-2845 (1987)
   PUBMED   3693401
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA501584.1, BC010237.1,
            BC065525.1, N53078.1 and AC005234.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Adducins are heteromeric proteins composed of different
            subunits referred to as adducin alpha, beta and gamma. The three
            subunits are encoded by distinct genes and belong to a family of
            membrane skeletal proteins involved in the assembly of
            spectrin-actin network in erythrocytes and at sites of cell-cell
            contact in epithelial tissues. While adducins alpha and gamma are
            ubiquitously expressed, the expression of adducin beta is
            restricted to brain and hematopoietic tissues. Adducin, originally
            purified from human erythrocytes, was found to be a heterodimer of
            adducins alpha and beta. Polymorphisms resulting in amino acid
            substitutions in these two subunits have been associated with the
            regulation of blood pressure in an animal model of hypertension.
            Heterodimers consisting of alpha and gamma subunits have also been
            described. Structurally, each subunit is comprised of two distinct
            domains. The amino-terminal region is protease resistant and
            globular in shape, while the carboxy-terminal region is protease
            sensitive. The latter contains multiple phosphorylation sites for
            protein kinase C, the binding site for calmodulin, and is required
            for association with spectrin and actin. Alternatively spliced
            transcript variants have been described. [provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Both variants 1 and 5 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.108685.1,
                                           SRR1803613.254150.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264436.9/ ENSP00000264436.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..726
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..726
                     /product="beta-adducin isoform a"
                     /note="erythrocyte adducin subunit beta; adducin 2 (beta)"
                     /calculated_mol_wt=80723
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35612.3)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05764; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:8810272; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Region          130..379
                     /region_name="Aldolase_II"
                     /note="Class II Aldolase and Adducin head (N-terminal)
                     domain. Aldolases are ubiquitous enzymes catalyzing
                     central steps of carbohydrate metabolism. Based on
                     enzymatic mechanisms, this superfamily has been divided
                     into two distinct classes (Class I and II); cl00214"
                     /db_xref="CDD:469663"
     Site            order(139,143,155,176,178..179,229,231..232,237..239,247,
                     249..250,261,289,300,307,311,318,336)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:238232"
     Site            order(160,173..174,199..201,227,229,290)
                     /site_type="active"
                     /db_xref="CDD:238232"
     Site            order(227,229,290)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:238232"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Region          425..444
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35612.3)"
     Region          <509..647
                     /region_name="LGT"
                     /note="Prolipoprotein diacylglyceryl transferase; cl00478"
                     /db_xref="CDD:469786"
     Region          525..726
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35612.3)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P35612.3)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q05764; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            699
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            701
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYB8; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000269|PubMed:8810272; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     Region          704..721
                     /region_name="Interaction with calmodulin.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35612.3)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKC.
                     /evidence=ECO:0000269|PubMed:8810272; propagated from
                     UniProtKB/Swiss-Prot (P35612.3)"
     CDS             1..726
                     /gene="ADD2"
                     /gene_synonym="ADDB"
                     /coded_by="NM_001617.4:469..2649"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1906.1"
                     /db_xref="GeneID:119"
                     /db_xref="HGNC:HGNC:244"
                     /db_xref="MIM:102681"
ORIGIN      
        1 mseetvpeaa sppppqgqpy fdrfseddpe ymrlrnraad lrqdfnlmeq kkrvtmilqs
       61 psfreelegl iqeqmkkgnn ssniwalrqi adfmastsha vfptssmnvs mmtpindlht
      121 adslnlakge rlmrckissv yrlldlygwa qlsdtyvtlr vskeqdhfli spkgvscsev
      181 tasslikvni lgevvekgss cfpvdttgfc lhsaiyaarp dvrciihlht pataavsamk
      241 wgllpvshna llvgdmayyd fngemeqead rinlqkclgp tckilvlrnh gvvalgdtve
      301 eafykifhlq aaceiqvsal ssaggvenli lleqekhrph evgsvqwags tfgpmqksrl
      361 gehefealmr mldnlgyrtg ytyrhpfvqe ktkhksevei patvtafvfe edgapvpalr
      421 qhaqkqqkek trwlntpnty lrvnvadevq rsmgsprpkt twmkadevek sssgmpirie
      481 npnqfvplyt dpqevlemrn kireqnrqdv ksagpqsqll asviaeksrs pstesqlmsk
      541 gdedtkddse etvpnpfsql tdqeleeykk everkkleld geketapeep gspaksapas
      601 pvqspakeae tksplvspsk sleegtkkte tskaattepe ttqpegvvvn greeeqtaee
      661 ilskglsqmt tsadtdvdts kdktesvtsg pmspegspsk spskkkkkfr tpsflkkskk
      721 kekves
//
LOCUS       NP_001265118             248 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform Tpm3.5cy [Homo sapiens].
ACCESSION   NP_001265118
VERSION     NP_001265118.1
DBSOURCE    REFSEQ: accession NM_001278189.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 248)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 248)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 248)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 248)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA472065.1, AF474157.1,
            AL590431.11 and AA863064.1.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (Tpm3.5, also known as variant 7)
            contains an alternate exon in the 3' coding region, which results
            in a frameshift, compared to variant Tpm3.1. The encoded isoform
            (Tpm3.5cy, also known as isoform 7 or Tm5NM5) is the same length as
            isoform Tpm3.1cy but has a distinct C-terminus.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.13306.1,
                                           SRR1660809.40057.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..248
                     /product="tropomyosin alpha-3 chain isoform Tpm3.5cy"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=28791
     Region          12..246
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..248
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001278189.2:100..846"
                     /note="isoform Tpm3.5cy is encoded by transcript variant
                     Tpm3.5"
                     /db_xref="CCDS:CCDS60275.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 magittieav krkiqvlqqq addaeeraer lqrevegerr areqaeaeva slnrriqlve
       61 eeldraqerl atalqkleea ekaadeserg mkvienralk deekmelqei qlkeakhiae
      121 eadrkyeeva rklviiegdl erteeraela esrcremdeq irlmdqnlkc lsaaeekysq
      181 kedkyeeeik iltdklkeae traefaersv aklektiddl edelyaqklk ykaiseeldh
      241 alndmtsi
//
LOCUS       NP_872307                381 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription termination factor 4, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_872307
VERSION     NP_872307.2
DBSOURCE    REFSEQ: accession NM_182501.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Chandrasekaran,V., Desai,N., Burton,N.O., Yang,H., Price,J.,
            Miska,E.A. and Ramakrishnan,V.
  TITLE     Visualizing formation of the active site in the mitochondrial
            ribosome
  JOURNAL   Elife 10, e68806 (2021)
   PUBMED   34609277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Hillen,H.S., Lavdovskaia,E., Nadler,F., Hanitsch,E., Linden,A.,
            Bohnsack,K.E., Urlaub,H. and Richter-Dennerlein,R.
  TITLE     Structural basis of GTPase-mediated mitochondrial ribosome
            biogenesis and recycling
  JOURNAL   Nat Commun 12 (1), 3672 (2021)
   PUBMED   34135319
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Cipullo,M., Gese,G.V., Khawaja,A., Hallberg,B.M. and Rorbach,J.
  TITLE     Structural basis for late maturation steps of the human
            mitoribosomal large subunit
  JOURNAL   Nat Commun 12 (1), 3673 (2021)
   PUBMED   34135318
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Wang,X.L., Liu,Q., Chen,G.J., Li,M.L. and Ding,Y.H.
  TITLE     Overexpression of MTERF4 promotes the amyloidogenic processing of
            APP by inhibiting ADAM10
  JOURNAL   Biochem Biophys Res Commun 482 (4), 928-934 (2017)
   PUBMED   27894840
  REMARK    GeneRIF: The overexpression of MTERF4 induced a significant
            increase in the levels of APP protein and secreted Abeta 42 in
            HEK293-APPswe cells compared with control cells these results
            suggest that MTERF4 promotes the amyloidogenic processing of APP by
            inhibiting ADAM10 in HEK293-APPswe cells; therefore, MTERF4 may
            play an important role in the pathogenesis of Alzheimer's disease.
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Yakubovskaya,E., Guja,K.E., Mejia,E., Castano,S., Hambardjieva,E.,
            Choi,W.S. and Garcia-Diaz,M.
  TITLE     Structure of the essential MTERF4:NSUN4 protein complex reveals how
            an MTERF protein collaborates to facilitate rRNA modification
  JOURNAL   Structure 20 (11), 1940-1947 (2012)
   PUBMED   23022348
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Spahr,H., Habermann,B., Gustafsson,C.M., Larsson,N.G. and
            Hallberg,B.M.
  TITLE     Structure of the human MTERF4-NSUN4 protein complex that regulates
            mitochondrial ribosome biogenesis
  JOURNAL   Proc Natl Acad Sci U S A 109 (38), 15253-15258 (2012)
   PUBMED   22949673
  REMARK    GeneRIF: analysis of the 3D crystal structure of the human
            MTERF4-NSUN4 complex
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Camara,Y., Asin-Cayuela,J., Park,C.B., Metodiev,M.D., Shi,Y.,
            Ruzzenente,B., Kukat,C., Habermann,B., Wibom,R., Hultenby,K.,
            Franz,T., Erdjument-Bromage,H., Tempst,P., Hallberg,B.M.,
            Gustafsson,C.M. and Larsson,N.G.
  TITLE     MTERF4 regulates translation by targeting the methyltransferase
            NSUN4 to the mammalian mitochondrial ribosome
  JOURNAL   Cell Metab 13 (5), 527-539 (2011)
   PUBMED   21531335
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Linder,T., Park,C.B., Asin-Cayuela,J., Pellegrini,M., Larsson,N.G.,
            Falkenberg,M., Samuelsson,T. and Gustafsson,C.M.
  TITLE     A family of putative transcription termination factors shared
            amongst metazoans and plants
  JOURNAL   Curr Genet 48 (4), 265-269 (2005)
   PUBMED   16193327
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA496994.1, BC053533.1, AA907534.1 and BM454834.1.
            
            On Feb 23, 2004 this sequence version replaced NP_872307.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.114955.1,
                                           SRR1660807.125374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000391980.7/
                                                  ENSP00000375840.2
            RefSeq Select criteria             :: based on conservation,
                                                  longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..381
                     /product="transcription termination factor 4,
                     mitochondrial isoform 1"
                     /note="transcription termination factor 4, mitochondrial;
                     MTERF domain-containing protein 2"
                     /calculated_mol_wt=39058
     transit_peptide 1..42
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:21531335; propagated from
                     UniProtKB/Swiss-Prot (Q7Z6M4.3)"
                     /calculated_mol_wt=4918
     mat_peptide     43..381
                     /product="Transcription termination factor 4,
                     mitochondrial. /id=PRO_0000255461"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
                     /calculated_mol_wt=39058
     mat_peptide     48..381
                     /product="mTERF domain-containing protein 2 processed.
                     /id=PRO_0000424341"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
                     /calculated_mol_wt=38584
     Region          <91..302
                     /region_name="mTERF"
                     /note="pfam02536"
                     /db_xref="CDD:460581"
     Region          142..172
                     /region_name="MTERF 1.
                     /evidence=ECO:0000269|PubMed:23022348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          177..204
                     /region_name="MTERF 2.
                     /evidence=ECO:0000269|PubMed:23022348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          209..239
                     /region_name="MTERF 3.
                     /evidence=ECO:0000269|PubMed:23022348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          245..270
                     /region_name="MTERF 4.
                     /evidence=ECO:0000269|PubMed:23022348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          290..318
                     /region_name="MTERF 5.
                     /evidence=ECO:0000269|PubMed:23022348"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          310..327
                     /region_name="Dimerization with NSUN4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     Region          322..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z6M4.3)"
     CDS             1..381
                     /gene="MTERF4"
                     /gene_synonym="MTERFD2"
                     /coded_by="NM_182501.4:15..1160"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2544.1"
                     /db_xref="GeneID:130916"
                     /db_xref="HGNC:HGNC:28785"
                     /db_xref="MIM:615393"
ORIGIN      
        1 maafgrqvld whrlipltwa cmarqtphlg eqrrttasll rklttasngg vieelscvrs
       61 nnyvqepecr rnlvqcllek qgtpvvqgsl elervmssll dmgfsnahin ellsvrrgas
      121 lqqlldiise fillglnpep vcvvlkkspq llklpimqmr krssylqklg lgegklkrvl
      181 yccpeiftmr qqdindtvrl lkekclftvq qvtkilhscp svlredlgql eykfqyayfr
      241 mgikhpdivk seylqysltk ikqrhiyler lgryqtpdkk gqtqipnpll kdilrvseae
      301 flartactsv eefqvfkkll areeeesess tsddkrasld ededdddeed ndeddndedd
      361 ddedddeaed ndededddee e
//
LOCUS       NP_001305818             402 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell surface protein tactile isoform 3 [Homo sapiens].
ACCESSION   NP_001305818
VERSION     NP_001305818.1
DBSOURCE    REFSEQ: accession NM_001318889.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 402)
  AUTHORS   Zhang,Q., Huang,T., Li,X., Liu,G., Xian,L., Mao,X., Lin,T., Fu,C.,
            Chen,X., Liang,W., Zheng,Y., Zhao,Y., Lin,Q., Xu,X., Lin,Y., Bu,J.,
            Wu,C., Zhou,M. and Shen,E.
  TITLE     Prognostic impact of enhanced CD96 expression on NK cells by
            TGF-beta1 in AML
  JOURNAL   Int Immunopharmacol 141, 112958 (2024)
   PUBMED   39159564
  REMARK    GeneRIF: Prognostic impact of enhanced CD96 expression on NK cells
            by TGF-beta1 in AML.
REFERENCE   2  (residues 1 to 402)
  AUTHORS   ElMenshawy,N., El-Chennawi,F., Darwish,A., Foda,A., Atita,D. and
            Eissa,M.
  TITLE     CD44, CD90 and CD96 expression in immune thrombocytopenia purpura
            (ITP) patients
  JOURNAL   J Immunoassay Immunochem 44 (4), 326-337 (2023)
   PUBMED   36949573
  REMARK    GeneRIF: CD44, CD90 and CD96 expression in immune thrombocytopenia
            purpura (ITP) patients.
REFERENCE   3  (residues 1 to 402)
  AUTHORS   Ohtsuki,S., Wang,C., Watanabe,R., Zhang,H., Akiyama,M., Bois,M.C.,
            Maleszewski,J.J., Warrington,K.J., Berry,G.J., Goronzy,J.J. and
            Weyand,C.M.
  TITLE     Deficiency of the CD155-CD96 immune checkpoint controls IL-9
            production in giant cell arteritis
  JOURNAL   Cell Rep Med 4 (4), 101012 (2023)
   PUBMED   37075705
  REMARK    GeneRIF: Deficiency of the CD155-CD96 immune checkpoint controls
            IL-9 production in giant cell arteritis.
REFERENCE   4  (residues 1 to 402)
  AUTHORS   Li,J., Xia,Q., Di,C., Li,C., Si,H., Zhou,B., Yu,S., Li,Y.,
            Huang,J., Lu,Y., Huang,M., Liang,H., Liu,X. and Zhao,Q.
  TITLE     Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and Cancer
            Stemness by Regulating Mitochondrial Fatty Acid beta-Oxidation
  JOURNAL   Adv Sci (Weinh) 10 (7), e2202956 (2023)
   PUBMED   36581470
  REMARK    GeneRIF: Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and
            Cancer Stemness by Regulating Mitochondrial Fatty Acid
            beta-Oxidation.
REFERENCE   5  (residues 1 to 402)
  AUTHORS   Feng,S., Isayev,O., Werner,J. and Bazhin,A.V.
  TITLE     CD96 as a Potential Immune Regulator in Cancers
  JOURNAL   Int J Mol Sci 24 (2), 1303 (2023)
   PUBMED   36674817
  REMARK    GeneRIF: CD96 as a Potential Immune Regulator in Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 402)
  AUTHORS   Hosen,N., Park,C.Y., Tatsumi,N., Oji,Y., Sugiyama,H., Gramatzki,M.,
            Krensky,A.M. and Weissman,I.L.
  TITLE     CD96 is a leukemic stem cell-specific marker in human acute myeloid
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 104 (26), 11008-11013 (2007)
   PUBMED   17576927
  REMARK    GeneRIF: CD96 is a cell surface marker present on many acute
            myeloid leukemia leukemic stem cells
REFERENCE   7  (residues 1 to 402)
  AUTHORS   Fuchs,A., Cella,M., Giurisato,E., Shaw,A.S. and Colonna,M.
  TITLE     Cutting edge: CD96 (tactile) promotes NK cell-target cell adhesion
            by interacting with the poliovirus receptor (CD155)
  JOURNAL   J Immunol 172 (7), 3994-3998 (2004)
   PUBMED   15034010
  REMARK    GeneRIF: CD96 promotes natural killer (NK) cell adhesion to target
            cells expressing the poliovirus receptor (PVR), stimulates
            cytotoxicity of activated NK cells, and mediates acquisition of PVR
            from target cells.
REFERENCE   8  (residues 1 to 402)
  AUTHORS   Gramatzki,M., Ludwig,W.D., Burger,R., Moos,P., Rohwer,P.,
            Grunert,C., Sendler,A., Kalden,J.R., Andreesen,R., Henschke,F. and
            Moldenhauer,G.
  TITLE     Antibodies TC-12 ('unique') and TH-111 (CD96) characterize T-cell
            acute lymphoblastic leukemia and a subgroup of acute myeloid
            leukemia
  JOURNAL   Exp Hematol 26 (13), 1209-1214 (1998)
   PUBMED   9845376
REFERENCE   9  (residues 1 to 402)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 402)
  AUTHORS   Wang,P.L., O'Farrell,S., Clayberger,C. and Krensky,A.M.
  TITLE     Identification and molecular cloning of tactile. A novel human T
            cell activation antigen that is a member of the Ig gene superfamily
  JOURNAL   J Immunol 148 (8), 2600-2608 (1992)
   PUBMED   1313846
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020749.1 and AC055748.21.
            
            Summary: The protein encoded by this gene belongs to the
            immunoglobulin superfamily. It is a type I membrane protein. The
            protein may play a role in the adhesive interactions of activated T
            and NK cells during the late phase of the immune response. It may
            also function in antigen presentation. Alternative splicing
            generates multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) lacks several exons and its 3'
            terminal exon extends past a splice site that is used in variant 1.
            This results in a novel 3' coding region and 3' UTR, compared to
            variant 1. It encodes isoform 3 which is shorter and has a distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020749.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..402
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13-q13.2"
     Protein         1..402
                     /product="T-cell surface protein tactile isoform 3"
                     /note="T-cell surface protein tactile; T cell activation,
                     increased late expression; cell surface antigen CD96; t
                     cell-activated increased late expression protein"
                     /calculated_mol_wt=45490
     Region          27..126
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          101..105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          115..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..402
                     /gene="CD96"
                     /gene_synonym="TACTILE"
                     /coded_by="NM_001318889.2:53..1261"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82817.1"
                     /db_xref="GeneID:10225"
                     /db_xref="HGNC:HGNC:16892"
                     /db_xref="MIM:606037"
ORIGIN      
        1 mekkwkycav yyiiqihfvk gvwektvnte envyatlgsd vnltcqtqtv gffvqmqwsk
       61 vtnkidliav yhpqygfyca ygrpceslvt ftetpengsk wtlhlrnmsc svsgryecml
      121 vlypegiqtk iynlliqthv tadewnsnht ieieinqtle ipcfqnsssk isseftyaws
      181 vedngtqetl isqnhlisns tllkdrvklg tdyrlhlspv qifddgrkfs chirvgpnki
      241 lrssttvkvf akpeipvive nnstdvlver rftcllknvf pkanitwfid gsflhdekeg
      301 iyitneerkg kdgflelksv ltrvhsnkpa qsdnltiwcm alspvpgnkv wnissekitf
      361 llgseisstd pplsvtestl dtqpspassv spasknvftl sy
//
LOCUS       NP_001339980             426 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 9 [Homo sapiens].
ACCESSION   NP_001339980
VERSION     NP_001339980.1
DBSOURCE    REFSEQ: accession NM_001353051.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002558.2.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.169886.1,
                                           SRR14038192.3791955.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..426
                     /product="cell division cycle protein 27 homolog isoform
                     9"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=48461
     Region          101..208
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          103..129
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          163..>333
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          169..197
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(170,173..174,177..178,180,204,207..208,211..212,
                     214..215,238,241..242,245..246,249)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          202..232
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          237..265
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <267..406
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          271..298
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          305..333
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          339..367
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..426
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001353051.2:1119..2399"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mkfppkipnr ktksktnkgg itqpnindsl eitkldssii segkistitp qiqafnlqka
       61 aaglmsllre mgkgylalcs ynckeainil shlpshhynt gwvlcqigra yfelseymqa
      121 erifsevrri enyrvegmei ysttlwhlqk dvalsvlskd ltdmdknspe awcaagncfs
      181 lqrehdiaik ffqraiqvdp nyayaytllg hefvlteeld kalacfrnai rvnprhynaw
      241 yglgmiyykq ekfslaemhf qkaldinpqs svllchigvv qhalkkseka ldtlnkaivi
      301 dpknplckfh rasvlfanek yksalqelee lkqivpkesl vyfligkvyk klgqthlalm
      361 nfswamdldp kgannqikea idkrylpdde epitqeeqim gtdesqessm tdaddtqlha
      421 aesdef
//
LOCUS       NP_001333155             620 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 48 isoform 5 [Homo sapiens].
ACCESSION   NP_001333155
VERSION     NP_001333155.1
DBSOURCE    REFSEQ: accession NM_001346226.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Yu,Z., Tong,L., Ma,C., Song,H., Wang,J., Chai,L., Wang,C., Wang,M.,
            Wang,C., Yan,R., Fu,Y., Jia,M., Zhao,W. and Zhao,C.
  TITLE     The UAF1-USP1 Deubiquitinase Complex Stabilizes cGAS and
            Facilitates Antiviral Responses
  JOURNAL   J Immunol 212 (2), 295-301 (2024)
   PUBMED   38054892
  REMARK    GeneRIF: The UAF1-USP1 Deubiquitinase Complex Stabilizes cGAS and
            Facilitates Antiviral Responses.
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Zarrella,K., Longmire,P., Zeltzer,S., Collins-McMillen,D.,
            Hancock,M., Buehler,J., Reitsma,J.M., Terhune,S.S., Nelson,J.A. and
            Goodrum,F.
  TITLE     Human cytomegalovirus UL138 interaction with USP1 activates STAT1
            in infection
  JOURNAL   PLoS Pathog 19 (6), e1011185 (2023)
   PUBMED   37289831
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Cote-Martin,A., Moody,C., Fradet-Turcotte,A., D'Abramo,C.M.,
            Lehoux,M., Joubert,S., Poirier,G.G., Coulombe,B., Laimins,L.A. and
            Archambault,J.
  TITLE     Human papillomavirus E1 helicase interacts with the WD repeat
            protein p80 to promote maintenance of the viral genome in
            keratinocytes
  JOURNAL   J Virol 82 (3), 1271-1283 (2008)
   PUBMED   18032488
  REMARK    GeneRIF: These findings suggest that the interaction of human
            papillomavirus 11 and 31 E1 proteins with p80 is required for
            efficient maintenance of the viral episome in undifferentiated
            keratinocytes.
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Park,J., Cho,N.H., Choi,J.K., Feng,P., Choe,J. and Jung,J.U.
  TITLE     Distinct roles of cellular Lck and p80 proteins in herpesvirus
            saimiri Tip function on lipid rafts
  JOURNAL   J Virol 77 (16), 9041-9051 (2003)
   PUBMED   12885920
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Park,J., Lee,B.S., Choi,J.K., Means,R.E., Choe,J. and Jung,J.U.
  TITLE     Herpesviral protein targets a cellular WD repeat endosomal protein
            to downregulate T lymphocyte receptor expression
  JOURNAL   Immunity 17 (2), 221-233 (2002)
   PUBMED   12196293
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Nair,J.S., DaFonseca,C.J., Tjernberg,A., Sun,W., Darnell,J.E. Jr.,
            Chait,B.T. and Zhang,J.J.
  TITLE     Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in
            response to IFN-gamma
  JOURNAL   Proc Natl Acad Sci U S A 99 (9), 5971-5976 (2002)
   PUBMED   11972023
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC123903.2 and AC138124.2.
            
            Summary: The protein encoded by this gene has been shown to
            interact with ubiquitin specific peptidase 1 (USP1), activating the
            deubiquitinating activity of USP1 and allowing it to remove the
            ubiquitin moiety from monoubiquitinated FANCD2. FANCD2 is
            ubiquitinated in response to DNA damage. [provided by RefSeq, Sep
            2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.47302.1,
                                           SRR1803616.180849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..620
                     /product="WD repeat-containing protein 48 isoform 5"
                     /note="WD repeat endosomal protein; WD repeat-containing
                     protein 48; USP1 associated factor 1; testicular tissue
                     protein Li 224"
                     /calculated_mol_wt=69434
     Region          17..229
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          22..58
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          63..103
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          115..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          156..192
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          198..233
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          240..267
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..332
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          452..616
                     /region_name="DUF3337"
                     /note="Domain of unknown function (DUF3337); pfam11816"
                     /db_xref="CDD:463358"
     CDS             1..620
                     /gene="WDR48"
                     /gene_synonym="Bun62; P80; SPG60; UAF1"
                     /coded_by="NM_001346226.2:178..2040"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:57599"
                     /db_xref="HGNC:HGNC:30914"
                     /db_xref="MIM:612167"
ORIGIN      
        1 mecqsaqdpy iasmehhtdw vndivlccng ktlisassdt tvkvwnahkg fcmstlrthk
       61 dyvkalayak dkelvasagl drqiflwdvn tltaltasnn tvttsslsgn kdsiyslamn
      121 qlgtiivsgs tekvlrvwdp rtcaklmklk ghtdnvkall lnrdgtqcls gssdgtirlw
      181 slgqqrciat yrvhdegvwa lqvndafthv ysggrdrkiy ctdlrnpdir vliceekapv
      241 lkmeldrsad pppaiwvatt kstvnkwtlk gihnfrasgd ydndctnpit plctqpdqvi
      301 kggasiiqch ilndkrhilt kdtnnnvayw dvlkackved lgkvdfedei kkrfkmvyvp
      361 nwfsvdlktg mltitldesd cfaawvsakd agfsspdgsd pklnlgglll qalleywprt
      421 hvnpmdeeen evnhvngeqe nrvqkgngyf qvpphtpvif geaggrtlfr llcrdsgget
      481 esmllnetvp qwviditvdk nmpkfnkipf ylqphassga ktlkkdrlsa sdmlqvrkvm
      541 ehvyekiinl dnesqttsss nnekpgeqek eediavlaee kiellcqdqv ldpnmdlrtv
      601 khfiwksggd ltlhyrqkst
//
LOCUS       NP_001355795            1285 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-VI isoform 8 [Homo sapiens].
ACCESSION   NP_001355795 XP_005248777
VERSION     NP_001355795.1
DBSOURCE    REFSEQ: accession NM_001368866.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1285)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1285)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1285)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   4  (residues 1 to 1285)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1285)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1285)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 1285)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 1285)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 1285)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 1285)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109897.30, KY781827.1,
            AL136093.8 and AL392166.19.
            
            On Mar 5, 2019 this sequence version replaced XP_005248777.1.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: Isoforms 1 and 8 are the same length but differ
            in sequence.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: KY781827.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2142348, SAMEA2144335 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..1285
                     /product="unconventional myosin-VI isoform 8"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=148473
     Region          71..759
                     /region_name="MYSc_Myo6"
                     /note="class VI myosin, motor domain; cd01382"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107,151..158,195..205,456..461)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276833"
     Site            151..158
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276833"
     Site            195..205
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276833"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          273..317
                     /region_name="Responsible for slow ATPase activity.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            456..461
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276833"
     Site            order(485..496,499..508)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276833"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64331; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          665..672
                     /region_name="Actin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            693..703
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276833"
     Site            705..759
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276833"
     Region          770..917
                     /region_name="CBD_MYO6-like"
                     /note="calmodulin binding domain found in unconventional
                     myosin-VI and similar proteins; cd21759"
                     /db_xref="CDD:409646"
     Region          782..810
                     /region_name="Required for binding calmodulin.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            order(786,789..790,792..810,812..813,816..831,833,
                     836..837,840..841,886)
                     /site_type="other"
                     /note="calmodulin binding site [polypeptide binding]"
                     /db_xref="CDD:409646"
     Site            820..830
                     /site_type="other"
                     /note="IQ motif"
                     /db_xref="CDD:409646"
     Region          835..916
                     /region_name="Three-helix bundle.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          917..984
                     /region_name="SAH. /evidence=ECO:0000269|PubMed:18511944"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          934..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          999..1068
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cd22294"
                     /db_xref="CDD:412090"
     Site            999..1024
                     /site_type="other"
                     /note="MIU motif"
                     /db_xref="CDD:412090"
     Site            1025
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64331; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1082..1122
                     /region_name="MyUb_Myo6"
                     /note="myosin VI ubiquitin-binding domain (MyUb) found in
                     unconventional myosin-VI and similar proteins; cd21958"
                     /db_xref="CDD:439319"
     Site            order(1087..1088,1090..1091,1117..1118,1120..1121)
                     /site_type="other"
                     /note="clathrin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Site            order(1090..1092,1095..1096,1098..1102,1104,1107..1108,
                     1111,1114..1115)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Region          1116..1118
                     /region_name="Interaction with OPTN.
                     /evidence=ECO:0000250|UniProtKB:Q9I8D1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1148..1276
                     /region_name="Interaction with TOM1.
                     /evidence=ECO:0000269|PubMed:31371777"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1168..1258
                     /region_name="Myosin-VI_CBD"
                     /note="Myosin VI cargo binding domain; pfam16521"
                     /db_xref="CDD:465157"
     CDS             1..1285
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_001368866.1:233..4090"
                     /note="isoform 8 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS93949.1"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveanplle afgnaktvrn nnssrfgkfv eihfnekssv vggfvshyll eksricvqgk
      241 eernyhifyr lcagasedir eklhlsspdn frylnrgctr yfanketdkq ilqnrkspey
      301 lkagsmkdpl lddhgdfirm ctamkkigld deekldlfrv vagvlhlgni dfeeagstsg
      361 gcnlknksaq sleycaellg ldqddlrvsl ttrvmlttag gtkgtvikvp lkveqannar
      421 dalaktvysh lfdhvvnrvn qcfpfetssy figvldiagf eyfehnsfeq fcinycnekl
      481 qqffnerilk eeqelyqkeg lgvnevhyvd nqdcidliea klvgildild eenrlpqpsd
      541 qhftsavhqk hkdhfrltip rksklavhrn irddegfiir hfagavcyet tqfveknnda
      601 lhmsleslic esrdkfirel fesstnnnkd tkqkagklsf isvgnkfktq lnllldklrs
      661 tgasfircik pnlkmtshhf egaqilsqlq csgmvsvldl mqggypsras fhelynmykk
      721 ympdklarld prlfckalfk alglnendyk fgltkvffrp gkfaefdqim ksdpdhlael
      781 vkrvnhwltc srwkkvqwcs lsviklknki kyraeacikm qktirmwlck rrhkpridgl
      841 vkvgtlkkrl dkfnevvsvl kdgkpemnkq iknleisidt lmakikstmm tqeqiqkeyd
      901 alvksseell salqkkkqqe eeaerlrriq eemekerkrr eedekrrrke eeerrmklem
      961 eakrkqeeee rkkreddekr iqaeveaqla rqkeeesqqq avleqerrdr elalriaqse
     1021 aelisdeaqa dlalrsldsy pvtskndgtr pkmtpeqmak emseflsrgp avlatkaaag
     1081 tkkydlskwk yaelrdtint scdiellaac reefhrrlkv yhawksknkk rnteteqrap
     1141 ksvtdyaqqn paaqiparqr eiemnrqqrf fripfirpad qykdpqskkk gwwyahfdgp
     1201 wiarqmelhp dkppillvag kddmemceln leetgltrkr gaeilprqfe eiwercggiq
     1261 ylqnaiesrq arptyataml qsllk
//
LOCUS       NP_002804                223 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 9 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002804
VERSION     NP_002804.2
DBSOURCE    REFSEQ: accession NM_002813.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Su,Y., Meng,L., Ge,C., Liu,Y., Zhang,C., Yang,Y., Tian,W. and
            Tian,H.
  TITLE     PSMD9 promotes the malignant progression of hepatocellular
            carcinoma by interacting with c-Cbl to activate EGFR signaling and
            recycling
  JOURNAL   J Exp Clin Cancer Res 43 (1), 142 (2024)
   PUBMED   38745188
  REMARK    GeneRIF: PSMD9 promotes the malignant progression of hepatocellular
            carcinoma by interacting with c-Cbl to activate EGFR signaling and
            recycling.
            Erratum:[J Exp Clin Cancer Res. 2024 Oct 18;43(1):287. doi:
            10.1186/s13046-024-03209-2. PMID: 39420369]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Li,Y., Liu,X., Zhao,F., Zhao,Z., Li,X., Wang,J., Huang,B. and
            Chen,A.
  TITLE     Comprehensive analysis of PSMD family members and validation of
            PSMD9 as a potential therapeutic target in human glioblastoma
  JOURNAL   CNS Neurosci Ther 30 (2), e14366 (2024)
   PUBMED   37485655
  REMARK    GeneRIF: Comprehensive analysis of PSMD family members and
            validation of PSMD9 as a potential therapeutic target in human
            glioblastoma.
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Christie,J., Anthony,C.M., Harish,M., Mudartha,D., Ud Din
            Farooqee,S.B. and Venkatraman,P.
  TITLE     The interaction network of the proteasome assembly chaperone PSMD9
            regulates proteostasis
  JOURNAL   FEBS J 290 (23), 5581-5604 (2023)
   PUBMED   37665644
  REMARK    GeneRIF: The interaction network of the proteasome assembly
            chaperone PSMD9 regulates proteostasis.
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Del Bosque-Plata,L., Amin,M. and Gragnoli,C.
  TITLE     PSMD9 is linked to T2D age of onset, years of isolated and combined
            insulin therapy, irregular menses, and hot flashes
  JOURNAL   Eur Rev Med Pharmacol Sci 26 (23), 8873-8878 (2022)
   PUBMED   36524506
  REMARK    GeneRIF: PSMD9 is linked to T2D age of onset, years of isolated and
            combined insulin therapy, irregular menses, and hot flashes.
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Watanabe,T.K., Saito,A., Suzuki,M., Fujiwara,T., Takahashi,E.,
            Slaughter,C.A., DeMartino,G.N., Hendil,K.B., Chung,C.H.,
            Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and characterization of a human proteasomal modulator
            subunit, p27 (PSMD9)
  JOURNAL   Genomics 50 (2), 241-250 (1998)
   PUBMED   9653651
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   10 (residues 1 to 223)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002383.2, BU726372.1,
            KF459562.1 and AC069503.25.
            
            On Feb 6, 2002 this sequence version replaced NP_002804.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. Three transcript variants
            encoding two different isoforms have been found for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.36874.1, BC004213.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000541212.6/ ENSP00000440485.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..223
                     /product="26S proteasome non-ATPase regulatory subunit 9
                     isoform 1"
                     /note="proteasome 26S non-ATPase regulatory subunit 9;
                     homolog of rat Bridge 1; 26S proteasome regulatory subunit
                     p27; 26S proteasome non-ATPase regulatory subunit 9;
                     proteasome (prosome, macropain) 26S subunit, non-ATPase,
                     9"
                     /calculated_mol_wt=24551
     Region          23..102
                     /region_name="Nas2_N"
                     /note="Nas2 N_terminal domain; pfam18265"
                     /db_xref="CDD:465689"
     Region          103..141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00233.3)"
     Site            129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CR00; propagated from
                     UniProtKB/Swiss-Prot (O00233.3)"
     Region          <137..>215
                     /region_name="RseP"
                     /note="Membrane-associated protease RseP, regulator of
                     RpoE activity [Posttranslational modification, protein
                     turnover, chaperones, Transcription]; COG0750"
                     /db_xref="CDD:440513"
     CDS             1..223
                     /gene="PSMD9"
                     /gene_synonym="p27; Rpn4"
                     /coded_by="NM_002813.7:68..739"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9225.1"
                     /db_xref="GeneID:5715"
                     /db_xref="HGNC:HGNC:9567"
                     /db_xref="MIM:603146"
ORIGIN      
        1 msdeearqsg gssqagvvtv sdvqelmrrk eeieaqikan ydvlesqkgi gmneplvdce
       61 gyprsdvdly qvrtarhnii clqndhkavm kqveealhql hardkekqar dmaeahkeam
      121 srklgqsesq gpprafakvn sispgspasi aglqvddeiv efgsvntqnf qslhnigsvv
      181 qhsegkplnv tvirrgekhq lrlvptrwag kgllgcniip lqr
//
LOCUS       NP_005244                326 aa            linear   PRI 20-NOV-2025
DEFINITION  fos-related antigen 2 [Homo sapiens].
ACCESSION   NP_005244 NP_078806
VERSION     NP_005244.1
DBSOURCE    REFSEQ: accession NM_005253.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Du,H., Sun,J., Wang,X., Zhao,L., Liu,X., Zhang,C., Wang,F. and
            Wu,J.
  TITLE     FOSL2-mediated transcription of ISG20 induces M2 polarization of
            macrophages and enhances tumorigenic ability of glioblastoma cells
  JOURNAL   J Neurooncol 169 (3), 659-670 (2024)
   PUBMED   39073688
  REMARK    GeneRIF: FOSL2-mediated transcription of ISG20 induces M2
            polarization of macrophages and enhances tumorigenic ability of
            glioblastoma cells.
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Rampioni Vinciguerra,G.L., Capece,M., Scafetta,G., Rentsch,S.,
            Vecchione,A., Lovat,F. and Croce,C.M.
  TITLE     Role of Fra-2 in cancer
  JOURNAL   Cell Death Differ 31 (2), 136-149 (2024)
   PUBMED   38104183
  REMARK    GeneRIF: Role of Fra-2 in cancer.
            Review article
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Chen,H., Wang,L., Liu,J., Wan,Z., Zhou,L., Liao,H. and Wan,R.
  TITLE     LncRNA ITGB2-AS1 promotes cisplatin resistance of non-small cell
            lung cancer by inhibiting ferroptosis via activating the
            FOSL2/NAMPT axis
  JOURNAL   Cancer Biol Ther 24 (1), 2223377 (2023)
   PUBMED   37370246
  REMARK    GeneRIF: LncRNA ITGB2-AS1 promotes cisplatin resistance of
            non-small cell lung cancer by inhibiting ferroptosis via activating
            the FOSL2/NAMPT axis.
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Zhang,S., Li,P., Li,J., Gao,J., Qi,Q., Dong,G., Liu,X., Jiao,Q.,
            Wang,Y., Du,L., Zhan,H., Xu,S. and Wang,C.
  TITLE     Chromatin accessibility uncovers KRAS-driven FOSL2 promoting
            pancreatic ductal adenocarcinoma progression through up-regulation
            of CCL28
  JOURNAL   Br J Cancer 129 (3), 426-443 (2023)
   PUBMED   37380804
  REMARK    GeneRIF: Chromatin accessibility uncovers KRAS-driven FOSL2
            promoting pancreatic ductal adenocarcinoma progression through
            up-regulation of CCL28.
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Ng,D.C., Shafaee,S., Lee,D. and Bikle,D.D.
  TITLE     Requirement of an AP-1 site in the calcium response region of the
            involucrin promoter
  JOURNAL   J Biol Chem 275 (31), 24080-24088 (2000)
   PUBMED   10816578
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Miyamoto,N.G., Medberry,P.S., Hesselgesser,J., Boehlk,S.,
            Nelson,P.J., Krensky,A.M. and Perez,H.D.
  TITLE     Interleukin-1beta induction of the chemokine RANTES promoter in the
            human astrocytoma line CH235 requires both constitutive and
            inducible transcription factors
  JOURNAL   J Neuroimmunol 105 (1), 78-90 (2000)
   PUBMED   10713367
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Outinen,P.A., Sood,S.K., Pfeifer,S.I., Pamidi,S., Podor,T.J.,
            Li,J., Weitz,J.I. and Austin,R.C.
  TITLE     Homocysteine-induced endoplasmic reticulum stress and growth arrest
            leads to specific changes in gene expression in human vascular
            endothelial cells
  JOURNAL   Blood 94 (3), 959-967 (1999)
   PUBMED   10419887
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Molven,A., Houge,G. and Berger,R.
  TITLE     Chromosomal assignment of the human gene encoding the Fos-related
            antigen-2 (FRA2) to chromosome 2p22-p23
  JOURNAL   Genomics 38 (1), 72-75 (1996)
   PUBMED   8954781
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Matsui,M., Tokuhara,M., Konuma,Y., Nomura,N. and Ishizaki,R.
  TITLE     Isolation of human fos-related genes and their expression during
            monocyte-macrophage differentiation
  JOURNAL   Oncogene 5 (3), 249-255 (1990)
   PUBMED   2107490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104695.2, BM023443.1,
            AK055579.1, BC022791.1, BX647822.1 and AK026959.1.
            
            On Feb 27, 2004 this sequence version replaced NP_078806.1.
            
            Summary: The Fos gene family consists of 4 members: FOS, FOSB,
            FOSL1, and FOSL2. These genes encode leucine zipper proteins that
            can dimerize with proteins of the JUN family, thereby forming the
            transcription factor complex AP-1. As such, the FOS proteins have
            been implicated as regulators of cell proliferation,
            differentiation, and transformation. [provided by RefSeq, Jul
            2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055579.1, SRR1660807.74443.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264716.9/ ENSP00000264716.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.2"
     Protein         1..326
                     /product="fos-related antigen 2"
                     /note="FRA-2; FOS like antigen 2; FOS like 2, AP-1
                     trancription factor subunit"
                     /calculated_mol_wt=35062
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Site            104
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P47930; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Region          110..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Region          126..128
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Region          129..136
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Region          134..187
                     /region_name="bZIP_Fos"
                     /note="Basic leucine zipper (bZIP) domain of the oncogene
                     Fos (Fos): a DNA-binding and dimerization domain; cd14721"
                     /db_xref="CDD:269869"
     Region          134..186
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269869"
     Site            order(145,148..149,152..153,155..156,159..160,162..163,
                     166..167,169..170,173..174,176..177,180..181,183..184)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269869"
     Region          193..242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Region          289..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15408.1)"
     Site            308
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P15408.1)"
     CDS             1..326
                     /gene="FOSL2"
                     /gene_synonym="ACED; FRA2"
                     /coded_by="NM_005253.4:864..1844"
                     /db_xref="CCDS:CCDS1766.1"
                     /db_xref="GeneID:2355"
                     /db_xref="HGNC:HGNC:3798"
                     /db_xref="MIM:601575"
ORIGIN      
        1 myqdypgnfd tssrgssgsp ahaesyssgg ggqqkfrvdm pgsgsafipt inaittsqdl
       61 qwmvqptvit smsnpyprsh pysplpglas vpghmalprp gviktigttv grrrrdeqls
      121 peeeekrrir rernklaaak crnrrrelte klqaeteele eeksglqkei aelqkekekl
      181 efmlvahgpv ckispeerrs ppapglqpmr sgggsvgavv vkqepleeds pssssagldk
      241 aqrsvikpis iaggfygeep lhtpivvtst pavtpgtsnl vftypsvleq espaspsesc
      301 skahrrssss gdqssdslns ptllal
//
LOCUS       NP_065194               1819 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-tubulin complex component 6 [Homo sapiens].
ACCESSION   NP_065194
VERSION     NP_065194.3
DBSOURCE    REFSEQ: accession NM_020461.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1819)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 1819)
  AUTHORS   Thomas-Wilson,A., Schacht,J.P., Chitayat,D., Blaser,S.,
            Santos,F.J.R., Glaser,K., Caffo,A., Wentzensen,I.M.,
            Henderson,L.B., Zhang,F., Zhu,Y., Di Corleto,E., da Silva Costa,F.,
            Vink,R., Alkhunaizi,E., Russell,L., Buckley,M.F., Roscioli,T.,
            Pereira,E.M. and Ganapathi,M.
  TITLE     Biallelic variants in TUBGCP6 result in microcephaly and
            chorioretinopathy 1: Report of four cases and a literature review
  JOURNAL   Am J Med Genet A 191 (7), 1935-1941 (2023)
   PUBMED   37031378
  REMARK    GeneRIF: Biallelic variants in TUBGCP6 result in microcephaly and
            chorioretinopathy 1: Report of four cases and a literature review.
            Review article
REFERENCE   3  (residues 1 to 1819)
  AUTHORS   Kato,K., Udagawa,R., Hayashi,Y., Maki,M., Yanagida,M.,
            Higashiura,S., Yagishita,R., Shimamoto,H. and Kimura,K.
  TITLE     SF3B14 is involved in the centrosome regulation through splicing of
            TUBGCP6 pre-mRNA
  JOURNAL   Biochem Biophys Res Commun 588, 133-139 (2022)
   PUBMED   34954520
  REMARK    GeneRIF: SF3B14 is involved in the centrosome regulation through
            splicing of TUBGCP6 pre-mRNA.
REFERENCE   4  (residues 1 to 1819)
  AUTHORS   Shurygina,M.F., Simonett,J.M., Parker,M.A., Mitchell,A.,
            Grigorian,F., Lifton,J., Nagiel,A., Shpak,A.A., Dadali,E.L.,
            Mishina,I.A., Weleber,R.G., Yang,P. and Pennesi,M.E.
  TITLE     Genotype Phenotype Correlation and Variability in Microcephaly
            Associated With Chorioretinopathy or Familial Exudative
            Vitreoretinopathy
  JOURNAL   Invest Ophthalmol Vis Sci 61 (13), 2 (2020)
   PUBMED   33137195
  REMARK    GeneRIF: Genotype Phenotype Correlation and Variability in
            Microcephaly Associated With Chorioretinopathy or Familial
            Exudative Vitreoretinopathy.
REFERENCE   5  (residues 1 to 1819)
  AUTHORS   Hull,S., Arno,G., Ostergaard,P., Pontikos,N., Robson,A.G.,
            Webster,A.R., Hogg,C.R., Wright,G.A., Henderson,R.H.H.,
            Martin,C.A., Jackson,A.P., Mansour,S., Moore,A.T. and
            Michaelides,M.
  TITLE     Clinical and Molecular Characterization of Familial Exudative
            Vitreoretinopathy Associated With Microcephaly
  JOURNAL   Am J Ophthalmol 207, 87-98 (2019)
   PUBMED   31077665
  REMARK    GeneRIF: a family of 2 children with learning difficulties,
            abnormal peripheral retinal vasculogenesis, and rod-cone dystrophy
            were investigated. They were found to have bi-allelic splicing
            variants in TUBGCP6.
REFERENCE   6  (residues 1 to 1819)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   7  (residues 1 to 1819)
  AUTHORS   Haren,L. and Merdes,A.
  TITLE     Direct binding of NuMA to tubulin is mediated by a novel sequence
            motif in the tail domain that bundles and stabilizes microtubules
  JOURNAL   J Cell Sci 115 (Pt 9), 1815-1824 (2002)
   PUBMED   11956313
REFERENCE   8  (residues 1 to 1819)
  AUTHORS   Murphy,S.M., Preble,A.M., Patel,U.K., O'Connell,K.L., Dias,D.P.,
            Moritz,M., Agard,D., Stults,J.T. and Stearns,T.
  TITLE     GCP5 and GCP6: two new members of the human gamma-tubulin complex
  JOURNAL   Mol Biol Cell 12 (11), 3340-3352 (2001)
   PUBMED   11694571
REFERENCE   9  (residues 1 to 1819)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 1819)
  AUTHORS   Hsu,H.L. and Yeh,N.H.
  TITLE     Dynamic changes of NuMA during the cell cycle and possible
            appearance of a truncated form of NuMA during apoptosis
  JOURNAL   J Cell Sci 109 (Pt 2), 277-288 (1996)
   PUBMED   8838651
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL022328.21.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_065194.2.
            
            Summary: The protein encoded by this gene is part of a large
            multisubunit complex required for microtubule nucleation at the
            centrosome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF272887.1, SRR7346977.2859410.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248846.10/ ENSP00000248846.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..1819
                     /product="gamma-tubulin complex component 6"
                     /note="tubulin gamma complex associated protein 6"
                     /calculated_mol_wt=200368
     Region          28..342
                     /region_name="GCP6_N"
                     /note="Gamma-tubulin complex component 6 N-terminus;
                     pfam19340"
                     /db_xref="CDD:466048"
     Region          353..633
                     /region_name="GCP_N_terminal"
                     /note="Gamma tubulin complex component N-terminal;
                     pfam17681"
                     /db_xref="CDD:465456"
     Region          <630..834
                     /region_name="DUF5401"
                     /note="Family of unknown function (DUF5401); pfam17380"
                     /db_xref="CDD:375164"
     Region          810..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT7.3)"
     Region          929..951
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT7.3)"
     Region          1000..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT7.3)"
     Region          1027..1269
                     /region_name="9 X 27 AA tandem repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT7.3)"
     Region          1041..1208
                     /region_name="DUF4573"
                     /note="Domain of unknown function (DUF4573); pfam15140"
                     /db_xref="CDD:434493"
     Region          1271..1412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96RT7.3)"
     Region          1513..1816
                     /region_name="GCP_C_terminal"
                     /note="Gamma tubulin complex component C-terminal;
                     pfam04130"
                     /db_xref="CDD:461187"
     CDS             1..1819
                     /gene="TUBGCP6"
                     /gene_synonym="GCP-6; GCP6; MCCRP; MCCRP1; MCPHCR"
                     /coded_by="NM_020461.4:565..6024"
                     /db_xref="CCDS:CCDS14087.1"
                     /db_xref="GeneID:85378"
                     /db_xref="HGNC:HGNC:18127"
                     /db_xref="MIM:610053"
ORIGIN      
        1 masitqlfdd lceallpaak thlgqrsvnr krakrslkkv aynalftnlf qdetqqlqpd
       61 msklparnki lmlsfdlrvg glgpkadrle elveeleaap ccpllevgsv ldllvqlags
      121 gppqvlprkr dyflnnkhvg rnvpysgydc ddlsvfemdv qslisreecl chsmiqetlq
      181 vmeaapgtgl ptvglfsfgd pcgdrferdt rvslfgalvh srtydmdvrl glppvpdnad
      241 lsglaikvpp svdqwedegf qsasnltpds qsepsvtpdv dlweaaltye askrrcwerv
      301 gcppghreep ylteagrdaf dkfcrlhqge lqllaggvlq apqpvlvkec elvkdvlnvl
      361 igvvsatfsl cqpaqafvvk rgvhvsgasp esissllsev aeygtcytrl shfslqpvld
      421 slyskglvfq aftsglrryl qyyracvlst pptlslltig flfkklgrql rylaelcgvg
      481 avlpgtcggg praafptgvk llsylyqeal hncsnehypv llsllktsce pytrfihdwv
      541 ysgvfrdayg efmiqvnhey lsfrdklywt hgyvliskev edcvpvflkh iahdiyvcgk
      601 tinllklccp rhylcwsdvp vprisvifsl eelkeiekdc avyvgrmerv arhssvskee
      661 kelrmeiakq eliahareaa srvlsalsdr qmsermalda rkreqfqrlk eqfvkdqerr
      721 qaarqeeldd dfsyarelrd rerrlkslee elerkarqal vdhysklsae aarreqkalw
      781 riqrhrlesa rlrflledek hiqemlkavs eahqpqeppd vllsvhpqvt spgpehpegg
      841 qgcdsgsaeq hspawdgwnr pglltpqplk plavgaggrg lqqaegarpf sdslsigdfl
      901 pvgpgaepsv qtgmvpllev alqtinldlp psapgeapaa astqpsrpqe ydfstvlrpa
      961 vatspapgpl qaaecslgss glqlwedscg kmdacgsasr etllpshppr raaleegssq
     1021 pterlfgqvs ggglptgdya seiaptrprw nthghvsdas irvgenvsdv aptqprwnth
     1081 ghvsnasisl gesvsdvapt rprwnihghv snasirvgen vsdvaptrpr wnthghvsna
     1141 sirvgenvsd vaptrprwnt hghvsdasis lgesvsdmap arprwnthgh vsdasislge
     1201 svsdmaptrp rwnthghvsd tsirvgenvs dvapirsrcn thghvsdasi slgepvsdvv
     1261 strprwnthv pippphmvlg alspeaepnt prpqqsppgh tsqsalslga qstvldcgpr
     1321 lpvevgpsls spssgcgegs isvgenvsdv aptqpwwpnt pgdsvseelg pgrsgdtedl
     1381 spnwplnsqe dtaaqsspgr geeaeasaae aqggeqayla glagqyhler ypdsyesmse
     1441 ppiahllrpv lprafafpvd pqvqsaadet avqlselltl pvlmkrsita plaahislvn
     1501 kaavdyffve lhleahyeal rhfllmedge faqslsdllf eklgagqtpg ellnplvlns
     1561 vlskalqcsl hgdtphasnl slalkylpev fapnapdvls clelrykvdw plnivitegc
     1621 vskysgvfsf llqlklmmwa lkdvcfhlkr tallshmags vqfrqlqlfk hemqhfvkvi
     1681 qgyianqilh vtwcefrarl atvgdleeiq rahaeylhka vfrgllteka apvmnvihsi
     1741 fslvlkfrsq lisqawgppg gprgaehpnf almqqsyntf kyyshflfkv vtklvnrgyq
     1801 phledfllri nfnnyyqda
//
LOCUS       NP_839952                347 aa            linear   PRI 20-NOV-2025
DEFINITION  dolichyl-diphosphooligosaccharide--protein glycosyltransferase
            subunit TUSC3 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_839952
VERSION     NP_839952.1
DBSOURCE    REFSEQ: accession NM_178234.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Deng,R., Lu,X., Hong,C., Cai,R., Wang,P., Xiong,L., Wang,X.,
            Chen,Q. and Lin,J.
  TITLE     Downregulation of TUSC3 promotes EMT and hepatocellular carcinoma
            progression through LIPC/AKT axis
  JOURNAL   J Transl Med 20 (1), 485 (2022)
   PUBMED   36274132
  REMARK    GeneRIF: Downregulation of TUSC3 promotes EMT and hepatocellular
            carcinoma progression through LIPC/AKT axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Sun,F., Jie,Q., Li,Q., Wei,Y., Li,H., Yue,X. and Ma,Y.
  TITLE     TUSC3 inhibits cell proliferation and invasion in cervical squamous
            cell carcinoma via suppression of the AKT signalling pathway
  JOURNAL   J Cell Mol Med 26 (5), 1629-1642 (2022)
   PUBMED   35137520
  REMARK    GeneRIF: TUSC3 inhibits cell proliferation and invasion in cervical
            squamous cell carcinoma via suppression of the AKT signalling
            pathway.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Ren,Y., Deng,R., Cai,R., Lu,X., Luo,Y., Wang,Z., Zhu,Y., Yin,M.,
            Ding,Y. and Lin,J.
  TITLE     TUSC3 induces drug resistance and cellular stemness via Hedgehog
            signaling pathway in colorectal cancer
  JOURNAL   Carcinogenesis 41 (12), 1755-1766 (2020)
   PUBMED   32338281
  REMARK    GeneRIF: TUSC3 induces drug resistance and cellular stemness via
            Hedgehog signaling pathway in colorectal cancer.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Ouidir,M., Mendola,P., Buck Louis,G.M., Kannan,K., Zhang,C. and
            Tekola-Ayele,F.
  TITLE     Concentrations of persistent organic pollutants in maternal plasma
            and epigenome-wide placental DNA methylation
  JOURNAL   Clin Epigenetics 12 (1), 103 (2020)
   PUBMED   32653021
  REMARK    GeneRIF: Concentrations of persistent organic pollutants in
            maternal plasma and epigenome-wide placental DNA methylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Wang,S. and Zhu,W.
  TITLE     Tumour suppressor candidate 3 inhibits biological function and
            increases endoplasmic reticulum stress of melanoma cells WM451 by
            regulating AKT/GSK3-beta/beta-catenin pathway
  JOURNAL   Cell Biochem Funct 38 (5), 604-612 (2020)
   PUBMED   32090352
  REMARK    GeneRIF: Tumour suppressor candidate 3 inhibits biological function
            and increases endoplasmic reticulum stress of melanoma cells WM451
            by regulating AKT/GSK3-beta/beta-catenin pathway.
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Kelleher,D.J., Karaoglu,D., Mandon,E.C. and Gilmore,R.
  TITLE     Oligosaccharyltransferase isoforms that contain different catalytic
            STT3 subunits have distinct enzymatic properties
  JOURNAL   Mol Cell 12 (1), 101-111 (2003)
   PUBMED   12887896
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Ishii,H., Baffa,R., Numata,S.I., Murakumo,Y., Rattan,S., Inoue,H.,
            Mori,M., Fidanza,V., Alder,H. and Croce,C.M.
  TITLE     The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
            and its expression is altered in multiple human tumors
  JOURNAL   Proc Natl Acad Sci U S A 96 (7), 3928-3933 (1999)
   PUBMED   10097140
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Pak,B.J., Park,H., Chang,E.R., Pang,S.C. and Graham,C.H.
  TITLE     Differential display analysis of oxygen-mediated changes in gene
            expression in first trimester human trophoblast cells
  JOURNAL   Placenta 19 (7), 483-488 (1998)
   PUBMED   9778121
REFERENCE   9  (residues 1 to 347)
  AUTHORS   MacGrogan,D., Levy,A., Bova,G.S., Isaacs,W.B. and Bookstein,R.
  TITLE     Structure and methylation-associated silencing of a gene within a
            homozygously deleted region of human chromosome band 8p22
  JOURNAL   Genomics 35 (1), 55-65 (1996)
   PUBMED   8661104
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA796279.1, BC010370.1,
            AC019292.10 and AI366810.1.
            
            Summary: This gene encodes a protein that has been associated with
            several biological functions including cellular magnesium uptake,
            protein glycosylation and embryonic development. This protein
            localizes to the endoplasmic reticulum and acts as a component of
            the oligosaccharyl transferase complex which is responsible for
            N-linked protein glycosylation. This gene is a candidate tumor
            suppressor gene. Homozygous mutations in this gene are associated
            with autosomal recessive nonsyndromic mental retardation-7 and in
            the proliferation and invasiveness of several cancers including
            metastatic pancreatic cancer, ovarian cancer and glioblastoma
            multiform. [provided by RefSeq, Oct 2017].
            
            Transcript Variant: This variant (2) lacks an exon in the 3' region
            compared to variant 1. The resulting isoform (b) contains a one aa
            shorter and distinct C-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.67774.1,
                                           SRR1660803.22868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMN03568911
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..347
                     /product="dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3 isoform 2 precursor"
                     /note="oligosaccharyltransferase 3 homolog A; magnesium
                     uptake/transporter TUSC3; putative prostate cancer tumor
                     suppressor; oligosaccharyl transferase subunit TUSC3;
                     dolichyl-diphosphooligosaccharide--protein
                     glycosyltransferase subunit TUSC3"
                     /calculated_mol_wt=35093
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4483
     Region          54..342
                     /region_name="OST3_OST6"
                     /note="OST3 / OST6 family, transporter family; pfam04756"
                     /db_xref="CDD:461420"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            222..242
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            277..297
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13454.1)"
     CDS             1..347
                     /gene="TUSC3"
                     /gene_synonym="D8S1992; M33; MagT2; MRT22; MRT7; N33;
                     OST3A; SLC58A2"
                     /coded_by="NM_178234.2:345..1388"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS5993.1"
                     /db_xref="GeneID:7991"
                     /db_xref="HGNC:HGNC:30242"
                     /db_xref="MIM:601385"
ORIGIN      
        1 mgargapsrr rqagrrlryl ptgsfpflll llllciqlgg gqkkkenlla ekveqlmews
       61 srrsifrmng dkfrkfikap prnysmivmf talqpqrqcs vcrqaneeyq ilanswryss
      121 afcnklffsm vdydegtdvf qqlnmnsapt fmhfppkgrp kradtfdlqr igfaaeqlak
      181 wiadrtdvhi rvfrppnysg tialallvsl vggllylrrn nlefiynktg wamvslcivf
      241 amtsgqmwnh irgppyahkn phngqvsyih gssqaqfvae shiilvlnaa itmgmvllne
      301 aatskgdvgk rriiclvglg lvvfffsfll sifrskyhgy pysflik
//
LOCUS       NP_001191020             165 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein eS10 [Homo sapiens].
ACCESSION   NP_001191020
VERSION     NP_001191020.1
DBSOURCE    REFSEQ: accession NM_001204091.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Ugajin,N., Imami,K., Takada,H., Ishihama,Y., Chiba,S. and
            Mishima,Y.
  TITLE     Znf598-mediated Rps10/eS10 ubiquitination contributes to the
            ribosome ubiquitination dynamics during zebrafish development
  JOURNAL   RNA 29 (12), 1910-1927 (2023)
   PUBMED   37751929
  REMARK    GeneRIF: Znf598-mediated Rps10/eS10 ubiquitination contributes to
            the ribosome ubiquitination dynamics during zebrafish development.
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Li,J., Su,Y., Chen,L., Lin,Y. and Ru,K.
  TITLE     Identification of novel mutations in patients with Diamond-Blackfan
            anemia and literature review of RPS10 and RPS26 mutations
  JOURNAL   Int J Lab Hematol 45 (5), 766-773 (2023)
   PUBMED   37376976
  REMARK    GeneRIF: Identification of novel mutations in patients with
            Diamond-Blackfan anemia and literature review of RPS10 and RPS26
            mutations.
            Review article
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Malygin,A.A., Shaulo,D.D. and Karpova,G.G.
  TITLE     Proteins S7, S10, S16 and S19 of the human 40S ribosomal subunit
            are most resistant to dissociation by salt
  JOURNAL   Biochim Biophys Acta 1494 (3), 213-216 (2000)
   PUBMED   11121577
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Pei,L.
  TITLE     Pituitary tumor-transforming gene protein associates with ribosomal
            protein S10 and a novel human homologue of DnaJ in testicular cells
  JOURNAL   J Biol Chem 274 (5), 3151-3158 (1999)
   PUBMED   9915854
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Frigerio,J.M., Dagorn,J.C. and Iovanna,J.L.
  TITLE     Cloning, sequencing and expression of the L5, L21, L27a, L28, S5,
            S9, S10 and S29 human ribosomal protein mRNAs
  JOURNAL   Biochim Biophys Acta 1262 (1), 64-68 (1995)
   PUBMED   7772601
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157372.18 and BU956627.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit. The protein belongs
            to the S10E family of ribosomal proteins. It is located in the
            cytoplasm. Variable expression of this gene in colorectal cancers
            compared to adjacent normal tissues has been observed, although no
            correlation between the level of expression and the severity of the
            disease has been found. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. Alternate splicing results in
            multiple transcript variants that encode the same protein.
            Naturally occurring read-through transcription occurs between this
            locus and the neighboring locus NUDT3 (nudix (nucleoside
            diphosphate linked moiety X)-type motif 3).[provided by RefSeq, Feb
            2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU956627.1, SRR14478891.1969234.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..165
                     /product="small ribosomal subunit protein eS10"
                     /note="40S ribosomal protein S10"
                     /calculated_mol_wt=18767
     Region          3..97
                     /region_name="S10_plectin"
                     /note="Plectin/S10 domain; pfam03501"
                     /db_xref="CDD:427337"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P63325; propagated from
                     UniProtKB/Swiss-Prot (P46783.1)"
     Region          92..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46783.1)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63325; propagated from
                     UniProtKB/Swiss-Prot (P46783.1)"
     Site            153
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P63325; propagated from
                     UniProtKB/Swiss-Prot (P46783.1)"
     Site            158
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:20159986; propagated from
                     UniProtKB/Swiss-Prot (P46783.1)"
     Site            160
                     /site_type="methylation"
                     /note="Symmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:20159986; propagated from
                     UniProtKB/Swiss-Prot (P46783.1)"
     CDS             1..165
                     /gene="RPS10"
                     /gene_synonym="DBA9; eS10; S10"
                     /coded_by="NM_001204091.2:43..540"
                     /db_xref="CCDS:CCDS4792.1"
                     /db_xref="GeneID:6204"
                     /db_xref="HGNC:HGNC:10383"
                     /db_xref="MIM:603632"
ORIGIN      
        1 mlmpkknria iyellfkegv mvakkdvhmp khpeladknv pnlhvmkamq slksrgyvke
       61 qfawrhfywy ltnegiqylr dylhlppeiv patlrrsrpe tgrprpkgle gerparltrg
      121 eadrdtyrrs avppgadkka eagagsatef qfrggfgrgr gqppq
//
LOCUS       NP_001340182             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340182 XP_016869038
VERSION     NP_001340182.1
DBSOURCE    REFSEQ: accession NM_001353253.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869038.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.125389.1,
                                           SRR1803616.146514.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353253.1:377..1351"
                     /note="isoform 1 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001316536             438 aa            linear   PRI 20-NOV-2025
DEFINITION  casein kinase I isoform gamma-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001316536
VERSION     NP_001316536.1
DBSOURCE    REFSEQ: accession NM_001329607.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Miao,Y., Cui,L., Chen,Z. and Zhang,L.
  TITLE     Gene expression profiling of DMU-212-induced apoptosis and
            anti-angiogenesis in vascular endothelial cells
  JOURNAL   Pharm Biol 54 (4), 660-666 (2016)
   PUBMED   26428916
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Chia,R., Haddock,S., Beilina,A., Rudenko,I.N., Mamais,A.,
            Kaganovich,A., Li,Y., Kumaran,R., Nalls,M.A. and Cookson,M.R.
  TITLE     Phosphorylation of LRRK2 by casein kinase 1alpha regulates
            trans-Golgi clustering via differential interaction with ARHGEF7
  JOURNAL   Nat Commun 5, 5827 (2014)
   PUBMED   25500533
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Martin,H.C., Kim,G.E., Pagnamenta,A.T., Murakami,Y., Carvill,G.L.,
            Meyer,E., Copley,R.R., Rimmer,A., Barcia,G., Fleming,M.R.,
            Kronengold,J., Brown,M.R., Hudspith,K.A., Broxholme,J., Kanapin,A.,
            Cazier,J.B., Kinoshita,T., Nabbout,R., Bentley,D., McVean,G.,
            Heavin,S., Zaiwalla,Z., McShane,T., Mefford,H.C., Shears,D.,
            Stewart,H., Kurian,M.A., Scheffer,I.E., Blair,E., Donnelly,P.,
            Kaczmarek,L.K. and Taylor,J.C.
  CONSRTM   WGS500 Consortium
  TITLE     Clinical whole-genome sequencing in severe early-onset epilepsy
            reveals new genes and improves molecular diagnosis
  JOURNAL   Hum Mol Genet 23 (12), 3200-3211 (2014)
   PUBMED   24463883
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Wang,Y., Hu,L., Tong,X. and Ye,X.
  TITLE     Casein kinase 1gamma1 inhibits the RIG-I/TLR signaling pathway
            through phosphorylating p65 and promoting its degradation
  JOURNAL   J Immunol 192 (4), 1855-1861 (2014)
   PUBMED   24442433
  REMARK    GeneRIF: CK1gamma1 phosphorylates p65 and consequently promotes its
            degradation by ubiquitin E3 ligases CUL2 and COMMD1.
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Meng,Z., Capalbo,L., Glover,D.M. and Dunphy,W.G.
  TITLE     Role for casein kinase 1 in the phosphorylation of Claspin on
            critical residues necessary for the activation of Chk1
  JOURNAL   Mol Biol Cell 22 (16), 2834-2847 (2011)
   PUBMED   21680713
  REMARK    GeneRIF: casein kinase 1 gamma 1 phosphorylates claspin
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Guo,L., Jiang,M., Ma,Y., Cheng,H., Ni,X., Ma,Y., Ji,C., Xie,Y. and
            Mao,Y.
  TITLE     Molecular cloning, mapping and characterization of a human
            CK1gamma1 gene
  JOURNAL   Int J Mol Med 10 (2), 227-230 (2002)
   PUBMED   12119564
  REMARK    GeneRIF: A 1756 bp cDNA encoded human protein kinase CK1 (438 AA,
            mol wt 50.272 Da, isoelectric point of 9.37) mapping to chromosome
            15q22.
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Kusuda,J., Hirai,M., Tanuma,R. and Hashimoto,K.
  TITLE     Cloning, expression analysis and chromosome mapping of human casein
            kinase 1 gamma1 (CSNK1G1): identification of two types of cDNA
            encoding the kinase protein associated with heterologous
            carboxy-terminal sequences
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 298-302 (2000)
   PUBMED   11124537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC087632.10, AC110054.4 and
            AC100840.2.
            
            Summary: This gene encodes a member of the casein kinase I gene
            family. This family is comprised of serine/threonine kinases that
            phosphorylate acidic proteins such as caseins. The encoded kinase
            plays a role in cell cycle checkpoint arrest in response to stalled
            replication forks by phosphorylating Claspin. A mutation in this
            gene may be associated with non-syndromic early-onset epilepsy
            (NSEOE). [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 3' coding region compared to variant 1. The encoded isoform
            (3) contains a longer and distinct C-terminus compared to isoform
            1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.126332.1,
                                           SRR3476690.871200.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..438
                     /product="casein kinase I isoform gamma-1 isoform 3"
                     /EC_number="2.7.11.1"
                     /calculated_mol_wt=50214
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCP0.1)"
     Region          43..331
                     /region_name="STKc_CK1_gamma"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, Casein Kinase 1 gamma; cd14126"
                     /db_xref="CDD:271028"
     Site            order(50..56,58,71,73,118..122,124,126,164,166,168..169,
                     171,187,190,213..216)
                     /site_type="active"
                     /db_xref="CDD:271028"
     Site            order(50..56,58,71,73,118..122,166,168..169,171,187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271028"
     Site            order(54,124,126,164,166,168,190,213..216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271028"
     Site            186..216
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271028"
     Region          331..392
                     /region_name="CK1gamma_C"
                     /note="Casein kinase 1 gamma C terminal; pfam12605"
                     /db_xref="CDD:463640"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q9HCP0.1)"
     Region          351..389
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCP0.1)"
     CDS             1..438
                     /gene="CSNK1G1"
                     /gene_synonym="CK1gamma1"
                     /coded_by="NM_001329607.2:411..1727"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86464.1"
                     /db_xref="GeneID:53944"
                     /db_xref="HGNC:HGNC:2454"
                     /db_xref="MIM:606274"
ORIGIN      
        1 mdhpsrekde rqrttkpmaq rsahcsrpsg sssssgvlmv gpnfrvgkki gcgnfgelrl
       61 gknlytneyv aiklepiksr apqlhleyrf ykqlgsageg lpqvyyfgpc gkynamvlel
      121 lgpsledlfd lcdrtftlkt vlmiaiqlls rmeyvhsknl iyrdvkpenf ligrqgnkke
      181 hvihiidfgl akeyidpetk khipyrehks ltgtarymsi nthlgkeqsr rddlealghm
      241 fmyflrgslp wqglkadtlk eryqkigdtk rntpiealce nfpeematyl ryvrrldffe
      301 kpdyeylrtl ftdlfekkgy tfdyaydwvg rpiptpvgsv hvdsgasait reshthrdrp
      361 sqqqplrnqv vsstngelnv ddptgahsna pitahaevev veeakcimfh kpwhwsqssa
      421 vkmkfvvfln mnvnfkci
//
LOCUS       NP_001034708             620 aa            linear   PRI 20-NOV-2025
DEFINITION  protein arginine N-methyltransferase 5 isoform b [Homo sapiens].
ACCESSION   NP_001034708
VERSION     NP_001034708.1
DBSOURCE    REFSEQ: accession NM_001039619.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Kurdi,M., Alkhotani,A., Sabbagh,A., Faizo,E., Lary,A.I.,
            Bamaga,A.K., Almansouri,M., Hafiz,B., Alsharif,T. and Baeesa,S.
  TITLE     The interplay mechanism between IDH mutation, MGMT-promoter
            methylation, and PRMT5 activity in the progression of grade 4
            astrocytoma: unraveling the complex triad theory
  JOURNAL   Oncol Res 32 (6), 1037-1045 (2024)
   PUBMED   38827324
  REMARK    GeneRIF: The interplay mechanism between IDH mutation,
            MGMT-promoter methylation, and PRMT5 activity in the progression of
            grade 4 astrocytoma: unraveling the complex triad theory.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Abe,Y., Sano,T., Otsuka,N., Ogawa,M. and Tanaka,N.
  TITLE     PRMT5-mediated methylation of STAT3 is required for lung cancer
            stem cell maintenance and tumour growth
  JOURNAL   Commun Biol 7 (1), 593 (2024)
   PUBMED   38760429
  REMARK    GeneRIF: PRMT5-mediated methylation of STAT3 is required for lung
            cancer stem cell maintenance and tumour growth.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Zhang,X., Liu,Q., Wang,L. and Peng,Q.
  TITLE     Identification of protein methyltransferases 5 associated with
            ferroptosis and immune cell infiltration of head and neck squamous
            cell carcinoma
  JOURNAL   Aging (Albany NY) 16 (8), 7426-7436 (2024)
   PUBMED   38663941
  REMARK    GeneRIF: Identification of protein methyltransferases 5 associated
            with ferroptosis and immune cell infiltration of head and neck
            squamous cell carcinoma.
REFERENCE   5  (residues 1 to 620)
  AUTHORS   Liu,Y., Jiang,H., Hu,K., Zou,H., Zhang,W., Liu,J. and Jian,X.
  TITLE     CircPRMT5 promotes progression of osteosarcoma by recruiting CNBP
            to regulate the translation and stability of CDK6 mRNA
  JOURNAL   PLoS One 19 (4), e0298947 (2024)
   PUBMED   38626179
  REMARK    GeneRIF: CircPRMT5 promotes progression of osteosarcoma by
            recruiting CNBP to regulate the translation and stability of CDK6
            mRNA.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 620)
  AUTHORS   Rho,J., Choi,S., Seong,Y.R., Cho,W.K., Kim,S.H. and Im,D.S.
  TITLE     Prmt5, which forms distinct homo-oligomers, is a member of the
            protein-arginine methyltransferase family
  JOURNAL   J Biol Chem 276 (14), 11393-11401 (2001)
   PUBMED   11152681
REFERENCE   7  (residues 1 to 620)
  AUTHORS   Schwarzler,A., Kreienkamp,H.J. and Richter,D.
  TITLE     Interaction of the somatostatin receptor subtype 1 with the human
            homolog of the Shk1 kinase-binding protein from yeast
  JOURNAL   J Biol Chem 275 (13), 9557-9562 (2000)
   PUBMED   10734105
REFERENCE   8  (residues 1 to 620)
  AUTHORS   Pollack,B.P., Kotenko,S.V., He,W., Izotova,L.S., Barnoski,B.L. and
            Pestka,S.
  TITLE     The human homologue of the yeast proteins Skb1 and Hsl7p interacts
            with Jak kinases and contains protein methyltransferase activity
  JOURNAL   J Biol Chem 274 (44), 31531-31542 (1999)
   PUBMED   10531356
REFERENCE   9  (residues 1 to 620)
  AUTHORS   Gilbreth,M., Yang,P., Bartholomeusz,G., Pimental,R.A., Kansra,S.,
            Gadiraju,R. and Marcus,S.
  TITLE     Negative regulation of mitosis in fission yeast by the shk1
            interacting protein skb1 and its human homolog, Skb1Hs
  JOURNAL   Proc Natl Acad Sci U S A 95 (25), 14781-14786 (1998)
   PUBMED   9843966
REFERENCE   10 (residues 1 to 620)
  AUTHORS   Krapivinsky,G., Pu,W., Wickman,K., Krapivinsky,L. and Clapham,D.E.
  TITLE     pICln binds to a mammalian homolog of a yeast protein involved in
            regulation of cell morphology
  JOURNAL   J Biol Chem 273 (18), 10811-10814 (1998)
   PUBMED   9556550
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK075251.1 and AK027737.1.
            
            Summary: This gene encodes an enzyme that belongs to the
            methyltransferase family. The encoded protein catalyzes the
            transfer of methyl groups to the amino acid arginine, in target
            proteins that include histones, transcriptional elongation factors
            and the tumor suppressor p53. This gene plays a role in several
            cellular processes, including transcriptional regulation, and the
            assembly of small nuclear ribonucleoproteins. A pseudogene of this
            gene has been defined on chromosome 4. Alternative splicing results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' coding region and initiates translation at an alternate
            start codon, compared to variant 1. The encoded isoform (b) is
            shorter and has a distinct N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1005267.1, AK075251.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..620
                     /product="protein arginine N-methyltransferase 5 isoform
                     b"
                     /EC_number="2.1.1.320"
                     /note="protein arginine N-methyltransferase 5; HMT1 hnRNP
                     methyltransferase-like 5; jak-binding protein 1; 72 kDa
                     ICln-binding protein; shk1 kinase-binding protein 1
                     homolog; histone-arginine N-methyltransferase PRMT5; SKB1
                     homolog"
                     /calculated_mol_wt=71190
     Region          20..273
                     /region_name="PRMT5_TIM"
                     /note="PRMT5 TIM barrel domain; pfam17285"
                     /db_xref="CDD:435840"
     Region          278..447
                     /region_name="PRMT5"
                     /note="PRMT5 arginine-N-methyltransferase; pfam05185"
                     /db_xref="CDD:428356"
     Region          451..618
                     /region_name="PRMT5_C"
                     /note="PRMT5 oligomerization domain; pfam17286"
                     /db_xref="CDD:435841"
     CDS             1..620
                     /gene="PRMT5"
                     /gene_synonym="HRMT1L5; HSL7; IBP72; JBP1; SKB1; SKB1Hs"
                     /coded_by="NM_001039619.3:152..2014"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41922.1"
                     /db_xref="GeneID:10419"
                     /db_xref="HGNC:HGNC:10894"
                     /db_xref="MIM:604045"
ORIGIN      
        1 mrgpnsgtek grlvipekqg fdflcmpvfh prfkrefiqe paknrpgpqt rsdlllsgrd
       61 wntlivgkls pwirpdskve kirrnseaam lqelnfgayl glpafllpln qedntnlarv
      121 ltnhihtghh ssmfwmrvpl vapedlrddi ienaptthte eysgeektwm wwhnfrtlcd
      181 yskriavale igadlpsnhv idrwlgepik aailptsifl tnkkgfpvls kmhqrlifrl
      241 lklevqfiit gtnhhsekef csylqyleyl sqnrpppnay elfakgyedy lqsplqplmd
      301 nlesqtyevf ekdpikysqy qqaiykclld rvpeeekdtn vqvlmvlgag rgplvnaslr
      361 aakqadrrik lyaveknpna vvtlenwqfe ewgsqvtvvs sdmrewvape kadiivsell
      421 gsfadnelsp ecldgaqhfl kddgvsipge ytsflapiss sklynevrac rekdrdpeaq
      481 fempyvvrlh nfhqlsapqp cftfshpnrd pmidnnryct lefpvevntv lhgfagyfet
      541 vlyqditlsi rpethspgmf swfpilfpik qpitvregqt icvrfwrcsn skkvwyewav
      601 tapvcsaihn ptgrsytigl
//
LOCUS       NP_003038                815 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium/hydrogen exchanger 1 [Homo sapiens].
ACCESSION   NP_003038
VERSION     NP_003038.2
DBSOURCE    REFSEQ: accession NM_003047.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 815)
  AUTHORS   Chen,A., Zhang,J., Yan,Z., Lu,Y., Chen,W., Sun,Y., Gu,Q., Li,F.,
            Yang,Y., Qiu,S., Lin,X., Zhang,D., Teng,J., Fang,Y., Shen,B.,
            Song,N. and Ding,X.
  TITLE     Acidic preconditioning induced intracellular acid adaptation to
            protect renal injury via dynamic phosphorylation of focal adhesion
            kinase-dependent activation of sodium hydrogen exchanger 1
  JOURNAL   Cell Commun Signal 22 (1), 393 (2024)
   PUBMED   39118129
  REMARK    GeneRIF: Acidic preconditioning induced intracellular acid
            adaptation to protect renal injury via dynamic phosphorylation of
            focal adhesion kinase-dependent activation of sodium hydrogen
            exchanger 1.
            Erratum:[Cell Commun Signal. 2024 Sep 11;22(1):439. doi:
            10.1186/s12964-024-01815-3. PMID: 39261884]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 815)
  AUTHORS   Hayashi,Y., Miyoshi,S., Watanabe,I., Yano,N., Nagashio,K.,
            Kaneko,M., Kaminota,T., Sanada,T., Hosokawa,Y., Kitani,T.,
            Mitani,S., Choudhury,M.E., Yano,H., Tanaka,J. and Hato,N.
  TITLE     Simultaneous disturbance of NHE1 and LOXL2 decreases tumorigenicity
            of head and neck squamous cell carcinoma
  JOURNAL   Auris Nasus Larynx 51 (3), 472-480 (2024)
   PUBMED   38520980
  REMARK    GeneRIF: Simultaneous disturbance of NHE1 and LOXL2 decreases
            tumorigenicity of head and neck squamous cell carcinoma.
REFERENCE   3  (residues 1 to 815)
  AUTHORS   Li,X. and Fliegel,L.
  TITLE     Permissive role of Na+/H+ exchanger isoform 1 in migration and
            invasion of triple-negative basal-like breast cancer cells
  JOURNAL   Mol Cell Biochem 477 (4), 1207-1216 (2022)
   PUBMED   35084672
  REMARK    GeneRIF: Permissive role of Na(+)/H(+) exchanger isoform 1 in
            migration and invasion of triple-negative basal-like breast cancer
            cells.
REFERENCE   4  (residues 1 to 815)
  AUTHORS   Zhu,X., Ma,K., Zhou,K., Pan,X., Liu,J., Nurnberg,B., Alesutan,I.,
            Volkl,J. and Lang,F.
  TITLE     Requirement of Na+/H+ Exchanger NHE1 for Vasopressin-Induced
            Osteogenic Signaling and Calcification in Human Aortic Smooth
            Muscle Cells
  JOURNAL   Kidney Blood Press Res 47 (6), 399-409 (2022)
   PUBMED   35339998
  REMARK    GeneRIF: Requirement of Na+/H+ Exchanger NHE1 for
            Vasopressin-Induced Osteogenic Signaling and Calcification in Human
            Aortic Smooth Muscle Cells.
REFERENCE   5  (residues 1 to 815)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   6  (residues 1 to 815)
  AUTHORS   Tse,C.M., Ma,A.I., Yang,V.W., Watson,A.J., Levine,S.,
            Montrose,M.H., Potter,J., Sardet,C., Pouyssegur,J. and Donowitz,M.
  TITLE     Molecular cloning and expression of a cDNA encoding the rabbit
            ileal villus cell basolateral membrane Na+/H+ exchanger
  JOURNAL   EMBO J 10 (8), 1957-1967 (1991)
   PUBMED   1712287
REFERENCE   7  (residues 1 to 815)
  AUTHORS   Dudley,C.R., Giuffra,L.A., Tippett,P., Kidd,K.K. and Reeders,S.T.
  TITLE     The Na+/H+ antiporter: a 'melt' polymorphism allows regional
            mapping to the short arm of chromosome 1
  JOURNAL   Hum Genet 86 (1), 79-83 (1990)
   PUBMED   1979310
REFERENCE   8  (residues 1 to 815)
  AUTHORS   Sardet,C., Counillon,L., Franchi,A. and Pouyssegur,J.
  TITLE     Growth factors induce phosphorylation of the Na+/H+ antiporter,
            glycoprotein of 110 kD
  JOURNAL   Science 247 (4943), 723-726 (1990)
   PUBMED   2154036
REFERENCE   9  (residues 1 to 815)
  AUTHORS   Sardet,C., Franchi,A. and Pouyssegur,J.
  TITLE     Molecular cloning, primary structure, and expression of the human
            growth factor-activatable Na+/H+ antiporter
  JOURNAL   Cell 56 (2), 271-280 (1989)
   PUBMED   2536298
REFERENCE   10 (residues 1 to 815)
  AUTHORS   Mattei,M.G., Sardet,C., Franchi,A. and Pouyssegur,J.
  TITLE     The human amiloride-sensitive Na+/H+ antiporter: localization to
            chromosome 1 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 48 (1), 6-8 (1988)
   PUBMED   2846238
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA853045.1, DA313453.1,
            AK314190.1, AF141357.1, AL137860.22 and BQ775318.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 17, 2003 this sequence version replaced NP_003038.1.
            
            Summary: This gene encodes a Na+/H+ antiporter that is a member of
            the solute carrier family 9. The encoded protein is a plasma
            membrane transporter that is expressed in the kidney and intestine.
            This protein plays a central role in regulating pH homeostasis,
            cell migration and cell volume. This protein may also be involved
            in tumor growth. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the functional protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: S68616.1, M96066.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263980.8/ ENSP00000263980.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..815
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..815
                     /product="sodium/hydrogen exchanger 1"
                     /note="solute carrier family 9, subfamily A (NHE1, cation
                     proton antiporter 1), member 1; solute carrier family 9
                     (sodium/hydrogen exchanger), member 1 (antiporter, Na+/H+,
                     amiloride sensitive); Na-Li countertransporter; Na(+)/H(+)
                     exchanger 1; protein phosphatase 1, regulatory subunit
                     143"
                     /calculated_mol_wt=90632
     Region          42..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            42
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            56
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            61
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            62
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            68
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            75
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:8068684; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Region          95..660
                     /region_name="b_cpa1"
                     /note="sodium/hydrogen exchanger 3; TIGR00840"
                     /db_xref="CDD:273294"
     Site            99..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            131..148
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            159..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            161
                     /site_type="other"
                     /note="Channel pore-lining. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            187..215
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            223..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            253..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            288..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            329..341
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            351..371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            370
                     /site_type="other"
                     /note="Not glycosylated; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            374..404
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            411..438
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            445..469
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            476..505
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          503..545
                     /region_name="Interaction with TESC.
                     /evidence=ECO:0000269|PubMed:30287853"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          509..516
                     /region_name="PI(4,5)P2-binding region.
                     /evidence=ECO:0000250|UniProtKB:P26431"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          515..545
                     /region_name="Interaction with CHP2.
                     /evidence=ECO:0000269|PubMed:21392185"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          540..545
                     /region_name="Confers pH-dependent PI(4,5)P2 binding.
                     /evidence=ECO:0000269|PubMed:27650500"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          552..560
                     /region_name="PI(4,5)P2-binding region.
                     /evidence=ECO:0000250|UniProtKB:P26431"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q61165; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Region          633..815
                     /region_name="Interaction with CALM1.
                     /evidence=ECO:0000269|PubMed:30287853"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          633..815
                     /region_name="Interaction with TESC.
                     /evidence=ECO:0000269|PubMed:12809501"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18757828; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Region          684..687
                     /region_name="Interaction with PPP3CA.
                     /evidence=ECO:0000269|PubMed:31375679"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Region          715..720
                     /region_name="Interaction with PPP3CA.
                     /evidence=ECO:0000269|PubMed:31375679"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Region          744..815
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19634.2)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:31375679; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61165; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     Site            796
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P26431; propagated from
                     UniProtKB/Swiss-Prot (P19634.2)"
     CDS             1..815
                     /gene="SLC9A1"
                     /gene_synonym="APNH; LIKNS; NHE-1; NHE1; PPP1R143"
                     /coded_by="NM_003047.5:792..3239"
                     /db_xref="CCDS:CCDS295.1"
                     /db_xref="GeneID:6548"
                     /db_xref="HGNC:HGNC:11071"
                     /db_xref="MIM:107310"
ORIGIN      
        1 mvlrsgicgl sphrifpsll vvvalvgllp vlrshglqls ptastirsse pprersigdv
       61 ttappevtpe srpvnhsvtd hgmkprkafp vlgidythvr tpfeislwil laclmkigfh
      121 viptissivp escllivvgl lvgglikgvg etppflqsdv fflfllppii ldagyflplr
      181 qftenlgtil ifavvgtlwn afflgglmya vclvggeqin niglldnllf gsiisavdpv
      241 avlavfeeih inellhilvf gesllndavt vvlyhlfeef anyehvgivd iflgflsffv
      301 valggvlvgv vygviaafts rftshirvie plfvflysym aylsaelfhl sgimaliasg
      361 vvmrpyvean ishkshttik yflkmwssvs etlififlgv stvagshhwn wtfvistllf
      421 cliarvlgvl gltwfinkfr ivkltpkdqf iiaygglrga iafslgylld kkhfpmcdlf
      481 ltaiitviff tvfvqgmtir plvdllavkk kqetkrsine eihtqfldhl ltgiedicgh
      541 yghhhwkdkl nrfnkkyvkk cliagerske pqliafyhkm emkqaielve sggmgkipsa
      601 vstvsmqnih pkslpseril palskdkeee irkilrnnlq ktrqrlrsyn rhtlvadpye
      661 eawnqmllrr qkarqleqki nnyltvpahk ldsptmsrar igsdplayep kedlpvitid
      721 paspqspesv dlvneelkgk vlglsrdpak vaeededddg gimmrskets spgtddvftp
      781 apsdspssqr iqrclsdpgp hpepgegepf fpkgq
//
LOCUS       NP_001295224             485 aa            linear   PRI 20-NOV-2025
DEFINITION  glycylpeptide N-tetradecanoyltransferase 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001295224 XP_005252700
VERSION     NP_001295224.1
DBSOURCE    REFSEQ: accession NM_001308295.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Zhang,T., Goel,A., Xu,X., Wu,Y., Tang,E., Zhang,F., Li,Y., Li,H.,
            Cai,Y. and Weng,W.
  TITLE     N-mytistoyltransferase 1 and 2 are potential tumor suppressors and
            novel targets of miR-182 in human non-small cell lung carcinomas
  JOURNAL   Lung Cancer 171, 70-81 (2022)
   PUBMED   35930829
  REMARK    GeneRIF: N-mytistoyltransferase 1 and 2 are potential tumor
            suppressors and novel targets of miR-182 in human non-small cell
            lung carcinomas.
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Seaton,K.E. and Smith,C.D.
  TITLE     N-Myristoyltransferase isozymes exhibit differential specificity
            for human immunodeficiency virus type 1 Gag and Nef
  JOURNAL   J Gen Virol 89 (Pt 1), 288-296 (2008)
   PUBMED   18089753
  REMARK    GeneRIF: Nef is preferentially myristoylated by NMT2, suggesting
            that selective inhibition of NMT2 may provide a novel means of
            blocking HIV virulence.
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Pal,R., Reitz,M.S. Jr., Tschachler,E., Gallo,R.C.,
            Sarngadharan,M.G. and Veronese,F.D.
  TITLE     Myristoylation of gag proteins of HIV-1 plays an important role in
            virus assembly
  JOURNAL   AIDS Res Hum Retroviruses 6 (6), 721-730 (1990)
   PUBMED   2194551
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Bryant,M. and Ratner,L.
  TITLE     Myristoylation-dependent replication and assembly of human
            immunodeficiency virus 1
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 523-527 (1990)
   PUBMED   2405382
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Tashiro,A., Shoji,S. and Kubota,Y.
  TITLE     Antimyristoylation of the gag proteins in the human
            immunodeficiency virus-infected cells with N-myristoyl glycinal
            diethylacetal resulted in inhibition of virus production
  JOURNAL   Biochem Biophys Res Commun 165 (3), 1145-1154 (1989)
   PUBMED   2692561
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Goddard,C., Aquino,A., Glazer,R.I. and Felsted,R.L.
  TITLE     Chemical characterization of p17gag from human immunodeficiency
            virus as an N-terminally myristoylated protein
  JOURNAL   Eur J Biochem 182 (2), 323-326 (1989)
   PUBMED   2737204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB465189.1, AF043325.1,
            AK094904.1, AL590365.14 and AF086423.1.
            
            On Apr 27, 2015 this sequence version replaced XP_005252700.1.
            
            Summary: This gene encodes one of two N-myristoyltransferase
            proteins. N-terminal myristoylation is a lipid modification that is
            involved in regulating the function and localization of signaling
            proteins. The encoded protein catalyzes the addition of a myristoyl
            group to the N-terminal glycine residue of many signaling proteins,
            including the human immunodeficiency virus type 1 (HIV-1) proteins,
            Gag and Nef. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (2) includes an alternate exon
            which results in the use of an alternate start codon and a
            frameshifted 5' coding region, compared to variant 1. The encoded
            isoform (2) has a shorter and distinct N-terminus, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.234355.1,
                                           SRR1803615.44610.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..485
                     /product="glycylpeptide N-tetradecanoyltransferase 2
                     isoform 2"
                     /EC_number="2.3.1.97"
                     /note="NMT 2; type II N-myristoyltransferase; peptide
                     N-myristoyltransferase 2; myristoyl-CoA:protein
                     N-myristoyltransferase 2; protein-lysine
                     myristoyltransferase NMT2"
                     /calculated_mol_wt=56586
     Region          106..473
                     /region_name="NMT1"
                     /note="N-myristoyl transferase [Lipid metabolism];
                     COG5092"
                     /db_xref="CDD:227423"
     CDS             1..485
                     /gene="NMT2"
                     /coded_by="NM_001308295.2:164..1621"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76284.1"
                     /db_xref="GeneID:9397"
                     /db_xref="HGNC:HGNC:7858"
                     /db_xref="MIM:603801"
ORIGIN      
        1 mrrrrstpke vlegiwepkr krrnrrekrr nqipeapsqt rhliprrlkf sslrnttpsg
       61 srfqreqpwn psvpmqklqd iqramellsa cqgparnide aakhryqfwd tqpvpkldev
      121 itshgaiepd kdnvrqepys lpqgfmwdtl dlsdaevlke lytllnenyv edddnmfrfd
      181 yspefllwal rppgwllqwh cgvrvssnkk lvgfisaipa niriydsvkk mveinflcvh
      241 kklrskrvap vlireitrrv nlegifqavy tagvvlpkpi atcrywhrsl nprklvevkf
      301 shlsrnmtlq rtmklyrlpd vtktsglrpm epkdiksvre lintylkqfh lapvmdeeev
      361 ahwflprehi idtfvvespn gkltdflsfy tlpstvmhhp ahkslkaays fynihtetpl
      421 ldlmsdalil akskgfdvfn aldlmenktf leklkfgigd gnlqyylynw rcpgtdsekv
      481 glvlq
//
LOCUS       NP_004623                398 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein mS29 isoform 1 [Homo sapiens].
ACCESSION   NP_004623
VERSION     NP_004623.1
DBSOURCE    REFSEQ: accession NM_004632.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Smith,T.B., Kopajtich,R., Demain,L.A.M., Rea,A., Thomas,H.B.,
            Schiff,M., Beetz,C., Joss,S., Conway,G.S., Shukla,A., Yeole,M.,
            Radhakrishnan,P., Azzouz,H., Ben Chehida,A., Elmaleh-Berges,M.,
            Glasgow,R.I.C., Thompson,K., Olahova,M., He,L., Jenkinson,E.M.,
            Jahic,A., Belyantseva,I.A., Barzik,M., Urquhart,J.E.,
            O'Sullivan,J., Williams,S.G., Bhaskar,S.S., Carrera,S.,
            Blakes,A.J.M., Banka,S., Yue,W.W., Ellingford,J.M., Houlden,H.,
            Munro,K.J., Friedman,T.B., Taylor,R.W., Prokisch,H., O'Keefe,R.T.
            and Newman,W.G.
  CONSRTM   DDD Study
  TITLE     Bi-allelic variants in DAP3 result in reduced assembly of the
            mitoribosomal small subunit with altered apoptosis and a
            Perrault-syndrome-spectrum phenotype
  JOURNAL   Am J Hum Genet 112 (1), 59-74 (2025)
   PUBMED   39701103
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Tan,S., Zhang,X., Guo,X., Pan,G., Yan,L., Ding,Z., Li,R., Wang,D.,
            Yan,Y., Dong,Z. and Li,T.
  TITLE     DAP3 promotes mitochondrial activity and tumour progression in
            hepatocellular carcinoma by regulating MT-ND5 expression
  JOURNAL   Cell Death Dis 15 (7), 540 (2024)
   PUBMED   39080251
  REMARK    GeneRIF: DAP3 promotes mitochondrial activity and tumour
            progression in hepatocellular carcinoma by regulating MT-ND5
            expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Sui,L., Zeng,J., Zhao,H., Ye,L., Martin,T.A., Sanders,A.J.,
            Ruge,F., Jiang,A., Dou,Q.P., Hargest,R., Song,X. and Jiang,W.G.
  TITLE     Death associated protein-3 (DAP3) and DAP3 binding cell death
            enhancer-1 (DELE1) in human colorectal cancer, and their impacts on
            clinical outcome and chemoresistance
  JOURNAL   Int J Oncol 62 (1) (2023)
   PUBMED   36382667
  REMARK    GeneRIF: Death associated protein3 (DAP3) and DAP3 binding cell
            death enhancer1 (DELE1) in human colorectal cancer, and their
            impacts on clinical outcome and chemoresistance.
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Han,M.J., Chiu,D.T. and Koc,E.C.
  TITLE     Regulation of mitochondrial ribosomal protein S29 (MRPS29)
            expression by a 5'-upstream open reading frame
  JOURNAL   Mitochondrion 10 (3), 274-283 (2010)
   PUBMED   20079882
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Morgan,C.J., Jacques,C., Savagner,F., Tourmen,Y., Mirebeau,D.P.,
            Malthiery,Y. and Reynier,P.
  TITLE     A conserved N-terminal sequence targets human DAP3 to mitochondria
  JOURNAL   Biochem Biophys Res Commun 280 (1), 177-181 (2001)
   PUBMED   11162496
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Hulkko,S.M., Wakui,H. and Zilliacus,J.
  TITLE     The pro-apoptotic protein death-associated protein 3 (DAP3)
            interacts with the glucocorticoid receptor and affects the receptor
            function
  JOURNAL   Biochem J 349 Pt 3 (Pt 3), 885-893 (2000)
   PUBMED   10903152
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Kissil,J.L. and Kimchi,A.
  TITLE     Assignment of death associated protein 3 (DAP3) to human chromosome
            1q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 252 (1997)
   PUBMED   9284927
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Kissil,J.L., Deiss,L.P., Bayewitch,M., Raveh,T., Khaspekov,G. and
            Kimchi,A.
  TITLE     Isolation of DAP3, a novel mediator of interferon-gamma-induced
            cell death
  JOURNAL   J Biol Chem 270 (46), 27932-27936 (1995)
   PUBMED   7499268
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162734.15, BC107487.1 and
            BQ183744.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 28S subunit protein that also
            participates in apoptotic pathways which are initiated by tumor
            necrosis factor-alpha, Fas ligand, and gamma interferon. This
            protein potentially binds ATP/GTP and might be a functional partner
            of the mitoribosomal protein S27. Multiple alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. Pseudogenes corresponding to this gene are found on
            chromosomes 1q and 2q. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (1). Variants 1, 2 and 3 encode the same isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.210349.1,
                                           SRR1163655.119506.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000368336.10/
                                                  ENSP00000357320.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..398
                     /product="small ribosomal subunit protein mS29 isoform 1"
                     /note="mitochondrial 28S ribosomal protein S29; 28S
                     ribosomal protein S29, mitochondrial; ionizing radiation
                     resistance conferring protein; mitochondrial small
                     ribosomal subunit protein mS29"
                     /calculated_mol_wt=45435
     Region          39..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51398.1)"
     Region          99..393
                     /region_name="DAP3"
                     /note="Mitochondrial ribosomal death-associated protein 3;
                     pfam10236"
                     /db_xref="CDD:431160"
     Site            175
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51398.1)"
     Site            207
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51398.1)"
     CDS             1..398
                     /gene="DAP3"
                     /gene_synonym="bMRP-10; DAP-3; MRP-S29; MRPS29; mS29;
                     PRLTS7; S29mt"
                     /coded_by="NM_004632.4:92..1288"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1120.1"
                     /db_xref="GeneID:7818"
                     /db_xref="HGNC:HGNC:2673"
                     /db_xref="MIM:602074"
ORIGIN      
        1 mmlkgitrli srihkldpgr flhmgtqarq siaahldnqv pvespraisr tnendpakhg
       61 dqhegqhyni spqdletvfp hglpprfvmq vktfseaclm vrkpalellh ylkntsfayp
      121 airyllygek gtgktlslch vihfcakqdw lilhipdahl wvkncrdllq ssynkqrfdq
      181 pleastwlkn fkttnerfln qikvqekyvw nkrestekgs plgevveqgi trvrnatdav
      241 givlkelkrq sslgmfhllv avdginalwg rttlkredks piapeelalv hnlrkmmknd
      301 whggaivsal sqtgslfkpr kaylpqellg kegfdaldpf ipilvsnynp kefesciqyy
      361 lennwlqhek apteegkkel lflsnanpsl lerhcayl
//
LOCUS       NP_001011550             317 aa            linear   PRI 20-NOV-2025
DEFINITION  melanoma-associated antigen 4 [Homo sapiens].
ACCESSION   NP_001011550
VERSION     NP_001011550.1
DBSOURCE    REFSEQ: accession NM_001011550.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Hashimoto,K., Nishimura,S., Shinyashiki,Y., Ito,T., Kakinoki,R. and
            Akagi,M.
  TITLE     Involvement of NY-ESO-1 and MAGE-A4 in the pathogenesis of desmoid
            tumors
  JOURNAL   Medicine (Baltimore) 102 (22), e33908 (2023)
   PUBMED   37266606
  REMARK    GeneRIF: Involvement of NY-ESO-1 and MAGE-A4 in the pathogenesis of
            desmoid tumors.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Cai,R., Zhao,F., Zhou,H., Wang,Z., Lin,D., Huang,L., Xie,W.,
            Chen,J., Zhou,L., Zhang,N. and Huang,C.
  TITLE     A tumor-associated autoantibody panel for the detection of
            non-small cell lung cancer
  JOURNAL   Front Oncol 12, 1056572 (2022)
   PUBMED   36531074
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Hashimoto,K., Nishimura,S., Ito,T., Oka,N., Kakinoki,R. and
            Akagi,M.
  TITLE     Clinicopathological assessment of cancer/testis antigens NY-ESO-1
            and MAGE-A4 in osteosarcoma
  JOURNAL   Eur J Histochem 66 (3), 3377 (2022)
   PUBMED   35736245
  REMARK    GeneRIF: Clinicopathological assessment of cancer/testis antigens
            NYESO1 and MAGEA4 in osteosarcoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Brasseur,F., Rimoldi,D., Lienard,D., Lethe,B., Carrel,S.,
            Arienti,F., Suter,L., Vanwijck,R., Bourlond,A., Humblet,Y. et al.
  TITLE     Expression of MAGE genes in primary and metastatic cutaneous
            melanoma
  JOURNAL   Int J Cancer 63 (3), 375-380 (1995)
   PUBMED   7591235
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Rogner,U.C., Wilke,K., Steck,E., Korn,B. and Poustka,A.
  TITLE     The melanoma antigen gene (MAGE) family is clustered in the
            chromosomal band Xq28
  JOURNAL   Genomics 29 (3), 725-731 (1995)
   PUBMED   8575766
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Imai,Y., Shichijo,S., Yamada,A., Katayama,T., Yano,H. and Itoh,K.
  TITLE     Sequence analysis of the MAGE gene family encoding human
            tumor-rejection antigens
  JOURNAL   Gene 160 (2), 287-290 (1995)
   PUBMED   7642112
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Ding,M., Beck,R.J., Keller,C.J. and Fenton,R.G.
  TITLE     Cloning and analysis of MAGE-1-related genes
  JOURNAL   Biochem Biophys Res Commun 202 (1), 549-555 (1994)
   PUBMED   8037761
REFERENCE   10 (residues 1 to 317)
  AUTHORS   De Plaen,E., Arden,K., Traversari,C., Gaforio,J.J., Szikora,J.P.,
            De Smet,C., Brasseur,F., van der Bruggen,P., Lethe,B., Lurquin,C.
            et al.
  TITLE     Structure, chromosomal localization, and expression of 12 genes of
            the MAGE family
  JOURNAL   Immunogenetics 40 (5), 360-369 (1994)
   PUBMED   7927540
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB120212.1 and AF274855.3.
            
            Summary: This gene is a member of the MAGEA gene family. The
            members of this family encode proteins with 50 to 80% sequence
            identity to each other. The promoters and first exons of the MAGEA
            genes show considerable variability, suggesting that the existence
            of this gene family enables the same function to be expressed under
            different transcriptional controls. The MAGEA genes are clustered
            at chromosomal location Xq28. They have been implicated in some
            hereditary disorders, such as dyskeratosis congenita. Several
            variants encoding the same protein have been found for this gene.
            [provided by RefSeq, Aug 2020].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 5. All twelve variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017723.1, AK313862.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..317
                     /product="melanoma-associated antigen 4"
                     /note="cancer/testis antigen family 1, member 4; MAGE-4
                     antigen; MAGE-41 antigen; MAGE-X2 antigen; cancer/testis
                     antigen 1.4; melanoma antigen family A, 4; melanoma
                     antigen family A4"
                     /calculated_mol_wt=34768
     Region          1..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43358.2)"
     Region          5..97
                     /region_name="MAGE_N"
                     /note="Melanoma associated antigen family N terminal;
                     pfam12440"
                     /db_xref="CDD:463582"
     Region          131..281
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     CDS             1..317
                     /gene="MAGEA4"
                     /gene_synonym="CT1.4; MAGE-41; MAGE-X2; MAGE4; MAGE4A;
                     MAGE4B"
                     /coded_by="NM_001011550.1:207..1160"
                     /db_xref="CCDS:CCDS14702.1"
                     /db_xref="GeneID:4103"
                     /db_xref="HGNC:HGNC:6802"
                     /db_xref="MIM:300175"
ORIGIN      
        1 msseqksqhc kpeegveaqe ealglvgaqa ptteeqeaav ssssplvpgt leevpaaesa
       61 gppqspqgas alpttisftc wrqpnegsss qeeegpstsp daeslfreal snkvdelahf
      121 llrkyrakel vtkaemlerv iknykrcfpv ifgkaseslk mifgidvkev dpasntytlv
      181 tclglsydgl lgnnqifpkt glliivlgti amegdsasee eiweelgvmg vydgrehtvy
      241 geprklltqd wvqenyleyr qvpgsnpary eflwgprala etsyvkvleh vvrvnarvri
      301 aypslreaal leeeegv
//
LOCUS       NP_001160166             489 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-3 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001160166
VERSION     NP_001160166.1
DBSOURCE    REFSEQ: accession NM_001166694.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Chmielowiec,K., Chmielowiec,J., Stronska-Pluta,A., Trybek,G.,
            Smiarowska,M., Suchanecka,A., Wozniak,G., Jaron,A. and Grzywacz,A.
  TITLE     Association of Polymorphism CHRNA5 and CHRNA3 Gene in People
            Addicted to Nicotine
  JOURNAL   Int J Environ Res Public Health 19 (17), 10478 (2022)
   PUBMED   36078193
  REMARK    GeneRIF: Association of Polymorphism CHRNA5 and CHRNA3 Gene in
            People Addicted to Nicotine.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Kitazaki,Y., Ikawa,M., Kishitani,T., Kamisawa,T., Nakane,S.,
            Nakamoto,Y. and Hamano,T.
  TITLE     Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies
  JOURNAL   Intern Med 60 (14), 2307-2313 (2021)
   PUBMED   33583893
  REMARK    GeneRIF: Progressive Encephalomyelitis with Rigidity and Myoclonus
            (PERM)-like Symptoms Associated with Anti-ganglionic Acetylcholine
            Receptor Antibodies.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Shibao,C.A., Joos,K., Phillips,J.A. 3rd, Cogan,J., Newman,J.H.,
            Hamid,R., Meiler,J., Capra,J., Sheehan,J., Vetrini,F., Yang,Y.,
            Black,B., Diedrich,A., Roberston,D. and Biaggioni,I.
  TITLE     Familial Autonomic Ganglionopathy Caused by Rare CHRNA3 Genetic
            Variants
  JOURNAL   Neurology 97 (2), e145-e155 (2021)
   PUBMED   33947782
  REMARK    GeneRIF: Familial Autonomic Ganglionopathy Caused by Rare CHRNA3
            Genetic Variants.
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Yi,X., Li,W., Wang,Y., Chen,X., Ye,F., Sun,G. and Chen,J.
  TITLE     The relationship between CHRNA5/A3/B4 gene cluster polymorphisms
            and lung cancer risk: An updated meta-analysis and systematic
            review
  JOURNAL   Medicine (Baltimore) 100 (6), e24355 (2021)
   PUBMED   33578531
  REMARK    GeneRIF: The relationship between CHRNA5/A3/B4 gene cluster
            polymorphisms and lung cancer risk: An updated meta-analysis and
            systematic review.
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Wang,F., Gerzanich,V., Wells,G.B., Anand,R., Peng,X., Keyser,K. and
            Lindstrom,J.
  TITLE     Assembly of human neuronal nicotinic receptor alpha5 subunits with
            alpha3, beta2, and beta4 subunits
  JOURNAL   J Biol Chem 271 (30), 17656-17665 (1996)
   PUBMED   8663494
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Raimondi,E., Rubboli,F., Moralli,D., Chini,B., Fornasari,D.,
            Tarroni,P., De Carli,L. and Clementi,F.
  TITLE     Chromosomal localization and physical linkage of the genes encoding
            the human alpha 3, alpha 5, and beta 4 neuronal nicotinic receptor
            subunits
  JOURNAL   Genomics 12 (4), 849-850 (1992)
   PUBMED   1572664
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Eng,C.M., Kozak,C.A., Beaudet,A.L. and Zoghbi,H.Y.
  TITLE     Mapping of multiple subunits of the neuronal nicotinic
            acetylcholine receptor to chromosome 15 in man and chromosome 9 in
            mouse
  JOURNAL   Genomics 9 (2), 278-282 (1991)
   PUBMED   2004777
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Mihovilovic,M. and Roses,A.D.
  TITLE     Expression of mRNAs in human thymus coding for the alpha 3 subunit
            of a neuronal acetylcholine receptor
  JOURNAL   Exp Neurol 111 (2), 175-180 (1991)
   PUBMED   1989896
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Papke,R.L. and Heinemann,S.F.
  TITLE     The role of the beta 4-subunit in determining the kinetic
            properties of rat neuronal nicotinic acetylcholine alpha
            3-receptors
  JOURNAL   J Physiol 440, 95-112 (1991)
   PUBMED   1725184
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Fornasari,D., Chini,B., Tarroni,P. and Clementi,F.
  TITLE     Molecular cloning of human neuronal nicotinic receptor alpha
            3-subunit
  JOURNAL   Neurosci Lett 111 (3), 351-356 (1990)
   PUBMED   2336208
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC006114.1.
            
            Summary: This locus encodes a member of the nicotinic acetylcholine
            receptor family of proteins. Members of this family of proteins
            form pentameric complexes comprised of both alpha and beta
            subunits. This locus encodes an alpha-type subunit, as it contains
            characteristic adjacent cysteine residues. The encoded protein is a
            ligand-gated ion channel that likely plays a role in
            neurotransmission. Polymorphisms in this gene have been associated
            with an increased risk of smoking initiation and an increased
            susceptibility to lung cancer. Alternatively spliced transcript
            variants have been described. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (2) differs in the 3' coding
            region and 3' UTR, compared to variant 1. The resulting isoform (2)
            has a distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006114.1, BT006646.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q25.1"
     Protein         1..489
                     /product="neuronal acetylcholine receptor subunit alpha-3
                     isoform 2 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     3; neuronal nicotinic acetylcholine receptor, alpha3
                     subunit; cholinergic receptor, nicotinic, alpha 3
                     (neuronal); cholinergic receptor, nicotinic alpha 3"
                     /calculated_mol_wt=52462
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3193
     Region          35..241
                     /region_name="LGIC_ECD_nAChR_A3"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit alpha 3 (CHRNA3); cd19016"
                     /db_xref="CDD:349817"
     Site            55
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            order(70,72,78..79,86,108,110,119..120,122,124..125,129,
                     131..132,136..138,140,150,152,154,158,180,240)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349817"
     Region          159..173
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349817"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Region          248..466
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            251..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            269..285
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            308..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32297.4)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04757; propagated from
                     UniProtKB/Swiss-Prot (P32297.4)"
     CDS             1..489
                     /gene="CHRNA3"
                     /gene_synonym="BAIPRCK; LNCR2; NACHRA3; PAOD2"
                     /coded_by="NM_001166694.2:203..1672"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS53964.1"
                     /db_xref="GeneID:1136"
                     /db_xref="HGNC:HGNC:1957"
                     /db_xref="MIM:118503"
ORIGIN      
        1 mgsgplslpl alspprllll lllsllpvar aseaehrlfe rlfedyneii rpvanvsdpv
       61 iihfevsmsq lvkvdevnqi metnlwlkqi wndyklkwnp sdyggaefmr vpaqkiwkpd
      121 ivlynnavgd fqvddktkal lkytgevtwi ppaifkssck idvtyfpfdy qnctmkfgsw
      181 sydkakidlv ligssmnlkd ywesgewaii kapgykhdik yncceeiypd ityslyirrl
      241 plfytinlii pcllisfltv lvfylpsdcg ekvtlcisvl lsltvfllvi tetipstslv
      301 ipligeyllf tmifvtlsiv itvfvlnvhy rtptthtmps wvktvflnll prvmfmtrpt
      361 snegnaqkpr plygaelsnl ncfsraeskg ckegypcqdg mcgychhrri kisnfsanlt
      421 rssssesvda vlslsalspe ikeaiqsvky iaenmkaqne akeeqkaqei qqlkrkekst
      481 etsdqepgl
//
LOCUS       NP_001354683             367 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform k [Homo sapiens].
ACCESSION   NP_001354683
VERSION     NP_001354683.1
DBSOURCE    REFSEQ: accession NM_001367754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.207749.1,
                                           SRR1660809.262125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..367
                     /product="rab5 GDP/GTP exchange factor isoform k"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=42633
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..359
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..367
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367754.1:78..1181"
                     /note="isoform k is encoded by transcript variant 38"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlv
      361 mlccgfh
//
LOCUS       NP_056016                746 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosome biogenesis protein BOP1 [Homo sapiens].
ACCESSION   NP_056016
VERSION     NP_056016.1
DBSOURCE    REFSEQ: accession NM_015201.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 746)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 746)
  AUTHORS   Li,J., Hu,W., Zhang,R., Chen,W., Li,X. and Tang,Z.
  TITLE     PDGF-C promotes cell proliferation partially via downregulating
            BOP1
  JOURNAL   Cell Biol Int 47 (12), 1942-1949 (2023)
   PUBMED   37615370
  REMARK    GeneRIF: PDGF-C promotes cell proliferation partially via
            downregulating BOP1.
REFERENCE   3  (residues 1 to 746)
  AUTHORS   Wu,X., Jing,Z., Huang,T. and Jing,Y.
  TITLE     BOP1 Promotes Prostate Cancer through the DUSP6/MAPK Pathway
  JOURNAL   Arch Esp Urol 76 (6), 445-453 (2023)
   PUBMED   37681336
  REMARK    GeneRIF: BOP1 Promotes Prostate Cancer through the DUSP6/MAPK
            Pathway.
REFERENCE   4  (residues 1 to 746)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 746)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 746)
  AUTHORS   Strezoska,Z., Pestov,D.G. and Lau,L.F.
  TITLE     Functional inactivation of the mouse nucleolar protein Bop1
            inhibits multiple steps in pre-rRNA processing and blocks cell
            cycle progression
  JOURNAL   J Biol Chem 277 (33), 29617-29625 (2002)
   PUBMED   12048210
REFERENCE   7  (residues 1 to 746)
  AUTHORS   Pestov,D.G., Stockelman,M.G., Strezoska,Z. and Lau,L.F.
  TITLE     ERB1, the yeast homolog of mammalian Bop1, is an essential gene
            required for maturation of the 25S and 5.8S ribosomal RNAs
  JOURNAL   Nucleic Acids Res 29 (17), 3621-3630 (2001)
   PUBMED   11522832
REFERENCE   8  (residues 1 to 746)
  AUTHORS   Pestov,D.G., Strezoska,Z. and Lau,L.F.
  TITLE     Evidence of p53-dependent cross-talk between ribosome biogenesis
            and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S
            transition
  JOURNAL   Mol Cell Biol 21 (13), 4246-4255 (2001)
   PUBMED   11390653
REFERENCE   9  (residues 1 to 746)
  AUTHORS   Nakatsura,T., Senju,S., Yamada,K., Jotsuka,T., Ogawa,M. and
            Nishimura,Y.
  TITLE     Gene cloning of immunogenic antigens overexpressed in pancreatic
            cancer
  JOURNAL   Biochem Biophys Res Commun 281 (4), 936-944 (2001)
   PUBMED   11237751
REFERENCE   10 (residues 1 to 746)
  AUTHORS   Zhang,Y., Koushik,S., Dai,R. and Mivechi,N.F.
  TITLE     Structural organization and promoter analysis of murine heat shock
            transcription factor-1 gene
  JOURNAL   J Biol Chem 273 (49), 32514-32521 (1998)
   PUBMED   9829985
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA510177.1, BQ711345.1, BC013787.1, AI937005.1 and AC145291.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.548849.1, BC013980.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000569669.6/ ENSP00000455106.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..746
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..746
                     /product="ribosome biogenesis protein BOP1"
                     /note="block of proliferation 1"
                     /calculated_mol_wt=83499
     Region          1..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14137.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14137.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14137.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14137.2)"
     Region          144..402
                     /region_name="BOP1NT"
                     /note="BOP1NT (NUC169) domain; pfam08145"
                     /db_xref="CDD:462371"
     Region          265..427
                     /region_name="Sufficient for nucleolar localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          <408..744
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          411..450
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          417..453
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          452..492
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          457..556
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          532..576
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          577..615
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          583..613
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          618..657
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          623..660
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          661..700
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          666..711
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          716..746
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14137.2)"
     Region          721..745
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..746
                     /gene="BOP1"
                     /coded_by="NM_015201.5:69..2309"
                     /db_xref="CCDS:CCDS6418.2"
                     /db_xref="GeneID:23246"
                     /db_xref="HGNC:HGNC:15519"
                     /db_xref="MIM:610596"
ORIGIN      
        1 magsrgagrt aapsvrpekr rsepelepep epeppllcts plshstgsds gvsdseesvf
       61 sgledsgsds sedddegdee gedgalddeg hsgikkttee qvqastpcpr temasarigd
      121 eyaedssdee dirntvgnvp lewyddfphv gydldgrriy kplrtrdeld qfldkmddpd
      181 ywrtvqdpmt grdlrltdeq valvrrlqsg qfgdvgfnpy epavdffsgd vmihpvtnrp
      241 adkrsfipsl vekekvsrmv haikmgwiqp rrprdptpsf ydlwaqedpn avlgrhkmhv
      301 papklalpgh aesynpppey llseeerlaw eqqepgerkl sflprkfpsl ravpaygrfi
      361 qerfercldl ylcprqrkmr vnvdpedlip klprprdlqp fptcqalvyr ghsdlvrcls
      421 vspggqwlvs gsddgslrlw evatarcvrt vpvggvvksv awnpspavcl vaaavedsvl
      481 llnpalgdrl vagstdqlls afvppeeppl qparwlease eerqvglrlr ichgkpvtqv
      541 twhgrgdyla vvlatqghtq vlihqlsrrr sqspfrrshg qvqrvafhpa rpfllvasqr
      601 svrlyhllrq eltkklmpnc kwvsslavhp agdnvicgsy dsklvwfdld lstkpyrmlr
      661 hhkkalrava fhpryplfas gsddgsvivc hgmvyndllq npllvpvkvl kghvltrdlg
      721 vldvifhptq pwvfssgadg tvrlft
//
LOCUS       NP_001122394             662 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor beta activator LRRC32 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001122394
VERSION     NP_001122394.1
DBSOURCE    REFSEQ: accession NM_001128922.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Ma,J., Chen,Y., Li,T., Cao,Y., Hu,B., Liu,Y., Zhang,Y., Li,X.,
            Liu,J., Zhang,W., Niu,H., Gao,J., Zhang,Z., Yue,K., Wang,J.,
            Bao,G., Wang,C., Wang,P.G., Zou,T. and Xie,S.
  TITLE     Suppression of lysosome metabolism-meditated GARP/TGF-beta1
            complexes specifically depletes regulatory T cells to inhibit
            breast cancer metastasis
  JOURNAL   Oncogene 43 (25), 1930-1940 (2024)
   PUBMED   38698265
  REMARK    GeneRIF: Suppression of lysosome metabolism-meditated
            GARP/TGF-beta1 complexes specifically depletes regulatory T cells
            to inhibit breast cancer metastasis.
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Zhang,X., Sharma,P., Maschmeyer,P., Hu,Y., Lou,M., Kim,J.,
            Fujii,H., Unutmaz,D., Schwabe,R.F. and Winau,F.
  TITLE     GARP on hepatic stellate cells is essential for the development of
            liver fibrosis
  JOURNAL   J Hepatol 79 (5), 1214-1225 (2023)
   PUBMED   37348791
  REMARK    GeneRIF: GARP on hepatic stellate cells is essential for the
            development of liver fibrosis.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Cai,H., Liu,Y., Dong,X., Jiang,F., Li,H., Ouyang,S., Yin,W., He,T.,
            Zeng,Q. and Yang,H.
  TITLE     Analysis of LAP+ and GARP+ Treg subsets in peripheral blood of
            patients with neuromyelitis optica spectrum disorders
  JOURNAL   Neurol Sci 44 (5), 1739-1747 (2023)
   PUBMED   36683084
  REMARK    GeneRIF: Analysis of LAP[+] and GARP[+] Treg subsets in peripheral
            blood of patients with neuromyelitis optica spectrum disorders.
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Lahimchi,M.R., Eslami,M. and Yousefi,B.
  TITLE     New insight into GARP striking role in cancer progression:
            application for cancer therapy
  JOURNAL   Med Oncol 40 (1), 33 (2022)
   PUBMED   36460874
  REMARK    GeneRIF: New insight into GARP striking role in cancer progression:
            application for cancer therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Maire,G., Forus,A., Foa,C., Bjerkehagen,B., Mainguene,C.,
            Kresse,S.H., Myklebost,O. and Pedeutour,F.
  TITLE     11q13 alterations in two cases of hibernoma: large heterozygous
            deletions and rearrangement breakpoints near GARP in 11q13.5
  JOURNAL   Genes Chromosomes Cancer 37 (4), 389-395 (2003)
   PUBMED   12800150
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Roubin,R., Pizette,S., Ollendorff,V., Planche,J., Birnbaum,D. and
            Delapeyriere,O.
  TITLE     Structure and developmental expression of mouse Garp, a gene
            encoding a new leucine-rich repeat-containing protein
  JOURNAL   Int J Dev Biol 40 (3), 545-555 (1996)
   PUBMED   8840187
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Ollendorff,V., Noguchi,T., deLapeyriere,O. and Birnbaum,D.
  TITLE     The GARP gene encodes a new member of the family of leucine-rich
            repeat-containing proteins
  JOURNAL   Cell Growth Differ 5 (2), 213-219 (1994)
   PUBMED   8180135
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Ollendorff,V., Szepetowski,P., Mattei,M.G., Gaudray,P. and
            Birnbaum,D.
  TITLE     New gene in the homologous human 11q13-q14 and mouse 7F chromosomal
            regions
  JOURNAL   Mamm Genome 2 (3), 195-200 (1992)
   PUBMED   1543912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070079.1, BI010671.1,
            BC052210.1, DA591993.1 and AP001189.5.
            
            Summary: This gene encodes a type I membrane protein which contains
            20 leucine-rich repeats. Alterations in the chromosomal region
            11q13-11q14 are involved in several pathologies. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-4 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070079.1, SRR1660809.91003.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260061.9/ ENSP00000260061.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..662
                     /product="transforming growth factor beta activator LRRC32
                     isoform a precursor"
                     /note="garpin; glycoprotein A repetitions predominant;
                     leucine-rich repeat-containing protein 32; transforming
                     growth factor beta activator LRRC32"
                     /calculated_mol_wt=70148
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1849
     Region          19..277
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     mat_peptide     20..662
                     /product="transforming growth factor beta activator LRRC32
                     isoform a"
                     /calculated_mol_wt=69949
     Site            order(28,31,33,36,38,51,54,56,59,61,75,78,80,83,85,99,102,
                     104,107,109,126,129,131,134,136,151,154,156,159,161,175,
                     178,180,183,185,199,202,204,207,209,220,223,225,228,230,
                     245,248,250,253,255,267,270,272,275,277)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          31..50
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(34..35,82,133,158,206,224,226,249,271)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          50..73
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          51..74
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          74..95
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          75..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          98..119
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          99..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          125..145
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          126..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="LRR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..219
                     /region_name="LRR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          199..219
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          220..244
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..240
                     /region_name="LRR 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          244..265
                     /region_name="LRR 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          245..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          266..286
                     /region_name="LRR 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          290..>574
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          316..339
                     /region_name="LRR 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          317..340
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          340..363
                     /region_name="LRR 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          341..364
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          364..385
                     /region_name="LRR 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          365..387
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          387..408
                     /region_name="LRR 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          388..411
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          411..432
                     /region_name="LRR 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          412..444
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          444..465
                     /region_name="LRR 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          445..463
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          467..488
                     /region_name="LRR 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          468..492
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          492..513
                     /region_name="LRR 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          493..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <496..654
                     /region_name="PLN03150"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:178695"
     Region          515..536
                     /region_name="LRR 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          516..537
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          537..558
                     /region_name="LRR 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          538..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          563..575
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            628..648
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     CDS             1..662
                     /gene="LRRC32"
                     /gene_synonym="CPPRDD; D11S833E; GARP"
                     /coded_by="NM_001128922.2:139..2127"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS8245.1"
                     /db_xref="GeneID:2615"
                     /db_xref="HGNC:HGNC:4161"
                     /db_xref="MIM:137207"
ORIGIN      
        1 mrpqilllla lltlglaaqh qdkvpckmvd kkvscqvlgl lqvpsvlppd tetldlsgnq
       61 lrsilasplg fytalrhldl stneisflqp gafqalthle hlslahnrla matalsaggl
      121 gplprvtsld lsgnslysgl lerllgeaps lhtlslaens ltrltrhtfr dmpaleqldl
      181 hsnvlmdied gafeglprlt hlnlsrnslt cisdfslqql rvldlscnsi eafqtasqpq
      241 aefqltwldl renkllhfpd laalprliyl nlsnnlirlp tgppqdskgi hapsegwsal
      301 plsapsgnas grplsqllnl dlsyneieli pdsflehlts lcflnlsrnc lrtfearrlg
      361 slpclmlldl shnaletlel garalgslrt lllqgnalrd lppytfanla slqrlnlqgn
      421 rvspcggpde pgpsgcvafs gitslrslsl vdneiellra gaflhtplte ldlssnpgle
      481 vatgalggle aslevlalqg nglmvlqvdl pcficlkrln laenrlshlp awtqavslev
      541 ldlrnnsfsl lpgsamggle tslrrlylqg nplsccgngw laaqlhqgrv dvdatqdlic
      601 rfssqeevsl shvrpedcek gglkninlii iltfilvsai llttlaaccc vrrqkfnqqy
      661 ka
//
LOCUS       NP_004161                524 aa            linear   PRI 20-NOV-2025
DEFINITION  excitatory amino acid transporter 3 [Homo sapiens].
ACCESSION   NP_004161
VERSION     NP_004161.4
DBSOURCE    REFSEQ: accession NM_004170.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Krishna,G., Pillai,V.S., Gopi,P., Nair,A.S. and Veettil,M.V.
  TITLE     Epstein-Barr virus infection controls the concentration of the
            intracellular antioxidant glutathione by upregulation of the
            glutamate transporter EAAT3 in tumor cells
  JOURNAL   Virus Genes 59 (1), 55-66 (2023)
   PUBMED   36344769
  REMARK    GeneRIF: Epstein-Barr virus infection controls the concentration of
            the intracellular antioxidant glutathione by upregulation of the
            glutamate transporter EAAT3 in tumor cells.
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Xiong,J., Wang,N., Zhong,H.J., Cui,B.W., Cheng,S., Sun,R.,
            Chen,J.Y., Xu,P.P., Cai,G., Wang,L., Sun,X.J., Huang,J.Y. and
            Zhao,W.L.
  TITLE     SLC1A1 mediated glutamine addiction and contributed to natural
            killer T-cell lymphoma progression with immunotherapeutic potential
  JOURNAL   EBioMedicine 72, 103614 (2021)
   PUBMED   34628354
  REMARK    GeneRIF: SLC1A1 mediated glutamine addiction and contributed to
            natural killer T-cell lymphoma progression with immunotherapeutic
            potential.
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Qiu,B., Matthies,D., Fortea,E., Yu,Z. and Boudker,O.
  TITLE     Cryo-EM structures of excitatory amino acid transporter 3 visualize
            coupled substrate, sodium, and proton binding and transport
  JOURNAL   Sci Adv 7 (10) (2021)
   PUBMED   33658209
  REMARK    GeneRIF: Cryo-EM structures of excitatory amino acid transporter 3
            visualize coupled substrate, sodium, and proton binding and
            transport.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Zerangue,N. and Kavanaugh,M.P.
  TITLE     Interaction of L-cysteine with a human excitatory amino acid
            transporter
  JOURNAL   J Physiol 493 (Pt 2) (Pt 2), 419-423 (1996)
   PUBMED   8782106
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Shashidharan,P., Huntley,G.W., Meyer,T., Morrison,J.H. and
            Plaitakis,A.
  TITLE     Neuron-specific human glutamate transporter: molecular cloning,
            characterization and expression in human brain
  JOURNAL   Brain Res 662 (1-2), 245-250 (1994)
   PUBMED   7859077
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Arriza,J.L., Fairman,W.A., Wadiche,J.I., Murdoch,G.H.,
            Kavanaugh,M.P. and Amara,S.G.
  TITLE     Functional comparisons of three glutamate transporter subtypes
            cloned from human motor cortex
  JOURNAL   J Neurosci 14 (9), 5559-5569 (1994)
   PUBMED   7521911
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Kanai,Y., Stelzner,M., Nussberger,S., Khawaja,S., Hebert,S.C.,
            Smith,C.P. and Hediger,M.A.
  TITLE     The neuronal and epithelial human high affinity glutamate
            transporter. Insights into structure and mechanism of transport
  JOURNAL   J Biol Chem 269 (32), 20599-20606 (1994)
   PUBMED   7914198
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Smith,C.P., Weremowicz,S., Kanai,Y., Stelzner,M., Morton,C.C. and
            Hediger,M.A.
  TITLE     Assignment of the gene coding for the human high-affinity glutamate
            transporter EAAC1 to 9p24: potential role in dicarboxylic
            aminoaciduria and neurodegenerative disorders
  JOURNAL   Genomics 20 (2), 335-336 (1994)
   PUBMED   8020993
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA643262.1, U03506.1,
            AB008536.1, BQ008494.1 and BQ029108.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 27, 2005 this sequence version replaced NP_004161.3.
            
            Summary: This gene encodes a member of the high-affinity glutamate
            transporters that play an essential role in transporting glutamate
            across plasma membranes. In brain, these transporters are crucial
            in terminating the postsynaptic action of the neurotransmitter
            glutamate, and in maintaining extracellular glutamate
            concentrations below neurotoxic levels. This transporter also
            transports aspartate, and mutations in this gene are thought to
            cause dicarboxylicamino aciduria, also known as glutamate-aspartate
            transport defect. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.20740.1,
                                           SRR1660805.54195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262352.8/ ENSP00000262352.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.2"
     Protein         1..524
                     /product="excitatory amino acid transporter 3"
                     /note="excitatory amino acid carrier 1; neuronal and
                     epithelial glutamate transporter; sodium-dependent
                     glutamate/aspartate transporter 3; solute carrier family 1
                     (neuronal/epithelial high affinity glutamate transporter,
                     system Xag), member 1"
                     /calculated_mol_wt=56970
     Site            19..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Region          25..468
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     Site            43
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43005.2)"
     Site            62..82
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            94..114
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            178
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43005.2)"
     Site            195
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43005.2)"
     Site            206..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            239..266
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            287..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            354..380
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            441..462
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43005.2)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51906; propagated from
                     UniProtKB/Swiss-Prot (P43005.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51906; propagated from
                     UniProtKB/Swiss-Prot (P43005.2)"
     CDS             1..524
                     /gene="SLC1A1"
                     /gene_synonym="DCBXA; EAAC1; EAAT3; hEAAC1; SCZD18"
                     /coded_by="NM_004170.6:213..1787"
                     /db_xref="CCDS:CCDS6452.1"
                     /db_xref="GeneID:6505"
                     /db_xref="HGNC:HGNC:10939"
                     /db_xref="MIM:133550"
ORIGIN      
        1 mgkparkgce wkrflknnwv llstvaavvl gittgvlvre hsnlstlekf yfafpgeilm
       61 rmlkliilpl iissmitgva aldsnvsgki glravvyyfc ttliavilgi vlvvsikpgv
      121 tqkvgeiart gstpevstvd amldlirnmf penlvqacfq qyktkreevk ppsdpemnmt
      181 eesftavmtt aisknktkey kivgmysdgi nvlglivfcl vfglvigkmg ekgqilvdff
      241 nalsdatmki vqiimcympl gilfliagki ievedweifr klglymatvl tglaihsivi
      301 lpliyfivvr knpfrfamgm aqalltalmi ssssatlpvt frcaeennqv dkritrfvlp
      361 vgatinmdgt alyeavaavf iaqlndldlg igqiitisit atsasigaag vpqaglvtmv
      421 ivlsavglpa edvtliiavd wlldrfrtmv nvlgdafgtg iveklskkel eqmdvssevn
      481 ivnpfalest ildnedsdtk ksyvnggfav dksdtisftq tsqf
//
LOCUS       NP_001353148             853 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001353148 XP_016861309
VERSION     NP_001353148.1
DBSOURCE    REFSEQ: accession NM_001366219.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 853)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 853)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 853)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 853)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 853)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 853)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 853)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 853)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 853)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 853)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861309.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.27679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..853
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..853
                     /product="disks large homolog 1 isoform 12"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=95035
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..172
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          171..259
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(182..188,205,208,238,242,245..246)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          268..352
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(277..283,300,303,333,337,340..341)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          353..414
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          412..502
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(424..430,441,444,474,478,481..482)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          531..597
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(536,558..559,580)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(539,541,544,553,571..572,591,593..594)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          662..840
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..853
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366219.1:624..3185"
                     /note="isoform 12 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS93449.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kvngtdadye yeeitlergn
      181 sglgfsiagg tdnphigdds sifitkiitg gaaaqdgrlr vndcilrvne vdvrdvthsk
      241 avealkeags ivrlyvkrrk pvsekimeik likgpkglgf siaggvgnqh ipgdnsiyvt
      301 kiieggaahk dgklqigdkl lavnnvclee vtheeavtal kntsdfvylk vakptsmymn
      361 dgyappditn sssqpvdnhv spssflgqtp asparyspvs kavlgddeit reprkvvlhr
      421 gstglgfniv ggedgegifi sfilaggpad lsgelrkgdr iisvnsvdlr aasheqaaaa
      481 lknagqavti vaqyrpeeys rfeakihdlr eqmmnssiss gsgslrtsqk rslyvralfd
      541 ydktkdsglp sqglnfkfgd ilhvinasdd ewwqarqvtp dgesdevgvi pskrrvekke
      601 rarlktvkfn sktrdkgeip ddmgskglkh vtsnasdses syrgqeeyvl syepvnqqev
      661 nytrpviilg pmkdrinddl isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek
      721 diqehkfiea gqynnhlygt svqsvrevae kgkhcildvs gnaikrlqia qlypisifik
      781 pksmenimem nkrlteeqar ktferamkle qeftehftai vqgdtlediy nqvkqiieeq
      841 sgsyiwvpak ekl
//
LOCUS       NP_001186702             183 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-5 isoform 2 [Homo sapiens].
ACCESSION   NP_001186702
VERSION     NP_001186702.1
DBSOURCE    REFSEQ: accession NM_001199773.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Xie,S., Li,X., Yan,J., Yu,H., Chen,S. and Chen,K.
  TITLE     Knockdown of liver cancer cell-secreted exosomal PSMA5 controls
            macrophage polarization to restrain cancer progression by blocking
            JAK2/STAT3 signaling
  JOURNAL   Immun Inflamm Dis 12 (2), e1146 (2024)
   PUBMED   38415977
  REMARK    GeneRIF: Knockdown of liver cancer cell-secreted exosomal PSMA5
            controls macrophage polarization to restrain cancer progression by
            blocking JAK2/STAT3 signaling.
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 183)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI825400.1, AL390252.9 and
            H08369.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. Multiple alternatively spliced transcript variants
            encoding two distinct isoforms have been found for this gene.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (3) has an alternate 5' UTR exon,
            resulting in a downstream AUG start codon, as compared to variant
            1. The resulting isoform (2) is shorter at the N-terminus, as
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.1050164.1,
                                           SRR14372080.2074839.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..183
                     /product="proteasome subunit alpha type-5 isoform 2"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit zeta; proteasome subunit zeta;
                     proteasome zeta chain; macropain zeta chain;
                     multicatalytic endopeptidase complex zeta chain;
                     proteasome component 5; proteasome subunit alpha type-5;
                     proteasome alpha 5 subunit; alpha-5; proteasome (prosome,
                     macropain) subunit, alpha type, 5; epididymis tissue sperm
                     binding protein Li 11n; proteasome subunit alpha 5"
                     /calculated_mol_wt=19904
     Region          <1..162
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     CDS             1..183
                     /gene="PSMA5"
                     /gene_synonym="PSC5; ZETA"
                     /coded_by="NM_001199773.2:190..741"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55619.1"
                     /db_xref="GeneID:5686"
                     /db_xref="HGNC:HGNC:9534"
                     /db_xref="MIM:176844"
ORIGIN      
        1 mepssiekiv eidahigcam sgliadaktl idkarvetqn hwftynetmt vesvtqavsn
       61 lalqfgeeda dpgamsrpfg vallfggvde kgpqlfhmdp sgtfvqcdar aigsasegaq
      121 sslqevyhks mtlkeaikss liilkqvmee klnatniela tvqpgqnfhm ftkeeleevi
      181 kdi
//
LOCUS       NP_001356016             372 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356016 XP_016871780
VERSION     NP_001356016.1
DBSOURCE    REFSEQ: accession NM_001369087.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_016871780.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.198599.1,
                                           SRR1803612.173865.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..372
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 5"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=42098
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..372
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369087.1:104..1222"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitgv
      361 sdaysqslpg ks
//
LOCUS       NP_001975                282 aa            linear   PRI 20-NOV-2025
DEFINITION  S-formylglutathione hydrolase [Homo sapiens].
ACCESSION   NP_001975 XP_166266
VERSION     NP_001975.1
DBSOURCE    REFSEQ: accession NM_001984.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Yao,W., Chen,X., Cui,X., Zhou,B., Zhao,B., Lin,Z. and Miao,J.
  TITLE     Esterase D interacts with metallothionein 2A and inhibits the
            migration of A549 lung cancer cells in vitro
  JOURNAL   J Cell Biochem 124 (3), 373-381 (2023)
   PUBMED   36649442
  REMARK    GeneRIF: Esterase D interacts with metallothionein 2A and inhibits
            the migration of A549 lung cancer cells in vitro.
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Young,L.J., Lee,E.Y., To,H.A., Bookstein,R., Shew,J.Y.,
            Donoso,L.A., Sery,T., Giblin,M., Shields,J.A. and Lee,W.H.
  TITLE     Human esterase D gene: complete cDNA sequence, genomic structure,
            and application in the genetic diagnosis of human retinoblastoma
  JOURNAL   Hum Genet 79 (2), 137-141 (1988)
   PUBMED   3164702
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Lee,W.H., Wheatley,W., Benedict,W.F., Huang,C.M. and Lee,E.Y.
  TITLE     Purification, biochemical characterization, and biological function
            of human esterase D
  JOURNAL   Proc Natl Acad Sci U S A 83 (18), 6790-6794 (1986)
   PUBMED   3462728
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Squire,J., Dryja,T.P., Dunn,J., Goddard,A., Hofmann,T.,
            Musarella,M., Willard,H.F., Becker,A.J., Gallie,B.L. and
            Phillips,R.A.
  TITLE     Cloning of the esterase D gene: a polymorphic gene probe closely
            linked to the retinoblastoma locus on chromosome 13
  JOURNAL   Proc Natl Acad Sci U S A 83 (17), 6573-6577 (1986)
   PUBMED   3462714
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Lee,E.Y. and Lee,W.H.
  TITLE     Molecular cloning of the human esterase D gene, a genetic marker of
            retinoblastoma
  JOURNAL   Proc Natl Acad Sci U S A 83 (17), 6337-6341 (1986)
   PUBMED   3462698
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Varki,A., Muchmore,E. and Diaz,S.
  TITLE     A sialic acid-specific O-acetylesterase in human erythrocytes:
            possible identity with esterase D, the genetic marker of
            retinoblastomas and Wilson disease
  JOURNAL   Proc Natl Acad Sci U S A 83 (4), 882-886 (1986)
   PUBMED   3456572
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Bonne-Tamir,B., Farrer,L.A., Frydman,M. and Kanaaneh,H.
  TITLE     Evidence for linkage between Wilson disease and esterase D in three
            kindreds: detection of linkage for an autosomal recessive disorder
            by the family study method
  JOURNAL   Genet Epidemiol 3 (3), 201-209 (1986)
   PUBMED   3459695
REFERENCE   10 (residues 1 to 282)
  AUTHORS   van Heyningen,V., Bobrow,M., Bodmer,W.F., Gardiner,S.E., Povey,S.
            and Hopkinson,D.A.
  TITLE     Chromosome assignment of some human enzyme loci: mitochondrial
            malate dehydrogenase to 7, mannosephosphate isomerase and pyruvate
            kinase to 15 and probably, esterase D to 13
  JOURNAL   Ann Hum Genet 38 (3), 295-303 (1975)
   PUBMED   1137344
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF112219.1.
            
            On Dec 17, 2003 this sequence version replaced XP_166266.2.
            
            Summary: This gene encodes a serine hydrolase that belongs to the
            esterase D family. The encoded enzyme is active toward numerous
            substrates including O-acetylated sialic acids, and it may be
            involved in the recycling of sialic acids. This gene is used as a
            genetic marker for retinoblastoma and Wilson's disease. [provided
            by RefSeq, Feb 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF112219.1, HM005379.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378720.8/ ENSP00000367992.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.2"
     Protein         1..282
                     /product="S-formylglutathione hydrolase"
                     /EC_number="3.1.2.12"
                     /EC_number="3.1.1.56"
                     /note="esterase D/formylglutathione hydrolase; esterase
                     10; methylumbelliferyl-acetate deacetylase; testicular
                     tissue protein Li 66"
                     /calculated_mol_wt=31332
     Region          2..281
                     /region_name="PLN02442"
                     /note="S-formylglutathione hydrolase"
                     /db_xref="CDD:178061"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0P3; propagated from
                     UniProtKB/Swiss-Prot (P10768.2)"
     Site            200
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10768.2)"
     CDS             1..282
                     /gene="ESD"
                     /gene_synonym="FGH"
                     /coded_by="NM_001984.2:113..961"
                     /db_xref="CCDS:CCDS9404.1"
                     /db_xref="GeneID:2098"
                     /db_xref="HGNC:HGNC:3465"
                     /db_xref="MIM:133280"
ORIGIN      
        1 malkqissnk cfgglqkvfe hdsvelnckm kfavylppka etgkcpalyw lsgltcteqn
       61 fisksgyhqs asehglvvia pdtsprgcni kgedeswdfg tgagfyvdat edpwktnyrm
      121 ysyvteelpq linanfpvdp qrmsifghsm gghgalical knpgkyksvs afapicnpvl
      181 cpwgkkafsg ylgtdqskwk aydathlvks ypgsqldili dqgkddqfll dgqllpdnfi
      241 aactekkipv vfrlqegydh syyfiatfit dhirhhakyl na
//
LOCUS       NP_001124292             155 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 22 homolog isoform b [Homo
            sapiens].
ACCESSION   NP_001124292
VERSION     NP_001124292.1
DBSOURCE    REFSEQ: accession NM_001130820.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 155)
  AUTHORS   Silva,D.A., Huang,X., Behal,R.H., Cole,D.G. and Qin,H.
  TITLE     The RABL5 homolog IFT22 regulates the cellular pool size and the
            amount of IFT particles partitioned to the flagellar compartment in
            Chlamydomonas reinhardtii
  JOURNAL   Cytoskeleton (Hoboken) 69 (1), 33-48 (2012)
   PUBMED   22076686
REFERENCE   8  (residues 1 to 155)
  AUTHORS   Adhiambo,C., Blisnick,T., Toutirais,G., Delannoy,E. and Bastin,P.
  TITLE     A novel function for the atypical small G protein Rab-like 5 in the
            assembly of the trypanosome flagellum
  JOURNAL   J Cell Sci 122 (Pt 6), 834-841 (2009)
   PUBMED   19240117
REFERENCE   9  (residues 1 to 155)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA709553.1, BC004522.2, AC006329.5 and CA841889.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. It encodes
            isoform b, which is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.178785.1,
                                           SRR1803615.157571.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..155
                     /product="intraflagellar transport protein 22 homolog
                     isoform b"
                     /note="RAB, member of RAS oncogene family-like 5; rab-like
                     protein 5; RAB, member RAS oncogene family-like 5;
                     intraflagellar transport protein 22 homolog;
                     intraflagellar transport 22 homolog"
                     /calculated_mol_wt=17410
     Region          1..>74
                     /region_name="Gem1"
                     /note="GTPase SAR1 family domain [General function
                     prediction only]; COG1100"
                     /db_xref="CDD:440717"
     CDS             1..155
                     /gene="IFT22"
                     /gene_synonym="CFAP9; FAP9; RABL5"
                     /coded_by="NM_001130820.3:104..571"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47670.1"
                     /db_xref="GeneID:64792"
                     /db_xref="HGNC:HGNC:21895"
                     /db_xref="MIM:620505"
ORIGIN      
        1 mlkakilfvg pcesgktvla nfltessdit eysptqgvrf escwpalmkd ahgvvivfna
       61 dipshrkeme mwyscfvqqp slqdtqcmli ahhkpgsgdd kgslslsppl nklklvhsnl
      121 eddpeeirme fikylksiin smsesrdree msimt
//
LOCUS       NP_001278511             190 aa            linear   PRI 20-NOV-2025
DEFINITION  rab GTPase-binding effector protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001278511
VERSION     NP_001278511.1
DBSOURCE    REFSEQ: accession NM_001291582.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 190)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 190)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 190)
  AUTHORS   Swanton,E., Bishop,N. and Woodman,P.
  TITLE     Human rabaptin-5 is selectively cleaved by caspase-3 during
            apoptosis
  JOURNAL   J Biol Chem 274 (53), 37583-37590 (1999)
   PUBMED   10608812
REFERENCE   7  (residues 1 to 190)
  AUTHORS   Neve,R.L., Coopersmith,R., McPhie,D.L., Santeufemio,C., Pratt,K.G.,
            Murphy,C.J. and Lynn,S.D.
  TITLE     The neuronal growth-associated protein GAP-43 interacts with
            rabaptin-5 and participates in endocytosis
  JOURNAL   J Neurosci 18 (19), 7757-7767 (1998)
   PUBMED   9742146
REFERENCE   8  (residues 1 to 190)
  AUTHORS   Vitale,G., Rybin,V., Christoforidis,S., Thornqvist,P.,
            McCaffrey,M., Stenmark,H. and Zerial,M.
  TITLE     Distinct Rab-binding domains mediate the interaction of Rabaptin-5
            with GTP-bound Rab4 and Rab5
  JOURNAL   EMBO J 17 (7), 1941-1951 (1998)
   PUBMED   9524117
REFERENCE   9  (residues 1 to 190)
  AUTHORS   Xiao,G.H., Shoarinejad,F., Jin,F., Golemis,E.A. and Yeung,R.S.
  TITLE     The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5
            GTPase activating protein (GAP) in modulating endocytosis
  JOURNAL   J Biol Chem 272 (10), 6097-6100 (1997)
   PUBMED   9045618
REFERENCE   10 (residues 1 to 190)
  AUTHORS   Stenmark,H., Vitale,G., Ullrich,O. and Zerial,M.
  TITLE     Rabaptin-5 is a direct effector of the small GTPase Rab5 in
            endocytic membrane fusion
  JOURNAL   Cell 83 (3), 423-432 (1995)
   PUBMED   8521472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB169027.1 and BC018742.1.
            
            Transcript Variant: This variant (4) lacks several 3' exons but
            contains an alternate 3' terminal exon, and it thus differs in its
            3' coding region and 3' UTR, compared to variant 1. The encoded
            isoform (4) has a distinct C-terminus and is significantly shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018742.1, SRR7346977.515236.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..190
                     /product="rab GTPase-binding effector protein 1 isoform 4"
                     /note="rab GTPase-binding effector protein 1; rabaptin-5;
                     neurocrescin; rabaptin-4; rabaptin-5alpha; renal carcinoma
                     antigen NY-REN-17"
                     /calculated_mol_wt=22232
     Region          9..>190
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     CDS             1..190
                     /gene="RABEP1"
                     /gene_synonym="RAB5EP; RABPT5"
                     /coded_by="NM_001291582.2:204..776"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:9135"
                     /db_xref="HGNC:HGNC:17677"
                     /db_xref="MIM:603616"
ORIGIN      
        1 maqpgpasqp dvslqqrvae lekinaeflr aqqqleqefn qkrakfkely lakeedlkrq
       61 navlqaaqdd lghlrtqlwe aqaemenika iatvsentkq eaidevkrqw reevaslqav
      121 mketvrdyeh qfhlrleqer tqwaqyresa ereiadlrrr lsegqeeenl enemkkdpiq
      181 dtilhlvvsp
//
LOCUS       NP_001129611             651 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor E2-alpha isoform E47 [Homo sapiens].
ACCESSION   NP_001129611 XP_016882671
VERSION     NP_001129611.1
DBSOURCE    REFSEQ: accession NM_001136139.4
KEYWORDS    RefSeq; MANE Plus Clinical.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 651)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 651)
  AUTHORS   Collinson,R.J., Wilson,L., Boey,D., Ng,Z.Y., Mirzai,B., Chuah,H.S.,
            Howman,R., Grove,C.S., Malherbe,J.A.J., Leahy,M.F., Linden,M.D.,
            Fuller,K.A., Erber,W.N. and Guo,B.B.
  TITLE     Transcription factor 3 is dysregulated in megakaryocytes in
            myelofibrosis
  JOURNAL   Platelets 35 (1), 2304173 (2024)
   PUBMED   38303515
  REMARK    GeneRIF: Transcription factor 3 is dysregulated in megakaryocytes
            in myelofibrosis.
REFERENCE   3  (residues 1 to 651)
  AUTHORS   Xie,W., Liu,W., Wang,L., Li,S., Liao,Z., Xu,H., Li,Y., Jiang,X. and
            Ren,C.
  TITLE     Embryonic stem cell related gene regulates alternative splicing of
            transcription factor 3 to maintain human embryonic stem cells'
            self-renewal and pluripotency
  JOURNAL   Stem Cells 42 (6), 540-553 (2024)
   PUBMED   38393342
  REMARK    GeneRIF: Embryonic stem cell related gene regulates alternative
            splicing of transcription factor 3 to maintain human embryonic stem
            cells' self-renewal and pluripotency.
REFERENCE   4  (residues 1 to 651)
  AUTHORS   Li,Y., Li,R., Li,Y., Li,G., Zhao,Y., Mou,H., Chen,Y., Xiao,L. and
            Gong,K.
  TITLE     Transcription Factor TCF3 Promotes Macrophage-Mediated Inflammation
            and MMP Secretion in Abdominal Aortic Aneurysm by Regulating
            miR-143-5p /CCL20
  JOURNAL   J Cardiovasc Pharmacol 82 (6), 458-469 (2023)
   PUBMED   37721971
  REMARK    GeneRIF: Transcription Factor TCF3 Promotes Macrophage-Mediated
            Inflammation and MMP Secretion in Abdominal Aortic Aneurysm by
            Regulating miR-143-5p /CCL20.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 651)
  AUTHORS   Zhang,W., Nowotny,H., Theodoropoulou,M., Simon,J., Hemmer,C.M.,
            Bidlingmaier,M., Auer,M.K., Reincke,M., Uhlenhaut,H. and Reisch,N.
  TITLE     E47 as a novel glucocorticoid-dependent gene mediating lipid
            metabolism in patients with endogenous glucocorticoid excess
  JOURNAL   Front Endocrinol (Lausanne) 14, 1249863 (2023)
   PUBMED   38047107
  REMARK    GeneRIF: E47 as a novel glucocorticoid-dependent gene mediating
            lipid metabolism in patients with endogenous glucocorticoid excess.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 651)
  AUTHORS   Chakraborty,T., Martin,J.F. and Olson,E.N.
  TITLE     Analysis of the oligomerization of myogenin and E2A products in
            vivo using a two-hybrid assay system
  JOURNAL   J Biol Chem 267 (25), 17498-17501 (1992)
   PUBMED   1325437
REFERENCE   7  (residues 1 to 651)
  AUTHORS   Inaba,T., Roberts,W.M., Shapiro,L.H., Jolly,K.W., Raimondi,S.C.,
            Smith,S.D. and Look,A.T.
  TITLE     Fusion of the leucine zipper gene HLF to the E2A gene in human
            acute B-lineage leukemia
  JOURNAL   Science 257 (5069), 531-534 (1992)
   PUBMED   1386162
REFERENCE   8  (residues 1 to 651)
  AUTHORS   Sommer,L., Hagenbuchle,O., Wellauer,P.K. and Strubin,M.
  TITLE     Nuclear targeting of the transcription factor PTF1 is mediated by a
            protein subunit that does not bind to the PTF1 cognate sequence
  JOURNAL   Cell 67 (5), 987-994 (1991)
   PUBMED   1720355
REFERENCE   9  (residues 1 to 651)
  AUTHORS   Lassar,A.B., Davis,R.L., Wright,W.E., Kadesch,T., Murre,C.,
            Voronova,A., Baltimore,D. and Weintraub,H.
  TITLE     Functional activity of myogenic HLH proteins requires
            hetero-oligomerization with E12/E47-like proteins in vivo
  JOURNAL   Cell 66 (2), 305-315 (1991)
   PUBMED   1649701
REFERENCE   10 (residues 1 to 651)
  AUTHORS   Hunger,S.P., Galili,N., Carroll,A.J., Crist,W.M., Link,M.P. and
            Cleary,M.L.
  TITLE     The t(1;19)(q23;p13) results in consistent fusion of E2A and PBX1
            coding sequences in acute lymphoblastic leukemias
  JOURNAL   Blood 77 (4), 687-693 (1991)
   PUBMED   1671560
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006274.1, CD674814.1,
            CD516687.1, BU528547.1, BG284440.1, M24404.1, AW028755.1,
            AC005321.1 and KC877695.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced XP_016882671.1.
            
            Summary: This gene encodes a member of the E protein (class I)
            family of helix-loop-helix transcription factors. E proteins
            activate transcription by binding to regulatory E-box sequences on
            target genes as heterodimers or homodimers, and are inhibited by
            heterodimerization with inhibitor of DNA-binding (class IV)
            helix-loop-helix proteins. E proteins play a critical role in
            lymphopoiesis, and the encoded protein is required for B and T
            lymphocyte development. Deletion of this gene or diminished
            activity of the encoded protein may play a role in lymphoid
            malignancies. This gene is also involved in several chromosomal
            translocations that are associated with lymphoid malignancies
            including pre-B-cell acute lymphoblastic leukemia (t(1;19), with
            PBX1), childhood leukemia (t(19;19), with TFPT) and acute leukemia
            (t(12;19), with ZNF384). Alternatively spliced transcript variants
            encoding multiple isoforms have been observed for this gene, and a
            pseudogene of this gene is located on the short arm of chromosome
            9. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) differs in the 3' UTR, lacks
            an exon and includes an alternate exon in the 3' coding region, but
            maintains the reading frame, compared to variant 1. The encoded
            isoform (E47, also known as Pan-1) is shorter than isoform E12.
            Variants 2 and 4 encode the same isoform (E47).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352441.308179.1,
                                           SRR14038191.1229519.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match :: ENST00000588136.7/ ENSP00000468487.1
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..651
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..651
                     /product="transcription factor E2-alpha isoform E47"
                     /note="VDR interacting repressor; transcription factor
                     E2-alpha; immunoglobulin transcription factor 1;
                     kappa-E2-binding factor; transcription factor ITF-1;
                     E2A-HLF fusion transcript protein; class B basic
                     helix-loop-helix protein 21; vitamin D
                     receptor-interacting repressor; negative vitamin D
                     response element-binding protein; helix-loop-helix protein
                     HE47; transcription factor 3 (E2A immunoglobulin enhancer
                     binding factors E12/E47); NOL1-TCF3 fusion"
                     /calculated_mol_wt=67134
     Region          538..611
                     /region_name="bHLH_E-protein_E47-like"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor E47 and similar proteins; cd18943"
                     /db_xref="CDD:381513"
     Site            order(548,552,554..556,558,563,584..585)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381513"
     Site            order(561..562,565..566,568..569,572,576,586,589,593,
                     595..597,599..600,602..604,606)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     Site            order(561..562,565..566,568..569,572,576,586,589,593,596,
                     599..604)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:381513"
     CDS             1..651
                     /gene="TCF3"
                     /gene_synonym="AGM8; AGM8A; AGM8B; bHLHb21; E2A; E47;
                     ITF1; p75; TCF-3; VDIR"
                     /coded_by="NM_001136139.4:356..2311"
                     /note="isoform E47 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45899.1"
                     /db_xref="GeneID:6929"
                     /db_xref="HGNC:HGNC:11633"
                     /db_xref="MIM:147141"
ORIGIN      
        1 mnqpqrmapv gtdkelsdll dfsmmfplpv tngkgrpasl agaqfggsgl edrpssgswg
       61 sgdqssssfd psrtfsegth fteshsslss stflgpglgg ksgergayas fgrdagvggl
      121 tqagflsgel alnspgplsp sgmkgtsqyy psysgssrrr aadgsldtqp kkvrkvppgl
      181 pssvyppssg edygrdatay psaktpssty papfyvadgs lhpsaelwsp pgqagfgpml
      241 gggssplplp pgsgpvgssg ssstfgglhq hermgyqlhg aevngglpsa ssfssapgat
      301 yggvsshtpp vsgadsllgs rgttagssgd algkalasiy spdhssnnfs sspstpvgsp
      361 qglagtsqwp ragapgalsp sydgglhglq skiedhldea ihvlrshavg tagdmhtllp
      421 ghgalasgft gpmslggrha glvggshped glagstslmh nhaalpsqpg tlpdlsrppd
      481 sysglgraga taaaseikre ekedeentsa adhseeekke lkaprartss tdevlsleek
      541 dlrdrerrma nnarervrvr dineafrelg rmcqmhlksd kaqtkllilq qavqvilgle
      601 qqvrernlnp kaaclkrree ekvsgvvgdp qmvlsaphpg lseahnpagh m
//
LOCUS       NP_065716                222 aa            linear   PRI 20-NOV-2025
DEFINITION  collectrin precursor [Homo sapiens].
ACCESSION   NP_065716
VERSION     NP_065716.1
DBSOURCE    REFSEQ: accession NM_020665.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Chu,P.L., Gigliotti,J.C., Cechova,S., Bodonyi-Kovacs,G., Wang,Y.T.,
            Chen,L., Wassertheil-Smoller,S., Cai,J., Isakson,B.E.,
            Franceschini,N. and Le,T.H.
  TITLE     Collectrin (Tmem27) deficiency in proximal tubules causes
            hypertension in mice and a TMEM27 variant associates with blood
            pressure in males in a Latino cohort
  JOURNAL   Am J Physiol Renal Physiol 324 (1), F30-F42 (2023)
   PUBMED   36264884
  REMARK    GeneRIF: Collectrin (Tmem27) deficiency in proximal tubules causes
            hypertension in mice and a TMEM27 variant associates with blood
            pressure in males in a Latino cohort.
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Grewal,R., Choung,H.Y.G., Roberts,L.L., Beane,T., Chen,L.,
            Gilroy,D.X., Rappold,P.M. and Le,T.H.
  TITLE     TMEM27 expression and clinical characteristics and survival in
            clear cell renal cell carcinoma
  JOURNAL   Acta Oncol 61 (12), 1507-1511 (2022)
   PUBMED   36369873
  REMARK    GeneRIF: TMEM27 expression and clinical characteristics and
            survival in clear cell renal cell carcinoma.
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Aslan Cetin,B., Aydogan Mathyk,B., Cift,T., Tuten,A., Bulut,B.,
            Yilmaz,N., Erenel,H., Ekmekci,H. and Gezer,A.
  TITLE     Serum collectrin levels in patients with early- and late-onset
            preeclampsia
  JOURNAL   J Matern Fetal Neonatal Med 31 (21), 2827-2831 (2018)
   PUBMED   28764560
  REMARK    GeneRIF: Maternal serum collectrin levels are significantly lower
            in patients with preeclampsia than in the control group. There is
            an inverse correlation between serum collectrin levels and blood
            pressure.
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Javorhazy,A., Farkas,N., Beothe,T., Pusztai,C., Szanto,A. and
            Kovacs,G.
  TITLE     Lack of TMEM27 expression is associated with postoperative
            progression of clinically localized conventional renal cell
            carcinoma
  JOURNAL   J Cancer Res Clin Oncol 142 (9), 1947-1953 (2016)
   PUBMED   27417314
  REMARK    GeneRIF: Lack of expression of the TMEM27 in conventional renal
            cell carcinoma defines a group of patients at high risk for
            cancer-related death.
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Kowalczuk,S., Broer,A., Tietze,N., Vanslambrouck,J.M., Rasko,J.E.
            and Broer,S.
  TITLE     A protein complex in the brush-border membrane explains a Hartnup
            disorder allele
  JOURNAL   FASEB J 22 (8), 2880-2887 (2008)
   PUBMED   18424768
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Mount,D.B.
  TITLE     Collectrin and the kidney
  JOURNAL   Curr Opin Nephrol Hypertens 16 (5), 427-429 (2007)
   PUBMED   17693757
  REMARK    GeneRIF: Collectrin has a role in amino acid transpor in the kidney
            [review]
            Review article
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Fukui,K., Yang,Q., Cao,Y., Takahashi,N., Hatakeyama,H., Wang,H.,
            Wada,J., Zhang,Y., Marselli,L., Nammo,T., Yoneda,K., Onishi,M.,
            Higashiyama,S., Matsuzawa,Y., Gonzalez,F.J., Weir,G.C., Kasai,H.,
            Shimomura,I., Miyagawa,J., Wollheim,C.B. and Yamagata,K.
  TITLE     The HNF-1 target collectrin controls insulin exocytosis by SNARE
            complex formation
  JOURNAL   Cell Metab 2 (6), 373-384 (2005)
   PUBMED   16330323
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Zhang,H., Wada,J., Hida,K., Tsuchiyama,Y., Hiragushi,K.,
            Shikata,K., Wang,H., Lin,S., Kanwar,Y.S. and Makino,H.
  TITLE     Collectrin, a collecting duct-specific transmembrane glycoprotein,
            is a novel homolog of ACE2 and is developmentally regulated in
            embryonic kidneys
  JOURNAL   J Biol Chem 276 (20), 17132-17139 (2001)
   PUBMED   11278314
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014317.1 and AI470468.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a type 1 transmembrane protein that is
            important for trafficking amino acid transporters to the apical
            brush border of proximal tubules. The encoded protein binds to
            amino acid transporters and regulates their expression on the
            plasma membrane. It also plays a role in controlling insulin
            exocytosis by regulating formation of the SNARE (soluble
            N-ethylmaleimide-sensitive-factor attachment protein receptor)
            complex in pancreatic beta cells. The extracellular domain of the
            encoded protein may be cleaved and shed from the plasma membrane
            specifically in pancreatic beta cells. [provided by RefSeq, Jun
            2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015099.1, SRR5189664.78391.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380342.4/ ENSP00000369699.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..222
                     /product="collectrin precursor"
                     /note="collectrin; kidney-specific membrane protein;
                     transmembrane protein 27"
                     /calculated_mol_wt=23578
     sig_peptide     1..14
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1675
     mat_peptide     15..222
                     /product="Collectrin. /id=PRO_0000245867"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBJ8.1)"
                     /calculated_mol_wt=23578
     Region          24..171
                     /region_name="Collectrin"
                     /note="Renal amino acid transporter; pfam16959"
                     /db_xref="CDD:465322"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     Site            125..126
                     /site_type="cleavage"
                     /note="Cleavage by BACE2.
                     /evidence=ECO:0000269|PubMed:22628310; propagated from
                     UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     Site            142..162
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESG4; propagated from
                     UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESG4; propagated from
                     UniProtKB/Swiss-Prot (Q9HBJ8.1)"
     CDS             1..222
                     /gene="CLTRN"
                     /gene_synonym="NX-17; NX17; TMEM27"
                     /coded_by="NM_020665.6:31..699"
                     /db_xref="CCDS:CCDS14170.1"
                     /db_xref="GeneID:57393"
                     /db_xref="HGNC:HGNC:29437"
                     /db_xref="MIM:300631"
ORIGIN      
        1 mlwllfflvt aihaelcqpg aenafkvrls irtalgdkay awdtneeylf kamvafsmrk
       61 vpnreateis hvllcnvtqr vsfwfvvtdp sknhtlpave vqsairmnkn rinnafflnd
      121 qtleflkips tlappmdpsv piwiiifgvi fciiivaial lilsgiwqrr rknkepsevd
      181 daedkcenmi tiengipsdp ldmkgghind afmtederlt pl
//
LOCUS       NP_003397                245 aa            linear   PRI 20-NOV-2025
DEFINITION  14-3-3 protein zeta/delta [Homo sapiens].
ACCESSION   NP_003397
VERSION     NP_003397.1
DBSOURCE    REFSEQ: accession NM_003406.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Lughmani,H., Patel,H. and Chakravarti,R.
  TITLE     Structural Features and Physiological Associations of Human
            14-3-3zeta Pseudogenes
  JOURNAL   Genes (Basel) 15 (4), 399 (2024)
   PUBMED   38674334
  REMARK    GeneRIF: Structural Features and Physiological Associations of
            Human 14-3-3zeta Pseudogenes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Shi,L., Wang,X., Guo,S., Gou,H., Shang,H., Jiang,X., Wei,C.,
            Wang,J., Li,C., Wang,L., Zhao,Z., Yu,W. and Yu,J.
  TITLE     TMEM65 promotes gastric tumorigenesis by targeting YWHAZ to
            activate PI3K-Akt-mTOR pathway and is a therapeutic target
  JOURNAL   Oncogene 43 (13), 931-943 (2024)
   PUBMED   38341472
  REMARK    GeneRIF: TMEM65 promotes gastric tumorigenesis by targeting YWHAZ
            to activate PI3K-Akt-mTOR pathway and is a therapeutic target.
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Mukherjee,S., Roy,S., Mukherjee,S., Harikishore,A., Bhunia,A. and
            Mandal,A.K.
  TITLE     14-3-3 interaction with phosphodiesterase 8A sustains PKA signaling
            and downregulates the MAPK pathway
  JOURNAL   J Biol Chem 300 (3), 105725 (2024)
   PUBMED   38325743
  REMARK    GeneRIF: 14-3-3 interaction with phosphodiesterase 8A sustains PKA
            signaling and downregulates the MAPK pathway.
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Koyama,S., Williams,L.T. and Kikuchi,A.
  TITLE     Characterization of the interaction of Raf-1 with ras p21 or 14-3-3
            protein in intact cells
  JOURNAL   FEBS Lett 368 (2), 321-325 (1995)
   PUBMED   7628630
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Liu,D., Bienkowska,J., Petosa,C., Collier,R.J., Fu,H. and
            Liddington,R.
  TITLE     Crystal structure of the zeta isoform of the 14-3-3 protein
  JOURNAL   Nature 376 (6536), 191-194 (1995)
   PUBMED   7603574
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Sato,T., Irie,S., Kitada,S. and Reed,J.C.
  TITLE     FAP-1: a protein tyrosine phosphatase that associates with Fas
  JOURNAL   Science 268 (5209), 411-415 (1995)
   PUBMED   7536343
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Kawamoto,S., Shoji,M., Setoguchi,Y., Kato,M., Hashizume,S.,
            Ichikawa,A., Osada,K., Katakura,Y., Tachibana,H. and Murakami,H.
  TITLE     Molecular cloning of the 31 kDa cytosolic phospholipase A2, as an
            antigen recognized by the lung cancer-specific human monoclonal
            antibody, AE6F4
  JOURNAL   Cytotechnology 17 (2), 103-108 (1995)
   PUBMED   7547034
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Zupan,L.A., Steffens,D.L., Berry,C.A., Landt,M. and Gross,R.W.
  TITLE     Cloning and expression of a human 14-3-3 protein mediating
            phospholipolysis. Identification of an arachidonoyl-enzyme
            intermediate during catalysis
  JOURNAL   J Biol Chem 267 (13), 8707-8710 (1992)
   PUBMED   1577711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC298291.1, BC072426.1,
            BM783874.1 and AC027373.11.
            
            Summary: This gene product belongs to the 14-3-3 family of proteins
            which mediate signal transduction by binding to
            phosphoserine-containing proteins. This highly conserved protein
            family is found in both plants and mammals, and this protein is 99%
            identical to the mouse, rat and sheep orthologs. The encoded
            protein interacts with IRS1 protein, suggesting a role in
            regulating insulin sensitivity. Several transcript variants that
            differ in the 5' UTR but that encode the same protein have been
            identified for this gene. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 2. All six transcripts encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.277687.1,
                                           SRR1803614.166107.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..245
                     /product="14-3-3 protein zeta/delta"
                     /note="14-3-3 delta; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, delta polypeptide;
                     14-3-3 zeta; phospholipase A2; protein kinase C inhibitor
                     protein-1; tyrosine 3/tryptophan 5 -monooxygenase
                     activation protein, zeta polypeptide; 14-3-3
                     protein/cytosolic phospholipase A2; epididymis secretory
                     protein Li 93; tyrosine 3-monooxygenase/tryptophan
                     5-monooxygenase activation protein, zeta polypeptide;
                     epididymis secretory protein Li 3; epididymis luminal
                     protein 4"
                     /calculated_mol_wt=27614
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Region          2..230
                     /region_name="14-3-3_beta_zeta"
                     /note="14-3-3 beta and zeta isoforms of 14-3-3 protein;
                     cd10022"
                     /db_xref="CDD:206758"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            order(5,8..9,12..13,15..16,18,21,58,61,65,75,78..79,82,
                     85..86,89)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            order(41..42,45..46,49,117,120,127..128,165,169,172..173,
                     176,209..213,216..217,220,224)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:206758"
     Site            56
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P63103;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:11956222,
                     ECO:0000269|PubMed:12865427, ECO:0000269|PubMed:15883165,
                     ECO:0000269|PubMed:16376338; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            68
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            127
                     /site_type="other"
                     /note="Interaction with phosphoserine on interacting
                     protein. /evidence=ECO:0000250|UniProtKB:P63103;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8.
                     /evidence=ECO:0000269|PubMed:15071501,
                     ECO:0000269|PubMed:15696159; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63102; propagated from
                     UniProtKB/Swiss-Prot (P63104.1)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000269|PubMed:31024343,
                     ECO:0000269|PubMed:9360956, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P63104.1)"
     CDS             1..245
                     /gene="YWHAZ"
                     /gene_synonym="14-3-3-zeta; HEL-S-3; HEL-S-93; HEL4;
                     KCIP-1; POPCHAS; YWHAD"
                     /coded_by="NM_003406.4:126..863"
                     /db_xref="CCDS:CCDS6290.1"
                     /db_xref="GeneID:7534"
                     /db_xref="HGNC:HGNC:12855"
                     /db_xref="MIM:601288"
ORIGIN      
        1 mdknelvqka klaeqaeryd dmaacmksvt eqgaelsnee rnllsvaykn vvgarrsswr
       61 vvssieqkte gaekkqqmar eyrekietel rdicndvlsl lekflipnas qaeskvfylk
      121 mkgdyyryla evaagddkkg ivdqsqqayq eafeiskkem qpthpirlgl alnfsvfyye
      181 ilnspekacs laktafdeai aeldtlsees ykdstlimql lrdnltlwts dtqgdeaeag
      241 eggen
//
LOCUS       NP_001356018             372 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356018
VERSION     NP_001356018.1
DBSOURCE    REFSEQ: accession NM_001369089.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 372)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 372)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 372)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.147643.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..372
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 5"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=42098
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..321
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..372
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369089.1:214..1332"
                     /note="isoform 5 is encoded by transcript variant 10"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilks fallprleyn daisahcnlc lpgssdspas asqvagitgv
      361 sdaysqslpg ks
//
LOCUS       NP_001354634             916 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ppp [Homo sapiens].
ACCESSION   NP_001354634
VERSION     NP_001354634.1
DBSOURCE    REFSEQ: accession NM_001367705.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 916)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 916)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.231921.1,
                                           SRR1660805.210675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..916
                     /product="SUN domain-containing protein 1 isoform ppp"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=101802
     Region          62..422
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          548..601
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(548,551..552,555,558..559,562..563,565..566,
                     569..570,572..573,576..577,579..580,583,586..587,590,
                     593..594,597..598,600..601)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          560..>693
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          678..736
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          779..914
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..916
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367705.1:52..2802"
                     /note="isoform ppp is encoded by transcript variant 68"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealcddckgk rhldahtaah sqsprlpgra gtlwhiwaca gyfllqilrr
      361 igavgqavsr tawsalwlav vapgkaasgv fwwlgigwyq fvtliswlnv flltrclrni
      421 ckflvllipl flllaglslr gqgnffsflp vlnwasmhrt qrvddpqdvf kpttsrlkqp
      481 lqgdseafpw hwmsgveqqv aslsgqchhh genlrelttl lqklqarvdq meggaagpsa
      541 svrdavgqpp retdfmafhq ehevrmshle dilgklreks eaiqkeleqt kqktisavge
      601 qllptvehlq leldqlksel sswrhvktgc etvdavqerv dvqvremvkl lfsedqqggs
      661 leqllqrfss qfvskgdlqt mlrdlqlqil rnvthhvsvt kqlptseavv savseagasg
      721 iteaqaraiv nsalklysqd ktgmvdfale sgggsilstr csetyetkta lmslfgiplw
      781 yfsqsprvvi qpdiypgncw afkgsqgylv vrlsmmihpa aftlehipkt lsptgnissa
      841 pkdfavygle neyqeegqll gqftydqdge slqmfqalkr pddtafqive lrifsnwghp
      901 eytclyrfrv hgepvk
//
LOCUS       NP_061841                539 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-2-syntrophin [Homo sapiens].
ACCESSION   NP_061841 XP_352506
VERSION     NP_061841.2
DBSOURCE    REFSEQ: accession NM_018968.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Jales Neto,L.H., Wicik,Z., Torres,G.H.F., Takayama,L.,
            Caparbo,V.F., Lopes,N.H.M., Pereira,A.C. and Pereira,R.M.R.
  TITLE     Overexpression of SNTG2, TRAF3IP2, and ITGA6 transcripts is
            associated with osteoporotic vertebral fracture in elderly women
            from community
  JOURNAL   Mol Genet Genomic Med 8 (9), e1391 (2020)
   PUBMED   32602654
  REMARK    GeneRIF: Overexpression of SNTG2, TRAF3IP2, and ITGA6 transcripts
            is associated with osteoporotic vertebral fracture in elderly women
            from community.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Rio,M., Royer,G., Gobin,S., de Blois,M.C., Ozilou,C., Bernheim,A.,
            Nizon,M., Munnich,A., Bonnefont,J.P., Romana,S., Vekemans,M.,
            Turleau,C. and Malan,V.
  TITLE     Monozygotic twins discordant for submicroscopic chromosomal
            anomalies in 2p25.3 region detected by array CGH
  JOURNAL   Clin Genet 84 (1), 31-36 (2013)
   PUBMED   23061379
  REMARK    GeneRIF: MYT1L and the SNTG2 genes within the reported region could
            probably relate to the phenotypic discordance of the monozygotic
            twins.
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Yamakawa,H., Oyama,S., Mitsuhashi,H., Sasagawa,N., Uchino,S.,
            Kohsaka,S. and Ishiura,S.
  TITLE     Neuroligins 3 and 4X interact with syntrophin-gamma2, and the
            interactions are affected by autism-related mutations
  JOURNAL   Biochem Biophys Res Commun 355 (1), 41-46 (2007)
   PUBMED   17292328
  REMARK    GeneRIF: A de novo binding partner of X-linked neuroligin 4 and
            neuroligin 3, which correlates with autism-related mutations.
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Ou,Y., Strege,P., Miller,S.M., Makielski,J., Ackerman,M.,
            Gibbons,S.J. and Farrugia,G.
  TITLE     Syntrophin gamma 2 regulates SCN5A gating by a PDZ domain-mediated
            interaction
  JOURNAL   J Biol Chem 278 (3), 1915-1923 (2003)
   PUBMED   12429735
  REMARK    GeneRIF: role in regulating SCN5A gating by a PDZ domain-mediated
            interaction
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC116614.6, BC035783.1,
            AJ003029.1 and BG208326.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 24, 2009 this sequence version replaced NP_061841.1.
            
            Summary: This gene encodes a protein belonging to the syntrophin
            family. Syntrophins are cytoplasmic peripheral membrane proteins
            that bind to components of mechanosenstive sodium channels and the
            extreme carboxy-terminal domain of dystrophin and
            dystrophin-related proteins. The PDZ domain of this protein product
            interacts with a protein component of a mechanosensitive sodium
            channel that affects channel gating. Absence or reduction of this
            protein product has been associated with Duchenne muscular
            dystrophy. There is evidence of alternative splicing yet the
            full-length nature of these variants has not been described.
            [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ003029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2154125
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308624.10/ ENSP00000311837.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.3"
     Protein         1..539
                     /product="gamma-2-syntrophin"
                     /note="syntrophin-5"
                     /calculated_mol_wt=60086
     Region          72..154
                     /region_name="PDZ_syntrophin-like"
                     /note="PDZ domain of syntrophins, and related domains;
                     cd06801"
                     /db_xref="CDD:467262"
     Site            order(83..89,101,104,134,138,141..142)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467262"
     Region          168..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NY99.2)"
     CDS             1..539
                     /gene="SNTG2"
                     /gene_synonym="G2SYN; SYN5"
                     /coded_by="NM_018968.4:149..1768"
                     /db_xref="CCDS:CCDS46220.1"
                     /db_xref="GeneID:54221"
                     /db_xref="HGNC:HGNC:13741"
                     /db_xref="MIM:608715"
ORIGIN      
        1 mgtegppppa asrgrqgcll vpartkttia llydeesena ydirlkltke vltiqkqdvv
       61 cvggshqgrn rrtvtlrrqp vgglglsikg gsehnvpvvi skifedqaad qtgmlfvgda
      121 vlqvngihve natheevvhl lrnagdevti tveylreapa flklplgspg pssdhssgas
      181 splfdsglhl ngnssttaps spsspiakdp ryekrwldtl svplsmaris rykagteklr
      241 wnafevlald gvssgilrfy taqdgtdwlr avsanirelt lqnmkmankc cspsdqvvhm
      301 gwvneklqga dssqtfrpkf lalkgpsfyv fstppvstfd wvraertyhl cevlfkvhkf
      361 wltedcwlqa nlylglqdfd fedqrpycfs ivaghgkshv fnvelgsela mweksfqrat
      421 fmevqrtgsr tymcswqgem lcftvdfalg ftcfesktkn vlwrfkfsql kgssddgktr
      481 vkllfqnldt kqietkelef qdlravlhci hsfiaakvas vdpgfmdsqs larkymyss
//
LOCUS       NP_005558                585 aa            linear   PRI 20-NOV-2025
DEFINITION  galectin-3-binding protein precursor [Homo sapiens].
ACCESSION   NP_005558
VERSION     NP_005558.1
DBSOURCE    REFSEQ: accession NM_005567.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 585)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 585)
  AUTHORS   Liu,Y., Liang,L., Li,J., Pang,T., Zhang,S.H. and Xia,Z.Y.
  TITLE     Aberrant expression of LGALS3BP drives an unfavorable prognosis and
            more aggressive in HCC via regulating PI3K/AKT signaling
  JOURNAL   Tissue Cell 89, 102471 (2024)
   PUBMED   39029315
  REMARK    GeneRIF: Aberrant expression of LGALS3BP drives an unfavorable
            prognosis and more aggressive in HCC via regulating PI3K/AKT
            signaling.
REFERENCE   3  (residues 1 to 585)
  AUTHORS   Panigrahi,A., Benicky,J., Aljuhani,R., Mukherjee,P., Novakova,Z.,
            Barinka,C. and Goldman,R.
  TITLE     Galectin-3-Binding Protein Inhibits Extracellular Heparan
            6-O-Endosulfatase Sulf-2
  JOURNAL   Mol Cell Proteomics 23 (7), 100793 (2024)
   PUBMED   38825040
  REMARK    GeneRIF: Galectin-3-Binding Protein Inhibits Extracellular Heparan
            6-O-Endosulfatase Sulf-2.
REFERENCE   4  (residues 1 to 585)
  AUTHORS   Yamanaka,T., Araki,K., Yokobori,T., Muranushi,R., Hoshino,K.,
            Hagiwara,K., Gantumur,D., Ishii,N., Tsukagoshi,M., Watanabe,A.,
            Harimoto,N., Masamune,A., Uojima,H., Mizokami,M., Ito,K. and
            Shirabe,K.
  TITLE     Potential of Mac-2-binding protein glycan isomer as a new
            therapeutic target in pancreatic cancer
  JOURNAL   Cancer Sci 115 (4), 1241-1249 (2024)
   PUBMED   38321872
  REMARK    GeneRIF: Potential of Mac-2-binding protein glycan isomer as a new
            therapeutic target in pancreatic cancer.
REFERENCE   5  (residues 1 to 585)
  AUTHORS   Li,L., Qin,S., Tan,H. and Zhou,J.
  TITLE     LGALS3BP is a novel and potential biomarker in clear cell renal
            cell carcinoma
  JOURNAL   Aging (Albany NY) 16 (4), 4033-4051 (2024)
   PUBMED   38393692
  REMARK    GeneRIF: LGALS3BP is a novel and potential biomarker in clear cell
            renal cell carcinoma.
REFERENCE   6  (residues 1 to 585)
  AUTHORS   Calabrese,G., Sures,I., Pompetti,F., Natoli,G., Palka,G. and
            Iacobelli,S.
  TITLE     The gene (LGALS3BP) encoding the serum protein 90K, associated with
            cancer and infection by the human immunodeficiency virus, maps at
            17q25
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 223-225 (1995)
   PUBMED   7698018
REFERENCE   7  (residues 1 to 585)
  AUTHORS   Yu,B. and Wright,S.D.
  TITLE     LPS-dependent interaction of Mac-2-binding protein with immobilized
            CD14
  JOURNAL   J Inflamm 45 (2), 115-125 (1995)
   PUBMED   7583357
REFERENCE   8  (residues 1 to 585)
  AUTHORS   Ullrich,A., Sures,I., D'Egidio,M., Jallal,B., Powell,T.J.,
            Herbst,R., Dreps,A., Azam,M., Rubinstein,M., Natoli,C. et al.
  TITLE     The secreted tumor-associated antigen 90K is a potent immune
            stimulator
  JOURNAL   J Biol Chem 269 (28), 18401-18407 (1994)
   PUBMED   8034587
REFERENCE   9  (residues 1 to 585)
  AUTHORS   Koths,K., Taylor,E., Halenbeck,R., Casipit,C. and Wang,A.
  TITLE     Cloning and characterization of a human Mac-2-binding protein, a
            new member of the superfamily defined by the macrophage scavenger
            receptor cysteine-rich domain
  JOURNAL   J Biol Chem 268 (19), 14245-14249 (1993)
   PUBMED   8390986
REFERENCE   10 (residues 1 to 585)
  AUTHORS   Rosenberg,I., Cherayil,B.J., Isselbacher,K.J. and Pillai,S.
  TITLE     Mac-2-binding glycoproteins. Putative ligands for a cytosolic
            beta-galactoside lectin
  JOURNAL   J Biol Chem 266 (28), 18731-18736 (1991)
   PUBMED   1917996
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L13210.1 and BC002403.2.
            
            Summary: The galectins are a family of beta-galactoside-binding
            proteins implicated in modulating cell-cell and cell-matrix
            interactions. LGALS3BP has been found elevated in the serum of
            patients with cancer and in those infected by the human
            immunodeficiency virus (HIV). It appears to be implicated in immune
            response associated with natural killer (NK) and
            lymphokine-activated killer (LAK) cell cytotoxicity. Using
            fluorescence in situ hybridization the full length 90K cDNA has
            been localized to chromosome 17q25. The native protein binds
            specifically to a human macrophage-associated lectin known as Mac-2
            and also binds galectin 1. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.560849.1, BC015761.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262776.8/ ENSP00000262776.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..585
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..585
                     /product="galectin-3-binding protein precursor"
                     /EC_number="3.6.1.6"
                     /note="L3 antigen; Mac-2-binding protein; serum protein
                     90K; MAC2BP; transport and golgi organization 10 homolog
                     B; mac-2 BP; tumor-associated antigen 90K; basement
                     membrane autoantigen p105; lectin galactoside-binding
                     soluble 3-binding protein"
                     /calculated_mol_wt=63277
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2073
     Region          24..124
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Site            69
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:15084671,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002,
                     ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9501082;
                     propagated from UniProtKB/Swiss-Prot (Q08380.1)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q08380.1)"
     Region          136..247
                     /region_name="BTB_POZ_M2BP"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Mac-2-binding
                     protein (MAC2BP/M2BP); cd18304"
                     /db_xref="CDD:349613"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q08380.1)"
     Region          256..329
                     /region_name="BACK_LGALS3BP"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     lectin galactoside-binding soluble 3-binding protein
                     (LGALS3BP); cd18496"
                     /db_xref="CDD:350571"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (Q08380.1)"
     Site            398
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q08380.1)"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401,
                     ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (Q08380.1)"
     Site            580
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19139490;
                     propagated from UniProtKB/Swiss-Prot (Q08380.1)"
     CDS             1..585
                     /gene="LGALS3BP"
                     /gene_synonym="90K; BTBD17B; CyCAP; gp90; M2BP; MAC-2-BP;
                     TANGO10B"
                     /coded_by="NM_005567.4:124..1881"
                     /db_xref="CCDS:CCDS11759.1"
                     /db_xref="GeneID:3959"
                     /db_xref="HGNC:HGNC:6564"
                     /db_xref="MIM:600626"
ORIGIN      
        1 mtpprlfwvw llvagtqgvn dgdmrladgg atnqgrveif yrgqwgtvcd nlwdltdasv
       61 vcralgfena tqalgraafg qgsgpimlde vqctgteasl adckslgwlk sncrherdag
      121 vvctnetrst htldlsrels ealgqifdsq rgcdlsisvn vqgedalgfc ghtviltanl
      181 eaqalwkepg snvtmsvdae cvpmvrdllr yfysrridit lssvkcfhkl asaygarqlq
      241 gycaslfail lpqdpsfqmp ldlyayavat gdalleklcl qflawnfeal tqaeawpsvp
      301 tdllqlllpr sdlavpsela llkavdtwsw gerasheeve glvekirfpm mlpeelfelq
      361 fnlslywshe alfqkktlqa lefhtvpfql larykglnlt edtykpriyt sptwsafvtd
      421 sswsarksql vyqsrrgplv kyssdyfqap sdyryypyqs fqtpqhpsfl fqdkrvswsl
      481 vylptiqscw nygfscssde lpvlgltksg gsdrtiayen kalmlceglf vadvtdfegw
      541 kaaipsaldt nsskstssfp cpaghfngfr tvirpfyltn ssgvd
//
LOCUS       NP_001337137             550 aa            linear   PRI 20-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform h [Homo
            sapiens].
ACCESSION   NP_001337137 XP_016855711
VERSION     NP_001337137.1
DBSOURCE    REFSEQ: accession NM_001350208.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 550)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB081133.1, AF392445.1,
            AL050343.17 and EL953716.1.
            
            On Apr 8, 2017 this sequence version replaced XP_016855711.1.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.203616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142853, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..550
                     /product="oxysterol-binding protein-related protein 9
                     isoform h"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=61433
     Region          191..537
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..550
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_001350208.2:762..2414"
                     /note="isoform h is encoded by transcript variant 10"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 msshslslst inpvdaiyqp splepvistm psqtvlppep vqlckseqrp sslpvgpvla
       61 tlghhqtptp nstgsghspp sssltspshv nlspntvpef sysssedefy dadefhqsgs
      121 spkrlidssg sasvlthsss gnslkrpdtt eslnsslsng tsdadlfdsh ddrdddaeag
      181 sveehksvim hllsqvrlgm dltkvvlptf ilerrsllem yadffahpdl fvsisdqkdp
      241 kdrmvqvvkw ylsafhagrk gsvakkpynp ilgeifqchw tlpndteent elvsegpvpw
      301 vsknsvtfva eqvshhppis afyaecfnkk iqfnahiwtk skflgmsigv hnigqgcvsc
      361 ldydehyilt fpngygrsil tvpwvelgge cnincsktgy saniifhtkp fyggkkhrit
      421 aeifspndkk sfcsiegewn gvmyakyatg entvfvdtkk lpiikkkvrk ledqneyesr
      481 slwkdvtfnl kirdidaate akhrleerqr aearerkeke iqwetrlfhe dgecwvydep
      541 llkrlgaakh
//
LOCUS       NP_001029102             128 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001029102
VERSION     NP_001029102.1
DBSOURCE    REFSEQ: accession NM_001033930.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Park,J., Wu,J., Szkop,K.J., Jeong,J., Jovanovic,P., Husmann,D.,
            Flores,N.M., Francis,J.W., Chen,Y.C., Benitez,A.M., Zahn,E.,
            Song,S., Ajani,J.A., Wang,L., Singh,K., Larsson,O., Garcia,B.A.,
            Topisirovic,I., Gozani,O. and Mazur,P.K.
  TITLE     SMYD5 methylation of rpL40 links ribosomal output to gastric cancer
  JOURNAL   Nature 632 (8025), 656-663 (2024)
   PUBMED   39048817
  REMARK    GeneRIF: SMYD5 methylation of rpL40 links ribosomal output to
            gastric cancer.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tong,L., Zheng,X., Wang,T., Gu,W., Shen,T., Yuan,W., Wang,S.,
            Xing,S., Liu,X., Zhang,C. and Zhang,C.
  TITLE     Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression
  JOURNAL   J Cell Mol Med 28 (6), e18164 (2024)
   PUBMED   38445807
  REMARK    GeneRIF: Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Lee,S.O., Kelliher,J.L., Song,W., Tengler,K., Sarkar,A., Dray,E.
            and Leung,J.W.C.
  TITLE     UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination
            and DNA repair
  JOURNAL   J Biol Chem 299 (8), 105043 (2023)
   PUBMED   37451480
  REMARK    GeneRIF: UBA80 and UBA52 fine-tune RNF168-dependent histone
            ubiquitination and DNA repair.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Eastham,M.J., Pelava,A., Wells,G.R., Watkins,N.J. and Schneider,C.
  TITLE     RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion Proteins,
            Are Not Essential for p53 Signalling
  JOURNAL   Biomolecules 13 (6), 898 (2023)
   PUBMED   37371478
  REMARK    GeneRIF: RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion
            Proteins, Are Not Essential for p53 Signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin/52-residue ribosomal protein fusion gene
            subfamily (UbA52) is composed primarily of processed pseudogenes
  JOURNAL   Genomics 14 (2), 520-522 (1992)
   PUBMED   1330885
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin-52 amino acid fusion protein gene shares
            several structural features with mammalian ribosomal protein genes
  JOURNAL   Nucleic Acids Res 19 (5), 1035-1040 (1991)
   PUBMED   1850507
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Monia,B.P., Ecker,D.J., Jonnalagadda,S., Marsh,J., Gotlib,L.,
            Butt,T.R. and Crooke,S.T.
  TITLE     Gene synthesis, expression, and processing of human ubiquitin
            carboxyl extension proteins
  JOURNAL   J Biol Chem 264 (7), 4093-4103 (1989)
   PUBMED   2537304
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Salvesen,G., Lloyd,C. and Farley,D.
  TITLE     cDNA encoding a human homolog of yeast ubiquitin 1
  JOURNAL   Nucleic Acids Res 15 (13), 5485 (1987)
   PUBMED   3037496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BQ428688.1, CB124676.1, BQ428515.1, AF545864.1,
            BU677484.1 and AC005253.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ubiquitin is a highly conserved nuclear and cytoplasmic
            protein that has a major role in targeting cellular proteins for
            degradation by the 26S proteosome. It is also involved in the
            maintenance of chromatin structure, the regulation of gene
            expression, and the stress response. Ubiquitin is synthesized as a
            precursor protein consisting of either polyubiquitin chains or a
            single ubiquitin moiety fused to an unrelated protein. This gene
            encodes a fusion protein consisting of ubiquitin at the N terminus
            and ribosomal protein L40 at the C terminus, a C-terminal extension
            protein (CEP). Multiple processed pseudogenes derived from this
            gene are present in the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.230820.1,
                                           SRR1660807.99101.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442744.7/ ENSP00000388107.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..128
                     /product="ubiquitin-ribosomal protein eL40 fusion protein
                     isoform 1 precursor"
                     /note="ubiquitin-52 amino acid fusion protein; ubiquitin
                     carboxyl extension protein 52; ubiquitin-CEP52;
                     ubiquitin-60S ribosomal protein L40; ubiquitin-ribosomal
                     protein eL40 fusion protein"
                     /calculated_mol_wt=14597
     mat_peptide     1..76
                     /product="Ubiquitin. /id=PRO_0000396433"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=8565
     Region          1..76
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(6..9,11,34..37,40,42,44,46..49,68..76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(8..12,31..35,40,42,44,46..49,68,70..76)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            54
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000269|PubMed:24660806,
                     ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
                     ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291;
                     propagated from UniProtKB/Swiss-Prot (P62987.2)"
     Site            68
                     /site_type="other"
                     /note="Essential for function; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            72
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     mat_peptide     77..128
                     /product="Large ribosomal subunit protein eL40.
                     /id=PRO_0000396434"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=6182
     Region          79..126
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     Site            98
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:39048817,
                     ECO:0000269|PubMed:39103523; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     CDS             1..128
                     /gene="UBA52"
                     /gene_synonym="CEP52; HUBCEP52; L40; RPL40"
                     /coded_by="NM_001033930.3:62..448"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12382.1"
                     /db_xref="GeneID:7311"
                     /db_xref="HGNC:HGNC:12458"
                     /db_xref="MIM:191321"
ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggiiep slrqlaqkyn cdkmicrkcy arlhpravnc rkkkcghtnn
      121 lrpkkkvk
//
LOCUS       NP_001336249             349 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001336249 XP_005265073
VERSION     NP_001336249.1
DBSOURCE    REFSEQ: accession NM_001349320.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Li,F., Niu,M., Qin,K., Guo,R., Yi,Y., Xu,J., Li,L., Xie,S., Fu,M.,
            Wen,N., Liao,W. and Xiao,Z.J.
  TITLE     FBXL2 promotes E47 protein instability to inhibit breast cancer
            stemness and paclitaxel resistance
  JOURNAL   Oncogene 42 (5), 339-350 (2023)
   PUBMED   36460773
  REMARK    GeneRIF: FBXL2 promotes E47 protein instability to inhibit breast
            cancer stemness and paclitaxel resistance.
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Niu,M., Xu,J., Liu,Y., Li,Y., He,T., Ding,L., He,Y., Yi,Y., Li,F.,
            Guo,R., Gao,Y., Li,R., Li,L., Fu,M., Hu,Q., Luo,Y., Zhang,C.,
            Qin,K., Yi,J., Yu,S., Yang,J., Chen,H., Wang,L., Li,Z., Dong,B.,
            Qi,S., Ouyang,L., Zhang,Y., Cao,Y. and Xiao,Z.J.
  TITLE     FBXL2 counteracts Grp94 to destabilize EGFR and inhibit EGFR-driven
            NSCLC growth
  JOURNAL   Nat Commun 12 (1), 5919 (2021)
   PUBMED   34635651
  REMARK    GeneRIF: FBXL2 counteracts Grp94 to destabilize EGFR and inhibit
            EGFR-driven NSCLC growth.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Wang,C., Gale,M. Jr., Keller,B.C., Huang,H., Brown,M.S.,
            Goldstein,J.L. and Ye,J.
  TITLE     Identification of FBL2 as a geranylgeranylated cellular protein
            required for hepatitis C virus RNA replication
  JOURNAL   Mol Cell 18 (4), 425-434 (2005)
   PUBMED   15893726
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Ilyin,G.P., Rialland,M., Glaise,D. and Guguen-Guillouzo,C.
  TITLE     Identification of a novel Skp2-like mammalian protein containing
            F-box and leucine-rich repeats
  JOURNAL   FEBS Lett 459 (1), 75-79 (1999)
   PUBMED   10508920
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC123900.2 and AC122176.2.
            
            On Mar 11, 2017 this sequence version replaced XP_005265073.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbls class and, in addition to an F-box, contains 12 tandem
            leucine-rich repeats. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (5), as well as variants 4 and 6,
            encodes isoform 4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.55050.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..349
                     /product="F-box/LRR-repeat protein 2 isoform 4"
                     /note="F-box protein containing leucine-rich repeats;
                     F-box/LRR-repeat protein 2; F-box protein FBL2/FBL3"
                     /calculated_mol_wt=38765
     Region          27..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          53..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          63..293
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          79..104
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          105..130
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          131..156
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          157..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          183..208
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          209..259
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          269..288
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..349
                     /gene="FBXL2"
                     /gene_synonym="FBL2; FBL3"
                     /coded_by="NM_001349320.2:406..1455"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:25827"
                     /db_xref="HGNC:HGNC:13598"
                     /db_xref="MIM:605652"
ORIGIN      
        1 mdaqksltvr llffstcysl srfcsklkhl dltscvsitn sslkgisegc rnleylnlsw
       61 cdqitkdgie alvrgcrglk alllrgctql edealkhiqn ychelvslnl qscsritdeg
      121 vvqicrgchr lqalclsgcs nltdasltal glncprlqil eaarcshltd agftllarnc
      181 helekmdlee cilitdstli qlsihcpklq alvslsfsdi ihllkmkeps hhnkklfgfs
      241 fckslshcel itddgilhls nstcgherlr vleldnclli tdvalehlen crglerlely
      301 dcqqvtragi krmraqlphv kvhayfapvt pptavagsgq rlcrccvil
//
LOCUS       NP_002785                201 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-2 isoform 1 [Homo sapiens].
ACCESSION   NP_002785
VERSION     NP_002785.1
DBSOURCE    REFSEQ: accession NM_002794.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Nothwang,H.G., Tamura,T., Tanaka,K. and Ichihara,A.
  TITLE     Sequence analyses and inter-species comparisons of three novel
            human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine
            potential proteolytic active-site residues
  JOURNAL   Biochim Biophys Acta 1219 (2), 361-368 (1994)
   PUBMED   7918633
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354864.16, BC101836.1,
            AL157951.5 and BM664618.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. Multiple alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.4284323.1,
                                           SRR14243140.4470568.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373237.4/ ENSP00000362334.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..201
                     /product="proteasome subunit beta type-2 isoform 1"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit C7-I; multicatalytic
                     endopeptidase complex subunit C7-1; proteasome component
                     C7-I; proteasome subunit, beta type, 2; proteasome beta 2
                     subunit; multicatalytic endopeptidase complex subunit
                     C7-I; proteasome subunit beta 2; proteasome subunit beta4;
                     beta-4; proteasome (prosome, macropain) subunit, beta
                     type, 2; testicular tissue protein Li 152; proteasome
                     subunit beta-4"
                     /calculated_mol_wt=22705
     Region          1..192
                     /region_name="proteasome_beta_type_2"
                     /note="proteasome beta type-2 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03758"
                     /db_xref="CDD:239727"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49721.1)"
     CDS             1..201
                     /gene="PSMB2"
                     /gene_synonym="HC7-I"
                     /coded_by="NM_002794.5:95..700"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS394.1"
                     /db_xref="GeneID:5690"
                     /db_xref="HGNC:HGNC:9539"
                     /db_xref="MIM:602175"
ORIGIN      
        1 meyligiqgp dyvlvasdrv aasnivqmkd dhdkmfkmse killlcvgea gdtvqfaeyi
       61 qknvqlykmr ngyelsptaa anftrrnlad clrsrtpyhv nlllagydeh egpalyymdy
      121 laalakapfa ahgygafltl sildryytpt isreravell rkcleelqkr filnlptfsv
      181 riidkngihd ldnisfpkqg s
//
LOCUS       NP_001341603             404 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-1 complex subunit gamma-like 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001341603
VERSION     NP_001341603.1
DBSOURCE    REFSEQ: accession NM_001354674.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Tavares,L.A., da Silva,E.M., da Silva-Januario,M.E., Januario,Y.C.,
            de Cavalho,J.V., Czernisz,E.S., Mardones,G.A. and daSilva,L.L.
  TITLE     CD4 downregulation by the HIV-1 protein Nef reveals distinct roles
            for the gamma1 and gamma2 subunits of the AP-1 complex in protein
            trafficking
  JOURNAL   J Cell Sci 130 (2), 429-443 (2017)
   PUBMED   27909244
  REMARK    GeneRIF: Depletion of the gamma2 or mu1A (AP1M1) subunits of AP-1,
            but not of gamma1 (AP1G1), precludes Nef-mediated lysosomal
            degradation of CD4.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Jurgens,M.C., Voros,J., Rautureau,G.J., Shepherd,D.A., Pye,V.E.,
            Muldoon,J., Johnson,C.M., Ashcroft,A.E., Freund,S.M. and
            Ferguson,N.
  TITLE     The hepatitis B virus preS1 domain hijacks host trafficking
            proteins by motif mimicry
  JOURNAL   Nat Chem Biol 9 (9), 540-547 (2013)
   PUBMED   23851574
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Mattera,R., Ritter,B., Sidhu,S.S., McPherson,P.S. and
            Bonifacino,J.S.
  TITLE     Definition of the consensus motif recognized by gamma-adaptin ear
            domains
  JOURNAL   J Biol Chem 279 (9), 8018-8028 (2004)
   PUBMED   14665628
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Page,L.J., Sowerby,P.J., Lui,W.W. and Robinson,M.S.
  TITLE     Gamma-synergin: an EH domain-containing protein that interacts with
            gamma-adaptin
  JOURNAL   J Cell Biol 146 (5), 993-1004 (1999)
   PUBMED   10477754
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Lewin,D.A., Sheff,D., Ooi,C.E., Whitney,J.A., Yamamoto,E.,
            Chicione,L.M., Webster,P., Bonifacino,J.S. and Mellman,I.
  TITLE     Cloning, expression, and localization of a novel gamma-adaptin-like
            molecule
  JOURNAL   FEBS Lett 435 (2-3), 263-268 (1998)
   PUBMED   9762922
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Takatsu,H., Sakurai,M., Shin,H.W., Murakami,K. and Nakayama,K.
  TITLE     Identification and characterization of novel clathrin
            adaptor-related proteins
  JOURNAL   J Biol Chem 273 (38), 24693-24700 (1998)
   PUBMED   9733768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135999.4 and AK304682.1.
            
            Summary: Adaptins are important components of clathrin-coated
            vesicles transporting ligand-receptor complexes from the plasma
            membrane or from the trans-Golgi network to lysosomes. The adaptin
            family of proteins is composed of four classes of molecules named
            alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together
            with medium and small subunits, form a heterotetrameric complex
            called an adaptor, whose role is to promote the formation of
            clathrin-coated pits and vesicles. The protein encoded by this gene
            is a gamma-adaptin protein and it belongs to the adaptor complexes
            large subunits family. This protein along with the complex is
            thought to function at some trafficking step in the complex
            pathways between the trans-Golgi network and the cell surface.
            [provided by RefSeq, Aug 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.136313.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..404
                     /product="AP-1 complex subunit gamma-like 2 isoform 2"
                     /note="gamma2-adaptin;
                     clathrin-associated/assembly/adaptor protein, large,
                     gamma-2; AP-1 complex subunit gamma-like 2; adaptor
                     related protein complex 1 gamma 2 subunit"
                     /calculated_mol_wt=44407
     Region          <1..194
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          291..399
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     CDS             1..404
                     /gene="AP1G2"
                     /gene_synonym="G2AD"
                     /coded_by="NM_001354674.2:1281..2495"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:8906"
                     /db_xref="HGNC:HGNC:556"
                     /db_xref="MIM:603534"
ORIGIN      
        1 mmqelqafle scppdlradc asgillaaer faptkrwhid tilhvlttag thvrddavan
       61 ltqliggaqe lhaysvrrly nalaedisqq plvqvaawci geygdlllag nceeieplqv
      121 deeevlalle kvlqshmslp atrgyaltal mklstrlcgd nnrirqvvsi ygscldvelq
      181 qraveydtlf rkydhmraai lekmplverd gpqadeeake skeaaqlsea apvptepqas
      241 qlldlldlld gasgdvqhpp hldpspggal vhlldlpcvp pppapipdlk vferegvqln
      301 lsfirppenp alllititat nfsegdvthf icqaavpksl qlqlqapsgn tvpargglpi
      361 tqlfrilnpn kaplrlklrl tydhfhqsvq eifevnnlpv eswq
//
LOCUS       NP_001356510             646 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform y [Homo sapiens].
ACCESSION   NP_001356510 XP_005266802
VERSION     NP_001356510.1
DBSOURCE    REFSEQ: accession NM_001369581.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_005266802.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.138333.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..646
                     /product="transcription factor 4 isoform y"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68839
     Region          537..621
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(545,549,551..553,555,560,581..582)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(558..559,562..563,565..566,569,573,583,586,590,593,
                     596..601)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..646
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369581.1:151..2091"
                     /note="isoform y is encoded by transcript variant 41"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqs llggdmdmgn pgtlsptkpg
      121 sqyyqyssnn prrrplhssa mevqtkkvrk vppglpssvy apsastadyn rdspgypssk
      181 patstfpssf fmqdghhssd pwssssgmnq pgyagmlgns shipqsssyc slhpherlsy
      241 pshssadins slppmstfhr sgtnhystss ctppangtds imanrgsgaa gssqtgdalg
      301 kalasiyspd htnnsfssnp stpvgsppsl sagtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit rsrssnndde dltpeqkaer
      541 ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv
      601 rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_001547                756 aa            linear   PRI 20-NOV-2025
DEFINITION  inhibitor of nuclear factor kappa-B kinase subunit beta isoform 1
            [Homo sapiens].
ACCESSION   NP_001547 XP_032491
VERSION     NP_001547.1
DBSOURCE    REFSEQ: accession NM_001556.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 756)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 756)
  AUTHORS   Chang,X., Guo,Y., Zhang,Q., Zheng,X., Cui,X., Hu,J., Zhang,Z.,
            Zhang,F. and Wang,X.
  TITLE     GRP78 recognizes EV-F 3D protein and activates NF-kappaB to repress
            virus replication by interacting with CHUK/IKBKB
  JOURNAL   J Virol 98 (6), e0026824 (2024)
   PUBMED   38775480
  REMARK    GeneRIF: GRP78 recognizes EV-F 3D protein and activates NF-kappaB
            to repress virus replication by interacting with CHUK/IKBKB.
REFERENCE   3  (residues 1 to 756)
  AUTHORS   Lan,L., Huang,C., Liu,D., Cheng,Y., Tang,R., Gu,J., Geng,L.,
            Cheng,Y. and Gong,S.
  TITLE     WNT2B activates macrophages via NF-kappaB signaling pathway in
            inflammatory bowel disease
  JOURNAL   FASEB J 38 (6), e23551 (2024)
   PUBMED   38489235
REFERENCE   4  (residues 1 to 756)
  AUTHORS   Iguchi,Y., Takahashi,Y., Li,J., Araki,K., Amakusa,Y., Kawakami,Y.,
            Kobayashi,K., Yokoi,S. and Katsuno,M.
  TITLE     IkappaB kinase phosphorylates cytoplasmic TDP-43 and promotes its
            proteasome degradation
  JOURNAL   J Cell Biol 223 (2) (2024)
   PUBMED   38197897
  REMARK    GeneRIF: IkappaB kinase phosphorylates cytoplasmic TDP-43 and
            promotes its proteasome degradation.
REFERENCE   5  (residues 1 to 756)
  AUTHORS   Mahmood,A.A., Abbas,R.F. and Hussein,H.M.
  TITLE     Novel association between single-nucleotide polymorphisms of
            IKKbeta at rs17875746 and rs12676482 and periodontitis
  JOURNAL   Dent Med Probl 60 (4), 627-634 (2023)
   PUBMED   37930783
  REMARK    GeneRIF: Novel association between single-nucleotide polymorphisms
            of IKKbeta at rs17875746 and rs12676482 and periodontitis.
REFERENCE   6  (residues 1 to 756)
  AUTHORS   DiDonato,J., Mercurio,F., Rosette,C., Wu-Li,J., Suyang,H., Ghosh,S.
            and Karin,M.
  TITLE     Mapping of the inducible IkappaB phosphorylation sites that signal
            its ubiquitination and degradation
  JOURNAL   Mol Cell Biol 16 (4), 1295-1304 (1996)
   PUBMED   8657102
REFERENCE   7  (residues 1 to 756)
  AUTHORS   Chen,Z.J., Parent,L. and Maniatis,T.
  TITLE     Site-specific phosphorylation of IkappaBalpha by a novel
            ubiquitination-dependent protein kinase activity
  JOURNAL   Cell 84 (6), 853-862 (1996)
   PUBMED   8601309
REFERENCE   8  (residues 1 to 756)
  AUTHORS   Hiscott,J., Marois,J., Garoufalis,J., D'Addario,M., Roulston,A.,
            Kwan,I., Pepin,N., Lacoste,J., Nguyen,H., Bensi,G. et al.
  TITLE     Characterization of a functional NF-kappa B site in the human
            interleukin 1 beta promoter: evidence for a positive autoregulatory
            loop
  JOURNAL   Mol Cell Biol 13 (10), 6231-6240 (1993)
   PUBMED   8413223
REFERENCE   9  (residues 1 to 756)
  AUTHORS   Ganchi,P.A., Sun,S.C., Greene,W.C. and Ballard,D.W.
  TITLE     I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B
            p65 and requires the transactivation domain to inhibit NF-kappa B
            p65 DNA binding
  JOURNAL   Mol Biol Cell 3 (12), 1339-1352 (1992)
   PUBMED   1493333
REFERENCE   10 (residues 1 to 756)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA709000.1, AF080158.1,
            BC090865.1 and AI379342.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 3, 2004 this sequence version replaced XP_032491.4.
            
            Summary: The protein encoded by this gene phosphorylates the
            inhibitor in the inhibitor/NF-kappa-B complex, causing dissociation
            of the inhibitor and activation of NF-kappa-B. The encoded protein
            itself is found in a complex of proteins. Several transcript
            variants, some protein-coding and some not, have been found for
            this gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.162535.1, AF080158.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000520810.6/ ENSP00000430684.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..756
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..756
                     /product="inhibitor of nuclear factor kappa-B kinase
                     subunit beta isoform 1"
                     /EC_number="2.7.11.1"
                     /EC_number="2.7.11.10"
                     /note="nuclear factor NF-kappa-B inhibitor kinase beta;
                     I-kappa-B kinase 2; I-kappa-B-kinase beta;
                     serine/threonine protein kinase IKBKB; nuclear factor
                     kappa B kinase subunit beta; inhibitor of kappa light
                     polypeptide gene enhancer in B-cells, kinase beta"
                     /calculated_mol_wt=86433
     Region          20..309
                     /region_name="STKc_IKK_beta"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta;
                     cd14038"
                     /db_xref="CDD:270940"
     Site            order(21..25,29,42,44,74,96..99,103,105,145,147,149..150,
                     152,166,169,184..187)
                     /site_type="active"
                     /db_xref="CDD:270940"
     Site            order(21..25,29,42,44,74,96..99,103,145,147,149..150,152,
                     166)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270940"
     Site            order(25,103,105,145,147,149,169,184..187)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270940"
     Site            order(109,111,114..115,118,219,224,252..253,255,261..264)
                     /site_type="other"
                     /note="SDD interface [polypeptide binding]"
                     /db_xref="CDD:270940"
     Site            order(121,123..124,158..159)
                     /site_type="other"
                     /note="ULD interface [polypeptide binding]"
                     /db_xref="CDD:270940"
     Site            165..187
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270940"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1 and PKC/PRKCZ.
                     /evidence=ECO:0000269|PubMed:10022904,
                     ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893;
                     propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Site            180
                     /site_type="acetylation"
                     /note="(Microbial infection) O-acetylthreonine, by
                     Yersinia YopJ. /evidence=ECO:0000269|PubMed:17116858;
                     propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1, PKC/PRKCZ and PDPK1.
                     /evidence=ECO:0000269|PubMed:10022904,
                     ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893,
                     ECO:0000269|PubMed:16207722; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            191
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:17114296; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            order(229,231..232,236)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:270940"
     Region          310..390
                     /region_name="Ubl_IKKA_like"
                     /note="ubiquitin-like (Ubl) domain found in inhibitor of
                     nuclear factor kappa-B kinases, IKK-alpha and IKK-beta,
                     and similar proteins; cd17046"
                     /db_xref="CDD:340566"
     Region          389..663
                     /region_name="IKBKB_SDD"
                     /note="IQBAL scaffold dimerization domain; pfam18397"
                     /db_xref="CDD:465745"
     Region          458..479
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Region          667..706
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:10195894,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; Phosphoserine, by
                     autocatalysis. /evidence=ECO:0000305|PubMed:10195894,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Site            682
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            697
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Region          706..742
                     /region_name="IKKbetaNEMObind"
                     /note="I-kappa-kinase-beta NEMO binding domain; pfam12179"
                     /db_xref="CDD:463485"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Region          737..742
                     /region_name="NEMO-binding.
                     /evidence=ECO:0000269|PubMed:12133833"
                     /note="propagated from UniProtKB/Swiss-Prot (O14920.1)"
     Site            740
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:10195894; propagated from
                     UniProtKB/Swiss-Prot (O14920.1)"
     CDS             1..756
                     /gene="IKBKB"
                     /gene_synonym="IKK-2; IKK-beta; IKK2; IKKB; IMD15; IMD15A;
                     IMD15B; NFKBIKB"
                     /coded_by="NM_001556.3:187..2457"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6128.1"
                     /db_xref="GeneID:3551"
                     /db_xref="HGNC:HGNC:5960"
                     /db_xref="MIM:603258"
ORIGIN      
        1 mswspslttq tcgawemker lgtggfgnvi rwhnqetgeq iaikqcrqel sprnrerwcl
       61 eiqimrrlth pnvvaardvp egmqnlapnd lpllameycq ggdlrkylnq fenccglreg
      121 ailtllsdia salrylhenr iihrdlkpen ivlqqgeqrl ihkiidlgya keldqgslct
      181 sfvgtlqyla pelleqqkyt vtvdywsfgt lafecitgfr pflpnwqpvq whskvrqkse
      241 vdivvsedln gtvkfssslp ypnnlnsvla erlekwlqlm lmwhprqrgt dptygpngcf
      301 kalddilnlk lvhilnmvtg tihtypvted eslqslkari qqdtgipeed qellqeagla
      361 lipdkpatqc isdgklnegh tldmdlvflf dnskityetq isprpqpesv scilqepkrn
      421 laffqlrkvw gqvwhsiqtl kedcnrlqqg qraammnllr nnsclskmkn smasmsqqlk
      481 akldffktsi qidlekyseq tefgitsdkl llawremeqa velcgrenev kllvermmal
      541 qtdivdlqrs pmgrkqggtl ddleeqarel yrrlrekprd qrtegdsqem vrlllqaiqs
      601 fekkvrviyt qlsktvvckq kalellpkve evvslmnede ktvvrlqekr qkelwnllki
      661 acskvrgpvs gspdsmnasr lsqpgqlmsq pstasnslpe pakkseelva eahnlctlle
      721 naiqdtvreq dqsftaldws wlqteeeehs cleqas
//
LOCUS       NP_001240312             204 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL15 isoform 1 [Homo sapiens].
ACCESSION   NP_001240312
VERSION     NP_001240312.1
DBSOURCE    REFSEQ: accession NM_001253383.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Wang,G., Qin,M., Zhang,B., Yan,Y., Yang,F., Chen,Q., Liu,Y.,
            Qiao,F. and Ni,Y.
  TITLE     Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification
  JOURNAL   Cell Biol Int 47 (10), 1749-1759 (2023)
   PUBMED   37431269
  REMARK    GeneRIF: Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification.
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Xu,C., He,X.Y., Ren,X.H., Han,D. and Cheng,S.X.
  TITLE     Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin in
            Living Circulating Tumor Cells at Single Cell Resolution To Study
            Tumor Heterogeneity
  JOURNAL   Anal Chem 94 (30), 10610-10616 (2022)
   PUBMED   35856393
  REMARK    GeneRIF: Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin
            in Living Circulating Tumor Cells at Single Cell Resolution To
            Study Tumor Heterogeneity.
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Wang,Q., Yang,C., Zhou,J., Wang,X., Wu,M. and Liu,Z.
  TITLE     Cloning and characterization of full-length human ribosomal protein
            L15 cDNA which was overexpressed in esophageal cancer
  JOURNAL   Gene 263 (1-2), 205-209 (2001)
   PUBMED   11223259
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC351786.1, DA205054.1 and
            AC124914.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L15E family of ribosomal proteins and a component of the 60S
            subunit. This gene shares sequence similarity with the yeast
            ribosomal protein YL10 gene. Elevated expression of this gene has
            been observed in esophageal tumors and gastric cancer tissues, and
            deletion of this gene has been observed in a Diamond-Blackfan
            anemia (DBA) patient. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (5) differs in the 5' UTR compared
            to variant 1. Variants 1-5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.243527.1,
                                           SRR1660809.125562.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..204
                     /product="large ribosomal subunit protein eL15 isoform 1"
                     /note="60S ribosomal protein L15; large ribosomal subunit
                     protein eL15"
                     /calculated_mol_wt=24015
     Region          2..191
                     /region_name="Ribosomal_L15e"
                     /note="Ribosomal L15; pfam00827"
                     /db_xref="CDD:459950"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61314; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P61313.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Region          165..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61313.2)"
     CDS             1..204
                     /gene="RPL15"
                     /gene_synonym="DBA12; EC45; eL15; L15; RPL10; RPLY10;
                     RPYL10"
                     /coded_by="NM_001253383.3:119..733"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2640.1"
                     /db_xref="GeneID:6138"
                     /db_xref="HGNC:HGNC:10306"
                     /db_xref="MIM:604174"
ORIGIN      
        1 mgaykyiqel wrkkqsdvmr fllrvrcwqy rqlsalhrap rptrpdkarr lgykakqgyv
       61 iyrirvrrgg rkrpvpkgat ygkpvhhgvn qlkfarslqs vaeeragrhc galrvlnsyw
      121 vgedstykff evilidpfhk airrnpdtqw itkpvhkhre mrgltsagrk srglgkghkf
      181 hhtiggsrra awrrrntlql hryr
//
LOCUS       NP_001275653             899 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit isoform b [Homo sapiens].
ACCESSION   NP_001275653 NP_001070961 XP_005269919
VERSION     NP_001275653.1
DBSOURCE    REFSEQ: accession NM_001288724.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 899)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 899)
  AUTHORS   De Paolis,V., Troisi,V., Bordin,A., Pagano,F., Caputo,V. and
            Parisi,C.
  TITLE     Unconventional p65/p52 NF-kappaB module regulates key tumor
            microenvironment-related genes in breast tumor-associated
            macrophages (TAMs)
  JOURNAL   Life Sci 357, 123059 (2024)
   PUBMED   39278618
  REMARK    GeneRIF: Unconventional p65/p52 NF-kappaB module regulates key
            tumor microenvironment-related genes in breast tumor-associated
            macrophages (TAMs).
REFERENCE   3  (residues 1 to 899)
  AUTHORS   Vallabhapurapu,S. and Karin,M.
  TITLE     Regulation and function of NF-kappaB transcription factors in the
            immune system
  JOURNAL   Annu Rev Immunol 27, 693-733 (2009)
   PUBMED   19302050
  REMARK    Review article
REFERENCE   4  (residues 1 to 899)
  AUTHORS   Heusch,M., Lin,L., Geleziunas,R. and Greene,W.C.
  TITLE     The generation of nfkb2 p52: mechanism and efficiency
  JOURNAL   Oncogene 18 (46), 6201-6208 (1999)
   PUBMED   10597218
REFERENCE   5  (residues 1 to 899)
  AUTHORS   Lombardi,L., Ciana,P., Cappellini,C., Trecca,D., Guerrini,L.,
            Migliazza,A., Maiolo,A.T. and Neri,A.
  TITLE     Structural and functional characterization of the promoter regions
            of the NFKB2 gene
  JOURNAL   Nucleic Acids Res 23 (12), 2328-2336 (1995)
   PUBMED   7541912
REFERENCE   6  (residues 1 to 899)
  AUTHORS   Liptay,S., Schmid,R.M., Nabel,E.G. and Nabel,G.J.
  TITLE     Transcriptional regulation of NF-kappa B2: evidence for kappa
            B-mediated positive and negative autoregulation
  JOURNAL   Mol Cell Biol 14 (12), 7695-7703 (1994)
   PUBMED   7969113
REFERENCE   7  (residues 1 to 899)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
REFERENCE   8  (residues 1 to 899)
  AUTHORS   Bours,V., Burd,P.R., Brown,K., Villalobos,J., Park,S., Ryseck,R.P.,
            Bravo,R., Kelly,K. and Siebenlist,U.
  TITLE     A novel mitogen-inducible gene product related to p50/p105-NF-kappa
            B participates in transactivation through a kappa B site
  JOURNAL   Mol Cell Biol 12 (2), 685-695 (1992)
   PUBMED   1531086
REFERENCE   9  (residues 1 to 899)
  AUTHORS   Schreck,R., Albermann,K. and Baeuerle,P.A.
  TITLE     Nuclear factor kappa B: an oxidative stress-responsive
            transcription factor of eukaryotic cells (a review)
  JOURNAL   Free Radic Res Commun 17 (4), 221-237 (1992)
   PUBMED   1473734
  REMARK    Review article
REFERENCE   10 (residues 1 to 899)
  AUTHORS   Schmid,R.M., Perkins,N.D., Duckett,C.S., Andrews,P.C. and
            Nabel,G.J.
  TITLE     Cloning of an NF-kappa B subunit which stimulates HIV transcription
            in synergy with p65
  JOURNAL   Nature 352 (6337), 733-736 (1991)
   PUBMED   1876189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB091090.1, AL121928.13 and
            BC002844.2.
            
            Summary: This gene encodes a subunit of the transcription factor
            complex nuclear factor-kappa-B (NFkB). The NFkB complex is
            expressed in numerous cell types and functions as a central
            activator of genes involved in inflammation and immune function.
            The protein encoded by this gene can function as both a
            transcriptional activator or repressor depending on its
            dimerization partner. The p100 full-length protein is
            co-translationally processed into a p52 active form. Chromosomal
            rearrangements and translocations of this locus have been observed
            in B cell lymphomas, some of which may result in the formation of
            fusion proteins. There is a pseudogene for this gene on chromosome
            18. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            an alternate in-frame splice site in the 3' coding region, compared
            to variant 1. The encoded isoform (b) is shorter than isoform a.
            Variants 2, 3, and 4 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002844.2, SRR7346977.2076849.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..899
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..899
                     /product="nuclear factor NF-kappa-B p100 subunit isoform
                     b"
                     /note="nuclear factor NF-kappa-B p100 subunit; oncogene
                     Lyt-10; DNA-binding factor KBF2; lymphocyte translocation
                     chromosome 10 protein; transcription factor NFKB2; NFKB,
                     p52/p100 subunit; nuclear factor Kappa-B, subunit 2;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells 2 (p49/p100); nuclear factor of Kappa light chain
                     gene enhancer in B cells 2; nuclear factor NF-kappa-B p52
                     subunit"
                     /calculated_mol_wt=96547
     mat_peptide     1..454
                     /product="Nuclear factor NF-kappa-B p52 subunit.
                     /id=PRO_0000030322"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
                     /calculated_mol_wt=49423
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          337..341
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          346..377
                     /region_name="GRR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          438..706
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed);
                     propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            order(487,489,493..494,497..499,501..502,506,509,524,526,
                     528,532..533,536..538,540..541,545,548,557,559,561,
                     565..566,571..573,575..576,580,583)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          487..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          487..519
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            490..491
                     /site_type="other"
                     /note="Breakpoint for translocation to form NFKB2-IGHA1
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          526..557
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..555
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..591
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..586
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(599,601,605..606,609..611,613..614,618,621,630,633,
                     635,639..640,643..645,647..648,652,655,665,667,669,
                     673..674,677..679,681..682,686,689,698)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          599..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          599..628
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          633..665
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..663
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          667..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          667..696
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          698..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          729..758
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          774..849
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            865
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     CDS             1..899
                     /gene="NFKB2"
                     /gene_synonym="CVID10; H2TF1; LYT-10; LYT10; NF-kB2; p100;
                     p49/p100; p52"
                     /coded_by="NM_001288724.1:564..3263"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS41565.1"
                     /db_xref="GeneID:4791"
                     /db_xref="HGNC:HGNC:7795"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggaaggygga ggggslgffp sslayspyqs gagpmgcypg ggggaqmaat vpsrdsgeea
      421 aepsapsrtp qcepqapeml qrareynarl fglaqrsara lldygvtada rallagqrhl
      481 ltaqdengdt plhlaiihgq tsvieqivyv ihhaqdlgvv nltnhlhqtp lhlavitgqt
      541 svvsfllrvg adpalldrhg dsamhlalra gagapellra llqsgapavp qllhmpdfeg
      601 lypvhlavra rspecldllv dsgaeveate rqggrtalhl atemeelglv thlvtklran
      661 vnartfagnt plhlaaglgy ptltrlllka gadihaenee plcplpsppt sdsdsdsegp
      721 ekdtrssfrg htpldltcst kvktlllnaa qntmeppltp pspagpglsl gdtalqnleq
      781 lldgpeaqgs waelaerlgl rslvdtyrqt tspsgsllrs yelaggdlag llealsdmgl
      841 eegvrllrgp etrdklpste vkedsaygsq sveqeaeklg pppeppgglc hghpqpqvh
//
LOCUS       NP_066283                382 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1A isoform 1 [Homo sapiens].
ACCESSION   NP_066283
VERSION     NP_066283.1
DBSOURCE    REFSEQ: accession NM_021003.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Cheng,P., Wang,Y., Wu,Q., Zhang,H., Fang,W. and Feng,F.
  TITLE     Role of TRIM59 in regulating PPM1A in the pathogenesis of silicosis
            and the intervention effect of tanshinone IIA
  JOURNAL   Biomed Pharmacother 177, 117014 (2024)
   PUBMED   38908195
  REMARK    GeneRIF: Role of TRIM59 in regulating PPM1A in the pathogenesis of
            silicosis and the intervention effect of tanshinone IIA.
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Weon,S., Jo,S., Nam,B., Choi,S.H., Park,Y.S., Kim,Y.G. and Kim,T.H.
  TITLE     Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway
  JOURNAL   J Cell Mol Med 27 (5), 650-658 (2023)
   PUBMED   36756789
  REMARK    GeneRIF: Extracellular PPM1A promotes mineralization of osteoblasts
            differentiation in ankylosing spondylitis via the FOXO1A-RUNX2
            pathway.
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Feng,D., Zhou,J., Liu,H., Wu,X., Li,F., Zhao,J., Zhang,Y., Wang,L.,
            Chao,M., Wang,Q., Qin,H., Ge,S., Liu,Q., Zhang,J. and Qu,Y.
  TITLE     Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain barrier
            disruption after subarachnoid hemorrhage
  JOURNAL   Sci Adv 8 (39), eabq2423 (2022)
   PUBMED   36179025
  REMARK    GeneRIF: Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain
            barrier disruption after subarachnoid hemorrhage.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Liu,C., Sun,W., Yang,K. and Xia,B.
  TITLE     Knockdown of TRIM65 suppressed the proliferation and invasiveness
            of gastric cancer cells by restricting the ubiquitin degradation of
            PPM1A
  JOURNAL   Exp Cell Res 416 (2), 113154 (2022)
   PUBMED   35421368
  REMARK    GeneRIF: Knockdown of TRIM65 suppressed the proliferation and
            invasiveness of gastric cancer cells by restricting the ubiquitin
            degradation of PPM1A.
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Fjeld,C.C. and Denu,J.M.
  TITLE     Kinetic analysis of human serine/threonine protein phosphatase
            2Calpha
  JOURNAL   J Biol Chem 274 (29), 20336-20343 (1999)
   PUBMED   10400656
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Takekawa,M., Maeda,T. and Saito,H.
  TITLE     Protein phosphatase 2Calpha inhibits the human stress-responsive
            p38 and JNK MAPK pathways
  JOURNAL   EMBO J 17 (16), 4744-4752 (1998)
   PUBMED   9707433
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Das,A.K., Helps,N.R., Cohen,P.T. and Barford,D.
  TITLE     Crystal structure of the protein serine/threonine phosphatase 2C at
            2.0 A resolution
  JOURNAL   EMBO J 15 (24), 6798-6809 (1996)
   PUBMED   9003755
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Redpath,N.T., Price,N.T., Severinov,K.V. and Proud,C.G.
  TITLE     Regulation of elongation factor-2 by multisite phosphorylation
  JOURNAL   Eur J Biochem 213 (2), 689-699 (1993)
   PUBMED   8386634
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Mann,D.J., Campbell,D.G., McGowan,C.H. and Cohen,P.T.
  TITLE     Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and
            comparative analysis of amino acid sequences
  JOURNAL   Biochim Biophys Acta 1130 (1), 100-104 (1992)
   PUBMED   1311954
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157756.3, DA439296.1,
            BC063243.1, AL132778.6 and AI076736.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the PP2C
            family of Ser/Thr protein phosphatases. PP2C family members are
            known to be negative regulators of cell stress response pathways.
            This phosphatase dephosphorylates, and negatively regulates the
            activities of, MAP kinases and MAP kinase kinases. It has been
            shown to inhibit the activation of p38 and JNK kinase cascades
            induced by environmental stresses. This phosphatase can also
            dephosphorylate cyclin-dependent kinases, and thus may be involved
            in cell cycle control. Overexpression of this phosphatase is
            reported to activate the expression of the tumor suppressor gene
            TP53/p53, which leads to G2/M cell cycle arrest and apoptosis.
            Three alternatively spliced transcript variants encoding distinct
            isoforms have been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.219432.1,
                                           SRR1803614.109713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395076.9/ ENSP00000378514.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..382
                     /product="protein phosphatase 1A isoform 1"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 1A"
                     /calculated_mol_wt=42317
     Region          23..291
                     /region_name="PP2Cc"
                     /note="Serine/threonine phosphatases, family 2C, catalytic
                     domain; The protein architecture and deduced catalytic
                     mechanism of PP2C phosphatases are similar to the PP1,
                     PP2A, PP2B family of protein Ser/Thr phosphatases, with
                     which PP2C shares no sequence...; cd00143"
                     /db_xref="CDD:238083"
     Site            order(33,37..38,60..62,239,282)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Region          285..363
                     /region_name="PP2C_C"
                     /note="Protein serine/threonine phosphatase 2C, C-terminal
                     domain; pfam07830"
                     /db_xref="CDD:429684"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35813.1)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49443; propagated from
                     UniProtKB/Swiss-Prot (P35813.1)"
     CDS             1..382
                     /gene="PPM1A"
                     /gene_synonym="PP2C-ALPHA; PP2CA; PP2Calpha"
                     /coded_by="NM_021003.5:478..1626"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9744.1"
                     /db_xref="GeneID:5494"
                     /db_xref="HGNC:HGNC:9275"
                     /db_xref="MIM:606108"
ORIGIN      
        1 mgafldkpkm ekhnaqgqgn glryglssmq gwrvemedah taviglpsgl eswsffavyd
       61 ghagsqvaky ccehlldhit nnqdfkgsag apsvenvkng irtgfleide hmrvmsekkh
      121 gadrsgstav gvlispqhty fincgdsrgl lcrnrkvhff tqdhkpsnpl ekeriqnagg
      181 svmiqrvngs lavsralgdf dykcvhgkgp teqlvspepe vhdierseed dqfiilacdg
      241 iwdvmgneel cdfvrsrlev tddlekvcne vvdtclykgs rdnmsvilic fpnapkvspe
      301 avkkeaeldk ylecrveeii kkqgegvpdl vhvmrtlase nipslppgge laskrnviea
      361 vynrlnpykn ddtdststdd mw
//
LOCUS       NP_006051                519 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 1 [Homo sapiens].
ACCESSION   NP_006051 NP_061033
VERSION     NP_006051.1
DBSOURCE    REFSEQ: accession NM_006060.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 519)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 519)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 519)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 519)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 519)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 519)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 519)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 519)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 519)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 519)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM148203.1, U40462.1 and
            JX459579.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 8, 2003 this sequence version replaced NP_061033.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (1) encodes isoform 1 (also known
            as Ik-1 as described in PMID:12937159). This isoform contains four
            N-terminal zinc finger motifs, binds DNA, and is localized to the
            nucleus.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.403115.1,
                                           SRR14038196.2982020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331340.8/ ENSP00000331614.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..519
                     /product="DNA-binding protein Ikaros isoform 1"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=57397
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          119..139
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(124,126,128,130..131,134..135,138,152,154,158..159,
                     162..163,166,180,182,184,186..187,190..191,194)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          132..156
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          147..167
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          154..163
                     /region_name="Required for both high-affinity DNA binding
                     and pericentromeric heterochromatin localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Region          159..184
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            159
                     /site_type="other"
                     /note="Required for both pericentromeric heterochromatin
                     localization and complete DNA binding.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            162
                     /site_type="other"
                     /note="Required for both pericentromeric heterochromatin
                     localization and complete DNA binding.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          175..195
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          180..195
                     /region_name="Required for both high-affinity DNA binding
                     and pericentromeric heterochromatin localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Site            188
                     /site_type="other"
                     /note="Required for both pericentromeric heterochromatin
                     localization and DNA binding. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Region          191..212
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          203..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            361
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23071339,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:23071339,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          381..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            427
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          468..471
                     /region_name="Required for binding PP1CC.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13422.1)"
     CDS             1..519
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_006060.6:222..1781"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75596.1"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvasnvkve
       61 tqsdeengra cemngeecae dlrmldasge kmngshrdqg ssalsgvggi rlpngklkcd
      121 icgiicigpn vlmvhkrsht gerpfqcnqc gasftqkgnl lrhiklhsge kpfkchlcny
      181 acrrrdaltg hlrthsvgkp hkcgycgrsy kqrssleehk erchnylesm glpgtlypvi
      241 keetnhsema edlckigser slvldrlasn vakrkssmpq kflgdkglsd tpydssasye
      301 kenemmkshv mdqainnain ylgaeslrpl vqtppggsev vpvispmyql hkplaegtpr
      361 snhsaqdsav enllllskak lvpsereasp snscqdstdt esnneeqrsg liyltnhiap
      421 harnglslke ehraydllra asensqdalr vvstsgeqmk vykcehcrvl fldhvmytih
      481 mgchgfrdpf ecnmcgyhsq dryefsshit rgehrfhms
//
LOCUS       NP_001275962             427 aa            linear   PRI 20-NOV-2025
DEFINITION  kallistatin isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001275962 XP_005267820
VERSION     NP_001275962.1
DBSOURCE    REFSEQ: accession NM_001289033.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Kim,H., Suh,G.J., Kwon,W.Y., Kim,K.S., Jung,Y.S., Kim,T. and
            Park,H.
  TITLE     Kallistatin deficiency exacerbates neuronal damage after cardiac
            arrest
  JOURNAL   Sci Rep 14 (1), 4279 (2024)
   PUBMED   38383562
  REMARK    GeneRIF: Kallistatin deficiency exacerbates neuronal damage after
            cardiac arrest.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Wang,Y., Chen,X.Y., Shang,K., Xu,Q., Li,Y.X., DU,Y. and Zhuan,L.
  TITLE     [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism]
  JOURNAL   Zhonghua Nan Ke Xue 28 (11), 976-984 (2022)
   PUBMED   37846113
  REMARK    GeneRIF: [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism].
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Cho,I., Lee,K.N., Joo,E., Kim,Y.M., Kim,T.E. and Park,K.H.
  TITLE     Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes
  JOURNAL   Am J Reprod Immunol 88 (3), e13584 (2022)
   PUBMED   35772987
  REMARK    GeneRIF: Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Krishna,S.M., Li,J., Wang,Y., Moran,C.S., Trollope,A., Huynh,P.,
            Jose,R., Biros,E., Ma,J. and Golledge,J.
  TITLE     Kallistatin limits abdominal aortic aneurysm by attenuating
            generation of reactive oxygen species and apoptosis
  JOURNAL   Sci Rep 11 (1), 17451 (2021)
   PUBMED   34465809
  REMARK    GeneRIF: Kallistatin limits abdominal aortic aneurysm by
            attenuating generation of reactive oxygen species and apoptosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Chen,L.M., Song,Q., Chao,L. and Chao,J.
  TITLE     Cellular localization of tissue kallikrein and kallistatin mRNAs in
            human kidney
  JOURNAL   Kidney Int 48 (3), 690-697 (1995)
   PUBMED   7474653
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Chai,K.X., Ward,D.C., Chao,J. and Chao,L.
  TITLE     Molecular cloning, sequence analysis, and chromosomal localization
            of the human protease inhibitor 4 (kallistatin) gene (PI4)
  JOURNAL   Genomics 23 (2), 370-378 (1994)
   PUBMED   7835886
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Chai,K.X., Chen,L.M., Chao,J. and Chao,L.
  TITLE     Kallistatin: a novel human serine proteinase inhibitor. Molecular
            cloning, tissue distribution, and expression in Escherichia coli
  JOURNAL   J Biol Chem 268 (32), 24498-24505 (1993)
   PUBMED   8227002
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Zhou,G.X., Chao,L. and Chao,J.
  TITLE     Kallistatin: a novel human tissue kallikrein inhibitor.
            Purification, characterization, and reactive center sequence
  JOURNAL   J Biol Chem 267 (36), 25873-25880 (1992)
   PUBMED   1334488
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Wang,M.Y., Day,J., Chao,L. and Chao,J.
  TITLE     Human kallistatin, a new tissue kallikrein-binding protein:
            purification and characterization
  JOURNAL   Adv Exp Med Biol 247B, 1-8 (1989)
   PUBMED   2558505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA036536.1, DA637776.1, BX248009.1 and BC014992.1.
            
            On Jan 10, 2014 this sequence version replaced XP_005267820.1.
            
            Transcript Variant: This variant (2) has an alternate splice site
            in the 5' region, which results in translation initiation at a
            downstream AUG codon, compared to variant 1. The resulting isoform
            (2) has a shorter N-terminus, compared to isoform 1. Both variants
            2 and 3 encode the same isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX248009.1, SRR14038191.2408034.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..427
                     /product="kallistatin isoform 2 precursor"
                     /note="protease inhibitor 4 (kallistatin); serine (or
                     cysteine) proteinase inhibitor, clade A (alpha-1
                     antiproteinase, antitrypsin), member 4; serpin A4;
                     kallikrein inhibitor; peptidase inhibitor 4; serpin
                     peptidase inhibitor, clade A (alpha-1 antiproteinase,
                     antitrypsin), member 4; testicular secretory protein Li
                     22; sserpin family A member 4"
                     /calculated_mol_wt=46355
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2205
     mat_peptide     21..427
                     /product="Kallistatin. /id=PRO_0000032425"
                     /note="propagated from UniProtKB/Swiss-Prot (P29622.3)"
                     /calculated_mol_wt=46355
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Region          44..426
                     /region_name="serpinA4_KST"
                     /note="serpin family A member 4, kallistatin; cd19552"
                     /db_xref="CDD:381020"
     Site            108
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19139490; propagated from
                     UniProtKB/Swiss-Prot (P29622.3)"
     Site            order(374..385,387..402)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381020"
     Site            388..389
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P29622.3)"
     CDS             1..427
                     /gene="SERPINA4"
                     /gene_synonym="KAL; kallistatin; KLST; KST; PI-4; PI4"
                     /coded_by="NM_001289033.2:231..1514"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS9927.1"
                     /db_xref="GeneID:5267"
                     /db_xref="HGNC:HGNC:8948"
                     /db_xref="MIM:147935"
ORIGIN      
        1 mhlidyllll lvgllalshg qlhvehdges csnsshqqil etgegspslk iapanadfaf
       61 rfyyliaset pgkniffspl sisaayamls lgacshsrsq ileglgfnlt elsesdvhrg
      121 fqhllhtlnl pghgletrvg salflshnlk flakflndtm avyeaklfht nfydtvgtiq
      181 lindhvkket rgkivdlvse lkkdvlmvlv nyiyfkalwe kpfissrttp kdfyvdentt
      241 vrvpmmlqdq ehhwylhdry lpcsvlrmdy kgdatvffil pnqgkmreie evltpemlmr
      301 wnnllrkrnf ykklelhlpk fsisgsyvld qilprlgftd lfskwadlsg itkqqkleas
      361 ksfhkatldv deagteaaaa tsfaikffsa qtnrhilrfn rpflvvifst stqsvlflgk
      421 vvdptkp
//
LOCUS       NP_078925                593 aa            linear   PRI 20-NOV-2025
DEFINITION  BBSome complex member BBS1 [Homo sapiens].
ACCESSION   NP_078925
VERSION     NP_078925.3
DBSOURCE    REFSEQ: accession NM_024649.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Alghaith,F.A., MacKay,S., Wallace,K., Locke,J., Robitaille,J.M.,
            Dyack,S. and Arts,H.H.
  TITLE     Recurrence of a BBS1 variant in Bardet-Biedl patients from Prince
            Edward Island
  JOURNAL   Clin Genet 104 (6), 713-715 (2023)
   PUBMED   37612261
  REMARK    GeneRIF: Recurrence of a BBS1 variant in Bardet-Biedl patients from
            Prince Edward Island.
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Freke,G.M., Martins,T., Davies,R.J., Beyer,T., Seda,M., Peskett,E.,
            Haq,N., Prasai,A., Otto,G., Jeyabalan Srikaran,J., Hernandez,V.,
            Diwan,G.D., Russell,R.B., Ueffing,M., Huranova,M., Boldt,K.,
            Beales,P.L. and Jenkins,D.
  TITLE     De-Suppression of Mesenchymal Cell Identities and Variable
            Phenotypic Outcomes Associated with Knockout of Bbs1
  JOURNAL   Cells 12 (22), 2662 (2023)
   PUBMED   37998397
  REMARK    GeneRIF: De-Suppression of Mesenchymal Cell Identities and Variable
            Phenotypic Outcomes Associated with Knockout of Bbs1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Viehl,L., Wegner,D.J., Hmiel,S.P., White,F.V., Jain,S., Cole,F.S.
            and Wambach,J.A.
  TITLE     Lethal neonatal respiratory failure due to biallelic variants in
            BBS1 and monoallelic variant in TTC21B
  JOURNAL   Pediatr Nephrol 38 (2), 605-609 (2023)
   PUBMED   35695966
  REMARK    GeneRIF: Lethal neonatal respiratory failure due to biallelic
            variants in BBS1 and monoallelic variant in TTC21B.
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Young,T.L., Woods,M.O., Parfrey,P.S., Green,J.S., Hefferton,D. and
            Davidson,W.S.
  TITLE     A founder effect in the newfoundland population reduces the
            Bardet-Biedl syndrome I (BBS1) interval to 1 cM
  JOURNAL   Am J Hum Genet 65 (6), 1680-1687 (1999)
   PUBMED   10577922
REFERENCE   6  (residues 1 to 593)
  AUTHORS   Katsanis,N., Lewis,R.A., Stockton,D.W., Mai,P.M., Baird,L.,
            Beales,P.L., Leppert,M. and Lupski,J.R.
  TITLE     Delineation of the critical interval of Bardet-Biedl syndrome 1
            (BBS1) to a small region of 11q13, through linkage and haplotype
            analysis of 91 pedigrees
  JOURNAL   Am J Hum Genet 65 (6), 1672-1679 (1999)
   PUBMED   10577921
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Beales,P.L., Warner,A.M., Hitman,G.A., Thakker,R. and Flinter,F.A.
  TITLE     Bardet-Biedl syndrome: a molecular and phenotypic study of 18
            families
  JOURNAL   J Med Genet 34 (2), 92-98 (1997)
   PUBMED   9039982
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002748.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 16, 2003 this sequence version replaced NP_078925.2.
            
            Summary: Mutations in this gene have been observed in patients with
            the major form (type 1) of Bardet-Biedl syndrome. The encoded
            protein may play a role in eye, limb, cardiac and reproductive
            system development. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.173357.1, BX647612.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000318312.12/ ENSP00000317469.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..593
                     /product="BBSome complex member BBS1"
                     /note="bardet-Biedl syndrome 1 protein; BBS2-like protein
                     2"
                     /calculated_mol_wt=64953
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8NFJ9.1)"
     Region          23..276
                     /region_name="BBS1"
                     /note="Ciliary BBSome complex subunit 1; pfam14779"
                     /db_xref="CDD:464312"
     CDS             1..593
                     /gene="BBS1"
                     /gene_synonym="BBS2L2"
                     /coded_by="NM_024649.5:26..1807"
                     /db_xref="CCDS:CCDS8142.1"
                     /db_xref="GeneID:582"
                     /db_xref="HGNC:HGNC:966"
                     /db_xref="MIM:209901"
ORIGIN      
        1 maaasssdsd acgaesnean skwldahydp manihtfsac laladlhgdg eyklvvgdlg
       61 pggqqprlkv lkgplvmtes plpalpaaaa tflmeqhepr tpalalasgp cvyvyknlrp
      121 yfkfslpqlp pnpleqdlwn qakedridpl tlkemlesir etaeeplsiq slrflqlels
      181 emeafvnqhk snsikrqtvi ttmttlkknl adedavsclv lgtenkellv ldpeaftila
      241 kmslpsvpvf levsgqfdve frlaaacrng niyilrrdsk hpkycielsa qpvglirvhk
      301 vlvvgstqds lhgfthkgkk lwtvqmpaai ltmnlleqhs rglqavmagl angevriyrd
      361 kallnvihtp davtslcfgr ygredntlim ttrgggliik ilkrtavfve ggsevgpppa
      421 qamklnvprk trlyvdqtlr ereagtamhr afqtdlyllr lraaraylqa lesslsplst
      481 tareplklha vvqglgptfk ltlhlqntst trpvlgllvc flynealysl praffkvpll
      541 vpglnyplet fveslsnkgi sdiikvlvlr egqsapllsa hvnmpgsegl aaa
//
LOCUS       NP_808807                563 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane prolyl 4-hydroxylase isoform c [Homo sapiens].
ACCESSION   NP_808807
VERSION     NP_808807.2
DBSOURCE    REFSEQ: accession NM_177938.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Gulcu Ustun,N.S.
  TITLE     A pathogenic P4HTM gene variant in two brothers with autism
            spectrum disorder
  JOURNAL   Psychiatr Genet 34 (2), 68-69 (2024)
   PUBMED   38441145
  REMARK    GeneRIF: A pathogenic P4HTM gene variant in two brothers with
            autism spectrum disorder.
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Saeed,S., Ning,L., Badreddine,A., Mirza,M.U., Boissel,M.,
            Khanam,R., Manzoor,J., Janjua,Q.M., Khan,W.I., Toussaint,B.,
            Vaillant,E., Amanzougarene,S., Derhourhi,M., Trant,J.F.,
            Siegert,A.M., Lam,B.Y.H., Yeo,G.S.H., Chabraoui,L., Touzani,A.,
            Kulkarni,A., Farooqi,I.S., Bonnefond,A., Arslan,M. and Froguel,P.
  TITLE     Biallelic Mutations in P4HTM Cause Syndromic Obesity
  JOURNAL   Diabetes 72 (9), 1228-1234 (2023)
   PUBMED   37083980
  REMARK    GeneRIF: Biallelic Mutations in P4HTM Cause Syndromic Obesity.
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Myllykoski,M., Sutinen,A., Koski,M.K., Kallio,J.P., Raasakka,A.,
            Myllyharju,J., Wierenga,R.K. and Koivunen,P.
  TITLE     Structure of transmembrane prolyl 4-hydroxylase reveals unique
            organization of EF and dioxygenase domains
  JOURNAL   J Biol Chem 296, 100197 (2021)
   PUBMED   33334883
  REMARK    GeneRIF: Structure of transmembrane prolyl 4-hydroxylase reveals
            unique organization of EF and dioxygenase domains.
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Maddirevula,S., Ben-Omran,T., AlMureikhi,M., Eyaid,W., Arabi,H.,
            Alkuraya,H., Alfaifi,A., Alfalah,A.H., Alsaif,H.S., Abdulwahab,F.,
            Alfadhel,M. and Alkuraya,F.S.
  TITLE     Further delineation of HIDEA syndrome
  JOURNAL   Am J Med Genet A 182 (12), 2999-3006 (2020)
   PUBMED   32965080
  REMARK    GeneRIF: Further delineation of HIDEA syndrome.
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Seo,K., Seo,S., Ki,S.H. and Shin,S.M.
  TITLE     Sestrin2 inhibits hypoxia-inducible factor-1alpha accumulation via
            AMPK-mediated prolyl hydroxylase regulation
  JOURNAL   Free Radic Biol Med 101, 511-523 (2016)
   PUBMED   27840318
  REMARK    GeneRIF: The results suggest that SESN2 increases degradation of
            HIF-1A via AMPK-PHD regulation that contributes to inhibition of in
            vitro and in vivo tumorigenesis.
REFERENCE   6  (residues 1 to 563)
  AUTHORS   Koivunen,P., Tiainen,P., Hyvarinen,J., Williams,K.E., Sormunen,R.,
            Klaus,S.J., Kivirikko,K.I. and Myllyharju,J.
  TITLE     An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is
            induced by hypoxia and acts on hypoxia-inducible factor alpha
  JOURNAL   J Biol Chem 282 (42), 30544-30552 (2007)
   PUBMED   17726031
REFERENCE   7  (residues 1 to 563)
  AUTHORS   Hirota,K. and Semenza,G.L.
  TITLE     Regulation of hypoxia-inducible factor 1 by prolyl and asparaginyl
            hydroxylases
  JOURNAL   Biochem Biophys Res Commun 338 (1), 610-616 (2005)
   PUBMED   16154531
  REMARK    GeneRIF: This review summarizes recent progress in elucidating the
            molecular mechanisms of hypoxia-inducible factor (HIF)-1
            activation, focusing on the role of oxygen-dependent asparaginyl
            hydroxylase in hypoxia signal transduction.
            Review article
REFERENCE   8  (residues 1 to 563)
  AUTHORS   Pekkala,M., Hieta,R., Bergmann,U., Kivirikko,K.I., Wierenga,R.K.
            and Myllyharju,J.
  TITLE     The peptide-substrate-binding domain of collagen prolyl
            4-hydroxylases is a tetratricopeptide repeat domain with functional
            aromatic residues
  JOURNAL   J Biol Chem 279 (50), 52255-52261 (2004)
   PUBMED   15456751
  REMARK    GeneRIF: crystal structure of the peptide-substrate-binding domain
REFERENCE   9  (residues 1 to 563)
  AUTHORS   Hirsila,M., Koivunen,P., Gunzler,V., Kivirikko,K.I. and
            Myllyharju,J.
  TITLE     Characterization of the human prolyl 4-hydroxylases that modify the
            hypoxia-inducible factor
  JOURNAL   J Biol Chem 278 (33), 30772-30780 (2003)
   PUBMED   12788921
  REMARK    GeneRIF: the longest and shortest isoenzymes have major transcripts
            encoding inactive polypeptides, which suggest novel regulation by
            alternative splicing.
REFERENCE   10 (residues 1 to 563)
  AUTHORS   Oehme,F., Ellinghaus,P., Kolkhof,P., Smith,T.J., Ramakrishnan,S.,
            Hutter,J., Schramm,M. and Flamme,I.
  TITLE     Overexpression of PH-4, a novel putative proline 4-hydroxylase,
            modulates activity of hypoxia-inducible transcription factors
  JOURNAL   Biochem Biophys Res Commun 296 (2), 343-349 (2002)
   PUBMED   12163023
  REMARK    GeneRIF: Data suggest that PH-4 is a novel hypoxia-inducible
            factor-prolyl hydroxylase that may be involved in the degradation
            of hypoxia-inducible transcription factors under normoxia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC047566.1, BC011710.2,
            BC000580.1 and AW072069.1.
            
            On May 13, 2005 this sequence version replaced NP_808807.1.
            
            Summary: The product of this gene belongs to the family of prolyl
            4-hydroxylases. This protein is a prolyl hydroxylase that may be
            involved in the degradation of hypoxia-inducible transcription
            factors under normoxia. It plays a role in adaptation to hypoxia
            and may be related to cellular oxygen sensing. Alternatively
            spliced variants encoding different isoforms have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) contains two additional
            segments in the coding region, compared to variant 1. The resulting
            isoform (c) is longer, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011710.2, SRR1803614.66591.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..563
                     /product="transmembrane prolyl 4-hydroxylase isoform c"
                     /EC_number="1.14.11.29"
                     /note="P4H with transmembrane domain; Prolyl hydroxlase
                     domain-containing 4; hypoxia-inducible factor prolyl
                     4-hydroxylase; proline 4-hydroxylase; transmembrane prolyl
                     4-hydroxylase; HPH-4; HIF-PH4; HIF-prolyl hydroxylase 4;
                     hypoxia-inducible factor prolyl hydroxylase 4; prolyl
                     4-hydroxylase, transmembrane (endoplasmic reticulum)"
                     /calculated_mol_wt=62982
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Site            61..81
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Region          89..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG6.2)"
     Region          192..252
                     /region_name="EF-hand_7"
                     /note="EF-hand domain pair; pfam13499"
                     /db_xref="CDD:463900"
     Region          246..519
                     /region_name="P4Hc"
                     /note="Prolyl 4-hydroxylase alpha subunit homologues;
                     smart00702"
                     /db_xref="CDD:214780"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG6.2)"
     CDS             1..563
                     /gene="P4HTM"
                     /gene_synonym="EGLN4; HIDEA; HIFPH4; P4H-TM; PH-4; PH4;
                     PHD4"
                     /coded_by="NM_177938.2:350..2041"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2781.2"
                     /db_xref="GeneID:54681"
                     /db_xref="HGNC:HGNC:28858"
                     /db_xref="MIM:614584"
ORIGIN      
        1 maaaavtgqr petaaaeeas rpqwappdhc qaqaaaglgd gedapvrplc kprgicsray
       61 flvlmvfvhl ylgnvlalll fvhysngdes sdpgpqhraq gpgpeptlgp ltrlegikvg
      121 herkvqlvtd rdhfirtlsl kpllfeipgf ltdeecrlii hlaqmkglqr sqilpteeye
      181 eamstmqvsq ldlfrlldqn rdghlqlrev laqtrlgngw wmtpesiqem yaaikadpdg
      241 dgvlslqefs nmdlrdfhky mrshkaesse lvrnshhtwl yqgegahhim rairqrvlrl
      301 trlspeivel seplqvvryg egghyhahvd sgpvypetic shtklvanes vpfetscrqv
      361 spnwglpsil rpgtpmtqaq pctvgvplgm gpgdhwvipv spwehpqlgt csvpplpysy
      421 mtvlfylnnv tgggetvfpv adnrtydems liqddvdlrd trrhcdkgnl rvkpqqgtav
      481 fwynylpdgq gwvgdvddys lhggclvtrg tkwiannwin vdpsrarqal fqqemarlar
      541 eggtdsqpew aldrayrdar vel
//
LOCUS       NP_001341225            1460 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001341225 XP_016870091
VERSION     NP_001341225.1
DBSOURCE    REFSEQ: accession NM_001354296.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On Aug 10, 2017 this sequence version replaced XP_016870091.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.56170.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1460
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 2"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=162767
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Site            172
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          574..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          739..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          846..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          889..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          1245..1308
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1356..1457
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1460
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001354296.2:366..4748"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS65131.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgkpd ktlrfslcsd nlegisegps nrsnsvssld legesvselg
      601 agpsgsngve alqlleheqa ttqdnlddkl rkfeirdmmg ltddrdiset vsetwstdvl
      661 gsdfdpnide drlqeiagaa aenmlgsllc lpgsgsvlld pctgstiset tseawsvevl
      721 psdseapdlk qeerlqeles csglgstsdd tdvrevssrp stpglsvvsg isatsedipn
      781 kiedlrsecs sdfggkdsvt spdmdeithg ahqltsppsq sesllamfdp lsshegasav
      841 vrpkvhyarp shpppdppil egavggnear lpnfgshvlt paemeafkqr hsyperlvrs
      901 rssdivssvr rpmsdpswnr rpgneerelp paaaigatsl vaaphsssss pskdssrget
      961 eerkdsddek sdrnrpwwrk rfvsampkap ipfrkkekqe kdkddlgpdr fstltddpsp
     1021 rlsaqaqvae dildkyrnai krtspsdgam anyestevmg dgesahdspr dealqnisad
     1081 dlpdsasqaa hpqdsafsyr dakkklrlal csadsvafpv lthstrnglp dhtdpednei
     1141 vcflkvqiae ainlqdknlm aqlqetmrcv crfdnrtcrk llasiaedyr krapyiaylt
     1201 rcrqglqttq ahlerllqrv lrdkevanry fttvcvrlll eskekkiref iqdfqkltaa
     1261 ddktaqvedf lqflygamaq dviwqnasee qlqdaqlaie rsvmnrifkl afypnqdgdi
     1321 lrdqvlhehi qrlskvvtan hralqipevy lreapwpsaq seirtisayk tprdkvqcil
     1381 rmcstimnll slanedsvpg addfvpvlvf vlikanppcl lstvqyissf yasclsgees
     1441 ywwmqftaav efiktiddrk
//
LOCUS       NP_116294                401 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 45 [Homo sapiens].
ACCESSION   NP_116294 NP_006441
VERSION     NP_116294.1
DBSOURCE    REFSEQ: accession NM_032905.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 401)
  AUTHORS   Fukumura,K., Sperotto,L., Seuss,S., Kang,H.S., Yoshimoto,R.,
            Sattler,M. and Mayeda,A.
  TITLE     SAP30BP interacts with RBM17/SPF45 to promote splicing in a subset
            of human short introns
  JOURNAL   Cell Rep 42 (12), 113534 (2023)
   PUBMED   38065098
  REMARK    GeneRIF: SAP30BP interacts with RBM17/SPF45 to promote splicing in
            a subset of human short introns.
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 401)
  AUTHORS   Fu,Y., Bai,C., Wang,S., Chen,D., Zhang,P., Wei,H., Rong,F.,
            Zhang,C., Chen,S. and Wang,Z.
  TITLE     AKT1 phosphorylates RBM17 to promote Sox2 transcription by
            modulating alternative splicing of FOXM1 to enhance cancer stem
            cell properties in colorectal cancer cells
  JOURNAL   FASEB J 37 (1), e22707 (2023)
   PUBMED   36520054
  REMARK    GeneRIF: AKT1 phosphorylates RBM17 to promote Sox2 transcription by
            modulating alternative splicing of FOXM1 to enhance cancer stem
            cell properties in colorectal cancer cells.
REFERENCE   5  (residues 1 to 401)
  AUTHORS   Liu,L., Vujovic,A., Deshpande,N.P., Sathe,S., Anande,G.,
            Chen,H.T.T., Xu,J., Minden,M.D., Yeo,G.W., Unnikrishnan,A.,
            Hope,K.J. and Lu,Y.
  TITLE     The splicing factor RBM17 drives leukemic stem cell maintenance by
            evading nonsense-mediated decay of pro-leukemic factors
  JOURNAL   Nat Commun 13 (1), 3833 (2022)
   PUBMED   35781533
  REMARK    GeneRIF: The splicing factor RBM17 drives leukemic stem cell
            maintenance by evading nonsense-mediated decay of pro-leukemic
            factors.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 401)
  AUTHORS   Perry,W.L. 3rd, Shepard,R.L., Sampath,J., Yaden,B., Chin,W.W.,
            Iversen,P.W., Jin,S., Lesoon,A., O'Brien,K.A., Peek,V.L., Rolfe,M.,
            Shyjan,A., Tighe,M., Williamson,M., Krishnan,V., Moore,R.E. and
            Dantzig,A.H.
  TITLE     Human splicing factor SPF45 (RBM17) confers broad multidrug
            resistance to anticancer drugs when overexpressed--a phenotype
            partially reversed by selective estrogen receptor modulators
  JOURNAL   Cancer Res 65 (15), 6593-6600 (2005)
   PUBMED   16061639
  REMARK    GeneRIF: Resistance to various chemotherapeutics resulting from
            stable transfection of RBM17 (SPF45) in A2780 ovarian carcinoma
            cells may be due to effects of SPF45 on transcription and splicing
            of ERbeta-regulated genes.
REFERENCE   7  (residues 1 to 401)
  AUTHORS   Sampath,J., Long,P.R., Shepard,R.L., Xia,X., Devanarayan,V.,
            Sandusky,G.E., Perry,W.L. 3rd, Dantzig,A.H., Williamson,M.,
            Rolfe,M. and Moore,R.E.
  TITLE     Human SPF45, a splicing factor, has limited expression in normal
            tissues, is overexpressed in many tumors, and can confer a
            multidrug-resistant phenotype to cells
  JOURNAL   Am J Pathol 163 (5), 1781-1790 (2003)
   PUBMED   14578179
  REMARK    GeneRIF: overexpression of SPF45 in HeLa, a cervical carcinoma cell
            line, resulted in drug resistance to doxorubicin and vincristine
REFERENCE   8  (residues 1 to 401)
  AUTHORS   Graveley,B.R.
  TITLE     Sex, AGility, and the regulation of alternative splicing
  JOURNAL   Cell 109 (4), 409-412 (2002)
   PUBMED   12086596
  REMARK    Review article
REFERENCE   9  (residues 1 to 401)
  AUTHORS   Lallena,M.J., Chalmers,K.J., Llamazares,S., Lamond,A.I. and
            Valcarcel,J.
  TITLE     Splicing regulation at the second catalytic step by Sex-lethal
            involves 3' splice site recognition by SPF45
  JOURNAL   Cell 109 (3), 285-296 (2002)
   PUBMED   12015979
REFERENCE   10 (residues 1 to 401)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CV570433.1, AF542550.1,
            CN291330.1, AL157395.17 and AA905075.1.
            
            On Jan 13, 2003 this sequence version replaced NP_006441.1.
            
            Summary: This gene encodes an RNA binding protein. The encoded
            protein is part of the spliceosome complex and functions in the
            second catalytic step of mRNA splicing. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 9 and 15. [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.162318.1, AF542550.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379888.9/ ENSP00000369218.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p15.1"
     Protein         1..401
                     /product="splicing factor 45"
                     /note="splicing factor 45kDa; 45 kDa-splicing factor"
                     /calculated_mol_wt=44831
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q8JZX4; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          57..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          114..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          235..279
                     /region_name="G-patch"
                     /note="G-patch domain; pfam01585"
                     /db_xref="CDD:396249"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96I25.1)"
     Region          303..397
                     /region_name="RRM_UHM_SPF45"
                     /note="RNA recognition motif (RRM) found in UHM domain of
                     45 kDa-splicing factor (SPF45) and similar proteins;
                     cd12647"
                     /db_xref="CDD:410051"
     CDS             1..401
                     /gene="RBM17"
                     /gene_synonym="SPF45"
                     /coded_by="NM_032905.5:179..1384"
                     /db_xref="CCDS:CCDS7077.1"
                     /db_xref="GeneID:84991"
                     /db_xref="HGNC:HGNC:16944"
                     /db_xref="MIM:606935"
ORIGIN      
        1 mslyddlgve tsdsktegws knfkllqsql qvkkaaltqa ksqrtkqstv lapvidlkrg
       61 gssddrqivd tpphvaaglk dpvpsgfsag evlipladey dpmfpndyek vvkrqreerq
      121 rqrelerqke ieerekrrkd rheasgfarr pdpdsdeded yererrkrsm ggaaiappts
      181 lvekdkelpr dfpyeedsrp rsqsskaaip ppvyeeqdrp rsptgpsnsf lanmggtvah
      241 kimqkygfre gqglgkheqg lstalsvekt skrggkiivg datekdaskk sdsnplteil
      301 kcptkvvllr nmvgagevde dlevetkeec ekygkvgkcv ifeipgapdd eavriflefe
      361 rvesaikavv dlngryfggr vvkacfynld kfrvldlaeq v
//
LOCUS       NP_005206               1447 aa            linear   PRI 20-NOV-2025
DEFINITION  netrin receptor DCC [Homo sapiens].
ACCESSION   NP_005206
VERSION     NP_005206.2
DBSOURCE    REFSEQ: accession NM_005215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1447)
  AUTHORS   Badary,D.M., Elsaied,H., Abdel-Fadeil,M.R., Ali,M.K., Abou-Taleb,H.
            and Iraqy,H.M.
  TITLE     Possible Role of Netrin-1/Deleted in Colorectal Cancer/Vascular
            Endothelial Growth Factor Signaling Pathway in the Pathogenesis of
            Placenta Accreta Spectrum: A Case-control Study
  JOURNAL   Int J Gynecol Pathol 43 (6), 565-572 (2024)
   PUBMED   38289148
  REMARK    GeneRIF: Possible Role of Netrin-1/Deleted in Colorectal
            Cancer/Vascular Endothelial Growth Factor Signaling Pathway in the
            Pathogenesis of Placenta Accreta Spectrum: A Case-control Study.
REFERENCE   2  (residues 1 to 1447)
  AUTHORS   Marquez-Gonzalez,R.M., Saucedo-Sarinana,A.M., de Jesus
            Tovar-Jacome,C., Barros-Nunez,P., Gallegos-Arreola,M.P.,
            Orozco-Gutierrez,M.H., Mariscal-Ramirez,I., Pineda-Razo,T.D.,
            Alcaraz-Wong,A.A., Marin-Contreras,M.E. and Rosales-Reynoso,M.A.
  TITLE     NME1 and DCC variants are associated with susceptibility and tumor
            characteristics in Mexican patients with colorectal cancer
  JOURNAL   J Egypt Natl Canc Inst 36 (1), 10 (2024)
   PUBMED   38556604
  REMARK    GeneRIF: NME1 and DCC variants are associated with susceptibility
            and tumor characteristics in Mexican patients with colorectal
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1447)
  AUTHORS   Serwer,T., Wahid,M., Imtiaz,F. and Memon,A.S.
  TITLE     Identification of specific codon 201 mutation of the DCC Gene in
            the colonoscopic specimen of colorectal cancer
  JOURNAL   J Pak Med Assoc 74 (2), 287-293 (2024)
   PUBMED   38419228
  REMARK    GeneRIF: Identification of specific codon 201 mutation of the DCC
            Gene in the colonoscopic specimen of colorectal cancer.
REFERENCE   4  (residues 1 to 1447)
  AUTHORS   Li,W., Lee,J., Vikis,H.G., Lee,S.H., Liu,G., Aurandt,J., Shen,T.L.,
            Fearon,E.R., Guan,J.L., Han,M., Rao,Y., Hong,K. and Guan,K.L.
  TITLE     Activation of FAK and Src are receptor-proximal events required for
            netrin signaling
  JOURNAL   Nat Neurosci 7 (11), 1213-1221 (2004)
   PUBMED   15494734
REFERENCE   5  (residues 1 to 1447)
  AUTHORS   Keino-Masu,K., Masu,M., Hinck,L., Leonardo,E.D., Chan,S.S.,
            Culotti,J.G. and Tessier-Lavigne,M.
  TITLE     Deleted in Colorectal Cancer (DCC) encodes a netrin receptor
  JOURNAL   Cell 87 (2), 175-185 (1996)
   PUBMED   8861902
REFERENCE   6  (residues 1 to 1447)
  AUTHORS   Cho,K.R., Oliner,J.D., Simons,J.W., Hedrick,L., Fearon,E.R.,
            Preisinger,A.C., Hedge,P., Silverman,G.A. and Vogelstein,B.
  TITLE     The DCC gene: structural analysis and mutations in colorectal
            carcinomas
  JOURNAL   Genomics 19 (3), 525-531 (1994)
   PUBMED   8188295
REFERENCE   7  (residues 1 to 1447)
  AUTHORS   Fearon,E.R., Ekstrand,B.C., Hu,G., Pierceall,W.E., Reale,M.A. and
            Bigner,S.H.
  TITLE     Studies of the deleted in colorectal cancer gene in normal and
            neoplastic tissues
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 637-643 (1994)
   PUBMED   7587124
REFERENCE   8  (residues 1 to 1447)
  AUTHORS   Meneret,A., Trouillard,O., Dunoyer,M., Depienne,C. and Roze,E.
  TITLE     Congenital Mirror Movements
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25763452
REFERENCE   9  (residues 1 to 1447)
  AUTHORS   Nigro,J.M., Cho,K.R., Fearon,E.R., Kern,S.E., Ruppert,J.M.,
            Oliner,J.D., Kinzler,K.W. and Vogelstein,B.
  TITLE     Scrambled exons
  JOURNAL   Cell 64 (3), 607-613 (1991)
   PUBMED   1991322
REFERENCE   10 (residues 1 to 1447)
  AUTHORS   Fearon,E.R., Cho,K.R., Nigro,J.M., Kern,S.E., Simons,J.W.,
            Ruppert,J.M., Hamilton,S.R., Preisinger,A.C., Thomas,G.,
            Kinzler,K.W. et al.
  TITLE     Identification of a chromosome 18q gene that is altered in
            colorectal cancers
  JOURNAL   Science 247 (4938), 49-56 (1990)
   PUBMED   2294591
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011155.13, X76132.1,
            BC036524.1 and AC103949.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 18, 2006 this sequence version replaced NP_005206.1.
            
            Summary: This gene encodes a netrin 1 receptor. The transmembrane
            protein is a member of the immunoglobulin superfamily of cell
            adhesion molecules, and mediates axon guidance of neuronal growth
            cones towards sources of netrin 1 ligand. The cytoplasmic tail
            interacts with the tyrosine kinases Src and focal adhesion kinase
            (FAK, also known as PTK2) to mediate axon attraction. The protein
            partially localizes to lipid rafts, and induces apoptosis in the
            absence of ligand. The protein functions as a tumor suppressor, and
            is frequently mutated or downregulated in colorectal cancer and
            esophageal carcinoma. [provided by RefSeq, Oct 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X76132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267772, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442544.7/ ENSP00000389140.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..1447
                     /product="netrin receptor DCC"
                     /note="colorectal cancer suppressor; tumor suppressor
                     protein DCC; immunoglobulin superfamily DCC subclass
                     member 1; deleted in colorectal carcinoma; putative
                     colorectal tumor suppressor"
                     /calculated_mol_wt=158326
     Region          39..136
                     /region_name="IgI_1_Neogenin_like"
                     /note="First immunoglobulin (Ig)-like domain in neogenin,
                     and similar domains; member of the I-set of Ig superfamily
                     (IgSF) domains; cd05722"
                     /db_xref="CDD:409387"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409387"
     Region          45..51
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409387"
     Region          55..65
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409387"
     Region          70..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409387"
     Region          78..81
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409387"
     Region          88..93
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409387"
     Site            94
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          95..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409387"
     Region          113..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409387"
     Region          125..136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409387"
     Region          139..216
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          241..327
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          257..261
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409562"
     Region          270..274
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409562"
     Region          293..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409562"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          307..312
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409562"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          322..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409562"
     Region          334..417
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          348..352
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409388"
     Region          361..365
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409388"
     Region          383..387
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409388"
     Region          397..402
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409388"
     Region          410..413
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409388"
     Region          429..521
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(429,494,509)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <478..901
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            478
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            order(510..511,513..514)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            628
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            702
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          946..1041
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(1030..1031,1033..1034)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            1098..1122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1126..1152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1148..1445
                     /region_name="Neogenin_C"
                     /note="Neogenin C-terminus; pfam06583"
                     /db_xref="CDD:461954"
     Region          1165..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Site            1178
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            1187
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Site            1267
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1.
                     /evidence=ECO:0000250|UniProtKB:Q63155; propagated from
                     UniProtKB/Swiss-Prot (P43146.2)"
     Region          1288..1330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1394..1419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     Region          1432..1439
                     /region_name="Interaction with MYO10.
                     /evidence=ECO:0000269|PubMed:21642953"
                     /note="propagated from UniProtKB/Swiss-Prot (P43146.2)"
     CDS             1..1447
                     /gene="DCC"
                     /gene_synonym="CRC18; CRCR1; HGPPS2; IGDCC1; MRMV1;
                     NTN1R1"
                     /coded_by="NM_005215.4:592..4935"
                     /db_xref="CCDS:CCDS11952.1"
                     /db_xref="GeneID:1630"
                     /db_xref="HGNC:HGNC:2701"
                     /db_xref="MIM:120470"
ORIGIN      
        1 menslrcvwv pklafvlfga slfsahlqvt gfqikaftal rflsepsdav tmrggnvlld
       61 csaesdrgvp vikwkkdgih lalgmderkq qlsngslliq nilhsrhhkp deglyqceas
      121 lgdsgsiisr takvavagpl rflsqtesvt afmgdtvllk cevigepmpt ihwqknqqdl
      181 tpipgdsrvv vlpsgalqis rlqpgdigiy rcsarnpass rtgneaevri lsdpglhrql
      241 yflqrpsnvv aiegkdavle ccvsgyppps ftwlrgeevi qlrskkysll ggsnllisnv
      301 tdddsgmytc vvtyknenis asaeltvlvp pwflnhpsnl yayesmdief ectvsgkpvp
      361 tvnwmkngdv vipsdyfqiv ggsnlrilgv vksdegfyqc vaeneagnaq tsaqlivpkp
      421 aipsssvlps aprdvvpvlv ssrfvrlswr ppaeakgniq tftvffsreg dnreralntt
      481 qpgslqltvg nlkpeamytf rvvaynewgp gessqpikva tqpelqvpgp venlqavsts
      541 ptsilitwep payangpvqg yrlfctevst gkeqnievdg lsykleglkk fteyslrfla
      601 ynrygpgvst dditvvtlsd vpsappqnvs levvnsrsik vswlpppsgt qngfitgyki
      661 rhrkttrrge metlepnnlw ylftglekgs qysfqvsamt vngtgppsnw ytaetpendl
      721 desqvpdqps slhvrpqtnc iimswtppln pnivvrgyii gygvgspyae tvrvdskqry
      781 ysierlesss hyvislkafn nagegvplye sattrsitdp tdpvdyypll ddfptsvpdl
      841 stpmlppvgv qavalthdav rvswadnsvp knqktsevrl ytvrwrtsfs asakyksedt
      901 tslsytatgl kpntmyefsv mvtknrrsst wsmtahatty eaaptsapkd ltvitregkp
      961 ravivswqpp leangkitay ilfytldkni piddwimeti sgdrlthqim dlnldtmyyf
     1021 riqarnskgv gplsdpilfr tlkvehpdkm andqgrhgdg gywpvdtnli drstlneppi
     1081 gqmhpphgsv tpqknsnllv iivvtvgvit vlvvvivavi ctrrssaqqr kkrathsagk
     1141 rkgsqkdlrp pdlwihheem emkniekpsg tdpagrdspi qscqdltpvs hsqsetqlgs
     1201 kstshsgqdt eeagssmstl erslaarrap raklmipmda qsnnpavvsa ipvptlesaq
     1261 ypgilpsptc gyphpqftlr pvpfptlsvd rgfgagrsqs vsegpttqqp pmlppsqpeh
     1321 ssseeapsrt iptacvrpth plrsfanpll pppmsaiepk vpytpllsqp gptlpkthvk
     1381 taslglagka rspllpvsvp tapevseesh kptedsanvy eqddlseqma sleglmkqln
     1441 aitgsaf
//
LOCUS       NP_039269               1009 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA ligase 3 isoform alpha precursor [Homo sapiens].
ACCESSION   NP_039269
VERSION     NP_039269.2
DBSOURCE    REFSEQ: accession NM_013975.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Deng,F., Laasik,M., Salminen,L., Lapatto,L., Huhtinen,K., Li,Y.,
            Hautaniemi,S., Hynninen,J., Niemi,M. and Lehtonen,R.
  TITLE     Toxicity and therapy outcome associations in LIG3, SLCO1B3, ABCB1,
            OPRM1 and GSTP1 in high-grade serous ovarian cancer
  JOURNAL   Basic Clin Pharmacol Toxicol 132 (6), 521-531 (2023)
   PUBMED   36988399
  REMARK    GeneRIF: Toxicity and therapy outcome associations in LIG3,
            SLCO1B3, ABCB1, OPRM1 and GSTP1 in high-grade serous ovarian
            cancer.
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   McNally,J.R., Ames,A.M., Admiraal,S.J. and O'Brien,P.J.
  TITLE     Human DNA ligases I and III have stand-alone end-joining
            capability, but differ in ligation efficiency and specificity
  JOURNAL   Nucleic Acids Res 51 (2), 796-805 (2023)
   PUBMED   36625284
  REMARK    GeneRIF: Human DNA ligases I and III have stand-alone end-joining
            capability, but differ in ligation efficiency and specificity.
REFERENCE   4  (residues 1 to 1009)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 1009)
  AUTHORS   Bian,R., Dang,W., Song,X., Liu,L., Jiang,C., Yang,Y., Li,Y., Li,L.,
            Li,X., Hu,Y., Bao,R. and Liu,Y.
  TITLE     Rac GTPase activating protein 1 promotes gallbladder cancer via
            binding DNA ligase 3 to reduce apoptosis
  JOURNAL   Int J Biol Sci 17 (9), 2167-2180 (2021)
   PUBMED   34239347
  REMARK    GeneRIF: Rac GTPase activating protein 1 promotes gallbladder
            cancer via binding DNA ligase 3 to reduce apoptosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1009)
  AUTHORS   Mackey,Z.B., Ramos,W., Levin,D.S., Walter,C.A., McCarrey,J.R. and
            Tomkinson,A.E.
  TITLE     An alternative splicing event which occurs in mouse pachytene
            spermatocytes generates a form of DNA ligase III with distinct
            biochemical properties that may function in meiotic recombination
  JOURNAL   Mol Cell Biol 17 (2), 989-998 (1997)
   PUBMED   9001252
REFERENCE   7  (residues 1 to 1009)
  AUTHORS   Kubota,Y., Nash,R.A., Klungland,A., Schar,P., Barnes,D.E. and
            Lindahl,T.
  TITLE     Reconstitution of DNA base excision-repair with purified human
            proteins: interaction between DNA polymerase beta and the XRCC1
            protein
  JOURNAL   EMBO J 15 (23), 6662-6670 (1996)
   PUBMED   8978692
REFERENCE   8  (residues 1 to 1009)
  AUTHORS   Caldecott,K.W., Tucker,J.D., Stanker,L.H. and Thompson,L.H.
  TITLE     Characterization of the XRCC1-DNA ligase III complex in vitro and
            its absence from mutant hamster cells
  JOURNAL   Nucleic Acids Res 23 (23), 4836-4843 (1995)
   PUBMED   8532526
REFERENCE   9  (residues 1 to 1009)
  AUTHORS   Chen,J., Tomkinson,A.E., Ramos,W., Mackey,Z.B., Danehower,S.,
            Walter,C.A., Schultz,R.A., Besterman,J.M. and Husain,I.
  TITLE     Mammalian DNA ligase III: molecular cloning, chromosomal
            localization, and expression in spermatocytes undergoing meiotic
            recombination
  JOURNAL   Mol Cell Biol 15 (10), 5412-5422 (1995)
   PUBMED   7565692
REFERENCE   10 (residues 1 to 1009)
  AUTHORS   Wei,Y.F., Robins,P., Carter,K., Caldecott,K., Pappin,D.J., Yu,G.L.,
            Wang,R.P., Shell,B.K., Nash,R.A., Schar,P. et al.
  TITLE     Molecular cloning and expression of human cDNAs encoding a novel
            DNA ligase IV and DNA ligase III, an enzyme active in DNA repair
            and recombination
  JOURNAL   Mol Cell Biol 15 (6), 3206-3216 (1995)
   PUBMED   7760816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB100562.1, BC068005.1,
            BM726768.1, AW166526.1, AA872458.1 and AC004223.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 24, 2005 this sequence version replaced NP_039269.1.
            
            Summary: This gene is a member of the DNA ligase family. Each
            member of this family encodes a protein that catalyzes the joining
            of DNA ends but they each have a distinct role in DNA metabolism.
            The protein encoded by this gene is involved in excision repair and
            is located in both the mitochondria and nucleus, with translation
            initiation from the upstream start codon allowing for transport to
            the mitochondria and translation initiation from a downstream start
            codon allowing for transport to the nucleus. Additionally,
            alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (alpha) represents the longer
            transcript and encodes the longer isoform (alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.177858.1,
                                           SRR1803611.130782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000378526.9/
                                                  ENSP00000367787.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..1009
                     /product="DNA ligase 3 isoform alpha precursor"
                     /EC_number="6.5.1.1"
                     /note="ligase II, DNA, ATP-dependent;
                     polydeoxyribonucleotide synthase [ATP] 3; ligase III, DNA,
                     ATP-dependent"
                     /calculated_mol_wt=108665
     sig_peptide     1..34
                     /calculated_mol_wt=4260
     mat_peptide     35..1009
                     /product="DNA ligase 3 isoform alpha"
                     /calculated_mol_wt=108665
     Region          96..181
                     /region_name="zf-PARP"
                     /note="Poly(ADP-ribose) polymerase and DNA-Ligase
                     Zn-finger region; pfam00645"
                     /db_xref="CDD:459887"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49916.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49916.2)"
     Region          224..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49916.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49916.2)"
     Region          277..280
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:20518483"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Region          318..830
                     /region_name="dnl1"
                     /note="DNA ligase I, ATP-dependent (dnl1); TIGR00574"
                     /db_xref="CDD:273147"
     Region          318..323
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:20518483"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Region          388..391
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:20518483"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Region          421..427
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:20518483"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Region          842..917
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49916.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49916.2)"
     Region          933..1003
                     /region_name="LIG3_BRCT"
                     /note="DNA ligase 3 BRCT domain; pfam16759"
                     /db_xref="CDD:465260"
     CDS             1..1009
                     /gene="LIG3"
                     /gene_synonym="LIG2; LIG3alpha; MTDPS20"
                     /coded_by="NM_013975.4:116..3145"
                     /note="isoform alpha precursor is encoded by transcript
                     variant alpha"
                     /db_xref="CCDS:CCDS11284.2"
                     /db_xref="GeneID:3980"
                     /db_xref="HGNC:HGNC:6600"
                     /db_xref="MIM:600940"
ORIGIN      
        1 mslafkiffp qtlralsrke lclfrkhhwr dvrqfsqwse tdllhghplf lrrkpvlsfq
       61 gshlrsraty lvflpglhvg lcsgpcemae qrfcvdyakr gtagckkcke kivkgvcrig
      121 kvvpnpfses ggdmkewyhi kcmfeklera rattkkiedl telegweele dnekeqitqh
      181 iadlsskaag tpkkkavvqa kltttgqvts pvkgasfvts tnprkfsgfs akpnnsgeap
      241 ssptpkrsls sskcdprhkd cllrefrklc amvadnpsyn tktqiiqdfl rkgsagdgfh
      301 gdvyltvkll lpgviktvyn lndkqivklf srifncnpdd mardleqgdv setirvffeq
      361 sksfppaaks lltiqevdef llrlskltke deqqqalqdi asrctandlk ciirlikhdl
      421 kmnsgakhvl daldpnayea fkasrnlqdv vervlhnaqe vekepgqrra lsvqaslmtp
      481 vqpmlaeack sveyamkkcp ngmfseikyd gervqvhkng dhfsyfsrsl kpvlphkvah
      541 fkdyipqafp gghsmildse vllidnktgk plpfgtlgvh kkaafqdanv clfvfdciyf
      601 ndvslmdrpl cerrkflhdn mveipnrimf semkrvtkal dladmitrvi qegleglvlk
      661 dvkgtyepgk rhwlkvkkdy lnegamadta dlvvlgafyg qgskggmmsi flmgcydpgs
      721 qkwctvtkca gghddatlar lqneldmvki skdpskipsw lkvnkiyypd fivpdpkkaa
      781 vweitgaefs kseahtadgi sirfprctri rddkdwksat nlpqlkelyq lskekadftv
      841 vagdegsstt ggsseenkgp sgsavsrkap skpsastkka egklsnsnsk dgnmqtakps
      901 amkvgeklat ksspvkvgek rkaadetlcq tkvlldiftg vrlylppstp dfsrlrryfv
      961 afdgdlvqef dmtsathvlg srdknpaaqq vspewiwaci rkrrlvapc
//
LOCUS       NP_002922                406 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RING1 [Homo sapiens].
ACCESSION   NP_002922
VERSION     NP_002922.2
DBSOURCE    REFSEQ: accession NM_002931.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Ryan,C.W., Regan,S.L., Mills,E.F., McGrath,B.T., Gong,E., Lai,Y.T.,
            Sheingold,J.B., Patel,K., Horowitz,T., Moccia,A., Tsan,Y.C.,
            Srivastava,A. and Bielas,S.L.
  TITLE     RING1 missense variants reveal sensitivity of DNA damage repair to
            H2A monoubiquitination dosage during neurogenesis
  JOURNAL   Nat Commun 15 (1), 7931 (2024)
   PUBMED   39256363
  REMARK    GeneRIF: RING1 missense variants reveal sensitivity of DNA damage
            repair to H2A monoubiquitination dosage during neurogenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Szustka,A., Kozal,K. and Krzeslak,A.
  TITLE     RING1 Inhibition Has a Cell-Specific Antitumoral Role by Promoting
            Autophagy in Endometrial Cancer Cells
  JOURNAL   Cell Physiol Biochem 58 (1), 1-13 (2024)
   PUBMED   38219048
  REMARK    GeneRIF: RING1 Inhibition Has a Cell-Specific Antitumoral Role by
            Promoting Autophagy in Endometrial Cancer Cells.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Liu,D., Guo,Y., Du,Q., Zhu,Y. and Guo,Y.
  TITLE     RING induces cell cycle arrest and apoptosis in human breast cancer
            cells by regulating the HSF1/MT2A axis
  JOURNAL   Exp Cell Res 433 (1), 113795 (2023)
   PUBMED   37797799
  REMARK    GeneRIF: RING induces cell cycle arrest and apoptosis in human
            breast cancer cells by regulating the HSF1/MT2A axis.
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Liang,Q., Wang,S., Zhou,X., Li,Y., Xing,S., Sha,Y., Yang,F.,
            Huang,W., Liu,N., Li,Z., Chen,Y., Xu,Y., Zhu,P., Lan,F. and Sun,N.
  TITLE     Essential role of MESP1-RING1A complex in cardiac differentiation
  JOURNAL   Dev Cell 57 (22), 2533-2549 (2022)
   PUBMED   36413948
  REMARK    GeneRIF: Essential role of MESP1-RING1A complex in cardiac
            differentiation.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Satijn,D.P. and Otte,A.P.
  TITLE     RING1 interacts with multiple Polycomb-group proteins and displays
            tumorigenic activity
  JOURNAL   Mol Cell Biol 19 (1), 57-68 (1999)
   PUBMED   9858531
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Satijn,D.P., Gunster,M.J., van der Vlag,J., Hamer,K.M., Schul,W.,
            Alkema,M.J., Saurin,A.J., Freemont,P.S., van Driel,R. and Otte,A.P.
  TITLE     RING1 is associated with the polycomb group protein complex and
            acts as a transcriptional repressor
  JOURNAL   Mol Cell Biol 17 (7), 4105-4113 (1997)
   PUBMED   9199346
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Kikuti,Y.Y., Tamiya,G., Ando,A., Chen,L., Kimura,M., Ferreira,E.,
            Tsuji,K., Trowsdale,J. and Inoko,H.
  TITLE     Physical mapping 220 kb centromeric of the human MHC and DNA
            sequence analysis of the 43-kb segment including the RING1, HKE6,
            and HKE4 genes
  JOURNAL   Genomics 42 (3), 422-435 (1997)
   PUBMED   9205114
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Lovering,R., Hanson,I.M., Borden,K.L., Martin,S., O'Reilly,N.J.,
            Evan,G.I., Rahman,D., Pappin,D.J., Trowsdale,J. and Freemont,P.S.
  TITLE     Identification and preliminary characterization of a protein motif
            related to the zinc finger
  JOURNAL   Proc Natl Acad Sci U S A 90 (6), 2112-2116 (1993)
   PUBMED   7681583
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Hanson,I.M., Poustka,A. and Trowsdale,J.
  TITLE     New genes in the class II region of the human major
            histocompatibility complex
  JOURNAL   Genomics 10 (2), 417-424 (1991)
   PUBMED   1906426
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL645940.4, BI259576.1 and
            BC051866.2.
            
            On Aug 20, 2004 this sequence version replaced NP_002922.1.
            
            Summary: This gene belongs to the RING finger family, members of
            which encode proteins characterized by a RING domain, a
            zinc-binding motif related to the zinc finger domain. The gene
            product can bind DNA and can act as a transcriptional repressor. It
            is associated with the multimeric polycomb group protein complex.
            The gene product interacts with the polycomb group proteins BMI1,
            EDR1, and CBX4, and colocalizes with these proteins in large
            nuclear domains. It interacts with the CBX4 protein via its
            glycine-rich C-terminal domain. The gene maps to the HLA class II
            region, where it is contiguous with the RING finger genes FABGL and
            HKE4. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.6253.1,
                                           SRR3476690.734216.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374656.5/ ENSP00000363787.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..406
                     /product="E3 ubiquitin-protein ligase RING1"
                     /EC_number="2.3.2.27"
                     /note="polycomb complex protein RING1; really interesting
                     new gene 1 protein; RING-type E3 ubiquitin transferase
                     RING1"
                     /calculated_mol_wt=42298
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          30..234
                     /region_name="Necessary for transcriptional repression.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Region          34..110
                     /region_name="RING-HC_RING2"
                     /note="RING finger, HC subclass, found in really
                     interesting new gene 2 protein (RING2) and similar
                     proteins; cd16740"
                     /db_xref="CDD:438398"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            order(45..46,60,62..63,65,67,74,78,82,90,92..95,98..100,
                     102..103,105..106,109..110)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438398"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          148..263
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          201..204
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          230..406
                     /region_name="Necessary for interaction with CBX2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            248
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q06587.2)"
     Region          261..400
                     /region_name="RAWUL_RING1"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in really interesting new gene 1
                     protein (RING1); cd17166"
                     /db_xref="CDD:340686"
     Site            order(263..265,283..286,290,293..295,297..298,301..302,
                     392..394)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:340686"
     Region          309..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06587.2)"
     CDS             1..406
                     /gene="RING1"
                     /gene_synonym="RING1A; RNF1"
                     /coded_by="NM_002931.4:204..1424"
                     /db_xref="CCDS:CCDS34424.1"
                     /db_xref="GeneID:6015"
                     /db_xref="HGNC:HGNC:10018"
                     /db_xref="MIM:602045"
ORIGIN      
        1 mttpanaqna sktwelslye lhrtpqeaim dgteiavspr slhselmcpi cldmlkntmt
       61 tkeclhrfcs dcivtalrsg nkecptcrkk lvskrslrpd pnfdaliski ypsreeyeah
      121 qdrvlirlsr lhnqqalsss ieeglrmqam hraqrvrrpi pgsdqtttms ggegepgege
      181 gdgedvssds apdsapgpap krprgggagg ssvgtggggt ggvgggagse dsgdrggtlg
      241 ggtlgppspp gapsppepgg eielvfrphp llvekgeycq tryvkttgna tvdhlskyla
      301 lrialerrqq qeagepggpg ggasdtggpd gcggegggag ggdgpeepal pslegvsekq
      361 ytiyiapggg afttlngslt lelvnekfwk vsrplelcya ptkdpk
//
LOCUS       NP_001337342             177 aa            linear   PRI 20-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 9 [Homo
            sapiens].
ACCESSION   NP_001337342
VERSION     NP_001337342.1
DBSOURCE    REFSEQ: accession NM_001350413.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390056.7, AL034373.13 and
            AL590011.5.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.283748.1,
                                           SRR1803613.206613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..177
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 9"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=20071
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UR5.1)"
     CDS             1..177
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350413.1:322..855"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mssavgprgp rpptvpppmq elpdlshlte eerniimavm drqkeeeeke eamlkcvvrd
       61 makpaacktp rnaenqphqp sprlhqqfes ykeqvrkige earryqgehk ddaptcgich
      121 ktkfadgcgh lcsycrtkfc arcggrvslr snnedkvvri htffsiicyc ivvnfik
//
LOCUS       NP_001340042             521 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform f [Homo sapiens].
ACCESSION   NP_001340042
VERSION     NP_001340042.1
DBSOURCE    REFSEQ: accession NM_001353113.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, AC026117.15,
            AC139764.5, AC109912.10 and BG182631.1.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.77642.1,
                                           SRR1803613.83212.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..521
                     /product="centrosomal protein of 63 kDa isoform f"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=60566
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <136..464
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96MT8.1)"
     CDS             1..521
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001353113.1:355..1920"
                     /note="isoform f is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS93388.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveair preeslaekk ytsqgqgdld svlsqlnfth tsedllqaev tclegslesv
      361 satckqlsqe lmekyeelkr meahnneyka eikklkeqil qgeqsyssal egmkmeishl
      421 tqelhqrdit iastkgsssd mekrlraemq kaedkavehk eildqleslk lenrhlsemv
      481 mklelglher wgftmlsslv lnfgiqairq pqrpkvlelq v
//
LOCUS       NP_001307949             128 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001307949
VERSION     NP_001307949.1
DBSOURCE    REFSEQ: accession NM_001321020.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Park,J., Wu,J., Szkop,K.J., Jeong,J., Jovanovic,P., Husmann,D.,
            Flores,N.M., Francis,J.W., Chen,Y.C., Benitez,A.M., Zahn,E.,
            Song,S., Ajani,J.A., Wang,L., Singh,K., Larsson,O., Garcia,B.A.,
            Topisirovic,I., Gozani,O. and Mazur,P.K.
  TITLE     SMYD5 methylation of rpL40 links ribosomal output to gastric cancer
  JOURNAL   Nature 632 (8025), 656-663 (2024)
   PUBMED   39048817
  REMARK    GeneRIF: SMYD5 methylation of rpL40 links ribosomal output to
            gastric cancer.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tong,L., Zheng,X., Wang,T., Gu,W., Shen,T., Yuan,W., Wang,S.,
            Xing,S., Liu,X., Zhang,C. and Zhang,C.
  TITLE     Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression
  JOURNAL   J Cell Mol Med 28 (6), e18164 (2024)
   PUBMED   38445807
  REMARK    GeneRIF: Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Lee,S.O., Kelliher,J.L., Song,W., Tengler,K., Sarkar,A., Dray,E.
            and Leung,J.W.C.
  TITLE     UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination
            and DNA repair
  JOURNAL   J Biol Chem 299 (8), 105043 (2023)
   PUBMED   37451480
  REMARK    GeneRIF: UBA80 and UBA52 fine-tune RNF168-dependent histone
            ubiquitination and DNA repair.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Eastham,M.J., Pelava,A., Wells,G.R., Watkins,N.J. and Schneider,C.
  TITLE     RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion Proteins,
            Are Not Essential for p53 Signalling
  JOURNAL   Biomolecules 13 (6), 898 (2023)
   PUBMED   37371478
  REMARK    GeneRIF: RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion
            Proteins, Are Not Essential for p53 Signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin/52-residue ribosomal protein fusion gene
            subfamily (UbA52) is composed primarily of processed pseudogenes
  JOURNAL   Genomics 14 (2), 520-522 (1992)
   PUBMED   1330885
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin-52 amino acid fusion protein gene shares
            several structural features with mammalian ribosomal protein genes
  JOURNAL   Nucleic Acids Res 19 (5), 1035-1040 (1991)
   PUBMED   1850507
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Monia,B.P., Ecker,D.J., Jonnalagadda,S., Marsh,J., Gotlib,L.,
            Butt,T.R. and Crooke,S.T.
  TITLE     Gene synthesis, expression, and processing of human ubiquitin
            carboxyl extension proteins
  JOURNAL   J Biol Chem 264 (7), 4093-4103 (1989)
   PUBMED   2537304
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Salvesen,G., Lloyd,C. and Farley,D.
  TITLE     cDNA encoding a human homolog of yeast ubiquitin 1
  JOURNAL   Nucleic Acids Res 15 (13), 5485 (1987)
   PUBMED   3037496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005253.1, BG035502.1,
            BE514609.1, BQ428515.1, AF545864.1 and BU677484.1.
            
            Summary: Ubiquitin is a highly conserved nuclear and cytoplasmic
            protein that has a major role in targeting cellular proteins for
            degradation by the 26S proteosome. It is also involved in the
            maintenance of chromatin structure, the regulation of gene
            expression, and the stress response. Ubiquitin is synthesized as a
            precursor protein consisting of either polyubiquitin chains or a
            single ubiquitin moiety fused to an unrelated protein. This gene
            encodes a fusion protein consisting of ubiquitin at the N terminus
            and ribosomal protein L40 at the C terminus, a C-terminal extension
            protein (CEP). Multiple processed pseudogenes derived from this
            gene are present in the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.581247.1,
                                           SRR1163658.453403.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..128
                     /product="ubiquitin-ribosomal protein eL40 fusion protein
                     isoform 1 precursor"
                     /note="ubiquitin-52 amino acid fusion protein; ubiquitin
                     carboxyl extension protein 52; ubiquitin-CEP52;
                     ubiquitin-60S ribosomal protein L40; ubiquitin-ribosomal
                     protein eL40 fusion protein"
                     /calculated_mol_wt=14597
     mat_peptide     1..76
                     /product="Ubiquitin. /id=PRO_0000396433"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=8565
     Region          1..76
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(6..9,11,34..37,40,42,44,46..49,68..76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(8..12,31..35,40,42,44,46..49,68,70..76)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            54
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000269|PubMed:24660806,
                     ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
                     ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291;
                     propagated from UniProtKB/Swiss-Prot (P62987.2)"
     Site            68
                     /site_type="other"
                     /note="Essential for function; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            72
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     mat_peptide     77..128
                     /product="Large ribosomal subunit protein eL40.
                     /id=PRO_0000396434"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=6182
     Region          79..126
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     Site            98
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:39048817,
                     ECO:0000269|PubMed:39103523; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     CDS             1..128
                     /gene="UBA52"
                     /gene_synonym="CEP52; HUBCEP52; L40; RPL40"
                     /coded_by="NM_001321020.2:332..718"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS12382.1"
                     /db_xref="GeneID:7311"
                     /db_xref="HGNC:HGNC:12458"
                     /db_xref="MIM:191321"
ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggiiep slrqlaqkyn cdkmicrkcy arlhpravnc rkkkcghtnn
      121 lrpkkkvk
//
LOCUS       NP_001273510            1649 aa            linear   PRI 20-NOV-2025
DEFINITION  PHD and RING finger domain-containing protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001273510 XP_005253081
VERSION     NP_001273510.1
DBSOURCE    REFSEQ: accession NM_001286581.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1649)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1649)
  AUTHORS   Lin,H.W., Shih,T.W., Amanna,A. and Chang,M.S.
  TITLE     PHRF1 Promotes Cell Invasion by Modulating SOX4 Expression in
            Colorectal Cancer HCT116-p53-/- Cells
  JOURNAL   Anticancer Res 43 (12), 5437-5446 (2023)
   PUBMED   38030167
  REMARK    GeneRIF: PHRF1 Promotes Cell Invasion by Modulating SOX4 Expression
            in Colorectal Cancer HCT116-p53[-/-] Cells.
REFERENCE   3  (residues 1 to 1649)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1649)
  AUTHORS   An,C.H., Son,H.J., Yoo,N.J. and Lee,S.H.
  TITLE     Downregulation of a putative tumor suppressor gene PHRF1 in gastric
            and colorectal cancers
  JOURNAL   Pathol Res Pract 216 (6), 152984 (2020)
   PUBMED   32360246
  REMARK    GeneRIF: Downregulation of a putative tumor suppressor gene PHRF1
            in gastric and colorectal cancers.
REFERENCE   5  (residues 1 to 1649)
  AUTHORS   Wang,Y., Wang,H., Pan,T., Li,L., Li,J. and Yang,H.
  TITLE     Overexpression of PHRF1 attenuates the proliferation and
            tumorigenicity of non-small cell lung cancer cells
  JOURNAL   Oncotarget 7 (39), 64360-64370 (2016)
   PUBMED   27608840
  REMARK    GeneRIF: Overexpression of PHRF1 attenuated the proliferation and
            tumorigenicity of non-small cell lung cancer cell lines.
REFERENCE   6  (residues 1 to 1649)
  AUTHORS   Webb,R., Kelly,J.A., Somers,E.C., Hughes,T., Kaufman,K.M.,
            Sanchez,E., Nath,S.K., Bruner,G., Alarcon-Riquelme,M.E.,
            Gilkeson,G.S., Kamen,D.L., Richardson,B.C., Harley,J.B. and
            Sawalha,A.H.
  TITLE     Early disease onset is predicted by a higher genetic risk for lupus
            and is associated with a more severe phenotype in lupus patients
  JOURNAL   Ann Rheum Dis 70 (1), 151-156 (2011)
   PUBMED   20881011
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1649)
  AUTHORS   Sanchez,E., Webb,R.D., Rasmussen,A., Kelly,J.A., Riba,L.,
            Kaufman,K.M., Garcia-de la Torre,I., Moctezuma,J.F.,
            Maradiaga-Cecena,M.A., Cardiel-Rios,M.H., Acevedo,E.,
            Cucho-Venegas,M., Garcia,M.A., Gamron,S., Pons-Estel,B.A.,
            Vasconcelos,C., Martin,J., Tusie-Luna,T., Harley,J.B.,
            Richardson,B., Sawalha,A.H. and Alarcon-Riquelme,M.E.
  TITLE     Genetically determined Amerindian ancestry correlates with
            increased frequency of risk alleles for systemic lupus
            erythematosus
  JOURNAL   Arthritis Rheum 62 (12), 3722-3729 (2010)
   PUBMED   20848568
  REMARK    GeneRIF: Observational study and meta-analysis of gene-disease
            association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 1649)
  AUTHORS   Salloum,R., Franek,B.S., Kariuki,S.N., Rhee,L., Mikolaitis,R.A.,
            Jolly,M., Utset,T.O. and Niewold,T.B.
  TITLE     Genetic variation at the IRF7/PHRF1 locus is associated with
            autoantibody profile and serum interferon-alpha activity in lupus
            patients
  JOURNAL   Arthritis Rheum 62 (2), 553-561 (2010)
   PUBMED   20112359
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1649)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 1649)
  AUTHORS   Harley,J.B., Alarcon-Riquelme,M.E., Criswell,L.A., Jacob,C.O.,
            Kimberly,R.P., Moser,K.L., Tsao,B.P., Vyse,T.J., Langefeld,C.D.,
            Nath,S.K., Guthridge,J.M., Cobb,B.L., Mirel,D.B., Marion,M.C.,
            Williams,A.H., Divers,J., Wang,W., Frank,S.G., Namjou,B.,
            Gabriel,S.B., Lee,A.T., Gregersen,P.K., Behrens,T.W., Taylor,K.E.,
            Fernando,M., Zidovetzki,R., Gaffney,P.M., Edberg,J.C., Rioux,J.D.,
            Ojwang,J.O., James,J.A., Merrill,J.T., Gilkeson,G.S., Seldin,M.F.,
            Yin,H., Baechler,E.C., Li,Q.Z., Wakeland,E.K., Bruner,G.R.,
            Kaufman,K.M. and Kelly,J.A.
  CONSRTM   International Consortium for Systemic Lupus Erythematosus Genetics
            (SLEGEN)
  TITLE     Genome-wide association scan in women with systemic lupus
            erythematosus identifies susceptibility variants in ITGAM, PXK,
            KIAA1542 and other loci
  JOURNAL   Nat Genet 40 (2), 204-210 (2008)
   PUBMED   18204446
  REMARK    GeneRIF: study presents four new regions having genetic
            associations with systemic lupus erythematosus in women of European
            descent: ITGAM, KIAA1542, PXK and rs10798269
            GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA656880.1, BC146771.1 and AP006284.2.
            
            On Nov 8, 2013 this sequence version replaced XP_005253081.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146771.1, AB040975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264555.10/ ENSP00000264555.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..1649
                     /product="PHD and RING finger domain-containing protein 1
                     isoform 1"
                     /note="PHD and RING finger domain-containing protein 1;
                     CTD-binding SR-like protein rA9; protein phosphatase 1,
                     regulatory subunit 125"
                     /calculated_mol_wt=178536
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          <49..106
                     /region_name="DNA_pol_phi"
                     /note="DNA polymerase phi; pfam04931"
                     /db_xref="CDD:461488"
     Region          102..152
                     /region_name="mRING-HC-C3HC3D_PHRF1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in PHD and RING finger domain-containing protein 1
                     (PHRF1) and similar proteins; cd16635"
                     /db_xref="CDD:438297"
     Region          185..230
                     /region_name="PHD_PHRF1"
                     /note="PHD finger found in PHD and RING finger
                     domain-containing protein 1 (PHRF1); cd15536"
                     /db_xref="CDD:277011"
     Site            order(185,197..201,205,225)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277011"
     Region          324..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63625; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          534..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          644..871
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            867
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          888..1240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            936
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            991
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1281..1395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          <1289..1555
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            1359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Site            1404
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1407..1439
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1455..1486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1526..1556
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     Region          1630..1649
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1Y6.3)"
     CDS             1..1649
                     /gene="PHRF1"
                     /gene_synonym="PPP1R125; RNF221"
                     /coded_by="NM_001286581.2:145..5094"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS65988.1"
                     /db_xref="GeneID:57661"
                     /db_xref="HGNC:HGNC:24351"
                     /db_xref="MIM:611780"
ORIGIN      
        1 mdddsldelv arspgpdghp qvgpadpagd feessvgssg dsgddsdseh gdgtdgedeg
       61 aseeedledr sgsedseddg etllevagtq gkleaagsfn sdddaescpi clnafrdqav
      121 gtpencahyf cldcivewsk nanscpvdrt lfkciciraq fggkilrkip ventkaseee
      181 edptfcevcg rsdredrlll cdgcdagyhm ecldpplqev pvdewfcpec aapgvvlaad
      241 agpvseeevs llladvvptt srlrpragrt raiartrqse rvratvnrnr istarrvqht
      301 pgrlgsslld eaieavatgl stavyqrplt prtparrkrk trrrkkvpgr kktpsgpsak
      361 skssatrskk rqhrvkkrrg kkvkseattr sriartlglr rpvhsscips vlkpvepslg
      421 llradigaas lslfgdpyel dpfdsseels anplsplsak rralsrsalq shqpvarpvs
      481 vglsrrrlpa avpepdleee pvpdllgsil sgqsllmlgs sdviihrdgs lsakraapvs
      541 fqrnsgslsr geegfkgclq pralpsgspa qgpsgnrpqs tglscqgrsr tpartagapv
      601 rldlpaapga vqarnlsngs vpgfrqshsp wfngtnkhtl plasaaskis srdskppcrs
      661 vvpgpplkpa prrtdiselp ripkirrddg ggrrdaapah gqsieipsac isrltgregt
      721 gqpgrgtrae seassrvpre pgvhtgssrp papsshgsla plgpsrgkgv gstfesfrin
      781 ipgnmahssq lsspgfcntf rpvddkeqrk enpsplfsik ktkqlrsevy dpsdptgsds
      841 sapgsspers gpgllpseit rtisinspka qtvqavrcvt sytvesifgt epepplgpss
      901 amsklrgava aegasdtere eptesqglaa rlrrpsppep wdeedgascs tffgseertv
      961 tcvtvvepea ppspdvlqaa thrvvelrpp srsrstsssr srkkakrkrv srehgrtrsg
     1021 trsesrdrss rsaspsvgee rprrqrskak srrsssdrss srerakrkka kdksrehrrg
     1081 pwghsrrtsr srsgspgsss yehyesrkkk krrsasrprg recsptssle rlcrhkhqre
     1141 rsherpdrke svawprdrrk rrsrspsseh rarehrrprs rekwpqtrsh sperkgavre
     1201 aspaplaqge pgredlptrl palgeahvsp evatadkapl qappvlevaa ecepddldld
     1261 ygdsveaghv fddfssdavf iqlddmsspp spestdsspe rdfplkpalp paslavaaiq
     1321 revslmhded psqppplpeg tqephllrpd aaekaeapss pdvapagked spsasgrvqe
     1381 aarpeevvsq tpllrsralv krvtwnlqes essapaedra praplhrpqk pregawdmed
     1441 vaptgvrqvf selpfpshvl pepgfpdtdp sqvyspglpp apaqpssipp calvsqptvq
     1501 filqgslplv gcgaaqtlap vpaaltpase pasqataasn seektpaprl aaektkkeey
     1561 mkklhmqera veevklaikp fyqkrevtke eykdilrkav qkichsksge inpvkvanlv
     1621 kayvdkyrhm rrhkkpeage epptqgaeg
//
LOCUS       NP_001230443             435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_001230443
VERSION     NP_001230443.1
DBSOURCE    REFSEQ: accession NM_001243514.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096635.2, AY388461.1,
            AB020639.1 and BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (14) lacks the 5' exon but has an
            alternate 5' exon and uses a downstream AUG start codon, compared
            to variant 1. The resulting isoform (2) is shorter at the
            N-terminus, compared to isoform 1. Variants 2-4, 9-15, and 17-21
            encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803612.73108.1, SRR1803614.69207.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243514.2:457..1764"
                     /note="isoform 2 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_056263                203 aa            linear   PRI 20-NOV-2025
DEFINITION  protein DPCD isoform 2 [Homo sapiens].
ACCESSION   NP_056263
VERSION     NP_056263.1
DBSOURCE    REFSEQ: accession NM_015448.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Dos Santos Morais,R., Santo,P.E., Ley,M., Schelcher,C., Abel,Y.,
            Plassart,L., Desligniere,E., Chagot,M.E., Quinternet,M.,
            Paiva,A.C.F., Hessmann,S., Morellet,N., M F Sousa,P.,
            Vandermoere,F., Bertrand,E., Charpentier,B., Bandeiras,T.M.,
            Plisson-Chastang,C., Verheggen,C., Cianferani,S. and Manival,X.
  TITLE     Deciphering cellular and molecular determinants of human DPCD
            protein in complex with RUVBL1/RUVBL2 AAA-ATPases
  JOURNAL   J Mol Biol 434 (19), 167760 (2022)
   PUBMED   35901867
  REMARK    GeneRIF: Deciphering cellular and molecular determinants of human
            DPCD protein in complex with RUVBL1/RUVBL2 AAA-ATPases.
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Zariwala,M., O'Neal,W.K., Noone,P.G., Leigh,M.W., Knowles,M.R. and
            Ostrowski,L.E.
  TITLE     Investigation of the possible role of a novel gene, DPCD, in
            primary ciliary dyskinesia
  JOURNAL   Am J Respir Cell Mol Biol 30 (4), 428-434 (2004)
   PUBMED   14630615
  REMARK    GeneRIF: a novel candidate gene for primary ciliary dyskinesia
            GeneRIF: The mouse homolog of this gene (named Dpcd, for Deleted in
            a mouse model of Primary Ciliary Dyskinesia) appears to be
            responsible for an inner arm defect in cilia.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY030728.1, BC001082.2 and
            BX361465.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene in mouse encodes a protein that may be involved
            in the generation and maintenance of ciliated cells. In mouse,
            expression of this gene increases during ciliated cell
            differentiation, and disruption of this gene has been linked to
            primary ciliary dyskinesia. [provided by RefSeq, Jul 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.501815.1,
                                           SRR5189667.321523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370151.9/ ENSP00000359170.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..203
                     /product="protein DPCD isoform 2"
                     /note="protein DPCD; deleted in a mouse model of primary
                     ciliary dyskinesia; RP11-529I10.4"
                     /calculated_mol_wt=23109
     Region          6..194
                     /region_name="DPCD"
                     /note="DPCD protein family; pfam14913"
                     /db_xref="CDD:464369"
     CDS             1..203
                     /gene="DPCD"
                     /coded_by="NM_015448.3:17..628"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS7514.1"
                     /db_xref="GeneID:25911"
                     /db_xref="HGNC:HGNC:24542"
                     /db_xref="MIM:616467"
ORIGIN      
        1 mavtgwlesl rtaqktallq dgrrkvhylf pdgkemaeey dektsellvr kwrvksalga
       61 mgqwqlevgd paplgagnlg pelikesnan pifmrkdtkm sfqwrirnlp ypkdvysvsv
      121 dqkerciivr ttnkkyykkf sipdldrhql plddallsfa hanctliisy qkpkevvvae
      181 selqkelkkv ktahsndgdc ktq
//
LOCUS       NP_001017361             217 aa            linear   PRI 20-NOV-2025
DEFINITION  KH domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_001017361 XP_087901
VERSION     NP_001017361.1
DBSOURCE    REFSEQ: accession NM_001017361.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Rath,A., Sethi,P., Jena,S.K. and Mitra,S.
  TITLE     Familial recurrent molar pregnancy: positive for KHDC3L gene
            mutation
  JOURNAL   BMJ Case Rep 16 (11), e254435 (2023)
   PUBMED   37918946
  REMARK    GeneRIF: Familial recurrent molar pregnancy: positive for KHDC3L
            gene mutation.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Pignata,L., Cecere,F., Verma,A., Hay Mele,B., Monticelli,M.,
            Acurzio,B., Giaccari,C., Sparago,A., Hernandez Mora,J.R.,
            Monteagudo-Sanchez,A., Esteller,M., Pereda,A., Tenorio-Castano,J.,
            Palumbo,O., Carella,M., Prontera,P., Piscopo,C., Accadia,M.,
            Lapunzina,P., Cubellis,M.V., de Nanclares,G.P., Monk,D., Riccio,A.
            and Cerrato,F.
  TITLE     Novel genetic variants of KHDC3L and other members of the
            subcortical maternal complex associated with Beckwith-Wiedemann
            syndrome or Pseudohypoparathyroidism 1B and multi-locus imprinting
            disturbances
  JOURNAL   Clin Epigenetics 14 (1), 71 (2022)
   PUBMED   35643636
  REMARK    GeneRIF: Novel genetic variants of KHDC3L and other members of the
            subcortical maternal complex associated with Beckwith-Wiedemann
            syndrome or Pseudohypoparathyroidism 1B and multi-locus imprinting
            disturbances.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Liu,J., Tan,Z., He,J., Jin,T., Han,Y., Hu,L. and Huang,S.
  TITLE     Two novel mutations in PADI6 and TLE6 genes cause female
            infertility due to arrest in embryonic development
  JOURNAL   J Assist Reprod Genet 38 (6), 1551-1559 (2021)
   PUBMED   34036456
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Fatemi,N., Ray,P.F., Ramezanali,F., Shahani,T., Amiri-Yekta,A.,
            Kherraf,Z.E., Cazin,C., Almadani,N., Varkiani,M., Sarmadi,S.,
            Sodeifi,N., Gourabi,H., Biglari,A. and Totonchi,M.
  TITLE     KH domain containing 3 like (KHDC3L) frame-shift mutation causes
            both recurrent pregnancy loss and hydatidiform mole
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 259, 100-104 (2021)
   PUBMED   33639414
  REMARK    GeneRIF: KH domain containing 3 like (KHDC3L) frame-shift mutation
            causes both recurrent pregnancy loss and hydatidiform mole.
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Andreasen,L., Bolund,L., Niemann,I., Hansen,E.S. and Sunde,L.
  TITLE     Mosaic moles and non-familial biparental moles are not caused by
            mutations in NLRP7, NLRP2 or C6orf221
  JOURNAL   Mol Hum Reprod 18 (12), 593-598 (2012)
   PUBMED   22909446
  REMARK    GeneRIF: Observations suggest that although NLRP7 and C6orf221
            mutations are related to diploid biparental FRHMs, neither of these
            genes, nor NLRP2, are related to diploid HMs with biparental
            contributions to the molar genome.
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Parry,D.A., Logan,C.V., Hayward,B.E., Shires,M., Landolsi,H.,
            Diggle,C., Carr,I., Rittore,C., Touitou,I., Philibert,L.,
            Fisher,R.A., Fallahian,M., Huntriss,J.D., Picton,H.M., Malik,S.,
            Taylor,G.R., Johnson,C.A., Bonthron,D.T. and Sheridan,E.G.
  TITLE     Mutations causing familial biparental hydatidiform mole implicate
            c6orf221 as a possible regulator of genomic imprinting in the human
            oocyte
  JOURNAL   Am J Hum Genet 89 (3), 451-458 (2011)
   PUBMED   21885028
  REMARK    GeneRIF: Mutations causing familial biparental hydatidiform mole
            implicate c6orf221 as a possible regulator of genomic imprinting in
            the human oocyte.
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Pierre,A., Gautier,M., Callebaut,I., Bontoux,M., Jeanpierre,E.,
            Pontarotti,P. and Monget,P.
  TITLE     Atypical structure and phylogenomic evolution of the new eutherian
            oocyte- and embryo-expressed KHDC1/DPPA5/ECAT1/OOEP gene family
  JOURNAL   Genomics 90 (5), 583-594 (2007)
   PUBMED   17913455
  REMARK    GeneRIF: This paper states that ECAT1 is not found in rodents.
REFERENCE   9  (residues 1 to 217)
  AUTHORS   Mitsui,K., Tokuzawa,Y., Itoh,H., Segawa,K., Murakami,M.,
            Takahashi,K., Maruyama,M., Maeda,M. and Yamanaka,S.
  TITLE     The homeoprotein Nanog is required for maintenance of pluripotency
            in mouse epiblast and ES cells
  JOURNAL   Cell 113 (5), 631-642 (2003)
   PUBMED   12787504
REFERENCE   10 (residues 1 to 217)
  AUTHORS   Tumer,Z., Eggermann,T., Maas,S., Bliek,J. and Mackay,D.
  TITLE     Maternal Effect Gene-Related Multilocus Imprinting Disturbances
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC019205.4, AB211062.1 and
            AI638315.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 22, 2005 this sequence version replaced XP_087901.2.
            
            Summary: The protein encoded by this gene belongs to the KHDC1
            family, members of which contain an atypical KH domain that may not
            bind RNA like canonical KH domains. This gene is specifically
            expressed in the oocytes, and recent studies suggest that it may
            function as a regulator of genomic imprinting in the oocyte.
            Mutations in this gene are associated with recurrent biparental
            complete hydatidiform mole. [provided by RefSeq, Dec 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB211062.1, BC132844.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370367.4/ ENSP00000359392.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..217
                     /product="KH domain-containing protein 3"
                     /note="ES cell-associated transcript 1 protein; KHDC3-like
                     protein"
                     /calculated_mol_wt=24175
     Region          1..40
                     /region_name="Involved in RNA binding.
                     /evidence=ECO:0000250|UniProtKB:Q9CWU5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q587J8.1)"
     Region          29..112
                     /region_name="MOEP19"
                     /note="KH-like RNA-binding domain; pfam16005"
                     /db_xref="CDD:464969"
     Region          129..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q587J8.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM.
                     /evidence=ECO:0000269|PubMed:31609975; propagated from
                     UniProtKB/Swiss-Prot (Q587J8.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by ATM.
                     /evidence=ECO:0000269|PubMed:31609975; propagated from
                     UniProtKB/Swiss-Prot (Q587J8.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CWU5; propagated from
                     UniProtKB/Swiss-Prot (Q587J8.1)"
     CDS             1..217
                     /gene="KHDC3L"
                     /gene_synonym="C6orf221; ECAT1; HYDM2"
                     /coded_by="NM_001017361.3:73..726"
                     /db_xref="CCDS:CCDS34484.1"
                     /db_xref="GeneID:154288"
                     /db_xref="HGNC:HGNC:33699"
                     /db_xref="MIM:611687"
ORIGIN      
        1 mdaprrfptl vqlmqpkamp vevlghlpkr fswfhseflk npkvvrlevw lvekifgrgg
       61 eriphvqgms qilihvnrld pngeaeilvf grpsyqedti kmimnladyh rqlqakgsgk
      121 alaqdvatqk aetqrssiev reagtqrsve vreagtqrsv evqevgtqgs pvevqeagtq
      181 qslqaanksg tqrspeaask avtqrfreda rdpvtrl
//
LOCUS       NP_055086                696 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein-like 1 precursor [Homo
            sapiens].
ACCESSION   NP_055086
VERSION     NP_055086.1
DBSOURCE    REFSEQ: accession NM_014271.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Yu,M., Zhang,Q., Wan,L., Wang,S., Zou,L., Chen,Z. and Li,F.
  TITLE     IL-1R8 expression in DLBCL regulates NK cell recruitment and
            influences patient prognosis
  JOURNAL   Funct Integr Genomics 23 (4), 328 (2023)
   PUBMED   37907630
  REMARK    GeneRIF: IL-1R8 expression in DLBCL regulates NK cell recruitment
            and influences patient prognosis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Kanwal,A., Pardo,J.V. and Naz,S.
  TITLE     RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias
  JOURNAL   J Psychiatry Neurosci 47 (6), E379-E390 (2022)
   PUBMED   36318984
  REMARK    GeneRIF: RGS3 and IL1RAPL1 missense variants implicate defective
            neurotransmission in early-onset inherited schizophrenias.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Montani,C., Gritti,L., Beretta,S., Verpelli,C. and Sala,C.
  TITLE     The Synaptic and Neuronal Functions of the X-Linked Intellectual
            Disability Protein Interleukin-1 Receptor Accessory Protein Like 1
            (IL1RAPL1)
  JOURNAL   Dev Neurobiol 79 (1), 85-95 (2019)
   PUBMED   30548231
  REMARK    GeneRIF: The mutations and deletion of IL1RAPL1 gene are related to
            different phenotypes (even in the same family and in patients with
            the same mutation) including different severity of Intellectual
            Disability.
            Review article
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Sun,Z. and Chadwick,B.P.
  TITLE     Loss of SETDB1 decompacts the inactive X chromosome in part through
            reactivation of an enhancer in the IL1RAPL1 gene
  JOURNAL   Epigenetics Chromatin 11 (1), 45 (2018)
   PUBMED   30103804
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Tranebjaerg,L., Lubs,H.A., Borghgraef,M., Brown,W.T., Fisch,G.,
            Fryns,J.P., Hagerman,R., Jacobs,P.A., Mandel,J.L., Mulley,J.,
            Oostra,B., Schwartz,C., Sherman,S., Willard,H. and Willems,P.
  TITLE     Seventh International Workshop on the Fragile X and X-linked Mental
            Retardation
  JOURNAL   Am J Med Genet 64 (1), 1-14 (1996)
   PUBMED   8826442
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Liu,C., Chalmers,D., Maki,R. and De Souza,E.B.
  TITLE     Rat homolog of mouse interleukin-1 receptor accessory protein:
            cloning, localization and modulation studies
  JOURNAL   J Neuroimmunol 66 (1-2), 41-48 (1996)
   PUBMED   8964912
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Kozak,L., Chiurazzi,P., Genuardi,M., Pomponi,M.G., Zollino,M. and
            Neri,G.
  TITLE     Mapping of a gene for non-specific X linked mental retardation:
            evidence for linkage to chromosomal region Xp21.1-Xp22.3
  JOURNAL   J Med Genet 30 (10), 866-869 (1993)
   PUBMED   8230164
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   10 (residues 1 to 696)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112495.2, AJ243874.1,
            DN994486.1, AF284435.1 and AC005748.10.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            interleukin 1 receptor family and is similar to the interleukin 1
            accessory proteins. This protein has an N-terminal signal peptide,
            three extracellular immunoglobulin Ig-like domains, a transmembrane
            domain, an intracellular Toll/IL-1R domain, and a long C-terminal
            tail which interacts with multiple signalling molecules. This gene
            is located at a region on chromosome X that is associated with a
            non-syndromic form of X-linked intellectual disability. Deletions
            and mutations in this gene were found in patients with intellectual
            disability. This gene is expressed at a high level in post-natal
            brain structures involved in the hippocampal memory system, which
            suggests a specialized role in the physiological processes
            underlying memory and learning abilities, and plays a role in
            synapse formation and stabilization. [provided by RefSeq, Jul
            2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ243874.1, SRR1803611.4925.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378993.6/ ENSP00000368278.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.3-p21.2"
     Protein         1..696
                     /product="interleukin-1 receptor accessory protein-like 1
                     precursor"
                     /EC_number="3.2.2.6"
                     /note="X-linked interleukin-1 receptor accessory
                     protein-like 1; oligophrenin-4; interleukin 1 receptor-8;
                     three immunoglobulin domain-containing IL-1
                     receptor-related 2"
                     /calculated_mol_wt=77943
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2044
     mat_peptide     19..696
                     /product="interleukin-1 receptor accessory protein-like 1"
                     /calculated_mol_wt=77943
     Region          32..136
                     /region_name="Ig1_IL1RAPL-1_like"
                     /note="First immunoglobulin (Ig)-like domain of X-linked
                     interleukin-1 receptor accessory protein-like 1
                     (IL1RAPL-1), and similar domains; cd05896"
                     /db_xref="CDD:409477"
     Region          33..36
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409477"
     Site            order(34,36..41)
                     /site_type="other"
                     /note="putative antagonist binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409477"
     Site            34
                     /site_type="other"
                     /note="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:P59823; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          40..44
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409477"
     Region          48..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409477"
     Site            63
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          73..77
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409477"
     Region          86..88
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409477"
     Region          95..99
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409477"
     Region          101..105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409477"
     Region          114..122
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409477"
     Site            122
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          125..136
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409477"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          148..234
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          160..164
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          178..182
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          199..203
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          213..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            213
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          226..229
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          248..350
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          263..267
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            264
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          280..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          317..321
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          331..336
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            331
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Site            358..378
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          405..559
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          549..644
                     /region_name="Interaction with NCS1.
                     /evidence=ECO:0000269|PubMed:12783849"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN1.2)"
     Region          659..680
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZN1.2)"
     CDS             1..696
                     /gene="IL1RAPL1"
                     /gene_synonym="IL-1-RAPL-1; IL-1RAPL-1; IL1R8; IL1RAPL;
                     IL1RAPL-1; MRX10; MRX21; MRX34; OPHN4; TIGIRR-2"
                     /coded_by="NM_014271.4:627..2717"
                     /db_xref="CCDS:CCDS14218.1"
                     /db_xref="GeneID:11141"
                     /db_xref="HGNC:HGNC:5996"
                     /db_xref="MIM:300206"
ORIGIN      
        1 mkapiphlil lyatftqslk vvtkrgsadg ctdwsidikk yqvlvgepvr ikcalfygyi
       61 rtnyslaqsa glslmwykss gpgdfeepia fdgsrmskee dsiwfrptll qdsglyacvi
      121 rnstycmkvs isltvgendt glcynskmky fekaelsksk eiscrdiedf llptrepeil
      181 wykecrtktw rpsivfkrdt llirevredd ignytcelky ggfvvrrtte ltvtapltdk
      241 ppkllypmes kltiqetqlg dsanltcraf fgysgdvspl iywmkgekfi edldenrvwe
      301 sdirilkehl geqevsisli vdsveegdlg nyscyvengn grrhasvllh krelmytvel
      361 agglgailll lvclvtiykc ykieimlfyr nhfgaeeldg dnkdydayls ytkvdpdqwn
      421 qetgeeerfa leilpdmlek hygyklfipd rdliptgtyi edvarcvdqs krliivmtpn
      481 yvvrrgwsif eletrlrnml vtgeikvili ecselrgimn yqevealkht iklltvikwh
      541 gpkcnklnsk fwkrlqyemp fkriepithe qaldvseqgp fgelqtvsai smaaatstal
      601 atahpdlrst fhntyhsqmr qkhyyrsyey dvpptgtlpl tsignqhtyc nipmtlingq
      661 rpqtkssreq npdeahtnsa ilpllprets issviw
//
LOCUS       NP_878914                429 aa            linear   PRI 20-NOV-2025
DEFINITION  nesprin-2 isoform 2 [Homo sapiens].
ACCESSION   NP_878914
VERSION     NP_878914.1
DBSOURCE    REFSEQ: accession NM_182910.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Li Mow Chee,F., Beernaert,B., Griffith,B.G.C., Loftus,A.E.P.,
            Kumar,Y., Wills,J.C., Lee,M., Valli,J., Wheeler,A.P.,
            Armstrong,J.D., Parsons,M., Leigh,I.M., Proby,C.M., von
            Kriegsheim,A., Bickmore,W.A., Frame,M.C. and Byron,A.
  TITLE     Mena regulates nesprin-2 to control actin-nuclear lamina
            associations, trans-nuclear membrane signalling and gene expression
  JOURNAL   Nat Commun 14 (1), 1602 (2023)
   PUBMED   36959177
  REMARK    GeneRIF: Mena regulates nesprin-2 to control actin-nuclear lamina
            associations, trans-nuclear membrane signalling and gene
            expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Yi,J., Zhao,X., Noell,C.R., Helmer,P., Solmaz,S.R. and Vallee,R.B.
  TITLE     Role of Nesprin-2 and RanBP2 in BICD2-associated brain
            developmental disorders
  JOURNAL   PLoS Genet 19 (3), e1010642 (2023)
   PUBMED   36930595
  REMARK    GeneRIF: Role of Nesprin-2 and RanBP2 in BICD2-associated brain
            developmental disorders.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Xu,Q., Miao,Y., Ren,J., Sun,Y., Li,C., Cai,X. and Wang,Z.
  TITLE     Silencing of Nesprin-2 inhibits the differentiation of
            myofibroblasts from fibroblasts induced by mechanical stretch
  JOURNAL   Int Wound J 19 (5), 978-986 (2022)
   PUBMED   34558192
  REMARK    GeneRIF: Silencing of Nesprin-2 inhibits the differentiation of
            myofibroblasts from fibroblasts induced by mechanical stretch.
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Wallis,S.S., Ventimiglia,L.N., Otigbah,E., Infante,E.,
            Cuesta-Geijo,M.A., Kidiyoor,G.R., Carbajal,M.A., Fleck,R.A.,
            Foiani,M., Garcia-Manyes,S., Martin-Serrano,J. and Agromayor,M.
  TITLE     The ESCRT machinery counteracts Nesprin-2G-mediated mechanical
            forces during nuclear envelope repair
  JOURNAL   Dev Cell 56 (23), 3192-3202 (2021)
   PUBMED   34818527
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Zhang,Q., Ragnauth,C., Greener,M.J., Shanahan,C.M. and Roberts,R.G.
  TITLE     The nesprins are giant actin-binding proteins, orthologous to
            Drosophila melanogaster muscle protein MSP-300
  JOURNAL   Genomics 80 (5), 473-481 (2002)
   PUBMED   12408964
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Zhen,Y.Y., Libotte,T., Munck,M., Noegel,A.A. and Korenbaum,E.
  TITLE     NUANCE, a giant protein connecting the nucleus and actin
            cytoskeleton
  JOURNAL   J Cell Sci 115 (Pt 15), 3207-3222 (2002)
   PUBMED   12118075
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Zhang,Q., Skepper,J.N., Yang,F., Davies,J.D., Hegyi,L.,
            Roberts,R.G., Weissberg,P.L., Ellis,J.A. and Shanahan,C.M.
  TITLE     Nesprins: a novel family of spectrin-repeat-containing proteins
            that localize to the nuclear membrane in multiple tissues
  JOURNAL   J Cell Sci 114 (Pt 24), 4485-4498 (2001)
   PUBMED   11792814
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Apel,E.D., Lewis,R.M., Grady,R.M. and Sanes,J.R.
  TITLE     Syne-1, a dystrophin- and Klarsicht-related protein associated with
            synaptic nuclei at the neuromuscular junction
  JOURNAL   J Biol Chem 275 (41), 31986-31995 (2000)
   PUBMED   10878022
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY184204.1 and AI685725.1.
            
            Summary: The protein encoded by this gene is a nuclear outer
            membrane protein that binds cytoplasmic F-actin. This binding
            tethers the nucleus to the cytoskeleton and aids in the maintenance
            of the structural integrity of the nucleus. Several transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 5. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL117404.1, AY184204.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.2"
     Protein         1..429
                     /product="nesprin-2 isoform 2"
                     /note="nesprin 2; synaptic nuclei expressed gene 2;
                     polytrophin; synaptic nuclear envelope protein 2; nuclear
                     envelope spectrin repeat protein 2; nucleus and actin
                     connecting element protein; spectrin repeat containing,
                     nuclear envelope 2; KASH domain-containing protein 2;
                     nesprin-2 spectrin repeats 3-54"
                     /calculated_mol_wt=48028
     Region          84..307
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            190..195
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          <398..429
                     /region_name="KASH"
                     /note="Nuclear envelope localization domain; pfam10541"
                     /db_xref="CDD:463142"
     CDS             1..429
                     /gene="SYNE2"
                     /gene_synonym="EDMD5; KASH2; Nesp2; Nesprin-2; NUA;
                     NUANCE; SYNE-2; TROPH"
                     /coded_by="NM_182910.2:369..1658"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23224"
                     /db_xref="HGNC:HGNC:17084"
                     /db_xref="MIM:608442"
ORIGIN      
        1 megdrnvppv ppasstpykp pygklllppg tdggkegprv lngnpqqedg glagiteqqs
       61 gafdrwemiq aqelhnklki kqnlqqlnsd isaittwlkk teaelemlkm akppsdiqei
      121 elrvkrlqei lkafdtykal vvsvnvsske flqtespest elqsrlrqls llweaaqgav
      181 dswrgglrqs lmqcqgsktr prsdvlffkd fhqlsqnlll wlasaknrrq kahvtdpkad
      241 prallecrre lmqlekelve rqpqvdmlqe isnsllikgh gedcieaeek vhviekklkq
      301 lreqvsqdlm alqgtqnpas plpsfdevds gdqppatsvp aprakfravr ttegeeetes
      361 rvpgstrpqr sflsrvvraa lplqllllll lllacllpss eedysctqan nfarsfypml
      421 rytngpppt
//
LOCUS       NP_036555                203 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL13 isoform 1 [Homo sapiens].
ACCESSION   NP_036555
VERSION     NP_036555.1
DBSOURCE    REFSEQ: accession NM_012423.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Molavi,G., Samadi,N., Hashemzadeh,S., Halimi,M. and
            Hosseingholi,E.Z.
  TITLE     Moonlight human ribosomal protein L13a downregulation is associated
            with p53 and HER2/neu expression in breast cancer
  JOURNAL   J Appl Biomed 18 (2-3), 46-53 (2020)
   PUBMED   34907725
  REMARK    GeneRIF: Moonlight human ribosomal protein L13a downregulation is
            associated with p53 and HER2/neu expression in breast cancer.
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Kour,R., Komar,A.A. and Mazumder,B.
  TITLE     Mutually exclusive amino acid residues of L13a are responsible for
            its ribosomal incorporation and translational silencing leading to
            resolution of inflammation
  JOURNAL   RNA 25 (10), 1377-1392 (2019)
   PUBMED   31308261
  REMARK    GeneRIF: show through cellular immunofluorescence experiments that
            nuclear but not nucleolar localization of L13a is resistant to
            extensive amino acid alterations, suggesting that multiple complex
            nuclear import signals are present within this protein
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Nicoloso,M., Qu,L.H., Michot,B. and Bachellerie,J.P.
  TITLE     Intron-encoded, antisense small nucleolar RNAs: the
            characterization of nine novel species points to their direct role
            as guides for the 2'-O-ribose methylation of rRNAs
  JOURNAL   J Mol Biol 260 (2), 178-195 (1996)
   PUBMED   8764399
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 203)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 203)
  AUTHORS   Price,S.R., Nightingale,M.S., Bobak,D.A., Tsuchiya,M., Moss,J. and
            Vaughan,M.
  TITLE     Conservation of a 23-kDa human transplantation antigen in mammalian
            species
  JOURNAL   Genomics 14 (4), 959-964 (1992)
   PUBMED   1282492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AK291120.1 and BC062537.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a member of the
            L13P family of ribosomal proteins that is a component of the 60S
            subunit. The encoded protein also plays a role in the repression of
            inflammatory genes as a component of the IFN-gamma-activated
            inhibitor of translation (GAIT) complex. This gene is
            co-transcribed with the small nucleolar RNA genes U32, U33, U34,
            and U35, which are located in the second, fourth, fifth, and sixth
            introns, respectively. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed throughout the genome. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070223.1, SRR1660805.176507.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000391857.9/ ENSP00000375730.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..203
                     /product="large ribosomal subunit protein uL13 isoform 1"
                     /note="tissue specific transplantation antigen 1; 60S
                     ribosomal protein L13a; 23 kDa highly basic protein; large
                     ribosomal subunit protein uL13; epididymis secretory sperm
                     binding protein; highly basic protein 23 kDa"
                     /calculated_mol_wt=23446
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12962325,
                     ECO:0000269|PubMed:25489052, ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P40429.2)"
     Region          6..200
                     /region_name="PTZ00068"
                     /note="60S ribosomal protein L13a; Provisional"
                     /db_xref="CDD:240253"
     Site            order(15,17..18,21,24,28,44,46,74..75,81..83,85..87,89,
                     91..92,94,96,100,103..104)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238230"
     Site            75
                     /site_type="other"
                     /note="L3 interface [polypeptide binding]"
                     /db_xref="CDD:238230"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ZIPK/DAPK3.
                     /evidence=ECO:0000269|PubMed:18995835; propagated from
                     UniProtKB/Swiss-Prot (P40429.2)"
     Site            191
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P40429.2)"
     CDS             1..203
                     /gene="RPL13A"
                     /gene_synonym="L13A; TSTA1; uL13"
                     /coded_by="NM_012423.4:23..634"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12768.1"
                     /db_xref="GeneID:23521"
                     /db_xref="HGNC:HGNC:10304"
                     /db_xref="MIM:619225"
ORIGIN      
        1 maevqvlvld grghllgrla aivakqvllg rkvvvvrceg inisgnfyrn klkylaflrk
       61 rmntnpsrgp yhfrapsrif wrtvrgmlph ktkrgqaald rlkvfdgipp pydkkkrmvv
      121 paalkvvrlk ptrkfaylgr lahevgwkyq avtatleekr kekakihyrk kkqlmrlrkq
      181 aeknvekkid kytevlkthg llv
//
LOCUS       NP_062547                822 aa            linear   PRI 20-NOV-2025
DEFINITION  sushi domain-containing protein 2 precursor [Homo sapiens].
ACCESSION   NP_062547
VERSION     NP_062547.1
DBSOURCE    REFSEQ: accession NM_019601.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Bai,H., Xian,N., Zhao,F., Zhou,Y. and Qin,S.
  TITLE     The dual role of SUSD2 in cancer development
  JOURNAL   Eur J Pharmacol 977, 176754 (2024)
   PUBMED   38897441
  REMARK    GeneRIF: The dual role of SUSD2 in cancer development.
            Review article
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Wu,Y., Duan,Y., Li,X., Zhao,R., Lan,B., Zhang,X., Wang,X., Chen,H.,
            Feng,S., Liu,Z., Cheng,Y., Xi,L., Wang,Y., Xue,F. and Xuan,C.
  TITLE     CBX8 Together with SET Facilitates Ovarian Carcinoma Growth and
            Metastasis by Suppressing the Transcription of SUSD2
  JOURNAL   Mol Cancer Res 20 (11), 1611-1622 (2022)
   PUBMED   35894945
  REMARK    GeneRIF: CBX8 Together with SET Facilitates Ovarian Carcinoma
            Growth and Metastasis by Suppressing the Transcription of SUSD2.
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Liu,S. and Wen,C.
  TITLE     miR-141-3p promotes retinoblastoma progression via inhibiting sushi
            domain-containing protein 2
  JOURNAL   Bioengineered 13 (3), 7410-7424 (2022)
   PUBMED   35259051
  REMARK    GeneRIF: miR-141-3p promotes retinoblastoma progression via
            inhibiting sushi domain-containing protein 2.
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Xia,L., Zhu,G., Huang,H., He,Y. and Liu,X.
  TITLE     LncRNA small nucleolar RNA host gene 16 (SNHG16) silencing protects
            lipopolysaccharide (LPS)-induced cell injury in human lung
            fibroblasts WI-38 through acting as miR-141-3p sponge
  JOURNAL   Biosci Biotechnol Biochem 85 (5), 1077-1087 (2021)
   PUBMED   33836533
  REMARK    GeneRIF: LncRNA small nucleolar RNA host gene 16 (SNHG16) silencing
            protects lipopolysaccharide (LPS)-induced cell injury in human lung
            fibroblasts WI-38 through acting as miR-141-3p sponge.
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Sivasubramaniyan,K., Harichandan,A., Schumann,S., Sobiesiak,M.,
            Lengerke,C., Maurer,A., Kalbacher,H. and Buhring,H.J.
  TITLE     Prospective isolation of mesenchymal stem cells from human bone
            marrow using novel antibodies directed against Sushi domain
            containing 2
  JOURNAL   Stem Cells Dev 22 (13), 1944-1954 (2013)
   PUBMED   23406305
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Watson,A.P., Evans,R.L. and Egland,K.A.
  TITLE     Multiple functions of sushi domain containing 2 (SUSD2) in breast
            tumorigenesis
  JOURNAL   Mol Cancer Res 11 (1), 74-85 (2013)
   PUBMED   23131994
  REMARK    GeneRIF: Authors found significantly fewer CD4 tumor infiltrating
            lymphocytes in breast tumors expressing Susd2.
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. 2nd, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC033107.1 and BI822588.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033107.1, SRR1803615.96957.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358321.4/ ENSP00000351075.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     Protein         1..822
                     /product="sushi domain-containing protein 2 precursor"
                     /note="Sushi domain (SCR repeat) containing; sushi
                     domain-containing protein 2; testicular tissue protein Li
                     190"
                     /calculated_mol_wt=87570
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2656
     mat_peptide     28..822
                     /product="Sushi domain-containing protein 2.
                     /id=PRO_0000249439"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGT4.1)"
                     /calculated_mol_wt=87570
     Region          29..64
                     /region_name="Somatomedin_B"
                     /note="Somatomedin B domain; pfam01033"
                     /db_xref="CDD:460034"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Site            177
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Region          289..429
                     /region_name="AMOP"
                     /note="AMOP domain; pfam03782"
                     /db_xref="CDD:461048"
     Region          448..613
                     /region_name="VWD"
                     /note="von Willebrand factor type D domain; pfam00094"
                     /db_xref="CDD:459671"
     Site            522
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q9UGT4.1)"
     Region          725..779
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(735,752)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Site            786..806
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UGT4.1)"
     CDS             1..822
                     /gene="SUSD2"
                     /gene_synonym="BK65A6.2; W5C5"
                     /coded_by="NM_019601.4:34..2502"
                     /db_xref="CCDS:CCDS13824.1"
                     /db_xref="GeneID:56241"
                     /db_xref="HGNC:HGNC:30667"
                     /db_xref="MIM:615825"
ORIGIN      
        1 mkpallpwal lllatalgpg pgptadaqes csmrcgaldg pcschptcsg lgtccldfrd
       61 fcleilpysg smmggkdfvv rhfkmssptd asvicrfkds iqtlghvdss gqvhcvspll
      121 yesgripftv sldnghsfpr agtwlavhpn kvsmmeksel vnetrwqyyg tantsgnlsl
      181 twhvkslptq titielwgye etgmpysqew takwsylypl athipnsgsf tftpkpapps
      241 yqrwrvgalr iidsknyagq kdvqalwtnd halawhlsdd fredpvawar tqcqaweele
      301 dqlpnfleel pdcpctltqa radsgrfftd ygcdmeqgsv ctyhpgavhc vrsvqaslry
      361 gsgqqccyta dgtqlltads sggstpdrgh dwgappfrtp prvpsmshwl ydvlsfyycc
      421 lwapdcprym qrrpsndcrn yrpprlasaf gdphfvtfdg tnftfngrge yvlleaaltd
      481 lrvqaraqpg tmsngtetrg tgltavavqe gnsdvvevrl anrtgglevl lnqevlsfte
      541 qswmdlkgmf lsvaagdrvs imlasgagle vsvqgpflsv svllpekflt hthgllgtln
      601 ndptddftlh sgrvlppgts pqelflfgan wtvhnassll tydswflvhn flyqpkhdpt
      661 feplfpsett lnpslaqeaa klcgddhfcn fdvaatgsls tgtatrvahq lhqrrmqslq
      721 pvvscgwlap ppngqkegnr ylagstiyfh cdngyslaga etstcqadgt wssptpkcqp
      781 grsyavllgi ifgglavvaa valvyvllrr rkgnthvwga qp
//
LOCUS       NP_001185901            1035 aa            linear   PRI 20-NOV-2025
DEFINITION  NHS-like protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001185901
VERSION     NP_001185901.1
DBSOURCE    REFSEQ: accession NM_001198972.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1035)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1035)
  AUTHORS   Guo,Y., Tian,S., Li,H., Zuo,S., Yu,C. and Sun,C.
  TITLE     Transcription factor KLF9 inhibits the proliferation, invasion, and
            migration of pancreatic cancer cells by repressing KIAA1522
  JOURNAL   Asia Pac J Clin Oncol 20 (3), 423-432 (2024)
   PUBMED   38520660
  REMARK    GeneRIF: Transcription factor KLF9 inhibits the proliferation,
            invasion, and migration of pancreatic cancer cells by repressing
            KIAA1522.
REFERENCE   3  (residues 1 to 1035)
  AUTHORS   Palukuri,M.V., Patil,R.S. and Marcotte,E.M.
  TITLE     Molecular complex detection in protein interaction networks through
            reinforcement learning
  JOURNAL   BMC Bioinformatics 24 (1), 306 (2023)
   PUBMED   37532987
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1035)
  AUTHORS   Ou,M., Chu,Y., Zhang,Q., Zhao,H. and Song,Q.
  TITLE     HOXA cluster antisense RNA 2 elevates KIAA1522 expression through
            microRNA-520d-3p and insulin like growth factor 2 mRNA binding
            protein 3 to promote the growth of vascular smooth muscle cells in
            thoracic aortic aneurysm
  JOURNAL   ESC Heart Fail 9 (5), 2955-2966 (2022)
   PUBMED   35730141
  REMARK    GeneRIF: HOXA cluster antisense RNA 2 elevates KIAA1522 expression
            through microRNA-520d-3p and insulin like growth factor 2 mRNA
            binding protein 3 to promote the growth of vascular smooth muscle
            cells in thoracic aortic aneurysm.
REFERENCE   5  (residues 1 to 1035)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1035)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 1035)
  AUTHORS   Wang,B., Jing,T., Jin,W., Chen,J., Wu,C., Wang,M. and Liu,Y.
  TITLE     KIAA1522 potentiates TNFalpha-NFkappaB signaling to antagonize
            platinum-based chemotherapy in lung adenocarcinoma
  JOURNAL   J Exp Clin Cancer Res 39 (1), 170 (2020)
   PUBMED   32854746
  REMARK    GeneRIF: KIAA1522 potentiates TNFalpha-NFkappaB signaling to
            antagonize platinum-based chemotherapy in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1035)
  AUTHORS   Li,Y., Wang,Y., Fan,H., Zhang,Z. and Li,N.
  TITLE     miR-125b-5p inhibits breast cancer cell proliferation, migration
            and invasion by targeting KIAA1522
  JOURNAL   Biochem Biophys Res Commun 504 (1), 277-282 (2018)
   PUBMED   30177391
  REMARK    GeneRIF: miR-125b-5p functions as a tumor suppressor and regulates
            breast cancer cell progression through targeting KIAA1522
REFERENCE   9  (residues 1 to 1035)
  AUTHORS   Liu,Y.Z., Yang,H., Cao,J., Jiang,Y.Y., Hao,J.J., Xu,X., Cai,Y. and
            Wang,M.R.
  TITLE     KIAA1522 is a novel prognostic biomarker in patients with non-small
            cell lung cancer
  JOURNAL   Sci Rep 6, 24786 (2016)
   PUBMED   27098511
  REMARK    GeneRIF: high expression of KIAA1522 can be used as an independent
            biomarker for predication of poor survival and platinum-resistance
            of NSCLC patients, and aberrant KIAA1522 might be a new target for
            the therapy of the disease.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1035)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2, AK298965.1, AB040955.1 and BC004879.1.
            
            Transcript Variant: This variant (2) has an alternate 5' exon
            compared to variant 1. The resulting isoform (2) has a shorter and
            distinct N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB040955.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1035
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..1035
                     /product="NHS-like protein 3 isoform 2"
                     /note="NHS-like protein 3"
                     /calculated_mol_wt=106964
     Region          23..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Region          76..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Region          133..162
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            320
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Region          332..869
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            545
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2A7S8; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Region          <724..1000
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            858
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            862
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Region          885..1035
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            929
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9P206.2)"
     Site            979
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P206.2)"
     CDS             1..1035
                     /gene="NHSL3"
                     /gene_synonym="KIAA1522"
                     /coded_by="NM_001198972.2:144..3251"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55588.1"
                     /db_xref="GeneID:57648"
                     /db_xref="HGNC:HGNC:29301"
ORIGIN      
        1 mvvfvgrrlp allglfkkkg sakaendkhl svgpgqgpgs avdehqdnvf fpsgrpphle
       61 elhtqaqegl rslqhqekqk lnkggwdhgd tqsiqssrtg pdednisfcs qttsyvaess
      121 taedalsirs emiqrkgstf rphdsfpksg ksgrrrrerr stvlglpqhv qkelglrner
      181 eapgtprapg ardavriptv dgrprgtsgm garvslqale aeaeagaete amlqrhidrv
      241 yrddtfvgrs tgtrappltr pmslavpglt ggagpaepls pamsispqat ylskliphav
      301 lpptvdvval grcslrtlsr cslhsaspas vrslgrfssv sspqprsrhp ssssdtwshs
      361 qssdtivsdg stlsskggse gqpesstasn svvpppqggs grgspsggst aeasdtlsir
      421 ssgqlsgrsv slrklkrppp pprrthslhq rglavpdgpl glppkperkq qpqlprpptt
      481 ggsegagaap cppnpanswv pglspggsrr pprspertls pssgyssqsg tptlppkgla
      541 gppaspgkaq ppkpervtsl rspgasvsss ltslcssssd papsdrsgpq iltplgdrfv
      601 ipphpkvpap fspppskprs pnpaapalaa pavvpgpvst tdaspqsppt pqttltplqe
      661 spviskdqsp ppspppsyhp pppptkkpev vveapsaset aeeplqdpnw ppppppapee
      721 qdlsmadfpp peeaffsvas pepagpsgsp elvsspaass ssatalqiqp pgspdpppap
      781 papapassap ghvaklpqke pvgcskgggp predvgaplv tpsllqmvrl rsvgapggap
      841 tpalgpsapq kplrralsgr aspvpapssg lhaavrlkac slaaseglss aqpngppeae
      901 prppqspast asfifskgsr klqlerpvsp etqadlqrnl vaelrsiseq rppqapkksp
      961 kapppvarkp svgvpppasp sypraeplta pptnglphtq drtkrelaen ggvlqlvgpe
     1021 ekmglpgsds qkela
//
LOCUS       NP_001092102             256 aa            linear   PRI 20-NOV-2025
DEFINITION  proline-rich AKT1 substrate 1 isoform b [Homo sapiens].
ACCESSION   NP_001092102
VERSION     NP_001092102.1
DBSOURCE    REFSEQ: accession NM_001098632.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Zhang,T., Wang,Y., Yu,H., Zhang,T., Guo,L., Xu,J., Wei,X., Wang,N.,
            Wu,Y., Wang,X. and Huang,L.
  TITLE     PGK1 represses autophagy-mediated cell death to promote the
            proliferation of liver cancer cells by phosphorylating PRAS40
  JOURNAL   Cell Death Dis 13 (1), 68 (2022)
   PUBMED   35058442
  REMARK    GeneRIF: PGK1 represses autophagy-mediated cell death to promote
            the proliferation of liver cancer cells by phosphorylating PRAS40.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Challa,S., Khulpateea,B.R., Nandu,T., Camacho,C.V., Ryu,K.W.,
            Chen,H., Peng,Y., Lea,J.S. and Kraus,W.L.
  TITLE     Ribosome ADP-ribosylation inhibits translation and maintains
            proteostasis in cancers
  JOURNAL   Cell 184 (17), 4531-4546 (2021)
   PUBMED   34314702
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Saito,A., Narasimhan,P., Hayashi,T., Okuno,S., Ferrand-Drake,M. and
            Chan,P.H.
  TITLE     Neuroprotective role of a proline-rich Akt substrate in apoptotic
            neuronal cell death after stroke: relationships with nerve growth
            factor
  JOURNAL   J Neurosci 24 (7), 1584-1593 (2004)
   PUBMED   14973226
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Kovacina,K.S., Park,G.Y., Bae,S.S., Guzzetta,A.W., Schaefer,E.,
            Birnbaum,M.J. and Roth,R.A.
  TITLE     Identification of a proline-rich Akt substrate as a 14-3-3 binding
            partner
  JOURNAL   J Biol Chem 278 (12), 10189-10194 (2003)
   PUBMED   12524439
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Park,I.H., Bachmann,R., Shirazi,H. and Chen,J.
  TITLE     Regulation of ribosomal S6 kinase 2 by mammalian target of
            rapamycin
  JOURNAL   J Biol Chem 277 (35), 31423-31429 (2002)
   PUBMED   12087098
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA005259.1, BC051844.2 and AC118341.2.
            
            Summary: AKT1S1 is a proline-rich substrate of AKT (MIM 164730)
            that binds 14-3-3 protein (see YWHAH, MIM 113508) when
            phosphorylated (Kovacina et al., 2003 [PubMed 12524439]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2, 3, 4,
            and 5 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051844.2, SRR1163655.372904.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..256
                     /product="proline-rich AKT1 substrate 1 isoform b"
                     /note="40 kDa proline-rich AKT substrate; AKT1 substrate 1
                     (proline rich)"
                     /calculated_mol_wt=27252
     Site            51
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          69..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D1F4; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          127..251
                     /region_name="PRAS"
                     /note="Proline-rich AKT1 substrate 1; pfam15798"
                     /db_xref="CDD:406279"
     Region          129..133
                     /region_name="TOS motif.
                     /evidence=ECO:0000269|PubMed:17510057"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:17517883,
                     ECO:0000269|PubMed:18372248, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          197..216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:18372248; propagated from
                     UniProtKB/Swiss-Prot (Q96B36.1)"
     Region          237..256
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB/AKT1 and DYRK3.
                     /evidence=ECO:0000269|PubMed:12524439,
                     ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q96B36.1)"
     CDS             1..256
                     /gene="AKT1S1"
                     /gene_synonym="Lobe; PRAS40"
                     /coded_by="NM_001098632.2:371..1141"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12784.1"
                     /db_xref="GeneID:84335"
                     /db_xref="HGNC:HGNC:28426"
                     /db_xref="MIM:610221"
ORIGIN      
        1 masgrpeelw eavvgaaerf rartgtelvl ltaapppppr pgpcayaahg rgalaeaarr
       61 clhdialahr aataarppap ppapqppspt pspprptlar edneededep tetetsgeql
      121 gisdngglfv mdedatlqdl ppfcesdpes tddgslseet pagpptcsvp pasalptqqy
      181 akslpvsvpv wgfkekrtea rssdeengpp sspdldriaa smralvlrea edtqvfgdlp
      241 rprlntsdfq klkrky
//
LOCUS       NP_055666                597 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 21 isoform 1 [Homo sapiens].
ACCESSION   NP_055666 XP_375685
VERSION     NP_055666.2
DBSOURCE    REFSEQ: accession NM_014851.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Chen,J., Song,W., Du,Y., Li,Z., Xuan,Z., Zhao,L., Chen,J., Zhao,Y.,
            Tuo,B., Zheng,S. and Song,P.
  TITLE     Inhibition of KLHL21 prevents cholangiocarcinoma progression
            through regulating cell proliferation and motility, arresting cell
            cycle and reducing Erk activation
  JOURNAL   Biochem Biophys Res Commun 499 (3), 433-440 (2018)
   PUBMED   29574153
  REMARK    GeneRIF: KLHL21 plays an essential role in the tumorigenesis and
            progression of cholangiocarcinoma.
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Shi,L., Zhang,W., Zou,F., Mei,L., Wu,G. and Teng,Y.
  TITLE     KLHL21, a novel gene that contributes to the progression of
            hepatocellular carcinoma
  JOURNAL   BMC Cancer 16 (1), 815 (2016)
   PUBMED   27769251
  REMARK    GeneRIF: Our study suggests that KLHL21 is a potential target for
            therapeutic intervention. Our findings also provide novel candidate
            genes on a genome-wide scale, which may have significant impact on
            the design and execution of effective therapy of HCC patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Mei,Z.Z., Chen,X.Y., Hu,S.W., Wang,N., Ou,X.L., Wang,J., Luo,H.H.,
            Liu,J. and Jiang,Y.
  TITLE     Kelch-like Protein 21 (KLHL21) Targets IkappaB Kinase-beta to
            Regulate Nuclear Factor kappa-Light Chain Enhancer of Activated B
            Cells (NF-kappaB) Signaling Negatively
  JOURNAL   J Biol Chem 291 (35), 18176-18189 (2016)
   PUBMED   27387502
  REMARK    GeneRIF: data clearly demonstrate that KLHL21 negatively regulates
            TNFalpha-activated NF-kappaB signaling via targeting IKKbeta,
            providing new insight into the mechanisms underlying NF-kappaB
            regulation in cells.
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Maerki,S., Olma,M.H., Staubli,T., Steigemann,P., Gerlich,D.W.,
            Quadroni,M., Sumara,I. and Peter,M.
  TITLE     The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone
            microtubules in anaphase and is required for cytokinesis
  JOURNAL   J Cell Biol 187 (6), 791-800 (2009)
   PUBMED   19995937
  REMARK    GeneRIF: KLHL21 localizes to midzone microtubules in anaphase &
            recruits aurora B & Cul3 to this region; results suggest that
            different Cul3 adaptors nonredundantly regulate aurora B during
            mitosis, possibly by ubiquitinating different pools of aurora B
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB007938.1 and BC064980.1.
            
            On or before Nov 26, 2004 this sequence version replaced
            XP_375685.1, NP_055666.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034039.1, AK075305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377658.8/ ENSP00000366886.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..597
                     /product="kelch-like protein 21 isoform 1"
                     /note="kelch-like protein 21"
                     /calculated_mol_wt=66487
     Region          14..138
                     /region_name="BTB_POZ_KLHL21"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 21 (KLHL21); cd18250"
                     /db_xref="CDD:349559"
     Region          49..547
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          133..232
                     /region_name="BACK_KLHL21"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 21 (KLHL21); cd18460"
                     /db_xref="CDD:350535"
     Region          287..335
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          326..368
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          336..382
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          372..409
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          384..422
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          412..451
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          423..470
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          472..512
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          502..548
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          513..560
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     Region          570..597
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJP4.4)"
     CDS             1..597
                     /gene="KLHL21"
                     /coded_by="NM_014851.4:53..1846"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30575.1"
                     /db_xref="GeneID:9903"
                     /db_xref="HGNC:HGNC:29041"
                     /db_xref="MIM:616262"
ORIGIN      
        1 merpaplavl pfsdpahals llrglsqlra erkfldvtle aaggrdfpah ravlaaaspy
       61 framfagqlr esraervrlh gvppdmlqll ldfsytgrva vsgdnaepll raadllqfpa
      121 vkeacgaflq qqldlancld mqdfaeafsc sglasaaqrf ilrhvgelga eqlerlplar
      181 llrylrddgl cvpkeeaayq lalrwvradp prraahwpql leavrlpfvr rfyllahvea
      241 eplvarcppc lrllreardf qaarydrhdr gpcprmrprp stglaeilvl vggcdqdcde
      301 lvtvdcynpq tgqwrylaef pdhlgggysi valgndiyvt ggsdgsrlyd cvwrynssvn
      361 ewaevapmlk areyhsssvl dgllyvvaad sterydhttd swealqpmty pmdncsttac
      421 rgrlyaigsl agketmvmqc ydpdtdlwsl vdcgqlppws fapktatlng lmyfvrddsa
      481 evdvynptrn ewdkipsmnq vhvggslavl ggklyvsggy dntfelsdvv eaydpetraw
      541 svvgrlpept fwhgsvsifr qfmpqtfsgg rgfeldsgsd dmdpgrprpp rdpdelh
//
LOCUS       NP_055258                180 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17B isoform 1 precursor [Homo sapiens].
ACCESSION   NP_055258
VERSION     NP_055258.1
DBSOURCE    REFSEQ: accession NM_014443.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Nyangiri,O.A., Mulindwa,J., Namulondo,J., Kitibwa,A., Nassuuna,J.,
            Elliott,A., Kimuda,M.P., Boobo,A., Nerima,B., Adriko,M.,
            Dunton,N.J., Madhan,G.K., Kristiansen,M., Casacuberta-Partal,M.,
            Noyes,H. and Matovu,E.
  CONSRTM   TrypanoGEN+ Research group of the H3Africa consortium
  TITLE     Variants of IL6, IL10, FCN2, RNASE3, IL12B and IL17B loci are
            associated with Schistosoma mansoni worm burden in the Albert Nile
            region of Uganda
  JOURNAL   PLoS Negl Trop Dis 17 (11), e0011796 (2023)
   PUBMED   38033168
  REMARK    GeneRIF: Variants of IL6, IL10, FCN2, RNASE3, IL12B and IL17B loci
            are associated with Schistosoma mansoni worm burden in the Albert
            Nile region of Uganda.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Husein-ElAhmed,H. and Steinhoff,M.
  TITLE     Potential role of INTERLEUKIN-17 in the pathogenesis of oral lichen
            planus: a systematic review with META-analysis
  JOURNAL   J Eur Acad Dermatol Venereol 36 (10), 1735-1744 (2022)
   PUBMED   35570406
  REMARK    GeneRIF: Potential role of INTERLEUKIN-17 in the pathogenesis of
            oral lichen planus: a systematic review with META-analysis.
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Bastid,J., Dejou,C., Docquier,A. and Bonnefoy,N.
  TITLE     The Emerging Role of the IL-17B/IL-17RB Pathway in Cancer
  JOURNAL   Front Immunol 11, 718 (2020)
   PUBMED   32373132
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Li,X., Bechara,R., Zhao,J., McGeachy,M.J. and Gaffen,S.L.
  TITLE     IL-17 receptor-based signaling and implications for disease
  JOURNAL   Nat Immunol 20 (12), 1594-1602 (2019)
   PUBMED   31745337
  REMARK    Review article
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Ramirez-Carrozzi,V., Ota,N., Sambandam,A., Wong,K., Hackney,J.,
            Martinez-Martin,N., Ouyang,W. and Pappu,R.
  TITLE     Cutting Edge: IL-17B Uses IL-17RA and IL-17RB to Induce Type 2
            Inflammation from Human Lymphocytes
  JOURNAL   J Immunol 202 (7), 1935-1941 (2019)
   PUBMED   30770417
  REMARK    GeneRIF: Our data reveal that analogous to other IL-17 family
            members, IL-17B has an inflammatory role in the human system.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Ryan,A.W., Thornton,J.M., Brophy,K., Daly,J.S., McLoughlin,R.M.,
            O'Morain,C., Abuzakouk,M., Kennedy,N.P., Stevens,F.M., Feighery,C.,
            Kelleher,D. and McManus,R.
  TITLE     Chromosome 5q candidate genes in coeliac disease: genetic variation
            at IL4, IL5, IL9, IL13, IL17B and NR3C1
  JOURNAL   Tissue Antigens 65 (2), 150-155 (2005)
   PUBMED   15713213
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Moore,E.E., Presnell,S., Garrigues,U., Guilbot,A., LeGuern,E.,
            Smith,D., Yao,L., Whitmore,T.E., Gilbert,T., Palmer,T.D.,
            Horner,P.J. and Kuestner,R.E.
  TITLE     Expression of IL-17B in neurons and evaluation of its possible role
            in the chromosome 5q-linked form of Charcot-Marie-Tooth disease
  JOURNAL   Neuromuscul Disord 12 (2), 141-150 (2002)
   PUBMED   11738356
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Shi,Y., Ullrich,S.J., Zhang,J., Connolly,K., Grzegorzewski,K.J.,
            Barber,M.C., Wang,W., Wathen,K., Hodge,V., Fisher,C.L., Olsen,H.,
            Ruben,S.M., Knyazev,I., Cho,Y.H., Kao,V., Wilkinson,K.A.,
            Carrell,J.A. and Ebner,R.
  TITLE     A novel cytokine receptor-ligand pair. Identification, molecular
            characterization, and in vivo immunomodulatory activity
  JOURNAL   J Biol Chem 275 (25), 19167-19176 (2000)
   PUBMED   10749887
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Li,H., Chen,J., Huang,A., Stinson,J., Heldens,S., Foster,J.,
            Dowd,P., Gurney,A.L. and Wood,W.I.
  TITLE     Cloning and characterization of IL-17B and IL-17C, two new members
            of the IL-17 cytokine family
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 773-778 (2000)
   PUBMED   10639155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC131025.1.
            
            Summary: The protein encoded by this gene is a T cell-derived
            cytokine that shares sequence similarity with IL17. This cytokine
            was reported to stimulate the release of TNF alpha (TNF) and IL1
            beta (IL1B) from a monocytic cell line. Immunohistochemical
            analysis of several nerve tissues indicated that this cytokine is
            primarily localized to neuronal cell bodies. Alternative splicing
            results in multiple splice variants. [provided by RefSeq, Dec
            2015].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF212311.1, AF152098.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2149178,
                                           SAMEA2158188 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261796.4/ ENSP00000261796.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..180
                     /product="interleukin-17B isoform 1 precursor"
                     /note="interleukin 20; cytokine-like protein ZCYTO7;
                     neuronal interleukin-17 related factor; interleukin-17
                     beta"
                     /calculated_mol_wt=18154
     sig_peptide     1..20
                     /calculated_mol_wt=2301
     mat_peptide     21..180
                     /product="interleukin-17B isoform 1"
                     /calculated_mol_wt=18154
     Region          96..179
                     /region_name="IL17"
                     /note="Interleukin-17; pfam06083"
                     /db_xref="CDD:461823"
     CDS             1..180
                     /gene="IL17B"
                     /gene_synonym="IL-17B; IL-20; NIRF; ZCYTO7"
                     /coded_by="NM_014443.3:68..610"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4297.1"
                     /db_xref="GeneID:27190"
                     /db_xref="HGNC:HGNC:5982"
                     /db_xref="MIM:604627"
ORIGIN      
        1 mdwphnllfl ltisiflglg qprspkskrk gqgrpgplap gphqvpldlv srmkpyarme
       61 eyernieemv aqlrnssela qrkcevnlql wmsnkrslsp wgysinhdps ripvdlpear
      121 clclgcvnpf tmqedrsmvs vpvfsqvpvr rrlcpppprt gpcrqravme tiavgctcif
//
LOCUS       NP_001351799            1188 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosome and spindle pole-associated protein 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001351799
VERSION     NP_001351799.1
DBSOURCE    REFSEQ: accession NM_001364870.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1188)
  AUTHORS   van den Berg,C.M., Volkov,V.A., Schnorrenberg,S., Huang,Z.,
            Stecker,K.E., Grigoriev,I., Gilani,S., Frikstad,K.M., Patzke,S.,
            Zimmermann,T., Dogterom,M. and Akhmanova,A.
  TITLE     CSPP1 stabilizes growing microtubule ends and damaged lattices from
            the luminal side
  JOURNAL   J Cell Biol 222 (4) (2023)
   PUBMED   36752787
  REMARK    GeneRIF: CSPP1 stabilizes growing microtubule ends and damaged
            lattices from the luminal side.
REFERENCE   2  (residues 1 to 1188)
  AUTHORS   Odabasi,E., Conkar,D., Deretic,J., Batman,U., Frikstad,K.M.,
            Patzke,S. and Firat-Karalar,E.N.
  TITLE     CCDC66 regulates primary cilium length and signaling via
            interactions with transition zone and axonemal proteins
  JOURNAL   J Cell Sci 136 (3) (2023)
   PUBMED   36606424
REFERENCE   3  (residues 1 to 1188)
  AUTHORS   Zhang,L., Yang,S.T., Wang,C., Zhang,L.C., Zhang,X., Li,F.C.,
            Wang,S.Y. and Ma,K.
  TITLE     Circle RNA circCSPP1 promotes human osteosarcoma cell proliferation
            and increases glucose metabolism by suppressing miR-200c maturation
  JOURNAL   Hum Exp Toxicol 41, 9603271221097364 (2022)
   PUBMED   35713481
  REMARK    GeneRIF: Circle RNA circCSPP1 promotes human osteosarcoma cell
            proliferation and increases glucose metabolism by suppressing
            miR-200c maturation.
REFERENCE   4  (residues 1 to 1188)
  AUTHORS   Latour,B.L., Van De Weghe,J.C., Rusterholz,T.D., Letteboer,S.J.,
            Gomez,A., Shaheen,R., Gesemann,M., Karamzade,A., Asadollahi,M.,
            Barroso-Gil,M., Chitre,M., Grout,M.E., van Reeuwijk,J., van
            Beersum,S.E., Miller,C.V., Dempsey,J.C., Morsy,H., Bamshad,M.J.,
            Nickerson,D.A., Neuhauss,S.C., Boldt,K., Ueffing,M.,
            Keramatipour,M., Sayer,J.A., Alkuraya,F.S., Bachmann-Gagescu,R.,
            Roepman,R. and Doherty,D.
  CONSRTM   University of Washington Center for Mendelian Genomics; Genomics
            England Research Consortium
  TITLE     Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes
            Joubert syndrome
  JOURNAL   J Clin Invest 130 (8), 4423-4439 (2020)
   PUBMED   32453716
REFERENCE   5  (residues 1 to 1188)
  AUTHORS   Xue,Y.F., Li,M., Li,W., Lin,Q., Yu,B.X., Zhu,Q.B. and Chen,H.J.
  TITLE     Roles of circ-CSPP1 on the proliferation and metastasis of glioma
            cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (10), 5519-5525 (2020)
   PUBMED   32495924
  REMARK    GeneRIF: Roles of circ-CSPP1 on the proliferation and metastasis of
            glioma cancer.
REFERENCE   6  (residues 1 to 1188)
  AUTHORS   Patzke,S., Redick,S., Warsame,A., Murga-Zamalloa,C.A., Khanna,H.,
            Doxsey,S. and Stokke,T.
  TITLE     CSPP is a ciliary protein interacting with Nephrocystin 8 and
            required for cilia formation
  JOURNAL   Mol Biol Cell 21 (15), 2555-2567 (2010)
   PUBMED   20519441
  REMARK    GeneRIF: CSPP isoforms require their common C-terminal domain to
            interact with Nephrocystin 8 (NPHP8/RPGRIP1L) and to form a ternary
            complex with NPHP8 and NPHP4.
REFERENCE   7  (residues 1 to 1188)
  AUTHORS   Asiedu,M., Wu,D., Matsumura,F. and Wei,Q.
  TITLE     Centrosome/spindle pole-associated protein regulates cytokinesis
            via promoting the recruitment of MyoGEF to the central spindle
  JOURNAL   Mol Biol Cell 20 (5), 1428-1440 (2009)
   PUBMED   19129481
  REMARK    GeneRIF: CSPP interacts with and recruits MyoGEF to the central
            spindle, where MyoGEF contributes to the spatiotemporal regulation
            of cytokinesis.
REFERENCE   8  (residues 1 to 1188)
  AUTHORS   Patzke,S., Stokke,T. and Aasheim,H.C.
  TITLE     CSPP and CSPP-L associate with centrosomes and microtubules and
            differently affect microtubule organization
  JOURNAL   J Cell Physiol 209 (1), 199-210 (2006)
   PUBMED   16826565
  REMARK    GeneRIF: Taken together, CSPP and CSPP-L interact with centrosomes
            and microtubules and can differently affect microtubule
            organization.
REFERENCE   9  (residues 1 to 1188)
  AUTHORS   Patzke,S., Hauge,H., Sioud,M., Finne,E.F., Sivertsen,E.A.,
            Delabie,J., Stokke,T. and Aasheim,H.C.
  TITLE     Identification of a novel centrosome/microtubule-associated
            coiled-coil protein involved in cell-cycle progression and spindle
            organization
  JOURNAL   Oncogene 24 (7), 1159-1173 (2005)
   PUBMED   15580290
  REMARK    GeneRIF: Novel centrosome/microtubule-associated coiled-coil
            protein (CSPP)is associated with centrosomes and microtubules and
            may play a role in the regulation of G(1)/S-phase progression and
            spindle assembly [CSPP].
REFERENCE   10 (residues 1 to 1188)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC109335.5 and AC087359.13.
            
            Summary: This gene encodes a centrosome and spindle pole associated
            protein. The encoded protein plays a role in cell-cycle progression
            and spindle organization, regulates cytokinesis, interacts with
            Nephrocystin 8 and is required for cilia formation. Mutations in
            this gene result in primary cilia abnormalities and classical
            Joubert syndrome. Alternatively spliced transcript variants
            encoding distinct isoforms have been found for this gene. [provided
            by RefSeq, Apr 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.127496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q13.1-q13.2"
     Protein         1..1188
                     /product="centrosome and spindle pole-associated protein 1
                     isoform 7"
                     /calculated_mol_wt=137862
     CDS             1..1188
                     /gene="CSPP1"
                     /gene_synonym="CSPP; CSPP-L; JBTS21"
                     /coded_by="NM_001364870.1:8..3574"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS94304.1"
                     /db_xref="GeneID:79848"
                     /db_xref="HGNC:HGNC:26193"
                     /db_xref="MIM:611654"
ORIGIN      
        1 mlfplqvaav tssvrddple hcvsprtrar speickmadn ldefieeqka rlaedkaele
       61 sdppymemkg klsaklsens kilismaken ippnsqqtrg slgidyglsl plgedyerkk
      121 hklkeelrqd yrryltqerl klernkeynq flrgkeesse kfrqvekste pksqrnkkpi
      181 gqvkpdltsq iqtscenseg prkdvltpse ayeellnqrr leedryrqld deielrnrri
      241 ikkaneevgi snlkhqrfas kagipdrrfh rfnedrvfdr ryhrpdqdpe vseemderfr
      301 yesdfdrrls rvytndsapd netsksanqd tcspfagmlf ggedreliqr rkekyrlell
      361 eqmaeqqrnk rrekdlelrv aasgaqdpek spdrlkqfsv aprhfeemip perpriafqt
      421 plpplsapsv ppipsvhpvp sqnedlrsgl ssalgemvsp riaplppppl lpplatnyrt
      481 pyddayyfyg srntfdpsla yygsgmmgvq paayvsapvt hqlaqpvvnt vgqnelkits
      541 dqvinsglif edkpkpskqs lqsyqealqq qirereerrk kereekeeye akleaemrty
      601 npwgkgggga plrdakgnli tdlnrmhrqn idayhnpdar tyedkravvs ldpnlatsna
      661 enledaanks sghmqtqssp fargnvfgep ptelqikqqe lyknflrfqi eekkqreeae
      721 rerlriaeek eerrlaeqra riqqeyeeeq ekkrekeeeq rlkneehirl aeerqkeaer
      781 kkkeeeekyn lqlqhycerd nligeetkhm rqpspivpal qnkiasklqr ppsvdsiirs
      841 fihessmsra qsppvparkn qlraeeekkn vimelsemrk qlrseerrlq erllhmdsdd
      901 eipirkkern pmdifdmarh rlqapvrrqs pkgldaatfq nvhdfnelkd rdsetrvdlk
      961 fmyldpprdh htleiqqqal lreqqkrlnr ikmqegakvd ldaipsakvr eqrmprddts
     1021 dflknslles dsafigayge typaieddvl pppsqlpsar errrnkwkgl didssrpnva
     1081 pdglslksis svnvdelrvr neermrrlne fhnkpintdd esslvdpddi mkhigddgsn
     1141 svatepwlrp gtsetlkrfm aeqlnqeqqq ipgkpgtftw qglstahg
//
LOCUS       NP_001117                456 aa            linear   PRI 20-NOV-2025
DEFINITION  adenylosuccinate synthetase isozyme 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001117
VERSION     NP_001117.2
DBSOURCE    REFSEQ: accession NM_001126.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Baresova,V., Krijt,M., Skopova,V., Souckova,O., Kmoch,S. and
            Zikanova,M.
  TITLE     CRISPR-Cas9 induced mutations along de novo purine synthesis in
            HeLa cells result in accumulation of individual enzyme substrates
            and affect purinosome formation
  JOURNAL   Mol Genet Metab 119 (3), 270-277 (2016)
   PUBMED   27590927
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Stepinski,J., Pawelczyk,T., Bizon,D. and Angielski,S.
  TITLE     Purine nucleotide cycle in rat renal cortex and medulla under
            conditions that mimic normal and low oxygen supply
  JOURNAL   Kidney Int 50 (4), 1195-1201 (1996)
   PUBMED   8887278
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Powell,S.M., Zalkin,H. and Dixon,J.E.
  TITLE     Cloning and characterization of the cDNA encoding human
            adenylosuccinate synthetase
  JOURNAL   FEBS Lett 303 (1), 4-10 (1992)
   PUBMED   1592113
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Zalkin,H. and Dixon,J.E.
  TITLE     De novo purine nucleotide biosynthesis
  JOURNAL   Prog Nucleic Acid Res Mol Biol 42, 259-287 (1992)
   PUBMED   1574589
  REMARK    Review article
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Lai,L.W., Hart,I.M. and Patterson,D.
  TITLE     A gene correcting the defect in the CHO mutant Ade -H, deficient in
            a branch point enzyme (adenylosuccinate synthetase) of de novo
            purine biosynthesis, is located on the long arm of chromosome 1
  JOURNAL   Genomics 9 (2), 322-328 (1991)
   PUBMED   2004783
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Ogawa,H., Shiraki,H., Matsuda,Y. and Nakagawa,H.
  TITLE     Interaction of adenylosuccinate synthetase with F-actin
  JOURNAL   Eur J Biochem 85 (2), 331-337 (1978)
   PUBMED   648524
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Van der Weyden,M.B. and Kelly,W.N.
  TITLE     Human adenylosuccinate synthetase. Partial purification, kinetic
            and regulatory properties of the enzyme from placenta
  JOURNAL   J Biol Chem 249 (22), 7282-7289 (1974)
   PUBMED   4436310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012356.1 and AL645465.15.
            
            On Sep 11, 2003 this sequence version replaced NP_001117.1.
            
            Summary: This gene encodes the enzyme adenylosuccinate synthetase
            which catalyzes the first committed step in the conversion of
            inosine monophosphate to adenosine monophosphate. A pseudogene of
            this gene is found on chromosome 17.[provided by RefSeq, Nov 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012356.1, GQ900992.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366535.4/ ENSP00000355493.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..456
                     /product="adenylosuccinate synthetase isozyme 2 isoform 1"
                     /EC_number="6.3.4.4"
                     /note="adenylosuccinate synthetase, acidic isozyme;
                     IMP--aspartate ligase 2; adenylosuccinate synthetase
                     (Ade(-)H-complementing); L-type adenylosuccinate
                     synthetase; adenylosuccinate synthetase, liver isozyme;
                     AMPSase 2; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=49966
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30520.3)"
     Region          32..453
                     /region_name="Adenylsucc_synt"
                     /note="Adenylosuccinate synthetase; pfam00709"
                     /db_xref="CDD:459912"
     CDS             1..456
                     /gene="ADSS2"
                     /gene_synonym="ADEH; ADSS; ADSS 2"
                     /coded_by="NM_001126.5:93..1463"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1624.1"
                     /db_xref="GeneID:159"
                     /db_xref="HGNC:HGNC:292"
                     /db_xref="MIM:103060"
ORIGIN      
        1 mafaetypaa sslpngdcgr prarpggnrv tvvlgaqwgd egkgkvvdll aqdadivcrc
       61 qggnnaghtv vvdsveydfh llpsgiinpn vtafigngvv ihlpglfeea eknvqkgkgl
      121 egwekrliis drahivfdfh qaadgiqeqq rqeqagknlg ttkkgigpvy sskaarsglr
      181 mcdlvsdfdg fserfkvlan qyksiyptle idiegelqkl kgymekikpm vrdgvyflye
      241 alhgppkkil veganaalld idfgtypfvt ssnctvggvc tglgmppqnv gevygvvkay
      301 ttrvgigafp teqdneigel lqtrgrefgv ttgrkrrcgw ldlvllkyah mingftalal
      361 tkldildmft eikvgvaykl dgeiiphipa nqevlnkvev qyktlpgwnt disnarafke
      421 lpvnaqnyvr fiedelqipv kwigvgksre smiqlf
//
LOCUS       NP_569732                329 aa            linear   PRI 20-NOV-2025
DEFINITION  tetraspanin-17 isoform b [Homo sapiens].
ACCESSION   NP_569732 XP_030295
VERSION     NP_569732.2
DBSOURCE    REFSEQ: accession NM_130465.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Guo,X.B., Zhang,X.C., Chen,P., Ma,L.M. and Shen,Z.Q.
  TITLE     miR-378a-3p inhibits cellular proliferation and migration in
            glioblastoma multiforme by targeting tetraspanin 17
  JOURNAL   Oncol Rep 42 (5), 1957-1971 (2019)
   PUBMED   31432186
  REMARK    GeneRIF: Data suggested that increased miR378a3p and decreased
            TSPAN17 levels were associated with improved survival in
            glioblastoma multiforme (GBM). Additionally, high levels of TSPAN17
            were linked to the poor prognosis of patients with GBM aged 5060,
            larger tumor sizes and an advanced World Health Organization stage.
            TSPAN17 was identified and confirmed as a direct target of miR378a.
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Reyat,J.S., Chimen,M., Noy,P.J., Szyroka,J., Rainger,G.E. and
            Tomlinson,M.G.
  TITLE     ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate
            VE-Cadherin Expression and Promote T Lymphocyte Transmigration
  JOURNAL   J Immunol 199 (2), 666-676 (2017)
   PUBMED   28600292
  REMARK    GeneRIF: Endothelial Tspan5- and Tspan17-ADAM10 complexes may
            regulate inflammation by maintaining normal VE-cadherin expression
            and promoting T lymphocyte transmigration.
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Dornier,E., Coumailleau,F., Ottavi,J.F., Moretti,J., Boucheix,C.,
            Mauduit,P., Schweisguth,F. and Rubinstein,E.
  TITLE     TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and
            promote Notch activation in flies and mammals
  JOURNAL   J Cell Biol 199 (3), 481-496 (2012)
   PUBMED   23091066
  REMARK    Erratum:[J Cell Biol. 2016 May 23;213(4):495-6. doi:
            10.1083/jcb.20120113304262016c. PMID: 27185832]
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091934.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 22, 2004 this sequence version replaced NP_569732.1.
            
            Summary: This gene encodes a member of the transmembrane 4
            superfamily. It is characterized by four tetraspanin transmembrane
            segments. The function of this gene has not yet been determined.
            [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (b) that is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067105.1, SRR3476690.251237.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000508164.6/ ENSP00000422053.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..329
                     /product="tetraspanin-17 isoform b"
                     /EC_number="3.6.5.3"
                     /note="F-box only protein 23, transmembrane 4 superfamily
                     member 17; tetraspan protein SB134"
                     /calculated_mol_wt=36611
     mat_peptide     1..270
                     /product="Tetraspanin-17. /id=PRO_0000219265"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
                     /calculated_mol_wt=30264
     Region          18..260
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     Region          115..235
                     /region_name="TM4SF9_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF9_like subfamily.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03159"
                     /db_xref="CDD:239412"
     Site            order(116,121,125,127..128,131,145,148..149,152..153)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239412"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96FV3.2)"
     Site            235..255
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96FV3.2)"
     CDS             1..329
                     /gene="TSPAN17"
                     /gene_synonym="FBX23; FBXO23; TM4SF17"
                     /coded_by="NM_130465.5:133..1122"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54952.1"
                     /db_xref="GeneID:26262"
                     /db_xref="HGNC:HGNC:13594"
                     /db_xref="MIM:620446"
ORIGIN      
        1 mpgkhqhfqe pevgccgkyf lfgfnivfwv lgalflaigl wawgekgvls nisaltdlgg
       61 ldpvwlfvvv ggvmsvlgfa gcigalrent fllkffsvfl glifflelat gilafvfkdw
      121 irdqlnlfin nnvkayrddi dlqnlidfaq eywsccgarg pndwnlniyf nctdlnpsre
      181 rcgvpfsccv rdpaedvlnt qcgydvrlkl eleqqgfiht kgcvgqfekw lqdnlivvag
      241 vfmgiallqi fgiclaqnlv sdikavkanw skwnddfenh wltptisevl stagpqqnsl
      301 tgapgpapps rhvffglggl ypeptfknw
//
LOCUS       NP_001008744             608 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosyl-DNA phosphodiesterase 1 isoform a [Homo sapiens].
ACCESSION   NP_001008744
VERSION     NP_001008744.1
DBSOURCE    REFSEQ: accession NM_001008744.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Geraud,M., Cristini,A., Salimbeni,S., Bery,N., Jouffret,V.,
            Russo,M., Ajello,A.C., Fernandez Martinez,L., Marinello,J.,
            Cordelier,P., Trouche,D., Favre,G., Nicolas,E., Capranico,G. and
            Sordet,O.
  TITLE     TDP1 mutation causing SCAN1 neurodegenerative syndrome hampers the
            repair of transcriptional DNA double-strand breaks
  JOURNAL   Cell Rep 43 (5), 114214 (2024)
   PUBMED   38761375
  REMARK    GeneRIF: TDP1 mutation causing SCAN1 neurodegenerative syndrome
            hampers the repair of transcriptional DNA double-strand breaks.
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Wei,X., Wang,Z., Hinson,C. and Yang,K.
  TITLE     Human TDP1, APE1 and TREX1 repair 3'-DNA-peptide/protein
            cross-links arising from abasic sites in vitro
  JOURNAL   Nucleic Acids Res 50 (7), 3638-3657 (2022)
   PUBMED   35349719
  REMARK    GeneRIF: Human TDP1, APE1 and TREX1 repair 3'-DNA-peptide/protein
            cross-links arising from abasic sites in vitro.
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Jakobsen,A.K., Yuusufi,S., Madsen,L.B., Meldgaard,P., Knudsen,B.R.
            and Stougaard,M.
  TITLE     TDP1 and TOP1 as targets in anticancer treatment of NSCLC: Activity
            and protein level in normal and tumor tissue from 150 NSCLC
            patients correlated to clinical data
  JOURNAL   Lung Cancer 164, 23-32 (2022)
   PUBMED   34974222
  REMARK    GeneRIF: TDP1 and TOP1 as targets in anticancer treatment of NSCLC:
            Activity and protein level in normal and tumor tissue from 150
            NSCLC patients correlated to clinical data.
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Dyrkheeva,N.S., Filimonov,A.S., Luzina,O.A., Zakharenko,A.L.,
            Ilina,E.S., Malakhova,A.A., Medvedev,S.P., Reynisson,J.,
            Volcho,K.P., Zakian,S.M., Salakhutdinov,N.F. and Lavrik,O.I.
  TITLE     New Hybrid Compounds Combining Fragments of Usnic Acid and
            Monoterpenoids for Effective Tyrosyl-DNA Phosphodiesterase 1
            Inhibition
  JOURNAL   Biomolecules 11 (7), 973 (2021)
   PUBMED   34356597
  REMARK    GeneRIF: New Hybrid Compounds Combining Fragments of Usnic Acid and
            Monoterpenoids for Effective Tyrosyl-DNA Phosphodiesterase 1
            Inhibition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 608)
  AUTHORS   Inamdar,K.V., Pouliot,J.J., Zhou,T., Lees-Miller,S.P.,
            Rasouli-Nia,A. and Povirk,L.F.
  TITLE     Conversion of phosphoglycolate to phosphate termini on 3' overhangs
            of DNA double strand breaks by the human tyrosyl-DNA
            phosphodiesterase hTdp1
  JOURNAL   J Biol Chem 277 (30), 27162-27168 (2002)
   PUBMED   12023295
  REMARK    GeneRIF: a role for hTdp1 in repair of free radical-mediated DNA
            double strand breaks bearing terminally blocked 3' overhangs.
REFERENCE   7  (residues 1 to 608)
  AUTHORS   Davies,D.R., Interthal,H., Champoux,J.J. and Hol,W.G.
  TITLE     The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1
  JOURNAL   Structure 10 (2), 237-248 (2002)
   PUBMED   11839309
  REMARK    GeneRIF: 1.69 A crystal structure of human tyrosyl-DNA
            phosphodiesterase
REFERENCE   8  (residues 1 to 608)
  AUTHORS   Interthal,H., Pouliot,J.J. and Champoux,J.J.
  TITLE     The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the
            phospholipase D superfamily
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 12009-12014 (2001)
   PUBMED   11572945
  REMARK    GeneRIF: Protein assay of expressed FLJ11090 shows that it encodes
            human tyrosyl-DNA phodphodiesterase (TDP1).
REFERENCE   9  (residues 1 to 608)
  AUTHORS   Pouliot,J.J., Yao,K.C., Robertson,C.A. and Nash,H.A.
  TITLE     Yeast gene for a Tyr-DNA phosphodiesterase that repairs
            topoisomerase I complexes
  JOURNAL   Science 286 (5439), 552-555 (1999)
   PUBMED   10521354
  REMARK    GeneRIF: Sequences nearly identical to FLJ11090 are highly
            homologous to the yeast TDP1 gene.  Tdp1 protein cleaves the
            linkage between a phosphotyrosyl group and the 3'-end of DNA, and
            has been shown to be involved in the repair of TOP1-induced DNA
            damage.
REFERENCE   10 (residues 1 to 608)
  AUTHORS   Salih,M.A.M., Takashima,H. and Boerkoel,C.F.
  TITLE     Spinocerebellar Ataxia with Axonal Neuropathy Type 1
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301284
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU849335.1, AK001952.1,
            BC015474.1, AL137128.4, AK023514.1 and BM661793.1.
            
            Summary: The protein encoded by this gene is involved in repairing
            stalled topoisomerase I-DNA complexes by catalyzing the hydrolysis
            of the phosphodiester bond between the tyrosine residue of
            topoisomerase I and the 3-prime phosphate of DNA. This protein may
            also remove glycolate from single-stranded DNA containing 3-prime
            phosphoglycolate, suggesting a role in repair of free-radical
            mediated DNA double-strand breaks. This gene is a member of the
            phospholipase D family and contains two PLD phosphodiesterase
            domains. Mutations in this gene are associated with the disease
            spinocerebellar ataxia with axonal neuropathy (SCAN1). [provided by
            RefSeq, Aug 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.149082.1,
                                           SRR1660809.125557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.11"
     Protein         1..608
                     /product="tyrosyl-DNA phosphodiesterase 1 isoform a"
                     /EC_number="3.1.4.-"
                     /note="tyr-DNA phosphodiesterase 1"
                     /calculated_mol_wt=68290
     Region          1..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUW8.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUW8.2)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NUW8.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9NUW8.2)"
     Region          166..582
                     /region_name="Tyr-DNA_phospho"
                     /note="Tyrosyl-DNA phosphodiesterase; pfam06087"
                     /db_xref="CDD:461824"
     Region          258..288
                     /region_name="PLD phosphodiesterase 1"
     Region          400..403
                     /region_name="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:12470949"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUW8.2)"
     Region          488..521
                     /region_name="PLD phosphodiesterase 2"
     Site            518
                     /site_type="other"
                     /note="Interaction with DNA.
                     /evidence=ECO:0000269|PubMed:12470949; propagated from
                     UniProtKB/Swiss-Prot (Q9NUW8.2)"
     CDS             1..608
                     /gene="TDP1"
                     /coded_by="NM_001008744.2:52..1878"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9888.1"
                     /db_xref="GeneID:55775"
                     /db_xref="HGNC:HGNC:18884"
                     /db_xref="MIM:607198"
ORIGIN      
        1 msqegdygrw tisssdesee ekpkpdkpst ssllcarqga aneprytcse aqkaahkrki
       61 spvkfsntds vlppkrqksg sqedlgwcls ssddelqpem pqkqaekvvi kkekdisapn
      121 dgtaqrtenh gapachrlke eedeyetsge gqdiwdmldk gnpfqfyltr vsgvkpkyns
      181 galhikdils plfgtlvssa qfnycfdvdw lvkqyppefr kkpillvhgd kreakahlha
      241 qakpyenisl cqakldiafg thhtkmmlll yeeglrvvih tsnlihadwh qktqgiwlsp
      301 lypriadgth ksgespthfk adlisylmay napslkewid vihkhdlset nvyligstpg
      361 rfqgsqkdnw ghfrlkkllk dhassmpnae swpvvgqfss vgslgadesk wlcsefkesm
      421 ltlgkesktp gkssvplyli ypsvenvrts legypaggsl pysiqtaekq nwlhsyfhkw
      481 saetsgrsna mphiktymrp spdfskiawf lvtsanlska awgalekngt qlmirsyelg
      541 vlflpsafgl dsfkvkqkff agsqepmatf pvpydlppel ygskdrpwiw nipyvkapdt
      601 hgnmwvps
//
LOCUS       NP_060534                203 aa            linear   PRI 20-NOV-2025
DEFINITION  akirin-2 [Homo sapiens].
ACCESSION   NP_060534
VERSION     NP_060534.1
DBSOURCE    REFSEQ: accession NM_018064.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 203)
  AUTHORS   de Almeida,M., Hinterndorfer,M., Brunner,H., Grishkovskaya,I.,
            Singh,K., Schleiffer,A., Jude,J., Deswal,S., Kalis,R., Vunjak,M.,
            Lendl,T., Imre,R., Roitinger,E., Neumann,T., Kandolf,S.,
            Schutzbier,M., Mechtler,K., Versteeg,G.A., Haselbach,D. and
            Zuber,J.
  TITLE     AKIRIN2 controls the nuclear import of proteasomes in vertebrates
  JOURNAL   Nature 599 (7885), 491-496 (2021)
   PUBMED   34711951
  REMARK    GeneRIF: AKIRIN2 controls the nuclear import of proteasomes in
            vertebrates.
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Krossa,S., Schmitt,A.D., Hattermann,K., Fritsch,J., Scheidig,A.J.,
            Mehdorn,H.M. and Held-Feindt,J.
  TITLE     Down regulation of Akirin-2 increases chemosensitivity in human
            glioblastomas more efficiently than Twist-1
  JOURNAL   Oncotarget 6 (25), 21029-21045 (2015)
   PUBMED   26036627
  REMARK    GeneRIF: Akirin-2 downregulation increases chemosensitivity in
            human glioblastomas more efficiently than Twist-1
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Armour,S.M., Bennett,E.J., Braun,C.R., Zhang,X.Y., McMahon,S.B.,
            Gygi,S.P., Harper,J.W. and Sinclair,D.A.
  TITLE     A high-confidence interaction map identifies SIRT1 as a mediator of
            acetylation of USP22 and the SAGA coactivator complex
  JOURNAL   Mol Cell Biol 33 (8), 1487-1502 (2013)
   PUBMED   23382074
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Macqueen,D.J. and Johnston,I.A.
  TITLE     Evolution of the multifaceted eukaryotic akirin gene family
  JOURNAL   BMC Evol Biol 9, 34 (2009)
   PUBMED   19200367
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 203)
  AUTHORS   Komiya,Y., Kurabe,N., Katagiri,K., Ogawa,M., Sugiyama,A.,
            Kawasaki,Y. and Tashiro,F.
  TITLE     A novel binding factor of 14-3-3beta functions as a transcriptional
            repressor and promotes anchorage-independent growth,
            tumorigenicity, and metastasis
  JOURNAL   J Biol Chem 283 (27), 18753-18764 (2008)
   PUBMED   18460465
REFERENCE   10 (residues 1 to 203)
  AUTHORS   Goto,A., Matsushita,K., Gesellchen,V., El Chamy,L.,
            Kuttenkeuler,D., Takeuchi,O., Hoffmann,J.A., Akira,S., Boutros,M.
            and Reichhart,J.M.
  TITLE     Akirins are highly conserved nuclear proteins required for
            NF-kappaB-dependent gene expression in drosophila and mice
  JOURNAL   Nat Immunol 9 (1), 97-104 (2008)
   PUBMED   18066067
  REMARK    Erratum:[Nat Immunol. 2008 Feb;9(2):216]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK001204.1, BC000764.2 and BM996262.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000764.2, AK222701.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257787.6/ ENSP00000257787.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q15"
     Protein         1..203
                     /product="akirin-2"
                     /note="fourteen-three-three beta interactant 1"
                     /calculated_mol_wt=22365
     Region          2..203
                     /region_name="akirin-2"
                     /note="cd22244"
                     /db_xref="CDD:412036"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q53H80.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q53H80.2)"
     Region          22..27
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:18066067"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53H80.2)"
     Site            22..27
                     /site_type="other"
                     /note="nuclear localization signal"
                     /db_xref="CDD:412036"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AXD8; propagated from
                     UniProtKB/Swiss-Prot (Q53H80.2)"
     Region          200..203
                     /region_name="SYVS motif.
                     /evidence=ECO:0000305|PubMed:34711951"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53H80.2)"
     CDS             1..203
                     /gene="AKIRIN2"
                     /gene_synonym="C6orf166; dJ486L4.2; FBI1"
                     /coded_by="NM_018064.4:550..1161"
                     /db_xref="CCDS:CCDS5013.1"
                     /db_xref="GeneID:55122"
                     /db_xref="HGNC:HGNC:21407"
                     /db_xref="MIM:615165"
ORIGIN      
        1 macgatlkrt ldfdpllspa spkrrrcapl saptsaaasp lsaaaataas fsaaaaspqk
       61 ylrmepspfg dvssrltteq ilynikqeyk rmqkrrhlet sfqqtdpcct sdaqphafll
      121 sgpaspgtss aassplkkeq plftlrqvgm icerllkere ekvreeyeei lntklaeqyd
      181 afvkfthdqi mrrygeqpas yvs
//
LOCUS       NP_003780                312 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor type 1-associated DEATH domain
            protein [Homo sapiens].
ACCESSION   NP_003780
VERSION     NP_003780.1
DBSOURCE    REFSEQ: accession NM_003789.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   van Loo,G. and Bertrand,M.J.M.
  TITLE     Death by TNF: a road to inflammation
  JOURNAL   Nat Rev Immunol 23 (5), 289-303 (2023)
   PUBMED   36380021
  REMARK    Review article
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Chen,Y., Gu,Y., Xiong,X., Zheng,Y., Liu,X., Wang,W. and Meng,G.
  TITLE     Roles of the adaptor protein tumor necrosis factor receptor type
            1-associated death domain protein (TRADD) in human diseases
  JOURNAL   Biomed Pharmacother 153, 113467 (2022)
   PUBMED   36076575
  REMARK    GeneRIF: Roles of the adaptor protein tumor necrosis factor
            receptor type 1-associated death domain protein (TRADD) in human
            diseases.
            Review article
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Feoktistova,M., Makarov,R., Yazdi,A.S. and Panayotova-Dimitrova,D.
  TITLE     RIPK1 and TRADD Regulate TNF-Induced Signaling and Ripoptosome
            Formation
  JOURNAL   Int J Mol Sci 22 (22), 12459 (2021)
   PUBMED   34830347
  REMARK    GeneRIF: RIPK1 and TRADD Regulate TNF-Induced Signaling and
            Ripoptosome Formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Zhang,N., Kisiswa,L., Ramanujan,A., Li,Z., Sim,E.W., Tian,X.,
            Yuan,W., Ibanez,C.F. and Lin,Z.
  TITLE     Structural basis of NF-kappaB signaling by the p75 neurotrophin
            receptor interaction with adaptor protein TRADD through their
            respective death domains
  JOURNAL   J Biol Chem 297 (2), 100916 (2021)
   PUBMED   34175311
  REMARK    GeneRIF: Structural basis of NF-kappaB signaling by the p75
            neurotrophin receptor interaction with adaptor protein TRADD
            through their respective death domains.
            Erratum:[J Biol Chem. 2022 Nov;298(11):102583. doi:
            10.1016/j.jbc.2022.102583. PMID: 36257251]
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Park,A. and Baichwal,V.R.
  TITLE     Systematic mutational analysis of the death domain of the tumor
            necrosis factor receptor 1-associated protein TRADD
  JOURNAL   J Biol Chem 271 (16), 9858-9862 (1996)
   PUBMED   8621670
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Hsu,H., Huang,J., Shu,H.B., Baichwal,V. and Goeddel,D.V.
  TITLE     TNF-dependent recruitment of the protein kinase RIP to the TNF
            receptor-1 signaling complex
  JOURNAL   Immunity 4 (4), 387-396 (1996)
   PUBMED   8612133
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Hsu,H., Shu,H.B., Pan,M.G. and Goeddel,D.V.
  TITLE     TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF
            receptor 1 signal transduction pathways
  JOURNAL   Cell 84 (2), 299-308 (1996)
   PUBMED   8565075
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hsu,H., Xiong,J. and Goeddel,D.V.
  TITLE     The TNF receptor 1-associated protein TRADD signals cell death and
            NF-kappa B activation
  JOURNAL   Cell 81 (4), 495-504 (1995)
   PUBMED   7758105
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Hasegawa,H.
  TITLE     [Nurses replies to expectations of the nursing profession]
  JOURNAL   Kango 27 (3), 66-80 (1975)
   PUBMED   1040062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA353575.1, BC004491.2 and
            CA426418.1.
            
            Summary: The protein encoded by this gene is a death domain
            containing adaptor molecule that interacts with TNFRSF1A/TNFR1 and
            mediates programmed cell death signaling and NF-kappaB activation.
            This protein binds adaptor protein TRAF2, reduces the recruitment
            of inhibitor-of-apoptosis proteins (IAPs) by TRAF2, and thus
            suppresses TRAF2 mediated apoptosis. This protein can also interact
            with receptor TNFRSF6/FAS and adaptor protein FADD/MORT1, and is
            involved in the Fas-induced cell death pathway. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.500582.1,
                                           SRR1163657.329789.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345057.9/ ENSP00000341268.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..312
                     /product="tumor necrosis factor receptor type 1-associated
                     DEATH domain protein"
                     /note="tumor necrosis factor receptor-1-associated
                     protein; TNFR1-associated death domain protein; tumor
                     necrosis factor receptor type 1 associated death domain
                     protein"
                     /calculated_mol_wt=34116
     Region          51..161
                     /region_name="TRADD_N"
                     /note="TRADD, N-terminal domain; pfam09034"
                     /db_xref="CDD:430379"
     Region          147..163
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:Q3U0V2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          170..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          215..304
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     Region          222..289
                     /region_name="Interaction with KRT14 and KRT18.
                     /evidence=ECO:0000269|PubMed:11684708"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Region          231..244
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250|UniProtKB:Q3U0V2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     Site            235
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:23955153,
                     ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:32766249,
                     ECO:0007744|PDB:6AC0; propagated from UniProtKB/Swiss-Prot
                     (Q15628.2)"
     Site            245
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:32766249;
                     propagated from UniProtKB/Swiss-Prot (Q15628.2)"
     CDS             1..312
                     /gene="TRADD"
                     /gene_synonym="Hs.89862"
                     /coded_by="NM_003789.4:81..1019"
                     /db_xref="CCDS:CCDS10829.1"
                     /db_xref="GeneID:8717"
                     /db_xref="HGNC:HGNC:12030"
                     /db_xref="MIM:603500"
ORIGIN      
        1 maagqnghee wvgsaylfve ssldkvvlsd ayahpqqkva vyralqaala esggspdvlq
       61 mlkihrsdpq livqlrfcgr qpcgrflray regalraalq rslaaalaqh svplqlelra
      121 gaerldalla deerclscil aqqpdrlrde elaeledalr nlkcgsgarg gdgevasapl
      181 qppvpslsev kpppppppaq tflfqgqpvv nrplslkdqq tfarsvglkw rkvgrslqrg
      241 cralrdpald slayeyereg lyeqafqllr rfvqaegrra tlqrlveale eneltslaed
      301 llgltdpngg la
//
LOCUS       NP_001794                 61 aa            linear   PRI 20-NOV-2025
DEFINITION  CAMPATH-1 antigen precursor [Homo sapiens].
ACCESSION   NP_001794
VERSION     NP_001794.2
DBSOURCE    REFSEQ: accession NM_001803.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 61)
  AUTHORS   de Vos-Hillebrand,L., Fietz,S., Hillebrand,P., Kulcsar,Z.,
            Diop,M.Y., Hollick,S., Maas,A.P., Strieth,S., Landsberg,J. and
            Dietrich,D.
  TITLE     CD52 mRNA expression predicts prognosis and response to immune
            checkpoint blockade in melanoma
  JOURNAL   Pigment Cell Melanoma Res 37 (2), 309-315 (2024)
   PUBMED   37975535
  REMARK    GeneRIF: CD52 mRNA expression predicts prognosis and response to
            immune checkpoint blockade in melanoma.
            Review article
REFERENCE   2  (residues 1 to 61)
  AUTHORS   Chiesa,R., Georgiadis,C., Syed,F., Zhan,H., Etuk,A., Gkazi,S.A.,
            Preece,R., Ottaviano,G., Braybrook,T., Chu,J., Kubat,A., Adams,S.,
            Thomas,R., Gilmour,K., O'Connor,D., Vora,A. and Qasim,W.
  CONSRTM   Base-Edited CAR T Group
  TITLE     Base-Edited CAR7 T Cells for Relapsed T-Cell Acute Lymphoblastic
            Leukemia
  JOURNAL   N Engl J Med 389 (10), 899-910 (2023)
   PUBMED   37314354
  REMARK    GeneRIF: Base-Edited CAR7 T Cells for Relapsed T-Cell Acute
            Lymphoblastic Leukemia.
REFERENCE   3  (residues 1 to 61)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 61)
  AUTHORS   Mao,R., Yang,F., Zhang,Y., Liu,H., Guo,P., Liu,Y. and Zhang,T.
  TITLE     High expression of CD52 in adipocytes: a potential therapeutic
            target for obesity with type 2 diabetes
  JOURNAL   Aging (Albany NY) 13 (8), 11043-11060 (2021)
   PUBMED   33705353
  REMARK    GeneRIF: High expression of CD52 in adipocytes: a potential
            therapeutic target for obesity with type 2 diabetes.
REFERENCE   5  (residues 1 to 61)
  AUTHORS   Bhamidipati,K., Silberstein,J.L., Chaichian,Y., Baker,M.C.,
            Lanz,T.V., Zia,A., Rasheed,Y.S., Cochran,J.R. and Robinson,W.H.
  TITLE     CD52 Is Elevated on B cells of SLE Patients and Regulates B Cell
            Function
  JOURNAL   Front Immunol 11, 626820 (2021)
   PUBMED   33658999
  REMARK    GeneRIF: CD52 Is Elevated on B cells of SLE Patients and Regulates
            B Cell Function.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 61)
  AUTHORS   Rowan,W.C., Hale,G., Tite,J.P. and Brett,S.J.
  TITLE     Cross-linking of the CAMPATH-1 antigen (CD52) triggers activation
            of normal human T lymphocytes
  JOURNAL   Int Immunol 7 (1), 69-77 (1995)
   PUBMED   7718516
REFERENCE   7  (residues 1 to 61)
  AUTHORS   Xia,M.Q., Hale,G., Lifely,M.R., Ferguson,M.A., Campbell,D.,
            Packman,L. and Waldmann,H.
  TITLE     Structure of the CAMPATH-1 antigen, a
            glycosylphosphatidylinositol-anchored glycoprotein which is an
            exceptionally good target for complement lysis
  JOURNAL   Biochem J 293 (Pt 3) (Pt 3), 633-640 (1993)
   PUBMED   7688956
REFERENCE   8  (residues 1 to 61)
  AUTHORS   Hale,G., Rye,P.D., Warford,A., Lauder,I. and Brito-Babapulle,A.
  TITLE     The glycosylphosphatidylinositol-anchored lymphocyte antigen CDw52
            is associated with the epididymal maturation of human spermatozoa
  JOURNAL   J Reprod Immunol 23 (2), 189-205 (1993)
   PUBMED   7685389
REFERENCE   9  (residues 1 to 61)
  AUTHORS   Valentin,H., Gelin,C., Coulombel,L., Zoccola,D., Morizet,J. and
            Bernard,A.
  TITLE     The distribution of the CDW52 molecule on blood cells and
            characterization of its involvement in T cell activation
  JOURNAL   Transplantation 54 (1), 97-104 (1992)
   PUBMED   1352921
REFERENCE   10 (residues 1 to 61)
  AUTHORS   Xia,M.Q., Tone,M., Packman,L., Hale,G. and Waldmann,H.
  TITLE     Characterization of the CAMPATH-1 (CDw52) antigen: biochemical
            analysis and cDNA cloning reveal an unusually small peptide
            backbone
  JOURNAL   Eur J Immunol 21 (7), 1677-1684 (1991)
   PUBMED   1711975
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI835519.1, BC000644.2 and X62466.1.
            
            On Jun 30, 2005 this sequence version replaced NP_001794.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.327494.1, BG535652.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374213.3/ ENSP00000363330.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..61
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..61
                     /product="CAMPATH-1 antigen precursor"
                     /note="CDW52 antigen (CAMPATH-1 antigen); CD52 antigen
                     (CAMPATH-1 antigen); cambridge pathology 1 antigen;
                     epididymal secretory protein E5; human epididymis-specific
                     protein 5; HEL-S-171mP; epididymis secretory sperm binding
                     protein Li 171mP"
                     /calculated_mol_wt=3866
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2766
     mat_peptide     25..36
                     /product="CAMPATH-1 antigen. /id=PRO_0000020904"
                     /note="propagated from UniProtKB/Swiss-Prot (P31358.1)"
                     /calculated_mol_wt=1208
     Site            27
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P31358.1)"
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31358.1)"
     Region          <43..61
                     /region_name="CD52"
                     /note="CAMPATH-1 antigen; pfam15116"
                     /db_xref="CDD:464513"
     CDS             1..61
                     /gene="CD52"
                     /gene_synonym="CDW52; EDDM5; HE5"
                     /coded_by="NM_001803.3:61..246"
                     /db_xref="CCDS:CCDS30647.1"
                     /db_xref="GeneID:1043"
                     /db_xref="HGNC:HGNC:1804"
                     /db_xref="MIM:114280"
ORIGIN      
        1 mkrflflllt isllvmvqiq tglsgqndts qtsspsassn isggiflffv anaiihlfcf
       61 s
//
LOCUS       NP_000801                462 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-5 precursor [Homo
            sapiens].
ACCESSION   NP_000801
VERSION     NP_000801.1
DBSOURCE    REFSEQ: accession NM_000810.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Chakraborty,A., Dey,S., Kumar,K., Dixit,A.B., Tripathi,M.,
            Sharma,M.C., Chandra,P.S. and Banerjee,J.
  TITLE     Novel variants in GABAA receptor subunits: A possible association
            with benzodiazepine resistance in patients with drug-resistant
            epilepsy
  JOURNAL   Epilepsy Res 189, 107056 (2023)
   PUBMED   36469977
  REMARK    GeneRIF: Novel variants in GABAA receptor subunits: A possible
            association with benzodiazepine resistance in patients with
            drug-resistant epilepsy.
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Arandelovic,J., Santrac,A., Batinic,B., Todorovic,L.,
            Stevanovic,V., Tiruveedhula,V.V.N.P.B., Sharmin,D., Rashid,F.,
            Stanojevic,B., Cook,J.M. and Savic,M.M.
  TITLE     Effects of alpha5 GABAA receptor modulation on social interaction,
            memory, and neuroinflammation in a mouse model of Alzheimer's
            disease
  JOURNAL   CNS Neurosci Ther 28 (11), 1767-1778 (2022)
   PUBMED   35822698
  REMARK    GeneRIF: Effects of alpha5 GABAA receptor modulation on social
            interaction, memory, and neuroinflammation in a mouse model of
            Alzheimer's disease.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Saha,S., Chatterjee,M., Dutta,N., Sinha,S. and Mukhopadhyay,K.
  TITLE     GABA Receptor SNPs and Elevated Plasma GABA Levels Affect the
            Severity of the Indian ASD Probands
  JOURNAL   J Mol Neurosci 72 (6), 1300-1312 (2022)
   PUBMED   35562522
  REMARK    GeneRIF: GABA Receptor SNPs and Elevated Plasma GABA Levels Affect
            the Severity of the Indian ASD Probands.
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Hou,S.J., Tsai,S.J., Kuo,P.H., Lin,W.Y., Liu,Y.L., Yang,A.C.,
            Lin,E. and Lan,T.H.
  TITLE     An association study in the Taiwan Biobank elicits the GABAA
            receptor genes GABRB3, GABRA5, and GABRG3 as candidate loci for
            sleep duration in the Taiwanese population
  JOURNAL   BMC Med Genomics 14 (1), 223 (2021)
   PUBMED   34530807
  REMARK    GeneRIF: An association study in the Taiwan Biobank elicits the
            GABAA receptor genes GABRB3, GABRA5, and GABRG3 as candidate loci
            for sleep duration in the Taiwanese population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Glatt,K., Glatt,H. and Lalande,M.
  TITLE     Structure and organization of GABRB3 and GABRA5
  JOURNAL   Genomics 41 (1), 63-69 (1997)
   PUBMED   9126483
  REMARK    Erratum:[1997 Aug 15;44(1):155]
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Knoll,J.H., Sinnett,D., Wagstaff,J., Glatt,K., Wilcox,A.S.,
            Whiting,P.M., Wingrove,P., Sikela,J.M. and Lalande,M.
  TITLE     FISH ordering of reference markers and of the gene for the alpha 5
            subunit of the gamma-aminobutyric acid receptor (GABRA5) within the
            Angelman and Prader-Willi syndrome chromosomal regions
  JOURNAL   Hum Mol Genet 2 (2), 183-189 (1993)
   PUBMED   8388764
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Glatt,K.A., Sinnett,D. and Lalande,M.
  TITLE     Dinucleotide repeat polymorphism at the GABAA receptor alpha 5
            (GABRA5) locus at chromosome 15q11-q13
  JOURNAL   Hum Mol Genet 1 (5), 348 (1992)
   PUBMED   1338907
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Wingrove,P., Hadingham,K., Wafford,K., Kemp,J.A., Ragan,C.I. and
            Whiting,P.
  TITLE     Cloning and expression of a cDNA encoding the human GABA-A receptor
            alpha 5 subunit
  JOURNAL   Biochem Soc Trans 20 (1), 18S (1992)
   PUBMED   1321750
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L08485.1, BC113422.1,
            BC011403.1 and R49008.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: GABA is the major inhibitory neurotransmitter in the
            mammalian brain where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. Chloride conductance of these
            channels can be modulated by agents such as benzodiazepines that
            bind to the GABA-A receptor. At least 16 distinct subunits of
            GABA-A receptors have been identified. Transcript variants
            utilizing three different alternative non-coding first exons have
            been described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.21771.1,
                                           SRR1660803.71543.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335625.10/ ENSP00000335592.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q12"
     Protein         1..462
                     /product="gamma-aminobutyric acid receptor subunit alpha-5
                     precursor"
                     /note="GABA(A) receptor subunit alpha-5;
                     gamma-aminobutyric acid type A receptor alpha5 subunit;
                     gamma-aminobutyric acid (GABA) A receptor, alpha 5; GABAAR
                     subunit alpha-5"
                     /calculated_mol_wt=48661
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3503
     mat_peptide     32..462
                     /product="gamma-aminobutyric acid receptor subunit
                     alpha-5"
                     /calculated_mol_wt=48661
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31644.1)"
     Region          58..256
                     /region_name="LGIC_ECD_GABAAR_A5"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-5 (GABAAR-A5 or GABRA5); cd19038"
                     /db_xref="CDD:349839"
     Site            order(71,99)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349839"
     Site            order(83,85..86,91..92,99,101..102,119,121..122,131..136,
                     139,141,143..144,150..152,154,164..166,194,256)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349839"
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30140029,
                     ECO:0007744|PDB:6A96; propagated from UniProtKB/Swiss-Prot
                     (P31644.1)"
     Region          173..187
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349839"
     Site            207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P31644.1)"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30140029,
                     ECO:0007744|PDB:6A96; propagated from UniProtKB/Swiss-Prot
                     (P31644.1)"
     Region          259..445
                     /region_name="LGIC_TM_GABAAR_alpha"
                     /note="transmembrane domain of alpha subunits of type-A
                     gamma-aminobutyric acid receptor (GABAAR); cd19052"
                     /db_xref="CDD:349854"
     Site            order(259,262..263,270..271,273..274,277,280..282,
                     285..288,290..292,294..295,298..299,305..306,308..309,
                     316..317,328,332,335,339,342..343,430)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349854"
     Region          259..282
                     /region_name="TM1 helix"
                     /note="TM1 helix [structural motif]"
                     /db_xref="CDD:349854"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31644.1)"
     Site            order(273,276..277,280,336,339..340,434)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349854"
     Region          286..310
                     /region_name="TM2 helix"
                     /note="TM2 helix [structural motif]"
                     /db_xref="CDD:349854"
     Site            287..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31644.1)"
     Region          318..344
                     /region_name="TM3 helix"
                     /note="TM3 helix [structural motif]"
                     /db_xref="CDD:349854"
     Site            319..340
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31644.1)"
     Region          377..412
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P31644.1)"
     Region          421..445
                     /region_name="TM4 helix"
                     /note="TM4 helix [structural motif]"
                     /db_xref="CDD:349854"
     Site            428..448
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P31644.1)"
     CDS             1..462
                     /gene="GABRA5"
                     /gene_synonym="DEE79; EIEE79"
                     /coded_by="NM_000810.4:190..1578"
                     /db_xref="CCDS:CCDS45194.1"
                     /db_xref="GeneID:2558"
                     /db_xref="HGNC:HGNC:4079"
                     /db_xref="MIM:137142"
ORIGIN      
        1 mdngmfsgfi miknlllfci smnlsshfgf sqmptssvkd etndnitift rildglldgy
       61 dnrlrpglge ritqvrtdiy vtsfgpvsdt emeytidvff rqswkderlr fkgpmqrlpl
      121 nnllaskiwt pdtffhngkk siahnmttpn kllrleddgt llytmrltis aecpmqledf
      181 pmdahacplk fgsyaypnse vvyvwtngst ksvvvaedgs rlnqyhlmgq tvgtenists
      241 tgeytimtah fhlkrkigyf viqtylpcim tvilsqvsfw lnresvpart vfgvttvltm
      301 ttlsisarns lpkvayatam dwfiavcyaf vfsaliefat vnyftkrgwa wdgkkaleaa
      361 kikkkrevil nkstnafttg kmshppnipk eqtpagtsnt tsvsvkpsee ktseskktyn
      421 siskidkmsr ivfpvlfgtf nlvywatyln repvikgaas pk
//
LOCUS       NP_001354672             515 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform f precursor [Homo sapiens].
ACCESSION   NP_001354672
VERSION     NP_001354672.1
DBSOURCE    REFSEQ: accession NM_001367743.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (27), as well as variant 28,
            encodes isoform f.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1660803.32065.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..515
                     /product="rab5 GDP/GTP exchange factor isoform f
                     precursor"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=55489
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2955
     Region          182..244
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          294..394
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..515
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367743.1:338..1885"
                     /note="isoform f precursor is encoded by transcript
                     variant 27"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mwllrqpcla gfllqvlegr vpqsqaeads gglgaggagl allpwlecng aistycnlcf
       61 lgssdppasa sqvarttevc hhaqlqreee eafassqssq gaqsltfskf eekktnektr
      121 kvttvkkffs assrvgskke iqeakapsps inrqtsietd rvskefiefl ktfhktgqei
      181 ykqtklfleg mhykrdlsie eqsecaqdfy hnvaermqtr gkvppervek imdqiekyim
      241 trlykyvfcp ettddekkdl aiqkriralr wvtpqmlcvp vnedipevsd mvvkaitdii
      301 emdskrvprd klacitkcsk hifnaikitk nepasaddfl ptliyivlkg npprlqsniq
      361 yitrfcnpsr lmtgedgyyf tnlccavafi ekldaqslnl sqedfdryms gqtsprkqea
      421 eswspdaclg vkqmyknldl lsqlnerqer imneakklek dlidwtdgia revqdiveky
      481 pleikppnqp laaidsenve ndklppplqp qvyag
//
LOCUS       NP_006580                668 aa            linear   PRI 20-NOV-2025
DEFINITION  protein ENTREP3 isoform a [Homo sapiens].
ACCESSION   NP_006580
VERSION     NP_006580.2
DBSOURCE    REFSEQ: accession NM_006589.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 668)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 668)
  AUTHORS   Ma,Y., Feng,H., Wang,Y., Hu,L., Su,X., Li,N. and Li,X.
  TITLE     COTE-1 promotes the proliferation and invasion of small cell lung
            cancer by regulating autophagy activity via the AMPK/mTOR signaling
            pathway
  JOURNAL   Mol Cell Probes 71, 101918 (2023)
   PUBMED   37454876
  REMARK    GeneRIF: COTE-1 promotes the proliferation and invasion of small
            cell lung cancer by regulating autophagy activity via the AMPK/mTOR
            signaling pathway.
REFERENCE   3  (residues 1 to 668)
  AUTHORS   Zhang,H., Chen,S., Xu,S. and Li,X.
  TITLE     COTE1 Facilitates Intrahepatic Cholangiocarcinoma Progression via
            Beclin1-Dependent Autophagy Inhibition
  JOURNAL   Biomed Res Int 2023, 5491682 (2023)
   PUBMED   37780485
  REMARK    GeneRIF: COTE1 Facilitates Intrahepatic Cholangiocarcinoma
            Progression via Beclin1-Dependent Autophagy Inhibition.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 668)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 668)
  AUTHORS   Wu,C.L., Tan,Q.X., Liu,D., Jiang,J.E., Lu,T., Huang,Z.M. and
            Su,Y.J.
  TITLE     High FAM189B Expression and Its Prognostic Value in Patients with
            Gastric Cancer
  JOURNAL   Biomed Res Int 2021, 8875971 (2021)
   PUBMED   34124264
  REMARK    GeneRIF: High FAM189B Expression and Its Prognostic Value in
            Patients with Gastric Cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 668)
  AUTHORS   Zhang,H., Tian,Y., Shen,J., Wang,Y., Xu,Y., Wang,Y., Han,Z. and
            Li,X.
  TITLE     Upregulation of the putative oncogene COTE1 contributes to human
            hepatocarcinogenesis through modulation of WWOX signaling
  JOURNAL   Int J Oncol 45 (2), 719-731 (2014)
   PUBMED   24899407
  REMARK    GeneRIF: our findings suggest that the cytoplasmic protein COTE1
            contributes to hepatocellular carcinoma tumorigenesis by regulating
            cell proliferation through the modulation of WWOX signaling
REFERENCE   7  (residues 1 to 668)
  AUTHORS   Zhang,H., Huang,C.J., Tian,Y., Wang,Y.P., Han,Z.G. and Li,X.C.
  TITLE     Ectopic overexpression of COTE1 promotes cellular invasion of
            hepatocellular carcinoma
  JOURNAL   Asian Pac J Cancer Prev 13 (11), 5799-5804 (2012)
   PUBMED   23317259
  REMARK    GeneRIF: Overexpression of COTE1 promotes cellular invasion of
            hepatocellular carcinoma.
REFERENCE   8  (residues 1 to 668)
  AUTHORS   Kallin,A., Johannessen,L.E., Cani,P.D., Marbehant,C.Y.,
            Essaghir,A., Foufelle,F., Ferre,P., Heldin,C.H., Delzenne,N.M. and
            Demoulin,J.B.
  TITLE     SREBP-1 regulates the expression of heme oxygenase 1 and the
            phosphatidylinositol-3 kinase regulatory subunit p55 gamma
  JOURNAL   J Lipid Res 48 (7), 1628-1636 (2007)
   PUBMED   17452746
REFERENCE   9  (residues 1 to 668)
  AUTHORS   Ludes-Meyers,J.H., Kil,H., Bednarek,A.K., Drake,J., Bedford,M.T.
            and Aldaz,C.M.
  TITLE     WWOX binds the specific proline-rich ligand PPXY: identification of
            candidate interacting proteins
  JOURNAL   Oncogene 23 (29), 5049-5055 (2004)
   PUBMED   15064722
REFERENCE   10 (residues 1 to 668)
  AUTHORS   Winfield,S.L., Tayebi,N., Martin,B.M., Ginns,E.I. and Sidransky,E.
  TITLE     Identification of three additional genes contiguous to the
            glucocerebrosidase locus on chromosome 1q21: implications for
            Gaucher disease
  JOURNAL   Genome Res 7 (10), 1020-1026 (1997)
   PUBMED   9331372
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK093335.1, BC006493.2 and BC040136.1.
            
            On Nov 3, 2003 this sequence version replaced NP_006580.1.
            
            Summary: This gene is located near the gene for the lysosomal
            enzyme glucosylceramidase; a deficiency in this enzyme is
            associated with Gaucher disease. The encoded protein has been
            identified as a potential binding partner of a WW domain-containing
            protein which is involved in apoptosis and tumor suppression.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.27608.1,
                                           SRR1163657.186137.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361361.7/ ENSP00000354958.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..668
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..668
                     /product="protein ENTREP3 isoform a"
                     /note="protein FAM189B; family with sequence similarity
                     189 member B; protein ENTREP3"
                     /calculated_mol_wt=71224
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Region          36..196
                     /region_name="CD20"
                     /note="CD20-like family; pfam04103"
                     /db_xref="CDD:461174"
     Site            67..87
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            160
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P81408.2)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81408.2)"
     Region          386..419
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81408.2)"
     Region          442..503
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81408.2)"
     Region          550..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81408.2)"
     Region          597..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     Region          645..668
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P81408.2)"
     CDS             1..668
                     /gene="ENTREP3"
                     /gene_synonym="C1orf2; COTE1; FAM189B"
                     /coded_by="NM_006589.3:607..2613"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1103.1"
                     /db_xref="GeneID:10712"
                     /db_xref="HGNC:HGNC:1233"
                     /db_xref="MIM:619447"
ORIGIN      
        1 mmpspsdssr sltsrpstrg lthlrlhrpw lqalltlglv qvllgilvvt fsmvassvtt
       61 tesikrscps wagfslafsg vvgivswkrp ftlvisffsl lsvlcvmlsm agsvlsckna
      121 qlardfqqcs legkvcvccp svpllrpcpe sgqelkvapn stcdeargal knllfsvcgl
      181 ticaaiictl saivcciqif sldlvhtlap ersvsgplgp lgctspppap llhtmldlee
      241 fvppvppppy yppeytcsse tdaqsityng smdspvplyp tdcppsyeav mglrgdsqat
      301 lfdpqlhdgs cicervasiv dvsmdsgslv lsaigdlpgg sspsedscll elqgsvrsvd
      361 yvlfrsiqrs ragyclsldc glrgpfeesp lprrppraar syscsapeap pplgaptaar
      421 schrlegwpp wvgpcfpelr rrvprgggrp aaapptrapt rrfsdssgsl tppghrpphp
      481 asppplllpr shsdpgitts sdtadfrdly tkvleeeaas vssadtglcs eaclfrlarc
      541 pspkllrars aekrrpvptf qkvplpsgpa pahslgdlkg swpgrglvtr flqisrkapd
      601 psgtgahghk qvprslwgrp greslhlrsc gdlssssslr rllsgrrler gtrphslsln
      661 ggsretgl
//
LOCUS       NP_001290368             286 aa            linear   PRI 20-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290368
VERSION     NP_001290368.1
DBSOURCE    REFSEQ: accession NM_001303439.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP398345.1, AW340131.1,
            DB160394.1, BI829228.1, AK056946.1 and CA312679.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the shorter isoform (1). Variants 1-9 encode
            the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD359680.1, BI829228.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303439.1:1272..2132"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_002678                717 aa            linear   PRI 20-NOV-2025
DEFINITION  pinin [Homo sapiens].
ACCESSION   NP_002678
VERSION     NP_002678.3
DBSOURCE    REFSEQ: accession NM_002687.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 717)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 717)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 717)
  AUTHORS   Piccinno,E., Scalavino,V., Labarile,N., De Marinis,L.,
            Armentano,R., Giannelli,G. and Serino,G.
  TITLE     Identification of a Novel miR-195-5p/PNN Axis in Colorectal Cancer
  JOURNAL   Int J Mol Sci 25 (11), 5980 (2024)
   PUBMED   38892168
  REMARK    GeneRIF: Identification of a Novel miR-195-5p/PNN Axis in
            Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 717)
  AUTHORS   He,M., Jiang,D., Xun,A., Yang,J., Luo,Q. and Wu,H.
  TITLE     Methyltransferase like 3 enhances pinin mRNA stability through N6
            -methyladenosine modification to augment tumourigenesis of colon
            adenocarcinoma
  JOURNAL   Exp Physiol 107 (11), 1283-1297 (2022)
   PUBMED   35996844
  REMARK    GeneRIF: Methyltransferase like 3 enhances pinin mRNA stability
            through N(6) -methyladenosine modification to augment
            tumourigenesis of colon adenocarcinoma.
REFERENCE   5  (residues 1 to 717)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 717)
  AUTHORS   Shi,Y., Ouyang,P. and Sugrue,S.P.
  TITLE     Characterization of the gene encoding pinin/DRS/memA and evidence
            for its potential tumor suppressor function
  JOURNAL   Oncogene 19 (2), 289-297 (2000)
   PUBMED   10645008
REFERENCE   7  (residues 1 to 717)
  AUTHORS   Ouyang,P.
  TITLE     Antibodies differentiate desmosome-form and nucleus-form pinin:
            evidence that pinin is a moonlighting protein with dual location at
            the desmosome and within the nucleus
  JOURNAL   Biochem Biophys Res Commun 263 (1), 192-200 (1999)
   PUBMED   10486276
REFERENCE   8  (residues 1 to 717)
  AUTHORS   Degen,W.G., Agterbos,M.A., Muyrers,J.P., Bloemers,H.P. and
            Swart,G.W.
  TITLE     memA/DRS, a putative mediator of multiprotein complexes, is
            overexpressed in the metastasizing human melanoma cell lines BLM
            and MV3
  JOURNAL   Biochim Biophys Acta 1444 (3), 384-394 (1999)
   PUBMED   10095061
REFERENCE   9  (residues 1 to 717)
  AUTHORS   Brandner,J.M., Reidenbach,S. and Franke,W.W.
  TITLE     Evidence that 'pinin', reportedly a differentiation-specific
            desmosomal protein, is actually a widespread nuclear protein
  JOURNAL   Differentiation 62 (3), 119-127 (1997)
   PUBMED   9447706
REFERENCE   10 (residues 1 to 717)
  AUTHORS   Ouyang,P. and Sugrue,S.P.
  TITLE     Characterization of pinin, a novel protein associated with the
            desmosome-intermediate filament complex
  JOURNAL   J Cell Biol 135 (4), 1027-1042 (1996)
   PUBMED   8922384
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL132639.4.
            
            On Nov 23, 2018 this sequence version replaced NP_002678.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.112731.1,
                                           SRR1660803.118083.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216832.9/ ENSP00000216832.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..717
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q21.1"
     Protein         1..717
                     /product="pinin"
                     /note="neutrophil protein; SR-like protein; nuclear
                     protein SDK3; domain-rich serine protein;
                     desmosome-associated protein; melanoma metastasis clone A
                     protein; 140 kDa nuclear and cell adhesion-related
                     phosphoprotein"
                     /calculated_mol_wt=81497
     Region          1..130
                     /region_name="Pinin_SDK_N"
                     /note="pinin/SDK conserved region; pfam04697"
                     /db_xref="CDD:461397"
     Region          2..284
                     /region_name="Necessary for interaction with RNPS1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          2..167
                     /region_name="Necessary for mediating alternative 5'
                     splicing"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          2..98
                     /region_name="Necessary for interactions with KRT8, KRT18
                     and KRT19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          46..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            54
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35691; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            124
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          136..261
                     /region_name="Pinin_SDK_memA"
                     /note="pinin/SDK/memA/ protein conserved region;
                     pfam04696"
                     /db_xref="CDD:461396"
     Region          221..284
                     /region_name="Sufficient for PSAP complex assembly"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          279..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35691; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Region          606..717
                     /region_name="Necessary for interaction with PPIG.
                     /evidence=ECO:0000269|PubMed:15358154"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H307.5)"
     CDS             1..717
                     /gene="PNN"
                     /gene_synonym="DRS; DRSP; memA; SDK3"
                     /coded_by="NM_002687.4:27..2180"
                     /db_xref="CCDS:CCDS9671.1"
                     /db_xref="GeneID:5411"
                     /db_xref="HGNC:HGNC:9162"
                     /db_xref="MIM:603154"
ORIGIN      
        1 mavavrtlqe qlekakeslk nvdenirklt grdpndvrpi qarllalsgp gggrgrgsll
       61 lrrgfsdsgg gppakqrdle gavsrlgger rtrresrqes dpedddvkkp alqssvvats
      121 kertrrdliq dqnmdekgkq rnrrifgllm gtlqkfkqes tvaterqkrr qeieqklevq
      181 aeeerkqven errelfeerr akqtelrlle qkvelaqlqe ewnehnakii kyirtktkph
      241 lfyipgrmcp atqklieesq rkmnalfegr riefaeqink mearprrqsm kekehqvvrn
      301 eeqkaeqeeg kvaqreeele etgnqhndve ieeageeeek eiaivhsdae keqeeeeqkq
      361 emevkmeeet evresekqqd sqpeevmdvl emvenvkhvi adqevmetnr vesvepsene
      421 askelepeme feiepdkeck tlspgkenvs aldmekesee keekesepqp epvaqpqpqs
      481 qpqlqlqsqs qpvlqsqpps qpedlslavl qptpqvtqeq ghllperkdf pvesvkltev
      541 pvepvltvhp esksktktrs rsrgrarnkt sksrsrssss ssssssstss ssgsssssgs
      601 sssrssssss sstsgsssrd sssstsssse srsrsrgrgh nrdrkhrrsv drkrrdtsgl
      661 ershksskgg ssrdtkgskd knsrsdrkrs isessrsgkr ssrserdrks drkdkrr
//
LOCUS       NP_001284586             612 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF2C isoform 4 [Homo sapiens].
ACCESSION   NP_001284586
VERSION     NP_001284586.1
DBSOURCE    REFSEQ: accession NM_001297657.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 612)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 612)
  AUTHORS   Kalkan,B.M., Ozcan,S.C., Cicek,E., Gonen,M. and Acilan,C.
  TITLE     Nek2A prevents centrosome clustering and induces cell death in
            cancer cells via KIF2C interaction
  JOURNAL   Cell Death Dis 15 (3), 222 (2024)
   PUBMED   38493150
  REMARK    GeneRIF: Nek2A prevents centrosome clustering and induces cell
            death in cancer cells via KIF2C interaction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 612)
  AUTHORS   Deng,H., Gong,X., Ji,G., Li,C. and Cheng,S.
  TITLE     KIF2C promotes clear cell renal cell carcinoma progression via
            activating JAK2/STAT3 signaling pathway
  JOURNAL   Mol Cell Probes 72, 101938 (2023)
   PUBMED   37863123
  REMARK    GeneRIF: KIF2C promotes clear cell renal cell carcinoma progression
            via activating JAK2/STAT3 signaling pathway.
REFERENCE   4  (residues 1 to 612)
  AUTHORS   Li,S., Ma,Y., Wu,C. and Hou,X.
  TITLE     Knockdown of kinesin family member 2C restricts cell proliferation
            and induces cell cycle arrest in gastric cancer
  JOURNAL   Histol Histopathol 38 (8), 907-916 (2023)
   PUBMED   36448588
  REMARK    GeneRIF: Knockdown of kinesin family member 2C restricts cell
            proliferation and induces cell cycle arrest in gastric cancer.
REFERENCE   5  (residues 1 to 612)
  AUTHORS   Cheng,L.J., Zhou,Z.M., Li,J.M., Zhu,H., Zhu,H., Zhou,Y.D.,
            Wang,L.R., Lin,M. and Sha,J.H.
  TITLE     Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in
            human testis
  JOURNAL   Life Sci 71 (23), 2741-2757 (2002)
   PUBMED   12383881
  REMARK    GeneRIF: identification as a candidate gene for the testis-specific
            KRPs and its specific expression in the testis was correlated with
            spermatogenesis and may be correlated with male infertility
REFERENCE   6  (residues 1 to 612)
  AUTHORS   Miki,H., Setou,M., Kaneshiro,K. and Hirokawa,N.
  TITLE     All kinesin superfamily protein, KIF, genes in mouse and human
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7004-7011 (2001)
   PUBMED   11416179
  REMARK    Review article
REFERENCE   7  (residues 1 to 612)
  AUTHORS   Sugata,N., Li,S., Earnshaw,W.C., Yen,T.J., Yoda,K., Masumoto,H.,
            Munekata,E., Warburton,P.E. and Todokoro,K.
  TITLE     Human CENP-H multimers colocalize with CENP-A and CENP-C at active
            centromere--kinetochore complexes
  JOURNAL   Hum Mol Genet 9 (19), 2919-2926 (2000)
   PUBMED   11092768
REFERENCE   8  (residues 1 to 612)
  AUTHORS   Wordeman,L., Wagenbach,M. and Maney,T.
  TITLE     Mutations in the ATP-binding domain affect the subcellular
            distribution of mitotic centromere-associated kinesin (MCAK)
  JOURNAL   Cell Biol Int 23 (4), 275-286 (1999)
   PUBMED   10600236
REFERENCE   9  (residues 1 to 612)
  AUTHORS   Maney,T., Hunter,A.W., Wagenbach,M. and Wordeman,L.
  TITLE     Mitotic centromere-associated kinesin is important for anaphase
            chromosome segregation
  JOURNAL   J Cell Biol 142 (3), 787-801 (1998)
   PUBMED   9700166
REFERENCE   10 (residues 1 to 612)
  AUTHORS   Kim,I.G., Jun,D.Y., Sohn,U. and Kim,Y.H.
  TITLE     Cloning and expression of human mitotic centromere-associated
            kinesin gene
  JOURNAL   Biochim Biophys Acta 1359 (3), 181-186 (1997)
   PUBMED   9434124
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC399082.1, AK302267.1,
            BC014924.1 and BU615368.1.
            
            Summary: This gene encodes a kinesin-like protein that functions as
            a microtubule-dependent molecular motor. The encoded protein can
            depolymerize microtubules at the plus end, thereby promoting
            mitotic chromosome segregation. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (4) has a shorter N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302267.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..612
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..612
                     /product="kinesin-like protein KIF2C isoform 4"
                     /note="mitotic centromere-associated kinesin; kinesin-like
                     protein KIF2C; kinesin-like protein 6; testis tissue
                     sperm-binding protein Li 68n"
                     /calculated_mol_wt=68688
     Region          145..473
                     /region_name="KISc_KIF2_like"
                     /note="Kinesin motor domain, KIF2-like group; cd01367"
                     /db_xref="CDD:276818"
     Site            order(153,235,238,240..243,379)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276818"
     Site            order(427,430,433)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276818"
     CDS             1..612
                     /gene="KIF2C"
                     /gene_synonym="CT139; KNSL6; MCAK"
                     /coded_by="NM_001297657.2:228..2066"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:11004"
                     /db_xref="HGNC:HGNC:6393"
                     /db_xref="MIM:604538"
ORIGIN      
        1 mstvselrit aqendmevel paaansrkqf svppaptrps cpavaeiplr mvseemeeqv
       61 hsirgsssan pvnsvrrksc lvkevekmkn kreekkaqns emrmkraqey dssfpnwefa
      121 rmikefratl echpltmtdp ieehricvcv rkrplnkqel akkeidvisi pskclllvhe
      181 pklkvdltky lenqafcfdf afdetasnev vyrftarplv qtifeggkat cfaygqtgsg
      241 kthtmggdls gkaqnaskgi yamasrdvfl lknqpcyrkl glevyvtffe iyngklfdll
      301 nkkaklrvle dgkqqvqvvg lqehlvnsad dvikmidmgs acrtsgqtfa nsnssrshac
      361 fqiilrakgr mhgkfslvdl agnergadts sadrqtrmeg aeinksllal keciralgqn
      421 kahtpfresk ltqvlrdsfi gensrtcmia tispgissce ytlntlryad rvkelsphsg
      481 psgeqliqme teemeacsng alipgnlske eeelssqmss fneamtqire leekameelk
      541 eiiqqgpdwl elsemteqpd ydletfvnka esalaqqakh fsalrdvika lrlamqleeq
      601 asrqisskkr pq
//
LOCUS       NP_001308428             283 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-10 isoform 5 [Homo sapiens].
ACCESSION   NP_001308428 XP_011509007
VERSION     NP_001308428.1
DBSOURCE    REFSEQ: accession NM_001321499.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            On Mar 25, 2016 this sequence version replaced XP_011509007.1.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294427.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..283
                     /product="septin-10 isoform 5"
                     /calculated_mol_wt=32894
     Region          <32..164
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            41..44
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     Site            95..97
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206648"
     CDS             1..283
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321499.2:140..991"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 massevarhl lfqshmatkt tcmssqgsdd eqivniipvi akadtvskte lqkfkiklms
       61 elvsngvqiy qfptdddtia kvnaamngql pfavvgsmde vkvgnkmvka rqypwgvvqv
      121 enenhcdfvk lremlictnm edlreqthtr hyelyrrckl eemgftdvgp enkpvsvqet
      181 yeakrhefhg erqrkeeemk qmfvqrvkek eailkeaere lqakfehlkr lhqeermkle
      241 ekrrlleeei iafskkkats eifhsqsfla tgsnlrkdkd rkk
//
LOCUS       NP_001354658             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354658
VERSION     NP_001354658.1
DBSOURCE    REFSEQ: accession NM_001367729.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (13), as well as variants 3, 4,
            9-12, and 14-20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.234973.1,
                                           SRR1803611.121142.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367729.1:111..1586"
                     /note="isoform c is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001182470             221 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 225B [Homo sapiens].
ACCESSION   NP_001182470 XP_002342783 XP_002344413 XP_002346060 XP_002346946
VERSION     NP_001182470.1
DBSOURCE    REFSEQ: accession NM_001195541.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Polasek,O., Marusic,A., Rotim,K., Hayward,C., Vitart,V.,
            Huffman,J., Campbell,S., Jankovic,S., Boban,M., Biloglav,Z.,
            Kolcic,I., Krzelj,V., Terzic,J., Matec,L., Tometic,G., Nonkovic,D.,
            Nincevic,J., Pehlic,M., Zedelj,J., Velagic,V., Juricic,D.,
            Kirac,I., Belak Kovacevic,S., Wright,A.F., Campbell,H. and Rudan,I.
  TITLE     Genome-wide association study of anthropometric traits in Korcula
            Island, Croatia
  JOURNAL   Croat Med J 50 (1), 7-16 (2009)
   PUBMED   19260139
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB477974.1, DB462723.1, AA781117.1 and HY200726.1.
            
            On or before Sep 16, 2010 this sequence version replaced
            XP_002342783.1, XP_002346946.1, XP_002346060.1, XP_002344413.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-3 all encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.29651.1,
                                           SRR5189667.333299.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431679.6/ ENSP00000492416.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..221
                     /product="transmembrane protein 225B"
                     /note="transmembrane protein 225-like"
                     /calculated_mol_wt=24896
     Site            14..34
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            109..129
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P0DP42.1)"
     CDS             1..221
                     /gene="TMEM225B"
                     /gene_synonym="GS1-259H13.2"
                     /coded_by="NM_001195541.3:200..865"
                     /db_xref="CCDS:CCDS87525.1"
                     /db_xref="GeneID:100289187"
                     /db_xref="HGNC:HGNC:53075"
ORIGIN      
        1 mltledkdmk gfswaivpal tslgyliilv vsifpfwvrl tneeshevff sglfencfna
       61 kcwkprplsi yiilgrvfll savflafvtt fimmpfasef fprtwkqnfv lacisfftga
      121 caflalvlha leikalrmkl gplqfsvlwp yyvlgfgifl fivagticli qemvcpcwhl
      181 lstsqsmeed hgslyldnle slggepssvq ketqvtaetv i
//
LOCUS       NP_001353495             821 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001353495 XP_016855515
VERSION     NP_001353495.1
DBSOURCE    REFSEQ: accession NM_001366566.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855515.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.37790.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..821
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 4"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=92527
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <523..>657
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..821
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366566.1:405..2870"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels eseedkggkm aaadsvqqrr qyrrqnqqss sdsgssssse
      421 derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr grrrrspspp ptrrrrspsp
      481 appprrrrtp tppprrrtps ppprrrspsp rrysppiqrr yspspppkrr taspppppkr
      541 raspspppkr rvshspppkq rsspvtkrrs pslsskhrkg sspsrstrea rspqpnkrhs
      601 psprprapqt ssspppvrrg assspqrrqs pspstrpirr vsrtpepkki kkaaspspqs
      661 vrrvsssrsv sgspepaakk ppappspvqs qspstnwspa vpvkkakspt pspspprnsd
      721 qegggkkkkk kkdkkhkkdk khkkhkkhkk ekavaaaaaa avtpaaiaaa tttlaqeepv
      781 aapepkkete seaednlddl ekhlrekalr smrkaqvspq s
//
LOCUS       NP_001350928             590 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform f precursor [Homo sapiens].
ACCESSION   NP_001350928
VERSION     NP_001350928.1
DBSOURCE    REFSEQ: accession NM_001363999.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 590)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 590)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 590)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 590)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 590)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 590)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 590)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 590)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 590)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 590)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.34229.1,
                                           SRR1803617.264358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..590
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..590
                     /product="calnexin isoform f precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65140
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     Region          71..440
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27824.2)"
     Region          260..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          276..409
                     /region_name="P domain (Extended arm).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          278..345
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          326..359
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          348..405
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          509..590
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK3.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     CDS             1..590
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001363999.1:178..1950"
                     /note="isoform f precursor is encoded by transcript
                     variant 9"
                     /db_xref="CCDS:CCDS93839.1"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 megkwllcml lvlgtaivea hdghdddvid ieddlddvie evedskpdtt appsspkvty
       61 kapvptgevy fadsfdrgtl sgwilskakk ddtddeiaky dgkweveemk esklpgdkgl
      121 vlmsrakhha isaklnkpfl fdtkplivqy evnfqngiec ggayvkllsk tpelnldqfh
      181 dktpytimfg pdkcgedykl hfifrhknpk tgiyeekhak rpdadlktyf tdkkthlytl
      241 ilnpdnsfei lvdqsvvnsg nllndmtppv npsreiedpe drkpedwder pkipdpeavk
      301 pddwdedapa kipdeeatkp egwlddepey vpdpdaekpe dwdedmdgew eapqianprc
      361 esapgcgvwq rpvidnpnyk gkwkppmidn psyqgiwkpr kipnpdffed lepfrmtpfs
      421 aiglelwsmt sdiffdnfii cadrrivddw andgwglkka adgaaepgvv gqmieaaeer
      481 pwlwvvyilt valpvflvil fccsgktsgm eykktdapqp dvkeeeeeke eekdkgdeee
      541 egeekleekq ksdaeedggt vsqeeedrkp kaeedeilnr sprnrkprre
//
LOCUS       NP_055458               1163 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 516 [Homo sapiens].
ACCESSION   NP_055458 XP_496278 XP_942502
VERSION     NP_055458.1
DBSOURCE    REFSEQ: accession NM_014643.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1163)
  AUTHORS   Xie,Z.Q., Chen,F., He,J., Zhong,L., Luo,G. and Fang,M.
  TITLE     MiR-371-5p regulates trophoblast cell proliferation, migration, and
            invasion by directly targeting ZNF516
  JOURNAL   Aging (Albany NY) 16 (10), 8585-8598 (2024)
   PUBMED   38761180
  REMARK    GeneRIF: MiR-371-5p regulates trophoblast cell proliferation,
            migration, and invasion by directly targeting ZNF516.
REFERENCE   3  (residues 1 to 1163)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1163)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   5  (residues 1 to 1163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1163)
  AUTHORS   O'Brien,R.P., Phelan,P.J., Conroy,J., O'Kelly,P., Green,A.,
            Keogan,M., O'Neill,D., Jennings,S., Traynor,C., Casey,J.,
            McCormack,M., Conroy,R., Chubb,A., Ennis,S., Shields,D.C.,
            Cavalleri,G.L. and Conlon,P.J.
  TITLE     A genome-wide association study of recipient genotype and
            medium-term kidney allograft function
  JOURNAL   Clin Transplant 27 (3), 379-387 (2013)
   PUBMED   23432519
REFERENCE   7  (residues 1 to 1163)
  AUTHORS   Yang,T.L., Guo,Y., Li,J., Zhang,L., Shen,H., Li,S.M., Li,S.K.,
            Tian,Q., Liu,Y.J., Papasian,C.J. and Deng,H.W.
  TITLE     Gene-gene interaction between RBMS3 and ZNF516 influences bone
            mineral density
  JOURNAL   J Bone Miner Res 28 (4), 828-837 (2013)
   PUBMED   23045156
  REMARK    GeneRIF: one interacting gene pair (RBMS3 versus ZNF516) which,
            even after Bonferroni correction for multiple testing, showed
            consistently significant effects on hip bone mineral density.
REFERENCE   8  (residues 1 to 1163)
  AUTHORS   Shaffer,J.R., Feingold,E., Wang,X., Lee,M., Tcuenco,K., Weeks,D.E.,
            Weyant,R.J., Crout,R., McNeil,D.W. and Marazita,M.L.
  TITLE     GWAS of dental caries patterns in the permanent dentition
  JOURNAL   J Dent Res 92 (1), 38-44 (2013)
   PUBMED   23064961
REFERENCE   9  (residues 1 to 1163)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
REFERENCE   10 (residues 1 to 1163)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018413.10, D86975.1,
            AC009716.22 and BC108287.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jul 5, 2007 this sequence version replaced
            XP_496278.2, XP_942502.1.
            
            Summary: Zinc-finger proteins bind nucleic acids and play important
            roles in various cellular functions, including cell proliferation,
            differentiation, and apoptosis. This gene encodes a zinc-finger
            protein, and belongs to the krueppel C2H2-type zinc-finger protein
            family. It may be involved in transcriptional regulation. [provided
            by RefSeq, Sep 2012].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86975.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443185.7/ ENSP00000394757.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..1163
                     /product="zinc finger protein 516"
                     /calculated_mol_wt=124159
     Region          1..431
                     /region_name="Mediates promoter DNA-binding and activation
                     of transcription. /evidence=ECO:0000250|UniProtKB:Q7TSH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          34..56
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          36..56
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          48..73
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          64..84
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          176..194
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          202..223
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(207,209,211,213..214,217..218,222,255,257,261..262,
                     265..266,269,283,285,287,289..290,293..294,297)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          248..270
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          250..270
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          278..298
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          460..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          533..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          679..730
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          838..1007
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     Region          <915..>1037
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          1098..1120
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          1100..1120
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1126..1163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92618.1)"
     CDS             1..1163
                     /gene="ZNF516"
                     /gene_synonym="HsT287"
                     /coded_by="NM_014643.4:371..3862"
                     /db_xref="CCDS:CCDS74234.1"
                     /db_xref="GeneID:9658"
                     /db_xref="HGNC:HGNC:28990"
                     /db_xref="MIM:615114"
ORIGIN      
        1 mdrnreaeme lrrgpsptra grghevdgdk atchtccicg ksfpfqssls qhmrkhtgek
       61 pykcpycdhr asqkgnlkih irshrtgtli qghepeagea plgemraseg ldacasptks
      121 asacnrllng asqadgarvl ngasqadsgr vllrsskkga egsacapgea kaavqcsfck
      181 sqferkkdle lhvhqahkpf kcrlcsyatl reesllshie rdhitaqgpg sgeacvengk
      241 pelspgefpc evcgqafsqt wflkahmkkh rgsfdhgchi cgrrfkepwf lknhmkahgp
      301 ktgsknrpks eldpiatinn vvqeevivag lslyevcakc gnlftnldsl nahnaihrrv
      361 easrtrapae egaegpsdtk qfflqclnlr psaagdscpg tqagrrvael dpvnsyqawq
      421 latrgkvaep aeylkygawd ealagdvafd kdrreyvlvs qekrkreqda paaqgpprkr
      481 asgpgdpapa ghldprsaar pnrraaattg qgkssecfec gkifrtyhqm vlhsrvhrra
      541 rrerdsdgdr aararcgsls egdsasqpss pgsacaaads pgsgladeaa edsgeegape
      601 papggqprrc cfseevtste lssgdqshkm gdnaserdtg eskagiaasv silenssret
      661 srrqeqhrfs mdlkmpafhp kqevpvpgdg vefpsstgae gqtghpaekl sdlhnkehsg
      721 ggkralapdl mpldlsarst rddpsnketa sslqaalvvh pcpycshkty ypevlwmhkr
      781 iwhrvscnsv appwiqpngy ksirsnlvfl srsgrtgppp alggkecqpl llarftrtqv
      841 pggmpgsksg ssplgvvtka asmpknkesh sggpcalwap gpdgyrqtkp chgqephgaa
      901 tqgplakprq easskpvpap ggggfsrsat ptptviarag aqpsanskpv ekfgvppaga
      961 gfaptnkhsa pdslkakfsa qpqgpppakg eggapplppr eppskaaqel rtlatcaags
     1021 rgdaalqaqp gvagappvlh sikqepvaeg hekrldilni fktyipkdfa tlyqgwgvsg
     1081 pglehrgtlr tqarpgefvc iecgksfhqp ghlrahmrah svvfesdgpr gsevhttsad
     1141 apkqgrdhsn tgtvqtvplr kgt
//
LOCUS       NP_079092                569 aa            linear   PRI 20-NOV-2025
DEFINITION  rab GTPase-binding effector protein 2 [Homo sapiens].
ACCESSION   NP_079092 XP_942883
VERSION     NP_079092.2
DBSOURCE    REFSEQ: accession NM_024816.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Lee,H.K., Kwon,D.H., Aylor,D.L. and Marchuk,D.A.
  TITLE     A cross-species approach using an in vivo evaluation platform in
            mice demonstrates that sequence variation in human RABEP2 modulates
            ischemic stroke outcomes
  JOURNAL   Am J Hum Genet 109 (10), 1814-1827 (2022)
   PUBMED   36167069
  REMARK    GeneRIF: A cross-species approach using an in vivo evaluation
            platform in mice demonstrates that sequence variation in human
            RABEP2 modulates ischemic stroke outcomes.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Noto,J.M., Rose,K.L., Hachey,A.J., Delgado,A.G., Romero-Gallo,J.,
            Wroblewski,L.E., Schneider,B.G., Shah,S.C., Cover,T.L.,
            Wilson,K.T., Israel,D.A., Roa,J.C., Schey,K.L., Zavros,Y.,
            Piazuelo,M.B. and Peek,R.M. Jr.
  TITLE     Carcinogenic Helicobacter pylori Strains Selectively Dysregulate
            the In Vivo Gastric Proteome, Which May Be Associated with Stomach
            Cancer Progression
  JOURNAL   Mol Cell Proteomics 18 (2), 352-371 (2019)
   PUBMED   30455363
  REMARK    GeneRIF: Results found that H. pylori upregulates RABEP2 in human
            gastric epithelium. In addition, the level of RABEP2 expression
            increases with severity of gastric malignant lesions in vivo.
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Logie,L., Van Aalten,L., Knebel,A., Force,T., Hastie,C.J.,
            MacLauchlan,H., Campbell,D.G., Gourlay,R., Prescott,A.,
            Davidson,J., Fuller,W. and Sutherland,C.
  TITLE     Rab-GTPase binding effector protein 2 (RABEP2) is a primed
            substrate for Glycogen Synthase kinase-3 (GSK3)
  JOURNAL   Sci Rep 7 (1), 17682 (2017)
   PUBMED   29247183
  REMARK    GeneRIF: Phosphorylation regulates RABEP2 function.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Airik,R., Schueler,M., Airik,M., Cho,J., Ulanowicz,K.A.,
            Porath,J.D., Hurd,T.W., Bekker-Jensen,S., Schroder,J.M.,
            Andersen,J.S. and Hildebrandt,F.
  TITLE     SDCCAG8 Interacts with RAB Effector Proteins RABEP2 and ERC1 and Is
            Required for Hedgehog Signaling
  JOURNAL   PLoS One 11 (5), e0156081 (2016)
   PUBMED   27224062
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Berndt,S.I., Gustafsson,S., Magi,R., Ganna,A., Wheeler,E.,
            Feitosa,M.F., Justice,A.E., Monda,K.L., Croteau-Chonka,D.C.,
            Day,F.R., Esko,T., Fall,T., Ferreira,T., Gentilini,D.,
            Jackson,A.U., Luan,J., Randall,J.C., Vedantam,S., Willer,C.J.,
            Winkler,T.W., Wood,A.R., Workalemahu,T., Hu,Y.J., Lee,S.H.,
            Liang,L., Lin,D.Y., Min,J.L., Neale,B.M., Thorleifsson,G., Yang,J.,
            Albrecht,E., Amin,N., Bragg-Gresham,J.L., Cadby,G., den Heijer,M.,
            Eklund,N., Fischer,K., Goel,A., Hottenga,J.J., Huffman,J.E.,
            Jarick,I., Johansson,A., Johnson,T., Kanoni,S., Kleber,M.E.,
            Konig,I.R., Kristiansson,K., Kutalik,Z., Lamina,C., Lecoeur,C.,
            Li,G., Mangino,M., McArdle,W.L., Medina-Gomez,C.,
            Muller-Nurasyid,M., Ngwa,J.S., Nolte,I.M., Paternoster,L.,
            Pechlivanis,S., Perola,M., Peters,M.J., Preuss,M., Rose,L.M.,
            Shi,J., Shungin,D., Smith,A.V., Strawbridge,R.J., Surakka,I.,
            Teumer,A., Trip,M.D., Tyrer,J., Van Vliet-Ostaptchouk,J.V.,
            Vandenput,L., Waite,L.L., Zhao,J.H., Absher,D., Asselbergs,F.W.,
            Atalay,M., Attwood,A.P., Balmforth,A.J., Basart,H., Beilby,J.,
            Bonnycastle,L.L., Brambilla,P., Bruinenberg,M., Campbell,H.,
            Chasman,D.I., Chines,P.S., Collins,F.S., Connell,J.M.,
            Cookson,W.O., de Faire,U., de Vegt,F., Dei,M., Dimitriou,M.,
            Edkins,S., Estrada,K., Evans,D.M., Farrall,M., Ferrario,M.M.,
            Ferrieres,J., Franke,L., Frau,F., Gejman,P.V., Grallert,H.,
            Gronberg,H., Gudnason,V., Hall,A.S., Hall,P., Hartikainen,A.L.,
            Hayward,C., Heard-Costa,N.L., Heath,A.C., Hebebrand,J., Homuth,G.,
            Hu,F.B., Hunt,S.E., Hypponen,E., Iribarren,C., Jacobs,K.B.,
            Jansson,J.O., Jula,A., Kahonen,M., Kathiresan,S., Kee,F.,
            Khaw,K.T., Kivimaki,M., Koenig,W., Kraja,A.T., Kumari,M.,
            Kuulasmaa,K., Kuusisto,J., Laitinen,J.H., Lakka,T.A.,
            Langenberg,C., Launer,L.J., Lind,L., Lindstrom,J., Liu,J.,
            Liuzzi,A., Lokki,M.L., Lorentzon,M., Madden,P.A., Magnusson,P.K.,
            Manunta,P., Marek,D., Marz,W., Mateo Leach,I., McKnight,B.,
            Medland,S.E., Mihailov,E., Milani,L., Montgomery,G.W., Mooser,V.,
            Muhleisen,T.W., Munroe,P.B., Musk,A.W., Narisu,N., Navis,G.,
            Nicholson,G., Nohr,E.A., Ong,K.K., Oostra,B.A., Palmer,C.N.,
            Palotie,A., Peden,J.F., Pedersen,N., Peters,A., Polasek,O.,
            Pouta,A., Pramstaller,P.P., Prokopenko,I., Putter,C.,
            Radhakrishnan,A., Raitakari,O., Rendon,A., Rivadeneira,F.,
            Rudan,I., Saaristo,T.E., Sambrook,J.G., Sanders,A.R., Sanna,S.,
            Saramies,J., Schipf,S., Schreiber,S., Schunkert,H., Shin,S.Y.,
            Signorini,S., Sinisalo,J., Skrobek,B., Soranzo,N., Stancakova,A.,
            Stark,K., Stephens,J.C., Stirrups,K., Stolk,R.P., Stumvoll,M.,
            Swift,A.J., Theodoraki,E.V., Thorand,B., Tregouet,D.A., Tremoli,E.,
            Van der Klauw,M.M., van Meurs,J.B., Vermeulen,S.H., Viikari,J.,
            Virtamo,J., Vitart,V., Waeber,G., Wang,Z., Widen,E., Wild,S.H.,
            Willemsen,G., Winkelmann,B.R., Witteman,J.C., Wolffenbuttel,B.H.,
            Wong,A., Wright,A.F., Zillikens,M.C., Amouyel,P., Boehm,B.O.,
            Boerwinkle,E., Boomsma,D.I., Caulfield,M.J., Chanock,S.J.,
            Cupples,L.A., Cusi,D., Dedoussis,G.V., Erdmann,J., Eriksson,J.G.,
            Franks,P.W., Froguel,P., Gieger,C., Gyllensten,U., Hamsten,A.,
            Harris,T.B., Hengstenberg,C., Hicks,A.A., Hingorani,A., Hinney,A.,
            Hofman,A., Hovingh,K.G., Hveem,K., Illig,T., Jarvelin,M.R.,
            Jockel,K.H., Keinanen-Kiukaanniemi,S.M., Kiemeney,L.A., Kuh,D.,
            Laakso,M., Lehtimaki,T., Levinson,D.F., Martin,N.G., Metspalu,A.,
            Morris,A.D., Nieminen,M.S., Njolstad,I., Ohlsson,C.,
            Oldehinkel,A.J., Ouwehand,W.H., Palmer,L.J., Penninx,B., Power,C.,
            Province,M.A., Psaty,B.M., Qi,L., Rauramaa,R., Ridker,P.M.,
            Ripatti,S., Salomaa,V., Samani,N.J., Snieder,H., Sorensen,T.I.,
            Spector,T.D., Stefansson,K., Tonjes,A., Tuomilehto,J.,
            Uitterlinden,A.G., Uusitupa,M., van der Harst,P., Vollenweider,P.,
            Wallaschofski,H., Wareham,N.J., Watkins,H., Wichmann,H.E.,
            Wilson,J.F., Abecasis,G.R., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunian,T., Heid,I.M., Hunter,D., Kaplan,R.C., Karpe,F.,
            Moffatt,M.F., Mohlke,K.L., O'Connell,J.R., Pawitan,Y., Schadt,E.E.,
            Schlessinger,D., Steinthorsdottir,V., Strachan,D.P.,
            Thorsteinsdottir,U., van Duijn,C.M., Visscher,P.M., Di Blasio,A.M.,
            Hirschhorn,J.N., Lindgren,C.M., Morris,A.P., Meyre,D., Scherag,A.,
            McCarthy,M.I., Speliotes,E.K., North,K.E., Loos,R.J. and
            Ingelsson,E.
  TITLE     Genome-wide meta-analysis identifies 11 new loci for anthropometric
            traits and provides insights into genetic architecture
  JOURNAL   Nat Genet 45 (5), 501-512 (2013)
   PUBMED   23563607
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Schindler,E.M., Baumgartner,M., Gribben,E.M., Li,L. and Efimova,T.
  TITLE     The role of proline-rich protein tyrosine kinase 2 in
            differentiation-dependent signaling in human epidermal
            keratinocytes
  JOURNAL   J Invest Dermatol 127 (5), 1094-1106 (2007)
   PUBMED   17205062
  REMARK    GeneRIF: Pyk2 regulation is associated with increased expression of
            Fra-1 and JunD, activator protein-1 transcription factors known to
            be required for involucrin expression.
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Chiappetta,G., Ferraro,A., Botti,G., Monaco,M., Pasquinelli,R.,
            Vuttariello,E., Arnaldi,L., Di Bonito,M., D'Aiuto,G.,
            Pierantoni,G.M. and Fusco,A.
  TITLE     FRA-1 protein overexpression is a feature of hyperplastic and
            neoplastic breast disorders
  JOURNAL   BMC Cancer 7, 17 (2007)
   PUBMED   17254320
  REMARK    GeneRIF: FRA-1 expression, including its intracellular
            localization, may be considered a useful marker for hyperplastic
            and neoplastic proliferative breast disorders
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Gournier,H., Stenmark,H., Rybin,V., Lippe,R. and Zerial,M.
  TITLE     Two distinct effectors of the small GTPase Rab5 cooperate in
            endocytic membrane fusion
  JOURNAL   EMBO J 17 (7), 1930-1940 (1998)
   PUBMED   9524116
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC109460.3, AK026935.1 and BC046118.1.
            
            On Nov 15, 2006 this sequence version replaced NP_079092.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026935.1, AK092299.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358201.9/ ENSP00000350934.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..569
                     /product="rab GTPase-binding effector protein 2"
                     /note="Rabaptin-5 beta; rabaptin-5beta"
                     /calculated_mol_wt=63412
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Region          21..>181
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     Region          180..265
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62835; propagated from
                     UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha.
                     /evidence=ECO:0000269|PubMed:29247183; propagated from
                     UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29247183; propagated from
                     UniProtKB/Swiss-Prot (Q9H5N1.2)"
     Region          291..546
                     /region_name="Rab5-bind"
                     /note="Rabaptin-like protein; pfam09311"
                     /db_xref="CDD:462752"
     Region          388..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5N1.2)"
     CDS             1..569
                     /gene="RABEP2"
                     /gene_synonym="FRA"
                     /coded_by="NM_024816.3:76..1785"
                     /db_xref="CCDS:CCDS42140.1"
                     /db_xref="GeneID:79874"
                     /db_xref="HGNC:HGNC:24817"
                     /db_xref="MIM:611869"
ORIGIN      
        1 maaaapvaad dderrrrpga aledsrsqeg angeaesgel srlraelaga laemetmkav
       61 aevsestkae avaavqrqcq eevaslqail kdsissyeaq italkqerqq qqqdceeker
      121 elgrlkqlls raypldslek qmekahedse klreivlpme keieelkakl lraeeliqei
      181 qrrprhapsl hgstellpls rdpspplepl eelsgdggpa aeafahncdd sasissfslg
      241 ggvgsssslp qsrqglspeq eetaslvstg tlvpegiylp ppgyqlvpdt qweqlqtegr
      301 qlqkdlesvs rerdelqegl rrsnedcakq mqvllaqvqn seqllrtlqg tvsqaqervq
      361 lqmaelvtth kclhhevkrl neenqglrae qlpssapqgs qqeqgeeesl pssvpelqql
      421 lcctrqeara rlqaqehgae rlrieivtlr ealeeetvar aslegqlrvq reetevleas
      481 lcslrtemer vqqeqskaql pdllseqrak vlrlqaelet seqvqrdfvr lsqalqvrle
      541 rirqaetleq vrsimdeapl tdvrdikdt
//
LOCUS       NP_001271292             718 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase tousled-like 2 isoform B [Homo
            sapiens].
ACCESSION   NP_001271292
VERSION     NP_001271292.1
DBSOURCE    REFSEQ: accession NM_001284363.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 718)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 718)
  AUTHORS   Liang,B., Yin,J.J., Zhang,S.N., Zhang,C., Hu,Z.L. and Wang,Y.
  TITLE     [Effect of TLK2 Expression Regulated by MiR-21 on Proliferation and
            Apoptosis of Acute Myeloid Leukemia Cells]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 32 (3), 658-662 (2024)
   PUBMED   38926950
  REMARK    GeneRIF: [Effect of TLK2 Expression Regulated by MiR-21 on
            Proliferation and Apoptosis of Acute Myeloid Leukemia Cells].
REFERENCE   3  (residues 1 to 718)
  AUTHORS   Ronald,S., Sunavala-Dossabhoy,G., Adams,L., Williams,B. and De
            Benedetti,A.
  TITLE     The expression of Tousled kinases in CaP cell lines and its
            relation to radiation response and DSB repair
  JOURNAL   Prostate 71 (13), 1367-1373 (2011)
   PUBMED   21647934
  REMARK    GeneRIF: TLKs appear to be intimately linked to the pattern of
            resistance to DNA damage, and specifically double-strand breaks.
REFERENCE   4  (residues 1 to 718)
  AUTHORS   Couch,F.J., Wang,X., Bamlet,W.R., de Andrade,M., Petersen,G.M. and
            McWilliams,R.R.
  TITLE     Association of mitotic regulation pathway polymorphisms with
            pancreatic cancer risk and outcome
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (1), 251-257 (2010)
   PUBMED   20056645
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 718)
  AUTHORS   Pilyugin,M., Demmers,J., Verrijzer,C.P., Karch,F. and Moshkin,Y.M.
  TITLE     Phosphorylation-mediated control of histone chaperone ASF1 levels
            by Tousled-like kinases
  JOURNAL   PLoS One 4 (12), e8328 (2009)
   PUBMED   20016786
  REMARK    GeneRIF: ASF1 cellular levels are tightly controlled by distinct
            pathways and provide a molecular mechanism for post-translational
            regulation of dASF1 and hASF1a by TLK kinases.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 718)
  AUTHORS   Groth,A., Lukas,J., Nigg,E.A., Sillje,H.H., Wernstedt,C., Bartek,J.
            and Hansen,K.
  TITLE     Human Tousled like kinases are targeted by an ATM- and
            Chk1-dependent DNA damage checkpoint
  JOURNAL   EMBO J 22 (7), 1676-1687 (2003)
   PUBMED   12660173
REFERENCE   7  (residues 1 to 718)
  AUTHORS   Sillje,H.H. and Nigg,E.A.
  TITLE     Identification of human Asf1 chromatin assembly factors as
            substrates of Tousled-like kinases
  JOURNAL   Curr Biol 11 (13), 1068-1073 (2001)
   PUBMED   11470414
REFERENCE   8  (residues 1 to 718)
  AUTHORS   Sillje,H.H., Takahashi,K., Tanaka,K., Van Houwe,G. and Nigg,E.A.
  TITLE     Mammalian homologues of the plant Tousled gene code for
            cell-cycle-regulated kinases with maximal activities linked to
            ongoing DNA replication
  JOURNAL   EMBO J 18 (20), 5691-5702 (1999)
   PUBMED   10523312
REFERENCE   9  (residues 1 to 718)
  AUTHORS   Zhang,S., Xing,H. and Muslin,A.J.
  TITLE     Nuclear localization of protein kinase U-alpha is regulated by
            14-3-3
  JOURNAL   J Biol Chem 274 (35), 24865-24872 (1999)
   PUBMED   10455159
REFERENCE   10 (residues 1 to 718)
  AUTHORS   Yamakawa,A., Kameoka,Y., Hashimoto,K., Yoshitake,Y., Nishikawa,K.,
            Tanihara,K. and Date,T.
  TITLE     cDNA cloning and chromosomal mapping of genes encoding novel
            protein kinases termed PKU-alpha and PKU-beta, which have nuclear
            localization signal
  JOURNAL   Gene 202 (1-2), 193-201 (1997)
   PUBMED   9427565
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK300586.1, AC008026.7,
            AC080038.5, BX647225.1 and BM668399.1.
            
            Summary: This gene encodes a nuclear serine/threonine kinase that
            was first identified in Arabidopsis. The encoded protein is thought
            to function in the regulation of chromatin assembly in the S phase
            of the cell cycle by regulating the levels of a histone H3/H4
            chaperone. This protein is associated with double-strand break
            repair of DNA damage caused by radiation. Pseudogenes of this gene
            are present on chromosomes 10 and 17. Alternate splicing results in
            multiple transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (B) differs in the 5' UTR and
            lacks two alternate in-frame exons in the coding region compared to
            variant C. The encoded protein (isoform B) is shorter than isoform
            C.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300586.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..718
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.2"
     Protein         1..718
                     /product="serine/threonine-protein kinase tousled-like 2
                     isoform B"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase tousled-like 2"
                     /calculated_mol_wt=82217
     Region          139..>378
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          401..709
                     /region_name="STKc_TLK2"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Tousled-Like Kinase 2; cd14041"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,499,538,540,
                     542..543,545,559,562,585..588)
                     /site_type="active"
                     /db_xref="CDD:270943"
     Site            order(414..418,422,435,437,473,490..493,497,538,540,
                     542..543,545,559)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270943"
     Site            order(418,497,499,538,540,542,562,585..588)
                     /site_type="other"
                     /note="polypeptide substrate binding site"
                     /db_xref="CDD:270943"
     Site            order(558..564,585..588)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270943"
     CDS             1..718
                     /gene="TLK2"
                     /gene_synonym="HsHPK; MRD57; PKU-ALPHA"
                     /coded_by="NM_001284363.1:26..2182"
                     /note="isoform B is encoded by transcript variant B"
                     /db_xref="CCDS:CCDS45753.1"
                     /db_xref="GeneID:11011"
                     /db_xref="HGNC:HGNC:11842"
                     /db_xref="MIM:608439"
ORIGIN      
        1 mmeelhsldp rrqellearf tgvgvskgpl nsessnqslc svgslsdkev etpekkqndq
       61 rnrkrkaepy etsqgkgtpr ghkisdyfer rveqplygld gsaakeatee qsalptlmsv
      121 mlakprldte qlaqrgaglc ftfvsaqqns psstgsgnte hscssqkqis iqhrqtqsdl
      181 tiekisalen sknsdlekke griddllran cdlrrqideq qkmlekyker lnrcvtmskk
      241 lliekskqek macrdksmqd rlrlghfttv rhgasfteqw tdgyafqnli kqqerinsqr
      301 eeierqrkml akrkppamgq appatneqkq rksktngaen etltlaeyhe qeeifklrlg
      361 hlkkeeaeiq aelerlervr nlhirelkri hnednsqfkd hptlndryll lhllgrggfs
      421 evykafdlte qryvavkihq lnknwrdekk enyhkhacre yrihkeldhp rivklydyfs
      481 ldtdsfctvl eycegndldf ylkqhklmse kearsiimqi vnalkylnei kppiihydlk
      541 pgnillvngt acgeikitdf glskimddds ynsvdgmelt sqgagtywyl ppecfvvgke
      601 ppkisnkvdv wsvgvifyqc lygrkpfghn qsqqdilqen tilkatevqf ppkpvvtpea
      661 kafirrclay rkedridvqq lacdpyllph irksvstssp agaaiastsg asnnsssn
//
LOCUS       NP_001274367             379 aa            linear   PRI 20-NOV-2025
DEFINITION  protein cordon-bleu isoform c [Homo sapiens].
ACCESSION   NP_001274367
VERSION     NP_001274367.1
DBSOURCE    REFSEQ: accession NM_001287438.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Abdul Majeed,S., Dunzendorfer,H., Weiner,J., Heiker,J.T., Kiess,W.,
            Korner,A. and Landgraf,K.
  TITLE     COBL, MKX and MYOC Are Potential Regulators of Brown Adipose Tissue
            Development Associated with Obesity-Related Metabolic Dysfunction
            in Children
  JOURNAL   Int J Mol Sci 24 (4), 3085 (2023)
   PUBMED   36834493
  REMARK    GeneRIF: COBL, MKX and MYOC Are Potential Regulators of Brown
            Adipose Tissue Development Associated with Obesity-Related
            Metabolic Dysfunction in Children.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 379)
  AUTHORS   Husson,C., Renault,L., Didry,D., Pantaloni,D. and Carlier,M.F.
  TITLE     Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin
            filament assembly
  JOURNAL   Mol Cell 43 (3), 464-477 (2011)
   PUBMED   21816349
  REMARK    GeneRIF: Cordon-Bleu works as a dynamizer of actin assembly by
            combining many properties of profilin with weak filament nucleating
            and powerful filament severing activities and sequestration of
            ADP-actin, which generate oscillatory polymerization kinetics.
REFERENCE   7  (residues 1 to 379)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 379)
  AUTHORS   de Krom,M., Staal,W.G., Ophoff,R.A., Hendriks,J., Buitelaar,J.,
            Franke,B., de Jonge,M.V., Bolton,P., Collier,D., Curran,S., van
            Engeland,H. and van Ree,J.M.
  TITLE     A common variant in DRD3 receptor is associated with autism
            spectrum disorder
  JOURNAL   Biol Psychiatry 65 (7), 625-630 (2009)
   PUBMED   19058789
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 379)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
REFERENCE   10 (residues 1 to 379)
  AUTHORS   Gasca,S., Hill,D.P., Klingensmith,J. and Rossant,J.
  TITLE     Characterization of a gene trap insertion into a novel gene,
            cordon-bleu, expressed in axial structures of the gastrulating
            mouse embryo
  JOURNAL   Dev Genet 17 (2), 141-154 (1995)
   PUBMED   7586755
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC111496.1, BC094695.1 and
            DA245843.1.
            
            Summary: This gene encodes a protein that contains WH2 domains
            (WASP, Wiskott-Aldrich syndrome protein, homology domain-2) that
            interact with actin. The encoded actin regulator protein is
            required for growth and assembly of brush border microvilli that
            play a role in maintaining intestinal homeostasis. A similar
            protein in mouse functions in midbrain neural tube closure. A
            pseudogene of this gene is located on chromosome X. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (3) lacks several 3' exons but
            contains an alternate 3' terminal exon, and it thus differs in its
            3' coding region and 3' UTR, compared to variant 1. The encoded
            isoform (c) has a distinct C-terminus and is shorter than isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094695.1, SRR1803611.206621.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.1"
     Protein         1..379
                     /product="protein cordon-bleu isoform c"
                     /note="protein cordon-bleu"
                     /calculated_mol_wt=41489
     Region          1..46
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5NBX1; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          152..230
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          298..303
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZUI5; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     Region          331..336
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O75128.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75128.2)"
     CDS             1..379
                     /gene="COBL"
                     /coded_by="NM_001287438.3:177..1316"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75601.1"
                     /db_xref="GeneID:23242"
                     /db_xref="HGNC:HGNC:22199"
                     /db_xref="MIM:610317"
ORIGIN      
        1 mdaprasaak pptgrkmkar appppgkaat lhvhsdqkpp hdgalgsqqn lvrmkealra
       61 stmdvtvvlp sglekrsvln gshammdllv elclqnhlnp shhaleirss etqqplsfkp
      121 ntligtlnvh tvflkekvpe ekvkpgppkv peksvrlvvn ylrtqkavvr vspevplqni
      181 lpvicakcev spehvvllrd niageelels kslnelgike lyawdnrret frksslgnde
      241 tdkekkkflg ffkvnkrsns kgclttpnsp smhsrsltlg pslslgsisg vsvksemkkr
      301 rappppgsgp pvqdkasekv slgsqidlqk kkrrapappp pqppppspli pnrtedkeen
      361 rkstmvycca sfptqakrf
//
LOCUS       NP_775785                561 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral amino acid transporter 9 isoform 1 [Homo sapiens].
ACCESSION   NP_775785
VERSION     NP_775785.2
DBSOURCE    REFSEQ: accession NM_173514.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Jansen,R.M., Peruzzo,R., Fromm,S.A., Yokom,A.L., Zoncu,R. and
            Hurley,J.H.
  TITLE     Structural basis for FLCN RagC GAP activation in MiT-TFE
            substrate-selective mTORC1 regulation
  JOURNAL   Sci Adv 8 (37), eadd2926 (2022)
   PUBMED   36103527
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Fromm,S.A., Lawrence,R.E. and Hurley,J.H.
  TITLE     Structural mechanism for amino acid-dependent Rag GTPase nucleotide
            state switching by SLC38A9
  JOURNAL   Nat Struct Mol Biol 27 (11), 1017-1023 (2020)
   PUBMED   32868926
  REMARK    GeneRIF: Structural mechanism for amino acid-dependent Rag GTPase
            nucleotide state switching by SLC38A9.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
  REMARK    GeneRIF: SLC38A9 is a physical and functional component of the
            amino acid sensing machinery that controls the activation of mTOR
REFERENCE   7  (residues 1 to 561)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Uchiyama,K., Takagi,T., Iwamoto,Y., Kondo,N., Okayama,T.,
            Yoshida,N., Kamada,K., Katada,K., Handa,O., Ishikawa,T., Yasuda,H.,
            Sakagami,J., Konishi,H., Yagi,N., Naito,Y. and Itoh,Y.
  TITLE     New genetic biomarkers predicting azathioprine blood concentrations
            in combination therapy with 5-aminosalicylic acid
  JOURNAL   PLoS One 9 (4), e95080 (2014)
   PUBMED   24762746
  REMARK    GeneRIF: SNPs within SLC38A9 are correlated with inflammatory bowel
            disease patients' 6-thioguanine nucleotide blood concentrations.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Schioth,H.B., Roshanbin,S., Hagglund,M.G. and Fredriksson,R.
  TITLE     Evolutionary origin of amino acid transporter families SLC32, SLC36
            and SLC38 and physiological, pathological and therapeutic aspects
  JOURNAL   Mol Aspects Med 34 (2-3), 571-585 (2013)
   PUBMED   23506890
  REMARK    Review article
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Januchowski,R., Zawierucha,P., Andrzejewska,M., Rucinski,M. and
            Zabel,M.
  TITLE     Microarray-based detection and expression analysis of ABC and SLC
            transporters in drug-resistant ovarian cancer cell lines
  JOURNAL   Biomed Pharmacother 67 (3), 240-245 (2013)
   PUBMED   23462296
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC371481.1, BC066891.1, AK075190.1 and AI580489.1.
            
            On Feb 3, 2009 this sequence version replaced NP_775785.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Variants 1 6, 7 and 8 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066891.1, SRR1660803.15636.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396865.7/ ENSP00000380074.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..561
                     /product="neutral amino acid transporter 9 isoform 1"
                     /note="putative sodium-coupled neutral amino acid
                     transporter 9; up-regulated in lung cancer 11"
                     /calculated_mol_wt=63645
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          115..556
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          129..134
                     /region_name="Important for arginine binding and amino
                     acid transport. /evidence=ECO:0000250|UniProtKB:Q08BA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            199..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            284..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            310..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            395..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          444..454
                     /region_name="CARC motif.
                     /evidence=ECO:0000269|PubMed:28336668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          457..463
                     /region_name="CRAC motif.
                     /evidence=ECO:0000269|PubMed:28336668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            480..500
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            508..528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     CDS             1..561
                     /gene="SLC38A9"
                     /gene_synonym="SNAT9; URLC11"
                     /coded_by="NM_173514.4:191..1876"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3968.1"
                     /db_xref="GeneID:153129"
                     /db_xref="HGNC:HGNC:26907"
                     /db_xref="MIM:616203"
ORIGIN      
        1 manmnsdsrh lgtsevdher dpgpmniqfe psdlrskrpf cieptnivnv nhviqrvsdh
       61 asamnkrihy ysrlttpadk aliapdhvvp apeecyvysp lgsayklqsy tegygkntsl
      121 vtifmiwntm mgtsilsipw gikqagfttg mcviilmgll tlyccyrvvk srtmmfsldt
      181 tsweypdvcr hyfgsfgqws sllfslvsli gamivywvlm snflfntgkf ifnfihhind
      241 tdtilstnns npvicpsags gghpdnssmi fyandtgaqq fekwwdksrt vpfylvglll
      301 pllnfkspsf fskfnilgtv svlyliflvt fkavrlgfhl efhwfiptef fvpeirfqfp
      361 qltgvltlaf fihnciitll knnkkqennv rdlciaymlv tltylyigvl vfasfpsppl
      421 skdcieqnfl dnfpssdtls fiarifllfq mmtvypllgy larvqllghi fgdiypsifh
      481 vlilnliivg agvimacfyp niggiirysg aacglafvfi ypsliyiisl hqeerltwpk
      541 lifhvfiiil gvanlivqff m
//
LOCUS       NP_065700                389 aa            linear   PRI 20-NOV-2025
DEFINITION  chromobox protein homolog 8 [Homo sapiens].
ACCESSION   NP_065700
VERSION     NP_065700.1
DBSOURCE    REFSEQ: accession NM_020649.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Cai,X., Lv,Y., Pan,J., Cao,Z., Zhang,J., Li,Y. and Zheng,H.
  TITLE     CBX8 Promotes Epithelial-mesenchymal Transition, Migration, and
            Invasion of Lung Cancer through Wnt/beta-catenin Signaling Pathway
  JOURNAL   Curr Protein Pept Sci 25 (5), 386-393 (2024)
   PUBMED   38265409
  REMARK    GeneRIF: CBX8 Promotes Epithelial-mesenchymal Transition,
            Migration, and Invasion of Lung Cancer through Wnt/beta-catenin
            Signaling Pathway.
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Chen,H., Su,Y., Yang,L., Xi,L., Li,X., Lan,B., Liu,M. and Xuan,C.
  TITLE     CBX8 promotes lung adenocarcinoma growth and metastasis through
            transcriptional repression of CDKN2C and SCEL
  JOURNAL   J Cell Physiol 238 (11), 2710-2723 (2023)
   PUBMED   37733753
  REMARK    GeneRIF: CBX8 promotes lung adenocarcinoma growth and metastasis
            through transcriptional repression of CDKN2C and SCEL.
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Liu,Q., Li,X. and Gao,W.
  TITLE     CBX8 Promotes Cell Proliferation and Metastasis and Leads to
            Radiotherapy Tolerance of Glioma Cells
  JOURNAL   Turk Neurosurg 33 (1), 46-52 (2023)
   PUBMED   35713250
  REMARK    GeneRIF: CBX8 Promotes Cell Proliferation and Metastasis and Leads
            to Radiotherapy Tolerance of Glioma Cells.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Wu,Y., Duan,Y., Li,X., Zhao,R., Lan,B., Zhang,X., Wang,X., Chen,H.,
            Feng,S., Liu,Z., Cheng,Y., Xi,L., Wang,Y., Xue,F. and Xuan,C.
  TITLE     CBX8 Together with SET Facilitates Ovarian Carcinoma Growth and
            Metastasis by Suppressing the Transcription of SUSD2
  JOURNAL   Mol Cancer Res 20 (11), 1611-1622 (2022)
   PUBMED   35894945
  REMARK    GeneRIF: CBX8 Together with SET Facilitates Ovarian Carcinoma
            Growth and Metastasis by Suppressing the Transcription of SUSD2.
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Hemenway,C.S., de Erkenez,A.C. and Gould,G.C.
  TITLE     The polycomb protein MPc3 interacts with AF9, an MLL fusion partner
            in t(9;11)(p22;q23) acute leukemias
  JOURNAL   Oncogene 20 (29), 3798-3805 (2001)
   PUBMED   11439343
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Garcia-Cuellar,M.P., Zilles,O., Schreiner,S.A., Birke,M.,
            Winkler,T.H. and Slany,R.K.
  TITLE     The ENL moiety of the childhood leukemia-associated MLL-ENL
            oncoprotein recruits human Polycomb 3
  JOURNAL   Oncogene 20 (4), 411-419 (2001)
   PUBMED   11313972
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Bardos,J.I., Saurin,A.J., Tissot,C., Duprez,E. and Freemont,P.S.
  TITLE     HPC3 is a new human polycomb orthologue that interacts and
            associates with RING1 and Bmi1 and has transcriptional repression
            properties
  JOURNAL   J Biol Chem 275 (37), 28785-28792 (2000)
   PUBMED   10825164
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK074560.1, AF174482.1, AC100791.15 and AC105337.7.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF174482.1, BC009376.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269385.9/ ENSP00000269385.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..389
                     /product="chromobox protein homolog 8"
                     /note="chromobox homolog 8 (Pc class homolog, Drosophila);
                     Pc class 3 homolog; rectachrome 1; polycomb 3"
                     /calculated_mol_wt=43265
     Region          11..59
                     /region_name="CD_polycomb_like"
                     /note="chromodomain of polycomb and chromobox family
                     proteins; cd18627"
                     /db_xref="CDD:349277"
     Site            order(11..14,30,32..33,35,39,41..44,46..47,49..50,52..55)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349277"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9HC52.3)"
     Region          124..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Region          298..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     Region          349..381
                     /region_name="CBX7_C"
                     /note="CBX family C-terminal motif; pfam17218"
                     /db_xref="CDD:465385"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9HC52.3)"
     CDS             1..389
                     /gene="CBX8"
                     /gene_synonym="PC3; RC1"
                     /coded_by="NM_020649.3:80..1249"
                     /db_xref="CCDS:CCDS11765.1"
                     /db_xref="GeneID:57332"
                     /db_xref="HGNC:HGNC:15962"
                     /db_xref="MIM:617354"
ORIGIN      
        1 melsavgerv faaeallkrr irkgrmeylv kwkgwsqkys twepeenild arllaafeer
       61 eremelygpk krgpkpktfl lkaqakakak tyefrsdsar giripypgrs pqdlastsra
      121 reglrnmgls ppasststss tcraeaprdr drdrdrdrer drerererer ererererer
      181 gtsrvddkps spgdsskkrg pkprkelpdp sqrplgepsa glgeylkgrk lddtpsgagk
      241 fpaghsviql arrqdsdlvq cgvtspssae atgklavdtf parvikhraa fleakgqgal
      301 dpngtrvrhg sgppssgggl yrdmgaqggr psliaripva rilgdpeees wspsltnlek
      361 vvvtdvtsnf ltvtikesnt dqgffkekr
//
LOCUS       NP_001011663             350 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb group RING finger protein 6 isoform a [Homo sapiens].
ACCESSION   NP_001011663
VERSION     NP_001011663.1
DBSOURCE    REFSEQ: accession NM_001011663.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Lan,X., Ding,S., Zhang,T., Yi,Y., Li,C., Jin,W., Chen,J., Liang,K.,
            Wang,H. and Jiang,W.
  TITLE     PCGF6 controls neuroectoderm specification of human pluripotent
            stem cells by activating SOX2 expression
  JOURNAL   Nat Commun 13 (1), 4601 (2022)
   PUBMED   35933409
  REMARK    GeneRIF: PCGF6 controls neuroectoderm specification of human
            pluripotent stem cells by activating SOX2 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Deloukas,P., Earthrowl,M.E., Grafham,D.V., Rubenfield,M.,
            French,L., Steward,C.A., Sims,S.K., Jones,M.C., Searle,S.,
            Scott,C., Howe,K., Hunt,S.E., Andrews,T.D., Gilbert,J.G.,
            Swarbreck,D., Ashurst,J.L., Taylor,A., Battles,J., Bird,C.P.,
            Ainscough,R., Almeida,J.P., Ashwell,R.I., Ambrose,K.D.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Bates,K.,
            Beasley,H., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.C.,
            Burrill,W., Burton,J., Cahill,P., Camire,D., Carter,N.P.,
            Chapman,J.C., Clark,S.Y., Clarke,G., Clee,C.M., Clegg,S., Corby,N.,
            Coulson,A., Dhami,P., Dutta,I., Dunn,M., Faulkner,L., Frankish,A.,
            Frankland,J.A., Garner,P., Garnett,J., Gribble,S., Griffiths,C.,
            Grocock,R., Gustafson,E., Hammond,S., Harley,J.L., Hart,E.,
            Heath,P.D., Ho,T.P., Hopkins,B., Horne,J., Howden,P.J., Huckle,E.,
            Hynds,C., Johnson,C., Johnson,D., Kana,A., Kay,M., Kimberley,A.M.,
            Kershaw,J.K., Kokkinaki,M., Laird,G.K., Lawlor,S., Lee,H.M.,
            Leongamornlert,D.A., Laird,G., Lloyd,C., Lloyd,D.M., Loveland,J.,
            Lovell,J., McLaren,S., McLay,K.E., McMurray,A.,
            Mashreghi-Mohammadi,M., Matthews,L., Milne,S., Nickerson,T.,
            Nguyen,M., Overton-Larty,E., Palmer,S.A., Pearce,A.V., Peck,A.I.,
            Pelan,S., Phillimore,B., Porter,K., Rice,C.M., Rogosin,A.,
            Ross,M.T., Sarafidou,T., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Standring,L., Sycamore,N., Tester,J., Thorpe,A.,
            Torcasso,W., Tracey,A., Tromans,A., Tsolas,J., Wall,M., Walsh,J.,
            Wang,H., Weinstock,K., West,A.P., Willey,D.L., Whitehead,S.L.,
            Wilming,L., Wray,P.W., Young,L., Chen,Y., Lovering,R.C.,
            Moschonas,N.K., Siebert,R., Fechtel,K., Bentley,D., Durbin,R.,
            Hubbard,T., Doucette-Stamm,L., Beck,S., Smith,D.R. and Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 10
  JOURNAL   Nature 429 (6990), 375-381 (2004)
   PUBMED   15164054
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Suzuki,M., Mizutani-Koseki,Y., Fujimura,Y., Miyagishima,H.,
            Kaneko,T., Takada,Y., Akasaka,T., Tanzawa,H., Takihara,Y.,
            Nakano,M., Masumoto,H., Vidal,M., Isono,K. and Koseki,H.
  TITLE     Involvement of the Polycomb-group gene Ring1B in the specification
            of the anterior-posterior axis in mice
  JOURNAL   Development 129 (18), 4171-4183 (2002)
   PUBMED   12183370
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Akasaka,T., Takahashi,N., Suzuki,M., Koseki,H., Bodmer,R. and
            Koga,H.
  TITLE     MBLR, a new RING finger protein resembling mammalian Polycomb gene
            products, is regulated by cell cycle-dependent phosphorylation
  JOURNAL   Genes Cells 7 (8), 835-850 (2002)
   PUBMED   12167161
  REMARK    GeneRIF: regulation by cell cycle-dependent phosphorylation
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Trimarchi,J.M., Fairchild,B., Wen,J. and Lees,J.A.
  TITLE     The E2F6 transcription factor is a component of the mammalian
            Bmi1-containing polycomb complex
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 1519-1524 (2001)
   PUBMED   11171983
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Kanno,M., Hasegawa,M., Ishida,A., Isono,K. and Taniguchi,M.
  TITLE     mel-18, a Polycomb group-related mammalian gene, encodes a
            transcriptional negative regulator with tumor suppressive activity
  JOURNAL   EMBO J 14 (22), 5672-5678 (1995)
   PUBMED   8521824
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591408.19, BC010235.1 and
            BC007602.1.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif, which is most closely related to those of polycomb group
            (PcG) proteins RNF110/MEL-18 and BMI1. PcG proteins are known to
            form protein complexes and function as transcription repressors.
            This protein has been shown to interact with some PcG proteins and
            act as a transcription repressor. The activity of this protein is
            found to be regulated by cell cycle dependent phosphorylation.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and   encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC010235.1, SRR1660809.187491.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369847.4/ ENSP00000358862.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.33"
     Protein         1..350
                     /product="polycomb group RING finger protein 6 isoform a"
                     /note="ring finger protein 134; Mel18 and Bmi1-like RING
                     finger protein; polycomb group RING finger protein 6"
                     /calculated_mol_wt=38916
     Region          1..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BYE7.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12167161; propagated from
                     UniProtKB/Swiss-Prot (Q9BYE7.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BYE7.2)"
     Region          125..215
                     /region_name="RING-HC_PCGF5"
                     /note="RING finger found in polycomb group RING finger
                     protein 5 (PCGF5) and similar proteins; cd16737"
                     /db_xref="CDD:438395"
     Site            order(125..129,131,137,139..140,142..143,145..146,
                     148..151,155..157,160..161,180,182..183,185..188,190..191,
                     193..194,197..198,200,202,205..206,209..210,213..214)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438395"
     Region          252..341
                     /region_name="RAWUL_PCGF6"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     6 (PCGF6) and similar proteins; cd17085"
                     /db_xref="CDD:340605"
     CDS             1..350
                     /gene="PCGF6"
                     /gene_synonym="MBLR; RNF134"
                     /coded_by="NM_001011663.2:75..1127"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31275.1"
                     /db_xref="GeneID:84108"
                     /db_xref="HGNC:HGNC:21156"
                     /db_xref="MIM:607816"
ORIGIN      
        1 megvavvtag svgaaktega aalpppppvs ppaltpapaa geegpaplse tgapgcsgsr
       61 ppelepersl grfrgrfede deeleeeeel eeeeeeeeed mshfslrleg grqdsedeee
      121 rlinlseltp yilcsickgy lidattitec lhtfcksciv rhfyysnrcp kcnivvhqtq
      181 plynirldrq lqdivyklvi nleerekkqm hdfykergle vpkpavpqpv psskgrskkv
      241 lesvfrippe ldmslllefi ganegtghfk plekkfvrvs geatighvek flrrkmgldp
      301 acqvdiicgd hlleqyqtlr eirraigdaa mqdgllvlhy glvvsplkit
//
LOCUS       NP_009096                464 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3A subunit 2 [Homo sapiens].
ACCESSION   NP_009096
VERSION     NP_009096.2
DBSOURCE    REFSEQ: accession NM_007165.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Tholen,J., Razew,M., Weis,F. and Galej,W.P.
  TITLE     Structural basis of branch site recognition by the human
            spliceosome
  JOURNAL   Science 375 (6576), 50-57 (2022)
   PUBMED   34822310
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Moraitou,M., Patrinou-Georgoula,M. and Guialis,A.
  TITLE     Structural/functional properties of a mammalian multi-component
            structure containing all major spliceosomal small nuclear
            ribonucleoprotein particles
  JOURNAL   Biochem J 332 (Pt 1) (Pt 1), 135-144 (1998)
   PUBMED   9576861
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Hong,W., Bennett,M., Xiao,Y., Feld Kramer,R., Wang,C. and Reed,R.
  TITLE     Association of U2 snRNP with the spliceosomal complex E
  JOURNAL   Nucleic Acids Res 25 (2), 354-361 (1997)
   PUBMED   9016565
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Rain,J.C., Tartakoff,A.M., Kramer,A. and Legrain,P.
  TITLE     Essential domains of the PRP21 splicing factor are implicated in
            the binding to PRP9 and PRP11 proteins and are conserved through
            evolution
  JOURNAL   RNA 2 (6), 535-550 (1996)
   PUBMED   8718683
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Dresser,D.W., Hacker,A., Lovell-Badge,R. and Guerrier,D.
  TITLE     The genes for a spliceosome protein (SAP62) and the anti-Mullerian
            hormone (AMH) are contiguous
  JOURNAL   Hum Mol Genet 4 (9), 1613-1618 (1995)
   PUBMED   8541848
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Bennett,M. and Reed,R.
  TITLE     Correspondence between a mammalian spliceosome component and an
            essential yeast splicing factor
  JOURNAL   Science 262 (5130), 105-108 (1993)
   PUBMED   8211113
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG325385.1, BC015804.1 and
            BC009903.2.
            
            On Jun 10, 2002 this sequence version replaced NP_009096.1.
            
            Summary: This gene encodes subunit 2 of the splicing factor 3a
            protein complex. The splicing factor 3a heterotrimer includes
            subunits 1, 2 and 3 and is necessary for the in vitro conversion of
            15S U2 snRNP into an active 17S particle that performs pre-mRNA
            splicing. Subunit 2 interacts with subunit 1 through its
            amino-terminus while the single zinc finger domain of subunit 2
            plays a role in its binding to the 15S U2 snRNP. Subunit 2 may also
            function independently of its RNA splicing function as a
            microtubule-binding protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009903.2, SRR3476690.238362.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221494.10/ ENSP00000221494.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..464
                     /product="splicing factor 3A subunit 2"
                     /note="pre-mRNA splicing factor SF3A, subunit 2; splicing
                     factor 3a, subunit 2, 66kD; spliceosome associated protein
                     62; SAP 62; splicing factor 3a, subunit 2, 66kDa"
                     /calculated_mol_wt=49125
     Region          1..217
                     /region_name="PRP11"
                     /note="Splicing factor 3a, subunit 2 [RNA processing and
                     modification]; COG5246"
                     /db_xref="CDD:227571"
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15428.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (Q15428.2)"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q62203; propagated from
                     UniProtKB/Swiss-Prot (Q15428.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15428.2)"
     Region          217..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15428.2)"
     Region          <302..>427
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     CDS             1..464
                     /gene="SF3A2"
                     /gene_synonym="PRP11; PRPF11; SAP62; SF3a66"
                     /coded_by="NM_007165.5:116..1510"
                     /db_xref="CCDS:CCDS12084.1"
                     /db_xref="GeneID:8175"
                     /db_xref="HGNC:HGNC:10766"
                     /db_xref="MIM:600796"
ORIGIN      
        1 mdfqhrpggk tgsggvasss esnrdrrerl rqlaletidi nkdpyfmknh lgsyecklcl
       61 tlhnnegsyl ahtqgkkhqt nlarraakea keapaqpape kvkvevkkfv kigrpgykvt
      121 kqrdsemgqq sllfqidype iaegimprhr fmsayeqrie ppdrrwqyll maaepyetia
      181 fkvpsreidk aegkfwthwn retkqfflqf hfkmekppap pslpagppgv krpppplmng
      241 lpprpplpes lpppppgglp lppmpptgpa psgppgppql pppapgvhpp apvvhppasg
      301 vhppapgvhp papgvhppap gvhpptsgvh ppapgvhppa pgvhppapgv hppapgvhpp
      361 apgvhpppsa gvhpqapgvh paapavhpqa pgvhppapgm hpqapgvhpq ppgvhpsapg
      421 vhpqppgvhp snpgvhpptp mppmlrpplp segpgnippp pptn
//
LOCUS       NP_001315548             501 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 5
            isoform 1 [Homo sapiens].
ACCESSION   NP_001315548 XP_016857628
VERSION     NP_001315548.1
DBSOURCE    REFSEQ: accession NM_001328619.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Song,A., Mao,Y. and Wei,H.
  TITLE     GLUT5: structure, functions, diseases and potential applications
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1519-1538 (2023)
   PUBMED   37674366
  REMARK    GeneRIF: GLUT5: structure, functions, diseases and potential
            applications.
            Review article
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Cui,Y., Liu,H., Wang,Z., Zhang,H., Tian,J., Wang,Z., Song,W.,
            Guo,H., Liu,L., Tian,R., Zuo,X., Ren,S., Zhang,F. and Niu,R.
  TITLE     Fructose promotes angiogenesis by improving vascular endothelial
            cell function and upregulating VEGF expression in cancer cells
  JOURNAL   J Exp Clin Cancer Res 42 (1), 184 (2023)
   PUBMED   37507736
  REMARK    GeneRIF: Fructose promotes angiogenesis by improving vascular
            endothelial cell function and upregulating VEGF expression in
            cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Fiorentino,T.V., De Vito,F., Suraci,E., Marasco,R., Hribal,M.L.,
            Luzza,F. and Sesti,G.
  TITLE     Obesity and overweight are linked to increased sodium-glucose
            cotransporter 1 and glucose transporter 5 levels in duodenum
  JOURNAL   Obesity (Silver Spring) 31 (3), 724-731 (2023)
   PUBMED   36746764
  REMARK    GeneRIF: Obesity and overweight are linked to increased
            sodium-glucose cotransporter 1 and glucose transporter 5 levels in
            duodenum.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Taneva,I., Grumann,D., Schmidt,D., Taneva,E., von Arnim,U.,
            Ansorge,T. and Wex,T.
  TITLE     Gene variants of the SLC2A5 gene encoding GLUT5, the major fructose
            transporter, do not contribute to clinical presentation of acquired
            fructose malabsorption
  JOURNAL   BMC Gastroenterol 22 (1), 167 (2022)
   PUBMED   35387598
  REMARK    GeneRIF: Gene variants of the SLC2A5 gene encoding GLUT5, the major
            fructose transporter, do not contribute to clinical presentation of
            acquired fructose malabsorption.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Mahraoui,L., Takeda,J., Mesonero,J., Chantret,I., Dussaulx,E.,
            Bell,G.I. and Brot-Laroche,E.
  TITLE     Regulation of expression of the human fructose transporter (GLUT5)
            by cyclic AMP
  JOURNAL   Biochem J 301 (Pt 1) (Pt 1), 169-175 (1994)
   PUBMED   8037665
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Rand,E.B., Depaoli,A.M., Davidson,N.O., Bell,G.I. and Burant,C.F.
  TITLE     Sequence, tissue distribution, and functional characterization of
            the rat fructose transporter GLUT5
  JOURNAL   Am J Physiol 264 (6 Pt 1), G1169-G1176 (1993)
   PUBMED   8333543
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Burant,C.F., Takeda,J., Brot-Laroche,E., Bell,G.I. and
            Davidson,N.O.
  TITLE     Fructose transporter in human spermatozoa and small intestine is
            GLUT5
  JOURNAL   J Biol Chem 267 (21), 14523-14526 (1992)
   PUBMED   1634504
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Davidson,N.O., Hausman,A.M., Ifkovits,C.A., Buse,J.B., Gould,G.W.,
            Burant,C.F. and Bell,G.I.
  TITLE     Human intestinal glucose transporter expression and localization of
            GLUT5
  JOURNAL   Am J Physiol 262 (3 Pt 1), C795-C800 (1992)
   PUBMED   1550217
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Kayano,T., Burant,C.F., Fukumoto,H., Gould,G.W., Fan,Y.S.,
            Eddy,R.L., Byers,M.G., Shows,T.B., Seino,S. and Bell,G.I.
  TITLE     Human facilitative glucose transporters. Isolation, functional
            characterization, and gene localization of cDNAs encoding an
            isoform (GLUT5) expressed in small intestine, kidney, muscle, and
            adipose tissue and an unusual glucose transporter pseudogene-like
            sequence (GLUT6)
  JOURNAL   J Biol Chem 265 (22), 13276-13282 (1990)
   PUBMED   1695905
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158048.35.
            
            On Jun 22, 2016 this sequence version replaced XP_016857628.1.
            
            Summary: The protein encoded by this gene is a fructose transporter
            responsible for fructose uptake by the small intestine. The encoded
            protein also is necessary for the increase in blood pressure due to
            high dietary fructose consumption. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 both encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.3424929.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..501
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 5 isoform 1"
                     /note="glucose transporter-like protein 5; glucose
                     transporter type 5, small intestine; solute carrier family
                     2 (facilitated glucose/fructose transporter), member 5;
                     testicular tissue protein Li 81"
                     /calculated_mol_wt=54843
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P22732.1)"
     Site            19..39
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Region          23..471
                     /region_name="MFS_GLUT_Class2"
                     /note="Class 2 Glucose transporters (GLUTs) of the Major
                     Facilitator Superfamily; cd17432"
                     /db_xref="CDD:340990"
     Site            order(32,36,167,170..171,174,288..289,293..294,297..298,
                     325,387..388,391..392,396,419..420,423)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:340990"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22732.1)"
     Site            69..91
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            127..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            162..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            278..298
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            343..363
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            372..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            413..433
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     Site            440..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22732.1)"
     CDS             1..501
                     /gene="SLC2A5"
                     /gene_synonym="GLUT-5; GLUT5"
                     /coded_by="NM_001328619.2:270..1775"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS99.1"
                     /db_xref="GeneID:6518"
                     /db_xref="HGNC:HGNC:11010"
                     /db_xref="MIM:138230"
ORIGIN      
        1 meqqdqsmke grltlvlala tliaafgssf qygynvaavn spallmqqfy netyygrtge
       61 fmedfpltll wsvtvsmfpf ggfigsllvg plvnkfgrkg allfnnifsi vpailmgcsr
      121 vatsfeliii srllvgicag vssnvvpmyl gelapknlrg algvvpqlfi tvgilvaqif
      181 glrnllanvd gwpillgltg vpaalqllll pffpespryl liqkkdeaaa kkalqtlrgw
      241 dsvdrevaei rqedeaekaa gfisvlklfr mrslrwqlls iivlmggqql sgvnaiyyya
      301 dqiylsagvp eehvqyvtag tgavnvvmtf cavfvvellg rrlllllgfs icliaccvlt
      361 aalalqdtvs wmpyisivcv isyvighalg pspipallit eiflqssrps afmvggsvhw
      421 lsnftvglif pfiqeglgpy sfivfavicl lttiyifliv petkaktfie inqiftkmnk
      481 vsevypekee lkelppvtse q
//
LOCUS       NP_001136430             510 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 15 isoform 2 [Homo sapiens].
ACCESSION   NP_001136430
VERSION     NP_001136430.1
DBSOURCE    REFSEQ: accession NM_001142958.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Zhao,Y., Shim,N., Cui,Y.H., Kang,J.H., Yoo,K.C., Kim,S., Yi,J.M.,
            Kim,M.J., Yoon,J.H. and Lee,S.J.
  TITLE     FBXO15 plays a critical suppressive functional role in regulation
            of breast cancer progression
  JOURNAL   Signal Transduct Target Ther 6 (1), 211 (2021)
   PUBMED   34083507
  REMARK    GeneRIF: FBXO15 plays a critical suppressive functional role in
            regulation of breast cancer progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Zeng,Z., Feingold,E., Wang,X., Weeks,D.E., Lee,M., Cuenco,D.T.,
            Broffitt,B., Weyant,R.J., Crout,R., McNeil,D.W., Levy,S.M.,
            Marazita,M.L. and Shaffer,J.R.
  TITLE     Genome-wide association study of primary dentition pit-and-fissure
            and smooth surface caries
  JOURNAL   Caries Res 48 (4), 330-338 (2014)
   PUBMED   24556642
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Simino,J., Sung,Y.J., Kume,R., Schwander,K. and Rao,D.C.
  TITLE     Gene-alcohol interactions identify several novel blood pressure
            loci including a promising locus near SLC16A9
  JOURNAL   Front Genet 4, 277 (2013)
   PUBMED   24376456
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Porcu,E., Medici,M., Pistis,G., Volpato,C.B., Wilson,S.G.,
            Cappola,A.R., Bos,S.D., Deelen,J., den Heijer,M., Freathy,R.M.,
            Lahti,J., Liu,C., Lopez,L.M., Nolte,I.M., O'Connell,J.R.,
            Tanaka,T., Trompet,S., Arnold,A., Bandinelli,S., Beekman,M.,
            Bohringer,S., Brown,S.J., Buckley,B.M., Camaschella,C., de
            Craen,A.J., Davies,G., de Visser,M.C., Ford,I., Forsen,T.,
            Frayling,T.M., Fugazzola,L., Gogele,M., Hattersley,A.T.,
            Hermus,A.R., Hofman,A., Houwing-Duistermaat,J.J., Jensen,R.A.,
            Kajantie,E., Kloppenburg,M., Lim,E.M., Masciullo,C., Mariotti,S.,
            Minelli,C., Mitchell,B.D., Nagaraja,R., Netea-Maier,R.T.,
            Palotie,A., Persani,L., Piras,M.G., Psaty,B.M., Raikkonen,K.,
            Richards,J.B., Rivadeneira,F., Sala,C., Sabra,M.M., Sattar,N.,
            Shields,B.M., Soranzo,N., Starr,J.M., Stott,D.J., Sweep,F.C.,
            Usala,G., van der Klauw,M.M., van Heemst,D., van Mullem,A.,
            Vermeulen,S.H., Visser,W.E., Walsh,J.P., Westendorp,R.G., Widen,E.,
            Zhai,G., Cucca,F., Deary,I.J., Eriksson,J.G., Ferrucci,L.,
            Fox,C.S., Jukema,J.W., Kiemeney,L.A., Pramstaller,P.P.,
            Schlessinger,D., Shuldiner,A.R., Slagboom,E.P., Uitterlinden,A.G.,
            Vaidya,B., Visser,T.J., Wolffenbuttel,B.H., Meulenbelt,I.,
            Rotter,J.I., Spector,T.D., Hicks,A.A., Toniolo,D., Sanna,S.,
            Peeters,R.P. and Naitza,S.
  TITLE     A meta-analysis of thyroid-related traits reveals novel loci and
            gender-specific differences in the regulation of thyroid function
  JOURNAL   PLoS Genet 9 (2), e1003266 (2013)
   PUBMED   23408906
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Tokuzawa,Y., Kaiho,E., Maruyama,M., Takahashi,K., Mitsui,K.,
            Maeda,M., Niwa,H. and Yamanaka,S.
  TITLE     Fbx15 is a novel target of Oct3/4 but is dispensable for embryonic
            stem cell self-renewal and mouse development
  JOURNAL   Mol Cell Biol 23 (8), 2699-2708 (2003)
   PUBMED   12665572
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB447209.1, AK094215.1 and
            BU729305.1.
            
            Summary: Members of the F-box protein family, such as FBXO15, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding region, and uses an upstream start codon, compared to
            variant 1. The resulting protein (isoform 2) is longer and has a
            distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK094215.1, SRR5189667.252465.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000419743.7/ ENSP00000393154.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.3"
     Protein         1..510
                     /product="F-box only protein 15 isoform 2"
                     /note="F-box only protein 15"
                     /calculated_mol_wt=57127
     Region          74..119
                     /region_name="F-box_FBXO15"
                     /note="F-box domain found in F-box only protein 15
                     (FBXO15) and similar proteins; cd22093"
                     /db_xref="CDD:438865"
     Site            order(77,81,84..85,88..89,93,95..96,100..102,104)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438865"
     CDS             1..510
                     /gene="FBXO15"
                     /gene_synonym="FBX15"
                     /coded_by="NM_001142958.2:50..1582"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45884.1"
                     /db_xref="GeneID:201456"
                     /db_xref="HGNC:HGNC:13617"
                     /db_xref="MIM:609093"
ORIGIN      
        1 matgrgrilq qhwlglqtlr gpsrgggaar grarafgcrk gpgvklsags aalrchaggg
       61 qhwessfscc sgfldgmpse illkifsyld avsllctgcv srrfyhland nfiwigiyst
      121 afsparsnwk fnsvekiams msflsvqdke agywkkeyit kqiasvkaal adilkpvnpy
      181 tglpvktkea lrifglgwai ilkekggkey imehvdlsin dtsvtviwyg kkwpclasls
      241 tldlcgmtpv ftdwyktptk hrlrwhslia kynlshltis tmigcdrlir ifclhpgllv
      301 gvwkkeeela fvmanlhfhh lverstlgsa tipyelpphs pflddspeyg lhgyqlhvdl
      361 hsggvfylcg tfrnlftkrg nienghvkli vihlknnreh lpligkvgls wktdifdgci
      421 kscsmmdvtl ldehgkpfwc fsspvclrsp atpsdsssfl gqtynvdyvd aegrvhvelv
      481 wireteeyli vnlvlylsia kinhwfgtey
//
LOCUS       NP_061977                246 aa            linear   PRI 20-NOV-2025
DEFINITION  protein lin-37 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_061977
VERSION     NP_061977.1
DBSOURCE    REFSEQ: accession NM_019104.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Uxa,S., Bernhart,S.H., Mages,C.F.S., Fischer,M., Kohler,R.,
            Hoffmann,S., Stadler,P.F., Engeland,K. and Muller,G.A.
  TITLE     DREAM and RB cooperate to induce gene repression and cell-cycle
            arrest in response to p53 activation
  JOURNAL   Nucleic Acids Res 47 (17), 9087-9103 (2019)
   PUBMED   31400114
  REMARK    GeneRIF: Abrogation of DREAM function by knockout of the DREAM
            component LIN37 results in a reduced repression of cell-cycle
            genes.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Sadasivam,S. and DeCaprio,J.A.
  TITLE     The DREAM complex: master coordinator of cell cycle-dependent gene
            expression
  JOURNAL   Nat Rev Cancer 13 (8), 585-595 (2013)
   PUBMED   23842645
  REMARK    Review article
            Erratum:[Nat Rev Cancer. 2013 Oct;13(10):752]
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Sadasivam,S., Duan,S. and DeCaprio,J.A.
  TITLE     The MuvB complex sequentially recruits B-Myb and FoxM1 to promote
            mitotic gene expression
  JOURNAL   Genes Dev 26 (5), 474-489 (2012)
   PUBMED   22391450
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Litovchick,L., Florens,L.A., Swanson,S.K., Washburn,M.P. and
            DeCaprio,J.A.
  TITLE     DYRK1A protein kinase promotes quiescence and senescence through
            DREAM complex assembly
  JOURNAL   Genes Dev 25 (8), 801-813 (2011)
   PUBMED   21498570
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Litovchick,L., Sadasivam,S., Florens,L., Zhu,X., Swanson,S.K.,
            Velmurugan,S., Chen,R., Washburn,M.P., Liu,X.S. and DeCaprio,J.A.
  TITLE     Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
            complex represses human cell cycle-dependent genes in quiescence
  JOURNAL   Mol Cell 26 (4), 539-551 (2007)
   PUBMED   17531812
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC396639.1, CB152701.1 and BC009071.1.
            
            Summary: This gene encodes a protein expressed in the eye.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.24306.1,
                                           SRR5189667.57993.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301159.14/ ENSP00000301159.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..246
                     /product="protein lin-37 homolog isoform 1"
                     /note="protein F25965; protein lin-37 homolog;
                     antolefinin"
                     /calculated_mol_wt=28252
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96GY3.1)"
     Region          37..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GY3.1)"
     Region          84..240
                     /region_name="LIN37"
                     /note="pfam15306"
                     /db_xref="CDD:464632"
     Region          129..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GY3.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D8N6; propagated from
                     UniProtKB/Swiss-Prot (Q96GY3.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96GY3.1)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (Q96GY3.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q96GY3.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96GY3.1)"
     CDS             1..246
                     /gene="LIN37"
                     /gene_synonym="F25965; lin-37; ZK418.4"
                     /coded_by="NM_019104.3:150..890"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS62642.1"
                     /db_xref="GeneID:55957"
                     /db_xref="HGNC:HGNC:33234"
                     /db_xref="MIM:621287"
ORIGIN      
        1 mfpvkvkvek selemakarn qldavlqcll ekshmdrerl deeagktpsd thnkdcsiaa
       61 tgkrpsarfp hqrrkkrrem ddglaeggpq rsntyviklf drsvdlaqfs entplypicr
      121 awmrnspsvr erecspsspl pplpedeegs evtnsksrdv yklppptppg ppgdacrsri
      181 psplqpemqg tpddepsepe pspstliyrn mqrwkrirqr wkeashrnql rysesmkilr
      241 emyerq
//
LOCUS       NP_543136                309 aa            linear   PRI 20-NOV-2025
DEFINITION  radial spoke head 1 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_543136
VERSION     NP_543136.1
DBSOURCE    REFSEQ: accession NM_080860.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Tate,G.
  TITLE     Whole-exome sequencing reveals a combination of extremely rare
            single-nucleotide polymorphism of DNAH9 and RSPH1 genes in a
            Japanese fetus with situs viscerum inversus
  JOURNAL   Med Mol Morphol 54 (3), 275-280 (2021)
   PUBMED   34008076
  REMARK    GeneRIF: Whole-exome sequencing reveals a combination of extremely
            rare single-nucleotide polymorphism of DNAH9 and RSPH1 genes in a
            Japanese fetus with situs viscerum inversus.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Blanchon,S., Legendre,M., Bottier,M., Tamalet,A., Montantin,G.,
            Collot,N., Faucon,C., Dastot,F., Copin,B., Clement,A., Filoche,M.,
            Coste,A., Amselem,S., Escudier,E., Papon,J.F. and Louis,B.
  TITLE     Deep phenotyping, including quantitative ciliary beating
            parameters, and extensive genotyping in primary ciliary dyskinesia
  JOURNAL   J Med Genet 57 (4), 237-244 (2020)
   PUBMED   31772028
  REMARK    GeneRIF: Deep phenotyping, including quantitative ciliary beating
            parameters, and extensive genotyping in primary ciliary dyskinesia.
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Shetty,J., Klotz,K.L., Wolkowicz,M.J., Flickinger,C.J. and
            Herr,J.C.
  TITLE     Radial spoke protein 44 (human meichroacidin) is an axonemal
            alloantigen of sperm and cilia
  JOURNAL   Gene 396 (1), 93-107 (2007)
   PUBMED   17451891
  REMARK    GeneRIF: Radial spoke protein 44 denotes the restricted
            localization of the protein to the radial spokes of the axonemes of
            both sperm and cilia.
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Tsuchida,J., Nishina,Y., Wakabayashi,N., Nozaki,M., Sakai,Y. and
            Nishimune,Y.
  TITLE     Molecular cloning and characterization of meichroacidin (male
            meiotic metaphase chromosome-associated acidic protein)
  JOURNAL   Dev Biol 197 (1), 67-76 (1998)
   PUBMED   9578619
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Taketo,M.M., Araki,Y., Matsunaga,A., Yokoi,A., Tsuchida,J.,
            Nishina,Y., Nozaki,M., Tanaka,H., Koga,M., Uchida,K., Matsumiya,K.,
            Okuyama,A., Rochelle,J.M., Nishimune,Y., Matsui,M. and Seldin,M.F.
  TITLE     Mapping of eight testis-specific genes to mouse chromosomes
  JOURNAL   Genomics 46 (1), 138-142 (1997)
   PUBMED   9403069
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB006536.1 and BU684013.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a male meiotic metaphase
            chromosome-associated acidic protein. This gene is expressed in
            tissues with motile cilia or flagella, including the trachea,
            lungs, airway brushings, and testes. Mutations in this gene result
            in primary ciliary dyskinesia-24. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Sep 2014].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.242360.1,
                                           SRR3476690.1003589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000291536.8/ ENSP00000291536.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..309
                     /product="radial spoke head 1 homolog isoform 1"
                     /note="testes specific gene A2 homolog; male meiotic
                     metaphase chromosome-associated acidic protein;
                     meichroacidin; cancer/testis antigen 79; testis specific
                     A2 homolog; radial spoke head 1 homolog"
                     /calculated_mol_wt=34993
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          <15..176
                     /region_name="COG4642"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:443680"
     Region          20..43
                     /region_name="MORN 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          44..66
                     /region_name="MORN 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          67..89
                     /region_name="MORN 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          90..112
                     /region_name="MORN 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          113..135
                     /region_name="MORN 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          159..181
                     /region_name="MORN 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     Region          222..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WYR4.1)"
     CDS             1..309
                     /gene="RSPH1"
                     /gene_synonym="CT79; RSP44; RSPH10A; TSA2; TSGA2"
                     /coded_by="NM_080860.4:39..968"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13688.1"
                     /db_xref="GeneID:89765"
                     /db_xref="HGNC:HGNC:12371"
                     /db_xref="MIM:609314"
ORIGIN      
        1 msdlgseele eegendigey eggrneager hgrgrarlpn gdtyegsyef gkrhgqgiyk
       61 fkngaryige yvrnkkhgqg tfiypdgsry egewandlrh ghgvyyyinn dtytgewfah
      121 qrhgqgtyly aetgskyvgt wvngqqegta elihlnhryq gkflnknpvg pgkyvfdvgc
      181 eqhgeyrltd mergeeeeee elvtvvpkwk atqitelalw tptlpkkpts tdgpgqdapg
      241 aesagepgee aqallegfeg emdmrpgded advlreesre ydqeefrydm degninseee
      301 etrqsdlqd
//
LOCUS       NP_001354684             371 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform l [Homo sapiens].
ACCESSION   NP_001354684
VERSION     NP_001354684.1
DBSOURCE    REFSEQ: accession NM_001367755.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 371)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 371)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 371)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 371)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 371)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 371)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 371)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 371)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 371)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 371)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.236220.1,
                                           SRR1660807.191153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..371
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..371
                     /product="rab5 GDP/GTP exchange factor isoform l"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=43324
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..359
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..371
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367755.1:78..1193"
                     /note="isoform l is encoded by transcript variant 39"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlr
      361 wflprlfprl v
//
LOCUS       NP_001307565             230 aa            linear   PRI 20-NOV-2025
DEFINITION  aquaporin-9 isoform 3 [Homo sapiens].
ACCESSION   NP_001307565
VERSION     NP_001307565.1
DBSOURCE    REFSEQ: accession NM_001320636.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Thon,P., Rahmel,T., Ziehe,D., Palmowski,L., Marko,B., Nowak,H.,
            Wolf,A., Witowski,A., Orlowski,J., Ellger,B., Wappler,F.,
            Schwier,E., Henzler,D., Kohler,T., Zarbock,A., Ehrentraut,S.F.,
            Putensen,C., Frey,U.H., Anft,M., Babel,N., Sitek,B., Adamzik,M.,
            Bergmann,L., Unterberg,M., Koos,B. and Rump,K.
  CONSRTM   SepsisDataNet.NRW Research Group
  TITLE     AQP3 and AQP9-Contrary Players in Sepsis?
  JOURNAL   Int J Mol Sci 25 (2), 1209 (2024)
   PUBMED   38279209
  REMARK    GeneRIF: AQP3 and AQP9-Contrary Players in Sepsis?
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Dong,Y., Li,J., Cao,D., Zhong,J., Liu,X., Duan,Y.G., Lee,K.F.,
            Yeung,W.S.B., Lee,C.L. and Chiu,P.C.N.
  TITLE     Integrated MicroRNA and Secretome Analysis of Human Endometrial
            Organoids Reveal the miR-3194-5p/Aquaporin/S100A9 Module in
            Regulating Trophoblast Functions
  JOURNAL   Mol Cell Proteomics 22 (4), 100526 (2023)
   PUBMED   36889440
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Olmez,F., Oglak,S.C. and Can,E.
  TITLE     The Implication of Aquaporin-9 in the Pathogenesis of Preterm
            Premature Rupture of Membranes
  JOURNAL   Z Geburtshilfe Neonatol 226 (4), 233-239 (2022)
   PUBMED   35508193
  REMARK    GeneRIF: The Implication of Aquaporin-9 in the Pathogenesis of
            Preterm Premature Rupture of Membranes.
            Erratum:[Z Geburtshilfe Neonatol. 2022 Aug;226(4):e40. doi:
            10.1055/a-1845-2928. PMID: 35580619]
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Ren,L., Li,P., Li,Z. and Chen,Q.
  TITLE     AQP9 and ZAP70 as immune-related prognostic biomarkers suppress
            proliferation, migration and invasion of laryngeal cancer cells
  JOURNAL   BMC Cancer 22 (1), 465 (2022)
   PUBMED   35477402
  REMARK    GeneRIF: AQP9 and ZAP70 as immune-related prognostic biomarkers
            suppress proliferation, migration and invasion of laryngeal cancer
            cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 230)
  AUTHORS   He,S., Yang,M., Yang,Y., Wang,F., Wang,X., Lu,T., Jiao,M. and Li,Y.
  TITLE     [Association study of single nucleotide polymorphisms of AQP7 and
            AQP9 genes with type 2 diabetes mellitus among ethnic Han Chinese
            population]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 39 (2), 234-239 (2022)
   PUBMED   35076928
  REMARK    GeneRIF: [Association study of single nucleotide polymorphisms of
            AQP7 and AQP9 genes with type 2 diabetes mellitus among ethnic Han
            Chinese population].
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Kuriyama,H., Kawamoto,S., Ishida,N., Ohno,I., Mita,S.,
            Matsuzawa,Y., Matsubara,K. and Okubo,K.
  TITLE     Molecular cloning and expression of a novel human aquaporin from
            adipose tissue with glycerol permeability
  JOURNAL   Biochem Biophys Res Commun 241 (1), 53-58 (1997)
   PUBMED   9405233
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Kuwahara,M., Gu,Y., Ishibashi,K., Marumo,F. and Sasaki,S.
  TITLE     Mercury-sensitive residues and pore site in AQP3 water channel
  JOURNAL   Biochemistry 36 (46), 13973-13978 (1997)
   PUBMED   9369468
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC296768.1 and AC066616.7.
            
            Summary: The aquaporins are a family of water-selective membrane
            channels. This gene encodes a member of a subset of aquaporins
            called the aquaglyceroporins. This protein allows passage of a
            broad range of noncharged solutes and also stimulates urea
            transport and osmotic water permeability. This protein may also
            facilitate the uptake of glycerol in hepatic tissue . The encoded
            protein may also play a role in specialized leukocyte functions
            such as immunological response and bactericidal activity. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) uses an alternate 5' most exon
            which results in a distinct 5' UTR and the use of a downstream
            start codon compared to variant 1. The encoded isoform (3) has a
            shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.20342.1, AK300055.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..230
                     /product="aquaporin-9 isoform 3"
                     /note="small solute channel 1; aquaglyceroporin-9"
                     /calculated_mol_wt=24415
     Region          <1..201
                     /region_name="MIP"
                     /note="Major intrinsic protein (MIP) superfamily. Members
                     of the MIP superfamily function as membrane channels that
                     selectively transport water, small neutral molecules, and
                     ions out of and between cells. The channel proteins share
                     a common fold: the N-terminal...; cl00200"
                     /db_xref="CDD:444743"
     Site            order(17..19,147..148,151,154)
                     /site_type="active"
                     /note="amphipathic channel [active]"
                     /db_xref="CDD:238204"
     Site            order(19..21,151..153)
                     /site_type="other"
                     /note="Asn-Pro-Ala signature motifs"
                     /db_xref="CDD:238204"
     CDS             1..230
                     /gene="AQP9"
                     /gene_synonym="AQP-9; HsT17287; SSC1; T17287"
                     /coded_by="NM_001320636.1:198..890"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81887.1"
                     /db_xref="GeneID:366"
                     /db_xref="HGNC:HGNC:643"
                     /db_xref="MIM:602914"
ORIGIN      
        1 mavamaiyva ggvsgghinp avslamclfg rmkwfklpfy vgaqflgafv gaatvfgiyy
       61 dglmsfaggk llivgenata hifatypapy lslanafadq vvatmillii vfaifdsrnl
      121 gaprglepia iglliivias slglnsgcam npardlsprl ftalagwgfe vfragnnfww
      181 ipvvgplvga viggliyvlv ieihhpepds vfkteqsedk pekyelsvim
//
LOCUS       NP_001156795             618 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 120 isoform 4 [Homo sapiens].
ACCESSION   NP_001156795
VERSION     NP_001156795.1
DBSOURCE    REFSEQ: accession NM_001163323.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    GeneRIF: centrosome-binding proteins, coiled-coil domain containing
            (CCDC) 120 and CCDC68 are two novel subdistal appendages (SDA)
            components required for hierarchical SDA assembly in human cells.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 618)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 618)
  AUTHORS   Torii,T., Miyamoto,Y., Tago,K., Sango,K., Nakamura,K., Sanbe,A.,
            Tanoue,A. and Yamauchi,J.
  TITLE     Arf6 guanine nucleotide exchange factor cytohesin-2 binds to
            CCDC120 and is transported along neurites to mediate neurite growth
  JOURNAL   J Biol Chem 289 (49), 33887-33903 (2014)
   PUBMED   25326380
  REMARK    GeneRIF: Arf6 guanine nucleotide exchange factor cytohesin-2 binds
            to CCDC120 and is transported along neurites to mediate neurite
            growth.
REFERENCE   9  (residues 1 to 618)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 618)
  AUTHORS   Tarpey,P.S., Smith,R., Pleasance,E., Whibley,A., Edkins,S.,
            Hardy,C., O'Meara,S., Latimer,C., Dicks,E., Menzies,A.,
            Stephens,P., Blow,M., Greenman,C., Xue,Y., Tyler-Smith,C.,
            Thompson,D., Gray,K., Andrews,J., Barthorpe,S., Buck,G., Cole,J.,
            Dunmore,R., Jones,D., Maddison,M., Mironenko,T., Turner,R.,
            Turrell,K., Varian,J., West,S., Widaa,S., Wray,P., Teague,J.,
            Butler,A., Jenkinson,A., Jia,M., Richardson,D., Shepherd,R.,
            Wooster,R., Tejada,M.I., Martinez,F., Carvill,G., Goliath,R., de
            Brouwer,A.P., van Bokhoven,H., Van Esch,H., Chelly,J., Raynaud,M.,
            Ropers,H.H., Abidi,F.E., Srivastava,A.K., Cox,J., Luo,Y.,
            Mallya,U., Moon,J., Parnau,J., Mohammed,S., Tolmie,J.L.,
            Shoubridge,C., Corbett,M., Gardner,A., Haan,E., Rujirabanjerd,S.,
            Shaw,M., Vandeleur,L., Fullston,T., Easton,D.F., Boyle,J.,
            Partington,M., Hackett,A., Field,M., Skinner,C., Stevenson,R.E.,
            Bobrow,M., Turner,G., Schwartz,C.E., Gecz,J., Raymond,F.L.,
            Futreal,P.A. and Stratton,M.R.
  TITLE     A systematic, large-scale resequencing screen of X-chromosome
            coding exons in mental retardation
  JOURNAL   Nat Genet 41 (5), 535-543 (2009)
   PUBMED   19377476
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA102343.1, AK300366.1 and
            BC008769.2.
            
            Summary: This gene encodes a protein that contains a coiled-coil
            domain. Several alternatively spliced transcript variants encoding
            multiple isoforms have been found for this gene. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence, lacks an alternate in-frame segment, and differs
            in the 3' UTR and coding sequence compared to variant 1. The
            resulting isoform (4) is shorter at the N-terminus, missing a 12 aa
            internal segment, and has a shorter and distinct C-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK300366.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA2142586,
                                    SAMEA2142853 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..618
                     /product="coiled-coil domain-containing protein 120
                     isoform 4"
                     /note="coiled-coil domain-containing protein 120"
                     /calculated_mol_wt=66223
     Region          5..129
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     CDS             1..618
                     /gene="CCDC120"
                     /gene_synonym="JM11"
                     /coded_by="NM_001163323.3:299..2155"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55413.1"
                     /db_xref="GeneID:90060"
                     /db_xref="HGNC:HGNC:28910"
                     /db_xref="MIM:300947"
ORIGIN      
        1 mevkaalfge aapqvkserl rglldrqrtl qealslklqe lrkvclqeae ltgqlppecp
       61 lepgerpqlv rrrpptaray ppphpnqahh slcpaeelal ealerevsvq qqiaaaarrl
      121 alapdlsteq rrrrrqvqad alrrlhelee qlrdvrarlg lpvlplpqpl plstgsvitt
      181 qgvclgmrla qlsqedvvlh sessslsesg ashdneephg cfslaerpsp pkawdqlrav
      241 sggsperrtp wkpppsdlyg dlksrrnsva sptsptrslp rsassfegrs vpatpvltrg
      301 agpqlckpeg lhsrqwsgsq dsqmgfprad pasdraslfv artrrsnsse allvdraagg
      361 gagsppapla psasgppvck ssevlyerpq ptpafssrta gppdppraar pssaapasrg
      421 aprlppvcgd flldysldrg lprsgggtgw gelppaaevp gplsrrdgll tmlpgpppvy
      481 aadsnspllr tkdphtratr tkpcglppea aegpevhpnp llwmppptri psagersghk
      541 nlaleglrdw yirnsglaag pqrrpvlpsv gpphppflha rcyevgqaly gapsqaplph
      601 srsftappvs gryggcfy
//
LOCUS       NP_003316               1017 aa            linear   PRI 20-NOV-2025
DEFINITION  protein HIRA [Homo sapiens].
ACCESSION   NP_003316
VERSION     NP_003316.3
DBSOURCE    REFSEQ: accession NM_003325.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1017)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1017)
  AUTHORS   Dasgupta,N., Lei,X., Shi,C.H., Arnold,R., Teneche,M.G.,
            Miller,K.N., Rajesh,A., Davis,A., Anschau,V., Campos,A.R.,
            Gilson,R., Havas,A., Yin,S., Chua,Z.M., Liu,T., Proulx,J.,
            Alcaraz,M., Rather,M.I., Baeza,J., Schultz,D.C., Yip,K.Y.,
            Berger,S.L. and Adams,P.D.
  TITLE     Histone chaperone HIRA, promyelocytic leukemia protein, and
            p62/SQSTM1 coordinate to regulate inflammation during cell
            senescence
  JOURNAL   Mol Cell 84 (17), 3271-3287 (2024)
   PUBMED   39178863
  REMARK    GeneRIF: Histone chaperone HIRA, promyelocytic leukemia protein,
            and p62/SQSTM1 coordinate to regulate inflammation during cell
            senescence.
REFERENCE   3  (residues 1 to 1017)
  AUTHORS   Nagagaki,Y., Kozakura,Y., Mahandaran,T., Fumoto,Y., Nakato,R.,
            Shirahige,K. and Ishikawa,F.
  TITLE     Histone H3.3 chaperone HIRA renders stress-responsive genes poised
            for prospective lethal stresses in acquired tolerance
  JOURNAL   Genes Cells 29 (9), 722-734 (2024)
   PUBMED   38977420
  REMARK    GeneRIF: Histone H3.3 chaperone HIRA renders stress-responsive
            genes poised for prospective lethal stresses in acquired tolerance.
REFERENCE   4  (residues 1 to 1017)
  AUTHORS   Javanshir,E., Ebrahimi,Z.J., Mirzohreh,S.T., Ghaffari,S.,
            Banisefid,E., Alamdari,N.M. and Roshanravan,N.
  TITLE     Disparity of gene expression in coronary artery disease: insights
            from MEIS1, HIRA, and Myocardin
  JOURNAL   Mol Biol Rep 51 (1), 712 (2024)
   PUBMED   38824221
  REMARK    GeneRIF: Disparity of gene expression in coronary artery disease:
            insights from MEIS1, HIRA, and Myocardin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1017)
  AUTHORS   Morozov,V.M., Riva,A., Sarwar,S., Kim,W.J., Li,J., Zhou,L.,
            Licht,J.D., Daaka,Y. and Ishov,A.M.
  TITLE     HIRA-mediated loading of histone variant H3.3 controls
            androgen-induced transcription by regulation of AR/BRD4 complex
            assembly at enhancers
  JOURNAL   Nucleic Acids Res 51 (19), 10194-10217 (2023)
   PUBMED   37638746
  REMARK    GeneRIF: HIRA-mediated loading of histone variant H3.3 controls
            androgen-induced transcription by regulation of AR/BRD4 complex
            assembly at enhancers.
REFERENCE   6  (residues 1 to 1017)
  AUTHORS   Lorain,S., Quivy,J.P., Monier-Gavelle,F., Scamps,C., Lecluse,Y.,
            Almouzni,G. and Lipinski,M.
  TITLE     Core histones and HIRIP3, a novel histone-binding protein, directly
            interact with WD repeat protein HIRA
  JOURNAL   Mol Cell Biol 18 (9), 5546-5556 (1998)
   PUBMED   9710638
REFERENCE   7  (residues 1 to 1017)
  AUTHORS   Llevadot,R., Scambler,P., Estivill,X. and Pritchard,M.
  TITLE     Genomic organization of TUPLE1/HIRA: a gene implicated in DiGeorge
            syndrome
  JOURNAL   Mamm Genome 7 (12), 911-914 (1996)
   PUBMED   8995764
REFERENCE   8  (residues 1 to 1017)
  AUTHORS   Lorain,S., Demczuk,S., Lamour,V., Toth,S., Aurias,A., Roe,B.A. and
            Lipinski,M.
  TITLE     Structural Organization of the WD repeat protein-encoding gene HIRA
            in the DiGeorge syndrome critical region of human chromosome 22
  JOURNAL   Genome Res 6 (1), 43-50 (1996)
   PUBMED   8681138
REFERENCE   9  (residues 1 to 1017)
  AUTHORS   Lamour,V., Lecluse,Y., Desmaze,C., Spector,M., Bodescot,M.,
            Aurias,A., Osley,M.A. and Lipinski,M.
  TITLE     A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional
            repressors cloned from the DiGeorge syndrome critical region
  JOURNAL   Hum Mol Genet 4 (5), 791-799 (1995)
   PUBMED   7633437
REFERENCE   10 (residues 1 to 1017)
  AUTHORS   Halford,S., Wadey,R., Roberts,C., Daw,S.C., Whiting,J.A.,
            O'Donnell,H., Dunham,I., Bentley,D., Lindsay,E., Baldini,A. et al.
  TITLE     Isolation of a putative transcriptional regulator from the region
            of 22q11 deleted in DiGeorge syndrome, Shprintzen syndrome and
            familial congenital heart disease
  JOURNAL   Hum Mol Genet 2 (12), 2099-2107 (1993)
   PUBMED   8111380
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000079.1, AC000092.1 and
            AC000085.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 21, 2002 this sequence version replaced NP_003316.2.
            
            Summary: This gene encodes a histone chaperone that preferentially
            places the variant histone H3.3 in nucleosomes. Orthologs of this
            gene in yeast, flies, and plants are necessary for the formation of
            transcriptionally silent heterochomatin. This gene plays an
            important role in the formation of the senescence-associated
            heterochromatin foci. These foci likely mediate the irreversible
            cell cycle changes that occur in senescent cells. It is considered
            the primary candidate gene in some haploinsufficiency syndromes
            such as DiGeorge syndrome, and insufficient production of the gene
            may disrupt normal embryonic development. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039835.1, X89887.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263208.5/ ENSP00000263208.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1017
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..1017
                     /product="protein HIRA"
                     /note="TUP1-like enhancer of split protein 1; DiGeorge
                     critical region gene 1; HIR histone cell cycle regulation
                     defective homolog A; histone regulator A"
                     /calculated_mol_wt=111705
     Region          <3..352
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          11..53
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          16..61
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          68..107
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          74..129
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Region          129..168
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          134..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          172..211
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          178..213
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          220..263
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          226..265
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          266..322
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          273..324
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          326..367
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          331..354
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          421..729
                     /region_name="Interaction with CCNA1.
                     /evidence=ECO:0000269|PubMed:11238922"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          421..479
                     /region_name="Interaction with ASF1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          439..475
                     /region_name="Required for repression of histone gene
                     transcription"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          494..555
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK2.
                     /evidence=ECO:0000269|PubMed:11238922; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Region          570..589
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Region          593..826
                     /region_name="Interaction with histone H2B"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          594..739
                     /region_name="Interaction with PAX3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          604..625
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11238922; propagated from
                     UniProtKB/Swiss-Prot (P54198.2)"
     Region          738..1017
                     /region_name="Interaction with histone H4"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          740..828
                     /region_name="Interaction with PAX3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P54198.2)"
     Region          764..962
                     /region_name="Hira"
                     /note="TUP1-like enhancer of split; pfam07569"
                     /db_xref="CDD:462211"
     CDS             1..1017
                     /gene="HIRA"
                     /gene_synonym="DGCR1; TUP1; TUPLE1"
                     /coded_by="NM_003325.4:258..3311"
                     /db_xref="CCDS:CCDS13759.1"
                     /db_xref="GeneID:7290"
                     /db_xref="HGNC:HGNC:4916"
                     /db_xref="MIM:600237"
ORIGIN      
        1 mkllkptwvn hngkpifsvd ihpdgtkfat ggqgqdsgkv viwnmspvlq eddekdenip
       61 kmlcqmdnhl acvncvrwsn sgmylasggd dklimvwkra tyigpstvfg ssgklanveq
      121 wrcvsilrnh sgdvmdvaws phdawlascs vdntvviwna vkfpeilatl rghsglvkgl
      181 twdpvgkyia sqaddrslkv wrtldwqlet sitkpfdecg gtthvlrlsw spdghylvsa
      241 hamnnsgpta qiieregwkt nmdfvghrka vtvvkfnpki fkkkqkngss akpscpyccc
      301 avgskdrsls vwltclkrpl vvihelfdks imdiswtlng lgilvcsmdg svafldfsqd
      361 elgdplseee ksrihqstyg kslaimteaq lstavienpe mlkyqrrqqq qqldqksaat
      421 remgsatsva gvvngesled irknllkkqv etrtadgrrr itplciaqld tgdfstaffn
      481 siplsgslag tmlsshsspq llpldsstpn sfgaskpcte pvvaasarpa gdsvnkdsmn
      541 atstpaalsp svlttpskie pmkafdsrft erskatpgap altsmtptav erlkeqnlvk
      601 elrprdlles ssdsdekvpl akasslskrk lelevetvek kkkgrprkds rlmpvslsvq
      661 spaaltaeke amclsapala lklpipspqr aftlqvssdp smyievenev tvvggvklsr
      721 lkcnregkew etvltsrilt aagscdvvcv acekrmlsvf stcgrrllsp illpspistl
      781 hctgsyvmal taaatlsvwd vhrqvvvvke eslhsilags dmtvsqillt qhgipvmnls
      841 dgkaycfnps lstwnlvsdk qdslaqcadf rsslpsqdam lcsgplaiiq grtsnsgrqa
      901 arlfsvphvv qqettlayle nqvaaaltlq ssheyrhwll vyarylvneg feyrlreick
      961 dllgpvhyst gsqwestvvg lrkrellkel lpvigqnlrf qrlftecqeq ldilrdk
//
LOCUS       NP_006824                327 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 6 [Homo sapiens].
ACCESSION   NP_006824
VERSION     NP_006824.2
DBSOURCE    REFSEQ: accession NM_006833.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Li,K., Zhang,J., Lyu,H., Yang,J., Wei,W., Wang,Y., Luo,H.,
            Zhang,Y., Jiang,X., Yi,H., Wang,M., Zhang,C., Wu,K., Xiao,L.,
            Wen,W., Xu,H., Li,G., Wan,Y., Yang,F., Yang,R., Fu,X., Qin,B.,
            Zhou,Z., Zhang,H. and Lee,M.H.
  TITLE     CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma Progression
            via YAP1 Activation
  JOURNAL   Adv Sci (Weinh) 11 (14), e2306827 (2024)
   PUBMED   38308184
  REMARK    GeneRIF: CSN6-SPOP-HMGCS1 Axis Promotes Hepatocellular Carcinoma
            Progression via YAP1 Activation.
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Zou,S., Qin,B., Yang,Z., Wang,W., Zhang,J., Zhang,Y., Meng,M.,
            Feng,J., Xie,Y., Fang,L., Xiao,L., Zhang,P., Meng,X., Choi,H.H.,
            Wen,W., Pan,Q., Ghesquiere,B., Lan,P., Lee,M.H. and Fang,L.
  TITLE     CSN6 Mediates Nucleotide Metabolism to Promote Tumor Development
            and Chemoresistance in Colorectal Cancer
  JOURNAL   Cancer Res 83 (3), 414-427 (2023)
   PUBMED   36512632
  REMARK    GeneRIF: CSN6 Mediates Nucleotide Metabolism to Promote Tumor
            Development and Chemoresistance in Colorectal Cancer.
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Wang,X. and Chen,T.
  TITLE     CUL4A regulates endometrial cancer cell proliferation, invasion and
            migration by interacting with CSN6
  JOURNAL   Mol Med Rep 23 (1) (2021)
   PUBMED   33179082
  REMARK    GeneRIF: CUL4A regulates endometrial cancer cell proliferation,
            invasion and migration by interacting with CSN6.
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Di Marzio,P., Choe,S., Ebright,M., Knoblauch,R. and Landau,N.R.
  TITLE     Mutational analysis of cell cycle arrest, nuclear localization and
            virion packaging of human immunodeficiency virus type 1 Vpr
  JOURNAL   J Virol 69 (12), 7909-7916 (1995)
   PUBMED   7494303
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Re,F., Braaten,D., Franke,E.K. and Luban,J.
  TITLE     Human immunodeficiency virus type 1 Vpr arrests the cell cycle in
            G2 by inhibiting the activation of p34cdc2-cyclin B
  JOURNAL   J Virol 69 (11), 6859-6864 (1995)
   PUBMED   7474100
REFERENCE   8  (residues 1 to 327)
  AUTHORS   He,J., Choe,S., Walker,R., Di Marzio,P., Morgan,D.O. and
            Landau,N.R.
  TITLE     Human immunodeficiency virus type 1 viral protein R (Vpr) arrests
            cells in the G2 phase of the cell cycle by inhibiting p34cdc2
            activity
  JOURNAL   J Virol 69 (11), 6705-6711 (1995)
   PUBMED   7474080
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Jowett,J.B., Planelles,V., Poon,B., Shah,N.P., Chen,M.L. and
            Chen,I.S.
  TITLE     The human immunodeficiency virus type 1 vpr gene arrests infected T
            cells in the G2 + M phase of the cell cycle
  JOURNAL   J Virol 69 (10), 6304-6313 (1995)
   PUBMED   7666531
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Mittmeyer,H.J.
  TITLE     [Distribution pattern of rigor mortis in various joint regions]
  JOURNAL   Beitr Gerichtl Med 33, 85-96 (1975)
   PUBMED   1222062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB990467.1, BC002520.2 and
            CD367717.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 25, 2003 this sequence version replaced NP_006824.1.
            
            Summary: The protein encoded by this gene is one of the eight
            subunits of COP9 signalosome, a highly conserved protein complex
            that functions as an important regulator in multiple signaling
            pathways. The structure and function of COP9 signalosome is similar
            to that of the 19S regulatory particle of 26S proteasome. COP9
            signalosome has been shown to interact with SCF-type E3 ubiquitin
            ligases and act as a positive regulator of E3 ubiquitin ligases.
            This protein belongs to translation initiation factor 3 (eIF3)
            superfamily. It is involved in the regulation of cell cycle and
            likely to be a cellular cofactor for HIV-1 accessory gene product
            Vpr. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.127123.1,
                                           SRR3476690.539176.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303904.8/ ENSP00000304102.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..327
                     /product="COP9 signalosome complex subunit 6"
                     /note="H_NH0506M12.12; COP9 constitutive photomorphogenic
                     homolog subunit 6; MOV34 homolog, 34 kD; SGN6; hVIP;
                     vpr-interacting protein; JAB1-containing signalosome
                     subunit 6"
                     /calculated_mol_wt=36032
     Region          39..321
                     /region_name="MPN_CSN6"
                     /note="Mpr1p, Pad1p N-terminal (MPN) domains without
                     catalytic isopeptidase activity, found in COP9 signalosome
                     complex subunit 6; cd08063"
                     /db_xref="CDD:163694"
     Region          211..327
                     /region_name="Interaction with Vpr"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7L5N1.1)"
     CDS             1..327
                     /gene="COPS6"
                     /gene_synonym="CSN6; MOV34-34KD"
                     /coded_by="NM_006833.5:23..1006"
                     /db_xref="CCDS:CCDS5682.1"
                     /db_xref="GeneID:10980"
                     /db_xref="HGNC:HGNC:21749"
                     /db_xref="MIM:614729"
ORIGIN      
        1 maaaaaaaaa tngtggssgm evdaavvpsv macgvtgsvs valhplviln isdhwirmrs
       61 qegrpvqvig aligkqegrn ievmnsfell shtveekiii dkeyyytkee qfkqvfkele
      121 flgwyttggp pdpsdihvhk qvceiiespl flklnpmtkh tdlpvsvfes vidiingeat
      181 mlfaeltytl ateeaerigv dhvarmtatg sgenstvaeh liaqhsaikm lhsrvklile
      241 yvkaseagev pfnheilrea yalchclpvl stdkfktdfy dqcndvglma ylgtitktcn
      301 tmnqfvnkfn vlydrqgigr rmrglff
//
LOCUS       NP_065396                375 aa            linear   PRI 20-NOV-2025
DEFINITION  killer cell immunoglobulin-like receptor 2DL5A precursor [Homo
            sapiens].
ACCESSION   NP_065396 XP_941833
VERSION     NP_065396.1
DBSOURCE    REFSEQ: accession NM_020535.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Margolis,D.J., Mitra,N., Hoffstad,O.J., Berna,R., Kim,B.S.,
            Chopra,A. and Phillips,E.J.
  TITLE     Association of KIR2DL5, KIR2DS5, and KIR2DS1 allelic variation and
            atopic dermatitis
  JOURNAL   Sci Rep 13 (1), 1730 (2023)
   PUBMED   36720995
  REMARK    GeneRIF: Association of KIR2DL5, KIR2DS5, and KIR2DS1 allelic
            variation and atopic dermatitis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Elfishawi,S.M., Mossallam,G.I., El-Fattah,R.A., El-Haddad,A. and
            Kamel,A.M.
  TITLE     The effect of killer cell immunoglobulin-like receptor genotype on
            outcome of hematopoietic stem cell transplantation from matched
            sibling
  JOURNAL   Hum Immunol 78 (11-12), 684-691 (2017)
   PUBMED   28993188
  REMARK    GeneRIF: KIR 2DL5 was associated with decreased CMV infection and
            better platelets engraftment after hematopoietic stem cell
            transplantation from matched sibling
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Anastasaki,C., Dahiya,S. and Gutmann,D.H.
  TITLE     KIR2DL5 mutation and loss underlies sporadic dermal neurofibroma
            pathogenesis and growth
  JOURNAL   Oncotarget 8 (29), 47574-47585 (2017)
   PUBMED   28548933
  REMARK    GeneRIF: these findings establish KIR2DL5 as a new Schwann cell
            growth regulator relevant to sp-DNF pathogenesis, which links
            sporadic and NF1-associated DNFs through RAS pathway
            hyperactivation.
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Suzuki,Y., Hamamoto,Y., Ogasawara,Y., Ishikawa,K., Yoshikawa,Y.,
            Sasazuki,T. and Muto,M.
  TITLE     Genetic polymorphisms of killer cell immunoglobulin-like receptors
            are associated with susceptibility to psoriasis vulgaris
  JOURNAL   J Invest Dermatol 122 (5), 1133-1136 (2004)
   PUBMED   15140215
  REMARK    GeneRIF: The frequencies of KIR2DS1 and KIR2DL5 were significantly
            increased in psoriasis vulgaris cases compared with controls
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 375)
  AUTHORS   Gomez-Lozano,N., Gardiner,C.M., Parham,P. and Vilches,C.
  TITLE     Some human KIR haplotypes contain two KIR2DL5 genes: KIR2DL5A and
            KIR2DL5B
  JOURNAL   Immunogenetics 54 (5), 314-319 (2002)
   PUBMED   12185535
  REMARK    GeneRIF: Human KIR2DL5 has at least 4 gene variants, whose exons
            differ by 2 to 8 nucleotides. These structurally similar variants
            are encoded by alleles of 2 different loci, KIR2DL5A and KIR2DL5B,
            which map to different regions of the KIR-gene cluster.
REFERENCE   8  (residues 1 to 375)
  AUTHORS   Moodie,S.J., Norman,P.J., King,A.L., Fraser,J.S., Curtis,D.,
            Ellis,H.J., Vaughan,R.W. and Ciclitira,P.J.
  TITLE     Analysis of candidate genes on chromosome 19 in coeliac disease: an
            association study of the KIR and LILR gene clusters
  JOURNAL   Eur J Immunogenet 29 (4), 287-291 (2002)
   PUBMED   12121272
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 375)
  AUTHORS   Vilches,C., Gardiner,C.M. and Parham,P.
  TITLE     Gene structure and promoter variation of expressed and nonexpressed
            variants of the KIR2DL5 gene
  JOURNAL   J Immunol 165 (11), 6416-6421 (2000)
   PUBMED   11086080
REFERENCE   10 (residues 1 to 375)
  AUTHORS   Vilches,C., Rajalingam,R., Uhrberg,M., Gardiner,C.M., Young,N.T.
            and Parham,P.
  TITLE     KIR2DL5, a novel killer-cell receptor with a D0-D2 configuration of
            Ig-like domains
  JOURNAL   J Immunol 164 (11), 5797-5804 (2000)
   PUBMED   10820258
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF204903.1.
            
            On Mar 4, 2006 this sequence version replaced XP_941833.1.
            
            Summary: Killer cell immunoglobulin-like receptors (KIRs) are
            transmembrane glycoproteins expressed by natural killer cells and
            subsets of T cells. The KIR genes are polymorphic and highly
            homologous and they are found in a cluster on chromosome 19q13.4
            within the 1 Mb leukocyte receptor complex (LRC). The gene content
            of the KIR gene cluster varies among haplotypes, although several
            'framework' genes are found in all haplotypes (KIR3DL3, KIR3DP1,
            KIR3DL4, KIR3DL2). The KIR proteins are classified by the number of
            extracellular immunoglobulin domains (2D or 3D) and by whether they
            have a long (L) or short (S) cytoplasmic domain. KIR proteins with
            the long cytoplasmic domain transduce inhibitory signals upon
            ligand binding via an immune tyrosine-based inhibitory motif
            (ITIM), while KIR proteins with the short cytoplasmic domain lack
            the ITIM motif and instead associate with the TYRO protein tyrosine
            kinase binding protein to transduce activating signals. The ligands
            for several KIR proteins are subsets of HLA class I molecules;
            thus, KIR proteins are thought to play an important role in
            regulation of the immune response. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF204903.1, AF271607.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000613155.1/ ENSP00000484296.1
            RefSeq Select criteria :: based on manual assertion, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..375
                     /product="killer cell immunoglobulin-like receptor 2DL5A
                     precursor"
                     /note="killer cell immunoglobulin-like receptor 2DL5A;
                     killer cell immunoglobulin-like receptor, two domains,
                     long cytoplasmic tail, 5A; killer cell immunoglobulin-like
                     receptor KIR2DL5A"
                     /calculated_mol_wt=38390
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2306
     mat_peptide     22..375
                     /product="Killer cell immunoglobulin-like receptor 2DL5A.
                     /id=PRO_0000300638"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N109.1)"
                     /calculated_mol_wt=38390
     Region          28..117
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          45..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          57..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          78..82
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          92..97
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..113
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          123..211
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            139
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N109.1)"
     Region          140..144
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N109.1)"
     Region          178..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          190..195
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          208..211
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          213..233
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N109.1)"
     Site            218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N109.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N109.1)"
     Region          334..375
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N109.1)"
     CDS             1..375
                     /gene="KIR2DL5A"
                     /gene_synonym="CD158F; KIR2DL5; KIR2DL5.1; KIR2DL5.3"
                     /coded_by="NM_020535.3:56..1183"
                     /db_xref="GeneID:57292"
                     /db_xref="HGNC:HGNC:16345"
                     /db_xref="MIM:605305"
ORIGIN      
        1 mslmvismac vgffllqgaw theggqdkpl lsawpsavvp rgghvtllcr srlgftifsl
       61 ykedgvpvpe lynkifwksi lmgpvtpaha gtyrcrgshp rspiewsaps nplvivvtgl
      121 fgkpslsaqp gptvrtgenv tlscssrssf dmyhlsregr aheprlpavp svngtfqadf
      181 plgpathggt ytcfgslhds pyewsdpsdp llvsvtgnss ssssspteps sktgirrhlh
      241 iligtsvaii lfiilfffll hcccsnkkna avmdqepagd rtvnredsdd qdpqevtyaq
      301 ldhcvftqtk itspsqrpkt pptdttmyme lpnakprsls pahkhhsqal rgssrettal
      361 sqnrvasshv paagi
//
LOCUS       NP_001185                889 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium/sodium hyperpolarization-activated cyclic
            nucleotide-gated channel 2 [Homo sapiens].
ACCESSION   NP_001185
VERSION     NP_001185.3
DBSOURCE    REFSEQ: accession NM_001194.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 889)
  AUTHORS   Pai,V.P. and Levin,M.
  TITLE     HCN2 channel-induced rescue of brain, eye, heart and gut
            teratogenesis caused by nicotine, ethanol and aberrant notch
            signalling
  JOURNAL   Wound Repair Regen 30 (6), 681-706 (2022)
   PUBMED   35662339
  REMARK    GeneRIF: HCN2 channel-induced rescue of brain, eye, heart and gut
            teratogenesis caused by nicotine, ethanol and aberrant notch
            signalling.
REFERENCE   2  (residues 1 to 889)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 889)
  AUTHORS   Lin,W., Qin,J., Ni,G., Li,Y., Xie,H., Yu,J., Li,H., Sui,L., Guo,Q.,
            Fang,Z. and Zhou,L.
  TITLE     Downregulation of hyperpolarization-activated cyclic
            nucleotide-gated channels (HCN) in the hippocampus of patients with
            medial temporal lobe epilepsy and hippocampal sclerosis (MTLE-HS)
  JOURNAL   Hippocampus 30 (10), 1112-1126 (2020)
   PUBMED   32543742
  REMARK    GeneRIF: Downregulation of hyperpolarization-activated cyclic
            nucleotide-gated channels (HCN) in the hippocampus of patients with
            medial temporal lobe epilepsy and hippocampal sclerosis (MTLE-HS).
REFERENCE   4  (residues 1 to 889)
  AUTHORS   Zhao,H., Wang,F., Tang,Y., Wang,X., Wang,T., Zhao,Q. and Huang,C.
  TITLE     HCN2 and TBX3 Reprogram Human-Induced Pluripotent Stem
            Cells-Derived Cardiomyocytes into Pacemaker-Like Cells
  JOURNAL   DNA Cell Biol 39 (2), 289-298 (2020)
   PUBMED   31916853
  REMARK    GeneRIF: overexpression of TBX3 and HCN2 could reprogram
            human-induced pluripotent stem cells-derived cardiomyocytes into
            pacemaker-like cells
REFERENCE   5  (residues 1 to 889)
  AUTHORS   Thomas,M., Ranjith,G., Radhakrishnan,A. and Arun Anirudhan,V.
  TITLE     Effects of HCN2 Mutations on Dendritic Excitability and Synaptic
            Plasticity: A Computational Study
  JOURNAL   Neuroscience 423, 148-161 (2019)
   PUBMED   31682955
  REMARK    GeneRIF: Effects of HCN2 Mutations on Dendritic Excitability and
            Synaptic Plasticity: A Computational Study.
REFERENCE   6  (residues 1 to 889)
  AUTHORS   Vaccari,T., Moroni,A., Rocchi,M., Gorza,L., Bianchi,M.E.,
            Beltrame,M. and DiFrancesco,D.
  TITLE     The human gene coding for HCN2, a pacemaker channel of the heart
  JOURNAL   Biochim Biophys Acta 1446 (3), 419-425 (1999)
   PUBMED   10524219
REFERENCE   7  (residues 1 to 889)
  AUTHORS   Ludwig,A., Zong,X., Stieber,J., Hullin,R., Hofmann,F. and Biel,M.
  TITLE     Two pacemaker channels from human heart with profoundly different
            activation kinetics
  JOURNAL   EMBO J 18 (9), 2323-2329 (1999)
   PUBMED   10228147
REFERENCE   8  (residues 1 to 889)
  AUTHORS   Kleiderlein,J.J., Nisson,P.E., Jessee,J., Li,W.B., Becker,K.G.,
            Derby,M.L., Ross,C.A. and Margolis,R.L.
  TITLE     CCG repeats in cDNAs from human brain
  JOURNAL   Hum Genet 103 (6), 666-673 (1998)
   PUBMED   9921901
  REMARK    Erratum:[Hum Genet 1999 Jan;104(1):113]
REFERENCE   9  (residues 1 to 889)
  AUTHORS   Santoro,B., Liu,D.T., Yao,H., Bartsch,D., Kandel,E.R.,
            Siegelbaum,S.A. and Tibbs,G.R.
  TITLE     Identification of a gene encoding a hyperpolarization-activated
            pacemaker channel of brain
  JOURNAL   Cell 93 (5), 717-729 (1998)
   PUBMED   9630217
REFERENCE   10 (residues 1 to 889)
  AUTHORS   Santoro,B., Grant,S.G., Bartsch,D. and Kandel,E.R.
  TITLE     Interactive cloning with the SH3 domain of N-src identifies a new
            brain specific ion channel protein, with homology to eag and cyclic
            nucleotide-gated channels
  JOURNAL   Proc Natl Acad Sci U S A 94 (26), 14815-14820 (1997)
   PUBMED   9405696
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005559.2, AJ012582.1,
            BC039619.1 and AF065164.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 16, 2007 this sequence version replaced NP_001185.2.
            
            Summary: The protein encoded by this gene is a
            hyperpolarization-activated cation channel involved in the
            generation of native pacemaker activity in the heart and in the
            brain. The encoded protein is activated by cAMP and can produce a
            fast, large current. Defects in this gene were noted as a possible
            cause of some forms of epilepsy. [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ012582.1, AF065164.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251287.3/ ENSP00000251287.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..889
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..889
                     /product="potassium/sodium hyperpolarization-activated
                     cyclic nucleotide-gated channel 2"
                     /note="brain cyclic nucleotide-gated channel 2;
                     hyperpolarization activated cyclic nucleotide gated
                     potassium channel 2"
                     /calculated_mol_wt=96820
     Region          1..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          <57..185
                     /region_name="PBP1"
                     /note="PAB1-binding protein, interacts with
                     poly(A)-binding protein [RNA processing and modification];
                     COG5180"
                     /db_xref="CDD:444064"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          150..>688
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          158..209
                     /region_name="Involved in subunit assembly.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKA9; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            216..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            241..261
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            289..309
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            318..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            370..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            407
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            441..461
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          544..652
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(608..609,618..620)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(640..642,646..648)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG/PRKG2.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Region          754..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JKA9; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            756
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     Site            868
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88703; propagated from
                     UniProtKB/Swiss-Prot (Q9UL51.3)"
     CDS             1..889
                     /gene="HCN2"
                     /gene_synonym="BCNG-2; BCNG2; EIG17; FEB2; GEFSP11; HAC-1"
                     /coded_by="NM_001194.4:66..2735"
                     /db_xref="CCDS:CCDS12035.1"
                     /db_xref="GeneID:610"
                     /db_xref="HGNC:HGNC:4846"
                     /db_xref="MIM:602781"
ORIGIN      
        1 mdarggggrp gespgatpap gpppppppap pqqqpppppp papppgpgpa ppqhppraea
       61 lppeaadegg prgrlrsrds scgrpgtpga astakgspng ecgrgepqcs pagpegparg
      121 pkvsfscrga asgpapgpgp aeeagseeag pageprgsqa sfmqrqfgal lqpgvnkfsl
      181 rmfgsqkave reqervksag awiihpysdf rfywdftmll fmvgnliiip vgitffkdet
      241 tapwivfnvv sdtfflmdlv lnfrtgivie dnteiildpe kikkkylrtw fvvdfvssip
      301 vdyiflivek gidsevykta ralrivrftk ilsllrllrl srliryihqw eeifhmtydl
      361 asavmricnl ismmlllchw dgclqflvpm lqdfprncwv singmvnhsw selysfalfk
      421 amshmlcigy grqapesmtd iwltmlsmiv gatcyamfig hataliqsld ssrrqyqeky
      481 kqveqymsfh klpadfrqki hdyyehryqg kmfdedsilg elngplreei vnfncrklva
      541 smplfanadp nfvtamltkl kfevfqpgdy iiregtigkk myfiqhgvvs vltkgnkemk
      601 lsdgsyfgei clltrgrrta svradtycrl yslsvdnfne vleeypmmrr afetvaidrl
      661 drigkknsil lhkvqhdlns gvfnnqenai iqeivkydre mvqqaelgqr vglfpppppp
      721 pqvtsaiatl qqaaamsfcp qvarplvgpl algsprlvrr pppgpapaaa spgppppasp
      781 pgapasprap rtspygglpa aplagpalpa rrlsrasrpl sasqpslphg apgpaastrp
      841 assstprlgp tpaaraaaps pdrrdsaspg aaggldpqds arsrlssnl
//
LOCUS       NP_055107                412 aa            linear   PRI 20-NOV-2025
DEFINITION  chromobox protein homolog 6 isoform 1 [Homo sapiens].
ACCESSION   NP_055107
VERSION     NP_055107.3
DBSOURCE    REFSEQ: accession NM_014292.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Freire-Beneitez,V., Pomella,N., Millner,T.O., Dumas,A.A.,
            Niklison-Chirou,M.V., Maniati,E., Wang,J., Rajeeve,V., Cutillas,P.
            and Marino,S.
  TITLE     Elucidation of the BMI1 interactome identifies novel regulatory
            roles in glioblastoma
  JOURNAL   NAR Cancer 3 (1), zcab009 (2021)
   PUBMED   34316702
  REMARK    Erratum:[NAR Cancer. 2021 May 25;3(2):zcab020. doi:
            10.1093/narcan/zcab020. PMID: 34319293]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Sakai,K., Nishiuchi,T., Tange,S., Suzuki,Y., Yano,S., Terashima,M.,
            Suzuki,T. and Matsumoto,K.
  TITLE     Proteasomal degradation of polycomb-group protein CBX6 confers
            MMP-2 expression essential for mesothelioma invasion
  JOURNAL   Sci Rep 10 (1), 16678 (2020)
   PUBMED   33028834
  REMARK    GeneRIF: Proteasomal degradation of polycomb-group protein CBX6
            confers MMP-2 expression essential for mesothelioma invasion.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Maertens,G.N., El Messaoudi-Aubert,S., Elderkin,S., Hiom,K. and
            Peters,G.
  TITLE     Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation
            of the INK4a tumour suppressor
  JOURNAL   EMBO J 29 (15), 2553-2565 (2010)
   PUBMED   20601937
REFERENCE   8  (residues 1 to 412)
  AUTHORS   El Messaoudi-Aubert,S., Nicholls,J., Maertens,G.N., Brookes,S.,
            Bernstein,E. and Peters,G.
  TITLE     Role for the MOV10 RNA helicase in polycomb-mediated repression of
            the INK4a tumor suppressor
  JOURNAL   Nat Struct Mol Biol 17 (7), 862-868 (2010)
   PUBMED   20543829
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Vincenz,C. and Kerppola,T.K.
  TITLE     Different polycomb group CBX family proteins associate with
            distinct regions of chromatin using nonhomologous protein sequences
  JOURNAL   Proc Natl Acad Sci U S A 105 (43), 16572-16577 (2008)
   PUBMED   18927235
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Tajul-Arifin,K., Teasdale,R., Ravasi,T., Hume,D.A. and Mattick,J.S.
  CONSRTM   RIKEN GER Group; GSL Members
  TITLE     Identification and analysis of chromodomain-containing proteins
            encoded in the mouse transcriptome
  JOURNAL   Genome Res 13 (6B), 1416-1429 (2003)
   PUBMED   12819141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD625491.1, BC064900.1 and AL008583.1.
            
            On Apr 29, 2004 this sequence version replaced NP_055107.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1114975.1, BC064900.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407418.8/ ENSP00000384490.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..412
                     /product="chromobox protein homolog 6 isoform 1"
                     /note="chromobox protein homolog 6; chromobox homolog 6"
                     /calculated_mol_wt=43767
     Region          8..65
                     /region_name="CD_Cbx6"
                     /note="chromodomain of chromobox homolog 6; cd18648"
                     /db_xref="CDD:349295"
     Site            order(10..13,32..33,35,39,41,43..44,46..47,49..50,52..53)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349295"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95503.1)"
     Region          127..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95503.1)"
     Region          <237..>331
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          243..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95503.1)"
     Region          357..388
                     /region_name="CBX7_C"
                     /note="CBX family C-terminal motif; pfam17218"
                     /db_xref="CDD:465385"
     CDS             1..412
                     /gene="CBX6"
                     /coded_by="NM_014292.5:27..1265"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13980.1"
                     /db_xref="GeneID:23466"
                     /db_xref="HGNC:HGNC:1556"
                     /db_xref="MIM:617438"
ORIGIN      
        1 melsavgerv faaesiikrr irkgrieylv kwkgwaikys twepeenild srliaafeqk
       61 ererelygpk krgpkpktfl lkaraqaeal risdvhfsvk psasasspkl hssaavhrlk
      121 kdirrchrms rrplprpdpq ggspglrppi spfsetvrii nrkvkprepk rnriilnlkv
      181 idkgagggga gqgagalarp kvpsrnrvig kskkfsesvl rtqirhmkfg afalykpppa
      241 plvapspgka easapgpgll laapaapyda rssgssgcps ptpqssdpdd tppkllpetv
      301 spsapswrep evldlslppe saatskrapp evtaaagpap ptapepagas sepeagdwrp
      361 emspcsnvvv tdvtsnlltv tikefcnped fekvaagvag aaggggsiga sk
//
LOCUS       NP_002296                135 aa            linear   PRI 20-NOV-2025
DEFINITION  galectin-1 [Homo sapiens].
ACCESSION   NP_002296
VERSION     NP_002296.1
DBSOURCE    REFSEQ: accession NM_002305.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Zhang,L., Chen,W., Li,X., Wang,G., Xing,F. and Zhu,X.
  TITLE     Galectin-1 overexpression induces normal fibroblasts translate into
            cancer-associated fibroblasts and attenuates the sensitivity of
            anlotinib in lung cancer
  JOURNAL   Cell Adh Migr 18 (1), 1-11 (2024)
   PUBMED   38557441
  REMARK    GeneRIF: Galectin-1 overexpression induces normal fibroblasts
            translate into cancer-associated fibroblasts and attenuates the
            sensitivity of anlotinib in lung cancer.
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Qin,H., Peng,M., Cheng,J., Wang,Z., Cui,Y., Huang,Y., Gui,Y.,
            Sun,Y., Xiang,W., Huang,X., Huang,T., Wang,L., Chen,J. and Hou,Y.
  TITLE     A novel LGALS1-depended and immune-associated fatty acid metabolism
            risk model in acute myeloid leukemia stem cells
  JOURNAL   Cell Death Dis 15 (7), 482 (2024)
   PUBMED   38965225
  REMARK    GeneRIF: A novel LGALS1-depended and immune-associated fatty acid
            metabolism risk model in acute myeloid leukemia stem cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Pan,Z., Xu,G., Zhang,Y., Wu,M., Yu,J., He,X., Zhang,W. and Hu,J.
  TITLE     Galectin-1 Promotes Gastric Carcinoma Progression and Cisplatin
            Resistance Through the NRP-1/c-JUN/Wee1 Pathway
  JOURNAL   J Gastric Cancer 24 (3), 300-315 (2024)
   PUBMED   38960889
  REMARK    GeneRIF: Galectin-1 Promotes Gastric Carcinoma Progression and
            Cisplatin Resistance Through the NRP-1/c-JUN/Wee1 Pathway.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Arvidsson,D., Rodrigues Silva,V.R., Ekblom,O., Ekblom-Bak,E.,
            Fryk,E., Jansson,P.A. and Borjesson,M.
  TITLE     Cardiorespiratory fitness and the association with galectin-1 in
            middle-aged individuals
  JOURNAL   PLoS One 19 (4), e0301412 (2024)
   PUBMED   38578722
  REMARK    GeneRIF: Cardiorespiratory fitness and the association with
            galectin-1 in middle-aged individuals.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Goldstone,S.D. and Lavin,M.F.
  TITLE     Isolation of a cDNA clone, encoding a human beta-galactoside
            binding protein, overexpressed during glucocorticoid-induced cell
            death
  JOURNAL   Biochem Biophys Res Commun 178 (2), 746-750 (1991)
   PUBMED   1713454
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Gitt,M.A. and Barondes,S.H.
  TITLE     Genomic sequence and organization of two members of a human lectin
            gene family
  JOURNAL   Biochemistry 30 (1), 82-89 (1991)
   PUBMED   1988031
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Allen,H.J., Sucato,D., Gottstine,S., Kisailus,E., Nava,H.,
            Petrelli,N., Castillo,N. and Wilson,D.
  TITLE     Localization of endogenous beta-galactoside-binding lectin in human
            cells and tissues
  JOURNAL   Tumour Biol 12 (1), 52-60 (1991)
   PUBMED   1996404
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Sharma,A., Chemelli,R. and Allen,H.J.
  TITLE     Human splenic galaptin: physicochemical characterization
  JOURNAL   Biochemistry 29 (22), 5309-5314 (1990)
   PUBMED   2383549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020675.1.
            
            Summary: The galectins are a family of beta-galactoside-binding
            proteins implicated in modulating cell-cell and cell-matrix
            interactions. This gene product may act as an autocrine negative
            growth factor that regulates cell proliferation. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020675.1, GQ891519.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215909.10/ ENSP00000215909.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..135
                     /product="galectin-1"
                     /note="beta-galactoside-binding lectin L-14-I;
                     lactose-binding lectin 1; galaptin; S-Lac lectin 1; HBL;
                     HPL; gal-1; HLBP14; 14 kDa lectin; 14 kDa laminin-binding
                     protein; putative MAPK-activating protein PM12;
                     beta-galactoside-binding protein 14kDa; lectin,
                     galactoside-binding, soluble, 1; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=14585
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P09382.2)"
     Region          11..134
                     /region_name="GLECT"
                     /note="Galectin; smart00276"
                     /db_xref="CDD:214596"
     Site            order(13..15,18,21,91..93,98,100,103)
                     /site_type="other"
                     /note="putative alternate dimerization interface
                     [polypeptide binding]"
                     /db_xref="CDD:238025"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16045; propagated from
                     UniProtKB/Swiss-Prot (P09382.2)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09382.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P09382.2)"
     Site            order(45,47,49,60,62,69,72,74)
                     /site_type="other"
                     /note="sugar binding pocket [chemical binding]"
                     /db_xref="CDD:238025"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P16045; propagated from
                     UniProtKB/Swiss-Prot (P09382.2)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P16045; propagated from
                     UniProtKB/Swiss-Prot (P09382.2)"
     CDS             1..135
                     /gene="LGALS1"
                     /gene_synonym="GAL1; GBP"
                     /coded_by="NM_002305.4:68..475"
                     /db_xref="CCDS:CCDS13954.1"
                     /db_xref="GeneID:3956"
                     /db_xref="HGNC:HGNC:6561"
                     /db_xref="MIM:150570"
ORIGIN      
        1 macglvasnl nlkpgeclrv rgevapdaks fvlnlgkdsn nlclhfnprf nahgdantiv
       61 cnskdggawg teqreavfpf qpgsvaevci tfdqanltvk lpdgyefkfp nrlnleainy
      121 maadgdfkik cvafd
//
LOCUS       NP_001295087             166 aa            linear   PRI 20-NOV-2025
DEFINITION  protransforming growth factor alpha isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001295087 XP_005264579
VERSION     NP_001295087.1
DBSOURCE    REFSEQ: accession NM_001308158.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Ma,X., Zheng,J., He,K., Wang,L., Wang,Z., Wang,K., Liu,Z., San,Z.,
            Zhao,L. and Wang,L.
  TITLE     TGFA expression is associated with poor prognosis and promotes the
            development of cervical cancer
  JOURNAL   J Cell Mol Med 28 (3), e18086 (2024)
   PUBMED   38152044
  REMARK    GeneRIF: TGFA expression is associated with poor prognosis and
            promotes the development of cervical cancer.
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Kamentseva,R.S., Kharchenko,M.V., Gabdrahmanova,G.V., Kotov,M.A.,
            Kosheverova,V.V. and Kornilova,E.S.
  TITLE     EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells
  JOURNAL   Int J Mol Sci 24 (17), 13408 (2023)
   PUBMED   37686213
  REMARK    GeneRIF: EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Sun,Y., Miao,X., Zhu,L., Liu,J., Lin,Y., Xiang,G., Wu,X., Wang,X.,
            Ni,Z. and Li,S.
  TITLE     Autocrine TGF-alpha is associated with Benzo(a)pyrene-induced mucus
            production and MUC5AC expression during allergic asthma
  JOURNAL   Ecotoxicol Environ Saf 241, 113833 (2022)
   PUBMED   36068759
  REMARK    GeneRIF: Autocrine TGF-alpha is associated with
            Benzo(a)pyrene-induced mucus production and MUC5AC expression
            during allergic asthma.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Qian,J.F., Lazar-Wesley,E., Breugnot,C. and May,E.
  TITLE     Human transforming growth factor alpha: sequence analysis of the
            4.5-kb and 1.6-kb mRNA species
  JOURNAL   Gene 132 (2), 291-296 (1993)
   PUBMED   8224876
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Thomas,D.M., Nasim,M.M., Gullick,W.J. and Alison,M.R.
  TITLE     Immunoreactivity of transforming growth factor alpha in the normal
            adult gastrointestinal tract
  JOURNAL   Gut 33 (5), 628-631 (1992)
   PUBMED   1612477
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Nasim,M.M., Thomas,D.M., Alison,M.R. and Filipe,M.I.
  TITLE     Transforming growth factor alpha expression in normal gastric
            mucosa, intestinal metaplasia, dysplasia and gastric carcinoma--an
            immunohistochemical study
  JOURNAL   Histopathology 20 (4), 339-343 (1992)
   PUBMED   1577411
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Bean,M.F. and Carr,S.A.
  TITLE     Characterization of disulfide bond position in proteins and
            sequence analysis of cystine-bridged peptides by tandem mass
            spectrometry
  JOURNAL   Anal Biochem 201 (2), 216-226 (1992)
   PUBMED   1632509
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Tricoli,J.V., Nakai,H., Byers,M.G., Rall,L.B., Bell,G.I. and
            Shows,T.B.
  TITLE     The gene for human transforming growth factor alpha is on the short
            arm of chromosome 2
  JOURNAL   Cytogenet Cell Genet 42 (1-2), 94-98 (1986)
   PUBMED   3459638
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Derynck,R., Roberts,A.B., Winkler,M.E., Chen,E.Y. and Goeddel,D.V.
  TITLE     Human transforming growth factor-alpha: precursor structure and
            expression in E. coli
  JOURNAL   Cell 38 (1), 287-297 (1984)
   PUBMED   6088071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK309066.1, BC005308.1,
            X70340.1, BM453873.1, BI760767.1 and CD369689.1.
            
            On Apr 28, 2015 this sequence version replaced XP_005264579.1.
            
            Summary: This gene encodes a growth factor that is a ligand for the
            epidermal growth factor receptor, which activates a signaling
            pathway for cell proliferation, differentiation and development.
            This protein may act as either a transmembrane-bound ligand or a
            soluble ligand. This gene has been associated with many types of
            cancers, and it may also be involved in some cases of cleft
            lip/palate. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon. This results in a distinct 5' UTR, causes
            translation initiation at an alternate start codon, and a distinct
            5' coding region, compared to variant 1. The encoded isoform (3)
            has a distinct N-terminus and is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.2304652.1,
                                           SRR14038194.10615.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..166
                     /product="protransforming growth factor alpha isoform 3
                     precursor"
                     /note="protransforming growth factor alpha; TGF-alpha"
                     /calculated_mol_wt=15182
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2626
     Region          <50..89
                     /region_name="PHA02887"
                     /note="EGF-like protein; Provisional"
                     /db_xref="CDD:165214"
     Region          <53..127
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     CDS             1..166
                     /gene="TGFA"
                     /gene_synonym="TFGA"
                     /coded_by="NM_001308158.2:206..706"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS77420.1"
                     /db_xref="GeneID:7039"
                     /db_xref="HGNC:HGNC:11765"
                     /db_xref="MIM:190170"
ORIGIN      
        1 mfkigrgald lfsellsfgg ivlaacqale nstsplsadp pvaaavvshf ndcpdshtqf
       61 cfhgtcrflv qedkpacvch sgyvgarceh adllavvaas qkkqaitalv vvsivalavl
      121 iitcvlihcc qvrkhcewcr alicrhekps allkgrtacc hsetvv
//
LOCUS       NP_001352312             180 aa            linear   PRI 20-NOV-2025
DEFINITION  AN1-type zinc finger protein 2A isoform 3 [Homo sapiens].
ACCESSION   NP_001352312 XP_016868263
VERSION     NP_001352312.1
DBSOURCE    REFSEQ: accession NM_001365383.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Pizzato Scomazzon,S., Riccio,A., Santopolo,S., Lanzilli,G.,
            Coccia,M., Rossi,A. and Santoro,M.G.
  TITLE     The Zinc-Finger AN1-Type Domain 2a Gene Acts as a Regulator of Cell
            Survival in Human Melanoma: Role of E3-Ligase cIAP2
  JOURNAL   Mol Cancer Res 17 (12), 2444-2456 (2019)
   PUBMED   31540997
  REMARK    GeneRIF: The findings identify ZFAND2A/AIRAP as a novel
            stress-regulated survival factor implicated in the stabilization of
            the antiapoptotic protein cIAP2 and as a new potential therapeutic
            target in melanoma
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Zach,L., Braunstein,I. and Stanhill,A.
  TITLE     Stress-induced start codon fidelity regulates arsenite-inducible
            regulatory particle-associated protein (AIRAP) translation
  JOURNAL   J Biol Chem 289 (30), 20706-20716 (2014)
   PUBMED   24898249
  REMARK    GeneRIF: arsenite- inducible regulatory particle-associated protein
            (AIRAP) transcript to be translationally induced during arsenite
            stress conditions.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Rossi,A., Riccio,A., Coccia,M., Trotta,E., La Frazia,S. and
            Santoro,M.G.
  TITLE     The proteasome inhibitor bortezomib is a potent inducer of zinc
            finger AN1-type domain 2a gene expression: role of heat shock
            factor 1 (HSF1)-heat shock factor 2 (HSF2) heterocomplexes
  JOURNAL   J Biol Chem 289 (18), 12705-12715 (2014)
   PUBMED   24619424
  REMARK    GeneRIF: Data indicate that both heat shock factors HSF1 and HSF2
            are recruited to the arsenite-inducible RNA-associated protein
            (AIRAP) promoter and regulate bortezomib-induced AIRAP expression.
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Rossi,A., Trotta,E., Brandi,R., Arisi,I., Coccia,M. and
            Santoro,M.G.
  TITLE     AIRAP, a new human heat shock gene regulated by heat shock factor 1
  JOURNAL   J Biol Chem 285 (18), 13607-13615 (2010)
   PUBMED   20185824
  REMARK    GeneRIF: The HSF1 binding HSE sequence in the AIRAP promoter
            critical for heat-induced transcription was identified.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091729.4.
            
            On Aug 21, 2018 this sequence version replaced XP_016868263.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.155861.1,
                                           SRR1803616.177840.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..180
                     /product="AN1-type zinc finger protein 2A isoform 3"
                     /note="arsenite inducible RNA associated protein; AN1-type
                     zinc finger protein 2A; zinc finger, AN1-type domain 2A"
                     /calculated_mol_wt=20201
     mat_peptide     1..145
                     /product="AN1-type zinc finger protein 2A.
                     /id=PRO_0000269888"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N6M9.2)"
                     /calculated_mol_wt=16477
     Region          10..46
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     Region          100..134
                     /region_name="zf-AN1"
                     /note="AN1-like Zinc finger; pfam01428"
                     /db_xref="CDD:460208"
     CDS             1..180
                     /gene="ZFAND2A"
                     /gene_synonym="AIRAP"
                     /coded_by="NM_001365383.1:279..821"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94044.1"
                     /db_xref="GeneID:90637"
                     /db_xref="HGNC:HGNC:28073"
                     /db_xref="MIM:610699"
ORIGIN      
        1 mefpdlgkhc sektckqldf lpvkcdackq dfckdhfpya ahkcpfafqk dvhvpvcplc
       61 ntpipvkkgq ipdvvvgdhi drdcdshpgk kkekiftyrc skegckkkem lqmvcaqchg
      121 nfciqhrhpl dhscrhgsrp tikagcspmt vsesrplgdf ltlapgglaq rlgywftrlm
//
LOCUS       NP_149094                686 aa            linear   PRI 20-NOV-2025
DEFINITION  rhophilin-2 [Homo sapiens].
ACCESSION   NP_149094
VERSION     NP_149094.3
DBSOURCE    REFSEQ: accession NM_033103.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Chen,H., Shen,D., Zhu,F., Ou,Q., Cheng,L. and Zhu,Y.
  TITLE     Long Noncoding RNA RP11-89K21.1 Interacts with miR-146a/b-5p to
            Promote Proliferation and Gefitinib Resistance Through Regulating
            RHPN2 and RhoA/ROCK Pathway in Lung Adenocarcinoma
  JOURNAL   Cancer Biother Radiopharm 38 (5), 282-292 (2023)
   PUBMED   33877886
  REMARK    GeneRIF: Long Noncoding RNA RP11-89K21.1 Interacts with
            miR-146a/b-5p to Promote Proliferation and Gefitinib Resistance
            Through Regulating RHPN2 and RhoA/ROCK Pathway in Lung
            Adenocarcinoma.
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Liu,Z., Fang,F., Li,J., Zhao,G., Zang,Q., Zhang,F. and Die,J.
  TITLE     [RHPN2 is highly expressed in osteosarcoma cells to promote cell
            proliferation and migration and inhibit apoptosis]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 42 (9), 1367-1373 (2022)
   PUBMED   36210710
  REMARK    GeneRIF: [RHPN2 is highly expressed in osteosarcoma cells to
            promote cell proliferation and migration and inhibit apoptosis].
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Yan,L., He,Z., Li,W., Liu,N. and Gao,S.
  TITLE     P76RBE silencing inhibits ovarian cancer cell proliferation,
            migration, and invasion via suppressing the integrin
            beta1/NF-kappaB pathway
  JOURNAL   Cell Cycle 20 (18), 1875-1889 (2021)
   PUBMED   34382920
  REMARK    GeneRIF: P76RBE silencing inhibits ovarian cancer cell
            proliferation, migration, and invasion via suppressing the integrin
            beta1/NF-kappaB pathway.
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Hawken,S.J., Greenwood,C.M., Hudson,T.J., Kustra,R., McLaughlin,J.,
            Yang,Q., Zanke,B.W. and Little,J.
  TITLE     The utility and predictive value of combinations of low penetrance
            genes for screening and risk prediction of colorectal cancer
  JOURNAL   Hum Genet 128 (1), 89-101 (2010)
   PUBMED   20437058
  REMARK    GeneRIF: Observational study of genetic testing. (HuGE Navigator)
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Niittymaki,I., Kaasinen,E., Tuupanen,S., Karhu,A., Jarvinen,H.,
            Mecklin,J.P., Tomlinson,I.P., Di Bernardo,M.C., Houlston,R.S. and
            Aaltonen,L.A.
  TITLE     Low-penetrance susceptibility variants in familial colorectal
            cancer
  JOURNAL   Cancer Epidemiol Biomarkers Prev 19 (6), 1478-1483 (2010)
   PUBMED   20501757
  REMARK    GeneRIF: Observational study of gene-disease association, gene-gene
            interaction, and gene-environment interaction. (HuGE Navigator)
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Zhan,X. and Desiderio,D.M.
  TITLE     Nitroproteins from a human pituitary adenoma tissue discovered with
            a nitrotyrosine affinity column and tandem mass spectrometry
  JOURNAL   Anal Biochem 354 (2), 279-289 (2006)
   PUBMED   16777052
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Mircescu,H., Steuve,S., Savonet,V., Degraef,C., Mellor,H.,
            Dumont,J.E., Maenhaut,C. and Pirson,I.
  TITLE     Identification and characterization of a novel activated RhoB
            binding protein containing a PDZ domain whose expression is
            specifically modulated in thyroid cells by cAMP
  JOURNAL   Eur J Biochem 269 (24), 6241-6249 (2002)
   PUBMED   12473120
  REMARK    GeneRIF: may play a key role between RhoB and potential downstream
            elements needed under stimulation of the thyrotropin/cAMP pathway
            in thyrocytes
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Peck,J.W., Oberst,M., Bouker,K.B., Bowden,E. and Burbelo,P.D.
  TITLE     The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton
            organization
  JOURNAL   J Biol Chem 277 (46), 43924-43932 (2002)
   PUBMED   12221077
  REMARK    GeneRIF: Rhophilin-2 may function normally in a Rho pathway to
            limit stress fiber formation and/or increase the turnover of
            F-actin structures in the absence of high levels of RhoA activity
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC348657.1, AJ347750.1,
            AC011449.6 and BC036447.2.
            
            On Apr 29, 2009 this sequence version replaced NP_149094.2.
            
            Summary: This gene encodes a member of the rhophilin family of
            Ras-homologous (Rho)-GTPase binding proteins. The encoded protein
            binds both GTP- and GDP-bound RhoA and GTP-bound RhoB and may be
            involved in the organization of the actin cytoskeleton. [provided
            by RefSeq, Apr 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036447.2, AK098246.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000254260.8/ ENSP00000254260.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..686
                     /product="rhophilin-2"
                     /note="76 kDa RhoB effector protein; GTP-Rho-binding
                     protein 2; rhophilin-like Rho-GTPase binding protein"
                     /calculated_mol_wt=76863
     Region          27..108
                     /region_name="HR1_Rhophilin-2"
                     /note="Protein kinase C-related kinase homology region 1
                     (HR1) Rho-binding domain of Rhophilin-2; cd11634"
                     /db_xref="CDD:212024"
     Site            order(41,44,47..48,51..52,54..55,58..59,61..62,77..78,81,
                     84..85,88)
                     /site_type="other"
                     /note="putative Rho binding site 1 [polypeptide binding]"
                     /db_xref="CDD:212024"
     Region          46..66
                     /region_name="Interaction with Rho"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUC4.1)"
     Site            order(49..50,52..53,56..57,59..60,63..64,72..73,75)
                     /site_type="other"
                     /note="putative Rho binding site 2 [polypeptide binding]"
                     /db_xref="CDD:212024"
     Region          112..496
                     /region_name="BRO1_Rhophilin_2"
                     /note="Protein-interacting Bro1-like domain of
                     RhoA-binding protein Rhophilin-2; cd09249"
                     /db_xref="CDD:185772"
     Site            order(227,230,243,246..247,291,294..295,306,309..310,480,
                     482,484,486)
                     /site_type="other"
                     /note="putative ESCRT-III binding site"
                     /db_xref="CDD:185772"
     Region          514..591
                     /region_name="PDZ_rhophilin-like"
                     /note="PDZ domain of rhophilin-1, rhophilin-2, and related
                     domains; cd06712"
                     /db_xref="CDD:467196"
     Site            order(525..531,539,542,571,575,578..579)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467196"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BWR8; propagated from
                     UniProtKB/Swiss-Prot (Q8IUC4.1)"
     CDS             1..686
                     /gene="RHPN2"
                     /gene_synonym="P76RBE; RHOBP"
                     /coded_by="NM_033103.5:37..2097"
                     /db_xref="CCDS:CCDS12427.1"
                     /db_xref="GeneID:85415"
                     /db_xref="HGNC:HGNC:19974"
                     /db_xref="MIM:617932"
ORIGIN      
        1 mtdallpaap qplekendgy frkgcnplaq tgrsklqnqr aalnqqilka vrmrtgaenl
       61 lkvatnskvr eqvrlelsfv nsdlqmlkee leglnisvgv yqnteeafti pliplglket
      121 kdvdfavvlk dfilehysed gylyedeiad lmdlrqacrt psrdeagvel lmtyfiqlgf
      181 vesrffpptr qmgllftwyd sltgvpvsqq nlllekasvl fntgalytqi gtrcdrqtqa
      241 glesaidafq raagvlnylk dtfthtpsyd mspamlsvlv kmmlaqaqes vfekislpgi
      301 rneffmlvkv aqeaakvgev yqqlhaamsq apvkenipys waslacvkah hyaalahyft
      361 aillidhqvk pgtdldhqek clsqlydhmp egltplatlk ndqqrrqlgk shlrramahh
      421 eesvreaslc kklrsievlq kvlcaaqers rltyaqhqee ddllnlidap svvakteqev
      481 diilpqfskl tvtdffqklg plsvfsankr wtpprsirft aeegdlgftl rgnapvqvhf
      541 ldpycsasva garegdyivs iqlvdckwlt lsevmkllks fgedeiemkv vslldstssm
      601 hnksatysvg mqktysmicl aiddddktdk tkkiskklsf lswgtnknrq ksastlclps
      661 vgaarpqvkk klpspfslln sdsswy
//
LOCUS       NP_001352708             284 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-1 chain isoform 16 [Homo sapiens].
ACCESSION   NP_001352708
VERSION     NP_001352708.1
DBSOURCE    REFSEQ: accession NM_001365779.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Nefedova,V.V., Kopylova,G.V., Shchepkin,D.V., Kochurova,A.M.,
            Kechko,O.I., Borzova,V.A., Ryabkova,N.S., Katrukha,I.A.,
            Mitkevich,V.A., Bershitsky,S.Y., Levitsky,D.I. and Matyushenko,A.M.
  TITLE     Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin
  JOURNAL   Int J Mol Sci 23 (24), 15723 (2022)
   PUBMED   36555368
  REMARK    GeneRIF: Impact of Troponin in Cardiomyopathy Development Caused by
            Mutations in Tropomyosin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Li,C., Hong,S., Hu,H., Liu,T., Yan,G. and Sun,D.
  TITLE     MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes to Tumor
            Growth in Colorectal Cancer via Epigenetically Silencing TPM1
  JOURNAL   Mol Cancer Res 20 (11), 1697-1708 (2022)
   PUBMED   35857351
  REMARK    GeneRIF: MYC-Induced Upregulation of Lncrna ELFN1-AS1 Contributes
            to Tumor Growth in Colorectal Cancer via Epigenetically Silencing
            TPM1.
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Teekakirikul,P., Zhu,W., Xu,X., Young,C.B., Tan,T., Smith,A.M.,
            Wang,C., Peterson,K.A., Gabriel,G.C., Ho,S., Sheng,Y., Moreau de
            Bellaing,A., Sonnenberg,D.A., Lin,J.H., Fotiou,E., Tenin,G.,
            Wang,M.X., Wu,Y.L., Feinstein,T., Devine,W., Gou,H., Bais,A.S.,
            Glennon,B.J., Zahid,M., Wong,T.C., Ahmad,F., Rynkiewicz,M.J.,
            Lehman,W.J., Keavney,B., Alastalo,T.P., Freckmann,M.L., Orwig,K.,
            Murray,S., Ware,S.M., Zhao,H., Feingold,B. and Lo,C.W.
  TITLE     Genetic resiliency associated with dominant lethal TPM1 mutation
            causing atrial septal defect with high heritability
  JOURNAL   Cell Rep Med 3 (2), 100501 (2022)
   PUBMED   35243414
  REMARK    GeneRIF: Genetic resiliency associated with dominant lethal TPM1
            mutation causing atrial septal defect with high heritability.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Cirino,A.L., Channaoui,N. and Ho,C.
  TITLE     Nonsyndromic Hypertrophic Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301725
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Chevray,P.M. and Nathans,D.
  TITLE     Protein interaction cloning in yeast: identification of mammalian
            proteins that react with the leucine zipper of Jun
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5789-5793 (1992)
   PUBMED   1631061
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Lees-Miller,J.P. and Helfman,D.M.
  TITLE     The molecular basis for tropomyosin isoform diversity
  JOURNAL   Bioessays 13 (9), 429-437 (1991)
   PUBMED   1796905
  REMARK    Review article
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Mak,A., Smillie,L.B. and Barany,M.
  TITLE     Specific phosphorylation at serine-283 of alpha tropomyosin from
            frog skeletal and rabbit skeletal and cardiac muscle
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3588-3592 (1978)
   PUBMED   278975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079328.11 and M19714.1.
            
            Summary: This gene is a member of the tropomyosin family of highly
            conserved, widely distributed actin-binding proteins involved in
            the contractile system of striated and smooth muscles and the
            cytoskeleton of non-muscle cells. Tropomyosin is composed of two
            alpha-helical chains arranged as a coiled-coil. It is polymerized
            end to end along the two grooves of actin filaments and provides
            stability to the filaments. The encoded protein is one type of
            alpha helical chain that forms the predominant tropomyosin of
            striated muscle, where it also functions in association with the
            troponin complex to regulate the calcium-dependent interaction of
            actin and myosin during muscle contraction. In smooth muscle and
            non-muscle cells, alternatively spliced transcript variants
            encoding a range of isoforms have been described. Mutations in this
            gene are associated with type 3 familial hypertrophic
            cardiomyopathy and dilated cardiomyopathy 1Y. [provided by RefSeq,
            Jun 2022].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.19118.1,
                                           SRR7410570.568064.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.2"
     Protein         1..284
                     /product="tropomyosin alpha-1 chain isoform 16"
                     /note="cardiomyopathy, hypertrophic 3; tropomyosin alpha-1
                     chain; sarcomeric tropomyosin kappa; epididymis secretory
                     protein Li 265"
                     /calculated_mol_wt=32596
     Region          1..38
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09493.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:3548719; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04692; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Region          48..282
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Region          116..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09493.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            213
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P04692; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P58771; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:17895359; propagated from
                     UniProtKB/Swiss-Prot (P09493.2)"
     CDS             1..284
                     /gene="TPM1"
                     /gene_synonym="C15orf13; CMD1Y; CMH3; HEL-S-265;
                     HTM-alpha; LVNC9; TMSA"
                     /coded_by="NM_001365779.1:84..938"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS92010.1"
                     /db_xref="GeneID:7168"
                     /db_xref="HGNC:HGNC:12010"
                     /db_xref="MIM:191010"
ORIGIN      
        1 mdaikkkmqm lkldkenald raeqaeadkk aaedrskqle delvslqkkl kgtedeldky
       61 sealkdaqek lelaekkatd aeadvaslnr riqlveeeld raqerlatal qkleeaekaa
      121 desergmkvi esraqkdeek meiqeiqlke akhiaedadr kyeevarklv iiesdlerae
      181 eraelsegkc aeleeelktv tnnlksleaq aekysqkedr yeeeikvlsd klkeaetrae
      241 faersvtkle ksiddledel yaqklkykai seeldhalnd mtsm
//
LOCUS       NP_001280034             432 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-glucuronidase isoform 4 [Homo sapiens].
ACCESSION   NP_001280034
VERSION     NP_001280034.1
DBSOURCE    REFSEQ: accession NM_001293105.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Yang,Y., Wang,Y., Wang,C., Wu,S. and Yao,D.
  TITLE     Macrophages and derived-TNF-alpha promote
            lipopolysaccharide-induced upregulation of endogenous
            beta-glucuronidase in the epithelial cells of the bile duct: A
            possible facilitator of hepatolithiasis formation
  JOURNAL   Clin Res Hepatol Gastroenterol 47 (1), 102062 (2023)
   PUBMED   36473630
  REMARK    GeneRIF: Macrophages and derived-TNF-alpha promote
            lipopolysaccharide-induced upregulation of endogenous
            beta-glucuronidase in the epithelial cells of the bile duct: A
            possible facilitator of hepatolithiasis formation.
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Kong,X., Zheng,Z., Song,G., Zhang,Z., Liu,H., Kang,J., Sun,G.,
            Sun,G., Huang,T., Li,X., Rong,D., Wang,K., Tang,W. and Xia,Y.
  TITLE     Over-Expression of GUSB Leads to Primary Resistance of Anti-PD1
            Therapy in Hepatocellular Carcinoma
  JOURNAL   Front Immunol 13, 876048 (2022)
   PUBMED   35812439
  REMARK    GeneRIF: Over-Expression of GUSB Leads to Primary Resistance of
            Anti-PD1 Therapy in Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Chojnowska,S., Ptaszynska-Sarosiek,I., Kepka,A., Szajda,S.D.,
            Waszkiewicz,N. and Zwierz,K.
  TITLE     Optimization of the method for alpha-l-fucosidase,
            beta-d-galactosidase and beta-d-glucuronidase determination in
            serum from hemolyzed blood
  JOURNAL   Adv Med Sci 63 (2), 306-311 (2018)
   PUBMED   29885630
  REMARK    GeneRIF: the beta-d-galactosidase, beta-d-glucuronidase and
            alpha-l-fucosidase activities in serums from hemolyzed blood, were
            determined.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Fratz-Berilla,E.J., Ketcham,S.A., Parhiz,H., Ashraf,M. and
            Madhavarao,C.N.
  TITLE     An improved purification method for the lysosomal storage disease
            protein beta-glucuronidase produced in CHO cells
  JOURNAL   Protein Expr Purif 140, 28-35 (2017)
   PUBMED   28734840
  REMARK    GeneRIF: We produced GUS from a CHO cell line grown in suspension
            in a 15 L perfused bioreactor and developed a three step
            purification procedure that yields approximately 99% pure enzyme
            with a recovery of more than 40%.
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Tomatsu,S., Montano,A.M., Dung,V.C., Grubb,J.H. and Sly,W.S.
  TITLE     Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis
            VII (Sly Syndrome)
  JOURNAL   Hum Mutat 30 (4), 511-519 (2009)
   PUBMED   19224584
  REMARK    GeneRIF: Study summarized information on the 49 unique,
            disease-causing mutations determined so far in the GUS gene.
            Review article
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Sun,A. and Wang,R.
  TITLE     Mucopolysaccharidosis Type VII
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38190471
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Wolfe,J.H., Sands,M.S., Barker,J.E., Gwynn,B., Rowe,L.B.,
            Vogler,C.A. and Birkenmeier,E.H.
  TITLE     Reversal of pathology in murine mucopolysaccharidosis type VII by
            somatic cell gene transfer
  JOURNAL   Nature 360 (6406), 749-753 (1992)
   PUBMED   1465145
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Tanaka,J., Gasa,S., Sakurada,K., Miyazaki,T., Kasai,M. and
            Makita,A.
  TITLE     Characterization of the subunits and sugar moiety of human
            placental and leukemic beta-glucuronidase
  JOURNAL   Biol Chem Hoppe Seyler 373 (1), 57-62 (1992)
   PUBMED   1311180
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Shipley,J.M., Miller,R.D., Wu,B.M., Grubb,J.H., Christensen,S.G.,
            Kyle,J.W. and Sly,W.S.
  TITLE     Analysis of the 5' flanking region of the human beta-glucuronidase
            gene
  JOURNAL   Genomics 10 (4), 1009-1018 (1991)
   PUBMED   1916806
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Bell,C.E. Jr., Sly,W.S. and Brot,F.E.
  TITLE     Human beta-glucuronidase deficiency mucopolysaccharidosis:
            identification of cross-reactive antigen in cultured fibroblasts of
            deficient patients by enzyme immunoassay
  JOURNAL   J Clin Invest 59 (1), 97-105 (1977)
   PUBMED   401508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC346632.1, CD014093.1,
            BC014142.2 and AA947121.1.
            
            Summary: This gene encodes a hydrolase that degrades
            glycosaminoglycans, including heparan sulfate, dermatan sulfate,
            and chondroitin-4,6-sulfate. The enzyme forms a homotetramer that
            is localized to the lysosome. Mutations in this gene result in
            mucopolysaccharidosis type VII. Alternative splicing results in
            multiple transcript variants. There are many pseudogenes of this
            locus in the human genome.[provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (4) lacks alternate exons in the
            5' coding region, compared to variant 1. The encoded protein
            (isoform 4) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD014093.1, SRR1660803.71195.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..432
                     /product="beta-glucuronidase isoform 4"
                     /EC_number="3.2.1.31"
                     /note="beta-glucuronidase; beta-D-glucuronidase; beta-G1"
                     /calculated_mol_wt=49501
     Region          <20..412
                     /region_name="Bgal_small_N"
                     /note="Beta galactosidase small chain; cl46900"
                     /db_xref="CDD:481240"
     CDS             1..432
                     /gene="GUSB"
                     /gene_synonym="BG; MPS7"
                     /coded_by="NM_001293105.2:360..1658"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:2990"
                     /db_xref="HGNC:HGNC:4696"
                     /db_xref="MIM:611499"
ORIGIN      
        1 mdpgpahksg aedwqcpflc hrglvnyqis vkgsnlfkle vrlldaenkv vangtgtqgq
       61 lkvpgvslww pylmherpay lyslevqlta qtslgpvsdf ytlpvgirtv avtksqflin
      121 gkpfyfhgvn khedadirgk gfdwpllvkd fnllrwlgan afrtshypya eevmqmcdry
      181 givvidecpg vglalpqffn nvslhhhmqv meevvrrdkn hpavvmwsva nepashlesa
      241 gyylkmviah tksldpsrpv tfvsnsnyaa dkgapyvdvi clnsyyswyh dyghleliql
      301 qlatqfenwy kkyqkpiiqs eygaetiagf hqdpplmfte eyqkslleqy hlgldqkrrk
      361 yvvgeliwnf adfmteqspt rvlgnkkgif trqrqpksaa fllrerywki anetryphsv
      421 aksqclensl ft
//
LOCUS       NP_001354453             510 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 17 [Homo sapiens].
ACCESSION   NP_001354453 XP_016872223
VERSION     NP_001354453.1
DBSOURCE    REFSEQ: accession NM_001367524.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872223.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.93845.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..510
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 17"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=55679
     Region          <11..221
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          351..>406
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..510
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367524.1:286..1818"
                     /note="isoform 17 is encoded by transcript variant 17"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mstsetskhr vtggelfedi vareyysead ashcihqile svnhihqhdi vhrdlkpenl
       61 llaskckgaa vkladfglai evqgeqqawf gfagtpgyls pevlrkdpyg kpvdiwacgv
      121 ilyillvgyp pfwdedqhkl yqqikagayd fpspewdtvt peaknlinqm ltinpakrit
      181 adqalkhpwv cqrstvasmm hrqetveclr kfnarrklkg ailttmlvsr nfsvgrqssa
      241 paspaasaag lagqaaksll nkksdggvkk rkssssvhlm epqttvvhna tdgikgstes
      301 cntttededl kaaplrtgng ssvpegrssr drtapsagmq pqpslcssam rkqeiikite
      361 qlieainngd feaytkicdp gltsfepeal gnlvegmdfh kfyfenrewv raadillpap
      421 lplclclllt fssqlptfpl fdlraalllc mlvplcpdgc rqaplkalll sskchsfcsc
      481 fvavpvttik ltyflpgava yacnpntlgg
//
LOCUS       NP_004940                847 aa            linear   PRI 20-NOV-2025
DEFINITION  desmocollin-2 isoform Dsc2b preproprotein [Homo sapiens].
ACCESSION   NP_004940
VERSION     NP_004940.1
DBSOURCE    REFSEQ: accession NM_004949.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Han,J.Y., Che,N., Mo,J., Zhang,D.F., Liang,X.H., Dong,X.Y.,
            Zhao,X.L. and Sun,B.C.
  TITLE     Desmoglein 2 and desmocollin 2 depletions promote malignancy
            through distinct mechanisms in triple-negative and luminal breast
            cancer
  JOURNAL   BMC Cancer 24 (1), 532 (2024)
   PUBMED   38671389
  REMARK    GeneRIF: Desmoglein 2 and desmocollin 2 depletions promote
            malignancy through distinct mechanisms in triple-negative and
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Sun,C., Wen,K., Zhang,B., Dong,Y., Chen,C., Neo,S.Y., Leng,B.,
            Gao,T.T. and Wu,J.
  TITLE     DSC2 suppresses the growth of gastric cancer through the inhibition
            of nuclear translocation of gamma-catenin and PTEN/PI3K/AKT
            signaling pathway
  JOURNAL   Aging (Albany NY) 15 (13), 6380-6399 (2023)
   PUBMED   37421607
  REMARK    GeneRIF: DSC2 suppresses the growth of gastric cancer through the
            inhibition of nuclear translocation of gamma-catenin and
            PTEN/PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Pariyar,M., Thorne,R.F., Scott,R.J. and Avery-Kiejda,K.A.
  TITLE     Verification and Validation of a Four-Gene Panel as a Prognostic
            Indicator in Triple Negative Breast Cancer
  JOURNAL   Front Oncol 12, 821334 (2022)
   PUBMED   35387118
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 847)
  AUTHORS   Syrris,P., Ward,D., Evans,A., Asimaki,A., Gandjbakhch,E.,
            Sen-Chowdhry,S. and McKenna,W.J.
  TITLE     Arrhythmogenic right ventricular dysplasia/cardiomyopathy
            associated with mutations in the desmosomal gene desmocollin-2
  JOURNAL   Am J Hum Genet 79 (5), 978-984 (2006)
   PUBMED   17033975
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Nuber,U.A., Schafer,S., Schmidt,A., Koch,P.J. and Franke,W.W.
  TITLE     The widespread human desmocollin Dsc2 and tissue-specific patterns
            of synthesis of various desmocollin subtypes
  JOURNAL   Eur J Cell Biol 66 (1), 69-74 (1995)
   PUBMED   7750520
REFERENCE   7  (residues 1 to 847)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Arnemann,J., Spurr,N.K., Wheeler,G.N., Parker,A.E. and Buxton,R.S.
  TITLE     Chromosomal assignment of the human genes coding for the major
            proteins of the desmosome junction, desmoglein DGI (DSG),
            desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and
            plakoglobin DPIII (JUP)
  JOURNAL   Genomics 10 (3), 640-645 (1991)
   PUBMED   1889810
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Parker,A.E., Wheeler,G.N., Arnemann,J., Pidsley,S.C., Ataliotis,P.,
            Thomas,C.L., Rees,D.A., Magee,A.I. and Buxton,R.S.
  TITLE     Desmosomal glycoproteins II and III. Cadherin-like junctional
            molecules generated by alternative splicing
  JOURNAL   J Biol Chem 266 (16), 10438-10445 (1991)
   PUBMED   2037591
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Garrod,D.R. and Fleming,S.
  TITLE     Early expression of desmosomal components during kidney tubule
            morphogenesis in human and murine embryos
  JOURNAL   Development 108 (2), 313-321 (1990)
   PUBMED   2112455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC382631.1, X56807.1,
            BC063291.1, BE350090.1 and AC012417.13.
            
            Summary: This gene encodes a member of the desmocollin protein
            subfamily. Desmocollins, along with desmogleins, are cadherin-like
            transmembrane glycoproteins that are major components of the
            desmosome. Desmosomes are cell-cell junctions that help resist
            shearing forces and are found in high concentrations in cells
            subject to mechanical stress. This gene is found in a cluster with
            other desmocollin family members on chromosome 18. Mutations in
            this gene are associated with arrhythmogenic right ventricular
            dysplasia-11, and reduced protein expression has been described in
            several types of cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (Dsc2b, also known as DGIII)
            contains an additional exon at the 3' end compared to transcript
            variant Dsc2a. This results in a frame-shift and a shorter isoform
            (Dsc2b) with a distinct C-terminus compared to isoform Dsc2a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X56807.1, SRR18074969.2194697.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..847
                     /product="desmocollin-2 isoform Dsc2b preproprotein"
                     /note="desmosomal glycoprotein II/III; cadherin family
                     member 2"
                     /calculated_mol_wt=90512
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3275
     Region          31..111
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; smart01055"
                     /db_xref="CDD:214999"
     Region          140..234
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          247..351
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(254..255,312,314,347,349..350)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          360..463
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(366..367,424,426,464,466..467)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          477..573
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(482..483,534,536,569,571..572)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     CDS             1..847
                     /gene="DSC2"
                     /gene_synonym="ARVD11; CDHF2; DG2; DGII/III; DSC3"
                     /coded_by="NM_004949.5:451..2994"
                     /note="isoform Dsc2b preproprotein is encoded by
                     transcript variant Dsc2b"
                     /db_xref="CCDS:CCDS11893.1"
                     /db_xref="GeneID:1824"
                     /db_xref="HGNC:HGNC:3036"
                     /db_xref="MIM:125645"
ORIGIN      
        1 meaarpsgsw ngalcrllll tlailifasd acknvtlhvp skldaeklvg rvnlkecfta
       61 anlihssdpd fqiledgsvy ttntillsse krsftillsn tenqekkkif vflehqtkvl
      121 kkrhtkekvl rrakrrwapi pcsmlenslg pfplflqqvq sdtaqnytiy ysirgpgvdq
      181 eprnlfyver dtgnlyctrp vdreqyesfe iiafattpdg ytpelplpli ikiedendny
      241 pifteetytf tifencrvgt tvgqvcatdk depdtmhtrl kysiigqvpp sptlfsmhpt
      301 tgvitttssq ldrelidkyq lkikvqdmdg qyfglqttst ciiniddvnd hlptftrtsy
      361 vtsveentvd veilrvtved kdlvntanwr anytilkgne ngnfkivtda ktnegvlcvv
      421 kplnyeekqq milqigvvne apfsreaspr samstatvtv nvedqdegpe cnppiqtvrm
      481 kenaevgtts ngykaydpet rsssgirykk ltdptgwvti dentgsikvf rsldreaeti
      541 kngiynitvl asdqggrtct gtlgiilqdv ndnspfipkk tviickptms saeivavdpd
      601 epihgppfdf slesstsevq rmwrlkaind taarlsyqnd ppfgsyvvpi tvrdrlgmss
      661 vtsldvtlcd citendcthr vdpriggggv qlgkwailai llgiallfci lftlvcgasg
      721 tskqpkvipd dlaqqnlivs nteapgddkv ysangfttqt vgasaqgvcg tvgsgikngg
      781 qetiemvkgg hqtsescrga ghhhtldscr gghtevdncr ytysewhsft qprlgeesir
      841 ghtlikn
//
LOCUS       NP_001305636             500 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of MON1-CCZ1 complex isoform 3 [Homo sapiens].
ACCESSION   NP_001305636
VERSION     NP_001305636.1
DBSOURCE    REFSEQ: accession NM_001318707.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Yong,X., Jia,G., Liu,Z., Zhou,C., Yi,J., Tang,Y., Chen,L., Chen,L.,
            Wang,Y., Sun,Q., Billadeau,D.D., Su,Z. and Jia,D.
  TITLE     Cryo-EM structure of the Mon1-Ccz1-RMC1 complex reveals molecular
            basis of metazoan RAB7A activation
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2301725120 (2023)
   PUBMED   37216550
REFERENCE   2  (residues 1 to 500)
  AUTHORS   van den Boomen,D.J.H., Sienkiewicz,A., Berlin,I., Jongsma,M.L.M.,
            van Elsland,D.M., Luzio,J.P., Neefjes,J.J.C. and Lehner,P.J.
  TITLE     A trimeric Rab7 GEF controls NPC1-dependent lysosomal cholesterol
            export
  JOURNAL   Nat Commun 11 (1), 5559 (2020)
   PUBMED   33144569
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Vaites,L.P., Paulo,J.A., Huttlin,E.L. and Harper,J.W.
  TITLE     Systematic Analysis of Human Cells Lacking ATG8 Proteins Uncovers
            Roles for GABARAPs and the CCZ1/MON1 Regulator C18orf8/RMC1 in
            Macroautophagic and Selective Autophagic Flux
  JOURNAL   Mol Cell Biol 38 (1), e00392-17 (2017)
   PUBMED   29038162
  REMARK    GeneRIF: Authors identified C18orf8/RMC1 as a new subunit of the
            CCZ1-MON1 RAB7 guanine exchange factor (GEF) that positively
            regulates RAB7 recruitment to LE/autophagosomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Yuan,M., Chen,J. and Zeng,Z.
  TITLE     Knockdown of macrophage inhibitory cytokine-1 in RPMI-8226 human
            multiple myeloma cells inhibits osteoclastic differentiation
            through inhibiting the RANKL-Erk1/2 signaling pathway
  JOURNAL   Mol Med Rep 14 (6), 5199-5204 (2016)
   PUBMED   27779672
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026634.11, AK294169.1, AC010853.11 and BC008305.1.
            
            Summary: This gene encodes a colon cancer associated protein.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (3) lacks three exons in its 5'
            UTR and uses a downstream in-frame start codon, compared to variant
            1. The encoded isoform (3) has a shorter N-terminus than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294169.1, SRR1803611.159603.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..500
                     /product="regulator of MON1-CCZ1 complex isoform 3"
                     /note="colon cancer-associated protein Mic1; macrophage
                     inhibitory cytokine 1; uncharacterized protein C18orf8; WD
                     repeat domain 98; WD repeat-containing protein 98;
                     regulator of MON1-CCZ1 complex"
                     /calculated_mol_wt=56838
     Region          318..475
                     /region_name="Mic1"
                     /note="Colon cancer-associated protein Mic1-like;
                     pfam07035"
                     /db_xref="CDD:429257"
     CDS             1..500
                     /gene="RMC1"
                     /gene_synonym="C18orf8; HsT2591; Mic-1; MIC1; WDR98"
                     /coded_by="NM_001318707.1:392..1894"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:29919"
                     /db_xref="HGNC:HGNC:24326"
                     /db_xref="MIM:620267"
ORIGIN      
        1 mycpesavil lsttvlenvl qpfhfragtm sklpkfeiel paapkstkps lserdiamat
       61 iygqlyvlfl rhhsrtsnst gaevvlyhlp regackkmhi lklnrtgkfa lnvvdnlvvv
      121 hhqdtetsvi fdiklrgefd gsvtfhhpvl parsiqpyqi pitgpaavts qspvpcklys
      181 sswivfqpdi iisasqgylw nlqvklepiv nllpdkgrlm dfllqrkeck mvilsvcsqm
      241 lsesdraslp viatvfdkln heykkyldae qsyamaveag qsrsspllkr pvrtqavldq
      301 sdvythvlsa fvekkemphk fviavlmeyi rslnqfqiav qhylhelvik tlvqhnlfym
      361 lhqflqyhvl sdskplacll lslesfyppa hqlsldmlkr lstandeive vllskhqvla
      421 alrfirgigg hdnisarkfl daakqtednm lfytifrffe qrnqrlrgsp nftpgehcee
      481 hvaffkqifg dqalmrpttf
//
LOCUS       NP_001308147             166 aa            linear   PRI 20-NOV-2025
DEFINITION  B9 domain-containing protein 1 isoform h [Homo sapiens].
ACCESSION   NP_001308147 XP_011522096
VERSION     NP_001308147.1
DBSOURCE    REFSEQ: accession NM_001321218.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Okazaki,M., Kobayashi,T., Chiba,S., Takei,R., Liang,L., Nakayama,K.
            and Katoh,Y.
  TITLE     Formation of the B9-domain protein complex MKS1-B9D2-B9D1 is
            essential as a diffusion barrier for ciliary membrane proteins
  JOURNAL   Mol Biol Cell 31 (20), 2259-2268 (2020)
   PUBMED   32726168
  REMARK    GeneRIF: Formation of the B9-domain protein complex MKS1-B9D2-B9D1
            is essential as a diffusion barrier for ciliary membrane proteins.
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Hopp,K., Heyer,C.M., Hommerding,C.J., Henke,S.A., Sundsbak,J.L.,
            Patel,S., Patel,P., Consugar,M.B., Czarnecki,P.G., Gliem,T.J.,
            Torres,V.E., Rossetti,S. and Harris,P.C.
  TITLE     B9D1 is revealed as a novel Meckel syndrome (MKS) gene by targeted
            exon-enriched next-generation sequencing and deletion analysis
  JOURNAL   Hum Mol Genet 20 (13), 2524-2534 (2011)
   PUBMED   21493627
  REMARK    GeneRIF: B9D1 is a novel Meckel syndrome gene
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Bialas,N.J., Inglis,P.N., Li,C., Robinson,J.F., Parker,J.D.,
            Healey,M.P., Davis,E.E., Inglis,C.D., Toivonen,T., Cottell,D.C.,
            Blacque,O.E., Quarmby,L.M., Katsanis,N. and Leroux,M.R.
  TITLE     Functional interactions between the ciliopathy-associated Meckel
            syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR)
            proteins
  JOURNAL   J Cell Sci 122 (Pt 5), 611-624 (2009)
   PUBMED   19208769
  REMARK    GeneRIF: MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1/EPPB9,
            MKSR-2/B9D2), localize to transition zones/basal bodies of sensory
            cilia; subcellular localization is largely co-dependent, pointing
            to a functional relationship between the proteins
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Williams,C.L., Winkelbauer,M.E., Schafer,J.C., Michaud,E.J. and
            Yoder,B.K.
  TITLE     Functional redundancy of the B9 proteins and nephrocystins in
            Caenorhabditis elegans ciliogenesis
  JOURNAL   Mol Biol Cell 19 (5), 2154-2168 (2008)
   PUBMED   18337471
  REMARK    GeneRIF: Ciliary transition zone localization.  Functions in a
            module with related proteins (MKS1 and B9D1) that cooperates with
            nephrocystins in ciliogenesis.
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY047032.1, AB030506.1,
            AC124066.6 and CA312151.1.
            
            On Mar 18, 2016 this sequence version replaced XP_011522096.1.
            
            Summary: This gene encodes a B9 domain-containing protein, one of
            several that are involved in ciliogenesis. Alterations in
            expression of this gene have been found in a family with Meckel
            syndrome. Meckel syndrome has been associated with at least six
            different genes. This gene is located within the Smith-Magenis
            syndrome region on chromosome 17. [provided by RefSeq, Mar 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.173319.1,
                                           SRR1803616.33241.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..166
                     /product="B9 domain-containing protein 1 isoform h"
                     /note="endothelial precursor protein B9; B9
                     domain-containing protein 1; MKS1-related protein 1; B9
                     protein domain 1"
                     /calculated_mol_wt=18572
     Region          11..159
                     /region_name="B9-C2"
                     /note="Ciliary basal body-associated, B9 protein;
                     pfam07162"
                     /db_xref="CDD:462108"
     CDS             1..166
                     /gene="B9D1"
                     /gene_synonym="B9; EPPB9; JBTS27; MKS9; MKSR-1; MKSR1"
                     /coded_by="NM_001321218.2:155..655"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:27077"
                     /db_xref="HGNC:HGNC:24123"
                     /db_xref="MIM:614144"
ORIGIN      
        1 mataspsvfl lmvngqvesa qfpeyddlyc kycfvygqdw aptagleegi sqitsksqdv
       61 rqalvwnfpi dvtfkstnpy gwpqivlsvy gpdvfgndvv rgygavhvpf spgrhkrtip
      121 mfvpestskl qkftswfmgr rpeytdpkvv aqgegreatf ravcqr
//
LOCUS       NP_060391                608 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear protein localization protein 4 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_060391
VERSION     NP_060391.2
DBSOURCE    REFSEQ: accession NM_017921.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 608)
  AUTHORS   Bekkari,H., Benmakhlouf,Y., Nourouti,N.G., Barakat,A. and
            Mechita,M.B.
  TITLE     Study of Clinical Characteristics of Intellectual Disability in
            Morocco
  JOURNAL   Innov Clin Neurosci 21 (7-9), 10-14 (2024)
   PUBMED   39329031
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 608)
  AUTHORS   Wang,N., Zhu,D., Liu,Y., Wu,J., Wang,M., Jin,S., Fu,F., Li,B.,
            Ji,H., Du,C. and Zheng,Z.
  TITLE     NPLOC4 is a potential target and a poor prognostic signature in
            lung squamous cell carcinoma
  JOURNAL   Sci Rep 13 (1), 20430 (2023)
   PUBMED   37993584
  REMARK    GeneRIF: NPLOC4 is a potential target and a poor prognostic
            signature in lung squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 608)
  AUTHORS   Tsioras,K., Smith,K.C., Edassery,S.L., Garjani,M., Li,Y.,
            Williams,C., McKenna,E.D., Guo,W., Wilen,A.P., Hark,T.J.,
            Marklund,S.L., Ostrow,L.W., Gilthorpe,J.D., Ichida,J.K., Kalb,R.G.,
            Savas,J.N. and Kiskinis,E.
  TITLE     Analysis of proteome-wide degradation dynamics in ALS SOD1
            iPSC-derived patient neurons reveals disrupted VCP homeostasis
  JOURNAL   Cell Rep 42 (10), 113160 (2023)
   PUBMED   37776851
REFERENCE   4  (residues 1 to 608)
  AUTHORS   Nguyen,T.Q., My Le,L.T., Kim,D.H., Ko,K.S., Lee,H.T., Kim
            Nguyen,Y.T., Kim,H.S., Han,B.W., Kang,W. and Yang,J.K.
  TITLE     Structural basis for the interaction between human Npl4 and
            Npl4-binding motif of human Ufd1
  JOURNAL   Structure 30 (11), 1530-1537 (2022)
   PUBMED   36087575
  REMARK    GeneRIF: Structural basis for the interaction between human Npl4
            and Npl4-binding motif of human Ufd1.
REFERENCE   5  (residues 1 to 608)
  AUTHORS   Fujisawa,R., Polo Rivera,C. and Labib,K.P.M.
  TITLE     Multiple UBX proteins reduce the ubiquitin threshold of the
            mammalian p97-UFD1-NPL4 unfoldase
  JOURNAL   Elife 11, e76763 (2022)
   PUBMED   35920641
  REMARK    GeneRIF: Multiple UBX proteins reduce the ubiquitin threshold of
            the mammalian p97-UFD1-NPL4 unfoldase.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 608)
  AUTHORS   McConnell,E., Lass,A. and Wojcik,C.
  TITLE     Ufd1-Npl4 is a negative regulator of cholera toxin
            retrotranslocation
  JOURNAL   Biochem Biophys Res Commun 355 (4), 1087-1090 (2007)
   PUBMED   17331469
  REMARK    GeneRIF: Ufd1-Npl4 is a negative regulator of retrotranslocation,
            delaying the retrotranslocation of endoplasmic reticulum-associated
            degradation substrates independently of its association with VCP
REFERENCE   7  (residues 1 to 608)
  AUTHORS   Arrigoni,R., Alam,S.L., Wamstad,J.A., Bardwell,V.J., Sundquist,W.I.
            and Schreiber-Agus,N.
  TITLE     The Polycomb-associated protein Rybp is a ubiquitin binding protein
  JOURNAL   FEBS Lett 580 (26), 6233-6241 (2006)
   PUBMED   17070805
  REMARK    Erratum:[FEBS Lett. 2006 Dec 11;580(28-29):6754]
REFERENCE   8  (residues 1 to 608)
  AUTHORS   Gevaert,K., Goethals,M., Martens,L., Van Damme,J., Staes,A.,
            Thomas,G.R. and Vandekerckhove,J.
  TITLE     Exploring proteomes and analyzing protein processing by mass
            spectrometric identification of sorted N-terminal peptides
  JOURNAL   Nat Biotechnol 21 (5), 566-569 (2003)
   PUBMED   12665801
REFERENCE   9  (residues 1 to 608)
  AUTHORS   Botta,A., Tandoi,C., Fini,G., Calabrese,G., Dallapiccola,B. and
            Novelli,G.
  TITLE     Cloning and characterization of the gene encoding human NPL4, a
            protein interacting with the ubiquitin fusion-degradation protein
            (UFD1L)
  JOURNAL   Gene 275 (1), 39-46 (2001)
   PUBMED   11574150
REFERENCE   10 (residues 1 to 608)
  AUTHORS   Meyer,H.H., Shorter,J.G., Seemann,J., Pappin,D. and Warren,G.
  TITLE     A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
            ubiquitin and nuclear transport pathways
  JOURNAL   EMBO J 19 (10), 2181-2192 (2000)
   PUBMED   10811609
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY116973.1, BC025930.1, AB040932.1, AK000664.1 and AC137896.5.
            
            On Sep 22, 2007 this sequence version replaced NP_060391.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000664.1, SRR1803614.16377.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331134.11/ ENSP00000331487.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..608
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..608
                     /product="nuclear protein localization protein 4 homolog
                     isoform 1"
                     /note="nuclear protein localization protein 4 homolog;
                     nuclear protein localization 4 homolog; NPLOC4 ubiquitin
                     recognition factor"
                     /calculated_mol_wt=67989
     Region          1..80
                     /region_name="UN_NPL4"
                     /note="Nuclear pore localization protein NPL4; pfam11543"
                     /db_xref="CDD:431926"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          105..245
                     /region_name="zf-NPL4"
                     /note="NPL4 family, putative zinc binding region;
                     pfam05020"
                     /db_xref="CDD:461523"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60670; propagated from
                     UniProtKB/Swiss-Prot (Q8TAT6.3)"
     Region          249..555
                     /region_name="NPL4"
                     /note="NPL4 family; pfam05021"
                     /db_xref="CDD:461524"
     Region          584..603
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     CDS             1..608
                     /gene="NPLOC4"
                     /gene_synonym="NPL4"
                     /coded_by="NM_017921.4:183..2009"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45812.1"
                     /db_xref="GeneID:55666"
                     /db_xref="HGNC:HGNC:18261"
                     /db_xref="MIM:606590"
ORIGIN      
        1 maesiiirvq spdgvkrita tkretaatfl kkvakefgfq nngfsvyinr nktgeitass
       61 nkslnllkik hgdllflfps slagpsseme tsvppgfkvf gapnvvedei dqylskqdgk
      121 iyrsrdpqlc rhgplgkcvh cvplepfded ylnhleppvk hmsfhayirk ltggadkgkf
      181 valeniscki ksgceghlpw pngictkcqp saitlnrqky rhvdnimfen htvadrfldf
      241 wrktgnqhfg ylygrytehk diplgiraev aaiyeppqig tqnslelled pkaevvdeia
      301 aklglrkvgw iftdlvsedt rkgtvrysrn kdtyflssee citagdfqnk hpnmcrlspd
      361 ghfgskfvta vatggpdnqv hfegyqvsnq cmalvrdecl lpckdapelg yakessseqy
      421 vpdvfykdvd kfgneitqla rplpveylii ditttfpkdp vytfsisqnp fpienrdvlg
      481 etqdfhslat ylsqntssvf ldtisdfhll lflvtnevmp lqdsisllle avrtrneela
      541 qtwkrseqwa tieqlcstvg gqlpglheyg avggsthtat aamwacqhct fmnqpgtghc
      601 emcslprt
//
LOCUS       NP_001429                458 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 1 [Homo sapiens].
ACCESSION   NP_001429
VERSION     NP_001429.2
DBSOURCE    REFSEQ: accession NM_001438.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB020639.1 and BU752915.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 18, 2004 this sequence version replaced NP_001429.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY388456.1, AB020639.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000408911.8/ ENSP00000386171.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..458
                     /product="estrogen-related receptor gamma isoform 1"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=51175
     Region          42..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62508.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000305|PubMed:18063693,
                     ECO:0000305|PubMed:19067653; propagated from
                     UniProtKB/Swiss-Prot (P62508.1)"
     Region          122..218
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(126,138..141,146..147,149..151,153..154,157,
                     177..178,181,184,198..199,202..209)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(128,131,145,148,164,170,180,183)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          237..456
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(265,268,272,275,313,326,330,340..342,435,438,440)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(280,294,297..298,301..302,448..449,452..453)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            376
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..458
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001438.4:131..1507"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41468.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 mdsvelclpe sfslhyeeel lcrmsnkdrh idsscssfik tepsspaslt dsvnhhspgg
       61 ssdasgsyss tmnghqngld spplypsapi lggsgpvrkl yddcsstive dpqtkceyml
      121 nsmpkrlclv cgdiasgyhy gvasceacka ffkrtiqgni eyscpatnec eitkrrrksc
      181 qacrfmkclk vgmlkegvrl drvrggrqky krridaensp ylnpqlvqpa kkpynkivsh
      241 llvaepekiy ampdptvpds dikalttlcd ladrelvvii gwakhipgfs tlsladqmsl
      301 lqsawmeili lgvvyrslsf edelvyaddy imdedqskla glldlnnail qlvkkyksmk
      361 lekeefvtlk aialansdsm hiedveavqk lqdvlhealq dyeagqhmed prragkmlmt
      421 lpllrqtstk avqhfynikl egkvpmhklf lemleakv
//
LOCUS       NP_001020413             682 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor-associated kinase 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001020413
VERSION     NP_001020413.1
DBSOURCE    REFSEQ: accession NM_001025242.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Rao,Z., Ao,G., Zhang,Y., Jiang,Z., Li,L. and Hua,Z.
  TITLE     HNRNP I promotes IRAK1 degradation to reduce podocyte apoptosis and
            inflammatory response alleviating renal injury in diabetic
            nephropathy
  JOURNAL   Immunobiology 229 (5), 152835 (2024)
   PUBMED   38986278
  REMARK    GeneRIF: HNRNP I promotes IRAK1 degradation to reduce podocyte
            apoptosis and inflammatory response alleviating renal injury in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Fisch,D., Zhang,T., Sun,H., Ma,W., Tan,Y., Gygi,S.P., Higgins,D.E.
            and Kagan,J.C.
  TITLE     Molecular definition of the endogenous Toll-like receptor
            signalling pathways
  JOURNAL   Nature 631 (8021), 635-644 (2024)
   PUBMED   38961291
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Chen,J.J., Lu,T.Z., Wang,T., Yan,W.H., Zhong,F.Y., Qu,X.H.,
            Gong,X.C., Li,J.G., Tou,F.F., Jiang,L.P. and Han,X.J.
  TITLE     The m6A reader HNRNPC promotes glioma progression by enhancing the
            stability of IRAK1 mRNA through the MAPK pathway
  JOURNAL   Cell Death Dis 15 (6), 390 (2024)
   PUBMED   38830885
  REMARK    GeneRIF: The m6A reader HNRNPC promotes glioma progression by
            enhancing the stability of IRAK1 mRNA through the MAPK pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Liu,Y., Yuan,J., Zhang,Y., Qin,F., Bai,X., Sun,W., Chen,T., Liu,F.,
            Zheng,Y., Qi,X., Zhao,W., Liu,B. and Gao,C.
  TITLE     OTUD5 promotes the inflammatory immune response by enhancing MyD88
            oligomerization and Myddosome formation
  JOURNAL   Cell Death Differ 31 (6), 753-767 (2024)
   PUBMED   38605168
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Zhou,M., Liu,Y., Xu,H., Chen,X., Zheng,N., Duan,Z., Ge,Y., Li,D.,
            Lin,T., Zeng,R., Chen,Q. and Li,M.
  TITLE     YTHDC1-Modified m6A Methylation of Hsa_circ_0102678 Promotes
            Keratinocyte Inflammation Induced by Cutibacterium acnes Biofilm
            through Regulating miR-146a/TRAF6 and IRAK1 Axis
  JOURNAL   J Innate Immun 15 (1), 822-835 (2023)
   PUBMED   37903473
  REMARK    GeneRIF: YTHDC1-Modified m6A Methylation of Hsa_circ_0102678
            Promotes Keratinocyte Inflammation Induced by Cutibacterium acnes
            Biofilm through Regulating miR-146a/TRAF6 and IRAK1 Axis.
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Muzio,M., Ni,J., Feng,P. and Dixit,V.M.
  TITLE     IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators
            of IL-1 signaling
  JOURNAL   Science 278 (5343), 1612-1615 (1997)
   PUBMED   9374458
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   8  (residues 1 to 682)
  AUTHORS   DiDonato,J.A., Hayakawa,M., Rothwarf,D.M., Zandi,E. and Karin,M.
  TITLE     A cytokine-responsive IkappaB kinase that activates the
            transcription factor NF-kappaB
  JOURNAL   Nature 388 (6642), 548-554 (1997)
   PUBMED   9252186
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Cao,Z., Henzel,W.J. and Gao,X.
  TITLE     IRAK: a kinase associated with the interleukin-1 receptor
  JOURNAL   Science 271 (5252), 1128-1131 (1996)
   PUBMED   8599092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U52112.2, L76191.1, BC054000.1,
            AF346607.1 and BC014963.1.
            
            Summary: This gene encodes the interleukin-1 receptor-associated
            kinase 1, one of two putative serine/threonine kinases that become
            associated with the interleukin-1 receptor (IL1R) upon stimulation.
            This gene is partially responsible for IL1-induced upregulation of
            the transcription factor NF-kappa B. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame segment in
            the CDS, as compared to variant 1. The encoded isoform 2 thus lacks
            an internal segment, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1100013.1, AF346607.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..682
                     /product="interleukin-1 receptor-associated kinase 1
                     isoform 2"
                     /EC_number="2.7.11.1"
                     /note="Pelle homolog"
                     /calculated_mol_wt=73290
     Region          17..100
                     /region_name="Death_IRAK1"
                     /note="Death domain of Interleukin 1 Receptor Associated
                     Kinase-1; cd08794"
                     /db_xref="CDD:260061"
     Site            order(19..20,22..25,58,67..68,71..77,82)
                     /site_type="other"
                     /note="putative IRAK1-IRAK4 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:260061"
     Region          218..513
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(218..221,224,226,237,239,272,288..291,340,344..345,
                     347,357..358)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..682
                     /gene="IRAK1"
                     /gene_synonym="IRAK; pelle"
                     /coded_by="NM_001025242.2:91..2139"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS35444.1"
                     /db_xref="GeneID:3654"
                     /db_xref="HGNC:HGNC:6112"
                     /db_xref="MIM:300283"
ORIGIN      
        1 maggpgpgep aapgaqhfly evppwvmcrf ykvmdalepa dwcqfaaliv rdqtelrlce
       61 rsgqrtasvl wpwinrnarv adlvhilthl qllrardiit awhppaplps pgttaprpss
      121 ipapaeaeaw sprklpssas tflspafpgs qthsgpelgl vpspaslwpp ppspapsstk
      181 pgpessvsll qgarpfpfcw plceisrgth nfseelkige ggfgcvyrav mrntvyavkr
      241 lkenadlewt avkqsfltev eqlsrfrhpn ivdfagycaq ngfyclvygf lpngsledrl
      301 hcqtqacppl swpqrldill gtaraiqflh qdspslihgd ikssnvllde rltpklgdfg
      361 larfsrfags spsqssmvar tqtvrgtlay lpeeyiktgr lavdtdtfsf gvvvletlag
      421 qravkthgar tkylkdlvee eaeeagvalr stqstlqagl aadawaapia mqiykkhldp
      481 rpgpcppelg lglgqlaccc lhrrakrrpp mtqensyvss tgrahsgaap wqplaapsga
      541 saqaaeqlqr gpnqpvesde slgglsaalr swhltpscpl dpaplreagc pqgdtagess
      601 wgsgpgsrpt aveglalgss asssseppqi iinparqkmv qklalyedga ldslqllsss
      661 slpglgleqd rqgpeesdef qs
//
LOCUS       NP_001308515             511 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 25 [Homo sapiens].
ACCESSION   NP_001308515
VERSION     NP_001308515.1
DBSOURCE    REFSEQ: accession NM_001321586.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 511)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.190719.1,
                                           SRR1803615.210858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..511
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 25"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57546
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          379..506
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..511
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321586.2:671..2206"
                     /note="isoform 25 is encoded by transcript variant 27"
                     /db_xref="CCDS:CCDS93606.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkinn kanvvtspke niptpalepq ttvihnpdgn
      361 kestessntt iededvkark qeiikvteql ieainngdfe aytkicdpgl tafepealgn
      421 lvegmdfhrf yfenalsksn kpihtiilnp hvhlvgddaa ciayirltqy mdgsgmpktm
      481 qseetrvwhr rdgkwqnvhf hrsgsptvpi n
//
LOCUS       NP_079481                178 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 28 [Homo
            sapiens].
ACCESSION   NP_079481
VERSION     NP_079481.2
DBSOURCE    REFSEQ: accession NM_025205.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Huang,C.Y., Weng,Y.T., Hsieh,N.T., Li,P.C., Lee,T.Y., Li,C.I.,
            Liu,H.S. and Lee,M.F.
  TITLE     Bioactive Vitamin D Attenuates MED28-Mediated Cell Growth and
            Epithelial-Mesenchymal Transition in Human Colorectal Cancer Cells
  JOURNAL   Biomed Res Int 2022, 2268818 (2022)
   PUBMED   36072467
  REMARK    GeneRIF: Bioactive Vitamin D Attenuates MED28-Mediated Cell Growth
            and Epithelial-Mesenchymal Transition in Human Colorectal Cancer
            Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Liu,C., Zhang,L., Shao,Z.M., Beatty,P., Sartippour,M., Lane,T.F.,
            Barsky,S.H., Livingston,E. and Nguyen,M.
  TITLE     Identification of a novel endothelial-derived gene EG-1
  JOURNAL   Biochem Biophys Res Commun 290 (1), 602-612 (2002)
   PUBMED   11779215
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Rozovskaia,T., Rozenblatt-Rosen,O., Sedkov,Y., Burakov,D., Yano,T.,
            Nakamura,T., Petruck,S., Ben-Simchon,L., Croce,C.M., Mazo,A. and
            Canaani,E.
  TITLE     Self-association of the SET domains of human ALL-1 and of
            Drosophila TRITHORAX and ASH1 proteins
  JOURNAL   Oncogene 19 (3), 351-357 (2000)
   PUBMED   10656681
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF318059.1 and AC006160.9.
            
            On Sep 30, 2004 this sequence version replaced NP_079481.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.104368.1,
                                           SRR1803613.277695.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237380.12/ ENSP00000237380.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..178
                     /product="mediator of RNA polymerase II transcription
                     subunit 28"
                     /note="endothelial-derived gene 1; endothelial-derived
                     protein 1; tumor angiogenesis marker EG-1; merlin and
                     Grb2-interacting cytoskeletal protein; mediator of RNA
                     polymerase II transcription, subunit 28 homolog"
                     /calculated_mol_wt=19389
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H204.1)"
     Region          43..143
                     /region_name="Med28"
                     /note="Mediator complex subunit 28; pfam11594"
                     /db_xref="CDD:463302"
     CDS             1..178
                     /gene="MED28"
                     /gene_synonym="1500003D12Rik; EG1; magicin"
                     /coded_by="NM_025205.5:15..551"
                     /db_xref="CCDS:CCDS33963.1"
                     /db_xref="GeneID:80306"
                     /db_xref="HGNC:HGNC:24628"
                     /db_xref="MIM:610311"
ORIGIN      
        1 maaplggmfs gqppgppqap pglpgqasll qaapgaprps sstlvdeles sfeacfaslv
       61 sqdyvngtdq eeirtgvdqc iqkfldiarq tecfflqkrl qlsvqkpeqv ikedvselrn
      121 elqrkdalvq khltklrhwq qvledinvqh kkpadipqgs layleqasan ipaplkpt
//
LOCUS       NP_001341968             434 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001341968
VERSION     NP_001341968.1
DBSOURCE    REFSEQ: accession NM_001355039.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Li,W., Han,J., Huang,B., Xu,T., Wan,Y., Luo,D., Kong,W., Yu,Y.,
            Zhang,L., Nian,Y., Chu,B. and Yin,C.
  TITLE     SLC25A1 and ACLY maintain cytosolic acetyl-CoA and regulate
            ferroptosis susceptibility via FSP1 acetylation
  JOURNAL   EMBO J 44 (6), 1641-1662 (2025)
   PUBMED   39881208
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Yu,H., Liu,S., Wang,S. and Gu,X.
  TITLE     The involvement of HDAC3 in the pathogenesis of lung injury and
            pulmonary fibrosis
  JOURNAL   Front Immunol 15, 1392145 (2024)
   PUBMED   39391308
  REMARK    GeneRIF: The involvement of HDAC3 in the pathogenesis of lung
            injury and pulmonary fibrosis.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Yoon,J.G., Lim,S.K., Seo,H., Lee,S., Cho,J., Kim,S.Y., Koh,H.Y.,
            Poduri,A.H., Ramakumaran,V., Vasudevan,P., de Groot,M.J., Ko,J.M.,
            Han,D., Chae,J.H. and Lee,C.H.
  TITLE     De novo missense variants in HDAC3 leading to epigenetic machinery
            dysfunction are associated with a variable neurodevelopmental
            disorder
  JOURNAL   Am J Hum Genet 111 (8), 1588-1604 (2024)
   PUBMED   39047730
  REMARK    GeneRIF: De novo missense variants in HDAC3 leading to epigenetic
            machinery dysfunction are associated with a variable
            neurodevelopmental disorder.
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Chen,H., Li,Y., Li,H., Chen,X., Fu,H., Mao,D., Chen,W., Lan,L.,
            Wang,C., Hu,K., Li,J., Zhu,C., Evans,I., Cheung,E., Lu,D., He,Y.,
            Behrens,A., Yin,D. and Zhang,C.
  TITLE     NBS1 lactylation is required for efficient DNA repair and
            chemotherapy resistance
  JOURNAL   Nature 631 (8021), 663-669 (2024)
   PUBMED   38961290
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Randhawa,G.S., Bell,D.W., Testa,J.R. and Feinberg,A.P.
  TITLE     Identification and mapping of human histone acetylation modifier
            gene homologues
  JOURNAL   Genomics 51 (2), 262-269 (1998)
   PUBMED   9722949
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Emiliani,S., Fischle,W., Van Lint,C., Al-Abed,Y. and Verdin,E.
  TITLE     Characterization of a human RPD3 ortholog, HDAC3
  JOURNAL   Proc Natl Acad Sci U S A 95 (6), 2795-2800 (1998)
   PUBMED   9501169
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Dangond,F., Hafler,D.A., Tong,J.K., Randall,J., Kojima,R., Utku,N.
            and Gullans,S.R.
  TITLE     Differential display cloning of a novel human histone deacetylase
            (HDAC3) cDNA from PHA-activated immune cells
  JOURNAL   Biochem Biophys Res Commun 242 (3), 648-652 (1998)
   PUBMED   9464271
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Lynch,E.D., Lee,M.K., Morrow,J.E., Welcsh,P.L., Leon,P.E. and
            King,M.C.
  TITLE     Nonsyndromic deafness DFNA1 associated with mutation of a human
            homolog of the Drosophila gene diaphanous
  JOURNAL   Science 278 (5341), 1315-1318 (1997)
   PUBMED   9360932
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Yang,W.M., Yao,Y.L., Sun,J.M., Davie,J.R. and Seto,E.
  TITLE     Isolation and characterization of cDNAs corresponding to an
            additional member of the human histone deacetylase gene family
  JOURNAL   J Biol Chem 272 (44), 28001-28007 (1997)
   PUBMED   9346952
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008781.7 and KC877130.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to the histone deacetylase/acuc/apha family. It
            has histone deacetylase activity and represses transcription when
            tethered to a promoter. It may participate in the regulation of
            transcription through its binding with the zinc-finger
            transcription factor YY1. This protein can also down-regulate p53
            function and thus modulate cell growth and apoptosis. This gene is
            regarded as a potential tumor suppressor gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1741985.1,
                                           SRR18074967.930989.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.3"
     Protein         1..434
                     /product="histone deacetylase 3 isoform 1"
                     /EC_number="3.5.1.98"
                     /note="SMAP45; protein deacylase HDAC3; protein
                     deacetylase HDAC3"
                     /calculated_mol_wt=49258
     Region          3..383
                     /region_name="HDAC3"
                     /note="Histone deacetylase 3 (HDAC3); cd10005"
                     /db_xref="CDD:212529"
     Region          3..316
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (O15379.2)"
     Site            order(134..135,143..144,170,172,259,266,296,298)
                     /site_type="active"
                     /db_xref="CDD:212529"
     CDS             1..434
                     /gene="HDAC3"
                     /gene_synonym="HD3; KDAC3; RPD3; RPD3-2"
                     /coded_by="NM_001355039.2:60..1364"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:8841"
                     /db_xref="HGNC:HGNC:4854"
                     /db_xref="MIM:605166"
ORIGIN      
        1 maktvayfyd pdvgnfhyga ghpmkphrla lthslvlhyg lykkmivfkp yqasqhdmcr
       61 fhsedyidfl qrvsptnmqg ftkslnafnv gddcpvfpgl fefcsrytga slqgatqlnn
      121 kicdiainwa gglhhakkfe asgfcyvndi vigilellky hprvlyidid ihhgdgvqea
      181 fyltdrvmtv sfhkygnyff pgtgdmyevg aesgryycln vplrdgiddq sykhlfqpvi
      241 nqvvdfyqpt civlqcgads lgcdrlgcfn lsirghgecv eyvksfnipl lvlggggytv
      301 rnvarcwtye tsllveeais eelpyseyfe yfapdftlhp dvstrienqn srqyldqirq
      361 tifenlkmln hapsvqihdv padlltydrt deadaeergp eenysrsgsr dfsllsigll
      421 grfkrekvng kvlv
//
LOCUS       NP_001354670             530 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform e [Homo sapiens].
ACCESSION   NP_001354670
VERSION     NP_001354670.1
DBSOURCE    REFSEQ: accession NM_001367741.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 530)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 530)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 530)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 530)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 530)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 530)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 530)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 530)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 530)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 530)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006001.2 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (25), as well as variant 26,
            encodes isoform e.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.53890.1,
                                           SRR1803612.218976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147596, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..530
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..530
                     /product="rab5 GDP/GTP exchange factor isoform e"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=60718
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..259
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          309..409
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..530
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367741.1:78..1670"
                     /note="isoform e is encoded by transcript variant 25"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgker rfhhvgqagl elltsgdppa sasqsagntg vepphpavpp
      241 ervekimdqi ekyimtrlyk yvfcpettdd ekkdlaiqkr iralrwvtpq mlcvpvnedi
      301 pevsdmvvka itdiiemdsk rvprdklaci tkcskhifna ikitknepas addflptliy
      361 ivlkgnpprl qsniqyitrf cnpsrlmtge dgyyftnlcc avafieklda qslnlsqedf
      421 drymsgqtsp rkqeaeswsp daclgvkqmy knldllsqln erqerimnea kklekdlidw
      481 tdgiarevqd ivekypleik ppnqplaaid senvendklp pplqpqvyag
//
LOCUS       NP_001191007              78 aa            linear   PRI 20-NOV-2025
DEFINITION  V-type proton ATPase subunit G 2 isoform c [Homo sapiens].
ACCESSION   NP_001191007
VERSION     NP_001191007.1
DBSOURCE    REFSEQ: accession NM_001204078.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 78)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 78)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 78)
  AUTHORS   Hohn,A., Sittig,A., Jung,T., Grimm,S. and Grune,T.
  TITLE     Lipofuscin is formed independently of macroautophagy and lysosomal
            activity in stress-induced prematurely senescent human fibroblasts
  JOURNAL   Free Radic Biol Med 53 (9), 1760-1769 (2012)
   PUBMED   22982048
REFERENCE   4  (residues 1 to 78)
  AUTHORS   Mewar,D., Marinou,I., Lee,M.E., Timms,J.M., Kilding,R., Teare,M.D.,
            Read,R.C. and Wilson,A.G.
  TITLE     Haplotype-specific gene expression profiles in a telomeric major
            histocompatibility complex gene cluster and susceptibility to
            autoimmune diseases
  JOURNAL   Genes Immun 7 (8), 625-631 (2006)
   PUBMED   16971954
REFERENCE   5  (residues 1 to 78)
  AUTHORS   Smith,A.N., Borthwick,K.J. and Karet,F.E.
  TITLE     Molecular cloning and characterization of novel tissue-specific
            isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and
            their evaluation in autosomal recessive distal renal tubular
            acidosis
  JOURNAL   Gene 297 (1-2), 169-177 (2002)
   PUBMED   12384298
REFERENCE   6  (residues 1 to 78)
  AUTHORS   Neville,M.J. and Campbell,R.D.
  TITLE     A new member of the Ig superfamily and a V-ATPase G subunit are
            among the predicted products of novel genes close to the TNF locus
            in the human MHC
  JOURNAL   J Immunol 162 (8), 4745-4754 (1999)
   PUBMED   10202016
REFERENCE   7  (residues 1 to 78)
  AUTHORS   Nelson,N. and Harvey,W.R.
  TITLE     Vacuolar and plasma membrane proton-adenosinetriphosphatases
  JOURNAL   Physiol Rev 79 (2), 361-385 (1999)
   PUBMED   10221984
  REMARK    Review article
REFERENCE   8  (residues 1 to 78)
  AUTHORS   Finbow,M.E. and Harrison,M.A.
  TITLE     The vacuolar H+-ATPase: a universal proton pump of eukaryotes
  JOURNAL   Biochem J 324 (Pt 3) (Pt 3), 697-712 (1997)
   PUBMED   9210392
  REMARK    Review article
REFERENCE   9  (residues 1 to 78)
  AUTHORS   Stevens,T.H. and Forgac,M.
  TITLE     Structure, function and regulation of the vacuolar (H+)-ATPase
  JOURNAL   Annu Rev Cell Dev Biol 13, 779-808 (1997)
   PUBMED   9442887
  REMARK    Review article
REFERENCE   10 (residues 1 to 78)
  AUTHORS   Dautry-Varsat,A.
  TITLE     Receptor-mediated endocytosis: the intracellular journey of
            transferrin and its receptor
  JOURNAL   Biochimie 68 (3), 375-381 (1986)
   PUBMED   2874839
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC047791.1 and AL662801.7.
            
            Summary: This gene encodes a component of vacuolar ATPase
            (V-ATPase), a multisubunit enzyme that mediates acidification of
            intracellular compartments of eukaryotic cells. V-ATPase dependent
            acidification is necessary for such intracellular processes as
            protein sorting, zymogen activation, receptor-mediated endocytosis,
            and synaptic vesicle proton gradient generation. V-ATPase is
            composed of a cytosolic V1 domain and a transmembrane V0 domain.
            The V1 domain consists of three A and three B subunits, two G
            subunits plus the C, D, E, F, and H subunits. The V1 domain
            contains the ATP catalytic site. The V0 domain consists of five
            different subunits: a, c, c', c'', and d. Additional isoforms of
            many of the V1 and V0 subunit proteins are encoded by multiple
            genes or alternatively spliced transcript variants. This encoded
            protein is one of three V1 domain G subunit proteins. This gene had
            previous gene symbols of ATP6G and ATP6G2. Alternatively spliced
            transcript variants encoding different isoforms have been
            described. Read-through transcription also exists between this gene
            and the downstream DEAD (Asp-Glu-Ala-Asp) box polypeptide 39B
            (DDX39B) gene. [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047791.1, BQ959563.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..78
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..78
                     /product="V-type proton ATPase subunit G 2 isoform c"
                     /EC_number="7.1.2.2"
                     /note="vacuolar ATP synthase subunit G 2; V-ATPase 13 kDa
                     subunit 2; vacuolar proton pump G subunit 2;
                     H(+)-transporting two-sector ATPase, subunit G2; V-type
                     proton ATPase subunit G 2; ATPase, H+ transporting,
                     lysosomal (vacuolar proton pump); ATPase, H+ transporting,
                     lysosomal 13kDa, V1 subunit G2"
                     /calculated_mol_wt=8823
     Region          3..67
                     /region_name="V-ATPase_G"
                     /note="Vacuolar (H+)-ATPase G subunit; pfam03179"
                     /db_xref="CDD:460836"
     CDS             1..78
                     /gene="ATP6V1G2"
                     /gene_synonym="ATP6G; ATP6G2; NG38; VMA10"
                     /coded_by="NM_001204078.2:50..286"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS56413.1"
                     /db_xref="GeneID:534"
                     /db_xref="HGNC:HGNC:862"
                     /db_xref="MIM:606853"
ORIGIN      
        1 masqsqgiqq llqaekraae kvadarkrka rrlkqatrrq vqgmqssqqr nrervlaqll
       61 gmvcdvrpqv hpnyrisa
//
LOCUS       NP_892030                500 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 isoform a [Homo sapiens].
ACCESSION   NP_892030 XP_378511
VERSION     NP_892030.3
DBSOURCE    REFSEQ: accession NM_182985.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 500)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 500)
  AUTHORS   Sun,L., Chen,Y., Xia,L., Wang,J., Zhu,J., Li,J., Wang,K., Shen,K.,
            Zhang,D., Zhang,G., Shi,T. and Chen,W.
  TITLE     TRIM69 suppressed the anoikis resistance and metastasis of gastric
            cancer through ubiquitin-proteasome-mediated degradation of PRKCD
  JOURNAL   Oncogene 42 (49), 3619-3632 (2023)
   PUBMED   37864033
  REMARK    GeneRIF: TRIM69 suppressed the anoikis resistance and metastasis of
            gastric cancer through ubiquitin-proteasome-mediated degradation of
            PRKCD.
REFERENCE   3  (residues 1 to 500)
  AUTHORS   Wang,Y., Risteski,P., Yang,Y., Chen,H., Droby,G., Walens,A.,
            Jayaprakash,D., Troester,M., Herring,L., Chernoff,J., Tolic,I.M.,
            Bowser,J. and Vaziri,C.
  TITLE     The TRIM69-MST2 signaling axis regulates centrosome dynamics and
            chromosome segregation
  JOURNAL   Nucleic Acids Res 51 (19), 10568-10589 (2023)
   PUBMED   37739411
  REMARK    GeneRIF: The TRIM69-MST2 signaling axis regulates centrosome
            dynamics and chromosome segregation.
REFERENCE   4  (residues 1 to 500)
  AUTHORS   Yuan,J., Lv,T., Yang,J., Wu,Z., Yan,L., Yang,J. and Shi,Y.
  TITLE     HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability by
            diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma
  JOURNAL   Redox Biol 58, 102546 (2022)
   PUBMED   36423520
  REMARK    GeneRIF: HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability
            by diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 500)
  AUTHORS   Song,Y., Nguyen,X.N., Kumar,A., da Silva,C., Picard,L., Etienne,L.
            and Cimarelli,A.
  TITLE     Trim69 is a microtubule regulator that acts as a pantropic viral
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 119 (43), e2211467119 (2022)
   PUBMED   36251989
  REMARK    GeneRIF: Trim69 is a microtubule regulator that acts as a pantropic
            viral inhibitor.
REFERENCE   6  (residues 1 to 500)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
  REMARK    GeneRIF: hTRIM69 is a novel E3 ubiquitin ligase identified from
            human testis and may function to ubiquitinate its particular
            substrates during spermatogenesis.
REFERENCE   7  (residues 1 to 500)
  AUTHORS   Bahmanyar,S., Kaplan,D.D., Deluca,J.G., Giddings,T.H. Jr.,
            O'Toole,E.T., Winey,M., Salmon,E.D., Casey,P.J., Nelson,W.J. and
            Barth,A.I.
  TITLE     beta-Catenin is a Nek2 substrate involved in centrosome separation
  JOURNAL   Genes Dev 22 (1), 91-105 (2008)
   PUBMED   18086858
REFERENCE   8  (residues 1 to 500)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     Forced expression of RNF36 induces cell apoptosis
  JOURNAL   Exp Cell Res 287 (2), 301-313 (2003)
   PUBMED   12837286
REFERENCE   9  (residues 1 to 500)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     A novel member of the RBCC family, Trif, expressed specifically in
            the spermatids of mouse testis
  JOURNAL   Mech Dev 108 (1-2), 213-216 (2001)
   PUBMED   11578878
  REMARK    GeneRIF: Gene and protein analysis of the mouse counterpart.
REFERENCE   10 (residues 1 to 500)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI827618.1, AY305385.1,
            AC122108.2, AF302088.1 and DB524904.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 28, 2006 this sequence version replaced NP_892030.2.
            
            Summary: This gene encodes a member of the RING-B-box-coiled-coil
            (RBCC) family and encodes a protein with an N-terminal RING finger
            motif, a PRY domain and a C-terminal SPRY domain. The mouse
            ortholog of this gene is specifically expressed in germ cells at
            the round spermatid stages during spermatogenesis and, when
            overexpressed, induces apoptosis. Alternatively spliced transcript
            variants encoding distinct isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (a) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047945.1, AK292252.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329464.9/ ENSP00000332284.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..500
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..500
                     /product="E3 ubiquitin-protein ligase TRIM69 isoform a"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 36; RFP-like domain-containing
                     protein trimless; E3 ubiquitin-protein ligase TRIM69;
                     RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=57288
     Region          1..152
                     /region_name="Necessary for nuclear localization.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WT6.2)"
     Region          35..93
                     /region_name="RING-HC_TRIM69_C-IV"
                     /note="RING finger, HC subclass, found in tripartite
                     motif-containing protein 69 (TRIM69) and similar proteins;
                     cd16611"
                     /db_xref="CDD:438273"
     Region          115..>141
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          168..299
                     /region_name="CC_brat-like"
                     /note="coiled-coil (CC) domain of Drosophila brain tumor
                     (brat) and similar proteins; cl29238"
                     /db_xref="CDD:475168"
     Region          311..497
                     /region_name="SPRY_PRY_TRIM69"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     69 (TRIM69), also known as RING finger protein 36 (RNF36);
                     cd15818"
                     /db_xref="CDD:293990"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5BK82; propagated from
                     UniProtKB/Swiss-Prot (Q86WT6.2)"
     CDS             1..500
                     /gene="TRIM69"
                     /gene_synonym="HSD-34; HSD34; RNF36; Trif"
                     /coded_by="NM_182985.5:178..1680"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS32220.1"
                     /db_xref="GeneID:140691"
                     /db_xref="HGNC:HGNC:17857"
                     /db_xref="MIM:616017"
ORIGIN      
        1 mevstnpssn idpgdyvemn dsithlpskv viqditmelh cplcndwfrd plmlscghnf
       61 ceaciqdfwr lqaketfcpe ckmlcqynnc tfnpvldklv ekikklpllk ghpqcpehge
      121 nlklfskpdg klicfqckda rlsvgqskef lqisdavhff teelaiqqgq lettlkelqt
      181 lrnmqkeaia ahkenklhlq qhvsmeflkl hqflhskekd iltelreegk alneemelnl
      241 sqlqeqclla kdmlvsiqak teqqnsfdfl kdittllhsl eqgmkvlatr elisrklnlg
      301 qykgpiqymv wremqdtlcp glspltldpk tahpnlvlsk sqtsvwhgdi kkimpddper
      361 fdssvavlgs rgftsgkwyw evevakktkw tvgvvresii rkgscpltpe qgfwllrlrn
      421 qtdlkaldlp sfsltltnnl dkvgiyldye ggqlsfynak tmthiytfsn tfmeklypyf
      481 cpclndggen keplhilhpq
//
LOCUS       NP_001356325            2301 aa            linear   PRI 20-NOV-2025
DEFINITION  receptor-type tyrosine-protein phosphatase zeta isoform 5 [Homo
            sapiens].
ACCESSION   NP_001356325 XP_016867966
VERSION     NP_001356325.1
DBSOURCE    REFSEQ: accession NM_001369396.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2301)
  AUTHORS   Wang,Y., Suo,J., Wang,Z., Ran,K., Tian,Y., Han,W., Liu,Y. and
            Peng,X.
  TITLE     The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells modulates
            tumor-associated macrophage polarization
  JOURNAL   Cell Signal 120, 111191 (2024)
   PUBMED   38685521
  REMARK    GeneRIF: The PTPRZ1-MET/STAT3/ISG20 axis in glioma stem-like cells
            modulates tumor-associated macrophage polarization.
REFERENCE   2  (residues 1 to 2301)
  AUTHORS   Nagai,K., Muto,Y., Miura,S., Takahashi,K., Naruse,Y., Hiruta,R.,
            Hashimoto,Y., Uzuki,M., Haga,Y., Fujii,R., Ueda,K., Kawaguchi,Y.,
            Fujii,M. and Kitazume,S.
  TITLE     Brain-specific glycosylation enzyme GnT-IX maintains levels of
            protein tyrosine phosphatase receptor PTPRZ, thereby mediating
            glioma growth
  JOURNAL   J Biol Chem 299 (9), 105128 (2023)
   PUBMED   37543361
  REMARK    GeneRIF: Brain-specific glycosylation enzyme GnT-IX maintains
            levels of protein tyrosine phosphatase receptor PTPRZ, thereby
            mediating glioma growth.
REFERENCE   3  (residues 1 to 2301)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2301)
  AUTHORS   Lacore,M.G., Delmas,C., Nicaise,Y., Kowalski-Chauvel,A.,
            Cohen-Jonathan-Moyal,E. and Seva,C.
  TITLE     The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells
  JOURNAL   Cells 11 (14), 2128 (2022)
   PUBMED   35883571
  REMARK    GeneRIF: The Glycoprotein M6a Is Associated with Invasiveness and
            Radioresistance of Glioblastoma Stem Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2301)
  AUTHORS   Nagai,K., Fujii,M. and Kitazume,S.
  TITLE     Protein Tyrosine Phosphatase Receptor Type Z in Central Nervous
            System Disease
  JOURNAL   Int J Mol Sci 23 (8), 4414 (2022)
   PUBMED   35457233
  REMARK    GeneRIF: Protein Tyrosine Phosphatase Receptor Type Z in Central
            Nervous System Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2301)
  AUTHORS   Ariyama,T., Hasegawa,K., Inazawa,J., Mizuno,K., Ogimoto,M.,
            Katagiri,T. and Yakura,H.
  TITLE     Assignment of the human protein tyrosine phosphatase,
            receptor-type, zeta (PTPRZ) gene to chromosome band 7q31.3
  JOURNAL   Cytogenet Cell Genet 70 (1-2), 52-54 (1995)
   PUBMED   7736789
REFERENCE   7  (residues 1 to 2301)
  AUTHORS   Levy,J.B., Canoll,P.D., Silvennoinen,O., Barnea,G., Morse,B.,
            Honegger,A.M., Huang,J.T., Cannizzaro,L.A., Park,S.H., Druck,T. et
            al.
  TITLE     The cloning of a receptor-type protein tyrosine phosphatase
            expressed in the central nervous system
  JOURNAL   J Biol Chem 268 (14), 10573-10581 (1993)
   PUBMED   8387522
REFERENCE   8  (residues 1 to 2301)
  AUTHORS   Krueger,N.X. and Saito,H.
  TITLE     A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is
            expressed in brain and has an N-terminal receptor domain homologous
            to carbonic anhydrases
  JOURNAL   Proc Natl Acad Sci U S A 89 (16), 7417-7421 (1992)
   PUBMED   1323835
REFERENCE   9  (residues 1 to 2301)
  AUTHORS   Krueger,N.X., Streuli,M. and Saito,H.
  TITLE     Structural diversity and evolution of human receptor-like protein
            tyrosine phosphatases
  JOURNAL   EMBO J 9 (10), 3241-3252 (1990)
   PUBMED   2170109
REFERENCE   10 (residues 1 to 2301)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc Natl Acad Sci U S A 87 (18), 7000-7004 (1990)
   PUBMED   2169617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006353.3, AC073095.4 and
            AC006020.2.
            
            On Apr 8, 2019 this sequence version replaced XP_016867966.1.
            
            Summary: This gene encodes a member of the receptor protein
            tyrosine phosphatase family. Expression of this gene is restricted
            to the central nervous system (CNS), and it may be involved in the
            regulation of specific developmental processes in the CNS.
            Alternatively spliced transcript variants encoding different
            isoforms have been described for this gene. [provided by RefSeq,
            May 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.29086.1,
                                           SRR1803616.62566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2301
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.32"
     Protein         1..2301
                     /product="receptor-type tyrosine-protein phosphatase zeta
                     isoform 5"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase, receptor-type, zeta
                     polypeptide 1; protein tyrosine phosphatase,
                     receptor-type, Z polypeptide 1; receptor-type tyrosine
                     phosphatase beta/zeta; protein-tyrosine phosphatase
                     receptor type Z polypeptide 2"
                     /calculated_mol_wt=252731
     Region          31..284
                     /region_name="alpha_CARP_receptor_like"
                     /note="Carbonic anhydrase alpha related protein,
                     receptor_like subfamily. Carbonic anhydrase related
                     proteins (CARPs) are sequence similar to carbonic
                     anhydrases. Carbonic anhydrases are zinc-containing
                     enzymes that catalyze the reversible hydration of
                     carbon...; cd03122"
                     /db_xref="CDD:239396"
     Region          299..387
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(383..384,386..387)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1703..1980
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     Region          2063..2266
                     /region_name="R-PTP-Z-2"
                     /note="catalytic domain of receptor-type tyrosine-protein
                     phosphatase Z, repeat 2; cd17669"
                     /db_xref="CDD:350507"
     CDS             1..2301
                     /gene="PTPRZ1"
                     /gene_synonym="HPTPZ; HPTPzeta; phosphacan; PTP-ZETA;
                     PTP18; PTPRZ; PTPZ; R-PTP-zeta-2; RPTPB; RPTPbeta"
                     /coded_by="NM_001369396.1:485..7390"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:5803"
                     /db_xref="HGNC:HGNC:9685"
                     /db_xref="MIM:176891"
ORIGIN      
        1 marcsdwang yyrqqrklve eigwsytgal nqknwgkkyp tcnspkqspi nidedltqvn
       61 vnlkklkfqg wdktslentf ihntgktvei nltndyrvsg gvsemvfkas kitfhwgkcn
      121 mssdgsehsl egqkfplemq iycfdadrfs sfeeavkgkg klralsilfe vgteenldfk
      181 aiidgvesvs rfgkqaaldp fillnllpns tdkyyiyngs ltsppctdtv dwivfkdtvs
      241 isesqlavfc evltmqqsgy vmlmdylqnn freqqykfsr qvfssytgke eiheavcsse
      301 penvqadpen ytsllvtwer prvvydtmie kfavlyqqld gedqtkhefl tdgyqdlgai
      361 lnnllpnmsy vlqivaictn glygkysdql ivdmptdnpe ldlfpeligt eeiikeeeeg
      421 kdieegaivn pgrdsatnqi rkkepqistt thynrigtky neaktnrspt rgsefsgkgd
      481 vpntslnsts qpvtklatek disltsqtvt elpphtvegt saslndgskt vlrsphmnls
      541 gtaeslntvs iteyeeesll tsfkldtgae dssgsspats aipfisenis qgyifssenp
      601 etitydvlip esarnaseds tssgseeslk dpsmegnvwf psstditaqp dvgsgresfl
      661 qtnyteirvd esekttksfs agpvmsqgps vtdlemphys tfayfptevt phaftpssrq
      721 qdlvstvnvv ysqttqpvyn getplqpsys sevfplvtpl lldnqilntt paasssdsal
      781 hatpvfpsvd vsfesilssy dgapllpfss asfsselfrh lhtvsqilpq vtsatesdkv
      841 plhaslpvag gdlllepsla qysdvlstth aasetlefgs esgvlyktlm fsqveppssd
      901 ammharssgp epsyalsdne gsqhiftvsy ssaipvhdsv gvtyqgslfs gpshipipks
      961 slitptasll qpthalsgdg ewsgassdse fllpdtdglt alnisspvsv aeftyttsvf
     1021 gddnkalsks eiiygnetel qipsfnemvy psestvmpnm ydnvnklnas lqetsvsiss
     1081 tkgmfpgsla htttkvfdhe isqvpennfs vqpthtvsqa sgdtslkpvl sansepassd
     1141 passemlsps tqllfyetsa sfstevllqp sfqasdvdtl lktvlpavps dpilvetpkv
     1201 dkisstmlhl ivsnsassen mlhstsvpvf dvsptshmhs aslqgltisy asekyepvll
     1261 ksesshqvvp slysndelfq tanleinqah ppkgrhvfat pvlsidepln tlinklihsd
     1321 eiltstkssv tgkvfagipt vasdtfvstd hsvpignghv aitavsphrd gsvtstkllf
     1381 pskatselsh saksdaglvg ggedgdtddd gddddddrgs dglsihkcms cssyresqek
     1441 vmndsdthen slmdqnnpis yslsenseed nrvtsvssds qtgmdrspgk spsanglsqk
     1501 hndgkeendi qtgsallpls peskawavlt sdeesgsgqg tsdslnenet stdfsfadtn
     1561 ekdadgilaa gdseitpgfp qsptssvtse nsevfhvsea easnsshesr iglaeglese
     1621 kkaviplviv saltficlvv lvgiliywrk cfqtahfyle dstsprvist pptpifpisd
     1681 dvgaipikhf pkhvadlhas sgfteefetl kefyqevqsc tvdlgitads snhpdnkhkn
     1741 ryinivaydh srvklaqlae kdgkltdyin anyvdgynrp kayiaaqgpl kstaedfwrm
     1801 iwehnveviv mitnlvekgr rkcdqywpad gseeygnflv tqksvqvlay ytvrnftlrn
     1861 tkikkgsqkg rpsgrvvtqy hytqwpdmgv peyslpvltf vrkaayakrh avgpvvvhcs
     1921 agvgrtgtyi vldsmlqqiq hegtvnifgf lkhirsqrny lvqteeqyvf ihdtlveail
     1981 sketevldsh ihayvnalli pgpagktkle kqfqllsqsn iqqsdysaal kqcnreknrt
     2041 ssiipversr vgisslsgeg tdyinasyim gyyqsnefii tqhpllhtik dfwrmiwdhn
     2101 aqlvvmipdg qnmaedefvy wpnkdepinc esfkvtlmae ehkclsneek liiqdfilea
     2161 tqddyvlevr hfqcpkwpnp dspisktfel isvikeeaan rdgpmivhde hggvtagtfc
     2221 alttlmhqle kensvdvyqv akminlmrpg vfadieqyqf lykvilslvs trqeenpsts
     2281 ldsngaalpd gniaeslesl v
//
LOCUS       NP_005776                317 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NRDP1 isoform 1 [Homo sapiens].
ACCESSION   NP_005776
VERSION     NP_005776.1
DBSOURCE    REFSEQ: accession NM_005785.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Xiong,S., Li,S., Li,Z., Song,Y., Yang,L., Yang,H., Xiong,J.,
            Pan,W., Guo,J., Fu,B. and Xu,S.
  TITLE     A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C stability
            promotes prostate cancer metastasis by inducing actin remodeling
  JOURNAL   Oncogene 43 (36), 2696-2707 (2024)
   PUBMED   39112516
  REMARK    GeneRIF: A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C
            stability promotes prostate cancer metastasis by inducing actin
            remodeling.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Li,Q.Q., Guo,M., He,G.H., Xi,K.H., Zhou,M.Y., Shi,R.Y. and
            Chen,G.Q.
  TITLE     VEGF-induced Nrdp1 deficiency in vascular endothelial cells
            promotes cancer metastasis by degrading vascular basement membrane
  JOURNAL   Oncogene 43 (24), 1836-1851 (2024)
   PUBMED   38654108
  REMARK    GeneRIF: VEGF-induced Nrdp1 deficiency in vascular endothelial
            cells promotes cancer metastasis by degrading vascular basement
            membrane.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Zong,C.Y., Ji,Q.Q., Chen,F.F., Yang,J.J., Zhou,H., Zhu,B.F. and
            Zhou,G.X.
  TITLE     Correlation between neuregulin receptor degradation protein-1 and
            Crohn's disease
  JOURNAL   J Physiol Pharmacol 75 (1) (2024)
   PUBMED   38583443
  REMARK    GeneRIF: Correlation between neuregulin receptor degradation
            protein-1 and Crohn's disease.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Zeng,W., Zhu,J.F., Guo,J., Huang,G.J., Ai,L.S., Zeng,Y. and
            Liao,W.J.
  TITLE     m6A-modified circFNDC3B inhibits colorectal cancer stemness and
            metastasis via RNF41-dependent ASB6 degradation
  JOURNAL   Cell Death Dis 13 (11), 1008 (2022)
   PUBMED   36446779
  REMARK    GeneRIF: m[6]A-modified circFNDC3B inhibits colorectal cancer
            stemness and metastasis via RNF41-dependent ASB6 degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Qiu,X.B., Markant,S.L., Yuan,J. and Goldberg,A.L.
  TITLE     Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel
            pathway for triggering apoptosis
  JOURNAL   EMBO J 23 (4), 800-810 (2004)
   PUBMED   14765125
  REMARK    GeneRIF: Nrdp1 can be important in the initiation of apoptosis by
            catalyzing ubiquitination and degradation of BRUCE.
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Qiu,X.B. and Goldberg,A.L.
  TITLE     Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and
            degradation of the epidermal growth factor receptor family member,
            ErbB3
  JOURNAL   Proc Natl Acad Sci U S A 99 (23), 14843-14848 (2002)
   PUBMED   12411582
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):17220.]
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Diamonti,A.J., Guy,P.M., Ivanof,C., Wong,K., Sweeney,C. and
            Carraway,K.L. 3rd.
  TITLE     An RBCC protein implicated in maintenance of steady-state
            neuregulin receptor levels
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2866-2871 (2002)
   PUBMED   11867753
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Abdullah,J.M., Li,X., Nachtman,R.G. and Jurecic,R.
  TITLE     FLRF, a novel evolutionarily conserved RING finger gene, is
            differentially expressed in mouse fetal and adult hematopoietic
            stem cells and progenitors
  JOURNAL   Blood Cells Mol Dis 27 (1), 320-333 (2001)
   PUBMED   11358394
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB989647.1, BC036267.1 and
            AC073896.41.
            
            Summary: This gene encodes an E3 ubiquitin ligase. The encoded
            protein plays a role in type 1 cytokine receptor signaling by
            controlling the balance between JAK2-associated cytokine receptor
            degradation and ectodomain shedding. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Variants 1, 3 and 4 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.220152.1,
                                           SRR1803616.160694.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000345093.9/ ENSP00000342755.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..317
                     /product="E3 ubiquitin-protein ligase NRDP1 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="neuregulin receptor degradation protein-1; fetal
                     liver ring finger; E3 ubiquitin-protein ligase NRDP1; ring
                     finger protein 41, E3 ubiquitin protein ligase; RING-type
                     E3 ubiquitin transferase NRDP1"
                     /calculated_mol_wt=35774
     Region          15..57
                     /region_name="mRING-HC-C3HC3D_Nrdp1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in neuregulin receptor degradation protein-1 (Nrdp1)
                     and similar proteins; cd16634"
                     /db_xref="CDD:438296"
     Region          137..315
                     /region_name="USP8_interact"
                     /note="USP8 interacting; pfam08941"
                     /db_xref="CDD:430333"
     CDS             1..317
                     /gene="RNF41"
                     /gene_synonym="FLRF; NRDP1; SBBI03"
                     /coded_by="NM_005785.4:372..1325"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8909.1"
                     /db_xref="GeneID:10193"
                     /db_xref="HGNC:HGNC:18401"
                     /db_xref="MIM:620051"
ORIGIN      
        1 mgydvtrfqg dvdedlicpi csgvleepvq aphcehafcn acitqwfsqq qtcpvdrsvv
       61 tvahlrpvpr imrnmlsklq iacdnavfgc savvrldnlm shlsdcehnp krpvtceqgc
      121 glempkdelp nhncikhlrs vvqqqqtria elektsaehk hqlaeqkrdi qllkaymrai
      181 rsvnpnlqnl eetieyneil ewvnslqpar vtrwggmist pdavlqavik rslvesgcpa
      241 sivneliena herswpqgla tletrqmnrr yyenyvakri pgkqavvvma cenqhmgddm
      301 vqepglvmif ahgveei
//
LOCUS       NP_001307942             445 aa            linear   PRI 20-NOV-2025
DEFINITION  C-terminal-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001307942 XP_011537658
VERSION     NP_001307942.1
DBSOURCE    REFSEQ: accession NM_001321013.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Pastoors,D., Havermans,M., Mulet-Lazaro,R., Brian,D., Noort,W.,
            Grasel,J., Hoogenboezem,R., Smeenk,L., Demmers,J.A.A., Milsom,M.D.,
            Enver,T., Groen,R.W.J., Bindels,E. and Delwel,R.
  TITLE     Oncogene EVI1 drives acute myeloid leukemia via a targetable
            interaction with CTBP2
  JOURNAL   Sci Adv 10 (20), eadk9076 (2024)
   PUBMED   38748792
  REMARK    GeneRIF: Oncogene EVI1 drives acute myeloid leukemia via a
            targetable interaction with CTBP2.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Cheung,C.H.Y., Cheng,C.K., Leung,K.T., Zhang,C., Ho,C.Y., Luo,X.,
            Kam,A.Y.F., Xia,T., Wan,T.S.K., Pitts,H.A., Chan,N.P.H.,
            Cheung,J.S., Wong,R.S.M., Zhang,X.B. and Ng,M.H.L.
  TITLE     C-terminal binding protein 2 is a novel tumor suppressor targeting
            the MYC-IRF4 axis in multiple myeloma
  JOURNAL   Blood Adv 8 (9), 2217-2234 (2024)
   PUBMED   38457926
  REMARK    GeneRIF: C-terminal binding protein 2 is a novel tumor suppressor
            targeting the MYC-IRF4 axis in multiple myeloma.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Sekiya,M., Ma,Y., Kainoh,K., Saito,K., Yamazaki,D., Tsuyuzaki,T.,
            Chen,W., Adi Putri,P.I.P., Ohno,H., Miyamoto,T., Takeuchi,Y.,
            Murayama,Y., Sugano,Y., Osaki,Y., Iwasaki,H., Yahagi,N., Suzuki,H.,
            Motomura,K., Matsuzaka,T., Murata,K., Mizuno,S., Takahashi,S. and
            Shimano,H.
  TITLE     Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function
  JOURNAL   Cell Rep 42 (8), 112914 (2023)
   PUBMED   37557182
  REMARK    GeneRIF: Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Holmes,M., Turner,J., Fox,A., Chisholm,O., Crossley,M. and Chong,B.
  TITLE     hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
            and modulates GATA-mediated activation
  JOURNAL   J Biol Chem 274 (33), 23491-23498 (1999)
   PUBMED   10438528
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and
            Otte,A.P.
  TITLE     C-Terminal binding protein is a transcriptional repressor that
            interacts with a specific class of vertebrate Polycomb proteins
  JOURNAL   Mol Cell Biol 19 (1), 777-787 (1999)
   PUBMED   9858600
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Turner,J. and Crossley,M.
  TITLE     Cloning and characterization of mCtBP2, a co-repressor that
            associates with basic Kruppel-like factor and other mammalian
            transcriptional regulators
  JOURNAL   EMBO J 17 (17), 5129-5140 (1998)
   PUBMED   9724649
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY046871.1, BM800106.1,
            AL731571.3 and BE671217.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011537658.1.
            
            Summary: This gene produces alternative transcripts encoding two
            distinct proteins. One protein is a transcriptional repressor,
            while the other isoform is a major component of specialized
            synapses known as synaptic ribbons. Both proteins contain a NAD+
            binding domain similar to NAD+-dependent 2-hydroxyacid
            dehydrogenases. A portion of the 3' untranslated region was used to
            map this gene to chromosome 21q21.3; however, it was noted that
            similar loci elsewhere in the genome are likely. Blast analysis
            shows that this gene is present on chromosome 10. Several
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Feb 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.2294562.1,
                                           SRR14038196.2322341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..445
                     /product="C-terminal-binding protein 2 isoform 1"
                     /note="ribeye"
                     /calculated_mol_wt=48814
     Site            22
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     Region          34..352
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(103,106..107,272,321,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(106,134,186..187,189..191,209..213,242..244,246,249,
                     270..272,296..297,321,323..324)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          414..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56545.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     CDS             1..445
                     /gene="CTBP2"
                     /coded_by="NM_001321013.2:245..1582"
                     /note="isoform 1 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS7643.1"
                     /db_xref="GeneID:1488"
                     /db_xref="HGNC:HGNC:2495"
                     /db_xref="MIM:602619"
ORIGIN      
        1 malvdkhkvk rqrldriceg irpqimngpl hprplvalld grdctvempi lkdlatvafc
       61 daqstqeihe kvlneavgam myhtitltre dlekfkalrv ivrigsgydn vdikaagelg
      121 iavcnipsaa veetadstic hilnlyrrnt wlyqalregt rvqsveqire vasgaarirg
      181 etlgligfgr tgqavavrak afgfsvifyd pylqdgiers lgvqrvytlq dllyqsdcvs
      241 lhcnlnehnh hlindftikq mrqgaflvna argglvdeka laqalkegri rgaaldvhes
      301 epfsfaqgpl kdapnlictp htawyseqas lemreaaate irraitgrip eslrncvnke
      361 ffvtsapwsv idqqaihpel ngatyryppg ivgvapgglp aamegiipgg ipvthnlptv
      421 ahpsqapspn qptkhgdnre hpneq
//
LOCUS       NP_783859                201 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
            isoform 1 [Homo sapiens].
ACCESSION   NP_783859
VERSION     NP_783859.1
DBSOURCE    REFSEQ: accession NM_175732.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Falabella,M., Pizzamiglio,C., Tabara,L.C., Munro,B.,
            Abdel-Hamid,M.S., Sonmezler,E., Macken,W.L., Lu,S., Tilokani,L.,
            Flannery,P.J., Patel,N., Pope,S.A.S., Heales,S.J.R.,
            Hammadi,D.B.H., Alston,C.L., Taylor,R.W., Lochmuller,H.,
            Woodward,C.E., Labrum,R., Vandrovcova,J., Houlden,H.,
            Chronopoulou,E., Pierre,G., Maroofian,R., Hanna,M.G., Taanman,J.W.,
            Hiz,S., Oktay,Y., Zaki,M.S., Horvath,R., Prudent,J. and
            Pitceathly,R.D.S.
  TITLE     Biallelic PTPMT1 variants disrupt cardiolipin metabolism and lead
            to a neurodevelopmental syndrome
  JOURNAL   Brain 148 (2), 647-662 (2025)
   PUBMED   39279645
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Ikari,N., Honjo,K., Sagami,Y., Nakamura,Y. and Arakawa,H.
  TITLE     Mieap forms membrane-less organelles involved in cardiolipin
            metabolism
  JOURNAL   iScience 27 (2), 108916 (2024)
   PUBMED   38322995
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Du,J.X., Luo,Y.H., Zhang,S.J., Wang,B., Chen,C., Zhu,G.Q., Zhu,P.,
            Cai,C.Z., Wan,J.L., Cai,J.L., Chen,S.P., Dai,Z. and Zhu,W.
  TITLE     Splicing factor SRSF1 promotes breast cancer progression via
            oncogenic splice switching of PTPMT1
  JOURNAL   J Exp Clin Cancer Res 40 (1), 171 (2021)
   PUBMED   33992102
  REMARK    GeneRIF: Splicing factor SRSF1 promotes breast cancer progression
            via oncogenic splice switching of PTPMT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Bao,M.H., Yang,C., Tse,A.P., Wei,L., Lee,D., Zhang,M.S., Goh,C.C.,
            Chiu,D.K., Yuen,V.W., Law,C.T., Chin,W.C., Chui,N.N., Wong,B.P.,
            Chan,C.Y., Ng,I.O., Chung,C.Y., Wong,C.M. and Wong,C.C.
  TITLE     Genome-wide CRISPR-Cas9 knockout library screening identified
            PTPMT1 in cardiolipin synthesis is crucial to survival in hypoxia
            in liver cancer
  JOURNAL   Cell Rep 34 (4), 108676 (2021)
   PUBMED   33503428
  REMARK    GeneRIF: Genome-wide CRISPR-Cas9 knockout library screening
            identified PTPMT1 in cardiolipin synthesis is crucial to survival
            in hypoxia in liver cancer.
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Niemi,N.M., Lanning,N.J., Westrate,L.M. and MacKeigan,J.P.
  TITLE     Downregulation of the mitochondrial phosphatase PTPMT1 is
            sufficient to promote cancer cell death
  JOURNAL   PLoS One 8 (1), e53803 (2013)
   PUBMED   23326511
  REMARK    GeneRIF: Our data suggest that inhibition of PTPMT1 causes a
            metabolic crisis in cancer cells that induces cell death, and may
            be a mechanism by which cancer cells can be sensitized to currently
            available therapies.
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Xiao,J., Engel,J.L., Zhang,J., Chen,M.J., Manning,G. and Dixon,J.E.
  TITLE     Structural and functional analysis of PTPMT1, a phosphatase
            required for cardiolipin synthesis
  JOURNAL   Proc Natl Acad Sci U S A 108 (29), 11860-11865 (2011)
   PUBMED   21730175
REFERENCE   8  (residues 1 to 201)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Pagliarini,D.J., Worby,C.A. and Dixon,J.E.
  TITLE     A PTEN-like phosphatase with a novel substrate specificity
  JOURNAL   J Biol Chem 279 (37), 38590-38596 (2004)
   PUBMED   15247229
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DR004030.1, BC020242.1, BC073798.1, BC014048.1 and AC104942.5.
            
            Transcript Variant: This variant (1) is the longer transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB013855.1, SRR1660807.125149.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000326674.10/
                                                  ENSP00000325958.9
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..201
                     /product="phosphatidylglycerophosphatase and
                     protein-tyrosine phosphatase 1 isoform 1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /EC_number="3.1.3.27"
                     /note="PTEN-like phosphatase; NB4
                     apoptosis/differentiation related protein;
                     phosphoinositide lipid phosphatase;
                     phosphatidylglycerophosphatase and protein-tyrosine
                     phosphatase 1"
                     /calculated_mol_wt=19889
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q8WUK0.1)"
                     /calculated_mol_wt=2973
     mat_peptide     28..201
                     /product="Phosphatidylglycerophosphatase and
                     protein-tyrosine phosphatase 1. /id=PRO_0000025423"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WUK0.1)"
                     /calculated_mol_wt=19889
     Region          37..185
                     /region_name="PTPMT1"
                     /note="protein-tyrosine phosphatase mitochondrial 1;
                     cd14524"
                     /db_xref="CDD:350374"
     CDS             1..201
                     /gene="PTPMT1"
                     /gene_synonym="DUSP23; MOSP; NEDAXBA; PLIP; PNAS-129"
                     /coded_by="NM_175732.3:25..630"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41643.1"
                     /db_xref="GeneID:114971"
                     /db_xref="HGNC:HGNC:26965"
                     /db_xref="MIM:609538"
ORIGIN      
        1 maatalleag larvlfyptl lytlfrgkvp grahrdwyhr idptvllgal plrsltrqlv
       61 qdenvrgvit mneeyetrfl cnssqewkrl gveqlrlstv dmtgiptldn lqkgvqfalk
      121 yqslgqcvyv hckagrsrsa tmvaayliqv hkwspeeavr aiakirsyih irpgqldvlk
      181 efhkqitara tkdgtfvisk t
//
LOCUS       NP_001341009             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341009 XP_016879182
VERSION     NP_001341009.1
DBSOURCE    REFSEQ: accession NM_001354080.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 4, 2017 this sequence version replaced XP_016879182.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.783202.1,
                                           SRR1660807.128826.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354080.1:453..1217"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001310872             684 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001310872
VERSION     NP_001310872.1
DBSOURCE    REFSEQ: accession NM_001323943.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.29892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..684
                     /product="DIS3-like exonuclease 1 isoform 4"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=77685
     Region          <17..62
                     /region_name="OB_Dis3"
                     /note="Dis3-like cold-shock domain 2 (CSD2); pfam17849"
                     /db_xref="CDD:436091"
     Region          95..445
                     /region_name="RNB"
                     /note="RNB domain; pfam00773"
                     /db_xref="CDD:459934"
     Region          511..586
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..684
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323943.2:1162..3216"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mtvttrlras pqvspclqdf rvvvridswe stsvypnghf vrvlgrigdl egeiatilve
       61 nsisvipfse aqmcempvnt pespwkvspe eeqkrkdlrk shlvfsidpk gcedvddtls
      121 vrtlnngnle lgvhiadvth fvapnsyidi eartrattyy ladrrydmlp svlsadlcsl
      181 lggvdryavs imweldkasy eikkvwygrt iirsayklfy eaaqelldgn lsvvddipef
      241 kdldeksrqa kleelvwaig kltdiarhvr akrdgcgale legvevcvql ddkknihdli
      301 pkqplevhet vaecmilanh wvakkiwesf phqallrqhp pphqeffsel recakakgff
      361 idtrsnktla dsldnandph dpivnrllrs matqamsnal yfstgscaee efhhyglald
      421 kythftspir rysdivvhrl lmaaiskdkk meikgnlfsn kdleelcrhi nnrnqaaqhs
      481 qkqstelfqc myfkdkdpat eercisdgvi ysirtngvll fiprfgikga aylknkdglv
      541 iscgpdscse wkpgslqrfq nkitstttdg esvtfhlfdh vtvrisiqas rchsdtirle
      601 iisnkpykip ntelihqssp llkselvkev tksveeaqla qevkvniiqe eyqeyrqtkg
      661 rslytlleei rdlalldvsn nygi
//
LOCUS       NP_055958                386 aa            linear   PRI 20-NOV-2025
DEFINITION  methionine aminopeptidase 1 [Homo sapiens].
ACCESSION   NP_055958
VERSION     NP_055958.2
DBSOURCE    REFSEQ: accession NM_015143.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Caglayan,A.O., Aktar,F., Bilguvar,K., Baranoski,J.F., Akgumus,G.T.,
            Harmanci,A.S., Erson-Omay,E.Z., Yasuno,K., Caksen,H. and Gunel,M.
  TITLE     METAP1 mutation is a novel candidate for autosomal recessive
            intellectual disability
  JOURNAL   J Hum Genet 66 (2), 215-218 (2021)
   PUBMED   32764695
  REMARK    GeneRIF: METAP1 mutation is a novel candidate for autosomal
            recessive intellectual disability.
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Frottin,F., Bienvenut,W.V., Bignon,J., Jacquet,E., Vaca
            Jacome,A.S., Van Dorsselaer,A., Cianferani,S., Carapito,C.,
            Meinnel,T. and Giglione,C.
  TITLE     MetAP1 and MetAP2 drive cell selectivity for a potent anti-cancer
            agent in synergy, by controlling glutathione redox state
  JOURNAL   Oncotarget 7 (39), 63306-63323 (2016)
   PUBMED   27542228
  REMARK    GeneRIF: MetAP1 and MetAP2 have roles in driving cell selectivity
            for a potent anti-cancer agent in synergy, by controlling
            glutathione redox state
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Kishor,C., Arya,T., Reddi,R., Chen,X., Saddanapu,V., Marapaka,A.K.,
            Gumpena,R., Ma,D., Liu,J.O. and Addlagatta,A.
  TITLE     Identification, biochemical and structural evaluation of
            species-specific inhibitors against type I methionine
            aminopeptidases
  JOURNAL   J Med Chem 56 (13), 5295-5305 (2013)
   PUBMED   23767698
  REMARK    GeneRIF: Data indicate that pyridinylpyrimidine-based molecules
            displayed species specificity behavior against methionine
            aminopeptidases (MetAPs).
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Addlagatta,A., Hu,X., Liu,J.O. and Matthews,B.W.
  TITLE     Structural basis for the functional differences between type I and
            type II human methionine aminopeptidases
  JOURNAL   Biochemistry 44 (45), 14741-14749 (2005)
   PUBMED   16274222
  REMARK    GeneRIF: A comparison of the structual differences between Type I
            and Type II methionine aminopeptidases.
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Serero,A., Giglione,C., Sardini,A., Martinez-Sanz,J. and Meinnel,T.
  TITLE     An unusual peptide deformylase features in the human mitochondrial
            N-terminal methionine excision pathway
  JOURNAL   J Biol Chem 278 (52), 52953-52963 (2003)
   PUBMED   14532271
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Dummitt,B., Fei,Y. and Chang,Y.H.
  TITLE     Functional expression of human methionine aminopeptidase type 1 in
            Saccharomyces cerevisiae
  JOURNAL   Protein Pept Lett 9 (4), 295-303 (2002)
   PUBMED   12144506
  REMARK    GeneRIF: Data show that human methionine aminopeptidase 1 (MetAP1)
            fully rescued the slow growth phenotype associated with deletion of
            yeast MetAP1, suggesting that the yeast and human proteins may have
            similar roles in vivo.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA178462.1, D42084.1 and BC030054.1.
            
            On Jan 3, 2008 this sequence version replaced NP_055958.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.387744.1,
                                           SRR1660803.154438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296411.11/ ENSP00000296411.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..386
                     /product="methionine aminopeptidase 1"
                     /EC_number="3.4.11.18"
                     /note="MAP 1; metAP 1; peptidase M 1"
                     /calculated_mol_wt=43084
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P53582.2)"
     Region          14..382
                     /region_name="APP_MetAP"
                     /note="A family including aminopeptidase P, aminopeptidase
                     M, and prolidase. Also known as metallopeptidase family
                     M24. This family of enzymes is able to cleave amido-,
                     imido- and amidino-containing bonds. Members exibit
                     relatively narrow substrate specificity...; cl00279"
                     /db_xref="CDD:469704"
     Site            order(203,220,231,294,327,358)
                     /site_type="active"
                     /db_xref="CDD:238519"
     CDS             1..386
                     /gene="METAP1"
                     /gene_synonym="MAP1A; MetAP1A"
                     /coded_by="NM_015143.3:34..1194"
                     /db_xref="CCDS:CCDS47110.1"
                     /db_xref="GeneID:23173"
                     /db_xref="HGNC:HGNC:15789"
                     /db_xref="MIM:610151"
ORIGIN      
        1 maavetrvce tdgcsseakl qcptciklgi qgsyfcsqec fkgswathkl lhkkakdeka
       61 krevsswtve gdintdpwag yrytgklrph yplmptrpvp syiqrpdyad hplgmseseq
      121 alkgtsqikl lssediegmr lvcrlarevl dvaagmikpg vtteeidhav hlaciarncy
      181 psplnyynfp kscctsvnev ichgipdrrp lqegdivnvd itlyrngyhg dlnetffvge
      241 vddgarklvq ttyeclmqai davkpgvryr elgniiqkha qangfsvvrs ycghgihklf
      301 htapnvphya knkavgvmks ghvftiepmi ceggwqdetw pdgwtavtrd gkrsaqfeht
      361 llvtdtgcei ltrrldsarp hfmsqf
//
LOCUS       NP_001356372             350 aa            linear   PRI 20-NOV-2025
DEFINITION  NIF3-like protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356372 XP_011509887
VERSION     NP_001356372.1
DBSOURCE    REFSEQ: accession NM_001369443.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Reed,C.J., Hutinet,G. and de Crecy-Lagard,V.
  TITLE     Comparative Genomic Analysis of the DUF34 Protein Family Suggests
            Role as a Metal Ion Chaperone or Insertase
  JOURNAL   Biomolecules 11 (9), 1282 (2021)
   PUBMED   34572495
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 350)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 350)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 350)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 350)
  AUTHORS   Merla,G., Howald,C., Antonarakis,S.E. and Reymond,A.
  TITLE     The subcellular localization of the ChoRE-binding protein, encoded
            by the Williams-Beuren syndrome critical region gene 14, is
            regulated by 14-3-3
  JOURNAL   Hum Mol Genet 13 (14), 1505-1514 (2004)
   PUBMED   15163635
REFERENCE   7  (residues 1 to 350)
  AUTHORS   Tascou,S., Kang,T.W., Trappe,R., Engel,W. and Burfeind,P.
  TITLE     Identification and characterization of NIF3L1 BP1, a novel
            cytoplasmic interaction partner of the NIF3L1 protein
  JOURNAL   Biochem Biophys Res Commun 309 (2), 440-448 (2003)
   PUBMED   12951069
REFERENCE   8  (residues 1 to 350)
  AUTHORS   Akiyama,H., Fujisawa,N., Tashiro,Y., Takanabe,N., Sugiyama,A. and
            Tashiro,F.
  TITLE     The role of transcriptional corepressor Nif3l1 in early stage of
            neural differentiation via cooperation with Trip15/CSN2
  JOURNAL   J Biol Chem 278 (12), 10752-10762 (2003)
   PUBMED   12522100
REFERENCE   9  (residues 1 to 350)
  AUTHORS   Hadano,S., Yanagisawa,Y., Skaug,J., Fichter,K., Nasir,J.,
            Martindale,D., Koop,B.F., Scherer,S.W., Nicholson,D.W.,
            Rouleau,G.A., Ikeda,J. and Hayden,M.R.
  TITLE     Cloning and characterization of three novel genes, ALS2CR1,
            ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis
            (ALS2) critical region at chromosome 2q33-q34: candidate genes for
            ALS2
  JOURNAL   Genomics 71 (2), 200-213 (2001)
   PUBMED   11161814
REFERENCE   10 (residues 1 to 350)
  AUTHORS   Tascou,S., Uedelhoven,J., Dixkens,C., Nayernia,K., Engel,W. and
            Burfeind,P.
  TITLE     Isolation and characterization of a novel human gene, NIF3L1, and
            its mouse ortholog, Nif3l1, highly conserved from bacteria to
            mammals
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 330-336 (2000)
   PUBMED   11124544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005037.2.
            
            On Apr 9, 2019 this sequence version replaced XP_011509887.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.73679.1,
                                           ERR3218379.414081.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..350
                     /product="NIF3-like protein 1 isoform 2"
                     /EC_number="3.5.4.16"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 1; NIF3 (Ngg1 interacting
                     factor 3, S.pombe homolog)-like 1; NIF3-like protein 1;
                     NIF3 NGG1 interacting factor 3-like 1; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 1 protein;
                     GTP cyclohydrolase I; putative GTP cyclohydrolase 1 type 2
                     NIF3L1"
                     /calculated_mol_wt=38853
     Region          6..327
                     /region_name="NIF3"
                     /note="NIF3 (NGG1p interacting factor 3); pfam01784"
                     /db_xref="CDD:426431"
     CDS             1..350
                     /gene="NIF3L1"
                     /gene_synonym="ALS2CR1; CALS-7; MDS015"
                     /coded_by="NM_001369443.1:1258..2310"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS42797.1"
                     /db_xref="GeneID:60491"
                     /db_xref="HGNC:HGNC:13390"
                     /db_xref="MIM:605778"
ORIGIN      
        1 mdlkallssl ndfaslsfae swdnvgllve pspphtvntl fltndlteev meevlqkkad
       61 lilsyhppif rpmkritwnt wkerlviral enrvgiysph taydaapqgv nnwlakglga
      121 ctsrpihpsk apnyptegnh rvefnvnytq dldkvmsavk gidgvsvtsf sartgneeqt
      181 rinlnctqka lmqvvdflsr nkqlyqktei lslekplllh tgmgrlctld esvslatmid
      241 rikrhlklsh irlalgvgrt lesqvkvval cagsgssvlq gveadlyltg emshhdtlda
      301 asqginvilc ehsntergfl sdlrdmldsh lenkiniils etdrdplqvv
//
LOCUS       NP_057417               2752 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 2 [Homo sapiens].
ACCESSION   NP_057417
VERSION     NP_057417.3
DBSOURCE    REFSEQ: accession NM_016333.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2752)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2752)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2752)
  AUTHORS   Guo,J., Zhang,Z., Wang,H., Li,Q., Fan,M., Zhang,W., Tao,Q.,
            Wang,Z., Ling,C., Xiao,H., Gao,Z. and Zhai,Z.
  TITLE     SRRM2 may be a potential biomarker and immunotherapy target for
            multiple myeloma: a real-world study based on flow cytometry
            detection
  JOURNAL   Clin Exp Med 24 (1), 28 (2024)
   PUBMED   38289482
  REMARK    GeneRIF: SRRM2 may be a potential biomarker and immunotherapy
            target for multiple myeloma: a real-world study based on flow
            cytometry detection.
            Erratum:[Clin Exp Med. 2024 Jul 18;24(1):159. doi:
            10.1007/s10238-024-01393-1. PMID: 39023571]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2752)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 2752)
  AUTHORS   Xu,S., Lai,S.K., Sim,D.Y., Ang,W.S.L., Li,H.Y. and Roca,X.
  TITLE     SRRM2 organizes splicing condensates to regulate alternative
            splicing
  JOURNAL   Nucleic Acids Res 50 (15), 8599-8614 (2022)
   PUBMED   35929045
  REMARK    GeneRIF: SRRM2 organizes splicing condensates to regulate
            alternative splicing.
REFERENCE   6  (residues 1 to 2752)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   7  (residues 1 to 2752)
  AUTHORS   McGarvey,T., Rosonina,E., McCracken,S., Li,Q., Arnaout,R.,
            Mientjes,E., Nickerson,J.A., Awrey,D., Greenblatt,J., Grosveld,G.
            and Blencowe,B.J.
  TITLE     The acute myeloid leukemia-associated protein, DEK, forms a
            splicing-dependent interaction with exon-product complexes
  JOURNAL   J Cell Biol 150 (2), 309-320 (2000)
   PUBMED   10908574
REFERENCE   8  (residues 1 to 2752)
  AUTHORS   Sawada,Y., Miura,Y., Umeki,K., Tamaoki,T., Fujinaga,K. and
            Ohtaki,S.
  TITLE     Cloning and characterization of a novel RNA-binding protein SRL300
            with RS domains
  JOURNAL   Biochim Biophys Acta 1492 (1), 191-195 (2000)
   PUBMED   11004489
REFERENCE   9  (residues 1 to 2752)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   10 (residues 1 to 2752)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092117.4, AB016092.1, AB002322.3 and AI083775.1.
            
            On Dec 1, 2006 this sequence version replaced NP_057417.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB016092.1, AB002322.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301740.13/ ENSP00000301740.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..2752
                     /product="serine/arginine repetitive matrix protein 2"
                     /note="splicing coactivator subunit SRm300; RNA binding
                     protein; taxREB803; 300 kDa nuclear matrix antigen;
                     testicular secretory protein Li 53; SR-related nuclear
                     matrix protein of 300 kDa; ser/Arg-related nuclear matrix
                     protein of 300 kDa; tax-responsive enhancer
                     element-binding protein 803; serine/arginine-rich splicing
                     factor-related nuclear matrix protein of 300 kDa"
                     /calculated_mol_wt=299485
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          39..102
                     /region_name="cwf21_SRRM2"
                     /note="cwf21 domain found in serine/arginine repetitive
                     matrix protein 2; cd21375"
                     /db_xref="CDD:410601"
     Site            101
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          141..2131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            169
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          197..259
                     /region_name="Sufficient for RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          293..>600
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          <313..>411
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            534
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            704
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            783
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            846
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            854
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            856
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            935
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            950
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            952
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            954
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            957
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            968
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            974
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            977
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            983
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            992
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            994
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            996
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1003
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1010
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1024
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1028
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1042
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1043
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1049
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1072
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1073
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1099
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1124
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1129
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1188
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1208
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1271
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1401
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1413
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1421
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1434
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1453
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1472
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1492
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1497
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1501
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1511
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1531
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1542
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1577
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1579
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BTI8; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1698
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1818
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1854
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1857
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1878
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1880
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1892
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1916
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1923
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1925
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1927
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1931
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1946
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1948
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1950
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1954
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1958
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1962
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1966
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1970
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1972
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1975
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1978
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1984
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1996
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            1999
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2008
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2011
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2018
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2020
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2022
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2030
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2032
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2042
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2044
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2069
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2071
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2090
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2092
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2194
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          <2195..>2452
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     Site            2207
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2231
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2246
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2274
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2288
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2289
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2291
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2302
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          2311..2342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2316
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2329
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2342
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2381
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2384
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Region          2389..2752
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2409
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2583
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2599
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2677
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2738
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     Site            2740
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UQ35.2)"
     CDS             1..2752
                     /gene="SRRM2"
                     /gene_synonym="300-KD; Cwc21; CWF21; HSPC075; MRD72;
                     SRL300; SRm300"
                     /coded_by="NM_016333.4:241..8499"
                     /db_xref="CCDS:CCDS32373.1"
                     /db_xref="GeneID:23524"
                     /db_xref="HGNC:HGNC:16639"
                     /db_xref="MIM:606032"
ORIGIN      
        1 myngiglptp rgsgtngyvq rnlslvrgrr gerpdykgee elrrleaalv krpnpdildh
       61 erkrrvelrc leleemmeeq gyeeqqiqek vatfrlmlle kdvnpggkee tpgqrpavte
      121 thqlaelnek knerlraafg isdsyvdgss fdpqrrarea kqpapeppkp yslvressss
      181 rsptpkqkkk kkkkdrgrrs esssprrerk ksskkkkhrs eseskkrkhr sptpkskrks
      241 kdkkrkrsrs ttpapksrra hrstsadsas ssdtsrsrsr saaakthtta lagrspspas
      301 grrgegdapf sepgttstqr psspetatkq psspyedkdk dkkeksatrp spspersstg
      361 peppaptpll aerhggspqp lattplsqep vnppseaspt rdrsppkspe klpqsssses
      421 sppspqptkv srhassspes pkpapapgsh reisssptsk nrshgrakrd kshshtpsrr
      481 mgrsrspata krgrsrsrtp tkrghsrsrs pqwrrsrsaq rwgrsrspqr rgrsrspqrp
      541 gwsrsrntqr rgrsrsarrg rshsrspatr grsrsrtpar rgrsrsrtpa rrrsrsrtpt
      601 rrrsrsrtpa rrgrsrsrtp arrrsrtrsp vrrrsrsrsp arrsgrsrsr tparrgrsrs
      661 rtparrgrsr srtparrsgr srsrtparrg rsrsrtprrg rsrsrslvrr grshsrtpqr
      721 rgrsgssser knksrtsqrr srsnsspemk ksrissrrsr slssprskak srlslrrsls
      781 gsspcpkqks qtpprrsrsg ssqpkaksrt pprrsrssss pppkqksktp srqshssssp
      841 hpkvksgtpp rqgsitspqa neqsvtpqrr scfesspdpe lksrtpsrhs csgsspprvk
      901 sstpprqsps rssspqpkvk aiisprqrsh sgssspspsr vtsrttprrs rsvspcsnve
      961 srllpryshs gssspdtkvk petpprqshs gsispypkvk aqtppgpsls gskspcpqek
     1021 skdslvqscp gslslcagvk sstppgesyf gvsslqlkgq sqtspdhrsd tsspevrqsh
     1081 sespslqsks qtspkggrsr ssspvtelas rspirqdrge fsaspmlksg mspeqsrfqs
     1141 dsssyptvds nsllgqsrle taeskekmal ppqedatasp prqkdkfspf pvqdrpessl
     1201 vfkdtlrtpp rersgagssp etkeqnsalp tssqdeelme vvekseepag qilshlssel
     1261 kemstsnfes speveerpav sltldqsqsq asleavevps masswggphf spehkelsns
     1321 plrensfgsp lefrnsgplg temntgfsse vkedlngpfl nqletdpsld mkeqstrssg
     1381 hssselspda vekagmssnq sisspvldav prtpsrerss sasspemkdg lprtpsrrsr
     1441 sgsspglrdg sgtpsrhsls gsspgmkdip rtpsrgrsec dsspepkalp qtprprsrsp
     1501 sspelnnkcl tpqrersgse ssvdqktvar tplgqrsrsg ssqeldvkps aspqersesd
     1561 sspdskaktr tplrqrsrsg sspevdsksr lsprrsrsgs spevkdkpra apraqsgsds
     1621 spepkapapr alprrsrsgs sskgrgpspe gssstesspe hppksrtarr gsrsspepkt
     1681 ksrtpprrrs srsspeltrk arlsrrsrsa ssspetrsrt pprhrrspsv sspepaeksr
     1741 ssrrrrsass prtkttsrrg rspspkprgl qrsrsrsrre ktrttrrrdr sgssqstsrr
     1801 rqrsrsrsrv trrrrggsgy hsrsparqes srtssrrrrg rsrtpptsrk rsrsrtspap
     1861 wkrsrsrasp athrrsrsrt plisrrrsrs rtspvsrrrs rsrtsvtrrr srsraspvsr
     1921 rrsrsrtppv trrrsrsrtp ttrrrsrsrt ppvtrrrsrs rtppvtrrrs rsrtspitrr
     1981 rsrsrtspvt rrrsrsrtsp vtrrrsrsrt spvtrrrsrs rtppairrrs rsrtpllprk
     2041 rsrsrsplai rrrsrsrtpr targkrsltr sppairrrsa sgsssdrsrs atppatrnhs
     2101 gsrtppvaln ssrmscfsrp smsptpldrc rspgmleplg ssrtpmsvlq qaggsmmdgp
     2161 gpripdhqrt svpenhaqsr ialaltaisl gtarpppsms aaglaarmsq vpapvplmsl
     2221 rtapaanlas ripaasaaam nlasartpai ptavnladsr tpaaaaamnl asprtavaps
     2281 avnladprtp tapavnlaga rtpaalaals ltgsgtppta anypsssrtp qapasanlvg
     2341 prsahatapv niagsrtaaa lapasltsar mapalsganl tsprvplsay ervsgrtspp
     2401 lldrarsrtp psapsqsrmt serapspssr mgqapsqsll ppaqdqprsp vpsafsdqsr
     2461 cliaqttpva gsqslssgav atttssagdh ngmlsvpapg vphsdvgepp astgaqqpsa
     2521 laalqpaker rsssssssss ssssssssss ssssssgsss sdsegsslpv qpevalkrvp
     2581 sptpapkeav regrppeptp akrkrrssss ssssssssss ssssssssss ssssssssss
     2641 ssssssssps pakpgpqalp kpaspkkppp gerrsrsprk pidslrdsrs lsyspverrr
     2701 pspqpsprdq qssssergsr rgqrgdsrsp shkrrretps prpmrhrssr sp
//
LOCUS       NP_001357157              76 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 E2 isoform 3 [Homo sapiens].
ACCESSION   NP_001357157
VERSION     NP_001357157.1
DBSOURCE    REFSEQ: accession NM_001370228.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Hong,X., Ma,N., Li,D., Zhang,M., Dong,W., Huang,J., Ci,X. and
            Zhang,S.
  TITLE     UBE2E2 enhances Snail-mediated epithelial-mesenchymal transition
            and Nrf2-mediated antioxidant activity in ovarian cancer
  JOURNAL   Cell Death Dis 14 (2), 100 (2023)
   PUBMED   36765041
  REMARK    GeneRIF: UBE2E2 enhances Snail-mediated epithelial-mesenchymal
            transition and Nrf2-mediated antioxidant activity in ovarian
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Pringa,E., Martinez-Noel,G., Muller,U. and Harbers,K.
  TITLE     Interaction of the ring finger-related U-box motif of a nuclear dot
            protein with ubiquitin-conjugating enzymes
  JOURNAL   J Biol Chem 276 (22), 19617-19623 (2001)
   PUBMED   11274149
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Moynihan,T.P., Ardley,H.C., Nuber,U., Rose,S.A., Jones,P.F.,
            Markham,A.F., Scheffner,M. and Robinson,P.A.
  TITLE     The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with
            RING finger/IBR motif-containing domains of HHARI and H7-AP1
  JOURNAL   J Biol Chem 274 (43), 30963-30968 (1999)
   PUBMED   10521492
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Kimura,M., Hattori,T., Matsuda,Y., Yoshioka,T., Sumi,N., Umeda,Y.,
            Nakashima,S. and Okano,Y.
  TITLE     cDNA cloning, characterization, and chromosome mapping of UBE2E2
            encoding a human ubiquitin-conjugating E2 enzyme
  JOURNAL   Cytogenet Cell Genet 78 (2), 107-111 (1997)
   PUBMED   9371400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135966.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.121662.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..76
                     /product="ubiquitin-conjugating enzyme E2 E2 isoform 3"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-conjugating enzyme E2E 2 (homologous to
                     yeast UBC4/5); ubiquitin-conjugating enzyme E2E 2 (UBC4/5
                     homolog, yeast); ubiquitin-protein ligase E2; ubiquitin
                     carrier protein E2; E2 ubiquitin-conjugating enzyme E2;
                     ubiquitin conjugating enzyme E2E 2"
                     /calculated_mol_wt=8153
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Region          58..>75
                     /region_name="UBCc_UEV"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain/ubiquitin E2 variant (UEV) domain; cl49610"
                     /db_xref="CDD:483950"
     CDS             1..76
                     /gene="UBE2E2"
                     /gene_synonym="UBCH8"
                     /coded_by="NM_001370228.1:147..377"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="GeneID:7325"
                     /db_xref="HGNC:HGNC:12478"
                     /db_xref="MIM:602163"
ORIGIN      
        1 msteaqrvdd spstsggssd gdqresvqqe pereqvqpkk kegkisskta aklstsakri
       61 qkelaeitld pppncr
//
LOCUS       NP_003084                159 aa            linear   PRI 20-NOV-2025
DEFINITION  U1 small nuclear ribonucleoprotein C [Homo sapiens].
ACCESSION   NP_003084
VERSION     NP_003084.1
DBSOURCE    REFSEQ: accession NM_003093.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Campagne,S., de Vries,T., Malard,F., Afanasyev,P., Dorn,G.,
            Dedic,E., Kohlbrecher,J., Boehringer,D., Clery,A. and Allain,F.H.
  TITLE     An in vitro reconstituted U1 snRNP allows the study of the
            disordered regions of the particle and the interactions with
            proteins and ligands
  JOURNAL   Nucleic Acids Res 49 (11), e63 (2021)
   PUBMED   33677607
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Zhang,Y., Qiu,J., Zuo,D., Yuan,Y., Qiu,Y., Qiao,L., He,W., Li,B.
            and Yuan,Y.
  TITLE     SNRPC promotes hepatocellular carcinoma cell motility by inducing
            epithelial-mesenchymal transition
  JOURNAL   FEBS Open Bio 11 (6), 1757-1770 (2021)
   PUBMED   33934562
  REMARK    GeneRIF: SNRPC promotes hepatocellular carcinoma cell motility by
            inducing epithelial-mesenchymal transition.
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Charenton,C., Wilkinson,M.E. and Nagai,K.
  TITLE     Mechanism of 5' splice site transfer for human spliceosome
            activation
  JOURNAL   Science 364 (6438), 362-367 (2019)
   PUBMED   30975767
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Gunnewiek,J.M., van Aarssen,Y., Wassenaar,R., Legrain,P., van
            Venrooij,W.J. and Nelissen,R.L.
  TITLE     Homodimerization of the human U1 snRNP-specific protein C
  JOURNAL   Nucleic Acids Res 23 (23), 4864-4871 (1995)
   PUBMED   8532530
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Nelissen,R.L., Will,C.L., van Venrooij,W.J. and Luhrmann,R.
  TITLE     The association of the U1-specific 70K and C proteins with U1
            snRNPs is mediated in part by common U snRNP proteins
  JOURNAL   EMBO J 13 (17), 4113-4125 (1994)
   PUBMED   8076607
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Nelissen,R.L., Heinrichs,V., Habets,W.J., Simons,F., Luhrmann,R.
            and van Venrooij,W.J.
  TITLE     Zinc finger-like structure in U1-specific protein C is essential
            for specific binding to U1 snRNP
  JOURNAL   Nucleic Acids Res 19 (3), 449-454 (1991)
   PUBMED   1826349
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Sillekens,P.T., Beijer,R.P., Habets,W.J. and van Venrooij,W.J.
  TITLE     Human U1 snRNP-specific C protein: complete cDNA and protein
            sequence and identification of a multigene family in mammals
  JOURNAL   Nucleic Acids Res 16 (17), 8307-8321 (1988)
   PUBMED   2971157
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Yamamoto,K., Miura,H., Moroi,Y., Yoshinoya,S., Goto,M., Nishioka,K.
            and Miyamoto,T.
  TITLE     Isolation and characterization of a complementary DNA expressing
            human U1 small nuclear ribonucleoprotein C polypeptide
  JOURNAL   J Immunol 140 (1), 311-317 (1988)
   PUBMED   2961811
  REMARK    Erratum:[J Immunol 1988 Apr 1;140(7):2477]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD109745.1, AK311955.1,
            AI356808.1 and BU153661.1.
            
            Summary: This gene encodes one of the specific protein components
            of the U1 small nuclear ribonucleoprotein (snRNP) particle required
            for the formation of the spliceosome. The encoded protein
            participates in the processing of nuclear precursor messenger RNA
            splicing. snRNP particles are attacked by autoantibodies frequently
            produced by patients with connective tissue diseases. The genome
            contains several pseudogenes of this functional gene. Alternative
            splicing results in a non-coding transcript variant.[provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP338623.1, SRR5189658.56470.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244520.10/ ENSP00000244520.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..159
                     /product="U1 small nuclear ribonucleoprotein C"
                     /note="U1 small nuclear RNP specific C; U1 snRNP protein
                     C; U1 snRNP C"
                     /calculated_mol_wt=17263
     Region          1..38
                     /region_name="zf-U1"
                     /note="U1 zinc finger; pfam06220"
                     /db_xref="CDD:368798"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P09234.1)"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09234.1)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09234.1)"
     Region          62..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09234.1)"
     Region          140..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09234.1)"
     CDS             1..159
                     /gene="SNRPC"
                     /gene_synonym="U1C; Yhc1"
                     /coded_by="NM_003093.3:40..519"
                     /db_xref="CCDS:CCDS34436.1"
                     /db_xref="GeneID:6631"
                     /db_xref="HGNC:HGNC:11157"
                     /db_xref="MIM:603522"
ORIGIN      
        1 mpkfycdycd tylthdspsv rkthcsgrkh kenvkdyyqk wmeeqaqsli dkttaafqqg
       61 kipptpfsap ppagamippp pslpgpprpg mmpaphmggp pmmpmmgppp pgmmpvgpap
      121 gmrppmgghm pmmpgppmmr pparpmmvpt rpgmtrpdr
//
LOCUS       NP_002253                179 aa            linear   PRI 20-NOV-2025
DEFINITION  natural killer cells antigen CD94 isoform 1 [Homo sapiens].
ACCESSION   NP_002253
VERSION     NP_002253.2
DBSOURCE    REFSEQ: accession NM_002262.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Verma,K., Croft,W., Pearce,H., Zuo,J., Stephens,C., Nunnick,J.,
            Kinsella,F.A., Malladi,R. and Moss,P.
  TITLE     Early expression of CD94 and loss of CD96 on CD8+ T cells after
            allogeneic stem cell tranplantation is predictive of subsequent
            relapse and survival
  JOURNAL   Haematologica 108 (2), 433-443 (2023)
   PUBMED   35924575
  REMARK    GeneRIF: Early expression of CD94 and loss of CD96 on CD8+ T cells
            after allogeneic stem cell tranplantation is predictive of
            subsequent relapse and survival.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Fang,H., Wang,W., Kadia,T.M., El Hussein,S., Wang,S.A. and
            Khoury,J.D.
  TITLE     CD94 expression patterns in reactive and neoplastic T-cell and
            NK-cell proliferations
  JOURNAL   Leuk Res 108, 106614 (2021)
   PUBMED   33990003
  REMARK    GeneRIF: CD94 expression patterns in reactive and neoplastic T-cell
            and NK-cell proliferations.
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Zhang,Q., Zheng,Y., Ning,M. and Li,T.
  TITLE     KLRD1, FOSL2 and LILRB3 as potential biomarkers for plaques
            progression in acute myocardial infarction and stable coronary
            artery disease
  JOURNAL   BMC Cardiovasc Disord 21 (1), 344 (2021)
   PUBMED   34271875
  REMARK    GeneRIF: KLRD1, FOSL2 and LILRB3 as potential biomarkers for
            plaques progression in acute myocardial infarction and stable
            coronary artery disease.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Prasnikar,E., Perdih,A. and Borisek,J.
  TITLE     Nonameric Peptide Orchestrates Signal Transduction in the
            Activating HLA-E/NKG2C/CD94 Immune Complex as Revealed by All-Atom
            Simulations
  JOURNAL   Int J Mol Sci 22 (13), 6670 (2021)
   PUBMED   34206395
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Shreeve,N., Depierreux,D., Hawkes,D., Traherne,J.A., Sovio,U.,
            Huhn,O., Jayaraman,J., Horowitz,A., Ghadially,H., Perry,J.R.B.,
            Moffett,A., Sled,J.G., Sharkey,A.M. and Colucci,F.
  TITLE     The CD94/NKG2A inhibitory receptor educates uterine NK cells to
            optimize pregnancy outcomes in humans and mice
  JOURNAL   Immunity 54 (6), 1231-1244 (2021)
   PUBMED   33887202
  REMARK    GeneRIF: The CD94/NKG2A inhibitory receptor educates uterine NK
            cells to optimize pregnancy outcomes in humans and mice.
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Brooks,A.G., Posch,P.E., Scorzelli,C.J., Borrego,F. and
            Coligan,J.E.
  TITLE     NKG2A complexed with CD94 defines a novel inhibitory natural killer
            cell receptor
  JOURNAL   J Exp Med 185 (4), 795-800 (1997)
   PUBMED   9034158
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Lazetic,S., Chang,C., Houchins,J.P., Lanier,L.L. and Phillips,J.H.
  TITLE     Human natural killer cell receptors involved in MHC class I
            recognition are disulfide-linked heterodimers of CD94 and NKG2
            subunits
  JOURNAL   J Immunol 157 (11), 4741-4745 (1996)
   PUBMED   8943374
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Phillips,J.H., Chang,C., Mattson,J., Gumperz,J.E., Parham,P. and
            Lanier,L.L.
  TITLE     CD94 and a novel associated protein (94AP) form a NK cell receptor
            involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes
  JOURNAL   Immunity 5 (2), 163-172 (1996)
   PUBMED   8769479
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Chang,C., Rodriguez,A., Carretero,M., Lopez-Botet,M., Phillips,J.H.
            and Lanier,L.L.
  TITLE     Molecular characterization of human CD94: a type II membrane
            glycoprotein related to the C-type lectin superfamily
  JOURNAL   Eur J Immunol 25 (9), 2433-2437 (1995)
   PUBMED   7589107
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Moretta,A., Vitale,M., Sivori,S., Bottino,C., Morelli,L.,
            Augugliaro,R., Barbaresi,M., Pende,D., Ciccone,E., Lopez-Botet,M.
            and Moretta,L.
  TITLE     Human natural killer cell receptors for HLA-class I molecules.
            Evidence that the Kp43 (CD94) molecule functions as receptor for
            HLA-B alleles
  JOURNAL   J Exp Med 180 (2), 545-555 (1994)
   PUBMED   8046333
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022075.29 and U30610.1.
            
            On May 2, 2017 this sequence version replaced NP_002253.1.
            
            Summary: Natural killer (NK) cells are a distinct lineage of
            lymphocytes that mediate cytotoxic activity and secrete cytokines
            upon immune stimulation. Several genes of the C-type lectin
            superfamily, including members of the NKG2 family, are expressed by
            NK cells and may be involved in the regulation of NK cell function.
            KLRD1 (CD94) is an antigen preferentially expressed on NK cells and
            is classified as a type II membrane protein because it has an
            external C terminus. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, May
            2017].
            
            Transcript Variant: This variant (1) , as well as variants 3 and 5,
            encodes isoform 1.
            
            Sequence Note: This record represents a predicted microRNA
            stem-loop as defined by miRBase. Some sequence at the 5' and 3'
            ends may not be included in the intermediate precursor miRNA
            produced by Drosha cleavage.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279864.3612.1, BC028009.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336164.9/ ENSP00000338130.4
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.2"
     Protein         1..179
                     /product="natural killer cells antigen CD94 isoform 1"
                     /note="natural killer cells antigen CD94; CD94 antigen;
                     KP43; NK cell receptor; killer cell lectin-like receptor
                     subfamily D, member 1"
                     /calculated_mol_wt=20382
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13241.2)"
     Region          61..176
                     /region_name="CLECT_NK_receptors_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in natural killer cell receptors (NKRs); cd03593"
                     /db_xref="CDD:153063"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13241.2)"
     Site            order(114,141,159,162..163)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153063"
     Site            132
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13241.2)"
     CDS             1..179
                     /gene="KLRD1"
                     /gene_synonym="CD94"
                     /coded_by="NM_002262.5:209..748"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8621.1"
                     /db_xref="GeneID:3824"
                     /db_xref="HGNC:HGNC:6378"
                     /db_xref="MIM:602894"
ORIGIN      
        1 mavfkttlwr lisgtlgiic lslmstlgil lknsftklsi epaftpgpni elqkdsdccs
       61 cqekwvgyrc ncyfisseqk twnesrhlca sqkssllqlq ntdeldfmss sqqfywigls
      121 yseehtawlw engsalsqyl fpsfetfntk nciaynpngn aldescedkn ryickqqli
//
LOCUS       NP_003074                334 aa            linear   PRI 20-NOV-2025
DEFINITION  snRNA-activating protein complex subunit 2 [Homo sapiens].
ACCESSION   NP_003074
VERSION     NP_003074.1
DBSOURCE    REFSEQ: accession NM_003083.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Harrigan,J.A., Belotserkovskaya,R., Coates,J., Dimitrova,D.S.,
            Polo,S.E., Bradshaw,C.R., Fraser,P. and Jackson,S.P.
  TITLE     Replication stress induces 53BP1-containing OPT domains in G1 cells
  JOURNAL   J Cell Biol 193 (1), 97-108 (2011)
   PUBMED   21444690
  REMARK    GeneRIF: The findings invoke a model wherein incomplete DNA
            synthesis during S phase leads to a DNA damage response and
            formation of 53BP1-OPT domains in the subsequent G1.
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Shanmugam,M. and Hernandez,N.
  TITLE     Mitotic functions for SNAP45, a subunit of the small nuclear
            RNA-activating protein complex SNAPc
  JOURNAL   J Biol Chem 283 (21), 14845-14856 (2008)
   PUBMED   18356157
  REMARK    GeneRIF: SNAP45 plays two roles in the cell, one as a subunit of
            the transcription factor SNAP(c) and another as a factor required
            for proper mitotic progression
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Emran,F., Florens,L., Ma,B., Swanson,S.K., Washburn,M.P. and
            Hernandez,N.
  TITLE     A role for Yin Yang-1 (YY1) in the assembly of snRNA transcription
            complexes
  JOURNAL   Gene 377, 96-108 (2006)
   PUBMED   16769183
REFERENCE   5  (residues 1 to 334)
  AUTHORS   Hinkley,C.S., Hirsch,H.A., Gu,L., LaMere,B. and Henry,R.W.
  TITLE     The small nuclear RNA-activating protein 190 Myb DNA binding domain
            stimulates TATA box-binding protein-TATA box recognition
  JOURNAL   J Biol Chem 278 (20), 18649-18657 (2003)
   PUBMED   12621023
REFERENCE   6  (residues 1 to 334)
  AUTHORS   Wong,M.W., Henry,R.W., Ma,B., Kobayashi,R., Klages,N., Matthias,P.,
            Strubin,M. and Hernandez,N.
  TITLE     The large subunit of basal transcription factor SNAPc is a Myb
            domain protein that interacts with Oct-1
  JOURNAL   Mol Cell Biol 18 (1), 368-377 (1998)
   PUBMED   9418884
REFERENCE   7  (residues 1 to 334)
  AUTHORS   Henry,R.W., Ma,B., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     Cloning and characterization of SNAP50, a subunit of the
            snRNA-activating protein complex SNAPc
  JOURNAL   EMBO J 15 (24), 7129-7136 (1996)
   PUBMED   9003788
REFERENCE   8  (residues 1 to 334)
  AUTHORS   Sadowski,C.L., Henry,R.W., Kobayashi,R. and Hernandez,N.
  TITLE     The SNAP45 subunit of the small nuclear RNA (snRNA) activating
            protein complex is required for RNA polymerase II and III snRNA
            gene transcription and interacts with the TATA box binding protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (9), 4289-4293 (1996)
   PUBMED   8633057
REFERENCE   9  (residues 1 to 334)
  AUTHORS   Yoon,J.B. and Roeder,R.G.
  TITLE     Cloning of two proximal sequence element-binding transcription
            factor subunits (gamma and delta) that are required for
            transcription of small nuclear RNA genes by RNA polymerases II and
            III and interact with the TATA-binding protein
  JOURNAL   Mol Cell Biol 16 (1), 1-9 (1996)
   PUBMED   8524284
REFERENCE   10 (residues 1 to 334)
  AUTHORS   Henry,R.W., Sadowski,C.L., Kobayashi,R. and Hernandez,N.
  TITLE     A TBP-TAF complex required for transcription of human snRNA genes
            by RNA polymerase II and III
  JOURNAL   Nature 374 (6523), 653-656 (1995)
   PUBMED   7715707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U44755.1 and AC010336.8.
            
            Summary: This gene encodes a subunit of the snRNA-activating
            protein complex which is associated with the TATA box-binding
            protein. The encoded protein is necessary for RNA polymerase II and
            III dependent small-nuclear RNA gene transcription. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Nov 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U44755.1, SRR3476690.130996.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221573.11/ ENSP00000221573.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..334
                     /product="snRNA-activating protein complex subunit 2"
                     /note="proximal sequence element-binding transcription
                     factor subunit delta; PSE-binding factor subunit delta;
                     PTF subunit delta; SNAPC 45 kDa subunit; SNAPc subunit 2;
                     snRNA-activating protein complex 45 kDa subunit; small
                     nuclear RNA activating complex, polypeptide 2, 45kD; small
                     nuclear RNA activating complex, polypeptide 2, 45kDa"
                     /calculated_mol_wt=35425
     Region          14..334
                     /region_name="SNAPC2"
                     /note="Small nuclear RNA activating complex (SNAPc),
                     subunit 2; pfam11035"
                     /db_xref="CDD:463210"
     Region          137..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13487.1)"
     Region          271..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13487.1)"
     CDS             1..334
                     /gene="SNAPC2"
                     /gene_synonym="PTFDELTA; SNAP45"
                     /coded_by="NM_003083.4:30..1034"
                     /db_xref="CCDS:CCDS12190.1"
                     /db_xref="GeneID:6618"
                     /db_xref="HGNC:HGNC:11135"
                     /db_xref="MIM:605076"
ORIGIN      
        1 mkppprrraa parylgevtg patwsarekr qlvrllqarq gqpepdatel arelrgrsea
       61 eirvflqqlk grvareaiqk vhpgglqgpr rreaqppapi evwtdlaeki tgpleealav
      121 afsqvltiaa tepvtllhsk ppkptqargk plllsapggq edpapeipss apaapssapr
      181 tpdpapekps essagpstee dfavdfekiy kylssvsrsg rspelsaaes avvldllmsl
      241 peelpllpct alvehmtety lrltapqpip aggslgpaae gdgagskape etppatekae
      301 hselkspwqa agicplnpfl vplellgraa tpar
//
LOCUS       NP_001337599             688 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001337599
VERSION     NP_001337599.1
DBSOURCE    REFSEQ: accession NM_001350670.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 688)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (7), as well as variants 5 and 6,
            encodes isoform 2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.201924.1,
                                           SRR1660809.256962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..688
                     /product="krev interaction trapped protein 1 isoform 2"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=78519
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          <282..373
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(282..284,286..287,291,294,304,306,308,312..313,
                     316..318,320..321,325,328,338,340,342,346..347,353..355,
                     357..358,362)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          306..338
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          373..592
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          588..687
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(602,621,623,629)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(633,638..641,675,679,682..683)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            675..686
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..688
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350670.1:732..2798"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS34679.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkygkveatr illekgkcnp
      301 nllngqlssp lhfaagggha eivqillnhp etdrhitdqq grsplnicee nkqnnweeaa
      361 kllkeainkp yekvriyrmd gsyrsvelkh gnnttvqqim egmrlsqetq qyftiwicse
      421 nlslqlkpyh kplqhvrdwp eilaeltnld pqretpqlfl rrdvrlplev ekqiedplai
      481 lilfdearyn llkgfytapd aklitlasll lqivygnyes kkhkqgflne enlksivpvt
      541 klkskaphwt nrilheyknl stsegvskem hhlqrmflqn cweiptygaa fftgqiftka
      601 spsnhkvipv yvgvnikglh llnmetkall islkygcfmw qlgdtdtcfq ihsmenkmsf
      661 ivhtkqaglv vkllmklngq lmpterns
//
LOCUS       NP_001057                461 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 1B precursor
            [Homo sapiens].
ACCESSION   NP_001057
VERSION     NP_001057.1
DBSOURCE    REFSEQ: accession NM_001066.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Hu,Y., Lou,X., Zhang,K., Pan,L., Bai,Y., Wang,L., Wang,M., Yan,Y.,
            Wan,J., Yao,X., Duan,X., Ni,C. and Qin,Z.
  TITLE     Tumor necrosis factor receptor 2 promotes endothelial cell-mediated
            suppression of CD8+ T cells through tuning glycolysis in
            chemoresistance of breast cancer
  JOURNAL   J Transl Med 22 (1), 672 (2024)
   PUBMED   39033271
  REMARK    GeneRIF: Tumor necrosis factor receptor 2 promotes endothelial
            cell-mediated suppression of CD8+ T cells through tuning glycolysis
            in chemoresistance of breast cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Al-Lamki,R.S., Tolkovsky,A.M., Alawwami,M., Lu,W., Field,S.F.,
            Wang,J., Pober,J.S. and Bradley,J.R.
  TITLE     Tumor Necrosis Factor Receptor-2 Signals Clear-Cell Renal Carcinoma
            Proliferation via Phosphorylated 4E Binding Protein-1 and
            Mitochondrial Gene Translation
  JOURNAL   Am J Pathol 194 (7), 1374-1387 (2024)
   PUBMED   38537932
  REMARK    GeneRIF: Tumor Necrosis Factor Receptor-2 Signals Clear-Cell Renal
            Carcinoma Proliferation via Phosphorylated 4E Binding Protein-1 and
            Mitochondrial Gene Translation.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Montoya-Buelna,M., Alvarado-Navarro,A., Munoz-Valle,J.F.,
            Lopez-Roa,R.I., Guerrero-Velazquez,C. and Fafutis-Morris,M.
  TITLE     Association of polymorphisms in the TNFA, TNFRSF1A and TNFRSF1B
            genes with lepromatous leprosy in Western Mexican patients
  JOURNAL   J Infect Dev Ctries 18 (5), 770-778 (2024)
   PUBMED   38865403
  REMARK    GeneRIF: Association of polymorphisms in the TNFA, TNFRSF1A and
            TNFRSF1B genes with lepromatous leprosy in Western Mexican
            patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Carvalho,B.F., Gomez,G.V.B., Carron,J., Macedo,L.T.,
            Goncalves,G.M., Vazquez,V.L., Serrano,S.V., Lourenco,G.J. and
            Lima,C.S.P.
  TITLE     TNFRSF1B Gene Variants in Clinicopathological Aspects and Prognosis
            of Patients with Cutaneous Melanoma
  JOURNAL   Int J Mol Sci 25 (5), 2868 (2024)
   PUBMED   38474115
  REMARK    GeneRIF: TNFRSF1B Gene Variants in Clinicopathological Aspects and
            Prognosis of Patients with Cutaneous Melanoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Pocsik,E., Higuchi,M. and Aggarwal,B.B.
  TITLE     Down-modulation of cell surface expression of p80 form of the tumor
            necrosis factor receptor by human immunodeficiency virus-1 tat gene
  JOURNAL   Lymphokine Cytokine Res 11 (6), 317-325 (1992)
   PUBMED   1335762
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Pennica,D., Lam,V.T., Mize,N.K., Weber,R.F., Lewis,M., Fendly,B.M.,
            Lipari,M.T. and Goeddel,D.V.
  TITLE     Biochemical properties of the 75-kDa tumor necrosis factor
            receptor. Characterization of ligand binding, internalization, and
            receptor phosphorylation
  JOURNAL   J Biol Chem 267 (29), 21172-21178 (1992)
   PUBMED   1328224
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Ryffel,B., Brockhaus,M., Greiner,B., Mihatsch,M.J. and Gudat,F.
  TITLE     Tumour necrosis factor receptor distribution in human lymphoid
            tissue
  JOURNAL   Immunology 74 (3), 446-452 (1991)
   PUBMED   1663076
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Kemper,O., Derre,J., Cherif,D., Engelmann,H., Wallach,D. and
            Berger,R.
  TITLE     The gene for the type II (p75) tumor necrosis factor receptor
            (TNF-RII) is localized on band 1p36.2-p36.3
  JOURNAL   Hum Genet 87 (5), 623-624 (1991)
   PUBMED   1655619
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Bost,R. and Hostein,J.
  TITLE     [Gastroduodenal reflux and non-ulcerous dyspepsia. Is it an
            accidental association?]
  JOURNAL   Ann Gastroenterol Hepatol (Paris) 27 (4), 191-192 (1991)
   PUBMED   1929203
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357835.11 and AL031276.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This protein and TNF-receptor 1 form a
            heterocomplex that mediates the recruitment of two anti-apoptotic
            proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase
            activity. The function of IAPs in TNF-receptor signalling is
            unknown, however, c-IAP1 is thought to potentiate TNF-induced
            apoptosis by the ubiquitination and degradation of
            TNF-receptor-associated factor 2, which mediates anti-apoptotic
            signals. Knockout studies in mice also suggest a role of this
            protein in protecting neurons from apoptosis by stimulating
            antioxidative pathways. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M32315.1, SRR1803617.222840.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376259.7/ ENSP00000365435.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..461
                     /product="tumor necrosis factor receptor superfamily
                     member 1B precursor"
                     /note="tumor necrosis factor beta receptor; tumor necrosis
                     factor binding protein 2; p75 TNF receptor; TNF-R2;
                     TNF-RII; p80 TNF-alpha receptor; tumor necrosis factor
                     receptor 2; tumor necrosis factor receptor type II; tumor
                     necrosis factor receptor superfamily member 1B"
                     /calculated_mol_wt=46091
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2219
     mat_peptide     23..461
                     /product="tumor necrosis factor receptor superfamily
                     member 1B"
                     /calculated_mol_wt=46091
     Site            30
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:25456591; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Region          39..76
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Region          40..201
                     /region_name="TNFRSF1B"
                     /note="Tumor necrosis factor receptor superfamily member
                     1B (TNFRSF1B), also known as TNFR2; cd10577"
                     /db_xref="CDD:276903"
     Region          40..75
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276903"
     Region          77..118
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Region          78..118
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276903"
     Site            order(80,82,84..86,88..90,92..96,98..99,116,128,130..131,
                     135..136)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276903"
     Site            order(99..100,103,121,171..173,197,199)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:276903"
     Region          119..162
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Region          120..143
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276903"
     Region          161..201
                     /region_name="CRD4"
                     /note="CRD4 [structural motif]"
                     /db_xref="CDD:276903"
     Region          163..201
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Site            171
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Site            206
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:25456591; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Region          208..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Site            221
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine.
                     /evidence=ECO:0000269|PubMed:25456591; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Site            222
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:25456591; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Site            258..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Region          321..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P20333.3)"
     Region          394..461
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20333.3)"
     CDS             1..461
                     /gene="TNFRSF1B"
                     /gene_synonym="CD120b; p75; p75TNFR; TBPII; TNF-R-II;
                     TNF-R75; TNFBR; TNFR1B; TNFR2; TNFR80"
                     /coded_by="NM_001066.3:102..1487"
                     /db_xref="CCDS:CCDS145.1"
                     /db_xref="GeneID:7133"
                     /db_xref="HGNC:HGNC:11917"
                     /db_xref="MIM:191191"
ORIGIN      
        1 mapvavwaal avglelwaaa halpaqvaft pyapepgstc rlreyydqta qmccskcspg
       61 qhakvfctkt sdtvcdsced stytqlwnwv peclscgsrc ssdqvetqac treqnrictc
      121 rpgwycalsk qegcrlcapl rkcrpgfgva rpgtetsdvv ckpcapgtfs nttsstdicr
      181 phqicnvvai pgnasmdavc tstsptrsma pgavhlpqpv strsqhtqpt pepstapsts
      241 fllpmgpspp aegstgdfal pvglivgvta lglliigvvn cvimtqvkkk plclqreakv
      301 phlpadkarg tqgpeqqhll itapssssss lessasaldr raptrnqpqa pgveasgage
      361 arastgssds spgghgtqvn vtcivnvcss sdhssqcssq asstmgdtds spsespkdeq
      421 vpfskeecaf rsqletpetl lgsteekplp lgvpdagmkp s
//
LOCUS       NP_006054                606 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 41 [Homo sapiens].
ACCESSION   NP_006054
VERSION     NP_006054.2
DBSOURCE    REFSEQ: accession NM_006063.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 606)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 606)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 606)
  AUTHORS   Jirka,C., Pak,J.H., Grosgogeat,C.A., Marchetii,M.M. and Gupta,V.A.
  TITLE     Dysregulation of NRAP degradation by KLHL41 contributes to
            pathophysiology in nemaline myopathy
  JOURNAL   Hum Mol Genet 28 (15), 2549-2560 (2019)
   PUBMED   30986853
REFERENCE   4  (residues 1 to 606)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   5  (residues 1 to 606)
  AUTHORS   Marttila,M., Hanif,M., Lemola,E., Nowak,K.J., Laitila,J.,
            Gronholm,M., Wallgren-Pettersson,C. and Pelin,K.
  TITLE     Nebulin interactions with actin and tropomyosin are altered by
            disease-causing mutations
  JOURNAL   Skelet Muscle 4, 15 (2014)
   PUBMED   25110572
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 606)
  AUTHORS   Zhang,D.D., Lo,S.C., Sun,Z., Habib,G.M., Lieberman,M.W. and
            Hannink,M.
  TITLE     Ubiquitination of Keap1, a BTB-Kelch substrate adaptor protein for
            Cul3, targets Keap1 for degradation by a proteasome-independent
            pathway
  JOURNAL   J Biol Chem 280 (34), 30091-30099 (2005)
   PUBMED   15983046
REFERENCE   7  (residues 1 to 606)
  AUTHORS   Lim,D.S., Roberts,R. and Marian,A.J.
  TITLE     Expression profiling of cardiac genes in human hypertrophic
            cardiomyopathy: insight into the pathogenesis of phenotypes
  JOURNAL   J Am Coll Cardiol 38 (4), 1175-1180 (2001)
   PUBMED   11583900
REFERENCE   8  (residues 1 to 606)
  AUTHORS   Spence,H.J., Johnston,I., Ewart,K., Buchanan,S.J., Fitzgerald,U.
            and Ozanne,B.W.
  TITLE     Krp1, a novel kelch related protein that is involved in pseudopod
            elongation in transformed cells
  JOURNAL   Oncogene 19 (10), 1266-1276 (2000)
   PUBMED   10713668
REFERENCE   9  (residues 1 to 606)
  AUTHORS   Taylor,A., Obholz,K., Linden,G., Sadiev,S., Klaus,S. and
            Carlson,K.D.
  TITLE     DNA sequence and muscle-specific expression of human sarcosin
            transcripts
  JOURNAL   Mol Cell Biochem 183 (1-2), 105-112 (1998)
   PUBMED   9655184
REFERENCE   10 (residues 1 to 606)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF333387.1, BC006534.2,
            AF056929.1 and AA194290.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 23, 2004 this sequence version replaced NP_006054.1.
            
            Summary: This gene is a member of the kelch-like family. The
            encoded protein contains a BACK domain, a BTB/POZ domain, and 5
            Kelch repeats. This protein is thought to function in skeletal
            muscle development and maintenance. Mutations in this gene have
            been associated with nemaline myopathy (NM), a rare congenital
            muscle disorder. [provided by RefSeq, Mar 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.230697.1,
                                           SRR1660809.122045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284669.2/ ENSP00000284669.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.1"
     Protein         1..606
                     /product="kelch-like protein 41"
                     /note="sarcomeric muscle protein; kel-like protein 23;
                     kelch-related protein 1; kelch repeat and BTB (POZ) domain
                     containing 10"
                     /calculated_mol_wt=67906
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ER30; propagated from
                     UniProtKB/Swiss-Prot (O60662.2)"
     Region          6..135
                     /region_name="BTB_POZ_KLHL41_KBTBD10"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 41 (KLHL41); cd18341"
                     /db_xref="CDD:349650"
     Region          39..578
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          335..384
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          346..398
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O60662.2)"
     Region          388..433
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          399..447
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60662.2)"
     Region          437..482
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          448..495
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O60662.2)"
     Region          485..530
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          497..542
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O60662.2)"
     Region          544..599
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O60662.2)"
     CDS             1..606
                     /gene="KLHL41"
                     /gene_synonym="KBTBD10; Krp1; SARCOSIN"
                     /coded_by="NM_006063.3:78..1898"
                     /db_xref="CCDS:CCDS2234.1"
                     /db_xref="GeneID:10324"
                     /db_xref="HGNC:HGNC:16905"
                     /db_xref="MIM:607701"
ORIGIN      
        1 mdsqrelaee lrlyqstllq dglkdlldek kfidctlkag dkslpchrli lsacspyfre
       61 yflseideak kkevvldnvd paildliiky lysasidlnd gnvqdifala srfqipsvft
      121 vcvsylqkrl apgnclailr lgllldcprl aisarefvsd rfvqickeed fmqlspqeli
      181 svisndslnv ekeeavfeav mkwvrtdken rvknlsevfd cirfrlmtek yfkdhvekdd
      241 iiksnpdlqk kikvlkdafa gklpepskna aktgagevng dvgdedllpg ylndiprhgm
      301 fvkdlillvn dtaavaydpt enecyltala eqiprnhssi vtqqnqiyvv gglyvdeenk
      361 dqplqsyffq ldsiasewvg lpplpsarcl fglgevddki yvvagkdlqt easldsvlcy
      421 dpvaakwnev kklpikvygh nvishkgmiy clggktddkk ctnrvfifnp kkgdwkdlap
      481 mkiprsmfgv avhkgkivia ggvtedglsa sveafdlttn kwdvmtefpq erssislvsl
      541 agslyaiggf amiqleskef aptevndiwk yeddkkewag mlkeiryasg asclatrlnl
      601 fklskl
//
LOCUS       NP_001353584            1461 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 1 [Homo sapiens].
ACCESSION   NP_001353584
VERSION     NP_001353584.1
DBSOURCE    REFSEQ: accession NM_001366655.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1461)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1461)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 1461)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 1461)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 1461)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 1461)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 1461)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 1461)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 1461)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 1461)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091928.3, AC011363.6, AC008456.6 and AC008388.7.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.185854.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..1461
                     /product="phospholipid-transporting ATPase VB isoform 1"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=165260
     Region          68..1213
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            83..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            111..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            317..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            369..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            order(433..435,766,790..792,868,915..917,1029,1032,1035,
                     1055,1058)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            433..439
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319770"
     Site            433
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319770"
     Region          496..541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          640..687
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1112..1132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1145..1164
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1195..1216
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1224..1246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1253..1273
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            1292..1316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          1346..1397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     CDS             1..1461
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001366655.1:663..5048"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS43394.1"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 malsvdsswh rwqwrvrdgf phcpsettpl lspekgrqsy nltqqrvvfp nnsifhqdwe
       61 evsrrypgnr tcttkytlft flprnlfeqf hrwanlyflf lvilnwmpsm evfhreitml
      121 plaivlfvim ikdgmedfkr hrfdkaincs niriyerkeq tyvqkcwkdv rvgdfiqmkc
      181 neivpadill lfssdpngic hletasldge tnlkqrcvvk gfsqqevqfe pelfhntivc
      241 ekpnnhlnkf kgymehpdqt rtgfgcesll lrgctirnte mavgiviyag hetkamlnns
      301 gprykrskie rrmnidiffc igililmcli gavghsiwng tfeehppfdv pdangsflps
      361 alggfymflt miillqvlip islyvsielv klgqvfflsn dldlydeetd lsiqcralni
      421 aedlgqiqyi fsdktgtlte nkmvfrrcti mgseyshqen akrletpkel dsdgeewtqy
      481 qclsfsarwa qdpatmrsqk gaqplrrsqs arvpiqghyr qrsmghress qppvafsssi
      541 ekdvtpdknl ltkvrdaalw letlsdsrpa kaslsttssi adfflaltic nsvmvsttte
      601 prqrvtikps skalgtslek iqqlfqklkl lslsqsfsst apsdtdlges lganvattds
      661 derddasvcs ggdstddggy rssmwdqgdi lesgsgtsle ealeapatdl arpefcyeae
      721 spdeaalvha ahaysftlvs rtpeqvtvrl pqgtcltfsl lctlgfdsvr krmsvvvrhp
      781 ltgeivvytk gadsvimdll edpacvpdin mekklrkira rtqkhldlya rdglrtlcia
      841 kkvvseedfr rwasfrreae asldnrdell metaqhlenq ltllgatgie drlqegvpdt
      901 iatlreagiq lwvltgdkqe tavniahscr llnqtdtvyt intenqetce silncaleel
      961 kqfrelqkpd rklfgfrlps ktpsitseav vpeaglvidg ktlnaifqgk lekkfleltq
     1021 ycrsvlccrs tplqksmivk lvrdklrvmt lsigdgandv smiqaadigi gisgqegmqa
     1081 vmssdfaitr fkhlkklllv hghwcysrla rmvvyylykn vcyvnllfwy qffcgfssst
     1141 midywqmiff nlfftslppl vfgvldkdis aetllalpel yksgqnsecy nlstfwismv
     1201 dafyqslicf fipylaykgs didvftfgtp intislttil lhqamemktw tifhgvvllg
     1261 sflmyflvsl lynatcvicn sptnpywvme gqlsnptfyl vcfltpvval lpryfflslq
     1321 gtcgkslisk aqkidklppd krnleiqswr srqrpapvpe varpthhpvs sitgqdfsas
     1381 tpkssnppkr khveesvlhe qrcgtecmrd dscsgdssaq lssgehllgp nrimaysrgq
     1441 tdmcrcskrs shrrsqsslt i
//
LOCUS       NP_001288069             154 aa            linear   PRI 20-NOV-2025
DEFINITION  iron-sulfur cluster assembly enzyme ISCU isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001288069
VERSION     NP_001288069.1
DBSOURCE    REFSEQ: accession NM_001301140.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Maio,N. and Rouault,T.A.
  TITLE     Iron-sulfur cluster biogenesis in mammalian cells: New insights
            into the molecular mechanisms of cluster delivery
  JOURNAL   Biochim Biophys Acta 1853 (6), 1493-1512 (2015)
   PUBMED   25245479
  REMARK    Review article
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Crooks,D.R., Jeong,S.Y., Tong,W.H., Ghosh,M.C., Olivierre,H.,
            Haller,R.G. and Rouault,T.A.
  TITLE     Tissue specificity of a human mitochondrial disease:
            differentiation-enhanced mis-splicing of the Fe-S scaffold gene
            ISCU renders patient cells more sensitive to oxidative stress in
            ISCU myopathy
  JOURNAL   J Biol Chem 287 (48), 40119-40130 (2012)
   PUBMED   23035118
  REMARK    GeneRIF: ISCU protein deficiency in patients results from
            muscle-specific mis-splicing and oxidative stress.
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Nordin,A., Larsson,E., Thornell,L.E. and Holmberg,M.
  TITLE     Tissue-specific splicing of ISCU results in a skeletal muscle
            phenotype in myopathy with lactic acidosis, while complete loss of
            ISCU results in early embryonic death in mice
  JOURNAL   Hum Genet 129 (4), 371-378 (2011)
   PUBMED   21165651
  REMARK    GeneRIF: Data show that the highest level of incorrectly spliced
            ISCU mRNA was found in skeletal muscle.
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Sanaker,P.S., Toompuu,M., Hogan,V.E., He,L., Tzoulis,C.,
            Chrzanowska-Lightowlers,Z.M., Taylor,R.W. and Bindoff,L.A.
  TITLE     Differences in RNA processing underlie the tissue specific
            phenotype of ISCU myopathy
  JOURNAL   Biochim Biophys Acta 1802 (6), 539-544 (2010)
   PUBMED   20206689
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Olsson,A., Lind,L., Thornell,L.E. and Holmberg,M.
  TITLE     Myopathy with lactic acidosis is linked to chromosome 12q23.3-24.11
            and caused by an intron mutation in the ISCU gene resulting in a
            splicing defect
  JOURNAL   Hum Mol Genet 17 (11), 1666-1672 (2008)
   PUBMED   18296749
  REMARK    GeneRIF: Intron mutation in the ISCU gene, leading to incorrectly
            spliced mRNA, is the cause of myopathy with lactic acidosis in this
            family.
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Mochel,F., Knight,M.A., Tong,W.H., Hernandez,D., Ayyad,K.,
            Taivassalo,T., Andersen,P.M., Singleton,A., Rouault,T.A.,
            Fischbeck,K.H. and Haller,R.G.
  TITLE     Splice mutation in the iron-sulfur cluster scaffold protein ISCU
            causes myopathy with exercise intolerance
  JOURNAL   Am J Hum Genet 82 (3), 652-660 (2008)
   PUBMED   18304497
  REMARK    GeneRIF: Gene ISCU was identified as a candidate within a region of
            shared homozygosity among patients with myopathy with severe
            exercise intolerance and myoglobinuria.
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Tong,W.H. and Rouault,T.
  TITLE     Distinct iron-sulfur cluster assembly complexes exist in the
            cytosol and mitochondria of human cells
  JOURNAL   EMBO J 19 (21), 5692-5700 (2000)
   PUBMED   11060020
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Hwang,D.M., Dempsey,A., Tan,K.T. and Liew,C.C.
  TITLE     A modular domain of NifU, a nitrogen fixation cluster protein, is
            highly conserved in evolution
  JOURNAL   J Mol Evol 43 (5), 536-540 (1996)
   PUBMED   8875867
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Mochel,F. and Haller,R.G.
  TITLE     Myopathy with Deficiency of ISCU - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301757
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK057251.1, BG702203.1 and
            BQ020993.1.
            
            Summary: This gene encodes a component of the iron-sulfur (Fe-S)
            cluster scaffold. Fe-S clusters are cofactors that play a role in
            the function of a diverse set of enzymes, including those that
            regulate metabolism, iron homeostasis, and oxidative stress
            response. Alternative splicing results in transcript variants
            encoding different protein isoforms that localize either to the
            cytosol or to the mitochondrion. Mutations in this gene have been
            found in patients with hereditary myopathy with lactic acidosis. A
            disease-associated mutation in an intron may activate a cryptic
            splice site, resulting in the production of a splice variant
            encoding a putatively non-functional protein. A pseudogene of this
            gene is present on chromosome 1. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (3) contains an alternate exon in
            the 3' region, resulting in a different 3' coding region and 3'
            UTR, compared to variant 2. Variants 3 and 5 encode the same
            protein (isoform 3), which has a distinct, shorter C-terminus,
            compared to isoform 2. Isoform 3 may not be stable (PMID:23035118).
            This variant may be preferentially produced in individuals
            containing an alternate intronic C vs G (rs767000507), which
            activates a cryptic splice acceptor site. The alternate C allele is
            associated with myopathy (PMIDs 18296749, 18304497).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.373269.1, BG702203.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..154
                     /product="iron-sulfur cluster assembly enzyme ISCU isoform
                     3 precursor"
                     /note="iron-sulfur cluster assembly enzyme ISCU,
                     mitochondrial; nifU-like N-terminal domain-containing
                     protein; IscU iron-sulfur cluster scaffold homolog"
                     /calculated_mol_wt=12942
     transit_peptide 1..34
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9H1K1.2)"
                     /calculated_mol_wt=3631
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:23508953; propagated from
                     UniProtKB/Swiss-Prot (Q9H1K1.2)"
     Site            order(34..37,40..41,69..70,95,97,134..135,137..138)
                     /site_type="other"
                     /note="trimerization site [polypeptide binding]"
                     /db_xref="CDD:143480"
     Region          35..139
                     /region_name="IscU_like"
                     /note="Iron-sulfur cluster scaffold-like proteins;
                     cl00528"
                     /db_xref="CDD:444957"
     Site            35
                     /site_type="other"
                     /note="Mediates ISCU dimerization and de novo [2Fe-2S]
                     cluster assembly. /evidence=ECO:0000269|PubMed:34824239;
                     propagated from UniProtKB/Swiss-Prot (Q9H1K1.2)"
     Site            order(69,95,138)
                     /site_type="active"
                     /db_xref="CDD:143480"
     CDS             1..154
                     /gene="ISCU"
                     /gene_synonym="2310020H20Rik; HML; hnifU; ISU2; NIFU;
                     NIFUN"
                     /coded_by="NM_001301140.1:1161..1625"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS76597.1"
                     /db_xref="GeneID:23479"
                     /db_xref="HGNC:HGNC:29882"
                     /db_xref="MIM:611911"
ORIGIN      
        1 maaagafrlr raasalllrs prlparelsa parlyhkkvv dhyenprnvg sldktsknvg
       61 tglvgapacg dvmklqiqvd ekgkivdarf ktfgcgsaia ssslatewvk gktveealti
      121 kntdiakelc lppvklhcsk svlfpaeekt qlsp
//
LOCUS       NP_001307678             555 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-T2 isoform e [Homo sapiens].
ACCESSION   NP_001307678 XP_011510435
VERSION     NP_001307678.1
DBSOURCE    REFSEQ: accession NM_001320749.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 555)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 555)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 555)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 555)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 555)
  AUTHORS   Wang,F., Zhao,Q.H., Liu,J.Z. and Kong,D.L.
  TITLE     MiRNA-188-5p alleviates the progression of osteosarcoma via target
            degrading CCNT2
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (1), 29-35 (2020)
   PUBMED   31957815
  REMARK    GeneRIF: MiRNA-188-5p alleviates the progression of osteosarcoma
            via target degrading CCNT2.
REFERENCE   6  (residues 1 to 555)
  AUTHORS   Napolitano,G., Licciardo,P., Gallo,P., Majello,B., Giordano,A. and
            Lania,L.
  TITLE     The CDK9-associated cyclins T1 and T2 exert opposite effects on
            HIV-1 Tat activity
  JOURNAL   AIDS 13 (12), 1453-1459 (1999)
   PUBMED   10465067
REFERENCE   7  (residues 1 to 555)
  AUTHORS   Bieniasz,P.D., Grdina,T.A., Bogerd,H.P. and Cullen,B.R.
  TITLE     Analysis of the effect of natural sequence variation in Tat and in
            cyclin T on the formation and RNA binding properties of Tat-cyclin
            T complexes
  JOURNAL   J Virol 73 (7), 5777-5786 (1999)
   PUBMED   10364329
REFERENCE   8  (residues 1 to 555)
  AUTHORS   Kwak,Y.T., Ivanov,D., Guo,J., Nee,E. and Gaynor,R.B.
  TITLE     Role of the human and murine cyclin T proteins in regulating HIV-1
            tat-activation
  JOURNAL   J Mol Biol 288 (1), 57-69 (1999)
   PUBMED   10329126
REFERENCE   9  (residues 1 to 555)
  AUTHORS   Wimmer,J., Fujinaga,K., Taube,R., Cujec,T.P., Zhu,Y., Peng,J.,
            Price,D.H. and Peterlin,B.M.
  TITLE     Interactions between Tat and TAR and human immunodeficiency virus
            replication are facilitated by human cyclin T1 but not cyclins T2a
            or T2b
  JOURNAL   Virology 255 (1), 182-189 (1999)
   PUBMED   10049833
REFERENCE   10 (residues 1 to 555)
  AUTHORS   Peng,J., Zhu,Y., Milton,J.T. and Price,D.H.
  TITLE     Identification of multiple cyclin subunits of human P-TEFb
  JOURNAL   Genes Dev 12 (5), 755-762 (1998)
   PUBMED   9499409
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294889.1 and AC016725.5.
            
            On Mar 4, 2016 this sequence version replaced XP_011510435.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin and its kinase partner CDK9 were found to be subunits of the
            transcription elongation factor p-TEFb. The p-TEFb complex
            containing this cyclin was reported to interact with, and act as a
            negative regulator of human immunodeficiency virus type 1 (HIV-1)
            Tat protein. A pseudogene of this gene is found on chromosome 1.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (e) contains an alternate internal
            exon and an alternate internal segment in the 3' end compared to
            variant a. The resulting isoform (e) is shorter at the N-terminus
            and has a longer and distinct C-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.18845.1,
                                           SRR1803611.34108.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..555
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.3"
     Protein         1..555
                     /product="cyclin-T2 isoform e"
                     /note="cyclin T2a; cyclin T2b; SDS-stable vimentin-bound
                     DNA fragment HEF42VIM22; subunit of positive elongation
                     transcription factor b"
                     /calculated_mol_wt=60907
     Region          <1..88
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          121..>252
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     CDS             1..555
                     /gene="CCNT2"
                     /gene_synonym="CYCT2"
                     /coded_by="NM_001320749.2:646..2313"
                     /note="isoform e is encoded by transcript variant e"
                     /db_xref="GeneID:905"
                     /db_xref="HGNC:HGNC:1600"
                     /db_xref="MIM:603862"
ORIGIN      
        1 matnslhltt fclqykptvi acvcihlack wsnweipvst dgkhwweyvd ptvtlellde
       61 ltheflqile ktpnrlkkir nwranqaark pkvdgqvset pllgsslvqn silvdsvtgv
      121 ptnpsfqkps tsafpapvpl nsgnisvqds htsdnlsmla tgmpstsygl sshqewpqhq
      181 dsarteqlys qkqetslsgs qyninfqqgp sislhsglhh rpdkisdhss vkqeythkag
      241 sskhhgpist tpgiipqkms ldkyrekrkl etldldvrdh yiaaqveqqh kqgqsqaass
      301 ssvtspikmk ipiantekym adkkeksgsl klripipptd ksaskeelkm kikvssserh
      361 sssdegsgks khssphisrd hkekhkehps srhhtsshkh shshsgsssg gskhsadgip
      421 ptvlrspvgl ssdgisssss ssrkrlhvnd ashnhhskms ksskssgsss sssssvkqyi
      481 sshnsvfnhp lpppppvtyq vgyghlstlv kldkkpvetn gpdanheyst ssqhmdykdt
      541 fdmldsllsa qgmnm
//
LOCUS       NP_000475                770 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform a precursor [Homo sapiens].
ACCESSION   NP_000475
VERSION     NP_000475.1
DBSOURCE    REFSEQ: accession NM_000484.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI559391.1, AK312326.1,
            BC065529.1 and BM876312.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a, also known as PreA4
            770).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.19016.1,
                                           SRR14038194.1684132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000346798.8/
                                                  ENSP00000284981.4
            Protein has antimicrobial activity :: PMID: 20209079
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..770
                     /product="amyloid-beta precursor protein isoform a
                     precursor"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=85181
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1781
     mat_peptide     18..770
                     /product="amyloid-beta precursor protein isoform a"
                     /calculated_mol_wt=85181
     mat_peptide     18..687
                     /product="Soluble APP-alpha. /id=PRO_0000000089"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=75989
     mat_peptide     18..671
                     /product="Soluble APP-beta. /id=PRO_0000000090"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=74052
     mat_peptide     18..286
                     /product="N-APP. /id=PRO_0000381966"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=30196
     Region          24..188
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          28..123
                     /region_name="GFLD subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Region          131..189
                     /region_name="CuBD subdomain.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            170
                     /site_type="other"
                     /note="Required for Cu(2+) reduction.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01217; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Region          194..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            197..198
                     /site_type="cleavage"
                     /note="Cleavage, by caspases.
                     /evidence=ECO:0000269|PubMed:10319819; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:8999878; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:8999878; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            217
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Site            219..220
                     /site_type="cleavage"
                     /note="Cleavage, by caspases.
                     /evidence=ECO:0000269|PubMed:10319819; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            262
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Region          294..341
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(297..305,320,322,324)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Site            301..302
                     /site_type="other"
                     /note="Reactive bond; propagated from UniProtKB/Swiss-Prot
                     (P05067.3)"
     Site            336
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P05067.3)"
     Region          344..365
                     /region_name="OX-2. /evidence=ECO:0000269|PubMed:2649245"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Region          366..548
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     Region          391..423
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Region          491..522
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Region          523..540
                     /region_name="Collagen-binding.
                     /evidence=ECO:0000269|PubMed:8576160"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            542
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            571
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            633
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:21712440,
                     ECO:0000269|PubMed:22576872; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            651
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:21712440,
                     ECO:0000269|PubMed:22576872; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            652
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:21712440,
                     ECO:0000269|PubMed:22576872; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            656
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine, in
                     L-APP isoforms. /evidence=ECO:0000269|PubMed:21712440;
                     propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            659
                     /site_type="glycosylation"
                     /note="O-linked (HexNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:22576872; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            663
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine, partial.
                     /evidence=ECO:0000269|PubMed:22576872,
                     ECO:0000305|PubMed:21712440; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            667
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) serine, partial.
                     /evidence=ECO:0000269|PubMed:22576872,
                     ECO:0000305|PubMed:21712440; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            671..672
                     /site_type="cleavage"
                     /note="Cleavage, by beta-secretase.
                     /evidence=ECO:0000305|PubMed:11851430; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     672..770
                     /product="C99. /id=PRO_0000000091"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=11147
     mat_peptide     672..713
                     /product="amyloid-beta precursor protein isoform a"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /exception="alternative processing"
                     /calculated_mol_wt=4514
     mat_peptide     672..711
                     /product="amyloid-beta precursor protein isoform a"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /calculated_mol_wt=4330
     Site            672..673
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-6, when associated with
                     variant 670-N-L-671; propagated from UniProtKB/Swiss-Prot
                     (P05067.3)"
     Site            678..679
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000269|PubMed:11604391,
                     ECO:0000269|PubMed:16154999; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            681
                     /site_type="glycosylation"
                     /note="O-linked (HexNAc...) tyrosine, partial.
                     /evidence=ECO:0000269|PubMed:22576872; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            687..688
                     /site_type="cleavage"
                     /note="Cleavage, by alpha-secretase.
                     /evidence=ECO:0000305|PubMed:11851430; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     688..770
                     /product="C83. /id=PRO_0000000094"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=9210
     mat_peptide     688..713
                     /product="P3(42). /id=PRO_0000000095"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=2577
     mat_peptide     688..711
                     /product="P3(40). /id=PRO_0000000096"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=2393
     Site            690..691
                     /site_type="cleavage"
                     /note="Cleavage, by theta-secretase.
                     /evidence=ECO:0000269|PubMed:16816112; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     691..770
                     /product="C80. /id=PRO_0000384574"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=8850
     Region          693..767
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Region          695..722
                     /region_name="Interaction with PSEN1.
                     /evidence=ECO:0000269|PubMed:30630874"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            702..722
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            704
                     /site_type="other"
                     /note="Implicated in free radical propagation.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            order(706..707,709..710,712..718,720..725)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     Site            706
                     /site_type="other"
                     /note="Susceptible to oxidation.
                     /evidence=ECO:0000269|PubMed:10535332; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            711..712
                     /site_type="cleavage"
                     /note="Cleavage, by gamma-secretase, site 1.
                     /evidence=ECO:0000305|PubMed:11851430; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     712..770
                     /product="Gamma-secretase C-terminal fragment 59.
                     /id=PRO_0000000097"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=6835
     Site            713..714
                     /site_type="cleavage"
                     /note="Cleavage, by gamma-secretase, site 2.
                     /evidence=ECO:0000305|PubMed:11851430; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     714..770
                     /product="Gamma-secretase C-terminal fragment 57.
                     /id=PRO_0000000098"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=6651
     Site            720..721
                     /site_type="cleavage"
                     /note="Cleavage, by gamma-secretase, site 3.
                     /evidence=ECO:0000269|PubMed:11851430,
                     ECO:0000305|PubMed:30630874; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     721..770
                     /product="Gamma-secretase C-terminal fragment 50.
                     /evidence=ECO:0000250. /id=PRO_0000000099"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=5911
     Region          724..734
                     /region_name="Basolateral sorting signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P08592; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by APP-kinase I.
                     /evidence=ECO:0000250|UniProtKB:P08592; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     Region          732..751
                     /region_name="Interaction with G(o)-alpha"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            739..740
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-6, caspase-8 or caspase-9.
                     /evidence=ECO:0000269|PubMed:10319819; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     mat_peptide     740..770
                     /product="C31. /id=PRO_0000000100"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
                     /calculated_mol_wt=3717
     Site            743
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK5 and MAPK10.
                     /evidence=ECO:0000269|PubMed:28720718,
                     ECO:0000269|PubMed:8131745, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Region          756..770
                     /region_name="Required for the interaction with KIF5B and
                     for anterograde transport in axons.
                     /evidence=ECO:0000269|PubMed:17062754"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Region          757..762
                     /region_name="YENPXY motif, contains endocytosis signal.
                     /evidence=ECO:0000269|PubMed:10383380"
                     /note="propagated from UniProtKB/Swiss-Prot (P05067.3)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11877420; propagated from
                     UniProtKB/Swiss-Prot (P05067.3)"
     CDS             1..770
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_000484.4:151..2463"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS13576.1"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ptdgnaglla epqiamfcgr lnmhmnvqng kwdsdpsgtk
       61 tcidtkegil qycqevypel qitnvveanq pvtiqnwckr grkqckthph fvipyrclvg
      121 efvsdallvp dkckflhqer mdvcethlhw htvaketcse kstnlhdygm llpcgidkfr
      181 gvefvccpla eesdnvdsad aeeddsdvww ggadtdyadg sedkvvevae eeevaeveee
      241 eadddedded gdeveeeaee pyeeatertt siattttttt esveevvrev cseqaetgpc
      301 ramisrwyfd vtegkcapff yggcggnrnn fdteeycmav cgsamsqsll kttqeplard
      361 pvklpttaas tpdavdkyle tpgdenehah fqkakerlea khrermsqvm reweeaerqa
      421 knlpkadkka viqhfqekve sleqeaaner qqlvethmar veamlndrrr lalenyital
      481 qavpprprhv fnmlkkyvra eqkdrqhtlk hfehvrmvdp kkaaqirsqv mthlrviyer
      541 mnqslsllyn vpavaeeiqd evdellqkeq nysddvlanm iseprisygn dalmpsltet
      601 kttvellpvn gefslddlqp whsfgadsvp antenevepv darpaadrgl ttrpgsgltn
      661 ikteeisevk mdaefrhdsg yevhhqklvf faedvgsnkg aiiglmvggv viatvivitl
      721 vmlkkkqyts ihhgvvevda avtpeerhls kmqqngyenp tykffeqmqn
//
LOCUS       NP_061158                253 aa            linear   PRI 20-NOV-2025
DEFINITION  bridging integrator 3 isoform 1 [Homo sapiens].
ACCESSION   NP_061158
VERSION     NP_061158.1
DBSOURCE    REFSEQ: accession NM_018688.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Thalappilly,S., Suliman,M., Gayet,O., Soubeyran,P., Hermant,A.,
            Lecine,P., Iovanna,J.L. and Dusetti,N.J.
  TITLE     Identification of multi-SH3 domain-containing protein interactome
            in pancreatic cancer: a yeast two-hybrid approach
  JOURNAL   Proteomics 8 (15), 3071-3081 (2008)
   PUBMED   18654987
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Ren,G., Vajjhala,P., Lee,J.S., Winsor,B. and Munn,A.L.
  TITLE     The BAR domain proteins: molding membranes in fission, fusion, and
            phagy
  JOURNAL   Microbiol Mol Biol Rev 70 (1), 37-120 (2006)
   PUBMED   16524918
  REMARK    Review article
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Habermann,B.
  TITLE     The BAR-domain family of proteins: a case of bending and binding?
  JOURNAL   EMBO Rep 5 (3), 250-255 (2004)
   PUBMED   14993925
  REMARK    Review article
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Routhier,E.L., Burn,T.C., Abbaszade,I., Summers,M., Albright,C.F.
            and Prendergast,G.C.
  TITLE     Human BIN3 complements the F-actin localization defects caused by
            loss of Hob3p, the fission yeast homolog of Rvs161p
  JOURNAL   J Biol Chem 276 (24), 21670-21677 (2001)
   PUBMED   11274158
  REMARK    GeneRIF: BIN3 is a BAR domain adapter protein implicated in actin
            regulation; it is homologous to budding yeast Rvs161 and fission
            yeast Hob3.
            GeneRIF: like RVS161, hob3+ and BIN3 regulate F-actin localization,
            but other roles for these genes have diverged somewhat during
            evolution
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA480525.1, AC105046.10,
            BC009824.2, BM670487.1 and AC037459.16.
            
            Summary: The product of this gene is a member of the BAR domain
            protein family. The encoded protein is comprised solely of a BAR
            domain which is predicted to form coiled-coil structures and
            proposed to mediate dimerization, sense and induce membrane
            curvature, and bind small GTPases. BAR domain proteins have been
            implicated in endocytosis, intracellular transport, and a diverse
            set of other processes. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.81939.1, BC009824.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000276416.11/ ENSP00000276416.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..253
                     /product="bridging integrator 3 isoform 1"
                     /calculated_mol_wt=29534
     Region          12..236
                     /region_name="BAR_Bin3"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Bridging
                     integrator 3; cd07590"
                     /db_xref="CDD:153274"
     Site            order(30,33..34,38,40..41,44..45,47..48,51..52,54..55,
                     58..59,61..62,65,85,88..89,184,187..188,190,195,198..199,
                     201..202,205..206,209..210,212..213,216..217,219..220)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153274"
     Region          220..240
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQY0.1)"
     CDS             1..253
                     /gene="BIN3"
                     /coded_by="NM_018688.6:71..832"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47825.1"
                     /db_xref="GeneID:55909"
                     /db_xref="HGNC:HGNC:1054"
                     /db_xref="MIM:606396"
ORIGIN      
        1 mswipfkigq pkkqivpktv erdfereygk lqqleeqtrr lqkdmkkstd adlamsksav
       61 kisldllsnp lceqdqdlln mvtaldtamk rmdafnqekv nqiqktviep lkkfgsvfps
      121 lnmavkrreq alqdyrrlqa kvekyeekek tgpvlaklhq areelrpvre dfeaknrqll
      181 eemprfygsr ldyfqpsfes liraqvvyys emhkifgdls hqldqpghsd eqrereneak
      241 lselralsiv add
//
LOCUS       NP_000985                135 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL32 [Homo sapiens].
ACCESSION   NP_000985
VERSION     NP_000985.1
DBSOURCE    REFSEQ: accession NM_000994.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Xu,L., Wang,L., Jiang,C., Zhu,Q., Chen,R., Wang,J. and Wang,S.
  TITLE     Biological effect of ribosomal protein L32 on human breast cancer
            cell behavior
  JOURNAL   Mol Med Rep 22 (3), 2478-2486 (2020)
   PUBMED   32705264
  REMARK    GeneRIF: Biological effect of ribosomal protein L32 on human breast
            cancer cell behavior.
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Vorobieva,N.V., Filipenko,M.L., Karpova,G.G., Mertvetsov,N.P. and
            Graphodatsky,A.S.
  TITLE     Assignment of the L32 ribosomal protein gene (RPL32) to human
            chromosome 3q13.3-->q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 190-191 (1997)
   PUBMED   9284913
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Young,J.A. and Trowsdale,J.
  TITLE     A processed pseudogene in an intron of the HLA-DP beta 1 chain gene
            is a member of the ribosomal protein L32 gene family
  JOURNAL   Nucleic Acids Res 13 (24), 8883-8891 (1985)
   PUBMED   3866218
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from CF124158.1, AC034198.7 and CA436299.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L32E family of ribosomal proteins. It is located in the
            cytoplasm. Although some studies have mapped this gene to
            3q13.3-q21, it is believed to map to 3p25-p24. As is typical for
            genes encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome.
            Alternatively spliced transcript variants encoding the same protein
            have been observed for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX419829.2, BX432517.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000429711.7/ ENSP00000416429.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.2"
     Protein         1..135
                     /product="large ribosomal subunit protein eL32"
                     /note="60S ribosomal protein L32"
                     /calculated_mol_wt=15729
     Region          17..124
                     /region_name="Ribosomal_L32e"
                     /note="Ribosomal protein L32; pfam01655"
                     /db_xref="CDD:460283"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62910.2)"
     CDS             1..135
                     /gene="RPL32"
                     /gene_synonym="eL32; L32; PP9932"
                     /coded_by="NM_000994.4:78..485"
                     /db_xref="CCDS:CCDS2614.1"
                     /db_xref="GeneID:6161"
                     /db_xref="HGNC:HGNC:10336"
ORIGIN      
        1 maalrplvkp kivkkrtkkf irhqsdryvk ikrnwrkprg idnrvrrrfk gqilmpnigy
       61 gsnkktkhml psgfrkflvh nvkelevllm cnksycaeia hnvssknrka iveraaqlai
      121 rvtnpnarlr seene
//
LOCUS       NP_001309432             370 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-1A adrenergic receptor isoform 6 [Homo sapiens].
ACCESSION   NP_001309432
VERSION     NP_001309432.1
DBSOURCE    REFSEQ: accession NM_001322503.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Ren,C., Cui,L., Li,R., Song,X., Li,J., Xi,Q., Zhang,Z. and Zhao,L.
  TITLE     Hsa_circ_0080608 Attenuates Lung Cancer Progression by Functioning
            as a Competitive Endogenous RNA to Regulate the miR-661/ADRA1A
            Pathway
  JOURNAL   Horm Metab Res 55 (12), 876-884 (2023)
   PUBMED   37820700
  REMARK    GeneRIF: Hsa_circ_0080608 Attenuates Lung Cancer Progression by
            Functioning as a Competitive Endogenous RNA to Regulate the
            miR-661/ADRA1A Pathway.
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Su,M., Wang,J., Xiang,G., Do,H.N., Levitz,J., Miao,Y. and
            Huang,X.Y.
  TITLE     Structural basis of agonist specificity of alpha1A-adrenergic
            receptor
  JOURNAL   Nat Commun 14 (1), 4819 (2023)
   PUBMED   37563160
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Chechekhin,V., Ivanova,A., Kulebyakin,K., Sysoeva,V., Naida,D.,
            Arbatsky,M., Basalova,N., Karagyaur,M., Skryabina,M., Efimenko,A.,
            Grigorieva,O., Kalinina,N., Tkachuk,V. and Tyurin-Kuzmin,P.
  TITLE     Alpha1A- and Beta3-Adrenoceptors Interplay in Adipose Multipotent
            Mesenchymal Stromal Cells: A Novel Mechanism of Obesity-Driven
            Hypertension
  JOURNAL   Cells 12 (4), 585 (2023)
   PUBMED   36831252
  REMARK    GeneRIF: Alpha1A- and Beta3-Adrenoceptors Interplay in Adipose
            Multipotent Mesenchymal Stromal Cells: A Novel Mechanism of
            Obesity-Driven Hypertension.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Zhang,J., Fu,X., Lu,Y., Cheng,C., Wang,K., Zhu,Y. and Xie,Q.
  TITLE     Hypermethylation in the promoter region of the ADRA1A gene is
            associated with opioid use disorder in Han Chinese
  JOURNAL   Brain Res 1793, 148050 (2022)
   PUBMED   35964682
  REMARK    GeneRIF: Hypermethylation in the promoter region of the ADRA1A gene
            is associated with opioid use disorder in Han Chinese.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Baranova,T., Podyacheva,E., Zemlyanukhina,T., Berlov,D.,
            Danilova,M., Glotov,O. and Glotov,A.
  TITLE     Vascular Reactions of the Diving Reflex in Men and Women Carrying
            Different ADRA1A Genotypes
  JOURNAL   Int J Mol Sci 23 (16), 9433 (2022)
   PUBMED   36012699
  REMARK    GeneRIF: Vascular Reactions of the Diving Reflex in Men and Women
            Carrying Different ADRA1A Genotypes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Coge,F., Guenin,S.P., Renouard-Try,A., Rique,H., Ouvry,C.,
            Fabry,N., Beauverger,P., Nicolas,J.P., Galizzi,J.P., Boutin,J.A.
            and Canet,E.
  TITLE     Truncated isoforms inhibit [3H]prazosin binding and cellular
            trafficking of native human alpha1A-adrenoceptors
  JOURNAL   Biochem J 343 Pt 1 (Pt 1), 231-239 (1999)
   PUBMED   10493934
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Hirasawa,A., Shibata,K., Horie,K., Takei,Y., Obika,K., Tanaka,T.,
            Muramoto,N., Takagaki,K., Yano,J. and Tsujimoto,G.
  TITLE     Cloning, functional expression and tissue distribution of human
            alpha 1c-adrenoceptor splice variants
  JOURNAL   FEBS Lett 363 (3), 256-260 (1995)
   PUBMED   7737411
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Hoehe,M.R., Berrettini,W.H., Schwinn,D.A. and Hsieh,W.T.
  TITLE     A two-allele PstI RFLP for the alpha-1C adrenergic receptor gene
            (ADRA1C)
  JOURNAL   Hum Mol Genet 1 (5), 349 (1992)
   PUBMED   1363873
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Schwinn,D.A., Lomasney,J.W., Lorenz,W., Szklut,P.J., Fremeau,R.T.
            Jr., Yang-Feng,T.L., Caron,M.G., Lefkowitz,R.J. and Cotecchia,S.
  TITLE     Molecular cloning and expression of the cDNA for a novel alpha
            1-adrenergic receptor subtype
  JOURNAL   J Biol Chem 265 (14), 8183-8189 (1990)
   PUBMED   1970822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289548.1, AC022839.8,
            AK311558.1, D32202.1 and AC015564.13.
            
            Summary: Alpha-1-adrenergic receptors (alpha-1-ARs) are members of
            the G protein-coupled receptor superfamily. They activate mitogenic
            responses and regulate growth and proliferation of many cells.
            There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of
            which signal through the Gq/11 family of G-proteins and different
            subtypes show different patterns of activation. This gene encodes
            alpha-1A-adrenergic receptor. Alternative splicing of this gene
            generates four transcript variants, which encode four different
            isoforms with distinct C-termini but having similar ligand binding
            properties. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY491776.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..370
                     /product="alpha-1A adrenergic receptor isoform 6"
                     /note="G protein coupled receptor; alpha-1A adrenoceptor;
                     alpha-1A adrenoreceptor; alpha-1C adrenergic receptor"
                     /calculated_mol_wt=40594
     Site            7
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35348.2)"
     Site            13
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35348.2)"
     Site            22
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35348.2)"
     Region          27..294
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Site            28..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Region          29..53
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320448"
     Region          62..84
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320448"
     Site            65..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Region          100..122
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320448"
     Site            100..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Site            144..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Region          145..161
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320448"
     Region          182..205
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320448"
     Site            182..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P35348.2)"
     Region          271..293
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320448"
     CDS             1..370
                     /gene="ADRA1A"
                     /gene_synonym="ADRA1C; ADRA1L1; ALPHA1AAR"
                     /coded_by="NM_001322503.1:687..1799"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:148"
                     /db_xref="HGNC:HGNC:277"
                     /db_xref="MIM:104221"
ORIGIN      
        1 mvflsgnasd ssnctqppap vniskaillg vilgglilfg vlgnilvils vachrhlhsv
       61 thyyivnlav adllltstvl pfsaifevlg ywafgrvfcn iwaavdvlcc tasimglcii
      121 sidryigvsy plryptivtq rrglmallcv walslvisig plfgwrqpap edeticqine
      181 epgyvlfsal gsfylplaii lvmycrvyvv akresrglks glktdksdse qvtlrihrkn
      241 apaggsgmas aktkthfsvr llkfsrekka aktlgivvgc fvlcwlpffl vmpidevslc
      301 hqagvqwhdl gslqppppgf krfsclslps swdyrdvppg rrhqaqlifv flvetgfhhv
      361 gqddldllts
//
LOCUS       NP_065990                593 aa            linear   PRI 20-NOV-2025
DEFINITION  copine-5 isoform a [Homo sapiens].
ACCESSION   NP_065990
VERSION     NP_065990.1
DBSOURCE    REFSEQ: accession NM_020939.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 593)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 593)
  AUTHORS   Zhu,P., Qian,T., Si,C., Liu,Y., Cui,L., Huang,W., Fu,L., Deng,C.
            and Zeng,T.
  TITLE     High expression of CPNE5 and CPNE9 predicts positive prognosis in
            multiple myeloma
  JOURNAL   Cancer Biomark 31 (1), 77-85 (2021)
   PUBMED   33780365
  REMARK    GeneRIF: High expression of CPNE5 and CPNE9 predicts positive
            prognosis in multiple myeloma.
REFERENCE   3  (residues 1 to 593)
  AUTHORS   Umeda,S., Kanda,M., Koike,M., Tanaka,H., Miwa,T., Tanaka,C.,
            Kobayashi,D., Suenaga,M., Hayashi,M., Yamada,S., Nakayama,G. and
            Kodera,Y.
  TITLE     Copine 5 expression predicts prognosis following curative resection
            of esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 40 (6), 3772-3780 (2018)
   PUBMED   30272363
  REMARK    GeneRIF: Data revealed that CPNE5 mRNA expression was significantly
            lower in ESCC tissues and cell lines and correlated with
            significantly shorter overall survival. Multivariable analysis
            identified low CPNE5 expression to be an independent prognostic
            factor of OS. Analysis of recurrence patterns revealed that
            significantly more patients with local recurrence expressed lower
            levels of CPNE5 mRNA.
REFERENCE   4  (residues 1 to 593)
  AUTHORS   Wang,K.S., Zuo,L., Pan,Y., Xie,C. and Luo,X.
  TITLE     Genetic variants in the CPNE5 gene are associated with alcohol
            dependence and obesity in Caucasian populations
  JOURNAL   J Psychiatr Res 71, 1-7 (2015)
   PUBMED   26522866
  REMARK    GeneRIF: Results provide the first evidence of genetic variants in
            the CPNE5 gene influencing both alcohol dependence and obesity
REFERENCE   5  (residues 1 to 593)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 593)
  AUTHORS   den Hoed,M., Eijgelsheim,M., Esko,T., Brundel,B.J., Peal,D.S.,
            Evans,D.M., Nolte,I.M., Segre,A.V., Holm,H., Handsaker,R.E.,
            Westra,H.J., Johnson,T., Isaacs,A., Yang,J., Lundby,A., Zhao,J.H.,
            Kim,Y.J., Go,M.J., Almgren,P., Bochud,M., Boucher,G.,
            Cornelis,M.C., Gudbjartsson,D., Hadley,D., van der Harst,P.,
            Hayward,C., den Heijer,M., Igl,W., Jackson,A.U., Kutalik,Z.,
            Luan,J., Kemp,J.P., Kristiansson,K., Ladenvall,C., Lorentzon,M.,
            Montasser,M.E., Njajou,O.T., O'Reilly,P.F., Padmanabhan,S., St
            Pourcain,B., Rankinen,T., Salo,P., Tanaka,T., Timpson,N.J.,
            Vitart,V., Waite,L., Wheeler,W., Zhang,W., Draisma,H.H.,
            Feitosa,M.F., Kerr,K.F., Lind,P.A., Mihailov,E., Onland-Moret,N.C.,
            Song,C., Weedon,M.N., Xie,W., Yengo,L., Absher,D., Albert,C.M.,
            Alonso,A., Arking,D.E., de Bakker,P.I., Balkau,B., Barlassina,C.,
            Benaglio,P., Bis,J.C., Bouatia-Naji,N., Brage,S., Chanock,S.J.,
            Chines,P.S., Chung,M., Darbar,D., Dina,C., Dorr,M., Elliott,P.,
            Felix,S.B., Fischer,K., Fuchsberger,C., de Geus,E.J., Goyette,P.,
            Gudnason,V., Harris,T.B., Hartikainen,A.L., Havulinna,A.S.,
            Heckbert,S.R., Hicks,A.A., Hofman,A., Holewijn,S.,
            Hoogstra-Berends,F., Hottenga,J.J., Jensen,M.K., Johansson,A.,
            Junttila,J., Kaab,S., Kanon,B., Ketkar,S., Khaw,K.T., Knowles,J.W.,
            Kooner,A.S., Kors,J.A., Kumari,M., Milani,L., Laiho,P.,
            Lakatta,E.G., Langenberg,C., Leusink,M., Liu,Y., Luben,R.N.,
            Lunetta,K.L., Lynch,S.N., Markus,M.R., Marques-Vidal,P., Mateo
            Leach,I., McArdle,W.L., McCarroll,S.A., Medland,S.E., Miller,K.A.,
            Montgomery,G.W., Morrison,A.C., Muller-Nurasyid,M., Navarro,P.,
            Nelis,M., O'Connell,J.R., O'Donnell,C.J., Ong,K.K., Newman,A.B.,
            Peters,A., Polasek,O., Pouta,A., Pramstaller,P.P., Psaty,B.M.,
            Rao,D.C., Ring,S.M., Rossin,E.J., Rudan,D., Sanna,S., Scott,R.A.,
            Sehmi,J.S., Sharp,S., Shin,J.T., Singleton,A.B., Smith,A.V.,
            Soranzo,N., Spector,T.D., Stewart,C., Stringham,H.M., Tarasov,K.V.,
            Uitterlinden,A.G., Vandenput,L., Hwang,S.J., Whitfield,J.B.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilson,J.F., Witteman,J.C.,
            Wong,A., Wong,Q., Jamshidi,Y., Zitting,P., Boer,J.M., Boomsma,D.I.,
            Borecki,I.B., van Duijn,C.M., Ekelund,U., Forouhi,N.G., Froguel,P.,
            Hingorani,A., Ingelsson,E., Kivimaki,M., Kronmal,R.A., Kuh,D.,
            Lind,L., Martin,N.G., Oostra,B.A., Pedersen,N.L., Quertermous,T.,
            Rotter,J.I., van der Schouw,Y.T., Verschuren,W.M., Walker,M.,
            Albanes,D., Arnar,D.O., Assimes,T.L., Bandinelli,S., Boehnke,M., de
            Boer,R.A., Bouchard,C., Caulfield,W.L., Chambers,J.C., Curhan,G.,
            Cusi,D., Eriksson,J., Ferrucci,L., van Gilst,W.H., Glorioso,N., de
            Graaf,J., Groop,L., Gyllensten,U., Hsueh,W.C., Hu,F.B.,
            Huikuri,H.V., Hunter,D.J., Iribarren,C., Isomaa,B., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kiemeney,L.A., van der Klauw,M.M.,
            Kooner,J.S., Kraft,P., Iacoviello,L., Lehtimaki,T., Lokki,M.L.,
            Mitchell,B.D., Navis,G., Nieminen,M.S., Ohlsson,C., Poulter,N.R.,
            Qi,L., Raitakari,O.T., Rimm,E.B., Rioux,J.D., Rizzi,F., Rudan,I.,
            Salomaa,V., Sever,P.S., Shields,D.C., Shuldiner,A.R., Sinisalo,J.,
            Stanton,A.V., Stolk,R.P., Strachan,D.P., Tardif,J.C.,
            Thorsteinsdottir,U., Tuomilehto,J., van Veldhuisen,D.J.,
            Virtamo,J., Viikari,J., Vollenweider,P., Waeber,G., Widen,E.,
            Cho,Y.S., Olsen,J.V., Visscher,P.M., Willer,C., Franke,L.,
            Erdmann,J., Thompson,J.R., Pfeufer,A., Sotoodehnia,N.,
            Newton-Cheh,C., Ellinor,P.T., Stricker,B.H., Metspalu,A.,
            Perola,M., Beckmann,J.S., Smith,G.D., Stefansson,K., Wareham,N.J.,
            Munroe,P.B., Sibon,O.C., Milan,D.J., Snieder,H., Samani,N.J. and
            Loos,R.J.
  CONSRTM   Global BPgen Consortium; CARDIoGRAM Consortium; PR GWAS Consortium;
            QRS GWAS Consortium; QT-IGC Consortium; CHARGE-AF Consortium
  TITLE     Identification of heart rate-associated loci and their effects on
            cardiac conduction and rhythm disorders
  JOURNAL   Nat Genet 45 (6), 621-631 (2013)
   PUBMED   23583979
REFERENCE   7  (residues 1 to 593)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 593)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 593)
  AUTHORS   Tripodis,N., Mason,R., Humphray,S.J., Davies,A.F., Herberg,J.A.,
            Trowsdale,J., Nizetic,D., Senger,G. and Ragoussis,J.
  TITLE     Physical map of human 6p21.2-6p21.3: region flanking the
            centromeric end of the major histocompatibility complex
  JOURNAL   Genome Res 8 (6), 631-643 (1998)
   PUBMED   9647638
REFERENCE   10 (residues 1 to 593)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA265730.1, DB320492.1,
            AI989513.1, BC053872.1, BC036840.1 and Z85996.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encode a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. More variants may
            exist, but their full-length natures could not be determined.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.869485.1, AB046819.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244751.7/ ENSP00000244751.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..593
                     /product="copine-5 isoform a"
                     /note="copine V"
                     /calculated_mol_wt=65603
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH3.2)"
     Region          23..137
                     /region_name="C2A_Copine"
                     /note="C2 domain first repeat in Copine; cd04048"
                     /db_xref="CDD:176013"
     Site            order(38,44,98,100,110)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176013"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZW4; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH3.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZW4; propagated from
                     UniProtKB/Swiss-Prot (Q9HCH3.2)"
     Region          177..288
                     /region_name="C2B_Copine"
                     /note="C2 domain second repeat in Copine; cd04047"
                     /db_xref="CDD:176012"
     Site            order(192,198,254,256,262)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176012"
     Region          298..554
                     /region_name="vWA_copine_like"
                     /note="VWA Copine: Copines are phospholipid-binding
                     proteins originally identified in paramecium. They are
                     found in human and orthologues have been found in C.
                     elegans and Arabidopsis Thaliana. None have been found in
                     D. Melanogaster or S. Cereviciae; cd01459"
                     /db_xref="CDD:238736"
     Site            order(334,336,338,432,462)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238736"
     Region          562..593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCH3.2)"
     CDS             1..593
                     /gene="CPNE5"
                     /gene_synonym="COPN5; CPN5"
                     /coded_by="NM_020939.2:68..1849"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4825.1"
                     /db_xref="GeneID:57699"
                     /db_xref="HGNC:HGNC:2318"
                     /db_xref="MIM:604209"
ORIGIN      
        1 meqpedmasl sefdslagsi patkveitvs crnlldkdmf sksdplcvmy tqgmenkqwr
       61 efgrtevidn tlnpdfvrkf ivdyffeekq nlrfdlydvd skspdlskhd flgqafctlg
      121 eivgspgsrl ekpltigafs lnsrtgkpmp avsnggvpgk kcgtiilsae elsncrdvat
      181 mqfcankldk kdffgksdpf lvfyrsnedg tftichktev mkntlnpvwq tfsipvralc
      241 ngdydrtikv evydwdrdgs hdfigeftts yrelargqsq fniyevvnpk kkmkkkkyvn
      301 sgtvtllsfa vesectfldy ikggtqinft vaidftasng npsqstslhy mspyqlnaya
      361 laltavgeii qhydsdkmfp algfgaklpp dgrvshefpl ngnqenpscc gidgileayh
      421 rslrtvqlyg ptnfapvvth varnaaavqd gsqysvllii tdgvisdmaq tkeaivnaak
      481 lpmsiiivgv gqaefdamve ldgddvriss rgklaerdiv qfvpfrdyvd rtgnhvlsma
      541 rlardvlaei pdqlvsymka qgirprpppa apthspsqsp artppasplh thi
//
LOCUS       NP_919340                317 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NRDP1 isoform 1 [Homo sapiens].
ACCESSION   NP_919340
VERSION     NP_919340.1
DBSOURCE    REFSEQ: accession NM_194359.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Xiong,S., Li,S., Li,Z., Song,Y., Yang,L., Yang,H., Xiong,J.,
            Pan,W., Guo,J., Fu,B. and Xu,S.
  TITLE     A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C stability
            promotes prostate cancer metastasis by inducing actin remodeling
  JOURNAL   Oncogene 43 (36), 2696-2707 (2024)
   PUBMED   39112516
  REMARK    GeneRIF: A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C
            stability promotes prostate cancer metastasis by inducing actin
            remodeling.
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Li,Q.Q., Guo,M., He,G.H., Xi,K.H., Zhou,M.Y., Shi,R.Y. and
            Chen,G.Q.
  TITLE     VEGF-induced Nrdp1 deficiency in vascular endothelial cells
            promotes cancer metastasis by degrading vascular basement membrane
  JOURNAL   Oncogene 43 (24), 1836-1851 (2024)
   PUBMED   38654108
  REMARK    GeneRIF: VEGF-induced Nrdp1 deficiency in vascular endothelial
            cells promotes cancer metastasis by degrading vascular basement
            membrane.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Zong,C.Y., Ji,Q.Q., Chen,F.F., Yang,J.J., Zhou,H., Zhu,B.F. and
            Zhou,G.X.
  TITLE     Correlation between neuregulin receptor degradation protein-1 and
            Crohn's disease
  JOURNAL   J Physiol Pharmacol 75 (1) (2024)
   PUBMED   38583443
  REMARK    GeneRIF: Correlation between neuregulin receptor degradation
            protein-1 and Crohn's disease.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Zeng,W., Zhu,J.F., Guo,J., Huang,G.J., Ai,L.S., Zeng,Y. and
            Liao,W.J.
  TITLE     m6A-modified circFNDC3B inhibits colorectal cancer stemness and
            metastasis via RNF41-dependent ASB6 degradation
  JOURNAL   Cell Death Dis 13 (11), 1008 (2022)
   PUBMED   36446779
  REMARK    GeneRIF: m[6]A-modified circFNDC3B inhibits colorectal cancer
            stemness and metastasis via RNF41-dependent ASB6 degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Qiu,X.B., Markant,S.L., Yuan,J. and Goldberg,A.L.
  TITLE     Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel
            pathway for triggering apoptosis
  JOURNAL   EMBO J 23 (4), 800-810 (2004)
   PUBMED   14765125
  REMARK    GeneRIF: Nrdp1 can be important in the initiation of apoptosis by
            catalyzing ubiquitination and degradation of BRUCE.
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Qiu,X.B. and Goldberg,A.L.
  TITLE     Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and
            degradation of the epidermal growth factor receptor family member,
            ErbB3
  JOURNAL   Proc Natl Acad Sci U S A 99 (23), 14843-14848 (2002)
   PUBMED   12411582
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):17220.]
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Diamonti,A.J., Guy,P.M., Ivanof,C., Wong,K., Sweeney,C. and
            Carraway,K.L. 3rd.
  TITLE     An RBCC protein implicated in maintenance of steady-state
            neuregulin receptor levels
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2866-2871 (2002)
   PUBMED   11867753
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Abdullah,J.M., Li,X., Nachtman,R.G. and Jurecic,R.
  TITLE     FLRF, a novel evolutionarily conserved RING finger gene, is
            differentially expressed in mouse fetal and adult hematopoietic
            stem cells and progenitors
  JOURNAL   Blood Cells Mol Dis 27 (1), 320-333 (2001)
   PUBMED   11358394
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP201682.1, BC032637.1 and
            AC073896.41.
            
            Summary: This gene encodes an E3 ubiquitin ligase. The encoded
            protein plays a role in type 1 cytokine receptor signaling by
            controlling the balance between JAK2-associated cytokine receptor
            degradation and ectodomain shedding. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 3 and 4 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.98093.1,
                                           SRR1803614.121559.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..317
                     /product="E3 ubiquitin-protein ligase NRDP1 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="neuregulin receptor degradation protein-1; fetal
                     liver ring finger; E3 ubiquitin-protein ligase NRDP1; ring
                     finger protein 41, E3 ubiquitin protein ligase; RING-type
                     E3 ubiquitin transferase NRDP1"
                     /calculated_mol_wt=35774
     Region          15..57
                     /region_name="mRING-HC-C3HC3D_Nrdp1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in neuregulin receptor degradation protein-1 (Nrdp1)
                     and similar proteins; cd16634"
                     /db_xref="CDD:438296"
     Region          137..315
                     /region_name="USP8_interact"
                     /note="USP8 interacting; pfam08941"
                     /db_xref="CDD:430333"
     CDS             1..317
                     /gene="RNF41"
                     /gene_synonym="FLRF; NRDP1; SBBI03"
                     /coded_by="NM_194359.2:276..1229"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS8909.1"
                     /db_xref="GeneID:10193"
                     /db_xref="HGNC:HGNC:18401"
                     /db_xref="MIM:620051"
ORIGIN      
        1 mgydvtrfqg dvdedlicpi csgvleepvq aphcehafcn acitqwfsqq qtcpvdrsvv
       61 tvahlrpvpr imrnmlsklq iacdnavfgc savvrldnlm shlsdcehnp krpvtceqgc
      121 glempkdelp nhncikhlrs vvqqqqtria elektsaehk hqlaeqkrdi qllkaymrai
      181 rsvnpnlqnl eetieyneil ewvnslqpar vtrwggmist pdavlqavik rslvesgcpa
      241 sivneliena herswpqgla tletrqmnrr yyenyvakri pgkqavvvma cenqhmgddm
      301 vqepglvmif ahgveei
//
LOCUS       NP_064501                847 aa            linear   PRI 20-NOV-2025
DEFINITION  follistatin-related protein 5 isoform a precursor [Homo sapiens].
ACCESSION   NP_064501
VERSION     NP_064501.2
DBSOURCE    REFSEQ: accession NM_020116.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Khanshour,A.M., Kidane,Y.H., Kozlitina,J., Cornelia,R., Rafipay,A.,
            De Mello,V., Weston,M., Paria,N., Khalid,A., Hecht,J.T.,
            Dobbs,M.B., Richards,B.S., Vargesson,N., Hamra,F.K., Wilson,M.,
            Wise,C., Gurnett,C.A. and Rios,J.J.
  TITLE     Genetic association and characterization of FSTL5 in isolated
            clubfoot
  JOURNAL   Hum Mol Genet 29 (22), 3717-3728 (2021)
   PUBMED   33105483
  REMARK    GeneRIF: Genetic association and characterization of FSTL5 in
            isolated clubfoot.
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Zhang,D.Y., Lei,J.S., Sun,W.L., Wang,D.D. and Lu,Z.
  TITLE     Follistatin Like 5 (FSTL5) inhibits epithelial to mesenchymal
            transition in hepatocellular carcinoma
  JOURNAL   Chin Med J (Engl) 133 (15), 1798-1804 (2020)
   PUBMED   32740091
  REMARK    GeneRIF: Follistatin Like 5 (FSTL5) inhibits epithelial to
            mesenchymal transition in hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Li,C., Dai,L., Zhang,J., Zhang,Y., Lin,Y., Cheng,L., Tian,H.,
            Zhang,X., Wang,Q., Yang,Q., Wang,Y., Shi,G., Cheng,F., Su,X.,
            Yang,Y., Zhang,S., Yu,D., Wei,Y. and Deng,H.
  TITLE     Follistatin-like protein 5 inhibits hepatocellular carcinoma
            progression by inducing caspase-dependent apoptosis and regulating
            Bcl-2 family proteins
  JOURNAL   J Cell Mol Med 22 (12), 6190-6201 (2018)
   PUBMED   30255547
  REMARK    GeneRIF: Mechanistic investigation demonstrated that FSTL5 promoted
            Hepatocellular carcinoma (HCC) cell apoptosis in a
            caspase-dependent manner and regulated Bcl-2 family proteins. These
            results indicate that FSTL5 may be a potential novel target for HCC
            treatment, and a biomarker for tumor prognosis.
            Erratum:[J Cell Mol Med. 2021 Apr;25(7):3665. doi:
            10.1111/jcmm.16364. PMID: 33835689]
REFERENCE   5  (residues 1 to 847)
  AUTHORS   Zhang,D., Ma,X., Sun,W., Cui,P. and Lu,Z.
  TITLE     Down-regulated FSTL5 promotes cell proliferation and survival by
            affecting Wnt/beta-catenin signaling in hepatocellular carcinoma
  JOURNAL   Int J Clin Exp Pathol 8 (3), 3386-3394 (2015)
   PUBMED   26045876
  REMARK    GeneRIF: FSTL5 plays a suppressive role in hepatocellular
            carcinoma. Down-regulation of FSTL5 could promote growth and
            survival of HCC cells by activation of Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Dowling,J.K., Becker,C.E., Bourke,N.M., Corr,S.C., Connolly,D.J.,
            Quinn,S.R., Pandolfi,P.P., Mansell,A. and O'Neill,L.A.J.
  TITLE     Promyelocytic leukemia protein interacts with the
            apoptosis-associated speck-like protein to limit inflammasome
            activation
  JOURNAL   J Biol Chem 289 (10), 6429-6437 (2014)
   PUBMED   24407287
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Remke,M., Hielscher,T., Korshunov,A., Northcott,P.A., Bender,S.,
            Kool,M., Westermann,F., Benner,A., Cin,H., Ryzhova,M., Sturm,D.,
            Witt,H., Haag,D., Toedt,G., Wittmann,A., Schottler,A., von
            Bueren,A.O., von Deimling,A., Rutkowski,S., Scheurlen,W.,
            Kulozik,A.E., Taylor,M.D., Lichter,P. and Pfister,S.M.
  TITLE     FSTL5 is a marker of poor prognosis in non-WNT/non-SHH
            medulloblastoma
  JOURNAL   J Clin Oncol 29 (29), 3852-3861 (2011)
   PUBMED   21911727
  REMARK    GeneRIF: FSTL5 expression denoted a dismal prognosis both within
            and across medulloblastoma subgroups.
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Croteau-Chonka,D.C., Marvelle,A.F., Lange,E.M., Lee,N.R.,
            Adair,L.S., Lange,L.A. and Mohlke,K.L.
  TITLE     Genome-wide association study of anthropometric traits and evidence
            of interactions with age and study year in Filipino women
  JOURNAL   Obesity (Silver Spring) 19 (5), 1019-1027 (2011)
   PUBMED   20966902
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Glusman,G., Kaur,A., Hood,L. and Rowen,L.
  TITLE     An enigmatic fourth runt domain gene in the fugu genome: ancestral
            gene loss versus accelerated evolution
  JOURNAL   BMC Evol Biol 4, 43 (2004)
   PUBMED   15527507
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fields,C. and Venter,J.C.
  TITLE     3,400 new expressed sequence tags identify diversity of transcripts
            in human brain
  JOURNAL   Nat Genet 4 (3), 256-267 (1993)
   PUBMED   8358434
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI549596.1, DA243182.1, BC036502.2, AB033089.1 and AA350666.1.
            
            On Jun 14, 2008 this sequence version replaced NP_064501.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036502.2, SRR1803617.105443.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2146411
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306100.10/ ENSP00000305334.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q32.2"
     Protein         1..847
                     /product="follistatin-related protein 5 isoform a
                     precursor"
                     /note="follistatin-related protein 5; follistatin-like
                     protein 5"
                     /calculated_mol_wt=93465
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2305
     mat_peptide     21..847
                     /product="Follistatin-related protein 5.
                     /id=PRO_0000010118"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N475.2)"
                     /calculated_mol_wt=93465
     Region          93..133
                     /region_name="KAZAL_FS"
                     /note="Kazal type serine protease inhibitors and
                     follistatin-like domains. Kazal inhibitors inhibit serine
                     proteases, such as, trypsin, chyomotrypsin, avian
                     ovomucoids, and elastases. The inhibitory domain has one
                     reactive site peptide bond, which serves the...; cd00104"
                     /db_xref="CDD:238052"
     Region          <180..240
                     /region_name="PTZ00183"
                     /note="centrin; Provisional"
                     /db_xref="CDD:185503"
     Region          256..323
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            318
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N475.2)"
     Region          341..433
                     /region_name="IgI_2_Follistatin_like"
                     /note="Second immunoglobulin (Ig)-like domain of a
                     Follistatin-related protein 5, and similar domains; member
                     of the I-set of Ig superfamily (IgSF) domains; cd05736"
                     /db_xref="CDD:409399"
     Region          341..344
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409399"
     Region          347..351
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409399"
     Region          358..365
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409399"
     Region          371..376
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409399"
     Region          378..380
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409399"
     Region          388..392
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409399"
     Site            394
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8N475.2)"
     Region          396..401
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409399"
     Region          410..416
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409399"
     Region          421..430
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409399"
     Region          <512..663
                     /region_name="YncE"
                     /note="DNA-binding beta-propeller fold protein YncE
                     [General function prediction only]; COG3391"
                     /db_xref="CDD:442618"
     CDS             1..847
                     /gene="FSTL5"
                     /coded_by="NM_020116.5:403..2946"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3802.1"
                     /db_xref="GeneID:56884"
                     /db_xref="HGNC:HGNC:21386"
                     /db_xref="MIM:620128"
ORIGIN      
        1 mfkcwsvvlv lgfifleseg rptkeggygl ksyqplmrlr hkqeknqess rvkgfmiqdg
       61 pfgscenkyc glgrhcvtsr etgqaecacm dlckrhykpv cgsdgefyen hcevhraacl
      121 kkqkitivhn edcffkgdkc ktteyskmkn mlldlqnqky imqenenpng ddisrkkllv
      181 dqmfkyfdad snglvdinel tqvikqeelg kdlfdctlyv llkyddfnad khlaleefyr
      241 afqviqlslp edqklsitaa tvgqsavlsc aiqgtlrppi iwkrnniiln nldledindf
      301 gddgslyitk vttthvgnyt cyadgyeqvy qthifqvnvp pvirvypesq arepgvtasl
      361 rchaegipkp qlgwlkngid itpklskqlt lqangsevhi snvryedtga ytciakneag
      421 vdedisslfv edsarktlan ilwreeglgi gnmfyvfyed gikviqpiec efqrhikpse
      481 kllgfqdevc pkaegdevqr cvwasavnvk dkfiyvaqpt ldrvlivdvq sqkvvqavst
      541 dpvpvklhyd kshdqvwvls wgtlektspt lqvitlasgn vphhtihtqp vgkqfdrvdd
      601 ffiptttlii thmrfgfilh kdeaalqkid letmsyikti nlkdykcvpq slaythlggy
      661 yfigckpdst gavspqvmvd gvtdsvigfn sdvtgtpyvs pdghylvsin dvkglvrvqy
      721 itirgeiqea fdiytnlhis dlafqpsfte ahqyniygss stqtdvlfve lssgkvkmik
      781 slkeplkaee wpwnrknrqi qdsglfgqyl mtpskdslfi ldgrlnklnc eitevekgnt
      841 viwvgda
//
LOCUS       NP_001335336             312 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral amino acid transporter A isoform 3 [Homo sapiens].
ACCESSION   NP_001335336
VERSION     NP_001335336.1
DBSOURCE    REFSEQ: accession NM_001348407.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Sarigecili,E., Bulut,F.D. and Anlas,O.
  TITLE     A rare cause of microcephaly, thin corpus callosum and refractory
            epilepsy due to a novel SLC1A4 gene mutation
  JOURNAL   Clin Neurol Neurosurg 218, 107283 (2022)
   PUBMED   35605507
  REMARK    GeneRIF: A rare cause of microcephaly, thin corpus callosum and
            refractory epilepsy due to a novel SLC1A4 gene mutation.
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Foster,A.C., Rangel-Diaz,N., Staubli,U., Yang,J.Y., Penjwini,M.,
            Viswanath,V. and Li,Y.X.
  TITLE     Phenylglycine analogs are inhibitors of the neutral amino acid
            transporters ASCT1 and ASCT2 and enhance NMDA receptor-mediated LTP
            in rat visual cortex slices
  JOURNAL   Neuropharmacology 126, 70-83 (2017)
   PUBMED   28807674
  REMARK    GeneRIF: Results suggest that ASCT1/2 may play an important role in
            regulating extracellular d-serine and NMDA receptor-mediated
            physiological effects and that ASCT1/2 inhibitors have the
            potential for therapeutic benefit.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Kvainickas,A., Orgaz,A.J., Nagele,H., Diedrich,B., Heesom,K.J.,
            Dengjel,J., Cullen,P.J. and Steinberg,F.
  TITLE     Retromer- and WASH-dependent sorting of nutrient transporters
            requires a multivalent interaction network with ANKRD50
  JOURNAL   J Cell Sci 130 (2), 382-395 (2017)
   PUBMED   27909246
  REMARK    GeneRIF: ANKRD50 simultaneously engages multiple parts of the
            SNX27-retromer-WASH complex machinery in a direct and co-operative
            interaction network that is needed to efficiently recycle the
            nutrient transporters
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Zerangue,N. and Kavanaugh,M.P.
  TITLE     ASCT-1 is a neutral amino acid exchanger with chloride channel
            activity
  JOURNAL   J Biol Chem 271 (45), 27991-27994 (1996)
   PUBMED   8910405
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Tamarappoo,B.K., McDonald,K.K. and Kilberg,M.S.
  TITLE     Expressed human hippocampal ASCT1 amino acid transporter exhibits a
            pH-dependent change in substrate specificity
  JOURNAL   Biochim Biophys Acta 1279 (2), 131-136 (1996)
   PUBMED   8603078
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Hofmann,K., Duker,M., Fink,T., Lichter,P. and Stoffel,W.
  TITLE     Human neutral amino acid transporter ASCT1: structure of the gene
            (SLC1A4) and localization to chromosome 2p13-p15
  JOURNAL   Genomics 24 (1), 20-26 (1994)
   PUBMED   7896285
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Shafqat,S., Tamarappoo,B.K., Kilberg,M.S., Puranam,R.S.,
            McNamara,J.O., Guadano-Ferraz,A. and Fremeau,R.T. Jr.
  TITLE     Cloning and expression of a novel Na(+)-dependent neutral amino
            acid transporter structurally related to mammalian Na+/glutamate
            cotransporters
  JOURNAL   J Biol Chem 268 (21), 15351-15355 (1993)
   PUBMED   8340364
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Arriza,J.L., Kavanaugh,M.P., Fairman,W.A., Wu,Y.N., Murdoch,G.H.,
            North,R.A. and Amara,S.G.
  TITLE     Cloning and expression of a human neutral amino acid transporter
            with structural similarity to the glutamate transporter gene family
  JOURNAL   J Biol Chem 268 (21), 15329-15332 (1993)
   PUBMED   8101838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007386.3.
            
            Summary: The protein encoded by this gene is a sodium-dependent
            neutral amino acid transporter for alanine, serine, cysteine, and
            threonine. Defects in this gene have been associated with
            developmental delay, microcephaly, and intellectual disability.
            [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (3) is
            shorter at the N-terminus compared to isoform 1. Variants 3 and 4
            both encode the same isoform (3).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.94838.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p14"
     Protein         1..312
                     /product="neutral amino acid transporter A isoform 3"
                     /note="glutamate/neutral amino acid transporter; neutral
                     amino acid transporter A;
                     alanine/serine/cysteine/threonine transporter 1; solute
                     carrier family 1 (glutamate/neutral amino acid
                     transporter), member 4"
                     /calculated_mol_wt=33087
     Region          <2..251
                     /region_name="GltP"
                     /note="Na+/H+-dicarboxylate symporter [Energy production
                     and conversion]; COG1301"
                     /db_xref="CDD:440912"
     CDS             1..312
                     /gene="SLC1A4"
                     /gene_synonym="ASCT1; SATT; SPATCCM"
                     /coded_by="NM_001348407.2:210..1148"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:6509"
                     /db_xref="HGNC:HGNC:10942"
                     /db_xref="MIM:600229"
ORIGIN      
        1 mnilglvlfa lvlgvalkkl gsegedlirf fnslneatmv lvswimwyvp vgimflvgsk
       61 ivemkdiivl vtslgkyifa silghvihgg ivlpliyfvf trknpfrfll gllapfataf
      121 atcsssatlp smmkcieenn gvdkrisrfi lpigatvnmd gaaifqcvaa vfiaqlnnve
      181 lnagqiftil vtatassvga agvpaggvlt iaiileaigl pthdlplila vdwivdrttt
      241 vvnvegdalg agilhhlnqk atkkgeqela evkveaipnc kseeetsplv thqnpagpva
      301 sapeleskes vl
//
LOCUS       NP_001354475             565 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 39 [Homo sapiens].
ACCESSION   NP_001354475 XP_005270254
VERSION     NP_001354475.1
DBSOURCE    REFSEQ: accession NM_001367546.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270254.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.633099.1,
                                           SRR3476690.930512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..565
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 39"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=62706
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          433..560
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..565
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367546.1:95..1792"
                     /note="isoform 39 is encoded by transcript variant 39"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkaaplrtg ngssvpegrs srdrtapsag
      421 mqpqpslcss amrkqeiiki teqlieainn gdfeaytkic dpgltsfepe algnlvegmd
      481 fhkfyfenll sknskpihtt ilnphvhvig edaaciayir ltqyidgqgr prtsqseetr
      541 vwhrrdgkwl nvhyhcsgap aaplq
//
LOCUS       NP_076493               1253 aa            linear   PRI 20-NOV-2025
DEFINITION  neural cell adhesion molecule L1 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_076493
VERSION     NP_076493.1
DBSOURCE    REFSEQ: accession NM_024003.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1253)
  AUTHORS   Mannan,R., Wang,X., Mahapatra,S., Wang,S., Chinnaiyan,A.K.,
            Skala,S.L., Zhang,Y., McMurry,L.M., Zelenka-Wang,S., Cao,X.,
            Sangoi,A.R., Dadhania,V., Picken,M.M., Menon,S., Al-Ahmadie,H.,
            Chinnaiyan,A.M., Dhanasekaran,S.M. and Mehra,R.
  TITLE     Expression of L1 Cell Adhesion Molecule, a Nephronal Principal Cell
            Marker, in Nephrogenic Adenoma
  JOURNAL   Mod Pathol 37 (8), 100540 (2024)
   PUBMED   38901674
  REMARK    GeneRIF: Expression of L1 Cell Adhesion Molecule, a Nephronal
            Principal Cell Marker, in Nephrogenic Adenoma.
REFERENCE   2  (residues 1 to 1253)
  AUTHORS   Hauser,S., Bickel,L., Weinspach,D., Gerg,M., Schafer,M.K.,
            Pfeifer,M., Hazin,J., Schelter,F., Weidle,U.H., Ramser,J.,
            Volkmann,J., Meindl,A., Schmitt,M., Schrotzlmair,F., Altevogt,P.
            and Kruger,A.
  TITLE     Full-length L1CAM and not its Delta2Delta27 splice variant promotes
            metastasis through induction of gelatinase expression
  JOURNAL   PLoS One 6 (4), e18989 (2011)
   PUBMED   21541352
  REMARK    GeneRIF: Metastasis formation upon up-regulation of full
            length-L1CAM correlated with increased invasive potential and
            elevated Matrix metalloproteinase (MMP)-2 and -9 expression and
            activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1253)
  AUTHORS   Pfeifer,M., Schirmer,U., Geismann,C., Schafer,H., Sebens,S. and
            Altevogt,P.
  TITLE     L1CAM expression in endometrial carcinomas is regulated by usage of
            two different promoter regions
  JOURNAL   BMC Mol Biol 11, 64 (2010)
   PUBMED   20799950
  REMARK    GeneRIF: Results suggest that the L1CAM gene has two functionally
            active promoter sites that are used in a cell-type specific manner.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1253)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   5  (residues 1 to 1253)
  AUTHORS   Stumpel,C. and Vos,Y.J.
  TITLE     L1 Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301657
REFERENCE   6  (residues 1 to 1253)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   7  (residues 1 to 1253)
  AUTHORS   Rosenthal,A., Jouet,M. and Kenwrick,S.
  TITLE     Aberrant splicing of neural cell adhesion molecule L1 mRNA in a
            family with X-linked hydrocephalus
  JOURNAL   Nat Genet 2 (2), 107-112 (1992)
   PUBMED   1303258
  REMARK    Erratum:[Nat Genet 1993 Mar;3(3):273]
REFERENCE   8  (residues 1 to 1253)
  AUTHORS   Kobayashi,M., Miura,M., Asou,H. and Uyemura,K.
  TITLE     Molecular cloning of cell adhesion molecule L1 from human nervous
            tissue: a comparison of the primary sequences of L1 molecules of
            different origin
  JOURNAL   Biochim Biophys Acta 1090 (2), 238-240 (1991)
   PUBMED   1932117
REFERENCE   9  (residues 1 to 1253)
  AUTHORS   Hlavin,M.L. and Lemmon,V.
  TITLE     Molecular structure and functional testing of human L1CAM: an
            interspecies comparison
  JOURNAL   Genomics 11 (2), 416-423 (1991)
   PUBMED   1769655
REFERENCE   10 (residues 1 to 1253)
  AUTHORS   Djabali,M., Mattei,M.G., Nguyen,C., Roux,D., Demengeot,J.,
            Denizot,F., Moos,M., Schachner,M., Goridis,C. and Jordan,B.R.
  TITLE     The gene encoding L1, a neural adhesion molecule of the
            immunoglobulin family, is located on the X chromosome in mouse and
            man
  JOURNAL   Genomics 7 (4), 587-593 (1990)
   PUBMED   2387585
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC126229.1, M74387.1,
            BC025843.1 and AI361399.1.
            
            Summary: The protein encoded by this gene is an axonal glycoprotein
            belonging to the immunoglobulin supergene family. The ectodomain,
            consisting of several immunoglobulin-like domains and
            fibronectin-like repeats (type III), is linked via a single
            transmembrane sequence to a conserved cytoplasmic domain. This cell
            adhesion molecule plays an important role in nervous system
            development, including neuronal migration and differentiation.
            Mutations in the gene cause X-linked neurological syndromes known
            as CRASH (corpus callosum hypoplasia, retardation, aphasia, spastic
            paraplegia and hydrocephalus). Alternative splicing of this gene
            results in multiple transcript variants, some of which include an
            alternate exon that is considered to be specific to neurons.
            [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            neuron-specific exon in the 3' coding region, compared to variant
            4. The resulting isoform (2) is shorter and lacks an internal
            segment containing a tyrosine-based sorting motif, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M74387.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..1253
                     /product="neural cell adhesion molecule L1 isoform 2
                     precursor"
                     /note="neural cell adhesion molecule L1; antigen
                     identified by monoclonal antibody R1"
                     /calculated_mol_wt=137346
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2190
     Region          35..130
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          53..57
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409396"
     Region          66..70
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409396"
     Region          93..97
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409396"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          111..116
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409396"
     Region          125..128
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409396"
     Region          140..230
                     /region_name="IgI_2_L1-CAM_like"
                     /note="Second immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM), and similar domains; member
                     of the I-set of Ig superfamily (IgSF) domains; cd05845"
                     /db_xref="CDD:409432"
     Region          140..143
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409432"
     Region          145..149
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409432"
     Region          152..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          167..173
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          176..179
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409432"
     Region          185..189
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409432"
     Region          191..195
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          206..214
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Region          217..230
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Site            247
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          248..330
                     /region_name="Ig3_L1-CAM"
                     /note="Third immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05876"
                     /db_xref="CDD:409460"
     Region          260..264
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409460"
     Region          273..277
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409460"
     Site            294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          295..299
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409460"
     Region          309..314
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409460"
     Region          322..325
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409460"
     Region          334..422
                     /region_name="Ig4_L1-CAM_like"
                     /note="Fourth immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM); cd05867"
                     /db_xref="CDD:409453"
     Region          350..354
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409453"
     Region          363..367
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409453"
     Region          387..391
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409453"
     Region          401..406
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409453"
     Region          414..417
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409453"
     Region          428..514
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            433
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          444..448
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409544"
     Region          457..461
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409544"
     Site            479
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          480..484
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409544"
     Site            490
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          494..499
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409544"
     Site            505
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          507..510
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409544"
     Region          519..594
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          554..556
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            588
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          612..709
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(612,681,696)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          <627..>837
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            671
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(697..698,700..701)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          698..725
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            726
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            777
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(812,887,902)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          824..907
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            825
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            849
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            876
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            order(903..904,906..907)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          918..1003
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(918,985,1000)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            979
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1022
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1030
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1071
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1121..1143
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Region          1144..1229
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK2.
                     /evidence=ECO:0000269|PubMed:8592152; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Region          1222..1253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32004.2)"
     Site            1239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P11627; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     Site            1244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P32004.2)"
     CDS             1..1253
                     /gene="L1CAM"
                     /gene_synonym="CAML1; CD171; HSAS; HSAS1; HYCX; MASA;
                     MIC5; N-CAM-L1; N-CAML1; NCAM-L1; S10; SPG1"
                     /coded_by="NM_024003.3:109..3870"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS14734.1"
                     /db_xref="GeneID:3897"
                     /db_xref="HGNC:HGNC:6470"
                     /db_xref="MIM:308840"
ORIGIN      
        1 mvvalryvwp lllcspclli qipeeyeghh vmeppviteq sprrlvvfpt ddislkceas
       61 gkpevqfrwt rdgvhfkpke elgvtvyqsp hsgsftitgn nsnfaqrfqg iyrcfasnkl
      121 gtamsheirl maegapkwpk etvkpvevee gesvvlpcnp ppsaeplriy wmnskilhik
      181 qdervtmgqn gnlyfanvlt sdnhsdyich ahfpgtrtii qkepidlrvk atnsmidrkp
      241 rllfptnsss hlvalqgqpl vleciaegfp tptikwlrps gpmpadrvty qnhnktlqll
      301 kvgeeddgey rclaenslgs arhayyvtve aapywlhkpq shlygpgeta rldcqvqgrp
      361 qpevtwring ipveelakdq kyriqrgali lsnvqpsdtm vtqcearnrh glllanayiy
      421 vvqlpakilt adnqtymavq gstayllcka fgapvpsvqw ldedgttvlq derffpyang
      481 tlgirdlqan dtgryfclaa ndqnnvtima nlkvkdatqi tqgprstiek kgsrvtftcq
      541 asfdpslqps itwrgdgrdl qelgdsdkyf iedgrlvihs ldysdqgnys cvasteldvv
      601 esraqllvvg spgpvprlvl sdlhlltqsq vrvswspaed hnapiekydi efedkemape
      661 kwyslgkvpg nqtsttlkls pyvhytfrvt ainkygpgep spvsetvvtp eaapeknpvd
      721 vkgegnettn mvitwkplrw mdwnapqvqy rvqwrpqgtr gpwqeqivsd pflvvsntst
      781 fvpyeikvqa vnsqgkgpep qvtigysged ypqaipeleg ieilnssavl vkwrpvdlaq
      841 vkghlrgynv tywregsqrk hskrhihkdh vvvpanttsv ilsglrpyss yhlevqafng
      901 rgsgpaseft fstpegvpgh pealhlecqs ntslllrwqp plshngvltg yvlsyhplde
      961 ggkgqlsfnl rdpelrthnl tdlsphlryr fqlqattkeg pgeaivregg tmalsgisdf
     1021 gnisatagen ysvvswvpke gqcnfrfhil fkalgeekgg aslspqyvsy nqssytqwdl
     1081 qpdtdyeihl fkermfrhqm avktngtgrv rlppagfate gwfigfvsai illllvllil
     1141 cfikrskggk ysvkdkedtq vdsearpmkd etfgeysdne ekafgssqps lngdikplgs
     1201 ddsladyggs vdvqfnedgs figqysgkke keaaggndss gatspinpav ale
//
LOCUS       NP_037423               1443 aa            linear   PRI 20-NOV-2025
DEFINITION  cleavage and polyadenylation specificity factor subunit 1 [Homo
            sapiens].
ACCESSION   NP_037423
VERSION     NP_037423.2
DBSOURCE    REFSEQ: accession NM_013291.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1443)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   2  (residues 1 to 1443)
  AUTHORS   Chen,X., Lloyd,S.M., Kweon,J., Gamalong,G.M. and Bao,X.
  TITLE     Epidermal progenitors suppress GRHL3-mediated differentiation
            through intronic polyadenylation promoted by CPSF-HNRNPA3
            collaboration
  JOURNAL   Nat Commun 12 (1), 448 (2021)
   PUBMED   33469008
  REMARK    GeneRIF: Epidermal progenitors suppress GRHL3-mediated
            differentiation through intronic polyadenylation promoted by
            CPSF-HNRNPA3 collaboration.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1443)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1443)
  AUTHORS   Ouyang,J., Sun,W., Xiao,X., Li,S., Jia,X., Zhou,L., Wang,P. and
            Zhang,Q.
  TITLE     CPSF1 mutations are associated with early-onset high myopia and
            involved in retinal ganglion cell axon projection
  JOURNAL   Hum Mol Genet 28 (12), 1959-1970 (2019)
   PUBMED   30689892
  REMARK    GeneRIF: Heterozygous loss-of-function mutations in CPSF1 are
            associated with early-onset high myopia and that CPSF1 may play an
            important role in the development of retinal ganglion cell axon
            projection.
REFERENCE   5  (residues 1 to 1443)
  AUTHORS   Clerici,M., Faini,M., Muckenfuss,L.M., Aebersold,R. and Jinek,M.
  TITLE     Structural basis of AAUAAA polyadenylation signal recognition by
            the human CPSF complex
  JOURNAL   Nat Struct Mol Biol 25 (2), 135-138 (2018)
   PUBMED   29358758
  REMARK    GeneRIF: cryo-electron microscopic analysis of a core CPSF module
            bound to the polyadenylation signal hexamer motif
            Erratum:[Nat Struct Mol Biol. 2018 Apr;25(4):355. doi:
            10.1038/s41594-018-0044-6. PMID: 29540792]
REFERENCE   6  (residues 1 to 1443)
  AUTHORS   Schul,W., Groenhout,B., Koberna,K., Takagaki,Y., Jenny,A.,
            Manders,E.M., Raska,I., van Driel,R. and de Jong,L.
  TITLE     The RNA 3' cleavage factors CstF 64 kDa and CPSF 100 kDa are
            concentrated in nuclear domains closely associated with coiled
            bodies and newly synthesized RNA
  JOURNAL   EMBO J 15 (11), 2883-2892 (1996)
   PUBMED   8654386
REFERENCE   7  (residues 1 to 1443)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   8  (residues 1 to 1443)
  AUTHORS   Jenny,A. and Keller,W.
  TITLE     Cloning of cDNAs encoding the 160 kDa subunit of the bovine
            cleavage and polyadenylation specificity factor
  JOURNAL   Nucleic Acids Res 23 (14), 2629-2635 (1995)
   PUBMED   7651824
REFERENCE   9  (residues 1 to 1443)
  AUTHORS   Thuresson,A.C., Astrom,J., Astrom,A., Gronvik,K.O. and Virtanen,A.
  TITLE     Multiple forms of poly(A) polymerases in human cells
  JOURNAL   Proc Natl Acad Sci U S A 91 (3), 979-983 (1994)
   PUBMED   8302877
REFERENCE   10 (residues 1 to 1443)
  AUTHORS   Keller,W., Bienroth,S., Lang,K.M. and Christofori,G.
  TITLE     Cleavage and polyadenylation factor CPF specifically interacts with
            the pre-mRNA 3' processing signal AAUAAA
  JOURNAL   EMBO J 10 (13), 4241-4249 (1991)
   PUBMED   1756731
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD299980.1 and BC017232.2.
            
            On Dec 16, 2004 this sequence version replaced NP_037423.1.
            
            Summary: Cleavage and polyadenylation specificity factor (CPSF) is
            a multisubunit complex that plays a central role in 3-prime
            processing of pre-mRNAs. CPSF recognizes the AAUAAA signal in the
            pre-mRNA and interacts with other proteins to facilitate both RNA
            cleavage and poly(A) synthesis. CPSF1 is the largest subunit of the
            CPSF complex (Murthy and Manley, 1995 [PubMed 7590244]).[supplied
            by OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC017232.2, U37012.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000616140.2/ ENSP00000484669.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1443
                     /product="cleavage and polyadenylation specificity factor
                     subunit 1"
                     /EC_number="2.4.2.30"
                     /note="polyadenylation specificity factor; CPSF 160 kDa
                     subunit; cleavage and polyadenylation specificity factor
                     160 kDa subunit; cleavage and polyadenylation specific
                     factor 1, 160kDa"
                     /calculated_mol_wt=160754
     Region          1..1437
                     /region_name="SFT1"
                     /note="Pre-mRNA cleavage and polyadenylation specificity
                     factor [RNA processing and modification]; COG5161"
                     /db_xref="CDD:227490"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          546..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          715..777
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EPU4; propagated from
                     UniProtKB/Swiss-Prot (Q10570.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q10570.2)"
     Region          893..908
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     Region          901..921
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q10570.2)"
     CDS             1..1443
                     /gene="CPSF1"
                     /gene_synonym="CPSF160; HSU37012; MYP27; P/cl.18"
                     /coded_by="NM_013291.3:62..4393"
                     /db_xref="CCDS:CCDS34966.1"
                     /db_xref="GeneID:29894"
                     /db_xref="HGNC:HGNC:2324"
                     /db_xref="MIM:606027"
ORIGIN      
        1 myavykqahp ptglefsmyc nffnnsernl vvagtsqlyv yrlnrdaeal tkndrstegk
       61 ahreklelaa sfsffgnvms masvqlagak rdalllsfkd aklsvveydp gthdlktlsl
      121 hyfeepelrd gfvqnvhtpr vrvdpdgrca amlvygtrlv vlpfrresla eeheglvgeg
      181 qrssflpsyi idvraldekl lniidlqflh gyyeptllil fepnqtwpgr vavrqdtcsi
      241 vaislnitqk vhpviwslts lpfdctqala vpkpiggvvv favnsllyln qsvppygval
      301 nslttgttaf plrtqegvri tldcaqatfi sydkmvislk ggeiyvltli tdgmrsvraf
      361 hfdkaaasvl ttsmvtmepg ylflgsrlgn slllkytekl qeppasavre aadkeeppsk
      421 kkrvdatagw saagksvpqd evdeievygs eaqsgtqlat ysfevcdsil nigpcanaav
      481 gepaflseef qnspepdlei vvcsghgkng alsvlqksir pqvvttfelp gcydmwtvia
      541 pvrkeeednp kgegteqeps ttpeadddgr rhgflilsre dstmilqtgq eimeldtsgf
      601 atqgptvfag nigdnryivq vsplgirlle gvnqlhfipv dlgapivqca vadpyvvims
      661 aeghvtmfll ksdsyggrhh rlalhkpplh hqskvitlcl yrdlsgmftt esrlggarde
      721 lggrsgpeae glgsetsptv ddeeemlygd sgslfspske earrssqppa drdpapfrae
      781 pthwcllvre ngtmeiyqlp dwrlvflvkn fpvgqrvlvd ssfgqpttqg earreeatrq
      841 gelplvkevl lvalgsrqsr pyllvhvdqe lliyeafphd sqlgqgnlkv rfkkvphnin
      901 frekkpkpsk kkaegggaee gagargrvar fryfediygy sgvficgpsp hwllvtgrga
      961 lrlhpmaidg pvdsfapfhn vncprgflyf nrqgelrisv lpaylsydap wpvrkiplrc
     1021 tahyvayhve skvyavatst ntpcariprm tgeekefeti erderyihpq qeafsiqlis
     1081 pvsweaipna rielqewehv tcmktvslrs eetvsglkgy vaagtclmqg eevtcrgril
     1141 imdvievvpe pgqpltknkf kvlyekeqkg pvtalchcng hlvsaigqki flwslrasel
     1201 tgmafidtql yihqmisvkn filaadvmks isllryqees ktlslvsrda kplevysvdf
     1261 mvdnaqlgfl vsdrdrnlmv ymylpeakes fggmrllrra dfhvgahvnt fwrtpcrgat
     1321 eglskksvvw enkhitwfat ldggiglllp mqektyrrll mlqnalttml phhaglnpra
     1381 frmlhvdrrt lqnavrnvld gellnrylyl stmerselak kigttpdiil ddlletdrvt
     1441 ahf
//
LOCUS       NP_001137322             696 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-2 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001137322
VERSION     NP_001137322.1
DBSOURCE    REFSEQ: accession NM_001143850.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Liu,Q., Zhu,C. and Dong,Y.
  TITLE     LncRNA TCTN2 Promotes the Malignant Development of Hepatocellular
            Carcinoma via Regulating mIR-1285-3p/ARF6 Axis
  JOURNAL   Recent Pat Anticancer Drug Discov 18 (4), 517-527 (2023)
   PUBMED   36278455
  REMARK    GeneRIF: LncRNA TCTN2 Promotes the Malignant Development of
            Hepatocellular Carcinoma via Regulating mIR-1285-3p/ARF6 Axis.
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Litz Philipsborn,S., Hartmajer,S., Shtorch Asor,A., Vinovezky,M.,
            Regev,M., Singer,A. and Reinstein,E.
  TITLE     A founder mutation in TCTN2 causes Meckel-Gruber syndrome type 8
            among Jews of Ethiopian and Yemenite origin
  JOURNAL   Am J Med Genet A 185 (5), 1610-1613 (2021)
   PUBMED   33590725
  REMARK    GeneRIF: A founder mutation in TCTN2 causes Meckel-Gruber syndrome
            type 8 among Jews of Ethiopian and Yemenite origin.
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Shaheen,R., Faqeih,E., Seidahmed,M.Z., Sunker,A., Alali,F.E.,
            AlQahtani,K. and Alkuraya,F.S.
  TITLE     A TCTN2 mutation defines a novel Meckel Gruber syndrome locus
  JOURNAL   Hum Mutat 32 (6), 573-578 (2011)
   PUBMED   21462283
  REMARK    GeneRIF: a truncating mutation in TCTN2 linked to Meckel Gruber
            syndrome was shown.
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Sang,L., Miller,J.J., Corbit,K.C., Giles,R.H., Brauer,M.J.,
            Otto,E.A., Baye,L.M., Wen,X., Scales,S.J., Kwong,M.,
            Huntzicker,E.G., Sfakianos,M.K., Sandoval,W., Bazan,J.F.,
            Kulkarni,P., Garcia-Gonzalo,F.R., Seol,A.D., O'Toole,J.F., Held,S.,
            Reutter,H.M., Lane,W.S., Rafiq,M.A., Noor,A., Ansar,M., Devi,A.R.,
            Sheffield,V.C., Slusarski,D.C., Vincent,J.B., Doherty,D.A.,
            Hildebrandt,F., Reiter,J.F. and Jackson,P.K.
  TITLE     Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy
            disease genes and pathways
  JOURNAL   Cell 145 (4), 513-528 (2011)
   PUBMED   21565611
  REMARK    GeneRIF: Network building strategy led to the proposal of
            candidates for new ciliopathy disease genes, leading to the
            identification of the first human mutations in the Nephronophthisis
            gene Ataxin10 (ATXN10) and Joubert syndrome gene Tectonic2 (TCTN2).
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 696)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292153.1, BC009112.1 and
            BQ774678.1.
            
            Summary: This gene encodes a type I membrane protein that belongs
            to the tectonic family. Studies in mice suggest that this protein
            may be involved in hedgehog signaling, and essential for
            ciliogenesis. Mutations in this gene are associated with Meckel
            syndrome type 8. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            acceptor splice site at an internal coding exon compared to variant
            1. This results in a shorter  isoform (2) missing 1 aa compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292153.1, SRR1803616.63891.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..696
                     /product="tectonic-2 isoform 2 precursor"
                     /calculated_mol_wt=73923
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
                     /calculated_mol_wt=2838
     mat_peptide     26..696
                     /product="tectonic-2 isoform 2"
                     /calculated_mol_wt=73923
     Site            145
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            155
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Region          170..443
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     Site            390
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96GX1.1)"
     Site            668..688
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GX1.1)"
     CDS             1..696
                     /gene="TCTN2"
                     /gene_synonym="C12orf38; JBTS24; MKS8; TECT2"
                     /coded_by="NM_001143850.3:129..2219"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS45007.1"
                     /db_xref="GeneID:79867"
                     /db_xref="HGNC:HGNC:25774"
                     /db_xref="MIM:613846"
ORIGIN      
        1 mgfqppaall lrlfllqgil rllwgdlafi ppfirmsgpa vsaslvgdte gvtvslavlq
       61 deagilpipt cgvlnneted wsvtvipgav levtvrwkrg ldwcssnetd sfsespcilq
      121 tllvsashns scsahlliqv eiyansslth nasenvtvip nqvyqplgpc pcnltagacd
      181 vrcccdqecs snlttlfrrs cftgvfggdv nppfdqlcsa gtttrgvpdw fpflcvqspl
      241 antpflgyfy hgavspkqds sfevyvdtda kdfadfgykq gdpimtvkka yftipqvsla
      301 gqcmqnapva flhnfdvkcv tnlelyqerd giinakiknv alggivtpkv iyeeatdldk
      361 fitntetpln ngstprivnv eehyifkwnn ntiseinvki fraeinahqk gimtqrfvvk
      421 flsynsgnee elsgnpgyql gkpvralnin rmnnvttlhl wqsagrglct satfkpilfg
      481 envlsgclle vginenctql renaverlds liqathvamr gnsdyadlsd gwleiirvda
      541 pdpgadplas svngmcldip ahlsirilis dagavegitq qeilgvetrf ssvnwqyqcg
      601 ltcehkadll pisasvqfik ipaqlphplt rfqinyteyd cnrnevcwpq llypwtqyyq
      661 gelhsqcvak glllllfltl alflsnpwtr ickays
//
LOCUS       NP_001269027             454 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional coactivator YAP1 isoform 5 [Homo sapiens].
ACCESSION   NP_001269027 XP_005271443
VERSION     NP_001269027.1
DBSOURCE    REFSEQ: accession NM_001282098.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 454)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 454)
  AUTHORS   Tang,W., Yang,Y., Fu,Z., Xu,W., Ou,W., Liu,F., Du,P. and Liu,C.Y.
  TITLE     The RNA helicase DDX21 activates YAP to promote tumorigenesis and
            is transcriptionally upregulated by beta-catenin in colorectal
            cancer
  JOURNAL   Oncogene 43 (44), 3227-3239 (2024)
   PUBMED   39285230
  REMARK    GeneRIF: The RNA helicase DDX21 activates YAP to promote
            tumorigenesis and is transcriptionally upregulated by beta-catenin
            in colorectal cancer.
REFERENCE   3  (residues 1 to 454)
  AUTHORS   He,C., Lv,X., Liu,J., Ruan,J., Chen,P., Huang,C., Angeletti,P.C.,
            Hua,G., Moness,M.L., Shi,D., Dhar,A., Yang,S., Murphy,S.,
            Montoute,I., Chen,X., Islam,K.N., George,S., Ince,T.A., Drapkin,R.,
            Guda,C., Davis,J.S. and Wang,C.
  TITLE     HPV-YAP1 oncogenic alliance drives malignant transformation of
            fallopian tube epithelial cells
  JOURNAL   EMBO Rep 25 (10), 4542-4569 (2024)
   PUBMED   39271776
  REMARK    GeneRIF: HPV-YAP1 oncogenic alliance drives malignant
            transformation of fallopian tube epithelial cells.
REFERENCE   4  (residues 1 to 454)
  AUTHORS   Meyer,N.P., Singh,T., Kutys,M.L., Nystul,T.G. and Barber,D.L.
  TITLE     Arp2/3 complex activity enables nuclear YAP for naive pluripotency
            of human embryonic stem cells
  JOURNAL   Elife 13, e89725 (2024)
   PUBMED   39319536
  REMARK    GeneRIF: Arp2/3 complex activity enables nuclear YAP for naive
            pluripotency of human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 454)
  AUTHORS   Jimbo,N., Ohbayashi,C., Fujii,T., Takeda,M., Mitsui,S., Tanaka,Y.,
            Itoh,T. and Maniwa,Y.
  TITLE     The expression of YAP1 and other transcription factors contributes
            to lineage plasticity in combined small cell lung carcinoma
  JOURNAL   J Pathol Clin Res 10 (5), e70001 (2024)
   PUBMED   39283755
  REMARK    GeneRIF: The expression of YAP1 and other transcription factors
            contributes to lineage plasticity in combined small cell lung
            carcinoma.
REFERENCE   6  (residues 1 to 454)
  AUTHORS   Gaffney,C.J., Oka,T., Mazack,V., Hilman,D., Gat,U., Muramatsu,T.,
            Inazawa,J., Golden,A., Carey,D.J., Farooq,A., Tromp,G. and Sudol,M.
  TITLE     Identification, basic characterization and evolutionary analysis of
            differentially spliced mRNA isoforms of human YAP1 gene
  JOURNAL   Gene 509 (2), 215-222 (2012)
   PUBMED   22939869
REFERENCE   7  (residues 1 to 454)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   8  (residues 1 to 454)
  AUTHORS   Chen,H.I., Einbond,A., Kwak,S.J., Linn,H., Koepf,E., Peterson,S.,
            Kelly,J.W. and Sudol,M.
  TITLE     Characterization of the WW domain of human yes-associated protein
            and its polyproline-containing ligands
  JOURNAL   J Biol Chem 272 (27), 17070-17077 (1997)
   PUBMED   9202023
REFERENCE   9  (residues 1 to 454)
  AUTHORS   Chen,H.I. and Sudol,M.
  TITLE     The WW domain of Yes-associated protein binds a proline-rich ligand
            that differs from the consensus established for Src homology
            3-binding modules
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7819-7823 (1995)
   PUBMED   7644498
REFERENCE   10 (residues 1 to 454)
  AUTHORS   Sudol,M., Bork,P., Einbond,A., Kastury,K., Druck,T., Negrini,M.,
            Huebner,K. and Lehman,D.
  TITLE     Characterization of the mammalian YAP (Yes-associated protein) gene
            and its role in defining a novel protein module, the WW domain
  JOURNAL   J Biol Chem 270 (24), 14733-14741 (1995)
   PUBMED   7782338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001527.5, BC038235.1,
            HE864159.1, BC026212.2, AP000942.6, AL832620.2 and AI128142.1.
            
            On Aug 31, 2013 this sequence version replaced XP_005271443.1.
            
            Summary: This gene encodes a downstream nuclear effector of the
            Hippo signaling pathway which is involved in development, growth,
            repair, and homeostasis. This gene is known to play a role in the
            development and progression of multiple cancers as a
            transcriptional regulator of this signaling pathway and may
            function as a potential target for cancer treatment. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (5) lacks two alternate in-frame
            exons in the coding region, compared to variant 9. The encoded
            protein (isoform 5) represents the YAP1-1beta isoform described in
            Figure 3 of PMID: 22939869. It is shorter, compared to isoform 9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 22939869
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..454
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.1"
     Protein         1..454
                     /product="transcriptional coactivator YAP1 isoform 5"
                     /note="65 kDa Yes-associated protein; yorkie homolog;
                     yes-associated protein 2; protein yorkie homolog;
                     yes-associated protein YAP65 homolog; transcriptional
                     coactivator YAP1; Yes associated protein 1"
                     /calculated_mol_wt=48624
     Region          174..203
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(188,199)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     CDS             1..454
                     /gene="YAP1"
                     /gene_synonym="COB1; YAP; YAP-1; YAP2; YAP65; YKI"
                     /coded_by="NM_001282098.2:403..1767"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS60945.1"
                     /db_xref="GeneID:10413"
                     /db_xref="HGNC:HGNC:16262"
                     /db_xref="MIM:606608"
ORIGIN      
        1 mdpgqqpppq papqgqgqpp sqppqgqgpp sgpgqpapaa tqaapqappa ghqivhvrgd
       61 setdlealfn avmnpktanv pqtvpmrlrk lpdsffkppe pkshsrqast dagtagaltp
      121 qhvrahsspa slqlgavspg tltptgvvsg paatptaqhl rqssfeipdd vplpagwema
      181 ktssgqryfl nhidqtttwq dprkamlsqm nvtaptsppv qqnmmnsasa mnqrisqsap
      241 vkqppplapq spqggvmggs nsnqqqqmrl qqlqmekerl rlkqqellrq vrpqelalrs
      301 qlptleqdgg tqnpvsspgm sqelrtmttn ssdpflnsgt yhsrdestds glsmssysvp
      361 rtpddflnsv demdtgdtin qstlpsqqnr fpdyleaipg tnvdlgtleg dgmniegeel
      421 mpslqealss dilndmesvl aatkldkesf ltwl
//
LOCUS       NP_036433               1455 aa            linear   PRI 20-NOV-2025
DEFINITION  membrane-associated guanylate kinase, WW and PDZ domain-containing
            protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_036433
VERSION     NP_036433.2
DBSOURCE    REFSEQ: accession NM_012301.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1455)
  AUTHORS   Zhang,Z., Yi,Y., Wang,Z., Zhang,H., Zhao,Y., He,R., Luo,Y. and
            Cui,Z.
  TITLE     LncRNA MAGI2-AS3-Encoded Polypeptide Restrains the Proliferation
            and Migration of Breast Cancer Cells
  JOURNAL   Mol Biotechnol 66 (6), 1409-1423 (2024)
   PUBMED   37358745
  REMARK    GeneRIF: LncRNA MAGI2-AS3-Encoded Polypeptide Restrains the
            Proliferation and Migration of Breast Cancer Cells.
REFERENCE   2  (residues 1 to 1455)
  AUTHORS   Wang,T., Li,C., Wang,X. and Liu,F.
  TITLE     MAGI2 ameliorates podocyte apoptosis of diabetic kidney disease
            through communication with TGF-beta-Smad3/nephrin pathway
  JOURNAL   FASEB J 37 (12), e23305 (2023)
   PUBMED   37950637
  REMARK    GeneRIF: MAGI2 ameliorates podocyte apoptosis of diabetic kidney
            disease through communication with TGF-beta-Smad3/nephrin pathway.
REFERENCE   3  (residues 1 to 1455)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1455)
  AUTHORS   Thibord,F., Chan,M.V., Chen,M.H. and Johnson,A.D.
  TITLE     A year of COVID-19 GWAS results from the GRASP portal reveals
            potential genetic risk factors
  JOURNAL   HGG Adv 3 (2), 100095 (2022)
   PUBMED   35224516
REFERENCE   5  (residues 1 to 1455)
  AUTHORS   Zhang,W., Wang,R., Yuan,J., Li,B., Zhang,L., Wang,Y., Zhu,R.,
            Zhang,J. and Huyan,T.
  TITLE     The TLR4/NF-kappaB/MAGI-2 signaling pathway mediates postoperative
            delirium
  JOURNAL   Aging (Albany NY) 14 (6), 2590-2606 (2022)
   PUBMED   35294925
  REMARK    GeneRIF: The TLR4/NF-kappaB/MAGI-2 signaling pathway mediates
            postoperative delirium.
REFERENCE   6  (residues 1 to 1455)
  AUTHORS   Wu,X., Hepner,K., Castelino-Prabhu,S., Do,D., Kaye,M.B., Yuan,X.J.,
            Wood,J., Ross,C., Sawyers,C.L. and Whang,Y.E.
  TITLE     Evidence for regulation of the PTEN tumor suppressor by a
            membrane-localized multi-PDZ domain containing scaffold protein
            MAGI-2
  JOURNAL   Proc Natl Acad Sci U S A 97 (8), 4233-4238 (2000)
   PUBMED   10760291
REFERENCE   7  (residues 1 to 1455)
  AUTHORS   Shoji,H., Tsuchida,K., Kishi,H., Yamakawa,N., Matsuzaki,T., Liu,Z.,
            Nakamura,T. and Sugino,H.
  TITLE     Identification and characterization of a PDZ protein that interacts
            with activin type II receptors
  JOURNAL   J Biol Chem 275 (8), 5485-5492 (2000)
   PUBMED   10681527
REFERENCE   8  (residues 1 to 1455)
  AUTHORS   Ohtsuka,T., Hata,Y., Ide,N., Yasuda,T., Inoue,E., Inoue,T.,
            Mizoguchi,A. and Takai,Y.
  TITLE     nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G
            protein that interacts with synaptic scaffolding molecule (S-SCAM)
  JOURNAL   Biochem Biophys Res Commun 265 (1), 38-44 (1999)
   PUBMED   10548487
REFERENCE   9  (residues 1 to 1455)
  AUTHORS   Ide,N., Hata,Y., Deguchi,M., Hirao,K., Yao,I. and Takai,Y.
  TITLE     Interaction of S-SCAM with neural plakophilin-related
            Armadillo-repeat protein/delta-catenin
  JOURNAL   Biochem Biophys Res Commun 256 (3), 456-461 (1999)
   PUBMED   10080919
REFERENCE   10 (residues 1 to 1455)
  AUTHORS   Wood,J.D., Yuan,J., Margolis,R.L., Colomer,V., Duan,K., Kushi,J.,
            Kaminsky,Z., Kleiderlein,J.J., Sharp,A.H. and Ross,C.A.
  TITLE     Atrophin-1, the DRPLA gene product, interacts with two families of
            WW domain-containing proteins
  JOURNAL   Mol Cell Neurosci 11 (3), 149-160 (1998)
   PUBMED   9647693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004945.1, AF038563.1,
            AC007237.3, AB014605.2, AC004808.1, AA448362.1 and AC004990.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 31, 2002 this sequence version replaced NP_036433.1.
            
            Summary: The protein encoded by this gene interacts with
            atrophin-1. Atrophin-1 contains a polyglutamine repeat, expansion
            of which is responsible for dentatorubral and pallidoluysian
            atrophy. This encoded protein is characterized by two WW domains, a
            guanylate kinase-like domain, and multiple PDZ domains. It has
            structural similarity to the membrane-associated guanylate kinase
            homologue (MAGUK) family. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF038563.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: locus in the vicinity of
                                      disease-associated variant(s)
            MANE Ensembl match     :: ENST00000354212.9/ ENSP00000346151.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..1455
                     /product="membrane-associated guanylate kinase, WW and PDZ
                     domain-containing protein 2 isoform 1"
                     /note="activin receptor interacting protein 1;
                     membrane-associated guanylate kinase, WW and PDZ
                     domain-containing protein 2; atrophin-1-interacting
                     protein 1; atrophin-1-interacting protein A;
                     membrane-associated guanylate kinase inverted 2"
                     /calculated_mol_wt=158624
     Region          14..99
                     /region_name="PDZ0_MAGI-1_3-like"
                     /note="PDZ domain 0 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06730"
                     /db_xref="CDD:467212"
     Site            order(27..33,45,48,79,83,86..87)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467212"
     Region          118..291
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Region          205..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          302..381
                     /region_name="Interaction with DDN.
                     /evidence=ECO:0000269|PubMed:16464232"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          305..335
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(319,330)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          350..381
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVQ1; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Site            order(365,376)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          424..508
                     /region_name="PDZ1_MAGI-1_3-like"
                     /note="PDZ domain 1 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06731"
                     /db_xref="CDD:467213"
     Site            order(424,445..449,451,472,474,480,482..483,505,507..508)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467213"
     Site            order(435..441,453,456,486,490,493..494)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467213"
     Region          601..682
                     /region_name="PDZ2_MAGI-1_3-like"
                     /note="PDZ domain 2 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06732"
                     /db_xref="CDD:467214"
     Site            order(614..620,629,632,659,663,666..667)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467214"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88382; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          776..860
                     /region_name="PDZ3_MAGI-1_3-like"
                     /note="PDZ domain 3 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06733"
                     /db_xref="CDD:467215"
     Site            order(787..793,805,808,838,842,845..846)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467215"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVQ1; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          869..913
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL8.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88382; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88382; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          920..1008
                     /region_name="PDZ4_MAGI-1_3-like"
                     /note="PDZ domain 4 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06734"
                     /db_xref="CDD:467216"
     Site            order(930..936,955,958,988,992,995..996)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467216"
     Region          1011..1136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL8.3)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVQ1; propagated from
                     UniProtKB/Swiss-Prot (Q86UL8.3)"
     Region          1145..1227
                     /region_name="PDZ5_MAGI-1_3-like"
                     /note="PDZ domain 5 of membrane-associated guanylate
                     kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and
                     related domains; cd06735"
                     /db_xref="CDD:467217"
     Site            order(1156..1162,1174,1177,1207,1211,1214..1215)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467217"
     Region          1231..1455
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UL8.3)"
     CDS             1..1455
                     /gene="MAGI2"
                     /gene_synonym="ACVRIP1; AIP-1; AIP1; ARIP1; MAGI-2;
                     NPHS15; SSCAM"
                     /coded_by="NM_012301.4:348..4715"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5594.1"
                     /db_xref="GeneID:9863"
                     /db_xref="HGNC:HGNC:18957"
                     /db_xref="MIM:606382"
ORIGIN      
        1 mskslkkksh wtskvhesvi grnpegqlgf elkggaengq fpylgevkpg kvayesgskl
       61 vseelllevn etpvagltir dvlavikhck dplrlkcvkq ggivdkdlrh ylnlrfqkgs
      121 vdhelqqiir dnlylrtvpc ttrphkegev pgvdyifitv edfmeleksg allesgtyed
      181 nyygtpkppa epaplllnvt dqilpgatps aegkrkrnks vsnmekasie ppeeeeeerp
      241 vvngngvvvt pessehedks agasgempsq pypapvysqp eelkeqmddt kptkpednee
      301 pdplpdnwem aytekgevyf idhntkttsw ldprlakkak ppeeckenel pygwekiddp
      361 iygtyyvdhi nrrtqfenpv leakrklqqh nmphtelgtk plqapgfrek plftrdasql
      421 kgtflsttlk ksnmgfgfti iggdepdefl qvksvipdgp aaqdgkmetg dvivyinevc
      481 vlghthadvv klfqsvpigq svnlvlcrgy plpfdpedpa nsmvpplaim erpppvmvng
      541 rhnyetyley isrtsqsvpd itdrpphslh smptdgqldg typppvhddn vsmassgatq
      601 aelmtltivk gaqgfgftia dsptgqrvkq ildiqgcpgl cegdlivein qqnvqnlsht
      661 evvdilkdcp igsetsliih rggffspwkt pkpimdrwen qgspqtslsa paipqnlpfp
      721 palhrssfpd steafdprkp dpyelyeksr aiyesrqqvp prtsfrmdss gpdykeldvh
      781 lrrmesgfgf rilggdepgq piligaviam gsadrdgrlh pgdelvyvdg ipvagkthry
      841 vidlmhhaar ngqvnltvrr kvlcggepcp engrspgsvs thhssprsdy atytnsnhaa
      901 pssnasppeg fashslqtsd vvihrkeneg fgfviissln rpesgstitv phkigriidg
      961 spadrcaklk vgdrilavng qsiinmphad ivklikdagl svtlriipqe elnsptsaps
     1021 sekqspmaqq splaqqspla qpspatpnsp iaqpappqpl qlqghensyr sevkarqdvk
     1081 pdirqppftd yrqppldyrq ppggdyqqpp pldyrqppll dyrqhspdtr qyplsdyrqp
     1141 qdfdyftvdm ekgakgfgfs irggreykmd lyvlrlaedg pairngrmrv gdqiieinge
     1201 strdmthara ieliksggrr vrlllkrgtg qvpeydepap wsspaaaapg lpevgvsldd
     1261 glapfspshp appsdpshqi spgptwdikr ehdvrkpkel sacgqkkqrl geqrersasp
     1321 qraarprlee apggqgrpea grpasearap glaaadaada araggkeapr aaagselcrr
     1381 egpgaapafa gpggggsgal eaegragara gprpgprppg gaparkaava pgpwkvpgsd
     1441 klpsvlkpga saasr
//
LOCUS       NP_002792                273 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-10 [Homo sapiens].
ACCESSION   NP_002792
VERSION     NP_002792.1
DBSOURCE    REFSEQ: accession NM_002801.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Frantzeskakis,M., Takahama,Y. and Ohigashi,I.
  TITLE     The Role of Proteasomes in the Thymus
  JOURNAL   Front Immunol 12, 646209 (2021)
   PUBMED   33815406
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Mebratu,Y.A., Negasi,Z.H., Dutta,S., Rojas-Quintero,J. and
            Tesfaigzi,Y.
  TITLE     Adaptation of Proteasomes and Lysosomes to Cellular Environments
  JOURNAL   Cells 9 (10), 2221 (2020)
   PUBMED   33019542
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Foss,G.S., Larsen,F., Solheim,J. and Prydz,H.
  TITLE     Constitutive and interferon-gamma-induced expression of the human
            proteasome subunit multicatalytic endopeptidase complex-like 1
  JOURNAL   Biochim Biophys Acta 1402 (1), 17-28 (1998)
   PUBMED   9551082
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hisamatsu,H., Shimbara,N., Saito,Y., Kristensen,P., Hendil,K.B.,
            Fujiwara,T., Takahashi,E., Tanahashi,N., Tamura,T., Ichihara,A. and
            Tanaka,K.
  TITLE     Newly identified pair of proteasomal subunits regulated
            reciprocally by interferon gamma
  JOURNAL   J Exp Med 183 (4), 1807-1816 (1996)
   PUBMED   8666937
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Larsen,F., Solheim,J., Kristensen,T., Kolsto,A.B. and Prydz,H.
  TITLE     A tight cluster of five unrelated human genes on chromosome 16q22.1
  JOURNAL   Hum Mol Genet 2 (10), 1589-1595 (1993)
   PUBMED   8268911
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP289065.1 and BM981173.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. Proteolytic processing is
            required to generate a mature subunit. Expression of this gene is
            induced by gamma interferon, and this gene product replaces
            catalytic subunit 2 (proteasome beta 7 subunit) in the
            immunoproteasome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.276274.1,
                                           SRR1163655.467374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358514.9/ ENSP00000351314.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..273
                     /product="proteasome subunit beta type-10"
                     /EC_number="3.4.25.1"
                     /note="proteasome MECl-1; macropain subunit MECl-1;
                     multicatalytic endopeptidase complex subunit MECl-1;
                     proteasome catalytic subunit 2i; proteasome subunit beta
                     7i; proteasome subunit MECL1; proteasome subunit beta-2i;
                     low molecular mass protein 10; proteasome (prosome,
                     macropain) subunit, beta type, 10; proteasome subunit beta
                     10; proteasome subunit beta2i"
                     /calculated_mol_wt=28805
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P40306.1)"
     Site            39..40
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000250|UniProtKB:O35955; propagated from
                     UniProtKB/Swiss-Prot (P40306.1)"
     mat_peptide     40..273
                     /product="Proteasome subunit beta type-10.
                     /id=PRO_0000026652"
                     /note="propagated from UniProtKB/Swiss-Prot (P40306.1)"
                     /calculated_mol_wt=24648
     Region          40..227
                     /region_name="proteasome_beta_type_7"
                     /note="proteasome beta type-7 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03763"
                     /db_xref="CDD:239732"
     Site            order(40,56,58,72,168,205,208..209)
                     /site_type="active"
                     /db_xref="CDD:239732"
     Site            order(58,61,63..68,88,90,105,117,120..121,123..124,127,
                     130,153,155,157..160,163,171..172,174..175,178..180,196,
                     203..206,209..210)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239732"
     Site            230
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P40306.1)"
     Region          231..267
                     /region_name="Pr_beta_C"
                     /note="Proteasome beta subunits C terminal; pfam12465"
                     /db_xref="CDD:463597"
     CDS             1..273
                     /gene="PSMB10"
                     /gene_synonym="beta2i; IMD121; LMP10; MECL1; PRAAS5"
                     /coded_by="NM_002801.4:102..923"
                     /db_xref="CCDS:CCDS10853.1"
                     /db_xref="GeneID:5699"
                     /db_xref="HGNC:HGNC:9538"
                     /db_xref="MIM:176847"
ORIGIN      
        1 mlkpaleprg gfsfencqrn aslervlpgl kvpharktgt tiaglvfqdg vilgadtrat
       61 ndsvvadksc ekihfiapki yccgagvaad aemttrmvas kmelhalstg reprvatvtr
      121 ilrqtlfryq ghvgaslivg gvdltgpqly gvhphgsysr lpftalgsgq daalavledr
      181 fqpnmtleaa qgllveavta gilgdlgsgg nvdacvitkt gakllrtlss ptepvkrsgr
      241 yhfvpgttav ltqtvkpltl elveetvqam eve
//
LOCUS       NP_776171                171 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 9C isoform a [Homo sapiens].
ACCESSION   NP_776171
VERSION     NP_776171.1
DBSOURCE    REFSEQ: accession NM_173810.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 171)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 171)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 171)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 171)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   5  (residues 1 to 171)
  AUTHORS   Martins-de-Souza,D., Gattaz,W.F., Schmitt,A., Rewerts,C.,
            Maccarrone,G., Dias-Neto,E. and Turck,C.W.
  TITLE     Prefrontal cortex shotgun proteome analysis reveals altered calcium
            homeostasis and immune system imbalance in schizophrenia
  JOURNAL   Eur Arch Psychiatry Clin Neurosci 259 (3), 151-163 (2009)
   PUBMED   19165527
  REMARK    GeneRIF: Using shotgun mass spectrometry, we found this protein
            differentially expressed in the dorsolateral prefrontal cortex from
            patients with schizophrenia.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC032123.2.
            
            Transcript Variant: This variant (1) encodes isoform a. Variants 1,
            2, and 3 all encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032123.2, SRR1660803.105027.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316461.9/ ENSP00000325266.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..171
                     /product="tetratricopeptide repeat protein 9C isoform a"
                     /note="tetratricopeptide repeat protein 9C; TPR repeat
                     protein 9C"
                     /calculated_mol_wt=19882
     Region          2..>148
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          8..41
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          8..36
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(9,12..13,16..17,19,73,76..77,80..81,83..84,109,
                     112..113,116..117,120)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          45..103
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          72..107
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          108..141
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5M4.1)"
     Region          108..135
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          142..165
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..171
                     /gene="TTC9C"
                     /coded_by="NM_173810.4:364..879"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8033.1"
                     /db_xref="GeneID:283237"
                     /db_xref="HGNC:HGNC:28432"
ORIGIN      
        1 mekrlqeaql ykeegnqryr egkyrdavsr yhrallqlrg ldpslpsplp nlgpqgpalt
       61 peqenilhtt qtdcynnlaa cllqmepvny ervreysqkv lerqpdnaka lyragvaffh
      121 lqdydqarhy llaavnrqpk danvrrylql tqselssyhr kekqlylgmf g
//
LOCUS       NP_000994                114 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein P1 isoform 1 [Homo sapiens].
ACCESSION   NP_000994 NP_001074326
VERSION     NP_000994.1
DBSOURCE    REFSEQ: accession NM_001003.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Tripathi,M., Gauthier,K., Sandireddy,R., Zhou,J., Guptta,P.,
            Sakthivel,S., Teo,W.W., Naing,Y.T., Arul,K., Tikno,K., Park,S.H.,
            Wu,Y., Wang,L., Bay,B.H., Sun,L., Giguere,V., Chow,P.K.H.,
            Ghosh,S., McDonnell,D.P., Yen,P.M. and Singh,B.K.
  TITLE     Esrra regulates Rplp1-mediated translation of lysosome proteins
            suppressed in metabolic dysfunction-associated steatohepatitis and
            reversed by alternate day fasting
  JOURNAL   Mol Metab 87, 101997 (2024)
   PUBMED   39032642
  REMARK    GeneRIF: Esrra regulates Rplp1-mediated translation of lysosome
            proteins suppressed in metabolic dysfunction-associated
            steatohepatitis and reversed by alternate day fasting.
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Yang,W., Wang,H., Li,Z., Zhang,L., Liu,J., Kirchhoff,F., Huan,C.
            and Zhang,W.
  TITLE     RPLP1 restricts HIV-1 transcription by disrupting C/EBPbeta binding
            to the LTR
  JOURNAL   Nat Commun 15 (1), 5290 (2024)
   PUBMED   38906865
  REMARK    GeneRIF: RPLP1 restricts HIV-1 transcription by disrupting
            C/EBPbeta binding to the LTR.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Peterson,R., Minchella,P., Cui,W., Graham,A. and Nothnick,W.B.
  TITLE     RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro
  JOURNAL   Int J Mol Sci 24 (3), 2690 (2023)
   PUBMED   36769010
  REMARK    GeneRIF: RPLP1 Is Up-Regulated in Human Adenomyosis and Endometrial
            Adenocarcinoma Epithelial Cells and Is Essential for Cell Survival
            and Migration In Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Chan,S.H., Hung,F.S., Chan,D.S. and Shaw,P.C.
  TITLE     Trichosanthin interacts with acidic ribosomal proteins P0 and P1
            and mitotic checkpoint protein MAD2B
  JOURNAL   Eur J Biochem 268 (7), 2107-2112 (2001)
   PUBMED   11277934
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Tchorzewski,M., Boldyreff,B., Issinger,O.G. and Grankowski,N.
  TITLE     Analysis of the protein-protein interactions between the human
            acidic ribosomal P-proteins: evaluation by the two hybrid system
  JOURNAL   Int J Biochem Cell Biol 32 (7), 737-746 (2000)
   PUBMED   10856704
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol Cell Biol 7 (11), 4065-4074 (1987)
   PUBMED   3323886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC027237.8.
            
            On Mar 28, 2007 this sequence version replaced NP_001074326.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1
            protein can interact with P0 and P2 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. Two alternatively spliced transcript
            variants that encode different proteins have been observed. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This predominant variant (1) is the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP367167.1, SRR5189652.227177.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260379.11/ ENSP00000346037.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23"
     Protein         1..114
                     /product="large ribosomal subunit protein P1 isoform 1"
                     /note="60S acidic ribosomal protein P1; acidic ribosomal
                     phosphoprotein P1; ribosomal protein, large, P1; large
                     ribosomal subunit protein P1"
                     /calculated_mol_wt=11383
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P05386.1)"
     Region          6..>63
                     /region_name="Ribosomal_P1"
                     /note="Ribosomal protein P1. This subfamily represents the
                     eukaryotic large ribosomal protein P1. Eukaryotic P1 and
                     P2 are functionally equivalent to the bacterial protein
                     L7/L12, but are not homologous to L7/L12. P1 is located in
                     the L12 stalk, with proteins...; cd05831"
                     /db_xref="CDD:100109"
     Region          69..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05386.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14997482,
                     ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P05386.1)"
     CDS             1..114
                     /gene="RPLP1"
                     /gene_synonym="LP1; P1; RPP1"
                     /coded_by="NM_001003.3:132..476"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10233.1"
                     /db_xref="GeneID:6176"
                     /db_xref="HGNC:HGNC:10372"
                     /db_xref="MIM:180520"
ORIGIN      
        1 masvselaci ysalilhdde vtvtedkina likaagvnve pfwpglfaka lanvnigsli
       61 cnvgaggpap aagaapaggp apstaaapae ekkveakkee seesdddmgf glfd
//
LOCUS       NP_001138424            2172 aa            linear   PRI 20-NOV-2025
DEFINITION  protein sidekick-2 precursor [Homo sapiens].
ACCESSION   NP_001138424
VERSION     NP_001138424.1
DBSOURCE    REFSEQ: accession NM_001144952.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2172)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2172)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 2172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 2172)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2172)
  AUTHORS   Otowa,T., Yoshida,E., Sugaya,N., Yasuda,S., Nishimura,Y., Inoue,K.,
            Tochigi,M., Umekage,T., Miyagawa,T., Nishida,N., Tokunaga,K.,
            Tanii,H., Sasaki,T., Kaiya,H. and Okazaki,Y.
  TITLE     Genome-wide association study of panic disorder in the Japanese
            population
  JOURNAL   J Hum Genet 54 (2), 122-126 (2009)
   PUBMED   19165232
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 2172)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
REFERENCE   7  (residues 1 to 2172)
  AUTHORS   Kaufman,L., Hayashi,K., Ross,M.J., Ross,M.D. and Klotman,P.E.
  TITLE     Sidekick-1 is upregulated in glomeruli in HIV-associated
            nephropathy
  JOURNAL   J Am Soc Nephrol 15 (7), 1721-1730 (2004)
   PUBMED   15213259
REFERENCE   8  (residues 1 to 2172)
  AUTHORS   Fu,G.K., Wang,J.T., Yang,J., Au-Young,J. and Stuve,L.L.
  TITLE     Circular rapid amplification of cDNA ends for high-throughput
            extension cloning of partial genes
  JOURNAL   Genomics 84 (1), 205-210 (2004)
   PUBMED   15203218
REFERENCE   9  (residues 1 to 2172)
  AUTHORS   Yamagata,M., Weiner,J.A. and Sanes,J.R.
  TITLE     Sidekicks: synaptic adhesion molecules that promote lamina-specific
            connectivity in the retina
  JOURNAL   Cell 110 (5), 649-660 (2002)
   PUBMED   12230981
REFERENCE   10 (residues 1 to 2172)
  AUTHORS   Nguyen,D.N., Liu,Y., Litsky,M.L. and Reinke,R.
  TITLE     The sidekick gene, a member of the immunoglobulin superfamily, is
            required for pattern formation in the Drosophila eye
  JOURNAL   Development 124 (17), 3303-3312 (1997)
   PUBMED   9310325
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC032019.7, AC124804.10, AC087301.8, AB040947.1 and BC066363.1.
            
            Summary: The protein encoded by this gene is a member of the
            immunoglobulin superfamily. The protein contains two immunoglobulin
            domains and thirteen fibronectin type III domains. Fibronectin type
            III domains are present in both extracellular and intracellular
            proteins and tandem repeats are known to contain binding sites for
            DNA, heparin and the cell surface. This protein, and a homologous
            mouse sequence, are very similar to the Drosophila sidekick gene
            product but the specific function of this superfamily member is not
            yet known. Evidence for alternative splicing at this gene locus has
            been observed but the full-length nature of additional variants has
            not yet been determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments and orthologous data.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000392650.8/ ENSP00000376421.3
            RefSeq Select criteria    :: based on conservation, expression,
                                         longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..2172
                     /product="protein sidekick-2 precursor"
                     /note="protein sidekick-2; sidekick homolog 2"
                     /calculated_mol_wt=237081
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2334
     mat_peptide     21..2172
                     /product="Protein sidekick-2. /id=PRO_0000226978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
                     /calculated_mol_wt=237081
     Region          26..95
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          121..197
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          130..134
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          144..148
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          166..170
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          180..185
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          193..196
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            193
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          233..286
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          233..237
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          248..252
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          267..271
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          281..286
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          308..397
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          326..330
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          339..343
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          363..367
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          377..382
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          390..393
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          404..492
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          419..423
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          432..436
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          458..462
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          472..477
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          485..488
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          497..571
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          <596..1028
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            609
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Site            743
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Site            936
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Site            948
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          960..>1337
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            1102
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          1188..>1522
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          1504..1608
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; smart00060"
                     /db_xref="CDD:214495"
     Region          <1577..1932
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            1670
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          1707..1729
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
     Site            1933..1953
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          2039..2067
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          2098..2172
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
     Region          2166..2172
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:Q6V4S5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q58EX2.3)"
     CDS             1..2172
                     /gene="SDK2"
                     /coded_by="NM_001144952.2:358..6876"
                     /db_xref="CCDS:CCDS45769.1"
                     /db_xref="GeneID:54549"
                     /db_xref="HGNC:HGNC:19308"
                     /db_xref="MIM:607217"
ORIGIN      
        1 mwglliwtll alhqiraara qddvspyfkt epvrtqvhle gnrlvltcma egswplefkw
       61 lhnnreltkf sleyrymits ldrthagfyr civrnrmgal lqrqtevqva ymgsfeegek
      121 hqsvshgeaa virapriasf pqpqvtwfrd grkippssri aitlentlvi lstvapdagr
      181 yyvqavndkn gdnktsqpit ltvenvggpa dpiaptiiip pkntsvvagt sevtlecvan
      241 arpliklhii wkkdgvllsg gisdhnrrlt ipnptgsdag yyeceavlrs ssvpsvvrga
      301 ylsvleppqf vkeperhita emekvvdipc qakgvpppsi twykdaavve vekltrfrqr
      361 ndgglqisgl vpddtgmfqc farnaagevq tstylavtsi apnitrgpld stvidgmsvv
      421 lacetsgapr paitwqkger ilasgsvqlp rftplesgsl lispthisda gtytclatns
      481 rgvdeasadl vvwartritk ppqdqsvikg tqasmvcgvt hdprvtiryi wekdgatlgt
      541 eshprirldr ngslhisqtw sgdigtytcr visaggndsr sahlrvrqlp hapehpvatl
      601 stverrainl twtkpfdgns pliryilems ennapwtvll asvdpkatsv tvkglvpars
      661 yqfrlcavnd vgkgqfskdt ervslpeepp tappqnvias grtnqsimiq wqpppeshqn
      721 gilkgyiiry claglpvgyq fknitdadvn nllledliiw tnyeievaay nsaglgvyss
      781 kvtewtlqgv ptvppgnvha eatnsttirf twnapspqfi nginqgykli awepeqeeev
      841 tmvtarpnfq dsihvgfvsg lkkfteyfts vlcfttpgdg prstpqlvrt hedvpgpvgh
      901 lsfseildts lkvswqepge kngiltgyri sweeynrtnt rvthylpnvt leyrvtglta
      961 lttytievaa mtskgqgqvs astissgvpp elpgpptnlg isnigprsvt lqfrpgydgk
     1021 tsisrwlvea qvgvvgegee wllihqlsne pdarsmevpd lnpftcysfr mrqvnivgts
     1081 ppsqpsrkiq tlqappdmap anvslrtase tslwlrwmpl pemeyngnpe svgykikysr
     1141 sdghgktlsh vvqdrverdy tiedleewte yrvqvqafna igsgpwsqtv vgrtresvps
     1201 sgptnvsala ttsssmlvrw sevpeadrng lvlgykvmyk ekdsdtqprf wlvegnssrs
     1261 aqltglgkyv lyevqvlaft rigdgspshp pilertlddv pgppmgilfp evrttsvrli
     1321 wqppaapngi ilayqithrl ntttantatv evlapsarqy tatglkpesv ylfritaqtr
     1381 kgwgeaaeal vvttekrdrp qppsrpmvqq edvrarsvll swepgsdgls pvryytiqtr
     1441 elpsgrwalh sasvshnass fivdrlkpft sykfrvkatn digdsefsee seslttlqaa
     1501 pdeaptilsv tphtttsvli rwqppaedki ngillgfrir yrellyeglr gftlrginnp
     1561 gatwaeltsm ysmrnlsrps ltqyeldnln khrryeirms vynavgegps sppqevfvge
     1621 avptaaprnv vvhgatatql dvtwepppld sqngdiqgyk iyfweaqrgn ltervktlfl
     1681 aensvklknl tgytaymvsv aafnaagdgp rstptqgqtq qaapsapssv kfseltttsv
     1741 nvsweapqfp ngilegyrlv yepcspvdgv skivtvdvkg nsplwlkvkd laegvtyrfr
     1801 iraktftygp eieanvttgp gegapgppgv piivryssai aihwssgdpg kgpitryvie
     1861 arpsdeglwd ilikdipkev ssytfsmdil kpgvsydfrv iavndygfgt psspsqsvpa
     1921 qkanpfyeew wflvvialvg lifilllvfv liirgqskky akktdsgnsa ksgalghsem
     1981 msldessfpa lelnnrrlsv knsfcrkngl ytrspprpsp gslhysdedv tkyndlipae
     2041 sssltekpse isdsqgsdse yevdsnhqka hsfvnhyisd ptyynswrrq qkgisraqay
     2101 sytesdsgep dhttvtnsts tqqgslfrpk asrtptpqnp pnppsqqstl yrppsslapg
     2161 srapiagfss fv
//
LOCUS       NP_003331                147 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D3 isoform 1 [Homo sapiens].
ACCESSION   NP_003331
VERSION     NP_003331.1
DBSOURCE    REFSEQ: accession NM_003340.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Yalcin,Z., Koot,D., Bezstarosti,K., Salas-Lloret,D.,
            Bleijerveld,O.B., Boersma,V., Falcone,M., Gonzalez-Prieto,R.,
            Altelaar,M., Demmers,J.A.A. and Jacobs,J.J.L.
  TITLE     Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control
  JOURNAL   Mol Cell Proteomics 22 (6), 100548 (2023)
   PUBMED   37059365
  REMARK    GeneRIF: Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control.
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jiang,C., Dai,X., He,S., Zhou,H., Fang,L., Guo,J., Liu,S.,
            Zhang,T., Pan,W., Yu,H., Fu,T., Li,D., Inuzuka,H., Wang,P., Xiao,J.
            and Wei,W.
  TITLE     Ring domains are essential for GATOR2-dependent mTORC1 activation
  JOURNAL   Mol Cell 83 (1), 74-89 (2023)
   PUBMED   36528027
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Ray,P., Nancarrow,D.J., Ferrer-Torres,D., Wang,Z., San Martinho,M.,
            Hinton,T., Wu,J.H., Wu,A., Turgeon,D.K., Hammer,M.A., Dame,M.K.,
            Lawrence,T.S., O'Brien,P.J., Spence,J.R., Beer,D.G. and Ray,D.
  TITLE     UBCH5 Family Members Differentially Impact Stabilization of Mutant
            p53 via RNF128 Iso1 During Barrett's Progression to Esophageal
            Adenocarcinoma
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (1), 129-149 (2022)
   PUBMED   34416429
  REMARK    GeneRIF: UBCH5 Family Members Differentially Impact Stabilization
            of Mutant p53 via RNF128 Iso1 During Barrett's Progression to
            Esophageal Adenocarcinoma.
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Rogakou,E.P., Pilch,D.R., Orr,A.H., Ivanova,V.S. and Bonner,W.M.
  TITLE     DNA double-stranded breaks induce histone H2AX phosphorylation on
            serine 139
  JOURNAL   J Biol Chem 273 (10), 5858-5868 (1998)
   PUBMED   9488723
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Jensen,J.P., Bates,P.W., Yang,M., Vierstra,R.D. and Weissman,A.M.
  TITLE     Identification of a family of closely related human ubiquitin
            conjugating enzymes
  JOURNAL   J Biol Chem 270 (51), 30408-30414 (1995)
   PUBMED   8530467
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Scheffner,M., Huibregtse,J.M. and Howley,P.M.
  TITLE     Identification of a human ubiquitin-conjugating enzyme that
            mediates the E6-AP-dependent ubiquitination of p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 8797-8801 (1994)
   PUBMED   8090726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM750658.1, DA557036.1,
            BC003395.1, AC018797.4 and BM967209.1.
            
            Summary: The modification of proteins with ubiquitin is an
            important cellular mechanism for targeting abnormal or short-lived
            proteins for degradation. Ubiquitination involves at least three
            classes of enzymes: ubiquitin-activating enzymes, or E1s,
            ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein
            ligases, or E3s. This gene encodes a member of the E2
            ubiquitin-conjugating enzyme family. This enzyme functions in the
            ubiquitination of the tumor-suppressor protein p53, which is
            induced by an E3 ubiquitin-protein ligase. [provided by RefSeq, Jan
            2017].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.237277.1,
                                           SRR1803611.223812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D3 isoform 1"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog,
                     yeast); ubiquitin-conjugating enzyme E2-17 kDa 3;
                     ubiquitin-protein ligase D3; ubiquitin carrier protein D3;
                     ubiquitin-conjugating enzyme E2(17)KB 3; ubiquitin
                     conjugating enzyme E2D 3; E2 ubiquitin-conjugating enzyme
                     D3; (E3-independent) E2 ubiquitin-conjugating enzyme D3;
                     ubiquitin-conjugating enzyme E2D 3 (homologous to yeast
                     UBC4/5)"
                     /calculated_mol_wt=16556
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="UBE2D3"
                     /gene_synonym="E2(17)KB3; UBC4/5; UBCH5C"
                     /coded_by="NM_003340.6:486..929"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3660.1"
                     /db_xref="GeneID:7323"
                     /db_xref="HGNC:HGNC:12476"
                     /db_xref="MIM:602963"
ORIGIN      
        1 malkrinkel sdlardppaq csagpvgddm fhwqatimgp ndspyqggvf fltihfptdy
       61 pfkppkvaft triyhpnins ngsicldilr sqwspaltis kvllsicsll cdpnpddplv
      121 peiariyktd rdkynrisre wtqkyam
//
LOCUS       NP_001352645             767 aa            linear   PRI 20-NOV-2025
DEFINITION  DISP complex protein LRCH3 isoform 4 [Homo sapiens].
ACCESSION   NP_001352645 XP_005269422
VERSION     NP_001352645.1
DBSOURCE    REFSEQ: accession NM_001365716.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 767)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 767)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 767)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 767)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 767)
  AUTHORS   O'Loughlin,T., Masters,T.A. and Buss,F.
  TITLE     The MYO6 interactome reveals adaptor complexes coordinating early
            endosome and cytoskeletal dynamics
  JOURNAL   EMBO Rep 19 (4) (2018)
   PUBMED   29467281
REFERENCE   6  (residues 1 to 767)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 767)
  AUTHORS   Foussard,H., Ferrer,P., Valenti,P., Polesello,C., Carreno,S. and
            Payre,F.
  TITLE     LRCH proteins: a novel family of cytoskeletal regulators
  JOURNAL   PLoS One 5 (8), e12257 (2010)
   PUBMED   20805893
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 767)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055764.23, AC144530.11 and AC135893.2.
            
            On Sep 12, 2018 this sequence version replaced XP_005269422.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.231164.1,
                                           SRR1660809.6191.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..767
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..767
                     /product="DISP complex protein LRCH3 isoform 4"
                     /note="leucine-rich repeat and calponin homology
                     domain-containing protein 3; leucine-rich repeats and
                     calponin homology (CH) domain containing 3; DISP complex
                     protein LRCH3"
                     /calculated_mol_wt=84895
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <80..>286
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..145
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          618..727
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Site            order(626,681,683..684,687..688,690,704..708,715,717..718,
                     720..721,724..725)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409119"
     CDS             1..767
                     /gene="LRCH3"
                     /coded_by="NM_001365716.1:26..2329"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:84859"
                     /db_xref="HGNC:HGNC:28637"
ORIGIN      
        1 maaaglvava aaaeysgtva sggnlpgvhc gpssgagpgf gpgswsrsld raleeaavtg
       61 vlslsgrklr efprgaanhd ltdttradls rnrlseipie achfvslenl nlyqnciryi
      121 peailnlqal tflnisrnql stlpvhlcnl plkvliasnn klvslpeeig hlrhlmeldv
      181 scneiqtips qignlealrd lnvrrnhlvh lpeelaelpl irldfscnki ttipvcyrnl
      241 rhlqtitldn nplqsppaqi cikgkvhifk ylniqackia pdlpdydrrp lgfgscheel
      301 yssrpygald sgfnsvdsgd krwsgneptd efsdlplrva eitkeqrlrr esqyqenrgs
      361 lvvtnggveh dldqidyids ctaeeeeaev rqpkgpdpds lssqfmayie qrrishegsp
      421 vkpvairefq ktedmrrylh qnrvpaepss llslsashnq lshtdlelhq rreqlvertr
      481 reaqlaalqy eeekirtkqi qrdavldfvk qkasqspqkq hplldgvdge cpfpsrrsqh
      541 tddsalcmsl sglnqvgcaa tlphssaftp lksddrpnal lsspatetgh asplppsaap
      601 ttdstdsitg qnsrqreeel elidqlrkhi eyrlkvslpc dlgaaltdgv vlchlanhvr
      661 prsvpsihvp spavpkltma kcrrnvenfl eacrkigvpq dnlcspsdil qlnlsvkrtv
      721 etllslgahs eessfvclsl qllgfvafyc tvmltlcvly ywlfpar
//
LOCUS       NP_115708                315 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat domain-containing protein 83 [Homo sapiens].
ACCESSION   NP_115708
VERSION     NP_115708.1
DBSOURCE    REFSEQ: accession NM_032332.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Kournoutis,A., Lamark,T., Johansen,T. and Abudu,Y.P.
  TITLE     WDR83/MORG1 inhibits RRAG GTPase-MTORC1 signaling to facilitate
            basal autophagy
  JOURNAL   Autophagy 20 (7), 1687-1688 (2024)
   PUBMED   38450633
  REMARK    GeneRIF: WDR83/MORG1 inhibits RRAG GTPase-MTORC1 signaling to
            facilitate basal autophagy.
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Bondeva,T. and Wolf,G.
  TITLE     Cloning of the Human MORG1 Promoter: Differential Regulation by
            Hypoxia and Prolyl-Hydroxylase Inhibitors
  JOURNAL   Genes (Basel) 13 (3), 427 (2022)
   PUBMED   35327980
  REMARK    GeneRIF: Cloning of the Human MORG1 Promoter: Differential
            Regulation by Hypoxia and Prolyl-Hydroxylase Inhibitors.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 315)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 315)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 315)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   7  (residues 1 to 315)
  AUTHORS   Hopfer,U., Hopfer,H., Jablonski,K., Stahl,R.A. and Wolf,G.
  TITLE     The novel WD-repeat protein Morg1 acts as a molecular scaffold for
            hypoxia-inducible factor prolyl hydroxylase 3 (PHD3)
  JOURNAL   J Biol Chem 281 (13), 8645-8655 (2006)
   PUBMED   16407229
  REMARK    GeneRIF: Functional characterization of the homologous rat gene.
REFERENCE   8  (residues 1 to 315)
  AUTHORS   Vomastek,T., Schaeffer,H.J., Tarcsafalvi,A., Smolkin,M.E.,
            Bissonette,E.A. and Weber,M.J.
  TITLE     Modular construction of a signaling scaffold: MORG1 interacts with
            components of the ERK cascade and links ERK signaling to specific
            agonists
  JOURNAL   Proc Natl Acad Sci U S A 101 (18), 6981-6986 (2004)
   PUBMED   15118098
  REMARK    GeneRIF: Component of a modular scaffold system that participates
            in the regulation of agonist-specific ERK signaling.
REFERENCE   9  (residues 1 to 315)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
  REMARK    GeneRIF: Includes the identification of this protein in C complex
            spliceosomes.
REFERENCE   10 (residues 1 to 315)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB143206.1 and BC005870.2.
            
            Summary: This gene encodes a member of the WD-40 protein family.
            The protein is proposed to function as a molecular scaffold for
            various multimeric protein complexes. The protein associates with
            several components of the extracellular signal-regulated kinase
            (ERK) pathway, and promotes ERK activity in response to serum or
            other signals. The protein also interacts with egl nine homolog 3
            (EGLN3, also known as PHD3) and regulates expression of
            hypoxia-inducible factor 1, and has been purified as part of the
            spliceosome. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter and 5' UTR, compared to variant 1. Both variants 1 and 2
            encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC005870.2, AK223195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..315
                     /product="WD repeat domain-containing protein 83"
                     /note="mitogen-activated protein kinase organizer 1; MAPK
                     organizer 1"
                     /calculated_mol_wt=34212
     Region          18..295
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          23..62
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Site            order(24,42,46,52..53,65..66,84,88,94..95,107..108,125,
                     130,136..137,152,167,172,178..179,191,208,212,218..219,
                     231..232,251,256,262..263,275..276,294)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          30..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          65..104
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          71..107
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..146
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          112..150
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          151..188
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          157..187
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          190..228
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          194..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          231..272
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          238..272
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          275..313
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRX9.1)"
     Region          279..303
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..315
                     /gene="WDR83"
                     /gene_synonym="MORG1"
                     /coded_by="NM_032332.4:39..986"
                     /db_xref="CCDS:CCDS12275.1"
                     /db_xref="GeneID:84292"
                     /db_xref="HGNC:HGNC:32672"
                     /db_xref="MIM:616850"
ORIGIN      
        1 mafpepkprp pelpqkrlkt ldcgqgavra vrfnvdgnyc ltcgsdktlk lwnplrgtll
       61 rtysghgyev ldaagsfdns slcsgggdka vvlwdvasgq vvrkfrghag kvntvqfnee
      121 atvilsgsid ssircwdcrs rrpepvqtld eardgvssvk vsdheilags vdgrvrrydl
      181 rmgqlfsdyv gspitctcfs rdgqctlvss ldstlrlldk dtgellgeyk ghknqeykld
      241 cclserdthv vscsedgkvf fwdlvegala lalpvgsgvv qslayhptep clltamggsv
      301 qcwreeayea edgag
//
LOCUS       NP_006417                572 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydropyrimidinase-related protein 4 [Homo sapiens].
ACCESSION   NP_006417
VERSION     NP_006417.2
DBSOURCE    REFSEQ: accession NM_006426.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Qiu,L., Sheng,P. and Wang,X.
  TITLE     Identification of Metabolic Syndrome-Related miRNA-mRNA Regulatory
            Networks and Key Genes Based on Bioinformatics Analysis
  JOURNAL   Biochem Genet 61 (1), 428-447 (2023)
   PUBMED   35877019
  REMARK    GeneRIF: Identification of Metabolic Syndrome-Related miRNA-mRNA
            Regulatory Networks and Key Genes Based on Bioinformatics Analysis.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Nagano,H., Hashimoto,N., Nakayama,A., Suzuki,S., Miyabayashi,Y.,
            Yamato,A., Higuchi,S., Fujimoto,M., Sakuma,I., Beppu,M.,
            Yokoyama,M., Suzuki,Y., Sugano,S., Ikeda,K., Tatsuno,I., Manabe,I.,
            Yokote,K., Inoue,S. and Tanaka,T.
  TITLE     p53-inducible DPYSL4 associates with mitochondrial supercomplexes
            and regulates energy metabolism in adipocytes and cancer cells
  JOURNAL   Proc Natl Acad Sci U S A 115 (33), 8370-8375 (2018)
   PUBMED   30061407
  REMARK    GeneRIF: DPYSL4 plays a key role in the tumor-suppressor function
            of p53 by regulating oxidative phosphorylation and the cellular
            energy supply via its association with mitochondrial
            supercomplexes, possibly linking to the pathophysiology of both
            cancer and obesity.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Fukada,M., Watakabe,I., Yuasa-Kawada,J., Kawachi,H., Kuroiwa,A.,
            Matsuda,Y. and Noda,M.
  TITLE     Molecular characterization of CRMP5, a novel member of the
            collapsin response mediator protein family
  JOURNAL   J Biol Chem 275 (48), 37957-37965 (2000)
   PUBMED   10956643
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Inatome,R., Tsujimura,T., Hitomi,T., Mitsui,N., Hermann,P.,
            Kuroda,S., Yamamura,H. and Yanagi,S.
  TITLE     Identification of CRAM, a novel unc-33 gene family protein that
            associates with CRMP3 and protein-tyrosine kinase(s) in the
            developing rat brain
  JOURNAL   J Biol Chem 275 (35), 27291-27302 (2000)
   PUBMED   10851247
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Honnorat,J., Byk,T., Kusters,I., Aguera,M., Ricard,D., Rogemond,V.,
            Quach,T., Aunis,D., Sobel,A., Mattei,M.G., Kolattukudy,P.,
            Belin,M.F. and Antoine,J.C.
  TITLE     Ulip/CRMP proteins are recognized by autoantibodies in
            paraneoplastic neurological syndromes
  JOURNAL   Eur J Neurosci 11 (12), 4226-4232 (1999)
   PUBMED   10594648
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Byk,T., Ozon,S. and Sobel,A.
  TITLE     The Ulip family phosphoproteins--common and specific properties
  JOURNAL   Eur J Biochem 254 (1), 14-24 (1998)
   PUBMED   9652388
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Hamajima,N., Matsuda,K., Sakata,S., Tamaki,N., Sasaki,M. and
            Nonaka,M.
  TITLE     A novel gene family defined by human dihydropyrimidinase and three
            related proteins with differential tissue distribution
  JOURNAL   Gene 180 (1-2), 157-163 (1996)
   PUBMED   8973361
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL512622.9, BC029280.1, BC136329.1 and BC142974.1.
            
            On Jun 12, 2008 this sequence version replaced NP_006417.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because transcript sequence consistent with
            the reference genome assembly was not available for all regions of
            the RefSeq transcript. The extent of this transcript is supported
            by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.112042.1, BC142974.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338492.9/ ENSP00000339850.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.3"
     Protein         1..572
                     /product="dihydropyrimidinase-related protein 4"
                     /note="CRMP-3; ULIP-4; UNC33-like phosphoprotein 4;
                     collapsin response mediator protein 3"
                     /calculated_mol_wt=61747
     Region          17..466
                     /region_name="D-HYD"
                     /note="D-hydantoinases (D-HYD) also called
                     dihydropyrimidases (DHPase) and related proteins; DHPases
                     are a family of enzymes that catalyze the reversible
                     hydrolytic ring opening of the amide bond in five- or
                     six-membered cyclic diamides, like dihydropyrimidine...;
                     cd01314"
                     /db_xref="CDD:238639"
     Site            order(28..29,31,44..45,180,201,204,207,230,234,238,241,
                     268..269,271..272,390,395,400)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:238639"
     Site            order(73,75,165,198,254,332)
                     /site_type="active"
                     /db_xref="CDD:238639"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35098; propagated from
                     UniProtKB/Swiss-Prot (O14531.2)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35098; propagated from
                     UniProtKB/Swiss-Prot (O14531.2)"
     CDS             1..572
                     /gene="DPYSL4"
                     /gene_synonym="CRMP3; DRP-4; ULIP4"
                     /coded_by="NM_006426.3:117..1835"
                     /db_xref="CCDS:CCDS7665.1"
                     /db_xref="GeneID:10570"
                     /db_xref="HGNC:HGNC:3016"
                     /db_xref="MIM:608407"
ORIGIN      
        1 msfqgkksip ritsdrllir ggrivnddqs fyadvhvedg likqigenli vpggiktida
       61 hglmvlpggv dvhtrlqmpv lgmtpaddfc qgtkaalagg ttmildhvfp dtgvsllaay
      121 eqwreradsa accdyslhvd itrwhesike elealvkekg vnsflvfmay kdrcqcsdsq
      181 myeifsiird lgalaqvhae ngdiveeeqk rllelgitgp eghvlshpee veaeavyrav
      241 tiakqancpl yvtkvmskga adaiaqakrr gvvvfgepit aslgtdgshy wsknwakaaa
      301 fvtsppvnpd pttadhltcl lssgdlqvtg sahctfttaq kavgkdnfal ipegtngiee
      361 rmsmvwekcv asgkmdenef vavtstnaak ifnfyprkgr vavgsdadlv iwnpkatkii
      421 sakthnlnve ynifegvecr gapavvisqg rvaledgkmf vtpgagrfvp rktfpdfvyk
      481 rikarnrlae ihgvprglyd gpvhevmvpa kpgsgapara scpgkisvpp vrnlhqsgfs
      541 lsgsqaddhi arrtaqkima ppggrsnits ls
//
LOCUS       NP_001274065             423 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 14 isoform c [Homo sapiens].
ACCESSION   NP_001274065 XP_005250494
VERSION     NP_001274065.1
DBSOURCE    REFSEQ: accession NM_001287136.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Zhao,Y., Chen,L., Xiang,Q., Lin,J., Jiang,S. and Li,W.
  TITLE     N6-methyladenosine-modified circCDK14 promotes ossification of the
            ligamentum flavum via epigenetic modulation by targeting AFF4
  JOURNAL   Cell Mol Life Sci 81 (1), 436 (2024)
   PUBMED   39414635
  REMARK    GeneRIF: N6-methyladenosine-modified circCDK14 promotes
            ossification of the ligamentum flavum via epigenetic modulation by
            targeting AFF4.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Parmasad,J.A., Ricke,K.M., Nguyen,B., Stykel,M.G., Buchner-Duby,B.,
            Bruce,A., Geertsma,H.M., Lian,E., Lengacher,N.A., Callaghan,S.M.,
            Joselin,A., Tomlinson,J.J., Schlossmacher,M.G., Stanford,W.L.,
            Ma,J., Brundin,P., Ryan,S.D. and Rousseaux,M.W.C.
  TITLE     Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy
  JOURNAL   Cell Death Dis 15 (4), 246 (2024)
   PUBMED   38575601
  REMARK    GeneRIF: Genetic and pharmacological reduction of CDK14 mitigates
            synucleinopathy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Zhang,M., Kan,D., Zhang,B., Chen,X., Wang,C., Chen,S., Gao,W.,
            Yang,Z., Li,Y., Chen,Y., Zhu,S., Wen,S., Niu,Y. and Shang,Z.
  TITLE     P300/SP1 complex mediating elevated METTL1 regulates CDK14 mRNA
            stability via internal m7G modification in CRPC
  JOURNAL   J Exp Clin Cancer Res 42 (1), 215 (2023)
   PUBMED   37599359
  REMARK    GeneRIF: P300/SP1 complex mediating elevated METTL1 regulates CDK14
            mRNA stability via internal m7G modification in CRPC.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Yang,T., Gao,Y.K. and Chen,J.Y.
  TITLE     KIAA0202, a human septin family member, interacting with hPFTAIRE1
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (4),
            520-525 (2002)
   PUBMED   12098780
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Yang,T. and Chen,J.Y.
  TITLE     Identification and cellular localization of human PFTAIRE1
  JOURNAL   Gene 267 (2), 165-172 (2001)
   PUBMED   11313143
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Lazzaro,M.A., Albert,P.R. and Julien,J.P.
  TITLE     A novel cdc2-related protein kinase expressed in the nervous system
  JOURNAL   J Neurochem 69 (1), 348-364 (1997)
   PUBMED   9202329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC325068.1, AK295086.1, AK316026.1, BC136477.1, BP336072.1,
            DB476188.1, AB020641.1, BM740394.1 and BC152436.1.
            
            On Nov 27, 2013 this sequence version replaced XP_005250494.1.
            
            Transcript Variant: This variant (3) contains alternate 5' exon
            structure and it thus differs in the 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (c) is shorter at the N-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.24171.1,
                                           SRR1803612.77613.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.13"
     Protein         1..423
                     /product="cyclin-dependent kinase 14 isoform c"
                     /EC_number="2.7.11.22"
                     /note="PFTAIRE protein kinase 1; cell division protein
                     kinase 14; serine/threonine-protein kinase PFTAIRE-1"
                     /calculated_mol_wt=47629
     Region          83..385
                     /region_name="STKc_PFTAIRE1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     PFTAIRE-1 kinase; cd07869"
                     /db_xref="CDD:143374"
     Site            order(95..98,103,116,118,134,148,164..167,170,172..173,
                     210,212,214..215,217,228,231,243,245..248,250,288..289)
                     /site_type="active"
                     /db_xref="CDD:143374"
     Site            order(95..98,103,116,118,148,164..167,170,173,214..215,
                     217,228)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:143374"
     Site            order(126..128,130,133..134,136..137,140..141,153,155,160,
                     199,202..205,233,235..238,242..243,359,363..365)
                     /site_type="other"
                     /note="putative CDK/cyclin interface [polypeptide
                     binding]"
                     /db_xref="CDD:143374"
     Site            order(134,172,210,212,231,243,245..248,250,288..289)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:143374"
     Site            227..250
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:143374"
     CDS             1..423
                     /gene="CDK14"
                     /gene_synonym="PFTAIRE1; PFTK1"
                     /coded_by="NM_001287136.1:158..1429"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75627.1"
                     /db_xref="GeneID:5218"
                     /db_xref="HGNC:HGNC:8883"
                     /db_xref="MIM:610679"
ORIGIN      
        1 mstrncqgmd svikpldtip edkkvrvqrt qstfdpfekp anqvkrvhse nnacinfkts
       61 stgkespkvr rhsspsspts pkfgkadsye kleklgegsy atvykgkskv ngklvalkvi
      121 rlqeeegtpf taireasllk glkhanivll hdiihtketl tlvfeyvhtd lcqymdkhpg
      181 glhpdnvklf lfqllrglsy ihqryilhrd lkpqnllisd tgelkladfg laraksvpsh
      241 tysnevvtlw yrppdvllgs teystcldmw gvgcifvemi qgvaafpgmk diqdqlerif
      301 lvlgtpnedt wpgvhslphf kperftlyss knlrqawnkl syvnhaedla skllqcspkn
      361 rlsaqaalsh eyfsdlpprl weltdmssif tvpnvrlqpe agesmrafgk nnsygkslsn
      421 skh
//
LOCUS       NP_037428                684 aa            linear   PRI 20-NOV-2025
DEFINITION  G-protein-signaling modulator 2 [Homo sapiens].
ACCESSION   NP_037428
VERSION     NP_037428.3
DBSOURCE    REFSEQ: accession NM_013296.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Kadhim,D.J., Azari,H., Sokhangouy,S.K., Hassanian,S.M.,
            Alshekarchi,H.I., Goshayeshi,L., Goshayeshi,L., Abbaszadegan,M.R.,
            Khojasteh-Leylakoohi,F., Khazaei,M., Gataa,I.S., Peters,G.J., A
            Ferns,G., Batra,J., Lam,A.K., Giovannetti,E. and Avan,A.
  TITLE     G-Protein Signaling Modulator 2 as a Potential Biomarker in
            Colorectal Cancer: Integrative Analysis Using Genetic Profiling and
            Pan-Cancer Studies
  JOURNAL   Genes (Basel) 15 (4), 474 (2024)
   PUBMED   38674408
  REMARK    GeneRIF: G-Protein Signaling Modulator 2 as a Potential Biomarker
            in Colorectal Cancer: Integrative Analysis Using Genetic Profiling
            and Pan-Cancer Studies.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Esser,R.L., Bruck,C., Thiele,J., Golumba-Nagy,V., Meyer,A.,
            Steinbach-Knodgen,E., Yan,S., Tho Pesch,C., Stahl,D., Schiller,J.
            and Kofler,D.M.
  TITLE     Truncated isoforms of GPSM2 containing the GoLoco motif region
            promote CD4+ T-cell migration in SLE
  JOURNAL   Lupus Sci Med 9 (1) (2022)
   PUBMED   35940821
  REMARK    GeneRIF: Truncated isoforms of GPSM2 containing the GoLoco motif
            region promote CD4(+) T-cell migration in SLE.
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Yang,D., Ji,F., Li,Y., Jiao,Y. and Fang,X.
  TITLE     GPSM2 Serves as an Independent Prognostic Biomarker for Liver
            Cancer Survival
  JOURNAL   Technol Cancer Res Treat 19, 1533033820945817 (2020)
   PUBMED   32812493
  REMARK    GeneRIF: GPSM2 Serves as an Independent Prognostic Biomarker for
            Liver Cancer Survival.
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Du,Q., Taylor,L., Compton,D.A. and Macara,I.G.
  TITLE     LGN blocks the ability of NuMA to bind and stabilize microtubules.
            A mechanism for mitotic spindle assembly regulation
  JOURNAL   Curr Biol 12 (22), 1928-1933 (2002)
   PUBMED   12445386
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Blumer,J.B., Chandler,L.J. and Lanier,S.M.
  TITLE     Expression analysis and subcellular distribution of the two
            G-protein regulators AGS3 and LGN indicate distinct functionality.
            Localization of LGN to the midbody during cytokinesis
  JOURNAL   J Biol Chem 277 (18), 15897-15903 (2002)
   PUBMED   11832491
  REMARK    GeneRIF: LGN is expressed in neuronal, astroglial, and microglial
            cultures
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Du,Q., Stukenberg,P.T. and Macara,I.G.
  TITLE     A mammalian Partner of inscuteable binds NuMA and regulates mitotic
            spindle organization
  JOURNAL   Nat Cell Biol 3 (12), 1069-1075 (2001)
   PUBMED   11781568
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Mochizuki,N., Cho,G., Wen,B. and Insel,P.A.
  TITLE     Identification and cDNA cloning of a novel human mosaic protein,
            LGN, based on interaction with G alpha i2
  JOURNAL   Gene 181 (1-2), 39-43 (1996)
   PUBMED   8973305
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC341689.1, BC027732.2,
            AI224972.1 and AL449266.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 9, 2008 this sequence version replaced NP_037428.2.
            
            Summary: The protein encoded by this gene belongs to a family of
            proteins that modulate activation of G proteins, which transduce
            extracellular signals received by cell surface receptors into
            integrated cellular responses. The N-terminal half of this protein
            contains 10 copies of leu-gly-asn (LGN) repeat, and the C-terminal
            half contains 4 GoLoco motifs, which are involved in guanine
            nucleotide exchange. This protein may play a role in neuroblast
            division and in the development of normal hearing. Mutations in
            this gene are associated with autosomal recessive nonsyndromic
            deafness (DFNB82). Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.14773.1,
                                           SRR1803615.188004.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264126.9/ ENSP00000264126.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..684
                     /product="G-protein-signaling modulator 2"
                     /note="G-protein signalling modulator 2 (AGS3-like, C.
                     elegans); mosaic protein LGN"
                     /calculated_mol_wt=76531
     Region          22..357
                     /region_name="Important for interaction with NUMA1, INSC
                     and FRMPD1. /evidence=ECO:0000250|UniProtKB:Q8VDU0"
                     /note="propagated from UniProtKB/Swiss-Prot (P81274.3)"
     Region          27..52
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          64..90
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          65..335
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Site            order(66..67,70..71,73,103,106..107,110..111,113..114,143,
                     146..147,150..151,154)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          101..131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P81274.3)"
     Region          203..230
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(243,246..247,250..251,253,283,286..287,290..291,
                     293..294,323,326..327,330..331,334)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          243..270
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          281..311
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          322..350
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          324..359
                     /region_name="TPR_7"
                     /note="Tetratricopeptide repeat; pfam13176"
                     /db_xref="CDD:433012"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P81274.3)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P81274.3)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P81274.3)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P81274.3)"
     Region          490..511
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Site            501
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P81274.3)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P81274.3)"
     Region          545..566
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P81274.3)"
     Region          594..616
                     /region_name="GoLoco"
                     /note="LGN motif, putative GEFs specific for G-alpha
                     GTPases; smart00390"
                     /db_xref="CDD:214645"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKG. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P81274.3)"
     Region          629..650
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     CDS             1..684
                     /gene="GPSM2"
                     /gene_synonym="CMCS; DFNB82; LGN; PINS"
                     /coded_by="NM_013296.5:493..2547"
                     /db_xref="CCDS:CCDS792.2"
                     /db_xref="GeneID:29899"
                     /db_xref="HGNC:HGNC:29501"
                     /db_xref="MIM:609245"
ORIGIN      
        1 meenlismre dhsfhvryrm easclelale gerlcksgdc ragvsffeaa vqvgtedlkt
       61 lsaiysqlgn ayfylhdyak aleyhhhdlt lartigdqlg eakasgnlgn tlkvlgnfde
      121 aivccqrhld isrelndkvg earalynlgn vyhakgksfg cpgpqdvgef peevrdalqa
      181 avdfyeenls lvtalgdraa qgrafgnlgn thyllgnfrd aviaheqrll iakefgdkaa
      241 erraysnlgn ayiflgefet aseyykktll larqlkdrav eaqscyslgn tytllqdyek
      301 aidyhlkhla iaqelndrig egracwslgn aytalgnhdq amhfaekhle isrevgdksg
      361 eltarlnlsd lqmvlglsys tnnsimsent eidsslngvr pklgrrhsme nmelmkltpe
      421 kvqnwnseil akqkpliakp sakllfvnrl kgkkyktnss tkvlqdasns idhripnsqr
      481 kisadtigde gffdllsrfq snrmddqrcc lqeknchtas tttsstppkm mlktssvpvv
      541 spntdefldl lassqsrrld dqrasfsnlp glrltqnsqs vlshlmtndn keadedffdi
      601 lvkcqgsrld dqrcapppat tkgptvpded ffslilrsqg krmdeqrvll qrdqnrdtdf
      661 glkdflqnna llefknsgkk sadh
//
LOCUS       NP_001300928             355 aa            linear   PRI 20-NOV-2025
DEFINITION  beclin-1 isoform b [Homo sapiens].
ACCESSION   NP_001300928
VERSION     NP_001300928.1
DBSOURCE    REFSEQ: accession NM_001313999.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Baek,S., Chang,J.W., Yoo,S.M., Choo,J., Jung,S., Nah,J. and
            Jung,Y.K.
  TITLE     TMEM9 activates Rab9-dependent alternative autophagy through
            interaction with Beclin1
  JOURNAL   Cell Mol Life Sci 81 (1), 322 (2024)
   PUBMED   39078420
  REMARK    GeneRIF: TMEM9 activates Rab9-dependent alternative autophagy
            through interaction with Beclin1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Oberstein,A., Jeffrey,P.D. and Shi,Y.
  TITLE     Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1
            is a novel BH3-only protein
  JOURNAL   J Biol Chem 282 (17), 13123-13132 (2007)
   PUBMED   17337444
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Furuya,N., Yu,J., Byfield,M., Pattingre,S. and Levine,B.
  TITLE     The evolutionarily conserved domain of Beclin 1 is required for
            Vps34 binding, autophagy and tumor suppressor function
  JOURNAL   Autophagy 1 (1), 46-52 (2005)
   PUBMED   16874027
  REMARK    GeneRIF: Evolutionarily conserved domain of Beclin 1 is essential
            for Vps34 interaction, autophagy function, and tumor suppressor
            function.
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Aita,V.M., Liang,X.H., Murty,V.V., Pincus,D.L., Yu,W., Cayanis,E.,
            Kalachikov,S., Gilliam,T.C. and Levine,B.
  TITLE     Cloning and genomic organization of beclin 1, a candidate tumor
            suppressor gene on chromosome 17q21
  JOURNAL   Genomics 59 (1), 59-65 (1999)
   PUBMED   10395800
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Liang,X.H., Kleeman,L.K., Jiang,H.H., Gordon,G., Goldman,J.E.,
            Berry,G., Herman,B. and Levine,B.
  TITLE     Protection against fatal Sindbis virus encephalitis by beclin, a
            novel Bcl-2-interacting protein
  JOURNAL   J Virol 72 (11), 8586-8596 (1998)
   PUBMED   9765397
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Panaretou,C., Domin,J., Cockcroft,S. and Waterfield,M.D.
  TITLE     Characterization of p150, an adaptor protein for the human
            phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by
            phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase
            complex
  JOURNAL   J Biol Chem 272 (4), 2477-2485 (1997)
   PUBMED   8999962
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC010276.1, KC776730.1 and
            AA427906.1.
            
            Summary: This gene encodes a protein that regulates autophagy, a
            catabolic process of degradation induced by starvation. The encoded
            protein is a component of the phosphatidylinositol-3-kinase (PI3K)
            complex which mediates vesicle-trafficking processes. This protein
            is thought to play a role in multiple cellular processes, including
            tumorigenesis, neurodegeneration and apoptosis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            3' coding region resulting in a frameshift, compared to variant 1.
            The encoded isoform (b) has a distinct C-terminus, and is shorter
            than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: KC776730.1, SRR1660809.168189.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..355
                     /product="beclin-1 isoform b"
                     /note="beclin 1 (coiled-coil, moesin-like BCL2-interacting
                     protein); beclin1-gamma; beclin1-beta; ATG6 autophagy
                     related 6 homolog; coiled-coil myosin-like
                     BCL2-interacting protein; testis secretory sperm-binding
                     protein Li 215e; beclin 1, autophagy related"
                     /calculated_mol_wt=40632
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:31123703; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          48..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393,
                     ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          105..129
                     /region_name="BH3"
                     /note="Beclin-1 BH3 domain, Bcl-2-interacting; pfam15285"
                     /db_xref="CDD:464614"
     Region          108..127
                     /region_name="BH3. /evidence=ECO:0000269|PubMed:17337444"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Region          112..159
                     /region_name="Interaction with BCL2 and BCL2L1 isoform
                     Bcl-X(L). /evidence=ECO:0000269|PubMed:17446862"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:19180116; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          135..261
                     /region_name="APG6_N"
                     /note="Apg6 coiled-coil region; pfam17675"
                     /db_xref="CDD:465452"
     Region          267..>348
                     /region_name="APG6"
                     /note="Apg6 BARA domain; pfam04111"
                     /db_xref="CDD:461178"
     CDS             1..355
                     /gene="BECN1"
                     /gene_synonym="ATG6; beclin1; VPS30"
                     /coded_by="NM_001313999.1:3..1070"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:8678"
                     /db_xref="HGNC:HGNC:1034"
                     /db_xref="MIM:604378"
ORIGIN      
        1 megsktsnns tmqvsfvcqr csqplkldts fkildrvtiq eltaplltta qakpgetqee
       61 etnsgeepfi etprqdgvsr rfipparmms tesansftli geasdggtme nlsrrlkvtg
      121 dlfdimsgqt dvdhplceec tdtlldqldt qlnvtenecq nykrcleile qmneddseql
      181 qmelkelale eerliqeled veknrkivae nlekvqaeae rldqeeaqyq reysefkrqq
      241 lelddelksv enqmryaqtq ldklkktnvf natfhiwhsg qfgtinnfrl grlpsvpvew
      301 neinaawgqt vlllhalank mglkfqryrl vpygnhsyle sltdkskdgc gerqd
//
LOCUS       NP_078922                744 aa            linear   PRI 20-NOV-2025
DEFINITION  protein zyg-11 homolog B isoform 1 [Homo sapiens].
ACCESSION   NP_078922 XP_038291
VERSION     NP_078922.1
DBSOURCE    REFSEQ: accession NM_024646.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Duan,B., Zhang,H., Zhu,Z., Yan,X., Ji,Z. and Li,J.
  TITLE     LncRNA LINC01871 sponging miR-142-3p to modulate ZYG11B promotes
            the chemoresistance of colorectal cancer cells by inducing
            autophagy
  JOURNAL   Anticancer Drugs 34 (7), 827-836 (2023)
   PUBMED   36847071
  REMARK    GeneRIF: LncRNA LINC01871 sponging miR-142-3p to modulate ZYG11B
            promotes the chemoresistance of colorectal cancer cells by inducing
            autophagy.
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Zhang,B., Li,Y., Feng,Q., Song,L., Dong,C. and Yan,X.
  TITLE     Structural insights into ORF10 recognition by ZYG11B
  JOURNAL   Biochem Biophys Res Commun 616, 14-18 (2022)
   PUBMED   35636250
  REMARK    GeneRIF: Structural insights into ORF10 recognition by ZYG11B.
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Fonseca,B.F. and Chakrabarti,L.A.
  TITLE     A close shave: How SARS-CoV-2 induces the loss of cilia
  JOURNAL   J Cell Biol 221 (7) (2022)
   PUBMED   35695891
  REMARK    GeneRIF: A close shave: How SARS-CoV-2 induces the loss of cilia.
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Yan,X., Li,Y., Wang,G., Zhou,Z., Song,G., Feng,Q., Zhao,Y., Mi,W.,
            Ma,Z. and Dong,C.
  TITLE     Molecular basis for recognition of Gly/N-degrons by CRL2ZYG11B and
            CRL2ZER1
  JOURNAL   Mol Cell 81 (16), 3262-3274 (2021)
   PUBMED   34214466
  REMARK    GeneRIF: Molecular basis for recognition of Gly/N-degrons by
            CRL2(ZYG11B) and CRL2(ZER1).
REFERENCE   5  (residues 1 to 744)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 744)
  AUTHORS   Timms,R.T., Zhang,Z., Rhee,D.Y., Harper,J.W., Koren,I. and
            Elledge,S.J.
  TITLE     A glycine-specific N-degron pathway mediates the quality control of
            protein N-myristoylation
  JOURNAL   Science 365 (6448) (2019)
   PUBMED   31273098
REFERENCE   7  (residues 1 to 744)
  AUTHORS   Balachandran,R.S., Heighington,C.S., Starostina,N.G.,
            Anderson,J.W., Owen,D.L., Vasudevan,S. and Kipreos,E.T.
  TITLE     The ubiquitin ligase CRL2ZYG11 targets cyclin B1 for degradation in
            a conserved pathway that facilitates mitotic slippage
  JOURNAL   J Cell Biol 215 (2), 151-166 (2016)
   PUBMED   27810909
  REMARK    GeneRIF: the ubiquitin ligase CRL2(ZYG-11) redundantly targets the
            degradation of cyclin B1 in Caenorhabditis elegans and human cells.
REFERENCE   8  (residues 1 to 744)
  AUTHORS   Okumura,F., Matsuzaki,M., Nakatsukasa,K. and Kamura,T.
  TITLE     The Role of Elongin BC-Containing Ubiquitin Ligases
  JOURNAL   Front Oncol 2, 10 (2012)
   PUBMED   22649776
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 744)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   10 (residues 1 to 744)
  AUTHORS   Vasudevan,S., Starostina,N.G. and Kipreos,E.T.
  TITLE     The Caenorhabditis elegans cell-cycle regulator ZYG-11 defines a
            conserved family of CUL-2 complex components
  JOURNAL   EMBO Rep 8 (3), 279-286 (2007)
   PUBMED   17304241
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099784.2, AK296460.1, AB051517.1 and AL139255.9.
            
            On Nov 22, 2004 this sequence version replaced XP_038291.5.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.209888.1,
                                           SRR1660803.11859.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294353.7/ ENSP00000294353.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..744
                     /product="protein zyg-11 homolog B isoform 1"
                     /note="protein zyg-11 homolog B"
                     /calculated_mol_wt=83790
     Region          107..136
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <128..>275
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          138..163
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          164..182
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          185..208
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D3.2)"
     Region          188..213
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          214..238
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          216..236
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D3.2)"
     Region          237..261
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0D3.2)"
     Region          239..267
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          268..293
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..744
                     /gene="ZYG11B"
                     /gene_synonym="ZYG11"
                     /coded_by="NM_024646.3:202..2436"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30717.1"
                     /db_xref="GeneID:79699"
                     /db_xref="HGNC:HGNC:25820"
                     /db_xref="MIM:618673"
ORIGIN      
        1 mpedqagaam eeaspyslld iclnfltthl ekfcsarqdg tlclqepgvf pqevadrllr
       61 tmafhgllnd gtvgifrgnq mrlkracirk akisavafrk afchhklvel datgvnadit
      121 itdiisglgs nkwiqqnlqc lvlnsltlsl edpyercfsr lsglralsit nvlfynedla
      181 evaslprles ldisntsitd itallackdr lksltmhhlk clkmtttqil dvvrelkhln
      241 hldisddkqf tsdialrlle qkdilpnlvs ldvsgrkhvt dkaveafiqq rpsmqfvgll
      301 atdagysefl tgeghlkvsg eanetqiaea lkryseraff vrealfhlfs lthvmektkp
      361 eilklvvtgm rnhpmnlpvq laasacvfnl tkqdlaagmp vrlladvthl llkamehfpn
      421 hqqlqkncll slcsdrilqd vpfnrfeaak lvmqwlcnhe dqnmqrmava iisilaakls
      481 teqtaqlgte lfivrqllqi vkqktnqnsv dttlkftlsa lwnltdespt tcrhfienqg
      541 lelfmrvles fptessiqqk vlgllnniae vqelhselmw kdfidhissl lhsvevevsy
      601 faagiiahli srgeqawtls rsqrnslldd lhsailkwpt pecemvayrs fnpffpllgc
      661 fttpgvqlwa vwamqhvcsk npsrycsmli eegglqhlyn ikdhehtdph vqqiavaild
      721 slekhivrhg rpppckkqpq arln
//
LOCUS       NP_003989                969 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p105 subunit isoform 1 [Homo sapiens].
ACCESSION   NP_003989
VERSION     NP_003989.2
DBSOURCE    REFSEQ: accession NM_003998.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 969)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 969)
  AUTHORS   Vazquez-Coto,D., Perez-Oliveira,S., Menendez-Gonzalez,M., Coto,E.
            and Alvarez,V.
  TITLE     Assessing the association between common functional Nuclear Factor
            Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA) and Alzheimer s
            disease
  JOURNAL   Behav Brain Res 476, 115264 (2025)
   PUBMED   39322062
  REMARK    GeneRIF: Assessing the association between common functional
            Nuclear Factor Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA)
            and Alzheimer s disease.
REFERENCE   3  (residues 1 to 969)
  AUTHORS   Al-Salihy,S.R., Al-Shawk,R.S., Al-Waysi,S.A. and Rasheed,M.N.
  TITLE     Association of nuclear factor-kappa B1 (NF-kappaB1) Ins/Del gene
            polymorphism with Hepatitis C virus outcomes
  JOURNAL   J Pak Med Assoc 74 (10 (Supple-8)), S34-S38 (2024)
   PUBMED   39434268
  REMARK    GeneRIF: Association of nuclear factor-kappa B1 (NF-kappaB1)
            Ins/Del gene polymorphism with Hepatitis C virus outcomes.
REFERENCE   4  (residues 1 to 969)
  AUTHORS   Eluard,B., Thieblemont,C. and Baud,V.
  TITLE     NF-kappaB in the New Era of Cancer Therapy
  JOURNAL   Trends Cancer 6 (8), 677-687 (2020)
   PUBMED   32409139
  REMARK    Review article
REFERENCE   5  (residues 1 to 969)
  AUTHORS   Lin,L. and Ghosh,S.
  TITLE     A glycine-rich region in NF-kappaB p105 functions as a processing
            signal for the generation of the p50 subunit
  JOURNAL   Mol Cell Biol 16 (5), 2248-2254 (1996)
   PUBMED   8628291
REFERENCE   6  (residues 1 to 969)
  AUTHORS   Muller,C.W., Rey,F.A., Sodeoka,M., Verdine,G.L. and Harrison,S.C.
  TITLE     Structure of the NF-kappa B p50 homodimer bound to DNA
  JOURNAL   Nature 373 (6512), 311-317 (1995)
   PUBMED   7830764
REFERENCE   7  (residues 1 to 969)
  AUTHORS   Rice,N.R., MacKichan,M.L. and Israel,A.
  TITLE     The precursor of NF-kappa B p50 has I kappa B-like functions
  JOURNAL   Cell 71 (2), 243-253 (1992)
   PUBMED   1423592
REFERENCE   8  (residues 1 to 969)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   9  (residues 1 to 969)
  AUTHORS   Urban,M.B., Schreck,R. and Baeuerle,P.A.
  TITLE     NF-kappa B contacts DNA by a heterodimer of the p50 and p65 subunit
  JOURNAL   EMBO J 10 (7), 1817-1825 (1991)
   PUBMED   2050119
REFERENCE   10 (residues 1 to 969)
  AUTHORS   Bours,V., Villalobos,J., Burd,P.R., Kelly,K. and Siebenlist,U.
  TITLE     Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding
            protein with homology to the rel oncogene and to cell-cycle motifs
  JOURNAL   Nature 348 (6296), 76-80 (1990)
   PUBMED   2234062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051765.1, AF213884.2 and
            AI076882.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 11, 2003 this sequence version replaced NP_003989.1.
            
            Summary: This gene encodes a 105 kD protein which can undergo
            cotranslational processing by the 26S proteasome to produce a 50 kD
            protein. The 105 kD protein is a Rel protein-specific transcription
            inhibitor and the 50 kD protein is a DNA binding subunit of the
            NF-kappa-B (NFKB) protein complex. NFKB is a transcription
            regulator that is activated by various intra- and extra-cellular
            stimuli such as cytokines, oxidant-free radicals, ultraviolet
            irradiation, and bacterial or viral products. Activated NFKB
            translocates into the nucleus and stimulates the expression of
            genes involved in a wide variety of biological functions.
            Inappropriate activation of NFKB has been associated with a number
            of inflammatory diseases while persistent inhibition of NFKB leads
            to inappropriate immune cell development or delayed cell growth.
            NFKB is a critical regulator of the immediate-early response to
            viral infection. Alternative splicing results in multiple
            transcript variants encoding different isoforms, at least one of
            which is proteolytically processed. [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051765.1, M55643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000226574.9/ ENSP00000226574.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..969
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..969
                     /product="nuclear factor NF-kappa-B p105 subunit isoform
                     1"
                     /note="nuclear factor kappa-B DNA binding subunit; nuclear
                     factor NF-kappa-B p50 subunit; nuclear factor NF-kappa-B
                     p105 subunit; DNA-binding factor KBF1; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells 1"
                     /calculated_mol_wt=105296
     Region          43..244
                     /region_name="RHD-n_NFkB1"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of kappa B1 (NF-kappa B1);
                     cd07935"
                     /db_xref="CDD:143651"
     Site            order(57,59..60,62..63,66..69,144,146..147,244)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143651"
     Region          251..352
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(252,254..256,258..260,300..302,315,327,346,349,351)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(254..255,257,270,272,274,307..308,311,313)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(275,277,308..309)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          361..366
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          373..395
                     /region_name="GRR. /evidence=ECO:0000269|PubMed:8628291"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          426..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            432
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            434..435
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed).
                     /evidence=ECO:0000269|PubMed:9529257; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          436..969
                     /region_name="Interaction with CFLAR.
                     /evidence=ECO:0000269|PubMed:13679070"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            441
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            442
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          499..759
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(543,545,549..550,553..555,557..558,562,565,580,582,
                     584,588..589,592..594,596..597,601,604,613,615,617,
                     621..622,625..627,629..630,634,637)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          543..580
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          582..613
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          651..685
                     /region_name="Essential for interaction with HIF1AN.
                     /evidence=ECO:0000269|PubMed:17003112"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          651..681
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            679
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:17003112; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          685..717
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63369; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          816..891
                     /region_name="Death_NFkB1_p105"
                     /note="Death domain of the Nuclear Factor-KappaB1
                     precursor protein p105; cd08797"
                     /db_xref="CDD:260063"
     Site            893
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11158290; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            928
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:11158290,
                     ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:12482991,
                     ECO:0000269|PubMed:25860612; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:12482991; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            938
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            944
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     CDS             1..969
                     /gene="NFKB1"
                     /gene_synonym="CVID12; EBP-1; KBF1; NF-kappa-B1;
                     NF-kappaB; NF-kappabeta; NF-kB; NF-kB1; NFkappaB;
                     NFKB-p105; NFKB-p50"
                     /coded_by="NM_003998.4:438..3347"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3657.1"
                     /db_xref="GeneID:4790"
                     /db_xref="HGNC:HGNC:7794"
                     /db_xref="MIM:164011"
ORIGIN      
        1 maeddpylgr peqmfhldps lthtifnpev fqpqmalpta dgpylqileq pkqrgfrfry
       61 vcegpshggl pgasseknkk sypqvkicny vgpakvivql vtngknihlh ahslvgkhce
      121 dgictvtagp kdmvvgfanl gilhvtkkkv fetlearmte acirgynpgl lvhpdlaylq
      181 aegggdrqlg drekelirqa alqqtkemdl svvrlmftaf lpdstgsftr rlepvvsdai
      241 ydskapnasn lkivrmdrta gcvtggeeiy llcdkvqkdd iqirfyeeee nggvwegfgd
      301 fsptdvhrqf aivfktpkyk dinitkpasv fvqlrrksdl etsepkpfly ypeikdkeev
      361 qrkrqklmpn fsdsfgggsg agaggggmfg sggggggtgs tgpgysfphy gfptyggitf
      421 hpgttksnag mkhgtmdtes kkdpegcdks ddkntvnlfg kvietteqdq epseatvgng
      481 evtltyatgt keesagvqdn lflekamqla krhanalfdy avtgdvkmll avqrhltavq
      541 dengdsvlhl aiihlhsqlv rdllevtsgl isddiinmrn dlyqtplhla vitkqedvve
      601 dllragadls lldrlgnsvl hlaakeghdk vlsillkhkk aallldhpng dglnaihlam
      661 msnslpclll lvaagadvna qeqksgrtal hlavehdnis lagclllegd ahvdsttydg
      721 ttplhiaagr gstrlaallk aagadplven feplydldds wenagedegv vpgttpldma
      781 tswqvfdiln gkpyepefts ddllaqgdmk qlaedvklql yklleipdpd knwatlaqkl
      841 glgilnnafr lspapsktlm dnyevsggtv relvealrqm gyteaieviq aasspvktts
      901 qahslplspa strqqidelr dsdsvcdsgv etsfrklsft esltsgasll tlnkmphdyg
      961 qegplegki
//
LOCUS       NP_001257916             416 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001257916
VERSION     NP_001257916.1
DBSOURCE    REFSEQ: accession NM_001270987.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Tang,Q., Yuan,Y., Li,L., Xu,Y., Ji,W., Xiao,S., Han,Y., Miao,W.,
            Cai,J., You,P., Chen,M., Ding,S., Li,Z., Qi,Z., Hou,W. and Luo,H.
  TITLE     Comprehensive analysis reveals that LTBR is a immune-related
            biomarker for glioma
  JOURNAL   Comput Biol Med 174, 108457 (2024)
   PUBMED   38599071
  REMARK    GeneRIF: Comprehensive analysis reveals that LTBR is a
            immune-related biomarker for glioma.
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Wu,Y., Zhao,S., Guo,W., Liu,Y., Requena Mullor,M.D.M.,
            Rodriguez,R.A. and Wei,R.
  TITLE     Systematic analysis of the prognostic value and immunological
            function of LTBR in human cancer
  JOURNAL   Aging (Albany NY) 16 (1), 129-152 (2024)
   PUBMED   38175686
  REMARK    GeneRIF: Systematic analysis of the prognostic value and
            immunological function of LTBR in human cancer.
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Shuptrine,C.W., Perez,V.M., Selitsky,S.R., Schreiber,T.H. and
            Fromm,G.
  TITLE     Shining a LIGHT on myeloid cell targeted immunotherapy
  JOURNAL   Eur J Cancer 187, 147-160 (2023)
   PUBMED   37167762
  REMARK    Review article
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Abudukeyoumu,A., Lai,Z.Z., Lu,J.J., Zhang,X., Hou,D.Y., Dong,J.,
            Wu,J.N., Li,M.Q. and Xie,F.
  TITLE     A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion
  JOURNAL   J Reprod Immunol 153, 103693 (2022)
   PUBMED   35987137
  REMARK    GeneRIF: A LIGHT-HVEM/LTbetaR axis contributes to the fibrosis of
            intrauterine adhesion.
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Remouchamps,C., Boutaffala,L., Ganeff,C. and Dejardin,E.
  TITLE     Biology and signal transduction pathways of the
            Lymphotoxin-alphabeta/LTbetaR system
  JOURNAL   Cytokine Growth Factor Rev 22 (5-6), 301-310 (2011)
   PUBMED   22152226
  REMARK    Review article
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Nakano,H., Oshima,H., Chung,W., Williams-Abbott,L., Ware,C.F.,
            Yagita,H. and Okumura,K.
  TITLE     TRAF5, an activator of NF-kappaB and putative signal transducer for
            the lymphotoxin-beta receptor
  JOURNAL   J Biol Chem 271 (25), 14661-14664 (1996)
   PUBMED   8663299
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Browning,J.L., Miatkowski,K., Sizing,I., Griffiths,D., Zafari,M.,
            Benjamin,C.D., Meier,W. and Mackay,F.
  TITLE     Signaling through the lymphotoxin beta receptor induces the death
            of some adenocarcinoma tumor lines
  JOURNAL   J Exp Med 183 (3), 867-878 (1996)
   PUBMED   8642291
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Baens,M., Aerssens,J., van Zand,K., Van den Berghe,H. and
            Marynen,P.
  TITLE     Isolation and regional assignment of human chromosome 12p cDNAs
  JOURNAL   Genomics 29 (1), 44-52 (1995)
   PUBMED   8530100
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Crowe,P.D., VanArsdale,T.L., Walter,B.N., Ware,C.F., Hession,C.,
            Ehrenfels,B., Browning,J.L., Din,W.S., Goodwin,R.G. and Smith,C.A.
  TITLE     A lymphotoxin-beta-specific receptor
  JOURNAL   Science 264 (5159), 707-710 (1994)
   PUBMED   8171323
REFERENCE   10 (residues 1 to 416)
  AUTHORS   Baens,M., Chaffanet,M., Cassiman,J.J., van den Berghe,H. and
            Marynen,P.
  TITLE     Construction and evaluation of a hncDNA library of human 12p
            transcribed sequences derived from a somatic cell hybrid
  JOURNAL   Genomics 16 (1), 214-218 (1993)
   PUBMED   8486360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005840.2, DC424721.1,
            AK293187.1, BC026262.1 and AK027080.1.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor superfamily. The major ligands of this receptor include
            lymphotoxin alpha/beta and tumor necrosis factor ligand superfamily
            member 14. The encoded protein plays a role in signalling during
            the development of lymphoid and other organs, lipid metabolism,
            immune response, and programmed cell death. Activity of this
            receptor has also been linked to carcinogenesis. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..416
                     /product="tumor necrosis factor receptor superfamily
                     member 3 isoform 2"
                     /note="tumor necrosis factor C receptor; lymphotoxin B
                     receptor; tumor necrosis factor receptor type III;
                     lymphotoxin beta receptor (TNFR superfamily, member 3);
                     tumor necrosis factor receptor 2-related protein"
                     /calculated_mol_wt=44679
     Region          4..149
                     /region_name="TNFRSF3"
                     /note="Tumor necrosis factor receptor superfamily member 3
                     (TNFRSF3), also known as lymphotoxin beta receptor (LTBR);
                     cd10578"
                     /db_xref="CDD:276904"
     Region          4..61
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276904"
     Region          64..105
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276904"
     Region          107..148
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276904"
     Region          129..>191
                     /region_name="TNFRSF"
                     /note="Tumor necrosis factor receptor superfamily
                     (TNFRSF); cl22855"
                     /db_xref="CDD:473981"
     Region          151..191
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276900"
     CDS             1..416
                     /gene="LTBR"
                     /gene_synonym="D12S370; LT-BETA-R; TNF-R-III; TNFCR;
                     TNFR-RP; TNFR2-RP; TNFR3; TNFRSF3"
                     /coded_by="NM_001270987.2:397..1647"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS59233.1"
                     /db_xref="GeneID:4055"
                     /db_xref="HGNC:HGNC:6718"
                     /db_xref="MIM:600979"
ORIGIN      
        1 meatgislas qlkvppyase nqtcrdqeke yyepqhricc srcppgtyvs akcsrirdtv
       61 catcaensyn ehwnylticq lcrpcdpvmg leeiapctsk rktqcrcqpg mfcaawalec
      121 thcellsdcp pgteaelkde vgkgnnhcvp ckaghfqnts spsarcqpht rcenqglvea
      181 apgtaqsdtt cknpleplpp emsgtmlmla vllplaffll latvfsciwk shpslcrklg
      241 sllkrrpqge gpnpvagswe ppkahpyfpd lvqpllpisg dvspvstglp aapvleagvp
      301 qqqspldltr epqlepgeqs qvahgtngih vtggsmtitg niyiyngpvl ggppgpgdlp
      361 atpeppypip eegdpgppgl stphqedgka whlaetehcg atpsnrgprn qfithd
//
LOCUS       NP_001356482            1046 aa            linear   PRI 20-NOV-2025
DEFINITION  NHS-like protein 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001356482 XP_006710854
VERSION     NP_001356482.1
DBSOURCE    REFSEQ: accession NM_001369553.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1046)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1046)
  AUTHORS   Guo,Y., Tian,S., Li,H., Zuo,S., Yu,C. and Sun,C.
  TITLE     Transcription factor KLF9 inhibits the proliferation, invasion, and
            migration of pancreatic cancer cells by repressing KIAA1522
  JOURNAL   Asia Pac J Clin Oncol 20 (3), 423-432 (2024)
   PUBMED   38520660
  REMARK    GeneRIF: Transcription factor KLF9 inhibits the proliferation,
            invasion, and migration of pancreatic cancer cells by repressing
            KIAA1522.
REFERENCE   3  (residues 1 to 1046)
  AUTHORS   Palukuri,M.V., Patil,R.S. and Marcotte,E.M.
  TITLE     Molecular complex detection in protein interaction networks through
            reinforcement learning
  JOURNAL   BMC Bioinformatics 24 (1), 306 (2023)
   PUBMED   37532987
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1046)
  AUTHORS   Ou,M., Chu,Y., Zhang,Q., Zhao,H. and Song,Q.
  TITLE     HOXA cluster antisense RNA 2 elevates KIAA1522 expression through
            microRNA-520d-3p and insulin like growth factor 2 mRNA binding
            protein 3 to promote the growth of vascular smooth muscle cells in
            thoracic aortic aneurysm
  JOURNAL   ESC Heart Fail 9 (5), 2955-2966 (2022)
   PUBMED   35730141
  REMARK    GeneRIF: HOXA cluster antisense RNA 2 elevates KIAA1522 expression
            through microRNA-520d-3p and insulin like growth factor 2 mRNA
            binding protein 3 to promote the growth of vascular smooth muscle
            cells in thoracic aortic aneurysm.
REFERENCE   5  (residues 1 to 1046)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1046)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 1046)
  AUTHORS   Wang,B., Jing,T., Jin,W., Chen,J., Wu,C., Wang,M. and Liu,Y.
  TITLE     KIAA1522 potentiates TNFalpha-NFkappaB signaling to antagonize
            platinum-based chemotherapy in lung adenocarcinoma
  JOURNAL   J Exp Clin Cancer Res 39 (1), 170 (2020)
   PUBMED   32854746
  REMARK    GeneRIF: KIAA1522 potentiates TNFalpha-NFkappaB signaling to
            antagonize platinum-based chemotherapy in lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1046)
  AUTHORS   Li,Y., Wang,Y., Fan,H., Zhang,Z. and Li,N.
  TITLE     miR-125b-5p inhibits breast cancer cell proliferation, migration
            and invasion by targeting KIAA1522
  JOURNAL   Biochem Biophys Res Commun 504 (1), 277-282 (2018)
   PUBMED   30177391
  REMARK    GeneRIF: miR-125b-5p functions as a tumor suppressor and regulates
            breast cancer cell progression through targeting KIAA1522
REFERENCE   9  (residues 1 to 1046)
  AUTHORS   Liu,Y.Z., Yang,H., Cao,J., Jiang,Y.Y., Hao,J.J., Xu,X., Cai,Y. and
            Wang,M.R.
  TITLE     KIAA1522 is a novel prognostic biomarker in patients with non-small
            cell lung cancer
  JOURNAL   Sci Rep 6, 24786 (2016)
   PUBMED   27098511
  REMARK    GeneRIF: high expression of KIAA1522 can be used as an independent
            biomarker for predication of poor survival and platinum-resistance
            of NSCLC patients, and aberrant KIAA1522 might be a new target for
            the therapy of the disease.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1046)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC114489.2.
            
            On Apr 11, 2019 this sequence version replaced XP_006710854.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2572629.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1046
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.1"
     Protein         1..1046
                     /product="NHS-like protein 3 isoform 4"
                     /note="NHS-like protein 3"
                     /calculated_mol_wt=108254
     Region          <735..1011
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..1046
                     /gene="NHSL3"
                     /gene_synonym="KIAA1522"
                     /coded_by="NM_001369553.1:92..3232"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS90910.1"
                     /db_xref="GeneID:57648"
                     /db_xref="HGNC:HGNC:29301"
ORIGIN      
        1 mgnshhkrka psgprvrsfw rfgrsakrpa gsakaendkh lsvgpgqgpg savdehqdnv
       61 ffpsgrpphl eelhtqaqeg lrslqhqekq klnkggwdhg dtqsiqssrt gpdednisfc
      121 sqttsyvaes staedalsir semiqrkgst frphdsfpks gksgrrrrer rstvlglpqh
      181 vqkelglrne reapgtprap gardavript vdgrprgtsg mgarvslqal eaeaeagaet
      241 eamlqrhidr vyrddtfvgr stgtrapplt rpmslavpgl tggagpaepl spamsispqa
      301 tylsklipha vlpptvdvva lgrcslrtls rcslhsaspa svrslgrfss vsspqprsrh
      361 pssssdtwsh sqssdtivsd gstlsskggs egqpesstas nsvvpppqgg sgrgspsggs
      421 taeasdtlsi rssgqlsgrs vslrklkrpp ppprrthslh qrglavpdgp lglppkperk
      481 qqpqlprppt tggsegagaa pcppnpansw vpglspggsr rpprspertl spssgyssqs
      541 gtptlppkgl agppaspgka qppkpervts lrspgasvss sltslcssss dpapsdrsgp
      601 qiltplgdrf vipphpkvpa pfspppskpr spnpaapala apavvpgpvs ttdaspqspp
      661 tpqttltplq espviskdqs pppspppsyh ppppptkkpe vvveapsase taeeplqdpn
      721 wppppppape eqdlsmadfp ppeeaffsva spepagpsgs pelvsspaas sssatalqiq
      781 ppgspdpppa ppapapassa pghvaklpqk epvgcskggg ppredvgapl vtpsllqmvr
      841 lrsvgapgga ptpalgpsap qkplrralsg raspvpapss glhaavrlka cslaasegls
      901 saqpngppea eprppqspas tasfifskgs rklqlerpvs petqadlqrn lvaelrsise
      961 qrppqapkks pkapppvark psvgvpppas psypraeplt apptnglpht qdrtkrelae
     1021 nggvlqlvgp eekmglpgsd sqkela
//
LOCUS       NP_001542                339 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001542
VERSION     NP_001542.1
DBSOURCE    REFSEQ: accession NM_001551.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Liu,J., Prickett,T.D., Elliott,E., Meroni,G. and Brautigan,D.L.
  TITLE     Phosphorylation and microtubule association of the Opitz syndrome
            protein mid-1 is regulated by protein phosphatase 2A via binding to
            the regulatory subunit alpha 4
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6650-6655 (2001)
   PUBMED   11371618
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Chung,H., Nairn,A.C., Murata,K. and Brautigan,D.L.
  TITLE     Mutation of Tyr307 and Leu309 in the protein phosphatase 2A
            catalytic subunit favors association with the alpha 4 subunit which
            promotes dephosphorylation of elongation factor-2
  JOURNAL   Biochemistry 38 (32), 10371-10376 (1999)
   PUBMED   10441131
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Onda,M., Inui,S., Maeda,K., Suzuki,M., Takahashi,E. and
            Sakaguchi,N.
  TITLE     Expression and chromosomal localization of the human alpha 4/IGBP1
            gene, the structure of which is closely related to the yeast TAP42
            protein of the rapamycin-sensitive signal transduction pathway
  JOURNAL   Genomics 46 (3), 373-378 (1997)
   PUBMED   9441740
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158141.14 and BC004137.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The proliferation and differentiation of B cells is
            dependent upon a B-cell antigen receptor (BCR) complex. Binding of
            antigens to specific B-cell receptors results in a tyrosine
            phosphorylation reaction through the BCR complex and leads to
            multiple signal transduction pathways. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004137.2, SRR5189655.103080.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356413.5/ ENSP00000348784.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..339
                     /product="immunoglobulin-binding protein 1 isoform 1"
                     /note="protein phosphatase 2A, regulatory subunit alpha-4;
                     B cell signal transduction molecule alpha 4; bA351K23.1
                     (immunoglobulin binding protein 1 (CD79A)); protein
                     alpha-4; CD79a-binding protein 1; immunoglobulin (CD79A)
                     binding protein 1; renal carcinoma antigen NY-REN-16;
                     protein phosphatase 2/4/6 regulatory subunit"
                     /calculated_mol_wt=39091
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          12..329
                     /region_name="TAP42"
                     /note="TAP42-like family; pfam04177"
                     /db_xref="CDD:461209"
     Region          98..202
                     /region_name="Interaction with PPP2CA"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          221..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          225..290
                     /region_name="Interaction with MID1.
                     /evidence=ECO:0000269|PubMed:11806752"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Site            255..256
                     /site_type="cleavage"
                     /note="Cleavage, by calpain; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          289..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     CDS             1..339
                     /gene="IGBP1"
                     /gene_synonym="ALPHA-4; alpha4; IBP1; MRXS28"
                     /coded_by="NM_001551.3:320..1339"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14396.1"
                     /db_xref="GeneID:3476"
                     /db_xref="HGNC:HGNC:5461"
                     /db_xref="MIM:300139"
ORIGIN      
        1 maaedelqlp rlpelfetgr qlldevevat epagsrivqe kvfkgldlle kaaemlsqld
       61 lfsrnedlee iastdlkyll vpafqgaltm kqvnpskrld hlqrarehfi nyltqchcyh
      121 vaefelpktm nnsaenhtan ssmaypslva masqrqakiq rykqkkeleh rlsamksave
      181 sgqaddervr eyyllhlqrw idisleeies idqeikilre rdssreasts nssrqerppv
      241 kpfiltrnma qakvfgagyp slptmtvsdw yeqhrkygal pdqgiakaap eefrkaaqqq
      301 eeqeekeeed deqtlhrare wddwkdthpr gygnrqnmg
//
LOCUS       NP_001161709            1079 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform g [Homo sapiens].
ACCESSION   NP_001161709
VERSION     NP_001161709.1
DBSOURCE    REFSEQ: accession NM_001168237.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1079)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1079)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1079)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1079)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1079)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1079)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1079)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1079)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1079)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1079)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL512326.25, FJ542284.1,
            AL139132.16 and BQ014912.1.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (g) lacks an alternate in-frame
            segment in the 3' coding region, compared to variant b, resulting
            in an isoform (g, also known as 1BLCTS) that is shorter than
            isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FJ542284.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1079
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1079
                     /product="tyrosine-protein kinase ABL2 isoform g"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=117811
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          2..106
                     /region_name="CAP"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          60..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          111..164
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(116,118,121..123,125,140,144..145,156,158,160..161)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(120..123,142,144)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          169..262
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(180,208,221)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            261
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and autocatalysis.
                     /evidence=ECO:0000269|PubMed:15735735; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          281..543
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(294,296..298,315,317,362,364,368,416,427,445..447,
                     449,457,491,495)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(294,296,299,315,317,332,336,345,361..362,364,368,
                     416,426..427)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(309..310,340..342,346,388,420..421,539..540)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(386..387,390,475,478..479,508..509)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            426..450
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Region          427..451
                     /region_name="Kinase activation loop.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            439
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis and SRC-type
                     Tyr-kinases. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            order(445..447,449,457,491,495)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Site            459
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12748290; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          611..641
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          654..674
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Region          658..660
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            669
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P00519; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P42684.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; Phosphotyrosine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:12748290;
                     propagated from UniProtKB/Swiss-Prot (P42684.1)"
     Region          960..1079
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1079
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_001168237.2:281..3520"
                     /note="isoform g is encoded by transcript variant g"
                     /db_xref="CCDS:CCDS53438.1"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mgqqvgrvge apglqqpqpr girgssaarp sgrrrdpagr ttetgfnift qhdhfascve
       61 dgfegdktgg sspealhrpy gcdvepqaln eairwssken llgatesdpn lfvalydfva
      121 sgdntlsitk geklrvlgyn qngewsevrs kngqgwvpsn yitpvnslek hswyhgpvsr
      181 saaeyllssl ingsflvres esspgqlsis lryegrvyhy rinttadgkv yvtaesrfst
      241 laelvhhhst vadglvttlh ypapkcnkpt vygvspihdk wemertditm khklgggqyg
      301 evyvgvwkky sltvavktlk edtmeveefl keaavmkeik hpnlvqllgv ctleppfyiv
      361 teympygnll dylrecnree vtavvllyma tqissameyl ekknfihrdl aarnclvgen
      421 hvvkvadfgl srlmtgdtyt ahagakfpik wtapeslayn tfsiksdvwa fgvllweiat
      481 ygmspypgid lsqvydllek gyrmeqpegc ppkvyelmra cwkwspadrp sfaethqafe
      541 tmfhdssise evaeelgraa ssssvvpylp rlpilpsktr tlkkqvenke niegaqdate
      601 nsasslapgf irgaqassgs palprkqrdk spsslledak etcftrdrkg gffssfmkkr
      661 naptppkrss sfremenqph kkyeltglpe qdrmamtlpr ncqrsklqle rtvstssqpe
      721 envdrandml pkkseesaap srerpkakll prgatalplr tpsgdlaite kdppgvgvag
      781 vaaapkgkek nggarlgmag vpedgeqpgw pspakaapvl ptthnhkvpv lisptlkhtp
      841 advqligtds qgnkfkllse hqvtssgdkd rprrvkpkca pppppvmrll qhpsicsdpt
      901 eeptaltagq stsetqeggk kaalgavpis gkagrpvmpp pqvplptssi spakmangta
      961 gtkvalrktk qaaekisadk iskealleca dllssaltep vpnsqlvdtg hqlldycsgy
     1021 vdcipqtrnk fafreavskl elslqelqvs saaagvpgtn pvlnnllscv qeisdvvqr
//
LOCUS       NP_009103                468 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear pore complex protein Nup50 isoform b [Homo sapiens].
ACCESSION   NP_009103
VERSION     NP_009103.2
DBSOURCE    REFSEQ: accession NM_007172.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Smitherman,M., Lee,K., Swanger,J., Kapur,R. and Clurman,B.E.
  TITLE     Characterization and targeted disruption of murine Nup50, a
            p27(Kip1)-interacting component of the nuclear pore complex
  JOURNAL   Mol Cell Biol 20 (15), 5631-5642 (2000)
   PUBMED   10891500
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Guan,T., Kehlenbach,R.H., Schirmer,E.C., Kehlenbach,A., Fan,F.,
            Clurman,B.E., Arnheim,N. and Gerace,L.
  TITLE     Nup50, a nucleoplasmically oriented nucleoporin with a role in
            nuclear protein export
  JOURNAL   Mol Cell Biol 20 (15), 5619-5630 (2000)
   PUBMED   10891499
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Trichet,V., Shkolny,D., Dunham,I., Beare,D. and McDermid,H.E.
  TITLE     Mapping and complex expression pattern of the human NPAP60L
            nucleoporin gene
  JOURNAL   Cytogenet Cell Genet 85 (3-4), 221-226 (1999)
   PUBMED   10449902
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z82243.1, BC070133.1 and
            AL008718.23.
            
            On Nov 3, 2002 this sequence version replaced NP_009103.1.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins are the main components of the nuclear pore
            complex in eukaryotic cells. The protein encoded by this gene is a
            member of the FG-repeat containing nucleoporins that functions as a
            soluble cofactor in importin-alpha:beta-mediated nuclear protein
            import. Pseudogenes of this gene are found on chromosomes 5, 6, and
            14. Two transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) represents the longer
            transcript and encodes the longer isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.49356.1,
                                           SRR1660809.157675.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000347635.9/ ENSP00000345895.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..468
                     /product="nuclear pore complex protein Nup50 isoform b"
                     /note="nuclear pore-associated protein 60L; nuclear pore
                     complex protein Nup50; nucleoporin Nup50; 50 kDa
                     nucleoporin; nucleoporin 50kD; nucleoporin 50kDa"
                     /calculated_mol_wt=50013
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          2..67
                     /region_name="NUP50"
                     /note="NUP50 (Nucleoporin 50 kDa); pfam08911"
                     /db_xref="CDD:462629"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          76..304
                     /region_name="5 X 2 AA repeats of F-G"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            83
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          122..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          144..206
                     /region_name="Binding to CDKN1B. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          201..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          238..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          304..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKX7.2)"
     Region          350..466
                     /region_name="RanBD_NUP50"
                     /note="Nucleoporin 50 Ran-binding domain; cd13170"
                     /db_xref="CDD:269991"
     Site            order(364,366..368,372..376,392,394,396..397,402..404,407,
                     409,413,417,425,427,444,448)
                     /site_type="other"
                     /note="putative RAN binding site [polypeptide binding]"
                     /db_xref="CDD:269991"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH2; propagated from
                     UniProtKB/Swiss-Prot (Q9UKX7.2)"
     CDS             1..468
                     /gene="NUP50"
                     /gene_synonym="NPAP60; NPAP60L"
                     /coded_by="NM_007172.4:383..1789"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14062.1"
                     /db_xref="GeneID:10762"
                     /db_xref="HGNC:HGNC:8065"
                     /db_xref="MIM:604646"
ORIGIN      
        1 makrnaekel tdrnwdqede aeevgtfsma seevlknrai kkakrrnvgf esdtggafkg
       61 fkglvvpsgg grfsgfgsga ggkpleglsn gnnitsappf asakaaadpk vafgslaang
      121 pttlvdkvsn pktngdsqqp sssglasska cvgnayhkql aalncsvrdw ivkhvntnpl
      181 cdltpifkdy ekylanieqq hgnsgrnses esnkvaaetq spslfgstkl qqestflfhg
      241 nktedtpdkk mevasekktd psslgatsas fnfgkkvdss vlgslssvpl tgfsfspgns
      301 slfgkdttqs kpvsspfptk plegqaegds geckggdeee ndeppkvvvt evkeedafys
      361 kkcklfykkd nefkekgigt lhlkptanqk tqllvradtn lgnillnvli ppnmpctrtg
      421 knnvlivcvp nppideknat mpvtmlirvk tsedadelhk illekkda
//
LOCUS       NP_067681                235 aa            linear   PRI 20-NOV-2025
DEFINITION  TIR domain-containing adapter molecule 2 [Homo sapiens].
ACCESSION   NP_067681 XP_352588
VERSION     NP_067681.1
DBSOURCE    REFSEQ: accession NM_021649.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Pereira,M. and Gazzinelli,R.T.
  TITLE     Regulation of innate immune signaling by IRAK proteins
  JOURNAL   Front Immunol 14, 1133354 (2023)
   PUBMED   36865541
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Susjan-Leite,P., Ramuta,T.Z., Borsic,E., Orehek,S. and
            Hafner-Bratkovic,I.
  TITLE     Supramolecular organizing centers at the interface of inflammation
            and neurodegeneration
  JOURNAL   Front Immunol 13, 940969 (2022)
   PUBMED   35979366
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Skjesol,A., Yurchenko,M., Bosl,K., Gravastrand,C., Nilsen,K.E.,
            Grovdal,L.M., Agliano,F., Patane,F., Lentini,G., Kim,H., Teti,G.,
            Kumar Sharma,A., Kandasamy,R.K., Sporsheim,B., Starheim,K.K.,
            Golenbock,D.T., Stenmark,H., McCaffrey,M., Espevik,T. and
            Husebye,H.
  TITLE     The TLR4 adaptor TRAM controls the phagocytosis of Gram-negative
            bacteria by interacting with the Rab11-family interacting protein 2
  JOURNAL   PLoS Pathog 15 (3), e1007684 (2019)
   PUBMED   30883606
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Yurchenko,M., Skjesol,A., Ryan,L., Richard,G.M., Kandasamy,R.K.,
            Wang,N., Terhorst,C., Husebye,H. and Espevik,T.
  TITLE     SLAMF1 is required for TLR4-mediated TRAM-TRIF-dependent signaling
            in human macrophages
  JOURNAL   J Cell Biol 217 (4), 1411-1429 (2018)
   PUBMED   29440514
  REMARK    GeneRIF: SLAMF1 is required for TLR4-mediated TRAM-TRIF-dependent
            signaling in human macrophages.
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Oshiumi,H., Sasai,M., Shida,K., Fujita,T., Matsumoto,M. and Seya,T.
  TITLE     TIR-containing adapter molecule (TICAM)-2, a bridging adapter
            recruiting to toll-like receptor 4 TICAM-1 that induces
            interferon-beta
  JOURNAL   J Biol Chem 278 (50), 49751-49762 (2003)
   PUBMED   14519765
  REMARK    GeneRIF: the adapter complex of TICAM-2 and TICAM-1 plays a crucial
            role in lipopolysaccharide-TLR4-mediated activation of IFN-beta
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Fitzgerald,K.A., Rowe,D.C., Barnes,B.J., Caffrey,D.R., Visintin,A.,
            Latz,E., Monks,B., Pitha,P.M. and Golenbock,D.T.
  TITLE     LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll
            adapters TRAM and TRIF
  JOURNAL   J Exp Med 198 (7), 1043-1055 (2003)
   PUBMED   14517278
  REMARK    Erratum:[J Exp Med. 2003 Nov 3;198(9):following 1450]
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Bin,L.H., Xu,L.G. and Shu,H.B.
  TITLE     TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing
            adapter protein involved in TIR signaling
  JOURNAL   J Biol Chem 278 (27), 24526-24532 (2003)
   PUBMED   12721283
  REMARK    GeneRIF: Overexpression of TIRP activates NF-kappaB and potentiates
            IL-1 receptor-mediated NF-kappaB activation
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Yamamoto,M., Sato,S., Mori,K., Hoshino,K., Takeuchi,O., Takeda,K.
            and Akira,S.
  TITLE     Cutting edge: a novel Toll/IL-1 receptor domain-containing adapter
            that preferentially activates the IFN-beta promoter in the
            Toll-like receptor signaling
  JOURNAL   J Immunol 169 (12), 6668-6672 (2002)
   PUBMED   12471095
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Ueno,K., Kumagai,T., Kijima,T., Kishimoto,T. and Hosoe,S.
  TITLE     Cloning and tissue expression of cDNAs from chromosome 5q21-22
            which is frequently deleted in advanced lung cancer
  JOURNAL   Hum Genet 102 (1), 63-68 (1998)
   PUBMED   9490301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA992598.1, AC010226.5, AB097022.1 and DA092564.1.
            
            On Dec 17, 2003 this sequence version replaced XP_352588.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA992598.1, SRR1660807.23442.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467148 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427199.3/ ENSP00000415139.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.3"
     Protein         1..235
                     /product="TIR domain-containing adapter molecule 2"
                     /note="TRIF-related adaptor molecule;
                     NF-kappa-B-activating protein 502; toll-like receptor
                     adaptor protein 3; toll/interleukin-1 receptor (TIR)
                     domain-containing adapter protein; cytoplasmic adaptor;
                     putative NF-kappa-B-activating protein 502; toll like
                     receptor adaptor molecule 2"
                     /calculated_mol_wt=26785
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XR7.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCE.
                     /evidence=ECO:0000269|PubMed:16757566; propagated from
                     UniProtKB/Swiss-Prot (Q86XR7.1)"
     Region          81..200
                     /region_name="TIR_2"
                     /note="TIR domain; pfam13676"
                     /db_xref="CDD:463954"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:25825441; propagated from
                     UniProtKB/Swiss-Prot (Q86XR7.1)"
     CDS             1..235
                     /gene="TICAM2"
                     /gene_synonym="MyD88-4; TICAM-2; TIRAP3; TIRP; TRAM"
                     /coded_by="NM_021649.7:443..1150"
                     /db_xref="CCDS:CCDS4119.1"
                     /db_xref="GeneID:353376"
                     /db_xref="HGNC:HGNC:21354"
                     /db_xref="MIM:608321"
ORIGIN      
        1 mgigkskins cplslswgkr hsvdtspgyh esdskksedl slcnvaehsn ttegptgkqe
       61 gaqsveemfe eeaeeevflk fvilhaeddt dealrvqnll qddfgikpgi ifaempcgrq
      121 hlqnlddavn gsawtilllt enflrdtwcn fqfytslmns vnrqhkynsv ipmrplnnpl
      181 prertpfalq tinaleeesr gfptqverif qesvyktqqt iwketrnmvq rqfia
//
LOCUS       NP_001121693             206 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription cofactor vestigial-like protein 4 isoform d [Homo
            sapiens].
ACCESSION   NP_001121693
VERSION     NP_001121693.1
DBSOURCE    REFSEQ: accession NM_001128221.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,Z., Quan,Y., Hu,M., Xu,Y., Chen,Y., Jin,P., Ma,J., Chen,X.,
            Fan,J., Fan,X., Gong,Y., Li,M. and Wang,Y.
  TITLE     VGLL4-TEAD1 promotes vascular smooth muscle cell differentiation
            from human pluripotent stem cells via TET2
  JOURNAL   J Mol Cell Cardiol 176, 21-32 (2023)
   PUBMED   36657637
  REMARK    GeneRIF: VGLL4-TEAD1 promotes vascular smooth muscle cell
            differentiation from human pluripotent stem cells via TET2.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Geng,H., Liu,G., Hu,J., Li,J., Wang,D., Zou,S. and Xu,X.
  TITLE     HOXB13 suppresses proliferation, migration and invasion, and
            promotes apoptosis of gastric cancer cells through transcriptional
            activation of VGLL4 to inhibit the involvement of TEAD4 in the
            Hippo signaling pathway
  JOURNAL   Mol Med Rep 24 (4) (2021)
   PUBMED   34396425
  REMARK    GeneRIF: HOXB13 suppresses proliferation, migration and invasion,
            and promotes apoptosis of gastric cancer cells through
            transcriptional activation of VGLL4 to inhibit the involvement of
            TEAD4 in the Hippo signaling pathway.
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Mesrouze,Y., Meyerhofer,M., Zimmermann,C., Fontana,P., Erdmann,D.
            and Chene,P.
  TITLE     Biochemical properties of VGLL4 from Homo sapiens and Tgi from
            Drosophila melanogaster and possible biological implications
  JOURNAL   Protein Sci 30 (9), 1871-1881 (2021)
   PUBMED   34075638
  REMARK    GeneRIF: Biochemical properties of VGLL4 from Homo sapiens and Tgi
            from Drosophila melanogaster and possible biological implications.
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Mickle,M., Adhikary,G., Shrestha,S., Xu,W. and Eckert,R.L.
  TITLE     VGLL4 inhibits YAP1/TEAD signaling to suppress the epidermal
            squamous cell carcinoma cancer phenotype
  JOURNAL   Mol Carcinog 60 (7), 497-507 (2021)
   PUBMED   34004031
  REMARK    GeneRIF: VGLL4 inhibits YAP1/TEAD signaling to suppress the
            epidermal squamous cell carcinoma cancer phenotype.
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Jin,H.S., Park,H.S., Shin,J.H., Kim,D.H., Jun,S.H., Lee,C.J. and
            Lee,T.H.
  TITLE     A novel inhibitor of apoptosis protein (IAP)-interacting protein,
            Vestigial-like (Vgl)-4, counteracts apoptosis-inhibitory function
            of IAPs by nuclear sequestration
  JOURNAL   Biochem Biophys Res Commun 412 (3), 454-459 (2011)
   PUBMED   21839727
  REMARK    GeneRIF: Vgl-4 may play a role in the apoptotic pathways by
            regulating translocation of IAPs between different cell
            compartments.
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Teng,A.C., Kuraitis,D., Deeke,S.A., Ahmadi,A., Dugan,S.G.,
            Cheng,B.L., Crowson,M.G., Burgon,P.G., Suuronen,E.J., Chen,H.H. and
            Stewart,A.F.
  TITLE     IRF2BP2 is a skeletal and cardiac muscle-enriched
            ischemia-inducible activator of VEGFA expression
  JOURNAL   FASEB J 24 (12), 4825-4834 (2010)
   PUBMED   20702774
  REMARK    GeneRIF: IRF2BP2 was identifies as a novel VGLL4 partner.
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Chen,H.H., Mullett,S.J. and Stewart,A.F.
  TITLE     Vgl-4, a novel member of the vestigial-like family of transcription
            cofactors, regulates alpha1-adrenergic activation of gene
            expression in cardiac myocytes
  JOURNAL   J Biol Chem 279 (29), 30800-30806 (2004)
   PUBMED   15140898
  REMARK    GeneRIF: Vgl-4 modulates the activity of TEF-1 factors and
            counteracts alpha1-adrenergic activation of gene expression in
            cardiac myocytes
            GeneRIF: A transcriptional cofactor of transcriptional enhancer
            factor-1 (TEF-1) transcription factors.  Interacts with TEF-1
            factors through 2 TDU (tondu) motifs.  Controls gene expression in
            cardiac myocytes.
            GeneRIF: This gene is named Vestigial-like 4, to distinguish it
            from 3 previously described genes Vgl-1, Vgl-2 and Vgl-3. Contains
            2 motifs, found in the Drosophila transcription cofactor Vestigial,
            that interact with the TEF-1 family of transcription factors.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK308761.1, D50911.3 and BU682809.1.
            
            Transcript Variant: This variant (4) contains alternate 5' exon
            structure and it thus differs in the 5' UTR and 5' coding region,
            compared to variant 1. The encoded isoform (d) has a distinct
            N-terminus and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.62588.1,
                                           SRR1660809.240566.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3-p25.2"
     Protein         1..206
                     /product="transcription cofactor vestigial-like protein 4
                     isoform d"
                     /note="Vestigial-like 4; transcription cofactor
                     vestigial-like protein 4; vestigial like 4"
                     /calculated_mol_wt=21574
     Region          <3..140
                     /region_name="VGLL4"
                     /note="Transcription cofactor vestigial-like protein 4;
                     pfam15245"
                     /db_xref="CDD:464585"
     Region          150..165
                     /region_name="TDU"
                     /note="Short repeats in human TONDU, fly vestigial and
                     other proteins; smart00711"
                     /db_xref="CDD:197839"
     CDS             1..206
                     /gene="VGLL4"
                     /gene_synonym="VGL-4"
                     /coded_by="NM_001128221.3:193..813"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS46756.1"
                     /db_xref="GeneID:9686"
                     /db_xref="HGNC:HGNC:28966"
                     /db_xref="MIM:618692"
ORIGIN      
        1 mnktangdcr rdprersrsp ieravaptms lhgshlytsl pslgleqpla ltknsldasr
       61 paglsptltp gerqqnrpsv itcasagarn cnlshcpiah sgcaapgpas yrrppsaatt
      121 cdpvveehfr rslgknykep epapnsvsit gsvddhfaka lgdtwlqika akdgassspe
      181 sasrrgqpas psahmvshsh spsvvs
//
LOCUS       NP_077321                559 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 10 isoform a [Homo sapiens].
ACCESSION   NP_077321
VERSION     NP_077321.3
DBSOURCE    REFSEQ: accession NM_024345.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Zemke,N.R., Hsu,E., Barshop,W.D., Sha,J., Wohlschlegel,J.A. and
            Berk,A.J.
  TITLE     Adenovirus E1A binding to DCAF10 targets proteasomal degradation of
            RUVBL1/2 AAA+ ATPases required for quaternary assembly of
            multiprotein machines, innate immunity, and responses to metabolic
            stress
  JOURNAL   J Virol 97 (12), e0099323 (2023)
   PUBMED   37962355
  REMARK    GeneRIF: Adenovirus E1A binding to DCAF10 targets proteasomal
            degradation of RUVBL1/2 AAA+ ATPases required for quaternary
            assembly of multiprotein machines, innate immunity, and responses
            to metabolic stress.
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Luo,Q., Wu,X., Zhao,P., Nan,Y., Chang,W., Zhu,X., Su,D. and Liu,Z.
  TITLE     OTUD1 Activates Caspase-Independent and Caspase-Dependent Apoptosis
            by Promoting AIF Nuclear Translocation and MCL1 Degradation
  JOURNAL   Adv Sci (Weinh) 8 (8), 2002874 (2021)
   PUBMED   33898171
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY015327.1, BC108686.1, AL138752.5 and CB045943.1.
            
            On Jul 28, 2006 this sequence version replaced NP_077321.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.866751.1,
                                           SRR1660803.67608.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377724.8/ ENSP00000366953.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..559
                     /product="DDB1- and CUL4-associated factor 10 isoform a"
                     /note="WD repeat domain 32; WD repeat-containing protein
                     32"
                     /calculated_mol_wt=60451
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AKB9; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2AKB9; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            134
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          166..205
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          <168..>334
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          172..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..247
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          214..250
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          251..290
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          256..282
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          296..335
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          350..396
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          408..448
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          470..508
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     Region          517..555
                     /region_name="WD40"
                     /note="WD40 repeats; smart00320"
                     /db_xref="CDD:197651"
     Region          526..559
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5QP82.1)"
     CDS             1..559
                     /gene="DCAF10"
                     /gene_synonym="WDR32"
                     /coded_by="NM_024345.5:71..1750"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6613.2"
                     /db_xref="GeneID:79269"
                     /db_xref="HGNC:HGNC:23686"
                     /db_xref="MIM:620295"
ORIGIN      
        1 mfpfgphspg gdgsagagae eptphegqaa atgppsplhp gadathpppp arsprrpgap
       61 slspaprsge lglpgapess tasapgepsp psppcrrpgp dcraksrgrh glgaglggpg
      121 arlfgwlker slgrglfvdp ardnfrtmts lygsihpads vylstrthga vfnleyspdg
      181 svltvaceqt evllfdpiss khiktlseah edcvnnirfl dnrlfatcsd dttialwdlr
      241 klntkvctlh ghtswvknie ydtntrllvt sgfdgnviiw dtnrytedgc phkkffhtrf
      301 lmrmrltpdc skmlistssg yllilhdldl tkslevgsyp ilrarrttss sdlttsssss
      361 gprvsgspch hsdsnssekh msrasqregv sprnslevvt pevlgesdhg ncitslqlhp
      421 kgwatllrcs snsddeectc vyefqegapv rpvsprcslr lthyieeanv grgyikelcf
      481 spdgrmissp hgygirllgf dkqcselvdc lpkeasplrv irslyshndv vlttkfspth
      541 cqiasgclsg rvslyqpkf
//
LOCUS       NP_006742               1256 aa            linear   PRI 20-NOV-2025
DEFINITION  protein ITPRID2 isoform 2 [Homo sapiens].
ACCESSION   NP_006742
VERSION     NP_006742.2
DBSOURCE    REFSEQ: accession NM_006751.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1256)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1256)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1256)
  AUTHORS   Atakpa-Adaji,P., Ivanova,A., Kujawa,K. and Taylor,C.W.
  TITLE     KRAP regulates mitochondrial Ca2+ uptake by licensing IP3 receptor
            activity and stabilizing ER-mitochondrial junctions
  JOURNAL   J Cell Sci 137 (12) (2024)
   PUBMED   38786982
  REMARK    GeneRIF: KRAP regulates mitochondrial Ca2+ uptake by licensing IP3
            receptor activity and stabilizing ER-mitochondrial junctions.
REFERENCE   4  (residues 1 to 1256)
  AUTHORS   Sanli,F., Tatar,A., Gundogdu,B. and Karatas,O.F.
  TITLE     IP3R1 dysregulation via mir-200c-3p/SSFA2 axis contributes to taxol
            resistance in head and neck cancer
  JOURNAL   Eur J Pharmacol 973, 176592 (2024)
   PUBMED   38642666
  REMARK    GeneRIF: IP3R1 dysregulation via mir-200c-3p/SSFA2 axis contributes
            to taxol resistance in head and neck cancer.
REFERENCE   5  (residues 1 to 1256)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   6  (residues 1 to 1256)
  AUTHORS   Fujimoto,T., Koyanagi,M., Baba,I., Nakabayashi,K., Kato,N.,
            Sasazuki,T. and Shirasawa,S.
  TITLE     Analysis of KRAP expression and localization, and genes regulated
            by KRAP in a human colon cancer cell line
  JOURNAL   J Hum Genet 52 (12), 978-984 (2007)
   PUBMED   17934691
  REMARK    GeneRIF: results suggested that KRAP might be a
            cytoskeleton-associated protein involving the structural integrity
            and/or signal transductions in human cancers.
REFERENCE   7  (residues 1 to 1256)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 1256)
  AUTHORS   Inokuchi,J., Komiya,M., Baba,I., Naito,S., Sasazuki,T. and
            Shirasawa,S.
  TITLE     Deregulated expression of KRAP, a novel gene encoding
            actin-interacting protein, in human colon cancer cells
  JOURNAL   J Hum Genet 49 (1), 46-52 (2004)
   PUBMED   14673706
  REMARK    GeneRIF: localized as a membrane-bound form with extracellular
            regions; results suggested KRAP might be involved in the regulation
            of filamentous actin and signals from the outside of the cells
REFERENCE   9  (residues 1 to 1256)
  AUTHORS   Zhu,X. and Naz,R.K.
  TITLE     Cloning and sequencing of cDNA encoding for a human sperm antigen
            involved in fertilization
  JOURNAL   Mol Reprod Dev 51 (2), 176-183 (1998)
   PUBMED   9740325
REFERENCE   10 (residues 1 to 1256)
  AUTHORS   Javed,A.A. and Naz,R.K.
  TITLE     Human cleavage signal-1 protein; cDNA cloning, transcription and
            immunological analysis
  JOURNAL   Gene 112 (2), 205-211 (1992)
   PUBMED   1555770
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009962.11, DB455116.1, DB462183.1, BC052581.1 and BX647967.1.
            
            On Feb 25, 2003 this sequence version replaced NP_006742.1.
            
            Transcript Variant: This variant (2) lacks an exon in the 3'
            region, as compared to variant 1. The resulting isoform (2) has a
            shorter and distinct C-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028706.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.3"
     Protein         1..1256
                     /product="protein ITPRID2 isoform 2"
                     /note="cleavage signal-1 protein; sperm specific antigen
                     2; ki-ras-induced actin-interacting protein; sperm
                     associated antigen 13; KRAS-induced actin-interacting
                     protein; ITPR-interacting domain-containing protein 2;
                     protein ITPRID2"
                     /calculated_mol_wt=137729
     Region          31..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q922B9; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          148..300
                     /region_name="KRAP_IP3R_bind"
                     /note="Ki-ras-induced actin-interacting
                     protein-IP3R-interacting domain; pfam14722"
                     /db_xref="CDD:464280"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          268..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          306..450
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            644
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            668
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            737
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            803
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          806..829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Region          864..1017
                     /region_name="SSFA2_C"
                     /note="Sperm-specific antigen 2 C-terminus; pfam14723"
                     /db_xref="CDD:464281"
     Site            869
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q922B9; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1040
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q922B9; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1055
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q922B9; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q922B9; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1063
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          1094..1137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Region          1154..1215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P28290.3)"
     Site            1156
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     Site            1168
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P28290.3)"
     CDS             1..1256
                     /gene="ITPRID2"
                     /gene_synonym="CS-1; CS1; KRAP; SPAG13; SSFA2"
                     /coded_by="NM_006751.7:338..4108"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2284.1"
                     /db_xref="GeneID:6744"
                     /db_xref="HGNC:HGNC:11319"
                     /db_xref="MIM:118990"
ORIGIN      
        1 mdrplsssae aeeelewqva srrrkawakc rsswqasete dlsteattqd eeedeeedlp
       61 gaqlpaaggr gnvpnekiai wlkdcrtplg asldeqssst lkgvlvrngg sfeddlslga
      121 eanhlhesda qiencnnila kerrlqfhqk grsmnstgsg kssgtvssvs ellelyeedp
      181 eeilynlgfg rdepdiaski psrffnsssf akgidikvfl saqmqrmeve npnyaltsrf
      241 rqievlttva nafsslysqv sgtplqrigs mssvtsnket dppppltrsn tanrlmktls
      301 klnlcvdkte kgessspsps aekgkilnvs vieesgnknd qksqkimkkk esssmlatvk
      361 eevsgssaav tenadsdris deansnfnqg teneqsketq shesklgees giveskldsd
      421 fnisshsele nsselksvhi stpekepcap ltipsirnim tqqkdsfeme evqstegeap
      481 hvpatyqlgl tkskrdhllr tasqhsdssg faedstdcls lnhlqvqesl qamgssadsc
      541 dsettvtslg edlatptaqd qpyfneseee slvplqkgle kaaavadkrk sgsqdfpqcn
      601 tientgtkqs tcspgdhiie iteveedlfp aetvellrea saesdvgkss eseftqytth
      661 hilkslasie akcsdmssen ttgppssmdr vntalqraqm kvcslsnqrm grsllkskdl
      721 lkqrylfaka gyplrrsqsl pttllspvrv vssvnvrlsp gketrcspps ftykytpeee
      781 qelekrvmeh dgqslvksti fispssvkke eapqseaprv eechhgrtpt csrlapppms
      841 qstcslhsih sewqerplce htrtlsthsv pnisgatcsa faspfgcpys hrhatypyrv
      901 csvnppsaie mqlrrvlhdi rnslqnlsqy pmmrgpdpaa apystqkssv lplyentfqe
      961 lqvmrrslnl frtqmmdlel amlrqqtmvy hhmteeerfe vdqlqglrns vrmelqdlel
     1021 qleerllgle eqlravrmps pfrssalmgm cgsrsadnls cpsplnvmep vtelmqeqsy
     1081 lkselglglg emgfeippge ssesvfsqat sesssvcsgp shanrrtgvp stasvgkskt
     1141 plvarkkvfr asvaltptap srtgsvqtpp dlesseevda aegapevvgp kseveeghgk
     1201 lpsmpaaeem hknveqdelq qvirevgmdp iscvilelsm ictgggvica ledtcc
//
LOCUS       NP_001070675            1220 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec31A isoform 1 [Homo sapiens].
ACCESSION   NP_001070675
VERSION     NP_001070675.1
DBSOURCE    REFSEQ: accession NM_001077207.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Tobias,E.S., Lucas-Herald,A.K., Sagar,D., Montezano,A.C.,
            Rios,F.J., De Lucca Camargo,L., Hamilton,G., Gazdagh,G.,
            Diver,L.A., Williams,N., Herzyk,P., Touyz,R.M., Greenfield,A.,
            McGowan,R. and Ahmed,S.F.
  TITLE     SEC31A may be associated with pituitary hormone deficiency and
            gonadal dysgenesis
  JOURNAL   Endocrine 84 (2), 345-349 (2024)
   PUBMED   38400880
  REMARK    GeneRIF: SEC31A may be associated with pituitary hormone deficiency
            and gonadal dysgenesis.
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1220)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1220)
  AUTHORS   Jin,L., Pahuja,K.B., Wickliffe,K.E., Gorur,A., Baumgartel,C.,
            Schekman,R. and Rape,M.
  TITLE     Ubiquitin-dependent regulation of COPII coat size and function
  JOURNAL   Nature 482 (7386), 495-500 (2012)
   PUBMED   22358839
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1220)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1220)
  AUTHORS   Kim,J.H., Hong,J.A., Pih,K.T. and Hwang,I.
  TITLE     Identification and isolation of differentially expressed genes in
            osmotically stressed human oral keratinocytes
  JOURNAL   Arch Oral Biol 46 (4), 335-341 (2001)
   PUBMED   11269867
REFERENCE   8  (residues 1 to 1220)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 1220)
  AUTHORS   Tang,B.L., Zhang,T., Low,D.Y., Wong,E.T., Horstmann,H. and Hong,W.
  TITLE     Mammalian homologues of yeast sec31p. An ubiquitously expressed
            form is localized to endoplasmic reticulum (ER) exit sites and is
            essential for ER-Golgi transport
  JOURNAL   J Biol Chem 275 (18), 13597-13604 (2000)
   PUBMED   10788476
REFERENCE   10 (residues 1 to 1220)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC021105.13 and AC108469.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene shares similarity with
            the yeast Sec31 protein, and is a component of the outer layer of
            the coat protein complex II (COPII). The encoded protein is
            involved in vesicle budding from the endoplasmic reticulum (ER) and
            contains multiple WD repeats near the N-terminus and a proline-rich
            region in the C-terminal half. It associates with the protein
            encoded by the SEC13 homolog, nuclear pore and COPII coat complex
            component (SEC13), and is required for ER-Golgi transport.
            Monoubiquitylation of this protein by CUL3-KLHL12 was found to
            regulate the size of COPII coats to accommodate unusually shaped
            cargo. Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (5) encodes the longest isoform
            (1). Both variants 5 and 10 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.119071.1,
                                           SRR1660805.167194.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000395310.7/ ENSP00000378721.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..1220
                     /product="protein transport protein Sec31A isoform 1"
                     /note="yeast Sec31p homolog; protein transport protein
                     Sec31A; web1-like protein; SEC31 homolog A, COPII coat
                     complex component; SEC31-related protein A; SEC31-like
                     protein 1; SEC31 homolog A, COPII coating complex
                     component"
                     /calculated_mol_wt=132884
     Region          4..47
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          13..332
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          13..65
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(26,40,46..47,52..53,91,95,101..102,117,121,139,144,
                     150..151,164,185,190,196..197,209..210,231,235,244..245,
                     258..259,277,282,288..289,301..302,320,325,331..332)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          68..111
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          70..119
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..160
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          125..162
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          161..471
                     /region_name="Interaction with SEC13.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          172..208
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          214..257
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          263..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          306..331
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            532
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Region          <573..>696
                     /region_name="ACE1-Sec16-like"
                     /note="Ancestral coatomer element 1 (ACE1) of COPII coat
                     complex assembly protein Sec16; cl14807"
                     /db_xref="CDD:449359"
     Site            order(574..578,580,582,593,595,596..597,599..600,604,610,
                     618,630,633,658..659)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:187736"
     Region          791..908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          800..1113
                     /region_name="Interaction with PDCD6.
                     /evidence=ECO:0000269|PubMed:16957052"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          <800..>1098
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          842..848
                     /region_name="ALG-2-binding site motif-2 (ABS-2)"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Region          924..1096
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94979.3)"
     Site            1161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94979.3)"
     Site            1163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O94979.3)"
     CDS             1..1220
                     /gene="SEC31A"
                     /gene_synonym="ABP125; ABP130; HPBKS; HSPC275; HSPC334;
                     NEDSOSB; SEC31L1"
                     /coded_by="NM_001077207.4:71..3733"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3596.1"
                     /db_xref="GeneID:22872"
                     /db_xref="HGNC:HGNC:17052"
                     /db_xref="MIM:610257"
ORIGIN      
        1 mklkevdrta mqawspaqnh piylatgtsa qqldatfstn asleifeldl sdpsldmksc
       61 atfssshryh kliwgpykmd skgdvsgvli aggengniil ydpskiiagd kevviaqndk
      121 htgpvraldv nifqtnlvas ganeseiyiw dlnnfatpmt pgaktqpped isciawnrqv
      181 qhilasasps gratvwdlrk nepiikvsdh snrmhcsgla whpdvatqmv laseddrlpv
      241 iqmwdlrfas splrvlenha rgilaiawsm adpelllscg kdakilcsnp ntgevlyelp
      301 tntqwcfdiq wcprnpavls aasfdgrisv ysimggstdg lrqkqvdkls ssfgnldpfg
      361 tgqplpplqi pqqtaqhsiv lplkkppkwi rrpvgasfsf ggklvtfenv rmpshqgaeq
      421 qqqqhhvfis qvvtekefls rsdqlqqavq sqgfinycqk kidasqtefe knvwsflkvn
      481 feddsrgkyl ellgyrkedl gkkialalnk vdganvalkd sdqvaqsdge espaaeeqll
      541 gehikeekee seflpssggt fnisvsgdid glitqalltg nfesavdlcl hdnrmadaii
      601 laiaggqell artqkkyfak sqskitrlit avvmknwkei vescdlknwr ealaavltya
      661 kpdefsalcd llgtrleneg dsllqtqacl cyicagnvek lvacwtkaqd gshplslqdl
      721 iekvvilrka vqltqamdts tvgvllaakm sqyanllaaq gsiaaalafl pdntnqpnim
      781 qlrdrlcraq gepvaghesp kipyekqqlp kgrpgpvagh hqmprvqtqq yyphgenppp
      841 pgfimhgnvn pnaagqlpts pghmhtqvpp ypqpqpyqpa qpypfgtggs amyrpqqpva
      901 pptsnaypnt pyissassyt gqsqlyaaqh qassptsspa tsfppppssg asfqhggpga
      961 ppsssayalp pgttgtlpaa selpasqrtg pqngwndppa lnrvpkkkkm penfmppvpi
     1021 tspimnplgd pqsqmlqqqp sapvplssqs sfpqphlpgg qpfhgvqqpl gqtgmppsfs
     1081 kpniegapga pigntfqhvq slptkkitkk pipdehlilk ttfedliqrc lssatdpqtk
     1141 rklddaskrl eflydklreq tlsptitsgl hniarsietr nysegltmht hivstsnfse
     1201 tsafmpvlkv vltqanklgv
//
LOCUS       NP_001167539             671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001167539
VERSION     NP_001167539.1
DBSOURCE    REFSEQ: accession NM_001174068.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.128699.1, AK313086.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001174068.2:188..2203"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_877437                374 aa            linear   PRI 20-NOV-2025
DEFINITION  formylglycine-generating enzyme isoform 1 precursor [Homo sapiens].
ACCESSION   NP_877437
VERSION     NP_877437.2
DBSOURCE    REFSEQ: accession NM_182760.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Zhang,P., Liu,Z., Wang,Y.Y., Luo,H.J., Yang,C.Z., Shen,H., Wu,H.T.,
            Li,J.H., Zhao,H.X. and Ran,Q.S.
  TITLE     SUMF1 overexpression promotes tumorous cell growth and migration
            and is correlated with the immune status of patients with glioma
  JOURNAL   Aging (Albany NY) 16 (5), 4699-4722 (2024)
   PUBMED   38460946
  REMARK    GeneRIF: SUMF1 overexpression promotes tumorous cell growth and
            migration and is correlated with the immune status of patients with
            glioma.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Liang,S., Gao,H., He,T., Li,L., Zhang,X., Zhao,L., Chen,J., Xie,Y.,
            Bao,J., Gao,Y., Dai,E. and Wang,Y.
  TITLE     Association between SUMF1 polymorphisms and COVID-19 severity
  JOURNAL   BMC Genom Data 24 (1), 34 (2023)
   PUBMED   37344788
  REMARK    GeneRIF: Association between SUMF1 polymorphisms and COVID-19
            severity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Cosma,M.P., Pepe,S., Parenti,G., Settembre,C., Annunziata,I.,
            Wade-Martins,R., Di Domenico,C., Di Natale,P., Mankad,A., Cox,B.,
            Uziel,G., Mancini,G.M., Zammarchi,E., Donati,M.A., Kleijer,W.J.,
            Filocamo,M., Carrozzo,R., Carella,M. and Ballabio,A.
  TITLE     Molecular and functional analysis of SUMF1 mutations in multiple
            sulfatase deficiency
  JOURNAL   Hum Mutat 23 (6), 576-581 (2004)
   PUBMED   15146462
  REMARK    GeneRIF: mutational analysis of SUMF1 in 20 Multiple sulfatase
            deficiency patients of different ethnic origin
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Cosma,M.P., Pepe,S., Annunziata,I., Newbold,R.F., Grompe,M.,
            Parenti,G. and Ballabio,A.
  TITLE     The multiple sulfatase deficiency gene encodes an essential and
            limiting factor for the activity of sulfatases
  JOURNAL   Cell 113 (4), 445-456 (2003)
   PUBMED   12757706
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Dierks,T., Schmidt,B., Borissenko,L.V., Peng,J., Preusser,A.,
            Mariappan,M. and von Figura,K.
  TITLE     Multiple sulfatase deficiency is caused by mutations in the gene
            encoding the human C(alpha)-formylglycine generating enzyme
  JOURNAL   Cell 113 (4), 435-444 (2003)
   PUBMED   12757705
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Cross,S.H., Charlton,J.A., Nan,X. and Bird,A.P.
  TITLE     Purification of CpG islands using a methylated DNA binding column
  JOURNAL   Nat Genet 6 (3), 236-244 (1994)
   PUBMED   8012384
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Schlotawa,L., Adang,L., De Castro,M. and Ahrens-Nicklas,R.
  TITLE     Multiple Sulfatase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30896912
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC121122.2, AC034191.6 and
            CA413741.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 7, 2003 this sequence version replaced NP_877437.1.
            
            Summary: This gene encodes an enzyme that catalyzes the hydrolysis
            of sulfate esters by oxidizing a cysteine residue in the substrate
            sulfatase to an active site 3-oxoalanine residue, which is also
            known as C-alpha-formylglycine. Mutations in this gene cause
            multiple sulfatase deficiency, a lysosomal storage disorder.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.48703.1,
                                           SRR1803615.30731.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272902.10/ ENSP00000272902.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.1"
     Protein         1..374
                     /product="formylglycine-generating enzyme isoform 1
                     precursor"
                     /EC_number="1.8.3.7"
                     /note="FGly-generating enzyme;
                     C-alpha-formylglycine-generating enzyme 1"
                     /calculated_mol_wt=37353
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3222
     mat_peptide     34..374
                     /product="formylglycine-generating enzyme isoform 1"
                     /calculated_mol_wt=37353
     Region          61..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBK3.3)"
     Region          91..367
                     /region_name="FGE-sulfatase"
                     /note="Sulfatase-modifying factor enzyme 1; pfam03781"
                     /db_xref="CDD:397722"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:15657036,
                     ECO:0000269|PubMed:15907468, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (Q8NBK3.3)"
     Region          341..360
                     /region_name="Interaction with sulfatases.
                     /evidence=ECO:0000269|PubMed:16368756"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBK3.3)"
     CDS             1..374
                     /gene="SUMF1"
                     /gene_synonym="AAPA3037; FGE; UNQ3037"
                     /coded_by="NM_182760.4:25..1149"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2564.1"
                     /db_xref="GeneID:285362"
                     /db_xref="HGNC:HGNC:20376"
                     /db_xref="MIM:607939"
ORIGIN      
        1 maapalglvc grcpelglvl lllllsllcg aagsqeagtg agagslagsc gcgtpqrpga
       61 hgssaaahry sreanapgpv pgerqlahsk mvpipagvft mgtddpqikq dgeaparrvt
      121 idafymdaye vsntefekfv nstgylteae kfgdsfvfeg mlseqvktni qqavaaapww
      181 lpvkganwrh pegpdstilh rpdhpvlhvs wndavayctw agkrlpteae weyscrgglh
      241 nrlfpwgnkl qpkgqhyani wqgefpvtnt gedgfqgtap vdafppngyg lynivgnawe
      301 wtsdwwtvhh sveetlnpkg ppsgkdrvkk ggsymchrsy cyryrcaars qntpdssasn
      361 lgfrcaadrl ptmd
//
LOCUS       NP_006132                492 aa            linear   PRI 20-NOV-2025
DEFINITION  cytoplasmic dynein 1 light intermediate chain 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006132
VERSION     NP_006132.1
DBSOURCE    REFSEQ: accession NM_006141.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Rahman,F., Johnson,J.L., Zhang,J., He,J., Pestonjamasp,K.,
            Cherqui,S. and Catz,S.D.
  TITLE     DYNC1LI2 regulates localization of the chaperone-mediated autophagy
            receptor LAMP2A and improves cellular homeostasis in cystinosis
  JOURNAL   Autophagy 18 (5), 1108-1126 (2022)
   PUBMED   34643468
  REMARK    GeneRIF: DYNC1LI2 regulates localization of the chaperone-mediated
            autophagy receptor LAMP2A and improves cellular homeostasis in
            cystinosis.
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Sharma,A., Dagar,S. and Mylavarapu,S.V.S.
  TITLE     Transgelin-2 and phosphoregulation of the LIC2 subunit of dynein
            govern mitotic spindle orientation
  JOURNAL   J Cell Sci 133 (12) (2020)
   PUBMED   32467330
  REMARK    GeneRIF: Transgelin-2 and phosphoregulation of the LIC2 subunit of
            dynein govern mitotic spindle orientation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Pfister,K.K., Fisher,E.M., Gibbons,I.R., Hays,T.S., Holzbaur,E.L.,
            McIntosh,J.R., Porter,M.E., Schroer,T.A., Vaughan,K.T.,
            Witman,G.B., King,S.M. and Vallee,R.B.
  TITLE     Cytoplasmic dynein nomenclature
  JOURNAL   J Cell Biol 171 (3), 411-413 (2005)
   PUBMED   16260502
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Hughes,S.M., Vaughan,K.T., Herskovits,J.S. and Vallee,R.B.
  TITLE     Molecular analysis of a cytoplasmic dynein light intermediate chain
            reveals homology to a family of ATPases
  JOURNAL   J Cell Sci 108 (Pt 1), 17-24 (1995)
   PUBMED   7738094
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL708642.1, AF035812.1, BM805417.1, BC022934.1, BX648863.1 and
            AC018557.9.
            
            Summary: Cytoplasmic dynein is a microtubule-associated motor
            protein (Hughes et al., 1995 [PubMed 7738094]). See DYNC1H1 (MIM
            600112) for general information about dyneins.[supplied by OMIM,
            Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.16809.1,
                                           SRR1803612.262817.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258198.7/ ENSP00000258198.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..492
                     /product="cytoplasmic dynein 1 light intermediate chain 2
                     isoform 1"
                     /note="dynein, cytoplasmic, light intermediate polypeptide
                     2; cytoplasmic dynein 1 light intermediate chain 2; LIC-2;
                     LIC53/55; dynein light intermediate chain 2, cytosolic"
                     /calculated_mol_wt=53968
     Region          30..488
                     /region_name="DLIC"
                     /note="Dynein light intermediate chain (DLIC); pfam05783"
                     /db_xref="CDD:368612"
     Region          187..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43237.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Region          371..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43237.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Site            397
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Region          437..492
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43237.1)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43237.1)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43237.1)"
     CDS             1..492
                     /gene="DYNC1LI2"
                     /gene_synonym="DNCLI2; LIC2"
                     /coded_by="NM_006141.3:19..1497"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10818.1"
                     /db_xref="GeneID:1783"
                     /db_xref="HGNC:HGNC:2966"
                     /db_xref="MIM:611406"
ORIGIN      
        1 mapvgvekkl llgpngpava aagdltseee egqslwssil sevstrarsk lpsgknilvf
       61 gedgsgkttl mtklqgaehg kkgrgleyly lsvhdedrdd htrcnvwild gdlyhkgllk
      121 favsaeslpe tlvifvadms rpwtvmeslq kwasvlrehi dkmkippekm relerkfvkd
      181 fqdymepeeg cqgspqrrgp ltsgsdeenv alplgdnvlt hnlgipvlvv ctkcdavsvl
      241 ekehdyrdeh ldfiqshlrr fclqygaali ytsvkeeknl dllykyivhk tygfhfttpa
      301 lvvekdavfi pagwdnekki ailhenfttv kpedayedfi vkppvrklvh dkelaaedeq
      361 vflmkqqsll akqpatptra sespargpsg sprtqgrggp asvpssspgt svkkpdpnik
      421 nnaasegvla sffnsllskk tgspgspgag gvqstakksg qktvlsnvqe eldrmtrkpd
      481 smvtnssten ea
//
LOCUS       NP_057403                275 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 7a [Homo sapiens].
ACCESSION   NP_057403
VERSION     NP_057403.1
DBSOURCE    REFSEQ: accession NM_016319.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Poh,J., Ponsford,A.H., Boyd,J., Woodsmith,J., Stelzl,U., Wanker,E.,
            Harper,N., MacEwan,D. and Sanderson,C.M.
  TITLE     A functionally defined high-density NRF2 interactome reveals new
            conditional regulators of ARE transactivation
  JOURNAL   Redox Biol 37, 101686 (2020)
   PUBMED   32911434
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Wei,N., Serino,G. and Deng,X.W.
  TITLE     The COP9 signalosome: more than a protease
  JOURNAL   Trends Biochem Sci 33 (12), 592-600 (2008)
   PUBMED   18926707
  REMARK    Review article
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125494.2, AF210052.1,
            BC011789.2 and BQ008460.1.
            
            Summary: This gene encodes a component of the COP9 signalosome, an
            evolutionarily conserved multi-subunit protease that regulates the
            activity of the ubiquitin conjugation pathway. Alternatively
            spliced transcript variants that encode the same protein have been
            described. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF210052.1, SRR1803616.50048.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..275
                     /product="COP9 signalosome complex subunit 7a"
                     /note="COP9 complex subunit 7a; COP9 constitutive
                     photomorphogenic homolog subunit 7A; dermal
                     papilla-derived protein 10; JAB1-containing signalosome
                     subunit 7a"
                     /calculated_mol_wt=30146
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:18850735; propagated from
                     UniProtKB/Swiss-Prot (Q9UBW8.1)"
     Region          87..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     Region          227..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBW8.1)"
     CDS             1..275
                     /gene="COPS7A"
                     /gene_synonym="CSN7; CSN7A; SGN7a"
                     /coded_by="NM_016319.4:151..978"
                     /db_xref="CCDS:CCDS8558.1"
                     /db_xref="GeneID:50813"
                     /db_xref="HGNC:HGNC:16758"
                     /db_xref="MIM:616009"
ORIGIN      
        1 msaevkvtgq nqeqflllak sakgaalatl ihqvleapgv yvfgelldmp nvrelaesdf
       61 astfrlltvf aygtyadyla earnlpplte aqknklrhls vvtlaakvkc ipyavlleal
      121 alrnvrqled lvieavyadv lrgsldqrnq rlevdysigr diqrqdlsai artlqewcvg
      181 cevvlsgiee qvsranqhke qqlglkqqie sevanlkkti kvttaaaaaa tsqdpeqhlt
      241 elrepapgtn qrqpskkask gkglrgsaki wsksn
//
LOCUS       NP_001340199             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340199
VERSION     NP_001340199.1
DBSOURCE    REFSEQ: accession NM_001353270.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.290464.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353270.1:657..1193"
                     /note="isoform 2 is encoded by transcript variant 32"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_001155052             359 aa            linear   PRI 20-NOV-2025
DEFINITION  POC1 centriolar protein homolog A isoform 2 [Homo sapiens].
ACCESSION   NP_001155052
VERSION     NP_001155052.1
DBSOURCE    REFSEQ: accession NM_001161580.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Li,Z.H., Li,J.Y., Wu,Z.T., Zhu,Y.J., Zhuo,T., Nong,J.S., Qian,J.,
            Peng,H.J., Dai,L., Wang,Y.Y., Chen,M.W. and Zeng,X.C.
  TITLE     Upregulation of POC1A in lung adenocarcinoma promotes tumour
            progression and predicts poor prognosis
  JOURNAL   J Cell Mol Med 28 (6), e18135 (2024)
   PUBMED   38429900
  REMARK    GeneRIF: Upregulation of POC1A in lung adenocarcinoma promotes
            tumour progression and predicts poor prognosis.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Perge,K., Capel,E., Villanueva,C., Gautheron,J., Diallo,S.,
            Auclair,M., Rondeau,S., Morichon,R., Brioude,F., Jeru,I., Rossi,M.,
            Nicolino,M. and Vigouroux,C.
  TITLE     Ciliopathy due to POC1A deficiency: clinical and metabolic
            features, and cellular modeling
  JOURNAL   Eur J Endocrinol 190 (2), 151-164 (2024)
   PUBMED   38245004
  REMARK    GeneRIF: Ciliopathy due to POC1A deficiency: clinical and metabolic
            features, and cellular modeling.
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Zhao,Q., Gao,S., Chen,X. and Zhu,X.
  TITLE     POC1A, prognostic biomarker of immunosuppressive microenvironment
            in cancer
  JOURNAL   Aging (Albany NY) 14 (12), 5195-5210 (2022)
   PUBMED   35748773
  REMARK    GeneRIF: POC1A, prognostic biomarker of immunosuppressive
            microenvironment in cancer.
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Mericq,V., Huang-Doran,I., Al-Naqeb,D., Basaure,J., Castiglioni,C.,
            de Bruin,C., Hendriks,Y., Bertini,E., Alkuraya,F.S., Losekoot,M.,
            Al-Rubeaan,K., Semple,R.K. and Wit,J.M.
  TITLE     Biallelic POC1A variants cause syndromic severe insulin resistance
            with muscle cramps
  JOURNAL   Eur J Endocrinol 186 (5), 543-552 (2022)
   PUBMED   35234134
  REMARK    GeneRIF: Biallelic POC1A variants cause syndromic severe insulin
            resistance with muscle cramps.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Sarig,O., Nahum,S., Rapaport,D., Ishida-Yamamoto,A.,
            Fuchs-Telem,D., Qiaoli,L., Cohen-Katsenelson,K., Spiegel,R.,
            Nousbeck,J., Israeli,S., Borochowitz,Z.U., Padalon-Brauch,G.,
            Uitto,J., Horowitz,M., Shalev,S. and Sprecher,E.
  TITLE     Short stature, onychodysplasia, facial dysmorphism, and
            hypotrichosis syndrome is caused by a POC1A mutation
  JOURNAL   Am J Hum Genet 91 (2), 337-342 (2012)
   PUBMED   22840363
  REMARK    GeneRIF: Short stature, onychodysplasia, facial dysmorphism, and
            hypotrichosis syndrome is caused by a POC1A mutation.
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Pearson,C.G., Osborn,D.P., Giddings,T.H. Jr., Beales,P.L. and
            Winey,M.
  TITLE     Basal body stability and ciliogenesis requires the conserved
            component Poc1
  JOURNAL   J Cell Biol 187 (6), 905-920 (2009)
   PUBMED   20008567
REFERENCE   9  (residues 1 to 359)
  AUTHORS   Keller,L.C., Geimer,S., Romijn,E., Yates,J. 3rd, Zamora,I. and
            Marshall,W.F.
  TITLE     Molecular architecture of the centriole proteome: the conserved
            WD40 domain protein POC1 is required for centriole duplication and
            length control
  JOURNAL   Mol Biol Cell 20 (4), 1150-1166 (2009)
   PUBMED   19109428
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Hames,R.S., Hames,R., Prosser,S.L., Euteneuer,U., Lopes,C.A.,
            Moore,W., Woodland,H.R. and Fry,A.M.
  TITLE     Pix1 and Pix2 are novel WD40 microtubule-associated proteins that
            colocalize with mitochondria in Xenopus germ plasm and centrosomes
            in human cells
  JOURNAL   Exp Cell Res 314 (3), 574-589 (2008)
   PUBMED   18068700
  REMARK    GeneRIF: Based on these data, we propose that Pix1 and Pix2 are
            microtubule-associated adaptor proteins that likely contribute to a
            range of developmental and cell division processes.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC110877.1, CA944751.1 and
            AC115284.4.
            
            Summary: POC1 proteins contain an N-terminal WD40 domain and a
            C-terminal coiled coil domain and are part of centrosomes. They
            play an important role in basal body and cilia formation. This gene
            encodes one of the two POC1 proteins found in humans. Mutations in
            this gene result in short stature, onychodysplasia, facial
            dysmorphism, and hypotrichosis (SOFT) syndrome. [provided by
            RefSeq, Sep 2012].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            3' coding region, compared to variant 1. The encoded isoform (2) is
            shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC110877.1, SRR11853564.19339.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2163105 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..359
                     /product="POC1 centriolar protein homolog A isoform 2"
                     /note="WD repeat domain 51A; WD repeat-containing protein
                     51A; POC1 centriolar protein homolog A; proteome of
                     centriole protein 1A"
                     /calculated_mol_wt=39716
     Region          <6..298
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          23..59
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          64..100
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..184
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          190..226
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          232..255
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..359
                     /gene="POC1A"
                     /gene_synonym="PIX2; SOFT; WDR51A"
                     /coded_by="NM_001161580.2:52..1131"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54592.1"
                     /db_xref="GeneID:25886"
                     /db_xref="HGNC:HGNC:24488"
                     /db_xref="MIM:614783"
ORIGIN      
        1 maapcaedps lerhfkghrd avtcvdfsin tkqlasgsmd sclmvwhmkp qsrayrftgh
       61 kdavtcvnfs psghllasgs rdktvriwvp nvkgestvfr ahtatvrsvh fcsdgqsfvt
      121 asddktvkvw athrqkflfs lsqhinwvrc akfspdgrli vsasddktvk lwdkssrecv
      181 hsycehggfv tyvdfhpsgt ciaaagmdnt vkvwdvrthr llqhyqlhsa avnglsfhps
      241 gnylitassd stlkildlme grllytlhgh qgpattvafs rtgeyfasgg sdeqvmvwks
      301 nfdivdhgev tkvprppatl assmgnltvs ileqrltlte dklkqclenq qlimqratp
//
LOCUS       NP_001626                695 aa            linear   PRI 20-NOV-2025
DEFINITION  amphiphysin isoform 1 [Homo sapiens].
ACCESSION   NP_001626
VERSION     NP_001626.1
DBSOURCE    REFSEQ: accession NM_001635.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Yao,X., Zhang,C., Zhang,Y., Geng,J., Bai,S., Hao,Y. and Guan,Y.
  TITLE     Amphiphysin-IgG autoimmune sciatic neuropathy and facial neuropathy
            related to primary central nervous system lymphoma: A case report
  JOURNAL   J Neuroimmunol 382, 578156 (2023)
   PUBMED   37556888
  REMARK    GeneRIF: Amphiphysin-IgG autoimmune sciatic neuropathy and facial
            neuropathy related to primary central nervous system lymphoma: A
            case report.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Zhang,X., Zou,L., Meng,L., Xiong,M., Pan,L., Chen,G., Zheng,Y.,
            Xiong,J., Wang,Z., Duong,D.M., Zhang,Z., Cao,X., Wang,T., Tang,L.,
            Ye,K. and Zhang,Z.
  TITLE     Amphiphysin I cleavage by asparagine endopeptidase leads to tau
            hyperphosphorylation and synaptic dysfunction
  JOURNAL   Elife 10, e65301 (2021)
   PUBMED   34018922
  REMARK    GeneRIF: Amphiphysin I cleavage by asparagine endopeptidase leads
            to tau hyperphosphorylation and synaptic dysfunction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 695)
  AUTHORS   David,C., McPherson,P.S., Mundigl,O. and de Camilli,P.
  TITLE     A role of amphiphysin in synaptic vesicle endocytosis suggested by
            its binding to dynamin in nerve terminals
  JOURNAL   Proc Natl Acad Sci U S A 93 (1), 331-335 (1996)
   PUBMED   8552632
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Yamamoto,R., Li,X., Winter,S., Francke,U. and Kilimann,M.W.
  TITLE     Primary structure of human amphiphysin, the dominant autoantigen of
            paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH)
            to chromosome 7p13-p14
  JOURNAL   Hum Mol Genet 4 (2), 265-268 (1995)
   PUBMED   7757077
REFERENCE   8  (residues 1 to 695)
  AUTHORS   David,C., Solimena,M. and De Camilli,P.
  TITLE     Autoimmunity in stiff-Man syndrome with breast cancer is targeted
            to the C-terminal region of human amphiphysin, a protein similar to
            the yeast proteins, Rvs167 and Rvs161
  JOURNAL   FEBS Lett 351 (1), 73-79 (1994)
   PUBMED   8076697
REFERENCE   9  (residues 1 to 695)
  AUTHORS   De Camilli,P., Thomas,A., Cofiell,R., Folli,F., Lichte,B.,
            Piccolo,G., Meinck,H.M., Austoni,M., Fassetta,G., Bottazzo,G.,
            Bates,D., Cartlidge,N., Solimena,M., Kilimann,M.W. et al.
  TITLE     The synaptic vesicle-associated protein amphiphysin is the 128-kD
            autoantigen of Stiff-Man syndrome with breast cancer
  JOURNAL   J Exp Med 178 (6), 2219-2223 (1993)
   PUBMED   8245793
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Lichte,B., Veh,R.W., Meyer,H.E. and Kilimann,M.W.
  TITLE     Amphiphysin, a novel protein associated with synaptic vesicles
  JOURNAL   EMBO J 11 (7), 2521-2530 (1992)
   PUBMED   1628617
  REMARK    Erratum:[EMBO J 1992 Oct;11(10):3809]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA125756.1, BC034376.1 and
            AC007245.3.
            
            Summary: This gene encodes a protein associated with the
            cytoplasmic surface of synaptic vesicles. A subset of patients with
            stiff-man syndrome who were also affected by breast cancer are
            positive for autoantibodies against this protein. Alternate
            splicing of this gene results in two transcript variants encoding
            different isoforms. Additional splice variants have been described,
            but their full length sequences have not been determined. A
            pseudogene of this gene is found on chromosome 11.[provided by
            RefSeq, Nov 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.274200.1,
                                           SRR1803615.115526.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356264.7/ ENSP00000348602.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..695
                     /product="amphiphysin isoform 1"
                     /note="amphiphysin (Stiff-Mann syndrome with breast cancer
                     128kD autoantigen); amphiphysin I"
                     /calculated_mol_wt=76126
     Region          26..236
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(45,48..49,53,56,59..60,63,73..74,76..77,80..81,
                     83..84,87,95,192,195..196,198,203..204,206..207,210..211,
                     213..214,217..218,220..221,225,228)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(68,75,134,137,140..141,165)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          244..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49418.1)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Region          <456..626
                     /region_name="rne"
                     /note="ribonuclease E; Reviewed; PRK10811"
                     /db_xref="CDD:236766"
     Region          486..617
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49418.1)"
     Site            506
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     Region          623..694
                     /region_name="SH3_Amphiphysin_I"
                     /note="Src Homology 3 domain of Amphiphysin I; cd12140"
                     /db_xref="CDD:213016"
     Site            order(634..640,659,661..664,687,689..690)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213016"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TQF7; propagated from
                     UniProtKB/Swiss-Prot (P49418.1)"
     CDS             1..695
                     /gene="AMPH"
                     /gene_synonym="AMPH1"
                     /coded_by="NM_001635.4:23..2110"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5456.1"
                     /db_xref="GeneID:273"
                     /db_xref="HGNC:HGNC:471"
                     /db_xref="MIM:600418"
ORIGIN      
        1 madiktgifa knvqkrlnra qekvlqklgk adetkdeqfe eyvqnfkrqe aegtrlqrel
       61 rgylaaikgm qeasmkltes lhevyepdwy gredvkmvge kcdvlwedfh qklvdgsllt
      121 ldtylgqfpd iknriakrsr klvdydsarh hlealqsskr kdesriskae eefqkaqkvf
      181 eefnvdlqee lpslwsrrvg fyvntfknvs sleakfhkei avlchklyev mtklgdqhad
      241 kaftiqgaps dsgplriakt psppeepspl psptaspnht lapaspapar prspsqtrkg
      301 ppvpplpkvt ptkelqqeni isffednfvp eisvttpsqn evpevkkeet lldldfdpfk
      361 pevtpagsag vthspmsqtl pwdlwttstd lvqpasggsf ngftqpqdts lftmqtdqsm
      421 icnlaeseqa pptepkaeep laavtpavgl dlgmdtraee pveeaviipg adadaavgtl
      481 vsaaegapge eaeaekatvp agegvsleea kigtettega esaqpeaeel eatvpqekvi
      541 psvviepasn heeegeneit igaepkette daappgptse tpelateqkp iqdpqptpsa
      601 pamgaadqla sareasqelp pgflykvetl hdfeaansde ltlqrgdvvl vvpsdseadq
      661 dagwlvgvke sdwlqyrdla tykglfpenf trrld
//
LOCUS       NP_004872                332 aa            linear   PRI 20-NOV-2025
DEFINITION  quinone oxidoreductase PIG3 isoform 1 [Homo sapiens].
ACCESSION   NP_004872
VERSION     NP_004872.2
DBSOURCE    REFSEQ: accession NM_004881.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Chaudhry,S.R., Lopes,J., Levin,N.K., Kalpage,H. and Tainsky,M.A.
  TITLE     Germline mutations in apoptosis pathway genes in ovarian cancer;
            the functional role of a TP53I3 (PIG3) variant in ROS production
            and DNA repair
  JOURNAL   Cell Death Discov 7 (1), 62 (2021)
   PUBMED   33782397
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Gu,M.M., Gao,D., Yao,P.A., Yu,L., Yang,X.D., Xing,C.G., Zhou,J.,
            Shang,Z.F. and Li,M.
  TITLE     p53-inducible gene 3 promotes cell migration and invasion by
            activating the FAK/Src pathway in lung adenocarcinoma
  JOURNAL   Cancer Sci 109 (12), 3783-3793 (2018)
   PUBMED   30281878
  REMARK    GeneRIF: Study found that PIG3 expression was positively associated
            with lymph node metastasis from lung adenocarcinoma (LUAD) but not
            from lung squamous cell carcinoma (LUSC). Further data revealed a
            role for PIG3 in inducing LUAD metastasis, and its role as a new
            FAK regulator, suggesting that it could be considered as a novel
            prognostic biomarker.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Chu,Y., Li,D., Zhang,H., Ding,J., Xu,P., Qiu,X. and Zhang,H.
  TITLE     PIG3 suppresses gastric cancer proliferation by regulating p53-
            mediated apoptosis
  JOURNAL   J Biol Regul Homeost Agents 32 (5), 1185-1189 (2018)
   PUBMED   30334411
  REMARK    GeneRIF: expression of PIG3 is frequently reduced in gastric cancer
            (GC) tissue, and PIG3 suppressed human GC growth through p53-
            mediated apoptosis; PIG3 may act as a potential diagnostic marker
            and a potential therapeutic target of GC
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Li,M., Li,S., Liu,B., Gu,M.M., Zou,S., Xiao,B.B., Yu,L., Ding,W.Q.,
            Zhou,P.K., Zhou,J. and Shang,Z.F.
  TITLE     PIG3 promotes NSCLC cell mitotic progression and is associated with
            poor prognosis of NSCLC patients
  JOURNAL   J Exp Clin Cancer Res 36 (1), 39 (2017)
   PUBMED   28259183
  REMARK    GeneRIF: Results revealed that PIG3 expression levels positively
            correlated with poor prognosis of non-small cell lung cancer
            (NSCLC) patients and indicate that PIG3 promotes NSCLC progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Quan,J., Li,Y., Jin,M., Chen,D., Yin,X. and Jin,M.
  TITLE     Suppression of p53-inducible gene 3 is significant for glioblastoma
            progression and predicts poor patient prognosis
  JOURNAL   Tumour Biol 39 (3), 1010428317694572 (2017)
   PUBMED   28351326
  REMARK    GeneRIF: our data suggest that high expression of p53-inducible
            gene 3 is significant for glioblastoma inhibition and p53-inducible
            gene 3 independently indicates good prognosis in patients, which
            might be a novel prognostic biomarker or potential therapeutic
            target in glioblastoma.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Nicholls,C.D., Shields,M.A., Lee,P.W., Robbins,S.M. and
            Beattie,T.L.
  TITLE     UV-dependent alternative splicing uncouples p53 activity and PIG3
            gene function through rapid proteolytic degradation
  JOURNAL   J Biol Chem 279 (23), 24171-24178 (2004)
   PUBMED   15067011
  REMARK    GeneRIF: p53 activity and PIG3 gene function are uncoupled by
            UV-dependent alternative splicing through rapid proteolytic
            degradation
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Pospisilova,S., Siligan,C., Ban,J., Jug,G. and Kovar,H.
  TITLE     Constitutive and DNA damage inducible activation of pig3 and MDM2
            genes by tumor-derived p53 mutant C277Y
  JOURNAL   Mol Cancer Res 2 (5), 296-304 (2004)
   PUBMED   15192123
  REMARK    GeneRIF: suppression of p53-C277Y by RNAi reduced pig3 promoter
            activity, RNA, and protein expression
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Contente,A., Dittmer,A., Koch,M.C., Roth,J. and Dobbelstein,M.
  TITLE     A polymorphic microsatellite that mediates induction of PIG3 by p53
  JOURNAL   Nat Genet 30 (3), 315-320 (2002)
   PUBMED   11919562
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Flatt,P.M., Polyak,K., Tang,L.J., Scatena,C.D., Westfall,M.D.,
            Rubinstein,L.A., Yu,J., Kinzler,K.W., Vogelstein,B., Hill,D.E. and
            Pietenpol,J.A.
  TITLE     p53-dependent expression of PIG3 during proliferation, genotoxic
            stress, and reversible growth arrest
  JOURNAL   Cancer Lett 156 (1), 63-72 (2000)
   PUBMED   10840161
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Polyak,K., Xia,Y., Zweier,J.L., Kinzler,K.W. and Vogelstein,B.
  TITLE     A model for p53-induced apoptosis
  JOURNAL   Nature 389 (6648), 300-305 (1997)
   PUBMED   9305847
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223382.1, BT007149.1 and
            CN285566.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2002 this sequence version replaced NP_004872.1.
            
            Summary: The protein encoded by this gene is similar to
            oxidoreductases, which are enzymes involved in cellular responses
            to oxidative stresses and irradiation. This gene is induced by the
            tumor suppressor p53 and is thought to be involved in p53-mediated
            cell death. It contains a p53 consensus binding site in its
            promoter region and a downstream pentanucleotide microsatellite
            sequence. P53 has been shown to transcriptionally activate this
            gene by interacting with the downstream pentanucleotide
            microsatellite sequence. The microsatellite is polymorphic, with a
            varying number of pentanucleotide repeats directly correlated with
            the extent of transcriptional activation by p53. It has been
            suggested that the microsatellite polymorphism may be associated
            with differential susceptibility to cancer. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, May 2011].
            
            Transcript Variant: This variant (1) and variant 2 encode the same
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223382.1, AF010309.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159080 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000238721.9/ ENSP00000238721.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..332
                     /product="quinone oxidoreductase PIG3 isoform 1"
                     /EC_number="1.6.5.5"
                     /note="quinone oxidoreductase homolog; p53-induced gene 3
                     protein; quinone oxidoreductase PIG3; NADPH:quinone
                     reductase PIG3"
                     /calculated_mol_wt=35405
     Region          1..328
                     /region_name="p53_inducible_oxidoreductase"
                     /note="PIG3 p53-inducible quinone oxidoreductase; cd05276"
                     /db_xref="CDD:176180"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9;
                     propagated from UniProtKB/Swiss-Prot (Q53FA7.2)"
     Site            order(40..41,123,127,130,148,151..153,172..173,177,192,
                     216..217,238..239,241,264..266,317,322)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176180"
     CDS             1..332
                     /gene="TP53I3"
                     /gene_synonym="PIG3"
                     /coded_by="NM_004881.5:509..1507"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1708.1"
                     /db_xref="GeneID:9540"
                     /db_xref="HGNC:HGNC:19373"
                     /db_xref="MIM:605171"
ORIGIN      
        1 mlavhfdkpg gpenlyvkev akpspgegev llkvaasaln radlmqrqgq ydpppgasni
       61 lgleasghva elgpgcqghw kigdtamall pgggqaqyvt vpegllmpip egltltqaaa
      121 ipeawltafq llhlvgnvqa gdyvlihagl sgvgtaaiql trmagaiplv tagsqkklqm
      181 aeklgaaagf nykkedfsea tlkftkgagv nlildciggs yweknvncla ldgrwvlygl
      241 mgggdingpl fskllfkrgs litsllrsrd nkykqmlvna fteqilphfs tegpqrllpv
      301 ldriypvtei qeahkymean knigkivlel pq
//
LOCUS       NP_001341754             803 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator
            1-alpha isoform 1 [Homo sapiens].
ACCESSION   NP_001341754
VERSION     NP_001341754.1
DBSOURCE    REFSEQ: accession NM_001354825.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Liang,F. and Huang,S.
  TITLE     PGC-1alpha inhibits NLRP3 signaling through transcriptional
            activation of POP1 to alleviate inflammation and strengthen
            osteogenic differentiation of lipopolysaccharide-induced human
            periodontal stem cells
  JOURNAL   Prostaglandins Other Lipid Mediat 174, 106853 (2024)
   PUBMED   38763227
  REMARK    GeneRIF: PGC-1alpha inhibits NLRP3 signaling through
            transcriptional activation of POP1 to alleviate inflammation and
            strengthen osteogenic differentiation of lipopolysaccharide-induced
            human periodontal stem cells.
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Kuang,J., Fang,J., Hu,S., Yang,X. and Fan,X.
  TITLE     MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS OF
            SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF PGC-1Alpha
  JOURNAL   Shock 62 (3), 426-436 (2024)
   PUBMED   38888503
  REMARK    GeneRIF: MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS
            OF SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF
            PGC-1Alpha.
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Mesarosova,L., Scheper,M., Iyer,A., Anink,J.J., Mills,J.D. and
            Aronica,E.
  TITLE     miR-193b-3p/ PGC-1alpha pathway regulates an insulin dependent
            anti-inflammatory response in Parkinson's disease
  JOURNAL   Neurobiol Dis 199, 106587 (2024)
   PUBMED   38950713
  REMARK    GeneRIF: miR-193b-3p/ PGC-1alpha pathway regulates an insulin
            dependent anti-inflammatory response in Parkinson's disease.
REFERENCE   4  (residues 1 to 803)
  AUTHORS   Yu,T., Gao,Q., Zhang,G., Li,T., Liu,X., Li,C., Zheng,L., Sun,X.,
            Wu,J., Cao,H., Bi,F., Wang,R., Liang,H., Li,X., Zhou,Y., Lv,L. and
            Shan,H.
  TITLE     lncRNA Gm20257 alleviates pathological cardiac hypertrophy by
            modulating the PGC-1alpha-mitochondrial complex IV axis
  JOURNAL   Front Med 18 (4), 664-677 (2024)
   PUBMED   38926249
  REMARK    GeneRIF: lncRNA Gm20257 alleviates pathological cardiac hypertrophy
            by modulating the PGC-1alpha-mitochondrial complex IV axis.
REFERENCE   5  (residues 1 to 803)
  AUTHORS   Zhou,S., Taskintuna,K., Hum,J., Gulati,J., Olaya,S., Steinman,J.
            and Golestaneh,N.
  TITLE     PGC-1alpha repression dysregulates lipid metabolism and induces
            lipid droplet accumulation in retinal pigment epithelium
  JOURNAL   Cell Death Dis 15 (6), 385 (2024)
   PUBMED   38824126
  REMARK    GeneRIF: PGC-1alpha repression dysregulates lipid metabolism and
            induces lipid droplet accumulation in retinal pigment epithelium.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Esterbauer,H., Oberkofler,H., Krempler,F. and Patsch,W.
  TITLE     Human peroxisome proliferator activated receptor gamma coactivator
            1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
            localization, and tissue expression
  JOURNAL   Genomics 62 (1), 98-102 (1999)
   PUBMED   10585775
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Puigserver,P., Adelmant,G., Wu,Z., Fan,M., Xu,J., O'Malley,B. and
            Spiegelman,B.M.
  TITLE     Activation of PPARgamma coactivator-1 through transcription factor
            docking
  JOURNAL   Science 286 (5443), 1368-1371 (1999)
   PUBMED   10558993
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Wu,Z., Puigserver,P., Andersson,U., Zhang,C., Adelmant,G.,
            Mootha,V., Troy,A., Cinti,S., Lowell,B., Scarpulla,R.C. and
            Spiegelman,B.M.
  TITLE     Mechanisms controlling mitochondrial biogenesis and respiration
            through the thermogenic coactivator PGC-1
  JOURNAL   Cell 98 (1), 115-124 (1999)
   PUBMED   10412986
REFERENCE   9  (residues 1 to 803)
  AUTHORS   Puigserver,P., Wu,Z., Park,C.W., Graves,R., Wright,M. and
            Spiegelman,B.M.
  TITLE     A cold-inducible coactivator of nuclear receptors linked to
            adaptive thermogenesis
  JOURNAL   Cell 92 (6), 829-839 (1998)
   PUBMED   9529258
REFERENCE   10 (residues 1 to 803)
  AUTHORS   Spanos,N.P., Spillane,J. and McPeake,J.D.
  TITLE     Cognitive strategies and response to suggestion in hypnotic and
            task-motivated subjects
  JOURNAL   Am J Clin Hypn 18 (4), 254-262 (1976)
   PUBMED   1258810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC115110.3, AC006229.17 and
            AC092834.3.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that regulates the genes involved in energy metabolism.
            This protein interacts with PPARgamma, which permits the
            interaction of this protein with multiple transcription factors.
            This protein can interact with, and regulate the activities of,
            cAMP response element binding protein (CREB) and nuclear
            respiratory factors (NRFs). It provides a direct link between
            external physiological stimuli and the regulation of mitochondrial
            biogenesis, and is a major factor that regulates muscle fiber type
            determination. This protein may be also involved in controlling
            blood pressure, regulating cellular cholesterol homoeostasis, and
            the development of obesity. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5), as well as variant 1, encodes
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ772117.1, SRR14038194.2964872.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..803
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-alpha isoform 1"
                     /note="ligand effect modulator-6; L-PGC-1alpha; PPAR gamma
                     coactivator variant form; PGC-1-alpha; PPARGC-1-alpha;
                     PPARAGCIalpha; PPARgamma coactivator 1alpha"
                     /calculated_mol_wt=91582
     Region          641..676
                     /region_name="Complexin_NTD"
                     /note="N-terminal SNARE complex binding domain of the
                     complexin family of SNARE regulators; cl45908"
                     /db_xref="CDD:459253"
     Region          680..770
                     /region_name="RRM_PPARGC1A"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-alpha
                     (PGC-1alpha, or PPARGC-1-alpha) and similar proteins;
                     cd12623"
                     /db_xref="CDD:410034"
     CDS             1..803
                     /gene="PPARGC1A"
                     /gene_synonym="LEM6; PGC-1(alpha); PGC-1alpha; PGC-1v;
                     PGC1; PGC1A; PPARGC1"
                     /coded_by="NM_001354825.2:631..3042"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="GeneID:10891"
                     /db_xref="HGNC:HGNC:9237"
                     /db_xref="MIM:604517"
ORIGIN      
        1 mdetsprlee dwkkvlqrea gwqcaalvge dqplcpdlpe ldlseldvnd ldtdsflggl
       61 kwcsdqseii snqynnepsn ifekideene anllavltet ldslpvdedg lpsfdaltdg
      121 dvttdneasp ssmpdgtppp qeaeepsllk klllapantq lsynecsgls tqnhanhnhr
      181 irtnpaivkt enswsnkaks icqqqkpqrr pcsellkylt tnddpphtkp tenrnssrdk
      241 ctskkkshtq sqsqhlqakp ttlslpltpe spndpkgspf enktiertls velsgtaglt
      301 ppttpphkan qdnpfraspk lksscktvvp ppskkpryse ssgtqgnnst kkgpeqsely
      361 aqlskssvlt ggheerktkr pslrlfgdhd ycqsinskte ilinisqelq dsrqlenkdv
      421 ssdwqgqics stdsdqcylr etleaskqvs pcstrkqlqd qeiraelnkh fghpsqavfd
      481 deadktgelr dsdfsneqfs klpmfinsgl amdglfddse desdklsypw dgtqsyslfn
      541 vspscssfns pcrdsvsppk slfsqrpqrm rsrsrsfsrh rscsrspysr srsrspgsrs
      601 ssrscyyyes shyrhrthrn splyvrsrsr spysrrpryd syeeyqherl kreeyrreye
      661 kreserakqr erqrqkaiee rrviyvgkir pdttrtelrd rfevfgeiee ctvnlrddgd
      721 sygfityryt cdafaaleng ytlrrsnetd felyfcgrkq ffksnyadld snsddfdpas
      781 tkskydsldf dsllkeaqrs lrr
//
LOCUS       NP_001457                565 aa            linear   PRI 20-NOV-2025
DEFINITION  frizzled-2 precursor [Homo sapiens].
ACCESSION   NP_001457
VERSION     NP_001457.1
DBSOURCE    REFSEQ: accession NM_001466.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 565)
  AUTHORS   Tophkhane,S.S., Fu,K., Verheyen,E.M. and Richman,J.M.
  TITLE     Craniofacial studies in chicken embryos confirm the pathogenicity
            of human FZD2 variants associated with Robinow syndrome
  JOURNAL   Dis Model Mech 17 (6) (2024)
   PUBMED   38967226
  REMARK    GeneRIF: Craniofacial studies in chicken embryos confirm the
            pathogenicity of human FZD2 variants associated with Robinow
            syndrome.
REFERENCE   2  (residues 1 to 565)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 565)
  AUTHORS   Han,Z., Ren,H., Sun,J., Jin,L., Wang,Q., Guo,C. and Tian,Z.
  TITLE     Integrated weighted gene coexpression network analysis identifies
            Frizzled 2 (FZD2) as a key gene in invasive malignant pleomorphic
            adenoma
  JOURNAL   J Transl Med 20 (1), 15 (2022)
   PUBMED   34986855
  REMARK    GeneRIF: Integrated weighted gene coexpression network analysis
            identifies Frizzled 2 (FZD2) as a key gene in invasive malignant
            pleomorphic adenoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 565)
  AUTHORS   Gonzalez-Fernandez,C., Gonzalez,P., Andres-Benito,P., Ferrer,I. and
            Rodriguez,F.J.
  TITLE     Wnt Signaling Alterations in the Human Spinal Cord of Amyotrophic
            Lateral Sclerosis Cases: Spotlight on Fz2 and Wnt5a
  JOURNAL   Mol Neurobiol 56 (10), 6777-6791 (2019)
   PUBMED   30924074
  REMARK    GeneRIF: Fz2 and Wnt5a, might be involved in human Amyotrophic
            lateral sclerosis pathology.
REFERENCE   5  (residues 1 to 565)
  AUTHORS   Huang,L., Luo,E.L., Xie,J., Gan,R.H., Ding,L.C., Su,B.H., Zhao,Y.,
            Lin,L.S., Zheng,D.L. and Lu,Y.G.
  TITLE     FZD2 regulates cell proliferation and invasion in tongue squamous
            cell carcinoma
  JOURNAL   Int J Biol Sci 15 (11), 2330-2339 (2019)
   PUBMED   31595151
  REMARK    GeneRIF: FZD2 acts as an oncogene in tongue cancer, promoting cell
            growth, invasion and migration.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 565)
  AUTHORS   Li,C., Chen,H., Hu,L., Xing,Y., Sasaki,T., Villosis,M.F., Li,J.,
            Nishita,M., Minami,Y. and Minoo,P.
  TITLE     Ror2 modulates the canonical Wnt signaling in lung epithelial cells
            through cooperation with Fzd2
  JOURNAL   BMC Mol Biol 9, 11 (2008)
   PUBMED   18215320
  REMARK    GeneRIF: Ror2 positively modulates Wnt3a-activated canonical
            signaling in a lung carcinoma, H441 cell line. This activity of
            Ror2 is dependent on cooperative interactions with Fzd2 but not
            Fzd7.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 565)
  AUTHORS   Sagara,N., Toda,G., Hirai,M., Terada,M. and Katoh,M.
  TITLE     Molecular cloning, differential expression, and chromosomal
            localization of human frizzled-1, frizzled-2, and frizzled-7
  JOURNAL   Biochem Biophys Res Commun 252 (1), 117-122 (1998)
   PUBMED   9813155
REFERENCE   8  (residues 1 to 565)
  AUTHORS   Tanaka,S., Akiyoshi,T., Mori,M., Wands,J.R. and Sugimachi,K.
  TITLE     A novel frizzled gene identified in human esophageal carcinoma
            mediates APC/beta-catenin signals
  JOURNAL   Proc Natl Acad Sci U S A 95 (17), 10164-10169 (1998)
   PUBMED   9707618
REFERENCE   9  (residues 1 to 565)
  AUTHORS   Zhao,Z., Lee,C.C., Baldini,A. and Caskey,C.T.
  TITLE     A human homologue of the Drosophila polarity gene frizzled has been
            identified and mapped to 17q21.1
  JOURNAL   Genomics 27 (2), 370-373 (1995)
   PUBMED   7558010
REFERENCE   10 (residues 1 to 565)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC052266.1, AC103703.5,
            AW023425.1 and AI376463.1.
            
            Summary: This intronless gene is a member of the frizzled gene
            family. Members of this family encode seven-transmembrane domain
            proteins that are receptors for the wingless type MMTV integration
            site family of signaling proteins. This gene encodes a protein that
            is coupled to the beta-catenin canonical signaling pathway.
            Competition between the wingless-type MMTV integration site family,
            member 3A and wingless-type MMTV integration site family, member 5A
            gene products for binding of this protein is thought to regulate
            the beta-catenin-dependent and -independent pathways. [provided by
            RefSeq, Dec 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC052266.1, AB017364.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315323.5/ ENSP00000323901.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..565
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..565
                     /product="frizzled-2 precursor"
                     /note="frizzled 2, seven transmembrane spanning receptor;
                     frizzled-2; frizzled homolog 2; frizzled family receptor
                     2"
                     /calculated_mol_wt=61135
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14332.1)"
                     /calculated_mol_wt=2437
     mat_peptide     24..565
                     /product="Frizzled-2. /id=PRO_0000012978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
                     /calculated_mol_wt=61135
     Region          35..161
                     /region_name="CRD_FZ2"
                     /note="Cysteine-rich Wnt-binding domain (CRD) of the
                     frizzled 2 (Fz2) receptor; cd07464"
                     /db_xref="CDD:143573"
     Site            order(46,48..50,52..54)
                     /site_type="other"
                     /note="putative Wnt binding site [polypeptide binding]"
                     /db_xref="CDD:143573"
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29748286,
                     ECO:0007744|PDB:6C0B; propagated from UniProtKB/Swiss-Prot
                     (Q14332.1)"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14332.1)"
     Region          160..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          234..563
                     /region_name="7tmF_FZD2"
                     /note="class F frizzled subfamily 2, member of
                     7-transmembrane G protein-coupled receptors; cd15245"
                     /db_xref="CDD:320373"
     Site            order(235,244,294,314,396,401,403,406..407,412,487,
                     490..491,516,521,524..525)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320373"
     Region          243..268
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320373"
     Site            248..268
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          277..298
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320373"
     Site            280..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          328..354
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320373"
     Site            328..348
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          371..387
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320373"
     Region          409..438
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320373"
     Site            415..435
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          458..485
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320373"
     Site            462..482
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          514..539
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320373"
     Site            520..540
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          543..548
                     /region_name="Lys-Thr-X-X-X-Trp motif, mediates
                     interaction with the PDZ domain of Dvl family members.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     Region          563..565
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14332.1)"
     CDS             1..565
                     /gene="FZD2"
                     /gene_synonym="fz-2; Fz2; fzE2; hFz2; OMOD2"
                     /coded_by="NM_001466.4:206..1903"
                     /db_xref="CCDS:CCDS11484.1"
                     /db_xref="GeneID:2535"
                     /db_xref="HGNC:HGNC:4040"
                     /db_xref="MIM:600667"
ORIGIN      
        1 mrprsalprl llpllllpaa gpaqfhgekg isipdhgfcq pisiplctdi aynqtimpnl
       61 lghtnqedag levhqfyplv kvqcspelrf flcsmyapvc tvleqaippc rsicerarqg
      121 cealmnkfgf qwperlrceh fprhgaeqic vgqnhsedga pallttappp glqpgaggtp
      181 ggpggggapp ryatlehpfh cprvlkvpsy lsykflgerd caapceparp dgsmffsqee
      241 trfarlwilt wsvlccastf ftvttylvdm qrfryperpi iflsgcytmv svayiagfvl
      301 qervvcnerf sedgyrtvvq gtkkegctil fmmlyffsma ssiwwvilsl twflaagmkw
      361 gheaieansq yfhlaawavp avktitilam gqidgdllsg vcfvglnsld plrgfvlapl
      421 fvylfigtsf llagfvslfr irtimkhdgt kteklerlmv rigvfsvlyt vpativiacy
      481 fyeqafrehw erswvsqhck slaipcpahy tprmspdftv ymikylmtli vgitsgfwiw
      541 sgktlhswrk fytrltnsrh gettv
//
LOCUS       NP_001275961             464 aa            linear   PRI 20-NOV-2025
DEFINITION  kallistatin isoform 1 [Homo sapiens].
ACCESSION   NP_001275961 XP_005267819
VERSION     NP_001275961.1
DBSOURCE    REFSEQ: accession NM_001289032.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Kim,H., Suh,G.J., Kwon,W.Y., Kim,K.S., Jung,Y.S., Kim,T. and
            Park,H.
  TITLE     Kallistatin deficiency exacerbates neuronal damage after cardiac
            arrest
  JOURNAL   Sci Rep 14 (1), 4279 (2024)
   PUBMED   38383562
  REMARK    GeneRIF: Kallistatin deficiency exacerbates neuronal damage after
            cardiac arrest.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Wang,Y., Chen,X.Y., Shang,K., Xu,Q., Li,Y.X., DU,Y. and Zhuan,L.
  TITLE     [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism]
  JOURNAL   Zhonghua Nan Ke Xue 28 (11), 976-984 (2022)
   PUBMED   37846113
  REMARK    GeneRIF: [Relationship of the kallistatin gene expression with male
            spermatogenic dysfunction and its possible mechanism].
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Cho,I., Lee,K.N., Joo,E., Kim,Y.M., Kim,T.E. and Park,K.H.
  TITLE     Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes
  JOURNAL   Am J Reprod Immunol 88 (3), e13584 (2022)
   PUBMED   35772987
  REMARK    GeneRIF: Plasma E-selectin and kallistatin as predictive markers of
            histologic chorioamnionitis in women with preterm premature rupture
            of membranes.
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Krishna,S.M., Li,J., Wang,Y., Moran,C.S., Trollope,A., Huynh,P.,
            Jose,R., Biros,E., Ma,J. and Golledge,J.
  TITLE     Kallistatin limits abdominal aortic aneurysm by attenuating
            generation of reactive oxygen species and apoptosis
  JOURNAL   Sci Rep 11 (1), 17451 (2021)
   PUBMED   34465809
  REMARK    GeneRIF: Kallistatin limits abdominal aortic aneurysm by
            attenuating generation of reactive oxygen species and apoptosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Chen,L.M., Song,Q., Chao,L. and Chao,J.
  TITLE     Cellular localization of tissue kallikrein and kallistatin mRNAs in
            human kidney
  JOURNAL   Kidney Int 48 (3), 690-697 (1995)
   PUBMED   7474653
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Chai,K.X., Ward,D.C., Chao,J. and Chao,L.
  TITLE     Molecular cloning, sequence analysis, and chromosomal localization
            of the human protease inhibitor 4 (kallistatin) gene (PI4)
  JOURNAL   Genomics 23 (2), 370-378 (1994)
   PUBMED   7835886
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Chai,K.X., Chen,L.M., Chao,J. and Chao,L.
  TITLE     Kallistatin: a novel human serine proteinase inhibitor. Molecular
            cloning, tissue distribution, and expression in Escherichia coli
  JOURNAL   J Biol Chem 268 (32), 24498-24505 (1993)
   PUBMED   8227002
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Zhou,G.X., Chao,L. and Chao,J.
  TITLE     Kallistatin: a novel human tissue kallikrein inhibitor.
            Purification, characterization, and reactive center sequence
  JOURNAL   J Biol Chem 267 (36), 25873-25880 (1992)
   PUBMED   1334488
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Wang,M.Y., Day,J., Chao,L. and Chao,J.
  TITLE     Human kallistatin, a new tissue kallikrein-binding protein:
            purification and characterization
  JOURNAL   Adv Exp Med Biol 247B, 1-8 (1989)
   PUBMED   2558505
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK309586.1 and BC014992.1.
            
            On Jan 10, 2014 this sequence version replaced XP_005267819.1.
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK309586.1, SRR14038197.1289347.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.13"
     Protein         1..464
                     /product="kallistatin isoform 1"
                     /note="protease inhibitor 4 (kallistatin); serine (or
                     cysteine) proteinase inhibitor, clade A (alpha-1
                     antiproteinase, antitrypsin), member 4; serpin A4;
                     kallikrein inhibitor; peptidase inhibitor 4; serpin
                     peptidase inhibitor, clade A (alpha-1 antiproteinase,
                     antitrypsin), member 4; testicular secretory protein Li
                     22; sserpin family A member 4"
                     /calculated_mol_wt=52363
     Region          81..463
                     /region_name="serpinA4_KST"
                     /note="serpin family A member 4, kallistatin; cd19552"
                     /db_xref="CDD:381020"
     Site            order(411..422,424..439)
                     /site_type="other"
                     /note="reactive center loop (RCL)"
                     /db_xref="CDD:381020"
     CDS             1..464
                     /gene="SERPINA4"
                     /gene_synonym="KAL; kallistatin; KLST; KST; PI-4; PI4"
                     /coded_by="NM_001289032.2:275..1669"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:5267"
                     /db_xref="HGNC:HGNC:8948"
                     /db_xref="MIM:147935"
ORIGIN      
        1 mpgdpekppp gthswyraal tegqgllaan pglrvqrmhl idylllllvg llalshgqlh
       61 vehdgescsn sshqqiletg egspslkiap anadfafrfy yliasetpgk niffsplsis
      121 aayamlslga cshsrsqile glgfnltels esdvhrgfqh llhtlnlpgh gletrvgsal
      181 flshnlkfla kflndtmavy eaklfhtnfy dtvgtiqlin dhvkketrgk ivdlvselkk
      241 dvlmvlvnyi yfkalwekpf issrttpkdf yvdenttvrv pmmlqdqehh wylhdrylpc
      301 svlrmdykgd atvffilpnq gkmreieevl tpemlmrwnn llrkrnfykk lelhlpkfsi
      361 sgsyvldqil prlgftdlfs kwadlsgitk qqkleasksf hkatldvdea gteaaaatsf
      421 aikffsaqtn rhilrfnrpf lvvifststq svlflgkvvd ptkp
//
LOCUS       NP_001307764            1907 aa            linear   PRI 20-NOV-2025
DEFINITION  C-myc promoter-binding protein isoform 3 [Homo sapiens].
ACCESSION   NP_001307764 XP_005254176
VERSION     NP_001307764.1
DBSOURCE    REFSEQ: accession NM_001320835.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1907)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1907)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1907)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1907)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1907)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1907)
  AUTHORS   Yoshimura,S., Gerondopoulos,A., Linford,A., Rigden,D.J. and
            Barr,F.A.
  TITLE     Family-wide characterization of the DENN domain Rab GDP-GTP
            exchange factors
  JOURNAL   J Cell Biol 191 (2), 367-381 (2010)
   PUBMED   20937701
REFERENCE   7  (residues 1 to 1907)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 1907)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 1907)
  AUTHORS   Semova,N., Kapanadze,B., Corcoran,M., Kutsenko,A., Baranova,A. and
            Semov,A.
  TITLE     Molecular cloning, structural analysis, and expression of a human
            IRLB, MYC promoter-binding protein: new DENN domain-containing
            protein family emerges
  JOURNAL   Genomics 82 (3), 343-354 (2003)
   PUBMED   12906859
REFERENCE   10 (residues 1 to 1907)
  AUTHORS   Stasiv,Y.Z., Mashkova,T.D., Chernov,B.K., Sokolova,I.V., Itkes,A.V.
            and Kisselev,L.L.
  TITLE     Cloning of a cDNA encoding a human protein which binds a sequence
            in the c-myc gene similar to the interferon-stimulated response
            element
  JOURNAL   Gene 145 (2), 267-272 (1994)
   PUBMED   8056341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011939.9.
            
            On Mar 9, 2016 this sequence version replaced XP_005254176.1.
            
            Summary: This gene encodes a DENN domain-containing protein that
            may function as a guanine nucleotide exchange factor that
            specifically activates ras-related protein Rab-10. This protein
            also contains a interferon stimulated response element-binding
            domain and may be involved in regulating the v-myc avian
            myelocytomatosis viral (MYC) oncogene. Alternate splicing results
            in multiple transcript variants. A pseudogene of this gene is found
            on chromosome 8. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            compared to variant 1. The encoded isoform (3) is longer than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1439223.1,
                                           SRR14038197.499883.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000443035.8/ ENSP00000391167.4
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..1907
                     /product="C-myc promoter-binding protein isoform 3"
                     /note="c-myc promoter binding protein; DENN
                     domain-containing protein 4A; DENN/MADD domain containing
                     4A"
                     /calculated_mol_wt=213645
     Region          194..276
                     /region_name="uDENN"
                     /note="Domain always found upstream of DENN domain, found
                     in a variety of signalling proteins; smart00800"
                     /db_xref="CDD:214824"
     Region          308..492
                     /region_name="DENN"
                     /note="DENN (AEX-3) domain; pfam02141"
                     /db_xref="CDD:460461"
     Region          559..632
                     /region_name="dDENN"
                     /note="Domain always found downstream of DENN domain,
                     found in a variety of signalling proteins; smart00801"
                     /db_xref="CDD:129037"
     Region          808..848
                     /region_name="PPR_2"
                     /note="PPR repeat family; pfam13041"
                     /db_xref="CDD:463778"
     Region          810..839
                     /region_name="PPR repeat"
                     /note="PPR repeat [structural motif]"
                     /db_xref="CDD:276811"
     CDS             1..1907
                     /gene="DENND4A"
                     /gene_synonym="IRLB; MYCPBP"
                     /coded_by="NM_001320835.1:386..6109"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92025.1"
                     /db_xref="GeneID:10260"
                     /db_xref="HGNC:HGNC:24321"
                     /db_xref="MIM:600382"
ORIGIN      
        1 miedkgprva dyfvvagltd vskpleeeih fndachkvak pkepitdvsv iikslgeevp
       61 qdyicidvtp tglsadlnng slvgpqiylc yrrgrdkppl tdlgvlydwk erlkqgceii
      121 qstpygrpan isgstssqri yityrrasen mtqntlavtd iciiipskge spphtfckvd
      181 knlnnsmwgs avylcykksv aktntvsyka glicrypqed yesfslpesv plfclpmgat
      241 iecwpsnsky plpvfstfvl tgasaekvyg aaiqfyepys eenltekqrl llgltsadgk
      301 sdssktihtn kcicllshwp ffdafrkflt flyrysisgp hvlpiekhis hfmhkvpfps
      361 pqrprilvql sphdnlilsq pvssplplsg gkfstllqnl gpenavtllv favtehkili
      421 hslrpsvlts vtealvsmif pfhwpcpyvp lcplaladvl sapcpfivgi dsryfdlydp
      481 ppdvscvdvd tntisqigdk knvawkilpk kpcknlmntl nnlhqqlakl qqrprddglm
      541 dlaindydfn sgkrlhmidl eiqeaflffm asilkgyrsy lrpitqapse tatdaaslfa
      601 lqaflrsrdr shqkfynmmt ktqmfirfie ecsfvsdkda slaffddcvd kvdmdksgev
      661 rlieldesfk sehtvfvtpp eiphlpngee pplqysyngf pvlrnnlfer pegflqakkn
      721 klpskssspn splpmfrrtk qeiksahkia kryssipqmw srcllrhcyg lwficlpayv
      781 kvchskvral ktaydvlkkm qskkmdppde vcyrilmqlc gqydqpvlav rvlfemqkag
      841 idpnaitygy ynkavlestw psrsrsgyfl wtkvrnvvlg vtqfkralkk hahlsqttls
      901 adgsdldavs hgsmdsghgt htveqapfnt glikvyatdd rsstggqsdl gynslskdev
      961 rrgdtstedi qeekdkkgsd csslsesest kgsadclpkl syqnsssivr ltgtsnnsag
     1021 kisgesmest pelllissle dtnetrniqs rcfrkrhksd netnlqqqvv wgnrnrnlsg
     1081 gvlmgfmlnr inqeatpgdi veklgadaki lsnviskstr pntldigkpp lrskrdslek
     1141 essdddtpfd gsnyladkvd spvifdledl dsetdvskag cvatqnpkri qrmnssfsvk
     1201 pfektdvatg fdplsllvae teqqqkeeee ededdsksis tpsarrdlae eivmymnnms
     1261 spltsrtpsi dlqracddkl nkkspplvka crrsslppns pkpvrltksk sytkseekpr
     1321 drlwsspafs ptcpfreesq dtlthsspsf nldtllvpkl dvlrnsmfta gkgvaekask
     1381 wysrftmytt sskdqssdrt slssvgaqds estsltdedv chelegpiss qetsatsgtk
     1441 ridlsrisle ssaslegsls kfalpgksev tssfnasntn ifqnyamevl isscsrcrtc
     1501 dclvhdeeim agwtaddsnl nttcpfcgni flpflnieir dlrrpgryfl ksspstenmh
     1561 fpssissqtr qscistsasg ldtsalsvqg nfdlnskskl qenfctrsiq ipanrsktam
     1621 skcpifpmar sistsgpldk edtgrqklis tgslpatlqg atdslglewh lpspdpvtvp
     1681 ylsplvvwke lesllenegd haitvadfvd hhpivfwnlv wyfrrldlps nlpglilsse
     1741 hcnkyskipr hcmsedskyv liqmlwdnmk lhqdpgqply ilwnahtqky pmvhllqksd
     1801 nsfnqellks mvksikmndv ygpmsqilet lnkcphfkrq rslyreilfl slvalgreni
     1861 didafdkeyk maydrltpsq vksthncdrp pstgvmecrk tfgepyl
//
LOCUS       NP_008984                181 aa            linear   PRI 20-NOV-2025
DEFINITION  CD160 antigen precursor [Homo sapiens].
ACCESSION   NP_008984
VERSION     NP_008984.1
DBSOURCE    REFSEQ: accession NM_007053.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Li,M., Wan,Z.X., Tang,Y.Y., Liang,X.H. and Tang,Y.L.
  TITLE     TIM-3/Galectin-9 and CD160 expression in salivary adenoid cystic
            carcinoma
  JOURNAL   Oral Dis 30 (4), 2262-2274 (2024)
   PUBMED   37455567
  REMARK    GeneRIF: TIM-3/Galectin-9 and CD160 expression in salivary adenoid
            cystic carcinoma.
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Liao,J., Lai,H., Liu,C., Zhang,X., Ou,Q., Li,Q., Li,Y., Wang,Z.,
            Liu,C., Wu,X., Wang,H., Yu,H., Sun,S., Zhao,X., Hu,Z., Zhang,Y.,
            Lin,Y., Yu,B., Huang,S. and Wang,J.
  TITLE     Plasma extracellular vesicle transcriptomics identifies CD160 for
            predicting immunochemotherapy efficacy in lung cancer
  JOURNAL   Cancer Sci 114 (7), 2774-2786 (2023)
   PUBMED   37014183
  REMARK    GeneRIF: Plasma extracellular vesicle transcriptomics identifies
            CD160 for predicting immunochemotherapy efficacy in lung cancer.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Yang,B., Zhai,F., An,H., Cao,Z., Liu,Y., Wang,R. and Cheng,X.
  TITLE     [Expression of CD160 in natural killer (NK) cells from patients
            with active tuberculosis and its relationship with cell functions]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 38 (10), 918-924 (2022)
   PUBMED   36163624
  REMARK    GeneRIF: [Expression of CD160 in natural killer (NK) cells from
            patients with active tuberculosis and its relationship with cell
            functions].
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Sun,Z., Li,Y., Zhang,Z., Fu,Y., Han,X., Hu,Q., Ding,H., Shang,H.
            and Jiang,Y.
  TITLE     CD160 Promotes NK Cell Functions by Upregulating Glucose Metabolism
            and Negatively Correlates With HIV Disease Progression
  JOURNAL   Front Immunol 13, 854432 (2022)
   PUBMED   36110864
  REMARK    GeneRIF: CD160 Promotes NK Cell Functions by Upregulating Glucose
            Metabolism and Negatively Correlates With HIV Disease Progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Le Bouteiller,P., Barakonyi,A., Giustiniani,J., Lenfant,F.,
            Marie-Cardine,A., Aguerre-Girr,M., Rabot,M., Hilgert,I.,
            Mami-Chouaib,F., Tabiasco,J., Boumsell,L. and Bensussan,A.
  TITLE     Engagement of CD160 receptor by HLA-C is a triggering mechanism
            used by circulating natural killer (NK) cells to mediate
            cytotoxicity
  JOURNAL   Proc Natl Acad Sci U S A 99 (26), 16963-16968 (2002)
   PUBMED   12486241
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Nikolova,M., Marie-Cardine,A., Boumsell,L. and Bensussan,A.
  TITLE     BY55/CD160 acts as a co-receptor in TCR signal transduction of a
            human circulating cytotoxic effector T lymphocyte subset lacking
            CD28 expression
  JOURNAL   Int Immunol 14 (5), 445-451 (2002)
   PUBMED   11978774
  REMARK    GeneRIF: BY55 functions as a co-receptor in TCR signal transduction
            of a human cytotoxic effector T lymphocyte subset lacking CD28
            expression
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Agrawal,S., Marquet,J., Freeman,G.J., Tawab,A., Bouteiller,P.L.,
            Roth,P., Bolton,W., Ogg,G., Boumsell,L. and Bensussan,A.
  TITLE     Cutting edge: MHC class I triggering by a novel cell surface ligand
            costimulates proliferation of activated human T cells
  JOURNAL   J Immunol 162 (3), 1223-1226 (1999)
   PUBMED   9973372
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Anumanthan,A., Bensussan,A., Boumsell,L., Christ,A.D.,
            Blumberg,R.S., Voss,S.D., Patel,A.T., Robertson,M.J., Nadler,L.M.
            and Freeman,G.J.
  TITLE     Cloning of BY55, a novel Ig superfamily member expressed on NK
            cells, CTL, and intestinal intraepithelial lymphocytes
  JOURNAL   J Immunol 161 (6), 2780-2790 (1998)
   PUBMED   9743336
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Bensussan,A., Gluckman,E., el Marsafy,S., Schiavon,V., Mansur,I.G.,
            Dausset,J., Boumsell,L. and Carosella,E.
  TITLE     BY55 monoclonal antibody delineates within human cord blood and
            bone marrow lymphocytes distinct cell subsets mediating cytotoxic
            activity
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 9136-9140 (1994)
   PUBMED   8090781
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD638675.1, BC014465.1, AC242845.1 and AA463248.1.
            
            Summary: CD160 is an 27 kDa glycoprotein which was initially
            identified with the monoclonal antibody BY55. Its expression is
            tightly associated with peripheral blood NK cells and CD8 T
            lymphocytes with cytolytic effector activity. The cDNA sequence of
            CD160 predicts a cysteine-rich,
            glycosylphosphatidylinositol-anchored protein of 181 amino acids
            with a single Ig-like domain weakly homologous to KIR2DL4 molecule.
            CD160 is expressed at the cell surface as a tightly
            disulfide-linked multimer. RNA blot analysis revealed CD160 mRNAs
            of 1.5 and 1.6 kb whose expression was highly restricted to
            circulating NK and T cells, spleen and small intestine. Within NK
            cells CD160 is expressed by CD56dimCD16+ cells whereas among
            circulating T cells its expression is mainly restricted to TCRgd
            bearing cells and to TCRab+CD8brightCD95+CD56+CD28-CD27-cells. In
            tissues, CD160 is expressed on all intestinal intraepithelial
            lymphocytes. CD160 shows a broad specificity for binding to both
            classical and nonclassical MHC class I molecules. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014465.1, AF060981.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369288.7/ ENSP00000358294.1
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..181
                     /product="CD160 antigen precursor"
                     /note="natural killer cell receptor, immunoglobulin
                     superfamily member; CD160 antigen; natural killer cell
                     receptor BY55; CD160-delta Ig"
                     /calculated_mol_wt=17371
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95971.1)"
                     /calculated_mol_wt=2457
     mat_peptide     25..159
                     /product="CD160 antigen. /id=PRO_0000014543"
                     /note="propagated from UniProtKB/Swiss-Prot (O95971.1)"
                     /calculated_mol_wt=14956
     Region          26..144
                     /region_name="IgC2_CD160"
                     /note="Immunoglobulin Constant-2 domain of Cluster of
                     Differentiation 160 (CD160); cd21392"
                     /db_xref="CDD:409621"
     Region          26..37
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409621"
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95971.1)"
     Region          39..48
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409621"
     Region          56..63
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409621"
     Region          74..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409621"
     Region          92..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409621"
     Region          108..116
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409621"
     Region          120..131
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409621"
     Region          137..142
                     /region_name="Ig strand H"
                     /note="Ig strand H [structural motif]"
                     /db_xref="CDD:409621"
     Site            137
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95971.1)"
     CDS             1..181
                     /gene="CD160"
                     /gene_synonym="BY55; NK1; NK28"
                     /coded_by="NM_007053.4:240..785"
                     /db_xref="CCDS:CCDS72861.1"
                     /db_xref="GeneID:11126"
                     /db_xref="HGNC:HGNC:17013"
                     /db_xref="MIM:604463"
ORIGIN      
        1 mllepgrgcc alaillaivd iqsggcinit ssasqegtrl nlictvwhkk eeaegfvvfl
       61 ckdrsgdcsp etslkqlrlk rdpgidgvge issqlmftis qvtplhsgty qccarsqksg
      121 irlqghffsi lftetgnytv tglkqrqhle fshnegtlss gflqekvwvm lvtslvalqa
      181 l
//
LOCUS       NP_001138880             471 aa            linear   PRI 20-NOV-2025
DEFINITION  non-POU domain-containing octamer-binding protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_001138880
VERSION     NP_001138880.1
DBSOURCE    REFSEQ: accession NM_001145408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 471)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 471)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 471)
  AUTHORS   Trifault,B., Mamontova,V., Cossa,G., Ganskih,S., Wei,Y.,
            Hofstetter,J., Bhandare,P., Baluapuri,A., Nieto,B., Solvie,D.,
            Ade,C.P., Gallant,P., Wolf,E., Larsen,D.H., Munschauer,M. and
            Burger,K.
  TITLE     Nucleolar detention of NONO shields DNA double-strand breaks from
            aberrant transcripts
  JOURNAL   Nucleic Acids Res 52 (6), 3050-3068 (2024)
   PUBMED   38224452
  REMARK    GeneRIF: Nucleolar detention of NONO shields DNA double-strand
            breaks from aberrant transcripts.
REFERENCE   4  (residues 1 to 471)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   5  (residues 1 to 471)
  AUTHORS   Clark,J., Lu,Y.J., Sidhar,S.K., Parker,C., Gill,S., Smedley,D.,
            Hamoudi,R., Linehan,W.M., Shipley,J. and Cooper,C.S.
  TITLE     Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
            gene in papillary renal cell carcinoma
  JOURNAL   Oncogene 15 (18), 2233-2239 (1997)
   PUBMED   9393982
REFERENCE   6  (residues 1 to 471)
  AUTHORS   Peters,U., Haberhausen,G., Kostrzewa,M., Nolte,D. and Muller,U.
  TITLE     AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as
            candidate genes of X-linked dystonia parkinsonism
  JOURNAL   Hum Genet 100 (5-6), 569-572 (1997)
   PUBMED   9341872
REFERENCE   7  (residues 1 to 471)
  AUTHORS   Traish,A.M., Huang,Y.H., Ashba,J., Pronovost,M., Pavao,M.,
            McAneny,D.B. and Moreland,R.B.
  TITLE     Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen
            receptor-negative human breast cancer
  JOURNAL   Diagn Mol Pathol 6 (4), 209-221 (1997)
   PUBMED   9360842
REFERENCE   8  (residues 1 to 471)
  AUTHORS   Hallier,M., Tavitian,A. and Moreau-Gachelin,F.
  TITLE     The transcription factor Spi-1/PU.1 binds RNA and interferes with
            the RNA-binding protein p54nrb
  JOURNAL   J Biol Chem 271 (19), 11177-11181 (1996)
   PUBMED   8626664
REFERENCE   9  (residues 1 to 471)
  AUTHORS   Dong,B., Horowitz,D.S., Kobayashi,R. and Krainer,A.R.
  TITLE     Purification and cDNA cloning of HeLa cell p54nrb, a nuclear
            protein with two RNA recognition motifs and extensive homology to
            human splicing factor PSF and Drosophila NONA/BJ6
  JOURNAL   Nucleic Acids Res 21 (17), 4085-4092 (1993)
   PUBMED   8371983
REFERENCE   10 (residues 1 to 471)
  AUTHORS   Zhang,W.W., Zhang,L.X., Busch,R.K., Farres,J. and Busch,H.
  TITLE     Purification and characterization of a DNA-binding heterodimer of
            52 and 100 kDa from HeLa cells
  JOURNAL   Biochem J 290 (Pt 1) (Pt 1), 267-272 (1993)
   PUBMED   8439294
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA116840.1, BC003129.1 and
            BC002364.1.
            
            Summary: This gene encodes an RNA-binding protein which plays
            various roles in the nucleus, including transcriptional regulation
            and RNA splicing. A rearrangement between this gene and the
            transcription factor E3 gene has been observed in papillary renal
            cell carcinoma. Alternatively spliced transcript variants have been
            described. Pseudogenes exist on Chromosomes 2 and 16. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.229226.1,
                                           SRR3476690.17957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..471
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..471
                     /product="non-POU domain-containing octamer-binding
                     protein isoform 1"
                     /note="non-POU domain-containing octamer (ATGCAAAT)
                     binding protein; 54 kDa nuclear RNA- and DNA-binding
                     protein; p54(nrb); 55 kDa nuclear protein; DNA-binding
                     p52/p100 complex, 52 kDa subunit; protein phosphatase 1,
                     regulatory subunit 114"
                     /calculated_mol_wt=54101
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            11
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          54..373
                     /region_name="DBHS"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Region          73..143
                     /region_name="RRM1_p54nrb"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     54 kDa nuclear RNA- and DNA-binding protein (p54nrb);
                     cd12588"
                     /db_xref="CDD:410001"
     Site            order(119..120,123..124,126..128)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410001"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          149..228
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Site            198
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          219..311
                     /region_name="NOPS_p54nrb_PSF_PSPC1"
                     /note="NOPS domain, including C-terminal coiled-coil
                     region, in p54nrb/PSF/PSPC1 family proteins; cd12946"
                     /db_xref="CDD:240581"
     Site            order(219..221,223,263..264,266..268,270..272,274..275,
                     277..278,281..282,285..286,288..289,292..293,296..297,
                     299..300,303..304,307)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:240581"
     Site            262
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            295
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            371
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99K48; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            377..378
                     /site_type="other"
                     /note="Breakpoint for translocation to form NONO-TFE3;
                     propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Region          443..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15233.4)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     Site            456
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15233.4)"
     CDS             1..471
                     /gene="NONO"
                     /gene_synonym="MRXS34; NMT55; NRB54; P54; P54NRB;
                     PPP1R114"
                     /coded_by="NM_001145408.2:268..1683"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14410.1"
                     /db_xref="GeneID:4841"
                     /db_xref="HGNC:HGNC:7871"
                     /db_xref="MIM:300084"
ORIGIN      
        1 mqsnktfnle kqnhtprkhh qhhhqqqhhq qqqqqppppp ipangqqass qnegltidlk
       61 nfrkpgektf tqrsrlfvgn lppditeeem rklfekygka gevfihkdkg fgfirletrt
      121 laeiakveld nmplrgkqlr vrfachsasl tvrnlpqyvs nelleeafsv fgqveravvi
      181 vddrgrpsgk givefsgkpa arkaldrcse gsfllttfpr pvtvepmdql ddeeglpekl
      241 viknqqfhke reqpprfaqp gsfeyeyamr wkaliemekq qqdqvdrnik eareklemem
      301 eaarhehqvm lmrqdlmrrq eelrrmeelh nqevqkrkql elrqeeerrr reeemrrqqe
      361 emmrrqqegf kgtfpdareq eirmgqmamg gamginnrga mppapvpagt pappgpatmm
      421 pdgtlgltpp tterfgqaat megigaiggt ppafnraapg aefapnkrrr y
//
LOCUS       NP_071902                731 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase COP1 isoform a [Homo sapiens].
ACCESSION   NP_071902
VERSION     NP_071902.2
DBSOURCE    REFSEQ: accession NM_022457.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Etemad,A., Tanaka,Y., Wang,S., Slae,M., Sultan,M., Elpeleg,O. and
            Hirokawa,N.
  TITLE     Mutations in the kinesin KIF12 promote MASH in humans and mice by
            disrupting lipogenic enzyme turnover
  JOURNAL   EMBO J 44 (6), 1608-1640 (2025)
   PUBMED   39920308
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Liu,P. and Xie,N.
  TITLE     RFWD2 increases proliferation and CDDP resistance of osteosarcoma
            cells
  JOURNAL   Gene 933, 148973 (2025)
   PUBMED   39349111
  REMARK    GeneRIF: RFWD2 increases proliferation and CDDP resistance of
            osteosarcoma cells.
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Li,X., Shao,L.Z., Li,Z.H., Wang,Y.H., Cai,Q.Y., Wang,S., Chen,H.,
            Sheng,J., Luo,X., Chen,X.M., Wang,Y.X., Ding,Y.B. and Liu,T.H.
  TITLE     STK40 inhibits trophoblast fusion by mediating COP1 ubiquitination
            to degrade P57Kip2
  JOURNAL   J Transl Med 22 (1), 852 (2024)
   PUBMED   39304928
  REMARK    GeneRIF: STK40 inhibits trophoblast fusion by mediating COP1
            ubiquitination to degrade P57[Kip2].
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Zhao,B., Wu,J., Cha,X., Mao,G., Shi,H., Fei,S. and Miao,B.
  TITLE     Effect of COP1 in Promoting the Tumorigenesis of Gastric Cancer by
            Down-Regulation of CDH18 via PI3K/AKT Signal Pathway
  JOURNAL   Anal Cell Pathol (Amst) 2023, 5617875 (2023)
   PUBMED   37025097
  REMARK    GeneRIF: Effect of COP1 in Promoting the Tumorigenesis of Gastric
            Cancer by Down-Regulation of CDH18 via PI3K/AKT Signal Pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Wertz,I.E., O'Rourke,K.M., Zhang,Z., Dornan,D., Arnott,D.,
            Deshaies,R.J. and Dixit,V.M.
  TITLE     Human De-etiolated-1 regulates c-Jun by assembling a CUL4A
            ubiquitin ligase
  JOURNAL   Science 303 (5662), 1371-1374 (2004)
   PUBMED   14739464
  REMARK    GeneRIF: DET1 promotes ubiquitination and degradation of c-Jun by
            assembling a multisubunit ubiquitin ligase containing DNA Damage
            Binding Protein-1 (DDB1), cullin 4A (CUL4A), Regulator of Cullins-1
            (ROC1), and constitutively photomorphogenic-1
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Bianchi,E., Denti,S., Catena,R., Rossetti,G., Polo,S.,
            Gasparian,S., Putignano,S., Rogge,L. and Pardi,R.
  TITLE     Characterization of human constitutive photomorphogenesis protein
            1, a RING finger ubiquitin ligase that interacts with Jun
            transcription factors and modulates their transcriptional activity
  JOURNAL   J Biol Chem 278 (22), 19682-19690 (2003)
   PUBMED   12615916
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Yi,C., Wang,H., Wei,N. and Deng,X.W.
  TITLE     An initial biochemical and cell biological characterization of the
            mammalian homologue of a central plant developmental switch, COP1
  JOURNAL   BMC Cell Biol 3, 30 (2002)
   PUBMED   12466024
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Hoecker,U. and Quail,P.H.
  TITLE     The phytochrome A-specific signaling intermediate SPA1 interacts
            directly with COP1, a constitutive repressor of light signaling in
            Arabidopsis
  JOURNAL   J Biol Chem 276 (41), 38173-38178 (2001)
   PUBMED   11461903
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Wang,H., Kang,D., Deng,X.W. and Wei,N.
  TITLE     Evidence for functional conservation of a mammalian homologue of
            the light-responsive plant protein COP1
  JOURNAL   Curr Biol 9 (13), 711-714 (1999)
   PUBMED   10395541
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL359265.8, BG717002.1 and BC094728.1.
            
            On Jun 9, 2002 this sequence version replaced NP_071902.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094728.1, AF527539.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367669.8/ ENSP00000356641.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.1-q25.2"
     Protein         1..731
                     /product="E3 ubiquitin-protein ligase COP1 isoform a"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase RFWD2; putative
                     ubiquitin ligase COP1; RING finger protein 200;
                     constitutive photomorphogenesis protein 1 homolog;
                     constitutive photomorphogenic protein 1; ring finger and
                     WD repeat domain 2, E3 ubiquitin protein ligase; RING-type
                     E3 ubiquitin transferase RFWD2; E3 ubiquitin-protein
                     ligase COP1"
                     /calculated_mol_wt=80344
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          109..113
                     /region_name="Nuclear localization signal 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          132..178
                     /region_name="RING-HC_COP1"
                     /note="RING finger, HC subclass, found in constitutive
                     photomorphogenesis protein 1 (COP1) and similar proteins;
                     cd16504"
                     /db_xref="CDD:438167"
     Region          195..206
                     /region_name="Nuclear localization signal 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          235..245
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          <240..731
                     /region_name="PLN00181"
                     /note="protein SPA1-RELATED; Provisional"
                     /db_xref="CDD:177776"
     Region          305..325
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          419..458
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          468..508
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Site            472
                     /site_type="other"
                     /note="Interaction with TRIB1.
                     /evidence=ECO:0000269|PubMed:27041596; propagated from
                     UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          473..510
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            491
                     /site_type="other"
                     /note="Interaction with TRIB1.
                     /evidence=ECO:0000269|PubMed:27041596; propagated from
                     UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          511..551
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          517..553
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          553..593
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          558..596
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          597..635
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          602..641
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          638..677
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          643..645
                     /region_name="Interaction with TRIB1.
                     /evidence=ECO:0000269|PubMed:27041596"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     Region          645..667
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          691..729
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NHY2.1)"
     CDS             1..731
                     /gene="COP1"
                     /gene_synonym="CFAP78; FAP78; RFWD2; RNF200"
                     /coded_by="NM_022457.7:309..2504"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30944.1"
                     /db_xref="GeneID:64326"
                     /db_xref="HGNC:HGNC:17440"
                     /db_xref="MIM:608067"
ORIGIN      
        1 msgsrqagsg sagtspgssa assvtsasss lssspsppsv avsaaalvsg gvaqaagsgg
       61 lggpvrpvlv apavsgsggg avstglsrhs caarpsagvg gsssslgsgs rkrpllaplc
      121 nglinsyedk sndfvcpicf dmieeaymtk cghsfcykci hqslednnrc pkcnyvvdni
      181 dhlypnflvn elilkqkqrf eekrfkldhs vsstnghrwq ifqdwlgtdq dnldlanvnl
      241 mlellvqkkk qleaeshaaq lqilmeflkv arrnkreqle qiqkelsvle edikrveems
      301 glyspvseds tvpqfeapsp shssiidste ysqppgfsgs sqtkkqpwyn stlasrrkrl
      361 tahfedleqc yfstrmsris ddsrtasqld efqeclskft rynsvrplat lsyasdlyng
      421 ssivssiefd rdcdyfaiag vtkkikvyey dtviqdavdi hypenemtcn skisciswss
      481 yhknllassd yegtvilwdg ftgqrskvyq ehekrcwsvd fnlmdpklla sgsddakvkl
      541 wstnldnsva sieakanvcc vkfspssryh lafgcadhcv hyydlrntkq pimvfkghrk
      601 avsyakfvsg eeivsastds qlklwnvgkp yclrsfkghi neknfvglas ngdyiacgse
      661 nnslylyykg lsktlltfkf dtvksvldkd rkeddtnefv savcwralpd gesnvliaan
      721 sqgtikvlel v
//
LOCUS       NP_001357591             776 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-1 [Homo sapiens].
ACCESSION   NP_001357591 XP_005250117
VERSION     NP_001357591.1
DBSOURCE    REFSEQ: accession NM_001370662.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Yang,T., Hu,J., Zhang,L., Liu,L., Pan,X., Zhou,Y., Wu,Y., Shi,X.,
            Obiegbusi,C.N. and Dong,X.
  TITLE     CircCUL1 inhibits trophoblast cell migration and invasion and
            promotes cell autophagy by sponging hsa-miR-30e-3p in fetal growth
            restriction via the ANXA1/PI3K/AKT axis
  JOURNAL   J Biochem Mol Toxicol 38 (7), e23759 (2024)
   PUBMED   39003567
  REMARK    GeneRIF: CircCUL1 inhibits trophoblast cell migration and invasion
            and promotes cell autophagy by sponging hsa-miR-30e-3p in fetal
            growth restriction via the ANXA1/PI3K/AKT axis.
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,Y., Huang,X., Wang,Y., Lei,Y., Yu,J., Yu,S., Gao,Y., Yang,J.,
            Zhao,F., Yu,H., Zeng,J., Chu,Y., Yang,M., Li,G., Xie,X. and
            Zhang,J.
  TITLE     NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer by
            Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins
  JOURNAL   Adv Sci (Weinh) 11 (9), e2305907 (2024)
   PUBMED   38126621
  REMARK    GeneRIF: NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer
            by Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Khalil,M.I., Yang,C., Vu,L., Chadha,S., Nabors,H., James,C.D.,
            Morgan,I.M. and Pyeon,D.
  TITLE     The membrane-associated ubiquitin ligase MARCHF8 stabilizes the
            human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in
            head and neck cancer
  JOURNAL   J Virol 98 (2), e0172623 (2024)
   PUBMED   38226814
  REMARK    GeneRIF: The membrane-associated ubiquitin ligase MARCHF8
            stabilizes the human papillomavirus oncoprotein E7 by degrading
            CUL1 and UBE2L3 in head and neck cancer.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Winston,J.T., Strack,P., Beer-Romero,P., Chu,C.Y., Elledge,S.J. and
            Harper,J.W.
  TITLE     The SCFbeta-TRCP-ubiquitin ligase complex associates specifically
            with phosphorylated destruction motifs in IkappaBalpha and
            beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
  JOURNAL   Genes Dev 13 (3), 270-283 (1999)
   PUBMED   9990852
  REMARK    Erratum:[Genes Dev 1999 Apr 15;13(8):1050]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Ng,R.W., Arooz,T., Yam,C.H., Chan,I.W., Lau,A.W. and Poon,R.Y.
  TITLE     Characterization of the cullin and F-box protein partner Skp1
  JOURNAL   FEBS Lett 438 (3), 183-189 (1998)
   PUBMED   9827542
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005229.2 and AC006323.3.
            
            On May 21, 2019 this sequence version replaced XP_005250117.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.7184.1,
                                           SRR1803613.75652.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..776
                     /product="cullin-1"
                     /note="CUL-1"
                     /calculated_mol_wt=89548
     Region          21..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Site            63
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13616.2)"
     Region          706..768
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..776
                     /gene="CUL1"
                     /coded_by="NM_001370662.1:281..2611"
                     /db_xref="CCDS:CCDS34772.1"
                     /db_xref="GeneID:8454"
                     /db_xref="HGNC:HGNC:2551"
                     /db_xref="MIM:603134"
ORIGIN      
        1 msstrsqnph glkqigldqi wddlragiqq vytrqsmaks rymelythvy nyctsvhqsn
       61 qargagvpps kskkgqtpgg aqfvglelyk rlkeflknyl tnllkdgedl mdesvlkfyt
      121 qqwedyrfss kvlngicayl nrhwvrrecd egrkgiyeiy slalvtwrdc lfrplnkqvt
      181 navlklieke rngetintrl isgvvqsyve lglneddafa kgptltvyke sfesqfladt
      241 erfytreste flqqnpvtey mkkaearlle eqrrvqvylh estqdelark ceqvliekhl
      301 eifhtefqnl ldadknedlg rmynlvsriq dglgelkkll ethihnqgla aiekcgeaal
      361 ndpkmyvqtv ldvhkkynal vmsafnndag fvaaldkacg rfinnnavtk maqssskspe
      421 llarycdsll kkssknpeea eledtlnqvm vvfkyiedkd vfqkfyakml akrlvhqnsa
      481 sddaeasmis klkqacgfey tsklqrmfqd igvskdlneq fkkhltnsep ldldfsiqvl
      541 ssgswpfqqs ctfalpsele rsyqrftafy asrhsgrklt wlyqlskgel vtncfknryt
      601 lqastfqmai llqynteday tvqqltdstq ikmdilaqvl qillkskllv ledenanvde
      661 velkpdtlik lylgyknkkl rvninvpmkt eqkqeqetth knieedrkll iqaaivrimk
      721 mrkvlkhqql lgevltqlss rfkprvpvik kcidilieke ylervdgekd tysyla
//
LOCUS       NP_001305262             414 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 56 isoform 6 [Homo sapiens].
ACCESSION   NP_001305262 XP_005250665
VERSION     NP_001305262.1
DBSOURCE    REFSEQ: accession NM_001318333.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 414)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 414)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 414)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 414)
  AUTHORS   David,O., Eskin-Schwartz,M., Ling,G., Dolgin,V., Kristal,E.,
            Benkowitz,E., Osyntsov,L., Gradstein,L., Birk,O.S., Loewenthal,N.
            and Yerushalmi,B.
  TITLE     Pituitary stalk interruption syndrome broadens the clinical
            spectrum of the TTC26 ciliopathy
  JOURNAL   Clin Genet 98 (3), 303-307 (2020)
   PUBMED   32617964
  REMARK    GeneRIF: Pituitary stalk interruption syndrome broadens the
            clinical spectrum of the TTC26 ciliopathy.
REFERENCE   5  (residues 1 to 414)
  AUTHORS   Shaheen,R., Alsahli,S., Ewida,N., Alzahrani,F., Shamseldin,H.E.,
            Patel,N., Al Qahtani,A., Alhebbi,H., Alhashem,A., Al-Sheddi,T.,
            Alomar,R., Alobeid,E., Abouelhoda,M., Monies,D., Al-Hussaini,A.,
            Alzouman,M.A., Shagrani,M., Faqeih,E. and Alkuraya,F.S.
  TITLE     Biallelic Mutations in Tetratricopeptide Repeat Domain 26
            (Intraflagellar Transport 56) Cause Severe Biliary Ciliopathy in
            Humans
  JOURNAL   Hepatology 71 (6), 2067-2079 (2020)
   PUBMED   31595528
  REMARK    GeneRIF: Biallelic Mutations in Tetratricopeptide Repeat Domain 26
            (Intraflagellar Transport 56) Cause Severe Biliary Ciliopathy in
            Humans.
REFERENCE   6  (residues 1 to 414)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   7  (residues 1 to 414)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 414)
  AUTHORS   Ishikawa,H., Ide,T., Yagi,T., Jiang,X., Hirono,M., Sasaki,H.,
            Yanagisawa,H., Wemmer,K.A., Stainier,D.Y., Qin,H., Kamiya,R. and
            Marshall,W.F.
  TITLE     TTC26/DYF13 is an intraflagellar transport protein required for
            transport of motility-related proteins into flagella
  JOURNAL   Elife 3, e01566 (2014)
   PUBMED   24596149
  REMARK    GeneRIF: TTC26 is an intraflagellar transport protein required for
            transport of motility-related proteins into flagella.
            Erratum:[Elife. 2014 Apr 01;3:e02897. doi: 10.7554/eLife.02897.
            PMID: 24692455]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 414)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   10 (residues 1 to 414)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP315162.1, BC034466.1, BC013912.1, AC009220.10 and CA450032.1.
            
            On Jan 1, 2016 this sequence version replaced XP_005250665.1.
            
            Transcript Variant: This variant (6) uses an alternate splice site
            in its 5' UTR and a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (6) has a shorter N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.381285.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..414
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q34"
     Protein         1..414
                     /product="intraflagellar transport protein 56 isoform 6"
                     /note="tetratricopeptide repeat protein 26; TPR repeat
                     protein 26; intraflagellar transport protein 56;
                     tetratricopeptide repeat domain 26"
                     /calculated_mol_wt=47764
     Region          <14..84
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Site            order(15..16,19..20,22,46,49..50,53..54,56..57,80,83..84,
                     87..88,91)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          15..39
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <18..>206
                     /region_name="PEP_TPR_lipo"
                     /note="putative PEP-CTERM system TPR-repeat lipoprotein;
                     TIGR02917"
                     /db_xref="CDD:274350"
     Region          44..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..414
                     /gene="IFT56"
                     /gene_synonym="BRENS; dyf-13; DYF13; TTC26"
                     /coded_by="NM_001318333.2:662..1906"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:79989"
                     /db_xref="HGNC:HGNC:21882"
                     /db_xref="MIM:617453"
ORIGIN      
        1 msfhqnlqdv tedqlslasi hymrshyqea idiykrilld nreylalnvy valcyykldy
       61 ydvsqevlav ylqqipdsti alnlkacnhf rlyngraaea elkslmdnas ssfefakeli
      121 rhnlvvfrgg egalqvlppl vdvipearln lviyylrqdd vqeaynlikd lepttpqeyi
      181 lkgvvnaalg qemgsrdhmk iaqqffqlvg gsasecdtip grqcmascff llkqfddvli
      241 ylnsfksyfy nddifnfnya qakaatgnts egeeaflliq sekmkndyiy lswlarcyim
      301 nkkprlawel ylkmetsges fsllqliand cykmgqfyys akafdvlerl dpnpeywegk
      361 rgacvgifqm iiagrepket lrevlhllrs tgntqveymi rimkkwaken rvsi
//
LOCUS       NP_001136120             198 aa            linear   PRI 20-NOV-2025
DEFINITION  small COPII coat GTPase SAR1A [Homo sapiens].
ACCESSION   NP_001136120
VERSION     NP_001136120.1
DBSOURCE    REFSEQ: accession NM_001142648.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Tang,V.T., Xiang,J., Chen,Z., McCormick,J., Abbineni,P.S.,
            Chen,X.W., Hoenerhoff,M., Emmer,B.T., Khoriaty,R., Lin,J.D. and
            Ginsburg,D.
  TITLE     Functional overlap between the mammalian Sar1a and Sar1b paralogs
            in vivo
  JOURNAL   Proc Natl Acad Sci U S A 121 (19), e2322164121 (2024)
   PUBMED   38687799
  REMARK    GeneRIF: Functional overlap between the mammalian Sar1a and Sar1b
            paralogs in vivo.
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Zhan,F., Deng,Q., Chen,Z., Xie,C., Xiang,S., Qiu,S., Tian,L.,
            Wu,C., Ou,Y., Chen,J. and Xu,L.
  TITLE     SAR1A regulates the RhoA/YAP and autophagy signaling pathways to
            influence osteosarcoma invasion and metastasis
  JOURNAL   Cancer Sci 113 (12), 4104-4119 (2022)
   PUBMED   36047971
  REMARK    GeneRIF: SAR1A regulates the RhoA/YAP and autophagy signaling
            pathways to influence osteosarcoma invasion and metastasis.
REFERENCE   4  (residues 1 to 198)
  AUTHORS   Chen,J., Ou,Y., Luo,R., Wang,J., Wang,D., Guan,J., Li,Y., Xia,P.,
            Chen,P.R. and Liu,Y.
  TITLE     SAR1B senses leucine levels to regulate mTORC1 signalling
  JOURNAL   Nature 596 (7871), 281-284 (2021)
   PUBMED   34290409
REFERENCE   5  (residues 1 to 198)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 198)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 198)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 198)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 198)
  AUTHORS   Jones,B., Jones,E.L., Bonney,S.A., Patel,H.N., Mensenkamp,A.R.,
            Eichenbaum-Voline,S., Rudling,M., Myrdal,U., Annesi,G., Naik,S.,
            Meadows,N., Quattrone,A., Islam,S.A., Naoumova,R.P., Angelin,B.,
            Infante,R., Levy,E., Roy,C.C., Freemont,P.S., Scott,J. and
            Shoulders,C.C.
  TITLE     Mutations in a Sar1 GTPase of COPII vesicles are associated with
            lipid absorption disorders
  JOURNAL   Nat Genet 34 (1), 29-31 (2003)
   PUBMED   12692552
REFERENCE   10 (residues 1 to 198)
  AUTHORS   South,S.T., Sacksteder,K.A., Li,X., Liu,Y. and Gould,S.J.
  TITLE     Inhibitors of COPI and COPII do not block PEX3-mediated peroxisome
            synthesis
  JOURNAL   J Cell Biol 149 (7), 1345-1360 (2000)
   PUBMED   10871277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB216796.1, BG327663.1, BC003658.2, DR763562.1, AL731540.4,
            EB388518.1 and AW128933.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.108259.1,
                                           SRR1803614.196227.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..198
                     /product="small COPII coat GTPase SAR1A"
                     /EC_number="3.6.5.2"
                     /note="GTP-binding protein SAR1a; COPII-associated small
                     GTPase; SAR1a gene homolog 1; SAR1 gene homolog A; SAR1
                     homolog A"
                     /calculated_mol_wt=22236
     Region          3..197
                     /region_name="Sar1"
                     /note="Sar1 is an essential component of COPII vesicle
                     coats; cd00879"
                     /db_xref="CDD:206645"
     Region          3..5
                     /region_name="STAR, SAR1-N-terminal activation
                     recruitment. Required for the activation by PREB and
                     subsequent recruitment to ER membrane.
                     /evidence=ECO:0000250|UniProtKB:Q9QVY3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR31.1)"
     Site            3..5
                     /site_type="active"
                     /note="STAR motif [active]"
                     /db_xref="CDD:206645"
     Region          15..19
                     /region_name="Mediates recruitment to ER membranes.
                     /evidence=ECO:0000250|UniProtKB:Q9QVY3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR31.1)"
     Site            32..39
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206645"
     Site            order(34..40,56,78,134..135,137,179..181)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206645"
     Site            order(34..35,39,43,50..62,84,89)
                     /site_type="other"
                     /note="GAP interaction site [polypeptide binding]"
                     /db_xref="CDD:206645"
     Site            44..59
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206645"
     Site            order(56..60,65,75,79,85,87..89)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206645"
     Site            56
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206645"
     Site            order(57..64,74,85,88..89)
                     /site_type="active"
                     /note="putative effector interaction site [active]"
                     /db_xref="CDD:206645"
     Site            60..74
                     /site_type="active"
                     /note="interswitch region [active]"
                     /db_xref="CDD:206645"
     Site            75..92
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206645"
     Site            75..78
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206645"
     Site            134..137
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206645"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NR31.1)"
     Site            179..181
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206645"
     CDS             1..198
                     /gene="SAR1A"
                     /gene_synonym="masra2; SAR1; Sara; SARA1"
                     /coded_by="NM_001142648.2:189..785"
                     /db_xref="CCDS:CCDS7298.1"
                     /db_xref="GeneID:56681"
                     /db_xref="HGNC:HGNC:10534"
                     /db_xref="MIM:607691"
ORIGIN      
        1 msfifewiyn gfssvlqflg lykksgklvf lgldnagktt llhmlkddrl gqhvptlhpt
       61 seeltiagmt fttfdlgghe qarrvwknyl paingivflv dcadhsrlve skvelnalmt
      121 detisnvpil ilgnkidrtd aiseeklrei fglygqttgk gnvtlkelna rpmevfmcsv
      181 lkrqgygegf rwlsqyid
//
LOCUS       NP_036418                288 aa            linear   PRI 20-NOV-2025
DEFINITION  mortality factor 4-like protein 2 [Homo sapiens].
ACCESSION   NP_036418
VERSION     NP_036418.1
DBSOURCE    REFSEQ: accession NM_012286.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Kooblall,K.G., Stokes,V.J., Shariq,O.A., English,K.A.,
            Stevenson,M., Broxholme,J., Wright,B., Lockstone,H.E., Buck,D.,
            Grozinsky-Glasberg,S., Yates,C.J., Thakker,R.V. and Lines,K.E.
  TITLE     miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2
  JOURNAL   Endocr Relat Cancer 29 (10), 557-568 (2022)
   PUBMED   35900839
  REMARK    GeneRIF: miR-3156-5p is downregulated in serum of MEN1 patients and
            regulates expression of MORF4L2.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Zheng,X., Sun,Z., Yu,L., Shi,D., Zhu,M., Yao,H. and Li,L.
  TITLE     Interactome Analysis of the Nucleocapsid Protein of SARS-CoV-2
            Virus
  JOURNAL   Pathogens 10 (9), 1155 (2021)
   PUBMED   34578187
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Cai,Y., Jin,J., Tomomori-Sato,C., Sato,S., Sorokina,I.,
            Parmely,T.J., Conaway,R.C. and Conaway,J.W.
  TITLE     Identification of new subunits of the multiprotein mammalian
            TRRAP/TIP60-containing histone acetyltransferase complex
  JOURNAL   J Biol Chem 278 (44), 42733-42736 (2003)
   PUBMED   12963728
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Yochum,G.S. and Ayer,D.E.
  TITLE     Role for the mortality factors MORF4, MRGX, and MRG15 in
            transcriptional repression via associations with Pf1, mSin3A, and
            Transducin-Like Enhancer of Split
  JOURNAL   Mol Cell Biol 22 (22), 7868-7876 (2002)
   PUBMED   12391155
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Sakai,K., Shirakawa,T., Li,Y., Kitagawa,Y. and Hirose,G.
  TITLE     Interaction of a paraneoplastic cerebellar degeneration-associated
            neuronal protein with the nuclear helix-loop-helix leucine zipper
            protein MRG X
  JOURNAL   Mol Cell Neurosci 19 (4), 477-484 (2002)
   PUBMED   11988016
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Bertram,M.J., Berube,N.G., Hang-Swanson,X., Ran,Q., Leung,J.K.,
            Bryce,S., Spurgers,K., Bick,R.J., Baldini,A., Ning,Y., Clark,L.J.,
            Parkinson,E.K., Barrett,J.C., Smith,J.R. and Pereira-Smith,O.M.
  TITLE     Identification of a gene that reverses the immortal phenotype of a
            subset of cells and is a member of a novel family of transcription
            factor-like genes
  JOURNAL   Mol Cell Biol 19 (2), 1479-1485 (1999)
   PUBMED   9891081
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA987770.1, AL049610.9 and BC093013.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189661.65532.1,
                                           SRR5189655.79087.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000441076.7/ ENSP00000391969.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..288
                     /product="mortality factor 4-like protein 2"
                     /note="MSL3-2 protein; protein MSL3-2; MORF-related gene X
                     protein; transcription factor-like protein MRGX"
                     /calculated_mol_wt=32177
     Region          1..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15014.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15014.1)"
     Region          102..276
                     /region_name="MRG"
                     /note="pfam05712"
                     /db_xref="CDD:461721"
     CDS             1..288
                     /gene="MORF4L2"
                     /gene_synonym="MORFL2; MRGX"
                     /coded_by="NM_012286.3:337..1203"
                     /db_xref="CCDS:CCDS14512.1"
                     /db_xref="GeneID:9643"
                     /db_xref="HGNC:HGNC:16849"
                     /db_xref="MIM:300409"
ORIGIN      
        1 mssrkqgsqp rgqqsaeeen fkkptrsnmq rskmrgassg kktagpqqkn lepalpgrwg
       61 grsaenppsg svrktrknkq ktpgngdggs tseapqpprk kraradptve seeafknrme
      121 vkvkipeelk pwlvedwdlv trqkqlfqlp akknvdaile eyanckksqg nvdnkeyavn
      181 evvagikeyf nvmlgtqlly kferpqyaei llahpdapms qvygaphllr lfvrigamla
      241 ytpldeksla lllgylhdfl kylaknsasl ftasdykvas aeyhrkal
//
LOCUS       NP_001317357             382 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase Chk1 isoform 4 [Homo sapiens].
ACCESSION   NP_001317357 XP_011540865
VERSION     NP_001317357.1
DBSOURCE    REFSEQ: accession NM_001330428.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Wang,J., Liu,Y., Wu,D., Tian,C., Gao,J., Yang,Q., Hong,X., Gu,F.,
            Zhang,K., Hu,Y., Xu,S., Liu,L. and Zeng,Y.
  TITLE     OTUB1 Targets CHK1 for Deubiquitination and Stabilization to
            Facilitate Lung Cancer Progression and Radioresistance
  JOURNAL   Int J Radiat Oncol Biol Phys 119 (4), 1222-1233 (2024)
   PUBMED   38266782
  REMARK    GeneRIF: OTUB1 Targets CHK1 for Deubiquitination and Stabilization
            to Facilitate Lung Cancer Progression and Radioresistance.
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Ando,S., Tanaka,K., Matsumoto,M., Oyama,Y., Tomabechi,Y.,
            Yamagata,A., Shirouzu,M., Nakagawa,R., Okimoto,N., Taiji,M.,
            Sato,K. and Ohama,T.
  TITLE     The luciferase-based in vivo protein-protein interaction assay
            revealed that CHK1 promotes PP2A and PME-1 interaction
  JOURNAL   J Biol Chem 300 (5), 107277 (2024)
   PUBMED   38588804
  REMARK    GeneRIF: The luciferase-based in vivo protein-protein interaction
            assay revealed that CHK1 promotes PP2A and PME-1 interaction.
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Egger,T., Morano,L., Blanchard,M.P., Basbous,J. and Constantinou,A.
  TITLE     Spatial organization and functions of Chk1 activation by TopBP1
            biomolecular condensates
  JOURNAL   Cell Rep 43 (4), 114064 (2024)
   PUBMED   38578830
  REMARK    GeneRIF: Spatial organization and functions of Chk1 activation by
            TopBP1 biomolecular condensates.
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Colaco,V., Goswami,N., Goel,V.K., Srivastava,S.K., Lalrohlua,P.,
            Senthil Kumar,N., Borah,P., Baruah,R. and Varma,A.K.
  TITLE     In silico and structure-based evaluation of deleterious mutations
            identified in human Chk1, Chk2, and Wee1 protein kinase
  JOURNAL   J Cell Biochem 125 (1), 89-99 (2024)
   PUBMED   38047473
  REMARK    GeneRIF: In silico and structure-based evaluation of deleterious
            mutations identified in human Chk1, Chk2, and Wee1 protein kinase.
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Giaccia,A.J. and Kastan,M.B.
  TITLE     The complexity of p53 modulation: emerging patterns from divergent
            signals
  JOURNAL   Genes Dev 12 (19), 2973-2983 (1998)
   PUBMED   9765199
  REMARK    Review article
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Flaggs,G., Plug,A.W., Dunks,K.M., Mundt,K.E., Ford,J.C.,
            Quiggle,M.R., Taylor,E.M., Westphal,C.H., Ashley,T., Hoekstra,M.F.
            and Carr,A.M.
  TITLE     Atm-dependent interactions of a mammalian chk1 homolog with meiotic
            chromosomes
  JOURNAL   Curr Biol 7 (12), 977-986 (1997)
   PUBMED   9382850
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Peng,C.Y., Graves,P.R., Thoma,R.S., Wu,Z., Shaw,A.S. and
            Piwnica-Worms,H.
  TITLE     Mitotic and G2 checkpoint control: regulation of 14-3-3 protein
            binding by phosphorylation of Cdc25C on serine-216
  JOURNAL   Science 277 (5331), 1501-1505 (1997)
   PUBMED   9278512
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Sanchez,Y., Wong,C., Thoma,R.S., Richman,R., Wu,Z.,
            Piwnica-Worms,H. and Elledge,S.J.
  TITLE     Conservation of the Chk1 checkpoint pathway in mammals: linkage of
            DNA damage to Cdk regulation through Cdc25
  JOURNAL   Science 277 (5331), 1497-1501 (1997)
   PUBMED   9278511
  REMARK    GeneRIF: Biochemical studies suggest the functional interactions of
            this protein with cell cycle regulators. Cdc25A, Cdc25B, and Cdc25C
            can be phosphoryalted by this protein.
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Ward,G.E. and Kirschner,M.W.
  TITLE     Identification of cell cycle-regulated phosphorylation sites on
            nuclear lamin C
  JOURNAL   Cell 61 (4), 561-577 (1990)
   PUBMED   2188730
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001132.4.
            
            On Aug 29, 2016 this sequence version replaced XP_011540865.1.
            
            Summary: The protein encoded by this gene belongs to the Ser/Thr
            protein kinase family. It is required for checkpoint mediated cell
            cycle arrest in response to DNA damage or the presence of
            unreplicated DNA. This protein acts to integrate signals from ATM
            and ATR, two cell cycle proteins involved in DNA damage responses,
            that also associate with chromatin in meiotic prophase I.
            Phosphorylation of CDC25A protein phosphatase by this protein is
            required for cells to delay cell cycle progression in response to
            double-strand DNA breaks. Several alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Oct
            2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.119311.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..382
                     /product="serine/threonine-protein kinase Chk1 isoform 4"
                     /EC_number="2.7.11.1"
                     /note="Checkpoint, S. pombe, homolog of, 1;
                     serine/threonine-protein kinase Chk1; CHK1 checkpoint
                     homolog; cell cycle checkpoint kinase; Chk1-S"
                     /calculated_mol_wt=43572
     Region          <4..171
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..382
                     /gene="CHEK1"
                     /gene_synonym="CHK1; OZEMA21"
                     /coded_by="NM_001330428.1:498..1646"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS81645.1"
                     /db_xref="GeneID:1111"
                     /db_xref="HGNC:HGNC:1925"
                     /db_xref="MIM:603078"
ORIGIN      
        1 mekpdigmpe pdaqrffhql magvvylhgi githrdikpe nlllderdnl kisdfglatv
       61 frynnrerll nkmcgtlpyv apellkrref haepvdvwsc givltamlag elpwdqpsds
      121 cqeysdwkek ktylnpwkki dsaplallhk ilvenpsari tipdikkdrw ynkplkkgak
      181 rprvtsggvs espsgfskhi qsnldfspvn sasseenvky sssqpeprtg lslwdtspsy
      241 idklvqgisf sqptcpdhml lnsqllgtpg ssqnpwqrlv krmtrfftkl dadksyqclk
      301 etceklgyqw kkscmnqvti sttdrrnnkl ifkvnllemd dkilvdfrls kgdglefkrh
      361 flkikgklid ivssqkiwlp at
//
LOCUS       NP_001036111             953 aa            linear   PRI 20-NOV-2025
DEFINITION  trafficking kinesin-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001036111
VERSION     NP_001036111.1
DBSOURCE    REFSEQ: accession NM_001042646.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Baltrusaitis,E.E., Ravitch,E.E., Fenton,A.R., Perez,T.A.,
            Holzbaur,E.L.F. and Dominguez,R.
  TITLE     Interaction between the mitochondrial adaptor MIRO and the motor
            adaptor TRAK
  JOURNAL   J Biol Chem 299 (12), 105441 (2023)
   PUBMED   37949220
  REMARK    GeneRIF: Interaction between the mitochondrial adaptor MIRO and the
            motor adaptor TRAK.
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Benhamida,J.K., Harmsen,H.J., Ma,D., William,C.M., Li,B.K.,
            Villafania,L., Sukhadia,P., Mullaney,K.A., Dewan,M.C., Vakiani,E.,
            Karajannis,M.A., Snuderl,M., Zagzag,D., Ladanyi,M., Rosenblum,M.K.
            and Bale,T.A.
  TITLE     Recurrent TRAK1::RAF1 Fusions in pediatric low-grade gliomas
  JOURNAL   Brain Pathol 33 (5), e13185 (2023)
   PUBMED   37399073
  REMARK    GeneRIF: Recurrent TRAK1::RAF1 Fusions in pediatric low-grade
            gliomas.
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Wu,H., Liu,Y., Li,H., Du,C., Li,K., Dong,S., Meng,Q. and Zhang,H.
  TITLE     TRAK1-Mediated Abnormality of Mitochondrial Fission Increases
            Seizure Susceptibility in Temporal Lobe Epilepsy
  JOURNAL   Mol Neurobiol 58 (3), 1237-1247 (2021)
   PUBMED   33119838
  REMARK    GeneRIF: TRAK1-Mediated Abnormality of Mitochondrial Fission
            Increases Seizure Susceptibility in Temporal Lobe Epilepsy.
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Ozyildirim,A.M., Wistow,G.J., Gao,J., Wang,J., Dickinson,D.P.,
            Frierson,H.F. Jr. and Laurie,G.W.
  TITLE     The lacrimal gland transcriptome is an unusually rich source of
            rare and poorly characterized gene transcripts
  JOURNAL   Invest Ophthalmol Vis Sci 46 (5), 1572-1580 (2005)
   PUBMED   15851553
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Brickley,K., Smith,M.J., Beck,M. and Stephenson,F.A.
  TITLE     GRIF-1 and OIP106, members of a novel gene family of coiled-coil
            domain proteins: association in vivo and in vitro with kinesin
  JOURNAL   J Biol Chem 280 (15), 14723-14732 (2005)
   PUBMED   15644324
  REMARK    GeneRIF: GRIF-1 and OIP106 have roles in protein and/or organelle
            transport in excitable cells in a manner analogous to glutamate
            receptor-interacting-protein 1
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Iyer,S.P. and Hart,G.W.
  TITLE     Roles of the tetratricopeptide repeat domain in O-GlcNAc
            transferase targeting and protein substrate specificity
  JOURNAL   J Biol Chem 278 (27), 24608-24616 (2003)
   PUBMED   12724313
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Iyer,S.P., Akimoto,Y. and Hart,G.W.
  TITLE     Identification and cloning of a novel family of coiled-coil domain
            proteins that interact with O-GlcNAc transferase
  JOURNAL   J Biol Chem 278 (7), 5399-5409 (2003)
   PUBMED   12435728
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB028965.1, AC018358.20 and H05058.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB028965.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327628.10/ ENSP00000328998.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.1"
     Protein         1..953
                     /product="trafficking kinesin-binding protein 1 isoform 1"
                     /note="OGT(O-Glc-NAc transferase)-interacting protein 106
                     KDa; 106 kDa O-GlcNAc transferase-interacting protein;
                     milton homolog 1; O-linked N-acetylglucosamine transferase
                     interacting protein 106; protein Milton; trafficking
                     protein, kinesin binding 1"
                     /calculated_mol_wt=105909
     Region          48..353
                     /region_name="HAP1_N"
                     /note="HAP1 N-terminal conserved region; pfam04849"
                     /db_xref="CDD:461455"
     Region          359..509
                     /region_name="Interaction with HGS.
                     /evidence=ECO:0000269|PubMed:18675823"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          414..583
                     /region_name="Milton"
                     /note="Kinesin associated protein; pfam12448"
                     /db_xref="CDD:463588"
     Site            447
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          472..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD31; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          658..672
                     /region_name="Interaction with OGT.
                     /evidence=ECO:0000269|PubMed:24995978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            680
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            719
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PD31; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Region          777..796
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            919
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     Site            935
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine.
                     /evidence=ECO:0000269|PubMed:24995978; propagated from
                     UniProtKB/Swiss-Prot (Q9UPV9.1)"
     CDS             1..953
                     /gene="TRAK1"
                     /gene_synonym="DEE68; EIEE68; MILT1; OIP106"
                     /coded_by="NM_001042646.3:114..2975"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43072.1"
                     /db_xref="GeneID:22906"
                     /db_xref="HGNC:HGNC:29947"
                     /db_xref="MIM:608112"
ORIGIN      
        1 malvfqfgqp vraqplpglc hgklirtnac dvcnstdlpe veiislleeq lphyklradt
       61 iygydhddwl htplispdan idltteqiee tlkyfllcae rvgqmtktyn didavtrlle
      121 ekerdlelaa rigqsllkkn ktlternell eeqvehiree vsqlrhelsm kdellqfyts
      181 aaeesepesv cstplkrnes sssvqnyfhl dslqkklkdl eeenvvlrse asqlktetit
      241 yeekeqqlvn dcvkelrdan vqiasiseel akktedaarq qeeithllsq ivdlqkkaka
      301 caveneelvq hlgaakdaqr qltaelrele dkyaecmeml heaqeelknl rnktmpntts
      361 rryhslglfp mdslaaeieg tmrkelqlee aespdithqk rvfetvrnin qvvkqrsltp
      421 spmnipgsnq ssamnsllss cvstprssfy gsdignvvld nktnsiilet eaadlgnder
      481 skkpgtpgtp gshdletalr rlslrrenyl serrffeeeq erklqelaek gelrsgsltp
      541 tesimslgth srfseftgfs gmsfssrsyl peklqivkpl egsatlhhwq qlaqphlggi
      601 ldprpgvvtk gfrtldvdld evyclndfee ddtgdhislp rlatstpvqh petsahhpgk
      661 cmsqtnstft fttcrilhps deltrvtpsl nsaptpacgs tshlkstpva tpctprrlsl
      721 aesftntres tttmstslgl vwllkergis aavydpqswd ragrgsllhs ytpkmavips
      781 tppnspmqtp tssppsfefk ctsppydnfl askpassilr evreknvrss esqtdvsvsn
      841 lnlvdkvrrf gvakvvnsgr ahvptlteeq gpllcgppgp apalvprglv peglplrcpt
      901 vtsaigglql nsgirrnrsf ptmvgssmqm kapvtltsgi lmgaklskqt slr
//
LOCUS       NP_001306876             406 aa            linear   PRI 20-NOV-2025
DEFINITION  5' exonuclease Apollo isoform b [Homo sapiens].
ACCESSION   NP_001306876
VERSION     NP_001306876.1
DBSOURCE    REFSEQ: accession NM_001319947.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Sonmez,C., Toia,B., Eickhoff,P., Matei,A.M., El Beyrouthy,M.,
            Wallner,B., Douglas,M.E., de Lange,T. and Lottersberger,F.
  TITLE     DNA-PK controls Apollo's access to leading-end telomeres
  JOURNAL   Nucleic Acids Res 52 (8), 4313-4327 (2024)
   PUBMED   38407308
  REMARK    GeneRIF: DNA-PK controls Apollo's access to leading-end telomeres.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Bories,C., Lejour,T., Adolphe,F., Kermasson,L., Couve,S.,
            Tanguy,L., Luszczewska,G., Watzky,M., Poillerat,V., Garnier,P.,
            Groisman,R., Ferlicot,S., Richard,S., Saparbaev,M., Revy,P., Gad,S.
            and Renaud,F.
  TITLE     DCLRE1B/Apollo germline mutations associated with renal cell
            carcinoma impair telomere protection
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167107 (2024)
   PUBMED   38430974
  REMARK    GeneRIF: DCLRE1B/Apollo germline mutations associated with renal
            cell carcinoma impair telomere protection.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Li,L., Wang,F., Deng,Z., Zhang,G., Zhu,L., Zhao,Z. and Liu,R.
  TITLE     DCLRE1B promotes tumor progression and predicts immunotherapy
            response through METTL3-mediated m6A modification in pancreatic
            cancer
  JOURNAL   BMC Cancer 23 (1), 1073 (2023)
   PUBMED   37936074
  REMARK    GeneRIF: DCLRE1B promotes tumor progression and predicts
            immunotherapy response through METTL3-mediated m6A modification in
            pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Yosaatmadja,Y., Baddock,H.T., Newman,J.A., Bielinski,M.,
            Gavard,A.E., Mukhopadhyay,S.M.M., Dannerfjord,A.A., Schofield,C.J.,
            McHugh,P.J. and Gileadi,O.
  TITLE     Structural and mechanistic insights into the Artemis endonuclease
            and strategies for its inhibition
  JOURNAL   Nucleic Acids Res 49 (16), 9310-9326 (2021)
   PUBMED   34387696
  REMARK    GeneRIF: Structural and mechanistic insights into the Artemis
            endonuclease and strategies for its inhibition.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Lenain,C., Bauwens,S., Amiard,S., Brunori,M., Giraud-Panis,M.J. and
            Gilson,E.
  TITLE     The Apollo 5' exonuclease functions together with TRF2 to protect
            telomeres from DNA repair
  JOURNAL   Curr Biol 16 (13), 1303-1310 (2006)
   PUBMED   16730175
  REMARK    GeneRIF: SNM1B (Apollo) protein exhibits a 5'-to-3' DNA exonuclease
            activity and functions together with TRF2 to protect telomeres from
            damage and fusion.
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Freibaum,B.D. and Counter,C.M.
  TITLE     hSnm1B is a novel telomere-associated protein
  JOURNAL   J Biol Chem 281 (22), 15033-15036 (2006)
   PUBMED   16606622
  REMARK    GeneRIF: the C terminus of Snm1B was shown to interact with the TRF
            homology domain of TRF2 indicating that Snm1B is likely recruited
            to the telomere via interaction with the double-stranded
            telomere-binding protein TRF2
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Ishiai,M., Kimura,M., Namikoshi,K., Yamazoe,M., Yamamoto,K.,
            Arakawa,H., Agematsu,K., Matsushita,N., Takeda,S., Buerstedde,J.M.
            and Takata,M.
  TITLE     DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
            focus formation
  JOURNAL   Mol Cell Biol 24 (24), 10733-10741 (2004)
   PUBMED   15572677
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Demuth,I., Digweed,M. and Concannon,P.
  TITLE     Human SNM1B is required for normal cellular response to both DNA
            interstrand crosslink-inducing agents and ionizing radiation
  JOURNAL   Oncogene 23 (53), 8611-8618 (2004)
   PUBMED   15467758
  REMARK    GeneRIF: siRNA knockdown of hSNM1B rendered cells sensitive to
            ionizing radiation, suggesting the possibility of hSNM1B
            involvement in homologous recombination repair of double-strand
            breaks arising as intermediates of ICL repair
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Dronkert,M.L., de Wit,J., Boeve,M., Vasconcelos,M.L., van Steeg,H.,
            Tan,T.L., Hoeijmakers,J.H. and Kanaar,R.
  TITLE     Disruption of mouse SNM1 causes increased sensitivity to the DNA
            interstrand cross-linking agent mitomycin C
  JOURNAL   Mol Cell Biol 20 (13), 4553-4561 (2000)
   PUBMED   10848582
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA414122.1, BC029687.1 and
            AI669133.1.
            
            Summary: DNA interstrand cross-links prevent strand separation,
            thereby physically blocking transcription, replication, and
            segregation of DNA. DCLRE1B is one of several evolutionarily
            conserved genes involved in repair of interstrand cross-links
            (Dronkert et al., 2000 [PubMed 10848582]).[supplied by OMIM, Mar
            2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: CR936679.1, SRR1660803.129023.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..406
                     /product="5' exonuclease Apollo isoform b"
                     /EC_number="3.5.2.6"
                     /note="DNA cross-link repair 1B (PSO2 homolog, S.
                     cerevisiae); 5' exonuclease Apollo; SNM1 homolog B;
                     beta-lactamase DCLRE1B"
                     /calculated_mol_wt=45681
     Region          <1..25
                     /region_name="metallo-hydrolase-like_MBL-fold"
                     /note="mainly hydrolytic enzymes and related proteins
                     which carry out various biological functions; MBL-fold
                     metallohydrolase domain; cl23716"
                     /db_xref="CDD:451500"
     Region          90..173
                     /region_name="DRMBL"
                     /note="DNA repair metallo-beta-lactamase; pfam07522"
                     /db_xref="CDD:429512"
     Region          370..403
                     /region_name="apollo_TRF2_binding"
                     /note="TRF2-binding region of apollo and similar proteins;
                     cd11662"
                     /db_xref="CDD:212560"
     Site            order(372,374..384)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212560"
     CDS             1..406
                     /gene="DCLRE1B"
                     /gene_synonym="APOLLO; DKCB8; SNM1B; SNMIB"
                     /coded_by="NM_001319947.2:421..1641"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="GeneID:64858"
                     /db_xref="HGNC:HGNC:17641"
                     /db_xref="MIM:609683"
ORIGIN      
        1 mlkepaltlg kqihtlyldn tncnpalvlp srqeaahqiv qlirkhpqhn ikiglyslgk
       61 eslleqlale fqtwvvlspr rlelvqllgl advftveeka grihavdhme ichsnmlrwn
      121 qthptiailp tsrkihsshp dihvipysdh ssyselrafv aalkpcqvvp ivsrrpcggf
      181 qdslsprisv plipdsvqqy mssssrkpsl lwllerrlkr prtqgvvfes peesadqsqa
      241 drdskkakke klspwpadle kqpshhplri kkqlfpdlys kewnkavpfc esqkrvtmlt
      301 aplgfsvhlr stdeefisqk treeiglgsp lvpmgdddgg peatgnqsaw mghgsplshs
      361 skgtpllate frglalkyll tpvnffqagy ssrrfdqqve kyhkpc
//
LOCUS       NP_001351451             596 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SLU7 isoform c [Homo sapiens].
ACCESSION   NP_001351451 XP_005265850
VERSION     NP_001351451.1
DBSOURCE    REFSEQ: accession NM_001364522.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Garate-Rascon,M., Recalde,M., Rojo,C., Fernandez-Barrena,M.G.,
            Avila,M.A., Arechederra,M. and Berasain,C.
  TITLE     SLU7: A New Hub of Gene Expression Regulation-From Epigenetics to
            Protein Stability in Health and Disease
  JOURNAL   Int J Mol Sci 23 (21), 13411 (2022)
   PUBMED   36362191
  REMARK    GeneRIF: SLU7: A New Hub of Gene Expression Regulation-From
            Epigenetics to Protein Stability in Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Garate-Rascon,M., Recalde,M., Jimenez,M., Elizalde,M., Azkona,M.,
            Uriarte,I., Latasa,M.U., Urtasun,R., Bilbao,I., Sangro,B.,
            Garcia-Ruiz,C., Fernandez-Checa,J.C., Corrales,F.J., Esquivel,A.,
            Pineda-Lucena,A., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     Splicing Factor SLU7 Prevents Oxidative Stress-Mediated Hepatocyte
            Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage
  JOURNAL   Hepatology 74 (5), 2791-2807 (2021)
   PUBMED   34170569
  REMARK    GeneRIF: Splicing Factor SLU7 Prevents Oxidative Stress-Mediated
            Hepatocyte Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage.
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Recalde,M., Garate-Rascon,M., Elizalde,M., Azkona,M., Latasa,M.U.,
            Barcena-Varela,M., Sangro,B., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     The splicing regulator SLU7 is required to preserve DNMT1 protein
            stability and DNA methylation
  JOURNAL   Nucleic Acids Res 49 (15), 8592-8609 (2021)
   PUBMED   34331453
  REMARK    GeneRIF: The splicing regulator SLU7 is required to preserve DNMT1
            protein stability and DNA methylation.
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Shomron,N., Reznik,M. and Ast,G.
  TITLE     Splicing factor hSlu7 contains a unique functional domain required
            to retain the protein within the nucleus
  JOURNAL   Mol Biol Cell 15 (8), 3782-3795 (2004)
   PUBMED   15181151
  REMARK    GeneRIF: The zinc-knuckle motif of hSlu7 determines the cellular
            localization of the protein through a nucleocytoplasmic-sensitive
            shuttling balance.
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     An upstream AG determines whether a downstream AG is selected
            during catalytic step II of splicing
  JOURNAL   Mol Cell Biol 21 (5), 1509-1514 (2001)
   PUBMED   11238888
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     The RNA splicing factor hSlu7 is required for correct 3'
            splice-site choice
  JOURNAL   Nature 402 (6758), 207-210 (1999)
   PUBMED   10647016
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     Human step II splicing factor hSlu7 functions in restructuring the
            spliceosome between the catalytic steps of splicing
  JOURNAL   Genes Dev 13 (7), 841-850 (1999)
   PUBMED   10197984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091842.3.
            
            On Jun 20, 2018 this sequence version replaced XP_005265850.1.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is a
            splicing factor that has been found to be essential during the
            second catalytic step in the pre-mRNA splicing process. It
            associates with the spliceosome and contains a zinc knuckle motif
            that is found in other splicing factors and is involved in
            protein-nucleic acid and protein-protein interactions. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (6), as well as variant 7, encodes
            isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.160274.1,
                                           SRR1803611.222445.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..596
                     /product="pre-mRNA-splicing factor SLU7 isoform c"
                     /note="step II splicing factor SLU7; zinc knuckle motif
                     containing; pre-mRNA-splicing factor SLU7; SLU7 splicing
                     factor homolog; SLU7 homolog, splicing factor"
                     /calculated_mol_wt=69273
     Region          171..444
                     /region_name="Slu7"
                     /note="Pre-mRNA splicing Prp18-interacting factor;
                     pfam11708"
                     /db_xref="CDD:463326"
     CDS             1..596
                     /gene="SLU7"
                     /gene_synonym="9G8; hSlu7"
                     /coded_by="NM_001364522.2:473..2263"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="GeneID:10569"
                     /db_xref="HGNC:HGNC:16939"
                     /db_xref="MIM:605974"
ORIGIN      
        1 mktsiggqit msatvvdavn aaplsgskem sleepkkmtr edwrkkkele eqrklgnapa
       61 evdeegkdin phipqyissv pwyidpskrp tlkhqrpqpe kqkqfsssge wykrgvkens
      121 iitkyrkgac encgamthkk kdcferprrv gakftgtnia pdehvqpqlm fdydgkrdrw
      181 ngynpeehmk iveeyakvdl akrtlkaqkl qeelasgklv eqanspkhqw geeepnsqme
      241 kdhnsedede dkyaddidmp gqnfdskrri tvrnlrired iakylrnldp nsayydpktr
      301 amrenpyana gknpdevsya gdnfvrytgd tismaqtqlf aweaydkgse vhlqadptkl
      361 ellyksfkvk kedfkeqqke silekyggqe hldappaell laqtedyvey srhgtvikgq
      421 eravacskye edvkihnhth iwgsywkegr wgykcchsff kysyctgeag keivnseeci
      481 ineitgeesv kkpqtlmelh qeklkeekkk kkkkkkkhrk sssdsddeek kheklkkaln
      541 aeearllhvk etmqiderkr pynsmyetre pteeemeayr mkrqrpddpm asflgq
//
LOCUS       NP_689739               1143 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog B isoform Par3Lb [Homo sapiens].
ACCESSION   NP_689739
VERSION     NP_689739.4
DBSOURCE    REFSEQ: accession NM_152526.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1143)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   2  (residues 1 to 1143)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1143)
  AUTHORS   Thompson,B.J.
  TITLE     Par-3 family proteins in cell polarity & adhesion
  JOURNAL   FEBS J 289 (3), 596-613 (2022)
   PUBMED   33565714
  REMARK    GeneRIF: Par-3 family proteins in cell polarity & adhesion.
            Review article
REFERENCE   4  (residues 1 to 1143)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   5  (residues 1 to 1143)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1143)
  AUTHORS   Izaki,T., Kamakura,S., Kohjima,M. and Sumimoto,H.
  TITLE     Phosphorylation-dependent binding of 14-3-3 to Par3beta, a human
            Par3-related cell polarity protein
  JOURNAL   Biochem Biophys Res Commun 329 (1), 211-218 (2005)
   PUBMED   15721295
  REMARK    GeneRIF: binding of 14-3-3 to Par3beta is dependent on
            phosphorylation
REFERENCE   7  (residues 1 to 1143)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 1143)
  AUTHORS   Kohjima,M., Noda,Y., Takeya,R., Saito,N., Takeuchi,K. and
            Sumimoto,H.
  TITLE     PAR3beta, a novel homologue of the cell polarity protein PAR3,
            localizes to tight junctions
  JOURNAL   Biochem Biophys Res Commun 299 (4), 641-646 (2002)
   PUBMED   12459187
  REMARK    GeneRIF: PAR3beta, expressed intrinsically or extrinsically,
            localizes to the tight junctions, indicating that the localization
            does not require the ternary complex formation.
REFERENCE   9  (residues 1 to 1143)
  AUTHORS   Gao,L., Macara,I.G. and Joberty,G.
  TITLE     Multiple splice variants of Par3 and of a novel related gene,
            Par3L, produce proteins with different binding properties
  JOURNAL   Gene 294 (1-2), 99-107 (2002)
   PUBMED   12234671
REFERENCE   10 (residues 1 to 1143)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016903.3, AC007736.3, AC009316.3, AC011750.8, AC008171.3,
            AC007465.4, AC007746.4 and AC007385.3.
            
            On Dec 8, 2006 this sequence version replaced NP_689739.3.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (Par3Lb) is
            shorter compared to isoform Par3La.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..1143
                     /product="partitioning defective 3 homolog B isoform
                     Par3Lb"
                     /note="partitioning-defective 3-beta; amyotrophic lateral
                     sclerosis 2 (juvenile) chromosome region, candidate 19;
                     partitioning defective 3 homolog B; PAR3-L protein;
                     partitioning defective 3-like protein; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 19 protein;
                     par-3 partitioning defective 3 homolog B"
                     /calculated_mol_wt=125972
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          197..294
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(212..218,234,237,267,271,274..275)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          377..469
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(392..398,413,416,446,450,453..454)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          <479..529
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     CDS             1..1143
                     /gene="PARD3B"
                     /gene_synonym="ALS2CR19; PAR3B; PAR3beta; PAR3L"
                     /coded_by="NM_152526.6:526..3957"
                     /note="isoform Par3Lb is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42806.1"
                     /db_xref="GeneID:117583"
                     /db_xref="HGNC:HGNC:14446"
                     /db_xref="MIM:619353"
ORIGIN      
        1 mkvtvcfgrt givvpckegq lrvgeltqqa lqrylktrek gpgywvkihh leytdggild
       61 pddvladvve dkdkliavfe eqeplhkies psgnpadrqs pdafetevaa qlaafkpigg
      121 eievtpsalk lgtpllvrrs sdpvpgppad tqpsashpgg qslklvvpds tqnledrevl
      181 ngvqtellts prtkdtlsdm trtveisgeg gplgihvvpf fsslsgrilg lfirgiedns
      241 rskreglfhe necivkinnv dlvdktfaqa qdvfrqamks psvllhvlpp qnreqyeksv
      301 igslnifgnn dgvlktkvpp pvhgksglkt anltgtdspe tdasaslqqn ksprvprlgg
      361 kpsspslspl mgfgsnknak kikidlkkgp eglgftvvtr dssihgpgpi fvknilpkga
      421 aikdgrlqsg drilevngrd vtgrtqeelv amlrstkqge taslviarqe ghflpreldg
      481 rlrmndqlia vngesllgks nheametlrr smsmegnirg miqlvilrrp erpmedpaec
      541 gafskpcfen cqnavttsrr ndnsilhplg tcspqdkqkg lllpndgwae sevppsptph
      601 salglgledy shssgvdsav yfpdqhinfr svtparqpes inlkasksmd lvpdeskvhs
      661 lagqksesps kdfgptlglk ksssleslqt avaevrkndl pfhrprphmv rgrgcnesfr
      721 aaidksydgp eeieadglsd ksshsgqgal ncesapqgns eledmenkar kvkktkekek
      781 kkekgklkvk ekkrkeened perkikkkgf gamlrfgkkk edkggkaeqk gtlkhgglre
      841 eelekmkeer erigakhqel rekqarglld yatgaigsvy dmdddemdpn yarvnhfrep
      901 ctsanvfrsp sppragpfgy prdghplspe rdhleglyak vnkpyhplvp adsgrptggs
      961 tdriqklrke yyqarregfp lyeddegrar pseydllwvp grgpdgnahn lrfegmerqy
     1021 aslprggpad pvdylpaapr glykerelpy ypgahpmhpp kgsyprptel rvadlrypqh
     1081 yppppapqhk gpfrqdvpps ppqhqrmpay qetgrpgprg gspdqypyrt qdsrqknpmt
     1141 aav
//
LOCUS       NP_001356343             297 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356343 XP_016881950
VERSION     NP_001356343.1
DBSOURCE    REFSEQ: accession NM_001369414.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 297)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 297)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138128.1, AC139353.3 and
            AC092309.3.
            
            On Apr 9, 2019 this sequence version replaced XP_016881950.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.492204.1,
                                           SRR14038191.1884473.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..297
                     /product="DNA excision repair protein ERCC-1 isoform 2"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=32431
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          220..297
                     /region_name="HhH2, dimerization with ERCC4/XPF.
                     /evidence=ECO:0000269|PubMed:16338413"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          <251..293
                     /region_name="MUS81"
                     /note="ERCC4-type crossover junction endonuclease
                     [Replication, recombination and repair]; COG1948"
                     /db_xref="CDD:441551"
     CDS             1..297
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369414.1:206..1099"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS12662.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq karrlfdvlh epflkvp
//
LOCUS       NP_060174                239 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 49 [Homo sapiens].
ACCESSION   NP_060174
VERSION     NP_060174.2
DBSOURCE    REFSEQ: accession NM_017704.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Zhou,X., Wang,W.T., Sun,J., Liu,H.Y., Bai,X.Y., Liu,J.J., Yu,B.F.,
            Guo,R. and Wang,H.L.
  TITLE     ANKRD49 inhibits etoposide-induced intrinsic apoptosis of GC-1
            cells by modulating NF-kappaB signaling
  JOURNAL   Mol Cell Biochem 457 (1-2), 21-29 (2019)
   PUBMED   30798416
  REMARK    GeneRIF: these results suggest that ANKRD49 plays an important role
            in reducing intrinsic apoptosis of GC-1 cells by modulating the
            NF-kappaB signaling pathway.
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Liu,C.G., Cui,X.L., Wei,Z.G. and Guo,J.S.
  TITLE     High expression of the ANKRD49 protein is associated with
            progression and poor prognosis of gastric cancer
  JOURNAL   Cancer Biomark 22 (4), 649-656 (2018)
   PUBMED   29865034
  REMARK    GeneRIF: The results of the present study highlighted an important
            role of the ANKRD49 protein in the progression of gastric cancer.
            The ANKRD49 protein could act as a potential biomarker for
            prognosis evaluation of gastric cancer and may be used as a
            molecular target for gastric cancer treatment.
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Cockman,M.E., Lancaster,D.E., Stolze,I.P., Hewitson,K.S.,
            McDonough,M.A., Coleman,M.L., Coles,C.H., Yu,X., Hay,R.T.,
            Ley,S.C., Pugh,C.W., Oldham,N.J., Masson,N., Schofield,C.J. and
            Ratcliffe,P.J.
  TITLE     Posttranslational hydroxylation of ankyrin repeats in IkappaB
            proteins by the hypoxia-inducible factor (HIF) asparaginyl
            hydroxylase, factor inhibiting HIF (FIH)
  JOURNAL   Proc Natl Acad Sci U S A 103 (40), 14767-14772 (2006)
   PUBMED   17003112
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Blau,C.A., Barbas,C.F. 3rd, Bomhoff,A.L., Neades,R., Yan,J.,
            Navas,P.A. and Peterson,K.R.
  TITLE     {gamma}-Globin gene expression in chemical inducer of dimerization
            (CID)-dependent multipotential cells established from human
            {beta}-globin locus yeast artificial chromosome ({beta}-YAC)
            transgenic mice
  JOURNAL   J Biol Chem 280 (44), 36642-36647 (2005)
   PUBMED   16131492
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Pitts,S.A., Kullar,H.S., Stankovic,T., Stewart,G.S., Last,J.I.,
            Bedenham,T., Armstrong,S.J., Piane,M., Chessa,L., Taylor,A.M. and
            Byrd,P.J.
  TITLE     hMRE11: genomic structure and a null mutation identified in a
            transcript protected from nonsense-mediated mRNA decay
  JOURNAL   Hum Mol Genet 10 (11), 1155-1162 (2001)
   PUBMED   11371508
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Yang,Y., Duan,Z., Skarpidi,E., Li,Q., Papayannopoulou,T. and
            Stamatoyannopoulos,G.
  TITLE     Cloning and characterization of a potential transcriptional
            activator of human gamma-globin genes
  JOURNAL   Blood Cells Mol Dis 27 (1), 1-15 (2001)
   PUBMED   11162141
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP000786.4, BG025192.1, BC017798.1, AK057696.1 and AL833977.1.
            
            On Jan 27, 2004 this sequence version replaced NP_060174.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.7934.1,
                                           SRR1803614.92340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000544612.6/ ENSP00000440396.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q21"
     Protein         1..239
                     /product="ankyrin repeat domain-containing protein 49"
                     /note="fetal globin-inducing factor"
                     /calculated_mol_wt=27159
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WVL7.1)"
     Region          73..103
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVL7.1)"
     Region          <77..>218
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          78..105
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(79..80,83..85,87..88,92,96,105,107,109,113..114,
                     117..119,121..122,126,129,138,140,142,146..147,150..152,
                     154..155,159,162)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          107..138
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          107..136
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVL7.1)"
     Region          140..170
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          140..169
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVL7.1)"
     Region          173..206
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVL7.1)"
     CDS             1..239
                     /gene="ANKRD49"
                     /gene_synonym="FGIF; GBIF"
                     /coded_by="NM_017704.3:143..862"
                     /db_xref="CCDS:CCDS8300.1"
                     /db_xref="GeneID:54851"
                     /db_xref="HGNC:HGNC:25970"
                     /db_xref="MIM:619571"
ORIGIN      
        1 mekekgnddg ipdqensldf sehfnqlell ethghliptg tqslwvgnsd edeeqddkne
       61 ewyrlqekkm ekdpsrlllw aaeknrlttv rrllsekath vntrdedeyt plhraaysgh
      121 ldivqeliaq gadvhavtvd gwtplhsack wnntrvasfl lqhdadinaq tkglltplhl
      181 aagnrdskdt lelllmnryv kpglknnlee tafdiarrts iyhylfeive gctnsspqs
//
LOCUS       NP_001317432             282 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 1 isoform
            2 [Homo sapiens].
ACCESSION   NP_001317432 XP_011523336
VERSION     NP_001317432.1
DBSOURCE    REFSEQ: accession NM_001330503.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 282)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 282)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 282)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 282)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 282)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 282)
  AUTHORS   Ishijima,S., Asai,T., Kita,K., Sonoda,T. and Tatibana,M.
  TITLE     Partial reconstitution of mammalian phosphoribosylpyrophosphate
            synthetase in Escherichia coli cells. Coexpression of catalytic
            subunits with the 39-kDa associated protein leads to formation of
            soluble multimeric complexes of various compositions
  JOURNAL   Biochim Biophys Acta 1342 (1), 28-36 (1997)
   PUBMED   9366267
REFERENCE   7  (residues 1 to 282)
  AUTHORS   Ishizuka,T., Ahmad,I., Kita,K., Sonoda,T., Ishijima,S., Sawa,K.,
            Suzuki,N. and Tatibana,M.
  TITLE     The human phosphoribosylpyrophosphate synthetase-associated protein
            39 gene (PRPSAP1) is located in the chromosome region 17q24-q25
  JOURNAL   Genomics 33 (2), 332-334 (1996)
   PUBMED   8660991
REFERENCE   8  (residues 1 to 282)
  AUTHORS   Ishizuka,T., Kita,K., Sonoda,T., Ishijima,S., Sawa,K., Suzuki,N.
            and Tatibana,M.
  TITLE     Cloning and sequencing of human complementary DNA for the
            phosphoribosylpyrophosphate synthetase-associated protein 39
  JOURNAL   Biochim Biophys Acta 1306 (1), 27-30 (1996)
   PUBMED   8611620
REFERENCE   9  (residues 1 to 282)
  AUTHORS   Tatibana,M., Kita,K., Taira,M., Ishijima,S., Sonoda,T.,
            Ishizuka,T., Iizasa,T. and Ahmad,I.
  TITLE     Mammalian phosphoribosyl-pyrophosphate synthetase
  JOURNAL   Adv Enzyme Regul 35, 229-249 (1995)
   PUBMED   7572345
  REMARK    Review article
REFERENCE   10 (residues 1 to 282)
  AUTHORS   Kita,K., Ishizuka,T., Ishijima,S., Sonoda,T. and Tatibana,M.
  TITLE     A novel 39-kDa phosphoribosylpyrophosphate synthetase-associated
            protein of rat liver. Cloning, high sequence similarity to the
            catalytic subunits, and a negative regulatory role
  JOURNAL   J Biol Chem 269 (11), 8334-8340 (1994)
   PUBMED   8132556
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC090699.10.
            
            On Aug 29, 2016 this sequence version replaced XP_011523336.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.353560.1,
                                           SRR1803611.188415.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..282
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..282
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 1 isoform 2"
                     /EC_number="2.7.6.1"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 1; PRPP synthase-associated protein 1; 39 kDa
                     phosphoribosypyrophosphate synthase-associated protein"
                     /calculated_mol_wt=31135
     Region          <1..52
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          93..276
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..282
                     /gene="PRPSAP1"
                     /gene_synonym="PAP39"
                     /coded_by="NM_001330503.2:456..1304"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82209.1"
                     /db_xref="GeneID:5635"
                     /db_xref="HGNC:HGNC:9466"
                     /db_xref="MIM:601249"
ORIGIN      
        1 mellimayal ktacarniig vipyfpyskq skmrkrgsiv ckllasmlak aglthiitmd
       61 lhqkeiqgff sfpvdnlras pfllqyiqee ipnyrnaviv akspdaakra qsyaerlrlg
      121 lavihgeaqc teldmddgrh sppmvknatv hpglelplmm akekppitvv gdvggriaii
      181 vddiiddves fvaaaeilke rgaykiyvma thgilsaeap rlieessvde vvvtntvphe
      241 vqklqcpkik tvdislilse airrihnges maylfrnitv dd
//
LOCUS       NP_000929               1174 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_000929
VERSION     NP_000929.1
DBSOURCE    REFSEQ: accession NM_000938.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Lin,H., Cui,Z., E,T., Xu,H., Wang,D., Wang,P., Ruan,X., Liu,L. and
            Xue,Y.
  TITLE     M6A-methylated circPOLR2B forms an R-loop and regulates the
            biological behavior of glioma stem cells through positive feedback
            loops
  JOURNAL   Cell Death Dis 15 (8), 554 (2024)
   PUBMED   39090090
  REMARK    GeneRIF: M6A-methylated circPOLR2B forms an R-loop and regulates
            the biological behavior of glioma stem cells through positive
            feedback loops.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Li,X.L., Xie,Y., Chen,Y.L., Zhang,Z.M., Tao,Y.F., Li,G., Wu,D.,
            Wang,H.R., Zhuo,R., Pan,J.J., Yu,J.J., Jia,S.Q., Zhang,Z.,
            Feng,C.X., Wang,J.W., Fang,F., Qian,G.H., Lu,J., Hu,S.Y., Li,Z.H.
            and Pan,J.
  TITLE     The RNA polymerase II subunit B (RPB2) functions as a growth
            regulator in human glioblastoma
  JOURNAL   Biochem Biophys Res Commun 674, 170-182 (2023)
   PUBMED   37423037
  REMARK    GeneRIF: The RNA polymerase II subunit B (RPB2) functions as a
            growth regulator in human glioblastoma.
REFERENCE   3  (residues 1 to 1174)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1174)
  AUTHORS   Lykke-Andersen,S., Rouviere,J.O. and Jensen,T.H.
  TITLE     ARS2/SRRT: at the nexus of RNA polymerase II transcription,
            transcript maturation and quality control
  JOURNAL   Biochem Soc Trans 49 (3), 1325-1336 (2021)
   PUBMED   34060620
  REMARK    GeneRIF: ARS2/SRRT: at the nexus of RNA polymerase II
            transcription, transcript maturation and quality control.
            Review article
REFERENCE   5  (residues 1 to 1174)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   6  (residues 1 to 1174)
  AUTHORS   Schaller,S., Grandemange,S., Shpakovski,G.V., Golemis,E.A.,
            Kedinger,C. and Vigneron,M.
  TITLE     Interactions between the full complement of human RNA polymerase II
            subunits
  JOURNAL   FEBS Lett 461 (3), 253-257 (1999)
   PUBMED   10567706
REFERENCE   7  (residues 1 to 1174)
  AUTHORS   Kershnar,E., Wu,S.Y. and Chiang,C.M.
  TITLE     Immunoaffinity purification and functional characterization of
            human transcription factor IIH and RNA polymerase II from clonal
            cell lines that conditionally express epitope-tagged subunits of
            the multiprotein complexes
  JOURNAL   J Biol Chem 273 (51), 34444-34453 (1998)
   PUBMED   9852112
REFERENCE   8  (residues 1 to 1174)
  AUTHORS   Acker,J., de Graaff,M., Cheynel,I., Khazak,V., Kedinger,C. and
            Vigneron,M.
  TITLE     Interactions between the human RNA polymerase II subunits
  JOURNAL   J Biol Chem 272 (27), 16815-16821 (1997)
   PUBMED   9201987
REFERENCE   9  (residues 1 to 1174)
  AUTHORS   Acker,J., Mattei,M.G., Wintzerith,M., Roeckel,N., Depetris,D.,
            Vigneron,M. and Kedinger,C.
  TITLE     Chromosomal localization of human RNA polymerase II subunit genes
  JOURNAL   Genomics 20 (3), 496-499 (1994)
   PUBMED   8034326
REFERENCE   10 (residues 1 to 1174)
  AUTHORS   Acker,J., Wintzerith,M., Vigneron,M. and Kedinger,C.
  TITLE     Primary structure of the second largest subunit of human RNA
            polymerase II (or B)
  JOURNAL   J Mol Biol 226 (4), 1295-1299 (1992)
   PUBMED   1518060
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC023503.2 and AK294901.1.
            
            Summary: This gene encodes the second largest subunit of RNA
            polymerase II (Pol II), a DNA-dependent RNA polymerase that
            catalyzes the transcription of DNA into precursors of mRNA, snRNA
            and microRNA. This subunit and the largest subunit form opposite
            sides of the center cleft of Pol II. Deletion of the flap loop
            region of this subunit results in a decrease in the rate of
            transcriptional elongation. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.148220.1, BC023503.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314595.6/ ENSP00000312735.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..1174
                     /product="DNA-directed RNA polymerase II subunit RPB2
                     isoform 1"
                     /EC_number="2.7.7.6"
                     /EC_number="2.7.7.48"
                     /note="RNA polymerase II second largest subunit;
                     DNA-directed RNA polymerase II subunit RPB2; RNA
                     polymerase II subunit 2; RNA polymerase II subunit B2;
                     DNA-directed RNA polymerase II subunit B; DNA-directed RNA
                     polymerase II 140 kDa polypeptide; polymerase (RNA) II
                     (DNA directed) polypeptide B, 140kDa; polymerase (RNA) II
                     subunit B; 3'-5' exoribonuclease; RNA-directed RNA
                     polymerase II subunit RPB2"
                     /calculated_mol_wt=133766
     Region          27..1172
                     /region_name="Ricin_B_lectin"
                     /note="Ricin-type beta-trefoil lectin domain; cl47023"
                     /db_xref="CDD:481363"
     Site            937
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30876.1)"
     Site            1052
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P30876.1)"
     CDS             1..1174
                     /gene="POLR2B"
                     /gene_synonym="hRPB140; POL2RB; RPB2"
                     /coded_by="NM_000938.3:91..3615"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3511.1"
                     /db_xref="GeneID:5431"
                     /db_xref="HGNC:HGNC:9188"
                     /db_xref="MIM:180661"
ORIGIN      
        1 mydadedmqy dedddeitpd lwqeacwivi ssyfdekglv rqqldsfdef iqmsvqrive
       61 dappidlqae aqhasgevee ppryllkfeq iylskpthwe rdgapspmmp nearlrnlty
      121 saplyvditk tvikegeeql qtqhqktfig kipimlrsty cllngltdrd lcelnecpld
      181 pggyfiings ekvliaqekm atntvyvfak kdskyaytge crsclenssr ptstiwvsml
      241 arggqgakks aigqrivatl pyikqevpii ivfralgfvs drdilehiiy dfedpemmem
      301 vkpsldeafv iqeqnvalnf igsrgakpgv tkekrikyak evlqkemlph vgvsdfcetk
      361 kayflgymvh rlllaalgrr elddrdhygn krldlagpll aflfrgmfkn llkevriyaq
      421 kfidrgkdfn lelaiktrii sdglkyslat gnwgdqkkah qaragvsqvl nrltfastls
      481 hlrrlnspig rdgklakprq lhntlwgmvc paetpeghav glvknlalma yisvgsqpsp
      541 ilefleewsm enleeispaa iadatkifvn gcwvgihkdp eqlmntlrkl rrqmdiivse
      601 vsmirdirer eiriytdagr icrpllivek qklllkkrhi dqlkereynn yswqdlvasg
      661 vveyidtlee etvmlamtpd dlqekevayc stythceihp smilgvcasi ipfpdhnqsp
      721 rntyqsamgk qamgvyitnf hvrmdtlahv lyypqkplvt trsmeylrfr elpaginsiv
      781 aiasytgynq edsvimnrsa vdrgffrsvf yrsykeqesk kgfdqeevfe kptretcqgm
      841 rhaiydkldd dgliapgvrv sgddviigkt vtlpenedel estnrrytkr dcstflrtse
      901 tgivdqvmvt lnqegykfck irvrsvripq igdkfasrhg qkgtcgiqyr qedmpftceg
      961 itpdiiinph aipsrmtigh lieclqgkvs ankgeigdat pfndavnvqk isnllsdygy
     1021 hlrgnevlyn gftgrkitsq ifigptyyqr lkhmvddkih srargpiqil nrqpmegrsr
     1081 dgglrfgeme rdcqiahgaa qflrerlfea sdpyqvhvcn lcgimaiant rthtyecrgc
     1141 rnktqislvr mpyackllfq elmsmsiapr mmsv
//
LOCUS       NP_001108488             878 aa            linear   PRI 20-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001108488
VERSION     NP_001108488.1
DBSOURCE    REFSEQ: accession NM_001115016.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Wu,D., Zhao,L., Feng,Z., Yu,C., Ding,J., Wang,L., Wang,F., Liu,D.,
            Zhu,H., Xing,F., Conaway,J.W., Conaway,R.C., Cai,Y. and Jin,J.
  TITLE     O-Linked N-acetylglucosamine transferase 1 regulates global histone
            H4 acetylation via stabilization of the nonspecific lethal protein
            NSL3
  JOURNAL   J Biol Chem 292 (24), 10014-10025 (2017)
   PUBMED   28450392
  REMARK    GeneRIF: Data suggest that O-GlcNAc transferase 1 (OGT1)
            specifically binds to, O-GlcNAcylates, and stabilizes nonspecific
            lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates
            global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16.
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Chatterjee,A., Seyfferth,J., Lucci,J., Gilsbach,R., Preissl,S.,
            Bottinger,L., Martensson,C.U., Panhale,A., Stehle,T., Kretz,O.,
            Sahyoun,A.H., Avilov,S., Eimer,S., Hein,L., Pfanner,N., Becker,T.
            and Akhtar,A.
  TITLE     MOF Acetyl Transferase Regulates Transcription and Respiration in
            Mitochondria
  JOURNAL   Cell 167 (3), 722-738 (2016)
   PUBMED   27768893
REFERENCE   5  (residues 1 to 878)
  AUTHORS   Meunier,S., Shvedunova,M., Van Nguyen,N., Avila,L., Vernos,I. and
            Akhtar,A.
  TITLE     An epigenetic regulator emerges as microtubule minus-end binding
            and stabilizing factor in mitosis
  JOURNAL   Nat Commun 6, 7889 (2015)
   PUBMED   26243146
  REMARK    GeneRIF: microtubule minus-end-binding protein, essential for
            spindle assembly and chromosome segregation
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 878)
  AUTHORS   Zhao,X., Su,J., Wang,F., Liu,D., Ding,J., Yang,Y., Conaway,J.W.,
            Conaway,R.C., Cao,L., Wu,D., Wu,M., Cai,Y. and Jin,J.
  TITLE     Crosstalk between NSL histone acetyltransferase and MLL/SET
            complexes: NSL complex functions in promoting histone H3K4
            di-methylation activity by MLL/SET complexes
  JOURNAL   PLoS Genet 9 (11), e1003940 (2013)
   PUBMED   24244196
REFERENCE   7  (residues 1 to 878)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
REFERENCE   8  (residues 1 to 878)
  AUTHORS   Rea,S., Xouri,G. and Akhtar,A.
  TITLE     Males absent on the first (MOF): from flies to humans
  JOURNAL   Oncogene 26 (37), 5385-5394 (2007)
   PUBMED   17694080
  REMARK    Review article
REFERENCE   9  (residues 1 to 878)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 878)
  AUTHORS   Mendjan,S., Taipale,M., Kind,J., Holz,H., Gebhardt,P., Schelder,M.,
            Vermeulen,M., Buscaino,A., Duncan,K., Mueller,J., Wilm,M.,
            Stunnenberg,H.G., Saumweber,H. and Akhtar,A.
  TITLE     Nuclear pore components are involved in the transcriptional
            regulation of dosage compensation in Drosophila
  JOURNAL   Mol Cell 21 (6), 811-823 (2006)
   PUBMED   16543150
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB275425.1 and BC063792.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063792.1, SRR14038195.535750.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431828.6/ ENSP00000396749.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..878
                     /product="KAT8 regulatory NSL complex subunit 3 isoform 1"
                     /note="serum inhibited-related protein; testis development
                     protein PRTD; NSL complex protein NSL3; non-specific
                     lethal 3 homolog"
                     /calculated_mol_wt=93040
     Region          <323..472
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
     CDS             1..878
                     /gene="KANSL3"
                     /gene_synonym="KIAA1310; NSL3; Rcd1"
                     /coded_by="NM_001115016.3:81..2717"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46361.1"
                     /db_xref="GeneID:55683"
                     /db_xref="HGNC:HGNC:25473"
                     /db_xref="MIM:617742"
ORIGIN      
        1 mahrggerdf qtsarrmgts llfqlsvher eldlvfldhs yakpwsahpd assarptrml
       61 fvtprrqhes tiesdvpidv etvtstpmpl ydnqkarsvm necerhvifa rtdadapppp
      121 edweehvnrt gwtmaqnklf nkilkalqsd rlarlanega cnepvlrrva vdkcarrvrq
      181 alasvswdtk liqwlhttlv etlslpmlaa yldalqtlkg kiptlidrml vssntktgaa
      241 gaealslllk rpwdpavgvl shnkpsklpg spliliassg psssvfptsr rhrfwqsqls
      301 clgkvipvat hllnngsgvg vlqclehmig avrskvleih shfphkpiil igwntgalva
      361 chvsvmeyvt avvclgfpll tvdgprgdvd dplldmktpv lfvigqnslq chpeamedfr
      421 ekiraenslv vvggaddnlr iskakkkseg ltqsmvdrci qdeivdfltg vltraeghmg
      481 seprdqdaek kkkprdvarr dlafevperg srpaspaakl paspsgsedl ssvsssptss
      541 pktkvttvts aqkssqigss qllkrhvqrt eavlthkqaq vpisseppee gekedlrvql
      601 krhhpssplp gsktskrpki kvslisqgdt aggpcapsqg sapeaaggkp itmtlgqasa
      661 gakeltgllt takssssegg vsaspvpsvv ssstapsalh tlqsrlvats pgsslpgats
      721 assllqglsf slqdisskts glpanpspgp apqatsvklp tpmqslgait tgtstivrti
      781 pvattlsslg atpggkptai hqlltnggla klasslpgla qisnqasglk vpttitltlr
      841 gqpsrittls pmgsgaapse esssqvlpss sqrlppap
//
LOCUS       NP_542775                671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_542775
VERSION     NP_542775.2
DBSOURCE    REFSEQ: accession NM_080737.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            On Jul 3, 2008 this sequence version replaced NP_542775.1.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014913.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_080737.3:357..2372"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_001091996             394 aa            linear   PRI 20-NOV-2025
DEFINITION  junctional adhesion molecule-like isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001091996
VERSION     NP_001091996.1
DBSOURCE    REFSEQ: accession NM_001098526.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 394)
  AUTHORS   Hao,Z., Xin,Z., Chen,Y., Shao,Z., Lin,W., Wu,W., Lin,M., Liu,Q.,
            Chen,D., Wu,D. and Wu,P.
  TITLE     JAML promotes the antitumor role of tumor-resident CD8+ T cells by
            facilitating their innate-like function in human lung cancer
  JOURNAL   Cancer Lett 590, 216839 (2024)
   PUBMED   38570084
  REMARK    GeneRIF: JAML promotes the antitumor role of tumor-resident CD8[+]
            T cells by facilitating their innate-like function in human lung
            cancer.
REFERENCE   2  (residues 1 to 394)
  AUTHORS   Cheng,S., Li,M., Li,C., Dai,Y., Zhuo,J., Wang,J., Qian,J. and
            Hao,Z.
  TITLE     JAML inhibits colorectal carcinogenesis by modulating the tumor
            immune microenvironment
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 382-396 (2024)
   PUBMED   38625487
  REMARK    GeneRIF: JAML inhibits colorectal carcinogenesis by modulating the
            tumor immune microenvironment.
REFERENCE   3  (residues 1 to 394)
  AUTHORS   Wu,Q., Wang,Y.B., Che,X.W., Wang,H. and Wang,W.
  TITLE     Junctional adhesion molecule-like protein as a novel target for
            kaempferol to ameliorate lung adenocarcinoma
  JOURNAL   J Integr Med 21 (3), 268-276 (2023)
   PUBMED   37069006
  REMARK    GeneRIF: Junctional adhesion molecule-like protein as a novel
            target for kaempferol to ameliorate lung adenocarcinoma.
REFERENCE   4  (residues 1 to 394)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 394)
  AUTHORS   Wu,Q., Li,R., Wang,Q.X., Zhang,M.Y., Liu,T.T. and Qu,Y.Q.
  TITLE     Junctional adhesion molecule-like protein promotes tumor
            progression via the Wnt/beta-catenin signaling pathway in lung
            adenocarcinoma
  JOURNAL   J Transl Med 20 (1), 260 (2022)
   PUBMED   35672776
  REMARK    GeneRIF: Junctional adhesion molecule-like protein promotes tumor
            progression via the Wnt/beta-catenin signaling pathway in lung
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 394)
  AUTHORS   Ramani,S.R., Tom,I., Lewin-Koh,N., Wranik,B., Depalatis,L.,
            Zhang,J., Eaton,D. and Gonzalez,L.C.
  TITLE     A secreted protein microarray platform for extracellular protein
            interaction discovery
  JOURNAL   Anal Biochem 420 (2), 127-138 (2012)
   PUBMED   21982860
REFERENCE   7  (residues 1 to 394)
  AUTHORS   Guo,Y.L., Bai,R., Chen,C.X., Liu,D.Q., Liu,Y., Zhang,C.Y. and
            Zen,K.
  TITLE     Role of junctional adhesion molecule-like protein in mediating
            monocyte transendothelial migration
  JOURNAL   Arterioscler Thromb Vasc Biol 29 (1), 75-83 (2009)
   PUBMED   18948633
REFERENCE   8  (residues 1 to 394)
  AUTHORS   Luissint,A.C., Lutz,P.G., Calderwood,D.A., Couraud,P.O. and
            Bourdoulous,S.
  TITLE     JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
            in cis by alpha4beta1 integrin activation
  JOURNAL   J Cell Biol 183 (6), 1159-1173 (2008)
   PUBMED   19064666
  REMARK    GeneRIF: Integrin activation is required for the dissociation of
            JAM-L-VLA-4 complexes and the accumulation of functional JAM-L
            dimers, which indicates that the leukocyte integrin VLA-4 controls
            JAM-L function in cis by controlling its dimerization state.
REFERENCE   9  (residues 1 to 394)
  AUTHORS   Zen,K., Liu,Y., McCall,I.C., Wu,T., Lee,W., Babbin,B.A., Nusrat,A.
            and Parkos,C.A.
  TITLE     Neutrophil migration across tight junctions is mediated by adhesive
            interactions between epithelial coxsackie and adenovirus receptor
            and a junctional adhesion molecule-like protein on neutrophils
  JOURNAL   Mol Biol Cell 16 (6), 2694-2703 (2005)
   PUBMED   15800062
REFERENCE   10 (residues 1 to 394)
  AUTHORS   Moog-Lutz,C., Cave-Riant,F., Guibal,F.C., Breau,M.A., Di Gioia,Y.,
            Couraud,P.O., Cayre,Y.E., Bourdoulous,S. and Lutz,P.G.
  TITLE     JAML, a novel protein with characteristics of a junctional adhesion
            molecule, is induced during differentiation of myeloid leukemia
            cells
  JOURNAL   Blood 102 (9), 3371-3378 (2003)
   PUBMED   12869515
  REMARK    GeneRIF: expressed on leukocytes with a possible role in leukocyte
            transmigration
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC296115.1, AY138965.1, AK097285.1 and AP002800.4.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY138965.1, AJ515553.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356289.10/ ENSP00000348635.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..394
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..394
                     /product="junctional adhesion molecule-like isoform 1
                     precursor"
                     /note="adhesion molecule AMICA; dendritic-cell specific
                     protein CREA7-1; adhesion molecule, interacts with CXADR
                     antigen 1; dendritic-cell specific protein CREA7-4;
                     adhesion molecule interacting with CXADR antigen 1"
                     /calculated_mol_wt=42209
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2149
     mat_peptide     20..394
                     /product="Junctional adhesion molecule-like.
                     /id=PRO_0000015074"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YT9.1)"
                     /calculated_mol_wt=42209
     Region          25..136
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YT9.1)"
     Region          138..251
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86YT9.1)"
     Site            276..296
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YT9.1)"
     Region          369..394
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YT9.1)"
     CDS             1..394
                     /gene="JAML"
                     /gene_synonym="AMICA; AMICA1; CREA7-1; CREA7-4; Gm638"
                     /coded_by="NM_001098526.2:92..1276"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41723.1"
                     /db_xref="GeneID:120425"
                     /db_xref="HGNC:HGNC:19084"
                     /db_xref="MIM:609770"
ORIGIN      
        1 mfcplklill pvlldyslgl ndlnvsppel tvhvgdsalm gcvfqstedk cifkidwtls
       61 pgehakdeyv lyyysnlsvp igrfqnrvhl mgdilcndgs lllqdvqead qgtyiceirl
      121 kgesqvfkka vvlhvlpeep kelmvhvggl iqmgcvfqst evkhvtkvew ifsgrrakee
      181 ivfryyhklr msveysqswg hfqnrvnlvg difrndgsim lqgvresdgg nytcsihlgn
      241 lvfkktivlh vspeeprtlv tpaalrplvl ggnqlviivg ivcatilllp vlilivkktc
      301 gnkssvnstv lvkntkktnp eikekpchfe rcegekhiys piivreviee eepsekseat
      361 ymtmhpvwps lrsdrnnsle kksgggmpkt qqaf
//
LOCUS       NP_001193469             277 aa            linear   PRI 20-NOV-2025
DEFINITION  F-actin-capping protein subunit beta isoform 2 [Homo sapiens].
ACCESSION   NP_001193469
VERSION     NP_001193469.1
DBSOURCE    REFSEQ: accession NM_001206540.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Carman,P.J., Barrie,K.R., Rebowski,G. and Dominguez,R.
  TITLE     Structures of the free and capped ends of the actin filament
  JOURNAL   Science 380 (6651), 1287-1292 (2023)
   PUBMED   37228182
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 277)
  AUTHORS   Wells,C.D., Fawcett,J.P., Traweger,A., Yamanaka,Y., Goudreault,M.,
            Elder,K., Kulkarni,S., Gish,G., Virag,C., Lim,C., Colwill,K.,
            Starostine,A., Metalnikov,P. and Pawson,T.
  TITLE     A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
            proteins in epithelial cells
  JOURNAL   Cell 125 (3), 535-548 (2006)
   PUBMED   16678097
REFERENCE   6  (residues 1 to 277)
  AUTHORS   Yang,C., Pring,M., Wear,M.A., Huang,M., Cooper,J.A., Svitkina,T.M.
            and Zigmond,S.H.
  TITLE     Mammalian CARMIL inhibits actin filament capping by capping protein
  JOURNAL   Dev Cell 9 (2), 209-221 (2005)
   PUBMED   16054028
REFERENCE   7  (residues 1 to 277)
  AUTHORS   Olavesen,M.G., Bentley,E., Mason,R.V., Stephens,R.J. and
            Ragoussis,J.
  TITLE     Fine mapping of 39 ESTs on human chromosome 6p23-p25
  JOURNAL   Genomics 46 (2), 303-306 (1997)
   PUBMED   9417921
REFERENCE   8  (residues 1 to 277)
  AUTHORS   Kuhlman,P.A. and Fowler,V.M.
  TITLE     Purification and characterization of an alpha 1 beta 2 isoform of
            CapZ from human erythrocytes: cytosolic location and inability to
            bind to Mg2+ ghosts suggest that erythrocyte actin filaments are
            capped by adducin
  JOURNAL   Biochemistry 36 (44), 13461-13472 (1997)
   PUBMED   9354614
REFERENCE   9  (residues 1 to 277)
  AUTHORS   Hart,M.C., Korshunova,Y.O. and Cooper,J.A.
  TITLE     Vertebrates have conserved capping protein alpha isoforms with
            specific expression patterns
  JOURNAL   Cell Motil Cytoskeleton 38 (2), 120-132 (1997)
   PUBMED   9331217
REFERENCE   10 (residues 1 to 277)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J Biol Chem 270 (37), 21472-21479 (1995)
   PUBMED   7665558
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY021163.1, CB267021.1,
            AI799520.1, BC008095.1 and BQ773230.1.
            
            Summary: This gene encodes the beta subunit of the barbed-end actin
            binding protein, which belongs to the F-actin capping protein
            family. The capping protein is a heterodimeric actin capping
            protein that blocks actin filament assembly and disassembly at the
            fast growing (barbed) filament ends and functions in regulating
            actin filament dynamics as well as in stabilizing actin filament
            lengths in muscle and nonmuscle cells. A pseudogene of this gene is
            located on the long arm of chromosome 2. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            found.[provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) has an additional exon in the
            3' region, and thus differs in the 3' coding region and 3' UTR,
            compared to variant 1. The resulting isoform (2) has a longer and
            distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1070889.1,
                                           SRR9304715.606479.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..277
                     /product="F-actin-capping protein subunit beta isoform 2"
                     /note="F-actin-capping protein subunit beta; capZ beta;
                     epididymis secretory sperm binding protein; capping
                     protein (actin filament) muscle Z-line, beta; capping
                     actin protein of muscle Z-line beta subunit"
                     /calculated_mol_wt=31219
     Region          11..239
                     /region_name="F_actin_cap_B"
                     /note="F-actin capping protein, beta subunit; pfam01115"
                     /db_xref="CDD:460070"
     CDS             1..277
                     /gene="CAPZB"
                     /gene_synonym="CAPB; CAPPB; CAPZ"
                     /coded_by="NM_001206540.3:102..935"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55579.1"
                     /db_xref="GeneID:832"
                     /db_xref="HGNC:HGNC:1491"
                     /db_xref="MIM:601572"
ORIGIN      
        1 msdqqldcal dlmrrlppqq ieknlsdlid lvpslcedll ssvdqplkia rdkvvgkdyl
       61 lcdynrdgds yrspwsnkyd ppledgamps arlrklevea nnafdqyrdl yfeggvssvy
      121 lwdldhgfag vilikkagdg skkikgcwds ihvvevqeks sgrtahyklt stvmlwlqtn
      181 ksgsgtmnlg gsltrqmekd etvsdcsphi anigrlvedm enkirstlne iyfgktkdiv
      241 nglrsidaip dnqkfkqlqr elsqvltqrq iyiqpdn
//
LOCUS       NP_001337608             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337608 XP_005250726
VERSION     NP_001337608.1
DBSOURCE    REFSEQ: accession NM_001350679.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 21, 2017 this sequence version replaced XP_005250726.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (16), as well as variants 1-4,
            9-15, and 17-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.34727.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350679.1:530..2740"
                     /note="isoform 1 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_002257                529 aa            linear   PRI 20-NOV-2025
DEFINITION  importin subunit alpha-1 [Homo sapiens].
ACCESSION   NP_002257 XP_001133253 XP_001133254 XP_001133256 XP_001133258
            XP_001133262 XP_001133265 XP_001133267 XP_001133271
VERSION     NP_002257.1
DBSOURCE    REFSEQ: accession NM_002266.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Lange,A., Mills,R.E., Lange,C.J., Stewart,M., Devine,S.E. and
            Corbett,A.H.
  TITLE     Classical nuclear localization signals: definition, function, and
            interaction with importin alpha
  JOURNAL   J Biol Chem 282 (8), 5101-5105 (2007)
   PUBMED   17170104
  REMARK    Review article
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Teng,S.C., Wu,K.J., Tseng,S.F., Wong,C.W. and Kao,L.
  TITLE     Importin KPNA2, NBS1, DNA repair and tumorigenesis
  JOURNAL   J Mol Histol 37 (5-7), 293-299 (2006)
   PUBMED   16752129
  REMARK    GeneRIF: This review focuses on recent experimental evidences
            demonstrating how NBS1 is translocated into the nucleus by an
            importin KPNA2 which mediates NBS1 subcellular localization and the
            functions of the NBS1 complex in tumorigenesis.
            Review article
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Dorr,S.N., Schlicker,M.N. and Hansmann,I.N.
  TITLE     Genomic structure of karyopherin alpha2 (KPNA2) within a low-copy
            repeat on chromosome 17q23-q24 and mutation analysis in patients
            with Russell-Silver syndrome
  JOURNAL   Hum Genet 109 (5), 479-486 (2001)
   PUBMED   11735022
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Herold,A., Truant,R., Wiegand,H. and Cullen,B.R.
  TITLE     Determination of the functional domain organization of the importin
            alpha nuclear import factor
  JOURNAL   J Cell Biol 143 (2), 309-318 (1998)
   PUBMED   9786944
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Weis,K., Ryder,U. and Lamond,A.I.
  TITLE     The conserved amino-terminal domain of hSRP1 alpha is essential for
            nuclear protein import
  JOURNAL   EMBO J 15 (8), 1818-1825 (1996)
   PUBMED   8617227
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Moroianu,J., Hijikata,M., Blobel,G. and Radu,A.
  TITLE     Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers:
            alpha 1 or alpha 2 subunit binds nuclear localization signal and
            beta subunit interacts with peptide repeat-containing nucleoporins
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6532-6536 (1995)
   PUBMED   7604027
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Weis,K., Mattaj,I.W. and Lamond,A.I.
  TITLE     Identification of hSRP1 alpha as a functional receptor for nuclear
            localization sequences
  JOURNAL   Science 268 (5213), 1049-1053 (1995)
   PUBMED   7754385
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Cuomo,C.A., Kirch,S.A., Gyuris,J., Brent,R. and Oettinger,M.A.
  TITLE     Rch1, a protein that specifically interacts with the RAG-1
            recombination-activating protein
  JOURNAL   Proc Natl Acad Sci U S A 91 (13), 6156-6160 (1994)
   PUBMED   8016130
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U28386.1, AK024833.1 and
            AA744568.1.
            
            On or before Jan 26, 2007 this sequence version replaced
            XP_001133254.1, XP_001133256.1, XP_001133258.1, XP_001133265.1,
            XP_001133267.1, XP_001133271.1, XP_001133253.1, XP_001133262.1.
            
            Summary: The import of proteins into the nucleus is a process that
            involves at least 2 steps. The first is an energy-independent
            docking of the protein to the nuclear envelope and the second is an
            energy-dependent translocation through the nuclear pore complex.
            Imported proteins require a nuclear localization sequence (NLS)
            which generally consists of a short region of basic amino acids or
            2 such regions spaced about 10 amino acids apart. Proteins involved
            in the first step of nuclear import have been identified in
            different systems. These include the Xenopus protein importin and
            its yeast homolog, SRP1 (a suppressor of certain
            temperature-sensitive mutations of RNA polymerase I in
            Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein
            interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and
            may be involved in the nuclear transport of proteins. KPNA2 also
            may play a role in V(D)J recombination. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053343.1, AK291954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330459.8/ ENSP00000332455.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..529
                     /product="importin subunit alpha-1"
                     /note="importin-alpha-P1; pendulin; importin subunit
                     alpha-2; RAG cohort protein 1; karyopherin alpha 2 (RAG
                     cohort 1, importin alpha 1); nuclear pore-targeting
                     complex 58kD component"
                     /calculated_mol_wt=57731
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          10..528
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          43..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          45..54
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P52292.1)"
     Region          71..111
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          112..151
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          115..147
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(138,142,146,180,184,188,227,231,235)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          142..238
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          155..191
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          197..236
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          200..244
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          246..282
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          253..278
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(269,273,277,311,315,319,353,357,361)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          283..322
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          286..322
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          315..403
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          328..362
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          367..409
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          370..404
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          410..456
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          413..447
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          457..496
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (P52292.1)"
     Region          460..495
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            490
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P52292.1)"
     CDS             1..529
                     /gene="KPNA2"
                     /gene_synonym="IPOA1; PTAC58; QIP2; RCH1; SRP1-alpha;
                     SRP1alpha"
                     /coded_by="NM_002266.4:130..1719"
                     /db_xref="CCDS:CCDS32713.1"
                     /db_xref="GeneID:3838"
                     /db_xref="HGNC:HGNC:6395"
                     /db_xref="MIM:600685"
ORIGIN      
        1 mstnenantp aarlhrfknk gkdstemrrr rievnvelrk akkddqmlkr rnvssfpdda
       61 tsplqenrnn qgtvnwsvdd ivkginssnv enqlqatqaa rkllsrekqp pidniiragl
      121 ipkfvsflgr tdcspiqfes awaltniasg tseqtkavvd ggaipafisl lasphahise
      181 qavwalgnia gdgsvfrdlv ikygavdpll allavpdmss lacgylrnlt wtlsnlcrnk
      241 npappidave qilptlvrll hhddpevlad tcwaisyltd gpnerigmvv ktgvvpqlvk
      301 llgaselpiv tpalraigni vtgtdeqtqv vidagalavf pslltnpktn iqkeatwtms
      361 nitagrqdqi qqvvnhglvp flvsvlskad fktqkeavwa vtnytsggtv eqivylvhcg
      421 iieplmnllt akdtkiilvi ldaisnifqa aeklgetekl simieecggl dkiealqnhe
      481 nesvykasls liekyfsvee eedqnvvpet tsegytfqvq dgapgtfnf
//
LOCUS       NP_001308749             542 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform n [Homo sapiens].
ACCESSION   NP_001308749
VERSION     NP_001308749.1
DBSOURCE    REFSEQ: accession NM_001321820.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.114512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..542
                     /product="E3 ubiquitin-protein ligase CBL-B isoform n"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=59083
     Region          <5..30
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          491..531
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(493..494,496..498,500..501,506,510)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..542
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321820.2:1612..3240"
                     /note="isoform n is encoded by transcript variant 20"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mkyskesdgq gcpfcrceik gtepiivdpf dprdegsrcc siidpfgmpm ldldddddre
       61 eslmmnrlan vrkctdrqns pvtspgsspl aqrrkpqpdp lqiphlslpp vpprldliqk
      121 givrspcgsp tgspksspcm vrkqdkplpa pppplrdppp ppperpppip pdnrlsrhih
      181 hvesvpsrdp pmpleawcpr dvfgtnqlvg crllgegspk pgitassnvn grhsrvgsdp
      241 vlmrkhrrhd lplegakvfs nghlgseeyd vpprlspppp vttllpsikc tgplanslse
      301 ktrdpveedd deykipsshp vslnsqpshc hnvkppvrsc dnghcmlngt hgpssekksn
      361 ipdlsiylkg edafdalpps lpppppparh sliehskppg sssrpssgqd lfllpsdpfv
      421 dlasgqvplp parrlpgenv ktnrtsqdyd qlpscsdgsq aparppkprp rrtapeihhr
      481 kphgpeaale nvdakiaklm gegyafeevk raleiaqnnv evarsilref afpppvsprl
      541 nl
//
LOCUS       NP_001356435             693 aa            linear   PRI 20-NOV-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 isoform a
            [Homo sapiens].
ACCESSION   NP_001356435 XP_016866080
VERSION     NP_001356435.1
DBSOURCE    REFSEQ: accession NM_001369506.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 693)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 693)
  AUTHORS   Zhang,J., Cao,L., Gao,A., Ren,R., Yu,L., Li,Q., Liu,Y., Qi,W.,
            Hou,Y., Sui,W., Su,G., Zhang,Y., Zhang,C. and Zhang,M.
  TITLE     E3 ligase RNF99 negatively regulates TLR-mediated inflammatory
            immune response via K48-linked ubiquitination of TAB2
  JOURNAL   Cell Death Differ 30 (4), 966-978 (2023)
   PUBMED   36681779
REFERENCE   3  (residues 1 to 693)
  AUTHORS   Koene,S., Klerx-Melis,F., Roest,A.A.W., Kleijwegt,M.C., Bootsma,M.,
            Haak,M.C., van Haeringen,M.H., Ruivenkamp,C.A.L., Nibbeling,E.A.R.
            and van Haeringen,A.
  TITLE     Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family
  JOURNAL   Am J Med Genet A 188 (12), 3510-3515 (2022)
   PUBMED   36000780
  REMARK    GeneRIF: Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family.
REFERENCE   4  (residues 1 to 693)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   5  (residues 1 to 693)
  AUTHORS   Liu,H., Zhang,H., Fan,H., Tang,S. and Weng,J.
  TITLE     TAB2 Promotes the Biological Functions of Head and Neck Squamous
            Cell Carcinoma Cells via EMT and PI3K Pathway
  JOURNAL   Dis Markers 2022, 1217918 (2022)
   PUBMED   35978886
  REMARK    GeneRIF: TAB2 Promotes the Biological Functions of Head and Neck
            Squamous Cell Carcinoma Cells via EMT and PI3K Pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 693)
  AUTHORS   Takaesu,G., Kishida,S., Hiyama,A., Yamaguchi,K., Shibuya,H.,
            Irie,K., Ninomiya-Tsuji,J. and Matsumoto,K.
  TITLE     TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK
            by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
  JOURNAL   Mol Cell 5 (4), 649-658 (2000)
   PUBMED   10882101
REFERENCE   7  (residues 1 to 693)
  AUTHORS   Mercurio,F., Zhu,H., Murray,B.W., Shevchenko,A., Bennett,B.L.,
            Li,J., Young,D.B., Barbosa,M., Mann,M., Manning,A. and Rao,A.
  TITLE     IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for
            NF-kappaB activation
  JOURNAL   Science 278 (5339), 860-866 (1997)
   PUBMED   9346484
REFERENCE   8  (residues 1 to 693)
  AUTHORS   Deacon,K. and Blank,J.L.
  TITLE     Characterization of the mitogen-activated protein kinase kinase 4
            (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated
            by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not
            cause activation of p38 kinase in vivo
  JOURNAL   J Biol Chem 272 (22), 14489-14496 (1997)
   PUBMED   9162092
REFERENCE   9  (residues 1 to 693)
  AUTHORS   Shibuya,H., Yamaguchi,K., Shirakabe,K., Tonegawa,A., Gotoh,Y.,
            Ueno,N., Irie,K., Nishida,E. and Matsumoto,K.
  TITLE     TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
            transduction
  JOURNAL   Science 272 (5265), 1179-1182 (1996)
   PUBMED   8638164
REFERENCE   10 (residues 1 to 693)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL138727.10, AL139103.13 and
            AL031133.1.
            
            On Apr 10, 2019 this sequence version replaced XP_016866080.1.
            
            Summary: The protein encoded by this gene is an activator of
            MAP3K7/TAK1, which is required for for the IL-1 induced activation
            of nuclear factor kappaB and MAPK8/JNK. This protein forms a kinase
            complex with TRAF6, MAP3K7 and TAB1, and it thus serves as an
            adaptor that links MAP3K7 and TRAF6. This protein, along with TAB1
            and MAP3K7, also participates in the signal transduction induced by
            TNFSF11/RANKl through the activation of the receptor activator of
            NF-kappaB (TNFRSF11A/RANK), which may regulate the development and
            function of osteoclasts. Studies of the related mouse protein
            indicate that it functions to protect against liver damage caused
            by chemical stressors. Mutations in this gene cause congenital
            heart defects, multiple types, 2 (CHTD2). Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.261143.1,
                                           SRR1660809.11138.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..693
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.1"
     Protein         1..693
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 2 isoform a"
                     /note="TAK1-binding protein 2; mitogen-activated protein
                     kinase kinase kinase 7-interacting protein 2"
                     /calculated_mol_wt=76363
     Region          9..50
                     /region_name="CUE_TAB2_TAB3"
                     /note="CUE domain found in the N-terminal of
                     TGF-beta-activated kinase 1 and MAP3K7-binding proteins
                     TAB2, TAB3 and similar proteins; cd14362"
                     /db_xref="CDD:270545"
     Region          91..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            173
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          219..310
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          330..381
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          540..>619
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          642..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          667..690
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          668..687
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     Site            673
                     /site_type="methylation"
                     /note="(Microbial infection) S-methylcysteine.
                     /evidence=ECO:0000269|PubMed:22158122,
                     ECO:0000269|PubMed:25412445; propagated from
                     UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     Region          675..685
                     /region_name="Interaction with polyubiquitin.
                     /evidence=ECO:0000269|PubMed:19935683"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYJ8.1)"
     CDS             1..693
                     /gene="TAB2"
                     /gene_synonym="CHTD2; MAP3K7IP2; TAB-2"
                     /coded_by="NM_001369506.1:543..2624"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS5214.1"
                     /db_xref="GeneID:23118"
                     /db_xref="HGNC:HGNC:17075"
                     /db_xref="MIM:605101"
ORIGIN      
        1 maqgshqidf qvlhdlrqkf pevpevvvsr cmlqnnnnld accavlsqes trylygegdl
       61 nfsddsgisg lrnhmtslnl dlqsqniyhh gregsrmngs rtlthsisdg qlqggqsnse
      121 lfqqepqtap aqvpqgfnvf gmssssgasn saphlgfhlg skgtsslsqq tprfnpimvt
      181 lapniqtgrn tptslhihgv pppvlnspqg nsiyirpyit tpggttrqtq qhsgwvsqfn
      241 pmnpqqvyqp sqpgpwttcp asnplshtss qqpnqqghqt shvympissp ttsqpptihs
      301 sgssqssahs qyniqnistg prknqieikl eppqrnnssk lrssgprtss tsssvnsqtl
      361 nrnqptvyia asppntdelm srsqpkvyis anaatgdeqv mrnqptlfis tnsgasaasr
      421 nmsgqvsmgp afihhhppks raignnsats prvvvtqpnt kytfkitvsp nkppavspgv
      481 vsptfeltnl lnhpdhyvet eniqhltdpt lahvdriset rklsmgsdda aytqallvhq
      541 karmerlqre leiqkkkldk lksevnemen nltrrrlkrs nsisqipsle emqqlrscnr
      601 qlqididclt keidlfqarg phfnpsaihn fydnigfvgp vppkpkdqrs iiktpktqdt
      661 eddegaqwnc tactflnhpa lirceqcemp rhf
//
LOCUS       NP_036308                387 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_036308
VERSION     NP_036308.1
DBSOURCE    REFSEQ: accession NM_012176.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 387)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 387)
  AUTHORS   Kang,J.Y., Wen,Z., Pan,D., Zhang,Y., Li,Q., Zhong,A., Yu,X.,
            Wu,Y.C., Chen,Y., Zhang,X., Kou,P.C., Geng,J., Wang,Y.Y., Hua,M.M.,
            Zong,R., Li,B., Shi,H.J., Li,D., Fu,X.D., Li,J., Nelson,D.L.,
            Guo,X., Zhou,Y., Gou,L.T., Huang,Y. and Liu,M.F.
  TITLE     LLPS of FXR1 drives spermiogenesis by activating translation of
            stored mRNAs
  JOURNAL   Science 377 (6607), eabj6647 (2022)
   PUBMED   35951695
REFERENCE   3  (residues 1 to 387)
  AUTHORS   George,J., Li,Y., Kadamberi,I.P., Parashar,D., Tsaih,S.W.,
            Gupta,P., Geethadevi,A., Chen,C., Ghosh,C., Sun,Y., Mittal,S.,
            Ramchandran,R., Rui,H., Lopez-Berestein,G., Rodriguez-Aguayo,C.,
            Leone,G., Rader,J.S., Sood,A.K., Dey,M., Pradeep,S. and
            Chaluvally-Raghavan,P.
  TITLE     RNA-binding protein FXR1 drives cMYC translation by recruiting
            eIF4F complex to the translation start site
  JOURNAL   Cell Rep 37 (5), 109934 (2021)
   PUBMED   34731628
  REMARK    Erratum:[Cell Rep. 2023 Mar 28;42(3):112228. doi:
            10.1016/j.celrep.2023.112228. PMID: 36884347]
REFERENCE   4  (residues 1 to 387)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 387)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 387)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   7  (residues 1 to 387)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 387)
  AUTHORS   Chiaur,D.S., Murthy,S., Cenciarelli,C., Parks,W., Loda,M.,
            Inghirami,G., Demetrick,D. and Pagano,M.
  TITLE     Five human genes encoding F-box proteins: chromosome mapping and
            analysis in human tumors
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 255-258 (2000)
   PUBMED   10828603
REFERENCE   9  (residues 1 to 387)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 387)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK024075.1, BC040011.1,
            BC048098.1 and AC034222.5.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.123476.1, AK024075.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281623.8/ ENSP00000281623.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..387
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..387
                     /product="F-box only protein 4 isoform 1"
                     /note="F-box protein Fbx4; F-box only protein 4"
                     /calculated_mol_wt=44005
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18598945,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKT5.2)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKT5.2)"
     Region          57..106
                     /region_name="F-box_FBXO4"
                     /note="F-box domain found in F-box only protein 4 (FBXO4)
                     and similar proteins; cd22085"
                     /db_xref="CDD:438857"
     Site            order(57..60,62,65..66,69..70,73..74,76,78,80..87,89..90,
                     94)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438857"
     Region          162..384
                     /region_name="FBX4_GTPase_like"
                     /note="C-terminal GTPase-like domain of F-Box Only Protein
                     4; cd11656"
                     /db_xref="CDD:212555"
     Site            order(165,171)
                     /site_type="other"
                     /note="SKP1 binding interface [polypeptide binding]"
                     /db_xref="CDD:212555"
     Site            order(340,342..343,345,356..357,359,361)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:212555"
     Site            order(341..342,345..346,357..361,372)
                     /site_type="other"
                     /note="TRF1 binding interface [polypeptide binding]"
                     /db_xref="CDD:212555"
     CDS             1..387
                     /gene="FBXO4"
                     /gene_synonym="FBX4"
                     /coded_by="NM_012176.3:30..1193"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3938.1"
                     /db_xref="GeneID:26272"
                     /db_xref="HGNC:HGNC:13583"
                     /db_xref="MIM:609090"
ORIGIN      
        1 magseprsgt nsppppfsdw grleaailsg wktfwqsvsk ervarttsre evdeaastlt
       61 rlpidvqlyi lsflsphdlc qlgstnhywn etvrdpilwr yfllrdlpsw ssvdwkslpd
      121 leilkkpise vtdgaffdym avyrmccpyt rraskssrpm ygavtsflhs liiqneprfa
      181 mfgpgleeln tslvlslmss eelcptaglp qrqidgigsg vnfqlnnqhk fnililystt
      241 rkerdraree htsavnkmfs rhnegddqqg srysvipqiq kvcevvdgfi yvanaeahkr
      301 hewqdefshi mamtdpafgs sgrpllvlsc isqgdvkrmp cfylahelhl nllnhpwlvq
      361 dteaetltgf lngiewilee veskrar
//
LOCUS       NP_060323                149 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin-like protein 4B isoform 1 [Homo sapiens].
ACCESSION   NP_060323
VERSION     NP_060323.1
DBSOURCE    REFSEQ: accession NM_017853.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 149)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   2  (residues 1 to 149)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 149)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 149)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 149)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 149)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 149)
  AUTHORS   Simeoni,F., Arvai,A., Bello,P., Gondeau,C., Hopfner,K.P.,
            Neyroz,P., Heitz,F., Tainer,J. and Divita,G.
  TITLE     Biochemical characterization and crystal structure of a Dim1 family
            associated protein: Dim2
  JOURNAL   Biochemistry 44 (36), 11997-12008 (2005)
   PUBMED   16142897
  REMARK    GeneRIF: crystal structure; in contrast to hDim1, hDim2 forms
            stable homodimers
REFERENCE   8  (residues 1 to 149)
  AUTHORS   Schelling,P., Claus,M.T., Johner,R., Marquez,V.E., Schulz,G.E. and
            Scapozza,L.
  TITLE     Biochemical and structural characterization of
            (South)-methanocarbathymidine that specifically inhibits growth of
            herpes simplex virus type 1 thymidine kinase-transduced
            osteosarcoma cells
  JOURNAL   J Biol Chem 279 (31), 32832-32838 (2004)
   PUBMED   15163659
REFERENCE   9  (residues 1 to 149)
  AUTHORS   Sun,X., Zhang,H., Wang,D., Ma,D., Shen,Y. and Shang,Y.
  TITLE     DLP, a novel Dim1 family protein implicated in pre-mRNA splicing
            and cell cycle progression
  JOURNAL   J Biol Chem 279 (31), 32839-32847 (2004)
   PUBMED   15161931
  REMARK    GeneRIF: DLP is implicated in not only cell cycle progression but
            also in a more specific molecular process such as pre-mRNA splicing
REFERENCE   10 (residues 1 to 149)
  AUTHORS   Zhang,Y.Z., Gould,K.L., Dunbrack,R.L. Jr., Cheng,H., Roder,H. and
            Golemis,E.A.
  TITLE     The evolutionarily conserved Dim1 protein defines a novel branch of
            the thioredoxin fold superfamily
  JOURNAL   Physiol Genomics 1 (3), 109-118 (1999)
   PUBMED   11015569
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP355646.1, BC009646.1 and AC009087.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000518.1, SRR3476690.964036.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268483.8/ ENSP00000268483.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..149
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.2"
     Protein         1..149
                     /product="thioredoxin-like protein 4B isoform 1"
                     /note="Dim1-like protein; thioredoxin-like protein 4B"
                     /calculated_mol_wt=16884
     Region          10..123
                     /region_name="DLP"
                     /note="Dim1 family, Dim1-like protein (DLP) subfamily; DLP
                     is a novel protein which shares 38% sequence identity to
                     Dim1. Like Dim1, it is also implicated in pre-mRNA
                     splicing and cell cycle progression. DLP is located in the
                     nucleus and has been shown to...; cd02986"
                     /db_xref="CDD:239284"
     Site            order(21,23..24,86..88)
                     /site_type="active"
                     /note="first critical site [active]"
                     /db_xref="CDD:239284"
     Site            40..43
                     /site_type="active"
                     /note="second critical site [active]"
                     /db_xref="CDD:239284"
     CDS             1..149
                     /gene="TXNL4B"
                     /gene_synonym="Dim2; DLP"
                     /coded_by="NM_017853.3:292..741"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10906.1"
                     /db_xref="GeneID:54957"
                     /db_xref="HGNC:HGNC:26041"
                     /db_xref="MIM:617722"
ORIGIN      
        1 msfllpklts kkevdqaiks taekvlvlrf grdedpvclq lddilsktss dlskmaaiyl
       61 vdvdqtavyt qyfdisyips tvfffngqhm kvdygspdht kfvgsfktkq dfidlieviy
      121 rgamrgkliv qspidpknip kydllyqdi
//
LOCUS       NP_001354397            1298 aa            linear   PRI 20-NOV-2025
DEFINITION  activating molecule in BECN1-regulated autophagy protein 1 isoform
            5 [Homo sapiens].
ACCESSION   NP_001354397
VERSION     NP_001354397.1
DBSOURCE    REFSEQ: accession NM_001367468.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Gottlieb,S., Shang,W., Ye,D., Kubo,S., Jiang,P.D., Shafer,S.,
            Xu,L., Zheng,L., Park,A.Y., Song,J., Chan,W., Zeng,Z., He,T.,
            Schwarz,B., Haupl,B., Oellerich,T., Lenardo,M.J. and Yao,Y.
  TITLE     AMBRA1 controls the translation of immune-specific genes in T
            lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2416722121 (2024)
   PUBMED   39436665
  REMARK    GeneRIF: AMBRA1 controls the translation of immune-specific genes
            in T lymphocytes.
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Sankar,D.S., Kaeser-Pebernard,S., Vionnet,C., Favre,S., de Oliveira
            Marchioro,L., Pillet,B., Zhou,J., Stumpe,M., Kovacs,W.J.,
            Kressler,D., Antonioli,M., Fimia,G.M. and Dengjel,J.
  TITLE     The ULK1 effector BAG2 regulates autophagy initiation by modulating
            AMBRA1 localization
  JOURNAL   Cell Rep 43 (9), 114689 (2024)
   PUBMED   39207901
  REMARK    GeneRIF: The ULK1 effector BAG2 regulates autophagy initiation by
            modulating AMBRA1 localization.
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Di Leo,L., Pagliuca,C., Kishk,A., Rizza,S., Tsiavou,C.,
            Pecorari,C., Dahl,C., Pacheco,M.P., Tholstrup,R., Brewer,J.R.,
            Berico,P., Hernando,E., Cecconi,F., Ballotti,R., Bertolotto,C.,
            Filomeni,G., Gjerstorff,M.F., Sauter,T., Lovat,P., Guldberg,P. and
            De Zio,D.
  TITLE     AMBRA1 levels predict resistance to MAPK inhibitors in melanoma
  JOURNAL   Proc Natl Acad Sci U S A 121 (25), e2400566121 (2024)
   PUBMED   38870061
  REMARK    GeneRIF: AMBRA1 levels predict resistance to MAPK inhibitors in
            melanoma.
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Qu,X., Li,X.Y., Feng,Y., Wang,X., Li,L., Wang,Y.P. and Chu,Y.L.
  TITLE     sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to reduce
            autophagy in gestational diabetes
  JOURNAL   Endokrynol Pol 75 (1), 61-70 (2024)
   PUBMED   38497391
  REMARK    GeneRIF: sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to
            reduce autophagy in gestational diabetes.
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Cecconi,F., Di Bartolomeo,S., Nardacci,R., Fuoco,C., Corazzari,M.,
            Giunta,L., Romagnoli,A., Stoykova,A., Chowdhury,K., Fimia,G.M. and
            Piacentini,M.
  TITLE     A novel role for autophagy in neurodevelopment
  JOURNAL   Autophagy 3 (5), 506-508 (2007)
   PUBMED   17622796
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Le Bot,N.
  TITLE     Autophagy: a new regulator of development
  JOURNAL   Nat Cell Biol 9 (7), 741 (2007)
   PUBMED   17603510
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Fimia,G.M., Stoykova,A., Romagnoli,A., Giunta,L., Di Bartolomeo,S.,
            Nardacci,R., Corazzari,M., Fuoco,C., Ucar,A., Schwartz,P.,
            Gruss,P., Piacentini,M., Chowdhury,K. and Cecconi,F.
  TITLE     Ambra1 regulates autophagy and development of the nervous system
  JOURNAL   Nature 447 (7148), 1121-1125 (2007)
   PUBMED   17589504
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Meyerson,M. and Harlow,E.
  TITLE     Identification of G1 kinase activity for cdk6, a novel cyclin D
            partner
  JOURNAL   Mol Cell Biol 14 (3), 2077-2086 (1994)
   PUBMED   8114739
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK302808.1, AC127035.6 and AC116021.5.
            
            Transcript Variant: This variant (5), as well as variant 10,
            encodes isoform 5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302808.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..1298
                     /product="activating molecule in BECN1-regulated autophagy
                     protein 1 isoform 5"
                     /note="WD repeat domain 94; DDB1 and CUL4 associated
                     factor 3; activating molecule in BECN1-regulated autophagy
                     protein 1; activating molecule in beclin-1-regulated
                     autophagy; autophagy/beclin-1 regulator 1"
                     /calculated_mol_wt=142377
     Region          1..22
                     /region_name="Interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:30166453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          51..90
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:23524951; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          56..92
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <59..198
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          93..133
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          99..135
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          135..175
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          140..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          254..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          275..281
                     /region_name="PxP motif 1.
                     /evidence=ECO:0000269|PubMed:25438055,
                     ECO:0000269|PubMed:30513302"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          343..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            443
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          458..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            482..483
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-6, caspase-7 and caspase-8.
                     /evidence=ECO:0000269|PubMed:22441670; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          538..561
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          590..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          747..796
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            747
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2AH22; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1043..1052
                     /region_name="LIR. /evidence=ECO:0000269|PubMed:25215947"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            1043
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000269|PubMed:30217973; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1060..1079
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1104..1106
                     /region_name="TQT motif 1.
                     /evidence=ECO:0000269|PubMed:20921139"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1112..1143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1116..1118
                     /region_name="TQT motif 2.
                     /evidence=ECO:0000269|PubMed:20921139"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1190..1214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            1205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1206..1212
                     /region_name="PxP motif 2.
                     /evidence=ECO:0000269|PubMed:25438055,
                     ECO:0000269|PubMed:30513302"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          1227..1298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     CDS             1..1298
                     /gene="AMBRA1"
                     /gene_synonym="DCAF3; WDR94"
                     /coded_by="NM_001367468.1:361..4257"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91466.1"
                     /db_xref="GeneID:55626"
                     /db_xref="HGNC:HGNC:25990"
                     /db_xref="MIM:611359"
ORIGIN      
        1 mkvvpeknav rilwgrerga ramgaqrllq elvedktrwm kwegkrvelp dsprstflla
       61 fspdrtllas thvnhniyit evktgkcvhs lighrrtpwc vtfhptisgl iasgcldgev
      121 riwdlhggse swftdsnnai aslafhptaq llliatanei hfwdwsrrep favvktasem
      181 ervrlvrfdp lghylltaiv npsnqqgdde peipidgtel shyrqrallq sqpvrrtpll
      241 hnflhmlssr ssgiqvgeqs tvqdsatpsp pppppqpste rprtsayirl rqrvsyptae
      301 ccqhlgilcl csrcsgtrvp sllphqdsvp pasarattps fsfvqtepfh ppeqasstqq
      361 dqgllnrpsa fstvqsstag ntlrnlslgp trrslggpls shpsryhrei apgltgsewt
      421 rtvlslnsrs eaesmppprt sassvsllsv lrqqeggsqa svytsategr gfpasglate
      481 sdggngssqn nsgsirhelq cdlrrffley drlqeldqsl sgeapqtqqa qemlnnnies
      541 erpgpshqpt phssennsnl srghlnrcra chnlltfnnd tlrwerttpn yssgeasssw
      601 qvpssfesvp ssgsqlpple rtegqtpsss rlelsssasp qeertvgvaf nqetghweri
      661 ytqssrsgtv sqealhqdmp eesseedslr rrllesslis lsrydgagsr ehpiypdpar
      721 lspaayyaqr miqylsrrds irqrsmryqq nrlrsstsss ssdnqgpsve gtdlefedfe
      781 dngdrsrhra prnarmsaps lgrfvprrfl lpeylpyagi fhergqpgla thssvnrvla
      841 gavigdgqsa vasniantty rlqwwdftkf dlpeisnasv nvlvqnckiy ndascdisad
      901 gqllaafips sqrgfpdegi lavyslaphn lgemlytkrf gpnaisvsls pmgryvmvgl
      961 asrrillhps tehmvaqvfr lqqahggets mrrvfnvlyp mpadqrrhvs insarwlpep
     1021 glglaygtnk gdlvicrpea lnsgveyywd qlnetvftvh snsrsserpg tsratwrtdr
     1081 dmglmnaigl qprnpatsvt sqgtqtlalq lqnaetqter evpepgtaas gpgegegsey
     1141 gasgedalsr iqrlmaeggm tavvqreqst tmasmggfgn niivshrihr ssqtgtepga
     1201 ahtsspqpst srgllpeagq laerglsprt aswdqpgtpg reptqptlps sspvpipvsl
     1261 psaegptlhc eltnnnhlld ggssrgdaag prgeprnr
//
LOCUS       NP_001334969             846 aa            linear   PRI 20-NOV-2025
DEFINITION  protein PTHB1 isoform 8 [Homo sapiens].
ACCESSION   NP_001334969
VERSION     NP_001334969.1
DBSOURCE    REFSEQ: accession NM_001348040.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Zhang,Y., Xu,M., Zhang,M., Yang,G. and Li,X.
  TITLE     A Novel BBS9 Mutation Identified via Whole-Exome Sequencing in a
            Chinese Family with Bardet-Biedl Syndrome
  JOURNAL   Biomed Res Int 2021, 4514967 (2021)
   PUBMED   34692830
  REMARK    GeneRIF: A Novel BBS9 Mutation Identified via Whole-Exome
            Sequencing in a Chinese Family with Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Jeziorny,K., Antosik,K., Jakiel,P., Mlynarski,W., Borowiec,M. and
            Zmyslowska,A.
  TITLE     Next-Generation Sequencing in the Diagnosis of Patients with
            Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance
  JOURNAL   Genes (Basel) 11 (11), 1283 (2020)
   PUBMED   33138063
  REMARK    GeneRIF: Next-Generation Sequencing in the Diagnosis of Patients
            with Bardet-Biedl Syndrome-New Variants and Relationship with
            Hyperglycemia and Insulin Resistance.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 846)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 846)
  AUTHORS   Nishimura,D.Y., Swiderski,R.E., Searby,C.C., Berg,E.M.,
            Ferguson,A.L., Hennekam,R., Merin,S., Weleber,R.G., Biesecker,L.G.,
            Stone,E.M. and Sheffield,V.C.
  TITLE     Comparative genomics and gene expression analysis identifies BBS9,
            a new Bardet-Biedl syndrome gene
  JOURNAL   Am J Hum Genet 77 (6), 1021-1033 (2005)
   PUBMED   16380913
  REMARK    GeneRIF: Comparative genomics and gene expression analysis
            identifies PHTB1 protein as BBS9, a new Bardet-Biedl syndrome gene.
REFERENCE   7  (residues 1 to 846)
  AUTHORS   Vernon,E.G., Malik,K., Reynolds,P., Powlesland,R., Dallosso,A.R.,
            Jackson,S., Henthorn,K., Green,E.D. and Brown,K.W.
  TITLE     The parathyroid hormone-responsive B1 gene is interrupted by a
            t(1;7)(q42;p15) breakpoint associated with Wilms' tumour
  JOURNAL   Oncogene 22 (9), 1371-1380 (2003)
   PUBMED   12618763
  REMARK    GeneRIF: gene is interrupted by a t(1;7)(q42;p15) breakpoint
            associated with Wilms' tumour; new alternately spliced isoforms
            were found in a wide range of adult and foetal tissues
REFERENCE   8  (residues 1 to 846)
  AUTHORS   Adams,A.E., Rosenblatt,M. and Suva,L.J.
  TITLE     Identification of a novel parathyroid hormone-responsive gene in
            human osteoblastic cells
  JOURNAL   Bone 24 (4), 305-313 (1999)
   PUBMED   10221542
REFERENCE   9  (residues 1 to 846)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 846)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074338.1, AC007312.1,
            AC087070.2, AC006195.1 and AC078833.5.
            
            Summary: This gene is downregulated by parathyroid hormone in
            osteoblastic cells, and therefore is thought to be involved in
            parathyroid hormone action in bones. The exact function of this
            gene has not yet been determined. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Jan 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.151851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..846
                     /product="protein PTHB1 isoform 8"
                     /note="protein PTHB1; PTH-responsive osteosarcoma B1
                     protein; bardet-Biedl syndrome 9 protein; parathyroid
                     hormone-responsive B1 gene protein"
                     /calculated_mol_wt=94549
     Region          1..418
                     /region_name="PHTB1_N"
                     /note="PTHB1 N-terminus; pfam14727"
                     /db_xref="CDD:464284"
     Region          441..779
                     /region_name="PHTB1_C"
                     /note="PTHB1 C-terminus; pfam14728"
                     /db_xref="CDD:464285"
     CDS             1..846
                     /gene="BBS9"
                     /gene_synonym="B1; C18; D1; PTHB1"
                     /coded_by="NM_001348040.3:490..3030"
                     /note="isoform 8 is encoded by transcript variant 9"
                     /db_xref="GeneID:27241"
                     /db_xref="HGNC:HGNC:30000"
                     /db_xref="MIM:607968"
ORIGIN      
        1 mslfkardww stilgdkeef dqgclclanv dnsgngqdki ivgsfmgylr ifsphpaktg
       61 dgaqaedlll evdlrdpvlq vevgkfvsgt emlhlavlhs rklcvysvsg tlgnvehgnq
      121 cqmklmyehn lqrtacnmty gsfggvkgrd liciqsmdgm lmvfeqesya fgrflpgfll
      181 pgplayssrt dsfltvsscq qvesykyqvl afatdadkrq eteqqklgsg krlvvdwtln
      241 igeqaldici vsfnqsassv fvlgernffc lkdngqirfm kkldwspscf lpycsvsegt
      301 intlignhnn mlhiyqdvtl kwatqlphip vavrvgclhd lkgvivtlsd dghlqcsylg
      361 tdpslfqapn vqsrelnyde ldvemkelqk iikdvnksqg vwpmteredd lnvsvvvspn
      421 fdsvsqatdv evgtdlvpsv tvkvtlqnrv ilqkaklsvy vqppleltcd qftfefmsip
      481 rviqckfrlp lkliclpgqp sktashkiti dtnkspvsll slfpgfasqs dddqvnvmgf
      541 hflggaritv lasktsqryr iqseqfedlw litnelilrl qeyfekqgvk dfacsfsgsi
      601 plqeyfelid hhfelringe kleellsera vqfraiqrrl larfkdktpa plqhldtlld
      661 gtykqviala daveenqgnl fqsftrlksa thlvillial wqklsadqva ileaaflplq
      721 edtqelgwee tvdaaishll ktclsksske qalnlnsqln ipkdtsqlkk hitllcdrls
      781 kggrlclstd aaapqtmvmp ggcttipesd leersveqds telftnhrhl taetprpvsp
      841 lqgvse
//
LOCUS       NP_001356028             339 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001356028
VERSION     NP_001356028.1
DBSOURCE    REFSEQ: accession NM_001369099.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.94937.1,
                                           SRR1803614.134664.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..339
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 8"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=39130
     Region          81..146
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(90,92..94,96..100,103..104,107..108,113..116)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          155..338
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..339
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369099.1:282..1301"
                     /note="isoform 8 is encoded by transcript variant 20"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mmkypgtwpc qgiigisfge svmevlrpql iridgrnyrk npvqeqtyqh eedeedfyqg
       61 smecadepcd ayeveqtpqg frstlrapsl lykhivgkrg dtrkkiemet ktsisipkpg
      121 qdgeivitgq hrngvisart ridvlldtfr rkqpfthfla fflnevevqe gflrfqeevl
      181 akcsmdhgvd ssifqnpkkl hltigmlvll seeeiqqtce mlqqckeefi klqelvdrvl
      241 erfqasgliv kewnsvklha tvmntlfrkd pnaegrynly taegkyifke resfdgrnil
      301 klfenfyfgs lklnsihisq rftvdsfgny ascgqidfs
//
LOCUS       NP_001317534             541 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform p [Homo sapiens].
ACCESSION   NP_001317534 XP_005266811
VERSION     NP_001317534.1
DBSOURCE    REFSEQ: accession NM_001330605.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 541)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 541)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 541)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 541)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 541)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 541)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 541)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 541)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 541)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 541)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013587.10 and AC091103.4.
            
            On Aug 30, 2016 this sequence version replaced XP_005266811.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (16) differs in the 5' UTR, lacks
            a portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 3. The resulting
            isoform (p) is shorter at the N-terminus compared to isoform c.
            Variants 16 and 19 encode the same isoform (p).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.273245.1,
                                           SRR1803615.265362.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..541
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..541
                     /product="transcription factor 4 isoform p"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=57781
     Region          432..516
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(440,444,446..448,450,455,476..477)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(453..454,457..458,460..461,464,468,478,481,485,488,
                     491..496)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..541
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001330605.3:131..1756"
                     /note="isoform p is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS82255.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg ypsskpatst fpssffmqdg hhssdpwsss sgmnqpgyag mlgnsshipq
      121 sssycslhph erlsypshss adinsslppm stfhrsgtnh ystssctppa ngtdsimanr
      181 gsgaagssqt gdalgkalas iyspdhtnns fssnpstpvg sppslsagta vwsrnggqas
      241 sspnyegplh slqsriedrl erlddaihvl rnhavgpsta mpgghgdmhg iigpshngam
      301 gglgsgygtg llsanrhslm vgthredgva lrgshsllpn qvpvpqlpvq satspdlnpp
      361 qdpyrgmppg lqgqsvssgs seiksddegd enlqdtksse dkkldddkkd iksitrsrss
      421 nnddedltpe qkaerekerr mannarerlr vrdineafke lgrmvqlhlk sdkpqtklli
      481 lhqavavils leqqvrernl npkaaclkrr eeekvssepp plslagphpg mgdasnhmgq
      541 m
//
LOCUS       NP_671717                403 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 22 isoform a [Homo sapiens].
ACCESSION   NP_671717
VERSION     NP_671717.1
DBSOURCE    REFSEQ: accession NM_147188.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Zhou,Y., Feng,W., Yang,C., Wei,X., Fan,L., Wu,Y., Gao,X., Shen,X.,
            Zhang,Z. and Zhao,J.
  TITLE     E3 ubiquitin ligase FBXO22 inhibits SARS-CoV-2 replication via
            promoting proteasome-dependent degradation of NSP5
  JOURNAL   J Med Virol 96 (9), e29891 (2024)
   PUBMED   39223933
  REMARK    GeneRIF: E3 ubiquitin ligase FBXO22 inhibits SARS-CoV-2 replication
            via promoting proteasome-dependent degradation of NSP5.
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Liu,L., Matsumoto,M., Watanabe-Matsui,M., Nakagawa,T., Nagasawa,Y.,
            Pang,J., Callens,B.K.K., Muto,A., Ochiai,K., Takekawa,H., Alam,M.,
            Nishizawa,H., Shirouzu,M., Shima,H., Nakayama,K. and Igarashi,K.
  TITLE     TANK Binding Kinase 1 Promotes BACH1 Degradation through Both
            Phosphorylation-Dependent and -Independent Mechanisms without
            Relying on Heme and FBXO22
  JOURNAL   Int J Mol Sci 25 (8), 4141 (2024)
   PUBMED   38673728
  REMARK    GeneRIF: TANK Binding Kinase 1 Promotes BACH1 Degradation through
            Both Phosphorylation-Dependent and -Independent Mechanisms without
            Relying on Heme and FBXO22.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Gao,F., Wang,C., Bai,X., Ji,J. and Huang,X.
  TITLE     ELK4 Promotes Cell Cycle Progression and Stem Cell-like
            Characteristics in HPV-associated Cervical Cancer by Regulating the
            FBXO22/PTEN Axis
  JOURNAL   Balkan Med J 40 (6), 409-414 (2023)
   PUBMED   37519006
  REMARK    GeneRIF: ELK4 Promotes Cell Cycle Progression and Stem Cell-like
            Characteristics in HPV-associated Cervical Cancer by Regulating the
            FBXO22/PTEN Axis.
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Li,S., Shi,L., Wang,Y., Zhang,L., Chu,S., Li,M., Bai,J. and Zhu,W.
  TITLE     FBXO22 inhibits proliferation and metastasis of cervical cancer
            cells by mediating ubiquitination-dependent degradation of GAK
  JOURNAL   Exp Cell Res 430 (1), 113719 (2023)
   PUBMED   37442264
  REMARK    GeneRIF: FBXO22 inhibits proliferation and metastasis of cervical
            cancer cells by mediating ubiquitination-dependent degradation of
            GAK.
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Vrba,L., Junk,D.J., Novak,P. and Futscher,B.W.
  TITLE     p53 induces distinct epigenetic states at its direct target
            promoters
  JOURNAL   BMC Genomics 9, 486 (2008)
   PUBMED   18922183
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Borziak,K. and Zhulin,I.B.
  TITLE     FIST: a sensory domain for diverse signal transduction pathways in
            prokaryotes and ubiquitin signaling in eukaryotes
  JOURNAL   Bioinformatics 23 (19), 2518-2521 (2007)
   PUBMED   17855421
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC020204.1, AC027104.6 and
            AW292124.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class and, as a transcriptional target of the
            tumor protein p53, is thought to be involved in degradation of
            specific proteins in response to p53 induction. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.206369.1,
                                           SRR1803615.239091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308275.8/ ENSP00000307833.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..403
                     /product="F-box only protein 22 isoform a"
                     /note="FIST domain containing 1; F-box only protein 22;
                     F-box protein FBX22p44"
                     /calculated_mol_wt=44377
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q8NEZ5.1)"
     Region          23..70
                     /region_name="F-box_FBXO22"
                     /note="F-box domain found in F-box only protein 22
                     (FBXO22) and similar proteins; cd22097"
                     /db_xref="CDD:438869"
     Site            order(26,29,32..33,36..37,41,43..44,48..50,52)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438869"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:37979583; propagated from
                     UniProtKB/Swiss-Prot (Q8NEZ5.1)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEZ5.1)"
     Site            194
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8NEZ5.1)"
     Region          <298..396
                     /region_name="FIST"
                     /note="Small ligand-binding sensory domain FIST [Signal
                     transduction mechanisms]; COG4398"
                     /db_xref="CDD:443524"
     CDS             1..403
                     /gene="FBXO22"
                     /gene_synonym="FBX22; FISTC1; TYMAS"
                     /coded_by="NM_147188.3:87..1298"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10287.1"
                     /db_xref="GeneID:26263"
                     /db_xref="HGNC:HGNC:13593"
                     /db_xref="MIM:609096"
ORIGIN      
        1 mepvgccgec rgssvdprst fvlsnlaevv ervltflpak allrvacvcr lwrecvrrvl
       61 rthrsvtwis aglaeaghle ghclvrvvae elenvrilph tvlymadset fisleecrgh
      121 krarkrtsme talaleklfp kqcqvlgivt pgivvtpmgs gsnrpqeiei gesgfallfp
      181 qiegikiqpf hfikdpknlt lerhqltevg lldnpelrvv lvfgyncckv gasnylqqvv
      241 stfsdmniil aggqvdnlss ltseknpldi dasgvvglsf sghriqsatv llnedvsdek
      301 taeaamqrlk aanipehnti gfmfacvgrg fqyyrakgnv eadafrkffp svplfgffgn
      361 geigcdrivt gnfilrkcne vkdddlfhsy ttimalihlg ssk
//
LOCUS       NP_001354709             618 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 18 isoform 5 [Homo sapiens].
ACCESSION   NP_001354709
VERSION     NP_001354709.1
DBSOURCE    REFSEQ: accession NM_001367780.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Ding,X., Barodia,S.K., Ma,L. and Goldberg,M.S.
  TITLE     Fbxl18 targets LRRK2 for proteasomal degradation and attenuates
            cell toxicity
  JOURNAL   Neurobiol Dis 98, 122-136 (2017)
   PUBMED   27890708
  REMARK    GeneRIF: Study showed that LRRK2 phosphorylation is required for
            LRRK2 to bind to Fbxl18, and that this interaction is important for
            regulating the amount of LRRK2 via ubiquitination of LRRK2 by the
            SCFFbxl18 ubiquitin ligase and subsequent proteasomal degradation
            of LRRK2. We also show that LRRK2 can induce caspase 8 mediated
            cell death and that the degradation of LRRK2 mediated by Fbxl18 can
            prevent LRRK2-mediated toxicity.
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Zhang,J., Yang,Z., Ou,J., Xia,X., Zhi,F. and Cui,J.
  TITLE     The F-box protein FBXL18 promotes glioma progression by promoting
            K63-linked ubiquitination of Akt
  JOURNAL   FEBS Lett 591 (1), 145-154 (2017)
   PUBMED   27926990
  REMARK    GeneRIF: FBXL18 plays an oncogenic role through promoting lysine
            63-linked ubiquitination of Akt in glioma.
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Liu,Y., Lear,T., Zhao,Y., Zhao,J., Zou,C., Chen,B.B. and
            Mallampalli,R.K.
  TITLE     F-box protein Fbxl18 mediates polyubiquitylation and proteasomal
            degradation of the pro-apoptotic SCF subunit Fbxl7
  JOURNAL   Cell Death Dis 6 (2), e1630 (2015)
   PUBMED   25654763
  REMARK    GeneRIF: Fbxl18 regulates apoptosis by mediating
            ubiquitin-dependent proteasomal degradation of the pro-apoptotic
            protein Fbxl7 that may impact cellular processes involved in cell
            cycle progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006483.3 and AC092171.4.
            
            Summary: The protein encoded by this gene is a member of a family
            of proteins that contain an approximately 40-amino acid F-box
            motif. This motif is important for interaction with SKP1 and for
            targeting some proteins for degradation. The encoded protein has
            been shown to control the cellular level of FBXL7, a protein that
            induces mitotic arrest, by targeting it for polyubiquitylation and
            proteasomal degradation. Members of the F-box protein family, such
            as FBXL18, are characterized by an approximately 40-amino acid
            F-box motif. F-box proteins interact with SKP1 through the F box,
            and they interact with ubiquitination targets through other protein
            interaction domains. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (5), as well as variant 6, encodes
            isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1163655.434799.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..618
                     /product="F-box/LRR-repeat protein 18 isoform 5"
                     /note="F-box/LRR-repeat protein 18"
                     /calculated_mol_wt=67771
     Region          1..575
                     /region_name="FBXL18_LRR"
                     /note="F-box/LRR-repeat protein 18, LRR; pfam19729"
                     /db_xref="CDD:466163"
     Region          192..217
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          245..284
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          285..314
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          315..384
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          351..376
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          385..432
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          433..459
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          460..489
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          490..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          516..540
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..618
                     /gene="FBXL18"
                     /gene_synonym="Fbl18"
                     /coded_by="NM_001367780.1:431..2287"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:80028"
                     /db_xref="HGNC:HGNC:21874"
                     /db_xref="MIM:609084"
ORIGIN      
        1 magcywlpgs tvehvarcrs lvkvnlsgch ltslrlskml salqhlrsla idvspgfdas
       61 qlsseckatl srvrelkqtl ftpsygvvpc ctslekllly feildrtreg ailsgqlmvg
      121 qsnvphyqnl rvfyarlapg yinqevvrly lavlsdrtpq nlhaflisvp gsfaesgatk
      181 nlldsmarnv vldalqlpks wlngssllqh mkfnnpfyfs fsrctlsggh liqqvinggk
      241 dlrslaslnl sgcvhclspd sllrkaeddi dssiletlva sccnlrhlnl saahhhsseg
      301 lgrhlcqlla rlrhlrslsl pvcsvadsap radrapaqpa mhavprgfgk kvrvgvqscp
      361 spfsgqacpq pssvfwsllk nlpflehlel igsnfssamp rnepairnsl ppcsraqsvg
      421 dsevaaigql aflrhltlaq lpsvltgsgl vniglqcqql rslslanlgm mgkvvympal
      481 sdmlkhckrl rdlrleqpyf sanaqffqal sqcpslqrlc lvsrsgtlqp davlafmarc
      541 lqvvmchlft geslatcksl qqsllrsfqa erpalnvvif pllhegltdv irdvplvhld
      601 eitlfksrva eeppnlww
//
LOCUS       NP_001186802             393 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-1,4-galactosyltransferase 3 [Homo sapiens].
ACCESSION   NP_001186802
VERSION     NP_001186802.1
DBSOURCE    REFSEQ: accession NM_001199873.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Bi,C., Shan,J., Li,M., Zhang,Q., Li,C., Tong,J. and Huang,Q.
  TITLE     Long noncoding RNA differentiation antagonizing nonprotein coding
            RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p
  JOURNAL   Neuroreport 32 (12), 965-974 (2021)
   PUBMED   34050113
  REMARK    GeneRIF: Long noncoding RNA differentiation antagonizing nonprotein
            coding RNA promotes the proliferation, invasion and migration of
            neuroblastoma cells via targeting beta-1, 4-galactosyltransferase
            III by sponging miR-338-3p.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Binieda,K., Rzepnikowska,W., Kolakowski,D., Kaminska,J.,
            Szczepankiewicz,A.A., Nieznanska,H., Kochanski,A. and Kabzinska,D.
  TITLE     Mutations in GDAP1 Influence Structure and Function of the
            Trans-Golgi Network
  JOURNAL   Int J Mol Sci 22 (2), 914 (2021)
   PUBMED   33477664
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Wu,T., Li,Y. and Chen,B.
  TITLE     B4GALT3 promotes cell proliferation and invasion in glioblastoma
  JOURNAL   Neurol Res 42 (6), 463-470 (2020)
   PUBMED   32202233
  REMARK    GeneRIF: B4GALT3 promotes cell proliferation and invasion in
            glioblastoma.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Tange,R., Tomatsu,T. and Sato,T.
  TITLE     Transcription of human beta4-galactosyltransferase 3 is regulated
            by differential DNA binding of Sp1/Sp3 in SH-SY5Y human
            neuroblastoma and A549 human lung cancer cell lines
  JOURNAL   Glycobiology 29 (3), 211-221 (2019)
   PUBMED   30561605
  REMARK    GeneRIF: These findings suggest that the transcription of the
            b4GalT3 gene is regulated by differential DNA binding of Sp3 and
            Sp1 in neuroblastoma and lung cancer. The increased expression of
            b4GalT3 in neuroblastoma may be ascribed to the enhanced expression
            of Sp3, which is observed for various cancers.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Liu,H., Chen,D., Bi,J., Han,J., Yang,M., Dong,W., Lin,T. and
            Huang,J.
  TITLE     Circular RNA circUBXN7 represses cell growth and invasion by
            sponging miR-1247-3p to enhance B4GALT3 expression in bladder
            cancer
  JOURNAL   Aging (Albany NY) 10 (10), 2606-2623 (2018)
   PUBMED   30312173
  REMARK    GeneRIF: In bladder tumor cells circUBXN7 serves as a competitive
            endogenous RNA of miR-1247-3p to elevate B4GALT3 expression,
            consequently inhibiting cell viability and invasion.
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Davidsson,J., Andersson,A., Paulsson,K., Heidenblad,M.,
            Isaksson,M., Borg,A., Heldrup,J., Behrendtz,M., Panagopoulos,I.,
            Fioretos,T. and Johansson,B.
  TITLE     Tiling resolution array comparative genomic hybridization,
            expression and methylation analyses of dup(1q) in Burkitt lymphomas
            and pediatric high hyperdiploid acute lymphoblastic leukemias
            reveal clustered near-centromeric breakpoints and overexpression of
            genes in 1q22-32.3
  JOURNAL   Hum Mol Genet 16 (18), 2215-2225 (2007)
   PUBMED   17613536
  REMARK    GeneRIF: B4GALT3, DAP3, RGS16, TMEM183A and UCK2--were
            significantly overexpressed in dup(1q)-positive ALLs compared with
            high hyperdiploid ALLs without dup(1q).
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Guo,S., Sato,T., Shirane,K. and Furukawa,K.
  TITLE     Galactosylation of N-linked oligosaccharides by human
            beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed
            in Sf-9 cells
  JOURNAL   Glycobiology 11 (10), 813-820 (2001)
   PUBMED   11588157
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Lo,N.W., Shaper,J.H., Pevsner,J. and Shaper,N.L.
  TITLE     The expanding beta 4-galactosyltransferase gene family: messages
            from the databanks
  JOURNAL   Glycobiology 8 (5), 517-526 (1998)
   PUBMED   9597550
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Almeida,R., Amado,M., David,L., Levery,S.B., Holmes,E.H., Merkx,G.,
            van Kessel,A.G., Rygaard,E., Hassan,H., Bennett,E. and Clausen,H.
  TITLE     A family of human beta4-galactosyltransferases. Cloning and
            expression of two novel UDP-galactose:beta-n-acetylglucosamine
            beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3
  JOURNAL   J Biol Chem 272 (51), 31979-31991 (1997)
   PUBMED   9405390
  REMARK    Erratum:[J Biol Chem 1998 Jul 17;273(29):18674]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC339671.1, AK291455.1,
            AL590714.27 and BC006099.1.
            
            Summary: This gene is one of seven beta-1,4-galactosyltransferase
            (beta4GalT) genes. They encode type II membrane-bound glycoproteins
            that appear to have exclusive specificity for the donor substrate
            UDP-galactose; all transfer galactose in a beta1,4 linkage to
            similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a
            distinct function in the biosynthesis of different glycoconjugates
            and saccharide structures. As type II membrane proteins, they have
            an N-terminal hydrophobic signal sequence that directs the protein
            to the Golgi apparatus and which then remains uncleaved to function
            as a transmembrane anchor. By sequence similarity, the beta4GalTs
            form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and
            beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene
            encodes an enzyme that may be mainly involved in the synthesis of
            the first N-acetyllactosamine unit of poly-N-acetyllactosamine
            chains. Multiple alternatively spliced transcript variants encoding
            the same protein have been found for this gene. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) is the longest transcript.
            Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.177429.1,
                                           SRR1803613.47106.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..393
                     /product="beta-1,4-galactosyltransferase 3"
                     /EC_number="2.4.1.90"
                     /EC_number="2.4.1.38"
                     /EC_number="2.4.1.275"
                     /note="beta-N-acetylglucosaminyl-glycolipid
                     beta-1,4-galactosyltransferase 3; b4Gal-T3;
                     beta-1,4-GalTase 3; epididymis secretory sperm binding
                     protein; nal synthase; N-acetyllactosamine synthase;
                     UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3;
                     UDP-galactose:beta-N-acetylglucosamine
                     beta-1,4-galactosyltransferase 3; UDP-Gal:betaGlcNAc beta
                     1,4- galactosyltransferase, polypeptide 3;
                     beta-N-acetylglucosaminylglycopeptide
                     beta-1,4-galactosyltransferase; neolactotriaosylceramide
                     beta-1,4-galactosyltransferase"
                     /calculated_mol_wt=43797
     Site            11..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          122..341
                     /region_name="b4GalT"
                     /note="Beta-4-Galactosyltransferase is involved in the
                     formation of the poly-N-acetyllactosamine core structures
                     present in glycoproteins and glycosphingolipids; cd00899"
                     /db_xref="CDD:132999"
     Site            order(130,132,134,169,195..197)
                     /site_type="active"
                     /note="ligand binding site [active]"
                     /db_xref="CDD:132999"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Site            order(195,197,291)
                     /site_type="active"
                     /note="metal binding site [active]"
                     /db_xref="CDD:132999"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     Region          339..393
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60512.2)"
     Site            385
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60512.2)"
     CDS             1..393
                     /gene="B4GALT3"
                     /gene_synonym="beta4Gal-T3"
                     /coded_by="NM_001199873.1:728..1909"
                     /db_xref="CCDS:CCDS1222.1"
                     /db_xref="GeneID:8703"
                     /db_xref="HGNC:HGNC:926"
                     /db_xref="MIM:604014"
ORIGIN      
        1 mlrrllerpc tlallvgsql avmmylslgg frslsalfgr dqgptfdysh prdvysnlsh
       61 lpgapggppa pqglpycper spllvgpvsv sfspvpslae ivernprvep ggryrpagce
      121 prsrtaiivp hrarehhlrl llyhlhpflq rqqlaygiyv ihqagngtfn rakllnvgvr
      181 ealrdeewdc lflhdvdllp endhnlyvcd prgprhvava mnkfgyslpy pqyfggvsal
      241 tpdqylkmng fpneywgwgg edddiatrvr lagmkisrpp tsvghykmvk hrgdkgneen
      301 phrfdllvrt qnswtqdgmn sltyqllare lgplytnita digtdprgpr apsgpryppg
      361 ssqafrqeml qrrpparpgp lstanhtalr gsh
//
LOCUS       NP_001305637             452 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of MON1-CCZ1 complex isoform 4 [Homo sapiens].
ACCESSION   NP_001305637
VERSION     NP_001305637.1
DBSOURCE    REFSEQ: accession NM_001318708.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Yong,X., Jia,G., Liu,Z., Zhou,C., Yi,J., Tang,Y., Chen,L., Chen,L.,
            Wang,Y., Sun,Q., Billadeau,D.D., Su,Z. and Jia,D.
  TITLE     Cryo-EM structure of the Mon1-Ccz1-RMC1 complex reveals molecular
            basis of metazoan RAB7A activation
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2301725120 (2023)
   PUBMED   37216550
REFERENCE   2  (residues 1 to 452)
  AUTHORS   van den Boomen,D.J.H., Sienkiewicz,A., Berlin,I., Jongsma,M.L.M.,
            van Elsland,D.M., Luzio,J.P., Neefjes,J.J.C. and Lehner,P.J.
  TITLE     A trimeric Rab7 GEF controls NPC1-dependent lysosomal cholesterol
            export
  JOURNAL   Nat Commun 11 (1), 5559 (2020)
   PUBMED   33144569
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 452)
  AUTHORS   Vaites,L.P., Paulo,J.A., Huttlin,E.L. and Harper,J.W.
  TITLE     Systematic Analysis of Human Cells Lacking ATG8 Proteins Uncovers
            Roles for GABARAPs and the CCZ1/MON1 Regulator C18orf8/RMC1 in
            Macroautophagic and Selective Autophagic Flux
  JOURNAL   Mol Cell Biol 38 (1), e00392-17 (2017)
   PUBMED   29038162
  REMARK    GeneRIF: Authors identified C18orf8/RMC1 as a new subunit of the
            CCZ1-MON1 RAB7 guanine exchange factor (GEF) that positively
            regulates RAB7 recruitment to LE/autophagosomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Yuan,M., Chen,J. and Zeng,Z.
  TITLE     Knockdown of macrophage inhibitory cytokine-1 in RPMI-8226 human
            multiple myeloma cells inhibits osteoclastic differentiation
            through inhibiting the RANKL-Erk1/2 signaling pathway
  JOURNAL   Mol Med Rep 14 (6), 5199-5204 (2016)
   PUBMED   27779672
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026634.11, AK295246.1, AC010853.11 and BC008305.1.
            
            Summary: This gene encodes a colon cancer associated protein.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (4) has multiple differences,
            which result in the use of a downstream in-frame start codon and a
            frameshift in the 3' coding region, compared to variant 1. The
            encoded isoform (4) has a shorter N-terminus and a distinct and
            shorter C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..452
                     /product="regulator of MON1-CCZ1 complex isoform 4"
                     /note="colon cancer-associated protein Mic1; macrophage
                     inhibitory cytokine 1; uncharacterized protein C18orf8; WD
                     repeat domain 98; WD repeat-containing protein 98;
                     regulator of MON1-CCZ1 complex"
                     /calculated_mol_wt=51122
     Region          318..>401
                     /region_name="Mic1"
                     /note="Colon cancer-associated protein Mic1-like;
                     pfam07035"
                     /db_xref="CDD:429257"
     CDS             1..452
                     /gene="RMC1"
                     /gene_synonym="C18orf8; HsT2591; Mic-1; MIC1; WDR98"
                     /coded_by="NM_001318708.1:536..1894"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:29919"
                     /db_xref="HGNC:HGNC:24326"
                     /db_xref="MIM:620267"
ORIGIN      
        1 mycpesavil lsttvlenvl qpfhfragtm sklpkfeiel paapkstkps lserdiamat
       61 iygqlyvlfl rhhsrtsnst gaevvlyhlp regackkmhi lklnrtgkfa lnvvdnlvvv
      121 hhqdtetsvi fdiklrgefd gsvtfhhpvl parsiqpyqi pitgpaavts qspvpcklys
      181 sswivfqpdi iisasqgylw nlqvklepiv nllpdkgrlm dfllqrkeck mvilsvcsqm
      241 lsesdraslp viatvfdkln heykkyldae qsyamaveag qsrsspllkr pvrtqavldq
      301 sdvythvlsa fvekkemphk fviavlmeyi rslnqfqiav qhylhelvik tlvqhnlfym
      361 lhqflqyhvl sdskplacll lslesfyppa hqlsldmlkm lqsrlkttcf siqysaflns
      421 etsvcegapi shqgntvknm llfsnrflet kl
//
LOCUS       NP_001336348             600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_001336348 XP_016862148
VERSION     NP_001336348.1
DBSOURCE    REFSEQ: accession NM_001349419.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_016862148.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (8), as well as variants 7 and
            9-15, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.179056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349419.1:2086..3888"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001353135             875 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 9 [Homo sapiens].
ACCESSION   NP_001353135 XP_016861303
VERSION     NP_001353135.1
DBSOURCE    REFSEQ: accession NM_001366206.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 875)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 875)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 875)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 875)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 875)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 875)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 875)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 875)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 875)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 875)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861303.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853561.21845.1,
                                           SRR1803611.151569.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..875
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..875
                     /product="disks large homolog 1 isoform 9"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=97901
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..172
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          171..259
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(182..188,205,208,238,242,245..246)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          268..352
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(277..283,300,303,333,337,340..341)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          353..414
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          412..502
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(424..430,441,444,474,478,481..482)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          531..597
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(536,558..559,580)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(539,541,544,553,571..572,591,593..594)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          684..862
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..875
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366206.1:227..2854"
                     /note="isoform 9 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS93451.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kvngtdadye yeeitlergn
      181 sglgfsiagg tdnphigdds sifitkiitg gaaaqdgrlr vndcilrvne vdvrdvthsk
      241 avealkeags ivrlyvkrrk pvsekimeik likgpkglgf siaggvgnqh ipgdnsiyvt
      301 kiieggaahk dgklqigdkl lavnnvclee vtheeavtal kntsdfvylk vakptsmymn
      361 dgyappditn sssqpvdnhv spssflgqtp asparyspvs kavlgddeit reprkvvlhr
      421 gstglgfniv ggedgegifi sfilaggpad lsgelrkgdr iisvnsvdlr aasheqaaaa
      481 lknagqavti vaqyrpeeys rfeakihdlr eqmmnssiss gsgslrtsqk rslyvralfd
      541 ydktkdsglp sqglnfkfgd ilhvinasdd ewwqarqvtp dgesdevgvi pskrrvekke
      601 rarlktvkfn sktrdkgqsf ndkrkknlfs rkfpfyknkd qseqetsdad qhvtsnasds
      661 essyrgqeey vlsyepvnqq evnytrpvii lgpmkdrind dlisefpdkf gscvphttrp
      721 krdyevdgrd yhfvtsreqm ekdiqehkfi eagqynnhly gtsvqsvrev aekgkhcild
      781 vsgnaikrlq iaqlypisif ikpksmenim emnkrlteeq arktferamk leqeftehft
      841 aivqgdtled iynqvkqiie eqsgsyiwvp akekl
//
LOCUS       NP_055838                676 aa            linear   PRI 20-NOV-2025
DEFINITION  WD and tetratricopeptide repeats protein 1 isoform b [Homo
            sapiens].
ACCESSION   NP_055838
VERSION     NP_055838.2
DBSOURCE    REFSEQ: accession NM_015023.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Wang,X., Cai,Q., Ping,J., Diaz-Zabala,H., Xia,Y. and Guo,X.
  TITLE     The putative oncogenic role of WDTC1 in colorectal cancer
  JOURNAL   Carcinogenesis 43 (6), 594-600 (2022)
   PUBMED   35238908
  REMARK    GeneRIF: The putative oncogenic role of WDTC1 in colorectal cancer.
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Lai,C.Q., Parnell,L.D., Arnett,D.K., Garcia-Bailo,B., Tsai,M.Y.,
            Kabagambe,E.K., Straka,R.J., Province,M.A., An,P., Borecki,I.B.,
            Tucker,K.L. and Ordovas,J.M.
  TITLE     WDTC1, the ortholog of Drosophila adipose gene, associates with
            human obesity, modulated by MUFA intake
  JOURNAL   Obesity (Silver Spring) 17 (3), 593-600 (2009)
   PUBMED   19238144
  REMARK    GeneRIF: WDTC1 variation may be an important risk factor
            contributing to obesity in both Puerto Rican and white populations.
            GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Hader,T., Muller,S., Aguilera,M., Eulenberg,K.G., Steuernagel,A.,
            Ciossek,T., Kuhnlein,R.P., Lemaire,L., Fritsch,R., Dohrmann,C.,
            Vetter,I.R., Jackle,H., Doane,W.W. and Bronner,G.
  TITLE     Control of triglyceride storage by a WD40/TPR-domain protein
  JOURNAL   EMBO Rep 4 (5), 511-516 (2003)
   PUBMED   12717455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB072151.1, BC032523.1, HY218382.1 and FO393419.1.
            
            On Aug 5, 2002 this sequence version replaced NP_055838.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (b) that is 1 aa shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032523.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..676
                     /product="WD and tetratricopeptide repeats protein 1
                     isoform b"
                     /note="DDB1 and CUL4 associated factor 9; adipose homolog;
                     WD and tetratricopeptide repeats protein 1"
                     /calculated_mol_wt=75660
     Region          <39..215
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          45..84
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          51..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          88..129
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          93..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..172
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          138..178
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..222
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          232..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          265..305
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          358..>467
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          361..394
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            order(365..366,369..370,372,396,399..400,403..404,
                     406..407,433,436..437,440..441,444)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          365..389
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          394..427
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          396..431
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          432..456
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          486..508
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          534..574
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          536..576
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <545..>625
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          577..616
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          654..676
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     CDS             1..676
                     /gene="WDTC1"
                     /gene_synonym="ADP; DCAF9"
                     /coded_by="NM_015023.5:420..2450"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS296.1"
                     /db_xref="GeneID:23038"
                     /db_xref="HGNC:HGNC:29175"
                     /db_xref="MIM:619763"
ORIGIN      
        1 makvnitrdl irrqikerga lsferryhvt dpfirrlgle aelqghsgcv nclewnekgd
       61 llasgsddqh tivwdplhhk kllsmhtght anifsvkflp hagdrilitg aadskvhvhd
      121 ltvketihmf gdhtnrvkri atapmwpntf wsaaedglir qydlrenskh sevlidltey
      181 cgqlveakcl tvnpqdnncl avgasgpfvr lydirmihnh rksmkqspsa gvhtfcdrqk
      241 plpdgaaqyy vaghlpvklp dynnrlrvlv atyvtfspng tellvnmgge qvylfdltyk
      301 qrpytfllpr kchssgvqng kmstngvsng vsnglhlhsn gfrlpesrgh vspqvelppy
      361 lervkqqane afacqqwtqa iqlyskavqr aphnamlygn raaaymkrkw dgdhydalrd
      421 clkaislnpc hlkahfrlar clfelkyvae aleclddfkg kfpeqahssa cdalgrdita
      481 alfskndgee kkgpgggapv rlrstsrkds isedemvlre rsydyqfryc ghcntttdik
      541 eanffgsnaq yivsgsddgs ffiwekettn lvrvlqgdes ivnclqphps ycflatsgid
      601 pvvrlwnprp esedltgrvv edmegasqan qrrmnadple vmllnmgyri tglssggaga
      661 sddedssegq vqcrps
//
LOCUS       NP_060099                861 aa            linear   PRI 20-NOV-2025
DEFINITION  protein argonaute-4 [Homo sapiens].
ACCESSION   NP_060099
VERSION     NP_060099.2
DBSOURCE    REFSEQ: accession NM_017629.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 861)
  AUTHORS   Wang,L., Li,D., Su,X., Zhao,Y., Huang,A., Li,H., Li,J., Xia,W.,
            Jia,T., Zhang,H., Dong,J., Liu,X. and Shao,N.
  TITLE     AGO4 suppresses tumor growth by modulating autophagy and apoptosis
            via enhancing TRIM21-mediated ubiquitination of GRP78 in a
            p53-independent manner
  JOURNAL   Oncogene 42 (1), 62-77 (2023)
   PUBMED   36371565
  REMARK    GeneRIF: AGO4 suppresses tumor growth by modulating autophagy and
            apoptosis via enhancing TRIM21-mediated ubiquitination of GRP78 in
            a p53-independent manner.
REFERENCE   2  (residues 1 to 861)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 861)
  AUTHORS   Choi,E.J., Ren,J., Zhang,K., Wu,W., Lee,Y.S., Lee,I. and Bao,X.
  TITLE     The Importance of AGO 1 and 4 in Post-Transcriptional Gene
            Regulatory Function of tRF5-GluCTC, an Respiratory Syncytial
            Virus-Induced tRNA-Derived RNA Fragment
  JOURNAL   Int J Mol Sci 21 (22), 8766 (2020)
   PUBMED   33233493
  REMARK    GeneRIF: The Importance of AGO 1 and 4 in Post-Transcriptional Gene
            Regulatory Function of tRF5-GluCTC, an Respiratory Syncytial
            Virus-Induced tRNA-Derived RNA Fragment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 861)
  AUTHORS   Elkayam,E., Faehnle,C.R., Morales,M., Sun,J., Li,H. and
            Joshua-Tor,L.
  TITLE     Multivalent Recruitment of Human Argonaute by GW182
  JOURNAL   Mol Cell 67 (4), 646-658 (2017)
   PUBMED   28781232
REFERENCE   5  (residues 1 to 861)
  AUTHORS   Hauptmann,J., Kater,L., Loffler,P., Merkl,R. and Meister,G.
  TITLE     Generation of catalytic human Ago4 identifies structural elements
            important for RNA cleavage
  JOURNAL   RNA 20 (10), 1532-1538 (2014)
   PUBMED   25114291
REFERENCE   6  (residues 1 to 861)
  AUTHORS   Pillai,R.S., Artus,C.G. and Filipowicz,W.
  TITLE     Tethering of human Ago proteins to mRNA mimics the miRNA-mediated
            repression of protein synthesis
  JOURNAL   RNA 10 (10), 1518-1525 (2004)
   PUBMED   15337849
REFERENCE   7  (residues 1 to 861)
  AUTHORS   Meister,G., Landthaler,M., Patkaniowska,A., Dorsett,Y., Teng,G. and
            Tuschl,T.
  TITLE     Human Argonaute2 mediates RNA cleavage targeted by miRNAs and
            siRNAs
  JOURNAL   Mol Cell 15 (2), 185-197 (2004)
   PUBMED   15260970
REFERENCE   8  (residues 1 to 861)
  AUTHORS   Sasaki,T., Shiohama,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of eight members of the Argonaute family in the
            human genome
  JOURNAL   Genomics 82 (3), 323-330 (2003)
   PUBMED   12906857
REFERENCE   9  (residues 1 to 861)
  AUTHORS   Doi,N., Zenno,S., Ueda,R., Ohki-Hamazaki,H., Ui-Tei,K. and Saigo,K.
  TITLE     Short-interfering-RNA-mediated gene silencing in mammalian cells
            requires Dicer and eIF2C translation initiation factors
  JOURNAL   Curr Biol 13 (1), 41-46 (2003)
   PUBMED   12526743
REFERENCE   10 (residues 1 to 861)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354864.16, AB046787.1,
            AL359186.15 and CA419947.1.
            
            On Mar 18, 2003 this sequence version replaced NP_060099.1.
            
            Summary: This gene encodes a member of the Argonaute family of
            proteins which contain PAZ and PIWI domains and play an integral
            role in RNA interference and short-interfering-RNA-mediated gene
            silencing. This gene is located on chromosome 1 in a cluster of
            related family members. [provided by RefSeq, Mar 2017].
            
            Sequence Note: Sequence Note: This RefSeq record was created from
            transcript and genomic sequence data to make the sequence
            consistent with the reference genome assembly. The genomic
            coordinates used for the transcript record were based on transcript
            alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC152450.1, AB046787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373210.4/ ENSP00000362306.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..861
                     /product="protein argonaute-4"
                     /note="eukaryotic translation initiation factor 2C, 4;
                     argonaute 4, RISC catalytic component; argonaute RISC
                     catalytic component 4"
                     /calculated_mol_wt=96966
     Region          26..155
                     /region_name="ArgoN"
                     /note="N-terminal domain of argonaute; pfam16486"
                     /db_xref="CDD:465134"
     Region          166..216
                     /region_name="ArgoL1"
                     /note="Argonaute linker 1 domain; pfam08699"
                     /db_xref="CDD:462567"
     Region          217..337
                     /region_name="PAZ_argonaute_like"
                     /note="PAZ domain, argonaute_like subfamily. Argonaute is
                     part of the RNA-induced silencing complex (RISC), and is
                     an endonuclease that plays a key role in the RNA
                     interference pathway. The PAZ domain has been named after
                     the proteins Piwi,Argonaut, and Zwille; cd02846"
                     /db_xref="CDD:239212"
     Site            order(269,284,298,302,320,327,329)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239212"
     Region          384..819
                     /region_name="Piwi_ago-like"
                     /note="PIWI domain, Argonaute-like subfamily. Argonaute is
                     the central component of the RNA-induced silencing complex
                     (RISC) and related complexes. The PIWI domain is the
                     C-terminal portion of Argonaute and consists of two
                     subdomains, one of which provides the...; cd04657"
                     /db_xref="CDD:240015"
     Site            order(521,525,537..540,543,551,554,558,562)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240015"
     Site            order(589,591,671,809)
                     /site_type="active"
                     /db_xref="CDD:240015"
     Region          825..846
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HCK5.2)"
     CDS             1..861
                     /gene="AGO4"
                     /gene_synonym="EIF2C4"
                     /coded_by="NM_017629.4:402..2987"
                     /db_xref="CCDS:CCDS397.1"
                     /db_xref="GeneID:192670"
                     /db_xref="HGNC:HGNC:18424"
                     /db_xref="MIM:607356"
ORIGIN      
        1 mealgpgppa slfqpprrpg lgtvgkpirl lanhfqvqip kidvyhydvd ikpekrprrv
       61 nrevvdtmvr hfkmqifgdr qpgydgkrnm ytahplpigr drvdmevtlp gegkdqtfkv
      121 svqwvsvvsl qlllealagh lnevpddsvq aldvitrhlp smrytpvgrs ffsppegyyh
      181 plgggrevwf gfhqsvrpam wnmmlnidvs atafyraqpi iefmcevldi qnineqtkpl
      241 tdsqrvkftk eirglkvevt hcgqmkrkyr vcnvtrrpas hqtfplqlen gqamectvaq
      301 yfkqkyslql kyphlpclqv gqeqkhtylp levcnivagq rcikkltdnq tstmikatar
      361 sapdrqeeis rlvksnsmvg gpdpylkefg ivvhnemtel tgrvlpapml qyggrnktva
      421 tpnqgvwdmr gkqfyagiei kvwavacfap qkqcredllk sftdqlrkis kdagmpiqgq
      481 pcfckyaqga dsvepmfkhl kmtyvglqli vvilpgktpv yaevkrvgdt llgmatqcvq
      541 vknvvktspq tlsnlclkin aklgginnvl vphqrpsvfq qpviflgadv thppagdgkk
      601 psiaavvgsm dghpsrycat vrvqtsrqei sqellysqev iqdltnmvre lliqfykstr
      661 fkptriiyyr ggvsegqmkq vawpeliair kacisleedy rpgityivvq krhhtrlfca
      721 dktervgksg nvpagttvds tithpsefdf ylcshagiqg tsrpshyqvl wddncftade
      781 lqlltyqlch tyvrctrsvs ipapayyarl vafraryhlv dkdhdsaegs hvsgqsngrd
      841 pqalakavqi hhdtqhtmyf a
//
LOCUS       NP_001356788             167 aa            linear   PRI 20-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001356788
VERSION     NP_001356788.1
DBSOURCE    REFSEQ: accession NM_001369859.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Hardy,S., Zolotarov,Y., Coleman,J., Roitman,S., Khursheed,H.,
            Aubry,I., Uetani,N. and Tremblay,M.L.
  TITLE     PRL-1/2 phosphatases control TRPM7 magnesium-dependent function to
            regulate cellular bioenergetics
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2221083120 (2023)
   PUBMED   36972446
  REMARK    GeneRIF: This study established the existence of a magnesium
            transporter protein complex (PTP4A2/CNNM3/TRPM7) governing the
            cellular uptake of this divalent cation. Moreover, PTP4A2 acts as a
            magnesium biosensor, controlling the activity of this complex to
            reprogram cellular metabolism.
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Li,Q., Bai,Y., Lyle,L.T., Yu,G., Amarasinghe,O., Nguele Meke,F.,
            Carlock,C. and Zhang,Z.Y.
  TITLE     Mechanism of PRL2 phosphatase-mediated PTEN degradation and
            tumorigenesis
  JOURNAL   Proc Natl Acad Sci U S A 117 (34), 20538-20548 (2020)
   PUBMED   32788364
  REMARK    GeneRIF: Mechanism of PRL2 phosphatase-mediated PTEN degradation
            and tumorigenesis.
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Cai,F., Huang,Y., Wang,M., Sun,M., Zhao,Y. and Hattori,M.
  TITLE     A FRET-based screening method to detect potential inhibitors of the
            binding of CNNM3 to PRL2
  JOURNAL   Sci Rep 10 (1), 12879 (2020)
   PUBMED   32733084
  REMARK    GeneRIF: A FRET-based screening method to detect potential
            inhibitors of the binding of CNNM3 to PRL2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Si,X., Zeng,Q., Ng,C.H., Hong,W. and Pallen,C.J.
  TITLE     Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase,
            with the beta-subunit of geranylgeranyltransferase II
  JOURNAL   J Biol Chem 276 (35), 32875-32882 (2001)
   PUBMED   11447212
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Zeng,Q., Hong,W. and Tan,Y.H.
  TITLE     Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
            phosphatases homologous to PRL-1
  JOURNAL   Biochem Biophys Res Commun 244 (2), 421-427 (1998)
   PUBMED   9514946
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
REFERENCE   10 (residues 1 to 167)
  AUTHORS   Zhao,Z., Lee,C.C., Monckton,D.G., Yazdani,A., Coolbaugh,M.I.,
            Li,X., Bailey,J., Shen,Y. and Caskey,C.T.
  TITLE     Characterization and genomic mapping of genes and pseudogenes of a
            new human protein tyrosine phosphatase
  JOURNAL   Genomics 35 (1), 172-181 (1996)
   PUBMED   8661118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136115.21, DB503104.1,
            BI549454.1 and BC070181.1.
            
            Summary: The protein encoded by this gene belongs to a small class
            of the protein tyrosine phosphatase (PTP) family. PTPs are cell
            signaling molecules that play regulatory roles in a variety of
            cellular processes. PTPs in this class contain a protein tyrosine
            phosphatase catalytic domain and a characteristic C-terminal
            prenylation motif. This PTP has been shown to primarily associate
            with plasmic and endosomal membrane through its C-terminal
            prenylation. This PTP was found to interact with the beta-subunit
            of Rab geranylgeranyltransferase II (beta GGT II), and thus may
            function as a regulator of GGT II activity. Overexpression of this
            gene in mammalian cells conferred a transformed phenotype, which
            suggested its role in tumorigenesis. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 11, 12 and 17. [provided by RefSeq, Aug 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.371452.1,
                                           SRR5189652.102244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..167
                     /product="protein tyrosine phosphatase type IVA 2 isoform
                     1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase IVA; phosphatase of
                     regenerating liver 2; protein tyrosine phosphatase IVA2;
                     protein tyrosine phosphatase type IVA 2; PTP(CAAXII);
                     protein-tyrosine phosphatase of regenerating liver 2;
                     protein tyrosine phosphatase type IVA, member 2"
                     /calculated_mol_wt=18996
     Region          1..155
                     /region_name="PTP-IVa2"
                     /note="protein tyrosine phosphatase type IVA 2; cd18536"
                     /db_xref="CDD:350512"
     Site            order(1..4,69..70,103,105..107,134..139,142)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:350512"
     Site            164
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000305;
                     propagated from UniProtKB/Swiss-Prot (Q12974.1)"
     CDS             1..167
                     /gene="PTP4A2"
                     /gene_synonym="HH13; HH7-2; HU-PP-1; OV-1; PRL-2; PRL2;
                     ptp-IV1a; ptp-IV1b; PTP4A; PTPCAAX2"
                     /coded_by="NM_001369859.1:868..1371"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS348.1"
                     /db_xref="GeneID:8073"
                     /db_xref="HGNC:HGNC:9635"
                     /db_xref="MIM:601584"
ORIGIN      
        1 mnrpapveis yenmrflith nptnatlnkf teelkkygvt tlvrvcdaty dkapvekegi
       61 hvldwpfddg apppnqivdd wlnllktkfr eepgccvavh cvaglgrapv lvalaliecg
      121 mkyedavqfi rqkrrgafns kqllylekyr pkmrlrfrdt nghccvq
//
LOCUS       NP_653208                228 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome b5 domain-containing protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_653208
VERSION     NP_653208.2
DBSOURCE    REFSEQ: accession NM_144607.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 228)
  AUTHORS   Zhang,X., Xiao,Z., Zhang,J., Xu,C., Liu,S., Cheng,L., Zhou,S.,
            Zhao,S., Zhang,Y., Wu,J., Wang,Y. and Liu,M.
  TITLE     Differential requirements of IQUB for the assembly of radial spoke
            1 and the motility of mouse cilia and flagella
  JOURNAL   Cell Rep 41 (8), 111683 (2022)
   PUBMED   36417862
REFERENCE   2  (residues 1 to 228)
  AUTHORS   Zhao,L., Xie,H., Kang,Y., Lin,Y., Liu,G., Sakato-Antoku,M.,
            Patel-King,R.S., Wang,B., Wan,C., King,S.M., Zhao,C. and Huang,K.
  TITLE     Heme-binding protein CYB5D1 is a radial spoke component required
            for coordinated ciliary beating
  JOURNAL   Proc Natl Acad Sci U S A 118 (17) (2021)
   PUBMED   33875586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC060779.1, AK289520.1 and AC104581.22.
            
            On Dec 20, 2003 this sequence version replaced NP_653208.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060779.1, SRR1803611.204307.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000332439.5/ ENSP00000331479.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..228
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..228
                     /product="cytochrome b5 domain-containing protein 1
                     isoform 1"
                     /note="cytochrome b5 domain-containing protein 1"
                     /calculated_mol_wt=26558
     Region          21..>70
                     /region_name="Cyt-b5"
                     /note="Cytochrome b5-like Heme/Steroid binding domain;
                     pfam00173"
                     /db_xref="CDD:459698"
     CDS             1..228
                     /gene="CYB5D1"
                     /coded_by="NM_144607.6:133..819"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11123.1"
                     /db_xref="GeneID:124637"
                     /db_xref="HGNC:HGNC:26516"
ORIGIN      
        1 mprrglvagp dleyfqrryf tpaevaqhnr pedlwvsylg rvydltslaq eykgnlllkp
       61 ivevagqdis hwfdpktrdi rkhidpltgc lryctprgrf vhvppqlpcs dwandfgkpw
      121 wqgsyyevgr lsaktrsiri intltsqeht levgvlesiw eilhrylpyn shaasytwky
      181 egknlnmdft leengirdee eefdylsmdg tlhtpailly fnddltel
//
LOCUS       NP_001253965             430 aa            linear   PRI 20-NOV-2025
DEFINITION  large neutral amino acids transporter small subunit 2 isoform c
            [Homo sapiens].
ACCESSION   NP_001253965
VERSION     NP_001253965.1
DBSOURCE    REFSEQ: accession NM_001267036.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 430)
  AUTHORS   Crocco,P., Dato,S., La Grotta,R., Passarino,G. and Rose,G.
  TITLE     Evidence for a relationship between genetic polymorphisms of the
            L-DOPA transporter LAT2/4F2hc and risk of hypertension in the
            context of chronic kidney disease
  JOURNAL   BMC Med Genomics 17 (1), 163 (2024)
   PUBMED   38890684
  REMARK    GeneRIF: Evidence for a relationship between genetic polymorphisms
            of the L-DOPA transporter LAT2/4F2hc and risk of hypertension in
            the context of chronic kidney disease.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 430)
  AUTHORS   Wang,F.M., Xu,L.Q., Zhang,Z.C., Guo,Q., Du,Z.P., Lei,Y., Han,X.,
            Wu,C.Y., Zhao,F. and Chen,J.L.
  TITLE     SLC7A8 overexpression inhibits the growth and metastasis of lung
            adenocarcinoma and is correlated with a dismal prognosis
  JOURNAL   Aging (Albany NY) 16 (2), 1605-1619 (2024)
   PUBMED   38244585
  REMARK    GeneRIF: SLC7A8 overexpression inhibits the growth and metastasis
            of lung adenocarcinoma and is correlated with a dismal prognosis.
REFERENCE   3  (residues 1 to 430)
  AUTHORS   Meng,F., Wang,L., Gao,G., Chen,J., Wang,X., Wu,G. and Miu,Y.
  TITLE     Identification and verification of microRNA signature and key genes
            in the development of osteosarcoma with lung metastasis
  JOURNAL   Medicine (Baltimore) 101 (49), e32258 (2022)
   PUBMED   36626488
  REMARK    GeneRIF: Identification and verification of microRNA signature and
            key genes in the development of osteosarcoma with lung metastasis.
REFERENCE   4  (residues 1 to 430)
  AUTHORS   Min,Q., Wang,Y., Wu,Q., Li,X., Teng,H., Fan,J., Cao,Y., Fan,P. and
            Zhan,Q.
  TITLE     Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma
  JOURNAL   JCI Insight 6 (17), e150203 (2021)
   PUBMED   34494553
  REMARK    GeneRIF: Genomic and epigenomic evolution of acquired resistance to
            combination therapy in esophageal squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 430)
  AUTHORS   Yan,R., Li,Y., Muller,J., Zhang,Y., Singer,S., Xia,L., Zhong,X.,
            Gertsch,J., Altmann,K.H. and Zhou,Q.
  TITLE     Mechanism of substrate transport and inhibition of the human
            LAT1-4F2hc amino acid transporter
  JOURNAL   Cell Discov 7 (1), 16 (2021)
   PUBMED   33758168
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 430)
  AUTHORS   Broer,A., Friedrich,B., Wagner,C.A., Fillon,S., Ganapathy,V.,
            Lang,F. and Broer,S.
  TITLE     Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2
            requires different domains
  JOURNAL   Biochem J 355 (Pt 3), 725-731 (2001)
   PUBMED   11311135
REFERENCE   7  (residues 1 to 430)
  AUTHORS   Rossier,G., Meier,C., Bauch,C., Summa,V., Sordat,B., Verrey,F. and
            Kuhn,L.C.
  TITLE     LAT2, a new basolateral 4F2hc/CD98-associated amino acid
            transporter of kidney and intestine
  JOURNAL   J Biol Chem 274 (49), 34948-34954 (1999)
   PUBMED   10574970
REFERENCE   8  (residues 1 to 430)
  AUTHORS   Bassi,M.T., Sperandeo,M.P., Incerti,B., Bulfone,A., Pepe,A.,
            Surace,E.M., Gattuso,C., De Grandi,A., Buoninconti,A., Riboni,M.,
            Manzoni,M., Andria,G., Ballabio,A., Borsani,G. and Sebastio,G.
  TITLE     SLC7A8, a gene mapping within the lysinuric protein intolerance
            critical region, encodes a new member of the
            glycoprotein-associated amino acid transporter family
  JOURNAL   Genomics 62 (2), 297-303 (1999)
   PUBMED   10610726
REFERENCE   9  (residues 1 to 430)
  AUTHORS   Pineda,M., Fernandez,E., Torrents,D., Estevez,R., Lopez,C.,
            Camps,M., Lloberas,J., Zorzano,A. and Palacin,M.
  TITLE     Identification of a membrane protein, LAT-2, that Co-expresses with
            4F2 heavy chain, an L-type amino acid transport activity with broad
            specificity for small and large zwitterionic amino acids
  JOURNAL   J Biol Chem 274 (28), 19738-19744 (1999)
   PUBMED   10391915
REFERENCE   10 (residues 1 to 430)
  AUTHORS   Borsani,G., Bassi,M.T., Sperandeo,M.P., De Grandi,A.,
            Buoninconti,A., Riboni,M., Manzoni,M., Incerti,B., Pepe,A.,
            Andria,G., Ballabio,A. and Sebastio,G.
  TITLE     SLC7A7, encoding a putative permease-related protein, is mutated in
            patients with lysinuric protein intolerance
  JOURNAL   Nat Genet 21 (3), 297-301 (1999)
   PUBMED   10080183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL117258.4, AK296702.1, BX248288.1, AB037669.1 and AF135830.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (c) is shorter and has a distinct N-terminus, compared to isoform
            a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.210534.1, AK296702.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..430
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..430
                     /product="large neutral amino acids transporter small
                     subunit 2 isoform c"
                     /note="solute carrier family 7 (amino acid transporter,
                     L-type), member 8; solute carrier family 7 (cationic amino
                     acid transporter, y+ system), member 8; large neutral
                     amino acids transporter small subunit 2; integral membrane
                     protein E16H; L-type amino acid transporter 2; solute
                     carrier family 7 (amino acid transporter light chain, L
                     system), member 8"
                     /calculated_mol_wt=48152
     Region          <65..392
                     /region_name="2A0308"
                     /note="L-type amino acid transporter; TIGR00911"
                     /db_xref="CDD:273332"
     CDS             1..430
                     /gene="SLC7A8"
                     /gene_synonym="LAT2; LPI-PC1"
                     /coded_by="NM_001267036.1:101..1393"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58305.1"
                     /db_xref="GeneID:23428"
                     /db_xref="HGNC:HGNC:11066"
                     /db_xref="MIM:604235"
ORIGIN      
        1 mgqygqelsw kclvkavclq ehsqpsqllc tlllcwcvlg rerpfrkaqs tssplegvpr
       61 flkrllltwv ncssvrwatr vqdiftagkl lalaliiimg ivqickgeyf wlepknafen
      121 fqepdiglva laflqgsfay ggwnflnyvt eelvdpyknl praifisipl vtfvyvfanv
      181 ayvtamspqe llasnavavt fgekllgvma wimpisvals tfggvngslf tssrlffaga
      241 reghlpsvla mihvkrctpi pallftcist llmlvtsdmy tlinyvgfin ylfygvtvag
      301 qivlrwkkpd iprpikinll fpiiyllfwa fllvfslwse pvvcgiglai mltgvpvyfl
      361 gvywqhkpkc fsdfielltl vsqkmcvvvy pevergsgte eanedmeeqq qpmyqptptk
      421 dkdvagqpqp
//
LOCUS       NP_001179                211 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2 homologous antagonist/killer [Homo sapiens].
ACCESSION   NP_001179
VERSION     NP_001179.1
DBSOURCE    REFSEQ: accession NM_001188.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Guan,Z., Li,H., Zhang,C., Huang,Z., Ye,M., Zhang,Y., Li,S. and
            Peng,K.
  TITLE     RVFV virulence factor NSs triggers the mitochondrial MCL-1-BAK axis
            to activate pathogenic NLRP3 pyroptosis
  JOURNAL   PLoS Pathog 20 (8), e1012387 (2024)
   PUBMED   39213434
  REMARK    GeneRIF: RVFV virulence factor NSs triggers the mitochondrial
            MCL-1-BAK axis to activate pathogenic NLRP3 pyroptosis.
            Erratum:[PLoS Pathog. 2025 Apr 24;21(4):e1013113. doi:
            10.1371/journal.ppat.1013113. PMID: 40273018]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Dadsena,S., Cuevas Arenas,R., Vieira,G., Brodesser,S., Melo,M.N.
            and Garcia-Saez,A.J.
  TITLE     Lipid unsaturation promotes BAX and BAK pore activity during
            apoptosis
  JOURNAL   Nat Commun 15 (1), 4700 (2024)
   PUBMED   38830851
  REMARK    GeneRIF: Lipid unsaturation promotes BAX and BAK pore activity
            during apoptosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Miller,M.S., Cowan,A.D., Brouwer,J.M., Smyth,S.T., Peng,L.,
            Wardak,A.Z., Uren,R.T., Luo,C., Roy,M.J., Shah,S., Tan,Z.,
            Reid,G.E., Colman,P.M. and Czabotar,P.E.
  TITLE     Sequence differences between BAX and BAK core domains manifest as
            differences in their interactions with lipids
  JOURNAL   FEBS J 291 (11), 2335-2353 (2024)
   PUBMED   38088212
  REMARK    GeneRIF: Sequence differences between BAX and BAK core domains
            manifest as differences in their interactions with lipids.
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Schweighofer,S.V., Jans,D.C., Keller-Findeisen,J., Folmeg,A.,
            Ilgen,P., Bates,M. and Jakobs,S.
  TITLE     Endogenous BAX and BAK form mosaic rings of variable size and
            composition on apoptotic mitochondria
  JOURNAL   Cell Death Differ 31 (4), 469-478 (2024)
   PUBMED   38503846
  REMARK    GeneRIF: Endogenous BAX and BAK form mosaic rings of variable size
            and composition on apoptotic mitochondria.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Sattler,M., Liang,H., Nettesheim,D., Meadows,R.P., Harlan,J.E.,
            Eberstadt,M., Yoon,H.S., Shuker,S.B., Chang,B.S., Minn,A.J.,
            Thompson,C.B. and Fesik,S.W.
  TITLE     Structure of Bcl-xL-Bak peptide complex: recognition between
            regulators of apoptosis
  JOURNAL   Science 275 (5302), 983-986 (1997)
   PUBMED   9020082
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Chittenden,T., Flemington,C., Houghton,A.B., Ebb,R.G., Gallo,G.J.,
            Elangovan,B., Chinnadurai,G. and Lutz,R.J.
  TITLE     A conserved domain in Bak, distinct from BH1 and BH2, mediates cell
            death and protein binding functions
  JOURNAL   EMBO J 14 (22), 5589-5596 (1995)
   PUBMED   8521816
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Kiefer,M.C., Brauer,M.J., Powers,V.C., Wu,J.J., Umansky,S.R.,
            Tomei,L.D. and Barr,P.J.
  TITLE     Modulation of apoptosis by the widely distributed Bcl-2 homologue
            Bak
  JOURNAL   Nature 374 (6524), 736-739 (1995)
   PUBMED   7715731
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Chittenden,T., Harrington,E.A., O'Connor,R., Flemington,C.,
            Lutz,R.J., Evan,G.I. and Guild,B.C.
  TITLE     Induction of apoptosis by the Bcl-2 homologue Bak
  JOURNAL   Nature 374 (6524), 733-736 (1995)
   PUBMED   7715730
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Farrow,S.N., White,J.H., Martinou,I., Raven,T., Pun,K.T.,
            Grinham,C.J., Martinou,J.C. and Brown,R.
  TITLE     Cloning of a bcl-2 homologue by interaction with adenovirus E1B 19K
  JOURNAL   Nature 374 (6524), 731-733 (1995)
   PUBMED   7715729
  REMARK    Erratum:[Nature 1995 Jun 1;375(6530):431]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB142221.1, BC004431.1,
            Z93017.6 and BM855203.1.
            
            Summary: The protein encoded by this gene belongs to the BCL2
            protein family. BCL2 family members form oligomers or heterodimers
            and act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. This protein localizes to
            mitochondria, and functions to induce apoptosis. It interacts with
            and accelerates the opening of the mitochondrial voltage-dependent
            anion channel, which leads to a loss in membrane potential and the
            release of cytochrome c. This protein also interacts with the tumor
            suppressor P53 after exposure to cell stress. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004431.1, U23765.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374467.4/ ENSP00000363591.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.31"
     Protein         1..211
                     /product="bcl-2 homologous antagonist/killer"
                     /note="pro-apoptotic protein BAK; apoptosis regulator BAK;
                     BCL2-like 7 protein; bcl2-L-7; bcl-2-like protein 7"
                     /calculated_mol_wt=23278
     Region          1..28
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16611.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q16611.1)"
     Region          29..183
                     /region_name="Bcl-2_like"
                     /note="Apoptosis regulator proteins of the Bcl-2 family,
                     named after B-cell lymphoma 2. This alignment model spans
                     what have been described as Bcl-2 homology regions BH1,
                     BH2, BH3, and BH4. Many members of this family have an
                     additional C-terminal transmembrane...; cd06845"
                     /db_xref="CDD:132900"
     Site            29..42
                     /site_type="active"
                     /note="BH4 [active]"
                     /db_xref="CDD:132900"
     Region          74..88
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16611.1)"
     Site            78..86
                     /site_type="active"
                     /note="BH3 [active]"
                     /db_xref="CDD:132900"
     Site            order(81..82,84..85,89,92..93,109..110,113..114,117..118,
                     124,126..127,129..130,134,138,183)
                     /site_type="active"
                     /note="BH3-homology region binding site [active]"
                     /db_xref="CDD:132900"
     Region          117..136
                     /region_name="BH1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16611.1)"
     Site            order(117..119,123..135)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Region          169..184
                     /region_name="BH2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16611.1)"
     Site            169..183
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     Site            188..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16611.1)"
     CDS             1..211
                     /gene="BAK1"
                     /gene_synonym="BAK; BAK-LIKE; BCL2L7; CDN1"
                     /coded_by="NM_001188.4:284..919"
                     /db_xref="CCDS:CCDS4781.1"
                     /db_xref="GeneID:578"
                     /db_xref="HGNC:HGNC:949"
                     /db_xref="MIM:600516"
ORIGIN      
        1 masgqgpgpp rqecgepalp saseeqvaqd teevfrsyvf yrhqqeqeae gvaapadpem
       61 vtlplqpsst mgqvgrqlai igddinrryd sefqtmlqhl qptaenayey ftkiatslfe
      121 sginwgrvva llgfgyrlal hvyqhgltgf lgqvtrfvvd fmlhhciarw iaqrggwvaa
      181 lnlgngpiln vlvvlgvvll gqfvvrrffk s
//
LOCUS       NP_001269338             317 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1 regulatory subunit 7 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001269338 XP_005247087
VERSION     NP_001269338.1
DBSOURCE    REFSEQ: accession NM_001282409.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Jiang,Y., Scott,K.L., Kwak,S.J., Chen,R. and Mardon,G.
  TITLE     Sds22/PP1 links epithelial integrity and tumor suppression via
            regulation of myosin II and JNK signaling
  JOURNAL   Oncogene 30 (29), 3248-3260 (2011)
   PUBMED   21399659
  REMARK    GeneRIF: human Sds22 is focally deleted and downregulated in
            multiple carcinomas, and this downregulation correlates with tumor
            progression, suggesting that sds22 inactivation may contribute to
            tumorigenesis and metastatic potential
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Posch,M., Khoudoli,G.A., Swift,S., King,E.M., Deluca,J.G. and
            Swedlow,J.R.
  TITLE     Sds22 regulates aurora B activity and microtubule-kinetochore
            interactions at mitosis
  JOURNAL   J Cell Biol 191 (1), 61-74 (2010)
   PUBMED   20921135
  REMARK    GeneRIF: Sds22 specifically defines protein phosphatase 1 function
            and localization in mitosis.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Lesage,B., Beullens,M., Pedelini,L., Garcia-Gimeno,M.A.,
            Waelkens,E., Sanz,P. and Bollen,M.
  TITLE     A complex of catalytically inactive protein phosphatase-1
            sandwiched between Sds22 and inhibitor-3
  JOURNAL   Biochemistry 46 (31), 8909-8919 (2007)
   PUBMED   17630778
  REMARK    GeneRIF: Sds22 and Inhibitor-3 form a heterotrimeric complex with
            PP1, both in cell lysates and after purification. A pool of PP1 is
            complexly controlled by both Sds22 and Inhibitor-3.
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Ceulemans,H., Vulsteke,V., De Maeyer,M., Tatchell,K., Stalmans,W.
            and Bollen,M.
  TITLE     Binding of the concave surface of the Sds22 superhelix to the alpha
            4/alpha 5/alpha 6-triangle of protein phosphatase-1
  JOURNAL   J Biol Chem 277 (49), 47331-47337 (2002)
   PUBMED   12226088
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Ceulemans,H., Van Eynde,A., Perez-Callejon,E., Beullens,M.,
            Stalmans,W. and Bollen,M.
  TITLE     Structure and splice products of the human gene encoding sds22, a
            putative mitotic regulator of protein phosphatase-1
  JOURNAL   Eur J Biochem 262 (1), 36-42 (1999)
   PUBMED   10231361
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Renouf,S., Beullens,M., Wera,S., Van Eynde,A., Sikela,J.,
            Stalmans,W. and Bollen,M.
  TITLE     Molecular cloning of a human polypeptide related to yeast sds22, a
            regulator of protein phosphatase-1
  JOURNAL   FEBS Lett 375 (1-2), 75-78 (1995)
   PUBMED   7498485
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Berry,R., Stevens,T.J., Walter,N.A., Wilcox,A.S., Rubano,T.,
            Hopkins,J.A., Weber,J., Goold,R., Soares,M.B. and Sikela,J.M.
  TITLE     Gene-based sequence-tagged-sites (STSs) as the basis for a human
            gene map
  JOURNAL   Nat Genet 10 (4), 415-423 (1995)
   PUBMED   7670491
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051689.1, AC005237.2 and
            BM676947.1.
            
            On Sep 7, 2013 this sequence version replaced XP_005247087.1.
            
            Summary: This gene encodes a protein subunit that regulates the
            activity of the serine/threonine phosphatase, protein
            phosphatase-1. The encoded protein is required for completion of
            the mitotic cycle and for targeting protein phosphatase-1 to
            mitotic kinetochores. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            protein (isoform 2, also known as sds22alpha2) is shorter compared
            to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051689.1, SRR1803613.67810.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..317
                     /product="protein phosphatase 1 regulatory subunit 7
                     isoform 2"
                     /note="protein phosphatase 1 regulatory subunit 22;
                     protein phosphatase 1, regulatory (inhibitor) subunit 7;
                     testis secretory sperm-binding protein Li 210a"
                     /calculated_mol_wt=36706
     Region          <40..155
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          57..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          79..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..122
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          120..311
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          123..144
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          145..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          167..188
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          189..210
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          211..232
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          233..254
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..317
                     /gene="PPP1R7"
                     /gene_synonym="SDS22"
                     /coded_by="NM_001282409.1:839..1792"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63194.1"
                     /db_xref="GeneID:5510"
                     /db_xref="HGNC:HGNC:9295"
                     /db_xref="MIM:602877"
ORIGIN      
        1 maaergagqq qsqemmeeeh elpvdmetin ldrdaedvdl nhyrigkieg fevlkkvktl
       61 clrqnlikci enleelqslr eldlydnqik kienlealte leildisfnl lrniegvdkl
      121 trlkklflvn nkiskienls nlhqlqmlel gsnriraien idtltnlesl flgknkitkl
      181 qnldaltnlt vlsmqsnrlt kieglqnlvn lrelylshng ievieglenn nkltmldias
      241 nrikkienis hltelqefwm ndnlleswsd ldelkgarsl etvylernpl qkdpqyrrkv
      301 mlalpsvrqi datfvrf
//
LOCUS       NP_001308857             448 aa            linear   PRI 20-NOV-2025
DEFINITION  creatine kinase U-type, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001308857
VERSION     NP_001308857.1
DBSOURCE    REFSEQ: accession NM_001321928.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Ayyappan,V., Jenkinson,N.M., Tressler,C.M., Tan,Z., Cheng,M.,
            Shen,X.E., Guerrero,A., Sonkar,K., Cai,R., Adelaja,O., Roy,S.,
            Meeker,A., Argani,P. and Glunde,K.
  TITLE     Context-dependent roles for ubiquitous mitochondrial creatine
            kinase CKMT1 in breast cancer progression
  JOURNAL   Cell Rep 43 (4), 114121 (2024)
   PUBMED   38615320
  REMARK    GeneRIF: Context-dependent roles for ubiquitous mitochondrial
            creatine kinase CKMT1 in breast cancer progression.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Zhu,L., Tang,Y., Li,X.Y., Kerk,S.A., Lyssiotis,C.A., Feng,W.,
            Sun,X., Hespe,G.E., Wang,Z., Stemmler,M.P., Brabletz,S.,
            Brabletz,T., Keller,E.T., Ma,J., Cho,J.S., Yang,J. and Weiss,S.J.
  TITLE     A Zeb1/MtCK1 metabolic axis controls osteoclast activation and
            skeletal remodeling
  JOURNAL   EMBO J 42 (7), e111148 (2023)
   PUBMED   36843552
  REMARK    GeneRIF: A Zeb1/MtCK1 metabolic axis controls osteoclast activation
            and skeletal remodeling.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Politis-Barber,V., Petrick,H.L., Raajendiran,A., DesOrmeaux,G.J.,
            Brunetta,H.S., Dos Reis,L.M., Mori,M.A., Wright,D.C., Watt,M.J. and
            Holloway,G.P.
  TITLE     Ckmt1 is Dispensable for Mitochondrial Bioenergetics Within
            White/Beige Adipose Tissue
  JOURNAL   Function (Oxf) 3 (5), zqac037 (2022)
   PUBMED   37954502
  REMARK    GeneRIF: Ckmt1 is Dispensable for Mitochondrial Bioenergetics
            Within White/Beige Adipose Tissue.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Yang,M., Liu,S., Xiong,Y., Zhao,J. and Deng,W.
  TITLE     An integrative pan-cancer analysis of molecular characteristics and
            oncogenic role of mitochondrial creatine kinase 1A (CKMT1A) in
            human tumors
  JOURNAL   Sci Rep 12 (1), 10025 (2022)
   PUBMED   35705641
  REMARK    GeneRIF: An integrative pan-cancer analysis of molecular
            characteristics and oncogenic role of mitochondrial creatine kinase
            1A (CKMT1A) in human tumors.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Brdiczka,D., Kaldis,P. and Wallimann,T.
  TITLE     In vitro complex formation between the octamer of mitochondrial
            creatine kinase and porin
  JOURNAL   J Biol Chem 269 (44), 27640-27644 (1994)
   PUBMED   7525559
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Haas,R.C. and Strauss,A.W.
  TITLE     Separate nuclear genes encode sarcomere-specific and ubiquitous
            human mitochondrial creatine kinase isoenzymes
  JOURNAL   J Biol Chem 265 (12), 6921-6927 (1990)
   PUBMED   2324105
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Haas,R.C., Korenfeld,C., Zhang,Z.F., Perryman,B., Roman,D. and
            Strauss,A.W.
  TITLE     Isolation and characterization of the gene and cDNA encoding human
            mitochondrial creatine kinase
  JOURNAL   J Biol Chem 264 (5), 2890-2897 (1989)
   PUBMED   2914937
  REMARK    Erratum:[J Biol Chem 1989 Sep 25;264(27):16332]
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Stallings,R.L., Olson,E., Strauss,A.W., Thompson,L.H.,
            Bachinski,L.L. and Siciliano,M.J.
  TITLE     Human creatine kinase genes on chromosomes 15 and 19, and proximity
            of the gene for the muscle form to the genes for apolipoprotein C2
            and excision repair
  JOURNAL   Am J Hum Genet 43 (2), 144-151 (1988)
   PUBMED   3400641
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Jacobus,W.E., Moreadith,R.W. and Vandegaer,K.M.
  TITLE     Control of heart oxidative phosphorylation by creatine kinase in
            mitochondrial membranes
  JOURNAL   Ann N Y Acad Sci 414, 73-89 (1983)
   PUBMED   6584077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK316319.1 and BC006467.1.
            
            Summary: Mitochondrial creatine (MtCK) kinase is responsible for
            the transfer of high energy phosphate from mitochondria to the
            cytosolic carrier, creatine. It belongs to the creatine kinase
            isoenzyme family. It exists as two isoenzymes, sarcomeric MtCK and
            ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine
            kinase occurs in two different oligomeric forms: dimers and
            octamers, in contrast to the exclusively dimeric cytosolic creatine
            kinase isoenzymes. Many malignant cancers with poor prognosis have
            shown overexpression of ubiquitous mitochondrial creatine kinase;
            this may be related to high energy turnover and failure to
            eliminate cancer cells via apoptosis. Ubiquitous mitochondrial
            creatine kinase has 80% homology with the coding exons of
            sarcomeric mitochondrial creatine kinase. Two genes located near
            each other on chromosome 15 have been identified which encode
            identical mitochondrial creatine kinase proteins. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK316319.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152474, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.3"
     Protein         1..448
                     /product="creatine kinase U-type, mitochondrial isoform 2"
                     /EC_number="2.7.3.2"
                     /note="creatine kinase, mitochondrial 1 (ubiquitous);
                     creatine kinase U-type, mitochondrial; acidic-type
                     mitochondrial creatine kinase; ubiquitous mitochondrial
                     creatine kinase"
                     /calculated_mol_wt=50290
     Region          80..437
                     /region_name="creatine_kinase_like"
                     /note="Phosphagen (guanidino) kinases such as creatine
                     kinase and similar enzymes; cd00716"
                     /db_xref="CDD:153076"
     Site            order(136,265,296,347,349)
                     /site_type="other"
                     /note="creatine binding site [chemical binding]"
                     /db_xref="CDD:153076"
     Site            order(192,194,196,255,292,300,356,358..360,384,386,
                     388..389,399)
                     /site_type="other"
                     /note="ADP binding site [chemical binding]"
                     /db_xref="CDD:153076"
     Site            order(381..390,393..402)
                     /site_type="active"
                     /note="substrate specificity loop [active]"
                     /db_xref="CDD:153076"
     CDS             1..448
                     /gene="CKMT1A"
                     /gene_synonym="CKMT1; mia-CK; U-MtCK"
                     /coded_by="NM_001321928.1:254..1600"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="GeneID:548596"
                     /db_xref="HGNC:HGNC:31736"
                     /db_xref="MIM:613415"
ORIGIN      
        1 magpfsrlls arpglrllal agagslaagf llrpepvraa serrrlypps qtwptgqlpg
       61 nctrsrrlcp psmvtgyplp saeypdlrkh nncmashltp avyarlcdkt tptgwtldqc
      121 iqtgvdnpgh pfiktvgmva gdeetyevfa dlfdpviqer hngydprtmk httdldaski
      181 rsgyfderyv lssrvrtgrs irglslppac traerrever vvvdalsglk gdlagryyrl
      241 semteaeqqq liddhflfdk pvsplltaag mardwpdarg iwhnneksfl iwvneedhtr
      301 vismekggnm krvferfcrg lkeverliqe rgwefmwner lgyiltcpsn lgtglragvh
      361 iklpllskds rfpkilenlr lqkrgtggvd taatggvfdi snldrlgkse velvqlvidg
      421 vnylidcerr lergqdirip tpvihtkh
//
LOCUS       NP_001158884             968 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p105 subunit isoform 2 proprotein [Homo
            sapiens].
ACCESSION   NP_001158884
VERSION     NP_001158884.1
DBSOURCE    REFSEQ: accession NM_001165412.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 968)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 968)
  AUTHORS   Vazquez-Coto,D., Perez-Oliveira,S., Menendez-Gonzalez,M., Coto,E.
            and Alvarez,V.
  TITLE     Assessing the association between common functional Nuclear Factor
            Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA) and Alzheimer s
            disease
  JOURNAL   Behav Brain Res 476, 115264 (2025)
   PUBMED   39322062
  REMARK    GeneRIF: Assessing the association between common functional
            Nuclear Factor Kappa-b gene polymorphisms (NFKB1, NFKBIZ, NFKBIA)
            and Alzheimer s disease.
REFERENCE   3  (residues 1 to 968)
  AUTHORS   Al-Salihy,S.R., Al-Shawk,R.S., Al-Waysi,S.A. and Rasheed,M.N.
  TITLE     Association of nuclear factor-kappa B1 (NF-kappaB1) Ins/Del gene
            polymorphism with Hepatitis C virus outcomes
  JOURNAL   J Pak Med Assoc 74 (10 (Supple-8)), S34-S38 (2024)
   PUBMED   39434268
  REMARK    GeneRIF: Association of nuclear factor-kappa B1 (NF-kappaB1)
            Ins/Del gene polymorphism with Hepatitis C virus outcomes.
REFERENCE   4  (residues 1 to 968)
  AUTHORS   Eluard,B., Thieblemont,C. and Baud,V.
  TITLE     NF-kappaB in the New Era of Cancer Therapy
  JOURNAL   Trends Cancer 6 (8), 677-687 (2020)
   PUBMED   32409139
  REMARK    Review article
REFERENCE   5  (residues 1 to 968)
  AUTHORS   Lin,L. and Ghosh,S.
  TITLE     A glycine-rich region in NF-kappaB p105 functions as a processing
            signal for the generation of the p50 subunit
  JOURNAL   Mol Cell Biol 16 (5), 2248-2254 (1996)
   PUBMED   8628291
REFERENCE   6  (residues 1 to 968)
  AUTHORS   Muller,C.W., Rey,F.A., Sodeoka,M., Verdine,G.L. and Harrison,S.C.
  TITLE     Structure of the NF-kappa B p50 homodimer bound to DNA
  JOURNAL   Nature 373 (6512), 311-317 (1995)
   PUBMED   7830764
REFERENCE   7  (residues 1 to 968)
  AUTHORS   Rice,N.R., MacKichan,M.L. and Israel,A.
  TITLE     The precursor of NF-kappa B p50 has I kappa B-like functions
  JOURNAL   Cell 71 (2), 243-253 (1992)
   PUBMED   1423592
REFERENCE   8  (residues 1 to 968)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
REFERENCE   9  (residues 1 to 968)
  AUTHORS   Urban,M.B., Schreck,R. and Baeuerle,P.A.
  TITLE     NF-kappa B contacts DNA by a heterodimer of the p50 and p65 subunit
  JOURNAL   EMBO J 10 (7), 1817-1825 (1991)
   PUBMED   2050119
REFERENCE   10 (residues 1 to 968)
  AUTHORS   Bours,V., Villalobos,J., Burd,P.R., Kelly,K. and Siebenlist,U.
  TITLE     Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding
            protein with homology to the rel oncogene and to cell-cycle motifs
  JOURNAL   Nature 348 (6296), 76-80 (1990)
   PUBMED   2234062
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051765.1, M58603.1,
            AF213884.2 and AI076882.1.
            
            Summary: This gene encodes a 105 kD protein which can undergo
            cotranslational processing by the 26S proteasome to produce a 50 kD
            protein. The 105 kD protein is a Rel protein-specific transcription
            inhibitor and the 50 kD protein is a DNA binding subunit of the
            NF-kappa-B (NFKB) protein complex. NFKB is a transcription
            regulator that is activated by various intra- and extra-cellular
            stimuli such as cytokines, oxidant-free radicals, ultraviolet
            irradiation, and bacterial or viral products. Activated NFKB
            translocates into the nucleus and stimulates the expression of
            genes involved in a wide variety of biological functions.
            Inappropriate activation of NFKB has been associated with a number
            of inflammatory diseases while persistent inhibition of NFKB leads
            to inappropriate immune cell development or delayed cell growth.
            NFKB is a critical regulator of the immediate-early response to
            viral infection. Alternative splicing results in multiple
            transcript variants encoding different isoforms, at least one of
            which is proteolytically processed. [provided by RefSeq, Aug 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M58603.1, SRR14038191.4566505.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related :: involved in immune response or antiviral
                                   activity
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..968
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..968
                     /product="nuclear factor NF-kappa-B p105 subunit isoform 2
                     proprotein"
                     /note="nuclear factor kappa-B DNA binding subunit; nuclear
                     factor NF-kappa-B p50 subunit; nuclear factor NF-kappa-B
                     p105 subunit; DNA-binding factor KBF1; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells 1"
                     /calculated_mol_wt=105225
     mat_peptide     1..433
                     /product="Nuclear factor NF-kappa-B p50 subunit.
                     /id=PRO_0000030311"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
                     /calculated_mol_wt=47508
     Region          42..243
                     /region_name="RHD-n_NFkB1"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor of kappa B1 (NF-kappa B1);
                     cd07935"
                     /db_xref="CDD:143651"
     Site            order(56,58..59,61..62,65..68,143,145..146,243)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143651"
     Region          250..351
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(251,253..255,257..259,299..301,314,326,345,348,350)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(253..254,256,269,271,273,306..307,310,312)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(274,276,307..308)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          360..365
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          372..394
                     /region_name="GRR. /evidence=ECO:0000269|PubMed:8628291"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          425..453
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            431
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            433..434
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed).
                     /evidence=ECO:0000269|PubMed:9529257; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          435..968
                     /region_name="Interaction with CFLAR.
                     /evidence=ECO:0000269|PubMed:13679070"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Site            440
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            441
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by EP300.
                     /evidence=ECO:0000305|PubMed:11739381; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          498..758
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(542,544,548..549,552..554,556..557,561,564,579,581,
                     583,587..588,591..593,595..596,600,603,612,614,616,
                     620..621,624..626,628..629,633,636)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          542..579
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          581..612
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          650..684
                     /region_name="Essential for interaction with HIF1AN.
                     /evidence=ECO:0000269|PubMed:17003112"
                     /note="propagated from UniProtKB/Swiss-Prot (P19838.2)"
     Region          650..680
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            678
                     /site_type="hydroxylation"
                     /note="(3S)-3-hydroxyasparagine, by HIF1AN, partial.
                     /evidence=ECO:0000269|PubMed:17003112; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          684..716
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63369; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Region          815..890
                     /region_name="Death_NFkB1_p105"
                     /note="Death domain of the Nuclear Factor-KappaB1
                     precursor protein p105; cd08797"
                     /db_xref="CDD:260063"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-beta, in vitro.
                     /evidence=ECO:0000269|PubMed:12871932,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            923
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:11158290; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            927
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:11158290,
                     ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:12482991,
                     ECO:0000269|PubMed:25860612; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            932
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:12482991; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            937
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25799; propagated from
                     UniProtKB/Swiss-Prot (P19838.2)"
     CDS             1..968
                     /gene="NFKB1"
                     /gene_synonym="CVID12; EBP-1; KBF1; NF-kappa-B1;
                     NF-kappaB; NF-kappabeta; NF-kB; NF-kB1; NFkappaB;
                     NFKB-p105; NFKB-p50"
                     /coded_by="NM_001165412.2:438..3344"
                     /note="isoform 2 proprotein is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS54783.1"
                     /db_xref="GeneID:4790"
                     /db_xref="HGNC:HGNC:7794"
                     /db_xref="MIM:164011"
ORIGIN      
        1 maeddpylgr peqmfhldps lthtifnpev fqpqmalptd gpylqileqp kqrgfrfryv
       61 cegpshgglp gasseknkks ypqvkicnyv gpakvivqlv tngknihlha hslvgkhced
      121 gictvtagpk dmvvgfanlg ilhvtkkkvf etlearmtea cirgynpgll vhpdlaylqa
      181 egggdrqlgd rekelirqaa lqqtkemdls vvrlmftafl pdstgsftrr lepvvsdaiy
      241 dskapnasnl kivrmdrtag cvtggeeiyl lcdkvqkddi qirfyeeeen ggvwegfgdf
      301 sptdvhrqfa ivfktpkykd initkpasvf vqlrrksdle tsepkpflyy peikdkeevq
      361 rkrqklmpnf sdsfgggsga gaggggmfgs ggggggtgst gpgysfphyg fptyggitfh
      421 pgttksnagm khgtmdtesk kdpegcdksd dkntvnlfgk vietteqdqe pseatvgnge
      481 vtltyatgtk eesagvqdnl flekamqlak rhanalfdya vtgdvkmlla vqrhltavqd
      541 engdsvlhla iihlhsqlvr dllevtsgli sddiinmrnd lyqtplhlav itkqedvved
      601 llragadlsl ldrlgnsvlh laakeghdkv lsillkhkka allldhpngd glnaihlamm
      661 snslpcllll vaagadvnaq eqksgrtalh lavehdnisl agclllegda hvdsttydgt
      721 tplhiaagrg strlaallka agadplvenf eplydlddsw enagedegvv pgttpldmat
      781 swqvfdilng kpyepeftsd dllaqgdmkq laedvklqly klleipdpdk nwatlaqklg
      841 lgilnnafrl spapsktlmd nyevsggtvr elvealrqmg yteaieviqa asspvkttsq
      901 ahslplspas trqqidelrd sdsvcdsgve tsfrklsfte sltsgasllt lnkmphdygq
      961 egplegki
//
LOCUS       NP_004808               1190 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_004808
VERSION     NP_004808.2
DBSOURCE    REFSEQ: accession NM_004817.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1190)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1190)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1190)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1190)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1190)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1190)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1190)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1190)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1190)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1190)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB090695.1, L27476.1,
            BC027592.1 and AL358113.21.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 11, 2004 this sequence version replaced NP_004808.1.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) encodes isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027592.1, L27476.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000377245.9/ ENSP00000366453.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1190
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1190
                     /product="tight junction protein 2 isoform 1"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=133827
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          32..118
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(43..49,67,70,98,102,105..106)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          144..>226
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          152..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          183..>274
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          306..384
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(306..312,317..333,336..338,341,343..344,351,
                     359..360,362..363,375..381)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(318..324,330,333,363,367,370..371)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          408..506
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          509..590
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(520..526,536,539,568,572,575..576)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          604..666
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(613,615,618,622,643..644,660,662..663)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          700..879
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          920..1079
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            925
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1006
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1067
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          1105..1190
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1118
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            1159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          1188..1190
                     /region_name="Interaction with SCRIB.
                     /evidence=ECO:0000269|PubMed:15975580"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     CDS             1..1190
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_004817.4:97..3669"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6627.1"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 mpvrgdrgfp prrelsgwlr apgmeeliwe qytvtlqkds krgfgiavsg grdnphfeng
       61 etsivisdvl pggpadgllq endrvvmvng tpmedvlhsf avqqlrksgk vaaivvkrpr
      121 kvqvaalqas ppldqddraf evmdefdgrs frsgysersr lnshggrsrs wedspergrp
      181 herarsrerd lsrdrsrgrs lergldqdha rtrdrsrgrs lergldhdfg psrdrdrdrs
      241 rgrsidqdye rayhraydpd yerayspeyr rgarhdarsr gprsrsrehp hsrspspepr
      301 grpgpigvll mksraneeyg lrlgsqifvk emtrtglatk dgnlhegdii lkingtvten
      361 msltdarkli eksrgklqlv vlrdsqqtli nipslndsds eiediseies nrsfspeerr
      421 hqysdydyhs sseklkerps sredtpsrls rmgatptpfk stgdiagtvv petnkepryq
      481 edppapqpka aprtflrpsp edeaiygpnt kmvrfkkgds vglrlaggnd vgifvagiqe
      541 gtsaeqeglq egdqilkvnt qdfrglvred avlylleipk gemvtilaqs radvyrdila
      601 cgrgdsffir shfeceketp qslaftrgev frvvdtlydg klgnwlavri gnelekglip
      661 nksraeqmas vqnaqrdnag dradfwrmrg qrsgvkknlr ksredltavv svstkfpaye
      721 rvllreagfk rpvvlfgpia diameklane lpdwfqtakt epkdagseks tgvvrlntvr
      781 qiieqdkhal ldvtpkavdl lnytqwfpiv iffnpdsrqg vktmrqrlnp tsnkssrklf
      841 dqanklkktc ahlftatinl nsandswfgs lkdtiqhqqg eavwvsegkm egmdddpedr
      901 msyltamgad ylscdsrlis dfedtdgegg aytdneldep aeeplvssit rssepvqhee
      961 sirkpspepr aqmrraassd qlrdnspppa fkpeppkakt qnkeesydfs ksyeyksnps
     1021 avagnetpga stkgypppva akptfgrsil kpstpippqe geevgessee qdnapksvlg
     1081 kvkifekmdh karlqrmqel qeaqnariei aqkhpdiyav pikthkpdpg tpqhtssrpp
     1141 epqkapsrpy qdtrgsygsd aeeeeyrqql sehskrgyyg qsaryrdtel
//
LOCUS       NP_001352602            1128 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001352602
VERSION     NP_001352602.1
DBSOURCE    REFSEQ: accession NM_001365673.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1128)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1128)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1128)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1128)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1128)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1128)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1128)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853560.16671.1,
                                           SRR1803611.35651.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1128
                     /product="cordon-bleu protein-like 1 isoform 4"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=123737
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          60..126
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          144..222
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          249..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          291..296
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          325..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          360..365
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          454..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          780..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          <789..1026
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          882..964
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          995..1081
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1077..1102
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1081..1082,1084..1086,1088..1090,1098..1101)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1098..1101
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     Region          1103..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     CDS             1..1128
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001365673.2:136..3522"
                     /note="isoform 4 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS63045.1"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mdgrtprpqd aparrkpkak aplppaetky tdvssaadsv estafimeqk enmidkdvel
       61 svvlpgdiik sttvhgskpm mdlliflcaq yhlnpssyti dllsaeqnhi kfkpntpigm
      121 levekvilkp kmldkkkptp iipektvrvv infkktqkti vrvsphaslq elapiicskc
      181 efdplhtlll kdyqsqepld ltkslndlgl relyamdvnr escqisqnld imkekenkgf
      241 fsffqrskkk rdqtasapat plvnkhrptf trsntiskpy isntlpsdap kkrraplppm
      301 pasqsvpqdl ahiqerpasc ivksmsvdet dkspceagrv ragslqlssm sagnsslrrt
      361 krkapsppsk ipphqsdens rvtalqpvdg vppdsasean speelsspag issdysleei
      421 dekeelsevp kveaenispk sqdipfvstd iintlkndpd salgngsgef sqnsmeekqe
      481 tkstdgqeph svvydtsngk kvvdsirnlk slgpnqenvv qneiivypen tednmkngvk
      541 kteinvegva knnnidmeve rpsnseahet dtaisykenh laassvpdqk lnqpsaektk
      601 daaiqttpsc nsfdgkhqdh nlsdskveec vqtsnnnist qhsclssqds vntsrefrsq
      661 gtliihsedp ltvkdpicah gnddllppvd ridknstasy lknyplyrqd ynpkpkpsne
      721 itreyipkig mttykivppk sleiskdwqs etieykddqd mhalgkkhth envketaiqt
      781 edsaisespe eplpnlkpkp nlrtehqvps svsspddamv splkpapkmt rdtgtapfap
      841 nleeinnile skfksrasna qakpssfflq mqkrvsghyv tsaaaksvha apnpapkelt
      901 nkeaerdmlp speqtlspls kmphsvpqpl vektdddvig qapaeasppp iapkpvtipa
      961 sqvstqnlkt lktfgaprpy sssgpspfal avvkrsqsfs kertespsas alvqppante
     1021 egkthsvnkf vdipqlgvsd kennsahneq nsqiptptdg psftvmrqss ltfqssdpeq
     1081 mrqslltair sgeaaaklkr vtipsntisv ngrsrlshsm spdaqdgh
//
LOCUS       NP_001265003            1838 aa            linear   PRI 20-NOV-2025
DEFINITION  collagen alpha-1(V) chain isoform 2 preproprotein [Homo sapiens].
ACCESSION   NP_001265003
VERSION     NP_001265003.1
DBSOURCE    REFSEQ: accession NM_001278074.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1838)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1838)
  AUTHORS   Duan,X., Ye,D., Yuan,J., Guan,B., Guan,W., Liu,S., Fang,J., Shi,J.,
            Zhu,Y., Li,Q., Lu,Q. and Xu,G.
  TITLE     COL5A1 overexpression correlates with poor prognosis in human
            cervical cancer
  JOURNAL   Int J Biol Markers 39 (3), 265-273 (2024)
   PUBMED   39043220
  REMARK    GeneRIF: COL5A1 overexpression correlates with poor prognosis in
            human cervical cancer.
REFERENCE   3  (residues 1 to 1838)
  AUTHORS   Wang,J., Zhang,Z., Zhuang,J., Kang,D. and Song,W.
  TITLE     CircCOL5A1 is involved in proliferation, invasion, and inhibition
            of ferroptosis of colorectal cancer cells via miR-1287-5p/SLC7A11
  JOURNAL   J Biochem Mol Toxicol 38 (8), e23772 (2024)
   PUBMED   39030862
  REMARK    GeneRIF: CircCOL5A1 is involved in proliferation, invasion, and
            inhibition of ferroptosis of colorectal cancer cells via
            miR-1287-5p/SLC7A11.
REFERENCE   4  (residues 1 to 1838)
  AUTHORS   Mitchell,A.L., Judis,L.M., Schwarze,U., Vaynshtok,P.M., Drumm,M.L.
            and Byers,P.H.
  TITLE     Characterization of tissue-specific and developmentally regulated
            alternative splicing of exon 64 in the COL5A1 gene
  JOURNAL   Connect Tissue Res 53 (3), 267-276 (2012)
   PUBMED   22149965
REFERENCE   5  (residues 1 to 1838)
  AUTHORS   Takahara,K., Hoffman,G.G. and Greenspan,D.S.
  TITLE     Complete structural organization of the human alpha 1 (V) collagen
            gene (COL5A1): divergence from the conserved organization of other
            characterized fibrillar collagen genes
  JOURNAL   Genomics 29 (3), 588-597 (1995)
   PUBMED   8575750
REFERENCE   6  (residues 1 to 1838)
  AUTHORS   Lee,S. and Greenspan,D.S.
  TITLE     Transcriptional promoter of the human alpha 1(V) collagen gene
            (COL5A1)
  JOURNAL   Biochem J 310 (Pt 1) (Pt 1), 15-22 (1995)
   PUBMED   7646438
REFERENCE   7  (residues 1 to 1838)
  AUTHORS   Malfait,F., Symoens,S. and Syx,D.
  TITLE     Classic Ehlers-Danlos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301422
REFERENCE   8  (residues 1 to 1838)
  AUTHORS   Greenspan,D.S., Byers,M.G., Eddy,R.L., Cheng,W., Jani-Sait,S. and
            Shows,T.B.
  TITLE     Human collagen gene COL5A1 maps to the q34.2----q34.3 region of
            chromosome 9, near the locus for nail-patella syndrome
  JOURNAL   Genomics 12 (4), 836-837 (1992)
   PUBMED   1572660
REFERENCE   9  (residues 1 to 1838)
  AUTHORS   Mann,K.
  TITLE     Isolation of the alpha 3-chain of human type V collagen and
            characterization by partial sequencing
  JOURNAL   Biol Chem Hoppe Seyler 373 (2), 69-75 (1992)
   PUBMED   1571108
REFERENCE   10 (residues 1 to 1838)
  AUTHORS   Greenspan,D.S., Cheng,W. and Hoffman,G.G.
  TITLE     The pro-alpha 1(V) collagen chain. Complete primary structure,
            distribution of expression, and comparison with the pro-alpha 1(XI)
            collagen chain
  JOURNAL   J Biol Chem 266 (36), 24727-24733 (1991)
   PUBMED   1722213
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL591890.31, AB371583.1,
            CN399221.1, AB209864.1, CN399265.1, CN399198.1, BM051019.1,
            AI190929.1, CB152831.1, ES314363.1, BC032405.1, CN484933.1 and
            CA446007.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an alpha chain for one of the low
            abundance fibrillar collagens. Fibrillar collagen molecules are
            trimers that can be composed of one or more types of alpha chains.
            Type V collagen is found in tissues containing type I collagen and
            appears to regulate the assembly of heterotypic fibers composed of
            both type I and type V collagen. This gene product is closely
            related to type XI collagen and it is possible that the collagen
            chains of types V and XI constitute a single collagen type with
            tissue-specific chain combinations. The encoded procollagen protein
            occurs commonly as the heterotrimer
            pro-alpha1(V)-pro-alpha1(V)-pro-alpha2(V). Mutations in this gene
            are associated with Ehlers-Danlos syndrome, types I and II.
            Alternative splicing of this gene results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (2) contains an alternate in-frame
            exon in the 3' coding region compared to variant 1. It encodes
            isoform 2 which is of the same length but contains an alternate
            segment, compared to isoform 1. This variant is based on
            experimental data in PMID 22149965 and is supported by partial
            transcripts and RNA-seq data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: PMID: 22149965
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1838
                     /product="collagen alpha-1(V) chain isoform 2
                     preproprotein"
                     /note="collagen alpha-1(V) chain; collagen, type V, alpha
                     1"
                     /calculated_mol_wt=179589
     sig_peptide     1..37
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
                     /calculated_mol_wt=4083
     proprotein      38..1838
                     /product="collagen alpha-1(V) chain isoform 2 proprotein"
                     /calculated_mol_wt=179589
     mat_peptide     38..1605
                     /product="Collagen alpha-1(V) chain. /id=PRO_0000005756"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
                     /calculated_mol_wt=153487
     Region          39..230
                     /region_name="TSPN"
                     /note="Thrombospondin N-terminal -like domains;
                     smart00210"
                     /db_xref="CDD:214560"
     Region          231..443
                     /region_name="Nonhelical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Site            234
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            236
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            240
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Region          242..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Site            262
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            263
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Region          281..457
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Site            338
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            340
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            346
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            347
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            416
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            417
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            420
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            421
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Region          <429..>750
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          444..558
                     /region_name="Interrupted collagenous region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Region          470..520
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Region          526..545
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Region          559..1574
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Region          559..1570
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Site            570
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            576
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            621
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            627
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            639
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            642
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            648
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            654
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            657
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Region          <669..>933
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            675
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            678
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            687
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            690
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            696
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            705
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            708
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            717
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            720
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            726
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            732
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            744
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            750
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            756
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            762
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            765
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            771
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            774
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            780
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            789
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            795
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            804
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            807
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            810
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            816
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            819
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Region          <826..>1073
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            834
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            846
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            861
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            864
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            870
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            873
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            876
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            882
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            888
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            891
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            897
                     /site_type="hydroxylation"
                     /note="5-hydroxylysine.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            903
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            906
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:2496661,
                     ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            930
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            945
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Region          <979..>1213
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            1017
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1020
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1023
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1029
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1221
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1224
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Region          <1360..>1520
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            1467
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Site            1470
                     /site_type="hydroxylation"
                     /note="Hydroxyproline.
                     /evidence=ECO:0000269|PubMed:8181482; propagated from
                     UniProtKB/Swiss-Prot (P20908.3)"
     Region          1571..1605
                     /region_name="Nonhelical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P20908.3)"
     Site            1601
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Site            1604
                     /site_type="sulfatation"
                     /note="Sulfotyrosine. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P20908.3)"
     Region          1607..1836
                     /region_name="COLFI"
                     /note="Fibrillar collagen C-terminal domain; pfam01410"
                     /db_xref="CDD:460199"
     CDS             1..1838
                     /gene="COL5A1"
                     /gene_synonym="EDSC; EDSCL1; FMDMF"
                     /coded_by="NM_001278074.1:384..5900"
                     /note="isoform 2 preproprotein is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS75932.1"
                     /db_xref="GeneID:1289"
                     /db_xref="HGNC:HGNC:2209"
                     /db_xref="MIM:120215"
ORIGIN      
        1 mdvhtrwkar salrpgapll ppllllllwa pppsraaqpa dllkvldfhn lpdgitkttg
       61 fcatrrsskg pdvayrvtkd aqlsaptkql ypasafpedf silttvkakk gsqaflvsiy
      121 neqgiqqigl elgrspvfly edhtgkpgpe dyplfrginl sdgkwhrial svhkknvtli
      181 ldckkkttkf ldrsdhpmid ingiivfgtr ildeevfegd iqqllfvsdh raaydycehy
      241 spdcdtavpd tpqsqdpnpd eyytegdgeg etyyyeypyy edpedlgkep tpskkpveaa
      301 kettevpeel tptpteaapm petsegagke edvgigdydy vpsedyytps pyddltygeg
      361 eenpdqptdp gagaeiptst adtsnssnpa pppgegaddl egefteetir nldenyydpy
      421 ydptsspsei gpgmpanqdt iyegiggprg ekgqkgepai iepgmliegp pgpegpaglp
      481 gppgtmgptg qvgdpgergp pgrpglpgad glpgppgtml mlpfrfgggg dagskgpmvs
      541 aqesqaqail qqarlalrgp agpmgltgrp gpvgppgsgg lkgepgdvgp qgprgvqgpp
      601 gpagkpgrrg ragsdgargm pgqtgpkgdr gfdglaglpg ekghrgdpgp sgppgppgdd
      661 gergddgevg prglpgepgp rgllgpkgpp gppgppgvtg mdgqpgpkgn vgpqgepgpp
      721 gqqgnpgaqg lpgpqgaigp pgekgplgkp glpgmpgadg ppghpgkegp pgekggqgpp
      781 gpqgpigypg prgvkgadgi rglkgtkgek gedgfpgfkg dmgikgdrge igppgprged
      841 gpegpkgrgg pngdpgplgp pgekgklgvp glpgypgrqg pkgsigfpgf pgangekggr
      901 gtpgkpgprg qrgptgprge rgprgitgkp gpkgnsggdg pagppgergp ngpqgptgfp
      961 gpkgppgppg kdglpghpgq rgetgfqgkt gppgppgvvg pqgptgetgp mgerghpgpp
     1021 gppgeqglpg lagkegtkgd pgpaglpgkd gppglrgfpg drglpgpvga lglkgnegpp
     1081 gppgpagspg ergpagaagp igipgrpgpq gppgpagekg apgekgpqgp agrdglqgpv
     1141 glpgpagpvg ppgedgdkge igepgqkgsk gdkgeqgppg ptgpqgpigq pgpsgadgep
     1201 gprgqqglfg qkgdegprgf pgppgpvglq glpgppgekg etgdvgqmgp pgppgprgps
     1261 gapgadgpqg ppggignpga vgekgepgea gepglpgegg ppgpkgerge kgesgpsgaa
     1321 gppgpkgppg ddgpkgspgp vgfpgdpgpp gepgpagqdg ppgdkgddge pgqtgspgpt
     1381 gepgpsgppg krgppgpagp egrqgekgak geaglegppg ktgpigpqga pgkpgpdglr
     1441 gipgpvgeqg lpgspgpdgp pgpmgppglp glkgdsgpkg ekghpgligl igppgeqgek
     1501 gdrglpgpqg ssgpkgeqgi tgpsgpigpp gppglpgppg pkgakgssgp tgpkgeaghp
     1561 gppgppgppg eviqplpiqa srtrrnidas qllddgngen yvdyadgmee ifgslnslkl
     1621 eieqmkrplg tqqnpartck dlqlchpdfp dgeywvdpnq gcsrdsfkvy cnftaggstc
     1681 vfpdkksegs kmarwpkeqp stwysqykrg sllsyvdaeg npvgvvqmtf lrllsasahq
     1741 nvtyhcyqsv awqdaatgsy dkalrflgsn deemsydnnp yiralvdgca tkkgyqktvl
     1801 eidtpkveqv pivdimfndf geasqkfgfe vgpacfmg
//
LOCUS       NP_060369                214 aa            linear   PRI 20-NOV-2025
DEFINITION  calcineurin B homologous protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_060369
VERSION     NP_060369.3
DBSOURCE    REFSEQ: accession NM_017899.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 214)
  AUTHORS   Dong,Y., Fan,B., Li,M., Zhang,J., Xie,S., Di,S., Jia,Q. and Gong,T.
  TITLE     TESC acts as a prognostic factor and promotes
            epithelial-mesenchymal transition progression in esophageal
            squamous carcinoma
  JOURNAL   Pathol Res Pract 253, 154964 (2024)
   PUBMED   38000203
  REMARK    GeneRIF: TESC acts as a prognostic factor and promotes
            epithelial-mesenchymal transition progression in esophageal
            squamous carcinoma.
REFERENCE   2  (residues 1 to 214)
  AUTHORS   Dong,Y., Li,H., Ilie,A., Gao,Y., Boucher,A., Zhang,X.C.,
            Orlowski,J. and Zhao,Y.
  TITLE     Structural basis of autoinhibition of the human NHE3-CHP1 complex
  JOURNAL   Sci Adv 8 (21), eabn3925 (2022)
   PUBMED   35613257
REFERENCE   3  (residues 1 to 214)
  AUTHORS   Dong,Y., Gao,Y., Ilie,A., Kim,D., Boucher,A., Li,B., Zhang,X.C.,
            Orlowski,J. and Zhao,Y.
  TITLE     Structure and mechanism of the human NHE1-CHP1 complex
  JOURNAL   Nat Commun 12 (1), 3474 (2021)
   PUBMED   34108458
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 214)
  AUTHORS   Zhang,R., Yang,F., Fan,H., Wang,H., Wang,Q., Yang,J. and Song,T.
  TITLE     Long non-coding RNA TUG1/microRNA-187-3p/TESC axis modulates
            progression of pituitary adenoma via regulating the NF-kappaB
            signaling pathway
  JOURNAL   Cell Death Dis 12 (6), 524 (2021)
   PUBMED   34021124
  REMARK    GeneRIF: Long non-coding RNA TUG1/microRNA-187-3p/TESC axis
            modulates progression of pituitary adenoma via regulating the
            NF-kappaB signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 214)
  AUTHORS   Zhou,Z.G., Chen,J.B., Zhang,R.X., Ye,L., Wang,J.C., Pan,Y.X.,
            Wang,X.H., Li,W.X., Zhang,Y.J., Xu,L. and Chen,M.S.
  TITLE     Tescalcin is an unfavorable prognosis factor that regulats cell
            proliferation and survival in hepatocellular carcinoma patients
  JOURNAL   Cancer Commun (Lond) 40 (8), 355-369 (2020)
   PUBMED   32609436
  REMARK    GeneRIF: Tescalcin is an unfavorable prognosis factor that regulats
            cell proliferation and survival in hepatocellular carcinoma
            patients.
REFERENCE   6  (residues 1 to 214)
  AUTHORS   Levay,K. and Slepak,V.Z.
  TITLE     Tescalcin is an essential factor in megakaryocytic differentiation
            associated with Ets family gene expression
  JOURNAL   J Clin Invest 117 (9), 2672-2683 (2007)
   PUBMED   17717601
REFERENCE   7  (residues 1 to 214)
  AUTHORS   Gutierrez-Ford,C., Levay,K., Gomes,A.V., Perera,E.M., Som,T.,
            Kim,Y.M., Benovic,J.L., Berkovitz,G.D. and Slepak,V.Z.
  TITLE     Characterization of tescalcin, a novel EF-hand protein with a
            single Ca2+-binding site: metal-binding properties, localization in
            tissues and cells, and effect on calcineurin
  JOURNAL   Biochemistry 42 (49), 14553-14565 (2003)
   PUBMED   14661968
REFERENCE   8  (residues 1 to 214)
  AUTHORS   Li,X., Liu,Y., Kay,C.M., Muller-Esterl,W. and Fliegel,L.
  TITLE     The Na+/H+ exchanger cytoplasmic tail: structure, function, and
            interactions with tescalcin
  JOURNAL   Biochemistry 42 (24), 7448-7456 (2003)
   PUBMED   12809501
REFERENCE   9  (residues 1 to 214)
  AUTHORS   Mailander,J., Muller-Esterl,W. and Dedio,J.
  TITLE     Human homolog of mouse tescalcin associates with Na(+)/H(+)
            exchanger type-1
  JOURNAL   FEBS Lett 507 (3), 331-335 (2001)
   PUBMED   11696366
REFERENCE   10 (residues 1 to 214)
  AUTHORS   Perera,E.M., Martin,H., Seeherunvong,T., Kos,L., Hughes,I.A.,
            Hawkins,J.R. and Berkovitz,G.D.
  TITLE     Tescalcin, a novel gene encoding a putative EF-hand Ca(2+)-binding
            protein, Col9a3, and renin are expressed in the mouse testis during
            the early stages of gonadal differentiation
  JOURNAL   Endocrinology 142 (1), 455-463 (2001)
   PUBMED   11145610
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB452909.1, BC015221.1 and AI372964.1.
            
            On Dec 1, 2009 this sequence version replaced NP_060369.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC015221.1, SRR14038193.1622048.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335209.12/ ENSP00000334785.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.22"
     Protein         1..214
                     /product="calcineurin B homologous protein 3 isoform 1"
                     /note="calcineurin B homologous protein 3;
                     calcineurin-like EF hand protein 3"
                     /calculated_mol_wt=24619
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BS2.3)"
     Region          <81..>150
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          114..>142
                     /region_name="EFh"
                     /note="EF-hand, calcium binding motif; A diverse
                     superfamily of calcium sensors and calcium signal
                     modulators; most examples in this alignment model have 2
                     active canonical EF hands. Ca2+ binding induces a
                     conformational change in the EF-hand motif, leading to...;
                     cl08302"
                     /db_xref="CDD:415501"
     CDS             1..214
                     /gene="TESC"
                     /gene_synonym="CHP3; TSC"
                     /coded_by="NM_017899.4:135..779"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9183.3"
                     /db_xref="GeneID:54997"
                     /db_xref="HGNC:HGNC:26065"
                     /db_xref="MIM:611585"
ORIGIN      
        1 mgaahsasee vrelegktgf ssdqieqlhr rfkqlsgdqp tirkenfnnv pdlelnpirs
       61 kivraffdnr nlrkgpsgla deinfedflt imsyfrpidt tmdeeqvels rkeklrflfh
      121 mydsdsdgri tleeyrnvve ellsgnphie kesarsiadg ammeaasvcm gqmepdqvye
      181 gitfedflki wqgidietkm hvrflnmetm alch
//
LOCUS       NP_835224                696 aa            linear   PRI 20-NOV-2025
DEFINITION  SEC14 domain and spectrin repeat-containing protein 1 [Homo
            sapiens].
ACCESSION   NP_835224
VERSION     NP_835224.3
DBSOURCE    REFSEQ: accession NM_178123.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Fujiwara,S., Matsui,T.S., Ohashi,K., Deguchi,S. and Mizuno,K.
  TITLE     Solo, a RhoA-targeting guanine nucleotide exchange factor, is
            critical for hemidesmosome formation and acinar development in
            epithelial cells
  JOURNAL   PLoS One 13 (4), e0195124 (2018)
   PUBMED   29672603
  REMARK    GeneRIF: Solo plays a crucial role in HD formation and acinar
            development in epithelial cells by regulating mechanical
            force-induced RhoA activation and keratin filament organization.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Fujiwara,S., Ohashi,K., Mashiko,T., Kondo,H. and Mizuno,K.
  TITLE     Interplay between Solo and keratin filaments is crucial for
            mechanical force-induced stress fiber reinforcement
  JOURNAL   Mol Biol Cell 27 (6), 954-966 (2016)
   PUBMED   26823019
  REMARK    GeneRIF: The interplay between Solo protein and keratin 8/keratin
            18 filaments plays a crucial role in tensile force-induced RhoA
            activation and consequent actin cytoskeletal reinforcement in
            endothelial cells.
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Slonchak,A., Shannon,R.P., Pali,G. and Khromykh,A.A.
  TITLE     Human MicroRNA miR-532-5p Exhibits Antiviral Activity against West
            Nile Virus via Suppression of Host Genes SESTD1 and TAB3 Required
            for Virus Replication
  JOURNAL   J Virol 90 (5), 2388-2402 (2015)
   PUBMED   26676784
  REMARK    GeneRIF: Upregulation of miR-532-5p and subsequent suppression of
            the SESTD1 and TAB3 genes represent an antiviral response aimed at
            limiting West Nile virus infection.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Kamboh,M.I., Wang,X., Kao,A.H., Barmada,M.M., Clarke,A.,
            Ramsey-Goldman,R., Manzi,S. and Demirci,F.Y.
  TITLE     Genome-wide association study of antiphospholipid antibodies
  JOURNAL   Autoimmune Dis 2013, 761046 (2013)
   PUBMED   23509613
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Miehe,S., Bieberstein,A., Arnould,I., Ihdene,O., Rutten,H. and
            Strubing,C.
  TITLE     The phospholipid-binding protein SESTD1 is a novel regulator of the
            transient receptor potential channels TRPC4 and TRPC5
  JOURNAL   J Biol Chem 285 (16), 12426-12434 (2010)
   PUBMED   20164195
  REMARK    GeneRIF: SESTD1 was found to associate with TRPC4 and TRPC5 via the
            channel's calmodulin- and inositol 1,4,5-trisphosphate
            receptor-binding domain.
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 696)
  AUTHORS   Sato,T. and Mishina,M.
  TITLE     Representational difference analysis, high-resolution physical
            mapping, and transcript identification of the zebrafish genomic
            region for a motor behavior
  JOURNAL   Genomics 82 (2), 218-229 (2003)
   PUBMED   12837271
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093911.2, BC047578.1, AY209190.1, AK096232.1 and AC016755.6.
            
            On May 17, 2008 this sequence version replaced NP_835224.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038194.3673092.1, BC047578.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428443.8/ ENSP00000415332.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31.2"
     Protein         1..696
                     /product="SEC14 domain and spectrin repeat-containing
                     protein 1"
                     /note="huntingtin-interacting protein-like protein;
                     protein Solo; SEC14 and spectrin domains 1"
                     /calculated_mol_wt=79218
     Region          33..153
                     /region_name="CRAL_TRIO_2"
                     /note="Divergent CRAL/TRIO domain; pfam13716"
                     /db_xref="CDD:463965"
     Region          273..478
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Region          275..378
                     /region_name="Spectrin 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     Region          381..494
                     /region_name="Spectrin 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     Region          413..605
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            496..501
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          500..602
                     /region_name="Spectrin 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VW0.2)"
     CDS             1..696
                     /gene="SESTD1"
                     /gene_synonym="Solo"
                     /coded_by="NM_178123.5:360..2450"
                     /db_xref="CCDS:CCDS33338.1"
                     /db_xref="GeneID:91404"
                     /db_xref="HGNC:HGNC:18379"
                     /db_xref="MIM:621011"
ORIGIN      
        1 measvilpil kkklaflsgg kdrrsglilt iplcleqtnm delsvtldyl lsipsekcka
       61 rgftvivdgr ksqwnvvktv vvmlqnvvpa evslvcvvkp defwdkkvth fcfwkekdrl
      121 gfevilvsan kltryiepcq ltedfggslt ydhmdwlnkr lvfekftkes tslldelali
      181 nngsdkgnqq ekersvdlnf lpsvdpetvl qtghellsel qqrrfngsdg gvswspmdde
      241 llaqpqvmkl ldslreqytr yqevcrqrsk rtqleeiqqk vmqvvnwleg pgseqlraqw
      301 gigdsirasq alqqkheeie sqhsewfavy velnqqiaal lnagdeedlv elkslqqqls
      361 dvcyrqasql efrqnllqaa lefhgvaqdl sqqldgllgm lcvdvapadg asiqqtlkll
      421 eeklksvdvg lqglrekgqg lldqisnqas waygkdvtie nkenvdhiqg vmedmqlrkq
      481 rcedmvdvrr lkmlqmvqlf kceedaaqav ewlselldal lkthirlgdd aqetkvllek
      541 hrkfvdvaqs tydygrqllq atvvlcqslr ctsrssgdtl prlnrvwkqf tiaseervhr
      601 lemaiafhsn aekilqdcpe epeaindeeq fdeieavgks lldrltvpvv ypdgteqyfg
      661 spsdmastae nirdrmklvn lkrqqlrhpe mvttes
//
LOCUS       NP_005137                800 aa            linear   PRI 20-NOV-2025
DEFINITION  U4/U6.U5 tri-snRNP-associated protein 1 [Homo sapiens].
ACCESSION   NP_005137
VERSION     NP_005137.1
DBSOURCE    REFSEQ: accession NM_005146.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 800)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 800)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   3  (residues 1 to 800)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   4  (residues 1 to 800)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 800)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 800)
  AUTHORS   Ishida,H., Komiya,S., Inoue,Y., Yutani,S., Inoue,A. and Itoh,K.
  TITLE     Expression of the SART1 tumor-rejection antigen in human
            osteosarcomas
  JOURNAL   Int J Oncol 17 (1), 29-32 (2000)
   PUBMED   10853014
REFERENCE   7  (residues 1 to 800)
  AUTHORS   Matsunaga,K., Nakao,M., Masuoka,K., Inoue,Y., Gouhara,R.,
            Imaizumi,T., Nishizaka,S. and Itoh,K.
  TITLE     Cytokines required for induction of histocompatibility leukocyte
            antigen-class I-restricted and tumor-specific cytotoxic T
            lymphocytes by a SART1-derived peptide
  JOURNAL   Jpn J Cancer Res 90 (9), 1007-1015 (1999)
   PUBMED   10551332
REFERENCE   8  (residues 1 to 800)
  AUTHORS   Kikuchi,M., Nakao,M., Inoue,Y., Matsunaga,K., Shichijo,S.,
            Yamana,H. and Itoh,K.
  TITLE     Identification of a SART-1-derived peptide capable of inducing
            HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes
  JOURNAL   Int J Cancer 81 (3), 459-466 (1999)
   PUBMED   10209962
REFERENCE   9  (residues 1 to 800)
  AUTHORS   Valenta,R., Natter,S., Seiberler,S., Wichlas,S., Maurer,D.,
            Hess,M., Pavelka,M., Grote,M., Ferreira,F., Szepfalusi,Z.,
            Valent,P. and Stingl,G.
  TITLE     Molecular characterization of an autoallergen, Hom s 1, identified
            by serum IgE from atopic dermatitis patients
  JOURNAL   J Invest Dermatol 111 (6), 1178-1183 (1998)
   PUBMED   9856836
REFERENCE   10 (residues 1 to 800)
  AUTHORS   Shichijo,S., Nakao,M., Imai,Y., Takasu,H., Kawamoto,M., Niiya,F.,
            Yang,D., Toh,Y., Yamana,H. and Itoh,K.
  TITLE     A gene encoding antigenic peptides of human squamous cell carcinoma
            recognized by cytotoxic T lymphocytes
  JOURNAL   J Exp Med 187 (3), 277-288 (1998)
   PUBMED   9449708
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU136920.1, AB006198.1 and
            AP006287.2.
            
            Summary: This gene encodes two proteins, the SART1(800) protein
            expressed in the nucleus of the majority of proliferating cells,
            and the SART1(259) protein expressed in the cytosol of epithelial
            cancers. The SART1(259) protein is translated by the mechanism of
            -1 frameshifting during posttranscriptional regulation; its
            full-length sequence is not published yet. The two encoded proteins
            are thought to be involved in the regulation of proliferation. Both
            proteins have tumor-rejection antigens. The SART1(259) protein
            possesses tumor epitopes capable of inducing HLA-A2402-restricted
            cytotoxic T lymphocytes in cancer patients. This SART1(259) antigen
            may be useful in specific immunotherapy for cancer patients and may
            serve as a paradigmatic tool for the diagnosis and treatment of
            patients with atopy. The SART1(259) protein is found to be
            essential for the recruitment of the tri-snRNP to the
            pre-spliceosome in the spliceosome assembly pathway. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.130432.1,
                                           SRR1660807.226377.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312397.10/ ENSP00000310448.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..800
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..800
                     /product="U4/U6.U5 tri-snRNP-associated protein 1"
                     /note="squamous cell carcinoma antigen recognised by T
                     cells; small nuclear ribonucleoprotein 110kDa (U4/U6.U5);
                     U4/U6.U5 tri-snRNP-associated 110 kDa protein; IgE
                     autoantigen; SART1(259) protein; SART1(800) protein;
                     squamous cell carcinoma antigen recognized by T-cells 1;
                     hypoxia associated factor; SART-1; hSnu66; hSART-1; SNU66
                     homolog; SART1, U4/U6.U5 tri-snRNP-associated protein 1"
                     /calculated_mol_wt=90124
     Region          1..120
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Region          117..137
                     /region_name="HIND"
                     /note="HIND motif; pfam19252"
                     /db_xref="CDD:466011"
     Region          165..753
                     /region_name="SART-1"
                     /note="SART-1 family; pfam03343"
                     /db_xref="CDD:460888"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z315; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          311..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          419..497
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Region          571..604
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43290.1)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            695
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O43290.1)"
     CDS             1..800
                     /gene="SART1"
                     /gene_synonym="Ara1; HAF; HOMS1; SART1259; SNRNP110;
                     Snu66"
                     /coded_by="NM_005146.5:48..2450"
                     /db_xref="CCDS:CCDS31611.1"
                     /db_xref="GeneID:9092"
                     /db_xref="HGNC:HGNC:10538"
                     /db_xref="MIM:605941"
ORIGIN      
        1 mgsskkhrge keaagttaaa gtggateqpp rhrehkkhkh rsggsggsgg errkrsrerg
       61 gergsgrrga eaearssthg rersqaepse rrvkrekrdd gyeaaasskt ssgdasslsi
      121 eetnklrakl glkplevnai kkeagtkeep vtadvinpma lrqreelrek laaakekrll
      181 nqklgkiktl geddpwlddt aawiersrql qkekdlaekr aklleemdqe fgvstlveee
      241 fgqrrqdlys ardlqgltve haidsfrege tmiltlkdkg vlqeeedvlv nvnlvdkera
      301 eknvelrkkk pdylpyaede svddlaqqkp rsilskydee legerphsfr leqggtadgl
      361 rereleeira klrlqaqsls tvgprlasey ltpeemvtfk ktkrrvkkir kkekevvvra
      421 ddllplgdqt qdgdfgsrlr grgrrrvsev eeekepvpqp lpsddtrven mdisdeeegg
      481 apppgspqvl eedeaelelq kqlekgrrlr qlqqlqqlrd sgekvveivk klesrqrgwe
      541 ededperkga ivfnatsefc rtlgeiptyg lagnreeqee lmdferdeer sanggsesdg
      601 eenigwstvn ldeekqqqdf sassttilde epivnrglaa alllcqnkgl lettvqkvar
      661 vkapnkslps avyciedkma iddkysrree yrgftqdfke kdgykpdvki eyvdetgrkl
      721 tpkeafrqls hrfhgkgsgk mkterrmkkl deeallkkms ssdtplgtva llqekqkaqk
      781 tpyivlsgsg ksmnantitk
//
LOCUS       NP_001182447             476 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium uptake protein 1, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001182447
VERSION     NP_001182447.1
DBSOURCE    REFSEQ: accession NM_001195518.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Hasan,P., Berezhnaya,E., Rodriguez-Prados,M., Weaver,D.,
            Bekeova,C., Cartes-Saavedra,B., Birch,E., Beyer,A.M., Santos,J.H.,
            Seifert,E.L., Elrod,J.W. and Hajnoczky,G.
  TITLE     MICU1 and MICU2 control mitochondrial calcium signaling in the
            mammalian heart
  JOURNAL   Proc Natl Acad Sci U S A 121 (35), e2402491121 (2024)
   PUBMED   39163336
  REMARK    GeneRIF: MICU1 and MICU2 control mitochondrial calcium signaling in
            the mammalian heart.
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Rodriguez-Prados,M., Berezhnaya,E., Castromonte,M.T.,
            Menezes-Filho,S.L., Paillard,M. and Hajnoczky,G.
  TITLE     MICU1 occludes the mitochondrial calcium uniporter in divalent-free
            conditions
  JOURNAL   Proc Natl Acad Sci U S A 120 (19), e2218999120 (2023)
   PUBMED   37126688
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Tomar,D., Thomas,M., Garbincius,J.F., Kolmetzky,D.W., Salik,O.,
            Jadiya,P., Joseph,S.K., Carpenter,A.C., Hajnoczky,G. and Elrod,J.W.
  TITLE     MICU1 regulates mitochondrial cristae structure and function
            independently of the mitochondrial Ca2+ uniporter channel
  JOURNAL   Sci Signal 16 (782), eabi8948 (2023)
   PUBMED   37098122
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Mallilankaraman,K., Doonan,P., Cardenas,C., Chandramoorthy,H.C.,
            Muller,M., Miller,R., Hoffman,N.E., Gandhirajan,R.K., Molgo,J.,
            Birnbaum,M.J., Rothberg,B.S., Mak,D.O., Foskett,J.K. and Madesh,M.
  TITLE     MICU1 is an essential gatekeeper for MCU-mediated mitochondrial
            Ca(2+) uptake that regulates cell survival
  JOURNAL   Cell 151 (3), 630-644 (2012)
   PUBMED   23101630
  REMARK    GeneRIF: MICU1 is a gatekeeper of mitochondrial calcium
            uniporter-mediated Ca(2 )uptake that is essential to prevent [Ca(2
            )]overload and associated stress.
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Baughman,J.M., Perocchi,F., Girgis,H.S., Plovanich,M.,
            Belcher-Timme,C.A., Sancak,Y., Bao,X.R., Strittmatter,L.,
            Goldberger,O., Bogorad,R.L., Koteliansky,V. and Mootha,V.K.
  TITLE     Integrative genomics identifies MCU as an essential component of
            the mitochondrial calcium uniporter
  JOURNAL   Nature 476 (7360), 341-345 (2011)
   PUBMED   21685886
  REMARK    GeneRIF: MICU1 physically interacts with MCU, a principal component
            of the mitochondrial calcium uniporter.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Perocchi,F., Gohil,V.M., Girgis,H.S., Bao,X.R., McCombs,J.E.,
            Palmer,A.E. and Mootha,V.K.
  TITLE     MICU1 encodes a mitochondrial EF hand protein required for Ca(2+)
            uptake
  JOURNAL   Nature 467 (7313), 291-296 (2010)
   PUBMED   20693986
  REMARK    GeneRIF: MICU1 represents the founding member of a set of proteins
            required for high-capacity mitochondrial calcium uptake
            GeneRIF: MICU1 (CBARA1) is an EF-hand containing protein associated
            with the mitochondrial inner membrane.  It is required for
            mitochondrial calcium uptake in HeLa cells.
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Bordicchia,M., Battistoni,I., Mancinelli,L., Giannini,E., Refi,G.,
            Minardi,D., Muzzonigro,G., Mazzucchelli,R., Montironi,R.,
            Piscitelli,F., Petrosino,S., Dessi-Fulgheri,P., Rappelli,A., Di
            Marzo,V. and Sarzani,R.
  TITLE     Cannabinoid CB1 receptor expression in relation to visceral adipose
            depots, endocannabinoid levels, microvascular damage, and the
            presence of the Cnr1 A3813G variant in humans
  JOURNAL   Metabolism 59 (5), 734-741 (2010)
   PUBMED   19919870
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Natter,S., Seiberler,S., Hufnagl,P., Binder,B.R., Hirschl,A.M.,
            Ring,J., Abeck,D., Schmidt,T., Valent,P. and Valenta,R.
  TITLE     Isolation of cDNA clones coding for IgE autoantigens with serum IgE
            from atopic dermatitis patients
  JOURNAL   FASEB J 12 (14), 1559-1569 (1998)
   PUBMED   9806765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK023318.1, AL513185.12 and
            AC091769.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an essential regulator of mitochondrial
            Ca2+ uptake under basal conditions. The encoded protein interacts
            with the mitochondrial calcium uniporter, a mitochondrial inner
            membrane Ca2+ channel, and is essential in preventing mitochondrial
            Ca2+ overload, which can cause excessive production of reactive
            oxygen species and cell stress. Alternatively spliced transcript
            variants encoding different isoforms have been described. [provided
            by RefSeq, Mar 2013].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 5' coding region compared to variant 1. The encoded
            protein (isoform 2) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004216.2, AK225298.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000361114.10/
                                                  ENSP00000354415.5
            RefSeq Select criteria             :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..476
                     /product="calcium uptake protein 1, mitochondrial isoform
                     2"
                     /note="calcium uptake protein 1, mitochondrial;
                     calcium-binding atopy-related autoantigen 1; atopy-related
                     autoantigen CALC"
                     /calculated_mol_wt=50585
     transit_peptide 1..33
                     /note="Mitochondrion. /evidence=ECO:0000255,
                     ECO:0000305|PubMed:26387864; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=3784
     mat_peptide     34..476
                     /product="Calcium uptake protein 1, mitochondrial.
                     /id=PRO_0000322990"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
                     /calculated_mol_wt=50585
     Region          68..106
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          99..110
                     /region_name="Polybasic region.
                     /evidence=ECO:0000269|PubMed:27099988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCX5; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          126..129
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          222..441
                     /region_name="EFh_MICU1"
                     /note="EF-hand, calcium binding motif, found in calcium
                     uptake protein 1, mitochondrial (MICU1) and similar
                     proteins; cd16173"
                     /db_xref="CDD:320081"
     Region          222..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Site            order(224,376,379,382..383,385,403)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:320081"
     Site            order(231,233,235,242,421,423,425,432)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:320081"
     Region          259..263
                     /region_name="K/R-ring.
                     /evidence=ECO:0000269|PubMed:32494073"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Region          277..307
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          375..404
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          412..441
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320081"
     Region          455..465
                     /region_name="C-helix region.
                     /evidence=ECO:0000269|PubMed:24514027"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BPX6.1)"
     Site            455
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:27642082; propagated from
                     UniProtKB/Swiss-Prot (Q9BPX6.1)"
     CDS             1..476
                     /gene="MICU1"
                     /gene_synonym="ara CALC; CALC; CBARA1; EFHA3; MPXPS"
                     /coded_by="NM_001195518.2:72..1502"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55715.1"
                     /db_xref="GeneID:10367"
                     /db_xref="HGNC:HGNC:1530"
                     /db_xref="MIM:605084"
ORIGIN      
        1 mfrlnslsal aelavgsrwy hggsqpiqir rrlmmvaflg asavtastgl lwkrahaesp
       61 pcvdnlksdi gdkgknkdeg dvcnhekkta dlaphpeekk kkrsgfrdrk vmeyenrira
      121 ystpdkifry fatlkvisep geaevfmtpe dfvrsitpne kqpehlgldq yiikrfdgkk
      181 isqerekfad egsifytlge cglisfsdyi flttvlstpq rnfeiafkmf dlngdgevdm
      241 eefeqvqsii rsqtsmgmrh rdrpttgntl ksglcsaltt yffgadlkgk ltiknflefq
      301 rklqhdvlkl eferhdpvdg riterqfggm llaysgvqsk kltamqrqlk khfkegkglt
      361 fqevenfftf lknindvdta lsfyhmagas ldkvtmqqva rtvakvelsd hvcdvvfalf
      421 dcdgngelsn kefvsimkqr lmrglekpkd mgftrlmqam wkcaqetawd falpkq
//
LOCUS       NP_006751                184 aa            linear   PRI 20-NOV-2025
DEFINITION  uroplakin-2 precursor [Homo sapiens].
ACCESSION   NP_006751
VERSION     NP_006751.1
DBSOURCE    REFSEQ: accession NM_006760.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 184)
  AUTHORS   van Pel,D.M., Pors,J., Yuen,E., Chan,R., Kos,Z., Hayes,M.M. and
            Wang,G.
  TITLE     Distinct Uroplakin II Staining Pattern in Apocrine Breast Carcinoma
  JOURNAL   Appl Immunohistochem Mol Morphol 30 (10), 681-686 (2022)
   PUBMED   36227121
  REMARK    GeneRIF: Distinct Uroplakin II Staining Pattern in Apocrine Breast
            Carcinoma.
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Pryma,C., Villamil,C., Gibb,E.A., Oo,H.Z., Seiler,R.,
            Contreras-Sanz,A., Douglas,J., Black,P.C. and Wang,G.
  TITLE     Uroplakin II as a single marker for luminal versus basal molecular
            subtypes in muscle invasive urothelial carcinoma
  JOURNAL   Virchows Arch 481 (3), 397-403 (2022)
   PUBMED   35612672
  REMARK    GeneRIF: Uroplakin II as a single marker for luminal versus basal
            molecular subtypes in muscle invasive urothelial carcinoma.
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Leivo,M.Z., Tacha,D.E. and Hansel,D.E.
  TITLE     Expression of uroplakin II and GATA-3 in bladder cancer mimickers:
            caveats in the use of a limited panel to determine cell of origin
            in bladder lesions
  JOURNAL   Hum Pathol 113, 28-33 (2021)
   PUBMED   33887302
  REMARK    GeneRIF: Expression of uroplakin II and GATA-3 in bladder cancer
            mimickers: caveats in the use of a limited panel to determine cell
            of origin in bladder lesions.
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Yuasa,T., Yoshiki,T., Isono,T., Tanaka,T., Hayashida,H. and
            Okada,Y.
  TITLE     Expression of transitional cell-specific genes, uroplakin Ia and
            II, in bladder cancer: detection of circulating cancer cells in the
            peripheral blood of metastatic patients
  JOURNAL   Int J Urol 6 (6), 286-292 (1999)
   PUBMED   10404304
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Lobban,E.D., Smith,B.A., Hall,G.D., Harnden,P., Roberts,P.,
            Selby,P.J., Trejdosiewicz,L.K. and Southgate,J.
  TITLE     Uroplakin gene expression by normal and neoplastic human urothelium
  JOURNAL   Am J Pathol 153 (6), 1957-1967 (1998)
   PUBMED   9846985
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Wu,R.L., Osman,I., Wu,X.R., Lu,M.L., Zhang,Z.F., Liang,F.X.,
            Hamza,R., Scher,H., Cordon-Cardo,C. and Sun,T.T.
  TITLE     Uroplakin II gene is expressed in transitional cell carcinoma but
            not in bilharzial bladder squamous cell carcinoma: alternative
            pathways of bladder epithelial differentiation and tumor formation
  JOURNAL   Cancer Res 58 (6), 1291-1297 (1998)
   PUBMED   9515818
  REMARK    Erratum:[Cancer Res 1998 Jul 1;58(13):2904]
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wu,X.R., Lin,J.H., Walz,T., Haner,M., Yu,J., Aebi,U. and Sun,T.T.
  TITLE     Mammalian uroplakins. A group of highly conserved urothelial
            differentiation-related membrane proteins
  JOURNAL   J Biol Chem 269 (18), 13716-13724 (1994)
   PUBMED   8175808
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Lin,J.H., Wu,X.R., Kreibich,G. and Sun,T.T.
  TITLE     Precursor sequence, processing, and urothelium-specific expression
            of a major 15-kDa protein subunit of asymmetric unit membrane
  JOURNAL   J Biol Chem 269 (3), 1775-1784 (1994)
   PUBMED   7507484
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD556028.1 and Y13645.1.
            
            Summary: This gene encodes one of the proteins of the highly
            conserved urothelium-specific integral membrane proteins of the
            asymmetric unit membrane which forms urothelium apical plaques in
            mammals. The asymmetric unit membrane is believed to strengthen the
            urothelium by preventing cell rupture during bladder distention.
            The encoded protein is expressed in the peripheral blood of bladder
            cancer patients with transitional cell carcinomas.[provided by
            RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y13645.1, ERR279850.3032.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264031.3/ ENSP00000264031.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..184
                     /product="uroplakin-2 precursor"
                     /note="uroplakin II"
                     /calculated_mol_wt=16875
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2581
     Region          21..184
                     /region_name="Uroplakin_II"
                     /note="Uroplakin II; pfam07353"
                     /db_xref="CDD:462150"
     mat_peptide     26..184
                     /product="uroplakin-2"
                     /calculated_mol_wt=16875
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00526.2)"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00526.2)"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00526.2)"
     Site            156..176
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00526.2)"
     CDS             1..184
                     /gene="UPK2"
                     /gene_synonym="UP2; UPII"
                     /coded_by="NM_006760.4:54..608"
                     /db_xref="CCDS:CCDS8404.1"
                     /db_xref="GeneID:7379"
                     /db_xref="HGNC:HGNC:12579"
                     /db_xref="MIM:611558"
ORIGIN      
        1 mapllpirtl plilillall spgaadfnis slsgllspal tesllvalpp chltggnatl
       61 mvrrandskv vtssfvvppc rgrrelvsvv dsgagftvtr lsayqvtnlv pgtkfyisyl
      121 vkkgtatess reipmstlpr rnmesiglgm artggmvvit vllsvamfll vlgfiialal
      181 gsrk
//
LOCUS       NP_001291393              84 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein E isoform 2 [Homo sapiens].
ACCESSION   NP_001291393
VERSION     NP_001291393.1
DBSOURCE    REFSEQ: accession NM_001304464.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Wu,Q., Liao,R., Miao,C., Hasnat,M., Li,L., Sun,L., Wang,X.,
            Yuan,Z., Jiang,Z., Zhang,L. and Yu,Q.
  TITLE     Oncofetal SNRPE promotes HCC tumorigenesis by regulating the FGFR4
            expression through alternative splicing
  JOURNAL   Br J Cancer 131 (1), 77-89 (2024)
   PUBMED   38796598
  REMARK    GeneRIF: Oncofetal SNRPE promotes HCC tumorigenesis by regulating
            the FGFR4 expression through alternative splicing.
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 84)
  AUTHORS   Fautsch,M.P. and Wieben,E.D.
  TITLE     Transcriptional regulation of the small nuclear ribonucleoprotein E
            protein gene. Identification of cis-acting sequences with homology
            to genes encoding ribosomal proteins
  JOURNAL   J Biol Chem 266 (34), 23288-23295 (1991)
   PUBMED   1835977
REFERENCE   7  (residues 1 to 84)
  AUTHORS   Neiswanger,K., Stanford,D.R., Sparkes,R.S., Nishimura,D.,
            Mohandas,T., Klisak,I., Heinzmann,C. and Wieben,E.D.
  TITLE     Assignment of the gene for the small nuclear ribonucleoprotein E
            (SNRPE) to human chromosome 1q25-q43
  JOURNAL   Genomics 7 (4), 503-508 (1990)
   PUBMED   2143747
REFERENCE   8  (residues 1 to 84)
  AUTHORS   Sauterer,R.A., Goyal,A. and Zieve,G.W.
  TITLE     Cytoplasmic assembly of small nuclear ribonucleoprotein particles
            from 6 S and 20 S RNA-free intermediates in L929 mouse fibroblasts
  JOURNAL   J Biol Chem 265 (2), 1048-1058 (1990)
   PUBMED   1688550
REFERENCE   9  (residues 1 to 84)
  AUTHORS   Feeney,R.J., Sauterer,R.A., Feeney,J.L. and Zieve,G.W.
  TITLE     Cytoplasmic assembly and nuclear accumulation of mature small
            nuclear ribonucleoprotein particles
  JOURNAL   J Biol Chem 264 (10), 5776-5783 (1989)
   PUBMED   2522439
REFERENCE   10 (residues 1 to 84)
  AUTHORS   Stanford,D.R., Rohleder,A., Neiswanger,K. and Wieben,E.D.
  TITLE     DNA sequence of a human Sm autoimmune antigen. The multigene family
            contains a processed pseudogene
  JOURNAL   J Biol Chem 262 (21), 9931-9934 (1987)
   PUBMED   2440864
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC114402.2 and AC118554.2.
            
            Summary: The protein encoded by this gene is a core component of U
            small nuclear ribonucleoproteins, which are key components of the
            pre-mRNA processing spliceosome. The encoded protein plays a role
            in the 3' end processing of histone transcripts. This protein is
            one of the targets in the autoimmune disease systemic lupus
            erythematosus, and mutations in this gene have been associated with
            hypotrichosis. Several pseudogenes of this gene have been
            identified. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (2) uses two alternate splice
            junctions in the 5' end compared to variant 1. The resulting
            isoform (2) has a shorter and distinct N-terminus compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DC370543.1, AK307255.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..84
                     /product="small nuclear ribonucleoprotein E isoform 2"
                     /note="sm protein E"
                     /calculated_mol_wt=9573
     Region          11..81
                     /region_name="Sm_E"
                     /note="Sm protein E; cd01718"
                     /db_xref="CDD:212465"
     Site            order(16,28,30,33,40..43,47,55,64,66,68..72,75..81)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212465"
     Site            order(25..31,33..45,47..51)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212465"
     Site            order(43,45..47,72,74)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212465"
     Site            68..79
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212465"
     CDS             1..84
                     /gene="SNRPE"
                     /gene_synonym="HYPT11; Sm-E; SME; snRNP-E"
                     /coded_by="NM_001304464.2:130..384"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6635"
                     /db_xref="HGNC:HGNC:11161"
                     /db_xref="MIM:128260"
ORIGIN      
        1 msglgatvvq nlifrylqnr sriqvwlyeq vnmriegcii gfdeymnlvl ddaeeihskt
       61 ksrkqlgrim lkgdnitllq svsn
//
LOCUS       NP_001129284             221 aa            linear   PRI 20-NOV-2025
DEFINITION  SIN3-HDAC complex-associated factor [Homo sapiens].
ACCESSION   NP_001129284
VERSION     NP_001129284.1
DBSOURCE    REFSEQ: accession NM_001135812.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 221)
  AUTHORS   Jhuang,Y.L., Yang,C.W., Tseng,Y.F., Hsu,C.L., Li,H.Y., Yuan,R.H.
            and Jeng,Y.M.
  TITLE     SIN3-HDAC complex-associated factor, a chromatin remodelling gene
            located in the 12p amplicon, is a potential germ cell
            tumour-specific oncogene
  JOURNAL   J Pathol 258 (4), 353-365 (2022)
   PUBMED   36056608
  REMARK    GeneRIF: SIN3-HDAC complex-associated factor, a chromatin
            remodelling gene located in the 12p amplicon, is a potential germ
            cell tumour-specific oncogene.
REFERENCE   3  (residues 1 to 221)
  AUTHORS   Zhang,Y., Li,J.H., Yuan,Q.G. and Yang,W.B.
  TITLE     Restraint of FAM60A has a cancer-inhibiting role in pancreatic
            carcinoma via the effects on the Akt/GSK-3beta/beta-catenin
            signaling pathway
  JOURNAL   Environ Toxicol 37 (6), 1432-1444 (2022)
   PUBMED   35213078
  REMARK    GeneRIF: Restraint of FAM60A has a cancer-inhibiting role in
            pancreatic carcinoma via the effects on the
            Akt/GSK-3beta/beta-catenin signaling pathway.
REFERENCE   4  (residues 1 to 221)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 221)
  AUTHORS   Sun,Y.H., Sun,X.W., Yang,L., Cheng,B. and Chen,Y.L.
  TITLE     [Research Progress of FAM60A in the Regulation of Cellular
            Function]
  JOURNAL   Zhongguo Yi Xue Ke Xue Yuan Xue Bao 43 (3), 469-474 (2021)
   PUBMED   34238425
  REMARK    GeneRIF: [Research Progress of FAM60A in the Regulation of Cellular
            Function].
REFERENCE   6  (residues 1 to 221)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 221)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
REFERENCE   8  (residues 1 to 221)
  AUTHORS   Smith,K.T., Sardiu,M.E., Martin-Brown,S.A., Seidel,C.,
            Mushegian,A., Egidy,R., Florens,L., Washburn,M.P. and Workman,J.L.
  TITLE     Human family with sequence similarity 60 member A (FAM60A) protein:
            a new subunit of the Sin3 deacetylase complex
  JOURNAL   Mol Cell Proteomics 11 (12), 1815-1828 (2012)
   PUBMED   22984288
  REMARK    GeneRIF: studies reveal that loss of FAM60A or another component of
            the Sin3 complex, SDS3, leads to a change in cell morphology and an
            increase in cell migration
REFERENCE   9  (residues 1 to 221)
  AUTHORS   Munoz,I.M., MacArtney,T., Sanchez-Pulido,L., Ponting,C.P., Rocha,S.
            and Rouse,J.
  TITLE     Family with sequence similarity 60A (FAM60A) protein is a cell
            cycle-fluctuating regulator of the SIN3-HDAC1 histone deacetylase
            complex
  JOURNAL   J Biol Chem 287 (39), 32346-32353 (2012)
   PUBMED   22865885
  REMARK    GeneRIF: Family with sequence similarity 60A (FAM60A) protein is a
            cell cycle-fluctuating regulator of the SIN3-HDAC1 histone
            deacetylase complex.
REFERENCE   10 (residues 1 to 221)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA741767.1, AK026932.1, DR763430.1 and BC004462.1.
            
            Transcript Variant: This variant (3) lacks a segment in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026932.1, AF212220.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337682.9/ ENSP00000337477.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.21"
     Protein         1..221
                     /product="SIN3-HDAC complex-associated factor"
                     /note="tera protein homolog; protein FAM60A; family with
                     sequence similarity 60 member A"
                     /calculated_mol_wt=24721
     Region          2..198
                     /region_name="FAM60A"
                     /note="Protein Family FAM60A; pfam15396"
                     /db_xref="CDD:464703"
     Region          112..152
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     Region          201..221
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NP50.1)"
     CDS             1..221
                     /gene="SINHCAF"
                     /gene_synonym="C12orf14; FAM60A; L4; TERA"
                     /coded_by="NM_001135812.2:148..813"
                     /db_xref="CCDS:CCDS8723.1"
                     /db_xref="GeneID:58516"
                     /db_xref="HGNC:HGNC:30702"
                     /db_xref="MIM:615027"
ORIGIN      
        1 mfgfhkpkmy rsiegccicr akssssrftd skryekdfqs cfglhetrsg dicnacvllv
       61 krwkklpags kknwnhvvda ragpslkttl kpkkvktlsg nriksnqisk lqkefkrhns
      121 dahsttssas paqspcysnq sddgsdtema sgsnrtpvfs fldltywkrq kiccgiiykg
      181 rfgevlidth lfkpccsnkk aaaekpeeqg peplpistqe w
//
LOCUS       NP_005384               1909 aa            linear   PRI 20-NOV-2025
DEFINITION  plexin-B3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_005384
VERSION     NP_005384.2
DBSOURCE    REFSEQ: accession NM_005393.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1909)
  AUTHORS   Zuo,Q., Yang,Y., Lyu,Y., Yang,C., Chen,C., Salman,S., Huang,T.Y.,
            Wicks,E.E., Jackson,W. 3rd, Datan,E., Qin,W. and Semenza,G.L.
  TITLE     Plexin-B3 expression stimulates MET signaling, breast cancer stem
            cell specification, and lung metastasis
  JOURNAL   Cell Rep 42 (3), 112164 (2023)
   PUBMED   36857181
  REMARK    GeneRIF: Plexin-B3 expression stimulates MET signaling, breast
            cancer stem cell specification, and lung metastasis.
REFERENCE   2  (residues 1 to 1909)
  AUTHORS   Wang,K., He,M., Fan,X., Zhou,J., Yang,J., Wang,L., Zhao,Z., Dai,C.
            and Zhang,Z.
  TITLE     SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis Outgrowth through
            Enhancing the Warburg Effect
  JOURNAL   J Immunol Res 2023, 3274467 (2023)
   PUBMED   36741230
  REMARK    GeneRIF: SEMA5A-PLXNB3 Axis Promotes PDAC Liver Metastasis
            Outgrowth through Enhancing the Warburg Effect.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1909)
  AUTHORS   Kuhlmann,L., Govindarajan,M., Mejia-Guerrero,S., Ignatchenko,V.,
            Liu,L.Y., Grunwald,B.T., Cruickshank,J., Berman,H., Khokha,R. and
            Kislinger,T.
  TITLE     Glycoproteomics Identifies Plexin-B3 as a Targetable Cell Surface
            Protein Required for the Growth and Invasion of Triple-Negative
            Breast Cancer Cells
  JOURNAL   J Proteome Res 21 (9), 2224-2236 (2022)
   PUBMED   35981243
  REMARK    GeneRIF: Glycoproteomics Identifies Plexin-B3 as a Targetable Cell
            Surface Protein Required for the Growth and Invasion of
            Triple-Negative Breast Cancer Cells.
REFERENCE   4  (residues 1 to 1909)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 1909)
  AUTHORS   Nihonmatsu-Kikuchi,N., Yu,X.J., Matsuda,Y., Ozawa,N., Ito,T.,
            Satou,K., Kaname,T., Iwasaki,Y., Akagi,A., Yoshida,M., Toru,S.,
            Hirokawa,K., Takashima,A., Hasegawa,M., Uchihara,T. and
            Tatebayashi,Y.
  TITLE     Essential roles of plexin-B3+ oligodendrocyte precursor cells in
            the pathogenesis of Alzheimer's disease
  JOURNAL   Commun Biol 4 (1), 870 (2021)
   PUBMED   34267322
  REMARK    GeneRIF: Essential roles of plexin-B3(+) oligodendrocyte precursor
            cells in the pathogenesis of Alzheimer's disease.
            Erratum:[Commun Biol. 2021 Dec 2;4(1):1372. doi:
            10.1038/s42003-021-02905-5. PMID: 34857866]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1909)
  AUTHORS   Conrotto,P., Corso,S., Gamberini,S., Comoglio,P.M. and Giordano,S.
  TITLE     Interplay between scatter factor receptors and B plexins controls
            invasive growth
  JOURNAL   Oncogene 23 (30), 5131-5137 (2004)
   PUBMED   15184888
REFERENCE   7  (residues 1 to 1909)
  AUTHORS   Artigiani,S., Conrotto,P., Fazzari,P., Gilestro,G.F., Barberis,D.,
            Giordano,S., Comoglio,P.M. and Tamagnone,L.
  TITLE     Plexin-B3 is a functional receptor for semaphorin 5A
  JOURNAL   EMBO Rep 5 (7), 710-714 (2004)
   PUBMED   15218527
  REMARK    GeneRIF: Plexin-B3 is a functional receptor for semaphorin 5A
REFERENCE   8  (residues 1 to 1909)
  AUTHORS   Perrot,V., Vazquez-Prado,J. and Gutkind,J.S.
  TITLE     Plexin B regulates Rho through the guanine nucleotide exchange
            factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF
  JOURNAL   J Biol Chem 277 (45), 43115-43120 (2002)
   PUBMED   12183458
REFERENCE   9  (residues 1 to 1909)
  AUTHORS   Tamagnone,L., Artigiani,S., Chen,H., He,Z., Ming,G.I., Song,H.,
            Chedotal,A., Winberg,M.L., Goodman,C.S., Poo,M., Tessier-Lavigne,M.
            and Comoglio,P.M.
  TITLE     Plexins are a large family of receptors for transmembrane,
            secreted, and GPI-anchored semaphorins in vertebrates
  JOURNAL   Cell 99 (1), 71-80 (1999)
   PUBMED   10520995
  REMARK    Erratum:[Cell 2001 Jan 26;104(2):following 320]
REFERENCE   10 (residues 1 to 1909)
  AUTHORS   Sandoval,N., Bauer,D., Brenner,V., Coy,J.F., Drescher,B.,
            Kioschis,P., Korn,B., Nyakatura,G., Poustka,A., Reichwald,K.,
            Rosenthal,A. and Platzer,M.
  TITLE     The genomic organization of a human creatine transporter (CRTR)
            gene located in Xq28
  JOURNAL   Genomics 35 (2), 383-385 (1996)
   PUBMED   8661155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK292535.1, AF149019.1 and
            AK295762.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 28, 2003 this sequence version replaced NP_005384.1.
            
            Summary: The protein encoded by this gene is a member of the plexin
            family. It functions as a receptor for semaphorin 5A, and plays a
            role in axon guidance, invasive growth and cell migration.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Sep
            2009].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292535.1, AB033032.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361971.10/ ENSP00000355378.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1909
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..1909
                     /product="plexin-B3 isoform 1 precursor"
                     /note="plexin 6"
                     /calculated_mol_wt=202134
     sig_peptide     1..43
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4732
     Region          47..472
                     /region_name="Sema_plexin_B3"
                     /note="The Sema domain, a protein interacting module, of
                     Plexin B3; cd11277"
                     /db_xref="CDD:200538"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Site            order(99..101,218,223,228..229,251,360..361,368,373..375)
                     /site_type="other"
                     /note="putative Semaphorin binding site [polypeptide
                     binding]"
                     /db_xref="CDD:200538"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          474..525
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          533..619
                     /region_name="TIG_plexin"
                     /note="TIG domain; pfam17960"
                     /db_xref="CDD:465588"
     Site            615
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          633..667
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          689..786
                     /region_name="TIG_2"
                     /note="TIG domain found in plexin; pfam18020"
                     /db_xref="CDD:465619"
     Site            802
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          835..926
                     /region_name="IPT_plexin_repeat1"
                     /note="First repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01180"
                     /db_xref="CDD:238585"
     Site            900
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          927..1012
                     /region_name="IPT_plexin_repeat2"
                     /note="Second repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01179"
                     /db_xref="CDD:238584"
     Site            957
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          1015..1146
                     /region_name="IPT"
                     /note="Immunoglobulin-like fold, Plexins, Transcription
                     factors (IPT). IPTs are also known as Transcription factor
                     ImmunoGlobin (TIG) domains. They are present in
                     intracellular transcription factors, cell surface
                     receptors (such as plexins and scatter factor...; cl15674"
                     /db_xref="CDD:472823"
     Site            1101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          <1176..1242
                     /region_name="TIG"
                     /note="IPT/TIG domain; pfam01833"
                     /db_xref="CDD:460355"
     Site            1218
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Site            1256..1276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULL4.2)"
     Region          1327..1871
                     /region_name="Plexin_cytopl"
                     /note="Plexin cytoplasmic RasGAP domain; pfam08337"
                     /db_xref="CDD:462434"
     CDS             1..1909
                     /gene="PLXNB3"
                     /gene_synonym="PLEXB3; PLEXR; PLXN6"
                     /coded_by="NM_005393.3:122..5851"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14729.1"
                     /db_xref="GeneID:5365"
                     /db_xref="HGNC:HGNC:9105"
                     /db_xref="MIM:300214"
ORIGIN      
        1 mchaaqetpl lhhfmapvma rwppfglcll llllsppplp ltgahrfsap nttlnhlala
       61 pgrgtlyvga vnrlfqlspe lqleavavtg pvidspdcvp frdpaecpqa qltdnanqll
      121 lvssraqelv acgqvrqgvc etrrlgdvae vlyqaedpgd gqfvaantpg vatvglvvpl
      181 pgrdlllvar glagklsagv pplairqlag sqpfsseglg rlvvgdfsdy nnsyvgafad
      241 arsayfvfrr rgaraqaeyr syvarvclgd tnlysyvevp lacqgqgliq aaflapgtll
      301 gvfaagprgt qaalcafpmv elgasmeqar rlcytaggrg psgaeeatve ygvtsrcvtl
      361 pldspesypc gdehtpspia grqplevqpl lklgqpvsav aalqadghmi aflgdtqgql
      421 ykvflhgsqg qvyhsqqvgp pgsaispdll ldssgshlyv ltahqvdrip vaacpqfpdc
      481 asclqaqdpl cgwcvlqgrc trkgqcgrag qlnqwlwsye edshclhiqs llpghhprqe
      541 qgqvtlsvpr lpildadeyf hcafgdydsl ahvegphvac vtppqdqvpl nppgtdhvtv
      601 plalmfedvt vaatnfsfyd csavqaleaa apcracvgsi wrchwcpqss hcvygehcpe
      661 gertiysaqe vdiqvrgpga cpqveglagp hlvpvgwesh lalrvrnlqh frglpasfhc
      721 wlelpgelrg lpatleetag dsglihcqah qfypsmsqre lpvpiyvtqg eaqrldntha
      781 lyvilydcam ghpdcshcqa anrslgclwc adgqpacryg plcppgavel lcpapsidav
      841 epltgppegg laltilgsnl grafadvqya vsvasrpcnp epslyrtsar ivcvtspapn
      901 gttgpvrvai ksqppgissq hftyqdpvll slsprwgpqa ggtqltirgq hlqtggntsa
      961 fvggqpcpil epvcpeaivc rtrpqaapge aavlvvfgha qrtllaspfr ytanpqlvaa
     1021 epsasfrggg rlirvrgtgl dvvqrpllsv wleadaevqa sraqpqdpqp rrscgapaad
     1081 pqaciqlggg llqcstvcsv nssslllcrs pavpdrahpq rvfftldnvq vdfasasggq
     1141 gflyqpnprl aplsregpar pyrlkpghvl dvegeglnlg iskeevrvhi grgeclvktl
     1201 trthlycepp ahapqpangs glpqfvvqmg nvqlalgpvq yeaepplsaf pveaqagvgm
     1261 gaavliaavl lltlmyrhks kqalrdyqkv lvqlesletg vgdqcrkeft dlmtemtdls
     1321 sdlegsgipf ldyrtyaera ffpghggcpl qpkpegpged ghcatvrqgl tqlsnllnsk
     1381 lflltlihtl eeqpsfsqrd rchvasllsl alhgkleylt dimrtllgdl aahyvhrnpk
     1441 lmlrrtetmv eklltnwlsi clyaflreva geplymlfra iqyqvdkgpv davtgkakrt
     1501 lndsrllred vefqpltlmv lvgpgaggaa gssemqrvpa rvldtdtitq vkekvldqvy
     1561 kgtpfsqrps vhaldlewrs glaghltlsd edltsvtqnh wkrlntlqhy kvpdgatvgl
     1621 vpqlhrgsti sqslaqrcpl geniptledg eeggvclwhl vkateepega kvrcsslrer
     1681 eparakaipe iyltrllsmk gtlqkfvddt fqailsvnrp ipiavkylfd lldelaekhg
     1741 iedpgtlhiw ktnslllrfw vnalknpqli fdvrvsdnvd ailaviaqtf idscttsehk
     1801 vgrdspvnkl lyareipryk qmveryyadi rqsspasyqe mnsalaelsg nytsaphcle
     1861 alqelynhih ryydqiisal eedpvgqklq lacrlqqvaa lvenkvtdl
//
LOCUS       NP_001337618             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337618 XP_005250719
VERSION     NP_001337618.1
DBSOURCE    REFSEQ: accession NM_001350689.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 22, 2017 this sequence version replaced XP_005250719.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (25), as well as variants 1-4,
            9-24, and 26-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.55870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350689.1:678..2888"
                     /note="isoform 1 is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_115748                177 aa            linear   PRI 20-NOV-2025
DEFINITION  DPY30 domain-containing protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_115748
VERSION     NP_115748.1
DBSOURCE    REFSEQ: accession NM_032372.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Kuhl,A., Melberg,A., Meinl,E., Nurnberg,G., Nurnberg,P.,
            Kehrer-Sawatzki,H. and Jenne,D.E.
  TITLE     Myofibrillar myopathy with arrhythmogenic right ventricular
            cardiomyopathy 7: corroboration and narrowing of the critical
            region on 10q22.3
  JOURNAL   Eur J Hum Genet 16 (3), 367-373 (2008)
   PUBMED   18197198
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA590784.1, AK093378.1 and
            BC018606.2.
            
            Summary: This gene encodes a member of a family of proteins that
            contains a DPY30 domain. This gene locus overlaps with a closely
            related gene on the opposite strand. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (1) encodes isoform 1. Variants 1
            and 2 encode the same protein (isoform 1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK093378.1, SRR5189667.285203.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256039.3/ ENSP00000256039.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..177
                     /product="DPY30 domain-containing protein 2 isoform 1"
                     /note="DPY30 domain-containing protein 2"
                     /calculated_mol_wt=20455
     Region          2..45
                     /region_name="DD_DYDC-like"
                     /note="dimerization/docking (D/D) domain found in the
                     DPY30 domain-containing protein (DYDC)-like family;
                     cd22966"
                     /db_xref="CDD:438535"
     CDS             1..177
                     /gene="DYDC2"
                     /coded_by="NM_032372.6:208..741"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7367.1"
                     /db_xref="GeneID:84332"
                     /db_xref="HGNC:HGNC:23468"
ORIGIN      
        1 metnylkrcf gnclaqalae vakvrpsdpi eylahwlyhy rktakakeen rekkihlqee
       61 ydsslkemem temlkqeeyq iqqncekchk eltsetvstk ktifmqedtn plekealkqe
      121 flpgtsslip gmpqqvppse sagqidqnfk mpqeinykea fqhevahemp pgskspf
//
LOCUS       NP_002778                234 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-2 [Homo sapiens].
ACCESSION   NP_002778
VERSION     NP_002778.1
DBSOURCE    REFSEQ: accession NM_002787.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Zhang,Y., Xiang,Z., Chen,L., Deng,X., Liu,H. and Peng,X.
  TITLE     PSMA2 promotes glioma proliferation and migration via EMT
  JOURNAL   Pathol Res Pract 256, 155278 (2024)
   PUBMED   38574629
  REMARK    GeneRIF: PSMA2 promotes glioma proliferation and migration via EMT.
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Sher,A.A., Lao,Y.T. and Coombs,K.M.
  TITLE     HLA-A, HSPA5, IGFBP5 and PSMA2 Are Restriction Factors for Zika
            Virus Growth in Astrocytic Cells
  JOURNAL   Viruses 15 (1), 97 (2022)
   PUBMED   36680137
  REMARK    GeneRIF: HLA-A, HSPA5, IGFBP5 and PSMA2 Are Restriction Factors for
            Zika Virus Growth in Astrocytic Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Okumura,K., Nogami,M., Taguchi,H., Hisamatsu,H. and Tanaka,K.
  TITLE     The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1)
            subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13
            by fluorescence in situ hybridization
  JOURNAL   Genomics 27 (2), 377-379 (1995)
   PUBMED   7558012
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Tamura,T., Osaka,F., Kawamura,Y., Higuti,T., Ishida,N.,
            Nothwang,H.G., Tsurumi,C., Tanaka,K. and Ichihara,A.
  TITLE     Isolation and characterization of alpha-type HC3 and beta-type HC5
            subunit genes of human proteasomes
  JOURNAL   J Mol Biol 244 (1), 117-124 (1994)
   PUBMED   7966316
REFERENCE   9  (residues 1 to 234)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Tamura,T., Lee,D.H., Osaka,F., Fujiwara,T., Shin,S., Chung,C.H.,
            Tanaka,K. and Ichihara,A.
  TITLE     Molecular cloning and sequence analysis of cDNAs for five major
            subunits of human proteasomes (multi-catalytic proteinase
            complexes)
  JOURNAL   Biochim Biophys Acta 1089 (1), 95-102 (1991)
   PUBMED   2025653
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010132.5.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC047697.1, AK222976.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000223321.9/ ENSP00000223321.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.1"
     Protein         1..234
                     /product="proteasome subunit alpha type-2"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit HC3; proteasome component C3;
                     macropain subunit C3; multicatalytic endopeptidase complex
                     subunit C3; proteasome (prosome, macropain) subunit, alpha
                     type, 2; proteasome subunit alpha 2; alpha-2"
                     /calculated_mol_wt=25768
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Region          6..231
                     /region_name="proteasome_alpha_type_2"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03750"
                     /db_xref="CDD:239719"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P49722; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            order(8..11,13..14,16..17,21,24,27..28,31,39,54,56..57,
                     80..82,84..85,116,119,122..123,126..130,147,152..153,155,
                     157..158,160)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239719"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            order(33,49,51,64,165)
                     /site_type="active"
                     /db_xref="CDD:239719"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            121
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P17220; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P25787.2)"
     CDS             1..234
                     /gene="PSMA2"
                     /gene_synonym="HC3; MU; PMSA2; PSC2"
                     /coded_by="NM_002787.5:17..721"
                     /db_xref="CCDS:CCDS5467.1"
                     /db_xref="GeneID:5683"
                     /db_xref="HGNC:HGNC:9531"
                     /db_xref="MIM:176842"
ORIGIN      
        1 maergysfsl ttfspsgklv qieyalaava ggapsvgika angvvlatek kqksilyder
       61 svhkvepitk higlvysgmg pdyrvlvhra rklaqqyylv yqepiptaql vqrvasvmqe
      121 ytqsggvrpf gvsllicgwn egrpylfqsd psgayfawka tamgknyvng ktflekryne
      181 dleledaiht ailtlkesfe gqmtedniev gicneagfrr ltptevkdyl aaia
//
LOCUS       NP_001290548             181 aa            linear   PRI 20-NOV-2025
DEFINITION  CD226 antigen isoform b [Homo sapiens].
ACCESSION   NP_001290548
VERSION     NP_001290548.1
DBSOURCE    REFSEQ: accession NM_001303619.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 181)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 181)
  AUTHORS   Morandi,E., Adoue,V., Bernard,I., Friebel,E., Nunez,N., Aubert,Y.,
            Masson,F., Dejean,A.S., Becher,B., Astier,A., Martinet,L. and
            Saoudi,A.
  TITLE     Impact of the Multiple Sclerosis-Associated Genetic Variant CD226
            Gly307Ser on Human CD8 T-Cell Functions
  JOURNAL   Neurol Neuroimmunol Neuroinflamm 11 (6), e200306 (2024)
   PUBMED   39231385
  REMARK    GeneRIF: Impact of the Multiple Sclerosis-Associated Genetic
            Variant CD226 Gly307Ser on Human CD8 T-Cell Functions.
REFERENCE   3  (residues 1 to 181)
  AUTHORS   Baker,F.L., Smith,K.A., Mylabathula,P.L., Zuniga,T.M., Diak,D.M.,
            Batatinha,H., Niemiro,G.M., Seckeler,M.D., Pedlar,C.R.,
            O'Connor,D.P., Colombo,J., Katsanis,E. and Simpson,R.J.
  TITLE     Exercise-induced beta2-adrenergic Receptor Activation Enhances the
            Antileukemic Activity of Expanded gammadelta T-Cells via DNAM-1
            Upregulation and PVR/Nectin-2 Recognition
  JOURNAL   Cancer Res Commun 4 (5), 1253-1267 (2024)
   PUBMED   38592213
  REMARK    GeneRIF: Exercise-induced beta2-adrenergic Receptor Activation
            Enhances the Antileukemic Activity of Expanded gammadelta T-Cells
            via DNAM-1 Upregulation and PVR/Nectin-2 Recognition.
REFERENCE   4  (residues 1 to 181)
  AUTHORS   Kari,S., Bucciarelli,F., Angles,T., Oster,A.C., Cauboue,P.,
            Laviolette,K., Mougenot,M., Morandi,E., Bernard,I., Pignolet,B.,
            Bost,C., Thomas,J., Nogueira,L., Saoudi,A., Liblau,R. and
            Astier,A.L.
  TITLE     Increased levels of circulating soluble CD226 in multiple sclerosis
  JOURNAL   Mult Scler 30 (6), 654-663 (2024)
   PUBMED   38424741
  REMARK    GeneRIF: Increased levels of circulating soluble CD226 in multiple
            sclerosis.
REFERENCE   5  (residues 1 to 181)
  AUTHORS   Jian,J.L., Zhu,C.S., Xu,Z.W., Ouyang,W.M., Ma,D.C., Zhang,Y.,
            Chen,L.J., Yang,A.G. and Jin,B.Q.
  TITLE     Identification and characterization of the CD226 gene promoter
  JOURNAL   J Biol Chem 281 (39), 28731-28736 (2006)
   PUBMED   16887814
  REMARK    GeneRIF: CD226 promoters P1 and P2 are regulated by Ets-1 and AP-1
REFERENCE   6  (residues 1 to 181)
  AUTHORS   Shibuya,K., Shirakawa,J., Kameyama,T., Honda,S., Tahara-Hanaoka,S.,
            Miyamoto,A., Onodera,M., Sumida,T., Nakauchi,H., Miyoshi,H. and
            Shibuya,A.
  TITLE     CD226 (DNAM-1) is involved in lymphocyte function-associated
            antigen 1 costimulatory signal for naive T cell differentiation and
            proliferation
  JOURNAL   J Exp Med 198 (12), 1829-1839 (2003)
   PUBMED   14676297
  REMARK    GeneRIF: CD226 is involved in LFA-1-mediated costimulatory signals
            for triggering naive T cell differentiation and proliferation.
REFERENCE   7  (residues 1 to 181)
  AUTHORS   Kojima,H., Kanada,H., Shimizu,S., Kasama,E., Shibuya,K.,
            Nakauchi,H., Nagasawa,T. and Shibuya,A.
  TITLE     CD226 mediates platelet and megakaryocytic cell adhesion to
            vascular endothelial cells
  JOURNAL   J Biol Chem 278 (38), 36748-36753 (2003)
   PUBMED   12847109
  REMARK    GeneRIF: CD226 mediates platelet and megakaryocytic cell adhesion
            to vascular endothelial cells
REFERENCE   8  (residues 1 to 181)
  AUTHORS   Bottino,C., Castriconi,R., Pende,D., Rivera,P., Nanni,M.,
            Carnemolla,B., Cantoni,C., Grassi,J., Marcenaro,S., Reymond,N.,
            Vitale,M., Moretta,L., Lopez,M. and Moretta,A.
  TITLE     Identification of PVR (CD155) and Nectin-2 (CD112) as cell surface
            ligands for the human DNAM-1 (CD226) activating molecule
  JOURNAL   J Exp Med 198 (4), 557-567 (2003)
   PUBMED   12913096
  REMARK    GeneRIF: Data show that both PVR and Nectin-2 represent specific
            ligands for the DNAM-1 triggering receptor.
REFERENCE   9  (residues 1 to 181)
  AUTHORS   Shibuya,K., Lanier,L.L., Phillips,J.H., Ochs,H.D., Shimizu,K.,
            Nakayama,E., Nakauchi,H. and Shibuya,A.
  TITLE     Physical and functional association of LFA-1 with DNAM-1 adhesion
            molecule
  JOURNAL   Immunity 11 (5), 615-623 (1999)
   PUBMED   10591186
REFERENCE   10 (residues 1 to 181)
  AUTHORS   Shibuya,A., Campbell,D., Hannum,C., Yssel,H., Franz-Bacon,K.,
            McClanahan,T., Kitamura,T., Nicholl,J., Sutherland,G.R.,
            Lanier,L.L. and Phillips,J.H.
  TITLE     DNAM-1, a novel adhesion molecule involved in the cytolytic
            function of T lymphocytes
  JOURNAL   Immunity 4 (6), 573-581 (1996)
   PUBMED   8673704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from GU935336.1 and AC090231.7.
            
            Summary: This gene encodes a glycoprotein expressed on the surface
            of NK cells, platelets, monocytes and a subset of T cells. It is a
            member of the Ig-superfamily containing 2 Ig-like domains of the
            V-set. The protein mediates cellular adhesion of platelets and
            megakaryocytic cells to vascular endothelial cells. The protein
            also plays a role in megakaryocytic cell maturation. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jan 2015].
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (b) has a shorter N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GU935336.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.2"
     Protein         1..181
                     /product="CD226 antigen isoform b"
                     /note="platelet and T cell activation antigen 1; DNAX
                     accessory molecule-1; T lineage-specific activation
                     antigen 1 antigen; CD226 antigen; adhesion glycoprotein"
                     /calculated_mol_wt=20925
     Region          <28..80
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          49..53
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          64..69
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..181
                     /gene="CD226"
                     /gene_synonym="DNAM-1; DNAM1; PTA1; TLiSA1"
                     /coded_by="NM_001303619.2:129..674"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS77197.1"
                     /db_xref="GeneID:10666"
                     /db_xref="HGNC:HGNC:16961"
                     /db_xref="MIM:605397"
ORIGIN      
        1 mtwpvqavrw ekiqprqidl ltycnlvhgr nftskfprqi vsncshgrws vivipdvtvs
       61 dsglyrcylq asagenetfv mrltvaegkt dnqytlfvag gtvllllfvi sittiivifl
      121 nrrrrrerrd lfteswdtqk apnnyrspis tsqptnqsmd dtrediyvny ptfsrrpktr
      181 v
//
LOCUS       NP_001341634             943 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin heavy chain isoform 5A isoform 2 [Homo sapiens].
ACCESSION   NP_001341634
VERSION     NP_001341634.1
DBSOURCE    REFSEQ: accession NM_001354705.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Cozzi,M., Magri,S., Tedesco,B., Patelli,G., Ferrari,V.,
            Casarotto,E., Chierichetti,M., Pramaggiore,P., Cornaggia,L.,
            Piccolella,M., Galbiati,M., Rusmini,P., Crippa,V., Mandrioli,J.,
            Pareyson,D., Pisciotta,C., D'Arrigo,S., Ratti,A., Nanetti,L.,
            Mariotti,C., Sarto,E., Pensato,V., Gellera,C., Di Bella,D.,
            Cristofani,R.M., Taroni,F. and Poletti,A.
  TITLE     Altered molecular and cellular mechanisms in KIF5A-associated
            neurodegenerative or neurodevelopmental disorders
  JOURNAL   Cell Death Dis 15 (9), 692 (2024)
   PUBMED   39333504
  REMARK    GeneRIF: Altered molecular and cellular mechanisms in
            KIF5A-associated neurodegenerative or neurodevelopmental disorders.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Wang,H., Guan,L., Ma,X., Wang,Y., Wang,J., Zhang,P. and Deng,M.
  TITLE     Whole-Genome Sequencing Identified a Novel Mutation in the
            N-Terminal Domain of KIF5A in Chinese Patients with Familial
            Amyotrophic Lateral Sclerosis
  JOURNAL   Genes (Basel) 15 (6), 680 (2024)
   PUBMED   38927616
  REMARK    GeneRIF: Whole-Genome Sequencing Identified a Novel Mutation in the
            N-Terminal Domain of KIF5A in Chinese Patients with Familial
            Amyotrophic Lateral Sclerosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 943)
  AUTHORS   Carrington,G., Fatima,U., Caramujo,I., Lewis,T., Casas-Mao,D. and
            Peckham,M.
  TITLE     A multiscale approach reveals the molecular architecture of the
            autoinhibited kinesin KIF5A
  JOURNAL   J Biol Chem 300 (3), 105713 (2024)
   PUBMED   38309508
  REMARK    GeneRIF: A multiscale approach reveals the molecular architecture
            of the autoinhibited kinesin KIF5A.
REFERENCE   5  (residues 1 to 943)
  AUTHORS   Rahman,A., Kamal,A., Roberts,E.A. and Goldstein,L.S.
  TITLE     Defective kinesin heavy chain behavior in mouse kinesin light chain
            mutants
  JOURNAL   J Cell Biol 146 (6), 1277-1288 (1999)
   PUBMED   10491391
REFERENCE   6  (residues 1 to 943)
  AUTHORS   Reid,E., Dearlove,A.M., Rhodes,M. and Rubinsztein,D.C.
  TITLE     A new locus for autosomal dominant 'pure' hereditary spastic
            paraplegia mapping to chromosome 12q13, and evidence for further
            genetic heterogeneity
  JOURNAL   Am J Hum Genet 65 (3), 757-763 (1999)
   PUBMED   10441583
REFERENCE   7  (residues 1 to 943)
  AUTHORS   Rahman,A., Friedman,D.S. and Goldstein,L.S.
  TITLE     Two kinesin light chain genes in mice. Identification and
            characterization of the encoded proteins
  JOURNAL   J Biol Chem 273 (25), 15395-15403 (1998)
   PUBMED   9624122
  REMARK    Erratum:[J Biol Chem 1998 Sep 11;273(37):24280]
REFERENCE   8  (residues 1 to 943)
  AUTHORS   Hamlin,P.J., Jones,P.F., Leek,J.P., Bransfield,K., Lench,N.J.,
            Aldersley,M.A., Howdle,P.D., Markham,A.F. and Robinson,P.A.
  TITLE     Assignment of GALGT encoding beta-1,
            4N-acetylgalactosaminyl-transferase (GalNAc-T) and KIF5A encoding
            neuronal kinesin (D12S1889) to human chromosome band 12q13 by
            assignment to ICI YAC 26EG10 and in situ hybridization.
            medjph@stjames.leeds.ac.uk
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 267-268 (1998)
   PUBMED   9858832
REFERENCE   9  (residues 1 to 943)
  AUTHORS   Niclas,J., Navone,F., Hom-Booher,N. and Vale,R.D.
  TITLE     Cloning and localization of a conventional kinesin motor expressed
            exclusively in neurons
  JOURNAL   Neuron 12 (5), 1059-1072 (1994)
   PUBMED   7514426
REFERENCE   10 (residues 1 to 943)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294881.1, AC022506.38 and
            CB243285.1.
            
            Summary: This gene encodes a member of the kinesin family of
            proteins. Members of this family are part of a multisubunit complex
            that functions as a microtubule motor in intracellular organelle
            transport. Mutations in this gene cause autosomal dominant spastic
            paraplegia 10. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294881.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..943
                     /product="kinesin heavy chain isoform 5A isoform 2"
                     /EC_number="5.6.1.3"
                     /note="kinesin, heavy chain, neuron-specific; KIF5A
                     variant protein; neuronal kinesin heavy chain; kinesin
                     heavy chain neuron-specific 1; neuron-specific kinesin
                     heavy chain"
                     /calculated_mol_wt=107122
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q12840.2)"
     Region          7..238
                     /region_name="Motor_domain"
                     /note="Myosin and Kinesin motor domain; cl22853"
                     /db_xref="CDD:473979"
     Region          <320..831
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          743..812
                     /region_name="Khc_CBD_cc"
                     /note="cargo binding coiled-coil domain found in kinesin
                     heavy chains; cd23649"
                     /db_xref="CDD:467880"
     CDS             1..943
                     /gene="KIF5A"
                     /gene_synonym="ALS25; D12S1889; MY050; NEIMY; NKHC; SPG10"
                     /coded_by="NM_001354705.2:229..3060"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS86312.1"
                     /db_xref="GeneID:3798"
                     /db_xref="HGNC:HGNC:6323"
                     /db_xref="MIM:602821"
ORIGIN      
        1 maetnnecsi kvlcrfrpln qaeilrgdkf ipifqgddsv vigvsyfeiy ldkirdlldv
       61 tktnlsvhed knrvpfvkgc terfvsspee ildvidegks nrhvavtnmn ehssrshsif
      121 linikqenme teqklsgkly lvdlagsekv sktgaegavl deakninksl salgnvisal
      181 aegtksyvpy rdskmtrilq dslggncrtt mficcspssy ndaetkstlm fgqraktikn
      241 tasvnlelta eqwkkkyeke kektkaqket iakleaelsr wrngenvpet erlageeaal
      301 gaelceetpv ndnssivvri apeerqkyee eirrlykqld dkddeinqqs qlieklkqqm
      361 ldqeellvst rgdnekvqre lshlqsenda akdevkevlq aleelavnyd qksqeveeks
      421 qqnqllvdel sqkvatmlsl eselqrlqev sghqrkriae vlnglmkdls efsvivgnge
      481 iklpveisga ieeeftvarl yiskiksevk svvkrcrqle nlqvechrkm evtgrelssc
      541 qllisqheak irslteymqs velkkrhlee sydslsdela klqaqetvhe valkdkepdt
      601 qdadevkkal elqmeshrea hhrqlarlrd einekqktid elkdlnqklq leleklqady
      661 eklkseehek stklqeltfl yerheqskqd lkgleetvar elqtlhnlrk lfvqdvttrv
      721 kksaemeped sggihsqkqk isflennleq ltkvhkqlvr dnadlrcelp klekrlrata
      781 ervkalegal keakegamkd krryqqevdr ikeavrykss gkrghsaqia kpvrpghypa
      841 ssptnpygtr specisytns lfqnyqnlyl qatpsstsdm yfansctssg atssggplas
      901 yqkanmdngn atdindnrsd lpcgyeaedq aklfplhqet aas
//
LOCUS       NP_064730                592 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform b [Homo sapiens].
ACCESSION   NP_064730
VERSION     NP_064730.1
DBSOURCE    REFSEQ: accession NM_020325.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.131391.1,
                                           SRR1803616.113943.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..592
                     /product="lysosomal cobalamin transporter ABCD4 isoform b"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=66781
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Region          68..584
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            190..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            279..299
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     Site            314..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14678.1)"
     CDS             1..592
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_020325.3:23..1801"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mavagpapga garprldlqf lqrflqilkv lfpswssqna lmfltllclt lleqfviyqv
       61 glipsqyygv lgnkdlegfk tltflavmli vlnstlksfd qftcnllyvs wrkdltehlh
      121 rlyfrgrayy tlnvlrddid npdqrisqdv erfcrqlssm askliispft lvyytyqcfq
      181 stgwlgpvsi fgyfilgtvv nktlmgpivm klvhqekleg dfrfkhmqir vnaepaafyr
      241 aghvehmrtd rrlqrllqtq relmskelwl yigintfdyl gsilsyvvia ipifsgvygd
      301 lspaelstlv sknafvciyl iscftqlidl sttlsdvagy thrigqlret lldmslksqd
      361 ceilgesewg ldtppgwpaa epadtaflle rvsisapssd kplikdlslk isegqsllit
      421 gntgtgktsl lrvlgglwts trgsvqmltd fgphgvlflp qkpfftdgtl reqviyplke
      481 vypdsgsadd erilrflela glsnlvarte gldqqvdwnw ydvlspgemq rlsfarlfyl
      541 qpkyavldea tsalteeves elyrigqqlg mtfisvghrq slekvpvltr ma
//
LOCUS       NP_001339867             751 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 12 [Homo sapiens].
ACCESSION   NP_001339867 XP_016868767
VERSION     NP_001339867.1
DBSOURCE    REFSEQ: accession NM_001352938.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 751)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 751)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 751)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 751)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 751)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 751)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 751)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 751)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 751)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 751)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868767.1.
            
            Transcript Variant: This variant (13), as well as variants 14 and
            15, encodes isoform 12.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.40857.1,
                                           SRR1803613.184163.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..751
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..751
                     /product="DNA repair-scaffolding protein isoform 12"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=82442
     Region          <11..205
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          357..741
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..751
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352938.1:373..2628"
                     /note="isoform 12 is encoded by transcript variant 13"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mkirhflsyr epssieiley ssdsekeddl envllidses phkyhvqfas darqimerli
       61 dprtksteti lhtpqkptak fprtpensak kkllrgglae rlnglqnrer saislwrhqc
      121 isyqktlsgr ksgvltvkil elheecamqv amceqllgsp atsssqsvap rpgaglkvlf
      181 tketagylrg rpqdtvrifp pwqkliipsg scpvilntyf cekvvakeds ektcevycpd
      241 iplprrsisl aqmfvikglt nnspeiqvvc sgvattgtaw thghkeakqr iptstplrds
      301 lldvvesqga aswpgagvrv vvqrvyslps rdstrgqqga ssghtdpagt racllvqdac
      361 gmfgevhlef tmskarqleg kscslvgmkv lqkvtrgrta gifslidtlw ppaiplktpg
      421 rdqpceeikt hlpppalcyi ltahpnlgqi diidedpiyk lyqppvtrcl rdilqmndlg
      481 trcsfyatvi yqkpqlksll lleqreiwll vtdvtlqtke erdprlpktl lvyvaplcvl
      541 gsevlealag aaphslffkd alrdqgrivc aertvlllqk pllsvvsgas scelpgpvml
      601 dsldsatpvn sicsvqgtvv gvdestafsw pvcdmcgngr leqrpedrga fscgdcsrvv
      661 tspvlkrhlq vfldcrsrpq crvkvkllqr sissllrfaa gedgsyevks vlgkevglln
      721 cfvqsvtahp tscigleeie llsaggasae h
//
LOCUS       NP_113668                568 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase RIO1 isoform 1 [Homo sapiens].
ACCESSION   NP_113668
VERSION     NP_113668.2
DBSOURCE    REFSEQ: accession NM_031480.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 568)
  AUTHORS   Handle,F., Puhr,M., Gruber,M., Andolfi,C., Schafer,G., Klocker,H.,
            Haybaeck,J., De Wulf,P. and Culig,Z.
  TITLE     The Oncogenic Protein Kinase/ATPase RIOK1 Is Up-Regulated via the
            c-myc/E2F Transcription Factor Axis in Prostate Cancer
  JOURNAL   Am J Pathol 193 (9), 1284-1297 (2023)
   PUBMED   37301535
  REMARK    GeneRIF: The Oncogenic Protein Kinase/ATPase RIOK1 Is Up-Regulated
            via the c-myc/E2F Transcription Factor Axis in Prostate Cancer.
REFERENCE   2  (residues 1 to 568)
  AUTHORS   Chen,Y., Zhou,S., Wan,K., Yu,L., Zhao,C., Deng,H., Ou,Q., Qin,J.,
            Hu,J. and Hou,Z.
  TITLE     RIOK1 mediates p53 degradation and radioresistance in colorectal
            cancer through phosphorylation of G3BP2
  JOURNAL   Oncogene 41 (25), 3433-3444 (2022)
   PUBMED   35589951
  REMARK    GeneRIF: RIOK1 mediates p53 degradation and radioresistance in
            colorectal cancer through phosphorylation of G3BP2.
REFERENCE   3  (residues 1 to 568)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 568)
  AUTHORS   Mulvaney,K.M., Blomquist,C., Acharya,N., Li,R., Ranaghan,M.J.,
            O'Keefe,M., Rodriguez,D.J., Young,M.J., Kesar,D., Pal,D.,
            Stokes,M., Nelson,A.J., Jain,S.S., Yang,A., Mullin-Bernstein,Z.,
            Columbus,J., Bozal,F.K., Skepner,A., Raymond,D., LaRussa,S.,
            McKinney,D.C., Freyzon,Y., Baidi,Y., Porter,D., Aguirre,A.J.,
            Ianari,A., McMillan,B. and Sellers,W.R.
  TITLE     Molecular basis for substrate recruitment to the PRMT5 methylosome
  JOURNAL   Mol Cell 81 (17), 3481-3495 (2021)
   PUBMED   34358446
REFERENCE   5  (residues 1 to 568)
  AUTHORS   Plassart,L., Shayan,R., Montellese,C., Rinaldi,D., Larburu,N.,
            Pichereaux,C., Froment,C., Lebaron,S., O'Donohue,M.F., Kutay,U.,
            Marcoux,J., Gleizes,P.E. and Plisson-Chastang,C.
  TITLE     The final step of 40S ribosomal subunit maturation is controlled by
            a dual key lock
  JOURNAL   Elife 10, e61254 (2021)
   PUBMED   33908345
  REMARK    GeneRIF: The final step of 40S ribosomal subunit maturation is
            controlled by a dual key lock.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 568)
  AUTHORS   Widmann,B., Wandrey,F., Badertscher,L., Wyler,E., Pfannstiel,J.,
            Zemp,I. and Kutay,U.
  TITLE     The kinase activity of human Rio1 is required for final steps of
            cytoplasmic maturation of 40S subunits
  JOURNAL   Mol Biol Cell 23 (1), 22-35 (2012)
   PUBMED   22072790
  REMARK    GeneRIF: These data reveal a role of hRio1 in the final stages of
            cytoplasmic pre-40S maturation
REFERENCE   7  (residues 1 to 568)
  AUTHORS   Guderian,G., Peter,C., Wiesner,J., Sickmann,A., Schulze-Osthoff,K.,
            Fischer,U. and Grimmler,M.
  TITLE     RioK1, a new interactor of protein arginine methyltransferase 5
            (PRMT5), competes with pICln for binding and modulates PRMT5
            complex composition and substrate specificity
  JOURNAL   J Biol Chem 286 (3), 1976-1986 (2011)
   PUBMED   21081503
  REMARK    GeneRIF: RioK1, a new interactor of protein arginine
            methyltransferase 5 (PRMT5), competes with pICln for binding and
            modulates PRMT5 complex composition and substrate specificity.
REFERENCE   8  (residues 1 to 568)
  AUTHORS   Ren,J., Wang,Y., Liang,Y., Zhang,Y., Bao,S. and Xu,Z.
  TITLE     Methylation of ribosomal protein S10 by protein-arginine
            methyltransferase 5 regulates ribosome biogenesis
  JOURNAL   J Biol Chem 285 (17), 12695-12705 (2010)
   PUBMED   20159986
REFERENCE   9  (residues 1 to 568)
  AUTHORS   LaRonde-LeBlanc,N. and Wlodawer,A.
  TITLE     A family portrait of the RIO kinases
  JOURNAL   J Biol Chem 280 (45), 37297-37300 (2005)
   PUBMED   16183636
REFERENCE   10 (residues 1 to 568)
  AUTHORS   Line,A., Slucka,Z., Stengrevics,A., Silina,K., Li,G. and Rees,R.C.
  TITLE     Characterisation of tumour-associated antigens in colon cancer
  JOURNAL   Cancer Immunol Immunother 51 (10), 574-582 (2002)
   PUBMED   12384809
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139095.15 and AL138878.10.
            
            On Oct 7, 2002 this sequence version replaced NP_113668.1.
            
            Summary: The protein encoded by this gene competes with pICln for
            inclusion in the protein arginine methyltransferase 5 complex. This
            complex targets substrates for dimethylation. The encoded protein
            is essential for the last steps in the maturation of 40S subunits.
            [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1097208.1,
                                           SRR1803617.170551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379834.7/ ENSP00000369162.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..568
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..568
                     /product="serine/threonine-protein kinase RIO1 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase RIO1"
                     /calculated_mol_wt=65452
     Region          14..70
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRS2.2)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BRS2.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BRS2.2)"
     Region          83..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRS2.2)"
     Region          182..371
                     /region_name="RIO1_euk"
                     /note="Catalytic domain of the atypical protein serine
                     kinase, Eukaryotic RIO1 kinase; cd05147"
                     /db_xref="CDD:270698"
     Site            order(186,191..192,194,206,208,265,277..280,289,329,331,
                     340..341)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270698"
     Region          490..568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BRS2.2)"
     CDS             1..568
                     /gene="RIOK1"
                     /gene_synonym="AD034; bA288G3.1; RIO1; RRP10"
                     /coded_by="NM_031480.3:196..1902"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4500.1"
                     /db_xref="GeneID:83732"
                     /db_xref="HGNC:HGNC:18656"
                     /db_xref="MIM:617753"
ORIGIN      
        1 mdyrrllmsr vvpgqfddad ssdsenrdlk tvkekddilf edlqdnvnen gegeiedeee
       61 egyddddddw dwdegvgkla kgyvwnggsn pqanrqtsds ssakmstpad kvlrkfenki
      121 nldklnvtds vinkvteksr qkeadmyrik dkadratveq vldprtrmil fkmltrgiit
      181 eingcistgk eanvyhasta ngesraikiy ktsilvfkdr dkyvsgefrf rhgyckgnpr
      241 kmvktwaeke mrnlirlnta eipcpepiml rshvlvmsfi gkddmpapll knvqlseska
      301 relylqviqy mrrmyqdarl vhadlsefnm lyhgggvyii dvsqsvehdh phaleflrkd
      361 canvndffmr hsvavmtvre lfefvtdpsi thenmdayls kameiasqrt keerssqdhv
      421 deevfkrayi prtlnevkny erdmdiimkl keedmamnaq qdnilyqtvt glkkdlsgvq
      481 kvpallenqv eertcsdsed igssecsdtd seeqgdharp kkhttdpdid kkerkkmvke
      541 aqrekrknki pkhvkkrkek taktkkgk
//
LOCUS       NP_001357590             776 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-1 [Homo sapiens].
ACCESSION   NP_001357590 XP_011514933
VERSION     NP_001357590.1
DBSOURCE    REFSEQ: accession NM_001370661.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Yang,T., Hu,J., Zhang,L., Liu,L., Pan,X., Zhou,Y., Wu,Y., Shi,X.,
            Obiegbusi,C.N. and Dong,X.
  TITLE     CircCUL1 inhibits trophoblast cell migration and invasion and
            promotes cell autophagy by sponging hsa-miR-30e-3p in fetal growth
            restriction via the ANXA1/PI3K/AKT axis
  JOURNAL   J Biochem Mol Toxicol 38 (7), e23759 (2024)
   PUBMED   39003567
  REMARK    GeneRIF: CircCUL1 inhibits trophoblast cell migration and invasion
            and promotes cell autophagy by sponging hsa-miR-30e-3p in fetal
            growth restriction via the ANXA1/PI3K/AKT axis.
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,Y., Huang,X., Wang,Y., Lei,Y., Yu,J., Yu,S., Gao,Y., Yang,J.,
            Zhao,F., Yu,H., Zeng,J., Chu,Y., Yang,M., Li,G., Xie,X. and
            Zhang,J.
  TITLE     NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer by
            Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins
  JOURNAL   Adv Sci (Weinh) 11 (9), e2305907 (2024)
   PUBMED   38126621
  REMARK    GeneRIF: NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer
            by Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Khalil,M.I., Yang,C., Vu,L., Chadha,S., Nabors,H., James,C.D.,
            Morgan,I.M. and Pyeon,D.
  TITLE     The membrane-associated ubiquitin ligase MARCHF8 stabilizes the
            human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in
            head and neck cancer
  JOURNAL   J Virol 98 (2), e0172623 (2024)
   PUBMED   38226814
  REMARK    GeneRIF: The membrane-associated ubiquitin ligase MARCHF8
            stabilizes the human papillomavirus oncoprotein E7 by degrading
            CUL1 and UBE2L3 in head and neck cancer.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Winston,J.T., Strack,P., Beer-Romero,P., Chu,C.Y., Elledge,S.J. and
            Harper,J.W.
  TITLE     The SCFbeta-TRCP-ubiquitin ligase complex associates specifically
            with phosphorylated destruction motifs in IkappaBalpha and
            beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
  JOURNAL   Genes Dev 13 (3), 270-283 (1999)
   PUBMED   9990852
  REMARK    Erratum:[Genes Dev 1999 Apr 15;13(8):1050]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Ng,R.W., Arooz,T., Yam,C.H., Chan,I.W., Lau,A.W. and Poon,R.Y.
  TITLE     Characterization of the cullin and F-box protein partner Skp1
  JOURNAL   FEBS Lett 438 (3), 183-189 (1998)
   PUBMED   9827542
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005229.2 and AC006323.3.
            
            On May 21, 2019 this sequence version replaced XP_011514933.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.195744.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..776
                     /product="cullin-1"
                     /note="CUL-1"
                     /calculated_mol_wt=89548
     Region          21..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Site            63
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13616.2)"
     Region          706..768
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..776
                     /gene="CUL1"
                     /coded_by="NM_001370661.1:340..2670"
                     /db_xref="CCDS:CCDS34772.1"
                     /db_xref="GeneID:8454"
                     /db_xref="HGNC:HGNC:2551"
                     /db_xref="MIM:603134"
ORIGIN      
        1 msstrsqnph glkqigldqi wddlragiqq vytrqsmaks rymelythvy nyctsvhqsn
       61 qargagvpps kskkgqtpgg aqfvglelyk rlkeflknyl tnllkdgedl mdesvlkfyt
      121 qqwedyrfss kvlngicayl nrhwvrrecd egrkgiyeiy slalvtwrdc lfrplnkqvt
      181 navlklieke rngetintrl isgvvqsyve lglneddafa kgptltvyke sfesqfladt
      241 erfytreste flqqnpvtey mkkaearlle eqrrvqvylh estqdelark ceqvliekhl
      301 eifhtefqnl ldadknedlg rmynlvsriq dglgelkkll ethihnqgla aiekcgeaal
      361 ndpkmyvqtv ldvhkkynal vmsafnndag fvaaldkacg rfinnnavtk maqssskspe
      421 llarycdsll kkssknpeea eledtlnqvm vvfkyiedkd vfqkfyakml akrlvhqnsa
      481 sddaeasmis klkqacgfey tsklqrmfqd igvskdlneq fkkhltnsep ldldfsiqvl
      541 ssgswpfqqs ctfalpsele rsyqrftafy asrhsgrklt wlyqlskgel vtncfknryt
      601 lqastfqmai llqynteday tvqqltdstq ikmdilaqvl qillkskllv ledenanvde
      661 velkpdtlik lylgyknkkl rvninvpmkt eqkqeqetth knieedrkll iqaaivrimk
      721 mrkvlkhqql lgevltqlss rfkprvpvik kcidilieke ylervdgekd tysyla
//
LOCUS       NP_001300884             176 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 7 [Homo sapiens].
ACCESSION   NP_001300884
VERSION     NP_001300884.1
DBSOURCE    REFSEQ: accession NM_001313955.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP225027.1, BI199088.1 and
            BC009751.2.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (9) lacks two non-consecutive
            exons in the 5' and mid-region and uses an alternate donor splice
            site in the mid-region, compared to variant 1. It represents
            translation initiation at a downstream AUG compared to variant 1;
            the 5'-most initiation codon, as used in variant 1, is associated
            with a truncated ORF that would render this transcript variant a
            candidate for nonsense-mediated mRNA decay (NMD). Leaky scanning
            may allow translation initiation at the downstream AUG, which would
            result in an isoform (7) that is shorter, with a distinct
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.542864.1,
                                           SRR1163655.653636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..176
                     /product="aurora kinase B isoform 7"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=19738
     Region          <10..171
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..176
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_001313955.2:222..752"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 mtlrlgvlwa kimeeladal mychgkkvih rdikpenlll glkgelkiad fgwsvhapsl
       61 rrktmcgtld ylppemiegr mhnekvdlwc igvlcyellv gnppfesash netyrrivkv
      121 dlkfpasvpm gaqdliskll rhnpserlpl aqvsahpwvr ansrrvlpps alqsva
//
LOCUS       NP_001337429             389 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-L2 isoform D [Homo sapiens].
ACCESSION   NP_001337429 XP_011540521
VERSION     NP_001337429.1
DBSOURCE    REFSEQ: accession NM_001350500.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Hluchy,M., Gajduskova,P., Ruiz de Los Mozos,I., Rajecky,M.,
            Kluge,M., Berger,B.T., Slaba,Z., Potesil,D., Weiss,E., Ule,J.,
            Zdrahal,Z., Knapp,S., Paruch,K., Friedel,C.C. and Blazek,D.
  TITLE     CDK11 regulates pre-mRNA splicing by phosphorylation of SF3B1
  JOURNAL   Nature 609 (7928), 829-834 (2022)
   PUBMED   36104565
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Wu,C., Zhu,Q., Yao,Y., Shi,Z., Jin,C. and Chen,L.
  TITLE     Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription
  JOURNAL   Dev Neurosci 44 (3), 121-130 (2022)
   PUBMED   34937039
  REMARK    GeneRIF: Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription.
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Loyer,P., Trembley,J.H., Grenet,J.A., Busson,A., Corlu,A., Zhao,W.,
            Kocak,M., Kidd,V.J. and Lahti,J.M.
  TITLE     Characterization of cyclin L1 and L2 interactions with CDK11 and
            splicing factors: influence of cyclin L isoforms on splice site
            selection
  JOURNAL   J Biol Chem 283 (12), 7721-7732 (2008)
   PUBMED   18216018
  REMARK    GeneRIF: CDK11(p110) interacts physically and functionally with
            cyclin Lalpha and -beta isoforms and SR proteins to regulate
            splicing.
REFERENCE   7  (residues 1 to 389)
  AUTHORS   de Graaf,K., Hekerman,P., Spelten,O., Herrmann,A., Packman,L.C.,
            Bussow,K., Muller-Newen,G. and Becker,W.
  TITLE     Characterization of cyclin L2, a novel cyclin with an
            arginine/serine-rich domain: phosphorylation by DYRK1A and
            colocalization with splicing factors
  JOURNAL   J Biol Chem 279 (6), 4612-4624 (2004)
   PUBMED   14623875
  REMARK    GeneRIF: characterize cyclin L2 as a highly mobile component of
            nuclear speckles and suggest that DYRK1A may regulate splicing by
            phosphorylation of cyclin L2
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Edelheit,S. and Meiri,N.
  TITLE     Cyclin S: a new member of the cyclin family plays a role in
            long-term memory
  JOURNAL   Eur J Neurosci 19 (2), 365-375 (2004)
   PUBMED   14725631
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Cheng,H. and Bjerknes,M.
  TITLE     Patterns of gene expression along the crypt-villus axis in mouse
            jejunal epithelium
  JOURNAL   Anat Rec 244 (1), 78-94 (1996)
   PUBMED   8838426
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Bunnell,B.A., Heath,L.S., Adams,D.E., Lahti,J.M. and Kidd,V.J.
  TITLE     Increased expression of a 58-kDa protein kinase leads to changes in
            the CHO cell cycle
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7467-7471 (1990)
   PUBMED   2217177
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2612]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY002650.1, AK056120.1,
            DA944374.1, CN402151.1, AK074112.1 and AK000685.1.
            
            On Apr 15, 2017 this sequence version replaced XP_011540521.1.
            
            Summary: The protein encoded by this gene belongs to the cyclin
            family. Through its interaction with several proteins, such as RNA
            polymerase II, splicing factors, and cyclin-dependent kinases, this
            protein functions as a regulator of the pre-mRNA splicing process,
            as well as in inducing apoptosis by modulating the expression of
            apoptotic and antiapoptotic proteins. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (9) contains two consecutive
            alternate exons, resulting in use of an alternate start codon,
            compared to variant 1. The resulting isoform (D) has a shorter but
            distinct N-terminus compared to isoform A. Variants 8 and 9 both
            encode the same isoform (D).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.97277.1,
                                           SRR1803614.118835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..389
                     /product="cyclin-L2 isoform D"
                     /note="cyclin M; paneth cell-enhanced expression protein;
                     cyclin S"
                     /calculated_mol_wt=43255
     Region          <90..186
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..389
                     /gene="CCNL2"
                     /gene_synonym="ANIA-6B; CCNM; CCNS; HCLA-ISO; HLA-ISO;
                     PCEE; SB138"
                     /coded_by="NM_001350500.2:716..1885"
                     /note="isoform D is encoded by transcript variant 9"
                     /db_xref="GeneID:81669"
                     /db_xref="HGNC:HGNC:20570"
                     /db_xref="MIM:613482"
ORIGIN      
        1 mgqlaaalms prrglplgae spsarcshas nlhprgfslf qvdsfkeaaa rsaekgpaas
       61 aleeeeeepk rmaclpaatp alcsassfen ymndslrtdv fvrfqpesia caciylaart
      121 leiplpnrph wfllfgatee eiqeiclkil qlyarkkvdl thlegevekr khaieeakaq
      181 argllpggtq vldgtsgfsp apklvespke gkgskpspls vkntkrrleg akkakadspv
      241 nglpkgresr srsrsreqsy srspsrsasp krrksdsgst sggsksqsrs rsrsdspprq
      301 aprsapykgs eirgsrkskd ckypqkphks rsrsssrsrs rsreradnpg kykkkshyyr
      361 dqrrersrsy ertgrryerd hpghsrhrr
//
LOCUS       NP_061133                195 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisomal membrane protein 2 [Homo sapiens].
ACCESSION   NP_061133 XP_941561
VERSION     NP_061133.1
DBSOURCE    REFSEQ: accession NM_018663.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Lismont,C., Koster,J., Provost,S., Baes,M., Van Veldhoven,P.P.,
            Waterham,H.R. and Fransen,M.
  TITLE     Deciphering the potential involvement of PXMP2 and PEX11B in
            hydrogen peroxide permeation across the peroxisomal membrane
            reveals a role for PEX11B in protein sorting
  JOURNAL   Biochim Biophys Acta Biomembr 1861 (10), 182991 (2019)
   PUBMED   31129117
  REMARK    GeneRIF: Authors provide evidence that PXMP2 is not essential for
            H2O2 permeation across the peroxisomal membrane, neither in control
            cells nor in cells lacking PEX11B, a peroxisomal membrane-shaping
            protein whose yeast homologue facilitates the permeation of
            molecules up to 400Da.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Nestler,M., Martin,U., Hortschansky,P., Saluz,H.P., Henke,A. and
            Munder,T.
  TITLE     The zinc containing pro-apoptotic protein siva interacts with the
            peroxisomal membrane protein pmp22
  JOURNAL   Mol Cell Biochem 287 (1-2), 147-155 (2006)
   PUBMED   16683188
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Jones,J.M., Morrell,J.C. and Gould,S.J.
  TITLE     PEX19 is a predominantly cytosolic chaperone and import receptor
            for class 1 peroxisomal membrane proteins
  JOURNAL   J Cell Biol 164 (1), 57-67 (2004)
   PUBMED   14709540
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Brosius,U., Dehmel,T. and Gartner,J.
  TITLE     Two different targeting signals direct human peroxisomal membrane
            protein 22 to peroxisomes
  JOURNAL   J Biol Chem 277 (1), 774-784 (2002)
   PUBMED   11590176
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Sacksteder,K.A., Jones,J.M., South,S.T., Li,X., Liu,Y. and
            Gould,S.J.
  TITLE     PEX19 binds multiple peroxisomal membrane proteins, is
            predominantly cytoplasmic, and is required for peroxisome membrane
            synthesis
  JOURNAL   J Cell Biol 148 (5), 931-944 (2000)
   PUBMED   10704444
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Miyawaki,T., Sohma,O., Suzuki,Y. and Takashima,S.
  TITLE     Developmental immunohistochemistry of the 22 kDa peroxisomal
            membrane protein in the human brain
  JOURNAL   Brain Res 700 (1-2), 285-288 (1995)
   PUBMED   8624723
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC135586.8, AF250136.1 and BC073997.1.
            
            On Mar 4, 2006 this sequence version replaced XP_941561.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.498838.1,
                                           SRR1163657.33268.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000317479.8/ ENSP00000321271.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..195
                     /product="peroxisomal membrane protein 2"
                     /note="22 kDa peroxisomal membrane protein; peroxisomal
                     membrane protein 2, 22kDa"
                     /calculated_mol_wt=22121
     Site            31..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR77.3)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR77.3)"
     Site            115..135
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR77.3)"
     Region          130..191
                     /region_name="Mpv17_PMP22"
                     /note="Mpv17 / PMP22 family; pfam04117"
                     /db_xref="CDD:461182"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NR77.3)"
     CDS             1..195
                     /gene="PXMP2"
                     /gene_synonym="MPV17L3; PMP22"
                     /coded_by="NM_018663.3:85..672"
                     /db_xref="CCDS:CCDS9279.1"
                     /db_xref="GeneID:5827"
                     /db_xref="HGNC:HGNC:9716"
                     /db_xref="MIM:617399"
ORIGIN      
        1 mapaasrlra eaglgalprr alaqyllflr lypvltkaat sgilsalgnf laqmiekkrk
       61 kensrsldvg gplryavygf fftgplshff yffmehwipp evplaglrrl lldrlvfapa
      121 flmlfflimn flegkdasaf aakmrggfwp alrmnwrvwt plqfininyv plkfrvlfan
      181 laalfwyayl aslgk
//
LOCUS       NP_001268457             233 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome activator complex subunit 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001268457
VERSION     NP_001268457.1
DBSOURCE    REFSEQ: accession NM_001281528.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 233)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   4  (residues 1 to 233)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   5  (residues 1 to 233)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 233)
  AUTHORS   Ahn,K., Erlander,M., Leturcq,D., Peterson,P.A., Fruh,K. and Yang,Y.
  TITLE     In vivo characterization of the proteasome regulator PA28
  JOURNAL   J Biol Chem 271 (30), 18237-18242 (1996)
   PUBMED   8663520
REFERENCE   7  (residues 1 to 233)
  AUTHORS   Ahn,J.Y., Tanahashi,N., Akiyama,K., Hisamatsu,H., Noda,C.,
            Tanaka,K., Chung,C.H., Shibmara,N., Willy,P.J., Mott,J.D. et al.
  TITLE     Primary structures of two homologous subunits of PA28, a
            gamma-interferon-inducible protein activator of the 20S proteasome
  JOURNAL   FEBS Lett 366 (1), 37-42 (1995)
   PUBMED   7789512
REFERENCE   8  (residues 1 to 233)
  AUTHORS   Realini,C., Dubiel,W., Pratt,G., Ferrell,K. and Rechsteiner,M.
  TITLE     Molecular cloning and expression of a gamma-interferon-inducible
            activator of the multicatalytic protease
  JOURNAL   J Biol Chem 269 (32), 20727-20732 (1994)
   PUBMED   8051173
REFERENCE   9  (residues 1 to 233)
  AUTHORS   Honore,B., Leffers,H., Madsen,P. and Celis,J.E.
  TITLE     Interferon-gamma up-regulates a unique set of proteins in human
            keratinocytes. Molecular cloning and expression of the cDNA
            encoding the RGD-sequence-containing protein IGUP I-5111
  JOURNAL   Eur J Biochem 218 (2), 421-430 (1993)
   PUBMED   8269930
REFERENCE   10 (residues 1 to 233)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BJ993879.1, BU192084.1 and
            BM981616.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. The immunoproteasome
            contains an alternate regulator, referred to as the 11S regulator
            or PA28, that replaces the 19S regulator. Three subunits (alpha,
            beta and gamma) of the 11S regulator have been identified. This
            gene encodes the alpha subunit of the 11S regulator, one of the two
            11S subunits that is induced by gamma-interferon. Three alpha and
            three beta subunits combine to form a heterohexameric ring.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 3, which has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.456110.1,
                                           SRR5189655.25938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..233
                     /product="proteasome activator complex subunit 1 isoform
                     3"
                     /note="29-kD MCP activator subunit;
                     interferon-gamma-inducible protein 5111; activator of
                     multicatalytic protease subunit 1; interferon-gamma IEF
                     SSP 5111; interferon gamma up-regulated I-5111 protein;
                     epididymis secretory sperm binding protein Li 129m;
                     proteasome activator complex subunit 1; IGUP I-5111; 11S
                     regulator complex subunit alpha; proteasome (prosome,
                     macropain) activator subunit 1 (PA28 alpha)"
                     /calculated_mol_wt=26739
     Region          8..68
                     /region_name="PA28_alpha"
                     /note="Proteasome activator pa28 alpha subunit; pfam02251"
                     /db_xref="CDD:460507"
     Region          60..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q06323.1)"
     Region          103..224
                     /region_name="PA28_beta"
                     /note="Proteasome activator pa28 beta subunit; pfam02252"
                     /db_xref="CDD:460508"
     CDS             1..233
                     /gene="PSME1"
                     /gene_synonym="HEL-S-129m; IFI5111; PA28A; PA28alpha;
                     REGalpha"
                     /coded_by="NM_001281528.2:70..771"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61415.1"
                     /db_xref="GeneID:5720"
                     /db_xref="HGNC:HGNC:9568"
                     /db_xref="MIM:600654"
ORIGIN      
        1 mamlrvqpea qakvdvfred lctktenllg syfpkkisel daflkepaln eanlsnlkap
       61 ldipvpdpvk ekekeerkkq qekedkdekk kgededkgpp cgpvncneki vvllqrlkpe
      121 ikdvieqlnl vttwlqlqip riedgnnfgv avqekvfelm tslhtklegf htqiskyfse
      181 rgdavtkaak qphvgdyrql vheldeaeyr dirlmvmeir nayvrrlcym tss
//
LOCUS       NP_001357094             671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001357094
VERSION     NP_001357094.1
DBSOURCE    REFSEQ: accession NM_001370165.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.162032.1,
                                           SRR1803616.210428.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372989.6/ ENSP00000362080.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001370165.1:446..2461"
                     /note="isoform 1 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_057717                102 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-hemoglobin-stabilizing protein [Homo sapiens].
ACCESSION   NP_057717
VERSION     NP_057717.1
DBSOURCE    REFSEQ: accession NM_016633.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Vasseur,C., Domingues-Hamdi,E., Pakdaman,S., Galacteros,F. and
            Baudin-Creuza,V.
  TITLE     Alpha haemoglobin-stabilising protein concentration in the red
            blood cells of patients with sickle cell anaemia with and without
            hydroxycarbamide treatment
  JOURNAL   Br J Haematol 196 (1), 183-192 (2022)
   PUBMED   34378186
  REMARK    GeneRIF: Alpha haemoglobin-stabilising protein concentration in the
            red blood cells of patients with sickle cell anaemia with and
            without hydroxycarbamide treatment.
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Ray,R., Kalantri,S.A., Bhattacharjee,S., Biswas,A., Shahab,A.,
            Biswas,S. and Bhattacharyya,M.
  TITLE     Association of alpha hemoglobin-stabilizing protein (AHSP) gene
            mutation and disease severity among HbE-beta thalassemia patients
  JOURNAL   Ann Hematol 98 (8), 1827-1834 (2019)
   PUBMED   31190133
  REMARK    GeneRIF: The study documents that among the HbE beta thalassemia
            patients with varying severity, an exon mutation in AHSP is
            significantly prevalent only among the transfusion-dependent
            beta-thalassemia patients.
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Surapolchai,P., Chuansumrit,A., Sirachainan,N., Kadegasem,P.,
            Leung,K.C. and So,C.C.
  TITLE     A molecular study on the role of alpha-hemoglobin-stabilizing
            protein in hemoglobin H disease
  JOURNAL   Ann Hematol 96 (6), 1005-1014 (2017)
   PUBMED   28337528
  REMARK    GeneRIF: Findings indicate that alpha-hemoglobin-stabilizing
            protein (AHSP) expression is a biomarker of hemoglobin H (HbH)
            disease severity and infer an important role of AHSP in modulating
            the pathophysiology of this disease.
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Gell,D., Kong,Y., Eaton,S.A., Weiss,M.J. and Mackay,J.P.
  TITLE     Biophysical characterization of the alpha-globin binding protein
            alpha-hemoglobin stabilizing protein
  JOURNAL   J Biol Chem 277 (43), 40602-40609 (2002)
   PUBMED   12192002
  REMARK    GeneRIF: determination as a predominantly alpha-helical globular
            protein with a somewhat asymmetric shape
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Kihm,A.J., Kong,Y., Hong,W., Russell,J.E., Rouda,S., Adachi,K.,
            Simon,M.C., Blobel,G.A. and Weiss,M.J.
  TITLE     An abundant erythroid protein that stabilizes free
            alpha-haemoglobin
  JOURNAL   Nature 417 (6890), 758-763 (2002)
   PUBMED   12066189
  REMARK    GeneRIF: An abundant erythroid protein that stabilizes free
            alpha-haemoglobin.
REFERENCE   8  (residues 1 to 102)
  AUTHORS   Miele,G., Manson,J. and Clinton,M.
  TITLE     A novel erythroid-specific marker of transmissible spongiform
            encephalopathies
  JOURNAL   Nat Med 7 (3), 361-364 (2001)
   PUBMED   11231637
REFERENCE   9  (residues 1 to 102)
  AUTHORS   Gubin,A.N., Njoroge,J.M., Bouffard,G.G. and Miller,J.L.
  TITLE     Gene expression in proliferating human erythroid cells
  JOURNAL   Genomics 59 (2), 168-177 (1999)
   PUBMED   10409428
REFERENCE   10 (residues 1 to 102)
  AUTHORS   Choi,S.S., Yun,J.W., Choi,E.K., Cho,Y.G., Sung,Y.C. and Shin,H.S.
  TITLE     Construction of a gene expression profile of a human fetal liver by
            single-pass cDNA sequencing
  JOURNAL   Mamm Genome 6 (9), 653-657 (1995)
   PUBMED   8535075
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG940214.1 and AF112995.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a molecular chaperone which binds
            specifically to free alpha-globin and is involved in hemoglobin
            assembly. The encoded protein binds to monomeric alpha-globin until
            it has been transferred to beta-globin to form a heterodimer, which
            in turn binds to another heterodimer to form the stable tetrameric
            hemoglobin. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF112995.1, AF147435.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000302312.9/ ENSP00000307199.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..102
                     /product="alpha-hemoglobin-stabilizing protein"
                     /note="alpha hemoglobin stabilising protein; erythroid
                     differentiation associated factor; erythroid
                     differentiation-related factor"
                     /calculated_mol_wt=11709
     Region          5..91
                     /region_name="AHSP"
                     /note="Alpha-haemoglobin stabilising protein; pfam09236"
                     /db_xref="CDD:462718"
     CDS             1..102
                     /gene="AHSP"
                     /gene_synonym="EDRF; ERAF"
                     /coded_by="NM_016633.4:68..376"
                     /db_xref="CCDS:CCDS10716.1"
                     /db_xref="GeneID:51327"
                     /db_xref="HGNC:HGNC:18075"
                     /db_xref="MIM:605821"
ORIGIN      
        1 mallkankdl isaglkefsv llnqqvfndp lvseedmvtv vedwmnfyin yyrqqvtgep
       61 qerdkalqel rqelntlanp flakyrdflk shelpshppp ss
//
LOCUS       NP_001281262             261 aa            linear   PRI 20-NOV-2025
DEFINITION  V-type proton ATPase 21 kDa proteolipid subunit c'' isoform 3 [Homo
            sapiens].
ACCESSION   NP_001281262 XP_005271001
VERSION     NP_001281262.1
DBSOURCE    REFSEQ: accession NM_001294333.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Wang,L., Wu,D., Robinson,C.V., Wu,H. and Fu,T.M.
  TITLE     Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
            Assembly
  JOURNAL   Mol Cell 80 (3), 501-511 (2020)
   PUBMED   33065002
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Vasanthakumar,T. and Rubinstein,J.L.
  TITLE     Structure and Roles of V-type ATPases
  JOURNAL   Trends Biochem Sci 45 (4), 295-307 (2020)
   PUBMED   32001091
  REMARK    Review article
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Hohn,A., Sittig,A., Jung,T., Grimm,S. and Grune,T.
  TITLE     Lipofuscin is formed independently of macroautophagy and lysosomal
            activity in stress-induced prematurely senescent human fibroblasts
  JOURNAL   Free Radic Biol Med 53 (9), 1760-1769 (2012)
   PUBMED   22982048
REFERENCE   6  (residues 1 to 261)
  AUTHORS   Forgac,M.
  TITLE     Structure and properties of the vacuolar (H+)-ATPases
  JOURNAL   J Biol Chem 274 (19), 12951-12954 (1999)
   PUBMED   10224039
  REMARK    Review article
REFERENCE   7  (residues 1 to 261)
  AUTHORS   Nelson,N. and Harvey,W.R.
  TITLE     Vacuolar and plasma membrane proton-adenosinetriphosphatases
  JOURNAL   Physiol Rev 79 (2), 361-385 (1999)
   PUBMED   10221984
  REMARK    Review article
REFERENCE   8  (residues 1 to 261)
  AUTHORS   Nishigori,H., Yamada,S., Tomura,H., Fernald,A.A., Le Beau,M.M.,
            Takeuchi,T. and Takeda,J.
  TITLE     Identification and characterization of the gene encoding a second
            proteolipid subunit of human vacuolar H(+)-ATPase (ATP6F)
  JOURNAL   Genomics 50 (2), 222-228 (1998)
   PUBMED   9653649
REFERENCE   9  (residues 1 to 261)
  AUTHORS   Finbow,M.E. and Harrison,M.A.
  TITLE     The vacuolar H+-ATPase: a universal proton pump of eukaryotes
  JOURNAL   Biochem J 324 (Pt 3) (Pt 3), 697-712 (1997)
   PUBMED   9210392
  REMARK    Review article
REFERENCE   10 (residues 1 to 261)
  AUTHORS   Stevens,T.H. and Forgac,M.
  TITLE     Structure, function and regulation of the vacuolar (H+)-ATPase
  JOURNAL   Annu Rev Cell Dev Biol 13, 779-808 (1997)
   PUBMED   9442887
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357079.24.
            
            On Jul 1, 2014 this sequence version replaced XP_005271001.1.
            
            Summary: This gene encodes a portion of the V0 domain of vacuolar
            ATPase (V-ATPase), a multisubunit enzyme that mediates
            acidification of eukaryotic intracellular organelles. Activity of
            this enzyme is necessary for such varied processes as protein
            sorting, zymogen activation, receptor-mediated endocytosis, and
            synaptic vesicle proton gradient generation. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (3) contains an alternate segment
            in the 3' region, which results in a frameshift, compared to
            variant 1. The encoded isoform (3) has a longer and distinct
            C-terminus, compared to variant 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.163164.1,
                                           SRR1803614.192223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..261
                     /product="V-type proton ATPase 21 kDa proteolipid subunit
                     c'' isoform 3"
                     /EC_number="7.1.2.2"
                     /note="V-ATPase 21 kDa proteolipid subunit c''; vacuolar
                     ATP synthase 21 kDa proteolipid subunit; H(+)-transporting
                     two-sector ATPase, subunit F; V-type proton ATPase 21 kDa
                     proteolipid subunit; V-ATPase subunit c''; vacuolar proton
                     pump 21 kDa proteolipid subunit; ATPase, H+ transporting,
                     lysosomal, 21-KD, V0 subunit C-prime, prime; V-ATPase
                     subunit b; ATPase, H+ transporting, lysosomal, subunit F;
                     ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b;
                     vacuolar proton pump 21 kDa proteolipid subunit c'';
                     V-type proton ATPase 21 kDa proteolipid subunit c''"
                     /calculated_mol_wt=27546
     Site            4..24
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Region          49..111
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt1"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18177"
                     /db_xref="CDD:349417"
     Site            52..72
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            91..111
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            98
                     /site_type="other"
                     /note="Essential for proton translocation.
                     /evidence=ECO:0000250|UniProtKB:Q2TA24; propagated from
                     UniProtKB/Swiss-Prot (Q99437.1)"
     Region          133..197
                     /region_name="ATP-synt_Vo_c_ATP6F_rpt2"
                     /note="V-type proton ATPase 21 kDa proteolipid subunit
                     (ATP6F/ATP6V0B) and similar proteins; cd18178"
                     /db_xref="CDD:349418"
     Site            138..158
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     Site            176..196
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99437.1)"
     CDS             1..261
                     /gene="ATP6V0B"
                     /gene_synonym="ATP6F; HATPL; VMA16"
                     /coded_by="NM_001294333.2:82..867"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS72772.1"
                     /db_xref="GeneID:533"
                     /db_xref="HGNC:HGNC:861"
                     /db_xref="MIM:603717"
ORIGIN      
        1 mtglallysg vfvafwacal avgvcytifd lgfrfdvawf ltetspfmws nlgiglaisl
       61 svvgaawgiy itgssiiggg vkapriktkn lvsiifceav aiygiimaiv isnmaepfsa
      121 tdpkaighrn yhagysmfga gltvglsnlf cgvcvgivgs gaaladaqnp slfvkilive
      181 ifgsaiglfg vivailqvmn plgkplcpcp qpsltlllek lkcspslpit idspkqlppp
      241 hfhllvfsyr gslflsliwc h
//
LOCUS       NP_036443                393 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA/RNA-binding protein KIN17 [Homo sapiens].
ACCESSION   NP_036443
VERSION     NP_036443.1
DBSOURCE    REFSEQ: accession NM_012311.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Huang,X., Dai,Z., Zeng,B., Xiao,X., Zahid,K.R., Lin,X., Liu,T. and
            Zeng,T.
  TITLE     KIN17 functions in DNA damage repair and chemosensitivity by
            modulating RAD51 in hepatocellular carcinoma
  JOURNAL   Hum Cell 37 (5), 1489-1504 (2024)
   PUBMED   38935235
  REMARK    GeneRIF: KIN17 functions in DNA damage repair and chemosensitivity
            by modulating RAD51 in hepatocellular carcinoma.
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Dai,Z., Huang,Q., Huang,X., Zhu,C., Zahid,K.R., Liu,T., Li,Q.,
            Wu,C., Peng,M., Xiao,X., Raza,U., Yu,N. and Zeng,T.
  TITLE     KIN17 promotes cell migration and invasion through stimulating the
            TGF-beta/Smad2 pathway in hepatocellular carcinoma
  JOURNAL   Mol Carcinog 62 (3), 369-384 (2023)
   PUBMED   36468848
  REMARK    GeneRIF: KIN17 promotes cell migration and invasion through
            stimulating the TGF-beta/Smad2 pathway in hepatocellular carcinoma.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   de Lourenco,I.O., Seixas,F.A.V., Fernandez,M.A., Almeida,F.C.L.,
            Fossey,M.A., de Souza,F.P. and Caruso,I.P.
  TITLE     1H, 15N, and 13C resonance assignments of the SH3-like tandem
            domain of human KIN protein
  JOURNAL   Biomol NMR Assign 15 (2), 449-453 (2021)
   PUBMED   34417717
  REMARK    GeneRIF: [1]H, [15]N, and [13]C resonance assignments of the
            SH3-like tandem domain of human KIN protein.
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Gaspar,V.P., Ramos,A.C., Cloutier,P., Pattaro Junior,J.R., Duarte
            Junior,F.F., Bouchard,A., Seixas,F.A.V., Coulombe,B. and
            Fernandez,M.A.
  TITLE     Interactome Analysis of KIN (Kin17) Shows New Functions of This
            Protein
  JOURNAL   Curr Issues Mol Biol 43 (2), 767-781 (2021)
   PUBMED   34449532
  REMARK    GeneRIF: Interactome Analysis of KIN (Kin17) Shows New Functions of
            This Protein.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Kannouche,P., Mauffrey,P., Pinon-Lataillade,G., Mattei,M.G.,
            Sarasin,A., Daya-Grosjean,L. and Angulo,J.F.
  TITLE     Molecular cloning and characterization of the human KIN17 cDNA
            encoding a component of the UVC response that is conserved among
            metazoans
  JOURNAL   Carcinogenesis 21 (9), 1701-1710 (2000)
   PUBMED   10964102
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Blattner,C., Kannouche,P., Litfin,M., Bender,K., Rahmsdorf,H.J.,
            Angulo,J.F. and Herrlich,P.
  TITLE     UV-Induced stabilization of c-fos and other short-lived mRNAs
  JOURNAL   Mol Cell Biol 20 (10), 3616-3625 (2000)
   PUBMED   10779351
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Kannouche,P. and Angulo,J.F.
  TITLE     Overexpression of kin17 protein disrupts nuclear morphology and
            inhibits the growth of mammalian cells
  JOURNAL   J Cell Sci 112 (Pt 19), 3215-3224 (1999)
   PUBMED   10504327
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Biard,D.S., Saintigny,Y., Maratrat,M., Vozenin,M.C., Martin,M.,
            Daburon,F. and Angulo,J.F.
  TITLE     Differential expression of the HsKin17 protein during
            differentiation of in vitro reconstructed human skin
  JOURNAL   Arch Dermatol Res 289 (8), 448-456 (1997)
   PUBMED   9266022
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Angulo,J.F., Rouer,E., Mazin,A., Mattei,M.G., Tissier,A.,
            Horellou,P., Benarous,R. and Devoret,R.
  TITLE     Identification and expression of the cDNA of KIN17, a zinc-finger
            gene located on mouse chromosome 2, encoding a new DNA-binding
            protein
  JOURNAL   Nucleic Acids Res 19 (19), 5117-5123 (1991)
   PUBMED   1923796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301789.1, AJ005273.1,
            AL158044.17 and AA768850.1.
            
            Summary: The protein encoded by this gene is a nuclear protein that
            forms intranuclear foci during proliferation and is redistributed
            in the nucleoplasm during the cell cycle. Short-wave ultraviolet
            light provokes the relocalization of the protein, suggesting its
            participation in the cellular response to DNA damage. Originally
            selected based on protein-binding with RecA antibodies, the mouse
            protein presents a limited similarity with a functional domain of
            the bacterial RecA protein, a characteristic shared by this human
            ortholog. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the supported protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.8556.1,
                                           SRR1660805.187703.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379562.9/ ENSP00000368881.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p14"
     Protein         1..393
                     /product="DNA/RNA-binding protein KIN17"
                     /note="binding to curved DNA; KIN, antigenic determinant
                     of recA protein homolog"
                     /calculated_mol_wt=45243
     Region          51..160
                     /region_name="Winged helix-turn-helix (wHTH)"
                     /note="propagated from UniProtKB/Swiss-Prot (O60870.2)"
     Region          55..177
                     /region_name="Kin17_mid"
                     /note="Domain of Kin17 curved DNA-binding protein;
                     pfam10357"
                     /db_xref="CDD:463057"
     Site            135
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, by METTL22, in vitro.
                     /evidence=ECO:0000269|PubMed:23349634,
                     ECO:0007744|PubMed:24129315; N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (O60870.2)"
     Region          209..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60870.2)"
     Region          276..328
                     /region_name="KN17_SH3"
                     /note="KN17 SH3-like C-terminal domain; pfam18131"
                     /db_xref="CDD:407963"
     Region          284..334
                     /region_name="C-terminal subdomain A.
                     /evidence=ECO:0000269|PubMed:17045609"
                     /note="propagated from UniProtKB/Swiss-Prot (O60870.2)"
     Region          339..392
                     /region_name="KOW_KIN17"
                     /note="KOW_Kin17 is a RNA-binding motif; cd13155"
                     /db_xref="CDD:240519"
     Region          340..391
                     /region_name="C-terminal subdomain B.
                     /evidence=ECO:0000269|PubMed:17045609"
                     /note="propagated from UniProtKB/Swiss-Prot (O60870.2)"
     CDS             1..393
                     /gene="KIN"
                     /gene_synonym="BTCD; KIN17; Rts2"
                     /coded_by="NM_012311.4:61..1242"
                     /db_xref="CCDS:CCDS7080.1"
                     /db_xref="GeneID:22944"
                     /db_xref="HGNC:HGNC:6327"
                     /db_xref="MIM:601720"
ORIGIN      
        1 mgksdfltpk aianrikskg lqklrwycqm cqkqcrdeng fkchcmsesh qrqlllasen
       61 pqqfmdyfse efrndflell rrrfgtkrvh nnivyneyis hrehihmnat qwetltdftk
      121 wlgreglckv detpkgwyiq yidrdpetir rqlelekkkk qdlddeekta kfieeqvrrg
      181 legkeqevpt ftelsrende ekvtfnlskg acsssgatss ksstlgpsal ktigssasvk
      241 rkessqsstq skekkkkksa ldeimeieee kkrtartdyw lqpeiivkii tkklgekyhk
      301 kkaivkevid kytavvkmid sgdklkldqt hletvipapg krilvlnggy rgnegtlesi
      361 nektfsativ ietgplkgrr vegiqyedis kla
//
LOCUS       NP_005008                367 aa            linear   PRI 20-NOV-2025
DEFINITION  choline-phosphate cytidylyltransferase A [Homo sapiens].
ACCESSION   NP_005008
VERSION     NP_005008.2
DBSOURCE    REFSEQ: accession NM_005017.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Mao,Z., Li,T., Zhao,H., Wang,X., Kang,Y. and Kang,Y.
  TITLE     Methylome and transcriptome profiling revealed epigenetic silencing
            of LPCAT1 and PCYT1A associated with lipidome alterations in
            polycystic ovary syndrome
  JOURNAL   J Cell Physiol 236 (9), 6362-6375 (2021)
   PUBMED   33521992
  REMARK    GeneRIF: Methylome and transcriptome profiling revealed epigenetic
            silencing of LPCAT1 and PCYT1A associated with lipidome alterations
            in polycystic ovary syndrome.
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Yu,J., Wu,C., Wu,Q., Huang,J., Fu,W., Xie,X., Li,W., Tang,W., Xu,C.
            and Jin,G.
  TITLE     PCYT1A suppresses proliferation and migration via inhibiting mTORC1
            pathway in lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 529 (2), 353-361 (2020)
   PUBMED   32703435
  REMARK    GeneRIF: PCYT1A suppresses proliferation and migration via
            inhibiting mTORC1 pathway in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Weinhold,P.A. and Feldman,D.A.
  TITLE     Fatty acids promote the formation of complexes between
            choline-phosphate cytidylyltransferase and cytidylyltransferase
            binding protein
  JOURNAL   Arch Biochem Biophys 318 (1), 147-156 (1995)
   PUBMED   7726555
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Kalmar,G.B., Kay,R.J., LaChance,A.C. and Cornell,R.B.
  TITLE     Primary structure and expression of a human CTP:phosphocholine
            cytidylyltransferase
  JOURNAL   Biochim Biophys Acta 1219 (2), 328-334 (1994)
   PUBMED   7918629
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Johnson,J.E. and Cornell,R.B.
  TITLE     Membrane-binding amphipathic alpha-helical peptide derived from
            CTP:phosphocholine cytidylyltransferase
  JOURNAL   Biochemistry 33 (14), 4327-4335 (1994)
   PUBMED   8155650
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Hunt,A.N., Normand,C.S. and Postle,A.D.
  TITLE     CTP:cholinephosphate cytidylyltransferase in human and rat lung:
            association in vitro with cytoskeletal actin
  JOURNAL   Biochim Biophys Acta 1043 (1), 19-26 (1990)
   PUBMED   2155660
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Vance,J.E. and Vance,D.E.
  TITLE     Does rat liver Golgi have the capacity to synthesize phospholipids
            for lipoprotein secretion?
  JOURNAL   J Biol Chem 263 (12), 5898-5909 (1988)
   PUBMED   2833521
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK309073.1, BC046355.1,
            DB223595.1 and AC069257.28.
            
            On Jun 9, 2003 this sequence version replaced NP_005008.1.
            
            Summary: This gene belongs to the cytidylyltransferase family and
            is involved in the regulation of phosphatidylcholine biosynthesis.
            Mutations in this gene are associated with spondylometaphyseal
            dysplasia with cone-rod dystrophy. Alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Aug
            2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.373901.1, BC046355.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..367
                     /product="choline-phosphate cytidylyltransferase A"
                     /EC_number="2.7.7.15"
                     /note="phosphorylcholine transferase A; CTP:phosphocholine
                     cytidylyltransferase A; CT A; CCT A; CCT-alpha;
                     CTP:phosphocholine cytidylyltransferase-alpha;
                     choline-phosphate cytidylyltransferase alpha;
                     phosphorylcholine transferase alpha; phosphate
                     cytidylyltransferase 1, choline, alpha"
                     /calculated_mol_wt=41600
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Region          75..224
                     /region_name="CCT"
                     /note="CTP:phosphocholine cytidylyltransferase; cd02174"
                     /db_xref="CDD:173925"
     Site            order(82..85,89,91..92,95,113,122,150..151,168..169,182,
                     195..197,200)
                     /site_type="active"
                     /db_xref="CDD:173925"
     Site            89..92
                     /site_type="other"
                     /note="(T/H)XGH motif"
                     /db_xref="CDD:173925"
     Region          228..287
                     /region_name="Amphipathic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Region          272..293
                     /region_name="Autoinhibitory (AI).
                     /evidence=ECO:0000250|UniProtKB:P19836"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Region          298..315
                     /region_name="Amphipathic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Region          313..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49586; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49586; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P49585.2)"
     CDS             1..367
                     /gene="PCYT1A"
                     /gene_synonym="CCTA; CCTalpha; CGL5; CT; CTA; CTPCT;
                     PCYT1; SMDCRD"
                     /coded_by="NM_005017.4:187..1290"
                     /db_xref="CCDS:CCDS3315.1"
                     /db_xref="GeneID:5130"
                     /db_xref="HGNC:HGNC:8754"
                     /db_xref="MIM:123695"
ORIGIN      
        1 mdaqcsakvn arkrrkeapg pngateedgv pskvqrcavg lrqpapfsde ievdfskpyv
       61 rvtmeeasrg tpcerpvrvy adgifdlfhs gharalmqak nlfpntyliv gvcsdelthn
      121 fkgftvmnen erydavqhcr yvdevvrnap wtltpeflae hridfvahdd ipyssagsdd
      181 vykhikeagm faptqrtegi stsdiitriv rdydvyarrn lqrgytakel nvsfinekky
      241 hlqervdkvk kkvkdveeks kefvqkveek sidliqkwee ksrefigsfl emfgpegalk
      301 hmlkegkgrm lqaispkqsp sssptrersp spsfrwpfsg ktsppcspan lsrhkaaayd
      361 isedeed
//
LOCUS       NP_001963                267 aa            linear   PRI 20-NOV-2025
DEFINITION  neutrophil elastase preproprotein [Homo sapiens].
ACCESSION   NP_001963
VERSION     NP_001963.1
DBSOURCE    REFSEQ: accession NM_001972.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Birk,D., Siepmann,E., Simon,S. and Sommerhoff,C.P.
  TITLE     Human Neutrophil Elastase: Characterization of Intra- vs.
            Extracellular Inhibition
  JOURNAL   Int J Mol Sci 25 (14), 7917 (2024)
   PUBMED   39063160
  REMARK    GeneRIF: Human Neutrophil Elastase: Characterization of Intra- vs.
            Extracellular Inhibition.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Fragoso,J.M., Vargas-Alarcon,G., Martinez-Flores,A.E.,
            Montufar-Robles,I., Barbosa-Cobos,R.E., Rojas-Velasco,G. and
            Ramirez-Bello,J.
  TITLE     ELANE rs17223045C/T and rs3761007G/A variants: Protective factors
            against COVID-19
  JOURNAL   Biomol Biomed 24 (3), 665-672 (2024)
   PUBMED   38226800
  REMARK    GeneRIF: ELANE rs17223045C/T and rs3761007G/A variants: Protective
            factors against COVID-19.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Zheng,S., Bulut,G.B., Kummarapurugu,A.B., Ma,J. and Voynow,J.A.
  TITLE     Neutrophil Elastase Degrades Histone Deacetylases and Sirtuin 1 in
            Primary Human Monocyte Derived Macrophages
  JOURNAL   Int J Mol Sci 25 (8), 4265 (2024)
   PUBMED   38673851
  REMARK    GeneRIF: Neutrophil Elastase Degrades Histone Deacetylases and
            Sirtuin 1 in Primary Human Monocyte Derived Macrophages.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Horwitz,M.S., Corey,S.J., Grimes,H.L. and Tidwell,T.
  TITLE     ELANE mutations in cyclic and severe congenital neutropenia:
            genetics and pathophysiology
  JOURNAL   Hematol Oncol Clin North Am 27 (1), 19-41 (2013)
   PUBMED   23351986
  REMARK    GeneRIF: A review discusses how ELANE mutations provide clues into
            the pathogenesis of cyclic and severe congenital neutropenia.
            Review article
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Dale,D.C. and Makaryan,V.
  TITLE     ELANE-Related Neutropenia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301705
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Zimmer,M., Medcalf,R.L., Fink,T.M., Mattmann,C., Lichter,P. and
            Jenne,D.E.
  TITLE     Three human elastase-like genes coordinately expressed in the
            myelomonocyte lineage are organized as a single genetic locus on
            19pter
  JOURNAL   Proc Natl Acad Sci U S A 89 (17), 8215-8219 (1992)
   PUBMED   1518849
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Higuchi,D.A., Wun,T.C., Likert,K.M. and Broze,G.J. Jr.
  TITLE     The effect of leukocyte elastase on tissue factor pathway inhibitor
  JOURNAL   Blood 79 (7), 1712-1719 (1992)
   PUBMED   1558967
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Aoki,Y. and Hase,T.
  TITLE     The primary structure and elastinolytic activity of medullasin (a
            serine protease of bone marrow)
  JOURNAL   Biochem Biophys Res Commun 178 (2), 501-506 (1991)
   PUBMED   1859409
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Fletcher,T.S., Shen,W.F. and Largman,C.
  TITLE     Primary structure of human pancreatic elastase 2 determined by
            sequence analysis of the cloned mRNA
  JOURNAL   Biochemistry 26 (23), 7256-7261 (1987)
   PUBMED   3427074
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M34379.1 and BI254663.1.
            
            Summary: Elastases form a subfamily of serine proteases that
            hydrolyze many proteins in addition to elastin. Humans have six
            elastase genes which encode structurally similar proteins. The
            encoded preproprotein is proteolytically processed to generate the
            active protease. Following activation, this protease hydrolyzes
            proteins within specialized neutrophil lysosomes, called azurophil
            granules, as well as proteins of the extracellular matrix. The
            enzyme may play a role in degenerative and inflammatory diseases
            through proteolysis of collagen-IV and elastin. This protein also
            degrades the outer membrane protein A (OmpA) of E. coli as well as
            the virulence factors of such bacteria as Shigella, Salmonella and
            Yersinia. Mutations in this gene are associated with cyclic
            neutropenia and severe congenital neutropenia (SCN). This gene is
            present in a gene cluster on chromosome 19. [provided by RefSeq,
            Jan 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M34379.1, X05875.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263621.2/ ENSP00000263621.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..267
                     /product="neutrophil elastase preproprotein"
                     /EC_number="3.4.21.37"
                     /note="medullasin; elastase 2, neutrophil; bone marrow
                     serine protease; leukocyte elastase; polymorphonuclear
                     elastase; granulocyte-derived elastase; elastase-2; PMN
                     elastase; polymorphonuclear leukocyte elastase"
                     /calculated_mol_wt=25778
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2759
     mat_peptide     30..267
                     /product="Neutrophil elastase. /id=PRO_0000027704"
                     /note="propagated from UniProtKB/Swiss-Prot (P08246.1)"
                     /calculated_mol_wt=25562
     Region          30..245
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            30
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(70,117,202)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            124
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:26274980,
                     ECO:0000269|PubMed:3550808; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:3550808; propagated from
                     UniProtKB/Swiss-Prot (P08246.1)"
     Site            order(196,217,219)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..267
                     /gene="ELANE"
                     /gene_synonym="ELA2; GE; HLE; HNE; NE; PMN-E; SCN1"
                     /coded_by="NM_001972.4:27..830"
                     /db_xref="CCDS:CCDS12045.1"
                     /db_xref="GeneID:1991"
                     /db_xref="HGNC:HGNC:3309"
                     /db_xref="MIM:130130"
ORIGIN      
        1 mtlgrrlacl flacvlpall lggtalasei vggrrarpha wpfmvslqlr gghfcgatli
       61 apnfvmsaah cvanvnvrav rvvlgahnls rreptrqvfa vqrifengyd pvnllndivi
      121 lqlngsatin anvqvaqlpa qgrrlgngvq clamgwgllg rnrgiasvlq elnvtvvtsl
      181 crrsnvctlv rgrqagvcfg dsgsplvcng lihgiasfvr ggcasglypd afapvaqfvn
      241 widsiiqrse dnpcphprdp dpasrth
//
LOCUS       NP_778239                292 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform g [Homo sapiens].
ACCESSION   NP_778239
VERSION     NP_778239.2
DBSOURCE    REFSEQ: accession NM_175069.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Apr 23, 2019 this sequence version replaced NP_778239.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (2) has multiple differences
            compared to variant 1. This variant encodes isoform (g) which has a
            shorter C-terminus compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055672.1, SRR7410570.434314.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..292
                     /product="aprataxin isoform g"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=33163
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     CDS             1..292
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_175069.3:67..945"
                     /note="isoform g is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6532.2"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qe
//
LOCUS       NP_612471                227 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger MYND domain-containing protein 19 [Homo sapiens].
ACCESSION   NP_612471
VERSION     NP_612471.1
DBSOURCE    REFSEQ: accession NM_138462.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Francke,F., Buck,F. and Bachner,D.
  TITLE     MYND domain specific interaction of the melanin-concentrating
            hormone receptor 1 interacting zinc-finger protein with alpha- and
            beta-tubulin
  JOURNAL   Biochem Biophys Res Commun 334 (4), 1292-1298 (2005)
   PUBMED   16039987
  REMARK    GeneRIF: Our results suggest that MIZIP might play an important
            role in mammalian cells by associating with tubulin and thus might
            provide a link between MCHR1 and tubulin functions.
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Bachner,D., Kreienkamp,H.J. and Richter,D.
  TITLE     MIZIP, a highly conserved, vertebrate specific
            melanin-concentrating hormone receptor 1 interacting zinc-finger
            protein
  JOURNAL   FEBS Lett 526 (1-3), 124-128 (2002)
   PUBMED   12208518
  REMARK    GeneRIF: was identified from human brain and interacts with the
            C-terminus of melanin-concentrating hormone receptor 1
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365502.57, BU147462.1 and AJ298882.2.
            
            Summary: ZMYND19 is a MYND zinc finger domain-containing protein
            that binds to the C terminus of melanin-concentrating hormone
            receptor-1 (MCHR1; MIM 601751) (Bachner et al., 2002 [PubMed
            12208518]), and to the N termini of alpha-tubulin (TUBA1; MIM
            191110), and beta-tubulin (TUBB; MIM 191130) (Francke et al., 2005
            [PubMed 16039987]).[supplied by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.295999.1, AJ298882.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298585.3/ ENSP00000298585.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..227
                     /product="zinc finger MYND domain-containing protein 19"
                     /note="melanin-concentrating hormone receptor 1
                     interacting zinc-finger protein; zinc finger, MYND domain
                     containing 19; MCH-R1-interacting zinc finger protein"
                     /calculated_mol_wt=26302
     Region          66..105
                     /region_name="HNHc"
                     /note="HNH nucleases; HNH endonuclease signature which is
                     found in viral, prokaryotic, and eukaryotic proteins. The
                     alignment includes members of the large group of homing
                     endonucleases, yeast intron 1 protein, MutS, as well as
                     bacterial colicins, pyocins, and...; cl00083"
                     /db_xref="CDD:469607"
     Region          174..212
                     /region_name="zf-MYND"
                     /note="MYND finger; pfam01753"
                     /db_xref="CDD:460312"
     CDS             1..227
                     /gene="ZMYND19"
                     /gene_synonym="MIZIP"
                     /coded_by="NM_138462.3:250..933"
                     /db_xref="CCDS:CCDS7048.1"
                     /db_xref="GeneID:116225"
                     /db_xref="HGNC:HGNC:21146"
                     /db_xref="MIM:611424"
ORIGIN      
        1 mtdfklgivr lgrvagktky tlideqdipl vesysfearm evdadgngak ifayafdknr
       61 grgsgrllhe llwerhrggv apgfqvvhln avtvdnrldn lqlvpwgwrp kaeetsskqr
      121 eqslywlaiq qlptdpieeq fpvlnvtryy nangdvveee ensctyyech yppctviekq
      181 lrefnicgrc qvarycgsqc qqkdwpahkk hcrerkrpfq heleper
//
LOCUS       NP_689603                297 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 178A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_689603
VERSION     NP_689603.2
DBSOURCE    REFSEQ: accession NM_152390.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Decker,C.E., Yang,Z., Rimer,R., Park-Min,K.H., Macaubas,C.,
            Mellins,E.D., Novack,D.V. and Faccio,R.
  TITLE     Tmem178 acts in a novel negative feedback loop targeting NFATc1 to
            regulate bone mass
  JOURNAL   Proc Natl Acad Sci U S A 112 (51), 15654-15659 (2015)
   PUBMED   26644563
  REMARK    GeneRIF: Tmem178 localizes to the ER membrane and regulates
            RANKL-induced Ca(2+) fluxes, thus controlling NFATc1 induction
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DN993805.1, BC029530.1 and AC007246.3.
            
            On Nov 25, 2009 this sequence version replaced NP_689603.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029530.1, AK075440.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281961.3/ ENSP00000281961.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.1"
     Protein         1..297
                     /product="transmembrane protein 178A isoform 1 precursor"
                     /note="transmembrane protein 178"
                     /calculated_mol_wt=30508
     sig_peptide     1..25
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBL3.1)"
                     /calculated_mol_wt=2529
     mat_peptide     26..297
                     /product="Transmembrane protein 178A. /id=PRO_0000287280"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
                     /calculated_mol_wt=30508
     Region          41..84
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Region          106..274
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            180..200
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBL3.1)"
     CDS             1..297
                     /gene="TMEM178A"
                     /gene_synonym="TMEM178"
                     /coded_by="NM_152390.3:59..952"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1804.1"
                     /db_xref="GeneID:130733"
                     /db_xref="HGNC:HGNC:28517"
ORIGIN      
        1 mepralvtal slglslcslg llvtaiftdh wyetdprrhk escersraga dppdqknrlm
       61 plshlplrds pplgrrllpg gpgradpesw rsllglggld aecgrplfat ysglwrkcyf
      121 lgidrdidtl ilkgiaqrct aikyhfsqpi rlrnipfnlt ktiqqdewhl lhlrritagf
      181 lgmavavllc gcivatvsff weesltqhva gllflmtgif ctislctyaa sisydlnrlp
      241 kliyslpadv ehgyswsifc awcslgfiva agglciaypf isrtkiaqlk sgrdstv
//
LOCUS       NP_001273554             305 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein with serine-rich domain 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001273554 XP_005255104
VERSION     NP_001273554.1
DBSOURCE    REFSEQ: accession NM_001286625.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Kumari,S., Adhikary,A. and Singh,K.K.
  TITLE     BioID proximity mapping reveals novel SAP18 interactions in the
            prespliceosomal complex
  JOURNAL   Biochem Biophys Res Commun 738, 150944 (2024)
   PUBMED   39522233
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Wang,X., Ling,R., Peng,Y., Qiu,W. and Chen,D.
  TITLE     RNPS1 stabilizes NAT10 protein to facilitate translation in cancer
            via tRNA ac4C modification
  JOURNAL   Int J Oral Sci 16 (1), 6 (2024)
   PUBMED   38246918
  REMARK    GeneRIF: RNPS1 stabilizes NAT10 protein to facilitate translation
            in cancer via tRNA ac[4]C modification.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Deka,B., Chandra,P., Yadav,P., Rehman,A., Kumari,S.,
            Kunnumakkara,A.B. and Singh,K.K.
  TITLE     RNPS1 functions as an oncogenic splicing factor in cervical cancer
            cells
  JOURNAL   IUBMB Life 75 (6), 514-529 (2023)
   PUBMED   36300671
  REMARK    GeneRIF: RNPS1 functions as an oncogenic splicing factor in
            cervical cancer cells.
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Mayeda,A., Badolato,J., Kobayashi,R., Zhang,M.Q., Gardiner,E.M. and
            Krainer,A.R.
  TITLE     Purification and characterization of human RNPS1: a general
            activator of pre-mRNA splicing
  JOURNAL   EMBO J 18 (16), 4560-4570 (1999)
   PUBMED   10449421
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Loyer,P., Trembley,J.H., Lahti,J.M. and Kidd,V.J.
  TITLE     The RNP protein, RNPS1, associates with specific isoforms of the
            p34cdc2-related PITSLRE protein kinase in vivo
  JOURNAL   J Cell Sci 111 (Pt 11), 1495-1506 (1998)
   PUBMED   9580558
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Burn,T.C., Connors,T.D., Van Raay,T.J., Dackowski,W.R.,
            Millholland,J.M., Klinger,K.W. and Landes,G.M.
  TITLE     Generation of a transcriptional map for a 700-kb region surrounding
            the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis
            type 2 (TSC2) disease genes on human chromosome 16p3.3
  JOURNAL   Genome Res 6 (6), 525-537 (1996)
   PUBMED   8828041
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Badolato,J., Gardiner,E., Morrison,N. and Eisman,J.
  TITLE     Identification and characterisation of a novel human RNA-binding
            protein
  JOURNAL   Gene 166 (2), 323-327 (1995)
   PUBMED   8543184
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA062271.1, L37368.1 and
            BC108316.1.
            
            On Nov 8, 2013 this sequence version replaced XP_005255104.1.
            
            Summary: This gene encodes a protein that is part of a
            post-splicing multiprotein complex involved in both mRNA nuclear
            export and mRNA surveillance. mRNA surveillance detects exported
            mRNAs with truncated open reading frames and initiates
            nonsense-mediated mRNA decay (NMD). When translation ends upstream
            from the last exon-exon junction, this triggers NMD to degrade
            mRNAs containing premature stop codons. This protein binds to the
            mRNA and remains bound after nuclear export, acting as a
            nucleocytoplasmic shuttling protein. This protein contains many
            serine residues. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant (2). Variants 1, 2, and 3 all encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.39894.1,
                                           SRR1803615.116467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..305
                     /product="RNA-binding protein with serine-rich domain 1
                     isoform a"
                     /note="SR protein; RNA-binding protein S1, serine-rich
                     domain; SR-related protein LDC2; RNA binding protein with
                     serine-rich domain"
                     /calculated_mol_wt=34077
     Region          1..220
                     /region_name="Necessary for interaction with the cleaved
                     p110 isoform of CDC2L1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          1..170
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          1..161
                     /region_name="Necessary for interaction with SRP54,
                     nuclear localization and exon-skipping.
                     /evidence=ECO:0000269|PubMed:14729963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:15684395; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          69..121
                     /region_name="Necessary for interactions with UPF2 and
                     UPF3B and UPF2-dependent NMD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          156..242
                     /region_name="Necessary for interaction with PNN and
                     exon-skipping"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          159..244
                     /region_name="Interaction with SAP18 and ACIN1.
                     /evidence=ECO:0000269|PubMed:20966198"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          163..236
                     /region_name="RRM_RNPS1"
                     /note="RNA recognition motif (RRM) found in RNA-binding
                     protein with serine-rich domain 1 (RNPS1) and similar
                     proteins; cd12365"
                     /db_xref="CDD:409800"
     Site            order(169..173,175..176,179..180,183..184,195,200..201,
                     221..231)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409800"
     Site            218
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15287.1)"
     Region          238..305
                     /region_name="Necessary for interaction with TRA2B,
                     nuclear localization and exon-skipping.
                     /evidence=ECO:0000269|PubMed:14729963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     Region          240..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15287.1)"
     CDS             1..305
                     /gene="RNPS1"
                     /gene_synonym="E5.1"
                     /coded_by="NM_001286625.1:281..1198"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10465.1"
                     /db_xref="GeneID:10921"
                     /db_xref="HGNC:HGNC:10080"
                     /db_xref="MIM:606447"
ORIGIN      
        1 mdlsgvkkks llgvkennkk sstrapsptk rkdrsdeksk drskdkgatk essekdrgrd
       61 ktrkrrsass gssstrsrss stsssgssts tgsssgssss sassrsgsss tsrsssssss
      121 sgspspsrrr hdnrrrsrsk skppkrdeke rkrrspspkp tkvhigrltr nvtkdhimei
      181 fstygkikmi dmpvermhph lskgyayvef enpdeaekal khmdggqidg qeitatavla
      241 pwprppprrf spprrmlppp pmwrrspprm rrrsrsprrr spvrrrsrsp grrrhrsrss
      301 snssr
//
LOCUS       NP_001357095             671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001357095
VERSION     NP_001357095.1
DBSOURCE    REFSEQ: accession NM_001370166.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.200817.1,
                                           SRR1803615.133706.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001370166.1:358..2373"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_003190                667 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform b [Homo sapiens].
ACCESSION   NP_003190
VERSION     NP_003190.1
DBSOURCE    REFSEQ: accession NM_003199.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 667)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 667)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 667)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 667)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 667)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 667)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 667)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 667)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 667)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 667)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M74719.1, BJ989626.1 and
            AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            3' end of an exon compared to variant 3. The resulting isoform (b,
            also known as TCF4-B-) is shorter at the N-terminus and lacks an
            alternate internal segment compared to isoform c.
            
            Sequence Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M74719.1, AK122765.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..667
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..667
                     /product="transcription factor 4 isoform b"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=71177
     Region          1..83
                     /region_name="Essential for MYOD1 inhibition.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          18..26
                     /region_name="9aaTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          24..245
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          263..321
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          336..379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62655; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          379..400
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          466..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          558..642
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(566,570,572..574,576,581,602..603)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(579..580,583..584,586..587,590,594,604,607,611,614,
                     617..622)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     Region          619..642
                     /region_name="Class A specific domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          634..667
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     CDS             1..667
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_003199.3:176..2179"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11960.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygresnlqg
      121 chqqsllggd mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl
      181 pssvyapsas tadynrdspg ypsskpatst fpssffmqdg hhssdpwsss sgmnqpgyag
      241 mlgnsshipq sssycslhph erlsypshss adinsslppm stfhrsgtnh ystssctppa
      301 ngtdsimanr gsgaagssqt gdalgkalas iyspdhtnns fssnpstpvg sppslsagta
      361 vwsrnggqas sspnyegplh slqsriedrl erlddaihvl rnhavgpsta mpgghgdmhg
      421 iigpshngam gglgsgygtg llsanrhslm vgthredgva lrgshsllpn qvpvpqlpvq
      481 satspdlnpp qdpyrgmppg lqgqsvssgs seiksddegd enlqdtksse dkkldddkkd
      541 iksitsnndd edltpeqkae rekerrmann arerlrvrdi neafkelgrm vqlhlksdkp
      601 qtkllilhqa vavilsleqq vrernlnpka aclkrreeek vsseppplsl agphpgmgda
      661 snhmgqm
//
LOCUS       NP_001138777            1134 aa            linear   PRI 20-NOV-2025
DEFINITION  IQ domain-containing protein N isoform c [Homo sapiens].
ACCESSION   NP_001138777
VERSION     NP_001138777.1
DBSOURCE    REFSEQ: accession NM_001145305.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1134)
  AUTHORS   Li,Q., Wang,Y., Zheng,W., Guo,J., Zhang,S., Gong,F., Lu,G.X.,
            Lin,G. and Dai,J.
  TITLE     Biallelic variants in IQCN cause sperm flagellar assembly defects
            and male infertility
  JOURNAL   Hum Reprod 38 (7), 1390-1398 (2023)
   PUBMED   37140151
  REMARK    GeneRIF: Biallelic variants in IQCN cause sperm flagellar assembly
            defects and male infertility.
REFERENCE   2  (residues 1 to 1134)
  AUTHORS   Wang,Y., Chen,G., Tang,Z., Mei,X., Lin,C., Kang,J., Lian,J., Lu,J.,
            Liu,Y., Lan,F., Huang,W. and Zhang,D.
  TITLE     Loss-of-function mutations in IQCN cause male infertility in humans
            and mice owing to total fertilization failure
  JOURNAL   Mol Hum Reprod 29 (7) (2023)
   PUBMED   37184908
  REMARK    GeneRIF: Loss-of-function mutations in IQCN cause male infertility
            in humans and mice owing to total fertilization failure.
REFERENCE   3  (residues 1 to 1134)
  AUTHORS   Dai,J., Li,Q., Zhou,Q., Zhang,S., Chen,J., Wang,Y., Guo,J., Gu,Y.,
            Gong,F., Tan,Y., Lu,G., Zheng,W. and Lin,G.
  TITLE     IQCN disruption causes fertilization failure and male infertility
            due to manchette assembly defect
  JOURNAL   EMBO Mol Med 14 (12), e16501 (2022)
   PUBMED   36321563
REFERENCE   4  (residues 1 to 1134)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1134)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1134)
  AUTHORS   de Mateo,S., Castillo,J., Estanyol,J.M., Ballesca,J.L. and Oliva,R.
  TITLE     Proteomic characterization of the human sperm nucleus
  JOURNAL   Proteomics 11 (13), 2714-2726 (2011)
   PUBMED   21630459
REFERENCE   7  (residues 1 to 1134)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1134)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC403083.1, AK302431.1, BC127100.1 and AL136867.1.
            
            Transcript Variant: This variant (3) has multiple differences
            compared to variant 1. These differences result in a distinct 5'
            UTR, translation initiation at a downstream start codon and lack of
            an internal in-frame segment, compared to variant 1. The encoded
            protein (isoform c) is shorter than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302431.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1134
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..1134
                     /product="IQ domain-containing protein N isoform c"
                     /note="IQ domain-containing protein N"
                     /calculated_mol_wt=122770
     Region          <34..>138
                     /region_name="Adgb_C_mid-like"
                     /note="C-terminal middle region of Androglobins (Adgbs)
                     and related proteins; including permuted globin domain and
                     IQ motif; cd22307"
                     /db_xref="CDD:412094"
     Region          51..85
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          62..80
                     /region_name="IQ motif"
                     /note="IQ motif [structural motif]"
                     /db_xref="CDD:412094"
     Region          82..117
                     /region_name="globin helix A"
                     /note="globin helix A [structural motif]"
                     /db_xref="CDD:412094"
     Region          118..129
                     /region_name="globin helix B"
                     /note="globin helix B [structural motif]"
                     /db_xref="CDD:412094"
     Region          <230..512
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          <305..816
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          883..901
                     /region_name="IQ"
                     /note="IQ calmodulin-binding motif; pfam00612"
                     /db_xref="CDD:459869"
     Region          <904..>925
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     Region          <928..>948
                     /region_name="IQCD"
                     /note="IQ (isoleucine-glutamine) motif containing D
                     (IQCD); cd23767"
                     /db_xref="CDD:467745"
     CDS             1..1134
                     /gene="IQCN"
                     /gene_synonym="KIAA1683; SPGF78"
                     /coded_by="NM_001145305.2:337..3741"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46018.1"
                     /db_xref="GeneID:80726"
                     /db_xref="HGNC:HGNC:29350"
                     /db_xref="MIM:620160"
ORIGIN      
        1 mekappqpqh eglkskehlp qqpaegktas rrvprlravv esqafknilv demdmmhara
       61 atliqanwrg ywlrqklisq mmaakaiqea wrrfnkrhil hsskslvkkt raeegdipyh
      121 apqqvrfqhp eenrllsppi mvnketqfps cdnlvlcrpq sspllqppaa qgtpepcvqg
      181 phaarvrgla flphqtvtir fpcpvsldak cqpclltrti rstclvhieg dsvktkrvsa
      241 rtnkarapet plsrrydqav trpsraqtqg pvkaetpkap fqicpgpmit ktllqtypvv
      301 svtlpqtypa stmtttppkt spvpkvtiik tpaqmypgpt vtktaphtcp mptmtkiqvh
      361 ptasrtgtpr qtcpatitak nrpqvsllas imkslpqvcp gpamaktppq mhpvttpakn
      421 plqtclsatm sktssqrspv gvtkpspqtr lpamitktpa qlrsvatilk tlclasptva
      481 nvkappqvav aagtpntsgs ihenppkaka tvnvkqaakv vkasspsyla egkirclaqp
      541 hpgtgvpraa aelpleaeki ktgtqkqakt dmafktsvav emagapswtk vaeegdkpph
      601 vyvpvdmavt lprgqlaapl tnassqrhpp clsqrplaap ltkassqghl pteltktpsl
      661 ahldtclskm hsqthlatga vkvqsqapla tcltktqsrg qpitdittcl ipahqaadls
      721 snthsqvllt gskvsnhacq rlgglsappw akpedrqtqp qphghvpgkt tqggpcpaac
      781 evqgmlvppm aptghstcnv eswgdngatr aqpsmpgqav pcqedtgpad agvvggqswn
      841 rawepargaa swdtwrnkav vpprrsgepm vsmqaaeeir ilavitiqag vrgylarrri
      901 rlwhrgamvi qatwrgyrvr rnlahlcrat ttiqsawrgy strrdqarhw qmlhpvtwve
      961 lgsragvmsd rswfqdgrar tvsdhrcfqs cqahacsvch slssrigspp svvmlvgssp
     1021 rtchtcgrtq ptrvvqgmgq gtegpgavsw asayqlaals prqphrqdka ataiqsawrg
     1081 fkirqqmrqq qmaakivqat wrghhtrscl knteallgpa dpsassrhmh wpgi
//
LOCUS       NP_932065                847 aa            linear   PRI 20-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 4 [Homo sapiens].
ACCESSION   NP_932065
VERSION     NP_932065.1
DBSOURCE    REFSEQ: accession NM_197961.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 847)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 847)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 847)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 847)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 847)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 847)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 847)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 847)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 847)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 847)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC030688.2, AC105129.4 and
            BU753778.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) contains an alternate exon in
            the 5' UTR and 5' coding region and lacks an exon in the 3' coding
            region compared to variant 1. These diferences result in the use of
            an alternate start codon compared to variant 1. The encoded isoform
            (4) is shorter and has a distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030688.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..847
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..847
                     /product="dipeptidyl peptidase 8 isoform 4"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=97333
     Region          8..162
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          175..595
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          634..>706
                     /region_name="FrsA"
                     /note="Fermentation-respiration switch esterase FrsA,
                     DUF1100 family [Signal transduction mechanisms]; COG1073"
                     /db_xref="CDD:440691"
     Region          687..840
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..847
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_197961.4:304..2847"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS10208.1"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 mwkrseqmki ksgkcnmaaa meteqlgvei fetadceeni esqdrpklep fyveryswsq
       61 lkklladtrk yhgymmakap hdfmfvkrnd pdgphsdriy ylamsgenre ntlfyseipk
      121 tinraavlml swkplldlfq atldygmysr eeellrerkr igtvgiasyd yhqgsgtflf
      181 qagsgiyhvk dggpqgftqq plrpnlvets cpnirmdpkl cpadpdwiaf ihsndiwisn
      241 ivtreerrlt yvhnelanme edarsagvat fvlqeefdry sgywwcpkae ttpsggkilr
      301 ilyeendese veiihvtspm letrradsfr ypktgtanpk vtfkmseimi daegriidvi
      361 dkeliqpfei lfegveyiar agwtpegkya wsilldrsqt rlqivlispe lfipveddvm
      421 erqrliesvp dsvtpliiye ettdiwinih difhvfpqsh eeeiefifas ecktgfrhly
      481 kitsilkesk ykrssgglpa psdfkcpike eiaitsgewe vlgrhgsniq vdevrrlvyf
      541 egtkdspleh hlyvvsyvnp gevtrltdrg yshsccisqh cdffiskysn qknphcvsly
      601 klsspeddpt cktkefwati ldsagplpdy tppeifsfes ttgftlygml ykphdlqpgk
      661 kyptvlfiyg gpqvqlvnnr fkgvkyfrln tlaslgyvvv vidnrgschr glkfegafky
      721 kmvaiagapv tlwifydtgy terymghpdq neqgyylgsv amqaekfpse pnrllllhgf
      781 ldenvhfaht sillsflvra gkpydlqiyp qerhsirvpe sgehyelhll hylqenlgsr
      841 iaalkvi
//
LOCUS       NP_689943               1257 aa            linear   PRI 20-NOV-2025
DEFINITION  protein broad-minded isoform 1 [Homo sapiens].
ACCESSION   NP_689943
VERSION     NP_689943.4
DBSOURCE    REFSEQ: accession NM_152730.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1257)
  AUTHORS   Bocquet,B., Borday,C., Erkilic,N., Mamaeva,D., Donval,A.,
            Masson,C., Parain,K., Kaminska,K., Quinodoz,M., Perea-Romero,I.,
            Garcia-Garcia,G., Jimenez-Medina,C., Boukhaddaoui,H., Coget,A.,
            Leboucq,N., Calzetti,G., Gandolfi,S., Percesepe,A., Barili,V.,
            Uliana,V., Delsante,M., Bozzetti,F., Scholl,H.P., Corton,M.,
            Ayuso,C., Millan,J.M., Rivolta,C., Meunier,I., Perron,M. and
            Kalatzis,V.
  TITLE     TBC1D32 variants disrupt retinal ciliogenesis and cause retinitis
            pigmentosa
  JOURNAL   JCI Insight 8 (21), e169426 (2023)
   PUBMED   37768732
  REMARK    GeneRIF: TBC1D32 variants disrupt retinal ciliogenesis and cause
            retinitis pigmentosa.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1257)
  AUTHORS   Satoda,Y., Noguchi,T., Fujii,T., Taniguchi,A., Katoh,Y. and
            Nakayama,K.
  TITLE     BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1
  JOURNAL   Mol Biol Cell 33 (9), ar79 (2022)
   PUBMED   35609210
  REMARK    GeneRIF: BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1.
REFERENCE   3  (residues 1 to 1257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1257)
  AUTHORS   Alsahan,N. and Alkuraya,F.S.
  TITLE     Confirming TBC1D32-related ciliopathy in humans
  JOURNAL   Am J Med Genet A 182 (8), 1985-1987 (2020)
   PUBMED   32573025
  REMARK    GeneRIF: Confirming TBC1D32-related ciliopathy in humans.
REFERENCE   5  (residues 1 to 1257)
  AUTHORS   Hietamaki,J., Gregory,L.C., Ayoub,S., Iivonen,A.P., Vaaralahti,K.,
            Liu,X., Brandstack,N., Buckton,A.J., Laine,T., Kansakoski,J.,
            Hero,M., Miettinen,P.J., Varjosalo,M., Wakeling,E., Dattani,M.T.
            and Raivio,T.
  TITLE     Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism
  JOURNAL   J Clin Endocrinol Metab 105 (6), 1748-1758 (2020)
   PUBMED   32060556
  REMARK    GeneRIF: Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism.
REFERENCE   6  (residues 1 to 1257)
  AUTHORS   Shaheen,R., Jiang,N., Alzahrani,F., Ewida,N., Al-Sheddi,T.,
            Alobeid,E., Musaev,D., Stanley,V., Hashem,M., Ibrahim,N.,
            Abdulwahab,F., Alshenqiti,A., Sonmez,F.M., Saqati,N., Alzaidan,H.,
            Al-Qattan,M.M., Al-Mohanna,F., Gleeson,J.G. and Alkuraya,F.S.
  TITLE     Bi-allelic Mutations in FAM149B1 Cause Abnormal Primary Cilium and
            a Range of Ciliopathy Phenotypes in Humans
  JOURNAL   Am J Hum Genet 104 (4), 731-737 (2019)
   PUBMED   30905400
REFERENCE   7  (residues 1 to 1257)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1257)
  AUTHORS   Adly,N., Alhashem,A., Ammari,A. and Alkuraya,F.S.
  TITLE     Ciliary genes TBC1D32/C6orf170 and SCLT1 are mutated in patients
            with OFD type IX
  JOURNAL   Hum Mutat 35 (1), 36-40 (2014)
   PUBMED   24285566
  REMARK    GeneRIF: study identified 2 cases with a severe ciliopathy
            phenotype consistent with oro-facio-digital syndrome type IX; the
            autozygome of each index harbored a single truncating variant and
            the affected genes (SCLT1 and TBC1D32/C6orf170) have roles in
            centrosomal biology and ciliogenesis; findings suggest a role of
            SCLT1 and TBC1D32 in ciliopathy pathogenesis
REFERENCE   9  (residues 1 to 1257)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   10 (residues 1 to 1257)
  AUTHORS   Ko,H.W., Norman,R.X., Tran,J., Fuller,K.P., Fukuda,M. and
            Eggenschwiler,J.T.
  TITLE     Broad-minded links cell cycle-related kinase to cilia assembly and
            hedgehog signal transduction
  JOURNAL   Dev Cell 18 (2), 237-247 (2010)
   PUBMED   20159594
  REMARK    GeneRIF: Studies in mouse and zebrafish implicate that TBC1D32 is
            involved in sonic hedgehog signaling.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK091554.1, AK131446.1,
            AL589910.9, AK055461.1, AK126259.1, AL035593.11 and BX112581.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 3, 2006 this sequence version replaced NP_689943.3.
            
            Summary: This gene encodes a TBC-domain containing protein. Studies
            of a similar protein in mouse and zebrafish suggest that the
            encoded protein is involved in sonic hedgehog signaling, and that
            it interacts with and stabilizes cell cycle-related kinase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript but encodes the supported protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000398212.7/ ENSP00000381270.2
            RefSeq Select criteria    :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..1257
                     /product="protein broad-minded isoform 1"
                     /note="protein broad-minded; broad-minded homolog"
                     /calculated_mol_wt=144626
     Region          12..1254
                     /region_name="BROMI"
                     /note="Broad-minded protein; pfam14961"
                     /db_xref="CDD:464406"
     Region          131..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96NH3.4)"
     CDS             1..1257
                     /gene="TBC1D32"
                     /gene_synonym="ALHSA; BROMI; C6orf170; C6orf171; OFD9;
                     RP100"
                     /coded_by="NM_152730.6:51..3824"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43501.1"
                     /db_xref="GeneID:221322"
                     /db_xref="HGNC:HGNC:21485"
                     /db_xref="MIM:615867"
ORIGIN      
        1 mahfssedqa mlqamlrrlf qsvkekitga pslecaeeil lhleetdenf hnyefvkylr
       61 qhigntlgsm ieeemekcts drnqgeecgy dtvvqqvtkr tqeskeykem mhylknimia
      121 vvesminkfe edetrnqerq kkiqkekshs yrtdncsdsd sslnqsykfc qgklqlildq
      181 ldpgqpkevr yealqtlcsa ppsdvlncen wttlcekltv slsdpdpvfs drilkfcaqt
      241 fllsplhmtk eiytslakyl esyflsrenh iptlsagvdi tnpnmtrllk kvrllneyqk
      301 eapsfwirhp ekymeeives tlslltvkhn qshvvsqkil dpiyffalvd tkavwfkkwm
      361 hahysrttvl rlletkyksl vttaiqqcvq yfemcktrka detlghskhc rnkqktfyyl
      421 gqelqyiyfi hslcllgrll iykqgrklfp iklknkkglv slidllvlft qliyyspscp
      481 kmtsaahsen yspasmvtev lwilsdqkec aveclynniv ietllqpihn lmkgneaspn
      541 csetalihia gilariasve eglilllyga nmnsseespt gahiiaqfsk klldedisif
      601 sgsemlpvvk gafisvcrhi ystceglqvl itynlhesia kawkktslls eriptpvegs
      661 dsvssvsqes qnimawednl lddllhfaat pkgllllqrt gainecvtfi fnryakklqv
      721 srhkkfgygv lvtrvastaa ggialkksgf inelitelws nleygrddvr vthprttpvd
      781 pidrscqksf lalvnllsyp aiyelvrnqd lpnkteyslr evptcvidii drliilnsea
      841 kirslfnyeq shifglrdfi idglsvernh vlvrinlvgg plerilpprl leksdnpypw
      901 pmfssyplpn cylsditrna gikqdndldk lllclkisdk qtewiencqr qfckmmkakp
      961 diisgealie llekfvlhlt espsecyfps veytatdanv kneslssvqq lgikmtvryg
     1021 kflsllkdga endltwvlkh cerflkqqqt sikssllclq gnyaghdwfv sslfmimlgd
     1081 kektfqflhq fsrlltsafl wlprlhissy lpndtvesgi hpvyfcsthy iemllkaelp
     1141 lvfsafhmsg fapsqiclqw itqcfwnyld wieichyiat cvflgpdyqv yiciavfkhl
     1201 qqdilqhtqt qdlqvflkee alhgfrvsdy feymeileqn yrtvllrdmr nirlqst
//
LOCUS       NP_001290340             276 aa            linear   PRI 20-NOV-2025
DEFINITION  regulation of nuclear pre-mRNA domain-containing protein 1A isoform
            2 [Homo sapiens].
ACCESSION   NP_001290340 XP_005258351
VERSION     NP_001290340.1
DBSOURCE    REFSEQ: accession NM_001303411.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Feng,X., Jiang,T., Yang,C., Pang,S., Ding,Z., Hu,H., Wang,H.,
            Dong,L. and Yang,N.
  TITLE     RPRD1A stabilizes NRF2 and aggravates HCC progression through
            competing with p62 for TRIM21 binding
  JOURNAL   Cell Death Dis 13 (1), 6 (2021)
   PUBMED   34921137
  REMARK    GeneRIF: RPRD1A stabilizes NRF2 and aggravates HCC progression
            through competing with p62 for TRIM21 binding.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Behr,E.R., Ritchie,M.D., Tanaka,T., Kaab,S., Crawford,D.C.,
            Nicoletti,P., Floratos,A., Sinner,M.F., Kannankeril,P.J.,
            Wilde,A.A., Bezzina,C.R., Schulze-Bahr,E., Zumhagen,S.,
            Guicheney,P., Bishopric,N.H., Marshall,V., Shakir,S.,
            Dalageorgou,C., Bevan,S., Jamshidi,Y., Bastiaenen,R.,
            Myerburg,R.J., Schott,J.J., Camm,A.J., Steinbeck,G., Norris,K.,
            Altman,R.B., Tatonetti,N.P., Jeffery,S., Kubo,M., Nakamura,Y.,
            Shen,Y., George,A.L. Jr. and Roden,D.M.
  TITLE     Genome wide analysis of drug-induced torsades de pointes: lack of
            common variants with large effect sizes
  JOURNAL   PLoS One 8 (11), e78511 (2013)
   PUBMED   24223155
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Zhang,X., Cao,Q., Liu,X., Liu,S., Wang,J., Sun,S., Wang,O.,
            Tian,Z., Liu,H., Kuang,J. and Zhang,W.
  TITLE     Cellular and molecular evidence for malignancy-inhibitory functions
            of p15RS
  JOURNAL   Cell Cycle 11 (10), 1988-1998 (2012)
   PUBMED   22580456
  REMARK    GeneRIF: The p15RS expression specifically downregulates the
            expression of cathepsin B and MMP-9 at RNA levels, which are known
            to promote cell invasion through degrading extracellular matrix
            proteins.
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Ni,Z., Olsen,J.B., Guo,X., Zhong,G., Ruan,E.D., Marcon,E.,
            Young,P., Guo,H., Li,J., Moffat,J., Emili,A. and Greenblatt,J.F.
  TITLE     Control of the RNA polymerase II phosphorylation state in promoter
            regions by CTD interaction domain-containing proteins RPRD1A and
            RPRD1B
  JOURNAL   Transcription 2 (5), 237-242 (2011)
   PUBMED   22231121
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Wu,Y., Zhang,Y., Zhang,H., Yang,X., Wang,Y., Ren,F., Liu,H.,
            Zhai,Y., Jia,B., Yu,J. and Chang,Z.
  TITLE     p15RS attenuates Wnt/{beta}-catenin signaling by disrupting
            {beta}-catenin.TCF4 Interaction
  JOURNAL   J Biol Chem 285 (45), 34621-34631 (2010)
   PUBMED   20739273
  REMARK    GeneRIF: p15RS inhibits Wnt signaling by interrupting
            beta-catenin.TCF4 complex formation and that Wnt signaling
            initiates downstream gene expression by removing p15RS from
            promoters.
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Liu,J., Liu,H., Zhang,X., Gao,P., Wang,J. and Hu,Z.
  TITLE     Identification and characterization of P15RS, a novel P15(INK4b)
            related gene on G1/S progression
  JOURNAL   Biochem Biophys Res Commun 299 (5), 880-885 (2002)
   PUBMED   12470661
  REMARK    GeneRIF: molecular cloning and characterization of P15RS, a novel
            P15(INK4b) related gene involved in G1/S progression
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB444937.1, AC091060.10,
            AK292907.1, AF419845.1 and BC000225.1.
            
            On Jan 1, 2015 this sequence version replaced XP_005258351.1.
            
            Summary: This gene encodes a cell-cycle and transcription
            regulatory protein. The encoded protein interacts with the cell
            cycle inhibitor cyclin-dependent kinase 4 inhibitor B and may
            function as a negative regulator of G(1)/S phase progression. This
            protein also forms homo- and hetrodimers with the protein,
            regulation of nuclear pre-mRNA domain-containing protein 1B, to
            form a scaffold that interacts with the C-terminal domain of RNA
            polymerase II subunit B1 and regulates several aspects of
            transcription. Alternate splicing results in multiple transcript
            variants. A pseudogene of this gene is found on chromosome 16.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (2) uses an alternate exon in the
            5' UTR and 5' coding region which results in the use of an
            alternate start codon compare to variant 1. The encoded isoform (2)
            is shorter and has a distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.14425.1,
                                           SRR11853563.15613.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..276
                     /product="regulation of nuclear pre-mRNA domain-containing
                     protein 1A isoform 2"
                     /note="regulation of nuclear pre-mRNA domain-containing
                     protein 1A; cyclin-dependent kinase 2B-inhibitor-related
                     protein; p15INK4B-related protein; CDKN2B-related protein;
                     Cyclin-dependent kinase inhibitor 2B-related protein
                     (p15INK4B-related protein)"
                     /calculated_mol_wt=31494
     Region          <15..95
                     /region_name="VHS_ENTH_ANTH"
                     /note="VHS, ENTH and ANTH domain superfamily; cl02544"
                     /db_xref="CDD:470608"
     Region          129..274
                     /region_name="CREPT"
                     /note="Cell-cycle alteration and expression-elevated
                     protein in tumour; pfam16566"
                     /db_xref="CDD:465181"
     CDS             1..276
                     /gene="RPRD1A"
                     /gene_synonym="HsT3101; P15RS"
                     /coded_by="NM_001303411.2:323..1153"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77178.1"
                     /db_xref="GeneID:55197"
                     /db_xref="HGNC:HGNC:25560"
                     /db_xref="MIM:610347"
ORIGIN      
        1 mrnsnwrfcq tgiyskpnrk ltflylandv iqnskrkgpe ftkdfapviv eafkhvsset
       61 desckkhlgr vlsiweersv yendvleqlk qalygdkkpr krtyeqikvd enencsslgs
      121 pseppqtldl vralqdlena asgdaavhqr iaslpvevqe vslldkitdk esgerlskmv
      181 edacmllady ngrlaaeidd rkqltrmlad flrcqkeala ekehkleeyk rklarvslvr
      241 kelrsriqsl pdlsrlpnvt gshmhlpfag diysed
//
LOCUS       NP_476518               1136 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog B isoform Par3Lc [Homo sapiens].
ACCESSION   NP_476518
VERSION     NP_476518.4
DBSOURCE    REFSEQ: accession NM_057177.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1136)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   2  (residues 1 to 1136)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1136)
  AUTHORS   Thompson,B.J.
  TITLE     Par-3 family proteins in cell polarity & adhesion
  JOURNAL   FEBS J 289 (3), 596-613 (2022)
   PUBMED   33565714
  REMARK    GeneRIF: Par-3 family proteins in cell polarity & adhesion.
            Review article
REFERENCE   4  (residues 1 to 1136)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   5  (residues 1 to 1136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1136)
  AUTHORS   Izaki,T., Kamakura,S., Kohjima,M. and Sumimoto,H.
  TITLE     Phosphorylation-dependent binding of 14-3-3 to Par3beta, a human
            Par3-related cell polarity protein
  JOURNAL   Biochem Biophys Res Commun 329 (1), 211-218 (2005)
   PUBMED   15721295
  REMARK    GeneRIF: binding of 14-3-3 to Par3beta is dependent on
            phosphorylation
REFERENCE   7  (residues 1 to 1136)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 1136)
  AUTHORS   Kohjima,M., Noda,Y., Takeya,R., Saito,N., Takeuchi,K. and
            Sumimoto,H.
  TITLE     PAR3beta, a novel homologue of the cell polarity protein PAR3,
            localizes to tight junctions
  JOURNAL   Biochem Biophys Res Commun 299 (4), 641-646 (2002)
   PUBMED   12459187
  REMARK    GeneRIF: PAR3beta, expressed intrinsically or extrinsically,
            localizes to the tight junctions, indicating that the localization
            does not require the ternary complex formation.
REFERENCE   9  (residues 1 to 1136)
  AUTHORS   Gao,L., Macara,I.G. and Joberty,G.
  TITLE     Multiple splice variants of Par3 and of a novel related gene,
            Par3L, produce proteins with different binding properties
  JOURNAL   Gene 294 (1-2), 99-107 (2002)
   PUBMED   12234671
REFERENCE   10 (residues 1 to 1136)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016903.3, AC007736.3, AC009316.3, AC011750.8, AC008171.3,
            AC007465.4, AC007746.4 and AC007385.3.
            
            On Dec 8, 2006 this sequence version replaced NP_476518.3.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (Par3Lc) is
            shorter compared to isoform Par3La.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2153307,
                              SAMN03267750 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..1136
                     /product="partitioning defective 3 homolog B isoform
                     Par3Lc"
                     /note="partitioning-defective 3-beta; amyotrophic lateral
                     sclerosis 2 (juvenile) chromosome region, candidate 19;
                     partitioning defective 3 homolog B; PAR3-L protein;
                     partitioning defective 3-like protein; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 19 protein;
                     par-3 partitioning defective 3 homolog B"
                     /calculated_mol_wt=124740
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          83..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          137..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          197..294
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(212..218,234,237,267,271,274..275)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          318..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          377..469
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(392..398,413,416,446,450,453..454)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          492..591
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(508..514,530,533,563,567,570..571)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     CDS             1..1136
                     /gene="PARD3B"
                     /gene_synonym="ALS2CR19; PAR3B; PAR3beta; PAR3L"
                     /coded_by="NM_057177.7:526..3936"
                     /note="isoform Par3Lc is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42805.1"
                     /db_xref="GeneID:117583"
                     /db_xref="HGNC:HGNC:14446"
                     /db_xref="MIM:619353"
ORIGIN      
        1 mkvtvcfgrt givvpckegq lrvgeltqqa lqrylktrek gpgywvkihh leytdggild
       61 pddvladvve dkdkliavfe eqeplhkies psgnpadrqs pdafetevaa qlaafkpigg
      121 eievtpsalk lgtpllvrrs sdpvpgppad tqpsashpgg qslklvvpds tqnledrevl
      181 ngvqtellts prtkdtlsdm trtveisgeg gplgihvvpf fsslsgrilg lfirgiedns
      241 rskreglfhe necivkinnv dlvdktfaqa qdvfrqamks psvllhvlpp qnreqyeksv
      301 igslnifgnn dgvlktkvpp pvhgksglkt anltgtdspe tdasaslqqn ksprvprlgg
      361 kpsspslspl mgfgsnknak kikidlkkgp eglgftvvtr dssihgpgpi fvknilpkga
      421 aikdgrlqsg drilevngrd vtgrtqeelv amlrstkqge taslviarqe ghflprelkg
      481 epdccalsle tseqltfeip lndsgsaglg vslkgnksre tgtdlgifik siihggaafk
      541 dgrlrmndql iavngesllg ksnheametl rrsmsmegni rgmiqlvilr rperpmedpa
      601 ecgafskpcf encqnavtts rrndnsilhp lgtcspqdkq kglllpndgw aesevppspt
      661 phsalglgle dyshssgvds avyfpdqhin frsvtparqp esinlkasks mdlvpdeskv
      721 hslagqksdg lsdksshsgq galncesapq gnseledmen karkvkktke kekkkekgkl
      781 kvkekkrkee nedperkikk kgfgamlrfg kkkedkggka eqkgtlkhgg lreeelekmk
      841 eererigakh qelrekqarg lldyatgaig svydmdddem dpnyarvnhf repctsanvf
      901 rspsppragp fgyprdghpl sperdhlegl yakvnkpyhp lvpadsgrpt ggstdriqkl
      961 rkeyyqarre gfplyeddeg rarpseydll wvpgrgpdgn ahnlrfegme rqyaslprgg
     1021 padpvdylpa aprglykere lpyypgahpm hppkgsyprp telrvadlry pqhyppppap
     1081 qhkgpfrqdv ppsppqhqrm payqetgrpg prggspdqyp yrtqdsrqkn pmtaav
//
LOCUS       NP_001290400             103 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin-like protein 4A isoform 2 [Homo sapiens].
ACCESSION   NP_001290400 XP_005266702
VERSION     NP_001290400.1
DBSOURCE    REFSEQ: accession NM_001303471.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Wood,K.A., Ellingford,J.M., Thomas,H.B., Douzgou,S., Beaman,G.M.,
            Hobson,E., Prescott,K., O'Keefe,R.T. and Newman,W.G.
  CONSRTM   Genomics UK Research Consortium
  TITLE     Expanding the genotypic spectrum of TXNL4A variants in Burn-McKeown
            syndrome
  JOURNAL   Clin Genet 101 (2), 255-259 (2022)
   PUBMED   34713892
  REMARK    GeneRIF: Expanding the genotypic spectrum of TXNL4A variants in
            Burn-McKeown syndrome.
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Wieczorek,D., Newman,W.G., Wieland,T., Berulava,T., Kaffe,M.,
            Falkenstein,D., Beetz,C., Graf,E., Schwarzmayr,T., Douzgou,S.,
            Clayton-Smith,J., Daly,S.B., Williams,S.G., Bhaskar,S.S.,
            Urquhart,J.E., Anderson,B., O'Sullivan,J., Boute,O., Gundlach,J.,
            Czeschik,J.C., van Essen,A.J., Hazan,F., Park,S., Hing,A.,
            Kuechler,A., Lohmann,D.R., Ludwig,K.U., Mangold,E., Steenpass,L.,
            Zeschnigk,M., Lemke,J.R., Lourenco,C.M., Hehr,U., Prott,E.C.,
            Waldenberger,M., Bohmer,A.C., Horsthemke,B., O'Keefe,R.T.,
            Meitinger,T., Burn,J., Ludecke,H.J. and Strom,T.M.
  TITLE     Compound heterozygosity of low-frequency promoter deletions and
            rare loss-of-function mutations in TXNL4A causes Burn-McKeown
            syndrome
  JOURNAL   Am J Hum Genet 95 (6), 698-707 (2014)
   PUBMED   25434003
  REMARK    GeneRIF: Reporter gene and in vivo assays showed that the promoter
            deletions led to reduced expression of TXNL4A. Depletion of TXNL4A
            (Dib1) in yeast demonstrated reduced assembly of the tri-snRNP
            complex.
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Zhang,Y., Lindblom,T., Chang,A., Sudol,M., Sluder,A.E. and
            Golemis,E.A.
  TITLE     Evidence that dim1 associates with proteins involved in pre-mRNA
            splicing, and delineation of residues essential for dim1
            interactions with hnRNP F and Npw38/PQBP-1
  JOURNAL   Gene 257 (1), 33-43 (2000)
   PUBMED   11054566
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Reuter,K., Nottrott,S., Fabrizio,P., Luhrmann,R. and Ficner,R.
  TITLE     Identification, characterization and crystal structure analysis of
            the human spliceosomal U5 snRNP-specific 15 kD protein
  JOURNAL   J Mol Biol 294 (2), 515-525 (1999)
   PUBMED   10610776
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Zhang,Y.Z., Gould,K.L., Dunbrack,R.L. Jr., Cheng,H., Roder,H. and
            Golemis,E.A.
  TITLE     The evolutionarily conserved Dim1 protein defines a novel branch of
            the thioredoxin fold superfamily
  JOURNAL   Physiol Genomics 1 (3), 109-118 (1999)
   PUBMED   11015569
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Ludecke,H.J. and Wieczorek,D.
  TITLE     TXNL4A-Related Craniofacial Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413799
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF972457.1, BE385528.1,
            AK309098.1, BC001046.2 and AC090360.9.
            
            On Jan 7, 2015 this sequence version replaced XP_005266702.1.
            
            Summary: The protein encoded by this gene is a member of the U5
            small ribonucleoprotein particle (snRNP), and is involved in
            pre-mRNA splicing. This protein contains a thioredoxin-like fold
            and it is expected to interact with multiple proteins.
            Protein-protein interactions have been observed with the
            polyglutamine tract-binding protein 1 (PQBP1). Mutations in both
            the coding region and promoter region of this gene have been
            associated with Burn-McKeown syndrome, which is a rare disorder
            characterized by craniofacial dysmorphisms, cardiac defects,
            hearing loss, and bilateral choanal atresia. A pseudogene of this
            gene is found on chromosome 2. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (2) contains an alternate exon in
            its 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.161379.1,
                                           SRR1803614.44165.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q23"
     Protein         1..103
                     /product="thioredoxin-like protein 4A isoform 2"
                     /note="thioredoxin-like 4; DIM1 protein homolog;
                     thioredoxin-like U5 snRNP protein U5-15kD; spliceosomal U5
                     snRNP-specific 15 kDa protein"
                     /calculated_mol_wt=12022
     Region          <13..103
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     CDS             1..103
                     /gene="TXNL4A"
                     /gene_synonym="BMKS; DIB1; DIM1; SNRNP15; TXNL4; U5-15kD"
                     /coded_by="NM_001303471.3:438..749"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10907"
                     /db_xref="HGNC:HGNC:30551"
                     /db_xref="MIM:611595"
ORIGIN      
        1 mllarkqilc vnvknfaviy lvditevpdf nkmyelydpc tvmfffrnkh imidlgtgnn
       61 nkinwamedk qemvdiietv yrgarkgrgl vvspkdystk yry
//
LOCUS       NP_000285                406 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphorylase b kinase gamma catalytic chain, liver/testis isoform
            isoform 1 [Homo sapiens].
ACCESSION   NP_000285
VERSION     NP_000285.1
DBSOURCE    REFSEQ: accession NM_000294.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Zhu,W., Liu,D., Lu,Y., Sun,J., Zhu,J., Xing,Y., Ma,X., Wang,Y.,
            Ji,M. and Jia,Y.
  TITLE     PHKG2 regulates RSL3-induced ferroptosis in Helicobacter pylori
            related gastric cancer
  JOURNAL   Arch Biochem Biophys 740, 109560 (2023)
   PUBMED   36948350
  REMARK    GeneRIF: PHKG2 regulates RSL3-induced ferroptosis in Helicobacter
            pylori related gastric cancer.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 406)
  AUTHORS   van den Berg,I.E., van Beurden,E.A., Malingre,H.E., van
            Amstel,H.K., Poll-The,B.T., Smeitink,J.A., Lamers,W.H. and
            Berger,R.
  TITLE     X-linked liver phosphorylase kinase deficiency is associated with
            mutations in the human liver phosphorylase kinase alpha subunit
  JOURNAL   Am J Hum Genet 56 (2), 381-387 (1995)
   PUBMED   7847371
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Herbert,M., Goldstein,J.L., Rehder,C., Austin,S., Kishnani,P.S. and
            Bali,D.S.
  TITLE     Phosphorylase Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21634085
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Hanks,S.K.
  TITLE     Messenger ribonucleic acid encoding an apparent isoform of
            phosphorylase kinase catalytic subunit is abundant in the adult
            testis
  JOURNAL   Mol Endocrinol 3 (1), 110-116 (1989)
   PUBMED   2915644
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Hanks,S.K.
  TITLE     Homology probing: identification of cDNA clones encoding members of
            the protein-serine kinase family
  JOURNAL   Proc Natl Acad Sci U S A 84 (2), 388-392 (1987)
   PUBMED   2948189
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Sovik,O., deBarsy,T. and Maehle,B.
  TITLE     Phosphorylase kinase deficiency: severe glycogen storage disease
            with evidence of autosomal recessive mode of inheritance
  JOURNAL   Eur J Pediatr 139 (3), 210 (1982)
   PUBMED   6962066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106886.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Phosphorylase kinase is a polymer of 16 subunits, four
            each of alpha, beta, gamma and delta. The alpha subunit includes
            the skeletal muscle and hepatic isoforms, encoded by two different
            genes. The beta subunit is the same in both the muscle and hepatic
            isoforms, and encoded by one gene. The gamma subunit also includes
            the skeletal muscle and hepatic isoforms, and the hepatic isoform
            is encoded by this gene. The delta subunit is a calmodulin and can
            be encoded by three different genes. The gamma subunits contain the
            active site of the enzyme, whereas the alpha and beta subunits have
            regulatory functions controlled by phosphorylation. The delta
            subunit mediates the dependence of the enzyme on calcium
            concentration. Mutations in this gene cause glycogen storage
            disease type 9C, also known as autosomal liver glycogenosis.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified in this gene.[provided by RefSeq, Feb
            2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.76650.1,
                                           SRR1803615.213690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000563588.6/ ENSP00000455607.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..406
                     /product="phosphorylase b kinase gamma catalytic chain,
                     liver/testis isoform isoform 1"
                     /EC_number="2.7.11.19"
                     /note="Phosphorylase kinase, gamma 2 (testis/liver);
                     phosphorylase kinase gamma subunit 2; PSK-C3; PHK-gamma-T;
                     phosphorylase kinase, gamma 2 (testis); phosphorylase
                     kinase subunit gamma-2; serine/threonine-protein kinase
                     PHKG2; PHK-gamma-LT"
                     /calculated_mol_wt=46311
     Region          13..291
                     /region_name="STKc_PhKG2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Phosphorylase kinase Gamma 2 subunit; cd14181"
                     /db_xref="CDD:271083"
     Site            order(30..31,33..34,36,38,51,53,91,107..108,110,114,116,
                     152..153,155,157..158,160,171,174,186..192,194)
                     /site_type="active"
                     /db_xref="CDD:271083"
     Site            order(30..31,33..34,36,38,51,53,91,107..108,110,114,153,
                     155,157..158,160,171)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271083"
     Site            order(34,114,116,152..153,155,157,174,186..192,194)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271083"
     Site            170..192
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271083"
     Region          306..330
                     /region_name="Calmodulin-binding (domain-N).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15735.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15735.1)"
     Region          346..370
                     /region_name="Calmodulin-binding (domain-C).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15735.1)"
     CDS             1..406
                     /gene="PHKG2"
                     /gene_synonym="GSD9C"
                     /coded_by="NM_000294.3:85..1305"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10690.1"
                     /db_xref="GeneID:5261"
                     /db_xref="HGNC:HGNC:8931"
                     /db_xref="MIM:172471"
ORIGIN      
        1 mtldvgpede lpdwaaakef yqkydpkdvi grgvssvvrr cvhratghef avkimevtae
       61 rlspeqleev reatrrethi lrqvaghphi itlidsyess sfmflvfdlm rkgelfdylt
      121 ekvalseket rsimrsllea vsflhanniv hrdlkpenil lddnmqirls dfgfschlep
      181 geklrelcgt pgylapeilk csmdethpgy gkevdlwacg vilftllags ppfwhrrqil
      241 mlrmimegqy qfsspewddr sstvkdlisr llqvdpearl taeqalqhpf fercegsqpw
      301 nltprqrfrv avwtvlaagr valsthrvrp ltknallrdp yalrsvrhli dncafrlygh
      361 wvkkgeqqnr aalfqhrppg pfpimgpeee gdsaaitede avlvlg
//
LOCUS       NP_001101                748 aa            linear   PRI 20-NOV-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 10
            isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001101
VERSION     NP_001101.1
DBSOURCE    REFSEQ: accession NM_001110.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 748)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 748)
  AUTHORS   Dolla,G., Nicolas,S., Dos Santos,L.R., Bourgeois,A.,
            Pardossi-Piquard,R., Bihl,F., Zaghrini,C., Justino,J., Payre,C.,
            Mansuelle,P., Garbers,C., Ronco,P., Checler,F., Lambeau,G. and
            Petit-Paitel,A.
  TITLE     Ectodomain shedding of PLA2R1 is mediated by the metalloproteases
            ADAM10 and ADAM17
  JOURNAL   J Biol Chem 300 (7), 107480 (2024)
   PUBMED   38897568
  REMARK    GeneRIF: Ectodomain shedding of PLA2R1 is mediated by the
            metalloproteases ADAM10 and ADAM17.
REFERENCE   3  (residues 1 to 748)
  AUTHORS   Piwkowska,A., Rachubik,P., Typiak,M., Kulesza,T., Audzeyenka,I.,
            Saleem,M.A., Gruba,N., Wysocka,M., Lesner,A. and Rogacka,D.
  TITLE     ADAM10 as a major activator of reactive oxygen species production
            and klotho shedding in podocytes under diabetic conditions
  JOURNAL   Biochem Pharmacol 225, 116328 (2024)
   PUBMED   38815628
  REMARK    GeneRIF: ADAM10 as a major activator of reactive oxygen species
            production and klotho shedding in podocytes under diabetic
            conditions.
REFERENCE   4  (residues 1 to 748)
  AUTHORS   Babendreyer,A., Kieselhorst,J., Rinkens,C., Lyashenko,A.M.,
            Dusterhoft,S., Jahr,H., Craveiro,R.B., Wolf,M. and Ludwig,A.
  TITLE     Downregulation of the metalloproteinases ADAM10 or ADAM17 promotes
            osteoclast differentiation
  JOURNAL   Cell Commun Signal 22 (1), 322 (2024)
   PUBMED   38863060
  REMARK    GeneRIF: Downregulation of the metalloproteinases ADAM10 or ADAM17
            promotes osteoclast differentiation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 748)
  AUTHORS   Gao,J.H., He,A.D., Liu,L.M., Zhou,Y.J., Guo,Y.W., Lu,M., Zeng,X.B.,
            Gong,X., Lu,Y.J., Liang,H.F., Zhang,B.X., Ma,R., Zhang,R.Y. and
            Ming,Z.Y.
  TITLE     Direct interaction of platelet with tumor cell aggravates
            hepatocellular carcinoma metastasis by activating
            TLR4/ADAM10/CX3CL1 axis
  JOURNAL   Cancer Lett 585, 216674 (2024)
   PUBMED   38280480
  REMARK    GeneRIF: Direct interaction of platelet with tumor cell aggravates
            hepatocellular carcinoma metastasis by activating
            TLR4/ADAM10/CX3CL1 axis.
REFERENCE   6  (residues 1 to 748)
  AUTHORS   Lammich,S., Buell,D., Zilow,S., Ludwig,A.K., Nuscher,B.,
            Lichtenthaler,S.F., Prinzen,C., Fahrenholz,F. and Haass,C.
  TITLE     Expression of the anti-amyloidogenic secretase ADAM10 is suppressed
            by its 5'-untranslated region
  JOURNAL   J Biol Chem 285 (21), 15753-15760 (2010)
   PUBMED   20348102
  REMARK    GeneRIF: the 5'-UTR of ADAM10 may have an important role for
            post-transcriptional regulation of ADAM10 expression and
            consequently Abeta production.
REFERENCE   7  (residues 1 to 748)
  AUTHORS   McKie,N., Edwards,T., Dallas,D.J., Houghton,A., Stringer,B.,
            Graham,R., Russell,G. and Croucher,P.I.
  TITLE     Expression of members of a novel membrane linked metalloproteinase
            family (ADAM) in human articular chondrocytes
  JOURNAL   Biochem Biophys Res Commun 230 (2), 335-339 (1997)
   PUBMED   9016778
REFERENCE   8  (residues 1 to 748)
  AUTHORS   Howard,L., Lu,X., Mitchell,S., Griffiths,S. and Glynn,P.
  TITLE     Molecular cloning of MADM: a catalytically active mammalian
            disintegrin-metalloprotease expressed in various cell types
  JOURNAL   Biochem J 317 (Pt 1) (Pt 1), 45-50 (1996)
   PUBMED   8694785
REFERENCE   9  (residues 1 to 748)
  AUTHORS   Wolfsberg,T.G., Primakoff,P., Myles,D.G. and White,J.M.
  TITLE     ADAM, a novel family of membrane proteins containing A Disintegrin
            And Metalloprotease domain: multipotential functions in cell-cell
            and cell-matrix interactions
  JOURNAL   J Cell Biol 131 (2), 275-278 (1995)
   PUBMED   7593158
  REMARK    Review article
REFERENCE   10 (residues 1 to 748)
  AUTHORS   O'Bryan,J.P., Fridell,Y.W., Koski,R., Varnum,B. and Liu,E.T.
  TITLE     The transforming receptor tyrosine kinase, Axl, is
            post-translationally regulated by proteolytic cleavage
  JOURNAL   J Biol Chem 270 (2), 551-557 (1995)
   PUBMED   7822279
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA941750.1, AF009615.1,
            BX372217.2, AY726599.1, BE327886.1, AA243020.1 and AC018904.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Members of the ADAM family are cell surface proteins with
            a unique structure possessing both potential adhesion and protease
            domains. This gene encodes and ADAM family member that cleaves many
            proteins including TNF-alpha and E-cadherin. Alternate splicing
            results in multiple transcript variants encoding different proteins
            that may undergo similar processing. [provided by RefSeq, Feb
            2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF009615.1, SRR14038192.331913.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260408.8/ ENSP00000260408.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..748
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..748
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 10 isoform 1 preproprotein"
                     /EC_number="3.4.24.81"
                     /note="a disintegrin and metalloprotease domain 10;
                     disintegrin and metalloproteinase domain-containing
                     protein 10; kuzbanian protein homolog; mammalian
                     disintegrin-metalloprotease"
                     /calculated_mol_wt=82147
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2014
     Region          46..156
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Region          171..178
                     /region_name="Cysteine switch. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Site            213..214
                     /site_type="cleavage"
                     /note="Cleavage, by furin and PCSK7.
                     /evidence=ECO:0000250|UniProtKB:Q10741; propagated from
                     UniProtKB/Swiss-Prot (O14672.1)"
     mat_peptide     214..748
                     /product="Disintegrin and metalloproteinase
                     domain-containing protein 10. /id=PRO_0000029067"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
                     /calculated_mol_wt=59402
     Region          220..459
                     /region_name="ZnMc_TACE_like"
                     /note="Zinc-dependent metalloprotease; TACE_like
                     subfamily. TACE, the tumor-necrosis factor-alpha
                     converting enzyme, releases soluble TNF-alpha from
                     transmembrane pro-TNF-alpha; cd04270"
                     /db_xref="CDD:239798"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14672.1)"
     Site            278
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:29224781, ECO:0007744|PDB:6BDZ,
                     ECO:0007744|PDB:6BE6; propagated from UniProtKB/Swiss-Prot
                     (O14672.1)"
     Site            order(383..384,387,393)
                     /site_type="active"
                     /db_xref="CDD:239798"
     Site            439
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14672.1)"
     Region          466..545
                     /region_name="DISIN"
                     /note="Homologues of snake disintegrins; smart00050"
                     /db_xref="CDD:214490"
     Site            551
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O14672.1)"
     Site            673..693
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Region          704..748
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Region          708..715
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Region          722..728
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     Region          734..748
                     /region_name="Interaction with AP2A1, AP2A2 and AP2M1.
                     /evidence=ECO:0000250|UniProtKB:O35598"
                     /note="propagated from UniProtKB/Swiss-Prot (O14672.1)"
     CDS             1..748
                     /gene="ADAM10"
                     /gene_synonym="AD10; AD18; CD156c; CDw156; HsT18717; kuz;
                     MADM; RAK"
                     /coded_by="NM_001110.4:174..2420"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10167.1"
                     /db_xref="GeneID:102"
                     /db_xref="HGNC:HGNC:188"
                     /db_xref="MIM:602192"
ORIGIN      
        1 mvllrvlill lswaagmggq ygnplnkyir hyeglsynvd slhqkhqrak ravshedqfl
       61 rldfhahgrh fnlrmkrdts lfsdefkvet snkvldydts hiytghiyge egsfshgsvi
      121 dgrfegfiqt rggtfyvepa eryikdrtlp fhsviyhedd inyphkygpq ggcadhsvfe
      181 rmrkyqmtgv eevtqipqee haangpellr kkrttsaekn tcqlyiqtdh lffkyygtre
      241 aviaqisshv kaidtiyqtt dfsgirnisf mvkririntt adekdptnpf rfpnigvekf
      301 lelnseqnhd dyclayvftd rdfddgvlgl awvgapsgss ggicekskly sdgkkkslnt
      361 giitvqnygs hvppkvshit fahevghnfg sphdsgtect pgesknlgqk engnyimyar
      421 atsgdklnnn kfslcsirni sqvlekkrnn cfvesgqpic gngmveqgee cdcgysdqck
      481 deccfdanqp egrkcklkpg kqcspsqgpc ctaqcafksk sekcrddsdc aregicngft
      541 alcpasdpkp nftdcnrhtq vcingqcags icekygleec tcassdgkdd kelchvccmk
      601 kmdpstcast gsvqwsrhfs grtitlqpgs pcndfrgycd vfmrcrlvda dgplarlkka
      661 ifspelyeni aewivahwwa vllmgialim lmagfikics vhtpssnpkl pppkplpgtl
      721 krrrppqpiq qpqrqrpres yqmghmrr
//
LOCUS       NP_898861                303 aa            linear   PRI 20-NOV-2025
DEFINITION  dysbindin isoform b [Homo sapiens].
ACCESSION   NP_898861
VERSION     NP_898861.1
DBSOURCE    REFSEQ: accession NM_183040.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Geraci,F., Passiatore,R., Penzel,N., Laudani,S., Bertolino,A.,
            Blasi,G., Graziano,A.C.E., Kikidis,G.C., Mazza,C., Parihar,M.,
            Rampino,A., Sportelli,L., Trevisan,N., Drago,F., Papaleo,F.,
            Sambataro,F., Pergola,G. and Leggio,G.M.
  TITLE     Sex dimorphism controls dysbindin-related cognitive dysfunctions in
            mice and humans with the contribution of COMT
  JOURNAL   Mol Psychiatry 29 (9), 2666-2677 (2024)
   PUBMED   38532008
  REMARK    GeneRIF: Sex dimorphism controls dysbindin-related cognitive
            dysfunctions in mice and humans with the contribution of COMT.
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Rodrigues,R., Quental,R., Santos Silva,R., Costa,L. and
            Estrela-Silva,S.
  TITLE     Unraveling Hermansky-Pudlak syndrome type 7: a case report and
            comprehensive literature review on the identification of DTNBP1
            variants
  JOURNAL   Ophthalmic Genet 45 (3), 262-266 (2024)
   PUBMED   38097925
  REMARK    GeneRIF: Unraveling Hermansky-Pudlak syndrome type 7: a case report
            and comprehensive literature review on the identification of DTNBP1
            variants.
            Review article
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Manago,F., Scheggia,D., Pontillo,M., Mereu,M., Mastrogiacomo,R.,
            Udayan,G., Valentini,P., Tata,M.C., Weinberger,D.R., Weickert,C.S.,
            Pompa,P.P., De Luca,M.A., Vicari,S. and Papaleo,F.
  TITLE     Dopaminergic signalling and behavioural alterations by Comt-Dtnbp1
            genetic interaction and their clinical relevance
  JOURNAL   Br J Pharmacol 180 (19), 2514-2531 (2023)
   PUBMED   37218669
  REMARK    GeneRIF: Dopaminergic signalling and behavioural alterations by
            Comt-Dtnbp1 genetic interaction and their clinical relevance.
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Pavesic Radonja,A., Blazevic Zelic,S., Rubesa,G. and Bradshaw,N.J.
  TITLE     SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3, DYSBINDIN-1
            AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A PANSS-BASED
            FOLLOW UP STUDY
  JOURNAL   Psychiatr Danub 35 (2), 180-186 (2023)
   PUBMED   37480305
  REMARK    GeneRIF: SYMPTOM SEVERITY IN SCHIZOPHRENIA PATIENTS WITH NPAS3,
            DYSBINDIN-1 AND/OR TRIOBP PROTEIN PATHOLOGY IN THEIR BLOOD SERUM: A
            PANSS-BASED FOLLOW UP STUDY.
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Straub,R.E., Jiang,Y., MacLean,C.J., Ma,Y., Webb,B.T.,
            Myakishev,M.V., Harris-Kerr,C., Wormley,B., Sadek,H., Kadambi,B.,
            Cesare,A.J., Gibberman,A., Wang,X., O'Neill,F.A., Walsh,D. and
            Kendler,K.S.
  TITLE     Genetic variation in the 6p22.3 gene DTNBP1, the human ortholog of
            the mouse dysbindin gene, is associated with schizophrenia
  JOURNAL   Am J Hum Genet 71 (2), 337-348 (2002)
   PUBMED   12098102
  REMARK    GeneRIF: single-nucleotide polymorphisms within the gene DTNBP1
            (dystrobrevin-binding protein 1, or dysbindin) are strongly
            associated with schizophrenia
            Erratum:[Am J Hum Genet 2002 Oct;72(4):1007]
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Benson,M.A., Newey,S.E., Martin-Rendon,E., Hawkes,R. and Blake,D.J.
  TITLE     Dysbindin, a novel coiled-coil-containing protein that interacts
            with the dystrobrevins in muscle and brain
  JOURNAL   J Biol Chem 276 (26), 24232-24241 (2001)
   PUBMED   11316798
  REMARK    GeneRIF: In mouse, dysbindin binds to alpha- and beta-dystrobrevin
            in muscle and brain.
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Introne,W.J., Huizing,M., Malicdan,M.C.V., O'Brien,K.J. and
            Gahl,W.A.
  TITLE     Hermansky-Pudlak Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301464
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX394617.2, AL136637.2,
            AK310590.1 and AK290718.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein that may play a role in
            organelle biogenesis associated with melanosomes, platelet dense
            granules, and lysosomes. A similar protein in mouse is a component
            of a protein complex termed biogenesis of lysosome-related
            organelles complex 1 (BLOC-1), and binds to alpha- and
            beta-dystrobrevins, which are components of the
            dystrophin-associated protein complex (DPC). Mutations in this gene
            are associated with Hermansky-Pudlak syndrome type 7. This gene may
            also be associated with schizophrenia. Multiple transcript variants
            encoding distinct isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) contains an additional segment
            in the coding region compared to variant 1. The resulting isoform
            (b) contains a shorter and distinct C-terminus compared to isoform
            a. This protein isoform is described by Talbot et al.
            (PMID:21390302).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136637.2, SRR1163655.680781.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.3"
     Protein         1..303
                     /product="dysbindin isoform b"
                     /note="dysbindin-1; biogenesis of lysosomal organelles
                     complex-1, subunit 8; Hermansky-Pudlak syndrome 7 protein;
                     BLOC-1 subunit 8; biogenesis of lysosome-related
                     organelles complex 1 subunit 8"
                     /calculated_mol_wt=34700
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96EV8.1)"
     Region          <60..>213
                     /region_name="COG4913"
                     /note="Uncharacterized conserved protein, contains a
                     C-terminal ATPase domain [Function unknown]"
                     /db_xref="CDD:443941"
     Region          175..>271
                     /region_name="Dysbindin"
                     /note="Dysbindin (Dystrobrevin binding protein 1);
                     pfam04440"
                     /db_xref="CDD:461312"
     Region          243..256
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EV8.1)"
     CDS             1..303
                     /gene="DTNBP1"
                     /gene_synonym="BLOC1S8; DBND; HPS7; My031; SDY"
                     /coded_by="NM_183040.2:190..1101"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4535.1"
                     /db_xref="GeneID:84062"
                     /db_xref="HGNC:HGNC:17328"
                     /db_xref="MIM:607145"
ORIGIN      
        1 mletlrerll svqqdftsgl ktlsdksrea kvkskprtvp flpkysagle llsryedtwa
       61 alhrrakdca sagelvdsev vmlsahwekk ktslvelqeq lqqlpaliad lesmtanlth
      121 leasfeeven nllhledlcg qcelerckhm qsqqlenykk nkrkeletfk aeldaehaqk
      181 vlemehtqqm klkerqkffe eafqqdmeqy lstgylqiae rrepigsmss mevnvdmleq
      241 mdlmdisdqe aldvflnsgg eentvlspal grvdklalae pgqyrchspp kvrrenhlpv
      301 tya
//
LOCUS       NP_001354462             542 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 26 [Homo sapiens].
ACCESSION   NP_001354462 XP_005270258
VERSION     NP_001354462.1
DBSOURCE    REFSEQ: accession NM_001367533.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 542)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 542)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 542)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 542)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 542)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 542)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 542)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 542)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 542)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 542)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270258.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.724858.1,
                                           SRR3476690.738679.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..542
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..542
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 26"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=60612
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          410..537
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..542
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367533.1:95..1723"
                     /note="isoform 26 is encoded by transcript variant 26"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk pqsnnknsle pqttvvhnat dgikgstesc
      361 ntttededlk aaplrtgngs svpegrssrd rtapsagmqp qpslcssamr kqeiikiteq
      421 lieainngdf eaytkicdpg ltsfepealg nlvegmdfhk fyfenllskn skpihttiln
      481 phvhvigeda aciayirltq yidgqgrprt sqseetrvwh rrdgkwlnvh yhcsgapaap
      541 lq
//
LOCUS       NP_001230157             677 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform e [Homo sapiens].
ACCESSION   NP_001230157
VERSION     NP_001230157.1
DBSOURCE    REFSEQ: accession NM_001243228.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299169.1, AK315074.1 and
            AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            5' end of an exon compared to variant 3. The resulting isoform (e)
            is shorter at the N-terminus and contains an alternate internal
            segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK315074.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..677
                     /product="transcription factor 4 isoform e"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=72302
     Region          1..83
                     /region_name="Essential for MYOD1 inhibition.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          18..26
                     /region_name="9aaTAD"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          269..327
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          342..385
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q62655; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          385..406
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P15884.3)"
     Region          568..652
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(576,580,582..584,586,591,612..613)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(589..590,593..594,596..597,600,604,614,617,621,624,
                     627..632)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     Region          629..652
                     /region_name="Class A specific domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     Region          644..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P15884.3)"
     CDS             1..677
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243228.2:536..2569"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58630.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mhhqqrmaal gtdkelsdll dfsamfsppv ssgkngptsl asghftgsnv edrsssgswg
       61 ngghpspsrn ygdgtpydhm tsrdlgshdn lsppfvnsri qsktergsys sygresnlqg
      121 chqqsllggd mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl
      181 psslvlspqv yapsastady nrdspgypss kpatstfpss ffmqdghhss dpwssssgmn
      241 qpgyagmlgn sshipqsssy cslhpherls ypshssadin sslppmstfh rsgtnhysts
      301 sctppangtd simanrgsga agssqtgdal gkalasiysp dhtnnsfssn pstpvgspps
      361 lsagtavwsr nggqassspn yegplhslqs riedrlerld daihvlrnha vgpstampgg
      421 hgdmhgiigp shngamgglg sgygtgllsa nrhslmvgth redgvalrgs hsllpnqvpv
      481 pqlpvqsats pdlnppqdpy rgmppglqgq svssgsseik sddegdenlq dtkssedkkl
      541 dddkkdiksi trsrssnndd edltpeqkae rekerrmann arerlrvrdi neafkelgrm
      601 vqlhlksdkp qtkllilhqa vavilsleqq vrernlnpka aclkrreeek vsseppplsl
      661 agphpgmgda snhmgqm
//
LOCUS       NP_004313                168 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl2-associated agonist of cell death [Homo sapiens].
ACCESSION   NP_004313
VERSION     NP_004313.1
DBSOURCE    REFSEQ: accession NM_004322.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Wang,Y., Dong,Y., Zhang,W., Wang,Y., Jao,Y., Liu,J., Zhang,M. and
            He,H.
  TITLE     AMPK/mTOR/p70S6K axis prevents apoptosis of Porphyromonas
            gingivalis-infected gingival epithelial cells via BadSer136
            phosphorylation
  JOURNAL   Apoptosis 28 (7-8), 1012-1023 (2023)
   PUBMED   37014579
  REMARK    GeneRIF: AMPK/mTOR/p70S6K axis prevents apoptosis of Porphyromonas
            gingivalis-infected gingival epithelial cells via Bad[Ser136]
            phosphorylation.
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 168)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 168)
  AUTHORS   Kumari,A., Gesumaria,L., Liu,Y.J., Hughitt,V.K., Zhang,X.,
            Ceribelli,M., Wilson,K.M., Klumpp-Thomas,C., Chen,L., McKnight,C.,
            Itkin,Z., Thomas,C.J., Mock,B.A., Schrump,D.S. and Chen,H.
  TITLE     mTOR inhibition overcomes RSK3-mediated resistance to BET
            inhibitors in small cell lung cancer
  JOURNAL   JCI Insight 8 (5), e156657 (2023)
   PUBMED   36883564
  REMARK    GeneRIF: mTOR inhibition overcomes RSK3-mediated resistance to BET
            inhibitors in small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 168)
  AUTHORS   Hsu,S.Y., Kaipia,A., Zhu,L. and Hsueh,A.J.
  TITLE     Interference of BAD (Bcl-xL/Bcl-2-associated death
            promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms
            and P11
  JOURNAL   Mol Endocrinol 11 (12), 1858-1867 (1997)
   PUBMED   9369453
REFERENCE   7  (residues 1 to 168)
  AUTHORS   Zha,J., Harada,H., Osipov,K., Jockel,J., Waksman,G. and
            Korsmeyer,S.J.
  TITLE     BH3 domain of BAD is required for heterodimerization with BCL-XL
            and pro-apoptotic activity
  JOURNAL   J Biol Chem 272 (39), 24101-24104 (1997)
   PUBMED   9305851
REFERENCE   8  (residues 1 to 168)
  AUTHORS   Wang,H.G., Rapp,U.R. and Reed,J.C.
  TITLE     Bcl-2 targets the protein kinase Raf-1 to mitochondria
  JOURNAL   Cell 87 (4), 629-638 (1996)
   PUBMED   8929532
REFERENCE   9  (residues 1 to 168)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 168)
  AUTHORS   Yang,E., Zha,J., Jockel,J., Boise,L.H., Thompson,C.B. and
            Korsmeyer,S.J.
  TITLE     Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax
            and promotes cell death
  JOURNAL   Cell 80 (2), 285-291 (1995)
   PUBMED   7834748
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291863.1, BG435829.1,
            BE255791.1, BC001901.2 and AW014069.1.
            
            Summary: The protein encoded by this gene is a member of the BCL-2
            family. BCL-2 family members are known to be regulators of
            programmed cell death. This protein positively regulates cell
            apoptosis by forming heterodimers with BCL-xL (B-cell
            lymphoma-extra large) and BCL-2, and reversing their death
            repressor activity. Proapoptotic activity of this protein is
            regulated through its phosphorylation. Protein kinases AKT and MAP
            kinase, as well as protein phosphatase calcineurin were found to be
            involved in the regulation of this protein. Alternative splicing of
            this gene results in two transcript variants which encode the same
            isoform. [provided by RefSeq, Dec 2019].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.115218.1,
                                           SRR1163658.197488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..168
                     /product="bcl2-associated agonist of cell death"
                     /note="BCL2-binding protein; BCL2-binding component 6;
                     BCL-X/BCL-2 binding protein; bcl2 antagonist of cell
                     death; BCL2-antagonist of cell death protein; bcl2-L-8;
                     bcl-2-like protein 8; bcl-2-binding component 6;
                     bcl-XL/Bcl-2-associated death promoter"
                     /calculated_mol_wt=18261
     Region          1..168
                     /region_name="Bcl-2_BAD"
                     /note="Pro-apoptotic Bcl-2 protein, BAD; pfam10514"
                     /db_xref="CDD:402236"
     Region          1..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92934.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            94
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:21444773; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            96
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:21444773; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35147; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA, PKB, PAK1, RPS6KA1, RPS6KB1
                     and PKC/PRKCQ. /evidence=ECO:0000250|UniProtKB:Q61337;
                     Phosphoserine, by PKB/AKT1.
                     /evidence=ECO:0000269|PubMed:10926925,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92934.3)"
     Region          110..124
                     /region_name="BH3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92934.3)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Region          125..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92934.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     Site            161
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q92934.3)"
     CDS             1..168
                     /gene="BAD"
                     /gene_synonym="BBC2; BCL2L8"
                     /coded_by="NM_004322.3:337..843"
                     /db_xref="CCDS:CCDS8065.1"
                     /db_xref="GeneID:572"
                     /db_xref="HGNC:HGNC:936"
                     /db_xref="MIM:603167"
ORIGIN      
        1 mfqipefeps eqedsssaer glgpspagdg psgsgkhhrq apgllwdash qqeqptsssh
       61 hggagaveir srhssypagt eddegmgeep spfrgrsrsa ppnlwaaqry grelrrmsde
      121 fvdsfkkglp rpksagtatq mrqssswtrv fqswwdrnlg rgssapsq
//
LOCUS       NP_077740                901 aa            linear   PRI 20-NOV-2025
DEFINITION  desmocollin-2 isoform Dsc2a preproprotein [Homo sapiens].
ACCESSION   NP_077740
VERSION     NP_077740.1
DBSOURCE    REFSEQ: accession NM_024422.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 901)
  AUTHORS   Han,J.Y., Che,N., Mo,J., Zhang,D.F., Liang,X.H., Dong,X.Y.,
            Zhao,X.L. and Sun,B.C.
  TITLE     Desmoglein 2 and desmocollin 2 depletions promote malignancy
            through distinct mechanisms in triple-negative and luminal breast
            cancer
  JOURNAL   BMC Cancer 24 (1), 532 (2024)
   PUBMED   38671389
  REMARK    GeneRIF: Desmoglein 2 and desmocollin 2 depletions promote
            malignancy through distinct mechanisms in triple-negative and
            luminal breast cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 901)
  AUTHORS   Sun,C., Wen,K., Zhang,B., Dong,Y., Chen,C., Neo,S.Y., Leng,B.,
            Gao,T.T. and Wu,J.
  TITLE     DSC2 suppresses the growth of gastric cancer through the inhibition
            of nuclear translocation of gamma-catenin and PTEN/PI3K/AKT
            signaling pathway
  JOURNAL   Aging (Albany NY) 15 (13), 6380-6399 (2023)
   PUBMED   37421607
  REMARK    GeneRIF: DSC2 suppresses the growth of gastric cancer through the
            inhibition of nuclear translocation of gamma-catenin and
            PTEN/PI3K/AKT signaling pathway.
REFERENCE   3  (residues 1 to 901)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 901)
  AUTHORS   Pariyar,M., Thorne,R.F., Scott,R.J. and Avery-Kiejda,K.A.
  TITLE     Verification and Validation of a Four-Gene Panel as a Prognostic
            Indicator in Triple Negative Breast Cancer
  JOURNAL   Front Oncol 12, 821334 (2022)
   PUBMED   35387118
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 901)
  AUTHORS   Syrris,P., Ward,D., Evans,A., Asimaki,A., Gandjbakhch,E.,
            Sen-Chowdhry,S. and McKenna,W.J.
  TITLE     Arrhythmogenic right ventricular dysplasia/cardiomyopathy
            associated with mutations in the desmosomal gene desmocollin-2
  JOURNAL   Am J Hum Genet 79 (5), 978-984 (2006)
   PUBMED   17033975
REFERENCE   6  (residues 1 to 901)
  AUTHORS   Nuber,U.A., Schafer,S., Schmidt,A., Koch,P.J. and Franke,W.W.
  TITLE     The widespread human desmocollin Dsc2 and tissue-specific patterns
            of synthesis of various desmocollin subtypes
  JOURNAL   Eur J Cell Biol 66 (1), 69-74 (1995)
   PUBMED   7750520
REFERENCE   7  (residues 1 to 901)
  AUTHORS   McNally,E., MacLeod,H. and Dellefave-Castillo,L.
  TITLE     Arrhythmogenic Right Ventricular Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301310
REFERENCE   8  (residues 1 to 901)
  AUTHORS   Arnemann,J., Spurr,N.K., Wheeler,G.N., Parker,A.E. and Buxton,R.S.
  TITLE     Chromosomal assignment of the human genes coding for the major
            proteins of the desmosome junction, desmoglein DGI (DSG),
            desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and
            plakoglobin DPIII (JUP)
  JOURNAL   Genomics 10 (3), 640-645 (1991)
   PUBMED   1889810
REFERENCE   9  (residues 1 to 901)
  AUTHORS   Parker,A.E., Wheeler,G.N., Arnemann,J., Pidsley,S.C., Ataliotis,P.,
            Thomas,C.L., Rees,D.A., Magee,A.I. and Buxton,R.S.
  TITLE     Desmosomal glycoproteins II and III. Cadherin-like junctional
            molecules generated by alternative splicing
  JOURNAL   J Biol Chem 266 (16), 10438-10445 (1991)
   PUBMED   2037591
REFERENCE   10 (residues 1 to 901)
  AUTHORS   Garrod,D.R. and Fleming,S.
  TITLE     Early expression of desmosomal components during kidney tubule
            morphogenesis in human and murine embryos
  JOURNAL   Development 108 (2), 313-321 (1990)
   PUBMED   2112455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC382631.1, BC063291.1,
            X56807.1, BE350090.1 and AC012417.13.
            
            Summary: This gene encodes a member of the desmocollin protein
            subfamily. Desmocollins, along with desmogleins, are cadherin-like
            transmembrane glycoproteins that are major components of the
            desmosome. Desmosomes are cell-cell junctions that help resist
            shearing forces and are found in high concentrations in cells
            subject to mechanical stress. This gene is found in a cluster with
            other desmocollin family members on chromosome 18. Mutations in
            this gene are associated with arrhythmogenic right ventricular
            dysplasia-11, and reduced protein expression has been described in
            several types of cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (Dsc2a, also known as DGII)
            encodes the longer isoform (Dsc2a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063291.1, SRR14038192.2462055.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280904.11/ ENSP00000280904.6
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..901
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..901
                     /product="desmocollin-2 isoform Dsc2a preproprotein"
                     /note="desmosomal glycoprotein II/III; cadherin family
                     member 2"
                     /calculated_mol_wt=96705
     sig_peptide     1..31
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3275
     Region          31..111
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; smart01055"
                     /db_xref="CDD:214999"
     Region          140..234
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          247..351
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(254..255,312,314,347,349..350)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          360..463
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Site            order(366..367,424,426,464,466..467)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          477..573
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(482..483,534,536,569,571..572)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          852..896
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..901
                     /gene="DSC2"
                     /gene_synonym="ARVD11; CDHF2; DG2; DGII/III; DSC3"
                     /coded_by="NM_024422.6:451..3156"
                     /note="isoform Dsc2a preproprotein is encoded by
                     transcript variant Dsc2a"
                     /db_xref="CCDS:CCDS11892.1"
                     /db_xref="GeneID:1824"
                     /db_xref="HGNC:HGNC:3036"
                     /db_xref="MIM:125645"
ORIGIN      
        1 meaarpsgsw ngalcrllll tlailifasd acknvtlhvp skldaeklvg rvnlkecfta
       61 anlihssdpd fqiledgsvy ttntillsse krsftillsn tenqekkkif vflehqtkvl
      121 kkrhtkekvl rrakrrwapi pcsmlenslg pfplflqqvq sdtaqnytiy ysirgpgvdq
      181 eprnlfyver dtgnlyctrp vdreqyesfe iiafattpdg ytpelplpli ikiedendny
      241 pifteetytf tifencrvgt tvgqvcatdk depdtmhtrl kysiigqvpp sptlfsmhpt
      301 tgvitttssq ldrelidkyq lkikvqdmdg qyfglqttst ciiniddvnd hlptftrtsy
      361 vtsveentvd veilrvtved kdlvntanwr anytilkgne ngnfkivtda ktnegvlcvv
      421 kplnyeekqq milqigvvne apfsreaspr samstatvtv nvedqdegpe cnppiqtvrm
      481 kenaevgtts ngykaydpet rsssgirykk ltdptgwvti dentgsikvf rsldreaeti
      541 kngiynitvl asdqggrtct gtlgiilqdv ndnspfipkk tviickptms saeivavdpd
      601 epihgppfdf slesstsevq rmwrlkaind taarlsyqnd ppfgsyvvpi tvrdrlgmss
      661 vtsldvtlcd citendcthr vdpriggggv qlgkwailai llgiallfci lftlvcgasg
      721 tskqpkvipd dlaqqnlivs nteapgddkv ysangfttqt vgasaqgvcg tvgsgikngg
      781 qetiemvkgg hqtsescrga ghhhtldscr gghtevdncr ytysewhsft qprlgekvyl
      841 cnqdenhkha qdyvltynye grgsvagsvg ccserqeedg lefldnlepk frtlaeacmk
      901 r
//
LOCUS       NP_002711                307 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 catalytic subunit isoform 1
            [Homo sapiens].
ACCESSION   NP_002711
VERSION     NP_002711.1
DBSOURCE    REFSEQ: accession NM_002720.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Wang,K., Peng,B., Xu,R., Lu,T., Chang,X., Shen,Z., Shi,J., Li,M.,
            Wang,C., Zhou,X., Xu,C., Chang,H. and Zhang,L.
  TITLE     Comprehensive analysis of PPP4C's impact on prognosis, immune
            microenvironment, and immunotherapy response in lung adenocarcinoma
            using single-cell sequencing and multi-omics
  JOURNAL   Front Immunol 15, 1416632 (2024)
   PUBMED   39026674
  REMARK    GeneRIF: Comprehensive analysis of PPP4C's impact on prognosis,
            immune microenvironment, and immunotherapy response in lung
            adenocarcinoma using single-cell sequencing and multi-omics.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Xu,W., Hua,Z., Wang,Y., Tang,W., Ou,W., Liu,F., Yang,Y., Ding,W.,
            Wang,Z., Cui,L., Ge,W., Gu,Y., Wang,X., Chen,Y., Liu,C.Y. and Du,P.
  TITLE     AMBRA1 promotes intestinal inflammation by antagonizing PP4R1/PP4c
            mediated IKK dephosphorylation in an autophagy-independent manner
  JOURNAL   Cell Death Differ 31 (5), 618-634 (2024)
   PUBMED   38424148
  REMARK    GeneRIF: AMBRA1 promotes intestinal inflammation by antagonizing
            PP4R1/PP4c mediated IKK dephosphorylation in an
            autophagy-independent manner.
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Loh,J.T., Teo,J.K.H., Kannan,S., Verma,C.S., Andiappan,A.K.,
            Lim,H.H. and Lam,K.P.
  TITLE     DOK3 promotes atopic dermatitis by enabling the phosphatase PP4C to
            inhibit the T cell signaling mediator CARD11
  JOURNAL   Sci Signal 16 (809), eadg5171 (2023)
   PUBMED   37906628
  REMARK    GeneRIF: DOK3 promotes atopic dermatitis by enabling the
            phosphatase PP4C to inhibit the T cell signaling mediator CARD11.
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Rethi-Nagy,Z., Abraham,E., Sinka,R., Juhasz,S. and Lipinszki,Z.
  TITLE     Protein Phosphatase 4 Is Required for Centrobin Function in DNA
            Damage Repair
  JOURNAL   Cells 12 (18), 2219 (2023)
   PUBMED   37759442
  REMARK    GeneRIF: Protein Phosphatase 4 Is Required for Centrobin Function
            in DNA Damage Repair.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Kloeker,S., Bryant,J.C., Strack,S., Colbran,R.J. and Wadzinski,B.E.
  TITLE     Carboxymethylation of nuclear protein serine/threonine phosphatase
            X
  JOURNAL   Biochem J 327 (Pt 2) (Pt 2), 481-486 (1997)
   PUBMED   9359419
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Bastians,H., Krebber,H., Hoheisel,J., Ohl,S., Lichter,P.,
            Ponstingl,H. and Joos,S.
  TITLE     Assignment of the human serine/threonine protein phosphatase 4 gene
            (PPP4C) to chromosome 16p11-p12 by fluorescence in situ
            hybridization
  JOURNAL   Genomics 42 (1), 181-182 (1997)
   PUBMED   9177794
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Brewis,N.D., Street,A.J., Prescott,A.R. and Cohen,P.T.
  TITLE     PPX, a novel protein serine/threonine phosphatase localized to
            centrosomes
  JOURNAL   EMBO J 12 (3), 987-996 (1993)
   PUBMED   8384557
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Brewis,N.D. and Cohen,P.T.
  TITLE     Protein phosphatase X has been highly conserved during mammalian
            evolution
  JOURNAL   Biochim Biophys Acta 1171 (2), 231-233 (1992)
   PUBMED   1336397
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG705710.1, AF097996.1 and AA765831.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.570602.1,
                                           SRR3476690.309638.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279387.12/ ENSP00000279387.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..307
                     /product="serine/threonine-protein phosphatase 4 catalytic
                     subunit isoform 1"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase X, catalytic subunit; protein
                     phosphatase 4 (formerly X), catalytic subunit;
                     serine/threonine-protein phosphatase 4 catalytic subunit;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=34949
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (P60510.1)"
     Region          6..290
                     /region_name="MPP_PP2A_PP4_PP6"
                     /note="PP2A, PP4, and PP6 phosphoprotein phosphatases,
                     metallophosphatase domain; cd07415"
                     /db_xref="CDD:277360"
     Site            order(48,64,67..68,70..71,73,75..76,88,103..107,118..119,
                     122..123,127..128,131..132,140,265,274,284,290)
                     /site_type="other"
                     /note="heterotrimer interface [polypeptide binding]"
                     /db_xref="CDD:277360"
     Site            order(54,56,82,86,114..115,119..120,124,164,186..188,197,
                     210..212,238,240,264..266)
                     /site_type="active"
                     /db_xref="CDD:277360"
     Site            order(54,56,82,114,164,238)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277360"
     Site            307
                     /site_type="methylation"
                     /note="Leucine methyl ester.
                     /evidence=ECO:0000269|PubMed:25130464; propagated from
                     UniProtKB/Swiss-Prot (P60510.1)"
     CDS             1..307
                     /gene="PPP4C"
                     /gene_synonym="PP-X; PP4; PP4C; PPH3; PPP4; PPX"
                     /coded_by="NM_002720.3:165..1088"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10669.1"
                     /db_xref="GeneID:5531"
                     /db_xref="HGNC:HGNC:9319"
                     /db_xref="MIM:602035"
ORIGIN      
        1 maeisdldrq ieqlrrceli kesevkalca kareilvees nvqrvdspvt vcgdihgqfy
       61 dlkelfrvgg dvpetnylfm gdfvdrgfys vetfllllal kvrypdritl irgnhesrqi
      121 tqvygfydec lrkygsvtvw rycteifdyl slsaiidgki fcvhgglsps iqtldqirti
      181 drkqevphdg pmcdllwsdp edttgwgvsp rgagylfgsd vvaqfnaand idmicrahql
      241 vmegykwhfn etvltvwsap nycyrcgnva aileldehlq kdfiifeaap qetrgipskk
      301 pvadyfl
//
LOCUS       NP_001036214            1268 aa            linear   PRI 20-NOV-2025
DEFINITION  cohesin subunit SA-2 isoform a [Homo sapiens].
ACCESSION   NP_001036214
VERSION     NP_001036214.1
DBSOURCE    REFSEQ: accession NM_001042749.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1268)
  AUTHORS   Fischer,A., Hernandez-Rodriguez,B., Mulet-Lazaro,R., Nuetzel,M.,
            Holzl,F., van Herk,S., Kavelaars,F.G., Stanewsky,H., Ackermann,U.,
            Niang,A.H., Diaz,N., Reuschel,E., Strieder,N., Hernandez-Lopez,I.,
            Valk,P.J.M., Vaquerizas,J.M., Rehli,M., Delwel,R. and Gebhard,C.
  TITLE     STAG2 mutations reshape the cohesin-structured spatial chromatin
            architecture to drive gene regulation in acute myeloid leukemia
  JOURNAL   Cell Rep 43 (8), 114498 (2024)
   PUBMED   39084219
  REMARK    GeneRIF: STAG2 mutations reshape the cohesin-structured spatial
            chromatin architecture to drive gene regulation in acute myeloid
            leukemia.
REFERENCE   3  (residues 1 to 1268)
  AUTHORS   Huber,J., Tanasie,N.L., Zernia,S. and Stigler,J.
  TITLE     Single-molecule imaging reveals a direct role of CTCF's zinc
            fingers in SA interaction and cluster-dependent RNA recruitment
  JOURNAL   Nucleic Acids Res 52 (11), 6490-6506 (2024)
   PUBMED   38742641
  REMARK    GeneRIF: Single-molecule imaging reveals a direct role of CTCF's
            zinc fingers in SA interaction and cluster-dependent RNA
            recruitment.
REFERENCE   4  (residues 1 to 1268)
  AUTHORS   Xu,W., Kim,J.S., Yang,T., Ya,A., Sadzewicz,L., Tallon,L.,
            Harris,B.T., Sarkaria,J., Jin,F. and Waldman,T.
  TITLE     STAG2 mutations regulate 3D genome organization, chromatin loops,
            and Polycomb signaling in glioblastoma multiforme
  JOURNAL   J Biol Chem 300 (6), 107341 (2024)
   PUBMED   38705393
  REMARK    GeneRIF: STAG2 mutations regulate 3D genome organization, chromatin
            loops, and Polycomb signaling in glioblastoma multiforme.
REFERENCE   5  (residues 1 to 1268)
  AUTHORS   Ros-Pardo,D., Gomez-Puertas,P. and Marcos-Alcalde,I.
  TITLE     STAG2: Computational Analysis of Missense Variants Involved in
            Disease
  JOURNAL   Int J Mol Sci 25 (2), 1280 (2024)
   PUBMED   38279279
  REMARK    GeneRIF: STAG2: Computational Analysis of Missense Variants
            Involved in Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1268)
  AUTHORS   Gregson,H.C., Schmiesing,J.A., Kim,J.S., Kobayashi,T., Zhou,S. and
            Yokomori,K.
  TITLE     A potential role for human cohesin in mitotic spindle aster
            assembly
  JOURNAL   J Biol Chem 276 (50), 47575-47582 (2001)
   PUBMED   11590136
REFERENCE   7  (residues 1 to 1268)
  AUTHORS   Sumara,I., Vorlaufer,E., Gieffers,C., Peters,B.H. and Peters,J.M.
  TITLE     Characterization of vertebrate cohesin complexes and their
            regulation in prophase
  JOURNAL   J Cell Biol 151 (4), 749-762 (2000)
   PUBMED   11076961
REFERENCE   8  (residues 1 to 1268)
  AUTHORS   Carramolino,L., Lee,B.C., Zaballos,A., Peled,A., Barthelemy,I.,
            Shav-Tal,Y., Prieto,I., Carmi,P., Gothelf,Y., Gonzalez de
            Buitrago,G., Aracil,M., Marquez,G., Barbero,J.L. and Zipori,D.
  TITLE     SA-1, a nuclear protein encoded by one member of a novel gene
            family: molecular cloning and detection in hemopoietic organs
  JOURNAL   Gene 195 (2), 151-159 (1997)
   PUBMED   9305759
  REMARK    Erratum:[Gene 1998 Jan 12;206(2):283]
REFERENCE   9  (residues 1 to 1268)
  AUTHORS   Wu,C., Friedlander,P., Lamoureux,C., Zannis-Hadjopoulos,M. and
            Price,G.B.
  TITLE     cDNA clones contain autonomous replication activity
  JOURNAL   Biochim Biophys Acta 1174 (3), 241-257 (1993)
   PUBMED   7690594
REFERENCE   10 (residues 1 to 1268)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ425643.1, DA534452.1,
            BX640970.1, BC001765.1, AL831939.2 and CF136218.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a subunit of the
            cohesin complex, which regulates the separation of sister
            chromatids during cell division. Targeted inactivation of this gene
            results in chromatid cohesion defects and aneuploidy, suggesting
            that genetic disruption of cohesin is a cause of aneuploidy in
            human cancer. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.152819.1, BX640970.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1268
                     /product="cohesin subunit SA-2 isoform a"
                     /note="SCC3 homolog 2; cohesin subunit SA-2; SA2
                     stromalin; sister chromatid cohesion 3 homolog B; stromal
                     antigen 2"
                     /calculated_mol_wt=145621
     Region          102..>395
                     /region_name="IRR1"
                     /note="Cohesin [Cell division and chromosome
                     partitioning]; COG5537"
                     /db_xref="CDD:227824"
     Region          157..270
                     /region_name="STAG"
                     /note="STAG domain; pfam08514"
                     /db_xref="CDD:462502"
     CDS             1..1268
                     /gene="STAG2"
                     /gene_synonym="bA517O1.1; HPE13; MKMS; NEDXCF; SA-2; SA2;
                     SCC3B"
                     /coded_by="NM_001042749.2:470..4276"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43990.1"
                     /db_xref="GeneID:10735"
                     /db_xref="HGNC:HGNC:11355"
                     /db_xref="MIM:300826"
ORIGIN      
        1 miaapeiptd fnllqeseth fssdtdfedi egknqkqgkg ktckkgkkgp aekgkggngg
       61 gkppsgpnrm nghhqqngve nmmlfevvkm gksamqsvvd dwiesykhdr dialldlinf
      121 fiqcsgckgv vtaemfrhmq nseiirkmte efdedsgdyp ltmagpqwkk fkssfcefig
      181 vlvrqcqysi iydeymmdtv islltglsds qvrafrhtst laamklmtal vnvalnlsin
      241 mdntqrqyea ernkmigkra nerlelllqk rkelqenqde ienmmnaifk gvfvhryrda
      301 iaeiraicie eigiwmkmys daflndsylk yvgwtmhdkq gevrlkclta lqglyynkel
      361 nsklelftsr fkdrivsmtl dkeydvavqa iklltlvlqs seevltaedc envyhlvysa
      421 hrpvavaage flykklfsrr dpeedgmmkr rgrqgpnanl vktlvfffle selhehaayl
      481 vdsmwdcate llkdwecmns llleeplsge ealtdrqesa lieimlctir qaaechppvg
      541 rgtgkrvlta kekktqlddr tkitelfava lpqllakysv daekvtnllq lpqyfdleiy
      601 ttgrlekhld allrqirniv ekhtdtdvle acsktyhalc neeftifnrv disrsqlide
      661 ladkfnrlle dflqegeepd eddayqvlst lkritafhna hdlskwdlfa cnykllktgi
      721 engdmpeqiv ihalqcthyv ilwqlakite ssstkedllr lkkqmrvfcq icqhyltnvn
      781 ttvkeqafti lcdilmifsh qimsggrdml eplvytpdss lqsellsfil dhvfieqddd
      841 nnsadgqqed easkiealhk rrnllaafck livytvvemn taadifkqym kyyndygdii
      901 ketmsktrqi dkiqcaktli lslqqlfnem iqengynfdr ssstfsgike larrfaltfg
      961 ldqlktreai amlhkdgief afkepnpqge shpplnlafl dilsefsskl lrqdkrtvyv
     1021 ylekfmtfqm slrredvwlp lmsyrnslla ggdddtmsvi sgissrgstv rskkskpstg
     1081 krkvvegmql slteessssd smwlsreqtl htpvmmqtpq ltstimrepk rlrpedsfms
     1141 vypmqtehhq tpldyntqvt wmlaqrqqee arqqqeraam syvklrtnlq hairrgtslm
     1201 eddeepived vmmssegrie dlnegmdfdt mdidlppskn rrertelkpd ffdpasimde
     1261 svlgvsmf
//
LOCUS       NP_001341828            2815 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform f [Homo sapiens].
ACCESSION   NP_001341828
VERSION     NP_001341828.1
DBSOURCE    REFSEQ: accession NM_001354899.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2815)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2815)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2815)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2815)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2815)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2815)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2815)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2815)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2815)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2815)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372079.1579229.1,
                                           SRR1660809.40420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2815
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2815
                     /product="adenomatous polyposis coli protein isoform f"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=308157
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          4..55
                     /region_name="APC_N_CC"
                     /note="Coiled-coil N-terminus of APC, dimerization domain;
                     pfam16689"
                     /db_xref="CDD:435517"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          127..207
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          312..364
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          365..438
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          425..467
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          437..480
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(471,475,479,514,518,522,558,562,566)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          477..519
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          484..525
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          488..525
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          520..563
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          532..567
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          564..610
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          575..616
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          611..655
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          621..661
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          625..659
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          656..697
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          663..703
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          667..703
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          698..739
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          704..991
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          800..850
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            880
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          895..915
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          930..959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          932..1309
                     /region_name="Responsible for down-regulation through a
                     process mediated by direct ubiquitination"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            959
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          992..1141
                     /region_name="Interaction with catenins.
                     /evidence=ECO:0000269|PubMed:8259519"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1008..1107
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Site            1010
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1014
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1071..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1162..1216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1229..>1246
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1255..1340
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1263..1673
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1283..1348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1364
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1367
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1375..1447
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1410
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1498..1541
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1555..1583
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1609..1632
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1634..1687
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1636..1689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1688..1709
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1701..1808
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1718..1811
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Site            1746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1833
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1836
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          1838..1865
                     /region_name="Highly charged"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1845..1919
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1853..1922
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          1937..1983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            1943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            1945
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2005..2024
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2007..2031
                     /region_name="Interaction with AXIN1.
                     /evidence=ECO:0000269|PubMed:10811618"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2015..2044
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2060
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2065
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2097
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61315; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2119..2607
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2123
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2139..2646
                     /region_name="Basic region.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2195..2540
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Site            2232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2447..2815
                     /region_name="Interaction with DLG1.
                     /evidence=ECO:0000269|PubMed:8638125"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2639..2686
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2642..2815
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     Site            2643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2646..2815
                     /region_name="Interaction with MAPRE1.
                     /evidence=ECO:0000269|PubMed:17293347"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2646
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2651
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2682
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70478; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Site            2696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2701..2815
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Site            2761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P25054.2)"
     Region          2775..2778
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     Region          2813..2815
                     /region_name="PDZ-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P25054.2)"
     CDS             1..2815
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354899.2:60..8507"
                     /note="isoform f is encoded by transcript variant 8"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 maaasydqll kqvealkmen snlrqeledn snhltklete asnmkevlkq lqgsiedeam
       61 assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec spvpmgsfpr
      121 rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid slpltenfsl
      181 qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrssqn khetgshdae rqnegqgvge
      241 inmatsgngq gsttrmdhet asvlssssth saprrltshl gtkvemvysl lsmlgthdkd
      301 dmsrtllams ssqdscismr qsgclplliq llhgndkdsv llgnsrgske ararasaalh
      361 niihsqpddk rgrreirvlh lleqirayce tcwewqeahe pgmdqdknpm papvehqicp
      421 avcvlmklsf deehrhamne lgglqaiael lqvdcemygl tndhysitlr ryagmaltnl
      481 tfgdvankat lcsmkgcmra lvaqlksese dlqqviasvl rnlswradvn skktlrevgs
      541 vkalmecale vkkestlksv lsalwnlsah ctenkadica vdgalaflvg tltyrsqtnt
      601 laiiesgggi lrnvssliat nedhrqilre nnclqtllqh lkshsltivs nacgtlwnls
      661 arnpkdqeal wdmgavsmlk nlihskhkmi amgsaaalrn lmanrpakyk danimspgss
      721 lpslhvrkqk aleaeldaqh lsetfdnidn lspkashrsk qrhkqslygd yvfdtnrhdd
      781 nrsdnfntgn mtvlspylnt tvlpsssssr gsldssrsek drslerergi glgnyhpate
      841 npgtsskrgl qisttaaqia kvmeevsaih tsqedrssgs ttelhcvtde rnalrrssaa
      901 hthsntynft ksensnrtcs mpyakleykr ssndslnsvs ssdgygkrgq mkpsiesyse
      961 ddeskfcsyg qypadlahki hsanhmddnd geldtpinys lkysdeqlns grqspsqner
     1021 warpkhiied eikqseqrqs rnqsttypvy testddkhlk fqphfgqqec vspyrsrgan
     1081 gsetnrvgsn hginqnvsqs lcqeddyedd kptnyserys eeeqheeeer ptnysikyne
     1141 ekrhvdqpid yslkyatdip ssqkqsfsfs ksssgqsskt ehmssssent stpssnakrq
     1201 nqlhpssaqs rsgqpqkaat ckvssinqet iqtycvedtp icfsrcssls slssaedeig
     1261 cnqttqeads antlqiaeik ekigtrsaed pvsevpavsq hprtkssrlq gsslssesar
     1321 hkavefssga kspsksgaqt pksppehyvq etplmfsrct svssldsfes rsiassvqse
     1381 pcsgmvsgii spsdlpdspg qtmppsrskt pppppqtaqt krevpknkap taekresgpk
     1441 qaavnaavqr vqvlpdadtl lhfatestpd gfscssslsa lsldepfiqk dvelrimppv
     1501 qendngnete seqpkesnen qekeaektid sekdllddsd dddieileec iisamptkss
     1561 rkakkpaqta sklpppvark psqlpvykll psqnrlqpqk hvsftpgddm prvycvegtp
     1621 infstatsls dltiesppne laagegvrgg aqsgefekrd tiptegrstd eaqggktssv
     1681 tipelddnka eegdilaeci nsampkgksh kpfrvkkimd qvqqasasss apnknqldgk
     1741 kkkptspvkp ipqnteyrtr vrknadsknn lnaervfsdn kdskkqnlkn nskvfndklp
     1801 nnedrvrgsf afdsphhytp iegtpycfsr ndslssldfd dddvdlsrek aelrkakenk
     1861 eseakvtsht eltsnqqsan ktqaiakqpi nrgqpkpilq kqstfpqssk dipdrgaatd
     1921 eklqnfaien tpvcfshnss lsslsdidqe nnnkenepik eteppdsqge pskpqasgya
     1981 pksfhvedtp vcfsrnssls slsidseddl lqecissamp kkkkpsrlkg dnekhsprnm
     2041 ggilgedltl dlkdiqrpds ehglspdsen fdwkaiqega nsivsslhqa aaaaclsrqa
     2101 ssdsdsilsl ksgislgspf hltpdqeekp ftsnkgpril kpgekstlet kkieseskgi
     2161 kggkkvyksl itgkvrsnse isgqmkqplq anmpsisrgr tmihipgvrn sssstspvsk
     2221 kgpplktpas kspsegqtat tsprgakpsv kselspvarq tsqiggsska psrsgsrdst
     2281 psrpaqqpls rpiqspgrns ispgrngisp pnklsqlprt sspstastks sgsgkmsyts
     2341 pgrqmsqqnl tkqtglskna ssiprsesas kglnqmnngn gankkvelsr msstkssgse
     2401 sdrserpvlv rqstfikeap sptlrrklee sasfeslsps srpasptrsq aqtpvlspsl
     2461 pdmslsthss vqaggwrklp pnlsptieyn dgrpakrhdi arshsespsr lpinrsgtwk
     2521 rehskhsssl prvstwrrtg ssssilsass essekaksed ekhvnsisgt kqskenqvsa
     2581 kgtwrkiken efsptnstsq tvssgatnga esktliyqma pavsktedvw vriedcpinn
     2641 prsgrsptgn tppvidsvse kanpnikdsk dnqakqnvgn gsvpmrtvgl enrlnsfiqv
     2701 dapdqkgtei kpgqnnpvpv setnessive rtpfssssss khsspsgtva arvtpfnynp
     2761 sprkssadst sarpsqiptp vnnntkkrds ktdstessgt qspkrhsgsy lvtsv
//
LOCUS       NP_001336298             193 aa            linear   PRI 20-NOV-2025
DEFINITION  centromere protein K isoform 5 [Homo sapiens].
ACCESSION   NP_001336298 XP_016865188
VERSION     NP_001336298.1
DBSOURCE    REFSEQ: accession NM_001349369.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 193)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 193)
  AUTHORS   Li,G., Shen,J., Cheng,W., Wang,X., Wang,D., Song,Y., Chen,Y.,
            Li,X., Zhang,M., Ding,Y., Ma,X., Qian,Q., Zhang,G., Ji,J. and
            Liu,B.
  TITLE     CENPK orchestrates ovarian cancer progression via GOLPH3-Mediated
            activation of mTOR signaling
  JOURNAL   Mol Cell Endocrinol 589, 112253 (2024)
   PUBMED   38670220
  REMARK    GeneRIF: CENPK orchestrates ovarian cancer progression via
            GOLPH3-Mediated activation of mTOR signaling.
REFERENCE   3  (residues 1 to 193)
  AUTHORS   Li,X., Han,Y.R., Xuefeng,X., Ma,Y.X., Xing,G.S., Yang,Z.W.,
            Zhang,Z., Shi,L. and Wu,X.L.
  TITLE     Lentivirus-mediated short hairpin RNA interference of CENPK
            inhibits growth of colorectal cancer cells with overexpression of
            Cullin 4A
  JOURNAL   World J Gastroenterol 28 (37), 5420-5443 (2022)
   PUBMED   36312839
  REMARK    GeneRIF: Lentivirus-mediated short hairpin RNA interference of
            CENPK inhibits growth of colorectal cancer cells with
            overexpression of Cullin 4A.
REFERENCE   4  (residues 1 to 193)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 193)
  AUTHORS   Tian,H., Wang,F., Deng,Y., Ying,L., Fang,W., Chen,D., Miao,C.,
            Li,H., Sun,S., Ma,Y., Cai,H. and Guo,T.
  TITLE     Centromeric protein K (CENPK) promotes gastric cancer proliferation
            and migration via interacting with XRCC5
  JOURNAL   Gastric Cancer 25 (5), 879-895 (2022)
   PUBMED   35715658
  REMARK    GeneRIF: Centromeric protein K (CENPK) promotes gastric cancer
            proliferation and migration via interacting with XRCC5.
REFERENCE   6  (residues 1 to 193)
  AUTHORS   Okada,M., Cheeseman,I.M., Hori,T., Okawa,K., McLeod,I.X.,
            Yates,J.R. 3rd, Desai,A. and Fukagawa,T.
  TITLE     The CENP-H-I complex is required for the efficient incorporation of
            newly synthesized CENP-A into centromeres
  JOURNAL   Nat Cell Biol 8 (5), 446-457 (2006)
   PUBMED   16622420
REFERENCE   7  (residues 1 to 193)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   8  (residues 1 to 193)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   9  (residues 1 to 193)
  AUTHORS   Yamashita,A., Ito,M., Takamatsu,N. and Shiba,T.
  TITLE     Characterization of Solt, a novel SoxLZ/Sox6 binding protein
            expressed in adult mouse testis
  JOURNAL   FEBS Lett 481 (2), 147-151 (2000)
   PUBMED   10996314
REFERENCE   10 (residues 1 to 193)
  AUTHORS   Taki,T., Hayashi,Y., Taniwaki,M., Seto,M., Ueda,R., Hanada,R.,
            Suzukawa,K., Yokota,J. and Morishita,K.
  TITLE     Fusion of the MLL gene with two different genes, AF-6 and
            AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8
            and 11 in infant leukemia
  JOURNAL   Oncogene 13 (10), 2121-2130 (1996)
   PUBMED   8950979
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG502832.1, BG505115.1, BC005400.1 and AC016620.7.
            
            On Mar 15, 2017 this sequence version replaced XP_016865188.1.
            
            Summary: CENPK is a subunit of a CENPH (MIM 605607)-CENPI (MIM
            300065)-associated centromeric complex that targets CENPA (MIM
            117139) to centromeres and is required for proper kinetochore
            function and mitotic progression (Okada et al., 2006 [PubMed
            16622420]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, initiates translation at a
            downstream start codon, and contains an alternate terminal exon,
            resulting in a novel 3' coding region, compared to variant 1. The
            encoded isoform (5) has a shorter N-terminus and a distinct
            C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.583260.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..193
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..193
                     /product="centromere protein K isoform 5"
                     /note="leucine zipper protein FKSG14; SoxLZ/Sox6-binding
                     protein Solt; protein AF-5alpha; interphase centromere
                     complex protein 37"
                     /calculated_mol_wt=22464
     Region          1..189
                     /region_name="CENP-K"
                     /note="Centromere-associated protein K; pfam11802"
                     /db_xref="CDD:463355"
     CDS             1..193
                     /gene="CENPK"
                     /gene_synonym="AF5alpha; CENP-K; FKSG14; P33; Solt"
                     /coded_by="NM_001349369.2:255..836"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:64105"
                     /db_xref="HGNC:HGNC:29479"
                     /db_xref="MIM:611502"
ORIGIN      
        1 mwkdmeecqn klsligtetl tdsnaqlsll imqvkcltae lsqwqkktpe tipltedvli
       61 tlgkeefqkl rqdlemvlst keskneklke dlereqrwld eqqqimesln vlhselknkv
      121 etfsesrifn elktkmlnik eykekllstl gefledhfpl pdrsvkkkkk niqessvnli
      181 tlhemlevls alg
//
LOCUS       NP_001295018             527 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 3 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001295018 XP_011520677
VERSION     NP_001295018.1
DBSOURCE    REFSEQ: accession NM_001308089.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 527)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 527)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 527)
  AUTHORS   Shamseldin,H.E., Yakulov,T.A., Hashem,A., Walz,G. and Alkuraya,F.S.
  TITLE     ANKS3 is mutated in a family with autosomal recessive laterality
            defect
  JOURNAL   Hum Genet 135 (11), 1233-1239 (2016)
   PUBMED   27417436
  REMARK    GeneRIF: Consistent with the proposed role of the ANKS3 variant in
            the pathogenesis of the reported family's phenotype, we show that
            the mutant RNA failed to rescue the laterality defect in anks3
            morphants compared to wild-type RNA. Furthermore, we describe a new
            mutant anks3 line that also displays laterality defect in the
            homozygous state
REFERENCE   4  (residues 1 to 527)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 527)
  AUTHORS   Ramachandran,H., Engel,C., Muller,B., Dengjel,J., Walz,G. and
            Yakulov,T.A.
  TITLE     Anks3 alters the sub-cellular localization of the Nek7 kinase
  JOURNAL   Biochem Biophys Res Commun 464 (3), 901-907 (2015)
   PUBMED   26188091
REFERENCE   6  (residues 1 to 527)
  AUTHORS   Leettola,C.N., Knight,M.J., Cascio,D., Hoffman,S. and Bowie,J.U.
  TITLE     Characterization of the SAM domain of the PKD-related protein ANKS6
            and its interaction with ANKS3
  JOURNAL   BMC Struct Biol 14, 17 (2014)
   PUBMED   24998259
  REMARK    GeneRIF: Study finds that ANKS3-SAM polymerizes and ANKS6-SAM can
            bind to one end of the polymer; study presents crystal structures
            of both the ANKS3-SAM polymer and the ANKS3-SAM/ANKS6-SAM complex,
            revealing the molecular details of their association.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 527)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 527)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020663.1, BC050387.1, AC023830.9, AB075857.1 and BC032314.1.
            
            On Apr 22, 2015 this sequence version replaced XP_011520677.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050387.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..527
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..527
                     /product="ankyrin repeat and SAM domain-containing protein
                     3 isoform 3"
                     /note="ankyrin repeat and SAM domain-containing protein 3"
                     /calculated_mol_wt=57897
     Region          <2..>91
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          6..36
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(7,11..12,15..17,19..20,24,27,36,39,41,45..46,49..51,
                     53..54,58,61,70,72,74,78..79,82..84,86..87,90,93)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          39..70
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          295..358
                     /region_name="SAM_ANKS3"
                     /note="SAM domain of ANKS3 subfamily; cd09519"
                     /db_xref="CDD:188918"
     CDS             1..527
                     /gene="ANKS3"
                     /coded_by="NM_001308089.2:375..1958"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS76813.1"
                     /db_xref="GeneID:124401"
                     /db_xref="HGNC:HGNC:29422"
                     /db_xref="MIM:617310"
ORIGIN      
        1 mkdiqgwtal fhctsaghqh mvrflldsga nanvrepicg ftplmeaaaa gheiivqyfl
       61 nhgvkvdard hsgatarmla kqyghmkiva lmdtyspslp kslyrspeky edlsssdesc
      121 papqrqrpcr kkgvsihegp ralaritgig lggraprpry eqapprgyvt fnssgenple
      181 eeglccrdvt spinerdves ssssssreeh afcanlgpvq ssssseglar aqglsseasv
      241 esnedsdhac kssarkqaks ymktknpdsq wppraatdre gflaesspqt qrapysgpqd
      301 laalleqigc lkylqvfeeq dvdlrifltl tesdlkeigi tlfgpkrkmt saiarwhssa
      361 rppgdalela yadrleaemq elaiqlhkrc eeveatrgqv cqeqelravv esclleqdra
      421 redlqarlre twalardaal vldqlracqa elssrvrqdq ppgaatlgla vppadskgwq
      481 aslqamslpe lsgaledrvr emgqalclvt qsleklqvln gkkwret
//
LOCUS       NP_001291711             194 aa            linear   PRI 20-NOV-2025
DEFINITION  cytotoxic and regulatory T-cell molecule isoform 2 [Homo sapiens].
ACCESSION   NP_001291711
VERSION     NP_001291711.1
DBSOURCE    REFSEQ: accession NM_001304782.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Zheng,S., Yang,B., Li,L., Chen,M., Zhang,L., Chi,W., Shao,Z.M.,
            Xiu,B., Chi,Y. and Wu,J.
  TITLE     CRTAM promotes antitumor immune response in triple negative breast
            cancer by enhancing CD8+ T cell infiltration
  JOURNAL   Int Immunopharmacol 129, 111625 (2024)
   PUBMED   38354509
  REMARK    GeneRIF: CRTAM promotes antitumor immune response in triple
            negative breast cancer by enhancing CD8+ T cell infiltration.
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Barragan-Galvez,J.C., Gonzalez-Orozco,M., Hernandez-Flores,A.,
            Maravillas-Montero,J.L., Chavez-Guerrero,Y. and Ortiz-Navarrete,V.
  TITLE     Prokaryotic Expression of the Immunoglobulin's Domains of CRTAM to
            Characterize a Monoclonal Antibody
  JOURNAL   Protein J 39 (3), 224-231 (2020)
   PUBMED   32300914
  REMARK    GeneRIF: Prokaryotic Expression of the Immunoglobulin's Domains of
            CRTAM to Characterize a Monoclonal Antibody.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Ramirez-Ramirez,D., Padilla-Castaneda,S., Galan-Enriquez,C.S.,
            Vadillo,E., Prieto-Chavez,J.L., Jimenez-Hernandez,E.,
            Vilchis-Ordonez,A., Sandoval,A., Balandran,J.C., Perez-Tapia,S.M.,
            Ortiz-Navarrete,V. and Pelayo,R.
  TITLE     CRTAM+ NK cells endowed with suppressor properties arise in
            leukemic bone marrow
  JOURNAL   J Leukoc Biol 105 (5), 999-1013 (2019)
   PUBMED   30791148
  REMARK    GeneRIF: The findings suggest, for the first time, that the tumor
            microenvironment in acute lymphoblastic leukemia directly
            contribute to exhaustion of NK cell functions by the CRTAM/Necl-2
            interaction, and that the potential regulatory role of
            exhausted-like NK cells may favor malignant progression at the
            expense of anti-tumor responses.
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Yeh,J.H., Sidhu,S.S. and Chan,A.C.
  TITLE     Regulation of a late phase of T cell polarity and effector
            functions by Crtam
  JOURNAL   Cell 132 (5), 846-859 (2008)
   PUBMED   18329370
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Patino-Lopez,G., Hevezi,P., Lee,J., Willhite,D., Verge,G.M.,
            Lechner,S.M., Ortiz-Navarrete,V. and Zlotnik,A.
  TITLE     Human class-I restricted T cell associated molecule is highly
            expressed in the cerebellum and is a marker for activated NKT and
            CD8+ T lymphocytes
  JOURNAL   J Neuroimmunol 171 (1-2), 145-155 (2006)
   PUBMED   16300832
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Boles,K.S., Barchet,W., Diacovo,T., Cella,M. and Colonna,M.
  TITLE     The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell
            responses through the cell-surface receptor CRTAM
  JOURNAL   Blood 106 (3), 779-786 (2005)
   PUBMED   15811952
  REMARK    GeneRIF: NK cells and T8 cells recognize Necl-2 through CRTAM,
            expressed only on activated cells. CRTAM-Necl-2 interactions
            promote cytotoxicity of NK cells and IFN-gamma secretion of T8
            cells as well as NK cell-mediated rejection of tumors expressing
            Necl-2
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Galibert,L., Diemer,G.S., Liu,Z., Johnson,R.S., Smith,J.L.,
            Walzer,T., Comeau,M.R., Rauch,C.T., Wolfson,M.F., Sorensen,R.A.,
            Van der Vuurst de Vries,A.R., Branstetter,D.G., Koelling,R.M.,
            Scholler,J., Fanslow,W.C., Baum,P.R., Derry,J.M. and Yan,W.
  TITLE     Nectin-like protein 2 defines a subset of T-cell zone dendritic
            cells and is a ligand for class-I-restricted T-cell-associated
            molecule
  JOURNAL   J Biol Chem 280 (23), 21955-21964 (2005)
   PUBMED   15781451
  REMARK    GeneRIF: Necl2/CRTAM molecular pair could regulate a large panel of
            cell/cell interactions both within and outside of the immune system
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Kennedy,J., Vicari,A.P., Saylor,V., Zurawski,S.M., Copeland,N.G.,
            Gilbert,D.J., Jenkins,N.A. and Zlotnik,A.
  TITLE     A molecular analysis of NKT cells: identification of a class-I
            restricted T cell-associated molecule (CRTAM)
  JOURNAL   J Leukoc Biol 67 (5), 725-734 (2000)
   PUBMED   10811014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC305734.1, AF001622.1, BC070266.1, AB209830.1 and AP004318.2.
            
            Summary: The CRTAM gene is upregulated in CD4 (see MIM
            186940)-positive and CD8 (see CD8A; MIM 186910)-positive T cells
            and encodes a type I transmembrane protein with V and C1-like Ig
            domains (Yeh et al., 2008 [PubMed 18329370]).[supplied by OMIM, Feb
            2009].
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter and therefore differs in the 5' UTR and 5' coding region,
            compared to variant 1. These differences cause translation
            initiation at an alternate start codon, compared to variant 1. The
            encoded isoform (2) has a distinct N-terminus and is shorter than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.907687.1,
                                           SRR1660805.41022.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..194
                     /product="cytotoxic and regulatory T-cell molecule isoform
                     2"
                     /note="class-I MHC-restricted T-cell-associated molecule"
                     /calculated_mol_wt=22125
     CDS             1..194
                     /gene="CRTAM"
                     /gene_synonym="CD355"
                     /coded_by="NM_001304782.2:79..663"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76489.1"
                     /db_xref="GeneID:56253"
                     /db_xref="HGNC:HGNC:24313"
                     /db_xref="MIM:612597"
ORIGIN      
        1 mwvkllsiva efcfspflvt deetasdale rnslssqdpq qptstvsvte dsstseidke
       61 ekeqttqdpd ltteanpqyl glarkksgil lltlvsflif ilfiivqlfi mklrkahviw
      121 kkenevseht lesyrsrsnn eetsseekng qsshpmrcmn yitklyseak tkrkenvqhs
      181 kleekhiqvp esiv
//
LOCUS       NP_003227                160 aa            linear   PRI 20-NOV-2025
DEFINITION  protransforming growth factor alpha isoform 1 preproprotein [Homo
            sapiens].
ACCESSION   NP_003227
VERSION     NP_003227.1
DBSOURCE    REFSEQ: accession NM_003236.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Ma,X., Zheng,J., He,K., Wang,L., Wang,Z., Wang,K., Liu,Z., San,Z.,
            Zhao,L. and Wang,L.
  TITLE     TGFA expression is associated with poor prognosis and promotes the
            development of cervical cancer
  JOURNAL   J Cell Mol Med 28 (3), e18086 (2024)
   PUBMED   38152044
  REMARK    GeneRIF: TGFA expression is associated with poor prognosis and
            promotes the development of cervical cancer.
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Kamentseva,R.S., Kharchenko,M.V., Gabdrahmanova,G.V., Kotov,M.A.,
            Kosheverova,V.V. and Kornilova,E.S.
  TITLE     EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells
  JOURNAL   Int J Mol Sci 24 (17), 13408 (2023)
   PUBMED   37686213
  REMARK    GeneRIF: EGF, TGF-alpha and Amphiregulin Differently Regulate
            Endometrium-Derived Mesenchymal Stromal/Stem Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Sun,Y., Miao,X., Zhu,L., Liu,J., Lin,Y., Xiang,G., Wu,X., Wang,X.,
            Ni,Z. and Li,S.
  TITLE     Autocrine TGF-alpha is associated with Benzo(a)pyrene-induced mucus
            production and MUC5AC expression during allergic asthma
  JOURNAL   Ecotoxicol Environ Saf 241, 113833 (2022)
   PUBMED   36068759
  REMARK    GeneRIF: Autocrine TGF-alpha is associated with
            Benzo(a)pyrene-induced mucus production and MUC5AC expression
            during allergic asthma.
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Qian,J.F., Lazar-Wesley,E., Breugnot,C. and May,E.
  TITLE     Human transforming growth factor alpha: sequence analysis of the
            4.5-kb and 1.6-kb mRNA species
  JOURNAL   Gene 132 (2), 291-296 (1993)
   PUBMED   8224876
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Thomas,D.M., Nasim,M.M., Gullick,W.J. and Alison,M.R.
  TITLE     Immunoreactivity of transforming growth factor alpha in the normal
            adult gastrointestinal tract
  JOURNAL   Gut 33 (5), 628-631 (1992)
   PUBMED   1612477
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Nasim,M.M., Thomas,D.M., Alison,M.R. and Filipe,M.I.
  TITLE     Transforming growth factor alpha expression in normal gastric
            mucosa, intestinal metaplasia, dysplasia and gastric carcinoma--an
            immunohistochemical study
  JOURNAL   Histopathology 20 (4), 339-343 (1992)
   PUBMED   1577411
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Bean,M.F. and Carr,S.A.
  TITLE     Characterization of disulfide bond position in proteins and
            sequence analysis of cystine-bridged peptides by tandem mass
            spectrometry
  JOURNAL   Anal Biochem 201 (2), 216-226 (1992)
   PUBMED   1632509
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Tricoli,J.V., Nakai,H., Byers,M.G., Rall,L.B., Bell,G.I. and
            Shows,T.B.
  TITLE     The gene for human transforming growth factor alpha is on the short
            arm of chromosome 2
  JOURNAL   Cytogenet Cell Genet 42 (1-2), 94-98 (1986)
   PUBMED   3459638
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Derynck,R., Roberts,A.B., Winkler,M.E., Chen,E.Y. and Goeddel,D.V.
  TITLE     Human transforming growth factor-alpha: precursor structure and
            expression in E. coli
  JOURNAL   Cell 38 (1), 287-297 (1984)
   PUBMED   6088071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA462271.1, X70340.1,
            DA229819.1, DA373586.1, BI760767.1 and CD369689.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a growth factor that is a ligand for the
            epidermal growth factor receptor, which activates a signaling
            pathway for cell proliferation, differentiation and development.
            This protein may act as either a transmembrane-bound ligand or a
            soluble ligand. This gene has been associated with many types of
            cancers, and it may also be involved in some cases of cleft
            lip/palate. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2011].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X70340.1, SRR11853566.15352.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295400.11/ ENSP00000295400.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..160
                     /product="protransforming growth factor alpha isoform 1
                     preproprotein"
                     /note="protransforming growth factor alpha; TGF-alpha"
                     /calculated_mol_wt=14879
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2145
     mat_peptide     24..160
                     /product="Protransforming growth factor alpha.
                     /id=PRO_0000302744"
                     /note="propagated from UniProtKB/Swiss-Prot (P01135.1)"
                     /calculated_mol_wt=14766
     Site            25
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P01135.1)"
     mat_peptide     40..89
                     /product="Transforming growth factor alpha.
                     /id=PRO_0000007753"
                     /note="propagated from UniProtKB/Swiss-Prot (P01135.1)"
                     /calculated_mol_wt=5552
     Region          <44..83
                     /region_name="PHA02887"
                     /note="EGF-like protein; Provisional"
                     /db_xref="CDD:165214"
     Region          <47..121
                     /region_name="PHA03099"
                     /note="epidermal growth factor-like protein (EGF-like
                     protein); Provisional"
                     /db_xref="CDD:165381"
     Site            99..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01135.1)"
     CDS             1..160
                     /gene="TGFA"
                     /gene_synonym="TFGA"
                     /coded_by="NM_003236.4:60..542"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1905.1"
                     /db_xref="GeneID:7039"
                     /db_xref="HGNC:HGNC:11765"
                     /db_xref="MIM:190170"
ORIGIN      
        1 mvpsagqlal falgivlaac qalenstspl sadppvaaav vshfndcpds htqfcfhgtc
       61 rflvqedkpa cvchsgyvga rcehadllav vaasqkkqai talvvvsiva lavliitcvl
      121 ihccqvrkhc ewcralicrh ekpsallkgr tacchsetvv
//
LOCUS       NP_001135773             914 aa            linear   PRI 20-NOV-2025
DEFINITION  meckelin isoform 2 [Homo sapiens].
ACCESSION   NP_001135773
VERSION     NP_001135773.1
DBSOURCE    REFSEQ: accession NM_001142301.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 914)
  AUTHORS   Pang,J., Kong,F., Tang,W., Xi,H., Ma,N., Sheng,X., Peng,Y. and
            Liu,Z.
  TITLE     Two novel TMEM67 variations in a Chinese family with recurrent
            pregnancy loss: a case report
  JOURNAL   BMC Med Genomics 17 (1), 156 (2024)
   PUBMED   38844949
  REMARK    GeneRIF: Two novel TMEM67 variations in a Chinese family with
            recurrent pregnancy loss: a case report.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 914)
  AUTHORS   Yinsheng,Z., Miyoshi,K., Qin,Y., Fujiwara,Y., Yoshimura,T. and
            Katayama,T.
  TITLE     TMEM67 is required for the gating function of the transition zone
            that controls entry of membrane-associated proteins ARL13B and
            INPP5E into primary cilia
  JOURNAL   Biochem Biophys Res Commun 636 (Pt 1), 162-169 (2022)
   PUBMED   36334440
  REMARK    GeneRIF: TMEM67 is required for the gating function of the
            transition zone that controls entry of membrane-associated proteins
            ARL13B and INPP5E into primary cilia.
REFERENCE   3  (residues 1 to 914)
  AUTHORS   Qiu,Y.L., Wang,L., Huang,M., Lian,M., Wang,F., Gong,Y., Ma,X.,
            Hao,C.Z., Zhang,J., Li,Z.D., Xing,Q.H., Cao,M. and Wang,J.S.
  TITLE     Association of novel TMEM67 variants with mild phenotypes of high
            gamma-glutamyl transpeptidase cholestasis and congenital hepatic
            fibrosis
  JOURNAL   J Cell Physiol 237 (6), 2713-2723 (2022)
   PUBMED   35621037
  REMARK    GeneRIF: Association of novel TMEM67 variants with mild phenotypes
            of high gamma-glutamyl transpeptidase cholestasis and congenital
            hepatic fibrosis.
REFERENCE   4  (residues 1 to 914)
  AUTHORS   Baala,L., Romano,S., Khaddour,R., Saunier,S., Smith,U.M.,
            Audollent,S., Ozilou,C., Faivre,L., Laurent,N., Foliguet,B.,
            Munnich,A., Lyonnet,S., Salomon,R., Encha-Razavi,F., Gubler,M.C.,
            Boddaert,N., de Lonlay,P., Johnson,C.A., Vekemans,M., Antignac,C.
            and Attie-Bitach,T.
  TITLE     The Meckel-Gruber syndrome gene, MKS3, is mutated in Joubert
            syndrome
  JOURNAL   Am J Hum Genet 80 (1), 186-194 (2007)
   PUBMED   17160906
  REMARK    GeneRIF: identified MKS3 mutations in four patients with JS, thus
            defining MKS3 as the sixth JS locus (JBTS6)
REFERENCE   5  (residues 1 to 914)
  AUTHORS   Smith,U.M., Consugar,M., Tee,L.J., McKee,B.M., Maina,E.N.,
            Whelan,S., Morgan,N.V., Goranson,E., Gissen,P., Lilliquist,S.,
            Aligianis,I.A., Ward,C.J., Pasha,S., Punyashthiti,R., Malik
            Sharif,S., Batman,P.A., Bennett,C.P., Woods,C.G., McKeown,C.,
            Bucourt,M., Miller,C.A., Cox,P., Algazali,L., Trembath,R.C.,
            Torres,V.E., Attie-Bitach,T., Kelly,D.A., Maher,E.R., Gattone,V.H.
            2nd, Harris,P.C. and Johnson,C.A.
  TITLE     The transmembrane protein meckelin (MKS3) is mutated in
            Meckel-Gruber syndrome and the wpk rat
  JOURNAL   Nat Genet 38 (2), 191-196 (2006)
   PUBMED   16415887
  REMARK    GeneRIF: Positional cloning of the Wpk gene suggested a MKS3
            candidate gene, TMEM67, for which we identified pathogenic
            mutations for five MKS3-linked consanguineous families.
REFERENCE   6  (residues 1 to 914)
  AUTHORS   Morgan,N.V., Gissen,P., Sharif,S.M., Baumber,L., Sutherland,J.,
            Kelly,D.A., Aminu,K., Bennett,C.P., Woods,C.G., Mueller,R.F.,
            Trembath,R.C., Maher,E.R. and Johnson,C.A.
  TITLE     A novel locus for Meckel-Gruber syndrome, MKS3, maps to chromosome
            8q24
  JOURNAL   Hum Genet 111 (4-5), 456-461 (2002)
   PUBMED   12384791
  REMARK    GeneRIF: mapping to chromosome 8 and possible role in Meckel-Gruber
            syndrome
REFERENCE   7  (residues 1 to 914)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   8  (residues 1 to 914)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 914)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
REFERENCE   10 (residues 1 to 914)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC368894.1, AK092244.1,
            AC010834.19, BC032835.2 and BM310097.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene localizes to the primary
            cilium and to the plasma membrane. The gene functions in centriole
            migration to the apical membrane and formation of the primary
            cilium. Multiple transcript variants encoding different isoforms
            have been found for this gene. Defects in this gene are a cause of
            Meckel syndrome type 3 (MKS3) and Joubert syndrome type 6 (JBTS6).
            [provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (2) has an alternate splice
            pattern in the 5' coding region. The resulting isoform (2) has a
            shorter and distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK092244.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..914
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..914
                     /product="meckelin isoform 2"
                     /note="meckel syndrome type 3 protein"
                     /calculated_mol_wt=103460
     Region          86..914
                     /region_name="Meckelin"
                     /note="Meckelin (Transmembrane protein 67); pfam09773"
                     /db_xref="CDD:462892"
     CDS             1..914
                     /gene="TMEM67"
                     /gene_synonym="JBTS6; MECKELIN; MKS3; NPHP11; TNEM67"
                     /coded_by="NM_001142301.1:246..2990"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:91147"
                     /db_xref="HGNC:HGNC:28396"
                     /db_xref="MIM:609884"
ORIGIN      
        1 mslshwpyfr lvlnfrpqvi clpqppkvlg yrlepphltl actlegmyni ieeilerdin
       61 gtllsqatce lcdgnensfm vvnalgdrcv rceptfvnts rscacsepni ltgglcfsst
      121 gnfplrrisa arygevgmsl tsewfakylq ssaaacwvya nltscqalgn mcvmnmnsyd
      181 fatfdacglf qfifentagl stvhsisfwr qnlpwlfygd qlglapqvls stslptnfsf
      241 kgenqntklk fvaasydirg nflkwqtleg gvlqlcpdte trlnaaysfg ttyqqnceip
      301 iskilidfpt pifydvyley tdenqhqyil avpvlnlnlq hnkifvnqds nsgkwlltrr
      361 iflvdavsgr endlgtqprv irvatqisls vhlvpnting niypplitia ysdidikdan
      421 sqsvkvsfsv tyemdhgeah vqtdialgvl gglavlasll ktagwkrrig spmidlqtvv
      481 kflvyyagdl anvffiitvg tglywliffk aqksvsvllp mpiqeerfvt yvgcafalka
      541 lqflhklisq itidvffidw erpkgkvlka vegeggvrsa tvpvsiwrty fvanewneiq
      601 tvrkinslfq vltvlfflev vgfknlalmd sssslsrnpp syiapyscil ryavsaalwl
      661 aigiiqvvff avfyerfied kirqfvdlcs msnisvflls hkcfgyyihg rsvhghadtn
      721 meemnmnlkr eaenlcsqrg lvpntdgqtf eiaisnqmrq hydrihetli rkngparlls
      781 ssastfeqsi kayhmmnkfl gsfidhvhke mdyfikdkll lerilgmefm epmeksifyn
      841 degysfssvl yygneatlli fdllffcvvd lacqnfilas fltylqqeif ryirntvgqk
      901 nlasktlvdq rfli
//
LOCUS       NP_055683                811 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF10 isoform 1 [Homo sapiens].
ACCESSION   NP_055683
VERSION     NP_055683.3
DBSOURCE    REFSEQ: accession NM_014868.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Ford,P.W., Garshott,D.M., Narasimhan,M., Ge,X., Jordahl,E.M.,
            Subramanya,S. and Bennett,E.J.
  TITLE     RNF10 and RIOK3 facilitate 40S ribosomal subunit degradation upon
            60S biogenesis disruption or amino acid starvation
  JOURNAL   Cell Rep 44 (3), 115371 (2025)
   PUBMED   40022732
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Huang,Z., Diehl,F.F., Wang,M., Li,Y., Song,A., Chen,F.X.,
            Rosa-Mercado,N.A., Beckmann,R., Green,R. and Cheng,J.
  TITLE     RIOK3 mediates the degradation of 40S ribosomes
  JOURNAL   Mol Cell 85 (4), 802-814 (2025)
   PUBMED   39947183
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Coria,A.R., Shah,A., Shafieinouri,M., Taylor,S.J., Orgebin,E.,
            Guiblet,W., Miller,J.T., Sharma,I.M. and Wu,C.C.
  TITLE     The integrated stress response regulates 18S nonfunctional rRNA
            decay in mammals
  JOURNAL   Mol Cell 85 (4), 787-801 (2025)
   PUBMED   39947182
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Lehmann,J.A., Lindner,D., Sung,H.M. and Stoecklin,G.
  TITLE     E3 ubiquitin ligase RNF10 promotes dissociation of stalled
            ribosomes and responds to ribosomal subunit imbalance
  JOURNAL   Nat Commun 15 (1), 10350 (2024)
   PUBMED   39609413
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 811)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 811)
  AUTHORS   Hoshikawa,S., Ogata,T., Fujiwara,S., Nakamura,K. and Tanaka,S.
  TITLE     A novel function of RING finger protein 10 in transcriptional
            regulation of the myelin-associated glycoprotein gene and myelin
            formation in Schwann cells
  JOURNAL   PLoS One 3 (10), e3464 (2008)
   PUBMED   18941509
  REMARK    GeneRIF: RNF10 is a trans-acting protein regulating MAG expression
            and is required for myelin formation.
REFERENCE   7  (residues 1 to 811)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 811)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   9  (residues 1 to 811)
  AUTHORS   Lin,J., Friesen,M.T., Bocangel,P., Cheung,D., Rawszer,K. and
            Wigle,J.T.
  TITLE     Characterization of Mesenchyme Homeobox 2 (MEOX2) transcription
            factor binding to RING finger protein 10
  JOURNAL   Mol Cell Biochem 275 (1-2), 75-84 (2005)
   PUBMED   16335786
  REMARK    GeneRIF: MEOX2 and Meox2 binding to RNF10 protein was
            characterized.
REFERENCE   10 (residues 1 to 811)
  AUTHORS   Seki,N., Hattori,A., Sugano,S., Muramatsu,M. and Saito,T.
  TITLE     cDNA cloning, expression profile, and genomic structure of human
            and mouse RNF10/Rnf 10 genes, encoding a novel RING finger protein
  JOURNAL   J Hum Genet 45 (1), 38-42 (2000)
   PUBMED   10697961
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA103961.1, BC016622.1,
            DB526099.1 and BQ015862.1.
            
            On Sep 4, 2003 this sequence version replaced NP_055683.2.
            
            Summary: The protein encoded by this gene contains a ring finger
            motif, which is known to be involved in protein-protein
            interactions. The specific function of this protein has not yet
            been determined. EST data suggests the existence of multiple
            alternatively spliced transcript variants, however, their full
            length nature is not known. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.177399.1,
                                           SRR1660807.18609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000325954.9/ ENSP00000322242.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..811
                     /product="E3 ubiquitin-protein ligase RNF10 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="epididymis secretory sperm binding protein; E3
                     ubiquitin-protein ligase RNF10"
                     /calculated_mol_wt=89796
     Region          1..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Region          101..185
                     /region_name="Interaction with MEOX2.
                     /evidence=ECO:0000269|PubMed:16335786"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Region          223..276
                     /region_name="RING-HC_RNF10"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 10 (RNF10) and similar proteins; cd16536"
                     /db_xref="CDD:438198"
     Region          653..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Region          724..761
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5U6.2)"
     Region          776..811
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5U6.2)"
     CDS             1..811
                     /gene="RNF10"
                     /gene_synonym="RIE2"
                     /coded_by="NM_014868.5:457..2892"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9201.1"
                     /db_xref="GeneID:9921"
                     /db_xref="HGNC:HGNC:10055"
                     /db_xref="MIM:615998"
ORIGIN      
        1 mplsspnaaa tasdmdknsg snsssassgs skgqqpprsa sagpageskp ksdgknssgs
       61 krynrkrels ypknesfnnq srrsssqksk tfnkmppqrg ggssklfsss fnggrrdeva
      121 eaqraefspa qfsgpkkinl nhllnftfep rgqtghfegs ghgswgkrnk wghkpfnkel
      181 flqancqfvv sedqdytahf adpdtlvnwd fveqvricsh evpscpicly pptaakitrc
      241 ghifcwacil hylslsektw skcpicyssv hkkdlksvva teshqyvvgd titmqlmkre
      301 kgvlvalpks kwmnvdhpih lgdeqhsqys klllaskeqv lhrvvleekv aleqqlaeek
      361 htpescfiea aiqelktree alsglagsrr evtgvvaale qlvlmaplak esvfqprkgv
      421 leylsafdee ttevcsldtp srplalplve eeeavsepep eglpeacddl eladdnlkeg
      481 tictessqqe pitksgftrl ssspcyyfyq aedgqhmflh pvnvrclvre ygslerspek
      541 isatvveiag ysmsedvrqr hrylshlplt cefsicelal qppvvsketl emfsddiekr
      601 krqrqkkare errrerriei eenkkqgkyp evhiplenlq qfpafnsytc ssdsalgpts
      661 teghgalsis plsrspgsha dflltplspt asqgspsfcv gsleedspfp sfaqmlrvgk
      721 akadvwpkta pkkdenslvp papvdsdges dnsdrvpvps fqnsfsqaie aafmkldtpa
      781 tsdplseekg gkkrkkqkqk llfstsvvht k
//
LOCUS       NP_000996                243 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein uS3 isoform 1 [Homo sapiens].
ACCESSION   NP_000996
VERSION     NP_000996.2
DBSOURCE    REFSEQ: accession NM_001005.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Jiang,Z., Yang,G., Wang,G., Wan,J., Zhang,Y., Song,W., Zhang,H.,
            Ni,J., Zhang,H., Luo,M., Wang,K. and Peng,B.
  TITLE     SEC14L3 knockdown inhibited clear cell renal cell carcinoma
            proliferation, metastasis and sunitinib resistance through an
            SEC14L3/RPS3/NFkappaB positive feedback loop
  JOURNAL   J Exp Clin Cancer Res 43 (1), 288 (2024)
   PUBMED   39425205
  REMARK    GeneRIF: SEC14L3 knockdown inhibited clear cell renal cell
            carcinoma proliferation, metastasis and sunitinib resistance
            through an SEC14L3/RPS3/NFkappaB positive feedback loop.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Havkin-Solomon,T., Itzhaki,E., Joffe,N., Reuven,N., Shaul,Y. and
            Dikstein,R.
  TITLE     Selective translational control of cellular and viral mRNAs by RPS3
            mRNA binding
  JOURNAL   Nucleic Acids Res 51 (9), 4208-4222 (2023)
   PUBMED   37070189
  REMARK    GeneRIF: Selective translational control of cellular and viral
            mRNAs by RPS3 mRNA binding.
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Ahn,W.S., Kim,H.D., Kim,T.S., Ahn,M.J., Park,Y.J. and Kim,J.
  TITLE     Phosphorylation of rpS3 by Lyn increases translation of Multi-Drug
            Resistance (MDR1) gene
  JOURNAL   BMB Rep 56 (5), 302-307 (2023)
   PUBMED   36724904
  REMARK    GeneRIF: Phosphorylation of rpS3 by Lyn increases translation of
            Multi-Drug Resistance (MDR1) gene.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Kim,J., Chubatsu,L.S., Admon,A., Stahl,J., Fellous,R. and Linn,S.
  TITLE     Implication of mammalian ribosomal protein S3 in the processing of
            DNA damage
  JOURNAL   J Biol Chem 270 (23), 13620-13629 (1995)
   PUBMED   7775413
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Polakiewicz,R.D., Munroe,D.J., Sait,S.N., Tycowski,K.T.,
            Nowak,N.J., Shows,T.B., Housman,D.E. and Page,D.C.
  TITLE     Mapping of ribosomal protein S3 and internally nested snoRNA U15A
            gene to human chromosome 11q13.3-q13.5
  JOURNAL   Genomics 25 (2), 577-580 (1995)
   PUBMED   7789996
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Pogue-Geile,K., Geiser,J.R., Shu,M., Miller,C., Wool,I.G.,
            Meisler,A.I. and Pipas,J.M.
  TITLE     Ribosomal protein genes are overexpressed in colorectal cancer:
            isolation of a cDNA clone encoding the human S3 ribosomal protein
  JOURNAL   Mol Cell Biol 11 (8), 3842-3849 (1991)
   PUBMED   1712897
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Bommer,U.A., Lutsch,G., Stahl,J. and Bielka,H.
  TITLE     Eukaryotic initiation factors eIF-2 and eIF-3: interactions,
            structure and localization in ribosomal initiation complexes
  JOURNAL   Biochimie 73 (7-8), 1007-1019 (1991)
   PUBMED   1742346
  REMARK    Review article
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Zhang,X.T., Tan,Y.M. and Tan,Y.H.
  TITLE     Isolation of a cDNA encoding human 40S ribosomal protein s3
  JOURNAL   Nucleic Acids Res 18 (22), 6689 (1990)
   PUBMED   2129557
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC034149.1, AP000744.4 and CB241053.1.
            
            On Sep 21, 2001 this sequence version replaced NP_000996.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit, where it forms part
            of the domain where translation is initiated. The protein belongs
            to the S3P family of ribosomal proteins. Studies of the mouse and
            rat proteins have demonstrated that the protein has an
            extraribosomal role as an endonuclease involved in the repair of
            UV-induced DNA damage. The protein appears to be located in both
            the cytoplasm and nucleus but not in the nucleolus. Higher levels
            of expression of this gene in colon adenocarcinomas and adenomatous
            polyps compared to adjacent normal colonic mucosa have been
            observed. This gene is co-transcribed with the small nucleolar RNA
            genes U15A and U15B, which are located in its first and fifth
            introns, respectively. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. Multiple alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (1) and variant 2 both encode the
            same protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034149.1, SRR1660803.48040.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000531188.6/ ENSP00000434643.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..243
                     /product="small ribosomal subunit protein uS3 isoform 1"
                     /EC_number="4.2.99.18"
                     /note="IMR-90 ribosomal protein S3; 40S ribosomal protein
                     S3; small ribosomal subunit protein uS3"
                     /calculated_mol_wt=26557
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Region          4..216
                     /region_name="PTZ00084"
                     /note="40S ribosomal protein S3; Provisional"
                     /db_xref="CDD:240260"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCD.
                     /evidence=ECO:0000269|PubMed:19059439; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK.
                     /evidence=ECO:0000269|PubMed:15950189; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            64
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            65
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            67
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1.
                     /evidence=ECO:0000269|PubMed:19460357; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKB.
                     /evidence=ECO:0000269|PubMed:20605787; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:21399639; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Region          214..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P23396.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1 and PKC/PRKCD.
                     /evidence=ECO:0000269|PubMed:19059439,
                     ECO:0000269|PubMed:21871177, ECO:0000269|Ref.12,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P23396.2)"
     CDS             1..243
                     /gene="RPS3"
                     /gene_synonym="S3; uS3"
                     /coded_by="NM_001005.5:31..762"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8236.1"
                     /db_xref="GeneID:6188"
                     /db_xref="HGNC:HGNC:10420"
                     /db_xref="MIM:600454"
ORIGIN      
        1 mavqiskkrk fvadgifkae lnefltrela edgysgvevr vtptrteiii latrtqnvlg
       61 ekgrrirelt avvqkrfgfp egsvelyaek vatrglcaia qaeslrykll gglavrracy
      121 gvlrfimesg akgcevvvsg klrgqraksm kfvdglmihs gdpvnyyvdt avrhvllrqg
      181 vlgikvkiml pwdptgkigp kkplpdhvsi vepkdeilpt tpiseqkggk peppampqpv
      241 pta
//
LOCUS       NP_001273886             341 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001273886
VERSION     NP_001273886.1
DBSOURCE    REFSEQ: accession NM_001286957.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Jreijiri,F., Cavarocchi,E., Amiri-Yekta,A., Cazin,C.,
            Hosseini,S.H., El Khouri,E., Patrat,C., Thierry-Mieg,N., Ray,P.F.,
            Dulioust,E., Whitfield,M. and Toure,A.
  TITLE     CCDC65, encoding a component of the axonemal Nexin-Dynein
            regulatory complex, is required for sperm flagellum structure in
            humans
  JOURNAL   Clin Genet 105 (3), 317-322 (2024)
   PUBMED   37975235
  REMARK    GeneRIF: CCDC65, encoding a component of the axonemal Nexin-Dynein
            regulatory complex, is required for sperm flagellum structure in
            humans.
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Deng,T., Shen,P., Li,A., Zhang,Z., Yang,H., Deng,X., Peng,X.,
            Hu,Z., Tang,Z., Liu,J., Hou,R., Liu,Z. and Fang,W.
  TITLE     CCDC65 as a new potential tumor suppressor induced by metformin
            inhibits activation of AKT1 via ubiquitination of ENO1 in gastric
            cancer
  JOURNAL   Theranostics 11 (16), 8112-8128 (2021)
   PUBMED   34335983
  REMARK    GeneRIF: CCDC65 as a new potential tumor suppressor induced by
            metformin inhibits activation of AKT1 via ubiquitination of ENO1 in
            gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Sigg,M.A., Menchen,T., Lee,C., Johnson,J., Jungnickel,M.K.,
            Choksi,S.P., Garcia,G. 3rd, Busengdal,H., Dougherty,G.W.,
            Pennekamp,P., Werner,C., Rentzsch,F., Florman,H.M., Krogan,N.,
            Wallingford,J.B., Omran,H. and Reiter,J.F.
  TITLE     Evolutionary Proteomics Uncovers Ancient Associations of Cilia with
            Signaling Pathways
  JOURNAL   Dev Cell 43 (6), 744-762 (2017)
   PUBMED   29257953
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Austin-Tse,C., Halbritter,J., Zariwala,M.A., Gilberti,R.M.,
            Gee,H.Y., Hellman,N., Pathak,N., Liu,Y., Panizzi,J.R.,
            Patel-King,R.S., Tritschler,D., Bower,R., O'Toole,E., Porath,J.D.,
            Hurd,T.W., Chaki,M., Diaz,K.A., Kohl,S., Lovric,S., Hwang,D.Y.,
            Braun,D.A., Schueler,M., Airik,R., Otto,E.A., Leigh,M.W.,
            Noone,P.G., Carson,J.L., Davis,S.D., Pittman,J.E., Ferkol,T.W.,
            Atkinson,J.J., Olivier,K.N., Sagel,S.D., Dell,S.D., Rosenfeld,M.,
            Milla,C.E., Loges,N.T., Omran,H., Porter,M.E., King,S.M.,
            Knowles,M.R., Drummond,I.A. and Hildebrandt,F.
  TITLE     Zebrafish Ciliopathy Screen Plus Human Mutational Analysis
            Identifies C21orf59 and CCDC65 Defects as Causing Primary Ciliary
            Dyskinesia
  JOURNAL   Am J Hum Genet 93 (4), 672-686 (2013)
   PUBMED   24094744
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Horani,A., Brody,S.L., Ferkol,T.W., Shoseyov,D., Wasserman,M.G.,
            Ta-shma,A., Wilson,K.S., Bayly,P.V., Amirav,I.,
            Cohen-Cymberknoh,M., Dutcher,S.K., Elpeleg,O. and Kerem,E.
  TITLE     CCDC65 mutation causes primary ciliary dyskinesia with normal
            ultrastructure and hyperkinetic cilia
  JOURNAL   PLoS One 8 (8), e72299 (2013)
   PUBMED   23991085
  REMARK    GeneRIF: Mutation in CCDC65, a nexin-dynein regulatory complex
            member, resulted in a frameshift mutation and PCD
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Lin,J., Tritschler,D., Song,K., Barber,C.F., Cobb,J.S., Porter,M.E.
            and Nicastro,D.
  TITLE     Building blocks of the nexin-dynein regulatory complex in
            Chlamydomonas flagella
  JOURNAL   J Biol Chem 286 (33), 29175-29191 (2011)
   PUBMED   21700706
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Zheng,Y., Zhang,J., Wang,L., Zhou,Z., Xu,M., Li,J. and Sha,J.H.
  TITLE     Cloning and characterization of a novel sperm tail protein,
            NYD-SP28
  JOURNAL   Int J Mol Med 18 (6), 1119-1125 (2006)
   PUBMED   17089017
  REMARK    GeneRIF: NYD-SP28, a sperm tail protein, was cloned and
            characterized.
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302082.1 and CA314956.1.
            
            Summary: This gene encodes a sperm tail protein that is highly
            expressed in adult testis, spermatocytes and spermatids. The
            protein plays a critical role in the assembly of the nexin-dynein
            regulatory complex. Mutations in this gene result in primary
            ciliary dyskinesia. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (2) uses alternate splice sites in
            the 5' coding region and uses a downstream start codon compared to
            variant 1. It encodes isoform 2 which has a shorter N-terminus
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302082.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..341
                     /product="dynein regulatory complex subunit 2 isoform 2"
                     /note="testis development protein NYD-SP28; coiled-coil
                     domain containing 65"
                     /calculated_mol_wt=40312
     CDS             1..341
                     /gene="DRC2"
                     /gene_synonym="CCDC65; CFAP250; FAP250; NYD-SP28"
                     /coded_by="NM_001286957.2:594..1619"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:85478"
                     /db_xref="HGNC:HGNC:29937"
                     /db_xref="MIM:611088"
ORIGIN      
        1 melealtkef eterktiidq hekeihylqd ifmameqnyi dseyesklef qsmwndlknm
       61 nleekhflrl hlenrvedlw rkfqdvlkny tdatedrkaa fetlqvkdek sskeievqmk
      121 kiqklqdait iskgkimihs resedenryi rndkelvlvq lrklkaqrtq araasqknlv
      181 rltlesnatl kalrkivdkg ekilklaeic rkfeteeekv lpfyssvltp keqegiqknn
      241 leelteeltk vmvdyigmen fwkrynkvkl eqlslqhrra qlldingklr emlkqyldgi
      301 svsdevlsql nplfivnyqs nllqplsiri ahpgdkqhpt t
//
LOCUS       NP_001129246             579 aa            linear   PRI 20-NOV-2025
DEFINITION  synapsin-3 isoform IIIg [Homo sapiens].
ACCESSION   NP_001129246
VERSION     NP_001129246.1
DBSOURCE    REFSEQ: accession NM_001135774.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Baris,R.O., Sahin,N., Bilgic,A.D., Ozdemir,C. and Edgunlu,T.G.
  TITLE     Molecular and in silico analyses of SYN III gene variants in autism
            spectrum disorder
  JOURNAL   Ir J Med Sci 192 (6), 2887-2895 (2023)
   PUBMED   37166614
  REMARK    GeneRIF: Molecular and in silico analyses of SYN III gene variants
            in autism spectrum disorder.
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Bolat,H., Unsel-Bolat,G., Ozgul,S., Pariltay,E., Tahillioglu,A.,
            Rohde,L.A., Akin,H. and Ercan,E.S.
  TITLE     Investigation of possible associations of the BDNF, SNAP-25 and SYN
            III genes with the neurocognitive measures: BDNF and SNAP-25 genes
            might be involved in attention domain, SYN III gene in executive
            function
  JOURNAL   Nord J Psychiatry 76 (8), 610-615 (2022)
   PUBMED   35077325
  REMARK    GeneRIF: Investigation of possible associations of the BDNF,
            SNAP-25 and SYN III genes with the neurocognitive measures: BDNF
            and SNAP-25 genes might be involved in attention domain, SYN III
            gene in executive function.
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Longhena,F., Faustini,G., Varanita,T., Zaltieri,M., Porrini,V.,
            Tessari,I., Poliani,P.L., Missale,C., Borroni,B., Padovani,A.,
            Bubacco,L., Pizzi,M., Spano,P. and Bellucci,A.
  TITLE     Synapsin III is a key component of alpha-synuclein fibrils in Lewy
            bodies of PD brains
  JOURNAL   Brain Pathol 28 (6), 875-888 (2018)
   PUBMED   29330884
  REMARK    GeneRIF: Synapsin III is a crucial alpha-synuclein interactant and
            a key component of Lewy bodies fibrils in the brain of patients
            affected by Parkinson's disease.
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Porton,B., Ferreira,A., DeLisi,L.E. and Kao,H.T.
  TITLE     A rare polymorphism affects a mitogen-activated protein kinase site
            in synapsin III: possible relationship to schizophrenia
  JOURNAL   Biol Psychiatry 55 (2), 118-125 (2004)
   PUBMED   14732590
  REMARK    GeneRIF: A missense polymorphism, S470N, was identified in the
            synapsin III gene and appeared more frequently in individuals with
            schizophrenia. The site affected by the polymorphism, Ser470, was
            determined to be a substrate for mitogen-activated protein kinase.
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Tsai,M.T., Hung,C.C., Tsai,C.Y., Liu,M.Y., Su,Y.C., Chen,Y.H.,
            Hsiao,K.J. and Chen,C.H.
  TITLE     Mutation analysis of synapsin III gene in schizophrenia
  JOURNAL   Am J Med Genet 114 (1), 79-83 (2002)
   PUBMED   11840510
  REMARK    GeneRIF: Evidence is not in favor of a large effect of synapsin III
            gene in the pathogenesis of schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Kao,H.T., Porton,B., Hilfiker,S., Stefani,G., Pieribone,V.A.,
            DeSalle,R. and Greengard,P.
  TITLE     Molecular evolution of the synapsin gene family
  JOURNAL   J Exp Zool 285 (4), 360-377 (1999)
   PUBMED   10578110
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Porton,B., Kao,H.T. and Greengard,P.
  TITLE     Characterization of transcripts from the synapsin III gene locus
  JOURNAL   J Neurochem 73 (6), 2266-2271 (1999)
   PUBMED   10582583
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Kao,H.T., Porton,B., Czernik,A.J., Feng,J., Yiu,G., Haring,M.,
            Benfenati,F. and Greengard,P.
  TITLE     A third member of the synapsin gene family
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4667-4672 (1998)
   PUBMED   9539796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83846.1, Z98256.1, Z82246.2,
            Z80902.2, Z82181.2 and Z71183.2.
            
            Summary: This gene is a member of the synapsin gene family.
            Synapsins encode neuronal phosphoproteins which associate with the
            cytoplasmic surface of synaptic vesicles. Family members are
            characterized by common protein domains, and they are implicated in
            synaptogenesis and the modulation of neurotransmitter release,
            suggesting a potential role in several neuropsychiatric diseases.
            The protein encoded by this gene shares the synapsin family domain
            model, with domains A, C, and E exhibiting the highest degree of
            conservation. The protein contains a unique domain J, located
            between domains C and E. Based on this gene's localization to
            22q12.3, a possible schizophrenia susceptibility locus, and the
            established neurobiological roles of the synapsins, this family
            member may represent a candidate gene for schizophrenia. The TIMP3
            gene is located within an intron of this gene and is transcribed in
            the opposite direction. Alternative splicing of this gene results
            in multiple splice variants that encode different isoforms.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.68476.1,
                                           SRR7410570.685449.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..579
                     /product="synapsin-3 isoform IIIg"
                     /note="synapsin-3; cN28H9.2 (synapsin III)"
                     /calculated_mol_wt=63085
     Region          1..29
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and CaMK1.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          19..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          28..90
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          92..190
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          192..394
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Region          <393..535
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          394..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          399..530
                     /region_name="J, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and MAPK.
                     /evidence=ECO:0000269|PubMed:14732590; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70441; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            483
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          531..579
                     /region_name="E"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     CDS             1..579
                     /gene="SYN3"
                     /coded_by="NM_001135774.2:253..1992"
                     /note="isoform IIIg is encoded by transcript variant IIIg"
                     /db_xref="GeneID:8224"
                     /db_xref="HGNC:HGNC:11496"
                     /db_xref="MIM:602705"
ORIGIN      
        1 mnflrrrlsd ssfmanlpng ymtdlqrpds stsspaspam errhpqplaa sfsspgsslf
       61 sslssamkqa pqatsglmep pgpstpivqr prillvidda htdwskyfhg kkvngeieir
      121 veqaefseln laayvtggcm vdmqvvrngt kvvrsfkpdf ilvrqhaysm algedyrslv
      181 iglqygglpa vnslysvynf cskpwvfsql ikifhslgpe kfplveqtff pnhkpmvtap
      241 hfpvvvklgh ahagmgkikv enqldfqdit svvamaktya tteafidsky diriqkigsn
      301 ykaymrtsis gnwkantgsa mleqvamter yrlwvdscse mfggldicav kavhskdgrd
      361 yiievmdssm pligehveed rqlmadlvvs kmsqlpmpgg tapsplrpwa pqiksakspg
      421 qaqlgpqlgq pqprpppqgg prqaqspqpq rsgspsqqrl spqgqqplsp qsgspqqqrs
      481 pgspqlsras sgsspnqask pgatlasqpr ppvqgrstsq qgeeskkpap phphlnksqs
      541 ltnslstsdt sqrgtpsede akaetirnlr ksfaslfsd
//
LOCUS       NP_005106                893 aa            linear   PRI 20-NOV-2025
DEFINITION  major vault protein isoform 1 [Homo sapiens].
ACCESSION   NP_005106
VERSION     NP_005106.2
DBSOURCE    REFSEQ: accession NM_005115.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Li,C., Gao,M., Zha,N. and Guo,G.
  TITLE     The prognostic value and immunological role of MVP in pan-cancer
            study
  JOURNAL   Aging (Albany NY) 16 (10), 8497-8510 (2024)
   PUBMED   38713157
  REMARK    GeneRIF: The prognostic value and immunological role of MVP in
            pan-cancer study.
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Taube,M., Lisiak,N., Toton,E. and Rubis,B.
  TITLE     Human Vault RNAs: Exploring Their Potential Role in Cellular
            Metabolism
  JOURNAL   Int J Mol Sci 25 (7), 4072 (2024)
   PUBMED   38612882
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Yu,C., Zhu,Q., Ma,C., Luo,C., Nie,L., Cai,H., Wang,Q., Wang,F.,
            Ren,H., Yan,H., Xu,K., Zhou,L., Zhang,C., Lu,G., Lu,Z., Zhu,Y. and
            Liu,S.
  TITLE     Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6
  JOURNAL   Front Immunol 14, 1289795 (2024)
   PUBMED   38264642
  REMARK    GeneRIF: Major vault protein regulates tumor-associated macrophage
            polarization through interaction with signal transducer and
            activator of transcription 6.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Holzmann,K., Ambrosch,I., Elbling,L., Micksche,M. and Berger,W.
  TITLE     A small upstream open reading frame causes inhibition of human
            major vault protein expression from a ubiquitous mRNA splice
            variant
  JOURNAL   FEBS Lett 494 (1-2), 99-104 (2001)
   PUBMED   11297743
  REMARK    GeneRIF: MVP gene expression regulated by alternative splicing due
            to generation of an upstream open reading frame
REFERENCE   6  (residues 1 to 893)
  AUTHORS   Dingemans,A.M., van Ark-Otte,J., van der Valk,P., Apolinario,R.M.,
            Scheper,R.J., Postmus,P.E. and Giaccone,G.
  TITLE     Expression of the human major vault protein LRP in human lung
            cancer samples and normal lung tissues
  JOURNAL   Ann Oncol 7 (6), 625-630 (1996)
   PUBMED   8879378
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Schroeijers,A.B., van
            der Valk,P. and Scheper,R.J.
  TITLE     Major vault protein LRP-related multidrug resistance
  JOURNAL   Eur J Cancer 32A (6), 979-984 (1996)
   PUBMED   8763338
  REMARK    Review article
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Izquierdo,M.A., Scheffer,G.L., Flens,M.J., Giaccone,G.,
            Broxterman,H.J., Meijer,C.J., van der Valk,P. and Scheper,R.J.
  TITLE     Broad distribution of the multidrug resistance-related vault lung
            resistance protein in normal human tissues and tumors
  JOURNAL   Am J Pathol 148 (3), 877-887 (1996)
   PUBMED   8774142
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Slovak,M.L., Ho,J.P., Cole,S.P., Deeley,R.G., Greenberger,L., de
            Vries,E.G., Broxterman,H.J., Scheffer,G.L. and Scheper,R.J.
  TITLE     The LRP gene encoding a major vault protein associated with drug
            resistance maps proximal to MRP on chromosome 16: evidence that
            chromosome breakage plays a key role in MRP or LRP gene
            amplification
  JOURNAL   Cancer Res 55 (19), 4214-4219 (1995)
   PUBMED   7671223
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Scheffer,G.L., Wijngaard,P.L., Flens,M.J., Izquierdo,M.A.,
            Slovak,M.L., Pinedo,H.M., Meijer,C.J., Clevers,H.C. and
            Scheper,R.J.
  TITLE     The drug resistance-related protein LRP is the human major vault
            protein
  JOURNAL   Nat Med 1 (6), 578-582 (1995)
   PUBMED   7585126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA940597.1, BQ932800.1,
            BC015623.2 and BM999583.1.
            
            On Apr 3, 2002 this sequence version replaced NP_005106.1.
            
            Summary: This gene encodes the major component of the vault
            complex. Vaults are multi-subunit ribonucleoprotein structures that
            may be involved in nucleo-cytoplasmic transport. The encoded
            protein may play a role in multiple cellular processes by
            regulating the MAP kinase, JAK/STAT and phosphoinositide
            3-kinase/Akt signaling pathways. The encoded protein also plays a
            role in multidrug resistance, and expression of this gene may be a
            prognostic marker for several types of cancer. Alternatively
            spliced transcript variants have been observed for this gene.
            [provided by RefSeq, May 2012].
            
            Transcript Variant: This variant (2, also known as S-MVP) uses a
            different splice site in the 5' UTR, compared to variant 1.
            Variants 1 and 2 encode the same isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005570.1, SRR1803617.77162.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357402.10/ ENSP00000349977.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..893
                     /product="major vault protein isoform 1"
                     /note="lung resistance-related protein; testicular
                     secretory protein Li 30"
                     /calculated_mol_wt=99196
     Region          2..56
                     /region_name="MVP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          4..850
                     /region_name="PTZ00491"
                     /note="major vault protein; Provisional"
                     /db_xref="CDD:240439"
     Region          57..111
                     /region_name="MVP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          112..164
                     /region_name="MVP 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          165..217
                     /region_name="MVP 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          218..272
                     /region_name="MVP 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          273..323
                     /region_name="MVP 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          324..379
                     /region_name="MVP 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          380..457
                     /region_name="MVP 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14764.4)"
     Region          458..520
                     /region_name="MVP 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     Region          856..893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14764.4)"
     CDS             1..893
                     /gene="MVP"
                     /gene_synonym="LRP; VAULT1"
                     /coded_by="NM_005115.5:85..2766"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10656.1"
                     /db_xref="GeneID:9961"
                     /db_xref="HGNC:HGNC:7531"
                     /db_xref="MIM:605088"
ORIGIN      
        1 mateefiiri ppyhyihvld qnsnvsrvev gpktyirqdn ervlfapmrm vtvpprhyct
       61 vanpvsrdaq glvlfdvtgq vrlrhadlei rlaqdpfply pgevlekdit plqvvlpnta
      121 lhlkalldfe dkdgdkvvag dewlfegpgt yiprkevevv eiiqatiirq nqalrlrark
      181 ecwdrdgker vtgeewlvtt vgaylpavfe evldlvdavi ltektalhlr arrnfrdfrg
      241 vsrrtgeewl vtvqdteahv pdvheevlgv vpittlgphn ycvildpvgp dgknqlgqkr
      301 vvkgeksffl qpgeqleqgi qdvyvlseqq glllralqpl eegedeekvs hqagdhwlir
      361 gpleyvpsak vevveerqai pldenegiyv qdvktgkvra vigstymltq devlwekelp
      421 pgveellnkg qdpladrgek dtakslqpla prnktrvvsy rvphnaavqv ydyrekrarv
      481 vfgpelvslg peeqftvlsl sagrpkrpha rralclllgp dfftdvitie tadharlqlq
      541 laynwhfevn drkdpqetak lfsvpdfvgd ackaiasrvr gavasvtfdd fhknsariir
      601 tavfgfetse akgpdgmalp rprdqavfpq nglvvssvdv qsvepvdqrt rdalqrsvql
      661 aieittnsqe aaakheaqrl eqeargrler qkildqseae karkellele alsmavestg
      721 takaeaesra eaariegegs vlqaklkaqa laieteaelq rvqkvrelel vyaraqlele
      781 vskaqqlaev evkkfkqmte aigpstirdl avagpemqvk llqslglkst litdgstpin
      841 lfntafgllg mgpegqplgr rvasgpspge gispqsaqap qapgdnhvvp vlr
//
LOCUS       NP_002287                615 aa            linear   PRI 20-NOV-2025
DEFINITION  delta(14)-sterol reductase LBR [Homo sapiens].
ACCESSION   NP_002287
VERSION     NP_002287.2
DBSOURCE    REFSEQ: accession NM_002296.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 615)
  AUTHORS   En,A., Takemoto,K., Yamakami,Y., Nakabayashi,K. and Fujii,M.
  TITLE     Upregulated expression of lamin B receptor increases cell
            proliferation and suppresses genomic instability: implications for
            cellular immortalization
  JOURNAL   FEBS J 291 (10), 2155-2171 (2024)
   PUBMED   38462947
  REMARK    GeneRIF: Upregulated expression of lamin B receptor increases cell
            proliferation and suppresses genomic instability: implications for
            cellular immortalization.
REFERENCE   2  (residues 1 to 615)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 615)
  AUTHORS   Patil,S., Deshpande,S. and Sengupta,K.
  TITLE     Nuclear envelope protein lamin B receptor protects the genome from
            chromosomal instability and tumorigenesis
  JOURNAL   Hum Mol Genet 32 (5), 745-763 (2023)
   PUBMED   36124691
  REMARK    GeneRIF: Nuclear envelope protein lamin B receptor protects the
            genome from chromosomal instability and tumorigenesis.
REFERENCE   4  (residues 1 to 615)
  AUTHORS   Wesley,C.C. and Levy,D.L.
  TITLE     Differentiation-dependent changes in lamin B1 dynamics and lamin B
            receptor localization
  JOURNAL   Mol Biol Cell 34 (2), ar10 (2023)
   PUBMED   36598800
  REMARK    GeneRIF: Differentiation-dependent changes in lamin B1 dynamics and
            lamin B receptor localization.
REFERENCE   5  (residues 1 to 615)
  AUTHORS   Tuysuz,B., Kasap,B., Saritas,M., Alkaya,D.U., Bozlak,S., Kiykim,A.,
            Durmaz,A., Yildirim,T., Akpinar,E., Apak,H. and Vural,M.
  TITLE     Natural history and genetic spectrum of the Turkish metaphyseal
            dysplasia cohort, including rare types caused by biallelic COL10A1,
            COL2A1, and LBR variants
  JOURNAL   Bone 167, 116614 (2023)
   PUBMED   36400164
  REMARK    GeneRIF: Natural history and genetic spectrum of the Turkish
            metaphyseal dysplasia cohort, including rare types caused by
            biallelic COL10A1, COL2A1, and LBR variants.
REFERENCE   6  (residues 1 to 615)
  AUTHORS   Ye,Q. and Worman,H.J.
  TITLE     Interaction between an integral protein of the nuclear envelope
            inner membrane and human chromodomain proteins homologous to
            Drosophila HP1
  JOURNAL   J Biol Chem 271 (25), 14653-14656 (1996)
   PUBMED   8663349
REFERENCE   7  (residues 1 to 615)
  AUTHORS   Schuler,E., Lin,F. and Worman,H.J.
  TITLE     Characterization of the human gene encoding LBR, an integral
            protein of the nuclear envelope inner membrane
  JOURNAL   J Biol Chem 269 (15), 11312-11317 (1994)
   PUBMED   8157663
REFERENCE   8  (residues 1 to 615)
  AUTHORS   Ye,Q. and Worman,H.J.
  TITLE     Primary structure analysis and lamin B and DNA binding of human
            LBR, an integral protein of the nuclear envelope inner membrane
  JOURNAL   J Biol Chem 269 (15), 11306-11311 (1994)
   PUBMED   8157662
REFERENCE   9  (residues 1 to 615)
  AUTHORS   Soullam,B. and Worman,H.J.
  TITLE     The amino-terminal domain of the lamin B receptor is a nuclear
            envelope targeting signal
  JOURNAL   J Cell Biol 120 (5), 1093-1100 (1993)
   PUBMED   7679672
REFERENCE   10 (residues 1 to 615)
  AUTHORS   Worman,H.J., Yuan,J., Blobel,G. and Georgatos,S.D.
  TITLE     A lamin B receptor in the nuclear envelope
  JOURNAL   Proc Natl Acad Sci U S A 85 (22), 8531-8534 (1988)
   PUBMED   2847165
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU134026.1, BC020079.1 and
            L25931.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 9, 2003 this sequence version replaced NP_002287.1.
            
            Summary: The protein encoded by this gene belongs to the ERG4/ERG24
            family. It localized in the nuclear envelope inner membrane and
            anchors the lamina and the heterochromatin to the membrane. It may
            mediate interaction between chromatin and lamin B. Mutations of
            this gene has been associated with autosomal recessive
            HEM/Greenberg skeletal dysplasia. Alternative splicing occurs at
            this locus and two transcript variants encoding the same protein
            have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020079.1, L25931.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272163.9/ ENSP00000272163.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..615
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.12"
     Protein         1..615
                     /product="delta(14)-sterol reductase LBR"
                     /EC_number="1.3.1.70"
                     /note="integral nuclear envelope inner membrane protein;
                     tudor domain containing 18; delta-14-SR; sterol
                     C14-reductase; C-14 sterol reductase; 3-beta-hydroxysterol
                     Delta (14)-reductase"
                     /calculated_mol_wt=70572
     Region          1..55
                     /region_name="LBR_tudor"
                     /note="Lamin-B receptor of TUDOR domain; pfam09465"
                     /db_xref="CDD:462808"
     Region          52..109
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3U9G9; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:21795390; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:21795390; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Region          205..615
                     /region_name="ICMT"
                     /note="Isoprenylcysteine carboxyl methyltransferase (ICMT)
                     family; cl21511"
                     /db_xref="CDD:473892"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            258..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            299..319
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            326..346
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            386..406
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            447..467
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            481..501
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            561..581
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14739.2)"
     Site            594
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     Site            601
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14739.2)"
     CDS             1..615
                     /gene="LBR"
                     /gene_synonym="C14SR; DHCR14B; LMN2R; PHA; PHASK; TDRD18"
                     /coded_by="NM_002296.4:100..1947"
                     /db_xref="CCDS:CCDS1545.1"
                     /db_xref="GeneID:3930"
                     /db_xref="HGNC:HGNC:6518"
                     /db_xref="MIM:600024"
ORIGIN      
        1 mpsrkfadge vvrgrwpgss lyyeveilsh dstsqlytvk ykdgtelelk endikpltsf
       61 rqrkggstss spsrrrgsrs rsrsrspgrp pksarrsasa shqadikear revevkltpl
      121 ilkpfgnsis ryngepehie rndaphkntq ekfslsqess yiatqyslrp rreevklkei
      181 dskeekyvak elavrtfevt pirakdlefg gvpgvflimf glpvflflll lmckqkdpsl
      241 lnfppplpal yelwetrvfg vyllwfliqv lfyllpigkv vegtplidgr rlkyrlngfy
      301 afiltsavig tslfqgvefh yvyshflqfa laatvfcvvl svylymrslk aprndlspas
      361 sgnavydffi grelnprigt fdlkyfcelr pgligwvvin lvmllaemki qdravpslam
      421 ilvnsfqlly vvdalwneea llttmdiihd gfgfmlafgd lvwvpfiysf qafylvshpn
      481 evswpmasli ivlklcgyvi frgansqkna frknpsdpkl ahlktihtst gknllvsgww
      541 gfvrhpnylg dlimalawsl pcgfnhilpy fyiiyftmll vhreardeyh ckkkygvawe
      601 kycqrvpyri fpyiy
//
LOCUS       NP_001354688            1298 aa            linear   PRI 20-NOV-2025
DEFINITION  protein broad-minded isoform 2 [Homo sapiens].
ACCESSION   NP_001354688 XP_016865886
VERSION     NP_001354688.1
DBSOURCE    REFSEQ: accession NM_001367759.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1298)
  AUTHORS   Bocquet,B., Borday,C., Erkilic,N., Mamaeva,D., Donval,A.,
            Masson,C., Parain,K., Kaminska,K., Quinodoz,M., Perea-Romero,I.,
            Garcia-Garcia,G., Jimenez-Medina,C., Boukhaddaoui,H., Coget,A.,
            Leboucq,N., Calzetti,G., Gandolfi,S., Percesepe,A., Barili,V.,
            Uliana,V., Delsante,M., Bozzetti,F., Scholl,H.P., Corton,M.,
            Ayuso,C., Millan,J.M., Rivolta,C., Meunier,I., Perron,M. and
            Kalatzis,V.
  TITLE     TBC1D32 variants disrupt retinal ciliogenesis and cause retinitis
            pigmentosa
  JOURNAL   JCI Insight 8 (21), e169426 (2023)
   PUBMED   37768732
  REMARK    GeneRIF: TBC1D32 variants disrupt retinal ciliogenesis and cause
            retinitis pigmentosa.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1298)
  AUTHORS   Satoda,Y., Noguchi,T., Fujii,T., Taniguchi,A., Katoh,Y. and
            Nakayama,K.
  TITLE     BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1
  JOURNAL   Mol Biol Cell 33 (9), ar79 (2022)
   PUBMED   35609210
  REMARK    GeneRIF: BROMI/TBC1D32 together with CCRK/CDK20 and FAM149B1/JBTS36
            contributes to intraflagellar transport turnaround involving
            ICK/CILK1.
REFERENCE   3  (residues 1 to 1298)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1298)
  AUTHORS   Alsahan,N. and Alkuraya,F.S.
  TITLE     Confirming TBC1D32-related ciliopathy in humans
  JOURNAL   Am J Med Genet A 182 (8), 1985-1987 (2020)
   PUBMED   32573025
  REMARK    GeneRIF: Confirming TBC1D32-related ciliopathy in humans.
REFERENCE   5  (residues 1 to 1298)
  AUTHORS   Hietamaki,J., Gregory,L.C., Ayoub,S., Iivonen,A.P., Vaaralahti,K.,
            Liu,X., Brandstack,N., Buckton,A.J., Laine,T., Kansakoski,J.,
            Hero,M., Miettinen,P.J., Varjosalo,M., Wakeling,E., Dattani,M.T.
            and Raivio,T.
  TITLE     Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism
  JOURNAL   J Clin Endocrinol Metab 105 (6), 1748-1758 (2020)
   PUBMED   32060556
  REMARK    GeneRIF: Loss-of-Function Variants in TBC1D32 Underlie Syndromic
            Hypopituitarism.
REFERENCE   6  (residues 1 to 1298)
  AUTHORS   Shaheen,R., Jiang,N., Alzahrani,F., Ewida,N., Al-Sheddi,T.,
            Alobeid,E., Musaev,D., Stanley,V., Hashem,M., Ibrahim,N.,
            Abdulwahab,F., Alshenqiti,A., Sonmez,F.M., Saqati,N., Alzaidan,H.,
            Al-Qattan,M.M., Al-Mohanna,F., Gleeson,J.G. and Alkuraya,F.S.
  TITLE     Bi-allelic Mutations in FAM149B1 Cause Abnormal Primary Cilium and
            a Range of Ciliopathy Phenotypes in Humans
  JOURNAL   Am J Hum Genet 104 (4), 731-737 (2019)
   PUBMED   30905400
REFERENCE   7  (residues 1 to 1298)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1298)
  AUTHORS   Adly,N., Alhashem,A., Ammari,A. and Alkuraya,F.S.
  TITLE     Ciliary genes TBC1D32/C6orf170 and SCLT1 are mutated in patients
            with OFD type IX
  JOURNAL   Hum Mutat 35 (1), 36-40 (2014)
   PUBMED   24285566
  REMARK    GeneRIF: study identified 2 cases with a severe ciliopathy
            phenotype consistent with oro-facio-digital syndrome type IX; the
            autozygome of each index harbored a single truncating variant and
            the affected genes (SCLT1 and TBC1D32/C6orf170) have roles in
            centrosomal biology and ciliogenesis; findings suggest a role of
            SCLT1 and TBC1D32 in ciliopathy pathogenesis
REFERENCE   9  (residues 1 to 1298)
  AUTHORS   Cirulli,E.T., Kasperaviciute,D., Attix,D.K., Need,A.C., Ge,D.,
            Gibson,G. and Goldstein,D.B.
  TITLE     Common genetic variation and performance on standardized cognitive
            tests
  JOURNAL   Eur J Hum Genet 18 (7), 815-820 (2010)
   PUBMED   20125193
  REMARK    Erratum:[Eur J Hum Genet. 2010 Jul;18(7):820]
REFERENCE   10 (residues 1 to 1298)
  AUTHORS   Ko,H.W., Norman,R.X., Tran,J., Fuller,K.P., Fukuda,M. and
            Eggenschwiler,J.T.
  TITLE     Broad-minded links cell cycle-related kinase to cilia assembly and
            hedgehog signal transduction
  JOURNAL   Dev Cell 18 (2), 237-247 (2010)
   PUBMED   20159594
  REMARK    GeneRIF: Studies in mouse and zebrafish implicate that TBC1D32 is
            involved in sonic hedgehog signaling.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139098.15, AL589910.9,
            AL590225.4, AL365508.19 and AL035593.11.
            
            On Dec 14, 2018 this sequence version replaced XP_016865886.1.
            
            Summary: This gene encodes a TBC-domain containing protein. Studies
            of a similar protein in mouse and zebrafish suggest that the
            encoded protein is involved in sonic hedgehog signaling, and that
            it interacts with and stabilizes cell cycle-related kinase.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.178768.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..1298
                     /product="protein broad-minded isoform 2"
                     /note="protein broad-minded; broad-minded homolog"
                     /calculated_mol_wt=149298
     Region          12..1295
                     /region_name="BROMI"
                     /note="Broad-minded protein; pfam14961"
                     /db_xref="CDD:464406"
     CDS             1..1298
                     /gene="TBC1D32"
                     /gene_synonym="ALHSA; BROMI; C6orf170; C6orf171; OFD9;
                     RP100"
                     /coded_by="NM_001367759.1:114..4010"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS93996.1"
                     /db_xref="GeneID:221322"
                     /db_xref="HGNC:HGNC:21485"
                     /db_xref="MIM:615867"
ORIGIN      
        1 mahfssedqa mlqamlrrlf qsvkekitga pslecaeeil lhleetdenf hnyefvkylr
       61 qhigntlgsm ieeemekcts drnqgeecgy dtvvqqvtkr tqeskeykem mhylknimia
      121 vvesminkfe edetrnqerq kkiqkekshs yrtdncsdsd sslnqsykfc qgklqlildq
      181 ldpgqpkevr yealqtlcsa ppsdvlncen wttlcekltv slsdpdpvfs drilkfcaqt
      241 fllsplhmtk eiytslakyl esyflsrenh iptlsagvdi tnpnmtrllk kvrllneyqk
      301 eapsfwirhp ekymeeives tlslltvkhn qshvvsqkil dpiyffalvd tkavwfkkwm
      361 hahysrttvl rlletkyksl vttaiqqcvq yfemcktrka detlghskhc rnkqktfyyl
      421 gqelqyiyfi hslcllgrll iykqgrklfp iklknkkglv slidllvlft qliyyspscp
      481 kmtsaahsen yspasmvtev lwilsdqkec aveclynniv ietllqpihn lmkgneaspn
      541 csetalihia gilariasve eglilllyga nmnsseespt gahiiaqfsk klldedisif
      601 sgsemlpvvk gafisvcrhi ystceglqvl itynlhesia kawkktslls eriptpvegs
      661 dsvssvsqes qnimawednl lddllhfaat pkgllllqrt gainecvtfi fnryakklqv
      721 srhkkfgygv lvtrvastaa ggialkksgf inelitelws nleygrddvr vthprttpvd
      781 pidrscqksf lalvnllsyp aiyelvrnqd lpnkteyslr evptcvidii drliilnsea
      841 kirslfnyeq shifglrlls viccdldtll lleaqyqvse mllnaqeeni leiseshrdf
      901 iidglsvern hvlvrinlvg gplerilppr lleksdnpyp wpmfssyplp ncylsditrn
      961 agikqdndld klllclkisd kqtewiencq rqfckmmkak pdiisgeali ellekfvlhl
     1021 tespsecyfp sveytatdan vkneslssvq qlgikmtvry gkflsllkdg aendltwvlk
     1081 hcerflkqqq tsikssllcl qgnyaghdwf vsslfmimlg dkektfqflh qfsrlltsaf
     1141 lwlprlhiss ylpndtvesg ihpvyfcsth yiemllkael plvfsafhms gfapsqiclq
     1201 witqcfwnyl dwieichyia tcvflgpdyq vyiciavfkh lqqdilqhtq tqdlqvflke
     1261 ealhgfrvsd yfeymeileq nyrtvllrdm rnirlqst
//
LOCUS       NP_001274742             517 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-1-syntrophin isoform 1 [Homo sapiens].
ACCESSION   NP_001274742 XP_005251318
VERSION     NP_001274742.1
DBSOURCE    REFSEQ: accession NM_001287813.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 517)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 517)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 517)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 517)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   5  (residues 1 to 517)
  AUTHORS   Hafner,A., Obermajer,N. and Kos,J.
  TITLE     gamma-1-syntrophin mediates trafficking of gamma-enolase towards
            the plasma membrane and enhances its neurotrophic activity
  JOURNAL   Neurosignals 18 (4), 246-258 (2010)
   PUBMED   21358174
  REMARK    GeneRIF: Brain-specific gamma1-syntrophin participates in
            gamma-enolase translocation towards the plasma membrane, a
            pre-requisite for its neurotrophic activity.
REFERENCE   6  (residues 1 to 517)
  AUTHORS   Hogan,A., Yakubchyk,Y., Chabot,J., Obagi,C., Daher,E., Maekawa,K.
            and Gee,S.H.
  TITLE     The phosphoinositol 3,4-bisphosphate-binding protein TAPP1
            interacts with syntrophins and regulates actin cytoskeletal
            organization
  JOURNAL   J Biol Chem 279 (51), 53717-53724 (2004)
   PUBMED   15485858
REFERENCE   7  (residues 1 to 517)
  AUTHORS   Bashiardes,S., Veile,R., Allen,M., Wise,C.A., Dobbs,M.,
            Morcuende,J.A., Szappanos,L., Herring,J.A., Bowcock,A.M. and
            Lovett,M.
  TITLE     SNTG1, the gene encoding gamma1-syntrophin: a candidate gene for
            idiopathic scoliosis
  JOURNAL   Hum Genet 115 (1), 81-89 (2004)
   PUBMED   15088139
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 517)
  AUTHORS   Hogan,A., Shepherd,L., Chabot,J., Quenneville,S., Prescott,S.M.,
            Topham,M.K. and Gee,S.H.
  TITLE     Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta.
            Regulation of nuclear localization by PDZ interactions
  JOURNAL   J Biol Chem 276 (28), 26526-26533 (2001)
   PUBMED   11352924
REFERENCE   9  (residues 1 to 517)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 517)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
  REMARK    GeneRIF: suggests a differentiated role of a modified
            dystrophin-associated complex in the central nervous system
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314084.1, AC087173.5 and
            AC090450.6.
            
            On Dec 20, 2013 this sequence version replaced XP_005251318.1.
            
            Summary: The protein encoded by this gene is a member of the
            syntrophin family. Syntrophins are cytoplasmic peripheral membrane
            proteins that typically contain 2 pleckstrin homology (PH) domains,
            a PDZ domain that bisects the first PH domain, and a C-terminal
            domain that mediates dystrophin binding. This family member plays a
            role in mediating gamma-enolase trafficking to the plasma membrane
            and in enhancing its neurotrophic activity. Mutations in this gene
            are associated with idiopathic scoliosis. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 4 all encode isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314084.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2144335 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..517
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..517
                     /product="gamma-1-syntrophin isoform 1"
                     /note="gamma1-syntrophin; syntrophin 4;
                     gamma-1-syntrophin"
                     /calculated_mol_wt=57838
     Region          56..138
                     /region_name="PDZ_syntrophin-like"
                     /note="PDZ domain of syntrophins, and related domains;
                     cd06801"
                     /db_xref="CDD:467262"
     Site            order(67..73,85,88,118,122,125..126)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467262"
     Region          191..259
                     /region_name="PH"
                     /note="Pleckstrin homology (PH) domain; cd00821"
                     /db_xref="CDD:275388"
     Region          284..389
                     /region_name="PH"
                     /note="Pleckstrin homology domain; smart00233"
                     /db_xref="CDD:214574"
     CDS             1..517
                     /gene="SNTG1"
                     /gene_synonym="G1SYN; SYN4"
                     /coded_by="NM_001287813.3:365..1918"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6147.1"
                     /db_xref="GeneID:54212"
                     /db_xref="HGNC:HGNC:13740"
                     /db_xref="MIM:608714"
ORIGIN      
        1 mdfrtaceet ktgicllqdg nqepfkvrlh lakdilmiqe qdvicvsgep fysgertvti
       61 rrqtvggfgl sikggaehni pvvvskiske qraelsgllf igdailqing invrkcrhee
      121 vvqvlrnage evtltvsflk rapaflklpl nedcacapsd qssgtssplc dsglhlnyhp
      181 nntdtlscss wptspglrwe krwcdlrlip llhsrfsqyv pgtdlsrqna fqviavdgvc
      241 tgiiqclsae dcvdwlqaia tnisnltkhn ikkinrnfpv nqqivymgwc eareqdplqd
      301 rvysptflal rgsclykfla ppvttwdwtr aektfsvyei mckilkdsdl ldrrkqcftv
      361 qsesgedlyf svelesdlaq werafqtatf leveriqckt yacvleshlm gltidfstgf
      421 icfdaatkav lwrykfsqlk gssddgkski kflfqnpdtk qieakelefs nlfavlhcih
      481 sffaakvacl dplflgnqat astaassatt skakytt
//
LOCUS       NP_037410                197 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17C precursor [Homo sapiens].
ACCESSION   NP_037410
VERSION     NP_037410.1
DBSOURCE    REFSEQ: accession NM_013278.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Garcia,E.M., Lenz,J.D., Schaub,R.E., Hackett,K.T., Salgado-Pabon,W.
            and Dillard,J.P.
  TITLE     IL-17C is a driver of damaging inflammation during Neisseria
            gonorrhoeae infection of human Fallopian tube
  JOURNAL   Nat Commun 15 (1), 3756 (2024)
   PUBMED   38704381
  REMARK    GeneRIF: IL-17C is a driver of damaging inflammation during
            Neisseria gonorrhoeae infection of human Fallopian tube.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Zhang,F., Yin,J., Liu,L., Liu,S., Zhang,G., Kong,Y., Wang,Y.,
            Wang,N., Chen,X. and Wang,F.
  TITLE     IL-17C neutralization protects the kidney against acute injury and
            chronic injury
  JOURNAL   EBioMedicine 92, 104607 (2023)
   PUBMED   37263138
  REMARK    GeneRIF: IL-17C neutralization protects the kidney against acute
            injury and chronic injury.
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Swedik,S.M., Madola,A., Cruz,M.A., Llorens-Bonilla,B.J. and
            Levine,A.D.
  TITLE     Th17-Derived Cytokines Synergistically Enhance IL-17C Production by
            the Colonic Epithelium
  JOURNAL   J Immunol 209 (9), 1768-1777 (2022)
   PUBMED   36130829
  REMARK    GeneRIF: Th17-Derived Cytokines Synergistically Enhance IL-17C
            Production by the Colonic Epithelium.
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Soares-Schanoski,A., Sauerwald,N., Goforth,C.W., Periasamy,S.,
            Weir,D.L., Lizewski,S., Lizewski,R., Ge,Y., Kuzmina,N.A.,
            Nair,V.D., Vangeti,S., Marjanovic,N., Cappuccio,A., Cheng,W.S.,
            Mofsowitz,S., Miller,C.M., Yu,X.B., George,M.C., Zaslavsky,E.,
            Bukreyev,A., Troyanskaya,O.G., Sealfon,S.C., Letizia,A.G. and
            Ramos,I.
  TITLE     Asymptomatic SARS-CoV-2 Infection Is Associated With Higher Levels
            of Serum IL-17C, Matrix Metalloproteinase 10 and Fibroblast Growth
            Factors Than Mild Symptomatic COVID-19
  JOURNAL   Front Immunol 13, 821730 (2022)
   PUBMED   35479098
  REMARK    GeneRIF: Asymptomatic SARS-CoV-2 Infection Is Associated With
            Higher Levels of Serum IL-17C, Matrix Metalloproteinase 10 and
            Fibroblast Growth Factors Than Mild Symptomatic COVID-19.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Swedik,S., Madola,A. and Levine,A.
  TITLE     IL-17C in human mucosal immunity: More than just a middle child
  JOURNAL   Cytokine 146, 155641 (2021)
   PUBMED   34293699
  REMARK    Review article
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Rajaraman,P., Brenner,A.V., Butler,M.A., Wang,S.S., Pfeiffer,R.M.,
            Ruder,A.M., Linet,M.S., Yeager,M., Wang,Z., Orr,N., Fine,H.A.,
            Kwon,D., Thomas,G., Rothman,N., Inskip,P.D. and Chanock,S.J.
  TITLE     Common variation in genes related to innate immunity and risk of
            adult glioma
  JOURNAL   Cancer Epidemiol Biomarkers Prev 18 (5), 1651-1658 (2009)
   PUBMED   19423540
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Lock,C., Hermans,G., Pedotti,R., Brendolan,A., Schadt,E.,
            Garren,H., Langer-Gould,A., Strober,S., Cannella,B., Allard,J.,
            Klonowski,P., Austin,A., Lad,N., Kaminski,N., Galli,S.J.,
            Oksenberg,J.R., Raine,C.S., Heller,R. and Steinman,L.
  TITLE     Gene-microarray analysis of multiple sclerosis lesions yields new
            targets validated in autoimmune encephalomyelitis
  JOURNAL   Nat Med 8 (5), 500-508 (2002)
   PUBMED   11984595
  REMARK    GeneRIF: expressed in multiple sclerosis brain lesions
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Li,H., Chen,J., Huang,A., Stinson,J., Heldens,S., Foster,J.,
            Dowd,P., Gurney,A.L. and Wood,W.I.
  TITLE     Cloning and characterization of IL-17B and IL-17C, two new members
            of the IL-17 cytokine family
  JOURNAL   Proc Natl Acad Sci U S A 97 (2), 773-778 (2000)
   PUBMED   10639155
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC116552.2.
            
            Summary: The protein encoded by this gene is a T cell-derived
            cytokine that shares the sequence similarity with IL17. This
            cytokine was reported to stimulate the release of tumor necrosis
            factor alpha and interleukin 1 beta from a monocytic cell line. The
            expression of this cytokine was found to be restricted to activated
            T cells. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358471.1, AF152099.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2163459
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000244241.5/ ENSP00000244241.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.2"
     Protein         1..197
                     /product="interleukin-17C precursor"
                     /note="cytokine CX2"
                     /calculated_mol_wt=19739
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2044
     Region          104..192
                     /region_name="IL17"
                     /note="Interleukin-17; pfam06083"
                     /db_xref="CDD:461823"
     CDS             1..197
                     /gene="IL17C"
                     /gene_synonym="CX2; IL-17C"
                     /coded_by="NM_013278.4:71..664"
                     /db_xref="CCDS:CCDS42217.1"
                     /db_xref="GeneID:27189"
                     /db_xref="HGNC:HGNC:5983"
                     /db_xref="MIM:604628"
ORIGIN      
        1 mtllpgllfl twlhtclahh dpslrghphs hgtphcysae elplgqapph llargakwgq
       61 alpvalvssl eaashrgrhe rpsattqcpv lrpeevlead thqrsispwr yrvdtdedry
      121 pqklafaecl crgcidartg retaalnsvr llqsllvlrr rpcsrdgsgl ptpgafafht
      181 efihvpvgct cvlprsv
//
LOCUS       NP_001340                501 aa            linear   PRI 20-NOV-2025
DEFINITION  aspartate--tRNA ligase, cytoplasmic isoform 1 [Homo sapiens].
ACCESSION   NP_001340
VERSION     NP_001340.2
DBSOURCE    REFSEQ: accession NM_001349.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Xiong,H., Liao,M., Zhang,H., Li,Y., Bai,J., Zhang,J., Li,L. and
            Zhang,L.
  TITLE     DARS expression in BCR/ABL1-negative myeloproliferative neoplasms
            and its association with the immune microenvironment
  JOURNAL   Sci Rep 14 (1), 16711 (2024)
   PUBMED   39030308
  REMARK    GeneRIF: DARS expression in BCR/ABL1-negative myeloproliferative
            neoplasms and its association with the immune microenvironment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Liu,B., Katoh,H., Komura,D., Yamamoto,A., Ochi,M., Onoyama,T.,
            Abe,H., Ushiku,T., Seto,Y., Suo,J. and Ishikawa,S.
  TITLE     Functional genomics screening identifies aspartyl-tRNA synthetase
            as a novel prognostic marker and a therapeutic target for gastric
            cancers
  JOURNAL   J Pathol 258 (2), 106-120 (2022)
   PUBMED   35696251
  REMARK    GeneRIF: Functional genomics screening identifies aspartyl-tRNA
            synthetase as a novel prognostic marker and a therapeutic target
            for gastric cancers.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Klugmann,M., Kalotay,E., Delerue,F., Ittner,L.M., Bongers,A.,
            Yu,J., Morris,M.J., Housley,G.D. and Frohlich,D.
  TITLE     Developmental delay and late onset HBSL pathology in hypomorphic
            Dars1M256L mice
  JOURNAL   Neurochem Res 47 (7), 1972-1984 (2022)
   PUBMED   35357600
  REMARK    GeneRIF: Developmental delay and late onset HBSL pathology in
            hypomorphic Dars1(M256L) mice.
            Erratum:[Neurochem Res. 2022 Jul;47(7):1985-1990. doi:
            10.1007/s11064-022-03602-3. PMID: 35449376]
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Khan,K., Baleanu-Gogonea,C., Willard,B., Gogonea,V. and Fox,P.L.
  TITLE     3-Dimensional architecture of the human multi-tRNA synthetase
            complex
  JOURNAL   Nucleic Acids Res 48 (15), 8740-8754 (2020)
   PUBMED   32644155
REFERENCE   5  (residues 1 to 501)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Quevillon,S., Robinson,J.C., Berthonneau,E., Siatecka,M. and
            Mirande,M.
  TITLE     Macromolecular assemblage of aminoacyl-tRNA synthetases:
            identification of protein-protein interactions and characterization
            of a core protein
  JOURNAL   J Mol Biol 285 (1), 183-195 (1999)
   PUBMED   9878398
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Beaulande,M., Tarbouriech,N. and Hartlein,M.
  TITLE     Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence,
            functional expression in Escherichia coli and characterization as
            human autoantigen
  JOURNAL   Nucleic Acids Res 26 (2), 521-524 (1998)
   PUBMED   9421509
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Reed,V.S., Wastney,M.E. and Yang,D.C.
  TITLE     Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA
            synthetase to the elongation factor 1 alpha
  JOURNAL   J Biol Chem 269 (52), 32932-32936 (1994)
   PUBMED   7806521
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Escalante,C. and Yang,D.C.
  TITLE     Expression of human aspartyl-tRNA synthetase in Escherichia coli.
            Functional analysis of the N-terminal putative amphiphilic helix
  JOURNAL   J Biol Chem 268 (8), 6014-6023 (1993)
   PUBMED   8449960
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Jacobo-Molina,A., Peterson,R. and Yang,D.C.
  TITLE     cDNA sequence, predicted primary structure, and evolving
            amphiphilic helix of human aspartyl-tRNA synthetase
  JOURNAL   J Biol Chem 264 (28), 16608-16612 (1989)
   PUBMED   2674137
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA597505.1, BC000629.2,
            BU615302.1, AC011999.9 and BX101357.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 15, 2004 this sequence version replaced NP_001340.1.
            
            Summary: This gene encodes a member of a multienzyme complex that
            functions in mediating the attachment of amino acids to their
            cognate tRNAs. The encoded protein ligates L-aspartate to
            tRNA(Asp). Mutations in this gene have been found in patients
            showing hypomyelination with brainstem and spinal cord involvement
            and leg spasticity. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jun 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK129521.1, SRR3476690.947879.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264161.9/ ENSP00000264161.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.3"
     Protein         1..501
                     /product="aspartate--tRNA ligase, cytoplasmic isoform 1"
                     /EC_number="6.1.1.12"
                     /note="aspartate tRNA ligase 1, cytoplasmic; aspartyl-tRNA
                     synthetase, cytoplasmic; cell proliferation-inducing gene
                     40 protein; testicular tissue protein Li 192"
                     /calculated_mol_wt=57005
     Region          3..501
                     /region_name="PLN02850"
                     /note="aspartate-tRNA ligase"
                     /db_xref="CDD:215456"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Region          251..254
                     /region_name="Aspartate. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P14868.2)"
     Site            374
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P14868.2)"
     Region          411..415
                     /region_name="Binding site for the 3'-end of tRNA.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P14868.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P14868.2)"
     CDS             1..501
                     /gene="DARS1"
                     /gene_synonym="aspRS; DARS; HBSL"
                     /coded_by="NM_001349.4:159..1664"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2180.1"
                     /db_xref="GeneID:1615"
                     /db_xref="HGNC:HGNC:2678"
                     /db_xref="MIM:603084"
ORIGIN      
        1 mpsasasrks qekpreimda aedyakeryg issmiqsqek pdrvlvrvrd ltiqkadevv
       61 wvrarvhtsr akgkqcflvl rqqqfnvqal vavgdhaskq mvkfaanink esivdvegvv
      121 rkvnqkigsc tqqdvelhvq kiyvislaep rlplqlddav rpeaegeeeg ratvnqdtrl
      181 dnrvidlrts tsqavfrlqs gichlfretl inkgfveiqt pkiisaaseg ganvftvsyf
      241 knnaylaqsp qlykqmcica dfekvfsigp vfraedsnth rhltefvgld iemafnyhyh
      301 evmeeiadtm vqifkglqer fqteiqtvnk qfpcepfkfl eptlrleyce alamlreagv
      361 emgdeddlst pnekllghlv kekydtdfyi ldkyplavrp fytmpdprnp kqsnsydmfm
      421 rgeeilsgaq rihdpqllte ralhhgidle kikayidsfr fgapphaggg iglervtmlf
      481 lglhnvrqts mfprdpkrlt p
//
LOCUS       NP_079040               1116 aa            linear   PRI 20-NOV-2025
DEFINITION  cation channel sperm-associated auxiliary subunit beta precursor
            [Homo sapiens].
ACCESSION   NP_079040
VERSION     NP_079040.2
DBSOURCE    REFSEQ: accession NM_024764.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1116)
  AUTHORS   Lin,S., Ke,M., Zhang,Y., Yan,Z. and Wu,J.
  TITLE     Structure of a mammalian sperm cation channel complex
  JOURNAL   Nature 595 (7869), 746-750 (2021)
   PUBMED   34225353
REFERENCE   2  (residues 1 to 1116)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   3  (residues 1 to 1116)
  AUTHORS   Brown,S.G., Miller,M.R., Lishko,P.V., Lester,D.H., Publicover,S.J.,
            Barratt,C.L.R. and Martins Da Silva,S.
  TITLE     Homozygous in-frame deletion in CATSPERE in a man producing
            spermatozoa with loss of CatSper function and compromised
            fertilizing capacity
  JOURNAL   Hum Reprod 33 (10), 1812-1816 (2018)
   PUBMED   30239785
REFERENCE   4  (residues 1 to 1116)
  AUTHORS   Prakash,T., Sharma,V.K., Adati,N., Ozawa,R., Kumar,N., Nishida,Y.,
            Fujikake,T., Takeda,T. and Taylor,T.D.
  TITLE     Expression of conjoined genes: another mechanism for gene
            regulation in eukaryotes
  JOURNAL   PLoS One 5 (10), e13284 (2010)
   PUBMED   20967262
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1116)
  AUTHORS   Koller,D.L., Ichikawa,S., Lai,D., Padgett,L.R., Doheny,K.F.,
            Pugh,E., Paschall,J., Hui,S.L., Edenberg,H.J., Xuei,X., Peacock,M.,
            Econs,M.J. and Foroud,T.
  TITLE     Genome-wide association study of bone mineral density in
            premenopausal European-American women and replication in
            African-American women
  JOURNAL   J Clin Endocrinol Metab 95 (4), 1802-1809 (2010)
   PUBMED   20164292
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   6  (residues 1 to 1116)
  AUTHORS   Liu,J., Xia,J., Cho,K.H., Clapham,D.E. and Ren,D.
  TITLE     CatSperbeta, a novel transmembrane protein in the CatSper channel
            complex
  JOURNAL   J Biol Chem 282 (26), 18945-18952 (2007)
   PUBMED   17478420
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI559703.1, AK126034.1, AL133373.5 and BC126214.1.
            
            On Aug 18, 2004 this sequence version replaced NP_079040.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126034.1, BC126214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256343.8/ ENSP00000256343.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1116
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.12"
     Protein         1..1116
                     /product="cation channel sperm-associated auxiliary
                     subunit beta precursor"
                     /note="cation channel, sperm associated beta; cation
                     channel sperm-associated protein subunit beta;
                     catSper-beta; cation channel sperm associated auxiliary
                     subunit beta"
                     /calculated_mol_wt=124583
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2359
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            100
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            226
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Region          569..1085
                     /region_name="CATSPERB"
                     /note="Cation channel sperm-associated protein subunit
                     beta protein family; pfam15149"
                     /db_xref="CDD:464533"
     Site            618
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            913
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            921
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            1010
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            1015
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H7T0.2)"
     Site            1054..1076
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7T0.2)"
     CDS             1..1116
                     /gene="CATSPERB"
                     /gene_synonym="C14orf161; CatSper(beta)"
                     /coded_by="NM_024764.4:158..3508"
                     /db_xref="CCDS:CCDS32142.1"
                     /db_xref="GeneID:79820"
                     /db_xref="HGNC:HGNC:20500"
                     /db_xref="MIM:611169"
ORIGIN      
        1 mespliyvsv lllnifefss givynkddte krfacsnkgf pqeneiikly lflenlkiqc
       61 ffqteneias kamlsvftsg glapslgimn styngifhfn ltlfsdrilw lvdiprenit
      121 qstdiaavee wlvritlhhg lniyategtl ldvirepilq wtpgdvipes eisklyphvv
      181 dlkvtkcpca ndvallgfiv dtivdgvyig itfggfwhdy dttwfnmtqt iysqlqeeye
      241 dlslvdmvlt nhflviltsl glfvsedlry psrhslsfsr adfcgfervd yvkgklwyne
      301 rcfanrehfe vdyvtvtfer nrtlsesssc fysqepflew vpclphifkg ikifptvltf
      361 lvdqergtgv ylfynkvrkt aiasvstlrn nepnsqskfp ifrfpssfss pvgmvfhprs
      421 hflyaygnqi wlsvdggntf qlianfhddi ikktfhsfyt saitfvsqrg kvystkagmg
      481 rysavgsvte riftlyydhl gflhkltlgr feasgpptaf gnsrnlfgqp pdmgfetala
      541 pqhtsldeii ffayvpenep qetiyskkfg nihygkvihs gktgrayirk vlqhttpkgf
      601 lssviaemke pfgleevnes sclsssllin kagnvykltl dsqvvqalfe dtdiektvvl
      661 pgyssflits ildnknalai atmpesapnn mtflkstwfl ynfgqrngrt wkiyskpcny
      721 wfqhddspsl nivkyidlgn syvlkakvir nakgfrmlei plltvfvgnp nllevtaevt
      781 fddtdsyvit isaaskvlhq gstslafimw sastecfvtt mvptlksscs ylrsmhhips
      841 kfipfedwis gvhkdsqgfn liktlpinyr ppsnmgiaip ltdnfyhadp skpiprnmfh
      901 mskktgkfkq canvstreec nctkdqkfsh avafsdcrek vprfkfpitq ypvsleiine
      961 dgrvplqspy lvtvtevnmr hnwklkhtvp enikrmkqlv epilgaavyn psglnlsikg
     1021 selfhfrvtv isgvtfcnli eefqiyvdea plpfpghtli avatavvlgg lifiafmfql
     1081 qgihpwrtfq rwirrnqekf ssislselih rsksee
//
LOCUS       NP_001356787             136 aa            linear   PRI 20-NOV-2025
DEFINITION  protein tyrosine phosphatase type IVA 2 isoform 4 [Homo sapiens].
ACCESSION   NP_001356787 XP_016857890
VERSION     NP_001356787.1
DBSOURCE    REFSEQ: accession NM_001369858.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Hardy,S., Zolotarov,Y., Coleman,J., Roitman,S., Khursheed,H.,
            Aubry,I., Uetani,N. and Tremblay,M.L.
  TITLE     PRL-1/2 phosphatases control TRPM7 magnesium-dependent function to
            regulate cellular bioenergetics
  JOURNAL   Proc Natl Acad Sci U S A 120 (14), e2221083120 (2023)
   PUBMED   36972446
  REMARK    GeneRIF: This study established the existence of a magnesium
            transporter protein complex (PTP4A2/CNNM3/TRPM7) governing the
            cellular uptake of this divalent cation. Moreover, PTP4A2 acts as a
            magnesium biosensor, controlling the activity of this complex to
            reprogram cellular metabolism.
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Li,Q., Bai,Y., Lyle,L.T., Yu,G., Amarasinghe,O., Nguele Meke,F.,
            Carlock,C. and Zhang,Z.Y.
  TITLE     Mechanism of PRL2 phosphatase-mediated PTEN degradation and
            tumorigenesis
  JOURNAL   Proc Natl Acad Sci U S A 117 (34), 20538-20548 (2020)
   PUBMED   32788364
  REMARK    GeneRIF: Mechanism of PRL2 phosphatase-mediated PTEN degradation
            and tumorigenesis.
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Cai,F., Huang,Y., Wang,M., Sun,M., Zhao,Y. and Hattori,M.
  TITLE     A FRET-based screening method to detect potential inhibitors of the
            binding of CNNM3 to PRL2
  JOURNAL   Sci Rep 10 (1), 12879 (2020)
   PUBMED   32733084
  REMARK    GeneRIF: A FRET-based screening method to detect potential
            inhibitors of the binding of CNNM3 to PRL2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Si,X., Zeng,Q., Ng,C.H., Hong,W. and Pallen,C.J.
  TITLE     Interaction of farnesylated PRL-2, a protein-tyrosine phosphatase,
            with the beta-subunit of geranylgeranyltransferase II
  JOURNAL   J Biol Chem 276 (35), 32875-32882 (2001)
   PUBMED   11447212
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Gjorloff-Wingren,A., Saxena,M., Han,S., Wang,X., Alonso,A.,
            Renedo,M., Oh,P., Williams,S., Schnitzer,J. and Mustelin,T.
  TITLE     Subcellular localization of intracellular protein tyrosine
            phosphatases in T cells
  JOURNAL   Eur J Immunol 30 (8), 2412-2421 (2000)
   PUBMED   10940933
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Zeng,Q., Hong,W. and Tan,Y.H.
  TITLE     Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
            phosphatases homologous to PRL-1
  JOURNAL   Biochem Biophys Res Commun 244 (2), 421-427 (1998)
   PUBMED   9514946
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Cates,C.A., Michael,R.L., Stayrook,K.R., Harvey,K.A., Burke,Y.D.,
            Randall,S.K., Crowell,P.L. and Crowell,D.N.
  TITLE     Prenylation of oncogenic human PTP(CAAX) protein tyrosine
            phosphatases
  JOURNAL   Cancer Lett 110 (1-2), 49-55 (1996)
   PUBMED   9018080
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Zhao,Z., Lee,C.C., Monckton,D.G., Yazdani,A., Coolbaugh,M.I.,
            Li,X., Bailey,J., Shen,Y. and Caskey,C.T.
  TITLE     Characterization and genomic mapping of genes and pseudogenes of a
            new human protein tyrosine phosphatase
  JOURNAL   Genomics 35 (1), 172-181 (1996)
   PUBMED   8661118
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136115.21 and BC070181.1.
            
            On Apr 22, 2019 this sequence version replaced XP_016857890.1.
            
            Summary: The protein encoded by this gene belongs to a small class
            of the protein tyrosine phosphatase (PTP) family. PTPs are cell
            signaling molecules that play regulatory roles in a variety of
            cellular processes. PTPs in this class contain a protein tyrosine
            phosphatase catalytic domain and a characteristic C-terminal
            prenylation motif. This PTP has been shown to primarily associate
            with plasmic and endosomal membrane through its C-terminal
            prenylation. This PTP was found to interact with the beta-subunit
            of Rab geranylgeranyltransferase II (beta GGT II), and thus may
            function as a regulator of GGT II activity. Overexpression of this
            gene in mammalian cells conferred a transformed phenotype, which
            suggested its role in tumorigenesis. Alternatively spliced
            transcript variants have been described. Related pseudogenes exist
            on chromosomes 11, 12 and 17. [provided by RefSeq, Aug 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.452416.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..136
                     /product="protein tyrosine phosphatase type IVA 2 isoform
                     4"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase IVA; phosphatase of
                     regenerating liver 2; protein tyrosine phosphatase IVA2;
                     protein tyrosine phosphatase type IVA 2; PTP(CAAXII);
                     protein-tyrosine phosphatase of regenerating liver 2;
                     protein tyrosine phosphatase type IVA, member 2"
                     /calculated_mol_wt=15538
     Region          1..124
                     /region_name="PTP_DSP_cys"
                     /note="cys-based protein tyrosine phosphatase and
                     dual-specificity phosphatase superfamily; cl28904"
                     /db_xref="CDD:475123"
     CDS             1..136
                     /gene="PTP4A2"
                     /gene_synonym="HH13; HH7-2; HU-PP-1; OV-1; PRL-2; PRL2;
                     ptp-IV1a; ptp-IV1b; PTP4A; PTPCAAX2"
                     /coded_by="NM_001369858.1:635..1045"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS53292.1"
                     /db_xref="GeneID:8073"
                     /db_xref="HGNC:HGNC:9635"
                     /db_xref="MIM:601584"
ORIGIN      
        1 mnrpapveis yenmrflith nptnatlnkf tedwpfddga pppnqivddw lnllktkfre
       61 epgccvavhc vaglgrapvl valaliecgm kyedavqfir qkrrgafnsk qllylekyrp
      121 kmrlrfrdtn ghccvq
//
LOCUS       NP_001269234             332 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 25 isoform 3 [Homo sapiens].
ACCESSION   NP_001269234 XP_005247044
VERSION     NP_001269234.1
DBSOURCE    REFSEQ: accession NM_001282305.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Chen,K.Q., Lei,G.L., Ke,B.Y., Chen,L., Wang,Z.B. and Wang,S.Z.
  TITLE     STK25: a viable therapeutic target for cancer treatments?
  JOURNAL   Anticancer Drugs 34 (9), 995-1001 (2023)
   PUBMED   36728989
  REMARK    GeneRIF: STK25: a viable therapeutic target for cancer treatments?
            Review article
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Zhang,X., Wang,B.Z., Kim,M., Nash,T.R., Liu,B., Rao,J., Lock,R.,
            Tamargo,M., Soni,R.K., Belov,J., Li,E., Vunjak-Novakovic,G. and
            Fine,B.
  TITLE     STK25 inhibits PKA signaling by phosphorylating PRKAR1A
  JOURNAL   Cell Rep 40 (7), 111203 (2022)
   PUBMED   35977512
  REMARK    GeneRIF: STK25 inhibits PKA signaling by phosphorylating PRKAR1A.
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Chen,J., Gao,P., Peng,L., Liu,T., Wu,F., Xu,K., Chen,L., Tan,F.,
            Xing,P., Wang,Z., Di,J., Jiang,B. and Su,X.
  TITLE     Downregulation of STK25 promotes autophagy via the Janus kinase
            2/signal transducer and activator of transcription 3 pathway in
            colorectal cancer
  JOURNAL   Mol Carcinog 61 (6), 572-586 (2022)
   PUBMED   35349179
  REMARK    GeneRIF: Downregulation of STK25 promotes autophagy via the Janus
            kinase 2/signal transducer and activator of transcription 3 pathway
            in colorectal cancer.
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Findlay,G.M., Yan,L., Procter,J., Mieulet,V. and Lamb,R.F.
  TITLE     A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of
            mTOR signalling
  JOURNAL   Biochem J 403 (1), 13-20 (2007)
   PUBMED   17253963
  REMARK    GeneRIF: Ste20 family member (MAP4K3) that is required for maximal
            S6K (S6 kinase)/4E-BP1 [eIF4E (eukaryotic initiation factor 4E)
            that is required for maximal S6K (S6 kinase).
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Preisinger,C., Short,B., De Corte,V., Bruyneel,E., Haas,A.,
            Kopajtich,R., Gettemans,J. and Barr,F.A.
  TITLE     YSK1 is activated by the Golgi matrix protein GM130 and plays a
            role in cell migration through its substrate 14-3-3zeta
  JOURNAL   J Cell Biol 164 (7), 1009-1020 (2004)
   PUBMED   15037601
  REMARK    GeneRIF: 14-3-3zeta is a specific substrate for YSK1 that localizes
            to the Golgi apparatus, and potentially links YSK1 signaling at the
            Golgi apparatus with protein transport.
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Osada,S., Izawa,M., Saito,R., Mizuno,K., Suzuki,A., Hirai,S. and
            Ohno,S.
  TITLE     YSK1, a novel mammalian protein kinase structurally related to
            Ste20 and SPS1, but is not involved in the known MAPK pathways
  JOURNAL   Oncogene 14 (17), 2047-2057 (1997)
   PUBMED   9160885
REFERENCE   10 (residues 1 to 332)
  AUTHORS   Pombo,C.M., Bonventre,J.V., Molnar,A., Kyriakis,J. and Force,T.
  TITLE     Activation of a human Ste20-like kinase by oxidant stress defines a
            novel stress response pathway
  JOURNAL   EMBO J 15 (17), 4537-4546 (1996)
   PUBMED   8887545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA624380.1, AK303719.1,
            AC110299.3, CB250694.1 and HY315908.1.
            
            On Aug 29, 2013 this sequence version replaced XP_005247044.1.
            
            Summary: This gene encodes a member of the germinal centre kinase
            III (GCK III) subfamily of the sterile 20 superfamily of kinases.
            The encoded enzyme plays a role in serine-threonine liver kinase B1
            (LKB1) signaling pathway to regulate neuronal polarization and
            morphology of the Golgi apparatus. The protein is translocated from
            the Golgi apparatus to the nucleus in response to chemical anoxia
            and plays a role in regulation of cell death. A pseudogene
            associated with this gene is located on chromosome 18. Multiple
            alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (2) uses an alternate 5' exon
            structure and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG and result in an isoform (3) with a
            shorter N-terminus, compared to isoform 1. Variants 2, 6, and 7
            encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303719.1, SRR14038194.3469688.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..332
                     /product="serine/threonine-protein kinase 25 isoform 3"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 25; Ste20, yeast
                     homolog; ste20-like kinase; ste20/oxidant stress response
                     kinase 1; sterile 20/oxidant stress-response kinase 1"
                     /calculated_mol_wt=37166
     Region          <1..197
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..332
                     /gene="STK25"
                     /gene_synonym="SOK1; YSK1"
                     /coded_by="NM_001282305.1:603..1601"
                     /note="isoform 3 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63199.1"
                     /db_xref="GeneID:10494"
                     /db_xref="HGNC:HGNC:11404"
                     /db_xref="MIM:602255"
ORIGIN      
        1 meylgggsal dllkpgplee tyiatilrei lkgldylhse rkihrdikaa nvllseqgdv
       61 kladfgvagq ltdtqikrnt fvgtpfwmap evikqsaydf kadiwslgit aielakgepp
      121 nsdlhpmrvl flipknsppt legqhskpfk efveaclnkd prfrptakel lkhkfitryt
      181 kktsflteli drykrwkseg hgeessseds didgeaedge qgpiwtfppt irpsphsklh
      241 kgtalhssqk paepvkrqpr sqclstlvrp vfgelkekhk qsggsvgale elenafslae
      301 escpgisdkl mvhlvervqr fshnrnhlts tr
//
LOCUS       NP_001230728             570 aa            linear   PRI 20-NOV-2025
DEFINITION  TSC22 domain family protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001230728
VERSION     NP_001230728.1
DBSOURCE    REFSEQ: accession NM_001243799.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Kamimura,R., Uchida,D., Kanno,S.I., Shiraishi,R., Hyodo,T.,
            Sawatani,Y., Shimura,M., Hasegawa,T., Tsubura-Okubo,M., Yaguchi,E.,
            Komiyama,Y., Fukumoto,C., Izumi,S., Fujita,A., Wakui,T. and
            Kawamata,H.
  TITLE     Identification of Binding Proteins for TSC22D1 Family Proteins
            Using Mass Spectrometry
  JOURNAL   Int J Mol Sci 22 (20), 10913 (2021)
   PUBMED   34681573
  REMARK    GeneRIF: Identification of Binding Proteins for TSC22D1 Family
            Proteins Using Mass Spectrometry.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Homig-Holzel,C., van Doorn,R., Vogel,C., Germann,M., Cecchini,M.G.,
            Verdegaal,E. and Peeper,D.S.
  TITLE     Antagonistic TSC22D1 variants control BRAF(E600)-induced senescence
  JOURNAL   EMBO J 30 (9), 1753-1765 (2011)
   PUBMED   21448135
  REMARK    GeneRIF: Differential regulation of antagonistic TSC22D1 variants
            is required for the establishment of oncogene-induced cellular
            senescence.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Lu,Y., Kitaura,J., Oki,T., Komeno,Y., Ozaki,K., Kiyono,M.,
            Kumagai,H., Nakajima,H., Nosaka,T., Aburatani,H. and Kitamura,T.
  TITLE     Identification of TSC-22 as a potential tumor suppressor that is
            upregulated by Flt3-D835V but not Flt3-ITD
  JOURNAL   Leukemia 21 (11), 2246-2257 (2007)
   PUBMED   17690703
  REMARK    GeneRIF: TSC-22 is a potential tumor suppressor that is upregulated
            by Flt3-D835V but not Flt3-ITD
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Sugawara,F., Yamada,Y., Watanabe,R., Ban,N., Miyawaki,K., Kuroe,A.,
            Hamasaki,A., Ikeda,H., Kurose,T., Usami,M., Ikeda,M. and Seino,Y.
  TITLE     The role of the TSC-22 (-396) A/G variant in the development of
            diabetic nephropathy
  JOURNAL   Diabetes Res Clin Pract 60 (3), 191-197 (2003)
   PUBMED   12757981
  REMARK    GeneRIF: findings suggest that the TSC-22 gene (-396) A allele is
            associated with an increasing risk of diabetic nephropathy
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Kester,H.A., Blanchetot,C., den Hertog,J., van der Saag,P.T. and
            van der Burg,B.
  TITLE     Transforming growth factor-beta-stimulated clone-22 is a member of
            a family of leucine zipper proteins that can homo- and
            heterodimerize and has transcriptional repressor activity
  JOURNAL   J Biol Chem 274 (39), 27439-27447 (1999)
   PUBMED   10488076
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Ohta,S., Shimekake,Y. and Nagata,K.
  TITLE     Molecular cloning and characterization of a transcription factor
            for the C-type natriuretic peptide gene promoter
  JOURNAL   Eur J Biochem 242 (3), 460-466 (1996)
   PUBMED   9022669
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Jay,P., Ji,J.W., Marsollier,C., Taviaux,S., Berge-Lefranc,J.L. and
            Berta,P.
  TITLE     Cloning of the human homologue of the TGF beta-stimulated clone 22
            gene
  JOURNAL   Biochem Biophys Res Commun 222 (3), 821-826 (1996)
   PUBMED   8651929
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Shibanuma,M., Kuroki,T. and Nose,K.
  TITLE     Isolation of a gene encoding a putative leucine zipper structure
            that is induced by transforming growth factor beta 1 and other
            growth factors
  JOURNAL   J Biol Chem 267 (15), 10219-10224 (1992)
   PUBMED   1587811
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB082525.1, AK091854.1 and
            AL138960.16.
            
            Summary: This gene encodes a member of the TSC22 domain family of
            leucine zipper transcription factors. The encoded protein is
            stimulated by transforming growth factor beta, and regulates the
            transcription of multiple genes including C-type natriuretic
            peptide. The encoded protein may play a critical role in tumor
            suppression through the induction of cancer cell apoptosis, and a
            single nucleotide polymorphism in the promoter of this gene has
            been associated with diabetic nephropathy. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (5) uses an alternate splice site
            and lacks an exon in the coding region, which results in a
            frameshift, compared to variant 1. The encoded isoform (4) is
            shorter and has a distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091854.1, DB319465.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..570
                     /product="TSC22 domain family protein 1 isoform 4"
                     /note="transforming growth factor beta-stimulated protein
                     TSC-22; cerebral protein 2; regulatory protein TSC-22;
                     TGFB-stimulated clone 22 homolog; transforming growth
                     factor beta-1-induced transcript 4 protein;
                     transcriptional regulator TSC-22; TGFbeta-stimulated clone
                     22"
                     /calculated_mol_wt=58728
     Region          1..98
                     /region_name="Required for interaction with TGFBR1 and
                     promotion of TGF-beta signaling.
                     /evidence=ECO:0000269|PubMed:21791611"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          22..110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          125..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Region          220..288
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q15714.3)"
     Region          458..486
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15714.3)"
     CDS             1..570
                     /gene="TSC22D1"
                     /gene_synonym="HUCEP-2; Ptg-2; TGFB1I4; TSC22"
                     /coded_by="NM_001243799.1:492..2204"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58291.1"
                     /db_xref="GeneID:8848"
                     /db_xref="HGNC:HGNC:16826"
                     /db_xref="MIM:607715"
ORIGIN      
        1 mhqppestaa aaaaadisar kmahpamfpr rgsgsgsasa lnaagtgvgs natssedfpp
       61 psllqppppa asstsgpqpp ppqslnllsq aqlqaqplap ggtqmkkksg fqitsvtpaq
      121 isasissnns iaedtesydd ldeshtedls sseildvsls ratdlgeper ssseetlnnf
      181 qeaetpgavs pnqphlpqph lphlpqqnvv ingnahphhl hhhhqihhgh hlqhghhhps
      241 hvavasasit ggppsspvsr klsttgssds itpvaptsav sssgspasvm tnmrapsttg
      301 giginsvtgt stvnnvnita vgsfnpnvts smlgnvnist snipsaagvs vgpgvtsgvn
      361 vnilsgmgng tisssaavss vpnaaagmtg gsvssqqqqp tvntsrfrvv kldsssepfk
      421 kgrwtctefy ekenavpate gvlinkvvet vkqnpievts erestsgssv sssvstlshy
      481 tesvgsgemg aptvvvqqqq qqqqqqqqqp alqgvtlqqm dfgstgpqsi pavsipqsis
      541 qsqisqvqlq sqelsyltmk vvllivylcm
//
LOCUS       NP_612367                260 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial import inner membrane translocase subunit Tim29 [Homo
            sapiens].
ACCESSION   NP_612367
VERSION     NP_612367.1
DBSOURCE    REFSEQ: accession NM_138358.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Guo,L., Liu,J.J., Long,S.Y., Wang,P.Y., Li,S., Wang,J.L., Wei,X.F.,
            Li,J., Lei,L., Huang,A.L. and Hu,J.L.
  TITLE     TIM22 and TIM29 inhibit HBV replication by up-regulating SRSF1
            expression
  JOURNAL   J Med Virol 96 (2), e29439 (2024)
   PUBMED   38294104
  REMARK    GeneRIF: TIM22 and TIM29 inhibit HBV replication by up-regulating
            SRSF1 expression.
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Valpadashi,A., Callegari,S., Linden,A., Neumann,P., Ficner,R.,
            Urlaub,H., Deckers,M. and Rehling,P.
  TITLE     Defining the architecture of the human TIM22 complex by chemical
            crosslinking
  JOURNAL   FEBS Lett 595 (2), 157-168 (2021)
   PUBMED   33125709
  REMARK    GeneRIF: Defining the architecture of the human TIM22 complex by
            chemical crosslinking.
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Kang,Y., Stroud,D.A., Baker,M.J., De Souza,D.P., Frazier,A.E.,
            Liem,M., Tull,D., Mathivanan,S., McConville,M.J., Thorburn,D.R.,
            Ryan,M.T. and Stojanovski,D.
  TITLE     Sengers Syndrome-Associated Mitochondrial Acylglycerol Kinase Is a
            Subunit of the Human TIM22 Protein Import Complex
  JOURNAL   Mol Cell 67 (3), 457-470 (2017)
   PUBMED   28712726
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Vukotic,M., Nolte,H., Konig,T., Saita,S., Ananjew,M., Kruger,M.,
            Tatsuta,T. and Langer,T.
  TITLE     Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the
            TIM22 Protein Translocase in Mitochondria
  JOURNAL   Mol Cell 67 (3), 471-483 (2017)
   PUBMED   28712724
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Callegari,S., Richter,F., Chojnacka,K., Jans,D.C., Lorenzi,I.,
            Pacheu-Grau,D., Jakobs,S., Lenz,C., Urlaub,H., Dudek,J.,
            Chacinska,A. and Rehling,P.
  TITLE     TIM29 is a subunit of the human carrier translocase required for
            protein transport
  JOURNAL   FEBS Lett 590 (23), 4147-4158 (2016)
   PUBMED   27718247
  REMARK    GeneRIF: TIM29 is required for the structural integrity of the
            TIM22 complex and for import of substrate proteins by the carrier
            translocase
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Kang,Y., Baker,M.J., Liem,M., Louber,J., McKenzie,M., Atukorala,I.,
            Ang,C.S., Keerthikumar,S., Mathivanan,S. and Stojanovski,D.
  TITLE     Tim29 is a novel subunit of the human TIM22 translocase and is
            involved in complex assembly and stability
  JOURNAL   Elife 5, e17463 (2016)
   PUBMED   27554484
  REMARK    GeneRIF: Here, the authors identify Tim29 (C19orf52) as a novel,
            metazoan-specific subunit of the human TIM22 complex. The protein
            is integrated into the mitochondrial inner membrane with it's
            C-terminus exposed to the intermembrane space.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC011442.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007244.1, SRR3476690.518010.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000270502.7/
                                                  ENSP00000270502.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..260
                     /product="mitochondrial import inner membrane translocase
                     subunit Tim29"
                     /note="uncharacterized protein C19orf52"
                     /calculated_mol_wt=25811
     transit_peptide 1..31
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q9BSF4.2)"
                     /calculated_mol_wt=3440
     Region          24..186
                     /region_name="Tim29"
                     /note="Translocase of the Inner Mitochondrial membrane 29;
                     pfam10171"
                     /db_xref="CDD:462977"
     mat_peptide     32..260
                     /product="Mitochondrial import inner membrane translocase
                     subunit Tim29. /id=PRO_0000271006"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSF4.2)"
                     /calculated_mol_wt=25811
     Site            60..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSF4.2)"
     CDS             1..260
                     /gene="TIMM29"
                     /gene_synonym="C19orf52; TIM29"
                     /coded_by="NM_138358.4:13..795"
                     /db_xref="CCDS:CCDS12252.1"
                     /db_xref="GeneID:90580"
                     /db_xref="HGNC:HGNC:25152"
                     /db_xref="MIM:617380"
ORIGIN      
        1 maaaalrrfw srrraeagda vvakpgvwar lgswarallr dyaeacrdas aeararpgra
       61 avyvgllgga aacftlapse gafeeallea sgtllllapa trnreseafv qrllwlrgrg
      121 rlryvnlglc slvyeapfda qaslyqarcr ylqprwtdfp grvldvgfvg rwwvlgawmr
      181 dcdinddefl hlpahlrvvg pqqlhsetne rlfdekykpv vltddqvdqa lweeqvlqke
      241 kkdrlalsqa hslvqaeapr
//
LOCUS       NP_001340232             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 3 [Homo sapiens].
ACCESSION   NP_001340232
VERSION     NP_001340232.1
DBSOURCE    REFSEQ: accession NM_001353303.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.30479.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 3"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36689
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353303.1:225..1199"
                     /note="isoform 3 is encoded by transcript variant 65"
                     /db_xref="CCDS:CCDS94340.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnlikvltr didhnaahff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001308142             801 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 18 isoform 1 [Homo sapiens].
ACCESSION   NP_001308142 XP_005249910
VERSION     NP_001308142.1
DBSOURCE    REFSEQ: accession NM_001321213.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 801)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   2  (residues 1 to 801)
  AUTHORS   Ding,X., Barodia,S.K., Ma,L. and Goldberg,M.S.
  TITLE     Fbxl18 targets LRRK2 for proteasomal degradation and attenuates
            cell toxicity
  JOURNAL   Neurobiol Dis 98, 122-136 (2017)
   PUBMED   27890708
  REMARK    GeneRIF: Study showed that LRRK2 phosphorylation is required for
            LRRK2 to bind to Fbxl18, and that this interaction is important for
            regulating the amount of LRRK2 via ubiquitination of LRRK2 by the
            SCFFbxl18 ubiquitin ligase and subsequent proteasomal degradation
            of LRRK2. We also show that LRRK2 can induce caspase 8 mediated
            cell death and that the degradation of LRRK2 mediated by Fbxl18 can
            prevent LRRK2-mediated toxicity.
REFERENCE   3  (residues 1 to 801)
  AUTHORS   Zhang,J., Yang,Z., Ou,J., Xia,X., Zhi,F. and Cui,J.
  TITLE     The F-box protein FBXL18 promotes glioma progression by promoting
            K63-linked ubiquitination of Akt
  JOURNAL   FEBS Lett 591 (1), 145-154 (2017)
   PUBMED   27926990
  REMARK    GeneRIF: FBXL18 plays an oncogenic role through promoting lysine
            63-linked ubiquitination of Akt in glioma.
REFERENCE   4  (residues 1 to 801)
  AUTHORS   Liu,Y., Lear,T., Zhao,Y., Zhao,J., Zou,C., Chen,B.B. and
            Mallampalli,R.K.
  TITLE     F-box protein Fbxl18 mediates polyubiquitylation and proteasomal
            degradation of the pro-apoptotic SCF subunit Fbxl7
  JOURNAL   Cell Death Dis 6 (2), e1630 (2015)
   PUBMED   25654763
  REMARK    GeneRIF: Fbxl18 regulates apoptosis by mediating
            ubiquitin-dependent proteasomal degradation of the pro-apoptotic
            protein Fbxl7 that may impact cellular processes involved in cell
            cycle progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 801)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 801)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006483.3 and AC092171.4.
            
            On Mar 18, 2016 this sequence version replaced XP_005249910.1.
            
            Summary: The protein encoded by this gene is a member of a family
            of proteins that contain an approximately 40-amino acid F-box
            motif. This motif is important for interaction with SKP1 and for
            targeting some proteins for degradation. The encoded protein has
            been shown to control the cellular level of FBXL7, a protein that
            induces mitotic arrest, by targeting it for polyubiquitylation and
            proteasomal degradation. Members of the F-box protein family, such
            as FBXL18, are characterized by an approximately 40-amino acid
            F-box motif. F-box proteins interact with SKP1 through the F box,
            and they interact with ubiquitination targets through other protein
            interaction domains. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294949.1, SRR1803617.198293.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..801
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..801
                     /product="F-box/LRR-repeat protein 18 isoform 1"
                     /note="F-box/LRR-repeat protein 18"
                     /calculated_mol_wt=87536
     Region          28..71
                     /region_name="F-box_FBXL18"
                     /note="F-box domain found in F-box/LRR-repeat protein 18
                     (FBXL18) and similar proteins; cd22128"
                     /db_xref="CDD:438900"
     Site            order(31,35,38..39,42..43,47,49..50,55..57,59)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438900"
     Region          85..678
                     /region_name="FBXL18_LRR"
                     /note="F-box/LRR-repeat protein 18, LRR; pfam19729"
                     /db_xref="CDD:466163"
     Region          345..384
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          385..414
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          415..484
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          451..476
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          485..532
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          533..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          560..589
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          590..615
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          616..640
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..801
                     /gene="FBXL18"
                     /gene_synonym="Fbl18"
                     /coded_by="NM_001321213.2:136..2541"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:80028"
                     /db_xref="HGNC:HGNC:21874"
                     /db_xref="MIM:609084"
ORIGIN      
        1 massgedisn ddddmhpaaa gmadgvhllg fsdeillhil shvpstdlil nvrrtcrkla
       61 alcldkslih tvllqkdyqa sedkvrqlvk eigreiqqls magcywlpgs tvehvarcrs
      121 lvkvnlsgch ltslrlskml salqhlrsla idvspgfdas qlsseckatl srvrelkqtl
      181 ftpsygvvpc ctslekllly feildrtreg ailsgqlmvg qsnvphyqnl rvfyarlapg
      241 yinqevvrly lavlsdrtpq nlhaflisvp gsfaesgatk nlldsmarnv vldalqlpks
      301 wlngssllqh mkfnnpfyfs fsrctlsggh liqqvinggk dlrslaslnl sgcvhclspd
      361 sllrkaeddi dssiletlva sccnlrhlnl saahhhsseg lgrhlcqlla rlrhlrslsl
      421 pvcsvadsap radrapaqpa mhavprgfgk kvrvgvqscp spfsgqacpq pssvfwsllk
      481 nlpflehlel igsnfssamp rnepairnsl ppcsraqsvg dsevaaigql aflrhltlaq
      541 lpsvltgsgl vniglqcqql rslslanlgm mgkvvympal sdmlkhckrl rdlrleqpyf
      601 sanaqffqal sqcpslqrlc lvsrsgtlqp davlafmarc lqvvmchlft geslatcksl
      661 qqsllrrwge vtgrrpqlft elreepsart sratgrrqpc lpdsgvvccp cgrplavsgi
      721 ilvgvspslv vkttcvyrvl fknldyasif flvclfetes hsvvqagvqw rdlsslqpll
      781 sglqpqppeq lglqvcttip g
//
LOCUS       NP_001257943            1329 aa            linear   PRI 20-NOV-2025
DEFINITION  kinectin isoform d [Homo sapiens].
ACCESSION   NP_001257943
VERSION     NP_001257943.1
DBSOURCE    REFSEQ: accession NM_001271014.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1329)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1329)
  AUTHORS   Niu,X., Shen,Y., Wen,Y., Mi,X., Xie,J., Zhang,Y. and Ding,Z.
  TITLE     KTN1 mediated unfolded protein response protects keratinocytes from
            ionizing radiation-induced DNA damage
  JOURNAL   J Dermatol Sci 114 (1), 24-33 (2024)
   PUBMED   38448340
  REMARK    GeneRIF: KTN1 mediated unfolded protein response protects
            keratinocytes from ionizing radiation-induced DNA damage.
REFERENCE   3  (residues 1 to 1329)
  AUTHORS   Moore,A., Crea,P.W., Makarious,M., Bandres-Ciga,S., Blauwendraat,C.
            and Diez-Fairen,M.
  TITLE     A genetic and transcriptomic assessment of the KTN1 gene in
            Parkinson's disease risk
  JOURNAL   Neurobiol Aging 134, 66-73 (2024)
   PUBMED   37992546
  REMARK    GeneRIF: A genetic and transcriptomic assessment of the KTN1 gene
            in Parkinson's disease risk.
REFERENCE   4  (residues 1 to 1329)
  AUTHORS   Alberts,A.S., Bouquin,N., Johnston,L.H. and Treisman,R.
  TITLE     Analysis of RhoA-binding proteins reveals an interaction domain
            conserved in heterotrimeric G protein beta subunits and the yeast
            response regulator protein Skn7
  JOURNAL   J Biol Chem 273 (15), 8616-8622 (1998)
   PUBMED   9535835
REFERENCE   5  (residues 1 to 1329)
  AUTHORS   Rao,P.N., Yu,H., Hodge,R., Pettenati,M.J. and Sheetz,M.P.
  TITLE     Assignment of the human kinectin gene (KTN1), encoding a
            kinesin-binding protein, to chromosome 14 band q22.1 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 196-197 (1997)
   PUBMED   9605849
REFERENCE   6  (residues 1 to 1329)
  AUTHORS   Hotta,K., Tanaka,K., Mino,A., Kohno,H. and Takai,Y.
  TITLE     Interaction of the Rho family small G proteins with kinectin, an
            anchoring protein of kinesin motor
  JOURNAL   Biochem Biophys Res Commun 225 (1), 69-74 (1996)
   PUBMED   8769096
REFERENCE   7  (residues 1 to 1329)
  AUTHORS   Print,C.G., Morris,C.M., Spurr,N.K., Rooke,L. and Krissansen,G.W.
  TITLE     The CG-1 gene, a member of the kinectin and ES/130 family, maps to
            human chromosome band 14q22
  JOURNAL   Immunogenetics 43 (4), 227-229 (1996)
   PUBMED   8575822
REFERENCE   8  (residues 1 to 1329)
  AUTHORS   Yu,H., Nicchitta,C.V., Kumar,J., Becker,M., Toyoshima,I. and
            Sheetz,M.P.
  TITLE     Characterization of kinectin, a kinesin-binding protein: primary
            sequence and N-terminal topogenic signal analysis
  JOURNAL   Mol Biol Cell 6 (2), 171-183 (1995)
   PUBMED   7787244
REFERENCE   9  (residues 1 to 1329)
  AUTHORS   Futterer,A., Kruppa,G., Kramer,B., Lemke,H. and Kronke,M.
  TITLE     Molecular cloning and characterization of human kinectin
  JOURNAL   Mol Biol Cell 6 (2), 161-170 (1995)
   PUBMED   7787243
REFERENCE   10 (residues 1 to 1329)
  AUTHORS   Print,C.G., Leung,E., Harrison,J.E., Watson,J.D. and
            Krissansen,G.W.
  TITLE     Cloning of a gene encoding a human leukocyte protein characterised
            by extensive heptad repeats
  JOURNAL   Gene 144 (2), 221-228 (1994)
   PUBMED   8039706
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA769269.1, AK302797.1,
            BC143720.1 and BM981127.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the kinectin protein family. The encoded protein is
            primarily localized to the endoplasmic reticulum membrane. This
            protein binds kinesin and may be involved in intracellular
            organelle motility. This protein also binds translation elongation
            factor-delta and may be involved in the assembly of the elongation
            factor-1 complex. Alternate splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, Aug 2012].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            lacks an alternate in-frame exon in the coding region compared to
            variant 2. This variant encodes isoform d, which is shorter than
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.117528.1, AK302797.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..1329
                     /product="kinectin isoform d"
                     /note="CG-1 antigen; kinesin receptor"
                     /calculated_mol_wt=152857
     Region          29..160
                     /region_name="Rib_recp_KP_reg"
                     /note="Ribosome receptor lysine/proline rich region;
                     pfam05104"
                     /db_xref="CDD:461548"
     Region          316..>532
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     Region          448..1269
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..1329
                     /gene="KTN1"
                     /gene_synonym="CG1; KNT; MU-RMS-40.19"
                     /coded_by="NM_001271014.2:303..4292"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="GeneID:3895"
                     /db_xref="HGNC:HGNC:6467"
                     /db_xref="MIM:600381"
ORIGIN      
        1 mefyesayfi vlipsivitv iflffwlfmk etlydevlak qkreqklipt ktdkkkaekk
       61 knkkkeiqng nlhesdsesv prdfklsdal aveddqvapv plnvvetsss vrerkkkekk
      121 qkpvleeqvi kesdaskipg kkvepvpvtk qptppseaaa skkkpgqkks kngsddqdkk
      181 vetlmvpskr qealplhqet kqesgsgkkk asskkqkten vfvdepliha ttyiplmdna
      241 dsspvvdkre vidllkpdqv egiqksgtkk lktetdkena evkfkdflls lktmmfsede
      301 alcvvdllke ksgviqdalk ksskgelttl ihqlqekdkl laavkedaaa tkdrckqltq
      361 emmtekersn vvitrmkdri gtlekehnvf qnkihvsyqe tqqmqmkfqq vreqmeaeia
      421 hlkqengilr davsnttnql eskqsaelnk lrqdyarlvn eltektgklq qeevqkknae
      481 qaatqlkvql qeaerrweev qsyirkrtae heaaqqdlqs kfvakenevq slhskltdtl
      541 vskqqleqrl mqlmeseqkr vnkeeslqmq vqdileqnea lkaqiqqfhs qiaaqtsasv
      601 laeelhkvia ekdkqikqte dslaserdrl tskeeelkdi qnmnfllkae vqklqalane
      661 qaaaahelek mqqsvyvkdd kirlleeqlq heisnkmeef kilndqnkal ksevqklqtl
      721 vseqpnkdvv eqmekciqek deklktveel letgliqvat keeelnairt enssltkevq
      781 dlkakqndqv sfaslveelk kvihekdgki ksveelleae llkvankekt vqdlkqeika
      841 lkeeignvql ekaqqlsits kvqelqnllk gkeeqmntmk avleekekdl antgkwlqdl
      901 qeeneslkah vqevaqhnlk eassasqfee leivlkeken elkrleamlk eresdlsskt
      961 qllqdvqden klfksqieql kqqnyqqass fppheellkv iserekeisg lwneldslkd
     1021 avehqrkknn dlreknweam ealastekml qdkvnktske rqqqveavel eakevlkklf
     1081 pkvsvpsnls ygewlhgfek kakecmagts gseevkvleh klkeademht llqlecekyk
     1141 svlaetegil qklqrsveqe enkwkvkvde shktikqmqs sftsseqele rlrsenkdie
     1201 nlrrerehle melekaemer styvtevrel kaqlnetltk lrteqnerqk vagdlhkaqq
     1261 sleliqskiv kaagdttvie nsdvspetes seketmsvsl nqtvtqlqql lqavnqqltk
     1321 ekehyqvle
//
LOCUS       NP_001035843             475 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform d [Homo sapiens].
ACCESSION   NP_001035843
VERSION     NP_001035843.1
DBSOURCE    REFSEQ: accession NM_001042384.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 475)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, BX499930.1,
            AK023738.1, CX751767.1, AC139764.5 and BG182631.1.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023738.1, SRR1803617.610.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..475
                     /product="centrosomal protein of 63 kDa isoform d"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=55460
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          139..>441
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..475
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001042384.2:355..1782"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS43152.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveais lesvsatckq lsqelmekye elkrmeahnn eykaeikklk eqilqgeqsy
      361 ssalegmkme ishltqelhq rditiastkg sssdmekrlr aemqkaedka vehkeildql
      421 eslklenrhl semvmklelg lherwgftml sslvlnfgiq airqpqrpkv lelqv
//
LOCUS       NP_003814                300 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 6B precursor
            [Homo sapiens].
ACCESSION   NP_003814
VERSION     NP_003814.1
DBSOURCE    REFSEQ: accession NM_003823.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Guan,J., Huang,X., Zhou,Z., Li,S., Wang,F., Han,Y. and Yin,N.
  TITLE     HIF-1alpha regulates DcR3 to promote the development of
            endometriosis
  JOURNAL   Eur J Obstet Gynecol Reprod Biol 296, 185-193 (2024)
   PUBMED   38458034
  REMARK    GeneRIF: HIF-1alpha regulates DcR3 to promote the development of
            endometriosis.
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Yang,L.Y., Lou,X.L., Wang,Y. and Hou,Y.Q.
  TITLE     [miR-148b inhibits M2 polarization of LPS-stimulated macrophages by
            targeting DcR3]
  JOURNAL   Zhonghua Yu Fang Yi Xue Za Zhi 57 (8), 1231-1237 (2023)
   PUBMED   37574317
  REMARK    GeneRIF: [miR-148b inhibits M2 polarization of LPS-stimulated
            macrophages by targeting DcR3].
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Ware,C.F., Croft,M. and Neil,G.A.
  TITLE     Realigning the LIGHT signaling network to control dysregulated
            inflammation
  JOURNAL   J Exp Med 219 (7) (2022)
   PUBMED   35604387
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Wu,N.L., Huang,D.Y., Hsieh,S.L., Dai,Y.S. and Lin,W.W.
  TITLE     Decoy receptor 3 is involved in epidermal keratinocyte commitment
            to terminal differentiation via EGFR and PKC activation
  JOURNAL   Exp Mol Med 54 (4), 542-551 (2022)
   PUBMED   35478210
  REMARK    GeneRIF: Decoy receptor 3 is involved in epidermal keratinocyte
            commitment to terminal differentiation via EGFR and PKC activation.
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Soliman,M.H. and Ebaid,A.M.
  TITLE     Association of Tumor Necrosis Like factor 1 A (TL1A) and its Decoy
            Receptor (DcR3) with The Disease Activity and Autoantibody
            Production in Rheumatoid Arthritis Patients
  JOURNAL   Egypt J Immunol 26 (1), 43-54 (2019)
   PUBMED   31332995
  REMARK    GeneRIF: significantly higher levels of TL1A and its decoy receptor
            DcR3 in RA patients than in controls; TL1A is significantly related
            to the disease activity and enhances IL-17 production
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Hsu,T.L., Chang,Y.C., Chen,S.J., Liu,Y.J., Chiu,A.W., Chio,C.C.,
            Chen,L. and Hsieh,S.L.
  TITLE     Modulation of dendritic cell differentiation and maturation by
            decoy receptor 3
  JOURNAL   J Immunol 168 (10), 4846-4853 (2002)
   PUBMED   11994433
  REMARK    GeneRIF: As a soluble receptor.Fc fusion protein, DcR3 modulates
            dendritic cell differentiation and maturation from CD14+ monocytes
            by up-regulation of CD86/B7.2 and down-regulation of CD40,
            CD54/ICAM-1, CD80/B7.1, CD1a, and HLA-DR.
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Migone,T.S., Zhang,J., Luo,X., Zhuang,L., Chen,C., Hu,B.,
            Hong,J.S., Perry,J.W., Chen,S.F., Zhou,J.X., Cho,Y.H., Ullrich,S.,
            Kanakaraj,P., Carrell,J., Boyd,E., Olsen,H.S., Hu,G., Pukac,L.,
            Liu,D., Ni,J., Kim,S., Gentz,R., Feng,P., Moore,P.A., Ruben,S.M.
            and Wei,P.
  TITLE     TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T
            cell costimulator
  JOURNAL   Immunity 16 (3), 479-492 (2002)
   PUBMED   11911831
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Bai,C., Connolly,B., Metzker,M.L., Hilliard,C.A., Liu,X.,
            Sandig,V., Soderman,A., Galloway,S.M., Liu,Q., Austin,C.P. and
            Caskey,C.T.
  TITLE     Overexpression of M68/DcR3 in human gastrointestinal tract tumors
            independent of gene amplification and its location in a four-gene
            cluster
  JOURNAL   Proc Natl Acad Sci U S A 97 (3), 1230-1235 (2000)
   PUBMED   10655513
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Yu,K.Y., Kwon,B., Ni,J., Zhai,Y., Ebner,R. and Kwon,B.S.
  TITLE     A newly identified member of tumor necrosis factor receptor
            superfamily (TR6) suppresses LIGHT-mediated apoptosis
  JOURNAL   J Biol Chem 274 (20), 13733-13736 (1999)
   PUBMED   10318773
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Pitti,R.M., Marsters,S.A., Lawrence,D.A., Roy,M., Kischkel,F.C.,
            Dowd,P., Huang,A., Donahue,C.J., Sherwood,S.W., Baldwin,D.T.,
            Godowski,P.J., Wood,W.I., Gurney,A.L., Hillan,K.J., Cohen,R.L.,
            Goddard,A.D., Botstein,D. and Ashkenazi,A.
  TITLE     Genomic amplification of a decoy receptor for Fas ligand in lung
            and colon cancer
  JOURNAL   Nature 396 (6712), 699-703 (1998)
   PUBMED   9872321
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM759033.1, BC034349.1 and
            AW204999.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the tumor necrosis factor receptor
            superfamily. The encoded protein is postulated to play a regulatory
            role in suppressing FasL- and LIGHT-mediated cell death. It acts as
            a decoy receptor that competes with death receptors for ligand
            binding. Over-expression of this gene has been noted in
            gastrointestinal tract tumors. Read-through transcription into this
            gene from the neighboring upstream gene, which encodes regulator of
            telomere elongation helicase 1 (RTEL1), generates a non-coding
            transcript. [provided by RefSeq, Feb 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.398972.1, AF104419.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369996.3/ ENSP00000359013.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..300
                     /product="tumor necrosis factor receptor superfamily
                     member 6B precursor"
                     /EC_number="3.6.4.12"
                     /note="decoy receptor for Fas ligand; tumor necrosis
                     factor receptor superfamily, member 6b, decoy; tumor
                     necrosis factor receptor superfamily member 6b"
                     /calculated_mol_wt=29757
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2941
     mat_peptide     30..300
                     /product="Tumor necrosis factor receptor superfamily
                     member 6B. /id=PRO_0000034570"
                     /note="propagated from UniProtKB/Swiss-Prot (O95407.1)"
                     /calculated_mol_wt=29757
     Region          31..70
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O95407.1)"
     Region          34..196
                     /region_name="TNFRSF6B"
                     /note="Tumor necrosis factor receptor superfamily member
                     6B (TNFRSF6B), also known as decoy receptor 3 (DcR3);
                     cd10575"
                     /db_xref="CDD:276901"
     Region          34..70
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276901"
     Region          72..113
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O95407.1)"
     Region          73..113
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276901"
     Site            order(78..81,83..85,89)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276901"
     Region          115..153
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276901"
     Region          115..150
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O95407.1)"
     Region          152..193
                     /region_name="TNFR-Cys 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O95407.1)"
     Site            173
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95407.1)"
     CDS             1..300
                     /gene="TNFRSF6B"
                     /gene_synonym="DCR3; DJ583P15.1.1; M68; M68E; TR6"
                     /coded_by="NM_003823.4:117..1019"
                     /db_xref="CCDS:CCDS13532.1"
                     /db_xref="GeneID:8771"
                     /db_xref="HGNC:HGNC:11921"
                     /db_xref="MIM:603361"
ORIGIN      
        1 mralegpgls llclvlalpa llpvpavrgv aetptypwrd aetgerlvca qcppgtfvqr
       61 pcrrdspttc gpcpprhytq fwnylercry cnvlcgeree earachathn racrcrtgff
      121 ahagfcleha scppgagvia pgtpsqntqc qpcppgtfsa ssssseqcqp hrnctalgla
      181 lnvpgssshd tlctsctgfp lstrvpgaee ceravidfva fqdisikrlq rllqaleape
      241 gwgptpragr aalqlklrrr ltellgaqdg allvrllqal rvarmpgler svrerflpvh
//
LOCUS       NP_001337611             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337611
VERSION     NP_001337611.1
DBSOURCE    REFSEQ: accession NM_001350682.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (18), as well as variants 1-4,
            9-17, and 19-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.250124.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350682.1:907..3117"
                     /note="isoform 1 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001357336             144 aa            linear   PRI 20-NOV-2025
DEFINITION  protein BUD31 homolog [Homo sapiens].
ACCESSION   NP_001357336 XP_005250731
VERSION     NP_001357336.1
DBSOURCE    REFSEQ: accession NM_001370407.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wu,X., Fan,R., Zhang,Y., Duan,C., Yao,X., Liu,K., Lin,D. and
            Chen,Z.
  TITLE     The role of BUD31 in clear cell renal cell carcinoma: prognostic
            significance, alternative splicing, and tumor immune environment
  JOURNAL   Clin Exp Med 24 (1), 191 (2024)
   PUBMED   39136845
  REMARK    GeneRIF: The role of BUD31 in clear cell renal cell carcinoma:
            prognostic significance, alternative splicing, and tumor immune
            environment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Choudhry,M., Gamallat,Y., Khosh Kish,E., Seyedi,S., Gotto,G.,
            Ghosh,S. and Bismar,T.A.
  TITLE     Downregulation of BUD31 Promotes Prostate Cancer Cell Proliferation
            and Migration via Activation of p-AKT and Vimentin In Vitro
  JOURNAL   Int J Mol Sci 24 (7), 6055 (2023)
   PUBMED   37047027
  REMARK    GeneRIF: Downregulation of BUD31 Promotes Prostate Cancer Cell
            Proliferation and Migration via Activation of p-AKT and Vimentin In
            Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Xu,W., Huang,H., Yu,L. and Cao,L.
  TITLE     Meta-analysis of gene expression profiles indicates genes in
            spliceosome pathway are up-regulated in hepatocellular carcinoma
            (HCC)
  JOURNAL   Med Oncol 32 (4), 96 (2015)
   PUBMED   25731616
  REMARK    GeneRIF: High BUD31 expression is associated with hepatocellular
            carcinoma.
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Hsu,C.L., Liu,J.S., Wu,P.L., Guan,H.H., Chen,Y.L., Lin,A.C.,
            Ting,H.J., Pang,S.T., Yeh,S.D., Ma,W.L., Chen,C.J., Wu,W.G. and
            Chang,C.
  TITLE     Identification of a new androgen receptor (AR) co-regulator BUD31
            and related peptides to suppress wild-type and mutated AR-mediated
            prostate cancer growth via peptide screening and X-ray structure
            analysis
  JOURNAL   Mol Oncol 8 (8), 1575-1587 (2014)
   PUBMED   25091737
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Hla,T., Jackson,A.Q., Appleby,S.B. and Maciag,T.
  TITLE     Characterization of edg-2, a human homologue of the Xenopus
            maternal transcript G10 from endothelial cells
  JOURNAL   Biochim Biophys Acta 1260 (2), 227-229 (1995)
   PUBMED   7841202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004922.2.
            
            On May 7, 2019 this sequence version replaced XP_005250731.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG707548.1, SRR1163658.293270.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..144
                     /product="protein BUD31 homolog"
                     /note="maternal G10 transcript; functional
                     spliceosome-associated protein 17; protein EDG-2; protein
                     G10 homolog; G10 maternal transcript homolog; BUD31
                     homolog"
                     /calculated_mol_wt=16869
     Region          1..143
                     /region_name="G10"
                     /note="G10 protein; pfam01125"
                     /db_xref="CDD:426066"
     Region          2..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Region          59..67
                     /region_name="Interaction with AR.
                     /evidence=ECO:0000269|PubMed:28076346"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41223.2)"
     CDS             1..144
                     /gene="BUD31"
                     /gene_synonym="Cwc14; EDG-2; EDG2; fSAP17; G10; YCR063W"
                     /coded_by="NM_001370407.1:202..636"
                     /db_xref="CCDS:CCDS5663.1"
                     /db_xref="GeneID:8896"
                     /db_xref="HGNC:HGNC:29629"
                     /db_xref="MIM:603477"
ORIGIN      
        1 mpkvkrsrka ppdgweliep tldeldqkmr eaetephegk rkveslwpif rihhqktryi
       61 fdlfykrkai srelyeycik egyadknlia kwkkqgyenl cclrciqtrd tnfgtncicr
      121 vpksklevgr iiecthcgcr gcsg
//
LOCUS       NP_001332811             216 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 16 [Homo sapiens].
ACCESSION   NP_001332811 XP_005248226
VERSION     NP_001332811.1
DBSOURCE    REFSEQ: accession NM_001345882.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pu,C., Tong,Y., Liu,Y., Lan,S., Wang,S., Yan,G., Zhang,H., Luo,D.,
            Ma,X., Yu,S., Huang,Q., Deng,R. and Li,R.
  TITLE     Selective degradation of PARP2 by PROTACs via recruiting DCAF16 for
            triple-negative breast cancer
  JOURNAL   Eur J Med Chem 236, 114321 (2022)
   PUBMED   35430559
  REMARK    GeneRIF: Selective degradation of PARP2 by PROTACs via recruiting
            DCAF16 for triple-negative breast cancer.
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Zhang,Y., Yu,H., Zhang,J., Gao,H., Wang,S., Li,S., Wei,P.,
            Liang,J., Yu,G., Wang,X., Li,X., Li,D. and Yang,W.
  TITLE     Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate
            dehydrogenase promotes colorectal cancer metastasis via increased
            S-adenosylmethionine
  JOURNAL   J Clin Invest 131 (21) (2021)
   PUBMED   34720086
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Zhang,X., Thielert,M., Li,H. and Cravatt,B.F.
  TITLE     SPIN4 Is a Principal Endogenous Substrate of the E3 Ubiquitin
            Ligase DCAF16
  JOURNAL   Biochemistry 60 (9), 637-642 (2021)
   PUBMED   33636084
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zhang,X., Crowley,V.M., Wucherpfennig,T.G., Dix,M.M. and
            Cravatt,B.F.
  TITLE     Electrophilic PROTACs that degrade nuclear proteins by engaging
            DCAF16
  JOURNAL   Nat Chem Biol 15 (7), 737-746 (2019)
   PUBMED   31209349
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005768.17.
            
            On Sep 14, 2016 this sequence version replaced XP_005248226.1.
            
            Transcript Variant: This variant (4) plus variants 1-3 and 5-6 all
            encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.17207.1,
                                           DRR138518.620868.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267760 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31"
     Protein         1..216
                     /product="DDB1- and CUL4-associated factor 16"
                     /calculated_mol_wt=24062
     Region          1..216
                     /region_name="DCA16"
                     /note="DDB1- and CUL4-associated factor 16; pfam15349"
                     /db_xref="CDD:434656"
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXF7.1)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NXF7.1)"
     CDS             1..216
                     /gene="DCAF16"
                     /gene_synonym="C4orf30"
                     /coded_by="NM_001345882.2:1046..1696"
                     /db_xref="CCDS:CCDS3423.1"
                     /db_xref="GeneID:54876"
                     /db_xref="HGNC:HGNC:25987"
                     /db_xref="MIM:620524"
ORIGIN      
        1 mgprnpspdh lseseseeee nisylnessg eewdsseeed smvpnlsple slawqvkcll
       61 kysttwkpln pnswlyhakl ldpstpvhil reiglrlshc shcvpklepi pewpplascg
      121 vppfqkplts psrlsrdhat lngalqfatk qlsrtlsrat pipeylkqip nscvsgcccg
      181 wltktvkett rtepinttys ytdfqkavnk lltasl
//
LOCUS       NP_872294                370 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin carboxyl-terminal hydrolase 12 [Homo sapiens].
ACCESSION   NP_872294
VERSION     NP_872294.2
DBSOURCE    REFSEQ: accession NM_182488.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Jiang,L., Qi,X., Lai,M., Zhou,J., Yuan,M., You,J., Liu,Q., Pan,J.,
            Zhao,L., Ying,M., Ji,J., Li,K., Zhang,Y., Pan,W., He,Q., Yang,B.
            and Cao,J.
  TITLE     WDR20 prevents hepatocellular carcinoma senescence by orchestrating
            the simultaneous USP12/46-mediated deubiquitination of c-Myc
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2407904121 (2024)
   PUBMED   39432777
  REMARK    GeneRIF: WDR20 prevents hepatocellular carcinoma senescence by
            orchestrating the simultaneous USP12/46-mediated deubiquitination
            of c-Myc.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Liu,X., Wang,B., Chang,M., Zhang,X., Zou,H., Zhang,Z. and Han,G.
  TITLE     USP12 regulates ER stress-associated osteogenesis in human
            periodontal ligament cells under tension stress
  JOURNAL   Cell Signal 114, 111015 (2024)
   PUBMED   38113977
  REMARK    GeneRIF: USP12 regulates ER stress-associated osteogenesis in human
            periodontal ligament cells under tension stress.
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Chen,C., Xue,N., Liu,K., He,Q., Wang,C., Guo,Y., Tian,J., Liu,X.,
            Pan,Y. and Chen,G.
  TITLE     USP12 promotes nonsmall cell lung cancer progression through
            deubiquitinating and stabilizing RRM2
  JOURNAL   Mol Carcinog 62 (10), 1518-1530 (2023)
   PUBMED   37341611
  REMARK    GeneRIF: USP12 promotes nonsmall cell lung cancer progression
            through deubiquitinating and stabilizing RRM2.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Zhan,X., He,Q., Sheng,J., Jiang,X., Lin,L., Huang,Y., He,S.,
            Chen,Y., Li,L., Zeng,Z., Hu,S., Wang,P. and Zhang,Y.
  TITLE     USP12 positively regulates M-MDSC function to inhibit antitumour
            immunity through deubiquitinating and stabilizing p65
  JOURNAL   Immunology 167 (4), 544-557 (2022)
   PUBMED   35898171
  REMARK    GeneRIF: USP12 positively regulates M-MDSC function to inhibit
            antitumour immunity through deubiquitinating and stabilizing p65.
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Sowa,M.E., Bennett,E.J., Gygi,S.P. and Harper,J.W.
  TITLE     Defining the human deubiquitinating enzyme interaction landscape
  JOURNAL   Cell 138 (2), 389-403 (2009)
   PUBMED   19615732
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Cohn,M.A., Kee,Y., Haas,W., Gygi,S.P. and D'Andrea,A.D.
  TITLE     UAF1 is a subunit of multiple deubiquitinating enzyme complexes
  JOURNAL   J Biol Chem 284 (8), 5343-5351 (2009)
   PUBMED   19075014
  REMARK    GeneRIF: two novel multisubunit deubiquitinating enzyme complexes
            containing USP12 and USP46, respectively. Both complexes contain
            the UAF1 protein as a bona fide subunit. Interestingly, UAF1
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Puente,X.S., Sanchez,L.M., Overall,C.M. and Lopez-Otin,C.
  TITLE     Human and mouse proteases: a comparative genomic approach
  JOURNAL   Nat Rev Genet 4 (7), 544-558 (2003)
   PUBMED   12838346
  REMARK    Review article
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Hansen-Hagge,T.E., Janssen,J.W., Hameister,H., Papa,F.R.,
            Zechner,U., Seriu,T., Jauch,A., Becke,D., Hochstrasser,M. and
            Bartram,C.R.
  TITLE     An evolutionarily conserved gene on human chromosome 5q33-q34,
            UBH1, encodes a novel deubiquitinating enzyme
  JOURNAL   Genomics 49 (3), 411-418 (1998)
   PUBMED   9615226
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC026072.1, AF022789.1 and AL355473.20.
            
            On Jul 28, 2010 this sequence version replaced NP_872294.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF022789.1, SRR1803617.159262.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282344.11/ ENSP00000282344.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..370
                     /product="ubiquitin carboxyl-terminal hydrolase 12"
                     /EC_number="3.4.19.12"
                     /note="ubiquitin specific protease 12 like 1;
                     ubiquitin-specific-processing protease 12;
                     deubiquitinating enzyme 12; ubiquitin-hydrolyzing enzyme
                     1; ubiquitin thioesterase 12; ubiquitin thiolesterase 12"
                     /calculated_mol_wt=42727
     Region          1..4
                     /region_name="Required for plasma membrane localization of
                     USP12/WDR20. /evidence=ECO:0000269|PubMed:30466959"
                     /note="propagated from UniProtKB/Swiss-Prot (O75317.2)"
     Region          40..367
                     /region_name="Peptidase_C19G"
                     /note="A subfamily of Peptidase C19. Peptidase C19
                     contains ubiquitinyl hydrolases. They are intracellular
                     peptidases that remove ubiquitin molecules from
                     polyubiquinated peptides by cleavage of isopeptide bonds.
                     They hydrolyze bonds involving the carboxyl...; cd02663"
                     /db_xref="CDD:239128"
     Site            order(43,48,317,333)
                     /site_type="active"
                     /db_xref="CDD:239128"
     Region          145..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75317.2)"
     CDS             1..370
                     /gene="USP12"
                     /gene_synonym="UBH1; USP12L1"
                     /coded_by="NM_182488.4:173..1285"
                     /db_xref="CCDS:CCDS31952.1"
                     /db_xref="GeneID:219333"
                     /db_xref="HGNC:HGNC:20485"
                     /db_xref="MIM:603091"
ORIGIN      
        1 meilmtvskf asictmgana salekeigpe qfpvnehyfg lvnfgntcyc nsvlqalyfc
       61 rpfrekvlay ksqprkkesl ltcladlfhs iatqkkkvgv ippkkfitrl rkenelfdny
      121 mqqdahefln yllntiadil qeerkqekqn grlpngnidn ennnstpdpt wvheifqgtl
      181 tnetrcltce tisskdedfl dlsvdveqnt sithclrgfs ntetlcseyk yyceecrskq
      241 eahkrmkvkk lpmilalhlk rfkymdqlhr ytklsyrvvf plelrlfnts gdatnpdrmy
      301 dlvavvvhcg sgpnrghyia ivkshdfwll fdddivekid aqaieefygl tsdisknses
      361 gyilfyqsrd
//
LOCUS       NP_001353504             915 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 11 [Homo
            sapiens].
ACCESSION   NP_001353504 XP_005245777
VERSION     NP_001353504.1
DBSOURCE    REFSEQ: accession NM_001366575.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 915)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 915)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 915)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 915)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 915)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 915)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 915)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 915)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 915)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 915)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_005245777.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.242134.1,
                                           SRR1803616.22832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..915
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..915
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 11"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=103536
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <381..741
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            527
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            607
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <617..>751
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            639
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            718
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            751
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            763
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            784
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            788
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            792
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            802
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            806
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            808
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            883
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            885
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            912
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..915
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366575.1:26..2773"
                     /note="isoform 11 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS90883.1"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsvtkh kgtekresps papkprkvel sesedkggkm aaadsvqqrr
      481 qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr
      541 mqmgkrwqsp vtksgrrrrs psppptrrrr spspappprr rrtptppprr rtpsppprrr
      601 spsprryspp iqrryspspp pkrrtasppp ppkrraspsp ppkrrvshsp ppkqrsspvt
      661 krrspslssk hrkgsspsrs trearspqpn krhspsprpr apqtsssppp vrrgassspq
      721 rrqspspstr pirrvsrtpe pkkikkaasp spqsvrrvss srsvsgspep aakkppapps
      781 pvqsqspstn wspavpvkka ksptpspspp rnsdqegggk kkkkkkdkkh kkdkkhkkhk
      841 khkkekavaa aaaaavtpaa iaaatttlaq eepvaapepk keteseaedn lddlekhlre
      901 kalrsmrkaq vspqs
//
LOCUS       NP_001336897             447 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 2
            isoform C [Homo sapiens].
ACCESSION   NP_001336897 XP_016884056
VERSION     NP_001336897.1
DBSOURCE    REFSEQ: accession NM_001349968.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wint,H., Li,J., Abe,T., Yamada,H., Higaki,T., Nasu,Y., Watanabe,M.,
            Takei,K. and Takeda,T.
  TITLE     Pacsin 2-dependent N-cadherin internalization regulates the
            migration behaviour of malignant cancer cells
  JOURNAL   J Cell Sci 136 (10) (2023)
   PUBMED   37132654
  REMARK    GeneRIF: Pacsin 2-dependent N-cadherin internalization regulates
            the migration behaviour of malignant cancer cells.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Zudeh,G., Franca,R., Lucafo,M., Bonten,E.J., Bramuzzo,M.,
            Sgarra,R., Lagatolla,C., Franzin,M., Evans,W.E., Decorti,G. and
            Stocco,G.
  TITLE     PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells
  JOURNAL   Life Sci Alliance 6 (3), e202201610 (2023)
   PUBMED   36596605
  REMARK    GeneRIF: PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Park,K., Yoo,H.S., Oh,C.K., Lee,J.R., Chung,H.J., Kim,H.N.,
            Kim,S.H., Kee,K.M., Kim,T.Y., Kim,M., Kim,B.G., Ra,J.S., Myung,K.,
            Kim,H., Han,S.H., Seo,M.D., Lee,Y. and Kim,D.W.
  TITLE     Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate
            drug resistance in chronic myeloid leukemia
  JOURNAL   Cancer Med 11 (21), 4005-4020 (2022)
   PUBMED   35352878
  REMARK    GeneRIF: Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1
            regulate drug resistance in chronic myeloid leukemia.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Ghadimi,M.P., Sanzenbacher,R., Thiede,B., Wenzel,J., Jing,Q.,
            Plomann,M., Borkhardt,A., Kabelitz,D. and Janssen,O.
  TITLE     Identification of interaction partners of the cytosolic polyproline
            region of CD95 ligand (CD178)
  JOURNAL   FEBS Lett 519 (1-3), 50-58 (2002)
   PUBMED   12023017
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Ritter,B., Modregger,J., Paulsson,M. and Plomann,M.
  TITLE     PACSIN 2, a novel member of the PACSIN family of cytoplasmic
            adapter proteins
  JOURNAL   FEBS Lett 454 (3), 356-362 (1999)
   PUBMED   10431838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB477051.1, AL022476.2,
            BC008037.2, HY342978.1, AF128536.1 and BI964045.1.
            
            On Mar 31, 2017 this sequence version replaced XP_016884056.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation by
            regulating tubulin polymerization. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            contains an alternate in-frame exon and  lacks an alternate
            in-frame exon in the 3' coding region, compared to variant 1. The
            resulting protein (isoform C) has the same N- and C-termini, but is
            shorter than isoform A. Variants 4, 7, 8 and 9 encode the same
            protein (isoform C).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..447
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 2 isoform C"
                     /note="syndapin2; syndapin-II; syndapin-2; cytoplasmic
                     phosphoprotein PACSIN2"
                     /calculated_mol_wt=51466
     Region          18..275
                     /region_name="F-BAR_PACSIN2"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein
                     kinase Substrate in Neurons 2 (PACSIN2); cd07679"
                     /db_xref="CDD:153363"
     Site            order(18..20,26..27,30,33,36..37,40..41,43..44,47..48,
                     51..52,54..55,58..59,62,65..66,74..75,79,83,86..87,89,97,
                     145,149,212,227,230,234,237..238,240..242,245,248..249,
                     251..252,255..258,263..264,267,270..271,274..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153363"
     Site            order(25,29,36,46,50,53,65,101,113,132,139..140,147..148,
                     150,203,207,210)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153363"
     Region          390..445
                     /region_name="SH3_PACSIN1-2"
                     /note="Src homology 3 domain of Protein kinase C and
                     Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN
                     2; cd11998"
                     /db_xref="CDD:212931"
     Site            order(396,398,401,405,424..425,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212931"
     CDS             1..447
                     /gene="PACSIN2"
                     /gene_synonym="SDPII"
                     /coded_by="NM_001349968.1:406..1749"
                     /note="isoform C is encoded by transcript variant 4"
                     /db_xref="GeneID:11252"
                     /db_xref="HGNC:HGNC:8571"
                     /db_xref="MIM:604960"
ORIGIN      
        1 msvtyddsvg vevssdsfwe vgnykrtvkr iddghrlcsd lmnclherar iekayaqqlt
       61 ewarrwrqlv ekgpqygtve kawmafmsea ervselhlev kaslmnddfe kiknwqkeaf
      121 hkqmmggfke tkeaedgfrk aqkpwakklk eveaakkahh aackeeklai sreanskadp
      181 slnpeqlkkl qdkiekckqd vlktkekyek slkeldqgtp qymenmeqvf eqcqqfeekr
      241 lrffrevlle vqkhldlsnv agykaiyhdl eqsiraadav edlrwfranh gpgmamnwpq
      301 fedeewsadl nrtlsrrekk katdgvtltg inqtgdqslp skpssvssye ktqsyptdws
      361 ddesnnpfss tdangdsnpf dddatsgtev rvralydyeg qehdelsfka gdeltkmede
      421 deqgwckgrl dngqvglypa nyveaiq
//
LOCUS       NP_001139194             361 aa            linear   PRI 20-NOV-2025
DEFINITION  homer protein homolog 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001139194
VERSION     NP_001139194.1
DBSOURCE    REFSEQ: accession NM_001145722.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 361)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 361)
  AUTHORS   Chen,L., Shan,X., Wan,X., Zha,W. and Fan,R.
  TITLE     HOMER3 promotes liver hepatocellular carcinoma cancer progression
            by -upregulating EZH2 and mediating miR-361/GPNMB axis
  JOURNAL   Pathol Res Pract 254, 155150 (2024)
   PUBMED   38266459
  REMARK    GeneRIF: HOMER3 promotes liver hepatocellular carcinoma cancer
            progression by -upregulating EZH2 and mediating miR-361/GPNMB axis.
REFERENCE   3  (residues 1 to 361)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 361)
  AUTHORS   Peixoto,A., Ferreira,D., Azevedo,R., Freitas,R., Fernandes,E.,
            Relvas-Santos,M., Gaiteiro,C., Soares,J., Cotton,S., Teixeira,B.,
            Paulo,P., Lima,L., Palmeira,C., Martins,G., Oliveira,M.J.,
            Silva,A.M.N., Santos,L.L. and Ferreira,J.A.
  TITLE     Glycoproteomics identifies HOMER3 as a potentially targetable
            biomarker triggered by hypoxia and glucose deprivation in bladder
            cancer
  JOURNAL   J Exp Clin Cancer Res 40 (1), 191 (2021)
   PUBMED   34108014
  REMARK    GeneRIF: Glycoproteomics identifies HOMER3 as a potentially
            targetable biomarker triggered by hypoxia and glucose deprivation
            in bladder cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 361)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 361)
  AUTHORS   Ishiguro,K. and Xavier,R.
  TITLE     Homer-3 regulates activation of serum response element in T cells
            via its EVH1 domain
  JOURNAL   Blood 103 (6), 2248-2256 (2004)
   PUBMED   14645007
  REMARK    GeneRIF: Homer-3 may be involved in the regulation of SRE
            activation in T cells via interaction between its EVH1 domain and
            C/EBP beta.
REFERENCE   7  (residues 1 to 361)
  AUTHORS   Norton,N., Williams,H.J., Williams,N.M., Spurlock,G., Zammit,S.,
            Jones,G., Jones,S., Owen,R., O'Donovan,M.C. and Owen,M.J.
  TITLE     Mutation screening of the Homer gene family and association
            analysis in schizophrenia
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 120B (1), 18-21 (2003)
   PUBMED   12815733
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 361)
  AUTHORS   Soloviev,M.M., Ciruela,F., Chan,W.Y. and McIlhinney,R.A.
  TITLE     Molecular characterisation of two structurally distinct groups of
            human homers, generated by extensive alternative splicing
  JOURNAL   J Mol Biol 295 (5), 1185-1200 (2000)
   PUBMED   10653696
REFERENCE   9  (residues 1 to 361)
  AUTHORS   Tu,J.C., Xiao,B., Yuan,J.P., Lanahan,A.A., Leoffert,K., Li,M.,
            Linden,D.J. and Worley,P.F.
  TITLE     Homer binds a novel proline-rich motif and links group 1
            metabotropic glutamate receptors with IP3 receptors
  JOURNAL   Neuron 21 (4), 717-726 (1998)
   PUBMED   9808459
REFERENCE   10 (residues 1 to 361)
  AUTHORS   Xiao,B., Tu,J.C., Petralia,R.S., Yuan,J.P., Doan,A., Breder,C.D.,
            Ruggiero,A., Lanahan,A.A., Wenthold,R.J. and Worley,P.F.
  TITLE     Homer regulates the association of group 1 metabotropic glutamate
            receptors with multivalent complexes of homer-related, synaptic
            proteins
  JOURNAL   Neuron 21 (4), 707-716 (1998)
   PUBMED   9808458
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002985.1, AK313995.1 and
            CN284196.1.
            
            Summary: This gene encodes a member of the HOMER family of
            postsynaptic density scaffolding proteins that share a similar
            domain structure consisting of an N-terminal
            Enabled/vasodilator-stimulated phosphoprotein homology 1 domain
            which mediates protein-protein interactions, and a carboxy-terminal
            coiled-coil domain and two leucine zipper motifs that are involved
            in self-oligomerization. The encoded protein binds numerous other
            proteins including group I metabotropic glutamate receptors,
            inositol 1,4,5-trisphosphate receptors and amyloid precursor
            proteins and has been implicated in diverse biological functions
            such as neuronal signaling, T-cell activation and trafficking of
            amyloid beta peptides. Alternative splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1), termed Homer-3A01, encodes
            the longest isoform (1). Both variants 1 and 2 encode the same
            protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK313995.1, SRR3476690.805818.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..361
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..361
                     /product="homer protein homolog 3 isoform 1"
                     /note="Homer, neuronal immediate early gene, 3; homer
                     protein homolog 3; homer homolog 3; homer scaffolding
                     protein 3"
                     /calculated_mol_wt=39705
     Region          1..80
                     /region_name="Required for interaction with NFATC2.
                     /evidence=ECO:0000269|PubMed:18218901"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Region          6..114
                     /region_name="EVH1_Homer_Vesl"
                     /note="Homer/Vesl family proteins EVH1 domain; cd01206"
                     /db_xref="CDD:269917"
     Site            order(27,73,77,92)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269917"
     Region          114..169
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2X5; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JP6; propagated from
                     UniProtKB/Swiss-Prot (Q9NSC5.2)"
     Region          <166..>360
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..361
                     /gene="HOMER3"
                     /gene_synonym="HOMER-3; VESL3"
                     /coded_by="NM_001145722.2:523..1608"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12391.1"
                     /db_xref="GeneID:9454"
                     /db_xref="HGNC:HGNC:17514"
                     /db_xref="MIM:604800"
ORIGIN      
        1 mstareqpif strahvfqid patkrnwipa gkhaltvsyf ydatrnvyri isiggakaii
       61 nstvtpnmtf tktsqkfgqw adsrantvyg lgfaseqhlt qfaekfqevk eaarlareks
      121 qdggeltspa lglashqvpp splvsangpg eeklfrsqsa dapgpterer lkkmlsegsv
      181 gevqweaeff alqdsnnkla galreanaaa aqwrqqleaq raeaerlrqr vaeleaqaas
      241 evtptgekeg lgqgqsleql ealvqtkdqe iqtlksqtgg prealeaaer eetqqkvqdl
      301 etrnaelehq lramerslee araererara evgraaqlld vslfelselr eglarlaeaa
      361 p
//
LOCUS       NP_055117                 68 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec61 subunit gamma [Homo sapiens].
ACCESSION   NP_055117
VERSION     NP_055117.1
DBSOURCE    REFSEQ: accession NM_014302.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Lowe,E., Anderl,J.L., Bade,D., Delgado-Martin,C., Dong,C.,
            Fan,R.A., Fang,Y., Jiang,J., Johnson,H.W.B., Kempema,A.,
            McGilvray,P., McMinn,D., Millare,B., Muchamuel,T., Poweleit,N.,
            Qian,Y., Rehan,S., Scapin,G., Sugahara,A., Tranter,D., Tuch,B.,
            Wang,J., Wang,L., Whang,J.A., Zuno-Mitchell,P., Paavilainen,V.O.,
            Park,E., Taunton,J., Kirk,C.J. and Anand,N.K.
  TITLE     Preclinical characterization of novel multi-client inhibitors of
            Sec61 with broad antitumor activity
  JOURNAL   J Pharmacol Exp Ther 392 (8), 103634 (2025)
   PUBMED   40669140
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Yuan,S., Liu,J., Yang,L., Zhang,X., Zhuang,K. and He,S.
  TITLE     Knockdown of circ_0044226 promotes endoplasmic reticulum
            stress-mediated autophagy and apoptosis in hepatic stellate cells
            via miR-4677-3p/SEC61G axis
  JOURNAL   J Bioenerg Biomembr 56 (3), 261-271 (2024)
   PUBMED   38421527
  REMARK    GeneRIF: Knockdown of circ_0044226 promotes endoplasmic reticulum
            stress-mediated autophagy and apoptosis in hepatic stellate cells
            via miR-4677-3p/SEC61G axis.
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Fan,Y., Wang,Y., Liu,F., Wang,H. and Li,Q.
  TITLE     SEC61G Promotes Cervical Cancer Proliferation by Activating MAPK
            Signaling Pathway
  JOURNAL   Dis Markers 2022, 7016079 (2022)
   PUBMED   36092956
  REMARK    GeneRIF: SEC61G Promotes Cervical Cancer Proliferation by
            Activating MAPK Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Zheng,Q., Wang,Z., Zhang,M., Yu,Y., Chen,R., Lu,T., Liu,L., Ma,J.,
            Liu,T., Zheng,H., Li,H. and Li,J.
  TITLE     Prognostic value of SEC61G in lung adenocarcinoma: a comprehensive
            study based on bioinformatics and in vitro validation
  JOURNAL   BMC Cancer 21 (1), 1216 (2021)
   PUBMED   34774014
  REMARK    GeneRIF: Prognostic value of SEC61G in lung adenocarcinoma: a
            comprehensive study based on bioinformatics and in vitro
            validation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 68)
  AUTHORS   Lu,T., Chen,Y., Gong,X., Guo,Q., Lin,C., Luo,Q., Tu,Z., Pan,J. and
            Li,J.
  TITLE     SEC61G overexpression and DNA amplification correlates with
            prognosis and immune cell infiltration in head and neck squamous
            cell carcinoma
  JOURNAL   Cancer Med 10 (21), 7847-7862 (2021)
   PUBMED   34590792
  REMARK    GeneRIF: SEC61G overexpression and DNA amplification correlates
            with prognosis and immune cell infiltration in head and neck
            squamous cell carcinoma.
REFERENCE   6  (residues 1 to 68)
  AUTHORS   Greenfield,J.J. and High,S.
  TITLE     The Sec61 complex is located in both the ER and the ER-Golgi
            intermediate compartment
  JOURNAL   J Cell Sci 112 (Pt 10), 1477-1486 (1999)
   PUBMED   10212142
REFERENCE   7  (residues 1 to 68)
  AUTHORS   Chen,Y., Le Caherec,F. and Chuck,S.L.
  TITLE     Calnexin and other factors that alter translocation affect the
            rapid binding of ubiquitin to apoB in the Sec61 complex
  JOURNAL   J Biol Chem 273 (19), 11887-11894 (1998)
   PUBMED   9565615
REFERENCE   8  (residues 1 to 68)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   9  (residues 1 to 68)
  AUTHORS   Wiertz,E.J., Tortorella,D., Bogyo,M., Yu,J., Mothes,W., Jones,T.R.,
            Rapoport,T.A. and Ploegh,H.L.
  TITLE     Sec61-mediated transfer of a membrane protein from the endoplasmic
            reticulum to the proteasome for destruction
  JOURNAL   Nature 384 (6608), 432-438 (1996)
   PUBMED   8945469
REFERENCE   10 (residues 1 to 68)
  AUTHORS   Hartmann,E., Sommer,T., Prehn,S., Gorlich,D., Jentsch,S. and
            Rapoport,T.A.
  TITLE     Evolutionary conservation of components of the protein
            translocation complex
  JOURNAL   Nature 367 (6464), 654-657 (1994)
   PUBMED   8107851
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU932672.1, AF086539.1 and
            CD385140.1.
            
            Summary: The Sec61 complex is the central component of the protein
            translocation apparatus of the endoplasmic reticulum (ER) membrane.
            Oligomers of the Sec61 complex form a transmembrane channel where
            proteins are translocated across and integrated into the ER
            membrane. This complex consists of three membrane proteins- alpha,
            beta, and gamma. This gene encodes the gamma-subunit protein.
            Alternatively spliced transcript variants encoding the same protein
            have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB107787.1, HY068417.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142586, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352861.9/ ENSP00000341538.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.2"
     Protein         1..68
                     /product="protein transport protein Sec61 subunit gamma"
                     /note="protein transport protein SEC61 gamma subunit;
                     Sec61 gamma subunit; SEC61 translocon gamma subunit"
                     /calculated_mol_wt=7610
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (P60059.1)"
     Region          <12..68
                     /region_name="secE"
                     /note="preprotein translocase subunit SecE; Reviewed;
                     cl00481"
                     /db_xref="CDD:469787"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P60059.1)"
     Site            33..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P60059.1)"
     CDS             1..68
                     /gene="SEC61G"
                     /gene_synonym="SSS1"
                     /coded_by="NM_014302.4:61..267"
                     /db_xref="CCDS:CCDS5513.1"
                     /db_xref="GeneID:23480"
                     /db_xref="HGNC:HGNC:18277"
                     /db_xref="MIM:609215"
ORIGIN      
        1 mdqvmqfvep srqfvkdsir lvkrctkpdr kefqkiamat aigfaimgfi gffvklihip
       61 inniivgg
//
LOCUS       NP_775098                736 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform c
            [Homo sapiens].
ACCESSION   NP_775098
VERSION     NP_775098.2
DBSOURCE    REFSEQ: accession NM_173075.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 736)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB236935.1, BC027946.1,
            AC093804.3, AC131953.1 and AL080130.1.
            
            On Jul 9, 2004 this sequence version replaced NP_775098.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (3) uses two alternate in-frame
            splice sites and lacks an alternate in-frame exon in the central
            coding region, compared to variant 1, resulting in an isoform (c)
            that is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027946.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..736
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform c"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=80758
     Region          292..320
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          395..532
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(410,478,495)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(477..482,495,517,521)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Region          560..686
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(571,645,664)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(582,584,632..633,635..642,644,652,658,668,670,673,
                     677,680..681,683..684)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..736
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_173075.5:555..2765"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43224.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 msevlpadsg vdtlavfmas sgttdvtnrn spatppntln lrsshnelln aeikhtetkn
       61 stppkcrkky altniqaamg lsdpaaqpll gngsaniklv kngenqlrka aeqgqqdpnk
      121 nlsptavini tseklegkep hpqdssscei lpsqprrtks flnyyadlet sareleqnrg
      181 nhhgtaeeks qpvqgqasti igngdlllqk pnrpqssped gqvatvsssp etkkdhpktg
      241 aktdcalhri qnlapsdees swttlsqdsa spsspdetdi wsdhsfqtdp dlppgwkrvs
      301 diagtyywhi ptgttqwerp vsipadlqgs rkgslssvtp sptpenedlh aatvnpdpsl
      361 kefegatlry aslklrnaph pddddscsin sdpeakcfav rslgwvemae edlapgkssv
      421 avnncirqls yckndirdtv giwgegkdmy lilendmlsl vdpmdrsvlh sqpivsirvw
      481 gvgrdngrdf ayvardkdtr ilkchvfrcd tpakaiatsl heicskimae rknakalacs
      541 slqeranvnl dvplqdfptp ktelvqkfhv qylgmlpvdk pvgmdilnsa ienlmtssnk
      601 edwlsvnmnv adatvtvise kneeevlvec rvrflsfmgv gkdvhtfafi mdtgnqrfec
      661 hvfwcepnag nvseavqaac mlryqkclva rppsqkvrpp pppadsvtrr vttnvkrgvl
      721 slidtlkqkr pvtemp
//
LOCUS       NP_036259                898 aa            linear   PRI 20-NOV-2025
DEFINITION  cip1-interacting zinc finger protein isoform 1 [Homo sapiens].
ACCESSION   NP_036259
VERSION     NP_036259.2
DBSOURCE    REFSEQ: accession NM_012127.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Chen,Y.R., Wu,Y.S., Wang,W.S., Zhang,J.S. and Wu,Q.G.
  TITLE     Upregulation of lncRNA DANCR functions as an oncogenic role in
            non-small lung cancer by regulating miR-214-5p/CIZ1 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2539-2547 (2020)
   PUBMED   32196604
  REMARK    GeneRIF: Upregulation of lncRNA DANCR functions as an oncogenic
            role in non-small lung cancer by regulating miR-214-5p/CIZ1 axis.
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Chen,X., Wang,P., Wang,S., Li,J., Ou,T. and Zeng,X.
  TITLE     CIZ1 knockdown suppresses the proliferation of bladder cancer cells
            by inducing apoptosis
  JOURNAL   Gene 719, 143946 (2019)
   PUBMED   31252164
  REMARK    GeneRIF: silencing of CIZ1 suppressed bladder cancer cell
            proliferation through inducing apoptosis and reducing cell cycle
            progression
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Coverley,D., Marr,J. and Ainscough,J.
  TITLE     Ciz1 promotes mammalian DNA replication
  JOURNAL   J Cell Sci 118 (Pt 1), 101-112 (2005)
   PUBMED   15585571
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Warder,D.E. and Keherly,M.J.
  TITLE     Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus
            DNA sequence ARYSR(0-2)YYAC
  JOURNAL   J Biomed Sci 10 (4), 406-417 (2003)
   PUBMED   12824700
  REMARK    GeneRIF: data indicate that Ciz1 is localized in the nucleus and is
            expressed in a wide range of tissues, especially the pancreas and
            the brain; formulated a consensus DNA sequence, ARYSR(0-2)YYAC,
            recognized by Ciz1
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Mitsui,K., Matsumoto,A., Ohtsuka,S., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
            zinc finger protein, ciz1
  JOURNAL   Biochem Biophys Res Commun 264 (2), 457-464 (1999)
   PUBMED   10529385
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK023978.1, AF159025.1 and
            BC021163.2.
            
            On Feb 13, 2004 this sequence version replaced NP_036259.1.
            
            Summary: The protein encoded by this gene is a zinc finger DNA
            binding protein that interacts with CIP1, part of a complex with
            cyclin E. The encoded protein may regulate the cellular
            localization of CIP1. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) has an alternate exon in place
            of the first exon and lacks an alternate in-frame exon compared to
            variant 6. The resulting isoform (1) is shorter at the N-terminus
            and lacks an alternate internal segment compared to isoform 5.
            Variants 1 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.24636.1,
                                           SRR1803616.130338.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..898
                     /product="cip1-interacting zinc finger protein isoform 1"
                     /note="zinc finger protein 356; nuclear protein NP94;
                     Cip1-interacting zinc finger protein"
                     /calculated_mol_wt=99915
     Region          48..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          <129..482
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          157..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          318..471
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          562..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          592..621
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          656..676
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(663..665,666,670,675,692,695..699,701..702)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <666..>717
                     /region_name="UFD2"
                     /note="U1-like Zn-finger-containing protein [General
                     function prediction only]; COG5112"
                     /db_xref="CDD:227443"
     Region          686..710
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          687..709
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Site            838
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULV3.2)"
     Region          859..898
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULV3.2)"
     CDS             1..898
                     /gene="CIZ1"
                     /gene_synonym="LSFR1; NP94; ZNF356"
                     /coded_by="NM_012127.3:43..2739"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6894.1"
                     /db_xref="GeneID:25792"
                     /db_xref="HGNC:HGNC:16744"
                     /db_xref="MIM:611420"
ORIGIN      
        1 mfsqqqqqql qqqqqqlqql qqqqlqqqql qqqqllqlqq llqqsppqap lpmavsrglp
       61 pqqpqqplln lqgtnsasll ngsmlqrall lqqlqgldqf amppatydta gltmptatlg
      121 nlrgygmasp glaapsltpp qlatpnlqqf fpqatrqsll gpppvgvpmn psqfnlsgrn
      181 pqkqartsss ttpnrkdsss qtmpvedksd ppegseeaae prmdtpedqd lppcpediak
      241 ekrtpapepe pceaselpak rlrsseepte keppgqlqvk aqpqarmtvp kqtqtpdllp
      301 ealeaqvlpr fqprvlqvqa qvqsqtqpri pstdtqvqpk lqkqaqtqts pehlvlqqkq
      361 vqpqlqqeae pqkqvqpqvq pqahsqgprq vqlqqeaepl kqvqpqvqpq ahsqpprqvq
      421 lqlqkqvqtq typqvhtqaq psvqpqehpp aqvsvqppeq theqphtqpq vsllapeqtp
      481 vvvhvcglem ppdaveaggg mektlpepvg tqvsmeeiqn esacgldvge cenrarempg
      541 vwgaggslkv tilqssdsra fstvpltpvp rpsdsvsstp aatstpskqa lqffcyicka
      601 scssqqefqd hmsepqhqqr lgeiqhmsqa cllsllpvpr dvletedeep pprrwcntcq
      661 lyymgdliqh rrtqdhkiak qslrpfctvc nryfktprkf vehvksqghk dkakelksle
      721 keiagqdedh fitvdavgcf egdeeeeedd edeeeievee elckqvrsrd isreewkgse
      781 tyspntaygv dflvpvmgyi crichkfyhs nsgaqlshck slghfenlqk ykaaknpspt
      841 trpvsrrcai narnaltalf tssgrppsqp ntqdktpskv tarpsqpplp rrstrlkt
//
LOCUS       NP_001229827             959 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001229827
VERSION     NP_001229827.1
DBSOURCE    REFSEQ: accession NM_001242898.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 959)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 959)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 959)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 959)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 959)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 959)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 959)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 959)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 959)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 959)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, DB452735.1,
            AK302472.1, AL671545.13 and AL096767.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.272956.1,
                                           SRR3476690.990363.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000612753.5/ ENSP00000478417.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..959
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..959
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 1"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=104104
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          408..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          657..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          <703..950
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3Q2; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          812..849
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     CDS             1..959
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001242898.2:372..3251"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74881.1"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlvsthhl
      541 hsssededie gafpnelslq qafsdyqiqq mtanfvdqfg fndeefadqd dninapfdri
      601 aeinfnidad edspsaalfe accsdriqpf dddedediwe dsdtrcaarv marprfgaph
      661 asescskngp erggqdgkas leahrdapga gappapgkke appvegdseg amwtavfdep
      721 anstptapgv vrdvgssvwa agtsapeekg wakftdfqpf ccsesgprcs spvdtecsha
      781 egsrsqgpek afspaspcaw nvcvtrkapl lasdssssgg shsedgdqka asamdavsrg
      841 pgreapplpt varteeavgr vgcadsrlls pacpapkevt aapavavppe atvaittals
      901 kagpaiptpa vssalavavp lgpimavtaa pamvatlgtv tkdgktdapp egaalngpv
//
LOCUS       NP_003620                461 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 1
            [Homo sapiens].
ACCESSION   NP_003620
VERSION     NP_003620.3
DBSOURCE    REFSEQ: accession NM_003629.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC021622.1, BC094768.1 and
            U90907.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 2, 2008 this sequence version replaced NP_003620.2.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749649.1, BC021622.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262741.10/ ENSP00000262741.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..461
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 1"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=54317
     Region          59..167
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(72,90,112,114)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(113,140)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          172..332
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Site            order(195,202,213..215,217..219,221..222,225..226,
                     228..229,232..233,236,252,255..256,259,263,266,292..293,
                     296,299)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:214018"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q64143; propagated from
                     UniProtKB/Swiss-Prot (Q92569.2)"
     Region          351..454
                     /region_name="SH2_cSH2_p85_like"
                     /note="C-terminal Src homology 2 (cSH2) domain found in
                     p85; cd09930"
                     /db_xref="CDD:198184"
     Site            order(365,383,385..386,403,405)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198184"
     Site            order(404,415,437,440,444)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..461
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_003629.4:678..2063"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS529.1"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 myntvwsmdr ddadwrevmm pystelifyi emdppalppk ppkpmtsavp ngmkdssvsl
       61 qdaewywgdi sreevndklr dmpdgtflvr dastkmqgdy tltlrkggnn klikiyhrdg
      121 kygfsdpltf nsvvelinhy hheslaqynp kldvklmypv sryqqdqlvk ednidavgkk
      181 lqeyhsqyqe kskeydrlye eytrtsqeiq mkrtaieafn etikifeeqc htqeqhskey
      241 ierfrregne keierimmny dklksrlgei hdskmrleqd lknqaldnre idkkmnsikp
      301 dliqlrkird qhlvwlnhkg vrqkrlnvwl giknedaden yfineedenl phydektwfv
      361 edinrvqaed llygkpdgaf liresskkgc yacsvvadge vkhcviysta rgygfaepyn
      421 lysslkelvl hyqqtslvqh ndslnvrlay pvhaqmpslc r
//
LOCUS       NP_001006945             766 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-4 isoform b [Homo sapiens].
ACCESSION   NP_001006945
VERSION     NP_001006945.1
DBSOURCE    REFSEQ: accession NM_001006944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Wu,S., Jin,J., Huang,J., Chen,G. and Chen,Y.
  TITLE     Comprehensive analysis of the RSK gene family in acute myeloid
            leukemia determines a prognostic signature for the prediction of
            clinical prognosis and treatment responses
  JOURNAL   Hematology 28 (1), 2235833 (2023)
   PUBMED   37462338
  REMARK    GeneRIF: Comprehensive analysis of the RSK gene family in acute
            myeloid leukemia determines a prognostic signature for the
            prediction of clinical prognosis and treatment responses.
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Qiu,M., Lin,Q., Liu,Y., Chen,P., Zhou,Y., Jiang,Y., Zhou,Z.,
            Wen,Q., Zhou,X., Liang,X., Gan,H. and Yu,H.
  TITLE     Potentially functional genetic variants in RPS6KA4 and MAP2K5 in
            the MAPK signaling pathway predict HBV-related hepatocellular
            carcinoma survival
  JOURNAL   Mol Carcinog 62 (9), 1378-1387 (2023)
   PUBMED   37278562
  REMARK    GeneRIF: Potentially functional genetic variants in RPS6KA4 and
            MAP2K5 in the MAPK signaling pathway predict HBV-related
            hepatocellular carcinoma survival.
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Sattarifard,H., Safaei,A., Khazeeva,E., Rastegar,M. and Davie,J.R.
  TITLE     Mitogen- and stress-activated protein kinase (MSK1/2) regulated
            gene expression in normal and disease states
  JOURNAL   Biochem Cell Biol 101 (3), 204-219 (2023)
   PUBMED   36812480
  REMARK    GeneRIF: Mitogen- and stress-activated protein kinase (MSK1/2)
            regulated gene expression in normal and disease states.
            Review article
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Akbar,N., Forteath,C., Hussain,M.S., Reyskens,K., Belch,J.J.F.,
            Lang,C.C., Mordi,I.R., Bhalraam,U., Arthur,J.S.C. and Khan,F.
  TITLE     Mitogen and Stress-Activated Kinases 1 and 2 Mediate Endothelial
            Dysfunction
  JOURNAL   Int J Mol Sci 22 (16), 8655 (2021)
   PUBMED   34445361
  REMARK    GeneRIF: Mitogen and Stress-Activated Kinases 1 and 2 Mediate
            Endothelial Dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Du,K. and Montminy,M.
  TITLE     CREB is a regulatory target for the protein kinase Akt/PKB
  JOURNAL   J Biol Chem 273 (49), 32377-32379 (1998)
   PUBMED   9829964
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Zhu,S. and Gerhard,D.S.
  TITLE     A transcript map of an 800-kb region on human chromosome 11q13,
            part of the candidate region for SCA5 and BBS1
  JOURNAL   Hum Genet 103 (6), 674-680 (1998)
   PUBMED   9921902
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Pierrat,B., Correia,J.S., Mary,J.L., Tomas-Zuber,M. and
            Lesslauer,W.
  TITLE     RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase
            under dominant control of p38alpha mitogen-activated protein kinase
            (p38alphaMAPK)
  JOURNAL   J Biol Chem 273 (45), 29661-29671 (1998)
   PUBMED   9792677
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Deak,M., Clifton,A.D., Lucocq,L.M. and Alessi,D.R.
  TITLE     Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
            activated by MAPK and SAPK2/p38, and may mediate activation of CREB
  JOURNAL   EMBO J 17 (15), 4426-4441 (1998)
   PUBMED   9687510
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Xing,J., Ginty,D.D. and Greenberg,M.E.
  TITLE     Coupling of the RAS-MAPK pathway to gene activation by RSK2, a
            growth factor-regulated CREB kinase
  JOURNAL   Science 273 (5277), 959-963 (1996)
   PUBMED   8688081
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI523588.1, AJ010119.1 and
            AF074715.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            non-identical kinase catalytic domains and phosphorylates various
            substrates, including CREB1 and ATF1. The encoded protein can also
            phosphorylate histone H3 to regulate certain inflammatory genes.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the coding region, compared to variant 1, resulting
            in a shorter protein (isoform b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..766
                     /product="ribosomal protein S6 kinase alpha-4 isoform b"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein kinase B; mitogen- and
                     stress-activated protein kinase 2; ribosomal protein S6
                     kinase, 90kDa, polypeptide 4; ribosomal protein S6 kinase
                     alpha-4; 90 kDa ribosomal protein S6 kinase 4; nuclear
                     mitogen- and stress-activated protein kinase 2"
                     /calculated_mol_wt=84753
     Region          32..364
                     /region_name="STKc_MSK2_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, Mitogen and stress-activated kinase 2; cd05614"
                     /db_xref="CDD:270765"
     Site            order(39..43,47,63,65,99,115..116,118,122,124,161,163,
                     165..166,168,178..179,182,197..202,230,236,239)
                     /site_type="active"
                     /db_xref="CDD:270765"
     Site            order(39..43,47,63,65,99,116..118,122,161,163,165..166,
                     168,178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270765"
     Site            order(43,122,124,161,163,165,182,197..202,230,236,239)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270765"
     Site            order(178..188,191..202)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270765"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            344
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270765"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            356..361
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270765"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Region          400..708
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(411..414,417,419,432,434,461,477..480,524,528..529,
                     531,544..545)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Region          667..690
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            681
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Region          719..766
                     /region_name="Required for nuclear targeting and
                     association with MAPK14"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Region          722..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            739
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     CDS             1..766
                     /gene="RPS6KA4"
                     /gene_synonym="MSK2; RSK-B; S6K-alpha-4"
                     /coded_by="NM_001006944.2:75..2375"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:8986"
                     /db_xref="HGNC:HGNC:10433"
                     /db_xref="MIM:603606"
ORIGIN      
        1 mgdedddesc avelritean ltgheekvsv enfellkvlg tgaygkvflv rkagghdagk
       61 lyamkvlrka alvqraktqe htrtersvle lvrqapflvt lhyafqtdak lhlildyvsg
      121 gemfthlyqr qyfkeaevrv yggeivlale hlhklgiiyr dlklenvlld seghivltdf
      181 glskefltee kertfsfcgt ieymapeiir sktghgkavd wwslgillfe lltgaspftl
      241 egerntqaev srrilkcspp fpprigpvaq dllqrllckd pkkrlgagpq gaqevrnhpf
      301 fqgldwvala arkipapfrp qirseldvgn faeeftrlep vysppgsppp gdprifqgys
      361 fvapsilfdh nnavmtdgle apgagdrpgr aavarsammq qyeldlrepa lgqgsfsvcr
      421 rcrqrqsgqe favkilsrrl eantqrevaa lrlcqshpnv vnlhevhhdq lhtylvlell
      481 rggellehir kkrhfsesea sqilrslvsa vsfmheeagv vhrdlkpeni lyaddtpgap
      541 vkiidfgfar lrpqspgvpm qtpcftlqya apellaqqgy descdlwslg vilymmlsgq
      601 vpfqgasgqg gqsqaaeimc kiregrfsld geawqgvsee akelvrgllt vdpakrlkle
      661 glrgsswlqd gsarsspplr tpdvlessgp avrsglnatf mafnrgkreg fflksvenap
      721 lakrrkqklr satasrrgsp apanpgrapv askgaprran gplpps
//
LOCUS       NP_005447                711 aa            linear   PRI 20-NOV-2025
DEFINITION  C-Jun-amino-terminal kinase-interacting protein 1 [Homo sapiens].
ACCESSION   NP_005447
VERSION     NP_005447.1
DBSOURCE    REFSEQ: accession NM_005456.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 711)
  AUTHORS   Marino Perez,L., Ielasi,F.S., Lee,A., Delaforge,E., Juyoux,P.,
            Tengo,M., Davis,R.J., Palencia,A. and Jensen,M.R.
  TITLE     Structural basis of homodimerization of the JNK scaffold protein
            JIP2 and its heterodimerization with JIP1
  JOURNAL   Structure 32 (9), 1394-1403 (2024)
   PUBMED   39013462
  REMARK    GeneRIF: Structural basis of homodimerization of the JNK scaffold
            protein JIP2 and its heterodimerization with JIP1.
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Saeed,R., Mohammed,A.K., Saleh,S.E., Aboulwafa,M.M., Aboshanab,K.M.
            and Taneera,J.
  TITLE     Dual Role of Mitogen-Activated Protein Kinase 8 Interacting
            Protein-1 in Inflammasome and Pancreatic beta-Cell Function
  JOURNAL   Int J Mol Sci 24 (5), 4990 (2023)
   PUBMED   36902422
  REMARK    GeneRIF: Dual Role of Mitogen-Activated Protein Kinase 8
            Interacting Protein-1 in Inflammasome and Pancreatic beta-Cell
            Function.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 711)
  AUTHORS   Shi,J., Lu,D., Gu,R., Xu,Y., Pan,R., Bo,F. and Zhang,Y.
  TITLE     Identification of Key Biomarkers and Immune Infiltration in
            Sporadic Vestibular Schwannoma Basing Transcriptome-Wide Profiling
  JOURNAL   World Neurosurg 160, e591-e600 (2022)
   PUBMED   35092815
  REMARK    GeneRIF: Identification of Key Biomarkers and Immune Infiltration
            in Sporadic Vestibular Schwannoma Basing Transcriptome-Wide
            Profiling.
REFERENCE   6  (residues 1 to 711)
  AUTHORS   Yasuda,J., Whitmarsh,A.J., Cavanagh,J., Sharma,M. and Davis,R.J.
  TITLE     The JIP group of mitogen-activated protein kinase scaffold proteins
  JOURNAL   Mol Cell Biol 19 (10), 7245-7254 (1999)
   PUBMED   10490659
REFERENCE   7  (residues 1 to 711)
  AUTHORS   Mooser,V., Maillard,A., Bonny,C., Steinmann,M., Shaw,P.,
            Yarnall,D.P., Burns,D.K., Schorderet,D.F., Nicod,P. and Waeber,G.
  TITLE     Genomic organization, fine-mapping, and expression of the human
            islet-brain 1 (IB1)/c-Jun-amino-terminal kinase interacting
            protein-1 (JIP-1) gene
  JOURNAL   Genomics 55 (2), 202-208 (1999)
   PUBMED   9933567
REFERENCE   8  (residues 1 to 711)
  AUTHORS   Whitmarsh,A.J., Cavanagh,J., Tournier,C., Yasuda,J. and Davis,R.J.
  TITLE     A mammalian scaffold complex that selectively mediates MAP kinase
            activation
  JOURNAL   Science 281 (5383), 1671-1674 (1998)
   PUBMED   9733513
REFERENCE   9  (residues 1 to 711)
  AUTHORS   Bonny,C., Nicod,P. and Waeber,G.
  TITLE     IB1, a JIP-1-related nuclear protein present in insulin-secreting
            cells
  JOURNAL   J Biol Chem 273 (4), 1843-1846 (1998)
   PUBMED   9442013
REFERENCE   10 (residues 1 to 711)
  AUTHORS   Dickens,M., Rogers,J.S., Cavanagh,J., Raitano,A., Xia,Z.,
            Halpern,J.R., Greenberg,M.E., Sawyers,C.L. and Davis,R.J.
  TITLE     A cytoplasmic inhibitor of the JNK signal transduction pathway
  JOURNAL   Science 277 (5326), 693-696 (1997)
   PUBMED   9235893
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC068470.1, AF074091.1 and
            AF007134.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a regulator of the pancreatic beta-cell
            function. It is highly similar to JIP-1, a mouse protein known to
            be a regulator of c-Jun amino-terminal kinase (Mapk8). This protein
            has been shown to prevent MAPK8 mediated activation of
            transcription factors, and to decrease IL-1 beta and MAP kinase
            kinase 1 (MEKK1) induced apoptosis in pancreatic beta cells. This
            protein also functions as a DNA-binding transactivator of the
            glucose transporter GLUT2. RE1-silencing transcription factor
            (REST) is reported to repress the expression of this gene in
            insulin-secreting beta cells. This gene is found to be mutated in a
            type 2 diabetes family, and thus is thought to be a susceptibility
            gene for type 2 diabetes. [provided by RefSeq, May 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC068470.1, AF074091.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000241014.6/ ENSP00000241014.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..711
                     /product="C-Jun-amino-terminal kinase-interacting protein
                     1"
                     /note="islet-brain 1; JNK-interacting protein 1; PRKM8
                     interacting protein; IB-1; JNK MAP kinase scaffold protein
                     1"
                     /calculated_mol_wt=77394
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVI9; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVI9; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          78..371
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8, MAPK9 and MAPK10.
                     /evidence=ECO:0000269|PubMed:12756254; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          127..285
                     /region_name="JNK-binding domain (JBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          157..176
                     /region_name="Minimal inhibitory domain (MID)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8, MAPK9 and MAPK10.
                     /evidence=ECO:0000269|PubMed:12756254; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          283..471
                     /region_name="Interaction with MAP3K7.
                     /evidence=ECO:0000269|PubMed:17709393"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          353..360
                     /region_name="D-box 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            355
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          364..372
                     /region_name="D-box 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          429..451
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            444
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          471..660
                     /region_name="Interaction with VRK2.
                     /evidence=ECO:0000269|PubMed:18286207"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            472
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16195223; propagated from
                     UniProtKB/Swiss-Prot (Q9UQF2.1)"
     Region          492..546
                     /region_name="SH3_JIP1"
                     /note="Src homology 3 domain of JNK-interacting protein 1;
                     cd11943"
                     /db_xref="CDD:212876"
     Site            order(497..500,502..503,505..506,521,523..525,527,538,
                     540..543)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:212876"
     Site            order(497,499,502,506,524..525,540,542..543)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212876"
     Region          563..711
                     /region_name="PTB_JIP"
                     /note="JNK-interacting protein-like (JIP)
                     Phosphotyrosine-binding (PTB) domain; cd01212"
                     /db_xref="CDD:269923"
     Site            order(570,655,675)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269923"
     Site            order(644..649,662,684,688)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269923"
     CDS             1..711
                     /gene="MAPK8IP1"
                     /gene_synonym="IB1; JIP-1; JIP1; PRKM8IP"
                     /coded_by="NM_005456.4:171..2306"
                     /db_xref="CCDS:CCDS7916.1"
                     /db_xref="GeneID:9479"
                     /db_xref="HGNC:HGNC:6882"
                     /db_xref="MIM:604641"
ORIGIN      
        1 maeresgglg ggaasppaas pflglhiasp pnfrlthdis leefededls eitdecgisl
       61 qckdtlslrp pragllsagg ggagsrlqae mlqmdlidat gdtpgaedde edddeeraar
      121 rpgagppkae sgqepasrgq gqsqgqsqgp gsgdtyrpkr pttlnlfpqv prsqdtlnnn
      181 slgkkhswqd rvsrsssplk tgeqtppheh iclsdelppq sgpapttdrg tstdspcrrs
      241 tatqmappgg ppaappggrg hshrdrihyq advrleatee iyltpvqrpp daaeptsafl
      301 pptesrmsvs sdpdpaayps tagrphpsis eeeegfdcls speraeppgg gwrgslgepp
      361 pppraslssd tsalsydsvk ytlvvdehaq lelvslrpcf gdysdesdsa tvydncasvs
      421 spyesaigee yeeaprpqpp aclsedstpd epdvhfskkf lnvfmsgrsr sssaesfglf
      481 sciingeeqe qthraifrfv prhedelele vddpllvelq aedywyeayn mrtgargvfp
      541 ayyaievtke pehmaalakn sdwvdqfrvk flgsvqvpyh kgndvlcaam qkiattrrlt
      601 vhfnppsscv leisvrgvki gvkaddsqea kgnkcshffq lknisfcgyh pknnkyfgfi
      661 tkhpadhrfa chvfvsedst kalaesvgra fqqfykqfve ytcptediyl e
//
LOCUS       NP_003807                819 aa            linear   PRI 20-NOV-2025
DEFINITION  disintegrin and metalloproteinase domain-containing protein 9
            precursor [Homo sapiens].
ACCESSION   NP_003807
VERSION     NP_003807.1
DBSOURCE    REFSEQ: accession NM_003816.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Jiang,L., Huang,W., Cao,M., Jiang,Y., Li,S., Li,M., Yang,R., Wu,Z.,
            Wang,Y., Lv,C. and Huang,Z.
  TITLE     Deciphering the oncogenic potential of ADAM9 in hepatocellular
            carcinoma through bioinformatics and experimental approaches
  JOURNAL   Sci Rep 14 (1), 26432 (2024)
   PUBMED   39488509
  REMARK    GeneRIF: Deciphering the oncogenic potential of ADAM9 in
            hepatocellular carcinoma through bioinformatics and experimental
            approaches.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Bazzone,L.E., Zhu,J., King,M., Liu,G., Guo,Z., MacKay,C.R.,
            Kyawe,P.P., Qaisar,N., Rojas-Quintero,J., Owen,C.A., Brass,A.L.,
            McDougall,W., Baer,C.E., Cashman,T., Trivedi,C.M., Gack,M.U.,
            Finberg,R.W. and Kurt-Jones,E.A.
  TITLE     ADAM9 promotes type I interferon-mediated innate immunity during
            encephalomyocarditis virus infection
  JOURNAL   Nat Commun 15 (1), 4153 (2024)
   PUBMED   38755212
  REMARK    GeneRIF: ADAM9 promotes type I interferon-mediated innate immunity
            during encephalomyocarditis virus infection.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Liu,J., Wang,Y., Zhang,S., Sun,L. and Shi,Y.
  TITLE     ADAM9 deubiquitination induced by USP22 suppresses proliferation,
            migration, invasion, and epithelial-mesenchymal transition of
            trophoblast cells in preeclampsia
  JOURNAL   Placenta 146, 50-57 (2024)
   PUBMED   38176298
  REMARK    GeneRIF: ADAM9 deubiquitination induced by USP22 suppresses
            proliferation, migration, invasion, and epithelial-mesenchymal
            transition of trophoblast cells in preeclampsia.
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Chang,A.C., Lin,L.W., Chen,Y.C., Chen,P.C., Liu,S.C., Tai,H.C.,
            Wu,H.C., Sung,S.Y., Lin,T.H. and Tang,C.H.
  TITLE     The ADAM9/WISP-1 axis cooperates with osteoblasts to stimulate
            primary prostate tumor growth and metastasis
  JOURNAL   Int J Biol Sci 19 (3), 760-771 (2023)
   PUBMED   36778124
  REMARK    GeneRIF: The ADAM9/WISP-1 axis cooperates with osteoblasts to
            stimulate primary prostate tumor growth and metastasis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Roghani,M., Becherer,J.D., Moss,M.L., Atherton,R.E.,
            Erdjument-Bromage,H., Arribas,J., Blackburn,R.K., Weskamp,G.,
            Tempst,P. and Blobel,C.P.
  TITLE     Metalloprotease-disintegrin MDC9: intracellular maturation and
            catalytic activity
  JOURNAL   J Biol Chem 274 (6), 3531-3540 (1999)
   PUBMED   9920899
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Izumi,Y., Hirata,M., Hasuwa,H., Iwamoto,R., Umata,T., Miyado,K.,
            Tamai,Y., Kurisaki,T., Sehara-Fujisawa,A., Ohno,S. and Mekada,E.
  TITLE     A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and
            PKCdelta are involved in TPA-induced ectodomain shedding of
            membrane-anchored heparin-binding EGF-like growth factor
  JOURNAL   EMBO J 17 (24), 7260-7272 (1998)
   PUBMED   9857183
REFERENCE   8  (residues 1 to 819)
  AUTHORS   McKie,N., Edwards,T., Dallas,D.J., Houghton,A., Stringer,B.,
            Graham,R., Russell,G. and Croucher,P.I.
  TITLE     Expression of members of a novel membrane linked metalloproteinase
            family (ADAM) in human articular chondrocytes
  JOURNAL   Biochem Biophys Res Commun 230 (2), 335-339 (1997)
   PUBMED   9016778
REFERENCE   9  (residues 1 to 819)
  AUTHORS   McKie,N., Dallas,D.J., Edwards,T., Apperley,J.F., Russell,R.G. and
            Croucher,P.I.
  TITLE     Cloning of a novel membrane-linked metalloproteinase from human
            myeloma cells
  JOURNAL   Biochem J 318 (Pt 2) (Pt 2), 459-462 (1996)
   PUBMED   8809033
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Weskamp,G., Kratzschmar,J., Reid,M.S. and Blobel,C.P.
  TITLE     MDC9, a widely expressed cellular disintegrin containing
            cytoplasmic SH3 ligand domains
  JOURNAL   J Cell Biol 132 (4), 717-726 (1996)
   PUBMED   8647900
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108863.4 and AC105091.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the ADAM (a disintegrin and
            metalloprotease domain) family. Members of this family are
            membrane-anchored proteins structurally related to snake venom
            disintegrins, and have been implicated in a variety of biological
            processes involving cell-cell and cell-matrix interactions,
            including fertilization, muscle development, and neurogenesis. The
            protein encoded by this gene interacts with SH3 domain-containing
            proteins, binds mitotic arrest deficient 2 beta protein, and is
            also involved in TPA-induced ectodomain shedding of
            membrane-anchored heparin-binding EGF-like growth factor. Several
            alternatively spliced transcript variants have been identified for
            this gene. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) represents the protein coding
            transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.37167.1,
                                           SRR1660805.170969.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000487273.7/ ENSP00000419446.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.22"
     Protein         1..819
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 9 precursor"
                     /note="cone rod dystrophy 9; ADAM metallopeptidase domain
                     9 (meltrin gamma); disintegrin and metalloproteinase
                     domain-containing protein 9; myeloma cell
                     metalloproteinase; cellular disintegrin-related protein;
                     metalloprotease/disintegrin/cysteine-rich protein 9"
                     /calculated_mol_wt=87651
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2924
     mat_peptide     29..819
                     /product="disintegrin and metalloproteinase
                     domain-containing protein 9"
                     /calculated_mol_wt=87651
     Region          44..163
                     /region_name="Pep_M12B_propep"
                     /note="Reprolysin family propeptide; pfam01562"
                     /db_xref="CDD:460254"
     Site            56..57
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:Q61072;
                     propagated from UniProtKB/Swiss-Prot (Q13443.1)"
     Site            125
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Site            154
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Site            205..206
                     /site_type="cleavage"
                     /note="Cleavage, by furin-like protease.
                     /evidence=ECO:0000250|UniProtKB:Q61072; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Region          212..404
                     /region_name="ZnMc_adamalysin_II_like"
                     /note="Zinc-dependent metalloprotease; adamalysin_II_like
                     subfamily. Adamalysin II is a snake venom zinc
                     endopeptidase. This subfamily contains other snake venom
                     metalloproteinases, as well as membrane-anchored
                     metalloproteases belonging to the ADAM family; cd04269"
                     /db_xref="CDD:239797"
     Site            231
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Site            order(347..348,351,357)
                     /site_type="active"
                     /db_xref="CDD:239797"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Region          423..496
                     /region_name="Disintegrin"
                     /note="pfam00200"
                     /db_xref="CDD:459709"
     Site            487
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Region          500..636
                     /region_name="ACR"
                     /note="ADAM Cysteine-Rich Domain; smart00608"
                     /db_xref="CDD:214743"
     Site            698..718
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13443.1)"
     Region          734..763
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13443.1)"
     Site            758
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13443.1)"
     Region          780..819
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13443.1)"
     CDS             1..819
                     /gene="ADAM9"
                     /gene_synonym="CORD9; MCMP; MDC9; Mltng"
                     /coded_by="NM_003816.3:92..2551"
                     /db_xref="CCDS:CCDS6112.1"
                     /db_xref="GeneID:8754"
                     /db_xref="HGNC:HGNC:216"
                     /db_xref="MIM:602713"
ORIGIN      
        1 mgsgarfpsg tlrvrwllll glvgpvlgaa rpgfqqtshl ssyeiitpwr ltrerreapr
       61 pyskqvsyvi qaegkehiih lernkdllpe dfvvytynke gtlitdhpni qnhchyrgyv
      121 egvhnssial sdcfglrgll hlenasygie plqnsshfeh iiyrmddvyk eplkcgvsnk
      181 dieketakde eeeppsmtql lrrrravlpq tryvelfivv dkerydmmgr nqtavreemi
      241 llanyldsmy imlnirivlv gleiwtngnl inivggagdv lgnfvqwrek flitrrrhds
      301 aqlvlkkgfg gtagmafvgt vcsrshaggi nvfgqitvet fasivahelg hnlgmnhddg
      361 rdcscgaksc imnsgasgsr nfsscsaedf ekltlnkggn cllnipkpde aysapscgnk
      421 lvdageecdc gtpkeceldp ccegstcklk sfaecaygdc ckdcrflpgg tlcrgktsec
      481 dvpeycngss qfcqpdvfiq ngypcqnnka ycyngmcqyy daqcqvifgs kakaapkdcf
      541 ievnskgdrf gncgfsgney kkcatgnalc gklqcenvqe ipvfgivpai iqtpsrgtkc
      601 wgvdfqlgsd vpdpgmvneg tkcgagkicr nfqcvdasvl nydcdvqkkc hghgvcnsnk
      661 nchcengwap pncetkgygg svdsgptyne mntalrdgll vffflivpli vcaififikr
      721 dqlwrsyfrk krsqtyesdg knqanpsrqp gsvprhvspv tpprevpiya nrfavptyaa
      781 kqpqqfpsrp pppqpkvssq gnliparpap applysslt
//
LOCUS       NP_001339534             710 aa            linear   PRI 20-NOV-2025
DEFINITION  propionyl-CoA carboxylase alpha chain, mitochondrial isoform d
            precursor [Homo sapiens].
ACCESSION   NP_001339534 XP_016876097
VERSION     NP_001339534.1
DBSOURCE    REFSEQ: accession NM_001352605.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Wang,J., Cui,M., Liu,Y., Chen,M., Xu,J., Xia,J., Sun,J., Jiang,L.,
            Fang,W., Song,H. and Cheng,C.
  TITLE     The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival
  JOURNAL   Appl Environ Microbiol 90 (6), e0213523 (2024)
   PUBMED   38727222
  REMARK    GeneRIF: The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival.
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Bychkov,I., Galushkin,A., Filatova,A., Nekrasov,A., Kurkina,M.,
            Baydakova,G., Ilyushkina,A., Skoblov,M. and Zakharova,E.
  TITLE     Functional Analysis of the PCCA and PCCB Gene Variants Predicted to
            Affect Splicing
  JOURNAL   Int J Mol Sci 22 (8), 4154 (2021)
   PUBMED   33923806
  REMARK    GeneRIF: Functional Analysis of the PCCA and PCCB Gene Variants
            Predicted to Affect Splicing.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Kennerknecht,I., Klett,C. and Hameister,H.
  TITLE     Assignment of the human gene propionyl coenzyme A carboxylase,
            alpha-chain, (PCCA) to chromosome 13q32 by in situ hybridization
  JOURNAL   Genomics 14 (2), 550-551 (1992)
   PUBMED   1427880
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Lamhonwah,A.M., Mahuran,D. and Gravel,R.A.
  TITLE     Human mitochondrial propionyl-CoA carboxylase: localization of the
            N-terminus of the pro- and mature alpha chains in the deduced
            primary sequence of a full-length cDNA
  JOURNAL   Nucleic Acids Res 17 (11), 4396 (1989)
   PUBMED   2740237
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Lamhonwah,A.M., Quan,F. and Gravel,R.A.
  TITLE     Sequence homology around the biotin-binding site of human
            propionyl-CoA carboxylase and pyruvate carboxylase
  JOURNAL   Arch Biochem Biophys 254 (2), 631-636 (1987)
   PUBMED   3555348
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,
            Quan,F. and Gravel,R.A.
  TITLE     Isolation of cDNA clones coding for the alpha and beta chains of
            human propionyl-CoA carboxylase: chromosomal assignments and DNA
            polymorphisms associated with PCCA and PCCB genes
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4864-4868 (1986)
   PUBMED   3460076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355338.33, AL356575.8,
            AL353697.21 and AL136526.27.
            
            On Jun 18, 2017 this sequence version replaced XP_016876097.1.
            
            Summary: The protein encoded by this gene is the alpha subunit of
            the heterodimeric mitochondrial enzyme Propionyl-CoA carboxylase.
            PCCA encodes the biotin-binding region of this enzyme. Mutations in
            either PCCA or PCCB (encoding the beta subunit) lead to an enzyme
            deficiency resulting in propionic acidemia. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.164351.1,
                                           SRR1803612.58708.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..710
                     /product="propionyl-CoA carboxylase alpha chain,
                     mitochondrial isoform d precursor"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, alpha
                     polypeptide; propionyl-CoA carboxylase alpha chain,
                     mitochondrial; PCCase alpha subunit; propanoyl-CoA:carbon
                     dioxide ligase alpha subunit; pccA complementation group;
                     propionyl-CoA carboxylase alpha subunit; propionyl CoA
                     carboxylase, alpha polypeptide"
                     /calculated_mol_wt=78063
     Region          63..512
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          525..635
                     /region_name="PCC_BT"
                     /note="Propionyl-coenzyme A carboxylase BT domain;
                     pfam18140"
                     /db_xref="CDD:465666"
     Region          643..709
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(666,675..677,684)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            676
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..710
                     /gene="PCCA"
                     /coded_by="NM_001352605.2:29..2161"
                     /note="isoform d precursor is encoded by transcript
                     variant 4"
                     /db_xref="GeneID:5095"
                     /db_xref="HGNC:HGNC:8653"
                     /db_xref="MIM:232000"
ORIGIN      
        1 magfwvgtap lvaagrrgrw ppqqlmlsaa lrtlkhvlyy srqclmvsrn lgsvgydpne
       61 ktfdkilvan rgeiacrvir tckkmgiktv aihsdvdass vhvkmadeav cvgpaptsks
      121 ylnmdaimea ikktraqavh pgygflsenk efarclaaed vvfigpdtha iqamgdkies
      181 kllakkaevn tipgfdgvvk daeeavriar eigypvmika saggggkgmr iawddeetrd
      241 gfrlssqeaa ssfgddrlli ekfidnprhi eiqvlgdkhg nalwlnerec siqrrnqkvv
      301 eeapsiflda etrramgeqa valaravkys sagtveflvd skknfyflem ntrlqvehpv
      361 tecitgldlv qemirvakgy plrhkqadir ingwavecrv yaedpyksfg lpsigrlsqy
      421 qeplhlpgvr vdsgiqpgsd isiyydpmis klitygsdrt ealkrmadal dnyvirgvth
      481 niallrevii nsrfvkgdis tkflsdvypd gfkghmltks eknqllaias slfvafqlra
      541 qhfqensrmp vikpdianwe lsvklhdkvh tvvasnngsv fsvevdgskl nvtstwnlas
      601 pllsvsvdgt qrtvqykvni ltrlaaelnk fmlekvtedt ssvlrspmpg vvvavsvkpg
      661 davaegqeic vieamkmqns mtagktgtvk svhcqagdtv gegdllvele
//
LOCUS       NP_001274177            1042 aa            linear   PRI 20-NOV-2025
DEFINITION  recQ-like DNA helicase BLM isoform 3 [Homo sapiens].
ACCESSION   NP_001274177
VERSION     NP_001274177.1
DBSOURCE    REFSEQ: accession NM_001287248.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1042)
  AUTHORS   Silva,J.P.L., Donaires,F.S., Gutierrez-Rodrigues,F., Martins,D.J.,
            Carvalho,V.S., Santana,B.A., Cunha,R.L.G., Kajigaya,S.,
            Menck,C.F.M., Young,N.S., Kjeldsen,E. and Calado,R.T.
  TITLE     RecQ helicase expression in patients with telomeropathies
  JOURNAL   Mol Biol Rep 51 (1), 754 (2024)
   PUBMED   38874681
  REMARK    GeneRIF: RecQ helicase expression in patients with telomeropathies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1042)
  AUTHORS   Tsukada,K., Jones,S.E., Bannister,J., Durin,M.A., Vendrell,I.,
            Fawkes,M., Fischer,R., Kessler,B.M., Chapman,J.R. and
            Blackford,A.N.
  TITLE     BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint
            DNA molecule resolution
  JOURNAL   Mol Cell 84 (4), 640-658 (2024)
   PUBMED   38266639
  REMARK    GeneRIF: BLM and BRCA1-BARD1 coordinate complementary mechanisms of
            joint DNA molecule resolution.
REFERENCE   3  (residues 1 to 1042)
  AUTHORS   Liu,S., Atkinson,E., Paulucci-Holthauzen,A. and Wang,B.
  TITLE     A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism
            controlling BLM ubiquitination and G-quadruplex resolution
  JOURNAL   Nat Commun 14 (1), 6111 (2023)
   PUBMED   37777511
  REMARK    GeneRIF: A CK2 and SUMO-dependent, PML NB-involved regulatory
            mechanism controlling BLM ubiquitination and G-quadruplex
            resolution.
            Erratum:[Nat Commun. 2024 Feb 5;15(1):1077. doi:
            10.1038/s41467-024-45551-1. PMID: 38316763]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1042)
  AUTHORS   Danino,Y.M., Molitor,L., Rosenbaum-Cohen,T., Kaiser,S., Cohen,Y.,
            Porat,Z., Marmor-Kollet,H., Katina,C., Savidor,A., Rotkopf,R.,
            Ben-Isaac,E., Golani,O., Levin,Y., Monchaud,D., Hickson,I.D. and
            Hornstein,E.
  TITLE     BLM helicase protein negatively regulates stress granule formation
            through unwinding RNA G-quadruplex structures
  JOURNAL   Nucleic Acids Res 51 (17), 9369-9384 (2023)
   PUBMED   37503837
  REMARK    GeneRIF: BLM helicase protein negatively regulates stress granule
            formation through unwinding RNA G-quadruplex structures.
REFERENCE   5  (residues 1 to 1042)
  AUTHORS   Foucault,F., Vaury,C., Barakat,A., Thibout,D., Planchon,P.,
            Jaulin,C., Praz,F. and Amor-Gueret,M.
  TITLE     Characterization of a new BLM mutation associated with a
            topoisomerase II alpha defect in a patient with Bloom's syndrome
  JOURNAL   Hum Mol Genet 6 (9), 1427-1434 (1997)
   PUBMED   9285778
REFERENCE   6  (residues 1 to 1042)
  AUTHORS   Ellis,N.A., Groden,J., Ye,T.Z., Straughen,J., Lennon,D.J.,
            Ciocci,S., Proytcheva,M. and German,J.
  TITLE     The Bloom's syndrome gene product is homologous to RecQ helicases
  JOURNAL   Cell 83 (4), 655-666 (1995)
   PUBMED   7585968
REFERENCE   7  (residues 1 to 1042)
  AUTHORS   German,J., Roe,A.M., Leppert,M.F. and Ellis,N.A.
  TITLE     Bloom syndrome: an analysis of consanguineous families assigns the
            locus mutated to chromosome band 15q26.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6669-6673 (1994)
   PUBMED   8022833
REFERENCE   8  (residues 1 to 1042)
  AUTHORS   Langer,K., Cunniff,C.M. and Kucine,N.
  TITLE     Bloom Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301572
REFERENCE   9  (residues 1 to 1042)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   10 (residues 1 to 1042)
  AUTHORS   McDaniel,L.D. and Schultz,R.A.
  TITLE     Elevated sister chromatid exchange phenotype of Bloom syndrome
            cells is complemented by human chromosome 15
  JOURNAL   Proc Natl Acad Sci U S A 89 (17), 7968-7972 (1992)
   PUBMED   1518822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD707743.1, BC062697.1,
            BC143280.1, AC021422.25, DA122319.1, BC115032.1, DB520927.1 and
            AC124248.6.
            
            Summary: The Bloom syndrome is an autosomal recessive disorder
            characterized by growth deficiency, microcephaly and
            immunodeficiency among others. It is caused by homozygous or
            compound heterozygous mutation in the gene encoding DNA helicase
            RecQ protein on chromosome 15q26. This Bloom-associated helicase
            unwinds a variety of DNA substrates including Holliday junction,
            and is involved in several pathways contributing to the maintenance
            of genome stability. Identification of pathogenic Bloom variants is
            required for heterozygote testing in at-risk families. [provided by
            RefSeq, May 2020].
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in a 5' exon and uses a downstream translation start compared to
            variant 1. The resulting protein (isoform 3) is shorter and has a
            distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143280.1, SRR14038197.2689245.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1042
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..1042
                     /product="recQ-like DNA helicase BLM isoform 3"
                     /EC_number="5.6.2.4"
                     /note="bloom syndrome protein; recQ protein-like 3; Bloom
                     syndrome RecQ like helicase; DNA helicase, RecQ-like type
                     2; Bloom syndrome, RecQ helicase-like; recQ-like DNA
                     helicase BLM; DNA 3'-5' helicase BLM"
                     /calculated_mol_wt=116875
     Region          1..37
                     /region_name="BDHCT"
                     /note="BDHCT (NUC031) domain; pfam08072"
                     /db_xref="CDD:462356"
     Region          50..272
                     /region_name="BDHCT_assoc"
                     /note="BDHCT-box associated domain on Bloom syndrome
                     protein; pfam16204"
                     /db_xref="CDD:465065"
     Region          282..768
                     /region_name="recQ_fam"
                     /note="ATP-dependent DNA helicase, RecQ family; TIGR00614"
                     /db_xref="CDD:129701"
     Region          838..917
                     /region_name="HRDC"
                     /note="Helicase and RNase D C-terminal; smart00341"
                     /db_xref="CDD:128635"
     CDS             1..1042
                     /gene="BLM"
                     /gene_synonym="BS; MGRISCE1; RECQ2; RECQL2; RECQL3"
                     /coded_by="NM_001287248.2:1391..4519"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:641"
                     /db_xref="HGNC:HGNC:1058"
                     /db_xref="MIM:604610"
ORIGIN      
        1 mehicklidt ipddklklld cgnellqqrn irrklltevd fnksdasllg slwryrpdsl
       61 dgpmegdscp tgnsmkelnf shlpsnsvsp gdclltttlg ktgfsatrkn lferplfnth
      121 lqksfvssnw aetprlgkkn essyfpgnvl tstavkdqnk htasindler etqpsydidn
      181 fdiddfdddd dwedimhnla asksstaayq pikegrpiks vserlssakt dclpvsstaq
      241 ninfsesiqn ytdksaqnla srnlkherfq slsfphtkem mkifhkkfgl hnfrtnqlea
      301 inaallgedc filmptgggk slcyqlpacv spgvtvvisp lrslivdqvq kltsldipat
      361 yltgdktdse atniylqlsk kdpiikllyv tpekicasnr listlenlye rkllarfvid
      421 eahcvsqwgh dfrqdykrmn mlrqkfpsvp vmaltatanp rvqkdiltql kilrpqvfsm
      481 sfnrhnlkyy vlpkkpkkva fdclewirkh hpydsgiiyc lsrrecdtma dtlqrdglaa
      541 layhaglsds ardevqqkwi nqdgcqvica tiafgmgidk pdvrfvihas lpksvegyyq
      601 esgragrdge ishcllfyty hdvtrlkrli mmekdgnhht rethfnnlys mvhycenite
      661 crriqllayf gengfnpdfc kkhpdvscdn ccktkdyktr dvtddvksiv rfvqehsssq
      721 gmrnikhvgp sgrftmnmlv diflgsksak iqsgifgkgs aysrhnaerl fkklildkil
      781 dedlyinand qaiayvmlgn kaqtvlngnl kvdfmetens ssvkkqkalv akvsqreemv
      841 kkclgeltev ckslgkvfgv hyfnifntvt lkklaeslss dpevllqidg vtedklekyg
      901 aevisvlqky sewtspaeds spgislsssr gpgrsaaeel deeipvsshy fasktrnerk
      961 rkkmpasqrs krrktassgs kakggsatcr kissktksss iigsssasht sqatsgansk
     1021 lgimappkpi nrpflkpsya fs
//
LOCUS       NP_001185923             591 aa            linear   PRI 20-NOV-2025
DEFINITION  NAD kinase isoform 2 [Homo sapiens].
ACCESSION   NP_001185923
VERSION     NP_001185923.1
DBSOURCE    REFSEQ: accession NM_001198994.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Praharaj,P.P., Li,Y., Mary,C., Soflaee,M.H., Ryu,K., Kim,D.,
            Tran,D.H., Dey,T., Tom,H.J., Rion,H., Gelin,M., Lemoff,A.,
            Zacharias,L.G., Patricio,J.S., Mathews,T.P., Chen,Z., Lionne,C.,
            Hoxhaj,G. and Labesse,G.
  TITLE     Cryo-EM structure and regulation of human NAD kinase
  JOURNAL   Sci Adv 11 (4), eads2664 (2025)
   PUBMED   39854463
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Meng,X., Peng,F., Yu,S., Chi,X., Wang,W. and Shao,S.
  TITLE     Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1 axis
  JOURNAL   J Cancer Res Clin Oncol 150 (5), 228 (2024)
   PUBMED   38700533
  REMARK    GeneRIF: Knockdown of NADK promotes LUAD ferroptosis via NADPH/FSP1
            axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Wu,T., Ding,K., Wang,C., Lin,G., Xie,C., Chen,X., Li,Q., Yu,F.,
            Mao,Y., Hong,W., Lu,L. and Li,S.
  TITLE     G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation
  JOURNAL   FASEB J 38 (3), e23449 (2024)
   PUBMED   38315451
  REMARK    GeneRIF: G-protein-coupled estrogen receptor 1 promotes peritoneal
            metastasis of gastric cancer through nicotinamide adenine
            dinucleotide kinase 1-mediated redox modulation.
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Magni,G., Amici,A., Emanuelli,M., Orsomando,G., Raffaelli,N. and
            Ruggieri,S.
  TITLE     Enzymology of NAD+ homeostasis in man
  JOURNAL   Cell Mol Life Sci 61 (1), 19-34 (2004)
   PUBMED   14704851
  REMARK    Review article
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Lerner,F., Niere,M., Ludwig,A. and Ziegler,M.
  TITLE     Structural and functional characterization of human NAD kinase
  JOURNAL   Biochem Biophys Res Commun 288 (1), 69-74 (2001)
   PUBMED   11594753
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF250320.1, BC001709.1, AL031282.1 and BM842058.1.
            
            Summary: NADK catalyzes the transfer of a phosphate group from ATP
            to NAD to generate NADP, which in its reduced form acts as an
            electron donor for biosynthetic reactions (Lerner et al., 2001
            [PubMed 11594753]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and CDS
            compared to variant 1. The resulting isoform (2) has two additional
            internal segments, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF250320.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2467144
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..591
                     /product="NAD kinase isoform 2"
                     /EC_number="2.7.1.23"
                     /note="poly(P)/ATP NAD kinase"
                     /calculated_mol_wt=63325
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95544.1)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95544.1)"
     Region          <200..578
                     /region_name="pnk"
                     /note="bifunctional NADP phosphatase/NAD kinase; cl28462"
                     /db_xref="CDD:333282"
     CDS             1..591
                     /gene="NADK"
                     /gene_synonym="dJ283E3.1; NADK1"
                     /coded_by="NM_001198994.2:168..1943"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55562.1"
                     /db_xref="GeneID:65220"
                     /db_xref="HGNC:HGNC:29831"
                     /db_xref="MIM:611616"
ORIGIN      
        1 memeqekmtm nkelspdaaa yccsachgde twsynhpirg raksrslsas palgstkefr
       61 rtrslhgpcp vttfgpkacv lqnpqtiiat plslasqllp spavshsgqg gvtgqvhvlp
      121 qpsdqgvlsg praargqtap qeeavtqeev ealvcghtqr wvpgpvydaa aggsgwaqls
      181 lragmgvgqa tghiqdpasq rltwnkspks vlvikkmrda sllqpfkelc thlmeargag
      241 gkgawgahgv ggasihitap rvgsaggmsr lalcfqenmi vyvekkvled paiasdesfg
      301 avkkkfctfr edyddisnqi dfiiclggdg tllyasslfq gsvppvmafh lgslgfltpf
      361 sfenfqsqvt qviegnaavv lrsrlkvrvv kelrgkktav hnglgengsq aagldmdvgk
      421 qamqyqvlne vvidrgpssy lsnvdvyldg hlittvqgdg vivstptgst ayaaaagasm
      481 ihpnvpaimi tpicphslsf rpivvpagve lkimlspear ntawvsfdgr krqeirhgds
      541 isittscypl psicvrdpvs dwfeslaqcl hwnvrkkqah feeeeeeeee g
//
LOCUS       NP_000535                703 aa            linear   PRI 20-NOV-2025
DEFINITION  antigen peptide transporter 2 isoform 1 [Homo sapiens].
ACCESSION   NP_000535
VERSION     NP_000535.3
DBSOURCE    REFSEQ: accession NM_000544.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 703)
  AUTHORS   Lee,J., Oldham,M.L., Manon,V. and Chen,J.
  TITLE     Principles of peptide selection by the transporter associated with
            antigen processing
  JOURNAL   Proc Natl Acad Sci U S A 121 (23), e2320879121 (2024)
   PUBMED   38805290
REFERENCE   2  (residues 1 to 703)
  AUTHORS   Kim,K., Oh,S.J., Lee,J., Kwon,A., Yu,C.Y., Kim,S., Choi,C.H.,
            Kang,S.B., Kim,T.O., Park,D.I. and Lee,C.K.
  TITLE     Regulatory Variants on the Leukocyte Immunoglobulin-Like Receptor
            Gene Cluster are Associated with Crohn's Disease and Interact with
            Regulatory Variants for TAP2
  JOURNAL   J Crohns Colitis 18 (1), 47-53 (2024)
   PUBMED   37523193
  REMARK    GeneRIF: Regulatory Variants on the Leukocyte Immunoglobulin-Like
            Receptor Gene Cluster are Associated with Crohn's Disease and
            Interact with Regulatory Variants for TAP2.
REFERENCE   3  (residues 1 to 703)
  AUTHORS   Darazam,I.A., Hakamifard,A., Momenilandi,M., Materna,M.,
            Gharehbagh,F.J., Shahrooei,M., Olyaei,N.A., Zerehpoosh,F.B.,
            Fayand,A., Hatami,F., Lotfollahi,L., Mansouri,N., Casanova,J.L.,
            Beziat,V. and Mansouri,D.
  TITLE     Delayed Diagnosis of Chronic Necrotizing Granulomatous Skin Lesions
            due to TAP2 Deficiency
  JOURNAL   J Clin Immunol 43 (1), 217-228 (2023)
   PUBMED   36227411
  REMARK    GeneRIF: Delayed Diagnosis of Chronic Necrotizing Granulomatous
            Skin Lesions due to TAP2 Deficiency.
REFERENCE   4  (residues 1 to 703)
  AUTHORS   Muller,I.K., Winter,C., Thomas,C., Spaapen,R.M., Trowitzsch,S. and
            Tampe,R.
  TITLE     Structure of an MHC I-tapasin-ERp57 editing complex defines
            chaperone promiscuity
  JOURNAL   Nat Commun 13 (1), 5383 (2022)
   PUBMED   36104323
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 703)
  AUTHORS   Tao,Y., Han,X., Liu,N., Shi,L., Shi,L., Liu,S. and Yao,Y.
  TITLE     Association study of TAP and HLA-I gene combination with chronic
            hepatitis C virus infection in a Han population in China
  JOURNAL   Int J Immunogenet 49 (3), 169-180 (2022)
   PUBMED   35485366
  REMARK    GeneRIF: Association study of TAP and HLA-I gene combination with
            chronic hepatitis C virus infection in a Han population in China.
REFERENCE   6  (residues 1 to 703)
  AUTHORS   Beck,S., Kelly,A., Radley,E., Khurshid,F., Alderton,R.P. and
            Trowsdale,J.
  TITLE     DNA sequence analysis of 66 kb of the human MHC class II region
            encoding a cluster of genes for antigen processing
  JOURNAL   J Mol Biol 228 (2), 433-441 (1992)
   PUBMED   1453454
REFERENCE   7  (residues 1 to 703)
  AUTHORS   Colonna,M., Bresnahan,M., Bahram,S., Strominger,J.L. and Spies,T.
  TITLE     Allelic variants of the human putative peptide transporter involved
            in antigen processing
  JOURNAL   Proc Natl Acad Sci U S A 89 (9), 3932-3936 (1992)
   PUBMED   1570316
REFERENCE   8  (residues 1 to 703)
  AUTHORS   Bodmer,J.G., Marsh,S.G., Albert,E.D., Bodmer,W.F., Dupont,B.,
            Erlich,H.A., Mach,B., Mayr,W.R., Parham,P., Sasazuki,T. et al.
  TITLE     Nomenclature for factors of the HLA system, 1991. WHO Nomenclature
            Committee for factors of the HLA system
  JOURNAL   Tissue Antigens 39 (4), 161-173 (1992)
   PUBMED   1529427
  REMARK    Erratum:[Tissue Antigens. 1992 Nov;40(5):229-43. doi:
            10.1111/j.1399-0039.1992.tb02050.x. PMID: 1362295]
REFERENCE   9  (residues 1 to 703)
  AUTHORS   Powis,S.H., Mockridge,I., Kelly,A., Kerr,L.A., Glynne,R.,
            Gileadi,U., Beck,S. and Trowsdale,J.
  TITLE     Polymorphism in a second ABC transporter gene located within the
            class II region of the human major histocompatibility complex
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1463-1467 (1992)
   PUBMED   1741401
REFERENCE   10 (residues 1 to 703)
  AUTHORS   Kelly,A., Powis,S.H., Kerr,L.A., Mockridge,I., Elliott,T.,
            Bastin,J., Uchanska-Ziegler,B., Ziegler,A., Trowsdale,J. and
            Townsend,A.
  TITLE     Assembly and function of the two ABC transporter proteins encoded
            in the human major histocompatibility complex
  JOURNAL   Nature 355 (6361), 641-644 (1992)
   PUBMED   1538751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG423357.1, BC002751.2,
            Z22935.1 and AL669918.5.
            
            On Aug 24, 2005 this sequence version replaced NP_000535.2.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the MDR/TAP subfamily. Members
            of the MDR/TAP subfamily are involved in multidrug resistance. This
            gene is located 7 kb telomeric to gene family member ABCB2. The
            protein encoded by this gene is involved in antigen presentation.
            This protein forms a heterodimer with ABCB2 in order to transport
            peptides from the cytoplasm to the endoplasmic reticulum. Mutations
            in this gene may be associated with ankylosing spondylitis,
            insulin-dependent diabetes mellitus, and celiac disease.
            Alternative splicing of this gene produces products which differ in
            peptide selectivity and level of restoration of surface expression
            of MHC class I molecules. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (1, B allele) represents the
            longer transcript and encodes the longest isoform (1). An allele
            (variant 1, A allele) exists in which a single nt change creates an
            internal stop codon, leading to a protein that is 17 aa shorter at
            the C-terminus.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M84748.1, Z22936.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..703
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..703
                     /product="antigen peptide transporter 2 isoform 1"
                     /EC_number="7.4.2.14"
                     /note="antigen peptide transporter 2; peptide supply
                     factor 2; peptide transporter PSF2; ABC transporter, MHC
                     2; ATP-binding cassette, sub-family B (MDR/TAP), member 3;
                     transporter 2, ABC (ATP binding cassette); really
                     interesting new gene 11 protein; peptide transporter
                     involved in antigen processing 2; transporter 2,
                     ATP-binding cassette, sub-family B (MDR/TAP)"
                     /calculated_mol_wt=77564
     Region          1..697
                     /region_name="3a01208"
                     /note="Conjugate Transporter-2 (CT2) Family protein;
                     TIGR00958"
                     /db_xref="CDD:273363"
     mat_peptide     1..686
                     /product="Antigen peptide transporter 2.
                     /id=PRO_0000093329"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
                     /calculated_mol_wt=75634
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            16
                     /site_type="other"
                     /note="Inter-subunit salt bridge with TAPBP.
                     /evidence=ECO:0000269|PubMed:26611325; propagated from
                     UniProtKB/Swiss-Prot (Q03519.1)"
     Site            57..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            267..287
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            294..314
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Region          301..389
                     /region_name="Part of the peptide-binding site.
                     /evidence=ECO:0000269|PubMed:8955196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            375..395
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Site            409..429
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     Region          414..433
                     /region_name="Part of the peptide-binding site.
                     /evidence=ECO:0000269|PubMed:8955196"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03519.1)"
     CDS             1..703
                     /gene="TAP2"
                     /gene_synonym="ABC18; ABCB3; APT2; D6S217E; MHC1D2; PSF-2;
                     PSF2; RING11"
                     /coded_by="NM_000544.3:123..2234"
                     /note="isoform 1 is encoded by transcript variant 1, B
                     allele"
                     /db_xref="GeneID:6891"
                     /db_xref="HGNC:HGNC:44"
                     /db_xref="MIM:170261"
ORIGIN      
        1 mrlpdlrpwt slllvdaall wllqgplgtl lpqglpglwl egtlrlgglw gllklrgllg
       61 fvgtlllplc latpltvslr alvagasrap parvasapws wllvgygaag lswslwavls
      121 ppgaqekeqd qvnnkvlmwr llklsrpdlp llvaaffflv lavlgetlip hysgrvidil
      181 ggdfdphafa saiffmclfs fgsslsagcr ggcftytmsr inlrireqlf ssllrqdlgf
      241 fqetktgeln srlssdttlm snwlplnanv llrslvkvvg lygfmlsisp rltllsllhm
      301 pftiaaekvy ntrhqevlre iqdavaragq vvreavgglq tvrsfgaeeh evcrykeale
      361 qcrqlywrrd leralyllvr rvlhlgvqml mlscglqqmq dgeltqgsll sfmiyqesvg
      421 syvqtlvyiy gdmlsnvgaa ekvfsymdrq pnlpspgtla pttlqgvvkf qdvsfaypnr
      481 pdrpvlkglt ftlrpgevta lvgpngsgks tvaallqnly qptggqvlld ekpisqyehc
      541 ylhsqvvsvg qepvlfsgsv rnniayglqs ceddkvmaaa qaahaddfiq emehgiytdv
      601 gekgsqlaag qkqrlaiara lvrdprvlil deatsaldvq ceqalqdwns rgdrtvlvia
      661 hrlqavqrah qilvlqegkl qklaqlqegq dlysrlvqqr lmd
//
LOCUS       NP_056513                476 aa            linear   PRI 20-NOV-2025
DEFINITION  G-patch domain and KOW motifs-containing protein [Homo sapiens].
ACCESSION   NP_056513
VERSION     NP_056513.2
DBSOURCE    REFSEQ: accession NM_015698.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Aksaas,A.K., Larsen,A.C., Rogne,M., Rosendal,K., Kvissel,A.K. and
            Skalhegg,B.S.
  TITLE     G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear
            RNA-binding protein regulated by protein kinase A
  JOURNAL   J Mol Signal 6, 10 (2011)
   PUBMED   21880142
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Glesne,D. and Huberman,E.
  TITLE     Smad6 is a protein kinase X phosphorylation substrate and is
            required for HL-60 cell differentiation
  JOURNAL   Oncogene 25 (29), 4086-4098 (2006)
   PUBMED   16491121
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Schindelhauer,D., Hellebrand,H., Grimm,L., Bader,I., Meitinger,T.,
            Wehnert,M., Ross,M. and Meindl,A.
  TITLE     Long-range map of a 3.5-Mb region in Xp11.23-22 with a
            sequence-ready map from a 1.1-Mb gene-rich interval
  JOURNAL   Genome Res 6 (11), 1056-1069 (1996)
   PUBMED   8938429
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE795098.1 and BC003148.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2001 this sequence version replaced NP_056513.1.
            
            Summary: This gene encodes a putative RNA-binding protein
            containing G-patch and KOW (Kyprides, Ouzounis, Woese) domains. The
            encoded protein interacts directly with protein kinase A and
            protein kinase X and is also found associated with the spliceosome.
            [provided by RefSeq, Aug 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000397.2, AB209806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000156109.7/ ENSP00000156109.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..476
                     /product="G-patch domain and KOW motifs-containing
                     protein"
                     /note="G patch domain and KOW motifs-containing protein;
                     protein MOS2 homolog"
                     /calculated_mol_wt=52098
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92917.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:21880142; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92917.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Region          154..208
                     /region_name="G-patch_2"
                     /note="G-patch domain; pfam12656"
                     /db_xref="CDD:432700"
     Region          203..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92917.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Region          244..300
                     /region_name="KOW_GPKOW_A"
                     /note="KOW motif of the 'G-patch domain and KOW
                     motifs-containing protein' (GPKOW) repeat A; cd13152"
                     /db_xref="CDD:240516"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKA.
                     /evidence=ECO:0000269|PubMed:21880142; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Region          327..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92917.2)"
     Region          419..469
                     /region_name="KOW_GPKOW_B"
                     /note="KOW motif of the 'G-patch domain and KOW
                     motifs-containing protein' (GPKOW) repeat B; cd13153"
                     /db_xref="CDD:240517"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     Site            473
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92917.2)"
     CDS             1..476
                     /gene="GPKOW"
                     /gene_synonym="GPATC5; GPATCH5; Mos2; Spp2; T54"
                     /coded_by="NM_015698.6:14..1444"
                     /db_xref="CCDS:CCDS35251.1"
                     /db_xref="GeneID:27238"
                     /db_xref="HGNC:HGNC:30677"
                     /db_xref="MIM:301003"
ORIGIN      
        1 madskegvlp ltaastapis fgftrtsarr rladsgdgag pspeekdflk tvegrelqsv
       61 kpqeapkelv ipliqnghrr qpparppgps tdtgaladgv vsqavkelia eskksleere
      121 nagvdptlai pmiqkgctps gegadsepra etvpeeanye avpveaygla mlrgmgwkpg
      181 egigrtfnqv vkprvnslrp kglglganlt eaqaltptgp srmprpdeeq ekdkedqpqg
      241 lvpggavvvl sgphrglygk vegldpdnvr amvrlavgsr vvtvseyylr pvsqqefdkn
      301 tldlrqqngt assrktlwnq elyiqqdnse rkrkhlpdrq dgpaakseka aprsqhwlhr
      361 dlrvrfvdnm ykggqyyntk miiedvlspd tcvcrtdegr vleglredml etlvpkaegd
      421 rvmvvlgpqt grvghllsrd rarsralvql prenqvvelh ydaicqymgp sdtddd
//
LOCUS       NP_076955                102 aa            linear   PRI 20-NOV-2025
DEFINITION  DET1- and DDB1-associated protein 1 [Homo sapiens].
ACCESSION   NP_076955
VERSION     NP_076955.1
DBSOURCE    REFSEQ: accession NM_024050.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 102)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 102)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 102)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 102)
  AUTHORS   Faust,T.B., Yoon,H., Nowak,R.P., Donovan,K.A., Li,Z., Cai,Q.,
            Eleuteri,N.A., Zhang,T., Gray,N.S. and Fischer,E.S.
  TITLE     Structural complementarity facilitates E7820-mediated degradation
            of RBM39 by DCAF15
  JOURNAL   Nat Chem Biol 16 (1), 7-14 (2020)
   PUBMED   31686031
REFERENCE   5  (residues 1 to 102)
  AUTHORS   Ting,T.C., Goralski,M., Klein,K., Wang,B., Kim,J., Xie,Y. and
            Nijhawan,D.
  TITLE     Aryl Sulfonamides Degrade RBM39 and RBM23 by Recruitment to
            CRL4-DCAF15
  JOURNAL   Cell Rep 29 (6), 1499-1510 (2019)
   PUBMED   31693891
REFERENCE   6  (residues 1 to 102)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   7  (residues 1 to 102)
  AUTHORS   Olma,M.H., Roy,M., Le Bihan,T., Sumara,I., Maerki,S., Larsen,B.,
            Quadroni,M., Peter,M., Tyers,M. and Pintard,L.
  TITLE     An interaction network of the mammalian COP9 signalosome identifies
            Dda1 as a core subunit of multiple Cul4-based E3 ligases
  JOURNAL   J Cell Sci 122 (Pt 7), 1035-1044 (2009)
   PUBMED   19295130
  REMARK    GeneRIF: Cells depleted of Dda1 spontaneously accumulated
            double-stranded DNA breaks in a similar way to Cul4A-, Cul4B- or
            Wdr23-depleted cells, indicating that Dda1 interacts physically and
            functionally with cullin-RING E3 ligases complexes.
REFERENCE   8  (residues 1 to 102)
  AUTHORS   Pick,E., Lau,O.S., Tsuge,T., Menon,S., Tong,Y., Dohmae,N.,
            Plafker,S.M., Deng,X.W. and Wei,N.
  TITLE     Mammalian DET1 regulates Cul4A activity and forms stable complexes
            with E2 ubiquitin-conjugating enzymes
  JOURNAL   Mol Cell Biol 27 (13), 4708-4719 (2007)
   PUBMED   17452440
REFERENCE   9  (residues 1 to 102)
  AUTHORS   Li,Z.M., Wen,Y.J., Lai,S.T., Ni,R., Deng,H.X., Kan,B., Li,J.,
            Liu,J., Jing,X.M., Cheng,P., Shi,W. and Jia,Y.X.
  TITLE     [Searching for genes interacting with human PCIA1 gene by using the
            bacterial two-hybrid system]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 24 (3), 279-283 (2007)
   PUBMED   17557237
  REMARK    GeneRIF: PCIA1 gene expression correlates with tumor formation,
            invasion and metastasis
REFERENCE   10 (residues 1 to 102)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC000615.2 and AC010463.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic and transcript sequence to make the sequence consistent
            with the reference genome assembly. The extent of this transcript
            is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.14282.1,
                                           SRR1163657.15470.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359866.9/ ENSP00000352928.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..102
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..102
                     /product="DET1- and DDB1-associated protein 1"
                     /note="cross-immune reaction antigen PCIA1; placenta
                     cross-immune reaction antigen 1"
                     /calculated_mol_wt=11704
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BW61.1)"
     Region          3..65
                     /region_name="DDA1"
                     /note="Det1 complexing ubiquitin ligase; pfam10172"
                     /db_xref="CDD:401980"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BW61.1)"
     Region          66..102
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW61.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BW61.1)"
     CDS             1..102
                     /gene="DDA1"
                     /gene_synonym="C19orf58; PCIA1"
                     /coded_by="NM_024050.6:93..401"
                     /db_xref="CCDS:CCDS12357.1"
                     /db_xref="GeneID:79016"
                     /db_xref="HGNC:HGNC:28360"
ORIGIN      
        1 madflkglpv ynksnfsrfh adsvckasnr rpsvylptre ypseqiivte ktnillrylh
       61 qqwdkknaak krdqeqvele gessapprkv artdspdmhe dt
//
LOCUS       NP_001008212             577 aa            linear   PRI 20-NOV-2025
DEFINITION  optineurin [Homo sapiens].
ACCESSION   NP_001008212
VERSION     NP_001008212.1
DBSOURCE    REFSEQ: accession NM_001008211.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Nan,H., Kim,Y.J., Chu,M., Li,D., Li,J., Jiang,D., Wu,Y., Ohtsuka,T.
            and Wu,L.
  TITLE     Genetic and clinical landscape of Chinese frontotemporal dementia:
            dominance of TBK1 and OPTN mutations
  JOURNAL   Alzheimers Res Ther 16 (1), 127 (2024)
   PUBMED   38872230
  REMARK    GeneRIF: Genetic and clinical landscape of Chinese frontotemporal
            dementia: dominance of TBK1 and OPTN mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Jin,J., Huang,R., Chang,Y. and Yi,X.
  TITLE     Roles and mechanisms of optineurin in bone metabolism
  JOURNAL   Biomed Pharmacother 172, 116258 (2024)
   PUBMED   38350370
  REMARK    GeneRIF: Roles and mechanisms of optineurin in bone metabolism.
            Review article
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Yamano,K., Sawada,M., Kikuchi,R., Nagataki,K., Kojima,W., Endo,R.,
            Kinefuchi,H., Sugihara,A., Fujino,T., Watanabe,A., Tanaka,K.,
            Hayashi,G., Murakami,H. and Matsuda,N.
  TITLE     Optineurin provides a mitophagy contact site for TBK1 activation
  JOURNAL   EMBO J 43 (5), 754-779 (2024)
   PUBMED   38287189
  REMARK    GeneRIF: Optineurin provides a mitophagy contact site for TBK1
            activation.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   D'Urso,B., Weil,R. and Genin,P.
  TITLE     [Optineurin and mitochondrial dysfunction in neurodegeneration]
  JOURNAL   Med Sci (Paris) 40 (2), 167-175 (2024)
   PUBMED   38411425
  REMARK    GeneRIF: [Optineurin and mitochondrial dysfunction in
            neurodegeneration].
            Review article
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Fong,K.S. and de Couet,H.G.
  TITLE     Novel proteins interacting with the leucine-rich repeat domain of
            human flightless-I identified by the yeast two-hybrid system
  JOURNAL   Genomics 58 (2), 146-157 (1999)
   PUBMED   10366446
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Sarfarazi,M., Child,A., Stoilova,D., Brice,G., Desai,T.,
            Trifan,O.C., Poinoosawmy,D. and Crick,R.P.
  TITLE     Localization of the fourth locus (GLC1E) for adult-onset primary
            open-angle glaucoma to the 10p15-p14 region
  JOURNAL   Am J Hum Genet 62 (3), 641-652 (1998)
   PUBMED   9497264
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Li,Y., Kang,J. and Horwitz,M.S.
  TITLE     Interaction of an adenovirus E3 14.7-kilodalton protein with a
            novel tumor necrosis factor alpha-inducible cellular protein
            containing leucine zipper domains
  JOURNAL   Mol Cell Biol 18 (3), 1601-1610 (1998)
   PUBMED   9488477
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552635.1, AF420371.1 and
            AF070533.1.
            
            Summary: This gene encodes the coiled-coil containing protein
            optineurin. Optineurin may play a role in normal-tension glaucoma
            and adult-onset primary open angle glaucoma. Optineurin interacts
            with adenovirus E3-14.7K protein and may utilize tumor necrosis
            factor-alpha or Fas-ligand pathways to mediate apoptosis,
            inflammation or vasoconstriction. Optineurin may also function in
            cellular morphogenesis and membrane trafficking, vesicle
            trafficking, and transcription activation through its interactions
            with the RAB8, huntingtin, and transcription factor IIIA proteins.
            Alternative splicing results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, 3, and 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.172907.1,
                                           SRR1803612.206278.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..577
                     /product="optineurin"
                     /note="nemo-related protein; tumor necrosis factor
                     alpha-inducible cellular protein containing leucine zipper
                     domains; transcrption factor IIIA-interacting protein;
                     Huntingtin interacting protein L; FIP-2; HIP-7; huntingtin
                     yeast partner L; E3-14.7K-interacting protein;
                     huntingtin-interacting protein 7; huntingtin-interacting
                     protein L; optic neuropathy-inducing protein;
                     transcription factor IIIA-interacting protein"
                     /calculated_mol_wt=65791
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          37..103
                     /region_name="NEMO"
                     /note="NF-kappa-B essential modulator NEMO; pfam11577"
                     /db_xref="CDD:431942"
     Region          58..209
                     /region_name="Interaction with Rab8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          101..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          176..181
                     /region_name="LIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21617041,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          186..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          245..>520
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          261..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          408..507
                     /region_name="CC2-LZ"
                     /note="Leucine zipper of domain CC2 of NEMO, NF-kappa-B
                     essential modulator; pfam16516"
                     /db_xref="CDD:465155"
     Region          411..577
                     /region_name="Interaction with HD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          412..520
                     /region_name="Interaction with MYO6.
                     /evidence=ECO:0000269|PubMed:15837803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          474..479
                     /region_name="UBAN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          551..576
                     /region_name="zf_C2H2_10"
                     /note="C2H2 type zinc-finger; pfam18414"
                     /db_xref="CDD:436483"
     CDS             1..577
                     /gene="OPTN"
                     /gene_synonym="ALS12; FIP2; GLC1E; HIP7; HYPL; NRP;
                     TFIIIA-INTP"
                     /coded_by="NM_001008211.1:454..2187"
                     /db_xref="CCDS:CCDS7094.1"
                     /db_xref="GeneID:10133"
                     /db_xref="HGNC:HGNC:17142"
                     /db_xref="MIM:602432"
ORIGIN      
        1 mshqplsclt ekedspsest gngpphlahp nldtftpeel lqqmkellte nhqlkeamkl
       61 nnqamkgrfe elsawtekqk eerqffeiqs keakerlmal sheneklkee lgklkgkser
      121 ssedptddsr lpraeaeqek dqlrtqvvrl qaekadllgi vselqlklns sgssedsfve
      181 irmaegeaeg svkeikhspg ptrtvstgta lskyrsrsad gaknyfehee ltvsqlllcl
      241 regnqkverl evalkeaker vsdfekktsn rseietqteg stekendeek gpetvgseve
      301 alnlqvtslf kelqeahtkl seaelmkkrl qekcqalerk nsaipselne kqelvytnkk
      361 lelqvesmls eikmeqakte dekskltvlq mthnkllqeh nnalktieel trkesekvdr
      421 avlkelsekl elaekalask qlqmdemkqt iakqeedlet mtilraqmev ycsdfhaera
      481 arekiheeke qlalqlavll kendafedgg rqslmemqsr hgartsdsdq qaylvqrgae
      541 drdwrqqrni pihscpkcge vlpdidtlqi hvmdcii
//
LOCUS       NP_001354678             284 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform h [Homo sapiens].
ACCESSION   NP_001354678
VERSION     NP_001354678.1
DBSOURCE    REFSEQ: accession NM_001367749.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (33), as well as variants 34 and
            35, encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.231851.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153733, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..284
                     /product="rab5 GDP/GTP exchange factor isoform h"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=32557
     Region          63..163
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..284
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367749.1:87..941"
                     /note="isoform h is encoded by transcript variant 33"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mdqiekyimt rlykyvfcpe ttddekkdla iqkriralrw vtpqmlcvpv nedipevsdm
       61 vvkaitdiie mdskrvprdk lacitkcskh ifnaikitkn epasaddflp tliyivlkgn
      121 pprlqsniqy itrfcnpsrl mtgedgyyft nlccavafie kldaqslnls qedfdrymsg
      181 qtsprkqeae swspdaclgv kqmyknldll sqlnerqeri mneakklekd lidwtdgiar
      241 evqdivekyp leikppnqpl aaidsenven dklppplqpq vyag
//
LOCUS       NP_001123617             504 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional coactivator YAP1 isoform 1 [Homo sapiens].
ACCESSION   NP_001123617
VERSION     NP_001123617.1
DBSOURCE    REFSEQ: accession NM_001130145.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Tang,W., Yang,Y., Fu,Z., Xu,W., Ou,W., Liu,F., Du,P. and Liu,C.Y.
  TITLE     The RNA helicase DDX21 activates YAP to promote tumorigenesis and
            is transcriptionally upregulated by beta-catenin in colorectal
            cancer
  JOURNAL   Oncogene 43 (44), 3227-3239 (2024)
   PUBMED   39285230
  REMARK    GeneRIF: The RNA helicase DDX21 activates YAP to promote
            tumorigenesis and is transcriptionally upregulated by beta-catenin
            in colorectal cancer.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   He,C., Lv,X., Liu,J., Ruan,J., Chen,P., Huang,C., Angeletti,P.C.,
            Hua,G., Moness,M.L., Shi,D., Dhar,A., Yang,S., Murphy,S.,
            Montoute,I., Chen,X., Islam,K.N., George,S., Ince,T.A., Drapkin,R.,
            Guda,C., Davis,J.S. and Wang,C.
  TITLE     HPV-YAP1 oncogenic alliance drives malignant transformation of
            fallopian tube epithelial cells
  JOURNAL   EMBO Rep 25 (10), 4542-4569 (2024)
   PUBMED   39271776
  REMARK    GeneRIF: HPV-YAP1 oncogenic alliance drives malignant
            transformation of fallopian tube epithelial cells.
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Meyer,N.P., Singh,T., Kutys,M.L., Nystul,T.G. and Barber,D.L.
  TITLE     Arp2/3 complex activity enables nuclear YAP for naive pluripotency
            of human embryonic stem cells
  JOURNAL   Elife 13, e89725 (2024)
   PUBMED   39319536
  REMARK    GeneRIF: Arp2/3 complex activity enables nuclear YAP for naive
            pluripotency of human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Jimbo,N., Ohbayashi,C., Fujii,T., Takeda,M., Mitsui,S., Tanaka,Y.,
            Itoh,T. and Maniwa,Y.
  TITLE     The expression of YAP1 and other transcription factors contributes
            to lineage plasticity in combined small cell lung carcinoma
  JOURNAL   J Pathol Clin Res 10 (5), e70001 (2024)
   PUBMED   39283755
  REMARK    GeneRIF: The expression of YAP1 and other transcription factors
            contributes to lineage plasticity in combined small cell lung
            carcinoma.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Gaffney,C.J., Oka,T., Mazack,V., Hilman,D., Gat,U., Muramatsu,T.,
            Inazawa,J., Golden,A., Carey,D.J., Farooq,A., Tromp,G. and Sudol,M.
  TITLE     Identification, basic characterization and evolutionary analysis of
            differentially spliced mRNA isoforms of human YAP1 gene
  JOURNAL   Gene 509 (2), 215-222 (2012)
   PUBMED   22939869
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Chen,H.I., Einbond,A., Kwak,S.J., Linn,H., Koepf,E., Peterson,S.,
            Kelly,J.W. and Sudol,M.
  TITLE     Characterization of the WW domain of human yes-associated protein
            and its polyproline-containing ligands
  JOURNAL   J Biol Chem 272 (27), 17070-17077 (1997)
   PUBMED   9202023
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Chen,H.I. and Sudol,M.
  TITLE     The WW domain of Yes-associated protein binds a proline-rich ligand
            that differs from the consensus established for Src homology
            3-binding modules
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7819-7823 (1995)
   PUBMED   7644498
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Sudol,M., Bork,P., Einbond,A., Kastury,K., Druck,T., Negrini,M.,
            Huebner,K. and Lehman,D.
  TITLE     Characterization of the mammalian YAP (Yes-associated protein) gene
            and its role in defining a novel protein module, the WW domain
  JOURNAL   J Biol Chem 270 (24), 14733-14741 (1995)
   PUBMED   7782338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001527.5, BC038235.1,
            AP000942.6, AL832620.2 and AI128142.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a downstream nuclear effector of the
            Hippo signaling pathway which is involved in development, growth,
            repair, and homeostasis. This gene is known to play a role in the
            development and progression of multiple cancers as a
            transcriptional regulator of this signaling pathway and may
            function as a potential target for cancer treatment. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 9. The
            encoded protein (isoform 1) represents the YAP1-2gamma isoform
            described in Figure 3 of PMID: 22939869. It is shorter, compared to
            isoform 9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.100687.1, BC038235.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282441.10/ ENSP00000282441.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.1"
     Protein         1..504
                     /product="transcriptional coactivator YAP1 isoform 1"
                     /note="65 kDa Yes-associated protein; yorkie homolog;
                     yes-associated protein 2; protein yorkie homolog;
                     yes-associated protein YAP65 homolog; transcriptional
                     coactivator YAP1; Yes associated protein 1"
                     /calculated_mol_wt=54331
     Region          1..59
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            61
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by LATS1 and LATS2.
                     /evidence=ECO:0000269|PubMed:17974916,
                     ECO:0000269|PubMed:18158288, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Region          91..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q2EJA0; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by LATS1 and LATS2.
                     /evidence=ECO:0000269|PubMed:17974916,
                     ECO:0000269|PubMed:18158288, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q2EJA0; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:21364637,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by LATS1 and LATS2.
                     /evidence=ECO:0000269|PubMed:17974916,
                     ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001,
                     ECO:0000269|PubMed:28169360, ECO:0000269|PubMed:31835537,
                     ECO:0000269|PubMed:34404733, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            128
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Region          133..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:21364637,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:21364637,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by LATS1 and LATS2.
                     /evidence=ECO:0000269|PubMed:17974916,
                     ECO:0000269|PubMed:18158288; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Region          174..203
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(188,199)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          231..263
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(247,258)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Region          275..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Region          291..504
                     /region_name="Transactivation domain"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Region          355..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46937.2)"
     Site            367
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:21364637,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            371
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            397
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by LATS1 and LATS2.
                     /evidence=ECO:0000269|PubMed:17974916,
                     ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:20048001,
                     ECO:0000269|PubMed:28169360; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:20048001; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000269|PubMed:20048001; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000269|PubMed:18280240; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK8 and MAPK9.
                     /evidence=ECO:0000269|PubMed:21364637; propagated from
                     UniProtKB/Swiss-Prot (P46937.2)"
     CDS             1..504
                     /gene="YAP1"
                     /gene_synonym="COB1; YAP; YAP-1; YAP2; YAP65; YKI"
                     /coded_by="NM_001130145.3:403..1917"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS44716.1"
                     /db_xref="GeneID:10413"
                     /db_xref="HGNC:HGNC:16262"
                     /db_xref="MIM:606608"
ORIGIN      
        1 mdpgqqpppq papqgqgqpp sqppqgqgpp sgpgqpapaa tqaapqappa ghqivhvrgd
       61 setdlealfn avmnpktanv pqtvpmrlrk lpdsffkppe pkshsrqast dagtagaltp
      121 qhvrahsspa slqlgavspg tltptgvvsg paatptaqhl rqssfeipdd vplpagwema
      181 ktssgqryfl nhidqtttwq dprkamlsqm nvtaptsppv qqnmmnsasg plpdgweqam
      241 tqdgeiyyin hknkttswld prldprfamn qrisqsapvk qppplapqsp qggvmggsns
      301 nqqqqmrlqq lqmekerlrl kqqellrqam rninpstans pkcqelalrs qlptleqdgg
      361 tqnpvsspgm sqelrtmttn ssdpflnsgt yhsrdestds glsmssysvp rtpddflnsv
      421 demdtgdtin qstlpsqqnr fpdyleaipg tnvdlgtleg dgmniegeel mpslqealss
      481 dilndmesvl aatkldkesf ltwl
//
LOCUS       NP_001349699             391 aa            linear   PRI 20-NOV-2025
DEFINITION  casein kinase II subunit alpha isoform a [Homo sapiens].
ACCESSION   NP_001349699 XP_024307606
VERSION     NP_001349699.1
DBSOURCE    REFSEQ: accession NM_001362770.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Goel,H. and O'Donnell,S.
  TITLE     Inherited loss of function variant in CSNK2A1: the oldest reported
            cases of Okur-Chung syndrome in a single family
  JOURNAL   Clin Dysmorphol 33 (3), 121-124 (2024)
   PUBMED   38818820
  REMARK    GeneRIF: Inherited loss of function variant in CSNK2A1: the oldest
            reported cases of Okur-Chung syndrome in a single family.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Ampofo,E., Pack,M., Wrublewsky,S., Boewe,A.S., Spigelman,A.F.,
            Koch,H., MacDonald,P.E., Laschke,M.W., Montenarh,M. and Gotz,C.
  TITLE     CK2 activity is crucial for proper glucagon expression
  JOURNAL   Diabetologia 67 (7), 1368-1385 (2024)
   PUBMED   38503901
  REMARK    GeneRIF: CK2 activity is crucial for proper glucagon expression.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Liu,Z.D., Shi,Y.H., Xu,Q.C., Zhao,G.Y., Zhu,Y.Q., Li,F.X., Ma,M.J.,
            Ye,J.Y., Huang,X.T., Wang,X.Y., Xu,X., Wang,J.Q., Zhao,W. and
            Yin,X.Y.
  TITLE     CSNK2A1 confers gemcitabine resistance to pancreatic ductal
            adenocarcinoma via inducing autophagy
  JOURNAL   Cancer Lett 585, 216640 (2024)
   PUBMED   38290659
  REMARK    GeneRIF: CSNK2A1 confers gemcitabine resistance to pancreatic
            ductal adenocarcinoma via inducing autophagy.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Nan,H., Chu,M., Zhang,J., Jiang,D., Wang,Y. and Wu,L.
  TITLE     Okur-Chung neurodevelopmental syndrome: Implications for phenotype
            and genotype expansion
  JOURNAL   Mol Genet Genomic Med 12 (3), e2398 (2024)
   PUBMED   38444259
  REMARK    GeneRIF: Okur-Chung neurodevelopmental syndrome: Implications for
            phenotype and genotype expansion.
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Chung,W. and Okur,V.
  TITLE     Okur-Chung Neurodevelopmental Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35679446
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Russo,G.L., Vandenberg,M.T., Yu,I.J., Bae,Y.S., Franza,B.R. Jr. and
            Marshak,D.R.
  TITLE     Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the
            HeLa cell division cycle
  JOURNAL   J Biol Chem 267 (28), 20317-20325 (1992)
   PUBMED   1400350
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Lin,A., Frost,J., Deng,T., Smeal,T., al-Alawi,N., Kikkawa,U.,
            Hunter,T., Brenner,D. and Karin,M.
  TITLE     Casein kinase II is a negative regulator of c-Jun DNA binding and
            AP-1 activity
  JOURNAL   Cell 70 (5), 777-789 (1992)
   PUBMED   1516134
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1423636]
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Sacks,D.B., Davis,H.W., Crimmins,D.L. and McDonald,J.M.
  TITLE     Insulin-stimulated phosphorylation of calmodulin
  JOURNAL   Biochem J 286 (Pt 1) (Pt 1), 211-216 (1992)
   PUBMED   1520270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049761.11.
            
            On Apr 26, 2018 this sequence version replaced XP_024307606.1.
            
            Summary: Casein kinase II is a serine/threonine protein kinase that
            phosphorylates acidic proteins such as casein. It is involved in
            various cellular processes, including cell cycle control,
            apoptosis, and circadian rhythm. The kinase exists as a tetramer
            and is composed of an alpha, an alpha-prime, and two beta subunits.
            The alpha subunits contain the catalytic activity while the beta
            subunits undergo autophosphorylation. The protein encoded by this
            gene represents the alpha subunit. Multiple transcript variants
            encoding different protein isoforms have been found for this gene.
            [provided by RefSeq, Apr 2018].
            
            Transcript Variant: This variant (4) differs in the 3' UTR compared
            to variant 1. Variants 1, 2, 4 and 5 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.134425.1,
                                           SRR1803612.273870.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..391
                     /product="casein kinase II subunit alpha isoform a"
                     /EC_number="2.7.11.1"
                     /note="CK2 catalytic subunit alpha; protein kinase CK2;
                     casein kinase II alpha 1 subunit; casein kinase II alpha 1
                     polypeptide pseudogene; casein kinase 2, alpha 1
                     polypeptide"
                     /calculated_mol_wt=45013
     Region          20..325
                     /region_name="STKc_CK2_alpha"
                     /note="Catalytic subunit (alpha) of the Serine/Threonine
                     Kinase, Casein Kinase 2; cd14132"
                     /db_xref="CDD:271034"
     Site            order(36,39..41,67,69,101,103..104,110)
                     /site_type="other"
                     /note="allosteric inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..42,50,54,103)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..41,57,59,103)
                     /site_type="other"
                     /note="CK2 beta interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Region          36..41
                     /region_name="Interaction with beta subunit.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P68400.1)"
     Site            order(45..49,53,66,68,80,95,113..116,120,122..123,156,158,
                     160..161,163,175,178,189,191..194,196,235)
                     /site_type="active"
                     /db_xref="CDD:271034"
     Site            order(47..48,50..51,53,66,68,95,113..114,116,160..161,163,
                     174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271034"
     Site            order(80,122,156,158,178,189,191..194,196,235)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(174..184,189..196)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271034"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     CDS             1..391
                     /gene="CSNK2A1"
                     /gene_synonym="CK2A1; Cka1; Cka2; CKII; OCNDS"
                     /coded_by="NM_001362770.2:346..1521"
                     /note="isoform a is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS13003.1"
                     /db_xref="GeneID:1457"
                     /db_xref="HGNC:HGNC:2457"
                     /db_xref="MIM:115440"
ORIGIN      
        1 msgpvpsrar vytdvnthrp reywdyeshv vewgnqddyq lvrklgrgky sevfeainit
       61 nnekvvvkil kpvkkkkikr eikilenlrg gpniitladi vkdpvsrtpa lvfehvnntd
      121 fkqlyqtltd ydirfymyei lkaldychsm gimhrdvkph nvmidhehrk lrlidwglae
      181 fyhpgqeynv rvasryfkgp ellvdyqmyd ysldmwslgc mlasmifrke pffhghdnyd
      241 qlvriakvlg tedlydyidk ynieldprfn dilgrhsrkr werfvhsenq hlvspealdf
      301 ldkllrydhq srltareame hpyfytvvkd qarmgsssmp ggstpvssan mmsgissvpt
      361 psplgplags pviaaanplg mpvpaaagaq q
//
LOCUS       NP_004458                312 aa            linear   PRI 20-NOV-2025
DEFINITION  fibrinogen-like protein 1 precursor [Homo sapiens].
ACCESSION   NP_004458 XP_942979 XP_948560
VERSION     NP_004458.3
DBSOURCE    REFSEQ: accession NM_004467.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Liu,T.Y., Yan,J.S., Li,X., Xu,L., Hao,J.L., Zhao,S.Y., Hu,Q.L.,
            Na,F.J., Li,H.M., Zhao,Y. and Zhao,M.F.
  TITLE     FGL1: a novel biomarker and target for non-small cell lung cancer,
            promoting tumor progression and metastasis through KDM4A/STAT3
            transcription mechanism
  JOURNAL   J Exp Clin Cancer Res 43 (1), 213 (2024)
   PUBMED   39085849
  REMARK    GeneRIF: FGL1: a novel biomarker and target for non-small cell lung
            cancer, promoting tumor progression and metastasis through
            KDM4A/STAT3 transcription mechanism.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Li,J.J., Wang,J.H., Tian,T., Liu,J., Zheng,Y.Q., Mo,H.Y., Sheng,H.,
            Chen,Y.X., Wu,Q.N., Han,Y., Liao,K., Pan,Y.Q., Zeng,Z.L., Liu,Z.X.,
            Yang,W., Xu,R.H. and Ju,H.Q.
  TITLE     The liver microenvironment orchestrates FGL1-mediated immune escape
            and progression of metastatic colorectal cancer
  JOURNAL   Nat Commun 14 (1), 6690 (2023)
   PUBMED   37872170
  REMARK    GeneRIF: The liver microenvironment orchestrates FGL1-mediated
            immune escape and progression of metastatic colorectal cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Yao,X.M., Zhang,F.H. and Liu,Y.
  TITLE     Clinical Significance and Prognostic Value of the Expression of
            LAG-3 and FGL1 in Esophageal Squamous Cell Carcinoma
  JOURNAL   Bull Exp Biol Med 174 (6), 774-778 (2023)
   PUBMED   37162630
  REMARK    GeneRIF: Clinical Significance and Prognostic Value of the
            Expression of LAG-3 and FGL1 in Esophageal Squamous Cell Carcinoma.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Yang,C., Qian,Q., Zhao,Y., Huang,B., Chen,R., Gong,Q., Ji,H.,
            Wang,C., Xia,L., You,Z., Zhang,J. and Chen,X.
  TITLE     Fibrinogen-like protein 1 promotes liver-resident memory T-cell
            exhaustion in hepatocellular carcinoma
  JOURNAL   Front Immunol 14, 1112672 (2023)
   PUBMED   36993960
  REMARK    GeneRIF: Fibrinogen-like protein 1 promotes liver-resident memory
            T-cell exhaustion in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Saito,T., Ji,G., Shinzawa,H., Okumoto,K., Hattori,E., Adachi,T.,
            Takeda,T., Sugahara,K., Ito,J.I., Watanabe,H., Saito,K.,
            Togashi,H., Ishii,K., Matsuura,T., Inageda,K., Muramatsu,M. and
            Kawata,S.
  TITLE     Genetic variations in humans associated with differences in the
            course of hepatitis C
  JOURNAL   Biochem Biophys Res Commun 317 (2), 335-341 (2004)
   PUBMED   15063762
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Yan,J., Yu,Y., Wang,N., Chang,Y., Ying,H., Liu,W., He,J., Li,S.,
            Jiang,W., Li,Y., Liu,H., Wang,H. and Xu,Y.
  TITLE     LFIRE-1/HFREP-1, a liver-specific gene, is frequently downregulated
            and has growth suppressor activity in hepatocellular carcinoma
  JOURNAL   Oncogene 23 (10), 1939-1949 (2004)
   PUBMED   14981537
  REMARK    GeneRIF: data demonstrated that liver-specific gene LFIRE-1/HFREP-1
            was frequently downregulated and might possess growth suppressor
            activity in HCC
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Zeng,L., Dai,J., Ying,K., Zhao,E., Jin,W., Ye,Y., Dai,J., Xu,J.,
            Xie,Y. and Mao,Y.
  TITLE     Identification of a novel human angiopoietin-like gene expressed
            mainly in heart
  JOURNAL   J Hum Genet 48 (3), 159-162 (2003)
   PUBMED   12624729
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hara,H., Yoshimura,H., Uchida,S., Toyoda,Y., Aoki,M., Sakai,Y.,
            Morimoto,S. and Shiokawa,K.
  TITLE     Molecular cloning and functional expression analysis of a cDNA for
            human hepassocin, a liver-specific protein with hepatocyte
            mitogenic activity
  JOURNAL   Biochim Biophys Acta 1520 (1), 45-53 (2001)
   PUBMED   11470158
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Yamamoto,T., Gotoh,M., Sasaki,H., Terada,M., Kitajima,M. and
            Hirohashi,S.
  TITLE     Molecular cloning and initial characterization of a novel
            fibrinogen-related gene, HFREP-1
  JOURNAL   Biochem Biophys Res Commun 193 (2), 681-687 (1993)
   PUBMED   8390249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG618053.1, D87342.1,
            AF042354.1 and AC087273.5.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_948560.1, XP_942979.1, NP_004458.2.
            
            Summary: Fibrinogen-like 1 is a member of the fibrinogen family.
            This protein is homologous to the carboxy terminus of the
            fibrinogen beta- and gamma- subunits which contains the four
            conserved cysteines of fibrinogens and fibrinogen related proteins.
            However, this protein lacks the platelet-binding site,
            cross-linking region and a thrombin-sensitive site which are
            necessary for fibrin clot formation. This protein may play a role
            in the development of hepatocellular carcinomas. Four alternatively
            spliced transcript variants encoding the same protein exist for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) appears to be the
            predominantly expressed transcript. It lacks an exon in the 5' UTR
            and has an alternate exon at the 5' end compared to the longest
            variant (4). All four variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225616.1, SRR5189652.91177.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155590, SAMEA2162895
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000427924.5/ ENSP00000401952.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..312
                     /product="fibrinogen-like protein 1 precursor"
                     /note="hepassocin; hepatocyte-derived fibrinogen-related
                     protein 1; hepatocellular carcinoma-related sequence;
                     fibrinogen-like protein 1; liver fibrinogen-related
                     protein 1"
                     /calculated_mol_wt=34011
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2387
     mat_peptide     23..312
                     /product="fibrinogen-like protein 1"
                     /calculated_mol_wt=34011
     Region          78..304
                     /region_name="FReD"
                     /note="Fibrinogen-related domains (FReDs); C terminal
                     globular domain of fibrinogen. Fibrinogen is involved in
                     blood clotting, being activated by thrombin to assemble
                     into fibrin clots. The N-termini of 2 times 3 chains come
                     together to form a globular...; cd00087"
                     /db_xref="CDD:238040"
     Site            201
                     /site_type="other"
                     /note="gamma-gamma dimer interface [polypeptide binding]"
                     /db_xref="CDD:238040"
     Site            order(240,242,244)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238040"
     Site            order(248,251..252,261..262)
                     /site_type="active"
                     /note="polymerization pocket [active]"
                     /db_xref="CDD:238040"
     CDS             1..312
                     /gene="FGL1"
                     /gene_synonym="HFREP1; HP-041; HPS; LFIRE-1; LFIRE1"
                     /coded_by="NM_004467.4:96..1034"
                     /db_xref="CCDS:CCDS6004.1"
                     /db_xref="GeneID:2267"
                     /db_xref="HGNC:HGNC:3695"
                     /db_xref="MIM:605776"
ORIGIN      
        1 makvfsfilv ttaltmgrei saledcaqeq mrlraqvrll etrvkqqqvk ikqllqenev
       61 qfldkgdent vidlgskrqy adcseifndg yklsgfykik plqspaefsv ycdmsdgggw
      121 tviqrrsdgs enfnrgwkdy engfgnfvqk hgeywlgnkn lhflttqedy tlkidladfe
      181 knsryaqykn fkvgdeknfy elnigeysgt agdslagnfh pevqwwashq rmkfstwdrd
      241 hdnyegncae edqsgwwfnr chsanlngvy ysgpytaktd ngivwytwhg wwyslksvvm
      301 kirpndfipn vi
//
LOCUS       NP_000959                427 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL4 [Homo sapiens].
ACCESSION   NP_000959
VERSION     NP_000959.2
DBSOURCE    REFSEQ: accession NM_000968.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Okuwaki,M., Saito,S., Hirawake-Mogi,H. and Nagata,K.
  TITLE     The interaction between nucleophosmin/NPM1 and the large ribosomal
            subunit precursors contribute to maintaining the nucleolar
            structure
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1868 (1), 118879 (2021)
   PUBMED   33039556
  REMARK    GeneRIF: The interaction between nucleophosmin/NPM1 and the large
            ribosomal subunit precursors contribute to maintaining the
            nucleolar structure.
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Twiss,J.L., Smith,D.S., Chang,B. and Shooter,E.M.
  TITLE     Translational control of ribosomal protein L4 mRNA is required for
            rapid neurite regeneration
  JOURNAL   Neurobiol Dis 7 (4), 416-428 (2000)
   PUBMED   10964612
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Chan,Y.L., Olvera,J. and Wool,I.G.
  TITLE     The primary structures of rat ribosomal proteins L4 and L41
  JOURNAL   Biochem Biophys Res Commun 214 (3), 810-818 (1995)
   PUBMED   7575549
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Bagni,C., Mariottini,P., Annesi,F. and Amaldi,F.
  TITLE     Human ribosomal protein L4: cloning and sequencing of the cDNA and
            primary structure of the protein
  JOURNAL   Biochim Biophys Acta 1216 (3), 475-478 (1993)
   PUBMED   8268230
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from CB149679.1, BC066925.1, CA417911.1 and AC116913.6.
            
            On Nov 1, 2001 this sequence version replaced NP_000959.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L4E family of ribosomal proteins. It is located in the
            cytoplasm. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.266028.1,
                                           SRR1803611.24478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000307961.11/ ENSP00000311430.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..427
                     /product="large ribosomal subunit protein uL4"
                     /note="60S ribosomal protein L4; 60S ribosomal protein L1"
                     /calculated_mol_wt=47566
     Region          2..372
                     /region_name="PTZ00428"
                     /note="60S ribosomal protein L4; Provisional"
                     /db_xref="CDD:185611"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            97
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9D8E6; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            106
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            259
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D8E6; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P50878; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P36578.5)"
     Site            333
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            353
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D8E6; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9D8E6; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P36578.5)"
     Region          369..427
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P36578.5)"
     CDS             1..427
                     /gene="RPL4"
                     /gene_synonym="L4; uL4"
                     /coded_by="NM_000968.4:66..1349"
                     /db_xref="CCDS:CCDS10218.1"
                     /db_xref="GeneID:6124"
                     /db_xref="HGNC:HGNC:10353"
                     /db_xref="MIM:180479"
ORIGIN      
        1 macarplisv ysekgessgk nvtlpavfka pirpdivnfv htnlrknnrq pyavselagh
       61 qtsaeswgtg ravariprvr gggthrsgqg afgnmcrggr mfaptktwrr whrrvnttqk
      121 ryaicsalaa salpalvmsk ghrieevpel plvvedkveg ykktkeavll lkklkawndi
      181 kkvyasqrmr agkgkmrnrr riqrrgpcii ynedngiika frnipgitll nvsklnilkl
      241 apgghvgrfc iwtesafrkl delygtwrka aslksnynlp mhkmintdls rilkspeiqr
      301 alraprkkih rrvlkknplk nlrimlklnp yaktmrrnti lrqarnhklr vdkaaaaaaa
      361 lqaksdekaa vagkkpvvgk kgkkaavgvk kqkkplvgkk aaatkkpape kkpaekkptt
      421 eekkpaa
//
LOCUS       NP_001353521             872 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 23 [Homo
            sapiens].
ACCESSION   NP_001353521 XP_016855511
VERSION     NP_001353521.1
DBSOURCE    REFSEQ: accession NM_001366592.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 872)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 872)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 872)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 872)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 872)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 872)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 872)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 872)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 872)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 872)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855511.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.165480.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..872
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..872
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 23"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=98301
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <121..209
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <350..709
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          <574..>708
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..872
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366592.1:26..2644"
                     /note="isoform 23 is encoded by transcript variant 35"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkekt pelpepsvkv kepsvqeats tsdilkvpkp epipepkeps peknskkeke
      241 kektrprsrs rsksrsrtrs rspshtrprr rhrsrsrsys prrrpsprrr psprrrtppr
      301 rmpppprhrr srspvrrrrr ssaslsgsss sssssrsrsp pkkppkrtss pprktrrlsp
      361 saspprrrhr psppatpppk trhsptpqqs nrtrksrvsv spgrtsvtkh kgtekresps
      421 papkprkvel seseedkggk maaadsvqqr rqyrrqnqqs ssdsgsssss ederpkrshv
      481 kngevgrrrr hspsrsasps prkrqketsp rgrrrrspsp pptrrrrsps pappprrrrt
      541 ptppprrrtp sppprrrsps prrysppiqr ryspspppkr rtaspppppk rraspspppk
      601 rrvshspppk qrsspvtkrr spslsskhrk gsspsrstre arspqpnkrh spsprprapq
      661 tssspppvrr gassspqrrq spspstrpir rvsrtpepkk ikkaaspspq svrrvsssrs
      721 vsgspepaak kppappspvq sqspstnwsp avpvkkaksp tpspspprns dqegggkkkk
      781 kkkdkkhkkd kkhkkhkkhk kekavaaaaa aavtpaaiaa atttlaqeep vaapepkket
      841 eseaednldd lekhlrekal rsmrkaqvsp qs
//
LOCUS       NP_006107                504 aa            linear   PRI 20-NOV-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 isoform
            alpha [Homo sapiens].
ACCESSION   NP_006107
VERSION     NP_006107.1
DBSOURCE    REFSEQ: accession NM_006116.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Zhang,J., Teng,P., Sun,B., Zhang,J., Zhou,X. and Chen,W.
  TITLE     Down-regulated TAB1 suppresses the replication of Coxsackievirus B5
            via activating the NF-kappaB pathways through interaction with
            viral 3D polymerase
  JOURNAL   Virol J 20 (1), 291 (2023)
   PUBMED   38072991
  REMARK    GeneRIF: Down-regulated TAB1 suppresses the replication of
            Coxsackievirus B5 via activating the NF-kappaB pathways through
            interaction with viral 3D polymerase.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Ma,M., Dang,Y., Chang,B., Wang,F., Xu,J., Chen,L., Su,H., Li,J.,
            Ge,B., Chen,C. and Liu,H.
  TITLE     TAK1 is an essential kinase for STING trafficking
  JOURNAL   Mol Cell 83 (21), 3885-3903 (2023)
   PUBMED   37832545
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Maddali,P., Ambesi,A. and McKeown-Longo,P.J.
  TITLE     Induction of pro-inflammatory genes by fibronectin DAMPs in three
            fibroblast cell lines: Role of TAK1 and MAP kinases
  JOURNAL   PLoS One 18 (5), e0286390 (2023)
   PUBMED   37228128
  REMARK    GeneRIF: Induction of pro-inflammatory genes by fibronectin DAMPs
            in three fibroblast cell lines: Role of TAK1 and MAP kinases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Yamaguchi,K., Nagai,S., Ninomiya-Tsuji,J., Nishita,M., Tamai,K.,
            Irie,K., Ueno,N., Nishida,E., Shibuya,H. and Matsumoto,K.
  TITLE     XIAP, a cellular member of the inhibitor of apoptosis protein
            family, links the receptors to TAB1-TAK1 in the BMP signaling
            pathway
  JOURNAL   EMBO J 18 (1), 179-187 (1999)
   PUBMED   9878061
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Arch,R.H., Gedrich,R.W. and Thompson,C.B.
  TITLE     Tumor necrosis factor receptor-associated factors (TRAFs)--a family
            of adapter proteins that regulates life and death
  JOURNAL   Genes Dev 12 (18), 2821-2830 (1998)
   PUBMED   9744859
  REMARK    Review article
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Kurozumi,K., Nishita,M., Yamaguchi,K., Fujita,T., Ueno,N. and
            Shibuya,H.
  TITLE     BRAM1, a BMP receptor-associated molecule involved in BMP
            signalling
  JOURNAL   Genes Cells 3 (4), 257-264 (1998)
   PUBMED   9663660
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Deacon,K. and Blank,J.L.
  TITLE     Characterization of the mitogen-activated protein kinase kinase 4
            (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated
            by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not
            cause activation of p38 kinase in vivo
  JOURNAL   J Biol Chem 272 (22), 14489-14496 (1997)
   PUBMED   9162092
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Shibuya,H., Yamaguchi,K., Shirakabe,K., Tonegawa,A., Gotoh,Y.,
            Ueno,N., Irie,K., Nishida,E. and Matsumoto,K.
  TITLE     TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
            transduction
  JOURNAL   Science 272 (5265), 1179-1182 (1996)
   PUBMED   8638164
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC050554.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene was identified as a
            regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is
            known to mediate various intracellular signaling pathways, such as
            those induced by TGF beta, interleukin 1, and WNT-1. This protein
            interacts and thus activates TAK1 kinase. It has been shown that
            the C-terminal portion of this protein is sufficient for binding
            and activation of TAK1, while a portion of the N-terminus acts as a
            dominant-negative inhibitor of TGF beta, suggesting that this
            protein may function as a mediator between TGF beta receptors and
            TAK1. This protein can also interact with and activate the
            mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus
            represents an alternative activation pathway, in addition to the
            MAPKK pathways, which contributes to the biological responses of
            MAPK14 to various stimuli. Alternatively spliced transcript
            variants encoding distinct isoforms have been reported. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (alpha) encodes the longer isoform
            (alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC038582.1, SRR1163655.271787.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216160.11/ ENSP00000216160.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..504
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 1 isoform alpha"
                     /note="TAK1-binding protein 1; transforming growth factor
                     beta-activated kinase-binding protein 1; mitogen-activated
                     protein kinase kinase kinase 7-interacting protein 1"
                     /calculated_mol_wt=54513
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15750.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            order(46,50..51,69..71,290)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Region          69..334
                     /region_name="PP2C"
                     /note="Protein phosphatase 2C; pfam00481"
                     /db_xref="CDD:395385"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            395
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:22307082,
                     ECO:0000269|PubMed:28939839; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:14592977; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Region          430..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15750.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:14592977; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:14592977,
                     ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:18021073,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            484
                     /site_type="other"
                     /note="Required for interaction with MAP3K7.
                     /evidence=ECO:0000269|PubMed:11323434; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     CDS             1..504
                     /gene="TAB1"
                     /gene_synonym="3'-Tab1; MAP3K7IP1"
                     /coded_by="NM_006116.3:24..1538"
                     /note="isoform alpha is encoded by transcript variant
                     alpha"
                     /db_xref="CCDS:CCDS13993.1"
                     /db_xref="GeneID:10454"
                     /db_xref="HGNC:HGNC:18157"
                     /db_xref="MIM:602615"
ORIGIN      
        1 maaqrrsllq seqqpswtdd lplchlsgvg sasnrsysad gkgteshppe dswlkfrsen
       61 ncflygvfng ydgnrvtnfv aqrlsaelll gqlnaehaea dvrrvllqaf dvversfles
      121 iddalaekas lqsqlpegvp qhqlppqyqk ilerlktler eisggamavv avllnnklyv
      181 anvgtnrall ckstvdglqv tqlnvdhtte nedelfrlsq lgldagkikq vgiicgqest
      241 rrigdykvky gytdidllsa akskpiiaep eihgaqpldg vtgflvlmse glykaleaah
      301 gpgqanqeia amidtefakq tsldavaqav vdrvkrihsd tfasggerar fcprhedmtl
      361 lvrnfgyplg emsqptpspa paaggrvypv svpyssaqst sktsvtlslv mpsqgqmvng
      421 ahsastldea tptltnqspt ltlqstntht qssssssdgg lfrsrpahsl ppgedgrvep
      481 yvdfaefyrl wsvdhgeqsv vtap
//
LOCUS       NP_005484                729 aa            linear   PRI 20-NOV-2025
DEFINITION  ran-binding protein 9 [Homo sapiens].
ACCESSION   NP_005484
VERSION     NP_005484.2
DBSOURCE    REFSEQ: accession NM_005493.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Deng,T., Xie,L., Xiaofang,C., Zhang,Z., Xiao,Y., Peng,Y., Yin,L.,
            Fu,Y. and Li,X.
  TITLE     ATM-Mediated translocation of RanBPM regulates DNA damage response
            by stabilizing p21 in non-small cell lung cancer cells
  JOURNAL   Cell Oncol (Dordr) 47 (1), 245-258 (2024)
   PUBMED   37676377
  REMARK    GeneRIF: ATM-Mediated translocation of RanBPM regulates DNA damage
            response by stabilizing p21 in non-small cell lung cancer cells.
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Ideguchi,H., Ueda,A., Tanaka,M., Yang,J., Tsuji,T., Ohno,S.,
            Hagiwara,E., Aoki,A. and Ishigatsubo,Y.
  TITLE     Structural and functional characterization of the USP11
            deubiquitinating enzyme, which interacts with the RanGTP-associated
            protein RanBPM
  JOURNAL   Biochem J 367 (Pt 1), 87-95 (2002)
   PUBMED   12084015
  REMARK    GeneRIF: RanBPM is the enzymic substrate for USP11 and is
            deubiquitinated specifically
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Caballero,O.L., Resto,V., Patturajan,M., Meerzaman,D., Guo,M.Z.,
            Engles,J., Yochem,R., Ratovitski,E., Sidransky,D. and Jen,J.
  TITLE     Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1)
  JOURNAL   Oncogene 21 (19), 3003-3010 (2002)
   PUBMED   12082530
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Nishitani,H., Hirose,E., Uchimura,Y., Nakamura,M., Umeda,M.,
            Nishii,K., Mori,N. and Nishimoto,T.
  TITLE     Full-sized RanBPM cDNA encodes a protein possessing a long stretch
            of proline and glutamine within the N-terminal region, comprising a
            large protein complex
  JOURNAL   Gene 272 (1-2), 25-33 (2001)
   PUBMED   11470507
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Nishimoto,T.
  TITLE     A new role of ran GTPase
  JOURNAL   Biochem Biophys Res Commun 262 (3), 571-574 (1999)
   PUBMED   10471364
  REMARK    Review article
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Nakamura,M., Masuda,H., Horii,J., Kuma,Ki., Yokoyama,N., Ohba,T.,
            Nishitani,H., Miyata,T., Tanaka,M. and Nishimoto,T.
  TITLE     When overexpressed, a novel centrosomal protein, RanBPM, causes
            ectopic microtubule nucleation similar to gamma-tubulin
  JOURNAL   J Cell Biol 143 (4), 1041-1052 (1998)
   PUBMED   9817760
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z93020.1, AB055311.1,
            BC052781.1 and AF306510.1.
            
            On Dec 12, 2003 this sequence version replaced NP_005484.1.
            
            Summary: This gene encodes a protein that binds RAN, a small GTP
            binding protein belonging to the RAS superfamily that is essential
            for the translocation of RNA and proteins through the nuclear pore
            complex. The protein encoded by this gene has also been shown to
            interact with several other proteins, including met proto-oncogene,
            homeodomain interacting protein kinase 2, androgen receptor, and
            cyclin-dependent kinase 11. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF306510.1, BC052781.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000011619.6/ ENSP00000011619.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p23"
     Protein         1..729
                     /product="ran-binding protein 9"
                     /note="novel centrosomal protein RanBPM; ran binding
                     protein, centrosomal; Ran Binding Protein in the
                     Microtubule organizing center; ran-binding protein M"
                     /calculated_mol_wt=77717
     Region          1..137
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          189..331
                     /region_name="SPRY_RanBP9_10"
                     /note="SPRY domain in Ran binding proteins 9 and 10;
                     cd12909"
                     /db_xref="CDD:293966"
     Region          364..397
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          401..407
                     /region_name="Interaction with CALB1.
                     /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          403..>457
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     Site            405
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          461..489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P69566; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          615..729
                     /region_name="Interaction with FMR1.
                     /evidence=ECO:0000269|PubMed:15381419"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S59.1)"
     Region          616..708
                     /region_name="CRA"
                     /note="CT11-RanBPM; smart00757"
                     /db_xref="CDD:214806"
     CDS             1..729
                     /gene="RANBP9"
                     /gene_synonym="BPM-L; BPM90; RanBP7; RANBPM"
                     /coded_by="NM_005493.3:331..2520"
                     /db_xref="CCDS:CCDS4529.1"
                     /db_xref="GeneID:10048"
                     /db_xref="HGNC:HGNC:13727"
                     /db_xref="MIM:603854"
ORIGIN      
        1 msgqpppppp qqqqqqqqls ppppaalapv sgvvlpappa vsagsspags pgggaggegl
       61 gaaaaalllh pppppppata appppppppp ppasaaapas gppappglaa gpgpaggapt
      121 palvagssaa apfphgdsal neqekelqrr lkrlypavde qetplprsws pkdkfsyigl
      181 sqnnlrvhyk ghgktpkdaa svrathpipa acgiyyfevk ivskgrdgym giglsaqgvn
      241 mnrlpgwdkh sygyhgddgh sfcssgtgqp ygptfttgdv igccvnlinn tcfytknghs
      301 lgiaftdlpp nlyptvglqt pgevvdanfg qhpfvfdied ymrewrtkiq aqidrfpigd
      361 regewqtmiq kmvssylvhh gycataeafa rstdqtvlee lasiknrqri qklvlagrmg
      421 eaiettqqly psllernpnl lftlkvrqfi emvngtdsev rclggrspks qdsypvsprp
      481 fsspsmspsh gmnihnlasg kgstahfsgf escsngvisn kahqsychsn khqssnlnvp
      541 elnsinmsrs qqvnnftsnd vdmetdhysn gvgetssngf lngsskhdhe medcdtemev
      601 dssqlrrqlc ggsqaaierm ihfgrelqam seqlrrdcgk ntankkmlkd afsllaysdp
      661 wnspvgnqld piqrepvcsa lnsailethn lpkqpplala mgqatqclgl marsgigsca
      721 fatvedylh
//
LOCUS       NP_001305875             216 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26A isoform 5 [Homo
            sapiens].
ACCESSION   NP_001305875
VERSION     NP_001305875.1
DBSOURCE    REFSEQ: accession NM_001318946.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Hou,J., Wu,H., Xu,B., Shang,J., Xu,X., Li,G., Zhang,H., Zhang,W.,
            Deng,Y., Hong,X., Hu,T., Zhang,M. and Zhan,Y.
  TITLE     The Prognostic Value and the Oncogenic and Immunological Roles of
            Vacuolar Protein Sorting Associated Protein 26 A in Pancreatic
            Adenocarcinoma
  JOURNAL   Int J Mol Sci 24 (4), 3486 (2023)
   PUBMED   36834898
  REMARK    GeneRIF: The Prognostic Value and the Oncogenic and Immunological
            Roles of Vacuolar Protein Sorting Associated Protein 26 A in
            Pancreatic Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Arighi,C.N., Hartnell,L.M., Aguilar,R.C., Haft,C.R. and
            Bonifacino,J.S.
  TITLE     Role of the mammalian retromer in sorting of the cation-independent
            mannose 6-phosphate receptor
  JOURNAL   J Cell Biol 165 (1), 123-133 (2004)
   PUBMED   15078903
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Seaman,M.N.
  TITLE     Cargo-selective endosomal sorting for retrieval to the Golgi
            requires retromer
  JOURNAL   J Cell Biol 165 (1), 111-122 (2004)
   PUBMED   15078902
REFERENCE   8  (residues 1 to 216)
  AUTHORS   Reddy,J.V. and Seaman,M.N.
  TITLE     Vps26p, a component of retromer, directs the interactions of Vps35p
            in endosome-to-Golgi retrieval
  JOURNAL   Mol Biol Cell 12 (10), 3242-3256 (2001)
   PUBMED   11598206
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Haft,C.R., de la Luz Sierra,M., Bafford,R., Lesniak,M.A., Barr,V.A.
            and Taylor,S.I.
  TITLE     Human orthologs of yeast vacuolar protein sorting proteins Vps26,
            29, and 35: assembly into multimeric complexes
  JOURNAL   Mol Biol Cell 11 (12), 4105-4116 (2000)
   PUBMED   11102511
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Mao,M., Fu,G., Wu,J.S., Zhang,Q.H., Zhou,J., Kan,L.X., Huang,Q.H.,
            He,K.L., Gu,B.W., Han,Z.G., Shen,Y., Gu,J., Yu,Y.P., Xu,S.H.,
            Wang,Y.X., Chen,S.J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8175-8180 (1998)
   PUBMED   9653160
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA498726.1, BX647725.1,
            AF054179.1 and AL596223.3.
            
            Summary: This gene belongs to a group of vacuolar protein sorting
            (VPS) genes. The encoded protein is a component of a large
            multimeric complex, termed the retromer complex, involved in
            retrograde transport of proteins from endosomes to the trans-Golgi
            network. The close structural similarity between the yeast and
            human proteins that make up this complex suggests a similarity in
            function. Expression studies in yeast and mammalian cells indicate
            that this protein interacts directly with VPS35, which serves as
            the core of the retromer complex. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) lacks an alternate exon in the
            5' region, and it thus differs in its 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (5) is shorter at the N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.161229.1,
                                           SRR1660809.77354.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..216
                     /product="vacuolar protein sorting-associated protein 26A
                     isoform 5"
                     /note="vacuolar protein sorting-associated protein 26A;
                     vesicle protein sorting 26A; vacuolar protein sorting 26
                     homolog A; VPS26 retromer complex comonent A"
                     /calculated_mol_wt=25375
     Region          <2..172
                     /region_name="Vps26"
                     /note="Vacuolar protein sorting-associated protein 26;
                     pfam03643"
                     /db_xref="CDD:397622"
     CDS             1..216
                     /gene="VPS26A"
                     /gene_synonym="HB58; Hbeta58; PEP8A; VPS26"
                     /coded_by="NM_001318946.2:358..1008"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:9559"
                     /db_xref="HGNC:HGNC:12711"
                     /db_xref="MIM:605506"
ORIGIN      
        1 mqvekpyesy iganvrlryf lkvtivrrlt dlvkeydliv hqlatypdvn nsikmevgie
       61 dclhiefeyn kskyhlkdvi vgkiyfllvr ikiqhmelql ikkeitgigp stttetetia
      121 kyeimdgapv kgesipirlf lagydptptm rdvnkkfsvr yflnlvlvde edrryfkqqe
      181 iilwrkapek lrkqrtnfhq rfespesqas aeqpem
//
LOCUS       NP_001356329             206 aa            linear   PRI 20-NOV-2025
DEFINITION  ras-related protein Ral-B [Homo sapiens].
ACCESSION   NP_001356329
VERSION     NP_001356329.1
DBSOURCE    REFSEQ: accession NM_001369400.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 206)
  AUTHORS   Yoshimachi,S., Shirakawa,R., Cao,M., Trinh,D.A., Gao,P., Sakata,N.,
            Miyazaki,K., Goto,K., Miura,T., Ariake,K., Maeda,S., Masuda,K.,
            Ishida,M., Ohtsuka,H., Unno,M. and Horiuchi,H.
  TITLE     Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma
  JOURNAL   Cancer Sci 112 (8), 3064-3073 (2021)
   PUBMED   34009715
  REMARK    GeneRIF: Ral GTPase-activating protein regulates the malignancy of
            pancreatic ductal adenocarcinoma.
REFERENCE   2  (residues 1 to 206)
  AUTHORS   Wang,Y., Zheng,Y., Chen,Q., Dai,Y. and Li,T.
  TITLE     MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway
  JOURNAL   Arch Biochem Biophys 704, 108719 (2021)
   PUBMED   33290747
  REMARK    GeneRIF: MicroRNA-139 inhibits pancreatic-cancer carcinogenesis by
            suppressing RalB via the Ral/RAC/PI3K pathway.
REFERENCE   3  (residues 1 to 206)
  AUTHORS   Naszai,M., Bellec,K., Yu,Y., Roman-Fernandez,A., Sandilands,E.,
            Johansson,J., Campbell,A.D., Norman,J.C., Sansom,O.J., Bryant,D.M.
            and Cordero,J.B.
  TITLE     RAL GTPases mediate EGFR-driven intestinal stem cell proliferation
            and tumourigenesis
  JOURNAL   Elife 10, e63807 (2021)
   PUBMED   34096503
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 206)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 206)
  AUTHORS   Khawaja,H., Campbell,A., Roberts,J.Z., Javadi,A., O'Reilly,P.,
            McArt,D., Allen,W.L., Majkut,J., Rehm,M., Bardelli,A., Di
            Nicolantonio,F., Scott,C.J., Kennedy,R., Vitale,N., Harrison,T.,
            Sansom,O.J., Longley,D.B., Evergren,E. and Van Schaeybroeck,S.
  TITLE     RALB GTPase: a critical regulator of DR5 expression and TRAIL
            sensitivity in KRAS mutant colorectal cancer
  JOURNAL   Cell Death Dis 11 (10), 930 (2020)
   PUBMED   33122623
  REMARK    GeneRIF: RALB GTPase: a critical regulator of DR5 expression and
            TRAIL sensitivity in KRAS mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 206)
  AUTHORS   Joneson,T. and Bar-Sagi,D.
  TITLE     Ras effectors and their role in mitogenesis and oncogenesis
  JOURNAL   J Mol Med (Berl) 75 (8), 587-593 (1997)
   PUBMED   9297626
  REMARK    Review article
REFERENCE   7  (residues 1 to 206)
  AUTHORS   Jilkina,O. and Bhullar,R.P.
  TITLE     Generation of antibodies specific for the RalA and RalB GTP-binding
            proteins and determination of their concentration and distribution
            in human platelets
  JOURNAL   Biochim Biophys Acta 1314 (1-2), 157-166 (1996)
   PUBMED   8972729
REFERENCE   8  (residues 1 to 206)
  AUTHORS   Jullien-Flores,V., Dorseuil,O., Romero,F., Letourneur,F.,
            Saragosti,S., Berger,R., Tavitian,A., Gacon,G. and Camonis,J.H.
  TITLE     Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with
            CDC42/Rac GTPase-activating protein activity
  JOURNAL   J Biol Chem 270 (38), 22473-22477 (1995)
   PUBMED   7673236
REFERENCE   9  (residues 1 to 206)
  AUTHORS   Hsieh,C.L., Swaroop,A. and Francke,U.
  TITLE     Chromosomal localization and cDNA sequence of human ralB, a GTP
            binding protein
  JOURNAL   Somat Cell Mol Genet 16 (4), 407-410 (1990)
   PUBMED   2120779
REFERENCE   10 (residues 1 to 206)
  AUTHORS   Chardin,P. and Tavitian,A.
  TITLE     Coding sequences of human ralA and ralB cDNAs
  JOURNAL   Nucleic Acids Res 17 (11), 4380 (1989)
   PUBMED   2662142
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC012363.6.
            
            Summary: This gene encodes a GTP-binding protein that belongs to
            the small GTPase superfamily and Ras family of proteins.
            GTP-binding proteins mediate the transmembrane signaling initiated
            by the occupancy of certain cell surface receptors. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..206
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.2"
     Protein         1..206
                     /product="ras-related protein Ral-B"
                     /EC_number="3.6.5.2"
                     /note="RAS-like protein B; v-ral simian leukemia viral
                     oncogene homolog B (ras related; GTP binding protein); ras
                     related GTP binding protein B; RALB Ras like
                     proto-oncogene B"
                     /calculated_mol_wt=23277
     Region          15..178
                     /region_name="RalA_RalB"
                     /note="Ral (Ras-like) family containing highly homologous
                     RalA and RalB; cd04139"
                     /db_xref="CDD:206710"
     Site            21..28
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206710"
     Site            order(22..23,70..72,74..75,79,82,97,99,102..103,106..107,
                     110)
                     /site_type="active"
                     /note="GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            order(23..29,39..40,46,71,128..129,131,158..159)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206710"
     Site            order(28..29,43,45,51..52,65..66,68,70..71,160)
                     /site_type="other"
                     /note="putative GEF interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:206710"
     Site            order(36,38,47..52,56,60..61,161..164,166)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:206710"
     Region          43..51
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            44..51
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206710"
     Site            46
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206710"
     Site            68..71
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206710"
     Site            70..88
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206710"
     Site            128..131
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206710"
     Site            order(140..141,144,148,156)
                     /site_type="active"
                     /note="alternate GDI interaction site [active]"
                     /db_xref="CDD:206710"
     Site            158..160
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206710"
     Region          180..206
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P11234.1)"
     Site            203
                     /site_type="methylation"
                     /note="Cysteine methyl ester. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P11234.1)"
     CDS             1..206
                     /gene="RALB"
                     /coded_by="NM_001369400.1:180..800"
                     /db_xref="CCDS:CCDS2131.1"
                     /db_xref="GeneID:5899"
                     /db_xref="HGNC:HGNC:9840"
                     /db_xref="MIM:179551"
ORIGIN      
        1 maankskgqs slalhkvimv gsggvgksal tlqfmydefv edyeptkads yrkkvvldge
       61 evqidildta gqedyaaird nyfrsgegfl lvfsitehes ftataefreq ilrvkaeedk
      121 ipllvvgnks dleerrqvpv eearskaeew gvqyvetsak tranvdkvff dlmreirtkk
      181 msenkdkngk kssknkksfk erccll
//
LOCUS       NP_001265869             326 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription initiation factor IIA subunit 1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001265869
VERSION     NP_001265869.1
DBSOURCE    REFSEQ: accession NM_001278940.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 326)
  AUTHORS   DeJong,J., Bernstein,R. and Roeder,R.G.
  TITLE     Human general transcription factor TFIIA: characterization of a
            cDNA encoding the small subunit and requirement for basal and
            activated transcription
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3313-3317 (1995)
   PUBMED   7724559
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Ozer,J., Moore,P.A., Bolden,A.H., Lee,A., Rosen,C.A. and
            Lieberman,P.M.
  TITLE     Molecular cloning of the small (gamma) subunit of human TFIIA
            reveals functions critical for activated transcription
  JOURNAL   Genes Dev 8 (19), 2324-2335 (1994)
   PUBMED   7958899
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Ha,I., Lane,W.S. and Reinberg,D.
  TITLE     Cloning of a human gene encoding the general transcription
            initiation factor IIB
  JOURNAL   Nature 352 (6337), 689-695 (1991)
   PUBMED   1876184
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136040.5, BC050703.1 and BC107156.1.
            
            Summary: Accurate transcription initiation on TATA-containing class
            II genes involves the ordered assembly of RNA polymerase II
            (POLR2A; MIM 180660) and several general initiation factors
            (summarized by DeJong and Roeder, 1993 [PubMed 8224848]). One of
            these factors is TFIIA, which when purified from HeLa extracts
            consists of 35-, 19-, and 12-kD subunits.[supplied by OMIM, Jul
            2010].
            
            Transcript Variant: This variant (3) includes an alternate exon and
            uses a downstream start codon compared to variant 1. It encodes
            isoform 3 which has a shorter N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.9486.1,
                                           SRR14038193.595634.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.1"
     Protein         1..326
                     /product="transcription initiation factor IIA subunit 1
                     isoform 3"
                     /note="glucose regulated protein, 58kD pseudogene; general
                     transcription factor IIA, 1, 19/37kDa; TFIIA alpha/beta
                     subunits; transcription initiation factor IIA subunit 1;
                     general transcription factor IIA 1; transcription
                     initiation factor TFIIA 42 kDa subunit"
                     /calculated_mol_wt=35634
     Region          100..326
                     /region_name="TFIIA"
                     /note="Transcription factor IIA, alpha/beta subunit;
                     pfam03153"
                     /db_xref="CDD:460829"
     CDS             1..326
                     /gene="GTF2A1"
                     /gene_synonym="TF2A1; TFIIA; TFIIA-42; TFIIAL"
                     /coded_by="NM_001278940.2:659..1639"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:2957"
                     /db_xref="HGNC:HGNC:4646"
                     /db_xref="MIM:600520"
ORIGIN      
        1 mqsravdgfh seeqqlllqv qqqhqpqqqq hhhhhhhqqa qpqqtvpqqa qtqqvlipas
       61 qqatapqviv pdskliqhmn asnmsaaata atlalpagvt pvqqiltnsg qllqvvraan
      121 gaqyifqpqq svvlqqqvip qmqpggvqap viqqvlaplp ggispqtgvi iqpqqilftg
      181 nktqvipttv aaptpaqaqi tatgqqqpqa qpaqtqaplv lqvdgtgdts seededeeed
      241 ydddeeedke kdgaedgqve eeplnseddv sdeegqelfd tenvvvcqyd kihrsknkwk
      301 fhlkdgimnl ngrdyifska igdaew
//
LOCUS       NP_579805                191 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin alpha Fc receptor isoform c precursor [Homo
            sapiens].
ACCESSION   NP_579805
VERSION     NP_579805.1
DBSOURCE    REFSEQ: accession NM_133271.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Liu,Q. and Stadtmueller,B.M.
  TITLE     SIgA structures bound to Streptococcus pyogenes M4 and human CD89
            provide insights into host-pathogen interactions
  JOURNAL   Nat Commun 14 (1), 6726 (2023)
   PUBMED   37872175
  REMARK    GeneRIF: SIgA structures bound to Streptococcus pyogenes M4 and
            human CD89 provide insights into host-pathogen interactions.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Wu,H., Wang,X., Yang,Z., Zhao,Q., Wen,Y., Li,X., Zhang,W. and
            Gao,R.
  TITLE     Serum Soluble CD89-IgA Complexes Are Elevated in IgA Nephropathy
            without Immunosuppressant History
  JOURNAL   Dis Markers 2020, 8393075 (2020)
   PUBMED   32076466
  REMARK    GeneRIF: Serum Soluble CD89-IgA Complexes Are Elevated in IgA
            Nephropathy without Immunosuppressant History.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Pleass,R.J., Andrews,P.D., Kerr,M.A. and Woof,J.M.
  TITLE     Alternative splicing of the human IgA Fc receptor CD89 in
            neutrophils and eosinophils
  JOURNAL   Biochem J 318 (Pt 3) (Pt 3), 771-777 (1996)
   PUBMED   8836118
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Patry,C., Sibille,Y., Lehuen,A. and Monteiro,R.C.
  TITLE     Identification of Fc alpha receptor (CD89) isoforms generated by
            alternative splicing that are differentially expressed between
            blood monocytes and alveolar macrophages
  JOURNAL   J Immunol 156 (11), 4442-4448 (1996)
   PUBMED   8666819
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Morton,H.C., Schiel,A.E., Janssen,S.W. and van de Winkel,J.G.
  TITLE     Alternatively spliced forms of the human myeloid Fc alpha receptor
            (CD89) in neutrophils
  JOURNAL   Immunogenetics 43 (4), 246-247 (1996)
   PUBMED   8575829
REFERENCE   7  (residues 1 to 191)
  AUTHORS   de Wit,T.P., Morton,H.C., Capel,P.J. and van de Winkel,J.G.
  TITLE     Structure of the gene for the human myeloid IgA Fc receptor (CD89)
  JOURNAL   J Immunol 155 (3), 1203-1209 (1995)
   PUBMED   7636188
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Kremer,E.J., Kalatzis,V., Baker,E., Callen,D.F., Sutherland,G.R.
            and Maliszewski,C.R.
  TITLE     The gene for the human IgA Fc receptor maps to 19q13.4
  JOURNAL   Hum Genet 89 (1), 107-108 (1992)
   PUBMED   1577457
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Maliszewski,C.R., March,C.J., Schoenborn,M.A., Gimpel,S. and
            Shen,L.
  TITLE     Expression cloning of a human Fc receptor for IgA
  JOURNAL   J Exp Med 172 (6), 1665-1672 (1990)
   PUBMED   2258698
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Kimata,H. and Saxon,A.
  TITLE     Subset of natural killer cells is induced by immune complexes to
            display Fc receptors for IgE and IgA and demonstrates isotype
            regulatory function
  JOURNAL   J Clin Invest 82 (1), 160-167 (1988)
   PUBMED   2455732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290922.1, S82919.1 and
            AC245128.3.
            
            Summary: This gene is a member of the immunoglobulin gene
            superfamily and encodes a receptor for the Fc region of IgA. The
            receptor is a transmembrane glycoprotein present on the surface of
            myeloid lineage cells such as neutrophils, monocytes, macrophages,
            and eosinophils, where it mediates immunologic responses to
            pathogens. It interacts with IgA-opsonized targets and triggers
            several immunologic defense processes, including phagocytosis,
            antibody-dependent cell-mediated cytotoxicity, and stimulation of
            the release of inflammatory mediators. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3, also known as a.3, Rla2,
            deltaE2, or U08) lacks an alternate in-frame exon in the 3' coding
            region, compared to variant 1. The encoded isoform (c) is shorter
            than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U43677.1, X92561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142670, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..191
                     /product="immunoglobulin alpha Fc receptor isoform c
                     precursor"
                     /note="immunoglobulin alpha Fc receptor; Fc fragment of
                     IgA, receptor for; Fc fragment of IgA receptor"
                     /calculated_mol_wt=19367
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2345
     Region          28..119
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,101,108)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          72..75
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          84..88
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          96..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          112..119
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     CDS             1..191
                     /gene="FCAR"
                     /gene_synonym="CD89; CTB-61M7.2; FcalphaR; FcalphaRI"
                     /coded_by="NM_133271.4:56..631"
                     /note="isoform c precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS12908.1"
                     /db_xref="GeneID:2204"
                     /db_xref="HGNC:HGNC:3608"
                     /db_xref="MIM:147045"
ORIGIN      
        1 mdpkqttllc lvlclgqriq aqegdfpmpf isaksspvip ldgsvkiqcq aireayltql
       61 miiknstyre igrrlkfwne tdpefvidhm dankagryqc qyrighyrfr ysdtlelvvt
      121 dsihqdyttq nlirmavagl vlvallailv enwhshtaln keasadvaep swsqqmcqpg
      181 ltfartpsvc k
//
LOCUS       NP_001346555             622 aa            linear   PRI 20-NOV-2025
DEFINITION  palmitoyltransferase ZDHHC17 isoform 2 [Homo sapiens].
ACCESSION   NP_001346555
VERSION     NP_001346555.1
DBSOURCE    REFSEQ: accession NM_001359626.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 622)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 622)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 622)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 622)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 622)
  AUTHORS   Chen,X., Hao,A., Li,X., Ye,K., Zhao,C., Yang,H., Ma,H., Hu,L.,
            Zhao,Z., Hu,L., Ye,F., Sun,Q., Zhang,H., Wang,H., Yao,X. and
            Fang,Z.
  TITLE     Activation of JNK and p38 MAPK Mediated by ZDHHC17 Drives
            Glioblastoma Multiforme Development and Malignant Progression
  JOURNAL   Theranostics 10 (3), 998-1015 (2020)
   PUBMED   31938047
  REMARK    GeneRIF: Activation of JNK and p38 MAPK Mediated by ZDHHC17 Drives
            Glioblastoma Multiforme Development and Malignant Progression.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 622)
  AUTHORS   Huang,K., Yanai,A., Kang,R., Arstikaitis,P., Singaraja,R.R.,
            Metzler,M., Mullard,A., Haigh,B., Gauthier-Campbell,C.,
            Gutekunst,C.A., Hayden,M.R. and El-Husseini,A.
  TITLE     Huntingtin-interacting protein HIP14 is a palmitoyl transferase
            involved in palmitoylation and trafficking of multiple neuronal
            proteins
  JOURNAL   Neuron 44 (6), 977-986 (2004)
   PUBMED   15603740
REFERENCE   7  (residues 1 to 622)
  AUTHORS   Ducker,C.E., Stettler,E.M., French,K.J., Upson,J.J. and Smith,C.D.
  TITLE     Huntingtin interacting protein 14 is an oncogenic human protein:
            palmitoyl acyltransferase
  JOURNAL   Oncogene 23 (57), 9230-9237 (2004)
   PUBMED   15489887
  REMARK    GeneRIF: has the ability to induce colony formation in cell
            culture, anchorage-independent growth, and tumors in mice
            GeneRIF: HIP14 is a protein: palmitoyl acyltransferase
REFERENCE   8  (residues 1 to 622)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
REFERENCE   9  (residues 1 to 622)
  AUTHORS   Singaraja,R.R., Hadano,S., Metzler,M., Givan,S., Wellington,C.L.,
            Warby,S., Yanai,A., Gutekunst,C.A., Leavitt,B.R., Yi,H.,
            Fichter,K., Gan,L., McCutcheon,K., Chopra,V., Michel,J.,
            Hersch,S.M., Ikeda,J.E. and Hayden,M.R.
  TITLE     HIP14, a novel ankyrin domain-containing protein, links huntingtin
            to intracellular trafficking and endocytosis
  JOURNAL   Hum Mol Genet 11 (23), 2815-2828 (2002)
   PUBMED   12393793
REFERENCE   10 (residues 1 to 622)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA803825.1, BC050324.1, AB023163.1 and AA843159.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.138199.1,
                                           SRR1803611.10692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.2"
     Protein         1..622
                     /product="palmitoyltransferase ZDHHC17 isoform 2"
                     /EC_number="2.3.1.225"
                     /note="huntingtin interacting protein 3; huntingtin
                     interacting protein 14; palmitoyltransferase ZDHHC17;
                     huntingtin yeast partner H; huntingtin-interacting protein
                     H; putative MAPK-activating protein PM11; putative
                     NF-kappa-B-activating protein 205; acyltransferase ZDHHC7;
                     acyltransferase ZDHHC17; zinc finger DHHC
                     domain-containing protein 17; zinc finger DHHC-type
                     containing 17; DHHC domain-containing cysteine-rich
                     protein 17; zinc finger DHHC-type palmitoyltransferase 17"
                     /calculated_mol_wt=71288
     Region          42..297
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(56..58,60..61,65,68,77,79,81,85..86,89..91,93..94,
                     98,101,110,112,114,119..120,123..125,127..128,132,135,144)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          79..110
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          112..144
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(146,148,152..153,156..158,160..161,165,168,177,179,
                     181,185..186,189..191,194..195,199,202,211,214,216,
                     220..221,224..226,228..229,233,236,245)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          146..177
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          179..211
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          214..245
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          428..558
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     CDS             1..622
                     /gene="ZDHHC17"
                     /gene_synonym="DHHC-17; DHHC17; HIP14; HIP3; HSPC294;
                     HYPH"
                     /coded_by="NM_001359626.1:10..1878"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:23390"
                     /db_xref="HGNC:HGNC:18412"
                     /db_xref="MIM:607799"
ORIGIN      
        1 madgpdeydt eagcvpllhp eeikpqshyn hgygeplgrk thiddystwd ivkatqygiy
       61 ercrelveag ydvrqpdken vtllhwaain nridlvkyyi skgaivdqlg gdlnstplhw
      121 atrqghlsmv vqlmkygadp slidgegcsc ihlaaqfght sivayliakg qdvdmmdqng
      181 mtplmwaayr thsvdptrll ltfnvsvnlg dkyhkntalh wavlagnttv isllleagan
      241 vdaqnikges aldlakqrkn vwminhlqea rqakgydnps flrklkadke frqkvmlgtp
      301 flviwlvgfi adlnidswli kglmyggvwa tvqflsksff dhsmhsalpl giylatkfwm
      361 yvtwffwfwn dlnflfihlp flansvalfy nfgkswksdp giikateeqk kktivelaet
      421 gsldlsifcs tclirkpvrs khcgvcnrci akfdhhcpwv gncvgagnhr yfmgylffll
      481 fmicwmiygc isywglhcet tytkdgfwty itqiatcspw mfwmflnsvf hfmwvavllm
      541 cqmyqisclg ittnermnar rykhfkvttt siespfnhgc vrniidffef rccglfrpvi
      601 vdwtrqytie ydqisgsgyq lv
//
LOCUS       NP_001274455             108 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 22 homolog isoform c [Homo
            sapiens].
ACCESSION   NP_001274455
VERSION     NP_001274455.1
DBSOURCE    REFSEQ: accession NM_001287526.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Silva,D.A., Huang,X., Behal,R.H., Cole,D.G. and Qin,H.
  TITLE     The RABL5 homolog IFT22 regulates the cellular pool size and the
            amount of IFT particles partitioned to the flagellar compartment in
            Chlamydomonas reinhardtii
  JOURNAL   Cytoskeleton (Hoboken) 69 (1), 33-48 (2012)
   PUBMED   22076686
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Adhiambo,C., Blisnick,T., Toutirais,G., Delannoy,E. and Bastin,P.
  TITLE     A novel function for the atypical small G protein Rab-like 5 in the
            assembly of the trypanosome flagellum
  JOURNAL   J Cell Sci 122 (Pt 6), 834-841 (2009)
   PUBMED   19240117
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA709553.1, DA700693.1, AC006329.5 and CA841889.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. Variants 3 through 6
            encode the same isoform (c), which is shorter at the N-terminus,
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA709553.1, SRR1660805.249647.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMN03267770
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..108
                     /product="intraflagellar transport protein 22 homolog
                     isoform c"
                     /note="RAB, member of RAS oncogene family-like 5; rab-like
                     protein 5; RAB, member RAS oncogene family-like 5;
                     intraflagellar transport protein 22 homolog;
                     intraflagellar transport 22 homolog"
                     /calculated_mol_wt=12262
     CDS             1..108
                     /gene="IFT22"
                     /gene_synonym="CFAP9; FAP9; RABL5"
                     /coded_by="NM_001287526.1:179..505"
                     /note="isoform c is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS47671.1"
                     /db_xref="GeneID:64792"
                     /db_xref="HGNC:HGNC:21895"
                     /db_xref="MIM:620505"
ORIGIN      
        1 mkdahgvviv fnadipshrk ememwyscfv qqpslqdtqc mliahhkpgs gddkgslsls
       61 pplnklklvh snleddpeei rmefikylks iinsmsesrd reemsimt
//
LOCUS       NP_536800                421 aa            linear   PRI 20-NOV-2025
DEFINITION  acetylcholinesterase collagenic tail peptide isoform III precursor
            [Homo sapiens].
ACCESSION   NP_536800
VERSION     NP_536800.2
DBSOURCE    REFSEQ: accession NM_080539.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Hesami,O., Ramezani,M., Ghasemi,A., Fatehi,F., Okhovat,A.A.,
            Ziaadini,B., Kariminejad,A. and Nafissi,S.
  TITLE     COLQ-Congenital myasthenic syndrome in an Iranian cohort: the
            clinical and genetics spectrum
  JOURNAL   Orphanet J Rare Dis 19 (1), 113 (2024)
   PUBMED   38475910
  REMARK    GeneRIF: COLQ-Congenital myasthenic syndrome in an Iranian cohort:
            the clinical and genetics spectrum.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Barbeau,S., Semprez,F., Dobbertin,A., Merriadec,L., Roussange,F.,
            Eymard,B., Sternberg,D., Fournier,E., Karasoy,H., Martinat,C. and
            Legay,C.
  TITLE     Molecular Analysis of a Congenital Myasthenic Syndrome Due to a
            Pathogenic Variant Affecting the C-Terminus of ColQ
  JOURNAL   Int J Mol Sci 24 (22), 16217 (2023)
   PUBMED   38003406
  REMARK    GeneRIF: Molecular Analysis of a Congenital Myasthenic Syndrome Due
            to a Pathogenic Variant Affecting the C-Terminus of ColQ.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Mishra,S., Nair,K.V. and Shukla,A.
  TITLE     Delineation of molecular characteristics of congenital myasthenic
            syndromes in Indian families and review of literature
  JOURNAL   Clin Dysmorphol 32 (4), 162-167 (2023)
   PUBMED   37646703
  REMARK    GeneRIF: Delineation of molecular characteristics of congenital
            myasthenic syndromes in Indian families and review of literature.
            Review article
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Uyen Dao,T.M., Barbeau,S., Messeant,J., Della-Gaspera,B.,
            Bouceba,T., Semprez,F., Legay,C. and Dobbertin,A.
  TITLE     The collagen ColQ binds to LRP4 and regulates the activation of the
            Muscle-Specific Kinase-LRP4 receptor complex by agrin at the
            neuromuscular junction
  JOURNAL   J Biol Chem 299 (8), 104962 (2023)
   PUBMED   37356721
  REMARK    GeneRIF: The collagen ColQ binds to LRP4 and regulates the
            activation of the Muscle-Specific Kinase-LRP4 receptor complex by
            agrin at the neuromuscular junction.
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Deprez,P. and Inestrosa,N.C.
  TITLE     Molecular modeling of the collagen-like tail of asymmetric
            acetylcholinesterase
  JOURNAL   Protein Eng 13 (1), 27-34 (2000)
   PUBMED   10679527
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Altamirano,C.V. and Lockridge,O.
  TITLE     Conserved aromatic residues of the C-terminus of human
            butyrylcholinesterase mediate the association of tetramers
  JOURNAL   Biochemistry 38 (40), 13414-13422 (1999)
   PUBMED   10529218
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Ohno,K., Brengman,J.M., Felice,K.J., Cornblath,D.R. and Engel,A.G.
  TITLE     Congenital end-plate acetylcholinesterase deficiency caused by a
            nonsense mutation and an A-->G splice-donor-site mutation at
            position +3 of the collagenlike-tail-subunit gene (COLQ): how does
            G at position +3 result in aberrant splicing?
  JOURNAL   Am J Hum Genet 65 (3), 635-644 (1999)
   PUBMED   10441569
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Donger,C., Krejci,E., Serradell,A.P., Eymard,B., Bon,S., Nicole,S.,
            Chateau,D., Gary,F., Fardeau,M., Massoulie,J. and Guicheney,P.
  TITLE     Mutation in the human acetylcholinesterase-associated collagen
            gene, COLQ, is responsible for congenital myasthenic syndrome with
            end-plate acetylcholinesterase deficiency (Type Ic)
  JOURNAL   Am J Hum Genet 63 (4), 967-975 (1998)
   PUBMED   9758617
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Ohno,K., Brengman,J., Tsujino,A. and Engel,A.G.
  TITLE     Human endplate acetylcholinesterase deficiency caused by mutations
            in the collagen-like tail subunit (ColQ) of the asymmetric enzyme
  JOURNAL   Proc Natl Acad Sci U S A 95 (16), 9654-9659 (1998)
   PUBMED   9689136
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX500613.1, AF057036.1,
            AK128401.1 and AI554171.1.
            
            On Apr 25, 2007 this sequence version replaced NP_536800.1.
            
            Summary: This gene encodes the subunit of a collagen-like molecule
            associated with acetylcholinesterase in skeletal muscle. Each
            molecule is composed of three identical subunits. Each subunit
            contains a proline-rich attachment domain (PRAD) that binds an
            acetylcholinesterase tetramer to anchor the catalytic subunit of
            the enzyme to the basal lamina. Mutations in this gene are
            associated with endplate acetylcholinesterase deficiency. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (III) is the only variant missing
            exon 3. Exon 3 encodes the proline-rich attachment domain; as a
            result, isoform III is the only isoform lacking this domain.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed/partial sample support SAMEA1965299,
                              SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..421
                     /product="acetylcholinesterase collagenic tail peptide
                     isoform III precursor"
                     /note="single strand of homotrimeric collagen-like tail
                     subunit of asymmetric acetylcholinesterase; AChE Q
                     subunit; acetylcholinesterase-associated collagen;
                     collagenic tail of endplate acetylcholinesterase;
                     acetylcholinesterase collagenic tail peptide;
                     collagen-like tail subunit (single strand of homotrimer)
                     of asymmetric acetylcholinesterase"
                     /calculated_mol_wt=40974
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3287
     mat_peptide     23..421
                     /product="acetylcholinesterase collagenic tail peptide
                     isoform III"
                     /calculated_mol_wt=41762
     Region          <68..>256
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          339..>363
                     /region_name="myxo_disulf_rpt"
                     /note="Myxococcus cysteine-rich repeat; TIGR02232"
                     /db_xref="CDD:200169"
     CDS             1..421
                     /gene="COLQ"
                     /gene_synonym="CMS5; EAD"
                     /coded_by="NM_080539.4:82..1347"
                     /note="isoform III precursor is encoded by transcript
                     variant III"
                     /db_xref="CCDS:CCDS43057.1"
                     /db_xref="GeneID:8292"
                     /db_xref="HGNC:HGNC:2226"
                     /db_xref="MIM:603033"
ORIGIN      
        1 mvvlnpmtlg iylqlfflsi vsqptfinsv lpisaalpsl dqkkrgghka cclltppppp
       61 lfpppffrgg rspgppglpg ktgpkgekge lgrpgrkgrp gppgvpgmpg pigwpgpegp
      121 rgekgdlgmm glpgsrgpmg skgypgsrge kgsrgekgdl gpkgekgfpg fpgmlgqkge
      181 mgpkgepgia ghrgptgrpg krgkqgqkgd sgvmgppgkp gpsgqpgrpg ppgpppagql
      241 imgpkgergf pgppgrclcg ptmnvnnpsy gesvygpssp rvpvifvvnn qeelerlntq
      301 naiafrrdqr slyfkdslgw lpiqltpfyp vdytadqhgt cgdgllqpge ecddgnsdvg
      361 ddcirchray cgdghrhegv edcdgsdfgy ltcetylpgs ygdlqctqyc yidstpcryf
      421 t
//
LOCUS       NP_036458                281 aa            linear   PRI 20-NOV-2025
DEFINITION  microtubule-associated protein RP/EB family member 3 isoform 1
            [Homo sapiens].
ACCESSION   NP_036458
VERSION     NP_036458.2
DBSOURCE    REFSEQ: accession NM_012326.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zhang,Y., Liu,F., Zheng,J., Jiang,K., Ai,H., Liu,L. and Mao,D.
  TITLE     MAPRE3 as an epigenetic target of EZH2 restricts ovarian cancer
            proliferation in vitro and in vivo
  JOURNAL   Exp Cell Res 435 (1), 113913 (2024)
   PUBMED   38199479
  REMARK    GeneRIF: MAPRE3 as an epigenetic target of EZH2 restricts ovarian
            cancer proliferation in vitro and in vivo.
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Bu,W. and Su,L.K.
  TITLE     Characterization of functional domains of human EB1 family proteins
  JOURNAL   J Biol Chem 278 (50), 49721-49731 (2003)
   PUBMED   14514668
  REMARK    GeneRIF: neither APC nor p150glued binding domain is necessary for
            EB1 or EBF3 to induce microtubule bundling
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Su,L.K. and Qi,Y.
  TITLE     Characterization of human MAPRE genes and their proteins
  JOURNAL   Genomics 71 (2), 142-149 (2001)
   PUBMED   11161807
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Nakagawa,H., Koyama,K., Murata,Y., Morito,M., Akiyama,T. and
            Nakamura,Y.
  TITLE     EB3, a novel member of the EB1 family preferentially expressed in
            the central nervous system, binds to a CNS-specific APC homologue
  JOURNAL   Oncogene 19 (2), 210-216 (2000)
   PUBMED   10644998
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Juwana,J.P., Henderikx,P., Mischo,A., Wadle,A., Fadle,N.,
            Gerlach,K., Arends,J.W., Hoogenboom,H., Pfreundschuh,M. and
            Renner,C.
  TITLE     EB/RP gene family encodes tubulin binding proteins
  JOURNAL   Int J Cancer 81 (2), 275-284 (1999)
   PUBMED   10188731
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Renner,C., Pfitzenmeier,J.P., Gerlach,K., Held,G., Ohnesorge,S.,
            Sahin,U., Bauer,S. and Pfreundschuh,M.
  TITLE     RP1, a new member of the adenomatous polyposis coli-binding
            EB1-like gene family, is differentially expressed in activated T
            cells
  JOURNAL   J Immunol 159 (3), 1276-1283 (1997)
   PUBMED   9233623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC417465.1, BC011557.1,
            AC013472.8 and AB025186.1.
            
            On Oct 13, 2000 this sequence version replaced NP_036458.1.
            
            Summary:  The protein encoded by this gene is a member of the RP/EB
            family of genes.  The protein localizes to the cytoplasmic
            microtubule network and binds APCL, a homolog of the adenomatous
            polyposis coli tumor suppressor gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB025186.1, SRR3476690.840810.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233121.7/ ENSP00000233121.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..281
                     /product="microtubule-associated protein RP/EB family
                     member 3 isoform 1"
                     /note="APC binding protein; end-binding protein 3; EB1
                     protein family member 3"
                     /calculated_mol_wt=31851
     Region          16..279
                     /region_name="BIM1"
                     /note="Microtubule-binding protein involved in cell cycle
                     control [Cell division and chromosome partitioning /
                     Cytoskeleton]; COG5217"
                     /db_xref="CDD:227542"
     Region          157..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PER3; propagated from
                     UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          217..281
                     /region_name="DCTN1-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          217..260
                     /region_name="APC-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     Region          261..281
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UPY8.1)"
     CDS             1..281
                     /gene="MAPRE3"
                     /gene_synonym="EB3; EBF3; EBF3-S; RP3"
                     /coded_by="NM_012326.4:174..1019"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1731.1"
                     /db_xref="GeneID:22924"
                     /db_xref="HGNC:HGNC:6892"
                     /db_xref="MIM:605788"
ORIGIN      
        1 mavnvystsv tsenlsrhdm lawvndslhl nytkieqlcs gaaycqfmdm lfpgcvhlrk
       61 vkfqaklehe yihnfkvlqa afkkmgvdki ipveklvkgk fqdnfefiqw fkkffdanyd
      121 gkdynpllar qgqdvapppn pgdqifnksk kligtavpqr tsptgpknmq tsgrlsnvap
      181 pcilrknpps arngghetda qilelnqqlv dlkltvdgle kerdfyfskl rdielicqeh
      241 esenspvisg iigilyatee gfappeddei eehqqedqde y
//
LOCUS       NP_116253                312 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor 38A [Homo sapiens].
ACCESSION   NP_116253
VERSION     NP_116253.2
DBSOURCE    REFSEQ: accession NM_032864.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Townsend,C., Leelaram,M.N., Agafonov,D.E., Dybkov,O., Will,C.L.,
            Bertram,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Mechanism of protein-guided folding of the active site U2/U6 RNA
            during spliceosome activation
  JOURNAL   Science 370 (6523) (2020)
   PUBMED   33243851
  REMARK    GeneRIF: Mechanism of protein-guided folding of the active site
            U2/U6 RNA during spliceosome activation.
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Dopie,J., Sweredoski,M.J., Moradian,A. and Belmont,A.S.
  TITLE     Tyramide signal amplification mass spectrometry (TSA-MS) ratio
            identifies nuclear speckle proteins
  JOURNAL   J Cell Biol 219 (9) (2020)
   PUBMED   32609799
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Varjosalo,M., Keskitalo,S., Van Drogen,A., Nurkkala,H.,
            Vichalkovski,A., Aebersold,R. and Gstaiger,M.
  TITLE     The protein interaction landscape of the human CMGC kinase group
  JOURNAL   Cell Rep 3 (4), 1306-1320 (2013)
   PUBMED   23602568
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Hegele,A., Kamburov,A., Grossmann,A., Sourlis,C., Wowro,S.,
            Weimann,M., Will,C.L., Pena,V., Luhrmann,R. and Stelzl,U.
  TITLE     Dynamic protein-protein interaction wiring of the human spliceosome
  JOURNAL   Mol Cell 45 (4), 567-580 (2012)
   PUBMED   22365833
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092038.1, BU508261.1, BF223635.1, BE465896.1 and AL138849.12.
            
            On Nov 7, 2002 this sequence version replaced NP_116253.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.141408.1,
                                           SRR1660803.23158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000257181.10/ ENSP00000257181.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..312
                     /product="pre-mRNA-splicing factor 38A"
                     /note="PRP38 pre-mRNA processing factor 38 domain
                     containing A"
                     /calculated_mol_wt=37345
     Region          1..179
                     /region_name="N-terminal protein interaction domain.
                     /evidence=ECO:0000269|PubMed:26673105"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Region          10..172
                     /region_name="PRP38"
                     /note="PRP38 family; pfam03371"
                     /db_xref="CDD:460901"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Region          181..312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NAV1.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NAV1.1)"
     CDS             1..312
                     /gene="PRPF38A"
                     /gene_synonym="Prp38; PRP38A"
                     /coded_by="NM_032864.4:149..1087"
                     /db_xref="CCDS:CCDS567.1"
                     /db_xref="GeneID:84950"
                     /db_xref="HGNC:HGNC:25930"
                     /db_xref="MIM:617031"
ORIGIN      
        1 manrtvkdah sihgtnpqyl vekiirtriy eskywkeecf gltaelvvdk amelrfvggv
       61 yggnikptpf lcltlkmlqi qpekdiivef iknedfkyvr mlgalymrlt gtaidcykyl
      121 eplyndyrki ksqnrngefe lmhvdefide llhservcdi ilprlqkryv leeaeqlepr
      181 vsaleedmdd vesseeeeee deklervpsp dhrrrsyrdl dkprrsptlr yrrsrsrspr
      241 rrsrspkrrs psprrerhrs ksprrhrsrs rdrrhrsrsk spghhrshrh rshskspers
      301 kkshkksrrg ne
//
LOCUS       NP_001354660             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354660
VERSION     NP_001354660.1
DBSOURCE    REFSEQ: accession NM_001367731.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (15), as well as variants 3, 4,
            9-14, and 16-20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.52028.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162328, SAMEA2163623
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367731.1:321..1796"
                     /note="isoform c is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_006040                 98 aa            linear   PRI 20-NOV-2025
DEFINITION  snRNA-activating protein complex subunit 5 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006040
VERSION     NP_006040.1
DBSOURCE    REFSEQ: accession NM_006049.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 98)
  AUTHORS   Sun,J., Li,X., Hou,X., Cao,S., Cao,W., Zhang,Y., Song,J., Wang,M.,
            Wang,H., Yan,X., Li,Z., Roeder,R.G. and Wang,W.
  TITLE     Structural basis of human SNAPc recognizing proximal sequence
            element of snRNA promoter
  JOURNAL   Nat Commun 13 (1), 6871 (2022)
   PUBMED   36369505
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 98)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 98)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 98)
  AUTHORS   Gao,Y.F., Mao,X.Y., Zhu,T., Mao,C.X., Liu,Z.X., Wang,Z.B., Li,L.,
            Li,X., Yin,J.Y., Zhang,W., Zhou,H.H. and Liu,Z.Q.
  TITLE     COL3A1 and SNAP91: novel glioblastoma markers with diagnostic and
            prognostic value
  JOURNAL   Oncotarget 7 (43), 70494-70503 (2016)
   PUBMED   27655637
  REMARK    GeneRIF: Kaplan-Meir analysis of GSE7696 indicate that COL3A1 and
            SNAP91 correlated with survival.
REFERENCE   5  (residues 1 to 98)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   6  (residues 1 to 98)
  AUTHORS   Ma,B. and Hernandez,N.
  TITLE     A map of protein-protein contacts within the small nuclear
            RNA-activating protein complex SNAPc
  JOURNAL   J Biol Chem 276 (7), 5027-5035 (2001)
   PUBMED   11056176
REFERENCE   7  (residues 1 to 98)
  AUTHORS   Henry,R.W., Mittal,V., Ma,B., Kobayashi,R. and Hernandez,N.
  TITLE     SNAP19 mediates the assembly of a functional core promoter complex
            (SNAPc) shared by RNA polymerases II and III
  JOURNAL   Genes Dev 12 (17), 2664-2672 (1998)
   PUBMED   9732265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY005747.1, DB037177.1,
            CN347010.1 and BU679510.1.
            
            Summary: This gene encodes a subunit of the small nuclear RNA
            (snRNA)-activating protein complex that plays a role in the
            transcription of snRNA genes. This complex binds to the promoters
            of snRNA genes transcribed by either RNA polymerase II or III and
            recruits other regulatory factors to activate snRNA gene
            transcription. The encoded protein may play a role in stabilizing
            this complex. A pseudogene of this gene has been identified on
            chromosome 6. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 4 encode the same isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.172914.1,
                                           SRR5189655.82730.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..98
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..98
                     /product="snRNA-activating protein complex subunit 5
                     isoform 1"
                     /note="snRNA-activating protein complex subunit 5; SNAPc
                     subunit 5; SNAPc 19 kDa subunit; snRNA-activating protein
                     complex 19 kDa subunit"
                     /calculated_mol_wt=11197
     Region          1..83
                     /region_name="SNAPC5"
                     /note="snRNA-activating protein complex subunit 19, SNAPc
                     subunit 19; pfam15497"
                     /db_xref="CDD:464748"
     Region          73..98
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75971.1)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75971.1)"
     CDS             1..98
                     /gene="SNAPC5"
                     /gene_synonym="SNAP19"
                     /coded_by="NM_006049.4:32..328"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10217.1"
                     /db_xref="GeneID:10302"
                     /db_xref="HGNC:HGNC:15484"
                     /db_xref="MIM:605979"
ORIGIN      
        1 mlsrlqelrk eeetllrlka alhdqlnrlk veelalqsmi ssrrgdemls shtvpeqshd
       61 mlvhvdneas inqttlelst kshvteeeee eeeeesds
//
LOCUS       NP_001287785             205 aa            linear   PRI 20-NOV-2025
DEFINITION  fos-related antigen 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001287785
VERSION     NP_001287785.1
DBSOURCE    REFSEQ: accession NM_001300856.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Li,L., Li,D., Jin,J., Xu,F., He,N., Ren,Y., Wang,X., Tian,L.,
            Chen,B., Li,X., Chen,Z., Zhang,L., Qiao,L., Wang,L. and Wang,J.
  TITLE     FOSL1-mediated LINC01566 negatively regulates CD4+ T-cell
            activation in myasthenia gravis
  JOURNAL   J Neuroinflammation 21 (1), 197 (2024)
   PUBMED   39113081
  REMARK    GeneRIF: FOSL1-mediated LINC01566 negatively regulates CD4[+]
            T-cell activation in myasthenia gravis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Ramar,V., Guo,S., Hudson,B., Khedri,A., Guo,A.A., Li,J. and Liu,M.
  TITLE     Interaction of NF-kappaB and FOSL1 drives glioma stemness
  JOURNAL   Cell Mol Life Sci 81 (1), 255 (2024)
   PUBMED   38856747
  REMARK    GeneRIF: Interaction of NF-kappaB and FOSL1 drives glioma stemness.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Luo,X., Wang,J., Chen,Y., Zhou,X., Shao,Z., Liu,K. and Shang,Z.
  TITLE     Melatonin inhibits the stemness of head and neck squamous cell
            carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis
  JOURNAL   J Pineal Res 76 (2), e12940 (2024)
   PUBMED   38402581
  REMARK    GeneRIF: Melatonin inhibits the stemness of head and neck squamous
            cell carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Arts,J., Herr,I., Lansink,M., Angel,P. and Kooistra,T.
  TITLE     Cell-type specific DNA-protein interactions at the tissue-type
            plasminogen activator promoter in human endothelial and HeLa cells
            in vivo and in vitro
  JOURNAL   Nucleic Acids Res 25 (2), 311-317 (1997)
   PUBMED   9016559
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Courseaux,A., Grosgeorge,J., Gaudray,P., Pannett,A.A., Forbes,S.A.,
            Williamson,C., Bassett,D., Thakker,R.V., Teh,B.T., Farnebo,F.,
            Shepherd,J., Skogseid,B., Larsson,C., Giraud,S., Zhang,C.X.,
            Salandre,J. and Calender,A.
  TITLE     Definition of the minimal MEN1 candidate area based on a 5-Mb
            integrated map of proximal 11q13. The European Consortium on Men1,
            (GENEM 1; Groupe d'Etude des Neoplasies Endocriniennes Multiples de
            type 1)
  JOURNAL   Genomics 37 (3), 354-365 (1996)
   PUBMED   8938448
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Tsuchiya,H., Fujii,M., Niki,T., Tokuhara,M., Matsui,M. and Seiki,M.
  TITLE     Human T-cell leukemia virus type 1 Tax activates transcription of
            the human fra-1 gene through multiple cis elements responsive to
            transmembrane signals
  JOURNAL   J Virol 67 (12), 7001-7007 (1993)
   PUBMED   8230424
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Sinke,R.J., Tanigami,A., Nakamura,Y. and Geurts van Kessel,A.
  TITLE     Reverse mapping of the gene encoding the human fos-related
            antigen-1 (fra-1) within chromosome band 11q13
  JOURNAL   Genomics 18 (1), 165 (1993)
   PUBMED   8276409
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Matsui,M., Tokuhara,M., Konuma,Y., Nomura,N. and Ishizaki,R.
  TITLE     Isolation of human fos-related genes and their expression during
            monocyte-macrophage differentiation
  JOURNAL   Oncogene 5 (3), 249-255 (1990)
   PUBMED   2107490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ937004.1, CB123614.1,
            BC016648.1, AA120824.1 and AP006287.2.
            
            Summary: The Fos gene family consists of 4 members: FOS, FOSB,
            FOSL1, and FOSL2. These genes encode leucine zipper proteins that
            can dimerize with proteins of the JUN family, thereby forming the
            transcription factor complex AP-1. As such, the FOS proteins have
            been implicated as regulators of cell proliferation,
            differentiation, and transformation. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (4) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.197107.1,
                                           SRR14038191.951972.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..205
                     /product="fos-related antigen 1 isoform 4"
                     /note="FOS-like antigen-1; fos-related antigen 1; FOS like
                     1, AP-1 trancription factor subunit"
                     /calculated_mol_wt=21837
     Region          49..102
                     /region_name="bZIP_Fos"
                     /note="Basic leucine zipper (bZIP) domain of the oncogene
                     Fos (Fos): a DNA-binding and dimerization domain; cd14721"
                     /db_xref="CDD:269869"
     Region          49..101
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269869"
     Site            order(60,63..64,67..68,70..71,74..75,77..78,81..82,84..85,
                     88..89,91..92,95..96,98..99)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269869"
     Region          63..>184
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     CDS             1..205
                     /gene="FOSL1"
                     /gene_synonym="FRA; fra-1; FRA1"
                     /coded_by="NM_001300856.2:50..667"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:8061"
                     /db_xref="HGNC:HGNC:13718"
                     /db_xref="MIM:136515"
ORIGIN      
        1 mfrdfgepgp ssgngggygg paqppaaaqa aqqispeeee rrrvrrernk laaakcrnrr
       61 keltdflqae tdkledeksg lqreieelqk qkerlelvle ahrpickipe gakegdtgst
      121 sgtssppapc rpvpcislsp gpvlepealh tptlmttpsl tpftpslvft ypstpepcas
      181 ahrksssssg dpssdplgsp tllal
//
LOCUS       NP_006127                286 aa            linear   PRI 20-NOV-2025
DEFINITION  F-actin-capping protein subunit alpha-2 [Homo sapiens].
ACCESSION   NP_006127
VERSION     NP_006127.1
DBSOURCE    REFSEQ: accession NM_006136.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Zhang,X.M., Xu,K.L., Kong,J.H., Dong,G., Dong,S.J., Yang,Z.X.,
            Xu,S.J., Wang,L., Luo,S.Y., Zhang,Y.D., Zhou,C.C., Gu,W.Y. and
            Mei,S.Y.
  TITLE     Heterozygous CAPZA2 mutations cause global developmental delay,
            hypotonia with epilepsy: a case report and the literature review
  JOURNAL   J Hum Genet 69 (5), 197-203 (2024)
   PUBMED   38374166
  REMARK    GeneRIF: Heterozygous CAPZA2 mutations cause global developmental
            delay, hypotonia with epilepsy: a case report and the literature
            review.
            Review article
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Carman,P.J., Barrie,K.R., Rebowski,G. and Dominguez,R.
  TITLE     Structures of the free and capped ends of the actin filament
  JOURNAL   Science 380 (6651), 1287-1292 (2023)
   PUBMED   37228182
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Wang,D., Ye,Z., Wei,W., Yu,J., Huang,L., Zhang,H. and Yue,J.
  TITLE     Capping protein regulates endosomal trafficking by controlling
            F-actin density around endocytic vesicles and recruiting RAB5
            effectors
  JOURNAL   Elife 10, e65910 (2021)
   PUBMED   34796874
  REMARK    GeneRIF: Capping protein regulates endosomal trafficking by
            controlling F-actin density around endocytic vesicles and
            recruiting RAB5 effectors.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Inman,K.G., Yang,R., Rustandi,R.R., Miller,K.E., Baldisseri,D.M.
            and Weber,D.J.
  TITLE     Solution NMR structure of S100B bound to the high-affinity target
            peptide TRTK-12
  JOURNAL   J Mol Biol 324 (5), 1003-1014 (2002)
   PUBMED   12470955
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Miyagawa,Y., Tanaka,H., Iguchi,N., Kitamura,K., Nakamura,Y.,
            Takahashi,T., Matsumiya,K., Okuyama,A. and Nishimune,Y.
  TITLE     Molecular cloning and characterization of the human orthologue of
            male germ cell-specific actin capping protein alpha3 (cpalpha3)
  JOURNAL   Mol Hum Reprod 8 (6), 531-539 (2002)
   PUBMED   12029070
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Hart,M.C., Korshunova,Y.O. and Cooper,J.A.
  TITLE     Vertebrates have conserved capping protein alpha isoforms with
            specific expression patterns
  JOURNAL   Cell Motil Cytoskeleton 38 (2), 120-132 (1997)
   PUBMED   9331217
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J Biol Chem 270 (37), 21472-21479 (1995)
   PUBMED   7665558
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI553815.1, BC005338.1,
            U03851.1, BX386541.2 and AC002543.1.
            
            Summary: The protein encoded by this gene is a member of the
            F-actin capping protein alpha subunit family. It is the alpha
            subunit of the barbed-end actin binding protein Cap Z. By capping
            the barbed end of actin filaments, Cap Z regulates the growth of
            the actin filaments at the barbed end. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.91645.1,
                                           SRR1803616.33636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361183.8/ ENSP00000354947.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..286
                     /product="F-actin-capping protein subunit alpha-2"
                     /note="F-actin capping protein alpha-2 subunit; capZ
                     alpha-2; capping protein (actin filament) muscle Z-line,
                     alpha 2; capping actin protein of muscle Z-line alpha
                     subunit 2; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=32818
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P47755.3)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47755.3)"
     Region          17..282
                     /region_name="F-actin_cap_A"
                     /note="F-actin capping protein alpha subunit; pfam01267"
                     /db_xref="CDD:460142"
     CDS             1..286
                     /gene="CAPZA2"
                     /gene_synonym="CAPPA2; CAPZ"
                     /coded_by="NM_006136.3:26..886"
                     /db_xref="CCDS:CCDS5768.1"
                     /db_xref="GeneID:830"
                     /db_xref="HGNC:HGNC:1490"
                     /db_xref="MIM:601571"
ORIGIN      
        1 madleeqlsd eekvriaakf iihappgefn evfndvrlll nndnllrega ahafaqynld
       61 qftpvkiegy edqvlitehg dlgngkfldp knricfkfdh lrkeatdprp cevenavesw
      121 rtsvetalra yvkehypngv ctvygkkidg qqtiiacies hqfqaknfwn grwrsewkft
      181 itpsttqvvg ilkiqvhyye dgnvqlvshk diqdsltvsn evqtakefik iveaaeneyq
      241 taisenyqtm sdttfkalrr qlpvtrtkid wnkilsykig kemqna
//
LOCUS       NP_001230161             600 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform h [Homo sapiens].
ACCESSION   NP_001230161
VERSION     NP_001230161.1
DBSOURCE    REFSEQ: accession NM_001243232.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 600)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK095041.1 and AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (8) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            5' end of an exon compared to variant 3. The resulting isoform (h)
            has a shorter and distinct N-terminus and contains an alternate
            internal segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK095041.1, SRR1660809.96790.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..600
                     /product="transcription factor 4 isoform h"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=64472
     Region          491..575
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(499,503,505..507,509,514,535..536)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(512..513,516..517,519..520,523,527,537,540,544,547,
                     550..555)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..600
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243232.1:282..2084"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS58627.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mkdiffqfii arvrkcysls clhtlpvvpt lrktergsys sygresnlqg chqsllggdm
       61 dmgnpgtlsp tkpgsqyyqy ssnnprrrpl hssamevqtk kvrkvppglp ssvyapsast
      121 adynrdspgy psskpatstf pssffmqdgh hssdpwssss gmnqpgyagm lgnsshipqs
      181 ssycslhphe rlsypshssa dinsslppms tfhrsgtnhy stssctppan gtdsimanrg
      241 sgaagssqtg dalgkalasi yspdhtnnsf ssnpstpvgs ppslsagtav wsrnggqass
      301 spnyegplhs lqsriedrle rlddaihvlr nhavgpstam pgghgdmhgi igpshngamg
      361 glgsgygtgl lsanrhslmv gthredgval rgshsllpnq vpvpqlpvqs atspdlnppq
      421 dpyrgmppgl qgqsvssgss eiksddegde nlqdtkssed kkldddkkdi ksitrsrssn
      481 nddedltpeq kaerekerrm annarerlrv rdineafkel grmvqlhlks dkpqtkllil
      541 hqavavilsl eqqvrernln pkaaclkrre eekvsseppp lslagphpgm gdasnhmgqm
//
LOCUS       NP_003185                339 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA-box-binding protein isoform 1 [Homo sapiens].
ACCESSION   NP_003185
VERSION     NP_003185.1
DBSOURCE    REFSEQ: accession NM_003194.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   van Prooije,T.H., Pennings,M., Dorresteijn,L., Gardeitchik,T.,
            Odekerken,V.J.J., Oosterloo,M., Pedersen,A.,
            Verschuuren-Bemelmans,C.C., Vrancken,A., Kamsteeg,E.J. and van de
            Warrenburg,B.P.C.
  TITLE     A New Case Series Suggests That SCA48 (ATX/STUB1) Is Primarily a
            Monogenic Disorder
  JOURNAL   Mov Disord 39 (9), 1636-1640 (2024)
   PUBMED   38973070
  REMARK    GeneRIF: A New Case Series Suggests That SCA48 (ATX/STUB1) Is
            Primarily a Monogenic Disorder.
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Hoffman-Zacharska,D. and Sulek,A.
  TITLE     The New Face of Dynamic Mutation-The CAA [CAG]n CAA CAG Motif as a
            Mutable Unit in the TBP Gene Causative for Spino-Cerebellar Ataxia
            Type 17
  JOURNAL   Int J Mol Sci 25 (15), 8190 (2024)
   PUBMED   39125760
  REMARK    GeneRIF: The New Face of Dynamic Mutation-The CAA [CAG]n CAA CAG
            Motif as a Mutable Unit in the TBP Gene Causative for
            Spino-Cerebellar Ataxia Type 17.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Miyasaka,S., Kitada,R. and Kokubo,T.
  TITLE     Taf1 N-terminal domain 2 (TAND2) of TFIID promotes formation of
            stable and mobile unstable TBP-TATA complexes
  JOURNAL   Gene 889, 147800 (2023)
   PUBMED   37716588
  REMARK    GeneRIF: Taf1 N-terminal domain 2 (TAND2) of TFIID promotes
            formation of stable and mobile unstable TBP-TATA complexes.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Bernardini,A., Mukherjee,P., Scheer,E., Kamenova,I., Antonova,S.,
            Mendoza Sanchez,P.K., Yayli,G., Morlet,B., Timmers,H.T.M. and
            Tora,L.
  TITLE     Hierarchical TAF1-dependent co-translational assembly of the basal
            transcription factor TFIID
  JOURNAL   Nat Struct Mol Biol 30 (8), 1141-1152 (2023)
   PUBMED   37386215
  REMARK    GeneRIF: Hierarchical TAF1-dependent co-translational assembly of
            the basal transcription factor TFIID.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Toyoshima,Y., Onodera,O., Yamada,M., Tsuji,S. and Takahashi,H.
  TITLE     Spinocerebellar Ataxia Type 17
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301611
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Seto,E., Usheva,A., Zambetti,G.P., Momand,J., Horikoshi,N.,
            Weinmann,R., Levine,A.J. and Shenk,T.
  TITLE     Wild-type p53 binds to the TATA-binding protein and represses
            transcription
  JOURNAL   Proc Natl Acad Sci U S A 89 (24), 12028-12032 (1992)
   PUBMED   1465435
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Polymeropoulos,M.H., Rath,D.S., Xiao,H. and Merril,C.R.
  TITLE     Trinucleotide repeat polymorphism at the human transcription factor
            IID gene
  JOURNAL   Nucleic Acids Res 19 (15), 4307 (1991)
   PUBMED   1870994
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Kao,C.C., Lieberman,P.M., Schmidt,M.C., Zhou,Q., Pei,R. and
            Berk,A.J.
  TITLE     Cloning of a transcriptionally active human TATA binding factor
  JOURNAL   Science 248 (4963), 1646-1650 (1990)
   PUBMED   2194289
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM720195.1, BC109053.1,
            AL031259.1 and CA422572.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Initiation of transcription by RNA polymerase II requires
            the activities of more than 70 polypeptides. The protein that
            coordinates these activities is transcription factor IID (TFIID),
            which binds to the core promoter to position the polymerase
            properly, serves as the scaffold for assembly of the remainder of
            the transcription complex, and acts as a channel for regulatory
            signals. TFIID is composed of the TATA-binding protein (TBP) and a
            group of evolutionarily conserved proteins known as TBP-associated
            factors or TAFs. TAFs may participate in basal transcription, serve
            as coactivators, function in promoter recognition or modify general
            transcription factors (GTFs) to facilitate complex assembly and
            transcription initiation. This gene encodes TBP, the TATA-binding
            protein. A distinctive feature of TBP is a long string of
            glutamines in the N-terminus. This region of the protein modulates
            the DNA binding activity of the C terminus, and modulation of DNA
            binding affects the rate of transcription complex formation and
            initiation of transcription. The number of CAG repeats encoding the
            polyglutamine tract is usually 25-42, and expansion of the number
            of repeats to 45-66 increases the length of the polyglutamine
            string and is associated with spinocerebellar ataxia 17, a
            neurodegenerative disorder classified as a polyglutamine disease.
            Two transcript variants encoding different isoforms have been found
            for this gene. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315222.1, BC110341.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392092.7/ ENSP00000375942.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..339
                     /product="TATA-box-binding protein isoform 1"
                     /note="TATA-box binding protein N-terminal domain;
                     TATA-box factor; TATA sequence-binding protein;
                     transcription initiation factor TFIID TBP subunit"
                     /calculated_mol_wt=37567
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20226.2)"
     Region          58..95
                     /region_name="polyglutamine repeat"
                     /note="38Q repeat"
     Region          127..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P20226.2)"
     Region          162..338
                     /region_name="PLN00062"
                     /note="TATA-box-binding protein; Provisional"
                     /db_xref="CDD:177693"
     Region          165..241
                     /region_name="Repetitive region"
                     /note="1; propagated from UniProtKB/Swiss-Prot (P20226.2)"
     Region          255..332
                     /region_name="Repetitive region"
                     /note="2; propagated from UniProtKB/Swiss-Prot (P20226.2)"
     CDS             1..339
                     /gene="TBP"
                     /gene_synonym="GTF2D; GTF2D1; HDL4; SCA17; TBP1; TFIID"
                     /coded_by="NM_003194.5:244..1263"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5315.1"
                     /db_xref="GeneID:6908"
                     /db_xref="HGNC:HGNC:11588"
                     /db_xref="MIM:600075"
ORIGIN      
        1 mdqnnslppy aqglaspqga mtpgipifsp mmpygtgltp qpiqntnsls ileeqqrqqq
       61 qqqqqqqqqq qqqqqqqqqq qqqqqqqqqq qqqqqavaaa avqqstsqqa tqgtsgqapq
      121 lfhsqtltta plpgttplyp spmtpmtpit patpasessg ivpqlqnivs tvnlgckldl
      181 ktialrarna eynpkrfaav imrireprtt alifssgkmv ctgakseeqs rlaarkyarv
      241 vqklgfpakf ldfkiqnmvg scdvkfpirl eglvlthqqf ssyepelfpg liyrmikpri
      301 vllifvsgkv vltgakvrae iyeafeniyp ilkgfrktt
//
LOCUS       NP_001317939            1716 aa            linear   PRI 20-NOV-2025
DEFINITION  intersectin-1 isoform 5 [Homo sapiens].
ACCESSION   NP_001317939 XP_005261083
VERSION     NP_001317939.1
DBSOURCE    REFSEQ: accession NM_001331010.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1716)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1716)
  AUTHORS   Lan,C., Zhang,H., Wang,K., Liu,X., Zhao,Y., Guo,Z., Zhang,N.,
            Zhou,Y., Gao,M., Gu,F. and Ma,Y.
  TITLE     The alternative splicing of intersectin 1 regulated by PTBP1
            promotes human glioma progression
  JOURNAL   Cell Death Dis 13 (9), 835 (2022)
   PUBMED   36171198
  REMARK    GeneRIF: The alternative splicing of intersectin 1 regulated by
            PTBP1 promotes human glioma progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1716)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1716)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1716)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1716)
  AUTHORS   Sengar,A.S., Wang,W., Bishay,J., Cohen,S. and Egan,S.E.
  TITLE     The EH and SH3 domain Ese proteins regulate endocytosis by linking
            to dynamin and Eps15
  JOURNAL   EMBO J 18 (5), 1159-1171 (1999)
   PUBMED   10064583
REFERENCE   7  (residues 1 to 1716)
  AUTHORS   Yamabhai,M., Hoffman,N.G., Hardison,N.L., McPherson,P.S.,
            Castagnoli,L., Cesareni,G. and Kay,B.K.
  TITLE     Intersectin, a novel adaptor protein with two Eps15 homology and
            five Src homology 3 domains
  JOURNAL   J Biol Chem 273 (47), 31401-31407 (1998)
   PUBMED   9813051
REFERENCE   8  (residues 1 to 1716)
  AUTHORS   Guipponi,M., Scott,H.S., Chen,H., Schebesta,A., Rossier,C. and
            Antonarakis,S.E.
  TITLE     Two isoforms of a human intersectin (ITSN) protein are produced by
            brain-specific alternative splicing in a stop codon
  JOURNAL   Genomics 53 (3), 369-376 (1998)
   PUBMED   9799604
REFERENCE   9  (residues 1 to 1716)
  AUTHORS   Chen,H. and Antonarakis,S.E.
  TITLE     The SH3D1A gene maps to human chromosome 21q22.1-->q22.2
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 213-215 (1997)
   PUBMED   9465890
REFERENCE   10 (residues 1 to 1716)
  AUTHORS   Sparks,A.B., Hoffman,N.G., McConnell,S.J., Fowlkes,D.M. and
            Kay,B.K.
  TITLE     Cloning of ligand targets: systematic isolation of SH3
            domain-containing proteins
  JOURNAL   Nat Biotechnol 14 (6), 741-744 (1996)
   PUBMED   9630982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027846.1, AP000308.1,
            AP000311.1, KF511399.1, AP000312.2 and AP000313.1.
            
            On Sep 3, 2016 this sequence version replaced XP_005261083.1.
            
            Summary: The protein encoded by this gene is a cytoplasmic
            membrane-associated protein that indirectly coordinates endocytic
            membrane traffic with the actin assembly machinery. In addition,
            the encoded protein may regulate the formation of clathrin-coated
            vesicles and could be involved in synaptic vesicle recycling. This
            protein has been shown to interact with dynamin, CDC42, SNAP23,
            SNAP25, SPIN90, EPS15, EPN1, EPN2, and STN2. Multiple transcript
            variants encoding different isoforms have been found for this gene,
            but the full-length nature of only two of them have been
            characterized so far. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC116185.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..1716
                     /product="intersectin-1 isoform 5"
                     /note="human intersectin-SH3 domain-containing protein
                     SH3P17; Src homology 3 domain-containing protein; SH3
                     domain-containing protein 1A; intersectin 1 (SH3 domain
                     protein)"
                     /calculated_mol_wt=194692
     Region          14..108
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          214..309
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0R4; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          322..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          326..702
                     /region_name="KLERQ"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          <363..>684
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          650..701
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE9; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          744..798
                     /region_name="SH3_Intersectin1_1"
                     /note="First Src homology 3 domain (or SH3A) of
                     Intersectin-1; cd11987"
                     /db_xref="CDD:212920"
     Site            order(749,751,754,758,778..779,792,794..795)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212920"
     Region          798..912
                     /region_name="INTAP"
                     /note="Intersectin and clathrin adaptor AP2 binding
                     region; pfam16617"
                     /db_xref="CDD:435467"
     Region          831..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0R4; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            897
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          912..963
                     /region_name="SH3_Intersectin1_2"
                     /note="Second Src homology 3 domain (or SH3B) of
                     Intersectin-1; cd11989"
                     /db_xref="CDD:212922"
     Site            order(917,919,922,926,943..944,957,959..960)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212922"
     Site            973
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE9; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            981
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            990
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          1001..1052
                     /region_name="SH3_Intersectin1_3"
                     /note="Third Src homology 3 domain (or SH3C) of
                     Intersectin-1; cd11991"
                     /db_xref="CDD:212924"
     Site            order(1006,1008,1011,1015,1032..1033,1046,1048..1049)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212924"
     Region          1069..1133
                     /region_name="SH3_Intersectin1_4"
                     /note="Fourth Src homology 3 domain (or SH3D) of
                     Intersectin-1; cd11993"
                     /db_xref="CDD:212926"
     Region          1069..1133
                     /region_name="Required for interaction with FCHSD2.
                     /evidence=ECO:0000269|PubMed:29887380"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            order(1078,1080,1083,1087,1105..1106,1124,1126..1127)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212926"
     Region          1099..1122
                     /region_name="Bipartite nuclear localization signal, in
                     isoform 2. /evidence=ECO:0000269|PubMed:29599122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            1132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            1139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          1153..1206
                     /region_name="SH3_Intersectin1_5"
                     /note="Fifth Src homology 3 domain (or SH3E) of
                     Intersectin-1; cd11995"
                     /db_xref="CDD:212928"
     Site            order(1159,1161,1164,1168,1186..1187,1200,1202..1203)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212928"
     Region          1233..1416
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(1239,1243,1339,1367..1368,1371..1372,1374..1375,
                     1378..1379,1382..1383,1386,1412,1416)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1435..1577
                     /region_name="PH_13"
                     /note="Pleckstrin homology domain; pfam16652"
                     /db_xref="CDD:465218"
     Region          1577..1711
                     /region_name="C2_Intersectin"
                     /note="C2 domain present in Intersectin; cd08375"
                     /db_xref="CDD:176021"
     Site            order(1613,1660,1662,1668)
                     /site_type="other"
                     /note="putative Ca2+ binding site [ion binding]"
                     /db_xref="CDD:176021"
     Site            1640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0R4; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     CDS             1..1716
                     /gene="ITSN1"
                     /gene_synonym="ITSN; SH3D1A; SH3P17"
                     /coded_by="NM_001331010.2:246..5396"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82664.1"
                     /db_xref="GeneID:6453"
                     /db_xref="HGNC:HGNC:6183"
                     /db_xref="MIM:602442"
ORIGIN      
        1 maqfptpfgg sldiwaitve erakhdqqfh slkpisgfit gdqarnfffq sglpqpvlaq
       61 iwaladmnnd grmdqvefsi amkliklklq gyqlpsalpp vmkqqpvais sapafgmggi
      121 asmppltava pvpmgsipvv gmsptlvssv ptaavpplan gappviqplp afahpaatlp
      181 ksssfsrsgp gsqlntklqk aqsfdvasvp pvaewavpqs srlkyrqlfn shdktmsghl
      241 tgpqartilm qsslpqaqla siwnlsdidq dgkltaeefi lamhlidvam sgqplppvlp
      301 peyippsfrr vrsgsgisvi sstsvdqrlp eepvledeqq qlekklpvtf edkkrenfer
      361 gnlelekrrq alleqqrkeq erlaqlerae qerkererqe qerkrqlele kqlekqrele
      421 rqreeerrke ierreaakre lerqrqlewe rnrrqellnq rnkeqedivv lkakkktlef
      481 elealndkkh qlegklqdir crlttqrqei estnksrelr iaeithlqqq lqesqqmlgr
      541 lipekqilnd qlkqvqqnsl hrdslvtlkr aleakelarq hlrdqldeve ketrsklqei
      601 difnnqlkel reihnkqqlq kqksmeaerl kqkeqerkii elekqkeeaq rraqerdkqw
      661 lehvqqedeh qrprklheee klkreesvkk kdgeekgkqe aqdklgrlfh qhqepakpav
      721 qapwstaekg pltisaqenv kvvyyralyp fesrshdeit iqpgdivmvd esqtgepgwl
      781 ggelkgktgw fpanyaekip enevpapvkp vtdstsapap klalretpap lavtssepst
      841 tpnnwadfss twptstnekp etdnwdawaa qpsltvpsag qlrqrsaftp atatgsspsp
      901 vlgqgekveg lqaqalypwr akkdnhlnfn kndvitvleq qdmwwfgevq gqkgwfpksy
      961 vklisgpirk stsmdsgsse spaslkrvas paakpvvsge efiamytyes seqgdltfqq
     1021 gdvilvtkkd gdwwtgtvgd kagvfpsnyv rlkdsegsgt agktgslgkk peiaqviasy
     1081 tatgpeqltl apgqlilirk knpggwwege lqargkkrqi gwfpanyvkl lspgtskitp
     1141 teppkstala avcqvigmyd ytaqnddela fnkgqiinvl nkedpdwwkg evngqvglfp
     1201 snyvklttdm dpsqqwcsdl hlldmltpte rkrqgyihel ivteenyvnd lqlvteifqk
     1261 plmesellte kevamifvnw kelimcnikl lkalrvrkkm sgekmpvkmi gdilsaqlph
     1321 mqpyirfcsr qlngaaliqq ktdeapdfke fvkrlamdpr ckgmplssfi lkpmqrvtry
     1381 pliiknilen tpenhpdhsh lkhalekaee lcsqvnegvr ekensdrlew iqahvqcegl
     1441 seqlvfnsvt nclgprkflh sgklykaksn kelygflfnd fllltqitkp lgssgtdkvf
     1501 spksnlqykm yktpiflnev lvklptdpsg depifhishi drvytlraes inertawvqk
     1561 ikaaselyie tekkkrekay lvrsqratgi grlmvnvveg ielkpcrshg ksnpycevtm
     1621 gsqchitkti qdtlnpkwns ncqffirdle qevlcitvfe rdqfspddfl grteirvadi
     1681 kkdqgskgpv tkclllhevp tgeivvrldl qlfdep
//
LOCUS       NP_001258906             426 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 25 isoform 1 [Homo sapiens].
ACCESSION   NP_001258906
VERSION     NP_001258906.1
DBSOURCE    REFSEQ: accession NM_001271977.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Chen,K.Q., Lei,G.L., Ke,B.Y., Chen,L., Wang,Z.B. and Wang,S.Z.
  TITLE     STK25: a viable therapeutic target for cancer treatments?
  JOURNAL   Anticancer Drugs 34 (9), 995-1001 (2023)
   PUBMED   36728989
  REMARK    GeneRIF: STK25: a viable therapeutic target for cancer treatments?
            Review article
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Zhang,X., Wang,B.Z., Kim,M., Nash,T.R., Liu,B., Rao,J., Lock,R.,
            Tamargo,M., Soni,R.K., Belov,J., Li,E., Vunjak-Novakovic,G. and
            Fine,B.
  TITLE     STK25 inhibits PKA signaling by phosphorylating PRKAR1A
  JOURNAL   Cell Rep 40 (7), 111203 (2022)
   PUBMED   35977512
  REMARK    GeneRIF: STK25 inhibits PKA signaling by phosphorylating PRKAR1A.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Chen,J., Gao,P., Peng,L., Liu,T., Wu,F., Xu,K., Chen,L., Tan,F.,
            Xing,P., Wang,Z., Di,J., Jiang,B. and Su,X.
  TITLE     Downregulation of STK25 promotes autophagy via the Janus kinase
            2/signal transducer and activator of transcription 3 pathway in
            colorectal cancer
  JOURNAL   Mol Carcinog 61 (6), 572-586 (2022)
   PUBMED   35349179
  REMARK    GeneRIF: Downregulation of STK25 promotes autophagy via the Janus
            kinase 2/signal transducer and activator of transcription 3 pathway
            in colorectal cancer.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Findlay,G.M., Yan,L., Procter,J., Mieulet,V. and Lamb,R.F.
  TITLE     A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of
            mTOR signalling
  JOURNAL   Biochem J 403 (1), 13-20 (2007)
   PUBMED   17253963
  REMARK    GeneRIF: Ste20 family member (MAP4K3) that is required for maximal
            S6K (S6 kinase)/4E-BP1 [eIF4E (eukaryotic initiation factor 4E)
            that is required for maximal S6K (S6 kinase).
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Preisinger,C., Short,B., De Corte,V., Bruyneel,E., Haas,A.,
            Kopajtich,R., Gettemans,J. and Barr,F.A.
  TITLE     YSK1 is activated by the Golgi matrix protein GM130 and plays a
            role in cell migration through its substrate 14-3-3zeta
  JOURNAL   J Cell Biol 164 (7), 1009-1020 (2004)
   PUBMED   15037601
  REMARK    GeneRIF: 14-3-3zeta is a specific substrate for YSK1 that localizes
            to the Golgi apparatus, and potentially links YSK1 signaling at the
            Golgi apparatus with protein transport.
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Osada,S., Izawa,M., Saito,R., Mizuno,K., Suzuki,A., Hirai,S. and
            Ohno,S.
  TITLE     YSK1, a novel mammalian protein kinase structurally related to
            Ste20 and SPS1, but is not involved in the known MAPK pathways
  JOURNAL   Oncogene 14 (17), 2047-2057 (1997)
   PUBMED   9160885
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Pombo,C.M., Bonventre,J.V., Molnar,A., Kyriakis,J. and Force,T.
  TITLE     Activation of a human Ste20-like kinase by oxidant stress defines a
            novel stress response pathway
  JOURNAL   EMBO J 15 (17), 4537-4546 (1996)
   PUBMED   8887545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC091505.1, BC007852.2,
            HY315908.1 and AC110299.3.
            
            Summary: This gene encodes a member of the germinal centre kinase
            III (GCK III) subfamily of the sterile 20 superfamily of kinases.
            The encoded enzyme plays a role in serine-threonine liver kinase B1
            (LKB1) signaling pathway to regulate neuronal polarization and
            morphology of the Golgi apparatus. The protein is translocated from
            the Golgi apparatus to the nucleus in response to chemical anoxia
            and plays a role in regulation of cell death. A pseudogene
            associated with this gene is located on chromosome 18. Multiple
            alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 4 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC091505.1, SRR11853566.16839.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316586.9/ ENSP00000325748.4
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..426
                     /product="serine/threonine-protein kinase 25 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 25; Ste20, yeast
                     homolog; ste20-like kinase; ste20/oxidant stress response
                     kinase 1; sterile 20/oxidant stress-response kinase 1"
                     /calculated_mol_wt=47981
     Region          15..291
                     /region_name="STKc_STK25"
                     /note="Catalytic domain of Serine/Threonine Kinase 25
                     (also called Yeast Sps1/Ste20-related kinase 1); cd06642"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,79,95..98,101..102,105,140,142..145,
                     147,157..158,161,175..178,180,207,216)
                     /site_type="active"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,66,79,95..98,101..102,105,144..145,
                     147,158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270810"
     Site            order(29..30,140,142..144,161,175..178,180,207,216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270810"
     Site            157..180
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270810"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15037601; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2W1; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Region          291..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00506.1)"
     CDS             1..426
                     /gene="STK25"
                     /gene_synonym="SOK1; YSK1"
                     /coded_by="NM_001271977.2:243..1523"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2549.1"
                     /db_xref="GeneID:10494"
                     /db_xref="HGNC:HGNC:11404"
                     /db_xref="MIM:602255"
ORIGIN      
        1 mahlrgfanq hsrvdpeelf tkldrigkgs fgevykgidn htkevvaiki idleeaedei
       61 ediqqeitvl sqcdspyitr yfgsylkstk lwiimeylgg gsaldllkpg pleetyiati
      121 lreilkgldy lhserkihrd ikaanvllse qgdvkladfg vagqltdtqi krntfvgtpf
      181 wmapevikqs aydfkadiws lgitaielak geppnsdlhp mrvlflipkn spptlegqhs
      241 kpfkefveac lnkdprfrpt akellkhkfi trytkktsfl telidrykrw kseghgeess
      301 sedsdidgea edgeqgpiwt fpptirpsph sklhkgtalh ssqkpaepvk rqprsqclst
      361 lvrpvfgelk ekhkqsggsv galeelenaf slaeescpgi sdklmvhlve rvqrfshnrn
      421 hltstr
//
LOCUS       NP_001008938            2032 aa            linear   PRI 20-NOV-2025
DEFINITION  cytoskeleton-associated protein 5 isoform a [Homo sapiens].
ACCESSION   NP_001008938
VERSION     NP_001008938.1
DBSOURCE    REFSEQ: accession NM_001008938.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2032)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2032)
  AUTHORS   Lakshmi,R.B., Nayak,P., Raz,L., Sarkar,A., Saroha,A., Kumari,P.,
            Nair,V.M., Kombarakkaran,D.P., Sajana,S., M,G. S, Agasti,S.S.,
            Paul,R., Ben-David,U. and Manna,T.K.
  TITLE     CKAP5 stabilizes CENP-E at kinetochores by regulating
            microtubule-chromosome attachments
  JOURNAL   EMBO Rep 25 (4), 1909-1935 (2024)
   PUBMED   38424231
  REMARK    GeneRIF: CKAP5 stabilizes CENP-E at kinetochores by regulating
            microtubule-chromosome attachments.
REFERENCE   3  (residues 1 to 2032)
  AUTHORS   Wang,Y., Ma,X., Wang,S., Li,Z., Wang,F., Tian,X., Fu,H., Xing,G.,
            Sun,L. and Wang,W.
  TITLE     Competing endogenous RNA analysis reveals the regulatory potency of
            CKAP5 in HPV+ HNSCC
  JOURNAL   Oral Dis 29 (8), 3152-3156 (2023)
   PUBMED   35710876
  REMARK    GeneRIF: Competing endogenous RNA analysis reveals the regulatory
            potency of CKAP5 in HPV+ HNSCC.
REFERENCE   4  (residues 1 to 2032)
  AUTHORS   Rajeev,R., Mukhopadhyay,S., Bhagyanath,S., Devu Priya,M.R.S. and
            Manna,T.K.
  TITLE     TACC3-ch-TOG interaction regulates spindle microtubule assembly by
            controlling centrosomal recruitment of gamma-TuRC
  JOURNAL   Biosci Rep 43 (3) (2023)
   PUBMED   36790370
  REMARK    GeneRIF: TACC3-ch-TOG interaction regulates spindle microtubule
            assembly by controlling centrosomal recruitment of gamma-TuRC.
REFERENCE   5  (residues 1 to 2032)
  AUTHORS   Rossi,F., Beltran,M., Damizia,M., Grelloni,C., Colantoni,A.,
            Setti,A., Di Timoteo,G., Dattilo,D., Centron-Broco,A.,
            Nicoletti,C., Fanciulli,M., Lavia,P. and Bozzoni,I.
  TITLE     Circular RNA ZNF609/CKAP5 mRNA interaction regulates microtubule
            dynamics and tumorigenicity
  JOURNAL   Mol Cell 82 (1), 75-89 (2022)
   PUBMED   34942120
  REMARK    GeneRIF: Circular RNA ZNF609/CKAP5 mRNA interaction regulates
            microtubule dynamics and tumorigenicity.
REFERENCE   6  (residues 1 to 2032)
  AUTHORS   Lauffart,B., Howell,S.J., Tasch,J.E., Cowell,J.K. and Still,I.H.
  TITLE     Interaction of the transforming acidic coiled-coil 1 (TACC1)
            protein with ch-TOG and GAS41/NuBI1 suggests multiple
            TACC1-containing protein complexes in human cells
  JOURNAL   Biochem J 363 (Pt 1), 195-200 (2002)
   PUBMED   11903063
  REMARK    GeneRIF: Interaction of the transforming acidic coiled-coil 1
            (TACC1) protein with ch-TOG and GAS41/NuBI1 suggests multiple
            TACC1-containing protein complexes in human cells
REFERENCE   7  (residues 1 to 2032)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   8  (residues 1 to 2032)
  AUTHORS   Spittle,C., Charrasse,S., Larroque,C. and Cassimeris,L.
  TITLE     The interaction of TOGp with microtubules and tubulin
  JOURNAL   J Biol Chem 275 (27), 20748-20753 (2000)
   PUBMED   10770946
REFERENCE   9  (residues 1 to 2032)
  AUTHORS   Charrasse,S., Mazel,M., Taviaux,S., Berta,P., Chow,T. and
            Larroque,C.
  TITLE     Characterization of the cDNA and pattern of expression of a new
            gene over-expressed in human hepatomas and colonic tumors
  JOURNAL   Eur J Biochem 234 (2), 406-413 (1995)
   PUBMED   8536682
REFERENCE   10 (residues 1 to 2032)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP282525.1, BC120869.1,
            D43948.1, CB052595.1, BM980015.1 and AC115088.6.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a cytoskeleton-associated protein which
            belongs to the TOG/XMAP215 family. The N-terminal half of this
            protein contains a microtubule-binding domain and the C-terminal
            half contains a KXGS motif for binding tubulin dimers. This protein
            has two distinct roles in spindle formation; it protects
            kinetochore microtubules from depolymerization and plays an
            essential role in centrosomal microtubule assembly. This protein
            may be necessary for the proper interaction of microtubules with
            the cell cortex for directional cell movement. It also plays a role
            in translation of the myelin basic protein (MBP) mRNA by
            interacting with heterogeneous nuclear ribonucleoprotein (hnRNP)
            A2, which associates with MBP. Alternatively spliced transcript
            variants encoding different isoforms have been identified.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.45127.1,
                                           SRR1803612.265289.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000529230.6/ ENSP00000432768.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2032
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..2032
                     /product="cytoskeleton-associated protein 5 isoform a"
                     /note="colonic and hepatic tumor over-expressed gene
                     protein; colonic and hepatic tumor overexpressed gene
                     protein"
                     /calculated_mol_wt=225365
     Region          1..223
                     /region_name="TOG 1.
                     /evidence=ECO:0000305|PubMed:24966168"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14008.3)"
     Region          268..502
                     /region_name="TOG 2.
                     /evidence=ECO:0000305|PubMed:24966168"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          516..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          588..817
                     /region_name="TOG 3.
                     /evidence=ECO:0000305|PubMed:24966168"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          811..851
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Site            816
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14008.3)"
     Site            845
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14008.3)"
     Region          853..1081
                     /region_name="TOG 4.
                     /evidence=ECO:0000305|PubMed:24966168"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1077..1160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1193..1428
                     /region_name="TOG 5.
                     /evidence=ECO:0000305|PubMed:24966168"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1422..1443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Site            1469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1801..1822
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Site            1861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1932..1957
                     /region_name="Interaction with TACC3.
                     /evidence=ECO:0000269|PubMed:25596274"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     Region          1949..2032
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14008.3)"
     CDS             1..2032
                     /gene="CKAP5"
                     /gene_synonym="ch-TOG; CHTOG; MSPS; TOG; TOGp"
                     /coded_by="NM_001008938.4:99..6197"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31477.1"
                     /db_xref="GeneID:9793"
                     /db_xref="HGNC:HGNC:28959"
                     /db_xref="MIM:611142"
ORIGIN      
        1 mgddsewlkl pvdqkcehkl wkarlsgyee alkifqkikd ekspewskfl glikkfvtds
       61 navvqlkgle aalvyvenah vagkttgevv sgvvskvfnq pkakakelgi eiclmyieie
      121 kgeavqeell kgldnknpki ivacietlrk alsefgskii llkpiikvlp klfesrekav
      181 rdeakliave iyrwirdalr pplqninsvq lkeleeewvk lptsaprptr flrsqqelea
      241 kleqqqsagg daegggddgd evpqidayel leaveilskl pkdfydkiea kkwqerkeal
      301 esvevliknp kleagdyadl vkalkkvvgk dtnvmlvala akcltglavg lrkkfgqyag
      361 hvvptilekf kekkpqvvqa lqeaidaifl tttlqnised vlavmdnknp tikqqtslfi
      421 arsfrhctas tlpksllkpf caallkhind sapevrdaaf ealgtalkvv gekavnpfla
      481 dvdklkldki kecsekveli hgkkaglaad kkefkplpgr taasgaagdk dtkdisapkp
      541 gplkkapaak aggppkkgkp aapggagntg tknkkgletk eivepelsie vceekasavl
      601 pptciqllds snwkerlacm eefqkavelm drtempcqal vrmlakkpgw ketnfqvmqm
      661 klhivaliaq kgnfsktsaq vvldglvdki gdvkcgnnak eamtaiaeac mlpwtaeqvv
      721 smafsqknpk nqsetlnwls naikefgfsg lnvkafisnv ktalaatnpa vrtaaitllg
      781 vmylyvgpsl rmffedekpa llsqidaefe kmqgqsppap trgiskhsts gtdegedgde
      841 pddgsndvvd llprteisdk itselvskig dknwkirkeg ldevagiind akfiqpnige
      901 lptalkgrln dsnkilvqqt lnilqqlava mgpnikqhvk nlgipiitvl gdsknnvraa
      961 alatvnawae qtgmkewleg edlseelkke npflrqellg wlaeklptlr stptdlilcv
     1021 phlyscledr ngdvrkkaqd alpffmmhlg yekmakatgk lkptskdqvl amlekakvnm
     1081 pakpapptka tskpmggsap akfqpasapa edcissstep kpdpkkakap glsskaksaq
     1141 gkkmpsktsl kededksgpi fivvpngkeq rmkdekglkv lkwnfttprd eyieqlktqm
     1201 sscvakwlqd emfhsdfqhh nkalavmvdh lesekegvig cldlilkwlt lrffdtntsv
     1261 lmkaleylkl lftllseeey hlteneassf ipylvvkvge pkdvirkdvr ailnrmclvy
     1321 paskmfpfim egtksknskq raecleelgc lvesygmnvc qptpgkalke iavhigdrdn
     1381 avrnaalnti vtvynvhgdq vfklignlse kdmsmleeri krsakrpsaa pikqveekpq
     1441 raqnissnan mlrkgpaedm ssklnqarsm sghpeaaqmv rrefqldlde iendngtvrc
     1501 empelvqhkl ddifepvlip epkiravsph fddmhsntas tinfiisqva sgdintsiqa
     1561 ltqidevlrq edkaeamsgh idqfliatfm qlrliynthm adeklekdei iklysciign
     1621 mislfqiesl areastgvlk dlmhglitlm ldsriedlee gqqvirsvnl lvvkvleksd
     1681 qtnilsallv llqdsllata sspkfselvm kclwrmvrll pdtinsinld rilldihifm
     1741 kvfpkeklkq cksefpirtl ktllhtlckl kgpkildhlt midnknesel eahlcrmmkh
     1801 smdqtgsksd ketekgasri deksskakvn dflaeifkki gskentkegl aelyeykkky
     1861 sdadiepflk nssqffqsyv erglrvieme regkgrists tgispqmevt cvptptstvs
     1921 signtngeev gpsvylerlk ilrqrcgldn tkqddrpplt sllskpavpt vasstdmlhs
     1981 klsqlresre qhqhsdldsn qthssgtvts ssstaniddl kkrlerikss rk
//
LOCUS       NP_001290367             286 aa            linear   PRI 20-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_001290367
VERSION     NP_001290367.1
DBSOURCE    REFSEQ: accession NM_001303438.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP398345.1, AW340131.1,
            DB160394.1, BP209696.1, AK056946.1 and CA312679.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP209696.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_001303438.1:1120..1980"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_570981                161 aa            linear   PRI 20-NOV-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase-like 3 isoform PPIL3b [Homo
            sapiens].
ACCESSION   NP_570981
VERSION     NP_570981.1
DBSOURCE    REFSEQ: accession NM_130906.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Gong,Z., Mu,Y., Chen,J., Chu,H., Lian,P., Wang,C., Wang,J. and
            Jiang,L.
  TITLE     Expression and Significance of Cyclophilin J in Primary Gastric
            Adenocarcinoma
  JOURNAL   Anticancer Res 37 (8), 4475-4481 (2017)
   PUBMED   28739742
  REMARK    GeneRIF: Cyclophilin J expression was up-regulated in gastric
            carcinoma compared to normal gastric tissues.
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Chen,J., Liefke,R., Jiang,L., Wang,J., Huang,C., Gong,Z.,
            Schiene-Fischer,C. and Yu,L.
  TITLE     Biochemical Features of Recombinant Human Cyclophilin J
  JOURNAL   Anticancer Res 36 (3), 1175-1180 (2016)
   PUBMED   26977013
  REMARK    GeneRIF: CYPJ structurally resembles CYPA. It is sensitive to
            inhibition by CsA and plays a role in regulating cell growth,
            proliferation, and apoptosis.
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Qi,Z.Y., Hui,G.Z., Li,Y., Zhou,Z.X., Gu,S.H., Ying,K. and Xie,Y.
  TITLE     cDNA microarray in isolation of novel differentially expressed
            genes related to human glioma and clone of a novel full-length gene
  JOURNAL   Chin Med J (Engl) 118 (10), 799-805 (2005)
   PUBMED   15989758
  REMARK    GeneRIF: The novel full-length gene of human PPIL3 may be
            correlated with the formation of human glioma.
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Huang,L.L., Zhao,X.M., Huang,C.Q., Yu,L. and Xia,Z.X.
  TITLE     Structure of recombinant human cyclophilin J, a novel member of the
            cyclophilin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 3), 316-321 (2005)
   PUBMED   15735342
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Hu,H., Huang,C.Q., Liu,H.L., Han,Y., Yu,L. and Bi,R.C.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            human cyclophilin J
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 61 (Pt 2), 216-218
            (2005)
   PUBMED   16510998
  REMARK    GeneRIF: Human cyclophilin J, a new member of the cyclophilin
            family, has been expressed and crystallized.
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Zhou,Z., Ying,K., Dai,J., Tang,R., Wang,W., Huang,Y., Zhao,W.,
            Xie,Y. and Mao,Y.
  TITLE     Molecular cloning and characterization of a novel peptidylprolyl
            isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 231-236 (2001)
   PUBMED   11435694
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961908.1, AF271652.1 and
            AC005037.2.
            
            Summary: This gene encodes a member of the cyclophilin family.
            Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl
            imide bonds in oligopeptides. They have been proposed to act either
            as catalysts or as molecular chaperones in protein-folding events.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (PPIL3b) includes an alternate
            in-frame segment, compared to variant PPIL3a, resulting in a
            shorter protein (isoform PPIL3b), compared to isoform PPIL3a.
            Variants PPIL3b and PPIL3c encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.494166.1,
                                           SRR5189658.135973.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392283.9/ ENSP00000376107.4
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..161
                     /product="peptidyl-prolyl cis-trans isomerase-like 3
                     isoform PPIL3b"
                     /EC_number="5.2.1.8"
                     /note="cyclophilin J; peptidyl-prolyl cis-trans
                     isomerase-like 3; cyclophilin-like protein 3;
                     peptidylprolyl cis-trans isomerase-like protein 3;
                     PPIase-like protein 3; cyclophilin-like protein PPIL3;
                     rotamase PPIL3; peptidylprolyl isomerase
                     (cyclophilin)-like 3"
                     /calculated_mol_wt=18023
     Region          1..154
                     /region_name="Cyclophilin_PPIL3_like"
                     /note="Proteins similar to Human cyclophilin-like
                     peptidylprolyl cis- trans isomerase (PPIL3). Members of
                     this family lack a key residue important for cyclosporin
                     binding: the tryptophan residue corresponding to W121 in
                     human hCyP-18a; most members have a...; cd01928"
                     /db_xref="CDD:238909"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9H2H8.1)"
     Site            order(43..44,49,100,102,110)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:238909"
     Site            61
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9D6L8; propagated from
                     UniProtKB/Swiss-Prot (Q9H2H8.1)"
     CDS             1..161
                     /gene="PPIL3"
                     /gene_synonym="CYPJ"
                     /coded_by="NM_130906.3:193..678"
                     /note="isoform PPIL3b is encoded by transcript variant
                     PPIL3b"
                     /db_xref="CCDS:CCDS2333.1"
                     /db_xref="GeneID:53938"
                     /db_xref="HGNC:HGNC:9262"
                     /db_xref="MIM:615811"
ORIGIN      
        1 msvtlhtdvg dikievfcer tpktcenfla lcasnyyngc ifhrnikgfm vqtgdptgtg
       61 rggnsiwgkk fedeyseylk hnvrgvvsma nngpntngsq ffitygkqph ldmkytvfgk
      121 vidgletlde leklpvnekt yrplndvhik ditihanpfa q
//
LOCUS       NP_001230854             382 aa            linear   PRI 20-NOV-2025
DEFINITION  MAP kinase-activated protein kinase 3 [Homo sapiens].
ACCESSION   NP_001230854
VERSION     NP_001230854.1
DBSOURCE    REFSEQ: accession NM_001243925.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Ludwig,S., Engel,K., Hoffmeyer,A., Sithanandam,G., Neufeld,B.,
            Palm,D., Gaestel,M. and Rapp,U.R.
  TITLE     3pK, a novel mitogen-activated protein (MAP) kinase-activated
            protein kinase, is targeted by three MAP kinase pathways
  JOURNAL   Mol Cell Biol 16 (12), 6687-6697 (1996)
   PUBMED   8943323
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Clifton,A.D., Young,P.R. and Cohen,P.
  TITLE     A comparison of the substrate specificity of MAPKAP kinase-2 and
            MAPKAP kinase-3 and their activation by cytokines and cellular
            stress
  JOURNAL   FEBS Lett 392 (3), 209-214 (1996)
   PUBMED   8774846
REFERENCE   7  (residues 1 to 382)
  AUTHORS   McLaughlin,M.M., Kumar,S., McDonnell,P.C., Van Horn,S., Lee,J.C.,
            Livi,G.P. and Young,P.R.
  TITLE     Identification of mitogen-activated protein (MAP) kinase-activated
            protein kinase-3, a novel substrate of CSBP p38 MAP kinase
  JOURNAL   J Biol Chem 271 (14), 8488-8492 (1996)
   PUBMED   8626550
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Sithanandam,G., Latif,F., Duh,F.M., Bernal,R., Smola,U., Li,H.,
            Kuzmin,I., Wixler,V., Geil,L. and Shrestha,S.
  TITLE     3pK, a new mitogen-activated protein kinase-activated protein
            kinase located in the small cell lung cancer tumor suppressor gene
            region
  JOURNAL   Mol Cell Biol 16 (3), 868-876 (1996)
   PUBMED   8622688
  REMARK    Erratum:[Mol Cell Biol 1996 Apr;16(4):1880]
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Ben-Levy,R., Leighton,I.A., Doza,Y.N., Attwood,P., Morrice,N.,
            Marshall,C.J. and Cohen,P.
  TITLE     Identification of novel phosphorylation sites required for
            activation of MAPKAP kinase-2
  JOURNAL   EMBO J 14 (23), 5920-5930 (1995)
   PUBMED   8846784
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Lavoie,J.N., Lambert,H., Hickey,E., Weber,L.A. and Landry,J.
  TITLE     Modulation of cellular thermoresistance and actin filament
            stability accompanies phosphorylation-induced changes in the
            oligomeric structure of heat shock protein 27
  JOURNAL   Mol Cell Biol 15 (1), 505-516 (1995)
   PUBMED   7799959
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM848086.1, U09578.1,
            AC096920.2 and BE301676.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the Ser/Thr protein kinase
            family. This kinase functions as a mitogen-activated protein kinase
            (MAP kinase)- activated protein kinase. MAP kinases are also known
            as extracellular signal-regulated kinases (ERKs), act as an
            integration point for multiple biochemical signals. This kinase was
            shown to be activated by growth inducers and stress stimulation of
            cells. In vitro studies demonstrated that ERK, p38 MAP kinase and
            Jun N-terminal kinase were all able to phosphorylate and activate
            this kinase, which suggested the role of this kinase as an
            integrative element of signaling in both mitogen and stress
            responses. This kinase was reported to interact with, phosphorylate
            and repress the activity of E47, which is a basic helix-loop-helix
            transcription factor known to be involved in the regulation of
            tissue-specific gene expression and cell differentiation. Alternate
            splicing results in multiple transcript variants that encode the
            same protein. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.211140.1,
                                           SRR1660807.98658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621469.5/ ENSP00000478922.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..382
                     /product="MAP kinase-activated protein kinase 3"
                     /EC_number="2.7.11.1"
                     /note="MAPKAP kinase 3; chromosome 3p kinase;
                     mitogen-activated protein kinase-activated protein kinase
                     3"
                     /calculated_mol_wt=42856
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Region          39..304
                     /region_name="STKc_MAPKAPK3"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Mitogen-activated protein kinase-activated protein kinase
                     3; cd14172"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,125,127,165..166,168,
                     170..171,173,186..187,190,203..207,209)
                     /site_type="active"
                     /db_xref="CDD:271074"
     Site            order(50..55,58,71,73,98,118..121,171,173,186..187)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271074"
     Site            order(52..55,57,206..210,214,216,219,240,242..245,
                     259..260,262..263,287..288)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:271074"
     Site            order(54,125,127,165..166,168,170,190,203..207,209)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271074"
     Site            order(186..195,197..207)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271074"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000250|UniProtKB:Q3UMW7; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            251
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          307..343
                     /region_name="Autoinhibitory helix. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q16644.1)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          335..344
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          345..369
                     /region_name="p38 MAPK-binding site.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          350..353
                     /region_name="Bipartite nuclear localization signal 1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          357..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     Region          364..368
                     /region_name="Bipartite nuclear localization signal 2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16644.1)"
     CDS             1..382
                     /gene="MAPKAPK3"
                     /gene_synonym="3PK; MAPKAP-K3; MAPKAP3; MAPKAPK-3; MDPT3;
                     MK-3; MK3"
                     /coded_by="NM_001243925.2:144..1292"
                     /db_xref="CCDS:CCDS2832.1"
                     /db_xref="GeneID:7867"
                     /db_xref="HGNC:HGNC:6888"
                     /db_xref="MIM:602130"
ORIGIN      
        1 mdgetaeeqg gpvpppvapg gpglggapgg rrepkkyavt ddyqlskqvl glgvngkvle
       61 cfhrrtgqkc alkllydspk arqevdhhwq asggphivci ldvyenmhhg krclliimec
      121 meggelfsri qergdqafte reaaeimrdi gtaiqflhsh niahrdvkpe nllytskekd
      181 avlkltdfgf akettqnalq tpcytpyyva pevlgpekyd kscdmwslgv imyillcgfp
      241 pfysntgqai spgmkrrirl gqygfpnpew sevsedakql irlllktdpt erltitqfmn
      301 hpwinqsmvv pqtplhtarv lqedkdhwde vkeemtsala tmrvdydqvk ikdlktsnnr
      361 llnkrrkkqa gsssasqgcn nq
//
LOCUS       NP_001184252             175 aa            linear   PRI 20-NOV-2025
DEFINITION  HIRA-interacting protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001184252
VERSION     NP_001184252.1
DBSOURCE    REFSEQ: accession NM_001197323.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Ignatyeva,M., Patel,A.K.M., Ibrahim,A., Albiheyri,R.S., Zari,A.T.,
            Bahieldin,A., Bronner,C., Sabir,J.S.M. and Hamiche,A.
  TITLE     Identification and Characterization of HIRIP3 as a Histone H2A
            Chaperone
  JOURNAL   Cells 13 (3), 273 (2024)
   PUBMED   38334665
  REMARK    GeneRIF: Identification and Characterization of HIRIP3 as a Histone
            H2A Chaperone.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Kim,J.E., Tannenbaum,S.R. and White,F.M.
  TITLE     Global phosphoproteome of HT-29 human colon adenocarcinoma cells
  JOURNAL   J Proteome Res 4 (4), 1339-1346 (2005)
   PUBMED   16083285
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Lorain,S., Quivy,J.P., Monier-Gavelle,F., Scamps,C., Lecluse,Y.,
            Almouzni,G. and Lipinski,M.
  TITLE     Core histones and HIRIP3, a novel histone-binding protein, directly
            interact with WD repeat protein HIRA
  JOURNAL   Mol Cell Biol 18 (9), 5546-5556 (1998)
   PUBMED   9710638
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA716463.1, BC000588.2,
            BE207110.1, Z25386.1, BU629222.1, BX101682.1 and BM673568.1.
            
            Summary: The HIRA protein shares sequence similarity with Hir1p and
            Hir2p, the two corepressors of histone gene transcription
            characterized in the yeast, Saccharomyces cerevisiae. The
            structural features of the HIRA protein suggest that it may
            function as part of a multiprotein complex. Several cDNAs encoding
            HIRA-interacting proteins, or HIRIPs, have been identified. In
            vitro, the protein encoded by this gene binds HIRA, as well as H2B
            and H3 core histones, indicating that a complex containing
            HIRA-HIRIP3 could function in some aspects of chromatin and histone
            metabolism. Alternatively spliced transcript variants encoding
            distinct isoforms have been found for this gene.[provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, resulting in frame-shift, compared to variant 1. The
            resulting isoform (2) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.87083.1,
                                           SRR1660803.17246.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..175
                     /product="HIRA-interacting protein 3 isoform 2"
                     /calculated_mol_wt=19578
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     CDS             1..175
                     /gene="HIRIP3"
                     /coded_by="NM_001197323.1:492..1019"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58449.1"
                     /db_xref="GeneID:8479"
                     /db_xref="HGNC:HGNC:4917"
                     /db_xref="MIM:603365"
ORIGIN      
        1 marekemqef trsffrgrpd lstlthsivr rrylahsgrs hlepeekqal krlveeellk
       61 mqvdeaasre dkldltkkgk rpptpcsdpe rkrfrfnses gwlrspwrgp pgcdeaealh
      121 sglwcpsklq eavglllltq gapeyppgrt gsarhegypf prevsgpega egggs
//
LOCUS       NP_958850                688 aa            linear   PRI 20-NOV-2025
DEFINITION  complement C1s subcomponent isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_958850
VERSION     NP_958850.1
DBSOURCE    REFSEQ: accession NM_201442.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 688)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 688)
  AUTHORS   Yuan,D., Zheng,Z., Shen,C., Ye,J. and Zhu,L.
  TITLE     Cytoprotective effects of C1s enzyme in macrophages in
            atherosclerosis mediated through the LRP5 and Wnt/beta-catenin
            pathway
  JOURNAL   Mol Immunol 166, 29-38 (2024)
   PUBMED   38218080
  REMARK    GeneRIF: Cytoprotective effects of C1s enzyme in macrophages in
            atherosclerosis mediated through the LRP5 and Wnt/beta-catenin
            pathway.
REFERENCE   3  (residues 1 to 688)
  AUTHORS   Yadav,M.K., Maharana,J., Yadav,R., Saha,S., Sarma,P., Soni,C.,
            Singh,V., Saha,S., Ganguly,M., Li,X.X., Mohapatra,S., Mishra,S.,
            Khant,H.A., Chami,M., Woodruff,T.M., Banerjee,R., Shukla,A.K. and
            Gati,C.
  TITLE     Molecular basis of anaphylatoxin binding, activation, and signaling
            bias at complement receptors
  JOURNAL   Cell 186 (22), 4956-4973 (2023)
   PUBMED   37852260
REFERENCE   4  (residues 1 to 688)
  AUTHORS   Alshekaili,J., Nasr,I., Al-Rawahi,M., Ansari,Z., Al Rahbi,N., Al
            Balushi,H., Al-Zadjali,S., Al Kindi,M., Al-Maawali,A. and Cook,M.C.
  TITLE     A homozygous loss-of-function C1S mutation is associated with
            Kikuchi-Fujimoto disease
  JOURNAL   Clin Immunol 252, 109646 (2023)
   PUBMED   37209807
  REMARK    GeneRIF: A homozygous loss-of-function C1S mutation is associated
            with Kikuchi-Fujimoto disease.
REFERENCE   5  (residues 1 to 688)
  AUTHORS   Amano,M.T., Ferriani,V.P., Florido,M.P., Reis,E.S., Delcolli,M.I.,
            Azzolini,A.E., Assis-Pandochi,A.I., Sjoholm,A.G., Farah,C.S.,
            Jensenius,J.C. and Isaac,L.
  TITLE     Genetic analysis of complement C1s deficiency associated with
            systemic lupus erythematosus highlights alternative splicing of
            normal C1s gene
  JOURNAL   Mol Immunol 45 (6), 1693-1702 (2008)
   PUBMED   18062908
  REMARK    GeneRIF: There are splice variants of C1s mRNA transcripts in
            normal human cells
REFERENCE   6  (residues 1 to 688)
  AUTHORS   Kapferer-Seebacher,I., van Dijk,F.S. and Zschocke,J.
  TITLE     Periodontal Ehlers-Danlos Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34324282
REFERENCE   7  (residues 1 to 688)
  AUTHORS   Reboul,A., Thielens,N., Villiers,M.B. and Colomb,M.G.
  TITLE     Purification of human complement subcomponent C4. C4 cleavage by
            C1s
  JOURNAL   FEBS Lett 103 (1), 156-161 (1979)
   PUBMED   467643
REFERENCE   8  (residues 1 to 688)
  AUTHORS   Kerr,M.A. and Porter,R.R.
  TITLE     The purification and properties of the second component of human
            complement
  JOURNAL   Biochem J 171 (1), 99-107 (1978)
   PUBMED   417728
REFERENCE   9  (residues 1 to 688)
  AUTHORS   Nagasawa,S. and Stroud,R.M.
  TITLE     Cleavage of C2 by C1s into the antigenically distinct fragments C2a
            and C2b: demonstration of binding of C2b to C4b
  JOURNAL   Proc Natl Acad Sci U S A 74 (7), 2998-3001 (1977)
   PUBMED   70787
REFERENCE   10 (residues 1 to 688)
  AUTHORS   Ziccardi,R.J. and Cooper,N.R.
  TITLE     Physicochemical and functional characterization of the C1r subunit
            of the first complement component
  JOURNAL   J Immunol 116 (2), 496-503 (1976)
   PUBMED   814163
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA638990.1 and BC056903.1.
            
            Summary: This gene encodes a serine protease, which is a major
            constituent of the human complement subcomponent C1. C1s associates
            with two other complement components C1r and C1q in order to yield
            the first component of the serum complement system. Defects in this
            gene are the cause of selective C1s deficiency. [provided by
            RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Both variants 1 and
            2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC056903.1, SRR1803616.253445.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..688
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..688
                     /product="complement C1s subcomponent isoform 1
                     preproprotein"
                     /EC_number="3.4.21.42"
                     /note="complement C1s subcomponent; basic proline-rich
                     peptide IB-1; C1 esterase; complement component 1
                     subcomponent s; complement component 1, s subcomponent"
                     /calculated_mol_wt=74888
     sig_peptide     1..15
                     /note="/evidence=ECO:0000269|PubMed:3007145; propagated
                     from UniProtKB/Swiss-Prot (P09871.1)"
                     /calculated_mol_wt=1815
     mat_peptide     16..688
                     /product="Complement C1s subcomponent. /id=PRO_0000027586"
                     /note="propagated from UniProtKB/Swiss-Prot (P09871.1)"
                     /calculated_mol_wt=74888
     mat_peptide     16..437
                     /product="Complement C1s subcomponent heavy chain.
                     /id=PRO_0000027587"
                     /note="propagated from UniProtKB/Swiss-Prot (P09871.1)"
                     /calculated_mol_wt=47254
     Region          18..129
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(20,22,24,51,56,93,124,126,128..129)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          143..171
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Site            149
                     /site_type="hydroxylation"
                     /note="(3R)-3-hydroxyasparagine.
                     /evidence=ECO:0000269|PubMed:2141278; propagated from
                     UniProtKB/Swiss-Prot (P09871.1)"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:2141278, ECO:0000269|PubMed:23922389;
                     propagated from UniProtKB/Swiss-Prot (P09871.1)"
     Region          175..287
                     /region_name="CUB"
                     /note="CUB domain; pfam00431"
                     /db_xref="CDD:395345"
     Site            order(184,186,188,215,222,258,284,286)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Region          294..355
                     /region_name="CCP"
                     /note="Complement control protein (CCP) modules (aka short
                     consensus repeats SCRs or SUSHI repeats) have been
                     identified in several proteins of the complement system;
                     cd00033"
                     /db_xref="CDD:153056"
     Site            order(303,322)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Region          359..421
                     /region_name="CCP"
                     /note="Domain abundant in complement control proteins;
                     SUSHI repeat; short complement-like repeat (SCR);
                     smart00032"
                     /db_xref="CDD:214478"
     Site            order(369,387)
                     /site_type="active"
                     /note="receptor-ligand interactions [active]"
                     /db_xref="CDD:153056"
     Site            406
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12788922,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218;
                     propagated from UniProtKB/Swiss-Prot (P09871.1)"
     Site            437..438
                     /site_type="cleavage"
                     /note="Cleavage, by C1R.
                     /evidence=ECO:0000269|PubMed:869924; propagated from
                     UniProtKB/Swiss-Prot (P09871.1)"
     mat_peptide     438..688
                     /product="Complement C1s subcomponent light chain.
                     /evidence=ECO:0000305|PubMed:869924. /id=PRO_0000027588"
                     /note="propagated from UniProtKB/Swiss-Prot (P09871.1)"
                     /calculated_mol_wt=27652
     Region          438..678
                     /region_name="Tryp_SPc"
                     /note="Trypsin-like serine protease; Many of these are
                     synthesized as inactive precursor zymogens that are
                     cleaved during limited proteolysis to generate their
                     active forms. Alignment contains also inactive enzymes
                     that have substitutions of the catalytic triad...;
                     cd00190"
                     /db_xref="CDD:238113"
     Site            438
                     /site_type="active"
                     /note="cleavage site [active]"
                     /db_xref="CDD:238113"
     Site            order(475,529,632)
                     /site_type="active"
                     /db_xref="CDD:238113"
     Site            order(626,654,656)
                     /site_type="other"
                     /note="substrate binding sites [chemical binding]"
                     /db_xref="CDD:238113"
     CDS             1..688
                     /gene="C1S"
                     /gene_synonym="EDSPD2"
                     /coded_by="NM_201442.4:322..2388"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS31735.1"
                     /db_xref="GeneID:716"
                     /db_xref="HGNC:HGNC:1247"
                     /db_xref="MIM:120580"
ORIGIN      
        1 mwcivlfsll awvyaeptmy geilspnypq aypseveksw dievpegygi hlyfthldie
       61 lsencaydsv qiisgdteeg rlcgqrssnn phspiveefq vpynklqvif ksdfsneerf
      121 tgfaayyvat dinectdfvd vpcshfcnnf iggyfcscpp eyflhddmkn cgvncsgdvf
      181 taligeiasp nypkpypens rceyqirlek gfqvvvtlrr edfdveaads agncldslvf
      241 vagdrqfgpy cghgfpgpln ietksnaldi ifqtdltgqk kgwklryhgd pmpcpkedtp
      301 nsvwepakak yvfrdvvqit cldgfevveg rvgatsfyst cqsngkwsns klkcqpvdcg
      361 ipesiengkv edpestlfgs virytceepy yymengggge yhcagngswv nevlgpelpk
      421 cvpvcgvpre pfeekqriig gsdadiknfp wqvffdnpwa ggalineywv ltaahvvegn
      481 reptmyvgst svqtsrlaks kmltpehvfi hpgwkllevp egrtnfdndi alvrlkdpvk
      541 mgptvspicl pgtssdynlm dgdlglisgw grtekrdrav rlkaarlpva plrkckevkv
      601 ekptadaeay vftpnmicag gekgmdsckg dsggafavqd pndktkfyaa glvswgpqcg
      661 tyglytrvkn yvdwimktmq enstpred
//
LOCUS       NP_001752                786 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-F isoform 1 [Homo sapiens].
ACCESSION   NP_001752
VERSION     NP_001752.2
DBSOURCE    REFSEQ: accession NM_001761.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 786)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 786)
  AUTHORS   Yang,H., Fouad,S., Smith,P., Bae,E.Y., Ji,Y., Lan,X., Van Ess,A.,
            Buffa,F.M., Fischer,R., Vendrell,I., Kessler,B.M. and
            D'Angiolella,V.
  TITLE     Cyclin F-EXO1 axis controls cell cycle-dependent execution of
            double-strand break repair
  JOURNAL   Sci Adv 10 (32), eado0636 (2024)
   PUBMED   39121215
  REMARK    GeneRIF: Cyclin F-EXO1 axis controls cell cycle-dependent execution
            of double-strand break repair.
REFERENCE   3  (residues 1 to 786)
  AUTHORS   Kwiatkowski,M., Krajewski,A., Durslewicz,J., Buchholz,K.,
            Grzanka,D., Gagat,M., Zabrzynski,J. and Klimaszewska-Wisniewska,A.
  TITLE     Overexpression of cyclin F/CCNF as an independent prognostic factor
            for poor survival in clear cell renal cell carcinoma
  JOURNAL   Sci Rep 14 (1), 9280 (2024)
   PUBMED   38654021
  REMARK    GeneRIF: Overexpression of cyclin F/CCNF as an independent
            prognostic factor for poor survival in clear cell renal cell
            carcinoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 786)
  AUTHORS   Ragagnin,A.M.G., Sundaramoorthy,V., Farzana,F., Gautam,S.,
            Saravanabavan,S., Takalloo,Z., Mehta,P., Do-Ha,D., Parakh,S.,
            Shadfar,S., Hunter,J., Vidal,M., Jagaraj,C.J., Brocardo,M.,
            Konopka,A., Yang,S., Rayner,S.L., Williams,K.L., Blair,I.P.,
            Chung,R.S., Lee,A., Ooi,L. and Atkin,J.D.
  TITLE     ALS/FTD-associated mutation in cyclin F inhibits ER-Golgi
            trafficking, inducing ER stress, ERAD and Golgi fragmentation
  JOURNAL   Sci Rep 13 (1), 20467 (2023)
   PUBMED   37993492
  REMARK    GeneRIF: ALS/FTD-associated mutation in cyclin F inhibits ER-Golgi
            trafficking, inducing ER stress, ERAD and Golgi fragmentation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 786)
  AUTHORS   Davidson,J.M., Wu,S.S.L., Rayner,S.L., Cheng,F., Duncan,K.,
            Russo,C., Newbery,M., Ding,K., Scherer,N.M., Balez,R.,
            Garcia-Redondo,A., Rabano,A., Rosa-Fernandes,L., Ooi,L.,
            Williams,K.L., Morsch,M., Blair,I.P., Di Ieva,A., Yang,S.,
            Chung,R.S. and Lee,A.
  TITLE     The E3 Ubiquitin Ligase SCF Cyclin F Promotes Sequestosome-1/p62
            Insolubility and Foci Formation and is Dysregulated in ALS and FTD
            Pathogenesis
  JOURNAL   Mol Neurobiol 60 (9), 5034-5054 (2023)
   PUBMED   37243816
  REMARK    GeneRIF: The E3 Ubiquitin Ligase SCF Cyclin F Promotes
            Sequestosome-1/p62 Insolubility and Foci Formation and is
            Dysregulated in ALS and FTD Pathogenesis.
REFERENCE   6  (residues 1 to 786)
  AUTHORS   Fung,T.K., Siu,W.Y., Yam,C.H., Lau,A. and Poon,R.Y.
  TITLE     Cyclin F is degraded during G2-M by mechanisms fundamentally
            different from other cyclins
  JOURNAL   J Biol Chem 277 (38), 35140-35149 (2002)
   PUBMED   12122006
  REMARK    GeneRIF: degradation during G2-M by mechanisms fundamentally
            different from other cyclins
REFERENCE   7  (residues 1 to 786)
  AUTHORS   Kong,M., Barnes,E.A., Ollendorff,V. and Donoghue,D.J.
  TITLE     Cyclin F regulates the nuclear localization of cyclin B1 through a
            cyclin-cyclin interaction
  JOURNAL   EMBO J 19 (6), 1378-1388 (2000)
   PUBMED   10716937
REFERENCE   8  (residues 1 to 786)
  AUTHORS   Bai,C., Sen,P., Hofmann,K., Ma,L., Goebl,M., Harper,J.W. and
            Elledge,S.J.
  TITLE     SKP1 connects cell cycle regulators to the ubiquitin proteolysis
            machinery through a novel motif, the F-box
  JOURNAL   Cell 86 (2), 263-274 (1996)
   PUBMED   8706131
REFERENCE   9  (residues 1 to 786)
  AUTHORS   Bai,C., Richman,R. and Elledge,S.J.
  TITLE     Human cyclin F
  JOURNAL   EMBO J 13 (24), 6087-6098 (1994)
   PUBMED   7813445
REFERENCE   10 (residues 1 to 786)
  AUTHORS   Kraus,B., Pohlschmidt,M., Leung,A.L., Germino,G.G., Snarey,A.,
            Schneider,M.C., Reeders,S.T. and Frischauf,A.M.
  TITLE     A novel cyclin gene (CCNF) in the region of the polycystic kidney
            disease gene (PKD1)
  JOURNAL   Genomics 24 (1), 27-33 (1994)
   PUBMED   7896286
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z36714.1, BC012349.1,
            AB208829.1 and DB523776.1.
            
            On Dec 1, 2006 this sequence version replaced NP_001752.1.
            
            Summary: This gene encodes a member of the cyclin family. Cyclins
            are important regulators of cell cycle transitions through their
            ability to bind and activate cyclin-dependent protein kinases. This
            member also belongs to the F-box protein family which is
            characterized by an approximately 40 amino acid motif, the F-box.
            The F-box proteins constitute one of the four subunits of the
            ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),
            which function in phosphorylation-dependent ubiquitination. The
            F-box proteins are divided into 3 classes: Fbws containing WD-40
            domains, Fbls containing leucine-rich repeats, and Fbxs containing
            either different protein-protein interaction modules or no
            recognizable motifs. The protein encoded by this gene belongs to
            the Fbxs class and it was one of the first proteins in which the
            F-box motif was identified. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z36714.1, SRR1803617.234804.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397066.9/ ENSP00000380256.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..786
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..786
                     /product="cyclin-F isoform 1"
                     /note="F-box only protein 1; G2/mitotic-specific cyclin-F"
                     /calculated_mol_wt=87509
     Region          20..28
                     /region_name="Nuclear localization signal 1.
                     /evidence=ECO:0000269|PubMed:10716937"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          29..76
                     /region_name="F-box domain"
     Region          31..82
                     /region_name="F-box_FBXO1"
                     /note="F-box domain found in F-box only protein 1 (FBXO1)
                     and similar proteins; cd22082"
                     /db_xref="CDD:438854"
     Site            order(35,39,42..43,46..47,51,53..54,58..60,62)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438854"
     Region          <88..124
                     /region_name="TPR"
                     /note="TPR repeat [General function prediction only];
                     COG0790"
                     /db_xref="CDD:440553"
     Region          307..401
                     /region_name="CYCLIN_CCNF_rpt1"
                     /note="first cyclin box found in G2/mitotic-specific
                     cyclin-F (CCNF) and similar proteins; cd20521"
                     /db_xref="CDD:410225"
     Region          310..313
                     /region_name="D box 1.
                     /evidence=ECO:0000269|PubMed:27653696"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          343..346
                     /region_name="D box 2.
                     /evidence=ECO:0000269|PubMed:27653696"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          349..352
                     /region_name="D box 3.
                     /evidence=ECO:0000269|PubMed:27653696"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          351..354
                     /region_name="D box 4.
                     /evidence=ECO:0000269|PubMed:27653696"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          429..540
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     Region          564..593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          568..574
                     /region_name="Nuclear localization signal 2.
                     /evidence=ECO:0000269|PubMed:10716937"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          582..766
                     /region_name="PEST"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          675..738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     Region          767..770
                     /region_name="D box 5.
                     /evidence=ECO:0000269|PubMed:27653696"
                     /note="propagated from UniProtKB/Swiss-Prot (P41002.2)"
     CDS             1..786
                     /gene="CCNF"
                     /gene_synonym="FBX1; FBXO1; FTDALS5"
                     /coded_by="NM_001761.3:36..2396"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10467.1"
                     /db_xref="GeneID:899"
                     /db_xref="HGNC:HGNC:1591"
                     /db_xref="MIM:600227"
ORIGIN      
        1 mgsggvvhcr cakcfcyptk rrirrrprnl tilslpedvl fhilkwlsve dilavravhs
       61 qlkdlvdnha svwacasfqe lwpspgnlkl feraaekgnf eaavklgiay lyneglsvsd
      121 earaevnglk asrffslaer lnvgaapfiw lfirppwsvs gscckavvhe slraecqlqr
      181 thkasilhcl grvlslfede ekqqqahdlf eeaahqgclt ssyllwesdr rtdvsdpgrc
      241 lhsfrklrdy aakgcweaql slakacanan qlglevrass eivcqlfqas qavskqqvfs
      301 vqkglndtmr yilidwlvev atmkdftslc lhltvecvdr ylrrrlvpry rlqllgiacm
      361 victrfiske iltireavwl tdntykyedl vrmmgeivsa legkirvptv vdykevlltl
      421 vpvelrtqhl csflcelsll htslsayapa rlaaaallla rlthgqtqpw ttqlwdltgf
      481 syedlipcvl slhkkcfhdd apkdyrqvsl tavkqrfedk rygeisqeev lsysqlcaal
      541 gvtqdspdpp tflstgeiha flsspsgrrt krkrenslqe drgsfvttpt aelssqeetl
      601 lgsfldwsld ccsgyegdqe segekegdvt apsgildvtv vylnpeqhcc qessdeeacp
      661 edkgpqdpqa laldtqipat pgpkplvrts repgkdvtts gyssvstasp tssvdgglga
      721 lpqptsvlsl dsdshtqpch hqarksclqc rppsppessv pqqqvkrinl cihseeedmn
      781 lglvrl
//
LOCUS       NP_001291314             163 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich single-pass membrane protein 2 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001291314 XP_005264939
VERSION     NP_001291314.1
DBSOURCE    REFSEQ: accession NM_001304385.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA830939.1, U90094.1 and BC028000.1.
            
            On Jan 23, 2015 this sequence version replaced XP_005264939.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA830939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..163
                     /product="leucine-rich single-pass membrane protein 2
                     isoform 2"
                     /calculated_mol_wt=17666
     Region          13..161
                     /region_name="DUF4714"
                     /note="Domain of unknown function (DUF4714); pfam15833"
                     /db_xref="CDD:464901"
     Site            96..116
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N112.1)"
     CDS             1..163
                     /gene="LSMEM2"
                     /gene_synonym="C3orf45"
                     /coded_by="NM_001304385.2:28..519"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:132228"
                     /db_xref="HGNC:HGNC:26781"
                     /db_xref="MIM:621358"
ORIGIN      
        1 mpslapdcpl lampeetqed svapmmpsqr srgplapnhv hevclhqves isdlhsggtl
       61 rpylteearp wdellgvlpp slcaqagcsp vyrrggflll lallvltclv lallavylsv
      121 lqseslrila htlrtqeetl lklrlaslsq lrrlnsseaq aps
//
LOCUS       NP_001245384             572 aa            linear   PRI 20-NOV-2025
DEFINITION  TNFAIP3-interacting protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001245384
VERSION     NP_001245384.1
DBSOURCE    REFSEQ: accession NM_001258455.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Panyard,D.J., Reus,L.M., Ali,M., Liu,J., Deming,Y.K., Lu,Q.,
            Kollmorgen,G., Carboni,M., Wild,N., Visser,P.J., Bertram,L.,
            Zetterberg,H., Blennow,K., Gobom,J., Western,D., Sung,Y.J.,
            Carlsson,C.M., Johnson,S.C., Asthana,S., Cruchaga,C., Tijms,B.M.,
            Engelman,C.D. and Snyder,M.P.
  TITLE     Post-GWAS multiomic functional investigation of the TNIP1 locus in
            Alzheimer's disease highlights a potential role for GPX3
  JOURNAL   Alzheimers Dement 20 (7), 5044-5053 (2024)
   PUBMED   38809917
  REMARK    GeneRIF: Post-GWAS multiomic functional investigation of the TNIP1
            locus in Alzheimer's disease highlights a potential role for GPX3.
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Martin-Vicente,M., Mthiyane,H., Jimenez-Sousa,M.A., Subramoney,K.,
            Hellferscee,O., Wolter,N., Walaza,S., Fernandez-Rodriguez,A.,
            Cohen,C., von Gottberg,A., Resino,S., Martinez,I. and
            Treurnicht,F.K.
  TITLE     TNFAIP3-interacting protein 1 polymorphisms and their association
            with symptomatic human respiratory syncytial virus infection and
            bronchiolitis in infants younger than one year from South Africa: A
            case-control study
  JOURNAL   Int J Infect Dis 136, 107-110 (2023)
   PUBMED   37751795
  REMARK    GeneRIF: TNFAIP3-interacting protein 1 polymorphisms and their
            association with symptomatic human respiratory syncytial virus
            infection and bronchiolitis in infants younger than one year from
            South Africa: A case-control study.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Rasmussen,N.L., Zhou,J., Olsvik,H., Kaeser-Pebernard,S., Lamark,T.,
            Dengjel,J. and Johansen,T.
  TITLE     The inflammation repressor TNIP1/ABIN-1 is degraded by autophagy
            following TBK1 phosphorylation of its LIR
  JOURNAL   Autophagy 19 (10), 2819-2820 (2023)
   PUBMED   36847414
  REMARK    GeneRIF: The inflammation repressor TNIP1/ABIN-1 is degraded by
            autophagy following TBK1 phosphorylation of its LIR.
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Le Guerroue,F., Bunker,E.N., Rosencrans,W.M., Nguyen,J.T.,
            Basar,M.A., Werner,A., Chou,T.F., Wang,C. and Youle,R.J.
  TITLE     TNIP1 inhibits selective autophagy via bipartite interaction with
            LC3/GABARAP and TAX1BP1
  JOURNAL   Mol Cell 83 (6), 927-941 (2023)
   PUBMED   36898370
  REMARK    GeneRIF: TNIP1 inhibits selective autophagy via bipartite
            interaction with LC3/GABARAP and TAX1BP1.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Klinkenberg,M., Van Huffel,S., Heyninck,K. and Beyaert,R.
  TITLE     Functional redundancy of the zinc fingers of A20 for inhibition of
            NF-kappaB activation and protein-protein interactions
  JOURNAL   FEBS Lett 498 (1), 93-97 (2001)
   PUBMED   11389905
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Gupta,K., Ott,D., Hope,T.J., Siliciano,R.F. and Boeke,J.D.
  TITLE     A human nuclear shuttling protein that interacts with human
            immunodeficiency virus type 1 matrix is packaged into virions
  JOURNAL   J Virol 74 (24), 11811-11824 (2000)
   PUBMED   11090181
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Heyninck,K., De Valck,D., Vanden Berghe,W., Van Criekinge,W.,
            Contreras,R., Fiers,W., Haegeman,G. and Beyaert,R.
  TITLE     The zinc finger protein A20 inhibits TNF-induced
            NF-kappaB-dependent gene expression by interfering with an RIP- or
            TRAF2-mediated transactivation signal and directly binds to a novel
            NF-kappaB-inhibiting protein ABIN
  JOURNAL   J Cell Biol 145 (7), 1471-1482 (1999)
   PUBMED   10385526
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Fukushi,M., Dixon,J., Kimura,T., Tsurutani,N., Dixon,M.J. and
            Yamamoto,N.
  TITLE     Identification and cloning of a novel cellular protein Naf1,
            Nef-associated factor 1, that increases cell surface CD4 expression
  JOURNAL   FEBS Lett 442 (1), 83-88 (1999)
   PUBMED   9923610
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008641.7 and AB177543.1.
            
            Summary: This gene encodes an A20-binding protein which plays a
            role in autoimmunity and tissue homeostasis through the regulation
            of nuclear factor kappa-B activation. Mutations in this gene have
            been associated with psoriatic arthritis, rheumatoid arthritis, and
            systemic lupus erythematosus. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (9) lacks an exon and uses an
            alternate splice site in the 3' coding region which results in a
            frameshift compared to variant 1. The resulting protein (isoform 5)
            is shorter and has a distinct C-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB177543.1, SRR14038196.700024.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..572
                     /product="TNFAIP3-interacting protein 1 isoform 5"
                     /note="Nef-associated factor 1 SNP; HIV-1 Nef-interacting
                     protein; virion-associated nuclear shuttling protein;
                     A20-binding inhibitor of NF-kappa-B activation 1"
                     /calculated_mol_wt=64369
     Region          14..>149
                     /region_name="Speriolin_N"
                     /note="Speriolin N terminus; pfam15058"
                     /db_xref="CDD:434426"
     Region          <214..>251
                     /region_name="PRK13922"
                     /note="rod shape-determining protein MreC; Provisional;
                     cl19252"
                     /db_xref="CDD:473155"
     Region          <298..>529
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..572
                     /gene="TNIP1"
                     /gene_synonym="ABIN-1; NAF1; nip40-1; VAN"
                     /coded_by="NM_001258455.1:37..1755"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS58984.1"
                     /db_xref="GeneID:10318"
                     /db_xref="HGNC:HGNC:16903"
                     /db_xref="MIM:607714"
ORIGIN      
        1 megrgpyriy dpggsvpsge asaaferlvk ensrlkekmq gikmlgelle esqmeatrlr
       61 qkaeelvkdn ellpppspsl gsfdplaelt gkdsnvtasp tapacpsdkp apvqkppssg
      121 tssefevvtp eeqnspesss hanamalgpl predgnlmlh lqrlettlsv caeepdhgql
      181 fthlgrmale fnrlaskvhk neqrtsilqt lceqlrkene alkakldkgl eqrdqaaerl
      241 reenlelkkl lmsngnkega sgrpgspkme gtgkkavagq qqasvtagkv pevvalgaae
      301 kkvkmleqqr sellevnkqw dqhfrsmkqq yeqkitelrq kladlqkqvt dleaereqkq
      361 rdfdrkllla kskiemeetd keqltaeake lrqkvkylqd qlspltrqre yqekeiqrln
      421 kaleealsiq tppsspptaf gspegagall rkqelvtqne llkqqvkife edfqrersdr
      481 ermneekeel kkqveklqaq vtlsnaqlka fkdeekarea lrqqkrkakp eytwrlpcgg
      541 vrnpnqssqv mdpptarpte pespkndreg pq
//
LOCUS       NP_005557                332 aa            linear   PRI 20-NOV-2025
DEFINITION  L-lactate dehydrogenase A chain isoform 1 [Homo sapiens].
ACCESSION   NP_005557
VERSION     NP_005557.1
DBSOURCE    REFSEQ: accession NM_005566.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Hu,C., Zhang,W., Jia,Y., Zhao,J., Chen,Q., Hao,C. and Yu,Y.
  TITLE     USP4 promotes PTC progression by stabilizing LDHA and activating
            the MAPK and AKT signaling pathway
  JOURNAL   Aging (Albany NY) 16 (19), 12850-12865 (2024)
   PUBMED   39393052
  REMARK    GeneRIF: USP4 promotes PTC progression by stabilizing LDHA and
            activating the MAPK and AKT signaling pathway.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Zhuo,Z., Wang,Y. and Xu,Y.
  TITLE     Advancements in research on lactate dehydrogenase A in urinary
            system tumors
  JOURNAL   BMC Urol 24 (1), 187 (2024)
   PUBMED   39215270
  REMARK    GeneRIF: Advancements in research on lactate dehydrogenase A in
            urinary system tumors.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Vats,P., Singh,J., Srivastava,S.K., Kumar,A. and Nema,R.
  TITLE     LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by Sponging
            miR-383-5p to Trigger the LDHA Axis
  JOURNAL   Asian Pac J Cancer Prev 25 (8), 2929-2944 (2024)
   PUBMED   39205592
  REMARK    GeneRIF: LncRNA TMPO-AS1 Promotes Triple-Negative Breast Cancer by
            Sponging miR-383-5p to Trigger the LDHA Axis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Papulino,C., Chianese,U., Ali,A., Favale,G., Tuccillo,C.,
            Ciardiello,F., Di Mauro,A., Mignogna,C., Ferrara,G., Budillon,A.,
            Megchelenbrink,W.L., Del Gaudio,N., Conte,M., Merciai,F.,
            Campiglia,P., Altucci,L., Carafa,V., Sommella,E. and Benedetti,R.
  TITLE     Inverse FASN and LDHA correlation drives metabolic resistance in
            breast cancer
  JOURNAL   J Transl Med 22 (1), 676 (2024)
   PUBMED   39044184
  REMARK    GeneRIF: Inverse FASN and LDHA correlation drives metabolic
            resistance in breast cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Miyajima,H., Shimizu,T. and Kaneko,E.
  TITLE     [Gene expression in lactate dehydrogenase-A subunit deficiency]
  JOURNAL   Rinsho Shinkeigaku 32 (10), 1087-1092 (1992)
   PUBMED   1297552
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Sudo,K., Maekawa,M., Shioya,M., Ikeda,K., Takahashi,N., Isogai,Y.,
            Li,S.S., Kanno,T., Machida,K. and Toriumi,J.
  TITLE     Molecular analysis of genetic mutation in electrophoretic variant
            of human lactate dehydrogenase-A(M) subunit
  JOURNAL   Biochem Int 27 (6), 1051-1057 (1992)
   PUBMED   1445373
REFERENCE   8  (residues 1 to 332)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Genotypic analysis of families with lactate dehydrogenase A (M)
            deficiency by selective DNA amplification
  JOURNAL   Hum Genet 88 (1), 34-38 (1991)
   PUBMED   1959923
REFERENCE   9  (residues 1 to 332)
  AUTHORS   Maekawa,M., Sudo,K., Li,S.S. and Kanno,T.
  TITLE     Analysis of genetic mutations in human lactate dehydrogenase-A(M)
            deficiency using DNA conformation polymorphism in combination with
            polyacrylamide gradient gel and silver staining
  JOURNAL   Biochem Biophys Res Commun 180 (2), 1083-1090 (1991)
   PUBMED   1953713
REFERENCE   10 (residues 1 to 332)
  AUTHORS   LeVan,K.M. and Goldberg,E.
  TITLE     Properties of human testis-specific lactate dehydrogenase expressed
            from Escherichia coli
  JOURNAL   Biochem J 273 (Pt 3) (Pt 3), 587-592 (1991)
   PUBMED   1996957
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC067223.1, BG424022.1,
            AC084117.6 and BM995301.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the A subunit of lactate dehydrogenase
            enzyme which catalyzes the reversible conversion of pyruvate to
            lactate with the concomitant oxidation of NADH to NAD in anaerobic
            glycolysis. The protein is found predominantly in skeletal muscle
            and belongs to the lactate dehydrogenase family. Mutations in this
            gene have been linked to exertional myoglobinuria. The human genome
            contains several non-transcribed pseudogenes of this gene.
            [provided by RefSeq, Sep 2023].
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026515.1, SRR1803616.91074.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000422447.8/ ENSP00000395337.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..332
                     /product="L-lactate dehydrogenase A chain isoform 1"
                     /EC_number="1.1.1.27"
                     /note="L-lactate dehydrogenase A chain; lactate
                     dehydrogenase M; LDH muscle subunit; renal carcinoma
                     antigen NY-REN-59; proliferation-inducing gene 19; LDH-A;
                     LDH-M; cell proliferation-inducing gene 19 protein;
                     epididymis secretory sperm binding protein Li 133P"
                     /calculated_mol_wt=36558
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P00338.2)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Region          19..329
                     /region_name="LDH_1"
                     /note="A subgroup of L-lactate dehydrogenases; cd05293"
                     /db_xref="CDD:133429"
     Site            order(20,181,184,186,203,208,265..267,270,297..298,301,
                     303..305)
                     /site_type="other"
                     /note="tetramer (dimer of dimers) interface [polypeptide
                     binding]"
                     /db_xref="CDD:133429"
     Site            order(29..31,52,54,57,95..99,136,138,161,165,193,248,252)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            order(33,38,60..61,64,66..67,169,171..172,178,244..245,
                     248..251)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:133429"
     Site            57
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            81
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            order(100,106,138,169,193,238,248)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133429"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06151; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            232
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06151; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P06151; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            243
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P06151; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04642; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04642; propagated from
                     UniProtKB/Swiss-Prot (P00338.2)"
     CDS             1..332
                     /gene="LDHA"
                     /gene_synonym="GSD11; HEL-S-133P; LDHM; PIG19"
                     /coded_by="NM_005566.4:99..1097"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7839.1"
                     /db_xref="GeneID:3939"
                     /db_xref="HGNC:HGNC:6535"
                     /db_xref="MIM:150000"
ORIGIN      
        1 matlkdqliy nllkeeqtpq nkitvvgvga vgmacaisil mkdladelal vdviedklkg
       61 emmdlqhgsl flrtpkivsg kdynvtansk lviitagarq qegesrlnlv qrnvnifkfi
      121 ipnvvkyspn ckllivsnpv diltyvawki sgfpknrvig sgcnldsarf rylmgerlgv
      181 hplschgwvl gehgdssvpv wsgmnvagvs lktlhpdlgt dkdkeqwkev hkqvvesaye
      241 viklkgytsw aiglsvadla esimknlrrv hpvstmikgl ygikddvfls vpcilgqngi
      301 sdlvkvtlts eeearlkksa dtlwgiqkel qf
//
LOCUS       NP_001001132            1220 aa            linear   PRI 20-NOV-2025
DEFINITION  intersectin-1 isoform ITSN-s [Homo sapiens].
ACCESSION   NP_001001132
VERSION     NP_001001132.1
DBSOURCE    REFSEQ: accession NM_001001132.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Lan,C., Zhang,H., Wang,K., Liu,X., Zhao,Y., Guo,Z., Zhang,N.,
            Zhou,Y., Gao,M., Gu,F. and Ma,Y.
  TITLE     The alternative splicing of intersectin 1 regulated by PTBP1
            promotes human glioma progression
  JOURNAL   Cell Death Dis 13 (9), 835 (2022)
   PUBMED   36171198
  REMARK    GeneRIF: The alternative splicing of intersectin 1 regulated by
            PTBP1 promotes human glioma progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1220)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1220)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1220)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1220)
  AUTHORS   Sengar,A.S., Wang,W., Bishay,J., Cohen,S. and Egan,S.E.
  TITLE     The EH and SH3 domain Ese proteins regulate endocytosis by linking
            to dynamin and Eps15
  JOURNAL   EMBO J 18 (5), 1159-1171 (1999)
   PUBMED   10064583
REFERENCE   7  (residues 1 to 1220)
  AUTHORS   Yamabhai,M., Hoffman,N.G., Hardison,N.L., McPherson,P.S.,
            Castagnoli,L., Cesareni,G. and Kay,B.K.
  TITLE     Intersectin, a novel adaptor protein with two Eps15 homology and
            five Src homology 3 domains
  JOURNAL   J Biol Chem 273 (47), 31401-31407 (1998)
   PUBMED   9813051
REFERENCE   8  (residues 1 to 1220)
  AUTHORS   Guipponi,M., Scott,H.S., Chen,H., Schebesta,A., Rossier,C. and
            Antonarakis,S.E.
  TITLE     Two isoforms of a human intersectin (ITSN) protein are produced by
            brain-specific alternative splicing in a stop codon
  JOURNAL   Genomics 53 (3), 369-376 (1998)
   PUBMED   9799604
REFERENCE   9  (residues 1 to 1220)
  AUTHORS   Chen,H. and Antonarakis,S.E.
  TITLE     The SH3D1A gene maps to human chromosome 21q22.1-->q22.2
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 213-215 (1997)
   PUBMED   9465890
REFERENCE   10 (residues 1 to 1220)
  AUTHORS   Sparks,A.B., Hoffman,N.G., McConnell,S.J., Fowlkes,D.M. and
            Kay,B.K.
  TITLE     Cloning of ligand targets: systematic isolation of SH3
            domain-containing proteins
  JOURNAL   Nat Biotechnol 14 (6), 741-744 (1996)
   PUBMED   9630982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC058925.1, AF114488.1 and
            AI857585.1.
            
            Summary: The protein encoded by this gene is a cytoplasmic
            membrane-associated protein that indirectly coordinates endocytic
            membrane traffic with the actin assembly machinery. In addition,
            the encoded protein may regulate the formation of clathrin-coated
            vesicles and could be involved in synaptic vesicle recycling. This
            protein has been shown to interact with dynamin, CDC42, SNAP23,
            SNAP25, SPIN90, EPS15, EPN1, EPN2, and STN2. Multiple transcript
            variants encoding different isoforms have been found for this gene,
            but the full-length nature of only two of them have been
            characterized so far. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding region compared to variant 1. The resulting isoform (ITSN-s)
            is shorter at the C-terminus compared to isoform ITSN-l.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF114488.1, SRR1803615.33040.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..1220
                     /product="intersectin-1 isoform ITSN-s"
                     /note="human intersectin-SH3 domain-containing protein
                     SH3P17; Src homology 3 domain-containing protein; SH3
                     domain-containing protein 1A; intersectin 1 (SH3 domain
                     protein)"
                     /calculated_mol_wt=137518
     Region          14..108
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          214..309
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0R4; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          322..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          326..702
                     /region_name="KLERQ"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          <363..>684
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          650..701
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE9; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          744..803
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(749,751,754,758,783..784,797,799..800)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          803..917
                     /region_name="INTAP"
                     /note="Intersectin and clathrin adaptor AP2 binding
                     region; pfam16617"
                     /db_xref="CDD:435467"
     Region          836..868
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            897
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0R4; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            901
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            904
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          917..968
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(922,924,927,931,948..949,962,964..965)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE9; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            995
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          1006..1057
                     /region_name="SH3_Intersectin1_3"
                     /note="Third Src homology 3 domain (or SH3C) of
                     Intersectin-1; cd11991"
                     /db_xref="CDD:212924"
     Site            order(1011,1013,1016,1020,1037..1038,1051,1053..1054)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212924"
     Region          1074..1138
                     /region_name="Required for interaction with FCHSD2.
                     /evidence=ECO:0000269|PubMed:29887380"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Region          1074..1138
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(1083,1085,1088,1092,1110..1111,1129,1131..1132)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1104..1127
                     /region_name="Bipartite nuclear localization signal, in
                     isoform 2. /evidence=ECO:0000269|PubMed:29599122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15811.3)"
     Site            1137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Site            1144
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15811.3)"
     Region          1158..1211
                     /region_name="SH3_Intersectin1_5"
                     /note="Fifth Src homology 3 domain (or SH3E) of
                     Intersectin-1; cd11995"
                     /db_xref="CDD:212928"
     Site            order(1164,1166,1169,1173,1191..1192,1205,1207..1208)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212928"
     CDS             1..1220
                     /gene="ITSN1"
                     /gene_synonym="ITSN; SH3D1A; SH3P17"
                     /coded_by="NM_001001132.2:246..3908"
                     /note="isoform ITSN-s is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33546.1"
                     /db_xref="GeneID:6453"
                     /db_xref="HGNC:HGNC:6183"
                     /db_xref="MIM:602442"
ORIGIN      
        1 maqfptpfgg sldiwaitve erakhdqqfh slkpisgfit gdqarnfffq sglpqpvlaq
       61 iwaladmnnd grmdqvefsi amkliklklq gyqlpsalpp vmkqqpvais sapafgmggi
      121 asmppltava pvpmgsipvv gmsptlvssv ptaavpplan gappviqplp afahpaatlp
      181 ksssfsrsgp gsqlntklqk aqsfdvasvp pvaewavpqs srlkyrqlfn shdktmsghl
      241 tgpqartilm qsslpqaqla siwnlsdidq dgkltaeefi lamhlidvam sgqplppvlp
      301 peyippsfrr vrsgsgisvi sstsvdqrlp eepvledeqq qlekklpvtf edkkrenfer
      361 gnlelekrrq alleqqrkeq erlaqlerae qerkererqe qerkrqlele kqlekqrele
      421 rqreeerrke ierreaakre lerqrqlewe rnrrqellnq rnkeqedivv lkakkktlef
      481 elealndkkh qlegklqdir crlttqrqei estnksrelr iaeithlqqq lqesqqmlgr
      541 lipekqilnd qlkqvqqnsl hrdslvtlkr aleakelarq hlrdqldeve ketrsklqei
      601 difnnqlkel reihnkqqlq kqksmeaerl kqkeqerkii elekqkeeaq rraqerdkqw
      661 lehvqqedeh qrprklheee klkreesvkk kdgeekgkqe aqdklgrlfh qhqepakpav
      721 qapwstaekg pltisaqenv kvvyyralyp fesrshdeit iqpgdivmvk gewvdesqtg
      781 epgwlggelk gktgwfpany aekipenevp apvkpvtdst sapapklalr etpaplavts
      841 sepsttpnnw adfsstwpts tnekpetdnw dawaaqpslt vpsagqlrqr saftpatatg
      901 sspspvlgqg ekveglqaqa lypwrakkdn hlnfnkndvi tvleqqdmww fgevqgqkgw
      961 fpksyvklis gpirkstsmd sgssespasl krvaspaakp vvsgeefiam ytyesseqgd
     1021 ltfqqgdvil vtkkdgdwwt gtvgdkagvf psnyvrlkds egsgtagktg slgkkpeiaq
     1081 viasytatgp eqltlapgql ilirkknpgg wwegelqarg kkrqigwfpa nyvkllspgt
     1141 skitpteppk stalaavcqv igmydytaqn ddelafnkgq iinvlnkedp dwwkgevngq
     1201 vglfpsnyvk lttdmdpsqq
//
LOCUS       NP_001300872             187 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming protein RhoA isoform 2 [Homo sapiens].
ACCESSION   NP_001300872
VERSION     NP_001300872.1
DBSOURCE    REFSEQ: accession NM_001313943.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 187)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 187)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   3  (residues 1 to 187)
  AUTHORS   Piao,J., Su,Z., He,J., Zhu,T., Fan,F., Wang,X., Yang,Z., Zhan,H.
            and Luo,D.
  TITLE     SphK1 deficiency ameliorates the development of atherosclerosis by
            inhibiting the S1P/S1PR3/Rhoa/ROCK pathway
  JOURNAL   Cell Signal 121, 111252 (2024)
   PUBMED   38852936
  REMARK    GeneRIF: SphK1 deficiency ameliorates the development of
            atherosclerosis by inhibiting the S1P/S1PR3/Rhoa/ROCK pathway.
REFERENCE   4  (residues 1 to 187)
  AUTHORS   Hutchins,C.M. and Gorfe,A.A.
  TITLE     Intrinsically Disordered Membrane Anchors of Rheb, RhoA, and DiRas3
            Small GTPases: Molecular Dynamics, Membrane Organization, and
            Interactions
  JOURNAL   J Phys Chem B 128 (27), 6518-6528 (2024)
   PUBMED   38942776
  REMARK    GeneRIF: Intrinsically Disordered Membrane Anchors of Rheb, RhoA,
            and DiRas3 Small GTPases: Molecular Dynamics, Membrane
            Organization, and Interactions.
REFERENCE   5  (residues 1 to 187)
  AUTHORS   Choi,J.H., Jeong,J., Kim,J., You,E., Keum,S., Song,S., Hwang,Y.E.,
            Ji,M., Park,K.S. and Rhee,S.
  TITLE     Genetic disruption of ATAT1 causes RhoA downregulation through
            abnormal truncation of C/EBPbeta
  JOURNAL   BMB Rep 57 (6), 293-298 (2024)
   PUBMED   38835115
  REMARK    GeneRIF: Genetic disruption of ATAT1 causes RhoA downregulation
            through abnormal truncation of C/EBPbeta.
REFERENCE   6  (residues 1 to 187)
  AUTHORS   Fagan,K.P., Oliveira,L. and Pittler,S.J.
  TITLE     Sequence of rho small GTP-binding protein cDNAs from human retina
            and identification of novel 5' end cloning artifacts
  JOURNAL   Exp Eye Res 59 (2), 235-237 (1994)
   PUBMED   7835413
REFERENCE   7  (residues 1 to 187)
  AUTHORS   Nemoto,Y., Namba,T., Teru-uchi,T., Ushikubi,F., Morii,N. and
            Narumiya,S.
  TITLE     A rho gene product in human blood platelets. I. Identification of
            the platelet substrate for botulinum C3 ADP-ribosyltransferase as
            rhoA protein
  JOURNAL   J Biol Chem 267 (29), 20916-20920 (1992)
   PUBMED   1328215
REFERENCE   8  (residues 1 to 187)
  AUTHORS   Moscow,J.A., Morrow,C.S., He,R., Mullenbach,G.T. and Cowan,K.H.
  TITLE     Structure and function of the 5'-flanking sequence of the human
            cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)
  JOURNAL   J Biol Chem 267 (9), 5949-5958 (1992)
   PUBMED   1556108
REFERENCE   9  (residues 1 to 187)
  AUTHORS   Cannizzaro,L.A., Madaule,P., Hecht,F., Axel,R., Croce,C.M. and
            Huebner,K.
  TITLE     Chromosome localization of human ARH genes, a ras-related gene
            family
  JOURNAL   Genomics 6 (2), 197-203 (1990)
   PUBMED   2407642
REFERENCE   10 (residues 1 to 187)
  AUTHORS   Yeramian,P., Chardin,P., Madaule,P. and Tavitian,A.
  TITLE     Nucleotide sequence of human rho cDNA clone 12
  JOURNAL   Nucleic Acids Res 15 (4), 1869 (1987)
   PUBMED   3822842
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC104452.2, BQ721697.1 and
            AC121247.2.
            
            Summary: This gene encodes a member of the Rho family of small
            GTPases, which cycle between inactive GDP-bound and active
            GTP-bound states and function as molecular switches in signal
            transduction cascades. Rho proteins promote reorganization of the
            actin cytoskeleton and regulate cell shape, attachment, and
            motility. Overexpression of this gene is associated with tumor cell
            proliferation and metastasis. Multiple alternatively spliced
            variants have been identified. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (3) contains an alternate 3'
            coding exon, compared to variant 1. The resulting isoform (2) has a
            shorter and distinct C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.7233.1,
                                           SRR1803612.52037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..187
                     /product="transforming protein RhoA isoform 2"
                     /EC_number="3.6.5.2"
                     /note="transforming protein RhoA; oncogene RHO H12;
                     Aplysia ras-related homolog 12; small GTP binding protein
                     RhoA; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=21033
     Region          5..>138
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     Site            12..19
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206648"
     Region          34..42
                     /region_name="Effector region. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            34
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-linked (GlcNAc) tyrosine,
                     by Photorhabdus PAU_02230, alternate.
                     /evidence=ECO:0000269|PubMed:24141704; propagated from
                     UniProtKB/Swiss-Prot (P61586.1)"
     Site            37
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-alpha-linked (GlcNAc)
                     threonine, by C.novyi toxin TcdA, alternate.
                     /evidence=ECO:0000269|PubMed:8810274; (Microbial
                     infection) O-linked (Glc) threonine, by C.difficile toxins
                     TcdA and TcdB, alternate.
                     /evidence=ECO:0000269|PubMed:24905543,
                     ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059;
                     propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            37
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206648"
     Site            40..42
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206648"
     Site            59..62
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206648"
     Site            order(61..62,78..79)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206648"
     Region          61..78
                     /region_name="Switch II region, involved in RAP1GDS1
                     isoform 2 binding. /evidence=ECO:0000269|PubMed:30190425,
                     ECO:0007744|PDB:5ZHX"
                     /note="propagated from UniProtKB/Swiss-Prot (P61586.1)"
     Site            117..120
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206648"
     CDS             1..187
                     /gene="RHOA"
                     /gene_synonym="ARH12; ARHA; EDFAOB; RHO12; RHOH12"
                     /coded_by="NM_001313943.2:160..723"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82775.1"
                     /db_xref="GeneID:387"
                     /db_xref="HGNC:HGNC:667"
                     /db_xref="MIM:165390"
ORIGIN      
        1 maairkklvi vgdgacgktc llivfskdqf pevyvptvfe nyvadievdg kqvelalwdt
       61 agqedydrlr plsypdtdvi lmcfsidspd slenipekwt pevkhfcpnv piilvgnkkd
      121 lrndehtrre lakmkqephc varleccgti laqlqppppr fkrfpclsll sswgyrrplp
      181 hpgaget
//
LOCUS       NP_001356489             174 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform d [Homo sapiens].
ACCESSION   NP_001356489
VERSION     NP_001356489.1
DBSOURCE    REFSEQ: accession NM_001369560.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.204065.1,
                                           SRR7410570.16299.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..174
                     /product="large ribosomal subunit protein uL22 isoform d"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=20116
     Region          4..155
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(5..6,28..30,32..33,35..36,89..94,102..107,139..140)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(8,10,13,15..17,20,24,27,87,91,94,106,108..110,112,
                     115,127..132)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     CDS             1..174
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369560.1:207..731"
                     /note="isoform d is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS92461.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 msyscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf rrynggvgrc
       61 aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn kapkmrrrty
      121 rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl mare
//
LOCUS       NP_003956                344 aa            linear   PRI 20-NOV-2025
DEFINITION  C-C chemokine receptor-like 2 isoform 1 [Homo sapiens].
ACCESSION   NP_003956 NP_001091101 XP_001717334
VERSION     NP_003956.2
DBSOURCE    REFSEQ: accession NM_003965.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Liu,A., Liu,Y., Chen,G., Lyu,W., Ye,F., Wang,J., Liao,Q., Zhu,L.,
            Du,Y. and Ye,R.D.
  TITLE     Structure of G protein-coupled receptor GPR1 bound to full-length
            chemerin adipokine reveals a chemokine-like reverse binding mode
  JOURNAL   PLoS Biol 22 (10), e3002838 (2024)
   PUBMED   39466725
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Su,Z., Brooks,J., Pelker,J., Andreyeva,T., Sobon,H., Gifford,R.,
            Powers,M., Wang,J., Dower,C., Hegen,M., Messing,D., Sheehan,A.D.
            and Brennan,J.J.
  TITLE     Studies with neutralizing antibodies suggest CXCL8-mediated
            neutrophil activation is independent of C-C motif chemokine
            receptor-like 2 (CCRL2) ligand binding function
  JOURNAL   PLoS One 18 (1), e0280590 (2023)
   PUBMED   36662882
  REMARK    GeneRIF: Studies with neutralizing antibodies suggest
            CXCL8-mediated neutrophil activation is independent of C-C motif
            chemokine receptor-like 2 (CCRL2) ligand binding function.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Rawat,P., Brummel,S.S., Singh,K.K., Kim,J., Frazer,K.A.,
            Nichols,S., Seage,G.R., Williams,P.L., Van Dyke,R.B.,
            Harismendy,O., Trout,R.N. and Spector,S.A.
  TITLE     Genomics Links Inflammation With Neurocognitive Impairment in
            Children Living With Human Immunodeficiency Virus Type-1
  JOURNAL   J Infect Dis 224 (5), 870-880 (2021)
   PUBMED   33373444
  REMARK    GeneRIF: Genomics Links Inflammation With Neurocognitive Impairment
            in Children Living With Human Immunodeficiency Virus Type-1.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Islam,S., Moni,M.A., Urmi,U.L., Tanaka,A. and Hoshino,H.
  TITLE     C-C Chemokine receptor-like 2 (CCRL2) acts as coreceptor for human
            immunodeficiency virus-2
  JOURNAL   Brief Bioinform 22 (4) (2021)
   PUBMED   33253374
  REMARK    GeneRIF: C-C Chemokine receptor-like 2 (CCRL2) acts as coreceptor
            for human immunodeficiency virus-2.
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Zabel,B.A., Nakae,S., Zuniga,L., Kim,J.Y., Ohyama,T., Alt,C.,
            Pan,J., Suto,H., Soler,D., Allen,S.J., Handel,T.M., Song,C.H.,
            Galli,S.J. and Butcher,E.C.
  TITLE     Mast cell-expressed orphan receptor CCRL2 binds chemerin and is
            required for optimal induction of IgE-mediated passive cutaneous
            anaphylaxis
  JOURNAL   J Exp Med 205 (10), 2207-2220 (2008)
   PUBMED   18794339
  REMARK    GeneRIF: Results identify chemerin as a natural nonsignaling
            protein ligand for both human and mouse CCRL2.
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Galligan,C.L., Matsuyama,W., Matsukawa,A., Mizuta,H., Hodge,D.R.,
            Howard,O.M. and Yoshimura,T.
  TITLE     Up-regulated expression and activation of the orphan chemokine
            receptor, CCRL2, in rheumatoid arthritis
  JOURNAL   Arthritis Rheum 50 (6), 1806-1814 (2004)
   PUBMED   15188357
  REMARK    GeneRIF: CCRL2 expression is up-regulated on synovial neutrophils
            of rheumatoid arthritis patients
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Wittamer,V., Franssen,J.D., Vulcano,M., Mirjolet,J.F., Le Poul,E.,
            Migeotte,I., Brezillon,S., Tyldesley,R., Blanpain,C., Detheux,M.,
            Mantovani,A., Sozzani,S., Vassart,G., Parmentier,M. and Communi,D.
  TITLE     Specific recruitment of antigen-presenting cells by chemerin, a
            novel processed ligand from human inflammatory fluids
  JOURNAL   J Exp Med 198 (7), 977-985 (2003)
   PUBMED   14530373
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Fan,P., Kyaw,H., Su,K., Zeng,Z., Augustus,M., Carter,K.C. and Li,Y.
  TITLE     Cloning and characterization of a novel human chemokine receptor
  JOURNAL   Biochem Biophys Res Commun 243 (1), 264-268 (1998)
   PUBMED   9473515
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Daugherty,B.L. and Springer,M.S.
  TITLE     The beta-chemokine receptor genes CCR1 (CMKBR1), CCR2 (CMKBR2), and
            CCR3 (CMKBR3) cluster within 285 kb on human chromosome 3p21
  JOURNAL   Genomics 41 (2), 294-295 (1997)
   PUBMED   9143512
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF015525.1 and BC071682.1.
            
            On or before Mar 27, 2009 this sequence version replaced
            NP_001091101.1, XP_001717334.1, NP_003956.1.
            
            Summary: This gene encodes a chemokine receptor like protein, which
            is predicted to be a seven transmembrane protein and most closely
            related to CCR1. Chemokines and their receptors mediated signal
            transduction are critical for the recruitment of effector immune
            cells to the site of inflammation. This gene is expressed at high
            levels in primary neutrophils and primary monocytes, and is further
            upregulated on neutrophil activation and during monocyte to
            macrophage differentiation. The function of this gene is unknown.
            This gene is mapped to the region where the chemokine receptor gene
            cluster is located. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript but encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF015525.1, SRR5189661.132309.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399036.4/ ENSP00000381994.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..344
                     /product="C-C chemokine receptor-like 2 isoform 1"
                     /note="C-C chemokine receptor-like 2; chemokine receptor
                     X; chemokine receptor CCR11; putative MCP-1 chemokine
                     receptor; atypical chemokine receptor 5; chemokine (C-C
                     motif) receptor-like 2"
                     /calculated_mol_wt=39382
     Site            3
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00421.2)"
     Region          39..311
                     /region_name="7tmA_CCRL2"
                     /note="CC chemokine receptor-like 2, member of the class A
                     family of seven-transmembrane G protein-coupled receptors;
                     cd15171"
                     /db_xref="CDD:320299"
     Region          39..66
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320299"
     Site            44..64
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Region          73..98
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320299"
     Site            75..95
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Site            order(94,97..98,103..108,110..111,114,160,162..166,
                     181..185,197,200..202,204..206,208..209,251,254..255,
                     257..258,261,278..279,281..283,286,289..290)
                     /site_type="other"
                     /note="putative peptide ligand binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:320299"
     Region          103..133
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320299"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Region          146..168
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320299"
     Region          197..226
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320299"
     Site            199..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Region          231..261
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320299"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Region          279..304
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320299"
     Site            287..307
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     Region          324..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00421.2)"
     CDS             1..344
                     /gene="CCRL2"
                     /gene_synonym="ACKR5; CKRX; CRAM; CRAM-A; CRAM-B; HCR"
                     /coded_by="NM_003965.5:257..1291"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43079.1"
                     /db_xref="GeneID:9034"
                     /db_xref="HGNC:HGNC:1612"
                     /db_xref="MIM:608379"
ORIGIN      
        1 manytlaped eydvliegel esdeaeqcdk ydaqalsaql vpslcsavfv igvldnllvv
       61 lilvkykglk rveniyllnl avsnlcfllt lpfwahaggd pmckiligly fvglysetff
      121 nclltvqryl vflhkgnffs arrrvpcgii tsvlawvtai latlpefvvy kpqmedqkyk
      181 cafsrtpflp adetfwkhfl tlkmnisvlv lplfiftfly vqmrktlrfr eqryslfklv
      241 faimvvfllm wapyniaffl stfkehfsls dckssynldk svhitkliat thccinplly
      301 afldgtfsky lcrcfhlrsn tplqprgqsa qgtsreepdh stev
//
LOCUS       NP_056216                991 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 7 isoform a [Homo sapiens].
ACCESSION   NP_056216 NP_001091885
VERSION     NP_056216.2
DBSOURCE    REFSEQ: accession NM_015401.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Maciejewski,K., Giers,M., Oleksiewicz,U. and Czerwinska,P.
  TITLE     The Epigenetic Modifiers HDAC2 and HDAC7 Inversely Associate with
            Cancer Stemness and Immunity in Solid Tumors
  JOURNAL   Int J Mol Sci 25 (14), 7841 (2024)
   PUBMED   39063083
  REMARK    GeneRIF: The Epigenetic Modifiers HDAC2 and HDAC7 Inversely
            Associate with Cancer Stemness and Immunity in Solid Tumors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Lu,W., Zhuang,G., Guan,Y., Li,Y., Liu,L. and Xiao,M.
  TITLE     Comprehensive analysis of HDAC7 expression and its prognostic value
            in diffuse large B cell lymphoma: A review
  JOURNAL   Medicine (Baltimore) 102 (45), e34577 (2023)
   PUBMED   37960766
  REMARK    GeneRIF: Comprehensive analysis of HDAC7 expression and its
            prognostic value in diffuse large B cell lymphoma: A review.
            Review article
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Qin,X., Long,Y., Bai,X., Cao,L., Yan,H., Zhang,K., Wang,B. and
            Wu,X.
  TITLE     The disordered C terminus of ALKBH5 promotes phase separation and
            paraspeckles assembly
  JOURNAL   J Biol Chem 299 (8), 105071 (2023)
   PUBMED   37474102
REFERENCE   5  (residues 1 to 991)
  AUTHORS   Ling,S., Chen,T., Wang,S., Zhang,W., Zhou,R., Xia,X., Yao,Z.,
            Fan,Y., Ning,S., Liu,J., Qin,L., Tucker,H.O., Wang,N. and Guo,X.
  TITLE     Deacetylation of FOXP1 by HDAC7 potentiates self-renewal of
            mesenchymal stem cells
  JOURNAL   Stem Cell Res Ther 14 (1), 188 (2023)
   PUBMED   37507770
  REMARK    GeneRIF: Deacetylation of FOXP1 by HDAC7 potentiates self-renewal
            of mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Lemercier,C., Brocard,M.P., Puvion-Dutilleul,F., Kao,H.Y.,
            Albagli,O. and Khochbin,S.
  TITLE     Class II histone deacetylases are directly recruited by BCL6
            transcriptional repressor
  JOURNAL   J Biol Chem 277 (24), 22045-22052 (2002)
   PUBMED   11929873
  REMARK    GeneRIF: Class II histone deacetylases are directly recruited by
            BCL6 transcriptional repressor
REFERENCE   7  (residues 1 to 991)
  AUTHORS   Fischle,W., Dequiedt,F., Fillion,M., Hendzel,M.J., Voelter,W. and
            Verdin,E.
  TITLE     Human HDAC7 histone deacetylase activity is associated with HDAC3
            in vivo
  JOURNAL   J Biol Chem 276 (38), 35826-35835 (2001)
   PUBMED   11466315
REFERENCE   8  (residues 1 to 991)
  AUTHORS   Lee,H.J., Chun,M. and Kandror,K.V.
  TITLE     Tip60 and HDAC7 interact with the endothelin receptor a and may be
            involved in downstream signaling
  JOURNAL   J Biol Chem 276 (20), 16597-16600 (2001)
   PUBMED   11262386
REFERENCE   9  (residues 1 to 991)
  AUTHORS   Marks,P.A., Richon,V.M. and Rifkind,R.A.
  TITLE     Histone deacetylase inhibitors: inducers of differentiation or
            apoptosis of transformed cells
  JOURNAL   J Natl Cancer Inst 92 (15), 1210-1216 (2000)
   PUBMED   10922406
  REMARK    Review article
REFERENCE   10 (residues 1 to 991)
  AUTHORS   Kao,H.Y., Downes,M., Ordentlich,P. and Evans,R.M.
  TITLE     Isolation of a novel histone deacetylase reveals that class I and
            class II deacetylases promote SMRT-mediated repression
  JOURNAL   Genes Dev 14 (1), 55-66 (2000)
   PUBMED   10640276
  REMARK    GeneRIF: Characterization of the mouse HDAC7 ortholog.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC376749.1, AY302468.1 and
            BC020505.2.
            
            On or before Mar 1, 2008 this sequence version replaced
            NP_001091885.1, NP_056216.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene has sequence homology to members of the histone
            deacetylase family. This gene is orthologous to mouse HDAC7 gene
            whose protein promotes repression mediated via the transcriptional
            corepressor SMRT. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1, also known as variant 3)
            encodes isoform a (also known as isoform c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299292.1, AY302468.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000080059.12/ ENSP00000080059.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..991
                     /product="histone deacetylase 7 isoform a"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase 7A; protein deacetylase HDAC7"
                     /calculated_mol_wt=106610
     Region          557..934
                     /region_name="HDAC7"
                     /note="Histone deacetylase 7; cd10008"
                     /db_xref="CDD:212532"
     Site            order(581,665,708..709,717..718,746,748,777,840,848..849,
                     880)
                     /site_type="active"
                     /db_xref="CDD:212532"
     CDS             1..991
                     /gene="HDAC7"
                     /gene_synonym="HD7; HD7A; HDAC7A"
                     /coded_by="NM_015401.5:119..3094"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8756.2"
                     /db_xref="GeneID:51564"
                     /db_xref="HGNC:HGNC:14067"
                     /db_xref="MIM:606542"
ORIGIN      
        1 mhspgadgtq vspgahycsp tgagcprpca dtpgpqpqpm dlrvgqrppv epppeptlla
       61 lqrpqrlhhh lflaglqqqr svepmrlsmd tpmpelqvgp qeqelrqllh kdkskrsava
      121 ssvvkqklae vilkkqqaal ertvhpnspg ipyrtleple tegatrsmls sflppvpslp
      181 sdppehfplr ktvsepnlkl rykpkksler rknpllrkes appslrrrpa etlgdsspss
      241 sstpasgcss pndsehgpnp ilgseallgq rlrlqetsva pfalptvsll paitlglpap
      301 aradsdrrth ptlgprgpil gsphtplflp hglepeaggt lpsrlqpill ldpsgshapl
      361 ltvpglgplp fhfaqslmtt erlsgsglhw plsrtrsepl ppsatapppp gpmqprleql
      421 kthvqvikrs akpsekprlr qipsaedlet dgggpgqvvd dglehrelgh gqpeargpap
      481 lqqhpqvllw eqqrlagrlp rgstgdtvll plaqgghrpl sraqsspaap aslsapepas
      541 qarvlssset partlpfttg liydsvmlkh qcscgdnsrh pehagriqsi wsrlqerglr
      601 sqceclrgrk asleelqsvh serhvllygt nplsrlkldn gklagllaqr mfvmlpcggv
      661 gvdtdtiwne lhssnaarwa agsvtdlafk vasrelkngf avvrppghha dhstamgfcf
      721 fnsvaiacrq lqqqskaski livdwdvhhg ngtqqtfyqd psvlyislhr hddgnffpgs
      781 gavdevgags gegfnvnvaw aggldppmgd peylaafriv vmpiarefsp dlvlvsagfd
      841 aaeghpaplg gyhvsakcfg ymtqqlmnla ggavvlaleg ghdltaicda seacvaallg
      901 nrvdplseeg wkqkpnlnai rsleavirvh skywgcmqrl ascpdswvpr vpgadkeeve
      961 avtalaslsv gilaedrpse qlveeeepmn l
//
LOCUS       NP_001289819             309 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-1 isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_001289819
VERSION     NP_001289819.1
DBSOURCE    REFSEQ: accession NM_001302890.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Inoue,H., Shiozaki,A., Kosuga,T., Shimizu,H., Kudou,M., Arita,T.,
            Konishi,H., Komatsu,S., Kuriu,Y., Kubota,T., Fujiwara,H.,
            Morinaga,Y., Konishi,E. and Otsuji,E.
  TITLE     CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer
  JOURNAL   J Gastroenterol 59 (7), 556-571 (2024)
   PUBMED   38536483
  REMARK    GeneRIF: CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer.
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Chen,Z., Mondal,A., Abderemane-Ali,F., Jang,S., Niranjan,S.,
            Montano,J.L., Zaro,B.W. and Minor,D.L. Jr.
  TITLE     EMC chaperone-CaV structure reveals an ion channel assembly
            intermediate
  JOURNAL   Nature 619 (7969), 410-419 (2023)
   PUBMED   37196677
  REMARK    GeneRIF: EMC chaperone-CaV structure reveals an ion channel
            assembly intermediate.
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Dahimene,S., von Elsner,L., Holling,T., Mattas,L.S., Pickard,J.,
            Lessel,D., Pilch,K.S., Kadurin,I., Pratt,W.S., Zhulin,I.B., Dai,H.,
            Hempel,M., Ruzhnikov,M.R.Z., Kutsche,K. and Dolphin,A.C.
  TITLE     Biallelic CACNA2D1 loss-of-function variants cause early-onset
            developmental epileptic encephalopathy
  JOURNAL   Brain 145 (8), 2721-2729 (2022)
   PUBMED   35293990
  REMARK    GeneRIF: Biallelic CACNA2D1 loss-of-function variants cause
            early-onset developmental epileptic encephalopathy.
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Schleithoff,L., Mehrke,G., Reutlinger,B. and Lehmann-Horn,F.
  TITLE     Genomic structure and functional expression of a human
            alpha(2)/delta calcium channel subunit gene (CACNA2)
  JOURNAL   Genomics 61 (2), 201-209 (1999)
   PUBMED   10534405
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Iles,D.E., Lehmann-Horn,F., Scherer,S.W., Tsui,L.C., Olde
            Weghuis,D., Suijkerbuijk,R.F., Heytens,L., Mikala,G., Schwartz,A.,
            Ellis,F.R. et al.
  TITLE     Localization of the gene encoding the alpha 2/delta-subunits of the
            L-type voltage-dependent calcium channel to chromosome 7q and
            analysis of the segregation of flanking markers in malignant
            hyperthermia susceptible families
  JOURNAL   Hum Mol Genet 3 (6), 969-975 (1994)
   PUBMED   7951247
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Powers,P.A., Scherer,S.W., Tsui,L.C., Gregg,R.G. and Hogan,K.
  TITLE     Localization of the gene encoding the alpha 2/delta subunit
            (CACNL2A) of the human skeletal muscle voltage-dependent Ca2+
            channel to chromosome 7q21-q22 by somatic cell hybrid analysis
  JOURNAL   Genomics 19 (1), 192-193 (1994)
   PUBMED   8188232
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Brust,P.F., Simerson,S., McCue,A.F., Deal,C.R., Schoonmaker,S.,
            Williams,M.E., Velicelebi,G., Johnson,E.C., Harpold,M.M. and
            Ellis,S.B.
  TITLE     Human neuronal voltage-dependent calcium channels: studies on
            subunit structure and role in channel assembly
  JOURNAL   Neuropharmacology 32 (11), 1089-1102 (1993)
   PUBMED   8107964
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   9  (residues 1 to 309)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
REFERENCE   10 (residues 1 to 309)
  AUTHORS   Ellis,S.B., Williams,M.E., Ways,N.R., Brenner,R., Sharp,A.H.,
            Leung,A.T., Campbell,K.P., McKenna,E., Koch,W.J., Hui,A.,
            Schwartz,A. and Harpold,M.M.
  TITLE     Sequence and expression of mRNAs encoding the alpha 1 and alpha 2
            subunits of a DHP-sensitive calcium channel
  JOURNAL   Science 241 (4873), 1661-1664 (1988)
   PUBMED   2458626
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP258070.1 and BC051339.1.
            
            Summary: The preproprotein encoded by this gene is cleaved into
            multiple chains that comprise the alpha-2 and delta subunits of the
            voltage-dependent calcium channel complex. Calcium channels mediate
            the influx of calcium ions into the cell upon membrane
            polarization. Mutations in this gene can cause cardiac
            deficiencies, including Brugada syndrome and short QT syndrome.
            Alternate splicing results in multiple transcript variants, some of
            which may lack the delta subunit portion. [provided by RefSeq, Nov
            2014].
            
            Transcript Variant: This variant (2) lacks multiple 3' exons and
            contains an alternate 3' coding region and 3' UTR, compared to
            variant 1. The encoded isoform (2) has a distinct C-terminus and is
            shorter than isoform 1. This isoform lacks the entire delta chain
            and a large portion of the alpha-2 chain.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051339.1, ERR3218370.224736.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..309
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-1 isoform 2 precursor"
                     /note="calcium channel, L type, alpha 2 polypeptide;
                     dihydropyridine-sensitive L-type, calcium channel
                     alpha-2/delta subunit; voltage-gated calcium channel
                     subunit alpha-2/delta-1; calcium channel,
                     voltage-dependent, alpha 2/delta subunit 1; alpha2delta-1"
                     /calculated_mol_wt=32189
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          104..223
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54290; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          239..>300
                     /region_name="vWFA"
                     /note="Von Willebrand factor type A (vWA) domain was
                     originally found in the blood coagulation protein von
                     Willebrand factor (vWF). Typically, the vWA domain is made
                     up of approximately 200 amino acid residues folded into a
                     classic a/b para-rossmann type of...; cl00057"
                     /db_xref="CDD:469594"
     Region          259..263
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
     CDS             1..309
                     /gene="CACNA2D1"
                     /gene_synonym="CACNA2; CACNL2A; CCHL2A; DEE110; LINC01112;
                     lncRNA-N3"
                     /coded_by="NM_001302890.2:319..1248"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS78253.1"
                     /db_xref="GeneID:781"
                     /db_xref="HGNC:HGNC:1399"
                     /db_xref="MIM:114204"
ORIGIN      
        1 maagcllalt ltlfqsllig psseepfpsa vtikswvdkm qedlvtlakt asgvnqlvdi
       61 yekyqdlytv epnnarqlve iaardiekll snrskalvrl aleaekvqaa hqwredfasn
      121 evvyynakdd ldpekndsep gsqrikpvfi edanfgrqis yqhaavhipt diyegstivl
      181 nelnwtsald evfkknreed psllwqvfgs atglaryypa spwvdnsrtp nkidlydvrr
      241 rpwyiqgaas pkdmlilvdv sgsvsgltlk lirtsvseml etlsdddfvn vasdskeisp
      301 speeifnae
//
LOCUS       NP_055543               1322 aa            linear   PRI 20-NOV-2025
DEFINITION  FERM and PDZ domain-containing protein 4 isoform e [Homo sapiens].
ACCESSION   NP_055543 XP_045712
VERSION     NP_055543.2
DBSOURCE    REFSEQ: accession NM_014728.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1322)
  AUTHORS   Li,R.K., Li,H., Tian,M.Q., Li,Y., Luo,S., Liang,X.Y., Liu,W.H.,
            Li,B.M., Shi,X.Q., Li,J., Li,B. and Shu,X.M.
  CONSRTM   China Epilepsy Gene 1.0 Project
  TITLE     Investigation of FRMPD4 variants associated with X-linked epilepsy
  JOURNAL   Seizure 116, 45-50 (2024)
   PUBMED   37330374
  REMARK    GeneRIF: Investigation of FRMPD4 variants associated with X-linked
            epilepsy.
REFERENCE   2  (residues 1 to 1322)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1322)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 1322)
  AUTHORS   Wang,M., Lin,L., Shi,Y., He,L., Wang,C. and Zhu,J.
  TITLE     Structure of the FERM domain of a neural scaffold protein FRMPD4
            implicated in X-linked intellectual disability
  JOURNAL   Biochem J 477 (23), 4623-4634 (2020)
   PUBMED   33216857
  REMARK    GeneRIF: Structure of the FERM domain of a neural scaffold protein
            FRMPD4 implicated in X-linked intellectual disability.
REFERENCE   5  (residues 1 to 1322)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1322)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   7  (residues 1 to 1322)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 1322)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1322)
  AUTHORS   Lee,H.W., Choi,J., Shin,H., Kim,K., Yang,J., Na,M., Choi,S.Y.,
            Kang,G.B., Eom,S.H., Kim,H. and Kim,E.
  TITLE     Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
            regulates dendritic spine morphogenesis
  JOURNAL   J Neurosci 28 (53), 14546-14556 (2008)
   PUBMED   19118189
  REMARK    GeneRIF: Preso positively regulates spine density through its
            interaction with the synaptic plasma membrane, actin filaments,
            PSD-95, and the betaPix-based Rac1 signaling pathway.
REFERENCE   10 (residues 1 to 1322)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB002314.3, AK289694.1,
            AC112655.4 and BX089361.1.
            
            On Nov 6, 2008 this sequence version replaced NP_055543.1.
            
            Summary: This gene encodes a multi-domain (WW, PDZ, FERM)
            containing protein. Through its interaction with other proteins
            (such as PSD-95), it functions as a positive regulator of dendritic
            spine morphogenesis and density, and is required for the
            maintenance of excitatory synaptic transmission. [provided by
            RefSeq, Jan 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB002314.3, SRR1660803.119143.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1322
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..1322
                     /product="FERM and PDZ domain-containing protein 4 isoform
                     e"
                     /note="PSD-95-interacting FERM and PDZ domain protein;
                     Preso; PDZ domain-containing protein 10;
                     PSD-95-interacting regulator of spine morphogenesis"
                     /calculated_mol_wt=144249
     Region          36..66
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(50,61)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          78..152
                     /region_name="PDZ_FRMPD1_3_4-like"
                     /note="PDZ domain of FERM and PDZ domain-containing
                     protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains;
                     cd06769"
                     /db_xref="CDD:467250"
     Site            order(88..94,102,105,133,137,140..141)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467250"
     Region          201..294
                     /region_name="FERM_F1_FRMPD4"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in FERM and PDZ
                     domain-containing protein 4 (FRMPD4); cd17170"
                     /db_xref="CDD:340690"
     Region          205..424
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          420..524
                     /region_name="FERM_C_FRMPD1_FRMPD3_FRMPD4"
                     /note="FERM domain C-lobe of FERM and PDZ domain
                     containing proteins 1, 3, and 4 (FRMPD1, 3, 4); cd13183"
                     /db_xref="CDD:270004"
     Site            order(428,449,451,459)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270004"
     Site            order(463,469..472,505,509,512..513)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Site            505..516
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Region          809..847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          900..927
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          952..983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          975..1023
                     /region_name="LGNbd_FRMPD4"
                     /note="LGN tetratricopeptide repeat-binding domain found
                     in FERM and PDZ domain-containing protein 4; cd21943"
                     /db_xref="CDD:409274"
     Site            order(988..992,994..1010,1012)
                     /site_type="other"
                     /note="TPR binding site [polypeptide binding]"
                     /db_xref="CDD:409274"
     Region          1027..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1105..1148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1160..1180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1207..1227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     CDS             1..1322
                     /gene="FRMPD4"
                     /gene_synonym="MRX104; PDZD10; PDZK10; XLID104"
                     /coded_by="NM_014728.3:507..4475"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS35201.1"
                     /db_xref="GeneID:9758"
                     /db_xref="HGNC:HGNC:29007"
                     /db_xref="MIM:300838"
ORIGIN      
        1 mdvfsfvkia klsshrtkss gwpppsgtwg lsqvppygwe mtanrdgrdy finhmtqaip
       61 fddprlescq iippaprkve mrrdpvlgfg fvagsekpvv vrsvtpggps egklipgdqi
      121 vmindepvsa aprervidlv rsckesillt viqpypspks afisaakkar lksnpvkvrf
      181 seeviingqv setvkdnsll fmpnvlkvyl engqtksfrf dcstsikdvi ltlqeklsik
      241 giehfslmle qrtegagtkl lllheqetlt qvtqrpsshk mrclfrisfv pkdpidllrr
      301 dpvafeylyv qscndvvqer fgpelkydia lrlaalqmyi atvttkqtqk islkyiekew
      361 gletflpsav lqsmkeknik kalshlvkan qnlvppgkkl salqakvhyl kflsdlrlyg
      421 grvfkatlvq aekrsevtll vgprygishv intktnlval ladfshvnri emfseeeslv
      481 rvelhvldvk pitllmessd amnlacltag yyrllvdsrr sifnmankkn tatqetgpen
      541 kgkhnllgpd wncipqmttf igegeqeaqi tyidskqktv eitdstmcpk ehrhlyidna
      601 yssdglnqql sqpgeapcea dyrslaqrsl ltlsgpetlk kaqesprgak vsfifgdfal
      661 ddgispptlg yetlldegpe mlekqrnlyi gsandmkgld ltpeaegiqf vensvyanig
      721 dvksfqaaeg ieepllhdic yaentddaed edevsceedl vvgemnqpai lnlsgssddi
      781 idltslpppe gddneddfll rslnmaiaap ppgfrdssde edsqsqaasf pedkekgssl
      841 qndeipvsli davptsaegk cekgldnavv stlgaleals vseeqqtsdn sgvailrays
      901 pesssdsgne tnssemtess elataqkqse nlsrmflath egyhplaeeq tefpasktpa
      961 gglppkssha laarpatdlp pkvvpskqll hsdhmemepe tmetksvtdy fsklhmgsva
     1021 ysctskrksk ladgegkapp ngnttgkkqq gtktaemeee asgkfgtvss rdsqhlstfn
     1081 lertafrkds qrwyvategg maeksgleaa tgktfprasg lgareaegke egapdgetsd
     1141 gsglgqgdrf ltdvtcassa kdldnpedad sstcdhpskl peadesvarl cdyhlakrms
     1201 slqseghfsl qssqgssvda gcgtgssgsa catpvesplc pslgkhlipd asgkgvnyip
     1261 seerapglpn hgatfkelhp qtegmcprmt vpalhtaint eplfgtlrdg chrlpkiket
     1321 tv
//
LOCUS       NP_001310336             175 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome inhibitor PI31 subunit isoform 3 [Homo sapiens].
ACCESSION   NP_001310336
VERSION     NP_001310336.1
DBSOURCE    REFSEQ: accession NM_001323407.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Yang,S., Tang,D., Zhao,Y.C., Liu,H., Luo,S., Stinchcombe,T.E.,
            Glass,C., Su,L., Shen,S., Christiani,D.C., Wang,Q. and Wei,Q.
  TITLE     Potentially functional variants of ERAP1, PSMF1 and NCF2 in the
            MHC-I-related pathway predict non-small cell lung cancer survival
  JOURNAL   Cancer Immunol Immunother 70 (10), 2819-2833 (2021)
   PUBMED   33651148
  REMARK    GeneRIF: Potentially functional variants of ERAP1, PSMF1 and NCF2
            in the MHC-I-related pathway predict non-small cell lung cancer
            survival.
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 175)
  AUTHORS   McCutchen-Maloney,S.L., Matsuda,K., Shimbara,N., Binns,D.D.,
            Tanaka,K., Slaughter,C.A. and DeMartino,G.N.
  TITLE     cDNA cloning, expression, and functional characterization of PI31,
            a proline-rich inhibitor of the proteasome
  JOURNAL   J Biol Chem 275 (24), 18557-18565 (2000)
   PUBMED   10764772
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Tanahashi,N., Kawahara,H., Murakami,Y. and Tanaka,K.
  TITLE     The proteasome-dependent proteolytic system
  JOURNAL   Mol Biol Rep 26 (1-2), 3-9 (1999)
   PUBMED   10363639
  REMARK    Review article
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302164.1, BC126462.1,
            AL031665.19 and AA699495.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            protein that inhibits the activation of the proteasome by the 11S
            and 19S regulators. Alternative transcript variants have been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302164.1, SRR5189667.42396.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..175
                     /product="proteasome inhibitor PI31 subunit isoform 3"
                     /note="proteasome inhibitor PI31 subunit; proteasome
                     (prosome, macropain) inhibitor subunit 1 (PI31)"
                     /calculated_mol_wt=19160
     Region          <1..60
                     /region_name="PI31_Prot_N"
                     /note="PI31 proteasome regulator N-terminal; pfam11566"
                     /db_xref="CDD:463296"
     Region          94..160
                     /region_name="PI31_Prot_C"
                     /note="PI31 proteasome regulator; pfam08577"
                     /db_xref="CDD:430086"
     CDS             1..175
                     /gene="PSMF1"
                     /gene_synonym="PI31"
                     /coded_by="NM_001323407.2:283..810"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9491"
                     /db_xref="HGNC:HGNC:9571"
                     /db_xref="MIM:617858"
ORIGIN      
        1 milnvleygs qqvadltlnl ddyidaehlg dfhrtyknse elrsrivsgi itpiheqwek
       61 anvssphref ppatarevdp lripphhpht srqppwcdpl gpfvvggedl dpfgprrggm
      121 ivdplrsgfp ralidpssgl pnrlppgavp pgarfdpfgp igtsppgprp drrgq
//
LOCUS       NP_001357096             671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001357096
VERSION     NP_001357096.1
DBSOURCE    REFSEQ: accession NM_001370167.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.133991.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001370167.1:513..2528"
                     /note="isoform 1 is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_821066                197 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SOCS box protein 6 isoform 2 [Homo sapiens].
ACCESSION   NP_821066
VERSION     NP_821066.1
DBSOURCE    REFSEQ: accession NM_177999.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 197)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 197)
  AUTHORS   Zeng,W., Zhu,J.F., Guo,J., Huang,G.J., Ai,L.S., Zeng,Y. and
            Liao,W.J.
  TITLE     m6A-modified circFNDC3B inhibits colorectal cancer stemness and
            metastasis via RNF41-dependent ASB6 degradation
  JOURNAL   Cell Death Dis 13 (11), 1008 (2022)
   PUBMED   36446779
  REMARK    GeneRIF: m[6]A-modified circFNDC3B inhibits colorectal cancer
            stemness and metastasis via RNF41-dependent ASB6 degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 197)
  AUTHORS   Gong,L., Wang,K., Wang,M., Hu,R., Li,H., Gao,D. and Lin,M.
  TITLE     CUL5-ASB6 Complex Promotes p62/SQSTM1 Ubiquitination and
            Degradation to Regulate Cell Proliferation and Autophagy
  JOURNAL   Front Cell Dev Biol 9, 684885 (2021)
   PUBMED   34164402
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 197)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 197)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 197)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 197)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   8  (residues 1 to 197)
  AUTHORS   Kohroki,J., Nishiyama,T., Nakamura,T. and Masuho,Y.
  TITLE     ASB proteins interact with Cullin5 and Rbx2 to form E3 ubiquitin
            ligase complexes
  JOURNAL   FEBS Lett 579 (30), 6796-6802 (2005)
   PUBMED   16325183
REFERENCE   9  (residues 1 to 197)
  AUTHORS   Wilcox,A., Katsanakis,K.D., Bheda,F. and Pillay,T.S.
  TITLE     Asb6, an adipocyte-specific ankyrin and SOCS box protein, interacts
            with APS to enable recruitment of elongins B and C to the insulin
            receptor signaling complex
  JOURNAL   J Biol Chem 279 (37), 38881-38888 (2004)
   PUBMED   15231829
REFERENCE   10 (residues 1 to 197)
  AUTHORS   Kile,B.T., Schulman,B.A., Alexander,W.S., Nicola,N.A., Martin,H.M.
            and Hilton,D.J.
  TITLE     The SOCS box: a tale of destruction and degradation
  JOURNAL   Trends Biochem Sci 27 (5), 235-241 (2002)
   PUBMED   12076535
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590369.18.
            
            Summary: The protein encoded by this gene belongs to a family of
            ankyrin repeat proteins that, along with four other protein
            families, contain a C-terminal SOCS box motif. Growing evidence
            suggests that the SOCS box, similar to the F-box, acts as a bridge
            between specific substrate-binding domains and the more generic
            proteins that comprise a large family of E3 ubiquitin protein
            ligases. Alternatively spliced transcript variants have been
            identified for this gene. [provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (2) is shorter and has a
            unique C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001719.1, BI199939.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..197
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..197
                     /product="ankyrin repeat and SOCS box protein 6 isoform 2"
                     /note="ankyrin repeat and SOCS box protein 6"
                     /calculated_mol_wt=22242
     Region          <17..>160
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(42,45..47,49..50,54,57,67,69,74..75,78..80,82..83,
                     87,90,99,102,104,108..109,112..114,116..117,121,124,133)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          67..99
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          67..97
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     Region          102..133
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          102..131
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NWX5.1)"
     CDS             1..197
                     /gene="ASB6"
                     /coded_by="NM_177999.3:153..746"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6925.1"
                     /db_xref="GeneID:140459"
                     /db_xref="HGNC:HGNC:17181"
                     /db_xref="MIM:615051"
ORIGIN      
        1 mpflhgfrri ifeyqplvda ilgslgiqdp erqesldrps yvaseesril vltellerka
       61 hspfyqegvs nallkmaelg ltraadvllr hganlnfedp vtyytalhia vlrnqpdmve
      121 llvhhgadvn rrdrekllcs mlwpaatgcr stilrtfvsy wkegqtsrpp pkmgtqcspa
      181 sssclvrpwe gtkrrpr
//
LOCUS       NP_001356339             299 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001356339 XP_005258694
VERSION     NP_001356339.1
DBSOURCE    REFSEQ: accession NM_001369410.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 299)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 299)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3.
            
            On Apr 9, 2019 this sequence version replaced XP_005258694.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.11990.1,
                                           SRR1803612.226806.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..299
                     /product="DNA excision repair protein ERCC-1 isoform 4"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=32863
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..261
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..299
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369410.1:145..1044"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkvra lgknprswgk erapnkhnlr pqsfkvkkep ktrhsgfrl
//
LOCUS       NP_001354737             130 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box and leucine-rich protein 22 isoform 3 [Homo sapiens].
ACCESSION   NP_001354737
VERSION     NP_001354737.1
DBSOURCE    REFSEQ: accession NM_001367808.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Spaich,S., Will,R.D., Just,S., Spaich,S., Kuhn,C., Frank,D.,
            Berger,I.M., Wiemann,S., Korn,B., Koegl,M., Backs,J., Katus,H.A.,
            Rottbauer,W. and Frey,N.
  TITLE     F-box and leucine-rich repeat protein 22 is a cardiac-enriched
            F-box protein that regulates sarcomeric protein turnover and is
            essential for maintenance of contractile function in vivo
  JOURNAL   Circ Res 111 (12), 1504-1516 (2012)
   PUBMED   22972877
  REMARK    GeneRIF: Fbxl22 promotes the proteasome-dependent degradation of
            sarcomeric proteins and is essential for maintenance of normal
            contractile function.
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC118274.9 and AK096945.1.
            
            Summary: This gene encodes a member of the F-box protein family.
            This F-box protein interacts with S-phase kinase-associated protein
            1A and cullin in order to form SCF complexes which function as
            ubiquitin ligases.[provided by RefSeq, Sep 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096945.1, DA917017.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..130
                     /product="F-box and leucine-rich protein 22 isoform 3"
                     /EC_number="3.4.19.12"
                     /note="F-box/LRR-repeat protein 22; F-box and leucine-rich
                     protein 22"
                     /calculated_mol_wt=14952
     Region          9..51
                     /region_name="F-box_FBXL22"
                     /note="F-box domain found in F-box/LRR-repeat protein 22
                     (FBXL22) and similar proteins; cd22129"
                     /db_xref="CDD:438901"
     Site            order(12,16,19..20,23..24,28,30..31,35..37,39)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438901"
     CDS             1..130
                     /gene="FBXL22"
                     /gene_synonym="Fbl22"
                     /coded_by="NM_001367808.1:7..399"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92015.1"
                     /db_xref="GeneID:283807"
                     /db_xref="HGNC:HGNC:27537"
                     /db_xref="MIM:609088"
ORIGIN      
        1 mwplltmhit qlnrecllhl fsfldkdsrk slartcsqlh dvfedpalws llhfrsltel
       61 qkdnfllgpa lrslsicwhs srvqvcsied wlksafqrsi csrheslvnd fllrvcdrvr
      121 glndtvapgt
//
LOCUS       NP_065823                695 aa            linear   PRI 20-NOV-2025
DEFINITION  FMR1-interacting protein NUFIP2 [Homo sapiens].
ACCESSION   NP_065823
VERSION     NP_065823.1
DBSOURCE    REFSEQ: accession NM_020772.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 695)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 695)
  AUTHORS   Zou,Z., Wei,J., Chen,Y., Kang,Y., Shi,H., Yang,F., Shi,Z., Chen,S.,
            Zhou,Y., Sepich-Poore,C., Zhuang,X., Zhou,X., Jiang,H., Wen,Z.,
            Jin,P., Luo,C. and He,C.
  TITLE     FMRP phosphorylation modulates neuronal translation through YTHDF1
  JOURNAL   Mol Cell 83 (23), 4304-4317 (2023)
   PUBMED   37949069
  REMARK    GeneRIF: FMRP phosphorylation modulates neuronal translation
            through YTHDF1.
REFERENCE   3  (residues 1 to 695)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 695)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 695)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 695)
  AUTHORS   Ramos,A., Hollingworth,D., Adinolfi,S., Castets,M., Kelly,G.,
            Frenkiel,T.A., Bardoni,B. and Pastore,A.
  TITLE     The structure of the N-terminal domain of the fragile X mental
            retardation protein: a platform for protein-protein interaction
  JOURNAL   Structure 14 (1), 21-31 (2006)
   PUBMED   16407062
REFERENCE   7  (residues 1 to 695)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 695)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 695)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
REFERENCE   10 (residues 1 to 695)
  AUTHORS   Bardoni,B., Castets,M., Huot,M.E., Schenck,A., Adinolfi,S.,
            Corbin,F., Pastore,A., Khandjian,E.W. and Mandel,J.L.
  TITLE     82-FIP, a novel FMRP (fragile X mental retardation protein)
            interacting protein, shows a cell cycle-dependent intracellular
            localization
  JOURNAL   Hum Mol Genet 12 (14), 1689-1698 (2003)
   PUBMED   12837692
  REMARK    GeneRIF: identification and characterization of FIP-82, a novel
            FMRP-interacting protein associated to polyribosomes as a component
            of mRNP complexes containing FMRP
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK293075.1, AB037742.1, AC005412.8 and BM969349.1.
            
            Sequence Note: This RefSeq was created from transcript and genomic
            sequence data to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.216214.1,
                                           SRR1660805.17924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225388.9/ ENSP00000225388.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..695
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..695
                     /product="FMR1-interacting protein NUFIP2"
                     /note="82-kD FMRP Interacting Protein;
                     proliferation-inducing gene 1; FMRP-interacting protein 2;
                     82 kDa FMRP-interacting protein; cell
                     proliferation-inducing gene 1 protein; NUFIP2, FMR1
                     interacting protein 2"
                     /calculated_mol_wt=75990
     Region          1..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Region          89..688
                     /region_name="NUFIP2"
                     /note="Nuclear fragile X mental retardation-interacting
                     protein 2; pfam15293"
                     /db_xref="CDD:464619"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Region          155..189
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Region          204..234
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Region          261..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            291
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Region          369..402
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            592
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            655
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z417.1)"
     CDS             1..695
                     /gene="NUFIP2"
                     /gene_synonym="182-FIP; 82-FIP; FIP-82; NUFP2; PIG1"
                     /coded_by="NM_020772.3:90..2177"
                     /db_xref="CCDS:CCDS32600.1"
                     /db_xref="GeneID:57532"
                     /db_xref="HGNC:HGNC:17634"
                     /db_xref="MIM:609356"
ORIGIN      
        1 meekpgqpqp qhhhshhhph hhpqqqqqqp hhhhhyyfyn hshnhhhhhh hqqphqylqh
       61 gaegspkaqp kplkheqkht lqqhqetpkk ktgygelngn agereislkn lssdeatnpi
      121 srvlngnqqv vdtslkqtvk antfgkagik tknfiqknsm dkkngksyen ksgenqsvdk
      181 sdtipipngv vtnnsgyitn gymgkgadnd gsgsesgytt pkkrkarrns akgcenlniv
      241 qdkimqqets vptlkqglet fkpdyseqkg nrvdgskpiw kyetgpggts rgkpavgdml
      301 rkssdskpgv sskkfddrpk gkhasavask edswtlfkpp pvfpvdnssa kivpkisyas
      361 kvkenlnkti qnssvsptss sssssstget qtqsssrlsq vpmsalksvt sanfsngpvl
      421 agtdgnvypp ggqpllttaa ntltpissgt dsvlqdmslt saaveqikts lfiypsnmqt
      481 mllstaqvdl psqtdqqnlg difqnqwgls finepsagpe tvtgkssehk vmevtfqgey
      541 patlvsqgae iipsgtehpv fpkayelekr tspqvlgsil ksgttsesga lslepshigd
      601 lqkadtssqg alvflskdye iesqnplasp tntllgsake qryqrglern dswgsfdlra
      661 aivyhtkeme siwnlqkqdp kriityneam dspdq
//
LOCUS       NP_003083                225 aa            linear   PRI 20-NOV-2025
DEFINITION  U2 small nuclear ribonucleoprotein B'' [Homo sapiens].
ACCESSION   NP_003083
VERSION     NP_003083.1
DBSOURCE    REFSEQ: accession NM_003092.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Hong,W., Bennett,M., Xiao,Y., Feld Kramer,R., Wang,C. and Reed,R.
  TITLE     Association of U2 snRNP with the spliceosomal complex E
  JOURNAL   Nucleic Acids Res 25 (2), 354-361 (1997)
   PUBMED   9016565
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Laitinen,J., Saris,P., Holtta,E. and Pettersson,I.
  TITLE     U2-snRNP B' protein gene is an early growth-inducible gene
  JOURNAL   J Cell Biochem 58 (4), 490-498 (1995)
   PUBMED   7593271
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Feeney,R.J. and Zieve,G.W.
  TITLE     Nuclear exchange of the U1 and U2 snRNP-specific proteins
  JOURNAL   J Cell Biol 110 (4), 871-881 (1990)
   PUBMED   2139037
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Habets,W.J., Sillekens,P.T., Hoet,M.H., Schalken,J.A.,
            Roebroek,A.J., Leunissen,J.A., van de Ven,W.J. and van
            Venrooij,W.J.
  TITLE     Analysis of a cDNA clone expressing a human autoimmune antigen:
            full-length sequence of the U2 small nuclear RNA-associated B'
            antigen
  JOURNAL   Proc Natl Acad Sci U S A 84 (8), 2421-2425 (1987)
   PUBMED   2951739
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC018022.1, BM772256.1,
            AI741327.1 and AL034428.4.
            
            Summary: The protein encoded by this gene associates with stem loop
            IV of U2 small nuclear ribonucleoprotein (U2 snRNP) in the presence
            of snRNP-A'. The encoded protein may play a role in pre-mRNA
            splicing. Autoantibodies from patients with systemic lupus
            erythematosus frequently recognize epitopes on the encoded protein.
            Two transcript variants encoding the same protein have been found
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.193633.1,
                                           SRR3476690.249153.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246071.8/ ENSP00000246071.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..225
                     /product="U2 small nuclear ribonucleoprotein B''"
                     /note="U2 snRNP B''; small nuclear ribonucleoprotein
                     polypeptide B"
                     /calculated_mol_wt=25355
     Region          6..96
                     /region_name="RRM1_U2B"
                     /note="RNA recognition motif 1 in U2 small nuclear
                     ribonucleoprotein B' (U2B') and similar proteins; cd12478"
                     /db_xref="CDD:409907"
     Site            order(10,12..13,16..17,19..20,24,40..51,53,77,80,82..89)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409907"
     Region          99..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08579.1)"
     Site            111
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQI7; propagated from
                     UniProtKB/Swiss-Prot (P08579.1)"
     Region          146..225
                     /region_name="RRM2_U2B"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     U2 small nuclear ribonucleoprotein B' (U2B'); cd12481"
                     /db_xref="CDD:240925"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P08579.1)"
     CDS             1..225
                     /gene="SNRPB2"
                     /gene_synonym="Msl1; U2B''"
                     /coded_by="NM_003092.5:175..852"
                     /db_xref="CCDS:CCDS13123.1"
                     /db_xref="GeneID:6629"
                     /db_xref="HGNC:HGNC:11155"
                     /db_xref="MIM:603520"
ORIGIN      
        1 mdirpnhtiy innmndkikk eelkrslyal fsqfghvvdi valktmkmrg qafvifkelg
       61 sstnalrqlq gfpfygkpmr iqyaktdsdi iskmrgtfad kekkkekkka ktveqtattt
      121 nkkpgqgtpn santqgnstp npqvpdyppn yilflnnlpe etnemmlsml fnqfpgfkev
      181 rlvpgrhdia fvefendgqa gaardalqgf kitpshamki tyakk
//
LOCUS       NP_001278360             114 aa            linear   PRI 20-NOV-2025
DEFINITION  apoptosis regulator BAX isoform zeta [Homo sapiens].
ACCESSION   NP_001278360
VERSION     NP_001278360.1
DBSOURCE    REFSEQ: accession NM_001291431.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 114)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 114)
  AUTHORS   Dadsena,S., Cuevas Arenas,R., Vieira,G., Brodesser,S., Melo,M.N.
            and Garcia-Saez,A.J.
  TITLE     Lipid unsaturation promotes BAX and BAK pore activity during
            apoptosis
  JOURNAL   Nat Commun 15 (1), 4700 (2024)
   PUBMED   38830851
  REMARK    GeneRIF: Lipid unsaturation promotes BAX and BAK pore activity
            during apoptosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 114)
  AUTHORS   Schweighofer,S.V., Jans,D.C., Keller-Findeisen,J., Folmeg,A.,
            Ilgen,P., Bates,M. and Jakobs,S.
  TITLE     Endogenous BAX and BAK form mosaic rings of variable size and
            composition on apoptotic mitochondria
  JOURNAL   Cell Death Differ 31 (4), 469-478 (2024)
   PUBMED   38503846
  REMARK    GeneRIF: Endogenous BAX and BAK form mosaic rings of variable size
            and composition on apoptotic mitochondria.
REFERENCE   4  (residues 1 to 114)
  AUTHORS   Liu,X., Zhang,J., Wang,Z., Yan,M., Xu,M., Li,G., Shender,V.,
            Wei,J.J., Li,J., Shao,C., Zhang,S., Kong,B., Song,K. and Liu,Z.
  TITLE     Splicing Factor PQBP1 Curtails BAX Expression to Promote Ovarian
            Cancer Progression
  JOURNAL   Adv Sci (Weinh) 11 (15), e2306229 (2024)
   PUBMED   38342602
  REMARK    GeneRIF: Splicing Factor PQBP1 Curtails BAX Expression to Promote
            Ovarian Cancer Progression.
REFERENCE   5  (residues 1 to 114)
  AUTHORS   Chen,Y., Li,S., Yang,Z., Wang,T., Yin,F., Zhao,X. and Zhang,Y.
  TITLE     Value of Bax and Bcl2 expression in peripheral blood mononuclear
            cells for clinical prognosis of patients with chronic heart failure
  JOURNAL   Medicine (Baltimore) 103 (3), e36943 (2024)
   PUBMED   38241555
  REMARK    GeneRIF: Value of Bax and Bcl2 expression in peripheral blood
            mononuclear cells for clinical prognosis of patients with chronic
            heart failure.
REFERENCE   6  (residues 1 to 114)
  AUTHORS   Salomons,G.S., Buitenhuis,C.K., Martinez Munoz,C.,
            Verwijs-Jassen,M., Behrendt,H., Zsiros,J. and Smets,L.A.
  TITLE     Mutational analysis of Bax and Bcl-2 in childhood acute
            lymphoblastic leukaemia
  JOURNAL   Int J Cancer 79 (3), 273-277 (1998)
   PUBMED   9645350
REFERENCE   7  (residues 1 to 114)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   8  (residues 1 to 114)
  AUTHORS   Apte,S.S., Mattei,M.G. and Olsen,B.R.
  TITLE     Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and
            isolation of a novel alternatively spliced transcript, BAX delta
  JOURNAL   Genomics 26 (3), 592-594 (1995)
   PUBMED   7607685
REFERENCE   9  (residues 1 to 114)
  AUTHORS   Miyashita,T. and Reed,J.C.
  TITLE     Tumor suppressor p53 is a direct transcriptional activator of the
            human bax gene
  JOURNAL   Cell 80 (2), 293-299 (1995)
   PUBMED   7834749
REFERENCE   10 (residues 1 to 114)
  AUTHORS   Krieger,N.S., Sessler,N.E. and Bushinsky,D.A.
  TITLE     Acidosis inhibits osteoblastic and stimulates osteoclastic activity
            in vitro
  JOURNAL   Am J Physiol 262 (3 Pt 2), F442-F448 (1992)
   PUBMED   1558161
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE396495.1, AF250190.1,
            AI565203.1 and AK291076.1.
            
            Summary: The protein encoded by this gene belongs to the BCL2
            protein family. BCL2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. This protein forms a
            heterodimer with BCL2, and functions as an apoptotic activator. The
            association and the ratio of BAX to BCL2 also determines survival
            or death of a cell following an apoptotic stimulus. This protein is
            reported to interact with, and increase the opening of, the
            mitochondrial voltage-dependent anion channel (VDAC), which leads
            to the loss in membrane potential and the release of cytochrome c.
            The expression of this gene is regulated by the tumor suppressor
            P53 and has been shown to be involved in P53-mediated apoptosis.
            Multiple alternatively spliced transcript variants, which encode
            different isoforms, have been reported for this gene. [provided by
            RefSeq, Dec 2019].
            
            Transcript Variant: This variant (zeta) lacks two consecutive exons
            in the 5' region which causes translation initiation at a
            downstream start codon, and has an alternate splice site in the 3'
            coding region which causes a frame-shift, compared to variant 1.
            The resulting isoform (zeta) has a shorter N-terminus and a shorter
            and distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.656866.1, AF250190.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..114
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..114
                     /product="apoptosis regulator BAX isoform zeta"
                     /note="apoptosis regulator BAX; bcl2-L-4; bcl-2-like
                     protein 4; BCL2-associated X protein omega; Baxdelta2G9;
                     BCL2 associated X protein; Baxdelta2omega;
                     Baxdelta2G9omega; Baxdelta2(G8)-RFS protein"
                     /calculated_mol_wt=12756
     Region          <1..114
                     /region_name="bcl-2"
                     /note="apoptosis regulator; TIGR00865"
                     /db_xref="CDD:273308"
     Site            order(20..22,27..39)
                     /site_type="active"
                     /note="BH1 [active]"
                     /db_xref="CDD:132900"
     Site            72..86
                     /site_type="active"
                     /note="BH2 [active]"
                     /db_xref="CDD:132900"
     CDS             1..114
                     /gene="BAX"
                     /gene_synonym="BCL2L4"
                     /coded_by="NM_001291431.2:90..434"
                     /note="isoform zeta is encoded by transcript variant zeta"
                     /db_xref="GeneID:581"
                     /db_xref="HGNC:HGNC:959"
                     /db_xref="MIM:600040"
ORIGIN      
        1 miaavdtdsp revffrvaad mfsdgnfnwg rvvalfyfas klvlkalctk vpelirtimg
       61 wtldflrerl lgwiqdqggw dgllsyfgtp twqtvtifva gvltasltiw kkmg
//
LOCUS       NP_003208                237 aa            linear   PRI 20-NOV-2025
DEFINITION  bax inhibitor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_003208
VERSION     NP_003208.2
DBSOURCE    REFSEQ: accession NM_003217.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Liao,Y., Qiu,Z. and Bai,L.
  TITLE     miR-302d-3p regulates the viability, migration and apoptosis of
            breast cancer cells through regulating the TMBIM6-mediated ERK
            signaling pathway
  JOURNAL   Mol Med Rep 24 (6) (2021)
   PUBMED   34651659
  REMARK    GeneRIF: miR302d3p regulates the viability, migration and apoptosis
            of breast cancer cells through regulating the TMBIM6mediated ERK
            signaling pathway.
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Bhattarai,K.R., Kim,H.K., Chaudhary,M., Ur Rashid,M.M., Kim,J.,
            Kim,H.R. and Chae,H.J.
  TITLE     TMBIM6 regulates redox-associated posttranslational modifications
            of IRE1alpha and ER stress response failure in aging mice and
            humans
  JOURNAL   Redox Biol 47, 102128 (2021)
   PUBMED   34562874
  REMARK    GeneRIF: TMBIM6 regulates redox-associated posttranslational
            modifications of IRE1alpha and ER stress response failure in aging
            mice and humans.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Grzmil,M., Thelen,P., Hemmerlein,B., Schweyer,S., Voigt,S., Mury,D.
            and Burfeind,P.
  TITLE     Bax inhibitor-1 is overexpressed in prostate cancer and its
            specific down-regulation by RNA interference leads to cell death in
            human prostate carcinoma cells
  JOURNAL   Am J Pathol 163 (2), 543-552 (2003)
   PUBMED   12875974
  REMARK    GeneRIF: Results indicate that the human Bax inhibitor-1 gene may
            serve as a prostate cancer expression marker based on its
            overexpression in prostate carcinoma and prostate cancer cell
            lines.
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Jean,J.C., Oakes,S.M. and Joyce-Brady,M.
  TITLE     The Bax inhibitor-1 gene is differentially regulated in adult
            testis and developing lung by two alternative TATA-less promoters
  JOURNAL   Genomics 57 (2), 201-208 (1999)
   PUBMED   10198159
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Cowling,R.T. and Birnboim,H.C.
  TITLE     Preliminary characterization of the protein encoded by human
            testis-enhanced gene transcript (TEGT)
  JOURNAL   Mol Membr Biol 15 (4), 177-187 (1998)
   PUBMED   10087504
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Xu,Q. and Reed,J.C.
  TITLE     Bax inhibitor-1, a mammalian apoptosis suppressor identified by
            functional screening in yeast
  JOURNAL   Mol Cell 1 (3), 337-346 (1998)
   PUBMED   9660918
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Walter,L., Marynen,P., Szpirer,J., Levan,G. and Gunther,E.
  TITLE     Identification of a novel conserved human gene, TEGT
  JOURNAL   Genomics 28 (2), 301-304 (1995)
   PUBMED   8530040
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK130050.1, BQ613936.1 and AA057740.1.
            
            On Jun 9, 2007 this sequence version replaced NP_003208.1.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and it encodes the shorter protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK130050.1, SRR3476690.463527.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267115.10/ ENSP00000267115.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..237
                     /product="bax inhibitor 1 isoform 1"
                     /note="BAX inhibitor 1; testis-enhanced gene transcript
                     protein; transmembrane BAX inhibitor motif-containing
                     protein 6; testis enhanced gene transcript"
                     /calculated_mol_wt=26407
     Region          16..228
                     /region_name="BI-1"
                     /note="BAX inhibitor (BI)-1; cd10430"
                     /db_xref="CDD:198412"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     Site            167..187
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P55061.2)"
     CDS             1..237
                     /gene="TMBIM6"
                     /gene_synonym="BAXI1; BI-1; TEGT"
                     /coded_by="NM_003217.3:86..799"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31797.1"
                     /db_xref="GeneID:7009"
                     /db_xref="HGNC:HGNC:11723"
                     /db_xref="MIM:600748"
ORIGIN      
        1 mnifdrkinf dallkfshit pstqqhlkkv yasfalcmfv aaagayvhmv thfiqaglls
       61 algslilmiw lmatphshet eqkrlgllag fafltgvglg palefciavn psilptafmg
      121 tamiftcftl salyarrrsy lflggilmsa lsllllsslg nvffgsiwlf qanlyvglvv
      181 mcgfvlfdtq liiekaehgd qdyiwhcidl fldfitvfrk lmmilamnek dkkkekk
//
LOCUS       NP_001269555             614 aa            linear   PRI 20-NOV-2025
DEFINITION  lamin isoform A-delta50 [Homo sapiens].
ACCESSION   NP_001269555
VERSION     NP_001269555.1
DBSOURCE    REFSEQ: accession NM_001282626.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 614)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 614)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 614)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 614)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 614)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 614)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 614)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 614)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 614)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 614)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 614)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA551594.1, AY357727.1,
            BU685425.1, BU732343.1 and AI872233.1.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Transcript Variant: This variant (7) uses an alternate 3' exon
            structure and thus differs in the 3' coding region and 3' UTR,
            compared to variant 1. This results in a shorter isoform
            (A-delta50, also known as progerin) with a distinct C-terminus when
            compared to isoform prelamin A. Although this isoform has been
            linked to Hutchinson-Gilford progeria syndrome, it is also found in
            unaffected individuals and thought to be linked to cellular
            terminal differentiation and physiological aging (see PubMed IDs:
            12702809, 16645051, and 18060063).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY357727.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..614
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..614
                     /product="lamin isoform A-delta50"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=69118
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          552..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..614
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_001282626.2:209..2053"
                     /note="isoform A-delta50 is encoded by transcript variant
                     7"
                     /db_xref="CCDS:CCDS72941.1"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhgshc sssgdpaeyn lrsrtvlcgt cgqpadkasa
      601 sgsgaqspqn csim
//
LOCUS       NP_001309191             395 aa            linear   PRI 20-NOV-2025
DEFINITION  G1/S-specific cyclin-E1 isoform 5 [Homo sapiens].
ACCESSION   NP_001309191 XP_006723520
VERSION     NP_001309191.1
DBSOURCE    REFSEQ: accession NM_001322262.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Lee,S.J., Jeon,S.H., Cho,S., Kim,C.M., Yoo,J.K., Oh,S.H., Kim,J.H.,
            Yang,Y.D. and Kim,J.K.
  TITLE     hsa-miR-CHA2, a novel microRNA, exhibits anticancer effects by
            suppressing cyclin E1 in human non-small cell lung cancer cells
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (6), 167250 (2024)
   PUBMED   38763409
  REMARK    GeneRIF: hsa-miR-CHA2, a novel microRNA, exhibits anticancer
            effects by suppressing cyclin E1 in human non-small cell lung
            cancer cells.
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Rustgi,N., Wu,S., Samec,T., Walker,P., Xiu,J., Lou,E., Goel,S.,
            Saeed,A. and Moy,R.H.
  TITLE     Molecular Landscape and Clinical Implication of CCNE1-amplified
            Esophagogastric Cancer
  JOURNAL   Cancer Res Commun 4 (6), 1399-1409 (2024)
   PUBMED   38717153
  REMARK    GeneRIF: Molecular Landscape and Clinical Implication of
            CCNE1-amplified Esophagogastric Cancer.
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Audrey,A., Kok,Y.P., Yu,S., de Haan,L., van de Kooij,B., van den
            Tempel,N., Chen,M., de Boer,H.R., van der Vegt,B. and van
            Vugt,M.A.T.M.
  TITLE     RAD52-dependent mitotic DNA synthesis is required for genome
            stability in Cyclin E1-overexpressing cells
  JOURNAL   Cell Rep 43 (4), 114116 (2024)
   PUBMED   38625790
  REMARK    GeneRIF: RAD52-dependent mitotic DNA synthesis is required for
            genome stability in Cyclin E1-overexpressing cells.
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Mumberg,D., Wick,M., Burger,C., Haas,K., Funk,M. and Muller,R.
  TITLE     Cyclin ET, a new splice variant of human cyclin E with a unique
            expression pattern during cell cycle progression and
            differentiation
  JOURNAL   Nucleic Acids Res 25 (11), 2098-2105 (1997)
   PUBMED   9153308
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Sewing,A., Ronicke,V., Burger,C., Funk,M. and Muller,R.
  TITLE     Alternative splicing of human cyclin E
  JOURNAL   J Cell Sci 107 (Pt 2), 581-588 (1994)
   PUBMED   8207080
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Hinds,P.W., Mittnacht,S., Dulic,V., Arnold,A., Reed,S.I. and
            Weinberg,R.A.
  TITLE     Regulation of retinoblastoma protein functions by ectopic
            expression of human cyclins
  JOURNAL   Cell 70 (6), 993-1006 (1992)
   PUBMED   1388095
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Koff,A., Cross,F., Fisher,A., Schumacher,J., Leguellec,K.,
            Philippe,M. and Roberts,J.M.
  TITLE     Human cyclin E, a new cyclin that interacts with two members of the
            CDC2 gene family
  JOURNAL   Cell 66 (6), 1217-1228 (1991)
   PUBMED   1833068
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Lew,D.J., Dulic,V. and Reed,S.I.
  TITLE     Isolation of three novel human cyclins by rescue of G1 cyclin (Cln)
            function in yeast
  JOURNAL   Cell 66 (6), 1197-1206 (1991)
   PUBMED   1833066
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008798.10, AK291549.1 and
            BQ018270.1.
            
            On Apr 8, 2016 this sequence version replaced XP_006723520.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin forms a complex with and functions as a regulatory subunit
            of CDK2, whose activity is required for cell cycle G1/S transition.
            This protein accumulates at the G1-S phase boundary and is degraded
            as cells progress through S phase. Overexpression of this gene has
            been observed in many tumors, which results in chromosome
            instability, and thus may contribute to tumorigenesis. This protein
            was found to associate with, and be involved in, the
            phosphorylation of NPAT protein (nuclear protein mapped to the ATM
            locus), which participates in cell-cycle regulated histone gene
            expression and plays a critical role in promoting cell-cycle
            progression in the absence of pRB. [provided by RefSeq, Apr 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.212726.1,
                                           SRR1163655.213004.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..395
                     /product="G1/S-specific cyclin-E1 isoform 5"
                     /note="G1/S-specific cyclin-E1"
                     /calculated_mol_wt=45019
     Region          88..224
                     /region_name="CYCLIN_CCNE1_rpt1"
                     /note="first cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20579"
                     /db_xref="CDD:410282"
     Site            order(94..95,97,100..101,104..105,108,112,147,182,
                     186..190,194..195,212,215..216,219..220,223..224)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410282"
     Region          228..341
                     /region_name="CYCLIN_CCNE1_rpt2"
                     /note="second cyclin box found in G1/S-specific cyclin-E1
                     (CCNE1); cd20581"
                     /db_xref="CDD:410284"
     Site            order(229,236..237,240,249..253,255,340..341)
                     /site_type="other"
                     /note="CDK interface [polypeptide binding]"
                     /db_xref="CDD:410284"
     CDS             1..395
                     /gene="CCNE1"
                     /gene_synonym="CCNE; pCCNE1"
                     /coded_by="NM_001322262.2:185..1372"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS46035.1"
                     /db_xref="GeneID:898"
                     /db_xref="HGNC:HGNC:1589"
                     /db_xref="MIM:123837"
ORIGIN      
        1 mkedggaefs arsrkrkanv tvflqdpdee makidrtard qcgsqpwdnn avcadpcsli
       61 ptpdkedddr vypnstckpr iiapsrgspl pvlswanree vwkimlnkek tylrdqhfle
      121 qhpllqpkmr ailldwlmev cevyklhret fylaqdffdr ymatqenvvk tllqligiss
      181 lfiaakleei yppklhqfay vtdgacsgde iltmelmimk alkwrlsplt ivswlnvymq
      241 vaylndlhev llpqypqqif iqiaelldlc vldvdclefp ygilaasaly hfssselmqk
      301 vsgyqwcdie ncvkwmvpfa mviretgssk lkhfrgvade dahniqthrd sldlldkara
      361 kkamlseqnr asplpsgllt ppqsgkkqss gpema
//
LOCUS       NP_008976                399 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein 43 isoform a [Homo sapiens].
ACCESSION   NP_008976
VERSION     NP_008976.1
DBSOURCE    REFSEQ: accession NM_007045.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Steib,E., Laporte,M.H., Gambarotto,D., Olieric,N., Zheng,C.,
            Borgers,S., Olieric,V., Le Guennec,M., Koll,F., Tassin,A.M.,
            Steinmetz,M.O., Guichard,P. and Hamel,V.
  TITLE     WDR90 is a centriolar microtubule wall protein important for
            centriole architecture integrity
  JOURNAL   Elife 9, e57205 (2020)
   PUBMED   32946374
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 399)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Yan,X., Habedanck,R. and Nigg,E.A.
  TITLE     A complex of two centrosomal proteins, CAP350 and FOP, cooperates
            with EB1 in microtubule anchoring
  JOURNAL   Mol Biol Cell 17 (2), 634-644 (2006)
   PUBMED   16314388
  REMARK    GeneRIF: CAP350 interacts directly with FOP (FGFR1 oncogene
            partner) to form a centrosomal complex required for microtubule
            anchoring.
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Guasch,G., Delaval,B., Arnoulet,C., Xie,M.J., Xerri,L., Sainty,D.,
            Birnbaum,D. and Pebusque,M.J.
  TITLE     FOP-FGFR1 tyrosine kinase, the product of a t(6;8) translocation,
            induces a fatal myeloproliferative disease in mice
  JOURNAL   Blood 103 (1), 309-312 (2004)
   PUBMED   12969958
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Andersen,J.S., Wilkinson,C.J., Mayor,T., Mortensen,P., Nigg,E.A.
            and Mann,M.
  TITLE     Proteomic characterization of the human centrosome by protein
            correlation profiling
  JOURNAL   Nature 426 (6966), 570-574 (2003)
   PUBMED   14654843
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Guasch,G., Ollendorff,V., Borg,J.P., Birnbaum,D. and Pebusque,M.J.
  TITLE     8p12 stem cell myeloproliferative disorder: the FOP-fibroblast
            growth factor receptor 1 fusion protein of the t(6;8) translocation
            induces cell survival mediated by mitogen-activated protein kinase
            and phosphatidylinositol 3-kinase/Akt/mTOR pathways
  JOURNAL   Mol Cell Biol 21 (23), 8129-8142 (2001)
   PUBMED   11689702
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Popovici,C., Zhang,B., Gregoire,M.J., Jonveaux,P.,
            Lafage-Pochitaloff,M., Birnbaum,D. and Pebusque,M.J.
  TITLE     The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative
            disorder fuses a novel gene, FOP, to fibroblast growth factor
            receptor 1
  JOURNAL   Blood 93 (4), 1381-1389 (1999)
   PUBMED   9949182
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC418208.1, AK312791.1 and
            Z94721.1.
            
            Summary: This gene encodes a largely hydrophilic centrosomal
            protein that is required for anchoring microtubules to subcellular
            structures. A t(6;8)(q27;p11) chromosomal translocation, fusing
            this gene and the fibroblast growth factor receptor 1 (FGFR1) gene,
            has been found in cases of myeloproliferative disorder. The
            resulting chimeric protein contains the N-terminal leucine-rich
            region of this encoded protein fused to the catalytic domain of
            FGFR1. Alterations in this gene may also be associated with Crohn's
            disease, Graves' disease, and vitiligo. Alternatively spliced
            transcript variants that encode different proteins have been
            identified. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.246086.1,
                                           SRR1803615.81276.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366847.9/ ENSP00000355812.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q27"
     Protein         1..399
                     /product="centrosomal protein 43 isoform a"
                     /note="fibroblast growth factor receptor 1 oncogene
                     partner; FGFR1 oncogene partner"
                     /calculated_mol_wt=42934
     Region          54..134
                     /region_name="FOP_dimer"
                     /note="FOP N terminal dimerization domain; pfam09398"
                     /db_xref="CDD:312785"
     Region          139..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95684.1)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95684.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            173..174
                     /site_type="other"
                     /note="Breakpoint for translocation to form CEP43-FGFR1 or
                     FGFR1-CEP43 fusion proteins; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Region          232..308
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95684.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     Region          331..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95684.1)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q66JX5; propagated from
                     UniProtKB/Swiss-Prot (O95684.1)"
     CDS             1..399
                     /gene="CEP43"
                     /gene_synonym="FGFR1OP; FOP"
                     /coded_by="NM_007045.4:17..1216"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5296.1"
                     /db_xref="GeneID:11116"
                     /db_xref="HGNC:HGNC:17012"
                     /db_xref="MIM:605392"
ORIGIN      
        1 maataaavva eedtelrdll vqtlensgvl nrikaelraa vflaleeqek venktplvne
       61 slkkflntkd grlvaslvae flqffnldft lavfqpetst lqglegrenl ardlgiieae
      121 gtvggpllle virrcqqkek gpttgegald lsdvhsppks pegktsaqtt pskiprykgq
      181 gkkktsgqka gdkkandean qsdtsvslse pksksslhll shetkigsfl snrtldgkdk
      241 aglcpdeddm egdsffddpi pkpektyglr keprkqagsl aslsdapplk sglsslagap
      301 slkdseskrg ntvlkdlkli sdkigslglg tgedddyvdd fnstshrsek seisigeeie
      361 edlsveiddi ntsdklddlt qdltvsqlsd vadyledva
//
LOCUS       NP_001240317            1171 aa            linear   PRI 20-NOV-2025
DEFINITION  neural cell adhesion molecule L1-like protein isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001240317
VERSION     NP_001240317.1
DBSOURCE    REFSEQ: accession NM_001253388.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1171)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   2  (residues 1 to 1171)
  AUTHORS   Qin,M., Gao,X., Luo,W., Ou,K., Lu,H., Liu,H. and Zhuang,Q.
  TITLE     Expression of CHL1 in Clear Cell Renal Cell Carcinoma and its
            Association With Prognosis
  JOURNAL   Appl Immunohistochem Mol Morphol 30 (3), 209-214 (2022)
   PUBMED   35262525
  REMARK    GeneRIF: Expression of CHL1 in Clear Cell Renal Cell Carcinoma and
            its Association With Prognosis.
REFERENCE   3  (residues 1 to 1171)
  AUTHORS   Tian,W., Yang,X., Yang,H., Lv,M., Sun,X. and Zhou,B.
  TITLE     Exosomal miR-338-3p suppresses non-small-cell lung cancer cells
            metastasis by inhibiting CHL1 through the MAPK signaling pathway
  JOURNAL   Cell Death Dis 12 (11), 1030 (2021)
   PUBMED   34718336
  REMARK    GeneRIF: Exosomal miR-338-3p suppresses non-small-cell lung cancer
            cells metastasis by inhibiting CHL1 through the MAPK signaling
            pathway.
            Erratum:[Cell Death Dis. 2022 May 19;13(5):473. doi:
            10.1038/s41419-022-04933-3. PMID: 35589682]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1171)
  AUTHORS   Chen,Y., Sun,T., Niu,Y., Wang,D., Liu,K., Wang,T., Wang,S., Xu,H.
            and Liu,J.
  TITLE     Cell adhesion molecule L1 like plays a role in the pathogenesis of
            idiopathic hypogonadotropic hypogonadism
  JOURNAL   J Endocrinol Invest 44 (8), 1739-1751 (2021)
   PUBMED   33453020
  REMARK    GeneRIF: Cell adhesion molecule L1 like plays a role in the
            pathogenesis of idiopathic hypogonadotropic hypogonadism.
            Erratum:[J Endocrinol Invest. 2023 Apr;46(4):853. doi:
            10.1007/s40618-022-01942-z. PMID: 36315353]
REFERENCE   5  (residues 1 to 1171)
  AUTHORS   Ognibene,M. and Pezzolo,A.
  TITLE     Ezrin interacts with the tumor suppressor CHL1 and promotes
            neuronal differentiation of human neuroblastoma
  JOURNAL   PLoS One 15 (12), e0244069 (2020)
   PUBMED   33326488
  REMARK    GeneRIF: Ezrin interacts with the tumor suppressor CHL1 and
            promotes neuronal differentiation of human neuroblastoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1171)
  AUTHORS   Gast,D., Riedle,S., Riedle,S., Schabath,H., Schlich,S.,
            Schneider,A., Issa,Y., Stoeck,A., Fogel,M., Joumaa,S., Wenger,T.,
            Herr,I., Gutwein,P. and Altevogt,P.
  TITLE     L1 augments cell migration and tumor growth but not beta3 integrin
            expression in ovarian carcinomas
  JOURNAL   Int J Cancer 115 (4), 658-665 (2005)
   PUBMED   15704102
  REMARK    GeneRIF: L1 could drive progression by enhancing cell migration and
            tumor growth in ovarian carcinoma.
REFERENCE   7  (residues 1 to 1171)
  AUTHORS   Chen,Q.Y., Chen,Q., Feng,G.Y., Lindpaintner,K., Chen,Y., Sun,X.,
            Chen,Z., Gao,Z., Tang,J. and He,L.
  TITLE     Case-control association study of the close homologue of L1 (CHL1)
            gene and schizophrenia in the Chinese population
  JOURNAL   Schizophr Res 73 (2-3), 269-274 (2005)
   PUBMED   15653271
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 1171)
  AUTHORS   Sakurai,K., Migita,O., Toru,M. and Arinami,T.
  TITLE     An association between a missense polymorphism in the close
            homologue of L1 (CHL1, CALL) gene and schizophrenia
  JOURNAL   Mol Psychiatry 7 (4), 412-415 (2002)
   PUBMED   11986985
  REMARK    GeneRIF: An association between a missense polymorphism in the
            close homologue of L1 (CHL1, CALL) gene and schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1171)
  AUTHORS   Angeloni,D., Lindor,N.M., Pack,S., Latif,F., Wei,M.H. and
            Lerman,M.I.
  TITLE     CALL gene is haploinsufficient in a 3p- syndrome patient
  JOURNAL   Am J Med Genet 86 (5), 482-485 (1999)
   PUBMED   10508992
REFERENCE   10 (residues 1 to 1171)
  AUTHORS   Wei,M.H., Karavanova,I., Ivanov,S.V., Popescu,N.C., Keck,C.L.,
            Pack,S., Eisen,J.A. and Lerman,M.I.
  TITLE     In silico-initiated cloning and molecular characterization of a
            novel human member of the L1 gene family of neural cell adhesion
            molecules
  JOURNAL   Hum Genet 103 (3), 355-364 (1998)
   PUBMED   9799093
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026187.4, BC143498.1,
            AC011609.9 and R40400.1.
            
            Summary: The protein encoded by this gene is a member of the L1
            gene family of neural cell adhesion molecules. It is a neural
            recognition molecule that may be involved in signal transduction
            pathways. The deletion of one copy of this gene may be responsible
            for mental defects in patients with 3p- syndrome. This protein may
            also play a role in the growth of certain cancers. Alternate
            splicing results in both coding and non-coding variants. [provided
            by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (3) lacks an in-frame exon in the
            coding region, compared to variant 1. This variant encodes isoform
            3, which is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.233623.1,
                                           SRR1803611.239914.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1171
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.3"
     Protein         1..1171
                     /product="neural cell adhesion molecule L1-like protein
                     isoform 3 precursor"
                     /note="cell adhesion molecule with homology to L1CAM
                     (close homologue of L1); cell adhesion molecule with
                     homology to L1CAM (close homolog of L1); L1 cell adhesion
                     molecule 2; neural cell adhesion molecule L1-like protein"
                     /calculated_mol_wt=128047
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2767
     Region          35..126
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          53..57
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          66..70
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          90..94
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          106..111
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          120..123
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          135..225
                     /region_name="IgI_2_L1-CAM_like"
                     /note="Second immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM), and similar domains; member
                     of the I-set of Ig superfamily (IgSF) domains; cd05845"
                     /db_xref="CDD:409432"
     Region          135..138
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409432"
     Region          140..144
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409432"
     Region          147..155
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409432"
     Region          162..168
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409432"
     Region          171..174
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409432"
     Region          180..184
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409432"
     Region          186..190
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409432"
     Region          201..209
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409432"
     Region          212..225
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409432"
     Region          262..344
                     /region_name="Ig3_L1-CAM_like"
                     /note="Third immunoglobulin (Ig)-like domain of the L1
                     cell adhesion molecule (CAM), and similar domains;
                     cd05731"
                     /db_xref="CDD:409394"
     Region          274..278
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409394"
     Region          287..291
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409394"
     Region          309..313
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409394"
     Region          323..328
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409394"
     Region          336..339
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409394"
     Region          348..435
                     /region_name="Ig4_L1-NrCAM_like"
                     /note="Fourth immunoglobulin (Ig)-like domain of L1,
                     Ng-CAM (Neuron-glia CAM cell adhesion molecule), and NrCAM
                     (Ng-CAM-related); cd04978"
                     /db_xref="CDD:409367"
     Region          364..368
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409367"
     Region          377..381
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409367"
     Region          400..404
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409367"
     Region          414..419
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409367"
     Region          427..430
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409367"
     Region          448..525
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          457..461
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          470..474
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          493..497
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          507..512
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          520..523
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          548..617
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cd00096"
                     /db_xref="CDD:409353"
     Region          548..552
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          565..569
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          590..594
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          604..609
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          <616..>868
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          628..717
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(628,694,709)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(710..711,713..714)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          834..927
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(916..917,919..920)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          932..1027
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(932,1001,1016)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(1017..1018,1020..1021)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          1067..1152
                     /region_name="Bravo_FIGEY"
                     /note="Bravo-like intracellular region; pfam13882"
                     /db_xref="CDD:464016"
     CDS             1..1171
                     /gene="CHL1"
                     /gene_synonym="CALL; L1CAM2"
                     /coded_by="NM_001253388.1:95..3610"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS74887.1"
                     /db_xref="GeneID:10752"
                     /db_xref="HGNC:HGNC:1939"
                     /db_xref="MIM:607416"
ORIGIN      
        1 meplllgrgl ivylmflllk fskaieipss vqqvptiikq skvqvafpfd eyfqieceak
       61 gnpeptfswt kdgnpfyftd hriipsnnsg tfripneghi shfqgkyrcf asnklgiams
      121 eeiefivpsv pkfpkekidp leveegdpiv lpcnppkglp plhiywmnie lehieqderv
      181 ymsqkgdlyf anveekdsrn dyccfaafpr lrtivqkmpm kltvnslkha ndssssteig
      241 skansikqrk pklllpptes gsessitilk geilllecfa eglptpqvdw nkiggdlpkg
      301 retkenygkt lkienvsyqd kgnyrctasn flgtathdfh viveepprwt kkpqsavyst
      361 gsngillcea egepqptikw rvngspvdnh pfagdvvfpr eisftnlqpn htavyqceas
      421 nvhgtilana nidvvdvrpl iqtkdgenya tvvgysaflh ceffaspeav vswqkveevk
      481 plegrryhiy engtlqinrt teedagsysc wvenaigkta vtanldirna tklrvspknp
      541 ripklhmlel hceskcdshl khslklswsk dgeafeingt edgriiidga nltisnvtle
      601 dqgiyccsah taldsaadit qvtvldvpdp penlhlserq nrsvrltwea gadhnsnise
      661 yivefegnke epgrweeltr vqgkkttvil plapfvryqf rviavnevgr sqpsqpsdhh
      721 etppaapdrn pqnirvqasq pkemiikwep lksmeqngpg leyrvtwkpq gapveweeet
      781 vtnhtlrvmt pavyapydvk vqainqlgsg pdpqsvtlys gedypdtapv ihgvdvinst
      841 lvkvtwstvp kdrvhgrlkg yqinwwktks lldgrthpke vnilrfsgqr nsgmvpslda
      901 fsefhltvla ynskgagpes epyifqtpeg vpeqptflkv ikvdkdtatl swglpkklng
      961 nltgyllqyq iindtyeige lndinittps kpswhlsnln attkykfylr actsqgcgkp
     1021 iteesstlge gkyaglyddi stqgwfiglm caialltlll ltvcfvkrnr ggkysvkeke
     1081 dlhpdpeiqs vkdetfgeys dsdekplkgs lrslnrdmqp tesadslvey gegdhglfse
     1141 dgsfigayag skekgsvesn gsstatfplr a
//
LOCUS       NP_001354635             798 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform qqq [Homo sapiens].
ACCESSION   NP_001354635
VERSION     NP_001354635.1
DBSOURCE    REFSEQ: accession NM_001367706.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..798
                     /product="SUN domain-containing protein 1 isoform qqq"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=88519
     Region          12..335
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <409..>633
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          461..514
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(461,464..465,468,471..472,475..476,478..479,
                     482..483,485..486,489..490,492..493,496,499..500,503,
                     506..507,510..511,513..514)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          591..649
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          692..796
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..798
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367706.1:105..2501"
                     /note="isoform qqq is encoded by transcript variant 69"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril
      181 wlarytassf ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy
      241 ygrmnvrevl redghlsvng ealcyfllqi lrrigavgqa vsrtawsalw lavvapgkaa
      301 sgvfwwlgig wyqfvtlisw lnvflltrcl rnickflvll iplflllagl slrgqgnffs
      361 flpvlnwasm hrtqrvddpq dvfkpttsrl kqplqgdsea fpwhwmsgve qqvaslsgqc
      421 hhhgenlrel ttllqklqar vdqmeggaag psasvrdavg qppretdfma fhqehevrms
      481 hledilgklr ekseaiqkel eqtkqktisa vgeqllptve hlqleldqlk selsswrhvk
      541 tgcetvdavq ervdvqvrem vkllfsedqq ggsleqllqr fssqfvskgd lqtmlrdlql
      601 qilrnvthhv svtkqlptse avvsavseag asgiteaqar aivnsalkly sqdktgmvdf
      661 alesgggsil strcsetyet ktalmslfgi plwyfsqspr vviqpdiypg ncwafkgsqg
      721 ylvvrlsmmi hpaaftlehi pktlsptgni ssapkdfavy krpddtafqi velrifsnwg
      781 hpeytclyrf rvhgepvk
//
LOCUS       NP_000779                260 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxycytidine kinase [Homo sapiens].
ACCESSION   NP_000779
VERSION     NP_000779.1
DBSOURCE    REFSEQ: accession NM_000788.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Dash,S., Ueda,T., Komuro,A., Honda,M., Sugisawa,R. and Okada,H.
  TITLE     Deoxycytidine kinase inactivation enhances gemcitabine resistance
            and sensitizes mitochondrial metabolism interference in pancreatic
            cancer
  JOURNAL   Cell Death Dis 15 (2), 131 (2024)
   PUBMED   38346958
  REMARK    GeneRIF: Deoxycytidine kinase inactivation enhances gemcitabine
            resistance and sensitizes mitochondrial metabolism interference in
            pancreatic cancer.
            Erratum:[Cell Death Dis. 2024 May 31;15(5):384. doi:
            10.1038/s41419-024-06628-3. PMID: 38821944]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Yoshida,K., Fujita,A., Narazaki,H., Asano,T. and Itoh,Y.
  TITLE     Drug resistance to nelarabine in leukemia cell lines might be
            caused by reduced expression of deoxycytidine kinase through
            epigenetic mechanisms
  JOURNAL   Cancer Chemother Pharmacol 89 (1), 83-91 (2022)
   PUBMED   34825941
  REMARK    GeneRIF: Drug resistance to nelarabine in leukemia cell lines might
            be caused by reduced expression of deoxycytidine kinase through
            epigenetic mechanisms.
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Hosokawa,M., Seiki,R., Iwakawa,S. and Ogawara,K.I.
  TITLE     Combination of azacytidine and curcumin is a potential alternative
            in decitabine-resistant colorectal cancer cells with attenuated
            deoxycytidine kinase
  JOURNAL   Biochem Biophys Res Commun 578, 157-162 (2021)
   PUBMED   34571370
  REMARK    GeneRIF: Combination of azacytidine and curcumin is a potential
            alternative in decitabine-resistant colorectal cancer cells with
            attenuated deoxycytidine kinase.
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Hellendahl,K.F., Fehlau,M., Hans,S., Neubauer,P. and Kurreck,A.
  TITLE     Semi-Automated High-Throughput Substrate Screening Assay for
            Nucleoside Kinases
  JOURNAL   Int J Mol Sci 22 (21), 11558 (2021)
   PUBMED   34768989
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Eriksson,S., Cederlund,E., Bergman,T., Jornvall,H. and Bohman,C.
  TITLE     Characterization of human deoxycytidine kinase. Correlation with
            cDNA sequences
  JOURNAL   FEBS Lett 280 (2), 363-366 (1991)
   PUBMED   2013338
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Chottiner,E.G., Shewach,D.S., Datta,N.S., Ashcraft,E., Gribbin,D.,
            Ginsburg,D., Fox,I.H. and Mitchell,B.S.
  TITLE     Cloning and expression of human deoxycytidine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 88 (4), 1531-1535 (1991)
   PUBMED   1996353
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Datta,N.S., Shewach,D.S., Mitchell,B.S. and Fox,I.H.
  TITLE     Kinetic properties and inhibition of human T lymphoblast
            deoxycytidine kinase
  JOURNAL   J Biol Chem 264 (16), 9359-9364 (1989)
   PUBMED   2542307
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Datta,N.S., Shewach,D.S., Hurley,M.C., Mitchell,B.S. and Fox,I.H.
  TITLE     Human T-lymphoblast deoxycytidine kinase: purification and
            properties
  JOURNAL   Biochemistry 28 (1), 114-123 (1989)
   PUBMED   2539852
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Bohman,C. and Eriksson,S.
  TITLE     Deoxycytidine kinase from human leukemic spleen: preparation and
            characteristics of homogeneous enzyme
  JOURNAL   Biochemistry 27 (12), 4258-4265 (1988)
   PUBMED   2844225
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI601939.1, CD014016.1 and
            BC103764.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary:  Deoxycytidine kinase (DCK) is required for the
            phosphorylation of several deoxyribonucleosides and their
            nucleoside analogs.  Deficiency of DCK is associated with
            resistance to antiviral and anticancer chemotherapeutic agents.
            Conversely, increased deoxycytidine kinase activity is associated
            with increased activation of these compounds to cytotoxic
            nucleoside triphosphate derivatives.  DCK is clinically important
            because of its relationship to drug resistance and sensitivity.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC103764.1, SRR1660803.117849.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286648.10/ ENSP00000286648.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..260
                     /product="deoxycytidine kinase"
                     /EC_number="2.7.1.74"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxynucleoside kinase; deoxyadenosine kinase;
                     deoxyguanosine kinase"
                     /calculated_mol_wt=30388
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000305|PubMed:20637175; propagated from
                     UniProtKB/Swiss-Prot (P27707.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK1.
                     /evidence=ECO:0000305|PubMed:20637175; propagated from
                     UniProtKB/Swiss-Prot (P27707.1)"
     Region          24..258
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            order(32,34..35,86,96..97,137,192,197)
                     /site_type="other"
                     /note="Substrate-binding site [chemical binding]"
                     /db_xref="CDD:238836"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CK1.
                     /evidence=ECO:0000305|PubMed:20637175; propagated from
                     UniProtKB/Swiss-Prot (P27707.1)"
     Site            74
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:20637175,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27707.1)"
     Site            104
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..260
                     /gene="DCK"
                     /coded_by="NM_000788.3:188..970"
                     /db_xref="CCDS:CCDS3548.1"
                     /db_xref="GeneID:1633"
                     /db_xref="HGNC:HGNC:2704"
                     /db_xref="MIM:125450"
ORIGIN      
        1 matppkrscp sfsassegtr ikkisiegni aagkstfvni lkqlcedwev vpepvarwcn
       61 vqstqdefee ltmsqknggn vlqmmyekpe rwsftfqtya clsriraqla slngklkdae
      121 kpvlffersv ysdryifasn lyesecmnet ewtiyqdwhd wmnnqfgqsl eldgiiylqa
      181 tpetclhriy lrgrneeqgi pleyleklhy kheswllhrt lktnfdylqe vpiltldvne
      241 dfkdkyeslv ekvkeflstl
//
LOCUS       NP_620164                245 aa            linear   PRI 20-NOV-2025
DEFINITION  carboxymethylenebutenolidase homolog [Homo sapiens].
ACCESSION   NP_620164
VERSION     NP_620164.1
DBSOURCE    REFSEQ: accession NM_138809.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Huang,Y., Xiong,C., Wang,C., Deng,J., Zuo,Z., Wu,H., Xiong,J.,
            Wu,X., Lu,H., Hao,Q. and Zhou,X.
  TITLE     p53-responsive CMBL reprograms glucose metabolism and suppresses
            cancer development by destabilizing phosphofructokinase PFKP
  JOURNAL   Cell Rep 42 (11), 113426 (2023)
   PUBMED   37967006
  REMARK    GeneRIF: p53-responsive CMBL reprograms glucose metabolism and
            suppresses cancer development by destabilizing phosphofructokinase
            PFKP.
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Ishizuka,T., Yoshigae,Y., Murayama,N. and Izumi,T.
  TITLE     Different hydrolases involved in bioactivation of prodrug-type
            angiotensin receptor blockers: carboxymethylenebutenolidase and
            carboxylesterase 1
  JOURNAL   Drug Metab Dispos 41 (11), 1888-1895 (2013)
   PUBMED   23946449
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Ishizuka,T., Fujimori,I., Kato,M., Noji-Sakikawa,C., Saito,M.,
            Yoshigae,Y., Kubota,K., Kurihara,A., Izumi,T., Ikeda,T. and
            Okazaki,O.
  TITLE     Human carboxymethylenebutenolidase as a bioactivating hydrolase of
            olmesartan medoxomil in liver and intestine
  JOURNAL   J Biol Chem 285 (16), 11892-11902 (2010)
   PUBMED   20177059
  REMARK    GeneRIF: By comparing the enzyme kinetics and chemical inhibition
            properties between the recombinant protein and tissue preparations,
            CMBL was shown to be the primary olmesartan medoxomil bioactivating
            enzyme in the liver and intestine.
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Fatima,S., Chui,C.H., Tang,W.K., Hui,K.S., Au,H.W., Li,W.Y.,
            Wong,M.M., Cheung,F., Tsao,S.W., Lam,K.Y., Beh,P.S., Wong,J.,
            Law,S., Srivastava,G., Ho,K.P., Chan,A.S. and Tang,J.C.
  TITLE     Transforming capacity of two novel genes JS-1 and JS-2 located in
            chromosome 5p and their overexpression in human esophageal squamous
            cell carcinoma
  JOURNAL   Int J Mol Med 17 (1), 159-170 (2006)
   PUBMED   16328025
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Frantz,B., Ngai,K.L., Chatterjee,D.K., Ornston,L.N. and
            Chakrabarty,A.M.
  TITLE     Nucleotide sequence and expression of clcD, a plasmid-borne
            dienelactone hydrolase gene from Pseudomonas sp. strain B13
  JOURNAL   J Bacteriol 169 (2), 704-709 (1987)
   PUBMED   3804974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA628493.1, BC001573.1 and AC012640.12.
            
            Summary: CMBL (EC 3.1.1.45) is a cysteine hydrolase of the
            dienelactone hydrolase family that is highly expressed in liver
            cytosol. CMBL preferentially cleaves cyclic esters, and it
            activates medoxomil-ester prodrugs in which the medoxomil moiety is
            linked to an oxygen atom (Ishizuka et al., 2010 [PubMed
            20177059]).[supplied by OMIM, Apr 2010].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038193.4231738.1, AJ278125.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296658.4/ ENSP00000296658.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..245
                     /product="carboxymethylenebutenolidase homolog"
                     /EC_number="3.1.-.-"
                     /note="carboxymethylenebutenolidase-like (Pseudomonas);
                     carboxymethylenebutenolidase homolog (Pseudomonas)"
                     /calculated_mol_wt=27917
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5;
                     propagated from UniProtKB/Swiss-Prot (Q96DG6.1)"
     Region          30..242
                     /region_name="DLH"
                     /note="Dienelactone hydrolase [Secondary metabolites
                     biosynthesis, transport and catabolism]; COG0412"
                     /db_xref="CDD:440181"
     Site            36
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96DG6.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96DG6.1)"
     CDS             1..245
                     /gene="CMBL"
                     /gene_synonym="JS-1"
                     /coded_by="NM_138809.4:298..1035"
                     /db_xref="CCDS:CCDS3878.1"
                     /db_xref="GeneID:134147"
                     /db_xref="HGNC:HGNC:25090"
                     /db_xref="MIM:613379"
ORIGIN      
        1 maneaypcpc dighrleygg lgrevqvehi kayvtkspvd agkaviviqd ifgwqlpntr
       61 yiadmisgng yttivpdffv gqepwdpsgd wsifpewlkt rnaqkidrei sailkylkqq
      121 chaqkigivg fcwggtavhh lmmkysefra gvsvygivkd sediynlknp tlfifaendv
      181 viplkdvsll tqklkehckv eyqiktfsgq thgfvhrkre dcspadkpyi dearrnliew
      241 lnkym
//
LOCUS       NP_057572                458 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 1 [Homo sapiens].
ACCESSION   NP_057572
VERSION     NP_057572.5
DBSOURCE    REFSEQ: accession NM_016488.7
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY039238.1 and AC079601.25.
            
            On Jun 4, 2004 this sequence version replaced NP_057572.4.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY039238.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2158800, SAMN03465416
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..458
                     /product="periphilin-1 isoform 1"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=52606
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Region          63..284
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Region          103..109
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            235
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Region          285..>341
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Region          345..406
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEY8.2)"
     Region          <409..>444
                     /region_name="HERV-K_REC"
                     /note="Rec (regulator of expression encoded by corf) of
                     HERV-K-113; pfam15695"
                     /db_xref="CDD:292323"
     CDS             1..458
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_016488.7:84..1460"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31777.1"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdgynrl vnivpkkppl ldrpgegsyn ryyshvdyrd
       61 ydegrsfshd rrsgpphrgd esgyrwtrdd hsasrqpeyr dmrdgfrrks fysshyarer
      121 spykrdntff respvgrkds phsrsgssvs srsyspersk sysfhqsqhr ksvrpgasyk
      181 rqnegnperd kerpvqslkt srdtspssgs avssskvldk psrltekela eaaskwaaek
      241 leksdesnlp eiseyeagst aplftdqpee pesntthgie lfedsqlttr skaiasktke
      301 ieqvyrqdce tfgmvvkmli ekdpsleksi qfalrqnlhe iesagqtwqq vppvrntemd
      361 hdgtpenege etaqsapqpp qapqplqprk krvrrttqlr rttgapditw gmlkkttqea
      421 erillrtqtp ftpenlflam lsvvhcnsrk dvkpenkq
//
LOCUS       NP_056392                980 aa            linear   PRI 20-NOV-2025
DEFINITION  ankycorbin isoform a [Homo sapiens].
ACCESSION   NP_056392
VERSION     NP_056392.2
DBSOURCE    REFSEQ: accession NM_015577.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Jeong,W., Kwon,H., Park,S.K., Lee,I.S. and Jho,E.H.
  TITLE     Retinoic acid-induced protein 14 links mechanical forces to Hippo
            signaling
  JOURNAL   EMBO Rep 25 (9), 4033-4061 (2024)
   PUBMED   39160347
  REMARK    GeneRIF: Retinoic acid-induced protein 14 links mechanical forces
            to Hippo signaling.
REFERENCE   4  (residues 1 to 980)
  AUTHORS   Zhang,R., Hu,M., Chen,H.N., Wang,X., Xia,Z., Liu,Y., Wang,R.,
            Xia,X., Shu,Y., Du,D., Meng,W., Qi,S., Li,Y., Xu,H., Zhou,Z.G. and
            Dai,L.
  TITLE     Phenotypic Heterogeneity Analysis of APC-Mutant Colon Cancer by
            Proteomics and Phosphoproteomics Identifies RAI14 as a Key
            Prognostic Determinant in East Asians and Westerners
  JOURNAL   Mol Cell Proteomics 22 (5), 100532 (2023)
   PUBMED   36934880
  REMARK    GeneRIF: Phenotypic Heterogeneity Analysis of APC-Mutant Colon
            Cancer by Proteomics and Phosphoproteomics Identifies RAI14 as a
            Key Prognostic Determinant in East Asians and Westerners.
REFERENCE   5  (residues 1 to 980)
  AUTHORS   Arnett,D.K., Li,N., Tang,W., Rao,D.C., Devereux,R.B., Claas,S.A.,
            Kraemer,R. and Broeckel,U.
  TITLE     Genome-wide association study identifies single-nucleotide
            polymorphism in KCNB1 associated with left ventricular mass in
            humans: the HyperGEN Study
  JOURNAL   BMC Med Genet 10, 43 (2009)
   PUBMED   19454037
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 980)
  AUTHORS   Kutty,R.K., Chen,S., Samuel,W., Vijayasarathy,C., Duncan,T.,
            Tsai,J.Y., Fariss,R.N., Carper,D., Jaworski,C. and Wiggert,B.
  TITLE     Cell density-dependent nuclear/cytoplasmic localization of NORPEG
            (RAI14) protein
  JOURNAL   Biochem Biophys Res Commun 345 (4), 1333-1341 (2006)
   PUBMED   16729964
  REMARK    GeneRIF: Subcellular localization of NORPEG in retinal pigment
            epithelial (ARPE-19) cells varies with cell density, with
            predominantly nuclear localization in nonconfluent cells, but a
            cytoplasmic localization in confluent cultures.
REFERENCE   7  (residues 1 to 980)
  AUTHORS   Yuan,W., Zheng,Y., Huo,R., Lu,L., Huang,X.Y., Yin,L.L., Li,J.M.,
            Zhou,Z.M. and Sha,J.H.
  TITLE     Expression of a novel alternative transcript of the novel retinal
            pigment epithelial cell gene NORPEG in human testes
  JOURNAL   Asian J Androl 7 (3), 277-288 (2005)
   PUBMED   16110356
REFERENCE   8  (residues 1 to 980)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 980)
  AUTHORS   Kutty,R.K., Kutty,G., Samuel,W., Duncan,T., Bridges,C.C.,
            El-Sherbeeny,A., Nagineni,C.N., Smith,S.B. and Wiggert,B.
  TITLE     Molecular characterization and developmental expression of NORPEG,
            a novel gene induced by retinoic acid
  JOURNAL   J Biol Chem 276 (4), 2831-2840 (2001)
   PUBMED   11042181
REFERENCE   10 (residues 1 to 980)
  AUTHORS   Peng,Y.F., Mandai,K., Sakisaka,T., Okabe,N., Yamamoto,Y.,
            Yokoyama,S., Mizoguchi,A., Shiozaki,H., Monden,M. and Takai,Y.
  TITLE     Ankycorbin: a novel actin cytoskeleton-associated protein
  JOURNAL   Genes Cells 5 (12), 1001-1008 (2000)
   PUBMED   11168586
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA485361.1, AF155135.1 and BC028681.1.
            
            On Mar 11, 2009 this sequence version replaced NP_056392.1.
            
            Transcript Variant: This variant (1) encodes the predominant
            isoform (a). Variants 1-3 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052988.1, SRR1660809.229465.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265109.8/ ENSP00000265109.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..980
                     /product="ankycorbin isoform a"
                     /note="novel retinal pigment epithelial cell protein;
                     ankycorbin; ankyrin repeat and coiled-coil
                     structure-containing protein; retinoic acid-induced
                     protein 14"
                     /calculated_mol_wt=109911
     Region          1..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          18..51
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          23..50
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..83
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          52..81
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          85..114
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          86..116
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(118,120,124..125,128..130,132..133,137,140,149,151,
                     153,157..158,161..163,165..166,170,173,182,184,186,
                     190..191,194..196,198..199,203,206,215)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          118..149
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          118..147
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          151..182
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          151..180
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          184..215
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          184..213
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          217..247
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          247..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            249
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          270..276
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000305|PubMed:16729964"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            281
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EP71; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5U312; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            341
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          387..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Region          <430..>946
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            667
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EP71; propagated from
                     UniProtKB/Swiss-Prot (Q9P0K7.2)"
     CDS             1..980
                     /gene="RAI14"
                     /gene_synonym="NORPEG; RAI13"
                     /coded_by="NM_015577.3:197..3139"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34142.1"
                     /db_xref="GeneID:26064"
                     /db_xref="HGNC:HGNC:14873"
                     /db_xref="MIM:606586"
ORIGIN      
        1 mkslkakfrk sdtnewnknd drllqaveng daekvasllg kkgasatkhd segktafhla
       61 aakghveclr vmithgvdvt aqdttghsal hlaaknshhe cirkllqskc paesvdssgk
      121 talhyaaaqg clqavqilce hkspinlkdl dgniplllav qnghseichf lldhgadvns
      181 rnksgrtalm laceigssna vealikkgad lnlvdslgyn alhysklsen agiqslllsk
      241 isqdadlktp tkpkqhdqvs kissersgtp kkrkappppi sptqlsdvss prsitstpls
      301 gkesvffaep pfkaeissir enkdrlsdst tgadslldis seadqqdlls llqakvaslt
      361 lhnkelqdkl qakspkeaea dlsfdsyhst qtdlgpslgk pgetsppdsk sspsvlihsl
      421 gksttdndvr iqqlqeilqd lqkrlessea erkqlqvelq srraelvcln nteisenssd
      481 lsqklketqs kyeeamkevl svqkqmklgl vspesmdnys hfhelrvtee einvlkqdlq
      541 naleesernk ekvreleekl verekgtvik ppveeyeemk ssycsvienm nkekaflfek
      601 yqeaqeeimk lkdtlksqmt qeasdeaedm keamnrmide lnkqvselsq lykeaqaele
      661 dyrkrksled vtaeyihkae heklmqltnv srakaedals emksqyskvl neltqlkqlv
      721 daqkensvsi tehlqvittl rtaakemeek isnlkehlas kevevaklek qlleekaamt
      781 damvprssye klqsslesev svlasklkes vkekekvhse vvqirsevsq vkrekeniqt
      841 llkskeqevn ellqkfqqaq eelaemkrya essskleedk dkkinemske vtklkealns
      901 lsqlsystss skrqsqqlea lqqqvkqlqn qlaeckkqhq evisvyrmhl lyavqgqmde
      961 dvqkvlkqil tmcknqsqkk
//
LOCUS       NP_056276               1311 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 521 isoform 1 [Homo sapiens].
ACCESSION   NP_056276
VERSION     NP_056276.1
DBSOURCE    REFSEQ: accession NM_015461.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1311)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1311)
  AUTHORS   Scicchitano,S., Faniello,M.C. and Mesuraca,M.
  TITLE     Zinc Finger 521 Modulates the Nrf2-Notch Signaling Pathway in Human
            Ovarian Carcinoma
  JOURNAL   Int J Mol Sci 24 (19), 14755 (2023)
   PUBMED   37834202
  REMARK    GeneRIF: Zinc Finger 521 Modulates the Nrf2-Notch Signaling Pathway
            in Human Ovarian Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1311)
  AUTHORS   Scicchitano,S., Montalcini,Y., Lucchino,V., Melocchi,V.,
            Gigantino,V., Chiarella,E., Bianchi,F., Weisz,A. and Mesuraca,M.
  TITLE     Enhanced ZNF521 expression induces an aggressive phenotype in human
            ovarian carcinoma cell lines
  JOURNAL   PLoS One 17 (10), e0274785 (2022)
   PUBMED   36191006
  REMARK    GeneRIF: Enhanced ZNF521 expression induces an aggressive phenotype
            in human ovarian carcinoma cell lines.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1311)
  AUTHORS   Chiarella,E., Aloisio,A., Scicchitano,S., Todoerti,K.,
            Cosentino,E.G., Lico,D., Neri,A., Amodio,N., Bond,H.M. and
            Mesuraca,M.
  TITLE     ZNF521 Enhances MLL-AF9-Dependent Hematopoietic Stem Cell
            Transformation in Acute Myeloid Leukemias by Altering the Gene
            Expression Landscape
  JOURNAL   Int J Mol Sci 22 (19), 10814 (2021)
   PUBMED   34639154
  REMARK    GeneRIF: ZNF521 Enhances MLL-AF9-Dependent Hematopoietic Stem Cell
            Transformation in Acute Myeloid Leukemias by Altering the Gene
            Expression Landscape.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1311)
  AUTHORS   Chiarella,E., Aloisio,A., Scicchitano,S., Bond,H.M. and Mesuraca,M.
  TITLE     Regulatory Role of microRNAs Targeting the Transcription Co-Factor
            ZNF521 in Normal Tissues and Cancers
  JOURNAL   Int J Mol Sci 22 (16), 8461 (2021)
   PUBMED   34445164
  REMARK    GeneRIF: Regulatory Role of microRNAs Targeting the Transcription
            Co-Factor ZNF521 in Normal Tissues and Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1311)
  AUTHORS   Matsubara,E., Sakai,I., Yamanouchi,J., Fujiwara,H., Yakushijin,Y.,
            Hato,T., Shigemoto,K. and Yasukawa,M.
  TITLE     The role of zinc finger protein 521/early hematopoietic zinc finger
            protein in erythroid cell differentiation
  JOURNAL   J Biol Chem 284 (6), 3480-3487 (2009)
   PUBMED   19049973
  REMARK    GeneRIF: ZNF521 modulates erythroid cell differentiation through
            direct binding with GATA-1.
REFERENCE   7  (residues 1 to 1311)
  AUTHORS   Bond,H.M., Mesuraca,M., Amodio,N., Mega,T., Agosti,V., Fanello,D.,
            Pelaggi,D., Bullinger,L., Grieco,M., Moore,M.A., Venuta,S. and
            Morrone,G.
  TITLE     Early hematopoietic zinc finger protein-zinc finger protein 521: a
            candidate regulator of diverse immature cells
  JOURNAL   Int J Biochem Cell Biol 40 (5), 848-854 (2008)
   PUBMED   17543573
  REMARK    GeneRIF: A review of possible roles for ZNF521 in development, stem
            cell regulation and oncogenesis.
            Review article
REFERENCE   8  (residues 1 to 1311)
  AUTHORS   Bond,H.M., Mesuraca,M., Carbone,E., Bonelli,P., Agosti,V.,
            Amodio,N., De Rosa,G., Di Nicola,M., Gianni,A.M., Moore,M.A.,
            Hata,A., Grieco,M., Morrone,G. and Venuta,S.
  TITLE     Early hematopoietic zinc finger protein (EHZF), the human homolog
            to mouse Evi3, is highly expressed in primitive human hematopoietic
            cells
  JOURNAL   Blood 103 (6), 2062-2070 (2004)
   PUBMED   14630787
  REMARK    GeneRIF: EHZF is likely to play a relevant role in the control of
            human hematopoiesis and might be implicated in the development of
            hematopoietic malignancies.
REFERENCE   9  (residues 1 to 1311)
  AUTHORS   Warming,S., Liu,P., Suzuki,T., Akagi,K., Lindtner,S.,
            Pavlakis,G.N., Jenkins,N.A. and Copeland,N.G.
  TITLE     Evi3, a common retroviral integration site in murine B-cell
            lymphoma, encodes an EBFAZ-related Kruppel-like zinc finger protein
  JOURNAL   Blood 101 (5), 1934-1940 (2003)
   PUBMED   12393497
REFERENCE   10 (residues 1 to 1311)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA102816.1, AK027354.1, BC113622.1 and AF141339.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.215351.1,
                                           SRR1660805.199349.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361524.8/ ENSP00000354794.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..1311
                     /product="zinc finger protein 521 isoform 1"
                     /note="LYST-interacting protein 3; early hematopoietic
                     zinc finger protein"
                     /calculated_mol_wt=147736
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Site            72..73
                     /site_type="other"
                     /note="Breakpoint for translocation to form PAX5-ZNF521;
                     propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          81..108
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          120..140
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(125,127,129,131..132,135..136,139,153,155,159..160,
                     163..164,167,181,183,185,187..188,191..192,195)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          128..>216
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          148..168
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          162..185
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          176..196
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          204..224
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          248..265
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          349..397
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          407..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(412,415,417,419..420,423..424,427,444,446,450..451,
                     454..455,459,484,486,488,490..491,494..495,498)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          439..460
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          479..498
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96K83.1)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96K83.1)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          636..656
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(641,643,645,647..648,651..652,655,671,673,677..678,
                     681..682,685,701,703,705,707..708,711..712)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          666..686
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          696..713
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          724..745
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(729,731,733,735..736,739..740,743,759,761,765..766,
                     769..770,773,790,792,794,796..797,800..801,804)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          754..774
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          785..805
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          811..829
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          863..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          888..909
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          932..952
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          961..981
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1168..1188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96K83.1)"
     Region          1227..1247
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1232,1234,1236,1238..1239,1242..1243,1246,1263,1265,
                     1269..1270,1273..1274,1278,1293,1295,1297,1299..1300,
                     1303..1304,1307)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1258..1279
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1288..1307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1311
                     /gene="ZNF521"
                     /gene_synonym="EHZF; Evi3"
                     /coded_by="NM_015461.3:164..4099"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32806.1"
                     /db_xref="GeneID:25925"
                     /db_xref="HGNC:HGNC:24605"
                     /db_xref="MIM:610974"
ORIGIN      
        1 msrrkqakpr slkdpnckle dktedgeald ckkrpedgee ledeavhscd sclqvfesls
       61 ditehkinqc qltdgvdved dptcswpass psskdqtsps hgegcdfgee eggpglpypc
      121 qfcdksfsrl sylkhheqsh sdklpfkcty csrlfkhkrs rdrhiklhtg dkkyhcsecd
      181 aafsrsdhlk ihlkthtsnk pykcaicrrg flsssslhgh mqvhernkdg sqsgsrmedw
      241 kmkdtqkcsq ceegfdfped lqkhiaechp ecspnedraa lqcvychelf veetslmnhm
      301 eqvhsgekkn scsicsesfh tveelyshmd shqqpescnh snspslvtvg ytsvssttpd
      361 snlsvdsstm veaappipks rgrkraaqqt pdmtgpsskq akvtysciyc nkqlfsslav
      421 lqihlktmhl dkpeqahicq yclevlpsly nlnehlkqvh eaqdpglivs ampaivyqcn
      481 fcsevvndln tlqehircsh gfanpaakds naffcphcym gfltdsslee hirqvhcdls
      541 gsrfgspvlg tpkepvvevy scsyctnspi fnsvlklnkh ikenhknipl alnyihngkk
      601 sralsplspv aieqtslkmm qavggaparp tgeyicnqcg akytsldsfq thlkthldtv
      661 lpkltcpqcn kefpnqesll khvtihfmit styyicescd kqftsvddlq khlldmhtfv
      721 ffrctlcqev fdskvsiqlh lavkhsnekk vyrctscnwd frnetdlqlh vkhnhlenqg
      781 kvhkcifcge sfgtevelqc hitthskkyn ckfcskafha iillekhlre khcvfetktp
      841 ncgtngaseq vqkeevelqt lltnsqeshn shdgseedvd tsepmygcdi cgaaytmetl
      901 lqnhqlrdhn irpgesaivk kkaelikgny kcnvcsrtff senglrehmq thlgpvkhym
      961 cpicgerfps lltltehkvt hsksldtgnc rickmplqse eeflehcqmh pdlrnsltgf
     1021 rcvvcmqtvt stlelkihgt fhmqktgngs avqttgrgqh vqklykcasc lkefrskqdl
     1081 vkldinglpy glcagcvnls ksaspginvp pgtnrpglgq nenlsaiegk gkvgglktrc
     1141 sscnvkfese selqnhiqti hrelvpdsns tqlktpqvsp mprispsqsd ekktyqcikc
     1201 qmvfynewdi qvhvanhmid eglnhecklc sqtfdspakl qchliehsfe gmggtfkcpv
     1261 cftvfvqank lqqhifsahg qedkiydctq cpqkfffqte lqnhtmtqhs s
//
LOCUS       NP_036304                618 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 24 isoform 3 [Homo sapiens].
ACCESSION   NP_036304
VERSION     NP_036304.2
DBSOURCE    REFSEQ: accession NM_012172.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Zhang,Z., Liu,X., Chu,C., Zhang,Y., Li,W., Yu,X., Han,Q., Sun,H.,
            Zhang,Y., Zhu,X., Chen,L., Wei,R., Fan,N., Zhou,M. and Li,X.
  TITLE     MIR937 amplification potentiates ovarian cancer progression by
            attenuating FBXO16 inhibition on ULK1-mediated autophagy
  JOURNAL   Cell Death Dis 15 (10), 735 (2024)
   PUBMED   39384743
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 618)
  AUTHORS   El-Mergawy,R., Chafin,L., Ovando-Ricardez,J.A., Rosas,L., Tsai,M.,
            Rojas,M., Mora,A.L. and Mallampalli,R.K.
  TITLE     FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for ubiquitin
            mediated degradation modulates mitochondrial respiration
  JOURNAL   J Biol Chem 300 (6), 107359 (2024)
   PUBMED   38735474
  REMARK    GeneRIF: FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for
            ubiquitin mediated degradation modulates mitochondrial respiration.
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Li,Z., Liu,X., Zhang,Y., Li,Y., Zhou,L. and Yuan,S.
  TITLE     FBXO24 modulates mRNA alternative splicing and MIWI degradation and
            is required for normal sperm formation and male fertility
  JOURNAL   Elife 12, 91666 (2024)
   PUBMED   38470475
  REMARK    GeneRIF: FBXO24 modulates mRNA alternative splicing and MIWI
            degradation and is required for normal sperm formation and male
            fertility.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Dong,B., Song,X., Wang,X., Dai,T., Wang,J., Yu,Z., Deng,J.,
            Evers,B.M. and Wu,Y.
  TITLE     FBXO24 Suppresses Breast Cancer Tumorigenesis by Targeting LSD1 for
            Ubiquitination
  JOURNAL   Mol Cancer Res 21 (12), 1303-1316 (2023)
   PUBMED   37540490
  REMARK    GeneRIF: FBXO24 Suppresses Breast Cancer Tumorigenesis by Targeting
            LSD1 for Ubiquitination.
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 618)
  AUTHORS   Chen,W., Xiong,S., Li,J., Li,X., Liu,Y., Zou,C. and
            Mallampalli,R.K.
  TITLE     The ubiquitin E3 ligase SCF-FBXO24 recognizes deacetylated
            nucleoside diphosphate kinase A to enhance its degradation
  JOURNAL   Mol Cell Biol 35 (6), 1001-1013 (2015)
   PUBMED   25582197
REFERENCE   7  (residues 1 to 618)
  AUTHORS   Taipale,M., Tucker,G., Peng,J., Krykbaeva,I., Lin,Z.Y., Larsen,B.,
            Choi,H., Berger,B., Gingras,A.C. and Lindquist,S.
  TITLE     A quantitative chaperone interaction network reveals the
            architecture of cellular protein homeostasis pathways
  JOURNAL   Cell 158 (2), 434-448 (2014)
   PUBMED   25036637
REFERENCE   8  (residues 1 to 618)
  AUTHORS   Taipale,M., Krykbaeva,I., Koeva,M., Kayatekin,C., Westover,K.D.,
            Karras,G.I. and Lindquist,S.
  TITLE     Quantitative analysis of HSP90-client interactions reveals
            principles of substrate recognition
  JOURNAL   Cell 150 (5), 987-1001 (2012)
   PUBMED   22939624
REFERENCE   9  (residues 1 to 618)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 618)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC397982.1, AK301864.1 and
            BC067293.1.
            
            On Jul 22, 2009 this sequence version replaced NP_036304.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2009].
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter, 5' UTR, and 5' coding region, compared to variant 1. The
            resulting isoform (3) has a longer and distinct N-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..618
                     /product="F-box only protein 24 isoform 3"
                     /note="F-box protein Fbx24; F-box only protein 24"
                     /calculated_mol_wt=69205
     Region          76..122
                     /region_name="F-box_FBXO24"
                     /note="F-box domain found in F-box only protein 24
                     (FBXO24) and similar proteins; cd22098"
                     /db_xref="CDD:438870"
     Site            order(80,84,87..88,91..92,96,98..99,103..105,107)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438870"
     Region          <401..>463
                     /region_name="ATS1"
                     /note="Alpha-tubulin suppressor ATS1 and related RCC1
                     domain-containing proteins [Cell cycle control, cell
                     division, chromosome partitioning, Cytoskeleton]; COG5184"
                     /db_xref="CDD:444065"
     CDS             1..618
                     /gene="FBXO24"
                     /gene_synonym="FBX24"
                     /coded_by="NM_012172.5:29..1885"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5699.2"
                     /db_xref="GeneID:26261"
                     /db_xref="HGNC:HGNC:13595"
                     /db_xref="MIM:609097"
ORIGIN      
        1 mvwesqqerg gqgprrqegr sregairmvr gsqrrklqkf trlcgreegl rvkrscpscg
       61 selgveekrg kgnpisiqlf ppelvehiis flpvrdlval gqtcryfhev cdgegvwrri
      121 crrlsprlqd qgsgvrpwkr aailnytkgl yfqafggrrr clsksvapll ahgyrrflpt
      181 kdhvfildyv gtlfflknal vstlgqmqwk racryvvlcr gakdfasdpr cdtvyrkyly
      241 vlatrepqev vgttssracd cvevylqssg qrvfkmtfhh smtfkqivlv gqetqralll
      301 lteegkiysl vvnetqldqp rsytvqlalr kvshylphlr vacmtsnqss tlyvtdqggv
      361 yfevhtpgvy rdlfgtlqaf dpldqqmpla lslpakilfc algynhlglv defgrifmqg
      421 nnrygqlgtg dkmdrgeptq vcylqrpitl wcglnhslvl sqssefskel lgcgcgaggr
      481 lpgwpkgsas fvklqvkvpl cacalcatre clyilsshdi eqhapyrhlp asrvvgtpep
      541 slgarapqdp ggmaqaceey lsqihscqtl qdrtekmkei vgwmplmaaq kdffwealdm
      601 lqraeggggg vgppapet
//
LOCUS       NP_060612                710 aa            linear   PRI 20-NOV-2025
DEFINITION  integrator complex subunit 10 isoform g [Homo sapiens].
ACCESSION   NP_060612
VERSION     NP_060612.2
DBSOURCE    REFSEQ: accession NM_018142.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Lin,M.H., Jensen,M.K., Elrod,N.D., Chu,H.F., Haseley,M., Beam,A.C.,
            Huang,K.L., Chiang,W., Russell,W.K., Williams,K., Proschel,C.,
            Wagner,E.J. and Tong,L.
  TITLE     Cytoplasmic binding partners of the Integrator endonuclease INTS11
            and its paralog CPSF73 are required for their nuclear function
  JOURNAL   Mol Cell 84 (15), 2900-2917 (2024)
   PUBMED   39032490
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Razew,M., Fraudeau,A., Pfleiderer,M.M., Linares,R. and Galej,W.P.
  TITLE     Structural basis of the Integrator complex assembly and association
            with transcription factors
  JOURNAL   Mol Cell 84 (13), 2542-2552 (2024)
   PUBMED   38823386
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Fianu,I., Ochmann,M., Walshe,J.L., Dybkov,O., Cruz,J.N., Urlaub,H.
            and Cramer,P.
  TITLE     Structural basis of Integrator-dependent RNA polymerase II
            termination
  JOURNAL   Nature 629 (8010), 219-227 (2024)
   PUBMED   38570683
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Offley,S.R., Pfleiderer,M.M., Zucco,A., Fraudeau,A., Welsh,S.A.,
            Razew,M., Galej,W.P. and Gardini,A.
  TITLE     A combinatorial approach to uncover an additional Integrator
            subunit
  JOURNAL   Cell Rep 42 (3), 112244 (2023)
   PUBMED   36920904
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Wu,Y., Lin,Z., Luo,M., Yu,X., Chen,S. and Liu,L.
  TITLE     Effects of genetic polymorphisms in INTS10 and their interaction
            with environmental factors on progression from persistent HBV
            infection to hepatocellular carcinoma
  JOURNAL   Mol Carcinog 60 (9), 620-626 (2021)
   PUBMED   34133796
  REMARK    GeneRIF: Effects of genetic polymorphisms in INTS10 and their
            interaction with environmental factors on progression from
            persistent HBV infection to hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Ellinghaus,E., Stanulla,M., Richter,G., Ellinghaus,D., te
            Kronnie,G., Cario,G., Cazzaniga,G., Horstmann,M., Panzer
            Grumayer,R., Cave,H., Trka,J., Cinek,O., Teigler-Schlegel,A.,
            ElSharawy,A., Hasler,R., Nebel,A., Meissner,B., Bartram,T.,
            Lescai,F., Franceschi,C., Giordan,M., Nurnberg,P., Heinzow,B.,
            Zimmermann,M., Schreiber,S., Schrappe,M. and Franke,A.
  TITLE     Identification of germline susceptibility loci in
            ETV6-RUNX1-rearranged childhood acute lymphoblastic leukemia
  JOURNAL   Leukemia 26 (5), 902-909 (2012)
   PUBMED   22076464
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Kooner,J.S., Chambers,J.C., Aguilar-Salinas,C.A., Hinds,D.A.,
            Hyde,C.L., Warnes,G.R., Gomez Perez,F.J., Frazer,K.A., Elliott,P.,
            Scott,J., Milos,P.M., Cox,D.R. and Thompson,J.F.
  TITLE     Genome-wide scan identifies variation in MLXIPL associated with
            plasma triglycerides
  JOURNAL   Nat Genet 40 (2), 149-151 (2008)
   PUBMED   18193046
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Baillat,D., Hakimi,M.A., Naar,A.M., Shilatifard,A., Cooch,N. and
            Shiekhattar,R.
  TITLE     Integrator, a multiprotein mediator of small nuclear RNA
            processing, associates with the C-terminal repeat of RNA polymerase
            II
  JOURNAL   Cell 123 (2), 265-276 (2005)
   PUBMED   16239144
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Yuryev,A. and Wennogle,L.P.
  TITLE     Novel raf kinase protein-protein interactions found by an
            exhaustive yeast two-hybrid analysis
  JOURNAL   Genomics 81 (2), 112-125 (2003)
   PUBMED   12620389
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC107964.4.
            
            On Dec 13, 2005 this sequence version replaced NP_060612.1.
            
            Summary: INTS10 is a subunit of the Integrator complex, which
            associates with the C-terminal domain of RNA polymerase II large
            subunit (POLR2A; MIM 180660) and mediates 3-prime end processing of
            small nuclear RNAs U1 (RNU1; MIM 180680) and U2 (RNU2; MIM 180690)
            (Baillat et al., 2005 [PubMed 16239144]).[supplied by OMIM, Mar
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.285292.1,
                                           SRR1660807.148622.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397977.8/ ENSP00000381064.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..710
                     /product="integrator complex subunit 10 isoform g"
                     /calculated_mol_wt=82105
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVR2.2)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2A7; propagated from
                     UniProtKB/Swiss-Prot (Q9NVR2.2)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2A7; propagated from
                     UniProtKB/Swiss-Prot (Q9NVR2.2)"
     CDS             1..710
                     /gene="INTS10"
                     /gene_synonym="C8orf35; INT10"
                     /coded_by="NM_018142.4:123..2255"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS6011.2"
                     /db_xref="GeneID:55174"
                     /db_xref="HGNC:HGNC:25548"
                     /db_xref="MIM:611353"
ORIGIN      
        1 msaqgdcefl vqrarelvpq dlwaakawli tarslypadf niqyemytie rnaertatag
       61 rllydmfvnf pdqpvvwrei siitsalrnd sqdkqtqflr slfetlpgrv qcemllkvte
      121 qcfntlerse mlllllrrfp etvvqhgvgl gealleaeti eeqespvncf rklfvcdvlp
      181 liinnhdvrl panllykyln kaaefyinyv trstqienqh qgaqdtsdlm spskrssqky
      241 iiegltekss qivdpwerlf kilnvvgmrc ewqmdkgrrs ygdilhrmkd lcrymnnfds
      301 eahakyknqv vystmlvffk nafqyvnsiq pslfqgpnap sqvplvlled vsnvygdvei
      361 drnkhihkkr klaegrektm ssddedcsak grnrhivvnk aelanstevl esfklaresw
      421 ellyslefld keftriclaw ktdtwlwlri fltdmiiyqg qykkaiaslh hlaalqgsis
      481 qpqitgqgtl ehqraliqla tchfalgeyr mtcekvldlm cymvlpiqdg gksqeepskv
      541 kpkfrkgsdl kllpctskai mpyclhlmla cfklraftdn rddmalghvi vllqqewprg
      601 enlflkavnk icqqgnfqye nffnyvtnid mleefaylrt qeggkihlel lpnqgmlikh
      661 htvtrgitkg vkedfrlame rqvsrcgenl mvvlhrfcin ekilllqtlt
//
LOCUS       NP_001315581             404 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3-kinase regulatory subunit gamma isoform 6
            [Homo sapiens].
ACCESSION   NP_001315581
VERSION     NP_001315581.1
DBSOURCE    REFSEQ: accession NM_001328652.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Qian,W., Mei,K., Zhu,L., Chu,Y., Lv,J. and Yun,C.
  TITLE     Circ_0044235 regulates the development of osteoarthritis by the
            modulation of miR-375/PIK3R3 axis
  JOURNAL   J Orthop Surg Res 19 (1), 241 (2024)
   PUBMED   38622668
  REMARK    GeneRIF: Circ_0044235 regulates the development of osteoarthritis
            by the modulation of miR-375/PIK3R3 axis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Lee,H., Zhuang,L. and Gan,B.
  TITLE     VHL governs m6A modification and PIK3R3 mRNA stability in clear
            cell renal cell carcinomas
  JOURNAL   J Clin Invest 134 (8), e179560 (2024)
   PUBMED   38618953
  REMARK    GeneRIF: VHL governs m6A modification and PIK3R3 mRNA stability in
            clear cell renal cell carcinomas.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Li,Z., Dai,R., Chen,M., Huang,L., Zhu,K., Li,M., Zhu,W., Li,Y.,
            Xie,N., Li,J., Wang,L., Lan,F. and Cao,C.M.
  TITLE     p55gamma degrades RIP3 via MG53 to suppress ischaemia-induced
            myocardial necroptosis and mediates cardioprotection of
            preconditioning
  JOURNAL   Cardiovasc Res 119 (14), 2421-2440 (2023)
   PUBMED   37527538
  REMARK    GeneRIF: p55gamma degrades RIP3 via MG53 to suppress
            ischaemia-induced myocardial necroptosis and mediates
            cardioprotection of preconditioning.
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Lin,W., Wang,K., Mo,J., Wang,L., Song,Z., Jiang,H., Wang,C. and
            Jin,C.
  TITLE     PIK3R3 is upregulated in liver cancer and activates Akt signaling
            to control cancer growth by regulation of CDKN1C and SMC1A
  JOURNAL   Cancer Med 12 (13), 14413-14425 (2023)
   PUBMED   37212524
  REMARK    GeneRIF: PIK3R3 is upregulated in liver cancer and activates Akt
            signaling to control cancer growth by regulation of CDKN1C and
            SMC1A.
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Dey,B.R., Furlanetto,R.W. and Nissley,S.P.
  TITLE     Cloning of human p55 gamma, a regulatory subunit of
            phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen
            with the insulin-like growth factor-I receptor
  JOURNAL   Gene 209 (1-2), 175-183 (1998)
   PUBMED   9524259
  REMARK    Erratum:[Gene 1998 May 28;212(1):155]
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Mothe,I., Delahaye,L., Filloux,C., Pons,S., White,M.F. and Van
            Obberghen,E.
  TITLE     Interaction of wild type and dominant-negative p55PIK regulatory
            subunit of phosphatidylinositol 3-kinase with insulin-like growth
            factor-1 signaling proteins
  JOURNAL   Mol Endocrinol 11 (13), 1911-1923 (1997)
   PUBMED   9415396
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Takahashi-Tezuka,M., Hibi,M., Fujitani,Y., Fukada,T., Yamaguchi,T.
            and Hirano,T.
  TITLE     Tec tyrosine kinase links the cytokine receptors to PI-3 kinase
            probably through JAK
  JOURNAL   Oncogene 14 (19), 2273-2282 (1997)
   PUBMED   9178903
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Tuscano,J.M., Engel,P., Tedder,T.F., Agarwal,A. and Kehrl,J.H.
  TITLE     Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl
            inositol-3 kinase in signal transduction via the human B lymphocyte
            antigen CD22
  JOURNAL   Eur J Immunol 26 (6), 1246-1252 (1996)
   PUBMED   8647200
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Pons,S., Asano,T., Glasheen,E., Miralpeix,M., Zhang,Y.,
            Fisher,T.L., Myers,M.G. Jr., Sun,X.J. and White,M.F.
  TITLE     The structure and function of p55PIK reveal a new regulatory
            subunit for phosphatidylinositol 3-kinase
  JOURNAL   Mol Cell Biol 15 (8), 4453-4465 (1995)
   PUBMED   7542745
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL358075.10.
            
            Summary: Phosphatidylinositol 3-kinase (PI3K) phosphorylates
            phosphatidylinositol and similar compounds, which then serve as
            second messengers in growth signaling pathways. PI3K is composed of
            a catalytic and a regulatory subunit. The protein encoded by this
            gene represents a regulatory subunit of PI3K. The encoded protein
            contains two SH2 domains through which it binds activated protein
            tyrosine kinases to regulate their activity. [provided by RefSeq,
            Jun 2016].
            
            Transcript Variant: This variant (10) lacks an alternate in-frame
            exon in the 3' end compared to variant 1. The resulting isoform (6)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.102047.1,
                                           SRR14038192.31192.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..404
                     /product="phosphatidylinositol 3-kinase regulatory subunit
                     gamma isoform 6"
                     /note="phosphatidylinositol 3-kinase, regulatory subunit,
                     polypeptide 3 (p55, gamma); PI3-kinase subunit p55-gamma;
                     PI3K regulatory subunit gamma; PI3-kinase regulatory
                     subunit gamma; ptdIns-3-kinase regulatory subunit
                     p55-gamma; phosphatidylinositol 3-kinase 55 kDa regulatory
                     subunit gamma; phosphoinositide-3-kinase, regulatory
                     subunit 3 (gamma)"
                     /calculated_mol_wt=47675
     Region          59..167
                     /region_name="SH2_nSH2_p85_like"
                     /note="N-terminal Src homology 2 (nSH2) domain found in
                     p85; cd09942"
                     /db_xref="CDD:198195"
     Site            order(72,90,112,114)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198195"
     Site            order(113,140)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198195"
     Region          172..332
                     /region_name="iSH2_PI3K_IA_R"
                     /note="Inter-Src homology 2 (iSH2) helical domain of Class
                     IA Phosphoinositide 3-kinase Regulatory subunits; cl25402"
                     /db_xref="CDD:355389"
     Site            order(195,202,213..215,217..219,221..222,225..226,
                     228..229,232..233,236,252,255..256,259,263,266,292..293,
                     296,299)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:214016"
     Region          <340..397
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(347,374)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198184"
     CDS             1..404
                     /gene="PIK3R3"
                     /gene_synonym="p55; p55-GAMMA; p55PIK"
                     /coded_by="NM_001328652.2:678..1892"
                     /note="isoform 6 is encoded by transcript variant 10"
                     /db_xref="GeneID:8503"
                     /db_xref="HGNC:HGNC:8981"
                     /db_xref="MIM:606076"
ORIGIN      
        1 myntvwsmdr ddadwrevmm pystelifyi emdppalppk ppkpmtsavp ngmkdssvsl
       61 qdaewywgdi sreevndklr dmpdgtflvr dastkmqgdy tltlrkggnn klikiyhrdg
      121 kygfsdpltf nsvvelinhy hheslaqynp kldvklmypv sryqqdqlvk ednidavgkk
      181 lqeyhsqyqe kskeydrlye eytrtsqeiq mkrtaieafn etikifeeqc htqeqhskey
      241 ierfrregne keierimmny dklksrlgei hdskmrleqd lknqaldnre idkkmnsikp
      301 dliqlrkird qhlvwlnhkg vrqkrlnvwl giknedadea dgevkhcviy stargygfae
      361 pynlysslke lvlhyqqtsl vqhndslnvr laypvhaqmp slcr
//
LOCUS       NP_002094                737 aa            linear   PRI 20-NOV-2025
DEFINITION  glycogen [starch] synthase, muscle isoform 1 [Homo sapiens].
ACCESSION   NP_002094
VERSION     NP_002094.2
DBSOURCE    REFSEQ: accession NM_002103.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 737)
  AUTHORS   Fastman,N.M., Liu,Y., Ramanan,V., Merritt,H., Ambing,E.,
            DePaoli-Roach,A.A., Roach,P.J., Hurley,T.D., Mellem,K.T.,
            Ullman,J.C., Green,E., Morgans,D. Jr. and Tzitzilonis,C.
  TITLE     The structural mechanism of human glycogen synthesis by the
            GYS1-GYG1 complex
  JOURNAL   Cell Rep 40 (1), 111041 (2022)
   PUBMED   35793618
  REMARK    GeneRIF: The structural mechanism of human glycogen synthesis by
            the GYS1-GYG1 complex.
REFERENCE   2  (residues 1 to 737)
  AUTHORS   McCorvie,T.J., Loria,P.M., Tu,M., Han,S., Shrestha,L., Froese,D.S.,
            Ferreira,I.M., Berg,A.P. and Yue,W.W.
  TITLE     Molecular basis for the regulation of human glycogen synthase by
            phosphorylation and glucose-6-phosphate
  JOURNAL   Nat Struct Mol Biol 29 (7), 628-638 (2022)
   PUBMED   35835870
REFERENCE   3  (residues 1 to 737)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 737)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 737)
  AUTHORS   Testoni,G., Olmeda,B., Duran,J., Lopez-Rodriguez,E., Aguilera,M.,
            Hernandez-Alvarez,M.I., Prats,N., Perez-Gil,J. and Guinovart,J.J.
  TITLE     Pulmonary glycogen deficiency as a new potential cause of
            respiratory distress syndrome
  JOURNAL   Hum Mol Genet 29 (21), 3554-3565 (2021)
   PUBMED   33219378
  REMARK    GeneRIF: Pulmonary glycogen deficiency as a new potential cause of
            respiratory distress syndrome.
REFERENCE   6  (residues 1 to 737)
  AUTHORS   Orho,M., Nikula-Ijas,P., Schalin-Jantti,C., Permutt,M.A. and
            Groop,L.C.
  TITLE     Isolation and characterization of the human muscle glycogen
            synthase gene
  JOURNAL   Diabetes 44 (9), 1099-1105 (1995)
   PUBMED   7657035
REFERENCE   7  (residues 1 to 737)
  AUTHORS   Lofman,M., Yki-Jarvinen,H., Parkkonen,M., Lindstrom,J., Koranyi,L.,
            Schalin-Jantti,C. and Groop,L.
  TITLE     Increased concentrations of glycogen synthase protein in skeletal
            muscle of patients with NIDDM
  JOURNAL   Am J Physiol 269 (1 Pt 1), E27-E32 (1995)
   PUBMED   7631777
REFERENCE   8  (residues 1 to 737)
  AUTHORS   Flotow,H., Graves,P.R., Wang,A.Q., Fiol,C.J., Roeske,R.W. and
            Roach,P.J.
  TITLE     Phosphate groups as substrate determinants for casein kinase I
            action
  JOURNAL   J Biol Chem 265 (24), 14264-14269 (1990)
   PUBMED   2117608
REFERENCE   9  (residues 1 to 737)
  AUTHORS   Browner,M.F., Nakano,K., Bang,A.G. and Fletterick,R.J.
  TITLE     Human muscle glycogen synthase cDNA sequence: a negatively charged
            protein with an asymmetric charge distribution
  JOURNAL   Proc Natl Acad Sci U S A 86 (5), 1443-1447 (1989)
   PUBMED   2493642
REFERENCE   10 (residues 1 to 737)
  AUTHORS   Rylatt,D.B., Aitken,A., Bilham,T., Condon,G.D., Embi,N. and
            Cohen,P.
  TITLE     Glycogen synthase from rabbit skeletal muscle. Amino acid sequence
            at the sites phosphorylated by glycogen synthase kinase-3, and
            extension of the N-terminal sequence containing the site
            phosphorylated by phosphorylase kinase
  JOURNAL   Eur J Biochem 107 (2), 529-537 (1980)
   PUBMED   6772446
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP313940.1 and BC002617.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2003 this sequence version replaced NP_002094.1.
            
            Summary: The protein encoded by this gene catalyzes the addition of
            glucose monomers to the growing glycogen molecule through the
            formation of alpha-1,4-glycoside linkages. Mutations in this gene
            are associated with muscle glycogen storage disease. Alternatively
            spliced transcript variants encoding different isoforms have been
            found for this gene.[provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.34801.1,
                                           SRR1660803.122420.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323798.8/ ENSP00000317904.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..737
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..737
                     /product="glycogen [starch] synthase, muscle isoform 1"
                     /EC_number="2.4.1.11"
                     /note="glycogen [starch] synthase, muscle; glycogen
                     synthase 1 (muscle)"
                     /calculated_mol_wt=83655
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK and PKA.
                     /evidence=ECO:0000269|PubMed:35690592; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Region          31..663
                     /region_name="Glycogen_syn"
                     /note="Glycogen synthase; pfam05693"
                     /db_xref="CDD:399009"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P13807.2)"
     Region          634..737
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P13807.2)"
     Site            641
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            653
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by GSK3-alpha and GSK3-beta.
                     /evidence=ECO:0000269|PubMed:35690592; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:35690592; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P13834; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            721
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1E4; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P13807.2)"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:35690592; propagated from
                     UniProtKB/Swiss-Prot (P13807.2)"
     CDS             1..737
                     /gene="GYS1"
                     /gene_synonym="GSY; GYS"
                     /coded_by="NM_002103.5:198..2411"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12747.1"
                     /db_xref="GeneID:2997"
                     /db_xref="HGNC:HGNC:4706"
                     /db_xref="MIM:138570"
ORIGIN      
        1 mplnrtlsms slpgledwed efdlenavlf evawevankv ggiytvlqtk akvtgdewgd
       61 nyflvgpyte qgvrtqvell eaptpalkrt ldsmnskgck vyfgrwlieg gplvvlldvg
      121 asawalerwk gelwdtcnig vpwydreand avlfgflttw flgeflaqse ekphvvahfh
      181 ewlagvglcl crarrlpvat iftthatllg rylcagavdf ynnlenfnvd keagerqiyh
      241 rycmeraaah cahvfttvsq itaieaqhll krkpdivtpn glnvkkfsam hefqnlhaqs
      301 kariqefvrg hfyghldfnl dktlyffiag ryefsnkgad vflealarln yllrvngseq
      361 tvvaffimpa rtnnfnvetl kgqavrkqlw dtantvkekf grklyesllv gslpdmnkml
      421 dkedftmmkr aifatqrqsf ppvcthnmld dssdpiltti rriglfnssa drvkvifhpe
      481 flsstspllp vdyeefvrgc hlgvfpsyye pwgytpaect vmgipsistn lsgfgcfmee
      541 hiadpsaygi yildrrfrsl ddscsqltsf lysfcqqsrr qriiqrnrte rlsdlldwky
      601 lgryymsarh malskafpeh ftyepneada aqgyryprpa svppspslsr hssphqsede
      661 edprngplee dgerydedee aakdrrnira pewprrasct sstsgskrns vdtatsssls
      721 tpseplspts slgeern
//
LOCUS       NP_001243465             385 aa            linear   PRI 20-NOV-2025
DEFINITION  protein arginine N-methyltransferase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001243465
VERSION     NP_001243465.1
DBSOURCE    REFSEQ: accession NM_001256536.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Jeong,H.C., Park,S.J., Choi,J.J., Go,Y.H., Hong,S.K., Kwon,O.S.,
            Shin,J.G., Kim,R.K., Lee,M.O., Lee,S.J., Shin,H.D., Moon,S.H. and
            Cha,H.J.
  TITLE     PRMT8 Controls the Pluripotency and Mesodermal Fate of Human
            Embryonic Stem Cells By Enhancing the PI3K/AKT/SOX2 Axis
  JOURNAL   Stem Cells 35 (9), 2037-2049 (2017)
   PUBMED   28543863
  REMARK    GeneRIF: PRMT8 in human embryonic stem cells plays an important
            role not only in maintaining pluripotency but also in controlling
            mesodermal differentiation.
REFERENCE   6  (residues 1 to 385)
  AUTHORS   Weimann,M., Grossmann,A., Woodsmith,J., Ozkan,Z., Birth,P.,
            Meierhofer,D., Benlasfer,N., Valovka,T., Timmermann,B.,
            Wanker,E.E., Sauer,S. and Stelzl,U.
  TITLE     A Y2H-seq approach defines the human protein methyltransferase
            interactome
  JOURNAL   Nat Methods 10 (4), 339-342 (2013)
   PUBMED   23455924
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Kim,J.D., Kako,K., Kakiuchi,M., Park,G.G. and Fukamizu,A.
  TITLE     EWS is a substrate of type I protein arginine methyltransferase,
            PRMT8
  JOURNAL   Int J Mol Med 22 (3), 309-315 (2008)
   PUBMED   18698489
  REMARK    GeneRIF: EWS is a substrate for PRMT8, as efficient as for PRMT1
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Pahlich,S., Zakaryan,R.P. and Gehring,H.
  TITLE     Identification of proteins interacting with protein arginine
            methyltransferase 8: the Ewing sarcoma (EWS) protein binds
            independent of its methylation state
  JOURNAL   Proteins 72 (4), 1125-1137 (2008)
   PUBMED   18320585
  REMARK    GeneRIF: The interaction between PRMT8 and the EWS protein was
            charcterized.
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Sayegh,J., Webb,K., Cheng,D., Bedford,M.T. and Clarke,S.G.
  TITLE     Regulation of protein arginine methyltransferase 8 (PRMT8) activity
            by its N-terminal domain
  JOURNAL   J Biol Chem 282 (50), 36444-36453 (2007)
   PUBMED   17925405
  REMARK    GeneRIF: PRMT8 N-terminal domain may function as an autoregulator
            that may be displaced by interaction with one or more physiological
            inducers.
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Lee,J., Sayegh,J., Daniel,J., Clarke,S. and Bedford,M.T.
  TITLE     PRMT8, a new membrane-bound tissue-specific member of the protein
            arginine methyltransferase family
  JOURNAL   J Biol Chem 280 (38), 32890-32896 (2005)
   PUBMED   16051612
  REMARK    GeneRIF: PRMT8 is an active arginine methyltransferase that is
            membrane-associated and tissue-specific
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315619.1 and AC005831.1.
            
            Summary: Arginine methylation is a widespread posttranslational
            modification mediated by arginine methyltransferases, such as
            PRMT8. Arginine methylation is involved in a number of cellular
            processes, including DNA repair, RNA transcription, signal
            transduction, protein compartmentalization, and possibly protein
            translation (Lee et al., 2005 [PubMed 16051612]).[supplied by OMIM,
            Mar 2008].
            
            Transcript Variant: This variant (2) uses an alternate 5' exon and
            it thus differs in the 5' UTR and 5' coding region, compared to
            variant 1. The resulting isoform (2) has a distinct N-terminus and
            is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315619.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.32"
     Protein         1..385
                     /product="protein arginine N-methyltransferase 8 isoform
                     2"
                     /EC_number="2.1.1.319"
                     /note="protein arginine N-methyltransferase 4;
                     heterogeneous nuclear ribonucleoprotein
                     methyltransferase-like protein 4; HMT1 hnRNP
                     methyltransferase-like 3; arginine methyltransferase 8"
                     /calculated_mol_wt=44038
     Region          77..>250
                     /region_name="COG4076"
                     /note="Predicted RNA methylase [General function
                     prediction only]"
                     /db_xref="CDD:443253"
     CDS             1..385
                     /gene="PRMT8"
                     /gene_synonym="HRMT1L3; HRMT1L4"
                     /coded_by="NM_001256536.1:47..1204"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58200.1"
                     /db_xref="GeneID:56341"
                     /db_xref="HGNC:HGNC:5188"
                     /db_xref="MIM:610086"
ORIGIN      
        1 meslasdgfk lkevssvnsp psqppqpvvp akpvqcvhhv stqpscpgrg kmskllnpee
       61 mtsrdyyfds yahfgiheem lkdevrtlty rnsmyhnkhv fkdkvvldvg sgtgilsmfa
      121 akagakkvfg iecssisdys ekiikanhld niitifkgkv eevelpvekv diiisewmgy
      181 clfyesmlnt vifardkwlk pgglmfpdra alyvvaiedr qykdfkihww envygfdmtc
      241 irdvamkepl vdivdpkqvv tnaclikevd iytvkteels ftsafclqiq rndyvhalvt
      301 yfnieftkch kkmgfstapd apythwkqtv fyledyltvr rgeeiygtis mkpnaknvrd
      361 ldftvdldfk gqlcetsvsn dykmr
//
LOCUS       NP_001289698            1205 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog B isoform Par3La [Homo sapiens].
ACCESSION   NP_001289698 XP_005246330
VERSION     NP_001289698.1
DBSOURCE    REFSEQ: accession NM_001302769.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1205)
  AUTHORS   Xu,H., Lin,X., Li,Z., He,X., Li,Y., Qiu,L., Lu,L., Liu,B., Zhan,M.
            and He,K.
  TITLE     VIRMA facilitates intrahepatic cholangiocarcinoma progression
            through epigenetic augmentation of TMED2 and PARD3B mRNA
            stabilization
  JOURNAL   J Gastroenterol 58 (9), 925-944 (2023)
   PUBMED   37391589
  REMARK    GeneRIF: VIRMA facilitates intrahepatic cholangiocarcinoma
            progression through epigenetic augmentation of TMED2 and PARD3B
            mRNA stabilization.
REFERENCE   2  (residues 1 to 1205)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1205)
  AUTHORS   Thompson,B.J.
  TITLE     Par-3 family proteins in cell polarity & adhesion
  JOURNAL   FEBS J 289 (3), 596-613 (2022)
   PUBMED   33565714
  REMARK    GeneRIF: Par-3 family proteins in cell polarity & adhesion.
            Review article
REFERENCE   4  (residues 1 to 1205)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   5  (residues 1 to 1205)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1205)
  AUTHORS   Izaki,T., Kamakura,S., Kohjima,M. and Sumimoto,H.
  TITLE     Phosphorylation-dependent binding of 14-3-3 to Par3beta, a human
            Par3-related cell polarity protein
  JOURNAL   Biochem Biophys Res Commun 329 (1), 211-218 (2005)
   PUBMED   15721295
  REMARK    GeneRIF: binding of 14-3-3 to Par3beta is dependent on
            phosphorylation
REFERENCE   7  (residues 1 to 1205)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   8  (residues 1 to 1205)
  AUTHORS   Kohjima,M., Noda,Y., Takeya,R., Saito,N., Takeuchi,K. and
            Sumimoto,H.
  TITLE     PAR3beta, a novel homologue of the cell polarity protein PAR3,
            localizes to tight junctions
  JOURNAL   Biochem Biophys Res Commun 299 (4), 641-646 (2002)
   PUBMED   12459187
  REMARK    GeneRIF: PAR3beta, expressed intrinsically or extrinsically,
            localizes to the tight junctions, indicating that the localization
            does not require the ternary complex formation.
REFERENCE   9  (residues 1 to 1205)
  AUTHORS   Gao,L., Macara,I.G. and Joberty,G.
  TITLE     Multiple splice variants of Par3 and of a novel related gene,
            Par3L, produce proteins with different binding properties
  JOURNAL   Gene 294 (1-2), 99-107 (2002)
   PUBMED   12234671
REFERENCE   10 (residues 1 to 1205)
  AUTHORS   Hadano,S., Hand,C.K., Osuga,H., Yanagisawa,Y., Otomo,A.,
            Devon,R.S., Miyamoto,N., Showguchi-Miyata,J., Okada,Y.,
            Singaraja,R., Figlewicz,D.A., Kwiatkowski,T., Hosler,B.A.,
            Sagie,T., Skaug,J., Nasir,J., Brown,R.H. Jr., Scherer,S.W.,
            Rouleau,G.A., Hayden,M.R. and Ikeda,J.E.
  TITLE     A gene encoding a putative GTPase regulator is mutated in familial
            amyotrophic lateral sclerosis 2
  JOURNAL   Nat Genet 29 (2), 166-173 (2001)
   PUBMED   11586298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016903.3, BF434006.1, AF428250.1, AC009316.3, AC008171.3,
            AC007465.4 and AC007385.3.
            
            On Nov 13, 2014 this sequence version replaced XP_005246330.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (Par3La).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB092439.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000406610.7/ ENSP00000385848.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..1205
                     /product="partitioning defective 3 homolog B isoform
                     Par3La"
                     /note="partitioning-defective 3-beta; amyotrophic lateral
                     sclerosis 2 (juvenile) chromosome region, candidate 19;
                     partitioning defective 3 homolog B; PAR3-L protein;
                     partitioning defective 3-like protein; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 19 protein;
                     par-3 partitioning defective 3 homolog B"
                     /calculated_mol_wt=132364
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          83..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          137..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          197..294
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(212..218,234,237,267,271,274..275)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          318..374
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          377..469
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(392..398,413,416,446,450,453..454)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          492..591
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(508..514,530,533,563,567,570..571)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          707..743
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            710
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            749
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9CSB4; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          784..921
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            801
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Region          1111..1205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TEW8.2)"
     Site            1184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TEW8.2)"
     CDS             1..1205
                     /gene="PARD3B"
                     /gene_synonym="ALS2CR19; PAR3B; PAR3beta; PAR3L"
                     /coded_by="NM_001302769.2:526..4143"
                     /note="isoform Par3La is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS77511.1"
                     /db_xref="GeneID:117583"
                     /db_xref="HGNC:HGNC:14446"
                     /db_xref="MIM:619353"
ORIGIN      
        1 mkvtvcfgrt givvpckegq lrvgeltqqa lqrylktrek gpgywvkihh leytdggild
       61 pddvladvve dkdkliavfe eqeplhkies psgnpadrqs pdafetevaa qlaafkpigg
      121 eievtpsalk lgtpllvrrs sdpvpgppad tqpsashpgg qslklvvpds tqnledrevl
      181 ngvqtellts prtkdtlsdm trtveisgeg gplgihvvpf fsslsgrilg lfirgiedns
      241 rskreglfhe necivkinnv dlvdktfaqa qdvfrqamks psvllhvlpp qnreqyeksv
      301 igslnifgnn dgvlktkvpp pvhgksglkt anltgtdspe tdasaslqqn ksprvprlgg
      361 kpsspslspl mgfgsnknak kikidlkkgp eglgftvvtr dssihgpgpi fvknilpkga
      421 aikdgrlqsg drilevngrd vtgrtqeelv amlrstkqge taslviarqe ghflprelkg
      481 epdccalsle tseqltfeip lndsgsaglg vslkgnksre tgtdlgifik siihggaafk
      541 dgrlrmndql iavngesllg ksnheametl rrsmsmegni rgmiqlvilr rperpmedpa
      601 ecgafskpcf encqnavtts rrndnsilhp lgtcspqdkq kglllpndgw aesevppspt
      661 phsalglgle dyshssgvds avyfpdqhin frsvtparqp esinlkasks mdlvpdeskv
      721 hslagqkses pskdfgptlg lkkssslesl qtavaevrkn dlpfhrprph mvrgrgcnes
      781 fraaidksyd gpeeieadgl sdksshsgqg alncesapqg nseledmenk arkvkktkek
      841 ekkkekgklk vkekkrkeen edperkikkk gfgamlrfgk kkedkggkae qkgtlkhggl
      901 reeelekmke ererigakhq elrekqargl ldyatgaigs vydmdddemd pnyarvnhfr
      961 epctsanvfr spsppragpf gyprdghpls perdhlegly akvnkpyhpl vpadsgrptg
     1021 gstdriqklr keyyqarreg fplyeddegr arpseydllw vpgrgpdgna hnlrfegmer
     1081 qyaslprggp adpvdylpaa prglykerel pyypgahpmh ppkgsyprpt elrvadlryp
     1141 qhyppppapq hkgpfrqdvp psppqhqrmp ayqetgrpgp rggspdqypy rtqdsrqknp
     1201 mtaav
//
LOCUS       NP_001307082             298 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-L2 isoform C [Homo sapiens].
ACCESSION   NP_001307082
VERSION     NP_001307082.1
DBSOURCE    REFSEQ: accession NM_001320153.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Hluchy,M., Gajduskova,P., Ruiz de Los Mozos,I., Rajecky,M.,
            Kluge,M., Berger,B.T., Slaba,Z., Potesil,D., Weiss,E., Ule,J.,
            Zdrahal,Z., Knapp,S., Paruch,K., Friedel,C.C. and Blazek,D.
  TITLE     CDK11 regulates pre-mRNA splicing by phosphorylation of SF3B1
  JOURNAL   Nature 609 (7928), 829-834 (2022)
   PUBMED   36104565
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wu,C., Zhu,Q., Yao,Y., Shi,Z., Jin,C. and Chen,L.
  TITLE     Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription
  JOURNAL   Dev Neurosci 44 (3), 121-130 (2022)
   PUBMED   34937039
  REMARK    GeneRIF: Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Loyer,P., Trembley,J.H., Grenet,J.A., Busson,A., Corlu,A., Zhao,W.,
            Kocak,M., Kidd,V.J. and Lahti,J.M.
  TITLE     Characterization of cyclin L1 and L2 interactions with CDK11 and
            splicing factors: influence of cyclin L isoforms on splice site
            selection
  JOURNAL   J Biol Chem 283 (12), 7721-7732 (2008)
   PUBMED   18216018
  REMARK    GeneRIF: CDK11(p110) interacts physically and functionally with
            cyclin Lalpha and -beta isoforms and SR proteins to regulate
            splicing.
REFERENCE   7  (residues 1 to 298)
  AUTHORS   de Graaf,K., Hekerman,P., Spelten,O., Herrmann,A., Packman,L.C.,
            Bussow,K., Muller-Newen,G. and Becker,W.
  TITLE     Characterization of cyclin L2, a novel cyclin with an
            arginine/serine-rich domain: phosphorylation by DYRK1A and
            colocalization with splicing factors
  JOURNAL   J Biol Chem 279 (6), 4612-4624 (2004)
   PUBMED   14623875
  REMARK    GeneRIF: characterize cyclin L2 as a highly mobile component of
            nuclear speckles and suggest that DYRK1A may regulate splicing by
            phosphorylation of cyclin L2
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Edelheit,S. and Meiri,N.
  TITLE     Cyclin S: a new member of the cyclin family plays a role in
            long-term memory
  JOURNAL   Eur J Neurosci 19 (2), 365-375 (2004)
   PUBMED   14725631
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Cheng,H. and Bjerknes,M.
  TITLE     Patterns of gene expression along the crypt-villus axis in mouse
            jejunal epithelium
  JOURNAL   Anat Rec 244 (1), 78-94 (1996)
   PUBMED   8838426
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Bunnell,B.A., Heath,L.S., Adams,D.E., Lahti,J.M. and Kidd,V.J.
  TITLE     Increased expression of a 58-kDa protein kinase leads to changes in
            the CHO cell cycle
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7467-7471 (1990)
   PUBMED   2217177
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2612]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY002650.1, AK056120.1,
            AL391244.11, CR628411.1, AK074112.1 and AK000685.1.
            
            Summary: The protein encoded by this gene belongs to the cyclin
            family. Through its interaction with several proteins, such as RNA
            polymerase II, splicing factors, and cyclin-dependent kinases, this
            protein functions as a regulator of the pre-mRNA splicing process,
            as well as in inducing apoptosis by modulating the expression of
            apoptotic and antiapoptotic proteins. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.191135.1,
                                           SRR7346977.2147598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..298
                     /product="cyclin-L2 isoform C"
                     /note="cyclin M; paneth cell-enhanced expression protein;
                     cyclin S"
                     /calculated_mol_wt=33708
     Region          <1..95
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..298
                     /gene="CCNL2"
                     /gene_synonym="ANIA-6B; CCNM; CCNS; HCLA-ISO; HLA-ISO;
                     PCEE; SB138"
                     /coded_by="NM_001320153.3:1420..2316"
                     /note="isoform C is encoded by transcript variant 3"
                     /db_xref="GeneID:81669"
                     /db_xref="HGNC:HGNC:20570"
                     /db_xref="MIM:613482"
ORIGIN      
        1 mndslrtdvf vrfqpesiac aciylaartl eiplpnrphw fllfgateee iqeiclkilq
       61 lyarkkvdlt hlegevekrk haieeakaqa rgllpggtqv ldgtsgfspa pklvespkeg
      121 kgskpsplsv kntkrrlega kkakadspvn glpkgresrs rsrsreqsys rspsrsaspk
      181 rrksdsgsts ggsksqsrsr srsdspprqa prsapykgse irgsrkskdc kypqkphksr
      241 srsssrsrsr sreradnpgk ykkkshyyrd qrrersrsye rtgrryerdh pghsrhrr
//
LOCUS       NP_001354667             492 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform d [Homo sapiens].
ACCESSION   NP_001354667
VERSION     NP_001354667.1
DBSOURCE    REFSEQ: accession NM_001367738.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 492)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079588.6 and AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (22), as well as variants 21, 23,
            and 24, encodes isoform d.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.75706.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..492
                     /product="rab5 GDP/GTP exchange factor isoform d"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56831
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          159..221
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          271..371
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..492
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367738.1:192..1670"
                     /note="isoform d is encoded by transcript variant 22"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkaeiqe
      121 akapspsinr qtsietdrvs kefieflktf hktgqeiykq tklflegmhy krdlsieeqs
      181 ecaqdfyhnv aermqtrgkv ppervekimd qiekyimtrl ykyvfcpett ddekkdlaiq
      241 kriralrwvt pqmlcvpvne dipevsdmvv kaitdiiemd skrvprdkla citkcskhif
      301 naikitknep asaddflptl iyivlkgnpp rlqsniqyit rfcnpsrlmt gedgyyftnl
      361 ccavafiekl daqslnlsqe dfdrymsgqt sprkqeaesw spdaclgvkq myknldllsq
      421 lnerqerimn eakklekdli dwtdgiarev qdivekyple ikppnqplaa idsenvendk
      481 lppplqpqvy ag
//
LOCUS       NP_620152                300 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat domain-containing protein 54 isoform 1 [Homo
            sapiens].
ACCESSION   NP_620152
VERSION     NP_620152.1
DBSOURCE    REFSEQ: accession NM_138797.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Gustafsson,M.O., Mohammad,D.K., Ylosmaki,E., Choi,H., Shrestha,S.,
            Wang,Q., Nore,B.F., Saksela,K. and Smith,C.I.
  TITLE     ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from
            a Human Src-Homology 3 (SH3) domain library
  JOURNAL   PLoS One 12 (4), e0174909 (2017)
   PUBMED   28369144
  REMARK    GeneRIF: the results show that the interaction between BTK and
            ANKRD54 is highly selective, since it was also identified in a
            screen using human SH3-domainome. A novel finding is that BTK not
            only binds to ANKRD54, but stands out as the preferred interactor,
            being highly dominant over all other human SH3-domains.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Gustafsson,M.O., Hussain,A., Mohammad,D.K., Mohamed,A.J.,
            Nguyen,V., Metalnikov,P., Colwill,K., Pawson,T., Smith,C.I. and
            Nore,B.F.
  TITLE     Regulation of nucleocytoplasmic shuttling of Bruton's tyrosine
            kinase (Btk) through a novel SH3-dependent interaction with ankyrin
            repeat domain 54 (ANKRD54)
  JOURNAL   Mol Cell Biol 32 (13), 2440-2453 (2012)
   PUBMED   22527282
  REMARK    GeneRIF: Liar is the first protein identified that specifically
            influences the nucleocytoplasmic shuttling of Btk and Txk and
            belongs to a rare group of known proteins carrying out this
            activity in a Crm1-dependent manner.
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY007929.1, BC066909.1 and BC014641.1.
            
            Transcript Variant: This variant (1) represents the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014641.1, SRR1163658.175952.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215941.9/ ENSP00000215941.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..300
                     /product="ankyrin repeat domain-containing protein 54
                     isoform 1"
                     /note="ankyrin repeat domain-containing protein 54;
                     lyn-interacting ankyrin repeat protein"
                     /calculated_mol_wt=32374
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          99..117
                     /region_name="Nuclear localization signal (NLS).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          109..138
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          <114..>236
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            order(119..121,123..124,128,131,140,142,144,148..149,
                     152..154,156..157,161,164,173,175,177,181..182,185..187,
                     189..190,194,197,206)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          141..241
                     /region_name="LYN-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          142..173
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          175..206
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          208..244
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     Region          283..293
                     /region_name="Nuclear export signal (NES).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT1.2)"
     CDS             1..300
                     /gene="ANKRD54"
                     /gene_synonym="LIAR"
                     /coded_by="NM_138797.4:97..999"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13959.1"
                     /db_xref="GeneID:129138"
                     /db_xref="HGNC:HGNC:25185"
                     /db_xref="MIM:613383"
ORIGIN      
        1 maaaagdadd eprsghssse gecavapepl tdaeglfsfa dfgsalgggg aglsgrasgg
       61 aqsplrylhv lwqqdaeprd elrckipagr lrraarphrr lgptgkevha lkrlrdsana
      121 ndvetvqqll edgadpcaad dkgrtalhfa scngndqivq llldhgadpn qrdglgntpl
      181 hlaactnhvp vittllrgga rvdaldragr tplhlakskl nilqeghaqc leavrlevkq
      241 iihmlreyle rlgqheqrer lddlctrlqm tstkeqvdev tdllasftsl slqmqsmekr
//
LOCUS       NP_001316561             603 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 46 [Homo sapiens].
ACCESSION   NP_001316561
VERSION     NP_001316561.1
DBSOURCE    REFSEQ: accession NM_001329632.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 603)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 603)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 603)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 603)
  AUTHORS   Choppara,S., Ganga,S., Manne,R., Dutta,P., Singh,S. and Santra,M.K.
  TITLE     The SCFFBXO46 ubiquitin ligase complex mediates degradation of the
            tumor suppressor FBXO31 and thereby prevents premature cellular
            senescence
  JOURNAL   J Biol Chem 293 (42), 16291-16306 (2018)
   PUBMED   30171069
  REMARK    GeneRIF: reveal that FBXO46 is a crucial proteasomal regulator of
            FBXO31 and thereby prevents senescence in normal growth conditions
REFERENCE   5  (residues 1 to 603)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 603)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007191.1.
            
            Summary: Members of the F-box protein family, such as FBXO46, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. All four variants encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX645927.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..603
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..603
                     /product="F-box only protein 46"
                     /calculated_mol_wt=64500
     Region          20..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          <110..>300
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Region          111..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          235..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          326..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          396..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PJ61.3)"
     Region          473..519
                     /region_name="F-box_FBXO46"
                     /note="F-box domain found in F-box only protein 46
                     (FBXO46) and similar proteins; cd22177"
                     /db_xref="CDD:438948"
     Site            order(476,480,483..484,487..488,492,494..495,499..501,503)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438948"
     CDS             1..603
                     /gene="FBXO46"
                     /gene_synonym="20D7-FC4; Fbx46; FBXO34L"
                     /coded_by="NM_001329632.1:589..2400"
                     /db_xref="CCDS:CCDS46116.1"
                     /db_xref="GeneID:23403"
                     /db_xref="HGNC:HGNC:25069"
                     /db_xref="MIM:609117"
ORIGIN      
        1 mdrgsllpfq lwcprpfgty sqnqprppsa alkpsacpep gggaepdhgp ahsentppal
       61 atevpasqpa pllsaaaagd egrvlldtwy vikpgntkek vaffvahqcg ggsrassmkv
      121 kghwgsdssk akrrrrcldp tkappdpggr egppaaeegp asagedvdll svaemvalve
      181 qraalalqsy prpttpapvv fvsaeqggpa kgvgserrsg ggdcsrvaea vahfeaqrds
      241 pptkglrkee rpgpgpgevr iafrisngre prapdsglps ggggrpgcay pgspgpgara
      301 kdkitcdlyq lispsrdalp snvefllara deasegdspa parpedtppa pppppardcg
      361 asgfhvdvvv tgvvdeciff gkdgtknvke etvcltvspe eppppgqlff lqnrgpdgpp
      421 epppadspat apgpddaegt adtslcrlyr hvshdfleir fkiqrllepr qymlllpehv
      481 lvkifsflpt ralaalkctc hhfkgiieaf gvratdsrws rdplyrddpc kqcrkryekg
      541 dvslcrwhpk pyhhdlpygr sywmccrrad retpgcrlgl hdnnwvlpcn gpgggragre
      601 egr
//
LOCUS       NP_001265407             485 aa            linear   PRI 20-NOV-2025
DEFINITION  runt-related transcription factor 2 isoform d [Homo sapiens].
ACCESSION   NP_001265407
VERSION     NP_001265407.1
DBSOURCE    REFSEQ: accession NM_001278478.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 485)
  AUTHORS   Komori,T.
  TITLE     Regulation of Skeletal Development and Maintenance by Runx2 and Sp7
  JOURNAL   Int J Mol Sci 25 (18), 10102 (2024)
   PUBMED   39337587
  REMARK    GeneRIF: Regulation of Skeletal Development and Maintenance by
            Runx2 and Sp7.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 485)
  AUTHORS   Vitale,E., Manicardi,V., Gugnoni,M., Torricelli,F., Donati,B.,
            Muccioli,S., Salviato,E., Rossi,T., Manzotti,G., Piana,S. and
            Ciarrocchi,A.
  TITLE     Exploring the transcriptional cooperation between RUNX2 and its
            associated elncRNA RAIN
  JOURNAL   Cell Death Dis 15 (9), 673 (2024)
   PUBMED   39271656
  REMARK    GeneRIF: Exploring the transcriptional cooperation between RUNX2
            and its associated elncRNA RAIN.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 485)
  AUTHORS   Yalaev,B., Tyurin,A., Akhiiarova,K. and Khusainova,R.
  TITLE     Hypomethylation of the RUNX2 Gene Is a New Potential Biomarker of
            Primary Osteoporosis in Men and Women
  JOURNAL   Int J Mol Sci 25 (13), 7312 (2024)
   PUBMED   39000419
  REMARK    GeneRIF: Hypomethylation of the RUNX2 Gene Is a New Potential
            Biomarker of Primary Osteoporosis in Men and Women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 485)
  AUTHORS   Drissi,H., Luc,Q., Shakoori,R., Chuva De Sousa Lopes,S., Choi,J.Y.,
            Terry,A., Hu,M., Jones,S., Neil,J.C., Lian,J.B., Stein,J.L., Van
            Wijnen,A.J. and Stein,G.S.
  TITLE     Transcriptional autoregulation of the bone related CBFA1/RUNX2 gene
  JOURNAL   J Cell Physiol 184 (3), 341-350 (2000)
   PUBMED   10911365
REFERENCE   5  (residues 1 to 485)
  AUTHORS   Geoffroy,V., Corral,D.A., Zhou,L., Lee,B. and Karsenty,G.
  TITLE     Genomic organization, expression of the human CBFA1 gene, and
            evidence for an alternative splicing event affecting protein
            function
  JOURNAL   Mamm Genome 9 (1), 54-57 (1998)
   PUBMED   9434946
REFERENCE   6  (residues 1 to 485)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   7  (residues 1 to 485)
  AUTHORS   Feldman,G.J., Robin,N.H., Brueton,L.A., Robertson,E.,
            Thompson,E.M., Siegel-Bartelt,J., Gasser,D.L., Bailey,L.C.,
            Zackai,E.H. and Muenke,M.
  TITLE     A gene for cleidocranial dysplasia maps to the short arm of
            chromosome 6
  JOURNAL   Am J Hum Genet 56 (4), 938-943 (1995)
   PUBMED   7717404
REFERENCE   8  (residues 1 to 485)
  AUTHORS   Levanon,D., Negreanu,V., Bernstein,Y., Bar-Am,I., Avivi,L. and
            Groner,Y.
  TITLE     AML1, AML2, and AML3, the human members of the runt domain
            gene-family: cDNA structure, expression, and chromosomal
            localization
  JOURNAL   Genomics 23 (2), 425-432 (1994)
   PUBMED   7835892
REFERENCE   9  (residues 1 to 485)
  AUTHORS   Ogawa,E., Maruyama,M., Kagoshima,H., Inuzuka,M., Lu,J., Satake,M.,
            Shigesada,K. and Ito,Y.
  TITLE     PEBP2/PEA2 represents a family of transcription factors homologous
            to the products of the Drosophila runt gene and the human AML1 gene
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6859-6863 (1993)
   PUBMED   8341710
REFERENCE   10 (residues 1 to 485)
  AUTHORS   Machol,K., Mendoza-Londono,R. and Lee,B.
  TITLE     Cleidocranial Dysplasia Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301686
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096865.28, AL358135.19 and
            AL161907.17.
            
            Summary: This gene is a member of the RUNX family of transcription
            factors and encodes a nuclear protein with an Runt DNA-binding
            domain. This protein is essential for osteoblastic differentiation
            and skeletal morphogenesis and acts as a scaffold for nucleic acids
            and regulatory factors involved in skeletal gene expression. The
            protein can bind DNA both as a monomer or, with more affinity, as a
            subunit of a heterodimeric complex. Two regions of potential
            trinucleotide repeat expansions are present in the N-terminal
            region of the encoded protein, and these and other mutations in
            this gene have been associated with the bone development disorder
            cleidocranial dysplasia (CCD). Transcript variants that encode
            different protein isoforms result from the use of alternate
            promoters as well as alternate splicing. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (4) contains an alternate 5'-most
            exon, lacks an in-frame exon in the 3' coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (d) has a distinct and shorter N-terminus, compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR6380202.78952.5, L40992.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..485
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..485
                     /product="runt-related transcription factor 2 isoform d"
                     /note="core-binding factor, runt domain, alpha subunit 1;
                     acute myeloid leukemia 3 protein; SL3-3 enhancer factor 1
                     alpha A subunit; runt related transcription factor 2;
                     SL3/AKV core-binding factor alpha A subunit;
                     osteoblast-specific transcription factor 2; PEA2-alpha A;
                     PEBP2-alpha A; oncogene AML-3; polyomavirus
                     enhancer-binding protein 2 alpha A subunit"
                     /calculated_mol_wt=52525
     Region          88..216
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <152..>342
                     /region_name="SOG2"
                     /note="RAM signalling pathway protein; pfam10428"
                     /db_xref="CDD:431280"
     Region          394..485
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..485
                     /gene="RUNX2"
                     /gene_synonym="AML3; CBF-alpha-1; CBFA1; CCD; CCD1; CLCD;
                     OSF-2; OSF2; PEA2aA; PEBP2aA"
                     /coded_by="NM_001278478.2:303..1760"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS64443.1"
                     /db_xref="GeneID:860"
                     /db_xref="HGNC:HGNC:10472"
                     /db_xref="MIM:600211"
ORIGIN      
        1 mripvdpsts rrfsppsssl qpgkmsdvsp vvaaqqqqqq qqqqqqqqqq qqqqqqqeaa
       61 aaaaaaaaaa aaaaavprlr pphdnrtmve iiadhpaelv rtdspnflcs vlpshwrcnk
      121 tlpvafkvva lgevpdgtvv tvmagndeny saelrnasav mknqvarfnd lrfvgrsgrg
      181 ksftltitvf tnppqvatyh raikvtvdgp reprrhrqkl ddskpslfsd rlsdlgriph
      241 psmrvgvppq nprpslnsap spfnpqgqsq itdprqaqss ppwsydqsyp sylsqmtsps
      301 ihsttplsst rgtglpaitd vprrisgase lgpfsdprqf psissltesr fsnprmhypa
      361 tftytppvts gmslgmsatt hyhtylpppy pgssqsqsgp fqtsstpyly ygtssgsyqf
      421 pmvpggdrsp srmlppcttt sngstllnpn lpnqndgvda dgshsssptv lnssgrmdes
      481 vwrpy
//
LOCUS       NP_006014                336 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor eIF2 assembly protein [Homo sapiens].
ACCESSION   NP_006014
VERSION     NP_006014.2
DBSOURCE    REFSEQ: accession NM_006023.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Wang,Y., Pan,H., Gong,X., Wang,Z., Qin,X., Zhou,S., Zhu,C., Hu,X.,
            Chen,S., Liu,H., Jin,H., Pang,Q. and Wu,W.
  TITLE     CDC123 promotes Hepatocellular Carcinoma malignant progression by
            regulating CDKAL1
  JOURNAL   Pathol Res Pract 254, 154987 (2024)
   PUBMED   38237400
  REMARK    GeneRIF: CDC123 promotes Hepatocellular Carcinoma malignant
            progression by regulating CDKAL1.
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Song,N., Deng,L., Zeng,L., He,L., Liu,C., Liu,L. and Fu,R.
  TITLE     USP9X deubiquitinates and stabilizes CDC123 to promote breast
            carcinogenesis through regulating cell cycle
  JOURNAL   Mol Carcinog 62 (10), 1487-1503 (2023)
   PUBMED   37314216
  REMARK    GeneRIF: USP9X deubiquitinates and stabilizes CDC123 to promote
            breast carcinogenesis through regulating cell cycle.
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Cardenal Peralta,C., Vandroux,P., Neumann-Arnold,L., Panvert,M.,
            Fagart,J., Seufert,W., Mechulam,Y. and Schmitt,E.
  TITLE     Binding of human Cdc123 to eIF2gamma
  JOURNAL   J Struct Biol 215 (3), 108006 (2023)
   PUBMED   37507029
  REMARK    GeneRIF: Binding of human Cdc123 to eIF2gamma.
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 336)
  AUTHORS   Bieganowski,P., Shilinski,K., Tsichlis,P.N. and Brenner,C.
  TITLE     Cdc123 and checkpoint forkhead associated with RING proteins
            control the cell cycle by controlling eIF2gamma abundance
  JOURNAL   J Biol Chem 279 (43), 44656-44666 (2004)
   PUBMED   15319434
REFERENCE   8  (residues 1 to 336)
  AUTHORS   Hoja,M.R., Wahlestedt,C. and Hoog,C.
  TITLE     A visual intracellular classification strategy for uncharacterized
            human proteins
  JOURNAL   Exp Cell Res 259 (1), 239-246 (2000)
   PUBMED   10942595
REFERENCE   9  (residues 1 to 336)
  AUTHORS   Onisto,M., Zeilante,P., Scannapieco,P., Pellati,D., Pozza,M.,
            Caenazzo,C., Negro,A. and Garbisa,S.
  TITLE     Expression study on D123 gene product: evidence for high positivity
            in testis
  JOURNAL   Exp Cell Res 242 (2), 451-459 (1998)
   PUBMED   9683532
REFERENCE   10 (residues 1 to 336)
  AUTHORS   Okuda,A. and Kimura,G.
  TITLE     An amino acid change in novel protein D123 is responsible for
            temperature-sensitive G1-phase arrest in a mutant of rat fibroblast
            line 3Y1
  JOURNAL   Exp Cell Res 223 (2), 242-249 (1996)
   PUBMED   8601400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP367374.1, BC009598.1 and AW006077.1.
            
            On Jan 24, 2009 this sequence version replaced NP_006014.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.45890.1,
                                           SRR5189658.92644.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000281141.9/ ENSP00000281141.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p14-p13"
     Protein         1..336
                     /product="translation initiation factor eIF2 assembly
                     protein"
                     /note="cell division cycle protein 123 homolog; PZ32;
                     HT-1080; cell division cycle 123 homolog"
                     /calculated_mol_wt=39004
     Region          14..314
                     /region_name="D123"
                     /note="pfam07065"
                     /db_xref="CDD:462079"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75794.1)"
     CDS             1..336
                     /gene="CDC123"
                     /gene_synonym="C10orf7; D123"
                     /coded_by="NM_006023.3:59..1069"
                     /db_xref="CCDS:CCDS7090.1"
                     /db_xref="GeneID:8872"
                     /db_xref="HGNC:HGNC:16827"
                     /db_xref="MIM:617708"
ORIGIN      
        1 mkkehvlhcq fsawypffrg vtiksvilpl pqnvkdylld dgtlvvsgrd dppthsqpds
       61 ddeaeeiqws ddentatlta pefpefatkv qeainslggs vfpklnwsap rdaywiamns
      121 slkcktlsdi fllfkssdfi trdftqpfih ctddspdpci eyelvlrkwc elipgaefrc
      181 fvkenkligi sqrdytqyyd hiskqkeeir rciqdffkkh iqykfldedf vfdiyrdsrg
      241 kvwlidfnpf gevtdsllft weelisennl ngdfsevdaq eqdspafrct nsevtvqpsp
      301 ylsyrlpkdf vdlstgedah klidflklkr nqqedd
//
LOCUS       NP_001124174             287 aa            linear   PRI 20-NOV-2025
DEFINITION  seipin isoform 3 [Homo sapiens].
ACCESSION   NP_001124174
VERSION     NP_001124174.2
DBSOURCE    REFSEQ: accession NM_001130702.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Guo,D., Hu,L., Xie,P., Sun,P. and Yu,W.
  TITLE     Seipin is involved in oxygen-glucose deprivation/reoxygenation
            induced neuroinflammation by regulating the TLR3/TRAF3/NF-kappaB
            pathway
  JOURNAL   Int Immunopharmacol 134, 112182 (2024)
   PUBMED   38703568
  REMARK    GeneRIF: Seipin is involved in oxygen-glucose
            deprivation/reoxygenation induced neuroinflammation by regulating
            the TLR3/TRAF3/NF-kappaB pathway.
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Zhu,X., An,X., Chen,M., Guo,D., Xie,P., Wang,B., Huang,Z. and Yu,W.
  TITLE     Seipin overexpression attenuates cerebral ischemia-reperfusion
            injury via preventing apoptosis and autophagy
  JOURNAL   Brain Behav 13 (12), e3195 (2023)
   PUBMED   37897134
  REMARK    GeneRIF: Seipin overexpression attenuates cerebral
            ischemia-reperfusion injury via preventing apoptosis and autophagy.
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Weterman,M.A.J., Bronk,M., Jongejan,A., Hoogendijk,J.E., Krudde,J.,
            Karjosukarso,D., Goebel,H.H., Aronica,E., Jobsis,G.J., van
            Ruissen,F., van Spaendonck-Zwarts,K.Y., de Visser,M. and Baas,F.
  TITLE     Pathogenic variants in three families with distal muscle
            involvement
  JOURNAL   Neuromuscul Disord 33 (1), 58-64 (2023)
   PUBMED   36539320
  REMARK    GeneRIF: Pathogenic variants in three families with distal muscle
            involvement.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Windpassinger,C., Auer-Grumbach,M., Irobi,J., Patel,H., Petek,E.,
            Horl,G., Malli,R., Reed,J.A., Dierick,I., Verpoorten,N.,
            Warner,T.T., Proukakis,C., Van den Bergh,P., Verellen,C., Van
            Maldergem,L., Merlini,L., De Jonghe,P., Timmerman,V., Crosby,A.H.
            and Wagner,K.
  TITLE     Heterozygous missense mutations in BSCL2 are associated with distal
            hereditary motor neuropathy and Silver syndrome
  JOURNAL   Nat Genet 36 (3), 271-276 (2004)
   PUBMED   14981520
  REMARK    GeneRIF: Heterozygous missense mutations in BSCL2 are associated
            with distal hereditary motor neuropathy and Silver syndrome.
            GeneRIF: seipin is an integral membrane protein of the endoplasmic
            reticulum (ER)
REFERENCE   5  (residues 1 to 287)
  AUTHORS   Simha,V. and Garg,A.
  TITLE     Phenotypic heterogeneity in body fat distribution in patients with
            congenital generalized lipodystrophy caused by mutations in the
            AGPAT2 or seipin genes
  JOURNAL   J Clin Endocrinol Metab 88 (11), 5433-5437 (2003)
   PUBMED   14602785
  REMARK    GeneRIF: Congenital lipodystrophy patients with Seipin mutations
            have a more severe lack of body fat, which affects both
            metabolically active and mechanical adipose tissue, compared with
            patients with mutations in the AGPAT2 gene.
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Magre,J., Delepine,M., Khallouf,E., Gedde-Dahl,T. Jr., Van
            Maldergem,L., Sobel,E., Papp,J., Meier,M., Megarbane,A., Bachy,A.,
            Verloes,A., d'Abronzo,F.H., Seemanova,E., Assan,R., Baudic,N.,
            Bourut,C., Czernichow,P., Huet,F., Grigorescu,F., de Kerdanet,M.,
            Lacombe,D., Labrune,P., Lanza,M., Loret,H., Matsuda,F., Navarro,J.,
            Nivelon-Chevalier,A., Polak,M., Robert,J.J., Tric,P.,
            Tubiana-Rufi,N., Vigouroux,C., Weissenbach,J., Savasta,S.,
            Maassen,J.A., Trygstad,O., Bogalho,P., Freitas,P., Medina,J.L.,
            Bonnicci,F., Joffe,B.I., Loyson,G., Panz,V.R., Raal,F.J.,
            O'Rahilly,S., Stephenson,T., Kahn,C.R., Lathrop,M. and Capeau,J.
  CONSRTM   BSCL Working Group
  TITLE     Identification of the gene altered in Berardinelli-Seip congenital
            lipodystrophy on chromosome 11q13
  JOURNAL   Nat Genet 28 (4), 365-370 (2001)
   PUBMED   11479539
  REMARK    GeneRIF: Alterations in BSCL2 (seipin gene) are responsible for
            BSCL (OMIM :606158).Predicted human seipin protein sequence.
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Patel,H., Hart,P.E., Warner,T.T., Houlston,R.S., Patton,M.A.,
            Jeffery,S. and Crosby,A.H.
  TITLE     The Silver syndrome variant of hereditary spastic paraplegia maps
            to chromosome 11q12-q14, with evidence for genetic heterogeneity
            within this subtype
  JOURNAL   Am J Hum Genet 69 (1), 209-215 (2001)
   PUBMED   11389484
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Ito,D.
  TITLE     BSCL2-Related Neurologic Disorders / Seipinopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301484
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Van Maldergem,L.
  TITLE     Berardinelli-Seip Congenital Lipodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027524.1 and DB296305.1.
            
            On Mar 12, 2011 this sequence version replaced NP_001124174.1.
            
            Summary: This gene encodes the multi-pass transmembrane protein
            seipin. This protein localizes to the endoplasmic reticulum and may
            be important for lipid droplet morphology. Mutations in this gene
            have been associated with congenital generalized lipodystrophy type
            2 or Berardinelli-Seip syndrome, a rare autosomal recessive disease
            characterized by a near absence of adipose tissue and severe
            insulin resistance. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            Naturally occurring read-through transcription occurs between this
            locus and the neighboring locus HNRNPUL2 (heterogeneous nuclear
            ribonucleoprotein U-like 2).[provided by RefSeq, Jul 2024].
            
            Transcript Variant: This variant (3) has multiple differences,
            compared to variant 1, one of which results in a translational
            frameshift. The resulting protein (isoform 3) is shorter at the
            N-terminus and has a distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK027524.1, SRR5189667.108411.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..287
                     /product="seipin isoform 3"
                     /note="Bernardinelli-Seip congenital lipodystrophy type 2
                     protein; Berardinelli-Seip congenital lipodystrophy 2
                     (seipin); BSCL2, seipin lipid droplet biogenesis
                     associated"
                     /calculated_mol_wt=32523
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96G97.3)"
     Region          58..222
                     /region_name="Seipin"
                     /note="Seipin and similar proteins; cd23993"
                     /db_xref="CDD:467827"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14981520; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     CDS             1..287
                     /gene="BSCL2"
                     /gene_synonym="GNG3LG; HMN5; HMN5C; HMND13; PELD; SPG17"
                     /coded_by="NM_001130702.2:219..1082"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55769.1"
                     /db_xref="GeneID:26580"
                     /db_xref="HGNC:HGNC:15832"
                     /db_xref="MIM:606158"
ORIGIN      
        1 mvndppvpal lwaqevgqvl agrarrlllq fgvlfctill llwvsvflyg sfyysymptv
       61 shlspvhfyy rtdcdsstts lcsfpvanvs ltkggrdrvl mygqpyrvtl elelpespvn
      121 qdlgmflvti scytrggrii stssrsvmlh yrsdllqmld tlvfsslllf gfaeqkqlle
      181 velyadyren syvpttgaii eihskriqly gaylrihahf tglrltseke tipgrksneg
      241 sllisqglka rrsqlrnqml qrmvralkip qgqrvscprr rnqissp
//
LOCUS       NP_001340977             705 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform k [Homo sapiens].
ACCESSION   NP_001340977
VERSION     NP_001340977.1
DBSOURCE    REFSEQ: accession NM_001354048.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 705)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 705)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 705)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 705)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 705)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 705)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 705)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AL390754.18 and
            AL139086.12.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (14), as well as variants 15-17,
            encodes isoform k.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.116358.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465404 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..705
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     k"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=79702
     Region          10..63
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(15,17,20,23..24,39,41..43,54,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          94..271
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(100,104,198,222..223,226..227,229..230,233..234,
                     237..238,241,267,271)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          302..400
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          460..550
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     Region          620..704
                     /region_name="betaPIX_CC"
                     /note="betaPIX coiled coil; pfam16523"
                     /db_xref="CDD:465158"
     CDS             1..705
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001354048.1:746..2863"
                     /note="isoform k is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS86361.1"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mtdnsnnqlv vrakfnfqqt nedelsfskg dvihvtrvee ggwwegtlng rtgwfpsnyv
       61 revkasekpv spksgtlksp pkgfdttain ksyynvvlqn ileteneysk elqtvlstyl
      121 rplqtsekls sanisylmgn leeicsfqqm lvqsleectk lpeaqqrvgg cflnlmpqmk
      181 tlyltycanh psavnvlteh seelgefmet kgasspgilv lttglskpfm rldkyptllk
      241 elerhmedyh tdrqdiqksm aafknlsaqc qevrkrkele lqilteairn wegddiktlg
      301 nvtymsqvli qcagseekne rylllfpnvl lmlsasprms gfiyqgklpt tgmtitkled
      361 senhrnafei sgsmierilv scnnqqdlqe wvehlqkqtk vtsvgnptik phsvpshtlp
      421 shpvtpsskh adskpapltp ayhtlphpsh hgtphttinw gpleppktpk pwslsclrpa
      481 pplrpsaalc ykedlskspk tmkkllpkrk perkpsdeef asrkstaale edaqilkvie
      541 ayctsaktrq tlnstwqgtd lmhnhvladd dqpsldslgr rsslsrleps dlsedsdyds
      601 iwtahsyrmg stsrsrkesa pqvllpeeek iiveetksng qtvieekslv dtvyalkdev
      661 qelrqdnkkm kksleeeqra rkdleklvrk vlknmndpaw detnl
//
LOCUS       NP_001379                364 aa            linear   PRI 20-NOV-2025
DEFINITION  developmentally-regulated GTP-binding protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001379
VERSION     NP_001379.1
DBSOURCE    REFSEQ: accession NM_001388.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Westrip,C.A.E., Zhuang,Q., Hall,C., Eaton,C.D. and Coleman,M.L.
  TITLE     Developmentally regulated GTPases: structure, function and roles in
            disease
  JOURNAL   Cell Mol Life Sci 78 (23), 7219-7235 (2021)
   PUBMED   34664086
  REMARK    GeneRIF: Developmentally regulated GTPases: structure, function and
            roles in disease.
            Review article
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Park,B.S., Im,H.L., Yoon,N.A., Tu,T.H., Park,J.W., Kim,J.G. and
            Lee,B.J.
  TITLE     Developmentally regulated GTP-binding protein-2 regulates adipocyte
            differentiation
  JOURNAL   Biochem Biophys Res Commun 578, 1-6 (2021)
   PUBMED   34520979
  REMARK    GeneRIF: Developmentally regulated GTP-binding protein-2 regulates
            adipocyte differentiation.
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Kim,S.C., Lee,W.H., Kim,S.H., Abdulkhayevich,A.A., Park,J.W.,
            Kim,Y.M., Moon,K.H., Lee,S.H. and Park,S.
  TITLE     Developmentally regulated GTP-binding protein 2 levels in prostate
            cancer cell lines impact docetaxel-induced apoptosis
  JOURNAL   Investig Clin Urol 62 (4), 485-495 (2021)
   PUBMED   34190439
  REMARK    GeneRIF: Developmentally regulated GTP-binding protein 2 levels in
            prostate cancer cell lines impact docetaxel-induced apoptosis.
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Li,B. and Trueb,B.
  TITLE     DRG represents a family of two closely related GTP-binding proteins
  JOURNAL   Biochim Biophys Acta 1491 (1-3), 196-204 (2000)
   PUBMED   10760581
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Vlangos,C.N., Das,P., Patel,P.I. and Elsea,S.H.
  TITLE     Assignment of developmentally regulated GTP-binding protein (DRG2)
            to human chromosome band 17p11.2 with somatic cell hybrids and
            localization to the Smith-Magenis syndrome critical interval
  JOURNAL   Cytogenet Cell Genet 88 (3-4), 283-285 (2000)
   PUBMED   10828610
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Sprang,S.R.
  TITLE     G proteins, effectors and GAPs: structure and mechanism
  JOURNAL   Curr Opin Struct Biol 7 (6), 849-856 (1997)
   PUBMED   9434906
  REMARK    Review article
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Schenker,T. and Trueb,B.
  TITLE     Assignment of the gene for a developmentally regulated GTP-binding
            protein (DRG2) to human chromosome bands 17p13-->p12 by in situ
            hybridization
  JOURNAL   Cytogenet Cell Genet 79 (3-4), 274-275 (1997)
   PUBMED   9605870
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Schenker,T., Lach,C., Kessler,B., Calderara,S. and Trueb,B.
  TITLE     A novel GTP-binding protein which is selectively repressed in SV40
            transformed fibroblasts
  JOURNAL   J Biol Chem 269 (41), 25447-25453 (1994)
   PUBMED   7929244
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA602486.1, BC000493.2 and
            X80754.1.
            
            Summary: This gene encodes a GTP-binding protein known to function
            in the regulation of cell growth and differentiation. Read-through
            transcripts containing this gene and a downstream gene have been
            identified, but they are not thought to encode a fusion protein.
            This gene is located within the Smith-Magenis syndrome region on
            chromosome 17. [provided by RefSeq, Jan 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.932256.1,
                                           SRR3476690.882587.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225729.8/ ENSP00000225729.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..364
                     /product="developmentally-regulated GTP-binding protein 2
                     isoform 1"
                     /note="TRAFAC GTPase DRG2; translation factor GTPase DRG2"
                     /calculated_mol_wt=40615
     Region          1..364
                     /region_name="Rbg1"
                     /note="Ribosome-interacting GTPase RBG1 [Translation,
                     ribosomal structure and biogenesis]; COG1163"
                     /db_xref="CDD:440777"
     CDS             1..364
                     /gene="DRG2"
                     /coded_by="NM_001388.5:77..1171"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11191.1"
                     /db_xref="GeneID:1819"
                     /db_xref="HGNC:HGNC:3030"
                     /db_xref="MIM:602986"
ORIGIN      
        1 mgilekisei ekeiartqkn kateyhlgll kaklakyraq llepsksass kgegfdvmks
       61 gdarvaligf psvgkstfls lmtstaseaa syefttltci pgvieykgan iqlldlpgii
      121 egaaqgkgrg rqviavarta dviimmldat kgevqrslle kelesvgirl nkhkpniyfk
      181 pkkgggisfn stvtltqcse klvqlilhey kifnaevlfr edcspdefid vivgnrvymp
      241 clyvynkidq ismeevdrla rkpnsvvisc gmklnldyll emlweylalt ciytkkrgqr
      301 pdftdaiilr kgasvehvch rihrslasqf kyalvwgtst kyspqrvglt htmehedviq
      361 ivkk
//
LOCUS       NP_001308722             938 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform e [Homo sapiens].
ACCESSION   NP_001308722
VERSION     NP_001308722.1
DBSOURCE    REFSEQ: accession NM_001321793.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 6 and 7 encode the same isoform (e).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.1167262.1,
                                           SRR14038193.1670847.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..938
                     /product="E3 ubiquitin-protein ligase CBL-B isoform e"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=104614
     Region          41..167
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          171..254
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          248..344
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(266,286,288..291,296,308,310)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(311..314,327..329)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          351..426
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(362..363,366,390,409..412)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(366..368,374..377,396,399..400,403,409..410,412)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          887..927
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(889..890,892..894,896..897,902,906)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..938
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321793.2:292..3108"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr rnltklslif shmlaeikai fpngqfqgdn fritkadaae
      181 fwrkffgdkt ivpwkvfrqc lhevhqissg leamalksti dltcndyisv fefdiftrlf
      241 qpwgsilrnw nflavthpgy mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv
      301 tgdgnilqti phnkplfqal idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy
      361 elycemgstf qlckicaend kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep
      421 iivdpfdprd egsrccsiid pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts
      481 pgssplaqrr kpqpdplqip hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq
      541 dkplpapppp lrdppppppe rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg
      601 tnqlvgcrll gegspkpgit assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl
      661 gseeydvppr lsppppvttl lpsikctgpl anslsektrd pveedddeyk ipsshpvsln
      721 sqpshchnvk ppvrscdngh cmlngthgps sekksnipdl siylkgedaf dalppslppp
      781 ppparhslie hskppgsssr pssgqdlfll psdpfvdlas gqvplpparr lpgenvktnr
      841 tsqdydqlps csdgsqapar ppkprprrta peihhrkphg peaalenvda kiaklmgegy
      901 afeevkrale iaqnnvevar silrefafpp pvsprlnl
//
LOCUS       NP_001298129             203 aa            linear   PRI 20-NOV-2025
DEFINITION  methylosome subunit pICln isoform b [Homo sapiens].
ACCESSION   NP_001298129
VERSION     NP_001298129.1
DBSOURCE    REFSEQ: accession NM_001311200.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 203)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 203)
  AUTHORS   Cui,Z., He,J., Zhu,J., Ni,W., Liu,L., Bian,Z., Mao,S., Gu,S.,
            Shan,Y., Chu,Z., Wu,Q., Lu,J., Liu,Y., Sun,F., Pan,Q., Zhang,Y.,
            Huang,N. and Ma,J.
  TITLE     O-GlcNAcylated LARP1 positively regulated by circCLNS1A facilitates
            hepatoblastoma progression through DKK4/beta-catenin signalling
  JOURNAL   Clin Transl Med 13 (4), e1239 (2023)
   PUBMED   37070251
  REMARK    GeneRIF: O-GlcNAcylated LARP1 positively regulated by circCLNS1A
            facilitates hepatoblastoma progression through DKK4/beta-catenin
            signalling.
REFERENCE   3  (residues 1 to 203)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 203)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 203)
  AUTHORS   Beketova,E., Fang,S., Owens,J.L., Liu,S., Chen,X., Zhang,Q.,
            Asberry,A.M., Deng,X., Malola,J., Huang,J., Li,C., Pili,R.,
            Elzey,B.D., Ratliff,T.L., Wan,J. and Hu,C.D.
  TITLE     Protein Arginine Methyltransferase 5 Promotes pICln-Dependent
            Androgen Receptor Transcription in Castration-Resistant Prostate
            Cancer
  JOURNAL   Cancer Res 80 (22), 4904-4917 (2020)
   PUBMED   32999000
  REMARK    GeneRIF: Protein Arginine Methyltransferase 5 Promotes
            pICln-Dependent Androgen Receptor Transcription in
            Castration-Resistant Prostate Cancer.
REFERENCE   6  (residues 1 to 203)
  AUTHORS   Schwartz,R.S., Rybicki,A.C. and Nagel,R.L.
  TITLE     Molecular cloning and expression of a chloride channel-associated
            protein pICln in human young red blood cells: association with
            actin
  JOURNAL   Biochem J 327 (Pt 2) (Pt 2), 609-616 (1997)
   PUBMED   9359436
REFERENCE   7  (residues 1 to 203)
  AUTHORS   Bekri,S., Adelaide,J., Merscher,S., Grosgeorge,J., Caroli-Bosc,F.,
            Perucca-Lostanlen,D., Kelley,P.M., Pebusque,M.J., Theillet,C.,
            Birnbaum,D. and Gaudray,P.
  TITLE     Detailed map of a region commonly amplified at 11q13-->q14 in human
            breast carcinoma
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 125-131 (1997)
   PUBMED   9533029
REFERENCE   8  (residues 1 to 203)
  AUTHORS   Nagl,U.O., Erdel,M., Schmarda,A., Seri,M., Pinggera,G.M.,
            Gschwentner,M., Duba,C., Galietta,L.J., Deetjen,P., Utermann,G. and
            Paulmichl,M.
  TITLE     Chromosomal localization of the genes (CLNS1A and CLNS1B) coding
            for the swelling-dependent chloride channel ICln
  JOURNAL   Genomics 38 (3), 438-441 (1996)
   PUBMED   8975725
REFERENCE   9  (residues 1 to 203)
  AUTHORS   Buyse,G., de Greef,C., Raeymaekers,L., Droogmans,G., Nilius,B. and
            Eggermont,J.
  TITLE     The ubiquitously expressed pICln protein forms homomeric complexes
            in vitro
  JOURNAL   Biochem Biophys Res Commun 218 (3), 822-827 (1996)
   PUBMED   8579598
REFERENCE   10 (residues 1 to 203)
  AUTHORS   Anguita,J., Chalfant,M.L., Civan,M.M. and Coca-Prados,M.
  TITLE     Molecular cloning of the human volume-sensitive chloride
            conductance regulatory protein, pICln, from ocular ciliary
            epithelium
  JOURNAL   Biochem Biophys Res Commun 208 (1), 89-95 (1995)
   PUBMED   7887970
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA004269.1, AL530926.3,
            U53454.1, AA757599.1 and AP000609.5.
            
            Summary: This gene encodes a protein that functions in multiple
            regulatory pathways. The encoded protein complexes with numerous
            cytosolic proteins and performs diverse functions including
            regulation of small nuclear ribonucleoprotein biosynthesis,
            platelet activation and cytoskeletal organization. The protein is
            also found associated with the plasma membrane where it functions
            as a chloride current regulator. Pseudogenes of this gene are found
            on chromosomes 1, 4 and 6. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (b) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL530926.3, SRR12921934.3990813.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..203
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..203
                     /product="methylosome subunit pICln isoform b"
                     /note="chloride channel regulatory protein; reticulocyte
                     protein ICln; chloride ion current inducer protein;
                     methylosome subunit pICln; i(Cln); reticulocyte pICln;
                     chloride channel, nucleotide sensitive 1A; chloride
                     conductance regulatory protein ICln"
                     /calculated_mol_wt=22217
     Region          35..>103
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     CDS             1..203
                     /gene="CLNS1A"
                     /gene_synonym="CLCI; CLNS1B; ICln"
                     /coded_by="NM_001311200.2:81..692"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS81601.1"
                     /db_xref="GeneID:1207"
                     /db_xref="HGNC:HGNC:2080"
                     /db_xref="MIM:602158"
ORIGIN      
        1 msflksfppp gpaegllrqq pdteavlngk glgtgtlyia esrlswldgs glgfsleypt
       61 islhalsrdr sdclgehlyv mvnakfevea mftamcecqa lhpdpededs ddydgeeydv
      121 eaheqgqgdi ptfytyeegl shltaegqat lerlegmlsq svssqynmag vrtedsirdy
      181 edgmevdttp tvagqfedad vdh
//
LOCUS       NP_001336311             561 aa            linear   PRI 20-NOV-2025
DEFINITION  neutral amino acid transporter 9 isoform 1 [Homo sapiens].
ACCESSION   NP_001336311 XP_006714600
VERSION     NP_001336311.1
DBSOURCE    REFSEQ: accession NM_001349382.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Jansen,R.M., Peruzzo,R., Fromm,S.A., Yokom,A.L., Zoncu,R. and
            Hurley,J.H.
  TITLE     Structural basis for FLCN RagC GAP activation in MiT-TFE
            substrate-selective mTORC1 regulation
  JOURNAL   Sci Adv 8 (37), eadd2926 (2022)
   PUBMED   36103527
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Fromm,S.A., Lawrence,R.E. and Hurley,J.H.
  TITLE     Structural mechanism for amino acid-dependent Rag GTPase nucleotide
            state switching by SLC38A9
  JOURNAL   Nat Struct Mol Biol 27 (11), 1017-1023 (2020)
   PUBMED   32868926
  REMARK    GeneRIF: Structural mechanism for amino acid-dependent Rag GTPase
            nucleotide state switching by SLC38A9.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Rebsamen,M., Pochini,L., Stasyk,T., de Araujo,M.E., Galluccio,M.,
            Kandasamy,R.K., Snijder,B., Fauster,A., Rudashevskaya,E.L.,
            Bruckner,M., Scorzoni,S., Filipek,P.A., Huber,K.V., Bigenzahn,J.W.,
            Heinz,L.X., Kraft,C., Bennett,K.L., Indiveri,C., Huber,L.A. and
            Superti-Furga,G.
  TITLE     SLC38A9 is a component of the lysosomal amino acid sensing
            machinery that controls mTORC1
  JOURNAL   Nature 519 (7544), 477-481 (2015)
   PUBMED   25561175
  REMARK    GeneRIF: SLC38A9 is a physical and functional component of the
            amino acid sensing machinery that controls the activation of mTOR
REFERENCE   7  (residues 1 to 561)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   8  (residues 1 to 561)
  AUTHORS   Uchiyama,K., Takagi,T., Iwamoto,Y., Kondo,N., Okayama,T.,
            Yoshida,N., Kamada,K., Katada,K., Handa,O., Ishikawa,T., Yasuda,H.,
            Sakagami,J., Konishi,H., Yagi,N., Naito,Y. and Itoh,Y.
  TITLE     New genetic biomarkers predicting azathioprine blood concentrations
            in combination therapy with 5-aminosalicylic acid
  JOURNAL   PLoS One 9 (4), e95080 (2014)
   PUBMED   24762746
  REMARK    GeneRIF: SNPs within SLC38A9 are correlated with inflammatory bowel
            disease patients' 6-thioguanine nucleotide blood concentrations.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Schioth,H.B., Roshanbin,S., Hagglund,M.G. and Fredriksson,R.
  TITLE     Evolutionary origin of amino acid transporter families SLC32, SLC36
            and SLC38 and physiological, pathological and therapeutic aspects
  JOURNAL   Mol Aspects Med 34 (2-3), 571-585 (2013)
   PUBMED   23506890
  REMARK    Review article
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Januchowski,R., Zawierucha,P., Andrzejewska,M., Rucinski,M. and
            Zabel,M.
  TITLE     Microarray-based detection and expression analysis of ABC and SLC
            transporters in drug-resistant ovarian cancer cell lines
  JOURNAL   Biomed Pharmacother 67 (3), 240-245 (2013)
   PUBMED   23462296
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC371481.1, DB207931.1, AC016632.7, BC066891.1, AK075190.1 and
            AI580489.1.
            
            On Mar 15, 2017 this sequence version replaced XP_006714600.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR compared
            to variant 1. Variants 1 6, 7 and 8 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.417.1,
                                           SRR1803614.125553.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q11.2"
     Protein         1..561
                     /product="neutral amino acid transporter 9 isoform 1"
                     /note="putative sodium-coupled neutral amino acid
                     transporter 9; up-regulated in lung cancer 11"
                     /calculated_mol_wt=63645
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          115..556
                     /region_name="SLC5-6-like_sbd"
                     /note="Solute carrier families 5 and 6-like; solute
                     binding domain; cl00456"
                     /db_xref="CDD:444915"
     Site            120..140
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          129..134
                     /region_name="Important for arginine binding and amino
                     acid transport. /evidence=ECO:0000250|UniProtKB:Q08BA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            199..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            239
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            248
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            266
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            274
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            284..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            310..334
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            357..377
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            395..415
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            438..458
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          444..454
                     /region_name="CARC motif.
                     /evidence=ECO:0000269|PubMed:28336668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Region          457..463
                     /region_name="CRAC motif.
                     /evidence=ECO:0000269|PubMed:28336668"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            480..500
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            508..528
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     Site            541..561
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NBW4.2)"
     CDS             1..561
                     /gene="SLC38A9"
                     /gene_synonym="SNAT9; URLC11"
                     /coded_by="NM_001349382.1:471..2156"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS3968.1"
                     /db_xref="GeneID:153129"
                     /db_xref="HGNC:HGNC:26907"
                     /db_xref="MIM:616203"
ORIGIN      
        1 manmnsdsrh lgtsevdher dpgpmniqfe psdlrskrpf cieptnivnv nhviqrvsdh
       61 asamnkrihy ysrlttpadk aliapdhvvp apeecyvysp lgsayklqsy tegygkntsl
      121 vtifmiwntm mgtsilsipw gikqagfttg mcviilmgll tlyccyrvvk srtmmfsldt
      181 tsweypdvcr hyfgsfgqws sllfslvsli gamivywvlm snflfntgkf ifnfihhind
      241 tdtilstnns npvicpsags gghpdnssmi fyandtgaqq fekwwdksrt vpfylvglll
      301 pllnfkspsf fskfnilgtv svlyliflvt fkavrlgfhl efhwfiptef fvpeirfqfp
      361 qltgvltlaf fihnciitll knnkkqennv rdlciaymlv tltylyigvl vfasfpsppl
      421 skdcieqnfl dnfpssdtls fiarifllfq mmtvypllgy larvqllghi fgdiypsifh
      481 vlilnliivg agvimacfyp niggiirysg aacglafvfi ypsliyiisl hqeerltwpk
      541 lifhvfiiil gvanlivqff m
//
LOCUS       NP_005807                569 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell surface protein tactile isoform 2 precursor [Homo sapiens].
ACCESSION   NP_005807
VERSION     NP_005807.1
DBSOURCE    REFSEQ: accession NM_005816.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Zhang,Q., Huang,T., Li,X., Liu,G., Xian,L., Mao,X., Lin,T., Fu,C.,
            Chen,X., Liang,W., Zheng,Y., Zhao,Y., Lin,Q., Xu,X., Lin,Y., Bu,J.,
            Wu,C., Zhou,M. and Shen,E.
  TITLE     Prognostic impact of enhanced CD96 expression on NK cells by
            TGF-beta1 in AML
  JOURNAL   Int Immunopharmacol 141, 112958 (2024)
   PUBMED   39159564
  REMARK    GeneRIF: Prognostic impact of enhanced CD96 expression on NK cells
            by TGF-beta1 in AML.
REFERENCE   2  (residues 1 to 569)
  AUTHORS   ElMenshawy,N., El-Chennawi,F., Darwish,A., Foda,A., Atita,D. and
            Eissa,M.
  TITLE     CD44, CD90 and CD96 expression in immune thrombocytopenia purpura
            (ITP) patients
  JOURNAL   J Immunoassay Immunochem 44 (4), 326-337 (2023)
   PUBMED   36949573
  REMARK    GeneRIF: CD44, CD90 and CD96 expression in immune thrombocytopenia
            purpura (ITP) patients.
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Ohtsuki,S., Wang,C., Watanabe,R., Zhang,H., Akiyama,M., Bois,M.C.,
            Maleszewski,J.J., Warrington,K.J., Berry,G.J., Goronzy,J.J. and
            Weyand,C.M.
  TITLE     Deficiency of the CD155-CD96 immune checkpoint controls IL-9
            production in giant cell arteritis
  JOURNAL   Cell Rep Med 4 (4), 101012 (2023)
   PUBMED   37075705
  REMARK    GeneRIF: Deficiency of the CD155-CD96 immune checkpoint controls
            IL-9 production in giant cell arteritis.
REFERENCE   4  (residues 1 to 569)
  AUTHORS   Li,J., Xia,Q., Di,C., Li,C., Si,H., Zhou,B., Yu,S., Li,Y.,
            Huang,J., Lu,Y., Huang,M., Liang,H., Liu,X. and Zhao,Q.
  TITLE     Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and Cancer
            Stemness by Regulating Mitochondrial Fatty Acid beta-Oxidation
  JOURNAL   Adv Sci (Weinh) 10 (7), e2202956 (2023)
   PUBMED   36581470
  REMARK    GeneRIF: Tumor Cell-Intrinsic CD96 Mediates Chemoresistance and
            Cancer Stemness by Regulating Mitochondrial Fatty Acid
            beta-Oxidation.
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Feng,S., Isayev,O., Werner,J. and Bazhin,A.V.
  TITLE     CD96 as a Potential Immune Regulator in Cancers
  JOURNAL   Int J Mol Sci 24 (2), 1303 (2023)
   PUBMED   36674817
  REMARK    GeneRIF: CD96 as a Potential Immune Regulator in Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Hosen,N., Park,C.Y., Tatsumi,N., Oji,Y., Sugiyama,H., Gramatzki,M.,
            Krensky,A.M. and Weissman,I.L.
  TITLE     CD96 is a leukemic stem cell-specific marker in human acute myeloid
            leukemia
  JOURNAL   Proc Natl Acad Sci U S A 104 (26), 11008-11013 (2007)
   PUBMED   17576927
  REMARK    GeneRIF: CD96 is a cell surface marker present on many acute
            myeloid leukemia leukemic stem cells
REFERENCE   7  (residues 1 to 569)
  AUTHORS   Fuchs,A., Cella,M., Giurisato,E., Shaw,A.S. and Colonna,M.
  TITLE     Cutting edge: CD96 (tactile) promotes NK cell-target cell adhesion
            by interacting with the poliovirus receptor (CD155)
  JOURNAL   J Immunol 172 (7), 3994-3998 (2004)
   PUBMED   15034010
  REMARK    GeneRIF: CD96 promotes natural killer (NK) cell adhesion to target
            cells expressing the poliovirus receptor (PVR), stimulates
            cytotoxicity of activated NK cells, and mediates acquisition of PVR
            from target cells.
REFERENCE   8  (residues 1 to 569)
  AUTHORS   Gramatzki,M., Ludwig,W.D., Burger,R., Moos,P., Rohwer,P.,
            Grunert,C., Sendler,A., Kalden,J.R., Andreesen,R., Henschke,F. and
            Moldenhauer,G.
  TITLE     Antibodies TC-12 ('unique') and TH-111 (CD96) characterize T-cell
            acute lymphoblastic leukemia and a subgroup of acute myeloid
            leukemia
  JOURNAL   Exp Hematol 26 (13), 1209-1214 (1998)
   PUBMED   9845376
REFERENCE   9  (residues 1 to 569)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   10 (residues 1 to 569)
  AUTHORS   Wang,P.L., O'Farrell,S., Clayberger,C. and Krensky,A.M.
  TITLE     Identification and molecular cloning of tactile. A novel human T
            cell activation antigen that is a member of the Ig gene superfamily
  JOURNAL   J Immunol 148 (8), 2600-2608 (1992)
   PUBMED   1313846
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092916.6, AL833681.1 and
            AC055748.21.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the
            immunoglobulin superfamily. It is a type I membrane protein. The
            protein may play a role in the adhesive interactions of activated T
            and NK cells during the late phase of the immune response. It may
            also function in antigen presentation. Alternative splicing
            generates multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform 2), compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315237.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352690.9/ ENSP00000342040.3
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.13-q13.2"
     Protein         1..569
                     /product="T-cell surface protein tactile isoform 2
                     precursor"
                     /note="T-cell surface protein tactile; T cell activation,
                     increased late expression; cell surface antigen CD96; t
                     cell-activated increased late expression protein"
                     /calculated_mol_wt=61258
     sig_peptide     1..21
                     /calculated_mol_wt=2648
     mat_peptide     22..569
                     /product="T-cell surface protein tactile isoform 2"
                     /calculated_mol_wt=61258
     Region          27..126
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          41..45
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409383"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409383"
     Region          101..105
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409383"
     Region          115..120
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409383"
     Region          347..>499
                     /region_name="COG5099"
                     /note="RNA-binding protein of the Puf family,
                     translational repressor [Translation, ribosomal structure
                     and biogenesis]"
                     /db_xref="CDD:227430"
     CDS             1..569
                     /gene="CD96"
                     /gene_synonym="TACTILE"
                     /coded_by="NM_005816.5:53..1762"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS2958.1"
                     /db_xref="GeneID:10225"
                     /db_xref="HGNC:HGNC:16892"
                     /db_xref="MIM:606037"
ORIGIN      
        1 mekkwkycav yyiiqihfvk gvwektvnte envyatlgsd vnltcqtqtv gffvqmqwsk
       61 vtnkidliav yhpqygfyca ygrpceslvt ftetpengsk wtlhlrnmsc svsgryecml
      121 vlypegiqtk iynlliqthv tadewnsnht ieieinqtle ipcfqnsssk isseftyaws
      181 vedngtqetl isqnhlisns tllkdrvklg tdyrlhlspv qifddgrkfs chirvgpnki
      241 lrssttvkvf akpeipvive nnstdvlver rftcllknvf pkanitwfid gsflhdekeg
      301 iyitneerkg kdgflelksv ltrvhsnkpa qsdnltiwcm alspvpgnkv wnissekitf
      361 llgseisstd pplsvtestl dtqpspassv sparypatss vtlvdvsalr pnttpqpsns
      421 smttrgfnyp wtssgtdtkk svsripsety ssspsgagst lhdnvftsta rafsevptta
      481 ngstktnhvh itgivvnkpk dgmswpviva allfccmilf glgvrkwcqy qkeimerppp
      541 fkpppppiky tciqepnesd lpyhemetl
//
LOCUS       NP_006618                220 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p29 [Homo sapiens].
ACCESSION   NP_006618
VERSION     NP_006618.1
DBSOURCE    REFSEQ: accession NM_006627.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   4  (residues 1 to 220)
  AUTHORS   Shastrula,P.K., Lund,P.J., Garcia,B.A. and Janicki,S.M.
  TITLE     Rpp29 regulates histone H3.3 chromatin assembly through
            transcriptional mechanisms
  JOURNAL   J Biol Chem 293 (32), 12360-12377 (2018)
   PUBMED   29921582
  REMARK    GeneRIF: Rpp29 regulates H3.3-mediated epigenetic mechanisms by
            processing a transcribed signal that recruits H3.3 to its
            incorporation sites
REFERENCE   5  (residues 1 to 220)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 220)
  AUTHORS   Mann,H., Ben-Asouli,Y., Schein,A., Moussa,S. and Jarrous,N.
  TITLE     Eukaryotic RNase P: role of RNA and protein subunits of a
            primordial catalytic ribonucleoprotein in RNA-based catalysis
  JOURNAL   Mol Cell 12 (4), 925-935 (2003)
   PUBMED   14580343
REFERENCE   7  (residues 1 to 220)
  AUTHORS   Jiang,T., Guerrier-Takada,C. and Altman,S.
  TITLE     Protein-RNA interactions in the subunits of human nuclear RNase P
  JOURNAL   RNA 7 (7), 937-941 (2001)
   PUBMED   11455963
REFERENCE   8  (residues 1 to 220)
  AUTHORS   Jarrous,N., Wolenski,J.S., Wesolowski,D., Lee,C. and Altman,S.
  TITLE     Localization in the nucleolus and coiled bodies of protein subunits
            of the ribonucleoprotein ribonuclease P
  JOURNAL   J Cell Biol 146 (3), 559-572 (1999)
   PUBMED   10444065
REFERENCE   9  (residues 1 to 220)
  AUTHORS   van Eenennaam,H., Pruijn,G.J. and van Venrooij,W.J.
  TITLE     hPop4: a new protein subunit of the human RNase MRP and RNase P
            ribonucleoprotein complexes
  JOURNAL   Nucleic Acids Res 27 (12), 2465-2472 (1999)
   PUBMED   10352175
REFERENCE   10 (residues 1 to 220)
  AUTHORS   Jarrous,N., Eder,P.S., Wesolowski,D. and Altman,S.
  TITLE     Rpp14 and Rpp29, two protein subunits of human ribonuclease P
  JOURNAL   RNA 5 (2), 153-157 (1999)
   PUBMED   10024167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010505.6, Y18863.1 and
            BU727144.1.
            
            Summary: This gene encodes one of the protein subunits of the small
            nucleolar ribonucleoprotein complexes: the endoribonuclease for
            mitochondrial RNA processing complex and the ribonuclease P
            complex. The encoded protein is localized to the nucleus and
            associates directly with the RNA component of these complexes. This
            protein is involved in processing of precursor RNAs. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes processing of precursor 4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.220549.1,
                                           SRR1803617.25698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000585603.6/ ENSP00000465213.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..220
                     /product="ribonuclease P protein subunit p29"
                     /EC_number="3.1.26.5"
                     /note="hPOP4; POP4 homolog, ribonuclease P/MRP subunit"
                     /calculated_mol_wt=25294
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95707.2)"
     Region          128..210
                     /region_name="RNase_P-MRP_p29"
                     /note="Ribonuclease P/MRP, subunit p29; pfam01868"
                     /db_xref="CDD:460367"
     CDS             1..220
                     /gene="POP4"
                     /gene_synonym="RPP29"
                     /coded_by="NM_006627.3:37..699"
                     /db_xref="CCDS:CCDS12416.1"
                     /db_xref="GeneID:10775"
                     /db_xref="HGNC:HGNC:30081"
                     /db_xref="MIM:606114"
ORIGIN      
        1 mksviyhals qkeandsdvq psgaqraeaf vraflkrstp rmspqaredq lqrkavvley
       61 ftrhkrkekk kkakglsarq rrelrlfdik peqqryslfl plhelwkqyi rdlcsglkpd
      121 tqpqmiqakl lkadlhgaii svtkskcpsy vgitgillqe tkhifkiitk edrlkvipkl
      181 ncvftvetdg fisyiygskf qlrssersak kfkakgtidl
//
LOCUS       NP_808227                391 aa            linear   PRI 20-NOV-2025
DEFINITION  casein kinase II subunit alpha isoform a [Homo sapiens].
ACCESSION   NP_808227
VERSION     NP_808227.1
DBSOURCE    REFSEQ: accession NM_177559.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Goel,H. and O'Donnell,S.
  TITLE     Inherited loss of function variant in CSNK2A1: the oldest reported
            cases of Okur-Chung syndrome in a single family
  JOURNAL   Clin Dysmorphol 33 (3), 121-124 (2024)
   PUBMED   38818820
  REMARK    GeneRIF: Inherited loss of function variant in CSNK2A1: the oldest
            reported cases of Okur-Chung syndrome in a single family.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Ampofo,E., Pack,M., Wrublewsky,S., Boewe,A.S., Spigelman,A.F.,
            Koch,H., MacDonald,P.E., Laschke,M.W., Montenarh,M. and Gotz,C.
  TITLE     CK2 activity is crucial for proper glucagon expression
  JOURNAL   Diabetologia 67 (7), 1368-1385 (2024)
   PUBMED   38503901
  REMARK    GeneRIF: CK2 activity is crucial for proper glucagon expression.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Liu,Z.D., Shi,Y.H., Xu,Q.C., Zhao,G.Y., Zhu,Y.Q., Li,F.X., Ma,M.J.,
            Ye,J.Y., Huang,X.T., Wang,X.Y., Xu,X., Wang,J.Q., Zhao,W. and
            Yin,X.Y.
  TITLE     CSNK2A1 confers gemcitabine resistance to pancreatic ductal
            adenocarcinoma via inducing autophagy
  JOURNAL   Cancer Lett 585, 216640 (2024)
   PUBMED   38290659
  REMARK    GeneRIF: CSNK2A1 confers gemcitabine resistance to pancreatic
            ductal adenocarcinoma via inducing autophagy.
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Nan,H., Chu,M., Zhang,J., Jiang,D., Wang,Y. and Wu,L.
  TITLE     Okur-Chung neurodevelopmental syndrome: Implications for phenotype
            and genotype expansion
  JOURNAL   Mol Genet Genomic Med 12 (3), e2398 (2024)
   PUBMED   38444259
  REMARK    GeneRIF: Okur-Chung neurodevelopmental syndrome: Implications for
            phenotype and genotype expansion.
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Chung,W. and Okur,V.
  TITLE     Okur-Chung Neurodevelopmental Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   35679446
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Hagiwara,T., Nakaya,K., Nakamura,Y., Nakajima,H., Nishimura,S. and
            Taya,Y.
  TITLE     Specific phosphorylation of the acidic central region of the N-myc
            protein by casein kinase II
  JOURNAL   Eur J Biochem 209 (3), 945-950 (1992)
   PUBMED   1425701
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Russo,G.L., Vandenberg,M.T., Yu,I.J., Bae,Y.S., Franza,B.R. Jr. and
            Marshak,D.R.
  TITLE     Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the
            HeLa cell division cycle
  JOURNAL   J Biol Chem 267 (28), 20317-20325 (1992)
   PUBMED   1400350
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Lin,A., Frost,J., Deng,T., Smeal,T., al-Alawi,N., Kikkawa,U.,
            Hunter,T., Brenner,D. and Karin,M.
  TITLE     Casein kinase II is a negative regulator of c-Jun DNA binding and
            AP-1 activity
  JOURNAL   Cell 70 (5), 777-789 (1992)
   PUBMED   1516134
  REMARK    Erratum:[Cell. 1992 Nov 27;71(5):887. PMID: 1423636]
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Sacks,D.B., Davis,H.W., Crimmins,D.L. and McDonald,J.M.
  TITLE     Insulin-stimulated phosphorylation of calmodulin
  JOURNAL   Biochem J 286 (Pt 1) (Pt 1), 211-216 (1992)
   PUBMED   1520270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU132198.1, M55265.1,
            BC053532.1 and AL049761.11.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Casein kinase II is a serine/threonine protein kinase that
            phosphorylates acidic proteins such as casein. It is involved in
            various cellular processes, including cell cycle control,
            apoptosis, and circadian rhythm. The kinase exists as a tetramer
            and is composed of an alpha, an alpha-prime, and two beta subunits.
            The alpha subunits contain the catalytic activity while the beta
            subunits undergo autophosphorylation. The protein encoded by this
            gene represents the alpha subunit. Multiple transcript variants
            encoding different protein isoforms have been found for this gene.
            [provided by RefSeq, Apr 2018].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a). Variants 1, 2, 4 and 5 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.35161.1,
                                           SRR1803613.132695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217244.9/ ENSP00000217244.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..391
                     /product="casein kinase II subunit alpha isoform a"
                     /EC_number="2.7.11.1"
                     /note="CK2 catalytic subunit alpha; protein kinase CK2;
                     casein kinase II alpha 1 subunit; casein kinase II alpha 1
                     polypeptide pseudogene; casein kinase 2, alpha 1
                     polypeptide"
                     /calculated_mol_wt=45013
     Region          20..325
                     /region_name="STKc_CK2_alpha"
                     /note="Catalytic subunit (alpha) of the Serine/Threonine
                     Kinase, Casein Kinase 2; cd14132"
                     /db_xref="CDD:271034"
     Site            order(36,39..41,67,69,101,103..104,110)
                     /site_type="other"
                     /note="allosteric inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..42,50,54,103)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Site            order(36..37,39..41,57,59,103)
                     /site_type="other"
                     /note="CK2 beta interface [polypeptide binding]"
                     /db_xref="CDD:271034"
     Region          36..41
                     /region_name="Interaction with beta subunit.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P68400.1)"
     Site            order(45..49,53,66,68,80,95,113..116,120,122..123,156,158,
                     160..161,163,175,178,189,191..194,196,235)
                     /site_type="active"
                     /db_xref="CDD:271034"
     Site            order(47..48,50..51,53,66,68,95,113..114,116,160..161,163,
                     174..175)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271034"
     Site            order(80,122,156,158,178,189,191..194,196,235)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271034"
     Site            order(174..184,189..196)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271034"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7592773,
                     ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P68400.1)"
     CDS             1..391
                     /gene="CSNK2A1"
                     /gene_synonym="CK2A1; Cka1; Cka2; CKII; OCNDS"
                     /coded_by="NM_177559.3:346..1521"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13003.1"
                     /db_xref="GeneID:1457"
                     /db_xref="HGNC:HGNC:2457"
                     /db_xref="MIM:115440"
ORIGIN      
        1 msgpvpsrar vytdvnthrp reywdyeshv vewgnqddyq lvrklgrgky sevfeainit
       61 nnekvvvkil kpvkkkkikr eikilenlrg gpniitladi vkdpvsrtpa lvfehvnntd
      121 fkqlyqtltd ydirfymyei lkaldychsm gimhrdvkph nvmidhehrk lrlidwglae
      181 fyhpgqeynv rvasryfkgp ellvdyqmyd ysldmwslgc mlasmifrke pffhghdnyd
      241 qlvriakvlg tedlydyidk ynieldprfn dilgrhsrkr werfvhsenq hlvspealdf
      301 ldkllrydhq srltareame hpyfytvvkd qarmgsssmp ggstpvssan mmsgissvpt
      361 psplgplags pviaaanplg mpvpaaagaq q
//
LOCUS       NP_001274176            1286 aa            linear   PRI 20-NOV-2025
DEFINITION  recQ-like DNA helicase BLM isoform 2 [Homo sapiens].
ACCESSION   NP_001274176
VERSION     NP_001274176.1
DBSOURCE    REFSEQ: accession NM_001287247.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1286)
  AUTHORS   Silva,J.P.L., Donaires,F.S., Gutierrez-Rodrigues,F., Martins,D.J.,
            Carvalho,V.S., Santana,B.A., Cunha,R.L.G., Kajigaya,S.,
            Menck,C.F.M., Young,N.S., Kjeldsen,E. and Calado,R.T.
  TITLE     RecQ helicase expression in patients with telomeropathies
  JOURNAL   Mol Biol Rep 51 (1), 754 (2024)
   PUBMED   38874681
  REMARK    GeneRIF: RecQ helicase expression in patients with telomeropathies.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1286)
  AUTHORS   Tsukada,K., Jones,S.E., Bannister,J., Durin,M.A., Vendrell,I.,
            Fawkes,M., Fischer,R., Kessler,B.M., Chapman,J.R. and
            Blackford,A.N.
  TITLE     BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint
            DNA molecule resolution
  JOURNAL   Mol Cell 84 (4), 640-658 (2024)
   PUBMED   38266639
  REMARK    GeneRIF: BLM and BRCA1-BARD1 coordinate complementary mechanisms of
            joint DNA molecule resolution.
REFERENCE   3  (residues 1 to 1286)
  AUTHORS   Liu,S., Atkinson,E., Paulucci-Holthauzen,A. and Wang,B.
  TITLE     A CK2 and SUMO-dependent, PML NB-involved regulatory mechanism
            controlling BLM ubiquitination and G-quadruplex resolution
  JOURNAL   Nat Commun 14 (1), 6111 (2023)
   PUBMED   37777511
  REMARK    GeneRIF: A CK2 and SUMO-dependent, PML NB-involved regulatory
            mechanism controlling BLM ubiquitination and G-quadruplex
            resolution.
            Erratum:[Nat Commun. 2024 Feb 5;15(1):1077. doi:
            10.1038/s41467-024-45551-1. PMID: 38316763]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1286)
  AUTHORS   Danino,Y.M., Molitor,L., Rosenbaum-Cohen,T., Kaiser,S., Cohen,Y.,
            Porat,Z., Marmor-Kollet,H., Katina,C., Savidor,A., Rotkopf,R.,
            Ben-Isaac,E., Golani,O., Levin,Y., Monchaud,D., Hickson,I.D. and
            Hornstein,E.
  TITLE     BLM helicase protein negatively regulates stress granule formation
            through unwinding RNA G-quadruplex structures
  JOURNAL   Nucleic Acids Res 51 (17), 9369-9384 (2023)
   PUBMED   37503837
  REMARK    GeneRIF: BLM helicase protein negatively regulates stress granule
            formation through unwinding RNA G-quadruplex structures.
REFERENCE   5  (residues 1 to 1286)
  AUTHORS   Foucault,F., Vaury,C., Barakat,A., Thibout,D., Planchon,P.,
            Jaulin,C., Praz,F. and Amor-Gueret,M.
  TITLE     Characterization of a new BLM mutation associated with a
            topoisomerase II alpha defect in a patient with Bloom's syndrome
  JOURNAL   Hum Mol Genet 6 (9), 1427-1434 (1997)
   PUBMED   9285778
REFERENCE   6  (residues 1 to 1286)
  AUTHORS   Ellis,N.A., Groden,J., Ye,T.Z., Straughen,J., Lennon,D.J.,
            Ciocci,S., Proytcheva,M. and German,J.
  TITLE     The Bloom's syndrome gene product is homologous to RecQ helicases
  JOURNAL   Cell 83 (4), 655-666 (1995)
   PUBMED   7585968
REFERENCE   7  (residues 1 to 1286)
  AUTHORS   German,J., Roe,A.M., Leppert,M.F. and Ellis,N.A.
  TITLE     Bloom syndrome: an analysis of consanguineous families assigns the
            locus mutated to chromosome band 15q26.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6669-6673 (1994)
   PUBMED   8022833
REFERENCE   8  (residues 1 to 1286)
  AUTHORS   Langer,K., Cunniff,C.M. and Kucine,N.
  TITLE     Bloom Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301572
REFERENCE   9  (residues 1 to 1286)
  AUTHORS   Turner,J.T., Brzezinski,J. and Dome,J.S.
  TITLE     Wilms Tumor Predisposition
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301471
REFERENCE   10 (residues 1 to 1286)
  AUTHORS   McDaniel,L.D. and Schultz,R.A.
  TITLE     Elevated sister chromatid exchange phenotype of Bloom syndrome
            cells is complemented by human chromosome 15
  JOURNAL   Proc Natl Acad Sci U S A 89 (17), 7968-7972 (1992)
   PUBMED   1518822
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD707743.1, BC062697.1,
            BC115028.1, BC101567.1, DB520927.1 and AC124248.6.
            
            Summary: The Bloom syndrome is an autosomal recessive disorder
            characterized by growth deficiency, microcephaly and
            immunodeficiency among others. It is caused by homozygous or
            compound heterozygous mutation in the gene encoding DNA helicase
            RecQ protein on chromosome 15q26. This Bloom-associated helicase
            unwinds a variety of DNA substrates including Holliday junction,
            and is involved in several pathways contributing to the maintenance
            of genome stability. Identification of pathogenic Bloom variants is
            required for heterozygote testing in at-risk families. [provided by
            RefSeq, May 2020].
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons in the 3' coding region compared to variant 1. The resulting
            protein (isoform 2) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC115028.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..1286
                     /product="recQ-like DNA helicase BLM isoform 2"
                     /EC_number="5.6.2.4"
                     /note="bloom syndrome protein; recQ protein-like 3; Bloom
                     syndrome RecQ like helicase; DNA helicase, RecQ-like type
                     2; Bloom syndrome, RecQ helicase-like; recQ-like DNA
                     helicase BLM; DNA 3'-5' helicase BLM"
                     /calculated_mol_wt=144341
     Region          1..368
                     /region_name="BLM_N"
                     /note="N-terminal region of Bloom syndrome protein;
                     pfam16202"
                     /db_xref="CDD:465064"
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          203..227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          250..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          301..600
                     /region_name="Necessary for interaction with SPIDR.
                     /evidence=ECO:0000269|PubMed:23509288"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          362..414
                     /region_name="Necessary for dimerization and
                     homooligomerization.
                     /evidence=ECO:0000269|PubMed:28228481"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          372..412
                     /region_name="BDHCT"
                     /note="BDHCT (NUC031) domain; pfam08072"
                     /db_xref="CDD:462356"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          425..647
                     /region_name="BDHCT_assoc"
                     /note="BDHCT-box associated domain on Bloom syndrome
                     protein; pfam16204"
                     /db_xref="CDD:465065"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          657..1123
                     /region_name="recQ_fam"
                     /note="ATP-dependent DNA helicase, RecQ family; TIGR00614"
                     /db_xref="CDD:129701"
     Site            717
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          795..798
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            808
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Site            863
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P54132.1)"
     Region          870..873
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:25901030"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          897..899
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            920
                     /site_type="other"
                     /note="3' overhang DNA-binding, via amide nitrogen.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Site            946
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Site            968
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     Region          1000..1003
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Region          <1109..1161
                     /region_name="HRDC"
                     /note="HRDC domain; cl02578"
                     /db_xref="CDD:470625"
     Region          1110..1112
                     /region_name="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M"
                     /note="propagated from UniProtKB/Swiss-Prot (P54132.1)"
     Site            1110
                     /site_type="other"
                     /note="3' overhang DNA-binding.
                     /evidence=ECO:0000269|PubMed:24816114,
                     ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ,
                     ECO:0007744|PDB:4O3M; propagated from UniProtKB/Swiss-Prot
                     (P54132.1)"
     CDS             1..1286
                     /gene="BLM"
                     /gene_synonym="BS; MGRISCE1; RECQ2; RECQL2; RECQL3"
                     /coded_by="NM_001287247.2:100..3960"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73782.1"
                     /db_xref="GeneID:641"
                     /db_xref="HGNC:HGNC:1058"
                     /db_xref="MIM:604610"
ORIGIN      
        1 maavpqnnlq eqlerhsart lnnklslskp kfsgftfkkk tssdnnvsvt nvsvaktpvl
       61 rnkdvnvted fsfseplpnt tnqqrvkdff knapagqetq rggsksllpd flqtpkevvc
      121 ttqntptvkk srdtalkkle fssspdslst indwddmddf dtsetsksfv tppqshfvrv
      181 staqkskkgk rnffkaqlyt tntvktdlpp psseseqidl teeqkddsew lssdvicidd
      241 gpiaevhine daqesdslkt hlederdnse kkknleeael hstekvpcie fddddydtdf
      301 vppspeeiis assssskcls tlkdldtsdr kedvlstskd llskpekmsm qelnpetstd
      361 cdarqislqq qlihvmehic klidtipddk lklldcgnel lqqrnirrkl ltevdfnksd
      421 asllgslwry rpdsldgpme gdscptgnsm kelnfshlps nsvspgdcll tttlgktgfs
      481 atrknlferp lfnthlqksf vssnwaetpr lgkknessyf pgnvltstav kdqnkhtasi
      541 ndleretqps ydidnfdidd fdddddwedi mhnlaaskss taayqpikeg rpiksvserl
      601 ssaktdclpv sstaqninfs esiqnytdks aqnlasrnlk herfqslsfp htkemmkifh
      661 kkfglhnfrt nqleainaal lgedcfilmp tgggkslcyq lpacvspgvt vvisplrsli
      721 vdqvqkltsl dipatyltgd ktdseatniy lqlskkdpii kllyvtpeki casnrlistl
      781 enlyerklla rfvideahcv sqwghdfrqd ykrmnmlrqk fpsvpvmalt atanprvqkd
      841 iltqlkilrp qvfsmsfnrh nlkyyvlpkk pkkvafdcle wirkhhpyds giiyclsrre
      901 cdtmadtlqr dglaalayha glsdsardev qqkwinqdgc qvicatiafg mgidkpdvrf
      961 vihaslpksv egyyqesgra grdgeishcl lfytyhdvtr lkrlimmekd gnhhtrethf
     1021 nnlysmvhyc enitecrriq llayfgengf npdfckkhpd vscdnccktk dyktrdvtdd
     1081 vksivrfvqe hsssqgmrni khvgpsgrft mnmlvdifle slssdpevll qidgvtedkl
     1141 ekygaevisv lqkysewtsp aedsspgisl sssrgpgrsa aeeldeeipv sshyfasktr
     1201 nerkrkkmpa sqrskrrkta ssgskakggs atcrkisskt ksssiigsss ashtsqatsg
     1261 ansklgimap pkpinrpflk psyafs
//
LOCUS       NP_055520               1966 aa            linear   PRI 20-NOV-2025
DEFINITION  dedicator of cytokinesis protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_055520
VERSION     NP_055520.3
DBSOURCE    REFSEQ: accession NM_014705.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1966)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1966)
  AUTHORS   Wu,C., Wang,C., Xiao,B., Li,S., Sheng,Y., Wang,Q., Tao,J., Zhang,Y.
            and Jiang,X.
  TITLE     Integration analysis of lncRNA and mRNA expression data identifies
            DOCK4 as a potential biomarker for elderly osteoporosis
  JOURNAL   BMC Med Genomics 17 (1), 70 (2024)
   PUBMED   38443923
  REMARK    GeneRIF: Integration analysis of lncRNA and mRNA expression data
            identifies DOCK4 as a potential biomarker for elderly osteoporosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1966)
  AUTHORS   Herbst,C., Bothe,V., Wegler,M., Axer-Schaefer,S.,
            Audebert-Bellanger,S., Gecz,J., Cogne,B., Feldman,H.B.,
            Horn,A.H.C., Hurst,A.C.E., Kelly,M.A., Kruer,M.C., Kurolap,A.,
            Laquerriere,A., Li,M., Mark,P.R., Morawski,M., Nizon,M.,
            Pastinen,T., Polster,T., Saugier-Veber,P., SeSong,J., Sticht,H.,
            Stieler,J.T., Thifffault,I., van Eyk,C.L., Marcorelles,P.,
            Vezain-Mouchard,M., Abou Jamra,R. and Oppermann,H.
  TITLE     Heterozygous loss-of-function variants in DOCK4 cause
            neurodevelopmental delay and microcephaly
  JOURNAL   Hum Genet 143 (3), 455-469 (2024)
   PUBMED   38526744
  REMARK    GeneRIF: Heterozygous loss-of-function variants in DOCK4 cause
            neurodevelopmental delay and microcephaly.
REFERENCE   4  (residues 1 to 1966)
  AUTHORS   Xu,X., He,B., Zeng,J., Yin,J., Wang,X., Luo,X., Liang,C., Luo,S.,
            Yan,H., Xiong,S., Tan,Z., Lv,D., Dai,Z., Lin,Z., Lin,J., Ye,X.,
            Chen,R., Li,Y., Wang,Y., Chen,W., Luo,Z., Li,K. and Ma,G.
  TITLE     Genetic variations in DOCK4 contribute to schizophrenia
            susceptibility in a Chinese cohort: A genetic neuroimaging study
  JOURNAL   Behav Brain Res 443, 114353 (2023)
   PUBMED   36822513
  REMARK    GeneRIF: Genetic variations in DOCK4 contribute to schizophrenia
            susceptibility in a Chinese cohort: A genetic neuroimaging study.
REFERENCE   5  (residues 1 to 1966)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1966)
  AUTHORS   Hiramoto,K., Negishi,M. and Katoh,H.
  TITLE     Dock4 is regulated by RhoG and promotes Rac-dependent cell
            migration
  JOURNAL   Exp Cell Res 312 (20), 4205-4216 (2006)
   PUBMED   17027967
  REMARK    GeneRIF: Taken together, these results suggest that Dock4 plays an
            important role in the regulation of cell migration through
            activation of Rac1, and that RhoG is a key upstream regulator for
            Dock4.
REFERENCE   7  (residues 1 to 1966)
  AUTHORS   Yan,D., Li,F., Hall,M.L., Sage,C., Hu,W.H., Giallourakis,C.,
            Upadhyay,G., Ouyang,X.M., Du,L.L., Bethea,J.R., Chen,Z.Y.,
            Yajnik,V. and Liu,X.Z.
  TITLE     An isoform of GTPase regulator DOCK4 localizes to the stereocilia
            in the inner ear and binds to harmonin (USH1C)
  JOURNAL   J Mol Biol 357 (3), 755-764 (2006)
   PUBMED   16464467
REFERENCE   8  (residues 1 to 1966)
  AUTHORS   Liang,H., Castro,P.D., Ma,J. and Nagarajan,L.
  TITLE     Finer delineation and transcript map of the 7q31 locus deleted in
            myeloid neoplasms
  JOURNAL   Cancer Genet Cytogenet 162 (2), 151-159 (2005)
   PUBMED   16213364
REFERENCE   9  (residues 1 to 1966)
  AUTHORS   Yajnik,V., Paulding,C., Sordella,R., McClatchey,A.I., Saito,M.,
            Wahrer,D.C., Reynolds,P., Bell,D.W., Lake,R., van den Heuvel,S.,
            Settleman,J. and Haber,D.A.
  TITLE     DOCK4, a GTPase activator, is disrupted during tumorigenesis
  JOURNAL   Cell 112 (5), 673-684 (2003)
   PUBMED   12628187
REFERENCE   10 (residues 1 to 1966)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA646980.1, AY233380.1,
            AB018259.2, BM545903.1 and BM126591.1.
            
            On Apr 14, 2006 this sequence version replaced NP_055520.2.
            
            Summary: This gene is a member of the dedicator of cytokinesis
            (DOCK) family and encodes a protein with a DHR-1 (CZH-1) domain, a
            DHR-2 (CZH-2) domain and an SH3 domain. This membrane-associated,
            cytoplasmic protein functions as a guanine nucleotide exchange
            factor and is involved in regulation of adherens junctions between
            cells. Mutations in this gene have been associated with ovarian,
            prostate, glioma, and colorectal cancers. Alternatively spliced
            variants which encode different protein isoforms have been
            described, but only one has been fully characterized. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.32565.1, BC117688.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1966
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1966
                     /product="dedicator of cytokinesis protein 4 isoform 1"
                     /note="dedicator of cytokinesis protein 4"
                     /calculated_mol_wt=225076
     Region          10..65
                     /region_name="SH3_DOCK4_B"
                     /note="Src Homology 3 domain of Class B Dedicator of
                     Cytokinesis 4; cd12049"
                     /db_xref="CDD:212982"
     Site            order(12..16,23,28..30,32,36..37,41..42,44,52,54,56,58,
                     60..61,63,65)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212982"
     Site            order(15,17,20,24,41..42,58,60..61)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212982"
     Region          73..392
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          400..584
                     /region_name="C2_Dock-B"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class B proteins; cd08695"
                     /db_xref="CDD:176077"
     Region          1197..1587
                     /region_name="DHR2_DOCK4"
                     /note="Dock Homology Region 2, a GEF domain, of Class B
                     Dedicator of Cytokinesis 4; cd11705"
                     /db_xref="CDD:212578"
     Site            order(1277,1287,1289..1290,1292..1293,1296..1297,
                     1299..1300,1303..1304)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212578"
     Site            order(1315,1317,1341,1344..1347,1349..1350,1363..1365,
                     1382..1384,1418..1421,1432..1433,1436,1438,1475..1476,
                     1479,1499..1500,1502..1503,1506..1508,1511..1513,
                     1516..1517,1520,1550,1572,1575)
                     /site_type="other"
                     /note="putative Rac/Cdc42 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212578"
     Site            1511..1516
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212578"
     Site            1599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1607
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1618
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1620
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1631
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1648..1729
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1742..1966
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1788..1794
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     CDS             1..1966
                     /gene="DOCK4"
                     /coded_by="NM_014705.4:262..6162"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47688.1"
                     /db_xref="GeneID:9732"
                     /db_xref="HGNC:HGNC:19192"
                     /db_xref="MIM:607679"
ORIGIN      
        1 mwipteheky gvviasfrgt vpyglsleig dtvqilekcd gwyrgfalkn pnikgifpss
       61 yvhlknacvk nkgqfemvip tedsvitemt stlrdwgtmw kqlyvrnegd lfhrlwhimn
      121 eildlrrqvl vghlthdrmk dvkrhitarl dwgneqlgld lvprkeyamv dpedisitel
      181 yrlmehrhrk kdtpvqassh hlfvqmkslm csnlgeelev ifslfdsken rpiserfflr
      241 lnrnglpkap dkperhcslf vdlgsselrk diyitvhiir igrmgagekk nacsvqyrrp
      301 fgcavlsiad lltgetkddl ilkvymcnte sewyqiheni ikklnarynl tgsnaglavs
      361 lqllhgdieq irreyssvfs hgvsitrklg fsniimpgem rndlyitier gefekggksv
      421 arnvevtmfi vdssgqtlkd fisfgsgepp aseyhsfvly hnnsprwsel lklpipvdkf
      481 rgahirfefr hcstkekgek klfgfsfvpl mqedgrtlpd gthelivhkc eentnlqdtt
      541 rylklpfskg iflgnnnqam katkesfcit sflcstkltq ngdmldllkw rthpdkitgc
      601 lsklkeidgs eivkflqdtl dtlfgilden sqkygskvfd slvhiinllq dskfhhfkpv
      661 mdtyieshfa galayrdlik vlkwyvdrit eaerqehiqe vlkaqeyifk yivqsrrlfs
      721 latggqneee frcciqellm svrfflsqes kgsgalsqsq avflssfpav ysellklfdv
      781 revanlvqdt lgslptilhv ddslqaiklq cigktvesql ytnpdsryil lpvvlhhlhi
      841 hlqeqkdlim carilsnvfc likknsseks vleeidviva slldillrti leitsrpqps
      901 ssamrfqfqd vtgefvacll sllrqmtdrh yqqlldsfnt keelrdfllq iftvfrilir
      961 pemfpkdwtv mrlvannvii ttvlylsdal rknflnenfd ykiwdsyfyl avifinqlcl
     1021 qlemftpskk kkvlekygdm rvtmgceifs mwqnlgehkl hfipaligpf levtlipqpd
     1081 lrnvmipifh dmmdweqrrs gnfkqveakl idkldslmse gkgdetyrel fnsillkkie
     1141 retwresgvs liatvtrlme rlldyrdcmk mgevdgkkig ctvsllnfyk telnkeemyi
     1201 ryihklydlh lkaqnfteaa ytlllydell ewsdrplref ltypmqtewq rkehlhltii
     1261 qnfdrgkcwe ngiilcrkia eqyesyydyr nlskmrmmea slydkimdqq rlepeffrvg
     1321 fygkkfpffl rnkefvcrgh dyerleafqq rmlnefphai amqhanqpde tifqaeaqyl
     1381 qiyavtpipe sqevlqregv pdniksfykv nhiwkfrydr pfhkgtkdke nefkslwver
     1441 tslylvqslp gisrwfevek revvemsple naievlenkn qqlktlisqc qtrqmqninp
     1501 ltmclngvid aavnggvsry qeaffvkeyi lshpedgeki arlrelmleq aqilefglav
     1561 hekfvpqdmr plhkklvdqf fvmksslgiq efsacmqasp vhfpngsprv crnsapasvs
     1621 pdgtrviprr splsypavnr ysssslssqa saevsnitgq sessdevfnm qpspstssls
     1681 sthsaspnvt ssapssaras pllsdkhkhs rensclspre rpcsaiyptp vepsqrmlfn
     1741 higdgalprs dpnlsapeka vnptpsswsl dsgkeaknms dsgklisppv pprptqtasp
     1801 arhttsvsps pagrsplkgs vqsftpspve yhspglisns pvlsgsyssg isslsrcsts
     1861 etsgfenqvn eqsaplpvpv pvpvpsygge epvrkesktp ppysvyertl rrpvplphsl
     1921 sipvtseppa lppkplaars shlengarrt dpgprprplp rkvsql
//
LOCUS       NP_001713                398 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC4 [Homo sapiens].
ACCESSION   NP_001713
VERSION     NP_001713.2
DBSOURCE    REFSEQ: accession NM_001722.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Ramsay,E.P., Abascal-Palacios,G., Daiss,J.L., King,H., Gouge,J.,
            Pilsl,M., Beuron,F., Morris,E., Gunkel,P., Engel,C. and Vannini,A.
  TITLE     Structure of human RNA polymerase III
  JOURNAL   Nat Commun 11 (1), 6409 (2020)
   PUBMED   33335104
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Renaud,M., Praz,V., Vieu,E., Florens,L., Washburn,M.P., l'Hote,P.
            and Hernandez,N.
  TITLE     Gene duplication and neofunctionalization: POLR3G and POLR3GL
  JOURNAL   Genome Res 24 (1), 37-51 (2014)
   PUBMED   24107381
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Weissglas-Volkov,D., Aguilar-Salinas,C.A., Nikkola,E., Deere,K.A.,
            Cruz-Bautista,I., Arellano-Campos,O., Munoz-Hernandez,L.L.,
            Gomez-Munguia,L., Ordonez-Sanchez,M.L., Reddy,P.M., Lusis,A.J.,
            Matikainen,N., Taskinen,M.R., Riba,L., Cantor,R.M.,
            Sinsheimer,J.S., Tusie-Luna,T. and Pajukanta,P.
  TITLE     Genomic study in Mexicans identifies a new locus for triglycerides
            and refines European lipid loci
  JOURNAL   J Med Genet 50 (5), 298-308 (2013)
   PUBMED   23505323
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Jackson,A.J., Ittmann,M. and Pugh,B.F.
  TITLE     The BN51 protein is a polymerase (Pol)-specific subunit of RNA Pol
            III which reveals a link between Pol III transcription and pre-rRNA
            processing
  JOURNAL   Mol Cell Biol 15 (1), 94-101 (1995)
   PUBMED   7799973
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Ittmann,M.M.
  TITLE     Cell cycle control of the BN51 cell cycle gene which encodes a
            subunit of RNA polymerase III
  JOURNAL   Cell Growth Differ 5 (7), 783-788 (1994)
   PUBMED   7947392
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Greco,A., Ittmann,M., Barletta,C., Basilico,C., Croce,C.M.,
            Cannizzaro,L.A. and Huebner,K.
  TITLE     Chromosomal localization of human genes required for G1 progression
            in mammalian cells
  JOURNAL   Genomics 4 (3), 240-245 (1989)
   PUBMED   2714790
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Ittmann,M., Greco,A. and Basilico,C.
  TITLE     Isolation of the human gene that complements a
            temperature-sensitive cell cycle mutation in BHK cells
  JOURNAL   Mol Cell Biol 7 (10), 3386-3393 (1987)
   PUBMED   3683386
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK026588.1, AY092086.1,
            BQ006609.1 and AC105206.8.
            
            On Nov 15, 2004 this sequence version replaced NP_001713.1.
            
            Summary: This gene complements a temperature-sensitive mutant
            isolated from the BHK-21 Syrian hamster cell line. It leads to a
            block in progression through the G1 phase of the cell cycle at
            nonpermissive temperatures. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.95896.1,
                                           SRR1803615.94370.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306433.9/ ENSP00000303088.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..398
                     /product="DNA-directed RNA polymerase III subunit RPC4"
                     /EC_number="2.7.7.6"
                     /note="BN51 (BHK21) temperature sensitivity complementing;
                     polymerase (RNA) III (DNA directed) polypeptide D, 44kDa;
                     temperature sensitive complementation, cell cycle
                     specific, tsBN51; RNA polymerase III subunit C4;
                     DNA-directed RNA polymerase III subunit D; DNA-directed
                     RNA polymerase III 47 kDa polypeptide; RPC53 homolog; RNA
                     polymerase III 47 kDa subunit; polymerase (RNA) III
                     subunit D"
                     /calculated_mol_wt=44265
     Region          1..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05423.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P05423.2)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P05423.2)"
     Site            95
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P05423.2)"
     Site            97
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P05423.2)"
     Site            99
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P05423.2)"
     Region          220..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P05423.2)"
     Region          263..389
                     /region_name="RNA_pol_Rpc4"
                     /note="RNA polymerase III RPC4; pfam05132"
                     /db_xref="CDD:461558"
     CDS             1..398
                     /gene="POLR3D"
                     /gene_synonym="BN51T; C53; RPC4; RPC53; TSBN51"
                     /coded_by="NM_001722.3:57..1253"
                     /db_xref="CCDS:CCDS34858.1"
                     /db_xref="GeneID:661"
                     /db_xref="HGNC:HGNC:1080"
                     /db_xref="MIM:187280"
ORIGIN      
        1 msegnaagep stpggprpll tgargligrr pappltpgrl psirsrdltl ggvkkktftp
       61 niisrkikee pkeevtvkke krerdrdrqr eghgrgrgrp eviqshsife qgpaemmkkk
      121 gnwdktvdvs dmgpshiini kkekretdee tkqilrmlek ddflddpglr ndtrnmpvql
      181 plahsgwlfk eendepdvkp wlagpkeedm evdipavkvk eeprdeeeea kmkappkaar
      241 ktpglpkdvs vaellrelsl tkeeellflq lpdtlpgqpp tqdikpikte vqgedgqvvl
      301 ikqekdreak laenactlad ltegqvgkll irksgrvqll lgkvtldvtm gtacsflqel
      361 vsvglgdsrt gemtvlghvk hklvcspdfe slldhkhr
//
LOCUS       NP_006640                771 aa            linear   PRI 20-NOV-2025
DEFINITION  U3 small nucleolar RNA-associated protein 14 homolog A isoform 1
            [Homo sapiens].
ACCESSION   NP_006640
VERSION     NP_006640.2
DBSOURCE    REFSEQ: accession NM_006649.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 771)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   2  (residues 1 to 771)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 771)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 771)
  AUTHORS   Li,K.K., Mao,C.Y., Zhang,J.G., Ma,Q., Wang,Y.J., Liu,X.H., Bao,T.
            and Guo,W.
  TITLE     Overexpression of U three protein 14a (UTP14a) is associated with
            poor prognosis of esophageal squamous cell carcinoma
  JOURNAL   Thorac Cancer 10 (11), 2071-2080 (2019)
   PUBMED   31496055
  REMARK    GeneRIF: Results suggest that UTP14a expression is correlated with
            tumor proliferation and invasion; higher expression of UTP14a is a
            predictor of poor prognosis in patients with esophageal squamous
            cell carcinoma (ESCC). Additionally, knockdown of UTP14a inhibits
            cell proliferation and invasion in ESCC cell line, ECA109.
REFERENCE   5  (residues 1 to 771)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 771)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   7  (residues 1 to 771)
  AUTHORS   Hu,L., Wang,J., Liu,Y., Zhang,Y., Zhang,L., Kong,R., Zheng,Z.,
            Du,X. and Ke,Y.
  TITLE     A small ribosomal subunit (SSU) processome component, the human U3
            protein 14A (hUTP14A) binds p53 and promotes p53 degradation
  JOURNAL   J Biol Chem 286 (4), 3119-3128 (2011)
   PUBMED   21078665
  REMARK    GeneRIF: hUTP14a physically interacts with p53 and functionally
            promotes p53 turn-over
REFERENCE   8  (residues 1 to 771)
  AUTHORS   Rohozinski,J., Lamb,D.J. and Bishop,C.E.
  TITLE     UTP14c is a recently acquired retrogene associated with
            spermatogenesis and fertility in man
  JOURNAL   Biol Reprod 74 (4), 644-651 (2006)
   PUBMED   16354793
REFERENCE   9  (residues 1 to 771)
  AUTHORS   Rohozinski,J. and Bishop,C.E.
  TITLE     The mouse juvenile spermatogonial depletion (jsd) phenotype is due
            to a mutation in the X-derived retrogene, mUtp14b
  JOURNAL   Proc Natl Acad Sci U S A 101 (32), 11695-11700 (2004)
   PUBMED   15289605
REFERENCE   10 (residues 1 to 771)
  AUTHORS   Scanlan,M.J., Chen,Y.T., Williamson,B., Gure,A.O., Stockert,E.,
            Gordan,J.D., Tureci,O., Sahin,U., Pfreundschuh,M. and Old,L.J.
  TITLE     Characterization of human colon cancer antigens recognized by
            autologous antibodies
  JOURNAL   Int J Cancer 76 (5), 652-658 (1998)
   PUBMED   9610721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291918.1 and BQ017502.1.
            
            On Jun 10, 2002 this sequence version replaced NP_006640.1.
            
            Summary: This gene encodes a member of the uridine triphosphate 14
            family. As an essential component of a large ribonucleoprotein
            complex bound to the U3 small nucleolar RNA, the encoded protein is
            involved in ribosome biogenesis and 18S rRNA synthesis. An
            autosomal retrotransposed copy of this X-linked gene exists on
            chromosome 13. Alternative splicing results in multiple transcript
            variants.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC009649.1, SRR1803614.48295.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394422.8/ ENSP00000377944.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..771
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..771
                     /product="U3 small nucleolar RNA-associated protein 14
                     homolog A isoform 1"
                     /note="serologically defined colon cancer antigen 16; U3
                     small nucleolar RNA-associated protein 14 homolog A;
                     antigen NY-CO-16; UTP14, U3 small nucleolar
                     ribonucleoprotein, homolog A; UTP14A small subunit (SSU)
                     processome component"
                     /calculated_mol_wt=87847
     Region          23..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Region          44..735
                     /region_name="Utp14"
                     /note="Utp14 protein; pfam04615"
                     /db_xref="CDD:461368"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Region          334..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Region          367..557
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     Region          740..771
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BVJ6.1)"
     CDS             1..771
                     /gene="UTP14A"
                     /gene_synonym="dJ537K23.3; NYCO16; SDCCAG16; Utp14"
                     /coded_by="NM_006649.4:48..2363"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14615.1"
                     /db_xref="GeneID:10813"
                     /db_xref="HGNC:HGNC:10665"
                     /db_xref="MIM:300508"
ORIGIN      
        1 mtanrlaesl lalsqqeela dlpkdyllse sedegdndge rkhqklleai ssldgknrrk
       61 laerseaslk vsefnvsseg sgeklvladl lepvktsssl atvkkqlsrv kskktvelpl
      121 nkeeierihr evafnktaqv lskwdpvvlk nrqaeqlvfp lekeepaiap iehvlsgwka
      181 rtpleqeifn llhknkqpvt dplltpveka slramsleea kmrraelqra ralqsyyeak
      241 arrekkiksk kyhkvvkkgk akkalkefeq lrkvnpaaal eelekiekar mmermslkhq
      301 nsgkwakska imakydlear qamqeqlskn keltqklqva seseeeeggt edveellvpd
      361 vvnevqmnad gpnpwmlrsc tsdtkeaatq edpeqlpele ahgvsesege erpvaeeeil
      421 lrefeerrsl rkrselsqda epagsqetkd sgsqevlsel rvlsqklken hqsrkqkass
      481 egtipqvqre epapeeeepl llqrpervqt leeleelgke ecfqnkelpr pvlegqqser
      541 tpnnrpdapk ekkkkeqmid lqnllttqsp svkslavpti eeledeeern hrqmikeafa
      601 gddvirdflk ekreaveask pkdvdltlpg wgewggvglk psakkrrrfl ikapegpprk
      661 dknlpnviin ekrnihaaah qvrvlpypft hhwqfertiq tpigstwntq rafqklttpk
      721 vvtkpghiin pikaedvgyr sssrsdlsvi qrnpkrittr hkkqlkkcsv d
//
LOCUS       NP_001185940              84 aa            linear   PRI 20-NOV-2025
DEFINITION  dynactin subunit 5 isoform 2 [Homo sapiens].
ACCESSION   NP_001185940
VERSION     NP_001185940.1
DBSOURCE    REFSEQ: accession NM_001199011.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 84)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 84)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 84)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 84)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 84)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 84)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 84)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 84)
  AUTHORS   Parisi,G., Fornasari,M.S. and Echave,J.
  TITLE     Dynactins p25 and p27 are predicted to adopt the LbetaH fold
  JOURNAL   FEBS Lett 562 (1-3), 1-4 (2004)
   PUBMED   15043994
REFERENCE   9  (residues 1 to 84)
  AUTHORS   Eckley,D.M., Gill,S.R., Melkonian,K.A., Bingham,J.B., Goodson,H.V.,
            Heuser,J.E. and Schroer,T.A.
  TITLE     Analysis of dynactin subcomplexes reveals a novel actin-related
            protein associated with the arp1 minifilament pointed end
  JOURNAL   J Cell Biol 147 (2), 307-320 (1999)
   PUBMED   10525537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA310703.1 and CR745557.1.
            
            Summary: This gene encodes a subunit of dynactin, a component of
            the cytoplasmic dynein motor machinery involved in
            minus-end-directed transport. The encoded protein is a component of
            the pointed-end subcomplex and is thought to bind membranous cargo.
            A pseudogene of this gene is located on the long arm of chromosome
            1. Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Jan
            2011].
            
            Transcript Variant: This variant (2) lacks multiple coding exons
            and uses a distinct 3' terminal exon compared to variant 1. The
            resulting protein (isoform 2) is shorter and has a distinct
            C-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR745557.1, AA811478.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..84
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..84
                     /product="dynactin subunit 5 isoform 2"
                     /note="dynactin 4; dynactin subunit p25; dynactin 5 (p25)"
                     /calculated_mol_wt=9609
     Region          13..>39
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     CDS             1..84
                     /gene="DCTN5"
                     /coded_by="NM_001199011.2:78..332"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58435.1"
                     /db_xref="GeneID:84516"
                     /db_xref="HGNC:HGNC:24594"
                     /db_xref="MIM:612962"
ORIGIN      
        1 melgellynk seyietasgn kvsrqsvlcg sqnivlngkn fvisvflspy irchsacrdr
       61 krsdesvrls vnnrewwglv nwrm
//
LOCUS       NP_001274431             637 aa            linear   PRI 20-NOV-2025
DEFINITION  IQ domain-containing protein E isoform 6 [Homo sapiens].
ACCESSION   NP_001274431 XP_005249734
VERSION     NP_001274431.1
DBSOURCE    REFSEQ: accession NM_001287502.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Estrada-Cuzcano,A., Etard,C., Delvallee,C., Stoetzel,C.,
            Schaefer,E., Scheidecker,S., Geoffroy,V., Schneider,A., Studer,F.,
            Mattioli,F., Chennen,K., Sigaudy,S., Plassard,D., Poch,O.,
            Piton,A., Strahle,U., Muller,J. and Dollfus,H.
  TITLE     Novel IQCE variations confirm its role in postaxial polydactyly and
            cause ciliary defect phenotype in zebrafish
  JOURNAL   Hum Mutat 41 (1), 240-254 (2020)
   PUBMED   31549751
  REMARK    GeneRIF: Novel IQCE variations confirm its role in postaxial
            polydactyly and cause ciliary defect phenotype in zebrafish.
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Umair,M., Shah,K., Alhaddad,B., Haack,T.B., Graf,E., Strom,T.M.,
            Meitinger,T. and Ahmad,W.
  TITLE     Exome sequencing revealed a splice site variant in the IQCE gene
            underlying post-axial polydactyly type A restricted to lower limb
  JOURNAL   Eur J Hum Genet 25 (8), 960-965 (2017)
   PUBMED   28488682
  REMARK    GeneRIF: Frameshift and a premature stop codon 22 in IQCE
            completely co-segregated with post-axial polydactyly phenotype
            within the family.
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Corominas,R., Yang,X., Lin,G.N., Kang,S., Shen,Y., Ghamsari,L.,
            Broly,M., Rodriguez,M., Tam,S., Wanamaker,S.A., Fan,C., Yi,S.,
            Tasan,M., Lemmens,I., Kuang,X., Zhao,N., Malhotra,D.,
            Michaelson,J.J., Vacic,V., Calderwood,M.A., Roth,F.P.,
            Tavernier,J., Horvath,S., Salehi-Ashtiani,K., Korkin,D., Sebat,J.,
            Hill,D.E., Hao,T., Vidal,M. and Iakoucheva,L.M.
  TITLE     Protein interaction network of alternatively spliced isoforms from
            brain links genetic risk factors for autism
  JOURNAL   Nat Commun 5, 3650 (2014)
   PUBMED   24722188
  REMARK    Erratum:[Nat Commun. 2023 Feb 2;14(1):569. doi:
            10.1038/s41467-023-36264-y. PMID: 36732511]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY029256.1 and AK302053.1.
            
            On Dec 17, 2013 this sequence version replaced XP_005249734.1.
            
            Transcript Variant: This variant (6) lacks two alternate exons in
            the 5' coding region, initiates translation at a downstream
            in-frame start codon, and contains an alternate 3' terminal exon
            and it thus differs in the 3' coding region and 3' UTR, compared to
            variant 1. The encoded isoform (6) is shorter at the N-terminus and
            has a distinct C-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302053.1, SRR1803616.221148.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..637
                     /product="IQ domain-containing protein E isoform 6"
                     /note="IQ domain-containing protein E"
                     /calculated_mol_wt=71038
     Region          <76..407
                     /region_name="Mplasa_alph_rch"
                     /note="helix-rich Mycoplasma protein; TIGR04523"
                     /db_xref="CDD:275316"
     CDS             1..637
                     /gene="IQCE"
                     /gene_synonym="1700028P05Rik; PAPA7"
                     /coded_by="NM_001287502.2:305..2218"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:23288"
                     /db_xref="HGNC:HGNC:29171"
                     /db_xref="MIM:617631"
ORIGIN      
        1 mplggraslt pqklwlgtak pgsltqalns pltwehawtg vpggtpdclt dtfrvkrphl
       61 rrsasnghvp gtpvyreked mydeiielkk slhvqksdvd lmrtklrrle eensrkdrqi
      121 eqlldpsrgt dfvrtlaekr pdaswvingl kqrilkleqq ckekdgtisk lqtdmkttnl
      181 eemriamety yeevhrlqtl lassettgkk plgekktgak rqkkmgsall slsrsvqelt
      241 eenqslkedl drvlstspti sktqgyvews kprllrrive lekklsvmes skshaaepvr
      301 shppaclass salhrqprgd rnkdherlrg avrdlkeert alqeqllqrd levkqllqak
      361 adlekeleca regeeerrer eevlreeiqt ltsklqelqe mkkeekedcp evphkaqelp
      421 aptpssrhce qdwppdssee glprprspcs dgrrdaaarv lqaqwkvykh kkkkavldea
      481 avvlqaafrg hltrtkllas kahgseppsv pglpdqsspv prvpspiaqa tgspvqeeai
      541 viiqsalrah lararhsatg krtttaastr rrsasathgd assppflaal pgnfihldsg
      601 traagllrsq pksghlqear avsgrkggvs hlelpln
//
LOCUS       NP_000966                178 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL5 isoform 1 [Homo sapiens].
ACCESSION   NP_000966
VERSION     NP_000966.2
DBSOURCE    REFSEQ: accession NM_000975.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Chen,J., Lei,C., Zhang,H., Huang,X., Yang,Y., Liu,J., Jia,Y.,
            Shi,H., Zhang,Y., Zhang,J. and Du,J.
  TITLE     RPL11 promotes non-small cell lung cancer cell proliferation by
            regulating endoplasmic reticulum stress and cell autophagy
  JOURNAL   BMC Mol Cell Biol 24 (1), 7 (2023)
   PUBMED   36869281
  REMARK    GeneRIF: RPL11 promotes non-small cell lung cancer cell
            proliferation by regulating endoplasmic reticulum stress and cell
            autophagy.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Babaylova,E.S., Gopanenko,A.V., Tupikin,A.E., Kabilov,M.R.,
            Malygin,A.A. and Karpova,G.G.
  TITLE     Deficiency of the Ribosomal Protein uL5 Leads to Significant
            Rearrangements of the Transcriptional and Translational Landscapes
            in Mammalian Cells
  JOURNAL   Int J Mol Sci 22 (24), 13485 (2021)
   PUBMED   34948282
  REMARK    GeneRIF: Deficiency of the Ribosomal Protein uL5 Leads to
            Significant Rearrangements of the Transcriptional and Translational
            Landscapes in Mammalian Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Graphodatsky,A.S., Vorobieva,N.V., Filipenko,M.L., Voronina,E.V.,
            Frengen,E. and Prydz,H.
  TITLE     Assignment of the L11 ribosomal protein gene (RPL11) to human
            chromosome 1p36.1-->p35 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 84 (1-2), 97-98 (1999)
   PUBMED   10343117
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Mishin,V.P., Filipenko,M.L., Muravlev,A.I., Karpova,G.G. and
            Mertvetsov,N.P.
  TITLE     [Cloning and determination of the primary structure of DNA
            complementary to the mRNA of human ribosomal protein L11]
  JOURNAL   Bioorg Khim 21 (2), 158-160 (1995)
   PUBMED   7748210
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BU954396.1, CA335141.1, BX118515.1, AL451000.16 and
            AA748897.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 5, 2001 this sequence version replaced NP_000966.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L5P family of ribosomal proteins. It is located in the
            cytoplasm. The protein probably associates with the 5S rRNA.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM740317.1, DA529750.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000643754.2/ ENSP00000496250.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..178
                     /product="large ribosomal subunit protein uL5 isoform 1"
                     /note="cell growth-inhibiting protein 34; 60S ribosomal
                     protein L11; CLL-associated antigen KW-12; large ribosomal
                     subunit protein uL5"
                     /calculated_mol_wt=20121
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12962325, ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Region          5..175
                     /region_name="PTZ00156"
                     /note="60S ribosomal protein L11; Provisional"
                     /db_xref="CDD:185485"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            47
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            52
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     Site            85
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62913.2)"
     CDS             1..178
                     /gene="RPL11"
                     /gene_synonym="DBA7; GIG34; L11; uL5"
                     /coded_by="NM_000975.5:19..555"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS238.1"
                     /db_xref="GeneID:6135"
                     /db_xref="HGNC:HGNC:10301"
                     /db_xref="MIM:604175"
ORIGIN      
        1 maqdqgeken pmrelrirkl clnicvgesg drltraakvl eqltgqtpvf skarytvrsf
       61 girrnekiav hctvrgakae eilekglkvr eyelrknnfs dtgnfgfgiq ehidlgikyd
      121 psigiygldf yvvlgrpgfs iadkkrrtgc igakhriske eamrwfqqky dgiilpgk
//
LOCUS       NP_116270                123 aa            linear   PRI 20-NOV-2025
DEFINITION  U7 snRNA-associated Sm-like protein LSm10 [Homo sapiens].
ACCESSION   NP_116270
VERSION     NP_116270.1
DBSOURCE    REFSEQ: accession NM_032881.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Bucholc,K., Aik,W.S., Yang,X.C., Wang,K., Zhou,Z.H., Dadlez,M.,
            Marzluff,W.F., Tong,L. and Dominski,Z.
  TITLE     Composition and processing activity of a semi-recombinant holo U7
            snRNP
  JOURNAL   Nucleic Acids Res 48 (3), 1508-1530 (2020)
   PUBMED   31819999
  REMARK    GeneRIF: While the molecular basis for this altered cleavage
            activity is unknown, one possibility is that binding of Lsm10 and
            Lsm11 to the spliceosomal Sm site affects the overall geometry of
            the U7-specific Sm ring, resulting in misalignment of the CPSF73
            endonuclease with the substrate.
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Skrajna,A., Yang,X.C., Bucholc,K., Zhang,J., Hall,T.M.T.,
            Dadlez,M., Marzluff,W.F. and Dominski,Z.
  TITLE     U7 snRNP is recruited to histone pre-mRNA in a FLASH-dependent
            manner by two separate regions of the stem-loop binding protein
  JOURNAL   RNA 23 (6), 938-951 (2017)
   PUBMED   28289156
  REMARK    GeneRIF: FLASH plays two roles in 3' end processing of histone
            pre-mRNAs: It interacts with Lsm11 to form a docking platform for
            the polyadenylation factors, and it cooperates with SLBP to recruit
            U7 snRNP to histone pre-mRNA.
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Ghule,P.N., Dominski,Z., Lian,J.B., Stein,J.L., van Wijnen,A.J. and
            Stein,G.S.
  TITLE     The subnuclear organization of histone gene regulatory proteins and
            3' end processing factors of normal somatic and embryonic stem
            cells is compromised in selected human cancer cell types
  JOURNAL   J Cell Physiol 220 (1), 129-135 (2009)
   PUBMED   19277982
  REMARK    GeneRIF: The subnuclear organization of histone gene regulatory
            proteins and 3' end processing factors (NPAT/LSM10) of normal
            somatic and embryonic stem cells is compromised in selected human
            cancer cell types.
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Azzouz,T.N., Pillai,R.S., Dapp,C., Chari,A., Meister,G.,
            Kambach,C., Fischer,U. and Schumperli,D.
  TITLE     Toward an assembly line for U7 snRNPs: interactions of U7-specific
            Lsm proteins with PRMT5 and SMN complexes
  JOURNAL   J Biol Chem 280 (41), 34435-34440 (2005)
   PUBMED   16087681
  REMARK    GeneRIF: Lsm10 and Lsm11, which replace the Sm proteins D1 and D2
            in the histone RNA processing U7 snRNPs, associate with pICln in
            vitro and in vivo without receiving sDMA modifications and with
            PRMT5 and SMN complexes
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Schumperli,D. and Pillai,R.S.
  TITLE     The special Sm core structure of the U7 snRNP: far-reaching
            significance of a small nuclear ribonucleoprotein
  JOURNAL   Cell Mol Life Sci 61 (19-20), 2560-2570 (2004)
   PUBMED   15526162
  REMARK    Review article
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Pillai,R.S., Grimmler,M., Meister,G., Will,C.L., Luhrmann,R.,
            Fischer,U. and Schumperli,D.
  TITLE     Unique Sm core structure of U7 snRNPs: assembly by a specialized
            SMN complex and the role of a new component, Lsm11, in histone RNA
            processing
  JOURNAL   Genes Dev 17 (18), 2321-2333 (2003)
   PUBMED   12975319
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Pillai,R.S., Will,C.L., Luhrmann,R., Schumperli,D. and Muller,B.
  TITLE     Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain
            Lsm10, a new 14 kDa Sm D1-like protein
  JOURNAL   EMBO J 20 (19), 5470-5479 (2001)
   PUBMED   11574479
  REMARK    GeneRIF: Purified U7 snRNPs lack the Sm proteins D1 and D2 but
            contain Lsm10, a new 14 kDa Sm D1-like protein.
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Dominski,Z., Zheng,L.X., Sanchez,R. and Marzluff,W.F.
  TITLE     Stem-loop binding protein facilitates 3'-end formation by
            stabilizing U7 snRNP binding to histone pre-mRNA
  JOURNAL   Mol Cell Biol 19 (5), 3561-3570 (1999)
   PUBMED   10207079
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC119675.2, BC007623.1 and AI150247.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1007107.1,
                                           SRR1163657.250253.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315732.3/ ENSP00000319341.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..123
                     /product="U7 snRNA-associated Sm-like protein LSm10"
                     /note="U7 snRNP-specific Sm-like protein LSM10"
                     /calculated_mol_wt=13949
     Region          8..85
                     /region_name="LSm10"
                     /note="Like-Sm protein 10; cd01733"
                     /db_xref="CDD:212480"
     Site            order(29..35,37..49,51..55)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212480"
     Site            order(47,49,75)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212480"
     Site            71..82
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212480"
     CDS             1..123
                     /gene="LSM10"
                     /gene_synonym="MST074; MSTP074"
                     /coded_by="NM_032881.3:167..538"
                     /db_xref="CCDS:CCDS408.1"
                     /db_xref="GeneID:84967"
                     /db_xref="HGNC:HGNC:17562"
                     /db_xref="MIM:617909"
ORIGIN      
        1 mavshsvker tisensliil lqglqgrvtt vdlrdesvah gridnvdafm nirlakvtyt
       61 drwghqvkld dlfvtgrnvr yvhipddvni tstieqqlqi ihrvrnfggk gqgrwefppk
      121 nck
//
LOCUS       NP_004994                156 aa            linear   PRI 20-NOV-2025
DEFINITION  acyl carrier protein, mitochondrial precursor [Homo sapiens].
ACCESSION   NP_004994
VERSION     NP_004994.1
DBSOURCE    REFSEQ: accession NM_005003.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Schulz,V., Steinhilper,R., Oltmanns,J., Freibert,S.A., Krapoth,N.,
            Linne,U., Welsch,S., Hoock,M.H., Schunemann,V., Murphy,B.J. and
            Lill,R.
  TITLE     Mechanism and structural dynamics of sulfur transfer during de novo
            [2Fe-2S] cluster assembly on ISCU2
  JOURNAL   Nat Commun 15 (1), 3269 (2024)
   PUBMED   38627381
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Suo,Y., Chen,A., La Clair,J.J. and Burkart,M.D.
  TITLE     Substrate Sequestration and Chain Flipping in Human Mitochondrial
            Acyl Carrier Protein
  JOURNAL   Biochemistry 62 (24), 3548-3553 (2023)
   PUBMED   38039071
  REMARK    GeneRIF: Substrate Sequestration and Chain Flipping in Human
            Mitochondrial Acyl Carrier Protein.
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Cipullo,M., Gese,G.V., Khawaja,A., Hallberg,B.M. and Rorbach,J.
  TITLE     Structural basis for late maturation steps of the human
            mitoribosomal large subunit
  JOURNAL   Nat Commun 12 (1), 3673 (2021)
   PUBMED   34135318
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Triepels,R., Smeitink,J., Loeffen,J., Smeets,R., Buskens,C.,
            Trijbels,F. and van den Heuvel,L.
  TITLE     The human nuclear-encoded acyl carrier subunit (NDUFAB1) of the
            mitochondrial complex I in human pathology
  JOURNAL   J Inherit Metab Dis 22 (2), 163-173 (1999)
   PUBMED   10234612
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Loeffen,J.L., Triepels,R.H., van den Heuvel,L.P., Schuelke,M.,
            Buskens,C.A., Smeets,R.J., Trijbels,J.M. and Smeitink,J.A.
  TITLE     cDNA of eight nuclear encoded subunits of NADH:ubiquinone
            oxidoreductase: human complex I cDNA characterization completed
  JOURNAL   Biochem Biophys Res Commun 253 (2), 415-422 (1998)
   PUBMED   9878551
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Emahazion,T., Beskow,A., Gyllensten,U. and Brookes,A.J.
  TITLE     Intron based radiation hybrid mapping of 15 complex I genes of the
            human electron transport chain
  JOURNAL   Cytogenet Cell Genet 82 (1-2), 115-119 (1998)
   PUBMED   9763677
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Runswick,M.J., Fearnley,I.M., Skehel,J.M. and Walker,J.E.
  TITLE     Presence of an acyl carrier protein in NADH:ubiquinone
            oxidoreductase from bovine heart mitochondria
  JOURNAL   FEBS Lett 286 (1-2), 121-124 (1991)
   PUBMED   1907568
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI603093.1, BC058920.1 and AF087660.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.6881.1,
                                           SRR5189655.145856.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000007516.8/
                                                  ENSP00000007516.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..156
                     /product="acyl carrier protein, mitochondrial precursor"
                     /note="mitochondrial acyl carrier protein; complex I SDAP
                     subunit; acyl carrier protein, mitochondrial;
                     NADH:ubiquinone oxidoreductase SDAP subunit; CI-SDAP;
                     NADH-ubiquinone oxidoreductase 9.6 kDa subunit; NADH
                     dehydrogenase (ubiquinone) 1, alpha/beta subcomplex, 1,
                     8kDa"
                     /calculated_mol_wt=10170
     transit_peptide 1..68
                     /note="Mitochondrion.
                     /evidence=ECO:0000269|PubMed:19892738,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O14561.3)"
                     /calculated_mol_wt=7266
     Region          <66..152
                     /region_name="PP-binding"
                     /note="Phosphopantetheine attachment site; cl09936"
                     /db_xref="CDD:447865"
     mat_peptide     69..156
                     /product="Acyl carrier protein, mitochondrial.
                     /id=PRO_0000000561"
                     /note="propagated from UniProtKB/Swiss-Prot (O14561.3)"
                     /calculated_mol_wt=10170
     Site            88
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9CR21; propagated from
                     UniProtKB/Swiss-Prot (O14561.3)"
     CDS             1..156
                     /gene="NDUFAB1"
                     /gene_synonym="ACP; ACP1; FASN2A; SDAP"
                     /coded_by="NM_005003.3:27..497"
                     /db_xref="CCDS:CCDS10614.1"
                     /db_xref="GeneID:4706"
                     /db_xref="HGNC:HGNC:7694"
                     /db_xref="MIM:603836"
ORIGIN      
        1 masrvlsayv srlpaafapl prvrmlavar plstalcsag tqtrlgtlqp alvlaqvpgr
       61 vtqlcrqysd mppltlegiq drvlyvlkly dkidpeklsv nshfmkdlgl dsldqveiim
      121 amedefgfei pdidaeklmc pqeivdyiad kkdvye
//
LOCUS       NP_001232                663 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-T2 isoform a [Homo sapiens].
ACCESSION   NP_001232
VERSION     NP_001232.1
DBSOURCE    REFSEQ: accession NM_001241.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Wang,F., Zhao,Q.H., Liu,J.Z. and Kong,D.L.
  TITLE     MiRNA-188-5p alleviates the progression of osteosarcoma via target
            degrading CCNT2
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (1), 29-35 (2020)
   PUBMED   31957815
  REMARK    GeneRIF: MiRNA-188-5p alleviates the progression of osteosarcoma
            via target degrading CCNT2.
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Napolitano,G., Licciardo,P., Gallo,P., Majello,B., Giordano,A. and
            Lania,L.
  TITLE     The CDK9-associated cyclins T1 and T2 exert opposite effects on
            HIV-1 Tat activity
  JOURNAL   AIDS 13 (12), 1453-1459 (1999)
   PUBMED   10465067
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Bieniasz,P.D., Grdina,T.A., Bogerd,H.P. and Cullen,B.R.
  TITLE     Analysis of the effect of natural sequence variation in Tat and in
            cyclin T on the formation and RNA binding properties of Tat-cyclin
            T complexes
  JOURNAL   J Virol 73 (7), 5777-5786 (1999)
   PUBMED   10364329
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Kwak,Y.T., Ivanov,D., Guo,J., Nee,E. and Gaynor,R.B.
  TITLE     Role of the human and murine cyclin T proteins in regulating HIV-1
            tat-activation
  JOURNAL   J Mol Biol 288 (1), 57-69 (1999)
   PUBMED   10329126
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Wimmer,J., Fujinaga,K., Taube,R., Cujec,T.P., Zhu,Y., Peng,J.,
            Price,D.H. and Peterlin,B.M.
  TITLE     Interactions between Tat and TAR and human immunodeficiency virus
            replication are facilitated by human cyclin T1 but not cyclins T2a
            or T2b
  JOURNAL   Virology 255 (1), 182-189 (1999)
   PUBMED   10049833
REFERENCE   10 (residues 1 to 663)
  AUTHORS   Peng,J., Zhu,Y., Milton,J.T. and Price,D.H.
  TITLE     Identification of multiple cyclin subunits of human P-TEFb
  JOURNAL   Genes Dev 12 (5), 755-762 (1998)
   PUBMED   9499409
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK294889.1, BC114366.2,
            AC016725.5 and AU157699.1.
            
            Summary: The protein encoded by this gene belongs to the highly
            conserved cyclin family, whose members are characterized by a
            dramatic periodicity in protein abundance through the cell cycle.
            Cyclins function as regulators of CDK kinases. Different cyclins
            exhibit distinct expression and degradation patterns which
            contribute to the temporal coordination of each mitotic event. This
            cyclin and its kinase partner CDK9 were found to be subunits of the
            transcription elongation factor p-TEFb. The p-TEFb complex
            containing this cyclin was reported to interact with, and act as a
            negative regulator of human immunodeficiency virus type 1 (HIV-1)
            Tat protein. A pseudogene of this gene is found on chromosome 1.
            Alternate splicing results in multiple transcript
            variants.[provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (a) encodes isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.271168.1,
                                           SRR1803615.32157.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.3"
     Protein         1..663
                     /product="cyclin-T2 isoform a"
                     /note="cyclin T2a; cyclin T2b; SDS-stable vimentin-bound
                     DNA fragment HEF42VIM22; subunit of positive elongation
                     transcription factor b"
                     /calculated_mol_wt=73551
     Region          1..300
                     /region_name="Interaction with MDFIC and MDFI.
                     /evidence=ECO:0000269|PubMed:17289077"
                     /note="propagated from UniProtKB/Swiss-Prot (O60583.2)"
     Region          8..146
                     /region_name="CYCLIN_CCNT2_rpt1"
                     /note="first cyclin box found in cyclin-T2 (CCNT2);
                     cd20596"
                     /db_xref="CDD:410299"
     Site            order(10..11,71..72,88..89,92,95,98..101,129,133,136,
                     140..142,144..145)
                     /site_type="other"
                     /note="putative CDK interface [polypeptide binding]"
                     /db_xref="CDD:410299"
     Region          150..263
                     /region_name="CYCLIN_CCNT2_rpt2"
                     /note="second cyclin box found in cyclin-T2 (CCNT2);
                     cd20598"
                     /db_xref="CDD:410301"
     Site            order(162..164,168..169,171..172,201,205..210,215..216,
                     220,223,234,237..238,241)
                     /site_type="other"
                     /note="putative AF4 family member binding site
                     [polypeptide binding]"
                     /db_xref="CDD:410301"
     Region          250..300
                     /region_name="Interaction with POLR2A.
                     /evidence=ECO:0000269|PubMed:15563843"
                     /note="propagated from UniProtKB/Swiss-Prot (O60583.2)"
     Region          296..>427
                     /region_name="ROM1"
                     /note="RhoGEF, Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases [Signal transduction
                     mechanisms]; COG5422"
                     /db_xref="CDD:227709"
     Region          341..430
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60583.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60583.2)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332;
                     propagated from UniProtKB/Swiss-Prot (O60583.2)"
     CDS             1..663
                     /gene="CCNT2"
                     /gene_synonym="CYCT2"
                     /coded_by="NM_001241.4:34..2025"
                     /note="isoform a is encoded by transcript variant a"
                     /db_xref="CCDS:CCDS2175.1"
                     /db_xref="GeneID:905"
                     /db_xref="HGNC:HGNC:1600"
                     /db_xref="MIM:603862"
ORIGIN      
        1 masgrgassr wfftreqlen tpsrrcgvea dkelscrqqa anliqemgqr lnvsqltint
       61 aivymhrfym hhsftkfnkn iisstalfla akveeqarkl ehvikvahac lhpleplldt
      121 kcdaylqqtq elviletiml qtlgfeitie hphtdvvkct qlvraskdla qtsyfmatns
      181 lhlttfclqy kptviacvci hlackwsnwe ipvstdgkhw weyvdptvtl elldelthef
      241 lqilektpnr lkkirnwran qaarkpkvdg qvsetpllgs slvqnsilvd svtgvptnps
      301 fqkpstsafp apvplnsgni svqdshtsdn lsmlatgmps tsyglsshqe wpqhqdsart
      361 eqlysqkqet slsgsqynin fqqgpsislh sglhhrpdki sdhssvkqey thkagsskhh
      421 gpisttpgii pqkmsldkyr ekrkletldl dvrdhyiaaq veqqhkqgqs qaassssvts
      481 pikmkipian tekymadkke ksgslklrip ipptdksask eelkmkikvs sserhsssde
      541 gsgkskhssp hisrdhkekh kehpssrhht sshkhshshs gsssggskhs adgipptvlr
      601 spvglssdgi sssssssrkr lhvndashnh hskmskssks sgglrtsqhp retgqeasgd
      661 qrs
//
LOCUS       NP_001351450             586 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SLU7 isoform b [Homo sapiens].
ACCESSION   NP_001351450
VERSION     NP_001351450.1
DBSOURCE    REFSEQ: accession NM_001364521.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Rojo,C., Fernandez-Barrena,M.G.,
            Avila,M.A., Arechederra,M. and Berasain,C.
  TITLE     SLU7: A New Hub of Gene Expression Regulation-From Epigenetics to
            Protein Stability in Health and Disease
  JOURNAL   Int J Mol Sci 23 (21), 13411 (2022)
   PUBMED   36362191
  REMARK    GeneRIF: SLU7: A New Hub of Gene Expression Regulation-From
            Epigenetics to Protein Stability in Health and Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 586)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   4  (residues 1 to 586)
  AUTHORS   Garate-Rascon,M., Recalde,M., Jimenez,M., Elizalde,M., Azkona,M.,
            Uriarte,I., Latasa,M.U., Urtasun,R., Bilbao,I., Sangro,B.,
            Garcia-Ruiz,C., Fernandez-Checa,J.C., Corrales,F.J., Esquivel,A.,
            Pineda-Lucena,A., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     Splicing Factor SLU7 Prevents Oxidative Stress-Mediated Hepatocyte
            Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage
  JOURNAL   Hepatology 74 (5), 2791-2807 (2021)
   PUBMED   34170569
  REMARK    GeneRIF: Splicing Factor SLU7 Prevents Oxidative Stress-Mediated
            Hepatocyte Nuclear Factor 4alpha Degradation, Preserving Hepatic
            Differentiation and Protecting From Liver Damage.
REFERENCE   5  (residues 1 to 586)
  AUTHORS   Recalde,M., Garate-Rascon,M., Elizalde,M., Azkona,M., Latasa,M.U.,
            Barcena-Varela,M., Sangro,B., Fernandez-Barrena,M.G., Avila,M.A.,
            Arechederra,M. and Berasain,C.
  TITLE     The splicing regulator SLU7 is required to preserve DNMT1 protein
            stability and DNA methylation
  JOURNAL   Nucleic Acids Res 49 (15), 8592-8609 (2021)
   PUBMED   34331453
  REMARK    GeneRIF: The splicing regulator SLU7 is required to preserve DNMT1
            protein stability and DNA methylation.
REFERENCE   6  (residues 1 to 586)
  AUTHORS   Shomron,N., Reznik,M. and Ast,G.
  TITLE     Splicing factor hSlu7 contains a unique functional domain required
            to retain the protein within the nucleus
  JOURNAL   Mol Biol Cell 15 (8), 3782-3795 (2004)
   PUBMED   15181151
  REMARK    GeneRIF: The zinc-knuckle motif of hSlu7 determines the cellular
            localization of the protein through a nucleocytoplasmic-sensitive
            shuttling balance.
REFERENCE   7  (residues 1 to 586)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   8  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     An upstream AG determines whether a downstream AG is selected
            during catalytic step II of splicing
  JOURNAL   Mol Cell Biol 21 (5), 1509-1514 (2001)
   PUBMED   11238888
REFERENCE   9  (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     The RNA splicing factor hSlu7 is required for correct 3'
            splice-site choice
  JOURNAL   Nature 402 (6758), 207-210 (1999)
   PUBMED   10647016
REFERENCE   10 (residues 1 to 586)
  AUTHORS   Chua,K. and Reed,R.
  TITLE     Human step II splicing factor hSlu7 functions in restructuring the
            spliceosome between the catalytic steps of splicing
  JOURNAL   Genes Dev 13 (7), 841-850 (1999)
   PUBMED   10197984
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091842.3.
            
            Summary: Pre-mRNA splicing occurs in two sequential
            transesterification steps. The protein encoded by this gene is a
            splicing factor that has been found to be essential during the
            second catalytic step in the pre-mRNA splicing process. It
            associates with the spliceosome and contains a zinc knuckle motif
            that is found in other splicing factors and is involved in
            protein-nucleic acid and protein-protein interactions. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5), as well as variants 2-4,
            encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803612.176674.1, SRR1803611.171033.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..586
                     /product="pre-mRNA-splicing factor SLU7 isoform b"
                     /note="step II splicing factor SLU7; zinc knuckle motif
                     containing; pre-mRNA-splicing factor SLU7; SLU7 splicing
                     factor homolog; SLU7 homolog, splicing factor"
                     /calculated_mol_wt=68256
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          77..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          129..169
                     /region_name="Bipartite nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Region          161..434
                     /region_name="Slu7"
                     /note="Pre-mRNA splicing Prp18-interacting factor;
                     pfam11708"
                     /db_xref="CDD:463326"
     Region          206..254
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O95391.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O95391.2)"
     Region          496..586
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95391.2)"
     CDS             1..586
                     /gene="SLU7"
                     /gene_synonym="9G8; hSlu7"
                     /coded_by="NM_001364521.2:204..1964"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS4352.1"
                     /db_xref="GeneID:10569"
                     /db_xref="HGNC:HGNC:16939"
                     /db_xref="MIM:605974"
ORIGIN      
        1 msatvvdavn aaplsgskem sleepkkmtr edwrkkkele eqrklgnapa evdeegkdin
       61 phipqyissv pwyidpskrp tlkhqrpqpe kqkqfsssge wykrgvkens iitkyrkgac
      121 encgamthkk kdcferprrv gakftgtnia pdehvqpqlm fdydgkrdrw ngynpeehmk
      181 iveeyakvdl akrtlkaqkl qeelasgklv eqanspkhqw geeepnsqme kdhnsedede
      241 dkyaddidmp gqnfdskrri tvrnlrired iakylrnldp nsayydpktr amrenpyana
      301 gknpdevsya gdnfvrytgd tismaqtqlf aweaydkgse vhlqadptkl ellyksfkvk
      361 kedfkeqqke silekyggqe hldappaell laqtedyvey srhgtvikgq eravacskye
      421 edvkihnhth iwgsywkegr wgykcchsff kysyctgeag keivnseeci ineitgeesv
      481 kkpqtlmelh qeklkeekkk kkkkkkkhrk sssdsddeek kheklkkaln aeearllhvk
      541 etmqiderkr pynsmyetre pteeemeayr mkrqrpddpm asflgq
//
LOCUS       NP_000325               1836 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel protein type 4 subunit alpha [Homo sapiens].
ACCESSION   NP_000325
VERSION     NP_000325.4
DBSOURCE    REFSEQ: accession NM_000334.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1836)
  AUTHORS   Talarico,M., Fortunato,F., Labalme,A., Januel,L., Chatron,N.,
            Sanlaville,D., Sammarra,I., Gagliardi,M., Procopio,R.,
            Valentino,P., Annesi,G., Lesca,G. and Gambardella,A.
  TITLE     Idiopathic generalized epilepsy in a family with SCN4A-related
            myotonia
  JOURNAL   Epilepsia Open 9 (3), 951-959 (2024)
   PUBMED   38544349
  REMARK    GeneRIF: Idiopathic generalized epilepsy in a family with
            SCN4A-related myotonia.
REFERENCE   2  (residues 1 to 1836)
  AUTHORS   Meng,F., Shi,Y., Ju,D., Wang,X., Dong,H., Li,X., Li,X. and Zhou,X.
  TITLE     [Prenatal diagnosis of a case with Congenital myasthenic syndrome
            due to compound heterozygous variants of SCN4A gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (4), 450-455 (2024)
   PUBMED   38565511
  REMARK    GeneRIF: [Prenatal diagnosis of a case with Congenital myasthenic
            syndrome due to compound heterozygous variants of SCN4A gene].
REFERENCE   3  (residues 1 to 1836)
  AUTHORS   Campanale,C., Laghetti,P., Saltarella,I., Altamura,C., Canioni,E.,
            Iosa,E., Maggi,L., Brugnoni,R., Tacconi,P. and Desaphy,J.F.
  TITLE     A c.1775C > T Point Mutation of Sodium Channel Alfa Subunit Gene
            (SCN4A) in a Three-Generation Sardinian Family with Sodium Channel
            Myotonia
  JOURNAL   J Neuromuscul Dis 11 (3), 725-734 (2024)
   PUBMED   38427496
  REMARK    GeneRIF: A c.1775C > T Point Mutation of Sodium Channel Alfa
            Subunit Gene (SCN4A) in a Three-Generation Sardinian Family with
            Sodium Channel Myotonia.
REFERENCE   4  (residues 1 to 1836)
  AUTHORS   Zhang,Y.J., Dai,L.F., Ren,S.S. and Ding,C.H.
  TITLE     [Two cases of potassium-aggravated myotonia induced by SCN4A gene
            variation]
  JOURNAL   Zhonghua Er Ke Za Zhi 61 (11), 1043-1045 (2023)
   PUBMED   37899345
  REMARK    GeneRIF: [Two cases of potassium-aggravated myotonia induced by
            SCN4A gene variation].
REFERENCE   5  (residues 1 to 1836)
  AUTHORS   Weber,F.
  TITLE     Hyperkalemic Periodic Paralysis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301669
REFERENCE   6  (residues 1 to 1836)
  AUTHORS   Weber,F. and Lehmann-Horn,F.
  TITLE     Hypokalemic Periodic Paralysis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301512
REFERENCE   7  (residues 1 to 1836)
  AUTHORS   Abicht,A., Muller,J.S. and Lochmuller,H.
  TITLE     Congenital Myasthenic Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301347
REFERENCE   8  (residues 1 to 1836)
  AUTHORS   McClatchey,A.I., Van den Bergh,P., Pericak-Vance,M.A., Raskind,W.,
            Verellen,C., McKenna-Yasek,D., Rao,K., Haines,J.L., Bird,T.,
            Brown,R.H. Jr. et al.
  TITLE     Temperature-sensitive mutations in the III-IV cytoplasmic loop
            region of the skeletal muscle sodium channel gene in paramyotonia
            congenita
  JOURNAL   Cell 68 (4), 769-774 (1992)
   PUBMED   1310898
REFERENCE   9  (residues 1 to 1836)
  AUTHORS   Ptacek,L.J., Tawil,R., Griggs,R.C., Storvick,D. and Leppert,M.
  TITLE     Linkage of atypical myotonia congenita to a sodium channel locus
  JOURNAL   Neurology 42 (2), 431-433 (1992)
   PUBMED   1310531
REFERENCE   10 (residues 1 to 1836)
  AUTHORS   Wang,J.Z., Rojas,C.V., Zhou,J.H., Schwartz,L.S., Nicholas,H. and
            Hoffman,E.P.
  TITLE     Sequence and genomic structure of the human adult skeletal muscle
            sodium channel alpha subunit gene on 17q
  JOURNAL   Biochem Biophys Res Commun 182 (2), 794-801 (1992)
   PUBMED   1310396
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M81758.1, AY212253.1 and
            AC127029.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 26, 2006 this sequence version replaced NP_000325.3.
            
            Summary: Voltage-gated sodium channels are transmembrane
            glycoprotein complexes composed of a large alpha subunit with 24
            transmembrane domains and one or more regulatory beta subunits.
            They are responsible for the generation and propagation of action
            potentials in neurons and muscle. This gene encodes one member of
            the sodium channel alpha subunit gene family. It is expressed in
            skeletal muscle, and mutations in this gene have been linked to
            several myotonia and periodic paralysis disorders. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M81758.1, AY212253.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000435607.3/ ENSP00000396320.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..1836
                     /product="sodium channel protein type 4 subunit alpha"
                     /note="skeletal muscle sodium channel alpha subunit;
                     skeletal muscle voltage-dependent sodium channel type IV
                     alpha subunit; sodium channel protein type IV subunit
                     alpha; voltage-gated sodium channel subunit alpha Nav1.4;
                     sodium channel protein skeletal muscle subunit alpha;
                     sodium channel, voltage-gated, type IV, alpha subunit;
                     CTC-264K15.6"
                     /calculated_mol_wt=207931
     Region          39..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          113..454
                     /region_name="I. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          130..457
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            132..150
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            158..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            193..210
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            214
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            217..233
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            253..272
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            288
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            291
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            303
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            315
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            321
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            333
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            362
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30190309,
                     ECO:0007744|PDB:6AGF; propagated from UniProtKB/Swiss-Prot
                     (P35499.4)"
     Site            407
                     /site_type="other"
                     /note="Important for inhibition by tetrodotoxin.
                     /evidence=ECO:0000250|UniProtKB:P15390; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            424..444
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          493..530
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          560..832
                     /region_name="II. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          577..790
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            579..597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            609..628
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            643..662
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            665..682
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            699..717
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            779..797
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          816..1026
                     /region_name="Na_trans_assoc"
                     /note="Sodium ion transport-associated; pfam06512"
                     /db_xref="CDD:461936"
     Region          863..885
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          930..992
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1013..1326
                     /region_name="III. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1030..1304
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1033..1050
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1064..1082
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1097..1115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1124..1142
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1160..1179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1191
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35499.4)"
     Site            1205
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30190309,
                     ECO:0007744|PDB:6AGF; propagated from UniProtKB/Swiss-Prot
                     (P35499.4)"
     Site            1270..1291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1296..1348
                     /region_name="Na_channel_gate"
                     /note="Inactivation gate of the voltage-gated sodium
                     channel alpha subunits; cd13433"
                     /db_xref="CDD:240441"
     Site            1310..1313
                     /site_type="other"
                     /note="putative hydrophobic latch"
                     /db_xref="CDD:240441"
     Region          1310..1312
                     /region_name="Important for rapid channel inactivation.
                     /evidence=ECO:0000250|UniProtKB:P15390"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1335..1633
                     /region_name="IV. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1353..1609
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            1355..1372
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1384..1402
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1415..1432
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1446..1462
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1482..1499
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Site            1575..1597
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     Region          1778..1836
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35499.4)"
     CDS             1..1836
                     /gene="SCN4A"
                     /gene_synonym="CMS16; CMYO22A; CMYP22A; HOKPP2; HYKPP;
                     HYPP; Na(V)1.4; NAC1A; Nav1.4; SkM1"
                     /coded_by="NM_000334.4:78..5588"
                     /db_xref="CCDS:CCDS45761.1"
                     /db_xref="GeneID:6329"
                     /db_xref="HGNC:HGNC:10591"
                     /db_xref="MIM:603967"
ORIGIN      
        1 marpslctlv plgpeclrpf treslaaieq raveeearlq rnkqmeieep erkprsdlea
       61 gknlpmiygd pppevigipl edldpyysnk ktfivlnkgk aifrfsatpa lyllspfsvv
      121 rrgaikvlih alfsmfimit iltncvfmtm sdpppwsknv eytftgiytf eslikilarg
      181 fcvddftflr dpwnwldfsv immayltefv dlgnisalrt frvlralkti tvipglktiv
      241 galiqsvkkl sdvmiltvfc lsvfalvglq lfmgnlrqkc vrwpppfndt nttwysndtw
      301 ygndtwygne mwygndswya ndtwnshasw atndtfdwda yisdegnfyf legsndallc
      361 gnssdaghcp egyeciktgr npnygytsyd tfswaflalf rlmtqdywen lfqltlraag
      421 ktymiffvvi iflgsfylin lilavvamay aeqneatlae dkekeeefqq mlekfkkhqe
      481 elekakaaqa leggeadgdp ahgkdcngsl dtsqgekgap rqsssgdsgi sdameeleea
      541 hqkcppwwyk cahkvliwnc capwlkfkni ihlivmdpfv dlgiticivl ntlfmamehy
      601 pmtehfdnvl tvgnlvftgi ftaemvlkli amdpyeyfqq gwnifdsiiv tlslvelgla
      661 nvqglsvlrs frllrvfkla kswptlnmli kiignsvgal gnltlvlaii vfifavvgmq
      721 lfgksykecv ckialdcnlp rwhmhdffhs flivfrilcg ewietmwdcm evagqamclt
      781 vflmvmvign lvvlnlflal llssfsadsl aasdedgemn nlqiaigrik lgigfakafl
      841 lgllhgkils pkdimlslge adgageagea getapedekk eppeedlkkd nhilnhmgla
      901 dgppssleld hlnfinnpyl tiqvpiasee sdlempteee tdtfsepeds kkppqplydg
      961 nssvcstady kppeedpeeq aeenpegeqp eecfteacvq rwpclyvdis qgrgkkwwtl
     1021 rracfkiveh nwfetfivfm illssgalaf ediyieqrrv irtileyadk vftyifimem
     1081 llkwvaygfk vyftnawcwl dflivdvsii slvanwlgys elgpikslrt lralrplral
     1141 srfegmrvvv nallgaipsi mnvllvclif wlifsimgvn lfagkfyyci ntttserfdi
     1201 sevnnksece slmhtgqvrw lnvkvnydnv glgylsllqv atfkgwmdim yaavdsreke
     1261 eqpqyevnly mylyfvifii fgsfftlnlf igviidnfnq qkkklggkdi fmteeqkkyy
     1321 namkklgskk pqkpiprpqn kiqgmvydlv tkqafditim iliclnmvtm mvetdnqsql
     1381 kvdilyninm ifiiiftgec vlkmlalrqy yftvgwnifd fvvvilsivg lalsdliqky
     1441 fvsptlfrvi rlarigrvlr lirgakgirt llfalmmslp alfniglllf lvmfiysifg
     1501 msnfayvkke sgiddmfnfe tfgnsiiclf eittsagwdg llnpilnsgp pdcdpnlenp
     1561 gtsvkgdcgn psigicffcs yiiisflivv nmyiaiilen fnvateesse plgeddfemf
     1621 yetwekfdpd atqfiaysrl sdfvdtlqep lriakpnkik litldlpmvp gdkihcldil
     1681 faltkevlgd sgemdalkqt meekfmaanp skvsyepitt tlkrkheevc aikiqrayrr
     1741 hllqrsmkqa symyrhshdg sgddapekeg llantmskmy ghengnsssp speekgeagd
     1801 agptmglmpi spsdtawppa pppgqtvrpg vkeslv
//
LOCUS       NP_001350735             170 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 5 [Homo sapiens].
ACCESSION   NP_001350735 XP_011523359
VERSION     NP_001350735.1
DBSOURCE    REFSEQ: accession NM_001363806.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5.
            
            On May 14, 2019 this sequence version replaced XP_011523359.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.118844.1, BQ961705.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..170
                     /product="MIF4G domain-containing protein isoform 5"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=19099
     CDS             1..170
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001363806.2:139..651"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS92390.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqvnnmpm malvnpvydc lfrlaqpdsl skeeevdclv lqlhrvgeql ekmngqrmde
      121 lfvlirdgfl lptglsslaq lllleiiefr aagwkttpaa hkyyysevsd
//
LOCUS       NP_056277                719 aa            linear   PRI 20-NOV-2025
DEFINITION  nucleolar protein 11 isoform 1 [Homo sapiens].
ACCESSION   NP_056277
VERSION     NP_056277.2
DBSOURCE    REFSEQ: accession NM_015462.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 719)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 719)
  AUTHORS   McCool,M.A., Bryant,C.J., Huang,H., Ogawa,L.M., Farley-Barnes,K.I.,
            Sondalle,S.B., Abriola,L., Surovtseva,Y.V. and Baserga,S.J.
  TITLE     Human nucleolar protein 7 (NOL7) is required for early pre-rRNA
            accumulation and pre-18S rRNA processing
  JOURNAL   RNA Biol 20 (1), 257-271 (2023)
   PUBMED   37246770
REFERENCE   3  (residues 1 to 719)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 719)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 719)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 719)
  AUTHORS   Carvill,G.L., Weckhuysen,S., McMahon,J.M., Hartmann,C.,
            Moller,R.S., Hjalgrim,H., Cook,J., Geraghty,E., O'Roak,B.J.,
            Petrou,S., Clarke,A., Gill,D., Sadleir,L.G., Muhle,H., von
            Spiczak,S., Nikanorova,M., Hodgson,B.L., Gazina,E.V., Suls,A.,
            Shendure,J., Dibbens,L.M., De Jonghe,P., Helbig,I., Berkovic,S.F.,
            Scheffer,I.E. and Mefford,H.C.
  TITLE     GABRA1 and STXBP1: novel genetic causes of Dravet syndrome
  JOURNAL   Neurology 82 (14), 1245-1253 (2014)
   PUBMED   24623842
REFERENCE   7  (residues 1 to 719)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 719)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 719)
  AUTHORS   Freed,E.F., Prieto,J.L., McCann,K.L., McStay,B. and Baserga,S.J.
  TITLE     NOL11, implicated in the pathogenesis of North American Indian
            childhood cirrhosis, is required for pre-rRNA transcription and
            processing
  JOURNAL   PLoS Genet 8 (8), e1002892 (2012)
   PUBMED   22916032
  REMARK    GeneRIF: NOL11 is a novel protein required for the early stages of
            ribosome biogenesis in humans and is implicated in the pathogenesis
            of North American Indian childhood cirrhosis.
REFERENCE   10 (residues 1 to 719)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA772356.1, AK023702.1, AK299483.1, AW273123.1 and AC006534.10.
            
            On Jun 10, 2002 this sequence version replaced NP_056277.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.20070.1,
                                           SRR1803613.1671.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253247.9/ ENSP00000253247.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..719
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..719
                     /product="nucleolar protein 11 isoform 1"
                     /calculated_mol_wt=80993
     Region          200..243
                     /region_name="NUC205"
                     /note="NUC205 domain; pfam08168"
                     /db_xref="CDD:429856"
     Site            346
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H8H0.1)"
     CDS             1..719
                     /gene="NOL11"
                     /coded_by="NM_015462.5:13..2172"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11671.1"
                     /db_xref="GeneID:25926"
                     /db_xref="HGNC:HGNC:24557"
                     /db_xref="MIM:615366"
ORIGIN      
        1 maaleeeftl ssvvlsagpe gllgveqsdk tdqflvtdsg rtvilykvsd qkplgswsvk
       61 qgqiitcpav cnfqtgeyvv vhdnkvlriw nnedvnldkv fkatlsaevy rilsvqgtep
      121 lvlfkegavr glealladpq qkietvisde evikwtkffv vfrhpvlifi tekhgnyfay
      181 vqmfnsrilt kytlllgqde nsviksftas vdrkfislms lssdgciyet lipirpadpe
      241 knqslvksll lkavvsgnar ngvaltaldq dhvavlgspl aaskeclsvw nikfqtlqts
      301 kelpqgtsgq lwyygehlfm lhgksltvip ykcevsslag algklkhsqd pgthvvshfv
      361 nwetpqgcgl gfqnseqsrr ilrrrkievs lqpevppskq llstimkdse khievevrkf
      421 lalkqtpdfh tvigdtvtgl lerckaepsf yprnclmqli qthvlsyslc pdlmeialkk
      481 kdvqllqlcl qqfpdipesv tcaclkifls igddslqetd vnmesvfdys insvhdekme
      541 eqteilqngf npeedkcnnc dqelnkkpqd etkestscpv vqkraallna ilhsaysetf
      601 llphlkdipa qhitlflkyl yflylkcsen atmtlpgihp ptlnqimdwi cllldanftv
      661 vvmmpeakrl linlyklvks qisvyselnk ievsfrelqk lnqeknnrgl ysievlelf
//
LOCUS       NP_071412                288 aa            linear   PRI 20-NOV-2025
DEFINITION  phenazine biosynthesis-like domain-containing protein isoform a
            [Homo sapiens].
ACCESSION   NP_071412
VERSION     NP_071412.2
DBSOURCE    REFSEQ: accession NM_022129.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Hou,P., Zhu,H., Chu,F., Gao,Y., Sun,X., Zhang,F., Wang,X., Feng,Y.,
            Li,X., Liu,Y., Wang,J., Wang,X., He,D.C., Wang,H. and He,H.
  TITLE     Phenazine biosynthesis-like domain-containing protein (PBLD) and
            Cedrelone promote antiviral immune response by activating NF-kB
  JOURNAL   Nat Commun 16 (1), 496 (2025)
   PUBMED   39779683
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Zhu,H., Hou,P., Chu,F., Li,X., Zhang,W., Sun,X., Liu,Y., Zhao,G.,
            Gao,Y., He,D.C., Wang,H. and He,H.
  TITLE     PBLD promotes IRF3 mediated the type I interferon (IFN-I) response
            and apoptosis to inhibit viral replication
  JOURNAL   Cell Death Dis 15 (10), 727 (2024)
   PUBMED   39362857
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Han,L., Lin,X., Yan,Q., Gu,C., Li,M., Pan,L., Meng,Y., Zhao,X.,
            Liu,S. and Li,A.
  TITLE     PBLD inhibits angiogenesis via impeding VEGF/VEGFR2-mediated
            microenvironmental cross-talk between HCC cells and endothelial
            cells
  JOURNAL   Oncogene 41 (13), 1851-1865 (2022)
   PUBMED   35140333
  REMARK    GeneRIF: PBLD inhibits angiogenesis via impeding
            VEGF/VEGFR2-mediated microenvironmental cross-talk between HCC
            cells and endothelial cells.
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Zhu,M., Wang,F., Mi,H., Li,L., Wang,J., Han,M. and Gu,Y.
  TITLE     Long noncoding RNA MEG3 suppresses cell proliferation, migration
            and invasion, induces apoptosis and paclitaxel-resistance via
            miR-4513/PBLD axis in breast cancer cells
  JOURNAL   Cell Cycle 19 (23), 3277-3288 (2020)
   PUBMED   33121324
  REMARK    GeneRIF: Long noncoding RNA MEG3 suppresses cell proliferation,
            migration and invasion, induces apoptosis and paclitaxel-resistance
            via miR-4513/PBLD axis in breast cancer cells.
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Zhang,J., Kang,B., Tan,X., Bai,Z., Liang,Y., Xing,R., Shao,J.,
            Xu,N., Wang,R., Liu,S. and Lu,Y.
  TITLE     Comparative analysis of the protein profiles from primary gastric
            tumors and their adjacent regions: MAWBP could be a new protein
            candidate involved in gastric cancer
  JOURNAL   J Proteome Res 6 (11), 4423-4432 (2007)
   PUBMED   17929853
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 288)
  AUTHORS   van Dijk,M., Mulders,J., Poutsma,A., Konst,A.A., Lachmeijer,A.M.,
            Dekker,G.A., Blankenstein,M.A. and Oudejans,C.B.
  TITLE     Maternal segregation of the Dutch preeclampsia locus at 10q22 with
            a new member of the winged helix gene family
  JOURNAL   Nat Genet 37 (5), 514-519 (2005)
   PUBMED   15806103
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Iriyama,C., Matsuda,S., Katsumata,R. and Hamaguchi,M.
  TITLE     Cloning and sequencing of a novel human gene which encodes a
            putative hydroxylase
  JOURNAL   J Hum Genet 46 (5), 289-292 (2001)
   PUBMED   11355021
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016395.5, CB121561.1 and AI114748.1.
            
            On Apr 3, 2005 this sequence version replaced NP_071412.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.235937.1,
                                           SRR1803613.113805.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358769.7/ ENSP00000351619.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..288
                     /product="phenazine biosynthesis-like domain-containing
                     protein isoform a"
                     /note="phenazine biosynthesis-like domain-containing
                     protein; MAWD-binding protein; epididymis secretory
                     protein Li 306; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=31654
     Region          1..287
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
     CDS             1..288
                     /gene="PBLD"
                     /gene_synonym="HEL-S-306; MAWBP; MAWDBP"
                     /coded_by="NM_022129.4:205..1071"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7277.2"
                     /db_xref="GeneID:64081"
                     /db_xref="HGNC:HGNC:23301"
                     /db_xref="MIM:612189"
ORIGIN      
        1 mklpifiada ftarafrgnp aavcllenel dedmhqkiar emnlsetafi rklhptdnfa
       61 qsscfglrwf tpasevplcg hatlasaavl fhkiknmnst ltfvtlsgel rarraedgiv
      121 ldlplypahp qdfhevedli ktaigntlvq dicyspdtqk llvrlsdvyn rsflenlkvn
      181 tenllqvent gkvkgliltl kgepggqtqa fdfysryfap wvgvaedpvt gsahavlssy
      241 wsqhlgkkem hafqcshrgg elgislrpdg rvdirggaav vlegtlta
//
LOCUS       NP_851308                496 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            delta isoform isoform 3 [Homo sapiens].
ACCESSION   NP_851308
VERSION     NP_851308.1
DBSOURCE    REFSEQ: accession NM_180977.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 496)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 496)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   3  (residues 1 to 496)
  AUTHORS   Oyama,N., Vaneynde,P., Reynhout,S., Pao,E.M., Timms,A., Fan,X.,
            Foss,K., Derua,R., Janssens,V., Chung,W. and Mirzaa,G.M.
  TITLE     Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis
  JOURNAL   J Med Genet 60 (5), 511-522 (2023)
   PUBMED   36216457
  REMARK    GeneRIF: Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis.
REFERENCE   4  (residues 1 to 496)
  AUTHORS   Liu,R., Huang,Y., Li,C., Wang,P., Wang,Y. and Zhang,L.
  TITLE     A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree
  JOURNAL   Clin Neurol Neurosurg 223, 107524 (2022)
   PUBMED   36403339
  REMARK    GeneRIF: A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree.
REFERENCE   5  (residues 1 to 496)
  AUTHORS   Anwar,M.I., Li,N., Zhou,Q., Chen,M., Hu,C., Wu,T., Chen,H., Li,Y.P.
            and Zhou,Y.
  TITLE     PPP2R5D promotes hepatitis C virus infection by binding to viral
            NS5B and enhancing viral RNA replication
  JOURNAL   Virol J 19 (1), 118 (2022)
   PUBMED   35836293
  REMARK    GeneRIF: PPP2R5D promotes hepatitis C virus infection by binding to
            viral NS5B and enhancing viral RNA replication.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 496)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   7  (residues 1 to 496)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   8  (residues 1 to 496)
  AUTHORS   Tanabe,O., Nagase,T., Murakami,T., Nozaki,H., Usui,H., Nishito,Y.,
            Hayashi,H., Kagamiyama,H. and Takeda,M.
  TITLE     Molecular cloning of a 74-kDa regulatory subunit (B' or delta) of
            human protein phosphatase 2A
  JOURNAL   FEBS Lett 379 (1), 107-111 (1996)
   PUBMED   8566219
REFERENCE   9  (residues 1 to 496)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
REFERENCE   10 (residues 1 to 496)
  AUTHORS   Mirzaa,G., Foss,K., Sudnawa,K. and Chung,W.K.
  TITLE     PPP2R5D-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30676711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA388594.1, AB000635.1 and
            BC001095.2.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a delta isoform of the regulatory subunit B56 subfamily.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            isoform (3), that is missing an internal segment compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB000635.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..496
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit delta isoform isoform 3"
                     /calculated_mol_wt=58322
     Region          6..407
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     CDS             1..496
                     /gene="PPP2R5D"
                     /gene_synonym="B56D; B56delta; HJS1; MRD35"
                     /coded_by="NM_180977.3:109..1599"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43464.1"
                     /db_xref="GeneID:5528"
                     /db_xref="HGNC:HGNC:9312"
                     /db_xref="MIM:601646"
ORIGIN      
        1 mpyklkkeke lfiqklrqcc vlfdfvsdpl sdlkfkevkr aglnemveyi thsrdvvtea
       61 iypeavtmfs vnlfrtlpps snptgaefdp eedeptleaa wphlqlvyef flrflespdf
      121 qpniakkyid qkfvlalldl fdsedprerd flktilhriy gkflglrayi rrqinhifyr
      181 fiyetehhng iaelleilgs iingfalplk eehkmflirv llplhkvksl svyhpqlayc
      241 vvqflekess ltepvivgll kfwpkthspk evmflnelee ildviepsef skvmeplfrq
      301 lakcvssphf qvaeralyyw nneyimslis dnaarvlpim fpalyrnsks hwnktihgli
      361 ynalklfmem nqklfddctq qykaekqkgr frmkereemw qkieelarln pqypmfrapp
      421 plppvysmet etptaediql lkrtveteav qmlkdikkek vllrrkselp qdvytikale
      481 ahkraeeflt asqeal
//
LOCUS       NP_001171434             267 aa            linear   PRI 20-NOV-2025
DEFINITION  CDK-activating kinase assembly factor MAT1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001171434
VERSION     NP_001171434.1
DBSOURCE    REFSEQ: accession NM_001177963.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Abdella,R., Talyzina,A., Chen,S., Inouye,C.J., Tjian,R. and He,Y.
  TITLE     Structure of the human Mediator-bound transcription preinitiation
            complex
  JOURNAL   Science 372 (6537), 52-56 (2021)
   PUBMED   33707221
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Greber,B.J., Remis,J., Ali,S. and Nogales,E.
  TITLE     2.5 A-resolution structure of human CDK-activating kinase bound to
            the clinical inhibitor ICEC0942
  JOURNAL   Biophys J 120 (4), 677-686 (2021)
   PUBMED   33476598
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Aprelikova,O., Xiong,Y. and Liu,E.T.
  TITLE     Both p16 and p21 families of cyclin-dependent kinase (CDK)
            inhibitors block the phosphorylation of cyclin-dependent kinases by
            the CDK-activating kinase
  JOURNAL   J Biol Chem 270 (31), 18195-18197 (1995)
   PUBMED   7629134
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Desai,D., Wessling,H.C., Fisher,R.P. and Morgan,D.O.
  TITLE     Effects of phosphorylation by CAK on cyclin binding by CDC2 and
            CDK2
  JOURNAL   Mol Cell Biol 15 (1), 345-350 (1995)
   PUBMED   7799941
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Le Goff,P., Montano,M.M., Schodin,D.J. and Katzenellenbogen,B.S.
  TITLE     Phosphorylation of the human estrogen receptor. Identification of
            hormone-regulated sites and examination of their influence on
            transcriptional activity
  JOURNAL   J Biol Chem 269 (6), 4458-4466 (1994)
   PUBMED   8308015
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD701743.1, U61835.1,
            BC000820.1 and AL160236.4.
            
            Summary: The protein encoded by this gene, along with cyclin H and
            CDK7, forms the CDK-activating kinase (CAK) enzymatic complex. This
            complex activates several cyclin-associated kinases and can also
            associate with TFIIH to activate transcription by RNA polymerase
            II. Two transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region compared to variant 1. The resulting protein (isoform 2) is
            shorter but has the same N- and C-termini compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.14807.1, U61835.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.1"
     Protein         1..267
                     /product="CDK-activating kinase assembly factor MAT1
                     isoform 2"
                     /note="menage a trois 1 (CAK assembly factor); cyclin G1
                     interacting protein; CDK-activating kinase assembly factor
                     MAT1; MNAT1, CDK activating kinase assembly factor; menage
                     a trois homolog 1, cyclin H assembly factor; RING finger
                     protein 66; RING finger protein MAT1; CDK7/cyclin-H
                     assembly factor; menage a trois-like protein 1 cyclin H
                     assembly factor; MNAT CDK-activating kinase assembly
                     factor 1"
                     /calculated_mol_wt=31017
     Region          1..267
                     /region_name="cdk7"
                     /note="CDK-activating kinase assembly factor MAT1;
                     TIGR00570"
                     /db_xref="CDD:129661"
     CDS             1..267
                     /gene="MNAT1"
                     /gene_synonym="CAP35; MAT1; RNF66; TFB3"
                     /coded_by="NM_001177963.2:103..906"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53899.1"
                     /db_xref="GeneID:4331"
                     /db_xref="HGNC:HGNC:7181"
                     /db_xref="MIM:602659"
ORIGIN      
        1 mddqgcprck ttkyrnpslk lmvnvcghtl cescvdllfv rgagncpecg tplrksnfrv
       61 qlfedptvdk eveirkkvlk iynkreedfp slreyndfle eveeivfnlt nnvdldntkk
      121 kmeiyqkenk dviqknklkl treqeeleea leverqeneq rrlfiqkeeq lqqilkrknk
      181 qafldelgqh islapihkle ealyeyqplq ietygphvpe lemlgrlgyl nhvraaspqd
      241 laggytssla chralqdafs glfwqps
//
LOCUS       NP_001354209             692 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor C isoform 9 precursor [Homo sapiens].
ACCESSION   NP_001354209 XP_016862835
VERSION     NP_001354209.1
DBSOURCE    REFSEQ: accession NM_001367280.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Arikan,S., Ozturk,O., Duygulu,S., Atalay,E.O. and Atalay,A.
  TITLE     Associations of IL-17 and IL-17 receptor polymorphisms with
            Behcet's disease in Denizli Province of Turkey
  JOURNAL   Immunol Res 71 (4), 600-608 (2023)
   PUBMED   36701075
  REMARK    GeneRIF: Associations of IL-17 and IL-17 receptor polymorphisms
            with Behcet's disease in Denizli Province of Turkey.
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Kang,J.H., Park,S., Rho,J., Hong,E.J., Cho,Y.E., Won,Y.S. and
            Kwon,H.J.
  TITLE     IL-17A promotes Helicobacter pylori-induced gastric carcinogenesis
            via interactions with IL-17RC
  JOURNAL   Gastric Cancer 26 (1), 82-94 (2023)
   PUBMED   36125689
  REMARK    GeneRIF: IL-17A promotes Helicobacter pylori-induced gastric
            carcinogenesis via interactions with IL-17RC.
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Goepfert,A., Barske,C., Lehmann,S., Wirth,E., Willemsen,J.,
            Gudjonsson,J.E., Ward,N.L., Sarkar,M.K., Hemmig,R., Kolbinger,F.
            and Rondeau,J.M.
  TITLE     IL-17-induced dimerization of IL-17RA drives the formation of the
            IL-17 signalosome to potentiate signaling
  JOURNAL   Cell Rep 41 (3), 111489 (2022)
   PUBMED   36260993
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Huang,X., Li,Z., Shen,X., Nie,N. and Shen,Y.
  TITLE     IL-17 upregulates MCP-1 expression via Act1 / TRAF6 / TAK1 in
            experimental autoimmune myocarditis
  JOURNAL   Cytokine 152, 155823 (2022)
   PUBMED   35183823
  REMARK    Erratum:[Cytokine. 2022 Jun;154:155879. doi:
            10.1016/j.cyto.2022.155879. PMID: 35413623]
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Schmidt,T., Luebbe,J., Kilian,C., Riedel,J.H., Hiekmann,S.,
            Asada,N., Ginsberg,P., Robben,L., Song,N., Kaffke,A., Peters,A.,
            Borchers,A., Flavell,R.A., Gagliani,N., Pelzcar,P., Huber,S.,
            Huber,T.B., Turner,J.E., Paust,H.J., Krebs,C.F. and Panzer,U.
  TITLE     IL-17 Receptor C Signaling Controls CD4+ TH17 Immune Responses and
            Tissue Injury in Immune-Mediated Kidney Diseases
  JOURNAL   J Am Soc Nephrol 32 (12), 3081-3098 (2021)
   PUBMED   35167487
  REMARK    GeneRIF: IL-17 Receptor C Signaling Controls CD4(+) TH17 Immune
            Responses and Tissue Injury in Immune-Mediated Kidney Diseases.
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Haudenschild,D.R., Curtiss,S.B., Moseley,T.A. and Reddi,A.H.
  TITLE     Generation of interleukin-17 receptor-like protein (IL-17RL) in
            prostate by alternative splicing of RNA
  JOURNAL   Prostate 66 (12), 1268-1274 (2006)
   PUBMED   16688746
  REMARK    GeneRIF: IL-17RL exists as multiple isoforms due to extensive
            alternative splicing. Changes in RNA IL-17RL splicing occur in
            advanced cancers.
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Gerritsen,M.E., Tomlinson,J.E., Zlot,C., Ziman,M. and Hwang,S.
  TITLE     Using gene expression profiling to identify the molecular basis of
            the synergistic actions of hepatocyte growth factor and vascular
            endothelial growth factor in human endothelial cells
  JOURNAL   Br J Pharmacol 140 (4), 595-610 (2003)
   PUBMED   14504135
  REMARK    Review article
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Haudenschild,D., Moseley,T., Rose,L. and Reddi,A.H.
  TITLE     Soluble and transmembrane isoforms of novel interleukin-17
            receptor-like protein by RNA splicing and expression in prostate
            cancer
  JOURNAL   J Biol Chem 277 (6), 4309-4316 (2002)
   PUBMED   11706037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018809.5.
            
            On Nov 16, 2018 this sequence version replaced XP_016862835.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that shares similarity with the interleukin-17 receptor (IL-17RA).
            Unlike IL-17RA, which is predominantly expressed in hemopoietic
            cells, and binds with high affinity to only IL-17A, this protein is
            expressed in nonhemopoietic tissues, and binds both IL-17A and
            IL-17F with similar affinities. The proinflammatory cytokines,
            IL-17A and IL-17F, have been implicated in the progression of
            inflammatory and autoimmune diseases. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            detected for this gene, and it has been proposed that soluble,
            secreted proteins lacking transmembrane and intracellular domains
            may function as extracellular antagonists to cytokine signaling.
            [provided by RefSeq, Feb 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.234409.1,
                                           SRR3476690.779486.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..692
                     /product="interleukin-17 receptor C isoform 9 precursor"
                     /note="IL17F receptor; IL-17RL; IL17Rhom; zcytoR14; IL-17
                     receptor C; interleukin-17 receptor homolog;
                     interleukin-17 receptor-like protein"
                     /calculated_mol_wt=73268
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          71..444
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          491..638
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..692
                     /gene="IL17RC"
                     /gene_synonym="CANDF9; IL17-RL; IL17RL"
                     /coded_by="NM_001367280.1:219..2297"
                     /note="isoform 9 precursor is encoded by transcript
                     variant 10"
                     /db_xref="CCDS:CCDS93202.1"
                     /db_xref="GeneID:84818"
                     /db_xref="HGNC:HGNC:18358"
                     /db_xref="MIM:610925"
ORIGIN      
        1 mpvpwfllsl algrspvvls lerlvgpqda thcspglscr lwdsdilclp gdivpapgpv
       61 lapthlqtel vlrcqketdc dlclrvavhl avhghweepe deekfggaad sgveeprnas
      121 lqaqvvlsfq ayptarcvll evqvpaalvq fgqsvgsvvy dcfeaalgse vriwsytqpr
      181 yekelnhtqq lpalpwlnvs adgdnvhlvl nvseeqhfgl slywnqvqgp pkprwhknlt
      241 gpqiitlnht dlvpclciqv wplepdsvrt nicpfredpr ahqnlwqaar lqlltlqswl
      301 ldapcslpae aalcwrapgg dpcqplvppl swenvtvdkv lefpllkghp nlcvqvnsse
      361 klqlqeclwa dslgplkddv llletrgpqd nrslcaleps gctslpskas traarlgeyl
      421 lqdlqsgqcl qlwdddlgal wacpmdkyih krwalvwlac llfaaalsli lllkkdhaka
      481 aargraalll ysaddsgfer lvgalasalc qlplrvavdl wsrrelsaqg pvawfhaqrr
      541 qtlqeggvvv llfspgaval csewlqdgvs gpgahgphda fraslscvlp dflqgrapgs
      601 yvgacfdrll hpdavpalfr tvpvftlpsq lpdflgalqq praprsgrlq eraeqvsral
      661 qpaldsyfhp pgtpapgrgv gpgagpgagd gt
//
LOCUS       NP_001356629             264 aa            linear   PRI 20-NOV-2025
DEFINITION  NF-kappa-B inhibitor beta isoform 4 [Homo sapiens].
ACCESSION   NP_001356629
VERSION     NP_001356629.1
DBSOURCE    REFSEQ: accession NM_001369700.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Suyang,H., Phillips,R., Douglas,I. and Ghosh,S.
  TITLE     Role of unphosphorylated, newly synthesized I kappa B beta in
            persistent activation of NF-kappa B
  JOURNAL   Mol Cell Biol 16 (10), 5444-5449 (1996)
   PUBMED   8816457
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Beauparlant,P., Kwon,H., Clarke,M., Lin,R., Sonenberg,N.,
            Wainberg,M. and Hiscott,J.
  TITLE     Transdominant mutants of I kappa B alpha block Tat-tumor necrosis
            factor synergistic activation of human immunodeficiency virus type
            1 gene expression and virus multiplication
  JOURNAL   J Virol 70 (9), 5777-5785 (1996)
   PUBMED   8709193
REFERENCE   8  (residues 1 to 264)
  AUTHORS   DiDonato,J., Mercurio,F., Rosette,C., Wu-Li,J., Suyang,H., Ghosh,S.
            and Karin,M.
  TITLE     Mapping of the inducible IkappaB phosphorylation sites that signal
            its ubiquitination and degradation
  JOURNAL   Mol Cell Biol 16 (4), 1295-1304 (1996)
   PUBMED   8657102
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Harhaj,E., Blaney,J., Millhouse,S. and Sun,S.C.
  TITLE     Differential effects of I kappa B molecules on Tat-mediated
            transactivation of HIV-1 LTR
  JOURNAL   Virology 216 (1), 284-287 (1996)
   PUBMED   8615004
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011455.6.
            
            Summary: The protein encoded by this gene belongs to the NF-kappa-B
            inhibitor family, which inhibit NF-kappa-B by complexing with, and
            trapping it in the cytoplasm. Phosphorylation of serine residues on
            these proteins by kinases marks them for destruction via the
            ubiquitination pathway, thereby allowing activation of the
            NF-kappa-B, which translocates to the nucleus to function as a
            transcription factor. Alternatively spliced transcript variants
            have been found for this gene.[provided by RefSeq, Jul 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.328360.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145893, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..264
                     /product="NF-kappa-B inhibitor beta isoform 4"
                     /note="NF-kappa-B inhibitor beta; ikB-B; nuclear factor of
                     kappa light polypeptide gene enhancer in B-cells
                     inhibitor, beta; TRIP-9; ikB-beta; ikappaBbeta;
                     NF-kappa-BIB; I-kappa-B-beta; TR-interacting protein 9;
                     thyroid receptor-interacting protein 9"
                     /calculated_mol_wt=27795
     Region          <56..206
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          57..112
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(114,116,120..121,124..126,128..129,133,136,145,147,
                     150,154..155,158..160,162..163,167,170,179,181,183,
                     187..188,191..193,195..196,200,203)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          114..145
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          147..179
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          181..206
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     CDS             1..264
                     /gene="NFKBIB"
                     /gene_synonym="IKBB; TRIP9"
                     /coded_by="NM_001369700.1:65..859"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:4793"
                     /db_xref="HGNC:HGNC:7798"
                     /db_xref="MIM:604495"
ORIGIN      
        1 magvaclgka adadewcdsg lgslgpdaaa pggpglgael gpglswaplv fgyvtedgdt
       61 alhlavihqh epfldfllgf sagteymdlq ndlgqeeees eedwklqlea enyeghtplh
      121 vavihkdvem vrllrdagad ldkpeptcgr splhlaveaq aadvlelllr aganpaarmy
      181 ggrtplgsam lrpnpilarl lrahgapepe gedeksgpcs sssdsdsgde gdeyddivvh
      241 ssrsqtrlpp tpaskplpdd prpv
//
LOCUS       NP_001356799            1165 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001356799
VERSION     NP_001356799.1
DBSOURCE    REFSEQ: accession NM_001369870.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1165)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1165)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1165)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1165)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1165)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1165)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1165)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1165)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1165)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162730.26, AL590238.9 and
            AL358113.21.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1909915.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1165
                     /product="tight junction protein 2 isoform 6"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=131063
     Region          9..95
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(20..26,44,47,75,79,82..83)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Region          121..>203
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Region          160..>251
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Region          283..361
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(283..289,294..310,313..315,318,320..321,328,
                     336..337,339..340,352..358)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(295..301,307,310,340,344,347..348)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Region          484..565
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(495..501,511,514,543,547,550..551)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Region          579..641
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(588,590,593,597,618..619,635,637..638)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          675..854
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     CDS             1..1165
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_001369870.1:358..3855"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 meeliweqyt vtlqkdskrg fgiavsggrd nphfengets ivisdvlpgg padgllqend
       61 rvvmvngtpm edvlhsfavq qlrksgkvaa ivvkrprkvq vaalqasppl dqddrafevm
      121 defdgrsfrs gysersrlns hggrsrswed spergrpher arsrerdlsr drsrgrsler
      181 gldqdhartr drsrgrsler gldhdfgpsr drdrdrsrgr sidqdyeray hraydpdyer
      241 ayspeyrrga rhdarsrgpr srsrehphsr spspeprgrp gpigvllmks raneeyglrl
      301 gsqifvkemt rtglatkdgn lhegdiilki ngtvtenmsl tdarklieks rgklqlvvlr
      361 dsqqtlinip slndsdseie diseiesnrs fspeerrhqy sdydyhssse klkerpredt
      421 psrlsrmgat ptpfkstgdi agtvvpetnk epryqedppa pqpkaaprtf lrpspedeai
      481 ygpntkmvrf kkgdsvglrl aggndvgifv agiqegtsae qeglqegdqi lkvntqdfrg
      541 lvredavlyl leipkgemvt ilaqsradvy rdilacgrgd sffirshfec eketpqslaf
      601 trgevfrvvd tlydgklgnw lavrignele kglipnksra eqmasvqnaq rdnagdradf
      661 wrmrgqrsgv kknlrksred ltavvsvstk fpayervllr eagfkrpvvl fgpiadiame
      721 klanelpdwf qtaktepkda gsekstgvvr lntvrqiieq dkhalldvtp kavdllnytq
      781 wfpiviffnp dsrqgvktmr qrlnptsnks srklfdqank lkktcahlft atinlnsand
      841 swfgslkdti qhqqgeavwv segkmegmdd dpedrmsylt amgadylscd srlisdfedt
      901 dgeggaytdn eldepaeepl vssitrssep vqheesirkp spepraqmrr aassdqlrdn
      961 spppafkpep pkaktqnkee sydfsksyey ksnpsavagn etpgastkgy pppvaakptf
     1021 grsilkpstp ippqegeevg esseeqdnap ksvlgkvkif ekmdhkarlq rmqelqeaqn
     1081 arieiaqkhp diyavpikth kpdpgtpqht ssrppepqka psrpyqdtrg sygsdaeeee
     1141 yrqqlsehsk rgyygqsary rdtel
//
LOCUS       NP_002054                452 aa            linear   PRI 20-NOV-2025
DEFINITION  glycine receptor subunit alpha-2 isoform A precursor [Homo
            sapiens].
ACCESSION   NP_002054
VERSION     NP_002054.1
DBSOURCE    REFSEQ: accession NM_002063.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 452)
  AUTHORS   Tian,Q., Tong,P., Chen,G., Deng,M., Cai,T., Tian,R., Zhang,Z.,
            Xia,K. and Hu,Z.
  TITLE     GLRA2 gene mutations cause high myopia in humans and mice
  JOURNAL   J Med Genet 60 (2), 193-203 (2023)
   PUBMED   35396272
  REMARK    GeneRIF: GLRA2 gene mutations cause high myopia in humans and mice.
REFERENCE   2  (residues 1 to 452)
  AUTHORS   Aboheimed,G.I., AlRasheed,M.M., Almudimeegh,S., Pena-Guerra,K.A.,
            Cardona-Londono,K.J., Salih,M.A., Seidahmed,M.Z., Al-Mohanna,F.,
            Colak,D., Harvey,R.J., Harvey,K., Arold,S.T., Kaya,N. and Ruiz,A.J.
  TITLE     Clinical, genetic, and functional characterization of the glycine
            receptor beta-subunit A455P variant in a family affected by
            hyperekplexia syndrome
  JOURNAL   J Biol Chem 298 (7), 102018 (2022)
   PUBMED   35526563
REFERENCE   3  (residues 1 to 452)
  AUTHORS   Raltschev,C., Hetsch,F., Winkelmann,A., Meier,J.C. and Semtner,M.
  TITLE     Electrophysiological Signature of Homomeric and Heteromeric Glycine
            Receptor Channels
  JOURNAL   J Biol Chem 291 (34), 18030-18040 (2016)
   PUBMED   27382060
  REMARK    GeneRIF: data show that the current-voltage relationships of
            homomeric channels formed by the alpha2 or alpha3 subunits change
            upon receptor desensitization from a linear to an inwardly
            rectifying shape, in contrast to their heteromeric counterparts.
REFERENCE   4  (residues 1 to 452)
  AUTHORS   McCracken,L.M., Trudell,J.R., McCracken,M.L. and Harris,R.A.
  TITLE     Zinc-dependent modulation of alpha2- and alpha3-glycine receptor
            subunits by ethanol
  JOURNAL   Alcohol Clin Exp Res 37 (12), 2002-2010 (2013)
   PUBMED   23895467
REFERENCE   5  (residues 1 to 452)
  AUTHORS   Wegner,F., Kraft,R., Busse,K., Hartig,W., Ahrens,J., Leffler,A.,
            Dengler,R. and Schwarz,J.
  TITLE     Differentiated human midbrain-derived neural progenitor cells
            express excitatory strychnine-sensitive glycine receptors
            containing alpha2beta subunits
  JOURNAL   PLoS One 7 (5), e36946 (2012)
   PUBMED   22606311
  REMARK    GeneRIF: investigated neural progenitor cells in respect to their
            glycine receptor function and subunit expression using
            electrophysiology, calcium imaging, immunocytochemistry, and
            quantitative real-time PCR
REFERENCE   6  (residues 1 to 452)
  AUTHORS   Davies,D.L., Crawford,D.K., Trudell,J.R., Mihic,S.J. and
            Alkana,R.L.
  TITLE     Multiple sites of ethanol action in alpha1 and alpha2 glycine
            receptors suggested by sensitivity to pressure antagonism
  JOURNAL   J Neurochem 89 (5), 1175-1185 (2004)
   PUBMED   15147510
  REMARK    GeneRIF: Effects of 12 times normal atmospheric pressure of
            helium-oxygen gas (pressure) on ethanol-induced potentiation of
            GlyR function in Xenopus oocytes expressing human alpha1, alpha2 or
            the mutant alpha1(A52S) GlyRs were measured by voltage clamp
            technics
REFERENCE   7  (residues 1 to 452)
  AUTHORS   Feng,J., Craddock,N., Jones,I.R., Cook,E.H. Jr., Goldman,D.,
            Heston,L.L., Peltonen,L., DeLisi,L.E. and Sommer,S.S.
  TITLE     Systematic screening for mutations in the glycine receptor alpha2
            subunit gene (GLRA2) in patients with schizophrenia and other
            psychiatric diseases
  JOURNAL   Psychiatr Genet 11 (1), 45-48 (2001)
   PUBMED   11409700
REFERENCE   8  (residues 1 to 452)
  AUTHORS   Cummings,C.J., Dahle,E.J. and Zoghbi,H.Y.
  TITLE     Analysis of the genomic structure of the human glycine receptor
            alpha2 subunit gene and exclusion of this gene as a candidate for
            Rett syndrome
  JOURNAL   Am J Med Genet 78 (2), 176-178 (1998)
   PUBMED   9674912
REFERENCE   9  (residues 1 to 452)
  AUTHORS   Monani,U. and Burghes,A.H.
  TITLE     Structure of the human alpha 2 subunit gene of the glycine
            receptor--use of vectorette and Alu-exon PCR
  JOURNAL   Genome Res 6 (12), 1200-1206 (1996)
   PUBMED   8973915
REFERENCE   10 (residues 1 to 452)
  AUTHORS   Grenningloh,G., Schmieden,V., Schofield,P.R., Seeburg,P.H.,
            Siddique,T., Mohandas,T.K., Becker,C.M. and Betz,H.
  TITLE     Alpha subunit variants of the human glycine receptor: primary
            structures, functional expression and chromosomal localization of
            the corresponding genes
  JOURNAL   EMBO J 9 (3), 771-776 (1990)
   PUBMED   2155780
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA495302.1, AY437083.1,
            BC045547.1 and AA081959.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The glycine receptor consists of two subunits, alpha and
            beta, and acts as a pentamer. The protein encoded by this gene is
            an alpha subunit and can bind strychnine. Several transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Jan 2010].
            
            Transcript Variant: This variant (1) encodes isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC045547.1, BC032864.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000218075.9/ ENSP00000218075.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..452
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..452
                     /product="glycine receptor subunit alpha-2 isoform A
                     precursor"
                     /note="glycine receptor subunit alpha-2; glycine receptor,
                     alpha-2 polypeptide; glycine receptor alpha 2 subunit"
                     /calculated_mol_wt=48802
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3219
     mat_peptide     28..452
                     /product="glycine receptor subunit alpha-2 isoform A"
                     /calculated_mol_wt=48802
     Region          46..441
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            257..278
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            284..304
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            295
                     /site_type="other"
                     /note="Important for obstruction of the ion pore in the
                     closed conformation.
                     /evidence=ECO:0000250|UniProtKB:P23415; propagated from
                     UniProtKB/Swiss-Prot (P23416.1)"
     Site            316..336
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     Site            421..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P23416.1)"
     CDS             1..452
                     /gene="GLRA2"
                     /gene_synonym="GLR; MRXSP"
                     /coded_by="NM_002063.4:523..1881"
                     /note="isoform A precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS14160.1"
                     /db_xref="GeneID:2742"
                     /db_xref="HGNC:HGNC:4327"
                     /db_xref="MIM:305990"
ORIGIN      
        1 mnrqlvnilt alfaffletn hfrtafckdh dsrsgkqpsq tlspsdfldk lmgrtsgyda
       61 rirpnfkgpp vnvtcnifin sfgsvtettm dyrvniflrq qwndsrlays eypddsldld
      121 psmldsiwkp dlffanekga nfhdvttdnk llriskngkv lysirltltl scpmdlknfp
      181 mdvqtctmql esfgytmndl ifewlsdgpv qvaegltlpq filkeekelg yctkhyntgk
      241 ftcievkfhl erqmgyyliq myipsllivi lswvsfwinm daaparvalg ittvltmttq
      301 ssgsraslpk vsyvkaidiw mavcllfvfa alleyaavnf vsrqhkeflr lrrrqkrqnk
      361 eedvtresrf nfsgygmghc lqvkdgtavk atpanplpqp pkdgdaikkk fvdrakridt
      421 israafplaf lifnifywit ykiirhedvh kk
//
LOCUS       NP_003860                559 aa            linear   PRI 20-NOV-2025
DEFINITION  cocaine esterase isoform 1 precursor [Homo sapiens].
ACCESSION   NP_003860
VERSION     NP_003860.3
DBSOURCE    REFSEQ: accession NM_003869.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Chen,X., Liu,Q., Chen,Y., Wang,L., Yang,R., Zhang,W., Pan,X.,
            Zhang,S., Chen,C., Wu,T., Xia,J., Cheng,B., Chen,X. and Ren,X.
  TITLE     Carboxylesterase 2 induces mitochondrial dysfunction via disrupting
            lipid homeostasis in oral squamous cell carcinoma
  JOURNAL   Mol Metab 65, 101600 (2022)
   PUBMED   36113774
  REMARK    GeneRIF: Carboxylesterase 2 induces mitochondrial dysfunction via
            disrupting lipid homeostasis in oral squamous cell carcinoma.
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Shen,Y., Eades,W., Liu,W. and Yan,B.
  TITLE     The COVID-19 Oral Drug Molnupiravir Is a CES2 Substrate: Potential
            Drug-Drug Interactions and Impact of CES2 Genetic Polymorphism In
            Vitro
  JOURNAL   Drug Metab Dispos 50 (9), 1151-1160 (2022)
   PUBMED   35790245
  REMARK    GeneRIF: The COVID-19 Oral Drug Molnupiravir Is a CES2 Substrate:
            Potential Drug-Drug Interactions and Impact of CES2 Genetic
            Polymorphism In Vitro.
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Song,Y.Q., Guan,X.Q., Weng,Z.M., Liu,J.L., Chen,J., Wang,L.,
            Cui,L.T., Fang,S.Q., Hou,J. and Ge,G.B.
  TITLE     Discovery of hCES2A inhibitors from Glycyrrhiza inflata via
            combination of docking-based virtual screening and
            fluorescence-based inhibition assays
  JOURNAL   Food Funct 12 (1), 162-176 (2021)
   PUBMED   33291124
  REMARK    GeneRIF: Discovery of hCES2A inhibitors from Glycyrrhiza inflata
            via combination of docking-based virtual screening and
            fluorescence-based inhibition assays.
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Pei,J., Sun,X., Yang,G. and Zhang,S.
  TITLE     LncRNA KCNQ1OT1 ameliorates the liver injury induced by
            acetaminophen through the regulation of miR-122-5p/CES2 axis
  JOURNAL   Mol Cell Biochem 475 (1-2), 107-118 (2020)
   PUBMED   32779042
  REMARK    GeneRIF: LncRNA KCNQ1OT1 ameliorates the liver injury induced by
            acetaminophen through the regulation of miR-122-5p/CES2 axis.
REFERENCE   6  (residues 1 to 559)
  AUTHORS   Saito,S., Iida,A., Sekine,A., Kawauchi,S., Higuchi,S., Ogawa,C. and
            Nakamura,Y.
  TITLE     Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
            nine esterase genes, and two other genes in the Japanese population
  JOURNAL   J Hum Genet 48 (5), 249-270 (2003)
   PUBMED   12721789
REFERENCE   7  (residues 1 to 559)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
REFERENCE   8  (residues 1 to 559)
  AUTHORS   Yan,B., Matoney,L. and Yang,D.
  TITLE     Human carboxylesterases in term placentae: enzymatic
            characterization, molecular cloning and evidence for the existence
            of multiple forms
  JOURNAL   Placenta 20 (7), 599-607 (1999)
   PUBMED   10452915
REFERENCE   9  (residues 1 to 559)
  AUTHORS   Pindel,E.V., Kedishvili,N.Y., Abraham,T.L., Brzezinski,M.R.,
            Zhang,J., Dean,R.A. and Bosron,W.F.
  TITLE     Purification and cloning of a broad substrate specificity human
            liver carboxylesterase that catalyzes the hydrolysis of cocaine and
            heroin
  JOURNAL   J Biol Chem 272 (23), 14769-14775 (1997)
   PUBMED   9169443
REFERENCE   10 (residues 1 to 559)
  AUTHORS   Schwer,H., Langmann,T., Daig,R., Becker,A., Aslanidis,C. and
            Schmitz,G.
  TITLE     Molecular cloning and characterization of a novel putative
            carboxylesterase, present in human intestine and liver
  JOURNAL   Biochem Biophys Res Commun 233 (1), 117-120 (1997)
   PUBMED   9144407
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032095.2 and BX538086.1.
            
            On Aug 23, 2018 this sequence version replaced NP_003860.2.
            
            Summary: This gene encodes a member of the carboxylesterase large
            family. The family members are responsible for the hydrolysis or
            transesterification of various xenobiotics, such as cocaine and
            heroin, and endogenous substrates with ester, thioester, or amide
            bonds. They may participate in fatty acyl and cholesterol ester
            metabolism, and may play a role in the blood-brain barrier system.
            The protein encoded by this gene is the major intestinal enzyme and
            functions in intestine drug clearance. Alternatively spliced
            transcript variants have been found for this gene.[provided by
            RefSeq, Oct 2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1) and contains a longer 5' UTR than some of the other variants.
            This variant represent use of an alternate promote that is used in
            some tissues, and uses a downstream start codon. The  upstream
            start codon is not well conserved.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.275156.1,
                                           SRR1803617.161983.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..559
                     /product="cocaine esterase isoform 1 precursor"
                     /EC_number="3.1.1.1"
                     /EC_number="3.1.1.84"
                     /EC_number="3.1.1.56"
                     /note="intestinal carboxylesterase; liver
                     carboxylesterase-2; carboxylesterase 2 (intestine, liver);
                     cocaine esterase; methylumbelliferyl-acetate deacetylase
                     2"
                     /calculated_mol_wt=58952
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2874
     mat_peptide     27..559
                     /product="Cocaine esterase. /id=PRO_0000008572"
                     /note="propagated from UniProtKB/Swiss-Prot (O00748.1)"
                     /calculated_mol_wt=58952
     Site            27
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000250|UniProtKB:P14943; propagated from
                     UniProtKB/Swiss-Prot (O00748.1)"
     Region          30..538
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O00748.1)"
     Site            order(148..150,227..229,232,374,378..379,411,458,461)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(228,345,457)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     Site            276
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O00748.1)"
     Region          556..559
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00748.1)"
     CDS             1..559
                     /gene="CES2"
                     /gene_synonym="CE-2; CES2A1; iCE; PCE-2"
                     /coded_by="NM_003869.6:1166..2845"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10825.2"
                     /db_xref="GeneID:8824"
                     /db_xref="HGNC:HGNC:1864"
                     /db_xref="MIM:605278"
ORIGIN      
        1 mrlhrlrarl savacgllll lvrgqgqdsa spirtthtgq vlgslvhvkg anagvqtflg
       61 ipfakpplgp lrfappeppe swsgvrdgtt hpamclqdlt aveseflsqf nmtfpsdsms
      121 edclylsiyt pahshegsnl pvmvwihgga lvfgmaslyd gsmlaalenv vvviiqyrlg
      181 vlgffstgdk hatgnwgyld qvaalrwvqq niahfggnpd rvtifgesag gtsvsslvvs
      241 pisqglfhga imesgvallp gliassadvi stvvanlsac dqvdsealvg clrgkskeei
      301 lainkpfkmi pgvvdgvflp rhpqellasa dfqpvpsivg vnnnefgwli pkvmriydtq
      361 kemdreasqa alqkmltllm lpptfgdllr eeyigdngdp qtlqaqfqem madsmfvipa
      421 lqvahfqcsr apvyfyefqh qpswlknirp phmkadhgde lpfvfrsffg gnyikfteee
      481 eqlsrkmmky wanfarngnp ngeglphwpl fdqeeqylql nlqpavgral kahrlqfwkk
      541 alpqkiqele epeerhtel
//
LOCUS       NP_008860               1246 aa            linear   PRI 20-NOV-2025
DEFINITION  superkiller complex protein 2 [Homo sapiens].
ACCESSION   NP_008860
VERSION     NP_008860.4
DBSOURCE    REFSEQ: accession NM_006929.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1246)
  AUTHORS   Nicholson-Shaw,T., Dowdle,M.E., Ajaj,Y., Perelis,M., Fulzele,A.,
            Yeo,G.W., Bennett,E.J. and Lykke-Andersen,J.
  TITLE     Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay
            factor
  JOURNAL   RNA 31 (8), 1195-1205 (2025)
   PUBMED   40441874
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1246)
  AUTHORS   Kogel,A., Keidel,A., Bonneau,F., Schafer,I.B. and Conti,E.
  TITLE     The human SKI complex regulates channeling of ribosome-bound RNA to
            the exosome via an intrinsic gatekeeping mechanism
  JOURNAL   Mol Cell 82 (4), 756-769 (2022)
   PUBMED   35120588
REFERENCE   3  (residues 1 to 1246)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1246)
  AUTHORS   Zinoviev,A., Ayupov,R.K., Abaeva,I.S., Hellen,C.U.T. and
            Pestova,T.V.
  TITLE     Extraction of mRNA from Stalled Ribosomes by the Ski Complex
  JOURNAL   Mol Cell 77 (6), 1340-1349 (2020)
   PUBMED   32006463
REFERENCE   5  (residues 1 to 1246)
  AUTHORS   Bourgeois,P., Esteve,C., Chaix,C., Beroud,C., Levy,N., Fabre,A. and
            Badens,C.
  CONSRTM   THES clinical consortium
  TITLE     Tricho-Hepato-Enteric Syndrome mutation update: Mutations spectrum
            of TTC37 and SKIV2L, clinical analysis and future prospects
  JOURNAL   Hum Mutat 39 (6), 774-789 (2018)
   PUBMED   29527791
  REMARK    GeneRIF: We then examined the lab diagnostic cohort in detail for
            clinical manifestations. For the first time, we are able to suggest
            that patients lacking SKIV2L seem more severely affected than those
            lacking TTC37, in terms of liver damage and prenatal growth
            impairment.
            Review article
REFERENCE   6  (residues 1 to 1246)
  AUTHORS   Albertella,M.R., Jones,H., Thomson,W., Olavesen,M.G. and
            Campbell,R.D.
  TITLE     Localization of eight additional genes in the human major
            histocompatibility complex, including the gene encoding the casein
            kinase II beta subunit (CSNK2B)
  JOURNAL   Genomics 36 (2), 240-251 (1996)
   PUBMED   8812450
REFERENCE   7  (residues 1 to 1246)
  AUTHORS   Dangel,A.W., Shen,L., Mendoza,A.R., Wu,L.C. and Yu,C.Y.
  TITLE     Human helicase gene SKI2W in the HLA class III region exhibits
            striking structural similarities to the yeast antiviral gene SKI2
            and to the human gene KIAA0052: emergence of a new gene family
  JOURNAL   Nucleic Acids Res 23 (12), 2120-2126 (1995)
   PUBMED   7610041
REFERENCE   8  (residues 1 to 1246)
  AUTHORS   Lee,S.G., Lee,I., Park,S.H., Kang,C. and Song,K.
  TITLE     Identification and characterization of a human cDNA homologous to
            yeast SKI2
  JOURNAL   Genomics 25 (3), 660-666 (1995)
   PUBMED   7759100
REFERENCE   9  (residues 1 to 1246)
  AUTHORS   Shen,L., Wu,L.C., Sanlioglu,S., Chen,R., Mendoza,A.R., Dangel,A.W.,
            Carroll,M.C., Zipf,W.B. and Yu,C.Y.
  TITLE     Structure and genetics of the partially duplicated gene RP located
            immediately upstream of the complement C4A and the C4B genes in the
            HLA class III region. Molecular cloning, exon-intron structure,
            composite retroposon, and breakpoint of gene duplication
  JOURNAL   J Biol Chem 269 (11), 8466-8476 (1994)
   PUBMED   8132574
REFERENCE   10 (residues 1 to 1246)
  AUTHORS   Fabre,A., Bourgeois,P., Chaix,C., Bertaux,K., Goulet,O. and
            Badens,C.
  TITLE     Trichohepatoenteric Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29334452
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U09877.1, AL529319.3,
            BG396326.1, BE395851.1 and Z48796.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 15, 2005 this sequence version replaced NP_008860.3.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            which is a human homologue of yeast SKI2 and may be involved in
            antiviral activity by blocking translation of poly(A) deficient
            mRNAs. This gene is located in the class III region of the major
            histocompatibility complex. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Z48796.1, U09877.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375394.7/ ENSP00000364543.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1246
                     /product="superkiller complex protein 2"
                     /EC_number="3.6.4.13"
                     /note="helicase SKI2W; helicase-like protein; superkiller
                     viralicidic activity 2-like; SKI2 homolog, superkiller
                     viralicidic activity 2-like; Ski2 like RNA helicase; SKI2
                     subunit of superkiller complex protein"
                     /calculated_mol_wt=137625
     Region          79..201
                     /region_name="Ski2_N"
                     /note="Ski2 N-terminal region; pfam17911"
                     /db_xref="CDD:465562"
     Region          220..246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15477.3)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15477.3)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15477.3)"
     Region          309..1238
                     /region_name="Dob10"
                     /note="Superfamily II RNA helicase [Replication,
                     recombination and repair]; COG4581"
                     /db_xref="CDD:443638"
     Region          423..426
                     /region_name="DEVH box.
                     /evidence=ECO:0000305|PubMed:35120588"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15477.3)"
     CDS             1..1246
                     /gene="SKIC2"
                     /gene_synonym="170A; DDX13; HLP; SKI2; SKI2W; SKIV2;
                     SKIV2L; SKIV2L1; THES2"
                     /coded_by="NM_006929.5:19..3759"
                     /db_xref="CCDS:CCDS4731.1"
                     /db_xref="GeneID:6499"
                     /db_xref="HGNC:HGNC:10898"
                     /db_xref="MIM:600478"
ORIGIN      
        1 mmeterlvlp ppdpldlplr avelgctghw ellnlpgape sslphglppc apdlqqeaeq
       61 lflsspawlp lhgvehsark wqrktdpwsl lavlgapvps dlqaqrhptt gqilgykevl
      121 lentnlsatt slslrrppgp asqslwgnpt qypfwpggmd eptitdlntr eeaeeeidfe
      181 kdlltippgf kkgmdfapkd cptpapglls lscmlepldl gggdedenea vgqpggprgd
      241 tvsaspcsap larassledl vlkeastavs tpeapeppsq eqwaipvdat spvgdfyrli
      301 pqpafqwafe pdvfqkqail hlerhdsvfv aahtsagktv vaeyaialaq khmtrtiyts
      361 pikalsnqkf rdfrntfgdv glltgdvqlh peasclimtt eilrsmlysg sdvirdlewv
      421 ifdevhyind vergvvweev limlpdhvsi illsatvpna lefadwigrl krrqiyvist
      481 vtrpvplehy lftgnssktq gelfllldsr gafhtkgyya aveakkerms khaqtfgakq
      541 pthqggpaqd rgvylsllas lrtraqlpvv vftfsrgrcd eqasgltsld lttsseksei
      601 hlflqrclar lrgsdrqlpq vlhmsellnr glgvhhsgil pilkeiveml fsrglvkvlf
      661 atetfamgvn mpartvvfds mrkhdgstfr dllpgeyvqm agragrrgld ptgtvillck
      721 grvpemadlh rmmmgkpsql qsqfrltytm ilnllrvdal rvedmmkrsf sefpsrkdsk
      781 aheqalaelt krlgaleepd mtgqlvdlpe yyswgeelte tqhmiqrrim esvnglksls
      841 agrvvvvknq ehhnalgvil qvssnstsrv fttlvlcdkp lsqdpqdrgp ataevpypdd
      901 lvgfklflpe gpcdhtvvkl qpgdmaaitt kvlrvngeki ledfskrqqp kfkkdpplaa
      961 vttavqellr laqahpagpp tldpvndlql kdmsvveggl rarkleeliq gaqcvhsprf
     1021 paqylklrer mqiqkemerl rfllsdqsll llpeyhqrve vlrtlgyvde agtvklagrv
     1081 acamsshell ltelmfdnal stlrpeeiaa llsglvcqsp gdagdqlpnt lkqgiervra
     1141 vakrigevqv acglnqtvee fvgelnfglv evvyewargm pfselaglsg tpeglvvrci
     1201 qrlaemcrsl rgaarlvgep vlgakmetaa tllrrdivfa aslytq
//
LOCUS       NP_694962                442 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 39 [Homo sapiens].
ACCESSION   NP_694962
VERSION     NP_694962.1
DBSOURCE    REFSEQ: accession NM_153230.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Wu,J., Yao,F., Li,Y., Zhao,Z., Liu,J., Xu,T., Chai,J., Yang,Y.,
            Song,J., Tian,C., Jia,Q., Li,M. and Li,L.
  TITLE     The cancer-testis antigen FBXO39 predicts poor prognosis and is
            associated with stemness and aggressiveness in glioma
  JOURNAL   Pathol Res Pract 239, 154168 (2022)
   PUBMED   36244247
  REMARK    GeneRIF: The cancer-testis antigen FBXO39 predicts poor prognosis
            and is associated with stemness and aggressiveness in glioma.
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Ramadan,R.A., Morsy,H., Samir,M., Shamseya,M., Shalaby,M. and
            El-Attar,E.A.
  TITLE     Significance of cancer testis-associated antigens (SPAG9 and
            FBXO39) in colon cancer
  JOURNAL   Indian J Cancer 59 (3), 394-401 (2022)
   PUBMED   34380828
  REMARK    GeneRIF: Significance of cancer testis-associated antigens (SPAG9
            and FBXO39) in colon cancer.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Liu,Y.C., Yan,S., Liu,D.M., Pei,D.X. and Li,Y.W.
  TITLE     Aberrant Expression of Cancer-Testis Antigen FBXO39 in Breast
            Cancer and its Clinical Significance
  JOURNAL   Clin Lab 66 (9) (2020)
   PUBMED   32902238
  REMARK    GeneRIF: Aberrant Expression of Cancer-Testis Antigen FBXO39 in
            Breast Cancer and its Clinical Significance.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Motalebzadeh,J., Shabani,S., Rezayati,S., Shakournia,N.,
            Mirzaei,R., Mahjoubi,B., Hoseini,K. and Mahjoubi,F.
  TITLE     Prognostic Value of FBXO39 and ETS-1 but not BMI-1 in Iranian
            Colorectal Cancer Patients
  JOURNAL   Asian Pac J Cancer Prev 19 (5), 1357-1362 (2018)
   PUBMED   29802700
  REMARK    GeneRIF: High FBXO39 expression is associated with Colorectal
            Cancer.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Shin,S.Y., Fauman,E.B., Petersen,A.K., Krumsiek,J., Santos,R.,
            Huang,J., Arnold,M., Erte,I., Forgetta,V., Yang,T.P., Walter,K.,
            Menni,C., Chen,L., Vasquez,L., Valdes,A.M., Hyde,C.L., Wang,V.,
            Ziemek,D., Roberts,P., Xi,L., Grundberg,E., Waldenberger,M.,
            Richards,J.B., Mohney,R.P., Milburn,M.V., John,S.L., Trimmer,J.,
            Theis,F.J., Overington,J.P., Suhre,K., Brosnan,M.J., Gieger,C.,
            Kastenmuller,G., Spector,T.D. and Soranzo,N.
  CONSRTM   Multiple Tissue Human Expression Resource (MuTHER) Consortium
  TITLE     An atlas of genetic influences on human blood metabolites
  JOURNAL   Nat Genet 46 (6), 543-550 (2014)
   PUBMED   24816252
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Seifi-Alan,M., Shamsi,R., Ghafouri-Fard,S., Mirfakhraie,R.,
            Zare-Abdollahi,D., Movafagh,A., Modarressi,M.H., Kazemi,G.,
            Geranpayeh,L. and Najafi-Ashtiani,M.
  TITLE     Expression analysis of two cancer-testis genes, FBXO39 and TDRD4,
            in breast cancer tissues and cell lines
  JOURNAL   Asian Pac J Cancer Prev 14 (11), 6625-6629 (2014)
   PUBMED   24377578
  REMARK    GeneRIF: FBXO39 showed significant up-regulation in invasive ductal
            breast carcinoma.
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Song,M.H., Ha,J.C., Lee,S.M., Park,Y.M. and Lee,S.Y.
  TITLE     Identification of BCP-20 (FBXO39) as a cancer/testis antigen from
            colon cancer patients by SEREX
  JOURNAL   Biochem Biophys Res Commun 408 (2), 195-201 (2011)
   PUBMED   21338577
  REMARK    GeneRIF: These data suggest that the BCP-20 (FBXO39) gene is a new
            Cancer/Testis antigen and may be useful for diagnosis and
            immunotherapy.
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC034305.6, BM554273.1, BC034782.1, DB524242.1 and AI125619.1.
            
            Summary: Members of the F-box protein family, such as FBXO39, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.378380.1,
                                           SRR5189667.241396.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321535.5/ ENSP00000321386.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..442
                     /product="F-box only protein 39"
                     /calculated_mol_wt=52515
     Region          16..59
                     /region_name="F-box_FBXO39"
                     /note="F-box domain found in F-box only protein 39
                     (FBXO39) and similar proteins; cd22108"
                     /db_xref="CDD:438880"
     Site            order(19,23,26..27,30..31,35,37..38,42..44,46)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438880"
     CDS             1..442
                     /gene="FBXO39"
                     /gene_synonym="CT144; FBOX39; Fbx39"
                     /coded_by="NM_153230.3:139..1467"
                     /db_xref="CCDS:CCDS11082.1"
                     /db_xref="GeneID:162517"
                     /db_xref="HGNC:HGNC:28565"
                     /db_xref="MIM:609106"
ORIGIN      
        1 mdeeseliqp qdqscwaflp dlclcrvfww lgdrdrsraa lvcrkwnqmm ysaelwryrt
       61 itfsgrpsrv hasevesavw yvkkfgryle hlevkfmnpy navltkkfqv tmrgllscls
      121 ksnnrlksls iqyleldrlv wrnsirssfi sslsfflkkm gkrldylnlk garltveqgc
      181 qildslsymr nenviselni edyfshhlav ynspqfkktm stfhnlvsln lnyncisdel
      241 lenlcenast lrtinikchv hdphgqviwg mswaklarqa tnlkvnfffe rimkyerlar
      301 illqeipirs islrscyfsd pdcsmrptli dllptfrhtl qkltcefnnn hesldeelhl
      361 liiscrklfy fkiwafldvs fverilksqk erqcalrvfk ariytnryet needktlqei
      421 yrkyrklies elsyfvivys vm
//
LOCUS       NP_001311059             366 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and SAM domain-containing protein 3 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001311059
VERSION     NP_001311059.1
DBSOURCE    REFSEQ: accession NM_001324130.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Shamseldin,H.E., Yakulov,T.A., Hashem,A., Walz,G. and Alkuraya,F.S.
  TITLE     ANKS3 is mutated in a family with autosomal recessive laterality
            defect
  JOURNAL   Hum Genet 135 (11), 1233-1239 (2016)
   PUBMED   27417436
  REMARK    GeneRIF: Consistent with the proposed role of the ANKS3 variant in
            the pathogenesis of the reported family's phenotype, we show that
            the mutant RNA failed to rescue the laterality defect in anks3
            morphants compared to wild-type RNA. Furthermore, we describe a new
            mutant anks3 line that also displays laterality defect in the
            homozygous state
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Ramachandran,H., Engel,C., Muller,B., Dengjel,J., Walz,G. and
            Yakulov,T.A.
  TITLE     Anks3 alters the sub-cellular localization of the Nek7 kinase
  JOURNAL   Biochem Biophys Res Commun 464 (3), 901-907 (2015)
   PUBMED   26188091
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Leettola,C.N., Knight,M.J., Cascio,D., Hoffman,S. and Bowie,J.U.
  TITLE     Characterization of the SAM domain of the PKD-related protein ANKS6
            and its interaction with ANKS3
  JOURNAL   BMC Struct Biol 14, 17 (2014)
   PUBMED   24998259
  REMARK    GeneRIF: Study finds that ANKS3-SAM polymerizes and ANKS6-SAM can
            bind to one end of the polymer; study presents crystal structures
            of both the ANKS3-SAM polymer and the ANKS3-SAM/ANKS6-SAM complex,
            revealing the molecular details of their association.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 366)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020663.1 and AC023830.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.12265.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..366
                     /product="ankyrin repeat and SAM domain-containing protein
                     3 isoform 5"
                     /note="ankyrin repeat and SAM domain-containing protein 3"
                     /calculated_mol_wt=40160
     Region          134..197
                     /region_name="SAM_ANKS3"
                     /note="SAM domain of ANKS3 subfamily; cd09519"
                     /db_xref="CDD:188918"
     CDS             1..366
                     /gene="ANKS3"
                     /coded_by="NM_001324130.2:1276..2376"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:124401"
                     /db_xref="HGNC:HGNC:29422"
                     /db_xref="MIM:617310"
ORIGIN      
        1 mapprgyvtf nssgenplee eglccrdvts pinerdvess sssssreeha fcanlgpvqs
       61 sssseglara qglsseasve snedsdhack ssarkqaksy mktknpdsqw ppraatdreg
      121 flaesspqtq rapysgpqdl aalleqigcl kylqvfeeqd vdlrifltlt esdlkeigit
      181 lfgpkrkmts aiarwhssar ppgdalelay adrleaemqe laiqlhkrce eveatrgqvc
      241 qeqelravve sclleqdrar edlqarlret walardaalv ldqlracqae lssrvrqdqp
      301 pgaatlglav ppadskgwqa slqamslpel sgaledrvre mgqalclvtq sleklqvlng
      361 kkwret
//
LOCUS       NP_001339865             778 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 10 [Homo sapiens].
ACCESSION   NP_001339865
VERSION     NP_001339865.1
DBSOURCE    REFSEQ: accession NM_001352936.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 778)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 778)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 778)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 778)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 778)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 778)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 778)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 778)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 778)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 778)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.59707.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..778
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..778
                     /product="DNA repair-scaffolding protein isoform 10"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=86111
     Region          <25..299
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          451..>710
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..778
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352936.1:225..2561"
                     /note="isoform 10 is encoded by transcript variant 11"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 maqvwrrvse hfwesettts kstsgltdit wsssgsdlsd edktlsqlqr delqfidwei
       61 dsdraeasdc defeddegav eisdcascas nqsltsdekl selpkpssie ileyssdsek
      121 eddlenvlli dsesphkyhv qfasdarqim erlidprtks tetilhtpqk ptakfprtpe
      181 nsakkkllrg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt vkilelheec
      241 amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv rifppwqkli
      301 ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi kgltnnspei
      361 qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga gvrvvvqrvy
      421 slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar qlegkscslv
      481 gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa lcyiltahpn
      541 lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql kslllleqre
      601 iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl ffkdalrdqg
      661 rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq elrseecprk
      721 gsgvvklfcp vrnrppdqlh wiggnrasec rrglcrtlav aagsvnfamw lqgwwwww
//
LOCUS       NP_001336357             319 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform c [Homo sapiens].
ACCESSION   NP_001336357 XP_016862151
VERSION     NP_001336357.1
DBSOURCE    REFSEQ: accession NM_001349428.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 319)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 319)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 319)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 319)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 319)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 319)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 319)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 319)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 319)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 319)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_016862151.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (17), as well as variant 18,
            encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.242580.1,
                                           SRR1803615.196615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..319
                     /product="kelch-like protein 24 isoform c"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=35211
     Region          34..282
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          73..112
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          116..160
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          163..208
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          211..248
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          255..297
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          264..310
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..319
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349428.1:1262..2221"
                     /note="isoform c is encoded by transcript variant 17"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mspllrqqfi pltsapvtll kllsirstgy sevivvvggc ervggfnlpy tecydpvtge
       61 wkslaklpef tkseyavcal rndilvsggr insrdvwiyn sqlniwirva slnkgrwrhk
      121 mavllgkvyv vggydgqnrl ssvecydsfs nrwtevaplk eavsspavts cvgklfvigg
      181 gpddntcsdk vqsydpetns wllraaipia krcitavsln nliyvagglt kaiycydpve
      241 dywmhvqntf srqencgmsv cngkiyilgg rrengeatdt ilcydpatsi itgvaamprp
      301 vsyhgcvtih rynekcfkl
//
LOCUS       NP_060104                389 aa            linear   PRI 20-NOV-2025
DEFINITION  BTB/POZ domain-containing protein KCTD9 [Homo sapiens].
ACCESSION   NP_060104 XP_005042
VERSION     NP_060104.2
DBSOURCE    REFSEQ: accession NM_017634.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 389)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 389)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 389)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 389)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 389)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 389)
  AUTHORS   Ji,A.X., Chu,A., Nielsen,T.K., Benlekbir,S., Rubinstein,J.L. and
            Prive,G.G.
  TITLE     Structural Insights into KCTD Protein Assembly and Cullin3
            Recognition
  JOURNAL   J Mol Biol 428 (1), 92-107 (2016)
   PUBMED   26334369
  REMARK    GeneRIF: The authors find that the KCTD proteins 5, 6, 9 and 17
            bind to Cul3 with high affinity, while the KCTD proteins 1 and 16
            do not have detectable binding.
REFERENCE   7  (residues 1 to 389)
  AUTHORS   Chen,T., Zhu,L., Zhou,Y., Pi,B., Liu,X., Deng,G., Zhang,R.,
            Wang,Y., Wu,Z., Han,M., Luo,X. and Ning,Q.
  TITLE     KCTD9 contributes to liver injury through NK cell activation during
            hepatitis B virus-induced acute-on-chronic liver failure
  JOURNAL   Clin Immunol 146 (3), 207-216 (2013)
   PUBMED   23376586
  REMARK    GeneRIF: These results suggest the involvement of KCTD9 in NK cell
            activation and provide additional insight into a potential
            therapeutic target for molecular manipulation for hepatitis B
            virus-induced acute-on-chronic liver failure patients
REFERENCE   8  (residues 1 to 389)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 389)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   10 (residues 1 to 389)
  AUTHORS   Zhou,Y.Y., Pi,B., Liu,X.J., Zhang,R., Deng,G.H., Chen,T.,
            Wang,H.W., Han,M.F., Yan,W.M., Xi,D., Huang,J.Q., Wang,Y.M.,
            Luo,X.P. and Ning,Q.
  TITLE     [Increased expression of KCTD9, a novel potassium channel related
            gene, correlates with disease severity in patients with viral
            hepatitis B]
  JOURNAL   Zhonghua Gan Zang Bing Za Zhi 16 (11), 835-839 (2008)
   PUBMED   19032868
  REMARK    GeneRIF: The increased expression of potassium channel gene KCTD9
            correlates with disease severity in patients with viral hepatitis
            B.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA115324.1, BC021216.2, AC103779.5 and BQ022851.1.
            
            On or before Feb 2, 2004 this sequence version replaced
            XP_005042.8, NP_060104.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.249513.1,
                                           SRR1660803.26606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149876 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221200.9/ ENSP00000221200.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..389
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..389
                     /product="BTB/POZ domain-containing protein KCTD9"
                     /note="potassium channel tetramerisation domain containing
                     9"
                     /calculated_mol_wt=42436
     Region          2..66
                     /region_name="KHA"
                     /note="dimerization domain of potassium ion channel,
                     similar to doublecortin-like domain, found in potassium
                     channel tetramerization domain containing 9 (KCTD9) and
                     similar proteins; cd17073"
                     /db_xref="CDD:340593"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L273.1)"
     Region          89..188
                     /region_name="BTB_POZ_KCTD9"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in potassium
                     channel tetramerization domain-containing protein 9
                     (KCTD9); cd18368"
                     /db_xref="CDD:349677"
     Site            order(90,96..103,106,137,139..141,143..144,146,150,
                     153..154,156,158..160,162..164,167,170)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349677"
     Region          222..377
                     /region_name="YjbI"
                     /note="Uncharacterized conserved protein YjbI, contains
                     pentapeptide repeats [Function unknown]; COG1357"
                     /db_xref="CDD:440968"
     CDS             1..389
                     /gene="KCTD9"
                     /gene_synonym="BTBD27"
                     /coded_by="NM_017634.4:188..1357"
                     /db_xref="CCDS:CCDS6048.1"
                     /db_xref="GeneID:54793"
                     /db_xref="HGNC:HGNC:22401"
                     /db_xref="MIM:617265"
ORIGIN      
        1 mrrvtlflng spkngkvvav ygtlsdllsv assklgikat svyngkggli ddialirddd
       61 vlfvcegepf idpqtdskpp egllgfhtdw ltlnvggryf tttrstlvnk epdsmlahmf
      121 kdkgvwgnkq dhrgaflidr speyfepiln ylrhgqlivn dginllgvle earffgidsl
      181 iehlevaikn sqppedhspi srkefvrfll atptkselrc qglnfsgadl srldlryinf
      241 kmanlsrcnl ahanlccanl eradlsgsvl dcanlqgvkm lcsnaegasl klcnfedpsg
      301 lkanleganl kgvdmegsqm tginlrvatl knaklkncnl rgatlagtdl encdlsgcdl
      361 qeanlrgsnv kgaifeemlt plhmsqsvr
//
LOCUS       NP_001310864             446 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptosomal-associated protein 47 isoform c [Homo sapiens].
ACCESSION   NP_001310864
VERSION     NP_001310864.1
DBSOURCE    REFSEQ: accession NM_001323935.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Jian,F., Wang,S., Tian,R., Wang,Y., Li,C., Li,Y., Wang,S., Fang,C.,
            Ma,C. and Rong,Y.
  TITLE     The STX17-SNAP47-VAMP7/VAMP8 complex is the default SNARE complex
            mediating autophagosome-lysosome fusion
  JOURNAL   Cell Res 34 (2), 151-168 (2024)
   PUBMED   38182888
  REMARK    GeneRIF: The STX17-SNAP47-VAMP7/VAMP8 complex is the default SNARE
            complex mediating autophagosome-lysosome fusion.
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wang,Y., Wang,H., Zhang,L., Zhang,J., Liu,N. and Zhao,P.
  TITLE     A novel identified circular RNA, circSnap47, promotes heart failure
            progression via regulation of miR-223-3p/MAPK axis
  JOURNAL   Mol Cell Biochem 478 (3), 459-469 (2023)
   PUBMED   35900666
  REMARK    GeneRIF: A novel identified circular RNA, circSnap47, promotes
            heart failure progression via regulation of miR-223-3p/MAPK axis.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Xiang,P., Mohamud,Y. and Luo,H.
  TITLE     SNAP47 Interacts with ATG14 to Promote VP1 Conjugation and CVB3
            Propagation
  JOURNAL   Cells 10 (8), 2141 (2021)
   PUBMED   34440910
  REMARK    GeneRIF: SNAP47 Interacts with ATG14 to Promote VP1 Conjugation and
            CVB3 Propagation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Sun,W., Guo,C., Meng,X., Yu,Y., Jin,Y., Tong,D., Geng,J., Huang,Q.,
            Qi,J., Liu,A., Guan,R., Xu,L., Sun,D., Ji,W., Liu,P., Liu,F.,
            Sun,H., Ji,G., Fu,S. and Bai,J.
  TITLE     Differential expression of PAI-RBP1, C1orf142, and COTL1 in
            non-small cell lung cancer cell lines with different tumor
            metastatic potential
  JOURNAL   J Investig Med 60 (4), 689-694 (2012)
   PUBMED   22373659
  REMARK    GeneRIF: Three proteins are identified: PAI-RBP1, C1orf142, and
            COTL1, which are differentially expressed in non-small cell lung
            cancer cell lines with different metastatic potential.
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Pfefferle,S., Schopf,J., Kogl,M., Friedel,C.C., Muller,M.A.,
            Carbajo-Lozoya,J., Stellberger,T., von Dall'Armi,E., Herzog,P.,
            Kallies,S., Niemeyer,D., Ditt,V., Kuri,T., Zust,R., Pumpor,K.,
            Hilgenfeld,R., Schwarz,F., Zimmer,R., Steffen,I., Weber,F.,
            Thiel,V., Herrler,G., Thiel,H.J., Schwegmann-Wessels,C.,
            Pohlmann,S., Haas,J., Drosten,C. and von Brunn,A.
  TITLE     The SARS-coronavirus-host interactome: identification of
            cyclophilins as target for pan-coronavirus inhibitors
  JOURNAL   PLoS Pathog 7 (10), e1002331 (2011)
   PUBMED   22046132
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Ghiani,C.A., Starcevic,M., Rodriguez-Fernandez,I.A., Nazarian,R.,
            Cheli,V.T., Chan,L.N., Malvar,J.S., de Vellis,J., Sabatti,C. and
            Dell'Angelica,E.C.
  TITLE     The dysbindin-containing complex (BLOC-1) in brain: developmental
            regulation, interaction with SNARE proteins and role in neurite
            outgrowth
  JOURNAL   Mol Psychiatry 15 (2), 115 (2010)
   PUBMED   19546860
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Holt,M., Varoqueaux,F., Wiederhold,K., Takamori,S., Urlaub,H.,
            Fasshauer,D. and Jahn,R.
  TITLE     Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous
            expression
  JOURNAL   J Biol Chem 281 (25), 17076-17083 (2006)
   PUBMED   16621800
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136378.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK054633.1, SRR9304718.241457.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..446
                     /product="synaptosomal-associated protein 47 isoform c"
                     /note="synaptosomal-associated protein 47; epididymis
                     luminal protein 170; synaptosomal-associated 47 kDa
                     protein; epididymis secretory protein Li 290; synaptosome
                     associated protein 47kDa; synaptosomal-associated protein,
                     47kDa"
                     /calculated_mol_wt=50295
     Region          20..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5SQN1.3)"
     Region          51..144
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          151..215
                     /region_name="SNARE_SNAP47N"
                     /note="N-terminal SNARE motif of SNAP47; cd15888"
                     /db_xref="CDD:277241"
     Site            order(153,156..161,163..168,170..171,174..175,177..182,
                     184..185,187..189,191..196,198..199,201..203,205..206,
                     208..210,212..213,215)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277241"
     Site            188
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277241"
     CDS             1..446
                     /gene="SNAP47"
                     /gene_synonym="C1orf142; ESFI5812; HEL-S-290; HEL170;
                     SNAP-47; SVAP1"
                     /coded_by="NM_001323935.1:415..1755"
                     /note="isoform c is encoded by transcript variant 7"
                     /db_xref="GeneID:116841"
                     /db_xref="HGNC:HGNC:30669"
                     /db_xref="MIM:619659"
ORIGIN      
        1 mraarrglhc agaerprrrg rlwdssgvpq rqkrpgpwrt qtqeqmsrdv cihtwpctyy
       61 lepkrrwvtg qlsltslslr fmtdstgeil vsfplssive ikkeashfif ssitilekgh
      121 akhwfsslrp srnvvfsiie hfwrelllsq pgavadasvp rtrgeeltgl magsqkrled
      181 tarvlhhqgq qldsvmrgld kmesdlevad rlltelespa wwpfssklwk tppetkpred
      241 vsmtscepfg kegilikipa vishrteshv kpgrltvlvs gleihdsssl lmhrferedv
      301 ddikvhspye isirqrfigk pdmayrlisa kmpevipile vqfskkmell edalvlrsar
      361 tsspaekscs vwhaasglmg rtlhreppag dqegtalhlq tslpalsead tqeltqgfrp
      421 mslstqtvlv mlcsesagal wrqrls
//
LOCUS       NP_060647               1770 aa            linear   PRI 20-NOV-2025
DEFINITION  NEDD4-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_060647
VERSION     NP_060647.2
DBSOURCE    REFSEQ: accession NM_018177.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1770)
  AUTHORS   Nicholson-Shaw,T., Dowdle,M.E., Ajaj,Y., Perelis,M., Fulzele,A.,
            Yeo,G.W., Bennett,E.J. and Lykke-Andersen,J.
  TITLE     Human CCR4 deadenylase homolog Angel1 is a non-stop mRNA decay
            factor
  JOURNAL   RNA 31 (8), 1195-1205 (2025)
   PUBMED   40441874
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1770)
  AUTHORS   Leslie,E.J., Carlson,J.C., Shaffer,J.R., Buxo,C.J., Castilla,E.E.,
            Christensen,K., Deleyiannis,F.W.B., Field,L.L., Hecht,J.T.,
            Moreno,L., Orioli,I.M., Padilla,C., Vieira,A.R., Wehby,G.L.,
            Feingold,E., Weinberg,S.M., Murray,J.C. and Marazita,M.L.
  TITLE     Association studies of low-frequency coding variants in
            nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Am J Med Genet A 173 (6), 1531-1538 (2017)
   PUBMED   28425186
  REMARK    GeneRIF: We found that a burden of low-frequency coding variants in
            N4BP2, CDSN, PRTG, and AHRR were associated with increased risk of
            Nonsyndromic cleft lip with or without cleft palate (NSCL/P) .
            Low-frequency variants in other genes were associated with
            decreased risk of NSCL/P. These results demonstrate that
            low-frequency variants contribute to the genetic etiology of NSCL/P
REFERENCE   3  (residues 1 to 1770)
  AUTHORS   Jeong,E.Y., Kim,T.G. and Ban,C.
  TITLE     Modulated nicking endonuclease function by the N-terminal extended
            region of the smr domain in human Bcl-3 binding protein
  JOURNAL   Proteins 80 (1), 327-332 (2012)
   PUBMED   22072629
  REMARK    GeneRIF: the N-terminal extended region of the Smr domain in the
            native B3bp may function as a regulatory region for the nicking
            endonuclease
REFERENCE   4  (residues 1 to 1770)
  AUTHORS   Diercks,T., AB,E., Daniels,M.A., de Jong,R.N., Besseling,R.,
            Kaptein,R. and Folkers,G.E.
  TITLE     Solution structure and characterization of the DNA-binding activity
            of the B3BP-Smr domain
  JOURNAL   J Mol Biol 383 (5), 1156-1170 (2008)
   PUBMED   18804481
  REMARK    GeneRIF: The solution structure of the functionally active Smr
            domain of the Bcl3-binding protein (also known as Nedd4-binding
            protein 2), a protein with unknown function that lacks other
            domains present in MutS proteins, is determined.
REFERENCE   5  (residues 1 to 1770)
  AUTHORS   Oshikawa,M., Sugai,Y., Usami,R., Ohtoko,K., Toyama,S. and Kato,S.
  TITLE     Fine expression profiling of full-length transcripts using a
            size-unbiased cDNA library prepared with the vector-capping method
  JOURNAL   DNA Res 15 (3), 123-136 (2008)
   PUBMED   18487259
REFERENCE   6  (residues 1 to 1770)
  AUTHORS   Zheng,M.Z., Qin,H.D., Yu,X.J., Zhang,R.H., Chen,L.Z., Feng,Q.S. and
            Zeng,Y.X.
  TITLE     Haplotype of gene Nedd4 binding protein 2 associated with sporadic
            nasopharyngeal carcinoma in the Southern Chinese population
  JOURNAL   J Transl Med 5, 36 (2007)
   PUBMED   17626640
  REMARK    GeneRIF: These data suggest that haplotype blocks ATTA and GTTG of
            N4BP2 is correlation with the risk of sporadic nasopharyngeal
            carcinoma in the Southern Chinese population.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1770)
  AUTHORS   Watanabe,N., Wachi,S. and Fujita,T.
  TITLE     Identification and characterization of BCL-3-binding protein:
            implications for transcription and DNA repair or recombination
  JOURNAL   J Biol Chem 278 (28), 26102-26110 (2003)
   PUBMED   12730195
  REMARK    GeneRIF: B3BP is a 5'-polynucleotide kinase
REFERENCE   8  (residues 1 to 1770)
  AUTHORS   Murillas,R., Simms,K.S., Hatakeyama,S., Weissman,A.M. and
            Kuehn,M.R.
  TITLE     Identification of developmentally expressed proteins that
            functionally interact with Nedd4 ubiquitin ligase
  JOURNAL   J Biol Chem 277 (4), 2897-2907 (2002)
   PUBMED   11717310
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC098591.4, AK001542.1,
            BC126466.1, AC095057.3, AB371584.1 and AW135590.1.
            
            On Jun 13, 2003 this sequence version replaced NP_060647.1.
            
            Summary: This gene encodes a protein containing a polynucleotide
            kinase domain (PNK) near the N-terminal region, and a Small MutS
            Related (Smr) domain near the C-terminal region. The encoded
            protein can bind to both B-cell leukemia/lymphoma 3 (BCL-3) and
            neural precursor cell expressed, developmentally downregulated 4,
            (Nedd4) proteins. This protein binds and hydrolyzes ATP, may
            function as a 5'-polynucleotide kinase, and has the capacity to be
            a ubiquitylation substrate. This protein may play a role in
            transcription-coupled DNA repair or genetic recombination.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY267013.1, BC126466.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261435.11/ ENSP00000261435.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14"
     Protein         1..1770
                     /product="NEDD4-binding protein 2 isoform 1"
                     /note="BCL-3-binding protein"
                     /calculated_mol_wt=198671
     Region          1..40
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          47..87
                     /region_name="CUE_N4BP2"
                     /note="CUE domain found in NEDD4-binding protein 2 (N4BP2)
                     and similar proteins; cd14365"
                     /db_xref="CDD:270548"
     Region          95..129
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          449..580
                     /region_name="AAA_33"
                     /note="AAA domain; pfam13671"
                     /db_xref="CDD:463952"
     Region          712..756
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          795..822
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          836..862
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          890..913
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Site            906
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UW6.2)"
     Site            1210
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          1580..1606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UW6.2)"
     Region          1621..1682
                     /region_name="DUF1771"
                     /note="Domain of unknown function (DUF1771); pfam08590"
                     /db_xref="CDD:462528"
     Region          1688..1770
                     /region_name="SMR"
                     /note="Small MutS-related domain; smart00463"
                     /db_xref="CDD:214676"
     CDS             1..1770
                     /gene="N4BP2"
                     /gene_synonym="B3BP"
                     /coded_by="NM_018177.6:393..5705"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3457.1"
                     /db_xref="GeneID:55728"
                     /db_xref="HGNC:HGNC:29851"
                     /db_xref="MIM:619139"
ORIGIN      
        1 mprrrknlgg npfrktanpk evvvssvasr eeptttlpsm getkvdqeel ftsiseifsd
       61 ldpdvvylml secdfkvena mdcllelsat dtkieesssq sfvasenqvg aaeskimekr
      121 peeesedskm dsfldmqlte dldsliqnaf eklnsspddq vysflpsqdv nsfndssefi
      181 npdssnmtpi fstqnmnlng enlensgstl slnplpshsv lneskcfikd ntlalesnyp
      241 edsllsssln vasdsiagcs slnqkqkell esecveaqfs eapvdldase pqaclnlpgl
      301 dlpgtggdqk strvsdvflp segfnfkphk hpelptkgkd vsycpvlapl plllpppppp
      361 pmwnpmipaf dlfqgnhgfv apvvttaahw rsvnytfpps vishtsptkv wrnkdgtsay
      421 qvqetpvsqv vrkktsyvgl vlvllrglpg sgksflartl qednpsgvil stddyfying
      481 qyqfdvkylg eahewnqnra keafekkisp iiidntnlqa wemkpyvals qkhkykvlfr
      541 epdtwwkfkp kelarrnihg vskekitrml ehyqrfvsvp iimsssvpek ierielcays
      601 cedrstsprd dediisekee nilslslkhl efteeknldv tketmlpenv aylsnadlnk
      661 rrkeisdmnp siqsalilet phmyfsdses klqatdksen eqiemvavkg ysktdtdssm
      721 ervspstccs ennqedcdla nsgplqneks spgeiveera tvtkkafgkq kskstlekfp
      781 rhelsnfvgd wpvdktigqr tkrnrktekt ssvqsdkkyn ypqshklvns vsvntdcvqq
      841 rgsphesved grksqcddas eplnsykyda yknidknsfn imgdwpssds laqrehrsrm
      901 pktglsepnl eigtndkmne islstaheac wgtssqklkt lgssnlgsse mllsemtces
      961 qtclskkshg qhtslpltft nsaptvsgvv epqtlaecqe qmpkrdpgke vgmctqtepq
     1021 dfallwkiek nkisisdsik vltgrldgfk pkvfnintks dvqeaipyrv mydkstfvee
     1081 seltsadese nlnilcklfg sfslealkdl yercnkdiiw atsllldset klcedtefen
     1141 fqkscdgsqi gpfslglnlk eiisqrgtle nsnspvpefs hgigisnads qstcdaergn
     1201 seqaemravt penhesmtsi fpsaavglkn nndilpnsqe ellysskqsf pgilkattpk
     1261 dmseteknlv vtetgdnihs pshfsdifnf vsstsnleln eeiyftdsle ikrnenfpkd
     1321 yvkfsdeeef mnedekemke ilmagsslsa gvsgedktei lnptpamaks ltidclelal
     1381 ppelafqlne lfgpvgidsg sltvedcvvh idlnlakvih ekwkesvmer qrqeevscgk
     1441 fmqdpslvgh tgldnpeqks sqrtgkkllk tltasemlpl ldhwntqtkk vslreimsee
     1501 ialqekhnlk retlmfekdc atklkekqlf kifpainqnf lvdifkdhny slehtvqfln
     1561 cvlegdpvkt vvaqefvhqn envtshtgqk skekkpkklk eteetpsels fqdfeypdyd
     1621 dyraeaflhq qkrmecyska keayrigkkn vatfyaqqgt lheqkmkean hlaaieifek
     1681 vnasllpqnv ldlhglhvde alehlmrvle kkteefkqng gkpylsvitg rgnhsqggva
     1741 rikpavikyl ishsfrfsei kpgclkvmlk
//
LOCUS       NP_001180573             279 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisomal biogenesis factor 19 isoform c [Homo sapiens].
ACCESSION   NP_001180573
VERSION     NP_001180573.1
DBSOURCE    REFSEQ: accession NM_001193644.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Liu,T., Liang,L., Zhao,P., Lin,W., Zhuang,Y., Jiang,L., Chen,H. and
            Li,C.
  TITLE     The M2 Protein of the Influenza A Virus Interacts with PEX19 to
            Facilitate Virus Replication by Disrupting the Function of
            Peroxisome
  JOURNAL   Viruses 16 (8), 1309 (2024)
   PUBMED   39205283
  REMARK    GeneRIF: The M2 Protein of the Influenza A Virus Interacts with
            PEX19 to Facilitate Virus Replication by Disrupting the Function of
            Peroxisome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Mayerhofer,P.U., Kattenfeld,T., Roscher,A.A. and Muntau,A.C.
  TITLE     Two splice variants of human PEX19 exhibit distinct functions in
            peroxisomal assembly
  JOURNAL   Biochem Biophys Res Commun 291 (5), 1180-1186 (2002)
   PUBMED   11883941
  REMARK    GeneRIF: a considerable functional diversity of the proteins
            encoded by two PEX19 splice variants and thereby provide first
            experimental evidence for specific biological functions of the
            different predicted domains of the PEX19 protein.
            GeneRIF: ALDRP interacts with PEX19 splice variants PEX19-delta-E2
            and PEX19-delta-E8.
            GeneRIF: MP70 interacts with PEX19 splice variants PEX19-delta-E2
            and PEX19p-delta-E8.
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Matsuzono,Y., Kinoshita,N., Tamura,S., Shimozawa,N., Hamasaki,M.,
            Ghaedi,K., Wanders,R.J., Suzuki,Y., Kondo,N. and Fujiki,Y.
  TITLE     Human PEX19: cDNA cloning by functional complementation, mutation
            analysis in a patient with Zellweger syndrome, and potential role
            in peroxisomal membrane assembly
  JOURNAL   Proc Natl Acad Sci U S A 96 (5), 2116-2121 (1999)
   PUBMED   10051604
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Gotte,K., Girzalsky,W., Linkert,M., Baumgart,E., Kammerer,S.,
            Kunau,W.H. and Erdmann,R.
  TITLE     Pex19p, a farnesylated protein essential for peroxisome biogenesis
  JOURNAL   Mol Cell Biol 18 (1), 616-628 (1998)
   PUBMED   9418908
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Kammerer,S., Arnold,N., Gutensohn,W., Mewes,H.W., Kunau,W.H.,
            Hofler,G., Roscher,A.A. and Braun,A.
  TITLE     Genomic organization and molecular characterization of a gene
            encoding HsPXF, a human peroxisomal farnesylated protein
  JOURNAL   Genomics 45 (1), 200-210 (1997)
   PUBMED   9339377
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Braun,A., Kammerer,S., Weissenhorn,W., Weiss,E.H. and Cleve,H.
  TITLE     Sequence of a putative human housekeeping gene (HK33) localized on
            chromosome 1
  JOURNAL   Gene 146 (2), 291-295 (1994)
   PUBMED   8076834
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Steinberg,S.J., Raymond,G.V., Braverman,N.E. and Moser,A.B.
  TITLE     Zellweger Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400252.1, CD557913.1,
            AL513282.10, AB062286.1 and BC064979.1.
            
            Summary: This gene is necessary for early peroxisomal biogenesis.
            It acts both as a cytosolic chaperone and as an import receptor for
            peroxisomal membrane proteins (PMPs). Peroxins (PEXs) are proteins
            that are essential for the assembly of functional peroxisomes. The
            peroxisome biogenesis disorders (PBDs) are a group of genetically
            heterogeneous autosomal recessive, lethal diseases characterized by
            multiple defects in peroxisome function. These disorders have at
            least 14 complementation groups, with more than one phenotype being
            observed for some complementation groups. Although the clinical
            features of PBD patients vary, cells from all PBD patients exhibit
            a defect in the import of one or more classes of peroxisomal matrix
            proteins into the organelle. Defects in this gene are a cause of
            Zellweger syndrome (ZWS), as well as peroxisome biogenesis disorder
            complementation group 14 (PBD-CG14), which is also known as
            PBD-CGJ. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (4, also known as PxFpdelta8 or
            PEX19pdeltaE8) uses an alternate splice site that results in a
            frameshift in the 3' coding region, compared to variant 1. The
            encoded isoform (c) has a distinct and shorter C-terminus, compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD557913.1, SRR3476690.288324.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..279
                     /product="peroxisomal biogenesis factor 19 isoform c"
                     /note="peroxisomal farnesylated protein; housekeeping
                     gene, 33kD; peroxin-19; 33 kDa housekeeping protein"
                     /calculated_mol_wt=30661
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P40855.1)"
     Region          2..91
                     /region_name="Necessary for PEX19 function on peroxisome
                     biogenesis"
                     /note="propagated from UniProtKB/Swiss-Prot (P40855.1)"
     Region          2..56
                     /region_name="Docking to the peroxisome membrane and
                     binding to PEX3"
                     /note="propagated from UniProtKB/Swiss-Prot (P40855.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P40855.1)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P40855.1)"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P40855.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9QYU1; propagated from
                     UniProtKB/Swiss-Prot (P40855.1)"
     Region          74..278
                     /region_name="Pex19"
                     /note="Pex19 protein family; pfam04614"
                     /db_xref="CDD:461367"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8VCI5; propagated from
                     UniProtKB/Swiss-Prot (P40855.1)"
     CDS             1..279
                     /gene="PEX19"
                     /gene_synonym="D1S2223E; HK33; PBD12A; PMP1; PMPI; PXF;
                     PXMP1"
                     /coded_by="NM_001193644.1:28..867"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="GeneID:5824"
                     /db_xref="HGNC:HGNC:9713"
                     /db_xref="MIM:600279"
ORIGIN      
        1 maaaeegcsv gaeadrelee llesalddfd kakpspapps tttapdasgp qkrspgdtak
       61 dalfasqekf fqelfdsela sqataefeka mkelaeeeph lveqfqklse aagrvgsdmt
      121 sqqeftsclk etlsglakna tdlqnssmse eeltkamegl gmdegdgegn ilpimqsimq
      181 nllskdvlyp slkeitekyp ewlqshresl ppeqfekyqe qhsvmckice qfeaetptds
      241 ettqkarfem vldlmqqlqd lghppkelag emvpvvnsv
//
LOCUS       NP_001340920             571 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001340920
VERSION     NP_001340920.1
DBSOURCE    REFSEQ: accession NM_001353991.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (5), as well as variants 6-10,
            encodes isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295738.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..571
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 5"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=65207
     Region          13..112
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          129..455
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     CDS             1..571
                     /gene="MTMR1"
                     /coded_by="NM_001353991.1:269..1984"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 meeaplfpge sikaivkdvm yicpfmgavs gtltvtdfkl yfknverdph fildvplgvi
       61 srvekigaqs hgdnscgiei vckdmrnlrl aykqeeqskl gifenlnkha fplsngqalf
      121 afsykekfpi ngwkvydpvs eykrqglpne swkiskinsn yefcdtypai ivvptsvkdd
      181 dlskvaafra kgrvpvlswi hpesqatitr csqplvgpnd krckedekyl qtimdanaqs
      241 hkliifdarq nsvadtnktk gggyesesay pnaelvflei hnihvmresl rklkeivyps
      301 idearwlsnv dgthwleyir mllagavria dkiesgktsv vvhcsdgwdr taqltslaml
      361 mldsyyrtik gfetlvekew isfghrfalr vghgndnhad adrspiflqf vdcvwqmtrq
      421 fpsafefnel flitildhly sclfgtflcn ceqqrfkedv ytktislwsy insqldefsn
      481 pffvnyenhv lypvaslshl elwvnyyvrw nprmrpqmpi hqnlkellav raelqkrveg
      541 lqrevatrav ssssergssp shsatsvhts v
//
LOCUS       NP_055559                795 aa            linear   PRI 20-NOV-2025
DEFINITION  TBC1 domain family member 5 isoform b [Homo sapiens].
ACCESSION   NP_055559 XP_376211
VERSION     NP_055559.1
DBSOURCE    REFSEQ: accession NM_014744.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 795)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 795)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   3  (residues 1 to 795)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   4  (residues 1 to 795)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 795)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 795)
  AUTHORS   Seaman,M.N., Harbour,M.E., Tattersall,D., Read,E. and Bright,N.
  TITLE     Membrane recruitment of the cargo-selective retromer subcomplex is
            catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
            TBC1D5
  JOURNAL   J Cell Sci 122 (Pt 14), 2371-2382 (2009)
   PUBMED   19531583
  REMARK    GeneRIF: Membrane recruitment of the cargo-selective retromer
            subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and
            inhibited by the Rab-GAP TBC1D5.
REFERENCE   7  (residues 1 to 795)
  AUTHORS   Ishibashi,K., Kanno,E., Itoh,T. and Fukuda,M.
  TITLE     Identification and characterization of a novel Tre-2/Bub2/Cdc16
            (TBC) protein that possesses Rab3A-GAP activity
  JOURNAL   Genes Cells 14 (1), 41-52 (2009)
   PUBMED   19077034
REFERENCE   8  (residues 1 to 795)
  AUTHORS   Yoshimura,S., Egerer,J., Fuchs,E., Haas,A.K. and Barr,F.A.
  TITLE     Functional dissection of Rab GTPases involved in primary cilium
            formation
  JOURNAL   J Cell Biol 178 (3), 363-369 (2007)
   PUBMED   17646400
REFERENCE   9  (residues 1 to 795)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 795)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            D86965.1, AC104451.2, AC090644.2 and BM976960.1.
            
            On Mar 8, 2004 this sequence version replaced XP_376211.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            lacks an alternate in-frame exon compared to variant 1. The
            resulting isoform (b) has the same N- and C-termini but is shorter
            compared to isoform a. Variants 2, 6, 7, 8, 9, and 10 all encode
            the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D86965.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..795
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..795
                     /product="TBC1 domain family member 5 isoform b"
                     /calculated_mol_wt=88874
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          56..64
                     /region_name="Required for interaction with retromer,
                     involved in interaction with ATG8 family proteins.
                     /evidence=ECO:0000269|PubMed:22354992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          57..62
                     /region_name="LIR 1.
                     /evidence=ECO:0000305|PubMed:22354992,
                     ECO:0000305|PubMed:23908376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          79..381
                     /region_name="TBC"
                     /note="Domain in Tre-2, BUB2p, and Cdc16p. Probable
                     Rab-GAPs; smart00164"
                     /db_xref="CDD:214540"
     Site            169
                     /site_type="other"
                     /note="Arginine finger.
                     /evidence=ECO:0000250|UniProtKB:Q96BZ9; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            204
                     /site_type="other"
                     /note="Glutamine finger.
                     /evidence=ECO:0000250|UniProtKB:Q96BZ9; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          475..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            544
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80XQ2; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          674..795
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     Region          785..789
                     /region_name="LIR 2.
                     /evidence=ECO:0000305|PubMed:22354992,
                     ECO:0000305|PubMed:23908376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Region          786..791
                     /region_name="Required for interaction with ATG8 family
                     proteins. /evidence=ECO:0000269|PubMed:22354992"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92609.1)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q92609.1)"
     CDS             1..795
                     /gene="TBC1D5"
                     /coded_by="NM_014744.2:1666..4053"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33714.1"
                     /db_xref="GeneID:9779"
                     /db_xref="HGNC:HGNC:19166"
                     /db_xref="MIM:615740"
ORIGIN      
        1 myhslsetrh plqpeeqevg idplssysnk sggdsnkngr rtsstldseg tfnsyrkewe
       61 elfvnnnyla tirqkgingq lrssrfrsic wklflcvlpq dksqwisrie elrawysnik
      121 eihitnprkv vgqqdlminn plsqdegslw nkffqdkelr smieqdvkrt fpemqffqqe
      181 nvrkiltdvl fcyareneql lykqgmhell apivfvlhcd hqaflhases aqpseemktv
      241 lnpeylehda yavfsqlmet aepwfstfeh dgqkgketlm tpipfarpqd lgptiaivtk
      301 vnqiqdhllk khdielymhl nrleiapqiy glrwvrllfg refplqdllv vwdalfadgl
      361 slglvdyifv amllyirdal issnyqtclg llmhypfigd vhslilkalf lrdpkrnprp
      421 vtyqfhpnld yykargadlm nksrtnakga plninkvsns linfgrklis pamapgsagg
      481 pvpggnssss ssvviptrts aeapshhlqq qqqqqrlmks esmpvqlnkg lssknisssp
      541 sveslpggre ftgsppssat kkdsffsnis rsrshsktmg rkeseeelea qisflqgqln
      601 dldamckyca kvmdthlvni qdvilqenle kedqilvsla glkqikdilk gslrfnqsql
      661 eaeeneqiti adnhycssgq gqgrgqgqsv qmsgaikqas setpgctdrg nsddfilisk
      721 dddgssargs fsgqaqplrt lrstsgksqa pvcsplvfsd plmgpasass snpssspddd
      781 sskdsgftiv spldi
//
LOCUS       NP_037417                731 aa            linear   PRI 20-NOV-2025
DEFINITION  nucleolar GTP-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_037417
VERSION     NP_037417.1
DBSOURCE    REFSEQ: accession NM_013285.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 731)
  AUTHORS   Nakamura,K., Reid,B.M., Chen,A., Chen,Z., Goode,E.L., Permuth,J.B.,
            Teer,J.K., Tyrer,J., Yu,X., Kanetsky,P.A., Pharoah,P.D.,
            Gayther,S.A., Sellers,T.A., Lawrenson,K. and Karreth,F.A.
  TITLE     Functional analysis of the 1p34.3 risk locus implicates GNL2 in
            high-grade serous ovarian cancer
  JOURNAL   Am J Hum Genet 109 (1), 116-135 (2022)
   PUBMED   34965383
  REMARK    GeneRIF: Functional analysis of the 1p34.3 risk locus implicates
            GNL2 in high-grade serous ovarian cancer.
REFERENCE   2  (residues 1 to 731)
  AUTHORS   Dong,Y., Cai,Q., Fu,L., Liu,H., Ma,M. and Wu,X.
  TITLE     Study of the G Protein Nucleolar 2 Value in Liver Hepatocellular
            Carcinoma Treatment and Prognosis
  JOURNAL   Biomed Res Int 2021, 4873678 (2021)
   PUBMED   34337013
  REMARK    GeneRIF: Study of the G Protein Nucleolar 2 Value in Liver
            Hepatocellular Carcinoma Treatment and Prognosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 731)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 731)
  AUTHORS   Datta,D., Anbarasu,K., Rajabather,S., Priya,R.S., Desai,P. and
            Mahalingam,S.
  TITLE     Nucleolar GTP-binding Protein-1 (NGP-1) Promotes G1 to S Phase
            Transition by Activating Cyclin-dependent Kinase Inhibitor p21
            Cip1/Waf1
  JOURNAL   J Biol Chem 290 (35), 21536-21552 (2015)
   PUBMED   26203195
  REMARK    GeneRIF: NGP-1 promotes cell cycle progression through the
            activation of the p53/p21(Cip-1/Waf1) pathway.
REFERENCE   5  (residues 1 to 731)
  AUTHORS   Casadio,A., Longman,D., Hug,N., Delavaine,L., Vallejos Baier,R.,
            Alonso,C.R. and Caceres,J.F.
  TITLE     Identification and characterization of novel factors that act in
            the nonsense-mediated mRNA decay pathway in nematodes, flies and
            mammals
  JOURNAL   EMBO Rep 16 (1), 71-78 (2015)
   PUBMED   25452588
  REMARK    GeneRIF: GNL2 and SEC13 are required for nonsense-mediated mRNA
            decay pathway in human cells.
REFERENCE   6  (residues 1 to 731)
  AUTHORS   Cheng,C.Y., Schache,M., Ikram,M.K., Young,T.L., Guggenheim,J.A.,
            Vitart,V., MacGregor,S., Verhoeven,V.J., Barathi,V.A., Liao,J.,
            Hysi,P.G., Bailey-Wilson,J.E., St Pourcain,B., Kemp,J.P.,
            McMahon,G., Timpson,N.J., Evans,D.M., Montgomery,G.W., Mishra,A.,
            Wang,Y.X., Wang,J.J., Rochtchina,E., Polasek,O., Wright,A.F.,
            Amin,N., van Leeuwen,E.M., Wilson,J.F., Pennell,C.E., van
            Duijn,C.M., de Jong,P.T., Vingerling,J.R., Zhou,X., Chen,P., Li,R.,
            Tay,W.T., Zheng,Y., Chew,M., Burdon,K.P., Craig,J.E., Iyengar,S.K.,
            Igo,R.P. Jr., Lass,J.H. Jr., Chew,E.Y., Haller,T., Mihailov,E.,
            Metspalu,A., Wedenoja,J., Simpson,C.L., Wojciechowski,R., Hohn,R.,
            Mirshahi,A., Zeller,T., Pfeiffer,N., Lackner,K.J., Bettecken,T.,
            Meitinger,T., Oexle,K., Pirastu,M., Portas,L., Nag,A.,
            Williams,K.M., Yonova-Doing,E., Klein,R., Klein,B.E.,
            Hosseini,S.M., Paterson,A.D., Makela,K.M., Lehtimaki,T.,
            Kahonen,M., Raitakari,O., Yoshimura,N., Matsuda,F., Chen,L.J.,
            Pang,C.P., Yip,S.P., Yap,M.K., Meguro,A., Mizuki,N., Inoko,H.,
            Foster,P.J., Zhao,J.H., Vithana,E., Tai,E.S., Fan,Q., Xu,L.,
            Campbell,H., Fleck,B., Rudan,I., Aung,T., Hofman,A.,
            Uitterlinden,A.G., Bencic,G., Khor,C.C., Forward,H., Parssinen,O.,
            Mitchell,P., Rivadeneira,F., Hewitt,A.W., Williams,C., Oostra,B.A.,
            Teo,Y.Y., Hammond,C.J., Stambolian,D., Mackey,D.A., Klaver,C.C.,
            Wong,T.Y., Saw,S.M. and Baird,P.N.
  CONSRTM   Consortium for Refractive Error and Myopia; Fuchs' Genetics
            Multi-Center Study Group; Wellcome Trust Case Control Consortium 2;
            Diabetes Control and Complications Trial/Epidemiology of Diabetes
            Interventions, and Complications Research Group
  TITLE     Nine loci for ocular axial length identified through genome-wide
            association studies, including shared loci with refractive error
  JOURNAL   Am J Hum Genet 93 (2), 264-277 (2013)
   PUBMED   24144296
REFERENCE   7  (residues 1 to 731)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 731)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 731)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 731)
  AUTHORS   Racevskis,J., Dill,A., Stockert,R. and Fineberg,S.A.
  TITLE     Cloning of a novel nucleolar guanosine 5'-triphosphate binding
            protein autoantigen from a breast tumor
  JOURNAL   Cell Growth Differ 7 (2), 271-280 (1996)
   PUBMED   8822211
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB452094.1, BC009250.2 and AA766044.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.126743.1,
                                           SRR3476690.1153684.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373062.8/ ENSP00000362153.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..731
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..731
                     /product="nucleolar GTP-binding protein 2 isoform 1"
                     /note="nucleolar GTPase; guanine nucleotide binding
                     protein-like 2 (nucleolar); nucleolar G-protein gene 1;
                     nucleolar GTP-binding protein 2; novel nucleolar guanosine
                     5'-triphosphate binding protein autoantigen; autoantigen
                     NGP-1; nucleostemin-2"
                     /calculated_mol_wt=83524
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13823.1)"
     Region          43..174
                     /region_name="NGP1NT"
                     /note="NGP1NT (NUC091) domain; pfam08153"
                     /db_xref="CDD:462379"
     Region          209..365
                     /region_name="NGP_1"
                     /note="A novel nucleolar GTP-binding protein, circularly
                     permuted subfamily of the Ras GTPases; cd01858"
                     /db_xref="CDD:206751"
     Site            order(255..256,258..259,284..286,319..325,364)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206751"
     Site            255..258
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206751"
     Site            284..286
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206751"
     Site            317..324
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206751"
     Site            342..349
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206751"
     Site            345
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206751"
     Site            361..364
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206751"
     Site            363..365
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206751"
     Region          481..502
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99LH1; propagated from
                     UniProtKB/Swiss-Prot (Q13823.1)"
     Region          555..594
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     Region          630..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13823.1)"
     CDS             1..731
                     /gene="GNL2"
                     /gene_synonym="HUMAUANTIG; Ngp-1; NGP1; Nog2; Nug2"
                     /coded_by="NM_013285.3:116..2311"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS421.1"
                     /db_xref="GeneID:29889"
                     /db_xref="HGNC:HGNC:29925"
                     /db_xref="MIM:609365"
ORIGIN      
        1 mvkpkykgrs tinpskastn pdrvqgaggq nmrdratirr lnmyrqkerr nsrgkiikpl
       61 qyqstvasgt varvepnikw fgntrvikqs slqkfqeemd tvmkdpykvv mkqsklpmsl
      121 lhdrirphnl kvhildtesf ettfgpksqr krpnlfasdm qslienaems tesydqgkdr
      181 dlvtedtgvr neaqeeiykk gqskriwgel ykvidssdvv vqvldardpm gtrsphiety
      241 lkkekpwkhl ifvlnkcdlv ptwatkrwva vlsqdyptla fhasltnpfg kgafiqllrq
      301 fgklhtdkkq isvgfigypn vgkssvintl rskkvcnvap iagetkvwqy itlmrrifli
      361 dcpgvvypse dsetdivlkg vvqvekiksp edhigavler akpeyiskty kidswenaed
      421 fleklafrtg kllkggepdl qtvgkmvlnd wqrgripffv kppnaeplva pqllpsssle
      481 vvpeaaqnnp geevtetage gsesiikeet eenshcdant emqqiltrvr qnfgkinvvp
      541 qfsgddlvpv evsdleeele sfsdeeeeeq eqqrddaees ssepeeenvg ndtkavikal
      601 dekiakyqkf ldkakakkfs avriskglse kifakpeeqr ktleedvddr apskkgkkrk
      661 aqreeeqehs nkapraltsk errravrqqr pkkvgvryye thnvknrnrn kkktndsegq
      721 khkrkkfrqk q
//
LOCUS       NP_001354664             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001354664
VERSION     NP_001354664.1
DBSOURCE    REFSEQ: accession NM_001367735.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (19), as well as variants 3, 4,
            9-18, and 20, encodes isoform c.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.54351.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367735.1:418..1893"
                     /note="isoform c is encoded by transcript variant 19"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001356026             347 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001356026 XP_016871783
VERSION     NP_001356026.1
DBSOURCE    REFSEQ: accession NM_001369097.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_016871783.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.67745.1,
                                           SRR1803612.253188.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..347
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 7"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40001
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..319
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..347
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369097.1:209..1252"
                     /note="isoform 7 is encoded by transcript variant 18"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkv slmhilrayq enpriekglg hrelvvv
//
LOCUS       NP_001317408             412 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 6 isoform 7 [Homo sapiens].
ACCESSION   NP_001317408 XP_011531262
VERSION     NP_001317408.1
DBSOURCE    REFSEQ: accession NM_001330479.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Song,C.C., Liu,T., Hogstrand,C., Zhong,C.C., Zheng,H., Sun,L.H. and
            Luo,Z.
  TITLE     SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved
            in the regulation of zinc metabolism in Golgi apparatus
  JOURNAL   Cell Mol Life Sci 81 (1), 422 (2024)
   PUBMED   39367979
  REMARK    GeneRIF: SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409
            involved in the regulation of zinc metabolism in Golgi apparatus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Aktay,I., Billur,D., Tuncay,E. and Turan,B.
  TITLE     An Overexpression of SLC30A6 Gene Contributes to Cardiomyocyte
            Dysfunction via Affecting Mitochondria and Inducing Activations in
            K-Acetylation and Epigenetic Proteins
  JOURNAL   Biochem Genet 62 (4), 3198-3214 (2024)
   PUBMED   38091184
  REMARK    GeneRIF: An Overexpression of SLC30A6 Gene Contributes to
            Cardiomyocyte Dysfunction via Affecting Mitochondria and Inducing
            Activations in K-Acetylation and Epigenetic Proteins.
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Zhu,B., Huo,R., Zhi,Q., Zhan,M., Chen,X. and Hua,Z.C.
  TITLE     Increased expression of zinc transporter ZIP4, ZIP11, ZnT1, and
            ZnT6 predicts poor prognosis in pancreatic cancer
  JOURNAL   J Trace Elem Med Biol 65, 126734 (2021)
   PUBMED   33631610
  REMARK    GeneRIF: Increased expression of zinc transporter ZIP4, ZIP11,
            ZnT1, and ZnT6 predicts poor prognosis in pancreatic cancer.
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Smith,J.L., Xiong,S., Markesbery,W.R. and Lovell,M.A.
  TITLE     Altered expression of zinc transporters-4 and -6 in mild cognitive
            impairment, early and late Alzheimer's disease brain
  JOURNAL   Neuroscience 140 (3), 879-888 (2006)
   PUBMED   16580781
  REMARK    GeneRIF: Our results show that Zn transporter-4 and Zn
            transporter-6 are significantly (P<0.05) increased in
            hippocampus/parahippocampal gyrus of early Alzheimer's disease and
            Alzheimer's disease subjects.
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Huang,L., Kirschke,C.P. and Gitschier,J.
  TITLE     Functional characterization of a novel mammalian zinc transporter,
            ZnT6
  JOURNAL   J Biol Chem 277 (29), 26389-26395 (2002)
   PUBMED   11997387
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121658.4 and AL121653.2.
            
            On Aug 29, 2016 this sequence version replaced XP_011531262.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function as zinc transporters. This protein can regulate
            subcellular levels of zinc in the Golgi and vesicles. Expression of
            this gene is altered in the Alzheimer's disease brain plaques.
            [provided by RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.192623.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..412
                     /product="zinc transporter 6 isoform 7"
                     /note="zinc transporter 6; solute carrier family 30 (zinc
                     transporter), member 6"
                     /calculated_mol_wt=45223
     Region          6..206
                     /region_name="Cation_efflux"
                     /note="Cation efflux family; pfam01545"
                     /db_xref="CDD:426316"
     CDS             1..412
                     /gene="SLC30A6"
                     /gene_synonym="MST103; MSTP103; ZNT6"
                     /coded_by="NM_001330479.2:471..1709"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="GeneID:55676"
                     /db_xref="HGNC:HGNC:19305"
                     /db_xref="MIM:611148"
ORIGIN      
        1 mwcsstnsia ltaytyltif dlfslmtcli sywvtlrkps pvysfgferl evlavfastv
       61 laqlgalfil kesaerfleq peihtgrllv gtfvalcfnl ftmlsirnkp fayvseaast
      121 swlqehvadl srslcgiipg lssiflprmn pfvlidlaga falcitymli einnyfavdt
      181 asaiaialmt fgtmypmsvy sgkvllqttp phvigqldkl irevstldgv levrnehfwt
      241 lgfgslagsv hvrirrdane qmvlahvtnr lytlvstltv qifkddwirp allsgpvaan
      301 vlnfsdhhvi pmpllkgtdd lnpvtstpak psspppefsf ntpgknvnpv illntqtrpy
      361 gfglnhghtp yssmlnqglg vpgigatqgl rtgftnipsr ygtnnrigqp rp
//
LOCUS       NP_001124149             379 aa            linear   PRI 20-NOV-2025
DEFINITION  elongin BC and Polycomb repressive complex 2-associated protein
            [Homo sapiens].
ACCESSION   NP_001124149
VERSION     NP_001124149.1
DBSOURCE    REFSEQ: accession NM_001130677.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 379)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 379)
  AUTHORS   Liefke,R., Karwacki-Neisius,V. and Shi,Y.
  TITLE     EPOP Interacts with Elongin BC and USP7 to Modulate the Chromatin
            Landscape
  JOURNAL   Mol Cell 64 (4), 659-672 (2016)
   PUBMED   27863226
  REMARK    Erratum:[Mol Cell. 2017 Jan 5;65(1):202. doi:
            10.1016/j.molcel.2016.12.006. PMID: 28061330]
REFERENCE   3  (residues 1 to 379)
  AUTHORS   Beringer,M., Pisano,P., Di Carlo,V., Blanco,E., Chammas,P.,
            Vizan,P., Gutierrez,A., Aranda,S., Payer,B., Wierer,M. and Di
            Croce,L.
  TITLE     EPOP Functionally Links Elongin and Polycomb in Pluripotent Stem
            Cells
  JOURNAL   Mol Cell 64 (4), 645-658 (2016)
   PUBMED   27863225
REFERENCE   4  (residues 1 to 379)
  AUTHORS   Alekseyenko,A.A., Gorchakov,A.A., Kharchenko,P.V. and Kuroda,M.I.
  TITLE     Reciprocal interactions of human C10orf12 and C17orf96 with PRC2
            revealed by BioTAP-XL cross-linking and affinity purification
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2488-2493 (2014)
   PUBMED   24550272
REFERENCE   5  (residues 1 to 379)
  AUTHORS   Zody,M.C., Garber,M., Adams,D.J., Sharpe,T., Harrow,J.,
            Lupski,J.R., Nicholson,C., Searle,S.M., Wilming,L., Young,S.K.,
            Abouelleil,A., Allen,N.R., Bi,W., Bloom,T., Borowsky,M.L.,
            Bugalter,B.E., Butler,J., Chang,J.L., Chen,C.K., Cook,A., Corum,B.,
            Cuomo,C.A., de Jong,P.J., DeCaprio,D., Dewar,K., FitzGerald,M.,
            Gilbert,J., Gibson,R., Gnerre,S., Goldstein,S., Grafham,D.V.,
            Grocock,R., Hafez,N., Hagopian,D.S., Hart,E., Norman,C.H.,
            Humphray,S., Jaffe,D.B., Jones,M., Kamal,M., Khodiyar,V.K.,
            LaButti,K., Laird,G., Lehoczky,J., Liu,X., Lokyitsang,T.,
            Loveland,J., Lui,A., Macdonald,P., Major,J.E., Matthews,L.,
            Mauceli,E., McCarroll,S.A., Mihalev,A.H., Mudge,J., Nguyen,C.,
            Nicol,R., O'Leary,S.B., Osoegawa,K., Schwartz,D.C., Shaw-Smith,C.,
            Stankiewicz,P., Steward,C., Swarbreck,D., Venkataraman,V.,
            Whittaker,C.A., Yang,X., Zimmer,A.R., Bradley,A., Hubbard,T.,
            Birren,B.W., Rogers,J., Lander,E.S. and Nusbaum,C.
  TITLE     DNA sequence of human chromosome 17 and analysis of rearrangement
            in the human lineage
  JOURNAL   Nature 440 (7087), 1045-1049 (2006)
   PUBMED   16625196
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006449.19.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR1163655.464319.1,
                                        SRR6380201.138676.21 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000621654.2/ ENSP00000484710.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..379
                     /product="elongin BC and Polycomb repressive complex
                     2-associated protein"
                     /note="proline rich 28; uncharacterized protein C17orf96;
                     proline-rich protein 28"
                     /calculated_mol_wt=39191
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          <6..328
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          39..48
                     /region_name="BC-box.
                     /evidence=ECO:0000250|UniProtKB:Q7TNS8"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Site            52
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          72..105
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          137..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          264..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     Region          <305..371
                     /region_name="EPOP"
                     /note="Elongin BC and Polycomb repressive complex
                     2-associated protein; pfam15223"
                     /db_xref="CDD:434546"
     Region          311..359
                     /region_name="Interaction with SUZ12.
                     /evidence=ECO:0000269|PubMed:29499137"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NHQ4.1)"
     CDS             1..379
                     /gene="EPOP"
                     /gene_synonym="C17orf96; PRR28"
                     /coded_by="NM_001130677.2:463..1602"
                     /db_xref="CCDS:CCDS45661.1"
                     /db_xref="GeneID:100170841"
                     /db_xref="HGNC:HGNC:34493"
                     /db_xref="MIM:617795"
ORIGIN      
        1 metlcpaprl avpasprgsp csptprkpcr gtqefsplcl ralafcalak prasslgpgp
       61 gelaarspvl rgpqaplrpg gwapdglkhl waptgrpgvp ntaagedadv aacprrgeee
      121 eggggfphfg vrscappgrc papphprest tsfasapprp apglepqrgp aasppqepss
      181 rppsppagls tepagpgtap rpflpgqpae vdgnpppaap eapaaspsta spapaapgdl
      241 rqehfdrlir rsklwcyakg faldtpslrr gperppakgp argaakkrrl pappprtaqp
      301 rrpaptlptt stfsllncfp cppalvvged gdlkpasslr lqgdskpppa hplwrwqmgg
      361 pavpeppglk fwginmdes
//
LOCUS       NP_001119800             728 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase LNX isoform a [Homo sapiens].
ACCESSION   NP_001119800
VERSION     NP_001119800.1
DBSOURCE    REFSEQ: accession NM_001126328.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 728)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 728)
  AUTHORS   Armbruester,V., Sauter,M., Roemer,K., Best,B., Hahn,S., Nty,A.,
            Schmid,A., Philipp,S., Mueller,A. and Mueller-Lantzsch,N.
  TITLE     Np9 protein of human endogenous retrovirus K interacts with ligand
            of numb protein X
  JOURNAL   J Virol 78 (19), 10310-10319 (2004)
   PUBMED   15367597
  REMARK    GeneRIF: identifed ligand of Numb protein X as an Np9-interacting
            partner; findings point to the possibility that Np9 affects
            tumorigenesis through the LNX/Numb/Notch pathway
REFERENCE   7  (residues 1 to 728)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of PDZRN3 and PDZRN4 genes in
            silico
  JOURNAL   Int J Mol Med 13 (4), 607-613 (2004)
   PUBMED   15010864
REFERENCE   8  (residues 1 to 728)
  AUTHORS   Nie,J., McGill,M.A., Dermer,M., Dho,S.E., Wolting,C.D. and
            McGlade,C.J.
  TITLE     LNX functions as a RING type E3 ubiquitin ligase that targets the
            cell fate determinant Numb for ubiquitin-dependent degradation
  JOURNAL   EMBO J 21 (1-2), 93-102 (2002)
   PUBMED   11782429
REFERENCE   9  (residues 1 to 728)
  AUTHORS   Xie,Y., Zhao,W., Wang,W., Zhao,S., Tang,R., Ying,K., Zhou,Z. and
            Mao,Y.
  TITLE     Identification of a human LNX protein containing multiple PDZ
            domains
  JOURNAL   Biochem Genet 39 (3-4), 117-126 (2001)
   PUBMED   11521506
REFERENCE   10 (residues 1 to 728)
  AUTHORS   Dho,S.E., Jacob,S., Wolting,C.D., French,M.B., Rohrschneider,L.R.
            and McGlade,C.J.
  TITLE     The mammalian numb phosphotyrosine-binding domain. Characterization
            of binding specificity and identification of a novel PDZ
            domain-containing numb binding protein, LNX
  JOURNAL   J Biol Chem 273 (15), 9179-9187 (1998)
   PUBMED   9535908
  REMARK    GeneRIF: The tyrosine phosphorylation of the LDNPAY sequence motif
            in mouse LNX could generate a binding site for the
            phosphorylation-dependent binding of other PTB domain-containing
            proteins.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB159390.1, BC022983.1,
            BC034737.1 and AC058822.6.
            
            Summary: This gene encodes a membrane-bound protein that is
            involved in signal transduction and protein interactions. The
            encoded product is an E3 ubiquitin-protein ligase, which mediates
            ubiquitination and subsequent proteasomal degradation of proteins
            containing phosphotyrosine binding (PTB) domains. This protein may
            play an important role in tumorogenesis. Alternatively spliced
            transcript variants encoding distinct isoforms have been described.
            A pseudogene, which is located on chromosome 17, has been
            identified for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a, also known as
            LNXp80).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022983.1, AK056823.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263925.8/ ENSP00000263925.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..728
                     /product="E3 ubiquitin-protein ligase LNX isoform a"
                     /EC_number="2.3.2.27"
                     /note="PDZ domain-containing ring finger protein 2;
                     multi-PDZ-domain-containing protein, E3 ubiquitin-protein
                     ligase LNX; numb-binding protein 1; ligand of numb-protein
                     X 1, E3 ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase LNX"
                     /calculated_mol_wt=80498
     Region          38..79
                     /region_name="mRING-HC-C3HC3D_LNX1"
                     /note="Modified RING finger, HC subclass (C3HC3D-type),
                     found in ligand of numb protein X 1 (LNX1); cd16779"
                     /db_xref="CDD:438435"
     Region          178..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBB1.1)"
     Region          181..184
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBB1.1)"
     Region          186..244
                     /region_name="Interaction with MAGEB18.
                     /evidence=ECO:0000269|PubMed:20864041"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBB1.1)"
     Region          270..358
                     /region_name="PDZ1_LNX1_2-like"
                     /note="PDZ domain 1 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06677"
                     /db_xref="CDD:467165"
     Site            order(285..291,304,307,337,341,344..345)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467165"
     Region          380..462
                     /region_name="PDZ2_LNX1_2-like"
                     /note="PDZ domain 2 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06678"
                     /db_xref="CDD:467166"
     Site            order(392..398,409,412,442,446,449..450)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467166"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TBB1.1)"
     Region          475..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBB1.1)"
     Region          506..591
                     /region_name="PDZ3_LNX1_2-like"
                     /note="PDZ domain 3 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06679"
                     /db_xref="CDD:467167"
     Site            order(517..523,538,541,571,575,578..579)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467167"
     Region          637..725
                     /region_name="PDZ4_LNX1_2-like"
                     /note="PDZ domain 4 of human Ligand of Numb protein X 1
                     (LNX1) and LNX2, and related domains; cd06680"
                     /db_xref="CDD:467168"
     Site            order(648..654,669,672,702,706,709..710)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467168"
     CDS             1..728
                     /gene="LNX1"
                     /gene_synonym="LNX; MPDZ; PDZRN2"
                     /coded_by="NM_001126328.3:186..2372"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47057.1"
                     /db_xref="GeneID:84708"
                     /db_xref="HGNC:HGNC:6657"
                     /db_xref="MIM:609732"
ORIGIN      
        1 mnqpesandp eplcavcgqa hsleenhfys ypeevdddli chiclqalld pldtpcghty
       61 ctlcltnflv ekdfcpmdrk plvlqhckks silvnkllnk llvtcpfreh ctqvlqrcdl
      121 ehhfqtsckg ashygltkdr krrsqdgcpd gcasltatap spevsaaati slmtdepgld
      181 npayvssaed gqpaispvds grsnrtrarp ferstirsrs fkkinralsv lrrtksgsav
      241 anhadqgren senttapevf prlyhlipdg eitsikinrv dpseslsirl vggsetplvh
      301 iiiqhiyrdg viardgrllp gdiilkvngm disnvphnya vrllrqpcqv lwltvmreqk
      361 frsrnngqap dayrprddsf hvilnksspe eqlgiklvrk vdepgvfifn vldggvayrh
      421 gqleendrvl ainghdlryg spesaahliq aserrvhlvv srqvrqrspd ifqeagwnsn
      481 gswspgpger sntpkplhpt itchekvvni qkdpgeslgm tvaggashre wdlpiyvisv
      541 epggvisrdg riktgdilln vdgveltevs rseavallkr tsssivlkal evkeyepqed
      601 csspaaldsn hnmappsdws pswvmwlelp rclynckdiv lrrntagslg fcivggyeey
      661 ngnkpffiks ivegtpaynd grircgdill avngrstsgm ihaclarllk elkgritlti
      721 vswpgtfl
//
LOCUS       NP_001191231             733 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform i precursor [Homo sapiens].
ACCESSION   NP_001191231
VERSION     NP_001191231.1
DBSOURCE    REFSEQ: accession NM_001204302.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 733)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 733)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 733)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 733)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 733)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 733)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 733)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 733)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 733)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 733)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI559391.1, X06989.1, Y00264.1
            and BM876312.1.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (9) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (i, also known
            as L-APP733) has the same N- and C-termini but is shorter compared
            to isoform a. No full-length transcript is available for this
            transcript; however, it is supported by PMID:1429732 and other
            publications.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1323547.1,
                                           SRR14038191.377326.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 20209079
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..733
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..733
                     /product="amyloid-beta precursor protein isoform i
                     precursor"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=81153
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1781
     mat_peptide     18..733
                     /product="amyloid-beta precursor protein isoform i"
                     /calculated_mol_wt=81153
     Region          24..188
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          294..341
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(297..305,320,322,324)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          347..529
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     mat_peptide     635..676
                     /product="amyloid-beta precursor protein isoform i"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /exception="alternative processing"
                     /calculated_mol_wt=4514
     mat_peptide     635..674
                     /product="amyloid-beta precursor protein isoform i"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /calculated_mol_wt=4330
     Region          656..730
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Site            order(669..670,672..673,675..681,683..688)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     CDS             1..733
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_001204302.2:151..2352"
                     /note="isoform i precursor is encoded by transcript
                     variant 9"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ptdgnaglla epqiamfcgr lnmhmnvqng kwdsdpsgtk
       61 tcidtkegil qycqevypel qitnvveanq pvtiqnwckr grkqckthph fvipyrclvg
      121 efvsdallvp dkckflhqer mdvcethlhw htvaketcse kstnlhdygm llpcgidkfr
      181 gvefvccpla eesdnvdsad aeeddsdvww ggadtdyadg sedkvvevae eeevaeveee
      241 eadddedded gdeveeeaee pyeeatertt siattttttt esveevvrev cseqaetgpc
      301 ramisrwyfd vtegkcapff yggcggnrnn fdteeycmav cgsaipttaa stpdavdkyl
      361 etpgdeneha hfqkakerle akhrermsqv mreweeaerq aknlpkadkk aviqhfqekv
      421 esleqeaane rqqlvethma rveamlndrr rlalenyita lqavpprprh vfnmlkkyvr
      481 aeqkdrqhtl khfehvrmvd pkkaaqirsq vmthlrviye rmnqslslly nvpavaeeiq
      541 devdellqke qnysddvlan miseprisyg ndalmpslte tkttvellpv ngefslddlq
      601 pwhsfgadsv pantenegsg ltnikteeis evkmdaefrh dsgyevhhqk lvffaedvgs
      661 nkgaiiglmv ggvviatviv itlvmlkkkq ytsihhgvve vdaavtpeer hlskmqqngy
      721 enptykffeq mqn
//
LOCUS       NP_060115                955 aa            linear   PRI 20-NOV-2025
DEFINITION  HAUS augmin-like complex subunit 6 isoform 1 [Homo sapiens].
ACCESSION   NP_060115 XP_940860
VERSION     NP_060115.3
DBSOURCE    REFSEQ: accession NM_017645.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Yao,Z., Chen,J., Wang,Y. and Cao,L.
  TITLE     Bioinformatics analysis and validation of HAUS6 as a key prognostic
            gene in squamous cell carcinoma of the tongue
  JOURNAL   Arch Oral Biol 164, 106000 (2024)
   PUBMED   38759391
  REMARK    GeneRIF: Bioinformatics analysis and validation of HAUS6 as a key
            prognostic gene in squamous cell carcinoma of the tongue.
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 955)
  AUTHORS   David,A.F., Roudot,P., Legant,W.R., Betzig,E., Danuser,G. and
            Gerlich,D.W.
  TITLE     Augmin accumulation on long-lived microtubules drives amplification
            and kinetochore-directed growth
  JOURNAL   J Cell Biol 218 (7), 2150-2168 (2019)
   PUBMED   31113824
  REMARK    GeneRIF: Our work shows that noncentrosomal microtubules nucleation
            is the predominant source of spindle microtubules also in human
            somatic cells. Importantly, our analysis of HAUS6-depleted cells
            shows that the Augmin complex is responsible for this activity.
REFERENCE   5  (residues 1 to 955)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 955)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
REFERENCE   7  (residues 1 to 955)
  AUTHORS   Lawo,S., Bashkurov,M., Mullin,M., Ferreria,M.G., Kittler,R.,
            Habermann,B., Tagliaferro,A., Poser,I., Hutchins,J.R., Hegemann,B.,
            Pinchev,D., Buchholz,F., Peters,J.M., Hyman,A.A., Gingras,A.C. and
            Pelletier,L.
  TITLE     HAUS, the 8-subunit human Augmin complex, regulates centrosome and
            spindle integrity
  JOURNAL   Curr Biol 19 (10), 816-826 (2009)
   PUBMED   19427217
REFERENCE   8  (residues 1 to 955)
  AUTHORS   Uehara,R., Nozawa,R.S., Tomioka,A., Petry,S., Vale,R.D., Obuse,C.
            and Goshima,G.
  TITLE     The augmin complex plays a critical role in spindle microtubule
            generation for mitotic progression and cytokinesis in human cells
  JOURNAL   Proc Natl Acad Sci U S A 106 (17), 6998-7003 (2009)
   PUBMED   19369198
REFERENCE   9  (residues 1 to 955)
  AUTHORS   Zhu,H., Coppinger,J.A., Jang,C.Y., Yates,J.R. 3rd and Fang,G.
  TITLE     FAM29A promotes microtubule amplification via recruitment of the
            NEDD1-gamma-tubulin complex to the mitotic spindle
  JOURNAL   J Cell Biol 183 (5), 835-848 (2008)
   PUBMED   19029337
  REMARK    GeneRIF: FAM29A promotes microtubule amplification via recruitment
            of the NEDD1-gamma-tubulin complex to the mitotic spindle.
REFERENCE   10 (residues 1 to 955)
  AUTHORS   Goshima,G., Mayer,M., Zhang,N., Stuurman,N. and Vale,R.D.
  TITLE     Augmin: a protein complex required for centrosome-independent
            microtubule generation within the spindle
  JOURNAL   J Cell Biol 181 (3), 421-429 (2008)
   PUBMED   18443220
  REMARK    GeneRIF: Results suggest that an important mitotic function for
            gamma-tubulin may lie within the spindle, where augmin (Dgt2-6;
            FAM29A) and gamma-tubulin function cooperatively to amplify the
            number of microtubules.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF537091.1, BC114492.1 and
            AL356000.13.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_940860.1, NP_060115.2.
            
            Summary: The protein encoded by this gene is a subunit of the
            augmin complex. The augmin complex plays a role in microtubule
            attachment to the kinetochore and central spindle formation. This
            protein may have a role in efficient chromosome congression and
            segregation by promoting microtubule-dependent microtubule
            amplification. Pseudogenes of this gene are located on chromosomes
            7 and 20. Alternative splicing results in multiple transcript
            variants that encode different protein isoforms. [provided by
            RefSeq, Aug 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF537091.1, SRR1660803.137365.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380502.8/ ENSP00000369871.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.1"
     Protein         1..955
                     /product="HAUS augmin-like complex subunit 6 isoform 1"
                     /note="dim gamma-tubulin homolog; family with sequence
                     similarity 29, member A"
                     /calculated_mol_wt=108491
     Region          14..239
                     /region_name="HAUS6_N"
                     /note="HAUS augmin-like complex subunit 6 N-terminus;
                     pfam14661"
                     /db_xref="CDD:464244"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Region          474..495
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            552
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            728
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Region          789..814
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            823
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Region          848..876
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7Z4H7.2)"
     CDS             1..955
                     /gene="HAUS6"
                     /gene_synonym="Dgt6; FAM29A"
                     /coded_by="NM_017645.5:254..3121"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6489.1"
                     /db_xref="GeneID:54801"
                     /db_xref="HGNC:HGNC:25948"
                     /db_xref="MIM:613433"
ORIGIN      
        1 mssasvtafe kehlwmylqa lgfepgpati acgkivshth lgvnmfdkln rdafhiisyf
       61 lfqvldqslt kevfkfcwpp fdqksdtefr khccewikri sgecgssfpq vvgslflspg
      121 gpkfihlmyh farfvamkyi ksnsknsshh fvetfnikpq dlhkciarch farsrflqil
      181 qrqdcvtqky qenaqlsvkq vrnlrsecig lenqikkmep yddhsnmeek iqkvrslwas
      241 vnetlmflek erevvssvls lvnqyaldgt nvainiprll ldkiekqmfq lhignvyeag
      301 klnlltviql lnevlkvmky ercqadqarl tvdlhyleke tkfqkerlsd lkhmryrikd
      361 dlttirhsvv ekqgewhkkw keflglspfs likgwtpsvd llppmsplsf dpaseevyak
      421 silcqypasl pdahkqhnqe ngcrgdsdtl galhdlansp asflsqsvss sdrnsvtvle
      481 kdtkmgtpke kneaiskkip efevenspls dvakntessa fggslpakks dpfqkeqdhl
      541 veevaravls dspqlsegke ikleelidsl gsnpfltrnq iprtpenlit eirsswrkai
      601 emeenrtkep iqmdaehrev lpeslpvlhn qrefsmadfl lettvsdfgq shlteekvis
      661 dcecvpqkhv ltshideppt qnqsdllnkk vickqdlecl aftklsetsr metfspavgn
      721 ridvmggsee efmkildhle vscnkpstnk tmlwnsfqis sgissksfkd ndfgilhetl
      781 peevghlsfn ssssseanfk lepnspmhgg tlledvvggr qttpesdfnl qalrsryeal
      841 kkslskkree sylsnsqtpe rhkpelsptp qnvqtddtln fldtcdlhte hikpslrtsi
      901 gerkrslspl ikfspveqrl rttiacslge lpnlkeedil nksldakepp sdltr
//
LOCUS       NP_620710                474 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily D member 1 isoform b [Homo sapiens].
ACCESSION   NP_620710
VERSION     NP_620710.2
DBSOURCE    REFSEQ: accession NM_139071.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Ross,C., Gong,L.Y., Jenkins,L.M., Ha,N.H., Majocha,M. and
            Hunter,K.W.
  TITLE     SMARCD1 is an essential expression-restricted metastasis modifier
  JOURNAL   Commun Biol 7 (1), 1299 (2024)
   PUBMED   39390150
  REMARK    GeneRIF: SMARCD1 is an essential expression-restricted metastasis
            modifier.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Zhao,Y., Liu,Y., Zhao,G., Lu,H., Liu,Y., Xue,C., Chang,Z., Liu,H.,
            Deng,Y., Liang,W., Wang,H., Rom,O., Garcia-Barrio,M.T., Zhu,T.,
            Guo,Y., Chang,L., Lin,J., Chen,Y.E. and Zhang,J.
  TITLE     Myeloid BAF60a deficiency alters metabolic homeostasis and
            exacerbates atherosclerosis
  JOURNAL   Cell Rep 42 (10), 113171 (2023)
   PUBMED   37768825
  REMARK    GeneRIF: Myeloid BAF60a deficiency alters metabolic homeostasis and
            exacerbates atherosclerosis.
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Chen,J., Yu,N., Ou,S., Wang,X., Li,H. and Zhu,H.
  TITLE     Integrated analysis reveals SMARCD1 is a potential biomarker and
            therapeutic target in skin cutaneous melanoma
  JOURNAL   J Cancer Res Clin Oncol 149 (13), 11619-11634 (2023)
   PUBMED   37401939
  REMARK    GeneRIF: Integrated analysis reveals SMARCD1 is a potential
            biomarker and therapeutic target in skin cutaneous melanoma.
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Ring,H.Z., Vameghi-Meyers,V., Wang,W., Crabtree,G.R. and Francke,U.
  TITLE     Five SWI/SNF-related, matrix-associated, actin-dependent regulator
            of chromatin (SMARC) genes are dispersed in the human genome
  JOURNAL   Genomics 51 (1), 140-143 (1998)
   PUBMED   9693044
REFERENCE   7  (residues 1 to 474)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   8  (residues 1 to 474)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   9  (residues 1 to 474)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   10 (residues 1 to 474)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB010252.1, CN272379.1,
            DA825057.1, N75126.1, BE905082.1, AC025154.31 and AA610093.1.
            
            On Mar 21, 2007 this sequence version replaced NP_620710.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and has sequence similarity to
            the yeast Swp73 protein. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform b), compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U66617.1, SRR18074968.2261520.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..474
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily D member
                     1 isoform b"
                     /note="mammalian chromatin remodeling complex
                     BRG1-associated factor 60A; chromatin remodeling complex
                     BAF60A subunit; Swp73-like protein; SWI/SNF complex 60 kDa
                     subunit A; SWI/SNF related, matrix associated, actin
                     dependent regulator of chromatin, subfamily d, member 1;
                     SWI/SNF-related matrix-associated actin-dependent
                     regulator of chromatin subfamily D member 1; 60 kDa
                     BRG-1/Brm-associated factor subunit A"
                     /calculated_mol_wt=53168
     Region          294..370
                     /region_name="SWIB_BAF60A"
                     /note="SWIB domain found in BRG1-associated factor 60A
                     (BAF60A) and similar proteins; cd17674"
                     /db_xref="CDD:349493"
     Site            order(313,316..317,319..320,323..324,329,334..335,337,354,
                     357..358)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349493"
     CDS             1..474
                     /gene="SMARCD1"
                     /gene_synonym="BAF60A; CRACD1; CSS11; Rsc6p"
                     /coded_by="NM_139071.3:29..1453"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8798.2"
                     /db_xref="GeneID:6602"
                     /db_xref="HGNC:HGNC:11106"
                     /db_xref="MIM:601735"
ORIGIN      
        1 maaragfqsv apsggagasg gagaaaalgp ggtpgppvrm gpapgqglyr spmpgaaypr
       61 pgmlpgsrmt pqgpsmgppg yggnpsvrpg laqsgmdqsr krpapqqiqq vqqqavqnrn
      121 hnakkkkmad kilpqrirel vpesqaymdl laferkldqt imrkrldiqe alkrpikqkr
      181 klrifisntf npaksdaedg egtvaswelr vegrlledsa lskydatkqk rkfssffksl
      241 vieldkdlyg pdnhlvewhr tattqetdgf qvkrpgdvnv rctvllmldy qppqfkldpr
      301 larllgihtq trpviiqalw qyikthklqd pherefvicd kylqqifesq rmkfseipqr
      361 lhallmppep iiinhvisvd pndqkktacy didvevddtl ktqmnsflls tasqqeiatl
      421 dnktmtdvvg npeeerraef yfqpwaqeav cryfyskvqq rrqeleqalg irnt
//
LOCUS       NP_001356027             347 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 7 [Homo
            sapiens].
ACCESSION   NP_001356027
VERSION     NP_001356027.1
DBSOURCE    REFSEQ: accession NM_001369098.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.19368.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..347
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 7"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=40001
     Region          59..124
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(68,70..72,74..78,81..82,85..86,91..94)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          133..319
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..347
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369098.1:214..1257"
                     /note="isoform 7 is encoded by transcript variant 19"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mevlrpqlir idgrnyrknp vqeqtyqhee deedfyqgsm ecadepcday eveqtpqgfr
       61 stlrapslly khivgkrgdt rkkiemetkt sisipkpgqd geivitgqhr ngvisartri
      121 dvlldtfrrk qpfthflaff lnevevqegf lrfqeevlak csmdhgvdss ifqnpkklhl
      181 tigmlvllse eeiqqtceml qqckeefind isggkpleve magieymndd pgmvdvlyak
      241 vhmkdgsnrl qelvdrvler fqasglivke wnsvklhatv mntlfrkdpn aegrynlyta
      301 egkyifkere sfdgrnilkv slmhilrayq enpriekglg hrelvvv
//
LOCUS       NP_036300                296 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 2 [Homo sapiens].
ACCESSION   NP_036300
VERSION     NP_036300.2
DBSOURCE    REFSEQ: accession NM_012168.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Guo,W., Ren,Y. and Qiu,X.
  TITLE     FBXO2 promotes the progression of papillary thyroid carcinoma
            through the p53 pathway
  JOURNAL   Sci Rep 14 (1), 22574 (2024)
   PUBMED   39343799
  REMARK    GeneRIF: FBXO2 promotes the progression of papillary thyroid
            carcinoma through the p53 pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Liu,Z., Chen,N.Y., Zhang,Z., Zhou,S. and Hu,S.Y.
  TITLE     F-box only protein 2 exacerbates non-alcoholic fatty liver disease
            by targeting the hydroxyl CoA dehydrogenase alpha subunit
  JOURNAL   World J Gastroenterol 29 (28), 4433-4450 (2023)
   PUBMED   37576703
  REMARK    GeneRIF: F-box only protein 2 exacerbates non-alcoholic fatty liver
            disease by targeting the hydroxyl CoA dehydrogenase alpha subunit.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Ji,J., Shen,J., Xu,Y., Xie,M., Qian,Q., Qiu,T., Shi,W., Ren,D.,
            Ma,J., Liu,W. and Liu,B.
  TITLE     FBXO2 targets glycosylated SUN2 for ubiquitination and degradation
            to promote ovarian cancer development
  JOURNAL   Cell Death Dis 13 (5), 442 (2022)
   PUBMED   35525855
  REMARK    GeneRIF: FBXO2 targets glycosylated SUN2 for ubiquitination and
            degradation to promote ovarian cancer development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Yamada,A., Hikichi,M., Nozawa,T. and Nakagawa,I.
  TITLE     FBXO2/SCF ubiquitin ligase complex directs xenophagy through
            recognizing bacterial surface glycan
  JOURNAL   EMBO Rep 22 (11), e52584 (2021)
   PUBMED   34515398
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Yoshida,Y., Chiba,T., Tokunaga,F., Kawasaki,H., Iwai,K., Suzuki,T.,
            Ito,Y., Matsuoka,K., Yoshida,M., Tanaka,K. and Tai,T.
  TITLE     E3 ubiquitin ligase that recognizes sugar chains
  JOURNAL   Nature 418 (6896), 438-442 (2002)
   PUBMED   12140560
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Erhardt,J.A., Hynicka,W., DiBenedetto,A., Shen,N., Stone,N.,
            Paulson,H. and Pittman,R.N.
  TITLE     A novel F box protein, NFB42, is highly enriched in neurons and
            induces growth arrest
  JOURNAL   J Biol Chem 273 (52), 35222-35227 (1998)
   PUBMED   9857061
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Thalmann,I., Rosenthal,H.L., Moore,B.W. and Thalmann,R.
  TITLE     Organ of Corti-specific polypeptides: OCP-I and OCP-II
  JOURNAL   Arch Otorhinolaryngol 226 (3), 123-128 (1980)
   PUBMED   7458746
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF187318.1, AL031731.44 and
            AW162121.1.
            
            On Oct 1, 2001 this sequence version replaced NP_036300.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. This protein is highly similar to the
            rat NFB42 (neural F Box 42 kDa) protein which is enriched in the
            nervous system and may play a role in maintaining neurons in a
            postmitotic state. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC096747.1, SRR3476690.299589.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354287.5/ ENSP00000346240.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..296
                     /product="F-box only protein 2"
                     /note="F-box gene 1; organ of Corti protein 1"
                     /calculated_mol_wt=33197
     Region          1..41
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UK22.2)"
     Region          57..119
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Site            order(57..58,61..62,66,68..69,74..76,78)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438852"
     Region          114..294
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     Site            173
                     /site_type="other"
                     /note="Important for carbohydrate binding.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (Q9UK22.2)"
     CDS             1..296
                     /gene="FBXO2"
                     /gene_synonym="FBG1; Fbs1; FBX2; NFB42; OCP1"
                     /coded_by="NM_012168.6:90..980"
                     /db_xref="CCDS:CCDS130.1"
                     /db_xref="GeneID:26232"
                     /db_xref="HGNC:HGNC:13581"
                     /db_xref="MIM:607112"
ORIGIN      
        1 mdgdgdpesv gqpeeaspee qpeeasaeee rpedqqeeea aaaaayldel peplllrvla
       61 alpaaelvqa crlvclrwke lvdgaplwll kcqqeglvpe ggveeerdhw qqfyflskrr
      121 rnllrnpcge edlegwcdve hggdgwrvee lpgdsgveft hdesvkkyfa ssfewcrkaq
      181 vidlqaegyw eelldttqpa ivvkdwysgr sdagclyelt vkllsehenv laefssgqva
      241 vpqdsdgggw meishtftdy gpgvrfvrfe hggqdsvywk gwfgarvtns svwvep
//
LOCUS       NP_001356348             273 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001356348
VERSION     NP_001356348.1
DBSOURCE    REFSEQ: accession NM_001369419.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 273)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 273)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3 and AC092309.3.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2492152.1,
                                           SRR14038197.1285588.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..273
                     /product="DNA excision repair protein ERCC-1 isoform 3"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=29862
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          235..264
                     /region_name="HHH"
                     /note="Helix-hairpin-helix motif; pfam00633"
                     /db_xref="CDD:425789"
     CDS             1..273
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369419.1:155..976"
                     /note="isoform 3 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS54279.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrsleqli
      241 aasredlalc pglgpqkarr lfdvlhepfl kvp
//
LOCUS       NP_001336187             902 aa            linear   PRI 20-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 3 isoform 4 [Homo sapiens].
ACCESSION   NP_001336187
VERSION     NP_001336187.1
DBSOURCE    REFSEQ: accession NM_001349258.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Wu,D., Zhao,L., Feng,Z., Yu,C., Ding,J., Wang,L., Wang,F., Liu,D.,
            Zhu,H., Xing,F., Conaway,J.W., Conaway,R.C., Cai,Y. and Jin,J.
  TITLE     O-Linked N-acetylglucosamine transferase 1 regulates global histone
            H4 acetylation via stabilization of the nonspecific lethal protein
            NSL3
  JOURNAL   J Biol Chem 292 (24), 10014-10025 (2017)
   PUBMED   28450392
  REMARK    GeneRIF: Data suggest that O-GlcNAc transferase 1 (OGT1)
            specifically binds to, O-GlcNAcylates, and stabilizes nonspecific
            lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates
            global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16.
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Chatterjee,A., Seyfferth,J., Lucci,J., Gilsbach,R., Preissl,S.,
            Bottinger,L., Martensson,C.U., Panhale,A., Stehle,T., Kretz,O.,
            Sahyoun,A.H., Avilov,S., Eimer,S., Hein,L., Pfanner,N., Becker,T.
            and Akhtar,A.
  TITLE     MOF Acetyl Transferase Regulates Transcription and Respiration in
            Mitochondria
  JOURNAL   Cell 167 (3), 722-738 (2016)
   PUBMED   27768893
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Meunier,S., Shvedunova,M., Van Nguyen,N., Avila,L., Vernos,I. and
            Akhtar,A.
  TITLE     An epigenetic regulator emerges as microtubule minus-end binding
            and stabilizing factor in mitosis
  JOURNAL   Nat Commun 6, 7889 (2015)
   PUBMED   26243146
  REMARK    GeneRIF: microtubule minus-end-binding protein, essential for
            spindle assembly and chromosome segregation
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Zhao,X., Su,J., Wang,F., Liu,D., Ding,J., Yang,Y., Conaway,J.W.,
            Conaway,R.C., Cao,L., Wu,D., Wu,M., Cai,Y. and Jin,J.
  TITLE     Crosstalk between NSL histone acetyltransferase and MLL/SET
            complexes: NSL complex functions in promoting histone H3K4
            di-methylation activity by MLL/SET complexes
  JOURNAL   PLoS Genet 9 (11), e1003940 (2013)
   PUBMED   24244196
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Rea,S., Xouri,G. and Akhtar,A.
  TITLE     Males absent on the first (MOF): from flies to humans
  JOURNAL   Oncogene 26 (37), 5385-5394 (2007)
   PUBMED   17694080
  REMARK    Review article
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Mendjan,S., Taipale,M., Kind,J., Holz,H., Gebhardt,P., Schelder,M.,
            Vermeulen,M., Buscaino,A., Duncan,K., Mueller,J., Wilm,M.,
            Stunnenberg,H.G., Saumweber,H. and Akhtar,A.
  TITLE     Nuclear pore components are involved in the transcriptional
            regulation of dosage compensation in Drosophila
  JOURNAL   Mol Cell 21 (6), 811-823 (2006)
   PUBMED   16543150
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079754.4.
            
            Transcript Variant: This variant (10) contains an alternate exon in
            the 3' coding region, compared to variant 1. The encoded isoform
            (4) is longer than isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2190993.1,
                                           SRR1803614.176410.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..902
                     /product="KAT8 regulatory NSL complex subunit 3 isoform 4"
                     /note="serum inhibited-related protein; testis development
                     protein PRTD; NSL complex protein NSL3; non-specific
                     lethal 3 homolog"
                     /calculated_mol_wt=95719
     Region          <323..472
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
     Region          476..563
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Site            523
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Site            536
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:A2RSY1; propagated from
                     UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Region          695..717
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Region          760..780
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P2N6.2)"
     Region          867..902
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2N6.2)"
     CDS             1..902
                     /gene="KANSL3"
                     /gene_synonym="KIAA1310; NSL3; Rcd1"
                     /coded_by="NM_001349258.2:81..2789"
                     /note="isoform 4 is encoded by transcript variant 10"
                     /db_xref="GeneID:55683"
                     /db_xref="HGNC:HGNC:25473"
                     /db_xref="MIM:617742"
ORIGIN      
        1 mahrggerdf qtsarrmgts llfqlsvher eldlvfldhs yakpwsahpd assarptrml
       61 fvtprrqhes tiesdvpidv etvtstpmpl ydnqkarsvm necerhvifa rtdadapppp
      121 edweehvnrt gwtmaqnklf nkilkalqsd rlarlanega cnepvlrrva vdkcarrvrq
      181 alasvswdtk liqwlhttlv etlslpmlaa yldalqtlkg kiptlidrml vssntktgaa
      241 gaealslllk rpwdpavgvl shnkpsklpg spliliassg psssvfptsr rhrfwqsqls
      301 clgkvipvat hllnngsgvg vlqclehmig avrskvleih shfphkpiil igwntgalva
      361 chvsvmeyvt avvclgfpll tvdgprgdvd dplldmktpv lfvigqnslq chpeamedfr
      421 ekiraenslv vvggaddnlr iskakkkseg ltqsmvdrci qdeivdfltg vltraeghmg
      481 seprdqdaek kkkprdvarr dlafevperg srpaspaakl paspsgsedl ssvsssptss
      541 pktkvttvts aqkssqigss qllkrhvqrt eavlthkqaq aqfaaflkqn mlvrkalppg
      601 tssclfvpis seppeegeke dlrvqlkrhh pssplpgskt skrpkikvsl isqgdtaggp
      661 capsqgsape ggkpitmtlg qasagakelt gllttaksss seggvsaspv psvvssstap
      721 salhtlqsrl vatspgsslp gatsassllq glsfslqdis sktsglpanp spgpapqats
      781 vklptpmqsl gaittgtsti vrtipvattl sslgatpggk ptaihqlltn gglaklassl
      841 pglaqisnqa sglkvpttit ltlrgqpsri ttlspmgsga apseesssqv lpsssqrlpp
      901 ap
//
LOCUS       NP_003816                211 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptosomal-associated protein 23 isoform SNAP23A [Homo sapiens].
ACCESSION   NP_003816
VERSION     NP_003816.2
DBSOURCE    REFSEQ: accession NM_003825.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Gigon,L., Fettrelet,T., Miholic,M., McLeish,K.R., Yousefi,S.,
            Stojkov,D. and Simon,H.U.
  TITLE     Syntaxin-4 and SNAP23 are involved in neutrophil degranulation, but
            not in the release of mitochondrial DNA during NET formation
  JOURNAL   Front Immunol 14, 1272699 (2023)
   PUBMED   37885878
  REMARK    GeneRIF: Syntaxin-4 and SNAP23 are involved in neutrophil
            degranulation, but not in the release of mitochondrial DNA during
            NET formation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Xie,B.W., Guan,B., Chen,W., Zhou,M., Gu,Q., Liu,Y. and Yan,D.
  TITLE     Tumor-derived extracellular vesicles delivering TNF-alpha promotes
            colorectal cancer metastasis via the NF-kB/LAMB3/AKT axis by
            targeting SNAP23
  JOURNAL   Arch Biochem Biophys 741, 109605 (2023)
   PUBMED   37086961
  REMARK    GeneRIF: Tumor-derived extracellular vesicles delivering TNF-alpha
            promotes colorectal cancer metastasis via the NF-kB/LAMB3/AKT axis
            by targeting SNAP23.
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Miller,K., Wagner,M.A., Jassey,A. and Jackson,W.T.
  TITLE     SNAP23 is essential for germination of EV-D68 replication
            organelles
  JOURNAL   Virology 578, 117-127 (2023)
   PUBMED   36527930
  REMARK    GeneRIF: SNAP23 is essential for germination of EV-D68 replication
            organelles.
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Mitani,F., Hayasaka,R., Hirayama,A. and Oneyama,C.
  TITLE     SNAP23-Mediated Perturbation of Cholesterol-Enriched Membrane
            Microdomain Promotes Extracellular Vesicle Production in
            Src-Activated Cancer Cells
  JOURNAL   Biol Pharm Bull 45 (10), 1572-1580 (2022)
   PUBMED   36184518
  REMARK    GeneRIF: SNAP23-Mediated Perturbation of Cholesterol-Enriched
            Membrane Microdomain Promotes Extracellular Vesicle Production in
            Src-Activated Cancer Cells.
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Galli,T., Zahraoui,A., Vaidyanathan,V.V., Raposo,G., Tian,J.M.,
            Karin,M., Niemann,H. and Louvard,D.
  TITLE     A novel tetanus neurotoxin-insensitive vesicle-associated membrane
            protein in SNARE complexes of the apical plasma membrane of
            epithelial cells
  JOURNAL   Mol Biol Cell 9 (6), 1437-1448 (1998)
   PUBMED   9614185
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Tang,B.L., Tan,A.E., Lim,L.K., Lee,S.S., Low,D.Y. and Hong,W.
  TITLE     Syntaxin 12, a member of the syntaxin family localized to the
            endosome
  JOURNAL   J Biol Chem 273 (12), 6944-6950 (1998)
   PUBMED   9507000
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Araki,S., Tamori,Y., Kawanishi,M., Shinoda,H., Masugi,J., Mori,H.,
            Niki,T., Okazawa,H., Kubota,T. and Kasuga,M.
  TITLE     Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c
  JOURNAL   Biochem Biophys Res Commun 234 (1), 257-262 (1997)
   PUBMED   9168999
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Mollinedo,F. and Lazo,P.A.
  TITLE     Identification of two isoforms of the vesicle-membrane fusion
            protein SNAP-23 in human neutrophils and HL-60 cells
  JOURNAL   Biochem Biophys Res Commun 231 (3), 808-812 (1997)
   PUBMED   9070898
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Ravichandran,V., Chawla,A. and Roche,P.A.
  TITLE     Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
            protein, SNAP-23, expressed in non-neuronal tissues
  JOURNAL   J Biol Chem 271 (23), 13300-13303 (1996)
   PUBMED   8663154
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290152.1, BC022890.1 and
            BM782600.1.
            
            On Feb 19, 2002 this sequence version replaced NP_003816.1.
            
            Summary: Specificity of vesicular transport is regulated, in part,
            by the interaction of a vesicle-associated membrane protein termed
            synaptobrevin/VAMP with a target compartment membrane protein
            termed syntaxin. These proteins, together with SNAP25
            (synaptosome-associated protein of 25 kDa), form a complex which
            serves as a binding site for the general membrane fusion machinery.
            Synaptobrevin/VAMP and syntaxin are believed to be involved in
            vesicular transport in most, if not all cells, while SNAP25 is
            present almost exclusively in the brain, suggesting that a
            ubiquitously expressed homolog of SNAP25 exists to facilitate
            transport vesicle/target membrane fusion in other tissues. The
            protein encoded by this gene is structurally and functionally
            similar to SNAP25 and binds tightly to multiple syntaxins and
            synaptobrevins/VAMPs. It is an essential component of the high
            affinity receptor for the general membrane fusion machinery and is
            an important regulator of transport vesicle docking and fusion. Two
            alternative transcript variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer transcript,
            containing eight exons and encoding the full-length isoform
            (SNAP23A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.112212.1,
                                           SRR1660809.125591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249647.8/ ENSP00000249647.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1-q15.2"
     Protein         1..211
                     /product="synaptosomal-associated protein 23 isoform
                     SNAP23A"
                     /note="synaptosomal-associated protein 23;
                     synaptosomal-associated protein, 23kDa; vesicle-membrane
                     fusion protein SNAP-23; synaptosome associated protein
                     23kDa"
                     /calculated_mol_wt=23223
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712;
                     propagated from UniProtKB/Swiss-Prot (O00161.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09044; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          86..148
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00161.1)"
     Region          149..207
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(149,151..152,155..160,162..163,166..167,169..171,
                     173..174,177..178,180..181,183..188,190..191,194,197,201,
                     204,207)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00161.1)"
     Site            180
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..211
                     /gene="SNAP23"
                     /gene_synonym="HsT17016; SNAP-23; SNAP23A; SNAP23B"
                     /coded_by="NM_003825.4:95..730"
                     /note="isoform SNAP23A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10087.1"
                     /db_xref="GeneID:8773"
                     /db_xref="HGNC:HGNC:11131"
                     /db_xref="MIM:602534"
ORIGIN      
        1 mdnlsseeiq qrahqitdes lestrrilgl aiesqdagik titmldeqke qlnrieegld
       61 qinkdmrete ktltelnkcc glcvcpcnrt knfesgkayk ttwgdggens pcnvvskqpg
      121 pvtngqlqqp ttgaasggyi kritndared emeenltqvg silgnlkdma lnigneidaq
      181 npqikritdk adtnrdridi anarakklid s
//
LOCUS       NP_057002                163 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P/MRP protein subunit POP5 isoform a [Homo sapiens].
ACCESSION   NP_057002
VERSION     NP_057002.2
DBSOURCE    REFSEQ: accession NM_015918.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Welting,T.J., Kikkert,B.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Differential association of protein subunits with the human RNase
            MRP and RNase P complexes
  JOURNAL   RNA 12 (7), 1373-1382 (2006)
   PUBMED   16723659
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Welting,T.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Mutual interactions between subunits of the human RNase MRP
            ribonucleoprotein complex
  JOURNAL   Nucleic Acids Res 32 (7), 2138-2146 (2004)
   PUBMED   15096576
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 163)
  AUTHORS   van Eenennaam,H., Lugtenberg,D., Vogelzangs,J.H., van Venrooij,W.J.
            and Pruijn,G.J.
  TITLE     hPop5, a protein subunit of the human RNase MRP and RNase P
            endoribonucleases
  JOURNAL   J Biol Chem 276 (34), 31635-31641 (2001)
   PUBMED   11413139
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 163)
  AUTHORS   van Eenennaam,H., Pruijn,G.J. and van Venrooij,W.J.
  TITLE     hPop4: a new protein subunit of the human RNase MRP and RNase P
            ribonucleoprotein complexes
  JOURNAL   Nucleic Acids Res 27 (12), 2465-2472 (1999)
   PUBMED   10352175
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC063943.23, BI668578.1 and AJ306296.1.
            
            On Apr 23, 2002 this sequence version replaced NP_057002.1.
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.45866.1,
                                           SRR5189667.341060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2151358
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357500.5/ ENSP00000350098.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..163
                     /product="ribonuclease P/MRP protein subunit POP5 isoform
                     a"
                     /EC_number="3.1.26.5"
                     /note="ribonuclease P/MRP protein subunit POP5; processing
                     of precursor 5, ribonuclease P/MRP subunit; POP5 homolog,
                     ribonuclease P/MRP subunit"
                     /calculated_mol_wt=18689
     Region          7..115
                     /region_name="RNase_P_Rpp14"
                     /note="Rpp14/Pop5 family; pfam01900"
                     /db_xref="CDD:460379"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q969H6.1)"
     CDS             1..163
                     /gene="POP5"
                     /gene_synonym="hPop5; HSPC004; RPP2; RPP20"
                     /coded_by="NM_015918.4:41..532"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9202.1"
                     /db_xref="GeneID:51367"
                     /db_xref="HGNC:HGNC:17689"
                     /db_xref="MIM:609992"
ORIGIN      
        1 mvrfkhryll celvsddprc rlslddrvls slvrdtiarv hgtfgaaacs igfavrylna
       61 ytgivllrcr kefyqlvwsa lpfitylenk ghrypcffnt lhvggtirtc qkfliqynrr
      121 qllillqnct degereaiqk svtrscllee eeesgeeaae ame
//
LOCUS       NP_002190                349 aa            linear   PRI 20-NOV-2025
DEFINITION  interferon regulatory factor 2 [Homo sapiens].
ACCESSION   NP_002190
VERSION     NP_002190.2
DBSOURCE    REFSEQ: accession NM_002199.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Tokumaru,S., Yamamoto,Y., Yoshizawa,K., Soejima,Y., Sanjo,H. and
            Taki,S.
  TITLE     Interferon regulatory factor-2 is required for the establishment of
            the gut intraepithelial T-cell compartment
  JOURNAL   Int Immunol 35 (5), 231-241 (2023)
   PUBMED   36521002
  REMARK    GeneRIF: Interferon regulatory factor-2 is required for the
            establishment of the gut intraepithelial T-cell compartment.
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Persyn,E., Wahlen,S., Kiekens,L., Van Loocke,W., Siwe,H., Van
            Ammel,E., De Vos,Z., Van Nieuwerburgh,F., Matthys,P., Taghon,T.,
            Vandekerckhove,B., Van Vlierberghe,P. and Leclercq,G.
  TITLE     IRF2 is required for development and functional maturation of human
            NK cells
  JOURNAL   Front Immunol 13, 1038821 (2022)
   PUBMED   36544762
  REMARK    GeneRIF: IRF2 is required for development and functional maturation
            of human NK cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Chen,Y.J., Luo,S.N., Wu,H., Zhang,N.P., Dong,L., Liu,T.T., Liang,L.
            and Shen,X.Z.
  TITLE     IRF-2 inhibits cancer proliferation by promoting AMER-1
            transcription in human gastric cancer
  JOURNAL   J Transl Med 20 (1), 68 (2022)
   PUBMED   35115027
  REMARK    GeneRIF: IRF-2 inhibits cancer proliferation by promoting AMER-1
            transcription in human gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Ren,K., Zhu,Y., Sun,H., Li,S., Duan,X., Li,S., Li,Y., Li,B. and
            Chen,L.
  TITLE     IRF2 inhibits ZIKV replication by promoting FAM111A expression to
            enhance the host restriction effect of RFC3
  JOURNAL   Virol J 18 (1), 256 (2021)
   PUBMED   34930359
  REMARK    GeneRIF: IRF2 inhibits ZIKV replication by promoting FAM111A
            expression to enhance the host restriction effect of RFC3.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Harada,H., Takahashi,E., Itoh,S., Harada,K., Hori,T.A. and
            Taniguchi,T.
  TITLE     Structure and regulation of the human interferon regulatory factor
            1 (IRF-1) and IRF-2 genes: implications for a gene network in the
            interferon system
  JOURNAL   Mol Cell Biol 14 (2), 1500-1509 (1994)
   PUBMED   7507207
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Palombella,V.J. and Maniatis,T.
  TITLE     Inducible processing of interferon regulatory factor-2
  JOURNAL   Mol Cell Biol 12 (8), 3325-3336 (1992)
   PUBMED   1630448
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Itoh,S., Harada,H., Fujita,T., Mimura,T. and Taniguchi,T.
  TITLE     Sequence of a cDNA coding for human IRF-2
  JOURNAL   Nucleic Acids Res 17 (20), 8372 (1989)
   PUBMED   2813069
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Harada,H., Fujita,T., Miyamoto,M., Kimura,Y., Maruyama,M.,
            Furia,A., Miyata,T. and Taniguchi,T.
  TITLE     Structurally similar but functionally distinct factors, IRF-1 and
            IRF-2, bind to the same regulatory elements of IFN and
            IFN-inducible genes
  JOURNAL   Cell 58 (4), 729-739 (1989)
   PUBMED   2475256
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP200998.1, AA361545.1,
            BC015803.2 and BQ017798.1.
            
            On Jul 24, 2007 this sequence version replaced NP_002190.1.
            
            Summary: IRF2 encodes interferon regulatory factor 2, a member of
            the interferon regulatory transcription factor (IRF) family. IRF2
            competitively inhibits the IRF1-mediated transcriptional activation
            of interferons alpha and beta, and presumably other genes that
            employ IRF1 for transcription activation. However, IRF2 also
            functions as a transcriptional activator of histone H4. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.764367.1,
                                           SRR1660809.207099.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2150385 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393593.8/ ENSP00000377218.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q35.1"
     Protein         1..349
                     /product="interferon regulatory factor 2"
                     /calculated_mol_wt=39223
     Region          7..112
                     /region_name="IRF"
                     /note="Interferon regulatory factor transcription factor;
                     pfam00605"
                     /db_xref="CDD:459863"
     Site            order(40,80,82..83,86)
                     /site_type="other"
                     /note="DNA sequence recognition sites [nucleotide
                     binding]"
                     /db_xref="CDD:238051"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12738767; propagated from
                     UniProtKB/Swiss-Prot (P14316.2)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:12738767; propagated from
                     UniProtKB/Swiss-Prot (P14316.2)"
     Site            order(85..86,88,91)
                     /site_type="metal-binding"
                     /db_xref="CDD:238051"
     Region          117..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14316.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P14316.2)"
     Region          228..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14316.2)"
     Region          297..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P14316.2)"
     CDS             1..349
                     /gene="IRF2"
                     /gene_synonym="IRF-2"
                     /coded_by="NM_002199.4:179..1228"
                     /db_xref="CCDS:CCDS3835.1"
                     /db_xref="GeneID:3660"
                     /db_xref="HGNC:HGNC:6117"
                     /db_xref="MIM:147576"
ORIGIN      
        1 mpvermrmrp wleeqinsnt ipglkwlnke kkifqipwmh aarhgwdvek daplfrnwai
       61 htgkhqpgvd kpdpktwkan frcamnslpd ieevkdksik kgnnafrvyr mlplserpsk
      121 kgkkpkteke dkvkhikqep vesslglsng vsdlspeyav ltstiknevd stvniivvgq
      181 shldsnienq eivtnppdic qvvevttesd eqpvsmsely plqispvssy aesettdsvp
      241 sdeesaegrp hwrkrniegk qylsnmgtrg syllpgmasf vtsnkpdlqv tikeesnpvp
      301 ynsswppfqd lplsssmtpa ssssrpdret rasvikktsd itqarvksc
//
LOCUS       NP_001162119             898 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001162119
VERSION     NP_001162119.1
DBSOURCE    REFSEQ: accession NM_001168648.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 898)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 898)
  AUTHORS   Ito,H. and Nagata,K.I.
  TITLE     Functions of CNKSR2 and Its Association with Neurodevelopmental
            Disorders
  JOURNAL   Cells 11 (2), 303 (2022)
   PUBMED   35053419
  REMARK    GeneRIF: Functions of CNKSR2 and Its Association with
            Neurodevelopmental Disorders.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 898)
  AUTHORS   Toraman,B., Bilginer,S.C., Hesapcioglu,S.T., Goker,Z., Soykam,H.O.,
            Erguner,B., Dincer,T., Yildiz,G., Unsal,S., Kasap,B.K., Kandil,S.
            and Kalay,E.
  TITLE     Finding underlying genetic mechanisms of two patients with autism
            spectrum disorder carrying familial apparently balanced chromosomal
            translocations
  JOURNAL   J Gene Med 23 (4), e3322 (2021)
   PUBMED   33591602
  REMARK    GeneRIF: Finding underlying genetic mechanisms of two patients with
            autism spectrum disorder carrying familial apparently balanced
            chromosomal translocations.
REFERENCE   4  (residues 1 to 898)
  AUTHORS   Zhang,Y., Yu,T., Li,N., Wang,J., Wang,J., Ge,Y. and Yao,R.
  TITLE     Psychomotor development and attention problems caused by a splicing
            variant of CNKSR2
  JOURNAL   BMC Med Genomics 13 (1), 182 (2020)
   PUBMED   33298018
  REMARK    GeneRIF: Psychomotor development and attention problems caused by a
            splicing variant of CNKSR2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 898)
  AUTHORS   Daoqi,M., Guohong,C., Yuan,W., Zhixiao,Y., Kaili,X. and Shiyue,M.
  TITLE     Exons deletion of CNKSR2 gene identified in X-linked syndromic
            intellectual disability
  JOURNAL   BMC Med Genet 21 (1), 69 (2020)
   PUBMED   32245427
  REMARK    GeneRIF: This study enhances our knowledge of the CNKSR2 gene
            mutation spectrum and provides further information about the
            phenotypic characteristics of X-linked syndromic intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 898)
  AUTHORS   Wang,X., Patel,R. and Studzinski,G.P.
  TITLE     hKSR-2, a vitamin D-regulated gene, inhibits apoptosis in
            arabinocytosine-treated HL60 leukemia cells
  JOURNAL   Mol Cancer Ther 7 (9), 2798-2806 (2008)
   PUBMED   18790760
REFERENCE   7  (residues 1 to 898)
  AUTHORS   Rajakulendran,T., Sahmi,M., Kurinov,I., Tyers,M., Therrien,M. and
            Sicheri,F.
  TITLE     CNK and HYP form a discrete dimer by their SAM domains to mediate
            RAF kinase signaling
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 2836-2841 (2008)
   PUBMED   18287031
  REMARK    GeneRIF: CNK and HYP form a discrete dimer by their SAM domains to
            mediate RAF kinase signaling.
REFERENCE   8  (residues 1 to 898)
  AUTHORS   Bumeister,R., Rosse,C., Anselmo,A., Camonis,J. and White,M.A.
  TITLE     CNK2 couples NGF signal propagation to multiple regulatory cascades
            driving cell differentiation
  JOURNAL   Curr Biol 14 (5), 439-445 (2004)
   PUBMED   15028221
REFERENCE   9  (residues 1 to 898)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
  REMARK    GeneRIF: CNK2 through interaction with Raf and Rlf may function as
            a regulator of Ras signaling.
REFERENCE   10 (residues 1 to 898)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA067208.1, AF418270.1,
            BM692904.1, AK056549.1, Z40257.1, F09543.1, T65396.1 and
            AL772392.4.
            
            Summary: This gene encodes a multidomain protein that functions as
            a scaffold protein to mediate the mitogen-activated protein kinase
            pathways downstream from Ras. This gene product is induced by
            vitamin D and inhibits apoptosis in certain cancer cells. It may
            also play a role in ternary complex assembly of synaptic proteins
            at the postsynaptic membrane and coupling of signal transduction to
            membrane/cytoskeletal remodeling. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (3, also known as CNK2B and
            MAGUIN-2) differs in the 3' UTR and 3' coding region, compared to
            variant 1. It encodes isoform 3 which has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.162885.1,
                                           SRR1803612.153798.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..898
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..898
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 3"
                     /note="connector enhancer of KSR2; membrane-associated
                     guanylate kinase-interacting protein; CNK homolog protein
                     2"
                     /calculated_mol_wt=101743
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          324..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          339..>487
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          480..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          539..559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          559..672
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     Region          682..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T4; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T4; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     CDS             1..898
                     /gene="CNKSR2"
                     /gene_synonym="CNK2; KSR2; MAGUIN; MRXSHG"
                     /coded_by="NM_001168648.3:481..3177"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55387.1"
                     /db_xref="GeneID:22866"
                     /db_xref="HGNC:HGNC:19701"
                     /db_xref="MIM:300724"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv vgwqlknlvn alredpsgvi ltlkkrpqsm
      301 ltsapallkn mrwkplalqp liprsptssv atpsstistp tkrdssalqd lyippppaep
      361 yiprdekgnl pcedlrghmv gkpvhkgses pnsfldqeyr krfniveedt vlycyeyekg
      421 rsssqgrres tptygklrpi smpveynwvg dyedpnkmkr dsrrensllr ymsnekiaqe
      481 eymfqrnskk dtgkkskkkg dksnspthys llpslqmdal rqdimgtpvp ettlyhtfqq
      541 sslqhkskkk nkgpiagksk rrisckdlgr gdcegwlwkk kdaksyfsqk wkkywfvlkd
      601 aslywyinee dekaegfisl pefkidrase crkkyafkac hpkiksfyfa aehlddmnrw
      661 lnrinmltag yaererikqe qdywsesdke eadtpstpkq dsppppydty prppsmscas
      721 pyveakhsrl sstetsqsqs sheefrqevt gssavspirk tasqrrswqd lietpltssg
      781 lhylqtlple dsvfsdsaai spehrrqstl ptqkchlqdh ygpyplaese rmqvlngngg
      841 kprsftlprd sgfnhcclna pvsacdpqdd vqppeveeee eeeeeegeaa genigeks
//
LOCUS       NP_001354833             929 aa            linear   PRI 20-NOV-2025
DEFINITION  cell adhesion molecule DSCAML1 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001354833
VERSION     NP_001354833.1
DBSOURCE    REFSEQ: accession NM_001367904.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 929)
  AUTHORS   Ogata,S., Hashizume,K., Hayase,Y., Kanno,Y., Hori,K., Balan,S.,
            Yoshikawa,T., Takahashi,H., Taya,S. and Hoshino,M.
  TITLE     Potential involvement of DSCAML1 mutations in neurodevelopmental
            disorders
  JOURNAL   Genes Cells 26 (3), 136-151 (2021)
   PUBMED   33501714
  REMARK    GeneRIF: Potential involvement of DSCAML1 mutations in
            neurodevelopmental disorders.
REFERENCE   2  (residues 1 to 929)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   3  (residues 1 to 929)
  AUTHORS   Kosova,G., Hotaling,J.M., Ohlander,S., Niederberger,C., Prins,G.S.
            and Ober,C.
  TITLE     Variants in DPF3 and DSCAML1 are associated with sperm morphology
  JOURNAL   J Assist Reprod Genet 31 (2), 131-137 (2014)
   PUBMED   24271036
  REMARK    GeneRIF: DSCAML1 protein rs680730 SNP is associated with poor sperm
            morphology.
REFERENCE   4  (residues 1 to 929)
  AUTHORS   Huang,J., Wang,Y., Raghavan,S., Feng,S., Kiesewetter,K. and Wang,J.
  TITLE     Human down syndrome cell adhesion molecules (DSCAMs) are
            functionally conserved with Drosophila Dscam[TM1] isoforms in
            controlling neurodevelopment
  JOURNAL   Insect Biochem Mol Biol 41 (10), 778-787 (2011)
   PUBMED   21645617
REFERENCE   5  (residues 1 to 929)
  AUTHORS   Fuerst,P.G., Bruce,F., Tian,M., Wei,W., Elstrott,J., Feller,M.B.,
            Erskine,L., Singer,J.H. and Burgess,R.W.
  TITLE     DSCAM and DSCAML1 function in self-avoidance in multiple cell types
            in the developing mouse retina
  JOURNAL   Neuron 64 (4), 484-497 (2009)
   PUBMED   19945391
  REMARK    GeneRIF: in all transgenic retinal cell types examined, both DSCAM
            and DSCAM-LIKE1 genes are functioning similarly in self-avoidance,
            whereas the stratification of neurites and synaptic specificity are
            intact in their absence.
REFERENCE   6  (residues 1 to 929)
  AUTHORS   Pollin,T.I., Damcott,C.M., Shen,H., Ott,S.H., Shelton,J.,
            Horenstein,R.B., Post,W., McLenithan,J.C., Bielak,L.F.,
            Peyser,P.A., Mitchell,B.D., Miller,M., O'Connell,J.R. and
            Shuldiner,A.R.
  TITLE     A null mutation in human APOC3 confers a favorable plasma lipid
            profile and apparent cardioprotection
  JOURNAL   Science 322 (5908), 1702-1705 (2008)
   PUBMED   19074352
REFERENCE   7  (residues 1 to 929)
  AUTHORS   Barlow,G.M., Micales,B., Chen,X.N., Lyons,G.E. and Korenberg,J.R.
  TITLE     Mammalian DSCAMs: roles in the development of the spinal cord,
            cortex, and cerebellum?
  JOURNAL   Biochem Biophys Res Commun 293 (3), 881-891 (2002)
   PUBMED   12051741
REFERENCE   8  (residues 1 to 929)
  AUTHORS   Agarwala,K.L., Ganesh,S., Tsutsumi,Y., Suzuki,T., Amano,K. and
            Yamakawa,K.
  TITLE     Cloning and functional characterization of DSCAML1, a novel
            DSCAM-like cell adhesion molecule that mediates homophilic
            intercellular adhesion
  JOURNAL   Biochem Biophys Res Commun 285 (3), 760-772 (2001)
   PUBMED   11453658
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000757.4 and AP002342.3.
            
            Summary: The protein encoded by this gene is a member of the Ig
            superfamily of cell adhesion molecules and is involved in neuronal
            differentiation. The encoded membrane-bound protein localizes to
            the cell surface, where it forms aggregates that repel neuronal
            processes of the same cell type. [provided by RefSeq, Sep 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..929
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..929
                     /product="cell adhesion molecule DSCAML1 isoform 2
                     precursor"
                     /note="Downs syndrome cell adhesion molecule like 1; down
                     syndrome cell adhesion molecule-like protein 1; down
                     syndrome cell adhesion molecule 2; DSCAM-like 1; cell
                     adhesion molecule DSCAML1"
                     /calculated_mol_wt=100437
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2154
     Region          27..122
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            29
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          43..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          56..60
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          80..84
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          100..105
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          113..117
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          130..218
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          142..146
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          158..162
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          180..184
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          195..200
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..214
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          233..311
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          243..247
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          256..260
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          291..296
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          305..308
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          314..403
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          332..336
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          345..349
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            368
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          369..373
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          383..388
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          396..399
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          407..502
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          425..429
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          438..442
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          468..472
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            471
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          482..487
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          495..498
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          505..593
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            513
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          522..526
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          535..539
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            556
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          557..561
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          572..577
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          586..589
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          596..686
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          613..617
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          627..631
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          652..656
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          666..671
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            666
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          679..682
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          689..785
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig)-like domain of Down Syndrome
                     Cell Adhesion molecule (DSCAM); cd05734"
                     /db_xref="CDD:409397"
     Region          689..693
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409397"
     Region          698..702
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409397"
     Region          704..714
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409397"
     Site            710
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          720..726
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409397"
     Region          733..736
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409397"
     Region          745..748
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409397"
     Site            749
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          750..756
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409397"
     Region          763..771
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409397"
     Region          776..785
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409397"
     Region          786..886
                     /region_name="Ig_DSCAM"
                     /note="Immunoglobulin (Ig) domain of Down Syndrome Cell
                     Adhesion molecule (DSCAM); cd05735"
                     /db_xref="CDD:409398"
     Region          786..789
                     /region_name="putative Ig strand A"
                     /note="putative Ig strand A [structural motif]"
                     /db_xref="CDD:409398"
     Site            796
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          797..801
                     /region_name="putative Ig strand A'"
                     /note="putative Ig strand A' [structural motif]"
                     /db_xref="CDD:409398"
     Region          804..811
                     /region_name="putative Ig strand B"
                     /note="putative Ig strand B [structural motif]"
                     /db_xref="CDD:409398"
     Site            809
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     Region          819..825
                     /region_name="putative Ig strand C"
                     /note="putative Ig strand C [structural motif]"
                     /db_xref="CDD:409398"
     Region          835..838
                     /region_name="putative Ig strand C'"
                     /note="putative Ig strand C' [structural motif]"
                     /db_xref="CDD:409398"
     Region          844..848
                     /region_name="putative Ig strand D"
                     /note="putative Ig strand D [structural motif]"
                     /db_xref="CDD:409398"
     Region          850..856
                     /region_name="putative Ig strand E"
                     /note="putative Ig strand E [structural motif]"
                     /db_xref="CDD:409398"
     Region          863..871
                     /region_name="putative Ig strand F"
                     /note="putative Ig strand F [structural motif]"
                     /db_xref="CDD:409398"
     Region          874..884
                     /region_name="putative Ig strand G"
                     /note="putative Ig strand G [structural motif]"
                     /db_xref="CDD:409398"
     Region          888..>929
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            926
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TD84.2)"
     CDS             1..929
                     /gene="DSCAML1"
                     /gene_synonym="DSCAM2"
                     /coded_by="NM_001367904.1:138..2927"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:57453"
                     /db_xref="HGNC:HGNC:14656"
                     /db_xref="MIM:611782"
ORIGIN      
        1 mwlvtfllll dslhkarped vgtslyfvnd slqqvtfsss vgvvvpcpaa gspsaalrwy
       61 latgddiydv phirhvhang tlqlypfsps afnsfihdnd yfctaenaag kirspnirvk
      121 avfrepytvr vedqrsmrgn vavfkclips svqeyvsvvs wekdtvsiip ehrffityhg
      181 glyisdvqke dalstyrcit khkysgetrq sngarlsvtd paesiptild gfhsqevwag
      241 htvelpctas gypipairwl kdgrplpads rwtkritglt isdlrtedsg tyicevtntf
      301 gsaeatgilm vidplhvtlt pkklktgigs tvilscaltg speftirwyr ntelvlpdea
      361 isirglsnet llitsaqksh sgayqcfatr kaqtaqdfai ialedgtpri vssfsekvvn
      421 pgeqfslmca akgappptvt walddepivr dgshrtnqyt msdgttishm nvtgpqirdg
      481 gvyrctarnl vgsaeyqari nvrgppsira mrnitavagr dtlincrvig ypyysikwyk
      541 dalllpdnhr qvvfengtlk ltdvqkgmde geylcsvliq pqlsisqsvh vavkvppliq
      601 pfefppasig qllyipcvvs sgdmpiritw rkdgqviisg sgvtieskef msslqissvs
      661 lkhngnytci asnaaatvsr erqlivrvpp rfvvqpnnqd giygkagvln csvdgypppk
      721 vmwkhakgsg npqqyhpvpl tgriqilpns sllirhvlee digyylcqas ngvgtdisks
      781 mfltvkipam itshpnttia ikghakelnc targerpiii rwekgdtvid pdrvmryaia
      841 tkdngdevvs tlklkpadrg dsvffschai nsygedrgli qltvqeppdp peleirevka
      901 rsmnlrwtqr fdgnsiitgf dieyknksg
//
LOCUS       NP_115514                684 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch repeat and BTB domain-containing protein 7 [Homo sapiens].
ACCESSION   NP_115514
VERSION     NP_115514.2
DBSOURCE    REFSEQ: accession NM_032138.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Li,X., Lin,Z., Xu,S., Zhang,N., Zhou,J. and Liao,B.
  TITLE     Knockdown of KBTBD7 attenuates septic lung injury by inhibiting
            ferroptosis and improving mitochondrial dysfunction
  JOURNAL   Int Immunopharmacol 133, 112129 (2024)
   PUBMED   38652964
  REMARK    GeneRIF: Knockdown of KBTBD7 attenuates septic lung injury by
            inhibiting ferroptosis and improving mitochondrial dysfunction.
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Zou,Z., Zhang,B., Li,Z., Lei,L., Sun,G., Jiang,X., Guan,J.,
            Zhang,Y., Xu,S. and Li,Q.
  TITLE     KBTBD7 promotes non-small cell lung carcinoma progression by
            enhancing ubiquitin-dependent degradation of PTEN
  JOURNAL   Cancer Med 11 (23), 4544-4554 (2022)
   PUBMED   35499228
  REMARK    GeneRIF: KBTBD7 promotes non-small cell lung carcinoma progression
            by enhancing ubiquitin-dependent degradation of PTEN.
            Erratum:[Cancer Med. 2024 Sep;13(17):e7462. doi: 10.1002/cam4.7462.
            PMID: 39248706]
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Genau,H.M. and Behrends,C.
  TITLE     GABARAP proteins as scaffolds in localized TIAM1-RAC1 signaling
  JOURNAL   Mol Cell Oncol 3 (1), e1027440 (2015)
   PUBMED   27308540
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Genau,H.M., Huber,J., Baschieri,F., Akutsu,M., Dotsch,V.,
            Farhan,H., Rogov,V. and Behrends,C.
  TITLE     CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP
            proteins to spatially restrict TIAM1-RAC1 signaling
  JOURNAL   Mol Cell 57 (6), 995-1010 (2015)
   PUBMED   25684205
  REMARK    GeneRIF: KBTBD6 and KBTBD7 specifically bind to GABARAP
            proteins.KBTBD6 and KBTBD7 form a heterodimeric CRL3 complex.
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Hu,J., Yuan,W., Tang,M., Wang,Y., Fan,X., Mo,X., Li,Y., Ying,Z.,
            Wan,Y., Ocorr,K., Bodmer,R., Deng,Y. and Wu,X.
  TITLE     KBTBD7, a novel human BTB-kelch protein, activates transcriptional
            activities of SRE and AP-1
  JOURNAL   BMB Rep 43 (1), 17-22 (2010)
   PUBMED   20132730
  REMARK    GeneRIF: KBTBD7 proteins may act as a new transcriptional activator
            in mitogen-activated protein kinase (MAPK) signaling.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354696.11, BC022033.2,
            AI631319.1, BU070208.1, BF436101.1, HY094395.1 and BU069965.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2002 this sequence version replaced NP_115514.1.
            
            Summary: The protein encoded by this gene is a transcriptional
            activator, having been shown to increase the transcription of
            activator protein-1 and serum response element. The encoded protein
            can also form a complex with KBTBD6 and CUL3, which regulates the
            ubiquitylation and degradation of TIAM1, which is a regulator of
            RAC1. [provided by RefSeq, Jul 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK091344.1, FJ150424.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379483.4/ ENSP00000368797.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..684
                     /product="kelch repeat and BTB domain-containing protein
                     7"
                     /note="kelch repeat and BTB (POZ) domain containing 7"
                     /calculated_mol_wt=77033
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          37..178
                     /region_name="BTB_POZ_KBTBD6_7"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing proteins KBTBD6 and KBTBD7;
                     cd18273"
                     /db_xref="CDD:349582"
     Region          55..544
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          168..270
                     /region_name="BACK_KBTBD6_7"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing proteins, KBTBD6
                     and KBTBD7; cd18482"
                     /db_xref="CDD:350557"
     Region          384..421
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          386..435
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          425..471
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          436..484
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          474..511
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          486..523
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          512..551
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          524..564
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          567..616
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          630..666
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     Region          668..671
                     /region_name="ATG8 interaction motif (AIM).
                     /evidence=ECO:0000269|PubMed:25684205"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WVZ9.1)"
     CDS             1..684
                     /gene="KBTBD7"
                     /coded_by="NM_032138.7:313..2367"
                     /db_xref="CCDS:CCDS9377.1"
                     /db_xref="GeneID:84078"
                     /db_xref="HGNC:HGNC:25266"
                     /db_xref="MIM:617739"
ORIGIN      
        1 mqsredvprs rrlasprggr rpkriskpsv safftgpeel kdtahsaall aqlksfydar
       61 llcdvtievv tpgsgpgtgr lfscnrnvla aacpyfksmf tggmyesqqa svtmhdvdae
      121 sfevlvdycy tgrvslsean vqrlyaasdm lqleyvreac asflarrldl tnctailkfa
      181 dafdhhklrs qaqsyiahnf kqlsrmgsir eetladltla qllavlrlds ldiesertvc
      241 hvavqwleaa akergpsaae vfkcvrwmhf teedqdyleg lltkpivkky cldviegalq
      301 mrygdllyks lvpvpnssss ssssnslvsa aenppqrlgm cakemviffg hprdpflcyd
      361 pysgdiytmp spltsfahtk tvtssavcvs pdhdiylaaq prkdlwvykp aqnswqqlad
      421 rllcregmdv aylngyiyil ggrdpitgvk lkevecysvq rnqwalvapv phsfysfeli
      481 vvqnylyavn skrmlcydps hnmwlncasl krsdfqeacv fndeiycicd ipvmkvynpa
      541 rgewrrisni pldsethnyq ivnhdqklll itsttpqwkk nrvtvyeydt redqwinigt
      601 mlgllqfdsg ficlcarvyp sclepgqsfi teeddarses stewdldgfs eldsesgsss
      661 sfsddevwvq vapqrnaqdq qgsl
//
LOCUS       NP_001240790             122 aa            linear   PRI 20-NOV-2025
DEFINITION  meiotic nuclear division protein 1 homolog isoform 2 [Homo
            sapiens].
ACCESSION   NP_001240790
VERSION     NP_001240790.1
DBSOURCE    REFSEQ: accession NM_001253861.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Fang,J., Zhen,J., Gong,Y., Ke,Y., Fu,B., Jiang,Y., Xie,J., Liu,Y.,
            Ding,Y., Huang,D. and Xiao,F.
  TITLE     MND1 functions as a potential prognostic biomarker associated with
            cell cycle and immune infiltration in kidney renal clear cell
            carcinoma
  JOURNAL   Aging (Albany NY) 14 (18), 7416-7442 (2022)
   PUBMED   36098680
  REMARK    GeneRIF: MND1 functions as a potential prognostic biomarker
            associated with cell cycle and immune infiltration in kidney renal
            clear cell carcinoma.
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Wei,J., Meng,G., Wu,J., Zhang,Q. and Zhang,J.
  TITLE     Genetic network and gene set enrichment analyses identify MND1 as
            potential diagnostic and therapeutic target gene for lung
            adenocarcinoma
  JOURNAL   Sci Rep 11 (1), 9430 (2021)
   PUBMED   33941804
  REMARK    GeneRIF: Genetic network and gene set enrichment analyses identify
            MND1 as potential diagnostic and therapeutic target gene for lung
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Dorosh,A., Tepla,O., Zatecka,E., Ded,L., Koci,K. and Peknicova,J.
  TITLE     Expression analysis of MND1/GAJ, SPATA22, GAPDHS and ACR genes in
            testicular biopsies from non-obstructive azoospermia (NOA) patients
  JOURNAL   Reprod Biol Endocrinol 11, 42 (2013)
   PUBMED   23675907
  REMARK    GeneRIF: Data indicate that the positive expression of studied
            genes fertilization rate for GAPDHS positive subset was 66%, ACR -
            71%, SPATA22 - 68%, MND1 - 70%, pregnancy rates were 8%, 6%, 18%
            and 36% respectively.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Chi,P., San Filippo,J., Sehorn,M.G., Petukhova,G.V. and Sung,P.
  TITLE     Bipartite stimulatory action of the Hop2-Mnd1 complex on the Rad51
            recombinase
  JOURNAL   Genes Dev 21 (14), 1747-1757 (2007)
   PUBMED   17639080
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Enomoto,R., Kinebuchi,T., Sato,M., Yagi,H., Kurumizaka,H. and
            Yokoyama,S.
  TITLE     Stimulation of DNA strand exchange by the human TBPIP/Hop2-Mnd1
            complex
  JOURNAL   J Biol Chem 281 (9), 5575-5581 (2006)
   PUBMED   16407260
  REMARK    GeneRIF: Data suggest that the human TBPIP/Hop2-Mnd1 complex may
            ensure proper pairing between homologous chromosomes through its
            stimulation of strand exchange during meiosis.
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Tsubouchi,H. and Roeder,G.S.
  TITLE     The Mnd1 protein forms a complex with hop2 to promote homologous
            chromosome pairing and meiotic double-strand break repair
  JOURNAL   Mol Cell Biol 22 (9), 3078-3088 (2002)
   PUBMED   11940665
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM820228.1, BG613292.1, BU533354.1 and AA542845.1.
            
            Summary: The product of the MND1 gene associates with HOP2 (MIM
            608665) to form a stable heterodimeric complex that binds DNA and
            stimulates the recombinase activity of RAD51 (MIM 179617) and DMC1
            (MIM 602721) (Chi et al., 2007 [PubMed 17639080]). Both the MND1
            and HOP2 genes are indispensable for meiotic
            recombination.[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the 3' coding
            region, which results in a frameshift, compared to variant 1. The
            encoded isoform (2) is shorter and has a distinct C-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU935172.1, BG613292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.3"
     Protein         1..122
                     /product="meiotic nuclear division protein 1 homolog
                     isoform 2"
                     /note="homolog of yeast MND1; meiotic nuclear division
                     protein 1 homolog; meiotic nuclear divisions 1 homolog"
                     /calculated_mol_wt=13713
     Region          16..75
                     /region_name="Mnd1"
                     /note="Mnd1 HTH domain; pfam03962"
                     /db_xref="CDD:461112"
     CDS             1..122
                     /gene="MND1"
                     /gene_synonym="GAJ"
                     /coded_by="NM_001253861.1:90..458"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75202.1"
                     /db_xref="GeneID:84057"
                     /db_xref="HGNC:HGNC:24839"
                     /db_xref="MIM:611422"
ORIGIN      
        1 mskkkglsae ekrtrmmeif setkdvfqlk dlekiapkek gitamsvkev lqslvddgmv
       61 dcerigtsny ywafpskalh arkhklevle sqlsegsqkh aslqksieka kigrcetakq
      121 ik
//
LOCUS       NP_001186208             479 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-6 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001186208
VERSION     NP_001186208.1
DBSOURCE    REFSEQ: accession NM_001199279.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Su,J., Yu,Z., Yin,Z., Zhang,Z., Zhao,J., Meng,Y., Li,R., Gao,Y.,
            Zhang,H., Yu,R. and Zhao,Y.
  TITLE     Molecular insights into the alpha6beta4 nicotinic acetylcholine
            receptor function and ligand recognition
  JOURNAL   Nat Commun 16 (1), 3153 (2025)
   PUBMED   40175361
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Zhang,F., Zhang,M., Yuan,X., Tao,Y. and Wang,J.
  TITLE     Involvement of CHRNA6 in the Immune Response in Lung Squamous Cell
            Carcinoma and its Potential as a Drug Target for the Disease
  JOURNAL   Curr Pharm Des 29 (26), 2091-2100 (2023)
   PUBMED   37680128
  REMARK    GeneRIF: Involvement of CHRNA6 in the Immune Response in Lung
            Squamous Cell Carcinoma and its Potential as a Drug Target for the
            Disease.
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Wen,L., Han,H., Liu,Q., Su,K., Yang,Z., Cui,W., Yuan,W., Ma,Y.,
            Fan,R., Chen,J., Jiang,K., Jiang,X., Payne,T.J., Wang,J. and
            Li,M.D.
  TITLE     Significant association of the CHRNB3-CHRNA6 gene cluster with
            nicotine dependence in the Chinese Han population
  JOURNAL   Sci Rep 7 (1), 9745 (2017)
   PUBMED   28851948
  REMARK    GeneRIF: This study is the first showing that CHRNB3/A6 are highly
            associated with nicotine dependence in a large Chinese Han sample.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Arvaniti,M., Jensen,M.M., Soni,N., Wang,H., Klein,A.B., Thiriet,N.,
            Pinborg,L.H., Muldoon,P.P., Wienecke,J., Imad Damaj,M.,
            Kohlmeier,K.A., Gondre-Lewis,M.C., Mikkelsen,J.D. and Thomsen,M.S.
  TITLE     Functional interaction between Lypd6 and nicotinic acetylcholine
            receptors
  JOURNAL   J Neurochem 138 (6), 806-820 (2016)
   PUBMED   27344019
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Zeiger,J.S., Haberstick,B.C., Schlaepfer,I., Collins,A.C.,
            Corley,R.P., Crowley,T.J., Hewitt,J.K., Hopfer,C.J., Lessem,J.,
            McQueen,M.B., Rhee,S.H. and Ehringer,M.A.
  TITLE     The neuronal nicotinic receptor subunit genes (CHRNA6 and CHRNB3)
            are associated with subjective responses to tobacco
  JOURNAL   Hum Mol Genet 17 (5), 724-734 (2008)
   PUBMED   18055561
  REMARK    GeneRIF: CHRNA6 is associated with subjective responses to tobacco.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Ebihara,M., Ohba,H., Ohno,S.I. and Yoshikawa,T.
  TITLE     Genomic organization and promoter analysis of the human nicotinic
            acetylcholine receptor alpha6 subunit (CHNRA6) gene: Alu and other
            elements direct transcriptional repression
  JOURNAL   Gene 298 (1), 101-108 (2002)
   PUBMED   12406580
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Bonati,M.T., Combi,R., Asselta,R., Duga,S., Malcovati,M.,
            Oldani,A., Zucconi,M., Ferini-Strambi,L., Dalpra,L. and
            Tenchini,M.L.
  TITLE     Exclusion of linkage of nine neuronal nicotinic acetylcholine
            receptor subunit genes expressed in brain in autosomal dominant
            nocturnal frontal lobe epilepsy in four unrelated families
  JOURNAL   J Neurol 249 (8), 967-974 (2002)
   PUBMED   12195439
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Graham,A., Court,J.A., Martin-Ruiz,C.M., Jaros,E., Perry,R.,
            Volsen,S.G., Bose,S., Evans,N., Ince,P., Kuryatov,A., Lindstrom,J.,
            Gotti,C. and Perry,E.K.
  TITLE     Immunohistochemical localisation of nicotinic acetylcholine
            receptor subunits in human cerebellum
  JOURNAL   Neuroscience 113 (3), 493-507 (2002)
   PUBMED   12150770
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Le Novere,N., Zoli,M. and Changeux,J.P.
  TITLE     Neuronal nicotinic receptor alpha 6 subunit mRNA is selectively
            concentrated in catecholaminergic nuclei of the rat brain
  JOURNAL   Eur J Neurosci 8 (11), 2428-2439 (1996)
   PUBMED   8950106
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC307404.1, AK298798.1 and
            BC014456.1.
            
            Summary: This gene encodes an alpha subunit of neuronal nicotinic
            acetylcholine receptors. These receptors consist of five subunits
            and function as ion channels involved in neurotransmission. The
            encoded protein is a subunit of neuronal nicotinic acetylcholine
            receptors that mediate dopaminergic neurotransmission and are
            activated by acetylcholine and exogenous nicotine. Alternatively
            spliced transcript variants have been observed for this gene.
            Single nucleotide polymorphisms in this gene have been associated
            with both nicotine and alcohol dependence. [provided by RefSeq, Dec
            2010].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region but maintains the reading frame, compared to variant 1. This
            variant encodes isoform 2, which is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298798.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..479
                     /product="neuronal acetylcholine receptor subunit alpha-6
                     isoform 2 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     6; neuronal acetylcholine receptor subunit alpha-6;
                     acetylcholine receptor, nicotinic, alpha 6 (neuronal);
                     cholinergic receptor, nicotinic, alpha 6 (neuronal);
                     cholinergic receptor, nicotinic alpha 6; alpha(alpha)6
                     nicotinic acetylcholine receptor (nAChR) subunit"
                     /calculated_mol_wt=51788
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3248
     mat_peptide     31..479
                     /product="neuronal acetylcholine receptor subunit alpha-6
                     isoform 2"
                     /calculated_mol_wt=51788
     Region          34..469
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          34..225
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(69,71,92,94,103..104,106,108..109,120..122,124,134,
                     136,138,142,164,224)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     CDS             1..479
                     /gene="CHRNA6"
                     /gene_synonym="CHNRA6"
                     /coded_by="NM_001199279.1:357..1796"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS56536.1"
                     /db_xref="GeneID:8973"
                     /db_xref="HGNC:HGNC:15963"
                     /db_xref="MIM:606888"
ORIGIN      
        1 mltskgqgfl hgglclwlcv ftpffkgcvg cateerlfhk lfshynqfir pvenvsdpvt
       61 vhfevaitql anviwndykl rwdpmeydgi etlrvpadki wkpdivlynn avgdfqvegk
      121 tkallkyngm itwtppaifk sscpmditff pfdhqncslk fgswtydkae idlliigskv
      181 dmndfwense weiidasgyk hdikynccee iytditysfy irrlpmfyti nliipclfis
      241 fltvlvfylp sdcgekvtlc isvllsltvf llvitetips tslvvplvge yllftmifvt
      301 lsivvtvfvl nihyrtptth tmprwvktvf lkllpqvllm rwpldktrgt gsdavprgla
      361 rrpakgklas hgeprhlkec fhchksnela tskrrlshqp lqwvvenseh spevedvins
      421 vqfiaenmks hnetkevedd wkyvamvvdr vflwvfiivc vfgtaglflq pllgntgks
//
LOCUS       NP_699199                370 aa            linear   PRI 20-NOV-2025
DEFINITION  gap junction delta-4 protein [Homo sapiens].
ACCESSION   NP_699199
VERSION     NP_699199.2
DBSOURCE    REFSEQ: accession NM_153368.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Cea,L.A., Bevilacqua,J.A., Arriagada,C., Cardenas,A.M., Bigot,A.,
            Mouly,V., Saez,J.C. and Caviedes,P.
  TITLE     The absence of dysferlin induces the expression of functional
            connexin-based hemichannels in human myotubes
  JOURNAL   BMC Cell Biol 17 Suppl 1 (Suppl 1), 15 (2016)
   PUBMED   27229680
  REMARK    GeneRIF: Human deltoid muscle biopsies of 5 Chilean dysferlinopathy
            patients exhibited the presence of muscular connexins (Cx40.1, Cx43
            and Cx45).
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Vaiyapuri,S., Moraes,L.A., Sage,T., Ali,M.S., Lewis,K.R.,
            Mahaut-Smith,M.P., Oviedo-Orta,E., Simon,A.M. and Gibbins,J.M.
  TITLE     Connexin40 regulates platelet function
  JOURNAL   Nat Commun 4, 2564 (2013)
   PUBMED   24096827
  REMARK    GeneRIF: Connexin40 regulates platelet function.
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Gemel,J., Nelson,T.K., Burt,J.M. and Beyer,E.C.
  TITLE     Inducible coexpression of connexin37 or connexin40 with connexin43
            selectively affects intercellular molecular transfer
  JOURNAL   J Membr Biol 245 (5-6), 231-241 (2012)
   PUBMED   22729648
  REMARK    GeneRIF: The data show that induced expression of either Cx37 or
            Cx40 in Cx43-expressing cells can selectively alter the
            intercellular exchange of some molecules without affecting the
            transfer of others.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Sohl,G., Nielsen,P.A., Eiberger,J. and Willecke,K.
  TITLE     Expression profiles of the novel human connexin genes hCx30.2,
            hCx40.1, and hCx62 differ from their putative mouse orthologues
  JOURNAL   Cell Commun Adhes 10 (1), 27-36 (2003)
   PUBMED   12881038
  REMARK    GeneRIF: expression patterns differ from mouse orthologs [Cx30.2;
            Cx40.1]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121749.14, AK074504.1 and AJ414564.1.
            
            On Apr 25, 2007 this sequence version replaced NP_699199.1.
            
            Summary: Connexins, such as GJD4, are involved in the formation of
            gap junctions, intercellular conduits that directly connect the
            cytoplasms of contacting cells. Each gap junction channel is formed
            by docking of 2 hemichannels, each of which contains 6 connexin
            subunits (Sohl et al., 2003 [PubMed 12881038]).[supplied by OMIM,
            Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074504.1, AJ414564.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321660.2/ ENSP00000315070.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.21"
     Protein         1..370
                     /product="gap junction delta-4 protein"
                     /note="connexin40.1; connexin-40.1; gap junction protein,
                     delta 4, 40.1kDa"
                     /calculated_mol_wt=40009
     Region          5..218
                     /region_name="Connexin"
                     /note="pfam00029"
                     /db_xref="CDD:459638"
     Site            20..40
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KN9.1)"
     Site            77..97
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KN9.1)"
     Site            147..167
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KN9.1)"
     Site            197..217
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KN9.1)"
     Region          224..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96KN9.1)"
     Region          <232..361
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..370
                     /gene="GJD4"
                     /gene_synonym="CX40.1"
                     /coded_by="NM_153368.3:228..1340"
                     /db_xref="CCDS:CCDS7191.1"
                     /db_xref="GeneID:219770"
                     /db_xref="HGNC:HGNC:23296"
                     /db_xref="MIM:611922"
ORIGIN      
        1 megvdllgfl iitlncnvtm vgklwfvltm llrmlvivla grpvyqdeqe rfvcntlqpg
       61 canvcydvfs pvshlrfwli qgvcvllpsa vfsvyvlhrg atlaalgprr cpdprepasg
      121 qrrcprpfge rgglqvpdfs agyiihlllr tlleaafgal hyflfgflap kkfpctrppc
      181 tgvvdcyvsr pteksllmlf lwavsalsfl lgladlvcsl rrrmrrrpgp ptspsirkqs
      241 gasghaegrr tdeeggreee gapappgara ggegagsprr tsrvsghtki pdedesevts
      301 saseklgrqp rgrphreaaq dprgsgseeq psaapsrlaa ppscsslqpp dppasssgap
      361 hlrarksewv
//
LOCUS       NP_001335140             629 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform q [Homo sapiens].
ACCESSION   NP_001335140 XP_005266804
VERSION     NP_001335140.1
DBSOURCE    REFSEQ: accession NM_001348211.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 629)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 629)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 629)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 629)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 629)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 629)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 629)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 629)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 629)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 629)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AK096862.1,
            BM011452.1 and AC091103.4.
            
            On Jan 24, 2017 this sequence version replaced XP_005266804.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (17) contains an alternate exon in
            the 5' UTR, lacks a portion of the 5' coding region, and initiates
            translation at an alternate start codon, compared to variant 3. The
            resulting isoform (q) is shorter at the N-terminus compared to
            isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.146036.1,
                                           SRR3476690.416969.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..629
                     /product="transcription factor 4 isoform q"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=67383
     Region          520..604
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(528,532,534..536,538,543,564..565)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(541..542,545..546,548..549,552,556,566,569,573,576,
                     579..584)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..629
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348211.2:176..2065"
                     /note="isoform q is encoded by transcript variant 17"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 meedsrdved rsssgswgng ghpspsrnyg dgtpydhmts rdlgshdnls ppfvnsriqs
       61 ktergsyssy gresnlqgch qqsllggdmd mgnpgtlspt kpgsqyyqys snnprrrplh
      121 ssamevqtkk vrkvppglps svyapsasta dynrdspgyp sskpatstfp ssffmqdghh
      181 ssdpwssssg mnqpgyagml gnsshipqss sycslhpher lsypshssad insslppmst
      241 fhrsgtnhys tssctppang tdsimanrgs gaagssqtgd algkalasiy spdhtnnsfs
      301 snpstpvgsp pslsagtavw srnggqasss pnyegplhsl qsriedrler lddaihvlrn
      361 havgpstamp gghgdmhgii gpshngamgg lgsgygtgll sanrhslmvg thredgvalr
      421 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      481 lqdtkssedk kldddkkdik sitrsrssnn ddedltpeqk aerekerrma nnarerlrvr
      541 dineafkelg rmvqlhlksd kpqtkllilh qavavilsle qqvrernlnp kaaclkrree
      601 ekvssepppl slagphpgmg dasnhmgqm
//
LOCUS       NP_001308748             348 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair protein RAD51 homolog 2 isoform 8 [Homo sapiens].
ACCESSION   NP_001308748
VERSION     NP_001308748.1
DBSOURCE    REFSEQ: accession NM_001321819.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Slupianek,A., Jozwiakowski,S.K., Gurdek,E. and Skorski,T.
  TITLE     BCR/ABL kinase interacts with and phosphorylates the RAD51 paralog,
            RAD51B
  JOURNAL   Leukemia 23 (12), 2308-2310 (2009)
   PUBMED   19657362
  REMARK    GeneRIF: BCR/ABL fragments were used for identifying the sites of
            BCR/ABL interaction with RAD51B
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Thomas,G., Jacobs,K.B., Kraft,P., Yeager,M., Wacholder,S.,
            Cox,D.G., Hankinson,S.E., Hutchinson,A., Wang,Z., Yu,K.,
            Chatterjee,N., Garcia-Closas,M., Gonzalez-Bosquet,J.,
            Prokunina-Olsson,L., Orr,N., Willett,W.C., Colditz,G.A.,
            Ziegler,R.G., Berg,C.D., Buys,S.S., McCarty,C.A., Feigelson,H.S.,
            Calle,E.E., Thun,M.J., Diver,R., Prentice,R., Jackson,R.,
            Kooperberg,C., Chlebowski,R., Lissowska,J., Peplonska,B.,
            Brinton,L.A., Sigurdson,A., Doody,M., Bhatti,P., Alexander,B.H.,
            Buring,J., Lee,I.M., Vatten,L.J., Hveem,K., Kumle,M., Hayes,R.B.,
            Tucker,M., Gerhard,D.S., Fraumeni,J.F. Jr., Hoover,R.N.,
            Chanock,S.J. and Hunter,D.J.
  TITLE     A multistage genome-wide association study in breast cancer
            identifies two new risk alleles at 1p11.2 and 14q24.1 (RAD51L1)
  JOURNAL   Nat Genet 41 (5), 579-584 (2009)
   PUBMED   19330030
  REMARK    GeneRIF: A multistage genome-wide association study in breast
            cancer identifies two new risk alleles at 1p11.2 and 14q24.1
            (RAD51L1).
            GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Quade,B.J., Weremowicz,S., Neskey,D.M., Vanni,R., Ladd,C., Dal
            Cin,P. and Morton,C.C.
  TITLE     Fusion transcripts involving HMGA2 are not a common molecular
            mechanism in uterine leiomyomata with rearrangements in 12q15
  JOURNAL   Cancer Res 63 (6), 1351-1358 (2003)
   PUBMED   12649198
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Lio,Y.C., Mazin,A.V., Kowalczykowski,S.C. and Chen,D.J.
  TITLE     Complex formation by the human Rad51B and Rad51C DNA repair
            proteins and their activities in vitro
  JOURNAL   J Biol Chem 278 (4), 2469-2478 (2003)
   PUBMED   12427746
  REMARK    GeneRIF: Rad51B and Rad51C function through interactions with the
            human Rad51 recombinase and play a crucial role in the homologous
            recombinational repair pathway
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Masson,J.Y., Tarsounas,M.C., Stasiak,A.Z., Stasiak,A., Shah,R.,
            McIlwraith,M.J., Benson,F.E. and West,S.C.
  TITLE     Identification and purification of two distinct complexes
            containing the five RAD51 paralogs
  JOURNAL   Genes Dev 15 (24), 3296-3307 (2001)
   PUBMED   11751635
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Takata,M., Sasaki,M.S., Sonoda,E., Fukushima,T., Morrison,C.,
            Albala,J.S., Swagemakers,S.M., Kanaar,R., Thompson,L.H. and
            Takeda,S.
  TITLE     The Rad51 paralog Rad51B promotes homologous recombinational repair
  JOURNAL   Mol Cell Biol 20 (17), 6476-6482 (2000)
   PUBMED   10938124
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Cartwright,R., Dunn,A.M., Simpson,P.J., Tambini,C.E. and Thacker,J.
  TITLE     Isolation of novel human and mouse genes of the recA/RAD51
            recombination-repair gene family
  JOURNAL   Nucleic Acids Res 26 (7), 1653-1659 (1998)
   PUBMED   9512535
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Albala,J.S., Thelen,M.P., Prange,C., Fan,W., Christensen,M.,
            Thompson,L.H. and Lennon,G.G.
  TITLE     Identification of a novel human RAD51 homolog, RAD51B
  JOURNAL   Genomics 46 (3), 476-479 (1997)
   PUBMED   9441753
  REMARK    Erratum:[Genomics 1998 Aug 1;51(3):480]
REFERENCE   10 (residues 1 to 348)
  AUTHORS   Rice,M.C., Smith,S.T., Bullrich,F., Havre,P. and Kmiec,E.B.
  TITLE     Isolation of human and mouse genes based on homology to REC2, a
            recombinational repair gene from the fungus Ustilago maydis
  JOURNAL   Proc Natl Acad Sci U S A 94 (14), 7417-7422 (1997)
   PUBMED   9207106
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121595.5, AL122013.5 and
            AL589168.3.
            
            Summary: The protein encoded by this gene is a member of the RAD51
            protein family. RAD51 family members are evolutionarily conserved
            proteins essential for DNA repair by homologous recombination. This
            protein has been shown to form a stable heterodimer with the family
            member RAD51C, which further interacts with the other family
            members, such as RAD51, XRCC2, and XRCC3. Overexpression of this
            gene was found to cause cell cycle G1 delay and cell apoptosis,
            which suggested a role of this protein in sensing DNA damage.
            Rearrangements between this locus and high mobility group AT-hook 2
            (HMGA2, GeneID 8091) have been observed in uterine leiomyomata.
            [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.177703.1,
                                           SRR14038195.327093.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2146236
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..348
                     /product="DNA repair protein RAD51 homolog 2 isoform 8"
                     /note="RecA-like protein; recombination repair protein;
                     DNA repair protein RAD51 homolog 2; RAD51 homolog B"
                     /calculated_mol_wt=37890
     Region          1..75
                     /region_name="Interaction with RAD51C"
                     /note="propagated from UniProtKB/Swiss-Prot (O15315.2)"
     Region          91..327
                     /region_name="Rad51B"
                     /note="RAD51B recombinase; cd19493"
                     /db_xref="CDD:410901"
     Site            order(111..116,144,210,258,312)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:410901"
     Site            252..253
                     /site_type="other"
                     /note="Breakpoint for translocation to form HMGA2-RAD51B;
                     propagated from UniProtKB/Swiss-Prot (O15315.2)"
     CDS             1..348
                     /gene="RAD51B"
                     /gene_synonym="R51H2; RAD51L1; REC2"
                     /coded_by="NM_001321819.1:78..1124"
                     /note="isoform 8 is encoded by transcript variant 10"
                     /db_xref="GeneID:5890"
                     /db_xref="HGNC:HGNC:9822"
                     /db_xref="MIM:602948"
ORIGIN      
        1 mgskklkrvg lsqelcdrls rhqiltcqdf lclsplelmk vtglsyrgvh ellcmvsrac
       61 apkmqtaygi kaqrsadfsp aflsttlsal dealhggvac gslteitgpp gcgktqfcim
      121 msilatlptn mgglegavvy idtesafsae rlveiaesrf pryfnteekl lltsskvhly
      181 reltcdevlq riesleeeii skgiklvild svasvvrkef daqlqgnlke rnkflareas
      241 slkylaeefs ipviltnqit thlsgalasq adlvspaddl slsegtsgss cviaalgntw
      301 shsvntrlil qyldserrqi liaksplapf tsfvytikee glvlqagk
//
LOCUS       NP_006365                426 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 25 isoform 1 [Homo sapiens].
ACCESSION   NP_006365
VERSION     NP_006365.2
DBSOURCE    REFSEQ: accession NM_006374.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Chen,K.Q., Lei,G.L., Ke,B.Y., Chen,L., Wang,Z.B. and Wang,S.Z.
  TITLE     STK25: a viable therapeutic target for cancer treatments?
  JOURNAL   Anticancer Drugs 34 (9), 995-1001 (2023)
   PUBMED   36728989
  REMARK    GeneRIF: STK25: a viable therapeutic target for cancer treatments?
            Review article
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Zhang,X., Wang,B.Z., Kim,M., Nash,T.R., Liu,B., Rao,J., Lock,R.,
            Tamargo,M., Soni,R.K., Belov,J., Li,E., Vunjak-Novakovic,G. and
            Fine,B.
  TITLE     STK25 inhibits PKA signaling by phosphorylating PRKAR1A
  JOURNAL   Cell Rep 40 (7), 111203 (2022)
   PUBMED   35977512
  REMARK    GeneRIF: STK25 inhibits PKA signaling by phosphorylating PRKAR1A.
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Chen,J., Gao,P., Peng,L., Liu,T., Wu,F., Xu,K., Chen,L., Tan,F.,
            Xing,P., Wang,Z., Di,J., Jiang,B. and Su,X.
  TITLE     Downregulation of STK25 promotes autophagy via the Janus kinase
            2/signal transducer and activator of transcription 3 pathway in
            colorectal cancer
  JOURNAL   Mol Carcinog 61 (6), 572-586 (2022)
   PUBMED   35349179
  REMARK    GeneRIF: Downregulation of STK25 promotes autophagy via the Janus
            kinase 2/signal transducer and activator of transcription 3 pathway
            in colorectal cancer.
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Voss,K., Stahl,S., Schleider,E., Ullrich,S., Nickel,J.,
            Mueller,T.D. and Felbor,U.
  TITLE     CCM3 interacts with CCM2 indicating common pathogenesis for
            cerebral cavernous malformations
  JOURNAL   Neurogenetics 8 (4), 249-256 (2007)
   PUBMED   17657516
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Findlay,G.M., Yan,L., Procter,J., Mieulet,V. and Lamb,R.F.
  TITLE     A MAP4 kinase related to Ste20 is a nutrient-sensitive regulator of
            mTOR signalling
  JOURNAL   Biochem J 403 (1), 13-20 (2007)
   PUBMED   17253963
  REMARK    GeneRIF: Ste20 family member (MAP4K3) that is required for maximal
            S6K (S6 kinase)/4E-BP1 [eIF4E (eukaryotic initiation factor 4E)
            that is required for maximal S6K (S6 kinase).
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Preisinger,C., Short,B., De Corte,V., Bruyneel,E., Haas,A.,
            Kopajtich,R., Gettemans,J. and Barr,F.A.
  TITLE     YSK1 is activated by the Golgi matrix protein GM130 and plays a
            role in cell migration through its substrate 14-3-3zeta
  JOURNAL   J Cell Biol 164 (7), 1009-1020 (2004)
   PUBMED   15037601
  REMARK    GeneRIF: 14-3-3zeta is a specific substrate for YSK1 that localizes
            to the Golgi apparatus, and potentially links YSK1 signaling at the
            Golgi apparatus with protein transport.
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Osada,S., Izawa,M., Saito,R., Mizuno,K., Suzuki,A., Hirai,S. and
            Ohno,S.
  TITLE     YSK1, a novel mammalian protein kinase structurally related to
            Ste20 and SPS1, but is not involved in the known MAPK pathways
  JOURNAL   Oncogene 14 (17), 2047-2057 (1997)
   PUBMED   9160885
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Pombo,C.M., Bonventre,J.V., Molnar,A., Kyriakis,J. and Force,T.
  TITLE     Activation of a human Ste20-like kinase by oxidant stress defines a
            novel stress response pathway
  JOURNAL   EMBO J 15 (17), 4537-4546 (1996)
   PUBMED   8887545
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC007852.2, HY315908.1 and
            AC110299.3.
            
            On Jun 10, 2002 this sequence version replaced NP_006365.1.
            
            Summary: This gene encodes a member of the germinal centre kinase
            III (GCK III) subfamily of the sterile 20 superfamily of kinases.
            The encoded enzyme plays a role in serine-threonine liver kinase B1
            (LKB1) signaling pathway to regulate neuronal polarization and
            morphology of the Golgi apparatus. The protein is translocated from
            the Golgi apparatus to the nucleus in response to chemical anoxia
            and plays a role in regulation of cell death. A pseudogene
            associated with this gene is located on chromosome 18. Multiple
            alternatively spliced transcript variants have been observed for
            this gene. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. Variants 1, 4 and 5 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291947.1, BC007852.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..426
                     /product="serine/threonine-protein kinase 25 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase 25; Ste20, yeast
                     homolog; ste20-like kinase; ste20/oxidant stress response
                     kinase 1; sterile 20/oxidant stress-response kinase 1"
                     /calculated_mol_wt=47981
     Region          15..291
                     /region_name="STKc_STK25"
                     /note="Catalytic domain of Serine/Threonine Kinase 25
                     (also called Yeast Sps1/Ste20-related kinase 1); cd06642"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,79,95..98,101..102,105,140,142..145,
                     147,157..158,161,175..178,180,207,216)
                     /site_type="active"
                     /db_xref="CDD:270810"
     Site            order(26..30,34,47,49,66,79,95..98,101..102,105,144..145,
                     147,158)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270810"
     Site            order(29..30,140,142..144,161,175..178,180,207,216)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270810"
     Site            157..180
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270810"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:15037601; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2W1; propagated from
                     UniProtKB/Swiss-Prot (O00506.1)"
     Region          291..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00506.1)"
     CDS             1..426
                     /gene="STK25"
                     /gene_synonym="SOK1; YSK1"
                     /coded_by="NM_006374.5:181..1461"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS2549.1"
                     /db_xref="GeneID:10494"
                     /db_xref="HGNC:HGNC:11404"
                     /db_xref="MIM:602255"
ORIGIN      
        1 mahlrgfanq hsrvdpeelf tkldrigkgs fgevykgidn htkevvaiki idleeaedei
       61 ediqqeitvl sqcdspyitr yfgsylkstk lwiimeylgg gsaldllkpg pleetyiati
      121 lreilkgldy lhserkihrd ikaanvllse qgdvkladfg vagqltdtqi krntfvgtpf
      181 wmapevikqs aydfkadiws lgitaielak geppnsdlhp mrvlflipkn spptlegqhs
      241 kpfkefveac lnkdprfrpt akellkhkfi trytkktsfl telidrykrw kseghgeess
      301 sedsdidgea edgeqgpiwt fpptirpsph sklhkgtalh ssqkpaepvk rqprsqclst
      361 lvrpvfgelk ekhkqsggsv galeelenaf slaeescpgi sdklmvhlve rvqrfshnrn
      421 hltstr
//
LOCUS       NP_001353507             804 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 14 [Homo
            sapiens].
ACCESSION   NP_001353507 XP_016855520
VERSION     NP_001353507.1
DBSOURCE    REFSEQ: accession NM_001366578.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 804)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 804)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 804)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 804)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 804)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 804)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 804)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855520.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.131215.1,
                                           SRR1803616.187280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..804
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 14"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=90326
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <301..630
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..804
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366578.1:405..2819"
                     /note="isoform 14 is encoded by transcript variant 19"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels esedkggkma
      361 aadsvqqrrq yrrqnqqsss dsgsssssed erpkrshvkn gevgrrrrhs psrsaspspr
      421 krqketsprm qmgkrwqspv tksgrrrrsp sppptrrrrs pspappprrr rtptppprrr
      481 tpsppprrrs psprrysppi qrryspsppp krrtaspppp pkrraspspp pkrrvshspp
      541 pkqrsspvtk rrspslsskh rkgsspsrst rearspqpnk rhspsprpra pqtssspppv
      601 rrgassspqr rqspspstrp irrvsrtpep kkikkaasps pqsvrrvsss rsvsgspepa
      661 akkppappsp vqsqspstnw spavpvkkak sptpspsppr nsdqegggkk kkkkkdkkhk
      721 kdkkhkkhkk hkkekavaaa aaaavtpaai aaatttlaqe epvaapepkk eteseaednl
      781 ddlekhlrek alrsmrkaqv spqs
//
LOCUS       NP_001357093             671 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_001357093 XP_016885460
VERSION     NP_001357093.1
DBSOURCE    REFSEQ: accession NM_001370164.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 671)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 671)
  AUTHORS   Alnaas,A.A., Watson-Siriboe,A., Tran,S., Negussie,M.,
            Henderson,J.A., Osterberg,J.R., Chon,N.L., Harrott,B.M., Oviedo,J.,
            Lyakhova,T., Michel,C., Reisdorph,N., Reisdorph,R., Shearn,C.T.,
            Lin,H. and Knight,J.D.
  TITLE     Multivalent lipid targeting by the calcium-independent C2A domain
            of synaptotagmin-like protein 4/granuphilin
  JOURNAL   J Biol Chem 296, 100159 (2021)
   PUBMED   33277360
  REMARK    GeneRIF: Multivalent lipid targeting by the calcium-independent C2A
            domain of synaptotagmin-like protein 4/granuphilin.
REFERENCE   4  (residues 1 to 671)
  AUTHORS   Liu,X.Y., Jiang,W., Ma,D., Ge,L.P., Yang,Y.S., Gou,Z.C., Xu,X.E.,
            Shao,Z.M. and Jiang,Y.Z.
  TITLE     SYTL4 downregulates microtubule stability and confers paclitaxel
            resistance in triple-negative breast cancer
  JOURNAL   Theranostics 10 (24), 10940-10956 (2020)
   PUBMED   33042263
  REMARK    GeneRIF: SYTL4 downregulates microtubule stability and confers
            paclitaxel resistance in triple-negative breast cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 671)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 671)
  AUTHORS   Torii,S., Zhao,S., Yi,Z., Takeuchi,T. and Izumi,T.
  TITLE     Granuphilin modulates the exocytosis of secretory granules through
            interaction with syntaxin 1a
  JOURNAL   Mol Cell Biol 22 (15), 5518-5526 (2002)
   PUBMED   12101244
REFERENCE   7  (residues 1 to 671)
  AUTHORS   Zhao,S., Torii,S., Yokota-Hashimoto,H., Takeuchi,T. and Izumi,T.
  TITLE     Involvement of Rab27b in the regulated secretion of pituitary
            hormones
  JOURNAL   Endocrinology 143 (5), 1817-1824 (2002)
   PUBMED   11956164
REFERENCE   8  (residues 1 to 671)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     The Slp homology domain of synaptotagmin-like proteins 1-4 and
            Slac2 functions as a novel Rab27A binding domain
  JOURNAL   J Biol Chem 277 (11), 9212-9218 (2002)
   PUBMED   11773082
  REMARK    GeneRIF: Synaptotagmin-like protein 4 (Slp4)/granuphilin-a contains
            an N-terminal Slp homology domain (SHD) (PMID: 11327731). The SHD
            of Slp4 specifically and directly binds the GTP-bound form of
            Rab3A, Rab8, and Rab27A.
REFERENCE   9  (residues 1 to 671)
  AUTHORS   Yi,Z., Yokota,H., Torii,S., Aoki,T., Hosaka,M., Zhao,S., Takata,K.,
            Takeuchi,T. and Izumi,T.
  TITLE     The Rab27a/granuphilin complex regulates the exocytosis of
            insulin-containing dense-core granules
  JOURNAL   Mol Cell Biol 22 (6), 1858-1867 (2002)
   PUBMED   11865063
REFERENCE   10 (residues 1 to 671)
  AUTHORS   Araki,W., Ohno,K., Matsunaga,K., Nakamura,H., Sugimoto,C. and
            Shimada,T.
  TITLE     [Two sisters with pseudoidiopathic hypoparathyroidism presenting
            extensive intracranial calcification]
  JOURNAL   Nihon Naika Gakkai Zasshi 78 (1), 81-82 (1989)
   PUBMED   2732579
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390040.9.
            
            On May 2, 2019 this sequence version replaced XP_016885460.1.
            
            Summary: This gene encodes a member of the synaptotagmin like
            protein family. Members of this family are characterized by an
            N-terminal Rab27 binding domain and C-terminal tandem C2 domains.
            The encoded protein binds specific small Rab GTPases and is
            involved in intracellular membrane trafficking. This protein binds
            Rab27 and may be involved in inhibiting dense core vesicle
            exocytosis. Alternate splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Mar
            2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.193360.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..671
                     /product="synaptotagmin-like protein 4 isoform 1"
                     /note="granuphilin-a; exophilin-2"
                     /calculated_mol_wt=75893
     Region          8..121
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          58..107
                     /region_name="FYVE_Slp4"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 4 (Slp4) and similar proteins; cd15764"
                     /db_xref="CDD:277303"
     Region          199..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R0Q1; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          357..481
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96C24.2)"
     Region          496..661
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..671
                     /gene="SYTL4"
                     /gene_synonym="SLP4"
                     /coded_by="NM_001370164.1:265..2280"
                     /note="isoform 1 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS14472.1"
                     /db_xref="GeneID:94121"
                     /db_xref="HGNC:HGNC:15588"
                     /db_xref="MIM:300723"
ORIGIN      
        1 mselldlsfl seeekdlils vlqrdeevrk adekrirrlk nelleikrkg akrgsqhysd
       61 rtcarcqesl grlspktntc rgcnhlvcrd criqesngtw rckvcakeie lkkatgdwfy
      121 dqkvnrfayr tgseiirmsl rhkpavskre tvgqsllhqt qmgdiwpgrk iiqerqkeps
      181 vlfevpklks gksaleaese sldsftadsd stsrrdsldk sglfpewkkm sapksqveke
      241 tqpggqnvvf vdegemifkk ntrkilrpse ytksvidlrp edvvhesgsl gdrsksvpgl
      301 nvdmeeeeee edidhlvklh rqklarssmq sgssmstigs mmsiyseagd fgnifvtgri
      361 afslkyeqqt qslvvhvkec hqlayadeak krsnpyvkty llpdksrqgk rktsikrdti
      421 nplydetlry eipesllaqr tlqfsvwhhg rfgrntflge aeiqmdswkl dkkldhclpl
      481 hgkisaespt glpshkgelv vslkyipask tpvggdrkks kggeggelqv wikeaknlta
      541 akaggtsdsf vkgyllpmrn kaskrktpvm kktlnphynh tfvyngvrle dlqhmclelt
      601 vwdreplasn dflggvrlgv gtgisngevv dwmdstgeev slwqkmrqyp gswaegtlql
      661 rssmakqklg l
//
LOCUS       NP_057616                448 aa            linear   PRI 20-NOV-2025
DEFINITION  inositol polyphosphate 5-phosphatase K isoform 1 [Homo sapiens].
ACCESSION   NP_057616
VERSION     NP_057616.2
DBSOURCE    REFSEQ: accession NM_016532.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Moes,B., Li,H., Molina-Ortiz,P., Radermecker,C., Rosu,A., Vande
            Catsyne,C.A., Sayyed,S.A., Fontela,J., Duque,M., Mostafa,A.,
            Azzi,A., Barata,J.T., Merino,R., Xu,C., Desmet,C.J. and
            Schurmans,S.
  TITLE     INPP5K controls the dynamic structure and signaling of wild-type
            and mutated, leukemia-associated IL-7 receptors
  JOURNAL   Blood 141 (14), 1708-1717 (2023)
   PUBMED   36599086
  REMARK    GeneRIF: INPP5K controls the dynamic structure and signaling of
            wild-type and mutated, leukemia-associated IL-7 receptors.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Sun,J., Harion,R., Naito,T. and Saheki,Y.
  TITLE     INPP5K and Atlastin-1 maintain the nonuniform distribution of
            ER-plasma membrane contacts in neurons
  JOURNAL   Life Sci Alliance 4 (11), e202101092 (2021)
   PUBMED   34556534
  REMARK    GeneRIF: INPP5K and Atlastin-1 maintain the nonuniform distribution
            of ER-plasma membrane contacts in neurons.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Hathazi,D., Cox,D., D'Amico,A., Tasca,G., Charlton,R.,
            Carlier,R.Y., Baumann,J., Kollipara,L., Zahedi,R.P., Feldmann,I.,
            Deleuze,J.F., Torella,A., Cohn,R., Robinson,E., Ricci,F.,
            Jungbluth,H., Fattori,F., Boland,A., O'Connor,E., Horvath,R.,
            Barresi,R., Lochmuller,H., Urtizberea,A., Jacquemont,M.L.,
            Nelson,I., Swan,L., Bonne,G. and Roos,A.
  TITLE     INPP5K and SIL1 associated pathologies with overlapping clinical
            phenotypes converge through dysregulation of PHGDH
  JOURNAL   Brain 144 (8), 2427-2442 (2021)
   PUBMED   33792664
  REMARK    GeneRIF: INPP5K and SIL1 associated pathologies with overlapping
            clinical phenotypes converge through dysregulation of PHGDH.
            Erratum:[Brain. 2024 Aug 1;147(8):e62. doi: 10.1093/brain/awae239.
            PMID: 39023925]
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Gurung,R., Tan,A., Ooms,L.M., McGrath,M.J., Huysmans,R.D.,
            Munday,A.D., Prescott,M., Whisstock,J.C. and Mitchell,C.A.
  TITLE     Identification of a novel domain in two mammalian
            inositol-polyphosphate 5-phosphatases that mediates membrane ruffle
            localization. The inositol 5-phosphatase skip localizes to the
            endoplasmic reticulum and translocates to membrane ruffles
            following epidermal growth factor stimulation
  JOURNAL   J Biol Chem 278 (13), 11376-11385 (2003)
   PUBMED   12536145
  REMARK    GeneRIF: identification of novel domain that mediates membrane
            ruffle localization
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Ijuin,T. and Takenawa,T.
  TITLE     SKIP negatively regulates insulin-induced GLUT4 translocation and
            membrane ruffle formation
  JOURNAL   Mol Cell Biol 23 (4), 1209-1220 (2003)
   PUBMED   12556481
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Ijuin,T., Mochizuki,Y., Fukami,K., Funaki,M., Asano,T. and
            Takenawa,T.
  TITLE     Identification and characterization of a novel inositol
            polyphosphate 5-phosphatase
  JOURNAL   J Biol Chem 275 (15), 10870-10875 (2000)
   PUBMED   10753883
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Drayer,A.L., Pesesse,X., De Smedt,F., Communi,D., Moreau,C. and
            Erneux,C.
  TITLE     The family of inositol and phosphatidylinositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 1001-1005 (1996)
   PUBMED   8968500
  REMARK    Review article
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Mitchell,C.A., Brown,S., Campbell,J.K., Munday,A.D. and Speed,C.J.
  TITLE     Regulation of second messengers by the inositol polyphosphate
            5-phosphatases
  JOURNAL   Biochem Soc Trans 24 (4), 994-1000 (1996)
   PUBMED   8968499
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100748.2, BC004362.1,
            AB036829.1 and BM510617.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 19, 2002 this sequence version replaced NP_057616.1.
            
            Summary: This gene encodes a protein with 5-phosphatase activity
            toward polyphosphate inositol. The protein localizes to the cytosol
            in regions lacking actin stress fibers. It is thought that this
            protein may negatively regulate the actin cytoskeleton.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform of
            this protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB036829.1, SRR3476690.994275.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000421807.7/ ENSP00000413937.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..448
                     /product="inositol polyphosphate 5-phosphatase K isoform
                     1"
                     /EC_number="3.1.3.56"
                     /EC_number="3.1.3.36"
                     /EC_number="3.1.3.86"
                     /note="phosphatidylinositol-4,5-bisphosphate
                     5-phosphatase; phosphatidylinositol-3,4,5-trisphosphate
                     5-phosphatase; skeletal muscle and kidney-enriched
                     inositol phosphatase"
                     /calculated_mol_wt=50959
     Region          14..320
                     /region_name="EEP"
                     /note="Exonuclease-Endonuclease-Phosphatase (EEP) domain
                     superfamily; cl00490"
                     /db_xref="CDD:469791"
     Region          16..318
                     /region_name="Catalytic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Site            order(22,54,149,192,194,269,310..311)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197306"
     Site            order(54,310)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:197306"
     Site            order(149,194,311)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197306"
     Region          318..448
                     /region_name="Required for interaction with GPR78 and
                     PAK1. /evidence=ECO:0000269|PubMed:26940976"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Region          321..448
                     /region_name="Required for ruffle localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BT40.3)"
     Region          331..431
                     /region_name="SKICH"
                     /note="SKICH domain; pfam17751"
                     /db_xref="CDD:465482"
     CDS             1..448
                     /gene="INPP5K"
                     /gene_synonym="MDCCAID; PPS; SKIP"
                     /coded_by="NM_016532.4:114..1460"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11004.1"
                     /db_xref="GeneID:51763"
                     /db_xref="HGNC:HGNC:33882"
                     /db_xref="MIM:607875"
ORIGIN      
        1 mssrklsgpk grrlsihvvt wnvasaappl dlsdllqlnn rnlnldiyvi glqelnsgii
       61 sllsdaafnd swssflmdvl splsfikvsh vrmqgilllv fakyqhlpyi qilstkstpt
      121 glfgywgnkg gvniclklyg yyvsiinchl pphisnnyqr lehfdrilem qncegrdipn
      181 ildhdliiwf gdmnfriedf glhfvresik nrcygglwek dqlsiakkhd pllrefqegr
      241 llfpptykfd rnsndydtse kkrkpawtdr ilwrlkrqpc agpdtpippa shfslslrgy
      301 sshmtygisd hkpvsgtfdl elkplvsapl ivlmpedlwt vendmmvsys stsdfpsspw
      361 dwiglykvgl rdvndyvsya wvgdskvscs dnlnqvyidi snipttedef llcyysnslr
      421 svvgisrpfq ippgslredp lgeaqpqi
//
LOCUS       NP_660150                423 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI alpha-1,4-mannosyltransferase I, catalytic subunit [Homo
            sapiens].
ACCESSION   NP_660150
VERSION     NP_660150.1
DBSOURCE    REFSEQ: accession NM_145167.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Kinoshita,T.
  TITLE     Biosynthesis and biology of mammalian GPI-anchored proteins
  JOURNAL   Open Biol 10 (3), 190290 (2020)
   PUBMED   32156170
  REMARK    Review article
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Eisenhaber,B., Sinha,S., Wong,W.C. and Eisenhaber,F.
  TITLE     Function of a membrane-embedded domain evolutionarily multiplied in
            the GPI lipid anchor pathway proteins PIG-B, PIG-M, PIG-U, PIG-W,
            PIG-V, and PIG-Z
  JOURNAL   Cell Cycle 17 (7), 874-880 (2018)
   PUBMED   29764287
  REMARK    GeneRIF: Function of a membrane-embedded domain evolutionarily
            multiplied in the GPI lipid anchor pathway proteins PIG-B, PIG-M,
            PIG-U, PIG-W, PIG-V, and PIG-Z has been described.
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Costa,J.R., Caputo,V.S., Makarona,K., Layton,D.M., Roberts,I.A.,
            Almeida,A.M. and Karadimitris,A.
  TITLE     Cell-type-specific transcriptional regulation of PIGM underpins the
            divergent hematologic phenotype in inherited GPl deficiency
  JOURNAL   Blood 124 (20), 3151-3154 (2014)
   PUBMED   25293775
  REMARK    GeneRIF: B cells but not red cells are glycosylphosphatidylinositol
            deficient in PIGM-associated inherited glycosylphosphatidylinositol
            deficiency, caused by a core promoter mutation that abrogates Sp1
            binding.
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Freeze,H.H.
  TITLE     Understanding human glycosylation disorders: biochemistry leads the
            charge
  JOURNAL   J Biol Chem 288 (10), 6936-6945 (2013)
   PUBMED   23329837
  REMARK    GeneRIF: Studies indicate that mutations in PGM1 by exome
            sequencing cause hypoglycemia and liver abnormalities.
            Review article
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Almeida,A.M., Murakami,Y., Layton,D.M., Hillmen,P., Sellick,G.S.,
            Maeda,Y., Richards,S., Patterson,S., Kotsianidis,I., Mollica,L.,
            Crawford,D.H., Baker,A., Ferguson,M., Roberts,I., Houlston,R.,
            Kinoshita,T. and Karadimitris,A.
  TITLE     Hypomorphic promoter mutation in PIGM causes inherited
            glycosylphosphatidylinositol deficiency
  JOURNAL   Nat Med 12 (7), 846-851 (2006)
   PUBMED   16767100
  REMARK    GeneRIF: Mutation substantially reduces transcription of PIGM and
            blocks mannosylation of glycosylphosphatidylinositol(GPI), leading
            to partial but severe deficiency of GPI.
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Maeda,Y., Watanabe,R., Harris,C.L., Hong,Y., Ohishi,K.,
            Kinoshita,K. and Kinoshita,T.
  TITLE     PIG-M transfers the first mannose to glycosylphosphatidylinositol
            on the lumenal side of the ER
  JOURNAL   EMBO J 20 (1-2), 250-261 (2001)
   PUBMED   11226175
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX643162.1, BC019865.1 and
            AL513302.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a transmembrane protein that is located
            in the endoplasmic reticulum and is involved in GPI-anchor
            biosynthesis. The glycosylphosphatidylinositol (GPI)-anchor is a
            glycolipid which contains three mannose molecules in its core
            backbone. The GPI-anchor is found on many blood cells and serves to
            anchor proteins to the cell surface. This gene encodes a
            mannosyltransferase, GPI-MT-I, that transfers the first mannose to
            GPI on the lumenal side of the endoplasmic reticulum. [provided by
            RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK074655.1, BC001803.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368090.5/ ENSP00000357069.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.2"
     Protein         1..423
                     /product="GPI alpha-1,4-mannosyltransferase I, catalytic
                     subunit"
                     /EC_number="2.4.1.-"
                     /note="PIG-M mannosyltransferase; GPI mannosyltransferase
                     1; GPI mannosyltransferase I; phosphatidylinositol-glycan
                     biosynthesis class M protein; DPM:GlcN-(acyl-)PI
                     mannosyltransferase; dol-P-Man dependent GPI
                     mannosyltransferase"
                     /calculated_mol_wt=49329
     Site            18..38
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            80..100
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            139..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Region          140..408
                     /region_name="Mannosyl_trans"
                     /note="Mannosyltransferase (PIG-M); pfam05007"
                     /db_xref="CDD:252941"
     Site            170..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            226..246
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            288..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            315..337
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            339..350
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            358..378
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     Site            385..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S5.1)"
     CDS             1..423
                     /gene="PIGM"
                     /gene_synonym="GPI-MT-I"
                     /coded_by="NM_145167.3:252..1523"
                     /db_xref="CCDS:CCDS1192.1"
                     /db_xref="GeneID:93183"
                     /db_xref="HGNC:HGNC:18858"
                     /db_xref="MIM:610273"
ORIGIN      
        1 mgstkhwgew llnlkvapag vfgvaflarv alvfygvfqd rtlhvrytdi dyqvftdaar
       61 fvtegrspyl ratyrytpll gwlltpniyl selfgkflfi scdlltafll yrllllkglg
      121 rrqacgycvf wllnplpmav ssrgnadsiv aslvlmvlyl ikkrlvacaa vfygfavhmk
      181 iypvtyilpi tlhllpdrdn dkslrqfryt fqaclyellk rlcnravllf vavagltffa
      241 lsfgfyyeyg weflehtyfy hltrrdirhn fspyfymlyl taeskwsfsl giaaflpqli
      301 llsavsfayy rdlvfccflh tsifvtfnkv ctsqyflwyl cllplvmplv rmpwkravvl
      361 lmlwfigqam wlapayvlef qgkntflfiw laglffllin csiliqiish ykeeplteri
      421 kyd
//
LOCUS       NP_000669                572 aa            linear   PRI 20-NOV-2025
DEFINITION  alpha-1D adrenergic receptor [Homo sapiens].
ACCESSION   NP_000669
VERSION     NP_000669.1
DBSOURCE    REFSEQ: accession NM_000678.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 572)
  AUTHORS   Wang,J., Ning,D., Xie,D., Chen,X., Cao,X. and Wan,C.
  TITLE     Functional Involvement of ADRA1D in Cutaneous Melanoma Progression
            and Angiogenesis
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (5), 44-50 (2023)
   PUBMED   37571902
  REMARK    GeneRIF: Functional Involvement of ADRA1D in Cutaneous Melanoma
            Progression and Angiogenesis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 572)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 572)
  AUTHORS   Gao,X., Enten,G.A., DeSantis,A.J., Volkman,B.F., Gaponenko,V. and
            Majetschak,M.
  TITLE     Characterization of heteromeric complexes between chemokine (C-X-C
            motif) receptor 4 and alpha1-adrenergic receptors utilizing
            intermolecular bioluminescence resonance energy transfer assays
  JOURNAL   Biochem Biophys Res Commun 528 (2), 368-375 (2020)
   PUBMED   32085899
  REMARK    GeneRIF: Characterization of heteromeric complexes between
            chemokine (C-X-C motif) receptor 4 and alpha1-adrenergic receptors
            utilizing intermolecular bioluminescence resonance energy transfer
            assays.
REFERENCE   4  (residues 1 to 572)
  AUTHORS   Janezic,E.M., Lauer,S.M., Williams,R.G., Chungyoun,M., Lee,K.S.,
            Navaluna,E., Lau,H.T., Ong,S.E. and Hague,C.
  TITLE     N-glycosylation of alpha1D-adrenergic receptor N-terminal domain is
            required for correct trafficking, function, and biogenesis
  JOURNAL   Sci Rep 10 (1), 7209 (2020)
   PUBMED   32350295
  REMARK    GeneRIF: N-glycosylation of alpha1D-adrenergic receptor N-terminal
            domain is required for correct trafficking, function, and
            biogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 572)
  AUTHORS   Carmona-Rosas,G., Hernandez-Espinosa,D.A., Alcantara-Hernandez,R.,
            Alfonzo-Mendez,M.A. and Garcia-Sainz,J.A.
  TITLE     Distinct phosphorylation sites/clusters in the carboxyl terminus
            regulate alpha1D-adrenergic receptor subcellular localization and
            signaling
  JOURNAL   Cell Signal 53, 374-389 (2019)
   PUBMED   30419287
  REMARK    GeneRIF: The roles of adrenoceptor alpha 1D phosphorylation
            sites/clusters were investigated. Carboxyl terminus phosphorylation
            seems to control receptor's membrane localization. Intracellular
            loop 3 mutation caused agonist-induced sustained ERK1/2 activation.
REFERENCE   6  (residues 1 to 572)
  AUTHORS   Esbenshade,T.A., Hirasawa,A., Tsujimoto,G., Tanaka,T., Yano,J.,
            Minneman,K.P. and Murphy,T.J.
  TITLE     Cloning of the human alpha 1d-adrenergic receptor and inducible
            expression of three human subtypes in SK-N-MC cells
  JOURNAL   Mol Pharmacol 47 (5), 977-985 (1995)
   PUBMED   7746284
REFERENCE   7  (residues 1 to 572)
  AUTHORS   Schwinn,D.A., Johnston,G.I., Page,S.O., Mosley,M.J., Wilson,K.H.,
            Worman,N.P., Campbell,S., Fidock,M.D., Furness,L.M.,
            Parry-Smith,D.J. et al.
  TITLE     Cloning and pharmacological characterization of human alpha-1
            adrenergic receptors: sequence corrections and direct comparison
            with other species homologues
  JOURNAL   J Pharmacol Exp Ther 272 (1), 134-142 (1995)
   PUBMED   7815325
REFERENCE   8  (residues 1 to 572)
  AUTHORS   Weinberg,D.H., Trivedi,P., Tan,C.P., Mitra,S., Perkins-Barrow,A.,
            Borkowski,D., Strader,C.D. and Bayne,M.
  TITLE     Cloning, expression and characterization of human alpha adrenergic
            receptors alpha 1a, alpha 1b and alpha 1c
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1296-1304 (1994)
   PUBMED   8024574
REFERENCE   9  (residues 1 to 572)
  AUTHORS   Schwinn,D.A. and Lomasney,J.W.
  TITLE     Pharmacologic characterization of cloned alpha 1-adrenoceptor
            subtypes: selective antagonists suggest the existence of a fourth
            subtype
  JOURNAL   Eur J Pharmacol 227 (4), 433-436 (1992)
   PUBMED   1359975
REFERENCE   10 (residues 1 to 572)
  AUTHORS   Bruno,J.F., Whittaker,J., Song,J.F. and Berelowitz,M.
  TITLE     Molecular cloning and sequencing of a cDNA encoding a human alpha
            1A adrenergic receptor
  JOURNAL   Biochem Biophys Res Commun 179 (3), 1485-1490 (1991)
   PUBMED   1656955
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL357040.14, S70782.1, U03864.1
            and AL121675.36.
            
            Summary: Alpha-1-adrenergic receptors (alpha-1-ARs) are members of
            the G protein-coupled receptor superfamily. They activate mitogenic
            responses and regulate growth and proliferation of many cells.
            There are 3 alpha-1-AR subtypes: alpha-1A, -1B and -1D, all of
            which signal through the Gq/11 family of G-proteins and different
            subtypes show different patterns of activation. This gene encodes
            alpha-1D-adrenergic receptor. Similar to alpha-1B-adrenergic
            receptor gene, this gene comprises 2 exons and a single intron that
            interrupts the coding region. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L31772.1, U03864.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379453.6/ ENSP00000368766.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..572
                     /product="alpha-1D adrenergic receptor"
                     /note="adrenergic, alpha -1D-, receptor; adrenergic,
                     alpha-1A-, receptor; alpha-1D adrenoceptor; alpha-1D
                     adrenoreceptor; alpha-1A adrenergic receptor;
                     alpha-adrenergic receptor 1a"
                     /calculated_mol_wt=60332
     Region          1..77
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Site            65
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25100.2)"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25100.2)"
     Site            96..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          97..413
                     /region_name="7tmA_alpha1D_AR"
                     /note="alpha-1 adrenergic receptors subtype D, member of
                     the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15327"
                     /db_xref="CDD:320450"
     Region          98..124
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320450"
     Region          131..157
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320450"
     Site            134..159
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          169..199
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320450"
     Site            170..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Site            order(172,176..177,180..181,248,255,258..259,262,361,
                     364..365,368,384,388,392)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:320450"
     Region          211..234
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320450"
     Site            214..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          251..280
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320450"
     Site            252..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          341..371
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320450"
     Site            349..373
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          381..406
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320450"
     Site            381..405
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     Region          444..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P25100.2)"
     CDS             1..572
                     /gene="ADRA1D"
                     /gene_synonym="ADRA1; ADRA1A; ADRA1R; ALPHA1; DAR;
                     dJ779E11.2"
                     /coded_by="NM_000678.4:331..2049"
                     /db_xref="CCDS:CCDS13079.1"
                     /db_xref="GeneID:146"
                     /db_xref="HGNC:HGNC:280"
                     /db_xref="MIM:104219"
ORIGIN      
        1 mtfrdllsvs fegprpdssa ggssaggggg saggaapseg pavggvpgga gggggvvgag
       61 sgednrssag epgsagaggd vngtaavggl vvsaqgvgvg vflaafilma vagnllvils
      121 vacnrhlqtv tnyfivnlav adlllsatvl pfsatmevlg fwafgrafcd vwaavdvlcc
      181 tasilslcti svdryvgvrh slkypaimte rkaaailall wvvalvvsvg pllgwkepvp
      241 pderfcgite eagyavfssv csfylpmavi vvmycrvyvv arsttrslea gvkrergkas
      301 evvlrihcrg aatgadgahg mrsakghtfr sslsvrllkf srekkaaktl aivvgvfvlc
      361 wfpfffvlpl gslfpqlkps egvfkvifwl gyfnscvnpl iypcssrefk raflrllrcq
      421 crrrrrrrpl wrvyghhwra stsglrqdca pssgdappga plaltalpdp dpeppgtpem
      481 qapvasrrkp psafrewrll gpfrrpttql rakvsslshk iraggaqrae aacaqrseve
      541 avslgvphev aegatcqaye ladysnlret di
//
LOCUS       NP_079359                508 aa            linear   PRI 20-NOV-2025
DEFINITION  enhancer of mRNA-decapping protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_079359
VERSION     NP_079359.2
DBSOURCE    REFSEQ: accession NM_025083.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 508)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 508)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 508)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 508)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 508)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 508)
  AUTHORS   Rudolph,C., Sigruener,A., Hartmann,A., Orso,E., Bals-Pratsch,M.,
            Gronwald,W., Seifert,B., Kalbitzer,H.R., Verdorfer,I.,
            Luetjens,C.M., Ortmann,O., Bornstein,S.R. and Schmitz,G.
  TITLE     ApoA-I-binding protein (AI-BP) and its homologues hYjeF_N2 and
            hYjeF_N3 comprise the YjeF_N domain protein family in humans with a
            role in spermiogenesis and oogenesis
  JOURNAL   Horm Metab Res 39 (5), 322-335 (2007)
   PUBMED   17533573
REFERENCE   7  (residues 1 to 508)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 508)
  AUTHORS   Benzinger,A., Muster,N., Koch,H.B., Yates,J.R. 3rd and Hermeking,H.
  TITLE     Targeted proteomic analysis of 14-3-3 sigma, a p53 effector
            commonly silenced in cancer
  JOURNAL   Mol Cell Proteomics 4 (6), 785-795 (2005)
   PUBMED   15778465
REFERENCE   9  (residues 1 to 508)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 508)
  AUTHORS   Albrecht,M. and Lengauer,T.
  TITLE     Novel Sm-like proteins with long C-terminal tails and associated
            methyltransferases
  JOURNAL   FEBS Lett 569 (1-3), 18-26 (2004)
   PUBMED   15225602
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091230.23 and BC011534.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 4, 2002 this sequence version replaced NP_079359.1.
            
            Summary: This gene encodes a protein that is important in mRNA
            degradation. The encoded protein is a component of a decapping
            complex that promotes efficient removal of the monomethylguanosine
            (m7G) cap from mRNAs, as part of the 5' to 3' mRNA decay pathway.
            Mutations in this gene have been identified in human patients with
            an autosomal recessive form of intellectual disability. [provided
            by RefSeq, May 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-4 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011534.1, SRR1803614.246983.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315127.9/ ENSP00000320503.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..508
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..508
                     /product="enhancer of mRNA-decapping protein 3 isoform 1"
                     /note="LSM16 homolog (EDC3, S. cerevisiae); enhancer of
                     mRNA-decapping protein 3; yjeF domain-containing protein
                     1; yjeF N-terminal domain-containing protein 2; yjeF
                     domain containing; enhancer of mRNA decapping 3 homolog"
                     /calculated_mol_wt=55947
     Region          1..79
                     /region_name="Required for P-body targeting and
                     interaction with DCP1A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          2..66
                     /region_name="LSm16_N"
                     /note="Like-Sm protein 16, N-terminal domain; cd01737"
                     /db_xref="CDD:212484"
     Site            order(2,5,28,33,56,59..64)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:212484"
     Site            order(10..15,19..30,33..36)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212484"
     Site            order(29,55)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212484"
     Site            51..62
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212484"
     Region          95..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          102..194
                     /region_name="Edc3_linker"
                     /note="Linker region of enhancer of mRNA-decapping protein
                     3; pfam16598"
                     /db_xref="CDD:465188"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96F86.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          191..296
                     /region_name="Required for interaction with DDX6.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96F86.1)"
     Region          198..301
                     /region_name="FDF"
                     /note="FDF domain; pfam09532"
                     /db_xref="CDD:430668"
     Region          302..455
                     /region_name="YjeF_N"
                     /note="YjeF-related protein N-terminus; pfam03853"
                     /db_xref="CDD:427546"
     CDS             1..508
                     /gene="EDC3"
                     /gene_synonym="hYjeF_N2-15q23; LSM16; MRT50; YJDC; YJEFN2"
                     /coded_by="NM_025083.5:164..1690"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10267.1"
                     /db_xref="GeneID:80153"
                     /db_xref="HGNC:HGNC:26114"
                     /db_xref="MIM:609842"
ORIGIN      
        1 matdwlgsiv sincgdslgv yqgrvsavdq vsqtisltrp fhngvkclvp evtfragdit
       61 elkileipgp gdnqhfgdlh qtelgpsgag cqvginqngt gkfvkkpass ssapqnipkr
      121 tdvksqdvav spqqqqcsks yvdrhmesls qsksfrrrhn swssssrhpn qatpkksglk
      181 ngqmknkdde cfgddieeip dtdfdfegnl alfdkaavfe eidtyerrsg trsrgipner
      241 ptryrhdeni lesepivyrr iivphnvske fctdsglvvp sisyelhkkl lsvaekhglt
      301 lerrlemtgv casqmaltll ggpnrlnpkn vhqrptvall cgphvkgaqg iscgrhlanh
      361 dvqvilflpn fvkmlesitn elslfsktqg qqvsslkdlp tspvdlvinc ldcpenvflr
      421 dqpwykaava wanqnrapvl sidppvheve qgidakwsla lglplplgeh agriylcdig
      481 ipqqvfqevg inyhspfgck fviplhsa
//
LOCUS       NP_055257                499 aa            linear   PRI 20-NOV-2025
DEFINITION  sialic acid-binding Ig-like lectin 8 isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_055257
VERSION     NP_055257.2
DBSOURCE    REFSEQ: accession NM_014442.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Li,T.A., Gonzalez-Gil,A., Awol,A.K., Ackerman,S.J., Orsburn,B.C.
            and Schnaar,R.L.
  TITLE     Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the
            human esophagus
  JOURNAL   Glycobiology 34 (10) (2024)
   PUBMED   39173029
  REMARK    GeneRIF: Sialylated keratan sulfates on MUC5B are Siglec-8 ligands
            in the human esophagus.
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Lee,H.S., Gonzalez-Gil,A., Drake,V., Li,T.A., Schnaar,R.L. and
            Kim,J.
  TITLE     Induction of the endogenous sialoglycan ligand for eosinophil death
            receptor Siglec-8 in chronic rhinosinusitis with hyperplastic nasal
            polyposis
  JOURNAL   Glycobiology 31 (8), 1026-1036 (2021)
   PUBMED   33755113
  REMARK    GeneRIF: Induction of the endogenous sialoglycan ligand for
            eosinophil death receptor Siglec-8 in chronic rhinosinusitis with
            hyperplastic nasal polyposis.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Trebo,A., Ditsch,N., Degenhardt,T., Kuhn,C., Rahmeh,M.,
            Schmoeckel,E., Mayr,D., Czogalla,B., Kolben,T., Meister,S.,
            Mahner,S., Jeschke,U. and Hester,A.
  TITLE     First Evidence for a Role of Siglec-8 in Breast Cancer
  JOURNAL   Int J Mol Sci 22 (4), 2000 (2021)
   PUBMED   33670444
  REMARK    GeneRIF: First Evidence for a Role of Siglec-8 in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Sajay-Asbaghi,M., Sadeghi-Shabestrai,M., Monfaredan,A.,
            Seyfizadeh,N., Razavi,A. and Kazemi,T.
  TITLE     Promoter region single nucleotide polymorphism of siglec-8 gene
            associates with susceptibility to allergic asthma
  JOURNAL   Per Med 17 (3), 195-201 (2020)
   PUBMED   32077788
  REMARK    GeneRIF: Promoter region single nucleotide polymorphism of siglec-8
            gene associates with susceptibility to allergic asthma.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Nutku,E., Aizawa,H., Hudson,S.A. and Bochner,B.S.
  TITLE     Ligation of Siglec-8: a selective mechanism for induction of human
            eosinophil apoptosis
  JOURNAL   Blood 101 (12), 5014-5020 (2003)
   PUBMED   12609831
  REMARK    GeneRIF: Sialic acid binding immunoglobulin-like lectin 8
            (Siglec-8) cross-linking with antibodies rapidly generated
            caspase-3-like activity and reduced eosinophil viability through
            induction of apoptosis
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Munday,J., Kerr,S., Ni,J., Cornish,A.L., Zhang,J.Q., Nicoll,G.,
            Floyd,H., Mattei,M.G., Moore,P., Liu,D. and Crocker,P.R.
  TITLE     Identification, characterization and leucocyte expression of
            Siglec-10, a novel human sialic acid-binding receptor
  JOURNAL   Biochem J 355 (Pt 2), 489-497 (2001)
   PUBMED   11284738
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Foussias,G., Yousef,G.M. and Diamandis,E.P.
  TITLE     Molecular characterization of a Siglec8 variant containing
            cytoplasmic tyrosine-based motifs, and mapping of the Siglec8 gene
  JOURNAL   Biochem Biophys Res Commun 278 (3), 775-781 (2000)
   PUBMED   11095983
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Kikly,K.K., Bochner,B.S., Freeman,S.D., Tan,K.B., Gallagher,K.T.,
            D'alessio,K.J., Holmes,S.D., Abrahamson,J.A., Erickson-Miller,C.L.,
            Murdock,P.R., Tachimoto,H., Schleimer,R.P. and White,J.R.
  TITLE     Identification of SAF-2, a novel siglec expressed on eosinophils,
            mast cells, and basophils
  JOURNAL   J Allergy Clin Immunol 105 (6 Pt 1), 1093-1100 (2000)
   PUBMED   10856141
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Floyd,H., Ni,J., Cornish,A.L., Zeng,Z., Liu,D., Carter,K.C.,
            Steel,J. and Crocker,P.R.
  TITLE     Siglec-8. A novel eosinophil-specific member of the immunoglobulin
            superfamily
  JOURNAL   J Biol Chem 275 (2), 861-866 (2000)
   PUBMED   10625619
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA388103.1, BC053319.1 and AF195092.1.
            
            On May 4, 2006 this sequence version replaced NP_055257.1.
            
            Summary: Sialic acid-binding immunoglobulin (Ig)-like lectins, or
            SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1
            transmembrane proteins each having a unique expression pattern,
            mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like
            subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have
            2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor
            tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a
            motif homologous to one identified in signaling lymphocyte
            activation molecule (SLAM; MIM 603492) that mediates an association
            with SLAM-associated protein (SAP; MIM 300490) (summarized by
            Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053319.1, SRR1803611.271576.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159764 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321424.7/ ENSP00000321077.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..499
                     /product="sialic acid-binding Ig-like lectin 8 isoform 1
                     precursor"
                     /note="SAF-2; CDw329; sialoadhesin family member 2"
                     /calculated_mol_wt=52266
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     mat_peptide     17..499
                     /product="Sialic acid-binding Ig-like lectin 8.
                     /id=PRO_0000014948"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
                     /calculated_mol_wt=52266
     Region          27..151
                     /region_name="IgV_CD33"
                     /note="Immunoglobulin Variable (IgV) domain at the
                     N-terminus of CD33 and related Siglecs (sialic
                     acid-binding Ig-like lectins); cd05712"
                     /db_xref="CDD:409377"
     Region          27..51
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          27..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409377"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409377"
     Region          40..51
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409377"
     Region          52..61
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409377"
     Region          70..93
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409377"
     Region          94..127
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          95..99
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409377"
     Region          105..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409377"
     Region          120..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409377"
     Site            order(125,133..134)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409377"
     Site            125
                     /site_type="other"
                     /note="Indispensable role in 6'-sulfo sialyl-Lewis X.
                     /evidence=ECO:0000269|PubMed:27357658; propagated from
                     UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          128..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409377"
     Region          157..242
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          171..175
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          188..192
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          207..211
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          221..226
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          236..239
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            249
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Site            267
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          269..344
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          279..283
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          292..296
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          314..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          325..330
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          340..343
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            364..384
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          410..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          445..450
                     /region_name="ITIM motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          451..470
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          468..473
                     /region_name="SLAM-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     Region          478..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYZ4.2)"
     CDS             1..499
                     /gene="SIGLEC8"
                     /gene_synonym="SAF2; SIGLEC-8; SIGLEC8L"
                     /coded_by="NM_014442.3:68..1567"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS33086.1"
                     /db_xref="GeneID:27181"
                     /db_xref="HGNC:HGNC:10877"
                     /db_xref="MIM:605639"
ORIGIN      
        1 mlllllllpl lwgtkgmegd rqygdgyllq vqelvtvqeg lcvhvpcsfs ypqdgwtdsd
       61 pvhgywfrag drpyqdapva tnnpdrevqa etqgrfqllg diwsndcsls irdarkrdkg
      121 syffrlergs mkwsyksqln yktkqlsvfv talthrpdil ilgtlesghs rnltcsvpwa
      181 ckqgtppmis wigasvsspg pttarssvlt ltpkpqdhgt sltcqvtlpg tgvtttstvr
      241 ldvsyppwnl tmtvfqgdat astalgngss lsvlegqslr lvcavnsnpp arlswtrgsl
      301 tlcpsrssnp gllelprvhv rdegeftcra qnaqgsqhis lslslqnegt gtsrpvsqvt
      361 laavggagat alaflsfcii fiivrscrkk sarpaagvgd tgmedakair gsasqgplte
      421 swkdgnplkk pppavapssg eegelhyatl sfhkvkpqdp qgqeatdsey seikihkret
      481 aetqaclrnh npsskevrg
//
LOCUS       NP_065181                406 aa            linear   PRI 20-NOV-2025
DEFINITION  NIPA-like protein 3 isoform a [Homo sapiens].
ACCESSION   NP_065181
VERSION     NP_065181.1
DBSOURCE    REFSEQ: accession NM_020448.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Grzmil,P., Konietzko,J., Boehm,D., Holter,S.M.,
            Aguilar-Pimentel,A., Javaheri,A., Kalaydjiev,S., Adler,T.,
            Bolle,I., Adham,I., Dixkens,C., Wolf,S., Fuchs,H.,
            Gailus-Durner,V., Wurst,W., Ollert,M., Busch,D.H., Schulz,H., de
            Angelis,M.H. and Burfeind,P.
  TITLE     Targeted disruption of the mouse Npal3 gene leads to deficits in
            behavior, increased IgE levels, and impaired lung function
  JOURNAL   Cytogenet Genome Res 125 (3), 186-200 (2009)
   PUBMED   19738379
  REMARK    GeneRIF: Study demonstrates that both human NPAL3 and mouse NPAL3
            are ubiquitously expressed and encode highly conserved proteins
            Erratum:[Cytogenet Genome Res. 2009;125(4):285. Hoelter, S M
            [corrected to Holter, S M]; Aguilar, A [corrected to
            Aguilar-Pimentel, A]; Gailus-Durne, V [corrected to Gailus-Durner,
            V]; Busch, D [corrected to Busch, D H]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA223169.1, BC063583.1 and AL031431.8.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.184807.1,
                                           SRR1803617.159584.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374399.9/ ENSP00000363520.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..406
                     /product="NIPA-like protein 3 isoform a"
                     /note="NIPA-like protein 3"
                     /calculated_mol_wt=44611
     Region          32..326
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     CDS             1..406
                     /gene="NIPAL3"
                     /gene_synonym="DJ462O23.2; NPAL3; SLC57A5"
                     /coded_by="NM_020448.5:361..1581"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30631.1"
                     /db_xref="GeneID:57185"
                     /db_xref="HGNC:HGNC:25233"
                     /db_xref="MIM:620034"
ORIGIN      
        1 mdgshsaalk lqqlpptsss savseasfsy kenligalla ifghlvvsia lnlqkychir
       61 lagskdpray fktktwwlgl flmllgelgv fasyafapls livplsavsv iasaiigiif
      121 ikekwkpkdf lrryvlsfvg cglavvgtyl lvtfapnshe kmtgenvtrh lvswpfllym
      181 lveiilfcll lyfykeknan nivvilllva llgsmtvvtv kavagmlvls iqgnlqldyp
      241 ifyvmfvcmv atavyqaafl sqasqmydss liasvgyils ttiaitagai fyldfigedv
      301 lhicmfalgc liaflgvfli trnrkkpipf epyismdamp gmqnmhdkgm tvqpelkasf
      361 sygalenndn iseiyapatl pvmqeehgsr sasgvpyrvl ehtkke
//
LOCUS       NP_001353140             883 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 10 [Homo sapiens].
ACCESSION   NP_001353140
VERSION     NP_001353140.1
DBSOURCE    REFSEQ: accession NM_001366211.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 883)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 883)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 883)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 883)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 883)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 883)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 883)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 883)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 883)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 883)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.211204.1,
                                           SRR1803611.123990.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..883
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..883
                     /product="disks large homolog 1 isoform 10"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=98183
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          692..870
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..883
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366211.1:495..3146"
                     /note="isoform 10 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS93453.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 lilitdeygc skggqeeyvl syepvnqqev nytrpviilg pmkdrinddl isefpdkfgs
      721 cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt svqsvrevae
      781 kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar ktferamkle
      841 qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_001165416             278 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform d [Homo sapiens].
ACCESSION   NP_001165416
VERSION     NP_001165416.1
DBSOURCE    REFSEQ: accession NM_001171945.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (4) has multiple differences
            compared to variant 1. These differences result in distinct 5' and
            3' UTRs and cause translation initiation at an alternate, upstream
            start codon, compared to variant 1. The encoded protein (isoform d)
            is shorter than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK309120.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMN02400308
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..278
                     /product="SUN domain-containing protein 1 isoform d"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=30234
     Region          83..>240
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     CDS             1..278
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001171945.2:209..1045"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55078.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mgrispgspg lprtvwfevv nmdfsrlhmy sppqcvpent gytyalsssy ssdaldfete
       61 hkldpvfdsp rmsrrslrla ttactlgdge avgadsgtss avslknraar ttkqrrstnk
      121 safsinhvsr qvtssgvshg gtvslqdavt rrppvldesw ireqttvdhf wgldddgdlk
      181 ggnkaaiqgn gdvgaaaata hngfscsncs mlserkdvlt ahpaapgpvs rvysrdrnqk
      241 cksqsfktqk kvcfpnlifp fcksqclhyl swrlkiip
//
LOCUS       NP_001243070             299 aa            linear   PRI 20-NOV-2025
DEFINITION  fibrinogen silencer-binding protein [Homo sapiens].
ACCESSION   NP_001243070
VERSION     NP_001243070.1
DBSOURCE    REFSEQ: accession NM_001256141.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Grossmann,A., Benlasfer,N., Birth,P., Hegele,A., Wachsmuth,F.,
            Apelt,L. and Stelzl,U.
  TITLE     Phospho-tyrosine dependent protein-protein interaction network
  JOURNAL   Mol Syst Biol 11 (3), 794 (2015)
   PUBMED   25814554
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Lau,K.F., Perkinton,M.S., Rodriguez,L., McLoughlin,D.M. and
            Miller,C.C.
  TITLE     An X11alpha/FSBP complex represses transcription of the GSK3beta
            gene promoter
  JOURNAL   Neuroreport 21 (11), 761-766 (2010)
   PUBMED   20531236
  REMARK    GeneRIF: we show here that through its PDZ domains, X11alpha
            interacts with a novel transcription factor, fibrinogen silencer
            binding protein
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023632.19, AF007866.1 and AK074272.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.158991.1,
                                           SRR1660805.101710.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267778 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000481490.3/ ENSP00000420405.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..299
                     /product="fibrinogen silencer-binding protein"
                     /calculated_mol_wt=34637
     Region          6..85
                     /region_name="Myb_DNA-bind_5"
                     /note="Myb/SANT-like DNA-binding domain; pfam13873"
                     /db_xref="CDD:433544"
     CDS             1..299
                     /gene="FSBP"
                     /coded_by="NM_001256141.2:77..976"
                     /db_xref="CCDS:CCDS59106.1"
                     /db_xref="GeneID:100861412"
                     /db_xref="HGNC:HGNC:43653"
                     /db_xref="MIM:616306"
ORIGIN      
        1 mvgkarssnf tlsekldllk lvkpyvkile ehtnkhsviv eknrcwdiia vnynaigvdr
       61 pprtaqglrt lykrlkeyak qellqqketq sdfksnisep tkkvmemipq issfclvrdr
      121 nhiqsanlde eaqagtsslq vmldhhpvai tvevkqeedi kpppplvlns qqsdtleqre
      181 ehelvhvmer slspslssvd mrmtsspssi prrddffrhe sgehfrsllg ydpqilqmlk
      241 eehqiilenq knfglyvqek rdglkrrqql eeellrakie veklkairlr hdlpeynsl
//
LOCUS       NP_073613                747 aa            linear   PRI 20-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 11 [Homo sapiens].
ACCESSION   NP_073613
VERSION     NP_073613.2
DBSOURCE    REFSEQ: accession NM_022776.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 747)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 747)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   3  (residues 1 to 747)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 747)
  AUTHORS   Peng,H., Yan,Z., Zeng,X., Zhang,S., Jiang,H., Huang,H. and Zhuo,H.
  TITLE     Serum and tissue proteomic signatures of patients with
            hepatocellular carcinoma using 2-D gel electrophoresis
  JOURNAL   Mol Med Rep 20 (2), 1025-1038 (2019)
   PUBMED   31173207
  REMARK    GeneRIF: OSBPL11 is down-regulated and may be a potential indicator
            for hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 747)
  AUTHORS   Zhou,Y., Robciuc,M.R., Wabitsch,M., Juuti,A., Leivonen,M.,
            Ehnholm,C., Yki-Jarvinen,H. and Olkkonen,V.M.
  TITLE     OSBP-related proteins (ORPs) in human adipose depots and cultured
            adipocytes: evidence for impacts on the adipocyte phenotype
  JOURNAL   PLoS One 7 (9), e45352 (2012)
   PUBMED   23028956
  REMARK    GeneRIF: ORP8 overexpression resulted in reduced expression of the
            aP2 mRNA, while down-regulation of adiponectin and aP2 was observed
            in ORP11 silenced cells. ORP8 overexpression or silencing of ORP11
            markedly decreased cellular triglyceride storage.
REFERENCE   6  (residues 1 to 747)
  AUTHORS   Bouchard,L., Faucher,G., Tchernof,A., Deshaies,Y., Marceau,S.,
            Lescelleur,O., Biron,S., Bouchard,C., Perusse,L. and Vohl,M.C.
  TITLE     Association of OSBPL11 gene polymorphisms with cardiovascular
            disease risk factors in obesity
  JOURNAL   Obesity (Silver Spring) 17 (7), 1466-1472 (2009)
   PUBMED   19325544
  REMARK    GeneRIF: The OSBPL11 gene is involved in cholesterol and glucose
            metabolism in obese individuals.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 747)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 747)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 747)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 747)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA722217.1, DA112146.1,
            BX506747.1 and BC065213.1.
            
            On Apr 4, 2002 this sequence version replaced NP_073613.1.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Like most members, the encoded protein contains an N-terminal
            pleckstrin homology domain and a highly conserved C-terminal
            OSBP-like sterol-binding domain. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065213.1, AF392454.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296220.6/ ENSP00000296220.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..747
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.2"
     Protein         1..747
                     /product="oxysterol-binding protein-related protein 11"
                     /note="OSBP-related protein 11; testicular tissue protein
                     Li 132"
                     /calculated_mol_wt=83512
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Region          61..167
                     /region_name="PH_ORP10_ORP11"
                     /note="Human Oxysterol binding protein (OSBP) related
                     proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology
                     (PH) domain; cd13291"
                     /db_xref="CDD:270106"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Region          158..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CI95; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     Region          372..738
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     Region          689..714
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BXB4.2)"
     CDS             1..747
                     /gene="OSBPL11"
                     /gene_synonym="ORP-11; ORP11; OSBP12; TCCCIA00292"
                     /coded_by="NM_022776.5:698..2941"
                     /db_xref="CCDS:CCDS3033.1"
                     /db_xref="GeneID:114885"
                     /db_xref="HGNC:HGNC:16397"
                     /db_xref="MIM:606739"
ORIGIN      
        1 mqggepvstm kvsesegkle gqatavtpnk nsscgggiss ssssrggsak gwqysdhmen
       61 vygylmkytn lvtgwqyrff vlnneaglle yfvneqsrnq kprgtlqlag avispsdeds
      121 htftvnaasg eqyklratda kerqhwvsrl qictqhhtea igknnpplks rsfslasssn
      181 spisqrrpsq naisffnvgh sklqslskrt nlppdhlvev remmshaegq qrdlirriec
      241 lptsghlssl dqdllmlkat smatmnclnd cfhilqlqha shqkgslpsg ttiewlepki
      301 slsnhyknga dqpfatdqsk pvavpeeqpv aesgllarep eeinaddeie dtcdhkeddl
      361 gaveeqrsvi lhllsqlklg mdltrvvlpt filekrslle myadfmshpd lfiaitngat
      421 aedrmirfve yyltsfhegr kgaiakkpyn piigetfhcs wkmpksevas svfsssstqg
      481 vtnhaplsge sltqvgsdcy tvrfvaeqvs hhppvsgfya ecterkmcvn ahvwtkskfl
      541 gmsigvtmvg egilsllehg eeytfslpca yarsiltvpw velggkvsvn caktgysasi
      601 tfhtkpfygg klhrvtaevk hnitntvvcr vqgewnsvle ftysngetky vdltklavtk
      661 krvrplekqd pfesrrlwkn vtdslresei dkatehkhtl eerqrteerh rtetgtpwkt
      721 kyfikegdgw vyhkplwkii pttqpae
//
LOCUS       NP_001335048             564 aa            linear   PRI 20-NOV-2025
DEFINITION  tripartite motif-containing protein 16 isoform a [Homo sapiens].
ACCESSION   NP_001335048
VERSION     NP_001335048.1
DBSOURCE    REFSEQ: accession NM_001348119.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 564)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 564)
  AUTHORS   Guo,D., Zhang,M., Wei,T., Zhang,X., Shi,X., Tang,H., Ding,M.,
            Li,J., Zhang,S. and Guo,W.
  TITLE     NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16
  JOURNAL   Cell Mol Life Sci 81 (1), 167 (2024)
   PUBMED   38581570
  REMARK    GeneRIF: NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 564)
  AUTHORS   Li,S., Wang,J., Chen,H., Hou,J., Shen,T., Li,J., Zhou,B., Zhang,B.,
            Liu,H. and Jiang,D.K.
  TITLE     TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin pathway
  JOURNAL   Mol Carcinog 62 (11), 1686-1699 (2023)
   PUBMED   37477507
  REMARK    GeneRIF: TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin
            pathway.
REFERENCE   4  (residues 1 to 564)
  AUTHORS   Roshanazadeh,M.R., Adelipour,M., Sanaei,A., Chenane,H. and
            Rashidi,M.
  TITLE     TRIM3 and TRIM16 as potential tumor suppressors in breast cancer
            patients
  JOURNAL   BMC Res Notes 15 (1), 312 (2022)
   PUBMED   36180926
  REMARK    GeneRIF: TRIM3 and TRIM16 as potential tumor suppressors in breast
            cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 564)
  AUTHORS   Wang,Y., Wu,Y. and Xie,S.
  TITLE     CircPTK2 inhibits cell cisplatin (CDDP) resistance by targeting
            miR-942/TRIM16 axis in non-small cell lung cancer (NSCLC)
  JOURNAL   Bioengineered 13 (2), 3651-3664 (2022)
   PUBMED   35230201
  REMARK    GeneRIF: CircPTK2 inhibits cell cisplatin (CDDP) resistance by
            targeting miR-942/TRIM16 axis in non-small cell lung cancer
            (NSCLC).
REFERENCE   6  (residues 1 to 564)
  AUTHORS   Gwinn,M.R., Whipkey,D.L., Tennant,L.B. and Weston,A.
  TITLE     Differential gene expression in normal human mammary epithelial
            cells treated with malathion monitored by DNA microarrays
  JOURNAL   Environ Health Perspect 113 (8), 1046-1051 (2005)
   PUBMED   16079077
REFERENCE   7  (residues 1 to 564)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 564)
  AUTHORS   Beer,H.D., Munding,C., Dubois,N., Mamie,C., Hohl,D. and Werner,S.
  TITLE     The estrogen-responsive B box protein: a novel regulator of
            keratinocyte differentiation
  JOURNAL   J Biol Chem 277 (23), 20740-20749 (2002)
   PUBMED   11919186
  REMARK    GeneRIF: role in regulating keratinocyte differentiation
REFERENCE   9  (residues 1 to 564)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 564)
  AUTHORS   Liu,H.L., Golder-Novoselsky,E., Seto,M.H., Webster,L., McClary,J.
            and Zajchowski,D.A.
  TITLE     The novel estrogen-responsive B-box protein (EBBP) gene is
            tamoxifen-regulated in cells expressing an estrogen receptor
            DNA-binding domain mutant
  JOURNAL   Mol Endocrinol 12 (11), 1733-1748 (1998)
   PUBMED   9817599
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005324.1.
            
            Summary: The protein encoded by this gene is a tripartite motif
            (TRIM) family member that contains two B box domains and a
            coiled-coiled region that are characteristic of the B box zinc
            finger protein family. While it lacks a RING domain found in other
            TRIM proteins, the encoded protein can homodimerize or
            heterodimerize with other TRIM proteins and has E3 ubiquitin ligase
            activity. This gene is also a tumor suppressor and is involved in
            secretory autophagy. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a). Variants 1, 2, and
            3 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2402253.1,
                                           SRR11853559.13436.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649191.2/ ENSP00000497185.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..564
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..564
                     /product="tripartite motif-containing protein 16 isoform
                     a"
                     /EC_number="2.3.2.27"
                     /note="estrogen-responsive B box protein; tripartite
                     motif-containing protein 16; E3 ubiquitin-protein ligase
                     TRIM16"
                     /calculated_mol_wt=63824
     Region          1..69
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95361.3)"
     Region          75..122
                     /region_name="Bbox1_TRIM16"
                     /note="B-box-type 1 zinc finger found in tripartite
                     motif-containing protein 16 (TRIM16) and similar proteins;
                     cd19839"
                     /db_xref="CDD:380897"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27693506; propagated from
                     UniProtKB/Swiss-Prot (O95361.3)"
     Region          129..173
                     /region_name="Bbox_SF"
                     /note="B-box-type zinc finger superfamily; cl00034"
                     /db_xref="CDD:469587"
     Region          <164..>283
                     /region_name="CusB_dom_1"
                     /note="Cation efflux system protein CusB domain 1;
                     cl46872"
                     /db_xref="CDD:481212"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:27693506; propagated from
                     UniProtKB/Swiss-Prot (O95361.3)"
     Region          365..546
                     /region_name="SPRY_PRY_TRIM16"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 16 (TRIM16); cd12890"
                     /db_xref="CDD:293948"
     CDS             1..564
                     /gene="TRIM16"
                     /gene_synonym="EBBP"
                     /coded_by="NM_001348119.1:1015..2709"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11171.1"
                     /db_xref="GeneID:10626"
                     /db_xref="HGNC:HGNC:17241"
                     /db_xref="MIM:609505"
ORIGIN      
        1 maeldlmapg plprataqpp aplspdsgsp spdsgsaspv eeedvgssek lgreteeqds
       61 dsaeqgdpag egkevlcdfc lddtrrvkav kscltcmvny ceehlqphqv niklqshllt
      121 epvkdhnwry cpahhsplsa fccpdqqcic qdccqehsgh tivsldaarr dkeaelqctq
      181 ldlerklkln enaisrlqan qksvlvsvse vkavaemqfg ellaavrkaq anvmlfleek
      241 eqaalsqang ikahleyrsa emekskqele rmaaisntvq fleeyckfkn teditfpsvy
      301 vglkdklsgi rkvitestvh liqllenykk klqefskeee ydirtqvsav vqrkywtskp
      361 epstreqflq yayditfdpd tahkylrlqe enrkvtnttp wehpypdlps rflhwrqvls
      421 qqslylhryy feveifgagt yvgltckgid rkgeernsci sgnnfswslq wngkeftawy
      481 sdmetplkag pfrrlgvyid fpggilsfyg veydtmtlvh kfackfsepv yaafwlskke
      541 nairivdlge epekpapslv gtap
//
LOCUS       NP_001285                669 aa            linear   PRI 20-NOV-2025
DEFINITION  putative lipid scramblase CLPTM1 isoform 2 [Homo sapiens].
ACCESSION   NP_001285
VERSION     NP_001285.1
DBSOURCE    REFSEQ: accession NM_001294.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 669)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 669)
  AUTHORS   Liu,N., Li,J., Gao,K., Perszyk,R.E., Zhang,J., Wang,J., Wu,Y.,
            Jenkins,A., Yuan,H., Traynelis,S.F. and Jiang,Y.
  TITLE     De novo CLPTM1 variants with reduced GABAA R current response in
            patients with epilepsy
  JOURNAL   Epilepsia 64 (11), 2968-2981 (2023)
   PUBMED   37577761
  REMARK    GeneRIF: De novo CLPTM1 variants with reduced GABAA R current
            response in patients with epilepsy.
REFERENCE   3  (residues 1 to 669)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 669)
  AUTHORS   Christodoulou,E., Visser,M., Potjer,T.P., van der Stoep,N.,
            Rodriguez-Girondo,M., van Doorn,R. and Gruis,N.
  TITLE     Assessing a single SNP located at TERT/CLPTM1L multi-cancer risk
            region as a genetic modifier for risk of pancreatic cancer and
            melanoma in Dutch CDKN2A mutation carriers
  JOURNAL   Fam Cancer 18 (4), 439-444 (2019)
   PUBMED   31203567
  REMARK    GeneRIF: a single SNP located at TERT/CLPTM1L multi-cancer risk
            region as a genetic modifier for risk of pancreatic cancer and
            melanoma in Dutch CDKN2A mutation carriers
REFERENCE   5  (residues 1 to 669)
  AUTHORS   Hung,R.J., Spitz,M.R., Houlston,R.S., Schwartz,A.G., Field,J.K.,
            Ying,J., Li,Y., Han,Y., Ji,X., Chen,W., Wu,X., Gorlov,I.P., Na,J.,
            de Andrade,M., Liu,G., Brhane,Y., Diao,N., Wenzlaff,A.,
            Davies,M.P.A., Liloglou,T., Timofeeva,M., Muley,T., Rennert,H.,
            Saliba,W., Ryan,B.M., Bowman,E., Barros-Dios,J.M., Perez-Rios,M.,
            Morgenstern,H., Zienolddiny,S., Skaug,V., Ugolini,D., Bonassi,S.,
            van der Heijden,E.H.F.M., Tardon,A., Bojesen,S.E., Landi,M.T.,
            Johansson,M., Bickeboller,H., Arnold,S., Le Marchand,L.,
            Melander,O., Andrew,A., Grankvist,K., Caporaso,N., Teare,M.D.,
            Schabath,M.B., Aldrich,M.C., Kiemeney,L.A., Wichmann,H.E.,
            Lazarus,P., Mayordomo,J., Neri,M., Haugen,A., Zhang,Z.F.,
            Ruano-Ravina,A., Brenner,H., Harris,C.C., Orlow,I., Rennert,G.,
            Risch,A., Brennan,P., Christiani,D.C., Amos,C.I., Yang,P. and
            Gorlova,O.Y.
  TITLE     Lung Cancer Risk in Never-Smokers of European Descent is Associated
            With Genetic Variation in the 5p15.33 TERT-CLPTM1Ll Region
  JOURNAL   J Thorac Oncol 14 (8), 1360-1369 (2019)
   PUBMED   31009812
  REMARK    GeneRIF: Authors detected three genome-wide statistically
            significant single nucleotide polymorphisms mapped to Chromosome 5
            CLPTM1L-TERT region.
REFERENCE   6  (residues 1 to 669)
  AUTHORS   Ichikawa,E., Watanabe,A., Nakano,Y., Akita,S., Hirano,A.,
            Kinoshita,A., Kondo,S., Kishino,T., Uchiyama,T., Niikawa,N. and
            Yoshiura,K.I.
  TITLE     PAX9 and TGFB3 are linked to susceptibility to nonsyndromic cleft
            lip with or without cleft palate in the Japanese: population-based
            and family-based candidate gene analyses
  JOURNAL   J Hum Genet 51 (1), 38-46 (2006)
   PUBMED   16247549
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 669)
  AUTHORS   Turhani,D., Item,C.B., Watzinger,E., Sinko,K., Watzinger,F.,
            Lauer,G. and Ewers,R.
  TITLE     Mutation analysis of CLPTM 1 and PVRL 1 genes in patients with
            non-syndromic clefts of lip, alveolus and palate
  JOURNAL   J Craniomaxillofac Surg 33 (5), 301-306 (2005)
   PUBMED   16122939
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 669)
  AUTHORS   Rossi,M.R., Hawthorn,L., Platt,J., Burkhardt,T., Cowell,J.K. and
            Ionov,Y.
  TITLE     Identification of inactivating mutations in the JAK1, SYNJ2, and
            CLPTM1 genes in prostate cancer cells using inhibition of
            nonsense-mediated decay and microarray analysis
  JOURNAL   Cancer Genet Cytogenet 161 (2), 97-103 (2005)
   PUBMED   16102578
  REMARK    GeneRIF: Identification of inactivating mutations in the JAK1,
            SYNJ2, and CLPTM1 genes in prostate cancer cells
REFERENCE   9  (residues 1 to 669)
  AUTHORS   Yoshiura,K., Machida,J., Daack-Hirsch,S., Patil,S.R.,
            Ashworth,L.K., Hecht,J.T. and Murray,J.C.
  TITLE     Characterization of a novel gene disrupted by a balanced
            chromosomal translocation t(2;19)(q11.2;q13.3) in a family with
            cleft lip and palate
  JOURNAL   Genomics 54 (2), 231-240 (1998)
   PUBMED   9828125
REFERENCE   10 (residues 1 to 669)
  AUTHORS   Takeuchi,T., Kuro-o,M., Miyazawa,H., Ohtsuki,Y. and Yamamoto,H.
  TITLE     Transgenic expression of a novel thymic epithelial cell antigen
            stimulates abberant development of thymocytes
  JOURNAL   J Immunol 159 (2), 726-733 (1997)
   PUBMED   9218588
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB033341.1, BI916245.1, AK074935.1, BC012359.1, BQ574654.1 and
            BM676309.1.
            
            Transcript Variant: This variant (2) represents the longest
            transcript and encodes the longest isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF037339.1, AK075262.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337392.10/ ENSP00000336994.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..669
                     /product="putative lipid scramblase CLPTM1 isoform 2"
                     /note="cleft lip and palate transmembrane protein 1; cleft
                     lip and palate associated transmembrane protein 1; CLPTM1,
                     transmembrane protein; putative lipid scramblase CLPTM1"
                     /calculated_mol_wt=75966
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:25489052,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            28
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Region          57..497
                     /region_name="CLPTM1"
                     /note="Cleft lip and palate transmembrane protein 1
                     (CLPTM1); pfam05602"
                     /db_xref="CDD:461689"
     Site            119
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16263699,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            355..375
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            391..411
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            413
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            503..523
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O96005.1)"
     Region          614..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O96005.1)"
     CDS             1..669
                     /gene="CLPTM1"
                     /coded_by="NM_001294.4:17..2026"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12651.1"
                     /db_xref="GeneID:1209"
                     /db_xref="HGNC:HGNC:2087"
                     /db_xref="MIM:604783"
ORIGIN      
        1 maaaqeadga rsavvaaggg ssgqvtsngs igrdppaetq pqnppaqpap nawqvikgvl
       61 frifiiwais swfrrgpapq dqagpggapr vasrnlfpkd tlmnlhvyis ehehftdfna
      121 tsalfweqhd lvygdwtsge nsdgcyehfa eldipqsvqq ngsiyihvyf tksgfhpdpr
      181 qkalyrrlat vhmsrminky krrrfqktkn lltgeteadp emikraedyg pvevishwhp
      241 nitinivddh tpwvkgsvpp pldqyvkfda vsgdyypiiy fndywnlqkd yypineslas
      301 lplrvsfcpl slwrwqlyaa qstkspwnfl gdelyeqsde eqdsvkvall etnpyllalt
      361 iivsivhsvf eflafkndiq fwnsrqsleg lsvrsvffgv fqsfvvllyi ldnetnfvvq
      421 vsvfigvlid lwkitkvmdv rldrehrvag ifprlsfkdk styiesstkv yddmafryls
      481 wilfpllgcy avysllyleh kgwyswvlsm lygflltfgf itmtpqlfin yklksvahlp
      541 wrmltykaln tfiddlfafv ikmpvmyrig clrddvvffi ylyqrwiyrv dptrvnefgm
      601 sgedptaaap vaevptaaga ltptpapttt tatreeasts lptkptqgas sasepqeapp
      661 kpaedkkkd
//
LOCUS       NP_002349                205 aa            linear   PRI 20-NOV-2025
DEFINITION  mitotic spindle assembly checkpoint protein MAD2A [Homo sapiens].
ACCESSION   NP_002349
VERSION     NP_002349.1
DBSOURCE    REFSEQ: accession NM_002358.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Makinoya,M., Miyatani,K., Matsumi,Y., Sakano,Y., Shimizu,S.,
            Shishido,Y., Hanaki,T., Kihara,K., Matsunaga,T., Yamamoto,M.,
            Tokuyasu,N., Takano,S., Sakamoto,T., Hasegawa,T., Saito,H.,
            Nakayama,Y., Osaki,M., Okada,F. and Fujiwara,Y.
  TITLE     Exosomal miR-493 suppresses MAD2L1 and induces chemoresistance to
            intraperitoneal paclitaxel therapy in gastric cancer patients with
            peritoneal metastasis
  JOURNAL   Sci Rep 14 (1), 10075 (2024)
   PUBMED   38698201
  REMARK    GeneRIF: Exosomal miR-493 suppresses MAD2L1 and induces
            chemoresistance to intraperitoneal paclitaxel therapy in gastric
            cancer patients with peritoneal metastasis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Park,S.E., Chung,K.S., Heo,S.W., Kim,S.Y., Lee,J.H., Hassan,A.H.E.,
            Lee,Y.S., Lee,J.Y. and Lee,K.T.
  TITLE     Therapeutic role of 2-stearoxyphenethyl phosphocholine targeting
            microtubule dynamics and Wnt/beta-catenin/EMT signaling in human
            colorectal cancer cells
  JOURNAL   Life Sci 334, 122227 (2023)
   PUBMED   37926298
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Jiang,W., Yang,X., Shi,K., Zhang,Y., Shi,X., Wang,J., Wang,Y.,
            Chenyan,A., Shan,J., Wang,Y., Chang,J., Chen,R., Zhou,T., Zhu,Y.,
            Yu,Y., Li,C. and Li,X.
  TITLE     MAD2 activates IGF1R/PI3K/AKT pathway and promotes
            cholangiocarcinoma progression by interfering USP44/LIMA1 complex
  JOURNAL   Oncogene 42 (45), 3344-3357 (2023)
   PUBMED   37752233
  REMARK    GeneRIF: MAD2 activates IGF1R/PI3K/AKT pathway and promotes
            cholangiocarcinoma progression by interfering USP44/LIMA1 complex.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Krishnan,R., Goodman,B., Jin,D.Y., Jeang,K.T., Collins,C.,
            Stetten,G. and Spencer,F.
  TITLE     Map location and gene structure of the Homo sapiens mitotic arrest
            deficient 2 (MAD2L1) gene at 4q27
  JOURNAL   Genomics 49 (3), 475-478 (1998)
   PUBMED   9615237
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Jin,D.Y., Spencer,F. and Jeang,K.T.
  TITLE     Human T cell leukemia virus type 1 oncoprotein Tax targets the
            human mitotic checkpoint protein MAD1
  JOURNAL   Cell 93 (1), 81-91 (1998)
   PUBMED   9546394
REFERENCE   8  (residues 1 to 205)
  AUTHORS   O'Neill,T.J., Zhu,Y. and Gustafson,T.A.
  TITLE     Interaction of MAD2 with the carboxyl terminus of the insulin
            receptor but not with the IGFIR. Evidence for release from the
            insulin receptor after activation
  JOURNAL   J Biol Chem 272 (15), 10035-10040 (1997)
   PUBMED   9092546
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Xu,L., Deng,H.X., Yang,Y., Xia,J.H., Hung,W.Y. and Siddque,T.
  TITLE     Assignment of mitotic arrest deficient protein 2 (MAD2L1) to human
            chromosome band 5q23.3 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 78 (1), 63-64 (1997)
   PUBMED   9345911
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Li,Y. and Benezra,R.
  TITLE     Identification of a human mitotic checkpoint gene: hsMAD2
  JOURNAL   Science 274 (5285), 246-248 (1996)
   PUBMED   8824189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA443733.1, AK313827.1,
            AK223433.1, BC000356.2 and AC097173.1.
            
            Summary: MAD2L1 is a component of the mitotic spindle assembly
            checkpoint that prevents the onset of anaphase until all
            chromosomes are properly aligned at the metaphase plate.  MAD2L1 is
            related to the MAD2L2 gene located on chromosome 1.  A MAD2
            pseudogene has been mapped to chromosome 14. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1576249.1,
                                           SRR14038196.1848721.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296509.11/ ENSP00000296509.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q27"
     Protein         1..205
                     /product="mitotic spindle assembly checkpoint protein
                     MAD2A"
                     /note="mitotic arrest deficient, yeast, homolog-like 1;
                     MAD2 (mitotic arrest deficient, yeast, homolog)-like 1;
                     MAD2-like protein 1; mitotic arrest deficient 2-like
                     protein 1; MAD2 mitotic arrest deficient-like 1"
                     /calculated_mol_wt=23379
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.12;
                     propagated from UniProtKB/Swiss-Prot (Q13257.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     Region          16..191
                     /region_name="HORMA"
                     /note="HORMA domain; pfam02301"
                     /db_xref="CDD:460526"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12574116; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12574116; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     Region          195..205
                     /region_name="Required for assuming the closed
                     conformation and for interaction with CDC20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13257.1)"
     Site            195
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:12574116,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13257.1)"
     CDS             1..205
                     /gene="MAD2L1"
                     /gene_synonym="HSMAD2; MAD2"
                     /coded_by="NM_002358.4:115..732"
                     /db_xref="CCDS:CCDS3715.1"
                     /db_xref="GeneID:4085"
                     /db_xref="HGNC:HGNC:6763"
                     /db_xref="MIM:601467"
ORIGIN      
        1 malqlsreqg itlrgsaeiv aeffsfgins ilyqrgiyps etftrvqkyg ltllvttdle
       61 likylnnvve qlkdwlykcs vqklvvvisn iesgevlerw qfdiecdkta kddsapreks
      121 qkaiqdeirs virqitatvt flpllevscs fdlliytdkd lvvpekwees gpqfitnsee
      181 vrlrsfttti hkvnsmvayk ipvnd
//
LOCUS       NP_001269256             449 aa            linear   PRI 20-NOV-2025
DEFINITION  pescadillo homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001269256
VERSION     NP_001269256.1
DBSOURCE    REFSEQ: accession NM_001282327.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Zhou,J., Lu,Y., Lin,Y., Li,C., Liu,J., Jiang,Z. and Chen,K.
  TITLE     Overexpression of hepatic pescadillo 1 in obesity induces lipid
            dysregulation by inhibiting autophagy
  JOURNAL   Transl Res 258, 1-15 (2023)
   PUBMED   36775058
  REMARK    GeneRIF: Overexpression of hepatic pescadillo 1 in obesity induces
            lipid dysregulation by inhibiting autophagy.
REFERENCE   3  (residues 1 to 449)
  AUTHORS   He,Y., Xiang,J., Li,Y., Huang,W., Gu,F., Wang,Y. and Chen,R.
  TITLE     PES1 is a biomarker of head and neck squamous cell carcinoma and is
            associated with the tumor microenvironment
  JOURNAL   Cancer Med 12 (11), 12622-12638 (2023)
   PUBMED   37076985
  REMARK    GeneRIF: PES1 is a biomarker of head and neck squamous cell
            carcinoma and is associated with the tumor microenvironment.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Li,D., Yao,C., Ding,Z., Liu,P., Chen,X., Liu,W., Yi,F., Jiang,C.,
            Li,H., Liu,Y. and Wu,J.
  TITLE     Pescadillo ribosomal biogenesis factor 1 reduction suppresses
            tumour growth and renders chemosensitivity of head and neck
            squamous cell carcinoma
  JOURNAL   Cancer Med 12 (5), 5703-5717 (2023)
   PUBMED   36217758
  REMARK    GeneRIF: Pescadillo ribosomal biogenesis factor 1 reduction
            suppresses tumour growth and renders chemosensitivity of head and
            neck squamous cell carcinoma.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Li,J., Yu,L., Zhang,H., Wu,J., Yuan,J., Li,X. and Li,M.
  TITLE     Down-regulation of pescadillo inhibits proliferation and
            tumorigenicity of breast cancer cells
  JOURNAL   Cancer Sci 100 (12), 2255-2260 (2009)
   PUBMED   19764998
  REMARK    GeneRIF: pescadillo might play a role in promoting the
            proliferation and carcinogenesis of human breast cancer, and
            thereby might be a potential target for human breast cancer
            treatment.
            Erratum:[Cancer Sci. 2021 Nov;112(11):4812. doi: 10.1111/cas.15148.
            PMID: 34766426]
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Oeffinger,M., Leung,A., Lamond,A. and Tollervey,D.
  TITLE     Yeast Pescadillo is required for multiple activities during 60S
            ribosomal subunit synthesis
  JOURNAL   RNA 8 (5), 626-636 (2002)
   PUBMED   12022229
  REMARK    Erratum:[RNA 2002 Jun;8(6):851. Lueng Anthony [corrected to Leung
            Anthony]]
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Suzuki,Y., Tsunoda,T., Sese,J., Taira,H., Mizushima-Sugano,J.,
            Hata,H., Ota,T., Isogai,T., Tanaka,T., Nakamura,Y., Suyama,A.,
            Sakaki,Y., Morishita,S., Okubo,K. and Sugano,S.
  TITLE     Identification and characterization of the potential promoter
            regions of 1031 kinds of human genes
  JOURNAL   Genome Res 11 (5), 677-684 (2001)
   PUBMED   11337467
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Kinoshita,Y., Jarell,A.D., Flaman,J.M., Foltz,G., Schuster,J.,
            Sopher,B.L., Irvin,D.K., Kanning,K., Kornblum,H.I., Nelson,P.S.,
            Hieter,P. and Morrison,R.S.
  TITLE     Pescadillo, a novel cell cycle regulatory protein abnormally
            expressed in malignant cells
  JOURNAL   J Biol Chem 276 (9), 6656-6665 (2001)
   PUBMED   11071894
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Allende,M.L., Amsterdam,A., Becker,T., Kawakami,K., Gaiano,N. and
            Hopkins,N.
  TITLE     Insertional mutagenesis in zebrafish identifies two novel genes,
            pescadillo and dead eye, essential for embryonic development
  JOURNAL   Genes Dev 10 (24), 3141-3155 (1996)
   PUBMED   8985183
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK127185.1 and BQ576244.1.
            
            Summary: This gene encodes a nuclear protein that contains a breast
            cancer associated gene 1 (BRCA1) C-terminal interaction domain. The
            encoded protein interacts with BOP1 and WDR12 to form the PeBoW
            complex, which plays a critical role in cell proliferation via
            pre-rRNA processing and 60S ribosomal subunit maturation.
            Expression of this gene may play an important role in breast cancer
            proliferation and tumorigenicity. Alternatively spliced transcript
            variants encoding multiple isoforms have been observed for this
            gene. Pseudogenes of this gene are located on the long arm of
            chromosome 4 and the short arm of chromosome 9. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) represents use of an alternate
            promoter and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG, and the resulting isoform (3) has a
            shorter N-terminus compared to isoform 1. Variants 2 and 4 encode
            the same protein (isoform 3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..449
                     /product="pescadillo homolog isoform 3"
                     /note="pescadillo homolog 1, containing BRCT domain"
                     /calculated_mol_wt=51333
     Region          <1..445
                     /region_name="NOP7"
                     /note="Protein required for biogenesis of the 60S
                     ribosomal subunit [Translation, ribosomal structure and
                     biogenesis]; COG5163"
                     /db_xref="CDD:227492"
     CDS             1..449
                     /gene="PES1"
                     /gene_synonym="NOP7; PES"
                     /coded_by="NM_001282327.1:923..2272"
                     /note="isoform 3 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74842.1"
                     /db_xref="GeneID:23481"
                     /db_xref="HGNC:HGNC:8848"
                     /db_xref="MIM:605819"
ORIGIN      
        1 mcflfstfpr tgkchvqtiq lcrrltvefm hyiiaaralr kvflsikgiy yqaevlgqpi
       61 vwitpyafsh dhptdvdyrv matftefytt llgfvnfrly qllnlhyppk legqaqaeak
      121 agegtyalds escmeklaal saslarvvvp ateeeaevde fptdgemsaq eedrrkelea
      181 qekhkklfeg lkfflnrevp realafiirs fggevswdks lcigatydvt dsrithqivd
      241 rpgqqtsvig rcyvqpqwvf dsvnarlllp vaeyfsgvql pphlspfvte kegdyvppek
      301 lkllalqrge dpgnlnesee eeeeddnneg dgdeegenee eeedaeagse keeearlaal
      361 eeqrmegkkp rvmagtlkle dkqrlaqeee seakrlaimm mkkrekylyq kimfgkrrki
      421 reanklaekr kahdeavrse kkakkarpe
//
LOCUS       NP_005334                189 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase HRas isoform 1 [Homo sapiens].
ACCESSION   NP_005334
VERSION     NP_005334.1
DBSOURCE    REFSEQ: accession NM_005343.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Ling,C., Liu,S.S., Wang,Y.Y., Huo,G.T., Yang,Y.W., Xu,N., Wang,H.,
            Wu,Y., Miao,Y.F., Fu,R., Zhao,Y.W. and Fan,C.F.
  TITLE     Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice
  JOURNAL   Zool Res 45 (3), 551-566 (2024)
   PUBMED   38757223
  REMARK    GeneRIF: Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice.
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Devi,P., Dwivedi,R., Sankar,R., Jain,A., Gupta,S. and Gupta,S.
  TITLE     Unraveling the Genetic Web: H-Ras Expression and Mutation in Oral
            Squamous Cell Carcinoma-A Systematic Review
  JOURNAL   Head Neck Pathol 18 (1), 21 (2024)
   PUBMED   38502412
  REMARK    GeneRIF: Unraveling the Genetic Web: H-Ras Expression and Mutation
            in Oral Squamous Cell Carcinoma-A Systematic Review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Zhang,Q., Zheng,L., Bai,Y., Su,C., Che,Y., Xu,J., Sun,K., Ni,J.,
            Huang,L., Shen,Y., Jia,L., Xu,L., Yin,R., Li,M. and Hu,J.
  TITLE     ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21HRAS splicing and stabilizing DDX3X to activate the
            cRaf-MEK-ERK cascade
  JOURNAL   Cancer Lett 577, 216426 (2023)
   PUBMED   37820992
  REMARK    GeneRIF: ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21[HRAS] splicing and stabilizing DDX3X to activate
            the cRaf-MEK-ERK cascade.
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Wang,J., Al-Majid,D., Brenner,J.C. and Smith,J.D.
  TITLE     Mutant HRas Signaling and Rationale for Use of Farnesyltransferase
            Inhibitors in Head and Neck Squamous Cell Carcinoma
  JOURNAL   Target Oncol 18 (5), 643-655 (2023)
   PUBMED   37665491
  REMARK    GeneRIF: Mutant HRas Signaling and Rationale for Use of
            Farnesyltransferase Inhibitors in Head and Neck Squamous Cell
            Carcinoma.
            Review article
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Gripp,K.W. and Weaver,K.N.
  TITLE     HRAS-Related Costello Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301680
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Sakai,E., Rikimaru,K., Ueda,M., Matsumoto,Y., Ishii,N., Enomoto,S.,
            Yamamoto,H. and Tsuchida,N.
  TITLE     The p53 tumor-suppressor gene and ras oncogene mutations in oral
            squamous-cell carcinoma
  JOURNAL   Int J Cancer 52 (6), 867-872 (1992)
   PUBMED   1459726
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Tanci,P., Genuardi,M., Santini,S.A. and Neri,G.
  TITLE     PCR detection of an insertion/deletion polymorphism in intron 1 of
            the HRAS1 locus
  JOURNAL   Nucleic Acids Res 20 (5), 1157 (1992)
   PUBMED   1549493
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Kinsella,B.T., Erdman,R.A. and Maltese,W.A.
  TITLE     Posttranslational modification of Ha-ras p21 by farnesyl versus
            geranylgeranyl isoprenoids is determined by the COOH-terminal amino
            acid
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 8934-8938 (1991)
   PUBMED   1924354
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Tong,L.A., de Vos,A.M., Milburn,M.V. and Kim,S.H.
  TITLE     Crystal structures at 2.2 A resolution of the catalytic domains of
            normal ras protein and an oncogenic mutant complexed with GDP
  JOURNAL   J Mol Biol 217 (3), 503-516 (1991)
   PUBMED   1899707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC137894.5, BM808879.1,
            BM801600.1 and BC006499.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the Ras oncogene family, whose
            members are related to the transforming genes of mammalian sarcoma
            retroviruses. The products encoded by these genes function in
            signal transduction pathways. These proteins can bind GTP and GDP,
            and they have intrinsic GTPase activity. This protein undergoes a
            continuous cycle of de- and re-palmitoylation, which regulates its
            rapid exchange between the plasma membrane and the Golgi apparatus.
            Mutations in this gene cause Costello syndrome, a disease
            characterized by increased growth at the prenatal stage, growth
            deficiency at the postnatal stage, predisposition to tumor
            formation, cognitive disability, skin and musculoskeletal
            abnormalities, distinctive facial appearance and cardiovascular
            abnormalities. Defects in this gene are implicated in a variety of
            cancers, including bladder cancer, follicular thyroid cancer, and
            oral squamous cell carcinoma. Multiple transcript variants, which
            encode different isoforms, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Both variants 1 and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.195820.1,
                                           SRR1163658.446806.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311189.8/ ENSP00000309845.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..189
                     /product="GTPase HRas isoform 1"
                     /EC_number="3.6.5.2"
                     /note="Ha-Ras1 proto-oncoprotein; Ras family small GTP
                     binding protein H-Ras; Harvey rat sarcoma viral oncogene
                     homolog; p19 H-RasIDX protein; transforming protein p21;
                     GTPase HRas; GTP- and GDP-binding peptide B;
                     transformation gene: oncogene HAMSV; c-has/bas p21
                     protein; v-Ha-ras Harvey rat sarcoma viral oncogene
                     homolog; Harvey rat sarcoma viral oncoprotein"
                     /calculated_mol_wt=21167
     mat_peptide     1..186
                     /product="GTPase HRas. /id=PRO_0000042996"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
                     /calculated_mol_wt=20999
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in GTPase HRas, alternate.
                     /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     mat_peptide     2..186
                     /product="GTPase HRas, N-terminally processed.
                     /id=PRO_0000326476"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
                     /calculated_mol_wt=20868
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine, in GTPase HRas, N-terminally
                     processed. /evidence=ECO:0000269|Ref.12; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Region          3..164
                     /region_name="H_N_K_Ras_like"
                     /note="Ras GTPase family containing H-Ras,N-Ras and
                     K-Ras4A/4B; cd04138"
                     /db_xref="CDD:133338"
     Site            10..17
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:133338"
     Site            order(11..12,59..60)
                     /site_type="other"
                     /note="putative GDI interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:133338"
     Site            order(12..18,28..30,32,35,60,116..117,119..120,145..146)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:133338"
     Site            order(17..18,30..32,34,37,40..41,54..55,57,59..61,63..65,
                     67,69..71,73,102..103,147)
                     /site_type="other"
                     /note="GEF interaction site [polypeptide binding]"
                     /db_xref="CDD:133338"
     Site            order(25,37..41)
                     /site_type="active"
                     /note="effector interaction site [active]"
                     /db_xref="CDD:133338"
     Region          32..40
                     /region_name="Effector region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
     Site            33..40
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:133338"
     Site            35
                     /site_type="glycosylation"
                     /note="(Microbial infection) O-linked (Glc) threonine, by
                     P.sordellii toxin TcsL.
                     /evidence=ECO:0000269|PubMed:19744486,
                     ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586,
                     ECO:0000269|PubMed:9632667; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     Site            35
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:133338"
     Site            57..60
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:133338"
     Site            59..77
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:133338"
     Site            116..119
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:133338"
     Site            145..147
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:133338"
     Region          166..185
                     /region_name="Hypervariable region"
                     /note="propagated from UniProtKB/Swiss-Prot (P01112.1)"
     Site            186
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8626715; propagated from
                     UniProtKB/Swiss-Prot (P01112.1)"
     CDS             1..189
                     /gene="HRAS"
                     /gene_synonym="C-BAS/HAS; C-H-RAS; C-HA-RAS1; CTLO;
                     H-RASIDX; HAMSV; HRAS1; p21ras; RASH1"
                     /coded_by="NM_005343.4:215..784"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7698.1"
                     /db_xref="GeneID:3265"
                     /db_xref="HGNC:HGNC:5173"
                     /db_xref="MIM:190020"
ORIGIN      
        1 mteyklvvvg aggvgksalt iqliqnhfvd eydptiedsy rkqvvidget clldildtag
       61 qeeysamrdq ymrtgegflc vfainntksf edihqyreqi krvkdsddvp mvlvgnkcdl
      121 aartvesrqa qdlarsygip yietsaktrq gvedafytlv reirqhklrk lnppdesgpg
      181 cmsckcvls
//
LOCUS       NP_149016                589 aa            linear   PRI 20-NOV-2025
DEFINITION  cysteine/serine-rich nuclear protein 1 isoform b [Homo sapiens].
ACCESSION   NP_149016
VERSION     NP_149016.2
DBSOURCE    REFSEQ: accession NM_033027.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 589)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 589)
  AUTHORS   Zhu,J., Xu,H.N., Lin,T. and Xia,Z.J.
  TITLE     Silencing of cysteine and serine rich nuclear protein 1 inhibits
            apoptosis, senescence and collagen degradation in human-derived
            vaginal fibroblasts in response to oxidative stress or DNA damage
  JOURNAL   Exp Cell Res 440 (2), 114139 (2024)
   PUBMED   38908423
  REMARK    GeneRIF: Silencing of cysteine and serine rich nuclear protein 1
            inhibits apoptosis, senescence and collagen degradation in
            human-derived vaginal fibroblasts in response to oxidative stress
            or DNA damage.
REFERENCE   3  (residues 1 to 589)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 589)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 589)
  AUTHORS   Macdonald,C.D., Falconer,A.M.D., Chan,C.M., Wilkinson,D.J.,
            Skelton,A., Reynard,L., Litherland,G.J., Europe-Finner,G.N. and
            Rowan,A.D.
  TITLE     Cytokine-induced cysteine- serine-rich nuclear protein-1 (CSRNP1)
            selectively contributes to MMP1 expression in human chondrocytes
  JOURNAL   PLoS One 13 (11), e0207240 (2018)
   PUBMED   30440036
  REMARK    GeneRIF: cFos bound to the AP-1 cis element within the proximal
            MMP1 promoter only when the gene was transcriptionally silent as
            previously observed for MMP13. cFos contributes to MMP1 expression.
            Silencing of ATF3 (a prime MMP13 modulator) did not affect MMP1
            expression whilst silencing CSRNP1 resulted in substantial
            repression of MMP1 but not MMP13.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 589)
  AUTHORS   St Pourcain,B., Skuse,D.H., Mandy,W.P., Wang,K., Hakonarson,H.,
            Timpson,N.J., Evans,D.M., Kemp,J.P., Ring,S.M., McArdle,W.L.,
            Golding,J. and Smith,G.D.
  TITLE     Variability in the common genetic architecture of
            social-communication spectrum phenotypes during childhood and
            adolescence
  JOURNAL   Mol Autism 5 (1), 18 (2014)
   PUBMED   24564958
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 589)
  AUTHORS   Wang,K., Ling,T., Wu,H. and Zhang,J.
  TITLE     Screening of candidate tumor-suppressor genes in 3p21.3 and
            investigation of the methylation of gene promoters in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 29 (3), 1175-1182 (2013)
   PUBMED   23292452
  REMARK    GeneRIF: Three candidate tumor-suppressor genes, SEMA3B, AXUD1 and
            GNAT1 may be involved in oral squamous cell carcinoma.
REFERENCE   8  (residues 1 to 589)
  AUTHORS   Esteves,S.L., Domingues,S.C., da Cruz e Silva,O.A., Fardilha,M. and
            da Cruz e Silva,E.F.
  TITLE     Protein phosphatase 1alpha interacting proteins in the human brain
  JOURNAL   OMICS 16 (1-2), 3-17 (2012)
   PUBMED   22321011
REFERENCE   9  (residues 1 to 589)
  AUTHORS   Gingras,S., Pelletier,S., Boyd,K. and Ihle,J.N.
  TITLE     Characterization of a family of novel cysteine- serine-rich nuclear
            proteins (CSRNP)
  JOURNAL   PLoS One 2 (8), e808 (2007)
   PUBMED   17726538
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 589)
  AUTHORS   Ishiguro,H., Tsunoda,T., Tanaka,T., Fujii,Y., Nakamura,Y. and
            Furukawa,Y.
  TITLE     Identification of AXUD1, a novel human gene induced by AXIN1 and
            its reduced expression in human carcinomas of the lung, liver,
            colon and kidney
  JOURNAL   Oncogene 20 (36), 5062-5066 (2001)
   PUBMED   11526492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092053.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 6, 2009 this sequence version replaced NP_149016.1.
            
            Summary: This gene encodes a protein that localizes to the nucleus
            and expression of this gene is induced in response to elevated
            levels of axin. The Wnt signalling pathway, which is negatively
            regulated by axin, is important in axis formation in early
            development and impaired regulation of this signalling pathway is
            often involved in tumors. A decreased level of expression of this
            gene in tumors compared to the level of expression in their
            corresponding normal tissues suggests that this gene product has a
            tumor suppressor function. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (2) contains an alternate 5'
            terminal exon, resulting in a novel 5' UTR and the use of a
            downstream start codon, compared to variant 1. The encoded isoform
            (b) has a shorter N-terminus compared to isoform a. Variants 2 and
            3 encode the same isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB053121.1, SRR1660805.175666.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000273153.10/ ENSP00000273153.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..589
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..589
                     /product="cysteine/serine-rich nuclear protein 1 isoform
                     b"
                     /note="AXIN1 up-regulated 1; axin-1 up-regulated gene 1
                     protein; TGF-beta-induced apoptosis protein 3"
                     /calculated_mol_wt=63377
     Region          1..62
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S65.2)"
     Region          80..304
                     /region_name="CSRNP_N"
                     /note="Cysteine/serine-rich nuclear protein N-terminus;
                     pfam16019"
                     /db_xref="CDD:464977"
     Region          309..388
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96S65.2)"
     CDS             1..589
                     /gene="CSRNP1"
                     /gene_synonym="AXUD1; CSRNP-1; FAM130B; TAIP-3; URAX1"
                     /coded_by="NM_033027.4:195..1964"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2682.1"
                     /db_xref="GeneID:64651"
                     /db_xref="HGNC:HGNC:14300"
                     /db_xref="MIM:606458"
ORIGIN      
        1 mtgllkrkfd qldednssvs ssssssgcqs rscspsssvs rawdseeegp wdqmplpdrd
       61 fcgprsftpl silkrarrer pgrvafdgit vfyfprcqgf tsvpsrggct lgmalrhsac
      121 rrfslaefaq eqararhekl rqrlkeekle mlqwklsaag vpqaeaglpp vvdaiddasv
      181 eedlavavag grleevsflq pyparrrral lrasgvrrid reekrelqal rqsredcgch
      241 cdricdpetc scslagikcq mdhtafpcgc cregcenpmg rvefnqarvq thfihtltrl
      301 qleqeaesfr eleapaqgsp pspgeealvp tfplakppmn nelgdnscss dmtdsstass
      361 sasgtseapd cpthpglpgp gfqpgvddds larilsfsds dfggeeeeee egsvgnldnl
      421 scfhpadifg tsdpgglasw thsysgcsft sgvldenanl dascflnggl egsregslpg
      481 tsvppsmdag rsssvdlsls scdsfellqa lpdyslgphy tsqkvsdsld nieaphfplp
      541 glsppgdass cfleslmgfs epaaealdpf idsqfedtvp aslmepvpv
//
LOCUS       NP_937863                225 aa            linear   PRI 20-NOV-2025
DEFINITION  U2 small nuclear ribonucleoprotein B'' [Homo sapiens].
ACCESSION   NP_937863
VERSION     NP_937863.1
DBSOURCE    REFSEQ: accession NM_198220.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   4  (residues 1 to 225)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Hong,W., Bennett,M., Xiao,Y., Feld Kramer,R., Wang,C. and Reed,R.
  TITLE     Association of U2 snRNP with the spliceosomal complex E
  JOURNAL   Nucleic Acids Res 25 (2), 354-361 (1997)
   PUBMED   9016565
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Laitinen,J., Saris,P., Holtta,E. and Pettersson,I.
  TITLE     U2-snRNP B' protein gene is an early growth-inducible gene
  JOURNAL   J Cell Biochem 58 (4), 490-498 (1995)
   PUBMED   7593271
REFERENCE   9  (residues 1 to 225)
  AUTHORS   Feeney,R.J. and Zieve,G.W.
  TITLE     Nuclear exchange of the U1 and U2 snRNP-specific proteins
  JOURNAL   J Cell Biol 110 (4), 871-881 (1990)
   PUBMED   2139037
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Habets,W.J., Sillekens,P.T., Hoet,M.H., Schalken,J.A.,
            Roebroek,A.J., Leunissen,J.A., van de Ven,W.J. and van
            Venrooij,W.J.
  TITLE     Analysis of a cDNA clone expressing a human autoimmune antigen:
            full-length sequence of the U2 small nuclear RNA-associated B'
            antigen
  JOURNAL   Proc Natl Acad Sci U S A 84 (8), 2421-2425 (1987)
   PUBMED   2951739
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA088017.1, BC036737.3,
            BM772256.1, AI741327.1 and AL034428.4.
            
            Summary: The protein encoded by this gene associates with stem loop
            IV of U2 small nuclear ribonucleoprotein (U2 snRNP) in the presence
            of snRNP-A'. The encoded protein may play a role in pre-mRNA
            splicing. Autoantibodies from patients with systemic lupus
            erythematosus frequently recognize epitopes on the encoded protein.
            Two transcript variants encoding the same protein have been found
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.164376.1,
                                           SRR3476690.1176981.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.1"
     Protein         1..225
                     /product="U2 small nuclear ribonucleoprotein B''"
                     /note="U2 snRNP B''; small nuclear ribonucleoprotein
                     polypeptide B"
                     /calculated_mol_wt=25355
     Region          6..96
                     /region_name="RRM1_U2B"
                     /note="RNA recognition motif 1 in U2 small nuclear
                     ribonucleoprotein B' (U2B') and similar proteins; cd12478"
                     /db_xref="CDD:409907"
     Site            order(10,12..13,16..17,19..20,24,40..51,53,77,80,82..89)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409907"
     Region          99..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08579.1)"
     Site            111
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9CQI7; propagated from
                     UniProtKB/Swiss-Prot (P08579.1)"
     Region          146..225
                     /region_name="RRM2_U2B"
                     /note="RNA recognition motif 2 (RRM2) found in vertebrate
                     U2 small nuclear ribonucleoprotein B' (U2B'); cd12481"
                     /db_xref="CDD:240925"
     Site            151
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P08579.1)"
     CDS             1..225
                     /gene="SNRPB2"
                     /gene_synonym="Msl1; U2B''"
                     /coded_by="NM_198220.3:75..752"
                     /db_xref="CCDS:CCDS13123.1"
                     /db_xref="GeneID:6629"
                     /db_xref="HGNC:HGNC:11155"
                     /db_xref="MIM:603520"
ORIGIN      
        1 mdirpnhtiy innmndkikk eelkrslyal fsqfghvvdi valktmkmrg qafvifkelg
       61 sstnalrqlq gfpfygkpmr iqyaktdsdi iskmrgtfad kekkkekkka ktveqtattt
      121 nkkpgqgtpn santqgnstp npqvpdyppn yilflnnlpe etnemmlsml fnqfpgfkev
      181 rlvpgrhdia fvefendgqa gaardalqgf kitpshamki tyakk
//
LOCUS       NP_006289                578 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein with KRAB and SCAN domains 8 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006289
VERSION     NP_006289.2
DBSOURCE    REFSEQ: accession NM_006298.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Satoh,J., Obayashi,S., Misawa,T., Sumiyoshi,K., Oosumi,K. and
            Tabunoki,H.
  TITLE     Protein microarray analysis identifies human cellular prion protein
            interactors
  JOURNAL   Neuropathol Appl Neurobiol 35 (1), 16-35 (2009)
   PUBMED   18482256
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Lee,P.L., Gelbart,T., West,C., Adams,M., Blackstone,R. and
            Beutler,E.
  TITLE     Three genes encoding zinc finger proteins on human chromosome
            6p21.3: members of a new subclass of the Kruppel gene family
            containing the conserved SCAN box domain
  JOURNAL   Genomics 43 (2), 191-201 (1997)
   PUBMED   9244436
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Beutler,E., Gelbart,T., West,C., Kuhl,W. and Lee,P.
  TITLE     A strategy for cloning the hereditary hemochromatosis gene
  JOURNAL   Blood Cells Mol Dis 21 (3), 207-216 (1995)
   PUBMED   8673473
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL358933.15, AB208793.1, BC130032.1 and BM664529.1.
            
            On Dec 17, 2004 this sequence version replaced NP_006289.1.
            
            Transcript Variant: This variant (2) lacks an internal exon in the
            5' UTR, compared to variant 1. Both variants 1 and 2 encode the
            same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.180801.1,
                                           SRR1660807.129098.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330236.7/ ENSP00000332750.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..578
                     /product="zinc finger protein with KRAB and SCAN domains 8
                     isoform 1"
                     /note="zinc finger protein with KRAB and SCAN domains 8;
                     zinc finger protein 192"
                     /calculated_mol_wt=65685
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15776.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15776.2)"
     Region          47..159
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          158..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15776.2)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P17029; propagated from
                     UniProtKB/Swiss-Prot (Q15776.2)"
     Region          221..>262
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          <315..564
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          324..344
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          380..400
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          408..428
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          436..456
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(441,443,445,447..448,451..452,455,469,471,475..476,
                     479..480,483,497,499,501,503..504,507..508,511)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          464..484
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(464,467,480,484)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          492..512
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          520..540
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(520,523,536,540)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:275368"
     Region          548..568
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..578
                     /gene="ZKSCAN8"
                     /gene_synonym="LD5-1; ZNF192; ZSCAN40"
                     /coded_by="NM_006298.4:240..1976"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS4645.1"
                     /db_xref="GeneID:7745"
                     /db_xref="HGNC:HGNC:12983"
                     /db_xref="MIM:602240"
ORIGIN      
        1 maeesrkpsa psppdqtpee dlvivkveed hgwdqesslh esnplgqevf rlrfrqlryq
       61 etlgpreali qlralchqwl rpdlntkeqi lellvleqfl tilpeelqtl vkehqlenge
      121 evvtlledle rqidilgrpv sarvhghrvl weevvhsasa peppntqlqs eatqhkspvp
      181 qesqeramst sqsptrsqkg ssgdqemtat lltagfqtle kiedmavsli reewlldpsq
      241 kdlcrdnrpe nfrnmfslgg etrsenrela skqvistgiq phgetaakcn gdvirglehe
      301 eardllgrle rqrgnptqer rhkcdecgks faqssglvrh wrihtgekpy qcnvcgkafs
      361 yrsallshqd ihnkvkryhc kecgkafsqn tglilhqrih tgekpyqcnq cgkafsqsag
      421 lilhqrihsg erpyecnecg kafshsshli ghqrihtgek pyecdecgkt frrsshligh
      481 qrshtgekpy kcnecgrafs qksgliehqr ihtgerpykc kecgkafngn tgliqhlrih
      541 tgekpyqcne cgkafiqrss lirhqrihsg eksesisv
//
LOCUS       NP_000990                 70 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL38 [Homo sapiens].
ACCESSION   NP_000990
VERSION     NP_000990.1
DBSOURCE    REFSEQ: accession NM_000999.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 70)
  AUTHORS   Qin,Y., Liu,L., Hu,X., Zhang,Y., Pan,Y. and Gao,H.
  TITLE     Expression and bioinformatics analysis of RPL38 protein and mRNA in
            gastric cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (13), 256-261 (2023)
   PUBMED   38158659
  REMARK    GeneRIF: Expression and bioinformatics analysis of RPL38 protein
            and mRNA in gastric cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 70)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 70)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 70)
  AUTHORS   Gopanenko,A.V., Kolobova,A.V., Meschaninova,M.I., Venyaminova,A.G.,
            Tupikin,A.E., Kabilov,M.R., Malygin,A.A. and Karpova,G.G.
  TITLE     Knockdown of the mRNA encoding the ribosomal protein eL38 in
            mammalian cells causes a substantial reorganization of genomic
            transcription
  JOURNAL   Biochimie 184, 132-142 (2021)
   PUBMED   33675855
  REMARK    GeneRIF: Knockdown of the mRNA encoding the ribosomal protein eL38
            in mammalian cells causes a substantial reorganization of genomic
            transcription.
REFERENCE   5  (residues 1 to 70)
  AUTHORS   Gopanenko,A.V., Kolobova,A.V., Tupikin,A.E., Kabilov,M.R.,
            Malygin,A.A. and Karpova,G.G.
  TITLE     Knockdown of the Ribosomal Protein eL38 in HEK293 Cells Changes the
            Translational Efficiency of Specific Genes
  JOURNAL   Int J Mol Sci 22 (9), 4531 (2021)
   PUBMED   33926116
  REMARK    GeneRIF: Knockdown of the Ribosomal Protein eL38 in HEK293 Cells
            Changes the Translational Efficiency of Specific Genes.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 70)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   7  (residues 1 to 70)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 70)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 70)
  AUTHORS   Espinosa,L., Martin,M., Nicolas,A., Fabre,M. and Navarro,E.
  TITLE     Primary sequence of the human, lysine-rich, ribosomal protein RPL38
            and detection of an unusual RPL38 processed pseudogene in the
            promoter region of the type-1 angiotensin II receptor gene
  JOURNAL   Biochim Biophys Acta 1354 (1), 58-64 (1997)
   PUBMED   9375793
REFERENCE   10 (residues 1 to 70)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BQ276548.1, Z26876.1, CB124619.1 and AC100786.2.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L38E family of ribosomal proteins. It is located in the
            cytoplasm. Alternative splice variants have been identified, both
            encoding the same protein. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome, including one located in
            the promoter region of the type 1 angiotensin II receptor gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) is the longer and predominant
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.54255.1, CD390038.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311111.11/ ENSP00000309830.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..70
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..70
                     /product="large ribosomal subunit protein eL38"
                     /note="60S ribosomal protein L38"
                     /calculated_mol_wt=8087
     Region          2..68
                     /region_name="Ribosomal_L38e"
                     /note="Ribosomal L38e protein family; pfam01781"
                     /db_xref="CDD:460326"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63173.2)"
     Site            67
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P63173.2)"
     CDS             1..70
                     /gene="RPL38"
                     /gene_synonym="eL38; L38"
                     /coded_by="NM_000999.4:107..319"
                     /db_xref="CCDS:CCDS11696.1"
                     /db_xref="GeneID:6169"
                     /db_xref="HGNC:HGNC:10349"
                     /db_xref="MIM:604182"
ORIGIN      
        1 mprkieeikd flltarrkda ksvkikknkd nvkfkvrcsr ylytlvitdk ekaeklkqsl
       61 ppglavkelk
//
LOCUS       NP_073208                246 aa            linear   PRI 20-NOV-2025
DEFINITION  U11/U12 small nuclear ribonucleoprotein 35 kDa protein isoform a
            [Homo sapiens].
ACCESSION   NP_073208
VERSION     NP_073208.1
DBSOURCE    REFSEQ: accession NM_022717.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Huckins,L.M., Chatzinakos,C., Breen,M.S., Hartmann,J., Klengel,T.,
            da Silva Almeida,A.C., Dobbyn,A., Girdhar,K., Hoffman,G.E.,
            Klengel,C., Logue,M.W., Lori,A., Maihofer,A.X., Morrison,F.G.,
            Nguyen,H.T., Park,Y., Ruderfer,D., Sloofman,L.G., van Rooij,S.J.H.,
            Baker,D.G., Chen,C.Y., Cox,N., Duncan,L.E., Geyer,M.A., Glatt,S.J.,
            Im,H.K., Risbrough,V.B., Smoller,J.W., Stein,D.J., Yehuda,R.,
            Liberzon,I., Koenen,K.C., Jovanovic,T., Kellis,M., Miller,M.W.,
            Bacanu,S.A., Nievergelt,C.M., Buxbaum,J.D., Sklar,P., Ressler,K.J.,
            Stahl,E.A. and Daskalakis,N.P.
  CONSRTM   PTSD Working Group of Psychiatric Genomics Consortium
  TITLE     Analysis of Genetically Regulated Gene Expression Identifies a
            Prefrontal PTSD Gene, SNRNP35, Specific to Military Cohorts
  JOURNAL   Cell Rep 31 (9), 107716 (2020)
   PUBMED   32492425
  REMARK    GeneRIF: Analysis of Genetically Regulated Gene Expression
            Identifies a Prefrontal PTSD Gene, SNRNP35, Specific to Military
            Cohorts.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Fertig,N., Domsic,R.T., Rodriguez-Reyna,T., Kuwana,M., Lucas,M.,
            Medsger,T.A. Jr. and Feghali-Bostwick,C.A.
  TITLE     Anti-U11/U12 RNP antibodies in systemic sclerosis: a new serologic
            marker associated with pulmonary fibrosis
  JOURNAL   Arthritis Rheum 61 (7), 958-965 (2009)
   PUBMED   19565553
  REMARK    GeneRIF: Anti-U11/U12 RNP antibodies are present in the sera of
            approximately 3% of patients with systemic sclerosis and are a
            marker for lung fibrosis, which is often severe.
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Pessa,H.K., Will,C.L., Meng,X., Schneider,C., Watkins,N.J.,
            Perala,N., Nymark,M., Turunen,J.J., Luhrmann,R. and Frilander,M.J.
  TITLE     Minor spliceosome components are predominantly localized in the
            nucleus
  JOURNAL   Proc Natl Acad Sci U S A 105 (25), 8655-8660 (2008)
   PUBMED   18559850
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Golas,M.M., Sander,B., Will,C.L., Luhrmann,R. and Stark,H.
  TITLE     Major conformational change in the complex SF3b upon integration
            into the spliceosomal U11/U12 di-snRNP as revealed by electron
            cryomicroscopy
  JOURNAL   Mol Cell 17 (6), 869-883 (2005)
   PUBMED   15780942
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Adams,D.S., Li,Q., Tan,X., Pero,S.C. and Czop,J.K.
  TITLE     Cloning and characterization of a family of cDNAs from human
            histiocyte macrophage cells encoding an arginine-rich basic protein
            related to the 70 kD U1-snRNP splicing factor
  JOURNAL   DNA Seq 9 (4), 205-215 (1998)
   PUBMED   10520751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM714052.1, BC047678.1 and
            AC145423.8.
            
            Summary: The protein encoded by this gene is a homolog of the
            U1-snRNP binding protein. The N-terminal half contains a RNA
            recognition motif and the C-terminal half is rich in Arg/Asp and
            Arg/Glu dipeptides, which is a characteristic of a variety of
            splicing factors. This protein is a component of the U11/U12 small
            nuclear ribonucleoproteins (snRNP) that form part of the U12-type
            spliceosome. Alternative splicing results in multiple transcript
            variants encoding two distinct isoforms and representing a
            non-protein coding variant. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) encodes the shorter isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.510716.1,
                                           SRR5189661.165690.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000526639.3/ ENSP00000432595.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..246
                     /product="U11/U12 small nuclear ribonucleoprotein 35 kDa
                     protein isoform a"
                     /note="U11/U12 snRNP 35K; U11/U12 small nuclear
                     ribonucleoprotein 35 kDa protein; U11/U12-35K; protein
                     HM-1; U11/U12 snRNP 35 kDa protein; small nuclear
                     ribonucleoprotein 35kDa (U11/U12); small nuclear
                     ribonucleoprotein, U11/U12 35kDa subunit; U1 snRNP-binding
                     protein homolog"
                     /calculated_mol_wt=29319
     Region          47..137
                     /region_name="RRM_snRNP35"
                     /note="RNA recognition motif (RRM) found in U11/U12 small
                     nuclear ribonucleoprotein 35 kDa protein (U11/U12-35K) and
                     similar proteins; cd12237"
                     /db_xref="CDD:409683"
     Region          187..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16560.1)"
     CDS             1..246
                     /gene="SNRNP35"
                     /gene_synonym="HM-1; HM1; U1SNRNPBP"
                     /coded_by="NM_022717.4:82..822"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9249.1"
                     /db_xref="GeneID:11066"
                     /db_xref="HGNC:HGNC:30852"
                     /db_xref="MIM:619631"
ORIGIN      
        1 mndwmpiake ydplkagsid gtdedphdra vwramlaryv pnkgvigdpl ltlfvarlnl
       61 qtkedklkev fsrygdirrl rlvrdlvtgf skgyafieyk eeravikayr dadglvidqh
      121 eifvdyeler tlkgwiprrl ggglggkkes gqlrfggrdr pfrkpinlpv vkndlyregk
      181 rerrersrsr erhwdsrtrd rdhdrgrekr wqereptrvw pdndwererd frddrikgre
      241 kkergk
//
LOCUS       NP_036203                195 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 3 [Homo sapiens].
ACCESSION   NP_036203
VERSION     NP_036203.1
DBSOURCE    REFSEQ: accession NM_012071.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Hancock,J.L., Kalimutho,M., Straube,J., Lim,M., Gresshoff,I.,
            Saunus,J.M., Lee,J.S., Lakhani,S.R., Simpson,K.J., Bush,A.I.,
            Anderson,R.L. and Khanna,K.K.
  TITLE     COMMD3 loss drives invasive breast cancer growth by modulating
            copper homeostasis
  JOURNAL   J Exp Clin Cancer Res 42 (1), 90 (2023)
   PUBMED   37072858
  REMARK    GeneRIF: COMMD3 loss drives invasive breast cancer growth by
            modulating copper homeostasis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Wang,S., Liu,Y., Li,S., Chen,Y., Liu,Y., Yan,J., Wu,J., Li,J.,
            Wang,L., Xiang,R., Shi,Y., Qin,X. and Yang,S.
  TITLE     COMMD3-Mediated Endosomal Trafficking of HER2 Inhibits the
            Progression of Ovarian Carcinoma
  JOURNAL   Mol Cancer Res 21 (3), 199-213 (2023)
   PUBMED   36445330
  REMARK    GeneRIF: COMMD3-Mediated Endosomal Trafficking of HER2 Inhibits the
            Progression of Ovarian Carcinoma.
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BF695081.1 and AF201948.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF201948.1, SRR5189664.146551.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376836.8/ ENSP00000366032.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.2"
     Protein         1..195
                     /product="COMM domain-containing protein 3"
                     /note="protein Bup"
                     /calculated_mol_wt=22020
     Region          98..194
                     /region_name="Commd3"
                     /note="COMM_Domain containing protein 3. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04751"
                     /db_xref="CDD:240099"
     CDS             1..195
                     /gene="COMMD3"
                     /gene_synonym="BUP; C10orf8"
                     /coded_by="NM_012071.4:31..618"
                     /db_xref="CCDS:CCDS7137.1"
                     /db_xref="GeneID:23412"
                     /db_xref="HGNC:HGNC:23332"
                     /db_xref="MIM:616700"
ORIGIN      
        1 melsesvqkg fqmladprsf dsnaftlllr aafqslldaq adeavldhpd lkhidpvvlk
       61 hchaaaatyi leagkhradk stlstyledc kfdrerielf cteyqnnkns leillgsigr
      121 slphitdvsw rleyqiktnq lhrmyrpayl vtlsvqntds psypeisfsc smeqlqdlvg
      181 klkdasksle ratql
//
LOCUS       NP_001291646             576 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and
            dual-specificity protein phosphatase PTEN isoform PTEN-L [Homo
            sapiens].
ACCESSION   NP_001291646
VERSION     NP_001291646.4
DBSOURCE    REFSEQ: accession NM_001304717.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 576)
  AUTHORS   Chowdhury,S.G., Misra,S., Ghosh,G., Mukherjee,A., Gopi,P.,
            Pandya,P., Islam,M.M. and Karmakar,P.
  TITLE     NHEJ is promoted by the phosphorylation and phosphatase activity of
            PTEN via regulation of DNA-PKcs
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119828 (2024)
   PUBMED   39197593
  REMARK    GeneRIF: NHEJ is promoted by the phosphorylation and phosphatase
            activity of PTEN via regulation of DNA-PKcs.
REFERENCE   2  (residues 1 to 576)
  AUTHORS   Huang,X., Zhang,D., Zhang,D., Guo,J., Gu,G., Wang,Y., Wu,G.,
            Wang,C., Fu,B. and Li,K.
  TITLE     Decoding PTEN: from biological functions to signaling pathways in
            tumors
  JOURNAL   Mol Biol Rep 51 (1), 1089 (2024)
   PUBMED   39446204
  REMARK    GeneRIF: Decoding PTEN: from biological functions to signaling
            pathways in tumors.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 576)
  AUTHORS   Derkyi-Kwarteng,L., Ghartey,F.N., Aidoo,E., Addae,E., Imbeah,E.G.,
            Brown,A.A. and Acquah,S.
  TITLE     A retrospective analysis suggests PTEN expression is associated
            with favorable clinicopathological features of breast cancer
  JOURNAL   Sci Rep 14 (1), 21645 (2024)
   PUBMED   39284903
  REMARK    GeneRIF: A retrospective analysis suggests PTEN expression is
            associated with favorable clinicopathological features of breast
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 576)
  AUTHORS   Trujano-Camacho,S., Cantu-de Leon,D., Perez-Yepez,E.,
            Contreras-Romero,C., Coronel-Hernandez,J., Millan-Catalan,O.,
            Rodriguez-Dorantes,M., Lopez-Camarillo,C., Gutierrez-Ruiz,C.,
            Jacobo-Herrera,N. and Perez-Plasencia,C.
  TITLE     HOTAIR Promotes the Hyperactivation of PI3K/Akt and
            Wnt/beta-Catenin Signaling Pathways via PTEN Hypermethylation in
            Cervical Cancer
  JOURNAL   Cells 13 (17), 1484 (2024)
   PUBMED   39273054
  REMARK    GeneRIF: HOTAIR Promotes the Hyperactivation of PI3K/Akt and
            Wnt/beta-Catenin Signaling Pathways via PTEN Hypermethylation in
            Cervical Cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 576)
  AUTHORS   Liang,H., He,S., Yang,J., Jia,X., Wang,P., Chen,X., Zhang,Z.,
            Zou,X., McNutt,M.A., Shen,W.H. and Yin,Y.
  TITLE     PTENalpha, a PTEN isoform translated through alternative
            initiation, regulates mitochondrial function and energy metabolism
  JOURNAL   Cell Metab 19 (5), 836-848 (2014)
   PUBMED   24768297
REFERENCE   6  (residues 1 to 576)
  AUTHORS   Hopkins,B.D., Fine,B., Steinbach,N., Dendy,M., Rapp,Z., Shaw,J.,
            Pappas,K., Yu,J.S., Hodakoski,C., Mense,S., Klein,J., Pegno,S.,
            Sulis,M.L., Goldstein,H., Amendolara,B., Lei,L., Maurer,M.,
            Bruce,J., Canoll,P., Hibshoosh,H. and Parsons,R.
  TITLE     A secreted PTEN phosphatase that enters cells to alter signaling
            and survival
  JOURNAL   Science 341 (6144), 399-402 (2013)
   PUBMED   23744781
  REMARK    GeneRIF: identified a 576-amino acid translational variant of PTEN,
            PTEN-Long, that arises from an alternative translation start site
            519 base pairs upstream of the ATG initiation sequence; PTEN-Long
            is a membrane-permeable lipid phosphatase that is secreted from
            cells and can enter other cells
REFERENCE   7  (residues 1 to 576)
  AUTHORS   Steck,P.A., Pershouse,M.A., Jasser,S.A., Yung,W.K., Lin,H.,
            Ligon,A.H., Langford,L.A., Baumgard,M.L., Hattier,T., Davis,T.,
            Frye,C., Hu,R., Swedlund,B., Teng,D.H. and Tavtigian,S.V.
  TITLE     Identification of a candidate tumour suppressor gene, MMAC1, at
            chromosome 10q23.3 that is mutated in multiple advanced cancers
  JOURNAL   Nat Genet 15 (4), 356-362 (1997)
   PUBMED   9090379
REFERENCE   8  (residues 1 to 576)
  AUTHORS   Li,J., Yen,C., Liaw,D., Podsypanina,K., Bose,S., Wang,S.I., Puc,J.,
            Miliaresis,C., Rodgers,L., McCombie,R., Bigner,S.H.,
            Giovanella,B.C., Ittmann,M., Tycko,B., Hibshoosh,H., Wigler,M.H.
            and Parsons,R.
  TITLE     PTEN, a putative protein tyrosine phosphatase gene mutated in human
            brain, breast, and prostate cancer
  JOURNAL   Science 275 (5308), 1943-1947 (1997)
   PUBMED   9072974
REFERENCE   9  (residues 1 to 576)
  AUTHORS   Peiffer,S.L., Herzog,T.J., Tribune,D.J., Mutch,D.G., Gersell,D.J.
            and Goodfellow,P.J.
  TITLE     Allelic loss of sequences from the long arm of chromosome 10 and
            replication errors in endometrial cancers
  JOURNAL   Cancer Res 55 (9), 1922-1926 (1995)
   PUBMED   7728760
REFERENCE   10 (residues 1 to 576)
  AUTHORS   Yehia,L. and Eng,C.
  TITLE     PTEN Hamartoma Tumor Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301661
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U92436.1, BC005821.2,
            AC063965.8 and AA836562.1.
            
            On Nov 26, 2018 this sequence version replaced NP_001291646.3.
            
            Summary: This gene was identified as a tumor suppressor that is
            mutated in a large number of cancers at high frequency. The protein
            encoded by this gene is a phosphatidylinositol-3,4,5-trisphosphate
            3-phosphatase. It contains a tensin like domain as well as a
            catalytic domain similar to that of the dual specificity protein
            tyrosine phosphatases. Unlike most of the protein tyrosine
            phosphatases, this protein preferentially dephosphorylates
            phosphoinositide substrates. It negatively regulates intracellular
            levels of phosphatidylinositol-3,4,5-trisphosphate in cells and
            functions as a tumor suppressor by negatively regulating AKT/PKB
            signaling pathway. The use of a non-canonical (CUG) upstream
            initiation site produces a longer isoform that initiates
            translation with a leucine, and is thought to be preferentially
            associated with the mitochondrial inner membrane. This longer
            isoform may help regulate energy metabolism in the mitochondria. A
            pseudogene of this gene is found on chromosome 9. Alternative
            splicing and the use of multiple translation start codons results
            in multiple transcript variants encoding different isoforms.
            [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (1) encodes multiple isoforms due
            to the use of alternative translation initiation codons. The
            longest isoform (PTEN-L, PMID:23744781; also known as PTENalpha,
            PMID: 24768297) is derived from the use of an upstream non-AUG
            (CUG) start codon, while two shorter isoforms are derived from
            downstream AUG start codons. PTEN-L, initiates with a Leucine,
            rather than a Methionine, is thought to be preferentially
            associated with the mitochondrial inner membrane (PMID: 24768297),
            and is represented in this RefSeq.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U92436.1, BC005821.2 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            non-AUG initiation codon :: PMID: 23744781, 24768297
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..576
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..576
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     3-phosphatase and dual-specificity protein phosphatase
                     PTEN isoform PTEN-L"
                     /EC_number="3.1.3.67"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="phosphatidylinositol-3,4,5-trisphosphate
                     3-phosphatase and dual-specificity protein phosphatase
                     PTEN; mitochondrial PTENalpha; MMAC1 phosphatase and
                     tensin homolog deleted on chromosome 10; mutated in
                     multiple advanced cancers 1; phosphatase and tensin-like
                     protein; PTENepsilon; PTEN variant PTEN-K267Rfs*9; PTEN
                     variant PTEN-R234Afs*11; inositol polyphosphate
                     3-phosphatase; mitochondrial phosphatase and tensin
                     protein alpha; protein tyrosine phosphatase; PTEN variant
                     PTEN-L247*"
                     /calculated_mol_wt=64864
     Region          197..354
                     /region_name="PTP_PTEN"
                     /note="protein tyrosine phosphatase-like catalytic domain
                     of phosphatase and tensin homolog; cd14509"
                     /db_xref="CDD:350359"
     Region          361..522
                     /region_name="PTEN_C2"
                     /note="C2 domain of PTEN tumour-suppressor protein;
                     pfam10409"
                     /db_xref="CDD:463081"
     CDS             1..576
                     /gene="PTEN"
                     /gene_synonym="10q23del; BZS; CWS1; DEC; GLM2; MHAM;
                     MMAC1; PTEN1; PTENbeta; PTENgama; TEP1"
                     /coded_by="NM_001304717.5:326..2056"
                     /note="isoform PTEN-L is encoded by transcript variant 2;
                     non-AUG (CUG) translation initiation codon;
                     translation initiation by tRNA-Leu at CUG codon"
                     /db_xref="GeneID:5728"
                     /db_xref="HGNC:HGNC:9588"
                     /db_xref="MIM:601728"
ORIGIN      
        1 lerggeaaaa aaaaaaapgr gsespvtisr agnagelvsp lllpptrrrr rrhiqgpgpv
       61 lnlpsaaaap pvarapeaag ggsrsedyss sphsaaaaar plaaeekqaq slqpsssrrs
      121 shypaavqsq aaaergasat aksraisilq kkprhqqllp slssfffshr lpdmtaiike
      181 ivsrnkrryq edgfdldlty iypniiamgf paerlegvyr nniddvvrfl dskhknhyki
      241 ynlcaerhyd takfncrvaq ypfedhnppq lelikpfced ldqwlseddn hvaaihckag
      301 kgrtgvmica yllhrgkflk aqealdfyge vrtrdkkgvt ipsqrryvyy ysyllknhld
      361 yrpvallfhk mmfetipmfs ggtcnpqfvv cqlkvkiyss nsgptrredk fmyfefpqpl
      421 pvcgdikvef fhkqnkmlkk dkmfhfwvnt ffipgpeets ekvengslcd qeidsicsie
      481 radndkeylv ltltkndldk ankdkanryf spnfkvklyf tktveepsnp eassstsvtp
      541 dvsdnepdhy rysdttdsdp enepfdedqh tqitkv
//
LOCUS       NP_001034859             453 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein with metallophosphoesterase domain isoform 1
            [Homo sapiens].
ACCESSION   NP_001034859 XP_934488 XP_938735
VERSION     NP_001034859.2
DBSOURCE    REFSEQ: accession NM_001039770.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 453)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 453)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC112211.2, AK126979.1, BC136872.1 and AK128242.1.
            
            On Oct 29, 2008 this sequence version replaced NP_001034859.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126979.1, SRR5189667.227919.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342462.5/ ENSP00000343398.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..453
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.3"
     Protein         1..453
                     /product="transmembrane protein with
                     metallophosphoesterase domain isoform 1"
                     /EC_number="3.1.-.-"
                     /calculated_mol_wt=49322
     Site            7..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT21.2)"
     Site            43..63
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT21.2)"
     Site            87..107
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT21.2)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT21.2)"
     Site            162..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZT21.2)"
     Region          206..449
                     /region_name="MPP_YkuE_C"
                     /note="Bacillus subtilis YkuE and related proteins,
                     C-terminal metallophosphatase domain; cd07385"
                     /db_xref="CDD:277331"
     Site            order(214,216,246,277..278,369,391,393)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:277331"
     Site            order(214,216,246,277,369,391,393)
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:277331"
     CDS             1..453
                     /gene="TMPPE"
                     /coded_by="NM_001039770.3:537..1898"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33732.1"
                     /db_xref="GeneID:643853"
                     /db_xref="HGNC:HGNC:33865"
ORIGIN      
        1 maifrqlslg akatlaavtv fvsmiasrsy laeslelraw rwllrlqlal fvnsllligs
       61 lyiwrstvsn lchspaaest cfqlwkvvvl aflalahssf ftmfflvaee pylfslaays
      121 clgayiimlf flfilsgmeq ayqllawrsg rvvgslektr klvlrpalav gvtavlsvag
      181 ilnaaqppav ktvevpihql pasmnnlkiv llsdihlgpt vgrtkmemfv rmvnvlepdi
      241 tvivgdlsds easvlrtava plgqlhshlg ayfvtgnhey ytsdvsnwfa lleslhvqpl
      301 hnenvkisat raqrggggsg sgsededwic lagvddiead ilhysghgmd ldkalegcsp
      361 dhtiillahq plaakralqa rpdinlilsg hthagqifpl nvaayllnpf faglyqvaqa
      421 tfvyvspgta yygipmrlgs raeitelilq rsp
//
LOCUS       NP_001269848             876 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 3 [Homo sapiens].
ACCESSION   NP_001269848 XP_005251247
VERSION     NP_001269848.1
DBSOURCE    REFSEQ: accession NM_001282919.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 876)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 876)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 876)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 876)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 876)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 876)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 876)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 876)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 876)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY012281.1, AK303579.1 and BM981420.1.
            
            On Sep 21, 2013 this sequence version replaced XP_005251247.1.
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 5' coding and lacks an exon in the 3' coding region. These
            differences cause translation initiation at a downstream AUG and a
            frameshift in the 3' coding egion . The resulting isoform (3) is
            shorter and has a distinct N-and C-termini, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303579.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..876
                     /product="DNA repair-scaffolding protein isoform 3"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=96739
     Region          3..309
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          461..790
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..876
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001282919.1:225..2855"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS64890.1"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 maqsltaeek titekhlelc prpkqettts kstsgltdit wsssgsdlsd edktlsqlqr
       61 delqfidwei dsdraeasdc defeddegav eisdcascas nqsltsdekl selpkpssie
      121 ileyssdsek eddlenvlli dsesphkyhv qfasdarqim erlidprtks tetilhtpqk
      181 ptakfprtpe nsakkkllrg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt
      241 vkilelheec amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv
      301 rifppwqkli ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi
      361 kgltnnspei qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga
      421 gvrvvvqrvy slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar
      481 qlegkscslv gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa
      541 lcyiltahpn lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql
      601 kslllleqre iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl
      661 ffkdalrdqg rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq
      721 gtvvgvdest afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr
      781 srpqcrvkvk vgarpehart psslqhseel rseecprkgs gvvklfcpvr nrppdqlhwi
      841 ggnrasecrr glcrtlavaa gsvnfamwlq gwwwww
//
LOCUS       NP_001093259             275 aa            linear   PRI 20-NOV-2025
DEFINITION  intercellular adhesion molecule 2 precursor [Homo sapiens].
ACCESSION   NP_001093259
VERSION     NP_001093259.1
DBSOURCE    REFSEQ: accession NM_001099789.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Tang,X., Huang,J., Jiang,Y., Qiu,J., Li,T., Li,W., Chen,Z.,
            Huang,Z., Yu,X., Yang,T., Ji,X., Tan,R., Lv,L., Yang,Z. and Chen,H.
  TITLE     Intercellular adhesion molecule 2 as a novel prospective tumor
            suppressor induced by ERG promotes ubiquitination-mediated radixin
            degradation to inhibit gastric cancer tumorigenicity and metastasis
  JOURNAL   J Transl Med 21 (1), 670 (2023)
   PUBMED   37759298
  REMARK    GeneRIF: Intercellular adhesion molecule 2 as a novel prospective
            tumor suppressor induced by ERG promotes ubiquitination-mediated
            radixin degradation to inhibit gastric cancer tumorigenicity and
            metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Chong,D.L.W., Rebeyrol,C., Jose,R.J., Williams,A.E., Brown,J.S.,
            Scotton,C.J. and Porter,J.C.
  TITLE     ICAM-1 and ICAM-2 Are Differentially Expressed and Up-Regulated on
            Inflamed Pulmonary Epithelium, but Neither ICAM-2 nor LFA-1: ICAM-1
            Are Required for Neutrophil Migration Into the Airways In Vivo
  JOURNAL   Front Immunol 12, 691957 (2021)
   PUBMED   34484188
  REMARK    GeneRIF: ICAM-1 and ICAM-2 Are Differentially Expressed and
            Up-Regulated on Inflamed Pulmonary Epithelium, but Neither ICAM-2
            nor LFA-1: ICAM-1 Are Required for Neutrophil Migration Into the
            Airways In Vivo.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Jin,X., Bu,Q., Zou,Y., Feng,Y. and Wei,M.
  TITLE     Lewis-antigen-containing ICAM-2/3 on Jurkat leukemia cells interact
            with DC-SIGN to regulate DC functions
  JOURNAL   Glycoconj J 35 (3), 287-297 (2018)
   PUBMED   29671117
  REMARK    GeneRIF: Lewis-antigen-containing ICAM-2/3 on Jurkat leukemia cells
            interact with DC-SIGN to regulate DC functions.
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Zuo,Y., Cui,Y., Di Poto,C., Varghese,R.S., Yu,G., Li,R. and
            Ressom,H.W.
  TITLE     INDEED: Integrated differential expression and differential network
            analysis of omic data for biomarker discovery
  JOURNAL   Methods 111, 12-20 (2016)
   PUBMED   27592383
  REMARK    GeneRIF: INDEED also identified some candidates previously reported
            to be relevant to HCC, such as intercellular adhesion molecule 2
            (ICAM2) and c4b-binding protein alpha chain (C4BPA), which were
            missed by both Differential expression and differential network
            analyses
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Sasaki,Y., Tamura,M., Takeda,K., Ogi,K., Nakagaki,T., Koyama,R.,
            Idogawa,M., Hiratsuka,H. and Tokino,T.
  TITLE     Identification and characterization of the intercellular adhesion
            molecule-2 gene as a novel p53 target
  JOURNAL   Oncotarget 7 (38), 61426-61437 (2016)
   PUBMED   27556181
  REMARK    GeneRIF: ICAM2 induction by p53 has a key role in inhibiting cancer
            cell migration and invasion.ICAM2 acts at least in part through the
            suppression of the MEK-ERK signaling pathway.
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Fawcett,J., Holness,C.L., Needham,L.A., Turley,H., Gatter,K.C.,
            Mason,D.Y. and Simmons,D.L.
  TITLE     Molecular cloning of ICAM-3, a third ligand for LFA-1,
            constitutively expressed on resting leukocytes
  JOURNAL   Nature 360 (6403), 481-484 (1992)
   PUBMED   1448173
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Sansom,D., Borrow,J., Solomon,E. and Trowsdale,J.
  TITLE     The human ICAM2 gene maps to 17q23-25
  JOURNAL   Genomics 11 (2), 462-464 (1991)
   PUBMED   1769660
REFERENCE   8  (residues 1 to 275)
  AUTHORS   de Fougerolles,A.R., Stacker,S.A., Schwarting,R. and Springer,T.A.
  TITLE     Characterization of ICAM-2 and evidence for a third
            counter-receptor for LFA-1
  JOURNAL   J Exp Med 174 (1), 253-267 (1991)
   PUBMED   1676048
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Staunton,D.E., Dustin,M.L. and Springer,T.A.
  TITLE     Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1
            homologous to ICAM-1
  JOURNAL   Nature 339 (6219), 61-64 (1989)
   PUBMED   2497351
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Dustin,M.L., Garcia-Aguilar,J., Hibbs,M.L., Larson,R.S.,
            Stacker,S.A., Staunton,D.E., Wardlaw,A.J. and Springer,T.A.
  TITLE     Structure and regulation of the leukocyte adhesion receptor LFA-1
            and its counterreceptors, ICAM-1 and ICAM-2
  JOURNAL   Cold Spring Harb Symp Quant Biol 54 Pt 2, 753-765 (1989)
   PUBMED   2577025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CA841927.1 and AK223219.1.
            
            Summary: The protein encoded by this gene is a member of the
            intercellular adhesion molecule (ICAM) family. All ICAM proteins
            are type I transmembrane glycoproteins, contain 2-9
            immunoglobulin-like C2-type domains, and bind to the leukocyte
            adhesion LFA-1 protein. This protein may play a role in lymphocyte
            recirculation by blocking LFA-1-dependent cell adhesion. It
            mediates adhesive interactions important for antigen-specific
            immune response, NK-cell mediated clearance, lymphocyte
            recirculation, and other cellular interactions important for immune
            response and surveillance. Several transcript variants encoding the
            same protein have been found for this gene. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR compared
            to variant 1. All 5 variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.259991.1,
                                           SRR5189655.154757.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680, SAMEA2150385
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000579788.6/ ENSP00000464665.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.3"
     Protein         1..275
                     /product="intercellular adhesion molecule 2 precursor"
                     /note="ICAM-2"
                     /calculated_mol_wt=28392
     sig_peptide     1..21
                     /calculated_mol_wt=2281
     mat_peptide     22..275
                     /product="intercellular adhesion molecule 2"
                     /calculated_mol_wt=28392
     Region          27..109
                     /region_name="IgI_N_ICAM-2"
                     /note="N-terminal immunoglobulin domain of the
                     intercellular adhesion molecules ICAM-2 (Cluster of
                     Differentiation 102 or CD102); member of the I-set of IgSF
                     domains; cd20995"
                     /db_xref="CDD:409587"
     Region          29..32
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409587"
     Region          35..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409587"
     Region          43..49
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409587"
     Site            47
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          56..61
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409587"
     Region          63..64
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409587"
     Region          66..72
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409587"
     Region          75..80
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409587"
     Site            82
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ;
                     propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          86..94
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409587"
     Region          98..108
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409587"
     Site            105
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          111..211
                     /region_name="IgC2_2_ICAM-1_like"
                     /note="Second immunoglobulin (Ig)-like C2-set domain of
                     intercellular cell adhesion molecule 1 (ICAM-1), and
                     similar domains; cd05755"
                     /db_xref="CDD:409413"
     Region          111..118
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409413"
     Region          129..138
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409413"
     Region          145..151
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409413"
     Region          153..156
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409413"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ;
                     propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          171..178
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409413"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19349973; propagated from
                     UniProtKB/Swiss-Prot (P13598.2)"
     Region          186..193
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409413"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:9153399,
                     ECO:0007744|PDB:1ZXQ; propagated from UniProtKB/Swiss-Prot
                     (P13598.2)"
     Region          202..209
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409413"
     Site            224..248
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P13598.2)"
     Region          251..275
                     /region_name="Required for interaction with EZR, MSN and
                     RDX and co-localization to microvilli.
                     /evidence=ECO:0000250|UniProtKB:P35330"
                     /note="propagated from UniProtKB/Swiss-Prot (P13598.2)"
     CDS             1..275
                     /gene="ICAM2"
                     /gene_synonym="CD102"
                     /coded_by="NM_001099789.2:156..983"
                     /db_xref="CCDS:CCDS11657.1"
                     /db_xref="GeneID:3384"
                     /db_xref="HGNC:HGNC:5345"
                     /db_xref="MIM:146630"
ORIGIN      
        1 mssfgyrtlt valftliccp gsdekvfevh vrpkklavep kgslevncst tcnqpevggl
       61 etsldkilld eqaqwkhylv snishdtvlq chftcsgkqe smnsnvsvyq pprqviltlq
      121 ptlvavgksf tiecrvptve pldsltlflf rgnetlhyet fgkaapapqe atatfnstad
      181 redghrnfsc lavldlmsrg gnifhkhsap kmleiyepvs dsqmviivtv vsvllslfvt
      241 svllcfifgq hlrqqrmgty gvraawrrlp qafrp
//
LOCUS       NP_001355925             342 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform a [Homo sapiens].
ACCESSION   NP_001355925 XP_024303345
VERSION     NP_001355925.1
DBSOURCE    REFSEQ: accession NM_001368996.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 342)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 342)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 342)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 342)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 342)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 342)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 342)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 342)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 342)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303345.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.103016.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..342
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..342
                     /product="aprataxin isoform a"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=38973
     Region          3..102
                     /region_name="FHA_APTX"
                     /note="forkhead associated (FHA) domain found in aprataxin
                     and similar proteins; cd22735"
                     /db_xref="CDD:438787"
     Site            order(29..31,34..36,38..42,63..65,91)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438787"
     Region          164..265
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(258,260,262..264)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            260
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          283..342
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..342
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001368996.1:103..1131"
                     /note="isoform a is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS47956.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhmv nelypyivef eeeaknpgle thrkrkrsgn
      121 sdsierdaaq eaeagtglep gsnsgqcsvp lkkgkdapik keslghwsqg lkismqdpkm
      181 qvykdeqvvv ikdkypkary hwlvlpwtsi sslkavareh lellkhmhtv gekvivdfag
      241 ssklrfrlgy haipsmshvh lhvisqdfds pclknkkhwn sfnteyfles qaviemvqea
      301 grvtvrdgmp ellklplrch ecqqllpsip qlkehlrkhw tq
//
LOCUS       NP_001351758             415 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 16 [Homo sapiens].
ACCESSION   NP_001351758 XP_011536773
VERSION     NP_001351758.1
DBSOURCE    REFSEQ: accession NM_001364829.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 415)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 415)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 415)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 415)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 415)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 415)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 415)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 415)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 415)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 415)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079684.16 and AC079601.25.
            
            On Jul 12, 2018 this sequence version replaced XP_011536773.1.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.216663.1,
                                           SRR1803612.80151.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..415
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..415
                     /product="periphilin-1 isoform 16"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=47368
     Region          211..>267
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Region          <366..>401
                     /region_name="HERV-K_REC"
                     /note="Rec (regulator of expression encoded by corf) of
                     HERV-K-113; pfam15695"
                     /db_xref="CDD:292323"
     CDS             1..415
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001364829.2:84..1331"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdesgyr wtrddhsasr qpeyrdmrdg frrksfyssh
       61 yarerspykr dntffrespv grkdsphsrs gssvssrsys persksysfh qsqhrnkerp
      121 vqslktsrdt spssgsavss skvldkpsrl tekelaeaas kwaaekleks desnlpeise
      181 yeagstaplf tdqpeepesn tthgielfed sqlttrskai asktkeieqv yrqdcetfgm
      241 vvkmliekdp sleksiqfal rqnlheiesa gqtwqqvppv rntemdhdgt penegeetaq
      301 salfgfqhda snhtivglgp nqvpemkett lqapqppqap qplqprkkrv rrttqlrrtt
      361 gapditwgml kkttqeaeri llrtqtpftp enlflamlsv vhcnsrkdvk penkq
//
LOCUS       NP_001181973             488 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional coactivator YAP1 isoform 3 [Homo sapiens].
ACCESSION   NP_001181973
VERSION     NP_001181973.1
DBSOURCE    REFSEQ: accession NM_001195044.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Tang,W., Yang,Y., Fu,Z., Xu,W., Ou,W., Liu,F., Du,P. and Liu,C.Y.
  TITLE     The RNA helicase DDX21 activates YAP to promote tumorigenesis and
            is transcriptionally upregulated by beta-catenin in colorectal
            cancer
  JOURNAL   Oncogene 43 (44), 3227-3239 (2024)
   PUBMED   39285230
  REMARK    GeneRIF: The RNA helicase DDX21 activates YAP to promote
            tumorigenesis and is transcriptionally upregulated by beta-catenin
            in colorectal cancer.
REFERENCE   3  (residues 1 to 488)
  AUTHORS   He,C., Lv,X., Liu,J., Ruan,J., Chen,P., Huang,C., Angeletti,P.C.,
            Hua,G., Moness,M.L., Shi,D., Dhar,A., Yang,S., Murphy,S.,
            Montoute,I., Chen,X., Islam,K.N., George,S., Ince,T.A., Drapkin,R.,
            Guda,C., Davis,J.S. and Wang,C.
  TITLE     HPV-YAP1 oncogenic alliance drives malignant transformation of
            fallopian tube epithelial cells
  JOURNAL   EMBO Rep 25 (10), 4542-4569 (2024)
   PUBMED   39271776
  REMARK    GeneRIF: HPV-YAP1 oncogenic alliance drives malignant
            transformation of fallopian tube epithelial cells.
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Meyer,N.P., Singh,T., Kutys,M.L., Nystul,T.G. and Barber,D.L.
  TITLE     Arp2/3 complex activity enables nuclear YAP for naive pluripotency
            of human embryonic stem cells
  JOURNAL   Elife 13, e89725 (2024)
   PUBMED   39319536
  REMARK    GeneRIF: Arp2/3 complex activity enables nuclear YAP for naive
            pluripotency of human embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Jimbo,N., Ohbayashi,C., Fujii,T., Takeda,M., Mitsui,S., Tanaka,Y.,
            Itoh,T. and Maniwa,Y.
  TITLE     The expression of YAP1 and other transcription factors contributes
            to lineage plasticity in combined small cell lung carcinoma
  JOURNAL   J Pathol Clin Res 10 (5), e70001 (2024)
   PUBMED   39283755
  REMARK    GeneRIF: The expression of YAP1 and other transcription factors
            contributes to lineage plasticity in combined small cell lung
            carcinoma.
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Gaffney,C.J., Oka,T., Mazack,V., Hilman,D., Gat,U., Muramatsu,T.,
            Inazawa,J., Golden,A., Carey,D.J., Farooq,A., Tromp,G. and Sudol,M.
  TITLE     Identification, basic characterization and evolutionary analysis of
            differentially spliced mRNA isoforms of human YAP1 gene
  JOURNAL   Gene 509 (2), 215-222 (2012)
   PUBMED   22939869
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Gavva,N.R., Gavva,R., Ermekova,K., Sudol,M. and Shen,C.J.
  TITLE     Interaction of WW domains with hematopoietic transcription factor
            p45/NF-E2 and RNA polymerase II
  JOURNAL   J Biol Chem 272 (39), 24105-24108 (1997)
   PUBMED   9305852
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Chen,H.I., Einbond,A., Kwak,S.J., Linn,H., Koepf,E., Peterson,S.,
            Kelly,J.W. and Sudol,M.
  TITLE     Characterization of the WW domain of human yes-associated protein
            and its polyproline-containing ligands
  JOURNAL   J Biol Chem 272 (27), 17070-17077 (1997)
   PUBMED   9202023
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Chen,H.I. and Sudol,M.
  TITLE     The WW domain of Yes-associated protein binds a proline-rich ligand
            that differs from the consensus established for Src homology
            3-binding modules
  JOURNAL   Proc Natl Acad Sci U S A 92 (17), 7819-7823 (1995)
   PUBMED   7644498
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Sudol,M., Bork,P., Einbond,A., Kastury,K., Druck,T., Negrini,M.,
            Huebner,K. and Lehman,D.
  TITLE     Characterization of the mammalian YAP (Yes-associated protein) gene
            and its role in defining a novel protein module, the WW domain
  JOURNAL   J Biol Chem 270 (24), 14733-14741 (1995)
   PUBMED   7782338
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001527.5, AY316529.1,
            AL832620.2, AP000942.6 and AI128142.1.
            
            Summary: This gene encodes a downstream nuclear effector of the
            Hippo signaling pathway which is involved in development, growth,
            repair, and homeostasis. This gene is known to play a role in the
            development and progression of multiple cancers as a
            transcriptional regulator of this signaling pathway and may
            function as a potential target for cancer treatment. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site and lacks an alternate exon in the 3' coding region,
            compared to variant 9. The encoded protein (isoform 3) represents
            the YAP1-2alpha isoform described in Figure 3 of PMID: 22939869. It
            is shorter, compared to isoform 9.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.98541.1, AY316529.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.1"
     Protein         1..488
                     /product="transcriptional coactivator YAP1 isoform 3"
                     /note="65 kDa Yes-associated protein; yorkie homolog;
                     yes-associated protein 2; protein yorkie homolog;
                     yes-associated protein YAP65 homolog; transcriptional
                     coactivator YAP1; Yes associated protein 1"
                     /calculated_mol_wt=52617
     Region          174..203
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(188,199)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          231..263
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(247,258)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     CDS             1..488
                     /gene="YAP1"
                     /gene_synonym="COB1; YAP; YAP-1; YAP2; YAP65; YKI"
                     /coded_by="NM_001195044.2:403..1869"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS53699.1"
                     /db_xref="GeneID:10413"
                     /db_xref="HGNC:HGNC:16262"
                     /db_xref="MIM:606608"
ORIGIN      
        1 mdpgqqpppq papqgqgqpp sqppqgqgpp sgpgqpapaa tqaapqappa ghqivhvrgd
       61 setdlealfn avmnpktanv pqtvpmrlrk lpdsffkppe pkshsrqast dagtagaltp
      121 qhvrahsspa slqlgavspg tltptgvvsg paatptaqhl rqssfeipdd vplpagwema
      181 ktssgqryfl nhidqtttwq dprkamlsqm nvtaptsppv qqnmmnsasg plpdgweqam
      241 tqdgeiyyin hknkttswld prldprfamn qrisqsapvk qppplapqsp qggvmggsns
      301 nqqqqmrlqq lqmekerlrl kqqellrqel alrsqlptle qdggtqnpvs spgmsqelrt
      361 mttnssdpfl nsgtyhsrde stdsglsmss ysvprtpddf lnsvdemdtg dtinqstlps
      421 qqnrfpdyle aipgtnvdlg tlegdgmnie geelmpslqe alssdilndm esvlaatkld
      481 kesfltwl
//
LOCUS       NP_115763               1243 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase WNK4 isoform 1 [Homo sapiens].
ACCESSION   NP_115763
VERSION     NP_115763.2
DBSOURCE    REFSEQ: accession NM_032387.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1243)
  AUTHORS   Li,M., Shao,X., Ning,Q., Sun,R., Li,R., Liu,Y., Yuan,Y. and
            Zhang,Y.
  TITLE     Downregulation of WNK4 expression facilitates the proliferation of
            gastric cancer cells via activation of the STAT3 signaling pathway
  JOURNAL   Neoplasma 71 (3), 209-218 (2024)
   PUBMED   38764295
  REMARK    GeneRIF: Downregulation of WNK4 expression facilitates the
            proliferation of gastric cancer cells via activation of the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 1243)
  AUTHORS   Wang,L., Wu,G. and Peng,J.B.
  TITLE     Identification of a novel KLHL3-interacting motif in the C-terminal
            region of WNK4
  JOURNAL   Biochem Biophys Res Commun 670, 87-93 (2023)
   PUBMED   37285722
  REMARK    GeneRIF: Identification of a novel KLHL3-interacting motif in the
            C-terminal region of WNK4.
REFERENCE   3  (residues 1 to 1243)
  AUTHORS   Ying,S., Guo,Q. and Zhang,C.
  TITLE     KLHL3-dependent WNK4 degradation affected by potassium through the
            neddylation and autophagy pathway
  JOURNAL   BMC Nephrol 24 (1), 217 (2023)
   PUBMED   37481568
  REMARK    GeneRIF: KLHL3-dependent WNK4 degradation affected by potassium
            through the neddylation and autophagy pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1243)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 1243)
  AUTHORS   Kahle,K.T., Gimenez,I., Hassan,H., Wilson,F.H., Wong,R.D.,
            Forbush,B., Aronson,P.S. and Lifton,R.P.
  TITLE     WNK4 regulates apical and basolateral Cl- flux in extrarenal
            epithelia
  JOURNAL   Proc Natl Acad Sci U S A 101 (7), 2064-2069 (2004)
   PUBMED   14769928
  REMARK    GeneRIF: general role for WNK4 in the regulation of electrolyte
            flux in diverse epithelia
REFERENCE   6  (residues 1 to 1243)
  AUTHORS   Wilson,F.H., Kahle,K.T., Sabath,E., Lalioti,M.D., Rapson,A.K.,
            Hoover,R.S., Hebert,S.C., Gamba,G. and Lifton,R.P.
  TITLE     Molecular pathogenesis of inherited hypertension with hyperkalemia:
            the Na-Cl cotransporter is inhibited by wild-type but not mutant
            WNK4
  JOURNAL   Proc Natl Acad Sci U S A 100 (2), 680-684 (2003)
   PUBMED   12515852
REFERENCE   7  (residues 1 to 1243)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1243)
  AUTHORS   Verissimo,F. and Jordan,P.
  TITLE     WNK kinases, a novel protein kinase subfamily in multi-cellular
            organisms
  JOURNAL   Oncogene 20 (39), 5562-5569 (2001)
   PUBMED   11571656
REFERENCE   9  (residues 1 to 1243)
  AUTHORS   Wilson,F.H., Disse-Nicodeme,S., Choate,K.A., Ishikawa,K.,
            Nelson-Williams,C., Desitter,I., Gunel,M., Milford,D.V.,
            Lipkin,G.W., Achard,J.M., Feely,M.P., Dussol,B., Berland,Y.,
            Unwin,R.J., Mayan,H., Simon,D.B., Farfel,Z., Jeunemaitre,X. and
            Lifton,R.P.
  TITLE     Human hypertension caused by mutations in WNK kinases
  JOURNAL   Science 293 (5532), 1107-1112 (2001)
   PUBMED   11498583
REFERENCE   10 (residues 1 to 1243)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100793.8, CA388932.1,
            BC136664.1 and BM683764.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2003 this sequence version replaced NP_115763.1.
            
            Summary: This gene encodes a member of the WNK family of
            serine-threonine protein kinases. The kinase is part of the tight
            junction complex in kidney cells, and regulates the balance between
            NaCl reabsorption and K(+) secretion. The kinase regulates the
            activities of several types of ion channels, cotransporters, and
            exchangers involved in electrolyte flux in epithelial cells.
            Mutations in this gene result in pseudohypoaldosteronism type
            IIB.[provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136664.1, AJ316534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000246914.10/ ENSP00000246914.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..1243
                     /product="serine/threonine-protein kinase WNK4 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase WNK4; protein
                     kinase with no lysine 4; protein kinase lysine-deficient
                     4"
                     /calculated_mol_wt=134609
     Region          1..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          172..432
                     /region_name="STKc_WNK4"
                     /note="Catalytic domain of the Serine/Threonine protein
                     kinase, With No Lysine (WNK) 4; cd14033"
                     /db_xref="CDD:270935"
     Site            order(180..184,186,188,201,203,234,254..257,261,263,302,
                     304,306..307,309,321,324,338..341)
                     /site_type="active"
                     /db_xref="CDD:270935"
     Site            order(180..184,186,188,201,203,234,254..257,261,302,304,
                     306..307,309,321)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270935"
     Site            order(184,261,263,302,304,306,324,338..341)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270935"
     Site            320..341
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270935"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q9JIH7; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          453..515
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          526..564
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          557..567
                     /region_name="Interaction with KLHL3.
                     /evidence=ECO:0000269|PubMed:24641320"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Site            575
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26732173; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          630..683
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          751..871
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          <798..1074
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          943..1110
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          1016..1019
                     /region_name="RFXV motif.
                     /evidence=ECO:0000269|PubMed:16669787,
                     ECO:0000269|PubMed:24641320"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7TPK6; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     Region          1166..1243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J92.1)"
     Site            1217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80UE6; propagated from
                     UniProtKB/Swiss-Prot (Q96J92.1)"
     CDS             1..1243
                     /gene="WNK4"
                     /gene_synonym="PHA2B; PRKWNK4"
                     /coded_by="NM_032387.5:90..3821"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11439.1"
                     /db_xref="GeneID:65266"
                     /db_xref="HGNC:HGNC:14544"
                     /db_xref="MIM:601844"
ORIGIN      
        1 mlaspatett vlmsqteadl alrpppplgt agqprlgppp rrarrfsgka eprprssrls
       61 rrssvdlgll sswslpaspa pdppdppdsa gpgparsppp sskeppegtw tegapvkaae
      121 dsarpelpds avgpgsrepl rvpeavaler rreqeekedm etqavatspd grylkfdiei
      181 grgsfktvyr gldtdttvev awcelqtrkl sraerqrfse evemlkglqh pnivrfydsw
      241 ksvlrgqvci vlvtelmtsg tlktylrrfr emkprvlqrw srqilrglhf lhsrvppilh
      301 rdlkcdnvfi tgptgsvkig dlglatlkra sfaksvigtp efmapemyee kydeavdvya
      361 fgmcmlemat seypysecqn aaqiyrkvts grkpnsfhkv kipevkeiie gcirtdkner
      421 ftiqdllaha ffreergvhv elaeeddgek pglklwlrme darrggrprd nqaieflfql
      481 grdaaeevaq emvalglvce adyqpvarav rervaaiqrk reklrkarel ealppepgpp
      541 patvpmapgp psvfppepee peadqhqpfl frhasysstt sdcetdgyls ssgfldasdp
      601 alqppggvps slaeshlclp safalsiprs gpgsdfspgd syasdaasgl sdvgegmgqm
      661 rrppgrnlrr rprsrlrvts vsdqndrvve cqlqthnskm vtfrfdldgd speeiaaamv
      721 ynefilpser dgflrrirei iqrvetllkr dtgpmeaaed tlspqeepap lpalpvplpd
      781 psneelqsst slehrswtaf stsssspgtp lspgnpfspg tpispgpifp itsppchpsp
      841 spfspissqv ssnpsphpts splpfssstp efpvplsqcp wsslpttspp tfsptcsqvt
      901 lsspffppcp stssfpstta apllslasaf slavmtvaqs llspspglls qsppappspl
      961 pslplpppva pggqespsph taeveseasp pparplpgea rlapiseegk pqlvgrfqvt
     1021 sskepaeplp lqptsptlsg spkpstpqlt sessdtedsa gggpetreal aesdraaegl
     1081 gagveeegdd gkepqvggsp qplshpspvw mnysysslcl sseesessge deefwaelqs
     1141 lrqkhlseve tlqtlqkkei edlysrlgkq pppgivapaa mlssrqrrls kgsfptsrrn
     1201 slqrseppgp gimrrnslsg sstgsqeqra skgvtfagdv grm
//
LOCUS       NP_001273634              71 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-fold modifier 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001273634
VERSION     NP_001273634.1
DBSOURCE    REFSEQ: accession NM_001286705.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 71)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 71)
  AUTHORS   Ke,D., Guo,H.H., Jiang,N., Shi,R.S. and Fan,T.Y.
  TITLE     Inhibition of UFM1 expression suppresses cancer progression and is
            linked to the dismal prognosis and immune infiltration in oral
            squamous cell carcinoma
  JOURNAL   Aging (Albany NY) 15 (22), 13059-13076 (2023)
   PUBMED   37980168
  REMARK    GeneRIF: Inhibition of UFM1 expression suppresses cancer
            progression and is linked to the dismal prognosis and immune
            infiltration in oral squamous cell carcinoma.
REFERENCE   3  (residues 1 to 71)
  AUTHORS   Ishimura,R., Ito,S., Mao,G., Komatsu-Hirota,S., Inada,T., Noda,N.N.
            and Komatsu,M.
  TITLE     Mechanistic insights into the roles of the UFM1 E3 ligase complex
            in ufmylation and ribosome-associated protein quality control
  JOURNAL   Sci Adv 9 (33), eadh3635 (2023)
   PUBMED   37595036
  REMARK    GeneRIF: Mechanistic insights into the roles of the UFM1 E3 ligase
            complex in ufmylation and ribosome-associated protein quality
            control.
REFERENCE   4  (residues 1 to 71)
  AUTHORS   Chung,C.H. and Yoo,H.M.
  TITLE     Emerging role of protein modification by UFM1 in cancer
  JOURNAL   Biochem Biophys Res Commun 633, 61-63 (2022)
   PUBMED   36344165
  REMARK    GeneRIF: Emerging role of protein modification by UFM1 in cancer.
            Review article
REFERENCE   5  (residues 1 to 71)
  AUTHORS   Mao,M., Chen,Y., Yang,J., Cheng,Y., Xu,L., Ji,F., Zhou,J.,
            Zhang,X., Li,Z., Chen,C., Ju,S., Zhang,J. and Wang,L.
  TITLE     Modification of PLAC8 by UFM1 affects tumorous proliferation and
            immune response by impacting PD-L1 levels in triple-negative breast
            cancer
  JOURNAL   J Immunother Cancer 10 (12) (2022)
   PUBMED   36543379
  REMARK    GeneRIF: Modification of PLAC8 by UFM1 affects tumorous
            proliferation and immune response by impacting PD-L1 levels in
            triple-negative breast cancer.
REFERENCE   6  (residues 1 to 71)
  AUTHORS   Tatsumi,K., Yamamoto-Mukai,H., Shimizu,R., Waguri,S., Sou,Y.S.,
            Sakamoto,A., Taya,C., Shitara,H., Hara,T., Chung,C.H., Tanaka,K.,
            Yamamoto,M. and Komatsu,M.
  TITLE     The Ufm1-activating enzyme Uba5 is indispensable for erythroid
            differentiation in mice
  JOURNAL   Nat Commun 2, 181 (2011)
   PUBMED   21304510
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 71)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   8  (residues 1 to 71)
  AUTHORS   Tatsumi,K., Sou,Y.S., Tada,N., Nakamura,E., Iemura,S., Natsume,T.,
            Kang,S.H., Chung,C.H., Kasahara,M., Kominami,E., Yamamoto,M.,
            Tanaka,K. and Komatsu,M.
  TITLE     A novel type of E3 ligase for the Ufm1 conjugation system
  JOURNAL   J Biol Chem 285 (8), 5417-5427 (2010)
   PUBMED   20018847
  REMARK    GeneRIF: A novel type of E3 ligase for the Ufm1 conjugation system.
REFERENCE   9  (residues 1 to 71)
  AUTHORS   Sasakawa,H., Sakata,E., Yamaguchi,Y., Komatsu,M., Tatsumi,K.,
            Kominami,E., Tanaka,K. and Kato,K.
  TITLE     Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier
            1
  JOURNAL   Biochem Biophys Res Commun 343 (1), 21-26 (2006)
   PUBMED   16527251
  REMARK    GeneRIF: The solution structure and dynamics of human Ufm1 (hsUfm1)
            by nuclear magnetic resonance spectroscopy was analysed.
REFERENCE   10 (residues 1 to 71)
  AUTHORS   Komatsu,M., Chiba,T., Tatsumi,K., Iemura,S., Tanida,I., Okazaki,N.,
            Ueno,T., Kominami,E., Natsume,T. and Tanaka,K.
  TITLE     A novel protein-conjugating system for Ufm1, a ubiquitin-fold
            modifier
  JOURNAL   EMBO J 23 (9), 1977-1986 (2004)
   PUBMED   15071506
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL356863.12.
            
            Summary: UFM1 is a ubiquitin-like protein that is conjugated to
            target proteins by E1-like activating enzyme UBA5 (UBE1DC1; MIM
            610552) and E2-like conjugating enzyme UFC1 (MIM 610554) in a
            manner analogous to ubiquitylation (see UBE2M; MIM 603173) (Komatsu
            et al., 2004 [PubMed 15071506]).[supplied by OMIM, Dec 2008].
            
            Transcript Variant: This variant (4) contains an alternate exon in
            the 3' coding region, which results in a frameshift, compared to
            variant 1. The encoded isoform (4) has a distinct C-terminus and is
            shorter than isoform 1. Variants 4 and 5 encode the same isoform
            (4).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.12188.1,
                                           SRR1660803.119837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..71
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.3"
     Protein         1..71
                     /product="ubiquitin-fold modifier 1 isoform 4"
                     /calculated_mol_wt=7359
     Region          4..64
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     CDS             1..71
                     /gene="UFM1"
                     /gene_synonym="BM-002; C13orf20; HLD14"
                     /coded_by="NM_001286705.2:70..285"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:51569"
                     /db_xref="HGNC:HGNC:20597"
                     /db_xref="MIM:610553"
ORIGIN      
        1 mskvsfkitl tsdprlpykv lsvpestpft avlkfaaeef kvpaatsaii tndgiginpa
       61 qtaglaveiq p
//
LOCUS       NP_001340025             324 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            5 [Homo sapiens].
ACCESSION   NP_001340025 XP_016880357
VERSION     NP_001340025.1
DBSOURCE    REFSEQ: accession NM_001353096.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            On Jun 29, 2017 this sequence version replaced XP_016880357.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.7774.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..324
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 5"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=35908
     Region          1..93
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          134..318
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     CDS             1..324
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353096.1:425..1399"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mgkvqvyqep nretrvqiqe svrgkdvfii qtvskdvntt imellimvya cktscaksii
       61 gvipyfpysk qckmrkrgsi vskllasmmc kaglthlitm dlhqkeiqgf fnipvdnlra
      121 spfllqyiqe eipdyrnavi vakspasakr aqsfaerlrl giavihgeaq daesdlvdgr
      181 hsppmvrsva aihpsleipm lipkekppit vvgdvggria iivddiiddv dsflaaaetl
      241 kergaykifv mathgllssd aprrieesai devvvtntip hevqklqcpk iktvdismil
      301 seairrihng esmsylfrni gldd
//
LOCUS       NP_006236                602 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
            delta isoform isoform 1 [Homo sapiens].
ACCESSION   NP_006236
VERSION     NP_006236.1
DBSOURCE    REFSEQ: accession NM_006245.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 602)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 602)
  AUTHORS   Wu,C.G., Balakrishnan,V.K., Merrill,R.A., Parihar,P.S.,
            Konovolov,K., Chen,Y.C., Xu,Z., Wei,H., Sundaresan,R., Cui,Q.,
            Wadzinski,B.E., Swingle,M.R., Musiyenko,A., Chung,W.K.,
            Honkanen,R.E., Suzuki,A., Huang,X., Strack,S. and Xing,Y.
  TITLE     B56delta long-disordered arms form a dynamic PP2A regulation
            interface coupled with global allostery and Jordan's syndrome
            mutations
  JOURNAL   Proc Natl Acad Sci U S A 121 (1), e2310727120 (2024)
   PUBMED   38150499
REFERENCE   3  (residues 1 to 602)
  AUTHORS   Oyama,N., Vaneynde,P., Reynhout,S., Pao,E.M., Timms,A., Fan,X.,
            Foss,K., Derua,R., Janssens,V., Chung,W. and Mirzaa,G.M.
  TITLE     Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis
  JOURNAL   J Med Genet 60 (5), 511-522 (2023)
   PUBMED   36216457
  REMARK    GeneRIF: Clinical, neuroimaging and molecular characteristics of
            PPP2R5D-related neurodevelopmental disorders: an expanded series
            with functional characterisation and genotype-phenotype analysis.
REFERENCE   4  (residues 1 to 602)
  AUTHORS   Liu,R., Huang,Y., Li,C., Wang,P., Wang,Y. and Zhang,L.
  TITLE     A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree
  JOURNAL   Clin Neurol Neurosurg 223, 107524 (2022)
   PUBMED   36403339
  REMARK    GeneRIF: A novel nonsense mutation in PPP2R5D is associated with
            neurodevelopmental disorders and shows incomplete penetrance in a
            Chinese pedigree.
REFERENCE   5  (residues 1 to 602)
  AUTHORS   Anwar,M.I., Li,N., Zhou,Q., Chen,M., Hu,C., Wu,T., Chen,H., Li,Y.P.
            and Zhou,Y.
  TITLE     PPP2R5D promotes hepatitis C virus infection by binding to viral
            NS5B and enhancing viral RNA replication
  JOURNAL   Virol J 19 (1), 118 (2022)
   PUBMED   35836293
  REMARK    GeneRIF: PPP2R5D promotes hepatitis C virus infection by binding to
            viral NS5B and enhancing viral RNA replication.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 602)
  AUTHORS   McCright,B., Rivers,A.M., Audlin,S. and Virshup,D.M.
  TITLE     The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
            encodes differentiation-induced phosphoproteins that target PP2A to
            both nucleus and cytoplasm
  JOURNAL   J Biol Chem 271 (36), 22081-22089 (1996)
   PUBMED   8703017
REFERENCE   7  (residues 1 to 602)
  AUTHORS   McCright,B., Brothman,A.R. and Virshup,D.M.
  TITLE     Assignment of human protein phosphatase 2A regulatory subunit genes
            b56alpha, b56beta, b56gamma, b56delta, and b56epsilon
            (PPP2R5A-PPP2R5E), highly expressed in muscle and brain, to
            chromosome regions 1q41, 11q12, 3p21, 6p21.1, and 7p11.2 --> p12
  JOURNAL   Genomics 36 (1), 168-170 (1996)
   PUBMED   8812429
REFERENCE   8  (residues 1 to 602)
  AUTHORS   Tanabe,O., Nagase,T., Murakami,T., Nozaki,H., Usui,H., Nishito,Y.,
            Hayashi,H., Kagamiyama,H. and Takeda,M.
  TITLE     Molecular cloning of a 74-kDa regulatory subunit (B' or delta) of
            human protein phosphatase 2A
  JOURNAL   FEBS Lett 379 (1), 107-111 (1996)
   PUBMED   8566219
REFERENCE   9  (residues 1 to 602)
  AUTHORS   McCright,B. and Virshup,D.M.
  TITLE     Identification of a new family of protein phosphatase 2A regulatory
            subunits
  JOURNAL   J Biol Chem 270 (44), 26123-26128 (1995)
   PUBMED   7592815
REFERENCE   10 (residues 1 to 602)
  AUTHORS   Mirzaa,G., Foss,K., Sudnawa,K. and Chung,W.K.
  TITLE     PPP2R5D-Related Neurodevelopmental Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30676711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA388594.1 and BC010692.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The product of this gene belongs to the phosphatase 2A
            regulatory subunit B family. Protein phosphatase 2A is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a delta isoform of the regulatory subunit B56 subfamily.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript, and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.13725.1,
                                           SRR1803611.68421.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000485511.6/ ENSP00000417963.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..602
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..602
                     /product="serine/threonine-protein phosphatase 2A 56 kDa
                     regulatory subunit delta isoform isoform 1"
                     /calculated_mol_wt=69861
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14738.1)"
     Region          37..52
                     /region_name="8 X 2 AA approximate tandem repeats of Q-P"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14738.1)"
     Region          56..>122
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); cl27532"
                     /db_xref="CDD:474937"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14738.1)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14738.1)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14738.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14738.1)"
     Region          110..513
                     /region_name="B56"
                     /note="Protein phosphatase 2A regulatory B subunit (B56
                     family); pfam01603"
                     /db_xref="CDD:460264"
     Region          523..530
                     /region_name="SH3-binding, class I. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14738.1)"
     Region          548..565
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14738.1)"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14738.1)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q14738.1)"
     CDS             1..602
                     /gene="PPP2R5D"
                     /gene_synonym="B56D; B56delta; HJS1; MRD35"
                     /coded_by="NM_006245.4:109..1917"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4878.1"
                     /db_xref="GeneID:5528"
                     /db_xref="HGNC:HGNC:9312"
                     /db_xref="MIM:601646"
ORIGIN      
        1 mpyklkkeke ppkvakctak psssgkdggg enteeaqpqp qpqpqpqaqs qppssnkrps
       61 nstppptqls kikysggpqi vkkerrqsss rfnlsknrel qklpalkdsp tqereelfiq
      121 klrqccvlfd fvsdplsdlk fkevkragln emveyithsr dvvteaiype avtmfsvnlf
      181 rtlppssnpt gaefdpeede ptleaawphl qlvyefflrf lespdfqpni akkyidqkfv
      241 lalldlfdse dprerdflkt ilhriygkfl glrayirrqi nhifyrfiye tehhngiael
      301 leilgsiing falplkeehk mflirvllpl hkvkslsvyh pqlaycvvqf lekessltep
      361 vivgllkfwp kthspkevmf lneleeildv iepsefskvm eplfrqlakc vssphfqvae
      421 ralyywnney imslisdnaa rvlpimfpal yrnskshwnk tihgliynal klfmemnqkl
      481 fddctqqyka ekqkgrfrmk ereemwqkie elarlnpqyp mfrappplpp vysmetetpt
      541 aediqllkrt veteavqmlk dikkekvllr rkselpqdvy tikaleahkr aeefltasqe
      601 al
//
LOCUS       NP_001246                499 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 20 homolog [Homo sapiens].
ACCESSION   NP_001246
VERSION     NP_001246.2
DBSOURCE    REFSEQ: accession NM_001255.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Sitry-Shevah,D., Miniowitz-Shemtov,S., Liburkin Dan,T. and
            Hershko,A.
  TITLE     The Mitotic Checkpoint Complex controls the association of Cdc20
            regulatory protein with the ubiquitin ligase APC/C in mitosis
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2413089121 (2024)
   PUBMED   39231204
  REMARK    GeneRIF: The Mitotic Checkpoint Complex controls the association of
            Cdc20 regulatory protein with the ubiquitin ligase APC/C in
            mitosis.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Li,Q., Chen,Q., Zheng,T., Wang,F., Teng,J., Zhou,H. and Chen,J.
  TITLE     CCDC68 Maintains Mitotic Checkpoint Activation by Promoting CDC20
            Integration into the MCC
  JOURNAL   Adv Sci (Weinh) 11 (35), e2406009 (2024)
   PUBMED   39018254
  REMARK    GeneRIF: CCDC68 Maintains Mitotic Checkpoint Activation by
            Promoting CDC20 Integration into the MCC.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Zhang,Y., Young,R., Garvanska,D.H., Song,C., Zhai,Y., Wang,Y.,
            Jiang,H., Fang,J., Nilsson,J., Alfieri,C. and Zhang,G.
  TITLE     Functional analysis of Cdc20 reveals a critical role of CRY box in
            mitotic checkpoint signaling
  JOURNAL   Commun Biol 7 (1), 164 (2024)
   PUBMED   38337031
  REMARK    GeneRIF: Functional analysis of Cdc20 reveals a critical role of
            CRY box in mitotic checkpoint signaling.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Fang,G., Yu,H. and Kirschner,M.W.
  TITLE     The checkpoint protein MAD2 and the mitotic regulator CDC20 form a
            ternary complex with the anaphase-promoting complex to control
            anaphase initiation
  JOURNAL   Genes Dev 12 (12), 1871-1883 (1998)
   PUBMED   9637688
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Kallio,M., Weinstein,J., Daum,J.R., Burke,D.J. and Gorbsky,G.J.
  TITLE     Mammalian p55CDC mediates association of the spindle checkpoint
            protein Mad2 with the cyclosome/anaphase-promoting complex, and is
            involved in regulating anaphase onset and late mitotic events
  JOURNAL   J Cell Biol 141 (6), 1393-1406 (1998)
   PUBMED   9628895
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Weinstein,J., Karim,J., Geschwind,D.H., Nelson,S.F., Krumm,J. and
            Sakamoto,K.M.
  TITLE     Genomic organization, 5' flanking enhancer region, and chromosomal
            assignment of the cell cycle gene, p55Cdc
  JOURNAL   Mol Genet Metab 64 (1), 52-57 (1998)
   PUBMED   9682218
  REMARK    Erratum:[Mol Genet Metab 2001 Apr;72(4):364]
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Weinstein,J.
  TITLE     Cell cycle-regulated expression, phosphorylation, and degradation
            of p55Cdc. A mammalian homolog of CDC20/Fizzy/slp1
  JOURNAL   J Biol Chem 272 (45), 28501-28511 (1997)
   PUBMED   9353311
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Weinstein,J., Jacobsen,F.W., Hsu-Chen,J., Wu,T. and Baum,L.G.
  TITLE     A novel mammalian protein, p55CDC, present in dividing cells is
            associated with protein kinase activity and has homology to the
            Saccharomyces cerevisiae cell division cycle proteins Cdc20 and
            Cdc4
  JOURNAL   Mol Cell Biol 14 (5), 3350-3363 (1994)
   PUBMED   7513050
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001088.2.
            
            On Nov 24, 2006 this sequence version replaced NP_001246.1.
            
            Summary: CDC20 appears to act as a regulatory protein interacting
            with several other proteins at multiple points in the cell cycle.
            It is required for two microtubule-dependent processes, nuclear
            movement prior to anaphase and chromosome separation. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001088.2, U05340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310955.11/ ENSP00000308450.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.2"
     Protein         1..499
                     /product="cell division cycle protein 20 homolog"
                     /note="CDC20 cell division cycle 20 homolog; fizzy
                     homolog"
                     /calculated_mol_wt=54592
     Region          17..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15525512,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:22014574; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            72
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15525512; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15525512; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15525512; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            157
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:15525512; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15525512; propagated from
                     UniProtKB/Swiss-Prot (Q12834.2)"
     Region          182..221
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          188..224
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <190..471
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          224..263
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          229..266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          266..303
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          272..307
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          307..346
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          312..352
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          353..395
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          359..397
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          397..438
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     Region          402..440
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          441..480
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12834.2)"
     CDS             1..499
                     /gene="CDC20"
                     /gene_synonym="bA276H19.3; CDC20A; OOMD14; OZEMA14;
                     p55CDC"
                     /coded_by="NM_001255.3:76..1575"
                     /db_xref="CCDS:CCDS484.1"
                     /db_xref="GeneID:991"
                     /db_xref="HGNC:HGNC:1723"
                     /db_xref="MIM:603618"
ORIGIN      
        1 maqfafesdl hsllqldapi pnapparwqr kakeaagpap spmraanrsh sagrtpgrtp
       61 gkssskvqtt pskpggdryi phrsaaqmev asfllskenq pensqtptkk ehqkawalnl
      121 ngfdveeaki lrlsgkpqna pegyqnrlkv lysqkatpgs srktcryips lpdrildape
      181 irndyylnlv dwssgnvlav aldnsvylws assgdilqll qmeqpgeyis svawikegny
      241 lavgtssaev qlwdvqqqkr lrnmtshsar vgslswnsyi lssgsrsghi hhhdvrvaeh
      301 hvatlsghsq evcglrwapd grhlasggnd nlvnvwpsap geggwvplqt ftqhqgavka
      361 vawcpwqsnv latgggtsdr hiriwnvcsg aclsavdahs qvcsilwsph ykelisghgf
      421 aqnqlviwky ptmakvaelk ghtsrvlslt mspdgatvas aaadetlrlw rcfeldparr
      481 rerekasaak sslihqgir
//
LOCUS       NP_116219                686 aa            linear   PRI 20-NOV-2025
DEFINITION  U3 small nucleolar RNA-associated protein 4 homolog isoform 1 [Homo
            sapiens].
ACCESSION   NP_116219
VERSION     NP_116219.2
DBSOURCE    REFSEQ: accession NM_032830.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 686)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 686)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 686)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 686)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 686)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 686)
  AUTHORS   Yu,B., Mitchell,G.A. and Richter,A.
  TITLE     Nucleolar localization of cirhin, the protein mutated in North
            American Indian childhood cirrhosis
  JOURNAL   Exp Cell Res 311 (2), 218-228 (2005)
   PUBMED   16225863
  REMARK    GeneRIF: Cirhin is a nucleolar protein and the R565W mutation, for
            which all North American Indian childhood cirrhosis patients are
            homozygous, has no effect on subcellular localization.
REFERENCE   7  (residues 1 to 686)
  AUTHORS   Carlton,V.E., Pawlikowska,L. and Bull,L.N.
  TITLE     Molecular basis of intrahepatic cholestasis
  JOURNAL   Ann Med 36 (8), 606-617 (2004)
   PUBMED   15768832
  REMARK    Review article
REFERENCE   8  (residues 1 to 686)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
  REMARK    GeneRIF: A missense mutation (R565W) in cirhin (FLJ14728) in North
            American Indian childhood cirrhosis
REFERENCE   9  (residues 1 to 686)
  AUTHORS   Drouin,E., Russo,P., Tuchweber,B., Mitchell,G. and Rasquin-Weber,A.
  TITLE     North American Indian cirrhosis in children: a review of 30 cases
  JOURNAL   J Pediatr Gastroenterol Nutr 31 (4), 395-404 (2000)
   PUBMED   11045837
REFERENCE   10 (residues 1 to 686)
  AUTHORS   Betard,C., Rasquin-Weber,A., Brewer,C., Drouin,E., Clark,S.,
            Verner,A., Darmond-Zwaig,C., Fortin,J., Mercier,J., Chagnon,P.,
            Fujiwara,T.M., Morgan,K., Richter,A., Hudson,T.J. and Mitchell,G.A.
  TITLE     Localization of a recessive gene for North American Indian
            childhood cirrhosis to chromosome region 16q22-and identification
            of a shared haplotype
  JOURNAL   Am J Hum Genet 67 (1), 222-228 (2000)
   PUBMED   10820129
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA277545.1 and BC009348.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 29, 2008 this sequence version replaced NP_116219.1.
            
            Summary: This gene encodes a WD40-repeat-containing protein that is
            localized to the nucleolus. Mutation of this gene causes North
            American Indian childhood cirrhosis, a severe intrahepatic
            cholestasis that results in transient neonatal jaundice, and
            progresses to periportal fibrosis and cirrhosis in childhood and
            adolescence. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1105789.1, AK027675.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314423.12/ ENSP00000327179.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..686
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..686
                     /product="U3 small nucleolar RNA-associated protein 4
                     homolog isoform 1"
                     /note="testis expressed gene 292; UTP4, small subunit
                     (SSU) processome component, homolog; cirrhosis, autosomal
                     recessive 1A (cirhin); UTP4 small subunit (SSU) processome
                     component; U3 small nucleolar RNA-associated protein 4
                     homolog"
                     /calculated_mol_wt=76759
     Region          <7..306
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          7..50
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          20..57
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          51..92
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          62..101
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          93..135
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          105..142
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          136..181
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          148..189
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..226
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          198..234
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..275
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          276..317
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          286..547
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          318..377
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          334..374
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          378..427
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          428..475
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          443..479
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          476..516
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          487..524
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          517..566
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          567..627
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     Region          628..666
                     /region_name="WD 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q969X6.1)"
     CDS             1..686
                     /gene="UTP4"
                     /gene_synonym="CIRH1A; CIRHIN; NAIC; TEX292"
                     /coded_by="NM_032830.3:44..2104"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10872.1"
                     /db_xref="GeneID:84916"
                     /db_xref="HGNC:HGNC:1983"
                     /db_xref="MIM:607456"
ORIGIN      
        1 mgefkvhrvr ffnyvpsgir cvaynnqsnr lavsrtdgtv eiynlsanyf qekffpghes
       61 ratealcwae gqrlfsagln geimeydlqa lnikyamdaf ggpiwsmaas psgsqllvgc
      121 edgsvklfqi tpdkiqfern fdrqksrils lswhpsgthi aagsidyisv fdvksgsavh
      181 kmivdrqymg vskrkcivwg vaflsdgtii svdsagkvqf wdsatgtlvk shlianadvq
      241 siavadqeds fvvgtaegtv fhfqlvpvts nssekqwvrt kpfqhhthdv rtvahsptal
      301 isggtdthlv frplmekvev knydaalrki tfphrclisc skkrqlllfq fahhlelwrl
      361 gstvatgkng dtlplsknad hllhlktkgp eniicscisp cgswiaystv srfflyrlny
      421 ehdnislkrv skmpaflrsa lqilfsedst klfvasnqga lhivqlsggs fkhlhafqpq
      481 sgtveamcll avspdgnwla asgtsagvhv ynvkqlklhc tvpaynfpvt amaiapntnn
      541 lviahsdqqv feysipdkqy tdwsrtvqkq gfhhlwlqrd tpithisfhp krpmhillhd
      601 aymfciidks lplpndktll ynpfpptnes dvirrrtaha fkiskiykpl lfmdlldert
      661 lvaverpldd iiaqlpppik kkkfgt
//
LOCUS       NP_003126                144 aa            linear   PRI 20-NOV-2025
DEFINITION  signal recognition particle 19 kDa protein isoform 1 [Homo
            sapiens].
ACCESSION   NP_003126
VERSION     NP_003126.1
DBSOURCE    REFSEQ: accession NM_003135.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Linder,M.I., Mizoguchi,Y., Hesse,S., Csaba,G., Tatematsu,M.,
            Lyszkiewicz,M., Zietara,N., Jeske,T., Hastreiter,M., Rohlfs,M.,
            Liu,Y., Grabowski,P., Ahomaa,K., Maier-Begandt,D., Schwestka,M.,
            Pazhakh,V., Isiaku,A.I., Briones Miranda,B., Blombery,P.,
            Saito,M.K., Rusha,E., Alizadeh,Z., Pourpak,Z., Kobayashi,M.,
            Rezaei,N., Unal,E., Hauck,F., Drukker,M., Walzog,B., Rappsilber,J.,
            Zimmer,R., Lieschke,G.J. and Klein,C.
  TITLE     Human genetic defects in SRP19 and SRPRA cause severe congenital
            neutropenia with distinctive proteome changes
  JOURNAL   Blood 141 (6), 645-658 (2023)
   PUBMED   36223592
  REMARK    GeneRIF: Human genetic defects in SRP19 and SRPRA cause severe
            congenital neutropenia with distinctive proteome changes.
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Kellogg,M.K., Miller,S.C., Tikhonova,E.B. and Karamyshev,A.L.
  TITLE     SRPassing Co-translational Targeting: The Role of the Signal
            Recognition Particle in Protein Targeting and mRNA Protection
  JOURNAL   Int J Mol Sci 22 (12), 6284 (2021)
   PUBMED   34208095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Becker,M.M., Lapouge,K., Segnitz,B., Wild,K. and Sinning,I.
  TITLE     Structures of human SRP72 complexes provide insights into SRP RNA
            remodeling and ribosome interaction
  JOURNAL   Nucleic Acids Res 45 (1), 470-481 (2017)
   PUBMED   27899666
  REMARK    GeneRIF: The crystal structures of the SRP68 protein-binding domain
            (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the
            SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions
            of SRP72 within SRP have been presented.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Politz,J.C., Yarovoi,S., Kilroy,S.M., Gowda,K., Zwieb,C. and
            Pederson,T.
  TITLE     Signal recognition particle components in the nucleolus
  JOURNAL   Proc Natl Acad Sci U S A 97 (1), 55-60 (2000)
   PUBMED   10618370
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Gowda,K., Chittenden,K. and Zwieb,C.
  TITLE     Binding site of the M-domain of human protein SRP54 determined by
            systematic site-directed mutagenesis of signal recognition particle
            RNA
  JOURNAL   Nucleic Acids Res 25 (2), 388-394 (1997)
   PUBMED   9016569
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Joslyn,G., Carlson,M., Thliveris,A., Albertsen,H., Gelbert,L.,
            Samowitz,W., Groden,J., Stevens,J., Spirio,L., Robertson,M. et al.
  TITLE     Identification of deletion mutations and three new genes at the
            familial polyposis locus
  JOURNAL   Cell 66 (3), 601-613 (1991)
   PUBMED   1678319
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Groden,J., Thliveris,A., Samowitz,W., Carlson,M., Gelbert,L.,
            Albertsen,H., Joslyn,G., Stevens,J., Spirio,L., Robertson,M. et al.
  TITLE     Identification and characterization of the familial adenomatous
            polyposis coli gene
  JOURNAL   Cell 66 (3), 589-600 (1991)
   PUBMED   1651174
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Lingelbach,K., Zwieb,C., Webb,J.R., Marshallsay,C., Hoben,P.J.,
            Walter,P. and Dobberstein,B.
  TITLE     Isolation and characterization of a cDNA clone encoding the 19 kDa
            protein of signal recognition particle (SRP): expression and
            binding to 7SL RNA
  JOURNAL   Nucleic Acids Res 16 (20), 9431-9442 (1988)
   PUBMED   2460823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008575.7, X12791.1, AW890522.1, CN265235.1 and AA845342.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.134293.1,
                                           SRR1660807.128387.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000505459.6/ ENSP00000424870.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..144
                     /product="signal recognition particle 19 kDa protein
                     isoform 1"
                     /EC_number="3.6.5.4"
                     /note="signal recognition particle 19 kDa protein; signal
                     recognition particle 19kD; signal recognition particle
                     19kDa"
                     /calculated_mol_wt=16025
     Region          17..115
                     /region_name="SRP19"
                     /note="SRP19 protein; pfam01922"
                     /db_xref="CDD:460383"
     Region          117..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09132.3)"
     CDS             1..144
                     /gene="SRP19"
                     /coded_by="NM_003135.3:91..525"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4108.1"
                     /db_xref="GeneID:6728"
                     /db_xref="HGNC:HGNC:11300"
                     /db_xref="MIM:182175"
ORIGIN      
        1 macaaarspa dqdrficiyp aylnnkktia egrripiska venptateiq dvcsavglnv
       61 fleknkmysr ewnrdvqyrg rvrvqlkqed gslclvqfps rksvmlyaae mipklktrtq
      121 ktggadqslq qgegskkgkg kkkk
//
LOCUS       NP_001341834            2683 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform l [Homo sapiens].
ACCESSION   NP_001341834
VERSION     NP_001341834.1
DBSOURCE    REFSEQ: accession NM_001354905.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2683)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2683)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2683)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2683)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2683)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2683)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2683)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2683)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2683)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2683)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2015133.1,
                                           SRR18074968.2982772.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2683
                     /product="adenomatous polyposis coli protein isoform l"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=293649
     Region          68..148
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <248..306
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          305..348
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(339,343,347,382,386,390,426,430,434)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          352..393
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          356..393
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          400..435
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          443..484
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          489..529
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          493..527
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          531..571
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          535..571
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          572..859
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          876..975
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1097..>1114
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1123..1208
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1131..1541
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1211..1233
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1477..1500
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1502..1555
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1556..1577
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1586..1679
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1713..1787
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1873..1892
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2063..2408
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2510..2683
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2683
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354905.2:84..8135"
                     /note="isoform l is encoded by transcript variant 14"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 massgqidll erlkelnlds snfpgvklrs kmslrsygsr egsvssrsge cspvpmgsfp
       61 rrgfvngsre stgyleelek ersllladld keekekdwyy aqlqnltkri dslpltenfs
      121 lqtdmtrrql eyearqirva meeqlgtcqd mekraqrria riqqiekdil rirqllqsqa
      181 teaerssqnk hetgshdaer qnegqgvgei nmatsgngqg sttrmdheta svlssssths
      241 aprrltshlg tkiraycetc wewqeahepg mdqdknpmpa pvehqicpav cvlmklsfde
      301 ehrhamnelg glqaiaellq vdcemygltn dhysitlrry agmaltnltf gdvankatlc
      361 smkgcmralv aqlksesedl qqviasvlrn lswradvnsk ktlrevgsvk almecalevk
      421 kestlksvls alwnlsahct enkadicavd galaflvgtl tyrsqtntla iiesgggilr
      481 nvssliatne dhrqilrenn clqtllqhlk shsltivsna cgtlwnlsar npkdqealwd
      541 mgavsmlknl ihskhkmiam gsaaalrnlm anrpakykda nimspgsslp slhvrkqkal
      601 eaeldaqhls etfdnidnls pkashrskqr hkqslygdyv fdtnrhddnr sdnfntgnmt
      661 vlspylnttv lpsssssrgs ldssrsekdr slerergigl gnyhpatenp gtsskrglqi
      721 sttaaqiakv meevsaihts qedrssgstt elhcvtdern alrrssaaht hsntynftks
      781 ensnrtcsmp yakleykrss ndslnsvsss dgygkrgqmk psiesysedd eskfcsygqy
      841 padlahkihs anhmddndge ldtpinyslk ysdeqlnsgr qspsqnerwa rpkhiiedei
      901 kqseqrqsrn qsttypvyte stddkhlkfq phfgqqecvs pyrsrgangs etnrvgsnhg
      961 inqnvsqslc qeddyeddkp tnyserysee eqheeeerpt nysikyneek rhvdqpidys
     1021 lkyatdipss qkqsfsfsks ssgqsskteh mssssentst pssnakrqnq lhpssaqsrs
     1081 gqpqkaatck vssinqetiq tycvedtpic fsrcsslssl ssaedeigcn qttqeadsan
     1141 tlqiaeikek igtrsaedpv sevpavsqhp rtkssrlqgs slssesarhk avefssgaks
     1201 psksgaqtpk sppehyvqet plmfsrctsv ssldsfesrs iassvqsepc sgmvsgiisp
     1261 sdlpdspgqt mppsrsktpp pppqtaqtkr evpknkapta ekresgpkqa avnaavqrvq
     1321 vlpdadtllh fatestpdgf scssslsals ldepfiqkdv elrimppvqe ndngnetese
     1381 qpkesnenqe keaektidse kdllddsddd dieileecii samptkssrk akkpaqtask
     1441 lpppvarkps qlpvykllps qnrlqpqkhv sftpgddmpr vycvegtpin fstatslsdl
     1501 tiesppnela agegvrggaq sgefekrdti ptegrstdea qggktssvti pelddnkaee
     1561 gdilaecins ampkgkshkp frvkkimdqv qqasasssap nknqldgkkk kptspvkpip
     1621 qnteyrtrvr knadsknnln aervfsdnkd skkqnlknns kvfndklpnn edrvrgsfaf
     1681 dsphhytpie gtpycfsrnd slssldfddd dvdlsrekae lrkakenkes eakvtshtel
     1741 tsnqqsankt qaiakqpinr gqpkpilqkq stfpqsskdi pdrgaatdek lqnfaientp
     1801 vcfshnssls slsdidqenn nkenepiket eppdsqgeps kpqasgyapk sfhvedtpvc
     1861 fsrnsslssl sidseddllq ecissampkk kkpsrlkgdn ekhsprnmgg ilgedltldl
     1921 kdiqrpdseh glspdsenfd wkaiqegans ivsslhqaaa aaclsrqass dsdsilslks
     1981 gislgspfhl tpdqeekpft snkgprilkp gekstletkk ieseskgikg gkkvykslit
     2041 gkvrsnseis gqmkqplqan mpsisrgrtm ihipgvrnss sstspvskkg pplktpasks
     2101 psegqtatts prgakpsvks elspvarqts qiggsskaps rsgsrdstps rpaqqplsrp
     2161 iqspgrnsis pgrngisppn klsqlprtss pstastkssg sgkmsytspg rqmsqqnltk
     2221 qtglsknass iprsesaskg lnqmnngnga nkkvelsrms stkssgsesd rserpvlvrq
     2281 stfikeapsp tlrrkleesa sfeslspssr pasptrsqaq tpvlspslpd mslsthssvq
     2341 aggwrklppn lsptieyndg rpakrhdiar shsespsrlp inrsgtwkre hskhssslpr
     2401 vstwrrtgss ssilsasses sekaksedek hvnsisgtkq skenqvsakg twrkikenef
     2461 sptnstsqtv ssgatngaes ktliyqmapa vsktedvwvr iedcpinnpr sgrsptgntp
     2521 pvidsvseka npnikdskdn qakqnvgngs vpmrtvglen rlnsfiqvda pdqkgteikp
     2581 gqnnpvpvse tnessivert pfsssssskh sspsgtvaar vtpfnynpsp rkssadstsa
     2641 rpsqiptpvn nntkkrdskt dstessgtqs pkrhsgsylv tsv
//
LOCUS       NP_001340924             571 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001340924
VERSION     NP_001340924.1
DBSOURCE    REFSEQ: accession NM_001353995.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (9), as well as variants 5-8 and
            10, encodes isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.221260.1,
                                           SRR1803615.157976.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMN03465404
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..571
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 5"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=65207
     Region          13..112
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          129..455
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     CDS             1..571
                     /gene="MTMR1"
                     /coded_by="NM_001353995.1:180..1895"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 meeaplfpge sikaivkdvm yicpfmgavs gtltvtdfkl yfknverdph fildvplgvi
       61 srvekigaqs hgdnscgiei vckdmrnlrl aykqeeqskl gifenlnkha fplsngqalf
      121 afsykekfpi ngwkvydpvs eykrqglpne swkiskinsn yefcdtypai ivvptsvkdd
      181 dlskvaafra kgrvpvlswi hpesqatitr csqplvgpnd krckedekyl qtimdanaqs
      241 hkliifdarq nsvadtnktk gggyesesay pnaelvflei hnihvmresl rklkeivyps
      301 idearwlsnv dgthwleyir mllagavria dkiesgktsv vvhcsdgwdr taqltslaml
      361 mldsyyrtik gfetlvekew isfghrfalr vghgndnhad adrspiflqf vdcvwqmtrq
      421 fpsafefnel flitildhly sclfgtflcn ceqqrfkedv ytktislwsy insqldefsn
      481 pffvnyenhv lypvaslshl elwvnyyvrw nprmrpqmpi hqnlkellav raelqkrveg
      541 lqrevatrav ssssergssp shsatsvhts v
//
LOCUS       NP_001171668             338 aa            linear   PRI 20-NOV-2025
DEFINITION  testis-specific serine/threonine-protein kinase 4 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001171668
VERSION     NP_001171668.1
DBSOURCE    REFSEQ: accession NM_001184739.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Peng,J., Sun,A., Zheng,J., Zhang,N., Zhang,X. and Gao,G.
  TITLE     Testis-specific serine/threonine kinase dTSSK2 regulates sperm
            motility and male fertility in Drosophila
  JOURNAL   Commun Biol 8 (1), 710 (2025)
   PUBMED   40335644
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Shen,Y., Zhang,F., Li,F., Jiang,X., Yang,Y., Li,X., Li,W., Wang,X.,
            Cheng,J., Liu,M., Zhang,X., Yuan,G., Pei,X., Cai,K., Hu,F., Sun,J.,
            Yan,L., Tang,L., Jiang,C., Tu,W., Xu,J., Wu,H., Kong,W., Li,S.,
            Wang,K., Sheng,K., Zhao,X., Yue,H., Yang,X. and Xu,W.
  TITLE     Loss-of-function mutations in QRICH2 cause male infertility with
            multiple morphological abnormalities of the sperm flagella
  JOURNAL   Nat Commun 10 (1), 433 (2019)
   PUBMED   30683861
  REMARK    Erratum:[Nat Commun. 2019 May 20;10(1):2289. doi:
            10.1038/s41467-019-10313-x. PMID: 31110204]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Wang,X.L., Wei,Y.H., Fu,G.L. and Yu,L.
  TITLE     Testis specific serine/threonine protein kinase 4 (TSSK4) leads to
            cell apoptosis relying on its kinase activity
  JOURNAL   J Huazhong Univ Sci Technolog Med Sci 35 (2), 235-240 (2015)
   PUBMED   25877358
  REMARK    GeneRIF: TSSK4 was able to induce cell apoptosis in vitro depending
            on its kinase activity, which leads to abnormal testes weight and
            apoptosis, shedding light on its function in the process of
            spermatogenesis and/or spermiogenesis
REFERENCE   4  (residues 1 to 338)
  AUTHORS   Wang,X., Wei,Y., Fu,G., Li,H., Saiyin,H., Lin,G., Wang,Z., Chen,S.
            and Yu,L.
  TITLE     Tssk4 is essential for maintaining the structural integrity of
            sperm flagellum
  JOURNAL   Mol Hum Reprod 21 (2), 136-145 (2015)
   PUBMED   25361759
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Aston,K.I., Krausz,C., Laface,I., Ruiz-Castane,E. and Carrell,D.T.
  TITLE     Evaluation of 172 candidate polymorphisms for association with
            oligozoospermia or azoospermia in a large cohort of men of European
            descent
  JOURNAL   Hum Reprod 25 (6), 1383-1397 (2010)
   PUBMED   20378615
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Su,D., Zhang,W., Yang,Y., Deng,Y., Ma,Y., Song,H. and Zhang,S.
  TITLE     Mutation screening and association study of the TSSK4 Gene in
            Chinese infertile men with impaired spermatogenesis
  JOURNAL   J Androl 29 (4), 374-378 (2008)
   PUBMED   18390560
  REMARK    GeneRIF: association of some single nucleotide polymorphisms in
            TSSK4 with male infertility.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Zeng,M., Deng,W., Wang,X., Qiu,W., Liu,Y., Sun,H., Tao,D., Zhang,S.
            and Ma,Y.
  TITLE     DAZL binds to the transcripts of several Tssk genes in germ cells
  JOURNAL   BMB Rep 41 (4), 300-304 (2008)
   PUBMED   18452650
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Chen,X., Lin,G., Wei,Y., Hexige,S., Niu,Y., Liu,L., Yang,C. and
            Yu,L.
  TITLE     TSSK5, a novel member of the testis-specific serine/threonine
            kinase family, phosphorylates CREB at Ser-133, and stimulates the
            CRE/CREB responsive pathway
  JOURNAL   Biochem Biophys Res Commun 333 (3), 742-749 (2005)
   PUBMED   15964553
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136295.3, AK131042.1 and
            AY461663.1.
            
            Summary: This gene encodes a member of the testis-specific
            serine/threonine kinase family. The encoded protein is thought to
            be involved in spermatogenesis via stimulation of the CREB/CRE
            responsive pathway through phosphorylation of the cAMP responsive
            element binding protein transcription factor. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, May
            2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK131042.1, SRR5189667.180041.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339917.10/ ENSP00000339179.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..338
                     /product="testis-specific serine/threonine-protein kinase
                     4 isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 22E;
                     serine/threonine-protein kinase 22E"
                     /calculated_mol_wt=38308
     Region          24..303
                     /region_name="STKc_TSSK4-like"
                     /note="Catalytic domain of testis-specific
                     serine/threonine kinase 4 and similar proteins; cd14162"
                     /db_xref="CDD:271064"
     Site            order(31..35,39,52,54,86,102..105,109,111..112,114,
                     157..158,160,162..163,165,175..176,179,209..213,215,
                     245..248)
                     /site_type="active"
                     /db_xref="CDD:271064"
     Site            order(31..34,39,52,54,86,102..105,109,162..163,165,
                     175..176)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271064"
     Site            order(109,111..112,114,158,160,162,179,209..213,215,
                     245..248)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271064"
     Site            order(175..186,203..213)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271064"
     CDS             1..338
                     /gene="TSSK4"
                     /gene_synonym="C14orf20; STK22E; TSK-4; TSK4; TSSK5"
                     /coded_by="NM_001184739.2:229..1245"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS53890.1"
                     /db_xref="GeneID:283629"
                     /db_xref="HGNC:HGNC:19825"
                     /db_xref="MIM:610711"
ORIGIN      
        1 mgkgdvleaa ptttayhslm deygyevgka ighgsygsvy eafytkqkvm vavkiiskkk
       61 asddylnkfl preiqvmkvl rhkylinfyr aiestsrvyi ilelaqggdv lewiqrygac
      121 seplagkwfs qltlgiaylh sksivhrlmp slsaagrdlk lenllldkwe nvkisdfgfa
      181 kmvpsnqpvg cspsyrqvnc fshlsqtycg sfayacpeil rglpynpfls dtwsmgvily
      241 tlvvahlpfd dtnlkkllre tqkevtfpan htisqecknl ilqmlrqatk ratildiikd
      301 swvlkfqpeq ptheirllea mcqlhnttkq hqslqitt
//
LOCUS       NP_001355738             825 aa            linear   PRI 20-NOV-2025
DEFINITION  AMP deaminase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001355738 NP_001244289
VERSION     NP_001355738.1
DBSOURCE    REFSEQ: accession NM_001368809.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Flores-Mendez,M., Ohl,L., Roule,T., Zhou,Y., Tintos-Hernandez,J.A.,
            Walsh,K., Ortiz-Gonzalez,X.R. and Akizu,N.
  TITLE     IMPDH2 filaments protect from neurodegeneration in AMPD2 deficiency
  JOURNAL   EMBO Rep 25 (9), 3990-4012 (2024)
   PUBMED   39075237
  REMARK    GeneRIF: IMPDH2 filaments protect from neurodegeneration in AMPD2
            deficiency.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Gilboa,T., Elefant,N., Meiner,V. and Hacohen,N.
  TITLE     Delineating the phenotype and genetic basis of AMPD2-related
            pontocerebellar hypoplasia
  JOURNAL   Neurogenetics 24 (1), 61-66 (2023)
   PUBMED   36445597
  REMARK    GeneRIF: Delineating the phenotype and genetic basis of
            AMPD2-related pontocerebellar hypoplasia.
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Van den Bergh,F. and Sabina,R.L.
  TITLE     Characterization of human AMP deaminase 2 (AMPD2) gene expression
            reveals alternative transcripts encoding variable N-terminal
            extensions of isoform L
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 401-410 (1995)
   PUBMED   8526848
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Mahnke-Zizelman,D.K. and Sabina,R.L.
  TITLE     Cloning of human AMP deaminase isoform E cDNAs. Evidence for a
            third AMPD gene exhibiting alternatively spliced 5'-exons
  JOURNAL   J Biol Chem 267 (29), 20866-20877 (1992)
   PUBMED   1400401
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355310.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 1, 2019 this sequence version replaced NP_001244289.1.
            
            Summary: The protein encoded by this gene is important in purine
            metabolism by converting AMP to IMP. The encoded protein, which
            acts as a homotetramer, is one of three AMP deaminases found in
            mammals. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longest isoform (1). Variants 1 and 4
            both encode the same isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314494.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: lack of evidence for use of
                                                upstream AUG
            MANE Ensembl match               :: ENST00000528667.7/
                                                ENSP00000436541.2
            RefSeq Select criteria           :: based on manual assertion,
                                                conservation, expression,
                                                longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..825
                     /product="AMP deaminase 2 isoform 1"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L);
                     AMP deaminase 2"
                     /calculated_mol_wt=94759
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01433.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            45
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Region          163..806
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..825
                     /gene="AMPD2"
                     /gene_synonym="AMPD; PCH9; SPG63"
                     /coded_by="NM_001368809.2:705..3182"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS805.2"
                     /db_xref="GeneID:271"
                     /db_xref="HGNC:HGNC:469"
                     /db_xref="MIM:102771"
ORIGIN      
        1 masypsgsgk pkakypfkkr aslqastaap eargglgapp lqsarslpgp apclkhfpld
       61 lrtsmdgkck eiaeelftrs laeselrsap yefpeespie qleerrqrle rqisqdvkle
      121 pdillrakqd flktdsdsdl qlykeqgegq gdrslrerdv lerefqrvti sgeekcgvpf
      181 tdlldaaksv vralfireky malslqsfcp ttrrylqqla ekpletrtye qgpdtpvsad
      241 apvhppaleq hpyehcepst mpgdlglglr mvrgvvhvyt rrepdehcse velpypdlqe
      301 fvadvnvlma liingpiksf cyrrlqylss kfqmhvllne mkelaaqkkv phrdfynirk
      361 vdthihassc mnqkhllrfi kramkrhlee ivhveqgreq tlrevfesmn ltaydlsvdt
      421 ldvhadrntf hrfdkfnaky npigesvlre ifiktdnrvs gkyfahiike vmsdleesky
      481 qnaelrlsiy grsrdewdkl arwavmhrvh spnvrwlvqv prlfdvyrtk gqlanfqeml
      541 eniflplfea tvhpashpel hlflehvdgf dsvddeskpe nhvfnlespl peawveednp
      601 pyayylyytf anmamlnhlr rqrgfhtfvl rphcgeagpi hhlvsafmla enishglllr
      661 kapvlqylyy laqigiamsp lsnnslflsy hrnplpeyls rglmvslstd dplqfhftke
      721 plmeeysiat qvwklsscdm celarnsvlm sgfshkvksh wlgpnytkeg pegndirrtn
      781 vpdirvgyry etlcqelali tqavqsemle tipeeagitm spgpq
//
LOCUS       NP_001356034             318 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 12 [Homo
            sapiens].
ACCESSION   NP_001356034
VERSION     NP_001356034.1
DBSOURCE    REFSEQ: accession NM_001369105.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 318)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.48188.1,
                                           SRR1803617.229409.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..318
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 12"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=36303
     Region          20..85
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(29,31..33,35..39,42..43,46..47,52..55)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          94..317
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..318
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369105.1:319..1275"
                     /note="isoform 12 is encoded by transcript variant 26"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mecadepcda yeveqtpqgf rstlrapsll ykhivgkrgd trkkiemetk tsisipkpgq
       61 dgeivitgqh rngvisartr idvlldtfrr kqpfthflaf flnevevqeg flrfqeevla
      121 kcsmdhgvds sifqnpkklh ltigmlvlls eeeiqqtcem lqqckeefin disggkplev
      181 emagieymnd dpgmvdvlya kvhmkdgsnr lqelvdrvle rfqasglivk ewnsvklhat
      241 vmntlfrkdp naegrynlyt aegkyifker esfdgrnilk lfenfyfgsl klnsihisqr
      301 ftvdsfgnya scgqidfs
//
LOCUS       NP_079223                995 aa            linear   PRI 20-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_079223
VERSION     NP_079223.3
DBSOURCE    REFSEQ: accession NM_024947.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 995)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 995)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 995)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 995)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 995)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 995)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 995)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 995)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 995)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 995)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP200133.1, BC131772.1, AC008040.7 and BC026001.1.
            
            On Jun 6, 2007 this sequence version replaced NP_079223.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.135168.1,
                                           SRR1803617.7470.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000495893.7/ ENSP00000420294.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..995
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..995
                     /product="polyhomeotic-like protein 3 isoform 1"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=107349
     Region          <358..>518
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          926..994
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(944..945,979..980,983..984,987)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(955..959,961..962,965..966,970,975)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..995
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_024947.4:19..3006"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46952.1"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 maeaefkdhs tamdtepnpg tssvstttss tttttittss srmqqpqisv ysgsdrhavq
       61 viqqalhrpp ssaaqylqqm yaaqqqhlml htaalqqqhl sssqlqslaa vqaslssgrp
      121 stsptgsvtq qssmsqtsin lstsptpaql isrsqassst sgsitqqtml lgstsptlta
      181 sqaqmylraq mliftpattv aavqsdipvv ssssssscqs aatqvqnltl rsqklgvlss
      241 sqngppksts qtqsltichn kttvtsskis qrdpspesnk kgespslesr stavtrtssi
      301 hqliapasys piqphslikh qqiplhspps kvshhqlilq qqqqqiqpit lqnstqdppp
      361 sqhciplqnh glppapsnaq sqhcspiqsh pspltvspnq sqsaqqsvvv spppphspsq
      421 sptiiihpqa liqphplvss alqpgpnlqq stanqvqata qlnlpshlpl paspvvhigp
      481 vqqsalvspg qqivspshqq ysslqsspip iasppqmsts ppaqipplpl qsmqslqvqp
      541 eilsqgqvlv qnalvseeel paaealvqlp fqtlpppqtv avnlqvqppa pvdppvvyqv
      601 edvceeempe esdecvrmdr tpppptlspa aitvgrgedl tsehplleqv elpavasvsa
      661 svikspsdps hvsvppppll lpaattrsns tsmhssipsi enkppqaivk pqilthvieg
      721 fviqeglepf pvsrssllie qpvkkrplld nqvinsvcvq pelqnntkha dnssdtemed
      781 miaeetleem dsellkcefc gkmgyanefl rskrfctmsc akrynvscsk kfalsrwnrk
      841 pdnqslghrg rrpsgpdgaa rehilrqlpi typsaeedla shedsvpsam ttrlrrqser
      901 ererelrdvr irkmpensdl lpvaqtepsi wtvddvwafi hslpgcqdia defraqeidg
      961 qallllkedh lmsamniklg palkicarin slkes
//
LOCUS       NP_000610                166 aa            linear   PRI 20-NOV-2025
DEFINITION  interferon gamma precursor [Homo sapiens].
ACCESSION   NP_000610
VERSION     NP_000610.2
DBSOURCE    REFSEQ: accession NM_000619.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Hanin,A., Comi,M., Sumida,T.S. and Hafler,D.A.
  TITLE     Cholesterol promotes IFNG mRNA expression in CD4+ effector/memory
            cells by SGK1 activation
  JOURNAL   Life Sci Alliance 7 (12), e202402890 (2024)
   PUBMED   39366761
  REMARK    GeneRIF: Cholesterol promotes IFNG mRNA expression in CD4[+]
            effector/memory cells by SGK1 activation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Hautala,N.M., Joensuu,M., Paakkola,T., Glumoff,V., Kettunen,K.,
            Saarela,J., Siiskonen,M., Chen,Z., Pylkas,K. and Hautala,T.
  TITLE     Recurrent ocular toxoplasmosis is associated with interferon-gamma
            deficiency possibly due to genetic origin
  JOURNAL   BMJ Open Ophthalmol 9 (1), e001769 (2024)
   PUBMED   39277179
  REMARK    GeneRIF: Recurrent ocular toxoplasmosis is associated with
            interferon-gamma deficiency possibly due to genetic origin.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Walter,M.R., Windsor,W.T., Nagabhushan,T.L., Lundell,D.J.,
            Lunn,C.A., Zauodny,P.J. and Narula,S.K.
  TITLE     Crystal structure of a complex between interferon-gamma and its
            soluble high-affinity receptor
  JOURNAL   Nature 376 (6537), 230-235 (1995)
   PUBMED   7617032
REFERENCE   6  (residues 1 to 166)
  AUTHORS   Emilie,D., Maillot,M.C., Nicolas,J.F., Fior,R. and Galanaud,P.
  TITLE     Antagonistic effect of interferon-gamma on tat-induced
            transactivation of HIV long terminal repeat
  JOURNAL   J Biol Chem 267 (29), 20565-20570 (1992)
   PUBMED   1400376
REFERENCE   7  (residues 1 to 166)
  AUTHORS   Grzesiek,S., Dobeli,H., Gentz,R., Garotta,G., Labhardt,A.M. and
            Bax,A.
  TITLE     1H, 13C, and 15N NMR backbone assignments and secondary structure
            of human interferon-gamma
  JOURNAL   Biochemistry 31 (35), 8180-8190 (1992)
   PUBMED   1525157
REFERENCE   8  (residues 1 to 166)
  AUTHORS   Slodowski,O., Bohm,J., Schone,B. and Otto,B.
  TITLE     Carboxy-terminal truncated rhuIFN-gamma with a substitution of
            Gln133 or Ser132 to leucine leads to higher biological activity
            than in the wild type
  JOURNAL   Eur J Biochem 202 (3), 1133-1140 (1991)
   PUBMED   1662603
REFERENCE   9  (residues 1 to 166)
  AUTHORS   Gray,P.W. and Goeddel,D.V.
  TITLE     Structure of the human immune interferon gene
  JOURNAL   Nature 298 (5877), 859-863 (1982)
   PUBMED   6180322
REFERENCE   10 (residues 1 to 166)
  AUTHORS   Devos,R., Cheroutre,H., Taya,Y., Degrave,W., Van Heuverswyn,H. and
            Fiers,W.
  TITLE     Molecular cloning of human immune interferon cDNA and its
            expression in eukaryotic cells
  JOURNAL   Nucleic Acids Res 10 (8), 2487-2501 (1982)
   PUBMED   6176945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC070256.1, V00543.1 and
            AC007458.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 22, 2004 this sequence version replaced NP_000610.1.
            
            Summary: This gene encodes a soluble cytokine that is a member of
            the type II interferon class. The encoded protein is secreted by
            cells of both the innate and adaptive immune systems. The active
            protein is a homodimer that binds to the interferon gamma receptor
            which triggers a cellular response to viral and microbial
            infections. Mutations in this gene are associated with an increased
            susceptibility to viral, bacterial and parasitic infections and to
            several autoimmune diseases. [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070256.1, SRR1163655.241293.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in cytokine storm inflammatory
                                      response
            MANE Ensembl match     :: ENST00000229135.4/ ENSP00000229135.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q15"
     Protein         1..166
                     /product="interferon gamma precursor"
                     /note="IFN-gamma; immune interferon"
                     /calculated_mol_wt=16776
     sig_peptide     1..23
                     /note="/evidence=ECO:0000269|PubMed:3109913,
                     ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
                     /calculated_mol_wt=2590
     Region          15..152
                     /region_name="IFN-gamma"
                     /note="Interferon gamma; pfam00714"
                     /db_xref="CDD:395581"
     mat_peptide     24..161
                     /product="Interferon gamma. /id=PRO_0000016444"
                     /note="propagated from UniProtKB/Swiss-Prot (P01579.1)"
                     /calculated_mol_wt=16178
     Site            24
                     /site_type="pyrrolidone-carboxylic-acid"
                     /note="Pyrrolidone carboxylic acid.
                     /evidence=ECO:0000269|PubMed:3109913,
                     ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Site            48
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine, in dimeric form.
                     /evidence=ECO:0000269|PubMed:6427223; propagated from
                     UniProtKB/Swiss-Prot (P01579.1)"
     Region          147..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01579.1)"
     CDS             1..166
                     /gene="IFNG"
                     /gene_synonym="IFG; IFI; IMD69"
                     /coded_by="NM_000619.3:126..626"
                     /db_xref="CCDS:CCDS8980.1"
                     /db_xref="GeneID:3458"
                     /db_xref="HGNC:HGNC:5438"
                     /db_xref="MIM:147570"
ORIGIN      
        1 mkytsyilaf qlcivlgslg cycqdpyvke aenlkkyfna ghsdvadngt lflgilknwk
       61 eesdrkimqs qivsfyfklf knfkddqsiq ksvetikedm nvkffnsnkk krddfekltn
      121 ysvtdlnvqr kaiheliqvm aelspaaktg krkrsqmlfr grrasq
//
LOCUS       NP_006271                173 aa            linear   PRI 20-NOV-2025
DEFINITION  translocon-associated protein subunit delta isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_006271
VERSION     NP_006271.1
DBSOURCE    REFSEQ: accession NM_006280.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Castiglioni,C., Feillet,F., Barnerias,C., Wiedemann,A., Muchart,J.,
            Cortes,F., Hernando-Davalillo,C., Montero,R., Dupre,T., Bruneel,A.,
            Seta,N., Vuillaumier-Barrot,S. and Serrano,M.
  TITLE     Expanding the phenotype of X-linked SSR4-CDG: Connective tissue
            implications
  JOURNAL   Hum Mutat 42 (2), 142-149 (2021)
   PUBMED   33300232
  REMARK    GeneRIF: Expanding the phenotype of X-linked SSR4-CDG: Connective
            tissue implications.
REFERENCE   3  (residues 1 to 173)
  AUTHORS   Ng,B.G., Raymond,K., Kircher,M., Buckingham,K.J., Wood,T.,
            Shendure,J., Nickerson,D.A., Bamshad,M.J., Wong,J.T.,
            Monteiro,F.P., Graham,B.H., Jackson,S., Sparkes,R., Scheuerle,A.E.,
            Cathey,S., Kok,F., Gibson,J.B. and Freeze,H.H.
  CONSRTM   University of Washington Center for Mendelian Genomics
  TITLE     Expanding the Molecular and Clinical Phenotype of SSR4-CDG
  JOURNAL   Hum Mutat 36 (11), 1048-1051 (2015)
   PUBMED   26264460
  REMARK    GeneRIF: We now report eight affected males with either de novo (4)
            or inherited (4) loss of function mutations in SSR4.
REFERENCE   4  (residues 1 to 173)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   5  (residues 1 to 173)
  AUTHORS   Wang,Z. and VandeBerg,J.L.
  TITLE     Cloning and molecular characterization of a human ortholog of
            Monodelphis TRAPD in ultraviolet B-induced melanoma
  JOURNAL   Melanoma Res 14 (2), 107-114 (2004)
   PUBMED   15057039
  REMARK    GeneRIF: results of this study implicate TRAPD as a candidate gene
            with potential functions that might be associated with
            ultraviolet-induced melanomagenesis and metastasis
REFERENCE   6  (residues 1 to 173)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 173)
  AUTHORS   Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
  TITLE     Genomic organization of two novel genes on human Xq28: compact head
            to head arrangement of IDH gamma and TRAP delta is conserved in rat
            and mouse
  JOURNAL   Genomics 44 (1), 8-14 (1997)
   PUBMED   9286695
REFERENCE   8  (residues 1 to 173)
  AUTHORS   Holthuis,J.C., van Riel,M.C. and Martens,G.J.
  TITLE     Translocon-associated protein TRAP delta and a novel TRAP-like
            protein are coordinately expressed with pro-opiomelanocortin in
            Xenopus intermediate pituitary
  JOURNAL   Biochem J 312 (Pt 1) (Pt 1), 205-213 (1995)
   PUBMED   7492314
REFERENCE   9  (residues 1 to 173)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 173)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z69043.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the delta subunit of the
            translocon-associated protein complex which is involved in
            translocating proteins across the endoplasmic reticulum membrane.
            The encoded protein is located in the Xq28 region and is arranged
            in a compact head-to-head manner with the isocitrate dehydrogenase
            3 (NAD+) gamma gene and both genes are driven by a CpG-embedded
            bidirectional promoter. Alternate splicing results in multiple
            transcript variants.[provided by RefSeq, Mar 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.464713.1,
                                           SRR5189661.135353.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370086.8/ ENSP00000359103.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..173
                     /product="translocon-associated protein subunit delta
                     isoform 2 precursor"
                     /note="translocon-associated protein subunit delta;
                     SSR-delta; TRAP-delta; signal sequence receptor, delta"
                     /calculated_mol_wt=16766
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2251
     mat_peptide     24..173
                     /product="Translocon-associated protein subunit delta.
                     /id=PRO_0000033292"
                     /note="propagated from UniProtKB/Swiss-Prot (P51571.1)"
                     /calculated_mol_wt=16766
     Region          24..172
                     /region_name="TRAP-delta"
                     /note="Translocon-associated protein, delta subunit
                     precursor (TRAP-delta); pfam05404"
                     /db_xref="CDD:398850"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P51571.1)"
     CDS             1..173
                     /gene="SSR4"
                     /gene_synonym="CDG1Y; TRAPD"
                     /coded_by="NM_006280.3:21..542"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS14731.1"
                     /db_xref="GeneID:6748"
                     /db_xref="HGNC:HGNC:11326"
                     /db_xref="MIM:300090"
ORIGIN      
        1 maamaslgal allllsslsr csaeaclepq itpsyyttsd avistetvfi veisltcknr
       61 vqnmalyadv ggkqfpvtrg qdvgryqvsw sldhksahag tyevrffdee sysllrkaqr
      121 nnedisiipp lftvsvdhrg twngpwvste vlaaaiglvi yylafsaksh iqa
//
LOCUS       NP_001008564             587 aa            linear   PRI 20-NOV-2025
DEFINITION  nucleoporin p58/p45 isoform b [Homo sapiens].
ACCESSION   NP_001008564
VERSION     NP_001008564.1
DBSOURCE    REFSEQ: accession NM_001008564.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Targa,A., Larrimore,K.E., Wong,C.K., Chong,Y.L., Fung,R., Lee,J.,
            Choi,H. and Rancati,G.
  TITLE     Non-genetic and genetic rewiring underlie adaptation to hypomorphic
            alleles of an essential gene
  JOURNAL   EMBO J 40 (21), e107839 (2021)
   PUBMED   34528284
  REMARK    GeneRIF: Non-genetic and genetic rewiring underlie adaptation to
            hypomorphic alleles of an essential gene.
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Le Rouzic,E., Mousnier,A., Rustum,C., Stutz,F., Hallberg,E.,
            Dargemont,C. and Benichou,S.
  TITLE     Docking of HIV-1 Vpr to the nuclear envelope is mediated by the
            interaction with the nucleoporin hCG1
  JOURNAL   J Biol Chem 277 (47), 45091-45098 (2002)
   PUBMED   12228227
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Ben-Efraim,I. and Gerace,L.
  TITLE     Gradient of increasing affinity of importin beta for nucleoporins
            along the pathway of nuclear import
  JOURNAL   J Cell Biol 152 (2), 411-417 (2001)
   PUBMED   11266456
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Shiota,C., Coffey,J., Grimsby,J., Grippo,J.F. and Magnuson,M.A.
  TITLE     Nuclear import of hepatic glucokinase depends upon glucokinase
            regulatory protein, whereas export is due to a nuclear export
            signal sequence in glucokinase
  JOURNAL   J Biol Chem 274 (52), 37125-37130 (1999)
   PUBMED   10601273
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Buss,F. and Stewart,M.
  TITLE     Macromolecular interactions in the nucleoporin p62 complex of rat
            nuclear pores: binding of nucleoporin p54 to the rod domain of p62
  JOURNAL   J Cell Biol 128 (3), 251-261 (1995)
   PUBMED   7531196
  REMARK    GeneRIF: The human gene NUPL1 shares 87% sequence identity with rat
            nucleoporin p58.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP249090.1, BG330006.1,
            BC001104.2, AK025800.1, AF113020.1 and AL138958.18.
            
            Summary: This gene encodes a member of the nucleoporin family that
            shares 87% sequence identity with rat nucleoporin p58. The protein
            is localized to the nuclear rim and is a component of the nuclear
            pore complex (NPC). All molecules entering or leaving the nucleus
            either diffuse through or are actively transported by the NPC.
            Alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1, resulting in a shorter protein
            (isoform b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.213883.1,
                                           SRR1803614.250565.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..587
                     /product="nucleoporin p58/p45 isoform b"
                     /note="nucleoporin p58/p45; nucleoporin-like protein 1;
                     nucleoporin like 1; 58 kDa nucleoporin; nucleoporin 58kDa"
                     /calculated_mol_wt=59623
     Region          3..587
                     /region_name="Nucleoporin_FG2"
                     /note="Nucleoporin FG repeated region; pfam15967"
                     /db_xref="CDD:435043"
     CDS             1..587
                     /gene="NUP58"
                     /gene_synonym="NUP45; NUPL1; PRO2463"
                     /coded_by="NM_001008564.2:150..1913"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS31949.1"
                     /db_xref="GeneID:9818"
                     /db_xref="HGNC:HGNC:20261"
                     /db_xref="MIM:607615"
ORIGIN      
        1 mstgfsfgsg tlgsttvaag gtstggvfsf gtgassnpsv glnfgnlgst stpattsaps
       61 sgfgtglfgs kpatgftlgg tntgtpatts aattgfslgf nkpaasatpf alpitstsas
      121 gltlssalts tpaastgftl nnlggttatt ttastglslg galaglggsl fqstntgtsg
      181 lgqnalgltl gttaatstag neglggidfs sssdkksdkt gtrpedskal kdenlppvic
      241 qdvenlqkfv keqkqvqeei srmsskamlk vqedikalkq llslaangiq rntlnidklk
      301 ietaqelkna eialrtqktp pglqheyaap adyfrilvqq fevqlqqyrq qieelenhla
      361 tqannshitp qdlsmamqki yqtfvalaaq lqsihenvkv lkeqylgyrk mflgdavdvf
      421 etrraeakkw qntprvttgp tpfstmpnaa avamaatltq qqqpatgpqp slgvsfgtpf
      481 gsgigtglqs sglgssnlgg fgtssgfgcs ttgastfgfg ttnkpsgsls agfgssstsg
      541 fnfsnpgita sagltfgvsn pasagfgtgg qllqlkkppa gnkrgkr
//
LOCUS       NP_001354452             554 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 16 [Homo sapiens].
ACCESSION   NP_001354452
VERSION     NP_001354452.1
DBSOURCE    REFSEQ: accession NM_001367523.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 554)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 554)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 554)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 554)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 554)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 554)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 554)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 554)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 554)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 554)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.214633.1,
                                           SRR1803617.69158.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..554
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..554
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 16"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=61406
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          395..>450
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..554
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367523.1:95..1759"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kkrkssssvh
      361 lmepqttvvh natdgikgst escntttede dlkvrkqeii kiteqlieai nngdfeaytk
      421 icdpgltsfe pealgnlveg mdfhkfyfen rewvraadil lpaplplclc llltfssqlp
      481 tfplfdlraa lllcmlvplc pdgcrqaplk alllsskchs fcscfvavpv ttikltyflp
      541 gavayacnpn tlgg
//
LOCUS       NP_653260                215 aa            linear   PRI 20-NOV-2025
DEFINITION  T-complex protein 10A homolog 1 [Homo sapiens].
ACCESSION   NP_653260
VERSION     NP_653260.1
DBSOURCE    REFSEQ: accession NM_144659.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Shen,S., Feng,H., Liu,L., Su,W., Yu,L. and Wu,J.
  TITLE     TCP10L negatively regulates alpha-fetoprotein expression in
            hepatocellular carcinoma
  JOURNAL   BMB Rep 53 (8), 431-436 (2020)
   PUBMED   32438969
  REMARK    GeneRIF: TCP10L negatively regulates alpha-fetoprotein expression
            in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Zhong,Z., Qiu,J., Chen,X., Wan,B., Ni,J., Yang,Y., Bai,M., Zhang,H.
            and Yu,L.
  TITLE     Identification of TCP10L as primate-specific gene derived via
            segmental duplication and homodimerization of TCP10L through the
            leucine zipper motif
  JOURNAL   Mol Biol Rep 35 (2), 171-178 (2008)
   PUBMED   17377852
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Denoeud,F., Kapranov,P., Ucla,C., Frankish,A., Castelo,R.,
            Drenkow,J., Lagarde,J., Alioto,T., Manzano,C., Chrast,J., Dike,S.,
            Wyss,C., Henrichsen,C.N., Holroyd,N., Dickson,M.C., Taylor,R.,
            Hance,Z., Foissac,S., Myers,R.M., Rogers,J., Hubbard,T., Harrow,J.,
            Guigo,R., Gingeras,T.R., Antonarakis,S.E. and Reymond,A.
  TITLE     Prominent use of distal 5' transcription start sites and discovery
            of a large number of additional exons in ENCODE regions
  JOURNAL   Genome Res 17 (6), 746-759 (2007)
   PUBMED   17567994
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Yu,H., Jiang,D., Guo,Z., Saiyin,H., Guo,J., Wang,X. and Yu,L.
  TITLE     TCP10L is expressed specifically in spermatogenic cells and binds
            to death associated protein kinase-3
  JOURNAL   Int J Androl 28 (3), 163-170 (2005)
   PUBMED   15910542
  REMARK    GeneRIF: The specific expression pattern of TCP10L and interaction
            with DAPK-3 implies that TCP10L might play crucially important
            roles in spermatogenesis through its interaction with DAPK-3.
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Jiang,D.J., Yu,H.X., Hexige,S.Y., Guo,Z.K., Wang,X., Ma,L.J.,
            Chen,Z., Zhao,S.Y. and Yu,L.
  TITLE     Human liver specific transcriptional factor TCP10L binds to MAD4
  JOURNAL   J Biochem Mol Biol 37 (4), 402-407 (2004)
   PUBMED   15469726
  REMARK    GeneRIF: Data suggest that the biological function of the
            interaction between T-complex protein 10-like and MAD4 may be to
            maintain the differentiation state in liver cells.
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Chen,Z., Yu,L., Wu,H., Yu,J., Zhang,L., Jiang,D., Ma,L., Li,D. and
            Zhao,S.
  TITLE     Identification of a novel liver-specific expressed gene, TCP10L,
            encoding a human leucine zipper protein with transcription
            inhibition activity
  JOURNAL   J Hum Genet 48 (11), 556-563 (2003)
   PUBMED   14586771
  REMARK    GeneRIF: The result revealed that TCP10L expressed specifically in
            the human liver and testis
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY036551.1, AF115967.1, BG721020.1, AP000274.2 and BC027970.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG717680.1, AF115967.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300258.8/ ENSP00000300258.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..215
                     /product="T-complex protein 10A homolog 1"
                     /note="T-complex protein 10A homolog 2; TCP10-like;
                     T-complex protein 10A-2; T-complex protein 10A-1"
                     /calculated_mol_wt=23732
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDR4.1)"
     Region          75..96
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDR4.1)"
     Region          150..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDR4.1)"
     CDS             1..215
                     /gene="TCP10L"
                     /gene_synonym="C21orf77; LINC00846; PRED77; TCP10A-1;
                     TCP10A-2"
                     /coded_by="NM_144659.7:105..752"
                     /db_xref="CCDS:CCDS13616.1"
                     /db_xref="GeneID:140290"
                     /db_xref="HGNC:HGNC:11657"
                     /db_xref="MIM:608365"
ORIGIN      
        1 mlagqleard pkegthpedp cpgagavmek tavaaevlte dcntgemppl qqqiirlhqe
       61 lgrqkslwad vhgklrshid alreqnmelr eklralqlqr wkarkksaas phagqeshtl
      121 alepafgkis plsadeetip kyaghknqsa tllgqrsssn nsappkpmsl kierisswkt
      181 ppqenrdknl srrrqdrrat ptgrptpcae rrggv
//
LOCUS       NP_001120793             191 aa            linear   PRI 20-NOV-2025
DEFINITION  chromobox protein homolog 5 [Homo sapiens].
ACCESSION   NP_001120793
VERSION     NP_001120793.1
DBSOURCE    REFSEQ: accession NM_001127321.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Zhou,L., Chen,Z., Zou,Y., Zhang,X., Wang,Z., Zhu,H., Lin,J.,
            Huang,Z., Zheng,L., Chen,J., Xie,M., Zhang,M., Zhang,R., Zhu,M.,
            Wang,Z., Zhou,H., Gao,S., Yin,Y., Wu,Y. and Kang,T.
  TITLE     ASB7 is a negative regulator of H3K9me3 homeostasis
  JOURNAL   Science 389 (6757), 309-316 (2025)
   PUBMED   40440427
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Lou,J., Deng,Q., Zhang,X., Bell,C.C., Das,A.B., Bediaga,N.G.,
            Zlatic,C.O., Johanson,T.M., Allan,R.S., Griffin,M.D.W.,
            Paradkar,P., Harvey,K.F., Dawson,M.A. and Hinde,E.
  TITLE     Heterochromatin protein 1 alpha (HP1alpha) undergoes a monomer to
            dimer transition that opens and compacts live cell genome
            architecture
  JOURNAL   Nucleic Acids Res 52 (18), 10918-10933 (2024)
   PUBMED   39193905
  REMARK    GeneRIF: Heterochromatin protein 1 alpha (HP1alpha) undergoes a
            monomer to dimer transition that opens and compacts live cell
            genome architecture.
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Sako,K., Furukawa,A., Nozawa,R.S., Kurita,J.I., Nishimura,Y. and
            Hirota,T.
  TITLE     Bipartite binding interface recruiting HP1 to chromosomal passenger
            complex at inner centromeres
  JOURNAL   J Cell Biol 223 (9) (2024)
   PUBMED   38781028
  REMARK    GeneRIF: Bipartite binding interface recruiting HP1 to chromosomal
            passenger complex at inner centromeres.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Ukmar-Godec,T., Yu,T., de Opakua,A.I., Pantoja,C.F., Munari,F. and
            Zweckstetter,M.
  TITLE     Conformational diversity of human HP1alpha
  JOURNAL   Protein Sci 33 (7), e5079 (2024)
   PUBMED   38895997
  REMARK    GeneRIF: Conformational diversity of human HP1alpha.
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Xiong,F., Wang,D., Xiong,W., Wang,X., Huang,W.H., Wu,G.H.,
            Liu,W.Z., Wang,Q., Chen,J.S., Kuai,Y.Y., Wang,B. and Chen,Y.J.
  TITLE     Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a therapeutic
            target for HP1alpha-positive intrahepatic cholangiocarcinoma
  JOURNAL   J Exp Clin Cancer Res 43 (1), 152 (2024)
   PUBMED   38812060
  REMARK    GeneRIF: Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a
            therapeutic target for HP1alpha-positive intrahepatic
            cholangiocarcinoma.
            Erratum:[J Exp Clin Cancer Res. 2024 Jul 5;43(1):186. doi:
            10.1186/s13046-024-03112-w. PMID: 38965576]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Lessard,J., Baban,S. and Sauvageau,G.
  TITLE     Stage-specific expression of polycomb group genes in human bone
            marrow cells
  JOURNAL   Blood 91 (4), 1216-1224 (1998)
   PUBMED   9454751
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Ye,Q., Callebaut,I., Pezhman,A., Courvalin,J.C. and Worman,H.J.
  TITLE     Domain-specific interactions of human HP1-type chromodomain
            proteins and inner nuclear membrane protein LBR
  JOURNAL   J Biol Chem 272 (23), 14983-14989 (1997)
   PUBMED   9169472
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Sugimoto,K., Yamada,T., Muro,Y. and Himeno,M.
  TITLE     Human homolog of Drosophila heterochromatin-associated protein 1
            (HP1) is a DNA-binding protein which possesses a DNA-binding motif
            with weak similarity to that of human centromere protein C (CENP-C)
  JOURNAL   J Biochem 120 (1), 153-159 (1996)
   PUBMED   8864858
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Ye,Q. and Worman,H.J.
  TITLE     Interaction between an integral protein of the nuclear envelope
            inner membrane and human chromodomain proteins homologous to
            Drosophila HP1
  JOURNAL   J Biol Chem 271 (25), 14653-14656 (1996)
   PUBMED   8663349
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Saunders,W.S., Chue,C., Goebl,M., Craig,C., Clark,R.F.,
            Powers,J.A., Eissenberg,J.C., Elgin,S.C., Rothfield,N.F. and
            Earnshaw,W.C.
  TITLE     Molecular cloning of a human homologue of Drosophila
            heterochromatin protein HP1 using anti-centromere autoantibodies
            with anti-chromo specificity
  JOURNAL   J Cell Sci 104 (Pt 2), 573-582 (1993)
   PUBMED   8505380
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP236173.1, BC006821.1,
            AC078778.34 and BC030149.2.
            
            Summary: This gene encodes a highly conserved nonhistone protein,
            which is a member of the heterochromatin protein family. The
            protein is enriched in the heterochromatin and associated with
            centromeres. The protein has a single N-terminal chromodomain which
            can bind to histone proteins via methylated lysine residues, and a
            C-terminal chromo shadow-domain (CSD) which is responsible for the
            homodimerization and interaction with a number of
            chromatin-associated nonhistone proteins. The encoded product is
            involved in the formation of functional kinetochore through
            interaction with essential kinetochore proteins. The gene has a
            pseudogene located on chromosome 3. Multiple alternatively spliced
            variants, encoding the same protein, have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence and transcripts to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP236173.1, SRR1660805.48245.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila); heterochromatin protein 1 homolog alpha;
                     antigen p25; HP1Hs alpha; HP1-ALPHA; epididymis luminal
                     protein 25; heterochromatin protein 1-alpha"
                     /calculated_mol_wt=22094
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13185; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Region          70..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="CBX5"
                     /gene_synonym="HEL25; HP1; HP1A; HP1alpha"
                     /coded_by="NM_001127321.1:121..696"
                     /db_xref="CCDS:CCDS8875.1"
                     /db_xref="GeneID:23468"
                     /db_xref="HGNC:HGNC:1555"
                     /db_xref="MIM:604478"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrv vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksesnkr ksnfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkeketak s
//
LOCUS       NP_001354107             495 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin epsilon and delta complex protein 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001354107
VERSION     NP_001354107.1
DBSOURCE    REFSEQ: accession NM_001367178.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Pudlowski,R., Xu,L., Milenkovic,L., Kumar,C., Hemsworth,K.,
            Aqrabawi,Z., Stearns,T. and Wang,J.T.
  TITLE     A delta-tubulin/epsilon-tubulin/Ted protein complex is required for
            centriole architecture
  JOURNAL   Elife 13, 98704 (2025)
   PUBMED   40067174
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Sarli,A., Al Sudani,Z.M., Vaghefi,F., Motallebi,F., Khosravi,T.,
            Rezaie,N. and Oladnabi,M.
  TITLE     Second report of TEDC1-related microcephaly caused by a novel
            biallelic mutation in an Iranian consanguineous family
  JOURNAL   Mol Biol Rep 51 (1), 181 (2024)
   PUBMED   38252227
  REMARK    GeneRIF: Second report of TEDC1-related microcephaly caused by a
            novel biallelic mutation in an Iranian consanguineous family.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 495)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Breslow,D.K., Hoogendoorn,S., Kopp,A.R., Morgens,D.W., Vu,B.K.,
            Kennedy,M.C., Han,K., Li,A., Hess,G.T., Bassik,M.C., Chen,J.K. and
            Nachury,M.V.
  TITLE     A CRISPR-based screen for Hedgehog signaling provides insights into
            ciliary function and ciliopathies
  JOURNAL   Nat Genet 50 (3), 460-471 (2018)
   PUBMED   29459677
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Filipuzzi,I., Thomas,J.R., Pries,V., Estoppey,D., Salcius,M.,
            Studer,C., Schirle,M. and Hoepfner,D.
  TITLE     Direct Interaction of Chivosazole F with Actin Elicits Cell
            Responses Similar to Latrunculin A but Distinct from Chondramide
  JOURNAL   ACS Chem Biol 12 (9), 2264-2269 (2017)
   PUBMED   28796488
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Behrends,C., Sowa,M.E., Gygi,S.P. and Harper,J.W.
  TITLE     Network organization of the human autophagy system
  JOURNAL   Nature 466 (7302), 68-76 (2010)
   PUBMED   20562859
REFERENCE   7  (residues 1 to 495)
  AUTHORS   DeGrado-Warren,J., Dufford,M., Chen,J., Bartel,P.L., Shattuck,D.
            and Frech,G.C.
  TITLE     Construction and characterization of a normalized yeast two-hybrid
            library derived from a human protein-coding clone collection
  JOURNAL   Biotechniques 44 (2), 265-273 (2008)
   PUBMED   18330356
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL928654.1 and BX248074.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX248074.1, DRR138514.11005.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392523.9/ ENSP00000376308.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.33"
     Protein         1..495
                     /product="tubulin epsilon and delta complex protein 1
                     isoform 6"
                     /note="uncharacterized protein C14orf80; tubulin epsilon
                     and delta complex protein 1"
                     /calculated_mol_wt=54100
     Region          90..331
                     /region_name="TEDC1"
                     /note="Tubulin epsilon and delta complex protein 1;
                     pfam14970"
                     /db_xref="CDD:464414"
     Region          417..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SX3.2)"
     CDS             1..495
                     /gene="TEDC1"
                     /gene_synonym="C14orf80"
                     /coded_by="NM_001367178.1:131..1618"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS91958.1"
                     /db_xref="GeneID:283643"
                     /db_xref="HGNC:HGNC:20127"
ORIGIN      
        1 mgrrrqrvdp aagaragalp eaiaalsrsl psgpspeifr rakfdrpeat salwqllfrv
       61 lsplpagnal aslalevqar lvksalcsqg yprlalaqlp edgsqgsrel llalswllar
      121 gpvpeqmlaq arvplgdemt vcqcealasp gppaphmeae gpvdvrhvqw lmgklrfrwr
      181 qlvssqqeqc allskihlyt rgchsdqsls hlsvteaeml rdpeggqqvs gagaaqnldl
      241 aypkclhsfc tpgmgprtfw ndlwlvceqp gllpgdwaap ldpggasacs llspfrallr
      301 tlerenqrle avlawrrsel vfwrwmdtvl gtcapevpaa asqptflpwv pergggeldl
      361 vvrelqalee elreaaerrr aaweakaggc grgpewsaar rasreaveke lgalqqcwer
      421 dggpaqphgp hrlvrredga agdrdlraav virtlrsqea cleavlrrlq gqcrqelarl
      481 vgarpgliwi pppgr
//
LOCUS       NP_001339871             696 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 14 [Homo sapiens].
ACCESSION   NP_001339871
VERSION     NP_001339871.1
DBSOURCE    REFSEQ: accession NM_001352942.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 696)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 696)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 696)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 696)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 696)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 696)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 696)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 696)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 696)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 696)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.276460.1,
                                           SRR1803612.217315.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN02400289 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..696
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..696
                     /product="DNA repair-scaffolding protein isoform 14"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=75963
     Region          <1..150
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          302..686
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..696
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352942.1:516..2606"
                     /note="isoform 14 is encoded by transcript variant 17"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 merlidprtk stetilhtpq kptakfprtp ensakkkllr gglaerlngl qnrersaisl
       61 wrhqcisyqk tlsgrksgvl tvkilelhee camqvamceq llgspatsss qsvaprpgag
      121 lkvlftketa gylrgrpqdt vrifppwqkl iipsgscpvi lntyfcekvv akedsektce
      181 vycpdiplpr rsislaqmfv ikgltnnspe iqvvcsgvat tgtawthghk eakqriptst
      241 plrdslldvv esqgaaswpg agvrvvvqrv yslpsrdstr gqqgassght dpagtracll
      301 vqdacgmfge vhleftmska rqlegkscsl vgmkvlqkvt rgrtagifsl idtlwppaip
      361 lktpgrdqpc eeikthlppp alcyiltahp nlgqidiide dpiyklyqpp vtrclrdilq
      421 mndlgtrcsf yatviyqkpq lkslllleqr eiwllvtdvt lqtkeerdpr lpktllvyva
      481 plcvlgsevl ealagaaphs lffkdalrdq grivcaertv lllqkpllsv vsgasscelp
      541 gpvmldslds atpvnsicsv qgtvvgvdes tafswpvcdm cgngrleqrp edrgafscgd
      601 csrvvtspvl krhlqvfldc rsrpqcrvkv kllqrsissl lrfaagedgs yevksvlgke
      661 vgllncfvqs vtahptscig leeiellsag gasaeh
//
LOCUS       NP_000969                140 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL14 [Homo sapiens].
ACCESSION   NP_000969
VERSION     NP_000969.1
DBSOURCE    REFSEQ: accession NM_000978.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Yaseen,N.R. and Blobel,G.
  TITLE     Cloning and characterization of human karyopherin beta3
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4451-4456 (1997)
   PUBMED   9114010
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Herault,Y., Michel,D., Chatelain,G. and Brun,G.
  TITLE     cDNA and predicted amino acid sequences of the human ribosomal
            protein genes rpS12 and rpL17
  JOURNAL   Nucleic Acids Res 19 (14), 4001 (1991)
   PUBMED   1861993
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Berchtold,M.W. and Berger,M.C.
  TITLE     Isolation and analysis of a human cDNA highly homologous to the
            yeast gene encoding L17A ribosomal protein
  JOURNAL   Gene 102 (2), 283-288 (1991)
   PUBMED   1874450
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from X55954.1, CA437923.1 and AC110749.12.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L14P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL17 because the
            encoded protein shares amino acid identity with ribosomal protein
            L17 from Saccharomyces cerevisiae; however, its official symbol is
            RPL23. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB133887.1, SRR1803614.109555.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000479035.7/ ENSP00000420311.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..140
                     /product="large ribosomal subunit protein uL14"
                     /note="60S ribosomal protein L23; ribosomal protein L17;
                     60S ribosomal protein L17"
                     /calculated_mol_wt=14734
     Region          2..139
                     /region_name="PTZ00054"
                     /note="60S ribosomal protein L23; Provisional"
                     /db_xref="CDD:185418"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P62829.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P62829.1)"
     CDS             1..140
                     /gene="RPL23"
                     /gene_synonym="L23; rpL17; uL14"
                     /coded_by="NM_000978.4:12..434"
                     /db_xref="CCDS:CCDS11330.1"
                     /db_xref="GeneID:9349"
                     /db_xref="HGNC:HGNC:10316"
                     /db_xref="MIM:603662"
ORIGIN      
        1 mskrgrggss gakfrislgl pvgavincad ntgaknlyii svkgikgrln rlpaagvgdm
       61 vmatvkkgkp elrkkvhpav virqrksyrr kdgvflyfed nagvivnnkg emkgsaitgp
      121 vakecadlwp riasnagsia
//
LOCUS       NP_689419                406 aa            linear   PRI 20-NOV-2025
DEFINITION  sorting nexin-6 isoform b [Homo sapiens].
ACCESSION   NP_689419
VERSION     NP_689419.3
DBSOURCE    REFSEQ: accession NM_152233.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Ghosh,C., Xing,Y., Li,S., Hoyle,R.G., Sun,M., Li,J. and Sun,Y.
  TITLE     Sorting nexin 6 interacts with Cullin3 and regulates programmed
            death ligand 1 expression
  JOURNAL   FEBS Lett 595 (20), 2558-2569 (2021)
   PUBMED   34510437
  REMARK    GeneRIF: Sorting nexin 6 interacts with Cullin3 and regulates
            programmed death ligand 1 expression.
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Ishibashi,Y., Maita,H., Yano,M., Koike,N., Tamai,K., Ariga,H. and
            Iguchi-Ariga,S.M.
  TITLE     Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from
            cytoplasm to nucleus
  JOURNAL   FEBS Lett 506 (1), 33-38 (2001)
   PUBMED   11591366
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Teasdale,R.D., Loci,D., Houghton,F., Karlsson,L. and Gleeson,P.A.
  TITLE     A large family of endosome-localized proteins related to sorting
            nexin 1
  JOURNAL   Biochem J 358 (Pt 1), 7-16 (2001)
   PUBMED   11485546
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Parks,W.T., Frank,D.B., Huff,C., Renfrew Haft,C., Martin,J.,
            Meng,X., de Caestecker,M.P., McNally,J.G., Reddi,A., Taylor,S.I.,
            Roberts,A.B., Wang,T. and Lechleider,R.J.
  TITLE     Sorting nexin 6, a novel SNX, interacts with the transforming
            growth factor-beta family of receptor serine-threonine kinases
  JOURNAL   J Biol Chem 276 (22), 19332-19339 (2001)
   PUBMED   11279102
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Wurthner,J.U., Frank,D.B., Felici,A., Green,H.M., Cao,Z.,
            Schneider,M.D., McNally,J.G., Lechleider,R.J. and Roberts,A.B.
  TITLE     Transforming growth factor-beta receptor-associated protein 1 is a
            Smad4 chaperone
  JOURNAL   J Biol Chem 276 (22), 19495-19502 (2001)
   PUBMED   11278302
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB021488.1, U83194.1,
            BI870378.1, AF121856.2, AK124315.1 and AI446034.1.
            
            On Oct 10, 2018 this sequence version replaced NP_689419.2.
            
            Summary: This gene encodes a member of the sorting nexin family.
            Members of this family contain a phox (PX) domain, which is a
            phosphoinositide binding domain, and are involved in intracellular
            trafficking. This protein associates with the long isoform of the
            leptin receptor, the transforming growth factor-beta family of
            receptor serine-threonine kinases, and with receptor tyrosine
            kinases for platelet-derived growth factor, insulin, and epidermal
            growth factor. This protein may form oligomeric complexes with
            family member proteins through interactions of both the PX domain
            and the coiled coil regions of the molecules. Translocation of this
            protein from the cytoplasm to the nucleus occurs after binding to
            proviral integration site 1 protein. This gene results in two
            transcripts encoding two distinct isoforms. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) encodes the longest isoform
            (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.119176.1,
                                           SRR1803617.10341.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000362031.10/ ENSP00000355217.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..406
                     /product="sorting nexin-6 isoform b"
                     /note="tumor necrosis factor receptor-associated factor
                     4(TRAF4)-associated factor 2; TRAF4-associated factor 2"
                     /calculated_mol_wt=46518
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          2..179
                     /region_name="Interaction with PIM1.
                     /evidence=ECO:0000269|PubMed:11591366"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine, in Sorting nexin-6,
                     N-terminally processed.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          30..170
                     /region_name="PX_SNX6"
                     /note="The phosphoinositide binding Phox Homology domain
                     of Sorting Nexin 6; cd07292"
                     /db_xref="CDD:132825"
     Site            order(69..71,96..97,140)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:132825"
     Site            116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          182..199
                     /region_name="Membrane-binding amphipathic helix.
                     /evidence=ECO:0000303|PubMed:23085988"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Region          186..403
                     /region_name="BAR_SNX6"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Sorting
                     Nexin 6; cd07662"
                     /db_xref="CDD:153346"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UNH7.1)"
     Site            order(216,219..220,223..224,226..227,230,233..234,237,
                     244..245,247..248,251,254..255,258..259,274,363,366..367,
                     369..371,374,377..378,380..382,384..385,388..389,391..392,
                     395..396,398..399)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153346"
     CDS             1..406
                     /gene="SNX6"
                     /gene_synonym="MSTP010; TFAF2"
                     /coded_by="NM_152233.4:33..1253"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS41942.2"
                     /db_xref="GeneID:58533"
                     /db_xref="HGNC:HGNC:14970"
                     /db_xref="MIM:606098"
ORIGIN      
        1 mmeglddgpd flseedrglk ainvdlqsda alqvdisdal serdkvkftv htksslpnfk
       61 qnefsvvrqh eefiwlhdsf venedyagyi ippapprpdf dasreklqkl gegegsmtke
      121 eftkmkqele aeylaifkkt vamhevflcr vaahpilrrd lnfhvfleyn qdlsvrgknk
      181 kekledffkn mvksadgviv sgvkdvddff ehertflley hnrvkdasak sdrmtrshks
      241 aaddynrigs slyalgtqds tdickfflkv selfdktrki earvsadedl klsdllkyyl
      301 resqaakdll yrrsrslvdy enankaldka raknkdvlqa etsqqlccqk fekisesakq
      361 elidfktrrv aafrknlvel aelelkhakg nlqllqncla vlngdt
//
LOCUS       NP_001092281             483 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-8 isoform a [Homo sapiens].
ACCESSION   NP_001092281
VERSION     NP_001092281.1
DBSOURCE    REFSEQ: accession NM_001098811.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Liu,H., Yan,P., Wu,C., Rao,M., Zhu,J., Lv,L., Li,W., Liang,Y.,
            Qi,S., Lu,K. and Kong,E.
  TITLE     Palmitoylated Sept8-204 modulates learning and anxiety by
            regulating filopodia arborization and actin dynamics
  JOURNAL   Sci Signal 16 (814), eadi8645 (2023)
   PUBMED   38051778
  REMARK    GeneRIF: Palmitoylated Sept8-204 modulates learning and anxiety by
            regulating filopodia arborization and actin dynamics.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Keele,G.R., Prokop,J.W., He,H., Holl,K., Littrell,J., Deal,A.W.,
            Kim,Y., Kyle,P.B., Attipoe,E., Johnson,A.C., Uhl,K.L.,
            Sirpilla,O.L., Jahanbakhsh,S., Robinson,M., Levy,S., Valdar,W.,
            Garrett,M.R. and Solberg Woods,L.C.
  TITLE     Sept8/SEPTIN8 involvement in cellular structure and kidney damage
            is identified by genetic mapping and a novel human tubule hypoxic
            model
  JOURNAL   Sci Rep 11 (1), 2071 (2021)
   PUBMED   33483609
  REMARK    GeneRIF: Sept8/SEPTIN8 involvement in cellular structure and kidney
            damage is identified by genetic mapping and a novel human tubule
            hypoxic model.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Yang,T., Gao,Y.K. and Chen,J.Y.
  TITLE     KIAA0202, a human septin family member, interacting with hPFTAIRE1
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 34 (4),
            520-525 (2002)
   PUBMED   12098780
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Blaser,S., Jersch,K., Hainmann,I., Wunderle,D., Zgaga-Griesz,A.,
            Busse,A. and Zieger,B.
  TITLE     Human septin-septin interaction: CDCrel-1 partners with KIAA0202
  JOURNAL   FEBS Lett 519 (1-3), 169-172 (2002)
   PUBMED   12023038
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Wenderfer,S.E., Slack,J.P., McCluskey,T.S. and Monaco,J.J.
  TITLE     Identification of 40 genes on a 1-Mb contig around the IL-4
            cytokine family gene cluster on mouse chromosome 11
  JOURNAL   Genomics 63 (3), 354-373 (2000)
   PUBMED   10704283
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Frazer,K.A., Ueda,Y., Zhu,Y., Gifford,V.R., Garofalo,M.R.,
            Mohandas,N., Martin,C.H., Palazzolo,M.J., Cheng,J.F. and Rubin,E.M.
  TITLE     Computational and biological analysis of 680 kb of DNA sequence
            from the human 5q31 cytokine gene cluster region
  JOURNAL   Genome Res 7 (5), 495-512 (1997)
   PUBMED   9149945
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF440761.1, AF440762.1 and
            BU739074.1.
            
            Summary: This gene is a member of the septin family of nucleotide
            binding proteins, originally described in yeast as cell division
            cycle regulatory proteins. Septins are highly conserved in yeast,
            Drosophila, and mouse, and appear to regulate cytoskeletal
            organization. Disruption of septin function disturbs cytokinesis
            and results in large multinucleate or polyploid cells. Multiple
            alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2014].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.11325.1, AF440762.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378719.7/ ENSP00000367991.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..483
                     /product="septin-8 isoform a"
                     /calculated_mol_wt=55625
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92599.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92599.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92599.4)"
     Region          41..309
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Region          51..58
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92599.4)"
     Site            51..58
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(53..59,103,106,186..187,189,241..242)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            78..86
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            80
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Region          103..106
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92599.4)"
     Site            103..106
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(105..143,145..152)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Region          186..189
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01056"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92599.4)"
     Site            186..189
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            241..243
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     Region          411..443
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92599.4)"
     CDS             1..483
                     /gene="SEPTIN8"
                     /gene_synonym="SEP2; SEPT8; Septin-8"
                     /coded_by="NM_001098811.2:103..1554"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43358.1"
                     /db_xref="GeneID:23176"
                     /db_xref="HGNC:HGNC:16511"
                     /db_xref="MIM:608418"
ORIGIN      
        1 maatdlerfs naepeprsls lgghvgfdsl pdqlvsksvt qgfsfnilcv getgigkstl
       61 mntlfnttfe teeashheac vrlrpqtydl qesnvqlklt ivdavgfgdq inkdesyrpi
      121 vdyidaqfen ylqeelkirr slfdyhdtri hvclyfitpt ghslksldlv tmkkldskvn
      181 iipiiakadt iskselhkfk ikimgelvsn gvqiyqfptd deavaeinav mnahlpfavv
      241 gsteevkvgn klvrarqypw gvvqvenenh cdfvklreml irvnmedlre qthsrhyely
      301 rrckleemgf qdsdgdsqpf slqetyeakr keflselqrk eeemrqmfvn kvketelelk
      361 ekerelhekf ehlkrvhqee krkveekrre leeetnafnr rkaavealqs qalhatsqqp
      421 lrkdkdkknr sdigahqpgm slssskvmmt kasveplncs swwpaiqccs clvrdatwre
      481 gfl
//
LOCUS       NP_001193612             117 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclic AMP-dependent transcription factor ATF-7 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001193612
VERSION     NP_001193612.1
DBSOURCE    REFSEQ: accession NM_001206683.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Zhang,J., Liu,D., Deng,G., Wang,Q., Li,L., Zhang,J. and Wu,H.
  TITLE     lncRNA prostate cancer-associated transcript 18 upregulates
            activating transcription factor 7 to prevent metastasis of
            triple-negative breast cancer via sponging miR-103a-3p
  JOURNAL   Bioengineered 12 (2), 12070-12086 (2021)
   PUBMED   34787047
  REMARK    GeneRIF: lncRNA prostate cancer-associated transcript 18
            upregulates activating transcription factor 7 to prevent metastasis
            of triple-negative breast cancer via sponging miR-103a-3p.
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Newman,S.P., Bates,N.P., Vernimmen,D., Parker,M.G. and Hurst,H.C.
  TITLE     Cofactor competition between the ligand-bound oestrogen receptor
            and an intron 1 enhancer leads to oestrogen repression of ERBB2
            expression in breast cancer
  JOURNAL   Oncogene 19 (4), 490-497 (2000)
   PUBMED   10698518
REFERENCE   6  (residues 1 to 117)
  AUTHORS   De Graeve,F., Bahr,A., Sabapathy,K.T., Hauss,C., Wagner,E.F.,
            Kedinger,C. and Chatton,B.
  TITLE     Role of the ATFa/JNK2 complex in Jun activation
  JOURNAL   Oncogene 18 (23), 3491-3500 (1999)
   PUBMED   10376527
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Goetz,J., Chatton,B., Mattei,M.G. and Kedinger,C.
  TITLE     Structure and expression of the ATFa gene
  JOURNAL   J Biol Chem 271 (47), 29589-29598 (1996)
   PUBMED   8939888
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Bocco,J.L., Bahr,A., Goetz,J., Hauss,C., Kallunki,T., Kedinger,C.
            and Chatton,B.
  TITLE     In vivo association of ATFa with JNK/SAP kinase activities
  JOURNAL   Oncogene 12 (9), 1971-1980 (1996)
   PUBMED   8649858
REFERENCE   9  (residues 1 to 117)
  AUTHORS   Pescini,R., Kaszubska,W., Whelan,J., DeLamarter,J.F. and Hooft van
            Huijsduijnen,R.
  TITLE     ATF-a0, a novel variant of the ATF/CREB transcription factor
            family, forms a dominant transcription inhibitor in ATF-a
            heterodimers
  JOURNAL   J Biol Chem 269 (2), 1159-1165 (1994)
   PUBMED   8288576
REFERENCE   10 (residues 1 to 117)
  AUTHORS   Gaire,M., Chatton,B. and Kedinger,C.
  TITLE     Isolation and characterization of two novel, closely related ATF
            cDNA clones from HeLa cells
  JOURNAL   Nucleic Acids Res 18 (12), 3467-3473 (1990)
   PUBMED   1694576
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB490927.2, BC042363.1, AC023509.42 and AA679547.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, 3'
            coding region and 3' UTR, compared to variant 2, resulting in an
            isoform (4) with a distinct and shorter C-terminus, compared to
            isoform 2. Variants 4, 5, and 13 all encode the same isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI596298.1, DB490927.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..117
                     /product="cyclic AMP-dependent transcription factor ATF-7
                     isoform 4"
                     /note="cyclic AMP-dependent transcription factor ATF-7;
                     transcription factor ATF-A"
                     /calculated_mol_wt=13147
     Region          47..84
                     /region_name="GCN4_cent"
                     /note="GCN4 central activation domain-like acidic
                     activation domain; cd12192"
                     /db_xref="CDD:213399"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK11.
                     /evidence=ECO:0000269|PubMed:18950637; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:18950637; propagated from
                     UniProtKB/Swiss-Prot (P17544.3)"
     Site            order(58..59,61..62,70..71,73..75,77..78,82..84)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:213399"
     CDS             1..117
                     /gene="ATF7"
                     /gene_synonym="ATFA"
                     /coded_by="NM_001206683.1:68..421"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS58238.1"
                     /db_xref="GeneID:11016"
                     /db_xref="HGNC:HGNC:792"
                     /db_xref="MIM:606371"
ORIGIN      
        1 mgddrpfvcn apgcgqrftn edhlavhkhk hemtlkfgpa rtdsviiadq tptptrflkn
       61 ceevglfnel assfehefkk aadedekkar srtvakklvv frprlfllcf giiflig
//
LOCUS       NP_054733               2136 aa            linear   PRI 20-NOV-2025
DEFINITION  U5 small nuclear ribonucleoprotein 200 kDa helicase [Homo sapiens].
ACCESSION   NP_054733
VERSION     NP_054733.2
DBSOURCE    REFSEQ: accession NM_014014.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2136)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2136)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2136)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2136)
  AUTHORS   Atkinson,R., Georgiou,M., Yang,C., Szymanska,K., Lahat,A.,
            Vasconcelos,E.J.R., Ji,Y., Moya Molina,M., Collin,J., Queen,R.,
            Dorgau,B., Watson,A., Kurzawa-Akanbi,M., Laws,R., Saxena,A., Shyan
            Beh,C., Siachisumo,C., Goertler,F., Karwatka,M., Davey,T.,
            Inglehearn,C.F., McKibbin,M., Luhrmann,R., Steel,D.H.,
            Elliott,D.J., Armstrong,L., Urlaub,H., Ali,R.R., Grellscheid,S.N.,
            Johnson,C.A., Mozaffari-Jovin,S. and Lako,M.
  TITLE     PRPF8-mediated dysregulation of hBrr2 helicase disrupts human
            spliceosome kinetics and 5 -splice-site selection causing
            tissue-specific defects
  JOURNAL   Nat Commun 15 (1), 3138 (2024)
   PUBMED   38605034
  REMARK    GeneRIF: PRPF8-mediated dysregulation of hBrr2 helicase disrupts
            human spliceosome kinetics and 5 -splice-site selection causing
            tissue-specific defects.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2136)
  AUTHORS   Guidarelli Mattioli,F., Saltalamacchia,A. and Magistrato,A.
  TITLE     Tracing Allostery in the Spliceosome Ski2-like RNA Helicase Brr2
  JOURNAL   J Phys Chem Lett 15 (13), 3502-3508 (2024)
   PUBMED   38517341
  REMARK    GeneRIF: Tracing Allostery in the Spliceosome Ski2-like RNA
            Helicase Brr2.
REFERENCE   6  (residues 1 to 2136)
  AUTHORS   Achsel,T., Ahrens,K., Brahms,H., Teigelkamp,S. and Luhrmann,R.
  TITLE     The human U5-220kD protein (hPrp8) forms a stable RNA-free complex
            with several U5-specific proteins, including an RNA unwindase, a
            homologue of ribosomal elongation factor EF-2, and a novel WD-40
            protein
  JOURNAL   Mol Cell Biol 18 (11), 6756-6766 (1998)
   PUBMED   9774689
REFERENCE   7  (residues 1 to 2136)
  AUTHORS   Laggerbauer,B., Achsel,T. and Luhrmann,R.
  TITLE     The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in
            vitro
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4188-4192 (1998)
   PUBMED   9539711
REFERENCE   8  (residues 1 to 2136)
  AUTHORS   Lauber,J., Fabrizio,P., Teigelkamp,S., Lane,W.S., Hartmann,E. and
            Luhrmann,R.
  TITLE     The HeLa 200 kDa U5 snRNP-specific protein and its homologue in
            Saccharomyces cerevisiae are members of the DEXH-box protein family
            of putative RNA helicases
  JOURNAL   EMBO J 15 (15), 4001-4015 (1996)
   PUBMED   8670905
REFERENCE   9  (residues 1 to 2136)
  AUTHORS   Laggerbauer,B., Lauber,J. and Luhrmann,R.
  TITLE     Identification of an RNA-dependent ATPase activity in mammalian U5
            snRNPs
  JOURNAL   Nucleic Acids Res 24 (5), 868-875 (1996)
   PUBMED   8600454
REFERENCE   10 (residues 1 to 2136)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB067751.1, AY572488.1,
            AB018331.2 and AW190145.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 19, 2003 this sequence version replaced NP_054733.1.
            
            Summary: Pre-mRNA splicing is catalyzed by the spliceosome, a
            complex of specialized RNA and protein subunits that removes
            introns from a transcribed pre-mRNA segment. The spliceosome
            consists of small nuclear RNA proteins (snRNPs) U1, U2, U4, U5 and
            U6, together with approximately 80 conserved proteins. U5 snRNP
            contains nine specific proteins. This gene encodes one of the U5
            snRNP-specific proteins. This protein belongs to the DEXH-box
            family of putative RNA helicases. It is a core component of
            U4/U6-U5 snRNPs and appears to catalyze an ATP-dependent unwinding
            of U4/U6 RNA duplices. Mutations in this gene cause
            autosomal-dominant retinitis pigmentosa. Alternatively spliced
            transcript variants encoding different isoforms have been found,
            but the full-length nature of these variants has not been
            determined. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.187493.1,
                                           SRR1803611.60324.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323853.10/ ENSP00000317123.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..2136
                     /product="U5 small nuclear ribonucleoprotein 200 kDa
                     helicase"
                     /EC_number="3.6.4.13"
                     /note="activating signal cointegrator 1 complex subunit
                     3-like 1; BRR2 homolog; U5 snRNP-specific 200 kDa protein;
                     small nuclear ribonucleoprotein, U5 200kDa subunit; small
                     nuclear ribonucleoprotein 200kDa (U5); bad response to
                     refrigeration 2 homolog"
                     /calculated_mol_wt=244378
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Region          50..80
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Region          254..363
                     /region_name="Helicase_PWI"
                     /note="N-terminal helicase PWI domain; pfam18149"
                     /db_xref="CDD:436309"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Region          395..2129
                     /region_name="Interaction with C9orf78 and WBP4.
                     /evidence=ECO:0000269|PubMed:35241646"
                     /note="propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Region          462..1017
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
     Region          464..677
                     /region_name="DEXHc_Brr2_1"
                     /note="N-terminal DEXH-box helicase domain of spliceosomal
                     Brr2 RNA helicase; cd18019"
                     /db_xref="CDD:350777"
     Site            order(480,482,485,506..510,615..616)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350777"
     Site            order(544..546,572..576,578..579,589,591..592,595,599,624)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350777"
     Region          615..618
                     /region_name="DEIH box"
                     /note="propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:F1LNJ2; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Site            971
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Region          982..1285
                     /region_name="Sec63"
                     /note="Sec63 Brl domain; pfam02889"
                     /db_xref="CDD:460740"
     Region          1282..2136
                     /region_name="Interaction with TSSC4.
                     /evidence=ECO:0000269|PubMed:35188580"
                     /note="propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Region          1309..1849
                     /region_name="BRR2"
                     /note="Replicative superfamily II helicase [Replication,
                     recombination and repair]; COG1204"
                     /db_xref="CDD:440817"
     Region          1325..1515
                     /region_name="DEXHc_Brr2_2"
                     /note="C-terminal D[D/E]X[H/Q]-box helicase domain of
                     spliceosomal Brr2 RNA helicase; cd18021"
                     /db_xref="CDD:350779"
     Site            order(1325,1327..1329,1332,1351..1357)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350779"
     Site            1428
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Region          1454..1457
                     /region_name="DEVH box"
                     /note="propagated from UniProtKB/Swiss-Prot (O75643.2)"
     Site            1765
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6P4T2; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Region          1809..2125
                     /region_name="SEC63"
                     /note="Domain of unknown function in Sec63p, Brr2p and
                     other proteins; smart00611"
                     /db_xref="CDD:214744"
     Site            2002
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Site            2131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Site            2133
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     Site            2135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O75643.2)"
     CDS             1..2136
                     /gene="SNRNP200"
                     /gene_synonym="ASCC3L1; BRR2; HELIC2; RP33; U5-200KD"
                     /coded_by="NM_014014.5:110..6520"
                     /db_xref="CCDS:CCDS2020.1"
                     /db_xref="GeneID:23020"
                     /db_xref="HGNC:HGNC:30859"
                     /db_xref="MIM:601664"
ORIGIN      
        1 madvtarslq yeykansnlv lqadrslidr trrdeptgev lslvgklegt rmgdkaqrtk
       61 pqmqeerrak rrkrdedrhd inkmkgytll segidemvgi iykpktketr etyevllsfi
      121 qaalgdqprd ilcgaadevl avlkneklrd kerrkeidll lgqtddtryh vlvnlgkkit
      181 dyggdkeiqn mddnidetyg vnvqfesdee egdedvygev reeasdddme gdeavvrctl
      241 sanlvasgel msskkkdlhp rdidafwlqr qlsrfyddai vsqkkadevl eilktasddr
      301 ecenqlvlll gfntfdfikv lrqhrmmily ctllasaqse aekerimgkm eadpelskfl
      361 yqlheteked lireersrre rvrqsrmdtd letmdldqgg ealaprqvld ledlvftqgs
      421 hfmankrcql pdgsfrrqrk gyeevhvpal kpkpfgseeq llpveklpky aqagfegfkt
      481 lnriqsklyr aaletdenll lcaptgagkt nvalmcmlre igkhinmdgt invddfkiiy
      541 iapmrslvqe mvgsfgkrla tygitvaelt gdhqlckeei satqiivctp ekwdiitrkg
      601 gertytqlvr liildeihll hddrgpvlea lvarairnie mtqedvrlig lsatlpnyed
      661 vatflrvdpa kglfyfdnsf rpvpleqtyv gitekkaikr fqimneivye kimehagknq
      721 vlvfvhsrke tgktaraird mclekdtlgl flregsaste vlrteaeqck nlelkdllpy
      781 gfaihhagmt rvdrtlvedl fadkhiqvlv statlawgvn lpahtviikg tqvyspekgr
      841 wtelgaldil qmlgragrpq ydtkgegili tshgelqyyl sllnqqlpie sqmvsklpdm
      901 lnaeivlgnv qnakdavnwl gyaylyirml rsptlygish ddlkgdplld qrrldlvhta
      961 almldknnlv kydkktgnfq vtelgriash yyitndtvqt ynqllkptls eielfrvfsl
     1021 ssefknitvr eeeklelqkl lervpipvke sieepsakin vllqafisql klegfalmad
     1081 mvyvtqsagr lmraifeivl nrgwaqltdk tlnlckmidk rmwqsmcplr qfrklpeevv
     1141 kkiekknfpf erlydlnhne igelirmpkm gktihkyvhl fpklelsvhl qpitrstlkv
     1201 eltitpdfqw dekvhgssea fwilvedvds evilhheyfl lkakyaqdeh litffvpvfe
     1261 plppqyfirv vsdrwlscet qlpvsfrhli lpekypppte lldlqplpvs alrnsafesl
     1321 yqdkfpffnp iqtqvfntvy nsddnvfvga ptgsgktica efailrmllq ssegrcvyit
     1381 pmealaeqvy mdwyekfqdr lnkkvvlltg etstdlkllg kgniiistpe kwdilsrrwk
     1441 qrknvqninl fvvdevhlig gengpvlevi csrmryissq ierpirival ssslsnakdv
     1501 ahwlgcsats tfnfhpnvrp vplelhiqgf nishtqtrll smakpvyhai tkhspkkpvi
     1561 vfvpsrkqtr ltaidilttc aadiqrqrfl hctekdlipy leklsdstlk etllngvgyl
     1621 heglspmerr lveqlfssga iqvvvasrsl cwgmnvaahl viimdtqyyn gkihayvdyp
     1681 iydvlqmvgh anrplqddeg rcvimcqgsk kdffkkflye plpveshldh cmhdhfnaei
     1741 vtktienkqd avdyltwtfl yrrmtqnpny ynlqgishrh lsdhlselve qtlsdleqsk
     1801 cisiedemdv aplnlgmiaa yyyinyttie lfsmslnakt kvrglieiis naaeyenipi
     1861 rhhednllrq laqkvphkln npkfndphvk tnlllqahls rmqlsaelqs dteeilskai
     1921 rliqacvdvl ssngwlspal aamelaqmvt qamwskdsyl kqlphftseh ikrctdkgve
     1981 svfdimemed eernallqlt dsqiadvarf cnrypniels yevvdkdsir sggpvvvlvq
     2041 lereeevtgp viaplfpqkr eegwwvvigd aksnslisik rltlqqkakv kldfvapatg
     2101 ahnytlyfms daymgcdqey kfsvdvkeae tdsdsd
//
LOCUS       NP_001269367              99 aa            linear   PRI 20-NOV-2025
DEFINITION  biogenesis of lysosome-related organelles complex 1 subunit 2
            isoform 2 [Homo sapiens].
ACCESSION   NP_001269367
VERSION     NP_001269367.1
DBSOURCE    REFSEQ: accession NM_001282438.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Yordanov,T.E., Hipolito,V.E.B., Liebscher,G., Vogel,G.F.,
            Stasyk,T., Herrmann,C., Geley,S., Teis,D., Botelho,R.J., Hess,M.W.
            and Huber,L.A.
  TITLE     Biogenesis of lysosome-related organelles complex-1 (BORC)
            regulates late endosomal/lysosomal size through PIKfyve-dependent
            phosphatidylinositol-3,5-bisphosphate
  JOURNAL   Traffic 20 (9), 674-696 (2019)
   PUBMED   31314175
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Wang,Z., Wei,H., Yu,Y., Sun,J., Yang,Y., Xing,G., Wu,S., Zhou,Y.,
            Zhu,Y., Zhang,C., Zhou,T., Zhao,X., Sun,Q. and He,F.
  TITLE     Characterization of Ceap-11 and Ceap-16, two novel
            splicing-variant-proteins, associated with centrosome, microtubule
            aggregation and cell proliferation
  JOURNAL   J Mol Biol 343 (1), 71-82 (2004)
   PUBMED   15381421
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Starcevic,M. and Dell'Angelica,E.C.
  TITLE     Identification of snapin and three novel proteins (BLOS1, BLOS2,
            and BLOS3/reduced pigmentation) as subunits of biogenesis of
            lysosome-related organelles complex-1 (BLOC-1)
  JOURNAL   J Biol Chem 279 (27), 28393-28401 (2004)
   PUBMED   15102850
  REMARK    GeneRIF: Biogenesis of lysosome-related organelles complex-1
            (BLOC-1) subunit 2 (BLOS2).BLOC-1 is required for the biogenesis of
            melanosomes and platelet dense granules.
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Li,W., Zhang,Q., Oiso,N., Novak,E.K., Gautam,R., O'Brien,E.P.,
            Tinsley,C.L., Blake,D.J., Spritz,R.A., Copeland,N.G., Jenkins,N.A.,
            Amato,D., Roe,B.A., Starcevic,M., Dell'Angelica,E.C., Elliott,R.W.,
            Mishra,V., Kingsmore,S.F., Paylor,R.E. and Swank,R.T.
  TITLE     Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
            dysbindin, a member of the biogenesis of lysosome-related
            organelles complex 1 (BLOC-1)
  JOURNAL   Nat Genet 35 (1), 84-89 (2003)
   PUBMED   12923531
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Ciciotte,S.L., Gwynn,B., Moriyama,K., Huizing,M., Gahl,W.A.,
            Bonifacino,J.S. and Peters,L.L.
  TITLE     Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a
            novel protein that is part of the pallidin-muted complex (BLOC-1)
  JOURNAL   Blood 101 (11), 4402-4407 (2003)
   PUBMED   12576321
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Moriyama,K. and Bonifacino,J.S.
  TITLE     Pallidin is a component of a multi-protein complex involved in the
            biogenesis of lysosome-related organelles
  JOURNAL   Traffic 3 (9), 666-677 (2002)
   PUBMED   12191018
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY165508.1, BU740315.1, CB218039.1, DB296446.1, AL138921.14 and
            BX112121.1.
            
            Summary: This gene encodes a protein with multiple functions. The
            encoded protein has been found in association with the centrosome,
            shown to co-localize with gamma-tubulin, and also found to be one
            of the proteins in the BLOC-1 complex which functions in the
            formation of lysosome-related organelles. A pseudogene of this gene
            is located on the X chromosome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Feb 2012].
            
            Transcript Variant: This variant (5) uses an alternate 5' exon
            structure and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG and result in an isoform (2) with a
            shorter N-terminus, compared to isoform 1. Variants 2, 4, and 5
            encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HY164345.1, HY165508.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2142348,
                                           SAMEA2146236 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..99
                     /product="biogenesis of lysosome-related organelles
                     complex 1 subunit 2 isoform 2"
                     /note="centrosome protein oncogene; biogenesis of
                     lysosome-related organelles complex 1 subunit 2;
                     centrosomal 10 kDa protein; BLOC-1 subunit 2; 11 kDa
                     centrosome associated protein"
                     /calculated_mol_wt=11358
     Region          1..94
                     /region_name="BLOC1_2"
                     /note="Biogenesis of lysosome-related organelles complex-1
                     subunit 2; pfam10046"
                     /db_xref="CDD:462951"
     CDS             1..99
                     /gene="BLOC1S2"
                     /gene_synonym="BLOS2; BORCS2; CEAP; CEAP11"
                     /coded_by="NM_001282438.1:153..452"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="GeneID:282991"
                     /db_xref="HGNC:HGNC:20984"
                     /db_xref="MIM:609768"
ORIGIN      
        1 mfskmatylt geltatsedy kllenmnklt slkylemkdi ainisrnlkd lnqkyaglqp
       61 yldqinviee qvaaleqaay kldayskkle akykklekr
//
LOCUS       NP_996885                112 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 9 [Homo sapiens].
ACCESSION   NP_996885
VERSION     NP_996885.1
DBSOURCE    REFSEQ: accession NM_207002.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 112)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 112)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 112)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 112)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 112)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 112)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 112)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 112)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 112)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 112)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            AY352518.1 and AA890664.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (9, also known as Bim-gamma) lacks
            several exons and includes an alternate 3' terminal exon, compared
            to variant 1. The resulting isoform (9) has a distinct and shorter
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY352518.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1965299, SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..112
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..112
                     /product="bcl-2-like protein 11 isoform 9"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=12281
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     CDS             1..112
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_207002.3:289..627"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS2092.1"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qdrspapmsc dkstqtpspp
       61 cqafnhylsa mvviledigd lslcfgfift gldlyghhhs qdteqlnhkd fs
//
LOCUS       NP_060908                293 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 6 [Homo sapiens].
ACCESSION   NP_060908
VERSION     NP_060908.1
DBSOURCE    REFSEQ: accession NM_018438.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 293)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 293)
  AUTHORS   Satoh,T., Yagi-Utsumi,M., Ishii,N., Mizushima,T., Yagi,H., Kato,R.,
            Tachida,Y., Tateno,H., Matsuo,I., Kato,K., Suzuki,T. and Yoshida,Y.
  TITLE     Structural basis of sugar recognition by SCFFBS2 ubiquitin ligase
            involved in NGLY1 deficiency
  JOURNAL   FEBS Lett 598 (18), 2259-2268 (2024)
   PUBMED   39171510
  REMARK    GeneRIF: Structural basis of sugar recognition by SCF[FBS2]
            ubiquitin ligase involved in NGLY1 deficiency.
REFERENCE   3  (residues 1 to 293)
  AUTHORS   Li,G., Shi,W., Xu,Y., Li,K., Chen,Z., Lv,M., Lv,J., Qiu,T.,
            Qian,Q., Ji,J., Liu,W., Liu,B. and Zhao,Y.
  TITLE     The USP18-FBXO6 axis maintains the malignancy of ovarian cancer
  JOURNAL   Biochem Biophys Res Commun 593, 101-107 (2022)
   PUBMED   35063764
  REMARK    GeneRIF: The USP18-FBXO6 axis maintains the malignancy of ovarian
            cancer.
REFERENCE   4  (residues 1 to 293)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 293)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 293)
  AUTHORS   Yoshida,Y., Tokunaga,F., Chiba,T., Iwai,K., Tanaka,K. and Tai,T.
  TITLE     Fbs2 is a new member of the E3 ubiquitin ligase family that
            recognizes sugar chains
  JOURNAL   J Biol Chem 278 (44), 43877-43884 (2003)
   PUBMED   12939278
  REMARK    GeneRIF: Fbs2 is a novel member of F-box protein family that
            recognizes N-glycans and plays a role in ERAD
REFERENCE   7  (residues 1 to 293)
  AUTHORS   Ilyin,G.P., Serandour,A.L., Pigeon,C., Rialland,M., Glaise,D. and
            Guguen-Guillouzo,C.
  TITLE     A new subfamily of structurally related human F-box proteins
  JOURNAL   Gene 296 (1-2), 11-20 (2002)
   PUBMED   12383498
REFERENCE   8  (residues 1 to 293)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   9  (residues 1 to 293)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 293)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314989.1, BC020880.1 and
            AF129536.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class, and its C-terminal region is highly
            similar to that of rat NFB42 (neural F Box 42 kDa) which may be
            involved in the control of the cell cycle. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF129536.1, BC020880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376753.9/ ENSP00000365944.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..293
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..293
                     /product="F-box only protein 6"
                     /note="F-box protein Fbx6; F-box protein FBG2;
                     F-box/G-domain protein 2; F-box protein that recognizes
                     sugar chains 2"
                     /calculated_mol_wt=33802
     Region          12..92
                     /region_name="F-box_FBXO6-like"
                     /note="F-box domain found in F-box only proteins FBXO6,
                     FBXO44 and similar proteins; cd22168"
                     /db_xref="CDD:438939"
     Site            order(12..14,16..17,20,24,27,29,31..32,34,37..42,44..45,
                     77)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438939"
     Region          79..257
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRD1.1)"
     Region          261..285
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRD1.1)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NRD1.1)"
     CDS             1..293
                     /gene="FBXO6"
                     /gene_synonym="FBG2; FBS2; FBX6; Fbx6b"
                     /coded_by="NM_018438.6:60..941"
                     /db_xref="CCDS:CCDS133.1"
                     /db_xref="GeneID:26270"
                     /db_xref="HGNC:HGNC:13585"
                     /db_xref="MIM:605647"
ORIGIN      
        1 mdaphskaal dsinelpeni llelfthvpa rqlllncrlv cslwrdlidl mtlwkrkclr
       61 egfitkdwdq pvadwkifyf lrslhrnllr npcaeedmfa wqidfnggdr wkveslpgah
      121 gtdfpdpkvk kyfvtsyemc lksqlvdlva egyweelldt frpdivvkdw faaradcgct
      181 yqlkvqlasa dyfvlasfep ppvtiqqwnn atwtevsytf sdyprgvryi lfqhggrdtq
      241 ywagwygprv tnssivvspk mtrnqassea qpgqkhgqee aaqspyravv qif
//
LOCUS       NP_001028255             280 aa            linear   PRI 20-NOV-2025
DEFINITION  phenazine biosynthesis-like domain-containing protein isoform b
            [Homo sapiens].
ACCESSION   NP_001028255
VERSION     NP_001028255.1
DBSOURCE    REFSEQ: accession NM_001033083.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Hou,P., Zhu,H., Chu,F., Gao,Y., Sun,X., Zhang,F., Wang,X., Feng,Y.,
            Li,X., Liu,Y., Wang,J., Wang,X., He,D.C., Wang,H. and He,H.
  TITLE     Phenazine biosynthesis-like domain-containing protein (PBLD) and
            Cedrelone promote antiviral immune response by activating NF-kB
  JOURNAL   Nat Commun 16 (1), 496 (2025)
   PUBMED   39779683
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 280)
  AUTHORS   Zhu,H., Hou,P., Chu,F., Li,X., Zhang,W., Sun,X., Liu,Y., Zhao,G.,
            Gao,Y., He,D.C., Wang,H. and He,H.
  TITLE     PBLD promotes IRF3 mediated the type I interferon (IFN-I) response
            and apoptosis to inhibit viral replication
  JOURNAL   Cell Death Dis 15 (10), 727 (2024)
   PUBMED   39362857
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 280)
  AUTHORS   Han,L., Lin,X., Yan,Q., Gu,C., Li,M., Pan,L., Meng,Y., Zhao,X.,
            Liu,S. and Li,A.
  TITLE     PBLD inhibits angiogenesis via impeding VEGF/VEGFR2-mediated
            microenvironmental cross-talk between HCC cells and endothelial
            cells
  JOURNAL   Oncogene 41 (13), 1851-1865 (2022)
   PUBMED   35140333
  REMARK    GeneRIF: PBLD inhibits angiogenesis via impeding
            VEGF/VEGFR2-mediated microenvironmental cross-talk between HCC
            cells and endothelial cells.
REFERENCE   4  (residues 1 to 280)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 280)
  AUTHORS   Zhu,M., Wang,F., Mi,H., Li,L., Wang,J., Han,M. and Gu,Y.
  TITLE     Long noncoding RNA MEG3 suppresses cell proliferation, migration
            and invasion, induces apoptosis and paclitaxel-resistance via
            miR-4513/PBLD axis in breast cancer cells
  JOURNAL   Cell Cycle 19 (23), 3277-3288 (2020)
   PUBMED   33121324
  REMARK    GeneRIF: Long noncoding RNA MEG3 suppresses cell proliferation,
            migration and invasion, induces apoptosis and paclitaxel-resistance
            via miR-4513/PBLD axis in breast cancer cells.
REFERENCE   6  (residues 1 to 280)
  AUTHORS   Zhang,J., Kang,B., Tan,X., Bai,Z., Liang,Y., Xing,R., Shao,J.,
            Xu,N., Wang,R., Liu,S. and Lu,Y.
  TITLE     Comparative analysis of the protein profiles from primary gastric
            tumors and their adjacent regions: MAWBP could be a new protein
            candidate involved in gastric cancer
  JOURNAL   J Proteome Res 6 (11), 4423-4432 (2007)
   PUBMED   17929853
REFERENCE   7  (residues 1 to 280)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 280)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 280)
  AUTHORS   van Dijk,M., Mulders,J., Poutsma,A., Konst,A.A., Lachmeijer,A.M.,
            Dekker,G.A., Blankenstein,M.A. and Oudejans,C.B.
  TITLE     Maternal segregation of the Dutch preeclampsia locus at 10q22 with
            a new member of the winged helix gene family
  JOURNAL   Nat Genet 37 (5), 514-519 (2005)
   PUBMED   15806103
REFERENCE   10 (residues 1 to 280)
  AUTHORS   Iriyama,C., Matsuda,S., Katsumata,R. and Hamaguchi,M.
  TITLE     Cloning and sequencing of a novel human gene which encodes a
            putative hydroxylase
  JOURNAL   J Hum Genet 46 (5), 289-292 (2001)
   PUBMED   11355021
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC016395.5, CB121561.1, AI114748.1 and AI439144.1.
            
            Transcript Variant: This variant (2) includes a different 3'
            terminal exon compared to variant 1. The resulting protein (isoform
            b) has a shorter, distinct C-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q21.3"
     Protein         1..280
                     /product="phenazine biosynthesis-like domain-containing
                     protein isoform b"
                     /note="phenazine biosynthesis-like domain-containing
                     protein; MAWD-binding protein; epididymis secretory
                     protein Li 306; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=31278
     Region          1..249
                     /region_name="YHI9"
                     /note="Predicted epimerase YddE/YHI9, PhzF superfamily
                     [General function prediction only]; COG0384"
                     /db_xref="CDD:440153"
     CDS             1..280
                     /gene="PBLD"
                     /gene_synonym="HEL-S-306; MAWBP; MAWDBP"
                     /coded_by="NM_001033083.2:205..1047"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44413.1"
                     /db_xref="GeneID:64081"
                     /db_xref="HGNC:HGNC:23301"
                     /db_xref="MIM:612189"
ORIGIN      
        1 mklpifiada ftarafrgnp aavcllenel dedmhqkiar emnlsetafi rklhptdnfa
       61 qsscfglrwf tpasevplcg hatlasaavl fhkiknmnst ltfvtlsgel rarraedgiv
      121 ldlplypahp qdfhevedli ktaigntlvq dicyspdtqk llvrlsdvyn rsflenlkvn
      181 tenllqvent gkvkgliltl kgepggqtqa fdfysryfap wvgvaedpvt gsahavlssy
      241 wsqhlgkkem hgrtalyqfl fylpnsklvf llictiplkm
//
LOCUS       NP_004579                215 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel regulatory subunit beta-2 precursor [Homo sapiens].
ACCESSION   NP_004579
VERSION     NP_004579.1
DBSOURCE    REFSEQ: accession NM_004588.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Li,Y., Yuan,T., Huang,B., Zhou,F., Peng,C., Li,X., Qiu,Y., Yang,B.,
            Zhao,Y., Huang,Z. and Jiang,D.
  TITLE     Structure of human NaV1.6 channel reveals Na+ selectivity and pore
            blockade by 4,9-anhydro-tetrodotoxin
  JOURNAL   Nat Commun 14 (1), 1030 (2023)
   PUBMED   36823201
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Noland,C.L., Chua,H.C., Kschonsak,M., Heusser,S.A., Braun,N.,
            Chang,T., Tam,C., Tang,J., Arthur,C.P., Ciferri,C., Pless,S.A. and
            Payandeh,J.
  TITLE     Structure-guided unlocking of NaX reveals a non-selective
            tetrodotoxin-sensitive cation channel
  JOURNAL   Nat Commun 13 (1), 1416 (2022)
   PUBMED   35301303
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Li,X., Xu,F., Xu,H., Zhang,S., Gao,Y., Zhang,H., Dong,Y., Zheng,Y.,
            Yang,B., Sun,J., Zhang,X.C., Zhao,Y. and Jiang,D.
  TITLE     Structural basis for modulation of human NaV1.3 by clinical drug
            and selective antagonist
  JOURNAL   Nat Commun 13 (1), 1286 (2022)
   PUBMED   35277491
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Alsaloum,M., Labau,J.I.R., Sosniak,D., Zhao,P., Almomani,R.,
            Gerrits,M., Hoeijmakers,J.G.J., Lauria,G., Faber,C.G., Waxman,S.G.
            and Dib-Hajj,S.
  TITLE     A novel gain-of-function sodium channel beta2 subunit mutation in
            idiopathic small fiber neuropathy
  JOURNAL   J Neurophysiol 126 (3), 827-839 (2021)
   PUBMED   34320850
  REMARK    GeneRIF: A novel gain-of-function sodium channel beta2 subunit
            mutation in idiopathic small fiber neuropathy.
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Shen,H., Liu,D., Wu,K., Lei,J. and Yan,N.
  TITLE     Structures of human Nav1.7 channel in complex with auxiliary
            subunits and animal toxins
  JOURNAL   Science 363 (6433), 1303-1308 (2019)
   PUBMED   30765606
  REMARK    GeneRIF: this study reports the cryo-electron microscopy structures
            of the human Nav1.7-beta1-beta2 complex bound to two combinations
            of pore blockers and gating modifier toxins (GMTs), tetrodotoxin
            with protoxin-II and saxitoxin with huwentoxin-IV, both determined
            at overall resolutions of 3.2 angstroms.
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Eubanks,J., Srinivasan,J., Dinulos,M.B., Disteche,C.M. and
            Catterall,W.A.
  TITLE     Structure and chromosomal localization of the beta2 subunit of the
            human brain sodium channel
  JOURNAL   Neuroreport 8 (12), 2775-2779 (1997)
   PUBMED   9295116
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Isom,L.L., Ragsdale,D.S., De Jongh,K.S., Westenbroek,R.E.,
            Reber,B.F., Scheuer,T. and Catterall,W.A.
  TITLE     Structure and function of the beta 2 subunit of brain sodium
            channels, a transmembrane glycoprotein with a CAM motif
  JOURNAL   Cell 83 (3), 433-442 (1995)
   PUBMED   8521473
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Hartshorne,R.P. and Catterall,W.A.
  TITLE     The sodium channel from rat brain. Purification and subunit
            composition
  JOURNAL   J Biol Chem 259 (3), 1667-1675 (1984)
   PUBMED   6319405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP002800.4, DA290917.1 and
            BC036793.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is the beta 2 subunit of
            the type II voltage-gated sodium channel. The encoded protein is
            involved in cell-cell adhesion and cell migration. Defects in this
            gene can be a cause of Brugada Syndrome, atrial fibrillation, or
            sudden infant death syndrome. [provided by RefSeq, Jul 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.258744.1,
                                           SRR3476690.817100.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000278947.6/ ENSP00000278947.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..215
                     /product="sodium channel regulatory subunit beta-2
                     precursor"
                     /note="sodium channel, voltage-gated, type II, beta
                     polypeptide; sodium channel, voltage gated, type II beta
                     subunit; neuronal voltage-gated sodium channel beta 2
                     subunit; sodium channel regulatory subunit beta-2"
                     /calculated_mol_wt=21087
     sig_peptide     1..29
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3257
     mat_peptide     30..215
                     /product="Sodium channel regulatory subunit beta-2.
                     /id=PRO_0000014931"
                     /note="propagated from UniProtKB/Swiss-Prot (O60939.1)"
                     /calculated_mol_wt=21087
     Region          30..146
                     /region_name="IgV_P0-like"
                     /note="Immunoglobulin (Ig)-like domain of protein zero
                     (P0) and similar proteins; cd05715"
                     /db_xref="CDD:409380"
     Region          30..53
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409380"
     Region          30..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409380"
     Site            order(31,33,45,53,97,100,115..116)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:409380"
     Region          36..42
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409380"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60939.1)"
     Region          44..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409380"
     Region          54..63
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409380"
     Site            56
                     /site_type="other"
                     /note="Binds SCN2A. /evidence=ECO:0000305|PubMed:30765605;
                     propagated from UniProtKB/Swiss-Prot (O60939.1)"
     Region          63..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409380"
     Region          64..75
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409380"
     Site            66
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30765606,
                     ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H,
                     ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J; propagated
                     from UniProtKB/Swiss-Prot (O60939.1)"
     Site            74
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O60939.1)"
     Region          76..90
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409380"
     Region          77..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409380"
     Region          85..90
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409380"
     Region          95..129
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409380"
     Region          98..104
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409380"
     Region          108..116
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409380"
     Region          123..130
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409380"
     Region          131..137
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409380"
     Site            135
                     /site_type="other"
                     /note="Binds SCN2A. /evidence=ECO:0000305|PubMed:30765605;
                     propagated from UniProtKB/Swiss-Prot (O60939.1)"
     Region          138..146
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409380"
     Region          138..146
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409380"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60939.1)"
     Region          187..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60939.1)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54900; propagated from
                     UniProtKB/Swiss-Prot (O60939.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P54900; propagated from
                     UniProtKB/Swiss-Prot (O60939.1)"
     CDS             1..215
                     /gene="SCN2B"
                     /gene_synonym="ATFB14"
                     /coded_by="NM_004588.5:209..856"
                     /db_xref="CCDS:CCDS8390.1"
                     /db_xref="GeneID:6327"
                     /db_xref="HGNC:HGNC:10589"
                     /db_xref="MIM:601327"
ORIGIN      
        1 mhrdawlprp afsltglslf fslvppgrsm evtvpatlnv lngsdarlpc tfnscytvnh
       61 kqfslnwtyq ecnncseemf lqfrmkiinl klerfqdrve fsgnpskydv svmlrnvqpe
      121 degiyncyim nppdrhrghg kihlqvlmee pperdstvav ivgasvggfl avvilvlmvv
      181 kcvrrkkeqk lstddlktee egktdgegnp ddgak
//
LOCUS       NP_001340181             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340181
VERSION     NP_001340181.1
DBSOURCE    REFSEQ: accession NM_001353252.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.49723.1,
                                           SRR1660809.163513.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353252.1:141..1115"
                     /note="isoform 1 is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001124437             785 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001124437
VERSION     NP_001124437.1
DBSOURCE    REFSEQ: accession NM_001130965.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5, AB018353.1,
            AK022816.1 and BM689998.1.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (1) encodes isoform a. Variants 1,
            72, and 73 all encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142707.1, SRR1660809.107361.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000401592.6/ ENSP00000384015.1
            RefSeq Select criteria :: based on computational evidence
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..785
                     /product="SUN domain-containing protein 1 isoform a"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=86979
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <365..>589
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          417..470
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(417,420..421,424,427..428,431..432,434..435,
                     438..439,441..442,445..446,448..449,452,455..456,459,
                     462..463,466..467,469..470)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          547..605
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          648..783
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..785
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001130965.3:50..2407"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47525.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllaglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl qgdseafpwh
      361 wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas vrdavgqppr
      421 etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq llptvehlql
      481 eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl eqllqrfssq
      541 fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi teaqaraivn
      601 salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy fsqsprvviq
      661 pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap kdfavyglen
      721 eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe ytclyrfrvh
      781 gepvk
//
LOCUS       NP_005307                548 aa            linear   PRI 20-NOV-2025
DEFINITION  general transcription factor IIH subunit 1 [Homo sapiens].
ACCESSION   NP_005307
VERSION     NP_005307.1
DBSOURCE    REFSEQ: accession NM_005316.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Mistry,H., Kumari,S., Aswal,V.K. and Gupta,G.D.
  TITLE     Structural characterization of transcription-coupled repair protein
            UVSSA and its interaction with TFIIH protein
  JOURNAL   Int J Biol Macromol 247, 125792 (2023)
   PUBMED   37442507
  REMARK    GeneRIF: Structural characterization of transcription-coupled
            repair protein UVSSA and its interaction with TFIIH protein.
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Geng,T., Li,M., Chen,R., Yang,S., Jin,G., Jin,T. and Chen,F.
  TITLE     Impact of GTF2H1 and RAD54L2 polymorphisms on the risk of lung
            cancer in the Chinese Han population
  JOURNAL   BMC Cancer 22 (1), 1181 (2022)
   PUBMED   36384536
  REMARK    GeneRIF: Impact of GTF2H1 and RAD54L2 polymorphisms on the risk of
            lung cancer in the Chinese Han population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Okuda,M., Suwa,T., Suzuki,H., Yamaguchi,Y. and Nishimura,Y.
  TITLE     Three human RNA polymerases interact with TFIIH via a common RPB6
            subunit
  JOURNAL   Nucleic Acids Res 50 (1), 1-16 (2022)
   PUBMED   34268577
  REMARK    GeneRIF: Three human RNA polymerases interact with TFIIH via a
            common RPB6 subunit.
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Tong,X., Drapkin,R., Reinberg,D. and Kieff,E.
  TITLE     The 62- and 80-kDa subunits of transcription factor IIH mediate the
            interaction with Epstein-Barr virus nuclear protein 2
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3259-3263 (1995)
   PUBMED   7724549
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Shiekhattar,R., Mermelstein,F., Fisher,R.P., Drapkin,R.,
            Dynlacht,B., Wessling,H.C., Morgan,D.O. and Reinberg,D.
  TITLE     Cdk-activating kinase complex is a component of human transcription
            factor TFIIH
  JOURNAL   Nature 374 (6519), 283-287 (1995)
   PUBMED   7533895
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Fischer,L., Gerard,M., Chalut,C., Lutz,Y., Humbert,S., Kanno,M.,
            Chambon,P. and Egly,J.M.
  TITLE     Cloning of the 62-kilodalton component of basic transcription
            factor BTF2
  JOURNAL   Science 257 (5075), 1392-1395 (1992)
   PUBMED   1529339
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC084117.6, M95809.1, BC004452.1 and AI275181.1.
            
            Transcript Variant: This variant (1) represents the shorter
            transcript.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extent of this RefSeq
            transcript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.142593.1,
                                           SRR1660803.186574.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265963.9/ ENSP00000265963.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.1"
     Protein         1..548
                     /product="general transcription factor IIH subunit 1"
                     /note="BTF2 p62; basic transcription factor 2 62 kDa
                     subunit; general transcription factor IIH polypeptide 1;
                     TFIIH basal transcription factor complex p62 subunit;
                     general transcription factor IIH, polypeptide 1, 62kDa;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=61901
     Region          9..102
                     /region_name="PH_TFIIH"
                     /note="Transcription Factor II H (TFIIH) Pleckstrin
                     homology (PH) domain; cd13229"
                     /db_xref="CDD:270049"
     Site            order(19,54..57,60,64..66,76,78,93,97)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270049"
     Region          101..148
                     /region_name="BSD"
                     /note="domain in transcription factors and
                     synapse-associated proteins; smart00751"
                     /db_xref="CDD:128990"
     Region          182..232
                     /region_name="BSD"
                     /note="domain in transcription factors and
                     synapse-associated proteins; smart00751"
                     /db_xref="CDD:128990"
     Site            240
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBA9; propagated from
                     UniProtKB/Swiss-Prot (P32780.1)"
     Region          321..340
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P32780.1)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32780.1)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P32780.1)"
     CDS             1..548
                     /gene="GTF2H1"
                     /gene_synonym="BTF2; P62; TFB1; TFIIH"
                     /coded_by="NM_005316.4:190..1836"
                     /db_xref="CCDS:CCDS7838.1"
                     /db_xref="GeneID:2965"
                     /db_xref="HGNC:HGNC:4655"
                     /db_xref="MIM:189972"
ORIGIN      
        1 matsseevll ivkkvrqkkq dgalylmaer iawapegkdr ftishmyadi kcqkispegk
       61 akiqlqlvlh agdttnfhfs nestavkerd avkdllqqll pkfkrkanke leeknrmlqe
      121 dpvlfqlykd lvvsqvisae efwanrlnvn atdssstsnh kqdvgisaaf ladvrpqtdg
      181 cnglrynlts diiesifrty pavkmkyaen vphnmtekef wtrffqshyf hrdrlntgsk
      241 dlfaecakid ekglktmvsl gvknplldlt aledkpldeg ygissvpsas nsksikensn
      301 aaiikrfnhh samvlaaglr kqeaqneqts epsnmdgnsg dadcfqpavk raklqesiey
      361 edlgknnsvk tialnlkksd ryyhgptpiq slqyatsqdi insfqsirqe meaytpkltq
      421 vlsssaasst italspggal mqggtqqain qmvpndiqse lkhlyvavge llrhfwscfp
      481 vntpfleekv vkmksnlerf qvtklcpfqe kirrqylstn lvshieemlq taynklhtwq
      541 srrlmkkt
//
LOCUS       NP_001007249             588 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 599 [Homo sapiens].
ACCESSION   NP_001007249 XP_086046
VERSION     NP_001007249.1
DBSOURCE    REFSEQ: accession NM_001007248.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055225.1 and AC020910.7.
            
            On Nov 26, 2004 this sequence version replaced XP_086046.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055225.1, SRR1803611.15021.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329285.13/ ENSP00000333802.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..588
                     /product="zinc finger protein 599"
                     /calculated_mol_wt=67361
     Region          9..69
                     /region_name="KRAB"
                     /note="krueppel associated box; smart00349"
                     /db_xref="CDD:214630"
     Region          201..221
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          229..249
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          253..>580
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          257..277
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(262,264,266,268..269,272..273,276,290,292,296..297,
                     300..301,304,318,320,322,324..325,328..329,332)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          285..305
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          313..333
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          341..361
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          369..389
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(374,376,378,380..381,384..385,388,402,404,408..409,
                     412..413,416,430,432,434,436..437,440..441,444)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          397..417
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          425..445
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          453..473
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          481..501
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(486,488,490,492..493,496..497,500,514,516,520..521,
                     524..525,528,542,544,546,548..549,552..553,556)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          509..529
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          537..557
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          565..585
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..588
                     /gene="ZNF599"
                     /coded_by="NM_001007248.3:375..2141"
                     /db_xref="CCDS:CCDS32991.1"
                     /db_xref="GeneID:148103"
                     /db_xref="HGNC:HGNC:26408"
ORIGIN      
        1 maapalalvs fedvvvtftg eewghldlaq rtlyqevmle tcrllvslgh pvpkpeliyl
       61 lehgqelwtv krglsqstca gekakpkite ptasqlafse essfqellaq rssrdsrlgq
      121 ardeekliki qegnlrpgtn phkeicpekl sykhddlepd dslglrvlqe rvtpqdalhe
      181 cdsqgpgkdp mtdarnnpyt ctecgkgfsk kwalvrhqqi hagvkpyecn ecgkacryma
      241 dvirhmrlht gekpykciec gkafkrrfhl tehqrihtgd kpyeckecgk afthrssfiq
      301 hnmthtrekp flckecgkaf yysssfaqhm rihtgkklye cgecgkafth rstfiqhnvt
      361 htgekpflck ecgktfclns sftqhmriht gekpyecgec gkafthrstf irhkrthtge
      421 kpfeckecgk afcdsssliq hmrihtgekp yecsecgkaf thhsvfirhn rthsgqkple
      481 ckecakafyy sssftrhmri htgekpyvcr ecgkaftqpa nfvrhnriht gekpfeckec
      541 ekafcdnfal tqhmrthtge kpfecnecgk tfshsssfth hrkihtrv
//
LOCUS       NP_001340180             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340180 XP_016869036
VERSION     NP_001340180.1
DBSOURCE    REFSEQ: accession NM_001353251.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869036.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.280185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353251.1:510..1484"
                     /note="isoform 1 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_009185                521 aa            linear   PRI 20-NOV-2025
DEFINITION  bifunctional polynucleotide phosphatase/kinase [Homo sapiens].
ACCESSION   NP_009185
VERSION     NP_009185.2
DBSOURCE    REFSEQ: accession NM_007254.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 521)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 521)
  AUTHORS   Chakraborty,A., Sreenivasmurthy,S.G., Miller,W., Huai,W.,
            Biswas,T., Mandal,S.M., Bosca,L., Krishnan,B., Ghosh,G. and
            Hazra,T.
  TITLE     Fructose-2,6-bisphosphate restores DNA repair activity of PNKP and
            ameliorates neurodegenerative symptoms in Huntington's disease
  JOURNAL   Proc Natl Acad Sci U S A 121 (39), e2406308121 (2024)
   PUBMED   39298485
  REMARK    GeneRIF: Fructose-2,6-bisphosphate restores DNA repair activity of
            PNKP and ameliorates neurodegenerative symptoms in Huntington's
            disease.
REFERENCE   3  (residues 1 to 521)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   4  (residues 1 to 521)
  AUTHORS   Shen,J., Gilmore,E.C., Marshall,C.A., Haddadin,M., Reynolds,J.J.,
            Eyaid,W., Bodell,A., Barry,B., Gleason,D., Allen,K., Ganesh,V.S.,
            Chang,B.S., Grix,A., Hill,R.S., Topcu,M., Caldecott,K.W.,
            Barkovich,A.J. and Walsh,C.A.
  TITLE     Mutations in PNKP cause microcephaly, seizures and defects in DNA
            repair
  JOURNAL   Nat Genet 42 (3), 245-249 (2010)
   PUBMED   20118933
  REMARK    GeneRIF: The neurological abnormalities in individuals with
            microcephaly, early onset, intractable seizures and develomental
            delays may reflect a role for PNKP in several DNA repair pathways.
REFERENCE   5  (residues 1 to 521)
  AUTHORS   Chappell,C., Hanakahi,L.A., Karimi-Busheri,F., Weinfeld,M. and
            West,S.C.
  TITLE     Involvement of human polynucleotide kinase in double-strand break
            repair by non-homologous end joining
  JOURNAL   EMBO J 21 (11), 2827-2832 (2002)
   PUBMED   12032095
  REMARK    GeneRIF: Involvement of human polynucleotide kinase in
            double-strand break repair by non-homologous end joining
REFERENCE   6  (residues 1 to 521)
  AUTHORS   Whitehouse,C.J., Taylor,R.M., Thistlethwaite,A., Zhang,H.,
            Karimi-Busheri,F., Lasko,D.D., Weinfeld,M. and Caldecott,K.W.
  TITLE     XRCC1 stimulates human polynucleotide kinase activity at damaged
            DNA termini and accelerates DNA single-strand break repair
  JOURNAL   Cell 104 (1), 107-117 (2001)
   PUBMED   11163244
REFERENCE   7  (residues 1 to 521)
  AUTHORS   Karimi-Busheri,F., Daly,G., Robins,P., Canas,B., Pappin,D.J.,
            Sgouros,J., Miller,G.G., Fakhrai,H., Davis,E.M., Le Beau,M.M. and
            Weinfeld,M.
  TITLE     Molecular characterization of a human DNA kinase
  JOURNAL   J Biol Chem 274 (34), 24187-24194 (1999)
   PUBMED   10446193
REFERENCE   8  (residues 1 to 521)
  AUTHORS   Jilani,A., Ramotar,D., Slack,C., Ong,C., Yang,X.M., Scherer,S.W.
            and Lasko,D.D.
  TITLE     Molecular cloning of the human gene, PNKP, encoding a
            polynucleotide kinase 3'-phosphatase and evidence for its role in
            repair of DNA strand breaks caused by oxidative damage
  JOURNAL   J Biol Chem 274 (34), 24176-24186 (1999)
   PUBMED   10446192
REFERENCE   9  (residues 1 to 521)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   10 (residues 1 to 521)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC118341.2, BU541073.1 and
            BC033822.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 9, 2003 this sequence version replaced NP_009185.1.
            
            Summary: This locus represents a gene involved in DNA repair. In
            response to ionizing radiation or oxidative damage, the protein
            encoded by this locus catalyzes 5' phosphorylation and 3'
            dephosphorylation of nucleic acids. Mutations at this locus have
            been associated with microcephaly, seizures, and developmental
            delay.[provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.200165.1,
                                           SRR3476690.320790.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322344.8/ ENSP00000323511.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..521
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..521
                     /product="bifunctional polynucleotide phosphatase/kinase"
                     /EC_number="2.7.1.78"
                     /EC_number="3.1.3.32"
                     /note="Homo sapiens polynucleotide kinase 3'-phosphatase
                     (PNKP); DNA 5'-kinase/3'-phosphatase"
                     /calculated_mol_wt=56945
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96T60.1)"
     Region          2..521
                     /region_name="PNK-3'Pase"
                     /note="polynucleotide 5'-kinase 3'-phosphatase; TIGR01663"
                     /db_xref="CDD:130724"
     Region          109..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T60.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96T60.1)"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96T60.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96T60.1)"
     Region          146..337
                     /region_name="Phosphatase.
                     /evidence=ECO:0000250|UniProtKB:Q9JLV6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T60.1)"
     Region          341..516
                     /region_name="Kinase.
                     /evidence=ECO:0000250|UniProtKB:Q9JLV6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96T60.1)"
     CDS             1..521
                     /gene="PNKP"
                     /gene_synonym="AOA4; CMT2B2; EIEE10; MCSZ; PNK"
                     /coded_by="NM_007254.4:122..1687"
                     /db_xref="CCDS:CCDS12783.1"
                     /db_xref="GeneID:11284"
                     /db_xref="HGNC:HGNC:9154"
                     /db_xref="MIM:605610"
ORIGIN      
        1 mgeveapgrl wlesppggap piflpsdgqa lvlgrgpltq vtdrkcsrtq velvadpetr
       61 tvavkqlgvn psttgtqelk pglegslgvg dtlylvnglh pltlrweetr tpesqpdtpp
      121 gtplvsqdek rdaelpkkrm rksnpgwenl ekllvftaag vkpqgkvagf dldgtlittr
      181 sgkvfptgps dwrilypeip rklreleaeg yklviftnqm sigrgklpae efkakveavv
      241 eklgvpfqvl vathaglyrk pvtgmwdhlq eqandgtpis igdsifvgda agrpanwapg
      301 rkkkdfscad rlfalnlglp fatpeefflk wpaagfelpa fdprtvsrsg plclpesral
      361 lsaspevvva vgfpgagkst flkkhlvsag yvhvnrdtlg swqrcvttce talkqgkrva
      421 idntnpdaas raryvqcara agvpcrcflf tatleqarhn nrfremtdss hipvsdmvmy
      481 gyrkqfeapt laegfsaile ipfrlwvepr lgrlycqfse g
//
LOCUS       NP_037458                657 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of MON1-CCZ1 complex isoform 1 [Homo sapiens].
ACCESSION   NP_037458
VERSION     NP_037458.3
DBSOURCE    REFSEQ: accession NM_013326.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Yong,X., Jia,G., Liu,Z., Zhou,C., Yi,J., Tang,Y., Chen,L., Chen,L.,
            Wang,Y., Sun,Q., Billadeau,D.D., Su,Z. and Jia,D.
  TITLE     Cryo-EM structure of the Mon1-Ccz1-RMC1 complex reveals molecular
            basis of metazoan RAB7A activation
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2301725120 (2023)
   PUBMED   37216550
REFERENCE   2  (residues 1 to 657)
  AUTHORS   van den Boomen,D.J.H., Sienkiewicz,A., Berlin,I., Jongsma,M.L.M.,
            van Elsland,D.M., Luzio,J.P., Neefjes,J.J.C. and Lehner,P.J.
  TITLE     A trimeric Rab7 GEF controls NPC1-dependent lysosomal cholesterol
            export
  JOURNAL   Nat Commun 11 (1), 5559 (2020)
   PUBMED   33144569
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Vaites,L.P., Paulo,J.A., Huttlin,E.L. and Harper,J.W.
  TITLE     Systematic Analysis of Human Cells Lacking ATG8 Proteins Uncovers
            Roles for GABARAPs and the CCZ1/MON1 Regulator C18orf8/RMC1 in
            Macroautophagic and Selective Autophagic Flux
  JOURNAL   Mol Cell Biol 38 (1), e00392-17 (2017)
   PUBMED   29038162
  REMARK    GeneRIF: Authors identified C18orf8/RMC1 as a new subunit of the
            CCZ1-MON1 RAB7 guanine exchange factor (GEF) that positively
            regulates RAB7 recruitment to LE/autophagosomes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Yuan,M., Chen,J. and Zeng,Z.
  TITLE     Knockdown of macrophage inhibitory cytokine-1 in RPMI-8226 human
            multiple myeloma cells inhibits osteoclastic differentiation
            through inhibiting the RANKL-Erk1/2 signaling pathway
  JOURNAL   Mol Med Rep 14 (6), 5199-5204 (2016)
   PUBMED   27779672
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026634.11, AK057192.1, AC010853.11 and AK294169.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 7, 2006 this sequence version replaced NP_037458.2.
            
            Summary: This gene encodes a colon cancer associated protein.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.213648.1,
                                           SRR1660809.149168.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269221.8/ ENSP00000269221.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..657
                     /product="regulator of MON1-CCZ1 complex isoform 1"
                     /note="colon cancer-associated protein Mic1; macrophage
                     inhibitory cytokine 1; uncharacterized protein C18orf8; WD
                     repeat domain 98; WD repeat-containing protein 98;
                     regulator of MON1-CCZ1 complex"
                     /calculated_mol_wt=74844
     Region          475..632
                     /region_name="Mic1"
                     /note="Colon cancer-associated protein Mic1-like;
                     pfam07035"
                     /db_xref="CDD:429257"
     CDS             1..657
                     /gene="RMC1"
                     /gene_synonym="C18orf8; HsT2591; Mic-1; MIC1; WDR98"
                     /coded_by="NM_013326.5:109..2082"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32803.1"
                     /db_xref="GeneID:29919"
                     /db_xref="HGNC:HGNC:24326"
                     /db_xref="MIM:620267"
ORIGIN      
        1 mgeedyylel cerpvqfeka npvncvffde ankqvfavrs ggatgvvvkg pddrnpisfr
       61 mddkgevkci kfslenkila vqrtsktvdf cnfipdnsql eytqecktkn anilgfcwts
      121 steivfitdq giefyqvlpe krslkllksh nlnvnwymyc pesavillst tvlenvlqpf
      181 hfragtmskl pkfeielpaa pkstkpslse rdiamatiyg qlyvlflrhh srtsnstgae
      241 vvlyhlpreg ackkmhilkl nrtgkfalnv vdnlvvvhhq dtetsvifdi klrgefdgsv
      301 tfhhpvlpar siqpyqipit gpaavtsqsp vpcklysssw ivfqpdiiis asqgylwnlq
      361 vklepivnll pdkgrlmdfl lqrkeckmvi lsvcsqmlse sdraslpvia tvfdklnhey
      421 kkyldaeqsy amaveagqsr sspllkrpvr tqavldqsdv ythvlsafve kkemphkfvi
      481 avlmeyirsl nqfqiavqhy lhelviktlv qhnlfymlhq flqyhvlsds kplaclllsl
      541 esfyppahql sldmlkrlst andeivevll skhqvlaalr firgigghdn isarkfldaa
      601 kqtednmlfy tifrffeqrn qrlrgspnft pgehceehva ffkqifgdqa lmrpttf
//
LOCUS       NP_001315550             354 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 2, facilitated glucose transporter member 5
            isoform 4 [Homo sapiens].
ACCESSION   NP_001315550
VERSION     NP_001315550.1
DBSOURCE    REFSEQ: accession NM_001328621.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Song,A., Mao,Y. and Wei,H.
  TITLE     GLUT5: structure, functions, diseases and potential applications
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 55 (10), 1519-1538 (2023)
   PUBMED   37674366
  REMARK    GeneRIF: GLUT5: structure, functions, diseases and potential
            applications.
            Review article
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Cui,Y., Liu,H., Wang,Z., Zhang,H., Tian,J., Wang,Z., Song,W.,
            Guo,H., Liu,L., Tian,R., Zuo,X., Ren,S., Zhang,F. and Niu,R.
  TITLE     Fructose promotes angiogenesis by improving vascular endothelial
            cell function and upregulating VEGF expression in cancer cells
  JOURNAL   J Exp Clin Cancer Res 42 (1), 184 (2023)
   PUBMED   37507736
  REMARK    GeneRIF: Fructose promotes angiogenesis by improving vascular
            endothelial cell function and upregulating VEGF expression in
            cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Fiorentino,T.V., De Vito,F., Suraci,E., Marasco,R., Hribal,M.L.,
            Luzza,F. and Sesti,G.
  TITLE     Obesity and overweight are linked to increased sodium-glucose
            cotransporter 1 and glucose transporter 5 levels in duodenum
  JOURNAL   Obesity (Silver Spring) 31 (3), 724-731 (2023)
   PUBMED   36746764
  REMARK    GeneRIF: Obesity and overweight are linked to increased
            sodium-glucose cotransporter 1 and glucose transporter 5 levels in
            duodenum.
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Taneva,I., Grumann,D., Schmidt,D., Taneva,E., von Arnim,U.,
            Ansorge,T. and Wex,T.
  TITLE     Gene variants of the SLC2A5 gene encoding GLUT5, the major fructose
            transporter, do not contribute to clinical presentation of acquired
            fructose malabsorption
  JOURNAL   BMC Gastroenterol 22 (1), 167 (2022)
   PUBMED   35387598
  REMARK    GeneRIF: Gene variants of the SLC2A5 gene encoding GLUT5, the major
            fructose transporter, do not contribute to clinical presentation of
            acquired fructose malabsorption.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Mahraoui,L., Takeda,J., Mesonero,J., Chantret,I., Dussaulx,E.,
            Bell,G.I. and Brot-Laroche,E.
  TITLE     Regulation of expression of the human fructose transporter (GLUT5)
            by cyclic AMP
  JOURNAL   Biochem J 301 (Pt 1) (Pt 1), 169-175 (1994)
   PUBMED   8037665
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Rand,E.B., Depaoli,A.M., Davidson,N.O., Bell,G.I. and Burant,C.F.
  TITLE     Sequence, tissue distribution, and functional characterization of
            the rat fructose transporter GLUT5
  JOURNAL   Am J Physiol 264 (6 Pt 1), G1169-G1176 (1993)
   PUBMED   8333543
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Burant,C.F., Takeda,J., Brot-Laroche,E., Bell,G.I. and
            Davidson,N.O.
  TITLE     Fructose transporter in human spermatozoa and small intestine is
            GLUT5
  JOURNAL   J Biol Chem 267 (21), 14523-14526 (1992)
   PUBMED   1634504
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Davidson,N.O., Hausman,A.M., Ifkovits,C.A., Buse,J.B., Gould,G.W.,
            Burant,C.F. and Bell,G.I.
  TITLE     Human intestinal glucose transporter expression and localization of
            GLUT5
  JOURNAL   Am J Physiol 262 (3 Pt 1), C795-C800 (1992)
   PUBMED   1550217
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Kayano,T., Burant,C.F., Fukumoto,H., Gould,G.W., Fan,Y.S.,
            Eddy,R.L., Byers,M.G., Shows,T.B., Seino,S. and Bell,G.I.
  TITLE     Human facilitative glucose transporters. Isolation, functional
            characterization, and gene localization of cDNAs encoding an
            isoform (GLUT5) expressed in small intestine, kidney, muscle, and
            adipose tissue and an unusual glucose transporter pseudogene-like
            sequence (GLUT6)
  JOURNAL   J Biol Chem 265 (22), 13276-13282 (1990)
   PUBMED   1695905
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158048.35.
            
            Summary: The protein encoded by this gene is a fructose transporter
            responsible for fructose uptake by the small intestine. The encoded
            protein also is necessary for the increase in blood pressure due to
            high dietary fructose consumption. [provided by RefSeq, Jun 2016].
            
            Transcript Variant: This variant (5) lacks three alternate coding
            exons compared to variant 1. The resulting isoform (4) is shorter
            at the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR18074968.1484041.1,
                                    SRR14038191.1455622.1 [ECO:0000331]
            RNAseq introns       :: mixed/partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.23"
     Protein         1..354
                     /product="solute carrier family 2, facilitated glucose
                     transporter member 5 isoform 4"
                     /note="glucose transporter-like protein 5; glucose
                     transporter type 5, small intestine; solute carrier family
                     2 (facilitated glucose/fructose transporter), member 5;
                     testicular tissue protein Li 81"
                     /calculated_mol_wt=38883
     Region          <1..324
                     /region_name="MFS"
                     /note="Major Facilitator Superfamily; cl28910"
                     /db_xref="CDD:475125"
     CDS             1..354
                     /gene="SLC2A5"
                     /gene_synonym="GLUT-5; GLUT5"
                     /coded_by="NM_001328621.2:156..1220"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:6518"
                     /db_xref="HGNC:HGNC:11010"
                     /db_xref="MIM:138230"
ORIGIN      
        1 mylgelapkn lrgalgvvpq lfitvgilva qifglrnlla nvdgwpillg ltgvpaalql
       61 lllpffpesp rylliqkkde aaakkalqtl rgwdsvdrev aeirqedeae kaagfisvlk
      121 lfrmrslrwq llsiivlmgg qqlsgvnaiy yyadqiylsa gvpeehvqyv tagtgavnvv
      181 mtfcavfvve llgrrlllll gfsicliacc vltaalalqd tvswmpyisi vcvisyvigh
      241 algpspipal liteiflqss rpsafmvggs vhwlsnftvg lifpfiqegl gpysfivfav
      301 icllttiyif livpetkakt fieinqiftk mnkvsevype keelkelppv tseq
//
LOCUS       NP_001354425             991 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory ankyrin repeat
            subunit B isoform D [Homo sapiens].
ACCESSION   NP_001354425 XP_016860741
VERSION     NP_001354425.1
DBSOURCE    REFSEQ: accession NM_001367496.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 991)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 991)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 991)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 991)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 991)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 991)
  AUTHORS   Kariuki,S.N., Ghodke-Puranik,Y., Dorschner,J.M., Chrabot,B.S.,
            Kelly,J.A., Tsao,B.P., Kimberly,R.P., Alarcon-Riquelme,M.E.,
            Jacob,C.O., Criswell,L.A., Sivils,K.L., Langefeld,C.D.,
            Harley,J.B., Skol,A.D. and Niewold,T.B.
  TITLE     Genetic analysis of the pathogenic molecular sub-phenotype
            interferon-alpha identifies multiple novel loci involved in
            systemic lupus erythematosus
  JOURNAL   Genes Immun 16 (1), 15-23 (2015)
   PUBMED   25338677
REFERENCE   7  (residues 1 to 991)
  AUTHORS   Kapoor,M., Wang,J.C., Wetherill,L., Le,N., Bertelsen,S.,
            Hinrichs,A.L., Budde,J., Agrawal,A., Almasy,L., Bucholz,K.,
            Dick,D.M., Harari,O., Xiaoling,X., Hesselbrock,V., Kramer,J.,
            Nurnberger,J.I. Jr., Rice,J., Schuckit,M., Tischfield,J.,
            Porjesz,B., Edenberg,H.J., Bierut,L., Foroud,T. and Goate,A.
  TITLE     Genome-wide survival analysis of age at onset of alcohol dependence
            in extended high-risk COGA families
  JOURNAL   Drug Alcohol Depend 142, 56-62 (2014)
   PUBMED   24962325
REFERENCE   8  (residues 1 to 991)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 991)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 991)
  AUTHORS   Dechamps,C., Bach,S., Portetelle,D. and Vandenbol,M.
  TITLE     The Tre2 oncoprotein, implicated in Ewing's sarcoma, interacts with
            two components of the cytoskeleton
  JOURNAL   Biotechnol Lett 28 (4), 223-231 (2006)
   PUBMED   16555005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010746.8, AC013264.4 and AC017035.6.
            
            On Dec 4, 2018 this sequence version replaced XP_016860741.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.271802.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..991
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..991
                     /product="serine/threonine-protein phosphatase 6
                     regulatory ankyrin repeat subunit B isoform D"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     ankyrin repeat subunit B; ankyrin repeat domain-containing
                     protein 44; serine/threonine-protein phosphatase 6
                     regulatory subunit ARS-B"
                     /calculated_mol_wt=107357
     Region          7..36
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          10..61
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Region          11..38
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..71
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..69
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          54..343
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          73..102
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          76..104
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(79..80,83..85,87..88,92,95,104,106,108,112..113,
                     116..118,120..121,125,128,137,139,141,145..146,149..151,
                     153..154,158,161,170)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          106..135
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          139..170
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          139..168
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          172..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          172..201
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          205..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..234
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..267
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          253..534
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..301
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          305..336
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          305..334
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          338..367
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          371..400
                     /region_name="ANK 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          375..402
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(404,406,410..411,414..416,418..419,423,426,435,437,
                     439,443..444,447..449,451..452,456,459,468,470,472,
                     476..477,489..491,493..494,517,520,529)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          404..435
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          404..433
                     /region_name="ANK 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          437..468
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          437..466
                     /region_name="ANK 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          470..529
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          470..498
                     /region_name="ANK 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          492..749
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          531..562
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          531..561
                     /region_name="ANK 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          564..597
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          566..595
                     /region_name="ANK 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          599..628
                     /region_name="ANK 18"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          600..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(601,605..606,609..611,613..614,618,621,630,633,635,
                     639..640,643..645,647..648,652,655,667,669,671,675..676,
                     679..681,683..684,688,691,700)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          633..667
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..662
                     /region_name="ANK 19"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          650..976
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          669..700
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          669..698
                     /region_name="ANK 20"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          702..733
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          702..731
                     /region_name="ANK 21"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          735..764
                     /region_name="ANK 22"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          771..836
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          771..800
                     /region_name="ANK 23"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          803..832
                     /region_name="ANK 24"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          838..867
                     /region_name="ANK 25"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          839..869
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(840,844..845,848..850,852..853,857,860,869,871,873,
                     877..878,881..883,885..886,890,894,903,905,907,911..912,
                     915..917,919..920,924,927,936)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          871..903
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          871..901
                     /region_name="ANK 26"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          905..936
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          905..934
                     /region_name="ANK 27"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          941..972
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          941..970
                     /region_name="ANK 28"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     CDS             1..991
                     /gene="ANKRD44"
                     /gene_synonym="ARSB; PP6-ARS-B"
                     /coded_by="NM_001367496.1:177..3152"
                     /note="isoform D is encoded by transcript variant E"
                     /db_xref="GeneID:91526"
                     /db_xref="HGNC:HGNC:25259"
                     /db_xref="MIM:620861"
ORIGIN      
        1 mavlkltdqp plvqaifsgd peeirmlihk tedvntldse krtplhvaaf lgdaeiiell
       61 ilsgarvnak dnmwltplhr avasrseeav qvlikhsadv nardknwqtp lhvaaankav
      121 kcaeviipll ssvnvsdrgg rtalhhaaln ghvemvnlll akganinafd kkdrralhwa
      181 aymghldvva llinhgaevt ckdkkgytpl haaasngqin vvkhllnlgv eideinvygn
      241 talhiacyng qdavvnelid yganvnqpnn ngftplhfaa asthgalcle llvnngadvn
      301 iqskdgkspl hmtavhgrft rsqtliqngg eidcvdkdgn tplhvaaryg hellintlit
      361 sgadtakcgi hsmfplhlaa lnahsdccrk llssgfeidt pdkfgrtclh aaaaggnvec
      421 ikllqssgad fhkkdkcgrt plhyaaanch fhcietlvtt ganvnetddw grtalhyaaa
      481 sdmdrnktil gnahdnseel erarelkeke atlclefllq ndanpsirdk egynsihyaa
      541 ayghrqclel llertnsgfe esdsgatksp lhlaaynghh qalevllqsl vdldirdekg
      601 rtaldlaafk ghtecveali nqgasifvkd nvtkrtplha svinghtlcl rllleiadnp
      661 eavdvkdakg qtplmlavay ghidavslll ekeanvdtvd ilgctalhrg imtgheecvq
      721 mlleqevsil ckdsrgrtpl hyaaarghat wlsellqmal seedccfkdn qgytplhwac
      781 yngnenciev lleqkcfrkf ignpftplhc aiindhgnca slllgaidss ivscrddkgr
      841 tplhaaafad hveclqlllr hsapvnavdn sgktalmmaa engqagavdi lvnsaqadlt
      901 vkdkdlntpl hlacskghek callildkiq deslineknn alqtplhvaa rnglkvvvee
      961 llakgacvla vdengigiss sclflrskqp y
//
LOCUS       NP_001356710             223 aa            linear   PRI 20-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001356710 XP_006713708
VERSION     NP_001356710.1
DBSOURCE    REFSEQ: accession NM_001369781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 223)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 223)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 223)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 223)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 223)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 223)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 223)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 223)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 223)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 223)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            On Apr 18, 2019 this sequence version replaced XP_006713708.1.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.118474.1,
                                           SRR1803614.31099.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..223
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..223
                     /product="myeloid leukemia factor 1 isoform 7"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=25118
     Region          9..157
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..223
                     /gene="MLF1"
                     /coded_by="NM_001369781.1:139..810"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS93416.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mtpssrelre pgvrgragik htdvssfqtm dqmvsnmrny mqklernfgq lsvdpnghsf
       61 csssvmtysk igdeppkvfq astqtrrapg giketrkamr dsdsglekma ighhihdrah
      121 vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk ykpgrhnlgn trmrsvghen
      181 pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks nkk
//
LOCUS       NP_001354631             766 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform mmm [Homo sapiens].
ACCESSION   NP_001354631
VERSION     NP_001354631.1
DBSOURCE    REFSEQ: accession NM_001367702.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 766)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 766)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 766)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 766)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 766)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 766)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 766)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 766)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 766)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 766)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2155550,
                              SAMEA2467147 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..766
                     /product="SUN domain-containing protein 1 isoform mmm"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=84566
     Region          62..295
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <369..>593
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          421..474
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(421,424..425,428,431..432,435..436,438..439,
                     442..443,445..446,449..450,452..453,456,459..460,463,
                     466..467,470..471,473..474)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          551..609
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          652..>757
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..766
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367702.1:52..2352"
                     /note="isoform mmm is encoded by transcript variant 65"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld ahtaahsqsp
      241 rlpgragtlw hiwacagkaa sgvfwwlgig wyqfvtlisw lnvflltrcl rnickflvll
      301 iplflllagl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl kqplqgdsea
      361 fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag psasvrdavg
      421 qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa vgeqllptve
      481 hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq ggsleqllqr
      541 fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag asgiteaqar
      601 aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi plwyfsqspr
      661 vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni ssapkdfavy
      721 gleneyqeeg qllgqftydq dgeslqmfqa ltrrhsfpns gtsdff
//
LOCUS       NP_001354738             130 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box and leucine-rich protein 22 isoform 3 [Homo sapiens].
ACCESSION   NP_001354738
VERSION     NP_001354738.1
DBSOURCE    REFSEQ: accession NM_001367809.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 130)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 130)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 130)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 130)
  AUTHORS   Spaich,S., Will,R.D., Just,S., Spaich,S., Kuhn,C., Frank,D.,
            Berger,I.M., Wiemann,S., Korn,B., Koegl,M., Backs,J., Katus,H.A.,
            Rottbauer,W. and Frey,N.
  TITLE     F-box and leucine-rich repeat protein 22 is a cardiac-enriched
            F-box protein that regulates sarcomeric protein turnover and is
            essential for maintenance of contractile function in vivo
  JOURNAL   Circ Res 111 (12), 1504-1516 (2012)
   PUBMED   22972877
  REMARK    GeneRIF: Fbxl22 promotes the proteasome-dependent degradation of
            sarcomeric proteins and is essential for maintenance of normal
            contractile function.
REFERENCE   5  (residues 1 to 130)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC118274.9.
            
            Summary: This gene encodes a member of the F-box protein family.
            This F-box protein interacts with S-phase kinase-associated protein
            1A and cullin in order to form SCF complexes which function as
            ubiquitin ligases.[provided by RefSeq, Sep 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AI399808.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146982, SAMEA2147975
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..130
                     /product="F-box and leucine-rich protein 22 isoform 3"
                     /EC_number="3.4.19.12"
                     /note="F-box/LRR-repeat protein 22; F-box and leucine-rich
                     protein 22"
                     /calculated_mol_wt=14952
     Region          9..51
                     /region_name="F-box_FBXL22"
                     /note="F-box domain found in F-box/LRR-repeat protein 22
                     (FBXL22) and similar proteins; cd22129"
                     /db_xref="CDD:438901"
     Site            order(12,16,19..20,23..24,28,30..31,35..37,39)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438901"
     CDS             1..130
                     /gene="FBXL22"
                     /gene_synonym="Fbl22"
                     /coded_by="NM_001367809.1:7..399"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92015.1"
                     /db_xref="GeneID:283807"
                     /db_xref="HGNC:HGNC:27537"
                     /db_xref="MIM:609088"
ORIGIN      
        1 mwplltmhit qlnrecllhl fsfldkdsrk slartcsqlh dvfedpalws llhfrsltel
       61 qkdnfllgpa lrslsicwhs srvqvcsied wlksafqrsi csrheslvnd fllrvcdrvr
      121 glndtvapgt
//
LOCUS       NP_963923               1043 aa            linear   PRI 20-NOV-2025
DEFINITION  tight junction protein 2 isoform 2 [Homo sapiens].
ACCESSION   NP_963923
VERSION     NP_963923.1
DBSOURCE    REFSEQ: accession NM_201629.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Ouyang,H., Wu,S., Li,W., Grey,M.J., Wu,W. and Hansen,S.H.
  TITLE     p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP
  JOURNAL   Cell Rep 42 (12), 113486 (2023)
   PUBMED   37995182
  REMARK    GeneRIF: p120 RasGAP and ZO-2 are essential for Hippo signaling and
            tumor-suppressor function mediated by p190A RhoGAP.
REFERENCE   4  (residues 1 to 1043)
  AUTHORS   Walsh,T., Pierce,S.B., Lenz,D.R., Brownstein,Z.,
            Dagan-Rosenfeld,O., Shahin,H., Roeb,W., McCarthy,S., Nord,A.S.,
            Gordon,C.R., Ben-Neriah,Z., Sebat,J., Kanaan,M., Lee,M.K.,
            Frydman,M., King,M.C. and Avraham,K.B.
  TITLE     Genomic duplication and overexpression of TJP2/ZO-2 leads to
            altered expression of apoptosis genes in progressive nonsyndromic
            hearing loss DFNA51
  JOURNAL   Am J Hum Genet 87 (1), 101-109 (2010)
   PUBMED   20602916
  REMARK    GeneRIF: TJP2- and GSK-3beta-mediated increased susceptibility to
            apoptosis of cells of the inner ear is the mechanism for
            adult-onset hearing loss in this kindred and may serve as one model
            for age-related hearing loss in the general population.
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Itoh,M., Morita,K. and Tsukita,S.
  TITLE     Characterization of ZO-2 as a MAGUK family member associated with
            tight as well as adherens junctions with a binding affinity to
            occludin and alpha catenin
  JOURNAL   J Biol Chem 274 (9), 5981-5986 (1999)
   PUBMED   10026224
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Denker,B.M. and Nigam,S.K.
  TITLE     Molecular structure and assembly of the tight junction
  JOURNAL   Am J Physiol 274 (1), F1-F9 (1998)
   PUBMED   9458817
  REMARK    Review article
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   Beatch,M., Jesaitis,L.A., Gallin,W.J., Goodenough,D.A. and
            Stevenson,B.R.
  TITLE     The tight junction protein ZO-2 contains three PDZ
            (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced
            region
  JOURNAL   J Biol Chem 271 (42), 25723-25726 (1996)
   PUBMED   8824195
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Duclos,F., Rodius,F., Wrogemann,K., Mandel,J.L. and Koenig,M.
  TITLE     The Friedreich ataxia region: characterization of two novel genes
            and reduction of the critical region to 300 kb
  JOURNAL   Hum Mol Genet 3 (6), 909-914 (1994)
   PUBMED   7951235
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   Amendola,M. and Squires,J.E.
  TITLE     Pediatric Genetic Cholestatic Liver Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   36108118
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB090695.1, AK295016.1,
            AL358113.21, AK304447.1 and AA724570.1.
            
            Summary: This gene encodes a zonula occluden that is a member of
            the membrane-associated guanylate kinase homolog family. The
            encoded protein functions as a component of the tight junction
            barrier in epithelial and endothelial cells and is necessary for
            proper assembly of tight junctions. Mutations in this gene have
            been identified in patients with hypercholanemia, and genomic
            duplication of a 270 kb region including this gene causes autosomal
            dominant deafness-51. Alternatively spliced transcripts encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (2) lacks two in-frame exons in
            the 3' coding region, compared to variant (1). The encoded isoform
            (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.193838.1,
                                           SRR1660803.26079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.11"
     Protein         1..1043
                     /product="tight junction protein 2 isoform 2"
                     /note="Friedreich ataxia region gene X104 (tight junction
                     protein ZO-2); zona occludens 2; zonula occludens protein
                     2"
                     /calculated_mol_wt=117627
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          32..118
                     /region_name="PDZ1_ZO1-like"
                     /note="PDZ domain 1 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06727"
                     /db_xref="CDD:467209"
     Site            order(43..49,67,70,98,102,105..106)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467209"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          144..>226
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            150
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          152..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            163
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          183..>274
                     /region_name="SF-CC1"
                     /note="splicing factor, CC1-like family; TIGR01622"
                     /db_xref="CDD:273721"
     Site            200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          306..384
                     /region_name="PDZ2_ZO1-like_ds"
                     /note="PDZ domain 2 of Zonula Occludens-1 (ZO-1), ZO-2 and
                     ZO-3, and related domains; form domain-swapping dimers;
                     cd06728"
                     /db_xref="CDD:467210"
     Site            order(306..312,317..333,336..338,341,343..344,351,
                     359..360,362..363,375..381)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            order(318..324,330,333,363,367,370..371)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467210"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          408..506
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          509..590
                     /region_name="PDZ3_ZO1-like_domain"
                     /note="PDZ domain 3 of Zonula Occludens-1 (ZO-1), homologs
                     ZO-2 and ZO-3, and related domains; cd06729"
                     /db_xref="CDD:467211"
     Site            order(520..526,536,539,568,572,575..576)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467211"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Region          604..666
                     /region_name="SH3_ZO-2"
                     /note="Src homology 3 domain of the Tight junction
                     protein, Zonula occludens protein 2; cd12027"
                     /db_xref="CDD:212960"
     Site            order(613,615,618,622,643..644,660,662..663)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212960"
     Region          700..879
                     /region_name="GuKc"
                     /note="Guanylate kinase homologues; smart00072"
                     /db_xref="CDD:214504"
     Site            702
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z0U1; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            920
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            925
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     Site            933
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY2.2)"
     CDS             1..1043
                     /gene="TJP2"
                     /gene_synonym="C9DUPq21.11; DFNA51; DUP9q21.11; FHCA1;
                     PFIC4; X104; ZO2"
                     /coded_by="NM_201629.3:319..3450"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6628.1"
                     /db_xref="GeneID:9414"
                     /db_xref="HGNC:HGNC:11828"
                     /db_xref="MIM:607709"
ORIGIN      
        1 mpvrgdrgfp prrelsgwlr apgmeeliwe qytvtlqkds krgfgiavsg grdnphfeng
       61 etsivisdvl pggpadgllq endrvvmvng tpmedvlhsf avqqlrksgk vaaivvkrpr
      121 kvqvaalqas ppldqddraf evmdefdgrs frsgysersr lnshggrsrs wedspergrp
      181 herarsrerd lsrdrsrgrs lergldqdha rtrdrsrgrs lergldhdfg psrdrdrdrs
      241 rgrsidqdye rayhraydpd yerayspeyr rgarhdarsr gprsrsrehp hsrspspepr
      301 grpgpigvll mksraneeyg lrlgsqifvk emtrtglatk dgnlhegdii lkingtvten
      361 msltdarkli eksrgklqlv vlrdsqqtli nipslndsds eiediseies nrsfspeerr
      421 hqysdydyhs sseklkerps sredtpsrls rmgatptpfk stgdiagtvv petnkepryq
      481 edppapqpka aprtflrpsp edeaiygpnt kmvrfkkgds vglrlaggnd vgifvagiqe
      541 gtsaeqeglq egdqilkvnt qdfrglvred avlylleipk gemvtilaqs radvyrdila
      601 cgrgdsffir shfeceketp qslaftrgev frvvdtlydg klgnwlavri gnelekglip
      661 nksraeqmas vqnaqrdnag dradfwrmrg qrsgvkknlr ksredltavv svstkfpaye
      721 rvllreagfk rpvvlfgpia diameklane lpdwfqtakt epkdagseks tgvvrlntvr
      781 qiieqdkhal ldvtpkavdl lnytqwfpiv iffnpdsrqg vktmrqrlnp tsnkssrklf
      841 dqanklkktc ahlftatinl nsandswfgs lkdtiqhqqg eavwvsegkm egmdddpedr
      901 msyltamgad ylscdsrlis dfedtdgegg aytdneldep aeeplvssit rssepvqhee
      961 ieiaqkhpdi yavpikthkp dpgtpqhtss rppepqkaps rpyqdtrgsy gsdaeeeeyr
     1021 qqlsehskrg yygqsaryrd tel
//
LOCUS       NP_057131                125 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3B subunit 6 [Homo sapiens].
ACCESSION   NP_057131
VERSION     NP_057131.1
DBSOURCE    REFSEQ: accession NM_016047.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 125)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 125)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 125)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 125)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 125)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 125)
  AUTHORS   Will,C.L., Urlaub,H., Achsel,T., Gentzel,M., Wilm,M. and
            Luhrmann,R.
  TITLE     Characterization of novel SF3b and 17S U2 snRNP proteins, including
            a human Prp5p homologue and an SF3b DEAD-box protein
  JOURNAL   EMBO J 21 (18), 4978-4988 (2002)
   PUBMED   12234937
REFERENCE   7  (residues 1 to 125)
  AUTHORS   Zhou,Z., Licklider,L.J., Gygi,S.P. and Reed,R.
  TITLE     Comprehensive proteomic analysis of the human spliceosome
  JOURNAL   Nature 419 (6903), 182-185 (2002)
   PUBMED   12226669
REFERENCE   8  (residues 1 to 125)
  AUTHORS   Will,C.L., Schneider,C., MacMillan,A.M., Katopodis,N.F.,
            Neubauer,G., Wilm,M., Luhrmann,R. and Query,C.C.
  TITLE     A novel U2 and U11/U12 snRNP protein that associates with the
            pre-mRNA branch site
  JOURNAL   EMBO J 20 (16), 4536-4546 (2001)
   PUBMED   11500380
REFERENCE   9  (residues 1 to 125)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 125)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC015463.1 and BG200650.1.
            
            Summary: This gene encodes a 14 kDa protein subunit of the splicing
            factor 3b complex. Splicing factor 3b associates with both the U2
            and U11/U12 small nuclear ribonucleoprotein complexes (U2 snRNP) of
            spliceosomes. This 14 kDa protein interacts directly with subunit 1
            of the splicing factor 3b complex. This 14 kDa protein also
            interacts directly with the adenosine that carries out the first
            transesterification step of splicing at the pre-mRNA branch site.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.172119.1,
                                           SRR1163657.34312.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233468.5/ ENSP00000233468.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..125
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..125
                     /product="splicing factor 3B subunit 6"
                     /note="spliceosome-associated protein, 14 kDa subunit;
                     pre-mRNA branch site protein p14; SF3b 14 kDa subunit;
                     splicing factor 3B, 14 kDa subunit; spliceosome-associated
                     protein, 14-kDa; splicing factor 3b, subunit 6, 14kDa"
                     /calculated_mol_wt=14454
     Region          16..29
                     /region_name="Interaction with pre-mRNA branch site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     Region          17..93
                     /region_name="RRM_SF3B14"
                     /note="RNA recognition motif (RRM) found in pre-mRNA
                     branch site protein p14 (SF3B14) and similar proteins;
                     cd12241"
                     /db_xref="CDD:409687"
     Site            order(17,19..20,22,32,46..53,56,59,61,65..67,92)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409687"
     Site            order(22,61,91..93)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409687"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     Site            41
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9Y3B4.1)"
     CDS             1..125
                     /gene="SF3B6"
                     /gene_synonym="CGI-110; HSPC175; Ht006; P14; SAP14;
                     SAP14a; SF3B14; SF3B14a"
                     /coded_by="NM_016047.4:98..475"
                     /db_xref="CCDS:CCDS1707.1"
                     /db_xref="GeneID:51639"
                     /db_xref="HGNC:HGNC:30096"
                     /db_xref="MIM:607835"
ORIGIN      
        1 mamqaakran irlppevnri lyirnlpyki taeemydifg kygpirqirv gntpetrgta
       61 yvvyedifda knacdhlsgf nvcnrylvvl yynanrafqk mdtkkkeeql kllkekygin
      121 tdppk
//
LOCUS       NP_001159525             210 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform d
            [Homo sapiens].
ACCESSION   NP_001159525
VERSION     NP_001159525.1
DBSOURCE    REFSEQ: accession NM_001166053.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 210)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC372060.1, DC377693.1,
            CX782504.1, AC131953.1 and AL080130.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (6) differs in the presence and
            absence of exons in the 5' UTR and 5' coding region, and uses a
            downstream translational start codon, compared to variant 1. The
            resulting isoform (d) is significantly shorter at the N-terminus,
            compared to isoform a. Variants 4, 5, 6 and 7 encode the same
            isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803613.181567.1, SRR1803617.44624.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..210
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform d"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=23357
     Region          34..160
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(45,119,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(56,58,106..107,109..116,118,126,132,142,144,147,151,
                     154..155,157..158)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..210
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001166053.1:292..924"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS54760.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 maerknakal acsslqeran vnldvplqvd fptpktelvq kfhvqylgml pvdkpvgmdi
       61 lnsaienlmt ssnkedwlsv nmnvadatvt visekneeev lvecrvrfls fmgvgkdvht
      121 fafimdtgnq rfechvfwce pnagnvseav qaacmlryqk clvarppsqk vrpppppads
      181 vtrrvttnvk rgvlslidtl kqkrpvtemp
//
LOCUS       NP_055317                504 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-processing factor 19 [Homo sapiens].
ACCESSION   NP_055317
VERSION     NP_055317.1
DBSOURCE    REFSEQ: accession NM_014502.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Shepelev,N.M., Kurochkina,A.O., Dontsova,O.A. and Rubtsova,M.P.
  TITLE     PRPF19 mRNA Encodes a Small Open Reading Frame That Is Important
            for Viability of Human Cells
  JOURNAL   Dokl Biochem Biophys 515 (1), 41-47 (2024)
   PUBMED   38472668
  REMARK    GeneRIF: PRPF19 mRNA Encodes a Small Open Reading Frame That Is
            Important for Viability of Human Cells.
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Wang,Y., Wang,J., He,J., Ji,B., Pang,Z., Wang,J., Liu,Y. and Ren,M.
  TITLE     Comprehensive analysis of PRPF19 immune infiltrates, DNA
            methylation, senescence-associated secretory phenotype and ceRNA
            network in bladder cancer
  JOURNAL   Front Immunol 14, 1289198 (2023)
   PUBMED   38022515
  REMARK    GeneRIF: Comprehensive analysis of PRPF19 immune infiltrates, DNA
            methylation, senescence-associated secretory phenotype and ceRNA
            network in bladder cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Hatakeyama,S., Yada,M., Matsumoto,M., Ishida,N. and Nakayama,K.I.
  TITLE     U box proteins as a new family of ubiquitin-protein ligases
  JOURNAL   J Biol Chem 276 (35), 33111-33120 (2001)
   PUBMED   11435423
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Gotzmann,J., Gerner,C., Meissner,M., Holzmann,K., Grimm,R.,
            Mikulits,W. and Sauermann,G.
  TITLE     hNMP 200: a novel human common nuclear matrix protein combining
            structural and regulatory functions
  JOURNAL   Exp Cell Res 261 (1), 166-179 (2000)
   PUBMED   11082287
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Gerner,C., Holzmann,K., Meissner,M., Gotzmann,J., Grimm,R. and
            Sauermann,G.
  TITLE     Reassembling proteins and chaperones in human nuclear matrix
            protein fractions
  JOURNAL   J Cell Biochem 74 (2), 145-151 (1999)
   PUBMED   10404385
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL555169.3, AP003721.3, AP000777.4 and AW673738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018698.2, AJ131186.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000227524.9/ ENSP00000227524.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.2"
     Protein         1..504
                     /product="pre-mRNA-processing factor 19"
                     /EC_number="2.3.2.27"
                     /note="nuclear matrix protein NMP200 related to splicing
                     factor PRP19; senescence evasion factor; nuclear matrix
                     protein 200; PRP19/PSO4 homolog; PRP19/PSO4 pre-mRNA
                     processing factor 19 homolog; psoralen 4; RING-type E3
                     ubiquitin transferase PRP19"
                     /calculated_mol_wt=55050
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.4,
                     ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          3..56
                     /region_name="RING-Ubox_PRP19"
                     /note="U-box domain, a modified RING finger, found in
                     pre-mRNA-processing factor 19 (Prp19) and similar
                     proteins; cd16656"
                     /db_xref="CDD:438318"
     Site            order(3,15,17,21..22,24,53..56)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:438318"
     Region          68..223
                     /region_name="May mediate interaction with PSMC5.
                     /evidence=ECO:0000250|UniProtKB:Q99KP6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          69..133
                     /region_name="Prp19"
                     /note="Prp19/Pso4-like; pfam08606"
                     /db_xref="CDD:400774"
     Site            122
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99KP6; propagated from
                     UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          219..259
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          224..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <233..504
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Site            244
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q99KP6; propagated from
                     UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Site            261
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          262..301
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          268..304
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          304..345
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          309..344
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          348..387
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          354..389
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          390..429
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          395..431
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          433..472
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          438..464
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          473..503
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UMS4.1)"
     Region          476..502
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..504
                     /gene="PRPF19"
                     /gene_synonym="hPSO4; NMP200; PRP19; PSO4; SNEV; UBOX4"
                     /coded_by="NM_014502.5:204..1718"
                     /db_xref="CCDS:CCDS7995.1"
                     /db_xref="GeneID:27339"
                     /db_xref="HGNC:HGNC:17896"
                     /db_xref="MIM:608330"
ORIGIN      
        1 mslicsisne vpehpcvspv snhvyerrli ekyiaengtd pinnqplsee qlidikvahp
       61 irpkppsats ipailkalqd ewdavmlhsf tlrqqlqttr qelshalyqh daacrviarl
      121 tkevtaarea latlkpqagl ivpqavpssq psvvgagepm dlgelvgmtp eiiqklqdka
      181 tvltterkkr gktvpeelvk peelskyrqv ashvglhsas ipgilaldlc psdtnkiltg
      241 gadknvvvfd ksseqilatl kghtkkvtsv vfhpsqdlvf saspdatiri wsvpnascvq
      301 vvrahesavt glslhatgdy llsssddqyw afsdiqtgrv ltkvtdetsg csltcaqfhp
      361 dglifgtgtm dsqikiwdlk ertnvanfpg hsgpitsiaf sengyylata addssvklwd
      421 lrklknfktl qldnnfevks lifdqsgtyl alggtdvqiy ickqwteilh ftehsglttg
      481 vafghhakfi astgmdrslk fysl
//
LOCUS       NP_940891                332 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal AT-AC splicing factor [Homo sapiens].
ACCESSION   NP_940891 XP_290495
VERSION     NP_940891.1
DBSOURCE    REFSEQ: accession NM_198489.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   2  (residues 1 to 332)
  AUTHORS   de Wolf,B., Oghabian,A., Akinyi,M.V., Hanks,S., Tromer,E.C., van
            Hooff,J.J.E., van Voorthuijsen,L., van Rooijen,L.E., Verbeeren,J.,
            Uijttewaal,E.C.H., Baltissen,M.P.A., Yost,S., Piloquet,P.,
            Vermeulen,M., Snel,B., Isidor,B., Rahman,N., Frilander,M.J. and
            Kops,G.J.P.L.
  TITLE     Chromosomal instability by mutations in the novel minor spliceosome
            component CENATAC
  JOURNAL   EMBO J 40 (14), e106536 (2021)
   PUBMED   34009673
  REMARK    GeneRIF: Chromosomal instability by mutations in the novel minor
            spliceosome component CENATAC.
REFERENCE   3  (residues 1 to 332)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Wang,T., Zou,Y., Huang,N., Teng,J. and Chen,J.
  TITLE     CCDC84 Acetylation Oscillation Regulates Centrosome Duplication by
            Modulating HsSAS-6 Degradation
  JOURNAL   Cell Rep 29 (7), 2078-2091 (2019)
   PUBMED   31722219
  REMARK    GeneRIF: CCDC84 Acetylation Oscillation Regulates Centrosome
            Duplication by Modulating HsSAS-6 Degradation.
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY073607.1, AB094093.1 and
            BU733365.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 17, 2003 this sequence version replaced XP_290495.2.
            
            Summary: This gene encodes a protein thought to contain a coiled
            coil motif. No function has been determined for the encoded
            protein. A pseudogene of this gene is located on chromosome 20.
            Alternate splicing results in multiple transcript variants.
            [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (1) represents the shortest
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.72242.1, AB094093.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334418.6/ ENSP00000334767.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..332
                     /product="centrosomal AT-AC splicing factor"
                     /note="coiled-coil domain-containing protein 84;
                     coiled-coil domain containing 84"
                     /calculated_mol_wt=37843
     Region          1..169
                     /region_name="Required for centrosome location.
                     /evidence=ECO:0000269|PubMed:31722219"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UT8.1)"
     Region          6..323
                     /region_name="CCDC84"
                     /note="Coiled coil protein 84; pfam14968"
                     /db_xref="CDD:464412"
     Site            31
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by NAT10.
                     /evidence=ECO:0000269|PubMed:31722219; propagated from
                     UniProtKB/Swiss-Prot (Q86UT8.1)"
     Region          169..213
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UT8.1)"
     CDS             1..332
                     /gene="CENATAC"
                     /gene_synonym="CCDC84; DLNB14; MVA4"
                     /coded_by="NM_198489.3:61..1059"
                     /db_xref="CCDS:CCDS8405.1"
                     /db_xref="GeneID:338657"
                     /db_xref="HGNC:HGNC:30460"
                     /db_xref="MIM:620142"
ORIGIN      
        1 mapaqrcplc rqtffcgrgh vysrkhqrql kealerllpq veaarkaira aqveryvpeh
       61 erccwclccg cevrehlshg nltvlyggll ehlaspehkk atnkfwwenk aevqmkekfl
      121 vtpqdyarfk ksmvkgldsy eekedkvike maaqireveq srqevvrsvl epqavpdpee
      181 gssaprswkg mnsqvasslq qpsnldlppa peldwmetgp sltfighqdi pgvgnihsga
      241 tppwmiqdee yiagnqeigp syeeflkeke kqklkklppd rvganfdhss rtsagwlpsf
      301 grvwnngrrw qsrhqfktea aamkkqshte ks
//
LOCUS       NP_001295019             974 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 7 isoform e [Homo sapiens].
ACCESSION   NP_001295019 XP_005269025
VERSION     NP_001295019.1
DBSOURCE    REFSEQ: accession NM_001308090.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 974)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 974)
  AUTHORS   Maciejewski,K., Giers,M., Oleksiewicz,U. and Czerwinska,P.
  TITLE     The Epigenetic Modifiers HDAC2 and HDAC7 Inversely Associate with
            Cancer Stemness and Immunity in Solid Tumors
  JOURNAL   Int J Mol Sci 25 (14), 7841 (2024)
   PUBMED   39063083
  REMARK    GeneRIF: The Epigenetic Modifiers HDAC2 and HDAC7 Inversely
            Associate with Cancer Stemness and Immunity in Solid Tumors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 974)
  AUTHORS   Lu,W., Zhuang,G., Guan,Y., Li,Y., Liu,L. and Xiao,M.
  TITLE     Comprehensive analysis of HDAC7 expression and its prognostic value
            in diffuse large B cell lymphoma: A review
  JOURNAL   Medicine (Baltimore) 102 (45), e34577 (2023)
   PUBMED   37960766
  REMARK    GeneRIF: Comprehensive analysis of HDAC7 expression and its
            prognostic value in diffuse large B cell lymphoma: A review.
            Review article
REFERENCE   4  (residues 1 to 974)
  AUTHORS   Qin,X., Long,Y., Bai,X., Cao,L., Yan,H., Zhang,K., Wang,B. and
            Wu,X.
  TITLE     The disordered C terminus of ALKBH5 promotes phase separation and
            paraspeckles assembly
  JOURNAL   J Biol Chem 299 (8), 105071 (2023)
   PUBMED   37474102
REFERENCE   5  (residues 1 to 974)
  AUTHORS   Ling,S., Chen,T., Wang,S., Zhang,W., Zhou,R., Xia,X., Yao,Z.,
            Fan,Y., Ning,S., Liu,J., Qin,L., Tucker,H.O., Wang,N. and Guo,X.
  TITLE     Deacetylation of FOXP1 by HDAC7 potentiates self-renewal of
            mesenchymal stem cells
  JOURNAL   Stem Cell Res Ther 14 (1), 188 (2023)
   PUBMED   37507770
  REMARK    GeneRIF: Deacetylation of FOXP1 by HDAC7 potentiates self-renewal
            of mesenchymal stem cells.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 974)
  AUTHORS   Lemercier,C., Brocard,M.P., Puvion-Dutilleul,F., Kao,H.Y.,
            Albagli,O. and Khochbin,S.
  TITLE     Class II histone deacetylases are directly recruited by BCL6
            transcriptional repressor
  JOURNAL   J Biol Chem 277 (24), 22045-22052 (2002)
   PUBMED   11929873
  REMARK    GeneRIF: Class II histone deacetylases are directly recruited by
            BCL6 transcriptional repressor
REFERENCE   7  (residues 1 to 974)
  AUTHORS   Fischle,W., Dequiedt,F., Fillion,M., Hendzel,M.J., Voelter,W. and
            Verdin,E.
  TITLE     Human HDAC7 histone deacetylase activity is associated with HDAC3
            in vivo
  JOURNAL   J Biol Chem 276 (38), 35826-35835 (2001)
   PUBMED   11466315
REFERENCE   8  (residues 1 to 974)
  AUTHORS   Lee,H.J., Chun,M. and Kandror,K.V.
  TITLE     Tip60 and HDAC7 interact with the endothelin receptor a and may be
            involved in downstream signaling
  JOURNAL   J Biol Chem 276 (20), 16597-16600 (2001)
   PUBMED   11262386
REFERENCE   9  (residues 1 to 974)
  AUTHORS   Marks,P.A., Richon,V.M. and Rifkind,R.A.
  TITLE     Histone deacetylase inhibitors: inducers of differentiation or
            apoptosis of transformed cells
  JOURNAL   J Natl Cancer Inst 92 (15), 1210-1216 (2000)
   PUBMED   10922406
  REMARK    Review article
REFERENCE   10 (residues 1 to 974)
  AUTHORS   Kao,H.Y., Downes,M., Ordentlich,P. and Evans,R.M.
  TITLE     Isolation of a novel histone deacetylase reveals that class I and
            class II deacetylases promote SMRT-mediated repression
  JOURNAL   Genes Dev 14 (1), 55-66 (2000)
   PUBMED   10640276
  REMARK    GeneRIF: Characterization of the mouse HDAC7 ortholog.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC376749.1, AK303481.1,
            AK299292.1, AK122588.1 and BM144303.1.
            
            On May 15, 2015 this sequence version replaced XP_005269025.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene has sequence homology to members of the histone
            deacetylase family. This gene is orthologous to mouse HDAC7 gene
            whose protein promotes repression mediated via the transcriptional
            corepressor SMRT. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1. The resulting
            isoform (e) has the same N- and C-termini but is shorter than
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303481.1, SRR18074967.3199104.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..974
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.11"
     Protein         1..974
                     /product="histone deacetylase 7 isoform e"
                     /EC_number="3.5.1.98"
                     /note="histone deacetylase 7A; protein deacetylase HDAC7"
                     /calculated_mol_wt=104980
     Region          540..917
                     /region_name="HDAC7"
                     /note="Histone deacetylase 7; cd10008"
                     /db_xref="CDD:212532"
     Site            order(564,648,691..692,700..701,729,731,760,823,831..832,
                     863)
                     /site_type="active"
                     /db_xref="CDD:212532"
     CDS             1..974
                     /gene="HDAC7"
                     /gene_synonym="HD7; HD7A; HDAC7A"
                     /coded_by="NM_001308090.2:119..3043"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS81685.1"
                     /db_xref="GeneID:51564"
                     /db_xref="HGNC:HGNC:14067"
                     /db_xref="MIM:606542"
ORIGIN      
        1 mhspgagcpr pcadtpgpqp qpmdlrvgqr ppvepppept llalqrpqrl hhhlflaglq
       61 qqrsvepmrl smdtpmpelq vgpqeqelrq llhkdkskrs avassvvkqk laevilkkqq
      121 aalertvhpn spgipyrtle pletegatrs mlssflppvp slpsdppehf plrktvsepn
      181 lklrykpkks lerrknpllr kesappslrr rpaetlgdss psssstpasg csspndsehg
      241 pnpilgseal lgqrlrlqet svapfalptv sllpaitlgl paparadsdr rthptlgprg
      301 pilgsphtpl flphglepea ggtlpsrlqp illldpsgsh aplltvpglg plpfhfaqsl
      361 mtterlsgsg lhwplsrtrs eplppsatap pppgpmqprl eqlkthvqvi krsakpsekp
      421 rlrqipsaed letdgggpgq vvddglehre lghgqpearg paplqqhpqv llweqqrlag
      481 rlprgstgdt vllplaqggh rplsraqssp aapaslsape pasqarvlss setpartlpf
      541 ttgliydsvm lkhqcscgdn srhpehagri qsiwsrlqer glrsqceclr grkasleelq
      601 svhserhvll ygtnplsrlk ldngklagll aqrmfvmlpc ggvgvdtdti wnelhssnaa
      661 rwaagsvtdl afkvasrelk ngfavvrppg hhadhstamg fcffnsvaia crqlqqqska
      721 skilivdwdv hhgngtqqtf yqdpsvlyis lhrhddgnff pgsgavdevg agsgegfnvn
      781 vawaggldpp mgdpeylaaf rivvmpiare fspdlvlvsa gfdaaeghpa plggyhvsak
      841 cfgymtqqlm nlaggavvla legghdltai cdaseacvaa llgnrvdpls eegwkqkpnl
      901 nairsleavi rvhskywgcm qrlascpdsw vprvpgadke eveavtalas lsvgilaedr
      961 pseqlveeee pmnl
//
LOCUS       NP_001337617             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337617 XP_005250725
VERSION     NP_001337617.1
DBSOURCE    REFSEQ: accession NM_001350688.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 21, 2017 this sequence version replaced XP_005250725.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (24), as well as variants 1-4,
            9-23, and 25-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.70098.1,
                                           SRR1803614.33259.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350688.1:547..2757"
                     /note="isoform 1 is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001073865             458 aa            linear   PRI 20-NOV-2025
DEFINITION  NALCN channel auxiliary factor 1 [Homo sapiens].
ACCESSION   NP_001073865 XP_001128712
VERSION     NP_001073865.1
DBSOURCE    REFSEQ: accession NM_001080396.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Kschonsak,M., Chua,H.C., Weidling,C., Chakouri,N., Noland,C.L.,
            Schott,K., Chang,T., Tam,C., Patel,N., Arthur,C.P., Leitner,A.,
            Ben-Johny,M., Ciferri,C., Pless,S.A. and Payandeh,J.
  TITLE     Structural architecture of the human NALCN channelosome
  JOURNAL   Nature 603 (7899), 180-186 (2022)
   PUBMED   34929720
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Xie,J., Ke,M., Xu,L., Lin,S., Huang,J., Zhang,J., Yang,F., Wu,J.
            and Yan,Z.
  TITLE     Structure of the human sodium leak channel NALCN in complex with
            FAM155A
  JOURNAL   Nat Commun 11 (1), 5831 (2020)
   PUBMED   33203861
  REMARK    GeneRIF: Structure of the human sodium leak channel NALCN in
            complex with FAM155A.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Kschonsak,M., Chua,H.C., Noland,C.L., Weidling,C., Clairfeuille,T.,
            Bahlke,O.O., Ameen,A.O., Li,Z.R., Arthur,C.P., Ciferri,C.,
            Pless,S.A. and Payandeh,J.
  TITLE     Structure of the human sodium leak channel NALCN
  JOURNAL   Nature 587 (7833), 313-318 (2020)
   PUBMED   32698188
  REMARK    GeneRIF: Structure of the human sodium leak channel NALCN.
REFERENCE   4  (residues 1 to 458)
  AUTHORS   Chua,H.C., Wulf,M., Weidling,C., Rasmussen,L.P. and Pless,S.A.
  TITLE     The NALCN channel complex is voltage sensitive and directly
            modulated by extracellular calcium
  JOURNAL   Sci Adv 6 (17), eaaz3154 (2020)
   PUBMED   32494638
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Reichert,M.C., Kupcinskas,J., Schulz,A., Schramm,C., Weber,S.N.,
            Krawczyk,M., Jungst,C., Casper,M., Grunhage,F., Appenrodt,B.,
            Zimmer,V., Tamelis,A., Lukosiene,J.I., Pauziene,N., Kiudelis,G.,
            Jonaitis,L., Goeser,T., Malinowski,M., Glanemann,M., Kupcinskas,L.
            and Lammert,F.
  TITLE     Common variation in FAM155A is associated with diverticulitis but
            not diverticulosis
  JOURNAL   Sci Rep 10 (1), 1658 (2020)
   PUBMED   32015353
  REMARK    GeneRIF: Common variation in FAM155A is associated with
            diverticulitis but not diverticulosis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Wang,K., Zhang,H., Bloss,C.S., Duvvuri,V., Kaye,W., Schork,N.J.,
            Berrettini,W. and Hakonarson,H.
  CONSRTM   Price Foundation Collaborative Group
  TITLE     A genome-wide association study on common SNPs and rare CNVs in
            anorexia nervosa
  JOURNAL   Mol Psychiatry 16 (9), 949-959 (2011)
   PUBMED   21079607
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Terracciano,A., Tanaka,T., Sutin,A.R., Sanna,S., Deiana,B., Lai,S.,
            Uda,M., Schlessinger,D., Abecasis,G.R., Ferrucci,L. and Costa,P.T.
            Jr.
  TITLE     Genome-wide association scan of trait depression
  JOURNAL   Biol Psychiatry 68 (9), 811-817 (2010)
   PUBMED   20800221
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Anney,R.J., Lasky-Su,J., O'Dushlaine,C., Kenny,E., Neale,B.M.,
            Mulligan,A., Franke,B., Zhou,K., Chen,W., Christiansen,H.,
            Arias-Vasquez,A., Banaschewski,T., Buitelaar,J., Ebstein,R.,
            Miranda,A., Mulas,F., Oades,R.D., Roeyers,H., Rothenberger,A.,
            Sergeant,J., Sonuga-Barke,E., Steinhausen,H., Asherson,P.,
            Faraone,S.V. and Gill,M.
  TITLE     Conduct disorder and ADHD: evaluation of conduct problems as a
            categorical and quantitative trait in the international multicentre
            ADHD genetics study
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1369-1378 (2008)
   PUBMED   18951430
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Li,S.H., McInnis,M.G., Margolis,R.L., Antonarakis,S.E. and
            Ross,C.A.
  TITLE     Novel triplet repeat containing genes in human brain: cloning,
            expression, and length polymorphisms
  JOURNAL   Genomics 16 (3), 572-579 (1993)
   PUBMED   8325628
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136964.8, DA779672.1, BC157855.1, AL445204.3, AW592075.1 and
            N69765.1.
            
            On Jan 18, 2007 this sequence version replaced XP_001128712.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.12606.1,
                                           SRR1660805.143535.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375915.4/ ENSP00000365080.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q33.3"
     Protein         1..458
                     /product="NALCN channel auxiliary factor 1"
                     /note="transmembrane protein FAM155A; family with sequence
                     similarity 155 member A"
                     /calculated_mol_wt=51362
     Site            40..60
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AL88.1)"
     Region          70..155
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AL88.1)"
     Site            217
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:33203861,
                     ECO:0007744|PDB:7CM3; propagated from UniProtKB/Swiss-Prot
                     (B1AL88.1)"
     Region          <269..>314
                     /region_name="Mid1"
                     /note="Stretch-activated Ca2+-permeable channel component;
                     pfam12929"
                     /db_xref="CDD:432882"
     Site            417..437
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AL88.1)"
     CDS             1..458
                     /gene="NALF1"
                     /gene_synonym="FAM155A; NLF-1; NLF1"
                     /coded_by="NM_001080396.3:901..2277"
                     /db_xref="CCDS:CCDS32006.1"
                     /db_xref="GeneID:728215"
                     /db_xref="HGNC:HGNC:33877"
                     /db_xref="MIM:619899"
ORIGIN      
        1 mtrgawmcrq yddglkiwla aprenekpfi dseraqkwrl slasllfftv llsdhlwfca
       61 eakltrardk ehqqqqrqqq qqqqqqrqrq qqqqqrrqqe pswpallasm gesspaaqah
      121 rllsassspt lppspgdggg gggkgnrgkd drgkalflgn sakpvwrlet cypqgassgq
      181 cftvenadav carnwsrgaa ggdgqevrsk hptplwnlsd fylsfcnsyt lwelfsglss
      241 pntlncsldv vlkeggemtt crqcveayqd ydhhaqekye efesvlhkyl qseeysvksc
      301 pedckivyka wlcsqyfevt qfncrktipc kqyclevqtr cpfilpdnde viygglssfi
      361 ctglyetflt ndepeccdvr reeksnnpsk gtveksgsch rtsltvssat rlcnsrlklc
      421 vlvlillhtv ltasaaqnta glsfggintl eenstnee
//
LOCUS       NP_116056                398 aa            linear   PRI 20-NOV-2025
DEFINITION  seipin isoform 2 [Homo sapiens].
ACCESSION   NP_116056
VERSION     NP_116056.3
DBSOURCE    REFSEQ: accession NM_032667.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 398)
  AUTHORS   Guo,D., Hu,L., Xie,P., Sun,P. and Yu,W.
  TITLE     Seipin is involved in oxygen-glucose deprivation/reoxygenation
            induced neuroinflammation by regulating the TLR3/TRAF3/NF-kappaB
            pathway
  JOURNAL   Int Immunopharmacol 134, 112182 (2024)
   PUBMED   38703568
  REMARK    GeneRIF: Seipin is involved in oxygen-glucose
            deprivation/reoxygenation induced neuroinflammation by regulating
            the TLR3/TRAF3/NF-kappaB pathway.
REFERENCE   2  (residues 1 to 398)
  AUTHORS   Zhu,X., An,X., Chen,M., Guo,D., Xie,P., Wang,B., Huang,Z. and Yu,W.
  TITLE     Seipin overexpression attenuates cerebral ischemia-reperfusion
            injury via preventing apoptosis and autophagy
  JOURNAL   Brain Behav 13 (12), e3195 (2023)
   PUBMED   37897134
  REMARK    GeneRIF: Seipin overexpression attenuates cerebral
            ischemia-reperfusion injury via preventing apoptosis and autophagy.
REFERENCE   3  (residues 1 to 398)
  AUTHORS   Weterman,M.A.J., Bronk,M., Jongejan,A., Hoogendijk,J.E., Krudde,J.,
            Karjosukarso,D., Goebel,H.H., Aronica,E., Jobsis,G.J., van
            Ruissen,F., van Spaendonck-Zwarts,K.Y., de Visser,M. and Baas,F.
  TITLE     Pathogenic variants in three families with distal muscle
            involvement
  JOURNAL   Neuromuscul Disord 33 (1), 58-64 (2023)
   PUBMED   36539320
  REMARK    GeneRIF: Pathogenic variants in three families with distal muscle
            involvement.
REFERENCE   4  (residues 1 to 398)
  AUTHORS   Windpassinger,C., Auer-Grumbach,M., Irobi,J., Patel,H., Petek,E.,
            Horl,G., Malli,R., Reed,J.A., Dierick,I., Verpoorten,N.,
            Warner,T.T., Proukakis,C., Van den Bergh,P., Verellen,C., Van
            Maldergem,L., Merlini,L., De Jonghe,P., Timmerman,V., Crosby,A.H.
            and Wagner,K.
  TITLE     Heterozygous missense mutations in BSCL2 are associated with distal
            hereditary motor neuropathy and Silver syndrome
  JOURNAL   Nat Genet 36 (3), 271-276 (2004)
   PUBMED   14981520
  REMARK    GeneRIF: Heterozygous missense mutations in BSCL2 are associated
            with distal hereditary motor neuropathy and Silver syndrome.
            GeneRIF: seipin is an integral membrane protein of the endoplasmic
            reticulum (ER)
REFERENCE   5  (residues 1 to 398)
  AUTHORS   Simha,V. and Garg,A.
  TITLE     Phenotypic heterogeneity in body fat distribution in patients with
            congenital generalized lipodystrophy caused by mutations in the
            AGPAT2 or seipin genes
  JOURNAL   J Clin Endocrinol Metab 88 (11), 5433-5437 (2003)
   PUBMED   14602785
  REMARK    GeneRIF: Congenital lipodystrophy patients with Seipin mutations
            have a more severe lack of body fat, which affects both
            metabolically active and mechanical adipose tissue, compared with
            patients with mutations in the AGPAT2 gene.
REFERENCE   6  (residues 1 to 398)
  AUTHORS   Magre,J., Delepine,M., Khallouf,E., Gedde-Dahl,T. Jr., Van
            Maldergem,L., Sobel,E., Papp,J., Meier,M., Megarbane,A., Bachy,A.,
            Verloes,A., d'Abronzo,F.H., Seemanova,E., Assan,R., Baudic,N.,
            Bourut,C., Czernichow,P., Huet,F., Grigorescu,F., de Kerdanet,M.,
            Lacombe,D., Labrune,P., Lanza,M., Loret,H., Matsuda,F., Navarro,J.,
            Nivelon-Chevalier,A., Polak,M., Robert,J.J., Tric,P.,
            Tubiana-Rufi,N., Vigouroux,C., Weissenbach,J., Savasta,S.,
            Maassen,J.A., Trygstad,O., Bogalho,P., Freitas,P., Medina,J.L.,
            Bonnicci,F., Joffe,B.I., Loyson,G., Panz,V.R., Raal,F.J.,
            O'Rahilly,S., Stephenson,T., Kahn,C.R., Lathrop,M. and Capeau,J.
  CONSRTM   BSCL Working Group
  TITLE     Identification of the gene altered in Berardinelli-Seip congenital
            lipodystrophy on chromosome 11q13
  JOURNAL   Nat Genet 28 (4), 365-370 (2001)
   PUBMED   11479539
  REMARK    GeneRIF: Alterations in BSCL2 (seipin gene) are responsible for
            BSCL (OMIM :606158).Predicted human seipin protein sequence.
REFERENCE   7  (residues 1 to 398)
  AUTHORS   Patel,H., Hart,P.E., Warner,T.T., Houlston,R.S., Patton,M.A.,
            Jeffery,S. and Crosby,A.H.
  TITLE     The Silver syndrome variant of hereditary spastic paraplegia maps
            to chromosome 11q12-q14, with evidence for genetic heterogeneity
            within this subtype
  JOURNAL   Am J Hum Genet 69 (1), 209-215 (2001)
   PUBMED   11389484
REFERENCE   8  (residues 1 to 398)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   9  (residues 1 to 398)
  AUTHORS   Ito,D.
  TITLE     BSCL2-Related Neurologic Disorders / Seipinopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301484
REFERENCE   10 (residues 1 to 398)
  AUTHORS   Van Maldergem,L.
  TITLE     Berardinelli-Seip Congenital Lipodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027524.1, BC041640.1 and
            DB296305.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 18, 2003 this sequence version replaced NP_116056.2.
            
            Summary: This gene encodes the multi-pass transmembrane protein
            seipin. This protein localizes to the endoplasmic reticulum and may
            be important for lipid droplet morphology. Mutations in this gene
            have been associated with congenital generalized lipodystrophy type
            2 or Berardinelli-Seip syndrome, a rare autosomal recessive disease
            characterized by a near absence of adipose tissue and severe
            insulin resistance. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            Naturally occurring read-through transcription occurs between this
            locus and the neighboring locus HNRNPUL2 (heterogeneous nuclear
            ribonucleoprotein U-like 2).[provided by RefSeq, Jul 2024].
            
            Transcript Variant: This variant (2) has an alternate 5' exon and
            uses a downstream AUG start codon, as compared to variant 1. The
            resulting isoform (2) has a shorter N-terminus, as compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075317.1, AK225029.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..398
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..398
                     /product="seipin isoform 2"
                     /note="Bernardinelli-Seip congenital lipodystrophy type 2
                     protein; Berardinelli-Seip congenital lipodystrophy 2
                     (seipin); BSCL2, seipin lipid droplet biogenesis
                     associated"
                     /calculated_mol_wt=44261
     Site            27..47
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96G97.3)"
     Region          58..222
                     /region_name="Seipin"
                     /note="Seipin and similar proteins; cd23993"
                     /db_xref="CDD:467827"
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14981520; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     Site            242
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     Site            243..263
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96G97.3)"
     Region          281..398
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96G97.3)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     Region          <293..>348
                     /region_name="PHA03169"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:223003"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FVJ6; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FVJ6; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96G97.3)"
     CDS             1..398
                     /gene="BSCL2"
                     /gene_synonym="GNG3LG; HMN5; HMN5C; HMND13; PELD; SPG17"
                     /coded_by="NM_032667.6:219..1415"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8031.1"
                     /db_xref="GeneID:26580"
                     /db_xref="HGNC:HGNC:15832"
                     /db_xref="MIM:606158"
ORIGIN      
        1 mvndppvpal lwaqevgqvl agrarrlllq fgvlfctill llwvsvflyg sfyysymptv
       61 shlspvhfyy rtdcdsstts lcsfpvanvs ltkggrdrvl mygqpyrvtl elelpespvn
      121 qdlgmflvti scytrggrii stssrsvmlh yrsdllqmld tlvfsslllf gfaeqkqlle
      181 velyadyren syvpttgaii eihskriqly gaylrihahf tglryllynf pmtcafigva
      241 snftflsviv lfsymqwvwg giwprhrfsl qvnirkrdns rkevqrrisa hqpgpegqee
      301 stpqsdvted gespedpsgt egqlseeekp dqqplsgeee lepeasdgsg swedaallte
      361 anlpapapas asapvletlg ssepaggalr qrptcsss
//
LOCUS       NP_056542                311 aa            linear   PRI 20-NOV-2025
DEFINITION  substance-P receptor isoform short [Homo sapiens].
ACCESSION   NP_056542
VERSION     NP_056542.1
DBSOURCE    REFSEQ: accession NM_015727.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Lambert,J., Petrovitch,D., Himes,K.P., Freiermuth,C.E., Braun,R.S.,
            Brown,J.L., Bischof,J.J., Lyons,M.S., Punches,B.E.,
            Littlefield,A.K., Kisor,D.F. and Sprague,J.E.
  TITLE     Association of genetic variants in CYP3A5, DRD2 and NK1R with
            opioid overdose
  JOURNAL   Chem Biol Interact 403, 111242 (2024)
   PUBMED   39265714
  REMARK    GeneRIF: Association of genetic variants in CYP3A5, DRD2 and NK1R
            with opioid overdose.
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Al-Keilani,M.S., Almomani,B.A., Jaradat,S.A., Al-Sawalha,N.A. and
            Qawasmeh,M.A.
  TITLE     Alpha Calcitonin Gene-related Peptide, Neuropeptide Y, and
            Substance P as Biomarkers for Diagnosis and Disease Activity and
            Severity in Multiple Sclerosis
  JOURNAL   CNS Neurol Disord Drug Targets 23 (4), 512-524 (2024)
   PUBMED   37013432
  REMARK    GeneRIF: Alpha Calcitonin Gene-related Peptide, Neuropeptide Y, and
            Substance P as Biomarkers for Diagnosis and Disease Activity and
            Severity in Multiple Sclerosis.
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Nguyen,L.P., Cho,M., Nguyen,T.U., Park,H.K., Nguyen,H.T.,
            Mykhailova,K., Hurh,S., Kim,H.R., Seong,J.Y., Lee,C.S., Ham,B.J.
            and Hwang,J.I.
  TITLE     Neurokinin-2 receptor negatively modulates substance P responses by
            forming complex with Neurokinin-1 receptor
  JOURNAL   Cell Biosci 13 (1), 212 (2023)
   PUBMED   37968728
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Gao,X. and Bayraktutan,U.
  TITLE     TNF-alpha evokes blood-brain barrier dysfunction through activation
            of Rho-kinase and neurokinin 1 receptor
  JOURNAL   Immunobiology 228 (5), 152706 (2023)
   PUBMED   37454559
  REMARK    GeneRIF: TNF-alpha evokes blood-brain barrier dysfunction through
            activation of Rho-kinase and neurokinin 1 receptor.
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Rosso,P., Fico,E., Colafrancesco,S., Bellizzi,M.G., Priori,R.,
            Cerbelli,B., Leopizzi,M., Giordano,C., Greco,A., Tirassa,P.,
            Severini,C. and Fusconi,M.
  TITLE     Involvement of Substance P (SP) and Its Related NK1 Receptor in
            Primary Sjogren's Syndrome (pSS) Pathogenesis
  JOURNAL   Cells 12 (10), 1347 (2023)
   PUBMED   37408182
  REMARK    GeneRIF: Involvement of Substance P (SP) and Its Related NK1
            Receptor in Primary Sjogren's Syndrome (pSS) Pathogenesis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Fong,T.M., Huang,R.R. and Strader,C.D.
  TITLE     Localization of agonist and antagonist binding domains of the human
            neurokinin-1 receptor
  JOURNAL   J Biol Chem 267 (36), 25664-25667 (1992)
   PUBMED   1281469
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Fong,T.M., Yu,H., Huang,R.R. and Strader,C.D.
  TITLE     The extracellular domain of the neurokinin-1 receptor is required
            for high-affinity binding of peptides
  JOURNAL   Biochemistry 31 (47), 11806-11811 (1992)
   PUBMED   1280161
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Takahashi,K., Tanaka,A., Hara,M. and Nakanishi,S.
  TITLE     The primary structure and gene organization of human substance P
            and neuromedin K receptors
  JOURNAL   Eur J Biochem 204 (3), 1025-1033 (1992)
   PUBMED   1312928
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Walsh,D.A., Mapp,P.I., Wharton,J., Rutherford,R.A., Kidd,B.L.,
            Revell,P.A., Blake,D.R. and Polak,J.M.
  TITLE     Localisation and characterisation of substance P binding to human
            synovial tissue in rheumatoid arthritis
  JOURNAL   Ann Rheum Dis 51 (3), 313-317 (1992)
   PUBMED   1374227
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Fong,T.M., Anderson,S.A., Yu,H., Huang,R.R. and Strader,C.D.
  TITLE     Differential activation of intracellular effector by two isoforms
            of human neurokinin-1 receptor
  JOURNAL   Mol Pharmacol 41 (1), 24-30 (1992)
   PUBMED   1310144
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007681.3, DB203452.1,
            M74290.1, M84426.1 and AC007400.4.
            
            Summary: This gene belongs to a gene family of tachykinin
            receptors. These tachykinin receptors are characterized by
            interactions with G proteins and contain seven hydrophobic
            transmembrane regions. This gene encodes the receptor for the
            tachykinin substance P, also referred to as neurokinin 1. The
            encoded protein is also involved in the mediation of
            phosphatidylinositol metabolism of substance P. [provided by
            RefSeq, Sep 2008].
            
            Transcript Variant: This variant (short) uses a different splice
            site in the 3' coding region, compared to variant long. The
            resulting protein (isoform short) has a shorter and distinct
            C-terminus when compared to the long isoform.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M84426.1, DRR138524.405334.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p12"
     Protein         1..311
                     /product="substance-P receptor isoform short"
                     /note="tachykinin receptor 1 (substance P receptor;
                     neurokinin-1 receptor); NK-1 receptor; NK-1R; neurokinin
                     receptor 1"
                     /calculated_mol_wt=35582
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25103.1)"
     Site            18
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25103.1)"
     Site            32..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          33..311
                     /region_name="7tm_GPCRs"
                     /note="seven-transmembrane G protein-coupled receptor
                     superfamily; cl28897"
                     /db_xref="CDD:475119"
     Region          35..59
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320668"
     Site            65..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          68..90
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320668"
     Region          106..128
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320668"
     Site            107..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          149..165
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320668"
     Region          194..217
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320668"
     Site            195..219
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          247..269
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320668"
     Site            249..270
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     Region          284..309
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320668"
     Site            284..308
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25103.1)"
     CDS             1..311
                     /gene="TACR1"
                     /gene_synonym="NK1R; NKIR; SPR; TAC1R"
                     /coded_by="NM_015727.3:587..1522"
                     /note="isoform short is encoded by transcript variant
                     short"
                     /db_xref="CCDS:CCDS46345.1"
                     /db_xref="GeneID:6869"
                     /db_xref="HGNC:HGNC:11526"
                     /db_xref="MIM:162323"
ORIGIN      
        1 mdnvlpvdsd lspnistnts epnqfvqpaw qivlwaaayt vivvtsvvgn vvvmwiilah
       61 krmrtvtnyf lvnlafaeas maafntvvnf tyavhnewyy glfyckfhnf fpiaavfasi
      121 ysmtavafdr ymaiihplqp rlsatatkvv icviwvlall lafpqgyyst tetmpsrvvc
      181 miewpehpnk iyekvyhicv tvliyflpll vigyaytvvg itlwaseipg dssdryheqv
      241 sakrkvvkmm ivvvctfaic wlpfhiffll pyinpdlylk kfiqqvylai mwlamsstmy
      301 npiiycclnd r
//
LOCUS       NP_001265475             476 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor subfamily 6 group A member 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001265475
VERSION     NP_001265475.1
DBSOURCE    REFSEQ: accession NM_001278546.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 476)
  AUTHORS   Neelathi,U.M., Ullah,E., George,A., Maftei,M.I., Boobalan,E.,
            Sanchez-Mendoza,D., Adams,C., McGaughey,D., Sergeev,Y.V., Ai
            Rawi,R., Naik,A., Bender,C., Maumenee,I.H., Michaelides,M.,
            Tan,T.G., Lin,S., Villasmil,R., Blain,D., Hufnagel,R.B., Arno,G.,
            Young,R.M., Guan,B. and Brooks,B.P.
  TITLE     Variants in NR6A1 cause a novel oculo vertebral renal syndrome
  JOURNAL   Nat Commun 16 (1), 6111 (2025)
   PUBMED   40610405
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 476)
  AUTHORS   Wu,Q., Li,X., Long,M., Xie,X. and Liu,Q.
  TITLE     Integrated analysis of histone lysine lactylation (Kla)-specific
            genes suggests that NR6A1, OSBP2 and UNC119B are novel therapeutic
            targets for hepatocellular carcinoma
  JOURNAL   Sci Rep 13 (1), 18642 (2023)
   PUBMED   37903971
  REMARK    GeneRIF: Integrated analysis of histone lysine lactylation
            (Kla)-specific genes suggests that NR6A1, OSBP2 and UNC119B are
            novel therapeutic targets for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 476)
  AUTHORS   Daisuke,H., Kato,H., Fukumura,K., Mayeda,A., Miyagi,Y., Seiki,M.
            and Koshikawa,N.
  TITLE     Novel LAMC2 fusion protein has tumor-promoting properties in
            ovarian carcinoma
  JOURNAL   Cancer Sci 112 (12), 4957-4967 (2021)
   PUBMED   34689384
  REMARK    GeneRIF: Novel LAMC2 fusion protein has tumor-promoting properties
            in ovarian carcinoma.
REFERENCE   4  (residues 1 to 476)
  AUTHORS   Zhou,W., Jiang,R., Wang,Y., Li,Y., Sun,Z. and Zhao,H.
  TITLE     hsa_circ_001653 up-regulates NR6A1 expression and elicits gastric
            cancer progression by binding to microRNA-377
  JOURNAL   Exp Physiol 105 (12), 2141-2153 (2020)
   PUBMED   33006200
  REMARK    GeneRIF: hsa_circ_001653 up-regulates NR6A1 expression and elicits
            gastric cancer progression by binding to microRNA-377.
REFERENCE   5  (residues 1 to 476)
  AUTHORS   Wang,Y., Wan,X., Hao,Y., Zhao,Y., Du,L., Huang,Y., Liu,Z., Wang,Y.,
            Wang,N. and Zhang,P.
  TITLE     NR6A1 regulates lipid metabolism through mammalian target of
            rapamycin complex 1 in HepG2 cells
  JOURNAL   Cell Commun Signal 17 (1), 77 (2019)
   PUBMED   31315616
  REMARK    GeneRIF: the role of NR6A1 in the lipogenesis in HepG2 cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 476)
  AUTHORS   Agoulnik,I.Y., Cho,Y., Niederberger,C., Kieback,D.G. and
            Cooney,A.J.
  TITLE     Cloning, expression analysis and chromosomal localization of the
            human nuclear receptor gene GCNF
  JOURNAL   FEBS Lett 424 (1-2), 73-78 (1998)
   PUBMED   9537518
REFERENCE   7  (residues 1 to 476)
  AUTHORS   Kapelle,M., Kratzschmar,J., Husemann,M. and Schleuning,W.D.
  TITLE     cDNA cloning of two closely related forms of human germ cell
            nuclear factor (GCNF)
  JOURNAL   Biochim Biophys Acta 1352 (1), 13-17 (1997)
   PUBMED   9177477
REFERENCE   8  (residues 1 to 476)
  AUTHORS   Yan,Z.H., Medvedev,A., Hirose,T., Gotoh,H. and Jetten,A.M.
  TITLE     Characterization of the response element and DNA binding properties
            of the nuclear orphan receptor germ cell nuclear factor/retinoid
            receptor-related testis-associated receptor
  JOURNAL   J Biol Chem 272 (16), 10565-10572 (1997)
   PUBMED   9099702
REFERENCE   9  (residues 1 to 476)
  AUTHORS   Lei,W., Hirose,T., Zhang,L.X., Adachi,H., Spinella,M.J.,
            Dmitrovsky,E. and Jetten,A.M.
  TITLE     Cloning of the human orphan receptor germ cell nuclear
            factor/retinoid receptor-related testis-associated receptor and its
            differential regulation during embryonal carcinoma cell
            differentiation
  JOURNAL   J Mol Endocrinol 18 (2), 167-176 (1997)
   PUBMED   9134503
REFERENCE   10 (residues 1 to 476)
  AUTHORS   Susens,U. and Borgmeyer,U.
  TITLE     Characterization of the human germ cell nuclear factor gene
  JOURNAL   Biochim Biophys Acta 1309 (3), 179-182 (1996)
   PUBMED   8982251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354928.9, S83309.1 and
            AL354979.17.
            
            Summary: This gene encodes an orphan nuclear receptor which is a
            member of the nuclear hormone receptor family. Its expression
            pattern suggests that it may be involved in neurogenesis and germ
            cell development. The protein can homodimerize and bind DNA, but in
            vivo targets have not been identified. Alternate splicing results
            in multiple transcript variants.[provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            This results in a shorter protein (isoform 4), compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: S83309.1, HQ709185.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..476
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..476
                     /product="nuclear receptor subfamily 6 group A member 1
                     isoform 4"
                     /note="retinoic acid receptor-related testis-associated
                     receptor; retinoid receptor-related testis-specific
                     receptor"
                     /calculated_mol_wt=53865
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          48..137
                     /region_name="NR_DBD_GCNF_like"
                     /note="DNA-binding domain of Germ cell nuclear factor
                     (GCNF) F1 is composed of two C4-type zinc fingers;
                     cd07169"
                     /db_xref="CDD:143543"
     Site            order(56,59,73,76,92,98,108,111)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143543"
     Site            order(66..68,74..75,77,79,82,85,105..106,109,112,123,126)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143543"
     Region          127..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          158..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          168..249
                     /region_name="Sufficient for interaction with UIMC1.
                     /evidence=ECO:0000250|UniProtKB:Q64249"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          252..463
                     /region_name="NR_LBD_DHR4_like"
                     /note="The ligand binding domain of orphan nuclear
                     receptor Ecdysone-induced receptor DHR4; cd06953"
                     /db_xref="CDD:132751"
     Site            order(282..283,287,321,325,328,342,365)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132751"
     Site            order(292,295,299,304,309..310,312..313,316..317)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132751"
     CDS             1..476
                     /gene="NR6A1"
                     /gene_synonym="CT150; GCNF; GCNF1; hGCNF; hRTR; NR61; RTR"
                     /coded_by="NM_001278546.2:193..1623"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS65127.1"
                     /db_xref="GeneID:2649"
                     /db_xref="HGNC:HGNC:7985"
                     /db_xref="MIM:602778"
ORIGIN      
        1 merdepppsg ggggggsagf leppaalppp prngfcqdel aeldpgtndr aeqrtclicg
       61 dratglhygi iscegckgff krsicnkrvy rcsrdkncvm srkqrnrcqy crllkclqmg
      121 mnrkairedg mpggrnksig pvqiseeeie rimsgqefee eanhwsnhgd sdhsspgnra
      181 sesnqpspgs tlsssrsvel ngfmafreqy mgmsvpphyq yiphlfsysg hspllpqqar
      241 sldpqsysli hqllsaedle plgtpmlied gyavtqaelf allcrladel lfrqiawikk
      301 lpffcelsik dytcllsstw qelillsslt vyskqifgel advtakysps deelhrfsde
      361 gmevierliy lyhkfhqlkv sneeyacmka inflnqdirg ltsasqleql nkrywyicqd
      421 fteykythqp nrfpdlmmcl peiryiagkm vnvpleqlpl lfkvvlhsck tsvgke
//
LOCUS       NP_001339887             499 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 24 [Homo sapiens].
ACCESSION   NP_001339887 XP_016868780
VERSION     NP_001339887.1
DBSOURCE    REFSEQ: accession NM_001352958.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868780.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.70546.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..499
                     /product="DNA repair-scaffolding protein isoform 24"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=54009
     Region          105..489
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..499
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352958.1:1409..2908"
                     /note="isoform 24 is encoded by transcript variant 32"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mfvikgltnn speiqvvcsg vattgtawth ghkeakqrip tstplrdsll dvvesqgaas
       61 wpgagvrvvv qrvyslpsrd strgqqgass ghtdpagtra cllvqdacgm fgevhleftm
      121 skarqlegks cslvgmkvlq kvtrgrtagi fslidtlwpp aiplktpgrd qpceeikthl
      181 pppalcyilt ahpnlgqidi idedpiykly qppvtrclrd ilqmndlgtr csfyatviyq
      241 kpqlksllll eqreiwllvt dvtlqtkeer dprlpktllv yvaplcvlgs evlealagaa
      301 phslffkdal rdqgrivcae rtvlllqkpl lsvvsgassc elpgpvmlds ldsatpvnsi
      361 csvqgtvvgv destafswpv cdmcgngrle qrpedrgafs cgdcsrvvts pvlkrhlqvf
      421 ldcrsrpqcr vkvkllqrsi ssllrfaage dgsyevksvl gkevgllncf vqsvtahpts
      481 cigleeiell saggasaeh
//
LOCUS       NP_001305833             391 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate dehydrogenase 1, mitochondrial isoform c [Homo sapiens].
ACCESSION   NP_001305833
VERSION     NP_001305833.1
DBSOURCE    REFSEQ: accession NM_001318904.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Qin,J., Zhao,Y., Li,S., Liu,Q., Huang,S. and Yu,X.
  TITLE     GDH1 exacerbates renal fibrosis by inhibiting the transcriptional
            activity of peroxisome proliferator-activated receptor gamma
  JOURNAL   FEBS J 291 (20), 4581-4601 (2024)
   PUBMED   39136063
  REMARK    GeneRIF: GDH1 exacerbates renal fibrosis by inhibiting the
            transcriptional activity of peroxisome proliferator-activated
            receptor gamma.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Tzimagiorgis,G., Leversha,M.A., Chroniary,K., Goulielmos,G.,
            Sargent,C.A., Ferguson-Smith,M. and Moschonas,N.K.
  TITLE     Structure and expression analysis of a member of the human
            glutamate dehydrogenase (GLUD) gene family mapped to chromosome
            10p11.2
  JOURNAL   Hum Genet 91 (5), 433-438 (1993)
   PUBMED   8314555
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Gillis,D.
  TITLE     Nonsyndromic Genetic Hyperinsulinism Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301549
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Nakatani,Y., Schneider,M., Banner,C. and Freese,E.
  TITLE     Complete nucleotide sequence of human glutamate dehydrogenase cDNA
  JOURNAL   Nucleic Acids Res 16 (13), 6237 (1988)
   PUBMED   3399399
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Amuro,N., Yamaura,M., Goto,Y. and Okazaki,T.
  TITLE     Molecular cloning and nucleotide sequence of the cDNA for human
            liver glutamate dehydrogenase precursor
  JOURNAL   Biochem Biophys Res Commun 152 (3), 1395-1400 (1988)
   PUBMED   3377777
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Mavrothalassitis,G., Tzimagiorgis,G., Mitsialis,A., Zannis,V.,
            Plaitakis,A., Papamatheakis,J. and Moschonas,N.
  TITLE     Isolation and characterization of cDNA clones encoding human liver
            glutamate dehydrogenase: evidence for a small gene family
  JOURNAL   Proc Natl Acad Sci U S A 85 (10), 3494-3498 (1988)
   PUBMED   3368458
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Banner,C., Silverman,S., Thomas,J.W., Lampel,K.A., Vitkovic,L.,
            Huie,D. and Wenthold,R.J.
  TITLE     Isolation of a human brain cDNA for glutamate dehydrogenase
  JOURNAL   J Neurochem 49 (1), 246-252 (1987)
   PUBMED   3585334
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Julliard,J.H. and Smith,E.L.
  TITLE     Partial amino acid sequence of the glutamate dehydrogenase of human
            liver and a revision of the sequence of the bovine enzyme
  JOURNAL   J Biol Chem 254 (9), 3427-3438 (1979)
   PUBMED   429360
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M20867.1, DB089525.1,
            BC112946.1 and AF086070.2.
            
            Summary: This gene encodes glutamate dehydrogenase, which is a
            mitochondrial matrix enzyme that catalyzes the oxidative
            deamination of glutamate to alpha-ketoglutarate and ammonia. This
            enzyme has an important role in regulating amino acid-induced
            insulin secretion. It is allosterically activated by ADP and
            inhibited by GTP and ATP. Activating mutations in this gene are a
            common cause of congenital hyperinsulinism. Alternative splicing of
            this gene results in multiple transcript variants. The related
            glutamate dehydrogenase 2 gene on the human X-chromosome originated
            from this gene via retrotransposition and encodes a soluble form of
            glutamate dehydrogenase. Related pseudogenes have been identified
            on chromosomes 10, 18 and X. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (5) contains an additional exon in
            the 5' region, and it thus differs in its 5' UTR and initiates
            translation at a downstream in-frame start codon, compared to
            variant 1. The encoded isoform (c) is shorter at the N-terminus,
            compared to isoform a. Variants 3, 4, 5, 6 and 7 all encode isoform
            c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.3871907.1,
                                           SRR18074967.243307.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.2"
     Protein         1..391
                     /product="glutamate dehydrogenase 1, mitochondrial isoform
                     c"
                     /EC_number="1.4.1.3"
                     /note="glutamate dehydrogenase 1, mitochondrial; glutamate
                     dehydrogenase (NAD(P)+); epididymis tissue sperm binding
                     protein Li 18mP; epididymis secretory sperm binding
                     protein"
                     /calculated_mol_wt=42819
     Region          <1..388
                     /region_name="GdhA"
                     /note="Glutamate dehydrogenase/leucine dehydrogenase
                     [Amino acid transport and metabolism]; COG0334"
                     /db_xref="CDD:440103"
     CDS             1..391
                     /gene="GLUD1"
                     /gene_synonym="GDH; GDH1; GLUD; hGDH1"
                     /coded_by="NM_001318904.2:803..1978"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS91291.1"
                     /db_xref="GeneID:2746"
                     /db_xref="HGNC:HGNC:4335"
                     /db_xref="MIM:138130"
ORIGIN      
        1 mtykcavvdv pfggakagvk inpknytdne lekitrrftm elakkgfigp gidvpapdms
       61 tgeremswia dtyastighy dinahacvtg kpisqggihg risatgrgvf hgienfinea
      121 symsilgmtp gfgdktfvvq gfgnvglhsm rylhrfgakc iavgesdgsi wnpdgidpke
      181 ledfklqhgs ilgfpkakpy egsileadcd ilipaasekq ltksnaprvk akiiaegang
      241 pttpeadkif lernimvipd lylnaggvtv syfewlknln hvsygrltfk yerdsnyhll
      301 msvqeslerk fgkhggtipi vptaefqdri sgasekdivh sglaytmers arqimrtamk
      361 ynlgldlrta ayvnaiekvf kvyneagvtf t
//
LOCUS       NP_057388                163 aa            linear   PRI 20-NOV-2025
DEFINITION  probable ribosome biogenesis protein RLP24 [Homo sapiens].
ACCESSION   NP_057388
VERSION     NP_057388.1
DBSOURCE    REFSEQ: accession NM_016304.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Durand,S., Bruelle,M., Bourdelais,F., Bennychen,B.,
            Blin-Gonthier,J., Isaac,C., Huyghe,A., Martel,S., Seyve,A.,
            Vanbelle,C., Adrait,A., Coute,Y., Meyronet,D., Catez,F., Diaz,J.J.,
            Lavial,F., Ricci,E.P., Ducray,F. and Gabut,M.
  TITLE     RSL24D1 sustains steady-state ribosome biogenesis and pluripotency
            translational programs in embryonic stem cells
  JOURNAL   Nat Commun 14 (1), 356 (2023)
   PUBMED   36690642
  REMARK    GeneRIF: RSL24D1 sustains steady-state ribosome biogenesis and
            pluripotency translational programs in embryonic stem cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Ramsuran,V., Kulkarni,H., He,W., Mlisana,K., Wright,E.J.,
            Werner,L., Castiblanco,J., Dhanda,R., Le,T., Dolan,M.J., Guan,W.,
            Weiss,R.A., Clark,R.A., Karim,S.S., Ahuja,S.K. and Ndung'u,T.
  TITLE     Duffy-null-associated low neutrophil counts influence HIV-1
            susceptibility in high-risk South African black women
  JOURNAL   Clin Infect Dis 52 (10), 1248-1256 (2011)
   PUBMED   21507922
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   8  (residues 1 to 163)
  AUTHORS   Saveanu,C., Namane,A., Gleizes,P.E., Lebreton,A., Rousselle,J.C.,
            Noaillac-Depeyre,J., Gas,N., Jacquier,A. and Fromont-Racine,M.
  TITLE     Sequential protein association with nascent 60S ribosomal particles
  JOURNAL   Mol Cell Biol 23 (13), 4449-4460 (2003)
   PUBMED   12808088
REFERENCE   9  (residues 1 to 163)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   10 (residues 1 to 163)
  AUTHORS   Saveanu,C., Bienvenu,D., Namane,A., Gleizes,P.E., Gas,N.,
            Jacquier,A. and Fromont-Racine,M.
  TITLE     Nog2p, a putative GTPase associated with pre-60S subunits and
            required for late 60S maturation steps
  JOURNAL   EMBO J 20 (22), 6475-6484 (2001)
   PUBMED   11707418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011912.7.
            
            Summary: This gene encodes a protein sharing a low level of
            sequence similarity with human ribosomal protein L24. Although this
            gene has been referred to as RPL24, L30, and 60S ribosomal protein
            L30 isolog in the sequence databases, it is distinct from the human
            genes officially named RPL24 (which itself has been referred to as
            ribosomal protein L30) and RPL30. The protein encoded by this gene
            localizes to the nucleolus and is thought to play a role in the
            biogenesis of the 60S ribosomal subunit. The precise function of
            this gene is currently unknown. This gene utilizes alternative
            polyadenylation signals and has multiple pseudogenes. [provided by
            RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.258086.1,
                                           SRR5189658.179228.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154529, SAMN03267772
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260443.9/ ENSP00000260443.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..163
                     /product="probable ribosome biogenesis protein RLP24"
                     /EC_number="3.6.5.3"
                     /note="homolog of yeast ribosomal like protein 24; 60S
                     ribosomal protein L30 isolog; my024 protein; ribosomal L24
                     domain-containing protein 1"
                     /calculated_mol_wt=19490
     Region          2..64
                     /region_name="Ribosomal_L24e"
                     /note="Ribosomal protein L24e; pfam01246"
                     /db_xref="CDD:460131"
     CDS             1..163
                     /gene="RSL24D1"
                     /gene_synonym="C15orf15; HRP-L30-iso; L30; RLP24; RPL24;
                     RPL24L; TVAS3"
                     /coded_by="NM_016304.3:52..543"
                     /db_xref="CCDS:CCDS10152.1"
                     /db_xref="GeneID:51187"
                     /db_xref="HGNC:HGNC:18479"
                     /db_xref="MIM:613262"
ORIGIN      
        1 mriekcyfcs gpiypghgmm fvrndckvfr fckskchknf kkkrnprkvr wtkafrkaag
       61 keltvdnsfe fekrrnepik yqrelwnkti damkrveeik qkrqakfimn rlkknkelqk
      121 vqdikevkqn ihliraplag kgkqleekmv qqlqedvdme dap
//
LOCUS       NP_001337602             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337602 XP_006716226
VERSION     NP_001337602.1
DBSOURCE    REFSEQ: accession NM_001350673.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            On Apr 21, 2017 this sequence version replaced XP_006716226.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (10), as well as variants 1-4, 9,
            and 11-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.260102.1,
                                           SRR1803611.155708.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350673.1:468..2678"
                     /note="isoform 1 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001339881             604 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 22 [Homo sapiens].
ACCESSION   NP_001339881
VERSION     NP_001339881.1
DBSOURCE    REFSEQ: accession NM_001352952.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 604)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 604)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 604)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 604)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 604)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 604)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 604)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 604)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 604)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 604)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Transcript Variant: This variant (27), as well as variants 28, 29,
            and 30, encodes isoform 22.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.9023.1,
                                           SRR1660803.236446.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2153733
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..604
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..604
                     /product="DNA repair-scaffolding protein isoform 22"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=65489
     Region          <1..58
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          210..594
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..604
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352952.1:600..2414"
                     /note="isoform 22 is encoded by transcript variant 27"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mqvamceqll gspatsssqs vaprpgaglk vlftketagy lrgrpqdtvr ifppwqklii
       61 psgscpviln tyfcekvvak edsektcevy cpdiplprrs islaqmfvik gltnnspeiq
      121 vvcsgvattg tawthghkea kqriptstpl rdslldvves qgaaswpgag vrvvvqrvys
      181 lpsrdstrgq qgassghtdp agtracllvq dacgmfgevh leftmskarq legkscslvg
      241 mkvlqkvtrg rtagifslid tlwppaiplk tpgrdqpcee ikthlpppal cyiltahpnl
      301 gqidiidedp iyklyqppvt rclrdilqmn dlgtrcsfya tviyqkpqlk slllleqrei
      361 wllvtdvtlq tkeerdprlp ktllvyvapl cvlgsevlea lagaaphslf fkdalrdqgr
      421 ivcaertvll lqkpllsvvs gasscelpgp vmldsldsat pvnsicsvqg tvvgvdesta
      481 fswpvcdmcg ngrleqrped rgafscgdcs rvvtspvlkr hlqvfldcrs rpqcrvkvkl
      541 lqrsissllr faagedgsye vksvlgkevg llncfvqsvt ahptscigle eiellsagga
      601 saeh
//
LOCUS       NP_001341918            1306 aa            linear   PRI 20-NOV-2025
DEFINITION  vascular endothelial growth factor receptor 3 isoform 3 precursor
            [Homo sapiens].
ACCESSION   NP_001341918
VERSION     NP_001341918.1
DBSOURCE    REFSEQ: accession NM_001354989.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1306)
  AUTHORS   Zhang,Y., Dong,X., Zhang,J., Zhao,M., Wang,J., Chu,J., Yang,Z.,
            Ma,S., Lin,K., Sun,H. and Luo,Z.
  TITLE     FLT4 gene polymorphisms influence isolated ventricular septal
            defect predisposition in a Southwest China population
  JOURNAL   BMC Med Genomics 17 (1), 197 (2024)
   PUBMED   39107825
  REMARK    GeneRIF: FLT4 gene polymorphisms influence isolated ventricular
            septal defect predisposition in a Southwest China population.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1306)
  AUTHORS   Schmidt,A., Hrupka,B., van Bebber,F., Sunil Kumar,S., Feng,X.,
            Tschirner,S.K., Assfalg,M., Muller,S.A., Hilger,L.S., Hofmann,L.I.,
            Pigoni,M., Jocher,G., Voytyuk,I., Self,E.L., Ito,M., Hyakkoku,K.,
            Yoshimura,A., Horiguchi,N., Feederle,R., De Strooper,B.,
            Schulte-Merker,S., Lammert,E., Moechars,D., Schmid,B. and
            Lichtenthaler,S.F.
  TITLE     The Alzheimer's disease-linked protease BACE2 cleaves VEGFR3 and
            modulates its signaling
  JOURNAL   J Clin Invest 134 (16), e170550 (2024)
   PUBMED   38888964
  REMARK    GeneRIF: The Alzheimer's disease-linked protease BACE2 cleaves
            VEGFR3 and modulates its signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1306)
  AUTHORS   Fournier,E., Dubreuil,P., Birnbaum,D. and Borg,J.P.
  TITLE     Mutation at tyrosine residue 1337 abrogates ligand-dependent
            transforming capacity of the FLT4 receptor
  JOURNAL   Oncogene 11 (5), 921-931 (1995)
   PUBMED   7675451
REFERENCE   4  (residues 1 to 1306)
  AUTHORS   Borg,J.P., deLapeyriere,O., Noguchi,T., Rottapel,R., Dubreuil,P.
            and Birnbaum,D.
  TITLE     Biochemical characterization of two isoforms of FLT4, a VEGF
            receptor-related tyrosine kinase
  JOURNAL   Oncogene 10 (5), 973-984 (1995)
   PUBMED   7898938
REFERENCE   5  (residues 1 to 1306)
  AUTHORS   Pajusola,K., Aprelikova,O., Armstrong,E., Morris,S. and Alitalo,K.
  TITLE     Two human FLT4 receptor tyrosine kinase isoforms with distinct
            carboxy terminal tails are produced by alternative processing of
            primary transcripts
  JOURNAL   Oncogene 8 (11), 2931-2937 (1993)
   PUBMED   7692369
REFERENCE   6  (residues 1 to 1306)
  AUTHORS   Galland,F., Karamysheva,A., Pebusque,M.J., Borg,J.P., Rottapel,R.,
            Dubreuil,P., Rosnet,O. and Birnbaum,D.
  TITLE     The FLT4 gene encodes a transmembrane tyrosine kinase related to
            the vascular endothelial growth factor receptor
  JOURNAL   Oncogene 8 (5), 1233-1240 (1993)
   PUBMED   8386825
REFERENCE   7  (residues 1 to 1306)
  AUTHORS   Van Zanten,M., Mansour,S., Ostergaard,P., Mortimer,P. and Gordon,K.
  TITLE     Milroy Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301417
REFERENCE   8  (residues 1 to 1306)
  AUTHORS   Pajusola,K., Aprelikova,O., Korhonen,J., Kaipainen,A.,
            Pertovaara,L., Alitalo,R. and Alitalo,K.
  TITLE     FLT4 receptor tyrosine kinase contains seven immunoglobulin-like
            loops and is expressed in multiple human tissues and cell lines
  JOURNAL   Cancer Res 52 (20), 5738-5743 (1992)
   PUBMED   1327515
  REMARK    Erratum:[Cancer Res 1993 Aug 15;53(16):3845]
REFERENCE   9  (residues 1 to 1306)
  AUTHORS   Galland,F., Karamysheva,A., Mattei,M.G., Rosnet,O., Marchetto,S.
            and Birnbaum,D.
  TITLE     Chromosomal localization of FLT4, a novel receptor-type tyrosine
            kinase gene
  JOURNAL   Genomics 13 (2), 475-478 (1992)
   PUBMED   1319394
REFERENCE   10 (residues 1 to 1306)
  AUTHORS   Aprelikova,O., Pajusola,K., Partanen,J., Armstrong,E., Alitalo,R.,
            Bailey,S.K., McMahon,J., Wasmuth,J., Huebner,K. and Alitalo,K.
  TITLE     FLT4, a novel class III receptor tyrosine kinase in chromosome
            5q33-qter
  JOURNAL   Cancer Res 52 (3), 746-748 (1992)
   PUBMED   1310071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC122714.2.
            
            Summary: This gene encodes a tyrosine kinase receptor for vascular
            endothelial growth factors C and D. The protein is thought to be
            involved in lymphangiogenesis and maintenance of the lymphatic
            endothelium. Mutations in this gene cause hereditary lymphedema
            type IA. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) contains an alternate 3'
            terminal exon compared to variant 1. This results in an isoform (3)
            with a shorter C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK309910.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1306
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..1306
                     /product="vascular endothelial growth factor receptor 3
                     isoform 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="vascular endothelial growth factor receptor 3; VEGF
                     receptor-3; Feline McDonough Sarcoma (FMS)-like tyrosine
                     kinase 4; fms related tyrosine kinase 4; primary
                     congenital lymphedema; fms-like tyrosine kinase 4;
                     tyrosine-protein kinase receptor FLT4"
                     /calculated_mol_wt=143914
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2559
     Site            33
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Region          137..224
                     /region_name="Ig_2"
                     /note="Immunoglobulin domain; pfam13895"
                     /db_xref="CDD:464026"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          230..329
                     /region_name="IgI_VEGFR"
                     /note="Immunoglobulin (Ig)-like domain of vascular
                     endothelial growth factor (VEGF) receptor(R); member of
                     the I-set of IgSF domains; cd05862"
                     /db_xref="CDD:409448"
     Region          230..234
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409448"
     Region          240..244
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409448"
     Region          246..255
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409448"
     Site            251
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          262..267
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409448"
     Region          270..272
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409448"
     Region          276..284
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409448"
     Region          289..297
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409448"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          307..313
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409448"
     Region          318..324
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409448"
     Region          331..418
                     /region_name="IgI_VEGFR-3"
                     /note="Immunoglobulin (Ig)-like domain of vascular
                     endothelial growth factor receptor 3 (VEGFR-3); member of
                     the I-set of Ig superfamily (IgSF) domains; cd05863"
                     /db_xref="CDD:409449"
     Region          332..337
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409449"
     Region          342..347
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409449"
     Region          349..360
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409449"
     Region          364..370
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409449"
     Region          372..375
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409449"
     Region          378..380
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409449"
     Region          382..387
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409449"
     Region          395..403
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409449"
     Region          409..418
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409449"
     Site            411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            515
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:23878260,
                     ECO:0007744|PDB:4BSK; propagated from UniProtKB/Swiss-Prot
                     (P35916.3)"
     Site            527
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          559..655
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            594
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          678..765
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            683
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            690
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          695..699
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          708..712
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          731..735
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          745..750
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            758
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          770..804
                     /region_name="VEGFR-2_TMD"
                     /note="VEGFR-2 Transmembrane domain; pfam17988"
                     /db_xref="CDD:375470"
     Site            776..796
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P35916.3)"
     Site            830
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            833
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Region          837..1176
                     /region_name="PTKc_VEGFR3"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Vascular Endothelial Growth Factor Receptor 3; cd05102"
                     /db_xref="CDD:270680"
     Site            order(851..855,859,877..879,896,925,927..931,933..934,
                     1028,1035,1037,1041..1042,1044,1054..1056,1073..1077,1086,
                     1121)
                     /site_type="active"
                     /db_xref="CDD:270680"
     Site            order(851..853,859,877..879,896,925,927..931,933..934,
                     1028,1035,1044,1054..1056)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270680"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            order(1037,1041,1073..1077,1086,1121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270680"
     Site            1054..1079
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270680"
     Site            1063
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis and SRC.
                     /evidence=ECO:0000269|PubMed:16076871,
                     ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1068
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16076871,
                     ECO:0000269|PubMed:20431062; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1230
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528,
                     ECO:0000269|PubMed:16076871; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1231
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528,
                     ECO:0000269|PubMed:16076871; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     Site            1265
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12881528; propagated from
                     UniProtKB/Swiss-Prot (P35916.3)"
     CDS             1..1306
                     /gene="FLT4"
                     /gene_synonym="CHTD7; FLT-4; FLT41; LMPH1A; LMPHM1; PCL;
                     VEGFR-3; VEGFR3"
                     /coded_by="NM_001354989.2:56..3976"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS87360.1"
                     /db_xref="GeneID:2324"
                     /db_xref="HGNC:HGNC:3767"
                     /db_xref="MIM:136352"
ORIGIN      
        1 mqrgaalclr lwlclglldg lvsgysmtpp tlniteeshv idtgdslsis crgqhplewa
       61 wpgaqeapat gdkdsedtgv vrdcegtdar pyckvlllhe vhandtgsyv cyykyikari
      121 egttaassyv fvrdfeqpfi nkpdtllvnr kdamwvpclv sipglnvtlr sqssvlwpdg
      181 qevvwddrrg mlvstpllhd alylqcettw gdqdflsnpf lvhitgnely diqllprksl
      241 ellvgeklvl nctvwaefns gvtfdwdypg kqaergkwvp errsqqthte lssiltihnv
      301 sqhdlgsyvc kanngiqrfr estevivhen pfisvewlkg pileatagde lvklpvklaa
      361 ypppefqwyk dgkalsgrhs phalvlkevt eastgtytla lwnsaaglrr nislelvvnv
      421 ppqihekeas spsiysrhsr qaltctaygv plplsiqwhw rpwtpckmfa qrslrrrqqq
      481 dlmpqcrdwr avttqdavnp iesldtwtef vegknktvsk lviqnanvsa mykcvvsnkv
      541 gqderliyfy vttipdgfti eskpseelle gqpvllscqa dsykyehlrw yrlnlstlhd
      601 ahgnpllldc knvhlfatpl aasleevapg arhatlslsi prvapehegh yvcevqdrrs
      661 hdkhchkkyl svqaleaprl tqnltdllvn vsdslemqcl vagahapsiv wykderllee
      721 ksgvdladsn qklsiqrvre edagrylcsv cnakgcvnss asvavegsed kgsmeivilv
      781 gtgviavffw vllllifcnm rrpahadikt gylsiimdpg evpleeqcey lsydasqwef
      841 prerlhlgrv lgygafgkvv easafgihkg sscdtvavkm lkegataseh ralmselkil
      901 ihignhlnvv nllgactkpq gplmvivefc kygnlsnflr akrdafspca ekspeqrgrf
      961 ramvelarld rrrpgssdrv lfarfskteg garraspdqe aedlwlsplt medlvcysfq
     1021 vargmeflas rkcihrdlaa rnillsesdv vkicdfglar diykdpdyvr kgsarlplkw
     1081 mapesifdkv yttqsdvwsf gvllweifsl gaspypgvqi neefcqrlrd gtrmrapela
     1141 tpairrimln cwsgdpkarp afselveilg dllqgrglqe eeevcmaprs sqsseegsfs
     1201 qvstmalhia qadaedspps lqrhslaary ynwvsfpgcl argaetrgss rmktfeefpm
     1261 tpttykgsvd nqtdsgmvla seefeqiesr hrqesgfrgt rrtrga
//
LOCUS       NP_001269525             189 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 7 isoform j precursor [Homo sapiens].
ACCESSION   NP_001269525 XP_005245447
VERSION     NP_001269525.1
DBSOURCE    REFSEQ: accession NM_001282596.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Chu,E., Wu,J., Kang,S.S. and Kang,Y.
  TITLE     SLAMF7 as a Promising Immunotherapeutic Target in Multiple Myeloma
            Treatments
  JOURNAL   Curr Oncol 30 (9), 7891-7903 (2023)
   PUBMED   37754488
  REMARK    GeneRIF: SLAMF7 as a Promising Immunotherapeutic Target in Multiple
            Myeloma Treatments.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Choe,U., Pham,Q., Kim,Y.S., Yu,L. and Wang,T.T.Y.
  TITLE     Identification and elucidation of cross talk between SLAM Family
            Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages
  JOURNAL   Sci Rep 13 (1), 11007 (2023)
   PUBMED   37420084
  REMARK    GeneRIF: Identification and elucidation of cross talk between SLAM
            Family Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 189)
  AUTHORS   O'Connell,P., Blake,M.K., Godbehere,S., Amalfitano,A. and
            Aldhamen,Y.A.
  TITLE     SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity
  JOURNAL   J Neuroinflammation 19 (1), 241 (2022)
   PUBMED   36199066
  REMARK    GeneRIF: SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Simmons,D.P., Nguyen,H.N., Gomez-Rivas,E., Jeong,Y., Jonsson,A.H.,
            Chen,A.F., Lange,J.K., Dyer,G.S., Blazar,P., Earp,B.E.,
            Coblyn,J.S., Massarotti,E.M., Sparks,J.A., Todd,D.J., Rao,D.A.,
            Kim,E.Y. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership (AMP) RA/SLE Network
  TITLE     SLAMF7 engagement superactivates macrophages in acute and chronic
            inflammation
  JOURNAL   Sci Immunol 7 (68), eabf2846 (2022)
   PUBMED   35148199
  REMARK    GeneRIF: SLAMF7 engagement superactivates macrophages in acute and
            chronic inflammation.
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Lee,J.K., Boles,K.S. and Mathew,P.A.
  TITLE     Molecular and functional characterization of a CS1 (CRACC) splice
            variant expressed in human NK cells that does not contain
            immunoreceptor tyrosine-based switch motifs
  JOURNAL   Eur J Immunol 34 (10), 2791-2799 (2004)
   PUBMED   15368295
  REMARK    GeneRIF: CS1-L and CS1-S may differentially regulate human NK cell
            functions
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Tovar,V., del Valle,J., Zapater,N., Martin,M., Romero,X.,
            Pizcueta,P., Bosch,J., Terhorst,C. and Engel,P.
  TITLE     Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family
            of leukocyte cell-surface receptors
  JOURNAL   Immunogenetics 54 (6), 394-402 (2002)
   PUBMED   12242590
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Murphy,J.J., Hobby,P., Vilarino-Varela,J., Bishop,B.,
            Iordanidou,P., Sutton,B.J. and Norton,J.D.
  TITLE     A novel immunoglobulin superfamily receptor (19A) related to CD2 is
            expressed on activated lymphocytes and promotes homotypic B-cell
            adhesion
  JOURNAL   Biochem J 361 (Pt 3), 431-436 (2002)
   PUBMED   11802771
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Bouchon,A., Cella,M., Grierson,H.L., Cohen,J.I. and Colonna,M.
  TITLE     Activation of NK cell-mediated cytotoxicity by a SAP-independent
            receptor of the CD2 family
  JOURNAL   J Immunol 167 (10), 5517-5521 (2001)
   PUBMED   11698418
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Boles,K.S. and Mathew,P.A.
  TITLE     Molecular cloning of CS1, a novel human natural killer cell
            receptor belonging to the CD2 subset of the immunoglobulin
            superfamily
  JOURNAL   Immunogenetics 52 (3-4), 302-307 (2001)
   PUBMED   11220635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388332.1, DA644251.1, AL121985.13 and BQ000581.1.
            
            On Sep 14, 2013 this sequence version replaced XP_005245447.1.
            
            Transcript Variant: This variant (10) lacks an alternate in-frame
            exon in the 5' coding region, and also lacks an alternate exon that
            results in a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (j) has a distinct C-terminus and is
            shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.666316.1, DA644251.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..189
                     /product="SLAM family member 7 isoform j precursor"
                     /note="CD2-like receptor activating cytotoxic cells; 19A24
                     protein; novel LY9 (lymphocyte antigen 9) like protein;
                     protein 19A; CD2 subset 1; membrane protein FOAP-12"
                     /calculated_mol_wt=17834
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3176
     CDS             1..189
                     /gene="SLAMF7"
                     /gene_synonym="19A; CD319; CRACC; CS1"
                     /coded_by="NM_001282596.2:56..625"
                     /note="isoform j precursor is encoded by transcript
                     variant 10"
                     /db_xref="GeneID:57823"
                     /db_xref="HGNC:HGNC:21394"
                     /db_xref="MIM:606625"
ORIGIN      
        1 magsptcltl iyilwqlteh lskpkvtmgl qsnkngtcvt nltccmehge edviytwkal
       61 gqaaneshng silpiswrwg esdmtficva rnpvsrnfss pilarklceg aaddpdssmv
      121 llclllvpll lslfvlglfl wflkrerqee nnpkgrssky gllhcgntek dgkspltahd
      181 arhtkaicl
//
LOCUS       NP_002528                189 aa            linear   PRI 20-NOV-2025
DEFINITION  ornithine decarboxylase antizyme 2 isoform 1 [Homo sapiens].
ACCESSION   NP_002528
VERSION     NP_002528.1
DBSOURCE    REFSEQ: accession NM_002537.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Li,Y., Gong,P., Hou,J.X., Huang,W., Ma,X.P., Wang,Y.L., Li,J.,
            Cui,X.B. and Li,N.
  TITLE     miR-34a Regulates Multidrug Resistance via Positively Modulating
            OAZ2 Signaling in Colon Cancer Cells
  JOURNAL   J Immunol Res 2018, 7498514 (2018)
   PUBMED   30175154
  REMARK    GeneRIF: this study reveals a critical role of miR-34a/OAZ2 cascade
            in conferring a proper cellular response to colon cancer
            chemotherapy
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Murai,N., Shimizu,A., Murakami,Y. and Matsufuji,S.
  TITLE     Subcellular localization and phosphorylation of antizyme 2
  JOURNAL   J Cell Biochem 108 (4), 1012-1021 (2009)
   PUBMED   19725046
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Ivanov,I.P. and Atkins,J.F.
  TITLE     Ribosomal frameshifting in decoding antizyme mRNAs from yeast and
            protists to humans: close to 300 cases reveal remarkable diversity
            despite underlying conservation
  JOURNAL   Nucleic Acids Res 35 (6), 1842-1858 (2007)
   PUBMED   17332016
  REMARK    Review article
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Mangold,U. and Leberer,E.
  TITLE     Regulation of all members of the antizyme family by antizyme
            inhibitor
  JOURNAL   Biochem J 385 (Pt 1), 21-28 (2005)
   PUBMED   15355308
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Chen,H., MacDonald,A. and Coffino,P.
  TITLE     Structural elements of antizymes 1 and 2 are required for
            proteasomal degradation of ornithine decarboxylase
  JOURNAL   J Biol Chem 277 (48), 45957-45961 (2002)
   PUBMED   12359729
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Zhou,J., Atkins,J.F. and Gesteland,R.F.
  TITLE     Structure of human ornithine decarboxylase antizyme 2 gene
  JOURNAL   Gene 232 (2), 165-171 (1999)
   PUBMED   10352227
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Ivanov,I.P., Gesteland,R.F. and Atkins,J.F.
  TITLE     A second mammalian antizyme: conservation of programmed ribosomal
            frameshifting
  JOURNAL   Genomics 52 (2), 119-129 (1998)
   PUBMED   9782076
  REMARK    GeneRIF: The protein product is generated using polyamine-regulated
            programmed ribosomal frameshifting.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA210449.1, BC035493.2 and
            BG059726.1.
            
            Summary: The protein encoded by this gene belongs to the ornithine
            decarboxylase antizyme family, which plays a role in cell growth
            and proliferation by regulating intracellular polyamines.
            Expression of antizymes requires +1 ribosomal frameshifting, which
            is enhanced by high levels of polyamines. Antizymes in turn bind to
            and inhibit ornithine decarboxylase (ODC), the key enzyme in
            polyamine biosynthesis; thus, completing the auto-regulatory
            circuit. This gene encodes antizyme 2, the second member of the
            antizyme family. Like antizyme 1, antizyme 2 has broad tissue
            distribution, inhibits ODC activity and polyamine uptake, and
            stimulates ODC degradation in vivo; however, it fails to promote
            ODC degradation in vitro. Antizyme 2 is expressed at lower levels
            than antizyme 1, but is evolutionary more conserved, suggesting it
            likely has an important biological role. Studies also show
            different subcellular localization of antizymes 1 and 2, indicating
            specific function for each antizyme in discrete compartments of the
            cell. Alternatively spliced transcript variants have been found for
            this gene. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.178414.1,
                                           SRR1660803.240986.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2162568
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ribosomal slippage     :: inferred from conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..189
                     /product="ornithine decarboxylase antizyme 2 isoform 1"
                     /note="ODC-Az 2"
                     /calculated_mol_wt=20880
     Region          <100..181
                     /region_name="ODC_AZ"
                     /note="Ornithine decarboxylase antizyme; pfam02100"
                     /db_xref="CDD:460445"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08608; propagated from
                     UniProtKB/Swiss-Prot (O95190.1)"
     CDS             1..189
                     /gene="OAZ2"
                     /gene_synonym="AZ2"
                     /coded_by="join(NM_002537.3:234..329,
                     NM_002537.3:331..804)"
                     /ribosomal_slippage
                     /note="protein translation is dependent on
                     polyamine-induced +1 ribosomal frameshift; isoform 1 is
                     encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS58372.1"
                     /db_xref="GeneID:4947"
                     /db_xref="HGNC:HGNC:8096"
                     /db_xref="MIM:604152"
ORIGIN      
        1 mintqdssil plsncpqlqc crhivpgplw csdaphplsk ipggrgggrd pslsaliykd
       61 ekltvtqdlp vndgkphivh fqyevtevkv sswdavlssq slfveipdgl ladgskegll
      121 allefaeekm kvnyvficfr kgredrapll ktfsflgfei vrpghpcvps rpdvmfmvyp
      181 ldqnlsded
//
LOCUS       NP_001355638             143 aa            linear   PRI 20-NOV-2025
DEFINITION  core-binding factor subunit beta isoform 5 [Homo sapiens].
ACCESSION   NP_001355638 XP_016879301
VERSION     NP_001355638.1
DBSOURCE    REFSEQ: accession NM_001368709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 143)
  AUTHORS   Samsa,W.E., Zhang,Z. and Gong,Z.
  TITLE     CBFbeta Regulates RUNX3 ADP-Ribosylation to Mediate Homologous
            Recombination Repair
  JOURNAL   J Cell Physiol 240 (1), e31503 (2025)
   PUBMED   39696918
REFERENCE   2  (residues 1 to 143)
  AUTHORS   Beyltjens,T., Boudin,E., Revencu,N., Boeckx,N., Bertrand,M.,
            Schutz,L., Haack,T.B., Weber,A., Biliouri,E., Vinksel,M.,
            Zagozen,A., Peterlin,B., Pai,S., Telegrafi,A., Henderson,L.B.,
            Ells,C., Turner,L., Wuyts,W., Van Hul,W., Hendrickx,G. and
            Mortier,G.R.
  TITLE     Heterozygous pathogenic variants involving CBFB cause a new
            skeletal disorder resembling cleidocranial dysplasia
  JOURNAL   J Med Genet 60 (5), 498-504 (2023)
   PUBMED   36241386
  REMARK    GeneRIF: Heterozygous pathogenic variants involving CBFB cause a
            new skeletal disorder resembling cleidocranial dysplasia.
REFERENCE   3  (residues 1 to 143)
  AUTHORS   Malik,N., Kim,Y.I., Yan,H., Tseng,Y.C., du Bois,W., Ayaz,G.,
            Tran,A.D., Vera-Ramirez,L., Yang,H., Michalowski,A.M., Kruhlak,M.,
            Lee,M., Hunter,K.W. and Huang,J.
  TITLE     Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer
  JOURNAL   Cancer Res 83 (8), 1280-1298 (2023)
   PUBMED   36799863
  REMARK    GeneRIF: Dysregulation of Mitochondrial Translation Caused by CBFB
            Deficiency Cooperates with Mutant PIK3CA and Is a Vulnerability in
            Breast Cancer.
REFERENCE   4  (residues 1 to 143)
  AUTHORS   Khan,A.S., Campbell,K.J., Cameron,E.R. and Blyth,K.
  TITLE     The RUNX/CBFbeta Complex in Breast Cancer: A Conundrum of Context
  JOURNAL   Cells 12 (4), 641 (2023)
   PUBMED   36831308
  REMARK    GeneRIF: The RUNX/CFBbeta Complex in Breast Cancer: A Conundrum of
            Context.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 143)
  AUTHORS   Jiang,Y., Chao,H.Y., Lu,X.Z., Wu,P. and Sun,X.C.
  TITLE     [Molecular Genetic Characteristics of Acute Myeloid Leukemia
            Patients with CBFbeta-MYH11 Positive]
  JOURNAL   Zhongguo Shi Yan Xue Ye Xue Za Zhi 30 (6), 1661-1667 (2022)
   PUBMED   36476886
  REMARK    GeneRIF: [Molecular Genetic Characteristics of Acute Myeloid
            Leukemia Patients with CBFbeta-MYH11 Positive].
REFERENCE   6  (residues 1 to 143)
  AUTHORS   Chiba,N., Watanabe,T., Nomura,S., Tanaka,Y., Minowa,M., Niki,M.,
            Kanamaru,R. and Satake,M.
  TITLE     Differentiation dependent expression and distinct subcellular
            localization of the protooncogene product, PEBP2beta/CBFbeta, in
            muscle development
  JOURNAL   Oncogene 14 (21), 2543-2552 (1997)
   PUBMED   9191054
REFERENCE   7  (residues 1 to 143)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 143)
  AUTHORS   Liu,P., Seidel,N., Bodine,D., Speck,N., Tarle,S. and Collins,F.S.
  TITLE     Acute myeloid leukemia with Inv (16) produces a chimeric
            transcription factor with a myosin heavy chain tail
  JOURNAL   Cold Spring Harb Symp Quant Biol 59, 547-553 (1994)
   PUBMED   7587111
REFERENCE   9  (residues 1 to 143)
  AUTHORS   Liu,P., Tarle,S.A., Hajra,A., Claxton,D.F., Marlton,P.,
            Freedman,M., Siciliano,M.J. and Collins,F.S.
  TITLE     Fusion between transcription factor CBF beta/PEBP2 beta and a
            myosin heavy chain in acute myeloid leukemia
  JOURNAL   Science 261 (5124), 1041-1044 (1993)
   PUBMED   8351518
REFERENCE   10 (residues 1 to 143)
  AUTHORS   Muller,C.W. and Schulz,G.E.
  TITLE     Structure of the complex of adenylate kinase from Escherichia coli
            with the inhibitor P1,P5-di(adenosine-5'-)pentaphosphate
  JOURNAL   J Mol Biol 202 (4), 909-912 (1988)
   PUBMED   2845103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009084.9 and AC074143.5.
            
            On Feb 19, 2019 this sequence version replaced XP_016879301.1.
            
            Summary: The protein encoded by this gene is the beta subunit of a
            heterodimeric core-binding transcription factor belonging to the
            PEBP2/CBF transcription factor family which master-regulates a host
            of genes specific to hematopoiesis (e.g., RUNX1) and osteogenesis
            (e.g., RUNX2). The beta subunit is a non-DNA binding regulatory
            subunit; it allosterically enhances DNA binding by alpha subunit as
            the complex binds to the core site of various enhancers and
            promoters, including murine leukemia virus, polyomavirus enhancer,
            T-cell receptor enhancers and GM-CSF promoters. Alternative
            splicing generates two mRNA variants, each encoding a distinct
            carboxyl terminus. In some cases, a pericentric inversion of
            chromosome 16 [inv(16)(p13q22)] produces a chimeric transcript
            consisting of the N terminus of core-binding factor beta in a
            fusion with the C-terminal portion of the smooth muscle myosin
            heavy chain 11. This chromosomal rearrangement is associated with
            acute myeloid leukemia of the M4Eo subtype. Two transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: Variants 5 and 6 encode isoforms that are the
            same length, but have distinct protein sequences.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.3111405.1,
                                           SRR14038192.4125386.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..143
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..143
                     /product="core-binding factor subunit beta isoform 5"
                     /note="SL3/AKV core-binding factor beta subunit;
                     polyomavirus enhancer binding protein 2, beta subunit;
                     SL3-3 enhancer factor 1 beta subunit; CBF-beta; PEA2-beta;
                     PEBP2-beta; SL3-3 enhancer factor 1 subunit beta"
                     /calculated_mol_wt=16979
     Region          1..128
                     /region_name="CBF_beta"
                     /note="Core binding factor beta subunit; pfam02312"
                     /db_xref="CDD:396750"
     CDS             1..143
                     /gene="CBFB"
                     /gene_synonym="CLCD2; PEBP2B"
                     /coded_by="NM_001368709.1:260..691"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:865"
                     /db_xref="HGNC:HGNC:1539"
                     /db_xref="MIM:121360"
ORIGIN      
        1 mprvvpdqrs kfeneeffrk lsreceikyt gfrdrpheer qarfqnacrd grseivylka
       61 pmilngvcvi wkgwidlqrl dgmgclefde eraqqedala qqafeearrr trefedrdrs
      121 hreemevrvs qllavtgkkt trp
//
LOCUS       NP_001340238             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 3 [Homo sapiens].
ACCESSION   NP_001340238
VERSION     NP_001340238.1
DBSOURCE    REFSEQ: accession NM_001353309.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.203769.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 3"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36689
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353309.1:387..1361"
                     /note="isoform 3 is encoded by transcript variant 71"
                     /db_xref="CCDS:CCDS94340.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnlikvltr didhnaahff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001305905             333 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            B isoform b [Homo sapiens].
ACCESSION   NP_001305905 XP_011508715
VERSION     NP_001305905.1
DBSOURCE    REFSEQ: accession NM_001318976.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Okuda,H., Kanai,A., Ito,S., Matsui,H. and Yokoyama,A.
  TITLE     AF4 uses the SL1 components of RNAP1 machinery to initiate MLL
            fusion- and AEP-dependent transcription
  JOURNAL   Nat Commun 6, 8869 (2015)
   PUBMED   26593443
  REMARK    GeneRIF: AEP coactivator complex facilitates the initiation of
            RNAP2-dependent transcription via SL1 activity by loading TBP onto
            the TATA element.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 333)
  AUTHORS   Muth,V., Nadaud,S., Grummt,I. and Voit,R.
  TITLE     Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA
            polymerase I transcription
  JOURNAL   EMBO J 20 (6), 1353-1362 (2001)
   PUBMED   11250901
REFERENCE   7  (residues 1 to 333)
  AUTHORS   Zhai,W. and Comai,L.
  TITLE     Repression of RNA polymerase I transcription by the tumor
            suppressor p53
  JOURNAL   Mol Cell Biol 20 (16), 5930-5938 (2000)
   PUBMED   10913176
REFERENCE   8  (residues 1 to 333)
  AUTHORS   Di Pietro,C., Rapisarda,A., Amico,V., Bonaiuto,C., Viola,A.,
            Scalia,M., Motta,S., Amato,A., Engel,H., Messina,A., Sichel,G.,
            Grzeschik,K. and Purrello,M.
  TITLE     Genomic localization of the human genes TAF1A, TAF1B and TAF1C,
            encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I
            general transcription initiation factor SL1
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 133-136 (2000)
   PUBMED   10894955
REFERENCE   9  (residues 1 to 333)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   10 (residues 1 to 333)
  AUTHORS   Comai,L., Zomerdijk,J.C., Beckmann,H., Zhou,S., Admon,A. and
            Tjian,R.
  TITLE     Reconstitution of transcription factor SL1: exclusive binding of
            TBP by SL1 or TFIID subunits
  JOURNAL   Science 266 (5193), 1966-1972 (1994)
   PUBMED   7801123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA910748.1, AC010969.11,
            AK295402.1, AK308070.1 and AA746267.1.
            
            On Jan 20, 2016 this sequence version replaced XP_011508715.1.
            
            Summary: Initiation of transcription by RNA polymerase I requires
            the formation of a complex composed of the TATA-binding protein
            (TBP) and three TBP-associated factors (TAFs) specific for RNA
            polymerase I. This complex, known as SL1, binds to the core
            promoter of ribosomal RNA genes to position the polymerase properly
            and acts as a channel for regulatory signals. This gene encodes one
            of the SL1-specific TAFs. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (b) is
            shorter at the N-terminus compared to isoform a. Variants 2 and 3
            both encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295402.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..333
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit B isoform b"
                     /note="SL1, 63kD subunit; TBP-associated factor 1B; TATA
                     box-binding protein-associated factor 1B; transcription
                     initiation factor SL1/TIF-IB subunit B; RNA polymerase
                     I-specific TBP-associated factor 63 kDa; TATA box binding
                     protein (TBP)-associated factor, RNA polymerase I, B,
                     63kD; TATA-box binding protein associated factor, RNA
                     polymerase I, B; TATA box binding protein (TBP)-associated
                     factor, RNA polymerase I, B, 63kDa"
                     /calculated_mol_wt=39416
     CDS             1..333
                     /gene="TAF1B"
                     /gene_synonym="MGC:9349; RAF1B; RAFI63; SL1; TAFI63"
                     /coded_by="NM_001318976.1:842..1843"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:9014"
                     /db_xref="HGNC:HGNC:11533"
                     /db_xref="MIM:604904"
ORIGIN      
        1 mklygrdrgi fgieswpdye diykktievg tfldlprfpd itedcylhpn ilcmkylmev
       61 nlpdemhslt chvvkmtgmg evdfltfdpi akmaktvkyd vqavaiivvv lkllflldds
      121 fewslsnlae khneknkkdk pwfdfrkwyq imkkafdekk qkweearaky lwksekplyy
      181 sfvdkpvayk kremvvnlqk qfstlvesta tagkkspssf qfnwteedtd rtcfhghslq
      241 gvlkekgqsl ltknslywls tqkfcrcyct hvttyeesny slsyqfilnl fsfllrikts
      301 llheevslve kklfekkysv krkksrskkv rrh
//
LOCUS       NP_001129511             377 aa            linear   PRI 20-NOV-2025
DEFINITION  NIF3-like protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001129511
VERSION     NP_001129511.1
DBSOURCE    REFSEQ: accession NM_001136039.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Reed,C.J., Hutinet,G. and de Crecy-Lagard,V.
  TITLE     Comparative Genomic Analysis of the DUF34 Protein Family Suggests
            Role as a Metal Ion Chaperone or Insertase
  JOURNAL   Biomolecules 11 (9), 1282 (2021)
   PUBMED   34572495
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Merla,G., Howald,C., Antonarakis,S.E. and Reymond,A.
  TITLE     The subcellular localization of the ChoRE-binding protein, encoded
            by the Williams-Beuren syndrome critical region gene 14, is
            regulated by 14-3-3
  JOURNAL   Hum Mol Genet 13 (14), 1505-1514 (2004)
   PUBMED   15163635
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Tascou,S., Kang,T.W., Trappe,R., Engel,W. and Burfeind,P.
  TITLE     Identification and characterization of NIF3L1 BP1, a novel
            cytoplasmic interaction partner of the NIF3L1 protein
  JOURNAL   Biochem Biophys Res Commun 309 (2), 440-448 (2003)
   PUBMED   12951069
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Akiyama,H., Fujisawa,N., Tashiro,Y., Takanabe,N., Sugiyama,A. and
            Tashiro,F.
  TITLE     The role of transcriptional corepressor Nif3l1 in early stage of
            neural differentiation via cooperation with Trip15/CSN2
  JOURNAL   J Biol Chem 278 (12), 10752-10762 (2003)
   PUBMED   12522100
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Hadano,S., Yanagisawa,Y., Skaug,J., Fichter,K., Nasir,J.,
            Martindale,D., Koop,B.F., Scherer,S.W., Nicholson,D.W.,
            Rouleau,G.A., Ikeda,J. and Hayden,M.R.
  TITLE     Cloning and characterization of three novel genes, ALS2CR1,
            ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis
            (ALS2) critical region at chromosome 2q33-q34: candidate genes for
            ALS2
  JOURNAL   Genomics 71 (2), 200-213 (2001)
   PUBMED   11161814
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Tascou,S., Uedelhoven,J., Dixkens,C., Nayernia,K., Engel,W. and
            Burfeind,P.
  TITLE     Isolation and characterization of a novel human gene, NIF3L1, and
            its mouse ortholog, Nif3l1, highly conserved from bacteria to
            mammals
  JOURNAL   Cytogenet Cell Genet 90 (3-4), 330-336 (2000)
   PUBMED   11124544
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP194872.1, AF283538.1 and BM974977.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.32804.1,
                                           SRR1803615.234537.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..377
                     /product="NIF3-like protein 1 isoform 1"
                     /EC_number="3.5.4.16"
                     /note="amyotrophic lateral sclerosis 2 (juvenile)
                     chromosome region, candidate 1; NIF3 (Ngg1 interacting
                     factor 3, S.pombe homolog)-like 1; NIF3-like protein 1;
                     NIF3 NGG1 interacting factor 3-like 1; amyotrophic lateral
                     sclerosis 2 chromosomal region candidate gene 1 protein;
                     GTP cyclohydrolase I; putative GTP cyclohydrolase 1 type 2
                     NIF3L1"
                     /calculated_mol_wt=41837
     Region          33..354
                     /region_name="NIF3"
                     /note="NIF3 (NGG1p interacting factor 3); pfam01784"
                     /db_xref="CDD:426431"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Region          244..377
                     /region_name="Mediates interaction with COPS2.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9EQ80; propagated from
                     UniProtKB/Swiss-Prot (Q9GZT8.2)"
     CDS             1..377
                     /gene="NIF3L1"
                     /gene_synonym="ALS2CR1; CALS-7; MDS015"
                     /coded_by="NM_001136039.2:92..1225"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46485.1"
                     /db_xref="GeneID:60491"
                     /db_xref="HGNC:HGNC:13390"
                     /db_xref="MIM:605778"
ORIGIN      
        1 mlsscvrpvp ttvrfvdsli cnssrsfmdl kallsslndf aslsfaeswd nvgllvepsp
       61 phtvntlflt ndlteevmee vlqkkadlil syhppifrpm kritwntwke rlviralenr
      121 vgiysphtay daapqgvnnw lakglgacts rpihpskapn yptegnhrve fnvnytqdld
      181 kvmsavkgid gvsvtsfsar tgneeqtrin lnctqkalmq vvdflsrnkq lyqkteilsl
      241 ekplllhtgm grlctldesv slatmidrik rhlklshirl algvgrtles qvkvvalcag
      301 sgssvlqgve adlyltgems hhdtldaasq ginvilcehs ntergflsdl rdmldshlen
      361 kiniilsetd rdplqvv
//
LOCUS       NP_060021               1009 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate receptor ionotropic, delta-1 precursor [Homo sapiens].
ACCESSION   NP_060021 XP_043613
VERSION     NP_060021.1
DBSOURCE    REFSEQ: accession NM_017551.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1009)
  AUTHORS   Allen,J.P., Garber,K.B., Perszyk,R., Khayat,C.T., Kell,S.A.,
            Kaneko,M., Quindipan,C., Saitta,S., Ladda,R.L., Hewson,S.,
            Inbar-Feigenberg,M., Prasad,C., Prasad,A.N., Olewiler,L., Mu,W.,
            Rosenthal,L.S., Scala,M., Striano,P., Zara,F., McCullock,T.W.,
            Jauss,R.T., Lemke,J.R., MacLean,D.M., Zhu,C., Yuan,H., Myers,S.J.
            and Traynelis,S.F.
  TITLE     Clinical features, functional consequences, and rescue pharmacology
            of missense GRID1 and GRID2 human variants
  JOURNAL   Hum Mol Genet 33 (4), 355-373 (2024)
   PUBMED   37944084
  REMARK    GeneRIF: Clinical features, functional consequences, and rescue
            pharmacology of missense GRID1 and GRID2 human variants.
REFERENCE   2  (residues 1 to 1009)
  AUTHORS   Piot,L., Heroven,C., Bossi,S., Zamith,J., Malinauskas,T.,
            Johnson,C., Wennagel,D., Stroebel,D., Charrier,C., Aricescu,A.R.,
            Mony,L. and Paoletti,P.
  TITLE     GluD1 binds GABA and controls inhibitory plasticity
  JOURNAL   Science 382 (6677), 1389-1394 (2023)
   PUBMED   38060673
REFERENCE   3  (residues 1 to 1009)
  AUTHORS   Falzone,M.E. and MacKinnon,R.
  TITLE     The mechanism of Galphaq regulation of PLCbeta3-catalyzed PIP2
            hydrolysis
  JOURNAL   Proc Natl Acad Sci U S A 120 (48), e2315011120 (2023)
   PUBMED   37991948
REFERENCE   4  (residues 1 to 1009)
  AUTHORS   Dai,J., Patzke,C., Liakath-Ali,K., Seigneur,E. and Sudhof,T.C.
  TITLE     GluD1 is a signal transduction device disguised as an ionotropic
            receptor
  JOURNAL   Nature 595 (7866), 261-265 (2021)
   PUBMED   34135511
  REMARK    Erratum:[Nature. 2025 Jun;642(8069):E27. doi:
            10.1038/s41586-025-09146-0. PMID: 40481306]
REFERENCE   5  (residues 1 to 1009)
  AUTHORS   Herbrechter,R., Hube,N., Buchholz,R. and Reiner,A.
  TITLE     Splicing and editing of ionotropic glutamate receptors: a
            comprehensive analysis based on human RNA-Seq data
  JOURNAL   Cell Mol Life Sci 78 (14), 5605-5630 (2021)
   PUBMED   34100982
REFERENCE   6  (residues 1 to 1009)
  AUTHORS   Yue,Z., Horton,A., Bravin,M., DeJager,P.L., Selimi,F. and Heintz,N.
  TITLE     A novel protein complex linking the delta 2 glutamate receptor and
            autophagy: implications for neurodegeneration in lurcher mice
  JOURNAL   Neuron 35 (5), 921-933 (2002)
   PUBMED   12372286
REFERENCE   7  (residues 1 to 1009)
  AUTHORS   Ly,C.D., Roche,K.W., Lee,H.K. and Wenthold,R.J.
  TITLE     Identification of rat EMAP, a delta-glutamate receptor binding
            protein
  JOURNAL   Biochem Biophys Res Commun 291 (1), 85-90 (2002)
   PUBMED   11829466
REFERENCE   8  (residues 1 to 1009)
  AUTHORS   Roche,K.W., Ly,C.D., Petralia,R.S., Wang,Y.X., McGee,A.W.,
            Bredt,D.S. and Wenthold,R.J.
  TITLE     Postsynaptic density-93 interacts with the delta2 glutamate
            receptor subunit at parallel fiber synapses
  JOURNAL   J Neurosci 19 (10), 3926-3934 (1999)
   PUBMED   10234023
REFERENCE   9  (residues 1 to 1009)
  AUTHORS   Treadaway,J. and Zuo,J.
  TITLE     Mapping of the mouse glutamate receptor delta1 subunit (Grid1) to
            chromosome 14
  JOURNAL   Genomics 54 (2), 359-360 (1998)
   PUBMED   9828146
REFERENCE   10 (residues 1 to 1009)
  AUTHORS   Yamazaki,M., Araki,K., Shibata,A. and Mishina,M.
  TITLE     Molecular cloning of a cDNA encoding a novel member of the mouse
            glutamate receptor channel family
  JOURNAL   Biochem Biophys Res Commun 183 (2), 886-892 (1992)
   PUBMED   1372507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL844892.5, DR001156.1,
            AK127168.1, AK293104.1, AB033046.1 and AC022028.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 22, 2004 this sequence version replaced XP_043613.9.
            
            Summary: This gene encodes a subunit of glutamate receptor
            channels. These channels mediate most of the fast excitatory
            synaptic transmission in the central nervous system and play key
            roles in synaptic plasticity.[provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK127168.1, AK293104.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327946.12/ ENSP00000330148.7
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1009
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1-q23.2"
     Protein         1..1009
                     /product="glutamate receptor ionotropic, delta-1
                     precursor"
                     /note="glutamate receptor delta-1 subunit; gluR delta-1
                     subunit; glutamate receptor ionotropic, delta-1"
                     /calculated_mol_wt=109817
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2333
     mat_peptide     21..1009
                     /product="glutamate receptor ionotropic, delta-1"
                     /calculated_mol_wt=109817
     Region          21..436
                     /region_name="Interaction with CBLN1.
                     /evidence=ECO:0000250|UniProtKB:Q61627"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Region          25..425
                     /region_name="PBP1_iGluR_delta_1"
                     /note="N-terminal leucine-isoleucine-valine binding
                     protein (LIVBP)-like domain of the delta1 receptor of an
                     orphan glutamate receptor family; cd06392"
                     /db_xref="CDD:380615"
     Site            order(71..73,77..78,97,100,104..105,108,131..132,164,169,
                     174..176,179,182..183,186,191,193..196,220,350..354)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380615"
     Site            73
                     /site_type="other"
                     /note="Essential for dimerization.
                     /evidence=ECO:0000250|UniProtKB:Q61627; propagated from
                     UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Site            131
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Site            200
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Site            422
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Region          436..806
                     /region_name="PBP2_iGluR_delta_1"
                     /note="The ligand-binding domain of an orphan ionotropic
                     glutamate receptor delta-1, a member of the type 2
                     periplasmic-binding fold protein superfamily; cd13730"
                     /db_xref="CDD:270448"
     Site            order(492,519..521,526,539,685..687,741..742)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:270448"
     Site            498
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:38060673,
                     ECO:0007744|PDB:8BLJ, ECO:0007744|PDB:8BN2,
                     ECO:0007744|PDB:8BN5; propagated from UniProtKB/Swiss-Prot
                     (Q9ULK0.2)"
     Site            563..583
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Site            638..658
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Site            831..851
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULK0.2)"
     Region          930..954
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULK0.2)"
     CDS             1..1009
                     /gene="GRID1"
                     /gene_synonym="GluD1; GluD1-b"
                     /coded_by="NM_017551.3:404..3433"
                     /db_xref="CCDS:CCDS31236.1"
                     /db_xref="GeneID:2894"
                     /db_xref="HGNC:HGNC:4575"
                     /db_xref="MIM:610659"
ORIGIN      
        1 mealtlwllp wicqcvsvra dsiihigaif eenaakddrv fqlavsdlsl nddilqseki
       61 tysikviean npfqavqeac dlmtqgilal vtstgcasan alqsltdamh iphlfvqrnp
      121 ggsprtachl npspdgeayt lasrppvrln dvmlrlvtel rwqkfvmfyd seydirglqs
      181 fldqasrlgl dvslqkvdkn ishvftslft tmkteelnry rdtlrraill lspqgahsfi
      241 neavetnlas kdshwvfvne eisdpeildl vhsalgrmtv vrqifpsakd nqkctrnnhr
      301 issllcdpqe gylqmlqisn lylydsvlml anafhrkled rkwhsmasln cirkstkpwn
      361 ggrsmldtik kghitgltgv mefredssnp yvqfeilgtt ysetfgkdmr klatwdsekg
      421 lngslqerpm gsrlqgltlk vvtvleepfv mvaenilgqp krykgfsidv ldalakalgf
      481 kyeiyqapdg ryghqlhnts wngmigelis kradlaisai titperesvv dfskrymdys
      541 vgilikkpee kisifslfap fdfavwacia aaipvvgvli fvlnriqavr aqsaaqprps
      601 asatlhsaiw ivygafvqqg gessvnsmam rivmgswwlf tlivcssyta nlaafltvsr
      661 mdnpirtfqd lskqvemsyg tvrdsavyey frakgtnple qdstfaelwr tisknggadn
      721 cvsspsegir kakkgnyafl wdvavveyaa ltdddcsvtv ignsisskgy gialqhgspy
      781 rdlfsqrile lqdtgdldvl kqkwwphmgr cdltshasaq adgkslklhs fagvfcilai
      841 glllaclvaa lelwwnsnrc hqetpkedke vnleqvhrrm nslmdediah kqispasiel
      901 salemgglap tqtleptrey qntqlsvstf lpeqsshgts rtlssgpssn lplplsssat
      961 mpsmqckhrs pngglfrqsp vktpipmsfq pvpggvlpea ldtshgtsi
//
LOCUS       NP_065873               1235 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium channel subfamily T member 1 isoform 1 [Homo sapiens].
ACCESSION   NP_065873 XP_029962
VERSION     NP_065873.2
DBSOURCE    REFSEQ: accession NM_020822.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1235)
  AUTHORS   Cole,B.A., Kalli,A.C., Pilati,N., Muench,S.P. and Lippiat,J.D.
  TITLE     A molecular switch in RCK2 triggers sodium-dependent activation of
            KNa1.1 (KCNT1) potassium channels
  JOURNAL   Biophys J 123 (14), 2145-2153 (2024)
   PUBMED   38605520
  REMARK    GeneRIF: A molecular switch in RCK2 triggers sodium-dependent
            activation of KNa1.1 (KCNT1) potassium channels.
REFERENCE   2  (residues 1 to 1235)
  AUTHORS   Yuan,T., Wang,Y., Jin,Y., Yang,H., Xu,S., Zhang,H., Chen,Q., Li,N.,
            Ma,X., Song,H., Peng,C., Geng,Z., Dong,J., Duan,G., Sun,Q.,
            Yang,Y., Yang,F. and Huang,Z.
  TITLE     Coupling of Slack and NaV1.6 sensitizes Slack to quinidine blockade
            and guides anti-seizure strategy development
  JOURNAL   Elife 12, 87559 (2024)
   PUBMED   38289338
  REMARK    GeneRIF: Coupling of Slack and NaV1.6 sensitizes Slack to quinidine
            blockade and guides anti-seizure strategy development.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1235)
  AUTHORS   Zhang,J., Liu,S., Fan,J., Yan,R., Huang,B., Zhou,F., Yuan,T.,
            Gong,J., Huang,Z. and Jiang,D.
  TITLE     Structural basis of human Slo2.2 channel gating and modulation
  JOURNAL   Cell Rep 42 (8), 112858 (2023)
   PUBMED   37494189
REFERENCE   4  (residues 1 to 1235)
  AUTHORS   Hinckley,C.A., Zhu,Z., Chu,J.H., Gubbels,C., Danker,T.,
            Cherry,J.J., Whelan,C.D., Engle,S.J. and Nguyen,V.
  TITLE     Functional evaluation of epilepsy-associated KCNT1 variants in
            multiple cellular systems reveals a predominant gain of function
            impact on channel properties
  JOURNAL   Epilepsia 64 (8), 2126-2136 (2023)
   PUBMED   37177976
  REMARK    GeneRIF: Functional evaluation of epilepsy-associated KCNT1
            variants in multiple cellular systems reveals a predominant gain of
            function impact on channel properties.
REFERENCE   5  (residues 1 to 1235)
  AUTHORS   Barcia,G., Fleming,M.R., Deligniere,A., Gazula,V.R., Brown,M.R.,
            Langouet,M., Chen,H., Kronengold,J., Abhyankar,A., Cilio,R.,
            Nitschke,P., Kaminska,A., Boddaert,N., Casanova,J.L., Desguerre,I.,
            Munnich,A., Dulac,O., Kaczmarek,L.K., Colleaux,L. and Nabbout,R.
  TITLE     De novo gain-of-function KCNT1 channel mutations cause malignant
            migrating partial seizures of infancy
  JOURNAL   Nat Genet 44 (11), 1255-1259 (2012)
   PUBMED   23086397
  REMARK    GeneRIF: Our data identify KCNT1 as a major disease-associated gene
            in Malignant migrating partial seizures of infancy .
REFERENCE   6  (residues 1 to 1235)
  AUTHORS   Heron,S.E., Smith,K.R., Bahlo,M., Nobili,L., Kahana,E.,
            Licchetta,L., Oliver,K.L., Mazarib,A., Afawi,Z., Korczyn,A.,
            Plazzi,G., Petrou,S., Berkovic,S.F., Scheffer,I.E. and Dibbens,L.M.
  TITLE     Missense mutations in the sodium-gated potassium channel gene KCNT1
            cause severe autosomal dominant nocturnal frontal lobe epilepsy
  JOURNAL   Nat Genet 44 (11), 1188-1190 (2012)
   PUBMED   23086396
  REMARK    GeneRIF: Mutations in KCNT1 cause a severe form of ADNFLE and
            sporadic NFLE.
REFERENCE   7  (residues 1 to 1235)
  AUTHORS   Wei,A.D., Gutman,G.A., Aldrich,R., Chandy,K.G., Grissmer,S. and
            Wulff,H.
  TITLE     International Union of Pharmacology. LII. Nomenclature and
            molecular relationships of calcium-activated potassium channels
  JOURNAL   Pharmacol Rev 57 (4), 463-472 (2005)
   PUBMED   16382103
  REMARK    Review article
REFERENCE   8  (residues 1 to 1235)
  AUTHORS   Humphray,S.J., Oliver,K., Hunt,A.R., Plumb,R.W., Loveland,J.E.,
            Howe,K.L., Andrews,T.D., Searle,S., Hunt,S.E., Scott,C.E.,
            Jones,M.C., Ainscough,R., Almeida,J.P., Ambrose,K.D., Ashwell,R.I.,
            Babbage,A.K., Babbage,S., Bagguley,C.L., Bailey,J., Banerjee,R.,
            Barker,D.J., Barlow,K.F., Bates,K., Beasley,H., Beasley,O.,
            Bird,C.P., Bray-Allen,S., Brown,A.J., Brown,J.Y., Burford,D.,
            Burrill,W., Burton,J., Carder,C., Carter,N.P., Chapman,J.C.,
            Chen,Y., Clarke,G., Clark,S.Y., Clee,C.M., Clegg,S., Collier,R.E.,
            Corby,N., Crosier,M., Cummings,A.T., Davies,J., Dhami,P., Dunn,M.,
            Dutta,I., Dyer,L.W., Earthrowl,M.E., Faulkner,L., Fleming,C.J.,
            Frankish,A., Frankland,J.A., French,L., Fricker,D.G., Garner,P.,
            Garnett,J., Ghori,J., Gilbert,J.G., Glison,C., Grafham,D.V.,
            Gribble,S., Griffiths,C., Griffiths-Jones,S., Grocock,R., Guy,J.,
            Hall,R.E., Hammond,S., Harley,J.L., Harrison,E.S., Hart,E.A.,
            Heath,P.D., Henderson,C.D., Hopkins,B.L., Howard,P.J., Howden,P.J.,
            Huckle,E., Johnson,C., Johnson,D., Joy,A.A., Kay,M., Keenan,S.,
            Kershaw,J.K., Kimberley,A.M., King,A., Knights,A., Laird,G.K.,
            Langford,C., Lawlor,S., Leongamornlert,D.A., Leversha,M., Lloyd,C.,
            Lloyd,D.M., Lovell,J., Martin,S., Mashreghi-Mohammadi,M.,
            Matthews,L., McLaren,S., McLay,K.E., McMurray,A., Milne,S.,
            Nickerson,T., Nisbett,J., Nordsiek,G., Pearce,A.V., Peck,A.I.,
            Porter,K.M., Pandian,R., Pelan,S., Phillimore,B., Povey,S.,
            Ramsey,Y., Rand,V., Scharfe,M., Sehra,H.K., Shownkeen,R.,
            Sims,S.K., Skuce,C.D., Smith,M., Steward,C.A., Swarbreck,D.,
            Sycamore,N., Tester,J., Thorpe,A., Tracey,A., Tromans,A.,
            Thomas,D.W., Wall,M., Wallis,J.M., West,A.P., Whitehead,S.L.,
            Willey,D.L., Williams,S.A., Wilming,L., Wray,P.W., Young,L.,
            Ashurst,J.L., Coulson,A., Blocker,H., Durbin,R., Sulston,J.E.,
            Hubbard,T., Jackson,M.J., Bentley,D.R., Beck,S., Rogers,J. and
            Dunham,I.
  TITLE     DNA sequence and analysis of human chromosome 9
  JOURNAL   Nature 429 (6990), 369-374 (2004)
   PUBMED   15164053
REFERENCE   9  (residues 1 to 1235)
  AUTHORS   Gertler,T., Bearden,D., Bhattacharjee,A. and Carvill,G.
  TITLE     KCNT1-Related Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30234941
REFERENCE   10 (residues 1 to 1235)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK127272.1, BC171770.1,
            DA095802.1, BX110871.1 and AL158822.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 19, 2009 this sequence version replaced NP_065873.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. This gene encodes a sodium-activated
            potassium channel subunit which is thought to function in ion
            conductance and developmental signaling pathways. Mutations in this
            gene cause the early-onset epileptic disorders, malignant migrating
            partial seizures of infancy and autosomal dominant nocturnal
            frontal lobe epilepsy. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC136618.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371757.7/ ENSP00000360822.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.3"
     Protein         1..1235
                     /product="potassium channel subfamily T member 1 isoform
                     1"
                     /note="potassium channel, subfamily T, member 1; Sequence
                     like a calcium-activated K+ channel; potassium channel,
                     sodium activated subfamily T, member 1; sodium and
                     chloride-activated ATP-sensitive potassium channel Slo2.2"
                     /calculated_mol_wt=139569
     Region          162..342
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          277..350
                     /region_name="Ion_trans_2"
                     /note="Ion channel; pfam07885"
                     /db_xref="CDD:462301"
     Region          504..598
                     /region_name="BK_channel_a"
                     /note="Calcium-activated BK potassium channel alpha
                     subunit; pfam03493"
                     /db_xref="CDD:460947"
     CDS             1..1235
                     /gene="KCNT1"
                     /gene_synonym="bA100C15.2; DEE14; EIEE14; ENFL5; KCa4.1;
                     KNa1.1; SLACK; Slo2.2"
                     /coded_by="NM_020822.3:75..3782"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35175.2"
                     /db_xref="GeneID:57582"
                     /db_xref="HGNC:HGNC:18865"
                     /db_xref="MIM:608167"
ORIGIN      
        1 mplpdgartp ggvcreargg gytnrtfefd dgqcaprrpc agdgalldta gfkmsdldse
       61 vlplppryrf rdlllgdpsf qnddrvqvef yvnentfker lklffiknqr sslrirlfnf
      121 slklltclly ivrvllddpa lgigcwgcpk qnysfndsss einwapilwv erkmtlwaiq
      181 vivaiisfle tmlliylsyk gniweqifrv sfvlemintl pfiitifwpp lrnlfipvfl
      241 ncwlakhale nmindfhrai lrtqsamfnq vlilfctllc lvftgtcgiq hleragenls
      301 lltsfyfciv tfstvgygdv tpkiwpsqll vvimicvalv vlplqfeelv ylwmerqksg
      361 gnysrhraqt ekhvvlcvss lkidllmdfl nefyahprlq dyyvvilcpt emdvqvrrvl
      421 qiplwsqrvi ylqgsalkdq dlmrakmdng eacfilssrn evdrtaadhq tilrawavkd
      481 fapncplyvq ilkpenkfhv kfadhvvcee eckyamlaln cicpatstli tllvhtsrgq
      541 egqespeqwq rmygrcsgne vyhirmgdsk ffreyegksf tyaafhahkk ygvcliglkr
      601 ednksillnp gprhilaasd tcfyinitke ensafifkqe ekrkkrafsg qglhegparl
      661 pvhsiiasmg tvamdlqgte hrptqsgggg ggsklalpte ngsgsrrpsi apvleladss
      721 allpcdllsd qsedevtpsd deglsvveyv kgyppnspyi gssptlchll pvkapfcclr
      781 ldkgckhnsy edakaygfkn kliivsaeta gnglynfivp lrayyrsrke lnpivllldn
      841 kpdhhfleai ccfpmvyyme gsvdnldsll qcgiiyadnl vvvdkestms aeedymadak
      901 tivnvqtmfr lfpslsitte lthpsnmrfm qfrakdsysl alsklekrer engsnlafmf
      961 rlpfaagrvf sismldtlly qsfvkdymit itrlllgldt tpgsgylcam kitegdlwir
     1021 tygrlfqklc sssaeipigi yrteshvfst sephdlraqs qisvnvedce dtrevkgpwg
     1081 sragtggssq grhtgggdpa ehpllrrksl qwarrlsrka pkqagraaaa ewisqqrlsl
     1141 yrrserqels elvknrmkhl glpttgydem ndhqntlsyv linpppdtrl epsdivylir
     1201 sdplahvass sqsrksscsh klsscnpetr detql
//
LOCUS       NP_057307                424 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 3
            [Homo sapiens].
ACCESSION   NP_057307 XP_005252937
VERSION     NP_057307.2
DBSOURCE    REFSEQ: accession NM_016223.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 424)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 424)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 424)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 424)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 424)
  AUTHORS   Tanaka,M., Nanba,D., Mori,S., Shiba,F., Ishiguro,H., Yoshino,K.,
            Matsuura,N. and Higashiyama,S.
  TITLE     ADAM binding protein Eve-1 is required for ectodomain shedding of
            epidermal growth factor receptor ligands
  JOURNAL   J Biol Chem 279 (40), 41950-41959 (2004)
   PUBMED   15280379
REFERENCE   6  (residues 1 to 424)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 424)
  AUTHORS   Mori,S., Tanaka,M., Nanba,D., Nishiwaki,E., Ishiguro,H.,
            Higashiyama,S. and Matsuura,N.
  TITLE     PACSIN3 binds ADAM12/meltrin alpha and up-regulates ectodomain
            shedding of heparin-binding epidermal growth factor-like growth
            factor
  JOURNAL   J Biol Chem 278 (46), 46029-46034 (2003)
   PUBMED   12952982
  REMARK    GeneRIF: PACSIN3 has a novel function as an up-regulator in the
            signaling of proHB-EGF shedding induced by TPA and angiotensin II
REFERENCE   8  (residues 1 to 424)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 424)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 424)
  AUTHORS   Howard,L., Nelson,K.K., Maciewicz,R.A. and Blobel,C.P.
  TITLE     Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
            two SH3 domain-containing proteins, endophilin I and SH3PX1
  JOURNAL   J Biol Chem 274 (44), 31693-31699 (1999)
   PUBMED   10531379
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI601317.1, BC011889.2 and
            BC007914.2.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005252937.1, NP_057307.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF242530.1, BC007914.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298838.11/ ENSP00000298838.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..424
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..424
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 3"
                     /note="syndapin III; SH3 domain-containing protein 6511"
                     /calculated_mol_wt=48356
     Region          16..273
                     /region_name="BAR"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain, a
                     dimerization module that binds membranes and detects
                     membrane curvature; cl12013"
                     /db_xref="CDD:472257"
     Site            order(25,28..29,33,35..36,39..40,42..43,53..54,56..57,
                     60..61,63..64,67,87,90..91,232,235..236,238,240,243..244,
                     246..247,250..251,254..255,257..258,261..262,264..265)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153365"
     Region          155..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99JB8; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          311..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            324
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            327
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UKS6.2)"
     Region          365..420
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(372,374,377,381,400..401,415,417..418)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212930"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UKS6.2)"
     CDS             1..424
                     /gene="PACSIN3"
                     /gene_synonym="CMYO27; SDPIII"
                     /coded_by="NM_016223.5:190..1464"
                     /db_xref="CCDS:CCDS31481.1"
                     /db_xref="GeneID:29763"
                     /db_xref="HGNC:HGNC:8572"
                     /db_xref="MIM:606513"
ORIGIN      
        1 mapeedagge alggsfweag nyrrtvqrve dghrlcgdlv scfqerarie kayaqqladw
       61 arkwrgtvek gpqygtleka whafftaaer lsalhlevre klqgqdserv rawqrgafhr
      121 pvlggfresr aaedgfrkaq kpwlkrlkev easkksyhaa rkdektaqtr eshakadsav
      181 sqeqlrklqe rvercakeae ktkaqyeqtl aelhrytpry medmeqafet cqaaerqrll
      241 ffkdmlltlh qhldlsssek fhelhrdlhq gieaasdeed lrwwrsthgp gmamnwpqfe
      301 ewsldtqrti srkekggrsp devtltsivp trdgtapppq spgspgtgqd eewsdeespr
      361 kaatgvrvra lydyagqead elsfrageel lkmseedeqg wcqgqlqsgr iglypanyve
      421 cvga
//
LOCUS       NP_919438                736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_919438
VERSION     NP_919438.1
DBSOURCE    REFSEQ: accession NM_194456.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF388384.1, AJ294850.1 and
            AF296765.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) includes 4 exons in the 5'
            UTR. Variants 1-4 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF388384.1, SRR1803612.182977.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_194456.1:785..2995"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_001186274             146 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform b [Homo sapiens].
ACCESSION   NP_001186274
VERSION     NP_001186274.1
DBSOURCE    REFSEQ: accession NM_001199345.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304659.1, DC421808.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2162823 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..146
                     /product="large ribosomal subunit protein uL22 isoform b"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=16963
     Region          <1..127
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     CDS             1..146
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001199345.2:95..535"
                     /note="isoform b is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS56070.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mhirkatkyl kdvtlqkqcv pfrrynggvg rcaqakqwgw tqgrwpkksa efllhmlkna
       61 esnaelkgld vdslviehiq vnkapkmrrr tyrahgrinp ymsspchiem iltekeqivp
      121 kpeeevaqkk kisqkklkkq klmare
//
LOCUS       NP_001269340             237 aa            linear   PRI 20-NOV-2025
DEFINITION  protein phosphatase 1 regulatory subunit 7 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001269340 XP_005247091
VERSION     NP_001269340.1
DBSOURCE    REFSEQ: accession NM_001282411.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 237)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 237)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 237)
  AUTHORS   Jiang,Y., Scott,K.L., Kwak,S.J., Chen,R. and Mardon,G.
  TITLE     Sds22/PP1 links epithelial integrity and tumor suppression via
            regulation of myosin II and JNK signaling
  JOURNAL   Oncogene 30 (29), 3248-3260 (2011)
   PUBMED   21399659
  REMARK    GeneRIF: human Sds22 is focally deleted and downregulated in
            multiple carcinomas, and this downregulation correlates with tumor
            progression, suggesting that sds22 inactivation may contribute to
            tumorigenesis and metastatic potential
REFERENCE   4  (residues 1 to 237)
  AUTHORS   Posch,M., Khoudoli,G.A., Swift,S., King,E.M., Deluca,J.G. and
            Swedlow,J.R.
  TITLE     Sds22 regulates aurora B activity and microtubule-kinetochore
            interactions at mitosis
  JOURNAL   J Cell Biol 191 (1), 61-74 (2010)
   PUBMED   20921135
  REMARK    GeneRIF: Sds22 specifically defines protein phosphatase 1 function
            and localization in mitosis.
REFERENCE   5  (residues 1 to 237)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   6  (residues 1 to 237)
  AUTHORS   Lesage,B., Beullens,M., Pedelini,L., Garcia-Gimeno,M.A.,
            Waelkens,E., Sanz,P. and Bollen,M.
  TITLE     A complex of catalytically inactive protein phosphatase-1
            sandwiched between Sds22 and inhibitor-3
  JOURNAL   Biochemistry 46 (31), 8909-8919 (2007)
   PUBMED   17630778
  REMARK    GeneRIF: Sds22 and Inhibitor-3 form a heterotrimeric complex with
            PP1, both in cell lysates and after purification. A pool of PP1 is
            complexly controlled by both Sds22 and Inhibitor-3.
REFERENCE   7  (residues 1 to 237)
  AUTHORS   Ceulemans,H., Vulsteke,V., De Maeyer,M., Tatchell,K., Stalmans,W.
            and Bollen,M.
  TITLE     Binding of the concave surface of the Sds22 superhelix to the alpha
            4/alpha 5/alpha 6-triangle of protein phosphatase-1
  JOURNAL   J Biol Chem 277 (49), 47331-47337 (2002)
   PUBMED   12226088
REFERENCE   8  (residues 1 to 237)
  AUTHORS   Ceulemans,H., Van Eynde,A., Perez-Callejon,E., Beullens,M.,
            Stalmans,W. and Bollen,M.
  TITLE     Structure and splice products of the human gene encoding sds22, a
            putative mitotic regulator of protein phosphatase-1
  JOURNAL   Eur J Biochem 262 (1), 36-42 (1999)
   PUBMED   10231361
REFERENCE   9  (residues 1 to 237)
  AUTHORS   Renouf,S., Beullens,M., Wera,S., Van Eynde,A., Sikela,J.,
            Stalmans,W. and Bollen,M.
  TITLE     Molecular cloning of a human polypeptide related to yeast sds22, a
            regulator of protein phosphatase-1
  JOURNAL   FEBS Lett 375 (1-2), 75-78 (1995)
   PUBMED   7498485
REFERENCE   10 (residues 1 to 237)
  AUTHORS   Berry,R., Stevens,T.J., Walter,N.A., Wilcox,A.S., Rubano,T.,
            Hopkins,J.A., Weber,J., Goold,R., Soares,M.B. and Sikela,J.M.
  TITLE     Gene-based sequence-tagged-sites (STSs) as the basis for a human
            gene map
  JOURNAL   Nat Genet 10 (4), 415-423 (1995)
   PUBMED   7670491
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC051689.1, AC005237.2,
            BG684153.1 and BC013001.2.
            
            On Sep 7, 2013 this sequence version replaced XP_005247091.1.
            
            Summary: This gene encodes a protein subunit that regulates the
            activity of the serine/threonine phosphatase, protein
            phosphatase-1. The encoded protein is required for completion of
            the mitotic cycle and for targeting protein phosphatase-1 to
            mitotic kinetochores. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (4) lacks alternate exons in the
            coding region and uses an alternate 3' terminal exon compared to
            variant 1. The encoded protein (isoform 4, also known as
            sds22beta2) is shorter and has a distinct C-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.61242.1,
                                           SRR1163657.470135.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..237
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..237
                     /product="protein phosphatase 1 regulatory subunit 7
                     isoform 4"
                     /note="protein phosphatase 1 regulatory subunit 22;
                     protein phosphatase 1, regulatory (inhibitor) subunit 7;
                     testis secretory sperm-binding protein Li 210a"
                     /calculated_mol_wt=27195
     Region          54..>229
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          57..78
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          79..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..122
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          123..144
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          145..166
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          167..188
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          189..210
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     CDS             1..237
                     /gene="PPP1R7"
                     /gene_synonym="SDS22"
                     /coded_by="NM_001282411.1:839..1552"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS63193.1"
                     /db_xref="GeneID:5510"
                     /db_xref="HGNC:HGNC:9295"
                     /db_xref="MIM:602877"
ORIGIN      
        1 maaergagqq qsqemmeeeh elpvdmetin ldrdaedvdl nhyrigkieg fevlkkvktl
       61 clrqnlikci enleelqslr eldlydnqik kienlealte leildisfnl lrniegvdkl
      121 trlkklflvn nkiskienls nlhqlqmlel gsnriraien idtltnlesl flgknkitkl
      181 qnldaltnlt vlsmqsnrlt kieglqnlvn lrelylshng ievieglenn vqdslty
//
LOCUS       NP_060868               1091 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-3 precursor
            [Homo sapiens].
ACCESSION   NP_060868
VERSION     NP_060868.2
DBSOURCE    REFSEQ: accession NM_018398.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Liu,G., Lv,Y., Wang,Y., Xu,Z., Chen,L., Chen,S., Xie,W., Feng,Y.,
            Liu,J., Bai,Y., He,Y., Li,X. and Wu,Q.
  TITLE     Remote ischemic preconditioning reduces mitochondrial apoptosis
            mediated by calpain 1 activation in myocardial ischemia-reperfusion
            injury through calcium channel subunit Cacna2d3
  JOURNAL   Free Radic Biol Med 212, 80-93 (2024)
   PUBMED   38151212
  REMARK    GeneRIF: Remote ischemic preconditioning reduces mitochondrial
            apoptosis mediated by calpain 1 activation in myocardial
            ischemia-reperfusion injury through calcium channel subunit
            Cacna2d3.
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Yu,L.L., Hu,B.W., Huang,H.X., Yu,B., Xiao,Q., Lv,Q.L., Luo,C.H.,
            Guo,C.X., Li,J.G., Xie,X.X. and Yin,J.Y.
  TITLE     A two-stage genome-wide association study identifies novel germline
            genetic variations in CACNA2D3 associated with radiotherapy
            response in nasopharyngeal carcinoma
  JOURNAL   J Transl Med 21 (1), 11 (2023)
   PUBMED   36624463
  REMARK    GeneRIF: A two-stage genome-wide association study identifies novel
            germline genetic variations in CACNA2D3 associated with
            radiotherapy response in nasopharyngeal carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Westhoff,M. and Dixon,R.E.
  TITLE     Mechanisms and Regulation of Cardiac CaV1.2 Trafficking
  JOURNAL   Int J Mol Sci 22 (11), 5927 (2021)
   PUBMED   34072954
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Auxerre-Plantie,E., Nakamori,M., Renaud,Y., Huguet,A., Choquet,C.,
            Dondi,C., Miquerol,L., Takahashi,M.P., Gourdon,G., Junion,G.,
            Jagla,T., Zmojdzian,M. and Jagla,K.
  TITLE     Straightjacket/alpha2delta3 deregulation is associated with cardiac
            conduction defects in myotonic dystrophy type 1
  JOURNAL   Elife 8, e51114 (2019)
   PUBMED   31829940
  REMARK    GeneRIF: The authors show that ventricular alpha2delta3 expression
            is low in healthy mice and humans, but significantly elevated in
            ventricular muscles from DM1 patients with conduction defects.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Smedler,E., Bergen,S.E., Song,J. and Landen,M.
  TITLE     Genes, biomarkers, and clinical features associated with the course
            of bipolar disorder
  JOURNAL   Eur Neuropsychopharmacol 29 (10), 1152-1160 (2019)
   PUBMED   31378653
  REMARK    GeneRIF: CNS sensitisation was associated with a common genetic
            variant near the calcium channel gene CACNA2D3 at genome-wide
            significance.
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Uhl,G.R., Liu,Q.R., Drgon,T., Johnson,C., Walther,D., Rose,J.E.,
            David,S.P., Niaura,R. and Lerman,C.
  TITLE     Molecular genetics of successful smoking cessation: convergent
            genome-wide association study results
  JOURNAL   Arch Gen Psychiatry 65 (6), 683-693 (2008)
   PUBMED   18519826
  REMARK    GeneRIF: Clinical trial and genome-wide association study of
            gene-disease association, gene-environment interaction, and
            pharmacogenomic / toxicogenomic. (HuGE Navigator)
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Abo-Dalo,B., Kim,H.G., Roes,M., Stefanova,M., Higgins,A., Shen,Y.,
            Mundlos,S., Quade,B.J., Gusella,J.F. and Kutsche,K.
  TITLE     Extensive molecular genetic analysis of the 3p14.3 region in
            patients with Zimmermann-Laband syndrome
  JOURNAL   Am J Med Genet A 143A (22), 2668-2674 (2007)
   PUBMED   17937436
  REMARK    GeneRIF: did not detect submicroscopic deletion or duplication nor
            sequence alteration in either CACNA2D3 or WNT5A in ZLS-affected
            individuals
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Qin,N., Yagel,S., Momplaisir,M.L., Codd,E.E. and D'Andrea,M.R.
  TITLE     Molecular cloning and characterization of the human voltage-gated
            calcium channel alpha(2)delta-4 subunit
  JOURNAL   Mol Pharmacol 62 (3), 485-496 (2002)
   PUBMED   12181424
  REMARK    GeneRIF: This publication primarily discusses the alpha2/delta 4
            subunit, but also contains cDNA data relating to the gene described
            in this record.
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Hanke,S., Bugert,P., Chudek,J. and Kovacs,G.
  TITLE     Cloning a calcium channel alpha2delta-3 subunit gene from a
            putative tumor suppressor gene region at chromosome 3p21.1 in
            conventional renal cell carcinoma
  JOURNAL   Gene 264 (1), 69-75 (2001)
   PUBMED   11245980
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC115282.2, AC133010.2,
            AC138059.3, AC137673.2, AC092057.2, AC109584.2, AC092797.2 and
            AC104298.2.
            
            On Oct 13, 2004 this sequence version replaced NP_060868.1.
            
            Summary: This gene encodes a member of the alpha-2/delta subunit
            family, a protein in the voltage-dependent calcium channel complex.
            Calcium channels mediate the influx of calcium ions into the cell
            upon membrane polarization and consist of a complex of alpha-1,
            alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. Various
            versions of each of these subunits exist, either expressed from
            similar genes or the result of alternative splicing. Research on a
            highly similar protein in rabbit suggests the protein described in
            this record is cleaved into alpha-2 and delta subunits. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.38772.1,
                                           SRR1660809.163023.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000474759.6/ ENSP00000419101.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1-p14.3"
     Protein         1..1091
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-3 precursor"
                     /note="calcium channel, voltage-dependent, alpha 2/delta 3
                     subunit; calcium channel alpha2-delta3 subunit;
                     voltage-dependent calcium channel subunit alpha-2/delta-3;
                     voltage-gated calcium channel subunit alpha-2/delta-3;
                     calcium channel, voltage-dependent, alpha 2/delta subunit
                     3; alpha2delta-3"
                     /calculated_mol_wt=119803
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3227
     Region          113..229
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Region          242..425
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(262,264,266,336,370)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          262..266
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Site            309
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Region          <439..569
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Region          508..622
                     /region_name="PDC2_MCP_like"
                     /note="second PDC (PhoQ/DcuS/CitA) domain of
                     methyl-accepting chemotaxis proteins and similar domains;
                     cd12912"
                     /db_xref="CDD:350337"
     Site            553
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Site            632
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Region          655..1068
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            793
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q8CFG5; propagated from
                     UniProtKB/Swiss-Prot (Q8IZS8.1)"
     Site            1069..1089
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZS8.1)"
     CDS             1..1091
                     /gene="CACNA2D3"
                     /gene_synonym="HSA272268"
                     /coded_by="NM_018398.3:163..3438"
                     /db_xref="CCDS:CCDS54598.1"
                     /db_xref="GeneID:55799"
                     /db_xref="HGNC:HGNC:15460"
                     /db_xref="MIM:606399"
ORIGIN      
        1 magpgsprra srgasallaa allyaalgdv vrseqqipls vvklwasafg geiksiaaky
       61 sgsqllqkky keyekdvaie eidglqlvkk laknmeemfh kkseavrrlv eaaeeahlkh
      121 efdadlqyey fnavlinerd kdgnflelgk efilapndhf nnlpvnisls dvqvptnmyn
      181 kdpaivngvy wseslnkvfv dnfdrdpsli wqyfgsakgf frqypgikwe pdengviafd
      241 crnrkwyiqa atspkdvvil vdvsgsmkgl rltiakqtvs sildtlgddd ffniiaynee
      301 lhyvepclng tlvqadrtnk ehfrehldkl fakgigmldi alneafnils dfnhtgqgsi
      361 csqaimlitd gavdtydtif akynwpdrkv riftyligre aafadnlkwm acankgfftq
      421 istladvqen vmeylhvlsr pkvidqehdv vwteayidst lpqaqkltdd qgpvlmttva
      481 mpvfskqnet rskgillgvv gtdvpvkell ktipkyklgi hgyafaitnn gyilthpelr
      541 llyeegkkrr kpnyssvdls evewedrddv lrnamvnrkt gkfsmevkkt vdkgkrvlvm
      601 tndyyytdik gtpfslgval srghgkyffr gnvtieeglh dlehpdvsla dewsycntdl
      661 hpehrhlsql eaiklylkgk epllqcdkel iqevlfdavv sapieaywts lalnksensd
      721 kgvevaflgt rtglsrinlf vgaeqltnqd flkagdkeni fnadhfplwy rraaeqipgs
      781 fvysipfstg pvnksnvvta stsiqllder kspvvaavgi qmkleffqrk fwtasrqcas
      841 ldgkcsiscd detvncylid nngfilvsed ytqtgdffge iegavmnkll tmgsfkritl
      901 ydyqamcran kessdgahgl ldpynaflsa vkwimtelvl flvefnlcsw whsdmtakaq
      961 klkqtlepcd teypafvser tikettgnia cedcsksfvi qqipssnlfm vvvdssclce
     1021 svapitmapi eiryneslkc erlkaqkirr rpeschgfhp eenarecgga pslqaqtvll
     1081 llplllmlfs r
//
LOCUS       NP_001357154             201 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 E2 isoform 1 [Homo sapiens].
ACCESSION   NP_001357154
VERSION     NP_001357154.1
DBSOURCE    REFSEQ: accession NM_001370225.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 201)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 201)
  AUTHORS   Chang,Y.H., Yamamoto,K., Fujino,T., Wang,T.W., Sugimoto,E.,
            Zhang,W., Yabushita,T., Suzaki,K., Pietsch,E.C., Weir,B.A.,
            Crescenzo,R., Cowley,G.S., Attar,R., Philippar,U., Wunderlich,M.,
            Mizukawa,B., Zheng,Y., Enomoto,Y., Imai,Y., Kitamura,T. and
            Goyama,S.
  TITLE     SETDB1 suppresses NK cell-mediated immunosurveillance in acute
            myeloid leukemia with granulo-monocytic differentiation
  JOURNAL   Cell Rep 43 (8), 114536 (2024)
   PUBMED   39096901
REFERENCE   3  (residues 1 to 201)
  AUTHORS   Hong,X., Ma,N., Li,D., Zhang,M., Dong,W., Huang,J., Ci,X. and
            Zhang,S.
  TITLE     UBE2E2 enhances Snail-mediated epithelial-mesenchymal transition
            and Nrf2-mediated antioxidant activity in ovarian cancer
  JOURNAL   Cell Death Dis 14 (2), 100 (2023)
   PUBMED   36765041
  REMARK    GeneRIF: UBE2E2 enhances Snail-mediated epithelial-mesenchymal
            transition and Nrf2-mediated antioxidant activity in ovarian
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 201)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 201)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 201)
  AUTHORS   Pringa,E., Martinez-Noel,G., Muller,U. and Harbers,K.
  TITLE     Interaction of the ring finger-related U-box motif of a nuclear dot
            protein with ubiquitin-conjugating enzymes
  JOURNAL   J Biol Chem 276 (22), 19617-19623 (2001)
   PUBMED   11274149
REFERENCE   7  (residues 1 to 201)
  AUTHORS   Ito,K., Adachi,S., Iwakami,R., Yasuda,H., Muto,Y., Seki,N. and
            Okano,Y.
  TITLE     N-Terminally extended human ubiquitin-conjugating enzymes (E2s)
            mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
  JOURNAL   Eur J Biochem 268 (9), 2725-2732 (2001)
   PUBMED   11322894
REFERENCE   8  (residues 1 to 201)
  AUTHORS   Niwa,J., Ishigaki,S., Doyu,M., Suzuki,T., Tanaka,K. and Sobue,G.
  TITLE     A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin
            ligase activity
  JOURNAL   Biochem Biophys Res Commun 281 (3), 706-713 (2001)
   PUBMED   11237715
REFERENCE   9  (residues 1 to 201)
  AUTHORS   Moynihan,T.P., Ardley,H.C., Nuber,U., Rose,S.A., Jones,P.F.,
            Markham,A.F., Scheffner,M. and Robinson,P.A.
  TITLE     The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with
            RING finger/IBR motif-containing domains of HHARI and H7-AP1
  JOURNAL   J Biol Chem 274 (43), 30963-30968 (1999)
   PUBMED   10521492
REFERENCE   10 (residues 1 to 201)
  AUTHORS   Kimura,M., Hattori,T., Matsuda,Y., Yoshioka,T., Sumi,N., Umeda,Y.,
            Nakashima,S. and Okano,Y.
  TITLE     cDNA cloning, characterization, and chromosome mapping of UBE2E2
            encoding a human ubiquitin-conjugating E2 enzyme
  JOURNAL   Cytogenet Cell Genet 78 (2), 107-111 (1997)
   PUBMED   9371400
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB476522.1, HY006728.1, BI603911.1 and AC116992.2.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.60068.1,
                                           SRR1803611.127658.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..201
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..201
                     /product="ubiquitin-conjugating enzyme E2 E2 isoform 1"
                     /EC_number="2.3.2.23"
                     /note="ubiquitin-conjugating enzyme E2E 2 (homologous to
                     yeast UBC4/5); ubiquitin-conjugating enzyme E2E 2 (UBC4/5
                     homolog, yeast); ubiquitin-protein ligase E2; ubiquitin
                     carrier protein E2; E2 ubiquitin-conjugating enzyme E2;
                     ubiquitin conjugating enzyme E2E 2"
                     /calculated_mol_wt=22124
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96LR5.1)"
     Region          58..198
                     /region_name="UBCc_UBE2E"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 E1-E3 and
                     related proteins; cd23793"
                     /db_xref="CDD:467413"
     CDS             1..201
                     /gene="UBE2E2"
                     /gene_synonym="UBCH8"
                     /coded_by="NM_001370225.1:170..775"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2637.1"
                     /db_xref="GeneID:7325"
                     /db_xref="HGNC:HGNC:12478"
                     /db_xref="MIM:602163"
ORIGIN      
        1 msteaqrvdd spstsggssd gdqresvqqe pereqvqpkk kegkisskta aklstsakri
       61 qkelaeitld pppncsagpk gdniyewrst ilgppgsvye ggvfflditf spdypfkppk
      121 vtfrtriyhc ninsqgvicl dilkdnwspa ltiskvllsi cslltdcnpa dplvgsiatq
      181 ymtnraehdr marqwtkrya t
//
LOCUS       NP_001317105             172 aa            linear   PRI 20-NOV-2025
DEFINITION  coordinator of PRMT5 and differentiation stimulator isoform 2 [Homo
            sapiens].
ACCESSION   NP_001317105 XP_005258057
VERSION     NP_001317105.1
DBSOURCE    REFSEQ: accession NM_001330176.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Krzyzanowski,A., Gasper,R., Adihou,H., Hart,P.'. and Waldmann,H.
  TITLE     Biochemical Investigation of the Interaction of pICln, RioK1 and
            COPR5 with the PRMT5-MEP50 Complex
  JOURNAL   Chembiochem 22 (11), 1908-1914 (2021)
   PUBMED   33624332
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Paul,C., Sardet,C. and Fabbrizio,E.
  TITLE     The histone- and PRMT5-associated protein COPR5 is required for
            myogenic differentiation
  JOURNAL   Cell Death Differ 19 (5), 900-908 (2012)
   PUBMED   22193545
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Lacroix,M., El Messaoudi,S., Rodier,G., Le Cam,A., Sardet,C. and
            Fabbrizio,E.
  TITLE     The histone-binding protein COPR5 is required for nuclear functions
            of the protein arginine methyltransferase PRMT5
  JOURNAL   EMBO Rep 9 (5), 452-458 (2008)
   PUBMED   18404153
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Douglas,J., Cilliers,D., Coleman,K., Tatton-Brown,K., Barker,K.,
            Bernhard,B., Burn,J., Huson,S., Josifova,D., Lacombe,D., Malik,M.,
            Mansour,S., Reid,E., Cormier-Daire,V., Cole,T. and Rahman,N.
  CONSRTM   Childhood Overgrowth Collaboration
  TITLE     Mutations in RNF135, a gene within the NF1 microdeletion region,
            cause phenotypic abnormalities including overgrowth
  JOURNAL   Nat Genet 39 (8), 963-965 (2007)
   PUBMED   17632510
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Jenne,D.E., Tinschert,S., Stegmann,E., Reimann,H., Nurnberg,P.,
            Horn,D., Naumann,I., Buske,A. and Thiel,G.
  TITLE     A common set of at least 11 functional genes is lost in the
            majority of NF1 patients with gross deletions
  JOURNAL   Genomics 66 (1), 93-97 (2000)
   PUBMED   10843809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM784600.1, AC004253.2, CD557513.1, BE899028.1 and BQ671018.1.
            
            On Aug 18, 2016 this sequence version replaced XP_005258057.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.68211.1,
                                           ERR279842.10113.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..172
                     /product="coordinator of PRMT5 and differentiation
                     stimulator isoform 2"
                     /note="cooperator of PRMT5; coordinator of PRMT5,
                     differentiation stimulator"
                     /calculated_mol_wt=18780
     Region          22..172
                     /region_name="COPR5"
                     /note="Cooperator of PRMT5 family; pfam15340"
                     /db_xref="CDD:434649"
     CDS             1..172
                     /gene="COPRS"
                     /gene_synonym="C17orf79; COPR5; HSA272196; TTP1"
                     /coded_by="NM_001330176.2:143..661"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82100.1"
                     /db_xref="GeneID:55352"
                     /db_xref="HGNC:HGNC:28848"
ORIGIN      
        1 mggdagdrep gpaarslgeg qagfatadhs sqeretekam drlargtqsi pndspargeg
       61 thseeegfam deedsdgeln twelsegtnc ppkeqpgdlf nedwdselka dqgnpydadd
      121 iqesisqelk pwvccapqgd miydpswhhp pplipyyskm vfetgqfdda ed
//
LOCUS       NP_001186780             357 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein mS29 isoform 3 [Homo sapiens].
ACCESSION   NP_001186780
VERSION     NP_001186780.1
DBSOURCE    REFSEQ: accession NM_001199851.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 357)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 357)
  AUTHORS   Smith,T.B., Kopajtich,R., Demain,L.A.M., Rea,A., Thomas,H.B.,
            Schiff,M., Beetz,C., Joss,S., Conway,G.S., Shukla,A., Yeole,M.,
            Radhakrishnan,P., Azzouz,H., Ben Chehida,A., Elmaleh-Berges,M.,
            Glasgow,R.I.C., Thompson,K., Olahova,M., He,L., Jenkinson,E.M.,
            Jahic,A., Belyantseva,I.A., Barzik,M., Urquhart,J.E.,
            O'Sullivan,J., Williams,S.G., Bhaskar,S.S., Carrera,S.,
            Blakes,A.J.M., Banka,S., Yue,W.W., Ellingford,J.M., Houlden,H.,
            Munro,K.J., Friedman,T.B., Taylor,R.W., Prokisch,H., O'Keefe,R.T.
            and Newman,W.G.
  CONSRTM   DDD Study
  TITLE     Bi-allelic variants in DAP3 result in reduced assembly of the
            mitoribosomal small subunit with altered apoptosis and a
            Perrault-syndrome-spectrum phenotype
  JOURNAL   Am J Hum Genet 112 (1), 59-74 (2025)
   PUBMED   39701103
REFERENCE   3  (residues 1 to 357)
  AUTHORS   Tan,S., Zhang,X., Guo,X., Pan,G., Yan,L., Ding,Z., Li,R., Wang,D.,
            Yan,Y., Dong,Z. and Li,T.
  TITLE     DAP3 promotes mitochondrial activity and tumour progression in
            hepatocellular carcinoma by regulating MT-ND5 expression
  JOURNAL   Cell Death Dis 15 (7), 540 (2024)
   PUBMED   39080251
  REMARK    GeneRIF: DAP3 promotes mitochondrial activity and tumour
            progression in hepatocellular carcinoma by regulating MT-ND5
            expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 357)
  AUTHORS   Sui,L., Zeng,J., Zhao,H., Ye,L., Martin,T.A., Sanders,A.J.,
            Ruge,F., Jiang,A., Dou,Q.P., Hargest,R., Song,X. and Jiang,W.G.
  TITLE     Death associated protein-3 (DAP3) and DAP3 binding cell death
            enhancer-1 (DELE1) in human colorectal cancer, and their impacts on
            clinical outcome and chemoresistance
  JOURNAL   Int J Oncol 62 (1) (2023)
   PUBMED   36382667
  REMARK    GeneRIF: Death associated protein3 (DAP3) and DAP3 binding cell
            death enhancer1 (DELE1) in human colorectal cancer, and their
            impacts on clinical outcome and chemoresistance.
REFERENCE   5  (residues 1 to 357)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 357)
  AUTHORS   Han,M.J., Chiu,D.T. and Koc,E.C.
  TITLE     Regulation of mitochondrial ribosomal protein S29 (MRPS29)
            expression by a 5'-upstream open reading frame
  JOURNAL   Mitochondrion 10 (3), 274-283 (2010)
   PUBMED   20079882
REFERENCE   7  (residues 1 to 357)
  AUTHORS   Morgan,C.J., Jacques,C., Savagner,F., Tourmen,Y., Mirebeau,D.P.,
            Malthiery,Y. and Reynier,P.
  TITLE     A conserved N-terminal sequence targets human DAP3 to mitochondria
  JOURNAL   Biochem Biophys Res Commun 280 (1), 177-181 (2001)
   PUBMED   11162496
REFERENCE   8  (residues 1 to 357)
  AUTHORS   Hulkko,S.M., Wakui,H. and Zilliacus,J.
  TITLE     The pro-apoptotic protein death-associated protein 3 (DAP3)
            interacts with the glucocorticoid receptor and affects the receptor
            function
  JOURNAL   Biochem J 349 Pt 3 (Pt 3), 885-893 (2000)
   PUBMED   10903152
REFERENCE   9  (residues 1 to 357)
  AUTHORS   Kissil,J.L. and Kimchi,A.
  TITLE     Assignment of death associated protein 3 (DAP3) to human chromosome
            1q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 252 (1997)
   PUBMED   9284927
REFERENCE   10 (residues 1 to 357)
  AUTHORS   Kissil,J.L., Deiss,L.P., Bayewitch,M., Raveh,T., Khaspekov,G. and
            Kimchi,A.
  TITLE     Isolation of DAP3, a novel mediator of interferon-gamma-induced
            cell death
  JOURNAL   J Biol Chem 270 (46), 27932-27936 (1995)
   PUBMED   7499268
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302281.1, AK298201.1,
            AL162734.15 and BQ183744.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 28S subunit protein that also
            participates in apoptotic pathways which are initiated by tumor
            necrosis factor-alpha, Fas ligand, and gamma interferon. This
            protein potentially binds ATP/GTP and might be a functional partner
            of the mitoribosomal protein S27. Multiple alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. Pseudogenes corresponding to this gene are found on
            chromosomes 1q and 2q. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (5) lacks an in-frame exon in the
            CDS, as compared to variant 2. The resulting isoform (3) lacks an
            internal segment, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.534229.1,
                                           SRR1660805.188667.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..357
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..357
                     /product="small ribosomal subunit protein mS29 isoform 3"
                     /note="mitochondrial 28S ribosomal protein S29; 28S
                     ribosomal protein S29, mitochondrial; ionizing radiation
                     resistance conferring protein; mitochondrial small
                     ribosomal subunit protein mS29"
                     /calculated_mol_wt=40913
     Region          58..352
                     /region_name="DAP3"
                     /note="Mitochondrial ribosomal death-associated protein 3;
                     pfam10236"
                     /db_xref="CDD:431160"
     CDS             1..357
                     /gene="DAP3"
                     /gene_synonym="bMRP-10; DAP-3; MRP-S29; MRPS29; mS29;
                     PRLTS7; S29mt"
                     /coded_by="NM_001199851.1:92..1165"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS55647.1"
                     /db_xref="GeneID:7818"
                     /db_xref="HGNC:HGNC:2673"
                     /db_xref="MIM:602074"
ORIGIN      
        1 mmlkgitrli srihkakhgd qhegqhynis pqdletvfph glpprfvmqv ktfseaclmv
       61 rkpalellhy lkntsfaypa iryllygekg tgktlslchv ihfcakqdwl ilhipdahlw
      121 vkncrdllqs synkqrfdqp leastwlknf kttnerflnq ikvqekyvwn krestekgsp
      181 lgevveqgit rvrnatdavg ivlkelkrqs slgmfhllva vdginalwgr ttlkredksp
      241 iapeelalvh nlrkmmkndw hggaivsals qtgslfkprk aylpqellgk egfdaldpfi
      301 pilvsnynpk efesciqyyl ennwlqheka pteegkkell flsnanpsll erhcayl
//
LOCUS       NP_000278                980 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome biogenesis factor 6 isoform 1 [Homo sapiens].
ACCESSION   NP_000278
VERSION     NP_000278.3
DBSOURCE    REFSEQ: accession NM_000287.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 980)
  AUTHORS   Yang,P., Zeng,C.Z., Tao,X.W., Rong,S.W., Long,Y. and Zeng,L.K.
  TITLE     [Zellweger syndrome caused by PEX6 gene variation in 2 cases and
            literature review]
  JOURNAL   Zhonghua Er Ke Za Zhi 62 (1), 43-48 (2024)
   PUBMED   38154976
  REMARK    GeneRIF: [Zellweger syndrome caused by PEX6 gene variation in 2
            cases and literature review].
            Review article
REFERENCE   2  (residues 1 to 980)
  AUTHORS   Galarreta,C.I., Wong,K., Carmichael,J., Woods,J., Tise,C.G.,
            Niehaus,A.D., Schildt,A.J., Verscaj,C.P. and Cusmano-Ozog,K.P.
  TITLE     A homozygous Gly470Ala variant in PEX6 causes severe Zellweger
            spectrum disorder
  JOURNAL   Am J Med Genet A 191 (8), 2057-2063 (2023)
   PUBMED   37144748
  REMARK    GeneRIF: A homozygous Gly470Ala variant in PEX6 causes severe
            Zellweger spectrum disorder.
REFERENCE   3  (residues 1 to 980)
  AUTHORS   Judy,R.M., Sheedy,C.J. and Gardner,B.M.
  TITLE     Insights into the Structure and Function of the Pex1/Pex6
            AAA-ATPase in Peroxisome Homeostasis
  JOURNAL   Cells 11 (13), 2067 (2022)
   PUBMED   35805150
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 980)
  AUTHORS   Daich Varela,M., Jani,P., Zein,W.M., D'Souza,P., Wolfe,L.,
            Chisholm,J., Zalewski,C., Adams,D., Warner,B.M., Huryn,L.A. and
            Hufnagel,R.B.
  TITLE     The peroxisomal disorder spectrum and Heimler syndrome: Deep
            phenotyping and review of the literature
  JOURNAL   Am J Med Genet C Semin Med Genet 184 (3), 618-630 (2020)
   PUBMED   32866347
  REMARK    GeneRIF: The peroxisomal disorder spectrum and Heimler syndrome:
            Deep phenotyping and review of the literature.
REFERENCE   5  (residues 1 to 980)
  AUTHORS   Tamura,S., Shimozawa,N., Suzuki,Y., Tsukamoto,T., Osumi,T. and
            Fujiki,Y.
  TITLE     A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p
  JOURNAL   Biochem Biophys Res Commun 245 (3), 883-886 (1998)
   PUBMED   9588209
REFERENCE   6  (residues 1 to 980)
  AUTHORS   Fukuda,S., Shimozawa,N., Suzuki,Y., Zhang,Z., Tomatsu,S.,
            Tsukamoto,T., Hashiguchi,N., Osumi,T., Masuno,M., Imaizumi,K.,
            Kuroki,Y., Fujiki,Y., Orii,T. and Kondo,N.
  TITLE     Human peroxisome assembly factor-2 (PAF-2): a gene responsible for
            group C peroxisome biogenesis disorder in humans
  JOURNAL   Am J Hum Genet 59 (6), 1210-1220 (1996)
   PUBMED   8940266
REFERENCE   7  (residues 1 to 980)
  AUTHORS   Yahraus,T., Braverman,N., Dodt,G., Kalish,J.E., Morrell,J.C.,
            Moser,H.W., Valle,D. and Gould,S.J.
  TITLE     The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a
            cytoplasmic ATPase required for stability of the PTS1 receptor
  JOURNAL   EMBO J 15 (12), 2914-2923 (1996)
   PUBMED   8670792
REFERENCE   8  (residues 1 to 980)
  AUTHORS   Li,T., Faridi,R., Newman,W.G. and Friedman,T.B.
  TITLE     Perrault Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25254289
REFERENCE   9  (residues 1 to 980)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 980)
  AUTHORS   Steinberg,S.J., Raymond,G.V., Braverman,N.E. and Moser,A.B.
  TITLE     Zellweger Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA462214.1, BC033487.1,
            BQ773648.1 and AL158815.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 10, 2008 this sequence version replaced NP_000278.2.
            
            Summary: This gene encodes a member of the AAA (ATPases associated
            with diverse cellular activities) family of ATPases. This member is
            a predominantly cytoplasmic protein, which plays a direct role in
            peroxisomal protein import and is required for PTS1 (peroxisomal
            targeting signal 1, a C-terminal tripeptide of the sequence
            ser-lys-leu) receptor activity. Mutations in this gene cause
            peroxisome biogenesis disorders of complementation group 4 and
            complementation group 6. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.253258.1, BC033487.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304611.13/ ENSP00000303511.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..980
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..980
                     /product="peroxisome biogenesis factor 6 isoform 1"
                     /note="peroxisome assembly factor 2; peroxisomal AAA-type
                     ATPase 1; peroxin-6; peroxisomal-type ATPase 1;
                     peroxisomal ATPase PEX6"
                     /calculated_mol_wt=103930
     Site            119
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13608.2)"
     Region          <466..977
                     /region_name="CDC48"
                     /note="AAA family ATPase, CDC48 subfamily; TIGR01243"
                     /db_xref="CDD:273521"
     CDS             1..980
                     /gene="PEX6"
                     /gene_synonym="HMLR2; PAF-2; PAF2; PBD4A; PDB4B; PXAAA1"
                     /coded_by="NM_000287.4:32..2974"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4877.1"
                     /db_xref="GeneID:5190"
                     /db_xref="HGNC:HGNC:8859"
                     /db_xref="MIM:601498"
ORIGIN      
        1 malavlrvle pfptetppla vllppggpwp aaelglvlal rpagespagp allvaalegp
       61 dagteeqgpg ppqllvsral lrllalgsga wvraravrrp palgwallgt slgpglgprv
      121 gpllvrrget lpvpgprvle trpalqgllg pgtrlavtel rgrarlcpes gdssrppppp
      181 vvssfavsgt vrrlqgvlgg tgdslgvsrs clrglglfqg ewvwvaqare ssntsqphla
      241 rvqvleprwd lsdrlgpgsg plgepladgl alvpatlafn lgcdplemge lriqrylegs
      301 iapedkgscs llpgppfare lhieivssph ystngnydgv lyrhfqiprv vqegdvlcvp
      361 tigqveileg speklprwre mffkvkktvg eapdgpasay ladtthtsly mvgstlspvp
      421 wlpseestlw sslsppglea lvselcavlk prlqpggall tgtssvllrg ppgcgkttvv
      481 aaacshlglh llkvpcsslc aessgavetk lqaifsrarr crpavlllta vdllgrdrdg
      541 lgedarvmav lrhlllnedp lnscpplmvv attsraqdlp advqtafphe levpalsegq
      601 rlsilralta hlplgqevnl aqlarrcagf vvgdlyallt hssraactri knsglagglt
      661 eedegelcaa gfpllaedfg qaleqlqtah sqavgapkip svswhdvggl qevkkeilet
      721 iqlplehpel lslglrrsgl llhgppgtgk tllakavate csltflsvkg pelinmyvgq
      781 seenvrevfa raraaapcii ffdeldslap srgrsgdsgg vmdrvvsqll aeldglhstq
      841 dvfvigatnr pdlldpallr pgrfdklvfv ganedrasql rvlsaitrkf klepsvslvn
      901 vldccppqlt gadlyslcsd amtaalkrrv hdleeglepg ssalmltmed llqaaarlqp
      961 svseqellry kriqrkfaac
//
LOCUS       NP_003482                235 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 10 isoform 1 [Homo sapiens].
ACCESSION   NP_003482
VERSION     NP_003482.1
DBSOURCE    REFSEQ: accession NM_003491.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Duong,N.X., Nguyen,T., Le,M.K., Sawada,N., Kira,S., Kondo,T.,
            Inukai,T. and Mitsui,T.
  TITLE     NAA10 gene expression is associated with mesenchymal transition,
            dedifferentiation, and progression of clear cell renal cell
            carcinoma
  JOURNAL   Pathol Res Pract 255, 155191 (2024)
   PUBMED   38340582
  REMARK    GeneRIF: NAA10 gene expression is associated with mesenchymal
            transition, dedifferentiation, and progression of clear cell renal
            cell carcinoma.
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Belbachir,N., Wu,Y., Shen,M., Zhang,S.L., Zhang,J.Z., Liu,C.,
            Knollmann,B.C., Lyon,G.J., Ma,N. and Wu,J.C.
  TITLE     Studying Long QT Syndrome Caused by NAA10 Genetic Variants Using
            Patient-Derived Induced Pluripotent Stem Cells
  JOURNAL   Circulation 148 (20), 1598-1601 (2023)
   PUBMED   37956223
  REMARK    GeneRIF: Studying Long QT Syndrome Caused by NAA10 Genetic Variants
            Using Patient-Derived Induced Pluripotent Stem Cells.
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Le,M.K., Vuong,H.G., Nguyen,T.T.T. and Kondo,T.
  TITLE     NAA10 overexpression dictates distinct epigenetic, genetic, and
            clinicopathological characteristics in adult gliomas
  JOURNAL   J Neuropathol Exp Neurol 82 (7), 650-658 (2023)
   PUBMED   37253389
  REMARK    GeneRIF: NAA10 overexpression dictates distinct epigenetic,
            genetic, and clinicopathological characteristics in adult gliomas.
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Sugiura,N., Adams,S.M. and Corriveau,R.A.
  TITLE     An evolutionarily conserved N-terminal acetyltransferase complex
            associated with neuronal development
  JOURNAL   J Biol Chem 278 (41), 40113-40120 (2003)
   PUBMED   12888564
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Jeong,J.W., Bae,M.K., Ahn,M.Y., Kim,S.H., Sohn,T.K., Bae,M.H.,
            Yoo,M.A., Song,E.J., Lee,K.J. and Kim,K.W.
  TITLE     Regulation and destabilization of HIF-1alpha by ARD1-mediated
            acetylation
  JOURNAL   Cell 111 (5), 709-720 (2002)
   PUBMED   12464182
  REMARK    GeneRIF: ARD1-mediated acetylation regulates and destabilizes HIF-1
            alpha by directly binding to it.
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Sekine,A., Saito,S., Iida,A., Mitsunobu,Y., Higuchi,S., Harigae,S.
            and Nakamura,Y.
  TITLE     Identification of single-nucleotide polymorphisms (SNPs) of human
            N-acetyltransferase genes NAT1, NAT2, AANAT, ARD1 and L1CAM in the
            Japanese population
  JOURNAL   J Hum Genet 46 (6), 314-319 (2001)
   PUBMED   11393533
  REMARK    GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Tribioli,C., Mancini,M., Plassart,E., Bione,S., Rivella,S.,
            Sala,C., Torri,G. and Toniolo,D.
  TITLE     Isolation of new genes in distal Xq28: transcriptional map and
            identification of a human homologue of the ARD1 N-acetyl
            transferase of Saccharomyces cerevisiae
  JOURNAL   Hum Mol Genet 3 (7), 1061-1067 (1994)
   PUBMED   7981673
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Ng,D.
  TITLE     Lenz Microphthalmia Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301694
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CR979270.1, BC000308.2,
            CA313208.1 and U52112.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: N-alpha-acetylation is among the most common
            post-translational protein modifications in eukaryotic cells. This
            process involves the transfer of an acetyl group from
            acetyl-coenzyme A to the alpha-amino group on a nascent polypeptide
            and is essential for normal cell function. This gene encodes an
            N-terminal acetyltransferase that functions as the catalytic
            subunit of the major amino-terminal acetyltransferase A complex.
            Mutations in this gene are the cause of Ogden syndrome. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jan 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.30048.1, ERR279872.1983.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000464845.6/ ENSP00000417763.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..235
                     /product="N-alpha-acetyltransferase 10 isoform 1"
                     /EC_number="2.3.1.255"
                     /note="N-acetyltransferase ARD1, human homolog of;
                     microphthalmia or anophthalmia and associated anomalies;
                     N-terminal acetyltransferase complex ARD1 subunit homolog
                     A; ARD1 homolog A, N-acetyltransferase; natA catalytic
                     subunit Naa10; arrest defective protein 1"
                     /calculated_mol_wt=26327
     Region          1..58
                     /region_name="Interaction with NAA15.
                     /evidence=ECO:0000269|PubMed:15496142"
                     /note="propagated from UniProtKB/Swiss-Prot (P41227.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Region          54..152
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     Site            136
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:27708256; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Region          178..235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P41227.1)"
     Site            182
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P41227.1)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKB.
                     /evidence=ECO:0000269|PubMed:19716809; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P41227.1)"
     CDS             1..235
                     /gene="NAA10"
                     /gene_synonym="ARD1; ARD1A; ARD1P; DXS707; hARD1; LZMS;
                     MAA; MCOPS1; NATD; OGDNS; TE2"
                     /coded_by="NM_003491.4:134..841"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14737.1"
                     /db_xref="GeneID:8260"
                     /db_xref="HGNC:HGNC:18704"
                     /db_xref="MIM:300013"
ORIGIN      
        1 mnirnarped lmnmqhcnll clpenyqmky yfyhglswpq lsyiaedeng kivgyvlakm
       61 eedpddvphg hitslavkrs hrrlglaqkl mdqasramie nfnakyvslh vrksnraalh
      121 lysntlnfqi sevepkyyad gedayamkrd ltqmadelrr hlelkekgrh vvlgaienkv
      181 eskgnsppss geacreekgl aaedsggdsk dlsevsette stdvkdssea sdsas
//
LOCUS       NP_004605                265 aa            linear   PRI 20-NOV-2025
DEFINITION  thymidine kinase 2, mitochondrial isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_004605
VERSION     NP_004605.4
DBSOURCE    REFSEQ: accession NM_004614.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 265)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 265)
  AUTHORS   Aoki,H., Higashi,M., Okita,M., Ando,N., Murayama,S., Ishikawa,K.
            and Yokota,T.
  TITLE     Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n
  JOURNAL   Cerebellum 22 (1), 70-84 (2023)
   PUBMED   35084690
  REMARK    GeneRIF: Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n.
REFERENCE   3  (residues 1 to 265)
  AUTHORS   Dominguez-Gonzalez,C., Hernandez-Voth,A., de Fuenmayor-Fernandez de
            la Hoz,C.P., Guerrero,L.B., Moris,G., Garcia-Garcia,J., Muelas,N.,
            Leon Hernandez,J.C., Rabasa,M., Lora,D., Blazquez,A., Arenas,J. and
            Martin,M.A.
  TITLE     Metrics of progression and prognosis in untreated adults with
            thymidine kinase 2 deficiency: An observational study
  JOURNAL   Neuromuscul Disord 32 (9), 728-735 (2022)
   PUBMED   35907766
  REMARK    GeneRIF: Metrics of progression and prognosis in untreated adults
            with thymidine kinase 2 deficiency: An observational study.
REFERENCE   4  (residues 1 to 265)
  AUTHORS   Wang,L. and Eriksson,S.
  TITLE     Mutational analyses of human thymidine kinase 2 reveal key residues
            in ATP-Mg2+ binding and catalysis
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 41 (3), 264-272 (2022)
   PUBMED   34758700
  REMARK    GeneRIF: Mutational analyses of human thymidine kinase 2 reveal key
            residues in ATP-Mg(2+) binding and catalysis.
REFERENCE   5  (residues 1 to 265)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 265)
  AUTHORS   Kierdaszuk,B., Krawiec,K., Kazimierczuk,Z., Jacobsson,U.,
            Johansson,N.G., Munch-Petersen,B., Eriksson,S. and Shugar,D.
  TITLE     Substrate/inhibitor specificities of human deoxycytidine kinase
            (dCK) and thymidine kinases (TK1 and TK2)
  JOURNAL   Adv Exp Med Biol 431, 623-627 (1998)
   PUBMED   9598140
REFERENCE   7  (residues 1 to 265)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning of the cDNA and chromosome localization of the gene for
            human thymidine kinase 2
  JOURNAL   J Biol Chem 272 (13), 8454-8458 (1997)
   PUBMED   9079672
REFERENCE   8  (residues 1 to 265)
  AUTHORS   Wang,J., El-Hattab,A.W. and Wong,L.J.C.
  TITLE     TK2-Related Mitochondrial DNA Maintenance Defect, Myopathic Form
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23230576
REFERENCE   9  (residues 1 to 265)
  AUTHORS   Jansson,O., Bohman,C., Munch-Petersen,B. and Eriksson,S.
  TITLE     Mammalian thymidine kinase 2. Direct photoaffinity labeling with
            [32P]dTTP of the enzyme from spleen, liver, heart and brain
  JOURNAL   Eur J Biochem 206 (2), 485-490 (1992)
   PUBMED   1597187
REFERENCE   10 (residues 1 to 265)
  AUTHORS   Willecke,K., Teber,T., Kucherlapati,R.S. and Ruddle,F.H.
  TITLE     Human mitochondrial thymidine kinase is coded for by a gene on
            chromosome 16 of the nucleus
  JOURNAL   Somatic Cell Genet 3 (3), 237-245 (1977)
   PUBMED   605384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF521891.1 and AC010542.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 5, 2010 this sequence version replaced NP_004605.3.
            
            Summary: This gene encodes a deoxyribonucleoside kinase that
            specifically phosphorylates thymidine, deoxycytidine, and
            deoxyuridine. The encoded enzyme localizes to the mitochondria and
            is required for mitochondrial DNA synthesis. Mutations in this gene
            are associated with a myopathic form of mitochondrial DNA depletion
            syndrome. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms, some of which lack transit
            peptide, so are not localized to mitochondria. [provided by RefSeq,
            Dec 2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.61244.1,
                                           SRR1660805.256015.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000544898.6/
                                                  ENSP00000440898.2
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..265
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..265
                     /product="thymidine kinase 2, mitochondrial isoform 1
                     precursor"
                     /EC_number="2.7.1.74"
                     /EC_number="2.7.1.21"
                     /note="mt-TK; thymidine kinase 2, mitochondrial;
                     deoxycytidine kinase TK2; 2'-deoxyuridine kinase TK2;
                     mitochondrial thymidine kinase"
                     /calculated_mol_wt=27488
     transit_peptide 1..33
                     /calculated_mol_wt=3535
     Region          20..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00142.4)"
     mat_peptide     34..265
                     /product="thymidine kinase 2, mitochondrial isoform 1"
                     /calculated_mol_wt=27488
     Region          53..265
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            order(61,63..64,99,109..110,143,196,201)
                     /site_type="other"
                     /note="Substrate-binding site [chemical binding]"
                     /db_xref="CDD:238836"
     Site            117
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..265
                     /gene="TK2"
                     /gene_synonym="MTDPS2; MTTK; PEOB3; SCA31; TK2-EXT"
                     /coded_by="NM_004614.5:62..859"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS10805.2"
                     /db_xref="GeneID:7084"
                     /db_xref="HGNC:HGNC:11831"
                     /db_xref="MIM:188250"
ORIGIN      
        1 mllwplrgwa aralrcfgpg srgspasgpg prrvqrrawp pdkeqekekk svicvegnia
       61 sgkttcleff snatdvevlt epvskwrnvr ghnplglmyh dasrwgltlq tyvqltmldr
      121 htrpqvssvr lmersihsar yifvenlyrs gkmpevdyvv lsewfdwilr nmdvsvdliv
      181 ylrtnpetcy qrlkkrcree ekvipleyle aihhlheewl ikgslfpmaa pvlvieadhh
      241 mermlelfeq nrdriltpen rkhcp
//
LOCUS       NP_055411                126 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA12 [Homo sapiens].
ACCESSION   NP_055411
VERSION     NP_055411.1
DBSOURCE    REFSEQ: accession NM_014596.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 126)
  AUTHORS   Ford,B.L., Wei,T., Liu,H., Scull,C.E., Najmi,S.M., Pitts,S.,
            Fan,W., Schneider,D.A. and Laiho,M.
  TITLE     Expression of RNA polymerase I catalytic core is influenced by
            RPA12
  JOURNAL   PLoS One 18 (5), e0285660 (2023)
   PUBMED   37167337
  REMARK    GeneRIF: Expression of RNA polymerase I catalytic core is
            influenced by RPA12.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 126)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 126)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   4  (residues 1 to 126)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 126)
  AUTHORS   Yin,X., Zhang,K., Wang,J., Zhou,X., Zhang,C., Song,X., Wu,Z.,
            Du,J., Chen,Q., Zhang,S. and Deng,W.
  TITLE     RNA polymerase I subunit 12 plays opposite roles in cell
            proliferation and migration
  JOURNAL   Biochem Biophys Res Commun 560, 112-118 (2021)
   PUBMED   33984768
  REMARK    GeneRIF: RNA polymerase I subunit 12 plays opposite roles in cell
            proliferation and migration.
REFERENCE   6  (residues 1 to 126)
  AUTHORS   Hong,L., Zhang,Y., Liu,N., Liu,C., Zhi,M., Pan,Y., Lan,M., Sun,L.
            and Fan,D.
  TITLE     Suppression of the cell proliferation in stomach cancer cells by
            the ZNRD1 gene
  JOURNAL   Biochem Biophys Res Commun 321 (3), 611-616 (2004)
   PUBMED   15358150
  REMARK    GeneRIF: This study clearly demonstrates that ZNRD1 may play an
            important role in the control of human gastric cancer development
            by regulating cell proliferation.
REFERENCE   7  (residues 1 to 126)
  AUTHORS   Shi,Y., Zhang,Y., Zhao,Y., Hong,L., Liu,N., Jin,X., Pan,Y. and
            Fan,D.
  TITLE     Overexpression of ZNRD1 promotes multidrug-resistant phenotype of
            gastric cancer cells through upregulation of P-glycoprotein
  JOURNAL   Cancer Biol Ther 3 (4), 377-381 (2004)
   PUBMED   14726695
  REMARK    GeneRIF: overexpression of ZNRD1 could promote multidrug-resistant
            phenotype of gastric cancer cells through upregulation of
            P-glycoprotein
REFERENCE   8  (residues 1 to 126)
  AUTHORS   Coriton,O., Lepourcelet,M., Hampe,A., Galibert,F. and Mosser,J.
  TITLE     Transcriptional analysis of the 69-kb sequence centromeric to
            HLA-J: a dense and complex structure of five genes
  JOURNAL   Mamm Genome 11 (12), 1127-1131 (2000)
   PUBMED   11130983
REFERENCE   9  (residues 1 to 126)
  AUTHORS   Fan,W., Wang,Z., Kyzysztof,F., Prange,C. and Lennon,G.
  TITLE     A new zinc ribbon gene (ZNRD1) is cloned from the human MHC class I
            region
  JOURNAL   Genomics 63 (1), 139-141 (2000)
   PUBMED   10662553
REFERENCE   10 (residues 1 to 126)
  AUTHORS   Lepourcelet,M., Andrieux,N., Giffon,T., Pichon,L., Hampe,A.,
            Galibert,F. and Mosser,J.
  TITLE     Systematic sequencing of the human HLA-A/HLA-F region:
            establishment of a cosmid contig and identification of a new gene
            cluster within 37 kb of sequence
  JOURNAL   Genomics 37 (3), 316-326 (1996)
   PUBMED   8938444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY071776.1 and AF238321.1.
            
            Summary: This gene encodes a DNA-directed RNA polymerase I subunit.
            The encoded protein contains two potential zinc-binding motifs and
            may play a role in regulation of cell proliferation. The encoded
            protein may be involved in cancer and human immunodeficiency virus
            progression. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (b) differs in the 5' UTR,
            compared to variant a. Variants a, b, c, and d encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.565400.1,
                                           SRR5189661.39900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..126
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p22.1"
     Protein         1..126
                     /product="DNA-directed RNA polymerase I subunit RPA12"
                     /EC_number="2.7.7.6"
                     /note="transcription-associated zinc ribbon protein; RNA
                     polymerase I small specific subunit Rpa12; zinc ribbon
                     domain containing 1; DNA-directed RNA polymerase I subunit
                     H"
                     /calculated_mol_wt=13773
     Region          19..118
                     /region_name="RPB9"
                     /note="DNA-directed RNA polymerase, subunit
                     M/Transcription elongation factor TFIIS [Transcription];
                     COG1594"
                     /db_xref="CDD:441202"
     Region          79..125
                     /region_name="Zn-ribbon_RPA12"
                     /note="C-terminal zinc ribbon domain of RPA12 subunit of
                     RNA polymerase I; cd10507"
                     /db_xref="CDD:259792"
     Site            order(87,90,115,118)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:259792"
     Region          106..107
                     /region_name="Hairpin.
                     /evidence=ECO:0000250|UniProtKB:Q9Y2Y1,
                     ECO:0000269|PubMed:34671025"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P1U0.1)"
     CDS             1..126
                     /gene="POLR1H"
                     /gene_synonym="A12.2; HTEX-6; HTEX6; hZR14; Rpa12;
                     tctex-6; TCTEX6; TEX6; ZNRD1; ZR14"
                     /coded_by="NM_014596.6:145..525"
                     /db_xref="CCDS:CCDS4670.1"
                     /db_xref="GeneID:30834"
                     /db_xref="HGNC:HGNC:13182"
                     /db_xref="MIM:607525"
ORIGIN      
        1 msvmdlantc ssfqsdldfc sdcgsvlplp gaqdtvtcir cgfninvrdf egkvvktsvv
       61 fhqlgtampm sveegpecqg pvvdrrcprc ghegmayhtr qmrsadegqt vfytctnckf
      121 qekeds
//
LOCUS       NP_001334632             317 aa            linear   PRI 20-NOV-2025
DEFINITION  THO complex subunit 6 isoform 3 [Homo sapiens].
ACCESSION   NP_001334632
VERSION     NP_001334632.1
DBSOURCE    REFSEQ: accession NM_001347703.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 317)
  AUTHORS   Ruaud,L., Roux,N., Boutaud,L., Bessieres,B., Ageorges,F.,
            Achaiaa,A., Bole,C., Nitschke,P., Masson,C., Vekemans,M.,
            Verloes,A. and Attie-Bitach,T.
  TITLE     Biallelic THOC6 pathogenic variants: Prenatal phenotype and review
            of the literature
  JOURNAL   Birth Defects Res 114 (10), 499-504 (2022)
   PUBMED   35426486
  REMARK    GeneRIF: Biallelic THOC6 pathogenic variants: Prenatal phenotype
            and review of the literature.
            Review article
REFERENCE   2  (residues 1 to 317)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 317)
  AUTHORS   Amos,J.S., Huang,L., Thevenon,J., Kariminedjad,A., Beaulieu,C.L.,
            Masurel-Paulet,A., Najmabadi,H., Fattahi,Z., Beheshtian,M.,
            Tonekaboni,S.H., Tang,S., Helbig,K.L., Alcaraz,W., Riviere,J.B.,
            Faivre,L., Innes,A.M., Lebel,R.R. and Boycott,K.M.
  CONSRTM   Care4Rare Canada Consortium
  TITLE     Autosomal recessive mutations in THOC6 cause intellectual
            disability: syndrome delineation requiring forward and reverse
            phenotyping
  JOURNAL   Clin Genet 91 (1), 92-99 (2017)
   PUBMED   27102954
  REMARK    GeneRIF: Results indicate three unrelated patients with bi-allelic
            mutations in THOC6 associated with intellectual disability and
            additional clinical features.
REFERENCE   4  (residues 1 to 317)
  AUTHORS   Anazi,S., Alshammari,M., Moneis,D., Abouelhoda,M., Ibrahim,N. and
            Alkuraya,F.S.
  TITLE     Confirming the candidacy of THOC6 in the etiology of intellectual
            disability
  JOURNAL   Am J Med Genet A 170A (5), 1367-1369 (2016)
   PUBMED   26739162
  REMARK    GeneRIF: In addition to confirming the morbid nature of THOC6 by
            providing an independent homozygous apparently loss of function
            allele in a patient with a compatible phenotype, our data also
            expand THOC6-related phenotype to include previously unreported
            imperforate anus and undescended testicles.
REFERENCE   5  (residues 1 to 317)
  AUTHORS   Beaulieu,C.L., Huang,L., Innes,A.M., Akimenko,M.A.,
            Puffenberger,E.G., Schwartz,C., Jerry,P., Ober,C., Hegele,R.A.,
            McLeod,D.R., Schwartzentruber,J., Majewski,J., Bulman,D.E.,
            Parboosingh,J.S. and Boycott,K.M.
  CONSRTM   FORGE Canada Consortium
  TITLE     Intellectual disability associated with a homozygous missense
            mutation in THOC6
  JOURNAL   Orphanet J Rare Dis 8, 62 (2013)
   PUBMED   23621916
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 317)
  AUTHORS   Boyne,J.R., Colgan,K.J. and Whitehouse,A.
  TITLE     Recruitment of the complete hTREX complex is required for Kaposi's
            sarcoma-associated herpesvirus intronless mRNA nuclear export and
            virus replication
  JOURNAL   PLoS Pathog 4 (10), e1000194 (2008)
   PUBMED   18974867
REFERENCE   7  (residues 1 to 317)
  AUTHORS   Cheng,H., Dufu,K., Lee,C.S., Hsu,J.L., Dias,A. and Reed,R.
  TITLE     Human mRNA export machinery recruited to the 5' end of mRNA
  JOURNAL   Cell 127 (7), 1389-1400 (2006)
   PUBMED   17190602
REFERENCE   8  (residues 1 to 317)
  AUTHORS   Masuda,S., Das,R., Cheng,H., Hurt,E., Dorman,N. and Reed,R.
  TITLE     Recruitment of the human TREX complex to mRNA during splicing
  JOURNAL   Genes Dev 19 (13), 1512-1517 (2005)
   PUBMED   15998806
REFERENCE   9  (residues 1 to 317)
  AUTHORS   Guo,S., Hakimi,M.A., Baillat,D., Chen,X., Farber,M.J.,
            Klein-Szanto,A.J., Cooch,N.S., Godwin,A.K. and Shiekhattar,R.
  TITLE     Linking transcriptional elongation and messenger RNA export to
            metastatic breast cancers
  JOURNAL   Cancer Res 65 (8), 3011-3016 (2005)
   PUBMED   15833825
REFERENCE   10 (residues 1 to 317)
  AUTHORS   Lemire,G., Innes,A.M. and Boycott,K.M.
  TITLE     THOC6 Intellectual Disability Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32790266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX425088.2, BC003118.1 and
            BM457458.1.
            
            Summary: This gene encodes a subunit of the multi-protein THO
            complex, which is involved in coordination between transcription
            and mRNA processing. The THO complex is a component of the TREX
            (transcription/export) complex, which is involved in transcription
            and export of mRNAs. A missense mutation in this gene is associated
            with a neurodevelopmental disorder called Beaulieu-Boycott-Innes
            syndrome. [provided by RefSeq, Dec 2016].
            
            Transcript Variant: This variant (3) differs in the 5' structure,
            resulting in the use of a downstream start codon compared to
            variant 1. The encoded isoform (3) has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..317
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..317
                     /product="THO complex subunit 6 isoform 3"
                     /note="WD repeat domain 58; functional
                     spliceosome-associated protein 35; THO complex subunit 6
                     homolog; WD repeat-containing protein 58; THO complex 6"
                     /calculated_mol_wt=34718
     Region          <7..263
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          55..91
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          106..141
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          147..186
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          233..261
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..317
                     /gene="THOC6"
                     /gene_synonym="fSAP35; MMRFCGU; WDR58"
                     /coded_by="NM_001347703.2:255..1208"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS86500.1"
                     /db_xref="GeneID:79228"
                     /db_xref="HGNC:HGNC:28369"
                     /db_xref="MIM:615403"
ORIGIN      
        1 mtifsqsvsp cgkflaagnn ygqiaifsls salsseakee skkpvvtfqa hdgpvysmvs
       61 tdrhllsagd gevkawlwae mlkkgckelw rrqppyrtsl evpeinalll vpkenslila
      121 ggdcqlhtmd letgtftrvl rghtdyihcl alrerspevl sggedgavrl wdlrtakevq
      181 tievykheec srphngrwig clatdsdwmv cgggpaltlw hlrsstptti fpirapqkhv
      241 tfyqdlilsa gqgrcvnqwq lsgelkaqvp gsspgllsls lnqqpaapec kvltaagnsc
      301 rvdvftnlgy rafslsf
//
LOCUS       NP_714912                381 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-12 receptor subunit beta-1 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_714912
VERSION     NP_714912.1
DBSOURCE    REFSEQ: accession NM_153701.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Huang,J., He,Q., Huang,L., Liu,L., Yang,P. and Chen,M.
  TITLE     Discovering the link between IL12RB1 gene polymorphisms and
            tuberculosis susceptibility: a comprehensive meta-analysis
  JOURNAL   Front Public Health 12, 1249880 (2024)
   PUBMED   38317798
  REMARK    GeneRIF: Discovering the link between IL12RB1 gene polymorphisms
            and tuberculosis susceptibility: a comprehensive meta-analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Rosas Mejia,O., Claeys,T.A., Williams,A., Zafar,A. and
            Robinson,R.T.
  TITLE     IL12RB1 allele bias in human TH cells is regulated by functional
            SNPs in its 3'UTR
  JOURNAL   Cytokine 158, 155993 (2022)
   PUBMED   36007427
  REMARK    GeneRIF: IL12RB1 allele bias in human TH cells is regulated by
            functional SNPs in its 3'UTR.
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Khattak,F.A., Akbar,N.U., Riaz,M., Hussain,M., Rehman,K., Khan,S.N.
            and Khan,T.A.
  TITLE     Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis
  JOURNAL   Int J Infect Dis 112, 338-345 (2021)
   PUBMED   34438084
  REMARK    GeneRIF: Novel IL-12Rbeta1 deficiency-mediates recurrent cutaneous
            leishmaniasis.
REFERENCE   5  (residues 1 to 381)
  AUTHORS   Yamamoto,K., Kobayashi,H., Miura,O., Hirosawa,S. and Miyasaka,N.
  TITLE     Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1
            and beta 2 chains, to human chromosome 19 band p13.1 and chromosome
            1 band p31.2, respectively, by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 257-258 (1997)
   PUBMED   9284929
REFERENCE   6  (residues 1 to 381)
  AUTHORS   Bacon,C.M., Petricoin,E.F. 3rd, Ortaldo,J.R., Rees,R.C.,
            Larner,A.C., Johnston,J.A. and O'Shea,J.J.
  TITLE     Interleukin 12 induces tyrosine phosphorylation and activation of
            STAT4 in human lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7307-7311 (1995)
   PUBMED   7638186
REFERENCE   7  (residues 1 to 381)
  AUTHORS   Bacon,C.M., McVicar,D.W., Ortaldo,J.R., Rees,R.C., O'Shea,J.J. and
            Johnston,J.A.
  TITLE     Interleukin 12 (IL-12) induces tyrosine phosphorylation of JAK2 and
            TYK2: differential use of Janus family tyrosine kinases by IL-2 and
            IL-12
  JOURNAL   J Exp Med 181 (1), 399-404 (1995)
   PUBMED   7528775
REFERENCE   8  (residues 1 to 381)
  AUTHORS   Ling,P., Gately,M.K., Gubler,U., Stern,A.S., Lin,P., Hollfelder,K.,
            Su,C., Pan,Y.C. and Hakimi,J.
  TITLE     Human IL-12 p40 homodimer binds to the IL-12 receptor but does not
            mediate biologic activity
  JOURNAL   J Immunol 154 (1), 116-127 (1995)
   PUBMED   7527811
REFERENCE   9  (residues 1 to 381)
  AUTHORS   Gillessen,S., Carvajal,D., Ling,P., Podlaski,F.J., Stremlo,D.L.,
            Familletti,P.C., Gubler,U., Presky,D.H., Stern,A.S. and Gately,M.K.
  TITLE     Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12
            antagonist
  JOURNAL   Eur J Immunol 25 (1), 200-206 (1995)
   PUBMED   7843232
REFERENCE   10 (residues 1 to 381)
  AUTHORS   Chua,A.O., Chizzonite,R., Desai,B.B., Truitt,T.P., Nunes,P.,
            Minetti,L.J., Warrier,R.R., Presky,D.H., Levine,J.F., Gately,M.K.
            et al.
  TITLE     Expression cloning of a human IL-12 receptor component. A new
            member of the cytokine receptor superfamily with strong homology to
            gp130
  JOURNAL   J Immunol 153 (1), 128-136 (1994)
   PUBMED   7911493
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA008204.1, BC029121.1 and
            AC020904.7.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            protein that belongs to the hemopoietin receptor superfamily. This
            protein binds to interleukine 12 (IL12) with a low affinity, and is
            thought to be a part of IL12 receptor complex. This protein forms a
            disulfide-linked oligomer, which is required for its IL12 binding
            activity. The coexpression of this and IL12RB2 proteins was shown
            to lead to the formation of high-affinity IL12 binding sites and
            reconstitution of IL12 dependent signaling. Mutations in this gene
            impair the development of interleukin-17-producing T lymphocytes
            and result in increased susceptibility to mycobacterial and
            Salmonella infections. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (2) represents the use of an
            alternate promoter, differs in the 5' UTR and has a different 3'
            structure which results in a translational frameshift and an early
            stop codon compared to variant 4. The encoded isoform (2) has a
            shorter N-terminus and a distinct C-terminus compared to isoform 4.
            
            Sequence Note: The 5' UTR was inferred from partial sequence data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029121.1, AK225919.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..381
                     /product="interleukin-12 receptor subunit beta-1 isoform 2
                     precursor"
                     /note="IL-12 receptor beta component; interleukin-12
                     receptor beta-1 chain; IL-12R subunit beta-1; IL-12
                     receptor subunit beta-1; cluster of differentiation 212;
                     interleukin 12 receptor, beta 1"
                     /calculated_mol_wt=39783
     sig_peptide     1..23
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
                     /calculated_mol_wt=2601
     mat_peptide     24..381
                     /product="interleukin-12 receptor subunit beta-1 isoform
                     2"
                     /calculated_mol_wt=39783
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     Region          222..226
                     /region_name="WSXWS motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P42701.1)"
     Site            329
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P42701.1)"
     CDS             1..381
                     /gene="IL12RB1"
                     /gene_synonym="CD212; IL-12R-BETA1; IL12RB; IMD30"
                     /coded_by="NM_153701.3:112..1257"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS32957.1"
                     /db_xref="GeneID:3594"
                     /db_xref="HGNC:HGNC:5971"
                     /db_xref="MIM:601604"
ORIGIN      
        1 meplvtwvvp llflfllsrq gaacrtsecc fqdppypdad sgsasgprdl rcyrissdry
       61 ecswqyegpt agvshflrcc lssgrccyfa agsatrlqfs dqagvsvlyt vtlwveswar
      121 nqtekspevt lqlynsvkye pplgdikvsk lagqlrmewe tpdnqvgaev qfrhrtpssp
      181 wklgdcgpqd ddtesclcpl emnvaqefql rrrqlgsqgs swskwsspvc vppenppqpq
      241 vrfsveqlgq dgrrrltlke qptqlelpeg cqglapgtev tyrlqlhmls cpckakatrt
      301 lhlgkmpyls gaaynvavis snqfgpglnq twhipadtht dgmisahcnl rlpdsrdspa
      361 sasrvagitg ichhtrlily f
//
LOCUS       NP_689764                339 aa            linear   PRI 20-NOV-2025
DEFINITION  U11/U12 small nuclear ribonucleoprotein 48 kDa protein [Homo
            sapiens].
ACCESSION   NP_689764
VERSION     NP_689764.3
DBSOURCE    REFSEQ: accession NM_152551.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Tidow,H., Andreeva,A., Rutherford,T.J. and Fersht,A.R.
  TITLE     Solution structure of the U11-48K CHHC zinc-finger domain that
            specifically binds the 5' splice site of U12-type introns
  JOURNAL   Structure 17 (2), 294-302 (2009)
   PUBMED   19217400
  REMARK    GeneRIF: A model in which the U11-48K Zn finger stabilizes U11-5'
            splice site base pairing and thus plays an important role during
            the minor spliceosome assembly.
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Turunen,J.J., Will,C.L., Grote,M., Luhrmann,R. and Frilander,M.J.
  TITLE     The U11-48K protein contacts the 5' splice site of U12-type introns
            and the U11-59K protein
  JOURNAL   Mol Cell Biol 28 (10), 3548-3560 (2008)
   PUBMED   18347052
  REMARK    GeneRIF: RNA interference-induced knockdown of 48K led to reduced
            cell growth and the inhibition of U12-type splicing, as well as the
            activation of cryptic, U2-type splice sites, suggesting that 48K
            plays a critical role in U12-type intron recognition.
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Golas,M.M., Sander,B., Will,C.L., Luhrmann,R. and Stark,H.
  TITLE     Major conformational change in the complex SF3b upon integration
            into the spliceosomal U11/U12 di-snRNP as revealed by electron
            cryomicroscopy
  JOURNAL   Mol Cell 17 (6), 869-883 (2005)
   PUBMED   15780942
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031058.1, AL832462.1, BC062458.1 and AL390026.1.
            
            On Jul 26, 2005 this sequence version replaced NP_689764.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.24205.1,
                                           SRR1803616.153226.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000342415.6/ ENSP00000339834.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..339
                     /product="U11/U12 small nuclear ribonucleoprotein 48 kDa
                     protein"
                     /note="U11/U12 snRNP 48K; small nuclear ribonucleoprotein
                     48kDa (U11/U12); U11/U12-48K; U11/U12 snRNP 48 kDa
                     protein; small nuclear ribonucleoprotein, U11/U12 48KDa
                     subunit; U11-48K"
                     /calculated_mol_wt=39834
     Region          57..79
                     /region_name="zf-U11-48K"
                     /note="U11-48K-like CHHC zinc finger; pfam05253"
                     /db_xref="CDD:461603"
     Region          255..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IEG0.2)"
     CDS             1..339
                     /gene="SNRNP48"
                     /gene_synonym="C6orf151; dJ336K20B.1; dJ512B11.2"
                     /coded_by="NM_152551.4:61..1080"
                     /db_xref="CCDS:CCDS4502.1"
                     /db_xref="GeneID:154007"
                     /db_xref="HGNC:HGNC:21368"
ORIGIN      
        1 megepppvee rrrlqeelne fvesgcrtle evtaslgwdl dsldpgeeea aedevvicpy
       61 dsnhhmpkss lakhmascrl rkmgytkeee demynpeffy envkipsitl nkdsqfqiik
      121 qartavgkds dcynqriyss lpvevplnhk rfvcdltqad rlalydfvve etkkkrsdsq
      181 iiendsdlfv dlaakinqdn srkspksyle ilaevrdykr rrqsyraknv hitkksytev
      241 irdvinvhme elsnhwqeeq ekaeddaekn eerrsasvds rqsggsylda ecsrhrrdrs
      301 rsphkrkrnk dkdkncesrr rkerdgerhh shkrrkqki
//
LOCUS       NP_001357164             259 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFXANK isoform d [Homo sapiens].
ACCESSION   NP_001357164 XP_005260193
VERSION     NP_001357164.1
DBSOURCE    REFSEQ: accession NM_001370235.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002126.1 and AC003110.1.
            
            On May 2, 2019 this sequence version replaced XP_005260193.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.378418.1,
                                           SRR1163657.202753.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..259
                     /product="DNA-binding protein RFXANK isoform d"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=27900
     Region          88..117
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          <93..248
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          93..120
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(122,124,128..129,132..134,136..137,141,144,153,155,
                     157,161..162,165..167,169..170,174,177,186,188,190,
                     194..195,198..200,202..203,207,210)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          122..153
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          122..151
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          155..186
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          155..184
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          188..217
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          188..216
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          221..250
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     CDS             1..259
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_001370235.1:426..1205"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqgsslkhst tltnrqrgne vsalpatlds lsihqlaaqg eldqlkehlr kgdnlvnkpd
      121 ergftpliwa safgeietvr fllewgadph ilakeresal slastggytd ivglllerdv
      181 diniydwngg tpllyavrgn hvkcvealla rgadlttead sgytpmdlav algyrkvqqv
      241 ienhilklfq snlvpadpe
//
LOCUS       NP_001123892            1152 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF complex subunit SMARCC2 isoform c [Homo sapiens].
ACCESSION   NP_001123892
VERSION     NP_001123892.1
DBSOURCE    REFSEQ: accession NM_001130420.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1152)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1152)
  AUTHORS   Bosch,E., Popp,B., Guse,E., Skinner,C., van der Sluijs,P.J.,
            Maystadt,I., Pinto,A.M., Renieri,A., Bruno,L.P., Granata,S.,
            Marcelis,C., Baysal,O., Hartwich,D., Holthofer,L., Isidor,B.,
            Cogne,B., Wieczorek,D., Capra,V., Scala,M., De Marco,P.,
            Ognibene,M., Jamra,R.A., Platzer,K., Carter,L.B., Kuismin,O., van
            Haeringen,A., Maroofian,R., Valenzuela,I., Cusco,I.,
            Martinez-Agosto,J.A., Rabani,A.M., Mefford,H.C., Pereira,E.M.,
            Close,C., Anyane-Yeboa,K., Wagner,M., Hannibal,M.C., Zacher,P.,
            Thiffault,I., Beunders,G., Umair,M., Bhola,P.T., McGinnis,E.,
            Millichap,J., van de Kamp,J.M., Prijoles,E.J., Dobson,A.,
            Shillington,A., Graham,B.H., Garcia,E.J., Galindo,M.K.,
            Ropers,F.G., Nibbeling,E.A.R., Hubbard,G., Karimov,C., Goj,G.,
            Bend,R., Rath,J., Morrow,M.M., Millan,F., Salpietro,V., Torella,A.,
            Nigro,V., Kurki,M., Stevenson,R.E., Santen,G.W.E., Zweier,M.,
            Campeau,P.M., Severino,M., Reis,A., Accogli,A. and Vasileiou,G.
  TITLE     Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals
  JOURNAL   Genet Med 25 (11), 100950 (2023)
   PUBMED   37551667
  REMARK    GeneRIF: Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals.
REFERENCE   3  (residues 1 to 1152)
  AUTHORS   Liu,S., Liu,P., Zhu,C., Yang,R., He,Z., Li,Y., Li,Y., Fei,X.,
            Hou,J., Wang,X. and Pan,Y.
  TITLE     FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination
  JOURNAL   Aging (Albany NY) 15 (12), 5381-5398 (2023)
   PUBMED   37348029
  REMARK    GeneRIF: FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination.
            Erratum:[Aging (Albany NY). 2023 Sep 14;15(17):9230-9232. doi:
            10.18632/aging.205071. PMID: 37708091]
REFERENCE   4  (residues 1 to 1152)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1152)
  AUTHORS   Li,C., Wang,T., Gu,J., Qi,S., Li,J., Chen,L., Wu,H., Shi,L.,
            Song,C., Li,H., Zhu,L., Lu,Y. and Zhou,Q.
  TITLE     SMARCC2 mediates the regulation of DKK1 by the transcription factor
            EGR1 through chromatin remodeling to reduce the proliferative
            capacity of glioblastoma
  JOURNAL   Cell Death Dis 13 (11), 990 (2022)
   PUBMED   36418306
  REMARK    GeneRIF: SMARCC2 mediates the regulation of DKK1 by the
            transcription factor EGR1 through chromatin remodeling to reduce
            the proliferative capacity of glioblastoma.
            Erratum:[Cell Death Dis. 2022 Dec 12;13(12):1033. doi:
            10.1038/s41419-022-05498-x. PMID: 36509739]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1152)
  AUTHORS   Wang,W., Chi,T., Xue,Y., Zhou,S., Kuo,A. and Crabtree,G.R.
  TITLE     Architectural DNA binding by a high-mobility-group/kinesin-like
            subunit in mammalian SWI/SNF-related complexes
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 492-498 (1998)
   PUBMED   9435219
REFERENCE   7  (residues 1 to 1152)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   8  (residues 1 to 1152)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   9  (residues 1 to 1152)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   10 (residues 1 to 1152)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209006.1, CX165574.1 and
            BM875330.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and contains a predicted
            leucine zipper motif typical of many transcription factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (3) contains an alternate in-frame
            exon in the central coding region and contains alternate in-frame
            segment in the 3' coding region, compared to variant 1. The encoded
            isoform (c), contains a novel internal segment, lacks a segment
            near the C-terminus, and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209006.1, SRR11853563.7640.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..1152
                     /product="SWI/SNF complex subunit SMARCC2 isoform c"
                     /note="chromatin remodeling complex BAF170 subunit;
                     SWI3-like protein; SWI/SNF complex 170 kDa subunit;
                     mammalian chromatin remodeling complex BRG1-associated
                     factor 170; SWI/SNF complex subunit SMARCC2; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin subfamily c member 2"
                     /calculated_mol_wt=126794
     Region          4..420
                     /region_name="SWIRM-assoc_2"
                     /note="SWIRM-associated domain at the N-terminal;
                     pfam16496"
                     /db_xref="CDD:465143"
     Region          379..>739
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Region          715..781
                     /region_name="SWIRM-assoc_3"
                     /note="SWIRM-associated domain at the C-terminal;
                     pfam16498"
                     /db_xref="CDD:465145"
     Region          <721..978
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <911..977
                     /region_name="SWIRM-assoc_1"
                     /note="SWIRM-associated region 1; pfam16495"
                     /db_xref="CDD:465142"
     Region          <1006..>1141
                     /region_name="PRK07003"
                     /note="DNA polymerase III subunit gamma/tau"
                     /db_xref="CDD:235906"
     CDS             1..1152
                     /gene="SMARCC2"
                     /gene_synonym="BAF170; CRACC2; CSS8; Rsc8"
                     /coded_by="NM_001130420.3:23..3481"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55835.1"
                     /db_xref="GeneID:6601"
                     /db_xref="HGNC:HGNC:11105"
                     /db_xref="MIM:601734"
ORIGIN      
        1 mavrkkdggp nvkyyeaadt vtqfdnvrlw lgknykkyiq aepptnksls slvvqllqfq
       61 eevfgkhvsn apltklpikc fldfkaggsl chilaaaykf ksdqgwrryd fqnpsrmdrn
      121 vemfmtieks lvqnnclsrp niflcpeiep kllgklkdii krhqgtvted knnashvvyp
      181 vpgnleeeew vrpvmkrdkq vllhwgyypd sydtwipase ieasvedapt pekprkvhak
      241 wildtdtfne wmneedyevn ddknpvsrrk kisaktltde vnspdsdrrd kkggnykkrk
      301 rspspsptpe akkknakkgp stpytkskrg hreeeqedlt kdmdepspvp nveevtlpkt
      361 vntkkdsesa pvkggtmtdl deqedesmet tgkdedenst gnkgeqtknp dlhednvteq
      421 thhiiipsya awfdynsvha ierralpeff ngknksktpe iylayrnfmi dtyrlnpqey
      481 ltstacrrnl agdvcaimrv hafleqwgli nyqvdaesrp tpmgppptsh fhvladtpsg
      541 lvplqpktpq grqvdadtka grkgkelddl vpetakgkpe lqtsasqqml nfpdkgkekp
      601 tdmqnfglrt dmytkknvps kskaaasatr ewteqetlll lealemykdd wnkvsehvgs
      661 rtqdecilhf lrlpiedpyl edseaslgpl ayqpipfsqs gnpvmstvaf lasvvdprva
      721 saaaksalee fskmkeevpt alveahvrkv eeaakvtgka dpafglessg iagttsdepe
      781 rieesgndea rvegqatdek kepkepregg gaieeeakek tseapkkdee kgkegdseke
      841 seksdgdpiv dpekekepke gqeevlkevv esegerktkv erdigegnls taaaaalaaa
      901 avkakhlaav eerkikslva llvetqmkkl eiklrhfeel etimdrerea leyqrqqlla
      961 drqafhmeql kyaemrarqq hfqqmhqqqq qpppalppgs qpipptgaag ppavhglava
     1021 pasvvpapag sgappgslgp seqigqagst agpqqqqpag apqpgavppg vpppgphgps
     1081 pfpnqqtpps mmpgavpgsg hpgvaaqspa ivaavqgnll psasplpdpg tplppdptap
     1141 spgtvtpvpp pq
//
LOCUS       NP_001147107             121 aa            linear   PRI 20-NOV-2025
DEFINITION  short coiled-coil protein isoform 5 [Homo sapiens].
ACCESSION   NP_001147107
VERSION     NP_001147107.1
DBSOURCE    REFSEQ: accession NM_001153635.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Wirth,M., Mouilleron,S., Zhang,W., Sjottem,E., Princely Abudu,Y.,
            Jain,A., Lauritz Olsvik,H., Bruun,J.A., Razi,M., Jefferies,H.B.J.,
            Lee,R., Joshi,D., O'Reilly,N., Johansen,T. and Tooze,S.A.
  TITLE     Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding
            Affinity and Specificity
  JOURNAL   J Mol Biol 433 (13), 166987 (2021)
   PUBMED   33845085
  REMARK    GeneRIF: Phosphorylation of the LIR Domain of SCOC Modulates ATG8
            Binding Affinity and Specificity.
            Erratum:[J Mol Biol. 2021 Jul 23;433(15):167049. doi:
            10.1016/j.jmb.2021.167049. PMID: 34052024]
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Stringer,S., Minica,C.C., Verweij,K.J., Mbarek,H., Bernard,M.,
            Derringer,J., van Eijk,K.R., Isen,J.D., Loukola,A.,
            Maciejewski,D.F., Mihailov,E., van der Most,P.J., Sanchez-Mora,C.,
            Roos,L., Sherva,R., Walters,R., Ware,J.J., Abdellaoui,A.,
            Bigdeli,T.B., Branje,S.J., Brown,S.A., Bruinenberg,M., Casas,M.,
            Esko,T., Garcia-Martinez,I., Gordon,S.D., Harris,J.M.,
            Hartman,C.A., Henders,A.K., Heath,A.C., Hickie,I.B., Hickman,M.,
            Hopfer,C.J., Hottenga,J.J., Huizink,A.C., Irons,D.E., Kahn,R.S.,
            Korhonen,T., Kranzler,H.R., Krauter,K., van Lier,P.A., Lubke,G.H.,
            Madden,P.A., Magi,R., McGue,M.K., Medland,S.E., Meeus,W.H.,
            Miller,M.B., Montgomery,G.W., Nivard,M.G., Nolte,I.M.,
            Oldehinkel,A.J., Pausova,Z., Qaiser,B., Quaye,L.,
            Ramos-Quiroga,J.A., Richarte,V., Rose,R.J., Shin,J.,
            Stallings,M.C., Stiby,A.I., Wall,T.L., Wright,M.J., Koot,H.M.,
            Paus,T., Hewitt,J.K., Ribases,M., Kaprio,J., Boks,M.P., Snieder,H.,
            Spector,T., Munafo,M.R., Metspalu,A., Gelernter,J., Boomsma,D.I.,
            Iacono,W.G., Martin,N.G., Gillespie,N.A., Derks,E.M. and Vink,J.M.
  TITLE     Genome-wide association study of lifetime cannabis use based on a
            large meta-analytic sample of 32 330 subjects from the
            International Cannabis Consortium
  JOURNAL   Transl Psychiatry 6 (3), e769 (2016)
   PUBMED   27023175
  REMARK    GeneRIF: SCOC SNPs were associated with lifetime cannabis use, but
            the association did not reach genome-wide significance.
            [Meta-Analysis]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Alborghetti,M.R., Furlan Ada,S., da Silva,J.C., Sforca,M.L.,
            Honorato,R.V., Granato,D.C., dos Santos Migueleti,D.L., Neves,J.L.,
            de Oliveira,P.S., Paes-Leme,A.F., Zeri,A.C., de Torriani,I.C. and
            Kobarg,J.
  TITLE     Structural analysis of intermolecular interactions in the kinesin
            adaptor complex fasciculation and elongation protein zeta 1/ short
            coiled-coil protein (FEZ1/SCOCO)
  JOURNAL   PLoS One 8 (10), e76602 (2013)
   PUBMED   24116125
  REMARK    GeneRIF: Studies indicate that FEZ1 (fasciculation and elongation
            protein zeta 1), SCOCO (short coiled-coil protein) and kinesins
            (kinesin heavy chain) are involved in biological transport process.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Behrens,C., Binotti,B., Schmidt,C., Robinson,C.V., Chua,J.J. and
            Kuhnel,K.
  TITLE     Crystal structure of the human short coiled coil protein and
            insights into SCOC-FEZ1 complex formation
  JOURNAL   PLoS One 8 (10), e76355 (2013)
   PUBMED   24098481
  REMARK    GeneRIF: SCOC forms a stable homogeneous complex with the coiled
            coil domain of FEZ1. SCOC dimerization and the SCOC surface residue
            R117 are important for this interaction.
            Erratum:[PLoS One. 2013;8(10).
            doi:10.1371/annotation/cb60d973-58aa-45e0-bbb3-1c7f5a42a8d2]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 121)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
  REMARK    GeneRIF: The identification of SCOC and WAC as novel regulatory
            proteins with diverse functions in autophagy contributes towards a
            fuller understanding of autophagosome formation.
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Van Valkenburgh,H., Shern,J.F., Sharer,J.D., Zhu,X. and Kahn,R.A.
  TITLE     ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
            specific and shared effectors: characterizing ARL1-binding proteins
  JOURNAL   J Biol Chem 276 (25), 22826-22837 (2001)
   PUBMED   11303027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB204055.1, BC062684.1,
            BG151522.1 and AA213765.1.
            
            Summary: This gene encodes a short coiled-coiled domain-containing
            protein that localizes to the Golgi apparatus. The encoded protein
            interacts with ADP-ribosylation factor-like proteins. Pseudogenes
            of this gene are found on chromosomes 1 and 14. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (7) differs in the 5' UTR, has
            multiple differences in the coding region, and initiates
            translation at an alternate start codon, compared to variant 1. The
            encoded isoform (5) has a distinct N-terminus and is shorter than
            isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC062684.1, BG538732.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..121
                     /product="short coiled-coil protein isoform 5"
                     /calculated_mol_wt=13726
     Region          42..112
                     /region_name="DUF2205"
                     /note="Short coiled-coil protein; pfam10224"
                     /db_xref="CDD:431150"
     CDS             1..121
                     /gene="SCOC"
                     /gene_synonym="HRIHFB2072; SCOCO; UNC-69"
                     /coded_by="NM_001153635.1:46..411"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:60592"
                     /db_xref="HGNC:HGNC:20335"
ORIGIN      
        1 mdgsrkeeee dstftnisla ddidhssril yprpksllpk mmnadmdvda enqveleekt
       61 rlinqvlelq htledlsarv davkeenlkl ksenqvlgqy ienlmsassv fqttdtkskr
      121 k
//
LOCUS       NP_001340524             468 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform h [Homo sapiens].
ACCESSION   NP_001340524 XP_005267996
VERSION     NP_001340524.1
DBSOURCE    REFSEQ: accession NM_001353595.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 468)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 468)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 468)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 468)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 468)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 468)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 468)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 468)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 468)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 468)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_005267996.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (10), as well as variant 11,
            encodes isoform h.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.225668.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..468
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..468
                     /product="lysosomal cobalamin transporter ABCD4 isoform h"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=51813
     Region          <53..465
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     CDS             1..468
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353595.2:432..1838"
                     /note="isoform h is encoded by transcript variant 10"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mtsitrtsas artwsdsags saawpassss prspssttlt saskgwlgpv sifgyfilgt
       61 vvnktlmgpi vmklvhqekl egdfrfkhmq irvnaepaaf yraghvehmr tdrrlqrllq
      121 tqrelmskel wlyigintfd ylgsilsyvv iaipifsgvy gdlspaelst lvsknafvci
      181 yliscftqli dlsttlsdva gythrigqlr etlldmslks qdceilgese wgldtppgwp
      241 aaepadtafl lervsisaps sdkplikdls lkisegqsll itgntgtgkt sllrvlgglw
      301 tstrgsvqml tdfgphgvlf lpqkpfftdg tlreqviypl kevypdsgsa dderilrfle
      361 laglsnlvar tegldqqvdw nwydvlspge mqrlsfarlf ylqpkyavld eatsalteev
      421 eselyrigqq lgmtfisvgh rqslekfhsl vlklcgggrw elmrikve
//
LOCUS       NP_003599                337 aa            linear   PRI 20-NOV-2025
DEFINITION  G-protein coupled receptor 65 [Homo sapiens].
ACCESSION   NP_003599
VERSION     NP_003599.2
DBSOURCE    REFSEQ: accession NM_003608.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Yue,X., Peng,L., Liu,S., Zhang,B., Zhang,X., Chang,H., Pei,Y.,
            Li,X., Liu,J., Shui,W., Wu,L., Xu,H., Liu,Z.J. and Hua,T.
  TITLE     Structural basis of stepwise proton sensing-mediated GPCR
            activation
  JOURNAL   Cell Res 35 (6), 423-436 (2025)
   PUBMED   40211064
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Yang,Z., Ping,Y.Q., Wang,M.W., Zhang,C., Zhou,S.H., Xi,Y.T.,
            Zhu,K.K., Ding,W., Zhang,Q.Y., Song,Z.C., Zhao,R.J., He,Z.L.,
            Wang,M.X., Qi,L., Ullmann,C., Ricken,A., Schoneberg,T., Gan,Z.J.,
            Yu,X., Xiao,P., Yi,F., Liebscher,I. and Sun,J.P.
  TITLE     Identification, structure, and agonist design of an androgen
            membrane receptor
  JOURNAL   Cell 188 (6), 1589-1604 (2025)
   PUBMED   39884271
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Howard,M.K., Hoppe,N., Huang,X.P., Mitrovic,D., Billesbolle,C.B.,
            Macdonald,C.B., Mehrotra,E., Rockefeller Grimes,P., Trinidad,D.D.,
            Delemotte,L., English,J.G., Coyote-Maestas,W. and Manglik,A.
  TITLE     Molecular basis of proton sensing by G protein-coupled receptors
  JOURNAL   Cell 188 (3), 671-687 (2025)
   PUBMED   39753132
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Caratis,F., Opielka,M., Hausmann,M., Velasco-Estevez,M., Rojek,B.,
            de Valliere,C., Seuwen,K., Rogler,G., Karaszewski,B. and
            Rutkowska,A.
  TITLE     The proton-sensing receptors TDAG8 and GPR4 are differentially
            expressed in human and mouse oligodendrocytes: Exploring their role
            in neuroinflammation and multiple sclerosis
  JOURNAL   PLoS One 19 (3), e0283060 (2024)
   PUBMED   38527054
  REMARK    GeneRIF: The proton-sensing receptors TDAG8 and GPR4 are
            differentially expressed in human and mouse oligodendrocytes:
            Exploring their role in neuroinflammation and multiple sclerosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Zhang,K., Zhang,M.X., Meng,X.X., Zhu,J., Wang,J.J., He,Y.F.,
            Li,Y.H., Zhao,S.C., Shi,Z.M., Zheng,L.N., Han,T. and Hong,W.
  TITLE     Targeting GPR65 alleviates hepatic inflammation and fibrosis by
            suppressing the JNK and NF-kappaB pathways
  JOURNAL   Mil Med Res 10 (1), 56 (2023)
   PUBMED   38001521
  REMARK    GeneRIF: Targeting GPR65 alleviates hepatic inflammation and
            fibrosis by suppressing the JNK and NF-kappaB pathways.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Ishii,S., Kihara,Y. and Shimizu,T.
  TITLE     Identification of T cell death-associated gene 8 (TDAG8) as a novel
            acid sensing G-protein-coupled receptor
  JOURNAL   J Biol Chem 280 (10), 9083-9087 (2005)
   PUBMED   15618224
  REMARK    GeneRIF: TDAG8 may play biological roles in immune response and
            cellular transformation under conditions accompanying tissue
            acidosis.
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Wang,J.Q., Kon,J., Mogi,C., Tobo,M., Damirin,A., Sato,K.,
            Komachi,M., Malchinkhuu,E., Murata,N., Kimura,T., Kuwabara,A.,
            Wakamatsu,K., Koizumi,H., Uede,T., Tsujimoto,G., Kurose,H.,
            Sato,T., Harada,A., Misawa,N., Tomura,H. and Okajima,F.
  TITLE     TDAG8 is a proton-sensing and psychosine-sensitive
            G-protein-coupled receptor
  JOURNAL   J Biol Chem 279 (44), 45626-45633 (2004)
   PUBMED   15326175
  REMARK    GeneRIF: TDAG8 is one of the proton-sensing GPCRs coupling to
            adenylyl cyclase and psychosine, and its related lysosphingolipids
            behave as if they were antagonists against protein-sensing
            receptors, including TDAG8, GPR4, and OGR1.
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Sin,W.C., Zhang,Y., Zhong,W., Adhikarakunnathu,S., Powers,S.,
            Hoey,T., An,S. and Yang,J.
  TITLE     G protein-coupled receptors GPR4 and TDAG8 are oncogenic and
            overexpressed in human cancers
  JOURNAL   Oncogene 23 (37), 6299-6303 (2004)
   PUBMED   15221007
  REMARK    GeneRIF: GPR4 and TDAG8 overexpression in human tumors plays a role
            in driving or maintaining tumor formation
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Im,D.S., Heise,C.E., Nguyen,T., O'Dowd,B.F. and Lynch,K.R.
  TITLE     Identification of a molecular target of psychosine and its role in
            globoid cell formation
  JOURNAL   J Cell Biol 153 (2), 429-434 (2001)
   PUBMED   11309421
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Kyaw,H., Zeng,Z., Su,K., Fan,P., Shell,B.K., Carter,K.C. and Li,Y.
  TITLE     Cloning, characterization, and mapping of human homolog of mouse
            T-cell death-associated gene
  JOURNAL   DNA Cell Biol 17 (6), 493-500 (1998)
   PUBMED   9655242
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL157955.5.
            
            On Aug 16, 2003 this sequence version replaced NP_003599.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA950973.1, SRR1803615.13159.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000267549.5/ ENSP00000267549.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..337
                     /product="G-protein coupled receptor 65"
                     /note="psychosine receptor; T-cell death-associated gene 8
                     protein"
                     /calculated_mol_wt=39202
     Site            2
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            6..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            10
                     /site_type="other"
                     /note="Proton sensing.
                     /evidence=ECO:0000305|PubMed:37722051; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            14
                     /site_type="other"
                     /note="Proton sensing.
                     /evidence=ECO:0000305|PubMed:37722051; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          15..301
                     /region_name="7tmA_GPR65_TDAG8"
                     /note="proton-sensing G protein-coupled receptor 65,
                     member of the class A family of seven-transmembrane G
                     protein-coupled receptors; cd15365"
                     /db_xref="CDD:320487"
     Region          15..42
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:320487"
     Site            47..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          49..74
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320487"
     Site            order(70,73..74,87..92,94..95,98,143,145..149,180,
                     183..185,187..189,191..192,239,242..243,245..246,249,
                     268..269,271..273,276,279..280)
                     /site_type="other"
                     /note="putative ligand binding pocket [chemical binding]"
                     /db_xref="CDD:320487"
     Site            79
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            83..118
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          87..117
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320487"
     Site            127..153
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          129..151
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320487"
     Site            142
                     /site_type="other"
                     /note="Required for activation.
                     /evidence=ECO:0000269|PubMed:39753132; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          154..174
                     /region_name="Extracellular loop 2 (ECL2).
                     /evidence=ECO:0000269|PubMed:39753132"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            175..212
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          180..209
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320487"
     Site            217..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          219..249
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320487"
     Site            243
                     /site_type="other"
                     /note="Proton sensing.
                     /evidence=ECO:0000305|PubMed:37722051; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Site            265..293
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL9.1)"
     Region          269..294
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320487"
     CDS             1..337
                     /gene="GPR65"
                     /gene_synonym="hTDAG8; TDAG8"
                     /coded_by="NM_003608.4:548..1561"
                     /db_xref="CCDS:CCDS9879.1"
                     /db_xref="GeneID:8477"
                     /db_xref="HGNC:HGNC:4517"
                     /db_xref="MIM:604620"
ORIGIN      
        1 mnstcieeqh dldhylfpiv yifviivsip anigslcvsf lqakkeselg iylfslslsd
       61 llyaltlplw idytwnkdnw tfspalckgs aflmymnfys stafltciav drylavvypl
      121 kffflrtrrf almvslsiwi letifnavml wedetvveyc daeksnftlc ydkyplekwq
      181 inlnlfrtct gyaiplvtil icnrkvyqav rhnkatenke kkriikllvs itvtfvlcft
      241 pfhvmllirc ilehavnfed hsnsgkrtyt myritvalts lncvadpily cfvtetgryd
      301 mwnilkfctg rcntsqrqrk rilsvstkdt melevle
//
LOCUS       NP_874369                546 aa            linear   PRI 20-NOV-2025
DEFINITION  histone acetyltransferase KAT5 isoform 1 [Homo sapiens].
ACCESSION   NP_874369
VERSION     NP_874369.1
DBSOURCE    REFSEQ: accession NM_182710.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 546)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 546)
  AUTHORS   Wang,Y., Li,M., Chen,Y., Jiang,Y., Zhang,Z., Yan,Z., Liu,X. and
            Wu,C.
  TITLE     SPIN1 facilitates chemoresistance and HR repair by promoting Tip60
            binding to H3K9me3
  JOURNAL   EMBO Rep 25 (9), 3970-3989 (2024)
   PUBMED   39090319
  REMARK    GeneRIF: SPIN1 facilitates chemoresistance and HR repair by
            promoting Tip60 binding to H3K9me3.
REFERENCE   3  (residues 1 to 546)
  AUTHORS   Sun,M., Yang,B., Xin,G., Wang,Y., Luo,J., Jiang,Q. and Zhang,C.
  TITLE     TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation
  JOURNAL   Sci China Life Sci 67 (9), 1957-1969 (2024)
   PUBMED   38763998
  REMARK    GeneRIF: TIP60 acetylation of Bub1 regulates centromeric H2AT120
            phosphorylation for faithful chromosome segregation.
REFERENCE   4  (residues 1 to 546)
  AUTHORS   Chen,H., Li,Y., Li,H., Chen,X., Fu,H., Mao,D., Chen,W., Lan,L.,
            Wang,C., Hu,K., Li,J., Zhu,C., Evans,I., Cheung,E., Lu,D., He,Y.,
            Behrens,A., Yin,D. and Zhang,C.
  TITLE     NBS1 lactylation is required for efficient DNA repair and
            chemotherapy resistance
  JOURNAL   Nature 631 (8021), 663-669 (2024)
   PUBMED   38961290
REFERENCE   5  (residues 1 to 546)
  AUTHORS   Xuan,F., Xuan,H., Huang,M., He,W., Xu,H., Shi,X. and Wen,H.
  TITLE     The Tudor-knot Domain of KAT5 Regulates Nucleosomal Substrate
            Acetylation
  JOURNAL   J Mol Biol 436 (7), 168414 (2024)
   PUBMED   38141874
  REMARK    GeneRIF: The Tudor-knot Domain of KAT5 Regulates Nucleosomal
            Substrate Acetylation.
REFERENCE   6  (residues 1 to 546)
  AUTHORS   Brady,M.E., Ozanne,D.M., Gaughan,L., Waite,I., Cook,S., Neal,D.E.
            and Robson,C.N.
  TITLE     Tip60 is a nuclear hormone receptor coactivator
  JOURNAL   J Biol Chem 274 (25), 17599-17604 (1999)
   PUBMED   10364196
REFERENCE   7  (residues 1 to 546)
  AUTHORS   Dechend,R., Hirano,F., Lehmann,K., Heissmeyer,V., Ansieau,S.,
            Wulczyn,F.G., Scheidereit,C. and Leutz,A.
  TITLE     The Bcl-3 oncoprotein acts as a bridging factor between
            NF-kappaB/Rel and nuclear co-regulators
  JOURNAL   Oncogene 18 (22), 3316-3323 (1999)
   PUBMED   10362352
REFERENCE   8  (residues 1 to 546)
  AUTHORS   Kimura,A. and Horikoshi,M.
  TITLE     Tip60 acetylates six lysines of a specific class in core histones
            in vitro
  JOURNAL   Genes Cells 3 (12), 789-800 (1998)
   PUBMED   10096020
REFERENCE   9  (residues 1 to 546)
  AUTHORS   Yamamoto,T. and Horikoshi,M.
  TITLE     Novel substrate specificity of the histone acetyltransferase
            activity of HIV-1-Tat interactive protein Tip60
  JOURNAL   J Biol Chem 272 (49), 30595-30598 (1997)
   PUBMED   9388189
REFERENCE   10 (residues 1 to 546)
  AUTHORS   Kamine,J., Elangovan,B., Subramanian,T., Coleman,D. and
            Chinnadurai,G.
  TITLE     Identification of a cellular protein that specifically interacts
            with the essential cysteine region of the HIV-1 Tat transactivator
  JOURNAL   Virology 216 (2), 357-366 (1996)
   PUBMED   8607265
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB103287.1, BC013211.1 and
            BU737532.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the MYST
            family of histone acetyl transferases (HATs) and was originally
            isolated as an HIV-1 TAT-interactive protein. HATs play important
            roles in regulating chromatin remodeling, transcription and other
            nuclear processes by acetylating histone and nonhistone proteins.
            This protein is a histone acetylase that has a role in DNA repair
            and apoptosis and is thought to play an important role in signal
            transduction. Alternative splicing of this gene results in multiple
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.827992.1,
                                           SRR3476690.787374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341318.9/ ENSP00000340330.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..546
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..546
                     /product="histone acetyltransferase KAT5 isoform 1"
                     /EC_number="2.3.1.48"
                     /note="cPLA2 interacting protein; HIV-1 Tat interactive
                     protein, 60kDa; K-acetyltransferase 5; Tat interacting
                     protein, 60kDa; histone acetyltransferase KAT5;
                     cPLA(2)-interacting protein; 60 kDa Tat-interactive
                     protein; histone acetyltransferase HTATIP; K(lysine)
                     acetyltransferase 5; protein acetyltransferase KAT5;
                     protein crotonyltransferase KAT5; protein
                     2-hydroxyisobutyryltransferase KAT5; protein
                     lactyltransferase KAT5"
                     /calculated_mol_wt=61667
     Region          40..98
                     /region_name="Tudor-knot"
                     /note="RNA binding activity-knot of a chromodomain;
                     pfam11717"
                     /db_xref="CDD:432022"
     Site            order(55,61..63,78,80..83,87,89..92,94..95,102,105..106)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:350845"
     Site            order(55,80,83,87)
                     /site_type="other"
                     /note="putative methylated histone tail binding site
                     [chemical binding]"
                     /db_xref="CDD:350845"
     Region          76..537
                     /region_name="PLN00104"
                     /note="MYST -like histone acetyltransferase; Provisional"
                     /db_xref="CDD:215056"
     Site            order(77,79..84,86..90)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     Site            order(77,80,84,86,90)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:350845"
     CDS             1..546
                     /gene="KAT5"
                     /gene_synonym="cPLA2; ESA1; HTATIP; HTATIP1; NEDFASB;
                     PLIP; TIP; TIP60; ZC2HC5"
                     /coded_by="NM_182710.3:17..1657"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8110.1"
                     /db_xref="GeneID:10524"
                     /db_xref="HGNC:HGNC:5275"
                     /db_xref="MIM:601409"
ORIGIN      
        1 maevvspvpg agrrepgevg rargppvadp gvalspqgei iegcrlpvlr rnqdnedewp
       61 laeilsvkdi sgrklfyvhy idfnkrldew vtherldlkk iqfpkkeakt ptknglpgsr
      121 pgsperevpa saqasgktlp ipvqitlrfn lpkereaipg gepdqplsss sclqpnhrst
      181 krkvevvspa tpvpsetapa svfpqngaar ravaaqpgrk rksnclgtde dsqdssdgip
      241 saprmtgslv sdrshddivt rmknieciel grhrlkpwyf spypqelttl pvlylcefcl
      301 kygrslkclq rhltkcdlrh ppgneiyrkg tisffeidgr knksysqnlc llakcfldhk
      361 tlyydtdpfl fyvmteydck gfhivgyfsk ekestedynv aciltlppyq rrgygkllie
      421 fsyelskveg ktgtpekpls dlgllsyrsy wsqtileilm glksesgerp qitineisei
      481 tsikkedvis tlqylnliny ykgqyiltls edivdghera mlkrllrids kclhftpkdw
      541 skrgkw
//
LOCUS       NP_201591                480 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor subfamily 6 group A member 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_201591
VERSION     NP_201591.2
DBSOURCE    REFSEQ: accession NM_033334.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Neelathi,U.M., Ullah,E., George,A., Maftei,M.I., Boobalan,E.,
            Sanchez-Mendoza,D., Adams,C., McGaughey,D., Sergeev,Y.V., Ai
            Rawi,R., Naik,A., Bender,C., Maumenee,I.H., Michaelides,M.,
            Tan,T.G., Lin,S., Villasmil,R., Blain,D., Hufnagel,R.B., Arno,G.,
            Young,R.M., Guan,B. and Brooks,B.P.
  TITLE     Variants in NR6A1 cause a novel oculo vertebral renal syndrome
  JOURNAL   Nat Commun 16 (1), 6111 (2025)
   PUBMED   40610405
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Wu,Q., Li,X., Long,M., Xie,X. and Liu,Q.
  TITLE     Integrated analysis of histone lysine lactylation (Kla)-specific
            genes suggests that NR6A1, OSBP2 and UNC119B are novel therapeutic
            targets for hepatocellular carcinoma
  JOURNAL   Sci Rep 13 (1), 18642 (2023)
   PUBMED   37903971
  REMARK    GeneRIF: Integrated analysis of histone lysine lactylation
            (Kla)-specific genes suggests that NR6A1, OSBP2 and UNC119B are
            novel therapeutic targets for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Daisuke,H., Kato,H., Fukumura,K., Mayeda,A., Miyagi,Y., Seiki,M.
            and Koshikawa,N.
  TITLE     Novel LAMC2 fusion protein has tumor-promoting properties in
            ovarian carcinoma
  JOURNAL   Cancer Sci 112 (12), 4957-4967 (2021)
   PUBMED   34689384
  REMARK    GeneRIF: Novel LAMC2 fusion protein has tumor-promoting properties
            in ovarian carcinoma.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Zhou,W., Jiang,R., Wang,Y., Li,Y., Sun,Z. and Zhao,H.
  TITLE     hsa_circ_001653 up-regulates NR6A1 expression and elicits gastric
            cancer progression by binding to microRNA-377
  JOURNAL   Exp Physiol 105 (12), 2141-2153 (2020)
   PUBMED   33006200
  REMARK    GeneRIF: hsa_circ_001653 up-regulates NR6A1 expression and elicits
            gastric cancer progression by binding to microRNA-377.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Wang,Y., Wan,X., Hao,Y., Zhao,Y., Du,L., Huang,Y., Liu,Z., Wang,Y.,
            Wang,N. and Zhang,P.
  TITLE     NR6A1 regulates lipid metabolism through mammalian target of
            rapamycin complex 1 in HepG2 cells
  JOURNAL   Cell Commun Signal 17 (1), 77 (2019)
   PUBMED   31315616
  REMARK    GeneRIF: the role of NR6A1 in the lipogenesis in HepG2 cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Agoulnik,I.Y., Cho,Y., Niederberger,C., Kieback,D.G. and
            Cooney,A.J.
  TITLE     Cloning, expression analysis and chromosomal localization of the
            human nuclear receptor gene GCNF
  JOURNAL   FEBS Lett 424 (1-2), 73-78 (1998)
   PUBMED   9537518
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Kapelle,M., Kratzschmar,J., Husemann,M. and Schleuning,W.D.
  TITLE     cDNA cloning of two closely related forms of human germ cell
            nuclear factor (GCNF)
  JOURNAL   Biochim Biophys Acta 1352 (1), 13-17 (1997)
   PUBMED   9177477
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Yan,Z.H., Medvedev,A., Hirose,T., Gotoh,H. and Jetten,A.M.
  TITLE     Characterization of the response element and DNA binding properties
            of the nuclear orphan receptor germ cell nuclear factor/retinoid
            receptor-related testis-associated receptor
  JOURNAL   J Biol Chem 272 (16), 10565-10572 (1997)
   PUBMED   9099702
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Lei,W., Hirose,T., Zhang,L.X., Adachi,H., Spinella,M.J.,
            Dmitrovsky,E. and Jetten,A.M.
  TITLE     Cloning of the human orphan receptor germ cell nuclear
            factor/retinoid receptor-related testis-associated receptor and its
            differential regulation during embryonal carcinoma cell
            differentiation
  JOURNAL   J Mol Endocrinol 18 (2), 167-176 (1997)
   PUBMED   9134503
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Susens,U. and Borgmeyer,U.
  TITLE     Characterization of the human germ cell nuclear factor gene
  JOURNAL   Biochim Biophys Acta 1309 (3), 179-182 (1996)
   PUBMED   8982251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354928.9, U80802.1 and
            AL354979.17.
            
            On Oct 1, 2004 this sequence version replaced NP_201591.1.
            
            Summary: This gene encodes an orphan nuclear receptor which is a
            member of the nuclear hormone receptor family. Its expression
            pattern suggests that it may be involved in neurogenesis and germ
            cell development. The protein can homodimerize and bind DNA, but in
            vivo targets have not been identified. Alternate splicing results
            in multiple transcript variants.[provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U80802.1, HQ692858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000487099.7/ ENSP00000420267.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..480
                     /product="nuclear receptor subfamily 6 group A member 1
                     isoform 1"
                     /note="retinoic acid receptor-related testis-associated
                     receptor; retinoid receptor-related testis-specific
                     receptor"
                     /calculated_mol_wt=54252
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          52..141
                     /region_name="NR_DBD_GCNF_like"
                     /note="DNA-binding domain of Germ cell nuclear factor
                     (GCNF) F1 is composed of two C4-type zinc fingers;
                     cd07169"
                     /db_xref="CDD:143543"
     Site            order(60,63,77,80,96,102,112,115)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143543"
     Site            order(70..72,78..79,81,83,86,89,109..110,113,116,127,130)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143543"
     Region          131..150
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          162..199
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          172..253
                     /region_name="Sufficient for interaction with UIMC1.
                     /evidence=ECO:0000250|UniProtKB:Q64249"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          256..467
                     /region_name="NR_LBD_DHR4_like"
                     /note="The ligand binding domain of orphan nuclear
                     receptor Ecdysone-induced receptor DHR4; cd06953"
                     /db_xref="CDD:132751"
     Site            order(286..287,291,325,329,332,346,369)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132751"
     Site            order(296,299,303,308,313..314,316..317,320..321)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132751"
     CDS             1..480
                     /gene="NR6A1"
                     /gene_synonym="CT150; GCNF; GCNF1; hGCNF; hRTR; NR61; RTR"
                     /coded_by="NM_033334.4:193..1635"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS35137.1"
                     /db_xref="GeneID:2649"
                     /db_xref="HGNC:HGNC:7985"
                     /db_xref="MIM:602778"
ORIGIN      
        1 merdepppsg ggggggsagf leppaalppp prngfcqdel aeldpgtisv sddraeqrtc
       61 licgdratgl hygiiscegc kgffkrsicn krvyrcsrdk ncvmsrkqrn rcqycrllkc
      121 lqmgmnrkai redgmpggrn ksigpvqise eeierimsgq efeeeanhws nhgdsdhssp
      181 gnrasesnqp spgstlsssr svelngfmaf reqymgmsvp phyqyiphlf sysghspllp
      241 qqarsldpqs yslihqllsa edleplgtpm liedgyavtq aelfallcrl adellfrqia
      301 wikklpffce lsikdytcll sstwqelill ssltvyskqi fgeladvtak yspsdeelhr
      361 fsdegmevie rliylyhkfh qlkvsneeya cmkainflnq dirgltsasq leqlnkrywy
      421 icqdfteyky thqpnrfpdl mmclpeiryi agkmvnvple qlpllfkvvl hscktsvgke
//
LOCUS       NP_653318                311 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-20 receptor subunit beta precursor [Homo sapiens].
ACCESSION   NP_653318
VERSION     NP_653318.2
DBSOURCE    REFSEQ: accession NM_144717.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 311)
  AUTHORS   Zhang,H., Liu,Y., Wang,B. and Wang,C.
  TITLE     Interleukin 20 receptor subunit beta (IL20RB) predicts poor
            prognosis and regulates immune cell infiltration in clear cell
            renal cell carcinoma
  JOURNAL   BMC Genom Data 23 (1), 58 (2022)
   PUBMED   35883015
  REMARK    GeneRIF: Interleukin 20 receptor subunit beta (IL20RB) predicts
            poor prognosis and regulates immune cell infiltration in clear cell
            renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 311)
  AUTHORS   Zhong,Y., Zhang,X. and Chong,W.
  TITLE     Interleukin-24 Immunobiology and Its Roles in Inflammatory Diseases
  JOURNAL   Int J Mol Sci 23 (2), 627 (2022)
   PUBMED   35054813
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 311)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 311)
  AUTHORS   Chen,J., Caspi,R.R. and Chong,W.P.
  TITLE     IL-20 receptor cytokines in autoimmune diseases
  JOURNAL   J Leukoc Biol 104 (5), 953-959 (2018)
   PUBMED   30260500
  REMARK    Review article
REFERENCE   5  (residues 1 to 311)
  AUTHORS   Kragstrup,T.W., Andersen,T., Heftdal,L.D., Hvid,M., Gerwien,J.,
            Sivakumar,P., Taylor,P.C., Senolt,L. and Deleuran,B.
  TITLE     The IL-20 Cytokine Family in Rheumatoid Arthritis and
            Spondyloarthritis
  JOURNAL   Front Immunol 9, 2226 (2018)
   PUBMED   30319661
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 311)
  AUTHORS   Pletnev,S., Magracheva,E., Kozlov,S., Tobin,G., Kotenko,S.V.,
            Wlodawer,A. and Zdanov,A.
  TITLE     Characterization of the recombinant extracellular domains of human
            interleukin-20 receptors and their complexes with interleukin-19
            and interleukin-20
  JOURNAL   Biochemistry 42 (43), 12617-12624 (2003)
   PUBMED   14580208
  REMARK    GeneRIF: forms stable complex with interleukin-19 and
            interleukin-20 [IL-20R1][IL-20R2]
REFERENCE   7  (residues 1 to 311)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   8  (residues 1 to 311)
  AUTHORS   Parrish-Novak,J., Xu,W., Brender,T., Yao,L., Jones,C., West,J.,
            Brandt,C., Jelinek,L., Madden,K., McKernan,P.A., Foster,D.C.,
            Jaspers,S. and Chandrasekher,Y.A.
  TITLE     Interleukins 19, 20, and 24 signal through two distinct receptor
            complexes. Differences in receptor-ligand interactions mediate
            unique biological functions
  JOURNAL   J Biol Chem 277 (49), 47517-47523 (2002)
   PUBMED   12351624
REFERENCE   9  (residues 1 to 311)
  AUTHORS   Dumoutier,L., Leemans,C., Lejeune,D., Kotenko,S.V. and Renauld,J.C.
  TITLE     Cutting edge: STAT activation by IL-19, IL-20 and mda-7 through
            IL-20 receptor complexes of two types
  JOURNAL   J Immunol 167 (7), 3545-3549 (2001)
   PUBMED   11564763
REFERENCE   10 (residues 1 to 311)
  AUTHORS   Blumberg,H., Conklin,D., Xu,W.F., Grossmann,A., Brender,T.,
            Carollo,S., Eagan,M., Foster,D., Haldeman,B.A., Hammond,A.,
            Haugen,H., Jelinek,L., Kelly,J.D., Madden,K., Maurer,M.F.,
            Parrish-Novak,J., Prunkard,D., Sexson,S., Sprecher,C., Waggie,K.,
            West,J., Whitmore,T.E., Yao,L., Kuechle,M.K., Dale,B.A. and
            Chandrasekher,Y.A.
  TITLE     Interleukin 20: discovery, receptor identification, and role in
            epidermal function
  JOURNAL   Cell 104 (1), 9-19 (2001)
   PUBMED   11163236
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AY358305.1 and BC063696.1.
            
            On Dec 20, 2003 this sequence version replaced NP_653318.1.
            
            Summary: IL20RB and IL20RA (MIM 605620) form a heterodimeric
            receptor for interleukin-20 (IL20; MIM 605619) (Blumberg et al.,
            2001 [PubMed 11163236]).[supplied by OMIM, Feb 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063696.1, AY358305.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000329582.9/ ENSP00000328133.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..311
                     /product="interleukin-20 receptor subunit beta precursor"
                     /note="fibronectin type III domain containing 6;
                     interleukin-20 receptor II; IL-20 receptor subunit beta;
                     interleukin 20 receptor beta subunit"
                     /calculated_mol_wt=31518
     sig_peptide     1..29
                     /calculated_mol_wt=3576
     Region          15..124
                     /region_name="Tissue_fac"
                     /note="Tissue factor; pfam01108"
                     /db_xref="CDD:460067"
     mat_peptide     30..311
                     /product="interleukin-20 receptor subunit beta"
                     /calculated_mol_wt=31518
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXL0.1)"
     Site            134
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXL0.1)"
     Region          136..225
                     /region_name="Interfer-bind"
                     /note="Interferon-alpha/beta receptor, fibronectin type
                     III; cl46366"
                     /db_xref="CDD:480706"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXL0.1)"
     CDS             1..311
                     /gene="IL20RB"
                     /gene_synonym="DIRS1; FNDC6; IL-20R-beta; IL-20R2;
                     IL-20RB"
                     /coded_by="NM_144717.4:132..1067"
                     /db_xref="CCDS:CCDS3093.1"
                     /db_xref="GeneID:53833"
                     /db_xref="HGNC:HGNC:6004"
                     /db_xref="MIM:605621"
ORIGIN      
        1 mqtftmvlee iwtslfmwff yalipclltd evailpapqn lsvlstnmkh llmwspviap
       61 getvyysvey qgeyeslyts hiwipsswcs ltegpecdvt dditatvpyn lrvratlgsq
      121 tsawsilkhp fnrnstiltr pgmeitkdgf hlvieledlg pqfeflvayw rrepgaeehv
      181 kmvrsggipv hletmepgaa ycvkaqtfvk aigrysafsq tecvevqgea iplvlalfaf
      241 vgfmlilvvv plfvwkmgrl lqysccpvvv lpdtlkitns pqkliscrre evdacatavm
      301 speellrawi s
//
LOCUS       NP_001353421             263 aa            linear   PRI 20-NOV-2025
DEFINITION  tetraspanin-17 isoform e [Homo sapiens].
ACCESSION   NP_001353421 XP_005265933
VERSION     NP_001353421.1
DBSOURCE    REFSEQ: accession NM_001366492.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Guo,X.B., Zhang,X.C., Chen,P., Ma,L.M. and Shen,Z.Q.
  TITLE     miR-378a-3p inhibits cellular proliferation and migration in
            glioblastoma multiforme by targeting tetraspanin 17
  JOURNAL   Oncol Rep 42 (5), 1957-1971 (2019)
   PUBMED   31432186
  REMARK    GeneRIF: Data suggested that increased miR378a3p and decreased
            TSPAN17 levels were associated with improved survival in
            glioblastoma multiforme (GBM). Additionally, high levels of TSPAN17
            were linked to the poor prognosis of patients with GBM aged 5060,
            larger tumor sizes and an advanced World Health Organization stage.
            TSPAN17 was identified and confirmed as a direct target of miR378a.
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Reyat,J.S., Chimen,M., Noy,P.J., Szyroka,J., Rainger,G.E. and
            Tomlinson,M.G.
  TITLE     ADAM10-Interacting Tetraspanins Tspan5 and Tspan17 Regulate
            VE-Cadherin Expression and Promote T Lymphocyte Transmigration
  JOURNAL   J Immunol 199 (2), 666-676 (2017)
   PUBMED   28600292
  REMARK    GeneRIF: Endothelial Tspan5- and Tspan17-ADAM10 complexes may
            regulate inflammation by maintaining normal VE-cadherin expression
            and promoting T lymphocyte transmigration.
REFERENCE   4  (residues 1 to 263)
  AUTHORS   Dornier,E., Coumailleau,F., Ottavi,J.F., Moretti,J., Boucheix,C.,
            Mauduit,P., Schweisguth,F. and Rubinstein,E.
  TITLE     TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and
            promote Notch activation in flies and mammals
  JOURNAL   J Cell Biol 199 (3), 481-496 (2012)
   PUBMED   23091066
  REMARK    Erratum:[J Cell Biol. 2016 May 23;213(4):495-6. doi:
            10.1083/jcb.20120113304262016c. PMID: 27185832]
REFERENCE   5  (residues 1 to 263)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   6  (residues 1 to 263)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091934.2 and CB215495.1.
            
            On Oct 6, 2018 this sequence version replaced XP_005265933.1.
            
            Summary: This gene encodes a member of the transmembrane 4
            superfamily. It is characterized by four tetraspanin transmembrane
            segments. The function of this gene has not yet been determined.
            [provided by RefSeq, Mar 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.6385.1,
                                           SRR1803616.19787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.2"
     Protein         1..263
                     /product="tetraspanin-17 isoform e"
                     /EC_number="3.6.5.3"
                     /note="F-box only protein 23, transmembrane 4 superfamily
                     member 17; tetraspan protein SB134"
                     /calculated_mol_wt=29735
     Region          <13..194
                     /region_name="Tetraspanin"
                     /note="Tetraspanin family; pfam00335"
                     /db_xref="CDD:459767"
     Region          49..169
                     /region_name="TM4SF9_like_LEL"
                     /note="Tetraspanin, extracellular domain or large
                     extracellular loop (LEL), TM4SF9_like subfamily.
                     Tetraspanins are trans-membrane proteins with 4
                     trans-membrane segments. Both the N- and C-termini lie on
                     the intracellular side of the membrane. This alignment...;
                     cd03159"
                     /db_xref="CDD:239412"
     Site            order(50,55,59,61..62,65,79,82..83,86..87)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:239412"
     CDS             1..263
                     /gene="TSPAN17"
                     /gene_synonym="FBX23; FBXO23; TM4SF17"
                     /coded_by="NM_001366492.2:133..924"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="GeneID:26262"
                     /db_xref="HGNC:HGNC:13594"
                     /db_xref="MIM:620446"
ORIGIN      
        1 mpgkhqhfqe pevgccgkyf lfgfnivfwf svflgliffl elatgilafv fkdwirdqln
       61 lfinnnvkay rddidlqnli dfaqeywscc gargpndwnl niyfnctdln psrercgvpf
      121 sccvrdpaed vlntqcgydv rlkleleqqg fihtkgcvgq fekwlqdnli vvagvfmgia
      181 llqifgicla qnlvsdikav kanwskwndd fenhwltpti sevlstagpq qnsltgapgp
      241 appsrhvffg lgglypeptf knw
//
LOCUS       NP_001036008             449 aa            linear   PRI 20-NOV-2025
DEFINITION  glycine receptor subunit alpha-3 isoform b precursor [Homo
            sapiens].
ACCESSION   NP_001036008
VERSION     NP_001036008.1
DBSOURCE    REFSEQ: accession NM_001042543.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Aboheimed,G.I., AlRasheed,M.M., Almudimeegh,S., Pena-Guerra,K.A.,
            Cardona-Londono,K.J., Salih,M.A., Seidahmed,M.Z., Al-Mohanna,F.,
            Colak,D., Harvey,R.J., Harvey,K., Arold,S.T., Kaya,N. and Ruiz,A.J.
  TITLE     Clinical, genetic, and functional characterization of the glycine
            receptor beta-subunit A455P variant in a family affected by
            hyperekplexia syndrome
  JOURNAL   J Biol Chem 298 (7), 102018 (2022)
   PUBMED   35526563
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Sandholm,N., Haukka,J.K., Toppila,I., Valo,E., Harjutsalo,V.,
            Forsblom,C. and Groop,P.H.
  TITLE     Confirmation of GLRA3 as a susceptibility locus for albuminuria in
            Finnish patients with type 1 diabetes
  JOURNAL   Sci Rep 8 (1), 12408 (2018)
   PUBMED   30120300
  REMARK    GeneRIF: In this study, the association between the common
            rs10011025 variant in the GLRA3 locus, and albuminuria, was
            confirmed in 1259 independent Finnish individuals with type 1
            diabetes (p = 0.0013), and meta-analysis of all Finnish individuals
            yielded a genome-wide significant association.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Tang,B., Devenish,S.O. and Lummis,S.C.R.
  TITLE     Identification of Novel Functionally Important Aromatic Residue
            Interactions in the Extracellular Domain of the Glycine Receptor
  JOURNAL   Biochemistry 57 (27), 4029-4035 (2018)
   PUBMED   29947514
  REMARK    GeneRIF: This study explores the roles of Tyr and Trp residues in
            the extracellular domains of the glycine receptor alpha 3 and shows
            that four such residues that have not been previously studied (Y24,
            Y58, W170, and Y197) contribute significantly to the function of
            the protein.
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Patrizio,A., Renner,M., Pizzarelli,R., Triller,A. and Specht,C.G.
  TITLE     Alpha subunit-dependent glycine receptor clustering and regulation
            of synaptic receptor numbers
  JOURNAL   Sci Rep 7 (1), 10899 (2017)
   PUBMED   28883437
  REMARK    GeneRIF: Using quantitative photoactivated localisation microscopy
            the authors found that alpha-1 and alpha-3 containing glycine
            receptors display the same alpha3:beta2 stoichiometry and gephyrin
            binding.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Gratacos,M., Costas,J., de Cid,R., Bayes,M., Gonzalez,J.R.,
            Baca-Garcia,E., de Diego,Y., Fernandez-Aranda,F.,
            Fernandez-Piqueras,J., Guitart,M., Martin-Santos,R., Martorell,L.,
            Menchon,J.M., Roca,M., Saiz-Ruiz,J., Sanjuan,J., Torrens,M.,
            Urretavizcaya,M., Valero,J., Vilella,E., Estivill,X. and
            Carracedo,A.
  CONSRTM   Psychiatric Genetics Network Group
  TITLE     Identification of new putative susceptibility genes for several
            psychiatric disorders by association analysis of regulatory and
            non-synonymous SNPs of 306 genes involved in neurotransmission and
            neurodevelopment
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 150B (6), 808-816 (2009)
   PUBMED   19086053
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Breitinger,H.G., Villmann,C., Rennert,J., Ballhausen,D. and
            Becker,C.M.
  TITLE     Hydroxylated residues influence desensitization behaviour of
            recombinant alpha3 glycine receptor channels
  JOURNAL   J Neurochem 83 (1), 30-36 (2002)
   PUBMED   12358726
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Sobetzko,D., Sander,T. and Becker,C.M.
  TITLE     Genetic variation of the human glycine receptor subunit genes GLRA3
            and GLRB and susceptibility to idiopathic generalized epilepsies
  JOURNAL   Am J Med Genet 105 (6), 534-538 (2001)
   PUBMED   11496371
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Nikolic,Z., Laube,B., Weber,R.G., Lichter,P., Kioschis,P.,
            Poustka,A., Mulhardt,C. and Becker,C.M.
  TITLE     The human glycine receptor subunit alpha3. Glra3 gene structure,
            chromosomal localization, and functional characterization of
            alternative transcripts
  JOURNAL   J Biol Chem 273 (31), 19708-19714 (1998)
   PUBMED   9677400
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Kingsmore,S.F., Suh,D. and Seldin,M.F.
  TITLE     Genetic mapping of the glycine receptor alpha 3 subunit on mouse
            chromosome 8
  JOURNAL   Mamm Genome 5 (12), 831-832 (1994)
   PUBMED   7894176
  REMARK    GeneRIF: Determines location of mouse glycine alpha 3.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC036086.1, AC107216.5 and
            U93917.1.
            
            Summary: This gene encodes a member of the ligand-gated ion channel
            protein family. The encoded protein is a member of the glycine
            receptor subfamily. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (2, also known as alpha3K) lacks
            an in-frame exon in the 3' coding region, compared to variant 1.
            The encoded isoform (b) is shorter, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U93917.1, SRR1803613.211947.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.1"
     Protein         1..449
                     /product="glycine receptor subunit alpha-3 isoform b
                     precursor"
                     /note="glycine receptor subunit alpha-3; glycine receptor,
                     alpha-3 polypeptide; ligand gated ion channel"
                     /calculated_mol_wt=48184
     sig_peptide     1..33
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3797
     Region          12..436
                     /region_name="LIC"
                     /note="Cation transporter family protein; TIGR00860"
                     /db_xref="CDD:273305"
     CDS             1..449
                     /gene="GLRA3"
                     /coded_by="NM_001042543.3:437..1786"
                     /note="isoform b precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS43283.1"
                     /db_xref="GeneID:8001"
                     /db_xref="HGNC:HGNC:4328"
                     /db_xref="MIM:600421"
ORIGIN      
        1 mahvrhfrtl vsgfyfweaa lllslvatke tdsarsrsap mspsdfldkl mgrtsgydar
       61 irpnfkgppv nvtcnifins fgsiaettmd yrvniflrqk wndprlayse ypddsldldp
      121 smldsiwkpd lffanekgan fhevttdnkl lrifkngnvl ysirltltls cpmdlknfpm
      181 dvqtcimqle sfgytmndli fewqdeapvq vaegltlpqf llkeekdlry ctkhyntgkf
      241 tcievrfhle rqmgyyliqm yipsllivil swvsfwinmd aaparvalgi ttvltmttqs
      301 sgsraslpkv syvkaidiwm avcllfvfsa lleyaavnfv srqhkellrf rrkrknkdde
      361 vresrfsfta ygmgpclqak dgmtpkgpnh pvqvmpkspd emrkvfidra kkidtisrac
      421 fplaflifni fywviykilr hedihqqqd
//
LOCUS       NP_710181                367 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory ankyrin repeat
            subunit B isoform B [Homo sapiens].
ACCESSION   NP_710181
VERSION     NP_710181.2
DBSOURCE    REFSEQ: accession NM_153697.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Kariuki,S.N., Ghodke-Puranik,Y., Dorschner,J.M., Chrabot,B.S.,
            Kelly,J.A., Tsao,B.P., Kimberly,R.P., Alarcon-Riquelme,M.E.,
            Jacob,C.O., Criswell,L.A., Sivils,K.L., Langefeld,C.D.,
            Harley,J.B., Skol,A.D. and Niewold,T.B.
  TITLE     Genetic analysis of the pathogenic molecular sub-phenotype
            interferon-alpha identifies multiple novel loci involved in
            systemic lupus erythematosus
  JOURNAL   Genes Immun 16 (1), 15-23 (2015)
   PUBMED   25338677
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Kapoor,M., Wang,J.C., Wetherill,L., Le,N., Bertelsen,S.,
            Hinrichs,A.L., Budde,J., Agrawal,A., Almasy,L., Bucholz,K.,
            Dick,D.M., Harari,O., Xiaoling,X., Hesselbrock,V., Kramer,J.,
            Nurnberger,J.I. Jr., Rice,J., Schuckit,M., Tischfield,J.,
            Porjesz,B., Edenberg,H.J., Bierut,L., Foroud,T. and Goate,A.
  TITLE     Genome-wide survival analysis of age at onset of alcohol dependence
            in extended high-risk COGA families
  JOURNAL   Drug Alcohol Depend 142, 56-62 (2014)
   PUBMED   24962325
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Dechamps,C., Bach,S., Portetelle,D. and Vandenbol,M.
  TITLE     The Tre2 oncoprotein, implicated in Ewing's sarcoma, interacts with
            two components of the cytoskeleton
  JOURNAL   Biotechnol Lett 28 (4), 223-231 (2006)
   PUBMED   16555005
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK301209.1, BC063622.1 and AI439698.1.
            
            On Aug 25, 2010 this sequence version replaced NP_710181.1.
            
            Transcript Variant: This variant (B) contains an alternate segment
            in the 3' UTR and lacks the last 18 exons, compared to variant A.
            The resulting protein (isoform B) is shorter than isoform A.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.211262.1,
                                           SRR1803617.43991.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..367
                     /product="serine/threonine-protein phosphatase 6
                     regulatory ankyrin repeat subunit B isoform B"
                     /note="serine/threonine-protein phosphatase 6 regulatory
                     ankyrin repeat subunit B; ankyrin repeat domain-containing
                     protein 44; serine/threonine-protein phosphatase 6
                     regulatory subunit ARS-B"
                     /calculated_mol_wt=39470
     Region          7..36
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          10..61
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Region          11..38
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..71
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          40..69
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          54..343
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          73..102
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          76..104
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(79..80,83..85,87..88,92,95,104,106,108,112..113,
                     116..118,120..121,125,128,137,139,141,145..146,149..151,
                     153..154,158,161,170)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          106..137
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          106..135
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          139..170
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          139..168
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          172..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          172..201
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          205..236
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          205..234
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..267
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          238..266
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..301
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          305..336
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          305..334
                     /region_name="ANK 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          338..367
                     /region_name="ANK 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N8A2.3)"
     Region          338..364
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          338..364
                     /region_name="ANK"
                     /note="ankyrin repeats; smart00248"
                     /db_xref="CDD:197603"
     CDS             1..367
                     /gene="ANKRD44"
                     /gene_synonym="ARSB; PP6-ARS-B"
                     /coded_by="NM_153697.3:177..1280"
                     /note="isoform B is encoded by transcript variant B"
                     /db_xref="CCDS:CCDS33355.2"
                     /db_xref="GeneID:91526"
                     /db_xref="HGNC:HGNC:25259"
                     /db_xref="MIM:620861"
ORIGIN      
        1 mavlkltdqp plvqaifsgd peeirmlihk tedvntldse krtplhvaaf lgdaeiiell
       61 ilsgarvnak dnmwltplhr avasrseeav qvlikhsadv nardknwqtp lhvaaankav
      121 kcaeviipll ssvnvsdrgg rtalhhaaln ghvemvnlll akganinafd kkdrralhwa
      181 aymghldvva llinhgaevt ckdkkgytpl haaasngqin vvkhllnlgv eideinvygn
      241 talhiacyng qdavvnelid yganvnqpnn ngftplhfaa asthgalcle llvnngadvn
      301 iqskdgkspl hmtavhgrft rsqtliqngg eidcvdkdgn tplhvaaryg hellintlit
      361 sgadtak
//
LOCUS       NP_001352765             966 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            11 [Homo sapiens].
ACCESSION   NP_001352765 XP_006724497
VERSION     NP_001352765.1
DBSOURCE    REFSEQ: accession NM_001365836.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 966)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 966)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 966)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 966)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 966)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 966)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 966)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 966)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 966)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 966)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, AL954743.9,
            BC000976.4 and AL096767.14.
            
            On Sep 13, 2018 this sequence version replaced XP_006724497.1.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC000976.4 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2163105, SAMN03465418 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..966
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..966
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 11"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=104811
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          408..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          657..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          <766..957
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3Q2; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          819..856
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Site            828
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     CDS             1..966
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001365836.1:647..3547"
                     /note="isoform 11 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS93184.1"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlvsthhl
      541 hsssededie gafpnelslq qafsdyqiqq mtanfvdqfg fndeefadqd dninapfdri
      601 aeinfnidad edspsaalfe accsdriqpf dddedediwe dsdtrcaarv marprfgaph
      661 asescskngp erggqdgkas leahrdapga gappapgkke appvegdseg amwtavfdep
      721 anstptapgv vrdvgssvwa agtsapeekg wakftdfqpf ccsesgprcs spvdtecsha
      781 egsrsqgpek asqasyfavs paspcawnvc vtrkapllas dssssggshs edgdqkaasa
      841 mdavsrgpgr eapplptvar teeavgrvgc adsrllspac papkevtaap avavppeatv
      901 aittalskag paiptpavss alavavplgp imavtaapam vatlgtvtkd gktdappega
      961 alngpv
//
LOCUS       NP_001296812             626 aa            linear   PRI 20-NOV-2025
DEFINITION  protein ALEX isoform Alex [Homo sapiens].
ACCESSION   NP_001296812
VERSION     NP_001296812.1
DBSOURCE    REFSEQ: accession NM_001309883.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 626)
  AUTHORS   Lin,J., Nie,Q., Cheng,J., Zhong,Y.N., Zhang,T., Zhang,X., Ge,X.,
            Ding,Y., Niu,C., Gao,Y., Wang,K., Gao,M., Wang,X., Chen,W., Yun,C.,
            Ye,C., Xu,J., Shaoyong,W., Zhang,L., Shang,P., Luo,X., Zhang,Z.,
            Zheng,X., Sha,X., Zhang,J., Nie,S., Zhang,X., Ren,F., Liu,H.,
            Dong,E., Yu,X., Ji,L., Pang,Y., Sun,J.P. and Jiang,C.
  TITLE     A microbial amino-acid-conjugated bile acid, tryptophan-cholic
            acid, improves glucose homeostasis via the orphan receptor MRGPRE
  JOURNAL   Cell 188 (17), 4530-4548 (2025)
   PUBMED   40446798
REFERENCE   2  (residues 1 to 626)
  AUTHORS   Crane,J.L., Shamblott,M.J., Axelman,J., Hsu,S., Levine,M.A. and
            Germain-Lee,E.L.
  TITLE     Imprinting status of Galpha(s), NESP55, and XLalphas in cell
            cultures derived from human embryonic germ cells: GNAS imprinting
            in human embryonic germ cells
  JOURNAL   Clin Transl Sci 2 (5), 355-360 (2009)
   PUBMED   20443919
  REMARK    GeneRIF: analysis of the imprinting Status of Galpha(s), NESP55,
            and XLalphas in cell cultures derived from human embryonic germ
            cells
REFERENCE   3  (residues 1 to 626)
  AUTHORS   Bastepe,M.
  TITLE     The GNAS Locus: Quintessential Complex Gene Encoding Gsalpha,
            XLalphas, and other Imprinted Transcripts
  JOURNAL   Curr Genomics 8 (6), 398-414 (2007)
   PUBMED   19412439
  REMARK    GeneRIF: GNAS locus has a highly complex imprinted expression
            pattern, giving rise to transcripts (including non-coding) that are
            maternally, paternally, or biallelically expressed.
REFERENCE   4  (residues 1 to 626)
  AUTHORS   Jakobsen,A.M., Ahlman,H., Kolby,L., Abrahamsson,J.,
            Fischer-Colbrie,R. and Nilsson,O.
  TITLE     NESP55, a novel chromogranin-like peptide, is expressed in
            endocrine tumours of the pancreas and adrenal medulla but not in
            ileal carcinoids
  JOURNAL   Br J Cancer 88 (11), 1746-1754 (2003)
   PUBMED   12771991
  REMARK    GeneRIF: Neuroendocrine secretory protein 55 is found in a subset
            of neuroendocrine tumours showing differentiation towards adrenal
            chromaffin cells and pancreatic islets cells and not in ileal
            carcinoids
REFERENCE   5  (residues 1 to 626)
  AUTHORS   Freson,K., Jaeken,J., Van Helvoirt,M., de Zegher,F.,
            Wittevrongel,C., Thys,C., Hoylaerts,M.F., Vermylen,J. and Van
            Geet,C.
  TITLE     Functional polymorphisms in the paternally expressed XLalphas and
            its cofactor ALEX decrease their mutual interaction and enhance
            receptor-mediated cAMP formation
  JOURNAL   Hum Mol Genet 12 (10), 1121-1130 (2003)
   PUBMED   12719376
REFERENCE   6  (residues 1 to 626)
  AUTHORS   Weiss,U., Ischia,R., Eder,S., Lovisetti-Scamihorn,P., Bauer,R. and
            Fischer-Colbrie,R.
  TITLE     Neuroendocrine secretory protein 55 (NESP55): alternative splicing
            onto transcripts of the GNAS gene and posttranslational processing
            of a maternally expressed protein
  JOURNAL   Neuroendocrinology 71 (3), 177-186 (2000)
   PUBMED   10729789
REFERENCE   7  (residues 1 to 626)
  AUTHORS   Ischia,R., Lovisetti-Scamihorn,P., Hogue-Angeletti,R.,
            Wolkersdorfer,M., Winkler,H. and Fischer-Colbrie,R.
  TITLE     Molecular cloning and characterization of NESP55, a novel
            chromogranin-like precursor of a peptide with 5-HT1B receptor
            antagonist activity
  JOURNAL   J Biol Chem 272 (17), 11657-11662 (1997)
   PUBMED   9111083
REFERENCE   8  (residues 1 to 626)
  AUTHORS   Haldeman-Englert,C.R., Hurst,A.C.E. and Levine,M.A.
  TITLE     Disorders of GNAS Inactivation
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   29072892
REFERENCE   9  (residues 1 to 626)
  AUTHORS   Szymczuk,V., Florenzano,P., de Castro,L.F., Collins,M.T. and
            Boyce,A.M.
  TITLE     Fibrous Dysplasia / McCune-Albright Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25719192
REFERENCE   10 (residues 1 to 626)
  AUTHORS   Weinstein,L.S., Gejman,P.V., de Mazancourt,P., American,N. and
            Spiegel,A.M.
  TITLE     A heterozygous 4-bp deletion mutation in the Gs alpha gene (GNAS1)
            in a patient with Albright hereditary osteodystrophy
  JOURNAL   Genomics 13 (4), 1319-1321 (1992)
   PUBMED   1505964
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL132655.13, AJ224867.1,
            AA948160.1, BF879848.1 and BF800576.1.
            
            Summary: This locus has a highly complex imprinted expression
            pattern. It gives rise to maternally, paternally, and biallelically
            expressed transcripts that are derived from four alternative
            promoters and 5' exons. Some transcripts contain a differentially
            methylated region (DMR) at their 5' exons, and this DMR is commonly
            found in imprinted genes and correlates with transcript expression.
            An antisense transcript is produced from an overlapping locus on
            the opposite strand. One of the transcripts produced from this
            locus, and the antisense transcript, are paternally expressed
            noncoding RNAs, and may regulate imprinting in this region. In
            addition, one of the transcripts contains a second overlapping ORF,
            which encodes a structurally unrelated protein - Alex. Alternative
            splicing of downstream exons is also observed, which results in
            different forms of the stimulatory G-protein alpha subunit, a key
            element of the classical signal transduction pathway linking
            receptor-ligand interactions with the activation of adenylyl
            cyclase and a variety of cellular reponses. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            Mutations in this gene result in pseudohypoparathyroidism type 1a,
            pseudohypoparathyroidism type 1b, Albright hereditary
            osteodystrophy, pseudopseudohypoparathyroidism, McCune-Albright
            syndrome, progressive osseus heteroplasia, polyostotic fibrous
            dysplasia of bone, and some pituitary tumors. [provided by RefSeq,
            Aug 2012].
            
            Transcript Variant: This variant (12) contains an alternate 5' exon
            structure compared to variant 1. It encodes the protein Alex (also
            known as alexX), which has no similarity to other proteins encoded
            by this gene. It interacts with XLas, and their interaction is
            essential for G-protein signaling in neuroendocrine cells. Variants
            2 and 12 encode the same protein (Alex).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ224867.1, AA062932.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene :: PMID: 19412439
            NMD candidate  :: PMID: 12719376
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..626
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.32"
     Protein         1..626
                     /product="protein ALEX isoform Alex"
                     /note="secretogranin VI; G protein subunit alpha S;
                     guanine nucleotide binding protein (G protein), alpha
                     stimulating activity polypeptide 1; guanine nucleotide
                     regulatory protein; adenylate cyclase-stimulating G alpha
                     protein; protein ALEX; extra large alphas protein;
                     alternative gene product encoded by XL-exon"
                     /calculated_mol_wt=67817
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84996.1)"
     Region          <125..345
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          173..223
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84996.1)"
     Region          236..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84996.1)"
     Region          556..612
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84996.1)"
     CDS             1..626
                     /gene="GNAS"
                     /gene_synonym="AHO; AIMAH1; C20orf45; GNAS1; GPSA; GSA;
                     GSP; NESP; PITA3; POH; SCG6; SgVI"
                     /coded_by="NM_001309883.1:473..2353"
                     /note="isoform Alex is encoded by transcript variant 12"
                     /db_xref="GeneID:2778"
                     /db_xref="HGNC:HGNC:4392"
                     /db_xref="MIM:139320"
ORIGIN      
        1 mmarpvdpqr spdptfrsst rhsgklepme atahllrkqc psrlnspawe asglhwssld
       61 spvgsmqalr psaqhswspe psvvpdqawe dtalhqkklc plsltslpre aavnfsyrsq
      121 tllqeaqvlq gspellprsp kpsglqrlap eeatalplrr lchlslmekd lgttahprgf
      181 pelshkstaa assrqsrprv rsaslpprtr lpsgsqapsa ahpkrlsdll ltsraaapgw
      241 rspdprsrla applgsttlp stwtapqsrl tarpsrspep qireseqrdp qlrrkqqrwk
      301 eplmprreek yplrgtdplp pgqpqriplp gqplqpqpil tpgqpqkipt pgqhqpiltp
      361 ghsqpiptpg qplppqpipt pgrpltpqpi ptpgrpltpq piqmpgrplr lppplrllrp
      421 gqpmspqlrq tqglplpqpl lppgqpksag rplqplppgp darsisdppa prsrlpirll
      481 rgllarlpgg aspraaaaaa cttmkgwpaa tmtpaetspt mgppdasagf sigeiaaaes
      541 psatysatfs ckpsgaasvd lrvpspkpra lsrsrrypwr rsadrcakkp wrsgprsaqr
      601 rnavssstnn srtkrwatcv rtaccf
//
LOCUS       NP_001356015             382 aa            linear   PRI 20-NOV-2025
DEFINITION  activating signal cointegrator 1 complex subunit 1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001356015 XP_024303799
VERSION     NP_001356015.1
DBSOURCE    REFSEQ: accession NM_001369086.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 382)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 382)
  AUTHORS   Chinnam,N.B., Thapar,R., Arvai,A.S., Sarker,A.H., Soll,J.M.,
            Paul,T., Syed,A., Rosenberg,D.J., Hammel,M., Bacolla,A.,
            Katsonis,P., Asthana,A., Tsai,M.S., Ivanov,I., Lichtarge,O.,
            Silverman,R.H., Mosammaparast,N., Tsutakawa,S.E. and Tainer,J.A.
  TITLE     ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase
  JOURNAL   J Biol Chem 300 (6), 107368 (2024)
   PUBMED   38750793
  REMARK    GeneRIF: ASCC1 structures and bioinformatics reveal a novel
            helix-clasp-helix RNA-binding motif linked to a two-histidine
            phosphodiesterase.
REFERENCE   3  (residues 1 to 382)
  AUTHORS   Sharova,M., Guseva,D., Kurenkov,A., Novoselova,O., Murtazina,A. and
            Skoblov,M.
  TITLE     Congenital myopathy as a new phenotype caused by two undescribed
            variants in ASCC1 gene
  JOURNAL   Am J Med Genet A 188 (10), 3100-3105 (2022)
   PUBMED   35838082
  REMARK    GeneRIF: Congenital myopathy as a new phenotype caused by two
            undescribed variants in ASCC1 gene.
REFERENCE   4  (residues 1 to 382)
  AUTHORS   Meunier,J., Villar-Quiles,R.N., Duband-Goulet,I. and Ferreiro,A.
  TITLE     Inherited Defects of the ASC-1 Complex in Congenital Neuromuscular
            Diseases
  JOURNAL   Int J Mol Sci 22 (11), 6039 (2021)
   PUBMED   34204919
  REMARK    GeneRIF: Inherited Defects of the ASC-1 Complex in Congenital
            Neuromuscular Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 382)
  AUTHORS   Knierim,E., Hirata,H., Wolf,N.I., Morales-Gonzalez,S.,
            Schottmann,G., Tanaka,Y., Rudnik-Schoneborn,S., Orgeur,M.,
            Zerres,K., Vogt,S., van Riesen,A., Gill,E., Seifert,F., Zwirner,A.,
            Kirschner,J., Goebel,H.H., Hubner,C., Stricker,S., Meierhofer,D.,
            Stenzel,W. and Schuelke,M.
  TITLE     Mutations in Subunits of the Activating Signal Cointegrator 1
            Complex Are Associated with Prenatal Spinal Muscular Atrophy and
            Congenital Bone Fractures
  JOURNAL   Am J Hum Genet 98 (3), 473-489 (2016)
   PUBMED   26924529
REFERENCE   6  (residues 1 to 382)
  AUTHORS   Torices,S., Alvarez-Rodriguez,L., Grande,L., Varela,I., Munoz,P.,
            Pascual,D., Balsa,A., Lopez-Hoyos,M., Martinez-Taboada,V. and
            Fernandez-Luna,J.L.
  TITLE     A Truncated Variant of ASCC1, a Novel Inhibitor of NF-kappaB, Is
            Associated with Disease Severity in Patients with Rheumatoid
            Arthritis
  JOURNAL   J Immunol 195 (11), 5415-5420 (2015)
   PUBMED   26503956
  REMARK    GeneRIF: ASCC1 inhibits NF-kappaB activation and a truncated and
            inactive variant of ASCC1 is associated with a more severe disease,
            which could have clinical value for assessing the progression and
            prognosis of Rheumatoid Arthritis.
REFERENCE   7  (residues 1 to 382)
  AUTHORS   Orloff,M., Peterson,C., He,X., Ganapathi,S., Heald,B., Yang,Y.R.,
            Bebek,G., Romigh,T., Song,J.H., Wu,W., David,S., Cheng,Y.,
            Meltzer,S.J. and Eng,C.
  TITLE     Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with
            Barrett esophagus and esophageal adenocarcinoma
  JOURNAL   JAMA 306 (4), 410-419 (2011)
   PUBMED   21791690
  REMARK    GeneRIF: Three major genes, MSR1, ASCC1, and CTHRC1 were associated
            with Barrett esophagus/esophageal adenocarcinoma
REFERENCE   8  (residues 1 to 382)
  AUTHORS   Almeida-Vega,S., Catlow,K., Kenny,S., Dimaline,R. and Varro,A.
  TITLE     Gastrin activates paracrine networks leading to induction of PAI-2
            via MAZ and ASC-1
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 296 (2), G414-G423 (2009)
   PUBMED   19074642
  REMARK    GeneRIF: Gastrin activates paracrine networks leading to induction
            of PAI-2 via MAZ and ASC-1.
REFERENCE   9  (residues 1 to 382)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 382)
  AUTHORS   Jung,D.J., Sung,H.S., Goo,Y.W., Lee,H.M., Park,O.K., Jung,S.Y.,
            Lim,J., Kim,H.J., Lee,S.K., Kim,T.S., Lee,J.W. and Lee,Y.C.
  TITLE     Novel transcription coactivator complex containing activating
            signal cointegrator 1
  JOURNAL   Mol Cell Biol 22 (14), 5203-5211 (2002)
   PUBMED   12077347
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL607035.12 and AC022392.5.
            
            On Mar 18, 2019 this sequence version replaced XP_024303799.1.
            
            Summary: This gene encodes a subunit of the activating signal
            cointegrator 1 (ASC-1) complex. The ASC-1 complex is a
            transcriptional coactivator that plays an important role in gene
            transactivation by multiple transcription factors including
            activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and
            serum response factor (SRF). The encoded protein contains an
            N-terminal KH-type RNA-binding motif which is required for AP-1
            transactivation by the ASC-1 complex. Mutations in this gene are
            associated with Barrett esophagus and esophageal adenocarcinoma.
            Alternatively spliced transcripts encoding multiple isoforms have
            been observed for this gene. [provided by RefSeq, Dec 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.607928.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..382
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.1"
     Protein         1..382
                     /product="activating signal cointegrator 1 complex subunit
                     1 isoform 4"
                     /note="ASC-1 complex subunit P50; trip4 complex subunit
                     p50"
                     /calculated_mol_wt=43302
     Region          81..146
                     /region_name="KH-I_ASCC1"
                     /note="type I K homology (KH) RNA-binding domain found in
                     activating signal cointegrator 1 complex subunit 1 (ASCC1)
                     and similar proteins; cd22419"
                     /db_xref="CDD:411847"
     Site            order(90,92..94,96..100,103..104,107..108,113..116)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:411847"
     Region          155..343
                     /region_name="AKAP7_NLS"
                     /note="AKAP7 2'5' RNA ligase-like domain; pfam10469"
                     /db_xref="CDD:402204"
     CDS             1..382
                     /gene="ASCC1"
                     /gene_synonym="ASC1p50; CGI-18; p50; SMABF2"
                     /coded_by="NM_001369086.1:282..1430"
                     /note="isoform 4 is encoded by transcript variant 7"
                     /db_xref="GeneID:51008"
                     /db_xref="HGNC:HGNC:24268"
                     /db_xref="MIM:614215"
ORIGIN      
        1 mmkypgtwpc qgiigisfge svmevlrpql iridgrnyrk npvqeqtyqh eedeedfyqg
       61 smecadepcd ayeveqtpqg frstlrapsl lykhivgkrg dtrkkiemet ktsisipkpg
      121 qdgeivitgq hrngvisart ridvlldtfr rkqpfthfla fflnevevqe gflrfqeevl
      181 akcsmdhgvd ssifqnpkkl hltigmlvll seeeiqqtce mlqqckeefi ndisggkple
      241 vemagieymn ddpgmvdvly akvhmkdgsn rlqelvdrvl erfqasgliv kewnsvklha
      301 tvmntlfrkd pnaegrynly taegkyifke resfdgrnil ksfallprle yndaisahcn
      361 lclpgssdsp asasqvagit vv
//
LOCUS       NP_036406                117 aa            linear   PRI 20-NOV-2025
DEFINITION  huntingtin-interacting protein M [Homo sapiens].
ACCESSION   NP_036406 XP_048235 XP_941457
VERSION     NP_036406.1
DBSOURCE    REFSEQ: accession NM_012274.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Seal,R.L., Denny,P., Bruford,E.A., Gribkova,A.K., Landsman,D.,
            Marzluff,W.F., McAndrews,M., Panchenko,A.R., Shaytan,A.K. and
            Talbert,P.B.
  TITLE     A standardized nomenclature for mammalian histone genes
  JOURNAL   Epigenetics Chromatin 15 (1), 34 (2022)
   PUBMED   36180920
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Molaro,A., Young,J.M. and Malik,H.S.
  TITLE     Evolutionary origins and diversification of testis-specific short
            histone H2A variants in mammals
  JOURNAL   Genome Res 28 (4), 460-473 (2018)
   PUBMED   29549088
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Suter,B., Fontaine,J.F., Yildirimman,R., Rasko,T., Schaefer,M.H.,
            Rasche,A., Porras,P., Vazquez-Alvarez,B.M., Russ,J., Rau,K.,
            Foulle,R., Zenkner,M., Saar,K., Herwig,R., Andrade-Navarro,M.A. and
            Wanker,E.E.
  TITLE     Development and application of a DNA microarray-based yeast
            two-hybrid system
  JOURNAL   Nucleic Acids Res 41 (3), 1496-1507 (2013)
   PUBMED   23275563
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL121578.1, AF049615.1 and AW291697.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jul 5, 2007 this sequence version replaced
            XP_048235.3, XP_941457.2.
            
            Summary: This gene encodes a protein shown to interact with
            huntingtin, which contains an expanded polyglutamine tract in
            individuals with Huntington's disease (PMID: 9700202). [provided by
            RefSeq, Aug 2011].
            
            ##Evidence-Data-START##
            Transcript is intronless :: AF049615.1, BC104429.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341016.5/ ENSP00000339511.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..117
                     /product="huntingtin-interacting protein M"
                     /note="huntingtin yeast partner M; huntingtin interacting
                     protein M; histone H2A.P"
                     /calculated_mol_wt=13310
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75409.2)"
     Region          71..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75409.2)"
     CDS             1..117
                     /gene="H2AP"
                     /gene_synonym="CXorf27; HIP17; HYPM"
                     /coded_by="NM_012274.2:62..415"
                     /db_xref="CCDS:CCDS43929.1"
                     /db_xref="GeneID:25763"
                     /db_xref="HGNC:HGNC:18417"
ORIGIN      
        1 msekknckns stnnnqtqdp srnelqvprs fvdrvvqder dvqsqsssti ntlltlldcl
       61 adyimervgl easnngsmrn tsqdrerevd nnrephsaes dvtrflfdem pksrknd
//
LOCUS       NP_872347                168 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 31 [Homo sapiens].
ACCESSION   NP_872347
VERSION     NP_872347.2
DBSOURCE    REFSEQ: accession NM_182541.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 168)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 168)
  AUTHORS   Li,J., Zou,X., Li,C., Zhong,J., Chen,Y., Zhang,X., Qi,F., Li,M.,
            Cai,Z. and Tang,A.
  TITLE     Expression of novel cancer/testis antigen TMEM31 increases during
            metastatic melanoma progression
  JOURNAL   Oncol Lett 13 (4), 2269-2273 (2017)
   PUBMED   28454390
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK130867.1.
            
            On Nov 15, 2004 this sequence version replaced NP_872347.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005598.1, AK130867.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319560.7/ ENSP00000316940.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.2"
     Protein         1..168
                     /product="transmembrane protein 31"
                     /note="testicular secretory protein Li 58"
                     /calculated_mol_wt=19682
     Region          1..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JXX7.1)"
     Region          <4..>86
                     /region_name="Pneumo_att_G"
                     /note="Pneumovirinae attachment membrane glycoprotein G;
                     pfam05539"
                     /db_xref="CDD:114270"
     Site            119..139
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JXX7.1)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5JXX7.1)"
     CDS             1..168
                     /gene="TMEM31"
                     /coded_by="NM_182541.2:192..698"
                     /db_xref="CCDS:CCDS35359.1"
                     /db_xref="GeneID:203562"
                     /db_xref="HGNC:HGNC:28601"
                     /db_xref="MIM:301102"
ORIGIN      
        1 mrlteksege qqlkpnnsna pnedqeeeiq qseqhtparq rtqradtqps rcrlpsrrtp
       61 ttssdrtinl levlpwptew ifnpyrlpal felypefllv fkeafhdish clkaqmekig
      121 lpiilhlfal stlyfykffl ptilslsffi llvlllllfi ivfiliff
//
LOCUS       NP_001304876             224 aa            linear   PRI 20-NOV-2025
DEFINITION  rRNA methyltransferase 3, mitochondrial isoform 2 [Homo sapiens].
ACCESSION   NP_001304876 XP_006721616
VERSION     NP_001304876.1
DBSOURCE    REFSEQ: accession NM_001317947.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Nguyen,T.G., Ritter,C. and Kummer,E.
  TITLE     Structural insights into the role of GTPBP10 in the RNA maturation
            of the mitoribosome
  JOURNAL   Nat Commun 14 (1), 7991 (2023)
   PUBMED   38042949
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Rebelo-Guiomar,P., Pellegrino,S., Dent,K.C., Sas-Chen,A.,
            Miller-Fleming,L., Garone,C., Van Haute,L., Rogan,J.F., Dinan,A.,
            Firth,A.E., Andrews,B., Whitworth,A.J., Schwartz,S., Warren,A.J.
            and Minczuk,M.
  TITLE     A late-stage assembly checkpoint of the human mitochondrial
            ribosome large subunit
  JOURNAL   Nat Commun 13 (1), 929 (2022)
   PUBMED   35177605
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Chen,Z., Wang,C., Feng,X., Nie,L., Tang,M., Zhang,H., Xiong,Y.,
            Swisher,S.K., Srivastava,M. and Chen,J.
  TITLE     Interactomes of SARS-CoV-2 and human coronaviruses reveal host
            factors potentially affecting pathogenesis
  JOURNAL   EMBO J 40 (17), e107776 (2021)
   PUBMED   34232536
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Lee,K.W. and Bogenhagen,D.F.
  TITLE     Assignment of 2'-O-methyltransferases to modification sites on the
            mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA)
  JOURNAL   J Biol Chem 289 (36), 24936-24942 (2014)
   PUBMED   25074936
  REMARK    GeneRIF: Data show that 2'-O-methyltransferases MRM1, MRM2, and
            RNMTL1 are responsible for modification of large subunit rRNA at
            residues G1145, U1369, and G1370, respectively.
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Rorbach,J., Boesch,P., Gammage,P.A., Nicholls,T.J., Pearce,S.F.,
            Patel,D., Hauser,A., Perocchi,F. and Minczuk,M.
  TITLE     MRM2 and MRM3 are involved in biogenesis of the large subunit of
            the mitochondrial ribosome
  JOURNAL   Mol Biol Cell 25 (17), 2542-2555 (2014)
   PUBMED   25009282
  REMARK    GeneRIF: MRM2 and MRM3 are human mitochondrial methyltransferases
            involved in the modification of 16S rRNA and are important factors
            for the biogenesis and function of the large subunit of the
            mitochondrial ribosome.
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Lee,K.W., Okot-Kotber,C., LaComb,J.F. and Bogenhagen,D.F.
  TITLE     Mitochondrial ribosomal RNA (rRNA) methyltransferase family members
            are positioned to modify nascent rRNA in foci near the
            mitochondrial DNA nucleoid
  JOURNAL   J Biol Chem 288 (43), 31386-31399 (2013)
   PUBMED   24036117
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Xu,J., De Zhu,J., Ni,M., Wan,F. and Gu,J.R.
  TITLE     The ATF/CREB site is the key element for transcription of the human
            RNA methyltransferase like 1(RNMTL1) gene, a newly discovered
            17p13.3 gene
  JOURNAL   Cell Res 12 (3-4), 177-197 (2002)
   PUBMED   12296377
  REMARK    GeneRIF: The ATF/CREB site is the key element for transcription of
            this protein found on human chromosome 17.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF177344.2, BI830018.1 and
            AK222900.1.
            
            On Dec 16, 2015 this sequence version replaced XP_006721616.1.
            
            Summary: Efficient translation of mitochondrial-derived transcripts
            requires proper assembly of the large subunit of the mitochondrial
            ribosome. Central to the biogenesis of this large subunit is the
            A-loop of mitochondrial 16S rRNA, which is modified by three rRNA
            methyltransferases located near mtDNA nucleoids. The protein
            encoded by this gene methylates G(1370) of 16S rRNA, and this
            modification is necessary for proper ribosomal large subnit
            assembly. Two transcript variants encoding different isoforms have
            been found for this gene. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (2) lacks an alternate internal
            exon compared to variant 1. The resulting isoform (2) is shorter at
            the N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138524.982875.1, DRR138528.3124.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.3"
     Protein         1..224
                     /product="rRNA methyltransferase 3, mitochondrial isoform
                     2"
                     /EC_number="2.1.1.-"
                     /note="putative RNA methyltransferase; RNA
                     methyltransferase-like protein 1; 16S rRNA [Gm1370]
                     2'-O-methyltransferase; 16S rRNA
                     (guanosine(1370)-2'-O)-methyltransferase; rRNA
                     methyltransferase 3, mitochondrial; RNA methyltransferase
                     like 1"
                     /calculated_mol_wt=24587
     Region          14..206
                     /region_name="SpoU-like_RNMTL1"
                     /note="SAM-dependent rRNA methylase related to RNMTL1;
                     cd18106"
                     /db_xref="CDD:349979"
     Site            order(29,32..33,35..38,146..147,184..187,191..194,197,
                     200..201,204..205)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:349979"
     Site            order(91,93,159..162,165,183..184,186,192..193,195,198)
                     /site_type="other"
                     /note="putative SAM binding site [chemical binding]"
                     /db_xref="CDD:349979"
     CDS             1..224
                     /gene="MRM3"
                     /gene_synonym="RMTL1; RNMTL1"
                     /coded_by="NM_001317947.2:370..1044"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55178"
                     /db_xref="HGNC:HGNC:18485"
                     /db_xref="MIM:612600"
ORIGIN      
        1 mtypktqlqh slplllicdn lrdpgnlgti lrsaagagcs kvlltkgcvd awepkvlrag
       61 mgahfrmpii nnlewetvpn ylppdtrvyv adncglyaqa emsnkasdhg wvcdqrvmkf
      121 hkyeeeedve tgasqdwlph vevqsydsdw teapaavvig getygvsles lqlaestggk
      181 rllipvvpgv dslnsamaas illfegkrql rgraedlsrd rsyh
//
LOCUS       NP_001244062              57 aa            linear   PRI 20-NOV-2025
DEFINITION  cytochrome c oxidase assembly protein COX14 [Homo sapiens].
ACCESSION   NP_001244062
VERSION     NP_001244062.1
DBSOURCE    REFSEQ: accession NM_001257133.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 57)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 57)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 57)
  AUTHORS   Bourens,M. and Barrientos,A.
  TITLE     A CMC1-knockout reveals translation-independent control of human
            mitochondrial complex IV biogenesis
  JOURNAL   EMBO Rep 18 (3), 477-494 (2017)
   PUBMED   28082314
REFERENCE   4  (residues 1 to 57)
  AUTHORS   Richter-Dennerlein,R., Oeljeklaus,S., Lorenzi,I., Ronsor,C.,
            Bareth,B., Schendzielorz,A.B., Wang,C., Warscheid,B., Rehling,P.
            and Dennerlein,S.
  TITLE     Mitochondrial Protein Synthesis Adapts to Influx of Nuclear-Encoded
            Protein
  JOURNAL   Cell 167 (2), 471-483 (2016)
   PUBMED   27693358
REFERENCE   5  (residues 1 to 57)
  AUTHORS   Lee,S.Y., Kang,M.G., Park,J.S., Lee,G., Ting,A.Y. and Rhee,H.W.
  TITLE     APEX Fingerprinting Reveals the Subcellular Localization of
            Proteins of Interest
  JOURNAL   Cell Rep 15 (8), 1837-1847 (2016)
   PUBMED   27184847
REFERENCE   6  (residues 1 to 57)
  AUTHORS   Ostergaard,E., Weraarpachai,W., Ravn,K., Born,A.P., Jonson,L.,
            Duno,M., Wibrand,F., Shoubridge,E.A. and Vissing,J.
  TITLE     Mutations in COA3 cause isolated complex IV deficiency associated
            with neuropathy, exercise intolerance, obesity, and short stature
  JOURNAL   J Med Genet 52 (3), 203-207 (2015)
   PUBMED   25604084
  REMARK    GeneRIF: COX14 was undetectable in COA3 subject fibroblasts, and
            that COA3 was undetectable in fibroblasts from a COX14 subject,
            demonstrating the interdependence of these two COX assembly factors
REFERENCE   7  (residues 1 to 57)
  AUTHORS   Lai,Y., Yu,Z., Wang,Y. and Ye,J.
  TITLE     Identification of PCAG1 as a novel prostate cancer-associated gene
  JOURNAL   Mol Med Rep 7 (3), 755-760 (2013)
   PUBMED   23292432
  REMARK    GeneRIF: While PCAG1 mRNA was highly expressed in prostate cancer
            tissues, it was almost absent in all common normal tissues and
            paired adjacent normal prostate tissues.
REFERENCE   8  (residues 1 to 57)
  AUTHORS   Szklarczyk,R., Wanschers,B.F., Cuypers,T.D., Esseling,J.J.,
            Riemersma,M., van den Brand,M.A., Gloerich,J., Lasonder,E., van den
            Heuvel,L.P., Nijtmans,L.G. and Huynen,M.A.
  TITLE     Iterative orthology prediction uncovers new mitochondrial proteins
            and identifies C12orf62 as the human ortholog of COX14, a protein
            involved in the assembly of cytochrome c oxidase
  JOURNAL   Genome Biol 13 (2), R12 (2012)
   PUBMED   22356826
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 57)
  AUTHORS   Weraarpachai,W., Sasarman,F., Nishimura,T., Antonicka,H., Aure,K.,
            Rotig,A., Lombes,A. and Shoubridge,E.A.
  TITLE     Mutations in C12orf62, a factor that couples COX I synthesis with
            cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis
  JOURNAL   Am J Hum Genet 90 (1), 142-151 (2012)
   PUBMED   22243966
REFERENCE   10 (residues 1 to 57)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DW418935.1 and AI208662.1.
            
            Summary: This gene encodes a small single-pass transmembrane
            protein that localizes to mitochondria. This protein may play a
            role in coordinating the early steps of cytochrome c oxidase (COX;
            also known as complex IV) subunit assembly and, in particular, the
            synthesis and assembly of the COX I subunit of the holoenzyme.
            Mutations in this gene have been associated with mitochondrial
            complex IV deficiency. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (2) has an additional exon in the
            5' UTR, compared to variant 1. Variants 1-3 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AA180788.1, SRR1163657.71411.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 22356826, 22243966;
                                                  reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..57
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..57
                     /product="cytochrome c oxidase assembly protein COX14"
                     /note="COX14 cytochrome c oxidase assembly homolog;
                     cytochrome c oxidase assembly homolog 14; COX14,
                     cytochrome c oxidase assembly factor"
                     /calculated_mol_wt=6468
     Region          1..57
                     /region_name="COX14"
                     /note="Cytochrome oxidase c assembly; pfam14880"
                     /db_xref="CDD:434280"
     Site            15..37
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96I36.1)"
     CDS             1..57
                     /gene="COX14"
                     /gene_synonym="C12orf62; MC4DN10; PCAG1"
                     /coded_by="NM_001257133.2:135..308"
                     /db_xref="CCDS:CCDS8800.1"
                     /db_xref="GeneID:84987"
                     /db_xref="HGNC:HGNC:28216"
                     /db_xref="MIM:614478"
ORIGIN      
        1 mptgkqladi gyktfstsmm lltvyggylc svrvyhyfqw rraqrqaaee qktsgim
//
LOCUS       NP_001164191             722 aa            linear   PRI 20-NOV-2025
DEFINITION  breast cancer anti-estrogen resistance protein 1 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001164191
VERSION     NP_001164191.1
DBSOURCE    REFSEQ: accession NM_001170720.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Delage,L., Lambert,M., Bardel,E., Kundlacz,C., Chartoire,D.,
            Conchon,A., Peugnet,A.L., Gorka,L., Auberger,P., Jacquel,A.,
            Soussain,C., Destaing,O., Delecluse,H.J., Delecluse,S., Merabet,S.,
            Traverse-Glehen,A., Salles,G., Bachy,E., Billaud,M.,
            Ghesquieres,H., Genestier,L., Rouault,J.P. and Sujobert,P.
  TITLE     BTG1 inactivation drives lymphomagenesis and promotes lymphoma
            dissemination through activation of BCAR1
  JOURNAL   Blood 141 (10), 1209-1220 (2023)
   PUBMED   36375119
  REMARK    GeneRIF: BTG1 inactivation drives lymphomagenesis and promotes
            lymphoma dissemination through activation of BCAR1.
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Li,H., Li,L., Qiu,X., Zhang,J. and Hua,Z.
  TITLE     The interaction of CFLAR with p130Cas promotes cell migration
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (2), 119390 (2023)
   PUBMED   36400248
  REMARK    GeneRIF: The interaction of CFLAR with p130Cas promotes cell
            migration.
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Camacho Leal Mdel,P., Sciortino,M., Tornillo,G., Colombo,S.,
            Defilippi,P. and Cabodi,S.
  TITLE     p130Cas/BCAR1 scaffold protein in tissue homeostasis and
            pathogenesis
  JOURNAL   Gene 562 (1), 1-7 (2015)
   PUBMED   25727852
  REMARK    GeneRIF: BCAR1 has a pivotal role in the regulation of tissue
            homeostasis in pathological conditions such as cancer. (Review)
            Review article
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Nikonova,A.S., Gaponova,A.V., Kudinov,A.E. and Golemis,E.A.
  TITLE     CAS proteins in health and disease: an update
  JOURNAL   IUBMB Life 66 (6), 387-395 (2014)
   PUBMED   24962474
  REMARK    Review article
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Barrett,A., Pellet-Many,C., Zachary,I.C., Evans,I.M. and Frankel,P.
  TITLE     p130Cas: a key signalling node in health and disease
  JOURNAL   Cell Signal 25 (4), 766-777 (2013)
   PUBMED   23277200
  REMARK    Review article
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Brinkman,A., van der Flier,S., Kok,E.M. and Dorssers,L.C.
  TITLE     BCAR1, a human homologue of the adapter protein p130Cas, and
            antiestrogen resistance in breast cancer cells
  JOURNAL   J Natl Cancer Inst 92 (2), 112-120 (2000)
   PUBMED   10639512
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Vuori,K., Hirai,H., Aizawa,S. and Ruoslahti,E.
  TITLE     Introduction of p130cas signaling complex formation upon
            integrin-mediated cell adhesion: a role for Src family kinases
  JOURNAL   Mol Cell Biol 16 (6), 2606-2613 (1996)
   PUBMED   8649368
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Sakai,R., Iwamatsu,A., Hirano,N., Ogawa,S., Tanaka,T., Mano,H.,
            Yazaki,Y. and Hirai,H.
  TITLE     A novel signaling molecule, p130, forms stable complexes in vivo
            with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
  JOURNAL   EMBO J 13 (16), 3748-3756 (1994)
   PUBMED   8070403
REFERENCE   10 (residues 1 to 722)
  AUTHORS   Dorssers,L.C., van Agthoven,T., Dekker,A., van Agthoven,T.L. and
            Kok,E.M.
  TITLE     Induction of antiestrogen resistance in human breast cancer cells
            by random insertional mutagenesis using defective retroviruses:
            identification of bcar-1, a common integration site
  JOURNAL   Mol Endocrinol 7 (7), 870-878 (1993)
   PUBMED   8413311
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA184411.1, AK302617.1,
            AB040024.1, BU730553.1, AC009078.6 and BQ016861.1.
            
            Summary: The protein encoded by this gene is a member of the
            Crk-associated substrate (CAS) family of scaffold proteins,
            characterized by the presence of multiple protein-protein
            interaction domains and many serine and tyrosine phosphorylation
            sites. The encoded protein contains a Src-homology 3 (SH3) domain,
            a proline-rich domain, a substrate domain which contains 15 repeat
            of the YxxP consensus phosphorylation motif for Src family kinases,
            a serine-rich domain, and a bipartite Src-binding domain, which can
            bind both SH2 and SH3 domains. This adaptor protein functions in
            multiple cellular pathways, including in cell motility, apoptosis
            and cell cycle control. Dysregulation of this gene can have a wide
            range of effects, affecting different pathways, including cardiac
            development, vascular smooth muscle cells, liver and kidney
            function, endothelial migration, and cancer. [provided by RefSeq,
            Sep 2017].
            
            Transcript Variant: This variant (8) has an alternate internal
            sequence, as compared to variant 1. The resulting isoform (8) is
            shorter and has a different N-terminus, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.1"
     Protein         1..722
                     /product="breast cancer anti-estrogen resistance protein 1
                     isoform 8"
                     /note="Cas scaffolding protein family member 1;
                     Crk-associated substrate p130Cas; breast cancer
                     anti-estrogen resistance protein 1; BCAR1, Cas family
                     scaffolding protein; BCAR1, Cas family scaffold protein"
                     /calculated_mol_wt=77600
     Region          5..64
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(12,14,17,21,42..43,56,58..59)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212934"
     Region          <112..142
                     /region_name="ALP_like"
                     /note="alkaline phosphatases and sulfatases; cl23718"
                     /db_xref="CDD:474031"
     Region          306..462
                     /region_name="Serine_rich_CAS"
                     /note="Serine rich Four helix bundle domain of CAS
                     (Crk-Associated Substrate) scaffolding proteins; a protein
                     interaction module; cl07433"
                     /db_xref="CDD:471673"
     Region          506..716
                     /region_name="CAS_C"
                     /note="Crk-Associated Substrate C-terminal domain;
                     pfam12026"
                     /db_xref="CDD:463437"
     CDS             1..722
                     /gene="BCAR1"
                     /gene_synonym="CAS; CAS1; CASS1; CRKAS; P130Cas"
                     /coded_by="NM_001170720.3:336..2504"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS54039.1"
                     /db_xref="GeneID:9564"
                     /db_xref="HGNC:HGNC:971"
                     /db_xref="MIM:602941"
ORIGIN      
        1 mqgknvlaka lydnvaespd elsfrkgdim tvleqdtqgl dgwwlcslhg rqgivpgnrl
       61 kilvvvptrv gqgyvyeaaq peqdeydipr hllapgpqdi ydvppvrgll psqygqevyd
      121 tppmavkgpn grdpllevyd vppsvekglp psnhhavydv ppsvskdvpd gpllreetyd
      181 vppafakakp fdpartplvl aapppdsppa edvydvpppa pdlydvppgl rrpgpgtlyd
      241 vprervlppe vadggvvdsg vyavpppaer eapaegkrls asstgstrss qsasslevag
      301 pgreplelev avealarlqq gvsatvahll dlagsagatg swrspsepqe plvqdlqaav
      361 aavqsavhel lefarsavgn aahtsdralh aklsrqlqkm edvhqtlvah gqaldagrgg
      421 sgatledldr lvacsravpe dakqlasflh gnasllfrrt katapgpegg gtlhpnptdk
      481 tssiqsrplp sppkftsqds pdgqyenseg gwmedydyvh lqgkeefekt qkellekgsi
      541 trqgksqlel qqlkqferle qevsrpidhd lanwtpaqpl apgrtgglgp sdrqlllfyl
      601 eqceanlttl tnavdaffta vatnqppkif vahskfvils ahklvfigdt lsrqakaadv
      661 rsqvthysnl lcdllrgiva ttkaaalqyp spsaaqdmve rvkelghstq qfrrvlgqla
      721 aa
//
LOCUS       NP_001271219             505 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-glucuronidase isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001271219 XP_005250355
VERSION     NP_001271219.1
DBSOURCE    REFSEQ: accession NM_001284290.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Yang,Y., Wang,Y., Wang,C., Wu,S. and Yao,D.
  TITLE     Macrophages and derived-TNF-alpha promote
            lipopolysaccharide-induced upregulation of endogenous
            beta-glucuronidase in the epithelial cells of the bile duct: A
            possible facilitator of hepatolithiasis formation
  JOURNAL   Clin Res Hepatol Gastroenterol 47 (1), 102062 (2023)
   PUBMED   36473630
  REMARK    GeneRIF: Macrophages and derived-TNF-alpha promote
            lipopolysaccharide-induced upregulation of endogenous
            beta-glucuronidase in the epithelial cells of the bile duct: A
            possible facilitator of hepatolithiasis formation.
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Kong,X., Zheng,Z., Song,G., Zhang,Z., Liu,H., Kang,J., Sun,G.,
            Sun,G., Huang,T., Li,X., Rong,D., Wang,K., Tang,W. and Xia,Y.
  TITLE     Over-Expression of GUSB Leads to Primary Resistance of Anti-PD1
            Therapy in Hepatocellular Carcinoma
  JOURNAL   Front Immunol 13, 876048 (2022)
   PUBMED   35812439
  REMARK    GeneRIF: Over-Expression of GUSB Leads to Primary Resistance of
            Anti-PD1 Therapy in Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Chojnowska,S., Ptaszynska-Sarosiek,I., Kepka,A., Szajda,S.D.,
            Waszkiewicz,N. and Zwierz,K.
  TITLE     Optimization of the method for alpha-l-fucosidase,
            beta-d-galactosidase and beta-d-glucuronidase determination in
            serum from hemolyzed blood
  JOURNAL   Adv Med Sci 63 (2), 306-311 (2018)
   PUBMED   29885630
  REMARK    GeneRIF: the beta-d-galactosidase, beta-d-glucuronidase and
            alpha-l-fucosidase activities in serums from hemolyzed blood, were
            determined.
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Fratz-Berilla,E.J., Ketcham,S.A., Parhiz,H., Ashraf,M. and
            Madhavarao,C.N.
  TITLE     An improved purification method for the lysosomal storage disease
            protein beta-glucuronidase produced in CHO cells
  JOURNAL   Protein Expr Purif 140, 28-35 (2017)
   PUBMED   28734840
  REMARK    GeneRIF: We produced GUS from a CHO cell line grown in suspension
            in a 15 L perfused bioreactor and developed a three step
            purification procedure that yields approximately 99% pure enzyme
            with a recovery of more than 40%.
REFERENCE   5  (residues 1 to 505)
  AUTHORS   Tomatsu,S., Montano,A.M., Dung,V.C., Grubb,J.H. and Sly,W.S.
  TITLE     Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis
            VII (Sly Syndrome)
  JOURNAL   Hum Mutat 30 (4), 511-519 (2009)
   PUBMED   19224584
  REMARK    GeneRIF: Study summarized information on the 49 unique,
            disease-causing mutations determined so far in the GUS gene.
            Review article
REFERENCE   6  (residues 1 to 505)
  AUTHORS   Sun,A. and Wang,R.
  TITLE     Mucopolysaccharidosis Type VII
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38190471
REFERENCE   7  (residues 1 to 505)
  AUTHORS   Wolfe,J.H., Sands,M.S., Barker,J.E., Gwynn,B., Rowe,L.B.,
            Vogler,C.A. and Birkenmeier,E.H.
  TITLE     Reversal of pathology in murine mucopolysaccharidosis type VII by
            somatic cell gene transfer
  JOURNAL   Nature 360 (6406), 749-753 (1992)
   PUBMED   1465145
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Tanaka,J., Gasa,S., Sakurada,K., Miyazaki,T., Kasai,M. and
            Makita,A.
  TITLE     Characterization of the subunits and sugar moiety of human
            placental and leukemic beta-glucuronidase
  JOURNAL   Biol Chem Hoppe Seyler 373 (1), 57-62 (1992)
   PUBMED   1311180
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Shipley,J.M., Miller,R.D., Wu,B.M., Grubb,J.H., Christensen,S.G.,
            Kyle,J.W. and Sly,W.S.
  TITLE     Analysis of the 5' flanking region of the human beta-glucuronidase
            gene
  JOURNAL   Genomics 10 (4), 1009-1018 (1991)
   PUBMED   1916806
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Bell,C.E. Jr., Sly,W.S. and Brot,F.E.
  TITLE     Human beta-glucuronidase deficiency mucopolysaccharidosis:
            identification of cross-reactive antigen in cultured fibroblasts of
            deficient patients by enzyme immunoassay
  JOURNAL   J Clin Invest 59 (1), 97-105 (1977)
   PUBMED   401508
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC346632.1, AK303819.1,
            AC073261.8 and AA947121.1.
            
            On Sep 27, 2013 this sequence version replaced XP_005250355.1.
            
            Summary: This gene encodes a hydrolase that degrades
            glycosaminoglycans, including heparan sulfate, dermatan sulfate,
            and chondroitin-4,6-sulfate. The enzyme forms a homotetramer that
            is localized to the lysosome. Mutations in this gene result in
            mucopolysaccharidosis type VII. Alternative splicing results in
            multiple transcript variants. There are many pseudogenes of this
            locus in the human genome.[provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) has multiple differences in
            the coding region but maintains the reading frame, compared to
            variant 1. This variant encodes isoform 2, which is shorter than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK303819.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2162568
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..505
                     /product="beta-glucuronidase isoform 2 precursor"
                     /EC_number="3.2.1.31"
                     /note="beta-glucuronidase; beta-D-glucuronidase; beta-G1"
                     /calculated_mol_wt=55894
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2470
     Region          27..485
                     /region_name="Bgal_small_N"
                     /note="Beta galactosidase small chain; cl46900"
                     /db_xref="CDD:481240"
     CDS             1..505
                     /gene="GUSB"
                     /gene_synonym="BG; MPS7"
                     /coded_by="NM_001284290.2:31..1548"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS64665.1"
                     /db_xref="GeneID:2990"
                     /db_xref="HGNC:HGNC:4696"
                     /db_xref="MIM:611499"
ORIGIN      
        1 margsavawa algpllwgca lglqggmlyp qespsrecke ldglwsfrad fsdnrrrgfe
       61 eqwyrrplwe sgptvdmpvp ssfndisqdw rlrhfvgwvw yerevilper wtqdlrtrvv
      121 lrigsahsya ivwvngvdtl eheggylpfe adisnlvqvq ltaqtslgpv sdfytlpvgi
      181 rtvavtksqf lingkpfyfh gvnkhedadi rgkgfdwpll vkdfnllrwl ganafrtshy
      241 pyaeevmqmc drygivvide cpgvglalpq ffnnvslhhh mqvmeevvrr dknhpavvmw
      301 svanepashl esagyylkmv iahtksldps rpvtfvsnsn yaadkgapyv dviclnsyys
      361 wyhdyghlel iqlqlatqfe nwykkyqkpi iqseygaeti agfhqdpplm fteeyqksll
      421 eqyhlgldqk rrkyvvgeli wnfadfmteq sptrvlgnkk giftrqrqpk saafllrery
      481 wkianetryp hsvaksqcle nslft
//
LOCUS       NP_037400                139 aa            linear   PRI 20-NOV-2025
DEFINITION  galactoside-binding soluble lectin 13 [Homo sapiens].
ACCESSION   NP_037400
VERSION     NP_037400.1
DBSOURCE    REFSEQ: accession NM_013268.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 139)
  AUTHORS   Zhang,H.L., Guo,Y.Q., Liu,S., Ye,Z.P., Li,L.C., Hu,B.X., Li,Z.L.,
            Chen,Y.H., Feng,G.K., Shen,H.Q., Deng,R. and Zhu,X.F.
  TITLE     Galectin-13 reduces membrane localization of SLC7A11 for
            ferroptosis propagation
  JOURNAL   Nat Chem Biol 21 (10), 1531-1543 (2025)
   PUBMED   40246981
REFERENCE   2  (residues 1 to 139)
  AUTHORS   Lestari,P.M., Wibowo,N., Prasmusinto,D., Yamin,M., Siregar,N.C.,
            Prihartono,J., Timan,I.S., Mose,J.C., Liberty,I.A., Kesty,C. and
            Stevanny,B.
  TITLE     Placental Protein 13 and Syncytiotrophoblast Basement Membrane
            Ultrastructures in Preeclampsia
  JOURNAL   Medicina (Kaunas) 60 (7), 1077 (2024)
   PUBMED   39064506
  REMARK    GeneRIF: Placental Protein 13 and Syncytiotrophoblast Basement
            Membrane Ultrastructures in Preeclampsia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 139)
  AUTHORS   Fu,J.H., Huo,J., Han,Y.M. and Chen,C.J.
  TITLE     [Predictive value of serum Gal-13, GLP-1 and VEGF levels in adverse
            pregnancy outcomes of gestational diabetes mellitus]
  JOURNAL   Zhonghua Yu Fang Yi Xue Za Zhi 57 (12), 2140-2146 (2023)
   PUBMED   38186168
  REMARK    GeneRIF: [Predictive value of serum Gal-13, GLP-1 and VEGF levels
            in adverse pregnancy outcomes of gestational diabetes mellitus].
REFERENCE   4  (residues 1 to 139)
  AUTHORS   Bhati,T., Ray,A., Arora,R., Siraj,F., Parvez,S. and Rastogi,S.
  TITLE     Intronic variants of LGALS13 gene encoding placental protein (PP13)
            are linked with increased risk of infection-associated spontaneous
            preterm birth
  JOURNAL   Am J Reprod Immunol 90 (3), e13759 (2023)
   PUBMED   37641375
  REMARK    GeneRIF: Intronic variants of LGALS13 gene encoding placental
            protein (PP13) are linked with increased risk of
            infection-associated spontaneous preterm birth.
REFERENCE   5  (residues 1 to 139)
  AUTHORS   Kazatsker,M.M., Sharabi-Nov,A., Meiri,H., Sammour,R. and Sammar,M.
  TITLE     Augmented Placental Protein 13 in Placental-Associated
            Extracellular Vesicles in Term and Preterm Preeclampsia Is Further
            Elevated by Corticosteroids
  JOURNAL   Int J Mol Sci 24 (15), 12051 (2023)
   PUBMED   37569423
  REMARK    GeneRIF: Augmented Placental Protein 13 in Placental-Associated
            Extracellular Vesicles in Term and Preterm Preeclampsia Is Further
            Elevated by Corticosteroids.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 139)
  AUTHORS   Visegrady,B., Than,N.G., Kilar,F., Sumegi,B., Than,G.N. and Bohn,H.
  TITLE     Homology modelling and molecular dynamics studies of human
            placental tissue protein 13 (galectin-13)
  JOURNAL   Protein Eng 14 (11), 875-880 (2001)
   PUBMED   11742106
  REMARK    GeneRIF: The primary structure of the newly sequence analysed
            placental tissue protein 13 (PP13) was highly homologous to several
            members of the beta-galactoside-binding S-type lectin (galectin)
            family
REFERENCE   7  (residues 1 to 139)
  AUTHORS   Than,N.G., Sumegi,B., Than,G.N., Berente,Z. and Bohn,H.
  TITLE     Isolation and sequence analysis of a cDNA encoding human placental
            tissue protein 13 (PP13), a new lysophospholipase, homologue of
            human eosinophil Charcot-Leyden Crystal protein
  JOURNAL   Placenta 20 (8), 703-710 (1999)
   PUBMED   10527825
REFERENCE   8  (residues 1 to 139)
  AUTHORS   Uhlmann,J., Wiemann,S. and Ponstingl,H.
  TITLE     DelGEF, an RCC1-related protein encoded by a gene on chromosome
            11p14 critical for two forms of hereditary deafness
  JOURNAL   FEBS Lett 460 (1), 153-160 (1999)
   PUBMED   10571079
REFERENCE   9  (residues 1 to 139)
  AUTHORS   Wang,A. and Dennis,E.A.
  TITLE     Mammalian lysophospholipases
  JOURNAL   Biochim Biophys Acta 1439 (1), 1-16 (1999)
   PUBMED   10395961
  REMARK    Review article
REFERENCE   10 (residues 1 to 139)
  AUTHORS   Bohn,H., Kraus,W. and Winckler,W.
  TITLE     Purification and characterization of two new soluble placental
            tissue proteins (PP13 and PP17)
  JOURNAL   Oncodev Biol Med 4 (5), 343-350 (1983)
   PUBMED   6856484
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005205.1.
            
            Summary: Lysophospholipases are enzymes that act on biological
            membranes to regulate the multifunctional lysophospholipids. The
            protein encoded by this gene has lysophospholipase activity. It is
            composed of two identical subunits which are held together by
            disulfide bonds. This protein has structural similarity to several
            members of the beta-galactoside-binding S-type lectin family.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066304.1, CB995660.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221797.5/ ENSP00000221797.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..139
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
     Protein         1..139
                     /product="galactoside-binding soluble lectin 13"
                     /EC_number="3.1.1.5"
                     /note="placental protein 13; beta-galactoside-binding
                     lectin; gal-13; placental tissue protein 13; lectin,
                     galactoside-binding, soluble, 13"
                     /calculated_mol_wt=15987
     Site            order(6..10,131..135)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238025"
     Site            6..10
                     /site_type="active"
                     /note="dimerization swap strand [active]"
                     /db_xref="CDD:238025"
     Region          11..135
                     /region_name="Gal-bind_lectin"
                     /note="Galactoside-binding lectin; smart00908"
                     /db_xref="CDD:214904"
     Site            order(15..17,20,23,94..96,101,103,106)
                     /site_type="other"
                     /note="putative alternate dimerization interface
                     [polypeptide binding]"
                     /db_xref="CDD:238025"
     Site            order(53,55,57,63,65,72,75,77)
                     /site_type="other"
                     /note="sugar binding pocket [chemical binding]"
                     /db_xref="CDD:238025"
     CDS             1..139
                     /gene="LGALS13"
                     /gene_synonym="GAL13; PLAC8; PP13"
                     /coded_by="NM_013268.3:46..465"
                     /db_xref="CCDS:CCDS33024.1"
                     /db_xref="GeneID:29124"
                     /db_xref="HGNC:HGNC:15449"
                     /db_xref="MIM:608717"
ORIGIN      
        1 msslpvpykl pvslsvgscv iikgtpihsf indpqlqvdf ytdmdedsdi afrfrvhfgn
       61 hvvmnrrefg iwmleettdy vpfedgkqfe lciyvhyney eikvngiriy gfvhrippsf
      121 vkmvqvsrdi sltsvcvcn
//
LOCUS       NP_001353582             529 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 2 [Homo sapiens].
ACCESSION   NP_001353582
VERSION     NP_001353582.1
DBSOURCE    REFSEQ: accession NM_001366653.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091928.3, AC011363.6 and AC008456.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK090832.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2142586,
                                           SAMEA2144335 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..529
                     /product="phospholipid-transporting ATPase VB isoform 2"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=61112
     Region          68..>455
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            83..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            111..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            317..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            369..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          429..>495
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     CDS             1..529
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001366653.2:663..2252"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 malsvdsswh rwqwrvrdgf phcpsettpl lspekgrqsy nltqqrvvfp nnsifhqdwe
       61 evsrrypgnr tcttkytlft flprnlfeqf hrwanlyflf lvilnwmpsm evfhreitml
      121 plaivlfvim ikdgmedfkr hrfdkaincs niriyerkeq tyvqkcwkdv rvgdfiqmkc
      181 neivpadill lfssdpngic hletasldge tnlkqrcvvk gfsqqevqfe pelfhntivc
      241 ekpnnhlnkf kgymehpdqt rtgfgcesll lrgctirnte mavgiviyag hetkamlnns
      301 gprykrskie rrmnidiffc igililmcli gavghsiwng tfeehppfdv pdangsflps
      361 alggfymflt miillqvlip islyvsielv klgqvfflsn dldlydeetd lsiqcralni
      421 aedlgqiqyi fsdktgtlte nkmvfrrcti mgseyshqen gieapkgsip lskrkypall
      481 rneeikdill alleavwhfh kllpvslwss lsqiravpit cklsfvykg
//
LOCUS       NP_006561                313 aa            linear   PRI 20-NOV-2025
DEFINITION  ras-related GTP-binding protein A [Homo sapiens].
ACCESSION   NP_006561
VERSION     NP_006561.1
DBSOURCE    REFSEQ: accession NM_006570.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Jiang,C., Liu,J., He,S., Xu,W., Huang,R., Pan,W., Li,X., Dai,X.,
            Guo,J., Zhang,T., Inuzuka,H., Wang,P., Asara,J.M., Xiao,J. and
            Wei,W.
  TITLE     PRMT1 orchestrates with SAMTOR to govern mTORC1 methionine sensing
            via Arg-methylation of NPRL2
  JOURNAL   Cell Metab 35 (12), 2183-2199 (2023)
   PUBMED   38006878
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Zhang,L., Yu,J., Zheng,M., Zhen,H., Xie,Q., Zhang,C., Zhou,Z. and
            Jin,G.
  TITLE     RAGA prevents tumor immune evasion of LUAD by promoting CD47
            lysosome degradation
  JOURNAL   Commun Biol 6 (1), 211 (2023)
   PUBMED   36823443
  REMARK    GeneRIF: RAGA prevents tumor immune evasion of LUAD by promoting
            CD47 lysosome degradation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Cui,Z., Napolitano,G., de Araujo,M.E.G., Esposito,A.,
            Monfregola,J., Huber,L.A., Ballabio,A. and Hurley,J.H.
  TITLE     Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator megacomplex
  JOURNAL   Nature 614 (7948), 572-579 (2023)
   PUBMED   36697823
  REMARK    GeneRIF: Structure of the lysosomal mTORC1-TFEB-Rag-Ragulator
            megacomplex.
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Hirose,E., Nakashima,N., Sekiguchi,T. and Nishimoto,T.
  TITLE     RagA is a functional homologue of S. cerevisiae Gtr1p involved in
            the Ran/Gsp1-GTPase pathway
  JOURNAL   J Cell Sci 111 (Pt 1), 11-21 (1998)
   PUBMED   9394008
REFERENCE   7  (residues 1 to 313)
  AUTHORS   Li,Y., Kang,J. and Horwitz,M.S.
  TITLE     Interaction of an adenovirus 14.7-kilodalton protein inhibitor of
            tumor necrosis factor alpha cytolysis with a new member of the
            GTPase superfamily of signal transducers
  JOURNAL   J Virol 71 (2), 1576-1582 (1997)
   PUBMED   8995684
REFERENCE   8  (residues 1 to 313)
  AUTHORS   Vladimirov,S.N., Ivanov,A.V., Karpova,G.G., Musolyamov,A.K.,
            Egorov,T.A., Thiede,B., Wittmann-Liebold,B. and Otto,A.
  TITLE     Characterization of the human small-ribosomal-subunit proteins by
            N-terminal and internal sequencing, and mass spectrometry
  JOURNAL   Eur J Biochem 239 (1), 144-149 (1996)
   PUBMED   8706699
REFERENCE   9  (residues 1 to 313)
  AUTHORS   Schurmann,A., Brauers,A., Massmann,S., Becker,W. and Joost,H.G.
  TITLE     Cloning of a novel family of mammalian GTP-binding proteins (RagA,
            RagBs, RagB1) with remote similarity to the Ras-related GTPases
  JOURNAL   J Biol Chem 270 (48), 28982-28988 (1995)
   PUBMED   7499430
REFERENCE   10 (residues 1 to 313)
  AUTHORS   Grove,J.R., Banerjee,P., Balasubramanyam,A., Coffer,P.J.,
            Price,D.J., Avruch,J. and Woodgett,J.R.
  TITLE     Cloning and expression of two human p70 S6 kinase polypeptides
            differing only at their amino termini
  JOURNAL   Mol Cell Biol 11 (11), 5541-5550 (1991)
   PUBMED   1922062
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC009990.2 and BX346838.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR3476690.413698.1,
                                        SRR1660803.162941.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380527.3/ ENSP00000369899.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p22.1"
     Protein         1..313
                     /product="ras-related GTP-binding protein A"
                     /note="adenovirus E3-14.7K interacting protein 1; rag A;
                     adenovirus E3 14.7 kDa-interacting protein 1"
                     /calculated_mol_wt=36435
     Region          9..292
                     /region_name="RagA_like"
                     /note="Rag GTPase, subfamily of Ras-related GTPases,
                     includes Ras-related GTP-binding proteins A and B;
                     cd11384"
                     /db_xref="CDD:206744"
     Site            14..21
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206744"
     Site            order(19..22,65,127..128,130,163..165)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206744"
     Site            42
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206744"
     Site            46..48
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206744"
     Site            62..65
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206744"
     Site            order(64..65,86..87)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206744"
     Site            127..130
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206744"
     Site            163..165
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206744"
     Site            order(202,204,227,230..231,234..235,238,241..242,244,
                     247..254,261,273)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:206744"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q7L523.1)"
     CDS             1..313
                     /gene="RRAGA"
                     /gene_synonym="FIP-1; FIP1; RAGA"
                     /coded_by="NM_006570.5:234..1175"
                     /db_xref="CCDS:CCDS6488.1"
                     /db_xref="GeneID:10670"
                     /db_xref="HGNC:HGNC:16963"
                     /db_xref="MIM:612194"
ORIGIN      
        1 mpntamkkkv llmgksgsgk tsmrsiifan yiardtrrlg atidvehshv rflgnlvlnl
       61 wdcggqdtfm enyftsqrdn ifrnvevliy vfdvesrele kdmhyyqscl eailqnspda
      121 kifclvhkmd lvqedqrdli fkereedlrr lsrplecacf rtsiwdetly kawssivyql
      181 ipnvqqlemn lrnfaqiiea devllferat flvishyqck eqrdvhrfek isniikqfkl
      241 scsklaasfq smevrnsnfa afidiftsnt yvmvvmsdps ipsaatlini rnarkhfekl
      301 ervdgpkhsl lmr
//
LOCUS       NP_001309863             900 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear factor NF-kappa-B p100 subunit isoform a [Homo sapiens].
ACCESSION   NP_001309863 XP_005269917
VERSION     NP_001309863.1
DBSOURCE    REFSEQ: accession NM_001322934.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 900)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 900)
  AUTHORS   De Paolis,V., Troisi,V., Bordin,A., Pagano,F., Caputo,V. and
            Parisi,C.
  TITLE     Unconventional p65/p52 NF-kappaB module regulates key tumor
            microenvironment-related genes in breast tumor-associated
            macrophages (TAMs)
  JOURNAL   Life Sci 357, 123059 (2024)
   PUBMED   39278618
  REMARK    GeneRIF: Unconventional p65/p52 NF-kappaB module regulates key
            tumor microenvironment-related genes in breast tumor-associated
            macrophages (TAMs).
REFERENCE   3  (residues 1 to 900)
  AUTHORS   Vallabhapurapu,S. and Karin,M.
  TITLE     Regulation and function of NF-kappaB transcription factors in the
            immune system
  JOURNAL   Annu Rev Immunol 27, 693-733 (2009)
   PUBMED   19302050
  REMARK    Review article
REFERENCE   4  (residues 1 to 900)
  AUTHORS   Heusch,M., Lin,L., Geleziunas,R. and Greene,W.C.
  TITLE     The generation of nfkb2 p52: mechanism and efficiency
  JOURNAL   Oncogene 18 (46), 6201-6208 (1999)
   PUBMED   10597218
REFERENCE   5  (residues 1 to 900)
  AUTHORS   Lombardi,L., Ciana,P., Cappellini,C., Trecca,D., Guerrini,L.,
            Migliazza,A., Maiolo,A.T. and Neri,A.
  TITLE     Structural and functional characterization of the promoter regions
            of the NFKB2 gene
  JOURNAL   Nucleic Acids Res 23 (12), 2328-2336 (1995)
   PUBMED   7541912
REFERENCE   6  (residues 1 to 900)
  AUTHORS   Liptay,S., Schmid,R.M., Nabel,E.G. and Nabel,G.J.
  TITLE     Transcriptional regulation of NF-kappa B2: evidence for kappa
            B-mediated positive and negative autoregulation
  JOURNAL   Mol Cell Biol 14 (12), 7695-7703 (1994)
   PUBMED   7969113
REFERENCE   7  (residues 1 to 900)
  AUTHORS   Potter,D.A., Larson,C.J., Eckes,P., Schmid,R.M., Nabel,G.J.,
            Verdine,G.L. and Sharp,P.A.
  TITLE     Purification of the major histocompatibility complex class I
            transcription factor H2TF1. The full-length product of the nfkb2
            gene
  JOURNAL   J Biol Chem 268 (25), 18882-18890 (1993)
   PUBMED   8360178
REFERENCE   8  (residues 1 to 900)
  AUTHORS   Bours,V., Burd,P.R., Brown,K., Villalobos,J., Park,S., Ryseck,R.P.,
            Bravo,R., Kelly,K. and Siebenlist,U.
  TITLE     A novel mitogen-inducible gene product related to p50/p105-NF-kappa
            B participates in transactivation through a kappa B site
  JOURNAL   Mol Cell Biol 12 (2), 685-695 (1992)
   PUBMED   1531086
REFERENCE   9  (residues 1 to 900)
  AUTHORS   Schreck,R., Albermann,K. and Baeuerle,P.A.
  TITLE     Nuclear factor kappa B: an oxidative stress-responsive
            transcription factor of eukaryotic cells (a review)
  JOURNAL   Free Radic Res Commun 17 (4), 221-237 (1992)
   PUBMED   1473734
  REMARK    Review article
REFERENCE   10 (residues 1 to 900)
  AUTHORS   Schmid,R.M., Perkins,N.D., Duckett,C.S., Andrews,P.C. and
            Nabel,G.J.
  TITLE     Cloning of an NF-kappa B subunit which stimulates HIV transcription
            in synergy with p65
  JOURNAL   Nature 352 (6337), 733-736 (1991)
   PUBMED   1876189
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121928.13, KT935449.1 and
            AK098415.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2016 this sequence version replaced XP_005269917.1.
            
            Summary: This gene encodes a subunit of the transcription factor
            complex nuclear factor-kappa-B (NFkB). The NFkB complex is
            expressed in numerous cell types and functions as a central
            activator of genes involved in inflammation and immune function.
            The protein encoded by this gene can function as both a
            transcriptional activator or repressor depending on its
            dimerization partner. The p100 full-length protein is
            co-translationally processed into a p52 active form. Chromosomal
            rearrangements and translocations of this locus have been observed
            in B cell lymphomas, some of which may result in the formation of
            fusion proteins. There is a pseudogene for this gene on chromosome
            18. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2013].
            
            Transcript Variant: This variant (5) and variant 1 both encode the
            same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1966682,
                              SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000661543.1/ ENSP00000499294.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..900
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.32"
     Protein         1..900
                     /product="nuclear factor NF-kappa-B p100 subunit isoform
                     a"
                     /note="nuclear factor NF-kappa-B p100 subunit; oncogene
                     Lyt-10; DNA-binding factor KBF2; lymphocyte translocation
                     chromosome 10 protein; transcription factor NFKB2; NFKB,
                     p52/p100 subunit; nuclear factor Kappa-B, subunit 2;
                     nuclear factor of kappa light polypeptide gene enhancer in
                     B-cells 2 (p49/p100); nuclear factor of Kappa light chain
                     gene enhancer in B cells 2; nuclear factor NF-kappa-B p52
                     subunit"
                     /calculated_mol_wt=96618
     mat_peptide     1..454
                     /product="Nuclear factor NF-kappa-B p52 subunit.
                     /id=PRO_0000030322"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
                     /calculated_mol_wt=49423
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          38..221
                     /region_name="RHD-n_NFkB2"
                     /note="N-terminal sub-domain of the Rel homology domain
                     (RHD) of nuclear factor kappa B2 (NF-kappa B2); cd07934"
                     /db_xref="CDD:143650"
     Site            order(52,54..55,57..58,61..63,140,142..143,221)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143650"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          228..327
                     /region_name="IPT_NFkappaB"
                     /note="IPT domain of the transcription factor NFkappaB and
                     related transcription factors. NFkappaB is considered a
                     central regulator of stress responses, activated by
                     different stressful conditions, including physical stress,
                     oxidative stress, and exposure to...; cd01177"
                     /db_xref="CDD:238582"
     Site            order(229,231..233,235..237,275..277,290,302,321,324,326)
                     /site_type="other"
                     /note="ankyrin protein binding site [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(231..232,234,247,249,251,282..283,286,288)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:238582"
     Site            order(252,254,283..284)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238582"
     Region          337..341
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          346..377
                     /region_name="GRR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          404..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          438..706
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            454..455
                     /site_type="cleavage"
                     /note="Cleavage (when cotranslationally processed);
                     propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            order(487,489,493..494,497..499,501..502,506,509,524,526,
                     528,532..533,536..538,540..541,545,548,557,559,561,
                     565..566,571..573,575..576,580,583)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          487..524
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          487..519
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            490..491
                     /site_type="other"
                     /note="Breakpoint for translocation to form NFKB2-IGHA1
                     oncogene; propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          526..557
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          526..555
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..591
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          559..586
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(599,601,605..606,609..611,613..614,618,621,630,633,
                     635,639..640,643..645,647..648,652,655,665,667,669,
                     673..674,677..679,681..682,686,689,698)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          599..630
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          599..628
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          633..665
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          633..663
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          667..698
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          667..696
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          698..734
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            715
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:8887665; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          729..758
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Region          774..849
                     /region_name="Death_NFkB2_p100"
                     /note="Death domain of the Nuclear Factor-KappaB2
                     precursor protein p100; cd08798"
                     /db_xref="CDD:176776"
     Site            812
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Region          849..900
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00653.4)"
     Site            866
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAP3K14.
                     /evidence=ECO:0000269|PubMed:11239468; propagated from
                     UniProtKB/Swiss-Prot (Q00653.4)"
     CDS             1..900
                     /gene="NFKB2"
                     /gene_synonym="CVID10; H2TF1; LYT-10; LYT10; NF-kB2; p100;
                     p49/p100; p52"
                     /coded_by="NM_001322934.2:165..2867"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS41564.1"
                     /db_xref="GeneID:4791"
                     /db_xref="HGNC:HGNC:7795"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvisqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggaaggygga ggggslgffp sslayspyqs gagpmgcypg ggggaqmaat vpsrdsgeea
      421 aepsapsrtp qcepqapeml qrareynarl fglaqrsara lldygvtada rallagqrhl
      481 ltaqdengdt plhlaiihgq tsvieqivyv ihhaqdlgvv nltnhlhqtp lhlavitgqt
      541 svvsfllrvg adpalldrhg dsamhlalra gagapellra llqsgapavp qllhmpdfeg
      601 lypvhlavra rspecldllv dsgaeveate rqggrtalhl atemeelglv thlvtklran
      661 vnartfagnt plhlaaglgy ptltrlllka gadihaenee plcplpsppt sdsdsdsegp
      721 ekdtrssfrg htpldltcst kvktlllnaa qntmeppltp pspagpglsl gdtalqnleq
      781 lldgpeaqgs waelaerlgl rslvdtyrqt tspsgsllrs yelaggdlag llealsdmgl
      841 eegvrllrgp etrdklpsta evkedsaygs qsveqeaekl gpppeppggl chghpqpqvh
//
LOCUS       NP_001165417             257 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform e [Homo sapiens].
ACCESSION   NP_001165417
VERSION     NP_001165417.1
DBSOURCE    REFSEQ: accession NM_001171946.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, 3'
            coding region and 3' UTR, compared to variant 1. The resulting
            isoform (e) has a distinct C-terminus and is shorter than isoform
            a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013613.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..257
                     /product="SUN domain-containing protein 1 isoform e"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=27952
     Region          62..>219
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     CDS             1..257
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001171946.2:68..841"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS55079.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ksqsfktqkk vcfpnlifpf
      241 cksqclhyls wrlkiip
//
LOCUS       NP_001138231            1319 aa            linear   PRI 20-NOV-2025
DEFINITION  pleckstrin homology-like domain family B member 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001138231
VERSION     NP_001138231.1
DBSOURCE    REFSEQ: accession NM_001144759.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1319)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1319)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1319)
  AUTHORS   Tuysuz,B., Uludag Alkaya,D., Geyik,F., Alaylioglu,M., Kasap,B.,
            Kurugoglu,S., Akman,Y.E., Vural,M. and Bilguvar,K.
  TITLE     Biallelic frameshift variants in PHLDB1 cause mild-type
            osteogenesis imperfecta with regressive spondylometaphyseal changes
  JOURNAL   J Med Genet 60 (8), 819-826 (2023)
   PUBMED   36543534
  REMARK    GeneRIF: Biallelic frameshift variants in PHLDB1 cause mild-type
            osteogenesis imperfecta with regressive spondylometaphyseal
            changes.
REFERENCE   4  (residues 1 to 1319)
  AUTHORS   Zhai,J., Zhang,P., Zhang,N., Luo,Y. and Wu,Y.
  TITLE     Analysis of WDFY4 rs7097397 and PHLDB1 rs7389 polymorphisms in
            Chinese patients with systemic lupus erythematosus
  JOURNAL   Clin Rheumatol 41 (7), 2035-2042 (2022)
   PUBMED   35188604
  REMARK    GeneRIF: Analysis of WDFY4 rs7097397 and PHLDB1 rs7389
            polymorphisms in Chinese patients with systemic lupus
            erythematosus.
REFERENCE   5  (residues 1 to 1319)
  AUTHORS   Viana-Pereira,M., Moreno,D.A., Linhares,P., Amorim,J., Nabico,R.,
            Costa,S., Vaz,R. and Reis,R.M.
  TITLE     Replication of GWAS identifies RTEL1, CDKN2A/B, and PHLDB1 SNPs as
            risk factors in Portuguese gliomas patients
  JOURNAL   Mol Biol Rep 47 (2), 877-886 (2020)
   PUBMED   31721021
  REMARK    GeneRIF: The rs6010620 (RTEL1), rs4977756 (CDKN2A/B), and rs498872
            (PHLDB1) are associated with glioma risk in the Portuguese
            population. The GA genotype of the rs498872 (PHLDB1) was associated
            with an increased risk of gliomas (OR 2.92) and glioblastomas (OR
            2.39).  In addition, the genotype AA of the rs498872 (PHLDB1) was
            associated with poor overall survival of gliomas patients (AA vs.
            GA, p = 0.037).
REFERENCE   6  (residues 1 to 1319)
  AUTHORS   Sanson,M., Hosking,F.J., Shete,S., Zelenika,D., Dobbins,S.E.,
            Ma,Y., Enciso-Mora,V., Idbaih,A., Delattre,J.Y., Hoang-Xuan,K.,
            Marie,Y., Boisselier,B., Carpentier,C., Wang,X.W., Di Stefano,A.L.,
            Labussiere,M., Gousias,K., Schramm,J., Boland,A., Lechner,D.,
            Gut,I., Armstrong,G., Liu,Y., Yu,R., Lau,C., Di Bernardo,M.C.,
            Robertson,L.B., Muir,K., Hepworth,S., Swerdlow,A., Schoemaker,M.J.,
            Wichmann,H.E., Muller,M., Schreiber,S., Franke,A., Moebus,S.,
            Eisele,L., Forsti,A., Hemminki,K., Lathrop,M., Bondy,M.,
            Houlston,R.S. and Simon,M.
  TITLE     Chromosome 7p11.2 (EGFR) variation influences glioma risk
  JOURNAL   Hum Mol Genet 20 (14), 2897-2904 (2011)
   PUBMED   21531791
REFERENCE   7  (residues 1 to 1319)
  AUTHORS   Hotta,A., Kawakatsu,T., Nakatani,T., Sato,T., Matsui,C.,
            Sukezane,T., Akagi,T., Hamaji,T., Grigoriev,I., Akhmanova,A.,
            Takai,Y. and Mimori-Kiyosue,Y.
  TITLE     Laminin-based cell adhesion anchors microtubule plus ends to the
            epithelial cell basal cortex through LL5alpha/beta
  JOURNAL   J Cell Biol 189 (5), 901-917 (2010)
   PUBMED   20513769
  REMARK    GeneRIF: Signaling from laminin-integrin associations in epithelial
            cells attaches microtubule plus ends to the epithelial basal cell
            cortex via PHLDB1 and PHLDB2.
REFERENCE   8  (residues 1 to 1319)
  AUTHORS   Homma,K., Kikuno,R.F., Nagase,T., Ohara,O. and Nishikawa,K.
  TITLE     Alternative splice variants encoding unstable protein domains exist
            in the human brain
  JOURNAL   J Mol Biol 343 (5), 1207-1220 (2004)
   PUBMED   15491607
REFERENCE   9  (residues 1 to 1319)
  AUTHORS   Katoh,M. and Katoh,M.
  TITLE     Identification and characterization of human LL5A gene and mouse
            Ll5a gene in silico
  JOURNAL   Int J Oncol 23 (5), 1477-1483 (2003)
   PUBMED   14532993
REFERENCE   10 (residues 1 to 1319)
  AUTHORS   Dowler,S., Currie,R.A., Campbell,D.G., Deak,M., Kular,G.,
            Downes,C.P. and Alessi,D.R.
  TITLE     Identification of pleckstrin-homology-domain-containing proteins
            with novel phosphoinositide-binding specificities
  JOURNAL   Biochem J 351 (Pt 1), 19-31 (2000)
   PUBMED   11001876
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX489377.1, AB014538.2, AK074918.1, AK125783.1 and AI917888.1.
            
            Transcript Variant: This variant (3) represents use of an alternate
            promoter, differs in the 5' UTR, and lacks two alternate in-frame
            exons in the coding region, compared to variant 1. The resulting
            isoform (b) lacks two internal segments, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK074070.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..1319
                     /product="pleckstrin homology-like domain family B member
                     1 isoform b"
                     /note="protein LL5-alpha"
                     /calculated_mol_wt=144609
     Region          24..142
                     /region_name="FHA_PHLB1"
                     /note="forkhead associated (FHA) domain found in
                     pleckstrin homology-like domain family B member 1 (PHLDB1)
                     and similar proteins; cd22713"
                     /db_xref="CDD:438765"
     Region          152..>546
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Region          <677..>1189
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          <680..>893
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          1208..1312
                     /region_name="PH_PHLDB1_2"
                     /note="Pleckstrin homology-like domain-containing family B
                     member 2 pleckstrin homology (PH) domain; cd14673"
                     /db_xref="CDD:270192"
     CDS             1..1319
                     /gene="PHLDB1"
                     /gene_synonym="LL5A; LL5alpha; OI23"
                     /coded_by="NM_001144759.3:107..4066"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS44750.1"
                     /db_xref="GeneID:23187"
                     /db_xref="HGNC:HGNC:23697"
                     /db_xref="MIM:612834"
ORIGIN      
        1 mdalnrnqig pgcqtqtmvq kgpldlietg kglkvqtdkp hlvslgsgrl staitllple
       61 egrtvigsaa rdislqgpgl apehcyienl rgtltlypcg nactidglpv rqptrltqgc
      121 mlclgqstfl rfnhpaeakw mksmipaggr apgppyspvp aeseslvngn htpqtatrgp
      181 sacashsslv ssiekdlqei mdslvleepg aagkkpaats plspmanggr yllspptspg
      241 amsvgssyen tspafsplss passgscash spsgqepgps vpplvparss syhlalqppq
      301 srpsgarses prlsrkgghe rppspglrgl ltdspaatvl aearratesp rlggqlpvva
      361 islseypasg alsqptsipg spkfqppvpa prnkigtlqd rppspfrepp gservlttsp
      421 srqlvgrtfs dglatrtlqp pesprlgrrg ldsmrelppl spslsrrals plptrttpdp
      481 klnrevaesp rprrwaahga spedfsltlg argrrtrsps ptlgeslaph kgsfsgrlsp
      541 ayslgsltga spcqspcvqr klssgdlrvp vtrerknsit eisdneddll eyhrrqrqer
      601 lreqemerle rqrletilnl caeysradgg peagelpsig eataalalag rrpsrglaga
      661 sgrsseepgv atqrlwesme rsdeenlkee csstestqqe hedapstklq gevlaleeer
      721 aqvlghveql kvrvkeleqq lqesareaem erallqgere aerallqkeq kavdqlqekl
      781 valetgiqke rdkeaealet etklfedlef qqleresrve eerelagqgl lrskaellrs
      841 iakrkerlai ldsqagqira qavqeserla rdknaslqll qkekekltvl erryhsltgg
      901 rpfpkttstl kevyrskmdg eatsplprtr sgplpsssgs sssssqlsva tlgrspspks
      961 alltqngtgs lprnlaatlq dietkrqlal qqkgqqviee qrrrlaelkq kaaaeaqcqw
     1021 dalhgaapfp agpsgfpplm hhsilhhlpa grergeegeh aydtlsless dsmetsistg
     1081 gnsacspdnm ssasgldmgk ieemekmlke ahaeknrlme sreremelrr qaleeerrrr
     1141 eqverrlqse sarrqqlvek evkmrekqfs qarpltrylp irkedfdlkt hiessghgvd
     1201 tclhvvlssk vcrgylvkmg gkikswkkrw fvfdrlkrtl syyvdkhetk lkgviyfqai
     1261 eevyydhlrs aakspnpalt fcvkthdrly ymvapsaeam riwmdvivtg aegytqfmn
//
LOCUS       NP_001317406             264 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 6 isoform 6 [Homo sapiens].
ACCESSION   NP_001317406
VERSION     NP_001317406.1
DBSOURCE    REFSEQ: accession NM_001330477.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Song,C.C., Liu,T., Hogstrand,C., Zhong,C.C., Zheng,H., Sun,L.H. and
            Luo,Z.
  TITLE     SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved
            in the regulation of zinc metabolism in Golgi apparatus
  JOURNAL   Cell Mol Life Sci 81 (1), 422 (2024)
   PUBMED   39367979
  REMARK    GeneRIF: SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409
            involved in the regulation of zinc metabolism in Golgi apparatus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Aktay,I., Billur,D., Tuncay,E. and Turan,B.
  TITLE     An Overexpression of SLC30A6 Gene Contributes to Cardiomyocyte
            Dysfunction via Affecting Mitochondria and Inducing Activations in
            K-Acetylation and Epigenetic Proteins
  JOURNAL   Biochem Genet 62 (4), 3198-3214 (2024)
   PUBMED   38091184
  REMARK    GeneRIF: An Overexpression of SLC30A6 Gene Contributes to
            Cardiomyocyte Dysfunction via Affecting Mitochondria and Inducing
            Activations in K-Acetylation and Epigenetic Proteins.
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Zhu,B., Huo,R., Zhi,Q., Zhan,M., Chen,X. and Hua,Z.C.
  TITLE     Increased expression of zinc transporter ZIP4, ZIP11, ZnT1, and
            ZnT6 predicts poor prognosis in pancreatic cancer
  JOURNAL   J Trace Elem Med Biol 65, 126734 (2021)
   PUBMED   33631610
  REMARK    GeneRIF: Increased expression of zinc transporter ZIP4, ZIP11,
            ZnT1, and ZnT6 predicts poor prognosis in pancreatic cancer.
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Smith,J.L., Xiong,S., Markesbery,W.R. and Lovell,M.A.
  TITLE     Altered expression of zinc transporters-4 and -6 in mild cognitive
            impairment, early and late Alzheimer's disease brain
  JOURNAL   Neuroscience 140 (3), 879-888 (2006)
   PUBMED   16580781
  REMARK    GeneRIF: Our results show that Zn transporter-4 and Zn
            transporter-6 are significantly (P<0.05) increased in
            hippocampus/parahippocampal gyrus of early Alzheimer's disease and
            Alzheimer's disease subjects.
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Huang,L., Kirschke,C.P. and Gitschier,J.
  TITLE     Functional characterization of a novel mammalian zinc transporter,
            ZnT6
  JOURNAL   J Biol Chem 277 (29), 26389-26395 (2002)
   PUBMED   11997387
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096672.1, AL121653.2 and
            AA594503.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function as zinc transporters. This protein can regulate
            subcellular levels of zinc in the Golgi and vesicles. Expression of
            this gene is altered in the Alzheimer's disease brain plaques.
            [provided by RefSeq, Aug 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096672.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145313, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..264
                     /product="zinc transporter 6 isoform 6"
                     /note="zinc transporter 6; solute carrier family 30 (zinc
                     transporter), member 6"
                     /calculated_mol_wt=28650
     Region          <5..134
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     CDS             1..264
                     /gene="SLC30A6"
                     /gene_synonym="MST103; MSTP103; ZNT6"
                     /coded_by="NM_001330477.2:612..1406"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:55676"
                     /db_xref="HGNC:HGNC:19305"
                     /db_xref="MIM:611148"
ORIGIN      
        1 mnpfvlidla gafalcitym lieinnyfav dtasaiaial mtfgtmypms vysgkvllqt
       61 tpphvigqld klirevstld gvlevrnehf wtlgfgslag svhvrirrda neqmvlahvt
      121 nrlytlvstl tvqifkddwi rpallsgpva anvlnfsdhh vipmpllkgt ddlnpvtstp
      181 akpsspppef sfntpgknvn pvillntqtr pygfglnhgh tpyssmlnqg lgvpgigatq
      241 glrtgftnip srygtnnrig qprp
//
LOCUS       NP_115521                745 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 30 [Homo sapiens].
ACCESSION   NP_115521
VERSION     NP_115521.3
DBSOURCE    REFSEQ: accession NM_032145.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Yuan,Y., Liu,Z., Li,B., Gong,Z., Piao,C., Liu,Z., Zhang,Z. and
            Dong,X.
  TITLE     FBXO30 functions as a tumor suppressor and an E3 ubiquitin ligase
            for hZIP1-mediated HIF-1alpha degradation in renal cell carcinoma
  JOURNAL   Int J Oncol 62 (3) (2023)
   PUBMED   36799168
  REMARK    GeneRIF: FBXO30 functions as a tumor suppressor and an E3 ubiquitin
            ligase for hZIP1mediated HIF1alpha degradation in renal cell
            carcinoma.
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Cheng,X., Pei,P., Yu,J., Zhang,Q., Li,D., Xie,X., Wu,J., Wang,S.
            and Zhang,T.
  TITLE     F-box protein FBXO30 mediates retinoic acid receptor gamma
            ubiquitination and regulates BMP signaling in neural tube defects
  JOURNAL   Cell Death Dis 10 (8), 551 (2019)
   PUBMED   31320612
  REMARK    GeneRIF: Retinoic acid receptor gamma levels are controlled by
            FBXO30-mediated ubiquitination and that FBXO30 is a key regulator
            of BMP signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 745)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 745)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   7  (residues 1 to 745)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   8  (residues 1 to 745)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 745)
  AUTHORS   Xiong,W., Zeng,Z.Y., Shen,S.R., Li,X.L., Li,W.F., Wang,R.,
            Xiong,F., Peng,C., Zhang,Q.H., Zhou,M., Yang,Y.X., Zhou,H.D.,
            Huang,H. and Li,G.Y.
  TITLE     [Studies on the relationship between D6S1581, a high frequency
            allele imbalance locus, and genetic susceptibility to
            nasopharyngeal carcinoma]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 20 (4), 311-314 (2003)
   PUBMED   12903040
  REMARK    GeneRIF: Results suggest that D6S1581 is highly associated with
            nasopharyngeal carcinoma, and there may be one or more NPC
            associated genes near D6S1581, including FBXO30.
REFERENCE   10 (residues 1 to 745)
  AUTHORS   Li,Z.H., Zhang,X.H. and Li,G.Y.
  TITLE     [Study on the fusion expression of FBXO30: a novel member of F-box
            protein family]
  JOURNAL   Hunan Yi Ke Da Xue Xue Bao 26 (6), 495-498 (2001)
   PUBMED   12536519
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL356599.19, BG718454.1,
            BC024326.1, AF248640.2 and AL023806.1.
            
            On Sep 11, 2003 this sequence version replaced NP_115521.2.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class and it is upregulated in nasopharyngeal
            carcinoma. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer transcript.
            Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.134945.1,
                                           SRR1660809.40145.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000237281.5/ ENSP00000237281.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.3"
     Protein         1..745
                     /product="F-box only protein 30"
                     /note="F-box only protein, helicase, 18; F-box domain
                     protein"
                     /calculated_mol_wt=82174
     Region          7..98
                     /region_name="zf-TRAF_2"
                     /note="TRAF-like zinc-finger; pfam15965"
                     /db_xref="CDD:464957"
     Region          211..231
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB52.3)"
     Region          305..324
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TB52.3)"
     Region          609..724
                     /region_name="F-box_4"
                     /note="pfam15966"
                     /db_xref="CDD:464958"
     CDS             1..745
                     /gene="FBXO30"
                     /gene_synonym="Fbx30"
                     /coded_by="NM_032145.5:210..2447"
                     /db_xref="CCDS:CCDS5208.1"
                     /db_xref="GeneID:84085"
                     /db_xref="HGNC:HGNC:15600"
                     /db_xref="MIM:609101"
ORIGIN      
        1 meeelqhshc vncvsrrcmt rpepgiscdl igcplvcgav fhsckadehr llcpfervpc
       61 lnsdfgcpft marnkvaehl emcpasvvcc tmewnrwpvs yadrksyenl srdvdevaql
      121 dmalalqdqr mlleslkvat mmskatdkvs kpreqisvks svpeiphang lvsvdeesyg
      181 alyqatvett rslaaaldil ntatrdigml ntsvpndmde qqnaresled qnlkdqdhly
      241 eeeigavggi dyndtnqnaq seqngssdll cdlntssydt salcngfple nictqvidqn
      301 qnlhgdskqs nltngdcvas sdgtskpsss lavaaqlrei ipssalpngt vqhilmpdde
      361 gegelcwkkv dlgdvknvdv lsfshapsfn flsnscwskp kedkavdtsd levaedpmgl
      421 qgidlitaal lfclgdspgg rgisdsrmad iyhidvgtqt fslpsailat stmvgeiasa
      481 sacdhanpql snpspfqtlg ldlvlecvar yqpkqrsmft fvcgqlfrrk efsshfknvh
      541 gdihaglngw meqrcplayy gctysqrrfc psiqgakiih drhlrsfgvq pcvstvlvep
      601 arncvlglhn dhlsslpfev lqhiagfldg fslcqlscvs klmrdvcgsl lqsrgmvilq
      661 wgkrkypegn sswqikekvw rfstafcsvn ewkfadilsm adhlkkcsyn vvekreeaip
      721 lpcmcvtrel tkegrslrsv lkpvl
//
LOCUS       NP_001171835             404 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 20 isoform 2 [Homo sapiens].
ACCESSION   NP_001171835
VERSION     NP_001171835.1
DBSOURCE    REFSEQ: accession NM_001184906.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Liu,J., Zhan,W., Chen,G., Yan,S., Chen,W. and Li,R.
  TITLE     SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer
  JOURNAL   Cell Signal 101, 110503 (2023)
   PUBMED   36374774
  REMARK    GeneRIF: SP1-induced PROX1-AS1 contributes to tumor progression by
            regulating miR-326/FBXL20 axis in colorectal cancer.
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Sun,R. and Lim,S.O.
  TITLE     FBXL20-mediated ubiquitination triggers the proteasomal degradation
            of 4-1BB
  JOURNAL   FEBS J 289 (15), 4549-4563 (2022)
   PUBMED   35112462
  REMARK    GeneRIF: FBXL20-mediated ubiquitination triggers the proteasomal
            degradation of 4-1BB.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Madduri,L.S.V., Brandquist,N.D., Palanivel,C., Talmon,G.A.,
            Baine,M.J., Zhou,S., Enke,C.A., Johnson,K.R., Ouellette,M.M. and
            Yan,Y.
  TITLE     p53/FBXL20 axis negatively regulates the protein stability of
            PR55alpha, a regulatory subunit of PP2A Ser/Thr phosphatase
  JOURNAL   Neoplasia 23 (12), 1192-1203 (2021)
   PUBMED   34731788
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Manne,R.K., Agrawal,Y., Malonia,S.K., Banday,S., Edachery,S.,
            Patel,A., Kumar,A., Shetty,P. and Santra,M.K.
  TITLE     FBXL20 promotes breast cancer malignancy by inhibiting apoptosis
            through degradation of PUMA and BAX
  JOURNAL   J Biol Chem 297 (4), 101253 (2021)
   PUBMED   34587475
  REMARK    GeneRIF: FBXL20 promotes breast cancer malignancy by inhibiting
            apoptosis through degradation of PUMA and BAX.
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Xiao,J., Zhang,T., Xu,D., Wang,H., Cai,Y., Jin,T., Liu,M., Jin,M.,
            Wu,K. and Yuan,J.
  TITLE     FBXL20-mediated Vps34 ubiquitination as a p53 controlled checkpoint
            in regulating autophagy and receptor degradation
  JOURNAL   Genes Dev 29 (2), 184-196 (2015)
   PUBMED   25593308
  REMARK    GeneRIF: which provides a signal to promote its ubiquitination and
            proteasomal degradation mediated by FBXL20 and the associated
            Skp1-Cullin1 complex, leading to inhibition of autophagy and
            receptor endocytosis
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Zhu,J., Li,K., Dong,L. and Chen,Y.
  TITLE     Role of FBXL20 in human colorectal adenocarcinoma
  JOURNAL   Oncol Rep 28 (6), 2290-2298 (2012)
   PUBMED   23023584
  REMARK    GeneRIF: study concludes FBXL20 plays an essential role in the
            carcinogenesis of colorectal adenocarcinoma and promotes
            carcinogenesis through the regulation of the Wnt signaling pathway
            and caspase activation
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Mells,G.F., Floyd,J.A., Morley,K.I., Cordell,H.J., Franklin,C.S.,
            Shin,S.Y., Heneghan,M.A., Neuberger,J.M., Donaldson,P.T., Day,D.B.,
            Ducker,S.J., Muriithi,A.W., Wheater,E.F., Hammond,C.J.,
            Dawwas,M.F., Jones,D.E., Peltonen,L., Alexander,G.J., Sandford,R.N.
            and Anderson,C.A.
  CONSRTM   UK PBC Consortium; Wellcome Trust Case Control Consortium 3
  TITLE     Genome-wide association study identifies 12 new susceptibility loci
            for primary biliary cirrhosis
  JOURNAL   Nat Genet 43 (4), 329-332 (2011)
   PUBMED   21399635
  REMARK    Erratum:[Nat Genet. 2011 Nov;43(11):1164. Richardson,Paul [added];
            Nasr, Ikram [added]; Aspinall,Richard [added]]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA747594.1, DQ223959.1 and AC015910.10.
            
            Summary: Members of the F-box protein family, such as FBXL20, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1. The resulting isoform (2) is shorter but has
            the same N- and C- termini compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.3029218.1,
                                           SRR7346977.814604.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..404
                     /product="F-box/LRR-repeat protein 20 isoform 2"
                     /note="F-box protein FBL2"
                     /calculated_mol_wt=44849
     Region          22..66
                     /region_name="F-box_FBXL2-like"
                     /note="F-box domain found in F-box/LRR-repeat protein 2
                     (FBXL2), F-box/LRR-repeat protein 20 (FBXL20) and similar
                     proteins; cd22115"
                     /db_xref="CDD:438887"
     Site            order(22..25,27..28,31..32,35..41,44,46..53,55..56,64)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438887"
     Region          <89..257
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          93..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          119..138
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          139..164
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          165..190
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          188..362
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          191..216
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          217..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          243..268
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          269..294
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          295..317
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          324..348
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          349..374
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..404
                     /gene="FBXL20"
                     /gene_synonym="Fbl2; Fbl20"
                     /coded_by="NM_001184906.2:225..1439"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54116.1"
                     /db_xref="GeneID:84961"
                     /db_xref="HGNC:HGNC:24679"
                     /db_xref="MIM:609086"
ORIGIN      
        1 mrrdvngvtk srfemfsnsd eavinkklpk elllrifsfl dvvtlcrcaq vsrawnvlal
       61 dgsnwqridl fdfqrdiegr vveniskrcg gflrklslrg clgvgdnalr tfaqncrnie
      121 vlnlngctkt tdaegcplle qlniswcdqv tkdgiqalvr gcgglkalfl kgctqledea
      181 lkyigahcpe lvtlnlqtcl qitdegliti crgchklqsl casgcsnitd ailnalgqnc
      241 prlrilevar csqltdvgft tlarnchele kmdleecvqi tdstliqlsi hcprlqvlsl
      301 shcelitddg irhlgngaca hdqlevield ncplitdasl ehlkschsle rielydcqqi
      361 tragikrlrt hlpnikvhay fapvtpppsv ggsrqrfcrc ciil
//
LOCUS       NP_001304983             110 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase HRas isoform 3 [Homo sapiens].
ACCESSION   NP_001304983
VERSION     NP_001304983.1
DBSOURCE    REFSEQ: accession NM_001318054.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 110)
  AUTHORS   Ling,C., Liu,S.S., Wang,Y.Y., Huo,G.T., Yang,Y.W., Xu,N., Wang,H.,
            Wu,Y., Miao,Y.F., Fu,R., Zhao,Y.W. and Fan,C.F.
  TITLE     Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice
  JOURNAL   Zool Res 45 (3), 551-566 (2024)
   PUBMED   38757223
  REMARK    GeneRIF: Overexpression of wild-type HRAS drives non-alcoholic
            steatohepatitis to hepatocellular carcinoma in mice.
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Devi,P., Dwivedi,R., Sankar,R., Jain,A., Gupta,S. and Gupta,S.
  TITLE     Unraveling the Genetic Web: H-Ras Expression and Mutation in Oral
            Squamous Cell Carcinoma-A Systematic Review
  JOURNAL   Head Neck Pathol 18 (1), 21 (2024)
   PUBMED   38502412
  REMARK    GeneRIF: Unraveling the Genetic Web: H-Ras Expression and Mutation
            in Oral Squamous Cell Carcinoma-A Systematic Review.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Zhang,Q., Zheng,L., Bai,Y., Su,C., Che,Y., Xu,J., Sun,K., Ni,J.,
            Huang,L., Shen,Y., Jia,L., Xu,L., Yin,R., Li,M. and Hu,J.
  TITLE     ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21HRAS splicing and stabilizing DDX3X to activate the
            cRaf-MEK-ERK cascade
  JOURNAL   Cancer Lett 577, 216426 (2023)
   PUBMED   37820992
  REMARK    GeneRIF: ITPR1-AS1 promotes small cell lung cancer metastasis by
            facilitating P21[HRAS] splicing and stabilizing DDX3X to activate
            the cRaf-MEK-ERK cascade.
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Wang,J., Al-Majid,D., Brenner,J.C. and Smith,J.D.
  TITLE     Mutant HRas Signaling and Rationale for Use of Farnesyltransferase
            Inhibitors in Head and Neck Squamous Cell Carcinoma
  JOURNAL   Target Oncol 18 (5), 643-655 (2023)
   PUBMED   37665491
  REMARK    GeneRIF: Mutant HRas Signaling and Rationale for Use of
            Farnesyltransferase Inhibitors in Head and Neck Squamous Cell
            Carcinoma.
            Review article
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Gripp,K.W. and Weaver,K.N.
  TITLE     HRAS-Related Costello Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301680
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Sakai,E., Rikimaru,K., Ueda,M., Matsumoto,Y., Ishii,N., Enomoto,S.,
            Yamamoto,H. and Tsuchida,N.
  TITLE     The p53 tumor-suppressor gene and ras oncogene mutations in oral
            squamous-cell carcinoma
  JOURNAL   Int J Cancer 52 (6), 867-872 (1992)
   PUBMED   1459726
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Tanci,P., Genuardi,M., Santini,S.A. and Neri,G.
  TITLE     PCR detection of an insertion/deletion polymorphism in intron 1 of
            the HRAS1 locus
  JOURNAL   Nucleic Acids Res 20 (5), 1157 (1992)
   PUBMED   1549493
REFERENCE   9  (residues 1 to 110)
  AUTHORS   Kinsella,B.T., Erdman,R.A. and Maltese,W.A.
  TITLE     Posttranslational modification of Ha-ras p21 by farnesyl versus
            geranylgeranyl isoprenoids is determined by the COOH-terminal amino
            acid
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 8934-8938 (1991)
   PUBMED   1924354
REFERENCE   10 (residues 1 to 110)
  AUTHORS   Tong,L.A., de Vos,A.M., Milburn,M.V. and Kim,S.H.
  TITLE     Crystal structures at 2.2 A resolution of the catalytic domains of
            normal ras protein and an oncogenic mutant complexed with GDP
  JOURNAL   J Mol Biol 217 (3), 503-516 (1991)
   PUBMED   1899707
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC137894.5, BM808879.1 and
            BC006499.2.
            
            Summary: This gene belongs to the Ras oncogene family, whose
            members are related to the transforming genes of mammalian sarcoma
            retroviruses. The products encoded by these genes function in
            signal transduction pathways. These proteins can bind GTP and GDP,
            and they have intrinsic GTPase activity. This protein undergoes a
            continuous cycle of de- and re-palmitoylation, which regulates its
            rapid exchange between the plasma membrane and the Golgi apparatus.
            Mutations in this gene cause Costello syndrome, a disease
            characterized by increased growth at the prenatal stage, growth
            deficiency at the postnatal stage, predisposition to tumor
            formation, cognitive disability, skin and musculoskeletal
            abnormalities, distinctive facial appearance and cardiovascular
            abnormalities. Defects in this gene are implicated in a variety of
            cancers, including bladder cancer, follicular thyroid cancer, and
            oral squamous cell carcinoma. Multiple transcript variants, which
            encode different isoforms, have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) includes an alternate exon
            resulting in a different 5' UTR and the use of a downstream
            translation start site compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006499.2, DRR138523.20315.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..110
                     /product="GTPase HRas isoform 3"
                     /EC_number="3.6.5.2"
                     /note="Ha-Ras1 proto-oncoprotein; Ras family small GTP
                     binding protein H-Ras; Harvey rat sarcoma viral oncogene
                     homolog; p19 H-RasIDX protein; transforming protein p21;
                     GTPase HRas; GTP- and GDP-binding peptide B;
                     transformation gene: oncogene HAMSV; c-has/bas p21
                     protein; v-Ha-ras Harvey rat sarcoma viral oncogene
                     homolog; Harvey rat sarcoma viral oncoprotein"
                     /calculated_mol_wt=11801
     Region          <67..85
                     /region_name="P-loop containing Nucleoside Triphosphate
                     Hydrolases"
                     /note="Members of the P-loop NTPase domain superfamily are
                     characterized by a conserved nucleotide phosphate-binding
                     motif, also referred to as the Walker A motif
                     (GxxxxGK[S/T], where x is any residue), and the Walker B
                     motif (hhhh[D/E], where h is a...; cl38936"
                     /db_xref="CDD:476819"
     CDS             1..110
                     /gene="HRAS"
                     /gene_synonym="C-BAS/HAS; C-H-RAS; C-HA-RAS1; CTLO;
                     H-RASIDX; HAMSV; HRAS1; p21ras; RASH1"
                     /coded_by="NM_001318054.2:534..866"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:3265"
                     /db_xref="HGNC:HGNC:5173"
                     /db_xref="MIM:190020"
ORIGIN      
        1 mtcpwcwwgt svtwlhalwn lgrlrtspea tasptsrprp rpgraaalal apapgpsgtp
       61 rdpcdpaapr agvedafytl vreirqhklr klnppdesgp gcmsckcvls
//
LOCUS       NP_056298                623 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch repeat and BTB domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_056298 XP_291224 XP_374418
VERSION     NP_056298.2
DBSOURCE    REFSEQ: accession NM_015483.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 623)
  AUTHORS   Hu,Y., Zhang,Z., Mao,Q., Zhang,X., Hao,A., Xun,Y., Wang,Y., Han,L.,
            Zhan,W., Liu,Q., Yin,Y., Peng,C., Moresco,E.M.Y., Chen,Z.,
            Beutler,B. and Sun,L.
  TITLE     Dynamic molecular architecture and substrate recruitment of
            cullin3-RING E3 ligase CRL3KBTBD2
  JOURNAL   Nat Struct Mol Biol 31 (2), 336-350 (2024)
   PUBMED   38332366
  REMARK    GeneRIF: Dynamic molecular architecture and substrate recruitment
            of cullin3-RING E3 ligase CRL3[KBTBD2].
REFERENCE   2  (residues 1 to 623)
  AUTHORS   Tsay,A. and Wang,J.C.
  TITLE     The Role of PIK3R1 in Metabolic Function and Insulin Sensitivity
  JOURNAL   Int J Mol Sci 24 (16), 12665 (2023)
   PUBMED   37628845
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 623)
  AUTHORS   Zhang,Z., Turer,E., Li,X., Zhan,X., Choi,M., Tang,M., Press,A.,
            Smith,S.R., Divoux,A., Moresco,E.M. and Beutler,B.
  TITLE     Insulin resistance and diabetes caused by genetic or diet-induced
            KBTBD2 deficiency in mice
  JOURNAL   Proc Natl Acad Sci U S A 113 (42), E6418-E6426 (2016)
   PUBMED   27708159
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC018648.5 and BC037887.2.
            
            On Feb 12, 2009 this sequence version replaced NP_056298.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037887.2, SRR1660805.199725.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154405, SAMN03267754
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000304056.9/ ENSP00000302586.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..623
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14.3"
     Protein         1..623
                     /product="kelch repeat and BTB domain-containing protein
                     2"
                     /note="BTB and kelch domain containing 1; BTB and kelch
                     domain-containing protein 1; kelch repeat and BTB (POZ)
                     domain containing 2"
                     /calculated_mol_wt=71200
     Region          5..137
                     /region_name="BTB_POZ_KBTBD2_BKLHD1"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch repeat
                     and BTB domain-containing protein 2 (KBTBD2); cd18270"
                     /db_xref="CDD:349579"
     Region          23..516
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          128..223
                     /region_name="BACK_KBTBD2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch repeat and BTB domain-containing protein 2 (KBTBD2);
                     cd18479"
                     /db_xref="CDD:350554"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          310..366
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          317..380
                     /region_name="Kelch 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          370..416
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          381..429
                     /region_name="Kelch 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          419..453
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          431..469
                     /region_name="Kelch 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          459..516
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          470..529
                     /region_name="Kelch 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     Region          519..568
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          535..581
                     /region_name="Kelch 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY47.2)"
     CDS             1..623
                     /gene="KBTBD2"
                     /gene_synonym="BKLHD1"
                     /coded_by="NM_015483.3:564..2435"
                     /db_xref="CCDS:CCDS34614.1"
                     /db_xref="GeneID:25948"
                     /db_xref="HGNC:HGNC:21751"
                     /db_xref="MIM:619393"
ORIGIN      
        1 mstqderqin teyavslleq lklfyeqqlf tdivlivegt efpchkmvla tcssyframf
       61 msglseskqt hvhlrnvdaa tlqiiityay tgnlamndst veqlyetacf lqvedvlqrc
      121 reylikkina encvrllsfa dlfsceelkq sakrmvehkf tavyhqdafm qlshdllidi
      181 lssdnlnvek eetvreaaml wleyntesrs qylssvlsqi ridalsevtq rawfqglppn
      241 dksvvvqgly ksmpkffkpr lgmtkeemmi fieassenpc slyssvcysp qaekvyklcs
      301 ppadlhkvgt vvtpdndiyi aggqvplknt ktnhsktskl qtafrtvncf ywfdaqqntw
      361 fpktpmlfvr ikpslvcceg yiyaiggdsv ggelnrrtve rydtekdewt mvsplpcawq
      421 wsaavvvhdc iyvmtlnlmy cyfprsdswv emamrqtsrs fasaaafgdk ifyigglhia
      481 tnsgirlpsg tvdgssvtve iydvnknewk maanipakry sdpcvravvi snslcvfmre
      541 thlnerakyv tyqydleldr wslrqhiser vlwdlgrdfr ctvgklypsc leespwkppt
      601 ylfstdgtee feldgemval ppv
//
LOCUS       NP_001120794             191 aa            linear   PRI 20-NOV-2025
DEFINITION  chromobox protein homolog 5 [Homo sapiens].
ACCESSION   NP_001120794
VERSION     NP_001120794.1
DBSOURCE    REFSEQ: accession NM_001127322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Zhou,L., Chen,Z., Zou,Y., Zhang,X., Wang,Z., Zhu,H., Lin,J.,
            Huang,Z., Zheng,L., Chen,J., Xie,M., Zhang,M., Zhang,R., Zhu,M.,
            Wang,Z., Zhou,H., Gao,S., Yin,Y., Wu,Y. and Kang,T.
  TITLE     ASB7 is a negative regulator of H3K9me3 homeostasis
  JOURNAL   Science 389 (6757), 309-316 (2025)
   PUBMED   40440427
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Lou,J., Deng,Q., Zhang,X., Bell,C.C., Das,A.B., Bediaga,N.G.,
            Zlatic,C.O., Johanson,T.M., Allan,R.S., Griffin,M.D.W.,
            Paradkar,P., Harvey,K.F., Dawson,M.A. and Hinde,E.
  TITLE     Heterochromatin protein 1 alpha (HP1alpha) undergoes a monomer to
            dimer transition that opens and compacts live cell genome
            architecture
  JOURNAL   Nucleic Acids Res 52 (18), 10918-10933 (2024)
   PUBMED   39193905
  REMARK    GeneRIF: Heterochromatin protein 1 alpha (HP1alpha) undergoes a
            monomer to dimer transition that opens and compacts live cell
            genome architecture.
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Sako,K., Furukawa,A., Nozawa,R.S., Kurita,J.I., Nishimura,Y. and
            Hirota,T.
  TITLE     Bipartite binding interface recruiting HP1 to chromosomal passenger
            complex at inner centromeres
  JOURNAL   J Cell Biol 223 (9) (2024)
   PUBMED   38781028
  REMARK    GeneRIF: Bipartite binding interface recruiting HP1 to chromosomal
            passenger complex at inner centromeres.
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Ukmar-Godec,T., Yu,T., de Opakua,A.I., Pantoja,C.F., Munari,F. and
            Zweckstetter,M.
  TITLE     Conformational diversity of human HP1alpha
  JOURNAL   Protein Sci 33 (7), e5079 (2024)
   PUBMED   38895997
  REMARK    GeneRIF: Conformational diversity of human HP1alpha.
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Xiong,F., Wang,D., Xiong,W., Wang,X., Huang,W.H., Wu,G.H.,
            Liu,W.Z., Wang,Q., Chen,J.S., Kuai,Y.Y., Wang,B. and Chen,Y.J.
  TITLE     Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a therapeutic
            target for HP1alpha-positive intrahepatic cholangiocarcinoma
  JOURNAL   J Exp Clin Cancer Res 43 (1), 152 (2024)
   PUBMED   38812060
  REMARK    GeneRIF: Unveiling the role of HP1alpha-HDAC1-STAT1 axis as a
            therapeutic target for HP1alpha-positive intrahepatic
            cholangiocarcinoma.
            Erratum:[J Exp Clin Cancer Res. 2024 Jul 5;43(1):186. doi:
            10.1186/s13046-024-03112-w. PMID: 38965576]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Lessard,J., Baban,S. and Sauvageau,G.
  TITLE     Stage-specific expression of polycomb group genes in human bone
            marrow cells
  JOURNAL   Blood 91 (4), 1216-1224 (1998)
   PUBMED   9454751
REFERENCE   7  (residues 1 to 191)
  AUTHORS   Ye,Q., Callebaut,I., Pezhman,A., Courvalin,J.C. and Worman,H.J.
  TITLE     Domain-specific interactions of human HP1-type chromodomain
            proteins and inner nuclear membrane protein LBR
  JOURNAL   J Biol Chem 272 (23), 14983-14989 (1997)
   PUBMED   9169472
REFERENCE   8  (residues 1 to 191)
  AUTHORS   Sugimoto,K., Yamada,T., Muro,Y. and Himeno,M.
  TITLE     Human homolog of Drosophila heterochromatin-associated protein 1
            (HP1) is a DNA-binding protein which possesses a DNA-binding motif
            with weak similarity to that of human centromere protein C (CENP-C)
  JOURNAL   J Biochem 120 (1), 153-159 (1996)
   PUBMED   8864858
REFERENCE   9  (residues 1 to 191)
  AUTHORS   Ye,Q. and Worman,H.J.
  TITLE     Interaction between an integral protein of the nuclear envelope
            inner membrane and human chromodomain proteins homologous to
            Drosophila HP1
  JOURNAL   J Biol Chem 271 (25), 14653-14656 (1996)
   PUBMED   8663349
REFERENCE   10 (residues 1 to 191)
  AUTHORS   Saunders,W.S., Chue,C., Goebl,M., Craig,C., Clark,R.F.,
            Powers,J.A., Eissenberg,J.C., Elgin,S.C., Rothfield,N.F. and
            Earnshaw,W.C.
  TITLE     Molecular cloning of a human homologue of Drosophila
            heterochromatin protein HP1 using anti-centromere autoantibodies
            with anti-chromo specificity
  JOURNAL   J Cell Sci 104 (Pt 2), 573-582 (1993)
   PUBMED   8505380
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DT217255.1, AK313506.1,
            AC078778.34 and BC030149.2.
            
            Summary: This gene encodes a highly conserved nonhistone protein,
            which is a member of the heterochromatin protein family. The
            protein is enriched in the heterochromatin and associated with
            centromeres. The protein has a single N-terminal chromodomain which
            can bind to histone proteins via methylated lysine residues, and a
            C-terminal chromo shadow-domain (CSD) which is responsible for the
            homodimerization and interaction with a number of
            chromatin-associated nonhistone proteins. The encoded product is
            involved in the formation of functional kinetochore through
            interaction with essential kinetochore proteins. The gene has a
            pseudogene located on chromosome 3. Multiple alternatively spliced
            variants, encoding the same protein, have been identified.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence and transcripts to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.57848.1,
                                           SRR1803611.143374.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145774
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..191
                     /product="chromobox protein homolog 5"
                     /note="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila); heterochromatin protein 1 homolog alpha;
                     antigen p25; HP1Hs alpha; HP1-ALPHA; epididymis luminal
                     protein 25; heterochromatin protein 1-alpha"
                     /calculated_mol_wt=22094
     Site            11
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Region          19..68
                     /region_name="CD_HP1alpha_Cbx5"
                     /note="chromodomain of heterochromatin protein 1 homolog
                     alpha; cd18651"
                     /db_xref="CDD:349298"
     Site            order(19..22,39,41,52,56..62)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:349298"
     Site            40
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13185; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Region          70..117
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P45973.1)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (P45973.1)"
     Region          116..173
                     /region_name="CSD_HP1alpha_Cbx5"
                     /note="chromo shadow domain of heterochromatin protein 1
                     homolog alpha; cd18655"
                     /db_xref="CDD:349302"
     Site            order(125,127..131,139,148,168,171..172)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:349302"
     Site            order(129,167..169,171..172)
                     /site_type="other"
                     /note="putative binding pit [polypeptide binding]"
                     /db_xref="CDD:349302"
     Site            order(157,161..162,164..165,168..169)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:349302"
     CDS             1..191
                     /gene="CBX5"
                     /gene_synonym="HEL25; HP1; HP1A; HP1alpha"
                     /coded_by="NM_001127322.1:319..894"
                     /db_xref="CCDS:CCDS8875.1"
                     /db_xref="GeneID:23468"
                     /db_xref="HGNC:HGNC:1555"
                     /db_xref="MIM:604478"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrv vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksesnkr ksnfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkeketak s
//
LOCUS       NP_803173                276 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-12 [Homo sapiens].
ACCESSION   NP_803173
VERSION     NP_803173.1
DBSOURCE    REFSEQ: accession NM_177424.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Ambrosio,A.L., Febvre,H.P. and Di Pietro,S.M.
  TITLE     Syntaxin 12 and COMMD3 are new factors that function with VPS33B in
            the biogenesis of platelet alpha-granules
  JOURNAL   Blood 139 (6), 922-935 (2022)
   PUBMED   34905616
  REMARK    GeneRIF: Syntaxin 12 and COMMD3 are new factors that function with
            VPS33B in the biogenesis of platelet alpha-granules.
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Bowman,S.L., Le,L., Zhu,Y., Harper,D.C., Sitaram,A., Theos,A.C.,
            Sviderskaya,E.V., Bennett,D.C., Raposo-Benedetti,G., Owen,D.J.,
            Dennis,M.K. and Marks,M.S.
  TITLE     A BLOC-1-AP-3 super-complex sorts a cis-SNARE complex into
            endosome-derived tubular transport carriers
  JOURNAL   J Cell Biol 220 (7) (2021)
   PUBMED   33886957
  REMARK    GeneRIF: A BLOC-1-AP-3 super-complex sorts a cis-SNARE complex into
            endosome-derived tubular transport carriers.
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 276)
  AUTHORS   McBride,H.M., Rybin,V., Murphy,C., Giner,A., Teasdale,R. and
            Zerial,M.
  TITLE     Oligomeric complexes link Rab5 effectors with NSF and drive
            membrane fusion via interactions between EEA1 and syntaxin 13
  JOURNAL   Cell 98 (3), 377-386 (1999)
   PUBMED   10458612
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Steegmaier,M., Yang,B., Yoo,J.S., Huang,B., Shen,M., Yu,S., Luo,Y.
            and Scheller,R.H.
  TITLE     Three novel proteins of the syntaxin/SNAP-25 family
  JOURNAL   J Biol Chem 273 (51), 34171-34179 (1998)
   PUBMED   9852078
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Prekeris,R., Klumperman,J., Chen,Y.A. and Scheller,R.H.
  TITLE     Syntaxin 13 mediates cycling of plasma membrane proteins via
            tubulovesicular recycling endosomes
  JOURNAL   J Cell Biol 143 (4), 957-971 (1998)
   PUBMED   9817754
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Advani,R.J., Bae,H.R., Bock,J.B., Chao,D.S., Doung,Y.C.,
            Prekeris,R., Yoo,J.S. and Scheller,R.H.
  TITLE     Seven novel mammalian SNARE proteins localize to distinct membrane
            compartments
  JOURNAL   J Biol Chem 273 (17), 10317-10324 (1998)
   PUBMED   9553086
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Tang,B.L., Tan,A.E., Lim,L.K., Lee,S.S., Low,D.Y. and Hong,W.
  TITLE     Syntaxin 12, a member of the syntaxin family localized to the
            endosome
  JOURNAL   J Biol Chem 273 (12), 6944-6950 (1998)
   PUBMED   9507000
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM148993.1, AL035306.1 and AF070635.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.156651.1,
                                           SRR1803611.83271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373943.9/ ENSP00000363054.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..276
                     /product="syntaxin-12"
                     /calculated_mol_wt=31511
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q86Y82.1)"
     Region          30..132
                     /region_name="Syntaxin_2"
                     /note="Syntaxin-like protein; pfam14523"
                     /db_xref="CDD:464199"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ER00; propagated from
                     UniProtKB/Swiss-Prot (Q86Y82.1)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86Y82.1)"
     Region          181..247
                     /region_name="SNARE_syntaxin12"
                     /note="SNARE motif of syntaxin 12; cd15876"
                     /db_xref="CDD:277229"
     Site            order(182,184..185,187..192,194..196,198..199,201..203,
                     205..206,208..210,212..213,215..220,222..227,229..234,
                     236..238)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277229"
     Site            212
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277229"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ER00; propagated from
                     UniProtKB/Swiss-Prot (Q86Y82.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ER00; propagated from
                     UniProtKB/Swiss-Prot (Q86Y82.1)"
     Site            249..269
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86Y82.1)"
     CDS             1..276
                     /gene="STX12"
                     /gene_synonym="STX13; STX14"
                     /coded_by="NM_177424.3:90..920"
                     /db_xref="CCDS:CCDS310.1"
                     /db_xref="GeneID:23673"
                     /db_xref="HGNC:HGNC:11430"
                     /db_xref="MIM:606892"
ORIGIN      
        1 msygpldmyr npgpsgpqlr dfssiiqtcs gniqrisqat aqiknlmsql gtkqdssklq
       61 enlqqlqhst nqlaketnel lkelgslplp lstseqrqqr lqkerlmndf saalnnfqav
      121 qrrvsekeke siararagsr lsaeerqree qlvsfdshee wnqmqsqede vaiteqdlel
      181 ikeretairq leadildvnq ifkdlammih dqgdlidsie anvessevhv erateqlqra
      241 ayyqkksrkk mcilvlvlsv iililgliiw lvyktk
//
LOCUS       NP_001304114             366 aa            linear   PRI 20-NOV-2025
DEFINITION  cadherin-1 isoform 3 [Homo sapiens].
ACCESSION   NP_001304114
VERSION     NP_001304114.1
DBSOURCE    REFSEQ: accession NM_001317185.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 366)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   2  (residues 1 to 366)
  AUTHORS   Dash,S., Biswas,J., Goswami,S., Mukherjee,S., Ganguli,N.,
            Duraivelan,K., Mondal,S., Mukhopadhyay,R. and Samanta,D.
  TITLE     Molecular Crosstalk Between Adherens Junction Proteins, E-cadherin
            and Nectin-4
  JOURNAL   J Mol Biol 436 (18), 168709 (2024)
   PUBMED   39009071
  REMARK    GeneRIF: Molecular Crosstalk Between Adherens Junction Proteins,
            E-cadherin and Nectin-4.
REFERENCE   3  (residues 1 to 366)
  AUTHORS   Peng,Y., Zhang,Y., Fang,R., Jiang,H., Lan,G., Xu,Z., Liu,Y.,
            Nie,Z., Ren,L., Wang,F., Zhang,S.D., Ma,Y., Yang,P., Ge,H.H.,
            Zhang,W.D., Luo,C., Li,A. and He,W.
  TITLE     Target Identification and Mechanistic Characterization of Indole
            Terpenoid Mimics: Proper Spindle Microtubule Assembly Is Essential
            for Cdh1-Mediated Proteolysis of CENP-A
  JOURNAL   Adv Sci (Weinh) 11 (29), e2305593 (2024)
   PUBMED   38873820
REFERENCE   4  (residues 1 to 366)
  AUTHORS   Yim,I.S. and Laronde,D.M.
  TITLE     Biomarkers of epithelial-mesenchymal transition: E-cadherin and
            beta-catenin in malignant transformation of oral lesions
  JOURNAL   Can J Dent Hyg 58 (2), 111-119 (2024)
   PUBMED   38974823
  REMARK    GeneRIF: Biomarkers of epithelial-mesenchymal transition:
            E-cadherin and beta-catenin in malignant transformation of oral
            lesions.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 366)
  AUTHORS   Lecuit,T. and Yap,A.S.
  TITLE     E-cadherin junctions as active mechanical integrators in tissue
            dynamics
  JOURNAL   Nat Cell Biol 17 (5), 533-539 (2015)
   PUBMED   25925582
  REMARK    Review article
REFERENCE   6  (residues 1 to 366)
  AUTHORS   Barbosa-Matos,R., Cordova,L., Schrader,K. and Oliveira,C.
  TITLE     Diffuse Gastric and Lobular Breast Cancer Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301318
REFERENCE   7  (residues 1 to 366)
  AUTHORS   Knudsen,K.A. and Wheelock,M.J.
  TITLE     Plakoglobin, or an 83-kD homologue distinct from beta-catenin,
            interacts with E-cadherin and N-cadherin
  JOURNAL   J Cell Biol 118 (3), 671-679 (1992)
   PUBMED   1639850
REFERENCE   8  (residues 1 to 366)
  AUTHORS   La Vecchia,C., Negri,E., Franceschi,S. and Gentile,A.
  TITLE     Family history and the risk of stomach and colorectal cancer
  JOURNAL   Cancer 70 (1), 50-55 (1992)
   PUBMED   1606546
REFERENCE   9  (residues 1 to 366)
  AUTHORS   Zanghieri,G., Di Gregorio,C., Sacchetti,C., Fante,R.,
            Sassatelli,R., Cannizzo,G., Carriero,A. and Ponz de Leon,M.
  TITLE     Familial occurrence of gastric cancer in the 2-year experience of a
            population-based registry
  JOURNAL   Cancer 66 (9), 2047-2051 (1990)
   PUBMED   2224804
REFERENCE   10 (residues 1 to 366)
  AUTHORS   Mansouri,A., Spurr,N., Goodfellow,P.N. and Kemler,R.
  TITLE     Characterization and chromosomal localization of the gene encoding
            the human cell adhesion molecule uvomorulin
  JOURNAL   Differentiation 38 (1), 67-71 (1988)
   PUBMED   3263290
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312551.1, AB025106.1,
            AC099314.3 and EU709494.1.
            
            Summary: This gene encodes a classical cadherin of the cadherin
            superfamily. Alternative splicing results in multiple transcript
            variants, at least one of which encodes a preproprotein that is
            proteolytically processed to generate the mature glycoprotein. This
            calcium-dependent cell-cell adhesion protein is comprised of five
            extracellular cadherin repeats, a transmembrane region and a highly
            conserved cytoplasmic tail. Mutations in this gene are correlated
            with gastric, breast, colorectal, thyroid and ovarian cancer. Loss
            of function of this gene is thought to contribute to cancer
            progression by increasing proliferation, invasion, and/or
            metastasis. The ectodomain of this protein mediates bacterial
            adhesion to mammalian cells and the cytoplasmic domain is required
            for internalization. This gene is present in a gene cluster with
            other members of the cadherin family on chromosome 16. [provided by
            RefSeq, Nov 2015].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in an exon in its 5' UTR, resulting in a different 5' UTR and the
            use of a downstream start site compared to variant 1. The encoded
            isoform (3) has a shorter N-terminus and lacks a predicted signal
            peptide compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB025106.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..366
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..366
                     /product="cadherin-1 isoform 3"
                     /note="calcium-dependent adhesion protein, epithelial;
                     cadherin 1, E-cadherin (epithelial); cell-CAM 120/80;
                     uvomorulin; epithelial cadherin; cadherin 1, type 1,
                     E-cadherin (epithelial); E-cadherin 1; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=40404
     Region          <3..75
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Region          82..170
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          302..361
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..366
                     /gene="CDH1"
                     /gene_synonym="Arc-1; BCDS1; CD324; CDHE; ECAD; LCAM; UVO"
                     /coded_by="NM_001317185.2:1740..2840"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:999"
                     /db_xref="HGNC:HGNC:1748"
                     /db_xref="MIM:192090"
ORIGIN      
        1 meqkityriw rdtanwlein pdtgaistra eldredfehv knstytalii atdngspvat
       61 gtgtlllils dvndnapipe prtiffcern pkpqviniid adlppntspf taelthgasa
      121 nwtiqyndpt qesiilkpkm alevgdykin lklmdnqnkd qvttlevsvc dcegaagvcr
      181 kaqpveaglq ipailgilgg ilallilill lllflrrrav vkepllpped dtrdnvyyyd
      241 eegggeedqd fdlsqlhrgl darpevtrnd vaptlmsvpr ylprpanpde ignfidenlk
      301 aadtdptapp ydsllvfdye gsgseaasls slnssesdkd qdydylnewg nrfkkladmy
      361 gggedd
//
LOCUS       NP_859056                104 aa            linear   PRI 20-NOV-2025
DEFINITION  complex III assembly factor LYRM7 isoform 1 [Homo sapiens].
ACCESSION   NP_859056
VERSION     NP_859056.2
DBSOURCE    REFSEQ: accession NM_181705.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 104)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 104)
  AUTHORS   Shinde,A., Chandak,N., Singh,J., Roy,M., Mane,M., Tang,X.,
            Vasiyani,H., Currim,F., Gohel,D., Shukla,S., Goyani,S.,
            Saranga,M.V., Brindley,D.N. and Singh,R.
  TITLE     TNF-alpha induced NF-kappaB mediated LYRM7 expression modulates the
            tumor growth and metastatic ability in breast cancer
  JOURNAL   Free Radic Biol Med 211, 158-170 (2024)
   PUBMED   38104742
  REMARK    GeneRIF: TNF-alpha induced NF-kappaB mediated LYRM7 expression
            modulates the tumor growth and metastatic ability in breast cancer.
REFERENCE   3  (residues 1 to 104)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 104)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 104)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 104)
  AUTHORS   Maio,N., Singh,A., Uhrigshardt,H., Saxena,N., Tong,W.H. and
            Rouault,T.A.
  TITLE     Cochaperone binding to LYR motifs confers specificity of iron
            sulfur cluster delivery
  JOURNAL   Cell Metab 19 (3), 445-457 (2014)
   PUBMED   24606901
REFERENCE   7  (residues 1 to 104)
  AUTHORS   Invernizzi,F., Tigano,M., Dallabona,C., Donnini,C., Ferrero,I.,
            Cremonte,M., Ghezzi,D., Lamperti,C. and Zeviani,M.
  TITLE     A homozygous mutation in LYRM7/MZM1L associated with early onset
            encephalopathy, lactic acidosis, and severe reduction of
            mitochondrial complex III activity
  JOURNAL   Hum Mutat 34 (12), 1619-1622 (2013)
   PUBMED   24014394
  REMARK    GeneRIF: LYRM7/MZM1L is a novel disease gene, causing
            cIII-defective, early onset, severe mitochondrial encephalopathy.
REFERENCE   8  (residues 1 to 104)
  AUTHORS   Sanchez,E., Lobo,T., Fox,J.L., Zeviani,M., Winge,D.R. and
            Fernandez-Vizarra,E.
  TITLE     LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of
            mitochondrial Complex III assembly in human cells
  JOURNAL   Biochim Biophys Acta 1827 (3), 285-293 (2013)
   PUBMED   23168492
REFERENCE   9  (residues 1 to 104)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 104)
  AUTHORS   Trynka,G., Zhernakova,A., Romanos,J., Franke,L., Hunt,K.A.,
            Turner,G., Bruinenberg,M., Heap,G.A., Platteel,M., Ryan,A.W., de
            Kovel,C., Holmes,G.K., Howdle,P.D., Walters,J.R., Sanders,D.S.,
            Mulder,C.J., Mearin,M.L., Verbeek,W.H., Trimble,V., Stevens,F.M.,
            Kelleher,D., Barisani,D., Bardella,M.T., McManus,R., van Heel,D.A.
            and Wijmenga,C.
  TITLE     Coeliac disease-associated risk variants in TNFAIP3 and REL
            implicate altered NF-kappaB signalling
  JOURNAL   Gut 58 (8), 1078-1083 (2009)
   PUBMED   19240061
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK000803.1 and AC005179.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 6, 2006 this sequence version replaced NP_859056.1.
            
            Summary: Inner mitochondrial membrane complex III (CIII) is the
            main enzyme complex in the mitochondrial respiratory chain, and
            Rieske Fe-S protein (UQCRFS1) is the last catalytic subunit added
            to the complex. The protein encoded by this gene is a
            nuclear-encoded mitochondrial matrix protein that stabilizes
            UQCRFS1 and chaperones it to the CIII complex. Defects in this gene
            are a cause of mitochondrial complex III deficiency, nuclear type
            8. Three transcript variants encoding two different isoforms have
            been found for this gene. [provided by RefSeq, Jun 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.179279.1,
                                           SRR1803611.212805.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379380.9/ ENSP00000368688.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.3-q31.1"
     Protein         1..104
                     /product="complex III assembly factor LYRM7 isoform 1"
                     /note="LYR motif-containing protein 7; Lyrm7 homolog;
                     complex III assembly factor LYRM7"
                     /calculated_mol_wt=11824
     Region          7..77
                     /region_name="Complex1_LYR_LYRM7"
                     /note="LYR (leucine-tyrosine-arginine) motif found in LYR
                     motif-containing protein 7 (LYRM7) and similar proteins;
                     cd20267"
                     /db_xref="CDD:380762"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5U5X0.1)"
     CDS             1..104
                     /gene="LYRM7"
                     /gene_synonym="C5orf31; MC3DN8; MZM1L"
                     /coded_by="NM_181705.4:78..392"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4148.1"
                     /db_xref="GeneID:90624"
                     /db_xref="HGNC:HGNC:28072"
                     /db_xref="MIM:615831"
ORIGIN      
        1 mgravkvlql fktlhrtrqq vfkndarale aarikineef knnksetssk kieelmkigs
       61 dvelllrtsv iqgihtdhnt lklvprkdll venvpycdap tqkq
//
LOCUS       NP_001340035             369 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            1 [Homo sapiens].
ACCESSION   NP_001340035
VERSION     NP_001340035.1
DBSOURCE    REFSEQ: accession NM_001353106.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107982.6 and AC090286.16.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.118317.1,
                                           SRR1660803.79271.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..369
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 1"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=40795
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Region          20..138
                     /region_name="Pribosyltran_N"
                     /note="N-terminal domain of ribose phosphate
                     pyrophosphokinase; pfam13793"
                     /db_xref="CDD:433483"
     Region          179..363
                     /region_name="Pribosyl_synth"
                     /note="Phosphoribosyl synthetase-associated domain;
                     pfam14572"
                     /db_xref="CDD:434046"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O60256.1)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60256.1)"
     CDS             1..369
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001353106.2:265..1374"
                     /note="isoform 1 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS11200.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mfcvtppele tkmnitkggl vlfsansnss cmelskkiae rlgvemgkvq vyqepnretr
       61 vqiqesvrgk dvfiiqtvsk dvnttimell imvyacktsc aksiigvipy fpyskqckmr
      121 krgsivskll asmmckaglt hlitmdlhqk eiqgffnipv dnlraspfll qyiqeeipdy
      181 rnavivaksp asakraqsfa erlrlgiavi hgeaqdaesd lvdgrhsppm vrsvaaihps
      241 leipmlipke kppitvvgdv ggriaiivdd iiddvdsfla aaetlkerga ykifvmathg
      301 llssdaprri eesaidevvv tntiphevqk lqcpkiktvd ismilseair rihngesmsy
      361 lfrnigldd
//
LOCUS       NP_001293073             673 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001293073 XP_005274825
VERSION     NP_001293073.1
DBSOURCE    REFSEQ: accession NM_001306144.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 673)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 673)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 673)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 673)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 673)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 16, 2015 this sequence version replaced XP_005274825.1.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK226109.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000445323.7/ ENSP00000414178.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..673
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 1"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=75587
     Region          1..51
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13613.4)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q13613.4)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13613.4)"
     Site            49
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2C4; propagated from
                     UniProtKB/Swiss-Prot (Q13613.4)"
     Region          115..214
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          231..557
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     Region          616..673
                     /region_name="Required for dimerization.
                     /evidence=ECO:0000269|PubMed:27018598"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13613.4)"
     Region          650..673
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13613.4)"
     CDS             1..673
                     /gene="MTMR1"
                     /coded_by="NM_001306144.3:136..2157"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS78512.1"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 mdrpaaaaaa gceggggpnp gpaggrrppr aaggatagsr qpsvetldsp tgshvewckq
       61 liaatissqi sgsvtsenvs rdykvfrrpd lralrdgnkl aqmeeaplfp gesikaivkd
      121 vmyicpfmga vsgtltvtdf klyfknverd phfildvplg visrvekiga qshgdnscgi
      181 eivckdmrnl rlaykqeeqs klgifenlnk hafplsngqa lfafsykekf pingwkvydp
      241 vseykrqglp neswkiskin snyefcdtyp aiivvptsvk dddlskvaaf rakgrvpvls
      301 wihpesqati trcsqplvgp ndkrckedek ylqtimdana qshkliifda rqnsvadtnk
      361 tkgggyeses aypnaelvfl eihnihvmre slrklkeivy psidearwls nvdgthwley
      421 irmllagavr iadkiesgkt svvvhcsdgw drtaqltsla mlmldsyyrt ikgfetlvek
      481 ewisfghrfa lrvghgndnh adadrspifl qfvdcvwqmt rqfpsafefn elflitildh
      541 lysclfgtfl cnceqqrfke dvytktislw syinsqldef snpffvnyen hvlypvasls
      601 hlelwvnyyv rwnprmrpqm pihqnlkell avraelqkrv eglqrevatr avssssergs
      661 spshsatsvh tsv
//
LOCUS       NP_001127808             758 aa            linear   PRI 20-NOV-2025
DEFINITION  striatin-interacting protein 2 isoform b [Homo sapiens].
ACCESSION   NP_001127808
VERSION     NP_001127808.1
DBSOURCE    REFSEQ: accession NM_001134336.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Pan,J., Zhang,Y., He,L., Wu,Y., Xiao,W., Zhang,J. and Xu,Y.
  TITLE     STRIP2 is regulated by the transcription factor Sp1 and promotes
            lung adenocarcinoma progression via activating the
            PI3K/AKT/mTOR/MYC signaling pathway
  JOURNAL   Genomics 116 (5), 110923 (2024)
   PUBMED   39191354
  REMARK    GeneRIF: STRIP2 is regulated by the transcription factor Sp1 and
            promotes lung adenocarcinoma progression via activating the
            PI3K/AKT/mTOR/MYC signaling pathway.
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Zhang,X., Chen,Q., He,Y., Shi,Q., Yin,C., Xie,Y., Yu,H., Bao,Y.,
            Wang,X., Tang,C. and Dong,Z.
  TITLE     STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent
  JOURNAL   J Exp Clin Cancer Res 42 (1), 19 (2023)
   PUBMED   36639675
  REMARK    GeneRIF: STRIP2 motivates non-small cell lung cancer progression by
            modulating the TMBIM6 stability through IGF2BP3 dependent.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Jeong,B.C., Bae,S.J., Ni,L., Zhang,X., Bai,X.C. and Luo,X.
  TITLE     Cryo-EM structure of the Hippo signaling integrator human STRIPAK
  JOURNAL   Nat Struct Mol Biol 28 (3), 290-299 (2021)
   PUBMED   33633399
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Qiu,L.M., Sun,Y.H., Chen,T.T., Chen,J.J. and Ma,H.T.
  TITLE     STRIP2, a member of the striatin-interacting phosphatase and kinase
            complex, is implicated in lung adenocarcinoma cell growth and
            migration
  JOURNAL   FEBS Open Bio 10 (3), 351-361 (2020)
   PUBMED   31901223
  REMARK    GeneRIF: STRIP2, a member of the striatin-interacting phosphatase
            and kinase complex, is implicated in lung adenocarcinoma cell
            growth and migration.
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Suryavanshi,N., Furmston,J. and Ridley,A.J.
  TITLE     The STRIPAK complex components FAM40A and FAM40B regulate
            endothelial cell contractility via ROCKs
  JOURNAL   BMC Cell Biol 19 (1), 26 (2018)
   PUBMED   30509168
  REMARK    GeneRIF: These results demonstrate the importance of the FAM40
            proteins for endothelial cell physiology, and suggest that they act
            as part of the CCM3-containing STRIPAK complex.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Lisa-Santamaria,P., Jimenez,A. and Revuelta,J.L.
  TITLE     The protein factor-arrest 11 (Far11) is essential for the toxicity
            of human caspase-10 in yeast and participates in the regulation of
            autophagy and the DNA damage signaling
  JOURNAL   J Biol Chem 287 (35), 29636-29647 (2012)
   PUBMED   22782902
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Pracheil,T., Thornton,J. and Liu,Z.
  TITLE     TORC2 signaling is antagonized by protein phosphatase 2A and the
            Far complex in Saccharomyces cerevisiae
  JOURNAL   Genetics 190 (4), 1325-1339 (2012)
   PUBMED   22298706
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Bai,S.W., Herrera-Abreu,M.T., Rohn,J.L., Racine,V., Tajadura,V.,
            Suryavanshi,N., Bechtel,S., Wiemann,S., Baum,B. and Ridley,A.J.
  TITLE     Identification and characterization of a set of conserved and new
            regulators of cytoskeletal organization, cell morphology and
            migration
  JOURNAL   BMC Biol 9, 54 (2011)
   PUBMED   21834987
  REMARK    Erratum:[BMC Biol. 2024 Oct 10;22(1):228. doi:
            10.1186/s12915-024-02036-3. PMID: 39390519]
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 758)
  AUTHORS   Goudreault,M., D'Ambrosio,L.M., Kean,M.J., Mullin,M.J.,
            Larsen,B.G., Sanchez,A., Chaudhry,S., Chen,G.I., Sicheri,F.,
            Nesvizhskii,A.I., Aebersold,R., Raught,B. and Gingras,A.C.
  TITLE     A PP2A phosphatase high density interaction network identifies a
            novel striatin-interacting phosphatase and kinase complex linked to
            the cerebral cavernous malformation 3 (CCM3) protein
  JOURNAL   Mol Cell Proteomics 8 (1), 157-171 (2009)
   PUBMED   18782753
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Kemp,H.A. and Sprague,G.F. Jr.
  TITLE     Far3 and five interacting proteins prevent premature recovery from
            pheromone arrest in the budding yeast Saccharomyces cerevisiae
  JOURNAL   Mol Cell Biol 23 (5), 1750-1763 (2003)
   PUBMED   12588993
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009244.25, DA409007.1 and BC019064.2.
            
            Transcript Variant: This variant (2) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (b)
            has a shorter and distinct C-terminus compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC019064.2, SRR1660803.165089.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.1"
     Protein         1..758
                     /product="striatin-interacting protein 2 isoform b"
                     /note="homolog of yeast FAR11 protein 2; protein FAM40B;
                     family with sequence similarity 40, member B; FAR11 factor
                     arrest 11 homolog B"
                     /calculated_mol_wt=85887
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          49..291
                     /region_name="N1221"
                     /note="N1221-like protein; pfam07923"
                     /db_xref="CDD:429737"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          321..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          360..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULQ0.2)"
     Region          456..751
                     /region_name="DUF3402"
                     /note="Domain of unknown function (DUF3402); pfam11882"
                     /db_xref="CDD:463384"
     CDS             1..758
                     /gene="STRIP2"
                     /gene_synonym="FAM40B; FAR11B"
                     /coded_by="NM_001134336.2:42..2318"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47709.1"
                     /db_xref="GeneID:57464"
                     /db_xref="HGNC:HGNC:22209"
                     /db_xref="MIM:617919"
ORIGIN      
        1 medpaapgtg gppangngng ggkgkqaapk greafrsqrr esegsvdcpt lefeygdadg
       61 haaelselys ytenleftnn rrcfeedfkt qvqgkewlel eedaqkayim glldrlevvs
      121 rerrlkvara vlylaqgtfg ecdsevdvlh wsryncflly qmgtfstfle llhmeidnsq
      181 acssalrkpa vsiadstelr vllsvmylmv enirleretd pcgwrtaret frtelsfsmh
      241 neepfalllf smvtkfcsgl aphfpikkvl lllwkvvmft lggfehlqtl kvqkraelgl
      301 pplaedsiqv vksmraaspp sytldlgesq lapppsklrg rrgsrrqllt kqdsldiyne
      361 rdlfkteepa teeeeesagd gertldgeld lleqdplvpp ppsqaplsae rvafpkglpw
      421 apkvrqkdie hflemsrnkf igftlgqdtd tlvglprpih esvktlkqhk yisiadvqik
      481 neeelekcpm slgeevvpet pceilyqgml yslpqymial lkillaaapt skaktdsini
      541 ladvlpeemp itvlqsmklg idvnrhkeii vksistllll llkhfklnhi yqfeyvsqhl
      601 vfanciplil kffnqnilsy itaknsisvl dypcctiqdl peltteslea gdnsqfcwrn
      661 lfscinllrl lnkltkwkhs rtmmlvvfks apilkralkv kqamlqlyvl kllklqtkyl
      721 grqwrksnmk tmsaiyqkvr hrmnddwayg ngessqss
//
LOCUS       NP_001352599            1173 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001352599
VERSION     NP_001352599.1
DBSOURCE    REFSEQ: accession NM_001365670.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1173)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1173)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1173)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1173)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1173)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1173)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1173)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1173)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1173)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1173)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.228034.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1173
                     /product="cordon-bleu protein-like 1 isoform 5"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=128386
     Region          106..172
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Region          190..268
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          <834..1071
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1122..1147
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1126..1127,1129..1131,1133..1135,1143..1146)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1143..1146
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     CDS             1..1173
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001365670.2:33..3554"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mppswsplmc graaeaaass rtpgremgqa vtrrlgagar aaprramdgr tprpqdapar
       61 rkpkakaplp paetkytdvs saadsvesta fimeqkenmi dkdvelsvvl pgdiiksttv
      121 hgskpmmdll iflcaqyhln pssytidlls aeqnhikfkp ntpigmleve kvilkpkmld
      181 kkkptpiipe ktvrvvinfk ktqktivrvs phaslqelap iicskcefdp lhtlllkdyq
      241 sqepldltks lndlglrely amdvnrescq isqnldimke kenkgffsff qrskkkrdqt
      301 asapatplvn khrptftrsn tiskpyisnt lpsdapkkrr aplppmpasq svpqdlahiq
      361 erpascivks msvdetdksp ceagrvrags lqlssmsagn sslrrtkrka psppskipph
      421 qsdensrvta lqpvdgvppd saseanspee lsspagissd ysleeideke elsevpkvea
      481 enispksqdi pfvstdiint lkndpdsalg ngsgefsqns meekqetkst dgqephsvvy
      541 dtsngkkvvd sirnlkslgp nqenvqneii vypentednm kngvkktein vegvaknnni
      601 dmeverpsns eahetdtais ykenhlaass vpdqklnqps aektkdaaiq ttpscnsfdg
      661 khqdhnlsds kveecvqtsn nnistqhscl ssqdsvntsr efrsqgtlii hsedpltvkd
      721 picahgnddl lppvdridkn stasylknyp lyrqdynpkp kpsneitrey ipkigmttyk
      781 ivppksleis kdwqsetiey kddqdmhalg kkhthenvke taiqtedsai sespeeplpn
      841 lkpkpnlrte hqvpssvssp ddamvsplkp apkmtrdtgt apfapnleei nnileskfks
      901 rasnaqakps sfflqmqkrv sghyvtsaaa ksvhaapnpa pkeltnkeae rdmlpspeqt
      961 lsplskmphs vpqplvektd ddvigqapae aspppiapkp vtipasqvst qnlktlktfg
     1021 aprpysssgp spfalavvkr sqsfskerte spsasalvqp panteegkth svnkfvdipq
     1081 lgvsdkenns ahneqnsqip tptdgpsftv mrqssltfqs sdpeqmrqsl ltairsgeaa
     1141 aklkrvtips ntisvngrsr lshsmspdaq dgh
//
LOCUS       NP_060315                183 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 8 isoform 1 [Homo sapiens].
ACCESSION   NP_060315
VERSION     NP_060315.1
DBSOURCE    REFSEQ: accession NM_017845.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Vinayagam,A., Stelzl,U., Foulle,R., Plassmann,S., Zenkner,M.,
            Timm,J., Assmus,H.E., Andrade-Navarro,M.A. and Wanker,E.E.
  TITLE     A directed protein interaction network for investigating
            intracellular signal transduction
  JOURNAL   Sci Signal 4 (189), rs8 (2011)
   PUBMED   21900206
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107398.4.
            
            Summary: The protein encoded by this gene binds coiled-coil
            domain-containing protein 22 (CCDC22), and this complex can
            regulate the turnover of I-kappa-B and the activation of
            NF-kappa-B. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2259041.1, BC008371.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381571.6/ ENSP00000370984.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p12"
     Protein         1..183
                     /product="COMM domain-containing protein 8 isoform 1"
                     /note="COMM domain-containing protein 8"
                     /calculated_mol_wt=20959
     Region          7..182
                     /region_name="Commd8"
                     /note="COMM_Domain containing protein 8. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04756"
                     /db_xref="CDD:240104"
     CDS             1..183
                     /gene="COMMD8"
                     /coded_by="NM_017845.5:52..603"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3475.1"
                     /db_xref="GeneID:54951"
                     /db_xref="HGNC:HGNC:26036"
                     /db_xref="MIM:616656"
ORIGIN      
        1 mepeegtplw rlqklpaelg pqllhkiidg icgraypvyq dyhtvwesee wmhvlediak
       61 ffkaivgknl pdeeifqqln qlnslhqeti mkcvksrkde ikqalsreiv aissaqlqdf
      121 dwqvklalss dkiaalrmpl lslhldvken gevkpysiem sreelqnliq sleaankvvl
      181 qlk
//
LOCUS       NP_060710                757 aa            linear   PRI 20-NOV-2025
DEFINITION  kin of IRRE-like protein 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_060710
VERSION     NP_060710.3
DBSOURCE    REFSEQ: accession NM_018240.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Wang,T., Chen,S., Wang,Z., Li,S., Fei,X., Wang,T. and Zhang,M.
  TITLE     KIRREL promotes the proliferation of gastric cancer cells and
            angiogenesis through the PI3K/AKT/mTOR pathway
  JOURNAL   J Cell Mol Med 28 (1), e18020 (2024)
   PUBMED   37909722
  REMARK    GeneRIF: KIRREL promotes the proliferation of gastric cancer cells
            and angiogenesis through the PI3K/AKT/mTOR pathway.
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Gu,Y., Wang,Y., Sha,Z., He,C., Zhu,Y., Li,J., Yu,A., Zhong,Z.,
            Wang,X., Sun,Y., Lan,F. and Yu,F.X.
  TITLE     Transmembrane protein KIRREL1 regulates Hippo signaling via a
            feedback loop and represents a therapeutic target in YAP/TAZ-active
            cancers
  JOURNAL   Cell Rep 40 (9), 111296 (2022)
   PUBMED   36044856
  REMARK    GeneRIF: Transmembrane protein KIRREL1 regulates Hippo signaling
            via a feedback loop and represents a therapeutic target in
            YAP/TAZ-active cancers.
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Paul,A., Annunziato,S., Lu,B., Sun,T., Evrova,O., Planas-Paz,L.,
            Orsini,V., Terracciano,L.M., Charlat,O., Loureiro,Z.Y., Ji,L.,
            Zamponi,R., Sigoillot,F., Lei,H., Lindeman,A., Russ,C.,
            Reece-Hoyes,J.S., Nicholson,T.B., Tchorz,J.S. and Cong,F.
  TITLE     Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo
            signaling recruiting SAV1 to cell-cell contact sites
  JOURNAL   Nat Commun 13 (1), 930 (2022)
   PUBMED   35177623
  REMARK    GeneRIF: Cell adhesion molecule KIRREL1 is a feedback regulator of
            Hippo signaling recruiting SAV1 to cell-cell contact sites.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Barletta,G.M., Kovari,I.A., Verma,R.K., Kerjaschki,D. and
            Holzman,L.B.
  TITLE     Nephrin and Neph1 co-localize at the podocyte foot process
            intercellular junction and form cis hetero-oligomers
  JOURNAL   J Biol Chem 278 (21), 19266-19271 (2003)
   PUBMED   12646566
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Huber,T.B., Schmidts,M., Gerke,P., Schermer,B., Zahn,A.,
            Hartleben,B., Sellin,L., Walz,G. and Benzing,T.
  TITLE     The carboxyl terminus of Neph family members binds to the PDZ
            domain protein zonula occludens-1
  JOURNAL   J Biol Chem 278 (15), 13417-13421 (2003)
   PUBMED   12578837
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Gerke,P., Huber,T.B., Sellin,L., Benzing,T. and Walz,G.
  TITLE     Homodimerization and heterodimerization of the glomerular podocyte
            proteins nephrin and NEPH1
  JOURNAL   J Am Soc Nephrol 14 (4), 918-926 (2003)
   PUBMED   12660326
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Sellin,L., Huber,T.B., Gerke,P., Quack,I., Pavenstadt,H. and
            Walz,G.
  TITLE     NEPH1 defines a novel family of podocin interacting proteins
  JOURNAL   FASEB J 17 (1), 115-117 (2003)
   PUBMED   12424224
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Donoviel,D.B., Freed,D.D., Vogel,H., Potter,D.G., Hawkins,E.,
            Barrish,J.P., Mathur,B.N., Turner,C.A., Geske,R., Montgomery,C.A.,
            Starbuck,M., Brandt,M., Gupta,A., Ramirez-Solis,R., Zambrowicz,B.P.
            and Powell,D.R.
  TITLE     Proteinuria and perinatal lethality in mice lacking NEPH1, a novel
            protein with homology to NEPHRIN
  JOURNAL   Mol Cell Biol 21 (14), 4829-4836 (2001)
   PUBMED   11416156
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC109192.1, AL139010.29 and AA628934.1.
            
            On Jan 31, 2008 this sequence version replaced NP_060710.2.
            
            Summary: NEPH1 is a member of the nephrin-like protein family,
            which includes NEPH2 (MIM 607761) and NEPH3 (MIM 607762). The
            cytoplasmic domains of these proteins interact with the C terminus
            of podocin (NPHS2; MIM 604766), and the genes are expressed in
            kidney podocytes, cells involved in ensuring size- and
            charge-selective ultrafiltration (Sellin et al., 2003 [PubMed
            12424224]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC109193.1, DRR138518.504189.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359209.11/ ENSP00000352138.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.1"
     Protein         1..757
                     /product="kin of IRRE-like protein 1 isoform 1 precursor"
                     /note="nephrin related; kin of IRRE-like protein 1;
                     nephrin-like protein 1; kin of irregular chiasm-like
                     protein 1; kin of IRRE like"
                     /calculated_mol_wt=81715
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1839
     mat_peptide     17..757
                     /product="Kin of IRRE-like protein 1. /id=PRO_0000015093"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J84.2)"
                     /calculated_mol_wt=81715
     Region          22..116
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          38..42
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Site            46
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          51..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          78..87
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          97..102
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          109..112
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          122..219
                     /region_name="IgI_2_KIRREL3-like"
                     /note="Second immunoglobulin (Ig)-like domain of Kirrel
                     (kin of irregular chiasm-like) 3, and similar domains;
                     member of the I-set of Ig superfamily (IgSF) domains;
                     cd05759"
                     /db_xref="CDD:409416"
     Region          123..126
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409416"
     Region          129..133
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409416"
     Region          140..147
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409416"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          152..157
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409416"
     Region          160..162
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409416"
     Region          165..172
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409416"
     Region          179..187
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409416"
     Region          196..204
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409416"
     Region          210..216
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409416"
     Region          222..291
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            297
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          308..373
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          391..488
                     /region_name="IgI_5_KIRREL3"
                     /note="Fifth immunoglobulin (Ig)-like domain of Kirrel
                     (kin of irregular chiasm-like) 3 protein; member of the
                     I-set of Ig superfamily (IgSF) domains; cd05898"
                     /db_xref="CDD:409479"
     Region          392..396
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409479"
     Region          398..401
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409479"
     Region          405..407
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          409..416
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409479"
     Region          423..428
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409479"
     Region          430..433
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409479"
     Region          441..448
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409479"
     Region          451..458
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409479"
     Region          469..476
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409479"
     Site            471
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          479..486
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409479"
     Site            500..520
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000250|UniProtKB:Q6X936; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by FYN.
                     /evidence=ECO:0000250|UniProtKB:Q6X936; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            622
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            625
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     Region          649..679
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96J84.2)"
     Site            724
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15144186; propagated from
                     UniProtKB/Swiss-Prot (Q96J84.2)"
     CDS             1..757
                     /gene="KIRREL1"
                     /gene_synonym="KIRREL; NEPH1; NPHS23"
                     /coded_by="NM_018240.7:33..2306"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1172.2"
                     /db_xref="GeneID:55243"
                     /db_xref="HGNC:HGNC:15734"
                     /db_xref="MIM:607428"
ORIGIN      
        1 mlsllvwilt lsdtfsqgtq trfsqepadq tvvagqravl pcvllnysgi vqwtkdglal
       61 gmgqglkawp ryrvvgsada gqynleitda elsddasyec qateaalrsr rakltvlipp
      121 edtridggpv illqagtphn ltcrafnakp aatiiwfrdg tqqegavast ellkdgkret
      181 tvsqllinpt dldigrvftc rsmneaipsg ketsieldvh hpptvtlsie pqtvqegerv
      241 vftcqatanp eilgyrwakg gfliedahes ryetnvdysf ftepvscevh nkvgstnvst
      301 lvnvhfapri vvdpkptttd igsdvtltcv wvgnppltlt wtkkdsnmvl snsnqlllks
      361 vtqadagtyt craivprigv aerevplyvn gppiisseav qyavrgdggk vecfigstpp
      421 pdriawawke nflevgtler ytvertnsgs gvlstltinn vmeadfqthy nctawnsfgp
      481 gtaiiqleer evlpvgiiag atigasilli fffialvffl yrrrkgsrkd vtlrkldikv
      541 etvnrepltm hsdreddtas vstatrvmka iyssfkddvd lkqdlrcdti dtreeyemkd
      601 ptngyynvra hedrpssrav lyadyrapgp arfdgrpssr lshssgyaql ntysrgpasd
      661 ygpeptppgp aapagtdtts qlsyenyekf nshpfpgaag yptyrlgypq appsglertp
      721 yeaydpigky atatrfsyts qhsdygqrfq qrmqthv
//
LOCUS       NP_001397                340 aa            linear   PRI 20-NOV-2025
DEFINITION  ephrin-B3 precursor [Homo sapiens].
ACCESSION   NP_001397
VERSION     NP_001397.1
DBSOURCE    REFSEQ: accession NM_001406.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Qiao,Z., Liao,M., Xiao,M., Luo,S., Wang,K., Niu,M., Jiang,H.,
            Sun,S., Xu,G., Xu,N., Xu,Q. and Liu,Y.
  TITLE     Ephrin B3 exacerbates colitis and colitis-associated colorectal
            cancer
  JOURNAL   Biochem Pharmacol 220, 116004 (2024)
   PUBMED   38142837
  REMARK    GeneRIF: Ephrin B3 exacerbates colitis and colitis-associated
            colorectal cancer.
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Garcia-Diaz,B., Bachelin,C., Coulpier,F., Gerschenfeld,G.,
            Deboux,C., Zujovic,V., Charnay,P., Topilko,P. and Baron-Van
            Evercooren,A.
  TITLE     Blood vessels guide Schwann cell migration in the adult
            demyelinated CNS through Eph/ephrin signaling
  JOURNAL   Acta Neuropathol 138 (3), 457-476 (2019)
   PUBMED   31011859
  REMARK    GeneRIF: Blood vessels guide Schwann cell migration in the adult
            demyelinated CNS through Eph/ephrin signaling.
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Wu,T., Zhang,B.Q., Raelson,J., Yao,Y.M., Wu,H.D., Xu,Z.X.,
            Marois-Blanchet,F.C., Tahir,M.R., Wang,Y., Bradley,W.E., Luo,H.,
            Wu,J., Sheng,J.Z. and Hu,S.J.
  TITLE     Analysis of the association of EPHB6, EFNB1 and EFNB3 variants with
            hypertension risks in males with hypogonadism
  JOURNAL   Sci Rep 8 (1), 14497 (2018)
   PUBMED   30262919
  REMARK    GeneRIF: Analysis of the association of EPHB6, EFNB1 and EFNB3
            variants with hypertension risks in males with hypogonadism.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Bergemann,A.D., Zhang,L., Chiang,M.K., Brambilla,R., Klein,R. and
            Flanagan,J.G.
  TITLE     Ephrin-B3, a ligand for the receptor EphB3, expressed at the
            midline of the developing neural tube
  JOURNAL   Oncogene 16 (4), 471-480 (1998)
   PUBMED   9484836
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Tang,X.X., Pleasure,D.E. and Ikegaki,N.
  TITLE     cDNA cloning, chromosomal localization, and expression pattern of
            EPLG8, a new member of the EPLG gene family encoding ligands of
            EPH-related protein-tyrosine kinase receptors
  JOURNAL   Genomics 41 (1), 17-24 (1997)
   PUBMED   9126477
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Gale,N.W., Flenniken,A., Compton,D.C., Jenkins,N., Copeland,N.G.,
            Gilbert,D.J., Davis,S., Wilkinson,D.G. and Yancopoulos,G.D.
  TITLE     Elk-L3, a novel transmembrane ligand for the Eph family of receptor
            tyrosine kinases, expressed in embryonic floor plate, roof plate
            and hindbrain segments
  JOURNAL   Oncogene 13 (6), 1343-1352 (1996)
   PUBMED   8808709
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ892951.1, U57001.1, U66406.1
            and BC022499.1.
            
            Summary:  EFNB3, a member of the ephrin gene family, is important
            in brain development as well as in its maintenance. Moreover, since
            levels of EFNB3 expression were particularly high in several
            forebrain subregions compared to other brain subregions, it may
            play a pivotal role in forebrain function.  The EPH and EPH-related
            receptors comprise the largest subfamily of receptor
            protein-tyrosine kinases and have been implicated in mediating
            developmental events, particularly in the nervous system. EPH
            Receptors typically have a single kinase domain and an
            extracellular region containing a Cys-rich domain and 2 fibronectin
            type III repeats. The ephrin ligands and receptors have been named
            by the Eph Nomenclature Committee (1997). Based on their structures
            and sequence relationships, ephrins are divided into the ephrin-A
            (EFNA) class, which are anchored to the membrane by a
            glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB)
            class, which are transmembrane proteins. The Eph family of
            receptors are similarly divided into 2 groups based on the
            similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042944.2, U66406.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226091.3/ ENSP00000226091.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..340
                     /product="ephrin-B3 precursor"
                     /note="eph-related receptor tyrosine kinase ligand 8;
                     EPH-related receptor transmembrane ligand ELK-L3"
                     /calculated_mol_wt=33342
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2511
     mat_peptide     28..340
                     /product="ephrin-B3"
                     /calculated_mol_wt=33342
     Region          31..168
                     /region_name="Cupredoxin"
                     /note="Cupredoxin superfamily; cl19115"
                     /db_xref="CDD:473140"
     Region          168..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Site            210
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Region          254..298
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     Site            271
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35393; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15768.1)"
     Region          338..340
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15768.1)"
     CDS             1..340
                     /gene="EFNB3"
                     /gene_synonym="EFL6; EPLG8; LERK8"
                     /coded_by="NM_001406.4:398..1420"
                     /db_xref="CCDS:CCDS11120.1"
                     /db_xref="GeneID:1949"
                     /db_xref="HGNC:HGNC:3228"
                     /db_xref="MIM:602297"
ORIGIN      
        1 mgpphsgpgg vrvgallllg vlglvsglsl epvywnsank rfqaeggyvl ypqigdrldl
       61 lcprarppgp hsspnyefyk lylvggaqgr rceappapnl lltcdrpdld lrftikfqey
      121 spnlwghefr shhdyyiiat sdgtregles lqggvcltrg mkvllrvgqs prggavprkp
      181 vsempmerdr gaahslepgk enlpgdptsn atsrgaegpl pppsmpavag aagglallll
      241 gvagaggamc wrrrrakpse srhpgpgsfg rggslglggg ggmgpreaep gelgialrgg
      301 gaadppfcph yekvsgdygh pvyivqdgpp qsppniyykv
//
LOCUS       NP_001307569             513 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 11 [Homo sapiens].
ACCESSION   NP_001307569 XP_006712493
VERSION     NP_001307569.1
DBSOURCE    REFSEQ: accession NM_001320640.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL713697.1, AL537027.3,
            DR761993.1, BC004101.2 and BM711160.1.
            
            On Mar 2, 2016 this sequence version replaced XP_006712493.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (11) lacks three alternate
            in-frame exons compared to variant 1. The resulting isoform (11)
            has the same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.737783.1,
                                           SRR11853560.16475.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..513
                     /product="myc box-dependent-interacting protein 1 isoform
                     11"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=56327
     Region          2..122
                     /region_name="Interaction with BIN2.
                     /evidence=ECO:0000269|PubMed:10903846"
                     /note="propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Region          31..272
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,228,231..232,234,239..240,242..243,246..247,
                     249..250,253..254,256..257,261,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          280..354
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00499.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O00499.1)"
     Region          441..512
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(452..458,477,479..482,505,507..508)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..513
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_001320640.2:212..1753"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakpvsllek
      181 aapqwcqgkl qahlvaqtnl lrnqaeeeli kaqkvfeemn vdlqeelpsl wnsrvgfyvn
      241 tfqsiaglee nfhkemskln qnlndvlvgl ekqhgsntft vkaqpsdnap akgnkspspp
      301 dgspaatpei rvnhepepag gatpgatlpk spsqlrkgpp vppppkhtps kevkqeqils
      361 lfedtfvpei svttpsqpae asevaggtqp aagaqepget aaseaasssl pavvvetfpa
      421 tvngtveggs gagrldlppg fmfkvqaqhd ytatdtdelq lkagdvvlvi pfqnpeeqde
      481 gwlmgvkesd wnqhkelekc rgvfpenfte rvp
//
LOCUS       NP_001354630             752 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform lll [Homo sapiens].
ACCESSION   NP_001354630
VERSION     NP_001354630.1
DBSOURCE    REFSEQ: accession NM_001367701.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2151741,
                              SAMEA2153733 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..752
                     /product="SUN domain-containing protein 1 isoform lll"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=83201
     Region          12..269
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <343..>539
                     /region_name="rad50"
                     /note="TIGR00606"
                     /db_xref="CDD:129694"
     Region          385..437
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(387..388,391,394..395,398..399,401..402,405..406,
                     408..409,412..413,415..416,419,422..423,426,429..430,
                     433..434,436..437)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          514..572
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          615..750
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..752
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367701.1:105..2363"
                     /note="isoform lll is encoded by transcript variant 64"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv
      181 revlredghl svngealcyf llqilrriga vgqavsrtaw salwlavvap gkaasgvfww
      241 lgigwyqfvt liswlnvfll trclrnickf lvlliplfll laglslrgqg nffsflpvln
      301 wasmhrtqrv ddpqdvfkpt tsrlkqplqg dseafpwhwm sgveqqvasl sgqchhhgen
      361 lrelttllqk lqarvdqmeg gaagpsastd fmafhqehev rmshledilg klrekseaiq
      421 keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd avqervdvqv
      481 remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt hhvsvtkqlp
      541 tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg silstrcset
      601 yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls mmihpaaftl
      661 ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm fqalkrpddt
      721 afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_002523                741 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear pore complex protein Nup88 isoform 2 [Homo sapiens].
ACCESSION   NP_002523
VERSION     NP_002523.2
DBSOURCE    REFSEQ: accession NM_002532.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 741)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 741)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 741)
  AUTHORS   Makise,M., Uchimura,R., Higashi,K., Mashiki,Y., Shiraishi,R.,
            Shutoku,Y. and Kuniyasu,A.
  TITLE     Overexpression of the nucleoporin Nup88 stimulates migration and
            invasion of HeLa cells
  JOURNAL   Histochem Cell Biol 156 (5), 409-421 (2021)
   PUBMED   34331103
  REMARK    GeneRIF: Overexpression of the nucleoporin Nup88 stimulates
            migration and invasion of HeLa cells.
REFERENCE   4  (residues 1 to 741)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 741)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 741)
  AUTHORS   Martinez,N., Alonso,A., Moragues,M.D., Ponton,J. and Schneider,J.
  TITLE     The nuclear pore complex protein Nup88 is overexpressed in tumor
            cells
  JOURNAL   Cancer Res 59 (21), 5408-5411 (1999)
   PUBMED   10554006
REFERENCE   7  (residues 1 to 741)
  AUTHORS   Stoffler,D., Fahrenkrog,B. and Aebi,U.
  TITLE     The nuclear pore complex: from molecular architecture to functional
            dynamics
  JOURNAL   Curr Opin Cell Biol 11 (3), 391-401 (1999)
   PUBMED   10395558
  REMARK    Review article
REFERENCE   8  (residues 1 to 741)
  AUTHORS   Boer,J., Bonten-Surtel,J. and Grosveld,G.
  TITLE     Overexpression of the nucleoporin CAN/NUP214 induces growth arrest,
            nucleocytoplasmic transport defects, and apoptosis
  JOURNAL   Mol Cell Biol 18 (3), 1236-1247 (1998)
   PUBMED   9488438
REFERENCE   9  (residues 1 to 741)
  AUTHORS   Fornerod,M., van Baal,S., Valentine,V., Shapiro,D.N. and
            Grosveld,G.
  TITLE     Chromosomal localization of genes encoding CAN/Nup214-interacting
            proteins--human CRM1 localizes to 2p16, whereas Nup88 localizes to
            17p13 and is physically linked to SF2p32
  JOURNAL   Genomics 42 (3), 538-540 (1997)
   PUBMED   9205132
REFERENCE   10 (residues 1 to 741)
  AUTHORS   Fornerod,M., van Deursen,J., van Baal,S., Reynolds,A., Davis,D.,
            Murti,K.G., Fransen,J. and Grosveld,G.
  TITLE     The human homologue of yeast CRM1 is in a dynamic subcomplex with
            CAN/Nup214 and a novel nuclear pore component Nup88
  JOURNAL   EMBO J 16 (4), 807-816 (1997)
   PUBMED   9049309
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX956129.1, BC000335.2,
            CX870338.1, AC004148.1, BQ937933.1 and AW089098.1.
            
            On Nov 3, 2002 this sequence version replaced NP_002523.1.
            
            Summary: The nuclear pore complex is a massive structure that
            extends across the nuclear envelope, forming a gateway that
            regulates the flow of macromolecules between the nucleus and the
            cytoplasm. Nucleoporins, a family of 50 to 100 proteins, are the
            main components of the nuclear pore complex in eukaryotic cells.
            The protein encoded by this gene belongs to the nucleoporin family
            and is associated with the oncogenic nucleoporin CAN/Nup214 in a
            dynamic subcomplex. This protein is also overexpressed in a large
            number of malignant neoplasms and precancerous dysplasias.
            Alternative splicing results in multiple transcript variants
            encoding different isoforms. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.305859.1,
                                           SRR1803616.17552.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000573584.6/ ENSP00000458954.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..741
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..741
                     /product="nuclear pore complex protein Nup88 isoform 2"
                     /note="nuclear pore complex protein 88; karyoporin;
                     nucleoporin 88kDa; nuclear pore complex protein Nup88;
                     nucleoporin Nup88"
                     /calculated_mol_wt=83411
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Region          14..740
                     /region_name="Nup88"
                     /note="Nuclear pore component; pfam10168"
                     /db_xref="CDD:462975"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99567.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     Site            698
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CEC0; propagated from
                     UniProtKB/Swiss-Prot (Q99567.2)"
     CDS             1..741
                     /gene="NUP88"
                     /gene_synonym="FADS4"
                     /coded_by="NM_002532.6:13..2238"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11070.1"
                     /db_xref="GeneID:4927"
                     /db_xref="HGNC:HGNC:8067"
                     /db_xref="MIM:602552"
ORIGIN      
        1 maaaegpvgd gelwqtwlpn hvvflrlreg lknqspteae kpassslpss pppqlltrnv
       61 vfglggelfl wdgedssflv vrlrgpsggg eepalsqyqr llcinpplfe iyqvllsptq
      121 hhvaligikg lmvlelpkrw gknsefeggk stvncsttpv aerfftssts ltlkhaawyp
      181 seildphvvl ltsdnviriy slrepqtptn viilseaeee slvlnkgray taslgetava
      241 fdfgplaavp ktlfgqngkd evvayplyil yengetflty isllhspgni gkllgplpmh
      301 paaednygyd acavlclpcv pnilviates gmlyhcvvle geeeddhtse kswdsridli
      361 pslyvfecve lelalklasg eddpfdsdfs cpvklhrdpk cpsryhcthe agvhsvgltw
      421 ihklhkflgs deedkdslqe lsteqkcfve hilctkplpc rqpapirgfw ivpdilgptm
      481 icitstyecl iwpllstvhp asppllctre dvevaesplr vlaetpdsfe khirsilqrs
      541 vanpaflkas ekdiapppee clqllsratq vfreqyilkq dlakeeiqrr vkllcdqkkk
      601 qledlsycre erkslremae rladkyeeak ekqedimnrm kkllhsfhse lpvlsdserd
      661 mkkelqlipd qlrhlgnaik qvtmkkdyqq qkmekvlslp kptiilsayq rkciqsilke
      721 egehiremvk qindirnhvn f
//
LOCUS       NP_001265027             159 aa            linear   PRI 20-NOV-2025
DEFINITION  glial cell line-derived neurotrophic factor isoform 5 [Homo
            sapiens].
ACCESSION   NP_001265027
VERSION     NP_001265027.1
DBSOURCE    REFSEQ: accession NM_001278098.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Avenel,I.C.N., Ewald,J.D., Ariey-Bonnet,J., Kristensen,I.H.,
            Petterson,S.A., Thesbjerg,M.N., Burton,M., Thomassen,M.,
            Wennerberg,K., Michaelsen,S.R. and Kristensen,B.W.
  TITLE     GDNF/GFRA1 signaling contributes to chemo- and radioresistance in
            glioblastoma
  JOURNAL   Sci Rep 14 (1), 17639 (2024)
   PUBMED   39085346
  REMARK    GeneRIF: GDNF/GFRA1 signaling contributes to chemo- and
            radioresistance in glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Keszler,G., Vekony,B., Elek,Z., Nemoda,Z., Angyal,N., Banlaki,Z.,
            Kovacs-Nagy,R., Ronai,Z. and Rethelyi,J.M.
  TITLE     MicroRNA-Mediated Suppression of Glial Cell Line-Derived
            Neurotrophic Factor Expression Is Modulated by a
            Schizophrenia-Associated Non-Coding Polymorphism
  JOURNAL   Int J Mol Sci 25 (8), 4477 (2024)
   PUBMED   38674063
  REMARK    GeneRIF: MicroRNA-Mediated Suppression of Glial Cell Line-Derived
            Neurotrophic Factor Expression Is Modulated by a
            Schizophrenia-Associated Non-Coding Polymorphism.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Alster,P., Otto-Slusarczyk,D., Szlufik,S., Duszynska-Was,K.,
            Drzewinska,A., Wiercinska-Drapalo,A., Struga,M., Kutylowski,M.,
            Friedman,A. and Madetko-Alster,N.
  TITLE     The significance of glial cell line-derived neurotrophic factor
            analysis in Progressive Supranuclear Palsy
  JOURNAL   Sci Rep 14 (1), 2805 (2024)
   PUBMED   38307947
  REMARK    GeneRIF: The significance of glial cell line-derived neurotrophic
            factor analysis in Progressive Supranuclear Palsy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Airavaara,M., Pletnikova,O., Doyle,M.E., Zhang,Y.E., Troncoso,J.C.
            and Liu,Q.R.
  TITLE     Identification of novel GDNF isoforms and cis-antisense GDNFOS gene
            and their regulation in human middle temporal gyrus of Alzheimer
            disease
  JOURNAL   J Biol Chem 286 (52), 45093-45102 (2011)
   PUBMED   22081608
  REMARK    GeneRIF: Identification of novel GDNF isoforms and cis-antisense
            GDNFOS gene and their regulation in human middle temporal gyrus of
            Alzheimer disease
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Schindelhauer,D., Schuffenhauer,S., Gasser,T., Steinkasserer,A. and
            Meitinger,T.
  TITLE     The gene coding for glial cell line derived neurotrophic factor
            (GDNF) maps to chromosome 5p12-p13.1
  JOURNAL   Genomics 28 (3), 605-607 (1995)
   PUBMED   7490108
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Oppenheim,R.W., Houenou,L.J., Johnson,J.E., Lin,L.F., Li,L.,
            Lo,A.C., Newsome,A.L., Prevette,D.M. and Wang,S.
  TITLE     Developing motor neurons rescued from programmed and
            axotomy-induced cell death by GDNF
  JOURNAL   Nature 373 (6512), 344-346 (1995)
   PUBMED   7830769
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Tomac,A., Lindqvist,E., Lin,L.F., Ogren,S.O., Young,D., Hoffer,B.J.
            and Olson,L.
  TITLE     Protection and repair of the nigrostriatal dopaminergic system by
            GDNF in vivo
  JOURNAL   Nature 373 (6512), 335-339 (1995)
   PUBMED   7830766
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Schaar,D.G., Sieber,B.A., Sherwood,A.C., Dean,D., Mendoza,G.,
            Ramakrishnan,L., Dreyfus,C.F. and Black,I.B.
  TITLE     Multiple astrocyte transcripts encode nigral trophic factors in rat
            and human
  JOURNAL   Exp Neurol 130 (2), 387-393 (1994)
   PUBMED   7867768
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ001900.1, DQ235474.1 and
            AC008869.5.
            
            Summary: This gene encodes a secreted ligand of the TGF-beta
            (transforming growth factor-beta) superfamily of proteins. Ligands
            of this family bind various TGF-beta receptors leading to
            recruitment and activation of SMAD family transcription factors
            that regulate gene expression. The encoded preproprotein is
            proteolytically processed to generate each subunit of the
            disulfide-linked homodimer. The recombinant form of this protein, a
            highly conserved neurotrophic factor, was shown to promote the
            survival and differentiation of dopaminergic neurons in culture,
            and was able to prevent apoptosis of motor neurons induced by
            axotomy. This protein is a ligand for the product of the RET
            (rearranged during transfection) protooncogene. Mutations in this
            gene may be associated with Hirschsprung disease and Tourette
            syndrome. This gene encodes multiple protein isoforms that may
            undergo similar proteolytic processing. [provided by RefSeq, Aug
            2016].
            
            Transcript Variant: This variant (6) has a unique internal exon,
            which causes translation initiation at a downstream AUG, compared
            to variant 1. The encoded isoform (5) has a shorter N-terminus,
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DQ235474.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA2147975,
                                           SAMEA2152798 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..159
                     /product="glial cell line-derived neurotrophic factor
                     isoform 5"
                     /note="astrocyte-derived trophic factor; glial cell
                     line-derived neurotrophic factor"
                     /calculated_mol_wt=17992
     Region          63..158
                     /region_name="TGF_beta_GDNF"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in glial cell line-derived neurotrophic
                     factor (GDNF) and similar proteins; cd19380"
                     /db_xref="CDD:381650"
     Site            order(71,73,77..80,90..94,103..105,107..108,110..111,
                     123..129,132,149..151)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381650"
     Site            order(72,85..87,89,134..139,141..145,147)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381650"
     CDS             1..159
                     /gene="GDNF"
                     /gene_synonym="ATF; ATF1; ATF2; HFB1-GDNF; HSCR3"
                     /coded_by="NM_001278098.1:185..664"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS75237.1"
                     /db_xref="GeneID:2668"
                     /db_xref="HGNC:HGNC:4232"
                     /db_xref="MIM:600837"
ORIGIN      
        1 mpedypdqfd dvmdfiqati krlkrspdkq mavlprrern rqaaaanpen srgkgrrgqr
       61 gknrgcvlta ihlnvtdlgl gyetkeelif rycsgscdaa ettydkilkn lsrnrrlvsd
      121 kvgqaccrpi afdddlsfld dnlvyhilrk hsakrcgci
//
LOCUS       NP_005052                407 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein uL3-like [Homo sapiens].
ACCESSION   NP_005052
VERSION     NP_005052.1
DBSOURCE    REFSEQ: accession NM_005061.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Bajpai,A.K., Gu,Q., Orgil,B.O., Alberson,N.R., Towbin,J.A.,
            Martinez,H.R., Lu,L. and Purevjav,E.
  TITLE     Exploring the Regulation and Function of Rpl3l in the Development
            of Early-Onset Dilated Cardiomyopathy and Congestive Heart Failure
            Using Systems Genetics Approach
  JOURNAL   Genes (Basel) 15 (1), 53 (2023)
   PUBMED   38254943
  REMARK    GeneRIF: Exploring the Regulation and Function of Rpl3l in the
            Development of Early-Onset Dilated Cardiomyopathy and Congestive
            Heart Failure Using Systems Genetics Approach.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Chaillou,T., Zhang,X. and McCarthy,J.J.
  TITLE     Expression of Muscle-Specific Ribosomal Protein L3-Like Impairs
            Myotube Growth
  JOURNAL   J Cell Physiol 231 (9), 1894-1902 (2016)
   PUBMED   26684695
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Casabonne,D., Reina,O., Benavente,Y., Becker,N., Maynadie,M.,
            Foretova,L., Cocco,P., Gonzalez-Neira,A., Nieters,A., Boffetta,P.,
            Middeldorp,J.M. and de Sanjose,S.
  TITLE     Single nucleotide polymorphisms of matrix metalloproteinase 9
            (MMP9) and tumor protein 73 (TP73) interact with Epstein-Barr virus
            in chronic lymphocytic leukemia: results from the European
            case-control study EpiLymph
  JOURNAL   Haematologica 96 (2), 323-327 (2011)
   PUBMED   21048031
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Mazumder,B., Sampath,P., Seshadri,V., Maitra,R.K., DiCorleto,P.E.
            and Fox,P.L.
  TITLE     Regulated release of L13a from the 60S ribosomal subunit as a
            mechanism of transcript-specific translational control
  JOURNAL   Cell 115 (2), 187-198 (2003)
   PUBMED   14567916
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Daniels,R.J., Peden,J.F., Lloyd,C., Horsley,S.W., Clark,K.,
            Tufarelli,C., Kearney,L., Buckle,V.J., Doggett,N.A., Flint,J. and
            Higgs,D.R.
  TITLE     Sequence, structure and pathology of the fully annotated terminal 2
            Mb of the short arm of human chromosome 16
  JOURNAL   Hum Mol Genet 10 (4), 339-352 (2001)
   PUBMED   11157797
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Van Raay,T.J., Connors,T.D., Klinger,K.W., Landes,G.M. and
            Burn,T.C.
  TITLE     A novel ribosomal protein L3-like gene (RPL3L) maps to the
            autosomal dominant polycystic kidney disease gene region
  JOURNAL   Genomics 37 (2), 172-176 (1996)
   PUBMED   8921388
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Burn,T.C., Connors,T.D., Van Raay,T.J., Dackowski,W.R.,
            Millholland,J.M., Klinger,K.W. and Landes,G.M.
  TITLE     Generation of a transcriptional map for a 700-kb region surrounding
            the polycystic kidney disease type 1 (PKD1) and tuberous sclerosis
            type 2 (TSC2) disease genes on human chromosome 16p3.3
  JOURNAL   Genome Res 6 (6), 525-537 (1996)
   PUBMED   8828041
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005363.1.
            
            Summary: This gene encodes a protein that shares sequence
            similarity with ribosomal protein L3. The protein belongs to the
            L3P family of ribosomal proteins. Unlike the ubiquitous expression
            of ribosomal protein genes, this gene has a tissue-specific pattern
            of expression, with the highest levels of expression in skeletal
            muscle and heart. It is not currently known whether the encoded
            protein is a functional ribosomal protein or whether it has evolved
            a function that is independent of the ribosome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050413.1, SRR5189655.26801.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268661.8/ ENSP00000268661.7
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..407
                     /product="ribosomal protein uL3-like"
                     /note="60S ribosomal protein L3-like; large ribosomal
                     subunit protein uL3-like"
                     /calculated_mol_wt=46165
     Region          1..398
                     /region_name="PTZ00103"
                     /note="60S ribosomal protein L3; Provisional"
                     /db_xref="CDD:240267"
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92901.3)"
     Region          387..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92901.3)"
     CDS             1..407
                     /gene="RPL3L"
                     /gene_synonym="CMD2D"
                     /coded_by="NM_005061.3:59..1282"
                     /db_xref="CCDS:CCDS10450.1"
                     /db_xref="GeneID:6123"
                     /db_xref="HGNC:HGNC:10351"
                     /db_xref="MIM:617416"
ORIGIN      
        1 mshrkfsapr hghlgflphk rshrhrgkvk twprddpsqp vhltaflgyk agmthtlrev
       61 hrpglkiskr eeveavtive tpplvvvgvv gyvatprglr sfktifaehl sdecrrrfyk
      121 dwhkskkkaf tkackrwrdt dgkkqlqkdf aamkkyckvi rvivhtqmkl lpfrqkkahi
      181 meiqlnggtv aekvawaqar lekqvpvhsv fsqsevidvi avtkgrgvkg vtsrwhtkkl
      241 prkthkglrk vacigawhpa rvgcsiarag qkgyhhrtel nkkifrigrg phmedgklvk
      301 nnastsydvt aksitplggf phygevnndf vmlkgciagt kkrvitlrks llvhhsrqav
      361 enielkfidt tskfghgrfq taqekrafmg pqkkhleket petsgdl
//
LOCUS       NP_001259025             295 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-4 isoform 2 [Homo sapiens].
ACCESSION   NP_001259025
VERSION     NP_001259025.1
DBSOURCE    REFSEQ: accession NM_001272096.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Kioumourtzoglou,D., Black,H.L., Al Tobi,M., Livingstone,R.,
            Petrie,J.R., Boyle,J.G., Gould,G.W. and Bryant,N.J.
  TITLE     Phosphorylation of Syntaxin 4 by the Insulin Receptor Drives
            Exocytic SNARE Complex Formation to Deliver GLUT4 to the Cell
            Surface
  JOURNAL   Biomolecules 13 (12), 1738 (2023)
   PUBMED   38136609
  REMARK    GeneRIF: Phosphorylation of Syntaxin 4 by the Insulin Receptor
            Drives Exocytic SNARE Complex Formation to Deliver GLUT4 to the
            Cell Surface.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Gigon,L., Fettrelet,T., Miholic,M., McLeish,K.R., Yousefi,S.,
            Stojkov,D. and Simon,H.U.
  TITLE     Syntaxin-4 and SNAP23 are involved in neutrophil degranulation, but
            not in the release of mitochondrial DNA during NET formation
  JOURNAL   Front Immunol 14, 1272699 (2023)
   PUBMED   37885878
  REMARK    GeneRIF: Syntaxin-4 and SNAP23 are involved in neutrophil
            degranulation, but not in the release of mitochondrial DNA during
            NET formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Schrauwen,I., Ghaffar,A., Bharadwaj,T., Shah,K., Rehman,S.,
            Acharya,A., Liaqat,K., Lin,N.S., Everard,J.L., Khan,A., Ahmed,Z.M.,
            Ahmad,W., Riazuddin,S. and Leal,S.M.
  TITLE     Syntaxin 4 is essential for hearing in human and zebrafish
  JOURNAL   Hum Mol Genet 32 (7), 1184-1192 (2023)
   PUBMED   36355422
  REMARK    GeneRIF: Syntaxin 4 is essential for hearing in human and
            zebrafish.
REFERENCE   5  (residues 1 to 295)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Mandon,B., Chou,C.L., Nielsen,S. and Knepper,M.A.
  TITLE     Syntaxin-4 is localized to the apical plasma membrane of rat renal
            collecting duct cells: possible role in aquaporin-2 trafficking
  JOURNAL   J Clin Invest 98 (4), 906-913 (1996)
   PUBMED   8770861
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Jagadish,M.N., Fernandez,C.S., Hewish,D.R., Macaulay,S.L.,
            Gough,K.H., Grusovin,J., Verkuylen,A., Cosgrove,L., Alafaci,A.,
            Frenkel,M.J. and Ward,C.W.
  TITLE     Insulin-responsive tissues contain the core complex protein SNAP-25
            (synaptosomal-associated protein 25) A and B isoforms in addition
            to syntaxin 4 and synaptobrevins 1 and 2
  JOURNAL   Biochem J 317 (Pt 3) (Pt 3), 945-954 (1996)
   PUBMED   8760387
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Li,C., Ullrich,B., Zhang,J.Z., Anderson,R.G., Brose,N. and
            Sudhof,T.C.
  TITLE     Ca(2+)-dependent and -independent activities of neural and
            non-neural synaptotagmins
  JOURNAL   Nature 375 (6532), 594-599 (1995)
   PUBMED   7791877
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Li,H., Hodge,D.R., Pei,G.K. and Seth,A.
  TITLE     Isolation and sequence analysis of the human syntaxin-encoding gene
  JOURNAL   Gene 143 (2), 303-304 (1994)
   PUBMED   8206394
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Bennett,M.K., Garcia-Arraras,J.E., Elferink,L.A., Peterson,K.,
            Fleming,A.M., Hazuka,C.D. and Scheller,R.H.
  TITLE     The syntaxin family of vesicular transport receptors
  JOURNAL   Cell 74 (5), 863-873 (1993)
   PUBMED   7690687
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK091833.1, BC002436.2 and BQ775670.1.
            
            Transcript Variant: This variant (2) contains a distinct 5' UTR,
            initiates translation at an alternate upstream start codon and uses
            alternate splice sites at internal exons, compared to variant 1.
            The encoded isoform (2) has a distinct N-terminus and is longer
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091833.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..295
                     /product="syntaxin-4 isoform 2"
                     /note="syntaxin 4A (placental); renal carcinoma antigen
                     NY-REN-31"
                     /calculated_mol_wt=33710
     Region          42..187
                     /region_name="SynN"
                     /note="Syntaxin N-terminus domain; syntaxins are nervous
                     system-specific proteins implicated in the docking of
                     synaptic vesicles with the presynaptic plasma membrane;
                     they are a family of receptors for intracellular transport
                     vesicles; each target membrane may...; cd00179"
                     /db_xref="CDD:238105"
     Site            order(47,119..120,123..124,127,130..131,137,140,172)
                     /site_type="active"
                     /note="nSec1 interaction sites [active]"
                     /db_xref="CDD:238105"
     Site            order(67,78,81..82,89,93,96,103,125,130,133,139,146..147,
                     150..151,153..154,157,184)
                     /site_type="active"
                     /note="interdomain interaction site [active]"
                     /db_xref="CDD:238105"
     Site            order(164..174,183..187)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238105"
     Region          197..259
                     /region_name="SNARE_syntaxin4"
                     /note="SNARE motif of syntaxin 4; cd15883"
                     /db_xref="CDD:277236"
     Site            order(202,204..205,207..212,214..216,218..219,221..223,
                     225..226,228..230,232..233,235..240,242..247,249..254,
                     256..258)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277236"
     Site            232
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277236"
     CDS             1..295
                     /gene="STX4"
                     /gene_synonym="DFNB123; p35-2; STX4A"
                     /coded_by="NM_001272096.1:344..1231"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS61916.1"
                     /db_xref="GeneID:6810"
                     /db_xref="HGNC:HGNC:11439"
                     /db_xref="MIM:186591"
ORIGIN      
        1 mgmtartkrt rsgsrwwctr arhgwgartr ssstsplghp pqvrtirqti vklgnkvqel
       61 ekqqvtilat plpeesmkqe lqnlrdeikq lgreirlqlk aiepqkeead enynsvntrm
      121 rktqhgvlsq qfvelinkcn smqseyrekn verirrqlki tnagmvsdee leqmldsgqs
      181 evfvsnilkd tqvtrqalne isarhseiqq lersirelhd iftflateve mqgeminrie
      241 knilssadyv ergqehvkta lenqkkarkk kvliaicvsi tvvllaviig vtvvg
//
LOCUS       NP_005068                770 aa            linear   PRI 20-NOV-2025
DEFINITION  transducin-like enhancer protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_005068
VERSION     NP_005068.2
DBSOURCE    REFSEQ: accession NM_005077.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Xue,L., Hu,M., Zhu,Q., Li,Y., Zhou,G., Zhang,X., Zhou,Y., Zhang,J.
            and Ding,P.
  TITLE     GRg1 inhibits the TLR4/NF-kB signaling pathway by upregulating
            miR-216a-5p to reduce growth factors and inflammatory cytokines in
            DR
  JOURNAL   Mol Biol Rep 50 (11), 9379-9394 (2023)
   PUBMED   37819496
  REMARK    GeneRIF: GRg1 inhibits the TLR4/NF-kB signaling pathway by
            upregulating miR-216a-5p to reduce growth factors and inflammatory
            cytokines in DR.
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Hasbay,B. and kayaselCuk,F.
  TITLE     Expression of TLE-1 in Gastrointestinal Stromal Tumour and Its
            Relationship to Clinicopathological Parameters
  JOURNAL   J Coll Physicians Surg Pak 33 (3), 286-291 (2023)
   PUBMED   36945158
  REMARK    GeneRIF: Expression of TLE-1 in Gastrointestinal Stromal Tumour and
            Its Relationship to Clinicopathological Parameters.
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Aref,S., El-Ghonemy,M.S., Atia,D.M., Elbaiomy,M.M.,
            Abdelsalam,S.A., Tawfik,A. and El-Sebaie,A.
  TITLE     Prognostic Value of TLE1 Gene Expression in Patients with T-cell
            Acute Lymphoblastic Leukemia
  JOURNAL   Asian Pac J Cancer Prev 22 (5), 1653-1658 (2021)
   PUBMED   34048198
  REMARK    GeneRIF: Prognostic Value of TLE1 Gene Expression in Patients with
            T-cell Acute Lymphoblastic Leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Husain,J., Lo,R., Grbavec,D. and Stifani,S.
  TITLE     Affinity for the nuclear compartment and expression during cell
            differentiation implicate phosphorylated Groucho/TLE1 forms of
            higher molecular mass in nuclear functions
  JOURNAL   Biochem J 317 (Pt 2) (Pt 2), 523-531 (1996)
   PUBMED   8713081
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Grbavec,D. and Stifani,S.
  TITLE     Molecular interaction between TLE1 and the carboxyl-terminal domain
            of HES-1 containing the WRPW motif
  JOURNAL   Biochem Biophys Res Commun 223 (3), 701-705 (1996)
   PUBMED   8687460
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Liu,Y., Dehni,G., Purcell,K.J., Sokolow,J., Carcangiu,M.L.,
            Artavanis-Tsakonas,S. and Stifani,S.
  TITLE     Epithelial expression and chromosomal location of human TLE genes:
            implications for notch signaling and neoplasia
  JOURNAL   Genomics 31 (1), 58-64 (1996)
   PUBMED   8808280
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Miyasaka,H., Choudhury,B.K., Hou,E.W. and Li,S.S.
  TITLE     Molecular cloning and expression of mouse and human cDNA encoding
            AES and ESG proteins with strong similarity to Drosophila enhancer
            of split groucho protein
  JOURNAL   Eur J Biochem 216 (1), 343-352 (1993)
   PUBMED   8365415
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Stifani,S., Blaumueller,C.M., Redhead,N.J., Hill,R.E. and
            Artavanis-Tsakonas,S.
  TITLE     Human homologs of a Drosophila Enhancer of split gene product
            define a novel family of nuclear proteins
  JOURNAL   Nat Genet 2 (2), 119-127 (1992)
   PUBMED   1303260
  REMARK    Erratum:[Nat Genet. 1992 Dec;2(4):343. doi: 10.1038/ng1292-343a.
            PMID: 1303292]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL365190.16, AB209854.1, BC010100.2 and DB211613.1.
            
            On Jun 24, 2002 this sequence version replaced NP_005068.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC010100.2, SRR1660807.122192.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376499.8/ ENSP00000365682.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.32"
     Protein         1..770
                     /product="transducin-like enhancer protein 1 isoform 2"
                     /note="transducin-like enhancer protein 1; enhancer of
                     split groucho-like protein 1; transducin-like enhancer of
                     split 1 (E(sp1) homolog, Drosophila); transducin like
                     enhancer of split 1"
                     /calculated_mol_wt=83070
     Region          1..131
                     /region_name="Q domain.
                     /evidence=ECO:0000305|PubMed:21429299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          18..133
                     /region_name="TLE_N"
                     /note="Groucho/TLE N-terminal Q-rich domain; pfam03920"
                     /db_xref="CDD:461094"
     Region          128..157
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          132..199
                     /region_name="GP domain.
                     /evidence=ECO:0000305|PubMed:21429299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          176..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          200..268
                     /region_name="CcN domain.
                     /evidence=ECO:0000305|PubMed:21429299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          225..228
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q04724.2)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          269..450
                     /region_name="SP domain.
                     /evidence=ECO:0000305|PubMed:21429299"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q04724.2)"
     Region          <319..476
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          470..501
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          483..768
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          487..526
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          528..558
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          534..572
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          572..602
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          577..613
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          614..644
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          620..655
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          660..693
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          696..726
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          701..735
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          737..767
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q04724.2)"
     Region          742..766
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..770
                     /gene="TLE1"
                     /gene_synonym="ESG; ESG1; GRG1; TLE-1"
                     /coded_by="NM_005077.5:1308..3620"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6661.1"
                     /db_xref="GeneID:7088"
                     /db_xref="HGNC:HGNC:11837"
                     /db_xref="MIM:600189"
ORIGIN      
        1 mfpqsrhptp hqaagqpfkf tipesldrik eefqflqaqy hslklecekl asektemqrh
       61 yvmyyemsyg lniemhkqte iakrlntica qvipflsqeh qqqvaqaver akqvtmaeln
      121 aiigqqqlqa qhlshghgpp vpltphpsgl qppgipplgg sagllalssa lsgqshlaik
      181 ddkkhhdaeh hrdrepgtsn sllvpdslrg tdkrrngpef sndikkrkvd dkdsshydsd
      241 gdksddnlvv dvsnedpssp raspahspre ngidknrllk kdassspast assasstslk
      301 skemslheka stpvlksstp tprsdmptpg tsatpglrpg lgkppaidpl vnqaaaglrt
      361 plavpgpypa pfgmvphagm ngeltspgaa yaslhnmspq msaaaaaaav vaygrspmvg
      421 fdppphmrvp tippnlagip ggkpaysfhv tadgqmqpvp fppdaligpg iprharqint
      481 lnhgevvcav tisnptrhvy tggkgcvkvw dishpgnksp vsqldclnrd nyirsckllp
      541 dgctlivgge astlsiwdla aptprikael tssapacyal aispdskvcf sccsdgniav
      601 wdlhnqtlvr qfqghtdgas cidisndgtk lwtggldntv rswdlregrq lqqhdftsqi
      661 fslgycptge wlavgmessn vevlhvnkpd kyqlhlhesc vlslkfaycg kwfvstgkdn
      721 llnawrtpyg asifqskess svlscdisvd dkyivtgsgd kkatvyeviy
//
LOCUS       NP_002787                264 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-4 [Homo sapiens].
ACCESSION   NP_002787
VERSION     NP_002787.2
DBSOURCE    REFSEQ: accession NM_002796.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Nothwang,H.G., Tamura,T., Tanaka,K. and Ichihara,A.
  TITLE     Sequence analyses and inter-species comparisons of three novel
            human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine
            potential proteolytic active-site residues
  JOURNAL   Biochim Biophys Acta 1219 (2), 361-368 (1994)
   PUBMED   7918633
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Gerards,W.L., Hop,F.W., Hendriks,I.L. and Bloemendal,H.
  TITLE     Cloning and expression of a human pro(tea)some beta-subunit cDNA: a
            homologue of the yeast PRE4-subunit essential for
            peptidylglutamyl-peptide hydrolase activity
  JOURNAL   FEBS Lett 346 (2-3), 151-155 (1994)
   PUBMED   8013624
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Lee,L.W., Moomaw,C.R., Orth,K., McGuire,M.J., DeMartino,G.N. and
            Slaughter,C.A.
  TITLE     Relationships among the subunits of the high molecular weight
            proteinase, macropain (proteasome)
  JOURNAL   Biochim Biophys Acta 1037 (2), 178-185 (1990)
   PUBMED   2306472
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL589764.19.
            
            On Aug 29, 2002 this sequence version replaced NP_002787.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX394340.2, BM479861.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000290541.7/ ENSP00000290541.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..264
                     /product="proteasome subunit beta type-4"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit HsN3; proteasome beta chain;
                     macropain beta chain; proteasome chain 3; multicatalytic
                     endopeptidase complex beta chain; proteasome subunit, beta
                     type, 4; hsBPROS26; 26 kDa prosomal protein; testis tissue
                     sperm-binding protein Li 79P; proteasome (prosome,
                     macropain) subunit, beta type, 4; proteasome subunit beta
                     4; proteasome subunit beta7; beta-7; proteasome subunit
                     beta-7"
                     /calculated_mol_wt=29073
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P28070.4)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P28070.4)"
     Region          52..247
                     /region_name="proteasome_beta_type_4"
                     /note="proteasome beta type-4 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03760"
                     /db_xref="CDD:239729"
     Site            order(54,70,72,86,186,225,228..229)
                     /site_type="active"
                     /db_xref="CDD:239729"
     Site            order(72,75,77..82,102,104,119,132,135..136,138..139,142,
                     145,171,173,175..178,181,189..190,192..193,196..198,216,
                     223..226,229..230)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239729"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P28070.4)"
     CDS             1..264
                     /gene="PSMB4"
                     /gene_synonym="HN3; HsN3; PRAAS3; PROS-26; PROS26"
                     /coded_by="NM_002796.3:16..810"
                     /db_xref="CCDS:CCDS996.1"
                     /db_xref="GeneID:5692"
                     /db_xref="HGNC:HGNC:9541"
                     /db_xref="MIM:602177"
ORIGIN      
        1 meaflgsrsg lwaggpapgq fyripstpds fmdpasalyr gpitrtqnpm vtgtsvlgvk
       61 feggvviaad mlgsygslar frnisrimrv nnstmlgasg dyadfqylkq vlgqmvidee
      121 llgdghsysp raihswltra mysrrskmnp lwntmviggy adgesflgyv dmlgvayeap
      181 slatgygayl aqpllrevle kqpvlsqtea rdlvercmrv lyyrdarsyn rfqiatvtek
      241 gveiegplst etnwdiahmi sgfe
//
LOCUS       NP_001353526             879 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 26 [Homo
            sapiens].
ACCESSION   NP_001353526 XP_011538780
VERSION     NP_001353526.1
DBSOURCE    REFSEQ: accession NM_001366597.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 879)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 879)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 879)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 879)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 879)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 879)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 879)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 879)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 879)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 879)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_011538780.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.149600.1,
                                           SRR1660809.181821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..879
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..879
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 26"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=99318
     Region          7..76
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <581..>715
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..879
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366597.1:251..2890"
                     /note="isoform 26 is encoded by transcript variant 44"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mskvnlevik pwitkrvtei lgfeddvvie fifnqlevkn pdskmmqinl tgflngknar
       61 efmgelwpll lsaqeniagi psaflelkke eikqrqieqe klasmkkqde dkdkrdkeek
      121 essrekrers rsprrrksrs psprrrsspv rrerkrshsr sprhrtksrs pspapekkek
      181 tpelpepsvk vkepsvqeat stsdilkvpk pepipepkep speknskkek ekektrprsr
      241 srsksrsrtr srspshtrpr rrhrsrsrsy sprrrpsprr rpsprrrtpp rrmpppprhr
      301 rsrspvrrrr rssaslsgss ssssssrsrs ppkkppkrts spprktrrls psaspprrrh
      361 rpsppatppp ktrhsptpqq snrtrksrvs vspgrtsgkv tkhkgtekre spspapkprk
      421 velseseedk ggkmaaadsv qqrrqyrrqn qqsssdsgss sssederpkr shvkngevgr
      481 rrrhspsrsa spsprkrqke tsprmqmgkr wqspvtksgr rrrspspppt rrrrspspap
      541 pprrrrtptp pprrrtpspp prrrspsprr ysppiqrrys pspppkrrta spppppkrra
      601 spspppkrrv shspppkqrs spvtkrrsps lsskhrkgss psrstrears pqpnkrhsps
      661 prprapqtss spppvrrgas sspqrrqsps pstrpirrvs rtpepkkikk aaspspqsvr
      721 rvsssrsvsg spepaakkpp appspvqsqs pstnwspavp vkkaksptps pspprnsdqe
      781 gggkkkkkkk dkkhkkdkkh kkhkkhkkek avaaaaaaav tpaaiaaatt tlaqeepvaa
      841 pepkketese aednlddlek hlrekalrsm rkaqvspqs
//
LOCUS       NP_001295045             983 aa            linear   PRI 20-NOV-2025
DEFINITION  polyhomeotic-like protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_001295045 XP_005247847
VERSION     NP_001295045.1
DBSOURCE    REFSEQ: accession NM_001308116.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Wang,H., Lan,S., Wang,L., Zhao,J., Jia,X., Xu,J., Sun,G., Liu,L.,
            Gong,S., Wang,N., Shan,B., Zhang,F. and Zhang,Z.
  TITLE     Expression of circ-PHC3 enhances ovarian cancer progression via
            regulation of the miR-497-5p/SOX9 pathway
  JOURNAL   J Ovarian Res 16 (1), 142 (2023)
   PUBMED   37468993
  REMARK    GeneRIF: Expression of circ-PHC3 enhances ovarian cancer
            progression via regulation of the miR-497-5p/SOX9 pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Crea,F., Di Paolo,A., Liu,H.H., Polillo,M., Clermont,P.L.,
            Guerrini,F., Ciabatti,E., Ricci,F., Barate,C., Fontanelli,G.,
            Barsotti,S., Morganti,R., Danesi,R., Wang,Y., Petrini,M.,
            Galimberti,S. and Helgason,C.D.
  TITLE     Polycomb genes are associated with response to imatinib in chronic
            myeloid leukemia
  JOURNAL   Epigenomics 7 (5), 757-765 (2015)
   PUBMED   26343356
  REMARK    GeneRIF: Data show that polycomb-group proteins BMI1, PHC3, CBX6
            and CBX7 expression was significantly increased during imatinib
            treatment.
REFERENCE   6  (residues 1 to 983)
  AUTHORS   Deshpande,A.M., Akunowicz,J.D., Reveles,X.T., Patel,B.B.,
            Saria,E.A., Gorlick,R.G., Naylor,S.L., Leach,R.J. and Hansen,M.F.
  TITLE     PHC3, a component of the hPRC-H complex, associates with E2F6
            during G0 and is lost in osteosarcoma tumors
  JOURNAL   Oncogene 26 (12), 1714-1722 (2007)
   PUBMED   17001316
  REMARK    GeneRIF: loss of PHC3 may favor tumorigenesis by potentially
            disrupting the ability of cells to remain in G(0)
REFERENCE   7  (residues 1 to 983)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 983)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 983)
  AUTHORS   Tonkin,E., Hagan,D.M., Li,W. and Strachan,T.
  TITLE     Identification and characterisation of novel mammalian homologues
            of Drosophila polyhomeoticpermits new insights into relationships
            between members of the polyhomeotic family
  JOURNAL   Hum Genet 111 (4-5), 435-442 (2002)
   PUBMED   12384788
REFERENCE   10 (residues 1 to 983)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK304411.1, AJ320486.3, AC008040.7 and AI042019.1.
            
            On Apr 22, 2015 this sequence version replaced XP_005247847.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region and uses a downstream start
            codon compared to variant 1. It encodes isoform 2 which has a
            shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC112944.1, SRR1660807.141825.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..983
                     /product="polyhomeotic-like protein 3 isoform 2"
                     /note="early development regulator 3; polyhomeotic-like
                     protein 3; homolog of polyhomeotic 3; early development
                     regulatory protein 3; polyhomeotic like 3"
                     /calculated_mol_wt=106031
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          103..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          225..283
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          313..332
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          339..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          <346..>506
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          477..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          601..620
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          691..720
                     /region_name="HD1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            761
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          827..847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          864..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NDX5.1)"
     Region          914..982
                     /region_name="SAM_Ph1,2,3"
                     /note="SAM domain of Ph (polyhomeotic) proteins of
                     Polycomb group; cd09577"
                     /db_xref="CDD:188976"
     Site            order(932..933,967..968,971..972,975)
                     /site_type="other"
                     /note="oligomer interface EH [polypeptide binding]"
                     /db_xref="CDD:188976"
     Site            order(943..947,949..950,953..954,958,963)
                     /site_type="other"
                     /note="oligomer interface ML [polypeptide binding]"
                     /db_xref="CDD:188976"
     CDS             1..983
                     /gene="PHC3"
                     /gene_synonym="EDR3; HPH3"
                     /coded_by="NM_001308116.2:70..3021"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77858.1"
                     /db_xref="GeneID:80012"
                     /db_xref="HGNC:HGNC:15682"
                     /db_xref="MIM:620031"
ORIGIN      
        1 mdtepnpgts svstttsstt tttittsssr mqqpqisvys gsdrhavqvi qqalhrppss
       61 aaqylqqmya aqqqhlmlht aalqqqhlss sqlqslaavq aslssgrpst sptgsvtqqs
      121 smsqtsinls tsptpaqlis rsqassstsg sitqqtmllg stsptltasq aqmylraqml
      181 iftpattvaa vqsdipvvss ssssscqsaa tqvqnltlrs qklgvlsssq ngppkstsqt
      241 qsltichnkt tvtsskisqr dpspesnkkg espslesrst avtrtssihq liapasyspi
      301 qphslikhqq iplhsppskv shhqlilqqq qqqiqpitlq nstqdpppsq hciplqnhgl
      361 ppapsnaqsq hcspiqshps pltvspnqsq saqqsvvvsp ppphspsqsp tiiihpqali
      421 qphplvssal qpgpnlqqst anqvqataql nlpshlplpa spvvhigpvq qsalvspgqq
      481 ivspshqqys slqsspipia sppqmstspp aqipplplqs mqslqvqpei lsqgqvlvqn
      541 alvseeelpa aealvqlpfq tlpppqtvav nlqvqppapv dppvvyqved vceeempees
      601 decvrmdrtp ppptlspaai tvgrgedlts ehplleqvel pavasvsasv ikspsdpshv
      661 svpppplllp aattrsnsts mhssipsien kppqaivkpq ilthviegfv iqeglepfpv
      721 srssllieqp vkkrplldnq vinsvcvqpe lqnntkhadn ssdtemedmi aeetleemds
      781 ellkcefcgk mgyaneflrs krfctmscak rynvscskkf alsrwnrkpd nqslghrgrr
      841 psgpdgaare hilrqlpity psaeedlash edsvpsamtt rlrrqserer erelrdvrir
      901 kmpensdllp vaqtepsiwt vddvwafihs lpgcqdiade fraqeidgqa llllkedhlm
      961 samniklgpa lkicarinsl kes
//
LOCUS       NP_001354682             408 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform j [Homo sapiens].
ACCESSION   NP_001354682
VERSION     NP_001354682.1
DBSOURCE    REFSEQ: accession NM_001367753.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 408)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 408)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.54674.1,
                                           SRR1803616.263850.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..408
                     /product="rab5 GDP/GTP exchange factor isoform j"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=46952
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          <118..137
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          187..287
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..408
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001367753.1:78..1304"
                     /note="isoform j is encoded by transcript variant 37"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkvpper
      121 vekimdqiek yimtrlykyv fcpettddek kdlaiqkrir alrwvtpqml cvpvnedipe
      181 vsdmvvkait diiemdskrv prdklacitk cskhifnaik itknepasad dflptliyiv
      241 lkgnpprlqs niqyitrfcn psrlmtgedg yyftnlccav afiekldaqs lnlsqedfdr
      301 ymsgqtsprk qeaeswspda clgvkqmykn ldllsqlner qerimneakk lekdlidwtd
      361 giarevqdiv ekypleikpp nqplaaidse nvendklppp lqpqvyag
//
LOCUS       NP_056036               1577 aa            linear   PRI 20-NOV-2025
DEFINITION  dynamin-binding protein isoform a [Homo sapiens].
ACCESSION   NP_056036 XP_050742
VERSION     NP_056036.1
DBSOURCE    REFSEQ: accession NM_015221.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1577)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1577)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1577)
  AUTHORS   Ouyang,C., Mu,J., Lu,Q., Li,J., Zhu,H., Wang,Q., Zou,M.H. and
            Xie,Z.
  TITLE     Autophagic degradation of KAT2A/GCN5 promotes directional migration
            of vascular smooth muscle cells by reducing TUBA/alpha-tubulin
            acetylation
  JOURNAL   Autophagy 16 (10), 1753-1770 (2020)
   PUBMED   31878840
  REMARK    GeneRIF: Autophagic degradation of KAT2A/GCN5 promotes directional
            migration of vascular smooth muscle cells by reducing
            TUBA/alpha-tubulin acetylation.
REFERENCE   5  (residues 1 to 1577)
  AUTHORS   Ansar,M., Chung,H.L., Taylor,R.L., Nazir,A., Imtiaz,S.,
            Sarwar,M.T., Manousopoulou,A., Makrythanasis,P., Saeed,S.,
            Falconnet,E., Guipponi,M., Pournaras,C.J., Ansari,M.A., Ranza,E.,
            Santoni,F.A., Ahmed,J., Shah,I., Gul,K., Black,G.C., Bellen,H.J.
            and Antonarakis,S.E.
  TITLE     Bi-allelic Loss-of-Function Variants in DNMBP Cause Infantile
            Cataracts
  JOURNAL   Am J Hum Genet 103 (4), 568-578 (2018)
   PUBMED   30290152
  REMARK    GeneRIF: DNMBP loss-of-function variants cause infantile-onset
            cataracts in humans.
REFERENCE   6  (residues 1 to 1577)
  AUTHORS   Minster,R.L., DeKosky,S.T. and Kamboh,M.I.
  TITLE     No association of dynamin binding protein (DNMBP) gene SNPs and
            Alzheimer's disease
  JOURNAL   Neurobiol Aging 29 (10), 1602-1604 (2008)
   PUBMED   17442457
  REMARK    GeneRIF: We observed no association of statistical significance in
            either the total sample or the APOE*4 non-carriers for any of the
            SNPs of Dynamin Binding Protein.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 1577)
  AUTHORS   Otani,T., Ichii,T., Aono,S. and Takeichi,M.
  TITLE     Cdc42 GEF Tuba regulates the junctional configuration of simple
            epithelial cells
  JOURNAL   J Cell Biol 175 (1), 135-146 (2006)
   PUBMED   17015620
  REMARK    GeneRIF: Tuba controls the shaping of cell junctions through the
            local activation of Cdc42 and its effectors.
REFERENCE   8  (residues 1 to 1577)
  AUTHORS   Kuwano,R., Miyashita,A., Arai,H., Asada,T., Imagawa,M., Shoji,M.,
            Higuchi,S., Urakami,K., Kakita,A., Takahashi,H., Tsukie,T.,
            Toyabe,S., Akazawa,K., Kanazawa,I. and Ihara,Y.
  CONSRTM   Japanese Genetic Study Consortium for Alzeheimer's Disease
  TITLE     Dynamin-binding protein gene on chromosome 10q is associated with
            late-onset Alzheimer's disease
  JOURNAL   Hum Mol Genet 15 (13), 2170-2182 (2006)
   PUBMED   16740596
  REMARK    GeneRIF: Results confirmed DNMBP may be one of the susceptibility
            genes for Alzheimer's disease.
            GeneRIF: Observational study of gene-disease association and
            gene-gene interaction. (HuGE Navigator)
REFERENCE   9  (residues 1 to 1577)
  AUTHORS   Cestra,G., Kwiatkowski,A., Salazar,M., Gertler,F. and De Camilli,P.
  TITLE     Tuba, a GEF for CDC42, links dynamin to actin regulatory proteins
  JOURNAL   Methods Enzymol 404, 537-545 (2005)
   PUBMED   16413298
REFERENCE   10 (residues 1 to 1577)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
  REMARK    GeneRIF: functions to bring together dynamin with actin regulatory
            proteins
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB481528.1, AL833283.1,
            AB023227.1 and AI023943.1.
            
            On Dec 18, 2003 this sequence version replaced XP_050742.5.
            
            Summary: This gene encodes a protein belonging to the guanine
            nucleotide exchange factor family, and which regulates the
            configuration of cell junctions. It contains multiple binding sites
            for dynamin and thus links dynamin to actin regulatory proteins.
            Polymorphisms in this gene have been linked to Alzheimer's disease
            in some populations, though there are conflicting reports of such
            linkages in other populations. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.29545.1, AL833283.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324109.9/ ENSP00000315659.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.2"
     Protein         1..1577
                     /product="dynamin-binding protein isoform a"
                     /note="scaffold protein TUBA"
                     /calculated_mol_wt=177217
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          6..56
                     /region_name="SH3_DNMBP_N1"
                     /note="First N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11794"
                     /db_xref="CDD:212728"
     Site            order(11,13,16,20,38..39,52,54..55)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212728"
     Region          70..123
                     /region_name="SH3_DNMBP_N2"
                     /note="Second N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11795"
                     /db_xref="CDD:212729"
     Site            order(75,77,80,84,102..103,117,119..120)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212729"
     Region          149..199
                     /region_name="SH3_DNMBP_N3"
                     /note="Third N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11796"
                     /db_xref="CDD:212730"
     Site            order(154,156,159,163,181..182,195,197..198)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212730"
     Region          211..244
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          247..296
                     /region_name="SH3_DNMBP_N4"
                     /note="Fourth N-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11797"
                     /db_xref="CDD:212731"
     Site            order(252,254,257,261,279..280,293,295..296)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212731"
     Region          335..395
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          591..624
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          639..659
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Site            684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          785..965
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(791,795,884,916..917,920..921,923..924,927..928,
                     931..932,935,961,965)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          1017..1208
                     /region_name="BAR_DNMBP"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin
                     Binding Protein; cd07589"
                     /db_xref="CDD:153273"
     Site            order(1029,1032..1033,1037,1039..1040,1043..1044,
                     1046..1047,1061..1062,1064..1065,1068..1069,1071..1072,
                     1075,1081,1084..1085,1169,1172..1173,1175,1180,1183..1184,
                     1186..1187,1190..1191,1194..1195,1197..1198,1201..1202,
                     1204..1205)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153273"
     Region          1289..1345
                     /region_name="SH3_DNMBP_C1"
                     /note="First C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba; cd11798"
                     /db_xref="CDD:212732"
     Site            order(1294,1296,1299,1303,1325..1326,1339,1341..1342)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212732"
     Region          1348..1487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6XZF7.1)"
     Region          1517..1573
                     /region_name="SH3_DNMBP_C2"
                     /note="Second C-terminal Src homology 3 domain of Dynamin
                     Binding Protein, also called Tuba, and similar domains;
                     cd12141"
                     /db_xref="CDD:213017"
     Site            order(1522,1524,1527,1531,1553..1554,1567,1569..1570)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213017"
     CDS             1..1577
                     /gene="DNMBP"
                     /gene_synonym="ARHGEF36; CTRCT48; TUBA"
                     /coded_by="NM_015221.4:121..4854"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7485.1"
                     /db_xref="GeneID:23268"
                     /db_xref="HGNC:HGNC:30373"
                     /db_xref="MIM:611282"
ORIGIN      
        1 meagsvvrai fdfcpsvsee lplfvgdiie vlavvdefwl lgkkedvtgq fpssfveivt
       61 ipslkegerl fvciceftsq eldnlplhrg dlvildgipt agwlqgrscw gargffpssc
      121 vrelclssqs rqwhsqsalf qipeysmgqa ralmglsaql deeldfregd vitiigvpep
      181 gwfegelegr rgifpegfve llgplrtvde svssgnqddc ivngevdtpv geeeigpded
      241 eeepgtygva lyrfqalepn eldfevgdki rilatledgw legslkgrtg ifpyrfvklc
      301 pdtrveetma lpqegslari petsldclen tlgveeqrhe tsdheaeepd ciiseaptsp
      361 lghltseydt drnsyqdedt aggpprspgv ewemplatds ptsdptevvn gissqpqvpf
      421 hpnlqksqyy stvggshphs eqypdllple artrdyaslp pkrmysqlkt lqkpvlplyr
      481 gssvsasrvv kprqsspqlh nlasytkkhh tssvysiser lemkpgpqaq glvmeaaths
      541 qgdgstdlds kltqqliefe kslagpgtep dkilrhfsim dfnsekdivr gsskliteqe
      601 lperrkalrp ppprpctpvs tsphllvdqn lkpapplvvr psrpaplpps aqqrtnavsp
      661 kllsrhrptc etlekegpgh mgrsldqtsp cplvlvriee merdldmysr aqeelnlmle
      721 ekqdessrae tledlkfces nieslnmelq qlremtllss qssslvapsg svsaenpeqr
      781 mlekrakvie ellqterdyi rdlemcieri mvpmqqaqvp nidfeglfgn mqmvikvskq
      841 llaaleisda vgpvflghrd elegtykiyc qnhdeaiall eiyekdekiq khlqdsladl
      901 kslynewgct nyinlgsfli kpvqrvmryp lllmellnst peshpdkvpl tnavlavkei
      961 nvnineykrr kdlvlkyrkg dedslmekis klnihsiikk snrvsshlkh ltgfapqikd
     1021 evfeeteknf rmqerliksf irdlslylqh iresacvkvv aavsmwdvcm erghrdleqf
     1081 ervhryisdq lftnfkerte rlvisplnql lsmftgphkl vqkrfdklld fyncteraek
     1141 lkdkktleel qsarnnyeal naqlldelpk fhqyaqglft ncvhgyaeah cdfvhqaleq
     1201 lkpllsllkv agregnliai fheehsrvlq qlqvftffpe slpatkkpfe rktidrqsar
     1261 kpllglpsym lqseelrasl laryppeklf qaernfnaaq dldvsllegd lvgvikkkdp
     1321 mgsqnrwlid ngvtkgfvys sflkpynprr shsdasvgsh sstesehgss sprfprqnsg
     1381 stltfnpssm avsftsgscq kqpqdasppp kecdqgtlsa slnpsnsess psrcpsdpds
     1441 tsqprsgdsa dvardvkqpt atprsyrnfr hpeivgysvp grngqsqdlv kgcartaqap
     1501 edrstepdgs eaegnqvyfa vytfkarnpn elsvsanqkl kilefkdvtg ntewwlaevn
     1561 gkkgyvpsny irkteyt
//
LOCUS       NP_004848                427 aa            linear   PRI 20-NOV-2025
DEFINITION  A-kinase anchor protein 5 [Homo sapiens].
ACCESSION   NP_004848
VERSION     NP_004848.3
DBSOURCE    REFSEQ: accession NM_004857.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Tutzauer,J., Serafin,D.S., Schmidt,T., Olde,B., Caron,K.M. and
            Leeb-Lundberg,L.M.F.
  TITLE     G protein-coupled estrogen receptor (GPER)/GPR30 forms a complex
            with the beta1-adrenergic receptor, a membrane-associated guanylate
            kinase (MAGUK) scaffold protein, and protein kinase A anchoring
            protein (AKAP) 5 in MCF7 breast cancer cells
  JOURNAL   Arch Biochem Biophys 752, 109882 (2024)
   PUBMED   38211639
  REMARK    GeneRIF: G protein-coupled estrogen receptor (GPER)/GPR30 forms a
            complex with the beta1-adrenergic receptor, a membrane-associated
            guanylate kinase (MAGUK) scaffold protein, and protein kinase A
            anchoring protein (AKAP) 5 in MCF7 breast cancer cells.
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Lin,Y.P., Scappini,E., Landaverde,C., Parekh-Glitsch,F.,
            Tucker,C.J., Mirams,G.R. and Parekh,A.B.
  TITLE     Nuanced Interactions between AKAP79 and STIM1 with Orai1 Ca2+
            Channels at Endoplasmic Reticulum-Plasma Membrane Junctions Sustain
            NFAT Activation
  JOURNAL   Mol Cell Biol 42 (11), e0017522 (2022)
   PUBMED   36317924
  REMARK    GeneRIF: Nuanced Interactions between AKAP79 and STIM1 with Orai1
            Ca[2+] Channels at Endoplasmic Reticulum-Plasma Membrane Junctions
            Sustain NFAT Activation.
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Watson,M., Almeida,T.B., Ray,A., Hanack,C., Elston,R., Btesh,J.,
            McNaughton,P.A. and Stott,K.
  TITLE     Hidden Multivalency in Phosphatase Recruitment by a Disordered AKAP
            Scaffold
  JOURNAL   J Mol Biol 434 (16), 167682 (2022)
   PUBMED   35697294
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Kar,P., Barak,P., Zerio,A., Lin,Y.P., Parekh,A.J., Watts,V.J.,
            Cooper,D.M.F., Zaccolo,M., Kramer,H. and Parekh,A.B.
  TITLE     AKAP79 Orchestrates a Cyclic AMP Signalosome Adjacent to Orai1 Ca2+
            Channels
  JOURNAL   Function (Oxf) 2 (5), zqab036 (2021)
   PUBMED   34458850
  REMARK    GeneRIF: AKAP79 Orchestrates a Cyclic AMP Signalosome Adjacent to
            Orai1 Ca[2+] Channels.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Coghlan,V.M., Perrino,B.A., Howard,M., Langeberg,L.K., Hicks,J.B.,
            Gallatin,W.M. and Scott,J.D.
  TITLE     Association of protein kinase A and protein phosphatase 2B with a
            common anchoring protein
  JOURNAL   Science 267 (5194), 108-111 (1995)
   PUBMED   7528941
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Carr,D.W., Stofko-Hahn,R.E., Fraser,I.D., Cone,R.D. and Scott,J.D.
  TITLE     Localization of the cAMP-dependent protein kinase to the
            postsynaptic densities by A-kinase anchoring proteins.
            Characterization of AKAP 79
  JOURNAL   J Biol Chem 267 (24), 16816-16823 (1992)
   PUBMED   1512224
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Carr,D.W., Hausken,Z.E., Fraser,I.D., Stofko-Hahn,R.E. and
            Scott,J.D.
  TITLE     Association of the type II cAMP-dependent protein kinase with a
            human thyroid RII-anchoring protein. Cloning and characterization
            of the RII-binding domain
  JOURNAL   J Biol Chem 267 (19), 13376-13382 (1992)
   PUBMED   1618839
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Hirsch,A.H., Glantz,S.B., Li,Y., You,Y. and Rubin,C.S.
  TITLE     Cloning and expression of an intron-less gene for AKAP 75, an
            anchor protein for the regulatory subunit of cAMP-dependent protein
            kinase II beta
  JOURNAL   J Biol Chem 267 (4), 2131-2134 (1992)
   PUBMED   1733921
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Carr,D.W., Stofko-Hahn,R.E., Fraser,I.D., Bishop,S.M., Acott,T.S.,
            Brennan,R.G. and Scott,J.D.
  TITLE     Interaction of the regulatory subunit (RII) of cAMP-dependent
            protein kinase with RII-anchoring proteins occurs through an
            amphipathic helix binding motif
  JOURNAL   J Biol Chem 266 (22), 14188-14192 (1991)
   PUBMED   1860836
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA942424.1, BC057229.1,
            AL122035.6 and BC131516.1.
            
            On Oct 12, 2007 this sequence version replaced NP_004848.2.
            
            Summary: The A-kinase anchor proteins (AKAPs) are a group of
            structurally diverse proteins, which have the common function of
            binding to the regulatory subunit of protein kinase A (PKA) and
            confining the holoenzyme to discrete locations within the cell.
            This gene encodes a member of the AKAP family. The encoded protein
            binds to the RII-beta regulatory subunit of PKA, and also to
            protein kinase C and the phosphatase calcineurin. It is
            predominantly expressed in cerebral cortex and may anchor the PKA
            protein at postsynaptic densities (PSD) and be involved in the
            regulation of postsynaptic events. It is also expressed in T
            lymphocytes and may function to inhibit interleukin-2 transcription
            by disrupting calcineurin-dependent dephosphorylation of NFAT.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315336.1, SRR1660809.28018.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394718.4/ ENSP00000378207.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q23.3"
     Protein         1..427
                     /product="A-kinase anchor protein 5"
                     /note="A-kinase anchoring protein 75/79; AKAP 79; A-kinase
                     anchor protein 79 kDa; cAMP-dependent protein kinase
                     regulatory subunit II high affinity-binding protein; A
                     kinase (PRKA) anchor protein 5"
                     /calculated_mol_wt=46957
     Region          1..170
                     /region_name="domain"
                     /note="essential to the intracellular anchoring function"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YVF0; propagated from
                     UniProtKB/Swiss-Prot (P24588.3)"
     Region          73..103
                     /region_name="AKAP domain"
     Region          77..102
                     /region_name="WSK"
                     /note="WSK motif; pfam03832"
                     /db_xref="CDD:461069"
     Region          171..205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24588.3)"
     Region          239..269
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24588.3)"
     Region          281..333
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24588.3)"
     Region          392..405
                     /region_name="PKA-RII subunit binding domain"
     Region          410..427
                     /region_name="Tethers NFATC2 to CRAC channels.
                     /evidence=ECO:0000269|PubMed:33941685"
                     /note="propagated from UniProtKB/Swiss-Prot (P24588.3)"
     CDS             1..427
                     /gene="AKAP5"
                     /gene_synonym="AKAP75; AKAP79; H21"
                     /coded_by="NM_004857.3:379..1662"
                     /db_xref="CCDS:CCDS9764.1"
                     /db_xref="GeneID:9495"
                     /db_xref="HGNC:HGNC:375"
                     /db_xref="MIM:604688"
ORIGIN      
        1 mettiseihv enkdekrsae gspgaerqke kasmlcfkrr kkaakalkpk agseaadvar
       61 kcpqeagasd qpeptrgawa slkrlvtrrk rsesskqqkp legemqpain aedadlskkk
      121 aksrlkipci kfprgpkrsn hskiiedsdc sikvqeeaei ldiqtqtpln dqatkakstq
      181 dlsegisrkd gdevcesnvs nsttsgekvi svelgldngh saiqtgtlil eeietikekq
      241 dvqpqqaspl etsetdhqqp vlsdvpplpa ipdqqiveea snstlesapn gkdyesteiv
      301 aeetkpkdte lsqesdfken giteekskse eskrmepiai iitdteisef dvtksknvpk
      361 qflisaeneq vgvfandngf edrtseqyet llietasslv knaiqlsieq lvnemasddn
      421 kinnllq
//
LOCUS       NP_001253967             269 aa            linear   PRI 20-NOV-2025
DEFINITION  centromere protein K isoform 1 [Homo sapiens].
ACCESSION   NP_001253967
VERSION     NP_001253967.1
DBSOURCE    REFSEQ: accession NM_001267038.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Li,G., Shen,J., Cheng,W., Wang,X., Wang,D., Song,Y., Chen,Y.,
            Li,X., Zhang,M., Ding,Y., Ma,X., Qian,Q., Zhang,G., Ji,J. and
            Liu,B.
  TITLE     CENPK orchestrates ovarian cancer progression via GOLPH3-Mediated
            activation of mTOR signaling
  JOURNAL   Mol Cell Endocrinol 589, 112253 (2024)
   PUBMED   38670220
  REMARK    GeneRIF: CENPK orchestrates ovarian cancer progression via
            GOLPH3-Mediated activation of mTOR signaling.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Li,X., Han,Y.R., Xuefeng,X., Ma,Y.X., Xing,G.S., Yang,Z.W.,
            Zhang,Z., Shi,L. and Wu,X.L.
  TITLE     Lentivirus-mediated short hairpin RNA interference of CENPK
            inhibits growth of colorectal cancer cells with overexpression of
            Cullin 4A
  JOURNAL   World J Gastroenterol 28 (37), 5420-5443 (2022)
   PUBMED   36312839
  REMARK    GeneRIF: Lentivirus-mediated short hairpin RNA interference of
            CENPK inhibits growth of colorectal cancer cells with
            overexpression of Cullin 4A.
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Tian,T., Chen,L., Dou,Z., Yang,Z., Gao,X., Yuan,X., Wang,C.,
            Liu,R., Shen,Z., Gui,P., Teng,M., Meng,X., Hill,D.L., Li,L.,
            Zhang,X., Liu,X., Sun,L., Zang,J. and Yao,X.
  TITLE     Structural insights into human CCAN complex assembled onto DNA
  JOURNAL   Cell Discov 8 (1), 90 (2022)
   PUBMED   36085283
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Tian,H., Wang,F., Deng,Y., Ying,L., Fang,W., Chen,D., Miao,C.,
            Li,H., Sun,S., Ma,Y., Cai,H. and Guo,T.
  TITLE     Centromeric protein K (CENPK) promotes gastric cancer proliferation
            and migration via interacting with XRCC5
  JOURNAL   Gastric Cancer 25 (5), 879-895 (2022)
   PUBMED   35715658
  REMARK    GeneRIF: Centromeric protein K (CENPK) promotes gastric cancer
            proliferation and migration via interacting with XRCC5.
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Okada,M., Cheeseman,I.M., Hori,T., Okawa,K., McLeod,I.X.,
            Yates,J.R. 3rd, Desai,A. and Fukagawa,T.
  TITLE     The CENP-H-I complex is required for the efficient incorporation of
            newly synthesized CENP-A into centromeres
  JOURNAL   Nat Cell Biol 8 (5), 446-457 (2006)
   PUBMED   16622420
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Foltz,D.R., Jansen,L.E., Black,B.E., Bailey,A.O., Yates,J.R. 3rd
            and Cleveland,D.W.
  TITLE     The human CENP-A centromeric nucleosome-associated complex
  JOURNAL   Nat Cell Biol 8 (5), 458-469 (2006)
   PUBMED   16622419
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Obuse,C., Yang,H., Nozaki,N., Goto,S., Okazaki,T. and Yoda,K.
  TITLE     Proteomics analysis of the centromere complex from HeLa interphase
            cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of
            the CEN-complex, while BMI-1 is transiently co-localized with the
            centromeric region in interphase
  JOURNAL   Genes Cells 9 (2), 105-120 (2004)
   PUBMED   15009096
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Yamashita,A., Ito,M., Takamatsu,N. and Shiba,T.
  TITLE     Characterization of Solt, a novel SoxLZ/Sox6 binding protein
            expressed in adult mouse testis
  JOURNAL   FEBS Lett 481 (2), 147-151 (2000)
   PUBMED   10996314
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Taki,T., Hayashi,Y., Taniwaki,M., Seto,M., Ueda,R., Hanada,R.,
            Suzukawa,K., Yokota,J. and Morishita,K.
  TITLE     Fusion of the MLL gene with two different genes, AF-6 and
            AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8
            and 11 in infant leukemia
  JOURNAL   Oncogene 13 (10), 2121-2130 (1996)
   PUBMED   8950979
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG502832.1, BC005400.1 and BC008504.1.
            
            Summary: CENPK is a subunit of a CENPH (MIM 605607)-CENPI (MIM
            300065)-associated centromeric complex that targets CENPA (MIM
            117139) to centromeres and is required for proper kinetochore
            function and mitotic progression (Okada et al., 2006 [PubMed
            16622420]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF315941.1, SRR7346977.403996.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..269
                     /product="centromere protein K isoform 1"
                     /note="leucine zipper protein FKSG14; SoxLZ/Sox6-binding
                     protein Solt; protein AF-5alpha; interphase centromere
                     complex protein 37"
                     /calculated_mol_wt=31524
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BS16.1)"
     Region          10..269
                     /region_name="CENP-K"
                     /note="Centromere-associated protein K; pfam11802"
                     /db_xref="CDD:463355"
     Site            96..97
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-CENPK oncogene; propagated from
                     UniProtKB/Swiss-Prot (Q9BS16.1)"
     CDS             1..269
                     /gene="CENPK"
                     /gene_synonym="AF5alpha; CENP-K; FKSG14; P33; Solt"
                     /coded_by="NM_001267038.2:179..988"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3984.1"
                     /db_xref="GeneID:64105"
                     /db_xref="HGNC:HGNC:29479"
                     /db_xref="MIM:611502"
ORIGIN      
        1 mnqedldpds ttdvgdvtnt eeelirecee mwkdmeecqn klsligtetl tdsnaqlsll
       61 imqvkcltae lsqwqkktpe tipltedvli tlgkeefqkl rqdlemvlst keskneklke
      121 dlereqrwld eqqqimesln vlhselknkv etfsesrifn elktkmlnik eykekllstl
      181 gefledhfpl pdrsvkkkkk niqessvnli tlhemleili nrlfdvphdp yvkisdsfwp
      241 pyvelllrng ialrhpedpt rirleafhq
//
LOCUS       NP_057283                103 aa            linear   PRI 20-NOV-2025
DEFINITION  U6 snRNA-associated Sm-like protein LSm7 [Homo sapiens].
ACCESSION   NP_057283
VERSION     NP_057283.1
DBSOURCE    REFSEQ: accession NM_016199.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Li,C., Zhang,Y., Wang,Y., Ouyang,J., Yang,Y., Zhu,Q., Lu,Y.,
            Kang,T., Li,Y., Xia,M., Chen,J., Li,Q., Zhu,C. and Ye,L.
  TITLE     RNA-binding protein LSM7 facilitates breast cancer metastasis
            through mediating alternative splicing of CD44
  JOURNAL   Life Sci 356, 123013 (2024)
   PUBMED   39182568
  REMARK    GeneRIF: RNA-binding protein LSM7 facilitates breast cancer
            metastasis through mediating alternative splicing of CD44.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Friesen,W.J. and Dreyfuss,G.
  TITLE     Specific sequences of the Sm and Sm-like (Lsm) proteins mediate
            their interaction with the spinal muscular atrophy disease gene
            product (SMN)
  JOURNAL   J Biol Chem 275 (34), 26370-26375 (2000)
   PUBMED   10851237
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Nottrott,S., Hartmuth,K., Fabrizio,P., Urlaub,H., Vidovic,I.,
            Ficner,R. and Luhrmann,R.
  TITLE     Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP
            protein with the 5' stem-loop of U4 snRNA
  JOURNAL   EMBO J 18 (21), 6119-6133 (1999)
   PUBMED   10545122
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Achsel,T., Brahms,H., Kastner,B., Bachi,A., Wilm,M. and Luhrmann,R.
  TITLE     A doughnut-shaped heteromer of human Sm-like proteins binds to the
            3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in
            vitro
  JOURNAL   EMBO J 18 (20), 5789-5802 (1999)
   PUBMED   10523320
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Salgado-Garrido,J., Bragado-Nilsson,E., Kandels-Lewis,S. and
            Seraphin,B.
  TITLE     Sm and Sm-like proteins assemble in two related complexes of deep
            evolutionary origin
  JOURNAL   EMBO J 18 (12), 3451-3462 (1999)
   PUBMED   10369684
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI553911.1, AF182293.1 and BC018621.1.
            
            Summary: Sm-like proteins were identified in a variety of organisms
            based on sequence homology with the Sm protein family (see SNRPD2;
            MIM 601061). Sm-like proteins contain the Sm sequence motif, which
            consists of 2 regions separated by a linker of variable length that
            folds as a loop. The Sm-like proteins are thought to form a stable
            heteromer present in tri-snRNP particles, which are important for
            pre-mRNA splicing.[supplied by OMIM, Apr 2004].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.371098.1, BU535736.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252622.15/ ENSP00000252622.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..103
                     /product="U6 snRNA-associated Sm-like protein LSm7"
                     /note="LSM7 homolog, U6 small nuclear RNA associated; LSM7
                     U6 small nuclear RNA and mRNA degradation associated"
                     /calculated_mol_wt=11471
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UK45.1)"
     Region          9..97
                     /region_name="LSm7"
                     /note="Like-Sm protein 7; cd01729"
                     /db_xref="CDD:212476"
     Site            order(13,15,18..19,24,26..28,31,33,38..45,47,69,71,73..86)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:212476"
     Site            order(23..29,31..43,45..49)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212476"
     Site            order(41,43,77)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212476"
     Site            73..84
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212476"
     CDS             1..103
                     /gene="LSM7"
                     /gene_synonym="LDCA; YNL147W"
                     /coded_by="NM_016199.3:21..332"
                     /db_xref="CCDS:CCDS45907.1"
                     /db_xref="GeneID:51690"
                     /db_xref="HGNC:HGNC:20470"
                     /db_xref="MIM:607287"
ORIGIN      
        1 madkekkkke sildlskyid ktirvkfqgg reasgilkgf dpllnlvldg tieymrdpdd
       61 qykltedtrq lglvvcrgts vvlicpqdgm eaipnpfiqq qda
//
LOCUS       NP_066357                106 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL42 [Homo sapiens].
ACCESSION   NP_066357
VERSION     NP_066357.3
DBSOURCE    REFSEQ: accession NM_021029.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 106)
  AUTHORS   He,Q., Xu,S., Ma,X., Ling,T., Feng,W., Lu,X., Liu,W. and Chen,Z.
  TITLE     Coupled folding-upon-binding of human tumor suppressor MIG6 to lung
            cancer EGFR kinase domain and molecular trimming/stapling of
            MIG6-derived beta-hairpins to target the coupling event
  JOURNAL   Eur Biophys J 52 (1-2), 17-25 (2023)
   PUBMED   36547692
  REMARK    GeneRIF: Coupled folding-upon-binding of human tumor suppressor
            MIG6 to lung cancer EGFR kinase domain and molecular
            trimming/stapling of MIG6-derived beta-hairpins to target the
            coupling event.
REFERENCE   2  (residues 1 to 106)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 106)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 106)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 106)
  AUTHORS   Xu,M., Wang,Y., He,H.T. and Yang,Q.
  TITLE     MiR-589-5p is a potential prognostic marker of hepatocellular
            carcinoma and regulates tumor cell growth by targeting MIG-6
  JOURNAL   Neoplasma 65 (5), 753-761 (2018)
   PUBMED   30249105
  REMARK    GeneRIF: miR-589-5p facilitated the growth of liver cancer cells by
            targeting MIG-6 and could be a prognosis biomarker for
            hepatocellular carcinoma
REFERENCE   6  (residues 1 to 106)
  AUTHORS   Prakash,T., Sharma,V.K., Adati,N., Ozawa,R., Kumar,N., Nishida,Y.,
            Fujikake,T., Takeda,T. and Taylor,T.D.
  TITLE     Expression of conjoined genes: another mechanism for gene
            regulation in eukaryotes
  JOURNAL   PLoS One 5 (10), e13284 (2010)
   PUBMED   20967262
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 106)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   8  (residues 1 to 106)
  AUTHORS   Oeltjen,J.C., Malley,T.M., Muzny,D.M., Miller,W., Gibbs,R.A. and
            Belmont,J.W.
  TITLE     Large-scale comparative sequence analysis of the human and murine
            Bruton's tyrosine kinase loci reveals conserved regulatory domains
  JOURNAL   Genome Res 7 (4), 315-329 (1997)
   PUBMED   9110171
REFERENCE   9  (residues 1 to 106)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 106)
  AUTHORS   Davies,M.S., Henney,A., Ward,W.H. and Craig,R.K.
  TITLE     Characterisation of an mRNA encoding a human ribosomal protein
            homologous to the yeast L44 ribosomal protein
  JOURNAL   Gene 45 (2), 183-191 (1986)
   PUBMED   3542712
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC062219.1, AW150895.1 and AL035422.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 22, 2018 this sequence version replaced NP_066357.2.
            
            Summary: Cytoplasmic ribosomes, organelles that catalyze protein
            synthesis, consist of a small 40S subunit and a large 60S subunit.
            Together these subunits are composed of 4 RNA species and
            approximately 80 structurally distinct proteins. This gene encodes
            a ribosomal protein that is a component of the 60S subunit. The
            protein, which shares sequence similarity with yeast ribosomal
            protein L44, belongs to the L44E (L36AE) family of ribosomal
            proteins. Although this gene has been referred to as ribosomal
            protein L44 (RPL44), its official name is ribosomal protein L36a
            (RPL36A). This gene and the human gene officially named ribosomal
            protein L36a-like (RPL36AL) encode nearly identical proteins;
            however, they are distinct genes. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome. Naturally occurring
            read-through transcription occurs between this locus and the
            heterogeneous nuclear ribonucleoprotein H2 (H') gene. [provided by
            RefSeq, Jan 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.42424.1,
                                           SRR1163658.249496.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000553110.8/ ENSP00000446503.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..106
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.1"
     Protein         1..106
                     /product="large ribosomal subunit protein eL42"
                     /note="60S ribosomal protein L44; L44-like ribosomal
                     protein; dJ164F3.3 (ribosomal protein L44); cell
                     growth-inhibiting gene 15 protein; cell migration-inducing
                     gene 6 protein"
                     /calculated_mol_wt=12310
     Region          1..86
                     /region_name="PTZ00157"
                     /note="60S ribosomal protein L36a; Provisional"
                     /db_xref="CDD:240296"
     Region          34..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P83881.2)"
     CDS             1..106
                     /gene="RPL36A"
                     /gene_synonym="eL42; L36A; L44L; MIG6; RPL44"
                     /coded_by="NM_021029.6:34..354"
                     /db_xref="CCDS:CCDS14483.3"
                     /db_xref="GeneID:6173"
                     /db_xref="HGNC:HGNC:10359"
                     /db_xref="MIM:300902"
ORIGIN      
        1 mvnvpktrrt fckkcgkhqp hkvtqykkgk dslyaqgkrr ydrkqsgygg qtkpifrkka
       61 kttkkivlrl ecvepncrsk rmlaikrckh felggdkkrk gqviqf
//
LOCUS       NP_003173                129 aa            linear   PRI 20-NOV-2025
DEFINITION  protachykinin-1 isoform beta precursor [Homo sapiens].
ACCESSION   NP_003173
VERSION     NP_003173.1
DBSOURCE    REFSEQ: accession NM_003182.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Shiraishi,A., Wada,A. and Satake,H.
  TITLE     Evolutionary scenarios for the specific recognition of
            nonhomologous endogenous peptides by G protein-coupled receptor
            paralogs
  JOURNAL   J Biol Chem 301 (2), 108125 (2025)
   PUBMED   39725036
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Wang,X., Zheng,J. and Xu,H.
  TITLE     Neural Circuitry Involving Substance P in Male Sexual Behavior
  JOURNAL   Neurosci Bull 40 (4), 544-546 (2024)
   PUBMED   38376747
  REMARK    GeneRIF: Neural Circuitry Involving Substance P in Male Sexual
            Behavior.
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Barde,S., Aguila,J., Zhong,W., Solarz,A., Mei,I., Prud'homme,J.,
            Palkovits,M., Turecki,G., Mulder,J., Uhlen,M., Nagy,C.,
            Mechawar,N., Hedlund,E. and Hokfelt,T.
  TITLE     Substance P, NPY, CCK and their receptors in five brain regions in
            major depressive disorder with transcriptomic analysis of locus
            coeruleus neurons
  JOURNAL   Eur Neuropsychopharmacol 78, 54-63 (2024)
   PUBMED   37931511
  REMARK    GeneRIF: Substance P, NPY, CCK and their receptors in five brain
            regions in major depressive disorder with transcriptomic analysis
            of locus coeruleus neurons.
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Gursoy,G., Karadag,S., Kose,S., Sakaci,T., Kocak,S.Y.,
            Doventas,Y.E., Oktar,A.C. and Bayar,M.D.
  TITLE     The role of calcitonin gene-related peptide and substance P in the
            pathogenesis of dialysis headache
  JOURNAL   Hemodial Int 28 (1), 85-91 (2024)
   PUBMED   37852938
  REMARK    GeneRIF: The role of calcitonin gene-related peptide and substance
            P in the pathogenesis of dialysis headache.
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Madsen,J.J., Petersen,J.E., Christensen,D.P., Hansen,J.B.,
            Schwartz,T.W., Frimurer,T.M. and Olsen,O.H.
  TITLE     Deciphering specificity and cross-reactivity in tachykinin NK1 and
            NK2 receptors
  JOURNAL   J Biol Chem 299 (12), 105438 (2023)
   PUBMED   37944618
  REMARK    GeneRIF: Deciphering specificity and cross-reactivity in tachykinin
            NK1 and NK2 receptors.
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Bannon,M.J., Poosch,M.S., Haverstick,D.M., Mandal,A., Xue,I.C.,
            Shibata,K. and Dragovic,L.J.
  TITLE     Preprotachykinin gene expression in the human basal ganglia:
            characterization of mRNAs and pre-mRNAs produced by alternate RNA
            splicing
  JOURNAL   Brain Res Mol Brain Res 12 (1-3), 225-231 (1992)
   PUBMED   1312203
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Takeda,Y., Chou,K.B., Takeda,J., Sachais,B.S. and Krause,J.E.
  TITLE     Molecular cloning, structural characterization and functional
            expression of the human substance P receptor
  JOURNAL   Biochem Biophys Res Commun 179 (3), 1232-1240 (1991)
   PUBMED   1718267
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Chiwakata,C., Brackmann,B., Hunt,N., Davidoff,M., Schulze,W. and
            Ivell,R.
  TITLE     Tachykinin (substance-P) gene expression in Leydig cells of the
            human and mouse testis
  JOURNAL   Endocrinology 128 (5), 2441-2448 (1991)
   PUBMED   1708336
REFERENCE   9  (residues 1 to 129)
  AUTHORS   McGregor,G.P. and Conlon,J.M.
  TITLE     Characterization of the C-terminal flanking peptide of human
            beta-preprotachykinin
  JOURNAL   Peptides 11 (5), 907-910 (1990)
   PUBMED   2284201
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Theodorsson-Norheim,E., Jornvall,H., Andersson,M., Norheim,I.,
            Oberg,K. and Jacobsson,G.
  TITLE     Isolation and characterization of neurokinin A, neurokinin A(3-10)
            and neurokinin A(4-10) from a neutral water extract of a metastatic
            ileal carcinoid tumour
  JOURNAL   Eur J Biochem 166 (3), 693-697 (1987)
   PUBMED   3038549
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN992454.1, AF050655.1 and
            U37529.1.
            
            Summary: This gene encodes four products of the tachykinin peptide
            hormone family, substance P and neurokinin A, as well as the
            related peptides, neuropeptide K and neuropeptide gamma. These
            hormones are thought to function as neurotransmitters which
            interact with nerve receptors and smooth muscle cells. They are
            known to induce behavioral responses and function as vasodilators
            and secretagogues. Substance P is an antimicrobial peptide with
            antibacterial and antifungal properties. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Nov 2014].
            
            Transcript Variant: Transcript variant beta encodes the full-length
            form of this gene. It encodes hormones substance P, neurokinin A,
            as well as the neuropeptide K.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018047.1, AK222957.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000319273.10/
                                                  ENSP00000321106.5
            Protein has antimicrobial activity :: PMID: 12074933
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3"
     Protein         1..129
                     /product="protachykinin-1 isoform beta precursor"
                     /note="neuropeptide gamma; neuropeptide K; tachykinin,
                     precursor 1 (substance K, substance P, neurokinin 1,
                     neurokinin 2, neuromedin L, neurokinin alpha, neuropeptide
                     K, neuropeptide gamma); tachykinin 2; protachykinin;
                     preprotachykinin; neurokinin A; protachykinin-1; PPT"
                     /calculated_mol_wt=12910
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2112
     proprotein      20..129
                     /product="protachykinin-1 isoform beta"
                     /calculated_mol_wt=12910
     mat_peptide     58..68
                     /product="substance P"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     12074933]"
                     /calculated_mol_wt=1349
     Site            59..60
                     /site_type="cleavage"
                     /note="Cleavage, by FAP.
                     /evidence=ECO:0000269|PubMed:21314817; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     Site            63..64
                     /site_type="cleavage"
                     /note="Cleavage, by MME.
                     /evidence=ECO:0000269|PubMed:6208535; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     Site            64..65
                     /site_type="cleavage"
                     /note="Cleavage, by MME.
                     /evidence=ECO:0000269|PubMed:6208535; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     Site            65..66
                     /site_type="cleavage"
                     /note="Cleavage, by ACE.
                     /evidence=ECO:0000269|PubMed:6208535; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     Site            66..67
                     /site_type="cleavage"
                     /note="Cleavage, by ACE and MME.
                     /evidence=ECO:0000269|PubMed:6208535; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     Site            68
                     /site_type="amidation"
                     /note="Methionine amide.
                     /evidence=ECO:0000269|PubMed:3770210; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     mat_peptide     72..107
                     /product="neuropeptide K"
                     /calculated_mol_wt=3982
     mat_peptide     98..107
                     /product="neurokinin A"
                     /calculated_mol_wt=1134
     Site            107
                     /site_type="amidation"
                     /note="Methionine amide.
                     /evidence=ECO:0000269|PubMed:3038549,
                     ECO:0000269|PubMed:3770210; propagated from
                     UniProtKB/Swiss-Prot (P20366.1)"
     CDS             1..129
                     /gene="TAC1"
                     /gene_synonym="Hs.2563; NK2; NKNA; NPK; TAC2"
                     /coded_by="NM_003182.3:120..509"
                     /note="isoform beta precursor is encoded by transcript
                     variant beta"
                     /db_xref="CCDS:CCDS5649.1"
                     /db_xref="GeneID:6863"
                     /db_xref="HGNC:HGNC:11517"
                     /db_xref="MIM:162320"
ORIGIN      
        1 mkilvalavf flvstqlfae eiganddlny wsdwydsdqi keelpepfeh llqriarrpk
       61 pqqffglmgk rdadssiekq vallkalygh gqishkrhkt dsfvglmgkr alnsvayers
      121 amqnyerrr
//
LOCUS       NP_001339539             413 aa            linear   PRI 20-NOV-2025
DEFINITION  propionyl-CoA carboxylase alpha chain, mitochondrial isoform i
            [Homo sapiens].
ACCESSION   NP_001339539 XP_016876106
VERSION     NP_001339539.1
DBSOURCE    REFSEQ: accession NM_001352610.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Wang,J., Cui,M., Liu,Y., Chen,M., Xu,J., Xia,J., Sun,J., Jiang,L.,
            Fang,W., Song,H. and Cheng,C.
  TITLE     The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival
  JOURNAL   Appl Environ Microbiol 90 (6), e0213523 (2024)
   PUBMED   38727222
  REMARK    GeneRIF: The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival.
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Bychkov,I., Galushkin,A., Filatova,A., Nekrasov,A., Kurkina,M.,
            Baydakova,G., Ilyushkina,A., Skoblov,M. and Zakharova,E.
  TITLE     Functional Analysis of the PCCA and PCCB Gene Variants Predicted to
            Affect Splicing
  JOURNAL   Int J Mol Sci 22 (8), 4154 (2021)
   PUBMED   33923806
  REMARK    GeneRIF: Functional Analysis of the PCCA and PCCB Gene Variants
            Predicted to Affect Splicing.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Kennerknecht,I., Klett,C. and Hameister,H.
  TITLE     Assignment of the human gene propionyl coenzyme A carboxylase,
            alpha-chain, (PCCA) to chromosome 13q32 by in situ hybridization
  JOURNAL   Genomics 14 (2), 550-551 (1992)
   PUBMED   1427880
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Lamhonwah,A.M., Mahuran,D. and Gravel,R.A.
  TITLE     Human mitochondrial propionyl-CoA carboxylase: localization of the
            N-terminus of the pro- and mature alpha chains in the deduced
            primary sequence of a full-length cDNA
  JOURNAL   Nucleic Acids Res 17 (11), 4396 (1989)
   PUBMED   2740237
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Lamhonwah,A.M., Quan,F. and Gravel,R.A.
  TITLE     Sequence homology around the biotin-binding site of human
            propionyl-CoA carboxylase and pyruvate carboxylase
  JOURNAL   Arch Biochem Biophys 254 (2), 631-636 (1987)
   PUBMED   3555348
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,
            Quan,F. and Gravel,R.A.
  TITLE     Isolation of cDNA clones coding for the alpha and beta chains of
            human propionyl-CoA carboxylase: chromosomal assignments and DNA
            polymorphisms associated with PCCA and PCCB genes
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4864-4868 (1986)
   PUBMED   3460076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355338.33, AL356575.8,
            AL353697.21 and AL136526.27.
            
            On Jun 18, 2017 this sequence version replaced XP_016876106.1.
            
            Summary: The protein encoded by this gene is the alpha subunit of
            the heterodimeric mitochondrial enzyme Propionyl-CoA carboxylase.
            PCCA encodes the biotin-binding region of this enzyme. Mutations in
            either PCCA or PCCB (encoding the beta subunit) lead to an enzyme
            deficiency resulting in propionic acidemia. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.24632.1,
                                           SRR1803611.215420.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..413
                     /product="propionyl-CoA carboxylase alpha chain,
                     mitochondrial isoform i"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, alpha
                     polypeptide; propionyl-CoA carboxylase alpha chain,
                     mitochondrial; PCCase alpha subunit; propanoyl-CoA:carbon
                     dioxide ligase alpha subunit; pccA complementation group;
                     propionyl-CoA carboxylase alpha subunit; propionyl CoA
                     carboxylase, alpha polypeptide"
                     /calculated_mol_wt=45274
     Region          <1..197
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          210..338
                     /region_name="PCC_BT"
                     /note="Propionyl-coenzyme A carboxylase BT domain;
                     pfam18140"
                     /db_xref="CDD:465666"
     Region          346..412
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(369,378..380,387)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            379
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..413
                     /gene="PCCA"
                     /coded_by="NM_001352610.2:895..2136"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:5095"
                     /db_xref="HGNC:HGNC:8653"
                     /db_xref="MIM:232000"
ORIGIN      
        1 mgeqavalar avkyssagtv eflvdskknf yflemntrlq vehpvtecit gldlvqemir
       61 vakgyplrhk qadiringwa vecrvyaedp yksfglpsig rlsqyqeplh lpgvrvdsgi
      121 qpgsdisiyy dpmisklity gsdrtealkr madaldnyvi rgvthniall reviinsrfv
      181 kgdistkfls dvypdgfkgh mltkseknql laiasslfva fqlraqhfqe nsrmpvikpd
      241 ianwelsvkl hdkvhtvvas nngsvfsvev dgsklnvtst wnlaspllsv svdgtqrtvq
      301 clsreaggnm siqflgtvyk vniltrlaae lnkfmlekvt edtssvlrsp mpgvvvavsv
      361 kpgdavaegq eicvieamkm qnsmtagktg tvksvhcqag dtvgegdllv ele
//
LOCUS       NP_872634                699 aa            linear   PRI 20-NOV-2025
DEFINITION  SRSF protein kinase 2 isoform a [Homo sapiens].
ACCESSION   NP_872634
VERSION     NP_872634.1
DBSOURCE    REFSEQ: accession NM_182692.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 699)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 699)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 699)
  AUTHORS   Yip,R.P.H., Kwok,D.C.Y., Lai,L.T.F., Ho,S.M., Wong,I.C.K.,
            Chan,C.P., Lau,W.C.Y. and Ngo,J.C.K.
  TITLE     SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid Assembly
            via Docking Interaction
  JOURNAL   PLoS Pathog 20 (2), e1011978 (2024)
   PUBMED   38324561
  REMARK    GeneRIF: SRPK2 Mediates HBV Core Protein Phosphorylation and Capsid
            Assembly via Docking Interaction.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 699)
  AUTHORS   Yang,Z. and Ding,W.X.
  TITLE     The pre-mRNA alternative splicing regulated by SRPK2: A new player
            in alcohol-associated liver disease?
  JOURNAL   Hepatology 78 (5), 1329-1331 (2023)
   PUBMED   37183907
  REMARK    GeneRIF: The pre-mRNA alternative splicing regulated by SRPK2: A
            new player in alcohol-associated liver disease?
REFERENCE   5  (residues 1 to 699)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 699)
  AUTHORS   Koizumi,J., Okamoto,Y., Onogi,H., Mayeda,A., Krainer,A.R. and
            Hagiwara,M.
  TITLE     The subcellular localization of SF2/ASF is regulated by direct
            interaction with SR protein kinases (SRPKs)
  JOURNAL   J Biol Chem 274 (16), 11125-11131 (1999)
   PUBMED   10196197
REFERENCE   7  (residues 1 to 699)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
REFERENCE   8  (residues 1 to 699)
  AUTHORS   Kuroyanagi,N., Onogi,H., Wakabayashi,T. and Hagiwara,M.
  TITLE     Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
            speckles
  JOURNAL   Biochem Biophys Res Commun 242 (2), 357-364 (1998)
   PUBMED   9446799
REFERENCE   9  (residues 1 to 699)
  AUTHORS   Bedford,M.T., Chan,D.C. and Leder,P.
  TITLE     FBP WW domains and the Abl SH3 domain bind to a specific class of
            proline-rich ligands
  JOURNAL   EMBO J 16 (9), 2376-2383 (1997)
   PUBMED   9171351
REFERENCE   10 (residues 1 to 699)
  AUTHORS   Gui,J.F., Lane,W.S. and Fu,X.D.
  TITLE     A serine kinase regulates intracellular localization of splicing
            factors in the cell cycle
  JOURNAL   Nature 369 (6482), 678-682 (1994)
   PUBMED   8208298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY031357.1, BC035214.1, CR746049.1 and BU632662.1.
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.145225.1,
                                           SRR1803613.111629.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393651.8/ ENSP00000377262.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..699
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.3"
     Protein         1..699
                     /product="SRSF protein kinase 2 isoform a"
                     /EC_number="2.7.11.1"
                     /note="SFRS protein kinase 2; serine/arginine-rich
                     splicing factor kinase 2; SR protein kinase 2;
                     serine/threonine-protein kinase SRPK2; serine kinase
                     SRPK2; SR-protein-specific kinase 2; serine/arginine-rich
                     protein-specific kinase 2"
                     /calculated_mol_wt=78898
     Region          79..>267
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(98..101,104,106,119,121,157,177..180,225,229..230,
                     232)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Region          <352..394
                     /region_name="2A1904"
                     /note="K+-dependent Na+/Ca+ exchanger; TIGR00927"
                     /db_xref="CDD:273344"
     Region          <515..697
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     CDS             1..699
                     /gene="SRPK2"
                     /gene_synonym="SFRSK2"
                     /coded_by="NM_182692.3:116..2215"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34724.1"
                     /db_xref="GeneID:6733"
                     /db_xref="HGNC:HGNC:11306"
                     /db_xref="MIM:602980"
ORIGIN      
        1 mssrkvlaiq arkrrpkrek hpkkpepqqk aplvpppppp ppppppplpd ptppepeeei
       61 lgsddeeqed padyckggyh pvkigdlfng ryhvirklgw ghfstvwlcw dmqgkrfvam
      121 kvvksaqhyt etaldeikll kcvresdpsd pnkdmvvqli ddfkisgmng ihvcmvfevl
      181 ghhllkwiik snyqglpvrc vksiirqvlq gldylhskck iihtdikpen ilmcvddayv
      241 rrmaaeatew qkagapppsg savstapqqk pigkisknkk kklkkkqkrq aellekrlqe
      301 ieelereaer kiieenitsa apsndqdgey cpevklkttg leeaaeaeta kdngeaedqe
      361 ekedaekeni ekdeddvdqe lanidptwie spktnghien gpfsleqqld dedddeedcp
      421 npeeynldep naesdytyss syeqfngelp ngrhkipesq fpefstslfs gslepvacgs
      481 vlsegsplte qeesspshdr srtvsasstg dlpkaktraa dllvnpldpr nadkirvkia
      541 dlgnacwvhk hftediqtrq yrsievliga gystpadiws tacmafelat gdylfephsg
      601 edysrdedhi ahiiellgsi prhfalsgky sreffnrrge lrhitklkpw slfdvlveky
      661 gwphedaaqf tdflipmlem vpekrasage clrhpwlns
//
LOCUS       NP_001265271             195 aa            linear   PRI 20-NOV-2025
DEFINITION  diablo IAP-binding mitochondrial protein isoform 3 [Homo sapiens].
ACCESSION   NP_001265271
VERSION     NP_001265271.1
DBSOURCE    REFSEQ: accession NM_001278342.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Zhang,D. and Yang,N.
  TITLE     In vivo and in vitro studies on the role of regulating Smac
            expression in the occurrence and development of colon cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (6), 206-210 (2024)
   PUBMED   38836659
  REMARK    GeneRIF: In vivo and in vitro studies on the role of regulating
            Smac expression in the occurrence and development of colon cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Li,Y., Song,Y. and Liang,Y.
  TITLE     AREL1 resists the apoptosis induced by TGF-beta by inhibiting SMAC
            in vascular endothelial cells
  JOURNAL   J Biochem Mol Toxicol 37 (10), e23439 (2023)
   PUBMED   37522329
  REMARK    GeneRIF: AREL1 resists the apoptosis induced by TGF-beta by
            inhibiting SMAC in vascular endothelial cells.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Fu,J., Jin,Y. and Arend,L.J.
  TITLE     Smac3, a novel Smac/DIABLO splicing variant, attenuates the
            stability and apoptosis-inhibiting activity of X-linked inhibitor
            of apoptosis protein
  JOURNAL   J Biol Chem 278 (52), 52660-52672 (2003)
   PUBMED   14523016
  REMARK    GeneRIF: Smac3 is a novel Smac/DIABLO splicing variant and
            attenuates the stability and apoptosis-inhibiting activity of XIAP
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Roberts,D.L., Merrison,W., MacFarlane,M. and Cohen,G.M.
  TITLE     The inhibitor of apoptosis protein-binding domain of Smac is not
            essential for its proapoptotic activity
  JOURNAL   J Cell Biol 153 (1), 221-228 (2001)
   PUBMED   11285287
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Liu,Z., Sun,C., Olejniczak,E.T., Meadows,R.P., Betz,S.F., Oost,T.,
            Herrmann,J., Wu,J.C. and Fesik,S.W.
  TITLE     Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
  JOURNAL   Nature 408 (6815), 1004-1008 (2000)
   PUBMED   11140637
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Srinivasula,S.M., Datta,P., Fan,X.J., Fernandes-Alnemri,T.,
            Huang,Z. and Alnemri,E.S.
  TITLE     Molecular determinants of the caspase-promoting activity of
            Smac/DIABLO and its role in the death receptor pathway
  JOURNAL   J Biol Chem 275 (46), 36152-36157 (2000)
   PUBMED   10950947
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Chai,J., Du,C., Wu,J.W., Kyin,S., Wang,X. and Shi,Y.
  TITLE     Structural and biochemical basis of apoptotic activation by
            Smac/DIABLO
  JOURNAL   Nature 406 (6798), 855-862 (2000)
   PUBMED   10972280
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Verhagen,A.M., Ekert,P.G., Pakusch,M., Silke,J., Connolly,L.M.,
            Reid,G.E., Moritz,R.L., Simpson,R.J. and Vaux,D.L.
  TITLE     Identification of DIABLO, a mammalian protein that promotes
            apoptosis by binding to and antagonizing IAP proteins
  JOURNAL   Cell 102 (1), 43-53 (2000)
   PUBMED   10929712
REFERENCE   10 (residues 1 to 195)
  AUTHORS   Du,C., Fang,M., Li,Y., Li,L. and Wang,X.
  TITLE     Smac, a mitochondrial protein that promotes cytochrome c-dependent
            caspase activation by eliminating IAP inhibition
  JOURNAL   Cell 102 (1), 33-42 (2000)
   PUBMED   10929711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA877400.1, BC046209.1,
            AY313210.1, AK057778.1 and N66735.1.
            
            Summary: This gene encodes an inhibitor of apoptosis protein
            (IAP)-binding protein. The encoded mitochondrial protein enters the
            cytosol when cells undergo apoptosis, and allows activation of
            caspases by binding to inhibitor of apoptosis proteins.
            Overexpression of the encoded protein sensitizes tumor cells to
            apoptosis. A mutation in this gene is associated with young-adult
            onset of nonsyndromic deafness-64. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (3) has a shorter 5' UTR, and
            lacks an alternate in-frame exon in the coding region, compared to
            variant 1. The encoded isoform (3, also known as Smac-delta and
            Smac3) is shorter, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057778.1, SRR1163655.596755.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2152798
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG   :: downstream AUG is associated
                                                  with N-terminal localization
                                                  signal (PMID:14523016)
            gene product(s) localized to mito. :: PMID: 10929711; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..195
                     /product="diablo IAP-binding mitochondrial protein isoform
                     3"
                     /note="second mitochondria-derived activator of caspase;
                     direct IAP-binding protein with low pI; diablo homolog,
                     mitochondrial; diablo-like protein; second
                     mitochondria-derived activator of caspases"
                     /calculated_mol_wt=15919
     transit_peptide 1..55
                     /calculated_mol_wt=6384
     Region          9..195
                     /region_name="Smac_DIABLO"
                     /note="Second Mitochondria-derived Activator of Caspases;
                     pfam09057"
                     /db_xref="CDD:462664"
     mat_peptide     56..195
                     /product="diablo IAP-binding mitochondrial protein isoform
                     3"
                     /calculated_mol_wt=15919
     CDS             1..195
                     /gene="DIABLO"
                     /gene_synonym="DFNA64; SMAC"
                     /coded_by="NM_001278342.1:555..1142"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS9229.1"
                     /db_xref="GeneID:56616"
                     /db_xref="HGNC:HGNC:21528"
                     /db_xref="MIM:605219"
ORIGIN      
        1 maalkswlsr svtsffryrq clcvpvvanf kkrcfselir pwhktvtigf gvtlcavpia
       61 qavytltsly rqytsllgkm nseeedevwq viigaraemt skhqeylkle ttwmtavgls
      121 emaaeaayqt gadqasitar nhiqlvklqv eevhqlsrka etklaeaqie elrqktqeeg
      181 eeraeseqea ylred
//
LOCUS       NP_001116298             659 aa            linear   PRI 20-NOV-2025
DEFINITION  epithelial splicing regulatory protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001116298
VERSION     NP_001116298.1
DBSOURCE    REFSEQ: accession NM_001122826.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 659)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 659)
  AUTHORS   Wang,P., Gao,X., Zheng,W. and Zhang,J.
  TITLE     Potential impact of epithelial splicing regulatory protein 1
            (ESRP1) associated with tumor immunity in pancreatic adenocarcinoma
  JOURNAL   J Proteomics 308, 105277 (2024)
   PUBMED   39127164
  REMARK    GeneRIF: Potential impact of epithelial splicing regulatory protein
            1 (ESRP1) associated with tumor immunity in pancreatic
            adenocarcinoma.
REFERENCE   3  (residues 1 to 659)
  AUTHORS   Chen,S., Zong,Y., Hou,Z., Deng,Z. and Xia,Z.
  TITLE     Splicing factor ESRP1 derived circ_0068162 promotes the progression
            of oral squamous cell carcinoma via the miR-186/JAG axis
  JOURNAL   Carcinogenesis 45 (3), 107-118 (2024)
   PUBMED   37966490
  REMARK    GeneRIF: Splicing factor ESRP1 derived circ_0068162 promotes the
            progression of oral squamous cell carcinoma via the miR-186/JAG
            axis.
REFERENCE   4  (residues 1 to 659)
  AUTHORS   Liu,D., Dredge,B.K., Bert,A.G., Pillman,K.A., Toubia,J., Guo,W.,
            Dyakov,B.J.A., Migault,M.M., Conn,V.M., Conn,S.J., Gregory,P.A.,
            Gingras,A.C., Patel,D., Wu,B. and Goodall,G.J.
  TITLE     ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA
  JOURNAL   Nucleic Acids Res 52 (3), 1387-1403 (2024)
   PUBMED   38015468
  REMARK    GeneRIF: ESRP1 controls biogenesis and function of a large abundant
            multiexon circRNA.
REFERENCE   5  (residues 1 to 659)
  AUTHORS   Wang,W., Taufalele,P.V., Millet,M., Homsy,K., Smart,K.,
            Berestesky,E.D., Schunk,C.T., Rowe,M.M., Bordeleau,F. and
            Reinhart-King,C.A.
  TITLE     Matrix stiffness regulates tumor cell intravasation through
            expression and ESRP1-mediated alternative splicing of MENA
  JOURNAL   Cell Rep 42 (4), 112338 (2023)
   PUBMED   37027295
  REMARK    GeneRIF: Matrix stiffness regulates tumor cell intravasation
            through expression and ESRP1-mediated alternative splicing of MENA.
REFERENCE   6  (residues 1 to 659)
  AUTHORS   Warzecha,C.C., Shen,S., Xing,Y. and Carstens,R.P.
  TITLE     The epithelial splicing factors ESRP1 and ESRP2 positively and
            negatively regulate diverse types of alternative splicing events
  JOURNAL   RNA Biol 6 (5), 546-562 (2009)
   PUBMED   19829082
  REMARK    GeneRIF: results further establish ESRP1 and ESRP2 as global
            regulators of an epithelial splicing regulatory network.
REFERENCE   7  (residues 1 to 659)
  AUTHORS   Warzecha,C.C., Sato,T.K., Nabet,B., Hogenesch,J.B. and
            Carstens,R.P.
  TITLE     ESRP1 and ESRP2 are epithelial cell-type-specific regulators of
            FGFR2 splicing
  JOURNAL   Mol Cell 33 (5), 591-601 (2009)
   PUBMED   19285943
  REMARK    GeneRIF: ESRP1 and ESRP2 are epithelial cell-type-specific
            regulators of FGFR2 splicing.
REFERENCE   8  (residues 1 to 659)
  AUTHORS   Leontieva,O.V. and Ionov,Y.
  TITLE     RNA-binding motif protein 35A is a novel tumor suppressor for
            colorectal cancer
  JOURNAL   Cell Cycle 8 (3), 490-497 (2009)
   PUBMED   19177006
  REMARK    GeneRIF: Results demonstrate that RBM35A functions as a tumor
            suppressor in colon cancer cells, and suggest that RBM35A is
            involved in posttranscriptional regulation of a number of genes by
            exerting a differential effect on protein translation via 5'UTRs of
            mRNAs.
REFERENCE   9  (residues 1 to 659)
  AUTHORS   Rohan,S., Tu,J.J., Kao,J., Mukherjee,P., Campagne,F., Zhou,X.K.,
            Hyjek,E., Alonso,M.A. and Chen,Y.T.
  TITLE     Gene expression profiling separates chromophobe renal cell
            carcinoma from oncocytoma and identifies vesicular transport and
            cell junction proteins as differentially expressed genes
  JOURNAL   Clin Cancer Res 12 (23), 6937-6945 (2006)
   PUBMED   17145811
  REMARK    GeneRIF: The FLJ20171 gene was shown to effectively separate these
            two chromophobe renal cell carcinoma (RCC) and benign oncocytoma
            groups by quantitative reverse transcription-PCR using fresh tissue
            samples, with similar trends seen on formalin-fixed tissues.
REFERENCE   10 (residues 1 to 659)
  AUTHORS   Harrington,J.J., Sherf,B., Rundlett,S., Jackson,P.D., Perry,R.,
            Cain,S., Leventhal,C., Thornton,M., Ramachandran,R.,
            Whittington,J., Lerner,L., Costanzo,D., McElligott,K., Boozer,S.,
            Mays,R., Smith,E., Veloso,N., Klika,A., Hess,J., Cothren,K., Lo,K.,
            Offenbacher,J., Danzig,J. and Ducar,M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat Biotechnol 19 (5), 440-445 (2001)
   PUBMED   11329013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX647570.1, BC099916.1, BC052574.1, BG212336.1, BG182742.1 and
            AI990751.1.
            
            Summary: ESPR1 is an epithelial cell-type-specific splicing
            regulator (Warzecha et al., 2009 [PubMed 19285943]).[supplied by
            OMIM, Aug 2009].
            
            Transcript Variant: This variant (3) has multiple differences in
            the 3' coding region, compared to variant 1, one of which results
            in a protein (isoform 3) with a shorter, distinct C-terminus when
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX647570.1, SRR14038197.64436.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..659
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..659
                     /product="epithelial splicing regulatory protein 1 isoform
                     3"
                     /note="RNA-binding protein 35A; RNA-binding motif protein
                     35A"
                     /calculated_mol_wt=73002
     Region          29..168
                     /region_name="DnaQ_like_exo"
                     /note="DnaQ-like (or DEDD) 3'-5' exonuclease domain
                     superfamily; cl10012"
                     /db_xref="CDD:447876"
     Region          216..308
                     /region_name="RRM1_ESRP1"
                     /note="RNA recognition motif 1 (RRM1) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12736"
                     /db_xref="CDD:410134"
     Region          310..419
                     /region_name="RRM2_ESRP1"
                     /note="RNA recognition motif 2 (RRM2) found in epithelial
                     splicing regulatory protein 1 (ESRP1) and similar
                     proteins; cd12739"
                     /db_xref="CDD:410136"
     Region          444..524
                     /region_name="RRM3_ESRP1_ESRP2"
                     /note="RNA recognition motif 3 (RRM3) found in epithelial
                     splicing regulatory protein ESRP1, ESRP2 and similar
                     proteins; cd12742"
                     /db_xref="CDD:410138"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H6T0; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     Site            578
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q6NXG1.2)"
     Region          629..>657
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     CDS             1..659
                     /gene="ESRP1"
                     /gene_synonym="DFNB109; RBM35A; RMB35A"
                     /coded_by="NM_001122826.2:146..2125"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS47895.1"
                     /db_xref="GeneID:54845"
                     /db_xref="HGNC:HGNC:25966"
                     /db_xref="MIM:612959"
ORIGIN      
        1 mtaspdylvv lfgitagatg aklgsdekel illfwkvvdl ankkvgqlhe vlvrpdqlel
       61 tedckeetki dveslssasq ldqalrqfnq svsnelnigv gtsfclctdg qlhvrqilhp
      121 easkknvllp ecfysffdlr kefkkccpgs pdidkldvat mteylnfeks ssvsrygasq
      181 vedmgniila misepynhrf sdpervnykf esgtcskmel iddntvvrar glpwqssdqd
      241 iarffkglni akggaalcln aqgrrngeal vrfvseehrd lalqrhkhhm gtryievyka
      301 tgedflkiag gtsnevaqfl skenqvivrm rglpftatae evvaffgqhc pitggkegil
      361 fvtypdgrpt gdafvlface eyaqnalrkh kdllgkryie lfrstaaevq qvlnrfssap
      421 liplptppii pvlpqqfvpp tnvrdcirlr glpyaatied ildflgefat dirthgvhmv
      481 lnhqgrpsgd afiqmksadr afmaaqkchk knmkdryvev fqcsaeemnf vlmggtlnrn
      541 glspppclsp psytfpapaa vipteaaiyq psvilnpral qpstayypag tqlfmnytay
      601 ypsppgspns lgyfptaanl sgvppqpgtv vrmqglaynt gvkeilnffq gyqclkdvw
//
LOCUS       NP_001257551             478 aa            linear   PRI 20-NOV-2025
DEFINITION  monocarboxylate transporter 2 [Homo sapiens].
ACCESSION   NP_001257551
VERSION     NP_001257551.1
DBSOURCE    REFSEQ: accession NM_001270622.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Sheng,G., Gao,Y., Wu,H., Liu,Y. and Yang,Y.
  TITLE     Functional heterogeneity of MCT1 and MCT4 in metabolic
            reprogramming affects osteosarcoma growth and metastasis
  JOURNAL   J Orthop Surg Res 18 (1), 131 (2023)
   PUBMED   36814318
  REMARK    GeneRIF: Functional heterogeneity of MCT1 and MCT4 in metabolic
            reprogramming affects osteosarcoma growth and metastasis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Medel,V., Crossley,N., Gajardo,I., Muller,E., Barros,L.F.,
            Shine,J.M. and Sierralta,J.
  TITLE     Whole-brain neuronal MCT2 lactate transporter expression links
            metabolism to human brain structure and function
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2204619119 (2022)
   PUBMED   35939682
  REMARK    GeneRIF: Whole-brain neuronal MCT2 lactate transporter expression
            links metabolism to human brain structure and function.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Kopnick,A.L., Geistlinger,K. and Beitz,E.
  TITLE     Cysteine 159 delineates a hinge region of the alternating access
            monocarboxylate transporter 1 and is targeted by cysteine-modifying
            inhibitors
  JOURNAL   FEBS J 288 (20), 6052-6062 (2021)
   PUBMED   33999492
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Yamaguchi,A., Narumi,K., Furugen,A., Iseki,K. and Kobayashi,M.
  TITLE     Identification of the essential extracellular aspartic acids
            conserved in human monocarboxylate transporters 1, 2, and 4
  JOURNAL   Biochem Biophys Res Commun 529 (4), 1061-1065 (2020)
   PUBMED   32819565
  REMARK    GeneRIF: Identification of the essential extracellular aspartic
            acids conserved in human monocarboxylate transporters 1, 2, and 4.
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Halestrap,A.P. and Meredith,D.
  TITLE     The SLC16 gene family-from monocarboxylate transporters (MCTs) to
            aromatic amino acid transporters and beyond
  JOURNAL   Pflugers Arch 447 (5), 619-628 (2004)
   PUBMED   12739169
  REMARK    Review article
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Fayol,L., Baud,O., Monier,A., Pellerin,L., Magistretti,P.,
            Evrard,P. and Verney,C.
  TITLE     Immunocytochemical expression of monocarboxylate transporters in
            the human visual cortex at midgestation
  JOURNAL   Brain Res Dev Brain Res 148 (1), 69-76 (2004)
   PUBMED   14757520
  REMARK    GeneRIF: MCT2 immunoreactivity was noted in astrocytic cell bodies
            from week 19 and spread subsequently to the astrocyte end-feet in
            contact with blood vessels of visual cortex.
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Fishbein,W.N., Merezhinskaya,N. and Foellmer,J.W.
  TITLE     Relative distribution of three major lactate transporters in frozen
            human tissues and their localization in unfixed skeletal muscle
  JOURNAL   Muscle Nerve 26 (1), 101-112 (2002)
   PUBMED   12115955
REFERENCE   9  (residues 1 to 478)
  AUTHORS   Lin,R.Y., Vera,J.C., Chaganti,R.S. and Golde,D.W.
  TITLE     Human monocarboxylate transporter 2 (MCT2) is a high affinity
            pyruvate transporter
  JOURNAL   J Biol Chem 273 (44), 28959-28965 (1998)
   PUBMED   9786900
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Cori,C.F.
  TITLE     The glucose-lactic acid cycle and gluconeogenesis
  JOURNAL   Curr Top Cell Regul 18, 377-387 (1981)
   PUBMED   7273846
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC119793.3, DR000391.1,
            BC007463.1, BC030693.2, AF058056.1 and AC079905.28.
            
            Summary: This gene is a member of the monocarboxylate transporter
            family. Members in this family transport metabolites, such as
            lactate, pyruvate, and ketone bodies. The protein encoded by this
            gene catalyzes the proton-linked transport of monocarboxylates and
            has the highest affinity for pyruvate. This protein has been
            reported to be more highly expressed in prostate and colorectal
            cancer specimens when compared to control specimens. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2012].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC007463.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..478
                     /product="monocarboxylate transporter 2"
                     /note="solute carrier family 16 (monocarboxylate
                     transporter), member 7; solute carrier family 16, member 7
                     (monocarboxylic acid transporter 2)"
                     /calculated_mol_wt=52069
     Region          15..458
                     /region_name="2A0113"
                     /note="monocarboxylate transporter 1; TIGR00892"
                     /db_xref="CDD:273325"
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            60..80
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            90..110
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            149..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Region          200..224
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            247..267
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            283..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            293
                     /site_type="other"
                     /note="May be protonated during monocarboxylate transport.
                     /evidence=ECO:0000269|PubMed:32415067; propagated from
                     UniProtKB/Swiss-Prot (O60669.2)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            374..394
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Site            407..427
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     Region          437..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60669.2)"
     CDS             1..478
                     /gene="SLC16A7"
                     /gene_synonym="MCT2"
                     /coded_by="NM_001270622.2:318..1754"
                     /db_xref="CCDS:CCDS8961.1"
                     /db_xref="GeneID:9194"
                     /db_xref="HGNC:HGNC:10928"
                     /db_xref="MIM:603654"
ORIGIN      
        1 mppmpsappv hpppdggwgw ivvgaafisi gfsyafpkav tvffkeiqqi fhttyseiaw
       61 issimlavmy aggpvssvlv nkygsrpvvi aggllcclgm vlasfsssvv qlyltmgfit
      121 glglafnlqp altiigkyfy rkrpmangla magspvflss lapfnqylfn tfgwkgsfli
      181 lgslllnacv agslmrplgp nqttsksknk tgkteddssp kkiktkkstw ekvnkyldfs
      241 lfkhrgfliy lsgnvimflg ffapiiflap yakdqgidey saafllsvma fvdmfarpsv
      301 glianskyir priqyffsfa imfngvchll cplaqdytsl vlyavffglg fgsvssvlfe
      361 tlmdlvgapr fssavglvti vecgpvllgp plagklvdlt geykymymsc gaivvaasvw
      421 llignainyr llakerkeen arqktresep lskskhsedv nvkvsnaqsv tseretni
//
LOCUS       NP_001317940            1144 aa            linear   PRI 20-NOV-2025
DEFINITION  intersectin-1 isoform 6 [Homo sapiens].
ACCESSION   NP_001317940 XP_005261088
VERSION     NP_001317940.1
DBSOURCE    REFSEQ: accession NM_001331011.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1144)
  AUTHORS   Lan,C., Zhang,H., Wang,K., Liu,X., Zhao,Y., Guo,Z., Zhang,N.,
            Zhou,Y., Gao,M., Gu,F. and Ma,Y.
  TITLE     The alternative splicing of intersectin 1 regulated by PTBP1
            promotes human glioma progression
  JOURNAL   Cell Death Dis 13 (9), 835 (2022)
   PUBMED   36171198
  REMARK    GeneRIF: The alternative splicing of intersectin 1 regulated by
            PTBP1 promotes human glioma progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1144)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1144)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 1144)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 1144)
  AUTHORS   Sengar,A.S., Wang,W., Bishay,J., Cohen,S. and Egan,S.E.
  TITLE     The EH and SH3 domain Ese proteins regulate endocytosis by linking
            to dynamin and Eps15
  JOURNAL   EMBO J 18 (5), 1159-1171 (1999)
   PUBMED   10064583
REFERENCE   7  (residues 1 to 1144)
  AUTHORS   Yamabhai,M., Hoffman,N.G., Hardison,N.L., McPherson,P.S.,
            Castagnoli,L., Cesareni,G. and Kay,B.K.
  TITLE     Intersectin, a novel adaptor protein with two Eps15 homology and
            five Src homology 3 domains
  JOURNAL   J Biol Chem 273 (47), 31401-31407 (1998)
   PUBMED   9813051
REFERENCE   8  (residues 1 to 1144)
  AUTHORS   Guipponi,M., Scott,H.S., Chen,H., Schebesta,A., Rossier,C. and
            Antonarakis,S.E.
  TITLE     Two isoforms of a human intersectin (ITSN) protein are produced by
            brain-specific alternative splicing in a stop codon
  JOURNAL   Genomics 53 (3), 369-376 (1998)
   PUBMED   9799604
REFERENCE   9  (residues 1 to 1144)
  AUTHORS   Chen,H. and Antonarakis,S.E.
  TITLE     The SH3D1A gene maps to human chromosome 21q22.1-->q22.2
  JOURNAL   Cytogenet Cell Genet 78 (3-4), 213-215 (1997)
   PUBMED   9465890
REFERENCE   10 (residues 1 to 1144)
  AUTHORS   Sparks,A.B., Hoffman,N.G., McConnell,S.J., Fowlkes,D.M. and
            Kay,B.K.
  TITLE     Cloning of ligand targets: systematic isolation of SH3
            domain-containing proteins
  JOURNAL   Nat Biotechnol 14 (6), 741-744 (1996)
   PUBMED   9630982
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC117560.1, AP000312.2 and
            CX163355.1.
            
            On Sep 3, 2016 this sequence version replaced XP_005261088.1.
            
            Summary: The protein encoded by this gene is a cytoplasmic
            membrane-associated protein that indirectly coordinates endocytic
            membrane traffic with the actin assembly machinery. In addition,
            the encoded protein may regulate the formation of clathrin-coated
            vesicles and could be involved in synaptic vesicle recycling. This
            protein has been shown to interact with dynamin, CDC42, SNAP23,
            SNAP25, SPIN90, EPS15, EPN1, EPN2, and STN2. Multiple transcript
            variants encoding different isoforms have been found for this gene,
            but the full-length nature of only two of them have been
            characterized so far. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.22035.1,
                                           SRR1660809.238493.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.11"
     Protein         1..1144
                     /product="intersectin-1 isoform 6"
                     /note="human intersectin-SH3 domain-containing protein
                     SH3P17; Src homology 3 domain-containing protein; SH3
                     domain-containing protein 1A; intersectin 1 (SH3 domain
                     protein)"
                     /calculated_mol_wt=129285
     Region          14..108
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          214..309
                     /region_name="EH"
                     /note="Eps15 homology domain; smart00027"
                     /db_xref="CDD:197477"
     Region          <363..>684
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Region          744..798
                     /region_name="SH3_Intersectin1_1"
                     /note="First Src homology 3 domain (or SH3A) of
                     Intersectin-1; cd11987"
                     /db_xref="CDD:212920"
     Site            order(749,751,754,758,778..779,792,794..795)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212920"
     Region          798..912
                     /region_name="INTAP"
                     /note="Intersectin and clathrin adaptor AP2 binding
                     region; pfam16617"
                     /db_xref="CDD:435467"
     Region          912..963
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(917,919,922,926,943..944,957,959..960)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1001..1062
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(1007,1009,1012,1016,1034..1035,1053,1055..1056)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          1082..1135
                     /region_name="SH3_Intersectin1_5"
                     /note="Fifth Src homology 3 domain (or SH3E) of
                     Intersectin-1; cd11995"
                     /db_xref="CDD:212928"
     Site            order(1088,1090,1093,1097,1115..1116,1129,1131..1132)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212928"
     CDS             1..1144
                     /gene="ITSN1"
                     /gene_synonym="ITSN; SH3D1A; SH3P17"
                     /coded_by="NM_001331011.2:246..3680"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS82665.1"
                     /db_xref="GeneID:6453"
                     /db_xref="HGNC:HGNC:6183"
                     /db_xref="MIM:602442"
ORIGIN      
        1 maqfptpfgg sldiwaitve erakhdqqfh slkpisgfit gdqarnfffq sglpqpvlaq
       61 iwaladmnnd grmdqvefsi amkliklklq gyqlpsalpp vmkqqpvais sapafgmggi
      121 asmppltava pvpmgsipvv gmsptlvssv ptaavpplan gappviqplp afahpaatlp
      181 ksssfsrsgp gsqlntklqk aqsfdvasvp pvaewavpqs srlkyrqlfn shdktmsghl
      241 tgpqartilm qsslpqaqla siwnlsdidq dgkltaeefi lamhlidvam sgqplppvlp
      301 peyippsfrr vrsgsgisvi sstsvdqrlp eepvledeqq qlekklpvtf edkkrenfer
      361 gnlelekrrq alleqqrkeq erlaqlerae qerkererqe qerkrqlele kqlekqrele
      421 rqreeerrke ierreaakre lerqrqlewe rnrrqellnq rnkeqedivv lkakkktlef
      481 elealndkkh qlegklqdir crlttqrqei estnksrelr iaeithlqqq lqesqqmlgr
      541 lipekqilnd qlkqvqqnsl hrdslvtlkr aleakelarq hlrdqldeve ketrsklqei
      601 difnnqlkel reihnkqqlq kqksmeaerl kqkeqerkii elekqkeeaq rraqerdkqw
      661 lehvqqedeh qrprklheee klkreesvkk kdgeekgkqe aqdklgrlfh qhqepakpav
      721 qapwstaekg pltisaqenv kvvyyralyp fesrshdeit iqpgdivmvd esqtgepgwl
      781 ggelkgktgw fpanyaekip enevpapvkp vtdstsapap klalretpap lavtssepst
      841 tpnnwadfss twptstnekp etdnwdawaa qpsltvpsag qlrqrsaftp atatgsspsp
      901 vlgqgekveg lqaqalypwr akkdnhlnfn kndvitvleq qdmwwfgevq gqkgwfpksy
      961 vklisgpirk stsmdsgsse spaslkrvas paakpvvsge eiaqviasyt atgpeqltla
     1021 pgqlilirkk npggwwegel qargkkrqig wfpanyvkll spgtskitpt eppkstalaa
     1081 vcqvigmydy taqnddelaf nkgqiinvln kedpdwwkge vngqvglfps nyvklttdmd
     1141 psqq
//
LOCUS       NP_439892                264 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 2 isoform 2 [Homo sapiens].
ACCESSION   NP_439892
VERSION     NP_439892.2
DBSOURCE    REFSEQ: accession NM_052827.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   Zakaria,M.F., Kato,H., Sonoda,S., Kato,K., Uehara,N.,
            Kyumoto-Nakamura,Y., Sharifa,M.M., Yu,L., Dai,L., Yamaza,H.,
            Kajioka,S., Nishimura,F. and Yamaza,T.
  TITLE     NaV1.1 contributes to the cell cycle of human mesenchymal stem
            cells by regulating AKT and CDK2
  JOURNAL   J Cell Sci 137 (19) (2024)
   PUBMED   39258309
  REMARK    GeneRIF: NaV1.1 contributes to the cell cycle of human mesenchymal
            stem cells by regulating AKT and CDK2.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Ji,Q., Ma,F., Zhang,X., Liu,Y., Wang,P. and Li,M.
  TITLE     Hsa_circ_0005320 affects cell proliferation and the cell cycle via
            the IGF2BP3/CDK2 axis in bladder cancer
  JOURNAL   Cell Signal 119, 111154 (2024)
   PUBMED   38565412
  REMARK    GeneRIF: Hsa_circ_0005320 affects cell proliferation and the cell
            cycle via the IGF2BP3/CDK2 axis in bladder cancer.
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Malumbres,M. and Barbacid,M.
  TITLE     Cell cycle, CDKs and cancer: a changing paradigm
  JOURNAL   Nat Rev Cancer 9 (3), 153-166 (2009)
   PUBMED   19238148
  REMARK    Review article
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Shiffman,D., Brooks,E.E., Brooks,A.R., Chan,C.S. and Milner,P.G.
  TITLE     Characterization of the human cyclin-dependent kinase 2 gene.
            Promoter analysis and gene structure
  JOURNAL   J Biol Chem 271 (21), 12199-12204 (1996)
   PUBMED   8647814
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Koff,A., Giordano,A., Desai,D., Yamashita,K., Harper,J.W.,
            Elledge,S., Nishimoto,T., Morgan,D.O., Franza,B.R. and Roberts,J.M.
  TITLE     Formation and activation of a cyclin E-cdk2 complex during the G1
            phase of the human cell cycle
  JOURNAL   Science 257 (5077), 1689-1694 (1992)
   PUBMED   1388288
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Pagano,M., Pepperkok,R., Verde,F., Ansorge,W. and Draetta,G.
  TITLE     Cyclin A is required at two points in the human cell cycle
  JOURNAL   EMBO J 11 (3), 961-971 (1992)
   PUBMED   1312467
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Ninomiya-Tsuji,J., Nomoto,S., Yasuda,H., Reed,S.I. and Matsumoto,K.
  TITLE     Cloning of a human cDNA encoding a CDC2-related kinase by
            complementation of a budding yeast cdc28 mutation
  JOURNAL   Proc Natl Acad Sci U S A 88 (20), 9006-9010 (1991)
   PUBMED   1717994
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Tsai,L.H., Harlow,E. and Meyerson,M.
  TITLE     Isolation of the human cdk2 gene that encodes the cyclin A- and
            adenovirus E1A-associated p33 kinase
  JOURNAL   Nature 353 (6340), 174-177 (1991)
   PUBMED   1653904
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Elledge,S.J. and Spottswood,M.R.
  TITLE     A new human p34 protein kinase, CDK2, identified by complementation
            of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of
            Xenopus Eg1
  JOURNAL   EMBO J 10 (9), 2653-2659 (1991)
   PUBMED   1714386
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA814453.1, AB012305.1,
            BC003065.2 and AA789250.1.
            
            On Jan 31, 2008 this sequence version replaced NP_439892.1.
            
            Summary: This gene encodes a member of a family of serine/threonine
            protein kinases that participate in cell cycle regulation. The
            encoded protein is the catalytic subunit of the cyclin-dependent
            protein kinase complex, which regulates progression through the
            cell cycle. Activity of this protein is especially critical during
            the G1 to S phase transition. This protein associates with and
            regulated by other subunits of the complex including cyclin A or E,
            CDK inhibitor p21Cip1 (CDKN1A), and p27Kip1 (CDKN1B). Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2014].
            
            Transcript Variant: This variant (2, also known as CDK2deltaT)
            lacks an alternate in-frame exon, compared to variant 1. The
            encoded isoform (2, also known as d-HSCDK2) is shorter than isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.113942.1,
                                           SRR1803615.169026.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..264
                     /product="cyclin-dependent kinase 2 isoform 2"
                     /EC_number="2.7.11.22"
                     /note="cdc2-related protein kinase; p33 protein kinase;
                     cell division protein kinase 2"
                     /calculated_mol_wt=29904
     Region          3..252
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(10..13,16,18,31,33,64,80..83,127,131..132,134,
                     144..145)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..264
                     /gene="CDK2"
                     /gene_synonym="CDKN2; p33(CDK2)"
                     /coded_by="NM_052827.4:180..974"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8899.1"
                     /db_xref="GeneID:1017"
                     /db_xref="HGNC:HGNC:1771"
                     /db_xref="MIM:116953"
ORIGIN      
        1 menfqkveki gegtygvvyk arnkltgevv alkkirldte tegvpstair eisllkelnh
       61 pnivklldvi htenklylvf eflhqdlkkf mdasaltgip lpliksylfq llqglafchs
      121 hrvlhrdlkp qnllintega ikladfglar afgvpvrtyt hevtrralfp gdseidqlfr
      181 ifrtlgtpde vvwpgvtsmp dykpsfpkwa rqdfskvvpp ldedgrslls qmlhydpnkr
      241 isakaalahp ffqdvtkpvp hlrl
//
LOCUS       NP_004930                740 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-dependent RNA helicase DDX1 [Homo sapiens].
ACCESSION   NP_004930
VERSION     NP_004930.1
DBSOURCE    REFSEQ: accession NM_004939.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 740)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 740)
  AUTHORS   Liu,J., Yang,T., Luo,Y., Ma,Z., Yu,Z., Zhang,L., Liu,G., Wen,J.,
            Lu,G., Zhang,G., Zhao,Y., Luo,W., Li,Y., Yang,N., Zhou,J., Lu,Y.,
            Chen,S. and Zeng,X.
  TITLE     DEAD-box helicase 1 inhibited CD8+ T cell antitumor activity by
            inducing PD-L1 expression in hepatocellular carcinoma
  JOURNAL   Cancer Sci 115 (3), 763-776 (2024)
   PUBMED   38243657
  REMARK    GeneRIF: DEAD-box helicase 1 inhibited CD8[+] T cell antitumor
            activity by inducing PD-L1 expression in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 740)
  AUTHORS   Garg,M., Li,L. and Godbout,R.
  TITLE     Role of DDX1 in the oxidative response of ataxia telangiectasia
            patient-derived fibroblasts
  JOURNAL   Redox Biol 69, 102988 (2024)
   PUBMED   38096740
  REMARK    GeneRIF: Role of DDX1 in the oxidative response of ataxia
            telangiectasia patient-derived fibroblasts.
REFERENCE   4  (residues 1 to 740)
  AUTHORS   Sharma,M., Mason,A.C., Dawson,T.R. and Wente,S.R.
  TITLE     Phosphorylation impacts GLE1 nuclear localization and association
            with DDX1
  JOURNAL   Adv Biol Regul 90, 100990 (2023)
   PUBMED   37801910
  REMARK    GeneRIF: Phosphorylation impacts GLE1 nuclear localization and
            association with DDX1.
REFERENCE   5  (residues 1 to 740)
  AUTHORS   Cao,L., Hui,X., Xu,T., Mao,H., Lin,X., Huang,K., Zhao,L. and Jin,M.
  TITLE     The RNA-Splicing Ligase RTCB Promotes Influenza A Virus Replication
            by Suppressing Innate Immunity via Interaction with RNA Helicase
            DDX1
  JOURNAL   J Immunol 211 (6), 1020-1031 (2023)
   PUBMED   37556111
  REMARK    GeneRIF: The RNA-Splicing Ligase RTCB Promotes Influenza A Virus
            Replication by Suppressing Innate Immunity via Interaction with RNA
            Helicase DDX1.
REFERENCE   6  (residues 1 to 740)
  AUTHORS   Golembowski,S., Gellrich,S., von Zimmermann,M., Rutz,S.,
            Lippert,S., Audring,H., Lorenz,P., Sterry,W. and Jahn,S.
  TITLE     Clonal evolution in a primary cutaneous follicle center B cell
            lymphoma revealed by single cell analysis in sequential biopsies
  JOURNAL   Immunobiology 201 (5), 631-644 (2000)
   PUBMED   10834319
REFERENCE   7  (residues 1 to 740)
  AUTHORS   Akiyama,K., Akao,Y., Yokoyama,M., Nakagawa,Y., Noguchi,T., Yagi,K.
            and Nishi,Y.
  TITLE     Expression of two dead box genes (DDX1 and DDX6) is independent of
            that of MYCN in human neuroblastoma cell lines
  JOURNAL   Biochem Mol Biol Int 47 (4), 563-568 (1999)
   PUBMED   10319407
REFERENCE   8  (residues 1 to 740)
  AUTHORS   Kitajima,Y., Yatsuki,H., Zhang,R., Matsuhashi,S. and Hori,K.
  TITLE     A novel human homologue of a dead-box RNA helicase family
  JOURNAL   Biochem Biophys Res Commun 199 (2), 748-754 (1994)
   PUBMED   8135819
REFERENCE   9  (residues 1 to 740)
  AUTHORS   Godbout,R. and Squire,J.
  TITLE     Amplification of a DEAD box protein gene in retinoblastoma cell
            lines
  JOURNAL   Proc Natl Acad Sci U S A 90 (16), 7578-7582 (1993)
   PUBMED   7689221
REFERENCE   10 (residues 1 to 740)
  AUTHORS   Schmid,S.R. and Linder,P.
  TITLE     D-E-A-D protein family of putative RNA helicases
  JOURNAL   Mol Microbiol 6 (3), 283-291 (1992)
   PUBMED   1552844
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X70649.1 and BC053673.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein
            that acts as an ATP-dependent RNA helicase that has been found to
            promote coronaviruses replication. [provided by RefSeq, Aug 2021].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X70649.1, SRR1803614.49929.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in SARS-CoV-2 infection
            MANE Ensembl match     :: ENST00000233084.8/ ENSP00000233084.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..740
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p24.3"
     Protein         1..740
                     /product="ATP-dependent RNA helicase DDX1"
                     /EC_number="3.6.4.13"
                     /note="DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 1;
                     DEAD box-1; DEAD (Asp-Glu-Ala-Asp) box helicase 1; DEAD
                     box polypeptide 1; DEAD box protein 1; DEAD box protein
                     retinoblastoma; DEAD (Asp-Glu-Ala-Asp) box polypeptide 1;
                     DEAD/H-box helicase 1; DEAD-box RNA helicase DDX1"
                     /calculated_mol_wt=82301
     Region          1..525
                     /region_name="Necessary for interaction with RELA.
                     /evidence=ECO:0000269|PubMed:19058135"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Region          1..448
                     /region_name="Interaction with dsRNA.
                     /evidence=ECO:0000250|UniProtKB:Q91VR5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Region          1..295
                     /region_name="Necessary for interaction with HNRNPK.
                     /evidence=ECO:0000269|PubMed:12183465"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Region          4..>64
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Site            48..54
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:350670"
     Region          93..245
                     /region_name="SPRY_DDX1"
                     /note="SPRY domain associated with DEAD box gene DDX1;
                     cd12873"
                     /db_xref="CDD:293933"
     Site            239
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92499.2)"
     Site            268
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92499.2)"
     Site            281
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92499.2)"
     Region          284..625
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Region          370..373
                     /region_name="DEAD box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Region          525..740
                     /region_name="Necessary for interaction with HNRNPK.
                     /evidence=ECO:0000269|PubMed:12183465"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     Region          536..631
                     /region_name="Necessary for interaction with replicase
                     polyprotein 1ab nsp14 of IBV.
                     /evidence=ECO:0000269|PubMed:20573827"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92499.2)"
     CDS             1..740
                     /gene="DDX1"
                     /gene_synonym="DBP-RB; UKVH5d"
                     /coded_by="NM_004939.3:67..2289"
                     /db_xref="CCDS:CCDS1686.1"
                     /db_xref="GeneID:1653"
                     /db_xref="HGNC:HGNC:2734"
                     /db_xref="MIM:601257"
ORIGIN      
        1 maafsemgvm peiaqaveem dwllptdiqa esiplilggg dvlmaaetgs gktgafsipv
       61 iqivyetlkd qqegkkgktt iktgasvlnk wqmnpydrgs afaigsdglc cqsrevkewh
      121 gcratkglmk gkhyyevsch dqglcrvgws tmqasldlgt dkfgfgfggt gkkshnkqfd
      181 nygeeftmhd tigcyldidk ghvkfskngk dlglafeipp hmknqalfpa cvlknaelkf
      241 nfgeeefkfp pkdgfvalsk apdgyivksq hsgnaqvtqt kflpnapkal ivepsrelae
      301 qtlnnikqfk kyidnpklre lliiggvaar dqlsvlengv divvgtpgrl ddlvstgkln
      361 lsqvrflvld eadgllsqgy sdfinrmhnq ipqvtsdgkr lqvivcsatl hsfdvkklse
      421 kimhfptwvd lkgedsvpdt vhhvvvpvnp ktdrlwerlg kshirtddvh akdntrpgan
      481 spemwseaik ilkgeyavra ikehkmdqai ifcrtkidcd nleqyfiqqg ggpdkkghqf
      541 scvclhgdrk pherkqnler fkkgdvrfli ctdvaargid ihgvpyvinv tlpdekqnyv
      601 hrigrvgrae rmglaislva tekekvwyhv cssrgkgcyn trlkedggct iwynemqlls
      661 eieehlncti sqvepdikvp vdefdgkvty gqkraagggs ykghvdilap tvqelaalek
      721 eaqtsflhlg ylpnqlfrtf
//
LOCUS       NP_001243898             302 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial potassium channel isoform 2 [Homo sapiens].
ACCESSION   NP_001243898
VERSION     NP_001243898.1
DBSOURCE    REFSEQ: accession NM_001256969.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Paggio,A., Checchetto,V., Campo,A., Menabo,R., Di Marco,G., Di
            Lisa,F., Szabo,I., Rizzuto,R. and De Stefani,D.
  TITLE     Identification of an ATP-sensitive potassium channel in
            mitochondria
  JOURNAL   Nature 572 (7771), 609-613 (2019)
   PUBMED   31435016
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Wang,C. and Brennan,W.A. Jr.
  TITLE     Rat skeletal muscle, liver and brain have different fetal and adult
            forms of the glucose transporter
  JOURNAL   Biochim Biophys Acta 946 (1), 11-18 (1988)
   PUBMED   3145016
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP307614.1, BQ427785.1, AC134772.2 and BC011993.1.
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            initiates translation at a downstream, in-frame start codon,
            compared to variant 1. Variants 3, 4, 5, 6 and 7 encode the same
            isoform (2), which has a shorter N-terminus compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.71192.1, BQ427785.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154125, SAMEA2158800
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..302
                     /product="mitochondrial potassium channel isoform 2"
                     /note="coiled-coil domain-containing protein 51;
                     mitochondrial potassium channel"
                     /calculated_mol_wt=33526
     CDS             1..302
                     /gene="CCDC51"
                     /gene_synonym="MITOK"
                     /coded_by="NM_001256969.3:234..1142"
                     /note="isoform 2 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS58830.1"
                     /db_xref="GeneID:79714"
                     /db_xref="HGNC:HGNC:25714"
                     /db_xref="MIM:618585"
ORIGIN      
        1 mvarglvrea redlevhqak lkevrdrldr vsredsqyle latlehrmlq eekrlrtayl
       61 raedserekf slfsaavres hekertraer tknwsligsv lgaligvags tyvnrvrlqe
      121 lkallleaqk gpvslqeair eqassysrqq rdlhnlmvdl rglvhaagpg qdsgsqagsp
      181 ptrdrdvdvl saalkeqlsh srqvhscleg lreqldglek tcsqmagvvq lvksaahpgl
      241 vepadgamps flleqgsmil alsdteqrle aqvnrntiys tlvtcvtfva tlpvlymlfk
      301 as
//
LOCUS       NP_055493                932 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            3 [Homo sapiens].
ACCESSION   NP_055493 XP_947633 XP_951179 XP_951181 XP_951183 XP_951184
            XP_951185 XP_951187 XP_951188
VERSION     NP_055493.2
DBSOURCE    REFSEQ: accession NM_014678.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 932)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 932)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 932)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 932)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 932)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 932)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 932)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 932)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 932)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 932)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, DB452735.1,
            BC006568.2, AL096767.14 and BC000976.4.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947633.1, XP_951179.1, XP_951181.1, XP_951183.1, XP_951184.1,
            XP_951185.1, XP_951187.1, XP_951188.1, NP_055493.1.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Transcript Variant: This variant (3) lacks an exon in the coding
            region but maintains the reading frame, compared to variant 1. The
            encoded isoform (3) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.212550.1,
                                           SRR1660809.88030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..932
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..932
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 3"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=101115
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          <676..927
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..932
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_014678.5:372..3170"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS33681.1"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlafsdyq
      541 iqqmtanfvd qfgfndeefa dqddninapf driaeinfni dadedspsaa lfeaccsdri
      601 qpfdddeded iwedsdtrca arvmarprfg aphasescsk ngperggqdg kasleahrda
      661 pgagappapg kkeappvegd segamwtavf depanstpta pgvvrdvgss vwaagtsape
      721 ekgwakftdf qpfccsesgp rcsspvdtec shaegsrsqg pekafspasp cawnvcvtrk
      781 apllasdsss sggshsedgd qkaasamdav srgpgreapp lptvarteea vgrvgcadsr
      841 llspacpapk evtaapavav ppeatvaitt alskagpaip tpavssalav avplgpimav
      901 taapamvatl gtvtkdgktd appegaalng pv
//
LOCUS       NP_001336661             538 aa            linear   PRI 20-NOV-2025
DEFINITION  PWWP domain-containing protein 2A isoform d [Homo sapiens].
ACCESSION   NP_001336661 XP_016864498
VERSION     NP_001336661.1
DBSOURCE    REFSEQ: accession NM_001349732.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Hong,H., Sun,Y., Deng,H., Yuan,K., Chen,J., Liu,W. and Cui,Z.
  TITLE     Dysregulation of cPWWP2A-miR-579 axis mediates
            dexamethasone-induced cytotoxicity in human osteoblasts
  JOURNAL   Biochem Biophys Res Commun 517 (3), 491-498 (2019)
   PUBMED   31376935
  REMARK    GeneRIF: It has been shown that dysregulation of the circular RNA
            PWWP2A-miR-579 axis is involved in dexamethasone-induced
            cytotoxicity in human osteoblasts.
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Zhang,T., Wei,G., Millard,C.J., Fischer,R., Konietzny,R.,
            Kessler,B.M., Schwabe,J.W.R. and Brockdorff,N.
  TITLE     A variant NuRD complex containing PWWP2A/B excludes MBD2/3 to
            regulate transcription at active genes
  JOURNAL   Nat Commun 9 (1), 3798 (2018)
   PUBMED   30228260
  REMARK    GeneRIF: Study in HeLa, HEK293F, and mouse embryonic stem cells
            reveal that loss of PWWP2A/B leads to increases in histone
            acetylation predominantly at highly expressed genes, accompanied by
            decreases in Pol II elongation. Collectively, these findings
            suggest a role for PWWP2A/B in regulating transcription through the
            fine-tuning of histone acetylation dynamics at actively transcribed
            genes.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Punzeler,S., Link,S., Wagner,G., Keilhauer,E.C., Kronbeck,N.,
            Spitzer,R.M., Leidescher,S., Markaki,Y., Mentele,E., Regnard,C.,
            Schneider,K., Takahashi,D., Kusakabe,M., Vardabasso,C., Zink,L.M.,
            Straub,T., Bernstein,E., Harata,M., Leonhardt,H., Mann,M.,
            Rupp,R.A. and Hake,S.B.
  TITLE     Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural
            crest differentiation
  JOURNAL   EMBO J 36 (15), 2263-2279 (2017)
   PUBMED   28645917
  REMARK    GeneRIF: Thus, PWWP2A is a novel H2A.Z-specific multivalent
            chromatin binder providing a surprising link between H2A.Z,
            chromosome segregation, and organ development.
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008706.5, DB450981.1, BC105110.1, AI288438.1, AK055921.1,
            AI972512.1 and BC018680.1.
            
            On Mar 24, 2017 this sequence version replaced XP_016864498.1.
            
            Transcript Variant: This variant (4) differs in its 5' UTR, and its
            3' terminal exon extends past a splice site that is used in variant
            1. These differences cause translation initiation at a downstream
            start codon and results in a novel 3' coding region and 3' UTR,
            compared to variant 1. The encoded isoform (d) has a shorter
            N-terminus and distinct C-terminus, compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.190815.1,
                                           DRR138512.140303.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..538
                     /product="PWWP domain-containing protein 2A isoform d"
                     /note="PWWP domain-containing protein 2A; MSTP101"
                     /calculated_mol_wt=59732
     Region          417..538
                     /region_name="PWWP_PWWP2A"
                     /note="PWWP domain found in PWWP domain-containing protein
                     2A (PWWP2A); cd20152"
                     /db_xref="CDD:438980"
     Site            order(449,452,478)
                     /site_type="other"
                     /note="putative methyl-histone binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438980"
     Site            450..453
                     /site_type="other"
                     /note="PWWP sequence motif"
                     /db_xref="CDD:438980"
     CDS             1..538
                     /gene="PWWP2A"
                     /gene_synonym="MST101"
                     /coded_by="NM_001349732.2:2021..3637"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:114825"
                     /db_xref="HGNC:HGNC:29406"
                     /db_xref="MIM:617823"
ORIGIN      
        1 mplqsntfqe gtevkceang avpddpspvp hpelslaesl wtskppplfh egapyppplf
       61 irdtynqsip qppprkikrp krkmyreept simnaiklrp rqvlcdkckn svvaekkeir
      121 kgssatdssk yedkkrrnes vttvnkklkt dhkvdgknqn esqkrnavvk vsniahsrgr
      181 vvkvsaqant skaqlstkkv lqsknmdhak arevlkiake kaqkkqnets tsknahskvh
      241 ftrryqnpss gslpprvrlk pqryrneend sslktglekm rsgkmapkpq srctstrsag
      301 eapsenqsps kgpeeassev qdtnevhvpg dqdepqtlgk kgsknnisvy mtlnqkksds
      361 ssasvcsids tddlkssnse csssesfdfp pgsmhapsts stsssskeek klsnslkmkv
      421 fsknvskcvt pdgrticvgd ivwakiygfp wwpariltit vsrkdngllv rqeariswfg
      481 spttsflals qlspflenfq srfnkkrkgl yrkaiteaak aakqltpevr alltqfet
//
LOCUS       NP_872317                224 aa            linear   PRI 20-NOV-2025
DEFINITION  cerebellin-2 precursor [Homo sapiens].
ACCESSION   NP_872317
VERSION     NP_872317.1
DBSOURCE    REFSEQ: accession NM_182511.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Shibata,M., Pattabiraman,K., Muchnik,S.K., Kaur,N., Morozov,Y.M.,
            Cheng,X., Waxman,S.G. and Sestan,N.
  TITLE     Hominini-specific regulation of CBLN2 increases prefrontal
            spinogenesis
  JOURNAL   Nature 598 (7881), 489-494 (2021)
   PUBMED   34599306
  REMARK    GeneRIF: Hominini-specific regulation of CBLN2 increases prefrontal
            spinogenesis.
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Dai,J., Patzke,C., Liakath-Ali,K., Seigneur,E. and Sudhof,T.C.
  TITLE     GluD1 is a signal transduction device disguised as an ionotropic
            receptor
  JOURNAL   Nature 595 (7866), 261-265 (2021)
   PUBMED   34135511
  REMARK    Erratum:[Nature. 2025 Jun;642(8069):E27. doi:
            10.1038/s41586-025-09146-0. PMID: 40481306]
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Huang,C., Yang,J., Li,M.T., Wang,Q., Zhao,J.L., Yang,X.X., Tian,Z.,
            Liu,Y.T., Guo,X.X., Wang,H., Lai,J.Z., Xing,Y.J. and Zeng,X.F.
  TITLE     CBLN2 rs2217560 was Associated with Pulmonary Arterial Hypertension
            in Systemic Lupus Erythematosus
  JOURNAL   Chin Med J (Engl) 131 (24), 3020-3021 (2018)
   PUBMED   30539924
  REMARK    GeneRIF: an important role of CBLN2 in PAH onset despite different
            etiologies
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Germain,M., Eyries,M., Montani,D., Poirier,O., Girerd,B.,
            Dorfmuller,P., Coulet,F., Nadaud,S., Maugenre,S., Guignabert,C.,
            Carpentier,W., Vonk-Noordegraaf,A., Levy,M., Chaouat,A.,
            Lambert,J.C., Bertrand,M., Dupuy,A.M., Letenneur,L., Lathrop,M.,
            Amouyel,P., de Ravel,T.J., Delcroix,M., Austin,E.D., Robbins,I.M.,
            Hemnes,A.R., Loyd,J.E., Berman-Rosenzweig,E., Barst,R.J.,
            Chung,W.K., Simonneau,G., Tregouet,D.A., Humbert,M. and Soubrier,F.
  TITLE     Genome-wide association analysis identifies a susceptibility locus
            for pulmonary arterial hypertension
  JOURNAL   Nat Genet 45 (5), 518-521 (2013)
   PUBMED   23502781
  REMARK    GeneRIF: Single nucleotide polymorphisms in CBLN2 gene is
            associated with pulmonary arterial hypertension.
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Krintel,S.B., Palermo,G., Johansen,J.S., Germer,S., Essioux,L.,
            Benayed,R., Badi,L., Ostergaard,M. and Hetland,M.L.
  TITLE     Investigation of single nucleotide polymorphisms and biological
            pathways associated with response to TNFalpha inhibitors in
            patients with rheumatoid arthritis
  JOURNAL   Pharmacogenet Genomics 22 (8), 577-589 (2012)
   PUBMED   22569225
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Rong,Y., Wei,P., Parris,J., Guo,H., Pattarini,R., Correia,K.,
            Li,L., Kusnoor,S.V., Deutch,A.Y. and Morgan,J.I.
  TITLE     Comparison of Cbln1 and Cbln2 functions using transgenic and
            knockout mice
  JOURNAL   J Neurochem 120 (4), 528-540 (2012)
   PUBMED   22117778
  REMARK    GeneRIF: Transgenic Cbln2 can exhibit functional redundancy with
            Cbln1 in the cerebellum, but it does not have the same properties
            as Cbln1 in thalamic neurons.
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Baranzini,S.E., Wang,J., Gibson,R.A., Galwey,N., Naegelin,Y.,
            Barkhof,F., Radue,E.W., Lindberg,R.L., Uitdehaag,B.M.,
            Johnson,M.R., Angelakopoulou,A., Hall,L., Richardson,J.C.,
            Prinjha,R.K., Gass,A., Geurts,J.J., Kragt,J., Sombekke,M.,
            Vrenken,H., Qualley,P., Lincoln,R.R., Gomez,R., Caillier,S.J.,
            George,M.F., Mousavi,H., Guerrero,R., Okuda,D.T., Cree,B.A.,
            Green,A.J., Waubant,E., Goodin,D.S., Pelletier,D., Matthews,P.M.,
            Hauser,S.L., Kappos,L., Polman,C.H. and Oksenberg,J.R.
  TITLE     Genome-wide association analysis of susceptibility and clinical
            phenotype in multiple sclerosis
  JOURNAL   Hum Mol Genet 18 (4), 767-778 (2009)
   PUBMED   19010793
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Kavety,B., Jenkins,N.A., Fletcher,C.F., Copeland,N.G. and
            Morgan,J.I.
  TITLE     Genomic structure and mapping of precerebellin and a
            precerebellin-related gene
  JOURNAL   Brain Res Mol Brain Res 27 (1), 152-156 (1994)
   PUBMED   7877445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX409761.1, AY359074.1 and BC110843.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY359074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269503.9/ ENSP00000269503.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q22.3"
     Protein         1..224
                     /product="cerebellin-2 precursor"
                     /note="cerebellin-2"
                     /calculated_mol_wt=18918
     sig_peptide     1..51
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5184
     mat_peptide     52..224
                     /product="Cerebellin-2. /id=PRO_0000003551"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IUK8.1)"
                     /calculated_mol_wt=18918
     Site            53
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8IUK8.1)"
     Region          86..224
                     /region_name="C1q"
                     /note="C1q domain; cl23878"
                     /db_xref="CDD:420072"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q8IUK8.1)"
     CDS             1..224
                     /gene="CBLN2"
                     /coded_by="NM_182511.4:578..1252"
                     /db_xref="CCDS:CCDS11999.1"
                     /db_xref="GeneID:147381"
                     /db_xref="HGNC:HGNC:1544"
                     /db_xref="MIM:600433"
ORIGIN      
        1 mqapgrgplg lrlmmpgrrg alrepggcgs clgvalalll lllpaccpvr aqndtepivl
       61 egkclvvcds spsadgavts slgisvrsgs akvafsatrs tnhepsemsn rtmtiyfdqv
      121 lvnignhfdl assifvaprk giysfsfhvv kvynrqtiqv slmqngypvi safagdqdvt
      181 reaasngvll lmeredkvhl klergnlmgg wkystfsgfl vfpl
//
LOCUS       NP_079541                465 aa            linear   PRI 20-NOV-2025
DEFINITION  tRNA-splicing endonuclease subunit Sen2 isoform 1 [Homo sapiens].
ACCESSION   NP_079541
VERSION     NP_079541.1
DBSOURCE    REFSEQ: accession NM_025265.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 465)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 465)
  AUTHORS   Canpolat,N., Liu,D., Atayar,E., Saygili,S., Kara,N.S.,
            Westfall,T.A., Ding,Q., Brown,B.J., Braun,T.A., Slusarski,D., Karli
            Oguz,K., Ozluk,Y., Tuysuz,B., Tastemel Ozturk,T., Sever,L.,
            Sezerman,O.U., Topaloglu,R., Caliskan,S., Attanasio,M. and
            Ozaltin,F.
  TITLE     A splice site mutation in the TSEN2 causes a new syndrome with
            craniofacial and central nervous system malformations, and atypical
            hemolytic uremic syndrome
  JOURNAL   Clin Genet 101 (3), 346-358 (2022)
   PUBMED   34964109
  REMARK    GeneRIF: A splice site mutation in the TSEN2 causes a new syndrome
            with craniofacial and central nervous system malformations, and
            atypical hemolytic uremic syndrome.
REFERENCE   3  (residues 1 to 465)
  AUTHORS   Sekulovski,S., Devant,P., Panizza,S., Gogakos,T., Pitiriciu,A.,
            Heitmeier,K., Ramsay,E.P., Barth,M., Schmidt,C., Tuschl,T.,
            Baas,F., Weitzer,S., Martinez,J. and Trowitzsch,S.
  TITLE     Assembly defects of human tRNA splicing endonuclease contribute to
            impaired pre-tRNA processing in pontocerebellar hypoplasia
  JOURNAL   Nat Commun 12 (1), 5610 (2021)
   PUBMED   34584079
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 465)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 465)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 465)
  AUTHORS   Weitzer,S. and Martinez,J.
  TITLE     The human RNA kinase hClp1 is active on 3' transfer RNA exons and
            short interfering RNAs
  JOURNAL   Nature 447 (7141), 222-226 (2007)
   PUBMED   17495927
REFERENCE   7  (residues 1 to 465)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 465)
  AUTHORS   Paushkin,S.V., Patel,M., Furia,B.S., Peltz,S.W. and Trotta,C.R.
  TITLE     Identification of a human endonuclease complex reveals a link
            between tRNA splicing and pre-mRNA 3' end formation
  JOURNAL   Cell 117 (3), 311-321 (2004)
   PUBMED   15109492
REFERENCE   9  (residues 1 to 465)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 465)
  AUTHORS   van Dijk,T. and Baas,F.
  TITLE     TSEN54 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090947.2, BC019582.1,
            BM671402.1 and AC018500.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of the subunits of the tRNA splicing
            endonuclease. This endonuclease catalyzes the first step in RNA
            splicing which is the removal of introns. Mutations in this gene
            have been associated with pontocerebellar hypoplasia type 2. A
            pseudogene has been identified on chromosome 4. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Feb 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1, 2 and 6 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.134131.1,
                                           SRR1660809.209832.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284995.11/ ENSP00000284995.6
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..465
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.2"
     Protein         1..465
                     /product="tRNA-splicing endonuclease subunit Sen2 isoform
                     1"
                     /EC_number="4.6.1.16"
                     /note="tRNA-splicing endonuclease subunit Sen2; hsSen2;
                     tRNA-intron endonuclease Sen2; TSEN2 tRNA splicing
                     endonuclease subunit"
                     /calculated_mol_wt=53116
     Region          157..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Region          <283..329
                     /region_name="tRNA_int_endo_N"
                     /note="tRNA intron endonuclease, N-terminal domain;
                     pfam02778"
                     /db_xref="CDD:397071"
     Region          339..430
                     /region_name="tRNA-intron_lyase_C"
                     /note="catalytic C-terminal domain of the tRNA-intron
                     lyase; cd22363"
                     /db_xref="CDD:411767"
     Site            order(369,377,416)
                     /site_type="active"
                     /db_xref="CDD:411767"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Site            411
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     Site            415
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6P7W5; propagated from
                     UniProtKB/Swiss-Prot (Q8NCE0.2)"
     CDS             1..465
                     /gene="TSEN2"
                     /gene_synonym="PCH2B; SEN2; SEN2L"
                     /coded_by="NM_025265.4:419..1816"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2611.1"
                     /db_xref="GeneID:80746"
                     /db_xref="HGNC:HGNC:28422"
                     /db_xref="MIM:608753"
ORIGIN      
        1 maeavfhapk rkrrvyetye splpipfgqd hgplkefkif raeminnnvi vrnaedieql
       61 ygkgyfgkgi lsrsrpsfti sdpklvakwk dmktnmpiit skryqhsvew aaelmrrqgq
      121 destvrrilk dytkplehpp vkrneeaqvh dklnsgmvsn megtaggerp svvngdsgks
      181 ggvgdprepl gclqegsgch pttesfeksv redasplphv ccckqdalil qrglhhedgs
      241 qhigllhpgd rgpdheyvlv eeaecamser eaapneelvq rnrlicrrnp yrifeylqls
      301 leeafflvya lgclsiyyek epltivklwk aftvvqptfr ttymayhyfr skgwvpkvgl
      361 kygtdlllyr kgppfyhasy sviielvddh fegslrrpls wkslaalsrv svnvskelml
      421 cylikpstmt dkemespecm krikvqevil srwvssrers dqddl
//
LOCUS       NP_003136                183 aa            linear   PRI 20-NOV-2025
DEFINITION  translocon-associated protein subunit beta precursor [Homo
            sapiens].
ACCESSION   NP_003136 XP_946862 XP_950520 XP_950521 XP_950523
VERSION     NP_003136.1
DBSOURCE    REFSEQ: accession NM_003145.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Gemmer,M., Chaillet,M.L., van Loenhout,J., Cuevas Arenas,R.,
            Vismpas,D., Grollers-Mulderij,M., Koh,F.A., Albanese,P.,
            Scheltema,R.A., Howes,S.C., Kotecha,A., Fedry,J. and Forster,F.
  TITLE     Visualization of translation and protein biogenesis at the ER
            membrane
  JOURNAL   Nature 614 (7946), 160-167 (2023)
   PUBMED   36697828
REFERENCE   2  (residues 1 to 183)
  AUTHORS   Kriegler,T., Kiburg,G. and Hessa,T.
  TITLE     Translocon-Associated Protein Complex (TRAP) is Crucial for
            Co-Translational Translocation of Pre-Proinsulin
  JOURNAL   J Mol Biol 432 (24), 166694 (2020)
   PUBMED   33137310
  REMARK    GeneRIF: Translocon-Associated Protein Complex (TRAP) is Crucial
            for Co-Translational Translocation of Pre-Proinsulin.
REFERENCE   3  (residues 1 to 183)
  AUTHORS   Garg,B., Pathria,G., Wagner,C., Maurer,M. and Wagner,S.N.
  TITLE     Signal Sequence Receptor 2 is required for survival of human
            melanoma cells as part of an unfolded protein response to
            endoplasmic reticulum stress
  JOURNAL   Mutagenesis 31 (5), 573-582 (2016)
   PUBMED   27180333
  REMARK    GeneRIF: The Unfolded Protein Response (UPR) to ER stress was shown
            as an inducer of SSR2 via transcriptional regulation through X-Box
            Binding Protein 1s (XBP1s).
REFERENCE   4  (residues 1 to 183)
  AUTHORS   Ishikawa,H. and Barber,G.N.
  TITLE     STING is an endoplasmic reticulum adaptor that facilitates innate
            immune signalling
  JOURNAL   Nature 455 (7213), 674-678 (2008)
   PUBMED   18724357
  REMARK    Erratum:[Nature. 2008 Nov 13;456(7219):274]
REFERENCE   5  (residues 1 to 183)
  AUTHORS   Sikorska,M., Sandhu,J.K., Deb-Rinker,P., Jezierski,A., Leblanc,J.,
            Charlebois,C., Ribecco-Lutkiewicz,M., Bani-Yaghoub,M. and
            Walker,P.R.
  TITLE     Epigenetic modifications of SOX2 enhancers, SRR1 and SRR2,
            correlate with in vitro neural differentiation
  JOURNAL   J Neurosci Res 86 (8), 1680-1693 (2008)
   PUBMED   18293417
REFERENCE   6  (residues 1 to 183)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   7  (residues 1 to 183)
  AUTHORS   Chinen,K., Sudo,K., Takahashi,E. and Nakamura,Y.
  TITLE     Isolation and mapping of the human beta-signal sequence receptor
            gene (SSR2)
  JOURNAL   Cytogenet Cell Genet 70 (3-4), 215-217 (1995)
   PUBMED   7789174
REFERENCE   8  (residues 1 to 183)
  AUTHORS   Bodescot,M. and Brison,O.
  TITLE     Cloning and sequence analysis of the beta subunit of the human
            translocon-associated protein
  JOURNAL   Biochim Biophys Acta 1217 (1), 101-102 (1994)
   PUBMED   8286409
REFERENCE   9  (residues 1 to 183)
  AUTHORS   Hartmann,E., Gorlich,D., Kostka,S., Otto,A., Kraft,R., Knespel,S.,
            Burger,E., Rapoport,T.A. and Prehn,S.
  TITLE     A tetrameric complex of membrane proteins in the endoplasmic
            reticulum
  JOURNAL   Eur J Biochem 214 (2), 375-381 (1993)
   PUBMED   7916687
REFERENCE   10 (residues 1 to 183)
  AUTHORS   Tajima,S., Lauffer,L., Rath,V.L. and Walter,P.
  TITLE     The signal recognition particle receptor is a complex that contains
            two distinct polypeptide chains
  JOURNAL   J Cell Biol 103 (4), 1167-1178 (1986)
   PUBMED   3021779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP196192.1, X74104.1 and
            AK222600.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_950520.1, XP_950521.1, XP_950523.1, XP_946862.1.
            
            Summary: The signal sequence receptor (SSR) is a glycosylated
            endoplasmic reticulum (ER) membrane receptor associated with
            protein translocation across the ER membrane. The SSR consists of 2
            subunits, a 34-kD glycoprotein (alpha-SSR or SSR1) and a 22-kD
            glycoprotein (beta-SSR or SSR2). The human beta-signal sequence
            receptor gene (SSR2) maps to chromosome bands 1q21-q23. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.19014.1,
                                           SRR5189667.257487.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal
            MANE Ensembl match               :: ENST00000295702.9/
                                                ENSP00000295702.4
            RefSeq Select criteria           :: based on single protein-coding
                                                transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..183
                     /product="translocon-associated protein subunit beta
                     precursor"
                     /note="translocon-associated protein beta;
                     translocon-associated protein subunit beta; SSR-beta;
                     signal sequence receptor subunit beta; signal sequence
                     receptor, beta (translocon-associated protein beta)"
                     /calculated_mol_wt=18274
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1879
     Region          4..179
                     /region_name="TRAP_beta"
                     /note="Translocon-associated protein beta (TRAPB);
                     pfam05753"
                     /db_xref="CDD:399046"
     mat_peptide     18..183
                     /product="Translocon-associated protein subunit beta.
                     /id=PRO_0000033290"
                     /note="propagated from UniProtKB/Swiss-Prot (P43308.1)"
                     /calculated_mol_wt=18274
     Site            88
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43308.1)"
     Site            104
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P43308.1)"
     Site            150..169
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P43308.1)"
     CDS             1..183
                     /gene="SSR2"
                     /gene_synonym="HSD25; TLAP; TRAP-BETA; TRAPB"
                     /coded_by="NM_003145.4:65..616"
                     /db_xref="CCDS:CCDS1126.1"
                     /db_xref="GeneID:6746"
                     /db_xref="HGNC:HGNC:11324"
                     /db_xref="MIM:600867"
ORIGIN      
        1 mrllsfvvla lfavtqaeeg arllasksll nryavegrdl tlqyniynvg ssaaldvels
       61 ddsfppedfg ivsgmlnvkw driapasnvs htvvlrplka gyfnftsati tylaqedgpv
      121 vigstsapgq ggilaqrefd rrfsphfldw aafgvmtlps igiplllwys skrkydtpkt
      181 kkn
//
LOCUS       NP_777559                188 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 36 [Homo sapiens].
ACCESSION   NP_777559
VERSION     NP_777559.3
DBSOURCE    REFSEQ: accession NM_174899.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 188)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 188)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC017869.1, BC033935.1, AK123085.1, AC009973.10 and BM997950.1.
            
            On Aug 5, 2006 this sequence version replaced NP_777559.2.
            
            Summary: Members of the F-box protein family, such as FBXO36, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.52603.1,
                                           SRR1660809.214853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283946.8/ ENSP00000283946.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..188
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q36.3"
     Protein         1..188
                     /product="F-box only protein 36"
                     /calculated_mol_wt=21974
     Region          94..139
                     /region_name="F-box_FBXO36"
                     /note="F-box domain found in F-box only protein 36
                     (FBXO36) and similar proteins; cd22106"
                     /db_xref="CDD:438878"
     Site            order(97,101,104..105,108..109,113,115..116,120..122,124)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438878"
     CDS             1..188
                     /gene="FBXO36"
                     /gene_synonym="Fbx36"
                     /coded_by="NM_174899.5:12..578"
                     /db_xref="CCDS:CCDS2472.1"
                     /db_xref="GeneID:130888"
                     /db_xref="HGNC:HGNC:27020"
                     /db_xref="MIM:609105"
ORIGIN      
        1 maswlpetlf etvgqgppps kdyyqllvtr sqvifrwwki slrseyrstk pgeakethed
       61 flenshlqgq talifgaril dyvinlckgk fdflerlsdd llltiisyld lediarlcqt
      121 shrfaklcms dklweqivqs tcdtitpdvr alaedtgwrq lfftnklqlq rqlrkrkqky
      181 gnlrekqp
//
LOCUS       NP_060937                259 aa            linear   PRI 20-NOV-2025
DEFINITION  vesicle transport protein USE1 [Homo sapiens].
ACCESSION   NP_060937
VERSION     NP_060937.2
DBSOURCE    REFSEQ: accession NM_018467.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 259)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 259)
  AUTHORS   Schnell,L., Zubrod,A., Catone,N., Bialas,J. and Aichem,A.
  TITLE     Tumor necrosis factor mediates USE1-independent FAT10ylation under
            inflammatory conditions
  JOURNAL   Life Sci Alliance 6 (11), e202301985 (2023)
   PUBMED   37604583
  REMARK    GeneRIF: Tumor necrosis factor mediates USE1-independent
            FAT10ylation under inflammatory conditions.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 259)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 259)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 259)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 259)
  AUTHORS   Aoki,T., Ichimura,S., Itoh,A., Kuramoto,M., Shinkawa,T., Isobe,T.
            and Tagaya,M.
  TITLE     Identification of the neuroblastoma-amplified gene product as a
            component of the syntaxin 18 complex implicated in
            Golgi-to-endoplasmic reticulum retrograde transport
  JOURNAL   Mol Biol Cell 20 (11), 2639-2649 (2009)
   PUBMED   19369418
  REMARK    GeneRIF: Results together suggest that NAG links between p31 and
            ZW10-RINT-1 and is involved in Golgi-to-ER transport.
REFERENCE   7  (residues 1 to 259)
  AUTHORS   Okumura,A.J., Hatsuzawa,K., Tamura,T., Nagaya,H., Saeki,K.,
            Okumura,F., Nagao,K., Nishikawa,M., Yoshimura,A. and Wada,I.
  TITLE     Involvement of a novel Q-SNARE, D12, in quality control of the
            endomembrane system
  JOURNAL   J Biol Chem 281 (7), 4495-4506 (2006)
   PUBMED   16354670
REFERENCE   8  (residues 1 to 259)
  AUTHORS   Nakajima,K., Hirose,H., Taniguchi,M., Kurashina,H., Arasaki,K.,
            Nagahama,M., Tani,K., Yamamoto,A. and Tagaya,M.
  TITLE     Involvement of BNIP1 in apoptosis and endoplasmic reticulum
            membrane fusion
  JOURNAL   EMBO J 23 (16), 3216-3226 (2004)
   PUBMED   15272311
REFERENCE   9  (residues 1 to 259)
  AUTHORS   Hirose,H., Arasaki,K., Dohmae,N., Takio,K., Hatsuzawa,K.,
            Nagahama,M., Tani,K., Yamamoto,A., Tohyama,M. and Tagaya,M.
  TITLE     Implication of ZW10 in membrane trafficking between the endoplasmic
            reticulum and Golgi
  JOURNAL   EMBO J 23 (6), 1267-1278 (2004)
   PUBMED   15029241
REFERENCE   10 (residues 1 to 259)
  AUTHORS   Matsuda,A., Suzuki,Y., Honda,G., Muramatsu,S., Matsuzaki,O.,
            Nagano,Y., Doi,T., Shimotohno,K., Harada,T., Nishida,E., Hayashi,H.
            and Sugano,S.
  TITLE     Large-scale identification and characterization of human genes that
            activate NF-kappaB and MAPK signaling pathways
  JOURNAL   Oncogene 22 (21), 3307-3318 (2003)
   PUBMED   12761501
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC020913.9.
            
            On Nov 23, 2018 this sequence version replaced NP_060937.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.251445.1,
                                           SRR5189667.84173.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263897.10/ ENSP00000263897.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..259
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..259
                     /product="vesicle transport protein USE1"
                     /note="Q-SNARE; SNARE-like tail-anchored protein 1
                     homolog; putative MAPK activating protein PM26; protein
                     p31; USE1-like protein; unconventional SNARE in the ER 1
                     homolog"
                     /calculated_mol_wt=29240
     Region          5..255
                     /region_name="Use1"
                     /note="Membrane fusion protein Use1; pfam09753"
                     /db_xref="CDD:462882"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZ43.2)"
     CDS             1..259
                     /gene="USE1"
                     /gene_synonym="D12; MDS032; P31; SLT1"
                     /coded_by="NM_018467.4:50..829"
                     /db_xref="CCDS:CCDS46011.1"
                     /db_xref="GeneID:55850"
                     /db_xref="HGNC:HGNC:30882"
                     /db_xref="MIM:610675"
ORIGIN      
        1 maasrlelnl vrllsrceam aaekrdpdew rlekyvgale dmlqalkvha skpasevine
       61 yswkvdflkg mlqaekltss sekalanqfl apgrvpttar ervpatktvh lqsrarytse
      121 mrsellgtds aepemdvrkr tgvagsqpvs ekqlaaeldl vlqrhqnlqe klaeemlgla
      181 rslktntlaa qsvikkdnqt lshslkmadq nleklktese rleqhtqksv nwllwamlii
      241 vcfifismil firimpklk
//
LOCUS       NP_006238                499 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 5 isoform 1 [Homo sapiens].
ACCESSION   NP_006238
VERSION     NP_006238.1
DBSOURCE    REFSEQ: accession NM_006247.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Dou,L., Wang,J., Deng,R., Wang,C., Xie,Z. and Yong,W.
  TITLE     Over-expression of human PP5 gene in mice induces corneal
            hyperplasia and leads to ocular surface squamous neoplasia
  JOURNAL   Biochem Biophys Res Commun 529 (2), 487-493 (2020)
   PUBMED   32703456
  REMARK    GeneRIF: Over-expression of human PP5 gene in mice induces corneal
            hyperplasia and leads to ocular surface squamous neoplasia.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Wang,L. and Yan,F.
  TITLE     Exploring the role of active site Mn2+ ions in the binding of
            protein phosphatase 5 with its substrate using molecular dynamics
            simulations
  JOURNAL   Biochem Biophys Res Commun 511 (3), 612-618 (2019)
   PUBMED   30826056
  REMARK    GeneRIF: The role of the catalytic Mn(2+) ions in regulating the
            binding of PP5 with its substrate was investigated through MD
            simulations. Results reveal that the different states of Mn(2+)
            ions can alter the structure of the active site and the
            conformations of the residues coordinating the Mn(2+) ions or the
            substrate.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Zhao,S. and Sancar,A.
  TITLE     Human blue-light photoreceptor hCRY2 specifically interacts with
            protein serine/threonine phosphatase 5 and modulates its activity
  JOURNAL   Photochem Photobiol 66 (5), 727-731 (1997)
   PUBMED   9383998
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Silverstein,A.M., Galigniana,M.D., Chen,M.S., Owens-Grillo,J.K.,
            Chinkers,M. and Pratt,W.B.
  TITLE     Protein phosphatase 5 is a major component of glucocorticoid
            receptor.hsp90 complexes with properties of an FK506-binding
            immunophilin
  JOURNAL   J Biol Chem 272 (26), 16224-16230 (1997)
   PUBMED   9195923
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Xu,X., Lagercrantz,J., Zickert,P., Bajalica-Lagercrantz,S. and
            Zetterberg,A.
  TITLE     Chromosomal localization and 5' sequence of the human protein
            serine/threonine phosphatase 5' gene
  JOURNAL   Biochem Biophys Res Commun 218 (2), 514-517 (1996)
   PUBMED   8561788
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Yong,W.H., Ueki,K., Chou,D., Reeves,S.A., von Deimling,A.,
            Gusella,J.F., Mohrenweiser,H.W., Buckler,A.J. and Louis,D.N.
  TITLE     Cloning of a highly conserved human protein serine-threonine
            phosphatase gene from the glioma candidate region on chromosome
            19q13.3
  JOURNAL   Genomics 29 (2), 533-536 (1995)
   PUBMED   8666404
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Chen,M.X., McPartlin,A.E., Brown,L., Chen,Y.H., Barker,H.M. and
            Cohen,P.T.
  TITLE     A novel human protein serine/threonine phosphatase, which possesses
            four tetratricopeptide repeat motifs and localizes to the nucleus
  JOURNAL   EMBO J 13 (18), 4278-4290 (1994)
   PUBMED   7925273
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001970.1 and AC007193.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a serine/threonine phosphatase which is
            a member of the protein phosphatase catalytic subunit family.
            Proteins in this family participate in pathways regulated by
            reversible phosphorylation at serine and threonine residues; many
            of these pathways are involved in the regulation of cell growth and
            differentiation. The product of this gene has been shown to
            participate in signaling pathways in response to hormones or
            cellular stress, and elevated levels of this protein may be
            associated with breast cancer development. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Feb
            2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223222.1, SRR7410570.655620.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000012443.9/ ENSP00000012443.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..499
                     /product="serine/threonine-protein phosphatase 5 isoform
                     1"
                     /EC_number="3.1.3.16"
                     /note="serine/threonine-protein phosphatase 5; PP-T;
                     protein phosphatase T"
                     /calculated_mol_wt=56748
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P53041.1)"
     Region          <19..147
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          28..61
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     Region          28..56
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(29,32..33,36..37,39,63,66..67,70..71,73..74,97,
                     100..101,104..105,108)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          61..91
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          62..95
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     Region          96..129
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     Region          96..124
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          176..491
                     /region_name="MPP_PP5_C"
                     /note="PP5, C-terminal metallophosphatase domain; cd07417"
                     /db_xref="CDD:277362"
     Region          184..499
                     /region_name="Catalytic"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     Site            order(242,244,271,274..275,303..304,352,386,400,427,451)
                     /site_type="active"
                     /db_xref="CDD:277362"
     Site            order(242,244,271,303,352,427)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:277362"
     Site            order(275,313,397,399..401,451,454)
                     /site_type="other"
                     /note="TPR interaction site [polypeptide binding]"
                     /db_xref="CDD:277362"
     Region          495..499
                     /region_name="Required for autoinhibition.
                     /evidence=ECO:0000250|UniProtKB:P53042"
                     /note="propagated from UniProtKB/Swiss-Prot (P53041.1)"
     CDS             1..499
                     /gene="PPP5C"
                     /gene_synonym="PP5; PPP5; PPT"
                     /coded_by="NM_006247.4:11..1510"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12684.1"
                     /db_xref="GeneID:5536"
                     /db_xref="HGNC:HGNC:9322"
                     /db_xref="MIM:600658"
ORIGIN      
        1 mamaegerte caepprdepp adgalkraee lktqandyfk akdyenaikf ysqaielnps
       61 naiyygnrsl aylrtecygy algdatraie ldkkyikgyy rraasnmalg kfraalrdye
      121 tvvkvkphdk dakmkyqecn kivkqkafer aiagdehkrs vvdsldiesm tiedeysgpk
      181 ledgkvtisf mkelmqwykd qkklhrkcay qilvqvkevl sklstlvett lketekitvc
      241 gdthgqfydl lnifelnglp setnpyifng dfvdrgsfsv eviltlfgfk llypdhfhll
      301 rgnhetdnmn qiygfegevk akytaqmyel fsevfewlpl aqcingkvli mhgglfsedg
      361 vtlddirkie rnrqppdsgp mcdllwsdpq pqngrsiskr gvscqfgpdv tkafleennl
      421 dyiirshevk aegyevahgg rcvtvfsapn ycdqmgnkas yihlqgsdlr pqfhqftavp
      481 hpnvkpmaya ntllqlgmm
//
LOCUS       NP_004255                144 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 21 isoform 1
            [Homo sapiens].
ACCESSION   NP_004255
VERSION     NP_004255.2
DBSOURCE    REFSEQ: accession NM_004264.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Pan,G., Aso,T. and Greenblatt,J.
  TITLE     Interaction of elongation factors TFIIS and elongin A with a human
            RNA polymerase II holoenzyme capable of promoter-specific
            initiation and responsive to transcriptional activators
  JOURNAL   J Biol Chem 272 (39), 24563-24571 (1997)
   PUBMED   9305922
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Scully,R., Anderson,S.F., Chao,D.M., Wei,W., Ye,L., Young,R.A.,
            Livingston,D.M. and Parvin,J.D.
  TITLE     BRCA1 is a component of the RNA polymerase II holoenzyme
  JOURNAL   Proc Natl Acad Sci U S A 94 (11), 5605-5610 (1997)
   PUBMED   9159119
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Cujec,T.P., Cho,H., Maldonado,E., Meyer,J., Reinberg,D. and
            Peterlin,B.M.
  TITLE     The human immunodeficiency virus transactivator Tat interacts with
            the RNA polymerase II holoenzyme
  JOURNAL   Mol Cell Biol 17 (4), 1817-1823 (1997)
   PUBMED   9121429
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Maldonado,E., Shiekhattar,R., Sheldon,M., Cho,H., Drapkin,R.,
            Rickert,P., Lees,E., Anderson,C.W., Linn,S. and Reinberg,D.
  TITLE     A human RNA polymerase II complex associated with SRB and
            DNA-repair proteins
  JOURNAL   Nature 381 (6577), 86-89 (1996)
   PUBMED   8609996
  REMARK    Erratum:[Nature 1996 Nov 28;384(6607):384]
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Chao,D.M., Gadbois,E.L., Murray,P.J., Anderson,S.F., Sonu,M.S.,
            Parvin,J.D. and Young,R.A.
  TITLE     A mammalian SRB protein associated with an RNA polymerase II
            holoenzyme
  JOURNAL   Nature 380 (6569), 82-85 (1996)
   PUBMED   8598913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092747.10.
            
            On Jun 10, 2002 this sequence version replaced NP_004255.1.
            
            Summary: This gene encodes a member of the mediator complex subunit
            21 family. The encoded protein interacts with the human RNA
            polymerase II holoenzyme and is involved in transcriptional
            regulation of RNA polymerase II transcribed genes. A pseudogene of
            this gene is located on chromosome 8. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.224775.1,
                                           SRR3476690.681190.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282892.4/ ENSP00000282892.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.23"
     Protein         1..144
                     /product="mediator of RNA polymerase II transcription
                     subunit 21 isoform 1"
                     /note="mediator of RNA polymerase II transcription subunit
                     21; RNAPII complex component SRB7; RNA polymerase II
                     holoenzyme component SRB7; SRB7 suppressor of RNA
                     polymerase B homolog"
                     /calculated_mol_wt=15433
     Region          3..127
                     /region_name="Med21"
                     /note="Subunit 21 of Mediator complex; pfam11221"
                     /db_xref="CDD:463241"
     CDS             1..144
                     /gene="MED21"
                     /gene_synonym="hSrb7; SRB7; SURB7"
                     /coded_by="NM_004264.5:23..457"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8711.1"
                     /db_xref="GeneID:9412"
                     /db_xref="HGNC:HGNC:11473"
                     /db_xref="MIM:603800"
ORIGIN      
        1 madrltqlqd avnsladqfc naigvlqqcg ppasfnniqt ainkdqpanp teeyaqlfaa
       61 liartakdid vlidslpsee staalqaasl ykleeenhea atcledvvyr gdmllekiqs
      121 aladiaqsql ktrsgthsqs lpds
//
LOCUS       NP_653209                286 aa            linear   PRI 20-NOV-2025
DEFINITION  protein HEXIM2 isoform 1 [Homo sapiens].
ACCESSION   NP_653209
VERSION     NP_653209.1
DBSOURCE    REFSEQ: accession NM_144608.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Walker,F.M., Sobral,L.M., Danis,E., Sanford,B., Donthula,S.,
            Balakrishnan,I., Wang,D., Pierce,A., Karam,S.D., Kargar,S.,
            Serkova,N.J., Foreman,N.K., Venkataraman,S., Dowell,R., Vibhakar,R.
            and Dahl,N.A.
  TITLE     Rapid P-TEFb-dependent transcriptional reorganization underpins the
            glioma adaptive response to radiotherapy
  JOURNAL   Nat Commun 15 (1), 4616 (2024)
   PUBMED   38816355
  REMARK    GeneRIF: Rapid P-TEFb-dependent transcriptional reorganization
            underpins the glioma adaptive response to radiotherapy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Li,Q., Price,J.P., Byers,S.A., Cheng,D., Peng,J. and Price,D.H.
  TITLE     Analysis of the large inactive P-TEFb complex indicates that it
            contains one 7SK molecule, a dimer of HEXIM1 or HEXIM2, and two
            P-TEFb molecules containing Cdk9 phosphorylated at threonine 186
  JOURNAL   J Biol Chem 280 (31), 28819-28826 (2005)
   PUBMED   15965233
  REMARK    GeneRIF: Positive transcription elongation factor b regulates
            eukaryotic gene expression at the level of elongation and is
            controlled by the reversible association with HEXIM2.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Fraldi,A., Varrone,F., Napolitano,G., Michels,A.A., Majello,B.,
            Bensaude,O. and Lania,L.
  TITLE     Inhibition of Tat activity by the HEXIM1 protein
  JOURNAL   Retrovirology 2, 42 (2005)
   PUBMED   15992410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Byers,S.A., Price,J.P., Cooper,J.J., Li,Q. and Price,D.H.
  TITLE     HEXIM2, a HEXIM1-related protein, regulates positive transcription
            elongation factor b through association with 7SK
  JOURNAL   J Biol Chem 280 (16), 16360-16367 (2005)
   PUBMED   15713662
  REMARK    GeneRIF: utilization of HEXIM1 or HEXIM2 to bind and inhibit P-TEFb
            can be differentially regulated in vivo.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yik,J.H., Chen,R., Pezda,A.C. and Zhou,Q.
  TITLE     Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the
            balance of active and inactive positive transcription elongation
            factor b complexes for control of transcription
  JOURNAL   J Biol Chem 280 (16), 16368-16376 (2005)
   PUBMED   15713661
  REMARK    GeneRIF: HEXIM2 can functionally and quantitatively compensate for
            the loss of HEXIM1
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Michels,A.A., Nguyen,V.T., Fraldi,A., Labas,V., Edwards,M.,
            Bonnet,F., Lania,L. and Bensaude,O.
  TITLE     MAQ1 and 7SK RNA interact with CDK9/cyclin T complexes in a
            transcription-dependent manner
  JOURNAL   Mol Cell Biol 23 (14), 4859-4869 (2003)
   PUBMED   12832472
  REMARK    Erratum:[Mol Cell Biol. 2003 Dec;23(24):9405]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP398345.1, AW340131.1,
            BU501076.1, AK056946.1 and CA312679.1.
            
            Summary: This gene encodes a member of the HEXIM family of
            proteins. This protein is a component of the 7SK small nuclear
            ribonucleoprotein. This protein has been found to negatively
            regulate the kinase activity of the cyclin-dependent kinase P-TEFb,
            which phosphorylates multiple target proteins to promote
            transcriptional elongation. This gene is located approximately 7 kb
            downstream from related family member HEXIM1 on chromosome 17.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jan 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-9 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056946.1, SRR1163657.170363.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..286
                     /product="protein HEXIM2 isoform 1"
                     /note="hexamethylene-bis-acetamide-inducible transcript 2;
                     hexamethylene bis-acetamide inducible 2; MAQ1 paralog;
                     protein HEXIM2; hexamethylene bis-acetamide-inducible
                     protein 2; hexamethylene bisacetamide inducible 2"
                     /calculated_mol_wt=32287
     Region          1..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          102..227
                     /region_name="HEXIM"
                     /note="Hexamethylene bis-acetamide-inducible protein;
                     pfam15313"
                     /db_xref="CDD:464638"
     Region          140..143
                     /region_name="Interaction with P-TEFb"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     Region          216..>271
                     /region_name="YabA"
                     /note="Regulator of replication initiation timing YabA
                     [Replication, recombination and repair]; COG4467"
                     /db_xref="CDD:443564"
     Region          226..286
                     /region_name="Interaction with CCNT1, HEXIM1 and HEXIM2.
                     /evidence=ECO:0000269|PubMed:15713661,
                     ECO:0000269|PubMed:15994294"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96MH2.1)"
     CDS             1..286
                     /gene="HEXIM2"
                     /gene_synonym="L3"
                     /coded_by="NM_144608.2:963..1823"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11496.1"
                     /db_xref="GeneID:124790"
                     /db_xref="HGNC:HGNC:28591"
                     /db_xref="MIM:615695"
ORIGIN      
        1 mmatpnqtac naespvalee aktsgapgsp qtpperhdsg gslpltprme shsededlag
       61 avgglgwnsr sprtqspggc saeavlarkk hrrrpskrkr hwrpylelsw aekqqrderq
      121 sqrasrvree mfakgqpvap ynttqflmnd rdpeepnldv phgishpgss geseagdsdg
      181 rgrahgefqr kdfsetyerf hteslqgrsk qelvrdylel ekrlsqaeee trrlqqlqac
      241 tgqqscrqve elaaevqrlr tenqrlrqen qmwnregcrc deepgt
//
LOCUS       NP_001353585             529 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase VB isoform 2 [Homo sapiens].
ACCESSION   NP_001353585
VERSION     NP_001353585.1
DBSOURCE    REFSEQ: accession NM_001366656.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Sanchiz-Calvo,M., Coccia,E., Cawthorne,C., Morrone Parfitt,G.,
            Torre-Muruzabal,T., Tsafaras,G., Van Laere,K., Cabezudo,D.,
            Cascalho,A., Van den Haute,C., Vangheluwe,P., Blanchard,J.,
            Bentea,E. and Baekelandt,V.
  TITLE     Loss of the lysosomal lipid flippase ATP10B leads to progressive
            dopaminergic neurodegeneration and parkinsonian motor deficits
  JOURNAL   Acta Neuropathol 150 (1), 5 (2025)
   PUBMED   40676227
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Diaz-Belloso,R., Munoz-Delgado,L., Martin-Bornez,M., Ojeda,E.,
            Perinan,M.T., Garcia-Diaz,S., Bonilla-Toribio,M., Buiza-Rueda,D.,
            Pineda-Sanchez,R., Jesus,S., Macias-Garcia,D., Adarmes-Gomez,A.,
            Carrillo,F., Mir,P. and Gomez-Garre,P.
  TITLE     Role of ATP10B in Parkinson disease in a cohort from southern Spain
  JOURNAL   Parkinsonism Relat Disord 124, 106989 (2024)
   PUBMED   38754220
  REMARK    GeneRIF: Role of ATP10B in Parkinson disease in a cohort from
            southern Spain.
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Wouters,R., Beletchi,I., Van den Haute,C., Baekelandt,V.,
            Martin,S., Eggermont,J. and Vangheluwe,P.
  TITLE     The lipid flippase ATP10B enables cellular lipid uptake under
            stress conditions
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (2), 119652 (2024)
   PUBMED   38086447
  REMARK    GeneRIF: The lipid flippase ATP10B enables cellular lipid uptake
            under stress conditions.
            Review article
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Ishiguro,M., Yoshino,H., Li,Y., Ikeda,A., Funayama,M., Nishioka,K.
            and Hattori,N.
  TITLE     Genetic analysis of ATP10B for Parkinson's disease in Japan
  JOURNAL   Parkinsonism Relat Disord 88, 10-12 (2021)
   PUBMED   34091411
  REMARK    GeneRIF: Genetic analysis of ATP10B for Parkinson's disease in
            Japan.
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Martin,S., Smolders,S., Van den Haute,C., Heeman,B., van Veen,S.,
            Crosiers,D., Beletchi,I., Verstraeten,A., Gossye,H., Gelders,G.,
            Pals,P., Hamouda,N.N., Engelborghs,S., Martin,J.J., Eggermont,J.,
            De Deyn,P.P., Cras,P., Baekelandt,V., Vangheluwe,P. and Van
            Broeckhoven,C.
  CONSRTM   BELNEU consortium
  TITLE     Mutated ATP10B increases Parkinson's disease risk by compromising
            lysosomal glucosylceramide export
  JOURNAL   Acta Neuropathol 139 (6), 1001-1024 (2020)
   PUBMED   32172343
  REMARK    GeneRIF: Mutated ATP10B increases Parkinson's disease risk by
            compromising lysosomal glucosylceramide export.
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Segawa,K., Kurata,S. and Nagata,S.
  TITLE     Human Type IV P-type ATPases That Work as Plasma Membrane
            Phospholipid Flippases and Their Regulation by Caspase and Calcium
  JOURNAL   J Biol Chem 291 (2), 762-772 (2016)
   PUBMED   26567335
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Naito,T., Takatsu,H., Miyano,R., Takada,N., Nakayama,K. and
            Shin,H.W.
  TITLE     Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and
            Is Involved in Plasma Membrane Dynamics
  JOURNAL   J Biol Chem 290 (24), 15004-15017 (2015)
   PUBMED   25947375
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Takatsu,H., Baba,K., Shima,T., Umino,H., Kato,U., Umeda,M.,
            Nakayama,K. and Shin,H.W.
  TITLE     ATP9B, a P4-ATPase (a putative aminophospholipid translocase),
            localizes to the trans-Golgi network in a CDC50 protein-independent
            manner
  JOURNAL   J Biol Chem 286 (44), 38159-38167 (2011)
   PUBMED   21914794
  REMARK    Erratum:[J Biol Chem. 2015 Jan 9;290(2):886]
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   10 (residues 1 to 529)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC091928.3, AC011363.6 and AC008456.6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.183252.1,
                                           SRR1803611.182801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..529
                     /product="phospholipid-transporting ATPase VB isoform 2"
                     /EC_number="7.6.2.1"
                     /note="probable phospholipid-transporting ATPase VB;
                     P4-ATPase flippase complex alpha subunit ATP10B; ATPase,
                     class V, type 10B"
                     /calculated_mol_wt=61112
     Region          68..>455
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     Site            83..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            111..132
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            317..338
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Site            369..390
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O94823.2)"
     Region          429..>495
                     /region_name="Haloacid Dehalogenase-like Hydrolases"
                     /note="The haloacid dehalogenase (HAD) superfamily
                     includes carbon and phosphorus hydrolases such as
                     2-haloalkonoate dehalogenase, epoxide hydrolase,
                     phosphoserine phosphatase, phosphomannomutase,
                     phosphoglycolate phosphatase, P-type ATPase, among others.
                     These...; cl21460"
                     /db_xref="CDD:473868"
     CDS             1..529
                     /gene="ATP10B"
                     /gene_synonym="ATPVB"
                     /coded_by="NM_001366656.2:486..2075"
                     /note="isoform 2 is encoded by transcript variant 6"
                     /db_xref="GeneID:23120"
                     /db_xref="HGNC:HGNC:13543"
                     /db_xref="MIM:619791"
ORIGIN      
        1 malsvdsswh rwqwrvrdgf phcpsettpl lspekgrqsy nltqqrvvfp nnsifhqdwe
       61 evsrrypgnr tcttkytlft flprnlfeqf hrwanlyflf lvilnwmpsm evfhreitml
      121 plaivlfvim ikdgmedfkr hrfdkaincs niriyerkeq tyvqkcwkdv rvgdfiqmkc
      181 neivpadill lfssdpngic hletasldge tnlkqrcvvk gfsqqevqfe pelfhntivc
      241 ekpnnhlnkf kgymehpdqt rtgfgcesll lrgctirnte mavgiviyag hetkamlnns
      301 gprykrskie rrmnidiffc igililmcli gavghsiwng tfeehppfdv pdangsflps
      361 alggfymflt miillqvlip islyvsielv klgqvfflsn dldlydeetd lsiqcralni
      421 aedlgqiqyi fsdktgtlte nkmvfrrcti mgseyshqen gieapkgsip lskrkypall
      481 rneeikdill alleavwhfh kllpvslwss lsqiravpit cklsfvykg
//
LOCUS       NP_001231775             442 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase Chk1 isoform 2 [Homo sapiens].
ACCESSION   NP_001231775
VERSION     NP_001231775.1
DBSOURCE    REFSEQ: accession NM_001244846.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 442)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 442)
  AUTHORS   Wang,J., Liu,Y., Wu,D., Tian,C., Gao,J., Yang,Q., Hong,X., Gu,F.,
            Zhang,K., Hu,Y., Xu,S., Liu,L. and Zeng,Y.
  TITLE     OTUB1 Targets CHK1 for Deubiquitination and Stabilization to
            Facilitate Lung Cancer Progression and Radioresistance
  JOURNAL   Int J Radiat Oncol Biol Phys 119 (4), 1222-1233 (2024)
   PUBMED   38266782
  REMARK    GeneRIF: OTUB1 Targets CHK1 for Deubiquitination and Stabilization
            to Facilitate Lung Cancer Progression and Radioresistance.
REFERENCE   3  (residues 1 to 442)
  AUTHORS   Ando,S., Tanaka,K., Matsumoto,M., Oyama,Y., Tomabechi,Y.,
            Yamagata,A., Shirouzu,M., Nakagawa,R., Okimoto,N., Taiji,M.,
            Sato,K. and Ohama,T.
  TITLE     The luciferase-based in vivo protein-protein interaction assay
            revealed that CHK1 promotes PP2A and PME-1 interaction
  JOURNAL   J Biol Chem 300 (5), 107277 (2024)
   PUBMED   38588804
  REMARK    GeneRIF: The luciferase-based in vivo protein-protein interaction
            assay revealed that CHK1 promotes PP2A and PME-1 interaction.
REFERENCE   4  (residues 1 to 442)
  AUTHORS   Egger,T., Morano,L., Blanchard,M.P., Basbous,J. and Constantinou,A.
  TITLE     Spatial organization and functions of Chk1 activation by TopBP1
            biomolecular condensates
  JOURNAL   Cell Rep 43 (4), 114064 (2024)
   PUBMED   38578830
  REMARK    GeneRIF: Spatial organization and functions of Chk1 activation by
            TopBP1 biomolecular condensates.
REFERENCE   5  (residues 1 to 442)
  AUTHORS   Colaco,V., Goswami,N., Goel,V.K., Srivastava,S.K., Lalrohlua,P.,
            Senthil Kumar,N., Borah,P., Baruah,R. and Varma,A.K.
  TITLE     In silico and structure-based evaluation of deleterious mutations
            identified in human Chk1, Chk2, and Wee1 protein kinase
  JOURNAL   J Cell Biochem 125 (1), 89-99 (2024)
   PUBMED   38047473
  REMARK    GeneRIF: In silico and structure-based evaluation of deleterious
            mutations identified in human Chk1, Chk2, and Wee1 protein kinase.
REFERENCE   6  (residues 1 to 442)
  AUTHORS   Giaccia,A.J. and Kastan,M.B.
  TITLE     The complexity of p53 modulation: emerging patterns from divergent
            signals
  JOURNAL   Genes Dev 12 (19), 2973-2983 (1998)
   PUBMED   9765199
  REMARK    Review article
REFERENCE   7  (residues 1 to 442)
  AUTHORS   Flaggs,G., Plug,A.W., Dunks,K.M., Mundt,K.E., Ford,J.C.,
            Quiggle,M.R., Taylor,E.M., Westphal,C.H., Ashley,T., Hoekstra,M.F.
            and Carr,A.M.
  TITLE     Atm-dependent interactions of a mammalian chk1 homolog with meiotic
            chromosomes
  JOURNAL   Curr Biol 7 (12), 977-986 (1997)
   PUBMED   9382850
REFERENCE   8  (residues 1 to 442)
  AUTHORS   Peng,C.Y., Graves,P.R., Thoma,R.S., Wu,Z., Shaw,A.S. and
            Piwnica-Worms,H.
  TITLE     Mitotic and G2 checkpoint control: regulation of 14-3-3 protein
            binding by phosphorylation of Cdc25C on serine-216
  JOURNAL   Science 277 (5331), 1501-1505 (1997)
   PUBMED   9278512
REFERENCE   9  (residues 1 to 442)
  AUTHORS   Sanchez,Y., Wong,C., Thoma,R.S., Richman,R., Wu,Z.,
            Piwnica-Worms,H. and Elledge,S.J.
  TITLE     Conservation of the Chk1 checkpoint pathway in mammals: linkage of
            DNA damage to Cdk regulation through Cdc25
  JOURNAL   Science 277 (5331), 1497-1501 (1997)
   PUBMED   9278511
  REMARK    GeneRIF: Biochemical studies suggest the functional interactions of
            this protein with cell cycle regulators. Cdc25A, Cdc25B, and Cdc25C
            can be phosphoryalted by this protein.
REFERENCE   10 (residues 1 to 442)
  AUTHORS   Ward,G.E. and Kirschner,M.W.
  TITLE     Identification of cell cycle-regulated phosphorylation sites on
            nuclear lamin C
  JOURNAL   Cell 61 (4), 561-577 (1990)
   PUBMED   2188730
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX419129.2, AW149126.1,
            CA868104.1, AK300082.1, DA567616.1, AK293143.1, BC004202.2,
            CA441277.1, BM455102.1, BX506561.1, BX114781.1, AI750792.1 and
            AA224205.1.
            
            Summary: The protein encoded by this gene belongs to the Ser/Thr
            protein kinase family. It is required for checkpoint mediated cell
            cycle arrest in response to DNA damage or the presence of
            unreplicated DNA. This protein acts to integrate signals from ATM
            and ATR, two cell cycle proteins involved in DNA damage responses,
            that also associate with chromatin in meiotic prophase I.
            Phosphorylation of CDC25A protein phosphatase by this protein is
            required for cells to delay cell cycle progression in response to
            double-strand DNA breaks. Several alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Oct
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293143.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..442
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.2"
     Protein         1..442
                     /product="serine/threonine-protein kinase Chk1 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="Checkpoint, S. pombe, homolog of, 1;
                     serine/threonine-protein kinase Chk1; CHK1 checkpoint
                     homolog; cell cycle checkpoint kinase; Chk1-S"
                     /calculated_mol_wt=50284
     Region          7..265
                     /region_name="STKc_Chk1"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Checkpoint kinase 1; cd14069"
                     /db_xref="CDD:270971"
     Site            order(15..19,23,36,38,68,84..87,91,93,129..130,132,
                     134..135,137,147..148,151,168..172,174)
                     /site_type="active"
                     /db_xref="CDD:270971"
     Site            order(15..18,23,36,38,68,84..87,91,134..135,137,147..148)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270971"
     Site            order(19,91,93,129..130,132,134,151,168..172,174)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270971"
     Site            order(93..94,96..98,133,173,200,204..206)
                     /site_type="other"
                     /note="allosteric inhibitor binding site [chemical
                     binding]"
                     /db_xref="CDD:270971"
     Site            147..172
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270971"
     CDS             1..442
                     /gene="CHEK1"
                     /gene_synonym="CHK1; OZEMA21"
                     /coded_by="NM_001244846.1:898..2226"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58191.1"
                     /db_xref="GeneID:1111"
                     /db_xref="HGNC:HGNC:1925"
                     /db_xref="MIM:603078"
ORIGIN      
        1 mavpfvedwd lvqtlgegay gevqlavnrv teeavavkiv dmkravdcpe nikkeicink
       61 mlnhenvvkf yghrregniq ylfleycsgg elfdriepdi gmpepdaqrf fhqlmagvvy
      121 lhgigithrd ikpenlllde rdnlkisdfg latvfrynnr erllnkmcgt lpyvapellk
      181 rrefhaepvd vwscgivlta mlagelpwdq psdscqeysd wkekktylnp wkkidsapla
      241 llhkilvenp saritipdik kdrwynkplk kgakrprvts ggvsespsgf skhiqsnldf
      301 spvnsassee nvkysssqpe prtglslwdt spsyidklvq gisfsqptcp dhmllnsqll
      361 gtpgssqnpw qrlvkrmtrf ftkldadksy qclketcekl gyqwkkscmn qgdglefkrh
      421 flkikgklid ivssqkiwlp at
//
LOCUS       NP_056299                243 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor SYF2 isoform 1 [Homo sapiens].
ACCESSION   NP_056299
VERSION     NP_056299.1
DBSOURCE    REFSEQ: accession NM_015484.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Tanaka,I., Chakraborty,A., Saulnier,O., Benoit-Pilven,C.,
            Vacher,S., Labiod,D., Lam,E.W.F., Bieche,I., Delattre,O.,
            Pouzoulet,F., Auboeuf,D., Vagner,S. and Dutertre,M.
  TITLE     ZRANB2 and SYF2-mediated splicing programs converging on ECT2 are
            involved in breast cancer cell resistance to doxorubicin
  JOURNAL   Nucleic Acids Res 48 (5), 2676-2693 (2020)
   PUBMED   31943118
  REMARK    GeneRIF: These data identify Aletrnative splicing programs
            controlled by ZRANB2 and SYF2 and converging on ECT2, that
            participate to breast cancer cell resistance to doxorubicin.
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Chen,Z.Y., Liu,H.Y., Jiang,N. and Yuan,J.M.
  TITLE     LncRNA HOST2 enhances gefitinib-resistance in non-small cell lung
            cancer by down-regulating miRNA-621
  JOURNAL   Eur Rev Med Pharmacol Sci 23 (22), 9939-9946 (2019)
   PUBMED   31799663
  REMARK    GeneRIF: LncRNA HOST2 enhances gefitinib-resistance in non-small
            cell lung cancer by down-regulating miRNA-621.
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Chu,P.C., Yang,Y.C., Lu,Y.T., Chen,H.T., Yu,L.C. and Chang,M.S.
  TITLE     Silencing of p29 affects DNA damage responses with UV irradiation
  JOURNAL   Cancer Res 66 (17), 8484-8491 (2006)
   PUBMED   16951160
  REMARK    GeneRIF: novel function of p29 in the regulation of DNA replication
            checkpoint responses in Hela cells.
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Chang,M.S., Chang,C.L., Huang,C.J. and Yang,Y.C.
  TITLE     p29, a novel GCIP-interacting protein, localizes in the nucleus
  JOURNAL   Biochem Biophys Res Commun 279 (2), 732-737 (2000)
   PUBMED   11118353
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DR155437.1, BC010862.1 and
            AL031432.1.
            
            Summary: This gene encodes a nuclear protein that interacts with
            cyclin D-type binding-protein 1, which is thought to be a cell
            cycle regulator at the G1/S transition. Alternate transcriptional
            splice variants, encoding different isoforms, have been
            characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.285144.1,
                                           SRR3476690.1175308.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467144, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000236273.9/ ENSP00000236273.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..243
                     /product="pre-mRNA-splicing factor SYF2 isoform 1"
                     /note="GCIP-interacting protein p29; CCNDBP1 interactor;
                     functional spliceosome-associated protein 29;
                     pre-mRNA-splicing factor SYF2; SYF2 homolog, RNA splicing
                     factor"
                     /calculated_mol_wt=28591
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95926.1)"
     Region          90..238
                     /region_name="SYF2"
                     /note="SYF2 splicing factor; pfam08231"
                     /db_xref="CDD:462400"
     CDS             1..243
                     /gene="SYF2"
                     /gene_synonym="CBPIN; fSAP29; NTC31; P29"
                     /coded_by="NM_015484.5:36..767"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS259.1"
                     /db_xref="GeneID:25949"
                     /db_xref="HGNC:HGNC:19824"
                     /db_xref="MIM:607090"
ORIGIN      
        1 maaiaasevl vdsaeegsla aaaelaaqkr eqrlrkfrel hlmrnearkl nhqevveedk
       61 rlklpanwea kkarlewelk eeekkkecaa rgedyekvkl leisaedaer werkkkrknp
      121 dlgfsdyaaa qlrqyhrltk qikpdmetye rlrekhgeef fptsnsllhg thvpsteeid
      181 rmvidlekqi ekrdkysrrr pynddadidy inernakfnk kaerfygkyt aeikqnlerg
      241 tav
//
LOCUS       NP_569057                742 aa            linear   PRI 20-NOV-2025
DEFINITION  collectin-12 [Homo sapiens].
ACCESSION   NP_569057
VERSION     NP_569057.2
DBSOURCE    REFSEQ: accession NM_130386.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Asadie,M., Miri,A., Badri,T., Hosseini Nejad,J. and Gharechahi,J.
  TITLE     Dysregulated AEBP1 and COLEC12 Genes in Late-Onset Alzheimer's
            Disease: Insights from Brain Cortex and Peripheral Blood Analysis
  JOURNAL   J Mol Neurosci 74 (2), 37 (2024)
   PUBMED   38568322
  REMARK    GeneRIF: Dysregulated AEBP1 and COLEC12 Genes in Late-Onset
            Alzheimer's Disease: Insights from Brain Cortex and Peripheral
            Blood Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Sun,X., Zhang,Q., Shu,P., Lin,X., Gao,X. and Shen,K.
  TITLE     COLEC12 Promotes Tumor Progression and Is Correlated With Poor
            Prognosis in Gastric Cancer
  JOURNAL   Technol Cancer Res Treat 22, 15330338231218163 (2023)
   PUBMED   38112409
  REMARK    GeneRIF: COLEC12 Promotes Tumor Progression and Is Correlated With
            Poor Prognosis in Gastric Cancer.
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Zhang,J., Song,L., Pedersen,D.V., Li,A., Lambris,J.D.,
            Andersen,G.R., Mollnes,T.E., Ma,Y.J. and Garred,P.
  TITLE     Soluble collectin-12 mediates C3-independent docking of properdin
            that activates the alternative pathway of complement
  JOURNAL   Elife 9, e60908 (2020)
   PUBMED   32909942
  REMARK    GeneRIF: Soluble collectin-12 mediates C3-independent docking of
            properdin that activates the alternative pathway of complement.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 742)
  AUTHORS   Coombs,P.J., Graham,S.A., Drickamer,K. and Taylor,M.E.
  TITLE     Selective binding of the scavenger receptor C-type lectin to Lewisx
            trisaccharide and related glycan ligands
  JOURNAL   J Biol Chem 280 (24), 22993-22999 (2005)
   PUBMED   15845541
  REMARK    GeneRIF: SRCL might be involved in selective clearance of specific
            desialylated glycoproteins from circulation and/or interaction of
            cells bearing Lewis(x)-type structures with the vascular
            endothelium
REFERENCE   7  (residues 1 to 742)
  AUTHORS   Yoshida,T., Tsuruta,Y., Iwasaki,M., Yamane,S., Ochi,T. and
            Suzuki,R.
  TITLE     SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn
            antigen
  JOURNAL   J Biochem 133 (3), 271-277 (2003)
   PUBMED   12761161
  REMARK    GeneRIF: SRCL is expressed in some but not all nurse-like cells;
            its C-type lectin domain binds specifically to several
            carbohydrates including GalNAc, T and Tn antigen in a
            Ca2+-dependent manner.
REFERENCE   8  (residues 1 to 742)
  AUTHORS   Ohmori,H., Makita,Y., Funamizu,M., Chiba,S., Ohtani,K., Suzuki,Y.,
            Wakamiya,N. and Hata,A.
  TITLE     Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene
  JOURNAL   J Hum Genet 48 (2), 82-85 (2003)
   PUBMED   12601552
  REMARK    GeneRIF: haplotype structure of the CL-P1 gene obtained from six
            single-nucleotide polymorphisms that were genotyped with 108
            alleles in Japanese subjects
REFERENCE   9  (residues 1 to 742)
  AUTHORS   Ohtani,K., Suzuki,Y., Eda,S., Kawai,T., Kase,T., Keshi,H.,
            Sakai,Y., Fukuoh,A., Sakamoto,T., Itabe,H., Suzutani,T.,
            Ogasawara,M., Yoshida,I. and Wakamiya,N.
  TITLE     The membrane-type collectin CL-P1 is a scavenger receptor on
            vascular endothelial cells
  JOURNAL   J Biol Chem 276 (47), 44222-44228 (2001)
   PUBMED   11564734
REFERENCE   10 (residues 1 to 742)
  AUTHORS   Nakamura,K., Funakoshi,H., Miyamoto,K., Tokunaga,F. and Nakamura,T.
  TITLE     Molecular cloning and functional characterization of a human
            scavenger receptor with C-type lectin (SRCL), a novel member of a
            scavenger receptor family
  JOURNAL   Biochem Biophys Res Commun 280 (4), 1028-1035 (2001)
   PUBMED   11162630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP005240.2 and AP000915.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NP_569057.1.
            
            Summary: This gene encodes a member of the C-lectin family,
            proteins that possess collagen-like sequences and carbohydrate
            recognition domains. This protein is a scavenger receptor that
            displays several functions associated with host defense. It can
            bind to carbohydrate antigens on microorganisms, facilitating their
            recognition and removal. It also mediates the recognition,
            internalization, and degradation of oxidatively modified low
            density lipoprotein by vascular endothelial cells. [provided by
            RefSeq, May 2018].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC060789.1, AB038518.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400256.5/ ENSP00000383115.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.32"
     Protein         1..742
                     /product="collectin-12"
                     /note="scavenger receptor with C-type lectin; scavenger
                     receptor class A, member 4; nurse cell scavenger receptor
                     2; hCL-P1; collectin placenta protein 1; collectin
                     sub-family member 12"
                     /calculated_mol_wt=81384
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5KU26.3)"
     Site            67
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5KU26.3)"
     Region          108..>442
                     /region_name="CCDC158"
                     /note="Coiled-coil domain-containing protein 158;
                     pfam15921"
                     /db_xref="CDD:464943"
     Site            159
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5KU26.3)"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5KU26.3)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5KU26.3)"
     Region          439..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5KU26.3)"
     Region          607..732
                     /region_name="CLECT_DC-SIGN_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human dendritic cell (DC)-specific intercellular
                     adhesion molecule 3-grabbing non-integrin (DC-SIGN) and
                     the related receptor, DC-SIGN receptor (DC-SIGNR);
                     cd03590"
                     /db_xref="CDD:153060"
     Site            order(663,694,696,706,712..713,718..721)
                     /site_type="other"
                     /note="carbohydrate binding site"
                     /db_xref="CDD:153060"
     Site            order(670,674,697,706..707)
                     /site_type="other"
                     /note="calcium binding site 1 [ion binding]"
                     /db_xref="CDD:153060"
     Site            order(674,707)
                     /site_type="other"
                     /note="calcium binding site 3 [ion binding]"
                     /db_xref="CDD:153060"
     CDS             1..742
                     /gene="COLEC12"
                     /gene_synonym="CLP1; NSR2; SCARA4; SRCL"
                     /coded_by="NM_130386.3:188..2416"
                     /db_xref="CCDS:CCDS32782.1"
                     /db_xref="GeneID:81035"
                     /db_xref="HGNC:HGNC:16016"
                     /db_xref="MIM:607621"
ORIGIN      
        1 mkddfaeeee vqsfgykrfg iqegtqctkc knnwalkfsi illyilcall titvailgyk
       61 vvekmdnvtg gmetsrqtyd dkltavesdl kklgdqtgkk aistnselst frsdildlrq
      121 qlreitekts knkdtleklq asgdalvdrq sqlketlenn sflittvnkt lqayngyvtn
      181 lqqdtsvlqg nlqnqmyshn vvimnlnnln ltqvqqrnli tnlqrsvddt sqaiqriknd
      241 fqnlqqvflq akkdtdwlke kvqslqtlaa nnsalakann dtledmnsql nsftgqmeni
      301 ttisqaneqn lkdlqdlhkd aenrtaikfn qleerfqlfe tdivniisni sytahhlrtl
      361 tsnlnevrtt ctdtltkhtd dltslnntla nirldsvslr mqqdlmrsrl dtevanlsvi
      421 meemklvdsk hgqliknfti lqgppgprgp rgdrgsqgpp gptgnkgqkg ekgepgppgp
      481 agergpigpa gppgerggkg skgsqgpkgs rgspgkpgpq gssgdpgppg ppgkeglpgp
      541 qgppgfqglq gtvgepgvpg prglpglpgv pgmpgpkgpp gppgpsgavv plalqneptp
      601 apedngcpph wknftdkcyy fsvekeifed aklfcedkss hlvfintree qqwikkqmvg
      661 reshwigltd serenewkwl dgtspdyknw kagqpdnwgh ghgpgedcag liyagqwndf
      721 qcedvnnfic ekdretvlss al
//
LOCUS       NP_115689                698 aa            linear   PRI 20-NOV-2025
DEFINITION  nitric oxide-associated protein 1 [Homo sapiens].
ACCESSION   NP_115689
VERSION     NP_115689.1
DBSOURCE    REFSEQ: accession NM_032313.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 698)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 698)
  AUTHORS   Harper,N.J., Burnside,C. and Klinge,S.
  TITLE     Principles of mitoribosomal small subunit assembly in eukaryotes
  JOURNAL   Nature 614 (7946), 175-181 (2023)
   PUBMED   36482135
REFERENCE   3  (residues 1 to 698)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 698)
  AUTHORS   Al-Furoukh,N., Kardon,J.R., Kruger,M., Szibor,M., Baker,T.A. and
            Braun,T.
  TITLE     NOA1, a novel ClpXP substrate, takes an unexpected nuclear detour
            prior to mitochondrial import
  JOURNAL   PLoS One 9 (7), e103141 (2014)
   PUBMED   25072814
  REMARK    GeneRIF: Our results uncovered an unexpected, mandatory detour of
            NOA1 through the nucleolus before uptake into mitochondria.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 698)
  AUTHORS   He,J., Cooper,H.M., Reyes,A., Di Re,M., Kazak,L., Wood,S.R.,
            Mao,C.C., Fearnley,I.M., Walker,J.E. and Holt,I.J.
  TITLE     Human C4orf14 interacts with the mitochondrial nucleoid and is
            involved in the biogenesis of the small mitochondrial ribosomal
            subunit
  JOURNAL   Nucleic Acids Res 40 (13), 6097-6108 (2012)
   PUBMED   22447445
  REMARK    GeneRIF: This study indicates rhat C4orf14 is involved in 28S
            subunit biogenesis and mtDNA maintenance.
REFERENCE   6  (residues 1 to 698)
  AUTHORS   Arakawa,S., Takahashi,A., Ashikawa,K., Hosono,N., Aoi,T.,
            Yasuda,M., Oshima,Y., Yoshida,S., Enaida,H., Tsuchihashi,T.,
            Mori,K., Honda,S., Negi,A., Arakawa,A., Kadonosono,K., Kiyohara,Y.,
            Kamatani,N., Nakamura,Y., Ishibashi,T. and Kubo,M.
  TITLE     Genome-wide association study identifies two susceptibility loci
            for exudative age-related macular degeneration in the Japanese
            population
  JOURNAL   Nat Genet 43 (10), 1001-1004 (2011)
   PUBMED   21909106
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 698)
  AUTHORS   Gu,J., Ye,Y., Spitz,M.R., Lin,J., Kiemeney,L.A., Xing,J.,
            Hildebrandt,M.A., Ki Hong,W., Amos,C.I. and Wu,X.
  TITLE     A genetic variant near the PMAIP1/Noxa gene is associated with
            increased bleomycin sensitivity
  JOURNAL   Hum Mol Genet 20 (4), 820-826 (2011)
   PUBMED   21106707
REFERENCE   8  (residues 1 to 698)
  AUTHORS   Tang,T., Zheng,B., Chen,S.H., Murphy,A.N., Kudlicka,K., Zhou,H. and
            Farquhar,M.G.
  TITLE     hNOA1 interacts with complex I and DAP3 and regulates mitochondrial
            respiration and apoptosis
  JOURNAL   J Biol Chem 284 (8), 5414-5424 (2009)
   PUBMED   19103604
REFERENCE   9  (residues 1 to 698)
  AUTHORS   Parihar,A., Parihar,M.S., Chen,Z. and Ghafourifar,P.
  TITLE     mAtNOS1 induces apoptosis of human mammary adenocarcinoma cells
  JOURNAL   Life Sci 82 (21-22), 1077-1082 (2008)
   PUBMED   18456285
  REMARK    GeneRIF: The present study suggests a novel function for mAtNOS1 in
            regulating mitochondrial nitric oxide and calcium and inducing
            apoptosis of MCF-7 cells
REFERENCE   10 (residues 1 to 698)
  AUTHORS   Zemojtel,T., Kolanczyk,M., Kossler,N., Stricker,S., Lurz,R.,
            Mikula,I., Duchniewicz,M., Schuelke,M., Ghafourifar,P.,
            Martasek,P., Vingron,M. and Mundlos,S.
  TITLE     Mammalian mitochondrial nitric oxide synthase: characterization of
            a novel candidate
  JOURNAL   FEBS Lett 580 (2), 455-462 (2006)
   PUBMED   16380119
  REMARK    Erratum:[FEBS Lett. 2007 May 15;581(10):2072-3]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC004894.2 and AC069307.7.
            
            Summary: The protein encoded by this gene is a nuclear-encoded
            GTPase that functions in the mitochondrion. Upon translation, this
            protein is imported into the nucleus and then into the nucleolus
            before being exported to the mitochondrion. The encoded protein is
            required for oxygen-dependent regulation of mitochondrial
            respiratory complexes and for mitochondrial protein synthesis.
            [provided by RefSeq, Dec 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC004894.2, SRR3476690.76227.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264230.5/ ENSP00000264230.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..698
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q12"
     Protein         1..698
                     /product="nitric oxide-associated protein 1"
                     /note="putative ortholog of Arabidopsis mitochondrial
                     nitric oxide synthase; nitric oxide synthase,
                     mitochondrial (putative); mitochondrial GTPase 3 homolog"
                     /calculated_mol_wt=78327
     Region          42..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC60.2)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8NC60.2)"
     Region          80..134
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC60.2)"
     Region          141..660
                     /region_name="GTPase_YqeH"
                     /note="ribosome biogenesis GTPase YqeH; TIGR03597"
                     /db_xref="CDD:213834"
     Region          179..394
                     /region_name="YqeH"
                     /note="Circularly permuted YqeH GTPase; cd01855"
                     /db_xref="CDD:206748"
     Site            order(248..249,251..252,317..319,347..353)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206748"
     Site            248..251
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206748"
     Region          279..306
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NC60.2)"
     Site            317..319
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206748"
     Site            345..352
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206748"
     Site            381..388
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206748"
     Site            383
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206748"
     CDS             1..698
                     /gene="NOA1"
                     /gene_synonym="C4orf14; hAtNOS1; hNOA1; mAtNOS1; MTG3"
                     /coded_by="NM_032313.4:22..2118"
                     /db_xref="CCDS:CCDS3510.1"
                     /db_xref="GeneID:84273"
                     /db_xref="HGNC:HGNC:28473"
                     /db_xref="MIM:614919"
ORIGIN      
        1 mlparlpfrl lslflrgsap taarhglrep llerrcaaas sfqhssslgr elpydpvdte
       61 gfgeggdmqe rflfpeyild pepqptrekq lqelqqqqee eerqrqqrre errqqnlrar
      121 srehpvvghp dpalppsgvn csgcgaelhc qdagvpgylp rekflrtaea dgglartvcq
      181 rcwllshhrr alrlqvsreq ylelvsaalr rpgpslvlym vdlldlpdal lpdlpalvgp
      241 kqlivlgnkv dllpqdapgy rqrlrerlwe dcaragllla pghqgpqrpv kdepqdgenp
      301 nppnwsrtvv rdvrlisakt gygveelisa lqrswryrgd vylvgatnag kstlfntlle
      361 sdyctakgse aidratispw pgttlnllkf picnptpyrm fkrhqrlkkd stqaeedlse
      421 qeqnqlnvlk khgyvvgrvg rtflyseeqk dnipfefdad slafdmendp vmgthkstkq
      481 veltaqdvkd ahwfydtpgi tkencilnll tekevnivlp tqsivprtfv lkpgmvlflg
      541 aigridflqg nqsawftvva snilpvhits ldradalyqk haghtllqip mggkermagf
      601 pplvaediml keglgaseav adikfssagw vsvtpnfkdr lhlrgytpeg tvltvrppll
      661 pyivnikgqr ikksvayktk kppslmynvr kkkgkinv
//
LOCUS       NP_001354615             729 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ww [Homo sapiens].
ACCESSION   NP_001354615
VERSION     NP_001354615.1
DBSOURCE    REFSEQ: accession NM_001367686.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.76869.1,
                                           SRR1803614.44861.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..729
                     /product="SUN domain-containing protein 1 isoform ww"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=80852
     Region          12..236
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <309..>533
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          361..414
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(361,364..365,368,371..372,375..376,378..379,
                     382..383,385..386,389..390,392..393,396,399..400,403,
                     406..407,410..411,413..414)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          491..549
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          592..727
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..729
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367686.1:105..2294"
                     /note="isoform ww is encoded by transcript variant 49"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqks hasyygrmnv
      181 revlredghl svngealwka asgvfwwlgi gwyqfvtlis wlnvflltrc lrnickflvl
      241 liplflllgl slrgqgnffs flpvlnwasm hrtqrvddpq dvfkpttsrl kqplqgdsea
      301 fpwhwmsgve qqvaslsgqc hhhgenlrel ttllqklqar vdqmeggaag psasvrdavg
      361 qppretdfma fhqehevrms hledilgklr ekseaiqkel eqtkqktisa vgeqllptve
      421 hlqleldqlk selsswrhvk tgcetvdavq ervdvqvrem vkllfsedqq ggsleqllqr
      481 fssqfvskgd lqtmlrdlql qilrnvthhv svtkqlptse avvsavseag asgiteaqar
      541 aivnsalkly sqdktgmvdf alesgggsil strcsetyet ktalmslfgi plwyfsqspr
      601 vviqpdiypg ncwafkgsqg ylvvrlsmmi hpaaftlehi pktlsptgni ssapkdfavy
      661 gleneyqeeg qllgqftydq dgeslqmfqa lkrpddtafq ivelrifsnw ghpeytclyr
      721 frvhgepvk
//
LOCUS       NP_001137359             450 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001137359
VERSION     NP_001137359.1
DBSOURCE    REFSEQ: accession NM_001143887.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Dressel,U., Thormeyer,D., Altincicek,B., Paululat,A., Eggert,M.,
            Schneider,S., Tenbaum,S.P., Renkawitz,R. and Baniahmad,A.
  TITLE     Alien, a highly conserved protein with characteristics of a
            corepressor for members of the nuclear hormone receptor superfamily
  JOURNAL   Mol Cell Biol 19 (5), 3383-3394 (1999)
   PUBMED   10207062
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Schaefer,L., Beermann,M.L. and Miller,J.B.
  TITLE     Coding sequence, genomic organization, chromosomal localization,
            and expression pattern of the signalosome component Cops2: the
            mouse homologue of Drosophila alien
  JOURNAL   Genomics 56 (3), 310-316 (1999)
   PUBMED   10087198
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB059510.1, AB209799.1, BX648602.1, CN281648.1, BM667648.1 and
            AC013452.9.
            
            Transcript Variant: This variant (2) represents the longer
            transcript and encodes the longer isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.14374.1,
                                           SRR1803616.197929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..450
                     /product="COP9 signalosome complex subunit 2 isoform 2"
                     /note="COP9 signalosome complex subunit 2; JAB1-containing
                     signalosome subunit 2; TRIP-15; alien homolog;
                     TR-interacting protein 15; thyroid receptor-interacting
                     protein 15; COP9 constitutive photomorphogenic homolog
                     subunit 2"
                     /calculated_mol_wt=52274
     Region          40..441
                     /region_name="RPN6"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5159"
                     /db_xref="CDD:227488"
     Region          316..420
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..450
                     /gene="COPS2"
                     /gene_synonym="ALIEN; CSN2; SGN2; TRIP15"
                     /coded_by="NM_001143887.2:22..1374"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45257.1"
                     /db_xref="GeneID:9318"
                     /db_xref="HGNC:HGNC:30747"
                     /db_xref="MIM:604508"
ORIGIN      
        1 msdmeddfmc ddeedydley sedsnsepnv dlenqyynsk alkeddpkaa lssfqkvlel
       61 egekgewgfk alkqmikinf kltnfpemmn rykqlltyir savtrnysek sinsildyis
      121 tskqnsdflc qmdllqefye ttlealkdak ndrlwfktnt klgklylere eygklqkilr
      181 qlhqscqtdd geddlkkgtq lleiyaleiq mytaqknnkk lkalyeqslh iksaiphpli
      241 mgvirecggk mhlregefek ahtdffeafk nydesgsprr ttclkylvla nmlmksginp
      301 fdsqeakpyk ndpeilamtn lvsayqnndi tefekilktn hsnimddpfi rehieellrn
      361 irtqvlikli kpytrihipf iskelnidva dvesllvqci ldntihgrid qvnqlleldh
      421 qkrggaryta ldkwtnqlns lnqavvskla
//
LOCUS       NP_001300822             215 aa            linear   PRI 20-NOV-2025
DEFINITION  high mobility group protein B1 isoform 1 [Homo sapiens].
ACCESSION   NP_001300822
VERSION     NP_001300822.1
DBSOURCE    REFSEQ: accession NM_001313893.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 215)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK122825.1 and AL353648.27.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK122825.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA2146411,
                                           SAMEA2149004 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..215
                     /product="high mobility group protein B1 isoform 1"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=24763
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..163
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156,159,162..163)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          150..183
                     /region_name="Binding to AGER/RAGE.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          161..215
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            172
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            173
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          178..184
                     /region_name="Nuclear localization signal (NLS) 2.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            182
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            183
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            184
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            185
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..215
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001313893.1:942..1589"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9335.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekdia ayrakgkpda akkgvvkaek
      181 skkkkeeeed eedeedeeee edeededeee dddde
//
LOCUS       NP_001278768             390 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 6 [Homo sapiens].
ACCESSION   NP_001278768
VERSION     NP_001278768.1
DBSOURCE    REFSEQ: accession NM_001291839.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 390)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 390)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC233268.2, DC391353.1,
            BC018349.1 and JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (Ik-4) differs in the 5' UTR, and
            lacks an alternate in-frame exon in both the 5' and central coding
            regions, compared to variant 1. The encoded isoform (6, also known
            as Ik-4 as described in PMID:12937159), is shorter than isoform 1.
            This isoform contains only two N-terminal zinc finger motifs, and
            represents a non-DNA-binding, dominant-negative isoform
            (PMID:9892693).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074968.1887252.1,
                                           SRR14372080.2502912.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..390
                     /product="DNA-binding protein Ikaros isoform 6"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=43335
     Region          <1..>112
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q03267; propagated from
                     UniProtKB/Swiss-Prot (Q13422.1)"
     Region          58..80
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     Region          60..80
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          72..97
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          88..108
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..390
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291839.2:66..1238"
                     /note="isoform 6 is encoded by transcript variant Ik-4"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvgerpfqc
       61 nqcgasftqk gnllrhiklh sgekpfkchl cnyacrrrda ltghlrthsv ikeetnhsem
      121 aedlckigse rslvldrlas nvakrkssmp qkflgdkgls dtpydssasy ekenemmksh
      181 vmdqainnai nylgaeslrp lvqtppggse vvpvispmyq lhkplaegtp rsnhsaqdsa
      241 venllllska klvpsereas psnscqdstd tesnneeqrs gliyltnhia pharnglslk
      301 eehraydllr aasensqdal rvvstsgeqm kvykcehcrv lfldhvmyti hmgchgfrdp
      361 fecnmcgyhs qdryefsshi trgehrfhms
//
LOCUS       NP_705614                551 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor E isoform 2 [Homo sapiens].
ACCESSION   NP_705614 XP_005264933
VERSION     NP_705614.1
DBSOURCE    REFSEQ: accession NM_153481.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 551)
  AUTHORS   Wang,J., Wang,X., Wang,M., Wang,J., Wu,Y. and Qi,X.
  TITLE     Clinical significance of Interleukin 17 receptor E in diabetic
            nephropathy
  JOURNAL   Int Immunopharmacol 120, 110324 (2023)
   PUBMED   37235960
  REMARK    GeneRIF: Clinical significance of Interleukin 17 receptor E in
            diabetic nephropathy.
REFERENCE   2  (residues 1 to 551)
  AUTHORS   Jiang,Y., Wang,L., Peng,Y., Qin,J., Tan,A. and Wang,S.
  TITLE     Interleukin 17 receptor E identifies heterogeneous T helper 17
            cells in peritoneal fluid of moderate and severe endometriosis
            patients
  JOURNAL   Clin Exp Immunol 207 (3), 360-369 (2022)
   PUBMED   35553626
  REMARK    GeneRIF: Interleukin 17 receptor E identifies heterogeneous T
            helper 17 cells in peritoneal fluid of moderate and severe
            endometriosis patients.
REFERENCE   3  (residues 1 to 551)
  AUTHORS   Swedik,S., Madola,A. and Levine,A.
  TITLE     IL-17C in human mucosal immunity: More than just a middle child
  JOURNAL   Cytokine 146, 155641 (2021)
   PUBMED   34293699
  REMARK    Review article
REFERENCE   4  (residues 1 to 551)
  AUTHORS   Barati,M., Sinaeian,M., Shokrollahi Barough,M., Pak,F., Semnani,V.,
            Kokhaei,P. and Momtazi-Borojeni,A.A.
  TITLE     Evaluation of Interleukin 25 and Interleukin 25 Receptor Expression
            in Peripheral Blood Mononuclear Cells of Breast Cancer Patients and
            Normal Subjects
  JOURNAL   J Interferon Cytokine Res 40 (3), 139-144 (2020)
   PUBMED   31905037
  REMARK    GeneRIF: Evaluation of Interleukin 25 and Interleukin 25 Receptor
            Expression in Peripheral Blood Mononuclear Cells of Breast Cancer
            Patients and Normal Subjects.
REFERENCE   5  (residues 1 to 551)
  AUTHORS   Nies,J.F. and Panzer,U.
  TITLE     IL-17C/IL-17RE: Emergence of a Unique Axis in TH17 Biology
  JOURNAL   Front Immunol 11, 341 (2020)
   PUBMED   32174926
  REMARK    GeneRIF: IL-17C/IL-17RE: Emergence of a Unique Axis in TH17
            Biology.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 551)
  AUTHORS   Wu,B., Jin,M., Zhang,Y., Wei,T. and Bai,Z.
  TITLE     Evolution of the IL17 receptor family in chordates: a new subfamily
            IL17REL
  JOURNAL   Immunogenetics 63 (12), 835-845 (2011)
   PUBMED   21732179
REFERENCE   7  (residues 1 to 551)
  AUTHORS   Chang,S.H., Reynolds,J.M., Pappu,B.P., Chen,G., Martinez,G.J. and
            Dong,C.
  TITLE     Interleukin-17C promotes Th17 cell responses and autoimmune disease
            via interleukin-17 receptor E
  JOURNAL   Immunity 35 (4), 611-621 (2011)
   PUBMED   21982598
REFERENCE   8  (residues 1 to 551)
  AUTHORS   Song,X., Zhu,S., Shi,P., Liu,Y., Shi,Y., Levin,S.D. and Qian,Y.
  TITLE     IL-17RE is the functional receptor for IL-17C and mediates mucosal
            immunity to infection with intestinal pathogens
  JOURNAL   Nat Immunol 12 (12), 1151-1158 (2011)
   PUBMED   21993849
  REMARK    GeneRIF: IL-17RE as a receptor of IL-17C that regulates early
            innate immunity to intestinal pathogens.
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 551)
  AUTHORS   Ramirez-Carrozzi,V., Sambandam,A., Luis,E., Lin,Z., Jeet,S.,
            Lesch,J., Hackney,J., Kim,J., Zhou,M., Lai,J., Modrusan,Z., Sai,T.,
            Lee,W., Xu,M., Caplazi,P., Diehl,L., de Voss,J., Balazs,M.,
            Gonzalez,L. Jr., Singh,H., Ouyang,W. and Pappu,R.
  TITLE     IL-17C regulates the innate immune function of epithelial cells in
            an autocrine manner
  JOURNAL   Nat Immunol 12 (12), 1159-1166 (2011)
   PUBMED   21993848
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 551)
  AUTHORS   Li,T.S., Li,X.N., Chang,Z.J., Fu,X.Y. and Liu,L.
  TITLE     Identification and functional characterization of a novel
            interleukin 17 receptor: a possible mitogenic activation through
            ras/mitogen-activated protein kinase signaling pathway
  JOURNAL   Cell Signal 18 (8), 1287-1298 (2006)
   PUBMED   16310341
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096801.1, BC137077.1 and
            AK074238.1.
            
            On Sep 12, 2013 this sequence version replaced XP_005264933.1.
            
            Summary: This gene encodes a transmembrane protein that functions
            as the receptor for interleukin-17C. The encoded protein signals to
            downstream components of the mitogen activated protein kinase
            (MAPK) pathway. Activity of this protein is important in the immune
            response to bacterial pathogens. Alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Sep 2013].
            
            Transcript Variant: This variant (2) lacks a portion of the 5'
            coding region and initiates translation at a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (2) has a
            shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096801.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..551
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..551
                     /product="interleukin-17 receptor E isoform 2"
                     /note="IL-17 receptor E"
                     /calculated_mol_wt=61527
     Region          1..332
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          372..495
                     /region_name="SEFIR"
                     /note="SEFIR domain; cl23749"
                     /db_xref="CDD:474043"
     CDS             1..551
                     /gene="IL17RE"
                     /coded_by="NM_153481.2:298..1953"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:132014"
                     /db_xref="HGNC:HGNC:18439"
                     /db_xref="MIM:614995"
ORIGIN      
        1 mpapaqrkll prrhlseksh hisipspdis hkglrskrtq psdpetwesl prldsqrhgg
       61 pefsfdllpe arairvtiss gpevsvrlch qwaleceels spydvqkivs gghtvelpye
      121 fllpclciea sylqedtvrr kkcpfqswpe aygsdfwksv hftdysqhtq mvmaltlrcp
      181 lkleaalcqr hdwhtlckdl pnataresdg wyvlekvdlh pqlcfkfsfg nsshvecphq
      241 tgsltswnvs mdtqaqqlil hfssrmhatf saawslpglg qdtlvppvyt vsqargsspv
      301 sldliipflr pgccvlvwrs dvqfawkhll cpdvsyrhlg llilallall tllgvvlalt
      361 crrpqsgpgp arpvlllhaa dseaqrrlvg alaellraal gggrdvivdl wegrhvarvg
      421 plpwlwaart rvareqgtvl llwsgadlrp vsgpdpraap llallhaapr pllllayfsr
      481 lcakgdippp lralpryrll rdlprllral darpfaeats wgrlgarqrr qsrlelcsrl
      541 ereaarladl g
//
LOCUS       NP_001339886             504 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 23 [Homo sapiens].
ACCESSION   NP_001339886 XP_016868779
VERSION     NP_001339886.1
DBSOURCE    REFSEQ: accession NM_001352957.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 504)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 504)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 504)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 504)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 504)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 504)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 504)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 504)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 504)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 504)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868779.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.2059808.1,
                                           SRR1660805.85035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..504
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..504
                     /product="DNA repair-scaffolding protein isoform 23"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=54759
     Region          <1..58
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          210..>503
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..504
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352957.1:663..2177"
                     /note="isoform 23 is encoded by transcript variant 31"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mqvamceqll gspatsssqs vaprpgaglk vlftketagy lrgrpqdtvr ifppwqklii
       61 psgscpviln tyfcekvvak edsektcevy cpdiplprrs islaqmfvik gltnnspeiq
      121 vvcsgvattg tawthghkea kqriptstpl rdslldvves qgaaswpgag vrvvvqrvys
      181 lpsrdstrgq qgassghtdp agtracllvq dacgmfgevh leftmskarq legkscslvg
      241 mkvlqkvtrg rtagifslid tlwppaiplk tpgrdqpcee ikthlpppal cyiltahpnl
      301 gqidiidedp iyklyqppvt rclrdilqmn dlgtrcsfya tviyqkpqlk slllleqrei
      361 wllvtdvtlq tkeerdprlp ktllvyvapl cvlgsevlea lagaaphslf fkdalrdqgr
      421 ivcaertvll lqkpllsvvs gasscelpgp vmldsldsat pvnsicsvqg tvvgvdesta
      481 fswpvcdmcg ngrleqrped ratk
//
LOCUS       NP_001356337             323 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA excision repair protein ERCC-1 isoform 1 [Homo sapiens].
ACCESSION   NP_001356337 XP_005258692
VERSION     NP_001356337.1
DBSOURCE    REFSEQ: accession NM_001369408.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Khalouei,A., Masoumi-Ardakani,Y., Jafarzaheh,A., Kalantari
            Khandani,B., Sedghy,F., Khosravi Mashizi,A., Yaghoobi,M.M.,
            Zangouey,M. and Shahouzehi,B.
  TITLE     Association of ERCC1 Gene Polymorphisms (rs3212986 and rs11615)
            With the Risk of Lung Cancer in a Population From Southeast Iran
  JOURNAL   J Res Health Sci 24 (4), e00631 (2024)
   PUBMED   39431656
  REMARK    GeneRIF: Association of ERCC1 Gene Polymorphisms (rs3212986 and
            rs11615) With the Risk of Lung Cancer in a Population From
            Southeast Iran.
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Imani,M.M., Akbari,S., Shalchi,M., Sadeghi,E. and Sadeghi,M.
  TITLE     Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis
  JOURNAL   Arch Oral Biol 162, 105955 (2024)
   PUBMED   38479279
  REMARK    GeneRIF: Relationship between ERCC1 and XPC polymorphisms and the
            susceptibility to head and neck carcinoma: A systematic review,
            meta-analysis, and trial sequential analysis.
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Jamai,D., Gargouri,R., Selmi,B. and Khabir,A.
  TITLE     ERCC1 and MGMT Methylation as a Predictive Marker of Relapse and
            FOLFOX Response in Colorectal Cancer Patients from South Tunisia
  JOURNAL   Genes (Basel) 14 (7), 1467 (2023)
   PUBMED   37510370
  REMARK    GeneRIF: ERCC1 and MGMT Methylation as a Predictive Marker of
            Relapse and FOLFOX Response in Colorectal Cancer Patients from
            South Tunisia.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Kraemer,K.H., DiGiovanna,J.J. and Tamura,D.
  TITLE     Xeroderma Pigmentosum
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301571
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Liu,P., Perryman,M.B., Liao,W. and Siciliano,M.J.
  TITLE     Efficiency and limitations of the hn-cDNA library approach for the
            isolation of human transcribed genes from hybrid cells
  JOURNAL   Somat Cell Mol Genet 18 (1), 7-18 (1992)
   PUBMED   1372133
REFERENCE   7  (residues 1 to 323)
  AUTHORS   van Duin,M., van Den Tol,J., Hoeijmakers,J.H., Bootsma,D.,
            Rupp,I.P., Reynolds,P., Prakash,L. and Prakash,S.
  TITLE     Conserved pattern of antisense overlapping transcription in the
            homologous human ERCC-1 and yeast RAD10 DNA repair gene regions
  JOURNAL   Mol Cell Biol 9 (4), 1794-1798 (1989)
   PUBMED   2471070
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Hoeijmakers,J.H.
  TITLE     Characterization of genes and proteins involved in excision repair
            of human cells
  JOURNAL   J Cell Sci Suppl 6, 111-125 (1987)
   PUBMED   2821019
REFERENCE   9  (residues 1 to 323)
  AUTHORS   van Duin,M., de Wit,J., Odijk,H., Westerveld,A., Yasui,A.,
            Koken,M.H., Hoeijmakers,J.H. and Bootsma,D.
  TITLE     Molecular characterization of the human excision repair gene
            ERCC-1: cDNA cloning and amino acid homology with the yeast DNA
            repair gene RAD10
  JOURNAL   Cell 44 (6), 913-923 (1986)
   PUBMED   2420469
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Westerveld,A., Hoeijmakers,J.H., van Duin,M., de Wit,J., Odijk,H.,
            Pastink,A., Wood,R.D. and Bootsma,D.
  TITLE     Molecular cloning of a human DNA repair gene
  JOURNAL   Nature 310 (5976), 425-429 (1984)
   PUBMED   6462228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC139353.3.
            
            On Apr 9, 2019 this sequence version replaced XP_005258692.1.
            
            Summary: The product of this gene functions in the nucleotide
            excision repair pathway, and is required for the repair of DNA
            lesions such as those induced by UV light or formed by
            electrophilic compounds including cisplatin. The encoded protein
            forms a heterodimer with the XPF endonuclease (also known as
            ERCC4), and the heterodimeric endonuclease catalyzes the 5'
            incision in the process of excising the DNA lesion. The
            heterodimeric endonuclease is also involved in recombinational DNA
            repair and in the repair of inter-strand crosslinks. Mutations in
            this gene result in cerebrooculofacioskeletal syndrome, and
            polymorphisms that alter expression of this gene may play a role in
            carcinogenesis. Multiple transcript variants encoding different
            isoforms have been found for this gene. The last exon of this gene
            overlaps with the CD3e molecule, epsilon associated protein gene on
            the opposite strand. [provided by RefSeq, Oct 2009].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1159961.1,
                                           SRR1803612.211387.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.32"
     Protein         1..323
                     /product="DNA excision repair protein ERCC-1 isoform 1"
                     /note="DNA excision repair protein ERCC-1; excision repair
                     cross-complementation group 1; excision repair
                     cross-complementing rodent repair deficiency,
                     complementation group 1 (includes overlapping antisense
                     sequence)"
                     /calculated_mol_wt=35432
     Region          1..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P07992.1)"
     Region          17..23
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P07992.1)"
     Region          99..226
                     /region_name="ERCC1_C-like"
                     /note="Central domain of ERCC1; cd22325"
                     /db_xref="CDD:411729"
     Site            order(117..119,166,179,183,186,189..190,193..198,200,204,
                     207..208,210..212,214..216,218..219,221..222)
                     /site_type="other"
                     /note="XPF interaction interface [polypeptide binding]"
                     /db_xref="CDD:411729"
     Region          <250..>281
                     /region_name="PRK00024"
                     /note="DNA repair protein RadC"
                     /db_xref="CDD:178801"
     CDS             1..323
                     /gene="ERCC1"
                     /gene_synonym="COFS4; RAD10; UV20"
                     /coded_by="NM_001369408.1:103..1074"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS12663.1"
                     /db_xref="GeneID:2067"
                     /db_xref="HGNC:HGNC:3433"
                     /db_xref="MIM:126380"
ORIGIN      
        1 mdpgkdkegv pqpsgppark kfvipldede vppgvakplf rstqslptvd tsaqaapqty
       61 aeyaisqple gagatcptgs eplagetpnq alkpgaksns iivsprqrgn pvlkfvrnvp
      121 wefgdvipdy vlgqstcalf lslryhnlhp dyihgrlqsl gknfalrvll vqvdvkdpqq
      181 alkelakmci ladctlilaw speeagryle tykayeqkpa dllmekleqd fvsrvteclt
      241 tvksvnktds qtllttfgsl eqliaasred lalcpglgpq kvralgknpr swgkerapnk
      301 hnlrpqsfkv kkepktrhsg frl
//
LOCUS       NP_001341012             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341012 XP_005256217
VERSION     NP_001341012.1
DBSOURCE    REFSEQ: accession NM_001354083.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 29, 2017 this sequence version replaced XP_005256217.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.44381.1,
                                           SRR1803611.112977.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354083.2:231..995"
                     /note="isoform a is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001354624             759 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform fff [Homo sapiens].
ACCESSION   NP_001354624
VERSION     NP_001354624.1
DBSOURCE    REFSEQ: accession NM_001367695.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 759)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 759)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 759)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 759)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 759)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 759)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 759)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 759)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 759)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 759)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2157437
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..759
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..759
                     /product="SUN domain-containing protein 1 isoform fff"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=84406
     Region          24..265
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          391..444
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(391,394..395,398,401..402,405..406,408..409,
                     412..413,415..416,419..420,422..423,426,429..430,433,
                     436..437,440..441,443..444)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          403..>536
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          521..579
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          622..757
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..759
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367695.1:52..2331"
                     /note="isoform fff is encoded by transcript variant 58"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalrttkq rrstnksafs inhvsrqvts sgvshggtvs
       61 lqdavtrrpp vldeswireq ttvdhfwgld ddgdlkggnk aaiqgngdvg aaaatahngf
      121 scsncsmlse rkdvltahpa apgpvsrvys rdrnqkcddc kgkrhldaht aahsqsprlp
      181 gragtlwhiw acagyfllqi lrrigavgqa vsrtawsalw lavvapgkaa sgvfwwlgig
      241 wyqfvtlisw lnvflltrcl rnickflvll iplflllagl slrgqgnffs flpvlnwasm
      301 hrtqrvddpq dvfkpttsrl kqplqgdsea fpwhwmsgve qqvaslsgqc hhhgenlrel
      361 ttllqklqar vdqmeggaag psasvrdavg qppretdfma fhqehevrms hledilgklr
      421 ekseaiqkel eqtkqktisa vgeqllptve hlqleldqlk selsswrhvk tgcetvdavq
      481 ervdvqvrem vkllfsedqq ggsleqllqr fssqfvskgd lqtmlrdlql qilrnvthhv
      541 svtkqlptse avvsavseag asgiteaqar aivnsalkly sqdktgmvdf alesgggsil
      601 strcsetyet ktalmslfgi plwyfsqspr vviqpdiypg ncwafkgsqg ylvvrlsmmi
      661 hpaaftlehi pktlsptgni ssapkdfavy gleneyqeeg qllgqftydq dgeslqmfqa
      721 lkrpddtafq ivelrifsnw ghpeytclyr frvhgepvk
//
LOCUS       NP_006020                353 aa            linear   PRI 20-NOV-2025
DEFINITION  paraneoplastic antigen Ma1 [Homo sapiens].
ACCESSION   NP_006020
VERSION     NP_006020.4
DBSOURCE    REFSEQ: accession NM_006029.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Schuller,M., Jenne,D. and Voltz,R.
  TITLE     The human PNMA family: novel neuronal proteins implicated in
            paraneoplastic neurological disease
  JOURNAL   J Neuroimmunol 169 (1-2), 172-176 (2005)
   PUBMED   16214224
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Pellkofer,H., Schubart,A.S., Hoftberger,R., Schutze,N., Pagany,M.,
            Schuller,M., Lassmann,H., Hohlfeld,R., Voltz,R. and Linington,C.
  TITLE     Modelling paraneoplastic CNS disease: T-cells specific for the
            onconeuronal antigen PNMA1 mediate autoimmune encephalomyelitis in
            the rat
  JOURNAL   Brain 127 (Pt 8), 1822-1830 (2004)
   PUBMED   15201193
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Dalmau,J., Gultekin,S.H., Voltz,R., Hoard,R., DesChamps,T.,
            Balmaceda,C., Batchelor,T., Gerstner,E., Eichen,J., Frennier,J.,
            Posner,J.B. and Rosenfeld,M.R.
  TITLE     Ma1, a novel neuron- and testis-specific protein, is recognized by
            the serum of patients with paraneoplastic neurological disorders
  JOURNAL   Brain 122 (Pt 1), 27-39 (1999)
   PUBMED   10050892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG719761.1, BG700354.1, AF320308.1 and AL834327.1.
            
            On Sep 22, 2004 this sequence version replaced NP_006020.3.
            
            Summary: This gene encodes a neuron- and testis-specific protein
            that is also expressed in some paraneoplastic syndromes affecting
            the nervous system. Some patients with neurologic disorders develop
            antibodies against the protein encoded by this gene. The
            identification of the antineuronal antibodies in the sera of these
            patients has facilitated the diagnosis of paraneoplastic
            neurological disorders and the early detection of the associated
            tumors. [provided by RefSeq, Feb 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC039577.1, SRR3476690.1079711.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316836.5/ ENSP00000318914.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..353
                     /product="paraneoplastic antigen Ma1"
                     /note="paraneoplastic neuronal antigen MA1; neuron- and
                     testis-specific protein 1; 37 kDa neuronal protein;
                     paraneoplastic Ma antigen 1"
                     /calculated_mol_wt=39630
     Region          1..325
                     /region_name="PNMA"
                     /note="pfam14893"
                     /db_xref="CDD:464357"
     CDS             1..353
                     /gene="PNMA1"
                     /gene_synonym="MA1"
                     /coded_by="NM_006029.5:746..1807"
                     /db_xref="CCDS:CCDS9818.1"
                     /db_xref="GeneID:9240"
                     /db_xref="HGNC:HGNC:9158"
                     /db_xref="MIM:604010"
ORIGIN      
        1 mamtlledwc rgmdvnsqra llvwgipvnc deaeieetlq aampqvsyrm lgrmfwreen
       61 akaalleltg avdyaaipre mpgkggvwkv lfkpptsdae flerlhlfla regwtvqdva
      121 rvlgfqnptp tpgpempaem lnyildnviq plvesiwykr ltlfsgrdip gpgeetfdpw
      181 lehtnevlee wqvsdvekrr rlmeslrgpa advirilksn npaittaecl kaleqvfgsv
      241 essrdaqikf lntyqnpgek lsayvirlep llqkvvekga idkdnvnqar leqviaganh
      301 sgairrqlwl tgagegpapn lfqllvqire eeakeeeeea eatllqlgle ghf
//
LOCUS       NP_001357120              44 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor beta activator LRRC32 isoform d
            precursor [Homo sapiens].
ACCESSION   NP_001357120
VERSION     NP_001357120.1
DBSOURCE    REFSEQ: accession NM_001370191.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 44)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 44)
  AUTHORS   Ma,J., Chen,Y., Li,T., Cao,Y., Hu,B., Liu,Y., Zhang,Y., Li,X.,
            Liu,J., Zhang,W., Niu,H., Gao,J., Zhang,Z., Yue,K., Wang,J.,
            Bao,G., Wang,C., Wang,P.G., Zou,T. and Xie,S.
  TITLE     Suppression of lysosome metabolism-meditated GARP/TGF-beta1
            complexes specifically depletes regulatory T cells to inhibit
            breast cancer metastasis
  JOURNAL   Oncogene 43 (25), 1930-1940 (2024)
   PUBMED   38698265
  REMARK    GeneRIF: Suppression of lysosome metabolism-meditated
            GARP/TGF-beta1 complexes specifically depletes regulatory T cells
            to inhibit breast cancer metastasis.
REFERENCE   3  (residues 1 to 44)
  AUTHORS   Zhang,X., Sharma,P., Maschmeyer,P., Hu,Y., Lou,M., Kim,J.,
            Fujii,H., Unutmaz,D., Schwabe,R.F. and Winau,F.
  TITLE     GARP on hepatic stellate cells is essential for the development of
            liver fibrosis
  JOURNAL   J Hepatol 79 (5), 1214-1225 (2023)
   PUBMED   37348791
  REMARK    GeneRIF: GARP on hepatic stellate cells is essential for the
            development of liver fibrosis.
REFERENCE   4  (residues 1 to 44)
  AUTHORS   Cai,H., Liu,Y., Dong,X., Jiang,F., Li,H., Ouyang,S., Yin,W., He,T.,
            Zeng,Q. and Yang,H.
  TITLE     Analysis of LAP+ and GARP+ Treg subsets in peripheral blood of
            patients with neuromyelitis optica spectrum disorders
  JOURNAL   Neurol Sci 44 (5), 1739-1747 (2023)
   PUBMED   36683084
  REMARK    GeneRIF: Analysis of LAP[+] and GARP[+] Treg subsets in peripheral
            blood of patients with neuromyelitis optica spectrum disorders.
REFERENCE   5  (residues 1 to 44)
  AUTHORS   Lahimchi,M.R., Eslami,M. and Yousefi,B.
  TITLE     New insight into GARP striking role in cancer progression:
            application for cancer therapy
  JOURNAL   Med Oncol 40 (1), 33 (2022)
   PUBMED   36460874
  REMARK    GeneRIF: New insight into GARP striking role in cancer progression:
            application for cancer therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 44)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 44)
  AUTHORS   Maire,G., Forus,A., Foa,C., Bjerkehagen,B., Mainguene,C.,
            Kresse,S.H., Myklebost,O. and Pedeutour,F.
  TITLE     11q13 alterations in two cases of hibernoma: large heterozygous
            deletions and rearrangement breakpoints near GARP in 11q13.5
  JOURNAL   Genes Chromosomes Cancer 37 (4), 389-395 (2003)
   PUBMED   12800150
REFERENCE   8  (residues 1 to 44)
  AUTHORS   Roubin,R., Pizette,S., Ollendorff,V., Planche,J., Birnbaum,D. and
            Delapeyriere,O.
  TITLE     Structure and developmental expression of mouse Garp, a gene
            encoding a new leucine-rich repeat-containing protein
  JOURNAL   Int J Dev Biol 40 (3), 545-555 (1996)
   PUBMED   8840187
REFERENCE   9  (residues 1 to 44)
  AUTHORS   Ollendorff,V., Noguchi,T., deLapeyriere,O. and Birnbaum,D.
  TITLE     The GARP gene encodes a new member of the family of leucine-rich
            repeat-containing proteins
  JOURNAL   Cell Growth Differ 5 (2), 213-219 (1994)
   PUBMED   8180135
REFERENCE   10 (residues 1 to 44)
  AUTHORS   Ollendorff,V., Szepetowski,P., Mattei,M.G., Gaudray,P. and
            Birnbaum,D.
  TITLE     New gene in the homologous human 11q13-q14 and mouse 7F chromosomal
            regions
  JOURNAL   Mamm Genome 2 (3), 195-200 (1992)
   PUBMED   1543912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001189.5.
            
            Summary: This gene encodes a type I membrane protein which contains
            20 leucine-rich repeats. Alterations in the chromosomal region
            11q13-11q14 are involved in several pathologies. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AW134685.1, DRR138525.41326.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..44
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..44
                     /product="transforming growth factor beta activator LRRC32
                     isoform d precursor"
                     /note="garpin; glycoprotein A repetitions predominant;
                     leucine-rich repeat-containing protein 32; transforming
                     growth factor beta activator LRRC32"
                     /calculated_mol_wt=3067
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1849
     CDS             1..44
                     /gene="LRRC32"
                     /gene_synonym="CPPRDD; D11S833E; GARP"
                     /coded_by="NM_001370191.1:139..273"
                     /note="isoform d precursor is encoded by transcript
                     variant 7"
                     /db_xref="GeneID:2615"
                     /db_xref="HGNC:HGNC:4161"
                     /db_xref="MIM:137207"
ORIGIN      
        1 mrpqilllla lltlglaaqh qdkvpckmvk sltqmtpiph tmes
//
LOCUS       NP_001354863            1209 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase ID isoform c [Homo sapiens].
ACCESSION   NP_001354863
VERSION     NP_001354863.1
DBSOURCE    REFSEQ: accession NM_001367934.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1209)
  AUTHORS   Honsho,M., Mawatari,S. and Fujiki,Y.
  TITLE     ATP8B2-Mediated Asymmetric Distribution of Plasmalogens Regulates
            Plasmalogen Homeostasis and Plays a Role in Intracellular Signaling
  JOURNAL   Front Mol Biosci 9, 915457 (2022)
   PUBMED   35832735
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1209)
  AUTHORS   Ansari,I.U., Longacre,M.J., Paulusma,C.C., Stoker,S.W.,
            Kendrick,M.A. and MacDonald,M.J.
  TITLE     Characterization of P4 ATPase Phospholipid Translocases (Flippases)
            in Human and Rat Pancreatic Beta Cells: THEIR GENE SILENCING
            INHIBITS INSULIN SECRETION
  JOURNAL   J Biol Chem 290 (38), 23110-23123 (2015)
   PUBMED   26240149
  REMARK    GeneRIF: the predominant P4 ATPases in pure pancreatic beta cells
            and human and rat pancreatic islets were ATP8B1, ATP8B2, and ATP9A.
            ATP8B1 and CDC50A were highly concentrated in ISG
REFERENCE   3  (residues 1 to 1209)
  AUTHORS   Takatsu,H., Tanaka,G., Segawa,K., Suzuki,J., Nagata,S., Nakayama,K.
            and Shin,H.W.
  TITLE     Phospholipid flippase activities and substrate specificities of
            human type IV P-type ATPases localized to the plasma membrane
  JOURNAL   J Biol Chem 289 (48), 33543-33556 (2014)
   PUBMED   25315773
  REMARK    Erratum:[J Biol Chem. 2016 Oct 7;291(41):21421. doi:
            10.1074/jbc.A114.593012. PMID: 27825076]
REFERENCE   4  (residues 1 to 1209)
  AUTHORS   Bryde,S., Hennrich,H., Verhulst,P.M., Devaux,P.F., Lenoir,G. and
            Holthuis,J.C.
  TITLE     CDC50 proteins are critical components of the human class-1
            P4-ATPase transport machinery
  JOURNAL   J Biol Chem 285 (52), 40562-40572 (2010)
   PUBMED   20961850
REFERENCE   5  (residues 1 to 1209)
  AUTHORS   van der Velden,L.M., Wichers,C.G., van Breevoort,A.E.,
            Coleman,J.A., Molday,R.S., Berger,R., Klomp,L.W. and van de
            Graaf,S.F.
  TITLE     Heteromeric interactions required for abundance and subcellular
            localization of human CDC50 proteins and class 1 P4-ATPases
  JOURNAL   J Biol Chem 285 (51), 40088-40096 (2010)
   PUBMED   20947505
REFERENCE   6  (residues 1 to 1209)
  AUTHORS   Paulusma,C.C. and Oude Elferink,R.P.
  TITLE     The type 4 subfamily of P-type ATPases, putative aminophospholipid
            translocases with a role in human disease
  JOURNAL   Biochim Biophys Acta 1741 (1-2), 11-24 (2005)
   PUBMED   15919184
  REMARK    Review article
REFERENCE   7  (residues 1 to 1209)
  AUTHORS   Kuhlbrandt,W.
  TITLE     Biology, structure and mechanism of P-type ATPases
  JOURNAL   Nat Rev Mol Cell Biol 5 (4), 282-295 (2004)
   PUBMED   15071553
  REMARK    Review article
REFERENCE   8  (residues 1 to 1209)
  AUTHORS   Harris,M.J. and Arias,I.M.
  TITLE     FIC1, a P-type ATPase linked to cholestatic liver disease, has
            homologues (ATP8B2 and ATP8B3) expressed throughout the body
  JOURNAL   Biochim Biophys Acta 1633 (2), 127-131 (2003)
   PUBMED   12880872
REFERENCE   9  (residues 1 to 1209)
  AUTHORS   Halleck,M.S., Lawler,J.F. Jr., Blackshaw,S., Gao,L., Nagarajan,P.,
            Hacker,C., Pyle,S., Newman,J.T., Nakanishi,Y., Ando,H.,
            Weinstock,D., Williamson,P. and Schlegel,R.A.
  TITLE     Differential expression of putative transbilayer amphipath
            transporters
  JOURNAL   Physiol Genomics 1 (3), 139-150 (1999)
   PUBMED   11015572
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1209)
  AUTHORS   Abbott,W.M., Mellor,A., Edwards,Y. and Feizi,T.
  TITLE     Soluble bovine galactose-binding lectin. cDNA cloning reveals the
            complete amino acid sequence and an antigenic relationship with the
            major encephalitogenic domain of myelin basic protein
  JOURNAL   Biochem J 259 (1), 283-290 (1989)
   PUBMED   2470348
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162591.16.
            
            Summary: The protein encoded by this gene belongs to the family of
            P-type cation transport ATPases, and to the subfamily of
            aminophospholipid-transporting ATPases. The aminophospholipid
            translocases transport phosphatidylserine and
            phosphatidylethanolamine from one side of a bilayer to another.
            Alternatively spliced transcript variants encoding different
            isoforms have been identified. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.216292.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..1209
                     /product="phospholipid-transporting ATPase ID isoform c"
                     /EC_number="7.6.2.1"
                     /note="phospholipid-transporting ATPase ID; probable
                     phospholipid-transporting ATPase ID; ATPase, class I, type
                     8B, member 2; P4-ATPase flippase complex alpha subunit
                     ATP8B2; 36/8-9 fusion protein with epitope for anti-lectin
                     antibody; ATPase, aminophospholipid transporter, class I,
                     type 8B, member 2"
                     /calculated_mol_wt=137310
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Region          50..991
                     /region_name="P-type_ATPase_APLT_Dnf-like"
                     /note="Aminophospholipid translocases (APLTs), similar to
                     Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2,
                     -10D, -11B, -11C; cd02073"
                     /db_xref="CDD:319770"
     Site            65..86
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            93..112
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            296..317
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            347..368
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            order(411..413,556,579..581,646,693..695,807,810,813,833,
                     836)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:319770"
     Site            411..417
                     /site_type="other"
                     /note="P-type ATPase signature motif"
                     /db_xref="CDD:319770"
     Site            411
                     /site_type="phosphorylation"
                     /note="phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:319770"
     Site            890..910
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            923..942
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            973..994
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1009..1031
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1038..1058
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1079..1103
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     Site            1175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P98198.2)"
     Region          1181..1209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P98198.2)"
     CDS             1..1209
                     /gene="ATP8B2"
                     /gene_synonym="ATPID"
                     /coded_by="NM_001367934.1:191..3820"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS91062.1"
                     /db_xref="GeneID:57198"
                     /db_xref="HGNC:HGNC:13534"
                     /db_xref="MIM:605867"
ORIGIN      
        1 mtvpkempek waraqappsw srkkpswgte eerrarandr eynekfqyas nciktskyni
       61 ltflpvnlfe qfqevantyf lfllilqlip qisslswftt ivplvlvlti tavkdatddy
      121 frhksdnqvn nrqsqvling ilqqeqwmnv cvgdiiklen nqfvaadlll lsssephglc
      181 yietaeldge tnmkvrqaip vtselgdisk lakfdgevic eppnnkldkf sgtlywkenk
      241 fplsnqnmll rgcvlrntew cfglvifagp dtklmqnsgr tkfkrtsidr lmntlvlwif
      301 gflvcmgvil aignaiwehe vgmrfqvylp wdeavdsaff sgflsfwsyi iilntvvpis
      361 lyvsvevirl ghsyfinwdk kmfcmkkrtp aeartttlne elgqveyifs dktgtltqni
      421 mvfnkcsing hsygdvfdvl ghkaelgerp epvdfsfnpl adkkflfwdp slleavkigd
      481 phtheffrll slchtvmsee knegelyyka qspdegalvt aarnfgfvfr srtpktitvh
      541 emgtaityql laildfnnir krmsvivrnp egkirlyckg adtilldrlh hstqellntt
      601 mdhlneyage glrtlvlayk dldeeyyeew aerrlqasla qdsredrlas iyeevennmm
      661 llgataiedk lqqgvpetia lltlanikiw vltgdkqeta vnigysckml tddmtevfiv
      721 tghtvlevre elrkarekmm dssrsvgngf tyqdklsssk ltsvleavag eyalvinghs
      781 lahaleadme lefletacac kaviccrvtp lqkaqvvelv kkykkavtla igdgandvsm
      841 iktahigvgi sgqegiqavl asdysfsqfk flqrlllvhg rwsylrmckf lcyffyknfa
      901 ftmvhfwfgf fcgfsaqtvy dqyfitlyni vytslpvlam gvfdqdvpeq rsmeypklye
      961 pgqlnllfnk refficiaqg iytsvlmffi pygvfadatr ddgtqladyq sfavtvatsl
     1021 vivvsvqigl dtgywtainh ffiwgslavy failfamhsn glfdmfpnqf rfvgnaqntl
     1081 aqptvwltiv lttvvcimpv vafrflrlnl kpdlsdtvry tqlvrkkqka qhrcmrrvgr
     1141 tgsrrsgyaf shqegfgeli msgknmrlss lalssfttrs ssswieslrr kksdsassps
     1201 ggadkplkg
//
LOCUS       NP_001073991            1620 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil and C2 domain-containing protein 2A isoform a [Homo
            sapiens].
ACCESSION   NP_001073991 XP_933462
VERSION     NP_001073991.2
DBSOURCE    REFSEQ: accession NM_001080522.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1620)
  AUTHORS   Harion,M., Qebibo,L., Riquet,A., Rougeot,C., Afenjar,A., Garel,C.,
            Louha,M., Lacaze,E., Audic-Gerard,F., Barth,M., Berquin,P.,
            Bonneau,D., Bourdain,F., Busa,T., Colin,E., Cuisset,J.M., Des
            Portes,V., Dorison,N., Francannet,C., Heron,B., Laroche,C.,
            Lebrun,M., Metreau,J., Odent,S., Pasquier,L., Trujillo,Y.P.,
            Perrin,L., Pinson,L., Rivier,F., Sigaudy,S., Thauvin-Robinet,C.,
            Louvier,U.W., Labayle,O., Rodriguez,D., Valence,S. and Burglen,L.
  TITLE     New insights into CC2D2A-related Joubert syndrome
  JOURNAL   J Med Genet 60 (6), 578-586 (2023)
   PUBMED   36319078
  REMARK    GeneRIF: New insights into CC2D2A-related Joubert syndrome.
REFERENCE   2  (residues 1 to 1620)
  AUTHORS   Cabrita Pinto,R.L., Viaggi,S., Canale,E., Martinez Popple,M.,
            Capra,V., Conteduca,G., Testa,B., Coviello,D. and Covone,A.E.
  TITLE     Exome Analysis Reveals Novel Missense and Deletion Variants in the
            CC2D2A Gene as Causative of Joubert Syndrome
  JOURNAL   Genes (Basel) 14 (4), 810 (2023)
   PUBMED   37107568
  REMARK    GeneRIF: Exome Analysis Reveals Novel Missense and Deletion
            Variants in the CC2D2A Gene as Causative of Joubert Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1620)
  AUTHORS   Barroso-Gil,M., Olinger,E., Ramsbottom,S.A., Molinari,E.,
            Miles,C.G. and Sayer,J.A.
  TITLE     Update of genetic variants in CEP120 and CC2D2A-With an emphasis on
            genotype-phenotype correlations, tissue specific transcripts and
            exploring mutation specific exon skipping therapies
  JOURNAL   Mol Genet Genomic Med 9 (12), e1603 (2021)
   PUBMED   33486889
  REMARK    GeneRIF: Update of genetic variants in CEP120 and CC2D2A-With an
            emphasis on genotype-phenotype correlations, tissue specific
            transcripts and exploring mutation specific exon skipping
            therapies.
REFERENCE   4  (residues 1 to 1620)
  AUTHORS   Khan,M.I., Latif,M., Saif,M., Ahmad,H., Khan,A.U., Naseer,M.I.,
            Hussain,H.M.J. and Jelani,M.
  TITLE     Whole exome sequencing identified a novel missense alteration in
            CC2D2A causing Joubert syndrome 9 in a Pakhtun family
  JOURNAL   J Gene Med 23 (1), e3279 (2021)
   PUBMED   32989887
  REMARK    GeneRIF: Whole exome sequencing identified a novel missense
            alteration in CC2D2A causing Joubert syndrome 9 in a Pakhtun
            family.
REFERENCE   5  (residues 1 to 1620)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Paterson,A.D., Lutufullah,M., Doherty,D.,
            Vincent,J.B. and Ayub,M.
  TITLE     Addendum. CC2D2A, encoding a coiled-coil and C2 domain protein,
            causes autosomal-recessive mental retardation with retinitis
            pigmentosa
  JOURNAL   Am J Hum Genet 83 (5), 656 (2008)
   PUBMED   19068953
  REMARK    GeneRIF: CC2D2A causes autosomal-recessive mental retardation with
            retinitis pigmentosa.
REFERENCE   6  (residues 1 to 1620)
  AUTHORS   Gorden,N.T., Arts,H.H., Parisi,M.A., Coene,K.L., Letteboer,S.J.,
            van Beersum,S.E., Mans,D.A., Hikida,A., Eckert,M., Knutzen,D.,
            Alswaid,A.F., Ozyurek,H., Dibooglu,S., Otto,E.A., Liu,Y.,
            Davis,E.E., Hutter,C.M., Bammler,T.K., Farin,F.M., Dorschner,M.,
            Topcu,M., Zackai,E.H., Rosenthal,P., Owens,K.N., Katsanis,N.,
            Vincent,J.B., Hildebrandt,F., Rubel,E.W., Raible,D.W., Knoers,N.V.,
            Chance,P.F., Roepman,R., Moens,C.B., Glass,I.A. and Doherty,D.
  TITLE     CC2D2A is mutated in Joubert syndrome and interacts with the
            ciliopathy-associated basal body protein CEP290
  JOURNAL   Am J Hum Genet 83 (5), 559-571 (2008)
   PUBMED   18950740
  REMARK    GeneRIF: CC2D2A is mutated in Joubert syndrome and interacts with
            the ciliopathy-associated basal body protein CEP290.
REFERENCE   7  (residues 1 to 1620)
  AUTHORS   Tallila,J., Jakkula,E., Peltonen,L., Salonen,R. and Kestila,M.
  TITLE     Identification of CC2D2A as a Meckel syndrome gene adds an
            important piece to the ciliopathy puzzle
  JOURNAL   Am J Hum Genet 82 (6), 1361-1367 (2008)
   PUBMED   18513680
  REMARK    GeneRIF: CC2D2A appears to have at least two cilia-related
            functions: the molecule seems to be a part of the basal body
            complex where the cilium is assembled from and also seems to act as
            a sensor for the intracellular calcium.
REFERENCE   8  (residues 1 to 1620)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Siddiqui,Z.K., Naeem,F., Paterson,A.D.,
            Lutfullah,M., Vincent,J.B. and Ayub,M.
  TITLE     CC2D2A, encoding a coiled-coil and C2 domain protein, causes
            autosomal-recessive mental retardation with retinitis pigmentosa
  JOURNAL   Am J Hum Genet 82 (4), 1011-1018 (2008)
   PUBMED   18387594
  REMARK    GeneRIF: A homozygous splice-site mutation segregating in the
            family with autosomal-recessive mental retardation, within a
            coiled-coil and C2 domain-containing gene, CC2D2A was identified.
REFERENCE   9  (residues 1 to 1620)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 1620)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from N35522.1, BX647334.1,
            EU450799.1 and CF528984.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 22, 2008 this sequence version replaced NP_001073991.1.
            
            Summary: This gene encodes a coiled-coil and calcium binding domain
            protein that appears to play a critical role in cilia formation.
            Mutations in this gene cause Meckel syndrome type 6, as well as
            Joubert syndrome type 9. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU450799.1, SRR14038192.1052260.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..1620
                     /product="coiled-coil and C2 domain-containing protein 2A
                     isoform a"
                     /note="coiled-coil and C2 domain-containing protein 2A"
                     /calculated_mol_wt=186055
     Region          1..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          131..383
                     /region_name="DUF5523"
                     /note="Family of unknown function (DUF5523); pfam17661"
                     /db_xref="CDD:465443"
     Region          592..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          645..819
                     /region_name="CC2D2AN-C2"
                     /note="CC2D2A N-terminal C2 domain; pfam15625"
                     /db_xref="CDD:464780"
     Region          1062..1087
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P2K1.3)"
     Region          1066..>1099
                     /region_name="DDA1"
                     /note="Det1 complexing ubiquitin ligase; pfam10172"
                     /db_xref="CDD:401980"
     Region          <1097..>1135
                     /region_name="C2"
                     /note="C2 domain; cl14603"
                     /db_xref="CDD:472691"
     CDS             1..1620
                     /gene="CC2D2A"
                     /gene_synonym="COACH2; JBTS9; MKS6; RP93"
                     /coded_by="NM_001080522.2:246..5108"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47026.1"
                     /db_xref="GeneID:57545"
                     /db_xref="HGNC:HGNC:29253"
                     /db_xref="MIM:612013"
ORIGIN      
        1 mnpreekvki iteefiende dadmgrqnkn skvrrqprkk qpptavpkem vsekshlgnp
       61 qepvqeepkt rllsmtvrrg prslppipst srtgfaefsm rgrmreklqa arskaesall
      121 qeiptprprr lrspskkele tefgtepgke vertqqevds qsysrvkfhd sarkikpkpq
      181 vppgfpsaee aynfftfnfd pepegseekp karhragtnq eeeegeeeep paqgggkemd
      241 eeellngdda edfllgldhv addfvavrpa dyesihdrlq meremlfips rqtvptykkl
      301 penvqprfle deglytgvrp evartnqnim enrllmqdpe rrwfgddgri lalpnpikpf
      361 psrppvltqe qsikaeletl ykkavkyvhs sqhvirsgdp pgnfqldidi sglifthhpc
      421 fsrehvlaak laqlydqyla rhqrnkakfl tdklqalrna vqtgldpekp hqsldtiqkt
      481 ineykseirq trkfrdaeqe kdrtllktii kvwkemkslr efqrftntpl klvlrkekad
      541 qkadeeayea eiqaeisell eehteeyaqk meeyrtslqq wkawrkvqra kkkkrkqaae
      601 ehpgdeiaep ypeedlvkps ppeptdravi eqevreraaq srrrpweptl vpelslagsv
      661 tpndqcprae vsrredvkkr svylkvlfnn kevsrtvsrp lgadfrvhfg qifnlqivnw
      721 pesltlqvye tvghssptll aevflpipet tvvtgrapte evefssnqhv tldhegvgsg
      781 vpfsfeadgs nqltlmtsgk vshsvawaig engiplippl sqqnigfrsa lkkadaissi
      841 gtsgltdmkk lakwaaeskl dpndpnnapl mqlisvatsg esyvpdffrl eqlqqefnfv
      901 sdqelnrskr frllhlrsqe vpefrnykqv pvydreimek vfqdyekrlr drnvietkeh
      961 idthraivak ylqqvresvi nrfliakqyf lladmiveee vpnisilgls lfklaeqkrp
     1021 lrprrkgrkk vtaqnlsdgd ikllvnivra ydipvrkpav skfqqpsrss rmfsekhaas
     1081 pstyspthna dyplgqvlvr pfvevsfqrt vchtttaegp npswneelel pfrapngdys
     1141 taslqsvkdv vfinifdevl hdvleddrer gsgihtrier hwlgcvkmpf stiyfqarid
     1201 gtfkidippv llgyskernm ilergfdsvr slsegsyitl fitiepqlvp gesirekfes
     1261 qedekllqat ekfqaecalk fpnrqclttv idisgktvfi trylkplnpp qellnvypnn
     1321 lqataelvar yvslipflpd tvsfggicdl wstsdqfldl lagdeeehav llcnyflslg
     1381 kkawllmgna ipegptayvl tweqgryliw npcsghfygq fdtfcplknv gcligpdniw
     1441 fniqryespl rinfdvtrpk lwksffsrsl pypglssvqp eeliyqrsdk aaaaelqdri
     1501 ekilkekimd wrprhltrwn ryctstlrhf lplleksqge dveddhrael lkqlgdyrfs
     1561 gfplhmpyse vkplidavys tgvhnidvpn vefalavyih pypknvlsvw iyvaslirnr
//
LOCUS       NP_079430                702 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform b [Homo sapiens].
ACCESSION   NP_079430 XP_376564 XP_379766
VERSION     NP_079430.3
DBSOURCE    REFSEQ: accession NM_025154.6
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 702)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 702)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 702)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 702)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 702)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 702)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 702)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 702)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 702)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 702)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            On Jul 7, 2006 this sequence version replaced NP_079430.2.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. This variant also
            lacks an in-frame exon in the 5' portion of the coding region. The
            encoded isoform (b) is shorter than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..702
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..702
                     /product="SUN domain-containing protein 1 isoform b"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=77780
     Region          12..208
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <282..>506
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          334..387
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(334,337..338,341,344..345,348..349,351..352,
                     355..356,358..359,362..363,365..366,369,372..373,376,
                     379..380,383..384,386..387)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          464..522
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          565..700
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..702
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_025154.6:105..2213"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43533.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkw kaasgvfwwl
      181 gigwyqfvtl iswlnvfllt rclrnickfl vlliplflll aglslrgqgn ffsflpvlnw
      241 asmhrtqrvd dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl
      301 relttllqkl qarvdqmegg aagpsasvrd avgqppretd fmafhqehev rmshledilg
      361 klrekseaiq keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd
      421 avqervdvqv remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt
      481 hhvsvtkqlp tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg
      541 silstrcset yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls
      601 mmihpaaftl ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm
      661 fqalkrpddt afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_002808                376 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 13 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002808
VERSION     NP_002808.3
DBSOURCE    REFSEQ: accession NM_002817.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   3  (residues 1 to 376)
  AUTHORS   He,S., Cao,R., Mao,Y., Li,N., Wang,Y., Ma,H. and Tian,K.
  TITLE     Alternative splicing of PSMD13 mediated by genetic variants is
            significantly associated with endometrial cancer risk
  JOURNAL   J Gynecol Oncol 34 (3), e40 (2023)
   PUBMED   36731897
  REMARK    GeneRIF: Alternative splicing of PSMD13 mediated by genetic
            variants is significantly associated with endometrial cancer risk.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Hori,T., Kato,S., Saeki,M., DeMartino,G.N., Slaughter,C.A.,
            Takeuchi,J., Toh-e,A. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p28 (Nas6p) and p40.5
            (Nas7p), two novel regulatory subunits of the 26S proteasome
  JOURNAL   Gene 216 (1), 113-122 (1998)
   PUBMED   9714768
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC136475.7, AB009398.1 and AA931044.1.
            
            On Sep 25, 2007 this sequence version replaced NP_002808.2.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. Two transcripts encoding
            different isoforms have been described. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.293980.1,
                                           SRR5189655.5737.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000532097.6/ ENSP00000436186.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5"
     Protein         1..376
                     /product="26S proteasome non-ATPase regulatory subunit 13
                     isoform 1"
                     /note="26S proteasome subunit p40.5; 26S proteasome
                     regulatory subunit S11; 26S proteasome non-ATPase
                     regulatory subunit 13; 26S proteasome regulatory subunit
                     p40.5; 26S proteasome regulatory subunit RPN9; proteasome
                     (prosome, macropain) 26S subunit, non-ATPase, 13"
                     /calculated_mol_wt=42815
     Region          231..335
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Site            298
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9UNM6.2)"
     CDS             1..376
                     /gene="PSMD13"
                     /gene_synonym="HSPC027; p40.5; Rpn9; S11"
                     /coded_by="NM_002817.4:75..1205"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7692.1"
                     /db_xref="GeneID:5719"
                     /db_xref="HGNC:HGNC:9558"
                     /db_xref="MIM:603481"
ORIGIN      
        1 mkdvpgflqq sqnsgpgqpa vwhrleelyt kklwhqltlq vldfvqdpcf aqgdglikly
       61 enfisefehr vnplslveii lhvvrqmtdp nvaltflekt rekvkssdea vilcktaiga
      121 lklnigdlqv tketiedvee mlnnlpgvts vhsrfydlss kyyqtignha syykdalrfl
      181 gcvdikdlpv seqqeraftl glagllgegv fnfgellmhp vleslrntdr qwlidtlyaf
      241 nsgnverfqt lktawgqqpd laaneaqllr kiqllclmem tftrpanhrq ltfeeiaksa
      301 kitvnevell vmkalsvglv kgsidevdkr vhmtwvqprv ldlqqikgmk drlefwctdv
      361 ksmemlvehq ahdilt
//
LOCUS       NP_001877                196 aa            linear   PRI 20-NOV-2025
DEFINITION  beta-crystallin A4 [Homo sapiens].
ACCESSION   NP_001877
VERSION     NP_001877.1
DBSOURCE    REFSEQ: accession NM_001886.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Zhang,X., Liang,C., Liu,M., Wang,Z., Leng,X., Xie,S., Tan,X.,
            Yang,Y. and Liu,Y.
  TITLE     A novel missense variant c.71G > T (p.Gly24Val) of the CRYBA4 gene
            contributes to autosomal-dominant congenital cataract in a Chinese
            family
  JOURNAL   Int Ophthalmol 43 (1), 43-50 (2023)
   PUBMED   35840783
  REMARK    GeneRIF: A novel missense variant c.71G > T (p.Gly24Val) of the
            CRYBA4 gene contributes to autosomal-dominant congenital cataract
            in a Chinese family.
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Wang,Z., Huang,C., Lv,H., Zhang,M. and Li,X.
  TITLE     In silico analysis and high-risk pathogenic phenotype predictions
            of non-synonymous single nucleotide polymorphisms in human
            Crystallin beta A4 gene associated with congenital cataract
  JOURNAL   PLoS One 15 (1), e0227859 (2020)
   PUBMED   31935276
  REMARK    GeneRIF: his study provides important reference value when
            narrowing down the number of pathogenic CRYBA4 nsSNPs and studying
            the pathogenesis of congenital cataracts. By using this method, we
            can easily find 44 high-risk pathogenic nsSNPs out of 157 CRYBA4
            nsSNPs
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Lampi,K.J., Ma,Z., Shih,M., Shearer,T.R., Smith,J.B., Smith,D.L.
            and David,L.L.
  TITLE     Sequence analysis of betaA3, betaB3, and betaA4 crystallins
            completes the identification of the major proteins in young human
            lens
  JOURNAL   J Biol Chem 272 (4), 2268-2275 (1997)
   PUBMED   8999933
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Bijlsma,E.K., Delattre,O., Juyn,J.A., Melot,T., Westerveld,A.,
            Dumanski,J.P., Thomas,G. and Hulsebos,T.J.
  TITLE     Regional fine mapping of the beta crystallin genes on chromosome 22
            excludes these genes as physically linked markers for
            neurofibromatosis type 2
  JOURNAL   Genes Chromosomes Cancer 8 (2), 112-118 (1993)
   PUBMED   7504514
REFERENCE   7  (residues 1 to 196)
  AUTHORS   David,L.L., Shearer,T.R. and Shih,M.
  TITLE     Sequence analysis of lens beta-crystallins suggests involvement of
            calpain in cataract formation
  JOURNAL   J Biol Chem 268 (3), 1937-1940 (1993)
   PUBMED   8420967
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Bardakjian,T., Weiss,A. and Schneider,A.
  TITLE     Microphthalmia/Anophthalmia/Coloboma Spectrum - RETIRED CHAPTER,
            FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301552
REFERENCE   9  (residues 1 to 196)
  AUTHORS   van Rens,G.L., Geurts van Kessel,A.H. and Bloemendal,H.
  TITLE     Localization of the beta A4-crystallin gene (CRYBA4) on human
            chromosome 22 in the region q11.2-->q13.1
  JOURNAL   Cytogenet Cell Genet 61 (3), 180-183 (1992)
   PUBMED   1424806
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Schuschke,G., Mielke,U., Bodamer,S. and Rosenkranz,M.
  TITLE     [Feral domestic pigeons as a hygienic problem in big cities--the
            situation in Magdeburg]
  JOURNAL   Z Gesamte Hyg 22 (1), 30-34 (1976)
   PUBMED   960806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z95115.1, BC069404.1,
            BF726612.1, BC096172.3 and BM667295.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Crystallins are separated into two classes:
            taxon-specific, or enzyme, and ubiquitous. The latter class
            constitutes the major proteins of vertebrate eye lens and maintains
            the transparency and refractive index of the lens. Since lens
            central fiber cells lose their nuclei during development, these
            crystallins are made and then retained throughout life, making them
            extremely stable proteins. Mammalian lens crystallins are divided
            into alpha, beta, and gamma families; beta and gamma crystallins
            are also considered as a superfamily. Alpha and beta families are
            further divided into acidic and basic groups. Seven protein regions
            exist in crystallins: four homologous motifs, a connecting peptide,
            and N- and C-terminal extensions. Beta-crystallins, the most
            heterogeneous, differ by the presence of the C-terminal extension
            (present in the basic group, none in the acidic group).
            Beta-crystallins form aggregates of different sizes and are able to
            self-associate to form dimers or to form heterodimers with other
            beta-crystallins. This gene, a beta acidic group member, is part of
            a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: Experimental evidence for the bovine
            betaA4-crystallin in PMID: 1874445 suggests that a possible
            translation start codon would exist at nt 3-5 in this human
            sequence. No experimental evidence currently exists for a longer
            protein being produced in human cells.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U59057.1, KM365089.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:8999933)
            MANE Ensembl match               :: ENST00000354760.4/
                                                ENSP00000346805.3
            RefSeq Select criteria           :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.1"
     Protein         1..196
                     /product="beta-crystallin A4"
                     /note="eye lens structural protein; crystallin, beta
                     polypeptide A4; beta-A4 crystallin; beta crystallin A4
                     chain transcript PS; beta crystallin alpha 4 chain"
                     /calculated_mol_wt=22243
     Region          2..11
                     /region_name="N-terminal extension"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0000269|PubMed:8999933; propagated from
                     UniProtKB/Swiss-Prot (P53673.3)"
     Region          12..51
                     /region_name="motif I"
     Region          13..96
                     /region_name="Crystall"
                     /note="Beta/Gamma crystallin; pfam00030"
                     /db_xref="CDD:459639"
     Region          52..99
                     /region_name="motif II"
     Region          99..104
                     /region_name="Connecting peptide"
                     /note="propagated from UniProtKB/Swiss-Prot (P53673.3)"
     Region          100..104
                     /region_name="connecting peptide"
     Region          105..146
                     /region_name="motif III"
     Region          106..194
                     /region_name="XTALbg"
                     /note="Beta/gamma crystallins; smart00247"
                     /db_xref="CDD:214583"
     Region          147..196
                     /region_name="motif IV"
     CDS             1..196
                     /gene="CRYBA4"
                     /gene_synonym="CTRCT23; CYRBA4; MCOPCT4"
                     /coded_by="NM_001886.3:37..627"
                     /db_xref="CCDS:CCDS13841.1"
                     /db_xref="GeneID:1413"
                     /db_xref="HGNC:HGNC:2396"
                     /db_xref="MIM:123631"
ORIGIN      
        1 mtlqctksag pwkmvvwded gfqgrrheft aecpsvlelg fetvrslkvl sgawvgfeha
       61 gfqgqqyile rgeypswdaw ggntaypaer ltsfrpaaca nhrdsrltif eqenflgkkg
      121 elsddypslq amgwegnevg sfhvhsgawv csqfpgyrgf qyvlecdhhs gdykhfrewg
      181 shaptfqvqs irriqq
//
LOCUS       NP_004965                499 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium voltage-gated channel subfamily A member 2 isoform a
            [Homo sapiens].
ACCESSION   NP_004965
VERSION     NP_004965.1
DBSOURCE    REFSEQ: accession NM_004974.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Xie,C., Kessi,M., Yin,F. and Peng,J.
  TITLE     Roles of KCNA2 in Neurological Diseases: from Physiology to
            Pathology
  JOURNAL   Mol Neurobiol 61 (11), 8491-8517 (2024)
   PUBMED   38517617
  REMARK    GeneRIF: Roles of KCNA2 in Neurological Diseases: from Physiology
            to Pathology.
            Review article
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Arlt,F.A., Miske,R., Machule,M.L., Broegger Christensen,P.,
            Mindorf,S., Teegen,B., Borowski,K., Buthut,M., Rossling,R.,
            Sanchez-Sendin,E., van Hoof,S., Cordero-Gomez,C., Bunger,I.,
            Radbruch,H., Kraft,A., Ayzenberg,I., Klausewitz,J., Hansen,N.,
            Timaus,C., Kortvelyessy,P., Postert,T., Baur-Seack,K., Rost,C.,
            Brunkhorst,R., Doppler,K., Haigis,N., Hamann,G., Kunze,A.,
            Stutzer,A., Maschke,M., Melzer,N., Rosenow,F., Siebenbrodt,K.,
            Stenor,C., Dichgans,M., Georgakis,M.K., Fang,R., Petzold,G.C.,
            Gortler,M., Zerr,I., Wunderlich,S., Mihaljevic,I., Turko,P.,
            Schmidt Ettrup,M., Buchholz,E., Foverskov Rasmussen,H., Nasouti,M.,
            Talucci,I., Maric,H.M., Heinemann,S.H., Endres,M., Komorowski,L.
            and Pruss,H.
  CONSRTM   DEMDAS study group
  TITLE     KCNA2 IgG autoimmunity in neuropsychiatric diseases
  JOURNAL   Brain Behav Immun 117, 399-411 (2024)
   PUBMED   38309639
  REMARK    GeneRIF: KCNA2 IgG autoimmunity in neuropsychiatric diseases.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Minguez-Vinas,T., Prakash,V., Wang,K., Lindstrom,S.H., Pozzi,S.,
            Scott,S.A., Spiteri,E., Stevenson,D.A., Ashley,E.A., Gunnarsson,C.
            and Pantazis,A.
  TITLE     Two epilepsy-associated variants in KCNA2 (KV 1.2) at position H310
            oppositely affect channel functional expression
  JOURNAL   J Physiol 601 (23), 5367-5389 (2023)
   PUBMED   37883018
  REMARK    GeneRIF: Two epilepsy-associated variants in KCNA2 (KV 1.2) at
            position H310 oppositely affect channel functional expression.
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Nilsson,M., Lindstrom,S.H., Kaneko,M., Wang,K., Minguez-Vinas,T.,
            Angelini,M., Steccanella,F., Holder,D., Ottolia,M., Olcese,R. and
            Pantazis,A.
  TITLE     An epilepsy-associated KV1.2 charge-transfer-center mutation
            impairs KV1.2 and KV1.4 trafficking
  JOURNAL   Proc Natl Acad Sci U S A 119 (17), e2113675119 (2022)
   PUBMED   35439054
  REMARK    GeneRIF: An epilepsy-associated KV1.2 charge-transfer-center
            mutation impairs KV1.2 and KV1.4 trafficking.
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Nakahira,K., Shi,G., Rhodes,K.J. and Trimmer,J.S.
  TITLE     Selective interaction of voltage-gated K+ channel beta-subunits
            with alpha-subunits
  JOURNAL   J Biol Chem 271 (12), 7084-7089 (1996)
   PUBMED   8636142
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Ramaswami,M., Tanouy,M. and Mathew,M.K.
  TITLE     Facile formation of heteromultimeric potassium channels by
            expression of cloned human cDNAs
  JOURNAL   Indian J Biochem Biophys 31 (4), 254-260 (1994)
   PUBMED   8002006
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Klocke,R., Roberds,S.L., Tamkun,M.M., Gronemeier,M., Augustin,A.,
            Albrecht,B., Pongs,O. and Jockusch,H.
  TITLE     Chromosomal mapping in the mouse of eight K(+)-channel genes
            representing the four Shaker-like subfamilies Shaker, Shab, Shaw,
            and Shal
  JOURNAL   Genomics 18 (3), 568-574 (1993)
   PUBMED   7905852
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Grissmer,S., Dethlefs,B., Wasmuth,J.J., Goldin,A.L., Gutman,G.A.,
            Cahalan,M.D. and Chandy,K.G.
  TITLE     Expression and chromosomal localization of a lymphocyte K+ channel
            gene
  JOURNAL   Proc Natl Acad Sci U S A 87 (23), 9411-9415 (1990)
   PUBMED   2251283
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL365361.12, AK290061.1,
            BC043564.1 and BM682747.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member contains six
            membrane-spanning domains with a shaker-type repeat in the fourth
            segment. It belongs to the delayed rectifier class, members of
            which allow nerve cells to efficiently repolarize following an
            action potential. The coding region of this gene is intronless, and
            the gene is clustered with genes KCNA3 and KCNA10 on chromosome 1.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290061.1, DA341137.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316361.10/ ENSP00000314520.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..499
                     /product="potassium voltage-gated channel subfamily A
                     member 2 isoform a"
                     /note="voltage-gated potassium channel protein Kv1.2;
                     potassium voltage-gated channel, shaker-related subfamily,
                     member 2; voltage-gated K(+) channel HuKIV; voltage-gated
                     potassium channel HBK5; voltage-gated potassium channel
                     subunit Kv1.2; potassium channel, voltage gated shaker
                     related subfamily A, member 2"
                     /calculated_mol_wt=56586
     Region          1..125
                     /region_name="Tetramerization domain.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Region          33..159
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Site            161..182
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Region          162..420
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            207
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            222..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Site            252
                     /site_type="other"
                     /note="Important for normal, slow channel gating.
                     /evidence=ECO:0000250|UniProtKB:P63142; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            255..275
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Site            290..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Region          312..325
                     /region_name="S4-S5 linker.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Site            326..347
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Region          374..379
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Site            381
                     /site_type="other"
                     /note="Important for binding with the scorpion
                     mesomartoxin, when the scorpion mesomartoxin-rKv1.2/KCNA2
                     interaction is modeled, this residue is close to the
                     'Y-57' residue of the toxin.
                     /evidence=ECO:0000250|UniProtKB:P63142; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            389..417
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P63141; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            434
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63141; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            440
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63141; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q09081; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q09081; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P63142; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Site            468
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P63141; propagated from
                     UniProtKB/Swiss-Prot (P16389.2)"
     Region          497..499
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P16389.2)"
     CDS             1..499
                     /gene="KCNA2"
                     /gene_synonym="DEE32; EIEE32; HBK5; HK4; HUKIV; KV1.2;
                     MK2; NGK1; RBK2"
                     /coded_by="NM_004974.4:627..2126"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS827.1"
                     /db_xref="GeneID:3737"
                     /db_xref="HGNC:HGNC:6220"
                     /db_xref="MIM:176262"
ORIGIN      
        1 mtvatgdpad eaaalpghpq dtydpeadhe ccervvinis glrfetqlkt laqfpetllg
       61 dpkkrmryfd plrneyffdr nrpsfdaily yyqsggrlrr pvnvpldifs eeirfyelge
      121 eamemfrede gyikeeerpl penefqrqvw llfeypessg pariiaivsv mvilisivsf
      181 cletlpifrd enedmhgsgv tfhtysnsti gyqqstsftd pffivetlci iwfsfeflvr
      241 ffacpskagf ftnimniidi vaiipyfitl gtelaekped aqqgqqamsl ailrvirlvr
      301 vfrifklsrh skglqilgqt lkasmrelgl lifflfigvi lfssavyfae aderesqfps
      361 ipdafwwavv smttvgygdm vpttiggkiv gslcaiagvl tialpvpviv snfnyfyhre
      421 tegeeqaqyl qvtscpkips spdlkksrsa stisksdyme iqegvnnsne dfreenlkta
      481 nctlantnyv nitkmltdv
//
LOCUS       NP_001035842             495 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform c [Homo sapiens].
ACCESSION   NP_001035842
VERSION     NP_001035842.1
DBSOURCE    REFSEQ: accession NM_001042383.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, BX499930.1,
            BC014050.2, CX751767.1, AC109912.10 and N36992.1.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.73112.1,
                                           SRR1803614.251545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..495
                     /product="centrosomal protein of 63 kDa isoform c"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=57777
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <163..>441
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..495
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001042383.2:355..1842"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43154.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveais lesvsatckq lsqelmekye elkrmeahnn eykaeikklk eqilqgeqsy
      361 ssalegmkme ishltqelhq rditiastkg sssdmekrlr aemqkaedka vehkeildql
      421 eslklenrhl semvmklelg lhecslpvsp lgsiatrfle eeelrshhil erldahieel
      481 kresektvrq ftalk
//
LOCUS       NP_001317950             249 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26C isoform 3 [Homo
            sapiens].
ACCESSION   NP_001317950 XP_011527725
VERSION     NP_001317950.1
DBSOURCE    REFSEQ: accession NM_001331021.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 249)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   2  (residues 1 to 249)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 249)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 249)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 249)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 249)
  AUTHORS   Koumandou,V.L., Klute,M.J., Herman,E.K., Nunez-Miguel,R.,
            Dacks,J.B. and Field,M.C.
  TITLE     Evolutionary reconstruction of the retromer complex and its
            function in Trypanosoma brucei
  JOURNAL   J Cell Sci 124 (Pt 9), 1496-1509 (2011)
   PUBMED   21502137
REFERENCE   7  (residues 1 to 249)
  AUTHORS   Aubry,L., Guetta,D. and Klein,G.
  TITLE     The arrestin fold: variations on a theme
  JOURNAL   Curr Genomics 10 (2), 133-142 (2009)
   PUBMED   19794886
REFERENCE   8  (residues 1 to 249)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 249)
  AUTHORS   Dahmane,N., Ghezala,G.A., Gosset,P., Chamoun,Z.,
            Dufresne-Zacharia,M.C., Lopes,C., Rabatel,N.,
            Gassanova-Maugenre,S., Chettouh,Z., Abramowski,V., Fayet,E.,
            Yaspo,M.L., Korn,B., Blouin,J.L., Lehrach,H., Poutska,A.,
            Antonarakis,S.E., Sinet,P.M., Creau,N. and Delabar,J.M.
  TITLE     Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21
            involved in Down syndrome
  JOURNAL   Genomics 48 (1), 12-23 (1998)
   PUBMED   9503011
REFERENCE   10 (residues 1 to 249)
  AUTHORS   Nakamura,A., Hattori,M. and Sakaki,Y.
  TITLE     Isolation of a novel human gene from the Down syndrome critical
            region of chromosome 21q22.2
  JOURNAL   J Biochem 122 (4), 872-877 (1997)
   PUBMED   9399594
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001412.2, AK303624.1,
            AP001432.2 and BX648191.1.
            
            On Sep 3, 2016 this sequence version replaced XP_011527725.1.
            
            Summary: The region of chromosome 21 between genes CBR and ERG
            (CBR-ERG region), which spans 2.5 Mb on 21q22.2, has been defined
            by analysis of patients with partial trisomy 21. It contributes
            significantly to the pathogenesis of many characteristics of Down
            syndrome, including morphological features, hypotonia, and
            cognitive disability. The DSCR3 (Down syndrome critical region gene
            3) gene is found in this region and is predictated to contain eight
            exons. DSCR3 is expressed in most tissues examined. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.217536.1,
                                           SRR1660805.83466.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..249
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..249
                     /product="vacuolar protein sorting-associated protein 26C
                     isoform 3"
                     /note="Down syndrome critical region protein A; Down
                     syndrome critical region protein 3; Down syndrome critical
                     region gene 3; Down syndrome critical region 3; DSCR3
                     arrestin fold containing; vacuolar protein
                     sorting-associated protein 26C"
                     /calculated_mol_wt=27828
     Region          7..235
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     cl22903"
                     /db_xref="CDD:451447"
     CDS             1..249
                     /gene="VPS26C"
                     /gene_synonym="DCRA; DSCR3; DSCRA"
                     /coded_by="NM_001331021.1:816..1565"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82672.1"
                     /db_xref="GeneID:10311"
                     /db_xref="HGNC:HGNC:3044"
                     /db_xref="MIM:605298"
ORIGIN      
        1 mgtaldikik rankvyhagp iqiinstiem vkpgkfpsgk teipfefplh lkgnkvlyet
       61 yhgvfvniqy tlrcdmkrsl lakdltktce fivhsapqkg kftpspvdft itpetlqnvk
      121 erallpkfll rghlnstncv itqpltgelv vesseaairs velqlvrvet cgcaegyard
      181 ateiqniqia dgdvcrglsv piymvfprlf tcptlettnf kvefevnivv llhpdhlite
      241 nfplklcri
//
LOCUS       NP_005561                510 aa            linear   PRI 20-NOV-2025
DEFINITION  protein ERGIC-53 precursor [Homo sapiens].
ACCESSION   NP_005561
VERSION     NP_005561.1
DBSOURCE    REFSEQ: accession NM_005570.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 510)
  AUTHORS   Zhang,Y., Liu,Z. and Zhang,B.
  TITLE     Separate roles of LMAN1 and MCFD2 in ER-to-Golgi trafficking of FV
            and FVIII
  JOURNAL   Blood Adv 7 (7), 1286-1296 (2023)
   PUBMED   36490287
REFERENCE   2  (residues 1 to 510)
  AUTHORS   Miller,M.H., Swaby,L.G., Vailoces,V.S., LaFratta,M., Zhang,Y.,
            Zhu,X., Hitchcock,D.J., Jewett,T.J., Zhang,B. and
            Tigno-Aranjuez,J.T.
  TITLE     LMAN1 is a receptor for house dust mite allergens
  JOURNAL   Cell Rep 42 (3), 112208 (2023)
   PUBMED   36870056
  REMARK    GeneRIF: LMAN1 is a receptor for house dust mite allergens.
REFERENCE   3  (residues 1 to 510)
  AUTHORS   Zhang,Y., Zhu,M., Zheng,C., Wei,W., Emmer,B.T. and Zhang,B.
  TITLE     LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi transport
            of alpha1-antitrypsin
  JOURNAL   Biochem J 479 (7), 839-855 (2022)
   PUBMED   35322856
  REMARK    GeneRIF: LMAN1-MCFD2 complex is a cargo receptor for the ER-Golgi
            transport of alpha1-antitrypsin.
REFERENCE   4  (residues 1 to 510)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 510)
  AUTHORS   Wigren,E., Bourhis,J.M., Kursula,I., Guy,J.E. and Lindqvist,Y.
  TITLE     Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex
            provides insight into combined deficiency of factor V and factor
            VIII
  JOURNAL   FEBS Lett 584 (5), 878-882 (2010)
   PUBMED   20138881
  REMARK    GeneRIF: Data present the crystal structure of the LMAN1/MCFD2
            complex and relate it to patient mutations. Circular dichroism data
            show that the majority of the substitution mutations give rise to a
            disordered or severely destabilized MCFD2 protein.
REFERENCE   6  (residues 1 to 510)
  AUTHORS   Neerman-Arbez,M., Antonarakis,S.E., Blouin,J.L., Zeinali,S.,
            Akhtari,M., Afshar,Y. and Tuddenham,E.G.
  TITLE     The locus for combined factor V-factor VIII deficiency (F5F8D) maps
            to 18q21, between D18S849 and D18S1103
  JOURNAL   Am J Hum Genet 61 (1), 143-150 (1997)
   PUBMED   9245995
REFERENCE   7  (residues 1 to 510)
  AUTHORS   Arar,C., Mignon,C., Mattei,M., Monsigny,M., Roche,A. and Legrand,A.
  TITLE     Mapping of the MR60/ERGIC-53 gene to human chromosome 18q21.3-18q22
            by in situ hybridization
  JOURNAL   Mamm Genome 7 (10), 791-792 (1996)
   PUBMED   8854877
REFERENCE   8  (residues 1 to 510)
  AUTHORS   Arar,C., Carpentier,V., Le Caer,J.P., Monsigny,M., Legrand,A. and
            Roche,A.C.
  TITLE     ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi
            intermediate compartment, is identical to MR60, an intracellular
            mannose-specific lectin of myelomonocytic cells
  JOURNAL   J Biol Chem 270 (8), 3551-3553 (1995)
   PUBMED   7876089
REFERENCE   9  (residues 1 to 510)
  AUTHORS   Fiedler,K. and Simons,K.
  TITLE     A putative novel class of animal lectins in the secretory pathway
            homologous to leguminous lectins
  JOURNAL   Cell 77 (5), 625-626 (1994)
   PUBMED   8205612
REFERENCE   10 (residues 1 to 510)
  AUTHORS   Schindler,R., Itin,C., Zerial,M., Lottspeich,F. and Hauri,H.P.
  TITLE     ERGIC-53, a membrane protein of the ER-Golgi intermediate
            compartment, carries an ER retention motif
  JOURNAL   Eur J Cell Biol 61 (1), 1-9 (1993)
   PUBMED   8223692
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC308886.1, BC032330.1,
            U09716.1, AC016229.10, AC067859.7, AK025773.1 and AI280513.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a membrane
            mannose-specific lectin that cycles between the endoplasmic
            reticulum, endoplasmic reticulum-Golgi intermediate compartment,
            and cis-Golgi, functioning as a cargo receptor for glycoprotein
            transport. The protein has an N-terminal signal sequence, a
            calcium-dependent and pH-sensitive carbohydrate recognition domain,
            a stalk region that functions in oligomerization, a transmembrane
            domain, and a short cytoplasmic domain required for organelle
            targeting. Allelic variants of this gene are associated with the
            autosomal recessive disorder combined factor V-factor VIII
            deficiency. [provided by RefSeq, Jul 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.186437.1,
                                           SRR1660805.147759.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000251047.6/ ENSP00000251047.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..510
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.32"
     Protein         1..510
                     /product="protein ERGIC-53 precursor"
                     /note="endoplasmic reticulum-golgi intermediate
                     compartment protein 53; protein ERGIC-53; intracellular
                     mannose-specific lectin MR60; ER-Golgi intermediate
                     compartment 53 kDa protein"
                     /calculated_mol_wt=54209
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3358
     mat_peptide     31..510
                     /product="protein ERGIC-53"
                     /calculated_mol_wt=54209
     Region          44..268
                     /region_name="lectin_ERGIC-53_ERGL"
                     /note="ERGIC-53 and ERGL type 1 transmembrane proteins,
                     N-terminal lectin domain; cd06902"
                     /db_xref="CDD:173890"
     Site            order(121,156,178,251..252)
                     /site_type="other"
                     /note="carbohydrate binding site [chemical binding]"
                     /db_xref="CDD:173890"
     Site            order(152,154..157,161..162,181)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:173890"
     Site            425
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49257.2)"
     Site            478..498
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49257.2)"
     Region          499..510
                     /region_name="Mediates interaction with RAB3GAP1, RAB3GAP2
                     and UBXN6. /evidence=ECO:0000269|PubMed:22337587"
                     /note="propagated from UniProtKB/Swiss-Prot (P49257.2)"
     Site            501
                     /site_type="other"
                     /note="Required for ER export; propagated from
                     UniProtKB/Swiss-Prot (P49257.2)"
     Region          509..510
                     /region_name="ER export motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P49257.2)"
     CDS             1..510
                     /gene="LMAN1"
                     /gene_synonym="ERGIC-53; ERGIC53; F5F8D; FMFD1; gp58;
                     MCFD1; MR60"
                     /coded_by="NM_005570.4:22..1554"
                     /db_xref="CCDS:CCDS11974.1"
                     /db_xref="GeneID:3998"
                     /db_xref="HGNC:HGNC:6631"
                     /db_xref="MIM:601567"
ORIGIN      
        1 magsrqrglr arvrplfcal llslgrfvrg dgvggdpava lphrrfeyky sfkgphlvqs
       61 dgtvpfwaha gnaipssdqi rvapslksqr gsvwtktkaa fenwevevtf rvtgrgriga
      121 dglaiwyaen qglegpvfgs adlwngvgif fdsfdndgkk nnpaiviign ngqihydhqn
      181 dgasqalasc qrdfrnkpyp vrakityyqn tltvminngf tpdkndyefc akvenmiipa
      241 qghfgisaat ggladdhdvl sfltfqltep gkepptpdke isekekekyq eefehfqqel
      301 dkkkeefqkg hpdlqgqpae eifesvgdre lrqvfegqnr ihleikqlnr qldmildeqr
      361 ryvsslteei skrgagmpgq hgqitqqeld tvvktqheil rqvnemknsm setvrlvsgm
      421 qhpgsaggvy ettqhfidik ehlhivkrdi dnlvqrnmps nekpkcpelp pfpsclstvh
      481 fiifvvvqtv lfigyimyrs qqeaaakkff
//
LOCUS       NP_005852                303 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CHIP isoform a [Homo sapiens].
ACCESSION   NP_005852
VERSION     NP_005852.2
DBSOURCE    REFSEQ: accession NM_005861.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Cao,Y., Chen,F., Zhu,S., Zhu,D. and Qi,H.
  TITLE     Staphylococcus aureus infection initiates hypoxia-mediated STIP1
            homology and U-box containing protein 1 upregulation to trigger
            osteomyelitis
  JOURNAL   Toxicon 248, 108049 (2024)
   PUBMED   39059559
  REMARK    GeneRIF: Staphylococcus aureus infection initiates hypoxia-mediated
            STIP1 homology and U-box containing protein 1 upregulation to
            trigger osteomyelitis.
REFERENCE   3  (residues 1 to 303)
  AUTHORS   van Prooije,T.H., Pennings,M., Dorresteijn,L., Gardeitchik,T.,
            Odekerken,V.J.J., Oosterloo,M., Pedersen,A.,
            Verschuuren-Bemelmans,C.C., Vrancken,A., Kamsteeg,E.J. and van de
            Warrenburg,B.P.C.
  TITLE     A New Case Series Suggests That SCA48 (ATX/STUB1) Is Primarily a
            Monogenic Disorder
  JOURNAL   Mov Disord 39 (9), 1636-1640 (2024)
   PUBMED   38973070
  REMARK    GeneRIF: A New Case Series Suggests That SCA48 (ATX/STUB1) Is
            Primarily a Monogenic Disorder.
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Baviera-Munoz,R., Carretero-Vilarroig,L., Pedro-Ibor,A., Jaijo,T.,
            Del Valle-Carranza,A., Martinez-Torres,I., Millan,J.M., Bataller,L.
            and Aller,E.
  TITLE     STUB1 Mutations as Possible Genetic Modifiers in Spinocerebellar
            Ataxia Type 8
  JOURNAL   Mov Disord 39 (9), 1641-1644 (2024)
   PUBMED   38962894
  REMARK    GeneRIF: STUB1 Mutations as Possible Genetic Modifiers in
            Spinocerebellar Ataxia Type 8.
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Tieliwaerdi,A., Aini,A., Amuti,M., Aierken,Y., Nijiati,M. and
            Luo,B.
  TITLE     STUB1 promotes the degradation of HSPB1 and induces ferroptosis in
            lung cancer cells
  JOURNAL   Environ Toxicol 39 (8), 4156-4170 (2024)
   PUBMED   38661247
  REMARK    GeneRIF: STUB1 promotes the degradation of HSPB1 and induces
            ferroptosis in lung cancer cells.
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Murata,S., Minami,Y., Minami,M., Chiba,T. and Tanaka,K.
  TITLE     CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded
            protein
  JOURNAL   EMBO Rep 2 (12), 1133-1138 (2001)
   PUBMED   11743028
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Jiang,J., Ballinger,C.A., Wu,Y., Dai,Q., Cyr,D.M., Hohfeld,J. and
            Patterson,C.
  TITLE     CHIP is a U-box-dependent E3 ubiquitin ligase: identification of
            Hsc70 as a target for ubiquitylation
  JOURNAL   J Biol Chem 276 (46), 42938-42944 (2001)
   PUBMED   11557750
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Connell,P., Ballinger,C.A., Jiang,J., Wu,Y., Thompson,L.J.,
            Hohfeld,J. and Patterson,C.
  TITLE     The co-chaperone CHIP regulates protein triage decisions mediated
            by heat-shock proteins
  JOURNAL   Nat Cell Biol 3 (1), 93-96 (2001)
   PUBMED   11146632
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Ballinger,C.A., Connell,P., Wu,Y., Hu,Z., Thompson,L.J., Yin,L.Y.
            and Patterson,C.
  TITLE     Identification of CHIP, a novel tetratricopeptide repeat-containing
            protein that interacts with heat shock proteins and negatively
            regulates chaperone functions
  JOURNAL   Mol Cell Biol 19 (6), 4535-4545 (1999)
   PUBMED   10330192
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Scanlan,M.J., Chen,Y.T., Williamson,B., Gure,A.O., Stockert,E.,
            Gordan,J.D., Tureci,O., Sahin,U., Pfreundschuh,M. and Old,L.J.
  TITLE     Characterization of human colon cancer antigens recognized by
            autologous antibodies
  JOURNAL   Int J Cancer 76 (5), 652-658 (1998)
   PUBMED   9610721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF217968.1, BC017178.1 and
            Z92544.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 2, 2004 this sequence version replaced NP_005852.1.
            
            Summary: This gene encodes a protein containing tetratricopeptide
            repeat and a U-box that functions as a ubiquitin
            ligase/cochaperone. The encoded protein binds to and ubiquitinates
            shock cognate 71 kDa protein (Hspa8) and DNA polymerase beta
            (Polb), among other targets. Mutations in this gene cause
            spinocerebellar ataxia, autosomal recessive 16. Alternative
            splicing results in multiple transcript variants. There is a
            pseudogene for this gene on chromosome 2. [provided by RefSeq, Jun
            2014].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.189232.1,
                                           SRR1163658.74836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219548.9/ ENSP00000219548.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..303
                     /product="E3 ubiquitin-protein ligase CHIP isoform a"
                     /EC_number="2.3.2.27"
                     /note="serologically defined colon cancer antigen 7; heat
                     shock protein A binding protein 2 (c-terminal); antigen
                     NY-CO-7; CLL-associated antigen KW-8; E3 ubiquitin-protein
                     ligase CHIP; carboxy terminus of Hsp70-interacting
                     protein; STIP1 homology and U-box containing protein 1, E3
                     ubiquitin protein ligase; RING-type E3 ubiquitin
                     transferase CHIP"
                     /calculated_mol_wt=34725
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          25..>124
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          26..59
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          26..54
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(27,30..31,34..35,37,61,64..65,68..69,71..72,95,
                     98..99,102..103,106)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          59..89
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          60..93
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          94..122
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          95..127
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          101..200
                     /region_name="Required for interaction with MAPK7.
                     /evidence=ECO:0000269|PubMed:20724525"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          142..225
                     /region_name="CHIP_TPR_N"
                     /note="CHIP N-terminal tetratricopeptide repeat domain;
                     pfam18391"
                     /db_xref="CDD:436460"
     Region          142..196
                     /region_name="Required for interaction with and
                     ubiquitination of MYOCD.
                     /evidence=ECO:0000250|UniProtKB:A6HD62"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          143..303
                     /region_name="Required for ubiquitination of FOXO1.
                     /evidence=ECO:0000269|PubMed:19483080"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          143..197
                     /region_name="Required for interaction with FOXO1.
                     /evidence=ECO:0000269|PubMed:19483080"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Site            149
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNE7.2)"
     Region          227..297
                     /region_name="RING-Ubox_CHIP"
                     /note="U-box domain, a modified RING finger, found in
                     carboxyl terminus of HSP70-interacting protein (CHIP) and
                     similar proteins; cd16654"
                     /db_xref="CDD:438316"
     Site            order(227,229..230,234..235,237,246..247,249,251,259..260,
                     263..264,269..270,272,281..286,288..289,292)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:438316"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9UNE7.2)"
     CDS             1..303
                     /gene="STUB1"
                     /gene_synonym="CHIP; HSPABP2; NY-CO-7; SCA48; SCAR16;
                     SDCCAG7; UBOX1"
                     /coded_by="NM_005861.4:117..1028"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10419.1"
                     /db_xref="GeneID:10273"
                     /db_xref="HGNC:HGNC:11427"
                     /db_xref="MIM:607207"
ORIGIN      
        1 mkgkeekegg arlgagggsp ekspsaqelk eqgnrlfvgr kypeaaacyg raitrnplva
       61 vyytnralcy lkmqqheqal adcrraleld gqsvkahffl gqcqlemesy deaianlqra
      121 yslakeqrln fgddipsalr iakkkrwnsi eerrihqese lhsylsrlia aerereleec
      181 qrnhegdedd shvraqqaci eakhdkymad mdelfsqvde krkkrdipdy lcgkisfelm
      241 repcitpsgi tydrkdieeh lqrvghfdpv trspltqeql ipnlamkevi dafisengwv
      301 edy
//
LOCUS       NP_001340233             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 3 [Homo sapiens].
ACCESSION   NP_001340233
VERSION     NP_001340233.1
DBSOURCE    REFSEQ: accession NM_001353304.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.119953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 3"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36689
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353304.1:228..1202"
                     /note="isoform 3 is encoded by transcript variant 66"
                     /db_xref="CCDS:CCDS94340.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnlikvltr didhnaahff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_569118                882 aa            linear   PRI 20-NOV-2025
DEFINITION  dipeptidyl peptidase 8 isoform 1 [Homo sapiens].
ACCESSION   NP_569118
VERSION     NP_569118.1
DBSOURCE    REFSEQ: accession NM_130434.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 882)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 882)
  AUTHORS   Li,K., Zhang,Y., Zhao,W., Wang,R., Li,Y., Wei,L., Wang,L., Chen,X.,
            Chen,Z., Liu,P., Nie,N., Tian,X. and Fu,R.
  TITLE     DPP8/9 inhibition attenuates the TGF-beta1-induced excessive
            deposition of extracellular matrix (ECM) in human mesangial cells
            via Smad and Akt signaling pathways
  JOURNAL   Toxicol Lett 395, 1-10 (2024)
   PUBMED   38458339
  REMARK    GeneRIF: DPP8/9 inhibition attenuates the TGF-beta1-induced
            excessive deposition of extracellular matrix (ECM) in human
            mesangial cells via Smad and Akt signaling pathways.
REFERENCE   3  (residues 1 to 882)
  AUTHORS   Zhang,Y., Li,K., Li,Y., Zhao,W., Wang,L., Chen,Z., Ma,X., Yao,T.,
            Wang,J., Dong,W., Li,X., Tian,X. and Fu,R.
  TITLE     Profibrotic mechanisms of DPP8 and DPP9 highly expressed in the
            proximal renal tubule epithelial cells
  JOURNAL   Pharmacol Res 169, 105630 (2021)
   PUBMED   33932609
  REMARK    GeneRIF: Profibrotic mechanisms of DPP8 and DPP9 highly expressed
            in the proximal renal tubule epithelial cells.
REFERENCE   4  (residues 1 to 882)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 882)
  AUTHORS   Hollingsworth,L.R., Sharif,H., Griswold,A.R., Fontana,P.,
            Mintseris,J., Dagbay,K.B., Paulo,J.A., Gygi,S.P., Bachovchin,D.A.
            and Wu,H.
  TITLE     DPP9 sequesters the C terminus of NLRP1 to repress inflammasome
            activation
  JOURNAL   Nature 592 (7856), 778-783 (2021)
   PUBMED   33731932
REFERENCE   6  (residues 1 to 882)
  AUTHORS   Chen,Y.S., Chien,C.H., Goparaju,C.M., Hsu,J.T., Liang,P.H. and
            Chen,X.
  TITLE     Purification and characterization of human prolyl dipeptidase DPP8
            in Sf9 insect cells
  JOURNAL   Protein Expr Purif 35 (1), 142-146 (2004)
   PUBMED   15039077
REFERENCE   7  (residues 1 to 882)
  AUTHORS   Shu,H., Chen,S., Bi,Q., Mumby,M. and Brekken,D.L.
  TITLE     Identification of phosphoproteins and their phosphorylation sites
            in the WEHI-231 B lymphoma cell line
  JOURNAL   Mol Cell Proteomics 3 (3), 279-286 (2004)
   PUBMED   14729942
REFERENCE   8  (residues 1 to 882)
  AUTHORS   Qi,S.Y., Riviere,P.J., Trojnar,J., Junien,J.L. and Akinsanya,K.O.
  TITLE     Cloning and characterization of dipeptidyl peptidase 10, a new
            member of an emerging subgroup of serine proteases
  JOURNAL   Biochem J 373 (Pt 1), 179-189 (2003)
   PUBMED   12662155
REFERENCE   9  (residues 1 to 882)
  AUTHORS   Ajami,K., Abbott,C.A., Obradovic,M., Gysbers,V., Kahne,T.,
            McCaughan,G.W. and Gorrell,M.D.
  TITLE     Structural requirements for catalysis, expression, and dimerization
            in the CD26/DPIV gene family
  JOURNAL   Biochemistry 42 (3), 694-701 (2003)
   PUBMED   12534281
REFERENCE   10 (residues 1 to 882)
  AUTHORS   Abbott,C.A., Yu,D.M., Woollatt,E., Sutherland,G.R., McCaughan,G.W.
            and Gorrell,M.D.
  TITLE     Cloning, expression and chromosomal localization of a novel human
            dipeptidyl peptidase (DPP) IV homolog, DPP8
  JOURNAL   Eur J Biochem 267 (20), 6140-6150 (2000)
   PUBMED   11012666
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011846.16, AF221634.1,
            AC105129.4 and BU753778.1.
            
            Summary: This gene encodes a member of the peptidase S9B family, a
            small family of dipeptidyl peptidases that are able to cleave
            peptide substrates at a prolyl bond. The encoded protein shares
            similarity with dipeptidyl peptidase IV in that it is ubiquitously
            expressed, and hydrolyzes the same substrates. These similarities
            suggest that, like dipeptidyl peptidase IV, this protein may play a
            role in T-cell activation and immune function. Alternatively
            spliced transcript variants encoding different isoforms have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes isoform 1. Both
            variants 1 and 8 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF221634.1, SRR3476690.698757.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300141.11/ ENSP00000300141.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..882
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..882
                     /product="dipeptidyl peptidase 8 isoform 1"
                     /EC_number="3.4.14.5"
                     /note="prolyl dipeptidase DPP8; dipeptidyl peptidase VIII;
                     DPP VIII; dipeptidyl peptidase IV-related protein 1"
                     /calculated_mol_wt=101291
     Region          1..146
                     /region_name="Dpp_8_9_N"
                     /note="Dipeptidyl peptidase 8 and 9 N-terminal; pfam19520"
                     /db_xref="CDD:466112"
     Region          159..579
                     /region_name="DPPIV_N"
                     /note="Dipeptidyl peptidase IV (DPP IV) N-terminal region;
                     pfam00930"
                     /db_xref="CDD:395744"
     Region          671..875
                     /region_name="Peptidase_S9"
                     /note="Prolyl oligopeptidase family; pfam00326"
                     /db_xref="CDD:459761"
     CDS             1..882
                     /gene="DPP8"
                     /gene_synonym="DP8; DPRP-1; DPRP1; MST097; MSTP097;
                     MSTP135; MSTP141"
                     /coded_by="NM_130434.5:216..2864"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10210.1"
                     /db_xref="GeneID:54878"
                     /db_xref="HGNC:HGNC:16490"
                     /db_xref="MIM:606819"
ORIGIN      
        1 maaameteql gveifetadc eeniesqdrp klepfyvery swsqlkklla dtrkyhgymm
       61 akaphdfmfv krndpdgphs driyylamsg enrentlfys eipktinraa vlmlswkpll
      121 dlfqatldyg mysreeellr erkrigtvgi asydyhqgsg tflfqagsgi yhvkdggpqg
      181 ftqqplrpnl vetscpnirm dpklcpadpd wiafihsndi wisnivtree rrltyvhnel
      241 anmeedarsa gvatfvlqee fdrysgywwc pkaettpsgg kilrilyeen deseveiihv
      301 tspmletrra dsfrypktgt anpkvtfkms eimidaegri idvidkeliq pfeilfegve
      361 yiaragwtpe gkyawsilld rsqtrlqivl ispelfipve ddvmerqrli esvpdsvtpl
      421 iiyeettdiw inihdifhvf pqsheeeief ifasecktgf rhlykitsil keskykrssg
      481 glpapsdfkc pikeeiaits gewevlgrhg sniqvdevrr lvyfegtkds plehhlyvvs
      541 yvnpgevtrl tdrgyshscc isqhcdffis kysnqknphc vslyklsspe ddptcktkef
      601 watildsagp lpdytppeif sfesttgftl ygmlykphdl qpgkkyptvl fiyggpqvql
      661 vnnrfkgvky frlntlaslg yvvvvidnrg schrglkfeg afkykmgqie iddqveglqy
      721 lasrydfidl drvgihgwsy ggylslmalm qrsdifrvai agapvtlwif ydtgyterym
      781 ghpdqneqgy ylgsvamqae kfpsepnrll llhgfldenv hfahtsills flvragkpyd
      841 lqiypqerhs irvpesgehy elhllhylqe nlgsriaalk vi
//
LOCUS       NP_001230160             625 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform g [Homo sapiens].
ACCESSION   NP_001230160
VERSION     NP_001230160.1
DBSOURCE    REFSEQ: accession NM_001243231.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 625)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AK096862.1 and
            AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (7) differs in the 5' UTR and
            coding sequence and uses an alternate in-frame splice site at the
            3' end of an exon compared to variant 3. The resulting isoform (g)
            has a shorter and distinct N-terminus and lacks an alternate
            internal segment compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK096862.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..625
                     /product="transcription factor 4 isoform g"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=66896
     Region          516..600
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(524,528,530..532,534,539,560..561)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(537..538,541..542,544..545,548,552,562,565,569,572,
                     575..580)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..625
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001243231.2:176..2053"
                     /note="isoform g is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS58628.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 meedsrdved rsssgswgng ghpspsrnyg dgtpydhmts rdlgshdnls ppfvnsriqs
       61 ktergsyssy gresnlqgch qqsllggdmd mgnpgtlspt kpgsqyyqys snnprrrplh
      121 ssamevqtkk vrkvppglps svyapsasta dynrdspgyp sskpatstfp ssffmqdghh
      181 ssdpwssssg mnqpgyagml gnsshipqss sycslhpher lsypshssad insslppmst
      241 fhrsgtnhys tssctppang tdsimanrgs gaagssqtgd algkalasiy spdhtnnsfs
      301 snpstpvgsp pslsagtavw srnggqasss pnyegplhsl qsriedrler lddaihvlrn
      361 havgpstamp gghgdmhgii gpshngamgg lgsgygtgll sanrhslmvg thredgvalr
      421 gshsllpnqv pvpqlpvqsa tspdlnppqd pyrgmppglq gqsvssgsse iksddegden
      481 lqdtkssedk kldddkkdik sitsnndded ltpeqkaere kerrmannar erlrvrdine
      541 afkelgrmvq lhlksdkpqt kllilhqava vilsleqqvr ernlnpkaac lkrreeekvs
      601 seppplslag phpgmgdasn hmgqm
//
LOCUS       NP_001123562             523 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 3 isoform a [Homo sapiens].
ACCESSION   NP_001123562
VERSION     NP_001123562.1
DBSOURCE    REFSEQ: accession NM_001130090.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Zhou,S., Yuan,S., Zhang,J., Meng,L., Zhang,X., Liu,S., Lu,G.,
            Lin,G., Liu,M. and Tan,Y.Q.
  TITLE     DRC3 is an assembly adapter of the nexin-dynein regulatory complex
            functional components during spermatogenesis in humans and mice
  JOURNAL   Signal Transduct Target Ther 8 (1), 26 (2023)
   PUBMED   36627292
  REMARK    GeneRIF: DRC3 is an assembly adapter of the nexin-dynein regulatory
            complex functional components during spermatogenesis in humans and
            mice.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Olbrich,H., Cremers,C., Loges,N.T., Werner,C., Nielsen,K.G.,
            Marthin,J.K., Philipsen,M., Wallmeier,J., Pennekamp,P., Menchen,T.,
            Edelbusch,C., Dougherty,G.W., Schwartz,O., Thiele,H., Altmuller,J.,
            Rommelmann,F. and Omran,H.
  TITLE     Loss-of-Function GAS8 Mutations Cause Primary Ciliary Dyskinesia
            and Disrupt the Nexin-Dynein Regulatory Complex
  JOURNAL   Am J Hum Genet 97 (4), 546-554 (2015)
   PUBMED   26387594
REFERENCE   6  (residues 1 to 523)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Wirschell,M., Olbrich,H., Werner,C., Tritschler,D., Bower,R.,
            Sale,W.S., Loges,N.T., Pennekamp,P., Lindberg,S., Stenram,U.,
            Carlen,B., Horak,E., Kohler,G., Nurnberg,P., Nurnberg,G.,
            Porter,M.E. and Omran,H.
  TITLE     The nexin-dynein regulatory complex subunit DRC1 is essential for
            motile cilia function in algae and humans
  JOURNAL   Nat Genet 45 (3), 262-268 (2013)
   PUBMED   23354437
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Bi,W., Yan,J., Stankiewicz,P., Park,S.S., Walz,K., Boerkoel,C.F.,
            Potocki,L., Shaffer,L.G., Devriendt,K., Nowaczyk,M.J., Inoue,K. and
            Lupski,J.R.
  TITLE     Genes in a refined Smith-Magenis syndrome critical deletion
            interval on chromosome 17p11.2 and the syntenic region of the mouse
  JOURNAL   Genome Res 12 (5), 713-728 (2002)
   PUBMED   11997338
REFERENCE   9  (residues 1 to 523)
  AUTHORS   Lucas,R.E., Vlangos,C.N., Das,P., Patel,P.I. and Elsea,S.H.
  TITLE     Genomic organisation of the approximately 1.5 Mb Smith-Magenis
            syndrome critical interval: transcription map, genomic contig, and
            candidate gene analysis
  JOURNAL   Eur J Hum Genet 9 (12), 892-902 (2001)
   PUBMED   11840190
REFERENCE   10 (residues 1 to 523)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB032678.1, BC050665.1 and AK093317.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Both variants 1 and
            2 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC050665.1, BC050419.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..523
                     /product="dynein regulatory complex subunit 3 isoform a"
                     /note="leucine-rich repeat-containing protein 48; leucine
                     rich repeat containing 48"
                     /calculated_mol_wt=60924
     Region          42..>188
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          44..65
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H069.2)"
     Region          47..65
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          66..87
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H069.2)"
     Region          67..88
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          88..109
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H069.2)"
     Region          89..110
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          110..131
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H069.2)"
     Region          111..132
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          132..153
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H069.2)"
     Region          133..157
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          158..169
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     CDS             1..523
                     /gene="DRC3"
                     /gene_synonym="CFAP134; LRRC48"
                     /coded_by="NM_001130090.1:380..1951"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45622.1"
                     /db_xref="GeneID:83450"
                     /db_xref="HGNC:HGNC:25384"
                     /db_xref="MIM:618758"
ORIGIN      
        1 mnqpcnsmep rvmdddmlkl avgdqgpqee agqlakqegi lfkdvlslql dfrnilridn
       61 lwqfenlrkl qldnniieki eglenlahlv wldlsfnnie tiegldtlvn ledlslfnnr
      121 iskidsldal vklqvlslgn nridnmmnii ylrrfkclrt lslsrnpise aedykmfica
      181 ylpdlmyldy rriddhtkkl aeakhqysid elkhqenlmq aqledeqaqr eelekhktaf
      241 vehlngsflf dsmyaedseg nnlsylpgvg elletykdkf viicvnifey glkqqekrkt
      301 eldtfsecvr eaiqenqeqg krkiakfeek hlsslsaire elelpniekm ilecsadise
      361 lfdalmtlem qlveqleeti nmfernivdm vglfienvqs lmaqcrdlen hhheklleis
      421 istlekiveg dldedlpndl ralfvdkdti vnavgashdi hllkidnred elvtrinswc
      481 trlidrihkd eimrnrkrvk einqyidhmq seldnlecgd ild
//
LOCUS       NP_598395                200 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 22 isoform b
            [Homo sapiens].
ACCESSION   NP_598395
VERSION     NP_598395.1
DBSOURCE    REFSEQ: accession NM_133640.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Rodriguez,P.Q., Unnersjo-Jess,D., Zambrano,S.S., Guo,J.,
            Moller-Hackbarth,K., Blom,H., Jahnukainen,T., Ebarasi,L. and
            Patrakka,J.
  TITLE     Inactivation of mediator complex protein 22 in podocytes results in
            intracellular vacuole formation, podocyte loss and premature death
  JOURNAL   Sci Rep 10 (1), 20037 (2020)
   PUBMED   33208756
  REMARK    GeneRIF: Inactivation of mediator complex protein 22 in podocytes
            results in intracellular vacuole formation, podocyte loss and
            premature death.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 200)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 200)
  AUTHORS   Angiolillo,A., Russo,G., Porcellini,A., Smaldone,S.,
            D'Alessandro,F. and Pietropaolo,C.
  TITLE     The human homologue of the mouse Surf5 gene encodes multiple
            alternatively spliced transcripts
  JOURNAL   Gene 284 (1-2), 169-178 (2002)
   PUBMED   11891058
  REMARK    GeneRIF: Hu-Surf5 encodes three different transcripts, Surf-5a,
            Surf-5b, and Surf-5c, which result from alternative splicing.
REFERENCE   7  (residues 1 to 200)
  AUTHORS   Duhig,T., Ruhrberg,C., Mor,O. and Fried,M.
  TITLE     The human Surfeit locus
  JOURNAL   Genomics 52 (1), 72-78 (1998)
   PUBMED   9740673
REFERENCE   8  (residues 1 to 200)
  AUTHORS   Garson,K., Duhig,T. and Fried,M.
  TITLE     Tissue-specific processing of the Surf-5 and Surf-4 mRNAs
  JOURNAL   Gene Expr 6 (4), 209-218 (1996)
   PUBMED   9196076
REFERENCE   9  (residues 1 to 200)
  AUTHORS   Garson,K., Duhig,T., Armes,N., Colombo,P. and Fried,M.
  TITLE     Surf5: a gene in the tightly clustered mouse surfeit locus is
            highly conserved and transcribed divergently from the rpL7A (Surf3)
            gene
  JOURNAL   Genomics 30 (2), 163-170 (1995)
   PUBMED   8586415
  REMARK    GeneRIF: This publication also contains human sequence.
REFERENCE   10 (residues 1 to 200)
  AUTHORS   Yon,J., Jones,T., Garson,K., Sheer,D. and Fried,M.
  TITLE     The organization and conservation of the human Surfeit gene cluster
            and its localization telomeric to the c-abl and can proto-oncogenes
            at chromosome band 9q34.1
  JOURNAL   Hum Mol Genet 2 (3), 237-240 (1993)
   PUBMED   8499913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY154869.1, AJ224359.1,
            GD160955.1 and AL772161.10.
            
            Summary: This gene encodes a protein component of the mediator
            complex, which functions in the regulation of transcription by
            bridging interactions between gene-specific regulatory factors, RNA
            polymerase II, and general transcription factors. Alternatively
            spliced transcript variants encoding different isoforms have been
            observed. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (b) represents the shorter
            transcript and encodes the longer isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ224359.1, SRR14038193.370109.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343730.10/ ENSP00000342343.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..200
                     /product="mediator of RNA polymerase II transcription
                     subunit 22 isoform b"
                     /note="surfeit locus protein 5; mediator of RNA polymerase
                     II transcription subunit 22"
                     /calculated_mol_wt=22090
     Region          20..121
                     /region_name="Med22"
                     /note="Surfeit locus protein 5 subunit 22 of Mediator
                     complex; pfam06179"
                     /db_xref="CDD:461845"
     Region          166..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15528.2)"
     CDS             1..200
                     /gene="MED22"
                     /gene_synonym="MED24; SRB6; surf-5; SURF5"
                     /coded_by="NM_133640.5:249..851"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS6963.1"
                     /db_xref="GeneID:6837"
                     /db_xref="HGNC:HGNC:11477"
                     /db_xref="MIM:185641"
ORIGIN      
        1 maqqralpqs ketllqsynk rlkddiksim dnfteiikta kiedetqvsr atqgeqdnye
       61 mhvraanivr ageslmklvs dlkqflilnd fpsvneaidq rnqqlrtlqe ecdrklitlr
      121 deisidlyel eeeyysssss lceandlplc eaygrldldt dsadglsapl laspepsagp
      181 lqvaapahsh aggpgpteha
//
LOCUS       NP_001291479             353 aa            linear   PRI 20-NOV-2025
DEFINITION  THUMP domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_001291479 XP_005255479
VERSION     NP_001291479.1
DBSOURCE    REFSEQ: accession NM_001304550.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Gamage,S.T., Khoogar,R., Manage,S.H., Crawford,M.C., Georgeson,J.,
            Polevoda,B.V., Sanders,C., Lee,K.A., Nance,K.D., Iyer,V.,
            Kustanovich,A., Perez,M., Thu,C.T., Nance,S.R., Amin,R.,
            Miller,C.N., Holewinski,R.J., Meyer,T., Koparde,V., Yang,A.,
            Jailwala,P., Nguyen,J.T., Andresson,T., Hunter,K., Gu,S.,
            Mock,B.A., Edmondson,E.F., Difilippantonio,S., Chari,R.,
            Schwartz,S., O'Connell,M.R., Chih-Chien Wu,C. and Meier,J.L.
  TITLE     Transfer RNA acetylation regulates in vivo mammalian stress
            signaling
  JOURNAL   bioRxiv (2024)
   PUBMED   39091849
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Broly,M., Polevoda,B.V., Awayda,K.M., Tong,N., Lentini,J.,
            Besnard,T., Deb,W., O'Rourke,D., Baptista,J., Ellard,S.,
            Almannai,M., Hashem,M., Abdulwahab,F., Shamseldin,H., Al-Tala,S.,
            Alkuraya,F.S., Leon,A., van Loon,R.L.E., Ferlini,A., Sanchini,M.,
            Bigoni,S., Ciorba,A., van Bokhoven,H., Iqbal,Z., Al-Maawali,A.,
            Al-Murshedi,F., Ganesh,A., Al-Mamari,W., Lim,S.C., Pais,L.S.,
            Brown,N., Riazuddin,S., Bezieau,S., Fu,D., Isidor,B., Cogne,B. and
            O'Connell,M.R.
  TITLE     THUMPD1 bi-allelic variants cause loss of tRNA acetylation and a
            syndromic neurodevelopmental disorder
  JOURNAL   Am J Hum Genet 109 (4), 587-600 (2022)
   PUBMED   35196516
  REMARK    GeneRIF: THUMPD1 bi-allelic variants cause loss of tRNA acetylation
            and a syndromic neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Li,K., Liu,J., Yang,X., Tu,Z., Huang,K. and Zhu,X.
  TITLE     Pan-cancer analysis of N4-acetylcytidine adaptor THUMPD1 as a
            predictor for prognosis and immunotherapy
  JOURNAL   Biosci Rep 41 (12) (2021)
   PUBMED   34762107
  REMARK    GeneRIF: Pan-cancer analysis of N4-acetylcytidine adaptor THUMPD1
            as a predictor for prognosis and immunotherapy.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Zhang,X., Jiang,G., Sun,M., Zhou,H., Miao,Y., Liang,M., Wang,E. and
            Zhang,Y.
  TITLE     Cytosolic THUMPD1 promotes breast cancer cells invasion and
            metastasis via the AKT-GSK3-Snail pathway
  JOURNAL   Oncotarget 8 (8), 13357-13366 (2017)
   PUBMED   28076326
  REMARK    GeneRIF: These results indicate that THUMPD1 promotes breast cancer
            cells invasion and migration via the AKT-GSK3beta-Snail pathway
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Sharma,S., Langhendries,J.L., Watzinger,P., Kotter,P., Entian,K.D.
            and Lafontaine,D.L.
  TITLE     Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine
            acetyltransferases that modify tRNAs assisted by the adaptor
            Tan1/THUMPD1
  JOURNAL   Nucleic Acids Res 43 (4), 2242-2258 (2015)
   PUBMED   25653167
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004381.1.
            
            On Jan 31, 2015 this sequence version replaced XP_005255479.1.
            
            Transcript Variant: This variant (2) differs in the 3' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640898.1, SRR1660807.131928.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..353
                     /product="THUMP domain-containing protein 1"
                     /note="THUMP domain containing 1"
                     /calculated_mol_wt=39184
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Region          45..254
                     /region_name="THUMP_THUMPD1_like"
                     /note="THUMP domain-containing protein 1-like; cd11717"
                     /db_xref="CDD:212586"
     Region          73..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Region          270..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     CDS             1..353
                     /gene="THUMPD1"
                     /gene_synonym="NEDSOA; Tan1"
                     /coded_by="NM_001304550.2:80..1141"
                     /db_xref="CCDS:CCDS10588.1"
                     /db_xref="GeneID:55623"
                     /db_xref="HGNC:HGNC:23807"
                     /db_xref="MIM:616662"
ORIGIN      
        1 maapaqqttq pgggkrkgka qyvlakrarr cdaggprqle pglqgilitc nmnerkcvee
       61 aysllneygd dmygpekftd kdqqpsgseg edddaeaalk kevgdikast emrlrrfqsv
      121 esgannvvfi rtlgiepekl vhhilqdmyk tkkkktrvil rmlpisgtck afledmkkya
      181 etflepwfka pnkgtfqivy ksrnnshvnr eevirelagi vctlnsenkv dltnpqytvv
      241 veiikavccl svvkdymlfr kynlqevvks pkdpsqlnsk qgngkeakle sadksdqnnt
      301 aegknnqqvp enteelgqtk ptsnpqvvne ggakpelasq ategsksnen dfs
//
LOCUS       NP_003305                292 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 1 [Homo sapiens].
ACCESSION   NP_003305 XP_001717218 XP_001723028 XP_001725180
VERSION     NP_003305.1
DBSOURCE    REFSEQ: accession NM_003314.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 292)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 292)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 292)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 292)
  AUTHORS   Kwan,D.H., Yung,L.Y., Ye,R.D. and Wong,Y.H.
  TITLE     Activation of Ras-dependent signaling pathways by G(14) -coupled
            receptors requires the adaptor protein TPR1
  JOURNAL   J Cell Biochem 113 (11), 3486-3497 (2012)
   PUBMED   22711498
  REMARK    GeneRIF: TPR1 is required for Galpha14 to stimulate Ras-dependent
            signaling pathways, but not for the propagation of signals along
            Ras-independent pathways.
REFERENCE   5  (residues 1 to 292)
  AUTHORS   Liu,A.M., Lo,R.Kh., Guo,E.X., Ho,M.K., Ye,R.D. and Wong,Y.H.
  TITLE     Galpha16 interacts with tetratricopeptide repeat 1 (TPR1) through
            its beta3 region to activate Ras independently of phospholipase
            Cbeta signaling
  JOURNAL   BMC Struct Biol 11, 17 (2011)
   PUBMED   21486497
  REMARK    GeneRIF: beta3 region of Galpha16 is essential for interaction with
            TPR1 and the subsequent activation of Ras
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 292)
  AUTHORS   Oh,W.K. and Song,J.
  TITLE     Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses
            Hsp70-HspBp1 complex formation
  JOURNAL   Mol Cells 16 (1), 84-91 (2003)
   PUBMED   14503850
  REMARK    GeneRIF: Results report cooperative interactions involving Hsp70,
            Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically
            denatured substrates.
REFERENCE   7  (residues 1 to 292)
  AUTHORS   Marty,C., Browning,D.D. and Ye,R.D.
  TITLE     Identification of tetratricopeptide repeat 1 as an adaptor protein
            that interacts with heterotrimeric G proteins and the small GTPase
            Ras
  JOURNAL   Mol Cell Biol 23 (11), 3847-3858 (2003)
   PUBMED   12748287
  REMARK    GeneRIF: Data show that tetratricopeptide repeat 1 is a novel
            adaptor protein for Ras and selected Galpha proteins that may be
            involved in protein-protein interaction relating to G-protein
            signaling.
REFERENCE   8  (residues 1 to 292)
  AUTHORS   Franchimont,D., Martens,H., Hagelstein,M.T., Louis,E., Dewe,W.,
            Chrousos,G.P., Belaiche,J. and Geenen,V.
  TITLE     Tumor necrosis factor alpha decreases, and interleukin-10
            increases, the sensitivity of human monocytes to dexamethasone:
            potential regulation of the glucocorticoid receptor
  JOURNAL   J Clin Endocrinol Metab 84 (8), 2834-2839 (1999)
   PUBMED   10443688
REFERENCE   9  (residues 1 to 292)
  AUTHORS   Zhao,S. and Sancar,A.
  TITLE     Human blue-light photoreceptor hCRY2 specifically interacts with
            protein serine/threonine phosphatase 5 and modulates its activity
  JOURNAL   Photochem Photobiol 66 (5), 727-731 (1997)
   PUBMED   9383998
REFERENCE   10 (residues 1 to 292)
  AUTHORS   Murthy,A.E., Bernards,A., Church,D., Wasmuth,J. and Gusella,J.F.
  TITLE     Identification and characterization of two novel tetratricopeptide
            repeat-containing genes
  JOURNAL   DNA Cell Biol 15 (9), 727-735 (1996)
   PUBMED   8836031
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP245572.1 and U46570.1.
            
            On or before Jun 10, 2008 this sequence version replaced
            XP_001723028.1, XP_001725180.1, XP_001717218.1.
            
            Summary: This gene encodes a protein that belongs to the tetratrico
            peptide repeat superfamily of proteins. The encoded protein plays a
            role in protein-protein interactions, and binds to the Galpha
            subunit of G protein-coupled receptors to activate the Ras
            signaling pathway. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1063557.1,
                                           SRR3476690.281072.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231238.10/ ENSP00000231238.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..292
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..292
                     /product="tetratricopeptide repeat protein 1"
                     /note="TPR repeat protein 1"
                     /calculated_mol_wt=33395
     Region          23..125
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99614.1)"
     Region          49..>221
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99614.1)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q99614.1)"
     Region          116..149
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99614.1)"
     Region          119..144
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(120..121,124..125,127,156,159..160,163..164,
                     166..167,190,193..194,197..198,201)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          149..184
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          155..188
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99614.1)"
     Region          189..222
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99614.1)"
     Region          189..217
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..292
                     /gene="TTC1"
                     /gene_synonym="TPR1"
                     /coded_by="NM_003314.3:85..963"
                     /db_xref="CCDS:CCDS4348.1"
                     /db_xref="GeneID:7265"
                     /db_xref="HGNC:HGNC:12391"
                     /db_xref="MIM:601963"
ORIGIN      
        1 mgeksencgv pedllnglkv tdtqeaecag ppvpdpknqh sqskllrdde ahlqedqgee
       61 ecfhdcsasf eeepgadkve nksnedvnss eldeeyliel eknmsdeekq krreestrlk
      121 eegneqfkkg dyieaessys ralemcpscf qkersilfsn raaarmkqdk kemaindcsk
      181 aiqlnpsyir ailrraelye ktdkldeale dyksilekdp sihqareacm rlpkqieern
      241 erlkeemlgk lkdlgnlvlr pfglstenfq ikqdsstgsy sinfvqnpnn nr
//
LOCUS       NP_001356485             184 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform a [Homo sapiens].
ACCESSION   NP_001356485
VERSION     NP_001356485.1
DBSOURCE    REFSEQ: accession NM_001369556.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD387471.1, CD387461.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..184
                     /product="large ribosomal subunit protein uL22 isoform a"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21266
     Region          1..165
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     Region          160..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18621.3)"
     CDS             1..184
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369556.1:110..664"
                     /note="isoform a is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS45865.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl
      181 mare
//
LOCUS       NP_963889                337 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription initiation factor IIA subunit 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_963889
VERSION     NP_963889.1
DBSOURCE    REFSEQ: accession NM_201595.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 337)
  AUTHORS   DeJong,J., Bernstein,R. and Roeder,R.G.
  TITLE     Human general transcription factor TFIIA: characterization of a
            cDNA encoding the small subunit and requirement for basal and
            activated transcription
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3313-3317 (1995)
   PUBMED   7724559
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Ozer,J., Moore,P.A., Bolden,A.H., Lee,A., Rosen,C.A. and
            Lieberman,P.M.
  TITLE     Molecular cloning of the small (gamma) subunit of human TFIIA
            reveals functions critical for activated transcription
  JOURNAL   Genes Dev 8 (19), 2324-2335 (1994)
   PUBMED   7958899
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Ha,I., Lane,W.S. and Reinberg,D.
  TITLE     Cloning of a human gene encoding the general transcription
            initiation factor IIB
  JOURNAL   Nature 352 (6337), 689-695 (1991)
   PUBMED   1876184
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL136040.5 and D14886.1.
            
            Summary: Accurate transcription initiation on TATA-containing class
            II genes involves the ordered assembly of RNA polymerase II
            (POLR2A; MIM 180660) and several general initiation factors
            (summarized by DeJong and Roeder, 1993 [PubMed 8224848]). One of
            these factors is TFIIA, which when purified from HeLa extracts
            consists of 35-, 19-, and 12-kD subunits.[supplied by OMIM, Jul
            2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream, in-frame start codon, compared to variant 1. The
            encoded isoform (2) has a shorter N-terminus, compared to isoform
            1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1027091.1,
                                           SRR14038194.3923653.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.1"
     Protein         1..337
                     /product="transcription initiation factor IIA subunit 1
                     isoform 2"
                     /note="glucose regulated protein, 58kD pseudogene; general
                     transcription factor IIA, 1, 19/37kDa; TFIIA alpha/beta
                     subunits; transcription initiation factor IIA subunit 1;
                     general transcription factor IIA 1; transcription
                     initiation factor TFIIA 42 kDa subunit"
                     /calculated_mol_wt=37021
     Region          1..337
                     /region_name="TFIIA"
                     /note="Transcription factor IIA, alpha/beta subunit;
                     pfam03153"
                     /db_xref="CDD:460829"
     CDS             1..337
                     /gene="GTF2A1"
                     /gene_synonym="TF2A1; TFIIA; TFIIA-42; TFIIAL"
                     /coded_by="NM_201595.3:331..1344"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9874.1"
                     /db_xref="GeneID:2957"
                     /db_xref="HGNC:HGNC:4646"
                     /db_xref="MIM:600520"
ORIGIN      
        1 melktlwenk lmqsravdgf hseeqqlllq vqqqhqpqqq qhhhhhhhqq aqpqqtvpqq
       61 aqtqqvlipa sqqatapqvi vpdskliqhm nasnmsaaat aatlalpagv tpvqqiltns
      121 gqllqvvraa ngaqyifqpq qsvvlqqqvi pqmqpggvqa pviqqvlapl pggispqtgv
      181 iiqpqqilft gnktqviptt vaaptpaqaq itatgqqqpq aqpaqtqapl vlqvdgtgdt
      241 sseededeee dydddeeedk ekdgaedgqv eeeplnsedd vsdeegqelf dtenvvvcqy
      301 dkihrsknkw kfhlkdgimn lngrdyifsk aigdaew
//
LOCUS       NP_001269163             227 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-6 isoform c [Homo sapiens].
ACCESSION   NP_001269163 XP_005267925
VERSION     NP_001269163.1
DBSOURCE    REFSEQ: accession NM_001282234.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Nederlof,P.M., Wang,H.R. and Baumeister,W.
  TITLE     Nuclear localization signals of human and Thermoplasma proteasomal
            alpha subunits are functional in vitro
  JOURNAL   Proc Natl Acad Sci U S A 92 (26), 12060-12064 (1995)
   PUBMED   8618844
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 227)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Bey,F., Silva Pereira,I., Coux,O., Viegas-Pequignot,E., Recillas
            Targa,F., Nothwang,H.G., Dutrillaux,B. and Scherrer,K.
  TITLE     The prosomal RNA-binding protein p27K is a member of the alpha-type
            human prosomal gene family
  JOURNAL   Mol Gen Genet 237 (1-2), 193-205 (1993)
   PUBMED   7681138
REFERENCE   10 (residues 1 to 227)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AA090836.1, HY028439.1,
            AK302008.1 and BQ009843.1.
            
            On Aug 24, 2013 this sequence version replaced XP_005267925.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. Multiple transcript variants encoding several different
            isoforms have been found for this gene. A pseudogene has been
            identified on the Y chromosome. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (4) has an alternate first exon
            compared to variant 1. The resulting isoform (c) has a shorter and
            distinct N-terminus compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.61349.1,
                                           SRR1163658.468735.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..227
                     /product="proteasome subunit alpha type-6 isoform c"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit iota; prosomal P27K protein;
                     proteasome subunit iota; proteasome iota chain; proteasome
                     subunit alpha 6; proteasome subunit alpha1; macropain iota
                     chain; multicatalytic endopeptidase complex iota chain; 27
                     kDa prosomal protein; PROS-27; proteasome (prosome,
                     macropain) subunit, alpha type, 6; testicular secretory
                     protein Li 44; alpha-1; proteasome subunit alpha-1"
                     /calculated_mol_wt=25159
     Region          7..201
                     /region_name="proteasome_alpha_type_6"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03754"
                     /db_xref="CDD:239723"
     Site            order(18,34,36,49,151)
                     /site_type="active"
                     /db_xref="CDD:239723"
     CDS             1..227
                     /gene="PSMA6"
                     /gene_synonym="IOTA; p27K; PROS27"
                     /coded_by="NM_001282234.1:143..826"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS61437.1"
                     /db_xref="GeneID:5687"
                     /db_xref="HGNC:HGNC:9535"
                     /db_xref="MIM:602855"
ORIGIN      
        1 maglrreyaf kainqgglts vavrgkdcav ivtqkkvpdk lldsstvthl fkitenigcv
       61 mtgmtadsrs qvqraryeaa nwkykygyei pvdmlckria disqvytqna emrplgccmi
      121 ligideeqgp qvykcdpagy ycgfkataag vkqtestsfl ekkvkkkfdw tfeqtvetai
      181 tclstvlsid fkpseievgv vtvenpkfri lteaeidahl valaerd
//
LOCUS       NP_000972                196 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL19 isoform 1 [Homo sapiens].
ACCESSION   NP_000972 XP_001126177
VERSION     NP_000972.1
DBSOURCE    REFSEQ: accession NM_000981.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Cai,Z., Wu,Y., Zhang,F. and Wu,H.
  TITLE     A three-gene signature and clinical outcome in pediatric acute
            myeloid leukemia
  JOURNAL   Clin Transl Oncol 23 (4), 866-873 (2021)
   PUBMED   32862280
  REMARK    GeneRIF: A three-gene signature and clinical outcome in pediatric
            acute myeloid leukemia.
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Davies,B. and Fried,M.
  TITLE     The L19 ribosomal protein gene (RPL19): gene organization,
            chromosomal mapping, and novel promoter region
  JOURNAL   Genomics 25 (2), 372-380 (1995)
   PUBMED   7789970
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Henry,J.L., Coggin,D.L. and King,C.R.
  TITLE     High-level expression of the ribosomal protein L19 in human breast
            tumors that overexpress erbB-2
  JOURNAL   Cancer Res 53 (6), 1403-1408 (1993)
   PUBMED   8095182
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Kumabe,T., Sohma,Y. and Yamamoto,T.
  TITLE     Human cDNAs encoding elongation factor 1 gamma and the ribosomal
            protein L19
  JOURNAL   Nucleic Acids Res 20 (10), 2598 (1992)
   PUBMED   1598220
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Feo,S., Davies,B. and Fried,M.
  TITLE     The mapping of seven intron-containing ribosomal protein genes
            shows they are unlinked in the human genome
  JOURNAL   Genomics 13 (1), 201-207 (1992)
   PUBMED   1577483
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Chan,Y.L., Lin,A., McNally,J., Peleg,D., Meyuhas,O. and Wool,I.G.
  TITLE     The primary structure of rat ribosomal protein L19. A determination
            from the sequence of nucleotides in a cDNA and from the sequence of
            amino acids in the protein
  JOURNAL   J Biol Chem 262 (3), 1111-1115 (1987)
   PUBMED   3542997
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC095445.1 and CF129418.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 20, 2006 this sequence version replaced XP_001126177.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L19E family of ribosomal proteins. It is located in the
            cytoplasm. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC095445.1, SRR5189664.134613.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000225430.9/ ENSP00000225430.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..196
                     /product="large ribosomal subunit protein eL19 isoform 1"
                     /EC_number="6.3.5.5"
                     /note="60S ribosomal protein L19; large ribosomal subunit
                     protein eL19"
                     /calculated_mol_wt=23335
     Region          4..167
                     /region_name="Ribosomal_L19e_E"
                     /note="Ribosomal protein L19e, eukaryotic. L19e is found
                     in the large ribosomal subunit of eukaryotes and archaea.
                     L19e is distinct from the ribosomal subunit L19, which is
                     found in prokaryotes. It consists of two small globular
                     domains connected by an...; cd01417"
                     /db_xref="CDD:238705"
     Site            order(4,8..9,18..24,26,29,38,42,53,55..60,62,64,66..67,
                     69..70,72,74..79,81..89,92,95..97,100..101,103,110,
                     117..118,120..121,124..126,129,131,134..135)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238705"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P84098.1)"
     Site            28..47
                     /site_type="active"
                     /note="putative translocon docking site [active]"
                     /db_xref="CDD:238705"
     Site            order(112..113,115..119,139..149)
                     /site_type="active"
                     /note="putative intersubunit bridge [active]"
                     /db_xref="CDD:238705"
     Region          157..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P84098.1)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P84098.1)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P84098.1)"
     CDS             1..196
                     /gene="RPL19"
                     /gene_synonym="eL19; L19"
                     /coded_by="NM_000981.4:63..653"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42312.1"
                     /db_xref="GeneID:6143"
                     /db_xref="HGNC:HGNC:10312"
                     /db_xref="MIM:180466"
ORIGIN      
        1 msmlrlqkrl assvlrcgkk kvwldpnetn eianansrqq irklikdgli irkpvtvhsr
       61 arcrkntlar rkgrhmgigk rkgtanarmp ekvtwmrrmr ilrrllrryr eskkidrhmy
      121 hslylkvkgn vfknkrilme hihklkadka rkklladqae arrsktkear krreerlqak
      181 keeiiktlsk eeetkk
//
LOCUS       NP_001182181             270 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform i [Homo sapiens].
ACCESSION   NP_001182181
VERSION     NP_001182181.2
DBSOURCE    REFSEQ: accession NM_001195252.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 270)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 270)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 270)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 270)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 270)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 270)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 270)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 270)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 270)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Apr 23, 2019 this sequence version replaced NP_001182181.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Transcript Variant: This variant (11) differs in the 5' UTR and
            uses an alternate in-frame splice site in the 5' coding region,
            compared to variant 1. The encoded isoform (i) is shorter than
            isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY208831.1, SRR7346977.508966.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..270
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..270
                     /product="aprataxin isoform i"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=31134
     Region          3..89
                     /region_name="FHA"
                     /note="forkhead associated (FHA) domain superfamily;
                     cl00062"
                     /db_xref="CDD:469597"
     Site            order(28..29,41..42,44,64..65)
                     /site_type="other"
                     /note="phosphopeptide binding site [polypeptide binding]"
                     /db_xref="CDD:438714"
     Region          92..193
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(186,188,190..192)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            188
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          211..270
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..270
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001195252.2:67..879"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS94395.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mmrvcwlvrq dsrhqrirlp hleavvigrg petkitdkkc srqqvqlkae cnkgyvkvkq
       61 vgvnptsids vvigkdqevk lqpgqvlhme slghwsqglk ismqdpkmqv ykdeqvvvik
      121 dkypkaryhw lvlpwtsiss lkavarehle llkhmhtvge kvivdfagss klrfrlgyha
      181 ipsmshvhlh visqdfdspc lknkkhwnsf nteyflesqa viemvqeagr vtvrdgmpel
      241 lklplrchec qqllpsipql kehlrkhwtq
//
LOCUS       NP_002615                154 aa            linear   PRI 20-NOV-2025
DEFINITION  prefoldin subunit 5 isoform alpha [Homo sapiens].
ACCESSION   NP_002615
VERSION     NP_002615.2
DBSOURCE    REFSEQ: accession NM_002624.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Wen,P., Jiang,D., Qu,F., Wang,G., Zhang,N., Shao,Q., Huang,Y.,
            Li,S., Wang,L. and Zeng,X.
  TITLE     PFDN5 plays a dual role in breast cancer and regulates tumor immune
            microenvironment: Insights from integrated bioinformatics analysis
            and experimental validation
  JOURNAL   Gene 933, 149000 (2025)
   PUBMED   39396557
  REMARK    GeneRIF: PFDN5 plays a dual role in breast cancer and regulates
            tumor immune microenvironment: Insights from integrated
            bioinformatics analysis and experimental validation.
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Yu,F., Li,L., Gu,Y., Wang,S., Zhou,L., Cheng,X., Jiang,H.,
            Huang,Y., Zhang,Y., Qian,W., Li,X. and Liu,Z.
  TITLE     Lysine demethylase 5C inhibits transcription of prefoldin subunit 5
            to activate c-Myc signal transduction and colorectal cancer
            progression
  JOURNAL   Mol Med 30 (1), 9 (2024)
   PUBMED   38216914
  REMARK    GeneRIF: Lysine demethylase 5C inhibits transcription of prefoldin
            subunit 5 to activate c-Myc signal transduction and colorectal
            cancer progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Fujioka,Y., Taira,T., Maeda,Y., Tanaka,S., Nishihara,H.,
            Iguchi-Ariga,S.M., Nagashima,K. and Ariga,H.
  TITLE     MM-1, a c-Myc-binding protein, is a candidate for a tumor
            suppressor in leukemia/lymphoma and tongue cancer
  JOURNAL   J Biol Chem 276 (48), 45137-45144 (2001)
   PUBMED   11567024
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Cowan,N.J. and Lewis,S.A.
  TITLE     A chaperone with a hydrophilic surface
  JOURNAL   Nat Struct Biol 6 (11), 990-991 (1999)
   PUBMED   10542082
REFERENCE   8  (residues 1 to 154)
  AUTHORS   Hansen,W.J., Cowan,N.J. and Welch,W.J.
  TITLE     Prefoldin-nascent chain complexes in the folding of cytoskeletal
            proteins
  JOURNAL   J Cell Biol 145 (2), 265-277 (1999)
   PUBMED   10209023
REFERENCE   9  (residues 1 to 154)
  AUTHORS   Mori,K., Maeda,Y., Kitaura,H., Taira,T., Iguchi-Ariga,S.M. and
            Ariga,H.
  TITLE     MM-1, a novel c-Myc-associating protein that represses
            transcriptional activity of c-Myc
  JOURNAL   J Biol Chem 273 (45), 29794-29800 (1998)
   PUBMED   9792694
REFERENCE   10 (residues 1 to 154)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB055803.1 and AB055805.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 9, 2002 this sequence version replaced NP_002615.1.
            
            Summary: This gene encodes a member of the prefoldin alpha subunit
            family. The encoded protein is one of six subunits of prefoldin, a
            molecular chaperone complex that binds and stabilizes newly
            synthesized polypeptides, thereby allowing them to fold correctly.
            The complex, consisting of two alpha and four beta subunits, forms
            a double beta barrel assembly with six protruding coiled-coils. The
            encoded protein may also repress the transcriptional activity of
            the proto-oncogene c-Myc. Alternatively spliced transcript variants
            encoding different isoforms have been described. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB055803.1, SRR1163655.418136.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334478.9/ ENSP00000334188.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.13"
     Protein         1..154
                     /product="prefoldin subunit 5 isoform alpha"
                     /note="c-myc binding protein; myc modulator-1"
                     /calculated_mol_wt=17197
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99471.2)"
     Region          14..137
                     /region_name="Prefoldin_5"
                     /note="Prefoldin subunit 5; cd23157"
                     /db_xref="CDD:467473"
     Region          14..53
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467473"
     Site            order(42,45..46,49..50,52..53,60..67,69..78,81..85,89..94,
                     103)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467473"
     Site            42
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q99471.2)"
     Site            56
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99471.2)"
     Region          97..137
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467473"
     CDS             1..154
                     /gene="PFDN5"
                     /gene_synonym="MM-1; MM1; PFD5"
                     /coded_by="NM_002624.4:27..491"
                     /note="isoform alpha is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8853.1"
                     /db_xref="GeneID:5204"
                     /db_xref="HGNC:HGNC:8869"
                     /db_xref="MIM:604899"
ORIGIN      
        1 maqsinitel nlpqlemlkn qldqevefls tsiaqlkvvq tkyveakdcl nvlnksnegk
       61 ellvpltssm yvpgklhdve hvlidvgtgy yvektaedak dffkrkidfl tkqmekiqpa
      121 lqekhamkqa vmemmsqkiq qltalgaaqa taka
//
LOCUS       NP_003578               1041 aa            linear   PRI 20-NOV-2025
DEFINITION  pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16 isoform 1
            [Homo sapiens].
ACCESSION   NP_003578
VERSION     NP_003578.2
DBSOURCE    REFSEQ: accession NM_003587.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1041)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1041)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1041)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1041)
  AUTHORS   Hautakangas,M.R., Widgren,P., Korpelainen,P., Kangas,S.M.,
            Komulainen,T., Vieira,P., Rahikkala,E., Pylkas,K., Tuominen,H.,
            Kokkonen,H., Miinalainen,I., Nadaf,J., Majewski,J., Hinttala,R. and
            Uusimaa,J.
  TITLE     Infantile onset encephalomyopathy, retinopathy, optic atrophy, and
            mitochondrial DNA depletion associated with a novel pathogenic
            DHX16 variant
  JOURNAL   Clin Genet 104 (6), 686-693 (2023)
   PUBMED   37574199
  REMARK    GeneRIF: Infantile onset encephalomyopathy, retinopathy, optic
            atrophy, and mitochondrial DNA depletion associated with a novel
            pathogenic DHX16 variant.
REFERENCE   5  (residues 1 to 1041)
  AUTHORS   Hage,A., Bharaj,P., van Tol,S., Giraldo,M.I., Gonzalez-Orozco,M.,
            Valerdi,K.M., Warren,A.N., Aguilera-Aguirre,L., Xie,X., Widen,S.G.,
            Moulton,H.M., Lee,B., Johnson,J.R., Krogan,N.J., Garcia-Sastre,A.,
            Shi,P.Y., Freiberg,A.N. and Rajsbaum,R.
  TITLE     The RNA helicase DHX16 recognizes specific viral RNA to trigger
            RIG-I-dependent innate antiviral immunity
  JOURNAL   Cell Rep 38 (10), 110434 (2022)
   PUBMED   35263596
  REMARK    GeneRIF: The RNA helicase DHX16 recognizes specific viral RNA to
            trigger RIG-I-dependent innate antiviral immunity.
REFERENCE   6  (residues 1 to 1041)
  AUTHORS   Shiina,T., Ota,M., Shimizu,S., Katsuyama,Y., Hashimoto,N.,
            Takasu,M., Anzai,T., Kulski,J.K., Kikkawa,E., Naruse,T., Kimura,N.,
            Yanagiya,K., Watanabe,A., Hosomichi,K., Kohara,S., Iwamoto,C.,
            Umehara,Y., Meyer,A., Wanner,V., Sano,K., Macquin,C., Ikeo,K.,
            Tokunaga,K., Gojobori,T., Inoko,H. and Bahram,S.
  TITLE     Rapid evolution of major histocompatibility complex class I genes
            in primates generates new disease alleles in humans via hitchhiking
            diversity
  JOURNAL   Genetics 173 (3), 1555-1570 (2006)
   PUBMED   16702430
REFERENCE   7  (residues 1 to 1041)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   8  (residues 1 to 1041)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 1041)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
REFERENCE   10 (residues 1 to 1041)
  AUTHORS   Imamura,O., Saiki,K., Tani,T., Ohshima,Y., Sugawara,M. and
            Furuichi,Y.
  TITLE     Cloning and characterization of a human DEAH-box RNA helicase, a
            functional homolog of fission yeast Cdc28/Prp8
  JOURNAL   Nucleic Acids Res 26 (9), 2063-2068 (1998)
   PUBMED   9547260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB072495.1, BC008825.2 and
            BQ772493.1.
            
            On Aug 15, 2009 this sequence version replaced NP_003578.1.
            
            Summary: DEAD box proteins, characterized by the conserved motif
            Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are
            implicated in a number of cellular processes involving alteration
            of RNA secondary structure such as translation initiation, nuclear
            and mitochondrial splicing, and ribosome and spliceosome assembly.
            Based on their distribution patterns, some members of this family
            are believed to be involved in embryogenesis, spermatogenesis, and
            cellular growth and division. This gene encodes a DEAD box protein,
            which is a functional homolog of fission yeast Prp8 protein
            involved in cell cycle progression. This gene is mapped to the MHC
            region on chromosome 6p21.3, a region where many malignant, genetic
            and autoimmune disease genes are linked. Three transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, May 2018].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB001601.1, BC009392.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000376442.8/ ENSP00000365625.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1041
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.33"
     Protein         1..1041
                     /product="pre-mRNA-splicing factor ATP-dependent RNA
                     helicase DHX16 isoform 1"
                     /EC_number="3.6.4.13"
                     /note="ATP-dependent RNA helicase #3; DEAD/H
                     (Asp-Glu-Ala-Asp/His) box polypeptide 16; DEAD/H box 16;
                     putative pre-mRNA-splicing factor ATP-dependent RNA
                     helicase DHX16; DEAH-box protein 16; DEAH
                     (Asp-Glu-Ala-His) box polypeptide 16; pre-mRNA processing
                     factor 2"
                     /calculated_mol_wt=119133
     Region          101..207
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60231.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Region          <148..376
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Region          371..391
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Region          398..>1025
                     /region_name="HrpA"
                     /note="HrpA-like RNA helicase [Translation, ribosomal
                     structure and biogenesis]; COG1643"
                     /db_xref="CDD:441249"
     Region          520..523
                     /region_name="DEAH box"
                     /note="propagated from UniProtKB/Swiss-Prot (O60231.2)"
     Site            712
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60231.2)"
     CDS             1..1041
                     /gene="DHX16"
                     /gene_synonym="DBP2; DDX16; NMOAS; PRO2014; Prp2; PRP8;
                     PRPF2"
                     /coded_by="NM_003587.5:166..3291"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4685.1"
                     /db_xref="GeneID:8449"
                     /db_xref="HGNC:HGNC:2739"
                     /db_xref="MIM:603405"
ORIGIN      
        1 matpaglerw vqdelhsvlg lserhvaqfl igtaqrctsa eefvqrlrdt dtldlsgpar
       61 dfalrlwnkv prkavvekpa raaerearal leknrsyrll edseesseet vsragsslqk
      121 krkkrkhlrk kreeeeeeea sekgkkktgg skqqtekpes edewertere rlqdleerda
      181 faervrqrdk drtrnvlers dkkayeeaqk rlkmaeedrk amvpelrkks rreylakrer
      241 ekledleael adeeflfgdv elsrherqel kykrrvrdla reyraageqe kleatnryhm
      301 pketrgqpar avdlveeesg apgeeqrrwe earlgaaslk fgardaasqe pkyqlvleee
      361 etiefvratq lqgdeepsap ptstqaqqke siqavrrslp vfpfreella aianhqvlii
      421 egetgsgktt qipqylfeeg ytnkgmkiac tqprrvaams vaarvaremg vklgnevgys
      481 irfedctser tvlrymtdgm llreflsepd lasysvvmvd eahertlhtd ilfglikdva
      541 rfrpelkvlv asatmdtarf stffddapvf ripgrrfpvd ifytkapead yleacvvsvl
      601 qihvtqppgd ilvfltgqee ieaacemlqd rcrrlgskir ellvlpiyan lpsdmqarif
      661 qptppgarkv vvatniaets ltiegiiyvl dpgfckqksy nprtgmeslt vtpcskasan
      721 qragragrva agkcfrlyta wayqheleet tvpeiqrtsl gnvvlllksl gihdlmhfdf
      781 ldpppyetll laleqlyalg alnhlgeltt sgrkmaelpv dpmlskmila sekyscseei
      841 ltvaamlsvn nsifyrpkdk vvhadnarvn fflpggdhlv llnvytqwae sgyssqwcye
      901 nfvqfrsmrr ardvreqleg llervevgls scqgdyirvr kaitagyfyh tarltrsgyr
      961 tvkqqqtvfi hpnsslfeqq prwllyhelv lttkefmrqv leiesswlle vaphyykake
     1021 ledphakkmp kkigktreel g
//
LOCUS       NP_004913               1094 aa            linear   PRI 20-NOV-2025
DEFINITION  protein transport protein Sec24C [Homo sapiens].
ACCESSION   NP_004913
VERSION     NP_004913.2
DBSOURCE    REFSEQ: accession NM_004922.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1094)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1094)
  AUTHORS   Tang,V.T. and Ginsburg,D.
  TITLE     Cargo selection in endoplasmic reticulum-to-Golgi transport and
            relevant diseases
  JOURNAL   J Clin Invest 133 (1), e163838 (2023)
   PUBMED   36594468
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1094)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1094)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1094)
  AUTHORS   Rebensburg,S.V., Wei,G., Larue,R.C., Lindenberger,J., Francis,A.C.,
            Annamalai,A.S., Morrison,J., Shkriabai,N., Huang,S.W.,
            KewalRamani,V., Poeschla,E.M., Melikyan,G.B. and Kvaratskhelia,M.
  TITLE     Sec24C is an HIV-1 host dependency factor crucial for virus
            replication
  JOURNAL   Nat Microbiol 6 (4), 435-444 (2021)
   PUBMED   33649557
  REMARK    GeneRIF: Sec24C is an HIV-1 host dependency factor crucial for
            virus replication.
REFERENCE   6  (residues 1 to 1094)
  AUTHORS   Kirchhausen,T.
  TITLE     Three ways to make a vesicle
  JOURNAL   Nat Rev Mol Cell Biol 1 (3), 187-198 (2000)
   PUBMED   11252894
  REMARK    Review article
            Erratum:[Nat Rev Mol Cell Biol 2001 Mar;2(3):216]
REFERENCE   7  (residues 1 to 1094)
  AUTHORS   Lippincott-Schwartz,J., Roberts,T.H. and Hirschberg,K.
  TITLE     Secretory protein trafficking and organelle dynamics in living
            cells
  JOURNAL   Annu Rev Cell Dev Biol 16, 557-589 (2000)
   PUBMED   11031247
  REMARK    Review article
REFERENCE   8  (residues 1 to 1094)
  AUTHORS   Tang,B.L., Kausalya,J., Low,D.Y., Lock,M.L. and Hong,W.
  TITLE     A family of mammalian proteins homologous to yeast Sec24p
  JOURNAL   Biochem Biophys Res Commun 258 (3), 679-684 (1999)
   PUBMED   10329445
REFERENCE   9  (residues 1 to 1094)
  AUTHORS   Tani,K., Oyama,Y., Hatsuzawa,K. and Tagaya,M.
  TITLE     Hypothetical protein KIAA0079 is a mammalian homologue of yeast
            Sec24p
  JOURNAL   FEBS Lett 447 (2-3), 247-250 (1999)
   PUBMED   10214955
REFERENCE   10 (residues 1 to 1094)
  AUTHORS   Pagano,A., Letourneur,F., Garcia-Estefania,D., Carpentier,J.L.,
            Orci,L. and Paccaud,J.P.
  TITLE     Sec24 proteins and sorting at the endoplasmic reticulum
  JOURNAL   J Biol Chem 274 (12), 7833-7840 (1999)
   PUBMED   10075675
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022400.9, AL596994.1,
            BQ710971.1, D38555.1 and CA419040.1.
            
            On Nov 18, 2003 this sequence version replaced NP_004913.1.
            
            Summary: The protein encoded by this gene is a member of the SEC24
            subfamily of the SEC23/SEC24 family, which is involved in vesicle
            trafficking. The encoded protein has similarity to yeast Sec24p
            component of COPII. COPII is the coat protein complex responsible
            for vesicle budding from the ER. The product of this gene may play
            a role in shaping the vesicle, as well as in cargo selection and
            concentration. Alternatively spliced transcript variants encoding
            the same protein have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript.  Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.74037.1,
                                           SRR1660803.188485.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1094
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..1094
                     /product="protein transport protein Sec24C"
                     /note="SEC24 family, member C; SEC24-related protein C;
                     SEC24 related gene family, member C; SEC24 homolog C,
                     COPII coat complex component"
                     /calculated_mol_wt=118194
     Region          1..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     Region          <4..329
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          181..1090
                     /region_name="COG5028"
                     /note="Vesicle coat complex COPII, subunit SEC24/subunit
                     SFB2/subunit SFB3 [Intracellular trafficking and
                     secretion]"
                     /db_xref="CDD:227361"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P53992.3)"
     Region          425..450
                     /region_name="Zinc finger-like"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     Region          962..1034
                     /region_name="Gelsolin-like. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P53992.3)"
     CDS             1..1094
                     /gene="SEC24C"
                     /coded_by="NM_004922.4:182..3466"
                     /db_xref="CCDS:CCDS7332.1"
                     /db_xref="GeneID:9632"
                     /db_xref="HGNC:HGNC:10705"
                     /db_xref="MIM:607185"
ORIGIN      
        1 mnvnqsvppv ppfgqpqpiy pgyhqssygg qsgstapaip ygayngpvpg yqqtppqgms
       61 rappssgapp astaqapcgq aaygqfgqgd vqngpsstvq mqrlpgsqpf gsplapvgnq
      121 ppvlqpygpp ptsaqvatql sgmqisgava pappssglgf gpptslasas gsfpnsglyg
      181 sypqgqappl sqaqghpgiq tpqrsapsqa ssftppasgg prlpsmtgpl lpgqsfggps
      241 vsqpnhvssp pqalppgtqm tgplgplppm hspqqpgyqp qqngsfgpar gpqsnyggpy
      301 paaptfgsqp gppqplppkr ldpdaipspi qvieddrnnr gtepfvtgvr gqvpplvttn
      361 flvkdqgnas pryirctsyn ipctsdmakq aqvplaavik plarlppeea spyvvdhges
      421 gplrcnrcka ymcpfmqfie ggrrfqccfc scindvppqy fqhldhtgkr vdaydrpels
      481 lgsyeflatv dycknnkfps ppafifmidv synairtglv rllceelksl ldflpregga
      541 eesairvgfv tynkvlhfyn vksslaqpqm mvvsdvadmf vplldgflvn vnesravits
      601 lldqipemfa dtretetvfv pviqagmeal kaaecagklf lfhtslpiae apgklknrdd
      661 rklintdkek tlfqpqtgay qtlakecvaq gccvdlflfp nqyvdvatls vvpqltggsv
      721 ykyasfqven dqerflsdlr rdvqkvvgfd avmrvrtstg iravdffgaf ymsnttdvel
      781 agldgdktvt vefkhddrln eesgallqca llytscagqr rlrihnlaln cctqladlyr
      841 ncetdtliny makfayrgvl nspvkavrdt litqcaqila cyrkncasps sagqlilpec
      901 mkllpvylnc vlksdvlqpg aevttddray vrqlvtsmdv tetnvffypr llpltkspve
      961 stteppavra seerlsngdi yllenglnlf lwvgasvqqg vvqslfsvss fsqitsglsv
     1021 lpvldnplsk kvrglidslr aqrsrymklt vvkqedkmem lfkhflvedk slsggasyvd
     1081 flchmhkeir qlls
//
LOCUS       NP_001317010             278 aa            linear   PRI 20-NOV-2025
DEFINITION  neurexin-1 isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001317010
VERSION     NP_001317010.1
DBSOURCE    REFSEQ: accession NM_001330081.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Sebastian,R., Jin,K., Pavon,N., Bansal,R., Potter,A., Song,Y.,
            Babu,J., Gabriel,R., Sun,Y., Aronow,B. and Pak,C.
  TITLE     Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids
  JOURNAL   Nat Commun 14 (1), 3770 (2023)
   PUBMED   37355690
  REMARK    GeneRIF: Schizophrenia-associated NRXN1 deletions induce
            developmental-timing- and cell-type-specific vulnerabilities in
            human brain organoids.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Rhoades,R., Henry,B., Prichett,D., Fang,Y. and Teng,S.
  TITLE     Computational Saturation Mutagenesis to Investigate the Effects of
            Neurexin-1 Mutations on AlphaFold Structure
  JOURNAL   Genes (Basel) 13 (5), 789 (2022)
   PUBMED   35627176
  REMARK    GeneRIF: Computational Saturation Mutagenesis to Investigate the
            Effects of Neurexin-1 Mutations on AlphaFold Structure.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Aksu Uzunhan,T. and Ayaz,A.
  TITLE     Homozygous exonic and intragenic NRXN1 deletion presenting as
            either West syndrome or autism spectrum disorder in two siblings
  JOURNAL   Clin Neurol Neurosurg 214, 107141 (2022)
   PUBMED   35101781
  REMARK    GeneRIF: Homozygous exonic and intragenic NRXN1 deletion presenting
            as either West syndrome or autism spectrum disorder in two
            siblings.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Yan,Q., Weyn-Vanhentenryck,S.M., Wu,J., Sloan,S.A., Zhang,Y.,
            Chen,K., Wu,J.Q., Barres,B.A. and Zhang,C.
  TITLE     Systematic discovery of regulated and conserved alternative exons
            in the mammalian brain reveals NMD modulating chromatin regulators
  JOURNAL   Proc Natl Acad Sci U S A 112 (11), 3445-3450 (2015)
   PUBMED   25737549
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Tabuchi,K. and Sudhof,T.C.
  TITLE     Structure and evolution of neurexin genes: insight into the
            mechanism of alternative splicing
  JOURNAL   Genomics 79 (6), 849-859 (2002)
   PUBMED   12036300
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Rowen,L., Young,J., Birditt,B., Kaur,A., Madan,A., Philipps,D.L.,
            Qin,S., Minx,P., Wilson,R.K., Hood,L. and Graveley,B.R.
  TITLE     Analysis of the human neurexin genes: alternative splicing and the
            generation of protein diversity
  JOURNAL   Genomics 79 (4), 587-597 (2002)
   PUBMED   11944992
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Ichtchenko,K., Hata,Y., Nguyen,T., Ullrich,B., Missler,M.,
            Moomaw,C. and Sudhof,T.C.
  TITLE     Neuroligin 1: a splice site-specific ligand for beta-neurexins
  JOURNAL   Cell 81 (3), 435-443 (1995)
   PUBMED   7736595
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Ullrich,B., Ushkaryov,Y.A. and Sudhof,T.C.
  TITLE     Cartography of neurexins: more than 1000 isoforms generated by
            alternative splicing and expressed in distinct subsets of neurons
  JOURNAL   Neuron 14 (3), 497-507 (1995)
   PUBMED   7695896
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Ushkaryov,Y.A., Petrenko,A.G., Geppert,M. and Sudhof,T.C.
  TITLE     Neurexins: synaptic cell surface proteins related to the
            alpha-latrotoxin receptor and laminin
  JOURNAL   Science 257 (5066), 50-56 (1992)
   PUBMED   1621094
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC007682.3.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that belongs to the neurexin family. Neurexins are cell-surface
            receptors that bind neuroligins to form Ca(2+)-dependent
            neurexin/neuroligin complexes at synapses in the central nervous
            system. This complex is required for efficient neurotransmission
            and is involved in the formation of synaptic contacts. Three
            members of this gene family have been studied in detail and are
            estimated to generate over 3,000 variants through the use of two
            alternative promoters (alpha and beta) and extensive alternative
            splicing in each family member. Recently, a third promoter (gamma)
            was identified for this gene in the 3' region. Mutations in this
            gene are associated with Pitt-Hopkins-like syndrome-2 and may
            contribute to susceptibility to schizophrenia. [provided by RefSeq,
            Aug 2016].
            
            Transcript Variant: This variant (7) lacks multiple 3' coding exons
            and contains an alternate 3' terminal exon compared to variant
            alpha2. The encoded isoform (7) is much shorter than isoform
            alpha2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046631.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1968832 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.3"
     Protein         1..278
                     /product="neurexin-1 isoform 7 precursor"
                     /note="neurexin I"
                     /calculated_mol_wt=27292
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3097
     Region          30..190
                     /region_name="LamG"
                     /note="Laminin G domain; Laminin G-like domains are
                     usually Ca++ mediated receptors that can have binding
                     sites for steroids, beta1 integrins, heparin, sulfatides,
                     fibulin-1, and alpha-dystroglycans. Proteins that contain
                     LamG domains serve a variety of...; cd00110"
                     /db_xref="CDD:238058"
     CDS             1..278
                     /gene="NRXN1"
                     /gene_synonym="Hs.22998; PTHSL2; SCZD17"
                     /coded_by="NM_001330081.2:1074..1910"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 7"
                     /db_xref="CCDS:CCDS86840.1"
                     /db_xref="GeneID:9378"
                     /db_xref="HGNC:HGNC:8008"
                     /db_xref="MIM:600565"
ORIGIN      
        1 mgtallqrgg cfllclslll lgcwaelgsg lefpgaegqw trfpkwnacc esemsfqlkt
       61 rsarglvlyf ddegfcdfle liltrggrlq lsfsifcaep atlladtpvn dgawhsvrir
      121 rqfrnttlfi dqveakwvev kskrrdmtvf sglfvgglpp elraaalklt lasvrerepf
      181 kgwirdvrvn ssqvlpvdsg evklddeppn sgggspceag eegeggvcln ggvcsvvddq
      241 avcdcsrtgf rgkdcsqedn nveglahlmm gdqgkskd
//
LOCUS       NP_004208                344 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 1 [Homo sapiens].
ACCESSION   NP_004208
VERSION     NP_004208.2
DBSOURCE    REFSEQ: accession NM_004217.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135178.13, BC000442.2 and
            BC009751.2.
            
            On Dec 21, 2005 this sequence version replaced NP_004208.1.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the predominant isoform (1). Variants 1 and
            4 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.562011.1,
                                           SRR5189652.192222.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000585124.6/ ENSP00000463999.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..344
                     /product="aurora kinase B isoform 1"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=39180
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            62
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Region          70..339
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(83..86,89,91,104,106,138,154..157,200,204..205,207,
                     217..218)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     Site            215
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000269|PubMed:26829474; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:14722118,
                     ECO:0000269|PubMed:26829474; propagated from
                     UniProtKB/Swiss-Prot (Q96GD4.3)"
     CDS             1..344
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_004217.4:72..1106"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11134.1"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 maqkensypw pygrqtapsg lstlpqrvlr kepvtpsalv lmsrsnvqpt aapgqkvmen
       61 ssgtpdiltr hftiddfeig rplgkgkfgn vylarekksh fivalkvlfk sqiekegveh
      121 qlrreieiqa hlhhpnilrl ynyfydrrri ylileyaprg elykelqksc tfdeqrtati
      181 meeladalmy chgkkvihrd ikpenlllgl kgelkiadfg wsvhapslrr ktmcgtldyl
      241 ppemiegrmh nekvdlwcig vlcyellvgn ppfesashne tyrrivkvdl kfpasvpmga
      301 qdliskllrh npserlplaq vsahpwvran srrvlppsal qsva
//
LOCUS       NP_612377                878 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-5 complex subunit beta-1 [Homo sapiens].
ACCESSION   NP_612377
VERSION     NP_612377.4
DBSOURCE    REFSEQ: accession NM_138368.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Mai,X., Wang,Y., Wang,X., Liu,M., Teng,F., Liu,Z., Su,M.Y. and
            Stjepanovic,G.
  TITLE     Structural basis for membrane remodeling by the AP5-SPG11-SPG15
            complex
  JOURNAL   Nat Struct Mol Biol 32 (8), 1334-1346 (2025)
   PUBMED   40175557
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Alford,J.E., Marongiu,M., Watkins,G.L. and Anderson,E.C.
  TITLE     Human Immunodeficiency Virus Type 2 (HIV-2) Gag Is Trafficked in an
            AP-3 and AP-5 Dependent Manner
  JOURNAL   PLoS One 11 (7), e0158941 (2016)
   PUBMED   27392064
  REMARK    GeneRIF: HIV-2 particle release was dependent on the adaptor
            protein complex AP-3 and the newly identified AP-5 complex, but
            much less so on AP-1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Hirst,J., Borner,G.H., Edgar,J., Hein,M.Y., Mann,M., Buchholz,F.,
            Antrobus,R. and Robinson,M.S.
  TITLE     Interaction between AP-5 and the hereditary spastic paraplegia
            proteins SPG11 and SPG15
  JOURNAL   Mol Biol Cell 24 (16), 2558-2569 (2013)
   PUBMED   23825025
  REMARK    GeneRIF: We propose AP-5, SPG15, SPG11 form a coat-like complex,
            with AP-5 involved in protein sorting, SPG15 facilitating docking
            of the coat onto membranes by interacting with PI3P via its FYVE
            domain, and SPG11 (possibly together with SPG15) forming a
            scaffold.
REFERENCE   5  (residues 1 to 878)
  AUTHORS   Hirst,J., Barlow,L.D., Francisco,G.C., Sahlender,D.A., Seaman,M.N.,
            Dacks,J.B. and Robinson,M.S.
  TITLE     The fifth adaptor protein complex
  JOURNAL   PLoS Biol 9 (10), e1001170 (2011)
   PUBMED   22022230
  REMARK    GeneRIF: AP-5 is an evolutionarily ancient complex, which is
            involved in endosomal sorting, and which has links with hereditary
            spastic paraplegia.
            Erratum:[PLoS Biol. 2012 Mar;10(3). doi:
            10.1371/annotation/89dff893-c156-44bb-a731-bfcc91843583]
REFERENCE   6  (residues 1 to 878)
  AUTHORS   Slabicki,M., Theis,M., Krastev,D.B., Samsonov,S., Mundwiller,E.,
            Junqueira,M., Paszkowski-Rogacz,M., Teyra,J., Heninger,A.K.,
            Poser,I., Prieur,F., Truchetto,J., Confavreux,C., Marelli,C.,
            Durr,A., Camdessanche,J.P., Brice,A., Shevchenko,A.,
            Pisabarro,M.T., Stevanin,G. and Buchholz,F.
  TITLE     A genome-scale DNA repair RNAi screen identifies SPG48 as a novel
            gene associated with hereditary spastic paraplegia
  JOURNAL   PLoS Biol 8 (6), e1000408 (2010)
   PUBMED   20613862
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 878)
  AUTHORS   Schroder,B., Wrocklage,C., Pan,C., Jager,R., Kosters,B.,
            Schafer,H., Elsasser,H.P., Mann,M. and Hasilik,A.
  TITLE     Integral and associated lysosomal membrane proteins
  JOURNAL   Traffic 8 (12), 1676-1686 (2007)
   PUBMED   17897319
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP001266.4, JQ313135.1 and BC109109.1.
            
            On Mar 7, 2012 this sequence version replaced NP_612377.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: JQ313135.1, DRR138518.188221.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000532090.3/ ENSP00000454303.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..878
                     /product="AP-5 complex subunit beta-1"
                     /note="AP-5 complex subunit beta; beta5; adaptor-related
                     protein complex 5 beta subunit; adaptor related protein
                     complex 5 beta 1 subunit"
                     /calculated_mol_wt=93819
     Region          <220..743
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Region          234..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2VPB7.4)"
     CDS             1..878
                     /gene="AP5B1"
                     /gene_synonym="AP-5; PP1030"
                     /coded_by="NM_138368.5:386..3022"
                     /db_xref="CCDS:CCDS58146.1"
                     /db_xref="GeneID:91056"
                     /db_xref="HGNC:HGNC:25104"
                     /db_xref="MIM:614367"
ORIGIN      
        1 mgplsrdawa qrlgafrasp safmagpege dlgrdllsdl rseklseqtk vsllalsmey
       61 paqlwpdasa aevaatslld tlvllpprps alrrplllaa ttalaaggal gptsgascrl
      121 lplllglaag sdlgrgfvpa seqrplqata ceclrelesc kpgllggslg llrgllgqeg
      181 pvqplsllla lalrntlvlq srvgaglggl ltdkvsptgg gpwdwtlvee gdgrlqpqap
      241 swpaaeegeg ersltarehs peearelraa viqlldtsyl ltpvaqaqll wllgwalrgl
      301 qgqppalfkp qlvrllgtaq ltllhamlal kaafgealft aqdealllrr ltlaaqhpal
      361 pppthlfylh cvlsfpenwp lgpegeeaap lllgpqlcrg llpsllhdpm allarlhllc
      421 llcaeeeeee kgqlpsprhy leellaglrq raaldggpra latlcfqasy lvacclagqp
      481 tvltplihgl aqlyqarpml aphfvdlldq vdselreplk vvlrqvvvsr pgrdealcwh
      541 lqmlakvadg daqsatlnfl qaaaahctnw dlqqgllrvc rallragvrg glvdllqvla
      601 rqledpdgrd harlyyilla hlaapklgva lgpslaapal asslvaenqg fvaalmvqea
      661 palvrlslgs hrvkgplpvl klqpealepi yslelrfrve gqlyapleav hvpclcpgrp
      721 arplllplqp rcpaparldv halyttstgl tchahlpplf vnfadlflpf pqppegaglg
      781 ffeelwdscl pegaesrvwc plgpqglegl vsrhlepfvv vaqpptsycv aihlppdskl
      841 llrleaalad gvpvalrtdd wavlplagdy lrglaaav
//
LOCUS       NP_001352335             466 aa            linear   PRI 20-NOV-2025
DEFINITION  cocaine esterase isoform 3 [Homo sapiens].
ACCESSION   NP_001352335
VERSION     NP_001352335.1
DBSOURCE    REFSEQ: accession NM_001365406.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 466)
  AUTHORS   Chen,X., Liu,Q., Chen,Y., Wang,L., Yang,R., Zhang,W., Pan,X.,
            Zhang,S., Chen,C., Wu,T., Xia,J., Cheng,B., Chen,X. and Ren,X.
  TITLE     Carboxylesterase 2 induces mitochondrial dysfunction via disrupting
            lipid homeostasis in oral squamous cell carcinoma
  JOURNAL   Mol Metab 65, 101600 (2022)
   PUBMED   36113774
  REMARK    GeneRIF: Carboxylesterase 2 induces mitochondrial dysfunction via
            disrupting lipid homeostasis in oral squamous cell carcinoma.
REFERENCE   2  (residues 1 to 466)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 466)
  AUTHORS   Shen,Y., Eades,W., Liu,W. and Yan,B.
  TITLE     The COVID-19 Oral Drug Molnupiravir Is a CES2 Substrate: Potential
            Drug-Drug Interactions and Impact of CES2 Genetic Polymorphism In
            Vitro
  JOURNAL   Drug Metab Dispos 50 (9), 1151-1160 (2022)
   PUBMED   35790245
  REMARK    GeneRIF: The COVID-19 Oral Drug Molnupiravir Is a CES2 Substrate:
            Potential Drug-Drug Interactions and Impact of CES2 Genetic
            Polymorphism In Vitro.
REFERENCE   4  (residues 1 to 466)
  AUTHORS   Song,Y.Q., Guan,X.Q., Weng,Z.M., Liu,J.L., Chen,J., Wang,L.,
            Cui,L.T., Fang,S.Q., Hou,J. and Ge,G.B.
  TITLE     Discovery of hCES2A inhibitors from Glycyrrhiza inflata via
            combination of docking-based virtual screening and
            fluorescence-based inhibition assays
  JOURNAL   Food Funct 12 (1), 162-176 (2021)
   PUBMED   33291124
  REMARK    GeneRIF: Discovery of hCES2A inhibitors from Glycyrrhiza inflata
            via combination of docking-based virtual screening and
            fluorescence-based inhibition assays.
REFERENCE   5  (residues 1 to 466)
  AUTHORS   Pei,J., Sun,X., Yang,G. and Zhang,S.
  TITLE     LncRNA KCNQ1OT1 ameliorates the liver injury induced by
            acetaminophen through the regulation of miR-122-5p/CES2 axis
  JOURNAL   Mol Cell Biochem 475 (1-2), 107-118 (2020)
   PUBMED   32779042
  REMARK    GeneRIF: LncRNA KCNQ1OT1 ameliorates the liver injury induced by
            acetaminophen through the regulation of miR-122-5p/CES2 axis.
REFERENCE   6  (residues 1 to 466)
  AUTHORS   Saito,S., Iida,A., Sekine,A., Kawauchi,S., Higuchi,S., Ogawa,C. and
            Nakamura,Y.
  TITLE     Catalog of 680 variations among eight cytochrome p450 (CYP) genes,
            nine esterase genes, and two other genes in the Japanese population
  JOURNAL   J Hum Genet 48 (5), 249-270 (2003)
   PUBMED   12721789
REFERENCE   7  (residues 1 to 466)
  AUTHORS   Chagnon,P., Michaud,J., Mitchell,G., Mercier,J., Marion,J.F.,
            Drouin,E., Rasquin-Weber,A., Hudson,T.J. and Richter,A.
  TITLE     A missense mutation (R565W) in cirhin (FLJ14728) in North American
            Indian childhood cirrhosis
  JOURNAL   Am J Hum Genet 71 (6), 1443-1449 (2002)
   PUBMED   12417987
REFERENCE   8  (residues 1 to 466)
  AUTHORS   Yan,B., Matoney,L. and Yang,D.
  TITLE     Human carboxylesterases in term placentae: enzymatic
            characterization, molecular cloning and evidence for the existence
            of multiple forms
  JOURNAL   Placenta 20 (7), 599-607 (1999)
   PUBMED   10452915
REFERENCE   9  (residues 1 to 466)
  AUTHORS   Pindel,E.V., Kedishvili,N.Y., Abraham,T.L., Brzezinski,M.R.,
            Zhang,J., Dean,R.A. and Bosron,W.F.
  TITLE     Purification and cloning of a broad substrate specificity human
            liver carboxylesterase that catalyzes the hydrolysis of cocaine and
            heroin
  JOURNAL   J Biol Chem 272 (23), 14769-14775 (1997)
   PUBMED   9169443
REFERENCE   10 (residues 1 to 466)
  AUTHORS   Schwer,H., Langmann,T., Daig,R., Becker,A., Aslanidis,C. and
            Schmitz,G.
  TITLE     Molecular cloning and characterization of a novel putative
            carboxylesterase, present in human intestine and liver
  JOURNAL   Biochem Biophys Res Commun 233 (1), 117-120 (1997)
   PUBMED   9144407
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK095522.1, BC032095.2 and
            BX538086.1.
            
            Summary: This gene encodes a member of the carboxylesterase large
            family. The family members are responsible for the hydrolysis or
            transesterification of various xenobiotics, such as cocaine and
            heroin, and endogenous substrates with ester, thioester, or amide
            bonds. They may participate in fatty acyl and cholesterol ester
            metabolism, and may play a role in the blood-brain barrier system.
            The protein encoded by this gene is the major intestinal enzyme and
            functions in intestine drug clearance. Alternatively spliced
            transcript variants have been found for this gene.[provided by
            RefSeq, Oct 2010].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            resulting in the use of a downtream start codon, relative to
            variant 1. The encoded isoform (3) has a shorter N-terminus than
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.121156.1, AK095522.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..466
                     /product="cocaine esterase isoform 3"
                     /EC_number="3.1.1.1"
                     /EC_number="3.1.1.84"
                     /EC_number="3.1.1.56"
                     /note="intestinal carboxylesterase; liver
                     carboxylesterase-2; carboxylesterase 2 (intestine, liver);
                     cocaine esterase; methylumbelliferyl-acetate deacetylase
                     2"
                     /calculated_mol_wt=51886
     Region          1..445
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(55..57,134..136,139,281,285..286,318,365,368)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(135,252,364)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     CDS             1..466
                     /gene="CES2"
                     /gene_synonym="CE-2; CES2A1; iCE; PCE-2"
                     /coded_by="NM_001365406.1:665..2065"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:8824"
                     /db_xref="HGNC:HGNC:1864"
                     /db_xref="MIM:605278"
ORIGIN      
        1 mclqdltave seflsqfnmt fpsdsmsedc lylsiytpah shegsnlpvm vwihggalvf
       61 gmaslydgsm laalenvvvv iiqyrlgvlg ffstgdkhat gnwgyldqva alrwvqqnia
      121 hfggnpdrvt ifgesaggts vsslvvspis qglfhgaime sgvallpgli assadvistv
      181 vanlsacdqv dsealvgclr gkskeeilai nkpfkmipgv vdgvflprhp qellasadfq
      241 pvpsivgvnn nefgwlipkv mriydtqkem dreasqaalq kmltllmlpp tfgdllreey
      301 igdngdpqtl qaqfqemmad smfvipalqv ahfqcsrapv yfyefqhqps wlknirpphm
      361 kadhgdelpf vfrsffggny ikfteeeeql srkmmkywan farngnpnge glphwplfdq
      421 eeqylqlnlq pavgralkah rlqfwkkalp qkiqeleepe erhtel
//
LOCUS       NP_056007               1216 aa            linear   PRI 20-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
            isoform a [Homo sapiens].
ACCESSION   NP_056007
VERSION     NP_056007.1
DBSOURCE    REFSEQ: accession NM_015192.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1216)
  AUTHORS   Dai,S., Wang,Q., Lyu,Y., Chen,Z., Liu,X., Zhao,G. and Zhang,H.
  TITLE     LncRNA AC100826.1 regulated PLCB1 to promote progression in
            non-small cell lung cancer
  JOURNAL   Thorac Cancer 15 (19), 1477-1489 (2024)
   PUBMED   38778543
  REMARK    GeneRIF: LncRNA AC100826.1 regulated PLCB1 to promote progression
            in non-small cell lung cancer.
REFERENCE   2  (residues 1 to 1216)
  AUTHORS   Chang,M., Cui,X., Sun,Q., Wang,Y., Liu,J., Sun,Z., Ren,J., Sun,Y.,
            Han,L. and Li,W.
  TITLE     Lnc-PLCB1 is stabilized by METTL14 induced m6A modification and
            inhibits Helicobacter pylori mediated gastric cancer by
            destabilizing DDX21
  JOURNAL   Cancer Lett 588, 216746 (2024)
   PUBMED   38387756
  REMARK    GeneRIF: Lnc-PLCB1 is stabilized by METTL14 induced m6A
            modification and inhibits Helicobacter pylori mediated gastric
            cancer by destabilizing DDX21.
REFERENCE   3  (residues 1 to 1216)
  AUTHORS   Wang,Y., Tu,Z., Zhao,W., Wang,L., Jiang,J., Gu,L., Li,M., Jiang,L.,
            Wang,Y. and Bi,Y.
  TITLE     PLCB1 Enhances Cell Migration and Invasion in Gastric Cancer Via
            Regulating Actin Cytoskeletal Remodeling and Epithelial-Mesenchymal
            Transition
  JOURNAL   Biochem Genet 61 (6), 2618-2632 (2023)
   PUBMED   37208557
  REMARK    GeneRIF: PLCB1 Enhances Cell Migration and Invasion in Gastric
            Cancer Via Regulating Actin Cytoskeletal Remodeling and
            Epithelial-Mesenchymal Transition.
REFERENCE   4  (residues 1 to 1216)
  AUTHORS   Wang,S.H., Cheng,J.Y., Tsai,H.H., Lo,T.C., Hung,J.T., Lin,C.C.,
            Lee,C.W., Ho,Y.H., Kuo,H.H., Yu,A.L. and Yu,J.
  TITLE     Conformational alteration in glycan induces phospholipase Cbeta1
            activation and angiogenesis
  JOURNAL   J Biomed Sci 29 (1), 105 (2022)
   PUBMED   36517806
  REMARK    GeneRIF: Conformational alteration in glycan induces phospholipase
            Cbeta1 activation and angiogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1216)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1216)
  AUTHORS   Hwang,S.C., Park,K.H., Ha,M.J., Noh,I.S., Park,T.B. and Lee,Y.H.
  TITLE     Distribution of phospholipase C isozymes in normal human lung
            tissue and their immunohistochemical localization
  JOURNAL   J Korean Med Sci 11 (4), 305-313 (1996)
   PUBMED   8878798
REFERENCE   7  (residues 1 to 1216)
  AUTHORS   Zini,N., Sabatelli,P., Faenza,I., Ognibene,A. and Maraldi,N.M.
  TITLE     Interleukin-1 alpha induces variations of the intranuclear amount
            of phosphatidylinositol 4,5-bisphosphate and phospholipase C beta 1
            in human osteosarcoma Saos-2 cells
  JOURNAL   Histochem J 28 (7), 495-504 (1996)
   PUBMED   8872139
REFERENCE   8  (residues 1 to 1216)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   9  (residues 1 to 1216)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1216)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB011153.3, AY004175.1,
            AL049593.10 and BQ184058.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene catalyzes the formation
            of inositol 1,4,5-trisphosphate and diacylglycerol from
            phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium
            as a cofactor and plays an important role in the intracellular
            transduction of many extracellular signals. This gene is activated
            by two G-protein alpha subunits, alpha-q and alpha-11. Two
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB011153.3, SRR1660807.77968.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338037.11/ ENSP00000338185.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p12.3"
     Protein         1..1216
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-1 isoform a"
                     /EC_number="3.1.4.11"
                     /note="triphosphoinositide phosphodiesterase;
                     phosphoinositidase C; monophosphatidylinositol
                     phosphodiesterase;
                     1-phosphatidyl-D-myo-inositol-4,5-bisphosphate;
                     inositoltrisphosphohydrolase; phospholipase C-I;
                     1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
                     beta-1; phospholipase C, beta 1
                     (phosphoinositide-specific); phosphoinositide
                     phospholipase C"
                     /calculated_mol_wt=138436
     Region          22..148
                     /region_name="PH_PLC_beta"
                     /note="Phospholipase C-beta (PLC-beta) pleckstrin homology
                     (PH) domain; cd13361"
                     /db_xref="CDD:270167"
     Site            order(27,29,40,57,122)
                     /site_type="other"
                     /note="Rac1 binding site [polypeptide binding]"
                     /db_xref="CDD:270167"
     Site            order(30,32,37,39,41,56..57)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270167"
     Region          153..303
                     /region_name="EFh_PI-PLCbeta1"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 1 (PI-PLC-beta1); cd16208"
                     /db_xref="CDD:320038"
     Region          153..182
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          186..215
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          224..253
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Site            236
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          270..303
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320038"
     Region          316..643
                     /region_name="PI-PLCc_beta"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta; cd08591"
                     /db_xref="CDD:176533"
     Site            order(331..332,361,363,378,412,479,481,569,596,598)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176533"
     Site            order(331,378)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176533"
     Site            order(332,361,363,412)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176533"
     Site            417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          469..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          677..796
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(694,720,751,753,755,757)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          834..891
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:P10894; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          903..939
                     /region_name="DUF1154"
                     /note="Protein of unknown function (DUF1154); pfam06631"
                     /db_xref="CDD:461969"
     Region          963..994
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            978
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          1003..1170
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     Region          1071..1095
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Region          1173..1216
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            1199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     Site            1200
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1B3; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ66.1)"
     CDS             1..1216
                     /gene="PLCB1"
                     /gene_synonym="DEE12; EIEE12; PI-PLC; PLC-154; PLC-beta-1;
                     PLC-I; PLC154; PLCB1A; PLCB1B"
                     /coded_by="NM_015192.4:387..4037"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13102.1"
                     /db_xref="GeneID:23236"
                     /db_xref="HGNC:HGNC:15917"
                     /db_xref="MIM:607120"
ORIGIN      
        1 magaqpgvha lqlkpvcvsd slkkgtkfvk wdddstivtp iilrtdpqgf ffywtdqnke
       61 telldlslvk darcgrhaka pkdpklrell dvgnigrleq rmitvvygpd lvnishlnlv
      121 afqeevakew tnevfslatn llaqnmsrda flekaytklk lqvtpegrip lkniyrlfsa
      181 drkrvetale acslpssrnd sipqedftpe vyrvflnnlc prpeidnifs efgakskpyl
      241 tvdqmmdfin lkqrdprlne ilypplkqeq vqvliekyep nnslarkgqi svdgfmryls
      301 geengvvspe kldlnedmsq plshyfinss hntyltagql agnssvemyr qvllsgcrcv
      361 eldcwkgrta eeepvithgf tmtteisfke vieaiaecaf ktspfpills fenhvdspkq
      421 qakmaeycrl ifgdallmep lekyplesgv plpspmdlmy kilvknkkks hkssegsgkk
      481 klseqasnty sdsssmfeps spgageadte sddddddddc kkssmdegta gseamateem
      541 snlvnyiqpv kfesfeiskk rnksfemssf vetkgleqlt kspvefveyn kmqlsriypk
      601 gtrvdssnym pqlfwnagcq mvalnfqtmd lamqinmgmy eyngksgyrl kpefmrrpdk
      661 hfdpftegiv dgivantlsv kiisgqflsd kkvgtyvevd mfglpvdtrr kafktktsqg
      721 navnpvweee pivfkkvvlp tlaclriavy eeggkfighr ilpvqairpg yhyiclrner
      781 nqpltlpavf vyievkdyvp dtyadvieal snpiryvnlm eqrakqlaal tledeeevkk
      841 eadpgetpse apsearttpa engvnhtttl tpkppsqalh sqpapgsvka paktedliqs
      901 vlteveaqti eelkqqksfv klqkkhykem kdlvkrhhkk ttdlikehtt kyneiqndyl
      961 rrraaleksa kkdskkksep sspdhgssti eqdlaaldae mtqklidlkd kqqqqllnlr
     1021 qeqyysekyq krehiklliq kltdvaeecq nnqlkklkei cekekkelkk kmdkkrqeki
     1081 teakskdksq meeektemir syiqevvqyi krleeaqskr qeklvekhke irqqildekp
     1141 klqveleqey qdkfkrlple ilefvqeamk gkisedsnhg saplslssdp gkvnhktpss
     1201 eelggdipgk efdtpl
//
LOCUS       NP_001121116             456 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit alpha-1 precursor [Homo
            sapiens].
ACCESSION   NP_001121116
VERSION     NP_001121116.1
DBSOURCE    REFSEQ: accession NM_001127644.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Amjad,M., Tabassum,A., Sher,K., Kumar,S., Zehra,S. and Fatima,S.
  TITLE     Impact of GABAA receptor gene variants (rs2279020 and rs211037) on
            the risk of predisposition to epilepsy: a case-control study
  JOURNAL   Neurol Sci 43 (7), 4431-4438 (2022)
   PUBMED   35150350
  REMARK    GeneRIF: Impact of GABAA receptor gene variants (rs2279020 and
            rs211037) on the risk of predisposition to epilepsy: a case-control
            study.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Kasaragod,V.B., Mortensen,M., Hardwick,S.W., Wahid,A.A.,
            Dorovykh,V., Chirgadze,D.Y., Smart,T.G. and Miller,P.S.
  TITLE     Mechanisms of inhibition and activation of extrasynaptic alphabeta
            GABAA receptors
  JOURNAL   Nature 602 (7897), 529-533 (2022)
   PUBMED   35140402
  REMARK    Erratum:[Nature. 2022 Apr;604(7905):E15. doi:
            10.1038/s41586-022-04663-8. PMID: 35332337]
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Riaz,M., Abbasi,M.H., Sheikh,N., Saleem,T. and Virk,A.O.
  TITLE     GABRA1 and GABRA6 gene mutations in idiopathic generalized epilepsy
            patients
  JOURNAL   Seizure 93, 88-94 (2021)
   PUBMED   34740144
  REMARK    GeneRIF: GABRA1 and GABRA6 gene mutations in idiopathic generalized
            epilepsy patients.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Kang,I., Lindquist,D.G., Kinane,T.B., Ercolani,L., Pritchard,G.A.
            and Miller,L.G.
  TITLE     Isolation and characterization of the promoter of the human GABAA
            receptor alpha 1 subunit gene
  JOURNAL   J Neurochem 62 (4), 1643-1646 (1994)
   PUBMED   8133292
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Johnson,K.J., Sander,T., Hicks,A.A., van Marle,A., Janz,D.,
            Mullan,M.J., Riley,B.P. and Darlison,M.G.
  TITLE     Confirmation of the localization of the human GABAA receptor alpha
            1-subunit gene (GABRA1) to distal 5q by linkage analysis
  JOURNAL   Genomics 14 (3), 745-748 (1992)
   PUBMED   1330891
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Schofield,P.R., Pritchett,D.B., Sontheimer,H., Kettenmann,H. and
            Seeburg,P.H.
  TITLE     Sequence and expression of human GABAA receptor alpha 1 and beta 1
            subunits
  JOURNAL   FEBS Lett 244 (2), 361-364 (1989)
   PUBMED   2465923
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Garrett,K.M., Duman,R.S., Saito,N., Blume,A.J., Vitek,M.P. and
            Tallman,J.F.
  TITLE     Isolation of a cDNA clone for the alpha subunit of the human GABA-A
            receptor
  JOURNAL   Biochem Biophys Res Commun 156 (2), 1039-1045 (1988)
   PUBMED   2847710
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA075784.1, X14766.1, R60404.1,
            DA228536.1 and AC021079.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammalian brain where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. Chloride conductance of these
            channels can be modulated by agents such as benzodiazepines that
            bind to the GABA-A receptor. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene cause juvenile
            myoclonic epilepsy and childhood absence epilepsy type 4. Multiple
            transcript variants encoding the same protein have been identified
            for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR,
            compared to variant 1. Variants 1-7 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.33690.1,
                                           SRR1660807.197895.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393943.10/ ENSP00000377517.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..456
                     /product="gamma-aminobutyric acid receptor subunit alpha-1
                     precursor"
                     /note="gamma-aminobutyric acid receptor subunit alpha-1;
                     GABA(A) receptor subunit alpha-1; GABA(A) receptor, alpha
                     1; gamma-aminobutyric acid (GABA) A receptor, alpha 1;
                     gamma-aminobutyric acid type A receptor alpha1 subunit;
                     GABAAR subunit alpha-1"
                     /calculated_mol_wt=48795
     sig_peptide     1..27
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14867.3)"
                     /calculated_mol_wt=3026
     Region          14..442
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     mat_peptide     28..456
                     /product="Gamma-aminobutyric acid receptor subunit
                     alpha-1. /id=PRO_0000000428"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
                     /calculated_mol_wt=48795
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P14867.3)"
     Region          56..249
                     /region_name="LGIC_ECD_GABAAR_A1"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit alpha-1 (GABAAR-A1 or GABRA1); cd19034"
                     /db_xref="CDD:349835"
     Site            order(64,92)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349835"
     Site            order(76,78..79,84..85,92,94..95,112,114..115,124..129,
                     132,134,136..137,143..145,147,157..159,187,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349835"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:29950725,
                     ECO:0000269|PubMed:30602789, ECO:0007744|PDB:6D6T,
                     ECO:0007744|PDB:6D6U, ECO:0007744|PDB:6I53; propagated
                     from UniProtKB/Swiss-Prot (P14867.3)"
     Region          166..180
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349835"
     Site            254..274
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            280..301
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            312..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     Site            422..441
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P14867.3)"
     CDS             1..456
                     /gene="GABRA1"
                     /gene_synonym="DEE19; ECA4; EIEE19; EJM; EJM5"
                     /coded_by="NM_001127644.2:319..1689"
                     /db_xref="CCDS:CCDS4357.1"
                     /db_xref="GeneID:2554"
                     /db_xref="HGNC:HGNC:4075"
                     /db_xref="MIM:137160"
ORIGIN      
        1 mrkspglsdc lwawilllst ltgrsygqps lqdelkdntt vftrildrll dgydnrlrpg
       61 lgervtevkt difvtsfgpv sdhdmeytid vffrqswkde rlkfkgpmtv lrlnnlmask
      121 iwtpdtffhn gkksvahnmt mpnkllrite dgtllytmrl tvraecpmhl edfpmdahac
      181 plkfgsyayt raevvyewtr eparsvvvae dgsrlnqydl lgqtvdsgiv qsstgeyvvm
      241 tthfhlkrki gyfviqtylp cimtvilsqv sfwlnresvp artvfgvttv ltmttlsisa
      301 rnslpkvaya tamdwfiavc yafvfsalie fatvnyftkr gyawdgksvv pekpkkvkdp
      361 likknntyap tatsytpnla rgdpglatia ksatiepkev kpetkppepk ktfnsvskid
      421 rlsriafpll fgifnlvywa tylnrepqlk aptphq
//
LOCUS       NP_001230060             164 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL13 isoform 3 [Homo sapiens].
ACCESSION   NP_001230060
VERSION     NP_001230060.1
DBSOURCE    REFSEQ: accession NM_001243131.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Costantini,A., Alm,J.J., Tonelli,F., Valta,H., Huber,C., Tran,A.N.,
            Daponte,V., Kirova,N., Kwon,Y.U., Bae,J.Y., Chung,W.Y., Tan,S.,
            Sznajer,Y., Nishimura,G., Nareoja,T., Warren,A.J.,
            Cormier-Daire,V., Kim,O.H., Forlino,A., Cho,T.J. and Makitie,O.
  TITLE     Novel RPL13 Variants and Variable Clinical Expressivity in a Human
            Ribosomopathy With Spondyloepimetaphyseal Dysplasia
  JOURNAL   J Bone Miner Res 36 (2), 283-297 (2021)
   PUBMED   32916022
  REMARK    GeneRIF: Novel RPL13 Variants and Variable Clinical Expressivity in
            a Human Ribosomopathy With Spondyloepimetaphyseal Dysplasia.
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Yaseen,N.R. and Blobel,G.
  TITLE     Cloning and characterization of human karyopherin beta3
  JOURNAL   Proc Natl Acad Sci U S A 94 (9), 4451-4456 (1997)
   PUBMED   9114010
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Adams,S.M., Helps,N.R., Sharp,M.G., Brammar,W.J., Walker,R.A. and
            Varley,J.M.
  TITLE     Isolation and characterization of a novel gene with differential
            expression in benign and malignant human breast tumours
  JOURNAL   Hum Mol Genet 1 (2), 91-96 (1992)
   PUBMED   1301162
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC106058.1, AK297198.1 and
            AC092123.4.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L13E family of ribosomal proteins. It is located in the
            cytoplasm. This gene is expressed at significantly higher levels in
            benign breast lesions than in breast carcinomas. Alternatively
            spliced transcript variants encoding distinct isoforms have been
            found for this gene. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Jul 2011].
            
            Transcript Variant: This variant (4) has an additional splice
            junction in the CDS, compared to variant 1. The resulting isoform
            (3) lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297198.1, DC350118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.3"
     Protein         1..164
                     /product="large ribosomal subunit protein eL13 isoform 3"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L13; breast basic conserved
                     protein 1; large ribosomal subunit protein eL13; breast
                     basic conserved 1"
                     /calculated_mol_wt=18714
     Region          8..140
                     /region_name="Ribosomal_L13e"
                     /note="Ribosomal protein L13e; cl01799"
                     /db_xref="CDD:470351"
     CDS             1..164
                     /gene="RPL13"
                     /gene_synonym="BBC1; D16S444E; D16S44E; eL13; L13;
                     SEMDIST"
                     /coded_by="NM_001243131.1:77..571"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58492.1"
                     /db_xref="GeneID:6137"
                     /db_xref="HGNC:HGNC:10303"
                     /db_xref="MIM:113703"
ORIGIN      
        1 mapsrngmvl kphfhkdwqr rvatwfnqpa rkirrrkarq akarriaprp asgpirpivr
       61 cptvryhtkv ragrgfslee lrvagihkkg dssaeelkla tqltgpvmpv rnvykkekar
      121 viteeeknfk afaslrmara narlfgirak rakeaaeqdv ekkk
//
LOCUS       NP_001518                488 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 2 [Homo sapiens].
ACCESSION   NP_001518
VERSION     NP_001518.3
DBSOURCE    REFSEQ: accession NM_001527.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 488)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 488)
  AUTHORS   Zhan,F., Zhang,R., Qiu,L. and Ren,Y.
  TITLE     ACAP3 negatively regulated by HDAC2 inhibits the malignant
            development of papillary thyroid carcinoma cells
  JOURNAL   Int J Biochem Cell Biol 174, 106635 (2024)
   PUBMED   39098591
  REMARK    GeneRIF: ACAP3 negatively regulated by HDAC2 inhibits the malignant
            development of papillary thyroid carcinoma cells.
REFERENCE   3  (residues 1 to 488)
  AUTHORS   Wang,M., Liao,J., Wang,J., Xu,M., Cheng,Y., Wei,L. and Huang,A.
  TITLE     HDAC2 promotes autophagy-associated HCC malignant progression by
            transcriptionally activating LAPTM4B
  JOURNAL   Cell Death Dis 15 (8), 593 (2024)
   PUBMED   39147759
  REMARK    GeneRIF: HDAC2 promotes autophagy-associated HCC malignant
            progression by transcriptionally activating LAPTM4B.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 488)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 488)
  AUTHORS   Maciejewski,K., Giers,M., Oleksiewicz,U. and Czerwinska,P.
  TITLE     The Epigenetic Modifiers HDAC2 and HDAC7 Inversely Associate with
            Cancer Stemness and Immunity in Solid Tumors
  JOURNAL   Int J Mol Sci 25 (14), 7841 (2024)
   PUBMED   39063083
  REMARK    GeneRIF: The Epigenetic Modifiers HDAC2 and HDAC7 Inversely
            Associate with Cancer Stemness and Immunity in Solid Tumors.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 488)
  AUTHORS   Hassig,C.A., Tong,J.K., Fleischer,T.C., Owa,T., Grable,P.G.,
            Ayer,D.E. and Schreiber,S.L.
  TITLE     A role for histone deacetylase activity in HDAC1-mediated
            transcriptional repression
  JOURNAL   Proc Natl Acad Sci U S A 95 (7), 3519-3524 (1998)
   PUBMED   9520398
REFERENCE   7  (residues 1 to 488)
  AUTHORS   Yang,W.M., Yao,Y.L., Sun,J.M., Davie,J.R. and Seto,E.
  TITLE     Isolation and characterization of cDNAs corresponding to an
            additional member of the human histone deacetylase gene family
  JOURNAL   J Biol Chem 272 (44), 28001-28007 (1997)
   PUBMED   9346952
REFERENCE   8  (residues 1 to 488)
  AUTHORS   Zhang,Y., Iratni,R., Erdjument-Bromage,H., Tempst,P. and
            Reinberg,D.
  TITLE     Histone deacetylases and SAP18, a novel polypeptide, are components
            of a human Sin3 complex
  JOURNAL   Cell 89 (3), 357-364 (1997)
   PUBMED   9150135
REFERENCE   9  (residues 1 to 488)
  AUTHORS   Laherty,C.D., Yang,W.M., Sun,J.M., Davie,J.R., Seto,E. and
            Eisenman,R.N.
  TITLE     Histone deacetylases associated with the mSin3 corepressor mediate
            mad transcriptional repression
  JOURNAL   Cell 89 (3), 349-356 (1997)
   PUBMED   9150134
  REMARK    GeneRIF: mSin3A interacts with HDAC2 via the HDAC-interacting
            domain (HID) of mSin3A.
REFERENCE   10 (residues 1 to 488)
  AUTHORS   Yang,W.M., Inouye,C., Zeng,Y., Bearss,D. and Seto,E.
  TITLE     Transcriptional repression by YY1 is mediated by interaction with a
            mammalian homolog of the yeast global regulator RPD3
  JOURNAL   Proc Natl Acad Sci U S A 93 (23), 12845-12850 (1996)
   PUBMED   8917507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK296856.1, BC031055.1 and
            FO393415.1.
            
            On Apr 2, 2010 this sequence version replaced NP_001518.2.
            
            Summary: This gene product belongs to the histone deacetylase
            family. Histone deacetylases act via the formation of large
            multiprotein complexes, and are responsible for the deacetylation
            of lysine residues at the N-terminal regions of core histones (H2A,
            H2B, H3 and H4). This protein forms transcriptional repressor
            complexes by associating with many different proteins, including
            YY1, a mammalian zinc-finger transcription factor. Thus, it plays
            an important role in transcriptional regulation, cell cycle
            progression and developmental events. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Apr 2010].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.896268.1,
                                           SRR14038196.2566080.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000519065.6/ ENSP00000430432.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..488
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
     Protein         1..488
                     /product="histone deacetylase 2"
                     /EC_number="3.5.1.98"
                     /note="transcriptional regulator homolog RPD3;
                     YY1-associated factor 1; protein deacylase HDAC2"
                     /calculated_mol_wt=55233
     Region          9..374
                     /region_name="HDAC2"
                     /note="Histone deacetylase 2 (HDAC2); cd10011"
                     /db_xref="CDD:212535"
     Region          9..322
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92769.2)"
     Site            75
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q92769.2)"
     Site            order(141..142,150..151,177,179,265,272,302,304)
                     /site_type="active"
                     /db_xref="CDD:212535"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q13547; propagated from
                     UniProtKB/Swiss-Prot (Q92769.2)"
     Region          389..488
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92769.2)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92769.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92769.2)"
     Site            422
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92769.2)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q92769.2)"
     CDS             1..488
                     /gene="HDAC2"
                     /gene_synonym="HD2; KDAC2; RPD3; YAF1"
                     /coded_by="NM_001527.4:241..1707"
                     /db_xref="CCDS:CCDS43493.2"
                     /db_xref="GeneID:3066"
                     /db_xref="HGNC:HGNC:4853"
                     /db_xref="MIM:605164"
ORIGIN      
        1 maysqgggkk kvcyyydgdi gnyyygqghp mkphrirmth nlllnyglyr kmeiyrphka
       61 taeemtkyhs deyikflrsi rpdnmseysk qmqrfnvged cpvfdglfef cqlstggsva
      121 gavklnrqqt dmavnwaggl hhakkseasg fcyvndivla ilellkyhqr vlyididihh
      181 gdgveeafyt tdrvmtvsfh kygeyfpgtg dlrdigagkg kyyavnfpmr dgiddesygq
      241 ifkpiiskvm emyqpsavvl qcgadslsgd rlgcfnltvk ghakcvevvk tfnlpllmlg
      301 gggytirnva rcwtyetava ldceipnelp yndyfeyfgp dfklhispsn mtnqntpeym
      361 ekikqrlfen lrmlphapgv qmqaipedav hedsgdedge dpdkrisira sdkriacdee
      421 fsdsedegeg grrnvadhkk gakkarieed kketedkktd vkeedkskdn sgektdtkgt
      481 kseqlsnp
//
LOCUS       NP_000349                683 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor-beta-induced protein ig-h3 precursor
            [Homo sapiens].
ACCESSION   NP_000349
VERSION     NP_000349.1
DBSOURCE    REFSEQ: accession NM_000358.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Pan,T., Liu,F., Hao,X., Wang,S., Wasi,M., Song,J.H., Lewis,V.O.,
            Lin,P.P., Moon,B., Bird,J.E., Panaretakis,T., Lin,S.H., Wu,D.,
            Farach-Carson,M.C., Wang,L., Zhang,N., An,Z., Zhang,X.H. and
            Satcher,R.L.
  TITLE     BIGH3 mediates apoptosis and gap junction failure in osteocytes
            during renal cell carcinoma bone metastasis progression
  JOURNAL   Cancer Lett 596, 217009 (2024)
   PUBMED   38849015
  REMARK    GeneRIF: BIGH3 mediates apoptosis and gap junction failure in
            osteocytes during renal cell carcinoma bone metastasis progression.
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Wang,H., Xu,Y.H. and Guo,Y.
  TITLE     Novel prognostic marker TGFBI affects the migration and invasion
            function of ovarian cancer cells and activates the integrin
            alphavbeta3-PI3K-Akt signaling pathway
  JOURNAL   J Ovarian Res 17 (1), 50 (2024)
   PUBMED   38395907
  REMARK    GeneRIF: Novel prognostic marker TGFBI affects the migration and
            invasion function of ovarian cancer cells and activates the
            integrin alphavbeta3-PI3K-Akt signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Gupta,V., Panigrahi,A., Somarajan,B.I., Gupta,S., Tripathy,K.,
            Singh,A., Sharma,A., Tandon,R., Pradhan,D., Sharma,A., Kushwaha,T.
            and Inampudi,K.K.
  TITLE     Distribution of TGFBI variants in patients with early onset
            glaucoma
  JOURNAL   Mol Vis 29, 365-377 (2023)
   PUBMED   38577561
  REMARK    GeneRIF: Distribution of TGFBI variants in patients with early
            onset glaucoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Li,M., Yang,E., Li,Y., Geng,Y., Wu,H. and Zhang,D.
  TITLE     Expression of TGFBI in infantile hemangioma tissues and its effect
            on the biological characteristics of hemangioma endothelial cells
  JOURNAL   Hua Xi Kou Qiang Yi Xue Za Zhi 41 (1), 29-36 (2023)
   PUBMED   38596938
  REMARK    GeneRIF: Expression of TGFBI in infantile hemangioma tissues and
            its effect on the biological characteristics of hemangioma
            endothelial cells.
REFERENCE   6  (residues 1 to 683)
  AUTHORS   LeBaron,R.G., Bezverkov,K.I., Zimber,M.P., Pavelec,R., Skonier,J.
            and Purchio,A.F.
  TITLE     Beta IG-H3, a novel secretory protein inducible by transforming
            growth factor-beta, is present in normal skin and promotes the
            adhesion and spreading of dermal fibroblasts in vitro
  JOURNAL   J Invest Dermatol 104 (5), 844-849 (1995)
   PUBMED   7738366
REFERENCE   7  (residues 1 to 683)
  AUTHORS   Escribano,J., Hernando,N., Ghosh,S., Crabb,J. and Coca-Prados,M.
  TITLE     cDNA from human ocular ciliary epithelium homologous to beta ig-h3
            is preferentially expressed as an extracellular protein in the
            corneal epithelium
  JOURNAL   J Cell Physiol 160 (3), 511-521 (1994)
   PUBMED   8077289
REFERENCE   8  (residues 1 to 683)
  AUTHORS   Skonier,J., Bennett,K., Rothwell,V., Kosowski,S., Plowman,G.,
            Wallace,P., Edelhoff,S., Disteche,C., Neubauer,M., Marquardt,H. et
            al.
  TITLE     beta ig-h3: a transforming growth factor-beta-responsive gene
            encoding a secreted protein that inhibits cell attachment in vitro
            and suppresses the growth of CHO cells in nude mice
  JOURNAL   DNA Cell Biol 13 (6), 571-584 (1994)
   PUBMED   8024701
REFERENCE   9  (residues 1 to 683)
  AUTHORS   Stone,E.M., Mathers,W.D., Rosenwasser,G.O., Holland,E.J.,
            Folberg,R., Krachmer,J.H., Nichols,B.E., Gorevic,P.D., Taylor,C.M.,
            Streb,L.M. et al.
  TITLE     Three autosomal dominant corneal dystrophies map to chromosome 5q
  JOURNAL   Nat Genet 6 (1), 47-51 (1994)
   PUBMED   8136834
REFERENCE   10 (residues 1 to 683)
  AUTHORS   Skonier,J., Neubauer,M., Madisen,L., Bennett,K., Plowman,G.D. and
            Purchio,A.F.
  TITLE     cDNA cloning and sequence analysis of beta ig-h3, a novel gene
            induced in a human adenocarcinoma cell line after treatment with
            transforming growth factor-beta
  JOURNAL   DNA Cell Biol 11 (7), 511-522 (1992)
   PUBMED   1388724
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA051240.1, BC000097.2 and
            M77349.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an RGD-containing protein that binds to
            type I, II and IV collagens. The RGD motif is found in many
            extracellular matrix proteins modulating cell adhesion and serves
            as a ligand recognition sequence for several integrins. This
            protein plays a role in cell-collagen interactions and may be
            involved in endochondrial bone formation in cartilage. The protein
            is induced by transforming growth factor-beta and acts to inhibit
            cell adhesion. Mutations in this gene are associated with multiple
            types of corneal dystrophy. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000097.2, AK094581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000442011.7/ ENSP00000416330.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..683
                     /product="transforming growth factor-beta-induced protein
                     ig-h3 precursor"
                     /note="transforming growth factor-beta-induced protein
                     ig-h3; betaig-h3; RGD-containing collagen-associated
                     protein; kerato-epithelin; RGD-CAP; beta ig-h3;
                     transforming growth factor, beta-induced, 68kD;
                     transforming growth factor beta-induced 68kDa"
                     /calculated_mol_wt=72418
     sig_peptide     1..23
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2281
     mat_peptide     24..683
                     /product="transforming growth factor-beta-induced protein
                     ig-h3"
                     /calculated_mol_wt=72418
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15582.1)"
     Region          133..236
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Region          253..373
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Region          386..500
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Region          514..634
                     /region_name="Fasciclin"
                     /note="Fasciclin domain; pfam02469"
                     /db_xref="CDD:396845"
     Region          642..644
                     /region_name="Cell attachment site. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15582.1)"
     CDS             1..683
                     /gene="TGFBI"
                     /gene_synonym="BIGH3; CDB1; CDG2; CDGG1; CSD; CSD1; CSD2;
                     CSD3; EBMD; LCD1"
                     /coded_by="NM_000358.3:69..2120"
                     /db_xref="CCDS:CCDS47266.1"
                     /db_xref="GeneID:7045"
                     /db_xref="HGNC:HGNC:11771"
                     /db_xref="MIM:601692"
ORIGIN      
        1 malfvrllal alalalgpaa tlagpakspy qlvlqhsrlr grqhgpnvca vqkvigtnrk
       61 yftnckqwyq rkicgkstvi syeccpgyek vpgekgcpaa lplsnlyetl gvvgstttql
      121 ytdrteklrp emegpgsfti fapsneawas lpaevldslv snvniellna lryhmvgrrv
      181 ltdelkhgmt ltsmyqnsni qihhypngiv tvncarllka dhhatngvvh lidkvistit
      241 nniqqiieie dtfetlraav aasglntmle gngqytllap tneafekips etlnrilgdp
      301 ealrdllnnh ilksamcaea ivaglsvetl egttlevgcs gdmltingka iisnkdilat
      361 ngvihyidel lipdsaktlf elaaesdvst aidlfrqagl gnhlsgserl tllaplnsvf
      421 kdgtppidah trnllrnhii kdqlaskyly hgqtletlgg kklrvfvyrn slcienscia
      481 ahdkrgrygt lftmdrvltp pmgtvmdvlk gdnrfsmlva aiqsagltet lnregvytvf
      541 aptneafral pprersrllg dakelanilk yhigdeilvs ggigalvrlk slqgdklevs
      601 lknnvvsvnk epvaepdima tngvvhvitn vlqppanrpq ergdeladsa leifkqasaf
      661 srasqrsvrl apvyqkller mkh
//
LOCUS       NP_001354399            1029 aa            linear   PRI 20-NOV-2025
DEFINITION  activating molecule in BECN1-regulated autophagy protein 1 isoform
            7 [Homo sapiens].
ACCESSION   NP_001354399
VERSION     NP_001354399.1
DBSOURCE    REFSEQ: accession NM_001367470.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1029)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1029)
  AUTHORS   Gottlieb,S., Shang,W., Ye,D., Kubo,S., Jiang,P.D., Shafer,S.,
            Xu,L., Zheng,L., Park,A.Y., Song,J., Chan,W., Zeng,Z., He,T.,
            Schwarz,B., Haupl,B., Oellerich,T., Lenardo,M.J. and Yao,Y.
  TITLE     AMBRA1 controls the translation of immune-specific genes in T
            lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2416722121 (2024)
   PUBMED   39436665
  REMARK    GeneRIF: AMBRA1 controls the translation of immune-specific genes
            in T lymphocytes.
REFERENCE   3  (residues 1 to 1029)
  AUTHORS   Sankar,D.S., Kaeser-Pebernard,S., Vionnet,C., Favre,S., de Oliveira
            Marchioro,L., Pillet,B., Zhou,J., Stumpe,M., Kovacs,W.J.,
            Kressler,D., Antonioli,M., Fimia,G.M. and Dengjel,J.
  TITLE     The ULK1 effector BAG2 regulates autophagy initiation by modulating
            AMBRA1 localization
  JOURNAL   Cell Rep 43 (9), 114689 (2024)
   PUBMED   39207901
  REMARK    GeneRIF: The ULK1 effector BAG2 regulates autophagy initiation by
            modulating AMBRA1 localization.
REFERENCE   4  (residues 1 to 1029)
  AUTHORS   Di Leo,L., Pagliuca,C., Kishk,A., Rizza,S., Tsiavou,C.,
            Pecorari,C., Dahl,C., Pacheco,M.P., Tholstrup,R., Brewer,J.R.,
            Berico,P., Hernando,E., Cecconi,F., Ballotti,R., Bertolotto,C.,
            Filomeni,G., Gjerstorff,M.F., Sauter,T., Lovat,P., Guldberg,P. and
            De Zio,D.
  TITLE     AMBRA1 levels predict resistance to MAPK inhibitors in melanoma
  JOURNAL   Proc Natl Acad Sci U S A 121 (25), e2400566121 (2024)
   PUBMED   38870061
  REMARK    GeneRIF: AMBRA1 levels predict resistance to MAPK inhibitors in
            melanoma.
REFERENCE   5  (residues 1 to 1029)
  AUTHORS   Qu,X., Li,X.Y., Feng,Y., Wang,X., Li,L., Wang,Y.P. and Chu,Y.L.
  TITLE     sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to reduce
            autophagy in gestational diabetes
  JOURNAL   Endokrynol Pol 75 (1), 61-70 (2024)
   PUBMED   38497391
  REMARK    GeneRIF: sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to
            reduce autophagy in gestational diabetes.
REFERENCE   6  (residues 1 to 1029)
  AUTHORS   Cecconi,F., Di Bartolomeo,S., Nardacci,R., Fuoco,C., Corazzari,M.,
            Giunta,L., Romagnoli,A., Stoykova,A., Chowdhury,K., Fimia,G.M. and
            Piacentini,M.
  TITLE     A novel role for autophagy in neurodevelopment
  JOURNAL   Autophagy 3 (5), 506-508 (2007)
   PUBMED   17622796
REFERENCE   7  (residues 1 to 1029)
  AUTHORS   Le Bot,N.
  TITLE     Autophagy: a new regulator of development
  JOURNAL   Nat Cell Biol 9 (7), 741 (2007)
   PUBMED   17603510
REFERENCE   8  (residues 1 to 1029)
  AUTHORS   Fimia,G.M., Stoykova,A., Romagnoli,A., Giunta,L., Di Bartolomeo,S.,
            Nardacci,R., Corazzari,M., Fuoco,C., Ucar,A., Schwartz,P.,
            Gruss,P., Piacentini,M., Chowdhury,K. and Cecconi,F.
  TITLE     Ambra1 regulates autophagy and development of the nervous system
  JOURNAL   Nature 447 (7148), 1121-1125 (2007)
   PUBMED   17589504
REFERENCE   9  (residues 1 to 1029)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1029)
  AUTHORS   Meyerson,M. and Harlow,E.
  TITLE     Identification of G1 kinase activity for cdk6, a novel cyclin D
            partner
  JOURNAL   Mol Cell Biol 14 (3), 2077-2086 (1994)
   PUBMED   8114739
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127035.6, AC115097.6, AC024293.18 and AC116021.5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.176312.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1029
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..1029
                     /product="activating molecule in BECN1-regulated autophagy
                     protein 1 isoform 7"
                     /note="WD repeat domain 94; DDB1 and CUL4 associated
                     factor 3; activating molecule in BECN1-regulated autophagy
                     protein 1; activating molecule in beclin-1-regulated
                     autophagy; autophagy/beclin-1 regulator 1"
                     /calculated_mol_wt=112425
     CDS             1..1029
                     /gene="AMBRA1"
                     /gene_synonym="DCAF3; WDR94"
                     /coded_by="NM_001367470.1:843..3932"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:55626"
                     /db_xref="HGNC:HGNC:25990"
                     /db_xref="MIM:611359"
ORIGIN      
        1 mervrlvrfd plghylltai vnpsnqqgdd epeipidgte lshyrqrall qsqpvrrtpl
       61 lhnflhmlss rssgiqtepf hppeqasstq qdqgllnrps afstvqssta gntlrnlslg
      121 ptrrslggpl sshpsryhre iapgltgsew trtvlslnsr seaesmpppr tsassvslls
      181 vlrqqeggsq asvytsateg rgfpasglat esdggngssq nnsgsirhel qcdlrrffle
      241 ydrlqeldqs lsgeapqtqq aqemlnnnie serpgpshqp tphssennsn lsrghlnrcr
      301 achnlltfnn dtlrwerttp nyssgeasss wqvpssfesv pssgsqlppl ertegqtpss
      361 srlelsssas pqeertvgva fnqetghwer iytqssrsgt vsqealhqdm peesseedsl
      421 rrrllessli slsrydgags rehpiypdpa rlspaayyaq rmiqylsrrd sirqrsmryq
      481 qnrlrsstss sssdnqgpsv egtdlefedf edngdrsrhr aprnarmsap slgrfvprrf
      541 llpeylpyag ifhergqpgl athssvnrvl agavigdgqs avasniantt yrlqwwdftk
      601 fdlpeisnas vnvlvqncki yndascdisa dgqllaafip ssqrgfpdeg ilavyslaph
      661 nlgemlytkr fgpnaisvsl spmgryvmvg lasrrillhp stehmvaqvf rlqqahgget
      721 smrrvfnvly pmpadqrrhv sinsarwlpe pglglaygtn kgdlvicrpe alnsgveyyw
      781 dqlnetvftv hsnsrsserp gtsratwrtd rdmglmnaig lqprnpatsv tsqgtqtlal
      841 qlqnaetqte revpepgtaa sgpgegegse ygasgedals riqrlmaegg mtavvqreqs
      901 ttmasmggfg nniivshrih rssqtgtepg aahtsspqps tsrgllpeag qlaerglspr
      961 taswdqpgtp greptqptlp ssspvpipvs lpsaegptlh celtnnnhll dggssrgdaa
     1021 gprgeprnr
//
LOCUS       NP_005868                793 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3A subunit 1 [Homo sapiens].
ACCESSION   NP_005868
VERSION     NP_005868.1
DBSOURCE    REFSEQ: accession NM_005877.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 793)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 793)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   3  (residues 1 to 793)
  AUTHORS   Nameki,N., Terawaki,S.I., Takizawa,M., Kitamura,M., Muto,Y. and
            Kuwasako,K.
  TITLE     Structural insights into recognition of SL4, the UUCG stem-loop, of
            human U1 snRNA by the ubiquitin-like domain, including the
            C-terminal tail in the SF3A1 subunit of U2 snRNP
  JOURNAL   J Biochem 174 (2), 203-216 (2023)
   PUBMED   37094335
  REMARK    GeneRIF: Structural insights into recognition of SL4, the UUCG
            stem-loop, of human U1 snRNA by the ubiquitin-like domain,
            including the C-terminal tail in the SF3A1 subunit of U2 snRNP.
REFERENCE   4  (residues 1 to 793)
  AUTHORS   Yang,F., Bian,T., Zhan,X., Chen,Z., Xing,Z., Larsen,N.A., Zhang,X.
            and Shi,Y.
  TITLE     Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP
            assembly
  JOURNAL   Nat Commun 14 (1), 897 (2023)
   PUBMED   36797247
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 793)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 793)
  AUTHORS   Kramer,A., Gruter,P., Groning,K. and Kastner,B.
  TITLE     Combined biochemical and electron microscopic analyses reveal the
            architecture of the mammalian U2 snRNP
  JOURNAL   J Cell Biol 145 (7), 1355-1368 (1999)
   PUBMED   10385517
REFERENCE   7  (residues 1 to 793)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   8  (residues 1 to 793)
  AUTHORS   Rain,J.C., Tartakoff,A.M., Kramer,A. and Legrain,P.
  TITLE     Essential domains of the PRP21 splicing factor are implicated in
            the binding to PRP9 and PRP11 proteins and are conserved through
            evolution
  JOURNAL   RNA 2 (6), 535-550 (1996)
   PUBMED   8718683
REFERENCE   9  (residues 1 to 793)
  AUTHORS   Kramer,A., Mulhauser,F., Wersig,C., Groning,K. and Bilbe,G.
  TITLE     Mammalian splicing factor SF3a120 represents a new member of the
            SURP family of proteins and is homologous to the essential splicing
            factor PRP21p of Saccharomyces cerevisiae
  JOURNAL   RNA 1 (3), 260-272 (1995)
   PUBMED   7489498
REFERENCE   10 (residues 1 to 793)
  AUTHORS   Chiara,M.D., Champion-Arnaud,P., Buvoli,M., Nadal-Ginard,B. and
            Reed,R.
  TITLE     Specific protein-protein interactions between the essential
            mammalian spliceosome-associated proteins SAP 61 and SAP 114
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6403-6407 (1994)
   PUBMED   8022796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC007684.2, AC004997.2 and
            CK300534.1.
            
            Summary: This gene encodes a subunit of the splicing factor 3a
            protein complex. The splicing factor 3a heterotrimer is a component
            of the mature U2 small nuclear ribonucleoprotein particle (snRNP).
            U2 small nuclear ribonucleoproteins play a critical role in
            spliceosome assembly and pre-mRNA splicing. [provided by RefSeq,
            Aug 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.875500.1,
                                           SRR3476690.853979.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000215793.13/ ENSP00000215793.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..793
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..793
                     /product="splicing factor 3A subunit 1"
                     /note="pre-mRNA splicing factor SF3a (120 kDa subunit);
                     pre-mRNA processing 21; splicing factor 3 subunit 1; SAP
                     114; spliceosome-associated protein 114; splicing factor
                     3a, subunit 1, 120kDa"
                     /calculated_mol_wt=88755
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Region          50..103
                     /region_name="SWAP"
                     /note="Suppressor-of-White-APricot splicing regulator;
                     smart00648"
                     /db_xref="CDD:197818"
     Region          52..94
                     /region_name="SURP motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            55
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Region          165..215
                     /region_name="Surp"
                     /note="Surp module; pfam01805"
                     /db_xref="CDD:460339"
     Region          166..208
                     /region_name="SURP motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            169
                     /site_type="other"
                     /note="Critical for binding to SF3A3; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Region          232..472
                     /region_name="PRP21_like_P"
                     /note="Pre-mRNA splicing factor PRP21 like protein;
                     pfam12230"
                     /db_xref="CDD:403444"
     Region          318..428
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            413
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Region          488..518
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Site            508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     Region          530..584
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Region          665..688
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Region          680..702
                     /region_name="Required and sufficient for nuclear import.
                     /evidence=ECO:0000269|PubMed:21349847"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15459.1)"
     Region          704..786
                     /region_name="Ubl_SF3a120"
                     /note="ubiquitin-like (Ubl) domain found in splicing
                     factor 3A 120kDa subunit (SF3a120) and similar proteins;
                     cd01800"
                     /db_xref="CDD:340498"
     Site            759
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q15459.1)"
     CDS             1..793
                     /gene="SF3A1"
                     /gene_synonym="PRP21; PRPF21; SAP114; SF3A120"
                     /coded_by="NM_005877.6:103..2484"
                     /db_xref="CCDS:CCDS13875.1"
                     /db_xref="GeneID:10291"
                     /db_xref="HGNC:HGNC:10765"
                     /db_xref="MIM:605595"
ORIGIN      
        1 mpagpvqavp ppppvptepk qpteeeassk edsapskpvv giiypppevr nivdktasfv
       61 arngpefear irqneinnpk fnflnpndpy hayyrhkvse fkegkaqeps aaipkvmqqq
      121 qqttqqqlpq kvqaqviqet ivpkepppef efiadppsis afdldvvklt aqfvarngrq
      181 fltqlmqkeq rnyqfdflrp qhslfnyftk lveqytkili ppkglfsklk keaenprevl
      241 dqvcyrvewa kfqererkke eeekekerva yaqidwhdfv vvetvdfqpn eqgnfppptt
      301 peelgarili qeryekfges eevemevesd eeddkqekae eppsqldqdt qvqdmdegsd
      361 deeegqkvpp ppetpmpppl pptpdqvivr kdydpkaskp lppapapdey lvspitgeki
      421 paskmqehmr iglldprwle qrdrsirekq sddevyapgl diesslkqla errtdifgve
      481 etaigkkige eeiqkpeekv twdghsgsma rtqqaaqani tlqeqieaih kakglvpedd
      541 tkekigpskp neipqqpppp ssatnipssa ppitsvprpp tmpppvrttv vsavpvmprp
      601 pmasvvrlpp gsviapmppi ihaprinvvp mppsappima prpppmivpt afvpappvap
      661 vpapapmppv hppppmedep tskklkteds lmpeeeflrr nkgpvsikvq vpnmqdktew
      721 klngqvlvft lpltdqvsvi kvkiheatgm pagkqklqye gifikdsnsl ayynmangav
      781 ihlalkergg rkk
//
LOCUS       NP_001350816             803 aa            linear   PRI 20-NOV-2025
DEFINITION  DISP complex protein LRCH3 isoform 1 [Homo sapiens].
ACCESSION   NP_001350816 XP_005269419
VERSION     NP_001350816.1
DBSOURCE    REFSEQ: accession NM_001363887.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 803)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 803)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 803)
  AUTHORS   O'Loughlin,T., Masters,T.A. and Buss,F.
  TITLE     The MYO6 interactome reveals adaptor complexes coordinating early
            endosome and cytoskeletal dynamics
  JOURNAL   EMBO Rep 19 (4) (2018)
   PUBMED   29467281
REFERENCE   6  (residues 1 to 803)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 803)
  AUTHORS   Foussard,H., Ferrer,P., Valenti,P., Polesello,C., Carreno,S. and
            Payre,F.
  TITLE     LRCH proteins: a novel family of cytoskeletal regulators
  JOURNAL   PLoS One 5 (8), e12257 (2010)
   PUBMED   20805893
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 803)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC055764.23, AC144530.11 and AC135893.2.
            
            On Jun 3, 2018 this sequence version replaced XP_005269419.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.87482.1,
                                           SRR1803613.61713.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..803
                     /product="DISP complex protein LRCH3 isoform 1"
                     /note="leucine-rich repeat and calponin homology
                     domain-containing protein 3; leucine-rich repeats and
                     calponin homology (CH) domain containing 3; DISP complex
                     protein LRCH3"
                     /calculated_mol_wt=88985
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <80..>286
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..145
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          152..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          175..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..218
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..242
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..261
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          654..763
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Site            order(662,717,719..720,723..724,726,740..744,751,753..754,
                     756..757,760..761)
                     /site_type="other"
                     /note="actin binding site [polypeptide binding]"
                     /db_xref="CDD:409119"
     CDS             1..803
                     /gene="LRCH3"
                     /coded_by="NM_001363887.1:54..2465"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS87193.1"
                     /db_xref="GeneID:84859"
                     /db_xref="HGNC:HGNC:28637"
ORIGIN      
        1 maaaglvava aaaeysgtva sggnlpgvhc gpssgagpgf gpgswsrsld raleeaavtg
       61 vlslsgrklr efprgaanhd ltdttradls rnrlseipie achfvslenl nlyqnciryi
      121 peailnlqal tflnisrnql stlpvhlcnl plkvliasnn klvslpeeig hlrhlmeldv
      181 scneiqtips qignlealrd lnvrrnhlvh lpeelaelpl irldfscnki ttipvcyrnl
      241 rhlqtitldn nplqsppaqi cikgkvhifk ylniqackia pdlpdydrrp lgfgscheel
      301 yssrpygald sgfnsvdsgd krwsgneptd efsdlplrva eitkeqrlrr esqyqenrgs
      361 lvvtnggveh dldqidyids ctaeeeeaev rqpkgpdpds lssqfmayie qrrishegsp
      421 vkpvairefq ktedmrrylh qnrvpaepss llslsashnq lshtdlelhq rreqlvertr
      481 reaqlaalqy eeekirtkqi qrdavldfvk qkasqspqkq hplldgvdge cpfpsrrsqh
      541 tddsalcmsl sglnqvgcaa tlphssaftp lksddrpnal lsspatetvh hspaysfpaa
      601 iqrnqpqrpe sflfragvra etnkghaspl ppsaapttds tdsitgqnsr qreeelelid
      661 qlrkhieyrl kvslpcdlga altdgvvlch lanhvrprsv psihvpspav pkltmakcrr
      721 nvenfleacr kigvpqdnlc spsdilqlnl svkrtvetll slgahseess fvclslqllg
      781 fvafyctvml tlcvlyywlf par
//
LOCUS       NP_742080                479 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit beta
            isoform 7 [Homo sapiens].
ACCESSION   NP_742080
VERSION     NP_742080.1
DBSOURCE    REFSEQ: accession NM_172083.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 479)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 479)
  AUTHORS   Borghi,R., Trivisano,M., Specchio,N., Tartaglia,M. and
            Compagnucci,C.
  TITLE     Understanding the pathogenetic mechanisms underlying altered
            neuronal function associated with CAMK2B mutations
  JOURNAL   Neurosci Biobehav Rev 152, 105299 (2023)
   PUBMED   37391113
  REMARK    GeneRIF: Understanding the pathogenetic mechanisms underlying
            altered neuronal function associated with CAMK2B mutations.
            Review article
REFERENCE   3  (residues 1 to 479)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 479)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 479)
  AUTHORS   Nicole,O. and Pacary,E.
  TITLE     CaMKIIbeta in Neuronal Development and Plasticity: An Emerging
            Candidate in Brain Diseases
  JOURNAL   Int J Mol Sci 21 (19), 7272 (2020)
   PUBMED   33019657
  REMARK    GeneRIF: CaMKIIbeta in Neuronal Development and Plasticity: An
            Emerging Candidate in Brain Diseases.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 479)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   7  (residues 1 to 479)
  AUTHORS   Penades,J.R., Bernal,D., Revert,F., Johansson,C., Fresquet,V.J.,
            Cervera,J., Wieslander,J., Quinones,S. and Saus,J.
  TITLE     Characterization and expression of multiple alternatively spliced
            transcripts of the Goodpasture antigen gene region. Goodpasture
            antibodies recognize recombinant proteins representing the
            autoantigen and one of its alternative forms
  JOURNAL   Eur J Biochem 229 (3), 754-760 (1995)
   PUBMED   7758473
REFERENCE   8  (residues 1 to 479)
  AUTHORS   Schworer,C.M., Colbran,R.J., Keefer,J.R. and Soderling,T.R.
  TITLE     Ca2+/calmodulin-dependent protein kinase II. Identification of a
            regulatory autophosphorylation site adjacent to the inhibitory and
            calmodulin-binding domains
  JOURNAL   J Biol Chem 263 (27), 13486-13489 (1988)
   PUBMED   3417668
REFERENCE   9  (residues 1 to 479)
  AUTHORS   Thiel,G., Czernik,A.J., Gorelick,F., Nairn,A.C. and Greengard,P.
  TITLE     Ca2+/calmodulin-dependent protein kinase II: identification of
            threonine-286 as the autophosphorylation site in the alpha subunit
            associated with the generation of Ca2+-independent activity
  JOURNAL   Proc Natl Acad Sci U S A 85 (17), 6337-6341 (1988)
   PUBMED   2842767
REFERENCE   10 (residues 1 to 479)
  AUTHORS   Bennett,M.K. and Kennedy,M.B.
  TITLE     Deduced primary structure of the beta subunit of brain type II
            Ca2+/calmodulin-dependent protein kinase determined by molecular
            cloning
  JOURNAL   Proc Natl Acad Sci U S A 84 (7), 1794-1798 (1987)
   PUBMED   3470758
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550751.1, DB175099.1,
            DA069361.1, AA399393.1, AJ252236.1, AC006454.4 and AK290148.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a beta chain.
            It is possible that distinct isoforms of this chain have different
            cellular localizations and interact differently with calmodulin.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (7), also known as beta 2, lacks
            an in-frame segment of the coding region, compared to variant 1. It
            encodes a shorter isoform (7), also known as beta 2 subunit, that
            is missing an internal segment compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ252237.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..479
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13"
     Protein         1..479
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit beta isoform 7"
                     /EC_number="2.7.11.17"
                     /note="CaM kinase II beta subunit; CaM-kinase II beta
                     chain; proline rich calmodulin-dependent protein kinase;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit beta; caMK-II subunit beta"
                     /calculated_mol_wt=53943
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          291..301
                     /region_name="calmodulin-binding domain"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          347..474
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..479
                     /gene="CAMK2B"
                     /gene_synonym="CAM2; CAMK2; CAMKB; CaMKIIbeta; MRD54"
                     /coded_by="NM_172083.3:174..1613"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS5488.1"
                     /db_xref="GeneID:816"
                     /db_xref="HGNC:HGNC:1461"
                     /db_xref="MIM:607707"
ORIGIN      
        1 mattvtctrf tdeyqlyedi gkgafsvvrr cvklctghey aakiintkkl sardhqkler
       61 earicrllkh snivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskckg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkea ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itahealkhp wvcqrstvas mmhrqetvec lkkfnarrkl
      301 kgailttmla trnfsaaksl lnkkadgvke ssdsanttie dedakarkqe iiktteqlie
      361 avnngdfeay akicdpglts fepealgnlv egmdfhrfyf enllaknskp ihttilnphv
      421 hvigedaaci ayirltqyid gqgrprtsqs eetrvwhrrd gkwqnvhfhc sgapvaplq
//
LOCUS       NP_115723                275 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 397 isoform 2 [Homo sapiens].
ACCESSION   NP_115723
VERSION     NP_115723.1
DBSOURCE    REFSEQ: accession NM_032347.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Bailey,S.L., Chang,S.C., Griffiths,B., Graham,A.N., Saffery,R.,
            Earle,E., Choo,K.H. and Kalitsis,P.
  TITLE     ZNF397, a new class of interphase to early prophase-specific,
            SCAN-zinc-finger, mammalian centromere protein
  JOURNAL   Chromosoma 117 (4), 367-380 (2008)
   PUBMED   18369653
  REMARK    GeneRIF: ZNF397, a new class of interphase to early
            prophase-specific, SCAN-zinc-finger, mammalian centromere protein.
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Lichter,P., Bray,P., Ried,T., Dawid,I.B. and Ward,D.C.
  TITLE     Clustering of C2-H2 zinc finger motif sequences within telomeric
            and fragile site regions of human chromosomes
  JOURNAL   Genomics 13 (4), 999-1007 (1992)
   PUBMED   1505991
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI772202.1, BC006172.1,
            AA805259.1 and AC011815.7.
            
            Summary: This gene encodes a protein with a N-terminal SCAN domain,
            and the longer isoform contains nine C2H2-type zinc finger repeats
            in the C-terminal domain. The protein localizes to centromeres
            during interphase and early prophase, and different isoforms can
            repress or activate transcription in transfection studies. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Additional variants have been described, but their
            biological validity has not been determined. [provided by RefSeq,
            Oct 2009].
            
            Transcript Variant: This variant (2) has an alternate 3' CDS and 3'
            UTR, as compared to variant 1. The resulting isoform (2) has a
            shorter and distinct C-terminus that lacks the zinc finger domains,
            as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC006172.1, SRR3476690.919252.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..275
                     /product="zinc finger protein 397 isoform 2"
                     /note="zinc finger protein 47; zinc finger and SCAN
                     domain-containing protein 15"
                     /calculated_mol_wt=30921
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NF99.2)"
     Region          46..152
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     CDS             1..275
                     /gene="ZNF397"
                     /gene_synonym="ZNF47; ZSCAN15"
                     /coded_by="NM_032347.3:157..984"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32814.1"
                     /db_xref="GeneID:84307"
                     /db_xref="HGNC:HGNC:18818"
                     /db_xref="MIM:609601"
ORIGIN      
        1 mavesgvist lipqdppeqe lilvkvednf swdekfkqng stqscqelfr qqfrkfcyqe
       61 tpgprealsr lqelcyqwlm pelhtkeqil ellvleqfls ilpeelqiwv qqhnpesgee
      121 avtlledler efddpgqqvp aspqgpavpw kdltclrasq estdihlqpl ktqlkswkpc
      181 lspksdcens etatkegise eksqglpqep sfrgiklsrp pkassairwe cvspgsfpgd
      241 iiaaeathst iscfaintlp atilpsknvn rkyfs
//
LOCUS       NP_057145                121 aa            linear   PRI 20-NOV-2025
DEFINITION  protein yippee-like 5 [Homo sapiens].
ACCESSION   NP_057145
VERSION     NP_057145.1
DBSOURCE    REFSEQ: accession NM_016061.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Zhou,D., Tang,W., Xu,Y., Xu,Y., Xu,B., Fu,S., Wang,Y., Chen,F.,
            Chen,Y., Han,Y. and Wang,G.
  TITLE     METTL3/YTHDF2 m6A axis accelerates colorectal carcinogenesis
            through epigenetically suppressing YPEL5
  JOURNAL   Mol Oncol 15 (8), 2172-2184 (2021)
   PUBMED   33411363
  REMARK    GeneRIF: METTL3/YTHDF2 m6A axis accelerates colorectal
            carcinogenesis through epigenetically suppressing YPEL5.
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Velusamy,T., Palanisamy,N., Kalyana-Sundaram,S.,
            Sahasrabuddhe,A.A., Maher,C.A., Robinson,D.R., Bahler,D.W.,
            Cornell,T.T., Wilson,T.E., Lim,M.S., Chinnaiyan,A.M. and
            Elenitoba-Johnson,K.S.
  TITLE     Recurrent reciprocal RNA chimera involving YPEL5 and PPP1CB in
            chronic lymphocytic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 110 (8), 3035-3040 (2013)
   PUBMED   23382248
  REMARK    GeneRIF: results indicate that SCN-iPS cells provide a useful
            disease model for SCN, and the activation of the Wnt3a/beta-catenin
            pathway may offer a novel therapy for SCN with ELANE mutation
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Olson,J.E., Wang,X., Pankratz,V.S., Fredericksen,Z.S., Vachon,C.M.,
            Vierkant,R.A., Cerhan,J.R. and Couch,F.J.
  TITLE     Centrosome-related genes, genetic variation, and risk of breast
            cancer
  JOURNAL   Breast Cancer Res Treat 125 (1), 221-228 (2011)
   PUBMED   20508983
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Hosono,K., Noda,S., Shimizu,A., Nakanishi,N., Ohtsubo,M.,
            Shimizu,N. and Minoshima,S.
  TITLE     YPEL5 protein of the YPEL gene family is involved in the cell cycle
            progression by interacting with two distinct proteins RanBPM and
            RanBP10
  JOURNAL   Genomics 96 (2), 102-111 (2010)
   PUBMED   20580816
  REMARK    GeneRIF: YPEL5 protein of the YPEL gene family is involved in the
            cell cycle progression by interacting with two distinct proteins
            RanBPM and RanBP10.
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Hosono,K., Sasaki,T., Minoshima,S. and Shimizu,N.
  TITLE     Identification and characterization of a novel gene family YPEL in
            a wide spectrum of eukaryotic species
  JOURNAL   Gene 340 (1), 31-43 (2004)
   PUBMED   15556292
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Roxstrom-Lindquist,K. and Faye,I.
  TITLE     The Drosophila gene Yippee reveals a novel family of putative zinc
            binding proteins highly conserved among eukaryotes
  JOURNAL   Insect Mol Biol 10 (1), 77-86 (2001)
   PUBMED   11240639
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF172940.1, AC016907.6 and AK025730.1.
            
            Transcript Variant: This variant (4) lacks two alternate exons,
            compared to variant 1. Variants 1, 2, 3, and 4 encode the same
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF151885.1, SRR1660805.257778.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261353.9/ ENSP00000261353.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.1"
     Protein         1..121
                     /product="protein yippee-like 5"
                     /EC_number="1.5.8.4"
                     /calculated_mol_wt=13711
     Region          14..107
                     /region_name="RLR_C_like"
                     /note="C-terminal domain of Retinoic acid-inducible gene
                     (RIG)-I-like Receptors, Cereblon (CRBN), and similar
                     protein domains; cl13152"
                     /db_xref="CDD:472430"
     Site            118
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P62700; propagated from
                     UniProtKB/Swiss-Prot (P62699.1)"
     CDS             1..121
                     /gene="YPEL5"
                     /gene_synonym="CGI-127"
                     /coded_by="NM_016061.3:81..446"
                     /db_xref="CCDS:CCDS1771.1"
                     /db_xref="GeneID:51646"
                     /db_xref="HGNC:HGNC:18329"
                     /db_xref="MIM:609726"
ORIGIN      
        1 mgrifldhig gtrlfscanc dtiltnrsel istrftgatg raflfnkvvn lqysevqdrv
       61 mltgrhmvrd vsckncnskl gwiyefated sqrykegrvi leralvrese gfeehvpsdn
      121 s
//
LOCUS       NP_001304915             354 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase Era, mitochondrial isoform 3 [Homo sapiens].
ACCESSION   NP_001304915
VERSION     NP_001304915.1
DBSOURCE    REFSEQ: accession NM_001317986.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Harper,N.J., Burnside,C. and Klinge,S.
  TITLE     Principles of mitoribosomal small subunit assembly in eukaryotes
  JOURNAL   Nature 614 (7946), 175-181 (2023)
   PUBMED   36482135
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 354)
  AUTHORS   Li,S., Kuang,M., Chen,L., Li,Y., Liu,S., Du,H., Cao,L. and You,F.
  TITLE     The mitochondrial protein ERAL1 suppresses RNA virus infection by
            facilitating RIG-I-like receptor signaling
  JOURNAL   Cell Rep 34 (3), 108631 (2021)
   PUBMED   33472079
  REMARK    GeneRIF: The mitochondrial protein ERAL1 suppresses RNA virus
            infection by facilitating RIG-I-like receptor signaling.
REFERENCE   4  (residues 1 to 354)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 354)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 354)
  AUTHORS   Dennerlein,S., Rozanska,A., Wydro,M., Chrzanowska-Lightowlers,Z.M.
            and Lightowlers,R.N.
  TITLE     Human ERAL1 is a mitochondrial RNA chaperone involved in the
            assembly of the 28S small mitochondrial ribosomal subunit
  JOURNAL   Biochem J 430 (3), 551-558 (2010)
   PUBMED   20604745
  REMARK    GeneRIF: Data show that loss of ERAL1 leads to rapid decay of
            nascent 12S mt-rRNA, consistent with a role as a mitochondrial RNA
            chaperone.
REFERENCE   7  (residues 1 to 354)
  AUTHORS   Uchiumi,T., Ohgaki,K., Yagi,M., Aoki,Y., Sakai,A., Matsumoto,S. and
            Kang,D.
  TITLE     ERAL1 is associated with mitochondrial ribosome and elimination of
            ERAL1 leads to mitochondrial dysfunction and growth retardation
  JOURNAL   Nucleic Acids Res 38 (16), 5554-5568 (2010)
   PUBMED   20430825
REFERENCE   8  (residues 1 to 354)
  AUTHORS   Akiyama,T., Gohda,J., Shibata,S., Nomura,Y., Azuma,S., Ohmori,Y.,
            Sugano,S., Arai,H., Yamamoto,T. and Inoue,J.
  TITLE     Mammalian homologue of E. coli Ras-like GTPase (ERA) is a possible
            apoptosis regulator with RNA binding activity
  JOURNAL   Genes Cells 6 (11), 987-1001 (2001)
   PUBMED   11733036
REFERENCE   9  (residues 1 to 354)
  AUTHORS   Britton,R.A., Chen,S.M., Wallis,D., Koeuth,T., Powell,B.S.,
            Shaffer,L.G., Largaespada,D., Jenkins,N.A., Copeland,N.G.,
            Court,D.L. and Lupski,J.R.
  TITLE     Isolation and preliminary characterization of the human and mouse
            homologues of the bacterial cell cycle gene era
  JOURNAL   Genomics 67 (1), 78-82 (2000)
   PUBMED   10945472
REFERENCE   10 (residues 1 to 354)
  AUTHORS   Li,T., Faridi,R., Newman,W.G. and Friedman,T.B.
  TITLE     Perrault Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25254289
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA559976.1, AK023342.1,
            BI758329.1, AC024267.18, BC019094.2 and BM683046.1.
            
            Summary: The protein encoded by this gene is a GTPase that
            localizes to the mitochondrion. The encoded protein binds to the 3'
            terminal stem loop of 12S mitochondrial rRNA and is required for
            proper assembly of the 28S small mitochondrial ribosomal subunit.
            Deletion of this gene has been shown to cause mitochondrial
            dysfunction, growth retardation, and apoptosis. Several transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2015].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.228972.1,
                                           SRR1163657.71425.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..354
                     /product="GTPase Era, mitochondrial isoform 3"
                     /note="GTPase, human homolog of E. coli essential cell
                     cycle protein Era; era (E. coli G-protein homolog)-like 1;
                     GTP-binding protein era homolog; GTPase Era,
                     mitochondrial; conserved ERA-like GTPase; ERA-like protein
                     1; Era G-protein-like 1"
                     /calculated_mol_wt=39073
     Region          116..351
                     /region_name="era"
                     /note="GTPase Era; Reviewed; PRK00089"
                     /db_xref="CDD:234624"
     CDS             1..354
                     /gene="ERAL1"
                     /gene_synonym="CEGA; ERA; ERA-W; ERAL1A; ERAL1B; H-ERA;
                     HERA-A; HERA-B; PRLTS6"
                     /coded_by="NM_001317986.2:20..1084"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:26284"
                     /db_xref="HGNC:HGNC:3424"
                     /db_xref="MIM:607435"
ORIGIN      
        1 maapswrgar lvqsvlrvwq vgphvarerv ipfssllgfq rrcvscvags afsgprlasa
       61 srsngqgsal dhflgfsqpd ssvtpcvpav smnrdeqdvl lvhhpdmpen srvlrvvllg
      121 apnagkstls nqllgrkvfp vsrkvhttrc qalgviteke tqvilldtpg iispgkqkrh
      181 hlelslledp wksmesadlv vvlvdvsdkw trnqlspqll rcltkysqip svlvmnkqyl
      241 ltqaqpgpwe yhsavltsqt peeicaniir ekllehlpqe vpynvqqkta vweegpggel
      301 viqqkllvpk esyvklligp kghvisqiaq eaghdlmdif lcdvdirlsv kllk
//
LOCUS       NP_001243347             177 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP synthase mitochondrial F1 complex assembly factor 1 isoform 4
            [Homo sapiens].
ACCESSION   NP_001243347
VERSION     NP_001243347.1
DBSOURCE    REFSEQ: accession NM_001256418.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Schauberger,E.M., Ewart,S.L., Arshad,S.H., Huebner,M., Karmaus,W.,
            Holloway,J.W., Friderici,K.H., Ziegler,J.T., Zhang,H.,
            Rose-Zerilli,M.J., Barton,S.J., Holgate,S.T., Kilpatrick,J.R.,
            Harley,J.B., Lajoie-Kadoch,S., Harley,I.T., Hamid,Q.,
            Kurukulaaratchy,R.J., Seibold,M.A., Avila,P.C.,
            Rodriguez-Cintron,W., Rodriguez-Santana,J.R., Hu,D., Gignoux,C.,
            Romieu,I., London,S.J., Burchard,E.G., Langefeld,C.D. and
            Wills-Karp,M.
  TITLE     Identification of ATPAF1 as a novel candidate gene for asthma in
            children
  JOURNAL   J Allergy Clin Immunol 128 (4), 753-760 (2011)
   PUBMED   21696813
  REMARK    GeneRIF: Asthma was found to be associated with a cluster of SNPs
            and SNP haplotypes containing the ATPAF1 gene
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Saito,K., Adachi,N., Koyama,H. and Matsushita,M.
  TITLE     OGFOD1, a member of the 2-oxoglutarate and iron dependent
            dioxygenase family, functions in ischemic signaling
  JOURNAL   FEBS Lett 584 (15), 3340-3347 (2010)
   PUBMED   20579638
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Pickova,A., Potocky,M. and Houstek,J.
  TITLE     Assembly factors of F1FO-ATP synthase across genomes
  JOURNAL   Proteins 59 (3), 393-402 (2005)
   PUBMED   15789402
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Pickova,A., Paul,J., Petruzzella,V. and Houstek,J.
  TITLE     Differential expression of ATPAF1 and ATPAF2 genes encoding
            F(1)-ATPase assembly proteins in mouse tissues
  JOURNAL   FEBS Lett 551 (1-3), 42-46 (2003)
   PUBMED   12965202
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Ackerman,S.H.
  TITLE     Atp11p and Atp12p are chaperones for F(1)-ATPase biogenesis in
            mitochondria
  JOURNAL   Biochim Biophys Acta 1555 (1-3), 101-105 (2002)
   PUBMED   12206899
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Wang,Z.G., White,P.S. and Ackerman,S.H.
  TITLE     Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human
            mitochondria
  JOURNAL   J Biol Chem 276 (33), 30773-30778 (2001)
   PUBMED   11410595
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB448244.1, AK301874.1,
            AI188403.1 and BC071731.1.
            
            Summary: This gene encodes an assembly factor for the F(1)
            component of the mitochondrial ATP synthase. This protein binds
            specifically to the F1 beta subunit and is thought to prevent this
            subunit from forming nonproductive homooligomers during enzyme
            assembly. Alternatively spliced transcript variants have been
            identified. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and uses a downstream in-frame
            start codon, compared to variant 1. The encoded isoform (4) is
            shorter at the N-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301874.1, AK310338.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p33"
     Protein         1..177
                     /product="ATP synthase mitochondrial F1 complex assembly
                     factor 1 isoform 4"
                     /note="homolog of yeast ATP11"
                     /calculated_mol_wt=20150
     Region          <2..156
                     /region_name="ATP11"
                     /note="ATP11 protein; pfam06644"
                     /db_xref="CDD:461972"
     CDS             1..177
                     /gene="ATPAF1"
                     /gene_synonym="ATP11; ATP11p"
                     /coded_by="NM_001256418.1:511..1044"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:64756"
                     /db_xref="HGNC:HGNC:18803"
                     /db_xref="MIM:608917"
ORIGIN      
        1 mvkektaeei kqiwqqyfaa kdtvyavipa ekfdliwnra qscptflcal prregyeffv
       61 gqwtgtelhf taliniqtrg eaaasqlily hypelkeekg ivlmtaemds tflnvaeaqc
      121 ianqvqlfya tdrketyglv etfnlrpnef kymsviaele qsglgaelkc aqnqnkt
//
LOCUS       NP_002099                657 aa            linear   PRI 20-NOV-2025
DEFINITION  histidine ammonia-lyase isoform 1 [Homo sapiens].
ACCESSION   NP_002099 XP_005268877
VERSION     NP_002099.1
DBSOURCE    REFSEQ: accession NM_002108.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 657)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 657)
  AUTHORS   Rivera-Paredez,B., Hidalgo-Bravo,A., Leon-Reyes,G.,
            Barajas-Olmos,F., Martinez-Hernandez,A., Orozco,L.,
            Denova-Gutierrez,E., Salmeron,J. and Velazquez-Cruz,R.
  TITLE     The role of single nucleotide variant rs3819817 of the Histidine
            Ammonia-Lyase gene and 25-Hydroxyvitamin D on bone mineral density,
            adiposity markers, and skin pigmentation, in Mexican population
  JOURNAL   J Endocrinol Invest 46 (9), 1911-1921 (2023)
   PUBMED   36862244
  REMARK    GeneRIF: The role of single nucleotide variant rs3819817 of the
            Histidine Ammonia-Lyase gene and 25-Hydroxyvitamin D on bone
            mineral density, adiposity markers, and skin pigmentation, in
            Mexican population.
REFERENCE   3  (residues 1 to 657)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 657)
  AUTHORS   Chen,K., Liu,H., Liu,Z., Bloomer,W., Amos,C.I., Lee,J.E., Li,X.,
            Nan,H. and Wei,Q.
  TITLE     Genetic variants in glutamine metabolic pathway genes predict
            cutaneous melanoma-specific survival
  JOURNAL   Mol Carcinog 58 (11), 2091-2103 (2019)
   PUBMED   31435991
  REMARK    GeneRIF: In the analysis of the genotype tissue expression (GTEx)
            project datasets, HAL rs17676826 C and NOXRED1 rs8012548 G alleles
            were significantly associated with their mRNA expression levels in
            sun-exposed skin of the lower leg (P = 6.62 x 10(-6) and 1.37 x
            10(-7) , respectively) and in sun-not-exposed suprapubic skin (P <
            .001 and 1.43 x 10(-8) , respectively).
REFERENCE   5  (residues 1 to 657)
  AUTHORS   Yu,B., Li,A.H., Muzny,D., Veeraraghavan,N., de Vries,P.S.,
            Bis,J.C., Musani,S.K., Alexander,D., Morrison,A.C., Franco,O.H.,
            Uitterlinden,A., Hofman,A., Dehghan,A., Wilson,J.G., Psaty,B.M.,
            Gibbs,R., Wei,P. and Boerwinkle,E.
  TITLE     Association of Rare Loss-Of-Function Alleles in HAL, Serum
            Histidine: Levels and Incident Coronary Heart Disease
  JOURNAL   Circ Cardiovasc Genet 8 (2), 351-355 (2015)
   PUBMED   25575548
  REMARK    GeneRIF: Three LoF mutations in HAL were associated with increased
            histidine levels, which in turn were shown to be inversely related
            to the risk of CHD among both African Americans and European
            Americans.
REFERENCE   6  (residues 1 to 657)
  AUTHORS   Aleman,G., Ortiz,V., Langley,E., Tovar,A.R. and Torres,N.
  TITLE     Regulation by glucagon of the rat histidase gene promoter in
            cultured rat hepatocytes and human hepatoblastoma cells
  JOURNAL   Am J Physiol Endocrinol Metab 289 (1), E172-E179 (2005)
   PUBMED   15741241
  REMARK    GeneRIF: This evidence supports that the Hal gene is turned on by
            glucocorticoids and by glucagon either via PKC or PKA, but prefers
            the PKA pathway.
REFERENCE   7  (residues 1 to 657)
  AUTHORS   Kawai,Y., Moriyama,A., Asai,K., Coleman-Campbell,C.M., Sumi,S.,
            Morishita,H. and Suchi,M.
  TITLE     Molecular characterization of histidinemia: identification of four
            missense mutations in the histidase gene
  JOURNAL   Hum Genet 116 (5), 340-346 (2005)
   PUBMED   15806399
  REMARK    GeneRIF: This report describes the first mutations occurring in the
            coding region of the histidase structural gene in patients with
            histidinemia.
            Erratum:[Hum Genet. 2005 Dec;118(3-4):531-2]
REFERENCE   8  (residues 1 to 657)
  AUTHORS   Suchi,M., Sano,H., Mizuno,H. and Wada,Y.
  TITLE     Molecular cloning and structural characterization of the human
            histidase gene (HAL)
  JOURNAL   Genomics 29 (1), 98-104 (1995)
   PUBMED   8530107
REFERENCE   9  (residues 1 to 657)
  AUTHORS   Suchi,M., Harada,N., Wada,Y. and Takagi,Y.
  TITLE     Molecular cloning of a cDNA encoding human histidase
  JOURNAL   Biochim Biophys Acta 1216 (2), 293-295 (1993)
   PUBMED   7916645
REFERENCE   10 (residues 1 to 657)
  AUTHORS   Taylor,R.G., Garcia-Heras,J., Sadler,S.J., Lafreniere,R.G.,
            Willard,H.F., Ledbetter,D.H. and McInnes,R.R.
  TITLE     Localization of histidase to human chromosome region 12q22----q24.1
            and mouse chromosome region 10C2----D1
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 178-181 (1991)
   PUBMED   2055114
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596896.1, D16626.1,
            AC126174.9 and AI248003.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 31, 2013 this sequence version replaced XP_005268877.1.
            
            Summary: Histidine ammonia-lyase is a cytosolic enzyme catalyzing
            the first reaction in histidine catabolism, the nonoxidative
            deamination of L-histidine to trans-urocanic acid. Histidine
            ammonia-lyase defects cause histidinemia which is characterized by
            increased histidine and histamine and decreased urocanic acid in
            body fluids. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Apr
            2012].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.162396.1, D16626.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261208.8/ ENSP00000261208.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..657
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..657
                     /product="histidine ammonia-lyase isoform 1"
                     /EC_number="4.3.1.3"
                     /note="histidase"
                     /calculated_mol_wt=72567
     Region          15..87
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          114..625
                     /region_name="hutH"
                     /note="histidine ammonia-lyase; TIGR01225"
                     /db_xref="CDD:200086"
     Site            order(164..166,168,170,187,190,299..303,307,395,398,428,
                     440)
                     /site_type="active"
                     /note="active sites [active]"
                     /db_xref="CDD:176460"
     Site            order(169..170,189,192..199,220,248..249,262,265,351..352,
                     355..356,358,361,392,394..396,398..399,402..403,409..410,
                     413,416..417,420..421,424..425,430..432,437,439..445,
                     447..448,451,455,462,465,469,473,476,479,491..492,
                     494..495,497..500,502,504..509,511..514,525..531,534,
                     540..541,544,547..548)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:176460"
     Site            396
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35492; propagated from
                     UniProtKB/Swiss-Prot (P42357.1)"
     Site            635
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P21213; propagated from
                     UniProtKB/Swiss-Prot (P42357.1)"
     Site            637
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P35492; propagated from
                     UniProtKB/Swiss-Prot (P42357.1)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P35492; propagated from
                     UniProtKB/Swiss-Prot (P42357.1)"
     CDS             1..657
                     /gene="HAL"
                     /gene_synonym="HIS; HSTD"
                     /coded_by="NM_002108.4:349..2322"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9058.1"
                     /db_xref="GeneID:3034"
                     /db_xref="HGNC:HGNC:4806"
                     /db_xref="MIM:609457"
ORIGIN      
        1 mprytvhvrg ewlavpcqda qltvgwlgre avrryiknkp dnggftsvdd ahflvrrckg
       61 lglldnedrl evalennefv evviegdams pdfipsqpeg vylyskyrep ekyieldgdr
      121 lttedlvnlg kgrykikltp taekrvqksr evidsiikek tvvygittgf gkfartvipi
      181 nklqelqvnl vrshssgvgk plspercrml lalrinvlak gysgisletl kqviemfnas
      241 clpyvpekgt vgasgdlapl shlalglvge gkmwspksgw adakyvleah glkpvilkpk
      301 eglalingtq mitslgceav erasaiarqa divaaltlev lkgttkafdt dihalrphrg
      361 qievafrfrs lldsdhhpse iaeshrfcdr vqdaytlrcc pqvhgvvndt iafvkniitt
      421 elnsatdnpm vfanrgetvs ggnfhgeypa kaldylaigi helaaiserr ierlcnpsls
      481 elpaflvaeg glnsgfmiah ctaaalvsen kalchpssvd slstsaated hvsmggwaar
      541 kalrviehve qvlaiellaa cqgieflrpl ktttplekvy dlvrsvvrpw ikdrfmapdi
      601 eaahrllleq kvwevaapyi ekyrmehipe srplsptafs lqflhkkstk ipesedl
//
LOCUS       NP_001336902             447 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 2
            isoform C [Homo sapiens].
ACCESSION   NP_001336902 XP_016884055
VERSION     NP_001336902.1
DBSOURCE    REFSEQ: accession NM_001349973.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wint,H., Li,J., Abe,T., Yamada,H., Higaki,T., Nasu,Y., Watanabe,M.,
            Takei,K. and Takeda,T.
  TITLE     Pacsin 2-dependent N-cadherin internalization regulates the
            migration behaviour of malignant cancer cells
  JOURNAL   J Cell Sci 136 (10) (2023)
   PUBMED   37132654
  REMARK    GeneRIF: Pacsin 2-dependent N-cadherin internalization regulates
            the migration behaviour of malignant cancer cells.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Zudeh,G., Franca,R., Lucafo,M., Bonten,E.J., Bramuzzo,M.,
            Sgarra,R., Lagatolla,C., Franzin,M., Evans,W.E., Decorti,G. and
            Stocco,G.
  TITLE     PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells
  JOURNAL   Life Sci Alliance 6 (3), e202201610 (2023)
   PUBMED   36596605
  REMARK    GeneRIF: PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Park,K., Yoo,H.S., Oh,C.K., Lee,J.R., Chung,H.J., Kim,H.N.,
            Kim,S.H., Kee,K.M., Kim,T.Y., Kim,M., Kim,B.G., Ra,J.S., Myung,K.,
            Kim,H., Han,S.H., Seo,M.D., Lee,Y. and Kim,D.W.
  TITLE     Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate
            drug resistance in chronic myeloid leukemia
  JOURNAL   Cancer Med 11 (21), 4005-4020 (2022)
   PUBMED   35352878
  REMARK    GeneRIF: Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1
            regulate drug resistance in chronic myeloid leukemia.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Ghadimi,M.P., Sanzenbacher,R., Thiede,B., Wenzel,J., Jing,Q.,
            Plomann,M., Borkhardt,A., Kabelitz,D. and Janssen,O.
  TITLE     Identification of interaction partners of the cytosolic polyproline
            region of CD95 ligand (CD178)
  JOURNAL   FEBS Lett 519 (1-3), 50-58 (2002)
   PUBMED   12023017
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Ritter,B., Modregger,J., Paulsson,M. and Plomann,M.
  TITLE     PACSIN 2, a novel member of the PACSIN family of cytoplasmic
            adapter proteins
  JOURNAL   FEBS Lett 454 (3), 356-362 (1999)
   PUBMED   10431838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG683098.1, BC008037.2,
            HY342978.1, AF128536.1 and BI964045.1.
            
            On Mar 31, 2017 this sequence version replaced XP_016884055.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation by
            regulating tubulin polymerization. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (9) differs in the 5' UTR,
            contains an alternate in-frame exon and  lacks an alternate
            in-frame exon in the 3' coding region, compared to variant 1. The
            resulting protein (isoform C) has the same N- and C-termini, but is
            shorter than isoform A. Variants 4, 7, 8 and 9 encode the same
            protein (isoform C).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..447
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 2 isoform C"
                     /note="syndapin2; syndapin-II; syndapin-2; cytoplasmic
                     phosphoprotein PACSIN2"
                     /calculated_mol_wt=51466
     Region          18..275
                     /region_name="F-BAR_PACSIN2"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein
                     kinase Substrate in Neurons 2 (PACSIN2); cd07679"
                     /db_xref="CDD:153363"
     Site            order(18..20,26..27,30,33,36..37,40..41,43..44,47..48,
                     51..52,54..55,58..59,62,65..66,74..75,79,83,86..87,89,97,
                     145,149,212,227,230,234,237..238,240..242,245,248..249,
                     251..252,255..258,263..264,267,270..271,274..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153363"
     Site            order(25,29,36,46,50,53,65,101,113,132,139..140,147..148,
                     150,203,207,210)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153363"
     Region          390..445
                     /region_name="SH3_PACSIN1-2"
                     /note="Src homology 3 domain of Protein kinase C and
                     Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN
                     2; cd11998"
                     /db_xref="CDD:212931"
     Site            order(396,398,401,405,424..425,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212931"
     CDS             1..447
                     /gene="PACSIN2"
                     /gene_synonym="SDPII"
                     /coded_by="NM_001349973.1:172..1515"
                     /note="isoform C is encoded by transcript variant 9"
                     /db_xref="GeneID:11252"
                     /db_xref="HGNC:HGNC:8571"
                     /db_xref="MIM:604960"
ORIGIN      
        1 msvtyddsvg vevssdsfwe vgnykrtvkr iddghrlcsd lmnclherar iekayaqqlt
       61 ewarrwrqlv ekgpqygtve kawmafmsea ervselhlev kaslmnddfe kiknwqkeaf
      121 hkqmmggfke tkeaedgfrk aqkpwakklk eveaakkahh aackeeklai sreanskadp
      181 slnpeqlkkl qdkiekckqd vlktkekyek slkeldqgtp qymenmeqvf eqcqqfeekr
      241 lrffrevlle vqkhldlsnv agykaiyhdl eqsiraadav edlrwfranh gpgmamnwpq
      301 fedeewsadl nrtlsrrekk katdgvtltg inqtgdqslp skpssvssye ktqsyptdws
      361 ddesnnpfss tdangdsnpf dddatsgtev rvralydyeg qehdelsfka gdeltkmede
      421 deqgwckgrl dngqvglypa nyveaiq
//
LOCUS       NP_001353523             804 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 14 [Homo
            sapiens].
ACCESSION   NP_001353523 XP_016855519
VERSION     NP_001353523.1
DBSOURCE    REFSEQ: accession NM_001366594.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 804)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 804)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 804)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 804)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 804)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 804)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 804)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 804)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 804)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 804)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855519.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.101572.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..804
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..804
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 14"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=90326
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <301..630
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..804
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366594.1:2055..4469"
                     /note="isoform 14 is encoded by transcript variant 38"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels esedkggkma
      361 aadsvqqrrq yrrqnqqsss dsgsssssed erpkrshvkn gevgrrrrhs psrsaspspr
      421 krqketsprm qmgkrwqspv tksgrrrrsp sppptrrrrs pspappprrr rtptppprrr
      481 tpsppprrrs psprrysppi qrryspsppp krrtaspppp pkrraspspp pkrrvshspp
      541 pkqrsspvtk rrspslsskh rkgsspsrst rearspqpnk rhspsprpra pqtssspppv
      601 rrgassspqr rqspspstrp irrvsrtpep kkikkaasps pqsvrrvsss rsvsgspepa
      661 akkppappsp vqsqspstnw spavpvkkak sptpspsppr nsdqegggkk kkkkkdkkhk
      721 kdkkhkkhkk hkkekavaaa aaaavtpaai aaatttlaqe epvaapepkk eteseaednl
      781 ddlekhlrek alrsmrkaqv spqs
//
LOCUS       NP_001032720             174 aa            linear   PRI 20-NOV-2025
DEFINITION  cytotoxic T-lymphocyte protein 4 isoform CTLA-4delTM precursor
            [Homo sapiens].
ACCESSION   NP_001032720
VERSION     NP_001032720.1
DBSOURCE    REFSEQ: accession NM_001037631.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 174)
  AUTHORS   Sun,T., Yang,Y., Qiu,Y., Wang,T., Yang,M., Shen,S. and Wang,W.
  TITLE     High PD-1 and CTLA-4 expression correlates with host immune
            suppression in patients and a mouse model infected with
            Echinococcus multilocularis
  JOURNAL   Parasit Vectors 17 (1), 437 (2024)
   PUBMED   39456030
  REMARK    GeneRIF: High PD-1 and CTLA-4 expression correlates with host
            immune suppression in patients and a mouse model infected with
            Echinococcus multilocularis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 174)
  AUTHORS   Dhaouadi,T., Riahi,A., Ben Abdallah,T., Gorgi,Y. and Sfar,I.
  TITLE     Association of four CTLA-4 gene polymorphisms with pemphigus risk:
            a systematic review, meta-analysis, and meta-regression
  JOURNAL   J Int Med Res 52 (10), 3000605241282116 (2024)
   PUBMED   39397428
  REMARK    GeneRIF: Association of four CTLA-4 gene polymorphisms with
            pemphigus risk: a systematic review, meta-analysis, and
            meta-regression.
REFERENCE   4  (residues 1 to 174)
  AUTHORS   Shamala,V. and Asha Devi,S.
  TITLE     Decoding the genetic influence of CT60 non-coding polymorphism in
            CTLA-4 gene and sCTLA-4 biomarker with rheumatoid arthritis in the
            Indian population
  JOURNAL   Mol Biol Rep 51 (1), 1023 (2024)
   PUBMED   39340674
  REMARK    GeneRIF: Decoding the genetic influence of CT60 non-coding
            polymorphism in CTLA-4 gene and sCTLA-4 biomarker with rheumatoid
            arthritis in the Indian population.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 174)
  AUTHORS   Oaks,M.K., Hallett,K.M., Penwell,R.T., Stauber,E.C., Warren,S.J.
            and Tector,A.J.
  TITLE     A native soluble form of CTLA-4
  JOURNAL   Cell Immunol 201 (2), 144-153 (2000)
   PUBMED   10831323
REFERENCE   6  (residues 1 to 174)
  AUTHORS   Magistrelli,G., Jeannin,P., Herbault,N., Benoit De Coignac,A.,
            Gauchat,J.F., Bonnefoy,J.Y. and Delneste,Y.
  TITLE     A soluble form of CTLA-4 generated by alternative splicing is
            expressed by nonstimulated human T cells
  JOURNAL   Eur J Immunol 29 (11), 3596-3602 (1999)
   PUBMED   10556814
REFERENCE   7  (residues 1 to 174)
  AUTHORS   Chen,C., Gault,A., Shen,L. and Nabavi,N.
  TITLE     Molecular cloning and expression of early T cell costimulatory
            molecule-1 and its characterization as B7-2 molecule
  JOURNAL   J Immunol 152 (10), 4929-4936 (1994)
   PUBMED   7513726
REFERENCE   8  (residues 1 to 174)
  AUTHORS   Linsley,P.S., Brady,W., Urnes,M., Grosmaire,L.S., Damle,N.K. and
            Ledbetter,J.A.
  TITLE     CTLA-4 is a second receptor for the B cell activation antigen B7
  JOURNAL   J Exp Med 174 (3), 561-569 (1991)
   PUBMED   1714933
REFERENCE   9  (residues 1 to 174)
  AUTHORS   Harper,K., Balzano,C., Rouvier,E., Mattei,M.G., Luciani,M.F. and
            Golstein,P.
  TITLE     CTLA-4 and CD28 activated lymphocyte molecules are closely related
            in both mouse and human as to sequence, message expression, gene
            structure, and chromosomal location
  JOURNAL   J Immunol 147 (3), 1037-1044 (1991)
   PUBMED   1713603
REFERENCE   10 (residues 1 to 174)
  AUTHORS   Dariavach,P., Mattei,M.G., Golstein,P. and Lefranc,M.P.
  TITLE     Human Ig superfamily CTLA-4 gene: chromosomal localization and
            identity of protein sequence between murine and human CTLA-4
            cytoplasmic domains
  JOURNAL   Eur J Immunol 18 (12), 1901-1905 (1988)
   PUBMED   3220103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010138.6, AF414120.1 and
            AI733018.1.
            
            Summary: This gene is a member of the immunoglobulin superfamily
            and encodes a protein which transmits an inhibitory signal to T
            cells. The protein contains a V domain, a transmembrane domain, and
            a cytoplasmic tail. Alternate transcriptional splice variants,
            encoding different isoforms, have been characterized. The
            membrane-bound isoform functions as a homodimer interconnected by a
            disulfide bond, while the soluble isoform functions as a monomer.
            Mutations in this gene have been associated with insulin-dependent
            diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac
            disease, systemic lupus erythematosus, thyroid-associated
            orbitopathy, and other autoimmune diseases. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform CTLA-4delTM (also known
            as sCTLA4) is soluble and lacks the transmembrane domain, compared
            to isoform a.  The exon skip represented in this variant is is
            based on human U90273.1, and is consistent with mouse U90270.1 and
            the data published in PMID:10831323 and PMID:10556814.
            
            CCDS Note: This CCDS representation is based on U90273.1 and on
            full-length RT-PCR evidence from PMIDs 10831323 and 10556814. This
            variant also has homology support from cow AF539438.1, mouse
            U90270.1 and rat U90271.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA2142670 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.2"
     Protein         1..174
                     /product="cytotoxic T-lymphocyte protein 4 isoform
                     CTLA-4delTM precursor"
                     /note="celiac disease 3; cytotoxic T-lymphocyte-associated
                     serine esterase-4; ligand and transmembrane spliced
                     cytotoxic T lymphocyte associated antigen 4;
                     insulin-dependent diabetes mellitus 12; cytotoxic T
                     lymphocyte associated antigen 4 short spliced form;
                     gluten-sensitive enteropathy"
                     /calculated_mol_wt=14863
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4300
     Region          39..152
                     /region_name="IgV_CTLA-4"
                     /note="Immunoglobulin Variable (IgV) domain of cytotoxic T
                     lymphocyte-associated antigen 4 (CTLA-4); cd05721"
                     /db_xref="CDD:409386"
     Region          39..60
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409386"
     Region          39..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409386"
     Region          45..48
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409386"
     Site            order(51,53,59,106,117)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409386"
     Region          52..60
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409386"
     Region          61..68
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409386"
     Region          69..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409386"
     Region          69..75
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409386"
     Region          76..97
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409386"
     Region          80..89
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409386"
     Region          94..97
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409386"
     Region          103..132
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409386"
     Region          103..108
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409386"
     Region          111..117
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409386"
     Region          125..132
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409386"
     Region          133..139
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409386"
     Site            order(134..135,138..139)
                     /site_type="other"
                     /note="antigen binding site [polypeptide binding]"
                     /db_xref="CDD:409386"
     Region          140..152
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409386"
     Region          140..152
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409386"
     CDS             1..174
                     /gene="CTLA4"
                     /gene_synonym="ALPS5; CD; CD152; CELIAC3; CTLA-4; GRD4;
                     GSE; IDDM12"
                     /coded_by="NM_001037631.3:173..697"
                     /note="isoform CTLA-4delTM precursor is encoded by
                     transcript variant 2"
                     /db_xref="CCDS:CCDS42803.1"
                     /db_xref="GeneID:1493"
                     /db_xref="HGNC:HGNC:2505"
                     /db_xref="MIM:123890"
ORIGIN      
        1 maclgfqrhk aqlnlatrtw pctllffllf ipvfckamhv aqpavvlass rgiasfvcey
       61 aspgkatevr vtvlrqadsq vtevcaatym mgneltfldd sictgtssgn qvnltiqglr
      121 amdtglyick velmypppyy lgigngtqiy viakekkpsy nrglcenapn rarm
//
LOCUS       NP_689414                852 aa            linear   PRI 20-NOV-2025
DEFINITION  taste receptor type 1 member 3 precursor [Homo sapiens].
ACCESSION   NP_689414 XP_371210
VERSION     NP_689414.2
DBSOURCE    REFSEQ: accession NM_152228.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Shi,Z., Xu,W., Wu,L., Yue,X., Liu,S., Ding,W., Zhang,J., Meng,B.,
            Zhao,L., Liu,X., Liu,J., Liu,Z.J. and Hua,T.
  TITLE     Structural and functional characterization of human sweet taste
            receptor
  JOURNAL   Nature 645 (8081), 801-808 (2025)
   PUBMED   40555359
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Ball,L., Bauer,J. and Krautwurst,D.
  TITLE     Heterodimerization of Chemoreceptors TAS1R3 and mGlu2 in Human
            Blood Leukocytes
  JOURNAL   Int J Mol Sci 24 (16), 12942 (2023)
   PUBMED   37629122
  REMARK    GeneRIF: Heterodimerization of Chemoreceptors TAS1R3 and mGlu2 in
            Human Blood Leukocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Sanematsu,K., Yamamoto,M., Nagasato,Y., Kawabata,Y., Watanabe,Y.,
            Iwata,S., Takai,S., Toko,K., Matsui,T., Wada,N. and Shigemura,N.
  TITLE     Prediction of dynamic allostery for the transmembrane domain of the
            sweet taste receptor subunit, TAS1R3
  JOURNAL   Commun Biol 6 (1), 340 (2023)
   PUBMED   37012338
  REMARK    GeneRIF: Prediction of dynamic allostery for the transmembrane
            domain of the sweet taste receptor subunit, TAS1R3.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Chandrashekar,J., Hoon,M.A., Ryba,N.J. and Zuker,C.S.
  TITLE     The receptors and cells for mammalian taste
  JOURNAL   Nature 444 (7117), 288-294 (2006)
   PUBMED   17108952
  REMARK    Review article
REFERENCE   5  (residues 1 to 852)
  AUTHORS   Xu,H., Staszewski,L., Tang,H., Adler,E., Zoller,M. and Li,X.
  TITLE     Different functional roles of T1R subunits in the heteromeric taste
            receptors
  JOURNAL   Proc Natl Acad Sci U S A 101 (39), 14258-14263 (2004)
   PUBMED   15353592
  REMARK    GeneRIF: findings demonstrate the different functional roles of
            T1R3 and T1R2 and the presence of multiple ligand binding sites on
            the sweet taste receptor
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Spadaccini,R., Trabucco,F., Saviano,G., Picone,D., Crescenzi,O.,
            Tancredi,T. and Temussi,P.A.
  TITLE     The mechanism of interaction of sweet proteins with the T1R2-T1R3
            receptor: evidence from the solution structure of G16A-MNEI
  JOURNAL   J Mol Biol 328 (3), 683-692 (2003)
   PUBMED   12706725
  REMARK    GeneRIF: The mechanism of interaction of the sweet protein monellin
            with T1R2-T1R3 receptor.
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Li,X., Staszewski,L., Xu,H., Durick,K., Zoller,M. and Adler,E.
  TITLE     Human receptors for sweet and umami taste
  JOURNAL   Proc Natl Acad Sci U S A 99 (7), 4692-4696 (2002)
   PUBMED   11917125
REFERENCE   8  (residues 1 to 852)
  AUTHORS   Nelson,G., Chandrashekar,J., Hoon,M.A., Feng,L., Zhao,G., Ryba,N.J.
            and Zuker,C.S.
  TITLE     An amino-acid taste receptor
  JOURNAL   Nature 416 (6877), 199-202 (2002)
   PUBMED   11894099
  REMARK    GeneRIF: sequence differences in T1R receptors within and between
            species (human and mouse) can significantly influence the
            selectivity and specificity of taste responses
REFERENCE   9  (residues 1 to 852)
  AUTHORS   Max,M., Shanker,Y.G., Huang,L., Rong,M., Liu,Z., Campagne,F.,
            Weinstein,H., Damak,S. and Margolskee,R.F.
  TITLE     Tas1r3, encoding a new candidate taste receptor, is allelic to the
            sweet responsiveness locus Sac
  JOURNAL   Nat Genet 28 (1), 58-63 (2001)
   PUBMED   11326277
REFERENCE   10 (residues 1 to 852)
  AUTHORS   Montmayeur,J.P., Liberles,S.D., Matsunami,H. and Buck,L.B.
  TITLE     A candidate taste receptor gene near a sweet taste locus
  JOURNAL   Nat Neurosci 4 (5), 492-498 (2001)
   PUBMED   11319557
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139287.24.
            
            On Nov 23, 2018 this sequence version replaced NP_689414.1.
            
            Summary: The protein encoded by this gene is a G-protein coupled
            receptor involved in taste responses. The encoded protein can form
            a heterodimeric receptor with TAS1R1 to elicit the umami taste
            response, or it can bind with TAS1R2 to form a receptor for the
            sweet taste response. [provided by RefSeq, Nov 2015].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BK000152.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000339381.6/ ENSP00000344411.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..852
                     /product="taste receptor type 1 member 3 precursor"
                     /note="sweet taste receptor T1R3; taste receptor, type 1,
                     member 3"
                     /calculated_mol_wt=91401
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2003
     Region          29..495
                     /region_name="PBP1_taste_receptor"
                     /note="ligand-binding domain of the T1R taste receptor;
                     cd06363"
                     /db_xref="CDD:380586"
     Site            order(107..108,110..111,114..115,118,129,152,155,159..160,
                     224)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:380586"
     Site            order(145,168..170,218,302)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:380586"
     Region          495..547
                     /region_name="NCD3G"
                     /note="Nine Cysteines Domain of family 3 GPCR; pfam07562"
                     /db_xref="CDD:462210"
     Region          590..819
                     /region_name="7tmC_TAS1R3"
                     /note="type 1 taste receptor subtype 3, member of the
                     class C of seven-transmembrane G protein-coupled
                     receptors; cd15290"
                     /db_xref="CDD:320417"
     Region          604..625
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:320417"
     Site            order(624,636..637,640..641,644,725,730,733..734,737,771,
                     774..775,778,782,790..791,794,797,801)
                     /site_type="other"
                     /note="putative allosteric modulator binding site
                     [chemical binding]"
                     /db_xref="CDD:320417"
     Region          634..658
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:320417"
     Region          681..701
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:320417"
     Region          726..752
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:320417"
     Region          760..783
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:320417"
     Region          788..813
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:320417"
     CDS             1..852
                     /gene="TAS1R3"
                     /gene_synonym="T1R3"
                     /coded_by="NM_152228.3:67..2625"
                     /db_xref="CCDS:CCDS30556.1"
                     /db_xref="GeneID:83756"
                     /db_xref="HGNC:HGNC:15661"
                     /db_xref="MIM:605865"
ORIGIN      
        1 mlgpavlgls lwallhpgtg aplclsqqlr mkgdyvlggl fplgeaeeag lrsrtrpssp
       61 vctrfssngl lwalamkmav eeinnksdll pglrlgydlf dtcsepvvam kpslmflaka
      121 gsrdiaaycn ytqyqprvla vigphssela mvtgkffsff lmpqvsygas mellsaretf
      181 psffrtvpsd rvqltaaael lqefgwnwva algsddeygr qglsifsala aargiciahe
      241 glvplpradd srlgkvqdvl hqvnqssvqv vllfasvhaa halfnysiss rlspkvwvas
      301 eawltsdlvm glpgmaqmgt vlgflqrgaq lhefpqyvkt hlalatdpaf csalgereqg
      361 leedvvgqrc pqcdcitlqn vsaglnhhqt fsvyaavysv aqalhntlqc nasgcpaqdp
      421 vkpwqllenm ynltfhvggl plrfdssgnv dmeydlklwv wqgsvprlhd vgrfngslrt
      481 erlkirwhts dnqkpvsrcs rqcqegqvrr vkgfhsccyd cvdceagsyr qnpddiactf
      541 cgqdewsper strcfrrrsr flawgepavl llllllslal glvlaalglf vhhrdsplvq
      601 asggplacfg lvclglvcls vllfpgqpsp arclaqqpls hlpltgclst lflqaaeifv
      661 eselplswad rlsgclrgpw awlvvllaml vevalctwyl vafppevvtd whmlptealv
      721 hcrtrswvsf glahatnatl aflcflgtfl vrsqpgcynr argltfamla yfitwvsfvp
      781 llanvqvvlr pavqmgalll cvlgilaafh lprcyllmrq pglntpeffl gggpgdaqgq
      841 ndgntgnqgk he
//
LOCUS       NP_004057                172 aa            linear   PRI 20-NOV-2025
DEFINITION  centrin-1 [Homo sapiens].
ACCESSION   NP_004057
VERSION     NP_004057.1
DBSOURCE    REFSEQ: accession NM_004066.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Sudhakar,D.V.S., Phanindranath,R., Jaishankar,S., Ramani,A.,
            Kalamkar,K.P., Kumar,U., Pawar,A.D., Dada,R., Singh,R., Gupta,N.J.,
            Deenadayal,M., Tolani,A.D., Sharma,Y., Anand,A., Gopalakrishnan,J.
            and Thangaraj,K.
  TITLE     Exome sequencing and functional analyses revealed CETN1 variants
            leads to impaired cell division and male fertility
  JOURNAL   Hum Mol Genet 32 (4), 533-542 (2023)
   PUBMED   36048845
  REMARK    GeneRIF: Exome sequencing and functional analyses revealed CETN1
            variants leads to impaired cell division and male fertility.
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Laporte,M.H., Bouhlel,I.B., Bertiaux,E., Morrison,C.G., Giroud,A.,
            Borgers,S., Azimzadeh,J., Bornens,M., Guichard,P., Paoletti,A. and
            Hamel,V.
  TITLE     Human SFI1 and Centrin form a complex critical for centriole
            architecture and ciliogenesis
  JOURNAL   EMBO J 41 (21), e112107 (2022)
   PUBMED   36125182
  REMARK    GeneRIF: Human SFI1 and Centrin form a complex critical for
            centriole architecture and ciliogenesis.
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Phanindranath,R., Sudhakar,D.V.S., Thangaraj,K. and Sharma,Y.
  TITLE     Conformational scanning of individual EF-hand motifs of calcium
            sensor protein centrin-1
  JOURNAL   Biochem Biophys Res Commun 570, 67-73 (2021)
   PUBMED   34273620
  REMARK    GeneRIF: Conformational scanning of individual EF-hand motifs of
            calcium sensor protein centrin-1.
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Tsang,W.Y., Spektor,A., Luciano,D.J., Indjeian,V.B., Chen,Z.,
            Salisbury,J.L., Sanchez,I. and Dynlacht,B.D.
  TITLE     CP110 cooperates with two calcium-binding proteins to regulate
            cytokinesis and genome stability
  JOURNAL   Mol Biol Cell 17 (8), 3423-3434 (2006)
   PUBMED   16760425
  REMARK    GeneRIF: These data demonstrate a functional role for CaM binding
            to CP110 and suggest that CP110 cooperates with CaM and centrin to
            regulate progression through cytokinesis.
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Zhao,Z.S., Lim,J.P., Ng,Y.W., Lim,L. and Manser,E.
  TITLE     The GIT-associated kinase PAK targets to the centrosome and
            regulates Aurora-A
  JOURNAL   Mol Cell 20 (2), 237-249 (2005)
   PUBMED   16246726
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Lutz,W., Lingle,W.L., McCormick,D., Greenwood,T.M. and
            Salisbury,J.L.
  TITLE     Phosphorylation of centrin during the cell cycle and its role in
            centriole separation preceding centrosome duplication
  JOURNAL   J Biol Chem 276 (23), 20774-20780 (2001)
   PUBMED   11279195
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Laoukili,J., Perret,E., Middendorp,S., Houcine,O., Guennou,C.,
            Marano,F., Bornens,M. and Tournier,F.
  TITLE     Differential expression and cellular distribution of centrin
            isoforms during human ciliated cell differentiation in vitro
  JOURNAL   J Cell Sci 113 (Pt 8), 1355-1364 (2000)
   PUBMED   10725219
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Errabolu,R., Sanders,M.A. and Salisbury,J.L.
  TITLE     Cloning of a cDNA encoding human centrin, an EF-hand protein of
            centrosomes and mitotic spindle poles
  JOURNAL   J Cell Sci 107 (Pt 1), 9-16 (1994)
   PUBMED   8175926
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029515.1, AP001178.4 and
            AI198628.1.
            
            Summary: The protein encoded by this gene plays important roles in
            the determination of centrosome position and segregation, and in
            the process of microtubule severing. This protein is localized to
            the centrosome of interphase cells, and redistributes to the region
            of the spindle poles during mitosis, reflecting the dynamic
            behavior of the centrosome during the cell cycle. [provided by
            RefSeq, Jan 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR5189667.349026.1,
                                        SRR5189667.282530.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327228.5/ ENSP00000319052.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.32"
     Protein         1..172
                     /product="centrin-1"
                     /note="EF-hand protein; calcium binding protein;
                     caltractin; centrin, EF-hand protein, 1; testicular tissue
                     protein Li 37"
                     /calculated_mol_wt=19439
     Region          1..31
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12798.1)"
     Region          22..172
                     /region_name="PTZ00183"
                     /note="centrin; Provisional"
                     /db_xref="CDD:185503"
     CDS             1..172
                     /gene="CETN1"
                     /gene_synonym="CEN1; CETN"
                     /coded_by="NM_004066.3:30..548"
                     /db_xref="CCDS:CCDS11820.1"
                     /db_xref="GeneID:1068"
                     /db_xref="HGNC:HGNC:1866"
                     /db_xref="MIM:603187"
ORIGIN      
        1 masgfkkpsa astgqkrkva pkpeltedqk qevreafdlf dvdgsgtida kelkvamral
       61 gfeprkeemk kmisevdreg tgkisfndfl avmtqkmsek dtkeeilkaf rlfdddetgk
      121 isfknlkrva nelgenltde elqemidead rdgdgevnee eflrimkkts ly
//
LOCUS       NP_001274454             108 aa            linear   PRI 20-NOV-2025
DEFINITION  intraflagellar transport protein 22 homolog isoform c [Homo
            sapiens].
ACCESSION   NP_001274454
VERSION     NP_001274454.1
DBSOURCE    REFSEQ: accession NM_001287525.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 108)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 108)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 108)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 108)
  AUTHORS   Katoh,Y., Terada,M., Nishijima,Y., Takei,R., Nozaki,S., Hamada,H.
            and Nakayama,K.
  TITLE     Overall Architecture of the Intraflagellar Transport (IFT)-B
            Complex Containing Cluap1/IFT38 as an Essential Component of the
            IFT-B Peripheral Subcomplex
  JOURNAL   J Biol Chem 291 (21), 10962-10975 (2016)
   PUBMED   26980730
REFERENCE   6  (residues 1 to 108)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 108)
  AUTHORS   Silva,D.A., Huang,X., Behal,R.H., Cole,D.G. and Qin,H.
  TITLE     The RABL5 homolog IFT22 regulates the cellular pool size and the
            amount of IFT particles partitioned to the flagellar compartment in
            Chlamydomonas reinhardtii
  JOURNAL   Cytoskeleton (Hoboken) 69 (1), 33-48 (2012)
   PUBMED   22076686
REFERENCE   8  (residues 1 to 108)
  AUTHORS   Adhiambo,C., Blisnick,T., Toutirais,G., Delannoy,E. and Bastin,P.
  TITLE     A novel function for the atypical small G protein Rab-like 5 in the
            assembly of the trypanosome flagellum
  JOURNAL   J Cell Sci 122 (Pt 6), 834-841 (2009)
   PUBMED   19240117
REFERENCE   9  (residues 1 to 108)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA709553.1, AU133515.1, BC009823.2, AC006329.5 and CA841889.1.
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. Variants 3 through 6
            encode the same isoform (c), which is shorter at the N-terminus,
            compared to isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023287.1, AU133515.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..108
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..108
                     /product="intraflagellar transport protein 22 homolog
                     isoform c"
                     /note="RAB, member of RAS oncogene family-like 5; rab-like
                     protein 5; RAB, member RAS oncogene family-like 5;
                     intraflagellar transport protein 22 homolog;
                     intraflagellar transport 22 homolog"
                     /calculated_mol_wt=12262
     CDS             1..108
                     /gene="IFT22"
                     /gene_synonym="CFAP9; FAP9; RABL5"
                     /coded_by="NM_001287525.2:408..734"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS47671.1"
                     /db_xref="GeneID:64792"
                     /db_xref="HGNC:HGNC:21895"
                     /db_xref="MIM:620505"
ORIGIN      
        1 mkdahgvviv fnadipshrk ememwyscfv qqpslqdtqc mliahhkpgs gddkgslsls
       61 pplnklklvh snleddpeei rmefikylks iinsmsesrd reemsimt
//
LOCUS       NP_001340921             571 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001340921
VERSION     NP_001340921.1
DBSOURCE    REFSEQ: accession NM_001353992.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (6), as well as variants 5 and
            7-10, encodes isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.117359.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..571
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 5"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=65207
     Region          13..112
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          129..455
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     CDS             1..571
                     /gene="MTMR1"
                     /coded_by="NM_001353992.1:320..2035"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 meeaplfpge sikaivkdvm yicpfmgavs gtltvtdfkl yfknverdph fildvplgvi
       61 srvekigaqs hgdnscgiei vckdmrnlrl aykqeeqskl gifenlnkha fplsngqalf
      121 afsykekfpi ngwkvydpvs eykrqglpne swkiskinsn yefcdtypai ivvptsvkdd
      181 dlskvaafra kgrvpvlswi hpesqatitr csqplvgpnd krckedekyl qtimdanaqs
      241 hkliifdarq nsvadtnktk gggyesesay pnaelvflei hnihvmresl rklkeivyps
      301 idearwlsnv dgthwleyir mllagavria dkiesgktsv vvhcsdgwdr taqltslaml
      361 mldsyyrtik gfetlvekew isfghrfalr vghgndnhad adrspiflqf vdcvwqmtrq
      421 fpsafefnel flitildhly sclfgtflcn ceqqrfkedv ytktislwsy insqldefsn
      481 pffvnyenhv lypvaslshl elwvnyyvrw nprmrpqmpi hqnlkellav raelqkrveg
      541 lqrevatrav ssssergssp shsatsvhts v
//
LOCUS       NP_002944                735 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-1 isoform a [Homo sapiens].
ACCESSION   NP_002944
VERSION     NP_002944.2
DBSOURCE    REFSEQ: accession NM_002953.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Zhou,N., Guo,C., Du,J., Xu,Q., Li,J., Huang,D., Zheng,X. and Tu,L.
  TITLE     PPP1R14B-mediated phosphorylation enhances protein stability of
            RPS6KA1 to promote hepatocellular carcinoma tumorigenesis
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119840 (2024)
   PUBMED   39216602
  REMARK    GeneRIF: PPP1R14B-mediated phosphorylation enhances protein
            stability of RPS6KA1 to promote hepatocellular carcinoma
            tumorigenesis.
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Guo,X., Huang,G., Qiu,D., He,H., Niu,X., Guo,Z. and Ye,Y.
  TITLE     RPS6KA1 is a histone acetylation-related oncoprotein in acute
            myeloid leukemia which is targeted by afzelin
  JOURNAL   BMC Cancer 24 (1), 1189 (2024)
   PUBMED   39333927
  REMARK    GeneRIF: RPS6KA1 is a histone acetylation-related oncoprotein in
            acute myeloid leukemia which is targeted by afzelin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Wu,S., Jin,J., Huang,J., Chen,G. and Chen,Y.
  TITLE     Comprehensive analysis of the RSK gene family in acute myeloid
            leukemia determines a prognostic signature for the prediction of
            clinical prognosis and treatment responses
  JOURNAL   Hematology 28 (1), 2235833 (2023)
   PUBMED   37462338
  REMARK    GeneRIF: Comprehensive analysis of the RSK gene family in acute
            myeloid leukemia determines a prognostic signature for the
            prediction of clinical prognosis and treatment responses.
REFERENCE   4  (residues 1 to 735)
  AUTHORS   Weidenauer,K., Schmidt,C., Rohde,C., Pauli,C., Blank,M.F., Heid,D.,
            Waclawiczek,A., Corbacioglu,A., Gollner,S., Lotze,M., Vierbaum,L.,
            Renders,S., Krijgsveld,J., Raffel,S., Sauer,T., Trumpp,A.,
            Pabst,C., Muller-Tidow,C. and Janssen,M.
  TITLE     The ribosomal protein S6 kinase alpha-1 (RPS6KA1) induces
            resistance to venetoclax/azacitidine in acute myeloid leukemia
  JOURNAL   Leukemia 37 (8), 1611-1625 (2023)
   PUBMED   37414921
  REMARK    GeneRIF: The ribosomal protein S6 kinase alpha-1 (RPS6KA1) induces
            resistance to venetoclax/azacitidine in acute myeloid leukemia.
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Moller,D.E., Xia,C.H., Tang,W., Zhu,A.X. and Jakubowski,M.
  TITLE     Human rsk isoforms: cloning and characterization of tissue-specific
            expression
  JOURNAL   Am J Physiol 266 (2 Pt 1), C351-C359 (1994)
   PUBMED   8141249
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Chen,R.H., Abate,C. and Blenis,J.
  TITLE     Phosphorylation of the c-Fos transrepression domain by
            mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 10952-10956 (1993)
   PUBMED   8248197
REFERENCE   8  (residues 1 to 735)
  AUTHORS   Rivera,V.M., Miranti,C.K., Misra,R.P., Ginty,D.D., Chen,R.H.,
            Blenis,J. and Greenberg,M.E.
  TITLE     A growth factor-induced kinase phosphorylates the serum response
            factor at a site that regulates its DNA-binding activity
  JOURNAL   Mol Cell Biol 13 (10), 6260-6273 (1993)
   PUBMED   8413226
REFERENCE   9  (residues 1 to 735)
  AUTHORS   Tratner,I., Ofir,R. and Verma,I.M.
  TITLE     Alteration of a cyclic AMP-dependent protein kinase phosphorylation
            site in the c-Fos protein augments its transforming potential
  JOURNAL   Mol Cell Biol 12 (3), 998-1006 (1992)
   PUBMED   1545828
REFERENCE   10 (residues 1 to 735)
  AUTHORS   Chen,R.H., Sarnecki,C. and Blenis,J.
  TITLE     Nuclear localization and regulation of erk- and rsk-encoded protein
            kinases
  JOURNAL   Mol Cell Biol 12 (3), 915-927 (1992)
   PUBMED   1545823
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627313.16.
            
            On Apr 15, 2002 this sequence version replaced NP_002944.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            nonidentical kinase catalytic domains and phosphorylates various
            substrates, including members of the mitogen-activated kinase
            (MAPK) signalling pathway. The activity of this protein has been
            implicated in controlling cell growth and differentiation.
            Alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014966.1, SRR1803615.117813.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374168.7/ ENSP00000363283.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..735
                     /product="ribosomal protein S6 kinase alpha-1 isoform a"
                     /EC_number="2.7.11.1"
                     /note="p90-RSK 1; ribosomal protein S6 kinase alpha-1;
                     S6K-alpha 1; dJ590P13.1 (ribosomal protein S6 kinase,
                     90kD, polypeptide 1); RSK-1; p90S6K; p90RSK1; MAPKAPK-1a;
                     MAPKAP kinase 1a; ribosomal S6 kinase 1; ribosomal protein
                     S6 kinase, 90kDa, polypeptide 1; MAPK-activated protein
                     kinase 1a; 90 kDa ribosomal protein S6 kinase 1; MAP
                     kinase-activated protein kinase 1a"
                     /calculated_mol_wt=82592
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     Region          66..382
                     /region_name="STKc_RSK_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, 90 kDa ribosomal protein S6 kinase; cd05582"
                     /db_xref="CDD:270734"
     Site            order(68..72,76,92,94,125,141..142,144,148,150,187,189,
                     191..192,194,204..205,208,222..227,254,260,263)
                     /site_type="active"
                     /db_xref="CDD:270734"
     Site            order(68..72,76,92,94,125,142..144,148,187,189,191..192,
                     194,204..205)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270734"
     Site            order(72,148,150,187,189,191,208,222..227,254,260,263)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270734"
     Site            order(204..215,217..227)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270734"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PDPK1.
                     /evidence=ECO:0000305|PubMed:9430688; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:9430688,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9430688,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15418.2)"
     Site            363
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270734"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15418.2)"
     Site            376..381
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270734"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:9430688,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15418.2)"
     Region          416..706
                     /region_name="STKc_RSK1_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Ribosomal S6 kinase 1 (also called Ribosomal
                     protein S6 kinase alpha-1 or 90kDa ribosomal protein S6
                     kinase 1); cd14175"
                     /db_xref="CDD:271077"
     Site            order(424..428,432,445,447,473,489..492,496,498,534..535,
                     537,539..540,542,556..557,560,575..579,581)
                     /site_type="active"
                     /db_xref="CDD:271077"
     Site            order(424..427,432,445,447,473,489..492,496,539..540,542,
                     556..557)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271077"
     Site            order(428,496,498,534..535,537,539,560,575..579,581)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271077"
     Site            556..579
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271077"
     Site            573
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:9430688; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     Site            732
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:9430688; propagated from
                     UniProtKB/Swiss-Prot (Q15418.2)"
     CDS             1..735
                     /gene="RPS6KA1"
                     /gene_synonym="HU-1; MAPKAPK1; MAPKAPK1A; p90Rsk; RSK;
                     RSK1"
                     /coded_by="NM_002953.4:161..2368"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS284.1"
                     /db_xref="GeneID:6195"
                     /db_xref="HGNC:HGNC:10430"
                     /db_xref="MIM:601684"
ORIGIN      
        1 mplaqlkepw plmelvpldp engqtsgeea glqpskdegv lkeisithhv kagsekadps
       61 hfellkvlgq gsfgkvflvr kvtrpdsghl yamkvlkkat lkvrdrvrtk merdiladvn
      121 hpfvvklhya fqtegklyli ldflrggdlf trlskevmft eedvkfylae lalgldhlhs
      181 lgiiyrdlkp enilldeegh ikltdfglsk eaidhekkay sfcgtveyma pevvnrqghs
      241 hsadwwsygv lmfemltgsl pfqgkdrket mtlilkaklg mpqflsteaq sllralfkrn
      301 panrlgsgpd gaeeikrhvf ystidwnkly rreikppfkp avaqpddtfy fdteftsrtp
      361 kdspgippsa gahqlfrgfs fvatglmedd gkprapqapl hsvvqqlhgk nlvfsdgyvv
      421 ketigvgsys eckrcvhkat nmeyavkvid kskrdpseei eillrygqhp niitlkdvyd
      481 dgkhvylvte lmrggelldk ilrqkffser easfvlhtig ktveylhsqg vvhrdlkpsn
      541 ilyvdesgnp eclricdfgf akqlraengl lmtpcytanf vapevlkrqg ydegcdiwsl
      601 gillytmlag ytpfangpsd tpeeiltrig sgkftlsggn wntvsetakd lvskmlhvdp
      661 hqrltakqvl qhpwvtqkdk lpqsqlshqd lqlvkgamaa tysalnsskp tpqlkpiess
      721 ilaqrrvrkl psttl
//
LOCUS       NP_076980                310 aa            linear   PRI 20-NOV-2025
DEFINITION  tRNA-splicing endonuclease subunit Sen34 isoform 1 [Homo sapiens].
ACCESSION   NP_076980
VERSION     NP_076980.2
DBSOURCE    REFSEQ: accession NM_024075.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 310)
  AUTHORS   Sekulovski,S., Devant,P., Panizza,S., Gogakos,T., Pitiriciu,A.,
            Heitmeier,K., Ramsay,E.P., Barth,M., Schmidt,C., Tuschl,T.,
            Baas,F., Weitzer,S., Martinez,J. and Trowitzsch,S.
  TITLE     Assembly defects of human tRNA splicing endonuclease contribute to
            impaired pre-tRNA processing in pontocerebellar hypoplasia
  JOURNAL   Nat Commun 12 (1), 5610 (2021)
   PUBMED   34584079
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 310)
  AUTHORS   Bierhals,T., Korenke,G.C., Uyanik,G. and Kutsche,K.
  TITLE     Pontocerebellar hypoplasia type 2 and TSEN2: review of the
            literature and two novel mutations
  JOURNAL   Eur J Med Genet 56 (6), 325-330 (2013)
   PUBMED   23562994
  REMARK    Review article
REFERENCE   3  (residues 1 to 310)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   4  (residues 1 to 310)
  AUTHORS   Budde,B.S., Namavar,Y., Barth,P.G., Poll-The,B.T., Nurnberg,G.,
            Becker,C., van Ruissen,F., Weterman,M.A., Fluiter,K., te Beek,E.T.,
            Aronica,E., van der Knaap,M.S., Hohne,W., Toliat,M.R., Crow,Y.J.,
            Steinling,M., Voit,T., Roelenso,F., Brussel,W., Brockmann,K.,
            Kyllerman,M., Boltshauser,E., Hammersen,G., Willemsen,M.,
            Basel-Vanagaite,L., Krageloh-Mann,I., de Vries,L.S., Sztriha,L.,
            Muntoni,F., Ferrie,C.D., Battini,R., Hennekam,R.C., Grillo,E.,
            Beemer,F.A., Stoets,L.M., Wollnik,B., Nurnberg,P. and Baas,F.
  TITLE     tRNA splicing endonuclease mutations cause pontocerebellar
            hypoplasia
  JOURNAL   Nat Genet 40 (9), 1113-1118 (2008)
   PUBMED   18711368
REFERENCE   5  (residues 1 to 310)
  AUTHORS   Paushkin,S.V., Patel,M., Furia,B.S., Peltz,S.W. and Trotta,C.R.
  TITLE     Identification of a human endonuclease complex reveals a link
            between tRNA splicing and pre-mRNA 3' end formation
  JOURNAL   Cell 117 (3), 311-321 (2004)
   PUBMED   15109492
REFERENCE   6  (residues 1 to 310)
  AUTHORS   Wende,H., Volz,A. and Ziegler,A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
   PUBMED   10941842
  REMARK    Erratum:[Immunogenetics 2001;52(3-4):308]
REFERENCE   7  (residues 1 to 310)
  AUTHORS   van Dijk,T. and Baas,F.
  TITLE     TSEN54 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301773
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BE779123.1, AK226013.1,
            AK054944.1 and AC245052.3.
            
            On Oct 31, 2006 this sequence version replaced NP_076980.1.
            
            Summary: This gene encodes a catalytic subunit of the tRNA splicing
            endonuclease, which catalyzes the removal of introns from precursor
            tRNAs. The endonuclease complex is also associated with a pre-mRNA
            3-prime end processing factor. A mutation in this gene results in
            the neurological disorder pontocerebellar hypoplasia type 2.
            Multiple alternatively spliced variants, encoding the same protein,
            have been identified.[provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (1) encodes the shorter isoform
            (1). Variants 1, 2, and 3 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK226013.1, AK225385.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..310
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..310
                     /product="tRNA-splicing endonuclease subunit Sen34 isoform
                     1"
                     /EC_number="4.6.1.16"
                     /note="leukocyte receptor cluster (LRC) member 5;
                     tRNA-splicing endonuclease subunit Sen34; CTD-3093M3.1;
                     tRNA-intron endonuclease Sen34; leukocyte receptor cluster
                     member 5; TSEN34 tRNA splicing endonuclease subunit"
                     /calculated_mol_wt=33521
     Region          119..177
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BSV6.1)"
     Region          218..306
                     /region_name="tRNA-intron_lyase_C"
                     /note="catalytic C-terminal domain of the tRNA-intron
                     lyase; cd22363"
                     /db_xref="CDD:411767"
     Site            order(220,226..227,232,236,238,243..244,258,260,263..265,
                     271..272,274..276,278..280,287,292,299..306)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:411767"
     Site            order(232,263..265,271..272,274..275,289,292,300..306)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:411767"
     Site            order(247,255,286)
                     /site_type="active"
                     /db_xref="CDD:411767"
     CDS             1..310
                     /gene="TSEN34"
                     /gene_synonym="LENG5; PCH2C; SEN34; SEN34L"
                     /coded_by="NM_024075.5:112..1044"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42609.1"
                     /db_xref="GeneID:79042"
                     /db_xref="HGNC:HGNC:15506"
                     /db_xref="MIM:608754"
ORIGIN      
        1 mlvvevangr slvwgaeavq alrerlgvgg rtvgalprgp rqnsrlglpl llmpeearll
       61 aeigavtlvs aprpdsrhhs laltsfkrqq eesfqeqsal aaearetrrq ellekitegq
      121 aakkqkleqa sgasssqeag ssqaakedet sdgqasgeqe eagpsssqag psngvaplpr
      181 sallvqlata rprpvkarpl dwrvqskdwp hagrpahelr ysiyrdlwer gfflsaagkf
      241 ggdflvypgd plrfhahyia qcwapedtip lqdlvaagrl gtsvrktlll cspqpdgkvv
      301 ytslqwaslq
//
LOCUS       NP_009215                349 aa            linear   PRI 20-NOV-2025
DEFINITION  twinfilin-2 [Homo sapiens].
ACCESSION   NP_009215
VERSION     NP_009215.1
DBSOURCE    REFSEQ: accession NM_007284.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Walker,C.K., Greathouse,K.M., Tuscher,J.J., Dammer,E.B.,
            Weber,A.J., Liu,E., Curtis,K.A., Boros,B.D., Freeman,C.D.,
            Seo,J.V., Ramdas,R., Hurst,C., Duong,D.M., Gearing,M.,
            Murchison,C.F., Day,J.J., Seyfried,N.T. and Herskowitz,J.H.
  TITLE     Cross-Platform Synaptic Network Analysis of Human Entorhinal Cortex
            Identifies TWF2 as a Modulator of Dendritic Spine Length
  JOURNAL   J Neurosci 43 (20), 3764-3785 (2023)
   PUBMED   37055180
  REMARK    GeneRIF: Cross-Platform Synaptic Network Analysis of Human
            Entorhinal Cortex Identifies TWF2 as a Modulator of Dendritic Spine
            Length.
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Ripke,S., O'Dushlaine,C., Chambert,K., Moran,J.L., Kahler,A.K.,
            Akterin,S., Bergen,S.E., Collins,A.L., Crowley,J.J., Fromer,M.,
            Kim,Y., Lee,S.H., Magnusson,P.K., Sanchez,N., Stahl,E.A.,
            Williams,S., Wray,N.R., Xia,K., Bettella,F., Borglum,A.D.,
            Bulik-Sullivan,B.K., Cormican,P., Craddock,N., de Leeuw,C.,
            Durmishi,N., Gill,M., Golimbet,V., Hamshere,M.L., Holmans,P.,
            Hougaard,D.M., Kendler,K.S., Lin,K., Morris,D.W., Mors,O.,
            Mortensen,P.B., Neale,B.M., O'Neill,F.A., Owen,M.J.,
            Milovancevic,M.P., Posthuma,D., Powell,J., Richards,A.L.,
            Riley,B.P., Ruderfer,D., Rujescu,D., Sigurdsson,E., Silagadze,T.,
            Smit,A.B., Stefansson,H., Steinberg,S., Suvisaari,J., Tosato,S.,
            Verhage,M., Walters,J.T., Levinson,D.F., Gejman,P.V., Kendler,K.S.,
            Laurent,C., Mowry,B.J., O'Donovan,M.C., Owen,M.J., Pulver,A.E.,
            Riley,B.P., Schwab,S.G., Wildenauer,D.B., Dudbridge,F., Holmans,P.,
            Shi,J., Albus,M., Alexander,M., Campion,D., Cohen,D., Dikeos,D.,
            Duan,J., Eichhammer,P., Godard,S., Hansen,M., Lerer,F.B.,
            Liang,K.Y., Maier,W., Mallet,J., Nertney,D.A., Nestadt,G.,
            Norton,N., O'Neill,F.A., Papadimitriou,G.N., Ribble,R.,
            Sanders,A.R., Silverman,J.M., Walsh,D., Williams,N.M., Wormley,B.,
            Arranz,M.J., Bakker,S., Bender,S., Bramon,E., Collier,D.,
            Crespo-Facorro,B., Hall,J., Iyegbe,C., Jablensky,A., Kahn,R.S.,
            Kalaydjieva,L., Lawrie,S., Lewis,C.M., Lin,K., Linszen,D.H.,
            Mata,I., McIntosh,A., Murray,R.M., Ophoff,R.A., Powell,J.,
            Rujescu,D., Van Os,J., Walshe,M., Weisbrod,M., Wiersma,D.,
            Donnelly,P., Barroso,I., Blackwell,J.M., Bramon,E., Brown,M.A.,
            Casas,J.P., Corvin,A.P., Deloukas,P., Duncanson,A., Jankowski,J.,
            Markus,H.S., Mathew,C.G., Palmer,C.N., Plomin,R., Rautanen,A.,
            Sawcer,S.J., Trembath,R.C., Viswanathan,A.C., Wood,N.W.,
            Spencer,C.C., Band,G., Bellenguez,C., Freeman,C., Hellenthal,G.,
            Giannoulatou,E., Pirinen,M., Pearson,R.D., Strange,A., Su,Z.,
            Vukcevic,D., Donnelly,P., Langford,C., Hunt,S.E., Edkins,S.,
            Gwilliam,R., Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M.,
            Gray,E., Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M.,
            Tashakkori-Ghanbaria,A., Waller,M.J., Weston,P., Widaa,S.,
            Whittaker,P., Barroso,I., Deloukas,P., Mathew,C.G., Blackwell,J.M.,
            Brown,M.A., Corvin,A.P., McCarthy,M.I., Spencer,C.C., Bramon,E.,
            Corvin,A.P., O'Donovan,M.C., Stefansson,K., Scolnick,E.,
            Purcell,S., McCarroll,S.A., Sklar,P., Hultman,C.M. and
            Sullivan,P.F.
  CONSRTM   Multicenter Genetic Studies of Schizophrenia Consortium; Psychosis
            Endophenotypes International Consortium; Wellcome Trust Case
            Control Consortium 2
  TITLE     Genome-wide association analysis identifies 13 new risk loci for
            schizophrenia
  JOURNAL   Nat Genet 45 (10), 1150-1159 (2013)
   PUBMED   23974872
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Nevalainen,E.M., Skwarek-Maruszewska,A., Braun,A., Moser,M. and
            Lappalainen,P.
  TITLE     Two biochemically distinct and tissue-specific twinfilin isoforms
            are generated from the mouse Twf2 gene by alternative promoter
            usage
  JOURNAL   Biochem J 417 (2), 593-600 (2009)
   PUBMED   18837697
REFERENCE   7  (residues 1 to 349)
  AUTHORS   Yamada,S., Uchimura,E., Ueda,T., Nomura,T., Fujita,S.,
            Matsumoto,K., Funeriu,D.P., Miyake,M. and Miyake,J.
  TITLE     Identification of twinfilin-2 as a factor involved in neurite
            outgrowth by RNAi-based screen
  JOURNAL   Biochem Biophys Res Commun 363 (4), 926-930 (2007)
   PUBMED   17910947
  REMARK    GeneRIF: twinfilin-2 is a protein that is involved in neurite
            outgrowth
REFERENCE   8  (residues 1 to 349)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
REFERENCE   9  (residues 1 to 349)
  AUTHORS   Vartiainen,M.K., Sarkkinen,E.M., Matilainen,T., Salminen,M. and
            Lappalainen,P.
  TITLE     Mammals have two twinfilin isoforms whose subcellular localizations
            and tissue distributions are differentially regulated
  JOURNAL   J Biol Chem 278 (36), 34347-34355 (2003)
   PUBMED   12807912
REFERENCE   10 (residues 1 to 349)
  AUTHORS   Rohwer,A., Kittstein,W., Marks,F. and Gschwendt,M.
  TITLE     Cloning, expression and characterization of an A6-related protein
  JOURNAL   Eur J Biochem 263 (2), 518-525 (1999)
   PUBMED   10406962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI551353.1, AL136773.1 and
            BC003161.1.
            
            Summary: The protein encoded by this gene was identified by its
            interaction with the catalytic domain of protein kinase C-zeta. The
            encoded protein contains an actin-binding site and an ATP-binding
            site. It is most closely related to twinfilin (PTK9), a conserved
            actin monomer-binding protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.160093.1,
                                           SRR3476690.791267.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305533.10/ ENSP00000303908.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..349
                     /product="twinfilin-2"
                     /note="protein tyrosine kinase 9-like (A6-related
                     protein); PTK9L protein tyrosine kinase 9-like (A6-related
                     protein); twinfilin-1-like protein; twinfilin,
                     actin-binding protein, homolog 2"
                     /calculated_mol_wt=39417
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6IBS0.2)"
     Region          4..142
                     /region_name="ADF_Twf-N_like"
                     /note="N-terminal ADF domain of twinfilin and related
                     proteins; cd11285"
                     /db_xref="CDD:200441"
     Site            5..6
                     /site_type="other"
                     /note="putative G-actin interface [polypeptide binding]"
                     /db_xref="CDD:200441"
     Site            14
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6IBS0.2)"
     Region          176..311
                     /region_name="ADF_Twf-C_like"
                     /note="C-terminal ADF domain of twinfilin and related
                     proteins; cd11284"
                     /db_xref="CDD:200440"
     Site            order(176..180,210,257,259,262,266..267,269..271,273..274,
                     276,294,296,298)
                     /site_type="other"
                     /note="G-actin binding interface [polypeptide binding]"
                     /db_xref="CDD:200440"
     Site            order(267,299,302)
                     /site_type="other"
                     /note="putative F-actin interface [polypeptide binding]"
                     /db_xref="CDD:200440"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6IBS0.2)"
     Region          322..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6IBS0.2)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6IBS0.2)"
     CDS             1..349
                     /gene="TWF2"
                     /gene_synonym="A6r; A6RP; MSTP011; PTK9L"
                     /coded_by="NM_007284.4:143..1192"
                     /db_xref="CCDS:CCDS2849.1"
                     /db_xref="GeneID:11344"
                     /db_xref="HGNC:HGNC:9621"
                     /db_xref="MIM:607433"
ORIGIN      
        1 mahqtgihat eelkeffaka ragsvrlikv viedeqlvlg asqepvgrwd qdydravlpl
       61 ldaqqpcyll yrldsqnaqg fewlflawsp dnspvrlkml yaatratvkk efggghikde
      121 lfgtvkddls fagyqkhlss caapapltsa erelqqirin evkteisves khqtlqglaf
      181 plqpeaqral qqlkqkmvny iqmkldlere tielvhtept dvaqlpsrvp rdaaryhffl
      241 ykhthegdpl esvvfiysmp gykcsikerm lysscksrll dsveqdfhle iakkieigdg
      301 aeltaeflyd evhpkqhafk qafakpkgpg gkrghkrlir gpgengdds
//
LOCUS       NP_001341019             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341019 XP_016879179
VERSION     NP_001341019.1
DBSOURCE    REFSEQ: accession NM_001354090.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Aug 4, 2017 this sequence version replaced XP_016879179.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.448227.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354090.2:655..1419"
                     /note="isoform a is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001308751             539 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform o [Homo sapiens].
ACCESSION   NP_001308751
VERSION     NP_001308751.1
DBSOURCE    REFSEQ: accession NM_001321822.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.222225.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..539
                     /product="E3 ubiquitin-protein ligase CBL-B isoform o"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=58579
     Region          488..528
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(490..491,493..495,497..498,503,507)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..539
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321822.2:1671..3290"
                     /note="isoform o is encoded by transcript variant 21"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mpmldldddd dreeslmmnr lanvrkctdr qnspvtspgs splaqrrkpq pdplqiphls
       61 lppvpprldl iqkgivrspc gsptgspkss pcmvrkqdkp lpapppplrd pppppperpp
      121 pippdnrlsr hihhvesvps rdppmpleaw cprdvfgtnq lvgcrllgeg spkpgitass
      181 nvngrhsrvg sdpvlmrkhr rhdlplegak vfsnghlgse eydvpprlsp pppvttllps
      241 ikctgplans lsektrdpve edddeykips shpvslnsqp shchnvkppv rscdnghcml
      301 ngthgpssek ksnipdlsiy lkgdvfdsas dpvplpparp ptrdnpkhgs slnrtpsdyd
      361 llipplgeda fdalppslpp pppparhsli ehskppgsss rpssgqdlfl lpsdpfvdla
      421 sgqvplppar rlpgenvktn rtsqdydqlp scsdgsqapa rppkprprrt apeihhrkph
      481 gpeaalenvd akiaklmgeg yafeevkral eiaqnnveva rsilrefafp ppvsprlnl
//
LOCUS       NP_001289437             584 aa            linear   PRI 20-NOV-2025
DEFINITION  72 kDa type IV collagenase isoform 3 [Homo sapiens].
ACCESSION   NP_001289437
VERSION     NP_001289437.1
DBSOURCE    REFSEQ: accession NM_001302508.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 584)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 584)
  AUTHORS   Hung,C.C., Tsai,C.L., Chin,Y.T., Wang,Y.C., Liu,C.H., Lin,M.L.,
            Chen,S.S., He,J.L., Tsai,C.W., Su,C.H., Bau,D.T. and Chang,W.S.
  TITLE     Impacts of Matrix Metalloproteinase-2 Promoter Genotypes on Breast
            Cancer Risk
  JOURNAL   Cancer Genomics Proteomics 21 (5), 502-510 (2024)
   PUBMED   39191502
  REMARK    GeneRIF: Impacts of Matrix Metalloproteinase-2 Promoter Genotypes
            on Breast Cancer Risk.
REFERENCE   3  (residues 1 to 584)
  AUTHORS   Liang,S., Li,L., Guo,Z., Sun,H. and Yang,Y.
  TITLE     Co-expression of CD44v6 and MMP2 predicts lung metastasis and
            unfavorable prognosis in osteosarcoma
  JOURNAL   Future Oncol 20 (25), 1799-1806 (2024)
   PUBMED   39011948
  REMARK    GeneRIF: Co-expression of CD44v6 and MMP2 predicts lung metastasis
            and unfavorable prognosis in osteosarcoma.
REFERENCE   4  (residues 1 to 584)
  AUTHORS   DeCoux,A., Lindsey,M.L., Villarreal,F., Garcia,R.A. and Schulz,R.
  TITLE     Myocardial matrix metalloproteinase-2: inside out and upside down
  JOURNAL   J Mol Cell Cardiol 77, 64-72 (2014)
   PUBMED   25261607
  REMARK    GeneRIF: The roles of MMP-2 in cardiac injury and repair. [Review]
            Review article
REFERENCE   5  (residues 1 to 584)
  AUTHORS   Verslegers,M., Lemmens,K., Van Hove,I. and Moons,L.
  TITLE     Matrix metalloproteinase-2 and -9 as promising benefactors in
            development, plasticity and repair of the nervous system
  JOURNAL   Prog Neurobiol 105, 60-78 (2013)
   PUBMED   23567503
  REMARK    Review article
REFERENCE   6  (residues 1 to 584)
  AUTHORS   Nagase,H., Visse,R. and Murphy,G.
  TITLE     Structure and function of matrix metalloproteinases and TIMPs
  JOURNAL   Cardiovasc Res 69 (3), 562-573 (2006)
   PUBMED   16405877
  REMARK    Review article
REFERENCE   7  (residues 1 to 584)
  AUTHORS   Bhavani,G.S., Shah,H., Shukla,A. and Girisha,K.M.
  TITLE     Multicentric Osteolysis Nodulosis and Arthropathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27413800
REFERENCE   8  (residues 1 to 584)
  AUTHORS   Devarajan,P., Johnston,J.J., Ginsberg,S.S., Van Wart,H.E. and
            Berliner,N.
  TITLE     Structure and expression of neutrophil gelatinase cDNA. Identity
            with type IV collagenase from HT1080 cells
  JOURNAL   J Biol Chem 267 (35), 25228-25232 (1992)
   PUBMED   1460022
REFERENCE   9  (residues 1 to 584)
  AUTHORS   Levy,A.T., Cioce,V., Sobel,M.E., Garbisa,S., Grigioni,W.F.,
            Liotta,L.A. and Stetler-Stevenson,W.G.
  TITLE     Increased expression of the Mr 72,000 type IV collagenase in human
            colonic adenocarcinoma
  JOURNAL   Cancer Res 51 (1), 439-444 (1991)
   PUBMED   1846313
REFERENCE   10 (residues 1 to 584)
  AUTHORS   Huhtala,P., Chow,L.T. and Tryggvason,K.
  TITLE     Structure of the human type IV collagenase gene
  JOURNAL   J Biol Chem 265 (19), 11077-11082 (1990)
   PUBMED   2162831
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA579926.1, AC007336.6,
            AK301536.1, BX357054.2 and BQ004983.1.
            
            Summary: This gene is a member of the matrix metalloproteinase
            (MMP) gene family, that are zinc-dependent enzymes capable of
            cleaving components of the extracellular matrix and molecules
            involved in signal transduction. The protein encoded by this gene
            is a gelatinase A, type IV collagenase, that contains three
            fibronectin type II repeats in its catalytic site that allow
            binding of denatured type IV and V collagen and elastin. Unlike
            most MMP family members, activation of this protein can occur on
            the cell membrane. This enzyme can be activated extracellularly by
            proteases, or, intracellulary by its S-glutathiolation with no
            requirement for proteolytical removal of the pro-domain. This
            protein is thought to be involved in multiple pathways including
            roles in the nervous system, endometrial menstrual breakdown,
            regulation of vascularization, and metastasis. Mutations in this
            gene have been associated with Winchester syndrome and
            Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Alternative
            splicing results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon, and initiates translation at a downstream start
            codon, compared to variant 1. The encoded isoform (3) has a shorter
            N-terminus than isoform 1. Variants 3, 4, and 5 all encode the same
            isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803611.103806.1, AL832088.1
                                    [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968540, SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..584
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q12.2"
     Protein         1..584
                     /product="72 kDa type IV collagenase isoform 3"
                     /EC_number="3.4.24.24"
                     /note="neutrophil gelatinase; matrix metalloproteinase-II;
                     collagenase type IV-A; matrix metallopeptidase 2
                     (gelatinase A, 72kDa gelatinase, 72kDa type IV
                     collagenase); matrix metalloproteinase-2"
                     /calculated_mol_wt=65634
     Region          42..370
                     /region_name="Peptidase_M10"
                     /note="Matrixin; pfam00413"
                     /db_xref="CDD:425668"
     Region          150..198
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(161,163,168,182,189,195,197)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          208..256
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(219,221,226,240,247,253,255)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          266..314
                     /region_name="FN2"
                     /note="Fibronectin type 2 domain; smart00059"
                     /db_xref="CDD:128373"
     Site            order(277,279,284,298,305,311,313)
                     /site_type="active"
                     /note="putative gelatin-binding site [active]"
                     /db_xref="CDD:238019"
     Region          390..584
                     /region_name="HX"
                     /note="Hemopexin-like repeats.; Hemopexin is a
                     heme-binding protein that transports heme to the liver.
                     Hemopexin-like repeats occur in vitronectin and some
                     matrix metalloproteinases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of...;
                     cd00094"
                     /db_xref="CDD:238046"
     Site            order(400,402,445,447,493,495,542,544)
                     /site_type="metal-binding"
                     /note="Metal binding sites [ion binding]"
                     /db_xref="CDD:238046"
     CDS             1..584
                     /gene="MMP2"
                     /gene_synonym="CLG4; CLG4A; MMP-2; MMP-II; MONA; TBE-1"
                     /coded_by="NM_001302508.1:212..1966"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS76869.1"
                     /db_xref="GeneID:4313"
                     /db_xref="HGNC:HGNC:7166"
                     /db_xref="MIM:120360"
ORIGIN      
        1 mqkffglpqt gdldqntiet mrkprcgnpd vanynffprk pkwdknqity riigytpdld
       61 petvddafar afqvwsdvtp lrfsrihdge adiminfgrw ehgdgypfdg kdgllahafa
      121 pgtgvggdsh fdddelwtlg egqvvrvkyg nadgeyckfp flfngkeyns ctdtgrsdgf
      181 lwcsttynfe kdgkygfcph ealftmggna egqpckfpfr fqgtsydsct tegrtdgyrw
      241 cgttedydrd kkygfcpeta mstvggnseg apcvfpftfl gnkyesctsa grsdgkmwca
      301 ttanydddrk wgfcpdqgys lflvaahefg hamglehsqd pgalmapiyt ytknfrlsqd
      361 dikgiqelyg aspdidlgtg ptptlgpvtp eickqdivfd giaqirgeif ffkdrfiwrt
      421 vtprdkpmgp llvatfwpel pekidavyea pqeekavffa gneywiysas tlergypkpl
      481 tslglppdvq rvdaafnwsk nkktyifagd kfwrynevkk kmdpgfpkli adawnaipdn
      541 ldavvdlqgg ghsyffkgay ylklenqslk svkfgsiksd wlgc
//
LOCUS       NP_001124197             160 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-5 isoform 2 [Homo sapiens].
ACCESSION   NP_001124197
VERSION     NP_001124197.1
DBSOURCE    REFSEQ: accession NM_001130725.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 160)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 160)
  AUTHORS   Wang,H., Bai,C., Dang,X. and Wang,H.
  TITLE     MiR-383 sensitizes osteosarcoma cells to bortezomib treatment via
            down-regulating PSMB5
  JOURNAL   Mol Biol Rep 51 (1), 170 (2024)
   PUBMED   38252234
  REMARK    GeneRIF: MiR-383 sensitizes osteosarcoma cells to bortezomib
            treatment via down-regulating PSMB5.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 160)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 160)
  AUTHORS   Liu,J., Mi,J., Liu,S., Chen,H. and Jiang,L.
  TITLE     PSMB5 overexpression is correlated with tumor proliferation and
            poor prognosis in hepatocellular carcinoma
  JOURNAL   FEBS Open Bio 12 (11), 2025-2041 (2022)
   PUBMED   36062301
  REMARK    GeneRIF: PSMB5 overexpression is correlated with tumor
            proliferation and poor prognosis in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 160)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   6  (residues 1 to 160)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 207 (3), 1059 (1995)
   PUBMED   7864893
  REMARK    Correction to:[Biochem Biophys Res Commun. 1994 Dec
            30;205(3):1785-9. doi: 10.1006/bbrc.1994.2876. PMID: 7811265]
REFERENCE   7  (residues 1 to 160)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 160)
  AUTHORS   Belich,M.P., Glynne,R.J., Senger,G., Sheer,D. and Trowsdale,J.
  TITLE     Proteasome components with reciprocal expression to that of the
            MHC-encoded LMP proteins
  JOURNAL   Curr Biol 4 (9), 769-776 (1994)
   PUBMED   7820546
REFERENCE   9  (residues 1 to 160)
  AUTHORS   Akiyama,K., Yokota,K., Kagawa,S., Shimbara,N., Tamura,T.,
            Akioka,H., Nothwang,H.G., Noda,C., Tanaka,K. and Ichihara,A.
  TITLE     cDNA cloning and interferon gamma down-regulation of proteasomal
            subunits X and Y
  JOURNAL   Science 265 (5176), 1231-1234 (1994)
   PUBMED   8066462
REFERENCE   10 (residues 1 to 160)
  AUTHORS   Lee,L.W., Moomaw,C.R., Orth,K., McGuire,M.J., DeMartino,G.N. and
            Slaughter,C.A.
  TITLE     Relationships among the subunits of the high molecular weight
            proteinase, macropain (proteasome)
  JOURNAL   Biochim Biophys Acta 1037 (2), 178-185 (1990)
   PUBMED   2306472
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CD048996.1, BU539357.1,
            BC107720.1 and BU632351.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit in the proteasome. This
            catalytic subunit is not present in the immunoproteasome and is
            replaced by catalytic subunit 3i (proteasome beta 8 subunit).
            Multiple transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (2) uses a different segment for
            its 5' UTR and lacks the 5' end of the coding region, compared to
            variant 1. The encoded protein (isoform 2) results from the use of
            a downstream start codon and is shorter when it is compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005466.1, SRR1163657.280211.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..160
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..160
                     /product="proteasome subunit beta type-5 isoform 2"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit MB1; beta-5; PSX large
                     multifunctional protease X; proteasome epsilon chain;
                     macropain epsilon chain; multicatalytic endopeptidase
                     complex epsilon chain; proteasome chain 6; proteasome
                     catalytic subunit 3; proteasome subunit, beta type, 5;
                     proteasome subunit X; proteasome beta 5 subunit;
                     proteasome (prosome, macropain) subunit, beta type, 5;
                     testicular tissue protein Li 153; proteasome subunit beta
                     5"
                     /calculated_mol_wt=17651
     Region          <1..144
                     /region_name="proteasome_beta_type_5"
                     /note="proteasome beta type-5 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03761"
                     /db_xref="CDD:239730"
     CDS             1..160
                     /gene="PSMB5"
                     /gene_synonym="LMPX; MB1"
                     /coded_by="NM_001130725.1:221..703"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45083.1"
                     /db_xref="GeneID:5693"
                     /db_xref="HGNC:HGNC:9542"
                     /db_xref="MIM:600306"
ORIGIN      
        1 maggaadcsf werllarqcr iyelrnkeri svaaasklla nmvyqykgmg lsmgtmicgw
       61 dkrgpglyyv dsegnrisga tfsvgsgsvy aygvmdrgys ydleveqayd larraiyqat
      121 yrdaysggav nlyhvredgw irvssdnvad lhekysgstp
//
LOCUS       NP_001350626             170 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL28 isoform 6 [Homo sapiens].
ACCESSION   NP_001350626 XP_024307404
VERSION     NP_001350626.1
DBSOURCE    REFSEQ: accession NM_001363697.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Frigerio,J.M., Dagorn,J.C. and Iovanna,J.L.
  TITLE     Cloning, sequencing and expression of the L5, L21, L27a, L28, S5,
            S9, S10 and S29 human ribosomal protein mRNAs
  JOURNAL   Biochim Biophys Acta 1262 (1), 64-68 (1995)
   PUBMED   7772601
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Brown,J.R., Daar,I.O., Krug,J.R. and Maquat,L.E.
  TITLE     Characterization of the functional gene and several processed
            pseudogenes in the human triosephosphate isomerase gene family
  JOURNAL   Mol Cell Biol 5 (7), 1694-1706 (1985)
   PUBMED   4022011
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK311760.1, BG716117.1,
            BF686026.1, DB540276.1 and AA579944.1.
            
            On May 25, 2018 this sequence version replaced XP_024307404.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L28E family of ribosomal proteins. It is located in the
            cytoplasm. Variable expression of this gene in colorectal cancers
            compared to adjacent normal tissues has been observed, although no
            correlation between the level of expression and the severity of the
            disease has been found. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms.[provided
            by RefSeq, Oct 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG716117.1, DB471544.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..170
                     /product="large ribosomal subunit protein eL28 isoform 6"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L28; large ribosomal subunit
                     protein eL28"
                     /calculated_mol_wt=18941
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:12962325, ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (P46779.3)"
     Region          5..110
                     /region_name="Ribosomal_L28e"
                     /note="Ribosomal L28e protein family; pfam01778"
                     /db_xref="CDD:460323"
     CDS             1..170
                     /gene="RPL28"
                     /gene_synonym="eL28; L28"
                     /coded_by="NM_001363697.1:43..555"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS86809.1"
                     /db_xref="GeneID:6158"
                     /db_xref="HGNC:HGNC:10330"
                     /db_xref="MIM:603638"
ORIGIN      
        1 msahlqwmvv rncssflikr nkqtystepn nlkarnsfry nglihrktvg vepaadgkgv
       61 vvvikrrsgq rkpatsyvrt tinknaratl ssirhmirkn kyrpdlrmla grvgrqqavs
      121 slehqprpgr lhlsntaars fcvmepsrtl qdlgstlglh pldasgtpel
//
LOCUS       NP_001274110             333 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 33 isoform 3 [Homo sapiens].
ACCESSION   NP_001274110
VERSION     NP_001274110.1
DBSOURCE    REFSEQ: accession NM_001287181.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 333)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 333)
  AUTHORS   Daakour,S., Hajingabo,L.J., Kerselidou,D., Devresse,A.,
            Kettmann,R., Simonis,N., Dequiedt,F. and Twizere,J.C.
  TITLE     Systematic interactome mapping of acute lymphoblastic leukemia
            cancer gene products reveals EXT-1 tumor suppressor as a Notch1 and
            FBWX7 common interactor
  JOURNAL   BMC Cancer 16, 335 (2016)
   PUBMED   27229929
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 333)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 333)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   5  (residues 1 to 333)
  AUTHORS   Kaczmarek,K., Niedzialkowska,E., Studencka,M., Schulz,Y. and
            Grzmil,P.
  TITLE     Ccdc33, a predominantly testis-expressed gene, encodes a putative
            peroxisomal protein
  JOURNAL   Cytogenet Genome Res 126 (3), 243-252 (2009)
   PUBMED   20068295
  REMARK    GeneRIF: Data show that CCDC33-dsRED fusion protein co-localized
            with a known peroxisomal protein, namely PXT1, and showed punctuate
            intracellular distribution.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK026821.1, AK290709.1 and BC025689.1.
            
            Transcript Variant: This variant (3) contains alternate exon
            structure in both its 5' and 3' regions, and it thus differs in
            both UTRs and in the 5' and 3' coding regions, compared to variant
            1. The encoded isoform (3) has distinct N- and C-termini and is
            shorter than isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026821.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144333, SAMEA2158569
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..333
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..333
                     /product="coiled-coil domain-containing protein 33 isoform
                     3"
                     /note="cancer/testis antigen 61; coiled-coil
                     domain-containing protein 33; hypothetical protein
                     HP11097"
                     /calculated_mol_wt=37309
     CDS             1..333
                     /gene="CCDC33"
                     /gene_synonym="CC2D3; CT61; HP11097"
                     /coded_by="NM_001287181.2:32..1033"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73753.1"
                     /db_xref="GeneID:80125"
                     /db_xref="HGNC:HGNC:26552"
                     /db_xref="MIM:618525"
ORIGIN      
        1 mgepgppspp apkaapglid sfsemnnyrr amqkmaedil slrrqasile genrilrsrl
       61 aqqeeeegqg kaseaqntvs mkqklllsel dmkklrdrvq hlqnelirkn drekelllly
      121 qaqqpqaall kqyqgklqkm kaleetvrhq ekviekmerv ledrlqdrsk ppplnrqqgk
      181 pytgfpmlsa sglplgsmge nlpvelysvl laenaklrte ldknrhqqap iilqqqalpd
      241 llsgtsdkfn llaklehaqs rilslesqle dsarrwgrek qdlatrlqeq ekgfrhpsns
      301 iiieqpvsdp pgvaprgsgg gagshrtpkv tgp
//
LOCUS       NP_001336901             447 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 2
            isoform C [Homo sapiens].
ACCESSION   NP_001336901 XP_016884054
VERSION     NP_001336901.1
DBSOURCE    REFSEQ: accession NM_001349972.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 447)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 447)
  AUTHORS   Wint,H., Li,J., Abe,T., Yamada,H., Higaki,T., Nasu,Y., Watanabe,M.,
            Takei,K. and Takeda,T.
  TITLE     Pacsin 2-dependent N-cadherin internalization regulates the
            migration behaviour of malignant cancer cells
  JOURNAL   J Cell Sci 136 (10) (2023)
   PUBMED   37132654
  REMARK    GeneRIF: Pacsin 2-dependent N-cadherin internalization regulates
            the migration behaviour of malignant cancer cells.
REFERENCE   3  (residues 1 to 447)
  AUTHORS   Zudeh,G., Franca,R., Lucafo,M., Bonten,E.J., Bramuzzo,M.,
            Sgarra,R., Lagatolla,C., Franzin,M., Evans,W.E., Decorti,G. and
            Stocco,G.
  TITLE     PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells
  JOURNAL   Life Sci Alliance 6 (3), e202201610 (2023)
   PUBMED   36596605
  REMARK    GeneRIF: PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 447)
  AUTHORS   Park,K., Yoo,H.S., Oh,C.K., Lee,J.R., Chung,H.J., Kim,H.N.,
            Kim,S.H., Kee,K.M., Kim,T.Y., Kim,M., Kim,B.G., Ra,J.S., Myung,K.,
            Kim,H., Han,S.H., Seo,M.D., Lee,Y. and Kim,D.W.
  TITLE     Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate
            drug resistance in chronic myeloid leukemia
  JOURNAL   Cancer Med 11 (21), 4005-4020 (2022)
   PUBMED   35352878
  REMARK    GeneRIF: Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1
            regulate drug resistance in chronic myeloid leukemia.
REFERENCE   5  (residues 1 to 447)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 447)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 447)
  AUTHORS   Ghadimi,M.P., Sanzenbacher,R., Thiede,B., Wenzel,J., Jing,Q.,
            Plomann,M., Borkhardt,A., Kabelitz,D. and Janssen,O.
  TITLE     Identification of interaction partners of the cytosolic polyproline
            region of CD95 ligand (CD178)
  JOURNAL   FEBS Lett 519 (1-3), 50-58 (2002)
   PUBMED   12023017
REFERENCE   8  (residues 1 to 447)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 447)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 447)
  AUTHORS   Ritter,B., Modregger,J., Paulsson,M. and Plomann,M.
  TITLE     PACSIN 2, a novel member of the PACSIN family of cytoplasmic
            adapter proteins
  JOURNAL   FEBS Lett 454 (3), 356-362 (1999)
   PUBMED   10431838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136845.1, DB477051.1,
            BC008037.2, HY342978.1, AF128536.1 and BI964045.1.
            
            On Mar 31, 2017 this sequence version replaced XP_016884054.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation by
            regulating tubulin polymerization. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (8) differs in the 5' UTR,
            contains an alternate in-frame exon and  lacks an alternate
            in-frame exon in the 3' coding region, compared to variant 1. The
            resulting protein (isoform C) has the same N- and C-termini, but is
            shorter than isoform A. Variants 4, 7, 8 and 9 encode the same
            protein (isoform C).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..447
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..447
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 2 isoform C"
                     /note="syndapin2; syndapin-II; syndapin-2; cytoplasmic
                     phosphoprotein PACSIN2"
                     /calculated_mol_wt=51466
     Region          18..275
                     /region_name="F-BAR_PACSIN2"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein
                     kinase Substrate in Neurons 2 (PACSIN2); cd07679"
                     /db_xref="CDD:153363"
     Site            order(18..20,26..27,30,33,36..37,40..41,43..44,47..48,
                     51..52,54..55,58..59,62,65..66,74..75,79,83,86..87,89,97,
                     145,149,212,227,230,234,237..238,240..242,245,248..249,
                     251..252,255..258,263..264,267,270..271,274..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153363"
     Site            order(25,29,36,46,50,53,65,101,113,132,139..140,147..148,
                     150,203,207,210)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153363"
     Region          390..445
                     /region_name="SH3_PACSIN1-2"
                     /note="Src homology 3 domain of Protein kinase C and
                     Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN
                     2; cd11998"
                     /db_xref="CDD:212931"
     Site            order(396,398,401,405,424..425,439,441..442)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212931"
     CDS             1..447
                     /gene="PACSIN2"
                     /gene_synonym="SDPII"
                     /coded_by="NM_001349972.1:161..1504"
                     /note="isoform C is encoded by transcript variant 8"
                     /db_xref="GeneID:11252"
                     /db_xref="HGNC:HGNC:8571"
                     /db_xref="MIM:604960"
ORIGIN      
        1 msvtyddsvg vevssdsfwe vgnykrtvkr iddghrlcsd lmnclherar iekayaqqlt
       61 ewarrwrqlv ekgpqygtve kawmafmsea ervselhlev kaslmnddfe kiknwqkeaf
      121 hkqmmggfke tkeaedgfrk aqkpwakklk eveaakkahh aackeeklai sreanskadp
      181 slnpeqlkkl qdkiekckqd vlktkekyek slkeldqgtp qymenmeqvf eqcqqfeekr
      241 lrffrevlle vqkhldlsnv agykaiyhdl eqsiraadav edlrwfranh gpgmamnwpq
      301 fedeewsadl nrtlsrrekk katdgvtltg inqtgdqslp skpssvssye ktqsyptdws
      361 ddesnnpfss tdangdsnpf dddatsgtev rvralydyeg qehdelsfka gdeltkmede
      421 deqgwckgrl dngqvglypa nyveaiq
//
LOCUS       NP_001353546             567 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of G-protein signaling 14 isoform 2 [Homo sapiens].
ACCESSION   NP_001353546 XP_005265851
VERSION     NP_001353546.1
DBSOURCE    REFSEQ: accession NM_001366617.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 567)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 567)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   3  (residues 1 to 567)
  AUTHORS   Wang,J., Guo,Y., He,Y., Qin,Y., Li,X., Yang,L., Liu,K. and Xiao,L.
  TITLE     Hepatic regulator of G protein signaling 14 ameliorates NAFLD
            through activating cAMP-AMPK signaling by targeting Gialpha1/3
  JOURNAL   Mol Metab 80, 101882 (2024)
   PUBMED   38237897
  REMARK    GeneRIF: Hepatic regulator of G protein signaling 14 ameliorates
            NAFLD through activating cAMP-AMPK signaling by targeting
            Gialpha1/3.
REFERENCE   4  (residues 1 to 567)
  AUTHORS   Montanez-Miranda,C., Bramlett,S.N. and Hepler,J.R.
  TITLE     RGS14 expression in CA2 hippocampus, amygdala, and basal ganglia:
            Implications for human brain physiology and disease
  JOURNAL   Hippocampus 33 (3), 166-181 (2023)
   PUBMED   36541898
  REMARK    GeneRIF: RGS14 expression in CA2 hippocampus, amygdala, and basal
            ganglia: Implications for human brain physiology and disease.
            Review article
REFERENCE   5  (residues 1 to 567)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   6  (residues 1 to 567)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 567)
  AUTHORS   Kimple,R.J., De Vries,L., Tronchere,H., Behe,C.I., Morris,R.A.,
            Gist Farquhar,M. and Siderovski,D.P.
  TITLE     RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
            guanine nucleotide dissociation inhibitor Activity
  JOURNAL   J Biol Chem 276 (31), 29275-29281 (2001)
   PUBMED   11387333
REFERENCE   8  (residues 1 to 567)
  AUTHORS   Cho,H., Kozasa,T., Takekoshi,K., De Gunzburg,J. and Kehrl,J.H.
  TITLE     RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha-
            and G13alpha-mediated signaling pathways
  JOURNAL   Mol Pharmacol 58 (3), 569-576 (2000)
   PUBMED   10953050
REFERENCE   9  (residues 1 to 567)
  AUTHORS   Traver,S., Bidot,C., Spassky,N., Baltauss,T., De Tand,M.F.,
            Thomas,J.L., Zalc,B., Janoueix-Lerosey,I. and Gunzburg,J.D.
  TITLE     RGS14 is a novel Rap effector that preferentially regulates the
            GTPase activity of galphao
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 19-29 (2000)
   PUBMED   10926822
REFERENCE   10 (residues 1 to 567)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC146507.2.
            
            On Oct 13, 2018 this sequence version replaced XP_005265851.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains one RGS domain, two
            Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The
            protein attenuates the signaling activity of G-proteins by binding,
            through its GoLoco domain, to specific types of activated,
            GTP-bound G alpha subunits. Acting as a GTPase activating protein
            (GAP), the protein increases the rate of conversion of the GTP to
            GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.114244.1,
                                           SRR1660807.8302.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..567
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..567
                     /product="regulator of G-protein signaling 14 isoform 2"
                     /calculated_mol_wt=61444
     Region          19..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          58..186
                     /region_name="RGS_RGS14"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS14 protein; cd08743"
                     /db_xref="CDD:188697"
     Site            order(88..90,92..93,130..135,137..138,165,167..169,173)
                     /site_type="other"
                     /note="putative G-alpha-3 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:188697"
     Region          192..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97492; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          302..372
                     /region_name="RBD1_RGS14"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 14 (RGS14); cd17137"
                     /db_xref="CDD:340657"
     Site            order(334,352)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340657"
     Region          373..444
                     /region_name="RBD2_RGS14"
                     /note="Ras-binding domain (RBD) 2 of regulator of G
                     protein signaling 14 (RGS14); cd17139"
                     /db_xref="CDD:340659"
     Site            order(385,407)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340659"
     Region          452..491
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Region          500..521
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          531..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     CDS             1..567
                     /gene="RGS14"
                     /coded_by="NM_001366617.1:102..1805"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:10636"
                     /db_xref="HGNC:HGNC:9996"
                     /db_xref="MIM:602513"
ORIGIN      
        1 mpgkpkhlgv pngrmvlavs dgelssttgp qgqgegrgss lsihslpsgp sspfpteeqp
       61 vaswalsfer llqdplglay fteflkkefs aenvtfwkac erfqqipasd tqqlaqearn
      121 iyqeflssqa lspvnidrqa wlgeevlaep rpdmfraqql qifnlmkfds yarfvksply
      181 recllaeaeg rplrepgssr lgspdatrkk pklkpgkslp lgveelgqlp pvegpggrpl
      241 rksfrrelgg tanaalrres qgslnssasl dlgflafvss kseshrkslg stegesesrp
      301 gkyccvylpd gtaslalarp gltirdmlag icekrglslp dikvylvgne qkalvldqdc
      361 tvladqevrl enritfelel talervvris akptkrlqea lqpilekhgl splevvlhrp
      421 gekqpldlgk lvssvaaqrl vldtlpgvki skardkspcr sqgcpprtqd kathpppasp
      481 sslvkvpssa tgkrqtcdie glvellnrvq ssgahdqrgl lrkedlvlpe flqlpaqgps
      541 seetppqtks aaqpiggsln sttdsal
//
LOCUS       NP_001259002             764 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamine--tRNA ligase isoform b [Homo sapiens].
ACCESSION   NP_001259002
VERSION     NP_001259002.1
DBSOURCE    REFSEQ: accession NM_001272073.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Shen,Y.W., Weng,Z.F., He,W., Chen,Y.H., Wang,Q.H., Zou,L.P.,
            Liu,L.Y. and Shang-Guan,H.K.
  TITLE     [QARS1 gene related glutaminyl-tRNA synthetase deficiency syndrome:
            report of three cases and a review of literature]
  JOURNAL   Zhonghua Er Ke Za Zhi 58 (12), 1006-1012 (2020)
   PUBMED   33256324
  REMARK    GeneRIF: [QARS1 gene related glutaminyl-tRNA synthetase deficiency
            syndrome: report of three cases and a review of literature].
            Review article
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Khan,K., Baleanu-Gogonea,C., Willard,B., Gogonea,V. and Fox,P.L.
  TITLE     3-Dimensional architecture of the human multi-tRNA synthetase
            complex
  JOURNAL   Nucleic Acids Res 48 (15), 8740-8754 (2020)
   PUBMED   32644155
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Bienvenut,W.V., Sumpton,D., Martinez,A., Lilla,S., Espagne,C.,
            Meinnel,T. and Giglione,C.
  TITLE     Comparative large scale characterization of plant versus mammal
            proteins reveals similar and idiosyncratic N-alpha-acetylation
            features
  JOURNAL   Mol Cell Proteomics 11 (6), M111.015131 (2012)
   PUBMED   22223895
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Lamour,V., Quevillon,S., Diriong,S., N'Guyen,V.C., Lipinski,M. and
            Mirande,M.
  TITLE     Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme
            as a case of horizontal gene transfer
  JOURNAL   Proc Natl Acad Sci U S A 91 (18), 8670-8674 (1994)
   PUBMED   8078941
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Kaiser,E., Hu,B., Becher,S., Eberhard,D., Schray,B., Baack,M.,
            Hameister,H. and Knippers,R.
  TITLE     The human EPRS locus (formerly the QARS locus): a gene encoding a
            class I and a class II aminoacyl-tRNA synthetase
  JOURNAL   Genomics 19 (2), 280-290 (1994)
   PUBMED   8188258
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301559.1 and BC000394.2.
            
            Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of
            tRNA by their cognate amino acid. Because of their central role in
            linking amino acids with nucleotide triplets contained in tRNAs,
            aminoacyl-tRNA synthetases are thought to be among the first
            proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA
            synthetases specific for glutamine (gln), glutamic acid (glu), and
            7 other amino acids are associated within a multienzyme complex.
            Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS)
            is absent from many prokaryotes, mitochondria, and chloroplasts, in
            which Gln-tRNA(Gln) is formed by transamidation of the misacylated
            Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I
            aminoacyl-tRNA synthetase family. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. The
            encoded isoform (b) is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301559.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:22223895)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..764
                     /product="glutamine--tRNA ligase isoform b"
                     /EC_number="6.1.1.18"
                     /note="glutamine-tRNA synthetase; glutamine--tRNA ligase"
                     /calculated_mol_wt=86449
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          6..763
                     /region_name="PLN02859"
                     /note="glutamine-tRNA ligase"
                     /db_xref="CDD:178450"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          259..269
                     /region_name="'HIGH' region.
                     /evidence=ECO:0000305|PubMed:26869582"
                     /note="propagated from UniProtKB/Swiss-Prot (P47897.1)"
     Site            298
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     Region          482..486
                     /region_name="'KMSKS' region.
                     /evidence=ECO:0000305|PubMed:26869582"
                     /note="propagated from UniProtKB/Swiss-Prot (P47897.1)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47897.1)"
     CDS             1..764
                     /gene="QARS1"
                     /gene_synonym="GLNRS; MSCCA; PRO2195; QARS"
                     /coded_by="NM_001272073.2:25..2319"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS63633.1"
                     /db_xref="GeneID:5859"
                     /db_xref="HGNC:HGNC:9751"
                     /db_xref="MIM:603727"
ORIGIN      
        1 maaldslslf tslglseqka retlknsals aqlreaatqa qqtlgstidk atgillygla
       61 srlrdtrrls flvsyiatal eyvrshpldp idtvdferec gvgvivtpeq ieeaveaain
      121 rhrpqllver yhfnmgllmg earavlkwad gkmiknevdm qvlhllgpkl eadlekkfkv
      181 akarleetdr rtakdvveng etadqtlslm eqlrgealkf hkpgenyktp gyvvtphtmn
      241 llkqhleitg gqvrtrfppe pngilhigha kainfnfgya kanngicflr fddtnpekee
      301 akfftaicdm vawlgytpyk vtyasdyfdq lyawavelir rglayvchqr geelkghntl
      361 pspwrdrpme eslllfeamr kgkfsegeat lrmklvmedg kmdpvayrvk ytphhrtgdk
      421 wciyptydyt hclcdsiehi thslctkefq arrssyfwlc naldvycpvq weygrlnlhy
      481 avvskrkilq lvatgavrdw ddprlftlta lrrrgfppea innfcarvgv tvaqttmeph
      541 lleacvrdvl ndtapramav leslrviitn fpaaksldiq vpnfpadetk gfhqvpfapi
      601 vfiertdfke epepgfkrla wgqpvglrht gyvielqhvv kgpsgcvesl evtcrradag
      661 ekpkafihwv sqplmcevrl yerlfqhknp edptevpggf lsdlnlaslh vvdaalvdcs
      721 valakpfdkf qferlgyfsv dpdshqgklv fnrtvtlked pgkv
//
LOCUS       NP_001354218             558 aa            linear   PRI 20-NOV-2025
DEFINITION  innate immunity activator protein isoform 3 [Homo sapiens].
ACCESSION   NP_001354218
VERSION     NP_001354218.1
DBSOURCE    REFSEQ: accession NM_001367289.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 558)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Chang,D., Luong,P., Li,Q., LeBarron,J., Anderson,M., Barrett,L. and
            Lencer,W.I.
  TITLE     Small-molecule modulators of INAVA cytosolic condensate and
            cell-cell junction assemblies
  JOURNAL   J Cell Biol 220 (9) (2021)
   PUBMED   34251416
  REMARK    GeneRIF: Small-molecule modulators of INAVA cytosolic condensate
            and cell-cell junction assemblies.
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    GeneRIF: Study identifies C1ORF106 as an epithelial cell junction
            protein, and the loss of C1ORF106 augments TNF-alpha-induced
            intestinal epithelial leakage and diarrhea that may play a critical
            role in the development of inflammatory bowel disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Sawcer,S., Hellenthal,G., Pirinen,M., Spencer,C.C.,
            Patsopoulos,N.A., Moutsianas,L., Dilthey,A., Su,Z., Freeman,C.,
            Hunt,S.E., Edkins,S., Gray,E., Booth,D.R., Potter,S.C., Goris,A.,
            Band,G., Oturai,A.B., Strange,A., Saarela,J., Bellenguez,C.,
            Fontaine,B., Gillman,M., Hemmer,B., Gwilliam,R., Zipp,F.,
            Jayakumar,A., Martin,R., Leslie,S., Hawkins,S., Giannoulatou,E.,
            D'alfonso,S., Blackburn,H., Martinelli Boneschi,F., Liddle,J.,
            Harbo,H.F., Perez,M.L., Spurkland,A., Waller,M.J., Mycko,M.P.,
            Ricketts,M., Comabella,M., Hammond,N., Kockum,I., McCann,O.T.,
            Ban,M., Whittaker,P., Kemppinen,A., Weston,P., Hawkins,C.,
            Widaa,S., Zajicek,J., Dronov,S., Robertson,N., Bumpstead,S.J.,
            Barcellos,L.F., Ravindrarajah,R., Abraham,R., Alfredsson,L.,
            Ardlie,K., Aubin,C., Baker,A., Baker,K., Baranzini,S.E.,
            Bergamaschi,L., Bergamaschi,R., Bernstein,A., Berthele,A.,
            Boggild,M., Bradfield,J.P., Brassat,D., Broadley,S.A., Buck,D.,
            Butzkueven,H., Capra,R., Carroll,W.M., Cavalla,P., Celius,E.G.,
            Cepok,S., Chiavacci,R., Clerget-Darpoux,F., Clysters,K., Comi,G.,
            Cossburn,M., Cournu-Rebeix,I., Cox,M.B., Cozen,W., Cree,B.A.,
            Cross,A.H., Cusi,D., Daly,M.J., Davis,E., de Bakker,P.I.,
            Debouverie,M., D'hooghe,M.B., Dixon,K., Dobosi,R., Dubois,B.,
            Ellinghaus,D., Elovaara,I., Esposito,F., Fontenille,C., Foote,S.,
            Franke,A., Galimberti,D., Ghezzi,A., Glessner,J., Gomez,R.,
            Gout,O., Graham,C., Grant,S.F., Guerini,F.R., Hakonarson,H.,
            Hall,P., Hamsten,A., Hartung,H.P., Heard,R.N., Heath,S., Hobart,J.,
            Hoshi,M., Infante-Duarte,C., Ingram,G., Ingram,W., Islam,T.,
            Jagodic,M., Kabesch,M., Kermode,A.G., Kilpatrick,T.J., Kim,C.,
            Klopp,N., Koivisto,K., Larsson,M., Lathrop,M., Lechner-Scott,J.S.,
            Leone,M.A., Leppa,V., Liljedahl,U., Bomfim,I.L., Lincoln,R.R.,
            Link,J., Liu,J., Lorentzen,A.R., Lupoli,S., Macciardi,F., Mack,T.,
            Marriott,M., Martinelli,V., Mason,D., McCauley,J.L., Mentch,F.,
            Mero,I.L., Mihalova,T., Montalban,X., Mottershead,J., Myhr,K.M.,
            Naldi,P., Ollier,W., Page,A., Palotie,A., Pelletier,J., Piccio,L.,
            Pickersgill,T., Piehl,F., Pobywajlo,S., Quach,H.L., Ramsay,P.P.,
            Reunanen,M., Reynolds,R., Rioux,J.D., Rodegher,M., Roesner,S.,
            Rubio,J.P., Ruckert,I.M., Salvetti,M., Salvi,E., Santaniello,A.,
            Schaefer,C.A., Schreiber,S., Schulze,C., Scott,R.J., Sellebjerg,F.,
            Selmaj,K.W., Sexton,D., Shen,L., Simms-Acuna,B., Skidmore,S.,
            Sleiman,P.M., Smestad,C., Sorensen,P.S., Sondergaard,H.B.,
            Stankovich,J., Strange,R.C., Sulonen,A.M., Sundqvist,E.,
            Syvanen,A.C., Taddeo,F., Taylor,B., Blackwell,J.M., Tienari,P.,
            Bramon,E., Tourbah,A., Brown,M.A., Tronczynska,E., Casas,J.P.,
            Tubridy,N., Corvin,A., Vickery,J., Jankowski,J., Villoslada,P.,
            Markus,H.S., Wang,K., Mathew,C.G., Wason,J., Palmer,C.N.,
            Wichmann,H.E., Plomin,R., Willoughby,E., Rautanen,A.,
            Winkelmann,J., Wittig,M., Trembath,R.C., Yaouanq,J.,
            Viswanathan,A.C., Zhang,H., Wood,N.W., Zuvich,R., Deloukas,P.,
            Langford,C., Duncanson,A., Oksenberg,J.R., Pericak-Vance,M.A.,
            Haines,J.L., Olsson,T., Hillert,J., Ivinson,A.J., De Jager,P.L.,
            Peltonen,L., Stewart,G.J., Hafler,D.A., Hauser,S.L., McVean,G.,
            Donnelly,P. and Compston,A.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2
  TITLE     Genetic risk and a primary role for cell-mediated immune mechanisms
            in multiple sclerosis
  JOURNAL   Nature 476 (7359), 214-219 (2011)
   PUBMED   21833088
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Anderson,C.A., Boucher,G., Lees,C.W., Franke,A., D'Amato,M.,
            Taylor,K.D., Lee,J.C., Goyette,P., Imielinski,M., Latiano,A.,
            Lagace,C., Scott,R., Amininejad,L., Bumpstead,S., Baidoo,L.,
            Baldassano,R.N., Barclay,M., Bayless,T.M., Brand,S., Buning,C.,
            Colombel,J.F., Denson,L.A., De Vos,M., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Fehrmann,R.S., Floyd,J.A., Florin,T.,
            Franchimont,D., Franke,L., Georges,M., Glas,J., Glazer,N.L.,
            Guthery,S.L., Haritunians,T., Hayward,N.K., Hugot,J.P., Jobin,G.,
            Laukens,D., Lawrance,I., Lemann,M., Levine,A., Libioulle,C.,
            Louis,E., McGovern,D.P., Milla,M., Montgomery,G.W., Morley,K.I.,
            Mowat,C., Ng,A., Newman,W., Ophoff,R.A., Papi,L., Palmieri,O.,
            Peyrin-Biroulet,L., Panes,J., Phillips,A., Prescott,N.J.,
            Proctor,D.D., Roberts,R., Russell,R., Rutgeerts,P., Sanderson,J.,
            Sans,M., Schumm,P., Seibold,F., Sharma,Y., Simms,L.A.,
            Seielstad,M., Steinhart,A.H., Targan,S.R., van den Berg,L.H.,
            Vatn,M., Verspaget,H., Walters,T., Wijmenga,C., Wilson,D.C.,
            Westra,H.J., Xavier,R.J., Zhao,Z.Z., Ponsioen,C.Y., Andersen,V.,
            Torkvist,L., Gazouli,M., Anagnou,N.P., Karlsen,T.H., Kupcinskas,L.,
            Sventoraityte,J., Mansfield,J.C., Kugathasan,S., Silverberg,M.S.,
            Halfvarson,J., Rotter,J.I., Mathew,C.G., Griffiths,A.M., Gearry,R.,
            Ahmad,T., Brant,S.R., Chamaillard,M., Satsangi,J., Cho,J.H.,
            Schreiber,S., Daly,M.J., Barrett,J.C., Parkes,M., Annese,V.,
            Hakonarson,H., Radford-Smith,G., Duerr,R.H., Vermeire,S.,
            Weersma,R.K. and Rioux,J.D.
  TITLE     Meta-analysis identifies 29 additional ulcerative colitis risk
            loci, increasing the number of confirmed associations to 47
  JOURNAL   Nat Genet 43 (3), 246-252 (2011)
   PUBMED   21297633
  REMARK    Erratum:[Nat Genet. 2011 Sep;43(9):919]
REFERENCE   9  (residues 1 to 558)
  AUTHORS   Franke,A., McGovern,D.P., Barrett,J.C., Wang,K.,
            Radford-Smith,G.L., Ahmad,T., Lees,C.W., Balschun,T., Lee,J.,
            Roberts,R., Anderson,C.A., Bis,J.C., Bumpstead,S., Ellinghaus,D.,
            Festen,E.M., Georges,M., Green,T., Haritunians,T., Jostins,L.,
            Latiano,A., Mathew,C.G., Montgomery,G.W., Prescott,N.J.,
            Raychaudhuri,S., Rotter,J.I., Schumm,P., Sharma,Y., Simms,L.A.,
            Taylor,K.D., Whiteman,D., Wijmenga,C., Baldassano,R.N., Barclay,M.,
            Bayless,T.M., Brand,S., Buning,C., Cohen,A., Colombel,J.F.,
            Cottone,M., Stronati,L., Denson,T., De Vos,M., D'Inca,R.,
            Dubinsky,M., Edwards,C., Florin,T., Franchimont,D., Gearry,R.,
            Glas,J., Van Gossum,A., Guthery,S.L., Halfvarson,J.,
            Verspaget,H.W., Hugot,J.P., Karban,A., Laukens,D., Lawrance,I.,
            Lemann,M., Levine,A., Libioulle,C., Louis,E., Mowat,C., Newman,W.,
            Panes,J., Phillips,A., Proctor,D.D., Regueiro,M., Russell,R.,
            Rutgeerts,P., Sanderson,J., Sans,M., Seibold,F., Steinhart,A.H.,
            Stokkers,P.C., Torkvist,L., Kullak-Ublick,G., Wilson,D.,
            Walters,T., Targan,S.R., Brant,S.R., Rioux,J.D., D'Amato,M.,
            Weersma,R.K., Kugathasan,S., Griffiths,A.M., Mansfield,J.C.,
            Vermeire,S., Duerr,R.H., Silverberg,M.S., Satsangi,J.,
            Schreiber,S., Cho,J.H., Annese,V., Hakonarson,H., Daly,M.J. and
            Parkes,M.
  TITLE     Genome-wide meta-analysis increases to 71 the number of confirmed
            Crohn's disease susceptibility loci
  JOURNAL   Nat Genet 42 (12), 1118-1125 (2010)
   PUBMED   21102463
REFERENCE   10 (residues 1 to 558)
  AUTHORS   Barrett,J.C., Lee,J.C., Lees,C.W., Prescott,N.J., Anderson,C.A.,
            Phillips,A., Wesley,E., Parnell,K., Zhang,H., Drummond,H.,
            Nimmo,E.R., Massey,D., Blaszczyk,K., Elliott,T., Cotterill,L.,
            Dallal,H., Lobo,A.J., Mowat,C., Sanderson,J.D., Jewell,D.P.,
            Newman,W.G., Edwards,C., Ahmad,T., Mansfield,J.C., Satsangi,J.,
            Parkes,M., Mathew,C.G., Donnelly,P., Peltonen,L., Blackwell,J.M.,
            Bramon,E., Brown,M.A., Casas,J.P., Corvin,A., Craddock,N.,
            Deloukas,P., Duncanson,A., Jankowski,J., Markus,H.S., Mathew,C.G.,
            McCarthy,M.I., Palmer,C.N., Plomin,R., Rautanen,A., Sawcer,S.J.,
            Samani,N., Trembath,R.C., Viswanathan,A.C., Wood,N., Spencer,C.C.,
            Barrett,J.C., Bellenguez,C., Davison,D., Freeman,C., Strange,A.,
            Donnelly,P., Langford,C., Hunt,S.E., Edkins,S., Gwilliam,R.,
            Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M., Gray,E.,
            Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J., Perez,M.L.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M., Waller,M., Weston,P.,
            Widaa,S., Whittaker,P., Deloukas,P., Peltonen,L., Mathew,C.G.,
            Blackwell,J.M., Brown,M.A., Corvin,A., McCarthy,M.I., Spencer,C.C.,
            Attwood,A.P., Stephens,J., Sambrook,J., Ouwehand,W.H.,
            McArdle,W.L., Ring,S.M. and Strachan,D.P.
  CONSRTM   UK IBD Genetics Consortium; Wellcome Trust Case Control Consortium
            2
  TITLE     Genome-wide association study of ulcerative colitis identifies
            three new susceptibility loci, including the HNF4A region
  JOURNAL   Nat Genet 41 (12), 1330-1334 (2009)
   PUBMED   19915572
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC099756.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1976338.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..558
                     /product="innate immunity activator protein isoform 3"
                     /note="uncharacterized protein C1orf106; innate immunity
                     activator protein"
                     /calculated_mol_wt=61444
     Region          2..131
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     CDS             1..558
                     /gene="INAVA"
                     /gene_synonym="C1orf106"
                     /coded_by="NM_001367289.1:283..1959"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:55765"
                     /db_xref="HGNC:HGNC:25599"
                     /db_xref="MIM:618051"
ORIGIN      
        1 meskdevsdt dsgiilqsgp dspvspmkel thavhkqqra learleacle elrrlclrea
       61 eltgtlpaey plkpgekapk vrrrigaayk lddwalhred plsslerqla lqlqiteaar
      121 rlcleenlsr qarrqrkhsm lqeekklqel qrclverrrn sepppaaalp lgrelsasdd
      181 sslsdgllle eeesqvpkpp pespappsrp lppqtleglq ptgpeagspe rapvqnspwk
      241 etsldhpyek prkssepwse ssspattpqd gpsasslwll epasyhvvpi rgvpgqwqgr
      301 tsapatpeiq grrgqsqslr vdsfragpeg rgrsafprrr pthytvtvpd scfpatkppl
      361 phaachscse dsgsdvssis hptspgsssp disflqplsp pkthrhrgaw vpagsrelva
      421 hhpklllppg yfpagryvvv aesplppgew elrraapgpa yeeegtplry qrlvpsrsri
      481 vrtpslkdsp agrglskaav seelkwwher arlrstrphs ldrqgafrvp tvcvlrrspd
      541 gapvqvfvpe kgeiisqv
//
LOCUS       NP_542783                341 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 isoform b [Homo sapiens].
ACCESSION   NP_542783
VERSION     NP_542783.2
DBSOURCE    REFSEQ: accession NM_080745.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 341)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 341)
  AUTHORS   Sun,L., Chen,Y., Xia,L., Wang,J., Zhu,J., Li,J., Wang,K., Shen,K.,
            Zhang,D., Zhang,G., Shi,T. and Chen,W.
  TITLE     TRIM69 suppressed the anoikis resistance and metastasis of gastric
            cancer through ubiquitin-proteasome-mediated degradation of PRKCD
  JOURNAL   Oncogene 42 (49), 3619-3632 (2023)
   PUBMED   37864033
  REMARK    GeneRIF: TRIM69 suppressed the anoikis resistance and metastasis of
            gastric cancer through ubiquitin-proteasome-mediated degradation of
            PRKCD.
REFERENCE   3  (residues 1 to 341)
  AUTHORS   Wang,Y., Risteski,P., Yang,Y., Chen,H., Droby,G., Walens,A.,
            Jayaprakash,D., Troester,M., Herring,L., Chernoff,J., Tolic,I.M.,
            Bowser,J. and Vaziri,C.
  TITLE     The TRIM69-MST2 signaling axis regulates centrosome dynamics and
            chromosome segregation
  JOURNAL   Nucleic Acids Res 51 (19), 10568-10589 (2023)
   PUBMED   37739411
  REMARK    GeneRIF: The TRIM69-MST2 signaling axis regulates centrosome
            dynamics and chromosome segregation.
REFERENCE   4  (residues 1 to 341)
  AUTHORS   Yuan,J., Lv,T., Yang,J., Wu,Z., Yan,L., Yang,J. and Shi,Y.
  TITLE     HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability by
            diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma
  JOURNAL   Redox Biol 58, 102546 (2022)
   PUBMED   36423520
  REMARK    GeneRIF: HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability
            by diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 341)
  AUTHORS   Song,Y., Nguyen,X.N., Kumar,A., da Silva,C., Picard,L., Etienne,L.
            and Cimarelli,A.
  TITLE     Trim69 is a microtubule regulator that acts as a pantropic viral
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 119 (43), e2211467119 (2022)
   PUBMED   36251989
  REMARK    GeneRIF: Trim69 is a microtubule regulator that acts as a pantropic
            viral inhibitor.
REFERENCE   6  (residues 1 to 341)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
  REMARK    GeneRIF: hTRIM69 is a novel E3 ubiquitin ligase identified from
            human testis and may function to ubiquitinate its particular
            substrates during spermatogenesis.
REFERENCE   7  (residues 1 to 341)
  AUTHORS   Bahmanyar,S., Kaplan,D.D., Deluca,J.G., Giddings,T.H. Jr.,
            O'Toole,E.T., Winey,M., Salmon,E.D., Casey,P.J., Nelson,W.J. and
            Barth,A.I.
  TITLE     beta-Catenin is a Nek2 substrate involved in centrosome separation
  JOURNAL   Genes Dev 22 (1), 91-105 (2008)
   PUBMED   18086858
REFERENCE   8  (residues 1 to 341)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     Forced expression of RNF36 induces cell apoptosis
  JOURNAL   Exp Cell Res 287 (2), 301-313 (2003)
   PUBMED   12837286
REFERENCE   9  (residues 1 to 341)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     A novel member of the RBCC family, Trif, expressed specifically in
            the spermatids of mouse testis
  JOURNAL   Mech Dev 108 (1-2), 213-216 (2001)
   PUBMED   11578878
  REMARK    GeneRIF: Gene and protein analysis of the mouse counterpart.
REFERENCE   10 (residues 1 to 341)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI827618.1, BC033314.1,
            AC122108.2 and DB524904.1.
            
            On Oct 9, 2003 this sequence version replaced NP_542783.1.
            
            Summary: This gene encodes a member of the RING-B-box-coiled-coil
            (RBCC) family and encodes a protein with an N-terminal RING finger
            motif, a PRY domain and a C-terminal SPRY domain. The mouse
            ortholog of this gene is specifically expressed in germ cells at
            the round spermatid stages during spermatogenesis and, when
            overexpressed, induces apoptosis. Alternatively spliced transcript
            variants encoding distinct isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (b) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant a, resulting in
            an isoform (b) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033314.1, SRR5189667.189196.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..341
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..341
                     /product="E3 ubiquitin-protein ligase TRIM69 isoform b"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 36; RFP-like domain-containing
                     protein trimless; E3 ubiquitin-protein ligase TRIM69;
                     RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=39123
     Region          152..338
                     /region_name="SPRY_PRY_TRIM69"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     69 (TRIM69), also known as RING finger protein 36 (RNF36);
                     cd15818"
                     /db_xref="CDD:293990"
     CDS             1..341
                     /gene="TRIM69"
                     /gene_synonym="HSD-34; HSD34; RNF36; Trif"
                     /coded_by="NM_080745.5:178..1203"
                     /note="isoform b is encoded by transcript variant b"
                     /db_xref="CCDS:CCDS10114.1"
                     /db_xref="GeneID:140691"
                     /db_xref="HGNC:HGNC:17857"
                     /db_xref="MIM:616017"
ORIGIN      
        1 meeelaiqqg qlettlkelq tlrnmqkeai aahkenklhl qqhvsmeflk lhqflhskek
       61 diltelreeg kalneemeln lsqlqeqcll akdmlvsiqa kteqqnsfdf lkdittllhs
      121 leqgmkvlat relisrklnl gqykgpiqym vwremqdtlc pglspltldp ktahpnlvls
      181 ksqtsvwhgd ikkimpddpe rfdssvavlg srgftsgkwy wevevakktk wtvgvvresi
      241 irkgscpltp eqgfwllrlr nqtdlkaldl psfsltltnn ldkvgiyldy eggqlsfyna
      301 ktmthiytfs ntfmeklypy fcpclndgge nkeplhilhp q
//
LOCUS       NP_115749                256 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb group RING finger protein 5 [Homo sapiens].
ACCESSION   NP_115749
VERSION     NP_115749.2
DBSOURCE    REFSEQ: accession NM_032373.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 256)
  AUTHORS   Hauri,S., Comoglio,F., Seimiya,M., Gerstung,M., Glatter,T.,
            Hansen,K., Aebersold,R., Paro,R., Gstaiger,M. and Beisel,C.
  TITLE     A High-Density Map for Navigating the Human Polycomb Complexome
  JOURNAL   Cell Rep 17 (2), 583-595 (2016)
   PUBMED   27705803
REFERENCE   6  (residues 1 to 256)
  AUTHORS   Gao,Z., Zhang,J., Bonasio,R., Strino,F., Sawai,A., Parisi,F.,
            Kluger,Y. and Reinberg,D.
  TITLE     PCGF homologs, CBX proteins, and RYBP define functionally distinct
            PRC1 family complexes
  JOURNAL   Mol Cell 45 (3), 344-356 (2012)
   PUBMED   22325352
REFERENCE   7  (residues 1 to 256)
  AUTHORS   Luo,T., Kuriakose,J.A., Zhu,B., Wakeel,A. and McBride,J.W.
  TITLE     Ehrlichia chaffeensis TRP120 interacts with a diverse array of
            eukaryotic proteins involved in transcription, signaling, and
            cytoskeleton organization
  JOURNAL   Infect Immun 79 (11), 4382-4391 (2011)
   PUBMED   21859857
REFERENCE   8  (residues 1 to 256)
  AUTHORS   Vandamme,J., Volkel,P., Rosnoblet,C., Le Faou,P. and Angrand,P.O.
  TITLE     Interaction proteomics analysis of polycomb proteins defines
            distinct PRC1 complexes in mammalian cells
  JOURNAL   Mol Cell Proteomics 10 (4), M110.002642 (2011)
   PUBMED   21282530
REFERENCE   9  (residues 1 to 256)
  AUTHORS   Wakeel,A., Kuriakose,J.A. and McBride,J.W.
  TITLE     An Ehrlichia chaffeensis tandem repeat protein interacts with
            multiple host targets involved in cell signaling, transcriptional
            regulation, and vesicle trafficking
  JOURNAL   Infect Immun 77 (5), 1734-1745 (2009)
   PUBMED   19273555
REFERENCE   10 (residues 1 to 256)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI464238.1, AL832496.1, AC026227.8 and BQ420347.1.
            
            On Jul 29, 2003 this sequence version replaced NP_115749.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2 and 4 all encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.109193.1,
                                           SRR1660807.55467.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000336126.6/ ENSP00000337500.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.32"
     Protein         1..256
                     /product="polycomb group RING finger protein 5"
                     /note="ring finger protein (C3HC4 type) 159; RING finger
                     protein 159"
                     /calculated_mol_wt=29583
     Region          6..100
                     /region_name="RING-HC_PCGF5"
                     /note="RING finger found in polycomb group RING finger
                     protein 5 (PCGF5) and similar proteins; cd16737"
                     /db_xref="CDD:438395"
     Site            order(7..13,15,21,23..24,26..27,29..30,32..35,39..41,
                     44..45,64,66..67,69..72,74..75,77..78,81..82,84,86,89..90,
                     93..94,97..98)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438395"
     Region          94..133
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE9.1)"
     Region          136..256
                     /region_name="RAWUL_PCGF5"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     5 (PCGF5) and similar proteins; cd17084"
                     /db_xref="CDD:340604"
     CDS             1..256
                     /gene="PCGF5"
                     /gene_synonym="RNF159"
                     /coded_by="NM_032373.5:358..1128"
                     /db_xref="CCDS:CCDS7413.1"
                     /db_xref="GeneID:84333"
                     /db_xref="HGNC:HGNC:28264"
                     /db_xref="MIM:617407"
ORIGIN      
        1 matqrkhlvk dfnpyitcyi ckgylikptt vteclhtfck tcivqhfeds ndcprcgnqv
       61 hetnplemlr ldntleeiif klvpglreqe leresefwkk nkpqengqdd tskadkpkvd
      121 eegdeneddk dyhrsdpqia icldclrnng qsgdnvvkgl mkkfircstr vtvgtikkfl
      181 slklklpssy eldvlcngei mgkdhtmefi ymtrwrlrge nfrclncsas qvcsqdgply
      241 qsypmvlqyr pridfg
//
LOCUS       NP_055572               1016 aa            linear   PRI 20-NOV-2025
DEFINITION  mastermind-like protein 1 [Homo sapiens].
ACCESSION   NP_055572 XP_942116
VERSION     NP_055572.1
DBSOURCE    REFSEQ: accession NM_014757.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1016)
  AUTHORS   Lim,J., Frecot,D.I., Stubenrauch,F., Iftner,T. and Simon,C.
  TITLE     Cottontail rabbit papillomavirus E6 proteins: Interaction with
            MAML1 and modulation of the Notch signaling pathway
  JOURNAL   Virology 576, 52-60 (2022)
   PUBMED   36155393
  REMARK    GeneRIF: Cottontail rabbit papillomavirus E6 proteins: Interaction
            with MAML1 and modulation of the Notch signaling pathway.
REFERENCE   2  (residues 1 to 1016)
  AUTHORS   Hamidi,A.A., Forghanifard,M.M., Gholamin,M., Moghbeli,M., Memar,B.,
            Jangjoo,A., Motie,M.R., Molaei,F. and Abbaszadegan,M.R.
  TITLE     Elucidated tumorigenic role of MAML1 and TWIST1 in gastric cancer
            is associated with Helicobacter pylori infection
  JOURNAL   Microb Pathog 162, 105304 (2022)
   PUBMED   34818576
  REMARK    GeneRIF: Elucidated tumorigenic role of MAML1 and TWIST1 in gastric
            cancer is associated with Helicobacter pylori infection.
REFERENCE   3  (residues 1 to 1016)
  AUTHORS   Lehal,R., Zaric,J., Vigolo,M., Urech,C., Frismantas,V., Zangger,N.,
            Cao,L., Berger,A., Chicote,I., Loubery,S., Choi,S.H., Koch,U.,
            Blacklow,S.C., Palmer,H.G., Bornhauser,B., Gonzalez-Gaitan,M.,
            Arsenijevic,Y., Zoete,V., Aster,J.C., Bourquin,J.P. and Radtke,F.
  TITLE     Pharmacological disruption of the Notch transcription factor
            complex
  JOURNAL   Proc Natl Acad Sci U S A 117 (28), 16292-16301 (2020)
   PUBMED   32601208
REFERENCE   4  (residues 1 to 1016)
  AUTHORS   Kim,J., Kwon,H., Shin,Y.K., Song,G., Lee,T., Kim,Y., Jeong,W.,
            Lee,U., Zhang,X., Nam,G., Jeung,H.C., Kim,W. and Jho,E.H.
  TITLE     MAML1/2 promote YAP/TAZ nuclear localization and tumorigenesis
  JOURNAL   Proc Natl Acad Sci U S A 117 (24), 13529-13540 (2020)
   PUBMED   32482852
  REMARK    GeneRIF: MAML1/2 promote YAP/TAZ nuclear localization and
            tumorigenesis.
REFERENCE   5  (residues 1 to 1016)
  AUTHORS   Forghanifard,M.M., Azaraz,S., Ardalan Khales,S., Morshedi Rad,D.
            and Abbaszadegan,M.R.
  TITLE     MAML1 promotes ESCC aggressiveness through upregulation of EMT
            marker TWIST1
  JOURNAL   Mol Biol Rep 47 (4), 2659-2668 (2020)
   PUBMED   32180088
  REMARK    GeneRIF: MAML1 promotes ESCC aggressiveness through upregulation of
            EMT marker TWIST1.
REFERENCE   6  (residues 1 to 1016)
  AUTHORS   Fryer,C.J., Lamar,E., Turbachova,I., Kintner,C. and Jones,K.A.
  TITLE     Mastermind mediates chromatin-specific transcription and turnover
            of the Notch enhancer complex
  JOURNAL   Genes Dev 16 (11), 1397-1411 (2002)
   PUBMED   12050117
  REMARK    GeneRIF: Mastermind mediates chromatin-specific transcription and
            turnover of the Notch enhancer complex
REFERENCE   7  (residues 1 to 1016)
  AUTHORS   Wu,G., Lyapina,S., Das,I., Li,J., Gurney,M., Pauley,A., Chui,I.,
            Deshaies,R.J. and Kitajewski,J.
  TITLE     SEL-10 is an inhibitor of notch signaling that targets notch for
            ubiquitin-mediated protein degradation
  JOURNAL   Mol Cell Biol 21 (21), 7403-7415 (2001)
   PUBMED   11585921
REFERENCE   8  (residues 1 to 1016)
  AUTHORS   Kitagawa,M., Oyama,T., Kawashima,T., Yedvobnick,B., Kumar,A.,
            Matsuno,K. and Harigaya,K.
  TITLE     A human protein with sequence similarity to Drosophila mastermind
            coordinates the nuclear form of notch and a CSL protein to build a
            transcriptional activator complex on target promoters
  JOURNAL   Mol Cell Biol 21 (13), 4337-4346 (2001)
   PUBMED   11390662
REFERENCE   9  (residues 1 to 1016)
  AUTHORS   Wu,L., Aster,J.C., Blacklow,S.C., Lake,R., Artavanis-Tsakonas,S.
            and Griffin,J.D.
  TITLE     MAML1, a human homologue of Drosophila mastermind, is a
            transcriptional co-activator for NOTCH receptors
  JOURNAL   Nat Genet 26 (4), 484-489 (2000)
   PUBMED   11101851
REFERENCE   10 (residues 1 to 1016)
  AUTHORS   Hsieh,J.J., Zhou,S., Chen,L., Young,D.B. and Hayward,S.D.
  TITLE     CIR, a corepressor linking the DNA binding factor CBF1 to the
            histone deacetylase complex
  JOURNAL   Proc Natl Acad Sci U S A 96 (1), 23-28 (1999)
   PUBMED   9874765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2, D83785.1,
            AF221759.1 and AA975821.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_942116.1.
            
            Summary: This protein is the human homolog of mastermind, a
            Drosophila protein that plays a role in the Notch signaling pathway
            involved in cell-fate determination. There is in vitro evidence
            that the human homolog forms a complex with the intracellular
            portion of human Notch receptors and can increase expression of a
            Notch-induced gene. This evidence supports its proposed function as
            a transcriptional co-activator in the Notch signaling pathway.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: D83785.1, DRR138524.171331.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000292599.4/ ENSP00000292599.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1016
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..1016
                     /product="mastermind-like protein 1"
                     /note="mastermind homolog; mastermind-like 1"
                     /calculated_mol_wt=107924
     Region          1..123
                     /region_name="Required for interaction with NOTCH
                     proteins. /evidence=ECO:0000269|PubMed:11101851"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Region          14..71
                     /region_name="MamL-1"
                     /note="MamL-1 domain; pfam09596"
                     /db_xref="CDD:462834"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Region          65..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6T264; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Region          263..487
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6T264; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Site            314
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Region          561..617
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Region          658..681
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Region          796..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92585.3)"
     Site            822
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     Site            1015
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6T264; propagated from
                     UniProtKB/Swiss-Prot (Q92585.3)"
     CDS             1..1016
                     /gene="MAML1"
                     /gene_synonym="Mam-1; Mam1"
                     /coded_by="NM_014757.5:292..3342"
                     /db_xref="CCDS:CCDS34315.1"
                     /db_xref="GeneID:9794"
                     /db_xref="HGNC:HGNC:13632"
                     /db_xref="MIM:605424"
ORIGIN      
        1 mvlptcpmae falprhsavm erlrrrielc rrhhstcear yeavsperle lerqhtfalh
       61 qrciqakakr agkhrqppaa tapapaapap rldaadgpeh grpathlhdt vkrnldsats
      121 pqngdqqngy gdlfpghkkt rreaplgvai ssnglppasp lgqsdkpsga dalqssgkhs
      181 lgldslnkkr ladsslhlng gsnpsesfpl slnkelkqep vedlpcmitg tvgsisqsnl
      241 mpdlnlneqe wkelieelnr svpdedmkdl fnedfeekkd pessgsatqt plaqdinikt
      301 efspaafeqe qlgspqvrag sagqtflgps sapvstdsps lggsqtlfht sgqpradnps
      361 pnlmpasaqa qnaqralagv vlpsqgpgga selssahqlq qiaakqkreq mlqnpqqatp
      421 apapgqmstw qqtgpshssl dvpypmekpa spssykqdft nskllmmpsv nkssprpggp
      481 ylqpshvnll shqppsnlnq nsannqgsvl dygntkplsh ykadcgqgsp gsgqskpalm
      541 aylpqqlshi sheqnslflm kpkpgnmpfr slvppgqeqn pssvpvqaqa tsvgtqppav
      601 svasshnssp ylssqqqaav mkqhqllldq qkqreqqqkh lqqqqflqrq qhllaeqekq
      661 qfqrhltrpp pqyqdptqgs fpqqvgqftg ssaavpgmnt lgpsnsscpr vfpqagnlmp
      721 mgpghasvss lptnsgqqdr gvaqfpgsqn mpqsslygma sgitqivaqp ppqatnghah
      781 iprqtnvgqn tsvsaaygqn slgssglsqq hnkgtlnpgl tkppvprvsp amggqnsswq
      841 hqgmpnlsgq tpgnsnvspf taassfhmqq qahlkmsspq fsqavpnrpm apmssaaavg
      901 sllppvsaqq rtsapapapp ptapqqglpg lspagpelga fsqspasqmg graglhctqa
      961 ypvrtagqel pfaysgqpgg sglssvaght dlidsllknr tseewmsdld dllgsq
//
LOCUS       NP_001354621             888 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform ccc [Homo sapiens].
ACCESSION   NP_001354621
VERSION     NP_001354621.1
DBSOURCE    REFSEQ: accession NM_001367692.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.193521.1,
                                           SRR1803613.148912.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..888
                     /product="SUN domain-containing protein 1 isoform ccc"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=98629
     Region          62..394
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          520..573
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(520,523..524,527,530..531,534..535,537..538,
                     541..542,544..545,548..549,551..552,555,558..559,562,
                     565..566,569..570,572..573)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          532..>665
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          650..708
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          751..886
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..888
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367692.1:52..2718"
                     /note="isoform ccc is encoded by transcript variant 55"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskgddck gkrhldahta
      301 ahsqsprlpg ragtlwhiwa cagyfllqil rrigavgqav srtawsalwl avvapgkaas
      361 gvfwwlgigw yqfvtliswl nvflltrclr nickflvlli plflllagls lrgqgnffsf
      421 lpvlnwasmh rtqrvddpqd vfkpttsrlk qplqgdseaf pwhwmsgveq qvaslsgqch
      481 hhgenlrelt tllqklqarv dqmeggaagp sasvrdavgq ppretdfmaf hqehevrmsh
      541 ledilgklre kseaiqkele qtkqktisav geqllptveh lqleldqlks elsswrhvkt
      601 gcetvdavqe rvdvqvremv kllfsedqqg gsleqllqrf ssqfvskgdl qtmlrdlqlq
      661 ilrnvthhvs vtkqlptsea vvsavseaga sgiteaqara ivnsalklys qdktgmvdfa
      721 lesgggsils trcsetyetk talmslfgip lwyfsqsprv viqpdiypgn cwafkgsqgy
      781 lvvrlsmmih paaftlehip ktlsptgnis sapkdfavyg leneyqeegq llgqftydqd
      841 geslqmfqal krpddtafqi velrifsnwg hpeytclyrf rvhgepvk
//
LOCUS       NP_061945                304 aa            linear   PRI 20-NOV-2025
DEFINITION  small glutamine-rich tetratricopeptide repeat-containing protein
            beta [Homo sapiens].
ACCESSION   NP_061945
VERSION     NP_061945.1
DBSOURCE    REFSEQ: accession NM_019072.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Cho,H., Liu,Y., Chung,S., Chandrasekar,S., Weiss,S. and Shan,S.O.
  TITLE     Dynamic stability of Sgt2 enables selective and privileged client
            handover in a chaperone triad
  JOURNAL   Nat Commun 15 (1), 134 (2024)
   PUBMED   38167697
  REMARK    GeneRIF: Dynamic stability of Sgt2 enables selective and privileged
            client handover in a chaperone triad.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Shi,L., Kan,J., Zhuo,L., Wang,S., Chen,S., Zhang,B. and Ke,B.
  TITLE     Bioinformatics identification of miR-514b-5p promotes NSCLC
            progression and induces PI3K/AKT and p38 pathways by targeting
            small glutamine-rich tetratricopeptide repeat-containing protein
            beta
  JOURNAL   FEBS J 290 (4), 1134-1150 (2023)
   PUBMED   36180981
  REMARK    GeneRIF: Bioinformatics identification of miR-514b-5p promotes
            NSCLC progression and induces PI3K/AKT and p38 pathways by
            targeting small glutamine-rich tetratricopeptide repeat-containing
            protein beta.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Cao,M., Xu,W., Yu,J., Zheng,H., Tan,X., Li,L., Rui,Y., Xu,G.,
            Cui,G., Xu,J., Cao,J., Tao,T., Ke,K. and Wu,Q.
  TITLE     Up-regulation of SGTB is associated with neuronal apoptosis after
            neuroinflammation induced by lipopolysaccharide
  JOURNAL   J Mol Histol 44 (5), 507-518 (2013)
   PUBMED   23820636
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Heavner,G.A., Audhya,T. and Goldstein,G.
  TITLE     Peptide analogs of thymopentin distinguish distinct thymopoietin
            receptor specificities on two human T cell lines
  JOURNAL   Regul Pept 27 (2), 257-262 (1990)
   PUBMED   2158125
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL713334.1, BC012044.1 and AC008560.6.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.40478.1,
                                           SRR3476690.422441.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381007.9/ ENSP00000370395.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..304
                     /product="small glutamine-rich tetratricopeptide
                     repeat-containing protein beta"
                     /note="small glutamine rich protein with tetratricopeptide
                     repeats 2; beta-SGT; small glutamine rich
                     tetratricopeptide repeat containing beta; small
                     glutamine-rich tetratricopeptide repeat (TPR)-containing,
                     beta"
                     /calculated_mol_wt=33298
     Region          5..64
                     /region_name="SGTA_dimer"
                     /note="Homodimerization domain of SGTA; pfam16546"
                     /db_xref="CDD:465168"
     Region          15..49
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Region          85..118
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Region          85..113
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(86,89..90,93..94,96,120,123..124,127..128,130..131,
                     154,157..158,161..162,165)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          92..>200
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          118..148
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          119..152
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Site            131
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Region          153..186
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Region          153..181
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            293
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O43765; propagated from
                     UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96EQ0.1)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EQ0.1)"
     CDS             1..304
                     /gene="SGTB"
                     /gene_synonym="SGT2"
                     /coded_by="NM_019072.3:216..1130"
                     /db_xref="CCDS:CCDS3988.1"
                     /db_xref="GeneID:54557"
                     /db_xref="HGNC:HGNC:23567"
                     /db_xref="MIM:620526"
ORIGIN      
        1 mssikhlvya virflreqsq mdtytsdeqe slevaiqcle tvfkispedt hlavsqplte
       61 mftssfcknd vlplsnsvpe dvgkadqlkd egnnhmkeen yaaavdcytq aieldpnnav
      121 yycnraaaqs klghytdaik dcekaiaids kyskaygrmg laltalnkfe eavtsyqkal
      181 dldpendsyk snlkiaeqkl revssptgtg lsfdmaslin npafismaas lmqnpqvqql
      241 msgmmtnaig gpaagvgglt dlssliqagq qfaqqiqqqn pelieqlrnh irsrsfsssa
      301 eehs
//
LOCUS       NP_001230442             435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_001230442
VERSION     NP_001230442.1
DBSOURCE    REFSEQ: accession NM_001243513.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB362218.1, AY388459.1,
            AB020639.1 and BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (13) lacks the 5' exon but has
            more than two alternate 5' exons and uses a downstream AUG start
            codon, compared to variant 1. The resulting isoform (2) is shorter
            at the N-terminus, compared to isoform 1. Variants 2-4, 9-15, and
            17-21 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY388459.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243513.1:282..1589"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_001354629             855 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform kkk [Homo sapiens].
ACCESSION   NP_001354629
VERSION     NP_001354629.1
DBSOURCE    REFSEQ: accession NM_001367700.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 855)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 855)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 855)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 855)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 855)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 855)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 855)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 855)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 855)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 855)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968968,
                              SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..855
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..855
                     /product="SUN domain-containing protein 1 isoform kkk"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=95063
     Region          62..361
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          487..540
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(487,490..491,494,497..498,501..502,504..505,
                     508..509,511..512,515..516,518..519,522,525..526,529,
                     532..533,536..537,539..540)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          499..>632
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          617..675
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          718..853
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..855
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367700.1:52..2619"
                     /note="isoform kkk is encoded by transcript variant 63"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskgddck gkrhldahta
      301 ahsqsprlpg ragtlwhiwa cagkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic
      361 kflvlliplf lllaglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl
      421 qgdseafpwh wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas
      481 vrdavgqppr etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq
      541 llptvehlql eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl
      601 eqllqrfssq fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi
      661 teaqaraivn salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy
      721 fsqsprvviq pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap
      781 kdfavyglen eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe
      841 ytclyrfrvh gepvk
//
LOCUS       NP_001308773             175 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 4 isoform 5 [Homo sapiens].
ACCESSION   NP_001308773
VERSION     NP_001308773.1
DBSOURCE    REFSEQ: accession NM_001321844.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068338.14.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279848.2896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..175
                     /product="COMM domain-containing protein 4 isoform 5"
                     /note="COMM domain-containing protein 4"
                     /calculated_mol_wt=18864
     Region          1..174
                     /region_name="Commd4"
                     /note="COMM_Domain containing protein 4. The COMM Domain
                     is found at the C-terminus of a variety of proteins;
                     presumably all COMM_Domain containing proteins are located
                     in the nucleus and the COMM domain plays a role in
                     protein-protein interactions. Several...; cd04752"
                     /db_xref="CDD:240100"
     CDS             1..175
                     /gene="COMMD4"
                     /coded_by="NM_001321844.2:182..709"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="GeneID:54939"
                     /db_xref="HGNC:HGNC:26027"
                     /db_xref="MIM:616701"
ORIGIN      
        1 mssvklrllc sqvlkellgq gidyekilkl tadakfesgd vkatvavlsf ilssaakhsv
       61 dgeslsselq qlglpkehaa slcrcyeekq splqkhlrvc slrmnrlagv gwrvdytlss
      121 sllqsveepm vhlrlevaaa pgtpaqpvam slsadkfqvl laelkqaqtl msslg
//
LOCUS       NP_002766                480 aa            linear   PRI 20-NOV-2025
DEFINITION  serine protease HTRA1 precursor [Homo sapiens].
ACCESSION   NP_002766
VERSION     NP_002766.1
DBSOURCE    REFSEQ: accession NM_002775.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Sun,Y., Yang,H., Guo,J., Du,J., Han,S. and Yang,X.
  TITLE     Identification of HTRA1, DPT and MXRA5 as potential biomarkers
            associated with osteoarthritis progression and immune infiltration
  JOURNAL   BMC Musculoskelet Disord 25 (1), 647 (2024)
   PUBMED   39148085
  REMARK    GeneRIF: Identification of HTRA1, DPT and MXRA5 as potential
            biomarkers associated with osteoarthritis progression and immune
            infiltration.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Beaufort,N., Ingendahl,L., Merdanovic,M., Schmidt,A.,
            Podlesainski,D., Richter,T., Neumann,T., Kuszner,M., Vetter,I.R.,
            Stege,P., Burston,S.G., Filipovic,A., Ruiz-Blanco,Y.B.,
            Bravo-Rodriguez,K., Mieres-Perez,J., Beuck,C., Uebel,S., Zobawa,M.,
            Schillinger,J., Malik,R., Todorov-Volgyi,K., Rey,J., Roberti,A.,
            Hagemeier,B., Wefers,B., Muller,S.A., Wurst,W., Sanchez-Garcia,E.,
            Zimmermann,A., Hu,X.Y., Clausen,T., Huber,R., Lichtenthaler,S.F.,
            Schmuck,C., Giese,M., Kaiser,M., Ehrmann,M. and Dichgans,M.
  TITLE     Rational correction of pathogenic conformational defects in HTRA1
  JOURNAL   Nat Commun 15 (1), 5944 (2024)
   PUBMED   39013852
  REMARK    GeneRIF: Rational correction of pathogenic conformational defects
            in HTRA1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Navneet,S., Ishii,M. and Rohrer,B.
  TITLE     Altered Elastin Turnover, Immune Response, and Age-Related Retinal
            Thinning in a Transgenic Mouse Model With RPE-Specific HTRA1
            Overexpression
  JOURNAL   Invest Ophthalmol Vis Sci 65 (8), 34 (2024)
   PUBMED   39028977
  REMARK    GeneRIF: Altered Elastin Turnover, Immune Response, and Age-Related
            Retinal Thinning in a Transgenic Mouse Model With RPE-Specific
            HTRA1 Overexpression.
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Shi,H., Yuan,M., Cai,J., Lan,L., Wang,Y., Wang,W., Zhou,J.,
            Wang,B., Yu,W., Dong,Z., Deng,D., Qian,Q., Li,Y., Zhou,X. and
            Liu,J.
  TITLE     HTRA1-driven detachment of type I collagen from endoplasmic
            reticulum contributes to myocardial fibrosis in dilated
            cardiomyopathy
  JOURNAL   J Transl Med 22 (1), 297 (2024)
   PUBMED   38515161
  REMARK    GeneRIF: HTRA1-driven detachment of type I collagen from
            endoplasmic reticulum contributes to myocardial fibrosis in dilated
            cardiomyopathy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Zhao,W., Wu,Y., Wang,S., Zhao,F., Liu,W., Xue,Z., Zhang,L.,
            Wang,J., Han,M., Li,X. and Huang,B.
  TITLE     HTRA1 promotes EMT through the HDAC6/Ac-alpha-tubulin pathway in
            human GBM cells
  JOURNAL   CNS Neurosci Ther 30 (2), e14605 (2024)
   PUBMED   38334007
  REMARK    GeneRIF: HTRA1 promotes EMT through the HDAC6/Ac-alpha-tubulin
            pathway in human GBM cells.
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Baldi,A., De Luca,A., Morini,M., Battista,T., Felsani,A., Baldi,F.,
            Catricala,C., Amantea,A., Noonan,D.M., Albini,A., Natali,P.G.,
            Lombardi,D. and Paggi,M.G.
  TITLE     The HtrA1 serine protease is down-regulated during human melanoma
            progression and represses growth of metastatic melanoma cells
  JOURNAL   Oncogene 21 (43), 6684-6688 (2002)
   PUBMED   12242667
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Hu,S.I., Carozza,M., Klein,M., Nantermet,P., Luk,D. and Crowl,R.M.
  TITLE     Human HtrA, an evolutionarily conserved serine protease identified
            as a differentially expressed gene product in osteoarthritic
            cartilage
  JOURNAL   J Biol Chem 273 (51), 34406-34412 (1998)
   PUBMED   9852107
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Zumbrunn,J. and Trueb,B.
  TITLE     Localization of the gene for a serine protease with IGF-binding
            domain (PRSS11) to human chromosome 10q25.3-q26.2
  JOURNAL   Genomics 45 (2), 461-462 (1997)
   PUBMED   9344681
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Zumbrunn,J. and Trueb,B.
  TITLE     Primary structure of a putative serine protease specific for
            IGF-binding proteins
  JOURNAL   FEBS Lett 398 (2-3), 187-192 (1996)
   PUBMED   8977104
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Onodera,O., Nozaki,H. and Fukutake,T.
  TITLE     HTRA1 Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20437615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA633502.1 and Y07921.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the trypsin family of serine
            proteases. This protein is a secreted enzyme that is proposed to
            regulate the availability of insulin-like growth factors (IGFs) by
            cleaving IGF-binding proteins. It has also been suggested to be a
            regulator of cell growth. Variations in the promoter region of this
            gene are the cause of susceptibility to age-related macular
            degeneration type 7. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC031082.1, D87258.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368984.8/ ENSP00000357980.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..480
                     /product="serine protease HTRA1 precursor"
                     /EC_number="3.4.21.-"
                     /note="IGFBP5-protease; protease, serine, 11 (IGF
                     binding); serine protease HTRA1; high-temperature
                     requirement A serine peptidase 1"
                     /calculated_mol_wt=49048
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2257
     mat_peptide     23..480
                     /product="serine protease HTRA1"
                     /calculated_mol_wt=49048
     Region          35..111
                     /region_name="IB"
                     /note="Insulin growth factor-binding protein homologues;
                     smart00121"
                     /db_xref="CDD:197525"
     Region          115..155
                     /region_name="KAZAL"
                     /note="Kazal type serine protease inhibitors; smart00280"
                     /db_xref="CDD:197624"
     Site            169
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000269|PubMed:21297635; propagated from
                     UniProtKB/Swiss-Prot (Q92743.1)"
     Site            171
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000269|PubMed:21297635; propagated from
                     UniProtKB/Swiss-Prot (Q92743.1)"
     Region          202..477
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
     Region          204..364
                     /region_name="Serine protease"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92743.1)"
     Site            278
                     /site_type="other"
                     /note="Involved in trimer stabilization.
                     /evidence=ECO:0000269|PubMed:21297635; propagated from
                     UniProtKB/Swiss-Prot (Q92743.1)"
     CDS             1..480
                     /gene="HTRA1"
                     /gene_synonym="ARMD7; CADASIL2; CARASIL; CARASIL2; HtrA;
                     L56; ORF480; PRSS11"
                     /coded_by="NM_002775.5:101..1543"
                     /db_xref="CCDS:CCDS7630.1"
                     /db_xref="GeneID:5654"
                     /db_xref="HGNC:HGNC:9476"
                     /db_xref="MIM:602194"
ORIGIN      
        1 mqipraallp llllllaapa saqlsragrs aplaagcpdr ceparcppqp ehceggrard
       61 acgccevcga pegaacglqe gpcgeglqcv vpfgvpasat vrrraqaglc vcassepvcg
      121 sdantyanlc qlraasrrse rlhrppvivl qrgacgqgqe dpnslrhkyn fiadvvekia
      181 pavvhielfr klpfskrevp vasgsgfivs edglivtnah vvtnkhrvkv elkngatyea
      241 kikdvdekad ialikidhqg klpvlllgrs selrpgefvv aigspfslqn tvttgivstt
      301 qrggkelglr nsdmdyiqtd aiinygnsgg plvnldgevi gintlkvtag isfaipsdki
      361 kkflteshdr qakgkaitkk kyigirmmsl tsskakelkd rhrdfpdvis gayiievipd
      421 tpaeagglke ndviisingq svvsandvsd vikrestlnm vvrrgnedim itvipeeidp
//
LOCUS       NP_835237                392 aa            linear   PRI 20-NOV-2025
DEFINITION  polymerase delta-interacting protein 3 isoform 2 [Homo sapiens].
ACCESSION   NP_835237
VERSION     NP_835237.1
DBSOURCE    REFSEQ: accession NM_178136.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 392)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 392)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 392)
  AUTHORS   Bjorkman,A., Johansen,S.L., Lin,L., Schertzer,M., Kanellis,D.C.,
            Katsori,A.M., Christensen,S.T., Luo,Y., Andersen,J.S.,
            Elsasser,S.J., Londono-Vallejo,A., Bartek,J. and Schou,K.B.
  TITLE     Human RTEL1 associates with Poldip3 to facilitate responses to
            replication stress and R-loop resolution
  JOURNAL   Genes Dev 34 (15-16), 1065-1074 (2020)
   PUBMED   32561545
  REMARK    GeneRIF: Human RTEL1 associates with Poldip3 to facilitate
            responses to replication stress and R-loop resolution.
REFERENCE   4  (residues 1 to 392)
  AUTHORS   Wang,X., Zhang,S., Zheng,R., Yue,F., Lin,S.H., Rahmeh,A.A.,
            Lee,E.Y., Zhang,Z. and Lee,M.Y.
  TITLE     PDIP46 (DNA polymerase delta interacting protein 46) is an
            activating factor for human DNA polymerase delta
  JOURNAL   Oncotarget 7 (5), 6294-6313 (2016)
   PUBMED   26819372
  REMARK    GeneRIF: Altered expression of PDIP46 or its mutation may affect
            Pol delta functions in vivo, and thereby be a nexus for altered
            genomic stability.
REFERENCE   5  (residues 1 to 392)
  AUTHORS   Suzuki,H., Shibagaki,Y., Hattori,S. and Matsuoka,M.
  TITLE     Nuclear TDP-43 causes neuronal toxicity by escaping from the
            inhibitory regulation by hnRNPs
  JOURNAL   Hum Mol Genet 24 (6), 1513-1527 (2015)
   PUBMED   25378556
  REMARK    GeneRIF: hnRNP-U inhibits TDP-43-mediated alterations in splicing
            of POLDIP3 mRNA.
REFERENCE   6  (residues 1 to 392)
  AUTHORS   Dufu,K., Livingstone,M.J., Seebacher,J., Gygi,S.P., Wilson,S.A. and
            Reed,R.
  TITLE     ATP is required for interactions between UAP56 and two conserved
            mRNA export proteins, Aly and CIP29, to assemble the TREX complex
  JOURNAL   Genes Dev 24 (18), 2043-2053 (2010)
   PUBMED   20844015
REFERENCE   7  (residues 1 to 392)
  AUTHORS   Ma,X.M., Yoon,S.O., Richardson,C.J., Julich,K. and Blenis,J.
  TITLE     SKAR links pre-mRNA splicing to mTOR/S6K1-mediated enhanced
            translation efficiency of spliced mRNAs
  JOURNAL   Cell 133 (2), 303-313 (2008)
   PUBMED   18423201
  REMARK    GeneRIF: SKAR-mediated recruitment of activated S6K1 to newly
            processed mRNPs serves as a conduit between mTOR checkpoint
            signaling and the pioneer round of translation when cells exist in
            conditions supportive of protein synthesis.
REFERENCE   8  (residues 1 to 392)
  AUTHORS   Smyk,A., Szuminska,M., Uniewicz,K.A., Graves,L.M. and Kozlowski,P.
  TITLE     Human enhancer of rudimentary is a molecular partner of
            PDIP46/SKAR, a protein interacting with DNA polymerase delta and
            S6K1 and regulating cell growth
  JOURNAL   FEBS J 273 (20), 4728-4741 (2006)
   PUBMED   16984396
  REMARK    GeneRIF: This study showed that PDIP46 aka SKAR, a protein
            possessing one RNA recognition motif (RRM) and being a protein
            partner of both the p50 subunit of DNA polymerase delta and p70
            ribosomal protein S6 kinase 1 (S6K1).
REFERENCE   9  (residues 1 to 392)
  AUTHORS   Richardson,C.J., Broenstrup,M., Fingar,D.C., Julich,K.,
            Ballif,B.A., Gygi,S. and Blenis,J.
  TITLE     SKAR is a specific target of S6 kinase 1 in cell growth control
  JOURNAL   Curr Biol 14 (17), 1540-1549 (2004)
   PUBMED   15341740
  REMARK    GeneRIF: SKAR is a specific target of S6K1 and regulates cell
            growth.
REFERENCE   10 (residues 1 to 392)
  AUTHORS   Liu,L., Rodriguez-Belmonte,E.M., Mazloum,N., Xie,B. and Lee,M.Y.
  TITLE     Identification of a novel protein, PDIP38, that interacts with the
            p50 subunit of DNA polymerase delta and proliferating cell nuclear
            antigen
  JOURNAL   J Biol Chem 278 (12), 10041-10047 (2003)
   PUBMED   12522211
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC368557.1 and AL160112.1.
            
            Summary: This gene encodes an RRM (RNA recognition
            motif)-containing protein that participates in the regulation of
            translation by recruiting ribosomal protein S6 kinase beta-1 to
            mRNAs. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1. The encoded isoform (2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.769458.1, AL160112.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148874 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..392
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..392
                     /product="polymerase delta-interacting protein 3 isoform
                     2"
                     /note="polymerase delta-interacting protein 3; polymerase
                     (DNA-directed), delta interacting protein 3; S6K1
                     Aly/REF-like target; RNA-binding protein P46; polymerase
                     (DNA) delta interacting protein 3; 46 kDa DNA polymerase
                     delta interaction protein"
                     /calculated_mol_wt=42764
     Region          251..319
                     /region_name="RRM_SKAR"
                     /note="RNA recognition motif (RRM) found in S6K1
                     Aly/REF-like target (SKAR) and similar proteins; cd12681"
                     /db_xref="CDD:410082"
     CDS             1..392
                     /gene="POLDIP3"
                     /gene_synonym="PDIP3; PDIP46; SKAR"
                     /coded_by="NM_178136.3:27..1205"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS14039.1"
                     /db_xref="GeneID:84271"
                     /db_xref="HGNC:HGNC:23782"
                     /db_xref="MIM:611520"
ORIGIN      
        1 madisldeli rkrgaaakgr lnarpgvggv rsrvgiqqgl lsqstrtatf qqrfdarqki
       61 glsdarlklg vkdarekllq kdarfrikgk vqdaremlns rkqqttvpqk prqvadarek
      121 islkrsspaa finppigtvt palkltktiq nlydldeddd giasvptkqm kfaasggflh
      181 hmaglssskl smskalpltk vvqndaytap alpssirtka ltnmsrtlvn keeppkelpa
      241 aepvlspleg tkmtvnnlhp rvteedivel fcvcgalkra rlvhpgvaev vfvkkddait
      301 aykkynnrcl dgqpmkcnlh mngnvitsdq pillrlsdsp smkkeselpr rvnsasssnp
      361 paevdpdtil kalfkssgas vttqptefki kl
//
LOCUS       NP_001293137             596 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform n [Homo sapiens].
ACCESSION   NP_001293137 XP_005266807
VERSION     NP_001293137.1
DBSOURCE    REFSEQ: accession NM_001306208.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 596)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 596)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 596)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 596)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 596)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 596)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 596)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 596)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 596)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 596)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK095041.1, FR748219.1 and
            AC091103.4.
            
            On Apr 16, 2015 this sequence version replaced XP_005266807.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (14) differs in the 5' UTR and
            coding sequence, and uses two alternate in-frame splice sites in
            the coding region, compared to variant 3. The encoded isoform (n)
            has a shorter and distinct N-terminus compared to isoform c.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments. Sequence
            Note: This gene is distinct from TCF7L2 (alias TCF-4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FR748219.1, SRR7410570.642107.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..596
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..596
                     /product="transcription factor 4 isoform n"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=63985
     Region          487..571
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(495,499,501..503,505,510,531..532)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(508..509,512..513,515..516,519,523,533,536,540,543,
                     546..551)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..596
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001306208.1:282..2072"
                     /note="isoform n is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS77191.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mkdiffqfii arvrkcysls clhtlpvvpt lrktergsys sygresnlqg chqsllggdm
       61 dmgnpgtlsp tkpgsqyyqy ssnnprrrpl hssamevqtk kvrkvppglp ssvyapsast
      121 adynrdspgy psskpatstf pssffmqdgh hssdpwssss gmnqpgyagm lgnsshipqs
      181 ssycslhphe rlsypshssa dinsslppms tfhrsgtnhy stssctppan gtdsimanrg
      241 sgaagssqtg dalgkalasi yspdhtnnsf ssnpstpvgs ppslsagtav wsrnggqass
      301 spnyegplhs lqsriedrle rlddaihvlr nhavgpstam pgghgdmhgi igpshngamg
      361 glgsgygtgl lsanrhslmv gthredgval rgshsllpnq vpvpqlpvqs atspdlnppq
      421 dpyrgmppgl qgqsvssgss eiksddegde nlqdtkssed kkldddkkdi ksitsnndde
      481 dltpeqkaer ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav
      541 avilsleqqv rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_000988                 97 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL37 [Homo sapiens].
ACCESSION   NP_000988
VERSION     NP_000988.1
DBSOURCE    REFSEQ: accession NM_000997.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 97)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 97)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 97)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 97)
  AUTHORS   Chaillou,T., Zhang,X. and McCarthy,J.J.
  TITLE     Expression of Muscle-Specific Ribosomal Protein L3-Like Impairs
            Myotube Growth
  JOURNAL   J Cell Physiol 231 (9), 1894-1902 (2016)
   PUBMED   26684695
REFERENCE   5  (residues 1 to 97)
  AUTHORS   Khatter,H., Myasnikov,A.G., Natchiar,S.K. and Klaholz,B.P.
  TITLE     Structure of the human 80S ribosome
  JOURNAL   Nature 520 (7549), 640-645 (2015)
   PUBMED   25901680
REFERENCE   6  (residues 1 to 97)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
   PUBMED   11401437
REFERENCE   7  (residues 1 to 97)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   8  (residues 1 to 97)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   9  (residues 1 to 97)
  AUTHORS   Su,S. and Bird,R.C.
  TITLE     Cell cycle, differentiation and tissue-independent expression of
            ribosomal protein L37
  JOURNAL   Eur J Biochem 232 (3), 789-797 (1995)
   PUBMED   7588717
REFERENCE   10 (residues 1 to 97)
  AUTHORS   Barnard,G.F., Staniunas,R.J., Puder,M., Steele,G.D. Jr. and
            Chen,L.B.
  TITLE     Human ribosomal protein L37 has motifs predicting serine/threonine
            phosphorylation and a zinc-finger domain
  JOURNAL   Biochim Biophys Acta 1218 (3), 425-428 (1994)
   PUBMED   7545944
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC008810.8.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L37E family of ribosomal proteins. It is located in the
            cytoplasm. The protein contains a C2C2-type zinc finger-like motif.
            As is typical for genes encoding ribosomal proteins, there are
            multiple processed pseudogenes of this gene dispersed through the
            genome. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.490308.1,
                                           SRR3476690.779581.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000274242.10/ ENSP00000274242.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..97
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..97
                     /product="large ribosomal subunit protein eL37"
                     /note="60S ribosomal protein L37; 60S ribosomal protein
                     L37a; G1.16"
                     /calculated_mol_wt=10947
     Region          1..88
                     /region_name="PTZ00073"
                     /note="60S ribosomal protein L37; Provisional"
                     /db_xref="CDD:240257"
     Site            10
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P61927.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61927.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P61927.2)"
     CDS             1..97
                     /gene="RPL37"
                     /gene_synonym="eL37; L37"
                     /coded_by="NM_000997.5:38..331"
                     /db_xref="CCDS:CCDS3934.1"
                     /db_xref="GeneID:6167"
                     /db_xref="HGNC:HGNC:10347"
                     /db_xref="MIM:604181"
ORIGIN      
        1 mtkgtssfgk rrnkthtlcr rcgskayhlq kstcgkcgyp akrkrkynws akakrrnttg
       61 tgrmrhlkiv yrrfrhgfre gttpkpkraa vaassss
//
LOCUS       NP_001193638             340 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-AMP-activated protein kinase subunit gamma-1 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001193638
VERSION     NP_001193638.1
DBSOURCE    REFSEQ: accession NM_001206709.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Bai,W., Guo,T., Wang,H., Li,B., Sun,Q., Wu,W., Zhang,J., Zhou,J.,
            Luo,J., Zhu,M., Lu,J., Li,P., Dong,B., Han,S., Pang,X., Zhang,G.,
            Bai,Y. and Wang,S.
  TITLE     S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming
  JOURNAL   EMBO Rep 25 (1), 128-143 (2024)
   PUBMED   38177907
  REMARK    GeneRIF: S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming.
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Dyck,J.R., Gao,G., Widmer,J., Stapleton,D., Fernandez,C.S.,
            Kemp,B.E. and Witters,L.A.
  TITLE     Regulation of 5'-AMP-activated protein kinase activity by the
            noncatalytic beta and gamma subunits
  JOURNAL   J Biol Chem 271 (30), 17798-17803 (1996)
   PUBMED   8663446
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Gao,G., Fernandez,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
            Dyck,J.R., Kemp,B.E. and Witters,L.A.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J Biol Chem 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Stapleton,D., Mitchelhill,K.I., Gao,G., Widmer,J., Michell,B.J.,
            Teh,T., House,C.M., Fernandez,C.S., Cox,T., Witters,L.A. and
            Kemp,B.E.
  TITLE     Mammalian AMP-activated protein kinase subfamily
  JOURNAL   J Biol Chem 271 (2), 611-614 (1996)
   PUBMED   8557660
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Hofmann,B., Nishanian,P., Nguyen,T., Insixiengmay,P. and Fahey,J.L.
  TITLE     Human immunodeficiency virus proteins induce the inhibitory
            cAMP/protein kinase A pathway in normal lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6676-6680 (1993)
   PUBMED   7688126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK097606.1, BC000358.2 and
            BM667691.1.
            
            Summary: The protein encoded by this gene is a regulatory subunit
            of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer
            consisting of an alpha catalytic subunit, and non-catalytic beta
            and gamma subunits. AMPK is an important energy-sensing enzyme that
            monitors cellular energy status. In response to cellular metabolic
            stresses, AMPK is activated, and thus phosphorylates and
            inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy
            beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in
            regulating de novo biosynthesis of fatty acid and cholesterol. This
            subunit is one of the gamma regulatory subunits of AMPK.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (3) that is longer than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097606.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..340
                     /product="5'-AMP-activated protein kinase subunit gamma-1
                     isoform 3"
                     /note="AMPK gamma-1 chain; 5'-AMP-activated protein
                     kinase, gamma-1 subunit; AMPK gamma1; protein kinase,
                     AMP-activated, gamma 1 non-catalytic subunit"
                     /calculated_mol_wt=38402
     Region          38..183
                     /region_name="CBS_euAMPK_gamma-like_repeat1"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains found in AMP-activated
                     protein kinase gamma-like proteins, repeat 1; cd04618"
                     /db_xref="CDD:341388"
     Site            order(45,47..49,71..73,161,175,177,179..180,183)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341388"
     Region          45..127
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Site            order(71,94,98..99,102,139,161..163,179)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341388"
     Region          139..183
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Region          209..332
                     /region_name="CBS_euAMPK_gamma-like_repeat2"
                     /note="CBS pair domain found in 5'-AMP (adenosine
                     monophosphate)-activated protein kinase; cd04641"
                     /db_xref="CDD:341399"
     Site            order(210,212..214,236..238,308,321,323,325..326,329)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341399"
     Region          210..275
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     Site            order(236,249,253..254,257,286,308..310,325)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341399"
     Region          286..329
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     CDS             1..340
                     /gene="PRKAG1"
                     /gene_synonym="AMPKG"
                     /coded_by="NM_001206709.2:37..1059"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55825.1"
                     /db_xref="GeneID:5571"
                     /db_xref="HGNC:HGNC:9385"
                     /db_xref="MIM:602742"
ORIGIN      
        1 metvissdss pavenehpqe tpesnnsvyt sfmkshrcyd liptssklvv fdtslqvkka
       61 ffalvtngvr aaplwdskkq sfvvlralsc plgmltitdf inilhryyks alvqiyelee
      121 hkietwrevy lqdsfkplvc ispnaslfda vsslirnkih rlpvidpesg ntlyilthkr
      181 ilkflklfit efpkpefmsk sleelqigty aniamvrttt pvyvalgifv qhrvsalpvv
      241 dekgrvvdiy skfdvinlaa ektynnldvs vtkalqhrsh yfegvlkcyl hetletiinr
      301 lveaevhrlv vvdendvvkg ivslsdilqa lvltggekkp
//
LOCUS       NP_001505                316 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription initiation factor IIB [Homo sapiens].
ACCESSION   NP_001505
VERSION     NP_001505.1
DBSOURCE    REFSEQ: accession NM_001514.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Girault,V., Stukalov,A., Carter-Timofte,M.E., Hertzog,J., Verin,M.,
            Austen,K., Haas,D.A., Oubraham,L., Piras,A., Maidl,S., Ollinger,R.,
            Rad,R., Protzer,U., Kaufer,B.B., Lebbink,R.J., Rehwinkel,J.,
            Mogensen,T.H. and Pichlmair,A.
  TITLE     Multi-proteomic profiling of the varicella-zoster virus-host
            interface reveals host susceptibilities to severe infection
  JOURNAL   Nat Microbiol 10 (8), 2048-2072 (2025)
   PUBMED   40739040
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Santana,J.F., Collins,G.S., Parida,M., Luse,D.S. and Price,D.H.
  TITLE     Differential dependencies of human RNA polymerase II promoters on
            TBP, TAF1, TFIIB and XPB
  JOURNAL   Nucleic Acids Res 50 (16), 9127-9148 (2022)
   PUBMED   35947745
  REMARK    GeneRIF: Differential dependencies of human RNA polymerase II
            promoters on TBP, TAF1, TFIIB and XPB.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Cai,F., Chen,S., Yu,X., Zhang,J., Liang,W., Zhang,Y., Chen,Y.,
            Chen,S., Hong,Y., Yan,W., Wang,W., Zhang,J. and Wu,Q.
  TITLE     Transcription factor GTF2B regulates AIP protein expression in
            growth hormone-secreting pituitary adenomas and influences tumor
            phenotypes
  JOURNAL   Neuro Oncol 24 (6), 925-935 (2022)
   PUBMED   34932801
  REMARK    GeneRIF: Transcription factor GTF2B regulates AIP protein
            expression in growth hormone-secreting pituitary adenomas and
            influences tumor phenotypes.
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Ing,N.H., Beekman,J.M., Tsai,S.Y., Tsai,M.J. and O'Malley,B.W.
  TITLE     Members of the steroid hormone receptor superfamily interact with
            TFIIB (S300-II)
  JOURNAL   J Biol Chem 267 (25), 17617-17623 (1992)
   PUBMED   1517211
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Malik,S., Hisatake,K., Sumimoto,H., Horikoshi,M. and Roeder,R.G.
  TITLE     Sequence of general transcription factor TFIIB and relationships to
            other initiation factors
  JOURNAL   Proc Natl Acad Sci U S A 88 (21), 9553-9557 (1991)
   PUBMED   1946368
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Ha,I., Lane,W.S. and Reinberg,D.
  TITLE     Cloning of a human gene encoding the general transcription
            initiation factor IIB
  JOURNAL   Nature 352 (6337), 689-695 (1991)
   PUBMED   1876184
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445991.15.
            
            Summary: This gene encodes the general transcription factor IIB,
            one of the ubiquitous factors required for transcription initiation
            by RNA polymerase II. The protein localizes to the nucleus where it
            forms a complex (the DAB complex) with transcription factors IID
            and IIA. Transcription factor IIB serves as a bridge between IID,
            the factor which initially recognizes the promoter sequence, and
            RNA polymerase II. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK289822.1, BC020597.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370500.10/ ENSP00000359531.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.2"
     Protein         1..316
                     /product="transcription initiation factor IIB"
                     /EC_number="2.3.1.48"
                     /note="RNA polymerase II transcription factor IIB;
                     S300-II; general transcription factor TFIIB"
                     /calculated_mol_wt=34702
     Region          3..292
                     /region_name="SUA7"
                     /note="Transcription initiation factor TFIIIB, Brf1
                     subunit/Transcription initiation factor TFIIB
                     [Transcription]; COG1405"
                     /db_xref="CDD:441015"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00403.1)"
     Site            76
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00403.1)"
     Region          124..200
                     /region_name="Repetitive region"
                     /note="1; propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Region          189..193
                     /region_name="Core promoter DNA-binding.
                     /evidence=ECO:0000269|PubMed:10619841"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Region          218..294
                     /region_name="Repetitive region"
                     /note="2; propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:12931194; propagated from
                     UniProtKB/Swiss-Prot (Q00403.1)"
     Region          244..316
                     /region_name="Necessary for TATA box-bound TBP complex
                     formation. /evidence=ECO:0000269|PubMed:8515820,
                     ECO:0000269|PubMed:8516311"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Region          249..252
                     /region_name="Core promoter DNA-binding.
                     /evidence=ECO:0000269|PubMed:7675079"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     Region          283..286
                     /region_name="Core promoter DNA-binding.
                     /evidence=ECO:0000269|PubMed:10619841,
                     ECO:0000269|PubMed:7675079"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00403.1)"
     CDS             1..316
                     /gene="GTF2B"
                     /gene_synonym="TF2B; TFIIB"
                     /coded_by="NM_001514.6:69..1019"
                     /db_xref="CCDS:CCDS715.1"
                     /db_xref="GeneID:2959"
                     /db_xref="HGNC:HGNC:4648"
                     /db_xref="MIM:189963"
ORIGIN      
        1 mastsrldal prvtcpnhpd ailvedyrag dmicpecglv vgdrvidvgs ewrtfsndka
       61 tkdpsrvgds qnpllsdgdl stmigkgtga asfdefgnsk yqnrrtmsss drammnafke
      121 ittmadrinl prnivdrtnn lfkqvyeqks lkgrandaia saclyiacrq egvprtfkei
      181 cavsriskke igrcfklilk aletsvdlit tgdfmsrfcs nlclpkqvqm aathiarkav
      241 eldlvpgrsp isvaaaaiym asqasaekrt qkeigdiagv advtirqsyr liyprapdlf
      301 ptdfkfdtpv dklpql
//
LOCUS       NP_037383                121 aa            linear   PRI 20-NOV-2025
DEFINITION  tachykinin-3 isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_037383
VERSION     NP_037383.1
DBSOURCE    REFSEQ: accession NM_013251.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 121)
  AUTHORS   Sun,W., Yang,F., Zhang,H., Yuan,Q., Ling,S., Wang,Y., Lv,P., Li,Z.,
            Luo,Y., Liu,D., Yin,W., Shi,P., Xu,H.E. and Tian,C.
  TITLE     Structural insights into neurokinin 3 receptor activation by
            endogenous and analogue peptide agonists
  JOURNAL   Cell Discov 9 (1), 66 (2023)
   PUBMED   37391393
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 121)
  AUTHORS   Guo,F., Fernando,T., Zhu,X. and Shi,Y.
  TITLE     The overexpression of neurokinin B-neurokinin 3 receptor system
            exerts direct effects on the ovary under PCOS-like conditions to
            interfere with mitochondrial function
  JOURNAL   Am J Reprod Immunol 89 (3), e13663 (2023)
   PUBMED   36453600
  REMARK    GeneRIF: The overexpression of neurokinin B-neurokinin 3 receptor
            system exerts direct effects on the ovary under PCOS-like
            conditions to interfere with mitochondrial function.
REFERENCE   3  (residues 1 to 121)
  AUTHORS   Guzelkas,I., Orbak,Z., Doneray,H., Ozturk,N. and Sagsoz,N.
  TITLE     Serum kisspeptin, leptin, neuropeptide Y, and neurokinin B levels
            in adolescents with polycystic ovary syndrome
  JOURNAL   J Pediatr Endocrinol Metab 35 (4), 481-487 (2022)
   PUBMED   35170267
  REMARK    GeneRIF: Serum kisspeptin, leptin, neuropeptide Y, and neurokinin B
            levels in adolescents with polycystic ovary syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 121)
  AUTHORS   Atay,E., Kilinc,S., Ulfer,G., Yigitbasi,T., Cakici,C., Turan,M.,
            Ceran,O. and Atay,Z.
  TITLE     The role of makorin ring finger protein-3, kisspeptin, and
            neurokinin B in the physiology of minipuberty
  JOURNAL   J Pediatr Endocrinol Metab 34 (3), 325-332 (2021)
   PUBMED   33675211
  REMARK    GeneRIF: The role of makorin ring finger protein-3, kisspeptin, and
            neurokinin B in the physiology of minipuberty.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 121)
  AUTHORS   Grachev,P., Millar,R.P. and O'Byrne,K.T.
  TITLE     The role of neurokinin B signalling in reproductive
            neuroendocrinology
  JOURNAL   Neuroendocrinology 99 (1), 7-17 (2014)
   PUBMED   24356581
  REMARK    Review article
REFERENCE   6  (residues 1 to 121)
  AUTHORS   Page,N.M., Woods,R.J., Gardiner,S.M., Lomthaisong,K.,
            Gladwell,R.T., Butlin,D.J., Manyonda,I.T. and Lowry,P.J.
  TITLE     Excessive placental secretion of neurokinin B during the third
            trimester causes pre-eclampsia
  JOURNAL   Nature 405 (6788), 797-800 (2000)
   PUBMED   10866201
REFERENCE   7  (residues 1 to 121)
  AUTHORS   Tian,Y., Wu,L.H., Oxender,D.L. and Chung,F.Z.
  TITLE     The unpredicted high affinities of a large number of naturally
            occurring tachykinins for chimeric NK1/NK3 receptors suggest a role
            for an inhibitory domain in determining receptor specificity
  JOURNAL   J Biol Chem 271 (34), 20250-20257 (1996)
   PUBMED   8702757
REFERENCE   8  (residues 1 to 121)
  AUTHORS   Bhogal,N., Donnelly,D. and Findlay,J.B.
  TITLE     The ligand binding site of the neurokinin 2 receptor. Site-directed
            mutagenesis and identification of neurokinin A binding residues in
            the human neurokinin 2 receptor
  JOURNAL   J Biol Chem 269 (44), 27269-27274 (1994)
   PUBMED   7961636
REFERENCE   9  (residues 1 to 121)
  AUTHORS   Balasubramanian,R. and Crowley,W.F. Jr.
  TITLE     Isolated Gonadotropin-Releasing Hormone (GnRH) Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301509
REFERENCE   10 (residues 1 to 121)
  AUTHORS   Rance,N.E. and Young,W.S. 3rd.
  TITLE     Hypertrophy and increased gene expression of neurons containing
            neurokinin-B and substance-P messenger ribonucleic acids in the
            hypothalami of postmenopausal women
  JOURNAL   Endocrinology 128 (5), 2239-2247 (1991)
   PUBMED   1708331
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032145.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tachykinin family of
            secreted neuropeptides. The encoded preproprotein is
            proteolytically processed to generate the mature peptide, which is
            primarily expressed in the central and peripheral nervous systems
            and functions as a neurotransmitter. This peptide is the ligand for
            the neurokinin-3 receptor. This protein is also expressed in the
            outer syncytiotrophoblast of the placenta and may be associated
            with pregnancy-induced hypertension and pre-eclampsia. Mutations in
            this gene are associated with normosmic hypogonadotropic
            hypogonadism. Alternative splicing results in multiple transcript
            variants, at least one of which encodes an isoform that is
            proteolytically processed. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032145.2, SRR5189652.179869.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000458521.7/ ENSP00000404056.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..121
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..121
                     /product="tachykinin-3 isoform 1 preproprotein"
                     /note="neuromedin K; LncZBTB39-1:2; gamma tachykinin 3;
                     preprotachykinin B; neurokinin b"
                     /calculated_mol_wt=11645
     Region          1..54
                     /region_name="Neurokinin_B"
                     /note="Neurokinin B; pfam03823"
                     /db_xref="CDD:461065"
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UHF0.1)"
                     /calculated_mol_wt=1811
     mat_peptide     81..90
                     /product="Neurokinin-B. /id=PRO_0000033566"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHF0.1)"
                     /calculated_mol_wt=1211
     Site            90
                     /site_type="amidation"
                     /note="Methionine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9UHF0.1)"
     Region          93..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHF0.1)"
     CDS             1..121
                     /gene="TAC3"
                     /gene_synonym="HH10; LncZBTB39; NK3; NKB; NKNB; PRO1155;
                     ZNEUROK1"
                     /coded_by="NM_013251.4:149..514"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS8928.1"
                     /db_xref="GeneID:6866"
                     /db_xref="HGNC:HGNC:11521"
                     /db_xref="MIM:162330"
ORIGIN      
        1 mrimllftai lafslaqsfg avckepqeev vpgggrskrd pdlyqllqrl fkshsslegl
       61 lkalsqastd pkestspekr dmhdffvglm gkrsvqpdsp tdvnqenvps fgilkyppra
      121 e
//
LOCUS       NP_001354643             891 aa            linear   PRI 20-NOV-2025
DEFINITION  la-related protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001354643
VERSION     NP_001354643.1
DBSOURCE    REFSEQ: accession NM_001367714.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 891)
  AUTHORS   Ma,J., Dong,D., Qi,H., Li,J., Yu,H., Hu,X., Sun,L. and Shen,L.
  TITLE     LARP1, an RNA-binding protein, participates in ovarian cancer cell
            survival by regulating mitochondrial oxidative phosphorylation in
            response to the influence of the PI3K/mTOR pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (8), 167453 (2024)
   PUBMED   39111634
  REMARK    GeneRIF: LARP1, an RNA-binding protein, participates in ovarian
            cancer cell survival by regulating mitochondrial oxidative
            phosphorylation in response to the influence of the PI3K/mTOR
            pathway.
REFERENCE   2  (residues 1 to 891)
  AUTHORS   Chettle,J., Louie,R.J., Larner,O., Best,R., Chen,K., Morris,J.,
            Dedeic,Z., Childers,A., Rogers,R.C., DuPont,B.R., Skinner,C.,
            Kury,S., Uguen,K., Planes,M., Monteil,D., Li,M., Eliyahu,A.,
            Greenbaum,L., Mor,N., Besnard,T., Isidor,B., Cogne,B., Blesson,A.,
            Comi,A., Wentzensen,I.M., Vuocolo,B., Lalani,S.R., Sierra,R.,
            Berry,L., Carter,K., Sanders,S.J. and Blagden,S.P.
  TITLE     LARP1 haploinsufficiency is associated with an autosomal dominant
            neurodevelopmental disorder
  JOURNAL   HGG Adv 5 (4), 100345 (2024)
   PUBMED   39182167
  REMARK    GeneRIF: LARP1 haploinsufficiency is associated with an autosomal
            dominant neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 891)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 891)
  AUTHORS   Smith,B.C. and Silvers,R.
  TITLE     1H, 13C, and 15N resonance assignments of the La Motif of the human
            La-related protein 1
  JOURNAL   Biomol NMR Assign 18 (1), 111-118 (2024)
   PUBMED   38691336
  REMARK    GeneRIF: [1]H, [13]C, and [15]N resonance assignments of the La
            Motif of the human La-related protein 1.
REFERENCE   5  (residues 1 to 891)
  AUTHORS   Kozlov,G., Jiang,J., Rutherford,T., Noronha,A.M., Wilds,C.J. and
            Gehring,K.
  TITLE     Enhanced binding of guanylated poly(A) RNA by the LaM domain of
            LARP1
  JOURNAL   RNA Biol 21 (1), 7-16 (2024)
   PUBMED   39016322
  REMARK    GeneRIF: Enhanced binding of guanylated poly(A) RNA by the LaM
            domain of LARP1.
REFERENCE   6  (residues 1 to 891)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 891)
  AUTHORS   Burrows,C., Abd Latip,N., Lam,S.J., Carpenter,L., Sawicka,K.,
            Tzolovsky,G., Gabra,H., Bushell,M., Glover,D.M., Willis,A.E. and
            Blagden,S.P.
  TITLE     The RNA binding protein Larp1 regulates cell division, apoptosis
            and cell migration
  JOURNAL   Nucleic Acids Res 38 (16), 5542-5553 (2010)
   PUBMED   20430826
REFERENCE   8  (residues 1 to 891)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 891)
  AUTHORS   Horke,S., Reumann,K., Schweizer,M., Will,H. and Heise,T.
  TITLE     Nuclear trafficking of La protein depends on a newly identified
            nucleolar localization signal and the ability to bind RNA
  JOURNAL   J Biol Chem 279 (25), 26563-26570 (2004)
   PUBMED   15060081
  REMARK    GeneRIF: Nuclear trafficking of La protein depends on a newly
            identified nucleolar localization signal and the ability to bind
            RNA
REFERENCE   10 (residues 1 to 891)
  AUTHORS   Chauvet,S., Maurel-Zaffran,C., Miassod,R., Jullien,N., Pradel,J.
            and Aragnol,D.
  TITLE     dlarp, a new candidate Hox target in Drosophila whose orthologue in
            mouse is expressed at sites of epithelium/mesenchymal interactions
  JOURNAL   Dev Dyn 218 (3), 401-413 (2000)
   PUBMED   10878606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008379.7 and AC112169.2.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1867096.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2155751
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..891
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..891
                     /product="la-related protein 1 isoform 3"
                     /note="la-related protein 1; La ribonucleoprotein domain
                     family member 1"
                     /calculated_mol_wt=102304
     Region          199..271
                     /region_name="LARP_1"
                     /note="La RNA-binding domain of La-related protein 1;
                     cd08037"
                     /db_xref="CDD:153406"
     Region          <202..350
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Site            order(205,208..209,214,217..218,220,239..241)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153406"
     Region          680..720
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          721..759
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     CDS             1..891
                     /gene="LARP1"
                     /gene_synonym="Lar1; LARP; Lhp1"
                     /coded_by="NM_001367714.1:356..3031"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS93807.1"
                     /db_xref="GeneID:23367"
                     /db_xref="HGNC:HGNC:29531"
                     /db_xref="MIM:612059"
ORIGIN      
        1 mkeqekgegs dskespktks desgeekngd edcqrggqkk kgnkhkwvpl qidmkpevpr
       61 eklasrptrp peprhipanr geikgsesat yvpvapptpa wqpeikpepa whdqdetssv
      121 ksdgaggara sfrgrgrgrg rgrgrgrggt rthfdyqfgy rkfdgvegpr tpkymnnity
      181 yfdnvsstel ysvdqellkd yikrqieyyf svdnlerdff lrrkmdadgf lpitliasfh
      241 rvqalttdis lifaalkdsk vveivdekvr rreepekwpl ppivdysqtd fsqllncpef
      301 vprqhyqket esapgsprav tpvptkteev snlktlpkgl saslpdldse nwievkkrpr
      361 psparpkkse esrfshltsl pqqlpsqqlm skdqdeqeel dflfdeemeq mdgrkntfta
      421 wsdeesdyei ddrdvnkili vtqtphymrr hpggdrtgnh tsrakmsael akvindglfy
      481 yeqdlwaekf epeysqikqe venfkkvnmi sreqfdtltp eppvdpnqev ppgpprfqqv
      541 ptdalanklf gapepstiar slpttvpesp nyrntrtprt prtpqlkdss qtsrfypvvk
      601 egrtldakmp rkrktrhssn ppleshvgwv mdsrehrprt asissspseg tptvgsygct
      661 pqslpkfqhp shellkengf tqhvyhkyrr rclnerkrlg igqsqemntl frfwsfflrd
      721 hfnkkmyeef kqlaledake gyrygleclf ryysyglekk frldifkdfq eetvkdyeag
      781 qlyglekfwa flkyskaknl didpklqeyl gkfrrledfr vdppmgeegn hkrhsvvagg
      841 gggegrkrcp sqsssrpaam isqpptpptg qpvredakwt sqhsntqtlg k
//
LOCUS       NP_001034937             234 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase GPX4 isoform C
            [Homo sapiens].
ACCESSION   NP_001034937
VERSION     NP_001034937.1
DBSOURCE    REFSEQ: accession NM_001039848.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Ye,H., Ding,X., Lv,X., Du,Y., Guo,R., Qiu,J., Li,R. and Cao,L.
  TITLE     KLF14 directly downregulates the expression of GPX4 to exert
            antitumor effects by promoting ferroptosis in cervical cancer
  JOURNAL   J Transl Med 22 (1), 923 (2024)
   PUBMED   39390559
  REMARK    GeneRIF: KLF14 directly downregulates the expression of GPX4 to
            exert antitumor effects by promoting ferroptosis in cervical
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 234)
  AUTHORS   Sok,S.P.M., Pipkin,K., Popescu,N.I., Reidy,M., Li,B., Van
            Remmen,H., Kinter,M., Sun,X.H., Fan,Z. and Zhao,M.
  TITLE     Gpx4 Regulates Invariant NKT Cell Homeostasis and Function by
            Preventing Lipid Peroxidation and Ferroptosis
  JOURNAL   J Immunol 213 (7), 941-951 (2024)
   PUBMED   39158281
  REMARK    GeneRIF: Gpx4 Regulates Invariant NKT Cell Homeostasis and Function
            by Preventing Lipid Peroxidation and Ferroptosis.
REFERENCE   4  (residues 1 to 234)
  AUTHORS   Li,X., He,J., Gao,X., Zheng,G., Chen,C., Chen,Y., Xing,Z., Wang,T.,
            Tang,J., Guo,Y. and He,Y.
  TITLE     GPX4 restricts ferroptosis of NKp46+ILC3s to control intestinal
            inflammation
  JOURNAL   Cell Death Dis 15 (9), 687 (2024)
   PUBMED   39300068
  REMARK    GeneRIF: GPX4 restricts ferroptosis of NKp46[+]ILC3s to control
            intestinal inflammation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 234)
  AUTHORS   Sneddon,A.A., Wu,H.C., Farquharson,A., Grant,I., Arthur,J.R.,
            Rotondo,D., Choe,S.N. and Wahle,K.W.
  TITLE     Regulation of selenoprotein GPx4 expression and activity in human
            endothelial cells by fatty acids, cytokines and antioxidants
  JOURNAL   Atherosclerosis 171 (1), 57-65 (2003)
   PUBMED   14642406
  REMARK    GeneRIF: lipids, cytokines and antioxidants modulate GPx4 in a
            complex manner that in the presence of adequate selenium, may
            favour protection against potentially proatherogenic processes.
REFERENCE   6  (residues 1 to 234)
  AUTHORS   Roveri,A., Flohe,L., Maiorino,M. and Ursini,F.
  TITLE     Phospholipid-hydroperoxide glutathione peroxidase in sperm
  JOURNAL   Methods Enzymol 347, 208-212 (2002)
   PUBMED   11898409
  REMARK    GeneRIF: Glutathione peroxidase is a moonlighting protein that
            functions both as a peroxidase as well as a structural protein in
            mature spermatozoa.
REFERENCE   7  (residues 1 to 234)
  AUTHORS   Kelner,M.J. and Montoya,M.A.
  TITLE     Structural organization of the human selenium-dependent
            phospholipid hydroperoxide glutathione peroxidase gene (GPX4):
            chromosomal localization to 19p13.3
  JOURNAL   Biochem Biophys Res Commun 249 (1), 53-55 (1998)
   PUBMED   9705830
REFERENCE   8  (residues 1 to 234)
  AUTHORS   Opalenik,S.R., Ding,Q., Mallery,S.R. and Thompson,J.A.
  TITLE     Glutathione depletion associated with the HIV-1 TAT protein
            mediates the extracellular appearance of acidic fibroblast growth
            factor
  JOURNAL   Arch Biochem Biophys 351 (1), 17-26 (1998)
   PUBMED   9501919
REFERENCE   9  (residues 1 to 234)
  AUTHORS   Esworthy,R.S., Doan,K., Doroshow,J.H. and Chu,F.F.
  TITLE     Cloning and sequencing of the cDNA encoding a human testis
            phospholipid hydroperoxide glutathione peroxidase
  JOURNAL   Gene 144 (2), 317-318 (1994)
   PUBMED   8039723
REFERENCE   10 (residues 1 to 234)
  AUTHORS   Chu,F.F.
  TITLE     The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to
            chromosomes 14, 5, and 19, respectively
  JOURNAL   Cytogenet Cell Genet 66 (2), 96-98 (1994)
   PUBMED   8287691
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM764133.1, BF740029.1 and
            BC021567.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Mutations in this gene are associated with
            Sedaghatian type of spondylometaphyseal dysplasia (SMDS). This
            isozyme is also a selenoprotein, containing the rare amino acid
            selenocysteine (Sec) at its active site. Sec is encoded by the UGA
            codon, which normally signals translation termination. The 3' UTRs
            of selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. Transcript variants resulting from alternative
            splicing or use of alternate promoters have been described to
            encode isoforms with different subcellular localization. [provided
            by RefSeq, Dec 2018].
            
            Transcript Variant: This variant (3) contains an alternate 5'
            terminal exon compared to variant 1. The resulting isoform (C) has
            a longer and a distinct N-terminus compared to isoform A. A similar
            isoform in rat (snGPx) has been reported to be localized in the
            sperm nucleus (PMID:11344099).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2265810.1, CF127510.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            multifunctional gene product(s)    :: PMID: 11898409
            protein contains selenocysteine    :: PMID: 8039723
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..234
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase GPX4 isoform C"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxidase; sperm nucleus
                     glutathione peroxidase; phospholipid hydroperoxide
                     glutathione peroxidase, mitochondrial; epididymis
                     secretory sperm binding protein; selenoprotein GPX4;
                     phospholipid hydroperoxide glutathione peroxidase GPX4"
                     /calculated_mol_wt=26967
     Region          77..230
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(110,145,200)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            110
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(144,147,149,152,155,159)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..234
                     /gene="GPX4"
                     /gene_synonym="GPx-4; GSHPx-4; MCSP; PHGPx; SMDS; snGPx;
                     snPHGPx"
                     /coded_by="NM_001039848.4:86..790"
                     /note="UGA stop codon recoded as selenocysteine; isoform C
                     is encoded by transcript variant 3"
                     /db_xref="GeneID:2879"
                     /db_xref="HGNC:HGNC:4556"
                     /db_xref="MIM:138322"
ORIGIN      
        1 mgragagspg rrrqrcqsrg rrrpraprrr kapacrrrra rrrrkkpcpr slrpeihecp
       61 ksqdpcasrd dwrcarsmhe fsakdidghm vnldkyrgfv civtnvasqu gktevnytql
      121 vdlharyaec glrilafpcn qfgkqepgsn eeikefaagy nvkfdmfski cvngddahpl
      181 wkwmkiqpkg kgilgnaikw nftkflidkn gcvvkrygpm eeplviekdl phyf
//
LOCUS       NP_001239570             475 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional prefoldin RPB5 interactor 1 isoform c [Homo
            sapiens].
ACCESSION   NP_001239570
VERSION     NP_001239570.1
DBSOURCE    REFSEQ: accession NM_001252641.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Xu,Y., Ji,Y., Li,X., Ding,J., Chen,L., Huang,Y. and Wei,W.
  TITLE     URI1 suppresses irradiation-induced reactive oxygen species (ROS)
            by activating autophagy in hepatocellular carcinoma cells
  JOURNAL   Int J Biol Sci 17 (12), 3091-3103 (2021)
   PUBMED   34421352
  REMARK    GeneRIF: URI1 suppresses irradiation-induced reactive oxygen
            species (ROS) by activating autophagy in hepatocellular carcinoma
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Yang,H., Gu,J., Zheng,Q., Li,M., Lian,X., Miao,J., Jiang,J. and
            Wei,W.
  TITLE     RPB5-mediating protein is required for the proliferation of
            hepatocellular carcinoma cells
  JOURNAL   J Biol Chem 286 (13), 11865-11874 (2011)
   PUBMED   21310960
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Theurillat,J.P., Metzler,S.C., Henzi,N., Djouder,N., Helbling,M.,
            Zimmermann,A.K., Jacob,F., Soltermann,A., Caduff,R.,
            Heinzelmann-Schwarz,V., Moch,H. and Krek,W.
  TITLE     URI is an oncogene amplified in ovarian cancer cells and is
            required for their survival
  JOURNAL   Cancer Cell 19 (3), 317-332 (2011)
   PUBMED   21397856
  REMARK    GeneRIF: Data show that URI is an 'addicting' oncogene selectively
            required for the survival of ovarian cancer cells with increased
            URI copy number.
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Wei,W., Gu,J.X., Zhu,C.Q., Sun,F.Y., Dorjsuren,D., Lin,Y. and
            Murakami,S.
  TITLE     Interaction with general transcription factor IIF (TFIIF) is
            required for the suppression of activated transcription by
            RPB5-mediating protein (RMP)
  JOURNAL   Cell Res 13 (2), 111-120 (2003)
   PUBMED   12737519
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Liu,L. and McKeehan,W.L.
  TITLE     Sequence analysis of LRPPRC and its SEC1 domain interaction
            partners suggests roles in cytoskeletal organization, vesicular
            trafficking, nucleocytosolic shuttling, and chromosome activity
  JOURNAL   Genomics 79 (1), 124-136 (2002)
   PUBMED   11827465
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Van Leuven,F., Torrekens,S., Moechars,D., Hilliker,C., Buellens,M.,
            Bollen,M. and Delabie,J.
  TITLE     Molecular cloning of a gene on chromosome 19q12 coding for a novel
            intracellular protein: analysis of expression in human and mouse
            tissues and in human tumor cells, particularly Reed-Sternberg cells
            in Hodgkin disease
  JOURNAL   Genomics 54 (3), 511-520 (1998)
   PUBMED   9878255
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Dorjsuren,D., Lin,Y., Wei,W., Yamashita,T., Nomura,T., Hayashi,N.
            and Murakami,S.
  TITLE     RMP, a novel RNA polymerase II subunit 5-interacting protein,
            counteracts transactivation by hepatitis B virus X protein
  JOURNAL   Mol Cell Biol 18 (12), 7546-7555 (1998)
   PUBMED   9819440
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC026184.2, AW954529.1,
            BG742069.1, AW003989.1 and AA678820.1.
            
            Summary: This gene encodes member of the prefoldin family of
            molecular chaperones. The encoded protein functions as a
            scaffolding protein and plays roles in ubiquitination and
            transcription, in part though interactions with the RNA polymerase
            II subunit RPB5. This gene may play a role in multiple malignancies
            including ovarian cancer and hepatocellular carcinoma.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the long arm of chromosome 22. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (3) differs in the 5' and 3' UTRs
            and initiates translation at an alternate start codon, compared to
            variant 1. The encoded isoform (c) is shorter and has distinct N-
            and C-termini, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026184.2, SRR5189667.168001.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12"
     Protein         1..475
                     /product="unconventional prefoldin RPB5 interactor 1
                     isoform c"
                     /note="RPB5-mediating protein; RNA polymerase II subunit
                     5-mediating protein; protein phosphatase 1, regulatory
                     subunit 19; unconventional prefoldin RPB5 interactor 1"
                     /calculated_mol_wt=53316
     Region          14..135
                     /region_name="Prefoldin_URI1"
                     /note="RNA polymerase II subunit 5-mediating protein
                     homolog; cd23159"
                     /db_xref="CDD:467475"
     Region          14..50
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467475"
     Site            order(39,42..43,46..47,49..50,56..63,65..74,77..81,85..90,
                     99)
                     /site_type="other"
                     /note="putative prefoldin oligomer interface [polypeptide
                     binding]"
                     /db_xref="CDD:467475"
     Region          93..133
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467475"
     CDS             1..475
                     /gene="URI1"
                     /gene_synonym="C19orf2; NNX3; PPP1R19; RMP; URI"
                     /coded_by="NM_001252641.2:36..1463"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58658.1"
                     /db_xref="GeneID:8725"
                     /db_xref="HGNC:HGNC:13236"
                     /db_xref="MIM:603494"
ORIGIN      
        1 mttwsslqgs hvskralaya lvvtncqeri qhwkkvdndy nalrerlstl pdklsynimv
       61 pfgpfafmpg klvhtnevtv llgdnwfakc sakqavglve hrkehvrkti ddlkkvmknf
      121 esrveftedl qkmsdaagdi vdireeikcd fefkakhria hkphskpkts difeadiand
      181 vkskdlladk elwarleele rqeellgeld skpdtviang edttsseeek edrntnvnam
      241 hqvtdshtpc hkdvassepf sgqvnsqlnc svngsssyhs dddddddddd dddniddddg
      301 dndhealgvg dnsiptiyfs htvepkrvri ntgknttlkf sekkeeakrk rknstgsghs
      361 aqelptirtp adiyrafvdv vngeyvprks ilksrsrens vcsdtsessa aefddrrgvl
      421 rsisceeatc sdtsesilee epqenqkkll plsvtpevlr lvgysrnlap lnvil
//
LOCUS       NP_001308657             426 aa            linear   PRI 20-NOV-2025
DEFINITION  serine protease HTRA2, mitochondrial isoform 4 preproprotein [Homo
            sapiens].
ACCESSION   NP_001308657 XP_005264323
VERSION     NP_001308657.1
DBSOURCE    REFSEQ: accession NM_001321728.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Aspholm,E.E., Lidman,J. and Burmann,B.M.
  TITLE     Structural basis of substrate recognition and allosteric activation
            of the proapoptotic mitochondrial HtrA2 protease
  JOURNAL   Nat Commun 15 (1), 4592 (2024)
   PUBMED   38816423
  REMARK    GeneRIF: Structural basis of substrate recognition and allosteric
            activation of the proapoptotic mitochondrial HtrA2 protease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Bi,P.Y., Killackey,S.A., Schweizer,L., Arnoult,D., Philpott,D.J.
            and Girardin,S.E.
  TITLE     Cytosolic retention of HtrA2 during mitochondrial protein import
            stress triggers the DELE1-HRI pathway
  JOURNAL   Commun Biol 7 (1), 391 (2024)
   PUBMED   38555279
  REMARK    GeneRIF: Cytosolic retention of HtrA2 during mitochondrial protein
            import stress triggers the DELE1-HRI pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Suzuki,Y., Takahashi-Niki,K., Akagi,T., Hashikawa,T. and
            Takahashi,R.
  TITLE     Mitochondrial protease Omi/HtrA2 enhances caspase activation
            through multiple pathways
  JOURNAL   Cell Death Differ 11 (2), 208-216 (2004)
   PUBMED   14605674
  REMARK    GeneRIF: protease activity of Omi/HtrA2 promotes caspase activation
            through multiple pathways
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Faccio,L., Fusco,C., Viel,A. and Zervos,A.S.
  TITLE     Tissue-specific splicing of Omi stress-regulated endoprotease leads
            to an inactive protease with a modified PDZ motif
  JOURNAL   Genomics 68 (3), 343-347 (2000)
   PUBMED   10995577
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Gray,C.W., Ward,R.V., Karran,E., Turconi,S., Rowles,A.,
            Viglienghi,D., Southan,C., Barton,A., Fantom,K.G., West,A.,
            Savopoulos,J., Hassan,N.J., Clinkenbeard,H., Hanning,C.,
            Amegadzie,B., Davis,J.B., Dingwall,C., Livi,G.P. and Creasy,C.L.
  TITLE     Characterization of human HtrA2, a novel serine protease involved
            in the mammalian cellular stress response
  JOURNAL   Eur J Biochem 267 (18), 5699-5710 (2000)
   PUBMED   10971580
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Savopoulos,J.W., Carter,P.S., Turconi,S., Pettman,G.R.,
            Karran,E.H., Gray,C.W., Ward,R.V., Jenkins,O. and Creasy,C.L.
  TITLE     Expression, purification, and functional analysis of the human
            serine protease HtrA2
  JOURNAL   Protein Expr Purif 19 (2), 227-234 (2000)
   PUBMED   10873535
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Faccio,L., Fusco,C., Chen,A., Martinotti,S., Bonventre,J.V. and
            Zervos,A.S.
  TITLE     Characterization of a novel human serine protease that has
            extensive homology to bacterial heat shock endoprotease HtrA and is
            regulated by kidney ischemia
  JOURNAL   J Biol Chem 275 (4), 2581-2588 (2000)
   PUBMED   10644717
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Morris,H. and Lim,S.Y.
  TITLE     Monogenic Parkinson Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301402
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005041.2.
            
            On Mar 30, 2016 this sequence version replaced XP_005264323.1.
            
            Summary: This gene encodes a serine protease. The protein has been
            localized in the endoplasmic reticulum and interacts with an
            alternatively spliced form of mitogen-activated protein kinase 14.
            The protein has also been localized to the mitochondria with
            release to the cytosol following apoptotic stimulus. The protein is
            thought to induce apoptosis by binding the apoptosis inhibitory
            protein baculoviral IAP repeat-containing 4. Nuclear localization
            of this protein has also been observed. Alternate splicing of this
            gene results in multiple transcript variants encoding different
            isoforms. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225932.1, SRR1163658.359708.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..426
                     /product="serine protease HTRA2, mitochondrial isoform 4
                     preproprotein"
                     /EC_number="3.4.21.108"
                     /note="protease, serine, 25; HtrA-like serine protease;
                     high temperature requirement protein A2; Omi
                     stress-regulated endoprotease; serine protease HTRA2,
                     mitochondrial; serine protease 25; serine proteinase OMI;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=41915
     transit_peptide 1..31
                     /calculated_mol_wt=3460
     proprotein      32..426
                     /product="serine protease HTRA2, mitochondrial isoform 4
                     proprotein"
                     /calculated_mol_wt=41915
     mat_peptide     134..426
                     /product="serine protease HTRA2, mitochondrial isoform 4"
                     /calculated_mol_wt=31497
     Region          182..423
                     /region_name="DegQ"
                     /note="Periplasmic serine protease, S1-C subfamily,
                     contain C-terminal PDZ domain [Posttranslational
                     modification, protein turnover, chaperones]; COG0265"
                     /db_xref="CDD:440035"
     CDS             1..426
                     /gene="HTRA2"
                     /gene_synonym="MGCA8; OMI; PARK13; PRSS25"
                     /coded_by="NM_001321728.1:603..1883"
                     /note="isoform 4 preproprotein is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS92786.1"
                     /db_xref="GeneID:27429"
                     /db_xref="HGNC:HGNC:14348"
                     /db_xref="MIM:606441"
ORIGIN      
        1 maapragrga gwslrawral ggirwgrrpr ltpdlrallt sgtsdprarv tygtpslwar
       61 lsvgvtepra cltsgtpgpr aqltavtpdt rtreasensg trsrawlava lgaggavlll
      121 lwgggrgppa vlaavpsppp asprsqynfi advvektapa vvyieildrh pflgrevpis
      181 ngsgfvvaad glivtnahvv adrrrvrvrl lsgdtyeavv tavdpvadia tlriqtkepl
      241 ptlplgrsad vrqgefvvam gspfalqnti tsgivssaqr pardlglpqt nveyiqtdaa
      301 idfgnsggpl vnldgevigv ntmkvtagis faipsdrlre flhrgekkns ssgisgsqrr
      361 yigvmmltls praglrpgdv ilaigeqmvq naedvyeavr tqsqlavqir rgretltlyv
      421 tpevte
//
LOCUS       NP_005828                140 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p20 [Homo sapiens].
ACCESSION   NP_005828
VERSION     NP_005828.2
DBSOURCE    REFSEQ: accession NM_005837.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Huang,Y., Zheng,Y., Yao,L., Qiao,F., Hou,Y., Hu,X., Li,D. and
            Shao,Z.
  TITLE     RNA binding protein POP7 regulates ILF3 mRNA stability and
            expression to promote breast cancer progression
  JOURNAL   Cancer Sci 113 (11), 3801-3813 (2022)
   PUBMED   35579257
  REMARK    GeneRIF: RNA binding protein POP7 regulates ILF3 mRNA stability and
            expression to promote breast cancer progression.
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Welting,T.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Mutual interactions between subunits of the human RNase MRP
            ribonucleoprotein complex
  JOURNAL   Nucleic Acids Res 32 (7), 2138-2146 (2004)
   PUBMED   15096576
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Hua,Y. and Zhou,J.
  TITLE     Rpp20 interacts with SMN and is re-distributed into SMN granules in
            response to stress
  JOURNAL   Biochem Biophys Res Commun 314 (1), 268-276 (2004)
   PUBMED   14715275
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Jiang,T. and Altman,S.
  TITLE     Protein-protein interactions with subunits of human nuclear RNase P
  JOURNAL   Proc Natl Acad Sci U S A 98 (3), 920-925 (2001)
   PUBMED   11158571
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Stolc,V., Katz,A. and Altman,S.
  TITLE     Rpp2, an essential protein subunit of nuclear RNase P, is required
            for processing of precursor tRNAs and 35S precursor rRNA in
            Saccharomyces cerevisiae
  JOURNAL   Proc Natl Acad Sci U S A 95 (12), 6716-6721 (1998)
   PUBMED   9618478
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Jarrous,N., Eder,P.S., Guerrier-Takada,C., Hoog,C. and Altman,S.
  TITLE     Autoantigenic properties of some protein subunits of catalytically
            active complexes of human ribonuclease P
  JOURNAL   RNA 4 (4), 407-417 (1998)
   PUBMED   9630247
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI666854.1 and BC001430.2.
            
            On Jul 25, 2007 this sequence version replaced NP_005828.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.137178.1, CD048511.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000303151.5/ ENSP00000304353.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..140
                     /product="ribonuclease P protein subunit p20"
                     /EC_number="3.1.26.5"
                     /note="POP7 (processing of precursor, S. cerevisiae)
                     homolog; hPOP7; RNaseP protein p20; ribonucleases P/MRP
                     protein subunit POP7 homolog; processing of precursor 7,
                     ribonuclease P subunit; processing of precursor 7,
                     ribonuclease P/MRP subunit; POP7 homolog, ribonuclease
                     P/MRP subunit"
                     /calculated_mol_wt=15520
     Region          33..133
                     /region_name="Rpp20"
                     /note="Rpp20 subunit of nuclear RNase MRP and P;
                     pfam12328"
                     /db_xref="CDD:372048"
     CDS             1..140
                     /gene="POP7"
                     /gene_synonym="0610037N12Rik; RPP2; RPP20"
                     /coded_by="NM_005837.3:195..617"
                     /db_xref="CCDS:CCDS5704.1"
                     /db_xref="GeneID:10248"
                     /db_xref="HGNC:HGNC:19949"
                     /db_xref="MIM:606113"
ORIGIN      
        1 maenreprga veaeldpvey tlrkrlpsrl prrpndiyvn mktdfkaqla rcqklldgga
       61 rgqnacseiy ihglglainr ainialqlqa gsfgslqvaa ntstvelvde lepetdtrep
      121 ltrirnnsai hirvfrvtpk
//
LOCUS       NP_001354252             434 aa            linear   PRI 20-NOV-2025
DEFINITION  CCA tRNA nucleotidyltransferase 1, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_001354252 XP_011532078
VERSION     NP_001354252.1
DBSOURCE    REFSEQ: accession NM_001367323.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Meynier,V., Hardwick,S.W., Catala,M., Roske,J.J., Oerum,S.,
            Chirgadze,D.Y., Barraud,P., Yue,W.W., Luisi,B.F. and Tisne,C.
  TITLE     Structural basis for human mitochondrial tRNA maturation
  JOURNAL   Nat Commun 15 (1), 4683 (2024)
   PUBMED   38824131
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Fatica,T., Naas,T., Liwak,U., Slaa,H., Souaid,M., Frangione,B.,
            Kattini,R., Gaudreau-Lapierre,A., Trinkle-Mulcahy,L.,
            Chakraborty,P. and Holcik,M.
  TITLE     TRNT-1 Deficiency Is Associated with Loss of tRNA Integrity and
            Imbalance of Distinct Proteins
  JOURNAL   Genes (Basel) 14 (5), 1043 (2023)
   PUBMED   37239403
  REMARK    GeneRIF: TRNT-1 Deficiency Is Associated with Loss of tRNA
            Integrity and Imbalance of Distinct Proteins.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Seki,M., Komuro,A., Ishikawa,T., Takahashi,M. and Nashimoto,M.
  TITLE     Genes for tRNA recycling are upregulated in response to infection
            with Theiler's mouse encephalitis virus
  JOURNAL   Biochem Biophys Res Commun 587, 63-68 (2022)
   PUBMED   34864548
  REMARK    GeneRIF: Genes for tRNA recycling are upregulated in response to
            infection with Theiler's mouse encephalitis virus.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Odom,J., Amin,H., Gijavanekar,C., Elsea,S.H., Kralik,S., Chinen,J.,
            Lin,Y., Yates,A.M.M., Mizerik,E., Potocki,L. and Scaglia,F.
  TITLE     A phenotypic expansion of TRNT1 associated sideroblastic anemia
            with immunodeficiency, fevers, and developmental delay
  JOURNAL   Am J Med Genet A 188 (1), 259-268 (2022)
   PUBMED   34510712
  REMARK    GeneRIF: A phenotypic expansion of TRNT1 associated sideroblastic
            anemia with immunodeficiency, fevers, and developmental delay.
            Review article
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Augustin,M.A., Reichert,A.S., Betat,H., Huber,R., Morl,M. and
            Steegborn,C.
  TITLE     Crystal structure of the human CCA-adding enzyme: insights into
            template-independent polymerization
  JOURNAL   J Mol Biol 328 (5), 985-994 (2003)
   PUBMED   12729736
  REMARK    GeneRIF: The crystal structure reveals a four domain architecture
            with a cluster of conserved residues forming a positively charged
            cleft between the first two domains.
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Nagaike,T., Suzuki,T., Tomari,Y., Takemoto-Hori,C., Negayama,F.,
            Watanabe,K. and Ueda,T.
  TITLE     Identification and characterization of mammalian mitochondrial tRNA
            nucleotidyltransferases
  JOURNAL   J Biol Chem 276 (43), 40041-40049 (2001)
   PUBMED   11504732
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Reichert,A.S., Thurlow,D.L. and Morl,M.
  TITLE     A eubacterial origin for the human tRNA nucleotidyltransferase?
  JOURNAL   Biol Chem 382 (10), 1431-1438 (2001)
   PUBMED   11727826
  REMARK    GeneRIF: human gene transcript CGI-47 (#AF151805) was cloned and
            encodes a bona fide CCA-adding enzyme and not a poly(A) polymerase.
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024060.6.
            
            On Nov 21, 2018 this sequence version replaced XP_011532078.1.
            
            Summary: The protein encoded by this gene is a CCA-adding enzyme
            which belongs to the tRNA nucleotidyltransferase/poly(A) polymerase
            family. This essential enzyme functions by catalyzing the addition
            of the conserved nucleotide triplet CCA to the 3' terminus of tRNA
            molecules. Mutations in this gene result in sideroblastic anemia
            with B-cell immunodeficiency, periodic fevers, and developmental
            delay. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.212232.1,
                                           SRR1803614.163649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.2"
     Protein         1..434
                     /product="CCA tRNA nucleotidyltransferase 1, mitochondrial
                     isoform 1"
                     /EC_number="2.7.7.72"
                     /note="mitochondrial CCA-adding
                     tRNA-nucleotidyltransferase; tRNA nucleotidyl transferase,
                     CCA-adding, 1; tRNA-nucleotidyltransferase 1,
                     mitochondrial; CCA tRNA nucleotidyltransferase 1,
                     mitochondrial; mt CCA-adding enzyme; mt tRNA
                     CCA-diphosphorylase; mt tRNA adenylyltransferase; mt tRNA
                     CCA-pyrophosphorylase; tRNA CCA nucleotidyl transferase 1;
                     ATP(CTP):tRNA nucleotidyltransferase"
                     /calculated_mol_wt=44922
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=5224
     mat_peptide     42..434
                     /product="CCA tRNA nucleotidyltransferase 1,
                     mitochondrial. /id=PRO_0000004782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=44922
     Region          43..428
                     /region_name="PcnB"
                     /note="tRNA nucleotidyltransferase/poly(A) polymerase
                     [Translation, ribosomal structure and biogenesis];
                     COG0617"
                     /db_xref="CDD:440382"
     Site            152
                     /site_type="other"
                     /note="May assist in discriminating ATP from CTP.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB1; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            193
                     /site_type="other"
                     /note="Involved in nucleotide selection.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            402
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     CDS             1..434
                     /gene="TRNT1"
                     /gene_synonym="CCA1; CGI-47; MtCCA; RPEM; SIFD"
                     /coded_by="NM_001367323.1:1107..2411"
                     /note="isoform 1 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS2561.2"
                     /db_xref="GeneID:51095"
                     /db_xref="HGNC:HGNC:17341"
                     /db_xref="MIM:612907"
ORIGIN      
        1 mlrclyhwhr pvlnrrwsrl clpkqylftm klqspefqsl fteglkslte lfvkenhelr
       61 iaggavrdll ngvkpqdidf attatptqmk emfqsagirm innrgekhgt itarlheenf
      121 eittlridvt tdgrhaevef ttdwqkdaer rdltinsmfl gfdgtlfdyf ngyedlknkk
      181 vrfvghakqr iqedylrilr yfrfygrivd kpgdhdpetl eaiaenakgl agisgeriwv
      241 elkkilvgnh vnhlihliyd ldvapyiglp anasleefdk vsknvdgfsp kpvtllaslf
      301 kvqddvtkld lrlkiakeek nlglfivknr kdlikatdss dplkpyqdfi idsrepdatt
      361 rvcellkyqg ehcllkemqq wsippfpvsg hdirkvgiss gkeigallqq lreqwkksgy
      421 qmekdellsy ikkt
//
LOCUS       NP_001180229             761 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001180229 XP_011508175
VERSION     NP_001180229.1
DBSOURCE    REFSEQ: accession NM_001193300.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135927.14.
            
            On May 10, 2019 this sequence version replaced XP_011508175.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, as
            compared to variant 1. Variants 1-3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.20968.1,
                                           SRR1803615.101560.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..761
                     /product="semaphorin-4A isoform 1 precursor"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=80167
     sig_peptide     1..32
                     /calculated_mol_wt=3425
     mat_peptide     33..761
                     /product="semaphorin-4A isoform 1"
                     /calculated_mol_wt=80167
     Region          55..495
                     /region_name="Sema_4A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4A (Sema4A); cd11256"
                     /db_xref="CDD:200517"
     Site            order(115..117,178,199,201..202,204,219,222,224,229,252,
                     276..280,282,361..362,386,390,393)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200517"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            order(253..254,256,259..261,295,297..299,301,303,326..328,
                     334..335,399,411)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200517"
     Region          496..540
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          566..638
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          576..580
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          588..592
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          607..611
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          621..626
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Site            684..704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          722..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     CDS             1..761
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_001193300.2:405..2690"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS1132.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 malpalgldp wsllglflfq llqlllpttt aggggqgpmp rvryyagder ralsffhqkg
       61 lqdfdtllls gdgntlyvga reailaldiq dpgvprlknm ipwpasdrkk secafkkksn
      121 etqcfnfirv lvsynvthly tcgtfafspa ctfielqdsy llpisedkvm egkgqspfdp
      181 ahkhtavlvd gmlysgtmnn flgsepilmr tlgsqpvlkt dnflrwlhhd asfvaaipst
      241 qvvyfffeet asefdfferl htsrvarvck ndvggekllq kkwttflkaq llctqpgqlp
      301 fnvirhavll padsptaphi yavftsqwqv ggtrssavca fslldiervf kgkykelnke
      361 tsrwttyrgp etnprpgscs vgpssdkalt fmkdhflmde qvvgtpllvk sgveytrlav
      421 etaqgldghs hlvmylgttt gslhkavvsg dssahlveei qlfpdpepvr nlqlaptqga
      481 vfvgfsggvw rvprancsvy escvdcvlar dphcawdpes rtccllsapn lnswkqdmer
      541 gnpewacasg pmsrslrpqs rpqiikevla vpnsilelpc phlsalasyy wshgpaavpe
      601 asstvyngsl llivqdgvgg lyqcwateng fsypvisywv dsqdqtlald pelagipreh
      661 vkvpltrvsg gaalaaqqsy wphfvtvtvl falvlsgali ilvasplral rargkvqgce
      721 tlrpgekapl sreqhlqspk ecrtsasdvd adnnclgtev a
//
LOCUS       NP_001354627             878 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform iii [Homo sapiens].
ACCESSION   NP_001354627
VERSION     NP_001354627.1
DBSOURCE    REFSEQ: accession NM_001367698.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 878)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 878)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 878)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 878)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 878)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 878)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 878)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 878)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 878)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 878)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.16206.1,
                                           SRR1803617.202257.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..878
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..878
                     /product="SUN domain-containing protein 1 isoform iii"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=97727
     Region          62..385
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          510..563
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(510,513..514,517,520..521,524..525,527..528,
                     531..532,534..535,538..539,541..542,545,548..549,552,
                     555..556,559..560,562..563)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          522..>655
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          640..698
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          741..876
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..878
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367698.1:52..2688"
                     /note="isoform iii is encoded by transcript variant 61"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealcyfllqi lrrigavgqa vsrtawsalw lavvapgkaa sgvfwwlgig
      361 wyqfvtlisw lnvflltrcl rnickflvll iplflllgls lrgqgnffsf lpvlnwasmh
      421 rtqrvddpqd vfkpttsrlk qplqgdseaf pwhwmsgveq qvaslsgqch hhgenlrelt
      481 tllqklqarv dqmeggaagp sasvrdavgq ppretdfmaf hqehevrmsh ledilgklre
      541 kseaiqkele qtkqktisav geqllptveh lqleldqlks elsswrhvkt gcetvdavqe
      601 rvdvqvremv kllfsedqqg gsleqllqrf ssqfvskgdl qtmlrdlqlq ilrnvthhvs
      661 vtkqlptsea vvsavseaga sgiteaqara ivnsalklys qdktgmvdfa lesgggsils
      721 trcsetyetk talmslfgip lwyfsqsprv viqpdiypgn cwafkgsqgy lvvrlsmmih
      781 paaftlehip ktlsptgnis sapkdfavyg leneyqeegq llgqftydqd geslqmfqal
      841 krpddtafqi velrifsnwg hpeytclyrf rvhgepvk
//
LOCUS       NP_001288074             279 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 isoform d [Homo sapiens].
ACCESSION   NP_001288074
VERSION     NP_001288074.1
DBSOURCE    REFSEQ: accession NM_001301145.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 279)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 279)
  AUTHORS   Sun,L., Chen,Y., Xia,L., Wang,J., Zhu,J., Li,J., Wang,K., Shen,K.,
            Zhang,D., Zhang,G., Shi,T. and Chen,W.
  TITLE     TRIM69 suppressed the anoikis resistance and metastasis of gastric
            cancer through ubiquitin-proteasome-mediated degradation of PRKCD
  JOURNAL   Oncogene 42 (49), 3619-3632 (2023)
   PUBMED   37864033
  REMARK    GeneRIF: TRIM69 suppressed the anoikis resistance and metastasis of
            gastric cancer through ubiquitin-proteasome-mediated degradation of
            PRKCD.
REFERENCE   3  (residues 1 to 279)
  AUTHORS   Wang,Y., Risteski,P., Yang,Y., Chen,H., Droby,G., Walens,A.,
            Jayaprakash,D., Troester,M., Herring,L., Chernoff,J., Tolic,I.M.,
            Bowser,J. and Vaziri,C.
  TITLE     The TRIM69-MST2 signaling axis regulates centrosome dynamics and
            chromosome segregation
  JOURNAL   Nucleic Acids Res 51 (19), 10568-10589 (2023)
   PUBMED   37739411
  REMARK    GeneRIF: The TRIM69-MST2 signaling axis regulates centrosome
            dynamics and chromosome segregation.
REFERENCE   4  (residues 1 to 279)
  AUTHORS   Yuan,J., Lv,T., Yang,J., Wu,Z., Yan,L., Yang,J. and Shi,Y.
  TITLE     HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability by
            diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma
  JOURNAL   Redox Biol 58, 102546 (2022)
   PUBMED   36423520
  REMARK    GeneRIF: HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability
            by diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 279)
  AUTHORS   Song,Y., Nguyen,X.N., Kumar,A., da Silva,C., Picard,L., Etienne,L.
            and Cimarelli,A.
  TITLE     Trim69 is a microtubule regulator that acts as a pantropic viral
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 119 (43), e2211467119 (2022)
   PUBMED   36251989
  REMARK    GeneRIF: Trim69 is a microtubule regulator that acts as a pantropic
            viral inhibitor.
REFERENCE   6  (residues 1 to 279)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
  REMARK    GeneRIF: hTRIM69 is a novel E3 ubiquitin ligase identified from
            human testis and may function to ubiquitinate its particular
            substrates during spermatogenesis.
REFERENCE   7  (residues 1 to 279)
  AUTHORS   Bahmanyar,S., Kaplan,D.D., Deluca,J.G., Giddings,T.H. Jr.,
            O'Toole,E.T., Winey,M., Salmon,E.D., Casey,P.J., Nelson,W.J. and
            Barth,A.I.
  TITLE     beta-Catenin is a Nek2 substrate involved in centrosome separation
  JOURNAL   Genes Dev 22 (1), 91-105 (2008)
   PUBMED   18086858
REFERENCE   8  (residues 1 to 279)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     Forced expression of RNF36 induces cell apoptosis
  JOURNAL   Exp Cell Res 287 (2), 301-313 (2003)
   PUBMED   12837286
REFERENCE   9  (residues 1 to 279)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     A novel member of the RBCC family, Trif, expressed specifically in
            the spermatids of mouse testis
  JOURNAL   Mech Dev 108 (1-2), 213-216 (2001)
   PUBMED   11578878
  REMARK    GeneRIF: Gene and protein analysis of the mouse counterpart.
REFERENCE   10 (residues 1 to 279)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI827618.1, AF302089.1,
            AC122108.2 and DB524904.1.
            
            Summary: This gene encodes a member of the RING-B-box-coiled-coil
            (RBCC) family and encodes a protein with an N-terminal RING finger
            motif, a PRY domain and a C-terminal SPRY domain. The mouse
            ortholog of this gene is specifically expressed in germ cells at
            the round spermatid stages during spermatogenesis and, when
            overexpressed, induces apoptosis. Alternatively spliced transcript
            variants encoding distinct isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (d) lacks an alternate exon and
            uses two alternate splice sites, and it thus differs in its 5' UTR,
            initiates translation at a downstream in-frame start codon, and
            lacks an in-frame segment in the central coding region, compared to
            variant a. The encoded isoform (d, also known as TRIMLESS beta) is
            shorter at the N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF302089.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..279
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..279
                     /product="E3 ubiquitin-protein ligase TRIM69 isoform d"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 36; RFP-like domain-containing
                     protein trimless; E3 ubiquitin-protein ligase TRIM69;
                     RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=31937
     Region          90..276
                     /region_name="SPRY_PRY_TRIM69"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     69 (TRIM69), also known as RING finger protein 36 (RNF36);
                     cd15818"
                     /db_xref="CDD:293990"
     CDS             1..279
                     /gene="TRIM69"
                     /gene_synonym="HSD-34; HSD34; RNF36; Trif"
                     /coded_by="NM_001301145.2:321..1160"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS76746.1"
                     /db_xref="GeneID:140691"
                     /db_xref="HGNC:HGNC:17857"
                     /db_xref="MIM:616017"
ORIGIN      
        1 meflklhqfl hskekdilte lreegkalne emelnlsqlq eqcllakdml dittllhsle
       61 qgmkvlatre lisrklnlgq ykgpiqymvw remqdtlcpg lspltldpkt ahpnlvlsks
      121 qtsvwhgdik kimpddperf dssvavlgsr gftsgkwywe vevakktkwt vgvvresiir
      181 kgscpltpeq gfwllrlrnq tdlkaldlps fsltltnnld kvgiyldyeg gqlsfynakt
      241 mthiytfsnt fmeklypyfc pclndggenk eplhilhpq
//
LOCUS       NP_001099048             218 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptonemal complex central element protein 2 [Homo sapiens].
ACCESSION   NP_001099048
VERSION     NP_001099048.1
DBSOURCE    REFSEQ: accession NM_001105578.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Dunce,J.M., Salmon,L.J. and Davies,O.R.
  TITLE     Structural basis of meiotic chromosome synaptic elongation through
            hierarchical fibrous assembly of SYCE2-TEX12
  JOURNAL   Nat Struct Mol Biol 28 (8), 681-693 (2021)
   PUBMED   34373646
  REMARK    GeneRIF: Structural basis of meiotic chromosome synaptic elongation
            through hierarchical fibrous assembly of SYCE2-TEX12.
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Cahoon,C.K. and Hawley,R.S.
  TITLE     Regulating the construction and demolition of the synaptonemal
            complex
  JOURNAL   Nat Struct Mol Biol 23 (5), 369-377 (2016)
   PUBMED   27142324
  REMARK    Review article
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Goldstein,J.I., Jarskog,L.F., Hilliard,C., Alfirevic,A., Duncan,L.,
            Fourches,D., Huang,H., Lek,M., Neale,B.M., Ripke,S., Shianna,K.,
            Szatkiewicz,J.P., Tropsha,A., van den Oord,E.J., Cascorbi,I.,
            Dettling,M., Gazit,E., Goff,D.C., Holden,A.L., Kelly,D.L.,
            Malhotra,A.K., Nielsen,J., Pirmohamed,M., Rujescu,D., Werge,T.,
            Levy,D.L., Josiassen,R.C., Kennedy,J.L., Lieberman,J.A., Daly,M.J.
            and Sullivan,P.F.
  TITLE     Clozapine-induced agranulocytosis is associated with rare HLA-DQB1
            and HLA-B alleles
  JOURNAL   Nat Commun 5, 4757 (2014)
   PUBMED   25187353
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Bolcun-Filas,E., Costa,Y., Speed,R., Taggart,M., Benavente,R., De
            Rooij,D.G. and Cooke,H.J.
  TITLE     SYCE2 is required for synaptonemal complex assembly, double strand
            break repair, and homologous recombination
  JOURNAL   J Cell Biol 176 (6), 741-747 (2007)
   PUBMED   17339376
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Costa,Y., Speed,R., Ollinger,R., Alsheimer,M., Semple,C.A.,
            Gautier,P., Maratou,K., Novak,I., Hoog,C., Benavente,R. and
            Cooke,H.J.
  TITLE     Two novel proteins recruited by synaptonemal complex protein 1
            (SYCP1) are at the centre of meiosis
  JOURNAL   J Cell Sci 118 (Pt 12), 2755-2762 (2005)
   PUBMED   15944401
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092069.2, DB449708.1,
            BC035819.2 and AD000092.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is part of the
            synaptonemal complex formed between homologous chromosomes during
            meiotic prophase. The encoded protein associates with SYCP1 and
            SYCE1 and is found only where chromosome cores are synapsed.
            [provided by RefSeq, Dec 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302373.1, DRR138512.481004.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000293695.8/ ENSP00000293695.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.13"
     Protein         1..218
                     /product="synaptonemal complex central element protein 2"
                     /calculated_mol_wt=24558
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIF2.2)"
     Region          <62..>181
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
     Region          171..218
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PIF2.2)"
     CDS             1..218
                     /gene="SYCE2"
                     /gene_synonym="CESC1"
                     /coded_by="NM_001105578.2:37..693"
                     /db_xref="CCDS:CCDS42509.1"
                     /db_xref="GeneID:256126"
                     /db_xref="HGNC:HGNC:27411"
                     /db_xref="MIM:611487"
ORIGIN      
        1 merqgvdvph vkckdqepqp lgeskehprw eenceeeagg gpasascqlt vlegksglyf
       61 ssldssidil qkraqelien inksrqkdha lmtnfrnslk tkvsdltekl eeriyqiynd
      121 hnkiiqeklq eftqkmakis hletelkqvc hsvetvykdl clqpeqslrl rwgpdhsrgk
      181 spprpgnsqp pdvfvssvae ttsqatasev qtnrdgec
//
LOCUS       NP_002624                562 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoglucomutase-1 isoform 1 [Homo sapiens].
ACCESSION   NP_002624
VERSION     NP_002624.2
DBSOURCE    REFSEQ: accession NM_002633.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Liu,S., Deng,Y., Yu,Y. and Xia,X.
  TITLE     Knock-down of PGM1 inhibits cell viability, glycolysis, and
            oxidative phosphorylation in glioma under low glucose condition via
            the Myc signaling pathway
  JOURNAL   Biochem Biophys Res Commun 656, 38-45 (2023)
   PUBMED   36947965
  REMARK    GeneRIF: Knock-down of PGM1 inhibits cell viability, glycolysis,
            and oxidative phosphorylation in glioma under low glucose condition
            via the Myc signaling pathway.
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Stiers,K.M., Owuocha,L.F. and Beamer,L.J.
  TITLE     Effects of the T337M and G391V disease-related variants on human
            phosphoglucomutase 1: structural disruptions large and small
  JOURNAL   Acta Crystallogr F Struct Biol Commun 78 (Pt 5), 200-209 (2022)
   PUBMED   35506765
  REMARK    GeneRIF: Effects of the T337M and G391V disease-related variants on
            human phosphoglucomutase 1: structural disruptions large and small.
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Beamer,L.J.
  TITLE     Enzyme dysfunction at atomic resolution: Disease-associated
            variants of human phosphoglucomutase-1
  JOURNAL   Biochimie 183, 44-48 (2021)
   PUBMED   32898648
  REMARK    GeneRIF: Enzyme dysfunction at atomic resolution:
            Disease-associated variants of human phosphoglucomutase-1.
            Review article
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Conte,F., Morava,E., Bakar,N.A., Wortmann,S.B., Poerink,A.J.,
            Grunewald,S., Crushell,E., Al-Gazali,L., de Vries,M.C., Morkrid,L.,
            Hertecant,J., Brocke Holmefjord,K.S., Kronn,D., Feigenbaum,A.,
            Fingerhut,R., Wong,S.Y., van Scherpenzeel,M., Voermans,N.C. and
            Lefeber,D.J.
  TITLE     Phosphoglucomutase-1 deficiency: Early presentation, metabolic
            management and detection in neonatal blood spots
  JOURNAL   Mol Genet Metab 131 (1-2), 135-146 (2020)
   PUBMED   33342467
  REMARK    GeneRIF: Phosphoglucomutase-1 deficiency: Early presentation,
            metabolic management and detection in neonatal blood spots.
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Backe,P.H., Laerdahl,J.K., Kittelsen,L.S., Dalhus,B., Morkrid,L.
            and Bjoras,M.
  TITLE     Structural basis for substrate and product recognition in human
            phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily
  JOURNAL   Sci Rep 10 (1), 5656 (2020)
   PUBMED   32221390
  REMARK    GeneRIF: Structural basis for substrate and product recognition in
            human phosphoglucomutase-1 (PGM1) isoform 2, a member of the
            alpha-D-phosphohexomutase superfamily.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Whitehouse,D.B., Putt,W., Lovegrove,J.U., Morrison,K.,
            Hollyoake,M., Fox,M.F., Hopkinson,D.A. and Edwards,Y.H.
  TITLE     Phosphoglucomutase 1: complete human and rabbit mRNA sequences and
            direct mapping of this highly polymorphic marker on human
            chromosome 1
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 411-415 (1992)
   PUBMED   1530890
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Drago,G.A., Hopkinson,D.A., Westwood,S.A. and Whitehouse,D.B.
  TITLE     Antigenic analysis of the major human phosphoglucomutase isozymes:
            PGM1, PGM2, PGM3 and PGM4
  JOURNAL   Ann Hum Genet 55 (4), 263-271 (1991)
   PUBMED   1840235
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Herbich,J., Szilvassy,J. and Schnedl,W.
  TITLE     Gene localisation of the PGM1 enzyme system and the Duffy blood
            groups on chromosome No. 1 by means of a new fragile site at 1p31
  JOURNAL   Hum Genet 70 (2), 178-180 (1985)
   PUBMED   3159642
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC019920.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_002624.1.
            
            Summary: The protein encoded by this gene is an isozyme of
            phosphoglucomutase (PGM) and belongs to the phosphohexose mutase
            family. There are several PGM isozymes, which are encoded by
            different genes and catalyze the transfer of phosphate between the
            1 and 6 positions of glucose. In most cell types, this PGM isozyme
            is predominant, representing about 90% of total PGM activity. In
            red cells, PGM2 is a major isozyme. This gene is highly
            polymorphic. Mutations in this gene cause glycogen storage disease
            type 14. Alternativley spliced transcript variants encoding
            different isoforms have been identified in this gene.[provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) is dominant and encodes a
            protein of 562aa.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001756.2, SRR3476690.1035358.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371084.8/ ENSP00000360125.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.3"
     Protein         1..562
                     /product="phosphoglucomutase-1 isoform 1"
                     /EC_number="5.4.2.2"
                     /note="PGM 1; glucose phosphomutase 1"
                     /calculated_mol_wt=61318
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:21406692; N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Region          5..562
                     /region_name="PGM1"
                     /note="Phosphoglucomutase 1 (PGM1) catalyzes the
                     bidirectional interconversion of glucose-1-phosphate
                     (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose
                     1,6-diphosphate intermediate, an important metabolic step
                     in prokaryotes and eukaryotes. In one direction; cd03085"
                     /db_xref="CDD:100087"
     Site            16
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            order(20,117,293,336,357,359,376,378,380,503,505..507,515)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:100087"
     Site            order(47..48,53..54,107,133..135,367)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:100087"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0F9; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            order(117..119,288,290,292..293,359,389,503,505..507,515)
                     /site_type="active"
                     /db_xref="CDD:100087"
     Site            order(117,288,290,292)
                     /site_type="metal-binding"
                     /note="metal binding site [ion binding]"
                     /db_xref="CDD:100087"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:25288802,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            349
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0F9; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0F9; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PAK1.
                     /evidence=ECO:0000269|PubMed:15378030; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            477
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            485
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0F9; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            509
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P38652; propagated from
                     UniProtKB/Swiss-Prot (P36871.3)"
     CDS             1..562
                     /gene="PGM1"
                     /gene_synonym="CDG1T; GSD14"
                     /coded_by="NM_002633.3:79..1767"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS625.1"
                     /db_xref="GeneID:5236"
                     /db_xref="HGNC:HGNC:8905"
                     /db_xref="MIM:171900"
ORIGIN      
        1 mvkivtvktq ayqdqkpgts glrkrvkvfq ssanyaenfi qsiistvepa qrqeatlvvg
       61 gdgrfymkea iqliariaaa ngigrlvigq ngilstpavs ciirkikaig giiltashnp
      121 ggpngdfgik fnisnggpap eaitdkifqi sktieeyavc pdlkvdlgvl gkqqfdlenk
      181 fkpftveivd sveayatmlr sifdfsalke llsgpnrlki ridamhgvvg pyvkkilcee
      241 lgapansavn cvpledfggh hpdpnltyaa dlvetmksge hdfgaafdgd gdrnmilgkh
      301 gffvnpsdsv aviaanifsi pyfqqtgvrg farsmptsga ldrvasatki alyetptgwk
      361 ffgnlmdask lslcgeesfg tgsdhirekd glwavlawls ilatrkqsve dilkdhwqky
      421 grnfftrydy eeveaegank mmkdlealmf drsfvgkqfs andkvytvek adnfeysdpv
      481 dgsisrnqgl rliftdgsri vfrlsgtgsa gatirlyids yekdvakinq dpqvmlapli
      541 sialkvsqlq ertgrtaptv it
//
LOCUS       NP_002465               1972 aa            linear   PRI 20-NOV-2025
DEFINITION  myosin-11 isoform SM1A [Homo sapiens].
ACCESSION   NP_002465 NP_075008
VERSION     NP_002465.1
DBSOURCE    REFSEQ: accession NM_002474.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1972)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1972)
  AUTHORS   Wei,X., Ma,Y., Xie,B., Gui,C., Shi,M., Wei,X., Huang,Y., Fan,X.,
            Wei,Q., Huang,Q., Deng,L., Zhang,C., Deng,X., Gui,B. and Chen,Y.
  TITLE     Complex genotype-phenotype correlation of MYH11: new insights from
            monozygotic twins with highly variable expressivity and outcomes
  JOURNAL   BMC Med Genomics 17 (1), 135 (2024)
   PUBMED   38773466
  REMARK    GeneRIF: Complex genotype-phenotype correlation of MYH11: new
            insights from monozygotic twins with highly variable expressivity
            and outcomes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1972)
  AUTHORS   Billon,C., Piccoli,G.B., de Sainte Agathe,J.M., Stoeva,R.,
            Derive,N., Heidet,L., Berrebi,D., Bruneval,P., Jeunemaitre,X. and
            Hureaux,M.
  TITLE     Genome-wide analysis identifies MYH11 compound heterozygous
            variants leading to visceral myopathy corresponding to late-onset
            form of megacystis-microcolon-intestinal hypoperistalsis syndrome
  JOURNAL   Mol Genet Genomics 299 (1), 44 (2024)
   PUBMED   38625590
  REMARK    GeneRIF: Genome-wide analysis identifies MYH11 compound
            heterozygous variants leading to visceral myopathy corresponding to
            late-onset form of megacystis-microcolon-intestinal hypoperistalsis
            syndrome.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1972)
  AUTHORS   Pan,M., Tan,X., Sun,T., Zhu,W., Liu,H., Liu,Q. and Dong,H.
  TITLE     A harmful MYH11 variant detected in a family with thoracic aortic
            dissection and patent ductus arteriosus
  JOURNAL   Forensic Sci Med Pathol 20 (1), 212-218 (2024)
   PUBMED   37306888
  REMARK    GeneRIF: A harmful MYH11 variant detected in a family with thoracic
            aortic dissection and patent ductus arteriosus.
REFERENCE   5  (residues 1 to 1972)
  AUTHORS   Aikawa,M., Sivam,P.N., Kuro-o,M., Kimura,K., Nakahara,K.,
            Takewaki,S., Ueda,M., Yamaguchi,H., Yazaki,Y., Periasamy,M. et al.
  TITLE     Human smooth muscle myosin heavy chain isoforms as molecular
            markers for vascular development and atherosclerosis
  JOURNAL   Circ Res 73 (6), 1000-1012 (1993)
   PUBMED   7916668
REFERENCE   6  (residues 1 to 1972)
  AUTHORS   van der Reijden,B.A., Dauwerse,J.G., Wessels,J.W., Beverstock,G.C.,
            Hagemeijer,A., van Ommen,G.J. and Breuning,M.H.
  TITLE     A gene for a myosin peptide is disrupted by the inv(16)(p13q22) in
            acute nonlymphocytic leukemia M4Eo
  JOURNAL   Blood 82 (10), 2948-2952 (1993)
   PUBMED   8219185
REFERENCE   7  (residues 1 to 1972)
  AUTHORS   Deng,Z., Liu,P., Marlton,P., Claxton,D.F., Lane,S., Callen,D.F.,
            Collins,F.S. and Siciliano,M.J.
  TITLE     Smooth muscle myosin heavy chain locus (MYH11) maps to
            16p13.13-p13.12 and establishes a new region of conserved synteny
            between human 16p and mouse 16
  JOURNAL   Genomics 18 (1), 156-159 (1993)
   PUBMED   8276405
REFERENCE   8  (residues 1 to 1972)
  AUTHORS   Matsuoka,R., Yoshida,M.C., Furutani,Y., Imamura,S., Kanda,N.,
            Yanagisawa,M., Masaki,T. and Takao,A.
  TITLE     Human smooth muscle myosin heavy chain gene mapped to chromosomal
            region 16q12
  JOURNAL   Am J Med Genet 46 (1), 61-67 (1993)
   PUBMED   7684189
REFERENCE   9  (residues 1 to 1972)
  AUTHORS   Ambartsumyan,L.
  TITLE     Megacystis-Microcolon-Intestinal Hypoperistalsis Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31070878
REFERENCE   10 (residues 1 to 1972)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX489788.1, AY520817.1,
            BC104906.1 and AA552189.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 16, 2003 this sequence version replaced NP_075008.1.
            
            Summary: The protein encoded by this gene is a smooth muscle myosin
            belonging to the myosin heavy chain family. The gene product is a
            subunit of a hexameric protein that consists of two heavy chain
            subunits and two pairs of non-identical light chain subunits. It
            functions as a major contractile protein, converting chemical
            energy into mechanical energy through the hydrolysis of ATP. A
            chromosomal rearrangement involving this gene is associated with
            acute myeloid leukemia of the M4Eo subtype. Mutations in this gene
            are associated with visceral myopathy,
            megacystis-microcolon-intestinal hypoperistalsis syndrome 2, and
            familial thoracic aortic aneurysm 4. [provided by RefSeq, May
            2022].
            
            Transcript Variant: This variant (SM1A) lacks two segments in the
            coding region, compared to variant SM2B. The encoded isoform (SM1A)
            is shorter and varies in the carboxyl terminus, compared to isoform
            SM2B.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: GQ900967.1, AB020673.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300036.6/ ENSP00000300036.5
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1972
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.11"
     Protein         1..1972
                     /product="myosin-11 isoform SM1A"
                     /note="myosin, heavy polypeptide 11, smooth muscle;
                     myosin, heavy chain 11, smooth muscle; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=227209
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          31..76
                     /region_name="Myosin_N"
                     /note="Myosin N-terminal SH3-like domain; pfam02736"
                     /db_xref="CDD:460670"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          99..771
                     /region_name="MYSc_Myh11"
                     /note="class II myosin heavy chain 11, motor domain;
                     cd14921"
                     /db_xref="CDD:276885"
     Site            order(126..134,178..185,231..241,459..464)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276885"
     Site            126..134
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276885"
     Site            129
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            178..185
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276885"
     Site            231..241
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276885"
     Site            459..464
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276885"
     Site            order(488..499,502..511)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276885"
     Region          661..683
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            703..713
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276885"
     Site            715..771
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276885"
     Region          762..776
                     /region_name="Actin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Region          848..1928
                     /region_name="Myosin_tail_1"
                     /note="Myosin tail; pfam01576"
                     /db_xref="CDD:460256"
     Region          858..882
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            1177
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z406; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1684
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1722
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63862; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Region          1744..1800
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Region          1866..1972
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Region          1935..1972
                     /region_name="C-terminal"
                     /note="propagated from UniProtKB/Swiss-Prot (P35749.3)"
     Site            1954
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1958
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     Site            1971
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08638; propagated from
                     UniProtKB/Swiss-Prot (P35749.3)"
     CDS             1..1972
                     /gene="MYH11"
                     /gene_synonym="AAT4; FAA4; SMHC; SMMHC; SMMS-1; VSCM2"
                     /coded_by="NM_002474.3:106..6024"
                     /note="isoform SM1A is encoded by transcript variant SM1A"
                     /db_xref="CCDS:CCDS10565.1"
                     /db_xref="GeneID:4629"
                     /db_xref="HGNC:HGNC:7569"
                     /db_xref="MIM:160745"
ORIGIN      
        1 maqkgqlsdd ekflfvdknf inspvaqadw aakrlvwvps ekqgfeaasi keekgdevvv
       61 elvengkkvt vgkddiqkmn ppkfskvedm aeltclneas vlhnlreryf sgliytysgl
      121 fcvvvnpykh lpiysekivd mykgkkrhem pphiyaiadt ayrsmlqdre dqsilctges
      181 gagktentkk viqylavvas shkgkkdtsi tgelekqllq anpileafgn aktvkndnss
      241 rfgkfirinf dvtgyivgan ietylleksr airqardert fhifyymiag akekmrsdll
      301 legfnnytfl sngfvpipaa qddemfqetv eamaimgfse eeqlsilkvv ssvlqlgniv
      361 fkkerntdqa smpdntaaqk vchlmginvt dftrsiltpr ikvgrdvvqk aqtkeqadfa
      421 vealakatye rlfrwiltrv nkaldkthrq gasflgildi agfeifevns feqlcinytn
      481 eklqqlfnht mfileqeeyq regiewnfid fgldlqpcie lierpnnppg vlalldeecw
      541 fpkatdksfv eklcteqgsh pkfqkpkqlk dktefsiihy agkvdynasa wltknmdpln
      601 dnvtsllnas sdkfvadlwk dvdrivgldq makmtesslp sasktkkgmf rtvgqlykeq
      661 lgklmttlrn ttpnfvrcii pnhekrsgkl daflvleqlr cngvlegiri crqgfpnriv
      721 fqefrqryei laanaipkgf mdgkqacilm ikaleldpnl yrigqskiff rtgvlahlee
      781 erdlkitdvi mafqamcrgy larkafakrq qqltamkviq rncaaylklr nwqwwrlftk
      841 vkpllqvtrq eeemqakede lqktkerqqk aenelkeleq khsqlteekn llqeqlqaet
      901 elyaeaeemr vrlaakkqel eeilhemear leeeedrgqq lqaerkkmaq qmldleeqle
      961 eeeaarqklq lekvtaeaki kkledeilvm ddqnnklske rklleerisd lttnlaeeee
     1021 kaknltklkn khesmisele vrlkkeeksr qeleklkrkl egdasdfheq iadlqaqiae
     1081 lkmqlakkee elqaalarld deiaqknnal kkireleghi sdlqedldse raarnkaekq
     1141 krdlgeelea lkteledtld statqqelra kreqevtvlk kaldeetrsh eaqvqemrqk
     1201 haqaveelte qleqfkraka nldknkqtle kenadlagel rvlgqakqev ehkkkkleaq
     1261 vqelqskcsd geraraelnd kvhklqneve svtgmlneae gkaiklakdv aslssqlqdt
     1321 qellqeetrq klnvstklrq leeernslqd qldeemeakq nlerhistln iqlsdskkkl
     1381 qdfastveal eegkkrfqke ienltqqyee kaaaydklek tknrlqqeld dlvvdldnqr
     1441 qlvsnlekkq rkfdqllaee knisskyade rdraeaeare ketkalslar aleealeake
     1501 elertnkmlk aemedlvssk ddvgknvhel ekskraletq meemktqlee ledelqated
     1561 aklrlevnmq alkgqferdl qardeqneek rrqlqrqlhe yetelederk qralaaaakk
     1621 klegdlkdle lqadsaikgr eeaikqlrkl qaqmkdfqre ledarasrde ifatakenek
     1681 kaksleadlm qlqedlaaae rarkqadlek eelaeelass lsgrnalqde krrleariaq
     1741 leeeleeeqg nmeamsdrvr katqqaeqls nelatersta qknesarqql erqnkelrsk
     1801 lhemegavks kfkstiaale akiaqleeqv eqearekqaa tkslkqkdkk lkeillqved
     1861 erkmaeqyke qaekgnarvk qlkrqleeae eesqrinanr rklqreldea tesneamgre
     1921 vnalksklrr gnetsfvpsr rsggrrvien adgseeetdt rdadfngtka se
//
LOCUS       NP_071731                448 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member EDAR precursor
            [Homo sapiens].
ACCESSION   NP_071731
VERSION     NP_071731.1
DBSOURCE    REFSEQ: accession NM_022336.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 448)
  AUTHORS   Fang,Z., Wang,Y., Huang,B., Chen,X., Jiang,R. and Yin,M.
  TITLE     Depletion of G9A attenuates imiquimod-induced psoriatic dermatitis
            via targeting EDAR-NF-kappaB signaling in keratinocyte
  JOURNAL   Cell Death Dis 14 (9), 627 (2023)
   PUBMED   37739945
  REMARK    GeneRIF: Depletion of G9A attenuates imiquimod-induced psoriatic
            dermatitis via targeting EDAR-NF-kappaB signaling in keratinocyte.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 448)
  AUTHORS   Yagi,S., Yasuno,S., Ansai,O., Hayashi,R. and Shimomura,Y.
  TITLE     Different degree of loss-of-function among four missense mutations
            in the EDAR gene responsible for autosomal recessive hypohidrotic
            ectodermal dysplasia may be associated with the phenotypic severity
  JOURNAL   J Dermatol 50 (3), 349-356 (2023)
   PUBMED   36258277
  REMARK    GeneRIF: Different degree of loss-of-function among four missense
            mutations in the EDAR gene responsible for autosomal recessive
            hypohidrotic ectodermal dysplasia may be associated with the
            phenotypic severity.
REFERENCE   3  (residues 1 to 448)
  AUTHORS   Zhao,Z., Zhang,T., Li,T., Ye,Y., Feng,C., Wang,H. and Zhang,X.
  TITLE     A novel EDAR variant identified in non-syndromic tooth agenesis:
            Insights from molecular dynamics
  JOURNAL   Arch Oral Biol 146, 105600 (2023)
   PUBMED   36470092
  REMARK    GeneRIF: A novel EDAR variant identified in non-syndromic tooth
            agenesis: Insights from molecular dynamics.
REFERENCE   4  (residues 1 to 448)
  AUTHORS   Williams,R., Jobling,S., Sims,A.H., Mou,C., Wilkinson,L.,
            Collu,G.M., Streuli,C.H., Gilmore,A.P., Headon,D.J. and Brennan,K.
  TITLE     Elevated EDAR signalling promotes mammary gland tumourigenesis with
            squamous metaplasia
  JOURNAL   Oncogene 41 (7), 1040-1049 (2022)
   PUBMED   34916592
  REMARK    GeneRIF: Elevated EDAR signalling promotes mammary gland
            tumourigenesis with squamous metaplasia.
REFERENCE   5  (residues 1 to 448)
  AUTHORS   Coletta,D.K., Hlusko,L.J., Scott,G.R., Garcia,L.A., Vachon,C.M.,
            Norman,A.D., Funk,J.L., Shaibi,G.Q., Hernandez,V., De Filippis,E.
            and Mandarino,L.J.
  TITLE     Association of EDARV370A with breast density and metabolic syndrome
            in Latinos
  JOURNAL   PLoS One 16 (10), e0258212 (2021)
   PUBMED   34618839
  REMARK    GeneRIF: Association of EDARV370A with breast density and metabolic
            syndrome in Latinos.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 448)
  AUTHORS   Kumar,A., Eby,M.T., Sinha,S., Jasmin,A. and Chaudhary,P.M.
  TITLE     The ectodermal dysplasia receptor activates the nuclear
            factor-kappaB, JNK, and cell death pathways and binds to
            ectodysplasin A
  JOURNAL   J Biol Chem 276 (4), 2668-2677 (2001)
   PUBMED   11035039
REFERENCE   7  (residues 1 to 448)
  AUTHORS   Monreal,A.W., Ferguson,B.M., Headon,D.J., Street,S.L.,
            Overbeek,P.A. and Zonana,J.
  TITLE     Mutations in the human homologue of mouse dl cause autosomal
            recessive and dominant hypohidrotic ectodermal dysplasia
  JOURNAL   Nat Genet 22 (4), 366-369 (1999)
   PUBMED   10431241
REFERENCE   8  (residues 1 to 448)
  AUTHORS   Ho,L., Williams,M.S. and Spritz,R.A.
  TITLE     A gene for autosomal dominant hypohidrotic ectodermal dysplasia
            (EDA3) maps to chromosome 2q11-q13
  JOURNAL   Am J Hum Genet 62 (5), 1102-1106 (1998)
   PUBMED   9545409
REFERENCE   9  (residues 1 to 448)
  AUTHORS   Aswegan,A.L., Josephson,K.D., Mowbray,R., Pauli,R.M., Spritz,R.A.
            and Williams,M.S.
  TITLE     Autosomal dominant hypohidrotic ectodermal dysplasia in a large
            family
  JOURNAL   Am J Med Genet 72 (4), 462-467 (1997)
   PUBMED   9375732
REFERENCE   10 (residues 1 to 448)
  AUTHORS   Wright,J.T., Grange,D.K. and Fete,M.
  TITLE     Hypohidrotic Ectodermal Dysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301291
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092160.5, AF130988.1,
            AC133784.2, AC073415.6 and AI017384.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the tumor necrosis factor
            receptor family. The encoded transmembrane protein is a receptor
            for the soluble ligand ectodysplasin A, and can activate the
            nuclear factor-kappaB, JNK, and caspase-independent cell death
            pathways. It is required for the development of hair, teeth, and
            other ectodermal derivatives. Mutations in this gene result in
            autosomal dominant and recessive forms of hypohidrotic ectodermal
            dysplasia. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF130988.1, AK313781.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258443.7/ ENSP00000258443.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..448
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..448
                     /product="tumor necrosis factor receptor superfamily
                     member EDAR precursor"
                     /note="downless, mouse, homolog of; ectodysplasin 1,
                     anhidrotic receptor; tumor necrosis factor receptor
                     superfamily member EDAR; EDA-A1 receptor; downless
                     homolog; ectodermal dysplasia receptor; anhidrotic
                     ectodysplasin receptor 1; hypohidrotic ectodermal
                     dysplasia; ectodysplasin A1 receptor"
                     /calculated_mol_wt=45814
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2786
     Region          13..148
                     /region_name="TNFRSF_EDAR"
                     /note="Tumor necrosis factor receptor superfamily member
                     ectodysplasin A receptor (EDAR); cd13421"
                     /db_xref="CDD:276926"
     mat_peptide     27..448
                     /product="tumor necrosis factor receptor superfamily
                     member EDAR"
                     /calculated_mol_wt=45814
     Region          30..71
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          31..71
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276926"
     Site            38
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          73..113
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          74..113
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276926"
     Region          115..148
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          116..148
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276926"
     Site            188..208
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          220..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNE0.1)"
     Region          354..428
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     CDS             1..448
                     /gene="EDAR"
                     /gene_synonym="DL; ECTD10A; ECTD10B; ED1R; ED3; ED5;
                     EDA-A1R; EDA1R; EDA3; HRM1"
                     /coded_by="NM_022336.4:280..1626"
                     /db_xref="CCDS:CCDS2081.1"
                     /db_xref="GeneID:10913"
                     /db_xref="HGNC:HGNC:2895"
                     /db_xref="MIM:604095"
ORIGIN      
        1 mahvgdctqt pwlpvlvvsl mcsaraeysn cgeneyynqt tglcqecppc gpgeepylsc
       61 gygtkdedyg cvpcpaekfs kggyqicrrh kdcegffrat vltpgdmend aecgpclpgy
      121 ymlenrprni ygmvcyscll appntkecvg atsgasanfp gtsgsstlsp fqhahkelsg
      181 qghlatalii amstifimai aivliimfyi lktkpsapac ctshpgksve aqvskdeekk
      241 eapdnvvmfs ekdefeklta tpakptksen dasseneqll srsvdsdeep apdkqgspel
      301 cllslvhlar eksatsnksa giqsrrkkil dvyanvcgvv eglsptelpf dclektsrml
      361 sstynsekav vktwrhlaes fglkrdeigg mtdgmqlfdr istagysipe lltklvqier
      421 ldaveslcad ilewagvvpp asqphaas
//
LOCUS       NP_003462                408 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-gated potassium channel subunit beta-1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_003462
VERSION     NP_003462.2
DBSOURCE    REFSEQ: accession NM_003471.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 408)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 408)
  AUTHORS   Quintanilha,J.C.F., Wang,J., Sibley,A.B., Jiang,C., Etheridge,A.S.,
            Shen,F., Jiang,G., Mulkey,F., Patel,J.N., Hertz,D.L., Dees,E.C.,
            McLeod,H.L., Bertagnolli,M., Rugo,H., Kindler,H.L., Kelly,W.K.,
            Ratain,M.J., Kroetz,D.L., Owzar,K., Schneider,B.P., Lin,D. and
            Innocenti,F.
  TITLE     Bevacizumab-induced hypertension and proteinuria: a genome-wide
            study of more than 1000 patients
  JOURNAL   Br J Cancer 126 (2), 265-274 (2022)
   PUBMED   34616010
  REMARK    GeneRIF: Bevacizumab-induced hypertension and proteinuria: a
            genome-wide study of more than 1000 patients.
            Erratum:[Br J Cancer. 2022 Jan;126(1):162. doi:
            10.1038/s41416-021-01617-1. PMID: 34853435]
REFERENCE   3  (residues 1 to 408)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 408)
  AUTHORS   Macias,A., de la Cruz,A., Peraza,D.A., Benito-Bueno,A., Gonzalez,T.
            and Valenzuela,C.
  TITLE     KV1.5-KVbeta1.3 Recycling Is PKC-Dependent
  JOURNAL   Int J Mol Sci 22 (3), 1336 (2021)
   PUBMED   33572906
  REMARK    GeneRIF: KV1.5-KVbeta1.3 Recycling Is PKC-Dependent.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 408)
  AUTHORS   Cho,I.H., Panzera,L.C., Chin,M., Alpizar,S.A., Olveda,G.E.,
            Hill,R.A. and Hoppa,M.B.
  TITLE     The potassium channel subunit Kvbeta1 serves as a major control
            point for synaptic facilitation
  JOURNAL   Proc Natl Acad Sci U S A 117 (47), 29937-29947 (2020)
   PUBMED   33168717
  REMARK    GeneRIF: The potassium channel subunit Kvbeta1 serves as a major
            control point for synaptic facilitation.
REFERENCE   6  (residues 1 to 408)
  AUTHORS   England,S.K., Uebele,V.N., Kodali,J., Bennett,P.B. and Tamkun,M.M.
  TITLE     A novel K+ channel beta-subunit (hKv beta 1.3) is produced via
            alternative mRNA splicing
  JOURNAL   J Biol Chem 270 (48), 28531-28534 (1995)
   PUBMED   7499366
REFERENCE   7  (residues 1 to 408)
  AUTHORS   McCormack,K., McCormack,T., Tanouye,M., Rudy,B. and Stuhmer,W.
  TITLE     Alternative splicing of the human Shaker K+ channel beta 1 gene and
            functional expression of the beta 2 gene product
  JOURNAL   FEBS Lett 370 (1-2), 32-36 (1995)
   PUBMED   7649300
REFERENCE   8  (residues 1 to 408)
  AUTHORS   England,S.K., Uebele,V.N., Shear,H., Kodali,J., Bennett,P.B. and
            Tamkun,M.M.
  TITLE     Characterization of a voltage-gated K+ channel beta subunit
            expressed in human heart
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6309-6313 (1995)
   PUBMED   7603988
REFERENCE   9  (residues 1 to 408)
  AUTHORS   Morales,M.J., Castellino,R.C., Crews,A.L., Rasmusson,R.L. and
            Strauss,H.C.
  TITLE     A novel beta subunit increases rate of inactivation of specific
            voltage-gated potassium channel alpha subunits
  JOURNAL   J Biol Chem 270 (11), 6272-6277 (1995)
   PUBMED   7890764
REFERENCE   10 (residues 1 to 408)
  AUTHORS   Majumder,K., De Biasi,M., Wang,Z. and Wible,B.A.
  TITLE     Molecular cloning and functional expression of a novel potassium
            channel beta-subunit from human atrium
  JOURNAL   FEBS Lett 361 (1), 13-16 (1995)
   PUBMED   7890032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091607.11, DA408045.1,
            L39833.1, AK057059.1, AC092927.5, BC043166.2 and AI344124.1.
            
            On Dec 31, 2002 this sequence version replaced NP_003462.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member includes distinct isoforms
            which are encoded by alternatively spliced transcript variants of
            this gene. Some of these isoforms are beta subunits, which form
            heteromultimeric complexes with alpha subunits and modulate the
            activity of the pore-forming alpha subunits. [provided by RefSeq,
            Apr 2015].
            
            Transcript Variant: This variant (2) has an alternate 5' sequence
            including the 5' UTR and the 5' coding region, as compared to
            variant 1. It encodes isoform 2, also known as kvb1.2, which has a
            shorter and distinct N-terminus than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.152667.1,
                                           SRR1803617.94606.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..408
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..408
                     /product="voltage-gated potassium channel subunit beta-1
                     isoform 2"
                     /note="potassium channel beta 3 chain; potassium channel
                     beta3 subunit; potassium channel shaker chain beta 1a;
                     K(+) channel subunit beta-1; potassium voltage-gated
                     channel, shaker-related subfamily, beta member 1; K+
                     channel Beta1a chain; potassium voltage-gated channel
                     subfamily A member regulatory beta subunit 1; potassium
                     channel, voltage gated subfamily A regulatory beta subunit
                     1"
                     /calculated_mol_wt=45361
     Region          78..400
                     /region_name="AKR_KCAB1B_AKR6A3-like"
                     /note="voltage-gated potassium channel subunit beta-1
                     (KCAB1B) and similar proteins; cd19159"
                     /db_xref="CDD:381385"
     Site            order(96..98,104,126,131,159,199,229..230,255,284..289,
                     293,295,303..305,345,362..366,370,373..374)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:381385"
     Site            order(126,131,159,199)
                     /site_type="active"
                     /note="catalytic tetrad [active]"
                     /db_xref="CDD:381385"
     CDS             1..408
                     /gene="KCNAB1"
                     /gene_synonym="AKR6A3; hKvb3; hKvBeta3; KCNA1B; KV-BETA-1;
                     Kvb1.3"
                     /coded_by="NM_003471.3:218..1444"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3175.1"
                     /db_xref="GeneID:7881"
                     /db_xref="HGNC:HGNC:6228"
                     /db_xref="MIM:601141"
ORIGIN      
        1 mhlykpacad ipspklglpk ssesalkcrw hlavtktqpq aackpvrpsg aaeqkyvekf
       61 lrvhgislqe ttraetgmay rnlgksglrv sclglgtwvt fggqisdeva erlmtiayes
      121 gvnlfdtaev yaagkaevil gsiikkkgwr rsslvittkl ywggkaeter glsrkhiieg
      181 lkgslqrlql eyvdvvfanr pdsntpmeei vramthvinq gmamywgtsr wsameimeay
      241 svarqfnmip pvceqaeyhl fqrekvevql pelyhkigvg amtwsplacg iisgkygngv
      301 pessraslkc yqwlkerivs eegrkqqnkl kdlspiaerl gctlpqlava wclrnegvss
      361 vllgsstpeq lienlgaiqv lpkmtshvvn eidnilrnkp yskkdyrs
//
LOCUS       NP_003027                728 aa            linear   PRI 20-NOV-2025
DEFINITION  ski oncogene [Homo sapiens].
ACCESSION   NP_003027
VERSION     NP_003027.1
DBSOURCE    REFSEQ: accession NM_003036.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 728)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 728)
  AUTHORS   Fusco,C., Nardella,G., Morlino,S., Micale,L., Tragni,V.,
            Agolini,E., Novelli,A., Massuras,S., Giambra,V., Pierri,C.L. and
            Castori,M.
  TITLE     Nucleotide substitutions at the p.Gly117 and p.Thr180 mutational
            hot-spots of SKI alter molecular dynamics and may affect cell cycle
  JOURNAL   J Hum Genet 69 (1), 53-58 (2024)
   PUBMED   37697026
  REMARK    GeneRIF: Nucleotide substitutions at the p.Gly117 and p.Thr180
            mutational hot-spots of SKI alter molecular dynamics and may affect
            cell cycle.
REFERENCE   3  (residues 1 to 728)
  AUTHORS   Pelgrims,E., Lynch,S.A., Hannes,L., Hoffer,M.J.V., Melotte,C., Van
            Haeringen,A., Swillen,A. and Breckpot,J.
  TITLE     Triplications of chromosome 1p36.3, including the genes GABRD and
            SKI, are associated with a developmental disorder and a facial
            gestalt
  JOURNAL   Am J Med Genet A 191 (7), 1889-1899 (2023)
   PUBMED   37129290
  REMARK    GeneRIF: Triplications of chromosome 1p36.3, including the genes
            GABRD and SKI, are associated with a developmental disorder and a
            facial gestalt.
REFERENCE   4  (residues 1 to 728)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 728)
  AUTHORS   Pearson-White,S.
  TITLE     SnoI, a novel alternatively spliced isoform of the ski
            protooncogene homolog, sno
  JOURNAL   Nucleic Acids Res 21 (19), 4632-4638 (1993)
   PUBMED   8233802
REFERENCE   6  (residues 1 to 728)
  AUTHORS   Nagase,T., Nomura,N. and Ishii,S.
  TITLE     Complex formation between proteins encoded by the ski gene family
  JOURNAL   J Biol Chem 268 (18), 13710-13716 (1993)
   PUBMED   8514802
REFERENCE   7  (residues 1 to 728)
  AUTHORS   Greally,M.T.
  TITLE     Shprintzen-Goldberg Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301454
REFERENCE   8  (residues 1 to 728)
  AUTHORS   Milewicz,D.M. and Cecchi,A.C.
  TITLE     Heritable Thoracic Aortic Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301299
REFERENCE   9  (residues 1 to 728)
  AUTHORS   Nomura,N., Sasamoto,S., Ishii,S., Date,T., Matsui,M. and
            Ishizaki,R.
  TITLE     Isolation of human cDNA clones of ski and the ski-related gene, sno
  JOURNAL   Nucleic Acids Res 17 (14), 5489-5500 (1989)
   PUBMED   2762147
REFERENCE   10 (residues 1 to 728)
  AUTHORS   Chaganti,R.S., Balazs,I., Jhanwar,S.C., Murty,V.V., Koduru,P.R.,
            Grzeschik,K.H. and Stavnezer,E.
  TITLE     The cellular homologue of the transforming gene of SKV avian
            retrovirus maps to human chromosome region 1q22----q24
  JOURNAL   Cytogenet Cell Genet 43 (3-4), 181-186 (1986)
   PUBMED   3026737
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590822.37 and X15218.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the nuclear protooncogene protein
            homolog of avian sarcoma viral (v-ski) oncogene. It functions as a
            repressor of TGF-beta signaling, and may play a role in neural tube
            development and muscle differentiation. [provided by RefSeq, Oct
            2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X15218.1, SRR14038192.3809015.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378536.5/ ENSP00000367797.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..728
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33-p36.32"
     Protein         1..728
                     /product="ski oncogene"
                     /note="ski oncoprotein; proto-oncogene c-Ski; v-ski avian
                     sarcoma viral oncogene homolog; Sloan-Kettering Institute
                     proto-oncogene"
                     /calculated_mol_wt=79874
     Region          91..192
                     /region_name="DHD_Ski"
                     /note="Dachshund-homology domain found in Ski and similar
                     proteins; cd21083"
                     /db_xref="CDD:410786"
     Region          217..311
                     /region_name="c-SKI_SMAD_bind"
                     /note="c-SKI Smad4 binding domain; pfam08782"
                     /db_xref="CDD:462602"
     Region          <318..478
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          321..357
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12755.1)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Region          452..542
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P12755.1)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     Region          538..>709
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P12755.1)"
     CDS             1..728
                     /gene="SKI"
                     /gene_synonym="SGS; SKV"
                     /coded_by="NM_003036.4:449..2635"
                     /db_xref="CCDS:CCDS39.1"
                     /db_xref="GeneID:6497"
                     /db_xref="HGNC:HGNC:10896"
                     /db_xref="MIM:164780"
ORIGIN      
        1 meaaaggrgc fqphpglqkt leqfhlssms slggpaafsa rwaqeaykke sakeagaaav
       61 papvpaatep ppvlhlpaiq ppppvlpgpf fmpsdrster cetvlegeti scfvvggekr
      121 lclpqilnsv lrdfslqqin avcdelhiyc srctadqlei lkvmgilpfs apscglitkt
      181 daerlcnall yggaypppck kelaaslalg lelsersvrv yhecfgkckg llvpelyssp
      241 saaciqcldc rlmypphkfv vhshkalenr tchwgfdsan wrayillsqd ytgkeeqarl
      301 grclddvkek fdygnkykrr vprvsseppa sirpktddts sqspapsekd kpsswlrtla
      361 gssnkslgcv hprqrlsafr pwspavsase kelsphlpal irdsfysyks fetavapnva
      421 lappaqqkvv ssppcaaavs rapeplatct qprkrkltvd tpgapetlap vaapeedkds
      481 eaevevesre eftsslssls spsftssssa kdlgspgara lpsavpdaaa padapsglea
      541 elehlrqale ggldtkeake kflhevvkmr vkqeeklsaa lqakrslhqe leflrvakke
      601 klreateakr nlrkeierlr aenekkmkea nesrlrlkre leqarqarvc dkgceagrlr
      661 akysaqiedl qvklqhaead reqlradllr erearehlek vvkelqeqlw prarpeaags
      721 egaaelep
//
LOCUS       NP_071347               1314 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF123 [Homo sapiens].
ACCESSION   NP_071347
VERSION     NP_071347.2
DBSOURCE    REFSEQ: accession NM_022064.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1314)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1314)
  AUTHORS   Gulei,D., Drula,R., Ghiaur,G., Buzoianu,A.D.,
            Kravtsova-Ivantsiv,Y., Tomuleasa,C. and Ciechanover,A.
  TITLE     The Tumor Suppressor Functions of Ubiquitin Ligase KPC1: From
            Cell-Cycle Control to NF-kappaB Regulator
  JOURNAL   Cancer Res 83 (11), 1762-1767 (2023)
   PUBMED   36880841
  REMARK    GeneRIF: The Tumor Suppressor Functions of Ubiquitin Ligase KPC1:
            From Cell-Cycle Control to NF-kappaB Regulator.
            Review article
REFERENCE   3  (residues 1 to 1314)
  AUTHORS   Goldhirsh,G., Kravtsova-Ivantsiv,Y., Satish,G., Ziv,T., Brik,A. and
            Ciechanover,A.
  TITLE     A short binding site in the KPC1 ubiquitin ligase mediates
            processing of NF-kappaB1 p105 to p50: A potential for a
            tumor-suppressive PROTAC
  JOURNAL   Proc Natl Acad Sci U S A 118 (49) (2021)
   PUBMED   34873064
  REMARK    GeneRIF: A short binding site in the KPC1 ubiquitin ligase mediates
            processing of NF-kappaB1 p105 to p50: A potential for a
            tumor-suppressive PROTAC.
REFERENCE   4  (residues 1 to 1314)
  AUTHORS   Somma,D., Kok,F.O., Kerrigan,D., Wells,C.A. and Carmody,R.J.
  TITLE     Defining the Role of Nuclear Factor (NF)-kappaB p105 Subunit in
            Human Macrophage by Transcriptomic Analysis of NFKB1 Knockout THP1
            Cells
  JOURNAL   Front Immunol 12, 669906 (2021)
   PUBMED   34721373
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1314)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1314)
  AUTHORS   Kotoshiba,S., Kamura,T., Hara,T., Ishida,N. and Nakayama,K.I.
  TITLE     Molecular dissection of the interaction between p27 and Kip1
            ubiquitylation-promoting complex, the ubiquitin ligase that
            regulates proteolysis of p27 in G1 phase
  JOURNAL   J Biol Chem 280 (18), 17694-17700 (2005)
   PUBMED   15746103
  REMARK    GeneRIF: Free p27 is recognized by the amino-terminal region of
            KPC1, which also associates with KPC2, and p27 is then
            polyubiquitylated by the carboxy-terminal RING-finger domain of
            KPC1.
REFERENCE   7  (residues 1 to 1314)
  AUTHORS   Kamura,T., Hara,T., Matsumoto,M., Ishida,N., Okumura,F.,
            Hatakeyama,S., Yoshida,M., Nakayama,K. and Nakayama,K.I.
  TITLE     Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
            at G1 phase
  JOURNAL   Nat Cell Biol 6 (12), 1229-1235 (2004)
   PUBMED   15531880
  REMARK    GeneRIF: KPC thus probably controls degradation of p27(Kip1) in G1
            phase after export of the latter from the nucleus
REFERENCE   8  (residues 1 to 1314)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   9  (residues 1 to 1314)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
REFERENCE   10 (residues 1 to 1314)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI596589.1, BC130632.1,
            AC099668.2 and BC088801.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 8, 2003 this sequence version replaced NP_071347.1.
            
            Summary: The protein encoded by this gene contains a C-terminal
            RING finger domain, a motif present in a variety of functionally
            distinct proteins and known to be involved in protein-protein and
            protein-DNA interactions, and an N-terminal SPRY domain. This
            protein displays E3 ubiquitin ligase activity toward the
            cyclin-dependent kinase inhibitor 1B which is also known as p27 or
            KIP1. Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL832034.1, AL832344.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327697.11/ ENSP00000328287.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1314
                     /product="E3 ubiquitin-protein ligase RNF123"
                     /EC_number="2.3.2.27"
                     /note="kip1 ubiquitination-promoting complex protein 1;
                     Kip1 ubiquitination-promoting complex subunit 1; RING-type
                     E3 ubiquitin transferase RNF123"
                     /calculated_mol_wt=148384
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q5XPI4.1)"
     Region          123..250
                     /region_name="SPRY_RNF123"
                     /note="SPRY domain at N-terminus of ring finger protein
                     123; cd12882"
                     /db_xref="CDD:293940"
     Site            675
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3ZXK7; propagated from
                     UniProtKB/Swiss-Prot (Q5XPI4.1)"
     Site            683
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q5XPI3; propagated from
                     UniProtKB/Swiss-Prot (Q5XPI4.1)"
     Region          968..974
                     /region_name="Interaction with NFKB1.
                     /evidence=ECO:0000269|PubMed:34873064"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XPI4.1)"
     Region          1252..1295
                     /region_name="RING-HC_RNF123"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 123 (RNF123) and similar proteins; cd16541"
                     /db_xref="CDD:438203"
     CDS             1..1314
                     /gene="RNF123"
                     /gene_synonym="FP1477; KPC1"
                     /coded_by="NM_022064.5:87..4031"
                     /db_xref="CCDS:CCDS33758.1"
                     /db_xref="GeneID:63891"
                     /db_xref="HGNC:HGNC:21148"
                     /db_xref="MIM:614472"
ORIGIN      
        1 maskgagmsf srksyrltsd aeksrvtgiv qekllndyln rifsssehap paatsrkpln
       61 fqnlpehldq llqvdneeee sqgqvegrlg pstvvldhtg gfeglllvdd dllgvighsn
      121 fgtirsttcv ykgkwlyevl issqglmqig wctiscrfnq eegvgdthns yaydgnrvrk
      181 wnvtttnygk awaagdivsc lidlddgtls fclngvslgt afenlsrglg mayfpaisls
      241 fkesvafnfg srplrypvag yrplqdppsa dlvraqrllg cfravlsvel dpvegrlldk
      301 esskwrlrgq ptvlltlahi fhhfapllrk vylveavlms fllgivekgt ptqaqsvvhq
      361 vldllwlfme dyevqdclkq lmmsllrlyr fspivpdlgl qihylrltia ilrheksrkf
      421 llsnvlfdvl rsvvffyiks plrveeaglq elipttwwph cssregkest emkeetaeer
      481 lrrrayergc qrlrkrievv eelqvqilkl lldnkddngg easryifltk frkflqenas
      541 grgnmpmlcp peymvcflhr lisalryywd eykasnphas fseeayippq vfyngkvdyf
      601 dlqrlgglls hlrktlkddl askanividp lelqstamdd ldedeepapa maqrpmqala
      661 vggplplprp gwlssptlgr anrflstaav slmtprrpls tsekvkvrtl sveqrtredi
      721 egshwnegll lgrppeepeq pltensllev ldgavmmynl svhqqlgkmv gvsddvneya
      781 malrdtedkl rrcpkrrkdi laeltksqkv fsekldhlsr rlawvhatvy sqekmldiyw
      841 llrvclrtie hgdrtgslfa fmpefylsva insysalkny fgpvhsmeel pgyeetltrl
      901 aailakhfad arivgtdird slmqalasyv cyphslrave ripeeqriam vrnllapyeq
      961 rpwaqtnwil vrlwrgcgfg yrytrlphll ktkledanlp slqkpcpstl lqqhmadllq
     1021 qgpdvapsfl nsvlnqlnwa fsefigmiqe iqqaaerler nfvdsrqlkv catcfdlsvs
     1081 llrvlemtit lvpeifldwt rptsemllrr laqllnqvln rvtaernlfd rvvtlrlpgl
     1141 esvdhypilv avtgilvqll vrgpasereq atsvlladpc fqlrsicyll gqpeppapgt
     1201 alpapdrkrf slqsyadyis adelaqveqm lahltsasaq aaaaslptse edlcpicyah
     1261 pisavfqpcg hksckacinq hlmnnkdcff ckttivsved wekgantstt ssaa
//
LOCUS       NP_683702                558 aa            linear   PRI 20-NOV-2025
DEFINITION  oxysterol-binding protein-related protein 9 isoform a [Homo
            sapiens].
ACCESSION   NP_683702
VERSION     NP_683702.1
DBSOURCE    REFSEQ: accession NM_148904.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 558)
  AUTHORS   Cabukusta,B., Borst Pauwels,S., Akkermans,J.J.L.L., Blomberg,N.,
            Mulder,A.A., Koning,R.I., Giera,M. and Neefjes,J.
  TITLE     The ORP9-ORP11 dimer promotes sphingomyelin synthesis
  JOURNAL   Elife 12, 91345 (2024)
   PUBMED   39106189
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 558)
  AUTHORS   He,R., Liu,F., Wang,H., Huang,S., Xu,K., Zhang,C., Liu,Y. and Yu,H.
  TITLE     ORP9 and ORP10 form a heterocomplex to transfer
            phosphatidylinositol 4-phosphate at ER-TGN contact sites
  JOURNAL   Cell Mol Life Sci 80 (3), 77 (2023)
   PUBMED   36853333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 558)
  AUTHORS   Tan,J.X. and Finkel,T.
  TITLE     A phosphoinositide signalling pathway mediates rapid lysosomal
            repair
  JOURNAL   Nature 609 (7928), 815-821 (2022)
   PUBMED   36071159
REFERENCE   4  (residues 1 to 558)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 558)
  AUTHORS   Hacker,B., Schultheiss,C., Doring,M. and Kurzik-Dumke,U.
  TITLE     Molecular partners of hNOT/ALG3, the human counterpart of the
            Drosophila NOT and yeast ALG3 gene, suggest its involvement in
            distinct cellular processes relevant to congenital disorders of
            glycosylation, cancer, neurodegeneration and a variety of further
            pathologies
  JOURNAL   Hum Mol Genet 27 (11), 1858-1878 (2018)
   PUBMED   29547901
REFERENCE   6  (residues 1 to 558)
  AUTHORS   Gauci,S., Helbig,A.O., Slijper,M., Krijgsveld,J., Heck,A.J. and
            Mohammed,S.
  TITLE     Lys-N and trypsin cover complementary parts of the phosphoproteome
            in a refined SCX-based approach
  JOURNAL   Anal Chem 81 (11), 4493-4501 (2009)
   PUBMED   19413330
  REMARK    GeneRIF: Includes data showing N-alpha terminal acetylation of this
            protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following
            cleavage of the initiating Met-1 residue.
REFERENCE   7  (residues 1 to 558)
  AUTHORS   Lessmann,E., Ngo,M., Leitges,M., Minguet,S., Ridgway,N.D. and
            Huber,M.
  TITLE     Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2
            substrate and regulates Akt phosphorylation
  JOURNAL   Cell Signal 19 (2), 384-392 (2007)
   PUBMED   16962287
  REMARK    GeneRIF: Furthermore, mammalian target of rapamycin was implicated
            in ORP9L phosphorylation in HEK293 cells. These studies identify
            ORP9 as a PDK-2 substrate and negative regulator of Akt
            phosphorylation at the PDK-2 site.
REFERENCE   8  (residues 1 to 558)
  AUTHORS   Wyles,J.P. and Ridgway,N.D.
  TITLE     VAMP-associated protein-A regulates partitioning of
            oxysterol-binding protein-related protein-9 between the endoplasmic
            reticulum and Golgi apparatus
  JOURNAL   Exp Cell Res 297 (2), 533-547 (2004)
   PUBMED   15212954
REFERENCE   9  (residues 1 to 558)
  AUTHORS   Jaworski,C.J., Moreira,E., Li,A., Lee,R. and Rodriguez,I.R.
  TITLE     A family of 12 human genes containing oxysterol-binding domains
  JOURNAL   Genomics 78 (3), 185-196 (2001)
   PUBMED   11735225
REFERENCE   10 (residues 1 to 558)
  AUTHORS   Lehto,M., Laitinen,S., Chinetti,G., Johansson,M., Ehnholm,C.,
            Staels,B., Ikonen,E. and Olkkonen,V.M.
  TITLE     The OSBP-related protein family in humans
  JOURNAL   J Lipid Res 42 (8), 1203-1213 (2001)
   PUBMED   11483621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ230093.1, BC025978.2,
            AL050343.17 and EL953716.1.
            
            Summary: This gene encodes a member of the oxysterol-binding
            protein (OSBP) family, a group of intracellular lipid receptors.
            Most members contain an N-terminal pleckstrin homology domain and a
            highly conserved C-terminal OSBP-like sterol-binding domain,
            although some members contain only the sterol-binding domain. This
            family member functions as a cholesterol transfer protein that
            regulates Golgi structure and function. Multiple transcript
            variants, most of which encode distinct isoforms, have been
            identified. Related pseudogenes have been identified on chromosomes
            3, 11 and 12. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) encodes the shortest isoform
            (a), which contains a sterol-binding domain, but not a pleckstrin
            homology domain. Both variants 1 and 2 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.183768.1, BC025978.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..558
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32.3"
     Protein         1..558
                     /product="oxysterol-binding protein-related protein 9
                     isoform a"
                     /note="oxysterol-binding protein-related protein 9;
                     OSBP-related protein 9"
                     /calculated_mol_wt=62397
     Region          199..545
                     /region_name="Oxysterol_BP"
                     /note="Oxysterol-binding protein; pfam01237"
                     /db_xref="CDD:460126"
     CDS             1..558
                     /gene="OSBPL9"
                     /gene_synonym="ORP-9; ORP9"
                     /coded_by="NM_148904.4:453..2129"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41334.1"
                     /db_xref="GeneID:114883"
                     /db_xref="HGNC:HGNC:16386"
                     /db_xref="MIM:606737"
ORIGIN      
        1 mvesikhciv llqiakstin pvdaiyqpsp lepvistmps qtvlppepvq lckseqrpss
       61 lpvgpvlatl ghhqtptpns tgsghsppss sltspshvnl spntvpefsy sssedefyda
      121 defhqsgssp krlidssgsa svlthsssgn slkrpdttes lnsslsngts dadlfdshdd
      181 rdddaeagsv eehksvimhl lsqvrlgmdl tkvvlptfil errsllemya dffahpdlfv
      241 sisdqkdpkd rmvqvvkwyl safhagrkgs vakkpynpil geifqchwtl pndteentel
      301 vsegpvpwvs knsvtfvaeq vshhppisaf yaecfnkkiq fnahiwtksk flgmsigvhn
      361 igqgcvscld ydehyiltfp ngygrsiltv pwvelggecn incsktgysa niifhtkpfy
      421 ggkkhritae ifspndkksf csiegewngv myakyatgen tvfvdtkklp iikkkvrkle
      481 dqneyesrsl wkdvtfnlki rdidaateak hrleerqrae arerkekeiq wetrlfhedg
      541 ecwvydepll krlgaakh
//
LOCUS       NP_001355326            1762 aa            linear   PRI 20-NOV-2025
DEFINITION  FERM and PDZ domain-containing protein 4 isoform c [Homo sapiens].
ACCESSION   NP_001355326 XP_011543915
VERSION     NP_001355326.1
DBSOURCE    REFSEQ: accession NM_001368397.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1762)
  AUTHORS   Li,R.K., Li,H., Tian,M.Q., Li,Y., Luo,S., Liang,X.Y., Liu,W.H.,
            Li,B.M., Shi,X.Q., Li,J., Li,B. and Shu,X.M.
  CONSRTM   China Epilepsy Gene 1.0 Project
  TITLE     Investigation of FRMPD4 variants associated with X-linked epilepsy
  JOURNAL   Seizure 116, 45-50 (2024)
   PUBMED   37330374
  REMARK    GeneRIF: Investigation of FRMPD4 variants associated with X-linked
            epilepsy.
REFERENCE   2  (residues 1 to 1762)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1762)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 1762)
  AUTHORS   Wang,M., Lin,L., Shi,Y., He,L., Wang,C. and Zhu,J.
  TITLE     Structure of the FERM domain of a neural scaffold protein FRMPD4
            implicated in X-linked intellectual disability
  JOURNAL   Biochem J 477 (23), 4623-4634 (2020)
   PUBMED   33216857
  REMARK    GeneRIF: Structure of the FERM domain of a neural scaffold protein
            FRMPD4 implicated in X-linked intellectual disability.
REFERENCE   5  (residues 1 to 1762)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1762)
  AUTHORS   Yuzawa,S., Kamakura,S., Iwakiri,Y., Hayase,J. and Sumimoto,H.
  TITLE     Structural basis for interaction between the conserved cell
            polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched
            protein (LGN)
  JOURNAL   Proc Natl Acad Sci U S A 108 (48), 19210-19215 (2011)
   PUBMED   22074847
REFERENCE   7  (residues 1 to 1762)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 1762)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 1762)
  AUTHORS   Lee,H.W., Choi,J., Shin,H., Kim,K., Yang,J., Na,M., Choi,S.Y.,
            Kang,G.B., Eom,S.H., Kim,H. and Kim,E.
  TITLE     Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
            regulates dendritic spine morphogenesis
  JOURNAL   J Neurosci 28 (53), 14546-14556 (2008)
   PUBMED   19118189
  REMARK    GeneRIF: Preso positively regulates spine density through its
            interaction with the synaptic plasma membrane, actin filaments,
            PSD-95, and the betaPix-based Rac1 signaling pathway.
REFERENCE   10 (residues 1 to 1762)
  AUTHORS   Nakayama,M., Kikuno,R. and Ohara,O.
  TITLE     Protein-protein interactions between large proteins: two-hybrid
            screening using a functionally classified library composed of long
            cDNAs
  JOURNAL   Genome Res 12 (11), 1773-1784 (2002)
   PUBMED   12421765
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002981.1, AC112499.8,
            AC119619.5 and AC112655.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 9, 2019 this sequence version replaced XP_011543915.1.
            
            Summary: This gene encodes a multi-domain (WW, PDZ, FERM)
            containing protein. Through its interaction with other proteins
            (such as PSD-95), it functions as a positive regulator of dendritic
            spine morphogenesis and density, and is required for the
            maintenance of excitatory synaptic transmission. [provided by
            RefSeq, Jan 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2145743,
                              SAMEA2154665 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000675598.1/ ENSP00000502607.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1762
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..1762
                     /product="FERM and PDZ domain-containing protein 4 isoform
                     c"
                     /note="PSD-95-interacting FERM and PDZ domain protein;
                     Preso; PDZ domain-containing protein 10;
                     PSD-95-interacting regulator of spine morphogenesis"
                     /calculated_mol_wt=193012
     Region          36..66
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(50,61)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          78..152
                     /region_name="PDZ_FRMPD1_3_4-like"
                     /note="PDZ domain of FERM and PDZ domain-containing
                     protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains;
                     cd06769"
                     /db_xref="CDD:467250"
     Site            order(88..94,102,105,133,137,140..141)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467250"
     Region          201..294
                     /region_name="FERM_F1_FRMPD4"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F1 sub-domain, found in FERM and PDZ
                     domain-containing protein 4 (FRMPD4); cd17170"
                     /db_xref="CDD:340690"
     Region          205..424
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          420..524
                     /region_name="FERM_C_FRMPD1_FRMPD3_FRMPD4"
                     /note="FERM domain C-lobe of FERM and PDZ domain
                     containing proteins 1, 3, and 4 (FRMPD1, 3, 4); cd13183"
                     /db_xref="CDD:270004"
     Site            order(428,449,451,459)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270004"
     Site            order(463,469..472,505,509,512..513)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Site            505..516
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270004"
     Region          809..847
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          900..927
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          952..983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          975..1023
                     /region_name="LGNbd_FRMPD4"
                     /note="LGN tetratricopeptide repeat-binding domain found
                     in FERM and PDZ domain-containing protein 4; cd21943"
                     /db_xref="CDD:409274"
     Site            order(988..992,994..1010,1012)
                     /site_type="other"
                     /note="TPR binding site [polypeptide binding]"
                     /db_xref="CDD:409274"
     Region          1027..1080
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1105..1148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1160..1180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     Region          1207..1227
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14CM0.1)"
     CDS             1..1762
                     /gene="FRMPD4"
                     /gene_synonym="MRX104; PDZD10; PDZK10; XLID104"
                     /coded_by="NM_001368397.1:500..5788"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS94551.1"
                     /db_xref="GeneID:9758"
                     /db_xref="HGNC:HGNC:29007"
                     /db_xref="MIM:300838"
ORIGIN      
        1 mdvfsfvkia klsshrtkss gwpppsgtwg lsqvppygwe mtanrdgrdy finhmtqaip
       61 fddprlescq iippaprkve mrrdpvlgfg fvagsekpvv vrsvtpggps egklipgdqi
      121 vmindepvsa aprervidlv rsckesillt viqpypspks afisaakkar lksnpvkvrf
      181 seeviingqv setvkdnsll fmpnvlkvyl engqtksfrf dcstsikdvi ltlqeklsik
      241 giehfslmle qrtegagtkl lllheqetlt qvtqrpsshk mrclfrisfv pkdpidllrr
      301 dpvafeylyv qscndvvqer fgpelkydia lrlaalqmyi atvttkqtqk islkyiekew
      361 gletflpsav lqsmkeknik kalshlvkan qnlvppgkkl salqakvhyl kflsdlrlyg
      421 grvfkatlvq aekrsevtll vgprygishv intktnlval ladfshvnri emfseeeslv
      481 rvelhvldvk pitllmessd amnlacltag yyrllvdsrr sifnmankkn tatqetgpen
      541 kgkhnllgpd wncipqmttf igegeqeaqi tyidskqktv eitdstmcpk ehrhlyidna
      601 yssdglnqql sqpgeapcea dyrslaqrsl ltlsgpetlk kaqesprgak vsfifgdfal
      661 ddgispptlg yetlldegpe mlekqrnlyi gsandmkgld ltpeaegiqf vensvyanig
      721 dvksfqaaeg ieepllhdic yaentddaed edevsceedl vvgemnqpai lnlsgssddi
      781 idltslpppe gddneddfll rslnmaiaap ppgfrdssde edsqsqaasf pedkekgssl
      841 qndeipvsli davptsaegk cekgldnavv stlgaleals vseeqqtsdn sgvailrays
      901 pesssdsgne tnssemtess elataqkqse nlsrmflath egyhplaeeq tefpasktpa
      961 gglppkssha laarpatdlp pkvvpskqll hsdhmemepe tmetksvtdy fsklhmgsva
     1021 ysctskrksk ladgegkapp ngnttgkkqq gtktaemeee asgkfgtvss rdsqhlstfn
     1081 lertafrkds qrwyvategg maeksgleaa tgktfprasg lgareaegke egapdgetsd
     1141 gsglgqgdrf ltdvtcassa kdldnpedad sstcdhpskl peadesvarl cdyhlakrms
     1201 slqseghfsl qssqgssvda gcgtgssgsa catpvesplc pslgkhlipd asgkgvnyip
     1261 seerapglpn hgatfkelhp qtegmcprmt vpalhtaint eplfgtlrdg chrlpkiket
     1321 taltepgker rggmpsawsq hpeadpillp snihseskvp ipnqdpndfs qanqaygeav
     1381 swrppdlrgg slrtppsqka lrhsssilsg svdletfrer tkgavslkcp giteaqeass
     1441 erraelplgr kltksfsqss mhlssegrfh krspvahkds klyrtlplrk legsnwrcrg
     1501 pfsycflnrg qdedgeeeee rgeatvqvsc lyrpqmtqam pepsspclav aiqkqrgels
     1561 rgsvlkvwae dlrdpddldf snlafdaria rinalkesty ampdgflaaq ndanellclv
     1621 ratkekrees rpeaydltls qykqllsies rqlgsacrkm amaekspeem llamtssfqv
     1681 lcclteacmr lvkvvnsetq rqeivgkide vvinyicllk aaeaatgknp gdpnvglsar
     1741 hsttmaalvs tltrslkrll nk
//
LOCUS       NP_001350475             634 aa            linear   PRI 20-NOV-2025
DEFINITION  N-acetylmuramoyl-L-alanine amidase isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001350475 XP_006722696
VERSION     NP_001350475.1
DBSOURCE    REFSEQ: accession NM_001363546.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 634)
  AUTHORS   Li,Y., Ma,H., Zhang,Y., He,T., Li,B., Ren,H., Feng,J., Sheng,J.,
            Li,K., Qian,Y., Wang,Y., Zhao,H., He,J., Li,H., Wu,H., Yao,Y. and
            Shi,M.
  TITLE     PGLYRP2 drives hepatocyte-intrinsic innate immunity by trapping and
            clearing hepatitis B virus
  JOURNAL   J Clin Invest 135 (8), e188083 (2025)
   PUBMED   39946201
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 634)
  AUTHORS   Luan,M., Jin,J., Wang,Y., Li,X. and Xie,A.
  TITLE     Association of PGLYRP2 gene polymorphism and sporadic Parkinson's
            disease in northern Chinese Han population
  JOURNAL   Neurosci Lett 775, 136547 (2022)
   PUBMED   35218888
  REMARK    GeneRIF: Association of PGLYRP2 gene polymorphism and sporadic
            Parkinson's disease in northern Chinese Han population.
REFERENCE   3  (residues 1 to 634)
  AUTHORS   Huang,F., Liu,X., Cheng,Y., Sun,X., Li,Y., Zhao,J., Cao,D., Wu,Q.,
            Pan,X., Deng,H., Tian,M. and Li,Z.
  TITLE     Antibody to peptidoglycan recognition protein (PGLYRP)-2 as a novel
            biomarker in rheumatoid arthritis
  JOURNAL   Clin Exp Rheumatol 39 (5), 988-994 (2021)
   PUBMED   33427621
  REMARK    GeneRIF: Antibody to peptidoglycan recognition protein (PGLYRP)-2
            as a novel biomarker in rheumatoid arthritis.
REFERENCE   4  (residues 1 to 634)
  AUTHORS   Li,H., Meng,D., Jia,J. and Wei,H.
  TITLE     PGLYRP2 as a novel biomarker for the activity and lipid metabolism
            of systemic lupus erythematosus
  JOURNAL   Lipids Health Dis 20 (1), 95 (2021)
   PUBMED   34461924
  REMARK    GeneRIF: PGLYRP2 as a novel biomarker for the activity and lipid
            metabolism of systemic lupus erythematosus.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 634)
  AUTHORS   Chen,J., Han,Y.S., Yi,W.J., Huang,H., Li,Z.B., Shi,L.Y., Wei,L.L.,
            Yu,Y., Jiang,T.T. and Li,J.C.
  TITLE     Serum sCD14, PGLYRP2 and FGA as potential biomarkers for
            multidrug-resistant tuberculosis based on data-independent
            acquisition and targeted proteomics
  JOURNAL   J Cell Mol Med 24 (21), 12537-12549 (2020)
   PUBMED   32967043
  REMARK    GeneRIF: Serum sCD14, PGLYRP2 and FGA as potential biomarkers for
            multidrug-resistant tuberculosis based on data-independent
            acquisition and targeted proteomics.
REFERENCE   6  (residues 1 to 634)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 634)
  AUTHORS   Zhang,H., Li,X.J., Martin,D.B. and Aebersold,R.
  TITLE     Identification and quantification of N-linked glycoproteins using
            hydrazide chemistry, stable isotope labeling and mass spectrometry
  JOURNAL   Nat Biotechnol 21 (6), 660-666 (2003)
   PUBMED   12754519
REFERENCE   8  (residues 1 to 634)
  AUTHORS   Kibardin,A.V., Mirkina,I.I., Zakeeva,I.R., Baranova,E.V.,
            Georgiev,G.P. and Kiselev,S.L.
  TITLE     [Expression analysis of proteins encoded by genes of the tag7/tagL
            (PGRP-S,L) family in human peripheral blood cells]
  JOURNAL   Genetika 39 (2), 244-249 (2003)
   PUBMED   12669421
  REMARK    GeneRIF: Various types of human blood cells were tested for
            expression of the Tag7/PGRP-SA and TagL/PGRP-L proteins, which
            belong to the family of proteins possessing the lysozyme-like
            peptidoglycan recognition protein (PGRP) domain
REFERENCE   9  (residues 1 to 634)
  AUTHORS   Liu,C., Xu,Z., Gupta,D. and Dziarski,R.
  TITLE     Peptidoglycan recognition proteins: a novel family of four human
            innate immunity pattern recognition molecules
  JOURNAL   J Biol Chem 276 (37), 34686-34694 (2001)
   PUBMED   11461926
REFERENCE   10 (residues 1 to 634)
  AUTHORS   De Pauw,P., Neyt,C., Vanderwinkel,E., Wattiez,R. and Falmagne,P.
  TITLE     Characterization of human serum N-acetylmuramyl-L-alanine amidase
            purified by affinity chromatography
  JOURNAL   Protein Expr Purif 6 (3), 371-378 (1995)
   PUBMED   7663175
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK055882.1, BC144238.1 and AY358156.1.
            
            On May 24, 2018 this sequence version replaced XP_006722696.1.
            
            Summary: This gene encodes a peptidoglycan recognition protein,
            which belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
            This protein hydrolyzes the link between N-acetylmuramoyl residues
            and L-amino acid residues in bacterial cell wall glycopeptides, and
            thus may play a scavenger role by digesting biologically active
            peptidoglycan into biologically inactive fragments. [provided by
            RefSeq, Sep 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055882.1, BC136551.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMN04284274
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..634
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.12"
     Protein         1..634
                     /product="N-acetylmuramoyl-L-alanine amidase isoform 2
                     precursor"
                     /EC_number="3.5.1.28"
                     /note="peptidoglycan recognition protein L;
                     N-acetylmuramoyl-L-alanine amidase; peptidoglycan
                     recognition protein long"
                     /calculated_mol_wt=65677
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2342
     Region          380..525
                     /region_name="PGRP"
                     /note="Animal peptidoglycan recognition proteins
                     homologous to Bacteriophage T3 lysozyme; smart00701"
                     /db_xref="CDD:128941"
     Site            order(410,447,522,528,530)
                     /site_type="active"
                     /note="amidase catalytic site [active]"
                     /db_xref="CDD:133475"
     Site            order(410,522,530)
                     /site_type="other"
                     /note="Zn binding residues [ion binding]"
                     /db_xref="CDD:133475"
     Site            order(411..412,443,447,461,468..469,474,522,526,528..530)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:133475"
     CDS             1..634
                     /gene="PGLYRP2"
                     /gene_synonym="HMFT0141; PGLYRPL; PGRP-L; PGRPL; tagL;
                     tagL-alpha; tagl-beta; TAGL-like"
                     /coded_by="NM_001363546.1:131..2035"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS86718.1"
                     /db_xref="GeneID:114770"
                     /db_xref="HGNC:HGNC:30013"
                     /db_xref="MIM:608199"
ORIGIN      
        1 maqgvlwill glllwsdpgt aslpllmdsv iqalaeleqk vpaaktrhta sawlmsapns
       61 gphnrlyhfl lgawslnate ldpcplspel lgltkevarh dvregkeygv vlapdgstva
      121 vepllaglea glqgrrvinl pldsmaapwe tgdtfpdvva iapdvratss pglrdgspdv
      181 ttadigantp datkgcpdvq aslpdakaks pptmvdslla vtlagnlglt flrgsqtqsh
      241 pdlgtegcwd qlsaprtftl ldpkaslltm aflngaldgv ilgdylsrtp eprpslshll
      301 sqyygagvar dpgfrsnfrr qngaaltsas ilaqqvwgtl vllqrlepvh lqlqcmsqeq
      361 laqvaanatk efteaflgcp aihprcrwga apyrgrpkll qlplgflyvh htyvpappct
      421 dftrcaanmr smqryhqdtq gwgdigysfv vgsdgyvyeg rgwhwvgaht lghnsrgfgv
      481 aivgnytaal pteaalrtvr dtlpscavra gllrpdyall ghrqlvrtdc pgdalfdllr
      541 twphftavsl rslhytarrp svytsstrpl ppacnscart asarpptsrr hvysgnlgpa
      601 faghsagnip dpvtsayaas aqpqtqpacp fpss
//
LOCUS       NP_689931                955 aa            linear   PRI 20-NOV-2025
DEFINITION  von Willebrand factor C and EGF domain-containing protein precursor
            [Homo sapiens].
ACCESSION   NP_689931
VERSION     NP_689931.2
DBSOURCE    REFSEQ: accession NM_152718.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 955)
  AUTHORS   Sun,C., Zhang,G., Cheng,S., Qian,H., Li,D. and Liu,M.
  TITLE     URG11 promotes proliferation and induced apoptosis of LNCaP cells
  JOURNAL   Int J Mol Med 43 (5), 2075-2085 (2019)
   PUBMED   30864678
  REMARK    GeneRIF: URG11 served an oncogenic role in the development of
            prostate cancer cells.
REFERENCE   5  (residues 1 to 955)
  AUTHORS   Pan,B., Ye,Y., Liu,H., Zhen,J., Zhou,H., Li,Y., Qu,L., Wu,Y.,
            Zeng,C. and Zhong,W.
  TITLE     URG11 Regulates Prostate Cancer Cell Proliferation, Migration, and
            Invasion
  JOURNAL   Biomed Res Int 2018, 4060728 (2018)
   PUBMED   29955600
  REMARK    GeneRIF: URG11 is critical for the proliferation, migration, and
            invasion in prostate cancer cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 955)
  AUTHORS   Du,R., Xia,L., Sun,S., Lian,Z., Zou,X., Gao,J., Xie,H., Fan,R.,
            Song,J., Li,X., Liu,J. and Fan,D.
  TITLE     URG11 promotes gastric cancer growth and invasion by activation of
            beta-catenin signalling pathway
  JOURNAL   J Cell Mol Med 14 (3), 621-635 (2010)
   PUBMED   19413886
  REMARK    GeneRIF: Data suggest that URG11 contributes to gastric cancer
            growth and metastasis at least partially through activation of
            beta-catenin signalling pathway.
REFERENCE   7  (residues 1 to 955)
  AUTHORS   Du,R., Huang,C., Bi,Q., Zhai,Y., Xia,L., Liu,J., Sun,S. and Fan,D.
  TITLE     URG11 mediates hypoxia-induced epithelial-to-mesenchymal transition
            by modulation of E-cadherin and beta-catenin
  JOURNAL   Biochem Biophys Res Commun 391 (1), 135-141 (2010)
   PUBMED   19900406
  REMARK    GeneRIF: URG11 mediates hypoxia-induced epithelial-to-mesenchymal
            transition through the suppression of E-cadherin and the activation
            of the beta-catenin/T-cell factor pathway.
REFERENCE   8  (residues 1 to 955)
  AUTHORS   Lian,Z., Liu,J., Li,L., Li,X., Clayton,M., Wu,M.C., Wang,H.Y.,
            Arbuthnot,P., Kew,M., Fan,D. and Feitelson,M.A.
  TITLE     Enhanced cell survival of Hep3B cells by the hepatitis B x antigen
            effector, URG11, is associated with upregulation of beta-catenin
  JOURNAL   Hepatology 43 (3), 415-424 (2006)
   PUBMED   16496348
  REMARK    GeneRIF: beta-catenin is activated by HBxAg, in part, through the
            upregulated expression of the HBxAg effector URG11; URG11
            stimulates the beta-catenin promoter and hepatocellular growth and
            survival
REFERENCE   9  (residues 1 to 955)
  AUTHORS   Lian,Z., Liu,J., Li,L., Li,X., Tufan,N.L., Clayton,M., Wu,M.C.,
            Wang,H.Y., Arbuthnot,P., Kew,M. and Feitelson,M.A.
  TITLE     Upregulated expression of a unique gene by hepatitis B x antigen
            promotes hepatocellular growth and tumorigenesis
  JOURNAL   Neoplasia 5 (3), 229-244 (2003)
   PUBMED   12869306
REFERENCE   10 (residues 1 to 955)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
   PUBMED   7566098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB126089.1, AK056571.1, AP003037.2 and AA328361.1.
            
            On Sep 15, 2006 this sequence version replaced NP_689931.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056571.1, BC142624.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335613.10/ ENSP00000334186.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.2"
     Protein         1..955
                     /product="von Willebrand factor C and EGF
                     domain-containing protein precursor"
                     /note="von Willebrand factor C and EGF domain-containing
                     protein; HBxAg up-regulated gene 11 protein; HBV X protein
                     up-regulated gene 11 protein"
                     /calculated_mol_wt=97826
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DN2.2)"
                     /calculated_mol_wt=2108
     mat_peptide     22..955
                     /product="von Willebrand factor C and EGF
                     domain-containing protein. /id=PRO_0000318580"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN2.2)"
                     /calculated_mol_wt=97826
     Region          142..180
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Region          190..218
                     /region_name="FXa_inhibition"
                     /note="Coagulation Factor Xa inhibitory site; pfam14670"
                     /db_xref="CDD:464251"
     Region          220..262
                     /region_name="EGF_CA"
                     /note="Calcium-binding EGF-like domain; smart00179"
                     /db_xref="CDD:214542"
     Site            order(220,223,239)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:238011"
     Region          292..329
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN2.2)"
     Region          360..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN2.2)"
     Region          386..440
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          443..>488
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Site            462
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DN2.2)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96DN2.2)"
     Region          501..559
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          572..625
                     /region_name="VWC"
                     /note="von Willebrand factor (vWF) type C domain;
                     smart00214"
                     /db_xref="CDD:214564"
     Region          629..684
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          687..742
                     /region_name="VWC"
                     /note="von Willebrand factor type C domain; cl17735"
                     /db_xref="CDD:450195"
     Region          <726..944
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          812..889
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN2.2)"
     Region          903..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96DN2.2)"
     CDS             1..955
                     /gene="VWCE"
                     /gene_synonym="URG11; VWC1"
                     /coded_by="NM_152718.2:280..3147"
                     /db_xref="CCDS:CCDS8002.1"
                     /db_xref="GeneID:220001"
                     /db_xref="HGNC:HGNC:26487"
                     /db_xref="MIM:611115"
ORIGIN      
        1 mwaglllraa cvalllpgap argytgrkpp ghfaaerrrl gphvclsgfg sgccpgwaps
       61 mggghctlpl csfgcgsgic iapnvcscqd geqgatcpet hgpcgeygcd ltcnhggcqe
      121 varvcpvgfs mtetavgirc tdidecvtss ceghcvnteg gfvcecgpgm qlsadrhscq
      181 dtdeclgtpc qqrcknsigs ykcscrtgfh lhgnrhscvd vnecrrpler rvchhschnt
      241 vgsflctcrp gfrlradrvs ceafpkavla psailqprqh pskmllllpe agrpalspgh
      301 sppsgapgpp agvrttrlps ptprlptssp sapvwllstl latpvptasl lgnlrppsll
      361 qgevmgtpss prgpesprla agpspcwhlg amhesrsrwt epgcsqcwce dgkvtcekvr
      421 ceaacshpip srdggccpsc tgcfhsgvvr aegdvfsppn enctvcvcla gnvscispec
      481 psgpcqtppq tdcctcvpvr cyfhgrwyad gavfsgggde cttcvcqnge vecsfmpcpe
      541 lacpreewrl gpgqccftcq eptpstgcsl ddngvefpig qiwspgdpce lcicqadgsv
      601 sckrtdcvds cphpiripgq ccpdcsagct ytgrifynne tfpsvldpcl scicllgsva
      661 cspvdcpitc typfhpdgec cpvcrdcnye grkvangqvf tlddepctrc tcqlgevsce
      721 kvpcqracad pallpgdccs scpdslsple ekqglsphgn vafskagrsl hgdteapvnc
      781 sscpgpptas psrpvlhllq lllrtnlmkt qtlptspaga hgphslalgl tatfpgepga
      841 sprlspgpst ppgaptlpla spgapqpppv tpersfsasg aqivsrwppl pgtllteasa
      901 lsmmdpspsk tpitllgprv lspttsrlst alaatthpgp qqppvgasrg eestm
//
LOCUS       NP_060640                312 aa            linear   PRI 20-NOV-2025
DEFINITION  regulation of nuclear pre-mRNA domain-containing protein 1A isoform
            1 [Homo sapiens].
ACCESSION   NP_060640
VERSION     NP_060640.2
DBSOURCE    REFSEQ: accession NM_018170.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Feng,X., Jiang,T., Yang,C., Pang,S., Ding,Z., Hu,H., Wang,H.,
            Dong,L. and Yang,N.
  TITLE     RPRD1A stabilizes NRF2 and aggravates HCC progression through
            competing with p62 for TRIM21 binding
  JOURNAL   Cell Death Dis 13 (1), 6 (2021)
   PUBMED   34921137
  REMARK    GeneRIF: RPRD1A stabilizes NRF2 and aggravates HCC progression
            through competing with p62 for TRIM21 binding.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Behr,E.R., Ritchie,M.D., Tanaka,T., Kaab,S., Crawford,D.C.,
            Nicoletti,P., Floratos,A., Sinner,M.F., Kannankeril,P.J.,
            Wilde,A.A., Bezzina,C.R., Schulze-Bahr,E., Zumhagen,S.,
            Guicheney,P., Bishopric,N.H., Marshall,V., Shakir,S.,
            Dalageorgou,C., Bevan,S., Jamshidi,Y., Bastiaenen,R.,
            Myerburg,R.J., Schott,J.J., Camm,A.J., Steinbeck,G., Norris,K.,
            Altman,R.B., Tatonetti,N.P., Jeffery,S., Kubo,M., Nakamura,Y.,
            Shen,Y., George,A.L. Jr. and Roden,D.M.
  TITLE     Genome wide analysis of drug-induced torsades de pointes: lack of
            common variants with large effect sizes
  JOURNAL   PLoS One 8 (11), e78511 (2013)
   PUBMED   24223155
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Zhang,X., Cao,Q., Liu,X., Liu,S., Wang,J., Sun,S., Wang,O.,
            Tian,Z., Liu,H., Kuang,J. and Zhang,W.
  TITLE     Cellular and molecular evidence for malignancy-inhibitory functions
            of p15RS
  JOURNAL   Cell Cycle 11 (10), 1988-1998 (2012)
   PUBMED   22580456
  REMARK    GeneRIF: The p15RS expression specifically downregulates the
            expression of cathepsin B and MMP-9 at RNA levels, which are known
            to promote cell invasion through degrading extracellular matrix
            proteins.
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Ni,Z., Olsen,J.B., Guo,X., Zhong,G., Ruan,E.D., Marcon,E.,
            Young,P., Guo,H., Li,J., Moffat,J., Emili,A. and Greenblatt,J.F.
  TITLE     Control of the RNA polymerase II phosphorylation state in promoter
            regions by CTD interaction domain-containing proteins RPRD1A and
            RPRD1B
  JOURNAL   Transcription 2 (5), 237-242 (2011)
   PUBMED   22231121
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Wu,Y., Zhang,Y., Zhang,H., Yang,X., Wang,Y., Ren,F., Liu,H.,
            Zhai,Y., Jia,B., Yu,J. and Chang,Z.
  TITLE     p15RS attenuates Wnt/{beta}-catenin signaling by disrupting
            {beta}-catenin.TCF4 Interaction
  JOURNAL   J Biol Chem 285 (45), 34621-34631 (2010)
   PUBMED   20739273
  REMARK    GeneRIF: p15RS inhibits Wnt signaling by interrupting
            beta-catenin.TCF4 complex formation and that Wnt signaling
            initiates downstream gene expression by removing p15RS from
            promoters.
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Liu,J., Liu,H., Zhang,X., Gao,P., Wang,J. and Hu,Z.
  TITLE     Identification and characterization of P15RS, a novel P15(INK4b)
            related gene on G1/S progression
  JOURNAL   Biochem Biophys Res Commun 299 (5), 880-885 (2002)
   PUBMED   12470661
  REMARK    GeneRIF: molecular cloning and characterization of P15RS, a novel
            P15(INK4b) related gene involved in G1/S progression
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK001518.1, AF419845.1,
            AW409855.1 and BC000225.1.
            
            On Jun 10, 2002 this sequence version replaced NP_060640.1.
            
            Summary: This gene encodes a cell-cycle and transcription
            regulatory protein. The encoded protein interacts with the cell
            cycle inhibitor cyclin-dependent kinase 4 inhibitor B and may
            function as a negative regulator of G(1)/S phase progression. This
            protein also forms homo- and hetrodimers with the protein,
            regulation of nuclear pre-mRNA domain-containing protein 1B, to
            form a scaffold that interacts with the C-terminal domain of RNA
            polymerase II subunit B1 and regulates several aspects of
            transcription. Alternate splicing results in multiple transcript
            variants. A pseudogene of this gene is found on chromosome 16.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001518.1, AF419845.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399022.9/ ENSP00000381984.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..312
                     /product="regulation of nuclear pre-mRNA domain-containing
                     protein 1A isoform 1"
                     /note="regulation of nuclear pre-mRNA domain-containing
                     protein 1A; cyclin-dependent kinase 2B-inhibitor-related
                     protein; p15INK4B-related protein; CDKN2B-related protein;
                     Cyclin-dependent kinase inhibitor 2B-related protein
                     (p15INK4B-related protein)"
                     /calculated_mol_wt=35589
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q96P16.1)"
     Region          4..131
                     /region_name="CID_RPRD1A"
                     /note="CID (CTD-Interacting Domain) of Regulation of
                     nuclear pre-mRNA domain-containing protein 1A; cd17011"
                     /db_xref="CDD:340808"
     Site            order(18..20,23,61,64..65,68..69,106,110,113..114)
                     /site_type="other"
                     /note="CTD binding site [polypeptide binding]"
                     /db_xref="CDD:340808"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96P16.1)"
     Site            156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96P16.1)"
     Region          165..310
                     /region_name="CREPT"
                     /note="Cell-cycle alteration and expression-elevated
                     protein in tumour; pfam16566"
                     /db_xref="CDD:465181"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96P16.1)"
     CDS             1..312
                     /gene="RPRD1A"
                     /gene_synonym="HsT3101; P15RS"
                     /coded_by="NM_018170.5:156..1094"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11917.1"
                     /db_xref="GeneID:55197"
                     /db_xref="HGNC:HGNC:25560"
                     /db_xref="MIM:610347"
ORIGIN      
        1 msafseaale kklselsnsq qsvqtlslwl ihhrkhsrpi vtvwerelrk akpnrkltfl
       61 ylandviqns krkgpeftkd fapviveafk hvssetdesc kkhlgrvlsi weersvyend
      121 vleqlkqaly gdkkprkrty eqikvdenen csslgspsep pqtldlvral qdlenaasgd
      181 aavhqriasl pvevqevsll dkitdkesge rlskmvedac mlladyngrl aaeiddrkql
      241 trmladflrc qkealaekeh kleeykrkla rvslvrkelr sriqslpdls rlpnvtgshm
      301 hlpfagdiys ed
//
LOCUS       NP_003324                128 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_003324
VERSION     NP_003324.1
DBSOURCE    REFSEQ: accession NM_003333.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Park,J., Wu,J., Szkop,K.J., Jeong,J., Jovanovic,P., Husmann,D.,
            Flores,N.M., Francis,J.W., Chen,Y.C., Benitez,A.M., Zahn,E.,
            Song,S., Ajani,J.A., Wang,L., Singh,K., Larsson,O., Garcia,B.A.,
            Topisirovic,I., Gozani,O. and Mazur,P.K.
  TITLE     SMYD5 methylation of rpL40 links ribosomal output to gastric cancer
  JOURNAL   Nature 632 (8025), 656-663 (2024)
   PUBMED   39048817
  REMARK    GeneRIF: SMYD5 methylation of rpL40 links ribosomal output to
            gastric cancer.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tong,L., Zheng,X., Wang,T., Gu,W., Shen,T., Yuan,W., Wang,S.,
            Xing,S., Liu,X., Zhang,C. and Zhang,C.
  TITLE     Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression
  JOURNAL   J Cell Mol Med 28 (6), e18164 (2024)
   PUBMED   38445807
  REMARK    GeneRIF: Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Lee,S.O., Kelliher,J.L., Song,W., Tengler,K., Sarkar,A., Dray,E.
            and Leung,J.W.C.
  TITLE     UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination
            and DNA repair
  JOURNAL   J Biol Chem 299 (8), 105043 (2023)
   PUBMED   37451480
  REMARK    GeneRIF: UBA80 and UBA52 fine-tune RNF168-dependent histone
            ubiquitination and DNA repair.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Eastham,M.J., Pelava,A., Wells,G.R., Watkins,N.J. and Schneider,C.
  TITLE     RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion Proteins,
            Are Not Essential for p53 Signalling
  JOURNAL   Biomolecules 13 (6), 898 (2023)
   PUBMED   37371478
  REMARK    GeneRIF: RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion
            Proteins, Are Not Essential for p53 Signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin/52-residue ribosomal protein fusion gene
            subfamily (UbA52) is composed primarily of processed pseudogenes
  JOURNAL   Genomics 14 (2), 520-522 (1992)
   PUBMED   1330885
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin-52 amino acid fusion protein gene shares
            several structural features with mammalian ribosomal protein genes
  JOURNAL   Nucleic Acids Res 19 (5), 1035-1040 (1991)
   PUBMED   1850507
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Monia,B.P., Ecker,D.J., Jonnalagadda,S., Marsh,J., Gotlib,L.,
            Butt,T.R. and Crooke,S.T.
  TITLE     Gene synthesis, expression, and processing of human ubiquitin
            carboxyl extension proteins
  JOURNAL   J Biol Chem 264 (7), 4093-4103 (1989)
   PUBMED   2537304
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Salvesen,G., Lloyd,C. and Farley,D.
  TITLE     cDNA encoding a human homolog of yeast ubiquitin 1
  JOURNAL   Nucleic Acids Res 15 (13), 5485 (1987)
   PUBMED   3037496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BQ428688.1, AF348700.1, BQ428515.1, AF545864.1,
            BU677484.1 and AC005253.1.
            
            Summary: Ubiquitin is a highly conserved nuclear and cytoplasmic
            protein that has a major role in targeting cellular proteins for
            degradation by the 26S proteosome. It is also involved in the
            maintenance of chromatin structure, the regulation of gene
            expression, and the stress response. Ubiquitin is synthesized as a
            precursor protein consisting of either polyubiquitin chains or a
            single ubiquitin moiety fused to an unrelated protein. This gene
            encodes a fusion protein consisting of ubiquitin at the N terminus
            and ribosomal protein L40 at the C terminus, a C-terminal extension
            protein (CEP). Multiple processed pseudogenes derived from this
            gene are present in the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.56978.1,
                                           SRR3476690.163591.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..128
                     /product="ubiquitin-ribosomal protein eL40 fusion protein
                     isoform 1 precursor"
                     /note="ubiquitin-52 amino acid fusion protein; ubiquitin
                     carboxyl extension protein 52; ubiquitin-CEP52;
                     ubiquitin-60S ribosomal protein L40; ubiquitin-ribosomal
                     protein eL40 fusion protein"
                     /calculated_mol_wt=14597
     mat_peptide     1..76
                     /product="Ubiquitin. /id=PRO_0000396433"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=8565
     Region          1..76
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(6..9,11,34..37,40,42,44,46..49,68..76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(8..12,31..35,40,42,44,46..49,68,70..76)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            54
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000269|PubMed:24660806,
                     ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
                     ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291;
                     propagated from UniProtKB/Swiss-Prot (P62987.2)"
     Site            68
                     /site_type="other"
                     /note="Essential for function; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            72
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     mat_peptide     77..128
                     /product="Large ribosomal subunit protein eL40.
                     /id=PRO_0000396434"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=6182
     Region          79..126
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     Site            98
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:39048817,
                     ECO:0000269|PubMed:39103523; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     CDS             1..128
                     /gene="UBA52"
                     /gene_synonym="CEP52; HUBCEP52; L40; RPL40"
                     /coded_by="NM_003333.5:40..426"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS12382.1"
                     /db_xref="GeneID:7311"
                     /db_xref="HGNC:HGNC:12458"
                     /db_xref="MIM:191321"
ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggiiep slrqlaqkyn cdkmicrkcy arlhpravnc rkkkcghtnn
      121 lrpkkkvk
//
LOCUS       NP_001263181             677 aa            linear   PRI 20-NOV-2025
DEFINITION  WD and tetratricopeptide repeats protein 1 isoform a [Homo
            sapiens].
ACCESSION   NP_001263181
VERSION     NP_001263181.1
DBSOURCE    REFSEQ: accession NM_001276252.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Wang,X., Cai,Q., Ping,J., Diaz-Zabala,H., Xia,Y. and Guo,X.
  TITLE     The putative oncogenic role of WDTC1 in colorectal cancer
  JOURNAL   Carcinogenesis 43 (6), 594-600 (2022)
   PUBMED   35238908
  REMARK    GeneRIF: The putative oncogenic role of WDTC1 in colorectal cancer.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Lai,C.Q., Parnell,L.D., Arnett,D.K., Garcia-Bailo,B., Tsai,M.Y.,
            Kabagambe,E.K., Straka,R.J., Province,M.A., An,P., Borecki,I.B.,
            Tucker,K.L. and Ordovas,J.M.
  TITLE     WDTC1, the ortholog of Drosophila adipose gene, associates with
            human obesity, modulated by MUFA intake
  JOURNAL   Obesity (Silver Spring) 17 (3), 593-600 (2009)
   PUBMED   19238144
  REMARK    GeneRIF: WDTC1 variation may be an important risk factor
            contributing to obesity in both Puerto Rican and white populations.
            GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Angers,S., Li,T., Yi,X., MacCoss,M.J., Moon,R.T. and Zheng,N.
  TITLE     Molecular architecture and assembly of the DDB1-CUL4A ubiquitin
            ligase machinery
  JOURNAL   Nature 443 (7111), 590-593 (2006)
   PUBMED   16964240
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Hader,T., Muller,S., Aguilera,M., Eulenberg,K.G., Steuernagel,A.,
            Ciossek,T., Kuhnlein,R.P., Lemaire,L., Fritsch,R., Dohrmann,C.,
            Vetter,I.R., Jackle,H., Doane,W.W. and Bronner,G.
  TITLE     Control of triglyceride storage by a WD40/TPR-domain protein
  JOURNAL   EMBO Rep 4 (5), 511-516 (2003)
   PUBMED   12717455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB072151.1, BC032523.1, AK315564.1, HY218382.1 and FO393419.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315564.1, ERR3218372.514239.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000319394.8/ ENSP00000317971.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..677
                     /product="WD and tetratricopeptide repeats protein 1
                     isoform a"
                     /note="DDB1 and CUL4 associated factor 9; adipose homolog;
                     WD and tetratricopeptide repeats protein 1"
                     /calculated_mol_wt=75789
     Region          <39..215
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          45..84
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          51..88
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          88..129
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          93..131
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          132..172
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          138..178
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..222
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          232..271
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          265..305
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            353
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          359..>468
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          362..395
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            order(366..367,370..371,373,397,400..401,404..405,
                     407..408,434,437..438,441..442,445)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          366..390
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          395..428
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          397..432
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          433..457
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          487..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          535..575
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          537..577
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <546..>626
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          578..617
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     Region          655..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5D0.2)"
     CDS             1..677
                     /gene="WDTC1"
                     /gene_synonym="ADP; DCAF9"
                     /coded_by="NM_001276252.2:420..2453"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS60044.1"
                     /db_xref="GeneID:23038"
                     /db_xref="HGNC:HGNC:29175"
                     /db_xref="MIM:619763"
ORIGIN      
        1 makvnitrdl irrqikerga lsferryhvt dpfirrlgle aelqghsgcv nclewnekgd
       61 llasgsddqh tivwdplhhk kllsmhtght anifsvkflp hagdrilitg aadskvhvhd
      121 ltvketihmf gdhtnrvkri atapmwpntf wsaaedglir qydlrenskh sevlidltey
      181 cgqlveakcl tvnpqdnncl avgasgpfvr lydirmihnh rksmkqspsa gvhtfcdrqk
      241 plpdgaaqyy vaghlpvklp dynnrlrvlv atyvtfspng tellvnmgge qvylfdltyk
      301 qrpytfllpr kchssgevqn gkmstngvsn gvsnglhlhs ngfrlpesrg hvspqvelpp
      361 ylervkqqan eafacqqwtq aiqlyskavq raphnamlyg nraaaymkrk wdgdhydalr
      421 dclkaislnp chlkahfrla rclfelkyva ealeclddfk gkfpeqahss acdalgrdit
      481 aalfskndge ekkgpgggap vrlrstsrkd sisedemvlr ersydyqfry cghcntttdi
      541 keanffgsna qyivsgsddg sffiwekett nlvrvlqgde sivnclqphp sycflatsgi
      601 dpvvrlwnpr pesedltgrv vedmegasqa nqrrmnadpl evmllnmgyr itglssggag
      661 asddedsseg qvqcrps
//
LOCUS       NP_001287965             446 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane and coiled-coil domain protein 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001287965 XP_005269096
VERSION     NP_001287965.1
DBSOURCE    REFSEQ: accession NM_001301036.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Wang,Y.H., Chan,Y.T., Hung,T.H., Hung,J.T., Kuo,M.W., Wang,S.H.,
            Huang,Y., Lin,Y.J., Chen,S.C., Yu,J.C., Wu,J.C., Yu,J. and Yu,A.L.
  TITLE     Transmembrane and coiled-coil domain family 3 (TMCC3) regulates
            breast cancer stem cell and AKT activation
  JOURNAL   Oncogene 40 (16), 2858-2871 (2021)
   PUBMED   33742122
  REMARK    GeneRIF: Transmembrane and coiled-coil domain family 3 (TMCC3)
            regulates breast cancer stem cell and AKT activation.
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Wisesa,S., Yamamoto,Y. and Sakisaka,T.
  TITLE     TMCC3 localizes at the three-way junctions for the proper tubular
            network of the endoplasmic reticulum
  JOURNAL   Biochem J 476 (21), 3241-3260 (2019)
   PUBMED   31696206
  REMARK    GeneRIF: A TMCC3 mutant lacking the N-terminal coiled-coil domain
            abolished localization to tubular network of the endoplasmic
            reticulum, suggesting that TMCC3 localized independently of binding
            to atlastins.
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 446)
  AUTHORS   Sohn,W.J., Kim,J.Y., Kim,D., Park,J.A., Lee,Y. and Kwon,H.J.
  TITLE     Expression and characterization of transmembrane and coiled-coil
            domain family 3
  JOURNAL   BMB Rep 49 (11), 629-634 (2016)
   PUBMED   27697108
  REMARK    GeneRIF: TMCC3 proteins are localized in endoplasmic reticulum
            through transmembrane domains and polymerized with other TMCC3
            protein an 1-3-3 proteins.
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Zhang,C., Kho,Y.S., Wang,Z., Chiang,Y.T., Ng,G.K., Shaw,P.C.,
            Wang,Y. and Qi,R.Z.
  TITLE     Transmembrane and coiled-coil domain family 1 is a novel protein of
            the endoplasmic reticulum
  JOURNAL   PLoS One 9 (1), e85206 (2014)
   PUBMED   24454821
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AB032971.1, AC026672.44 and AI361720.1.
            
            On Jul 18, 2014 this sequence version replaced XP_005269096.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and uses a downstream start codon
            compared to variant 1. The encoded isoform (2) has a shorter
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.89316.1,
                                           SRR1660805.144293.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q22"
     Protein         1..446
                     /product="transmembrane and coiled-coil domain protein 3
                     isoform 2"
                     /note="transmembrane and coiled-coil domains 3;
                     transmembrane and coiled-coil domains protein 3;
                     transmembrane and coiled-coil domain protein 3"
                     /calculated_mol_wt=50043
     Region          33..432
                     /region_name="Tmemb_cc2"
                     /note="Predicted transmembrane and coiled-coil 2 protein;
                     pfam10267"
                     /db_xref="CDD:463036"
     CDS             1..446
                     /gene="TMCC3"
                     /coded_by="NM_001301036.2:95..1435"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73506.1"
                     /db_xref="GeneID:57458"
                     /db_xref="HGNC:HGNC:29199"
                     /db_xref="MIM:617459"
ORIGIN      
        1 mntlslplni rrggsdtnln fdvpdgildf hkvkltadsl kqkilkvteq ikieqtsrdg
       61 nvaeylklvn nadkqqagri kqvfekknqk sahsiaqlqk kleqyhrklr eieqngasrs
      121 skdiskdhlk dihrslkdah vksrtaphcm essksgmpgv sltppvfvfn ksrefanlir
      181 nkfgsadnia hlknsleefr peasaraygg sativnkpky gsddecssgt sgsadsngnq
      241 sfgaggastl dsqgklavil eelreikdtq aqlaedieal kvqfkreygf isqtlqeery
      301 ryerledqlh dltdlhqhet anlkqelasi eekvayqaye rsrdiqeale scqtriskle
      361 lhqqeqqalq tdtvnakvll grcinvilaf mtvilvcvst iakfvspmmk srchilgtff
      421 avtllaifck nwdhilcaie rmiipr
//
LOCUS       NP_115861                165 aa            linear   PRI 20-NOV-2025
DEFINITION  peptidyl-prolyl cis-trans isomerase-like 3 isoform PPIL3a [Homo
            sapiens].
ACCESSION   NP_115861
VERSION     NP_115861.1
DBSOURCE    REFSEQ: accession NM_032472.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Gong,Z., Mu,Y., Chen,J., Chu,H., Lian,P., Wang,C., Wang,J. and
            Jiang,L.
  TITLE     Expression and Significance of Cyclophilin J in Primary Gastric
            Adenocarcinoma
  JOURNAL   Anticancer Res 37 (8), 4475-4481 (2017)
   PUBMED   28739742
  REMARK    GeneRIF: Cyclophilin J expression was up-regulated in gastric
            carcinoma compared to normal gastric tissues.
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Chen,J., Liefke,R., Jiang,L., Wang,J., Huang,C., Gong,Z.,
            Schiene-Fischer,C. and Yu,L.
  TITLE     Biochemical Features of Recombinant Human Cyclophilin J
  JOURNAL   Anticancer Res 36 (3), 1175-1180 (2016)
   PUBMED   26977013
  REMARK    GeneRIF: CYPJ structurally resembles CYPA. It is sensitive to
            inhibition by CsA and plays a role in regulating cell growth,
            proliferation, and apoptosis.
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Qi,Z.Y., Hui,G.Z., Li,Y., Zhou,Z.X., Gu,S.H., Ying,K. and Xie,Y.
  TITLE     cDNA microarray in isolation of novel differentially expressed
            genes related to human glioma and clone of a novel full-length gene
  JOURNAL   Chin Med J (Engl) 118 (10), 799-805 (2005)
   PUBMED   15989758
  REMARK    GeneRIF: The novel full-length gene of human PPIL3 may be
            correlated with the formation of human glioma.
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Huang,L.L., Zhao,X.M., Huang,C.Q., Yu,L. and Xia,Z.X.
  TITLE     Structure of recombinant human cyclophilin J, a novel member of the
            cyclophilin family
  JOURNAL   Acta Crystallogr D Biol Crystallogr 61 (Pt 3), 316-321 (2005)
   PUBMED   15735342
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Hu,H., Huang,C.Q., Liu,H.L., Han,Y., Yu,L. and Bi,R.C.
  TITLE     Crystallization and preliminary X-ray crystallographic studies of
            human cyclophilin J
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 61 (Pt 2), 216-218
            (2005)
   PUBMED   16510998
  REMARK    GeneRIF: Human cyclophilin J, a new member of the cyclophilin
            family, has been expressed and crystallized.
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Zhou,Z., Ying,K., Dai,J., Tang,R., Wang,W., Huang,Y., Zhao,W.,
            Xie,Y. and Mao,Y.
  TITLE     Molecular cloning and characterization of a novel peptidylprolyl
            isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain
  JOURNAL   Cytogenet Cell Genet 92 (3-4), 231-236 (2001)
   PUBMED   11435694
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF251049.1, AF271652.1 and
            AC005037.2.
            
            Summary: This gene encodes a member of the cyclophilin family.
            Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl
            imide bonds in oligopeptides. They have been proposed to act either
            as catalysts or as molecular chaperones in protein-folding events.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Sep 2008].
            
            Transcript Variant: This variant (PPIL3a) encodes the longer
            isoform (PPIL3a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF251049.1, CD050829.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..165
                     /product="peptidyl-prolyl cis-trans isomerase-like 3
                     isoform PPIL3a"
                     /EC_number="5.2.1.8"
                     /note="cyclophilin J; peptidyl-prolyl cis-trans
                     isomerase-like 3; cyclophilin-like protein 3;
                     peptidylprolyl cis-trans isomerase-like protein 3;
                     PPIase-like protein 3; cyclophilin-like protein PPIL3;
                     rotamase PPIL3; peptidylprolyl isomerase
                     (cyclophilin)-like 3"
                     /calculated_mol_wt=18496
     Region          1..158
                     /region_name="cyclophilin"
                     /note="cyclophilin-type peptidylprolyl cis- trans
                     isomerases. This family contains eukaryotic, bacterial and
                     archeal proteins which exhibit a peptidylprolyl cis- trans
                     isomerases activity (PPIase, Rotamase) and in addition
                     bind the immunosuppressive drug...; cl00197"
                     /db_xref="CDD:469651"
     Site            order(30,32,35..36,38,94..95,104,106,114..115,119)
                     /site_type="active"
                     /db_xref="CDD:238194"
     CDS             1..165
                     /gene="PPIL3"
                     /gene_synonym="CYPJ"
                     /coded_by="NM_032472.4:193..690"
                     /note="isoform PPIL3a is encoded by transcript variant
                     PPIL3a"
                     /db_xref="CCDS:CCDS2332.1"
                     /db_xref="GeneID:53938"
                     /db_xref="HGNC:HGNC:9262"
                     /db_xref="MIM:615811"
ORIGIN      
        1 msvtlhtdvg dikievfcer tpktcemesr cvpqagvqwr dlgslqpppp gfkqvfclsl
       61 prtgrggnsi wgkkfedeys eylkhnvrgv vsmanngpnt ngsqffityg kqphldmkyt
      121 vfgkvidgle tldeleklpv nektyrplnd vhikditiha npfaq
//
LOCUS       NP_001287712             304 aa            linear   PRI 20-NOV-2025
DEFINITION  protein Largen isoform 1 [Homo sapiens].
ACCESSION   NP_001287712 XP_005272067
VERSION     NP_001287712.1
DBSOURCE    REFSEQ: accession NM_001300783.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Thiebaut,R., Esmiol,S., Lecine,P., Mahfouz,B., Hermant,A.,
            Nicoletti,C., Parnis,S., Perroy,J., Borg,J.P., Pascoe,L.,
            Hugot,J.P. and Ollendorff,V.
  TITLE     Characterization and Genetic Analyses of New Genes Coding for NOD2
            Interacting Proteins
  JOURNAL   PLoS One 11 (11), e0165420 (2016)
   PUBMED   27812135
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Scannell Bryan,M., Argos,M., Pierce,B., Tong,L., Rakibuz-Zaman,M.,
            Ahmed,A., Rahman,M., Islam,T., Yunus,M., Parvez,F., Roy,S.,
            Jasmine,F., Baron,J.A., Kibriya,M.G. and Ahsan,H.
  TITLE     Genome-wide association studies and heritability estimates of body
            mass index related phenotypes in Bangladeshi adults
  JOURNAL   PLoS One 9 (8), e105062 (2014)
   PUBMED   25133637
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Yamamoto,K., Gandin,V., Sasaki,M., McCracken,S., Li,W.,
            Silvester,J.L., Elia,A.J., Wang,F., Wakutani,Y., Alexandrova,R.,
            Oo,Y.D., Mullen,P.J., Inoue,S., Itsumi,M., Lapin,V., Haight,J.,
            Wakeham,A., Shahinian,A., Ikura,M., Topisirovic,I., Sonenberg,N.
            and Mak,T.W.
  TITLE     Largen: a molecular regulator of mammalian cell size control
  JOURNAL   Mol Cell 53 (6), 904-915 (2014)
   PUBMED   24656129
  REMARK    GeneRIF: Largen, the product of a gene PRR16, increases cell size
            upon overexpression in human cells.
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Wang,H., St Julien,K.R., Stevenson,D.K., Hoffmann,T.J., Witte,J.S.,
            Lazzeroni,L.C., Krasnow,M.A., Quaintance,C.C., Oehlert,J.W.,
            Jelliffe-Pawlowski,L.L., Gould,J.B., Shaw,G.M. and O'Brodovich,H.M.
  TITLE     A genome-wide association study (GWAS) for bronchopulmonary
            dysplasia
  JOURNAL   Pediatrics 132 (2), 290-297 (2013)
   PUBMED   23897914
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Kennedy,R.B., Ovsyannikova,I.G., Pankratz,V.S., Haralambieva,I.H.,
            Vierkant,R.A. and Poland,G.A.
  TITLE     Genome-wide analysis of polymorphisms associated with cytokine
            responses in smallpox vaccine recipients
  JOURNAL   Hum Genet 131 (9), 1403-1421 (2012)
   PUBMED   22610502
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Sakai,Y., Shaw,C.A., Dawson,B.C., Dugas,D.V., Al-Mohtaseb,Z.,
            Hill,D.E. and Zoghbi,H.Y.
  TITLE     Protein interactome reveals converging molecular pathways among
            autism disorders
  JOURNAL   Sci Transl Med 3 (86), 86ra49 (2011)
   PUBMED   21653829
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Barberi,T., Willis,L.M., Socci,N.D. and Studer,L.
  TITLE     Derivation of multipotent mesenchymal precursors from human
            embryonic stem cells
  JOURNAL   PLoS Med 2 (6), e161 (2005)
   PUBMED   15971941
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC113418.2 and AC093301.3.
            
            On Jul 12, 2014 this sequence version replaced XP_005272067.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP258446.1, BC092474.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407149.7/ ENSP00000385118.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.1"
     Protein         1..304
                     /product="protein Largen isoform 1"
                     /note="mesenchymal stem cell protein DSC54; proline-rich
                     protein 16; protein Largen"
                     /calculated_mol_wt=32681
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569H4.1)"
     Region          53..304
                     /region_name="DUF4589"
                     /note="Domain of unknown function (DUF4589); pfam15252"
                     /db_xref="CDD:464592"
     Region          66..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569H4.1)"
     Region          114..160
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569H4.1)"
     Region          239..304
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q569H4.1)"
     CDS             1..304
                     /gene="PRR16"
                     /gene_synonym="DSC54; LARGEN"
                     /coded_by="NM_001300783.2:188..1102"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS75290.1"
                     /db_xref="GeneID:51334"
                     /db_xref="HGNC:HGNC:29654"
                     /db_xref="MIM:615931"
ORIGIN      
        1 msakskgnps sscpaegppa asktkvkeqi kiivedlelv lgdlkdvake lkevvdqidt
       61 ltsdlqlede mtdssktdtl nssssgttas slekikvqan aplikppahp sailtvlrkp
      121 npppppprlt pvkcedpkrv vptanpvktn gtllrngglp ggpnkipngd iccipnsnld
      181 kapvqllmhr pekdrcpqag prervrfnek vqyhgycpdc dtryniknre vhlhsepvhp
      241 pgkiphqgpp lpptphlppf plenggmgis hsnsfppirp atvppptapk pqktilrkst
      301 tttv
//
LOCUS       NP_005671                588 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            B isoform a [Homo sapiens].
ACCESSION   NP_005671
VERSION     NP_005671.3
DBSOURCE    REFSEQ: accession NM_005680.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 588)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 588)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 588)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 588)
  AUTHORS   Okuda,H., Kanai,A., Ito,S., Matsui,H. and Yokoyama,A.
  TITLE     AF4 uses the SL1 components of RNAP1 machinery to initiate MLL
            fusion- and AEP-dependent transcription
  JOURNAL   Nat Commun 6, 8869 (2015)
   PUBMED   26593443
  REMARK    GeneRIF: AEP coactivator complex facilitates the initiation of
            RNAP2-dependent transcription via SL1 activity by loading TBP onto
            the TATA element.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 588)
  AUTHORS   Muth,V., Nadaud,S., Grummt,I. and Voit,R.
  TITLE     Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA
            polymerase I transcription
  JOURNAL   EMBO J 20 (6), 1353-1362 (2001)
   PUBMED   11250901
REFERENCE   7  (residues 1 to 588)
  AUTHORS   Zhai,W. and Comai,L.
  TITLE     Repression of RNA polymerase I transcription by the tumor
            suppressor p53
  JOURNAL   Mol Cell Biol 20 (16), 5930-5938 (2000)
   PUBMED   10913176
REFERENCE   8  (residues 1 to 588)
  AUTHORS   Di Pietro,C., Rapisarda,A., Amico,V., Bonaiuto,C., Viola,A.,
            Scalia,M., Motta,S., Amato,A., Engel,H., Messina,A., Sichel,G.,
            Grzeschik,K. and Purrello,M.
  TITLE     Genomic localization of the human genes TAF1A, TAF1B and TAF1C,
            encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I
            general transcription initiation factor SL1
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 133-136 (2000)
   PUBMED   10894955
REFERENCE   9  (residues 1 to 588)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   10 (residues 1 to 588)
  AUTHORS   Comai,L., Zomerdijk,J.C., Beckmann,H., Zhou,S., Admon,A. and
            Tjian,R.
  TITLE     Reconstitution of transcription factor SL1: exclusive binding of
            TBP by SL1 or TFIID subunits
  JOURNAL   Science 266 (5193), 1966-1972 (1994)
   PUBMED   7801123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010969.11.
            
            On Nov 23, 2018 this sequence version replaced NP_005671.2.
            
            Summary: Initiation of transcription by RNA polymerase I requires
            the formation of a complex composed of the TATA-binding protein
            (TBP) and three TBP-associated factors (TAFs) specific for RNA
            polymerase I. This complex, known as SL1, binds to the core
            promoter of ribosomal RNA genes to position the polymerase properly
            and acts as a channel for regulatory signals. This gene encodes one
            of the SL1-specific TAFs. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018137.2, SRR1803612.109259.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263663.10/ ENSP00000263663.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p25.1"
     Protein         1..588
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit B isoform a"
                     /note="SL1, 63kD subunit; TBP-associated factor 1B; TATA
                     box-binding protein-associated factor 1B; transcription
                     initiation factor SL1/TIF-IB subunit B; RNA polymerase
                     I-specific TBP-associated factor 63 kDa; TATA box binding
                     protein (TBP)-associated factor, RNA polymerase I, B,
                     63kD; TATA-box binding protein associated factor, RNA
                     polymerase I, B; TATA box binding protein (TBP)-associated
                     factor, RNA polymerase I, B, 63kDa"
                     /calculated_mol_wt=68701
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q53T94.1)"
     Region          7..39
                     /region_name="zf-RRN7"
                     /note="Zinc-finger of RNA-polymerase I-specific TFIIB,
                     Rrn7; pfam11781"
                     /db_xref="CDD:463348"
     Region          40..68
                     /region_name="B-reader"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53T94.1)"
     Region          69..73
                     /region_name="B-linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53T94.1)"
     Region          74..261
                     /region_name="N-terminal cyclin fold"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53T94.1)"
     Region          262..372
                     /region_name="C-terminal cyclin fold"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53T94.1)"
     Site            440
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q53T94.1)"
     CDS             1..588
                     /gene="TAF1B"
                     /gene_synonym="MGC:9349; RAF1B; RAFI63; SL1; TAFI63"
                     /coded_by="NM_005680.3:69..1835"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33143.1"
                     /db_xref="GeneID:9014"
                     /db_xref="HGNC:HGNC:11533"
                     /db_xref="MIM:604904"
ORIGIN      
        1 mdleeaeefk erctqcaavs wgltdegkyy ctschnvter yqevtntdli pntqikalnr
       61 glkkknntek gwdwyvcegf qyilyqqaea lknlgvgpel kndvlhnfwk rylqkskqay
      121 cknpvyttgr kptvlednls hsdwasepel lsdvscppfl esgaesqsdi htrkpfpvsk
      181 asqsetsvcs gsldgveysq rkekgivkmt mpqtlafcyl sllwqreait lsdllrfvee
      241 dhipyinafq hfpeqmklyg rdrgifgies wpdyediykk tvevgtfldl prfpditedc
      301 ylhpnilcmk ylmevnlpde mhsltchvvk mtgmgevdfl tfdpiakmak tvkydvqava
      361 iivvvlkllf llddsfewsl snlaekhnek nkkdkpwfdf rkwyqimkka fdekkqkwee
      421 arakylwkse kplyysfvdk pvaykkremv vnlqkqfstl vestatagkk spssfqfnwt
      481 eedtdrtcfh ghslqgvlke kgqslltkns lywlstqkfc rcycthvtty eesnyslsyq
      541 filnlfsfll riktsllhee vslvekklfe kkysvkrkks rskkvrrh
//
LOCUS       NP_001230209             570 aa            linear   PRI 20-NOV-2025
DEFINITION  CD166 antigen isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001230209
VERSION     NP_001230209.1
DBSOURCE    REFSEQ: accession NM_001243280.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Morosi,L.G., Piperno,G.M., Lopez,L., Amadio,R., Joshi,S.,
            Rustighi,A., Del Sal,G. and Benvenuti,F.
  TITLE     ALCAM-mediated cDC1 CD8 T cells interactions are suppressed in
            advanced lung tumors
  JOURNAL   Oncoimmunology 13 (1), 2367843 (2024)
   PUBMED   38887373
  REMARK    GeneRIF: ALCAM-mediated cDC1 CD8 T cells interactions are
            suppressed in advanced lung tumors.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Wagner,M., Sobczynski,M., Wisniewski,A., Matusiak,L.,
            Kusnierczyk,P. and Jasek,M.
  TITLE     Polymorphisms in the CD6-ALCAM axis may modulate psoriasis risk and
            outcomes
  JOURNAL   Hum Immunol 85 (3), 110797 (2024)
   PUBMED   38580538
  REMARK    GeneRIF: Polymorphisms in the CD6-ALCAM axis may modulate psoriasis
            risk and outcomes.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Moradi,L., Tajik,F., Saeednejad Zanjani,L., Panahi,M.,
            Gheytanchi,E., Biabanaki,Z.S., Kazemi-Sefat,G.E., Hashemi,F.,
            Dehghan Manshadi,M. and Madjd,Z.
  TITLE     Clinical significance of CD166 and HER-2 in different types of
            gastric cancer
  JOURNAL   Clin Transl Oncol 26 (3), 664-681 (2024)
   PUBMED   37537510
  REMARK    GeneRIF: Clinical significance of CD166 and HER-2 in different
            types of gastric cancer.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Jamann,H., Desu,H.L., Cui,Q.L., Halaweh,A., Tastet,O., Klement,W.,
            Zandee,S., Pernin,F., Mamane,V.H., Ouedraogo,O., Daigneault,A.,
            Sidibe,H., Millette,F., Peelen,E., Dhaeze,T., Hoornaert,C.,
            Rebillard,R.M., Thai,K., Grasmuck,C., Vande Velde,C., Prat,A.,
            Arbour,N., Stratton,J.A., Antel,J. and Larochelle,C.
  TITLE     ALCAM on human oligodendrocytes mediates CD4 T cell adhesion
  JOURNAL   Brain 147 (1), 147-162 (2024)
   PUBMED   37640028
  REMARK    GeneRIF: ALCAM on human oligodendrocytes mediates CD4 T cell
            adhesion.
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Singer,N.G., Mitra,R., Lialios,F., Richardson,B.C., Marks,R.M.,
            Pesando,J.M., Fox,D.A. and Nickoloff,B.J.
  TITLE     CD6 dependent interactions of T cells and keratinocytes: functional
            evidence for a second CD6 ligand on gamma-interferon activated
            keratinocytes
  JOURNAL   Immunol Lett 58 (1), 9-14 (1997)
   PUBMED   9436462
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Skonier,J.E., Bowen,M.A., Emswiler,J., Aruffo,A. and Bajorath,J.
  TITLE     Recognition of diverse proteins by members of the immunoglobulin
            superfamily: delineation of the receptor binding site in the human
            CD6 ligand ALCAM
  JOURNAL   Biochemistry 35 (38), 12287-12291 (1996)
   PUBMED   8823162
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Whitney,G.S., Starling,G.C., Bowen,M.A., Modrell,B., Siadak,A.W.
            and Aruffo,A.
  TITLE     The membrane-proximal scavenger receptor cysteine-rich domain of
            CD6 contains the activated leukocyte cell adhesion molecule binding
            site
  JOURNAL   J Biol Chem 270 (31), 18187-18190 (1995)
   PUBMED   7543097
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Bajorath,J., Bowen,M.A. and Aruffo,A.
  TITLE     Molecular model of the N-terminal receptor-binding domain of the
            human CD6 ligand ALCAM
  JOURNAL   Protein Sci 4 (8), 1644-1647 (1995)
   PUBMED   8520490
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Bowen,M.A., Patel,D.D., Li,X., Modrell,B., Malacko,A.R., Wang,W.C.,
            Marquardt,H., Neubauer,M., Pesando,J.M., Francke,U. et al.
  TITLE     Cloning, mapping, and characterization of activated leukocyte-cell
            adhesion molecule (ALCAM), a CD6 ligand
  JOURNAL   J Exp Med 181 (6), 2213-2220 (1995)
   PUBMED   7760007
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078806.18 and AC023602.5.
            
            Summary: This gene encodes activated leukocyte cell adhesion
            molecule (ALCAM), also known as CD166 (cluster of differentiation
            166), which is a member of a subfamily of immunoglobulin receptors
            with five immunoglobulin-like domains (VVC2C2C2) in the
            extracellular domain. This protein binds to T-cell differentiation
            antigene CD6, and is implicated in the processes of cell adhesion
            and migration. Multiple alternatively spliced transcript variants
            encoding different isoforms have been found. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            3' CDS, compared to variant 1. The resulting isoform (2) lacks an
            internal segment in the C-terminal region, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.80622.1,
                                           SRR1660809.23155.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..570
                     /product="CD166 antigen isoform 2 precursor"
                     /note="CD166 antigen"
                     /calculated_mol_wt=60826
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2857
     mat_peptide     28..570
                     /product="CD166 antigen isoform 2"
                     /calculated_mol_wt=60826
     Region          38..113
                     /region_name="IGv"
                     /note="Immunoglobulin V-Type; smart00406"
                     /db_xref="CDD:214650"
     Region          39..43
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          55..59
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          96..100
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          110..115
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          137..231
                     /region_name="C2-set_2"
                     /note="CD80-like C2-set immunoglobulin domain; pfam08205"
                     /db_xref="CDD:400489"
     Region          143..157
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          167..171
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          203..207
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          217..222
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          255..329
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          266..270
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          280..284
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          296..300
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          339..393
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          415..489
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     CDS             1..570
                     /gene="ALCAM"
                     /gene_synonym="CD166; MEMD"
                     /coded_by="NM_001243280.2:501..2213"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS58841.1"
                     /db_xref="GeneID:214"
                     /db_xref="HGNC:HGNC:400"
                     /db_xref="MIM:601662"
ORIGIN      
        1 meskgasscr llfcllisat vfrpglgwyt vnsaygdtii ipcrldvpqn lmfgkwkyek
       61 pdgspvfiaf rsstkksvqy ddvpeykdrl nlsenytlsi snarisdekr fvcmlvtedn
      121 vfeaptivkv fkqpskpeiv skalfleteq lkklgdcise dsypdgnitw yrngkvlhpl
      181 egavviifkk emdpvtqlyt mtstleyktt kadiqmpftc svtyygpsgq ktihseqavf
      241 diyypteqvt iqvlppknai kegdnitlkc lgngnpppee flfylpgqpe girssntytl
      301 tdvrrnatgd ykcslidkks miastaitvh yldlslnpsg evtrqigdal pvsctisasr
      361 natvvwmkdn irlrsspsfs slhyqdagny vcetalqeve glkkresltl ivegkpqikm
      421 tkktdpsgls ktiichvegf pkpaiqwtit gsgsvinqte espyingryy skiiispeen
      481 vtltctaenq lertvnslnv sanenrekvn dqaklivgiv vglllaalva gvvywlymkk
      541 sktaskhvnk dlgnmeenkk leennhktea
//
LOCUS       NP_001277133             544 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-decapping enzyme 1A isoform b [Homo sapiens].
ACCESSION   NP_001277133 XP_005265377
VERSION     NP_001277133.1
DBSOURCE    REFSEQ: accession NM_001290204.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 544)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 544)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 544)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 544)
  AUTHORS   Wu,H., Zhang,J., Bai,Y., Zhang,S., Zhang,Z., Tong,W., Han,P.,
            Fu,B., Zhang,Y. and Shen,Z.
  TITLE     DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma
  JOURNAL   Aging (Albany NY) 13 (19), 23020-23035 (2021)
   PUBMED   34609335
  REMARK    GeneRIF: DCP1A is an unfavorable prognostic-related enhancer RNA in
            hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 544)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   6  (residues 1 to 544)
  AUTHORS   Leonard,D., Ajuh,P., Lamond,A.I. and Legerski,R.J.
  TITLE     hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA
            splicing
  JOURNAL   Biochem Biophys Res Commun 308 (4), 793-801 (2003)
   PUBMED   12927788
REFERENCE   7  (residues 1 to 544)
  AUTHORS   Ingelfinger,D., Arndt-Jovin,D.J., Luhrmann,R. and Achsel,T.
  TITLE     The human LSm1-7 proteins colocalize with the mRNA-degrading
            enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
  JOURNAL   RNA 8 (12), 1489-1501 (2002)
   PUBMED   12515382
REFERENCE   8  (residues 1 to 544)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
  REMARK    GeneRIF: These data suggest that a human decapping complex
            containing decapping enzymes hDcp1a and hDcp2 may be recruited to
            mRNAs containing premature termination codons by the hUpf proteins.
REFERENCE   9  (residues 1 to 544)
  AUTHORS   Callebaut,I.
  TITLE     An EVH1/WH1 domain as a key actor in TGFbeta signalling
  JOURNAL   FEBS Lett 519 (1-3), 178-180 (2002)
   PUBMED   12023040
REFERENCE   10 (residues 1 to 544)
  AUTHORS   Bai,R.Y., Koester,C., Ouyang,T., Hahn,S.A., Hammerschmidt,M.,
            Peschel,C. and Duyster,J.
  TITLE     SMIF, a Smad4-interacting protein that functions as a co-activator
            in TGFbeta signalling
  JOURNAL   Nat Cell Biol 4 (3), 181-190 (2002)
   PUBMED   11836524
  REMARK    GeneRIF: Overexpression of wild-type SMIF enhanced expression of
            TGFbeta/BMP regulated genes, whereas a dominant-negative SMIF
            mutant suppressed expression.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC371232.1, AK295205.1,
            AC112218.2 and CD676826.1.
            
            On Mar 1, 2014 this sequence version replaced XP_005265377.2.
            
            Summary: Decapping is a key step in general and regulated mRNA
            decay. The protein encoded by this gene is a decapping enzyme. This
            protein and another decapping enzyme form a decapping complex,
            which interacts with the nonsense-mediated decay factor hUpf1 and
            may be recruited to mRNAs containing premature termination codons.
            This protein also participates in the TGF-beta signaling pathway.
            Alternative splicing of this gene results in multiple transcript
            variants. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1, resulting
            in an isoform (b) that is shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.89745.1, AK295205.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..544
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.1"
     Protein         1..544
                     /product="mRNA-decapping enzyme 1A isoform b"
                     /EC_number="3.6.1.62"
                     /note="transcription factor SMIF; Smad4-interacting
                     transcriptional co-activator; mRNA-decapping enzyme 1A;
                     decapping enzyme hDcp1a; putative protein product of
                     Nbla00360; DCP1 decapping enzyme homolog A; DCP1 decapping
                     enzyme-like protein A"
                     /calculated_mol_wt=59199
     Region          6..126
                     /region_name="Dcp1"
                     /note="mRNA decapping enzyme 1 (Dcp1); cd09804"
                     /db_xref="CDD:197362"
     Site            order(7..8,12,14..15,18..19,29,31,53,70..72,75,77)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:197362"
     Region          <230..494
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          501..543
                     /region_name="mRNA_decap_C"
                     /note="mRNA-decapping enzyme C-terminus; pfam16741"
                     /db_xref="CDD:465253"
     CDS             1..544
                     /gene="DCP1A"
                     /gene_synonym="HSA275986; Nbla00360; SMAD4IP1; SMIF"
                     /coded_by="NM_001290204.2:27..1661"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74946.1"
                     /db_xref="GeneID:55802"
                     /db_xref="HGNC:HGNC:18714"
                     /db_xref="MIM:607010"
ORIGIN      
        1 mealsragqe mslaalkqhd pyitsiadlt gqvalytfcp kanqwektdi egtlfvyrrs
       61 aspyhgftiv nrlnmhnlve pvnkdlefql hepfllyrna slsiysiwfy dkndchriak
      121 lmadvveeet rrsqqaardk qspsqangcs dhrpidilem lsrakdeyer sapsghkhlt
      181 veelfgtslp keqpavvgld seemerlpgd asqkepnsfl pfpfeqlgga pqsetlgvps
      241 aahhsvqpei ttpvlitpas itqsnekhap tytiplspvl sptlpaeapt aqvppslprn
      301 stmmqavktt prqrspllnq pvpelshasl ianqspfrap lnvtntagts lpsvdllqkl
      361 rltpqhdqiq tqplgkgamv asfspaagql atpesfiepp sktaaarvaa saslsnmvla
      421 plqsmqqnqd pevfvqpkvl ssaipvagap lvtatttavs svllapsvfq qtvtrssdle
      481 rkasspsplt igtpesqrkp siilsksqlq dtlihliknd ssflstlhev ylqvltknkd
      541 nhnl
//
LOCUS       NP_055670                807 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-5 complex subunit zeta-1 isoform 1 [Homo sapiens].
ACCESSION   NP_055670 XP_166527 XP_379771 XP_499251 XP_499396
VERSION     NP_055670.1
DBSOURCE    REFSEQ: accession NM_014855.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 807)
  AUTHORS   Mai,X., Wang,Y., Wang,X., Liu,M., Teng,F., Liu,Z., Su,M.Y. and
            Stjepanovic,G.
  TITLE     Structural basis for membrane remodeling by the AP5-SPG11-SPG15
            complex
  JOURNAL   Nat Struct Mol Biol 32 (8), 1334-1346 (2025)
   PUBMED   40175557
REFERENCE   2  (residues 1 to 807)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 807)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 807)
  AUTHORS   Denton,K., Mou,Y., Xu,C.C., Shah,D., Chang,J., Blackstone,C. and
            Li,X.J.
  TITLE     Impaired mitochondrial dynamics underlie axonal defects in
            hereditary spastic paraplegias
  JOURNAL   Hum Mol Genet 27 (14), 2517-2530 (2018)
   PUBMED   29726929
  REMARK    GeneRIF: Here, we have generated induced pluripotent stem cells
            (iPSCs) from patients with two autosomal recessive forms of
            hereditary spastic paraplegia (HSP) , SPG15 and SPG48, which are
            caused by mutations in the ZFYVE26 and AP5Z1 genes encoding
            proteins in the same complex, the spastizin and AP5Z1 proteins,
            respectively.
REFERENCE   5  (residues 1 to 807)
  AUTHORS   Hirst,J., Borner,G.H., Edgar,J., Hein,M.Y., Mann,M., Buchholz,F.,
            Antrobus,R. and Robinson,M.S.
  TITLE     Interaction between AP-5 and the hereditary spastic paraplegia
            proteins SPG11 and SPG15
  JOURNAL   Mol Biol Cell 24 (16), 2558-2569 (2013)
   PUBMED   23825025
REFERENCE   6  (residues 1 to 807)
  AUTHORS   Hirst,J., Barlow,L.D., Francisco,G.C., Sahlender,D.A., Seaman,M.N.,
            Dacks,J.B. and Robinson,M.S.
  TITLE     The fifth adaptor protein complex
  JOURNAL   PLoS Biol 9 (10), e1001170 (2011)
   PUBMED   22022230
  REMARK    Erratum:[PLoS Biol. 2012 Mar;10(3). doi:
            10.1371/annotation/89dff893-c156-44bb-a731-bfcc91843583]
REFERENCE   7  (residues 1 to 807)
  AUTHORS   Slabicki,M., Theis,M., Krastev,D.B., Samsonov,S., Mundwiller,E.,
            Junqueira,M., Paszkowski-Rogacz,M., Teyra,J., Heninger,A.K.,
            Poser,I., Prieur,F., Truchetto,J., Confavreux,C., Marelli,C.,
            Durr,A., Camdessanche,J.P., Brice,A., Shevchenko,A.,
            Pisabarro,M.T., Stevanin,G. and Buchholz,F.
  TITLE     A genome-scale DNA repair RNAi screen identifies SPG48 as a novel
            gene associated with hereditary spastic paraplegia
  JOURNAL   PLoS Biol 8 (6), e1000408 (2010)
   PUBMED   20613862
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 807)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 807)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY145300.1, BI766915.1,
            CD671081.1, BQ228738.1, BC008841.2, AB007875.1, AC092610.1 and
            AI927641.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Nov 23, 2005 this sequence version replaced
            XP_499251.1, XP_499396.1, XP_166527.6, XP_379771.2.
            
            Summary: This gene was identified by genome-wide screen for genes
            involved in homologous recombination DNA double-strand break repair
            (HR-DSBR). The encoded protein was found in a complex with other
            proteins that have a role in HR-DSBR. Knockdown of this gene
            reduced homologous recombination, and mutations in this gene were
            found in patients with spastic paraplegia. It was concluded that
            this gene likely encodes a helicase (PMID:20613862). [provided by
            RefSeq, Jan 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.81952.1,
                                           SRR1660805.176643.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649063.2/ ENSP00000497815.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..807
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..807
                     /product="AP-5 complex subunit zeta-1 isoform 1"
                     /note="zeta5; adapter-related protein complex 5 zeta
                     subunit; AP-5 complex subunit zeta-1; adaptor related
                     protein complex 5 zeta 1 subunit; adaptor-related protein
                     complex 5 zeta subunit"
                     /calculated_mol_wt=88474
     Region          320..437
                     /region_name="SPG48"
                     /note="AP-5 complex subunit, vesicle trafficking;
                     pfam14764"
                     /db_xref="CDD:464303"
     CDS             1..807
                     /gene="AP5Z1"
                     /gene_synonym="KIAA0415; SPG48; zeta"
                     /coded_by="NM_014855.3:94..2517"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS47528.1"
                     /db_xref="GeneID:9907"
                     /db_xref="HGNC:HGNC:22197"
                     /db_xref="MIM:613653"
ORIGIN      
        1 mfsagaesll hqareiqdee lkkfcsrick llqaedlgpd tldslqrlfl iisatkysrr
       61 lektcvdllq atlglpacpe qlqvlcaail remspsdsls lawdhtqnsr qlslvasvll
      121 aqgdrneevr avgqgvlral esrqpegpsl rhllpvmakv vvlspgtlqe dqatllskrl
      181 vdwlryaslq qglphsggff stprarqpgp vtevdgavat dfftvlssgh rftddqwlnv
      241 qafsmlrawl lhsgpegpgt ldtddrseqe gstlsvisat ssagrllppr erlrevafey
      301 cqrlieqsnr ralrkgdsdl qkaclveavl vldvlcrqdp sflyrslscl kalhgrvrgd
      361 pasvrvllpl ahfflshgea aavdseavyq hlftripveq fhspmlafef iqfcrdnlhl
      421 fsghlstlrl sfpnlfkfla wnsppltsef vallpalvda gtalemlhal ldlpcltavl
      481 dlqlrsapaa serplwdtsl rapscleafr dpqfqglfqy llrpkasgat erlaplhqll
      541 qpmagcarva qcaqavptll qaffsavtqv adgslinqla llllgrsdsl ypapgyaagv
      601 hsvlssqfla lctlkpslvv elardllefl gsvnglcsra slvtsvvwai geylsvtydr
      661 rctveqinkf fealeallfe vtqcrpsaal prcppqvvtv lmttltklas rsqdlipras
      721 lllskmrtla hspatssths eegaeairtr atelltllkm psvaqfvltp stevcspryh
      781 rdantalpla lrtvsrlver eaglmpg
//
LOCUS       NP_001278775              77 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 16 [Homo sapiens].
ACCESSION   NP_001278775
VERSION     NP_001278775.1
DBSOURCE    REFSEQ: accession NM_001291846.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM148203.1, BU537824.1 and
            AW337855.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (16) lacks five 3' exons but
            contains two alternate 3' exons, and it thus differs in its 3'
            coding region and 3' UTR, compared to variant 1. The encoded
            isoform (16) has a distinct C-terminus and is significantly shorter
            than isoform 1. This isoform contains no N-terminal zinc finger
            motifs and is likely non-DNA-binding. Both variants 16 and 17
            encode isoform 16.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM148203.1, DN998683.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..77
                     /product="DNA-binding protein Ikaros isoform 16"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=8158
     CDS             1..77
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291846.2:222..455"
                     /note="isoform 16 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS87502.1"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvvtygadd
       61 frdfhaiipk sfsllel
//
LOCUS       NP_277047                417 aa            linear   PRI 20-NOV-2025
DEFINITION  testis-specific Y-encoded-like protein 5 [Homo sapiens].
ACCESSION   NP_277047
VERSION     NP_277047.2
DBSOURCE    REFSEQ: accession NM_033512.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Ancia,M., Wahni,K., Chakrowf,J., El Aakchioui,A., Claude,E., de
            Lhoneux,G., Liberelle,M., Janvier,S., Baranova,E., Malo Pueyo,J.,
            Jijon Vergara,A., Papadopoulos,N., Balty,C., Dejeu,J.,
            Decottignies,A., Messens,J. and Frederick,R.
  TITLE     Structural insights into the interaction between testis-specific
            Y-encoded-like protein 5 and ubiquitin-specific protease 7
  JOURNAL   Protein Sci 34 (5), e70116 (2025)
   PUBMED   40260937
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Dalui,S., Dasgupta,A., Adhikari,S., Das,C. and Roy,S.
  TITLE     Human testis-specific Y-encoded protein-like protein 5 is a histone
            H3/H4-specific chaperone that facilitates histone deposition in
            vitro
  JOURNAL   J Biol Chem 298 (8), 102200 (2022)
   PUBMED   35772497
  REMARK    GeneRIF: Human testis-specific Y-encoded protein-like protein 5 is
            a histone H3/H4-specific chaperone that facilitates histone
            deposition in vitro.
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Huang,C., He,C., Ruan,P. and Zhou,R.
  TITLE     TSPYL5 activates endoplasmic reticulum stress to inhibit cell
            proliferation, migration and invasion in colorectal cancer
  JOURNAL   Oncol Rep 44 (2), 449-456 (2020)
   PUBMED   32627024
  REMARK    GeneRIF: TSPYL5 activates endoplasmic reticulum stress to inhibit
            cell proliferation, migration and invasion in colorectal cancer.
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Episkopou,H., Diman,A., Claude,E., Viceconte,N. and Decottignies,A.
  TITLE     TSPYL5 Depletion Induces Specific Death of ALT Cells through
            USP7-Dependent Proteasomal Degradation of POT1
  JOURNAL   Mol Cell 75 (3), 469-482 (2019)
   PUBMED   31278054
  REMARK    GeneRIF: PML depletion suppressed POT1 poly-ubiquitination,
            suggesting an interplay between USP7 and PML to trigger POT1
            degradation in TSPYL5-depleted ALT(+) cells. We demonstrate that
            ALT telomeres need to be protected from POT1 degradation in
            ALT-associated PML bodies and identify TSPYL5 as an ALT(+)
            cancer-specific therapeutic target.
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Na,H.J., Yeum,C.E., Kim,H.S., Lee,J., Kim,J.Y. and Cho,Y.S.
  TITLE     TSPYL5-mediated inhibition of p53 promotes human endothelial cell
            function
  JOURNAL   Angiogenesis 22 (2), 281-293 (2019)
   PUBMED   30471052
  REMARK    GeneRIF: TSPYL5, a novel angiogenic regulator, plays a key role in
            maintaining endothelial integrity and function.
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Qiu,X., Hu,B., Huang,Y., Deng,Y., Wang,X. and Zheng,F.
  TITLE     Hypermethylation of ACP1, BMP4, and TSPYL5 in Hepatocellular
            Carcinoma and Their Potential Clinical Significance
  JOURNAL   Dig Dis Sci 61 (1), 149-157 (2016)
   PUBMED   26386860
  REMARK    GeneRIF: Suggest that hypermethylation of ACP1, BMP4, and TSPYL5
            are common events in HCC and could be used as potentially
            detectable biomarkers in HCC tissues.
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Liu,M., Ingle,J.N., Fridley,B.L., Buzdar,A.U., Robson,M.E.,
            Kubo,M., Wang,L., Batzler,A., Jenkins,G.D., Pietrzak,T.L.,
            Carlson,E.E., Goetz,M.P., Northfelt,D.W., Perez,E.A.,
            Williard,C.V., Schaid,D.J., Nakamura,Y. and Weinshilboum,R.M.
  TITLE     TSPYL5 SNPs: association with plasma estradiol concentrations and
            aromatase expression
  JOURNAL   Mol Endocrinol 27 (4), 657-670 (2013)
   PUBMED   23518928
  REMARK    GeneRIF: TSPYL5 knockdown decreased, and overexpression increased
            aromatase (CYP19A1) expression through the skin/adipose (I.4)
            promoter.
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Epping,M.T., Meijer,L.A., Krijgsman,O., Bos,J.L., Pandolfi,P.P. and
            Bernards,R.
  TITLE     TSPYL5 suppresses p53 levels and function by physical interaction
            with USP7
  JOURNAL   Nat Cell Biol 13 (1), 102-108 (2011)
   PUBMED   21170034
  REMARK    GeneRIF: Data identify TSPYL5 as a suppressor of p53 function
            through its interaction with USP7.
REFERENCE   9  (residues 1 to 417)
  AUTHORS   Kim,E.J., Lee,S.Y., Kim,T.R., Choi,S.I., Cho,E.W., Kim,K.C. and
            Kim,I.G.
  TITLE     TSPYL5 is involved in cell growth and the resistance to radiation
            in A549 cells via the regulation of p21(WAF1/Cip1) and PTEN/AKT
            pathway
  JOURNAL   Biochem Biophys Res Commun 392 (3), 448-453 (2010)
   PUBMED   20079711
  REMARK    GeneRIF: This study provides the first demonstration that TSPYL5
            modulates cell growth and sensitization of cells to the detrimental
            effects of damaging agents via regulation of p21(WAF1/Cip1) and
            PTEN/AKT pathway.
REFERENCE   10 (residues 1 to 417)
  AUTHORS   Jung,Y., Park,J., Bang,Y.J. and Kim,T.Y.
  TITLE     Gene silencing of TSPYL5 mediated by aberrant promoter methylation
            in gastric cancers
  JOURNAL   Lab Invest 88 (2), 153-160 (2008)
   PUBMED   18059362
  REMARK    GeneRIF: aberrant methylation at a CpG island of TSPYL5 may play an
            important role in development of gastric cancers
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC045630.1, AB051537.1 and AK091445.1.
            
            On Jun 29, 2004 this sequence version replaced NP_277047.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AB051537.1, SRR1803615.227473.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322128.5/ ENSP00000322802.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.1"
     Protein         1..417
                     /product="testis-specific Y-encoded-like protein 5"
                     /note="TSPY-like protein 5"
                     /calculated_mol_wt=45012
     Region          1..55
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VY4.2)"
     Region          93..112
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VY4.2)"
     Region          127..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VY4.2)"
     Region          213..382
                     /region_name="PTZ00007"
                     /note="(NAP-L) nucleosome assembly protein -L;
                     Provisional; cl08298"
                     /db_xref="CDD:471807"
     Region          391..417
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86VY4.2)"
     CDS             1..417
                     /gene="TSPYL5"
                     /coded_by="NM_033512.3:85..1338"
                     /db_xref="CCDS:CCDS34927.1"
                     /db_xref="GeneID:85453"
                     /db_xref="HGNC:HGNC:29367"
                     /db_xref="MIM:614721"
ORIGIN      
        1 msgrsrgrks sraknrgkgr akarvrpapd daprdpdpsq yqslgedtqa aqvqagagwg
       61 gleaaasaql lrlgeeaacr lpldcglalr araagdhgqa aarpgpgkaa slserlaadt
      121 vfvgtagtvg rpknaprvgn rrgpagkkap etcstagrgp qviaggrqkk gaagentsvs
      181 ageekkeerd agsgppateg smdtlenvql klenmnaqad raylrlsrkf gqlrlqhler
      241 rnhliqnipg fwgqafqnhp qlasflnsqe kevlsylnsl eveelglarl gykikfyfdr
      301 npyfqnkvli keygcgpsgq vvsrstpiqw lpghdlqsls qgnpennrsf fgwfsnhssi
      361 esdkiveiin eelwpnplqf yllsegarve kgkekegrqg pgkqpmettq pgvsqsn
//
LOCUS       NP_001277143             445 aa            linear   PRI 20-NOV-2025
DEFINITION  C-terminal-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001277143
VERSION     NP_001277143.1
DBSOURCE    REFSEQ: accession NM_001290214.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Pastoors,D., Havermans,M., Mulet-Lazaro,R., Brian,D., Noort,W.,
            Grasel,J., Hoogenboezem,R., Smeenk,L., Demmers,J.A.A., Milsom,M.D.,
            Enver,T., Groen,R.W.J., Bindels,E. and Delwel,R.
  TITLE     Oncogene EVI1 drives acute myeloid leukemia via a targetable
            interaction with CTBP2
  JOURNAL   Sci Adv 10 (20), eadk9076 (2024)
   PUBMED   38748792
  REMARK    GeneRIF: Oncogene EVI1 drives acute myeloid leukemia via a
            targetable interaction with CTBP2.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Cheung,C.H.Y., Cheng,C.K., Leung,K.T., Zhang,C., Ho,C.Y., Luo,X.,
            Kam,A.Y.F., Xia,T., Wan,T.S.K., Pitts,H.A., Chan,N.P.H.,
            Cheung,J.S., Wong,R.S.M., Zhang,X.B. and Ng,M.H.L.
  TITLE     C-terminal binding protein 2 is a novel tumor suppressor targeting
            the MYC-IRF4 axis in multiple myeloma
  JOURNAL   Blood Adv 8 (9), 2217-2234 (2024)
   PUBMED   38457926
  REMARK    GeneRIF: C-terminal binding protein 2 is a novel tumor suppressor
            targeting the MYC-IRF4 axis in multiple myeloma.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Sekiya,M., Ma,Y., Kainoh,K., Saito,K., Yamazaki,D., Tsuyuzaki,T.,
            Chen,W., Adi Putri,P.I.P., Ohno,H., Miyamoto,T., Takeuchi,Y.,
            Murayama,Y., Sugano,Y., Osaki,Y., Iwasaki,H., Yahagi,N., Suzuki,H.,
            Motomura,K., Matsuzaka,T., Murata,K., Mizuno,S., Takahashi,S. and
            Shimano,H.
  TITLE     Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function
  JOURNAL   Cell Rep 42 (8), 112914 (2023)
   PUBMED   37557182
  REMARK    GeneRIF: Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Holmes,M., Turner,J., Fox,A., Chisholm,O., Crossley,M. and Chong,B.
  TITLE     hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
            and modulates GATA-mediated activation
  JOURNAL   J Biol Chem 274 (33), 23491-23498 (1999)
   PUBMED   10438528
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and
            Otte,A.P.
  TITLE     C-Terminal binding protein is a transcriptional repressor that
            interacts with a specific class of vertebrate Polycomb proteins
  JOURNAL   Mol Cell Biol 19 (1), 777-787 (1999)
   PUBMED   9858600
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Turner,J. and Crossley,M.
  TITLE     Cloning and characterization of mCtBP2, a co-repressor that
            associates with basic Kruppel-like factor and other mammalian
            transcriptional regulators
  JOURNAL   EMBO J 17 (17), 5129-5140 (1998)
   PUBMED   9724649
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL157888.16, BM712328.1,
            BC052276.1 and AL731571.3.
            
            Summary: This gene produces alternative transcripts encoding two
            distinct proteins. One protein is a transcriptional repressor,
            while the other isoform is a major component of specialized
            synapses known as synaptic ribbons. Both proteins contain a NAD+
            binding domain similar to NAD+-dependent 2-hydroxyacid
            dehydrogenases. A portion of the 3' untranslated region was used to
            map this gene to chromosome 21q21.3; however, it was noted that
            similar loci elsewhere in the genome are likely. Blast analysis
            shows that this gene is present on chromosome 10. Several
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Feb 2014].
            
            Transcript Variant: This variant (4) contains a distinct 5' UTR and
            5' CDS, compared to variant 2. Variants 1, 3, 4, and 5-8 all encode
            the same isoform (1), which has a distinct N-terminus that is 540
            aa shorter than the N-terminus of isoform 2. The protein is thought
            to bind to the C-terminus of the adenovirus E1A proteins. Studies
            in mice suggest that this protein is involved in transcriptional
            repression.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052276.1, SRR14038196.1344679.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..445
                     /product="C-terminal-binding protein 2 isoform 1"
                     /note="ribeye"
                     /calculated_mol_wt=48814
     Site            22
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     Region          34..352
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(103,106..107,272,321,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(106,134,186..187,189..191,209..213,242..244,246,249,
                     270..272,296..297,321,323..324)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          414..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56545.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     CDS             1..445
                     /gene="CTBP2"
                     /coded_by="NM_001290214.3:448..1785"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS7643.1"
                     /db_xref="GeneID:1488"
                     /db_xref="HGNC:HGNC:2495"
                     /db_xref="MIM:602619"
ORIGIN      
        1 malvdkhkvk rqrldriceg irpqimngpl hprplvalld grdctvempi lkdlatvafc
       61 daqstqeihe kvlneavgam myhtitltre dlekfkalrv ivrigsgydn vdikaagelg
      121 iavcnipsaa veetadstic hilnlyrrnt wlyqalregt rvqsveqire vasgaarirg
      181 etlgligfgr tgqavavrak afgfsvifyd pylqdgiers lgvqrvytlq dllyqsdcvs
      241 lhcnlnehnh hlindftikq mrqgaflvna argglvdeka laqalkegri rgaaldvhes
      301 epfsfaqgpl kdapnlictp htawyseqas lemreaaate irraitgrip eslrncvnke
      361 ffvtsapwsv idqqaihpel ngatyryppg ivgvapgglp aamegiipgg ipvthnlptv
      421 ahpsqapspn qptkhgdnre hpneq
//
LOCUS       NP_005608                151 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein uS11 [Homo sapiens].
ACCESSION   NP_005608
VERSION     NP_005608.1
DBSOURCE    REFSEQ: accession NM_005617.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 151)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 151)
  AUTHORS   Han,L., Huo,Y., Huang,L., Zheng,Y., Yu,X., Zhang,N. and Yang,M.
  TITLE     Genome-wide functional integration identified MAZ-controlled RPS14
            dysregulation in hepatocellular carcinoma
  JOURNAL   Arch Toxicol 98 (3), 985-997 (2024)
   PUBMED   38189915
  REMARK    GeneRIF: Genome-wide functional integration identified
            MAZ-controlled RPS14 dysregulation in hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 151)
  AUTHORS   Hu,S., Cai,J., Fang,H., Chen,Z., Zhang,J. and Cai,R.
  TITLE     RPS14 promotes the development and progression of glioma via p53
            signaling pathway
  JOURNAL   Exp Cell Res 423 (1), 113451 (2023)
   PUBMED   36535509
  REMARK    GeneRIF: RPS14 promotes the development and progression of glioma
            via p53 signaling pathway.
REFERENCE   4  (residues 1 to 151)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 151)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 151)
  AUTHORS   Diaz,J.J. and Roufa,D.J.
  TITLE     Fine-structure map of the human ribosomal protein gene RPS14
  JOURNAL   Mol Cell Biol 12 (4), 1680-1686 (1992)
   PUBMED   1549121
REFERENCE   7  (residues 1 to 151)
  AUTHORS   Rhoads,D.D. and Roufa,D.J.
  TITLE     A cloned human ribosomal protein gene functions in rodent cells
  JOURNAL   Mol Cell Biol 7 (10), 3767-3774 (1987)
   PUBMED   3683397
REFERENCE   8  (residues 1 to 151)
  AUTHORS   Chen,I.T., Dixit,A., Rhoads,D.D. and Roufa,D.J.
  TITLE     Homologous ribosomal proteins in bacteria, yeast, and humans
  JOURNAL   Proc Natl Acad Sci U S A 83 (18), 6907-6911 (1986)
   PUBMED   3529092
REFERENCE   9  (residues 1 to 151)
  AUTHORS   Rhoads,D.D., Dixit,A. and Roufa,D.J.
  TITLE     Primary structure of human ribosomal protein S14 and the gene that
            encodes it
  JOURNAL   Mol Cell Biol 6 (8), 2774-2783 (1986)
   PUBMED   3785212
REFERENCE   10 (residues 1 to 151)
  AUTHORS   Dana,S. and Wasmuth,J.J.
  TITLE     Selective linkage disruption in human-Chinese hamster cell hybrids:
            deletion mapping of the leuS, hexB, emtB, and chr genes on human
            chromosome 5
  JOURNAL   Mol Cell Biol 2 (10), 1220-1228 (1982)
   PUBMED   7177110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC011388.7, BC006784.1 and AA467888.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 40S subunit. The protein belongs
            to the S11P family of ribosomal proteins. It is located in the
            cytoplasm. Transcript variants utilizing alternative transcription
            initiation sites have been described in the literature. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome. In
            Chinese hamster ovary cells, mutations in this gene can lead to
            resistance to emetine, a protein synthesis inhibitor. Multiple
            alternatively spliced transcript variants encoding the same protein
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) lacks a big segment in the 5'
            UTR, as compared to variant 1. Variants 1-3 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.119410.1,
                                           SRR1803613.205922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407193.7/ ENSP00000385425.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..151
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1"
     Protein         1..151
                     /product="small ribosomal subunit protein uS11"
                     /note="emetine resistance; 40S ribosomal protein S14"
                     /calculated_mol_wt=16142
     Region          1..140
                     /region_name="PTZ00129"
                     /note="40S ribosomal protein S14; Provisional"
                     /db_xref="CDD:185465"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P62263.3)"
     Region          131..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62263.3)"
     Site            133
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P62263.3)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62263.3)"
     CDS             1..151
                     /gene="RPS14"
                     /gene_synonym="EMTB; S14; uS11"
                     /coded_by="NM_005617.4:40..495"
                     /db_xref="CCDS:CCDS4307.1"
                     /db_xref="GeneID:6208"
                     /db_xref="HGNC:HGNC:10387"
                     /db_xref="MIM:130620"
ORIGIN      
        1 maprkgkekk eeqvislgpq vaegenvfgv chifasfndt fvhvtdlsgk eticrvtggm
       61 kvkadrdess pyaamlaaqd vaqrckelgi talhiklrat ggnrtktpgp gaqsalrala
      121 rsgmkigrie dvtpipsdst rrkggrrgrr l
//
LOCUS       NP_001355931             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001355931 XP_024303350
VERSION     NP_001355931.1
DBSOURCE    REFSEQ: accession NM_001369002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303350.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.199964.1,
                                           SRR3476690.153681.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369002.1:385..1149"
                     /note="isoform j is encoded by transcript variant 23"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001354251             434 aa            linear   PRI 20-NOV-2025
DEFINITION  CCA tRNA nucleotidyltransferase 1, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_001354251 XP_011532079
VERSION     NP_001354251.1
DBSOURCE    REFSEQ: accession NM_001367322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Meynier,V., Hardwick,S.W., Catala,M., Roske,J.J., Oerum,S.,
            Chirgadze,D.Y., Barraud,P., Yue,W.W., Luisi,B.F. and Tisne,C.
  TITLE     Structural basis for human mitochondrial tRNA maturation
  JOURNAL   Nat Commun 15 (1), 4683 (2024)
   PUBMED   38824131
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Fatica,T., Naas,T., Liwak,U., Slaa,H., Souaid,M., Frangione,B.,
            Kattini,R., Gaudreau-Lapierre,A., Trinkle-Mulcahy,L.,
            Chakraborty,P. and Holcik,M.
  TITLE     TRNT-1 Deficiency Is Associated with Loss of tRNA Integrity and
            Imbalance of Distinct Proteins
  JOURNAL   Genes (Basel) 14 (5), 1043 (2023)
   PUBMED   37239403
  REMARK    GeneRIF: TRNT-1 Deficiency Is Associated with Loss of tRNA
            Integrity and Imbalance of Distinct Proteins.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Seki,M., Komuro,A., Ishikawa,T., Takahashi,M. and Nashimoto,M.
  TITLE     Genes for tRNA recycling are upregulated in response to infection
            with Theiler's mouse encephalitis virus
  JOURNAL   Biochem Biophys Res Commun 587, 63-68 (2022)
   PUBMED   34864548
  REMARK    GeneRIF: Genes for tRNA recycling are upregulated in response to
            infection with Theiler's mouse encephalitis virus.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Odom,J., Amin,H., Gijavanekar,C., Elsea,S.H., Kralik,S., Chinen,J.,
            Lin,Y., Yates,A.M.M., Mizerik,E., Potocki,L. and Scaglia,F.
  TITLE     A phenotypic expansion of TRNT1 associated sideroblastic anemia
            with immunodeficiency, fevers, and developmental delay
  JOURNAL   Am J Med Genet A 188 (1), 259-268 (2022)
   PUBMED   34510712
  REMARK    GeneRIF: A phenotypic expansion of TRNT1 associated sideroblastic
            anemia with immunodeficiency, fevers, and developmental delay.
            Review article
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Augustin,M.A., Reichert,A.S., Betat,H., Huber,R., Morl,M. and
            Steegborn,C.
  TITLE     Crystal structure of the human CCA-adding enzyme: insights into
            template-independent polymerization
  JOURNAL   J Mol Biol 328 (5), 985-994 (2003)
   PUBMED   12729736
  REMARK    GeneRIF: The crystal structure reveals a four domain architecture
            with a cluster of conserved residues forming a positively charged
            cleft between the first two domains.
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Nagaike,T., Suzuki,T., Tomari,Y., Takemoto-Hori,C., Negayama,F.,
            Watanabe,K. and Ueda,T.
  TITLE     Identification and characterization of mammalian mitochondrial tRNA
            nucleotidyltransferases
  JOURNAL   J Biol Chem 276 (43), 40041-40049 (2001)
   PUBMED   11504732
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Reichert,A.S., Thurlow,D.L. and Morl,M.
  TITLE     A eubacterial origin for the human tRNA nucleotidyltransferase?
  JOURNAL   Biol Chem 382 (10), 1431-1438 (2001)
   PUBMED   11727826
  REMARK    GeneRIF: human gene transcript CGI-47 (#AF151805) was cloned and
            encodes a bona fide CCA-adding enzyme and not a poly(A) polymerase.
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024060.6.
            
            On Nov 21, 2018 this sequence version replaced XP_011532079.1.
            
            Summary: The protein encoded by this gene is a CCA-adding enzyme
            which belongs to the tRNA nucleotidyltransferase/poly(A) polymerase
            family. This essential enzyme functions by catalyzing the addition
            of the conserved nucleotide triplet CCA to the 3' terminus of tRNA
            molecules. Mutations in this gene result in sideroblastic anemia
            with B-cell immunodeficiency, periodic fevers, and developmental
            delay. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.178902.1,
                                           SRR1660805.83040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.2"
     Protein         1..434
                     /product="CCA tRNA nucleotidyltransferase 1, mitochondrial
                     isoform 1"
                     /EC_number="2.7.7.72"
                     /note="mitochondrial CCA-adding
                     tRNA-nucleotidyltransferase; tRNA nucleotidyl transferase,
                     CCA-adding, 1; tRNA-nucleotidyltransferase 1,
                     mitochondrial; CCA tRNA nucleotidyltransferase 1,
                     mitochondrial; mt CCA-adding enzyme; mt tRNA
                     CCA-diphosphorylase; mt tRNA adenylyltransferase; mt tRNA
                     CCA-pyrophosphorylase; tRNA CCA nucleotidyl transferase 1;
                     ATP(CTP):tRNA nucleotidyltransferase"
                     /calculated_mol_wt=44922
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=5224
     mat_peptide     42..434
                     /product="CCA tRNA nucleotidyltransferase 1,
                     mitochondrial. /id=PRO_0000004782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=44922
     Region          43..428
                     /region_name="PcnB"
                     /note="tRNA nucleotidyltransferase/poly(A) polymerase
                     [Translation, ribosomal structure and biogenesis];
                     COG0617"
                     /db_xref="CDD:440382"
     Site            152
                     /site_type="other"
                     /note="May assist in discriminating ATP from CTP.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB1; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            193
                     /site_type="other"
                     /note="Involved in nucleotide selection.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            402
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     CDS             1..434
                     /gene="TRNT1"
                     /gene_synonym="CCA1; CGI-47; MtCCA; RPEM; SIFD"
                     /coded_by="NM_001367322.1:378..1682"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS2561.2"
                     /db_xref="GeneID:51095"
                     /db_xref="HGNC:HGNC:17341"
                     /db_xref="MIM:612907"
ORIGIN      
        1 mlrclyhwhr pvlnrrwsrl clpkqylftm klqspefqsl fteglkslte lfvkenhelr
       61 iaggavrdll ngvkpqdidf attatptqmk emfqsagirm innrgekhgt itarlheenf
      121 eittlridvt tdgrhaevef ttdwqkdaer rdltinsmfl gfdgtlfdyf ngyedlknkk
      181 vrfvghakqr iqedylrilr yfrfygrivd kpgdhdpetl eaiaenakgl agisgeriwv
      241 elkkilvgnh vnhlihliyd ldvapyiglp anasleefdk vsknvdgfsp kpvtllaslf
      301 kvqddvtkld lrlkiakeek nlglfivknr kdlikatdss dplkpyqdfi idsrepdatt
      361 rvcellkyqg ehcllkemqq wsippfpvsg hdirkvgiss gkeigallqq lreqwkksgy
      421 qmekdellsy ikkt
//
LOCUS       NP_001122390             753 aa            linear   PRI 20-NOV-2025
DEFINITION  MAP/microtubule affinity-regulating kinase 3 isoform a [Homo
            sapiens].
ACCESSION   NP_001122390
VERSION     NP_001122390.2
DBSOURCE    REFSEQ: accession NM_001128918.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 753)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 753)
  AUTHORS   Aparicio-Bautista,D.I., Jimenez-Ortega,R.F., Becerra-Cervera,A.,
            Aquino-Galvez,A., de Leon-Suarez,V.P., Casas-Avila,L., Salmeron,J.,
            Hidalgo-Bravo,A., Rivera-Paredez,B. and Velazquez-Cruz,R.
  TITLE     Interaction between MARK3 (rs11623869), PLCB4 (rs6086746) and
            GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women
  JOURNAL   Front Endocrinol (Lausanne) 15, 1392063 (2024)
   PUBMED   38715801
  REMARK    GeneRIF: Interaction between MARK3 (rs11623869), PLCB4 (rs6086746)
            and GEMIN2 (rs2277458) variants with bone mineral density and serum
            25-hidroxivitamin D levels in Mexican Mestizo women.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 753)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 753)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 753)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 753)
  AUTHORS   Li,M.G., Katsura,K., Nomiyama,H., Komaki,K., Ninomiya-Tsuji,J.,
            Matsumoto,K., Kobayashi,T. and Tamura,S.
  TITLE     Regulation of the interleukin-1-induced signaling pathways by a
            novel member of the protein phosphatase 2C family (PP2Cepsilon)
  JOURNAL   J Biol Chem 278 (14), 12013-12021 (2003)
   PUBMED   12556533
REFERENCE   7  (residues 1 to 753)
  AUTHORS   Sun,T.Q., Lu,B., Feng,J.J., Reinhard,C., Jan,Y.N., Fantl,W.J. and
            Williams,L.T.
  TITLE     PAR-1 is a Dishevelled-associated kinase and a positive regulator
            of Wnt signalling
  JOURNAL   Nat Cell Biol 3 (7), 628-636 (2001)
   PUBMED   11433294
REFERENCE   8  (residues 1 to 753)
  AUTHORS   Peng,C.Y., Graves,P.R., Ogg,S., Thoma,R.S., Byrnes,M.J. 3rd, Wu,Z.,
            Stephenson,M.T. and Piwnica-Worms,H.
  TITLE     C-TAK1 protein kinase phosphorylates human Cdc25C on serine 216 and
            promotes 14-3-3 protein binding
  JOURNAL   Cell Growth Differ 9 (3), 197-208 (1998)
   PUBMED   9543386
REFERENCE   9  (residues 1 to 753)
  AUTHORS   Ono,T., Kawabe,T., Sonta,S. and Okamoto,T.
  TITLE     Assignment of MARK3 alias KP78 to human chromosome band 14q32.3 by
            in situ hybridization
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 101-102 (1997)
   PUBMED   9533022
REFERENCE   10 (residues 1 to 753)
  AUTHORS   Meller,N., Liu,Y.C., Collins,T.L., Bonnefoy-Berard,N., Baier,G.,
            Isakov,N. and Altman,A.
  TITLE     Direct interaction between protein kinase C theta (PKC theta) and
            14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition
            of PKC theta translocation and function
  JOURNAL   Mol Cell Biol 16 (10), 5782-5791 (1996)
   PUBMED   8816492
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA707357.1, AL133367.4,
            AF465413.1, BX248250.1 and BC024773.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 11, 2014 this sequence version replaced NP_001122390.1.
            
            Summary: The protein encoded by this gene is activated by
            phosphorylation and in turn is involved in the phosphorylation of
            tau proteins MAP2 and MAP4. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.154392.1,
                                           SRR1803613.163292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000429436.7/ ENSP00000411397.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..753
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.32-q32.33"
     Protein         1..753
                     /product="MAP/microtubule affinity-regulating kinase 3
                     isoform a"
                     /EC_number="2.7.11.1"
                     /note="EMK-2; C-TAK1; ELKL motif kinase 2; protein kinase
                     STK10; ser/Thr protein kinase PAR-1; cdc25C-associated
                     protein kinase 1; MAP/microtubule affinity-regulating
                     kinase 3; serine/threonine-protein kinase p78"
                     /calculated_mol_wt=84298
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27448.5)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Region          55..307
                     /region_name="STKc_MARK"
                     /note="Catalytic domain of the Serine/Threonine Kinases,
                     MAP/microtubule affinity-regulating kinases; cd14072"
                     /db_xref="CDD:270974"
     Site            order(62..66,70,83,85,116,132..135,139,141..142,144,
                     177..178,180,182..183,185,195..196,199,212..217,219,
                     249..252,254)
                     /site_type="active"
                     /db_xref="CDD:270974"
     Site            order(62..65,70,83,85,116,132..135,139,182..183,185,
                     195..196)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270974"
     Site            order(66,139,141,177..178,180,182,199,213..217,219)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270974"
     Site            195..217
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270974"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by LKB1.
                     /evidence=ECO:0000269|PubMed:14976552; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Region          325..367
                     /region_name="UBA_MARK3_4"
                     /note="UBA domain found in MAP/microtubule
                     affinity-regulating kinase MARK3, MARK4, and similar
                     proteins; cd14407"
                     /db_xref="CDD:270590"
     Site            368
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03141; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Region          370..600
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27448.5)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03141; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            383
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            469
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            543
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q03141; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P27448.5)"
     Site            564
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PKC/PRKCZ.
                     /evidence=ECO:0000269|PubMed:15084291; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            598
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Site            601
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Region          632..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27448.5)"
     Site            643
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P27448.5)"
     Region          654..751
                     /region_name="MARK1-3_C"
                     /note="C-terminal, kinase associated domain 1 (KA1), a
                     phospholipid binding domain, of microtubule
                     affinity-regulating kinases 1-3; cd12196"
                     /db_xref="CDD:213381"
     Site            order(656,659,729,731..732)
                     /site_type="other"
                     /note="putative phospholipid binding site [chemical
                     binding]"
                     /db_xref="CDD:213381"
     CDS             1..753
                     /gene="MARK3"
                     /gene_synonym="CTAK1; KP78; Par-1a; PAR1A; VIPB"
                     /coded_by="NM_001128918.3:616..2877"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45165.1"
                     /db_xref="GeneID:4140"
                     /db_xref="HGNC:HGNC:6897"
                     /db_xref="MIM:602678"
ORIGIN      
        1 mstrtplptv nerdtenhts hgdgrqevts rtsrsgarcr nsiascadeq phignyrllk
       61 tigkgnfakv klarhiltgr evaikiidkt qlnptslqkl frevrimkil nhpnivklfe
      121 vietektlyl imeyasggev fdylvahgrm kekearskfr qivsavqych qkrivhrdlk
      181 aenllldadm nikiadfgfs neftvggkld tfcgsppyaa pelfqgkkyd gpevdvwslg
      241 vilytlvsgs lpfdgqnlke lrervlrgky ripfymstdc enllkrflvl npikrgtleq
      301 imkdrwinag heedelkpfv epeldisdqk ridimvgmgy sqeeiqesls kmkydeitat
      361 ylllgrksse ldasdsssss nlslakvrps sdlnnstgqs phhkvqrsvs ssqkqrrysd
      421 hagpaipsvv aypkrsqtst adsdlkedgi ssrkssgsav ggkgiapasp mlgnasnpnk
      481 adiperkkss tvpssntasg gmtrrntyvc serttadrhs viqngkenst ipdqrtpvas
      541 thsissaatp drirfprgta srstfhgqpr errtatyngp paspslshea tplsqtrsrg
      601 stnlfsklts kltrrnmsfr fikrlpteye rngryegssr nvsaeqkden keakprslrf
      661 twsmkttssm dpgdmmreir kvldanncdy eqrerfllfc vhgdghaenl vqwemevckl
      721 prlslngvrf krisgtsiaf kniaskiane lkl
//
LOCUS       NP_036436                491 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_036436
VERSION     NP_036436.1
DBSOURCE    REFSEQ: accession NM_012304.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Camuzi,D., Buexm,L.A., Lourenco,S.Q.C., Grazziotin,R., Guaraldi,S.,
            Valverde,P., Rapozo,D., Brooks,J.M., Mehanna,H., Ribeiro Pinto,L.F.
            and Soares-Lima,S.C.
  TITLE     FBXL7 Body Hypomethylation Is Frequent in Tumors from the Digestive
            and Respiratory Tracts and Is Associated with Risk-Factor Exposure
  JOURNAL   Int J Mol Sci 23 (14), 7801 (2022)
   PUBMED   35887149
  REMARK    GeneRIF: FBXL7 Body Hypomethylation Is Frequent in Tumors from the
            Digestive and Respiratory Tracts and Is Associated with Risk-Factor
            Exposure.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Ni,J., Shen,L., Xu,L., Jin,Q. and Wang,G.
  TITLE     7-Ethoxyrosmanol alleviates hyperglycemia-induced vascular
            endothelial dysfunction by regulating FBXL7 expression
  JOURNAL   J Bioenerg Biomembr 53 (5), 553-560 (2021)
   PUBMED   34427826
  REMARK    GeneRIF: 7-Ethoxyrosmanol alleviates hyperglycemia-induced vascular
            endothelial dysfunction by regulating FBXL7 expression.
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Moro,L., Simoneschi,D., Kurz,E., Arbini,A.A., Jang,S.,
            Guaragnella,N., Giannattasio,S., Wang,W., Chen,Y.A., Pires,G.,
            Dang,A., Hernandez,E., Kapur,P., Mishra,A., Tsirigos,A., Miller,G.,
            Hsieh,J.T. and Pagano,M.
  TITLE     Epigenetic silencing of the ubiquitin ligase subunit FBXL7 impairs
            c-SRC degradation and promotes epithelial-to-mesenchymal transition
            and metastasis
  JOURNAL   Nat Cell Biol 22 (9), 1130-1142 (2020)
   PUBMED   32839549
  REMARK    GeneRIF: Epigenetic silencing of the ubiquitin ligase subunit FBXL7
            impairs c-SRC degradation and promotes epithelial-to-mesenchymal
            transition and metastasis.
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Venables,J.P., Bourgeois,C.F., Dalgliesh,C., Kister,L., Stevenin,J.
            and Elliott,D.J.
  TITLE     Up-regulation of the ubiquitous alternative splicing factor
            Tra2beta causes inclusion of a germ cell-specific exon
  JOURNAL   Hum Mol Genet 14 (16), 2289-2303 (2005)
   PUBMED   16000324
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Watanabe,N., Arai,H., Nishihara,Y., Taniguchi,M., Watanabe,N.,
            Hunter,T. and Osada,H.
  TITLE     M-phase kinases induce phospho-dependent ubiquitination of somatic
            Wee1 by SCFbeta-TrCP
  JOURNAL   Proc Natl Acad Sci U S A 101 (13), 4419-4424 (2004)
   PUBMED   15070733
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Ilyin,G.P., Rialland,M., Pigeon,C. and Guguen-Guillouzo,C.
  TITLE     cDNA cloning and expression analysis of new members of the
            mammalian F-box protein family
  JOURNAL   Genomics 67 (1), 40-47 (2000)
   PUBMED   10945468
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010477.8, AB020647.2 and
            BU633031.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by a 42-48 amino acid motif, the F-box,
            which binds to the S-phase kinase-associated protein 1 (Skp1)
            protein. The F-box proteins constitute one of the four subunits of
            E3 ubiquitin protein ligases called SCFs (SKP1-Cul1-F-box), which
            play a role in phosphorylation-dependent ubiquitination of
            proteins. The F-box proteins are divided into 3 subfamilies based
            on the other domain in the protein: F-box proteins that also have a
            WD-40 domain (Fbws subfamily), F-box proteins that also have
            leucine-rich repeats (Fbls subfamily) and F-box proteins that
            contain other motifs or lack known protein-interaction domains
            (Fbxs subfamily). The protein encoded by this gene belongs to the
            Fbls subfamily. Alternative splicing results in multiple transcript
            variants of this gene. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB020647.2, BC136424.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000504595.2/ ENSP00000423630.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.1"
     Protein         1..491
                     /product="F-box/LRR-repeat protein 7 isoform 1"
                     /note="F-box protein Fbl7; F-box/LRR-repeat protein 7"
                     /calculated_mol_wt=54444
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          114..157
                     /region_name="F-box_FBXL7"
                     /note="F-box domain found in F-box/LRR-repeat protein 7
                     (FBXL7) and similar proteins; cd22120"
                     /db_xref="CDD:438892"
     Site            order(117,121,124..125,128..129,133,135..136,140..142,144)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438892"
     Region          129..151
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          154..187
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          170..195
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          <185..366
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          188..213
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          196..221
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          214..234
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          222..247
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          240..273
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          253..281
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          274..299
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          282..307
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          297..464
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          300..325
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          308..333
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          326..351
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          334..359
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          352..377
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          360..385
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          378..403
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          386..411
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          404..429
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          412..437
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          430..453
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          438..463
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJT9.1)"
     Region          456..480
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..491
                     /gene="FBXL7"
                     /gene_synonym="FBL6; FBL7"
                     /coded_by="NM_012304.5:498..1973"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS54833.1"
                     /db_xref="GeneID:23194"
                     /db_xref="HGNC:HGNC:13604"
                     /db_xref="MIM:605656"
ORIGIN      
        1 mganngkqyg segkgsssis sdvssstdht ptkaqknvat sedsdlsmrt lstpspalic
       61 ppnlpgfqng rgsstssssi tgetvamvhs ppptrlthpl irlasrpqke qasidrlpdh
      121 smvqifsflp tnqlcrcarv crrwynlawd prlwrtirlt getinvdral kvltrrlcqd
      181 tpnvclmlet vtvsgcrrlt drglytiaqc cpelrrlevs gcynisneav fdvvslcpnl
      241 ehldvsgcsk vtcisltrea siklsplhgk qisiryldmt dcfvledegl htiaahctql
      301 thlylrrcvr ltdeglrylv iycasikels vsdcrfvsdf glreiakles rlrylsiahc
      361 grvtdvgiry vakycsklry lnargcegit dhgveylakn ctklksldig kcplvsdtgl
      421 eclalncfnl krlslksces itgqglqiva ancfdlqtln vqdcevsvea lrfvkrhckr
      481 cviehtnpaf f
//
LOCUS       NP_001287845             304 aa            linear   PRI 20-NOV-2025
DEFINITION  cAMP-dependent protein kinase catalytic subunit beta isoform 11
            [Homo sapiens].
ACCESSION   NP_001287845 XP_005271078
VERSION     NP_001287845.1
DBSOURCE    REFSEQ: accession NM_001300916.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Tanaka,M., Takeshita,K., Kunita,A., Hasegawa,K. and Ushiku,T.
  TITLE     PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic
            Papillary Neoplasms Including Those With Atypical Morphology: An
            Analysis of 22 Cases Expanding Morphologic Spectrum
  JOURNAL   Am J Surg Pathol 48 (8), 1032-1040 (2024)
   PUBMED   38841868
  REMARK    GeneRIF: PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal
            Oncocytic Papillary Neoplasms Including Those With Atypical
            Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum.
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Pei,W., Yin,W., Yu,T., Zhang,X., Zhang,Q., Yang,X., Shi,C., Shen,W.
            and Liu,G.
  TITLE     Dual-Specificity Phosphatase 4 Promotes Malignant Features in
            Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation
  JOURNAL   Dig Dis Sci 69 (8), 2856-2874 (2024)
   PUBMED   38824257
  REMARK    GeneRIF: Dual-Specificity Phosphatase 4 Promotes Malignant Features
            in Colorectal Cancer Through Cyclic-AMP Response Element Binding
            Protein/Protein Kinase CAMP-Activated Catalytic Subunit Beta
            Activation.
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Itoh,T., Omori,Y., Seino,M., Hirose,K., Date,F., Ono,Y.,
            Mizukami,Y., Aoki,S., Ishida,M., Mizuma,M., Morikawa,T.,
            Higuchi,R., Honda,G., Okamura,Y., Kinoshita,K., Unno,M. and
            Furukawa,T.
  TITLE     Gene Rearrangement and Expression of PRKACA and PRKACB Govern
            Morphobiology of Pancreatobiliary Oncocytic Neoplasms
  JOURNAL   Mod Pathol 37 (1), 100358 (2024)
   PUBMED   37871652
  REMARK    GeneRIF: Gene Rearrangement and Expression of PRKACA and PRKACB
            Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Maimaitiaili,Y., Fukumura,Y., Hirabayashi,K., Kinowaki,Y.,
            Naito,Y., Saito,A., Rong,L., Nakahodo,J. and Yao,T.
  TITLE     Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors
            of the pancreatobiliary and other systems
  JOURNAL   Virchows Arch 481 (6), 865-876 (2022)
   PUBMED   36152045
  REMARK    GeneRIF: Investigation of -PRKACA/-PRKACB fusion genes in oncocytic
            tumors of the pancreatobiliary and other systems.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Orstavik,S., Reinton,N., Frengen,E., Langeland,B.T., Jahnsen,T. and
            Skalhegg,B.S.
  TITLE     Identification of novel splice variants of the human catalytic
            subunit Cbeta of cAMP-dependent protein kinase
  JOURNAL   Eur J Biochem 268 (19), 5066-5073 (2001)
   PUBMED   11589697
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Scarpetta,M.A. and Uhler,M.D.
  TITLE     Evidence for two additional isoforms of the endogenous protein
            kinase inhibitor of cAMP-dependent protein kinase in mouse
  JOURNAL   J Biol Chem 268 (15), 10927-10931 (1993)
   PUBMED   7684369
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Da Silva,J.D., Tkachenko,N. and Soares,A.R.
  TITLE     Ellis-van Creveld Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   37903214
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum Genet 88 (6), 653-657 (1992)
   PUBMED   1551670
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol Endocrinol 4 (3), 465-475 (1990)
   PUBMED   2342480
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Taylor,S.S., Buechler,J.A. and Yonemoto,W.
  TITLE     cAMP-dependent protein kinase: framework for a diverse family of
            regulatory enzymes
  JOURNAL   Annu Rev Biochem 59, 971-1005 (1990)
   PUBMED   2165385
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC418574.1, BM905428.1,
            BC016285.1, BX369882.1 and AA761973.1.
            
            On Jul 16, 2014 this sequence version replaced XP_005271078.1.
            
            Summary: The protein encoded by this gene is a member of the
            serine/threonine protein kinase family. The encoded protein is a
            catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase,
            which mediates signalling though cAMP. cAMP signaling is important
            to a number of processes, including cell proliferaton and
            differentiation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2014].
            
            Transcript Variant: This variant (11) differs in the 3' exon
            structure, compared to variant 1. The encoded isoform (11) has a
            distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.346234.1,
                                           SRR7410570.16150.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..304
                     /product="cAMP-dependent protein kinase catalytic subunit
                     beta isoform 11"
                     /EC_number="2.7.11.11"
                     /note="protein kinase A catalytic subunit beta; protein
                     kinase, cAMP-dependent, catalytic, beta; protein kinase,
                     cAMP-dependent, beta catalytic subunit"
                     /calculated_mol_wt=35179
     Region          89..>302
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(97..100,103,105,118,120,152,168..171,214,218..219,
                     221,231..232)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..304
                     /gene="PRKACB"
                     /gene_synonym="CAFD2; PKA C-beta; PKACB"
                     /coded_by="NM_001300916.2:92..1006"
                     /note="isoform 11 is encoded by transcript variant 11"
                     /db_xref="GeneID:5567"
                     /db_xref="HGNC:HGNC:9381"
                     /db_xref="MIM:176892"
ORIGIN      
        1 maayreppcn qytgtttalq klegfasrlf hrhskgtahd qktalendsl hfsehtalwd
       61 rsmkeflaka kedflkkwen ptqnnagled ferkktlgtg sfgrvmlvkh kateqyyamk
      121 ildkqkvvkl kqiehtlnek rilqavnfpf lvrleyafkd nsnlymvmey vpggemfshl
      181 rrigrfseph arfyaaqivl tfeylhsldl iyrdlkpenl lidhqgyiqv tdfgfakrvk
      241 grtwtlcgtp eylapeiils kgynkavdww algvliyema agyppffadq piqiyekivs
      301 gknf
//
LOCUS       NP_002809                239 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome activator complex subunit 2 [Homo sapiens].
ACCESSION   NP_002809
VERSION     NP_002809.2
DBSOURCE    REFSEQ: accession NM_002818.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Li,R., Yan,L., Jiu,J., Liu,H., Li,D., Li,X., Zhang,J., Li,S.,
            Fan,Z., Lv,Z., Zhu,Y. and Wang,B.
  TITLE     PSME2 offers value as a biomarker of M1 macrophage infiltration in
            pan-cancer and inhibits osteosarcoma malignant phenotypes
  JOURNAL   Int J Biol Sci 20 (4), 1452-1470 (2024)
   PUBMED   38385075
  REMARK    GeneRIF: PSME2 offers value as a biomarker of M1 macrophage
            infiltration in pan-cancer and inhibits osteosarcoma malignant
            phenotypes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Ahn,K., Erlander,M., Leturcq,D., Peterson,P.A., Fruh,K. and Yang,Y.
  TITLE     In vivo characterization of the proteasome regulator PA28
  JOURNAL   J Biol Chem 271 (30), 18237-18242 (1996)
   PUBMED   8663520
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Ahn,J.Y., Tanahashi,N., Akiyama,K., Hisamatsu,H., Noda,C.,
            Tanaka,K., Chung,C.H., Shibmara,N., Willy,P.J., Mott,J.D. et al.
  TITLE     Primary structures of two homologous subunits of PA28, a
            gamma-interferon-inducible protein activator of the 20S proteasome
  JOURNAL   FEBS Lett 366 (1), 37-42 (1995)
   PUBMED   7789512
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Mott,J.D., Pramanik,B.C., Moomaw,C.R., Afendis,S.J., DeMartino,G.N.
            and Slaughter,C.A.
  TITLE     PA28, an activator of the 20 S proteasome, is composed of two
            nonidentical but homologous subunits
  JOURNAL   J Biol Chem 269 (50), 31466-31471 (1994)
   PUBMED   7989312
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Dubiel,W., Pratt,G., Ferrell,K. and Rechsteiner,M.
  TITLE     Purification of an 11 S regulator of the multicatalytic protease
  JOURNAL   J Biol Chem 267 (31), 22369-22377 (1992)
   PUBMED   1429590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136295.3.
            
            On May 7, 2003 this sequence version replaced NP_002809.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. The immunoproteasome
            contains an alternate regulator, referred to as the 11S regulator
            or PA28, that replaces the 19S regulator. Three subunits (alpha,
            beta and gamma) of the 11S regulator have been identified. This
            gene encodes the beta subunit of the 11S regulator, one of the two
            11S subunits that is induced by gamma-interferon. Three beta and
            three alpha subunits combine to form a heterohexameric ring. Six
            pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225876.1, BC004368.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000216802.10/ ENSP00000216802.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..239
                     /product="proteasome activator complex subunit 2"
                     /note="11S regulator complex beta subunit; proteasome
                     activator hPA28 subunit beta; proteasome activator
                     28-beta; MCP activator, 31-kD subunit; activator of
                     multicatalytic protease subunit 2; cell migration-inducing
                     protein 22; REG-beta; 11S regulator complex subunit beta;
                     proteasome activator 28 subunit beta; proteasome (prosome,
                     macropain) activator subunit 2 (PA28 beta)"
                     /calculated_mol_wt=27271
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UL46.4)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UL46.4)"
     Region          12..66
                     /region_name="PA28_alpha"
                     /note="Proteasome activator pa28 alpha subunit; pfam02251"
                     /db_xref="CDD:460507"
     Region          93..237
                     /region_name="PA28_beta"
                     /note="Proteasome activator pa28 beta subunit; pfam02252"
                     /db_xref="CDD:460508"
     CDS             1..239
                     /gene="PSME2"
                     /gene_synonym="PA28B; PA28beta; REGbeta"
                     /coded_by="NM_002818.3:30..749"
                     /db_xref="CCDS:CCDS9614.1"
                     /db_xref="GeneID:5721"
                     /db_xref="HGNC:HGNC:9569"
                     /db_xref="MIM:602161"
ORIGIN      
        1 makpcgvrls gearkqvevf rqnlfqeaee flyrflpqki iylnqllqed slnvadltsl
       61 rapldipipd pppkddemet dkqekkevhk cgflpgnekv lsllalvkpe vwtlkekcil
      121 vitwiqhlip kiedgndfgv aiqekvlerv navktkveaf qttiskyfse rgdavakask
      181 ethvmdyral vherdeaayg elramvldlr afyaelyhii ssnlekivnp kgeekpsmy
//
LOCUS       NP_001003395             175 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor protein D53 isoform 2 [Homo sapiens].
ACCESSION   NP_001003395
VERSION     NP_001003395.1
DBSOURCE    REFSEQ: accession NM_001003395.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Nourse,C.R., Mattei,M.G., Gunning,P. and Byrne,J.A.
  TITLE     Cloning of a third member of the D52 gene family indicates
            alternative coding sequence usage in D52-like transcripts
  JOURNAL   Biochim Biophys Acta 1443 (1-2), 155-168 (1998)
   PUBMED   9838088
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Byrne,J.A., Mattei,M.G., Basset,P. and Gunning,P.
  TITLE     Identification and in situ hybridization mapping of a mouse Tpd52l1
            (D53) orthologue to chromosome 10A4-B2
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 199-201 (1998)
   PUBMED   9730602
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK124817.1, U44428.1, U44429.1,
            AL121938.10 and AI222450.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contain coiled-coil domains and may form hetero- or homomers. The
            encoded protein is involved in cell proliferation and calcium
            signaling. It also interacts with the mitogen-activated protein
            kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates
            MAP3K5-induced apoptosis. Multiple alternatively spliced transcript
            variants have been observed. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (2) has a shorter N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ928174.1, BQ928925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..175
                     /product="tumor protein D53 isoform 2"
                     /note="tumor protein D53; tumor protein D52 like 1"
                     /calculated_mol_wt=19325
     Region          15..122
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     CDS             1..175
                     /gene="TPD52L1"
                     /gene_synonym="D53; TPD53"
                     /coded_by="NM_001003395.3:356..883"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43502.1"
                     /db_xref="GeneID:7164"
                     /db_xref="HGNC:HGNC:12006"
                     /db_xref="MIM:604069"
ORIGIN      
        1 mlseeekeel kaelvqlede ittlrqvlsa kerhlveikq klgmnlmnel kqnfskswhd
       61 mqtttaykkt hetlshagqk ataafsnvgt aiskkfgdms ysirhsismp amrnsptfks
      121 feervettvt slktkvggtn pnggsfeevl sstahasaqs laggsrrtke eelqc
//
LOCUS       NP_001305789             180 aa            linear   PRI 20-NOV-2025
DEFINITION  deoxyguanosine kinase, mitochondrial isoform d [Homo sapiens].
ACCESSION   NP_001305789 XP_005264230
VERSION     NP_001305789.1
DBSOURCE    REFSEQ: accession NM_001318860.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Guzman,H., Yazdani,S., Harmon,J.L., Chapman,K.A., Vitola,B.,
            Pyle,L., McKnight,H., Sigal,W., Lord,K., De Leon,D.D., Merchant,N.
            and Ganetzky,R.
  TITLE     Case report: Two unexpected cases of DGUOK-related mitochondrial
            DNA depletion syndrome presenting with hyperinsulinemic
            hypoglycemia
  JOURNAL   Front Endocrinol (Lausanne) 14, 1268135 (2023)
   PUBMED   38027095
  REMARK    GeneRIF: Case report: Two unexpected cases of DGUOK-related
            mitochondrial DNA depletion syndrome presenting with
            hyperinsulinemic hypoglycemia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Unal,O., Hismi,B., Kilic,M., Gulsen,H.H., Coskun,T., Sivri,S.H.,
            Dursun,A., Yuce,A. and Tokatli,A.
  TITLE     Deoxyguanosine kinase deficiency: a report of four patients
  JOURNAL   J Pediatr Endocrinol Metab 30 (6), 697-702 (2017)
   PUBMED   28493820
  REMARK    GeneRIF: DGUOK deficiency and mutation is associated with
            mitochondrial DNA depletion syndromes.
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Jullig,M. and Eriksson,S.
  TITLE     Mitochondrial and submitochondrial localization of human
            deoxyguanosine kinase
  JOURNAL   Eur J Biochem 267 (17), 5466-5472 (2000)
   PUBMED   10951205
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Johansson,M., Bajalica-Lagercrantz,S., Lagercrantz,J. and
            Karlsson,A.
  TITLE     Localization of the human deoxyguanosine kinase gene (DGUOK) to
            chromosome 2p13
  JOURNAL   Genomics 38 (3), 450-451 (1996)
   PUBMED   8975728
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Wang,L., Hellman,U. and Eriksson,S.
  TITLE     Cloning and expression of human mitochondrial deoxyguanosine kinase
            cDNA
  JOURNAL   FEBS Lett 390 (1), 39-43 (1996)
   PUBMED   8706825
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning and expression of human deoxyguanosine kinase cDNA
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7258-7262 (1996)
   PUBMED   8692979
REFERENCE   10 (residues 1 to 180)
  AUTHORS   El-Hattab,A.W. and Scaglia,F.
  TITLE     Deoxyguanosine Kinase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301766
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU099795.1, AC073046.7,
            BG470729.1 and U41668.1.
            
            On Jan 14, 2016 this sequence version replaced XP_005264230.1.
            
            Summary: In mammalian cells, the phosphorylation of purine
            deoxyribonucleosides is mediated predominantly by two
            deoxyribonucleoside kinases, cytosolic deoxycytidine kinase and
            mitochondrial deoxyguanosine kinase. The protein encoded by this
            gene is responsible for phosphorylation of purine
            deoxyribonucleosides in the mitochondrial matrix. In addition, this
            protein phosphorylates several purine deoxyribonucleoside analogs
            used in the treatment of lymphoproliferative disorders, and this
            phosphorylation is critical for the effectiveness of the analogs.
            Alternative splice variants encoding different protein isoforms
            have been described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) lacks an alternate exon
            compared to variant 1. The resulting isoform (d) is shorter at the
            N-terminus compared to isoform a. Variants 4 and 5 both encode the
            same isoform (d).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.41318.1,
                                           SRR1163657.202615.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..180
                     /product="deoxyguanosine kinase, mitochondrial isoform d"
                     /EC_number="2.7.1.113"
                     /EC_number="2.7.1.76"
                     /note="deoxyguanosine kinase, mitochondrial;
                     deoxyadenosine kinase, mitochondrial"
                     /calculated_mol_wt=21577
     Region          1..178
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            21
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..180
                     /gene="DGUOK"
                     /gene_synonym="dGK; MTDPS3; NCPH; NCPH1; PEOB4"
                     /coded_by="NM_001318860.2:210..752"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:1716"
                     /db_xref="HGNC:HGNC:2858"
                     /db_xref="MIM:601465"
ORIGIN      
        1 mmyreparws ytfqtfsfls rlkvqlepfp ekllqarkpv qifersvysd ryifaknlfe
       61 ngslsdiewh iyqdwhsfll wefasritlh gfiylqaspq vclkrlyqra reeekgiela
      121 yleqlhgqhe awlihkttkl hfealmnipv lvldvnddfs eevtkqedlm revntfvknl
//
LOCUS       NP_001339536             655 aa            linear   PRI 20-NOV-2025
DEFINITION  propionyl-CoA carboxylase alpha chain, mitochondrial isoform f
            [Homo sapiens].
ACCESSION   NP_001339536 XP_016876103
VERSION     NP_001339536.1
DBSOURCE    REFSEQ: accession NM_001352607.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 655)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 655)
  AUTHORS   Wang,J., Cui,M., Liu,Y., Chen,M., Xu,J., Xia,J., Sun,J., Jiang,L.,
            Fang,W., Song,H. and Cheng,C.
  TITLE     The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival
  JOURNAL   Appl Environ Microbiol 90 (6), e0213523 (2024)
   PUBMED   38727222
  REMARK    GeneRIF: The mitochondrial carboxylase PCCA interacts with Listeria
            monocytogenes phospholipase PlcB to modulate bacterial survival.
REFERENCE   3  (residues 1 to 655)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 655)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 655)
  AUTHORS   Bychkov,I., Galushkin,A., Filatova,A., Nekrasov,A., Kurkina,M.,
            Baydakova,G., Ilyushkina,A., Skoblov,M. and Zakharova,E.
  TITLE     Functional Analysis of the PCCA and PCCB Gene Variants Predicted to
            Affect Splicing
  JOURNAL   Int J Mol Sci 22 (8), 4154 (2021)
   PUBMED   33923806
  REMARK    GeneRIF: Functional Analysis of the PCCA and PCCB Gene Variants
            Predicted to Affect Splicing.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 655)
  AUTHORS   Galarreta Aima,C.I., Shchelochkov,O.A., Jerves Serrano,T. and
            Venditti,C.P.
  TITLE     Propionic Acidemia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22593918
REFERENCE   7  (residues 1 to 655)
  AUTHORS   Kennerknecht,I., Klett,C. and Hameister,H.
  TITLE     Assignment of the human gene propionyl coenzyme A carboxylase,
            alpha-chain, (PCCA) to chromosome 13q32 by in situ hybridization
  JOURNAL   Genomics 14 (2), 550-551 (1992)
   PUBMED   1427880
REFERENCE   8  (residues 1 to 655)
  AUTHORS   Lamhonwah,A.M., Mahuran,D. and Gravel,R.A.
  TITLE     Human mitochondrial propionyl-CoA carboxylase: localization of the
            N-terminus of the pro- and mature alpha chains in the deduced
            primary sequence of a full-length cDNA
  JOURNAL   Nucleic Acids Res 17 (11), 4396 (1989)
   PUBMED   2740237
REFERENCE   9  (residues 1 to 655)
  AUTHORS   Lamhonwah,A.M., Quan,F. and Gravel,R.A.
  TITLE     Sequence homology around the biotin-binding site of human
            propionyl-CoA carboxylase and pyruvate carboxylase
  JOURNAL   Arch Biochem Biophys 254 (2), 631-636 (1987)
   PUBMED   3555348
REFERENCE   10 (residues 1 to 655)
  AUTHORS   Lamhonwah,A.M., Barankiewicz,T.J., Willard,H.F., Mahuran,D.J.,
            Quan,F. and Gravel,R.A.
  TITLE     Isolation of cDNA clones coding for the alpha and beta chains of
            human propionyl-CoA carboxylase: chromosomal assignments and DNA
            polymorphisms associated with PCCA and PCCB genes
  JOURNAL   Proc Natl Acad Sci U S A 83 (13), 4864-4868 (1986)
   PUBMED   3460076
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355338.33, AL356575.8,
            AL353697.21 and AL136526.27.
            
            On Jun 18, 2017 this sequence version replaced XP_016876103.1.
            
            Summary: The protein encoded by this gene is the alpha subunit of
            the heterodimeric mitochondrial enzyme Propionyl-CoA carboxylase.
            PCCA encodes the biotin-binding region of this enzyme. Mutations in
            either PCCA or PCCB (encoding the beta subunit) lead to an enzyme
            deficiency resulting in propionic acidemia. Multiple transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, May 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.514847.1,
                                           SRR1803614.171617.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q32.3"
     Protein         1..655
                     /product="propionyl-CoA carboxylase alpha chain,
                     mitochondrial isoform f"
                     /EC_number="6.4.1.3"
                     /note="propionyl Coenzyme A carboxylase, alpha
                     polypeptide; propionyl-CoA carboxylase alpha chain,
                     mitochondrial; PCCase alpha subunit; propanoyl-CoA:carbon
                     dioxide ligase alpha subunit; pccA complementation group;
                     propionyl-CoA carboxylase alpha subunit; propionyl CoA
                     carboxylase, alpha polypeptide"
                     /calculated_mol_wt=71860
     Region          37..486
                     /region_name="PccA"
                     /note="Acetyl/propionyl-CoA carboxylase, alpha subunit
                     [Lipid transport and metabolism]; COG4770"
                     /db_xref="CDD:443802"
     Region          499..608
                     /region_name="PCC_BT"
                     /note="Propionyl-coenzyme A carboxylase BT domain;
                     pfam18140"
                     /db_xref="CDD:465666"
     Region          <605..654
                     /region_name="biotinyl_domain"
                     /note="The biotinyl-domain or biotin carboxyl carrier
                     protein (BCCP) domain is present in all biotin-dependent
                     enzymes, such as acetyl-CoA carboxylase, pyruvate
                     carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA
                     carboxylase, geranyl-CoA carboxylase; cd06850"
                     /db_xref="CDD:133459"
     Site            order(611,620..622,629)
                     /site_type="active"
                     /note="carboxyltransferase (CT) interaction site [active]"
                     /db_xref="CDD:133459"
     Site            621
                     /site_type="other"
                     /note="biotinylation site [posttranslational
                     modification]"
                     /db_xref="CDD:133459"
     CDS             1..655
                     /gene="PCCA"
                     /coded_by="NM_001352607.2:29..1996"
                     /note="isoform f is encoded by transcript variant 6"
                     /db_xref="GeneID:5095"
                     /db_xref="HGNC:HGNC:8653"
                     /db_xref="MIM:232000"
ORIGIN      
        1 magfwvgtap lvaagrrgrw ppqqlmlsaa lrtlktfdki lvanrgeiac rvirtckkmg
       61 iktvaihsdv dassvhvkma deavcvgpap tsksylnmda imeaikktra qavhpgygfl
      121 senkefarcl aaedvvfigp dthaiqamgd kieskllakk aevntipgfd gvvkdaeeav
      181 riareigypv mikasagggg kgmriawdde etrdgfrlss qeaassfgdd rlliekfidn
      241 prhieiqvlg dkhgnalwln erecsiqrrn qkvveeapsi fldaetrram geqavalara
      301 vkyssagtve flvdskknfy flemntrlqv ehpvtecitg ldlvqemirv akgyplrhkq
      361 adiringwav ecrvyaedpy ksfglpsigr lsqyqeplhl pgvrvdsgiq pgsdisiyyd
      421 pmisklityg sdrtealkrm adaldnyvir gvthniallr eviinsrfvk gdistkflsd
      481 vypdgfkghm ltkseknqll aiasslfvaf qlraqhfqen srmpvikpdi anwelsvklh
      541 dkvhtvvasn ngsvfsvevd gsklnvtstw nlaspllsvs vdgtqrtvqc lsreaggnms
      601 iqflgtvvae gqeicvieam kmqnsmtagk tgtvksvhcq agdtvgegdl lvele
//
LOCUS       NP_036331                857 aa            linear   PRI 20-NOV-2025
DEFINITION  protein argonaute-1 isoform 1 [Homo sapiens].
ACCESSION   NP_036331
VERSION     NP_036331.1
DBSOURCE    REFSEQ: accession NM_012199.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Fang,X., Ren,L.H., Shrestha,S.M., Ji,Q., Xu,Z., Wang,D., Ding,Q.,
            Liang,X. and Shi,R.H.
  TITLE     LINC01116 modulates EMT process via binding with AGO1 mRNA in
            oesophageal squamous cell carcinoma
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1870 (5), 119447 (2023)
   PUBMED   36990227
  REMARK    GeneRIF: LINC01116 modulates EMT process via binding with AGO1 mRNA
            in oesophageal squamous cell carcinoma.
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Kowalczyk,M., Kowalczyk,E., Galita,G., Majsterek,I., Talarowska,M.,
            Poplawski,T., Kwiatkowski,P., Lichota,A. and Sienkiewicz,M.
  TITLE     Association of Polymorphic Variants in Argonaute Genes with
            Depression Risk in a Polish Population
  JOURNAL   Int J Mol Sci 23 (18), 10586 (2022)
   PUBMED   36142498
  REMARK    GeneRIF: Association of Polymorphic Variants in Argonaute Genes
            with Depression Risk in a Polish Population.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 857)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 857)
  AUTHORS   Carmell,M.A., Xuan,Z., Zhang,M.Q. and Hannon,G.J.
  TITLE     The Argonaute family: tentacles that reach into RNAi, developmental
            control, stem cell maintenance, and tumorigenesis
  JOURNAL   Genes Dev 16 (21), 2733-2742 (2002)
   PUBMED   12414724
  REMARK    Review article
REFERENCE   7  (residues 1 to 857)
  AUTHORS   Martinez,J., Patkaniowska,A., Urlaub,H., Luhrmann,R. and Tuschl,T.
  TITLE     Single-stranded antisense siRNAs guide target RNA cleavage in RNAi
  JOURNAL   Cell 110 (5), 563-574 (2002)
   PUBMED   12230974
REFERENCE   8  (residues 1 to 857)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
REFERENCE   9  (residues 1 to 857)
  AUTHORS   Koesters,R., Adams,V., Betts,D., Moos,R., Schmid,M., Siermann,A.,
            Hassam,S., Weitz,S., Lichter,P., Heitz,P.U., von Knebel
            Doeberitz,M. and Briner,J.
  TITLE     Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence,
            genomic organization, localization to chromosomal bands 1p34-p35,
            and expression
  JOURNAL   Genomics 61 (2), 210-218 (1999)
   PUBMED   10534406
REFERENCE   10 (residues 1 to 857)
  AUTHORS   Reddy,P.H., Stockburger,E., Gillevet,P. and Tagle,D.A.
  TITLE     Mapping and characterization of novel (CAG)n repeat cDNAs from
            adult human brain derived by the oligo capture method
  JOURNAL   Genomics 46 (2), 174-182 (1997)
   PUBMED   9417904
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY052874.1, BC063275.1,
            AK314148.1, AF093097.1, CR936823.1 and AL139286.13.
            
            Summary: This gene encodes a member of the argonaute family of
            proteins, which associate with small RNAs and have important roles
            in RNA interference (RNAi) and RNA silencing. This protein binds to
            microRNAs (miRNAs) or small interfering RNAs (siRNAs) and represses
            translation of mRNAs that are complementary to them. It is also
            involved in transcriptional gene silencing (TGS) of promoter
            regions that are complementary to bound short antigene RNAs
            (agRNAs), as well as in the degradation of miRNA-bound mRNA
            targets. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. A recent study
            showed this gene to be an authentic stop codon readthrough target,
            and that its mRNA could give rise to an additional C-terminally
            extended isoform by use of an alternative in-frame translation
            termination codon. [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UAG termination codon. This
            RefSeq represents the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF093097.1, BC063275.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373204.6/ ENSP00000362300.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..857
                     /product="protein argonaute-1 isoform 1"
                     /note="Golgi Endoplasmic Reticulum protein 95 kDa;
                     putative RNA-binding protein Q99; protein argonaute-1;
                     eIF2C 1; eIF-2C 1; argonaute1; eukaryotic translation
                     initiation factor 2C, 1; argonaute 1, RISC catalytic
                     component; argonaute RISC catalytic component 1"
                     /calculated_mol_wt=97084
     Region          34..164
                     /region_name="ArgoN"
                     /note="N-terminal domain of argonaute; pfam16486"
                     /db_xref="CDD:465134"
     Region          174..224
                     /region_name="ArgoL1"
                     /note="Argonaute linker 1 domain; pfam08699"
                     /db_xref="CDD:462567"
     Region          225..345
                     /region_name="PAZ_argonaute_like"
                     /note="PAZ domain, argonaute_like subfamily. Argonaute is
                     part of the RNA-induced silencing complex (RISC), and is
                     an endonuclease that plays a key role in the RNA
                     interference pathway. The PAZ domain has been named after
                     the proteins Piwi,Argonaut, and Zwille; cd02846"
                     /db_xref="CDD:239212"
     Site            order(277,292,306,310,328,335,337)
                     /site_type="other"
                     /note="nucleic acid-binding interface [nucleotide
                     binding]"
                     /db_xref="CDD:239212"
     Region          309..314
                     /region_name="Interaction with guide RNA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     Region          390..815
                     /region_name="Piwi_ago-like"
                     /note="PIWI domain, Argonaute-like subfamily. Argonaute is
                     the central component of the RNA-induced silencing complex
                     (RISC) and related complexes. The PIWI domain is the
                     C-terminal portion of Argonaute and consists of two
                     subdomains, one of which provides the...; cd04657"
                     /db_xref="CDD:240015"
     Region          522..564
                     /region_name="Interaction with guide RNA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     Site            order(527,531,543..546,549,557,560,564,568)
                     /site_type="active"
                     /note="5' RNA guide strand anchoring site [active]"
                     /db_xref="CDD:240015"
     Site            order(595,597,667,805)
                     /site_type="active"
                     /db_xref="CDD:240015"
     Region          670..675
                     /region_name="Impairs access of bound RNA to the active
                     site"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     Region          708..712
                     /region_name="Interaction with guide RNA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     Region          751..759
                     /region_name="Interaction with guide RNA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     Region          788..813
                     /region_name="Interaction with guide RNA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UL18.3)"
     CDS             1..857
                     /gene="AGO1"
                     /gene_synonym="EIF2C; EIF2C1; GERP95; hAgo1; NEDLBAS; Q99"
                     /coded_by="NM_012199.5:214..2787"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS398.1"
                     /db_xref="GeneID:26523"
                     /db_xref="HGNC:HGNC:3262"
                     /db_xref="MIM:606228"
ORIGIN      
        1 meagpsgaaa gaylpplqqv fqaprrpgig tvgkpiklla nyfevdipki dvyhyevdik
       61 pdkcprrvnr evveymvqhf kpqifgdrkp vydgkkniyt vtalpigner vdfevtipge
      121 gkdrifkvsi kwlaivswrm lhealvsgqi pvplesvqal dvamrhlasm rytpvgrsff
      181 sppegyyhpl gggrevwfgf hqsvrpamwk mmlnidvsat afykaqpvie fmcevldirn
      241 ideqpkpltd sqrvrftkei kglkvevthc gqmkrkyrvc nvtrrpashq tfplqlesgq
      301 tvectvaqyf kqkynlqlky phlpclqvgq eqkhtylple vcnivagqrc ikkltdnqts
      361 tmikatarsa pdrqeeisrl mknasynldp yiqefgikvk ddmtevtgrv lpapilqygg
      421 rnraiatpnq gvwdmrgkqf yngieikvwa iacfapqkqc reevlknftd qlrkiskdag
      481 mpiqgqpcfc kyaqgadsve pmfrhlknty sglqliivil pgktpvyaev krvgdtllgm
      541 atqcvqvknv vktspqtlsn lclkinvklg ginnilvphq rsavfqqpvi flgadvthpp
      601 agdgkkpsit avvgsmdahp srycatvrvq rprqeiiedl symvrelliq fykstrfkpt
      661 riifyrdgvp egqlpqilhy ellairdaci klekdyqpgi tyivvqkrhh trlfcadkne
      721 rigksgnipa gttvdtnith pfefdfylcs hagiqgtsrp shyyvlwddn rftadelqil
      781 tyqlchtyvr ctrsvsipap ayyarlvafr aryhlvdkeh dsgegshisg qsngrdpqal
      841 akavqvhqdt lrtmyfa
//
LOCUS       NP_001129602             714 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid-beta precursor protein isoform f precursor [Homo sapiens].
ACCESSION   NP_001129602
VERSION     NP_001129602.1
DBSOURCE    REFSEQ: accession NM_001136130.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 714)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 714)
  AUTHORS   Majernikova,N., Marmolejo-Garza,A., Salinas,C.S., Luu,M.D.A.,
            Zhang,Y., Trombetta-Lima,M., Tomin,T., Birner-Gruenberger,R.,
            Lehtonen,S., Koistinaho,J., Wolters,J.C., Ayton,S., den
            Dunnen,W.F.A. and Dolga,A.M.
  TITLE     The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression
  JOURNAL   Cell Death Dis 15 (10), 782 (2024)
   PUBMED   39468028
  REMARK    GeneRIF: The link between amyloid beta and ferroptosis pathway in
            Alzheimer's disease progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 714)
  AUTHORS   Munch,N.S., Das,S. and Seeger,S.
  TITLE     Unveiling the effect of CaCl2 on amyloid beta aggregation via
            supercritical angle Raman and fluorescence spectroscopy and
            microscopy
  JOURNAL   Phys Chem Chem Phys 26 (41), 26266-26276 (2024)
   PUBMED   39371012
  REMARK    GeneRIF: Unveiling the effect of CaCl2 on amyloid beta aggregation
            via supercritical angle Raman and fluorescence spectroscopy and
            microscopy.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 714)
  AUTHORS   Tsoy,A., Umbayev,B., Kassenova,A., Kaupbayeva,B. and Askarova,S.
  TITLE     Pathology of Amyloid-beta (Abeta) Peptide Peripheral Clearance in
            Alzheimer's Disease
  JOURNAL   Int J Mol Sci 25 (20), 10964 (2024)
   PUBMED   39456746
  REMARK    GeneRIF: Pathology of Amyloid-beta (Abeta) Peptide Peripheral
            Clearance in Alzheimer's Disease.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 714)
  AUTHORS   Soscia,S.J., Kirby,J.E., Washicosky,K.J., Tucker,S.M.,
            Ingelsson,M., Hyman,B., Burton,M.A., Goldstein,L.E., Duong,S.,
            Tanzi,R.E. and Moir,R.D.
  TITLE     The Alzheimer's disease-associated amyloid beta-protein is an
            antimicrobial peptide
  JOURNAL   PLoS One 5 (3), e9505 (2010)
   PUBMED   20209079
  REMARK    GeneRIF: Alzheimer's disease-associated amyloid beta-protein
            peptides display antimicrobial activity against C. albicans, E.
            coli, S. epidermidis, S. pneumoniae, S. aureus, L. monocytogenes,
            E. faecalis, and S. agalactiae.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 714)
  AUTHORS   Bird,T.D.
  TITLE     Early-Onset Familial Alzheimer Disease - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301414
REFERENCE   7  (residues 1 to 714)
  AUTHORS   Bird,T.D.
  TITLE     Alzheimer Disease Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301340
REFERENCE   8  (residues 1 to 714)
  AUTHORS   Mant,R., Asherson,P., Gill,M., McGuffin,P., Owen,M., Wert,S.E.,
            Gregory,R.J., Smith,A.E., Cohn,J.A., Wilson,J.M. et al.
  TITLE     Schizophrenia scepticism
  JOURNAL   Nat Genet 2 (1), 12 (1992)
   PUBMED   1303244
REFERENCE   9  (residues 1 to 714)
  AUTHORS   Mullan,M., Crawford,F., Axelman,K., Houlden,H., Lilius,L.,
            Winblad,B. and Lannfelt,L.
  TITLE     A pathogenic mutation for probable Alzheimer's disease in the APP
            gene at the N-terminus of beta-amyloid
  JOURNAL   Nat Genet 1 (5), 345-347 (1992)
   PUBMED   1302033
REFERENCE   10 (residues 1 to 714)
  AUTHORS   Hendriks,L., van Duijn,C.M., Cras,P., Cruts,M., Van Hul,W., van
            Harskamp,F., Warren,A., McInnis,M.G., Antonarakis,S.E., Martin,J.J.
            et al.
  TITLE     Presenile dementia and cerebral haemorrhage linked to a mutation at
            codon 692 of the beta-amyloid precursor protein gene
  JOURNAL   Nat Genet 1 (3), 218-221 (1992)
   PUBMED   1303239
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI559391.1, AK294534.1,
            BC065523.1, BC065529.1 and BM876312.1.
            
            Summary: This gene encodes a cell surface receptor and
            transmembrane precursor protein that is cleaved by secretases to
            form a number of peptides. Some of these peptides are secreted and
            can bind to the acetyltransferase complex APBB1/TIP60 to promote
            transcriptional activation, while others form the protein basis of
            the amyloid plaques found in the brains of patients with Alzheimer
            disease. In addition, two of the peptides are antimicrobial
            peptides, having been shown to have bacteriocidal and antifungal
            activities. Mutations in this gene have been implicated in
            autosomal dominant Alzheimer disease and cerebroarterial
            amyloidosis (cerebral amyloid angiopathy). Multiple transcript
            variants encoding several different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2014].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (f) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.307973.1, AK294534.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            Protein has antimicrobial activity :: PMID: 20209079
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..714
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..714
                     /product="amyloid-beta precursor protein isoform f
                     precursor"
                     /note="peptidase nexin-II; cerebral vascular amyloid
                     peptide; protease nexin-II; amyloid beta A4 protein;
                     beta-amyloid peptide; alzheimer disease amyloid protein;
                     beta-amyloid peptide(1-40); beta-amyloid peptide(1-42);
                     amyloid precursor protein; beta-amyloid precursor protein;
                     testicular tissue protein Li 2; amyloid beta (A4)
                     precursor protein; alzheimer disease amyloid A4 protein
                     homolog"
                     /calculated_mol_wt=79071
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1781
     mat_peptide     18..714
                     /product="amyloid-beta precursor protein isoform f"
                     /calculated_mol_wt=79071
     Region          <19..132
                     /region_name="A4_EXTRA"
                     /note="amyloid A4; smart00006"
                     /db_xref="CDD:128326"
     Region          238..285
                     /region_name="Kunitz_ABPP-like"
                     /note="Kunitz domain found in the amyloid-beta precursor
                     protein (ABPP) subfamily; cd22607"
                     /db_xref="CDD:438650"
     Site            order(241..249,264,266,268)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438650"
     Region          310..492
                     /region_name="APP_E2"
                     /note="E2 domain of amyloid precursor protein; pfam12925"
                     /db_xref="CDD:463752"
     mat_peptide     616..657
                     /product="amyloid-beta precursor protein isoform f"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     20209079]"
                     /exception="alternative processing"
                     /calculated_mol_wt=4514
     mat_peptide     616..655
                     /product="amyloid-beta precursor protein isoform f"
                     /experiment="DESCRIPTION:antimicrobial peptide[20209079]"
                     /calculated_mol_wt=4330
     Region          637..711
                     /region_name="JMTM_Notch_APP"
                     /note="juxtamembrane and transmembrane (JMTM) domain found
                     in Notch and APP family proteins; cl41775"
                     /db_xref="CDD:425406"
     Site            order(650..651,653..654,656..662,664..669)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:411983"
     CDS             1..714
                     /gene="APP"
                     /gene_synonym="AAA; ABETA; ABPP; AD1; alpha-sAPP; APPI;
                     CTFgamma; CVAP; PN-II; PN2; preA4"
                     /coded_by="NM_001136130.3:151..2295"
                     /note="isoform f precursor is encoded by transcript
                     variant 6"
                     /db_xref="CCDS:CCDS46639.1"
                     /db_xref="GeneID:351"
                     /db_xref="HGNC:HGNC:620"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ypelqitnvv eanqpvtiqn wckrgrkqck thphfvipyr
       61 clvgefvsda llvpdkckfl hqermdvcet hlhwhtvake tcsekstnlh dygmllpcgi
      121 dkfrgvefvc cplaeesdnv dsadaeedds dvwwggadtd yadgsedkvv evaeeeevae
      181 veeeeaddde ddedgdevee eaeepyeeat erttsiattt ttttesveev vrevcseqae
      241 tgpcramisr wyfdvtegkc apffyggcgg nrnnfdteey cmavcgsams qsllkttqep
      301 lardpvklpt taastpdavd kyletpgden ehahfqkake rleakhrerm sqvmreweea
      361 erqaknlpka dkkaviqhfq ekvesleqea anerqqlvet hmarveamln drrrlaleny
      421 italqavppr prhvfnmlkk yvraeqkdrq htlkhfehvr mvdpkkaaqi rsqvmthlrv
      481 iyermnqsls llynvpavae eiqdevdell qkeqnysddv lanmisepri sygndalmps
      541 ltetkttvel lpvngefsld dlqpwhsfga dsvpantene vepvdarpaa drglttrpgs
      601 gltnikteei sevkmdaefr hdsgyevhhq klvffaedvg snkgaiiglm vggvviatvi
      661 vitlvmlkkk qytsihhgvv evdaavtpee rhlskmqqng yenptykffe qmqn
//
LOCUS       NP_004698                140 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-like protein ATG12 isoform 1 [Homo sapiens].
ACCESSION   NP_004698
VERSION     NP_004698.3
DBSOURCE    REFSEQ: accession NM_004707.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Zhang,R., Hao,J., Yu,H., Wang,Z.J., Lan,F., Peng,Y. and Qiu,Y.
  TITLE     circ_SIRT1 upregulates ATG12 to facilitate Imatinib resistance in
            CML through interacting with EIF4A3
  JOURNAL   Gene 893, 147917 (2024)
   PUBMED   37866664
  REMARK    GeneRIF: circ_SIRT1 upregulates ATG12 to facilitate Imatinib
            resistance in CML through interacting with EIF4A3.
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Keulers,T.G., Koch,A., van Gisbergen,M.W., Barbeau,L.M.O.,
            Zonneveld,M.I., de Jong,M.C., Savelkouls,K.G.M., Wanders,R.G.,
            Bussink,J., Melotte,V. and Rouschop,K.M.A.
  TITLE     ATG12 deficiency results in intracellular glutamine depletion,
            abrogation of tumor hypoxia and a favorable prognosis in cancer
  JOURNAL   Autophagy 18 (8), 1898-1914 (2022)
   PUBMED   34904929
  REMARK    GeneRIF: ATG12 deficiency results in intracellular glutamine
            depletion, abrogation of tumor hypoxia and a favorable prognosis in
            cancer.
REFERENCE   4  (residues 1 to 140)
  AUTHORS   Zhang,S., Liu,X., Abdulmomen Ali Mohammed,S., Li,H., Cai,W.,
            Guan,W., Liu,D., Wei,Y., Rong,D., Fang,Y., Haider,F., Lv,H.,
            Jin,Z., Chen,X., Mo,Z., Li,L., Yang,S. and Wang,H.
  TITLE     Adaptor SH3BGRL drives autophagy-mediated chemoresistance through
            promoting PIK3C3 translation and ATG12 stability in breast cancers
  JOURNAL   Autophagy 18 (8), 1822-1840 (2022)
   PUBMED   34870550
  REMARK    GeneRIF: Adaptor SH3BGRL drives autophagy-mediated chemoresistance
            through promoting PIK3C3 translation and ATG12 stability in breast
            cancers.
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Komatsu,M., Ueno,T. and Kominami,E.
  TITLE     Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
            substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
            conjugation of hApg12p to hApg5p
  JOURNAL   J Biol Chem 277 (16), 13739-13744 (2002)
   PUBMED   11825910
  REMARK    GeneRIF: Human Apg3p/Aut1p homologue is an authentic E2 enzyme for
            multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates
            the conjugation of hApg12p to hApg5p
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Nishitani,T., Komatsu,M., Yamazaki,H.,
            Ueno,T. and Kominami,E.
  TITLE     Murine Apg12p has a substrate preference for murine Apg7p over
            three Apg8p homologs
  JOURNAL   Biochem Biophys Res Commun 292 (1), 256-262 (2002)
   PUBMED   11890701
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Tanida,I., Tanida-Miyake,E., Ueno,T. and Kominami,E.
  TITLE     The human homolog of Saccharomyces cerevisiae Apg7p is a
            Protein-activating enzyme for multiple substrates including human
            Apg12p, GATE-16, GABARAP, and MAP-LC3
  JOURNAL   J Biol Chem 276 (3), 1701-1706 (2001)
   PUBMED   11096062
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Mizushima,N., Sugita,H., Yoshimori,T. and Ohsumi,Y.
  TITLE     A new protein conjugation system in human. The counterpart of the
            yeast Apg12p conjugation system essential for autophagy
  JOURNAL   J Biol Chem 273 (51), 33889-33892 (1998)
   PUBMED   9852036
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Ueno,K., Kumagai,T., Kijima,T., Kishimoto,T. and Hosoe,S.
  TITLE     Cloning and tissue expression of cDNAs from chromosome 5q21-22
            which is frequently deleted in advanced lung cancer
  JOURNAL   Hum Genet 102 (1), 63-68 (1998)
   PUBMED   9490301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC012266.2, AC026449.6 and DB530852.1.
            
            On Mar 4, 2010 this sequence version replaced NP_004698.2.
            
            Summary: Autophagy is a process of bulk protein degradation in
            which cytoplasmic components, including organelles, are enclosed in
            double-membrane structures called autophagosomes and delivered to
            lysosomes or vacuoles for degradation. ATG12 is the human homolog
            of a yeast protein involved in autophagy (Mizushima et al., 1998
            [PubMed 9852036]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.92489.1,
                                           SRR1803613.265879.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149398 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000509910.2/ ENSP00000425107.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.3"
     Protein         1..140
                     /product="ubiquitin-like protein ATG12 isoform 1"
                     /note="Apg12 (autophagy, yeast) homolog; ubiquitin-like
                     protein ATG12; ATG12 autophagy related 12 homolog; APG12
                     autophagy 12-like"
                     /calculated_mol_wt=14982
     Region          1..50
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O94817.1)"
     Region          54..139
                     /region_name="Ubl_ATG12"
                     /note="ubiquitin-like (Ubl) domain found in
                     autophagy-related protein 12 (ATG12); cd01612"
                     /db_xref="CDD:340454"
     Site            order(54,56..57,59,68,70,72..76,79,83..84,87..88,90..91,
                     93)
                     /site_type="other"
                     /note="Atg12;
                     Atg5-Atg16-Atg3 interaction site [polypeptide binding]"
                     /db_xref="CDD:340454"
     Site            order(60,69)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340454"
     Site            order(108..109,111..115,118,121..123,139)
                     /site_type="other"
                     /note="Atg5 conjugation site [polypeptide binding]"
                     /db_xref="CDD:340454"
     CDS             1..140
                     /gene="ATG12"
                     /gene_synonym="APG12; APG12L; FBR93; HAPG12"
                     /coded_by="NM_004707.4:14..436"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4122.2"
                     /db_xref="GeneID:9140"
                     /db_xref="HGNC:HGNC:588"
                     /db_xref="MIM:609608"
ORIGIN      
        1 maeepqsvlq lptsiaagge gltdvspett tpeppssaav spgteepagd tkkkidillk
       61 avgdtpimkt kkwavertrt iqglidfikk flklvaseql fiyvnqsfap spdqevgtly
      121 ecfgsdgklv lhycksqawg
//
LOCUS       NP_060206                353 aa            linear   PRI 20-NOV-2025
DEFINITION  THUMP domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_060206
VERSION     NP_060206.2
DBSOURCE    REFSEQ: accession NM_017736.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 353)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 353)
  AUTHORS   Gamage,S.T., Khoogar,R., Manage,S.H., Crawford,M.C., Georgeson,J.,
            Polevoda,B.V., Sanders,C., Lee,K.A., Nance,K.D., Iyer,V.,
            Kustanovich,A., Perez,M., Thu,C.T., Nance,S.R., Amin,R.,
            Miller,C.N., Holewinski,R.J., Meyer,T., Koparde,V., Yang,A.,
            Jailwala,P., Nguyen,J.T., Andresson,T., Hunter,K., Gu,S.,
            Mock,B.A., Edmondson,E.F., Difilippantonio,S., Chari,R.,
            Schwartz,S., O'Connell,M.R., Chih-Chien Wu,C. and Meier,J.L.
  TITLE     Transfer RNA acetylation regulates in vivo mammalian stress
            signaling
  JOURNAL   bioRxiv (2024)
   PUBMED   39091849
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 353)
  AUTHORS   Broly,M., Polevoda,B.V., Awayda,K.M., Tong,N., Lentini,J.,
            Besnard,T., Deb,W., O'Rourke,D., Baptista,J., Ellard,S.,
            Almannai,M., Hashem,M., Abdulwahab,F., Shamseldin,H., Al-Tala,S.,
            Alkuraya,F.S., Leon,A., van Loon,R.L.E., Ferlini,A., Sanchini,M.,
            Bigoni,S., Ciorba,A., van Bokhoven,H., Iqbal,Z., Al-Maawali,A.,
            Al-Murshedi,F., Ganesh,A., Al-Mamari,W., Lim,S.C., Pais,L.S.,
            Brown,N., Riazuddin,S., Bezieau,S., Fu,D., Isidor,B., Cogne,B. and
            O'Connell,M.R.
  TITLE     THUMPD1 bi-allelic variants cause loss of tRNA acetylation and a
            syndromic neurodevelopmental disorder
  JOURNAL   Am J Hum Genet 109 (4), 587-600 (2022)
   PUBMED   35196516
  REMARK    GeneRIF: THUMPD1 bi-allelic variants cause loss of tRNA acetylation
            and a syndromic neurodevelopmental disorder.
REFERENCE   4  (residues 1 to 353)
  AUTHORS   Li,K., Liu,J., Yang,X., Tu,Z., Huang,K. and Zhu,X.
  TITLE     Pan-cancer analysis of N4-acetylcytidine adaptor THUMPD1 as a
            predictor for prognosis and immunotherapy
  JOURNAL   Biosci Rep 41 (12) (2021)
   PUBMED   34762107
  REMARK    GeneRIF: Pan-cancer analysis of N4-acetylcytidine adaptor THUMPD1
            as a predictor for prognosis and immunotherapy.
REFERENCE   5  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 353)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 353)
  AUTHORS   Zhang,X., Jiang,G., Sun,M., Zhou,H., Miao,Y., Liang,M., Wang,E. and
            Zhang,Y.
  TITLE     Cytosolic THUMPD1 promotes breast cancer cells invasion and
            metastasis via the AKT-GSK3-Snail pathway
  JOURNAL   Oncotarget 8 (8), 13357-13366 (2017)
   PUBMED   28076326
  REMARK    GeneRIF: These results indicate that THUMPD1 promotes breast cancer
            cells invasion and migration via the AKT-GSK3beta-Snail pathway
REFERENCE   8  (residues 1 to 353)
  AUTHORS   Sharma,S., Langhendries,J.L., Watzinger,P., Kotter,P., Entian,K.D.
            and Lafontaine,D.L.
  TITLE     Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine
            acetyltransferases that modify tRNAs assisted by the adaptor
            Tan1/THUMPD1
  JOURNAL   Nucleic Acids Res 43 (4), 2242-2258 (2015)
   PUBMED   25653167
REFERENCE   9  (residues 1 to 353)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   10 (residues 1 to 353)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004381.1.
            
            On Feb 9, 2004 this sequence version replaced NP_060206.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000281.1, SRR1660809.133661.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000396083.7/ ENSP00000379392.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..353
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.3"
     Protein         1..353
                     /product="THUMP domain-containing protein 1"
                     /note="THUMP domain containing 1"
                     /calculated_mol_wt=39184
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Region          45..254
                     /region_name="THUMP_THUMPD1_like"
                     /note="THUMP domain-containing protein 1-like; cd11717"
                     /db_xref="CDD:212586"
     Region          73..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Region          270..353
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXG2.2)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NXG2.2)"
     CDS             1..353
                     /gene="THUMPD1"
                     /gene_synonym="NEDSOA; Tan1"
                     /coded_by="NM_017736.5:80..1141"
                     /db_xref="CCDS:CCDS10588.1"
                     /db_xref="GeneID:55623"
                     /db_xref="HGNC:HGNC:23807"
                     /db_xref="MIM:616662"
ORIGIN      
        1 maapaqqttq pgggkrkgka qyvlakrarr cdaggprqle pglqgilitc nmnerkcvee
       61 aysllneygd dmygpekftd kdqqpsgseg edddaeaalk kevgdikast emrlrrfqsv
      121 esgannvvfi rtlgiepekl vhhilqdmyk tkkkktrvil rmlpisgtck afledmkkya
      181 etflepwfka pnkgtfqivy ksrnnshvnr eevirelagi vctlnsenkv dltnpqytvv
      241 veiikavccl svvkdymlfr kynlqevvks pkdpsqlnsk qgngkeakle sadksdqnnt
      301 aegknnqqvp enteelgqtk ptsnpqvvne ggakpelasq ategsksnen dfs
//
LOCUS       NP_000936                170 aa            linear   PRI 20-NOV-2025
DEFINITION  calcineurin subunit B type 1 [Homo sapiens].
ACCESSION   NP_000936
VERSION     NP_000936.1
DBSOURCE    REFSEQ: accession NM_000945.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Li,M., Gong,W., Chen,J., Zhang,Y., Ma,Y. and Tu,X.
  TITLE     PPP3R1 Promotes MSCs Senescence by Inducing Plasma Membrane
            Depolarization and Increasing Ca2+ Influx
  JOURNAL   Int J Mol Sci 24 (5), 4421 (2023)
   PUBMED   36901851
  REMARK    GeneRIF: PPP3R1 Promotes MSCs Senescence by Inducing Plasma
            Membrane Depolarization and Increasing Ca[2+] Influx.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Miyata,H., Oura,S., Morohoshi,A., Shimada,K., Mashiko,D., Oyama,Y.,
            Kaneda,Y., Matsumura,T., Abbasi,F. and Ikawa,M.
  TITLE     SPATA33 localizes calcineurin to the mitochondria and regulates
            sperm motility in mice
  JOURNAL   Proc Natl Acad Sci U S A 118 (35) (2021)
   PUBMED   34446558
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Loh,C., Shaw,K.T., Carew,J., Viola,J.P., Luo,C., Perrino,B.A. and
            Rao,A.
  TITLE     Calcineurin binds the transcription factor NFAT1 and reversibly
            regulates its activity
  JOURNAL   J Biol Chem 271 (18), 10884-10891 (1996)
   PUBMED   8631904
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Kissinger,C.R., Parge,H.E., Knighton,D.R., Lewis,C.T.,
            Pelletier,L.A., Tempczyk,A., Kalish,V.J., Tucker,K.D.,
            Showalter,R.E., Moomaw,E.W. et al.
  TITLE     Crystal structures of human calcineurin and the human
            FKBP12-FK506-calcineurin complex
  JOURNAL   Nature 378 (6557), 641-644 (1995)
   PUBMED   8524402
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Kawamura,A. and Su,M.S.
  TITLE     Interaction of FKBP12-FK506 with calcineurin A at the B
            subunit-binding domain
  JOURNAL   J Biol Chem 270 (26), 15463-15466 (1995)
   PUBMED   7541044
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Guerini,D., Krinks,M.H., Sikela,J.M., Hahn,W.E. and Klee,C.B.
  TITLE     Isolation and sequence of a cDNA clone for human calcineurin B, the
            Ca2+-binding subunit of the Ca2+/calmodulin-stimulated protein
            phosphatase
  JOURNAL   DNA 8 (9), 675-682 (1989)
   PUBMED   2558868
REFERENCE   10 (residues 1 to 170)
  AUTHORS   King,M.M., Huang,C.Y., Chock,P.B., Nairn,A.C., Hemmings,H.C. Jr.,
            Chan,K.F. and Greengard,P.
  TITLE     Mammalian brain phosphoproteins as substrates for calcineurin
  JOURNAL   J Biol Chem 259 (13), 8080-8083 (1984)
   PUBMED   6330098
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC017083.7, BM468705.1, BC027913.1 and BQ228635.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC027913.1, SRR18074967.2554985.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000234310.8/ ENSP00000234310.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p14"
     Protein         1..170
                     /product="calcineurin subunit B type 1"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2B regulatory subunit B alpha;
                     calcineurin B, type I (19kDa); protein phosphatase 2B
                     regulatory subunit 1"
                     /calculated_mol_wt=19169
     Region          20..157
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q63810; propagated from
                     UniProtKB/Swiss-Prot (P63098.2)"
     Site            118
                     /site_type="other"
                     /note="Interaction with PxVP motif in substrates of the
                     catalytic subunit. /evidence=ECO:0000269|PubMed:23468591;
                     propagated from UniProtKB/Swiss-Prot (P63098.2)"
     Site            122
                     /site_type="other"
                     /note="Interaction with PxVP motif in substrates of the
                     catalytic subunit. /evidence=ECO:0000269|PubMed:23468591;
                     propagated from UniProtKB/Swiss-Prot (P63098.2)"
     Region          131..136
                     /region_name="Calcineurin A binding.
                     /evidence=ECO:0000269|PubMed:12218175,
                     ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738,
                     ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591,
                     ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827,
                     ECO:0000269|PubMed:8524402"
                     /note="propagated from UniProtKB/Swiss-Prot (P63098.2)"
     CDS             1..170
                     /gene="PPP3R1"
                     /gene_synonym="CALNB1; CNB; CNB1"
                     /coded_by="NM_000945.4:406..918"
                     /db_xref="CCDS:CCDS46310.1"
                     /db_xref="GeneID:5534"
                     /db_xref="HGNC:HGNC:9317"
                     /db_xref="MIM:601302"
ORIGIN      
        1 mgneasyple mcshfdadei krlgkrfkkl dldnsgslsv eefmslpelq qnplvqrvid
       61 ifdtdgngev dfkefiegvs qfsvkgdkeq klrfafriyd mdkdgyisng elfqvlkmmv
      121 gnnlkdtqlq qivdktiina dkdgdgrisf eefcavvggl dihkkmvvdv
//
LOCUS       NP_065135                450 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-10 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_065135
VERSION     NP_065135.2
DBSOURCE    REFSEQ: accession NM_020402.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Gu,S., Knowland,D., Matta,J.A., O'Carroll,M.L., Davini,W.B.,
            Dhara,M., Kweon,H.J. and Bredt,D.S.
  TITLE     Hair cell alpha9alpha10 nicotinic acetylcholine receptor functional
            expression regulated by ligand binding and deafness gene products
  JOURNAL   Proc Natl Acad Sci U S A 117 (39), 24534-24544 (2020)
   PUBMED   32929005
  REMARK    GeneRIF: Hair cell alpha9alpha10 nicotinic acetylcholine receptor
            functional expression regulated by ligand binding and deafness gene
            products.
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zouridakis,M., Giastas,P., Zarkadas,E., Chroni-Tzartou,D.,
            Bregestovski,P. and Tzartos,S.J.
  TITLE     Crystal structures of free and antagonist-bound states of human
            alpha9 nicotinic receptor extracellular domain
  JOURNAL   Nat Struct Mol Biol 21 (11), 976-980 (2014)
   PUBMED   25282151
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Azam,L. and McIntosh,J.M.
  TITLE     Molecular basis for the differential sensitivity of rat and human
            alpha9alpha10 nAChRs to alpha-conotoxin RgIA
  JOURNAL   J Neurochem 122 (6), 1137-1144 (2012)
   PUBMED   22774872
  REMARK    GeneRIF: A two order of magnitude species difference is reported in
            potency of alpha-conotoxin RgIA for rat versus human alpha9alpha10
            nAChR.
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Rigbi,A., Yakir,A., Sarner-Kanyas,K., Pollak,Y. and Lerer,B.
  TITLE     Why do young women smoke? VI. A controlled study of nicotine
            effects on attention: pharmacogenetic interactions
  JOURNAL   Pharmacogenomics J 11 (1), 45-52 (2011)
   PUBMED   20231857
  REMARK    GeneRIF: Clinical trial of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Saccone,N.L., Schwantes-An,T.H., Wang,J.C., Grucza,R.A.,
            Breslau,N., Hatsukami,D., Johnson,E.O., Rice,J.P., Goate,A.M. and
            Bierut,L.J.
  TITLE     Multiple cholinergic nicotinic receptor genes affect nicotine
            dependence risk in African and European Americans
  JOURNAL   Genes Brain Behav 9 (7), 741-750 (2010)
   PUBMED   20584212
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Rigbi,A., Kanyas,K., Yakir,A., Greenbaum,L., Pollak,Y.,
            Ben-Asher,E., Lancet,D., Kertzman,S. and Lerer,B.
  TITLE     Why do young women smoke? V. Role of direct and interactive effects
            of nicotinic cholinergic receptor gene variation on neurocognitive
            function
  JOURNAL   Genes Brain Behav 7 (2), 164-172 (2008)
   PUBMED   17559419
  REMARK    GeneRIF: Observational study of gene-disease association and
            gene-environment interaction. (HuGE Navigator)
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Shi,J., Hattori,E., Zou,H., Badner,J.A., Christian,S.L.,
            Gershon,E.S. and Liu,C.
  TITLE     No evidence for association between 19 cholinergic genes and
            bipolar disorder
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 144B (6), 715-723 (2007)
   PUBMED   17373692
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Peng,H., Ferris,R.L., Matthews,T., Hiel,H., Lopez-Albaitero,A. and
            Lustig,L.R.
  TITLE     Characterization of the human nicotinic acetylcholine receptor
            subunit alpha (alpha) 9 (CHRNA9) and alpha (alpha) 10 (CHRNA10) in
            lymphocytes
  JOURNAL   Life Sci 76 (3), 263-280 (2004)
   PUBMED   15531379
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Sgard,F., Charpantier,E., Bertrand,S., Walker,N., Caput,D.,
            Graham,D., Bertrand,D. and Besnard,F.
  TITLE     A novel human nicotinic receptor subunit, alpha10, that confers
            functionality to the alpha9-subunit
  JOURNAL   Mol Pharmacol 61 (1), 150-159 (2002)
   PUBMED   11752216
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Lustig,L.R., Peng,H., Hiel,H., Yamamoto,T. and Fuchs,P.A.
  TITLE     Molecular cloning and mapping of the human nicotinic acetylcholine
            receptor alpha10 (CHRNA10)
  JOURNAL   Genomics 73 (3), 272-283 (2001)
   PUBMED   11350119
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF199235.2 and AC060812.15.
            
            On Nov 11, 2000 this sequence version replaced NP_065135.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF199235.2, AJ278118.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000250699.2/ ENSP00000250699.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.4"
     Protein         1..450
                     /product="neuronal acetylcholine receptor subunit alpha-10
                     isoform a precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     10; neuronal acetylcholine receptor subunit alpha-10;
                     NACHR alpha-10; nicotinic acetylcholine receptor subunit
                     alpha-10; acetylcholine receptor, nicotinic, alpha 10
                     (neuronal); cholinergic receptor, nicotinic, alpha 10
                     (neuronal); cholinergic receptor, nicotinic alpha 10"
                     /calculated_mol_wt=47119
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2604
     mat_peptide     25..450
                     /product="Neuronal acetylcholine receptor subunit
                     alpha-10. /id=PRO_0000000376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
                     /calculated_mol_wt=47119
     Region          30..236
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            40
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Site            56
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Site            order(65,67,73..74,81,103,105,114..115,117,119..120,
                     131..133,135,145,147,149,153,175,235)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     Site            238..258
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Region          239..>324
                     /region_name="LGIC_TM_cation"
                     /note="transmembrane domain of Cys-loop
                     neurotransmitter-gated ion channels, includes 5HT3, nAChR,
                     and ZAC; cd19051"
                     /db_xref="CDD:349853"
     Region          239..261
                     /region_name="TM1 helix"
                     /note="TM1 helix [structural motif]"
                     /db_xref="CDD:349853"
     Region          243..434
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     Site            268..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Region          269..290
                     /region_name="TM2 helix"
                     /note="TM2 helix [structural motif]"
                     /db_xref="CDD:349853"
     Region          300..322
                     /region_name="TM3 helix"
                     /note="TM3 helix [structural motif]"
                     /db_xref="CDD:349853"
     Site            302..322
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Region          355..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     Site            429..449
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZZ6.1)"
     CDS             1..450
                     /gene="CHRNA10"
                     /coded_by="NM_020402.4:73..1425"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7745.1"
                     /db_xref="GeneID:57053"
                     /db_xref="HGNC:HGNC:13800"
                     /db_xref="MIM:606372"
ORIGIN      
        1 mglrshhlsl gllllfllpa eclgaegrla lklfrdlfan ytsalrpvad tdqtlnvtle
       61 vtlsqiidmd ernqvltlyl wirqewtday lrwdpnaygg ldairipssl vwrpdivlyn
      121 kadaqppgsa stnvvlrhdg avrwdapait rsscrvdvaa fpfdaqhcgl tfgswthggh
      181 qldvrprgaa asladfvenv ewrvlgmpar rrvltygccs epypdvtftl llrrraaayv
      241 cnlllpcvli sllaplafhl padsgekvsl gvtvllaltv fqlllaesmp paesvpligk
      301 yymatmtmvt fstaltilim nlhycgpsvr pvpawarall lghlarglcv rergepcgqs
      361 rppelspspq speggagppa gpcheprclc rqeallhhva tiantfrshr aaqrchedwk
      421 rlarvmdrff laiffsmalv msllvlvqal
//
LOCUS       NP_001008783             416 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 35 member D3 [Homo sapiens].
ACCESSION   NP_001008783 XP_294017
VERSION     NP_001008783.1
DBSOURCE    REFSEQ: accession NM_001008783.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Qian,C., Wu,Z., Sun,R., Yu,H., Zeng,J., Rao,Y. and Li,Y.
  TITLE     Localization, proteomics, and metabolite profiling reveal a
            putative vesicular transporter for UDP-glucose
  JOURNAL   Elife 10, e65417 (2021)
   PUBMED   34269178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Zhang,Z., Hao,C.J., Li,C.G., Zang,D.J., Zhao,J., Li,X.N., Wei,A.H.,
            Wei,Z.B., Yang,L., He,X., Zhen,X.C., Gao,X., Speakman,J.R. and
            Li,W.
  TITLE     Mutation of SLC35D3 causes metabolic syndrome by impairing dopamine
            signaling in striatal D1 neurons
  JOURNAL   PLoS Genet 10 (2), e1004124 (2014)
   PUBMED   24550737
  REMARK    GeneRIF: Our results suggest that the SLC35D3 gene, close to the
            D6S1009 locus, is a candidate gene for MetS, which is involved in
            metabolic control in the central nervous system by regulating
            dopamine signaling.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK316095.1, AK295424.1, BC067217.1 and BE669463.1.
            
            On Jan 1, 2005 this sequence version replaced XP_294017.5.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087842.1, SRR1803614.17469.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331858.5/ ENSP00000333591.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q23.3"
     Protein         1..416
                     /product="solute carrier family 35 member D3"
                     /note="frc, fringe-like 1; fringe connection-like protein
                     1"
                     /calculated_mol_wt=44052
     Region          8..299
                     /region_name="RhaT"
                     /note="Permease of the drug/metabolite transporter (DMT)
                     superfamily [Carbohydrate transport and metabolism, Amino
                     acid transport and metabolism, General function prediction
                     only]; COG0697"
                     /db_xref="CDD:440461"
     Site            9..29
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            131..151
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            155..175
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            257..277
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Site            280..300
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     Region          334..384
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5M8T2.1)"
     CDS             1..416
                     /gene="SLC35D3"
                     /gene_synonym="FRCL1"
                     /coded_by="NM_001008783.3:129..1379"
                     /db_xref="CCDS:CCDS34544.1"
                     /db_xref="GeneID:340146"
                     /db_xref="HGNC:HGNC:15621"
                     /db_xref="MIM:612519"
ORIGIN      
        1 mrqlcrgrvl gisvaiahgv fsgslnillk flisryqfsf ltlvqcltss taalslellr
       61 rlgliavppf glslarsfag vavlstlqss ltlwslrgls lpmyvvfkrc lplvtmligv
      121 lvlkngapsp gvlaavlitt cgaalagagd ltgdpigyvt gvlavlvhaa ylvliqkasa
      181 dtehgpltaq yviavsatpl lvicsfastd sihawtfpgw kdpamvcifv aciligcamn
      241 fttlhctyin savttsfvgv vksiatitvg mvafsdvept slfiagvvvn tlgsiiycva
      301 kfmetrkqsn yedleaqprg eeaqlsgdql pfvmeelpge ggngrsegge aaggpaqesr
      361 qevrgsprgv plvagsseeg srrslkdayl evwrlvrgtr ymkkdylien eelpsp
//
LOCUS       NP_001357116             662 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor beta activator LRRC32 isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001357116 XP_005273959
VERSION     NP_001357116.1
DBSOURCE    REFSEQ: accession NM_001370187.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 662)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 662)
  AUTHORS   Ma,J., Chen,Y., Li,T., Cao,Y., Hu,B., Liu,Y., Zhang,Y., Li,X.,
            Liu,J., Zhang,W., Niu,H., Gao,J., Zhang,Z., Yue,K., Wang,J.,
            Bao,G., Wang,C., Wang,P.G., Zou,T. and Xie,S.
  TITLE     Suppression of lysosome metabolism-meditated GARP/TGF-beta1
            complexes specifically depletes regulatory T cells to inhibit
            breast cancer metastasis
  JOURNAL   Oncogene 43 (25), 1930-1940 (2024)
   PUBMED   38698265
  REMARK    GeneRIF: Suppression of lysosome metabolism-meditated
            GARP/TGF-beta1 complexes specifically depletes regulatory T cells
            to inhibit breast cancer metastasis.
REFERENCE   3  (residues 1 to 662)
  AUTHORS   Zhang,X., Sharma,P., Maschmeyer,P., Hu,Y., Lou,M., Kim,J.,
            Fujii,H., Unutmaz,D., Schwabe,R.F. and Winau,F.
  TITLE     GARP on hepatic stellate cells is essential for the development of
            liver fibrosis
  JOURNAL   J Hepatol 79 (5), 1214-1225 (2023)
   PUBMED   37348791
  REMARK    GeneRIF: GARP on hepatic stellate cells is essential for the
            development of liver fibrosis.
REFERENCE   4  (residues 1 to 662)
  AUTHORS   Cai,H., Liu,Y., Dong,X., Jiang,F., Li,H., Ouyang,S., Yin,W., He,T.,
            Zeng,Q. and Yang,H.
  TITLE     Analysis of LAP+ and GARP+ Treg subsets in peripheral blood of
            patients with neuromyelitis optica spectrum disorders
  JOURNAL   Neurol Sci 44 (5), 1739-1747 (2023)
   PUBMED   36683084
  REMARK    GeneRIF: Analysis of LAP[+] and GARP[+] Treg subsets in peripheral
            blood of patients with neuromyelitis optica spectrum disorders.
REFERENCE   5  (residues 1 to 662)
  AUTHORS   Lahimchi,M.R., Eslami,M. and Yousefi,B.
  TITLE     New insight into GARP striking role in cancer progression:
            application for cancer therapy
  JOURNAL   Med Oncol 40 (1), 33 (2022)
   PUBMED   36460874
  REMARK    GeneRIF: New insight into GARP striking role in cancer progression:
            application for cancer therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 662)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 662)
  AUTHORS   Maire,G., Forus,A., Foa,C., Bjerkehagen,B., Mainguene,C.,
            Kresse,S.H., Myklebost,O. and Pedeutour,F.
  TITLE     11q13 alterations in two cases of hibernoma: large heterozygous
            deletions and rearrangement breakpoints near GARP in 11q13.5
  JOURNAL   Genes Chromosomes Cancer 37 (4), 389-395 (2003)
   PUBMED   12800150
REFERENCE   8  (residues 1 to 662)
  AUTHORS   Roubin,R., Pizette,S., Ollendorff,V., Planche,J., Birnbaum,D. and
            Delapeyriere,O.
  TITLE     Structure and developmental expression of mouse Garp, a gene
            encoding a new leucine-rich repeat-containing protein
  JOURNAL   Int J Dev Biol 40 (3), 545-555 (1996)
   PUBMED   8840187
REFERENCE   9  (residues 1 to 662)
  AUTHORS   Ollendorff,V., Noguchi,T., deLapeyriere,O. and Birnbaum,D.
  TITLE     The GARP gene encodes a new member of the family of leucine-rich
            repeat-containing proteins
  JOURNAL   Cell Growth Differ 5 (2), 213-219 (1994)
   PUBMED   8180135
REFERENCE   10 (residues 1 to 662)
  AUTHORS   Ollendorff,V., Szepetowski,P., Mattei,M.G., Gaudray,P. and
            Birnbaum,D.
  TITLE     New gene in the homologous human 11q13-q14 and mouse 7F chromosomal
            regions
  JOURNAL   Mamm Genome 2 (3), 195-200 (1992)
   PUBMED   1543912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001189.5 and KF455417.1.
            
            On May 2, 2019 this sequence version replaced XP_005273959.1.
            
            Summary: This gene encodes a type I membrane protein which contains
            20 leucine-rich repeats. Alterations in the chromosomal region
            11q13-11q14 are involved in several pathologies. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3), as well as variants 1, 2, and
            4, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.252461.1,
                                           SRR1803616.242181.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307, SAMEA2162946
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..662
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..662
                     /product="transforming growth factor beta activator LRRC32
                     isoform a precursor"
                     /note="garpin; glycoprotein A repetitions predominant;
                     leucine-rich repeat-containing protein 32; transforming
                     growth factor beta activator LRRC32"
                     /calculated_mol_wt=70148
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1849
     Region          19..277
                     /region_name="LRR_RI"
                     /note="Leucine-rich repeats (LRRs), ribonuclease inhibitor
                     (RI)-like subfamily. LRRs are 20-29 residue sequence
                     motifs present in many proteins that participate in
                     protein-protein interactions and have different functions
                     and cellular locations. LRRs correspond...; cd00116"
                     /db_xref="CDD:238064"
     mat_peptide     20..662
                     /product="Transforming growth factor beta activator
                     LRRC32. /id=PRO_0000021615"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
                     /calculated_mol_wt=69949
     Site            order(28,31,33,36,38,51,54,56,59,61,75,78,80,83,85,99,102,
                     104,107,109,126,129,131,134,136,151,154,156,159,161,175,
                     178,180,183,185,199,202,204,207,209,220,223,225,228,230,
                     245,248,250,253,255,267,270,272,275,277)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          31..50
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(34..35,82,133,158,206,224,226,249,271)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          50..73
                     /region_name="LRR 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          51..74
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          74..95
                     /region_name="LRR 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          75..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          98..119
                     /region_name="LRR 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          99..125
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          125..145
                     /region_name="LRR 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          126..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          150..171
                     /region_name="LRR 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          151..174
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          174..195
                     /region_name="LRR 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          175..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..219
                     /region_name="LRR 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          199..219
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          220..244
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          220..240
                     /region_name="LRR 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          244..265
                     /region_name="LRR 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          245..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          266..286
                     /region_name="LRR 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Site            271
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          290..>574
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Site            308
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          316..339
                     /region_name="LRR 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          317..340
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          340..363
                     /region_name="LRR 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          341..364
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            345
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          364..385
                     /region_name="LRR 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          365..387
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          387..408
                     /region_name="LRR 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          388..411
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          411..432
                     /region_name="LRR 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          412..444
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          444..465
                     /region_name="LRR 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          445..463
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          467..488
                     /region_name="LRR 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          468..492
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          492..513
                     /region_name="LRR 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          493..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <496..654
                     /region_name="PLN03150"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:178695"
     Region          515..536
                     /region_name="LRR 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          516..537
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          537..558
                     /region_name="LRR 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     Region          538..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            545
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q14392.1)"
     Region          563..575
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Site            628..648
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14392.1)"
     CDS             1..662
                     /gene="LRRC32"
                     /gene_synonym="CPPRDD; D11S833E; GARP"
                     /coded_by="NM_001370187.1:139..2127"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS8245.1"
                     /db_xref="GeneID:2615"
                     /db_xref="HGNC:HGNC:4161"
                     /db_xref="MIM:137207"
ORIGIN      
        1 mrpqilllla lltlglaaqh qdkvpckmvd kkvscqvlgl lqvpsvlppd tetldlsgnq
       61 lrsilasplg fytalrhldl stneisflqp gafqalthle hlslahnrla matalsaggl
      121 gplprvtsld lsgnslysgl lerllgeaps lhtlslaens ltrltrhtfr dmpaleqldl
      181 hsnvlmdied gafeglprlt hlnlsrnslt cisdfslqql rvldlscnsi eafqtasqpq
      241 aefqltwldl renkllhfpd laalprliyl nlsnnlirlp tgppqdskgi hapsegwsal
      301 plsapsgnas grplsqllnl dlsyneieli pdsflehlts lcflnlsrnc lrtfearrlg
      361 slpclmlldl shnaletlel garalgslrt lllqgnalrd lppytfanla slqrlnlqgn
      421 rvspcggpde pgpsgcvafs gitslrslsl vdneiellra gaflhtplte ldlssnpgle
      481 vatgalggle aslevlalqg nglmvlqvdl pcficlkrln laenrlshlp awtqavslev
      541 ldlrnnsfsl lpgsamggle tslrrlylqg nplsccgngw laaqlhqgrv dvdatqdlic
      601 rfssqeevsl shvrpedcek gglkninlii iltfilvsai llttlaaccc vrrqkfnqqy
      661 ka
//
LOCUS       NP_001265568             278 aa            linear   PRI 20-NOV-2025
DEFINITION  ran-specific GTPase-activating protein isoform 1 [Homo sapiens].
ACCESSION   NP_001265568
VERSION     NP_001265568.1
DBSOURCE    REFSEQ: accession NM_001278639.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 278)
  AUTHORS   Kodiha,M., Azad,N., Chu,S., Crampton,N. and Stochaj,U.
  TITLE     Oxidative stress and signaling through EGFR and PKA pathways
            converge on the nuclear transport factor RanBP1
  JOURNAL   Eur J Cell Biol 103 (1), 151376 (2024)
   PUBMED   38011756
  REMARK    GeneRIF: Oxidative stress and signaling through EGFR and PKA
            pathways converge on the nuclear transport factor RanBP1.
REFERENCE   2  (residues 1 to 278)
  AUTHORS   Kahm,Y.J., Kim,I.G. and Kim,R.K.
  TITLE     RanBP1: A Potential Therapeutic Target for Cancer Stem Cells in
            Lung Cancer and Glioma
  JOURNAL   Int J Mol Sci 24 (7), 6855 (2023)
   PUBMED   37047826
  REMARK    GeneRIF: RanBP1: A Potential Therapeutic Target for Cancer Stem
            Cells in Lung Cancer and Glioma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 278)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 278)
  AUTHORS   Nan,G., Zhao,S.H., Wang,T., Chao,D., Tian,R.F., Wang,W.J., Fu,X.,
            Lin,P., Guo,T., Wang,B., Sun,X.X., Chen,X., Chen,Z.N., Wang,S.J.
            and Cui,H.Y.
  TITLE     CD147 supports paclitaxel resistance via interacting with RanBP1
  JOURNAL   Oncogene 41 (7), 983-996 (2022)
   PUBMED   34974521
  REMARK    GeneRIF: CD147 supports paclitaxel resistance via interacting with
            RanBP1.
REFERENCE   5  (residues 1 to 278)
  AUTHORS   Chi,N.C., Adam,E.J. and Adam,S.A.
  TITLE     Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear
            import factor p97
  JOURNAL   J Biol Chem 272 (10), 6818-6822 (1997)
   PUBMED   9045717
REFERENCE   6  (residues 1 to 278)
  AUTHORS   Chi,N.C., Adam,E.J., Visser,G.D. and Adam,S.A.
  TITLE     RanBP1 stabilizes the interaction of Ran with p97 nuclear protein
            import
  JOURNAL   J Cell Biol 135 (3), 559-569 (1996)
   PUBMED   8909533
REFERENCE   7  (residues 1 to 278)
  AUTHORS   Hayashi,N., Yokoyama,N., Seki,T., Azuma,Y., Ohba,T. and
            Nishimoto,T.
  TITLE     RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits
            RCC1 via Ran/TC4
  JOURNAL   Mol Gen Genet 247 (6), 661-669 (1995)
   PUBMED   7616957
REFERENCE   8  (residues 1 to 278)
  AUTHORS   Ren,M., Villamarin,A., Shih,A., Coutavas,E., Moore,M.S.,
            LoCurcio,M., Clarke,V., Oppenheim,J.D., D'Eustachio,P. and
            Rush,M.G.
  TITLE     Separate domains of the Ran GTPase interact with different factors
            to regulate nuclear protein import and RNA processing
  JOURNAL   Mol Cell Biol 15 (4), 2117-2124 (1995)
   PUBMED   7891706
REFERENCE   9  (residues 1 to 278)
  AUTHORS   Bischoff,F.R., Krebber,H., Smirnova,E., Dong,W. and Ponstingl,H.
  TITLE     Co-activation of RanGTPase and inhibition of GTP dissociation by
            Ran-GTP binding protein RanBP1
  JOURNAL   EMBO J 14 (4), 705-715 (1995)
   PUBMED   7882974
REFERENCE   10 (residues 1 to 278)
  AUTHORS   Coutavas,E., Ren,M., Oppenheim,J.D., D'Eustachio,P. and Rush,M.G.
  TITLE     Characterization of proteins that interact with the cell-cycle
            regulatory protein Ran/TC4
  JOURNAL   Nature 366 (6455), 585-587 (1993)
   PUBMED   8255297
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC397929.1, CA489474.1,
            X83617.1, AW404614.1 and HY229989.1.
            
            Summary: This gene encodes a protein that forms a complex with
            Ras-related nuclear protein (Ran) and metabolizes guanoside
            triphosphate (GTP). This complex participates in the regulation of
            the cell cycle by controlling transport of proteins and nucleic
            acids into the nucleus. There are multiple pseudogenes for this
            gene on chromosomes 9, 12, 17, and X. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189652.220377.1,
                                           SRR5189661.170025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000430524.6/ ENSP00000401564.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..278
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..278
                     /product="ran-specific GTPase-activating protein isoform
                     1"
                     /note="ran-specific GTPase-activating protein; HpaII tiny
                     fragments locus 9A; testis secretory sperm-binding protein
                     Li 221n"
                     /calculated_mol_wt=31773
     Region          101..237
                     /region_name="RanBD_RanBP1"
                     /note="Ran-binding domain; cd13179"
                     /db_xref="CDD:270000"
     Site            order(112..113,115..118,131,133,135,144..147,164,166,
                     168..169,171..175,178..180,188..191,198,200,205,208,210,
                     214,218)
                     /site_type="other"
                     /note="Ran#RanBP1#RanGAP complex [polypeptide binding]"
                     /db_xref="CDD:270000"
     Site            order(112..113,116..118,127,133,135,142..147,151,162,164,
                     166,168..175,178..180,188..191,194..196,198,200,205,212,
                     214,216,218)
                     /site_type="other"
                     /note="CRM1-RanBP1-RanGTP complex [polypeptide binding]"
                     /db_xref="CDD:270000"
     CDS             1..278
                     /gene="RANBP1"
                     /gene_synonym="HTF9A"
                     /coded_by="NM_001278639.2:82..918"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS74823.1"
                     /db_xref="GeneID:5902"
                     /db_xref="HGNC:HGNC:9847"
                     /db_xref="MIM:601180"
ORIGIN      
        1 mgsalgrarr tlsgrpfqra pcktrralsl saalrnvtka qggcpkslvl wgcrpkrprk
       61 rrtslklawr gtfcssslki sedthedhdt stentdesnh dpqfepivsl peqeiktlee
      121 deeelfkmra klfrfasend lpewkergtg dvkllkhkek gairllmrrd ktlkicanhy
      181 itpmmelkpn agsdrawvwn thadfadecp kpellairfl naenaqkfkt kfeecrkeie
      241 erekkagsgk ndhaekvaek lealsvkeet kedaeekq
//
LOCUS       NP_001239219             164 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor ligand superfamily member 8 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001239219
VERSION     NP_001239219.1
DBSOURCE    REFSEQ: accession NM_001252290.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Liu,C., Yan,S., Chen,H., Wu,Z., Li,L. and Li,Y.
  TITLE     Several genetic variants associated with systemic sclerosis in a
            Chinese Han population
  JOURNAL   Clin Rheumatol 42 (3), 773-781 (2023)
   PUBMED   36301368
  REMARK    GeneRIF: Several genetic variants associated with systemic
            sclerosis in a Chinese Han population.
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Sallin,M.A., Kauffman,K.D., Riou,C., Du Bruyn,E., Foreman,T.W.,
            Sakai,S., Hoft,S.G., Myers,T.G., Gardina,P.J., Sher,A., Moore,R.,
            Wilder-Kofie,T., Moore,I.N., Sette,A., Lindestam Arlehamn,C.S.,
            Wilkinson,R.J. and Barber,D.L.
  TITLE     Host resistance to pulmonary Mycobacterium tuberculosis infection
            requires CD153 expression
  JOURNAL   Nat Microbiol 3 (11), 1198-1205 (2018)
   PUBMED   30202016
  REMARK    GeneRIF: Polyfunctional CD153-expressing CD4 T cells are increased
            in latent Mycobacterium tuberculosis infection compared to active
            Tuberculosis.
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Pera,M.F., Bennett,W. and Cerretti,D.P.
  TITLE     CD30 and its ligand: possible role in regulation of teratoma stem
            cells
  JOURNAL   APMIS 106 (1), 169-72 (1998)
   PUBMED   9524575
  REMARK    Review article
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Croager,E.J. and Abraham,L.J.
  TITLE     Characterisation of the human CD30 ligand gene structure
  JOURNAL   Biochim Biophys Acta 1353 (3), 231-235 (1997)
   PUBMED   9349718
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Gruss,H.J., DaSilva,N., Hu,Z.B., Uphoff,C.C., Goodwin,R.G. and
            Drexler,H.G.
  TITLE     Expression and regulation of CD30 ligand and CD30 in human
            leukemia-lymphoma cell lines
  JOURNAL   Leukemia 8 (12), 2083-2094 (1994)
   PUBMED   7528856
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Gruss,H.J., Boiani,N., Williams,D.E., Armitage,R.J., Smith,C.A. and
            Goodwin,R.G.
  TITLE     Pleiotropic effects of the CD30 ligand on CD30-expressing cells and
            lymphoma cell lines
  JOURNAL   Blood 83 (8), 2045-2056 (1994)
   PUBMED   8161776
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Smith,C.A., Gruss,H.J., Davis,T., Anderson,D., Farrah,T., Baker,E.,
            Sutherland,G.R., Brannan,C.I., Copeland,N.G., Jenkins,N.A. et al.
  TITLE     CD30 antigen, a marker for Hodgkin's lymphoma, is a receptor whose
            ligand defines an emerging family of cytokines with homology to TNF
  JOURNAL   Cell 73 (7), 1349-1360 (1993)
   PUBMED   8391931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313619.1, CD690231.1,
            BX108999.1 and AW118787.1.
            
            Summary: The protein encoded by this gene is a cytokine that
            belongs to the tumor necrosis factor (TNF) ligand family. This
            cytokine is a ligand for TNFRSF8/CD30, which is a cell surface
            antigen and a marker for Hodgkin lymphoma and related hematologic
            malignancies. The engagement of this cytokine expressed on B cell
            surface plays an inhibitory role in modulating Ig class switch.
            This cytokine was shown to enhance cell proliferation of some
            lymphoma cell lines, while to induce cell death and reduce cell
            proliferation of other lymphoma cell lines. The pleiotropic
            biologic activities of this cytokine on different CD30+ lymphoma
            cell lines may play a pathophysiologic role in Hodgkin's and some
            non-Hodgkin's lymphomas. Two transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2011].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the coding region of the last exon and contains an alternate
            downstream exon compared to variant 1. The resulting isoform (2)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD690231.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32-q33.1"
     Protein         1..164
                     /product="tumor necrosis factor ligand superfamily member
                     8 isoform 2"
                     /note="CD30 antigen ligand; CD153 antigen; CD30 ligand;
                     CD30-L; tumor necrosis factor (ligand) superfamily, member
                     8; tumor necrosis factor ligand 3A; tumor necrosis factor
                     superfamily member 8"
                     /calculated_mol_wt=17703
     Site            38..62
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P32971.1)"
     Site            81
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32971.1)"
     Site            109
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P32971.1)"
     Region          113..>136
                     /region_name="TNF"
                     /note="Tumor Necrosis Factor; TNF superfamily members
                     include the cytokines: TNF (TNF-alpha), LT
                     (lymphotoxin-alpha, TNF-beta), CD40 ligand, Apo2L (TRAIL),
                     Fas ligand, and osteoprotegerin (OPG) ligand. These
                     proteins generally have an intracellular N-terminal...;
                     cl00147"
                     /db_xref="CDD:444713"
     CDS             1..164
                     /gene="TNFSF8"
                     /gene_synonym="CD153; CD30L; CD30LG; TNLG3A"
                     /coded_by="NM_001252290.1:293..787"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS75884.1"
                     /db_xref="GeneID:944"
                     /db_xref="HGNC:HGNC:11938"
                     /db_xref="MIM:603875"
ORIGIN      
        1 mdpglqqaln gmappgdtam hvpagsvash lgttsrsyfy lttatlalcl vftvatimvl
       61 vvqrtdsipn spdnvplkgg ncsedllcil krapfkkswa ylqvakhlnk tklswnkdgi
      121 lhgvryqdgn lviqfpdycg milhhshstl dsgkghccle tlqp
//
LOCUS       NP_689929                770 aa            linear   PRI 20-NOV-2025
DEFINITION  protein PAT1 homolog 1 [Homo sapiens].
ACCESSION   NP_689929
VERSION     NP_689929.2
DBSOURCE    REFSEQ: accession NM_152716.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 770)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 770)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 770)
  AUTHORS   Marnef,A., Maldonado,M., Bugaut,A., Balasubramanian,S., Kress,M.,
            Weil,D. and Standart,N.
  TITLE     Distinct functions of maternal and somatic Pat1 protein paralogs
  JOURNAL   RNA 16 (11), 2094-2107 (2010)
   PUBMED   20826699
  REMARK    GeneRIF: hPat1b localizes to P-bodies, while mPat1a-GFP is either
            found weakly in P-bodies or disperses P-bodies in a
            dominant-negative fashion.
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Ozgur,S., Chekulaeva,M. and Stoecklin,G.
  TITLE     Human Pat1b connects deadenylation with mRNA decapping and controls
            the assembly of processing bodies
  JOURNAL   Mol Cell Biol 30 (17), 4308-4323 (2010)
   PUBMED   20584987
  REMARK    GeneRIF: By tethering Pat1b to a reporter mRNA, the study provides
            evidence that Pat1b is also functionally linked to both
            deadenylation and decapping.
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Braun,J.E., Tritschler,F., Haas,G., Igreja,C., Truffault,V.,
            Weichenrieder,O. and Izaurralde,E.
  TITLE     The C-terminal alpha-alpha superhelix of Pat is required for mRNA
            decapping in metazoa
  JOURNAL   EMBO J 29 (14), 2368-2380 (2010)
   PUBMED   20543818
  REMARK    GeneRIF: Data show that PatL1 is essential for the interaction with
            mRNA decapping factors (i.e. DCP2, EDC4 and LSm1-7), whereas the
            P-rich region and Mid domain have distinct functions in modulating
            these interactions.
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Scheller,N., Resa-Infante,P., de la Luna,S., Galao,R.P.,
            Albrecht,M., Kaestner,L., Lipp,P., Lengauer,T., Meyerhans,A. and
            Diez,J.
  TITLE     Identification of PatL1, a human homolog to yeast P body component
            Pat1
  JOURNAL   Biochim Biophys Acta 1773 (12), 1786-1792 (2007)
   PUBMED   17936923
  REMARK    GeneRIF: The identification of two human PAT1 genes is described
            and one of them, PATL1, codes for an open reading frame with
            similar features as the yeast PAT1.
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC409866.1 and BC111047.1.
            
            On May 31, 2008 this sequence version replaced NP_689929.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.423178.1, AL831992.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300146.10/ ENSP00000300146.9
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.1"
     Protein         1..770
                     /product="protein PAT1 homolog 1"
                     /note="PAT1-like protein 1; protein PAT1 homolog b;
                     protein associated with topoisomerase II homolog 1"
                     /calculated_mol_wt=86719
     Region          1..397
                     /region_name="Involved in nuclear foci localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          1..84
                     /region_name="Region A, interaction with DDX6/RCK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          16..>613
                     /region_name="PAT1"
                     /note="Topoisomerase II-associated protein PAT1;
                     pfam09770"
                     /db_xref="CDD:401645"
     Region          85..388
                     /region_name="Region N, interaction with decapping
                     machinery"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          86..95
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            179
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            217
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          223..397
                     /region_name="Involved in RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            223
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            263
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            284
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          314..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          360..399
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Site            385
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q3TC46; propagated from
                     UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          389..448
                     /region_name="Region H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          398..770
                     /region_name="Involved in nuclear speckle localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     Region          449..770
                     /region_name="Region C"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86TB9.2)"
     CDS             1..770
                     /gene="PATL1"
                     /gene_synonym="hPat1b; Pat1b"
                     /coded_by="NM_152716.3:143..2455"
                     /db_xref="CCDS:CCDS44613.1"
                     /db_xref="GeneID:219988"
                     /db_xref="HGNC:HGNC:26721"
                     /db_xref="MIM:614660"
ORIGIN      
        1 mfryesledc pldededafq glgeedeeid qfnddtfgsg avdddwqeah erlaeleekl
       61 pvavneqtgn gerdemdllg dheenlaerl skmvienele dpaimravqt rpvlqpqpgs
      121 lnssiwdgse vlrrirgpll aqemptvsvl eyalpqrppq gpeddrdlse ralprrstsp
      181 iigsppvrav pigtppkqma vpsftqqilc pkpvhvrppm pprypapyge rmspnqlcsv
      241 pnssllghpf ppsvppvlsp lqraqllgga qlqpgrmsps qfarvpgfvg splaamnpkl
      301 lqgrvgqmlp papgfraffs appsatpppq qhppgpgphl qnlrsqapmf rpdtthlhpq
      361 hrrllhqrqq qnrsqhrnln gagdrgshrs shqdhlrkdp yanlmlqrek dwvskiqmmq
      421 lqstdpyldd fyyqnyfekl eklsaaeeiq gdgpkkertk litpqvakle haykpvqfeg
      481 slgkltvssv nnprkmidav vtsrseddet kekqvrdkrr ktlviiekty sllldvedye
      541 rryllsleee rpalmddrkh kicsmydnlr gklpgqerps ddhfvqimci rkgkrmvari
      601 lpflsteqaa dilmttarnl pflikkdaqd evlpcllspf slllyhlpsv sitsllrqlm
      661 nlpqsaatpa lsnphltavl qnkfglslll illsrgedlq ssdpatestq nnqwtevmfm
      721 atrellripq aalakpisip tnlvslfsry vdrqklnlle tklqlvqgir
//
LOCUS       NP_057006                373 aa            linear   PRI 20-NOV-2025
DEFINITION  sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating [Homo
            sapiens].
ACCESSION   NP_057006
VERSION     NP_057006.1
DBSOURCE    REFSEQ: accession NM_015922.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 373)
  AUTHORS   Chen,M., Zhao,Y., Yang,X., Zhao,Y., Liu,Q., Liu,Y., Hou,Y., Sun,H.
            and Jin,W.
  TITLE     NSDHL promotes triple-negative breast cancer metastasis through the
            TGFbeta signaling pathway and cholesterol biosynthesis
  JOURNAL   Breast Cancer Res Treat 187 (2), 349-362 (2021)
   PUBMED   33864166
  REMARK    GeneRIF: NSDHL promotes triple-negative breast cancer metastasis
            through the TGFbeta signaling pathway and cholesterol biosynthesis.
REFERENCE   2  (residues 1 to 373)
  AUTHORS   Tang,M.M., Tan,W.C., Surana,U., Leong,K.F. and Pramano,Z.A.D.
  TITLE     CHILD syndrome in a Malaysian adult with identification of a novel
            heterozygous missense mutation NSDHL c.602A>G
  JOURNAL   Int J Dermatol 60 (4), e154-e156 (2021)
   PUBMED   33169834
  REMARK    GeneRIF: CHILD syndrome in a Malaysian adult with identification of
            a novel heterozygous missense mutation NSDHL c.602A>G.
REFERENCE   3  (residues 1 to 373)
  AUTHORS   Xiao,Y., Xie,J., Liu,L., Huang,W., Han,Q., Qin,J., Liu,S. and
            Jiang,Z.
  TITLE     NAD(P)-dependent steroid dehydrogenase-like protein and neutral
            cholesterol ester hydrolase 1 serve as novel markers for early
            detection of gastric cancer identified using quantitative
            proteomics
  JOURNAL   J Clin Lab Anal 35 (2), e23652 (2021)
   PUBMED   33219617
  REMARK    GeneRIF: NAD(P)-dependent steroid dehydrogenase-like protein and
            neutral cholesterol ester hydrolase 1 serve as novel markers for
            early detection of gastric cancer identified using quantitative
            proteomics.
REFERENCE   4  (residues 1 to 373)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 373)
  AUTHORS   Yoon,S.H., Kim,H.S., Kim,R.N., Jung,S.Y., Hong,B.S., Kang,E.J.,
            Lee,H.B., Moon,H.G., Noh,D.Y. and Han,W.
  TITLE     NAD(P)-dependent steroid dehydrogenase-like is involved in breast
            cancer cell growth and metastasis
  JOURNAL   BMC Cancer 20 (1), 375 (2020)
   PUBMED   32366230
  REMARK    GeneRIF: NAD(P)-dependent steroid dehydrogenase-like is involved in
            breast cancer cell growth and metastasis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 373)
  AUTHORS   Heiss,N.S., Rogner,U.C., Kioschis,P., Korn,B. and Poustka,A.
  TITLE     Transcription mapping in a 700-kb region around the DXS52 locus in
            Xq28: isolation of six novel transcripts and a novel ATPase isoform
            (hPMCA5)
  JOURNAL   Genome Res 6 (6), 478-491 (1996)
   PUBMED   8828037
REFERENCE   7  (residues 1 to 373)
  AUTHORS   Levin,M.L., Chatterjee,A., Pragliola,A., Worley,K.C., Wehnert,M.,
            Zhuchenko,O., Smith,R.F., Lee,C.C. and Herman,G.E.
  TITLE     A comparative transcription map of the murine bare patches (Bpa)
            and striated (Str) critical regions and human Xq28
  JOURNAL   Genome Res 6 (6), 465-477 (1996)
   PUBMED   8828036
REFERENCE   8  (residues 1 to 373)
  AUTHORS   Kurban,M., El Feghaly,J. and Hamie,L.
  TITLE     NSDHL-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21290788
REFERENCE   9  (residues 1 to 373)
  AUTHORS   Angel,T.A., Faust,C.J., Gonzales,J.C., Kenwrick,S., Lewis,R.A. and
            Herman,G.E.
  TITLE     Genetic mapping of the X-linked dominant mutations striated (Str)
            and bare patches (Bpa) to a 600-kb region of the mouse X
            chromosome: implications for mapping human disorders in Xq28
  JOURNAL   Mamm Genome 4 (3), 171-176 (1993)
   PUBMED   8439729
REFERENCE   10 (residues 1 to 373)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U47105.2, BC007816.2 and
            U82671.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is localized in the
            endoplasmic reticulum and is involved in cholesterol biosynthesis.
            Mutations in this gene are associated with CHILD syndrome, which is
            a X-linked dominant disorder of lipid metabolism with disturbed
            cholesterol biosynthesis, and typically lethal in males.
            Alternatively spliced transcript variants with differing 5' UTR
            have been found for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the more
            predominant transcript. Transcript variants 1 and 2 encode the same
            protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026549.1, SRR1803615.156504.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370274.8/ ENSP00000359297.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..373
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..373
                     /product="sterol-4-alpha-carboxylate 3-dehydrogenase,
                     decarboxylating"
                     /EC_number="1.1.1.170"
                     /note="short chain dehydrogenase/reductase family 31E,
                     member 1; protein H105e3; 3-beta-hydroxysteroid
                     dehydrogenase; epididymis secretory sperm binding protein;
                     NAD(P) dependent steroid dehydrogenase-like protein
                     transcript; 3beta-hydroxysteroid-4alpha-carboxylate
                     3-dehydrogenase (decarboxylating)"
                     /calculated_mol_wt=41769
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15738.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15738.2)"
     Region          39..366
                     /region_name="3b-HSD-NSDHL-like_SDR_e"
                     /note="human NSDHL (NAD(P)H steroid dehydrogenase-like
                     protein)-like, extended (e) SDRs; cd09813"
                     /db_xref="CDD:187673"
     Site            order(44,46..49,68..70,104..106,120,143..145,172,176,
                     200..203)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187673"
     Site            order(121,145,172,176)
                     /site_type="active"
                     /db_xref="CDD:187673"
     Site            order(145,172,202,215,226,231)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:187673"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15738.2)"
     Region          370..373
                     /region_name="Prevents secretion from ER.
                     /evidence=ECO:0000250|UniProtKB:Q9R1J0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15738.2)"
     CDS             1..373
                     /gene="NSDHL"
                     /gene_synonym="H105E3; SDR31E1; XAP104"
                     /coded_by="NM_015922.3:99..1220"
                     /db_xref="CCDS:CCDS14717.1"
                     /db_xref="GeneID:50814"
                     /db_xref="HGNC:HGNC:13398"
                     /db_xref="MIM:300275"
ORIGIN      
        1 mepavsepmr dqvarthlte dtpkvnadie kvnqnqakrc tviggsgflg qhmveqllar
       61 gyavnvfdiq qgfdnpqvrf flgdlcsrqd lypalkgvnt vfhcasppps snnkelfyrv
      121 nyigtknvie tckeagvqkl iltssasvif egvdikngte dlpyamkpid yytetkilqe
      181 ravlgandpe knflttairp hgifgprdpq lvpilieaar ngkmkfvign gknlvdftfv
      241 envvhghila aeqlsrdstl ggkafhitnd epipfwtfls riltglnyea pkyhipywva
      301 yylalllsll vmvispviql qptftpmrva lagtfhyysc erakkamgyq plvtmddame
      361 rtvqsfrhlr rvk
//
LOCUS       NP_001123554            2135 aa            linear   PRI 20-NOV-2025
DEFINITION  plexin-B1 precursor [Homo sapiens].
ACCESSION   NP_001123554
VERSION     NP_001123554.1
DBSOURCE    REFSEQ: accession NM_001130082.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2135)
  AUTHORS   Xuan,Z., Zhang,Y., Li,D., Wang,K., Huang,P. and Shi,J.
  TITLE     PLXNB1/SEMA4D signals mediate interactions between malignant
            epithelial and immune cells to promote colorectal cancer liver
            metastasis
  JOURNAL   J Cell Mol Med 28 (20), e70142 (2024)
   PUBMED   39443302
  REMARK    GeneRIF: PLXNB1/SEMA4D signals mediate interactions between
            malignant epithelial and immune cells to promote colorectal cancer
            liver metastasis.
REFERENCE   2  (residues 1 to 2135)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2135)
  AUTHORS   Yang,G., Ullah,H.M.A., Parker,E., Gorsi,B., Libowitz,M.,
            Maguire,C., King,J.B., Coon,H., Lopez-Larson,M., Anderson,J.S.,
            Yandell,M. and Shcheglovitov,A.
  TITLE     Neurite outgrowth deficits caused by rare PLXNB1 mutation in
            pediatric bipolar disorder
  JOURNAL   Mol Psychiatry 28 (6), 2525-2539 (2023)
   PUBMED   37032361
  REMARK    GeneRIF: Neurite outgrowth deficits caused by rare PLXNB1 mutation
            in pediatric bipolar disorder.
REFERENCE   4  (residues 1 to 2135)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2135)
  AUTHORS   Welch,B.A., Cho,H.J., Ucakturk,S.A., Farmer,S.M., Cetinkaya,S.,
            Abaci,A., Akkus,G., Simsek,E., Kotan,L.D., Turan,I., Gurbuz,F.,
            Yuksel,B., Wray,S. and Topaloglu,A.K.
  TITLE     PLXNB1 mutations in the etiology of idiopathic hypogonadotropic
            hypogonadism
  JOURNAL   J Neuroendocrinol 34 (4), e13103 (2022)
   PUBMED   35170806
  REMARK    GeneRIF: PLXNB1 mutations in the etiology of idiopathic
            hypogonadotropic hypogonadism.
REFERENCE   6  (residues 1 to 2135)
  AUTHORS   Swiercz,J.M., Kuner,R., Behrens,J. and Offermanns,S.
  TITLE     Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA
            and growth cone morphology
  JOURNAL   Neuron 35 (1), 51-63 (2002)
   PUBMED   12123608
REFERENCE   7  (residues 1 to 2135)
  AUTHORS   Vikis,H.G., Li,W. and Guan,K.L.
  TITLE     The plexin-B1/Rac interaction inhibits PAK activation and enhances
            Sema4D ligand binding
  JOURNAL   Genes Dev 16 (7), 836-845 (2002)
   PUBMED   11937491
  REMARK    GeneRIF: The plexin-B1/Rac interaction inhibits PAK activation and
            enhances Sema4D ligand binding
REFERENCE   8  (residues 1 to 2135)
  AUTHORS   Vikis,H.G., Li,W., He,Z. and Guan,K.L.
  TITLE     The semaphorin receptor plexin-B1 specifically interacts with
            active Rac in a ligand-dependent manner
  JOURNAL   Proc Natl Acad Sci U S A 97 (23), 12457-12462 (2000)
   PUBMED   11035813
REFERENCE   9  (residues 1 to 2135)
  AUTHORS   Tamagnone,L., Artigiani,S., Chen,H., He,Z., Ming,G.I., Song,H.,
            Chedotal,A., Winberg,M.L., Goodman,C.S., Poo,M., Tessier-Lavigne,M.
            and Comoglio,P.M.
  TITLE     Plexins are a large family of receptors for transmembrane,
            secreted, and GPI-anchored semaphorins in vertebrates
  JOURNAL   Cell 99 (1), 71-80 (1999)
   PUBMED   10520995
  REMARK    Erratum:[Cell 2001 Jan 26;104(2):following 320]
REFERENCE   10 (residues 1 to 2135)
  AUTHORS   Maestrini,E., Tamagnone,L., Longati,P., Cremona,O., Gulisano,M.,
            Bione,S., Tamanini,F., Neel,B.G., Toniolo,D. and Comoglio,P.M.
  TITLE     A family of transmembrane proteins with homology to the
            MET-hepatocyte growth factor receptor
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 674-678 (1996)
   PUBMED   8570614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC134772.2, BC066773.1 and AB007867.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC066773.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296440.11/ ENSP00000296440.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..2135
                     /product="plexin-B1 precursor"
                     /note="plexin 5; semaphorin receptor SEP"
                     /calculated_mol_wt=230308
     sig_peptide     1..19
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
                     /calculated_mol_wt=2008
     mat_peptide     20..2135
                     /product="Plexin-B1. /id=PRO_0000024671"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
                     /calculated_mol_wt=230308
     Region          28..480
                     /region_name="Sema_plexin_B1"
                     /note="The Sema domain, a protein interacting module, of
                     Plexin B1; cd11275"
                     /db_xref="CDD:200536"
     Site            31
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Site            order(80..82,136,138..140,178,202,207,209..210,212..213,
                     235,242,361..362,367..368,375,380..382)
                     /site_type="other"
                     /note="Semaphorin binding site [polypeptide binding]"
                     /db_xref="CDD:200536"
     Site            334
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          481..527
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          541..627
                     /region_name="TIG_plexin"
                     /note="TIG domain; pfam17960"
                     /db_xref="CDD:465588"
     Site            543
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          641..677
                     /region_name="PSI"
                     /note="domain found in Plexins, Semaphorins and Integrins;
                     smart00423"
                     /db_xref="CDD:214655"
     Region          671..829
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          <681..839
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          849..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          921..1020
                     /region_name="TIG_2"
                     /note="TIG domain found in plexin; pfam18020"
                     /db_xref="CDD:465619"
     Region          1021..>1061
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Region          1070..1161
                     /region_name="IPT_plexin_repeat1"
                     /note="First repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01180"
                     /db_xref="CDD:238585"
     Region          1162..1249
                     /region_name="IPT_plexin_repeat2"
                     /note="Second repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01179"
                     /db_xref="CDD:238584"
     Site            1183
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Region          1252..1376
                     /region_name="IPT_plexin_repeat3"
                     /note="Third repeat of the IPT domain of Plexins and Cell
                     Surface Receptors (PCSR) . Plexins are involved in the
                     regulation of cell proliferation and of cellular adhesion
                     and repulsion receptors. In general, there are three
                     copies of the IPT domain present...; cd01181"
                     /db_xref="CDD:238586"
     Site            1253
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973;
                     propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Site            1305..1306
                     /site_type="cleavage"
                     /note="Cleavage, by proprotein convertases; propagated
                     from UniProtKB/Swiss-Prot (O43157.3)"
     Site            1330
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O43157.3)"
     Site            1491..1511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          1562..2097
                     /region_name="Plexin_cytopl"
                     /note="Plexin cytoplasmic RasGAP domain; pfam08337"
                     /db_xref="CDD:462434"
     Site            1815
                     /site_type="other"
                     /note="Important for interaction with RAC1 and RND1;
                     propagated from UniProtKB/Swiss-Prot (O43157.3)"
     Region          1883..1908
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43157.3)"
     CDS             1..2135
                     /gene="PLXNB1"
                     /gene_synonym="PLEXIN-B1; PLXN5; SEP"
                     /coded_by="NM_001130082.3:139..6546"
                     /db_xref="CCDS:CCDS2765.1"
                     /db_xref="GeneID:5364"
                     /db_xref="HGNC:HGNC:9103"
                     /db_xref="MIM:601053"
ORIGIN      
        1 mpalgpallq alwagwvltl qplpptaftp ngtylqhlar dptsgtlylg atnflfqlsp
       61 glqleatvst gpvldsrdcl ppvmpdecpq aqptnnpnql llvspgalvv cgsvhqgvce
      121 qrrlgqleql llrperpgdt qyvaandpav stvglvaqgl agepllfvgr gytsrgvggg
      181 ippittralw ppdpqaafsy eetaklavgr lseyshhfvs afargasayf lflrrdlqaq
      241 srafrayvsr vclrdqhyys yvelplaceg grygliqaaa vatsrevahg evlfaafssa
      301 apptvgrpps aaagasgasa lcafpldevd rlanrtrdac ytregraedg tevayieydv
      361 nsdcaqlpvd tldaypcgsd htpspmasrv pleatpilew pgiqltavav tmedghtiaf
      421 lgdsqgqlhr vylgpgsdgh pystqsiqqg savsrdltfd gtfehlyvmt qstllkvpva
      481 scaqhldcas clahrdpycg wcvllgrcsr rsecsrgqgp eqwlwsfqpe lgclqvaams
      541 panisreetr evflsvpdlp plwpgesysc hfgehqspal ltgsgvmcps pdpseapvlp
      601 rgadyvsvsv elrfgavvia ktslsfydcv avtelrpsaq cqacvssrwg cnwcvwqhlc
      661 thkascdagp mvashqsplv spdpparggp spspptapka latpapdtlp vepgapstat
      721 asdispgasp sllspwgpwa gsgsisspgs tgsplheeps ppspqngpgt avpaptdfrp
      781 satpedllas plspsevaav ppadpgpeal hptvpldlpp atvpattfpg amgsvkpald
      841 wltreggelp eadewtggda pafststlls gdgdsaeleg ppaplilpss ldyqydtpgl
      901 weleeatlga sscpcvesvq gstlmpvhve reirllgrnl hlfqdgpgdn ecvmelegle
      961 vvvearvece pppdtqchvt cqqhqlsyea lqpelrvglf lrragrlrvd saeglhvvly
     1021 dcsvghgdcs rcqtampqyg cvwcegerpr cvtreacgea eavatqcpap lihsvepltg
     1081 pvdggtrvti rgsnlgqhvq dvlgmvtvag vpcavdaqey evssslvcit gasgeevaga
     1141 tavevpgrgr gvsehdfayq dpkvhsifpa rgpraggtrl tlngsklltg rledirvvvg
     1201 dqpchllpeq qseqlrcets prptpatlpv avwfgaterr lqrgqfkytl dpnitsagpt
     1261 ksflsggrei cvrgqnldvv qtprirvtvv srmlqpsqgl grrrrvvpet acslgpscss
     1321 qqfeepchvn ssqlitcrtp alpglpedpw vrvefildnl vfdfatlnpt pfsyeadptl
     1381 qplnpedptm pfrhkpgsvf svegenldla mskeevvami gdgpcvvktl trhhlycepp
     1441 veqplprhha lreapdslpe ftvqmgnlrf slghvqydge spgafpvaaq vglgvgtsll
     1501 algviiivlm yrrkskqalr dykkvqiqle nlessvrdrc kkeftdlmte mtdltsdllg
     1561 sgipfldykv yaeriffpgh resplhrdlg vpesrrptve qglgqlsnll nsklfltkfi
     1621 htlesqrtfs ardrayvasl ltvalhgkle yftdilrtll sdlvaqyvak npklmlrrte
     1681 tvveklltnw msiclytfvr dsvgeplyml frgikhqvdk gpvdsvtgka kytlndnrll
     1741 redveyrplt lnallavgpg ageaqgvpvk vldcdtisqa kekmldqlyk gvpltqrpdp
     1801 rtldvewrsg vaghlilsde dvtsevqglw rrlntlqhyk vpdgatvalv pcltkhvlre
     1861 nqdyvpgert pmledvdegg irpwhlvkps depepprprr gslrggerer akaipeiylt
     1921 rllsmkgtlq kfvddlfqvi lstsrpvpla vkyffdllde qaqqhgisdq dtihiwktns
     1981 lplrfwinii knpqfvfdvq tsdnmdavll viaqtfmdac tladhklgrd spinkllyar
     2041 diprykrmve ryyadirqtv pasdqemnsv laelswnysg dlgarvalhe lykyinkyyd
     2101 qiitaleedg taqkmqlgyr lqqiaaaven kvtdl
//
LOCUS       NP_001304115             227 aa            linear   PRI 20-NOV-2025
DEFINITION  cadherin-1 isoform 4 [Homo sapiens].
ACCESSION   NP_001304115
VERSION     NP_001304115.1
DBSOURCE    REFSEQ: accession NM_001317186.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 227)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   2  (residues 1 to 227)
  AUTHORS   Dash,S., Biswas,J., Goswami,S., Mukherjee,S., Ganguli,N.,
            Duraivelan,K., Mondal,S., Mukhopadhyay,R. and Samanta,D.
  TITLE     Molecular Crosstalk Between Adherens Junction Proteins, E-cadherin
            and Nectin-4
  JOURNAL   J Mol Biol 436 (18), 168709 (2024)
   PUBMED   39009071
  REMARK    GeneRIF: Molecular Crosstalk Between Adherens Junction Proteins,
            E-cadherin and Nectin-4.
REFERENCE   3  (residues 1 to 227)
  AUTHORS   Peng,Y., Zhang,Y., Fang,R., Jiang,H., Lan,G., Xu,Z., Liu,Y.,
            Nie,Z., Ren,L., Wang,F., Zhang,S.D., Ma,Y., Yang,P., Ge,H.H.,
            Zhang,W.D., Luo,C., Li,A. and He,W.
  TITLE     Target Identification and Mechanistic Characterization of Indole
            Terpenoid Mimics: Proper Spindle Microtubule Assembly Is Essential
            for Cdh1-Mediated Proteolysis of CENP-A
  JOURNAL   Adv Sci (Weinh) 11 (29), e2305593 (2024)
   PUBMED   38873820
REFERENCE   4  (residues 1 to 227)
  AUTHORS   Yim,I.S. and Laronde,D.M.
  TITLE     Biomarkers of epithelial-mesenchymal transition: E-cadherin and
            beta-catenin in malignant transformation of oral lesions
  JOURNAL   Can J Dent Hyg 58 (2), 111-119 (2024)
   PUBMED   38974823
  REMARK    GeneRIF: Biomarkers of epithelial-mesenchymal transition:
            E-cadherin and beta-catenin in malignant transformation of oral
            lesions.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 227)
  AUTHORS   Lecuit,T. and Yap,A.S.
  TITLE     E-cadherin junctions as active mechanical integrators in tissue
            dynamics
  JOURNAL   Nat Cell Biol 17 (5), 533-539 (2015)
   PUBMED   25925582
  REMARK    Review article
REFERENCE   6  (residues 1 to 227)
  AUTHORS   Barbosa-Matos,R., Cordova,L., Schrader,K. and Oliveira,C.
  TITLE     Diffuse Gastric and Lobular Breast Cancer Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301318
REFERENCE   7  (residues 1 to 227)
  AUTHORS   Knudsen,K.A. and Wheelock,M.J.
  TITLE     Plakoglobin, or an 83-kD homologue distinct from beta-catenin,
            interacts with E-cadherin and N-cadherin
  JOURNAL   J Cell Biol 118 (3), 671-679 (1992)
   PUBMED   1639850
REFERENCE   8  (residues 1 to 227)
  AUTHORS   La Vecchia,C., Negri,E., Franceschi,S. and Gentile,A.
  TITLE     Family history and the risk of stomach and colorectal cancer
  JOURNAL   Cancer 70 (1), 50-55 (1992)
   PUBMED   1606546
REFERENCE   9  (residues 1 to 227)
  AUTHORS   Zanghieri,G., Di Gregorio,C., Sacchetti,C., Fante,R.,
            Sassatelli,R., Cannizzo,G., Carriero,A. and Ponz de Leon,M.
  TITLE     Familial occurrence of gastric cancer in the 2-year experience of a
            population-based registry
  JOURNAL   Cancer 66 (9), 2047-2051 (1990)
   PUBMED   2224804
REFERENCE   10 (residues 1 to 227)
  AUTHORS   Mansouri,A., Spurr,N., Goodfellow,P.N. and Kemler,R.
  TITLE     Characterization and chromosomal localization of the gene encoding
            the human cell adhesion molecule uvomorulin
  JOURNAL   Differentiation 38 (1), 67-71 (1988)
   PUBMED   3263290
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312551.1, BC144283.1 and
            EU709494.1.
            
            Summary: This gene encodes a classical cadherin of the cadherin
            superfamily. Alternative splicing results in multiple transcript
            variants, at least one of which encodes a preproprotein that is
            proteolytically processed to generate the mature glycoprotein. This
            calcium-dependent cell-cell adhesion protein is comprised of five
            extracellular cadherin repeats, a transmembrane region and a highly
            conserved cytoplasmic tail. Mutations in this gene are correlated
            with gastric, breast, colorectal, thyroid and ovarian cancer. Loss
            of function of this gene is thought to contribute to cancer
            progression by increasing proliferation, invasion, and/or
            metastasis. The ectodomain of this protein mediates bacterial
            adhesion to mammalian cells and the cytoplasmic domain is required
            for internalization. This gene is present in a gene cluster with
            other members of the cadherin family on chromosome 16. [provided by
            RefSeq, Nov 2015].
            
            Transcript Variant: This variant (4) lacks an exon in its 5' UTR,
            resulting in a different 5' UTR and the use of a downstream start
            site compared to variant 1. The encoded isoform (4) has a shorter
            N-terminus and lacks a predicted signal peptide compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.208131.1, BC144283.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..227
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..227
                     /product="cadherin-1 isoform 4"
                     /note="calcium-dependent adhesion protein, epithelial;
                     cadherin 1, E-cadherin (epithelial); cell-CAM 120/80;
                     uvomorulin; epithelial cadherin; cadherin 1, type 1,
                     E-cadherin (epithelial); E-cadherin 1; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=24915
     Region          163..222
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..227
                     /gene="CDH1"
                     /gene_synonym="Arc-1; BCDS1; CD324; CDHE; ECAD; LCAM; UVO"
                     /coded_by="NM_001317186.2:1944..2627"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:999"
                     /db_xref="HGNC:HGNC:1748"
                     /db_xref="MIM:192090"
ORIGIN      
        1 malevgdyki nlklmdnqnk dqvttlevsv cdcegaagvc rkaqpveagl qipailgilg
       61 gilallilil llllflrrra vvkepllppe ddtrdnvyyy deegggeedq dfdlsqlhrg
      121 ldarpevtrn dvaptlmsvp rylprpanpd eignfidenl kaadtdptap pydsllvfdy
      181 egsgseaasl sslnssesdk dqdydylnew gnrfkkladm ygggedd
//
LOCUS       NP_073617                391 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein transferase RMND5A [Homo sapiens].
ACCESSION   NP_073617
VERSION     NP_073617.1
DBSOURCE    REFSEQ: accession NM_022780.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Gottemukkala,K.V., Chrustowicz,J., Sherpa,D., Sepic,S., Vu,D.T.,
            Karayel,O., Papadopoulou,E.C., Gross,A., Schorpp,K., von Gronau,S.,
            Hadian,K., Murray,P.J., Mann,M., Schulman,B.A. and Alpi,A.F.
  TITLE     Non-canonical substrate recognition by the human WDR26-CTLH E3
            ligase regulates prodrug metabolism
  JOURNAL   Mol Cell 84 (10), 1948-1963 (2024)
   PUBMED   38759627
  REMARK    GeneRIF: Non-canonical substrate recognition by the human
            WDR26-CTLH E3 ligase regulates prodrug metabolism.
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Deng,X., Ma,J., Zhou,W., Yuan,Y., Wang,B. and Meng,X.
  TITLE     GID2 Interacts With CDKN3 and Regulates Pancreatic Cancer Growth
            and Apoptosis
  JOURNAL   Lab Invest 103 (6), 100122 (2023)
   PUBMED   36828188
  REMARK    GeneRIF: GID2 Interacts With CDKN3 and Regulates Pancreatic Cancer
            Growth and Apoptosis.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Li,J., Chen,Y., Qin,X., Wen,J., Ding,H., Xia,W., Li,S., Su,X.,
            Wang,W., Li,H., Zhao,Q., Fang,T., Qu,L. and Shao,N.
  TITLE     MiR-138 downregulates miRNA processing in HeLa cells by targeting
            RMND5A and decreasing Exportin-5 stability
  JOURNAL   Nucleic Acids Res 42 (1), 458-474 (2014)
   PUBMED   24057215
  REMARK    GeneRIF: The study identifies a miR-138-RMND5A-Exportin-5 as a
            previously unknown miRNA processing regulatory pathway in HeLa
            cells.
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Vogel,T.W., Manjila,S. and Cohen,A.R.
  TITLE     Novel neurodevelopmental disorder in the case of a giant
            occipitoparietal meningoencephalocele
  JOURNAL   J Neurosurg Pediatr 10 (1), 25-29 (2012)
   PUBMED   22681319
  REMARK    GeneRIF: Duplications of this region involving RMND5A, whose
            product contains a C-terminal to lis homology (LisH) domain, have
            not previously been associated with a defined phenotype but may
            present insight into encephalocele formation.
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells.
REFERENCE   9  (residues 1 to 391)
  AUTHORS   Bowzard,J.B., Cheng,D., Peng,J. and Kahn,R.A.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J Biol Chem 282 (24), 17568-17580 (2007)
   PUBMED   17452337
REFERENCE   10 (residues 1 to 391)
  AUTHORS   Colland,F., Jacq,X., Trouplin,V., Mougin,C., Groizeleau,C.,
            Hamburger,A., Meil,A., Wojcik,J., Legrain,P. and Gauthier,J.M.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023972.1, BC047668.1, BC012165.1, AC064848.5 and BU620245.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.90910.1,
                                           SRR1660805.158266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000283632.5/ ENSP00000283632.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..391
                     /product="E3 ubiquitin-protein transferase RMND5A"
                     /EC_number="2.3.2.27"
                     /note="C-terminal to LisH motif, 44 kDa; protein RMD5
                     homolog A; GID complex subunit 2 homolog A; 44-kD protein
                     coding for CTLH motif"
                     /calculated_mol_wt=43862
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H871.1)"
     Region          17..391
                     /region_name="COG5109"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227440"
     Region          153..297
                     /region_name="CTLH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:402305"
     CDS             1..391
                     /gene="RMND5A"
                     /gene_synonym="CTLH; GID2; GID2A; p44CTLH; RMD5"
                     /coded_by="NM_022780.4:378..1553"
                     /db_xref="CCDS:CCDS1991.1"
                     /db_xref="GeneID:64795"
                     /db_xref="HGNC:HGNC:25850"
                     /db_xref="MIM:618964"
ORIGIN      
        1 mdqcvtvere lekvlhkfsg ygqlcergle elidytgglk heilqshgqd aelsgtlslv
       61 ltqcckrikd tvqklasdhk dihssvsrvg kaidknfdsd issvgidgcw qadsqrllne
      121 vmvehffrqg mldvaeelcq esglsvdpsq kepfvelnri lealkvrvlr palewavsnr
      181 emliaqnssl efklhrlyfi sllmggttnq realqyaknf qpfalnhqkd iqvlmgslvy
      241 lrqgienspy vhlldanqwa dicdiftrda callglsves plsvsfsagc valpalinik
      301 avieqrqctg vwnqkdelpi evdlgkkcwy hsifacpilr qqttdnnppm klvcghiisr
      361 dalnkmfngs klkcpycpme qspgdakqif f
//
LOCUS       NP_055255                158 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-36 alpha [Homo sapiens].
ACCESSION   NP_055255
VERSION     NP_055255.1
DBSOURCE    REFSEQ: accession NM_014440.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Ahmad,F., Alam,M.A., Ansari,A.W., Jochebeth,A., Leo,R.,
            Al-Abdulla,M.N., Al-Khawaga,S., AlHammadi,A., Al-Malki,A., Al
            Naama,K., Ahmad,A., Buddenkotte,J. and Steinhoff,M.
  TITLE     Emerging Role of the IL-36/IL-36R Axis in Multiple Inflammatory
            Skin Diseases
  JOURNAL   J Invest Dermatol 144 (2), 206-224 (2024)
   PUBMED   38189700
  REMARK    GeneRIF: Emerging Role of the IL-36/IL-36R Axis in Multiple
            Inflammatory Skin Diseases.
            Review article
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Zysk,W., Sitko,K., Tukaj,S., Zaryczanska,A. and Trzeciak,M.
  TITLE     Altered Gene Expression of IL-35 and IL-36alpha in the Skin of
            Patients with Atopic Dermatitis
  JOURNAL   Int J Mol Sci 25 (1), 404 (2023)
   PUBMED   38203575
  REMARK    GeneRIF: Altered Gene Expression of IL-35 and IL-36alpha in the
            Skin of Patients with Atopic Dermatitis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Dong,H., Hao,Y., Li,W., Yang,W. and Gao,P.
  TITLE     IL-36 Cytokines: Their Roles in Asthma and Potential as a
            Therapeutic
  JOURNAL   Front Immunol 13, 921275 (2022)
   PUBMED   35903102
  REMARK    GeneRIF: IL-36 Cytokines: Their Roles in Asthma and Potential as a
            Therapeutic.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Huang,S., Feng,T., Wang,J. and Dong,L.
  TITLE     IL-36 is Closely Related to Neutrophilic Inflammation in Chronic
            Obstructive Pulmonary Disease
  JOURNAL   Int J Chron Obstruct Pulmon Dis 17, 1339-1347 (2022)
   PUBMED   35698471
  REMARK    GeneRIF: IL-36 is Closely Related to Neutrophilic Inflammation in
            Chronic Obstructive Pulmonary Disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Kumar,S., McDonnell,P.C., Lehr,R., Tierney,L., Tzimas,M.N.,
            Griswold,D.E., Capper,E.A., Tal-Singer,R., Wells,G.I., Doyle,M.L.
            and Young,P.R.
  TITLE     Identification and initial characterization of four novel members
            of the interleukin-1 family
  JOURNAL   J Biol Chem 275 (14), 10308-10314 (2000)
   PUBMED   10744718
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Smith,D.E., Renshaw,B.R., Ketchem,R.R., Kubin,M., Garka,K.E. and
            Sims,J.E.
  TITLE     Four new members expand the interleukin-1 superfamily
  JOURNAL   J Biol Chem 275 (2), 1169-1175 (2000)
   PUBMED   10625660
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Mulero,J.J., Pace,A.M., Nelken,S.T., Loeb,D.B., Correa,T.R.,
            Drmanac,R. and Ford,J.E.
  TITLE     IL1HY1: A novel interleukin-1 receptor antagonist gene
  JOURNAL   Biochem Biophys Res Commun 263 (3), 702-706 (1999)
   PUBMED   10512743
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Nothwang,H.G., Strahm,B., Denich,D., Kubler,M., Schwabe,J.,
            Gingrich,J.C., Jauch,A., Cox,A., Nicklin,M.J., Kurnit,D.M. and
            Hildebrandt,F.
  TITLE     Molecular cloning of the interleukin-1 gene cluster: construction
            of an integrated YAC/PAC contig and a partial transcriptional map
            in the region of chromosome 2q13
  JOURNAL   Genomics 41 (3), 370-378 (1997)
   PUBMED   9169134
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Nicklin,M.J., Weith,A. and Duff,G.W.
  TITLE     A physical map of the region encompassing the human interleukin-1
            alpha, interleukin-1 beta, and interleukin-1 receptor antagonist
            genes
  JOURNAL   Genomics 19 (2), 382-384 (1994)
   PUBMED   8188271
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC016724.11, AK314149.1 and
            AF201831.1.
            
            Summary: The protein encoded by this gene is a cytokine that can
            activate NF-kappa-B and MAPK signaling pathways to generate an
            inflammatory response. The encoded protein functions primarily in
            skin and demonstrates increased expression in psoriasis. In
            addition, decreased expression of this gene has been linked to a
            poor prognosis in both hepatocellular carcinoma and colorectal
            cancer patients. [provided by RefSeq, Nov 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314149.1, BC107043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2156670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259211.7/ ENSP00000259211.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.1"
     Protein         1..158
                     /product="interleukin-36 alpha"
                     /note="interleukin 1 family, member 6 (epsilon);
                     interleukin-1 family member 6; IL-1F6 (FIL-1-epsilon);
                     FIL1 epsilon; IL-1 epsilon; interleukin-1 epsilon"
                     /calculated_mol_wt=17553
     mat_peptide     6..158
                     /product="Interleukin-36 alpha. /id=PRO_0000153644"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHA7.1)"
                     /calculated_mol_wt=17112
     Region          9..156
                     /region_name="beta-trefoil_IL36"
                     /note="beta-trefoil domain found in the family of
                     interleukin-36 (IL-36) and similar proteins; cd23300"
                     /db_xref="CDD:466782"
     Site            order(11,46,48,61,63,109,111,116,152..154,156)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:466782"
     CDS             1..158
                     /gene="IL36A"
                     /gene_synonym="FIL1; FIL1(EPSILON); FIL1E; IL-1F6;
                     IL1(EPSILON); IL1F6"
                     /coded_by="NM_014440.3:414..890"
                     /db_xref="CCDS:CCDS42734.1"
                     /db_xref="GeneID:27179"
                     /db_xref="HGNC:HGNC:15562"
                     /db_xref="MIM:605509"
ORIGIN      
        1 mekalkidtp qqgsiqdinh rvwvlqdqtl iavprkdrms pvtialiscr hvetlekdrg
       61 npiylglngl nlclmcakvg dqptlqlkek dimdlynqpe pvksflfyhs qsgrnstfes
      121 vafpgwfiav sseggcplil tqelgkantt dfgltmlf
//
LOCUS       NP_001317328             109 aa            linear   PRI 20-NOV-2025
DEFINITION  spindle and kinetochore-associated protein 2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001317328 XP_011523047
VERSION     NP_001317328.1
DBSOURCE    REFSEQ: accession NM_001330399.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 109)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 109)
  AUTHORS   Valenzuela-Garcia,L.I., Ayala-Garcia,V.M., Ramos-Rosales,D.F.,
            Jacquez-Flores,R.E., Urtiz-Estrada,N., Hernandez,E.M.M. and
            Barraza-Salas,M.
  TITLE     The rs7208505 Polymorphism and Differential Expression of the SKA2
            Gene in the Prefrontal Cortex of Suicide Victims from the Mexican
            Population
  JOURNAL   Arch Suicide Res 28 (2), 674-685 (2024)
   PUBMED   37204142
  REMARK    GeneRIF: The rs7208505 Polymorphism and Differential Expression of
            the SKA2 Gene in the Prefrontal Cortex of Suicide Victims from the
            Mexican Population.
REFERENCE   3  (residues 1 to 109)
  AUTHORS   Hartmann,J., Bajaj,T., Otten,J., Klengel,C., Ebert,T.,
            Gellner,A.K., Junglas,E., Hafner,K., Anderzhanova,E.A., Tang,F.,
            Missig,G., Rexrode,L., Trussell,D.T., Li,K.X., Pohlmann,M.L.,
            Mackert,S., Geiger,T.M., Heinz,D.E., Lardenoije,R., Dedic,N.,
            McCullough,K.M., Prochnicki,T., Rhomberg,T., Martinelli,S.,
            Payton,A., Robinson,A.C., Stein,V., Latz,E., Carlezon,W.A. Jr.,
            Hausch,F., Schmidt,M.V., Murgatroyd,C., Berretta,S., Klengel,T.,
            Pantazopoulos,H., Ressler,K.J. and Gassen,N.C.
  TITLE     SKA2 regulated hyperactive secretory autophagy drives
            neuroinflammation-induced neurodegeneration
  JOURNAL   Nat Commun 15 (1), 2635 (2024)
   PUBMED   38528004
  REMARK    GeneRIF: SKA2 regulated hyperactive secretory autophagy drives
            neuroinflammation-induced neurodegeneration.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 109)
  AUTHORS   Goltser-Dubner,T., Shalev,A., Benarroch,F., Canetti,L., Yogev,M.,
            Kalla,C., Masarwa,R., Martin,J., Pevzner,D., Oz,O., Saloner,C.,
            Amer,R., Lavon,M., Lotan,A., Galili-Weisstub,E. and Segman,R.
  TITLE     Decreased mononuclear cell NR3C1 SKA2 and FKPB5 expression levels
            among adult survivors of suicide bombing terror attacks in
            childhood are associated with the development of PTSD
  JOURNAL   Mol Psychiatry 28 (9), 3851-3855 (2023)
   PUBMED   37845495
  REMARK    GeneRIF: Decreased mononuclear cell NR3C1 SKA2 and FKPB5 expression
            levels among adult survivors of suicide bombing terror attacks in
            childhood are associated with the development of PTSD.
REFERENCE   5  (residues 1 to 109)
  AUTHORS   Yu,D.C., Chen,X.Y., Li,X., Zhou,H.Y., Yu,D.Q., Yu,X.L., Hu,Y.C.,
            Zhang,R.H., Zhang,X.B., Zhang,K. and An,J.D.
  TITLE     Transcript levels of spindle and kinetochore-associated complex 1/3
            as prognostic biomarkers correlated with immune infiltrates in
            hepatocellular carcinoma
  JOURNAL   Sci Rep 11 (1), 11165 (2021)
   PUBMED   34045512
  REMARK    GeneRIF: Transcript levels of spindle and kinetochore-associated
            complex 1/3 as prognostic biomarkers correlated with immune
            infiltrates in hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 109)
  AUTHORS   Cao,G., Huang,B., Liu,Z., Zhang,J., Xu,H., Xia,W., Li,J., Li,S.,
            Chen,L., Ding,H., Zhao,Q., Fan,M., Shen,B. and Shao,N.
  TITLE     Intronic miR-301 feedback regulates its host gene, ska2, in A549
            cells by targeting MEOX2 to affect ERK/CREB pathways
  JOURNAL   Biochem Biophys Res Commun 396 (4), 978-982 (2010)
   PUBMED   20470754
  REMARK    GeneRIF: blocking of miR-301 in A549 cells leads to a decrease in
            the expression of the host gene, ska2.
REFERENCE   7  (residues 1 to 109)
  AUTHORS   Gaitanos,T.N., Santamaria,A., Jeyaprakash,A.A., Wang,B., Conti,E.
            and Nigg,E.A.
  TITLE     Stable kinetochore-microtubule interactions depend on the Ska
            complex and its new component Ska3/C13Orf3
  JOURNAL   EMBO J 28 (10), 1442-1452 (2009)
   PUBMED   19360002
REFERENCE   8  (residues 1 to 109)
  AUTHORS   Welburn,J.P., Grishchuk,E.L., Backer,C.B., Wilson-Kubalek,E.M.,
            Yates,J.R. 3rd and Cheeseman,I.M.
  TITLE     The human kinetochore Ska1 complex facilitates microtubule
            depolymerization-coupled motility
  JOURNAL   Dev Cell 16 (3), 374-385 (2009)
   PUBMED   19289083
REFERENCE   9  (residues 1 to 109)
  AUTHORS   Rice,L., Waters,C.E., Eccles,J., Garside,H., Sommer,P., Kay,P.,
            Blackhall,F.H., Zeef,L., Telfer,B., Stratford,I., Clarke,R.,
            Singh,D., Stevens,A., White,A. and Ray,D.W.
  TITLE     Identification and functional analysis of SKA2 interaction with the
            glucocorticoid receptor
  JOURNAL   J Endocrinol 198 (3), 499-509 (2008)
   PUBMED   18583474
  REMARK    GeneRIF: Study discovered that FAM33A is protein partners for GRs
            and is involved in cell proliferation and GC signalling.
REFERENCE   10 (residues 1 to 109)
  AUTHORS   Hanisch,A., Sillje,H.H. and Nigg,E.A.
  TITLE     Timely anaphase onset requires a novel spindle and kinetochore
            complex comprising Ska1 and Ska2
  JOURNAL   EMBO J 25 (23), 5504-5515 (2006)
   PUBMED   17093495
  REMARK    GeneRIF: These data suggest that the Ska1/Ska2 complex plays a
            critical role in the maintenance of the metaphase plate and/or
            spindle checkpoint silencing.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB158057.1, DA020580.1, AC099850.7 and AK022820.1.
            
            On Aug 29, 2016 this sequence version replaced XP_011523047.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.888459.1,
                                           SRR1803613.97369.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155974 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..109
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q22"
     Protein         1..109
                     /product="spindle and kinetochore-associated protein 2
                     isoform 3"
                     /note="spindle and KT (kinetochore) associated 2; family
                     with sequence similarity 33, member A; spindle and
                     kinetochore-associated protein 2"
                     /calculated_mol_wt=12624
     Region          5..100
                     /region_name="SKA2"
                     /note="Spindle and kinetochore-associated protein 2;
                     cd12955"
                     /db_xref="CDD:214020"
     Site            order(5..9,11..12,15..16)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:214020"
     Site            order(12,15,19,22,25..26,29,50,53,57,61,71,78,85..86,89,
                     92,98)
                     /site_type="other"
                     /note="SKA3 interface [polypeptide binding]"
                     /db_xref="CDD:214020"
     Site            order(16,19..20,22..23,26,29..30,33,40,49,53,56,60,64,67,
                     70..71,74,78,81..82,84,88)
                     /site_type="other"
                     /note="SKA1 interface [polypeptide binding]"
                     /db_xref="CDD:214020"
     CDS             1..109
                     /gene="SKA2"
                     /gene_synonym="FAM33A"
                     /coded_by="NM_001330399.2:24..353"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82175.1"
                     /db_xref="GeneID:348235"
                     /db_xref="HGNC:HGNC:28006"
                     /db_xref="MIM:616674"
ORIGIN      
        1 meaevdklel mfqkaesdld yiqyrleyei ktnhpdsase knpvtllkel sviksryqtl
       61 yarfkpvave qkesksrica tvkktmnmiq klqkqtdlev mlsvdschh
//
LOCUS       NP_004564               1185 aa            linear   PRI 20-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
            isoform 1 [Homo sapiens].
ACCESSION   NP_004564
VERSION     NP_004564.2
DBSOURCE    REFSEQ: accession NM_004573.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1185)
  AUTHORS   Phoenix,K.N., Yue,Z., Yue,L., Cronin,C.G., Liang,B.T.,
            Hoeppner,L.H. and Claffey,K.P.
  TITLE     PLCbeta2 Promotes VEGF-Induced Vascular Permeability
  JOURNAL   Arterioscler Thromb Vasc Biol 42 (10), 1229-1241 (2022)
   PUBMED   35861069
  REMARK    GeneRIF: PLCbeta2 Promotes VEGF-Induced Vascular Permeability.
REFERENCE   2  (residues 1 to 1185)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1185)
  AUTHORS   Zhang,H., Xie,T., Shui,Y. and Qi,Y.
  TITLE     Knockdown of PLCB2 expression reduces melanoma cell viability and
            promotes melanoma cell apoptosis by altering Ras/Raf/MAPK signals
  JOURNAL   Mol Med Rep 21 (1), 420-428 (2020)
   PUBMED   31746389
  REMARK    GeneRIF: Knockdown of PLCB2 expression reduces melanoma cell
            viability and promotes melanoma cell apoptosis by altering
            Ras/Raf/MAPK signals.
REFERENCE   4  (residues 1 to 1185)
  AUTHORS   Bertagnolo,V., Grassilli,S., Volinia,S., Al-Qassab,Y., Brugnoli,F.,
            Vezzali,F., Lambertini,E., Palomba,M., Piubello,Q., Orvieto,E.,
            Natali,C., Piva,R., Croce,C.M. and Capitani,S.
  TITLE     Ectopic expression of PLC-beta2 in non-invasive breast tumor cells
            plays a protective role against malignant progression and is
            correlated with the deregulation of miR-146a
  JOURNAL   Mol Carcinog 58 (5), 708-721 (2019)
   PUBMED   30582225
  REMARK    GeneRIF: High PLCB2 expression is associated with breast cancer.
REFERENCE   5  (residues 1 to 1185)
  AUTHORS   Brugnoli,F., Grassilli,S., Lanuti,P., Marchisio,M., Al-Qassab,Y.,
            Vezzali,F., Capitani,S. and Bertagnolo,V.
  TITLE     Up-modulation of PLC-beta2 reduces the number and malignancy of
            triple-negative breast tumor cells with a CD133+/EpCAM+ phenotype:
            a promising target for preventing progression of TNBC
  JOURNAL   BMC Cancer 17 (1), 617 (2017)
   PUBMED   28870198
  REMARK    GeneRIF: this work adds substantial information about the role of
            PLC-beta2 in invasive breast tumors, demonstrating that its
            up-regulation in cells with a basal-B triple-negative phenotype is
            sufficient to down-modulate the expression of surface antigens
            crucial for malignancy and to reduce the number of cells with a
            stem-like phenotype.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1185)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   7  (residues 1 to 1185)
  AUTHORS   Buhl,A.M., Osawa,S. and Johnson,G.L.
  TITLE     Mitogen-activated protein kinase activation requires two signal
            inputs from the human anaphylatoxin C5a receptor
  JOURNAL   J Biol Chem 270 (34), 19828-19832 (1995)
   PUBMED   7649993
REFERENCE   8  (residues 1 to 1185)
  AUTHORS   Park,D., Jhon,D.Y., Kriz,R., Knopf,J. and Rhee,S.G.
  TITLE     Cloning, sequencing, expression, and Gq-independent activation of
            phospholipase C-beta 2
  JOURNAL   J Biol Chem 267 (23), 16048-16055 (1992)
   PUBMED   1644792
REFERENCE   9  (residues 1 to 1185)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1185)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA981116.1, AB209583.1,
            M95678.1 and BU147302.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 13, 2006 this sequence version replaced NP_004564.1.
            
            Summary: The protein encoded by this gene is a phosphodiesterase
            that catalyzes the hydrolysis of phosphatidylinositol
            4,5-bisphosphate to the second messengers inositol
            1,4,5-trisphosphate (IP3) and diacylglycerol. The encoded protein
            is activated by G proteins and has been shown to be involved in the
            type 2 taste receptor signal transduction pathway. In addition,
            nuclear factor kappa B can regulate the transcription of this gene,
            whose protein product is also an important regulator of platelet
            responses. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000260402.8/ ENSP00000260402.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..1185
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-2 isoform 1"
                     /EC_number="3.1.4.11"
                     /note="phosphoinositide phospholipase C-beta-2;
                     1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
                     beta-2"
                     /calculated_mol_wt=133894
     Region          12..141
                     /region_name="PH_14"
                     /note="PH domain; pfam17787"
                     /db_xref="CDD:465506"
     Region          149..299
                     /region_name="EFh_PI-PLCbeta2"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 2 (PI-PLC-beta2); cd16209"
                     /db_xref="CDD:320039"
     Region          149..178
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          182..211
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          220..249
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          266..299
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          311..649
                     /region_name="PI-PLCc_beta2"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta2; cd08624"
                     /db_xref="CDD:176561"
     Site            order(327..328,357,359,374,408,461,463,575,602,604)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176561"
     Site            order(327,374)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176561"
     Site            order(328,357,359,408)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176561"
     Region          460..533
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Region          681..802
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(700,725,757,761,763)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          859..888
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Region          879..>1074
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          943..979
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Site            953
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q00722.2)"
     Region          978..1153
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     CDS             1..1185
                     /gene="PLCB2"
                     /gene_synonym="PLC-beta-2"
                     /coded_by="NM_004573.3:264..3821"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42020.1"
                     /db_xref="GeneID:5330"
                     /db_xref="HGNC:HGNC:9055"
                     /db_xref="MIM:604114"
ORIGIN      
        1 msllnpvllp pkvkaylsqg erfikwddet tvaspvilrv dpkgyylywt yqskemefld
       61 itsirdtrfg kfakmpksqk lrdvfnmdfp dnsfllktlt vvsgpdmvdl tfhnfvsyke
      121 nvgkawaedv lalvkhplta nasrstfldk ilvklkmqln segkipvknf fqmfpadrkr
      181 veaalsachl pkgkndainp edfpepvyks flmslcprpe ideiftsyha kakpymtkeh
      241 ltkfinqkqr dsrlnsllfp parpdqvqgl idkyepsgin aqrgqlspeg mvwflcgpen
      301 svlaqdklll hhdmtqplnh yfinsshnty ltagqfsgls saemyrqvll sgcrcveldc
      361 wkgkppdeep iithgftmtt diffkeaiea iaesafktsp ypiilsfenh vdsprqqakm
      421 aeycrtifgd mllteplekf plkpgvplps pedlrgkili knkknqfsgp tssskdtgge
      481 aegssppsap agegtvwage egteleeeev eeeeeeesgn ldeeeikkmq sdegtaglev
      541 tayeemsslv nyiqptkfvs fefsaqknrs yvissftelk aydllskasv qfvdynkrqm
      601 sriypkgtrm dssnympqmf wnagcqmval nfqtmdlpmq qnmavfefng qsgyllkhef
      661 mrrpdkqfnp fsvdridvvv attlsitvis gqflsersvr tyvevelfgl pgdpkrryrt
      721 klspstnsin pvwkeepfvf ekilmpelas lrvavmeegn kflghriipi nalnsgyhhl
      781 clhsesnmpl tmpalfifle mkdyipgawa dltvalanpi kffsahdtks vklkeamggl
      841 pekpfplasp vasqvngala ptsngspaar agareeamke aaeprtasle elrelkgvvk
      901 lqrrhekelr elerrgarrw eellqrgaaq laelgppgvg gvgacklgpg kgsrkkrslp
      961 reesagaapg egpegvdgrv relkdrlele llrqgeeqye cvlkrkeqhv aeqiskmmel
     1021 arekqaaelk alketsendt kemkkkletk rleriqgmtk vttdkmaqer lkreinnshi
     1081 qevvqvikqm tenlerhqek leekqaacle qiremekqfq kealaeyear mkgleaevke
     1141 svraclrtcf pseakdkper acecppelce qdpliakada qesrl
//
LOCUS       NP_001354250             434 aa            linear   PRI 20-NOV-2025
DEFINITION  CCA tRNA nucleotidyltransferase 1, mitochondrial isoform 1 [Homo
            sapiens].
ACCESSION   NP_001354250 XP_011532080
VERSION     NP_001354250.1
DBSOURCE    REFSEQ: accession NM_001367321.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Meynier,V., Hardwick,S.W., Catala,M., Roske,J.J., Oerum,S.,
            Chirgadze,D.Y., Barraud,P., Yue,W.W., Luisi,B.F. and Tisne,C.
  TITLE     Structural basis for human mitochondrial tRNA maturation
  JOURNAL   Nat Commun 15 (1), 4683 (2024)
   PUBMED   38824131
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Fatica,T., Naas,T., Liwak,U., Slaa,H., Souaid,M., Frangione,B.,
            Kattini,R., Gaudreau-Lapierre,A., Trinkle-Mulcahy,L.,
            Chakraborty,P. and Holcik,M.
  TITLE     TRNT-1 Deficiency Is Associated with Loss of tRNA Integrity and
            Imbalance of Distinct Proteins
  JOURNAL   Genes (Basel) 14 (5), 1043 (2023)
   PUBMED   37239403
  REMARK    GeneRIF: TRNT-1 Deficiency Is Associated with Loss of tRNA
            Integrity and Imbalance of Distinct Proteins.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Seki,M., Komuro,A., Ishikawa,T., Takahashi,M. and Nashimoto,M.
  TITLE     Genes for tRNA recycling are upregulated in response to infection
            with Theiler's mouse encephalitis virus
  JOURNAL   Biochem Biophys Res Commun 587, 63-68 (2022)
   PUBMED   34864548
  REMARK    GeneRIF: Genes for tRNA recycling are upregulated in response to
            infection with Theiler's mouse encephalitis virus.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Odom,J., Amin,H., Gijavanekar,C., Elsea,S.H., Kralik,S., Chinen,J.,
            Lin,Y., Yates,A.M.M., Mizerik,E., Potocki,L. and Scaglia,F.
  TITLE     A phenotypic expansion of TRNT1 associated sideroblastic anemia
            with immunodeficiency, fevers, and developmental delay
  JOURNAL   Am J Med Genet A 188 (1), 259-268 (2022)
   PUBMED   34510712
  REMARK    GeneRIF: A phenotypic expansion of TRNT1 associated sideroblastic
            anemia with immunodeficiency, fevers, and developmental delay.
            Review article
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Augustin,M.A., Reichert,A.S., Betat,H., Huber,R., Morl,M. and
            Steegborn,C.
  TITLE     Crystal structure of the human CCA-adding enzyme: insights into
            template-independent polymerization
  JOURNAL   J Mol Biol 328 (5), 985-994 (2003)
   PUBMED   12729736
  REMARK    GeneRIF: The crystal structure reveals a four domain architecture
            with a cluster of conserved residues forming a positively charged
            cleft between the first two domains.
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Nagaike,T., Suzuki,T., Tomari,Y., Takemoto-Hori,C., Negayama,F.,
            Watanabe,K. and Ueda,T.
  TITLE     Identification and characterization of mammalian mitochondrial tRNA
            nucleotidyltransferases
  JOURNAL   J Biol Chem 276 (43), 40041-40049 (2001)
   PUBMED   11504732
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Reichert,A.S., Thurlow,D.L. and Morl,M.
  TITLE     A eubacterial origin for the human tRNA nucleotidyltransferase?
  JOURNAL   Biol Chem 382 (10), 1431-1438 (2001)
   PUBMED   11727826
  REMARK    GeneRIF: human gene transcript CGI-47 (#AF151805) was cloned and
            encodes a bona fide CCA-adding enzyme and not a poly(A) polymerase.
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC024060.6.
            
            On Nov 21, 2018 this sequence version replaced XP_011532080.1.
            
            Summary: The protein encoded by this gene is a CCA-adding enzyme
            which belongs to the tRNA nucleotidyltransferase/poly(A) polymerase
            family. This essential enzyme functions by catalyzing the addition
            of the conserved nucleotide triplet CCA to the 3' terminus of tRNA
            molecules. Mutations in this gene result in sideroblastic anemia
            with B-cell immunodeficiency, periodic fevers, and developmental
            delay. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Dec 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.83885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p26.2"
     Protein         1..434
                     /product="CCA tRNA nucleotidyltransferase 1, mitochondrial
                     isoform 1"
                     /EC_number="2.7.7.72"
                     /note="mitochondrial CCA-adding
                     tRNA-nucleotidyltransferase; tRNA nucleotidyl transferase,
                     CCA-adding, 1; tRNA-nucleotidyltransferase 1,
                     mitochondrial; CCA tRNA nucleotidyltransferase 1,
                     mitochondrial; mt CCA-adding enzyme; mt tRNA
                     CCA-diphosphorylase; mt tRNA adenylyltransferase; mt tRNA
                     CCA-pyrophosphorylase; tRNA CCA nucleotidyl transferase 1;
                     ATP(CTP):tRNA nucleotidyltransferase"
                     /calculated_mol_wt=44922
     transit_peptide 1..41
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=5224
     mat_peptide     42..434
                     /product="CCA tRNA nucleotidyltransferase 1,
                     mitochondrial. /id=PRO_0000004782"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96Q11.2)"
                     /calculated_mol_wt=44922
     Region          43..428
                     /region_name="PcnB"
                     /note="tRNA nucleotidyltransferase/poly(A) polymerase
                     [Translation, ribosomal structure and biogenesis];
                     COG0617"
                     /db_xref="CDD:440382"
     Site            152
                     /site_type="other"
                     /note="May assist in discriminating ATP from CTP.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB1; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            193
                     /site_type="other"
                     /note="Involved in nucleotide selection.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            400
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     Site            402
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96Q11.2)"
     CDS             1..434
                     /gene="TRNT1"
                     /gene_synonym="CCA1; CGI-47; MtCCA; RPEM; SIFD"
                     /coded_by="NM_001367321.1:79..1383"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2561.2"
                     /db_xref="GeneID:51095"
                     /db_xref="HGNC:HGNC:17341"
                     /db_xref="MIM:612907"
ORIGIN      
        1 mlrclyhwhr pvlnrrwsrl clpkqylftm klqspefqsl fteglkslte lfvkenhelr
       61 iaggavrdll ngvkpqdidf attatptqmk emfqsagirm innrgekhgt itarlheenf
      121 eittlridvt tdgrhaevef ttdwqkdaer rdltinsmfl gfdgtlfdyf ngyedlknkk
      181 vrfvghakqr iqedylrilr yfrfygrivd kpgdhdpetl eaiaenakgl agisgeriwv
      241 elkkilvgnh vnhlihliyd ldvapyiglp anasleefdk vsknvdgfsp kpvtllaslf
      301 kvqddvtkld lrlkiakeek nlglfivknr kdlikatdss dplkpyqdfi idsrepdatt
      361 rvcellkyqg ehcllkemqq wsippfpvsg hdirkvgiss gkeigallqq lreqwkksgy
      421 qmekdellsy ikkt
//
LOCUS       NP_998772                242 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein axonemal assembly factor 19 isoform 1 [Homo sapiens].
ACCESSION   NP_998772
VERSION     NP_998772.1
DBSOURCE    REFSEQ: accession NM_213607.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Zubair,M., Khan,R., Ma,A., Hameed,U., Khan,M., Abbas,T., Ahmad,R.,
            Zhou,J.T., Shah,W., Hussain,A., Ahmed,N., Khan,I., Khan,K.,
            Zhang,Y.W., Zhang,H., Wu,L.M. and Shi,Q.H.
  TITLE     A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms
  JOURNAL   Asian J Androl 24 (3), 255-259 (2022)
   PUBMED   35259782
  REMARK    GeneRIF: A recurrent homozygous missense mutation in CCDC103 causes
            asthenoteratozoospermia due to disorganized dynein arms.
REFERENCE   3  (residues 1 to 242)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 242)
  AUTHORS   King,S.M. and Patel-King,R.S.
  TITLE     The outer dynein arm assembly factor CCDC103 forms molecular
            scaffolds through multiple self-interaction sites
  JOURNAL   Cytoskeleton (Hoboken) 77 (1-2), 25-35 (2020)
   PUBMED   31858719
  REMARK    GeneRIF: The outer dynein arm assembly factor CCDC103 forms
            molecular scaffolds through multiple self-interaction sites.
REFERENCE   5  (residues 1 to 242)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 242)
  AUTHORS   Shoemark,A., Moya,E., Hirst,R.A., Patel,M.P., Robson,E.A.,
            Hayward,J., Scully,J., Fassad,M.R., Lamb,W., Schmidts,M., Dixon,M.,
            Patel-King,R.S., Rogers,A.V., Rutman,A., Jackson,C.L., Goggin,P.,
            Rubbo,B., Ollosson,S., Carr,S., Walker,W., Adler,B.,
            Loebinger,M.R., Wilson,R., Bush,A., Williams,H., Boustred,C.,
            Jenkins,L., Sheridan,E., Chung,E.M.K., Watson,C.M., Cullup,T.,
            Lucas,J.S., Kenia,P., O'Callaghan,C., King,S.M., Hogg,C. and
            Mitchison,H.M.
  TITLE     High prevalence of CCDC103 p.His154Pro mutation causing primary
            ciliary dyskinesia disrupts protein oligomerisation and is
            associated with normal diagnostic investigations
  JOURNAL   Thorax 73 (2), 157-166 (2018)
   PUBMED   28790179
  REMARK    GeneRIF: The CCDC103 p.His154Pro mutation is more prevalent than
            previously thought in the South Asian community in the UK and
            causes primary ciliary dyskinesia that can be difficult to diagnose
            using pathology-based clinical tests.
REFERENCE   7  (residues 1 to 242)
  AUTHORS   Casey,J.P., Goggin,P., McDaid,J., White,M., Ennis,S., Betts,D.R.,
            Lucas,J.S., Elnazir,B. and Lynch,S.A.
  TITLE     A case report of primary ciliary dyskinesia, laterality defects and
            developmental delay caused by the co-existence of a single gene and
            chromosome disorder
  JOURNAL   BMC Med Genet 16, 45 (2015)
   PUBMED   26123568
  REMARK    GeneRIF: A variable and complex phenotype caused by the
            co-inheritance of a single gene mutation in CCDC103 and a
            microduplication at 17q12, both on chromosome 17.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 242)
  AUTHORS   Tarkar,A., Loges,N.T., Slagle,C.E., Francis,R., Dougherty,G.W.,
            Tamayo,J.V., Shook,B., Cantino,M., Schwartz,D., Jahnke,C.,
            Olbrich,H., Werner,C., Raidt,J., Pennekamp,P., Abouhamed,M.,
            Hjeij,R., Kohler,G., Griese,M., Li,Y., Lemke,K., Klena,N., Liu,X.,
            Gabriel,G., Tobita,K., Jaspers,M., Morgan,L.C., Shapiro,A.J.,
            Letteboer,S.J., Mans,D.A., Carson,J.L., Leigh,M.W., Wolf,W.E.,
            Chen,S., Lucas,J.S., Onoufriadis,A., Plagnol,V., Schmidts,M.,
            Boldt,K., Roepman,R., Zariwala,M.A., Lo,C.W., Mitchison,H.M.,
            Knowles,M.R., Burdine,R.D., Loturco,J.J. and Omran,H.
  CONSRTM   UK10K
  TITLE     DYX1C1 is required for axonemal dynein assembly and ciliary
            motility
  JOURNAL   Nat Genet 45 (9), 995-1003 (2013)
   PUBMED   23872636
REFERENCE   9  (residues 1 to 242)
  AUTHORS   Panizzi,J.R., Becker-Heck,A., Castleman,V.H., Al-Mutairi,D.A.,
            Liu,Y., Loges,N.T., Pathak,N., Austin-Tse,C., Sheridan,E.,
            Schmidts,M., Olbrich,H., Werner,C., Haffner,K., Hellman,N.,
            Chodhari,R., Gupta,A., Kramer-Zucker,A., Olale,F., Burdine,R.D.,
            Schier,A.F., O'Callaghan,C., Chung,E.M., Reinhardt,R.,
            Mitchison,H.M., King,S.M., Omran,H. and Drummond,I.A.
  TITLE     CCDC103 mutations cause primary ciliary dyskinesia by disrupting
            assembly of ciliary dynein arms
  JOURNAL   Nat Genet 44 (6), 714-719 (2012)
   PUBMED   22581229
  REMARK    GeneRIF: These results identify Ccdc103 as a dynein arm attachment
            factor that causes primary ciliary dyskinesia when mutated.
            Publication Status: Online-Only
REFERENCE   10 (residues 1 to 242)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA185416.1, AK023156.1,
            AK289760.1, AC015936.14 and BQ448043.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023156.1, SRR1660809.191446.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000417826.3/ ENSP00000391692.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..242
                     /product="dynein axonemal assembly factor 19 isoform 1"
                     /note="coiled-coil domain-containing protein 103;
                     coiled-coil domain containing 103"
                     /calculated_mol_wt=27032
     Region          7..74
                     /region_name="Dynein_attach_N"
                     /note="Dynein attachment factor N-terminus; pfam15867"
                     /db_xref="CDD:464912"
     Region          99..188
                     /region_name="RPAP3_C"
                     /note="Potential Monad-binding region of RPAP3; pfam13877"
                     /db_xref="CDD:464012"
     CDS             1..242
                     /gene="DNAAF19"
                     /gene_synonym="CCDC103; CILD17; PR46b; SMH"
                     /coded_by="NM_213607.3:141..869"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11490.1"
                     /db_xref="GeneID:388389"
                     /db_xref="HGNC:HGNC:32700"
                     /db_xref="MIM:614677"
ORIGIN      
        1 merndiinfk alekelqaal tadekykren aaklraveqr vasyeefrgi vlashlkple
       61 rkdkmggkrt vpwnchtiqg rtfqdvatei spekaplqpe tsadfyrdwr rhlpsgpery
      121 qallqlggpr lgclfqtdvg fgllgellva ladhvgpadr aavlgilcsl astgrftlnl
      181 sllsraeres ckglfqklqa mgnprsvkeg lsweeqglee qsgglqeeer llqellelyq
      241 vd
//
LOCUS       NP_001164563             230 aa            linear   PRI 20-NOV-2025
DEFINITION  claudin-2 [Homo sapiens].
ACCESSION   NP_001164563
VERSION     NP_001164563.1
DBSOURCE    REFSEQ: accession NM_001171092.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 230)
  AUTHORS   Eguchi,H., Yu,Y., Yoshino,Y., Hara,H., Tanaka,H. and Ikari,A.
  TITLE     Plasma-activated medium ameliorates the chemoresistance of human
            lung adenocarcinoma cells mediated via downregulation of claudin-2
            expression
  JOURNAL   Arch Biochem Biophys 751, 109846 (2024)
   PUBMED   38056686
  REMARK    GeneRIF: Plasma-activated medium ameliorates the chemoresistance of
            human lung adenocarcinoma cells mediated via downregulation of
            claudin-2 expression.
REFERENCE   2  (residues 1 to 230)
  AUTHORS   Telgenhoff,D.
  TITLE     Claudin-2 in hyperproliferative migrating keratinocytes and
            migration inhibition via siRNA knockdown
  JOURNAL   Anat Histol Embryol 52 (5), 723-731 (2023)
   PUBMED   37147871
  REMARK    GeneRIF: Claudin-2 in hyperproliferative migrating keratinocytes
            and migration inhibition via siRNA knockdown.
REFERENCE   3  (residues 1 to 230)
  AUTHORS   Ahmad,R., Kumar,B., Tamang,R.L., Talmon,G.A., Dhawan,P. and
            Singh,A.B.
  TITLE     P62/SQSTM1 binds with claudin-2 to target for selective autophagy
            in stressed intestinal epithelium
  JOURNAL   Commun Biol 6 (1), 740 (2023)
   PUBMED   37460613
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 230)
  AUTHORS   Arai,W., Konno,T., Kohno,T., Kodera,Y., Tsujiwaki,M., Shindo,Y.,
            Chiba,H., Miyajima,M., Sakuma,Y., Watanabe,A. and Kojima,T.
  TITLE     Downregulation of angulin-1/LSR induces malignancy via upregulation
            of EGF-dependent claudin-2 and TGF-beta-dependent cell metabolism
            in human lung adenocarcinoma A549 cells
  JOURNAL   Oncotarget 14, 261-275 (2023)
   PUBMED   36961882
  REMARK    GeneRIF: Downregulation of angulin-1/LSR induces malignancy via
            upregulation of EGF-dependent claudin-2 and TGF-beta-dependent cell
            metabolism in human lung adenocarcinoma A549 cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 230)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 230)
  AUTHORS   Kniesel,U. and Wolburg,H.
  TITLE     Tight junctions of the blood-brain barrier
  JOURNAL   Cell Mol Neurobiol 20 (1), 57-76 (2000)
   PUBMED   10690502
  REMARK    Review article
REFERENCE   7  (residues 1 to 230)
  AUTHORS   Itoh,M., Furuse,M., Morita,K., Kubota,K., Saitou,M. and Tsukita,S.
  TITLE     Direct binding of three tight junction-associated MAGUKs, ZO-1,
            ZO-2, and ZO-3, with the COOH termini of claudins
  JOURNAL   J Cell Biol 147 (6), 1351-1363 (1999)
   PUBMED   10601346
REFERENCE   8  (residues 1 to 230)
  AUTHORS   Morita,K., Furuse,M., Fujimoto,K. and Tsukita,S.
  TITLE     Claudin multigene family encoding four-transmembrane domain protein
            components of tight junction strands
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 511-516 (1999)
   PUBMED   9892664
REFERENCE   9  (residues 1 to 230)
  AUTHORS   Furuse,M., Fujita,K., Hiiragi,T., Fujimoto,K. and Tsukita,S.
  TITLE     Claudin-1 and -2: novel integral membrane proteins localizing at
            tight junctions with no sequence similarity to occludin
  JOURNAL   J Cell Biol 141 (7), 1539-1550 (1998)
   PUBMED   9647647
REFERENCE   10 (residues 1 to 230)
  AUTHORS   Shelton,C., LaRusch,J. and Whitcomb,D.C.
  TITLE     Pancreatitis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24624459
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF177340.1, AK075405.1 and
            AA973123.1.
            
            Summary: This gene product belongs to the claudin protein family
            whose members have been identified as major integral membrane
            proteins localized exclusively at tight junctions. Claudins are
            expressed in an organ-specific manner and regulate tissue-specific
            physiologic properties of tight junctions. This protein is
            expressed in the intestine. Alternatively spliced transcript
            variants with different 5' untranslated region have been found for
            this gene.[provided by RefSeq, Jan 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF177340.1, DA018143.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..230
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq22.3"
     Protein         1..230
                     /product="claudin-2"
                     /note="SP82"
                     /calculated_mol_wt=24418
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     Region          23..181
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            65
                     /site_type="other"
                     /note="Paracellular cation selectivity.
                     /evidence=ECO:0000250|UniProtKB:O88552; propagated from
                     UniProtKB/Swiss-Prot (P57739.1)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     Site            117..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     Region          205..230
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88552; propagated from
                     UniProtKB/Swiss-Prot (P57739.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88552; propagated from
                     UniProtKB/Swiss-Prot (P57739.1)"
     Region          229..230
                     /region_name="Interactions with TJP1, TJP2 and TJP3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P57739.1)"
     CDS             1..230
                     /gene="CLDN2"
                     /gene_synonym="claudin-2; OAZON"
                     /coded_by="NM_001171092.1:520..1212"
                     /db_xref="CCDS:CCDS14524.1"
                     /db_xref="GeneID:9075"
                     /db_xref="HGNC:HGNC:2041"
                     /db_xref="MIM:300520"
ORIGIN      
        1 maslglqlvg yilgllgllg tlvamllpsw ktssyvgasi vtavgfskgl wmecathstg
       61 itqcdiystl lglpadiqaa qammvtssai sslaciisvv gmrctvfcqe srakdrvava
      121 ggvffilggl lgfipvawnl hgilrdfysp lvpdsmkfei gealylgiis slfsliagii
      181 lcfscssqrn rsnyydayqa qplatrsspr pgqppkvkse fnsysltgyv
//
LOCUS       NP_001269384             514 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-2 isoform 2 precursor
            [Homo sapiens].
ACCESSION   NP_001269384 XP_005273453
VERSION     NP_001269384.1
DBSOURCE    REFSEQ: accession NM_001282455.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 514)
  AUTHORS   Demontis,D., Rajagopal,V.M., Thorgeirsson,T.E., Als,T.D., Grove,J.,
            Leppala,K., Gudbjartsson,D.F., Pallesen,J., Hjorthoj,C.,
            Reginsson,G.W., Tyrfingsson,T., Runarsdottir,V., Qvist,P.,
            Christensen,J.H., Bybjerg-Grauholm,J., Baekvad-Hansen,M.,
            Huckins,L.M., Stahl,E.A., Timmermann,A., Agerbo,E., Hougaard,D.M.,
            Werge,T., Mors,O., Mortensen,P.B., Nordentoft,M., Daly,M.J.,
            Stefansson,H., Stefansson,K., Nyegaard,M. and Borglum,A.D.
  TITLE     Genome-wide association study implicates CHRNA2 in cannabis use
            disorder
  JOURNAL   Nat Neurosci 22 (7), 1066-1074 (2019)
   PUBMED   31209380
  REMARK    GeneRIF: The index variant (rs56372821) is a strong expression
            quantitative trait locus for CHRNA2; analyses of the genetically
            regulated gene expression identified a significant association of
            CHRNA2 expression with cannabis use disorder (CUD) in brain tissue.
            At the polygenic level, analyses revealed a significant decrease in
            the risk of CUD with increased load of variants associated with
            cognitive performance.
REFERENCE   2  (residues 1 to 514)
  AUTHORS   Wang,M., Liu,D., Schwender,H., Wang,H., Wang,P., Zhou,Z., Li,J.,
            Wu,T., Zhu,H. and Beaty,T.H.
  TITLE     Evaluating the effect of nicotinic cholinergic receptor genes on
            the risk of nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Oral Dis 24 (6), 1068-1072 (2018)
   PUBMED   29688589
  REMARK    GeneRIF: In our analysis, we found one pair of SNPs in CHRNA1 and
            CHRNA7, plus one pair of SNPs in CHRNA2 and CHRNA3 reached
            corrected significance in tests for GxG interaction. Our study
            suggested evidence of interactions between CHRNs in controlling the
            risk of NSCL/P.
REFERENCE   3  (residues 1 to 514)
  AUTHORS   Jun,H., Yu,H., Gong,J., Jiang,J., Qiao,X., Perkey,E., Kim,D.I.,
            Emont,M.P., Zestos,A.G., Cho,J.S., Liu,J., Kennedy,R.T.,
            Maillard,I., Xu,X.Z.S. and Wu,J.
  TITLE     An immune-beige adipocyte communication via nicotinic acetylcholine
            receptor signaling
  JOURNAL   Nat Med 24 (6), 814-822 (2018)
   PUBMED   29785025
  REMARK    GeneRIF: These results reveal a beige-selective immune-adipose
            interaction mediated through CHRNA2 and identify a novel function
            of nicotinic acetylcholine receptors in energy metabolism.
REFERENCE   4  (residues 1 to 514)
  AUTHORS   Kouvatsos,N., Giastas,P., Chroni-Tzartou,D., Poulopoulou,C. and
            Tzartos,S.J.
  TITLE     Crystal structure of a human neuronal nAChR extracellular domain in
            pentameric assembly: Ligand-bound alpha2 homopentamer
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9635-9640 (2016)
   PUBMED   27493220
  REMARK    GeneRIF: A crystal structure of a human neuronal CHRNA2
            extracellular domain in pentameric assembly has been reported.
REFERENCE   5  (residues 1 to 514)
  AUTHORS   Trivisano,M., Terracciano,A., Milano,T., Cappelletti,S.,
            Pietrafusa,N., Bertini,E.S., Vigevano,F. and Specchio,N.
  TITLE     Mutation of CHRNA2 in a family with benign familial infantile
            seizures: Potential role of nicotinic acetylcholine receptor in
            various phenotypes of epilepsy
  JOURNAL   Epilepsia 56 (5), e53-e57 (2015)
   PUBMED   25847220
  REMARK    GeneRIF: a heterozygous single-nucleotide substitution in CHRNA2
            gene (c.1126 C>T; p. Arg376Trp) in subjects with benign familial
            infantile seizures
REFERENCE   6  (residues 1 to 514)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
REFERENCE   7  (residues 1 to 514)
  AUTHORS   Garcia-Colunga,J. and Miledi,R.
  TITLE     Effects of serotonergic agents on neuronal nicotinic acetylcholine
            receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (7), 2919-2923 (1995)
   PUBMED   7708749
REFERENCE   8  (residues 1 to 514)
  AUTHORS   Wood,S., Schertzer,M. and Yaremko,M.L.
  TITLE     Identification of the human neuronal nicotinic cholinergic alpha 2
            receptor locus, (CHRNA2), within an 8p21 mapped locus, by sequence
            homology with rat DNA
  JOURNAL   Somat Cell Mol Genet 21 (2), 147-150 (1995)
   PUBMED   7570187
REFERENCE   9  (residues 1 to 514)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
REFERENCE   10 (residues 1 to 514)
  AUTHORS   Anand,R. and Lindstrom,J.
  TITLE     Chromosomal localization of seven neuronal nicotinic acetylcholine
            receptor subunit genes in humans
  JOURNAL   Genomics 13 (4), 962-967 (1992)
   PUBMED   1505988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF311103.5, AK296348.1 and
            AW292180.1.
            
            On Sep 7, 2013 this sequence version replaced XP_005273453.1.
            
            Summary: Nicotinic acetylcholine receptors (nAChRs) are
            ligand-gated ion channels formed by a pentameric arrangement of
            alpha and beta subunits to create distinct muscle and neuronal
            receptors. Neuronal receptors are found throughout the peripheral
            and central nervous system where they are involved in fast synaptic
            transmission. This gene encodes an alpha subunit that is widely
            expressed in the brain. The proposed structure for nAChR subunits
            is a conserved N-terminal extracellular domain followed by three
            conserved transmembrane domains, a variable cytoplasmic loop, a
            fourth conserved transmembrane domain, and a short C-terminal
            extracellular region. Mutations in this gene cause autosomal
            dominant nocturnal frontal lobe epilepsy type 4. Single nucleotide
            polymorphisms (SNPs) in this gene have been associated with
            nicotine dependence. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.90046.1, AK296348.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..514
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..514
                     /product="neuronal acetylcholine receptor subunit alpha-2
                     isoform 2 precursor"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     2 (neuronal); cholinergic receptor, nicotinic alpha 2;
                     neuronal acetylcholine receptor subunit alpha-2;
                     acetylcholine receptor, nicotinic, alpha 2 (neuronal);
                     cholinergic receptor, nicotinic, alpha 2 (neuronal);
                     nicotinic acetylcholine receptor subunit alpha-2"
                     /calculated_mol_wt=55336
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2822
     Region          <28..>75
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          57..507
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          59..250
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Site            order(87..88,95,117,119,128..129,131,133..134,145..147,
                     149,159,161,163,167,189,249)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349787"
     CDS             1..514
                     /gene="CHRNA2"
                     /coded_by="NM_001282455.2:575..2119"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS64856.1"
                     /db_xref="GeneID:1135"
                     /db_xref="HGNC:HGNC:1956"
                     /db_xref="MIM:118502"
ORIGIN      
        1 mgpscpvfls ftklslwwll ltpaggeeak rppprapgdp lsspsptalp qggshteted
       61 rlfkhlfrgy nrwarpvpnt sdvdeknqmm ttnvwlkqew sdyklrwnpt dfgnitslrv
      121 psemiwipdi vlynnadgef avthmtkahl fstgtvhwvp paiyksscsi dvtffpfdqq
      181 nckmkfgswt ydkakidleq meqtvdlkdy wesgewaivn atgtynskky dccaeiypdv
      241 tyafvirrlp lfytinliip clliscltvl vfylpsdcge kitlcisvll sltvflllit
      301 eiipstslvi pligeyllft mifvtlsivi tvfvlnvhhr spsthtmphw vrgallgcvp
      361 rwllmnrppp pvelchplrl klspsyhwle snvdaeerev vveeedrwac aghvapsvgt
      421 lcshghlhsg asgpkaeall qegelllsph mqkalegvhy iadhlrseda dssvkedwky
      481 vamvidrifl wlfiivcflg tiglflppfl agmi
//
LOCUS       NP_997239                243 aa            linear   PRI 20-NOV-2025
DEFINITION  UPF0688 protein C1orf174 [Homo sapiens].
ACCESSION   NP_997239
VERSION     NP_997239.2
DBSOURCE    REFSEQ: accession NM_207356.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Ingham,N.J., Rook,V., Di Domenico,F., James,E., Lewis,M.A.,
            Girotto,G., Buniello,A. and Steel,K.P.
  TITLE     Functional analysis of candidate genes from genome-wide association
            studies of hearing
  JOURNAL   Hear Res 387, 107879 (2020)
   PUBMED   31927188
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Lee,O.H., Kim,H., He,Q., Baek,H.J., Yang,D., Chen,L.Y., Liang,J.,
            Chae,H.K., Safari,A., Liu,D. and Songyang,Z.
  TITLE     Genome-wide YFP fluorescence complementation screen identifies new
            regulators for telomere signaling in human cells
  JOURNAL   Mol Cell Proteomics 10 (2), M110.001628 (2011)
   PUBMED   21044950
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC067302.1 and AL691523.6.
            
            On Mar 6, 2009 this sequence version replaced NP_997239.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067302.1, SRR5189658.90011.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361605.4/ ENSP00000355306.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.32"
     Protein         1..243
                     /product="UPF0688 protein C1orf174"
                     /note="RP13-531C17.2"
                     /calculated_mol_wt=25846
     Region          6..231
                     /region_name="UPF0688"
                     /note="UPF0688 family; pfam15772"
                     /db_xref="CDD:464860"
     Region          78..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL3.2)"
     Region          132..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYL3.2)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL3.2)"
     Site            189
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYL3.2)"
     CDS             1..243
                     /gene="C1orf174"
                     /coded_by="NM_207356.3:87..818"
                     /db_xref="CCDS:CCDS53.1"
                     /db_xref="GeneID:339448"
                     /db_xref="HGNC:HGNC:27915"
ORIGIN      
        1 mrsrkltgav rssarlkars csaarlasaq evagstsakt acltssshka tdtrtskkfk
       61 cdkghlvkse lqklvpknds aslpkvtpet pcenefaegs allpgseagv svqqgaaslp
      121 lggcrvvsds rlaktrdgls vpkhsagsga eesnssstvq kqnepglqte dvqkpplqmd
      181 nsvfldddsn qpmpvsrffg nvelmqdlpp assscpsmsr refrkmhfra kddddddddd
      241 aem
//
LOCUS       NP_004505                660 aa            linear   PRI 20-NOV-2025
DEFINITION  forkhead box protein K2 [Homo sapiens].
ACCESSION   NP_004505 XP_947798 XP_951372 XP_951373 XP_951374
VERSION     NP_004505.2
DBSOURCE    REFSEQ: accession NM_004514.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Yu,Y., Cao,W.M., Cheng,F., Shi,Z., Han,L., Yi,J., da Silva,E.M.,
            Dopeso,H., Chen,H., Yang,J., Wang,X., Zhang,C. and Zhang,H.
  TITLE     FOXK2 amplification promotes breast cancer development and
            chemoresistance
  JOURNAL   Cancer Lett 597, 217074 (2024)
   PUBMED   38901667
  REMARK    GeneRIF: FOXK2 amplification promotes breast cancer development and
            chemoresistance.
REFERENCE   3  (residues 1 to 660)
  AUTHORS   El-Mergawy,R., Chafin,L., Ovando-Ricardez,J.A., Rosas,L., Tsai,M.,
            Rojas,M., Mora,A.L. and Mallampalli,R.K.
  TITLE     FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for ubiquitin
            mediated degradation modulates mitochondrial respiration
  JOURNAL   J Biol Chem 300 (6), 107359 (2024)
   PUBMED   38735474
  REMARK    GeneRIF: FOXK2 targeting by the SCF-E3 ligase subunit FBXO24 for
            ubiquitin mediated degradation modulates mitochondrial respiration.
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Liu,X., Tang,N., Liu,Y., Fu,J., Zhao,Y., Wang,H., Wang,H. and Hu,Z.
  TITLE     FOXK2 regulates PFKFB3 in promoting glycolysis and tumorigenesis in
            multiple myeloma
  JOURNAL   Leuk Res 132, 107343 (2023)
   PUBMED   37356282
  REMARK    GeneRIF: FOXK2 regulates PFKFB3 in promoting glycolysis and
            tumorigenesis in multiple myeloma.
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Zheng,J., Yan,X., Lu,T., Song,W., Li,Y., Liang,J., Zhang,J.,
            Cai,J., Sui,X., Xiao,J., Chen,H., Chen,G., Zhang,Q., Liu,Y.,
            Yang,Y., Zheng,K. and Pan,Z.
  TITLE     CircFOXK2 promotes hepatocellular carcinoma progression and leads
            to a poor clinical prognosis via regulating the Warburg effect
  JOURNAL   J Exp Clin Cancer Res 42 (1), 63 (2023)
   PUBMED   36922872
  REMARK    GeneRIF: CircFOXK2 promotes hepatocellular carcinoma progression
            and leads to a poor clinical prognosis via regulating the Warburg
            effect.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Liu,P.P., Chen,Y.C., Li,C., Hsieh,Y.H., Chen,S.W., Chen,S.H.,
            Jeng,W.Y. and Chuang,W.J.
  TITLE     Solution structure of the DNA-binding domain of interleukin
            enhancer binding factor 1 (FOXK1a)
  JOURNAL   Proteins 49 (4), 543-553 (2002)
   PUBMED   12402362
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Nirula,A., Moore,D.J. and Gaynor,R.B.
  TITLE     Constitutive binding of the transcription factor interleukin-2
            (IL-2) enhancer binding factor to the IL-2 promoter
  JOURNAL   J Biol Chem 272 (12), 7736-7745 (1997)
   PUBMED   9065434
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Li,C., Lusis,A.J., Sparkes,R., Nirula,A. and Gaynor,R.
  TITLE     Characterization and chromosomal mapping of the gene encoding the
            cellular DNA binding protein ILF
  JOURNAL   Genomics 13 (3), 665-671 (1992)
   PUBMED   1339390
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Li,C., Lai,C.F., Sigman,D.S. and Gaynor,R.B.
  TITLE     Cloning of a cellular factor, interleukin binding factor, that
            binds to NFAT-like motifs in the human immunodeficiency virus long
            terminal repeat
  JOURNAL   Proc Natl Acad Sci U S A 88 (17), 7739-7743 (1991)
   PUBMED   1909027
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Durand,D.B., Shaw,J.P., Bush,M.R., Replogle,R.E., Belagaje,R. and
            Crabtree,G.R.
  TITLE     Characterization of antigen receptor response elements within the
            interleukin-2 enhancer
  JOURNAL   Mol Cell Biol 8 (4), 1715-1724 (1988)
   PUBMED   3260003
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124287.10, U58196.1 and
            AC124283.11.
            
            On Jun 10, 2003 this sequence version replaced NP_004505.1.
            
            Summary: The protein encoded by this gene contains a fork head DNA
            binding domain. This protein can bind to the purine-rich motifs of
            the HIV long terminal repeat (LTR), and to the similar purine-rich
            motif in the interleukin 2 (IL2) promoter. It may be involved in
            the regulation of viral and cellular promoter elements. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.107086.1,
                                           SRR1803613.198923.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335255.10/ ENSP00000335677.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..660
                     /product="forkhead box protein K2"
                     /note="cellular transcription factor ILF-1; FOXK1;
                     interleukin enhancer-binding factor 1; G/T-mismatch
                     specific binding protein"
                     /calculated_mol_wt=68931
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Region          35..157
                     /region_name="FHA_FOXK2"
                     /note="forkhead associated (FHA) domain found in forkhead
                     box protein K2 (FOXK2) and similar proteins; cd22723"
                     /db_xref="CDD:438775"
     Site            order(57..58,76..77,79,117,119..120)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438775"
     Region          85..104
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Region          129..171
                     /region_name="Required for interaction with DVL2 and
                     SUDS3. /evidence=ECO:0000269|PubMed:25805136"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            144
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Region          <180..577
                     /region_name="COG5025"
                     /note="Transcription factor of the Forkhead/HNF3 family
                     [Transcription]"
                     /db_xref="CDD:227358"
     Region          203..260
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Region          256..353
                     /region_name="FH_FOXK2"
                     /note="Forkhead (FH) domain found in Forkhead box protein
                     K2 (FOXK2) and similar proteins; cd20055"
                     /db_xref="CDD:410829"
     Site            order(258,261..263,281..282,285,300,304..305,307..308,
                     311..312,318,326,328..330,332,350,353)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410829"
     Region          300..318
                     /region_name="DNA-binding, major groove.
                     /evidence=ECO:0000269|PubMed:16624804"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Region          328..332
                     /region_name="DNA-binding, minor groove.
                     /evidence=ECO:0000269|PubMed:16624804"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Region          348..353
                     /region_name="DNA-binding, minor groove.
                     /evidence=ECO:0000269|PubMed:16624804"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Region          359..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:20810654; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            424
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and CDK2.
                     /evidence=ECO:0000269|PubMed:20810654,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UCQ1; propagated from
                     UniProtKB/Swiss-Prot (Q01167.3)"
     Region          610..632
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01167.3)"
     CDS             1..660
                     /gene="FOXK2"
                     /gene_synonym="ILF; ILF-1; ILF1; nGTBP"
                     /coded_by="NM_004514.4:158..2140"
                     /db_xref="CCDS:CCDS11813.1"
                     /db_xref="GeneID:3607"
                     /db_xref="HGNC:HGNC:6036"
                     /db_xref="MIM:147685"
ORIGIN      
        1 maaaaaalsg agtppaggga ggggaggggs ppggwavarl egrefeylmk krsvtigrns
       61 sqgsvdvsmg hssfisrrhl eiftppgggg hggaapelpp aqprpdaggd fylrclgkng
      121 vfvdgvfqrr gapplqlprv ctfrfpstni kitftalsse krekqeases pvkavqphis
      181 pltinipdtm ahlisplpsp tgtisaansc pssprgagss gykvgrvmps dlnlmadnsq
      241 penekeasgg dspkddskpp ysyaqlivqa itmapdkqlt lngiythitk nypyyrtadk
      301 gwqnsirhnl slnryfikvp rsqeepgkgs fwridpases klieqafrkr rprgvpcfrt
      361 plgplssrsa paspnhagvl sahssgaqtp eslsregspa plepepgaaq pklaviqear
      421 faqsapgspl ssqpvlitvq rqlpqaikpv tytvatpvtt stsqppvvqt vhvvhqipav
      481 svtsvaglap antytvsgqa vvtpaavlap pkaeaqengd hrevkvkvep ipaighatlg
      541 tasriiqtaq ttpvqtvtiv qqaplgqhql piktvtqngt hvasvptavh gqvnnaaasp
      601 lhmlathasa saslptkrhn gdqpeqpelk riktedgegi vialsvdtpp aavrekgvqn
//
LOCUS       NP_001268364             410 aa            linear   PRI 20-NOV-2025
DEFINITION  dual specificity mitogen-activated protein kinase kinase 4 isoform
            2 [Homo sapiens].
ACCESSION   NP_001268364
VERSION     NP_001268364.1
DBSOURCE    REFSEQ: accession NM_001281435.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 410)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 410)
  AUTHORS   Pan,C., Su,Z., Xie,H., Ning,Y., Li,S. and Xiao,H.
  TITLE     Hsa_circ_0081069 facilitates tongue squamous cell carcinoma
            progression by modulating MAP2K4 expression via miR-634
  JOURNAL   Odontology 111 (2), 474-486 (2023)
   PUBMED   36181561
  REMARK    GeneRIF: Hsa_circ_0081069 facilitates tongue squamous cell
            carcinoma progression by modulating MAP2K4 expression via miR-634.
REFERENCE   3  (residues 1 to 410)
  AUTHORS   Wang,B., Yang,S., Jia,Y., Yang,J., Du,K., Luo,Y., Li,Y., Wang,Z.,
            Liu,Y. and Zhu,B.
  TITLE     PCAT19 Regulates the Proliferation and Apoptosis of Lung Cancer
            Cells by Inhibiting miR-25-3p via Targeting the MAP2K4 Signal Axis
  JOURNAL   Dis Markers 2022, 2442094 (2022)
   PUBMED   35615401
  REMARK    GeneRIF: PCAT19 Regulates the Proliferation and Apoptosis of Lung
            Cancer Cells by Inhibiting miR-25-3p via Targeting the MAP2K4
            Signal Axis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 410)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 410)
  AUTHORS   Kragelj,J., Orand,T., Delaforge,E., Tengo,L., Blackledge,M.,
            Palencia,A. and Jensen,M.R.
  TITLE     Enthalpy-Entropy Compensation in the Promiscuous Interaction of an
            Intrinsically Disordered Protein with Homologous Protein Partners
  JOURNAL   Biomolecules 11 (8), 1204 (2021)
   PUBMED   34439869
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 410)
  AUTHORS   Gale,N.W., Holland,S.J., Valenzuela,D.M., Flenniken,A., Pan,L.,
            Ryan,T.E., Henkemeyer,M., Strebhardt,K., Hirai,H., Wilkinson,D.G.,
            Pawson,T., Davis,S. and Yancopoulos,G.D.
  TITLE     Eph receptors and ligands comprise two major specificity subclasses
            and are reciprocally compartmentalized during embryogenesis
  JOURNAL   Neuron 17 (1), 9-19 (1996)
   PUBMED   8755474
REFERENCE   7  (residues 1 to 410)
  AUTHORS   Salmeron,A., Ahmad,T.B., Carlile,G.W., Pappin,D., Narsimhan,R.P.
            and Ley,S.C.
  TITLE     Activation of MEK-1 and SEK-1 by Tpl-2 proto-oncoprotein, a novel
            MAP kinase kinase kinase
  JOURNAL   EMBO J 15 (4), 817-826 (1996)
   PUBMED   8631303
REFERENCE   8  (residues 1 to 410)
  AUTHORS   Lin,A., Minden,A., Martinetto,H., Claret,F.X., Lange-Carter,C.,
            Mercurio,F., Johnson,G.L. and Karin,M.
  TITLE     Identification of a dual specificity kinase that activates the Jun
            kinases and p38-Mpk2
  JOURNAL   Science 268 (5208), 286-290 (1995)
   PUBMED   7716521
REFERENCE   9  (residues 1 to 410)
  AUTHORS   Derijard,B., Raingeaud,J., Barrett,T., Wu,I.H., Han,J.,
            Ulevitch,R.J. and Davis,R.J.
  TITLE     Independent human MAP-kinase signal transduction pathways defined
            by MEK and MKK isoforms
  JOURNAL   Science 267 (5198), 682-685 (1995)
   PUBMED   7839144
  REMARK    Erratum:[Science 1995 Jul 7;269(5220):17]
REFERENCE   10 (residues 1 to 410)
  AUTHORS   Yan,M., Dai,T., Deak,J.C., Kyriakis,J.M., Zon,L.I., Woodgett,J.R.
            and Templeton,D.J.
  TITLE     Activation of stress-activated protein kinase by MEKK1
            phosphorylation of its activator SEK1
  JOURNAL   Nature 372 (6508), 798-800 (1994)
   PUBMED   7997270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005410.3, AK131544.1 and
            AC005244.1.
            
            Summary: This gene encodes a member of the mitogen-activated
            protein kinase (MAPK) family. Members of this family act as an
            integration point for multiple biochemical signals and are involved
            in a wide variety of cellular processes such as proliferation,
            differentiation, transcription regulation, and development. They
            form a three-tiered signaling module composed of MAPKKKs, MAPKKs,
            and MAPKs. This protein is phosphorylated at serine and threonine
            residues by MAPKKKs and subsequently phosphorylates downstream MAPK
            targets at threonine and tyrosine residues. A similar protein in
            mouse has been reported to play a role in liver organogenesis. A
            pseudogene of this gene is located on the long arm of chromosome X.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) contains an alternate in-frame
            exon in the 5' coding region compared to variant 1. It encodes
            isoform 2 which is longer compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.184439.1,
                                           SRR1803611.144078.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..410
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..410
                     /product="dual specificity mitogen-activated protein
                     kinase kinase 4 isoform 2"
                     /EC_number="2.7.12.2"
                     /note="dual specificity mitogen-activated protein kinase
                     kinase 4; MAP kinase kinase 4; c-Jun N-terminal kinase
                     kinase 1; SAPK/ERK kinase 1; MAPK/ERK kinase 4;
                     JNK-activated kinase 1; MEK 4; MAPKK 4; JNK-activating
                     kinase 1; stress-activated protein kinase kinase 1; c-Jun
                     NH2-terminal kinase kinase 1"
                     /calculated_mol_wt=45453
     Region          106..396
                     /region_name="PKc_MKK4"
                     /note="Catalytic domain of the dual-specificity Protein
                     Kinase, Mitogen-activated protein Kinase Kinase 4;
                     cd06616"
                     /db_xref="CDD:270790"
     Site            order(106..110,132,137,139,157,176,178..180,188)
                     /site_type="other"
                     /note="allosteric peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270790"
     Site            order(119..123,127,140,142,173,189..192,194..195,198,240,
                     242..245,247,257..258,261,274..277,279,310,319)
                     /site_type="active"
                     /db_xref="CDD:270790"
     Site            order(119..123,125,127,140,142,173,189..192,194..195,
                     197..198,242,244..245,247,258)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270790"
     Site            order(122..123,240,242..244,261,274..277,279,310,319)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270790"
     Site            257..279
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270790"
     CDS             1..410
                     /gene="MAP2K4"
                     /gene_synonym="JNKK; JNKK1; MAPKK4; MEK4; MKK4; PRKMK4;
                     SAPKK-1; SAPKK1; SEK1; SERK1; SKK1"
                     /coded_by="NM_001281435.2:11..1243"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS62095.1"
                     /db_xref="GeneID:6416"
                     /db_xref="HGNC:HGNC:6844"
                     /db_xref="MIM:601335"
ORIGIN      
        1 maapspsggg gsgggsgsgt pgpvgspapg hpavssmqgf qinfcekaqs krkalklnfa
       61 nppfkstarf tlnpnptgvq nphierlrth siessgklki speqhwdfta edlkdlgeig
      121 rgaygsvnkm vhkpsgqima vkrirstvde keqkqllmdl dvvmrssdcp yivqfygalf
      181 regdcwicme lmstsfdkfy kyvysvlddv ipeeilgkit latvkalnhl kenlkiihrd
      241 ikpsnilldr sgniklcdfg isgqlvdsia ktrdagcrpy maperidpsa srqgydvrsd
      301 vwslgitlye latgrfpypk wnsvfdqltq vvkgdppqls nseerefsps finfvnlclt
      361 kdeskrpkyk ellkhpfilm yeeravevac yvckildqmp atpsspmyvd
//
LOCUS       NP_001308517             512 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 27 [Homo sapiens].
ACCESSION   NP_001308517 XP_005263314
VERSION     NP_001308517.1
DBSOURCE    REFSEQ: accession NM_001321588.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 512)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 512)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 512)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 512)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 512)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 512)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 512)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 512)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 512)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 512)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            On Mar 26, 2016 this sequence version replaced XP_005263314.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (29) encodes isoform (27, also
            known as delta 9).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.138509.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..512
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..512
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 27"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=57699
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          359..486
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..512
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321588.2:671..2209"
                     /note="isoform 27 is encoded by transcript variant 29"
                     /db_xref="CCDS:CCDS93605.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkepq ttvihnpdgn kestessntt iededvkark
      361 qeiikvteql ieainngdfe aytkicdpgl tafepealgn lvegmdfhrf yfenalsksn
      421 kpihtiilnp hvhlvgddaa ciayirltqy mdgsgmpktm qseetrvwhr rdgkwqnvhf
      481 hrsgsptvpi kppcipngke nfsggtslwq ni
//
LOCUS       NP_680545                163 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p25-like protein [Homo sapiens].
ACCESSION   NP_680545
VERSION     NP_680545.1
DBSOURCE    REFSEQ: accession NM_148179.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 163)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 163)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 163)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 163)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 163)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   6  (residues 1 to 163)
  AUTHORS   Kim,J.M., Lee,K.H., Jeon,Y.J., Oh,J.H., Jeong,S.Y., Song,I.S.,
            Kim,J.M., Lee,D.S. and Kim,N.S.
  TITLE     Identification of genes related to Parkinson's disease using
            expressed sequence tags
  JOURNAL   DNA Res 13 (6), 275-286 (2006)
   PUBMED   17213182
REFERENCE   7  (residues 1 to 163)
  AUTHORS   Rosenblad,M.A., Lopez,M.D., Piccinelli,P. and Samuelsson,T.
  TITLE     Inventory and analysis of the protein subunits of the ribonucleases
            P and MRP provides further evidence of homology between the yeast
            and human enzymes
  JOURNAL   Nucleic Acids Res 34 (18), 5145-5156 (2006)
   PUBMED   16998185
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL528391.3, DT218980.1 and AI016726.1.
            
            Summary: This gene encodes a protein that appears to belong to a
            family of evolutionarily related proteins (DUF78), that may share
            one or more domains in common. Members of this family are small
            archaebacterial proteins with no known function. Alternative
            splicing has been observed at this locus and two variants, both
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' UTR compared to variant 1. Variants 1 and 2 encode the
            same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.348032.1,
                                           SRR7346977.456035.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..163
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..163
                     /product="ribonuclease P protein subunit p25-like protein"
                     /note="alba-like protein C9orf23; rpp25-like protein;
                     RNase P protein subunit-like p25; ribonuclease P/MRP 25kDa
                     subunit-like"
                     /calculated_mol_wt=17500
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5L8.1)"
     Region          27..89
                     /region_name="Alba"
                     /note="pfam01918"
                     /db_xref="CDD:426509"
     Region          129..163
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N5L8.1)"
     CDS             1..163
                     /gene="RPP25L"
                     /gene_synonym="bA296L22.5; C9orf23"
                     /coded_by="NM_148179.3:275..766"
                     /db_xref="CCDS:CCDS6559.1"
                     /db_xref="GeneID:138716"
                     /db_xref="HGNC:HGNC:19909"
ORIGIN      
        1 mehyrkagsv elpapspmpq lppdtlemrv rdgskirnll glalgrlegg sarhvvfsgs
       61 graagkavsc aeivkrrvpg lhqltklrfl qtedswvpas pdtgldpltv rrhvpavwvl
      121 lsrdpldpne cgyqppgapp glgsmpsssc gprsrrrard trs
//
LOCUS       NP_000960                297 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL18 [Homo sapiens].
ACCESSION   NP_000960
VERSION     NP_000960.2
DBSOURCE    REFSEQ: accession NM_000969.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 297)
  AUTHORS   Hu,X., Li,F., Zhou,Y., Gan,H., Wang,T., Li,L., Long,H., Li,B. and
            Pang,P.
  TITLE     DDX24 promotes metastasis by regulating RPL5 in non-small cell lung
            cancer
  JOURNAL   Cancer Med 11 (23), 4513-4525 (2022)
   PUBMED   35864588
  REMARK    GeneRIF: DDX24 promotes metastasis by regulating RPL5 in non-small
            cell lung cancer.
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Zhang,H., Liu,J., Dang,Q., Wang,X., Chen,J., Lin,X., Yang,N.,
            Du,J., Shi,H., Liu,Y. and Han,J.
  TITLE     Ribosomal protein RPL5 regulates colon cancer cell proliferation
            and migration through MAPK/ERK signaling pathway
  JOURNAL   BMC Mol Cell Biol 23 (1), 48 (2022)
   PUBMED   36384455
  REMARK    GeneRIF: Ribosomal protein RPL5 regulates colon cancer cell
            proliferation and migration through MAPK/ERK signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Matsumori,H., Watanabe,K., Tachiwana,H., Fujita,T., Ito,Y.,
            Tokunaga,M., Sakata-Sogawa,K., Osakada,H., Haraguchi,T., Awazu,A.,
            Ochiai,H., Sakata,Y., Ochiai,K., Toki,T., Ito,E., Goldberg,I.G.,
            Tokunaga,K., Nakao,M. and Saitoh,N.
  TITLE     Ribosomal protein L5 facilitates rDNA-bundled condensate and
            nucleolar assembly
  JOURNAL   Life Sci Alliance 5 (7), e202101045 (2022)
   PUBMED   35321919
  REMARK    GeneRIF: Ribosomal protein L5 facilitates rDNA-bundled condensate
            and nucleolar assembly.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Hirano,K., Ito,M. and Hartshorne,D.J.
  TITLE     Interaction of the ribosomal protein, L5, with protein phosphatase
            type 1
  JOURNAL   J Biol Chem 270 (34), 19786-19790 (1995)
   PUBMED   7649987
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Frigerio,J.M., Dagorn,J.C. and Iovanna,J.L.
  TITLE     Cloning, sequencing and expression of the L5, L21, L27a, L28, S5,
            S9, S10 and S29 human ribosomal protein mRNAs
  JOURNAL   Biochim Biophys Acta 1262 (1), 64-68 (1995)
   PUBMED   7772601
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Pogue-Geile,K., Geiser,J.R., Shu,M., Miller,C., Wool,I.G.,
            Meisler,A.I. and Pipas,J.M.
  TITLE     Ribosomal protein genes are overexpressed in colorectal cancer:
            isolation of a cDNA clone encoding the human S3 ribosomal protein
  JOURNAL   Mol Cell Biol 11 (8), 3842-3849 (1991)
   PUBMED   1712897
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Steitz,J.A., Berg,C., Hendrick,J.P., La Branche-Chabot,H.,
            Metspalu,A., Rinke,J. and Yario,T.
  TITLE     A 5S rRNA/L5 complex is a precursor to ribosome assembly in
            mammalian cells
  JOURNAL   J Cell Biol 106 (3), 545-556 (1988)
   PUBMED   3279045
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BP247508.1, AF113210.1 and N67963.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 3, 2001 this sequence version replaced NP_000960.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L18P family of ribosomal proteins and component of the 60S
            subunit. The encoded protein binds 5S rRNA to form a stable complex
            called the 5S ribonucleoprotein particle (RNP), which is necessary
            for the transport of nonribosome-associated cytoplasmic 5S rRNA to
            the nucleolus for assembly into ribosomes. The encoded protein may
            also function to inhibit tumorigenesis through the activation of
            downstream tumor suppressors and the downregulation of oncoprotein
            expression. Mutations in this gene have been identified in patients
            with Diamond-Blackfan Anemia (DBA). This gene is co-transcribed
            with the small nucleolar RNA gene U21, which is located in its
            fifth intron. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            throughout the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the supported protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1139019.1,
                                           SRR3476690.127437.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370321.8/ ENSP00000359345.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p22.1"
     Protein         1..297
                     /product="large ribosomal subunit protein uL18"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L5; protein phosphatase 1,
                     regulatory subunit 135"
                     /calculated_mol_wt=34232
     Region          1..295
                     /region_name="PTZ00069"
                     /note="60S ribosomal protein L5; Provisional"
                     /db_xref="CDD:240254"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Site            48
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Site            185
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P47962; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Site            232
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     Region          253..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P46777.3)"
     Site            272
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P46777.3)"
     CDS             1..297
                     /gene="RPL5"
                     /gene_synonym="L5; MSTP030; PPP1R135; uL18"
                     /coded_by="NM_000969.5:76..969"
                     /db_xref="CCDS:CCDS741.1"
                     /db_xref="GeneID:6125"
                     /db_xref="HGNC:HGNC:10360"
                     /db_xref="MIM:603634"
ORIGIN      
        1 mgfvkvvknk ayfkryqvkf rrrregktdy yarkrlviqd knkyntpkyr mivrvtnrdi
       61 icqiayarie gdmivcaaya helpkygvkv gltnyaaayc tglllarrll nrfgmdkiye
      121 gqvevtgdey nvesidgqpg aftcyldagl artttgnkvf galkgavdgg lsiphstkrf
      181 pgydseskef naevhrkhim gqnvadymry lmeededayk kqfsqyikns vtpdmmeemy
      241 kkahaairen pvyekkpkke vkkkrwnrpk mslaqkkdrv aqkkasflra qeraaes
//
LOCUS       NP_001008213             577 aa            linear   PRI 20-NOV-2025
DEFINITION  optineurin [Homo sapiens].
ACCESSION   NP_001008213
VERSION     NP_001008213.1
DBSOURCE    REFSEQ: accession NM_001008212.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Nan,H., Kim,Y.J., Chu,M., Li,D., Li,J., Jiang,D., Wu,Y., Ohtsuka,T.
            and Wu,L.
  TITLE     Genetic and clinical landscape of Chinese frontotemporal dementia:
            dominance of TBK1 and OPTN mutations
  JOURNAL   Alzheimers Res Ther 16 (1), 127 (2024)
   PUBMED   38872230
  REMARK    GeneRIF: Genetic and clinical landscape of Chinese frontotemporal
            dementia: dominance of TBK1 and OPTN mutations.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Jin,J., Huang,R., Chang,Y. and Yi,X.
  TITLE     Roles and mechanisms of optineurin in bone metabolism
  JOURNAL   Biomed Pharmacother 172, 116258 (2024)
   PUBMED   38350370
  REMARK    GeneRIF: Roles and mechanisms of optineurin in bone metabolism.
            Review article
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Yamano,K., Sawada,M., Kikuchi,R., Nagataki,K., Kojima,W., Endo,R.,
            Kinefuchi,H., Sugihara,A., Fujino,T., Watanabe,A., Tanaka,K.,
            Hayashi,G., Murakami,H. and Matsuda,N.
  TITLE     Optineurin provides a mitophagy contact site for TBK1 activation
  JOURNAL   EMBO J 43 (5), 754-779 (2024)
   PUBMED   38287189
  REMARK    GeneRIF: Optineurin provides a mitophagy contact site for TBK1
            activation.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   D'Urso,B., Weil,R. and Genin,P.
  TITLE     [Optineurin and mitochondrial dysfunction in neurodegeneration]
  JOURNAL   Med Sci (Paris) 40 (2), 167-175 (2024)
   PUBMED   38411425
  REMARK    GeneRIF: [Optineurin and mitochondrial dysfunction in
            neurodegeneration].
            Review article
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Fong,K.S. and de Couet,H.G.
  TITLE     Novel proteins interacting with the leucine-rich repeat domain of
            human flightless-I identified by the yeast two-hybrid system
  JOURNAL   Genomics 58 (2), 146-157 (1999)
   PUBMED   10366446
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Sarfarazi,M., Child,A., Stoilova,D., Brice,G., Desai,T.,
            Trifan,O.C., Poinoosawmy,D. and Crick,R.P.
  TITLE     Localization of the fourth locus (GLC1E) for adult-onset primary
            open-angle glaucoma to the 10p15-p14 region
  JOURNAL   Am J Hum Genet 62 (3), 641-652 (1998)
   PUBMED   9497264
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Li,Y., Kang,J. and Horwitz,M.S.
  TITLE     Interaction of an adenovirus E3 14.7-kilodalton protein with a
            novel tumor necrosis factor alpha-inducible cellular protein
            containing leucine zipper domains
  JOURNAL   Mol Cell Biol 18 (3), 1601-1610 (1998)
   PUBMED   9488477
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI552635.1, AF420373.1,
            BC032762.1, AF420371.1, AF070533.1 and AL355355.25.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the coiled-coil containing protein
            optineurin. Optineurin may play a role in normal-tension glaucoma
            and adult-onset primary open angle glaucoma. Optineurin interacts
            with adenovirus E3-14.7K protein and may utilize tumor necrosis
            factor-alpha or Fas-ligand pathways to mediate apoptosis,
            inflammation or vasoconstriction. Optineurin may also function in
            cellular morphogenesis and membrane trafficking, vesicle
            trafficking, and transcription activation through its interactions
            with the RAB8, huntingtin, and transcription factor IIIA proteins.
            Alternative splicing results in multiple transcript variants
            encoding the same protein. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.228417.1,
                                           SRR1660809.111304.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378747.8/ ENSP00000368021.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..577
                     /product="optineurin"
                     /note="nemo-related protein; tumor necrosis factor
                     alpha-inducible cellular protein containing leucine zipper
                     domains; transcrption factor IIIA-interacting protein;
                     Huntingtin interacting protein L; FIP-2; HIP-7; huntingtin
                     yeast partner L; E3-14.7K-interacting protein;
                     huntingtin-interacting protein 7; huntingtin-interacting
                     protein L; optic neuropathy-inducing protein;
                     transcription factor IIIA-interacting protein"
                     /calculated_mol_wt=65791
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          37..103
                     /region_name="NEMO"
                     /note="NF-kappa-B essential modulator NEMO; pfam11577"
                     /db_xref="CDD:431942"
     Region          58..209
                     /region_name="Interaction with Rab8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          101..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          176..181
                     /region_name="LIR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TBK1.
                     /evidence=ECO:0000269|PubMed:21617041,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          186..209
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            198
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          245..>520
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Region          261..297
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          408..507
                     /region_name="CC2-LZ"
                     /note="Leucine zipper of domain CC2 of NEMO, NF-kappa-B
                     essential modulator; pfam16516"
                     /db_xref="CDD:465155"
     Region          411..577
                     /region_name="Interaction with HD"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          412..520
                     /region_name="Interaction with MYO6.
                     /evidence=ECO:0000269|PubMed:15837803"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          474..479
                     /region_name="UBAN"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96CV9.3)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96CV9.3)"
     Region          551..576
                     /region_name="zf_C2H2_10"
                     /note="C2H2 type zinc-finger; pfam18414"
                     /db_xref="CDD:436483"
     CDS             1..577
                     /gene="OPTN"
                     /gene_synonym="ALS12; FIP2; GLC1E; HIP7; HYPL; NRP;
                     TFIIIA-INTP"
                     /coded_by="NM_001008212.2:304..2037"
                     /db_xref="CCDS:CCDS7094.1"
                     /db_xref="GeneID:10133"
                     /db_xref="HGNC:HGNC:17142"
                     /db_xref="MIM:602432"
ORIGIN      
        1 mshqplsclt ekedspsest gngpphlahp nldtftpeel lqqmkellte nhqlkeamkl
       61 nnqamkgrfe elsawtekqk eerqffeiqs keakerlmal sheneklkee lgklkgkser
      121 ssedptddsr lpraeaeqek dqlrtqvvrl qaekadllgi vselqlklns sgssedsfve
      181 irmaegeaeg svkeikhspg ptrtvstgta lskyrsrsad gaknyfehee ltvsqlllcl
      241 regnqkverl evalkeaker vsdfekktsn rseietqteg stekendeek gpetvgseve
      301 alnlqvtslf kelqeahtkl seaelmkkrl qekcqalerk nsaipselne kqelvytnkk
      361 lelqvesmls eikmeqakte dekskltvlq mthnkllqeh nnalktieel trkesekvdr
      421 avlkelsekl elaekalask qlqmdemkqt iakqeedlet mtilraqmev ycsdfhaera
      481 arekiheeke qlalqlavll kendafedgg rqslmemqsr hgartsdsdq qaylvqrgae
      541 drdwrqqrni pihscpkcge vlpdidtlqi hvmdcii
//
LOCUS       NP_003944                269 aa            linear   PRI 20-NOV-2025
DEFINITION  myelin protein zero-like protein 1 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_003944
VERSION     NP_003944.1
DBSOURCE    REFSEQ: accession NM_003953.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Wang,A., Fan,F., Zang,C., Li,C., Hong,H., Wang,Z., Gao,Y., Chen,L.,
            Yu,X., Zhou,C. and Zhao,C.
  TITLE     MPZL1 Promotes Lung Adenocarcinoma Progression by Enhancing Tumor
            Proliferation, Invasion, Migration, and Suppressing Immune Function
            via Transforming Growth Factor-beta1
  JOURNAL   Hum Gene Ther 34 (11-12), 540-553 (2023)
   PUBMED   37183407
  REMARK    GeneRIF: MPZL1 Promotes Lung Adenocarcinoma Progression by
            Enhancing Tumor Proliferation, Invasion, Migration, and Suppressing
            Immune Function via Transforming Growth Factor-beta1.
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Feng,J., Ouyang,H., Wang,J., Pan,D., Sheng,L., Xu,C., Lin,W.,
            Hu,D., Chang,C. and Jia,D.
  TITLE     MPZL1 upregulation promotes tumor metastasis and correlates with
            unfavorable prognosis in non-small cell lung cancer
  JOURNAL   Carcinogenesis 43 (10), 919-929 (2022)
   PUBMED   35727197
  REMARK    GeneRIF: MPZL1 upregulation promotes tumor metastasis and
            correlates with unfavorable prognosis in non-small cell lung
            cancer.
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Sun,D., Gou,H., Wang,D., Li,C., Li,Y., Su,H., Wang,X., Zhang,X. and
            Yu,J.
  TITLE     LncRNA TNFRSF10A-AS1 promotes gastric cancer by directly binding to
            oncogenic MPZL1 and is associated with patient outcome
  JOURNAL   Int J Biol Sci 18 (8), 3156-3166 (2022)
   PUBMED   35637954
  REMARK    GeneRIF: LncRNA TNFRSF10A-AS1 promotes gastric cancer by directly
            binding to oncogenic MPZL1 and is associated with patient outcome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Zhao,R., Guerrah,A., Tang,H. and Zhao,Z.J.
  TITLE     Cell surface glycoprotein PZR is a major mediator of concanavalin
            A-induced cell signaling
  JOURNAL   J Biol Chem 277 (10), 7882-7888 (2002)
   PUBMED   11751924
  REMARK    GeneRIF: PZR is a major receptor of ConA and has an important role
            in cell signaling via c-Src. Considering the various biological
            activities of ConA, the study of PZR may have major therapeutic
            implications
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Zhao,R. and Zhao,Z.J.
  TITLE     Dissecting the interaction of SHP-2 with PZR, an immunoglobulin
            family protein containing immunoreceptor tyrosine-based inhibitory
            motifs
  JOURNAL   J Biol Chem 275 (8), 5453-5459 (2000)
   PUBMED   10681522
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Tang,D.S., Yu,K.P., Tang,X.X., Zhang,H.L., Pan,Q., Dai,H.P. and
            Xia,J.H.
  TITLE     Cloning of Human Myelin Protein Zero-like Genes by Bioinformatics
            Strategy
  JOURNAL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 32 (4),
            364-368 (2000)
   PUBMED   12075424
REFERENCE   10 (residues 1 to 269)
  AUTHORS   Zhao,Z.J. and Zhao,R.
  TITLE     Purification and cloning of PZR, a binding protein and putative
            physiological substrate of tyrosine phosphatase SHP-2
  JOURNAL   J Biol Chem 273 (45), 29367-29372 (1998)
   PUBMED   9792637
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA725074.1, AY359019.1, Z99943.1 and AW292498.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK075334.1, SRR1660805.14382.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359523.7/ ENSP00000352513.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q24.2"
     Protein         1..269
                     /product="myelin protein zero-like protein 1 isoform a
                     precursor"
                     /note="protein zero related; myelin protein zero-like
                     protein 1; immunoglobulin family transmembrane protein"
                     /calculated_mol_wt=25705
     sig_peptide     1..35
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
                     /calculated_mol_wt=3395
     mat_peptide     36..269
                     /product="Myelin protein zero-like protein 1.
                     /id=PRO_0000240335"
                     /note="propagated from UniProtKB/Swiss-Prot (O95297.1)"
                     /calculated_mol_wt=25705
     Region          38..154
                     /region_name="IgV_P0-like"
                     /note="Immunoglobulin (Ig)-like domain of protein zero
                     (P0) and similar proteins; cd05715"
                     /db_xref="CDD:409380"
     Region          38..61
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409380"
     Region          38..42
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409380"
     Site            order(39,41,53,61,105,108,123..124)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:409380"
     Region          44..50
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409380"
     Site            50
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19349973,
                     ECO:0000269|PubMed:30392906; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Region          52..62
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409380"
     Region          62..70
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409380"
     Region          70..78
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409380"
     Region          71..83
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409380"
     Region          84..98
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409380"
     Region          85..91
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409380"
     Region          93..98
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409380"
     Region          103..137
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409380"
     Region          106..112
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409380"
     Region          116..124
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409380"
     Site            130
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30392906; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Region          131..138
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409380"
     Region          139..145
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409380"
     Region          146..154
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409380"
     Region          146..154
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409380"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Region          199..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Site            206
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Site            208
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Site            221
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Region          239..244
                     /region_name="ITIM motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10681522,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O95297.1)"
     Region          261..266
                     /region_name="ITIM motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O95297.1)"
     Site            263
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10681522,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O95297.1)"
     CDS             1..269
                     /gene="MPZL1"
                     /gene_synonym="MPZL1b; PZR; PZR1b; PZRa; PZRb"
                     /coded_by="NM_003953.6:171..980"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1264.1"
                     /db_xref="GeneID:9019"
                     /db_xref="HGNC:HGNC:7226"
                     /db_xref="MIM:604376"
ORIGIN      
        1 maasagagav iaapdsrrwl wsvlaaalgl ltagvsalev ytpkeifvan gtqgkltckf
       61 kststtgglt svswsfqpeg adttvsffhy sqgqvylgny ppfkdriswa gdldkkdasi
      121 nienmqfihn gtyicdvknp pdivvqpghi rlyvvekenl pvfpvwvvvg ivtavvlglt
      181 llismilavl yrrknskrdy tgcstsesls pvkqaprksp sdteglvksl psgshqgpvi
      241 yaqldhsggh hsdkinkses vvyadirkn
//
LOCUS       NP_003080                437 aa            linear   PRI 20-NOV-2025
DEFINITION  U1 small nuclear ribonucleoprotein 70 kDa isoform 1 [Homo sapiens].
ACCESSION   NP_003080
VERSION     NP_003080.2
DBSOURCE    REFSEQ: accession NM_003089.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Kumari,S., Adhikary,A. and Singh,K.K.
  TITLE     BioID proximity mapping reveals novel SAP18 interactions in the
            prespliceosomal complex
  JOURNAL   Biochem Biophys Res Commun 738, 150944 (2024)
   PUBMED   39522233
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Paul,T., Zhang,P., Zhang,Z., Fargason,T., De Silva,N.I.U.,
            Powell,E., Ekpenyong,E., Jamal,S., Yu,Y., Prevelige,P., Lu,R. and
            Zhang,J.
  TITLE     The U1-70K and SRSF1 interaction is modulated by phosphorylation
            during the early stages of spliceosome assembly
  JOURNAL   Protein Sci 33 (8), e5117 (2024)
   PUBMED   39023093
  REMARK    GeneRIF: The U1-70K and SRSF1 interaction is modulated by
            phosphorylation during the early stages of spliceosome assembly.
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Jiang,D., Zhu,X.L., An,Y. and Li,Y.R.
  TITLE     Clinical significance of small nuclear ribonucleoprotein U1 subunit
            70 in patients with hepatocellular carcinoma
  JOURNAL   PeerJ 12, e16876 (2024)
   PUBMED   38500533
  REMARK    GeneRIF: Clinical significance of small nuclear ribonucleoprotein
            U1 subunit 70 in patients with hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 437)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Spritz,R.A., Strunk,K., Surowy,C.S. and Mohrenweiser,H.W.
  TITLE     Human U1-70K ribonucleoprotein antigen gene: organization,
            nucleotide sequence, and mapping to locus 19q13.3
  JOURNAL   Genomics 8 (2), 371-379 (1990)
   PUBMED   2147422
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Du Clos,T.W.
  TITLE     C-reactive protein reacts with the U1 small nuclear
            ribonucleoprotein
  JOURNAL   J Immunol 143 (8), 2553-2559 (1989)
   PUBMED   2477447
REFERENCE   9  (residues 1 to 437)
  AUTHORS   Query,C.C., Bentley,R.C. and Keene,J.D.
  TITLE     A common RNA recognition motif identified within a defined U1 RNA
            binding domain of the 70K U1 snRNP protein
  JOURNAL   Cell 57 (1), 89-101 (1989)
   PUBMED   2467746
REFERENCE   10 (residues 1 to 437)
  AUTHORS   Spritz,R.A., Strunk,K., Surowy,C.S., Hoch,S.O., Barton,D.E. and
            Francke,U.
  TITLE     The human U1-70K snRNP protein: cDNA cloning, chromosomal
            localization, expression, alternative splicing and RNA-binding
  JOURNAL   Nucleic Acids Res 15 (24), 10373-10391 (1987)
   PUBMED   2447561
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB189176.1, BC001315.1, X06815.1 and BM969999.1.
            
            On Apr 5, 2003 this sequence version replaced NP_003080.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.196941.1,
                                           SRR3476690.182849.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000598441.6/ ENSP00000472998.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..437
                     /product="U1 small nuclear ribonucleoprotein 70 kDa
                     isoform 1"
                     /note="U1 small nuclear ribonucleoprotein 70 kDa; U1 snRNP
                     70 kDa; small nuclear ribonucleoprotein 70kDa (U1); small
                     nuclear ribonucleoprotein, U1 70kDa subunit"
                     /calculated_mol_wt=51426
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (P08621.2)"
     Region          3..94
                     /region_name="U1snRNP70_N"
                     /note="U1 small nuclear ribonucleoprotein of 70kDa MW N
                     terminal; pfam12220"
                     /db_xref="CDD:432406"
     Region          48..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08621.2)"
     Region          92..202
                     /region_name="Required for interaction with U1 RNA.
                     /evidence=ECO:0000269|PubMed:2467746"
                     /note="propagated from UniProtKB/Swiss-Prot (P08621.2)"
     Region          102..187
                     /region_name="RRM_snRNP70"
                     /note="RNA recognition motif (RRM) found in U1 small
                     nuclear ribonucleoprotein 70 kDa (U1-70K) and similar
                     proteins; cd12236"
                     /db_xref="CDD:409682"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P08621.2)"
     Site            126
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P08621.2)"
     Region          187..437
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P08621.2)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P08621.2)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P08621.2)"
     Site            320
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P08621.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P08621.2)"
     CDS             1..437
                     /gene="SNRNP70"
                     /gene_synonym="RNPU1Z; RPU1; Snp1; SNRP70; U1-70K; U170K;
                     U1AP; U1RNP"
                     /coded_by="NM_003089.6:197..1510"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12756.1"
                     /db_xref="GeneID:6625"
                     /db_xref="HGNC:HGNC:11150"
                     /db_xref="MIM:180740"
ORIGIN      
        1 mtqflppnll alfaprdpip ylppleklph ekhhnqpycg iapyirefed prdappptra
       61 etreermerk rrekierrqq evetelkmwd phndpnaqgd afktlfvarv nydttesklr
      121 refevygpik rihmvyskrs gkprgyafie yeherdmhsa ykhadgkkid grrvlvdver
      181 grtvkgwrpr rlggglggtr rggadvnirh sgrddtsryd erpgpsplph rdrdrdrere
      241 rrersrerdk ererrrsrsr drrrrsrsrd keerrrsrer skdkdrdrkr rssrsrerar
      301 rererkeelr ggggdmaeps eagdappddg ppgelgpdgp dgpeekgrdr drerrrshrs
      361 ererrrdrdr drdrdrehkr gergsergrd eargggggqd ngleglgnds rdmymesegg
      421 dgylapengy lmeaape
//
LOCUS       NP_001230869             320 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphoribosyl pyrophosphate synthase-associated protein 2 isoform
            3 [Homo sapiens].
ACCESSION   NP_001230869
VERSION     NP_001230869.1
DBSOURCE    REFSEQ: accession NM_001243940.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Bogaert,A., Fijalkowska,D., Staes,A., Van de Steene,T.,
            Vuylsteke,M., Stadler,C., Eyckerman,S., Spirohn,K., Hao,T.,
            Calderwood,M.A. and Gevaert,K.
  TITLE     N-terminal proteoforms may engage in different protein complexes
  JOURNAL   Life Sci Alliance 6 (8), e202301972 (2023)
   PUBMED   37316325
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T. and Itakura,M.
  TITLE     Assignment of the human phosphoribosylpyrophosphate
            synthetase-associated protein 41 gene (PRPSAP2) to 17p11.2-p12
  JOURNAL   Genomics 54 (1), 180-181 (1998)
   PUBMED   9806849
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Katashima,R., Iwahana,H., Fujimura,M., Yamaoka,T., Ishizuka,T.,
            Tatibana,M. and Itakura,M.
  TITLE     Molecular cloning of a human cDNA for the 41-kDa
            phosphoribosylpyrophosphate synthetase-associated protein
  JOURNAL   Biochim Biophys Acta 1396 (3), 245-250 (1998)
   PUBMED   9545573
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX648850.1, BC143475.1,
            BC106050.1, AI955172.1 and AI379788.1.
            
            Summary: This gene encodes a protein that associates with the
            enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes
            the formation of phosphoribosylpyrophosphate which is a substrate
            for synthesis of purine and pyrimidine nucleotides, histidine,
            tryptophan and NAD. PRS exists as a complex with two catalytic
            subunits and two associated subunits. This gene encodes a
            non-catalytic associated subunit of PRS. Alternate splicing results
            in multiple transcript variants. [provided by RefSeq, Sep 2011].
            
            Transcript Variant: This variant (3) has a shorter 5' UTR and lacks
            an in-frame exon in the coding region, compared to variant 1. The
            encoded isoform (3) is shorter, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143475.1, SRR1163658.282673.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMN03267754
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..320
                     /product="phosphoribosyl pyrophosphate synthase-associated
                     protein 2 isoform 3"
                     /note="phosphoribosyl pyrophosphate synthase-associated
                     protein 2; PRPP synthase-associated protein 2; 41 kDa
                     phosphoribosypyrophosphate synthetase-associated protein"
                     /calculated_mol_wt=35417
     Region          20..314
                     /region_name="PrsA"
                     /note="Phosphoribosylpyrophosphate synthetase [Nucleotide
                     transport and metabolism]; COG0462"
                     /db_xref="CDD:440230"
     CDS             1..320
                     /gene="PRPSAP2"
                     /gene_synonym="PAP41"
                     /coded_by="NM_001243940.1:129..1091"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58525.1"
                     /db_xref="GeneID:5636"
                     /db_xref="HGNC:HGNC:9467"
                     /db_xref="MIM:603762"
ORIGIN      
        1 mfcvtppele tkmnitkggl vlfsansnss cmelskkiae rlgvemgkvq vyqepnretr
       61 vqiqesvrgk dvfiiqtvsk dvnttimell imvyacktsc aksiigvipy fpyskqckmr
      121 krgsivskll asmmckaglt hlitmdlhqk eiqgffnipv dnlraspfll qyiqeeipdy
      181 rnavivaksp asakraqsfa erlrlgiavi hgeaqdaesd lvdgrhsppm vrsvaaihps
      241 leipmlipke kppitvvgdv ggriaiivvv vtntiphevq klqcpkiktv dismilseai
      301 rrihngesms ylfrnigldd
//
LOCUS       NP_060267                525 aa            linear   PRI 20-NOV-2025
DEFINITION  BTB/POZ domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_060267
VERSION     NP_060267.2
DBSOURCE    REFSEQ: accession NM_017797.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Xu,L., Yang,L., Moitra,P.K., Hashimoto,K., Rallabhandi,P., Kaul,S.,
            Meroni,G., Jensen,J.P., Weissman,A.M. and D'Arpa,P.
  TITLE     BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the
            RBCC/tripartite motif protein, TRIM5delta
  JOURNAL   Exp Cell Res 288 (1), 84-93 (2003)
   PUBMED   12878161
  REMARK    GeneRIF: subcellular colocalization of BTBD1 and BTBD2 to
            cytoplasmic bodies; TRIM5delta colocalized with BTBD1/2 and
            appeared to serve as a scaffold for the assembly of endogenous
            BTBD1/2 proteins
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Yamada,A., Kawano,K., Koga,M., Takamori,S., Nakagawa,M. and Itoh,K.
  TITLE     Gene and peptide analyses of newly defined lung cancer antigens
            recognized by HLA-A2402-restricted tumor-specific cytotoxic T
            lymphocytes
  JOURNAL   Cancer Res 63 (11), 2829-2835 (2003)
   PUBMED   12782588
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Xu,L., Yang,L., Hashimoto,K., Anderson,M., Kohlhagen,G., Pommier,Y.
            and D'Arpa,P.
  TITLE     Characterization of BTBD1 and BTBD2, two similar
            BTB-domain-containing Kelch-like proteins that interact with
            Topoisomerase I
  JOURNAL   BMC Genomics 3, 1 (2002)
   PUBMED   11818025
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Carim-Todd,L., Sumoy,L., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     Identification and characterization of BTBD1, a novel BTB domain
            containing gene on human chromosome 15q24
  JOURNAL   Gene 262 (1-2), 275-281 (2001)
   PUBMED   11179693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004678.1, AF355797.1,
            BU849231.1, BC000564.2 and BC008035.2.
            
            On Apr 10, 2002 this sequence version replaced NP_060267.1.
            
            Summary: The C-terminus of the protein encoded by this gene binds
            topoisomerase I. The N-terminus contains a proline-rich region and
            a BTB/POZ domain (broad-complex, Tramtrack and bric a brac/Pox
            virus and Zinc finger), both of which are typically involved in
            protein-protein interactions. Subcellularly, the protein localizes
            to cytoplasmic bodies. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF355797.1, BC094820.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000255608.9/ ENSP00000255608.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..525
                     /product="BTB/POZ domain-containing protein 2"
                     /note="BTB (POZ) domain containing 2"
                     /calculated_mol_wt=55800
     Region          1..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BX70.1)"
     Region          95..221
                     /region_name="BTB_POZ_BTBD1_2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in BTB/POZ
                     domain-containing proteins, BTBD1 and BTBD2; cd18281"
                     /db_xref="CDD:349590"
     Region          217..322
                     /region_name="BACK_BTBD2"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     BTB/POZ domain-containing protein 2 (BTBD2); cd18523"
                     /db_xref="CDD:350598"
     Region          375..524
                     /region_name="PHR"
                     /note="PHR domain; pfam08005"
                     /db_xref="CDD:462339"
     CDS             1..525
                     /gene="BTBD2"
                     /coded_by="NM_017797.4:12..1589"
                     /db_xref="CCDS:CCDS12078.1"
                     /db_xref="GeneID:55643"
                     /db_xref="HGNC:HGNC:15504"
                     /db_xref="MIM:608531"
ORIGIN      
        1 maaggsggra scppgvgvgp gtggspgpsa naaatpapgn aaaaaaaaaa aaaapgptpp
       61 appgpgtdaq aagaeraeea agpgaaalqr eaaynwqask ptvqerfafl fnnevlcdvh
      121 flvgkglssq ripahrfvla vgsavfdamf nggmattste ielpdvepaa flallkflys
      181 devqigpetv mttlytakky avpaleahcv eflkknlrad nafmlltqar lfdepqlasl
      241 clenidknta daitaegftd idldtlvavl erdtlgirev rlfnavvrws eaecqrqqlq
      301 vtpenrrkvl gkalglirfp lmtieefaag paqsgilvdr evvslflhft vnpkprvefi
      361 drprcclrgk ecsinrfqqv esrwgysgts drirfsvnkr ifvvgfglyg sihgptdyqv
      421 niqiihtdsn tvlgqndtgf scdgsastfr vmfkepvevl pnvnytacat lkgpdshygt
      481 kglrkvthes pttgaktcft fcyaagnnng tsvedgqipe vifyt
//
LOCUS       NP_291027                630 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM41 isoform 1 [Homo sapiens].
ACCESSION   NP_291027
VERSION     NP_291027.3
DBSOURCE    REFSEQ: accession NM_033549.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Zhen,Z., Chen,Y., Wang,H., Tang,H., Zhang,H., Liu,H., Jiang,Y. and
            Mao,Z.
  TITLE     Nuclear cGAS restricts L1 retrotransposition by promoting
            TRIM41-mediated ORF2p ubiquitination and degradation
  JOURNAL   Nat Commun 14 (1), 8217 (2023)
   PUBMED   38086852
  REMARK    GeneRIF: Nuclear cGAS restricts L1 retrotransposition by promoting
            TRIM41-mediated ORF2p ubiquitination and degradation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Zhang,X., Hu,Z., Wang,X., Li,L., Zhu,B., Lin,X., Zhang,J. and
            Hua,Z.
  TITLE     ANXA10 promotes melanoma metastasis by suppressing E3 ligase
            TRIM41-directed PKD1 degradation
  JOURNAL   Cancer Lett 519, 237-249 (2021)
   PUBMED   34324862
  REMARK    GeneRIF: ANXA10 promotes melanoma metastasis by suppressing E3
            ligase TRIM41-directed PKD1 degradation.
            Erratum:[Cancer Lett. 2023 Aug 10;569:216310. doi:
            10.1016/j.canlet.2023.216310. PMID: 37474390]
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Yu,Z., Li,X., Yang,M., Huang,J., Fang,Q., Jia,J., Li,Z., Gu,Y.,
            Chen,T. and Cao,X.
  TITLE     TRIM41 is required to innate antiviral response by
            polyubiquitinating BCL10 and recruiting NEMO
  JOURNAL   Signal Transduct Target Ther 6 (1), 90 (2021)
   PUBMED   33640899
  REMARK    GeneRIF: TRIM41 is required to innate antiviral response by
            polyubiquitinating BCL10 and recruiting NEMO.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 630)
  AUTHORS   Chen,D., Gould,C., Garza,R., Gao,T., Hampton,R.Y. and Newton,A.C.
  TITLE     Amplitude control of protein kinase C by RINCK, a novel E3
            ubiquitin ligase
  JOURNAL   J Biol Chem 282 (46), 33776-33787 (2007)
   PUBMED   17893151
  REMARK    GeneRIF: RINCK is an E3 ligase that specifically recognizes the C1
            domain of PKC isoforms
REFERENCE   8  (residues 1 to 630)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   9  (residues 1 to 630)
  AUTHORS   Tanaka,M., Fukuda,Y., Mashima,K. and Hanai,R.
  TITLE     Intracellular localization and domain organization of human TRIM41
            proteins
  JOURNAL   Mol Biol Rep 32 (2), 87-93 (2005)
   PUBMED   16022281
  REMARK    GeneRIF: observed in the cytoplasm and the nucleus; nuclear
            transport is mediated by an N-terminal segment common to both alpha
            and beta isoforms, but independent of a classical nuclear
            localization signal sequence.
REFERENCE   10 (residues 1 to 630)
  AUTHORS   Kobayashi,M. and Hanai,R.
  TITLE     M phase-specific association of human topoisomerase IIIbeta with
            chromosomes
  JOURNAL   Biochem Biophys Res Commun 287 (1), 282-287 (2001)
   PUBMED   11549288
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA341383.1, BC090953.1 and
            BC018765.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 10, 2004 this sequence version replaced NP_291027.2.
            
            Summary: This gene encodes a member of the tripartite motif (TRIM)
            family. The TRIM family is characterized by a signature motif
            composed of a RING finger, one or more B-box domains, and a
            coiled-coil region. This encoded protein may play a role in protein
            kinase C signaling. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Oct
            2011].
            
            Transcript Variant: This variant (1, also referred to as alpha)
            represents the longest transcript and encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC018765.1, BC090953.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000315073.10/ ENSP00000320869.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..630
                     /product="E3 ubiquitin-protein ligase TRIM41 isoform 1"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase TRIM41; RING-finger
                     protein that interacts with C kinase; RING
                     finger-interacting protein with C kinase; RING-type E3
                     ubiquitin transferase TRIM41"
                     /calculated_mol_wt=71539
     Region          15..>48
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          51..86
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV44.3)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8WV44.3)"
     Region          143..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV44.3)"
     Region          <182..211
                     /region_name="RING_Ubox"
                     /note="RING finger (Really Interesting New Gene) domain
                     and U-box domain superfamily; cl17238"
                     /db_xref="CDD:473075"
     Region          225..268
                     /region_name="Bbox2_TRIM7-like"
                     /note="B-box-type 2 zinc finger found in tripartite
                     motif-containing proteins TRIM7, TRIM27 and similar
                     proteins; cd19762"
                     /db_xref="CDD:380820"
     Region          <249..>395
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          432..630
                     /region_name="SPRY_PRY_TRIM41"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     41 (TRIM41); cd13741"
                     /db_xref="CDD:240499"
     Site            447
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8WV44.3)"
     Region          503..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WV44.3)"
     CDS             1..630
                     /gene="TRIM41"
                     /gene_synonym="RINCK"
                     /coded_by="NM_033549.5:720..2612"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4466.1"
                     /db_xref="GeneID:90933"
                     /db_xref="HGNC:HGNC:19013"
                     /db_xref="MIM:610530"
ORIGIN      
        1 maavamtpnp vqtlqeeavc aicldyftdp vsigcghnfc rvcvtqlwgg edeedrdeld
       61 reeeeedgee eeveavgaga gwdtpmrded yegdmeeeve eeeegvfwts gmsrsswdnm
      121 dyvweeedee edldyylgdm eeedlrgede edeeevleev eeedldpvtp lppppaprrc
      181 ftcpqcrksf prrsfrpnlq lanmvqvirq mhptpgrgsr vtdqgicpkh qealklfcev
      241 deeaicvvcr esrshkqhsv vpleevvqey kaklqghvep lrkhleavqk mkakeerrvt
      301 elksqmksel aavasefgrl trflaeeqag lerrlremhe aqlgragaaa srlaeqaaql
      361 srllaeaqer sqqgglrllq diketfnrce evqlqppevw spdpcqphsh dfltdaivrk
      421 msrmfcqaar vdltldpdta hpalmlspdr rgvrlaerrq evadhpkrfs adccvlgaqg
      481 frsgrhywev evggrrgwav gaaresthhk ekvgpggssv gsgdasssrh hhrrrrlhlp
      541 qqpllqrevw cvgtngkryq aqssteqtll spsekprrfg vyldyeagrl gfynaetlah
      601 vhtfsaaflg ervfpffrvl skgtriklcp
//
LOCUS       NP_001138441             947 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NEDD4-like isoform 5 [Homo sapiens].
ACCESSION   NP_001138441
VERSION     NP_001138441.1
DBSOURCE    REFSEQ: accession NM_001144969.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 947)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 947)
  AUTHORS   Chen,G., Pei,Y., Ye,Q., Xie,Z., Gyawali,L. and Liang,X.
  TITLE     NEDD4L-mediated RASGRP2 suppresses high-glucose and oxLDL-induced
            vascular endothelial cell dysfunctions by activating Rap1 and R-Ras
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119844 (2024)
   PUBMED   39260747
  REMARK    GeneRIF: NEDD4L-mediated RASGRP2 suppresses high-glucose and
            oxLDL-induced vascular endothelial cell dysfunctions by activating
            Rap1 and R-Ras.
REFERENCE   3  (residues 1 to 947)
  AUTHORS   Wang,R., Wang,R., Zhou,S., Liu,T., Dang,J., Chen,Q., Chen,J. and
            Wang,Z.
  TITLE     Ubiquitination of angiotensin-converting enzyme 2 contributes to
            the development of pulmonary arterial hypertension mediated by
            neural precursor cell-expressed developmentally down-regulated gene
            4-Like
  JOURNAL   Respir Res 25 (1), 326 (2024)
   PUBMED   39210401
  REMARK    GeneRIF: Ubiquitination of angiotensin-converting enzyme 2
            contributes to the development of pulmonary arterial hypertension
            mediated by neural precursor cell-expressed developmentally
            down-regulated gene 4-Like.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 947)
  AUTHORS   Yang,B. and Kumar,S.
  TITLE     Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with
            distinct physiological functions
  JOURNAL   Cell Death Differ 17 (1), 68-77 (2010)
   PUBMED   19557014
  REMARK    Review article
REFERENCE   5  (residues 1 to 947)
  AUTHORS   Russo,C.J., Melista,E., Cui,J., DeStefano,A.L., Bakris,G.L.,
            Manolis,A.J., Gavras,H. and Baldwin,C.T.
  TITLE     Association of NEDD4L ubiquitin ligase with essential hypertension
  JOURNAL   Hypertension 46 (3), 488-491 (2005)
   PUBMED   16103266
  REMARK    GeneRIF: Significant association between several SNPs and
            hypertension in US whites, Greek whites, and African-Americans.
            Genetic variation in NEDD4L may play role in development or
            progression of some forms of hypertension.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 947)
  AUTHORS   Qi,H., Grenier,J., Fournier,A. and Labrie,C.
  TITLE     Androgens differentially regulate the expression of NEDD4L
            transcripts in LNCaP human prostate cancer cells
  JOURNAL   Mol Cell Endocrinol 210 (1-2), 51-62 (2003)
   PUBMED   14615060
  REMARK    GeneRIF: Results describe the isolation of three new NEDD4L
            transcripts designated NEDD4Lf, NEDD4Lg and NEDD4Lh, which encode
            different forms of the NEDD4L protein.
REFERENCE   7  (residues 1 to 947)
  AUTHORS   Itani,O.A., Campbell,J.R., Herrero,J., Snyder,P.M. and Thomas,C.P.
  TITLE     Alternate promoters and variable splicing lead to hNedd4-2 isoforms
            with a C2 domain and varying number of WW domains
  JOURNAL   Am J Physiol Renal Physiol 285 (5), F916-F929 (2003)
   PUBMED   12876068
  REMARK    GeneRIF: Alternate transcripts of Nedd4-2 may interact with ENaC
            differently. hNedd4-2 has role in regulation of ENaC. Protein
            domains are important for Nedd4-2 function.
            GeneRIF: Identification of multiple splice forms and 5' variants of
            Nedd4l.  5' variants inhibit ENaC-mediated Na+ transport when
            reconstituted in FRT epithelia.  Other splice forms encode Nedd4L
            isoforms with 2 to 4 WW domains having varying affinity for ENaC.
REFERENCE   8  (residues 1 to 947)
  AUTHORS   Chen,H., Ross,C.A., Wang,N., Huo,Y., MacKinnon,D.F., Potash,J.B.,
            Simpson,S.G., McMahon,F.J., DePaulo,J.R. Jr. and McInnis,M.G.
  TITLE     NEDD4L on human chromosome 18q21 has multiple forms of transcripts
            and is a homologue of the mouse Nedd4-2 gene
  JOURNAL   Eur J Hum Genet 9 (12), 922-930 (2001)
   PUBMED   11840194
  REMARK    GeneRIF: Candidate gene for autosomal dominant orthostatic
            hypotensive disorder.
REFERENCE   9  (residues 1 to 947)
  AUTHORS   Winberg,G., Matskova,L., Chen,F., Plant,P., Rotin,D., Gish,G.,
            Ingham,R., Ernberg,I. and Pawson,T.
  TITLE     Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3
            protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
  JOURNAL   Mol Cell Biol 20 (22), 8526-8535 (2000)
   PUBMED   11046148
REFERENCE   10 (residues 1 to 947)
  AUTHORS   Nuber,U., Schwarz,S., Kaiser,P., Schneider,R. and Scheffner,M.
  TITLE     Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7
            (E2-F1) and characterization of their interaction with E6-AP and
            RSP5
  JOURNAL   J Biol Chem 271 (5), 2795-2800 (1996)
   PUBMED   8576257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107896.7, AY112985.2,
            DQ181796.1, BP260852.1, AF070601.1, DA759940.1, AC090236.4 and
            DB317092.1.
            
            Summary: This gene encodes a member of the Nedd4 family of HECT
            domain E3 ubiquitin ligases. HECT domain E3 ubiquitin ligases
            transfer ubiquitin from E2 ubiquitin-conjugating enzymes to protein
            substrates, thus targeting specific proteins for lysosomal
            degradation. The encoded protein mediates the ubiquitination of
            multiple target substrates and plays a critical role in epithelial
            sodium transport by regulating the cell surface expression of the
            epithelial sodium channel, ENaC. Single nucleotide polymorphisms in
            this gene may be associated with essential hypertension.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene. [provided by RefSeq, Mar
            2012].
            
            Transcript Variant: This variant (h) uses an alternate first exon
            and lacks a downstream in-frame exon, compared to variant j, which
            results in the use of a different start codon and a protein
            (isoform 5) with a shorter and distinct N-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY112985.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..947
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.31"
     Protein         1..947
                     /product="E3 ubiquitin-protein ligase NEDD4-like isoform
                     5"
                     /EC_number="2.3.2.26"
                     /EC_number="2.3.2.36"
                     /note="ubiquitin-protein ligase Rsp5; HECT-type E3
                     ubiquitin transferase NED4L; neural precursor cell
                     expressed, developmentally down-regulated 4-like, E3
                     ubiquitin protein ligase"
                     /calculated_mol_wt=109274
     Region          13..145
                     /region_name="C2_NEDD4_NEDD4L"
                     /note="C2 domain present in the Human neural precursor
                     cell-expressed, developmentally down-regulated 4 (NEDD4)
                     and NEDD4-like (NEDD4L/NEDD42); cd04033"
                     /db_xref="CDD:175999"
     Site            order(34,87,89,94)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:175999"
     Region          190..216
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          359..388
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          472..502
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(486,497)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          521..553
                     /region_name="WW"
                     /note="Domain with 2 conserved Trp (W) residues;
                     smart00456"
                     /db_xref="CDD:197736"
     Site            order(537,548)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Site            order(596,627,638,700,873,908..909,912..916,936,943)
                     /site_type="active"
                     /note="catalytic cleft [active]"
                     /db_xref="CDD:238033"
     Region          614..943
                     /region_name="HECTc"
                     /note="Domain Homologous to E6-AP Carboxyl Terminus with;
                     smart00119"
                     /db_xref="CDD:214523"
     Site            order(728,731..732,734..735,738,743,745,749..750,752,757,
                     762,779,783)
                     /site_type="active"
                     /note="E2 interaction site [active]"
                     /db_xref="CDD:238033"
     CDS             1..947
                     /gene="NEDD4L"
                     /gene_synonym="hNEDD4-2; NEDD4-2; NEDD4.2; PVNH7; RSP5"
                     /coded_by="NM_001144969.2:217..3060"
                     /note="isoform 5 is encoded by transcript variant h"
                     /db_xref="CCDS:CCDS59323.1"
                     /db_xref="GeneID:23327"
                     /db_xref="HGNC:HGNC:7728"
                     /db_xref="MIM:606384"
ORIGIN      
        1 mrrlafeqge srilrvkvvs gidlakkdif gasdpyvkls lyvadenrel alvqtktikk
       61 tlnpkwneef yfrvnpsnhr llfevfdenr ltrddflgqv dvplshlpte dptmerpytf
      121 kdfllrprsh ksrvkgflrl kmaympkngg qdeensdqrd dmehgwevvd sndsasqhqe
      181 elpppplppg weekvdnlgr tyyvnhnnrt tqwhrpslmd vssesdnnir qinqeaahrr
      241 frsrrhised lepepseggd vpepwetise evniagdslg lalppppasp gsrtspqels
      301 eelsrrlqit pdsngeqfss liqrepssrl rscsvtdava eqghlpppsv ayvhttpglp
      361 sgweerkdak grtyyvnhnn rtttwtrpim qlaedgasgs atnsnnhlie pqirrprsls
      421 sptvtlsapl egakdspvrr avkdtlsnpq spqpspynsp kpqhkvtqsf lppgwemria
      481 pngrpffidh ntktttwedp rlkfpvhmrs ktslnpndlg plppgweeri hldgrtfyid
      541 hnskitqwed prlqnpaitg pavpysrefk qkydyfrkkl kkpadipnrf emklhrnnif
      601 eesyrrimsv krpdvlkarl wiefesekgl dyggvarewf fllskemfnp yyglfeysat
      661 dnytlqinpn sglcnedhls yftfigrvag lavfhgklld gffirpfykm mlgkqitlnd
      721 mesvdseyyn slkwilendp teldlmfcid eenfgqtyqv dlkpngseim vtnenkreyi
      781 dlviqwrfvn rvqkqmnafl egftellpid likifdenel ellmcglgdv dvndwrqhsi
      841 ykngycpnhp viqwfwkavl lmdaekrirl lqfvtgtsrv pmngfaelyg sngpqlftie
      901 qwgspeklpr ahtcfnrldl ppyetfedlr ekllmavena qgfegvd
//
LOCUS       NP_001278964             661 aa            linear   PRI 20-NOV-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 isoform b
            [Homo sapiens].
ACCESSION   NP_001278964
VERSION     NP_001278964.1
DBSOURCE    REFSEQ: accession NM_001292035.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 661)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 661)
  AUTHORS   Zhang,J., Cao,L., Gao,A., Ren,R., Yu,L., Li,Q., Liu,Y., Qi,W.,
            Hou,Y., Sui,W., Su,G., Zhang,Y., Zhang,C. and Zhang,M.
  TITLE     E3 ligase RNF99 negatively regulates TLR-mediated inflammatory
            immune response via K48-linked ubiquitination of TAB2
  JOURNAL   Cell Death Differ 30 (4), 966-978 (2023)
   PUBMED   36681779
REFERENCE   3  (residues 1 to 661)
  AUTHORS   Koene,S., Klerx-Melis,F., Roest,A.A.W., Kleijwegt,M.C., Bootsma,M.,
            Haak,M.C., van Haeringen,M.H., Ruivenkamp,C.A.L., Nibbeling,E.A.R.
            and van Haeringen,A.
  TITLE     Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family
  JOURNAL   Am J Med Genet A 188 (12), 3510-3515 (2022)
   PUBMED   36000780
  REMARK    GeneRIF: Sacral abnormalities including caudal appendage, skeletal
            dysplasia, and prenatal cardiomyopathy associated with a pathogenic
            TAB2 variant in a 3-generation family.
REFERENCE   4  (residues 1 to 661)
  AUTHORS   Ciuffa,R., Uliana,F., Mannion,J., Mehnert,M., Tenev,T., Marulli,C.,
            Satanowski,A., Keller,L.M.L., Rodilla Ramirez,P.N., Ori,A.,
            Gstaiger,M., Meier,P. and Aebersold,R.
  TITLE     Novel biochemical, structural, and systems insights into
            inflammatory signaling revealed by contextual interaction
            proteomics
  JOURNAL   Proc Natl Acad Sci U S A 119 (40), e2117175119 (2022)
   PUBMED   36179048
REFERENCE   5  (residues 1 to 661)
  AUTHORS   Liu,H., Zhang,H., Fan,H., Tang,S. and Weng,J.
  TITLE     TAB2 Promotes the Biological Functions of Head and Neck Squamous
            Cell Carcinoma Cells via EMT and PI3K Pathway
  JOURNAL   Dis Markers 2022, 1217918 (2022)
   PUBMED   35978886
  REMARK    GeneRIF: TAB2 Promotes the Biological Functions of Head and Neck
            Squamous Cell Carcinoma Cells via EMT and PI3K Pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 661)
  AUTHORS   Takaesu,G., Kishida,S., Hiyama,A., Yamaguchi,K., Shibuya,H.,
            Irie,K., Ninomiya-Tsuji,J. and Matsumoto,K.
  TITLE     TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK
            by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
  JOURNAL   Mol Cell 5 (4), 649-658 (2000)
   PUBMED   10882101
REFERENCE   7  (residues 1 to 661)
  AUTHORS   Mercurio,F., Zhu,H., Murray,B.W., Shevchenko,A., Bennett,B.L.,
            Li,J., Young,D.B., Barbosa,M., Mann,M., Manning,A. and Rao,A.
  TITLE     IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for
            NF-kappaB activation
  JOURNAL   Science 278 (5339), 860-866 (1997)
   PUBMED   9346484
REFERENCE   8  (residues 1 to 661)
  AUTHORS   Deacon,K. and Blank,J.L.
  TITLE     Characterization of the mitogen-activated protein kinase kinase 4
            (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated
            by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not
            cause activation of p38 kinase in vivo
  JOURNAL   J Biol Chem 272 (22), 14489-14496 (1997)
   PUBMED   9162092
REFERENCE   9  (residues 1 to 661)
  AUTHORS   Shibuya,H., Yamaguchi,K., Shirakabe,K., Tonegawa,A., Gotoh,Y.,
            Ueno,N., Irie,K., Nishida,E. and Matsumoto,K.
  TITLE     TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
            transduction
  JOURNAL   Science 272 (5265), 1179-1182 (1996)
   PUBMED   8638164
REFERENCE   10 (residues 1 to 661)
  AUTHORS   Kunsch,C., Ruben,S.M. and Rosen,C.A.
  TITLE     Selection of optimal kappa B/Rel DNA-binding motifs: interaction of
            both subunits of NF-kappa B with DNA is required for
            transcriptional activation
  JOURNAL   Mol Cell Biol 12 (10), 4412-4421 (1992)
   PUBMED   1406630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX645362.1, AK295750.1 and
            BC035910.2.
            
            Summary: The protein encoded by this gene is an activator of
            MAP3K7/TAK1, which is required for for the IL-1 induced activation
            of nuclear factor kappaB and MAPK8/JNK. This protein forms a kinase
            complex with TRAF6, MAP3K7 and TAB1, and it thus serves as an
            adaptor that links MAP3K7 and TRAF6. This protein, along with TAB1
            and MAP3K7, also participates in the signal transduction induced by
            TNFSF11/RANKl through the activation of the receptor activator of
            NF-kappaB (TNFRSF11A/RANK), which may regulate the development and
            function of osteoclasts. Studies of the related mouse protein
            indicate that it functions to protect against liver damage caused
            by chemical stressors. Mutations in this gene cause congenital
            heart defects, multiple types, 2 (CHTD2). Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, May
            2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AK295750.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA2145245,
                                    SAMEA2145743 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..661
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.1"
     Protein         1..661
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 2 isoform b"
                     /note="TAK1-binding protein 2; mitogen-activated protein
                     kinase kinase kinase 7-interacting protein 2"
                     /calculated_mol_wt=72674
     Region          508..>587
                     /region_name="COG4372"
                     /note="Uncharacterized protein, contains DUF3084 domain
                     [Function unknown]"
                     /db_xref="CDD:443500"
     Region          635..658
                     /region_name="ZnF_RBZ"
                     /note="Zinc finger domain; smart00547"
                     /db_xref="CDD:197784"
     Region          636..655
                     /region_name="RanBP2-type Zn finger"
                     /note="RanBP2-type Zn finger [structural motif]"
                     /db_xref="CDD:275376"
     CDS             1..661
                     /gene="TAB2"
                     /gene_synonym="CHTD2; MAP3K7IP2; TAB-2"
                     /coded_by="NM_001292035.3:308..2293"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:23118"
                     /db_xref="HGNC:HGNC:17075"
                     /db_xref="MIM:605101"
ORIGIN      
        1 mqnnnnldac cavlsqestr ylygegdlnf sddsgisglr nhmtslnldl qsqniyhhgr
       61 egsrmngsrt lthsisdgql qggqsnself qqepqtapaq vpqgfnvfgm ssssgasnsa
      121 phlgfhlgsk gtsslsqqtp rfnpimvtla pniqtgrntp tslhihgvpp pvlnspqgns
      181 iyirpyittp ggttrqtqqh sgwvsqfnpm npqqvyqpsq pgpwttcpas nplshtssqq
      241 pnqqghqtsh vympissptt sqpptihssg ssqssahsqy niqnistgpr knqieiklep
      301 pqrnnssklr ssgprtssts ssvnsqtlnr nqptvyiaas ppntdelmsr sqpkvyisan
      361 aatgdeqvmr nqptlfistn sgasaasrnm sgqvsmgpaf ihhhppksra ignnsatspr
      421 vvvtqpntky tfkitvspnk ppavspgvvs ptfeltnlln hpdhyveten iqhltdptla
      481 hvdrisetrk lsmgsddaay tqallvhqka rmerlqrele iqkkkldklk sevnemennl
      541 trrrlkrsns isqipsleem qqlrscnrql qididcltke idlfqargph fnpsaihnfy
      601 dnigfvgpvp pkpkdqrsii ktpktqdted degaqwncta ctflnhpali rceqcemprh
      661 f
//
LOCUS       NP_110392                378 aa            linear   PRI 20-NOV-2025
DEFINITION  N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 4
            isoform 1 [Homo sapiens].
ACCESSION   NP_110392
VERSION     NP_110392.1
DBSOURCE    REFSEQ: accession NM_030765.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   Kottgen,A., Albrecht,E., Teumer,A., Vitart,V., Krumsiek,J.,
            Hundertmark,C., Pistis,G., Ruggiero,D., O'Seaghdha,C.M., Haller,T.,
            Yang,Q., Tanaka,T., Johnson,A.D., Kutalik,Z., Smith,A.V., Shi,J.,
            Struchalin,M., Middelberg,R.P., Brown,M.J., Gaffo,A.L., Pirastu,N.,
            Li,G., Hayward,C., Zemunik,T., Huffman,J., Yengo,L., Zhao,J.H.,
            Demirkan,A., Feitosa,M.F., Liu,X., Malerba,G., Lopez,L.M., van der
            Harst,P., Li,X., Kleber,M.E., Hicks,A.A., Nolte,I.M., Johansson,A.,
            Murgia,F., Wild,S.H., Bakker,S.J., Peden,J.F., Dehghan,A.,
            Steri,M., Tenesa,A., Lagou,V., Salo,P., Mangino,M., Rose,L.M.,
            Lehtimaki,T., Woodward,O.M., Okada,Y., Tin,A., Muller,C.,
            Oldmeadow,C., Putku,M., Czamara,D., Kraft,P., Frogheri,L.,
            Thun,G.A., Grotevendt,A., Gislason,G.K., Harris,T.B., Launer,L.J.,
            McArdle,P., Shuldiner,A.R., Boerwinkle,E., Coresh,J., Schmidt,H.,
            Schallert,M., Martin,N.G., Montgomery,G.W., Kubo,M., Nakamura,Y.,
            Tanaka,T., Munroe,P.B., Samani,N.J., Jacobs,D.R. Jr., Liu,K.,
            D'Adamo,P., Ulivi,S., Rotter,J.I., Psaty,B.M., Vollenweider,P.,
            Waeber,G., Campbell,S., Devuyst,O., Navarro,P., Kolcic,I.,
            Hastie,N., Balkau,B., Froguel,P., Esko,T., Salumets,A., Khaw,K.T.,
            Langenberg,C., Wareham,N.J., Isaacs,A., Kraja,A., Zhang,Q.,
            Wild,P.S., Scott,R.J., Holliday,E.G., Org,E., Viigimaa,M.,
            Bandinelli,S., Metter,J.E., Lupo,A., Trabetti,E., Sorice,R.,
            Doring,A., Lattka,E., Strauch,K., Theis,F., Waldenberger,M.,
            Wichmann,H.E., Davies,G., Gow,A.J., Bruinenberg,M., Stolk,R.P.,
            Kooner,J.S., Zhang,W., Winkelmann,B.R., Boehm,B.O., Lucae,S.,
            Penninx,B.W., Smit,J.H., Curhan,G., Mudgal,P., Plenge,R.M.,
            Portas,L., Persico,I., Kirin,M., Wilson,J.F., Mateo Leach,I., van
            Gilst,W.H., Goel,A., Ongen,H., Hofman,A., Rivadeneira,F.,
            Uitterlinden,A.G., Imboden,M., von Eckardstein,A., Cucca,F.,
            Nagaraja,R., Piras,M.G., Nauck,M., Schurmann,C., Budde,K.,
            Ernst,F., Farrington,S.M., Theodoratou,E., Prokopenko,I.,
            Stumvoll,M., Jula,A., Perola,M., Salomaa,V., Shin,S.Y.,
            Spector,T.D., Sala,C., Ridker,P.M., Kahonen,M., Viikari,J.,
            Hengstenberg,C., Nelson,C.P., Meschia,J.F., Nalls,M.A., Sharma,P.,
            Singleton,A.B., Kamatani,N., Zeller,T., Burnier,M., Attia,J.,
            Laan,M., Klopp,N., Hillege,H.L., Kloiber,S., Choi,H., Pirastu,M.,
            Tore,S., Probst-Hensch,N.M., Volzke,H., Gudnason,V., Parsa,A.,
            Schmidt,R., Whitfield,J.B., Fornage,M., Gasparini,P.,
            Siscovick,D.S., Polasek,O., Campbell,H., Rudan,I., Bouatia-Naji,N.,
            Metspalu,A., Loos,R.J., van Duijn,C.M., Borecki,I.B., Ferrucci,L.,
            Gambaro,G., Deary,I.J., Wolffenbuttel,B.H., Chambers,J.C., Marz,W.,
            Pramstaller,P.P., Snieder,H., Gyllensten,U., Wright,A.F., Navis,G.,
            Watkins,H., Witteman,J.C., Sanna,S., Schipf,S., Dunlop,M.G.,
            Tonjes,A., Ripatti,S., Soranzo,N., Toniolo,D., Chasman,D.I.,
            Raitakari,O., Kao,W.H., Ciullo,M., Fox,C.S., Caulfield,M.,
            Bochud,M. and Gieger,C.
  CONSRTM   LifeLines Cohort Study; CARDIoGRAM Consortium; DIAGRAM Consortium;
            ICBP Consortium; MAGIC Consortium
  TITLE     Genome-wide association analyses identify 18 new loci associated
            with serum urate concentrations
  JOURNAL   Nat Genet 45 (2), 145-154 (2013)
   PUBMED   23263486
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Seko,A. and Yamashita,K.
  TITLE     beta1,3-N-Acetylglucosaminyltransferase-7 (beta3Gn-T7) acts
            efficiently on keratan sulfate-related glycans
  JOURNAL   FEBS Lett 556 (1-3), 216-220 (2004)
   PUBMED   14706853
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Shiraishi,N., Natsume,A., Togayachi,A., Endo,T., Akashima,T.,
            Yamada,Y., Imai,N., Nakagawa,S., Koizumi,S., Sekine,S.,
            Narimatsu,H. and Sasaki,K.
  TITLE     Identification and characterization of three novel beta
            1,3-N-acetylglucosaminyltransferases structurally related to the
            beta 1,3-galactosyltransferase family
  JOURNAL   J Biol Chem 276 (5), 3498-3507 (2001)
   PUBMED   11042166
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Amado,M., Almeida,R., Schwientek,T. and Clausen,H.
  TITLE     Identification and characterization of large galactosyltransferase
            gene families: galactosyltransferases for all functions
  JOURNAL   Biochim Biophys Acta 1473 (1), 35-53 (1999)
   PUBMED   10580128
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC048338.29.
            
            Summary: This gene encodes a member of the
            beta-1,3-N-acetylglucosaminyltransferase protein family. The
            encoded enzyme is involved in the biosynthesis of
            poly-N-acetyllactosamine chains and prefers lacto-N-neotetraose as
            a substrate. It is a type II transmembrane protein. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.153308.1, AY358940.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000324189.5/ ENSP00000319636.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..378
                     /product="N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 4 isoform 1"
                     /EC_number="2.4.1.149"
                     /note="beta-1,3-N-acetylglucosaminyltransferase bGn-T4;
                     BGnT-4; beta-1,3-Gn-T4;
                     beta-1,3-N-acetylglucosaminyltransferase 4;
                     N-acetyllactosaminide
                     beta-1,3-N-acetylglucosaminyltransferase 4"
                     /calculated_mol_wt=42179
     Site            29..49
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0J1.1)"
     Region          59..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0J1.1)"
     Region          132..321
                     /region_name="Galactosyl_T"
                     /note="Galactosyltransferase; cl21608"
                     /db_xref="CDD:473923"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9C0J1.1)"
     CDS             1..378
                     /gene="B3GNT4"
                     /gene_synonym="B3GN-T4; beta3Gn-T4"
                     /coded_by="NM_030765.4:191..1327"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9227.1"
                     /db_xref="GeneID:79369"
                     /db_xref="HGNC:HGNC:15683"
                     /db_xref="MIM:605864"
ORIGIN      
        1 mlppqpsaah qgrggrsgll pkgpamlcrl cwlvsyslav lllgcllflr kaakpagdpt
       61 ahqpfwappt prhsrcppnh tvssaslslp srhrlfltyr hcrnfsille psgcskdtfl
      121 llaiksqpgh verraairst wgrvggwarg rqlklvfllg vagsappaql layesrefdd
      181 ilqwdftedf fnltlkelhl qrwvvaacpq ahfmlkgddd vfvhvpnvle fldgwdpaqd
      241 llvgdvirqa lpnrntkvky fippsmyrat hyppyagggg yvmsratvrr lqaimedael
      301 fpiddvfvgm clrrlglspm hhagfktfgi rrpldpldpc lyrglllvhr lsplemwtmw
      361 alvtdeglkc aagpipqr
//
LOCUS       NP_037393                798 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome proliferator-activated receptor gamma coactivator
            1-alpha isoform 2 [Homo sapiens].
ACCESSION   NP_037393
VERSION     NP_037393.1
DBSOURCE    REFSEQ: accession NM_013261.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 798)
  AUTHORS   Liang,F. and Huang,S.
  TITLE     PGC-1alpha inhibits NLRP3 signaling through transcriptional
            activation of POP1 to alleviate inflammation and strengthen
            osteogenic differentiation of lipopolysaccharide-induced human
            periodontal stem cells
  JOURNAL   Prostaglandins Other Lipid Mediat 174, 106853 (2024)
   PUBMED   38763227
  REMARK    GeneRIF: PGC-1alpha inhibits NLRP3 signaling through
            transcriptional activation of POP1 to alleviate inflammation and
            strengthen osteogenic differentiation of lipopolysaccharide-induced
            human periodontal stem cells.
REFERENCE   2  (residues 1 to 798)
  AUTHORS   Kuang,J., Fang,J., Hu,S., Yang,X. and Fan,X.
  TITLE     MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS OF
            SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF PGC-1Alpha
  JOURNAL   Shock 62 (3), 426-436 (2024)
   PUBMED   38888503
  REMARK    GeneRIF: MECHANISM OF MICRORNA-218-5P IN MITOCHONDRIAL BIOGENESIS
            OF SEPSIS-INDUCED ACUTE KIDNEY INJURY BY THE REGULATION OF
            PGC-1Alpha.
REFERENCE   3  (residues 1 to 798)
  AUTHORS   Mesarosova,L., Scheper,M., Iyer,A., Anink,J.J., Mills,J.D. and
            Aronica,E.
  TITLE     miR-193b-3p/ PGC-1alpha pathway regulates an insulin dependent
            anti-inflammatory response in Parkinson's disease
  JOURNAL   Neurobiol Dis 199, 106587 (2024)
   PUBMED   38950713
  REMARK    GeneRIF: miR-193b-3p/ PGC-1alpha pathway regulates an insulin
            dependent anti-inflammatory response in Parkinson's disease.
REFERENCE   4  (residues 1 to 798)
  AUTHORS   Yu,T., Gao,Q., Zhang,G., Li,T., Liu,X., Li,C., Zheng,L., Sun,X.,
            Wu,J., Cao,H., Bi,F., Wang,R., Liang,H., Li,X., Zhou,Y., Lv,L. and
            Shan,H.
  TITLE     lncRNA Gm20257 alleviates pathological cardiac hypertrophy by
            modulating the PGC-1alpha-mitochondrial complex IV axis
  JOURNAL   Front Med 18 (4), 664-677 (2024)
   PUBMED   38926249
  REMARK    GeneRIF: lncRNA Gm20257 alleviates pathological cardiac hypertrophy
            by modulating the PGC-1alpha-mitochondrial complex IV axis.
REFERENCE   5  (residues 1 to 798)
  AUTHORS   Zhou,S., Taskintuna,K., Hum,J., Gulati,J., Olaya,S., Steinman,J.
            and Golestaneh,N.
  TITLE     PGC-1alpha repression dysregulates lipid metabolism and induces
            lipid droplet accumulation in retinal pigment epithelium
  JOURNAL   Cell Death Dis 15 (6), 385 (2024)
   PUBMED   38824126
  REMARK    GeneRIF: PGC-1alpha repression dysregulates lipid metabolism and
            induces lipid droplet accumulation in retinal pigment epithelium.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 798)
  AUTHORS   Esterbauer,H., Oberkofler,H., Krempler,F. and Patsch,W.
  TITLE     Human peroxisome proliferator activated receptor gamma coactivator
            1 (PPARGC1) gene: cDNA sequence, genomic organization, chromosomal
            localization, and tissue expression
  JOURNAL   Genomics 62 (1), 98-102 (1999)
   PUBMED   10585775
REFERENCE   7  (residues 1 to 798)
  AUTHORS   Puigserver,P., Adelmant,G., Wu,Z., Fan,M., Xu,J., O'Malley,B. and
            Spiegelman,B.M.
  TITLE     Activation of PPARgamma coactivator-1 through transcription factor
            docking
  JOURNAL   Science 286 (5443), 1368-1371 (1999)
   PUBMED   10558993
REFERENCE   8  (residues 1 to 798)
  AUTHORS   Wu,Z., Puigserver,P., Andersson,U., Zhang,C., Adelmant,G.,
            Mootha,V., Troy,A., Cinti,S., Lowell,B., Scarpulla,R.C. and
            Spiegelman,B.M.
  TITLE     Mechanisms controlling mitochondrial biogenesis and respiration
            through the thermogenic coactivator PGC-1
  JOURNAL   Cell 98 (1), 115-124 (1999)
   PUBMED   10412986
REFERENCE   9  (residues 1 to 798)
  AUTHORS   Puigserver,P., Wu,Z., Park,C.W., Graves,R., Wright,M. and
            Spiegelman,B.M.
  TITLE     A cold-inducible coactivator of nuclear receptors linked to
            adaptive thermogenesis
  JOURNAL   Cell 92 (6), 829-839 (1998)
   PUBMED   9529258
REFERENCE   10 (residues 1 to 798)
  AUTHORS   Spanos,N.P., Spillane,J. and McPeake,J.D.
  TITLE     Cognitive strategies and response to suggestion in hypnotic and
            task-motivated subjects
  JOURNAL   Am J Clin Hypn 18 (4), 254-262 (1976)
   PUBMED   1258810
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF106698.1, AC092834.3,
            AF186379.1 and BM976883.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is a transcriptional
            coactivator that regulates the genes involved in energy metabolism.
            This protein interacts with PPARgamma, which permits the
            interaction of this protein with multiple transcription factors.
            This protein can interact with, and regulate the activities of,
            cAMP response element binding protein (CREB) and nuclear
            respiratory factors (NRFs). It provides a direct link between
            external physiological stimuli and the regulation of mitochondrial
            biogenesis, and is a major factor that regulates muscle fiber type
            determination. This protein may be also involved in controlling
            blood pressure, regulating cellular cholesterol homoeostasis, and
            the development of obesity. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) has a distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF106698.1, SRR11853560.21849.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264867.7/ ENSP00000264867.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..798
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.2"
     Protein         1..798
                     /product="peroxisome proliferator-activated receptor gamma
                     coactivator 1-alpha isoform 2"
                     /note="ligand effect modulator-6; L-PGC-1alpha; PPAR gamma
                     coactivator variant form; PGC-1-alpha; PPARGC-1-alpha;
                     PPARAGCIalpha; PPARgamma coactivator 1alpha"
                     /calculated_mol_wt=90896
     Site            79
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          100..140
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          144..148
                     /region_name="LXXLL motif.
                     /evidence=ECO:0000250|UniProtKB:O70343"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            184
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          213..277
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            254
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            271
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            278
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          290..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          293..339
                     /region_name="Interaction with PPARG.
                     /evidence=ECO:0000269|PubMed:10713165"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            347
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          350..798
                     /region_name="Mediates interaction with RNF34.
                     /evidence=ECO:0000269|PubMed:22064484"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            413
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            442
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            451
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          542..599
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          613..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          636..671
                     /region_name="Complexin_NTD"
                     /note="N-terminal SNARE complex binding domain of the
                     complexin family of SNARE regulators; cl45908"
                     /db_xref="CDD:459253"
     Region          650..669
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Region          675..765
                     /region_name="RRM_PPARGC1A"
                     /note="RNA recognition motif (RRM) found in peroxisome
                     proliferator-activated receptor gamma coactivator 1-alpha
                     (PGC-1alpha, or PPARGC-1-alpha) and similar proteins;
                     cd12623"
                     /db_xref="CDD:410034"
     Site            758
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     Site            779
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:O70343; propagated from
                     UniProtKB/Swiss-Prot (Q9UBK2.1)"
     CDS             1..798
                     /gene="PPARGC1A"
                     /gene_synonym="LEM6; PGC-1(alpha); PGC-1alpha; PGC-1v;
                     PGC1; PGC1A; PPARGC1"
                     /coded_by="NM_013261.5:91..2487"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3429.1"
                     /db_xref="GeneID:10891"
                     /db_xref="HGNC:HGNC:9237"
                     /db_xref="MIM:604517"
ORIGIN      
        1 mawdmcnqds esvwsdieca alvgedqplc pdlpeldlse ldvndldtds flgglkwcsd
       61 qseiisnqyn nepsnifeki deeneanlla vltetldslp vdedglpsfd altdgdvttd
      121 neaspssmpd gtpppqeaee psllkkllla pantqlsyne csglstqnha nhnhrirtnp
      181 aivktensws nkaksicqqq kpqrrpcsel lkylttnddp phtkptenrn ssrdkctskk
      241 kshtqsqsqh lqakpttlsl pltpespndp kgspfenkti ertlsvelsg tagltppttp
      301 phkanqdnpf raspklkssc ktvvpppskk prysessgtq gnnstkkgpe qselyaqlsk
      361 ssvltgghee rktkrpslrl fgdhdycqsi nskteilini sqelqdsrql enkdvssdwq
      421 gqicsstdsd qcylretlea skqvspcstr kqlqdqeira elnkhfghps qavfddeadk
      481 tgelrdsdfs neqfsklpmf insglamdgl fddsedesdk lsypwdgtqs yslfnvspsc
      541 ssfnspcrds vsppkslfsq rpqrmrsrsr sfsrhrscsr spysrsrsrs pgsrsssrsc
      601 yyyesshyrh rthrnsplyv rsrsrspysr rprydsyeey qherlkreey rreyekrese
      661 rakqrerqrq kaieerrviy vgkirpdttr telrdrfevf geieectvnl rddgdsygfi
      721 tyrytcdafa alengytlrr snetdfelyf cgrkqffksn yadldsnsdd fdpastksky
      781 dsldfdsllk eaqrslrr
//
LOCUS       NP_001341228            1460 aa            linear   PRI 20-NOV-2025
DEFINITION  GTPase-activating protein and VPS9 domain-containing protein 1
            isoform 2 [Homo sapiens].
ACCESSION   NP_001341228 XP_016870093
VERSION     NP_001341228.1
DBSOURCE    REFSEQ: accession NM_001354299.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1460)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1460)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1460)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1460)
  AUTHORS   Khademi,B., Khorrami,M., Ayromlou,H., Rikhtegar,R., Moghadam,E.A.,
            Tahmasebivand,M., Mousavi,S.R., Kheirollahi,M., Fakhr,F.,
            Alizadeh-Ghodsi,M. and Emamalizadeh,B.
  TITLE     An interdependence between GAPVD1 gene polymorphism, expression
            level and response to interferon beta in patients with multiple
            sclerosis
  JOURNAL   J Neuroimmunol 353, 577507 (2021)
   PUBMED   33548618
  REMARK    GeneRIF: An interdependence between GAPVD1 gene polymorphism,
            expression level and response to interferon beta in patients with
            multiple sclerosis.
REFERENCE   5  (residues 1 to 1460)
  AUTHORS   Ibrahim,H., Reus,P., Mundorf,A.K., Grothoff,A.L., Rudenko,V.,
            Buschhaus,C., Stefanski,A., Berleth,N., Stork,B., Stuhler,K.,
            Kalfalah,F. and Reinke,H.
  TITLE     Phosphorylation of GAPVD1 Is Regulated by the PER Complex and
            Linked to GAPVD1 Degradation
  JOURNAL   Int J Mol Sci 22 (7), 3787 (2021)
   PUBMED   33917494
  REMARK    GeneRIF: Phosphorylation of GAPVD1 Is Regulated by the PER Complex
            and Linked to GAPVD1 Degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1460)
  AUTHORS   Kim,H., Oh,H., Oh,Y.S., Bae,J., Hong,N.H., Park,S.J., Ahn,S.,
            Lee,M., Rhee,S., Lee,S.H., Jun,Y., Kim,S.H., Huh,Y.H. and Song,W.K.
  TITLE     SPIN90, an adaptor protein, alters the proximity between Rab5 and
            Gapex5 and facilitates Rab5 activation during EGF endocytosis
  JOURNAL   Exp Mol Med 51 (7), 1-14 (2019)
   PUBMED   31358736
  REMARK    GeneRIF: The findings suggest that SPIN90, as an adaptor protein,
            simultaneously binds inactive Rab5 and Gapex5, thereby altering
            their spatial proximity and facilitating Rab5 activation.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1460)
  AUTHORS   Guo,Z., Neilson,L.J., Zhong,H., Murray,P.S., Zanivan,S. and
            Zaidel-Bar,R.
  TITLE     E-cadherin interactome complexity and robustness resolved by
            quantitative proteomics
  JOURNAL   Sci Signal 7 (354), rs7 (2014)
   PUBMED   25468996
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 1460)
  AUTHORS   Su,X., Kong,C. and Stahl,P.D.
  TITLE     GAPex-5 mediates ubiquitination, trafficking, and degradation of
            epidermal growth factor receptor
  JOURNAL   J Biol Chem 282 (29), 21278-21284 (2007)
   PUBMED   17545148
  REMARK    GeneRIF: EGF-stimulated receptor ubiquitination and trafficking are
            mediated via GAPex-5: GAPex-5-mediated EGFR ubiquitination is
            independent of Rab5 activation
REFERENCE   9  (residues 1 to 1460)
  AUTHORS   Hunker,C.M., Galvis,A., Kruk,I., Giambini,H., Veisaga,M.L. and
            Barbieri,M.A.
  TITLE     Rab5-activating protein 6, a novel endosomal protein with a role in
            endocytosis
  JOURNAL   Biochem Biophys Res Commun 340 (3), 967-975 (2006)
   PUBMED   16410077
REFERENCE   10 (residues 1 to 1460)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL354710.17 and AL627223.23.
            
            On Aug 11, 2017 this sequence version replaced XP_016870093.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.17548.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2151119
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..1460
                     /product="GTPase-activating protein and VPS9
                     domain-containing protein 1 isoform 2"
                     /note="GTPase-activating protein and VPS9
                     domain-containing protein 1; Rab5-activating protein 6;
                     Rab5 exchange factor"
                     /calculated_mol_wt=162767
     Region          84..449
                     /region_name="RasGAP_RAP6"
                     /note="Ras-GTPase Activating Domain of Rab5-activating
                     protein 6; cd05129"
                     /db_xref="CDD:213331"
     Site            order(129,168,170,172..173,179,182,186,304,312..313,
                     316..317,320,342,345..346,349,353,355,359..360)
                     /site_type="other"
                     /note="putative Rab5 interface [polypeptide binding]"
                     /db_xref="CDD:213331"
     Site            172
                     /site_type="other"
                     /note="Arginine finger, crucial for GTP hydrolysis by
                     stabilizing the transition state.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00167; propagated
                     from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            466
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            566
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            569
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          574..608
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          739..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            757
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            762
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          846..874
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            876
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          889..1023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            902
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            903
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            966
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1019
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1046
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PAR5; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1078
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:32356940; propagated from
                     UniProtKB/Swiss-Prot (Q14C86.2)"
     Region          1245..1308
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          1356..1457
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..1460
                     /gene="GAPVD1"
                     /gene_synonym="GAPex-5; GAPEX5; RAP6"
                     /coded_by="NM_001354299.2:425..4807"
                     /note="isoform 2 is encoded by transcript variant 13"
                     /db_xref="CCDS:CCDS65131.1"
                     /db_xref="GeneID:26130"
                     /db_xref="HGNC:HGNC:23375"
                     /db_xref="MIM:611714"
ORIGIN      
        1 mvkldihtla hhlkqerlyv nsekqliqrl nadvlktaek lyrtawiakq qrinldrlii
       61 tsaeaspaec cqhakiledt qfvdgykqlg fqetaygefl srlrenprli asslvagekl
      121 nqentqsviy tvftslygnc imqedesyll qvlryliefe lkesdnprrl lrrgtcafsi
      181 lfklfseglf saklfltatl hepimqllve dedhletdpn klierfspsq qeklfgekgs
      241 drfrqkvqem vesneaklva lvnkfigylk qntycfphsl rwivsqmykt lscvdrlevg
      301 evramctdll lacficpavv npeqygiisd apinevarfn lmqvgrllqq lamtgseegd
      361 prtksslgkf dkscvaafld vviggravet pplssvnlle glsrtvvyit ysqlitlvnf
      421 mksvmsgdql redrmaldnl lanlppakpg kssslemtpy ntpqlspatt pankknrlpi
      481 atrsrsrtnm lmdlhmdheg ssqetiqevq peevlvislg tgpqltpgmm senevlnmql
      541 sdggqgdvpv denklhgkpd ktlrfslcsd nlegisegps nrsnsvssld legesvselg
      601 agpsgsngve alqlleheqa ttqdnlddkl rkfeirdmmg ltddrdiset vsetwstdvl
      661 gsdfdpnide drlqeiagaa aenmlgsllc lpgsgsvlld pctgstiset tseawsvevl
      721 psdseapdlk qeerlqeles csglgstsdd tdvrevssrp stpglsvvsg isatsedipn
      781 kiedlrsecs sdfggkdsvt spdmdeithg ahqltsppsq sesllamfdp lsshegasav
      841 vrpkvhyarp shpppdppil egavggnear lpnfgshvlt paemeafkqr hsyperlvrs
      901 rssdivssvr rpmsdpswnr rpgneerelp paaaigatsl vaaphsssss pskdssrget
      961 eerkdsddek sdrnrpwwrk rfvsampkap ipfrkkekqe kdkddlgpdr fstltddpsp
     1021 rlsaqaqvae dildkyrnai krtspsdgam anyestevmg dgesahdspr dealqnisad
     1081 dlpdsasqaa hpqdsafsyr dakkklrlal csadsvafpv lthstrnglp dhtdpednei
     1141 vcflkvqiae ainlqdknlm aqlqetmrcv crfdnrtcrk llasiaedyr krapyiaylt
     1201 rcrqglqttq ahlerllqrv lrdkevanry fttvcvrlll eskekkiref iqdfqkltaa
     1261 ddktaqvedf lqflygamaq dviwqnasee qlqdaqlaie rsvmnrifkl afypnqdgdi
     1321 lrdqvlhehi qrlskvvtan hralqipevy lreapwpsaq seirtisayk tprdkvqcil
     1381 rmcstimnll slanedsvpg addfvpvlvf vlikanppcl lstvqyissf yasclsgees
     1441 ywwmqftaav efiktiddrk
//
LOCUS       NP_005149               1167 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform c [Homo sapiens].
ACCESSION   NP_005149 NP_001093578
VERSION     NP_005149.4
DBSOURCE    REFSEQ: accession NM_005158.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1167)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1167)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1167)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1167)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1167)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1167)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1167)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1167)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1167)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1167)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX538317.1, BC065912.1,
            AL359179.18, AL139132.16 and BQ014912.1.
            
            On or before Nov 24, 2009 this sequence version replaced
            NP_001093578.1, NP_005149.3.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (c) differs in the 5' UTR and 5'
            coding region, compared to variant b, resulting in an isoform (c,
            also known as 1ALCTL) with a distinct and shorter N-terminus,
            compared to isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC065912.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1167
                     /product="tyrosine-protein kinase ABL2 isoform c"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=126554
     Region          96..149
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(101,103,106..108,110,125,129..130,141,143,145..146)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            order(105..108,127,129)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Region          154..247
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            order(165,193,206)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Region          266..528
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(279,281..283,300,302,347,349,353,401,412,430..432,
                     434,442,476,480)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(279,281,284,300,302,317,321,330,346..347,349,353,
                     401,411..412)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            order(294..295,325..327,331,373,405..406,524..525)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(371..372,375,460,463..464,493..494)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            411..435
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Site            order(430..432,434,442,476,480)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Region          1048..1167
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1167
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_005158.5:33..3536"
                     /note="isoform c is encoded by transcript variant c"
                     /db_xref="CCDS:CCDS41441.2"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mvlgtvllpp nsygrdqdts lcclctease salpdltdhf ascvedgfeg dktggsspea
       61 lhrpygcdve pqalneairw sskenllgat esdpnlfval ydfvasgdnt lsitkgeklr
      121 vlgynqngew sevrskngqg wvpsnyitpv nslekhswyh gpvsrsaaey llsslingsf
      181 lvresesspg qlsislryeg rvyhyrintt adgkvyvtae srfstlaelv hhhstvadgl
      241 vttlhypapk cnkptvygvs pihdkwemer tditmkhklg ggqygevyvg vwkkysltva
      301 vktlkedtme veeflkeaav mkeikhpnlv qllgvctlep pfyivteymp ygnlldylre
      361 cnreevtavv llymatqiss ameylekknf ihrdlaarnc lvgenhvvkv adfglsrlmt
      421 gdtytahaga kfpikwtape slayntfsik sdvwafgvll weiatygmsp ypgidlsqvy
      481 dllekgyrme qpegcppkvy elmracwkws padrpsfaet hqafetmfhd ssiseevaee
      541 lgraassssv vpylprlpil psktrtlkkq venkeniega qdatensass lapgfirgaq
      601 assgspalpr kqrdkspssl ledaketcft rdrkggffss fmkkrnaptp pkrsssfrem
      661 enqphkkyel tgnfssvasl qhadgfsftp aqqeanlvpp kcyggsfaqr nlcnddgggg
      721 ggsgtagggw sgitgfftpr likktlglra gkptasddts kpfprsnsts smssglpeqd
      781 rmamtlprnc qrsklqlert vstssqpeen vdrandmlpk kseesaapsr erpkakllpr
      841 gatalplrtp sgdlaitekd ppgvgvagva aapkgkekng garlgmagvp edgeqpgwps
      901 pakaapvlpt thnhkvpvli sptlkhtpad vqligtdsqg nkfkllsehq vtssgdkdrp
      961 rrvkpkcapp pppvmrllqh psicsdptee ptaltagqst setqeggkka algavpisgk
     1021 agrpvmpppq vplptssisp akmangtagt kvalrktkqa aekisadkis keallecadl
     1081 lssaltepvp nsqlvdtghq lldycsgyvd cipqtrnkfa freavsklel slqelqvssa
     1141 aagvpgtnpv lnnllscvqe isdvvqr
//
LOCUS       NP_001341831            2752 aa            linear   PRI 20-NOV-2025
DEFINITION  adenomatous polyposis coli protein isoform i [Homo sapiens].
ACCESSION   NP_001341831
VERSION     NP_001341831.1
DBSOURCE    REFSEQ: accession NM_001354902.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2752)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 2752)
  AUTHORS   Song,J., Ke,B. and Fang,X.
  TITLE     APC and ZBTB2 May Mediate M2 Macrophage Infiltration to Promote the
            Development of Renal Fibrosis: A Bioinformatics Analysis
  JOURNAL   Biomed Res Int 2024, 5674711 (2024)
   PUBMED   39328595
  REMARK    GeneRIF: APC and ZBTB2 May Mediate M2 Macrophage Infiltration to
            Promote the Development of Renal Fibrosis: A Bioinformatics
            Analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2752)
  AUTHORS   Arteaga-Blanco,L.A., Evans,A.E. and Dixon,D.A.
  TITLE     Plasma-Derived Extracellular Vesicles and Non-Extracellular Vesicle
            Components from APCMin/+ Mice Promote Pro-Tumorigenic Activities
            and Activate Human Colonic Fibroblasts via the NF-kappaB Signaling
            Pathway
  JOURNAL   Cells 13 (14), 1195 (2024)
   PUBMED   39056778
  REMARK    GeneRIF: Plasma-Derived Extracellular Vesicles and
            Non-Extracellular Vesicle Components from APC[Min/+] Mice Promote
            Pro-Tumorigenic Activities and Activate Human Colonic Fibroblasts
            via the NF-kappaB Signaling Pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2752)
  AUTHORS   Lambertz,S. and Ballhausen,W.G.
  TITLE     Identification of an alternative 5' untranslated region of the
            adenomatous polyposis coli gene
  JOURNAL   Hum Genet 90 (6), 650-652 (1993)
   PUBMED   8383094
REFERENCE   5  (residues 1 to 2752)
  AUTHORS   Yen,T., Stanich,P.P., Axell,L. and Patel,S.G.
  TITLE     APC-Associated Polyposis Conditions
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301519
REFERENCE   6  (residues 1 to 2752)
  AUTHORS   Nakatsuru,S., Yanagisawa,A., Ichii,S., Tahara,E., Kato,Y.,
            Nakamura,Y. and Horii,A.
  TITLE     Somatic mutation of the APC gene in gastric cancer: frequent
            mutations in very well differentiated adenocarcinoma and
            signet-ring cell carcinoma
  JOURNAL   Hum Mol Genet 1 (8), 559-563 (1992)
   PUBMED   1338691
REFERENCE   7  (residues 1 to 2752)
  AUTHORS   Miki,Y., Nishisho,I., Horii,A., Miyoshi,Y., Utsunomiya,J.,
            Kinzler,K.W., Vogelstein,B. and Nakamura,Y.
  TITLE     Disruption of the APC gene by a retrotransposal insertion of L1
            sequence in a colon cancer
  JOURNAL   Cancer Res 52 (3), 643-645 (1992)
   PUBMED   1310068
REFERENCE   8  (residues 1 to 2752)
  AUTHORS   Nagase,H., Miyoshi,Y., Horii,A., Aoki,T., Petersen,G.M.,
            Vogelstein,B., Maher,E., Ogawa,M., Maruyama,M., Utsunomiya,J. et
            al.
  TITLE     Screening for germ-line mutations in familial adenomatous polyposis
            patients: 61 new patients and a summary of 150 unrelated patients
  JOURNAL   Hum Mutat 1 (6), 467-473 (1992)
   PUBMED   1338764
REFERENCE   9  (residues 1 to 2752)
  AUTHORS   Nishisho,I., Nakamura,Y., Miyoshi,Y., Miki,Y., Ando,H., Horii,A.,
            Koyama,K., Utsunomiya,J., Baba,S. and Hedge,P.
  TITLE     Mutations of chromosome 5q21 genes in FAP and colorectal cancer
            patients
  JOURNAL   Science 253 (5020), 665-669 (1991)
   PUBMED   1651563
REFERENCE   10 (residues 1 to 2752)
  AUTHORS   Kinzler,K.W., Nilbert,M.C., Su,L.K., Vogelstein,B., Bryan,T.M.,
            Levy,D.B., Smith,K.J., Preisinger,A.C., Hedge,P., McKechnie,D. et
            al.
  TITLE     Identification of FAP locus genes from chromosome 5q21
  JOURNAL   Science 253 (5020), 661-665 (1991)
   PUBMED   1651562
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC136500.1 and AC008575.7.
            
            Summary: This gene encodes a tumor suppressor protein that acts as
            an antagonist of the Wnt signaling pathway. It is also involved in
            other processes including cell migration and adhesion,
            transcriptional activation, and apoptosis. Defects in this gene
            cause familial adenomatous polyposis (FAP), an autosomal dominant
            pre-malignant disease that usually progresses to malignancy.
            Mutations in the APC gene have been found to occur in most
            colorectal cancers, where disease-associated mutations tend to be
            clustered in a small region designated the mutation cluster region
            (MCR) and result in a truncated protein product. [provided by
            RefSeq, Jun 2022].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.253963.1,
                                           SRR1803616.213020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..2752
                     /product="adenomatous polyposis coli protein isoform i"
                     /note="adenomatous polyposis coli protein; WNT signaling
                     pathway regulator; adenomatosis polyposis coli tumor
                     suppressor; deleted in polyposis 2.5; protein phosphatase
                     1, regulatory subunit 46; adenomatous polyposis coli
                     (APC); epididymis secretory sperm binding protein; APC,
                     WNT signaling pathway regulator"
                     /calculated_mol_wt=300756
     Region          137..217
                     /region_name="Suppressor_APC"
                     /note="Adenomatous polyposis coli tumour suppressor
                     protein; pfam11414"
                     /db_xref="CDD:463275"
     Region          <317..375
                     /region_name="APC_rep"
                     /note="Adenomatous polyposis coli (APC) repeat; pfam18797"
                     /db_xref="CDD:465870"
     Region          374..417
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(408,412,416,451,455,459,495,499,503)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          421..462
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          425..462
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          469..504
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          512..553
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          558..598
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          562..596
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          600..640
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          604..640
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          641..928
                     /region_name="Arm_APC_u3"
                     /note="Armadillo-associated region on APC; pfam16629"
                     /db_xref="CDD:435476"
     Region          945..1044
                     /region_name="APC_u5"
                     /note="Unstructured region on APC between 1st and 2nd
                     catenin-bdg motifs; pfam16630"
                     /db_xref="CDD:406923"
     Region          1166..>1183
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1192..1277
                     /region_name="APC_u9"
                     /note="Unstructured region on APC between 1st two
                     creatine-rich regions; pfam16633"
                     /db_xref="CDD:435478"
     Region          <1200..1610
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          1280..1302
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1546..1569
                     /region_name="APC_r"
                     /note="APC repeat; pfam05923"
                     /db_xref="CDD:461781"
     Region          1571..1624
                     /region_name="APC_u13"
                     /note="Unstructured region on APC between APC_crr and
                     SAMP; pfam16634"
                     /db_xref="CDD:406927"
     Region          1625..1646
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          1655..1748
                     /region_name="APC_u14"
                     /note="Unstructured region on APC between SAMP and
                     APC_crr; pfam16635"
                     /db_xref="CDD:435479"
     Region          1782..1856
                     /region_name="APC_u15"
                     /note="Unstructured region on APC between APC_crr regions
                     5 and 6; pfam16636"
                     /db_xref="CDD:435480"
     Region          1942..1961
                     /region_name="SAMP"
                     /note="SAMP Motif; pfam05924"
                     /db_xref="CDD:461782"
     Region          2132..2477
                     /region_name="APC_basic"
                     /note="APC basic domain; pfam05956"
                     /db_xref="CDD:428690"
     Region          2579..2752
                     /region_name="EB1_binding"
                     /note="EB-1 Binding Domain; pfam05937"
                     /db_xref="CDD:399141"
     CDS             1..2752
                     /gene="APC"
                     /gene_synonym="BTPS2; DESMD; DP2; DP2.5; DP3; GS; PPP1R46"
                     /coded_by="NM_001354902.2:221..8479"
                     /note="isoform i is encoded by transcript variant 11"
                     /db_xref="GeneID:324"
                     /db_xref="HGNC:HGNC:583"
                     /db_xref="MIM:611731"
ORIGIN      
        1 myaslgsgpv aplpasvpps vlgswstggs rscvrqetks pggartsghw asvwqevlkq
       61 lqgsiedeam assgqidlle rlkelnldss nfpgvklrsk mslrsygsre gsvssrsgec
      121 spvpmgsfpr rgfvngsres tgyleeleke rsllladldk eekekdwyya qlqnltkrid
      181 slpltenfsl qtdmtrrqle yearqirvam eeqlgtcqdm ekraqrriar iqqiekdilr
      241 irqllqsqat eaerssqnkh etgshdaerq negqgvgein matsgngqgs ttrmdhetas
      301 vlssssthsa prrltshlgt kiraycetcw ewqeahepgm dqdknpmpap vehqicpavc
      361 vlmklsfdee hrhamnelgg lqaiaellqv dcemygltnd hysitlrrya gmaltnltfg
      421 dvankatlcs mkgcmralva qlksesedlq qviasvlrnl swradvnskk tlrevgsvka
      481 lmecalevkk estlksvlsa lwnlsahcte nkadicavdg alaflvgtlt yrsqtntlai
      541 iesgggilrn vssliatned hrqilrennc lqtllqhlks hsltivsnac gtlwnlsarn
      601 pkdqealwdm gavsmlknli hskhkmiamg saaalrnlma nrpakykdan imspgsslps
      661 lhvrkqkale aeldaqhlse tfdnidnlsp kashrskqrh kqslygdyvf dtnrhddnrs
      721 dnfntgnmtv lspylnttvl psssssrgsl dssrsekdrs lerergiglg nyhpatenpg
      781 tsskrglqis ttaaqiakvm eevsaihtsq edrssgstte lhcvtderna lrrssaahth
      841 sntynftkse nsnrtcsmpy akleykrssn dslnsvsssd gygkrgqmkp siesysedde
      901 skfcsygqyp adlahkihsa nhmddndgel dtpinyslky sdeqlnsgrq spsqnerwar
      961 pkhiiedeik qseqrqsrnq sttypvytes tddkhlkfqp hfgqqecvsp yrsrgangse
     1021 tnrvgsnhgi nqnvsqslcq eddyeddkpt nyseryseee qheeeerptn ysikyneekr
     1081 hvdqpidysl kyatdipssq kqsfsfskss sgqssktehm ssssentstp ssnakrqnql
     1141 hpssaqsrsg qpqkaatckv ssinqetiqt ycvedtpicf srcsslssls saedeigcnq
     1201 ttqeadsant lqiaeikeki gtrsaedpvs evpavsqhpr tkssrlqgss lssesarhka
     1261 vefssgaksp sksgaqtpks ppehyvqetp lmfsrctsvs sldsfesrsi assvqsepcs
     1321 gmvsgiisps dlpdspgqtm ppsrsktppp ppqtaqtkre vpknkaptae kresgpkqaa
     1381 vnaavqrvqv lpdadtllhf atestpdgfs cssslsalsl depfiqkdve lrimppvqen
     1441 dngneteseq pkesnenqek eaektidsek dllddsdddd ieileeciis amptkssrka
     1501 kkpaqtaskl pppvarkpsq lpvykllpsq nrlqpqkhvs ftpgddmprv ycvegtpinf
     1561 statslsdlt iesppnelaa gegvrggaqs gefekrdtip tegrstdeaq ggktssvtip
     1621 elddnkaeeg dilaecinsa mpkgkshkpf rvkkimdqvq qasasssapn knqldgkkkk
     1681 ptspvkpipq nteyrtrvrk nadsknnlna ervfsdnkds kkqnlknnsk vfndklpnne
     1741 drvrgsfafd sphhytpieg tpycfsrnds lssldfdddd vdlsrekael rkakenkese
     1801 akvtshtelt snqqsanktq aiakqpinrg qpkpilqkqs tfpqsskdip drgaatdekl
     1861 qnfaientpv cfshnsslss lsdidqennn kenepikete ppdsqgepsk pqasgyapks
     1921 fhvedtpvcf srnsslssls idseddllqe cissampkkk kpsrlkgdne khsprnmggi
     1981 lgedltldlk diqrpdsehg lspdsenfdw kaiqegansi vsslhqaaaa aclsrqassd
     2041 sdsilslksg islgspfhlt pdqeekpfts nkgprilkpg ekstletkki eseskgikgg
     2101 kkvykslitg kvrsnseisg qmkqplqanm psisrgrtmi hipgvrnsss stspvskkgp
     2161 plktpasksp segqtattsp rgakpsvkse lspvarqtsq iggsskapsr sgsrdstpsr
     2221 paqqplsrpi qspgrnsisp grngisppnk lsqlprtssp stastkssgs gkmsytspgr
     2281 qmsqqnltkq tglsknassi prsesaskgl nqmnngngan kkvelsrmss tkssgsesdr
     2341 serpvlvrqs tfikeapspt lrrkleesas feslspssrp asptrsqaqt pvlspslpdm
     2401 slsthssvqa ggwrklppnl sptieyndgr pakrhdiars hsespsrlpi nrsgtwkreh
     2461 skhssslprv stwrrtgsss silsassess ekaksedekh vnsisgtkqs kenqvsakgt
     2521 wrkikenefs ptnstsqtvs sgatngaesk tliyqmapav sktedvwvri edcpinnprs
     2581 grsptgntpp vidsvsekan pnikdskdnq akqnvgngsv pmrtvglenr lnsfiqvdap
     2641 dqkgteikpg qnnpvpvset nessivertp fsssssskhs spsgtvaarv tpfnynpspr
     2701 kssadstsar psqiptpvnn ntkkrdsktd stessgtqsp krhsgsylvt sv
//
LOCUS       NP_005025                 58 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I, II, and III subunit RPABC4 [Homo
            sapiens].
ACCESSION   NP_005025
VERSION     NP_005025.1
DBSOURCE    REFSEQ: accession NM_005034.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 58)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 58)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 58)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 58)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 58)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 58)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   7  (residues 1 to 58)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
REFERENCE   8  (residues 1 to 58)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 58)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 58)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC018157.1 and AC025647.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of the smallest subunits of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. This subunit is shared by the other
            two DNA-directed RNA polymerases. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM807282.1, BG708922.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000353107.8/ ENSP00000342889.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..58
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.2"
     Protein         1..58
                     /product="DNA-directed RNA polymerases I, II, and III
                     subunit RPABC4"
                     /EC_number="2.7.7.6"
                     /note="DNA directed RNA polymerases I, II, and III 7.0 kda
                     polypeptide; polymerase (RNA) II subunit K; RNA polymerase
                     II 7.0 kDa subunit; DNA-directed RNA polymerase II subunit
                     K; RNA polymerases I, II, and III subunit ABC4; polymerase
                     (RNA) II (DNA directed) polypeptide K, 7.0kDa"
                     /calculated_mol_wt=6873
     Region          15..58
                     /region_name="RPOLCX"
                     /note="RNA polymerase subunit CX; smart00659"
                     /db_xref="CDD:128906"
     CDS             1..58
                     /gene="POLR2K"
                     /gene_synonym="ABC10-alpha; hRPB7.0; hsRPB10a; RPABC4;
                     RPB10alpha; RPB12; RPB7.0"
                     /coded_by="NM_005034.4:84..260"
                     /db_xref="CCDS:CCDS6285.1"
                     /db_xref="GeneID:5440"
                     /db_xref="HGNC:HGNC:9198"
                     /db_xref="MIM:606033"
ORIGIN      
        1 mdtqkdvqpp kqqpmiyicg echteneiks rdpircrecg yrimykkrtk rlvvfdar
//
LOCUS       NP_001252525             129 aa            linear   PRI 20-NOV-2025
DEFINITION  prefoldin subunit 6 [Homo sapiens].
ACCESSION   NP_001252525
VERSION     NP_001252525.1
DBSOURCE    REFSEQ: accession NM_001265596.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Frommelt,F., Fossati,A., Uliana,F., Wendt,F., Xue,P., Heusel,M.,
            Wollscheid,B., Aebersold,R., Ciuffa,R. and Gstaiger,M.
  TITLE     DIP-MS: ultra-deep interaction proteomics for the deconvolution of
            protein complexes
  JOURNAL   Nat Methods 21 (4), 635-647 (2024)
   PUBMED   38532014
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Herranz-Montoya,I., Park,S. and Djouder,N.
  TITLE     A comprehensive analysis of prefoldins and their implication in
            cancer
  JOURNAL   iScience 24 (11), 103273 (2021)
   PUBMED   34761191
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Liang,J., Xia,L., Oyang,L., Lin,J., Tan,S., Yi,P., Han,Y., Luo,X.,
            Wang,H., Tang,L., Pan,Q., Tian,Y., Rao,S., Su,M., Shi,Y., Cao,D.,
            Zhou,Y. and Liao,Q.
  TITLE     The functions and mechanisms of prefoldin complex and
            prefoldin-subunits
  JOURNAL   Cell Biosci 10, 87 (2020)
   PUBMED   32699605
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 129)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 129)
  AUTHORS   Simons,C.T., Staes,A., Rommelaere,H., Ampe,C., Lewis,S.A. and
            Cowan,N.J.
  TITLE     Selective contribution of eukaryotic prefoldin subunits to actin
            and tubulin binding
  JOURNAL   J Biol Chem 279 (6), 4196-4203 (2004)
   PUBMED   14634002
REFERENCE   7  (residues 1 to 129)
  AUTHORS   Hansen,W.J., Cowan,N.J. and Welch,W.J.
  TITLE     Prefoldin-nascent chain complexes in the folding of cytoskeletal
            proteins
  JOURNAL   J Cell Biol 145 (2), 265-277 (1999)
   PUBMED   10209023
REFERENCE   8  (residues 1 to 129)
  AUTHORS   Vainberg,I.E., Lewis,S.A., Rommelaere,H., Ampe,C.,
            Vandekerckhove,J., Klein,H.L. and Cowan,N.J.
  TITLE     Prefoldin, a chaperone that delivers unfolded proteins to cytosolic
            chaperonin
  JOURNAL   Cell 93 (5), 863-873 (1998)
   PUBMED   9630229
REFERENCE   9  (residues 1 to 129)
  AUTHORS   Herberg,J.A., Beck,S. and Trowsdale,J.
  TITLE     TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form
            a dense cluster at the centromeric end of the MHC
  JOURNAL   J Mol Biol 277 (4), 839-857 (1998)
   PUBMED   9545376
REFERENCE   10 (residues 1 to 129)
  AUTHORS   Herberg,J.A., Sgouros,J., Jones,T., Copeman,J., Humphray,S.J.,
            Sheer,D., Cresswell,P., Beck,S. and Trowsdale,J.
  TITLE     Genomic analysis of the Tapasin gene, located close to the TAP loci
            in the MHC
  JOURNAL   Eur J Immunol 28 (2), 459-467 (1998)
   PUBMED   9521053
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM745352.1, DA256816.1 and BE794658.1.
            
            Summary: PFDN6 is a subunit of the heteromeric prefoldin complex
            that chaperones nascent actin (see MIM 102560) and alpha- and
            beta-tubulin (see MIM 602529 and MIM 191130, respectively) chains
            pending their transfer to the cytosolic chaperonin containing TCP1
            (MIM 186980) (CCT) complex (Hansen et al., 1999 [PubMed
            10209023]).[supplied by OMIM, Jul 2010].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.243995.1,
                                           SRR1163657.404009.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..129
                     /product="prefoldin subunit 6"
                     /note="KE2 protein; HLA class II region expressed gene
                     KE2"
                     /calculated_mol_wt=14452
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Region          13..113
                     /region_name="Prefoldin_6"
                     /note="Prefoldin subunit 6; cd23161"
                     /db_xref="CDD:467477"
     Site            order(13,16,24..30,32,60,70..71,73..75,77..79,81..82,
                     84..86,88..90,92..93,108..113)
                     /site_type="other"
                     /note="prefoldin beta subunit /TRiC interface [polypeptide
                     binding]"
                     /db_xref="CDD:467477"
     Region          13..50
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467477"
     Site            21
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Site            order(36,39..40,42..43,45..47,49,53..68,71..72,79,83)
                     /site_type="other"
                     /note="prefoldin oligomer interface [polypeptide binding]"
                     /db_xref="CDD:467477"
     Site            66
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O15212.1)"
     Region          70..113
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:467477"
     CDS             1..129
                     /gene="PFDN6"
                     /gene_synonym="H2-KE2; HKE2; KE-2; PFD6"
                     /coded_by="NM_001265596.1:112..501"
                     /db_xref="CCDS:CCDS4773.1"
                     /db_xref="GeneID:10471"
                     /db_xref="HGNC:HGNC:4926"
                     /db_xref="MIM:605660"
ORIGIN      
        1 maeliqkklq gevekyqqlq kdlsksmsgr qkleaqlten nivkeelall dgsnvvfkll
       61 gpvlvkqelg earatvgkrl dyitaeikry esqlrdlerq seqqretlaq lqqefqraqa
      121 akagapgka
//
LOCUS       NP_055157                303 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial carrier homolog 2 isoform 1 [Homo sapiens].
ACCESSION   NP_055157
VERSION     NP_055157.1
DBSOURCE    REFSEQ: accession NM_014342.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Ulupinar,P., Caglayan,E., Rayaman,E., Nagata,K. and Turan,K.
  TITLE     The mitochondrial carrier homolog 2 is involved in down-regulation
            of influenza A virus replication
  JOURNAL   Mol Biol Rep 51 (1), 642 (2024)
   PUBMED   38727866
  REMARK    GeneRIF: The mitochondrial carrier homolog 2 is involved in
            down-regulation of influenza A virus replication.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Zheng,X. and Chu,B.
  TITLE     The biology of mitochondrial carrier homolog 2
  JOURNAL   Mitochondrion 75, 101837 (2024)
   PUBMED   38158152
  REMARK    GeneRIF: The biology of mitochondrial carrier homolog 2.
            Review article
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Goldman,A., Mullokandov,M., Zaltsman,Y., Regev,L., Levin-Zaidman,S.
            and Gross,A.
  TITLE     MTCH2 cooperates with MFN2 and lysophosphatidic acid synthesis to
            sustain mitochondrial fusion
  JOURNAL   EMBO Rep 25 (1), 45-67 (2024)
   PUBMED   38177900
  REMARK    GeneRIF: MTCH2 cooperates with MFN2 and lysophosphatidic acid
            synthesis to sustain mitochondrial fusion.
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Eswarappa,S.M., Potdar,A.A., Koch,W.J., Fan,Y., Vasu,K.,
            Lindner,D., Willard,B., Graham,L.M., DiCorleto,P.E. and Fox,P.L.
  TITLE     Programmed translational readthrough generates antiangiogenic
            VEGF-Ax
  JOURNAL   Cell 157 (7), 1605-1618 (2014)
   PUBMED   24949972
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Renstrom,F., Payne,F., Nordstrom,A., Brito,E.C., Rolandsson,O.,
            Hallmans,G., Barroso,I., Nordstrom,P. and Franks,P.W.
  CONSRTM   GIANT Consortium
  TITLE     Replication and extension of genome-wide association study results
            for obesity in 4923 adults from northern Sweden
  JOURNAL   Hum Mol Genet 18 (8), 1489-1496 (2009)
   PUBMED   19164386
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Willer,C.J., Speliotes,E.K., Loos,R.J., Li,S., Lindgren,C.M.,
            Heid,I.M., Berndt,S.I., Elliott,A.L., Jackson,A.U., Lamina,C.,
            Lettre,G., Lim,N., Lyon,H.N., McCarroll,S.A., Papadakis,K., Qi,L.,
            Randall,J.C., Roccasecca,R.M., Sanna,S., Scheet,P., Weedon,M.N.,
            Wheeler,E., Zhao,J.H., Jacobs,L.C., Prokopenko,I., Soranzo,N.,
            Tanaka,T., Timpson,N.J., Almgren,P., Bennett,A., Bergman,R.N.,
            Bingham,S.A., Bonnycastle,L.L., Brown,M., Burtt,N.P., Chines,P.,
            Coin,L., Collins,F.S., Connell,J.M., Cooper,C., Smith,G.D.,
            Dennison,E.M., Deodhar,P., Elliott,P., Erdos,M.R., Estrada,K.,
            Evans,D.M., Gianniny,L., Gieger,C., Gillson,C.J., Guiducci,C.,
            Hackett,R., Hadley,D., Hall,A.S., Havulinna,A.S., Hebebrand,J.,
            Hofman,A., Isomaa,B., Jacobs,K.B., Johnson,T., Jousilahti,P.,
            Jovanovic,Z., Khaw,K.T., Kraft,P., Kuokkanen,M., Kuusisto,J.,
            Laitinen,J., Lakatta,E.G., Luan,J., Luben,R.N., Mangino,M.,
            McArdle,W.L., Meitinger,T., Mulas,A., Munroe,P.B., Narisu,N.,
            Ness,A.R., Northstone,K., O'Rahilly,S., Purmann,C., Rees,M.G.,
            Ridderstrale,M., Ring,S.M., Rivadeneira,F., Ruokonen,A.,
            Sandhu,M.S., Saramies,J., Scott,L.J., Scuteri,A., Silander,K.,
            Sims,M.A., Song,K., Stephens,J., Stevens,S., Stringham,H.M.,
            Tung,Y.C., Valle,T.T., Van Duijn,C.M., Vimaleswaran,K.S.,
            Vollenweider,P., Waeber,G., Wallace,C., Watanabe,R.M.,
            Waterworth,D.M., Watkins,N., Witteman,J.C., Zeggini,E., Zhai,G.,
            Zillikens,M.C., Altshuler,D., Caulfield,M.J., Chanock,S.J.,
            Farooqi,I.S., Ferrucci,L., Guralnik,J.M., Hattersley,A.T., Hu,F.B.,
            Jarvelin,M.R., Laakso,M., Mooser,V., Ong,K.K., Ouwehand,W.H.,
            Salomaa,V., Samani,N.J., Spector,T.D., Tuomi,T., Tuomilehto,J.,
            Uda,M., Uitterlinden,A.G., Wareham,N.J., Deloukas,P.,
            Frayling,T.M., Groop,L.C., Hayes,R.B., Hunter,D.J., Mohlke,K.L.,
            Peltonen,L., Schlessinger,D., Strachan,D.P., Wichmann,H.E.,
            McCarthy,M.I., Boehnke,M., Barroso,I., Abecasis,G.R. and
            Hirschhorn,J.N.
  CONSRTM   Wellcome Trust Case Control Consortium; Genetic Investigation of
            ANthropometric Traits Consortium
  TITLE     Six new loci associated with body mass index highlight a neuronal
            influence on body weight regulation
  JOURNAL   Nat Genet 41 (1), 25-34 (2009)
   PUBMED   19079261
  REMARK    GeneRIF: Observational study, meta-analysis, and genome-wide
            association study of gene-disease association. (HuGE Navigator)
REFERENCE   8  (residues 1 to 303)
  AUTHORS   Grinberg,M., Schwarz,M., Zaltsman,Y., Eini,T., Niv,H.,
            Pietrokovski,S. and Gross,A.
  TITLE     Mitochondrial carrier homolog 2 is a target of tBID in cells
            signaled to die by tumor necrosis factor alpha
  JOURNAL   Mol Cell Biol 25 (11), 4579-4590 (2005)
   PUBMED   15899861
  REMARK    GeneRIF: Mtch2 is a mitochondrial target of tBID and possibly
            participates in the mitochondrial apoptotic program.
REFERENCE   9  (residues 1 to 303)
  AUTHORS   Yerushalmi,G.M., Leibowitz-Amit,R., Shaharabany,M. and Tsarfaty,I.
  TITLE     Met-HGF/SF signal transduction induces mimp, a novel mitochondrial
            carrier homologue, which leads to mitochondrial depolarization
  JOURNAL   Neoplasia 4 (6), 510-522 (2002)
   PUBMED   12407445
REFERENCE   10 (residues 1 to 303)
  AUTHORS   Beier,H. and Grimm,M.
  TITLE     Misreading of termination codons in eukaryotes by natural nonsense
            suppressor tRNAs
  JOURNAL   Nucleic Acids Res 29 (23), 4767-4782 (2001)
   PUBMED   11726686
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK313032.1, AY380792.1 and
            AC104942.5.
            
            Summary: This gene encodes a member of the SLC25 family of
            nuclear-encoded transporters that are localized in the inner
            mitochondrial membrane. Members of this superfamily are involved in
            many metabolic pathways and cell functions. Genome-wide association
            studies in human have identified single-nucleotide polymorphisms in
            several loci associated with obesity. This gene is one such locus,
            which is highly expressed in white adipose tissue and adipocytes,
            and thought to play a regulatory role in adipocyte differentiation
            and biology. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. A recent study
            showed this gene to be an authentic stop codon readthrough target
            that can produce two isoforms from the same mRNA by use of
            alternative in-frame translation termination codons. [provided by
            RefSeq, Dec 2017].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UAG termination codon. This
            RefSeq represents the shorter isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.269157.1,
                                           SRR1803614.157346.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000302503.8/
                                                  ENSP00000303222.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..303
                     /product="mitochondrial carrier homolog 2 isoform 1"
                     /note="met-induced mitochondrial protein; mitochondrial
                     carrier homolog 2; solute carrier family 25, member 50"
                     /calculated_mol_wt=33200
     Region          2..98
                     /region_name="Solcar 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            16..36
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            78..92
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Region          118..206
                     /region_name="Solcar 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Region          128..>192
                     /region_name="Mito_carr"
                     /note="Mitochondrial carrier protein; pfam00153"
                     /db_xref="CDD:395101"
     Site            136..156
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            181..199
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            232..252
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     Site            281..303
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y6C9.1)"
     CDS             1..303
                     /gene="MTCH2"
                     /gene_synonym="HSPC032; MIMP; SLC25A50"
                     /coded_by="NM_014342.4:95..1006"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7943.1"
                     /db_xref="GeneID:23788"
                     /db_xref="HGNC:HGNC:17587"
                     /db_xref="MIM:613221"
ORIGIN      
        1 madaasqvll gsgltilsqp lmyvkvliqv gyeplpptig rnifgrqvcq lpglfsyaqh
       61 iasidgrrgl ftgltprlcs gvlgtvvhgk vlqhyqesdk geelgpgnvq kevsssfdhv
      121 ikettremia rsaatlithp fhvitlrsmv qfigreskyc glcdsiitiy reegilgffa
      181 glvprllgdi lslwlcnsla ylvntyalds gvstmnemks ysqavtgffa smltypfvlv
      241 snlmavnncg laggcppysp iytswidcwc mlqkegnmsr gnslffrkvp fgktyccdlk
      301 mli
//
LOCUS       NP_001193703             413 aa            linear   PRI 20-NOV-2025
DEFINITION  general transcription factor 3C polypeptide 3 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001193703
VERSION     NP_001193703.1
DBSOURCE    REFSEQ: accession NM_001206774.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 413)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 413)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 413)
  AUTHORS   Huang,S., Chen,J., Wang,H., Sun,B., Wang,H., Zhang,Z., Zhang,X. and
            Chen,Z.
  TITLE     Influenza A virus matrix protein 1 interacts with hTFIIIC102-s, a
            short isoform of the polypeptide 3 subunit of human general
            transcription factor IIIC
  JOURNAL   Arch Virol 154 (7), 1101-1110 (2009)
   PUBMED   19521658
REFERENCE   4  (residues 1 to 413)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   5  (residues 1 to 413)
  AUTHORS   Koch,H.B., Zhang,R., Verdoodt,B., Bailey,A., Zhang,C.D., Yates,J.R.
            3rd, Menssen,A. and Hermeking,H.
  TITLE     Large-scale identification of c-MYC-associated proteins using a
            combined TAP/MudPIT approach
  JOURNAL   Cell Cycle 6 (2), 205-217 (2007)
   PUBMED   17314511
REFERENCE   6  (residues 1 to 413)
  AUTHORS   Hirschowitz,E.A., Hiestand,D.M. and Yannelli,J.R.
  TITLE     Vaccines for lung cancer
  JOURNAL   J Thorac Oncol 1 (1), 93-104 (2006)
   PUBMED   17409835
  REMARK    Review article
REFERENCE   7  (residues 1 to 413)
  AUTHORS   Zhan,Y., Hegde,R., Srinivasula,S.M., Fernandes-Alnemri,T. and
            Alnemri,E.S.
  TITLE     Death effector domain-containing proteins DEDD and FLAME-3 form
            nuclear complexes with the TFIIIC102 subunit of human transcription
            factor IIIC
  JOURNAL   Cell Death Differ 9 (4), 439-447 (2002)
   PUBMED   11965497
  REMARK    GeneRIF: DEDD and FLAME-3 form nuclear complexes with TFIIIC102
REFERENCE   8  (residues 1 to 413)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   9  (residues 1 to 413)
  AUTHORS   Behar,G., Coleclough,C., Houlgatte,R., Auffray,C. and Lefkovits,I.
  TITLE     Human lymphocyte cDNA ordered library analyzed by 2D gel
            electrophoresis. 3. Analysis of individual clones
  JOURNAL   Appl Theor Electrophor 5 (2), 99-105 (1995)
   PUBMED   8573604
REFERENCE   10 (residues 1 to 413)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB078021.1, AF465407.1 and
            AC012486.9.
            
            Summary: The protein encoded by this gene is part of the TFIIIC2
            complex, which binds to the promoters of small nuclear and
            cytoplasmic RNA genes in order to recruit RNA polymerase III. The
            TFIIIC2 complex is composed of six subunits. Two transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (2) lacks multiple exons from the
            3' end and has an alternate 3' segment, compared to variant 1. The
            resulting isoform (2) has a much shorter and distinct C-terminus,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF465407.1, SRR1660803.146605.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..413
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.1"
     Protein         1..413
                     /product="general transcription factor 3C polypeptide 3
                     isoform 2"
                     /note="general transcription factor 3C polypeptide 3;
                     TF3C-gamma; TFIIIC 102 kDa subunit; transcription factor
                     IIIC subunit gamma; general transcription factor IIIC,
                     polypeptide 3, 102kDa"
                     /calculated_mol_wt=47127
     Region          1..121
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          <146..351
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          149..182
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          152..177
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          183..216
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          183..211
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(184,187..188,191..192,194,218,221..222,225..226,
                     228..229,252,255..256,259..260,263)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          216..246
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          217..250
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          251..278
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          252..284
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          286..316
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          290..323
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     Region          326..361
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y5Q9.1)"
     CDS             1..413
                     /gene="GTF3C3"
                     /gene_synonym="NEDFBS; TFIIIC102; TFiiiC2-102;
                     TFIIICgamma"
                     /coded_by="NM_001206774.2:73..1314"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56153.1"
                     /db_xref="GeneID:9330"
                     /db_xref="HGNC:HGNC:4666"
                     /db_xref="MIM:604888"
ORIGIN      
        1 msgfspelid ylegkisfee ferrreerkt rekkslqekg klsaeenpdd sevpsssgin
       61 stksqdkdvn egetsdgvrk svhkvfasml geneddeeee eeeeeeeeee etpeqptagd
      121 vfvlemvlnr etkkmmkekr prsklpralr glmgeanirf argereeail mcmeiirqap
      181 layepfstla miyedqgdme kslqfeliaa hlnpsdteew vrlaemsleq dnikqaifcy
      241 tkalkyeptn vrylwerssl yeqmgdhkma mdgyrrilnl lspsdgerfm qlardmaksy
      301 yeandvtsai niideafskh qglvsmedvn iaaelyisnk qydkaleiit dfsgivlekk
      361 tseegtseen kapenvtcti pdgvpiditv klmvclvhln ileplnvcnk ict
//
LOCUS       NP_001341030             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341030 XP_016879176
VERSION     NP_001341030.1
DBSOURCE    REFSEQ: accession NM_001354101.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Sep 13, 2017 this sequence version replaced XP_016879176.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF356585.1, CR991450.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354101.2:1433..2197"
                     /note="isoform a is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_689479                215 aa            linear   PRI 20-NOV-2025
DEFINITION  Fanconi anemia core complex-associated protein 24 isoform 1 [Homo
            sapiens].
ACCESSION   NP_689479
VERSION     NP_689479.1
DBSOURCE    REFSEQ: accession NM_152266.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 215)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 215)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 215)
  AUTHORS   Daschkey,S., Bienemann,K., Schuster,V., Kreth,H.W., Linka,R.M.,
            Honscheid,A., Fritz,G., Johannes,C., Fleckenstein,B., Kempkes,B.,
            Gombert,M., Ginzel,S. and Borkhardt,A.
  TITLE     Fatal Lymphoproliferative Disease in Two Siblings Lacking
            Functional FAAP24
  JOURNAL   J Clin Immunol 36 (7), 684-692 (2016)
   PUBMED   27473539
  REMARK    GeneRIF: This is the first report of an FAAP24 loss of function
            mutation found in human patients with EBV-associated
            lymphoproliferation.
REFERENCE   4  (residues 1 to 215)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 215)
  AUTHORS   Yang,H., Zhang,T., Tao,Y., Wang,F., Tong,L. and Ding,J.
  TITLE     Structural insights into the functions of the FANCM-FAAP24 complex
            in DNA repair
  JOURNAL   Nucleic Acids Res 41 (22), 10573-10583 (2013)
   PUBMED   24003026
  REMARK    GeneRIF: Results show that the first HhH motif of FAAP24 is a
            potential binding site for DNA, which plays a critical role in
            targeting FANCM-FAAP24 to chromatin.
REFERENCE   6  (residues 1 to 215)
  AUTHORS   Yan,Z., Delannoy,M., Ling,C., Daee,D., Osman,F., Muniandy,P.A.,
            Shen,X., Oostra,A.B., Du,H., Steltenpool,J., Lin,T., Schuster,B.,
            Decaillet,C., Stasiak,A., Stasiak,A.Z., Stone,S., Hoatlin,M.E.,
            Schindler,D., Woodcock,C.L., Joenje,H., Sen,R., de Winter,J.P.,
            Li,L., Seidman,M.M., Whitby,M.C., Myung,K., Constantinou,A. and
            Wang,W.
  TITLE     A histone-fold complex and FANCM form a conserved DNA-remodeling
            complex to maintain genome stability
  JOURNAL   Mol Cell 37 (6), 865-878 (2010)
   PUBMED   20347428
REFERENCE   7  (residues 1 to 215)
  AUTHORS   Collis,S.J., Ciccia,A., Deans,A.J., Horejsi,Z., Martin,J.S.,
            Maslen,S.L., Skehel,J.M., Elledge,S.J., West,S.C. and Boulton,S.J.
  TITLE     FANCM and FAAP24 function in ATR-mediated checkpoint signaling
            independently of the Fanconi anemia core complex
  JOURNAL   Mol Cell 32 (3), 313-324 (2008)
   PUBMED   18995830
  REMARK    GeneRIF: DNA damage recognition and remodeling activities of FANCM
            and FAAP24 cooperate to promote efficient activation of DNA damage
            checkpoints in Fanconi anemia.
REFERENCE   8  (residues 1 to 215)
  AUTHORS   Kim,J.M., Kee,Y., Gurtan,A. and D'Andrea,A.D.
  TITLE     Cell cycle-dependent chromatin loading of the Fanconi anemia core
            complex by FANCM/FAAP24
  JOURNAL   Blood 111 (10), 5215-5222 (2008)
   PUBMED   18174376
  REMARK    GeneRIF: FANCM is an anchor required for recruitment of the FA core
            complex to chromatin, and the FANCM/FAAP24 interaction is essential
            for this chromatin-loading activity
REFERENCE   9  (residues 1 to 215)
  AUTHORS   Gari,K., Decaillet,C., Stasiak,A.Z., Stasiak,A. and Constantinou,A.
  TITLE     The Fanconi anemia protein FANCM can promote branch migration of
            Holliday junctions and replication forks
  JOURNAL   Mol Cell 29 (1), 141-148 (2008)
   PUBMED   18206976
  REMARK    GeneRIF: FAAP24 is dispensable for DNA binding and branch migration
            activity of FANCM.
REFERENCE   10 (residues 1 to 215)
  AUTHORS   Ciccia,A., Ling,C., Coulthard,R., Yan,Z., Xue,Y., Meetei,A.R.,
            Laghmani el,H., Joenje,H., McDonald,N., de Winter,J.P., Wang,W. and
            West,S.C.
  TITLE     Identification of FAAP24, a Fanconi anemia core complex protein
            that interacts with FANCM
  JOURNAL   Mol Cell 25 (3), 331-343 (2007)
   PUBMED   17289582
  REMARK    GeneRIF: FAAP24 targets FANCM to structures that mimic
            intermediates formed during the replication/repair of damaged DNA.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CD690094.1, AK128668.1, CN368337.1, BX390218.2, BC020247.1,
            BM679170.1 and AC011449.6.
            
            Summary: FAAP24 is a component of the Fanconi anemia (FA) core
            complex (see MIM 227650), which plays a crucial role in DNA damage
            response (Ciccia et al., 2007 [PubMed 17289582]).[supplied by OMIM,
            Mar 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK128668.1, SRR5189667.156605.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000588258.6/ ENSP00000466121.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..215
                     /product="Fanconi anemia core complex-associated protein
                     24 isoform 1"
                     /note="Fanconi anemia-associated protein of 24 kDa;
                     Fanconi anemia core complex associated protein 24"
                     /calculated_mol_wt=23766
     Region          17..138
                     /region_name="XPF_nuclease_FAAP24"
                     /note="XPF-like nuclease domain of Fanconi anemia
                     associated protein 24 kDa (FAAP24); cd20076"
                     /db_xref="CDD:410852"
     Site            order(101..102,105..106,109..110,115..118,124,128,
                     131..132,134..135)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:410852"
     Region          160..215
                     /region_name="RuvA domain 2-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BTP7.2)"
     Region          166..215
                     /region_name="HHH_2"
                     /note="Helix-hairpin-helix motif; pfam12826"
                     /db_xref="CDD:432812"
     CDS             1..215
                     /gene="FAAP24"
                     /gene_synonym="C19orf40"
                     /coded_by="NM_152266.5:119..766"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12426.1"
                     /db_xref="GeneID:91442"
                     /db_xref="HGNC:HGNC:28467"
                     /db_xref="MIM:610884"
ORIGIN      
        1 meknppddtg pvhvplghiv anekwrgsql aqemqgkikl ifedgltpdf ylsnrccily
       61 vteadlvagn gyrkrlvrvr nsnnlkgivv vektrmseqy fpalqkftvl dlgmvllpva
      121 sqmeasclvi qlvqeqtkep sknpllgkkr alllsepsll rtvqqipgvg kvkaplllqk
      181 fpsiqqlsna sigeleqvvg qavaqqihaf ftqpr
//
LOCUS       NP_112570                257 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein uS15m [Homo sapiens].
ACCESSION   NP_112570
VERSION     NP_112570.2
DBSOURCE    REFSEQ: accession NM_031280.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 257)
  AUTHORS   David,F., Roussel,E., Froment,C., Draia-Nicolau,T., Pujol,F.,
            Burlet-Schiltz,O., Henras,A.K., Lacazette,E., Morfoisse,F.,
            Tatin,F., Diaz,J.J., Catez,F., Garmy-Susini,B. and Prats,A.C.
  TITLE     Mitochondrial Ribosomal Protein MRPS15 Is a Component of Cytosolic
            Ribosomes and Regulates Translation in Stressed Cardiomyocytes
  JOURNAL   Int J Mol Sci 25 (6), 3250 (2024)
   PUBMED   38542224
  REMARK    GeneRIF: Mitochondrial Ribosomal Protein MRPS15 Is a Component of
            Cytosolic Ribosomes and Regulates Translation in Stressed
            Cardiomyocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Davies,S.M., Rackham,O., Shearwood,A.M., Hamilton,K.L., Narsai,R.,
            Whelan,J. and Filipovska,A.
  TITLE     Pentatricopeptide repeat domain protein 3 associates with the
            mitochondrial small ribosomal subunit and regulates translation
  JOURNAL   FEBS Lett 583 (12), 1853-1858 (2009)
   PUBMED   19427859
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Suzuki,T., Terasaki,M., Takemoto-Hori,C., Hanada,T., Ueda,T.,
            Wada,A. and Watanabe,K.
  TITLE     Proteomic analysis of the mammalian mitochondrial ribosome.
            Identification of protein components in the 28 S small subunit
  JOURNAL   J Biol Chem 276 (35), 33181-33195 (2001)
   PUBMED   11402041
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Cavdar Koc,E., Burkhart,W., Blackburn,K., Moseley,A. and
            Spremulli,L.L.
  TITLE     The small subunit of the mammalian mitochondrial ribosome.
            Identification of the full complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (22), 19363-19374 (2001)
   PUBMED   11279123
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM048518.1, AK315441.1,
            BU927793.1, BC031336.1, CF123360.1 and AC119675.2.
            
            On Oct 31, 2001 this sequence version replaced NP_112570.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 28S subunit protein that belongs to
            the ribosomal protein S15P family. The encoded protein is more than
            two times the size of its E. coli counterpart, with the 12S rRNA
            binding sites conserved. Between human and mouse, the encoded
            protein is the least conserved among small subunit ribosomal
            proteins. Pseudogenes corresponding to this gene are found on
            chromosomes 15q and 19q. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK315441.1, BC031336.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000373116.6/
                                                  ENSP00000362208.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..257
                     /product="small ribosomal subunit protein uS15m"
                     /note="28S ribosomal protein S15, mitochondrial; MRP-S15;
                     mitochondrial small ribosomal subunit protein uS15m"
                     /calculated_mol_wt=29711
     Region          109..187
                     /region_name="Ribosomal_S15"
                     /note="Ribosomal protein S15; pfam00312"
                     /db_xref="CDD:459756"
     Region          225..257
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P82914.1)"
     CDS             1..257
                     /gene="MRPS15"
                     /gene_synonym="DC37; MPR-S15; RPMS15; S15mt; uS15m"
                     /coded_by="NM_031280.4:110..883"
                     /db_xref="CCDS:CCDS411.1"
                     /db_xref="GeneID:64960"
                     /db_xref="HGNC:HGNC:14504"
                     /db_xref="MIM:611979"
ORIGIN      
        1 mlrvawrtls lirtravtqv lvpglpgggs akfpfnqwgl qprslllqaa rgyvvrkpaq
       61 srldddppps tllkdyqnvp giekvddvvk rllslemank kemlkikqeq fmkkivanpe
      121 dtrslearii alsvkirsye ehlekhrkdk ahkryllmsi dqrkkmlknl rntnydvfek
      181 icwglgieyt fpplyyrrah rrfvtkkalc irvfqetqkl kkrrralkaa aaaqkqakrr
      241 npdspakaip ktlkdsq
//
LOCUS       NP_006576                548 aa            linear   PRI 20-NOV-2025
DEFINITION  T-complex protein 1 subunit theta isoform 1 [Homo sapiens].
ACCESSION   NP_006576 XP_375936
VERSION     NP_006576.2
DBSOURCE    REFSEQ: accession NM_006585.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 548)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 548)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 548)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   4  (residues 1 to 548)
  AUTHORS   Gestaut,D., Roh,S.H., Ma,B., Pintilie,G., Joachimiak,L.A.,
            Leitner,A., Walzthoeni,T., Aebersold,R., Chiu,W. and Frydman,J.
  TITLE     The Chaperonin TRiC/CCT Associates with Prefoldin through a
            Conserved Electrostatic Interface Essential for Cellular
            Proteostasis
  JOURNAL   Cell 177 (3), 751-765 (2019)
   PUBMED   30955883
REFERENCE   5  (residues 1 to 548)
  AUTHORS   Fasci,D., van Ingen,H., Scheltema,R.A. and Heck,A.J.R.
  TITLE     Histone Interaction Landscapes Visualized by Crosslinking Mass
            Spectrometry in Intact Cell Nuclei
  JOURNAL   Mol Cell Proteomics 17 (10), 2018-2033 (2018)
   PUBMED   30021884
REFERENCE   6  (residues 1 to 548)
  AUTHORS   Yokota,S., Yanagi,H., Yura,T. and Kubota,H.
  TITLE     Cytosolic chaperonin-containing t-complex polypeptide 1 changes the
            content of a particular subunit species concomitant with substrate
            binding and folding activities during the cell cycle
  JOURNAL   Eur J Biochem 268 (17), 4664-4673 (2001)
   PUBMED   11532003
REFERENCE   7  (residues 1 to 548)
  AUTHORS   Hynes,G.M. and Willison,K.R.
  TITLE     Individual subunits of the eukaryotic cytosolic chaperonin mediate
            interactions with binding sites located on subdomains of beta-actin
  JOURNAL   J Biol Chem 275 (25), 18985-18994 (2000)
   PUBMED   10748209
REFERENCE   8  (residues 1 to 548)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   9  (residues 1 to 548)
  AUTHORS   Yamazaki,M., Ono,A., Watanabe,K., Sasaki,K., Tashiro,H. and
            Nomura,T.
  TITLE     Nucleotide sequence surrounding the locus marker D21S246 on human
            chromosome 21
  JOURNAL   DNA Res 2 (4), 187-189 (1995)
   PUBMED   8590283
REFERENCE   10 (residues 1 to 548)
  AUTHORS   Kubota,H., Hynes,G. and Willison,K.
  TITLE     The eighth Cct gene, Cctq, encoding the theta subunit of the
            cytosolic chaperonin containing TCP-1
  JOURNAL   Gene 154 (2), 231-236 (1995)
   PUBMED   7890169
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC072001.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_375936.1, NP_006576.1.
            
            Summary: This gene encodes the theta subunit of the CCT chaperonin,
            which is abundant in the eukaryotic cytosol and may be involved in
            the transport and assembly of newly synthesized proteins.
            Alternative splicing results in multiple transcript variants of
            this gene. A pseudogene related to this gene is located on
            chromosome 1. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC072001.1, SRR1660807.58830.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000286788.9/ ENSP00000286788.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..548
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..548
                     /product="T-complex protein 1 subunit theta isoform 1"
                     /note="T-complex protein 1 subunit theta; CCT-theta;
                     TCP-1-theta; renal carcinoma antigen NY-REN-15; chaperonin
                     containing TCP1, subunit 8 (theta); chaperonin containing
                     T-complex polypeptide 1 subunit 8"
                     /calculated_mol_wt=59490
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7;
                     propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Region          10..539
                     /region_name="chap_CCT_theta"
                     /note="T-complex protein 1, theta subunit; TIGR02346"
                     /db_xref="CDD:274087"
     Site            order(20,24,52..55,57,75,77,81,85,88,382,520..526)
                     /site_type="other"
                     /note="ring oligomerisation interface [polypeptide
                     binding]"
                     /db_xref="CDD:239457"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            order(47..49,99,103,166,394,412,452,497,499)
                     /site_type="other"
                     /note="ATP/Mg binding site [chemical binding]"
                     /db_xref="CDD:239457"
     Site            162
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            400
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            order(432,450,459,461..462,465)
                     /site_type="active"
                     /note="stacking interactions [active]"
                     /db_xref="CDD:239457"
     Site            466
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     Region          529..548
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P50990.4)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P50990.4)"
     CDS             1..548
                     /gene="CCT8"
                     /gene_synonym="C21orf112; Cctq; D21S246; PRED71"
                     /coded_by="NM_006585.4:59..1705"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33528.1"
                     /db_xref="GeneID:10694"
                     /db_xref="HGNC:HGNC:1623"
                     /db_xref="MIM:617786"
ORIGIN      
        1 malhvpkapg faqmlkegak hfsgleeavy rniqackela qttrtaygpn gmnkmvinhl
       61 eklfvtndaa tilrelevqh paakmivmas hmqeqevgdg tnfvlvfaga llelaeellr
      121 iglsvsevie gyeiacrkah eilpnlvccs aknlrdidev ssllrtsims kqygnevfla
      181 kliaqacvsi fpdsghfnvd nirvckilgs gissssvlhg mvfkketegd vtsvkdakia
      241 vyscpfdgmi tetkgtvlik taeelmnfsk geenlmdaqv kaiadtganv vvtggkvadm
      301 alhyankyni mlvrlnskwd lrrlcktvga talprltppv leemghcdsv ylsevgdtqv
      361 vvfkhekedg aistivlrgs tdnlmddier avddgvntfk vltrdkrlvp gggateiela
      421 kqitsygetc pgleqyaikk faeafeaipr alaensgvka nevisklyav hqegnknvgl
      481 dieaevpavk dmleagildt ylgkywaikl atnaavtvlr vdqiimakpa ggpkppsgkk
      541 dwdddqnd
//
LOCUS       NP_006405                283 aa            linear   PRI 20-NOV-2025
DEFINITION  ribonuclease P protein subunit p38 [Homo sapiens].
ACCESSION   NP_006405
VERSION     NP_006405.2
DBSOURCE    REFSEQ: accession NM_006414.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Wu,J., Niu,S., Tan,M., Huang,C., Li,M., Song,Y., Wang,Q., Chen,J.,
            Shi,S., Lan,P. and Lei,M.
  TITLE     Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
  JOURNAL   Cell 175 (5), 1393-1404 (2018)
   PUBMED   30454648
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Oshima,K., Kakiuchi,Y., Tanaka,Y., Ueda,T., Nakashima,T., Kimura,M.
            and Yao,M.
  TITLE     Structural basis for recognition of a kink-turn motif by an
            archaeal homologue of human RNase P protein Rpp38
  JOURNAL   Biochem Biophys Res Commun 474 (3), 541-546 (2016)
   PUBMED   27114305
  REMARK    GeneRIF: A pull-down assay further suggested the presence of a
            second K-turn in SL12. Based on the present results, together with
            available data, we discuss a structural basis for recognition of
            K-turn motifs in PhopRNA by PhoRpp38.
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Welting,T.J., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Mutual interactions between subunits of the human RNase MRP
            ribonucleoprotein complex
  JOURNAL   Nucleic Acids Res 32 (7), 2138-2146 (2004)
   PUBMED   15096576
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Jiang,T., Guerrier-Takada,C. and Altman,S.
  TITLE     Protein-RNA interactions in the subunits of human nuclear RNase P
  JOURNAL   RNA 7 (7), 937-941 (2001)
   PUBMED   11455963
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Jarrous,N., Wolenski,J.S., Wesolowski,D., Lee,C. and Altman,S.
  TITLE     Localization in the nucleolus and coiled bodies of protein subunits
            of the ribonucleoprotein ribonuclease P
  JOURNAL   J Cell Biol 146 (3), 559-572 (1999)
   PUBMED   10444065
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Jarrous,N., Eder,P.S., Guerrier-Takada,C., Hoog,C. and Altman,S.
  TITLE     Autoantigenic properties of some protein subunits of catalytically
            active complexes of human ribonuclease P
  JOURNAL   RNA 4 (4), 407-417 (1998)
   PUBMED   9630247
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Eder,P.S., Kekuda,R., Stolc,V. and Altman,S.
  TITLE     Characterization of two scleroderma autoimmune antigens that
            copurify with human ribonuclease P
  JOURNAL   Proc Natl Acad Sci U S A 94 (4), 1101-1106 (1997)
   PUBMED   9037013
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP247818.1, BC029494.1 and AW292674.1.
            
            On May 23, 2007 this sequence version replaced NP_006405.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. All variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.241608.1,
                                           SRR1660803.421362.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..283
                     /product="ribonuclease P protein subunit p38"
                     /EC_number="3.1.26.5"
                     /note="RNaseP protein p38; ribonuclease P/MRP 38kDa
                     subunit"
                     /calculated_mol_wt=31703
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Region          107..185
                     /region_name="Ribosomal_L7Ae"
                     /note="Ribosomal protein L7Ae/L30e/S12e/Gadd45 family;
                     cl00600"
                     /db_xref="CDD:469835"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78345.2)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P78345.2)"
     CDS             1..283
                     /gene="RPP38"
                     /coded_by="NM_006414.5:66..917"
                     /db_xref="CCDS:CCDS7108.1"
                     /db_xref="GeneID:10557"
                     /db_xref="HGNC:HGNC:30329"
                     /db_xref="MIM:606116"
ORIGIN      
        1 maaapqapgr gslrktrplv vktslnnpyi irwsalesed mhfilqtled rlkaiglqki
       61 edkkkknktp flkkesrekc siavdisenl kekktdakqq vsgwtpahvr kqlaigvnev
      121 tralerrell lvlvcksvkp amitshliql slsrsvpacq vprlseriap viglkcvlal
      181 afkknttdfv devraiiprv pslsvpwlqd riedsgenle teplesqdre lldtsfedls
      241 kpkrkladgr qasvtlqplk ikklipnpnk irkppkskka tpk
//
LOCUS       NP_061910                245 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex component RRP41 [Homo sapiens].
ACCESSION   NP_061910
VERSION     NP_061910.1
DBSOURCE    REFSEQ: accession NM_019037.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 245)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 245)
  AUTHORS   Wang,N., Miao,X., Lu,W., Ji,Y., Zheng,Y., Meng,D., Liu,H. and
            Xiang,C.
  TITLE     RUNX3 exerts tumor-suppressive role through inhibiting EXOSC4
            expression
  JOURNAL   Funct Integr Genomics 24 (3), 103 (2024)
   PUBMED   38913281
  REMARK    GeneRIF: RUNX3 exerts tumor-suppressive role through inhibiting
            EXOSC4 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 245)
  AUTHORS   Taniue,K., Tanu,T., Shimoura,Y., Mitsutomi,S., Han,H., Kakisaka,R.,
            Ono,Y., Tamamura,N., Takahashi,K., Wada,Y., Mizukami,Y. and
            Akimitsu,N.
  TITLE     RNA Exosome Component EXOSC4 Amplified in Multiple Cancer Types Is
            Required for the Cancer Cell Survival
  JOURNAL   Int J Mol Sci 23 (1), 496 (2022)
   PUBMED   35008922
  REMARK    GeneRIF: RNA Exosome Component EXOSC4 Amplified in Multiple Cancer
            Types Is Required for the Cancer Cell Survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 245)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 245)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 245)
  AUTHORS   Raijmakers,R., Noordman,Y.E., van Venrooij,W.J. and Pruijn,G.J.
  TITLE     Protein-protein interactions of hCsl4p with other human exosome
            subunits
  JOURNAL   J Mol Biol 315 (4), 809-818 (2002)
   PUBMED   11812149
REFERENCE   7  (residues 1 to 245)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   8  (residues 1 to 245)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   9  (residues 1 to 245)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   10 (residues 1 to 245)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM839994.1, BC002777.2 and AK000598.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.324876.1,
                                           SRR1660803.24566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000316052.6/ ENSP00000315476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..245
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..245
                     /product="exosome complex component RRP41"
                     /note="exosome complex exonuclease RRP41; exosome
                     component Rrp41; ribosomal RNA-processing protein 41"
                     /calculated_mol_wt=26252
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NPD3.3)"
     Region          11..237
                     /region_name="RNase_PH_RRP41"
                     /note="RRP41 subunit of eukaryotic exosome; cd11370"
                     /db_xref="CDD:206775"
     Site            order(34,36,51,53..55,73,75,80,98,101,105,119,124,129,
                     147..149,156,196..207,210,214)
                     /site_type="other"
                     /note="hexamer interface [polypeptide binding]"
                     /db_xref="CDD:206775"
     Site            order(36,54..57,59,112,116,119,147..150,152..154,156,229,
                     232..233,236..237)
                     /site_type="other"
                     /note="Rrp4 interface [polypeptide binding]"
                     /db_xref="CDD:206775"
     CDS             1..245
                     /gene="EXOSC4"
                     /gene_synonym="hRrp41p; p12A; RRP41; RRP41A; Rrp41p; SKI6;
                     Ski6p"
                     /coded_by="NM_019037.3:58..795"
                     /db_xref="CCDS:CCDS6414.1"
                     /db_xref="GeneID:54512"
                     /db_xref="HGNC:HGNC:18189"
                     /db_xref="MIM:606491"
ORIGIN      
        1 maglellsdq gyrvdgrrag elrkiqarmg vfaqadgsay ieqgntkala vvygpheirg
       61 sraralpdra lvncqyssat fstgerkrrp hgdrkscemg lqlrqtfeaa iltqlhprsq
      121 idiyvqvlqa dggtyaacvn aatlavldag ipmrdfvcac sagfvdgtal adlshveeaa
      181 ggpqlalall pasgqialle mdarlhedhl ervleaaaqa ardvhtlldr vvrqhvreas
      241 illgd
//
LOCUS       NP_004200                229 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptogyrin-3 [Homo sapiens].
ACCESSION   NP_004200
VERSION     NP_004200.2
DBSOURCE    REFSEQ: accession NM_004209.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 229)
  AUTHORS   Ho,P.W., Li,L., Liu,H.F., Choi,Z.Y., Chang,E.E.S., Pang,S.Y.,
            Malki,Y., Leung,C.T., Kung,M.H., Ramsden,D.B. and Ho,S.L.
  TITLE     In vivo overexpression of synaptogyrin-3 promotes striatal synaptic
            dopamine uptake in LRRK2R1441G mutant mouse model of Parkinson's
            disease
  JOURNAL   Brain Behav 13 (2), e2886 (2023)
   PUBMED   36624932
  REMARK    GeneRIF: In vivo overexpression of synaptogyrin-3 promotes striatal
            synaptic dopamine uptake in LRRK2[R1441G] mutant mouse model of
            Parkinson's disease.
REFERENCE   2  (residues 1 to 229)
  AUTHORS   Murphy,R.M., Tasoulas,J., Porrello,A., Carper,M.B., Tsai,Y.H.,
            Coffey,A.R., Kumar,S., Zeng,P.Y., Schrank,T.P., Midkiff,B.R.,
            Cohen,S., Salazar,A.H., Hayward,M.C., Hayes,D.N., Olshan,A.,
            Gupta,G.P., Nichols,A.C., Yarbrough,W.G., Pecot,C.V. and
            Amelio,A.L.
  TITLE     Tumor Cell Extrinsic Synaptogyrin 3 Expression as a Diagnostic and
            Prognostic Biomarker in Head and Neck Cancer
  JOURNAL   Cancer Res Commun 2 (9), 987-1004 (2022)
   PUBMED   36148399
  REMARK    GeneRIF: Tumor Cell Extrinsic Synaptogyrin 3 Expression as a
            Diagnostic and Prognostic Biomarker in Head and Neck Cancer.
REFERENCE   3  (residues 1 to 229)
  AUTHORS   Li,L., Ho,P.W., Liu,H., Pang,S.Y., Chang,E.E., Choi,Z.Y., Malki,Y.,
            Kung,M.H., Ramsden,D.B. and Ho,S.L.
  TITLE     Transcriptional Regulation of the Synaptic Vesicle Protein
            Synaptogyrin-3 (SYNGR3) Gene: The Effects of NURR1 on Its
            Expression
  JOURNAL   Int J Mol Sci 23 (7), 3646 (2022)
   PUBMED   35409005
  REMARK    GeneRIF: Transcriptional Regulation of the Synaptic Vesicle Protein
            Synaptogyrin-3 (SYNGR3) Gene: The Effects of NURR1 on Its
            Expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 229)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 229)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 229)
  AUTHORS   Chen,S., Lu,F.F., Seeman,P. and Liu,F.
  TITLE     Quantitative proteomic analysis of human substantia nigra in
            Alzheimer's disease, Huntington's disease and Multiple sclerosis
  JOURNAL   Neurochem Res 37 (12), 2805-2813 (2012)
   PUBMED   22926577
REFERENCE   7  (residues 1 to 229)
  AUTHORS   Chang,H., Jeung,H.C., Jung,J.J., Kim,T.S., Rha,S.Y. and Chung,H.C.
  TITLE     Identification of genes associated with chemosensitivity to
            SAHA/taxane combination treatment in taxane-resistant breast cancer
            cells
  JOURNAL   Breast Cancer Res Treat 125 (1), 55-63 (2011)
   PUBMED   20224928
REFERENCE   8  (residues 1 to 229)
  AUTHORS   Egana,L.A., Cuevas,R.A., Baust,T.B., Parra,L.A., Leak,R.K.,
            Hochendoner,S., Pena,K., Quiroz,M., Hong,W.C., Dorostkar,M.M.,
            Janz,R., Sitte,H.H. and Torres,G.E.
  TITLE     Physical and functional interaction between the dopamine
            transporter and the synaptic vesicle protein synaptogyrin-3
  JOURNAL   J Neurosci 29 (14), 4592-4604 (2009)
   PUBMED   19357284
  REMARK    GeneRIF: This study demonstrates the interaction of the mouse
            homolog, synaptogyrin 3, with the dopamine transporter (DAT).
REFERENCE   9  (residues 1 to 229)
  AUTHORS   Belizaire,R., Komanduri,C., Wooten,K., Chen,M., Thaller,C. and
            Janz,R.
  TITLE     Characterization of synaptogyrin 3 as a new synaptic vesicle
            protein
  JOURNAL   J Comp Neurol 470 (3), 266-281 (2004)
   PUBMED   14755516
  REMARK    GeneRIF: This study identifies the mouse homolog, synaptogyrin 3,
            as a synaptic vesicle protein.
REFERENCE   10 (residues 1 to 229)
  AUTHORS   Kedra,D., Pan,H.Q., Seroussi,E., Fransson,I., Guilbaud,C.,
            Collins,J.E., Dunham,I., Blennow,E., Roe,B.A., Piehl,F. and
            Dumanski,J.P.
  TITLE     Characterization of the human synaptogyrin gene family
  JOURNAL   Hum Genet 103 (2), 131-141 (1998)
   PUBMED   9760194
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005606.3 and BC014087.2.
            
            On Dec 23, 1999 this sequence version replaced NP_004200.1.
            
            Summary: This gene encodes an integral membrane protein. The exact
            function of this protein is unclear, but studies of a similar
            murine protein suggest that it is a synaptic vesicle protein that
            also interacts with the dopamine transporter. The gene product
            belongs to the synaptogyrin gene family. [provided by RefSeq, Dec
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014087.2, SRR1803611.203285.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248121.7/ ENSP00000248121.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..229
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..229
                     /product="synaptogyrin-3"
                     /calculated_mol_wt=24424
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O43761.2)"
     Region          20..165
                     /region_name="MARVEL"
                     /note="Membrane-associating domain; pfam01284"
                     /db_xref="CDD:366555"
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43761.2)"
     Site            70..90
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43761.2)"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43761.2)"
     Site            148..168
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43761.2)"
     Region          209..229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43761.2)"
     CDS             1..229
                     /gene="SYNGR3"
                     /coded_by="NM_004209.6:134..823"
                     /db_xref="CCDS:CCDS10456.1"
                     /db_xref="GeneID:9143"
                     /db_xref="HGNC:HGNC:11501"
                     /db_xref="MIM:603927"
ORIGIN      
        1 megasfgagr agaaldpvsf arrpqtllrv aswvfsiavf gpivnegyvn tdsgpelrcv
       61 fngnagacrf gvalglgafl acaafllldv rfqqissvrd rrravlldlg fsglwsflwf
      121 vgfcfltnqw qrtapgpatt qagdaaraai afsffsilsw valtvkalqr frlgtdmslf
      181 ateqlstgas qaypgypvgs gvegtetyqs ppftetldts pkgyqvpay
//
LOCUS       NP_060830                528 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-taxilin isoform 1 [Homo sapiens].
ACCESSION   NP_060830
VERSION     NP_060830.2
DBSOURCE    REFSEQ: accession NM_018360.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Tao,J., Gu,P., Lai,H., Peng,H., Guo,Z., Yuan,Y., Yu,X., Shen,X.,
            Liu,J., Xier,Z., Li,G. and Yang,Y.
  TITLE     TXLNG improves insulin resistance in obese subjects in vitro and in
            vivo by inhibiting ATF4 transcriptional activity
  JOURNAL   Mol Cell Endocrinol 568-569, 111928 (2023)
   PUBMED   37028586
  REMARK    GeneRIF: TXLNG improves insulin resistance in obese subjects in
            vitro and in vivo by inhibiting ATF4 transcriptional activity.
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Ma,D., Wang,F., Wang,R., Hu,Y., Chen,Z., Huang,N., Tian,Y., Xia,Y.,
            Teng,J. and Chen,J.
  TITLE     alpha-/gamma-Taxilin are required for centriolar subdistal
            appendage assembly and microtubule organization
  JOURNAL   Elife 11, e73252 (2022)
   PUBMED   35119360
  REMARK    GeneRIF: alpha-/gamma-Taxilin are required for centriolar subdistal
            appendage assembly and microtubule organization.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Makiyama,T., Higashi,S., Sakane,H., Nogami,S. and Shirataki,H.
  TITLE     gamma-Taxilin temporally regulates centrosome disjunction in a
            Nek2A-dependent manner
  JOURNAL   Exp Cell Res 362 (2), 412-423 (2018)
   PUBMED   29225051
  REMARK    GeneRIF: Taken together with the result that gamma-taxilin protein
            expression levels were decreased at the onset of mitosis, we
            propose that gamma-taxilin participates in Nek2A-mediated
            centrosome disjunction as a negative regulator through its
            interaction with Nek2A.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Du,K., Chai,Y., Hou,L., Chang,W., Chen,S., Luo,W., Cai,T.,
            Zhang,X., Chen,N., Chen,Y. and Chen,J.
  TITLE     Over-expression and siRNA of a novel environmental
            lipopolysaccharide-responding gene on the cell cycle of the human
            hepatoma-derived cell line HepG2
  JOURNAL   Toxicology 243 (3), 303-310 (2008)
   PUBMED   18068885
  REMARK    GeneRIF: evaluation of the effects of a novel environmental
            lipopolysaccharide-responding (Elrg) gene on the regulation of
            proliferation and cell cycle of the hepatoma-derived cell line,
            HepG2
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Yu,V.W., Gauthier,C. and St-Arnaud,R.
  TITLE     Inhibition of ATF4 transcriptional activity by FIAT/gamma-taxilin
            modulates bone mass accrual
  JOURNAL   Ann N Y Acad Sci 1068, 131-142 (2006)
   PUBMED   16831913
REFERENCE   9  (residues 1 to 528)
  AUTHORS   Yu,V.W., Ambartsoumian,G., Verlinden,L., Moir,J.M., Prud'homme,J.,
            Gauthier,C., Roughley,P.J. and St-Arnaud,R.
  TITLE     FIAT represses ATF4-mediated transcription to regulate bone mass in
            transgenic mice
  JOURNAL   J Cell Biol 169 (4), 591-601 (2005)
   PUBMED   15911876
REFERENCE   10 (residues 1 to 528)
  AUTHORS   Nogami,S., Satoh,S., Tanaka-Nakadate,S., Yoshida,K., Nakano,M.,
            Terano,A. and Shirataki,H.
  TITLE     Identification and characterization of taxilin isoforms
  JOURNAL   Biochem Biophys Res Commun 319 (3), 936-943 (2004)
   PUBMED   15184072
  REMARK    GeneRIF: identification of isoforms of taxilin; interaction with
            syntaxin; tissue distribution [beta-taxilin, gamma-taxilin].
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC101576.1, AF143740.2,
            DA516680.1, AK123142.1, AW197225.1 and AA731379.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 15, 2009 this sequence version replaced NP_060830.1.
            
            Summary: This gene encodes a member of the taxilin family. The
            encoded protein binds to the C-terminal coiled-coil region of
            syntaxin family members 1A, 3A and 4A, and may play a role in
            intracellular vesicle trafficking. This gene is up-regulated by
            lipopolysaccharide and the gene product may be involved in cell
            cycle regulation. The related mouse protein was also shown to
            inhibit activating transcription factor 4-mediated transcription
            and thus regulate bone mass accrual. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.131237.1,
                                           SRR1660805.89071.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380122.10/ ENSP00000369465.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..528
                     /product="gamma-taxilin isoform 1"
                     /note="lipopolysaccharide specific response-5 protein;
                     gamma-taxilin; factor inhibiting activating transcription
                     factor 4 (ATF4)-mediated transcription; environmental
                     LPS-responding; lipopolysaccharide-specific response
                     protein 5; factor inhibiting ATF4-mediated transcription;
                     environmental lipopolysaccharide-responding gene protein"
                     /calculated_mol_wt=60455
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            24
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            79
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BHN1; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Region          102..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Region          137..444
                     /region_name="Taxilin"
                     /note="Myosin-like coiled-coil protein; pfam09728"
                     /db_xref="CDD:462861"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Region          486..528
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     Site            517
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9NUQ3.2)"
     CDS             1..528
                     /gene="TXLNG"
                     /gene_synonym="CXorf15; ELRG; FIAT; LSR5; TXLNGX"
                     /coded_by="NM_018360.3:23..1609"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14178.1"
                     /db_xref="GeneID:55787"
                     /db_xref="HGNC:HGNC:18578"
                     /db_xref="MIM:300677"
ORIGIN      
        1 matrveeaar grgggaeeat eagrggrrrs prqkfeigtm eeagicglgv kadmlcnsqs
       61 ndilqhqgsn cggtsnkhsl eedegsdfit enrnlvspay ctqesreeip ggeartdppd
      121 gqqdsecnrn kektlgkevl llmqalntls tpeeklaalc kkyadllees rsvqkqmkil
      181 qkkqaqivke kvhlqsehsk ailarskles lcrelqrhnk tlkeenmqqa reeeerrkea
      241 tahfqitlne iqaqleqhdi hnaklrqeni elgeklkkli eqyalreehi dkvfkhkelq
      301 qqlvdaklqq ttqlikeade khqrerefll keatesrhky eqmkqqevql kqqlslymdk
      361 feefqttmak snelfttfrq emekmtkkik kleketiiwr tkwennnkal lqmaeektvr
      421 dkeykalqik lerleklcra lqternelne kvevlkeqvs ikaaikaanr dlatpvmqpc
      481 taldshkeln tsskralgah leaepksqrs avqkppstgs apaiesvd
//
LOCUS       NP_060322               1062 aa            linear   PRI 20-NOV-2025
DEFINITION  NACHT, LRR and PYD domains-containing protein 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_060322
VERSION     NP_060322.1
DBSOURCE    REFSEQ: accession NM_017852.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1062)
  AUTHORS   Rui,X., Zhang,X., Jia,X., Han,J., Wang,C., Cao,Q., Zhong,O.,
            Ding,J., Zhao,C., Zhang,J., Ling,X., Li,H., Ma,X., Meng,Q. and
            Huo,R.
  TITLE     Variants in NLRP2 and ZFP36L2, non-core components of the human
            subcortical maternal complex, cause female infertility with
            embryonic development arrest
  JOURNAL   Mol Hum Reprod 30 (9) (2024)
   PUBMED   39178021
  REMARK    GeneRIF: Variants in NLRP2 and ZFP36L2, non-core components of the
            human subcortical maternal complex, cause female infertility with
            embryonic development arrest.
REFERENCE   2  (residues 1 to 1062)
  AUTHORS   Gu,B., Le,G.H., Herrera,S., Blair,S.J., Meissner,T.B. and
            Strominger,J.L.
  TITLE     HLA-C expression in extravillous trophoblasts is determined by an
            ELF3-NLRP2/NLRP7 regulatory axis
  JOURNAL   Proc Natl Acad Sci U S A 121 (31), e2404229121 (2024)
   PUBMED   39052836
  REMARK    GeneRIF: HLA-C expression in extravillous trophoblasts is
            determined by an ELF3-NLRP2/NLRP7 regulatory axis.
REFERENCE   3  (residues 1 to 1062)
  AUTHORS   Rossi,M.N., Matteo,V., Diomedi-Camassei,F., De Leo,E., Devuyst,O.,
            Lamkanfi,M., Caiello,I., Loricchio,E., Bellomo,F., Taranta,A.,
            Emma,F., De Benedetti,F. and Prencipe,G.
  TITLE     Nlrp2 deletion ameliorates kidney damage in a mouse model of
            cystinosis
  JOURNAL   Front Immunol 15, 1373224 (2024)
   PUBMED   38633264
  REMARK    GeneRIF: Nlrp2 deletion ameliorates kidney damage in a mouse model
            of cystinosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1062)
  AUTHORS   Fontalba,A., Gutierrez,O. and Fernandez-Luna,J.L.
  TITLE     NLRP2, an inhibitor of the NF-kappaB pathway, is transcriptionally
            activated by NF-kappaB and exhibits a nonfunctional allelic variant
  JOURNAL   J Immunol 179 (12), 8519-8524 (2007)
   PUBMED   18056399
  REMARK    GeneRIF: These findings provide molecular insight into the
            expression of NLRP2 by NF-kappaB.
            GeneRIF: Observational study of genotype prevalence. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 1062)
  AUTHORS   Kinoshita,T., Wang,Y., Hasegawa,M., Imamura,R. and Suda,T.
  TITLE     PYPAF3, a PYRIN-containing APAF-1-like protein, is a feedback
            regulator of caspase-1-dependent interleukin-1beta secretion
  JOURNAL   J Biol Chem 280 (23), 21720-21725 (2005)
   PUBMED   15817483
  REMARK    GeneRIF: PYPAF3 is a feedback regulator of interleukin-1beta
            secretion, and PYPAF2 and PYPAF3, together with PYNOD, constitute
            an anti-inflammatory subgroup of PYRIN-containing apoptotic
            protease-activating factor-1-like proteins
REFERENCE   6  (residues 1 to 1062)
  AUTHORS   Bruey,J.M., Bruey-Sedano,N., Newman,R., Chandler,S., Stehlik,C. and
            Reed,J.C.
  TITLE     PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that
            regulates NF-kappaB and caspase-1 activation in macrophages
  JOURNAL   J Biol Chem 279 (50), 51897-51907 (2004)
   PUBMED   15456791
  REMARK    GeneRIF: functions as a modulator of the activation of NF-kappaB
            and pro-caspase-1 in macrophages
REFERENCE   7  (residues 1 to 1062)
  AUTHORS   Agostini,L., Martinon,F., Burns,K., McDermott,M.F., Hawkins,P.N.
            and Tschopp,J.
  TITLE     NALP3 forms an IL-1beta-processing inflammasome with increased
            activity in Muckle-Wells autoinflammatory disorder
  JOURNAL   Immunity 20 (3), 319-325 (2004)
   PUBMED   15030775
REFERENCE   8  (residues 1 to 1062)
  AUTHORS   Martinon,F., Hofmann,K. and Tschopp,J.
  TITLE     The pyrin domain: a possible member of the death domain-fold family
            implicated in apoptosis and inflammation
  JOURNAL   Curr Biol 11 (4), R118-R120 (2001)
   PUBMED   11250163
REFERENCE   9  (residues 1 to 1062)
  AUTHORS   Bertin,J. and DiStefano,P.S.
  TITLE     The PYRIN domain: a novel motif found in apoptosis and inflammation
            proteins
  JOURNAL   Cell Death Differ 7 (12), 1273-1274 (2000)
   PUBMED   11270363
  REMARK    Review article
REFERENCE   10 (residues 1 to 1062)
  AUTHORS   Tumer,Z., Eggermann,T., Maas,S., Bliek,J. and Mackay,D.
  TITLE     Maternal Effect Gene-Related Multilocus Imprinting Disturbances
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40373180
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB066882.1, DB046128.1,
            AF310106.1, BC001039.2 and AK025952.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene is a member of the nucleotide-binding and
            leucine-rich repeat receptor (NLR) family, and is predicted to
            contain an N-terminal pyrin effector domain (PYD), a
            centrally-located nucleotide-binding and oligomerization domain
            (NACHT) and C-terminal leucine-rich repeats (LRR). Members of this
            gene family are thought to be important regulators of immune
            responses. This gene product interacts with components of the IkB
            kinase (IKK) complex, and can regulate both caspase-1 and NF-kB
            (nuclear factor kappa-light-chain-enhancer of activated B cells)
            activity. The pyrin domain is necessary and sufficient for
            suppression of NF-kB activity. An allelic variant (rs147585490) has
            been found that is incapable of blocking the transcriptional
            activity of NF-kB. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Dec 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1). Both variants 1 and 2 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF310106.1, SRR1803616.253406.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000448584.7/ ENSP00000409370.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1062
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..1062
                     /product="NACHT, LRR and PYD domains-containing protein 2
                     isoform 1"
                     /note="NACHT, leucine rich repeat and PYD containing 2;
                     nucleotide-binding oligomerization domain, leucine rich
                     repeat and pyrin domain containing 2; NACHT, LRR and PYD
                     domains-containing protein 2; nucleotide-binding site
                     protein 1; PYRIN-containing APAF1-like protein 2; PYRIN
                     domain and NACHT domain-containing protein 1"
                     /calculated_mol_wt=120385
     Region          11..94
                     /region_name="Pyrin_NALPs"
                     /note="Pyrin death domain found in NALP proteins; cd08320"
                     /db_xref="CDD:260032"
     Region          46..>553
                     /region_name="NACHT"
                     /note="Predicted NTPase, NACHT family domain [Signal
                     transduction mechanisms]; COG5635"
                     /db_xref="CDD:444362"
     Region          207..375
                     /region_name="NACHT"
                     /note="NACHT domain; pfam05729"
                     /db_xref="CDD:428606"
     Region          503..620
                     /region_name="NLRC4_HD2"
                     /note="NLRC4 helical domain HD2; pfam17776"
                     /db_xref="CDD:465499"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          757..784
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          785..812
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          788..1018
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          812..832
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          813..837
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          841..861
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          842..869
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          869..889
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          870..898
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          898..918
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          899..926
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          926..946
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          927..955
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          955..976
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          956..983
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          983..1003
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     Region          1010..1033
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NX02.1)"
     CDS             1..1062
                     /gene="NLRP2"
                     /gene_synonym="CLR19.9; NALP2; NBS1; OZEMA18; PAN1;
                     PYPAF2"
                     /coded_by="NM_017852.5:112..3300"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12913.1"
                     /db_xref="GeneID:55655"
                     /db_xref="HGNC:HGNC:22948"
                     /db_xref="MIM:609364"
ORIGIN      
        1 mvssaqmgfn lqalleqlsq delskfkyli ttfslahelq kiphkevdka dgkqlveilt
       61 thcdsywvem aslqvfekmh rmdlserakd evreaalksf nkrkplslgi trkerppldv
      121 demlerfkte aqaftetkgn viclgkevfk gkkpdkdnrc ryilktkfre mwkswpgdsk
      181 evqvmaeryk mlipfsnprv lpgpfsytvv lygpaglgkt tlaqklmldw aednlihkfk
      241 yafylscrel srlgpcsfae lvfrdwpelq ddiphilaqa rkilfvidgf delgaapgal
      301 iedicgdwek kkpvpvllgs llnrvmlpka allvttrpra lrdlrilaee piyirvegfl
      361 eedrrayflr hfgdedqamr afelmrsnaa lfqlgsapav cwivcttlkl qmekgedpvp
      421 tcltrtglfl rflcsrfpqg aqlrgalrtl sllaaqglwa qtsvlhredl erlgvqesdl
      481 rlfldgdilr qdrvskgcys fihlsfqqfl talfytleke eeedrdghtw digdvqklls
      541 gverlrnpdl iqagyysfgl anekrakele atfgcrmspd ikqellrcdi sckgghstvt
      601 dlqellgcly esqeeelvke vmaqfkeisl hlnavdvvps sfcvkhcrnl qkmslqvike
      661 nlpenvtase sdaeversqd dqhmlpfwtd lcsifgsnkd lmglaindsf lsaslvrilc
      721 eqiasdtchl qrvvfknisp adahrnlcla lrghktvtyl tlqgndqddm fpalcevlrh
      781 pecnlrylgl vscsattqqw adlslalevn qsltcvnlsd nelldegakl lyttlrhpkc
      841 flqrlslenc hlteanckdl aavlvvsrel thlclaknpi gntgvkflce glrypecklq
      901 tlvlwncdit sdgccdltkl lqekssllcl dlglnhigvk gmkflcealr kplcnlrclw
      961 lwgcsippfs cedlcsalsc nqslvtldlg qnplgssgvk mlfetltcss gtlrtlrlki
     1021 ddfndelnkl leeieeknpq liidtekhhp waerpsshdf mi
//
LOCUS       NP_001138570             664 aa            linear   PRI 20-NOV-2025
DEFINITION  ski-like protein isoform 3 [Homo sapiens].
ACCESSION   NP_001138570
VERSION     NP_001138570.1
DBSOURCE    REFSEQ: accession NM_001145098.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Chi,C., Liang,X., Cui,T., Gao,X., Liu,R. and Yin,C.
  TITLE     SKIL/SnoN attenuates TGF-beta1/SMAD signaling-dependent collagen
            synthesis in hepatic fibrosis
  JOURNAL   Biomol Biomed 23 (6), 1014-1025 (2023)
   PUBMED   37389959
  REMARK    GeneRIF: SKIL/SnoN attenuates TGF-beta1/SMAD signaling-dependent
            collagen synthesis in hepatic fibrosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 664)
  AUTHORS   Lu,Z., Zhang,Y., Yan,H., Su,Y., Guo,L., Liao,Y., Lu,T., Yu,H.,
            Wang,L., Li,J., Li,W., Yang,Y., Xiao,X., Lv,L., Tan,Y., Zhang,D.
            and Yue,W.
  TITLE     ATAD3B and SKIL polymorphisms associated with antipsychotic-induced
            QTc interval change in patients with schizophrenia: a genome-wide
            association study
  JOURNAL   Transl Psychiatry 12 (1), 56 (2022)
   PUBMED   35136033
  REMARK    GeneRIF: ATAD3B and SKIL polymorphisms associated with
            antipsychotic-induced QTc interval change in patients with
            schizophrenia: a genome-wide association study.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Ma,F., Ding,M.G., Lei,Y.Y., Luo,L.H., Jiang,S., Feng,Y.H. and
            Liu,X.L.
  TITLE     SKIL facilitates tumorigenesis and immune escape of NSCLC via
            upregulating TAZ/autophagy axis
  JOURNAL   Cell Death Dis 11 (12), 1028 (2020)
   PUBMED   33268765
  REMARK    GeneRIF: SKIL facilitates tumorigenesis and immune escape of NSCLC
            via upregulating TAZ/autophagy axis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Cohen,S.B., Zheng,G., Heyman,H.C. and Stavnezer,E.
  TITLE     Heterodimers of the SnoN and Ski oncoproteins form preferentially
            over homodimers and are more potent transforming agents
  JOURNAL   Nucleic Acids Res 27 (4), 1006-1014 (1999)
   PUBMED   9927733
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Pearson-White,S. and Crittenden,R.
  TITLE     Proto-oncogene Sno expression, alternative isoforms and immediate
            early serum response
  JOURNAL   Nucleic Acids Res 25 (14), 2930-2937 (1997)
   PUBMED   9207045
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Pearson-White,S.
  TITLE     SnoI, a novel alternatively spliced isoform of the ski
            protooncogene homolog, sno
  JOURNAL   Nucleic Acids Res 21 (19), 4632-4638 (1993)
   PUBMED   8233802
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Nagase,T., Nomura,N. and Ishii,S.
  TITLE     Complex formation between proteins encoded by the ski gene family
  JOURNAL   J Biol Chem 268 (18), 13710-13716 (1993)
   PUBMED   8514802
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Nomura,N., Sasamoto,S., Ishii,S., Date,T., Matsui,M. and
            Ishizaki,R.
  TITLE     Isolation of human cDNA clones of ski and the ski-related gene, sno
  JOURNAL   Nucleic Acids Res 17 (14), 5489-5500 (1989)
   PUBMED   2762147
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA464211.1, AK300053.1,
            AC073288.27 and AI245308.1.
            
            Summary: The protein encoded by this gene is a component of the
            SMAD pathway, which regulates cell growth and differentiation
            through transforming growth factor-beta (TGFB). In the absence of
            ligand, the encoded protein binds to the promoter region of
            TGFB-responsive genes and recruits a nuclear repressor complex.
            TGFB signaling causes SMAD3 to enter the nucleus and degrade this
            protein, allowing these genes to be activated. Four transcript
            variants encoding three different isoforms have been found for this
            gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region, and uses a downstream start codon compared to
            variant 1. The resulting protein (isoform 3) is shorter compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK300053.1, SRR1803613.111760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.2"
     Protein         1..664
                     /product="ski-like protein isoform 3"
                     /note="ski-like protein; ski-related oncogene snoN;
                     SKI-like oncogene"
                     /calculated_mol_wt=74654
     Region          117..216
                     /region_name="DHD_Sno"
                     /note="Dachshund-homology domain found in Ski-like protein
                     (Sno) and similar proteins; cd21084"
                     /db_xref="CDD:410787"
     Region          241..336
                     /region_name="c-SKI_SMAD_bind"
                     /note="c-SKI Smad4 binding domain; smart01046"
                     /db_xref="CDD:198114"
     Region          335..>664
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          <516..>664
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..664
                     /gene="SKIL"
                     /gene_synonym="SNO; SnoA; SnoI; SnoN"
                     /coded_by="NM_001145098.3:252..2246"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS46954.1"
                     /db_xref="GeneID:6498"
                     /db_xref="HGNC:HGNC:10897"
                     /db_xref="MIM:165340"
ORIGIN      
        1 mgddgsppak kmitdihang ktinkvptvk kehlddygea pvetdgehvk rtctsvpetl
       61 hlnpslkhtl aqfhlssqss lggpaafsar hsqesmsptv flplpspqvl pgpllipsds
      121 steltqtvle gesiscfqvg gekrlclpqv lnsvlreftl qqintvcdel yiycsrctsd
      181 qlhilkvlgi lpfnapscgl itltdaqrlc nallrprtfp qngsvlpaks slaqlketgs
      241 afeveheclg kcqglfapqf yvqpdapciq cleccgmfap qtfvmhshrs pdkrtchwgf
      301 esakwhcylh vnqkylgtpe ekklkiilee mkekfsmrsg krnqsktdap sgmelqswyp
      361 vikqegdhvs qthsflhpsy ylymcdkvva pnvsltsavs qskeltktea sksisrqsek
      421 ahssgklqkt vsypdvslee qekmdlktsr elcsrldasi snnstskrks esatcnlvrd
      481 inkvgiglva aasspllvkd viceddkgki meevmrtylk qqeklnlilq kkqqlqmevk
      541 mlsssksmke lteeqqnlqk eleslqneha qrmeefyveq kdlekkleqi mkqkctcdsn
      601 lekdkeaeya gqlaelrqrl dhaeadrqel qdelrqerea rqklemmike lklqilkssk
      661 take
//
LOCUS       NP_001309809             271 aa            linear   PRI 20-NOV-2025
DEFINITION  zeta-sarcoglycan isoform 3 [Homo sapiens].
ACCESSION   NP_001309809
VERSION     NP_001309809.1
DBSOURCE    REFSEQ: accession NM_001322880.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Peall,K.J., Ritz,K., Waite,A.J., Groen,J.L., Morris,H.R., Baas,F.,
            Blake,D.J. and Tijssen,M.A.
  TITLE     SGCZ mutations are unlikely to be associated with myoclonus
            dystonia
  JOURNAL   Neuroscience 272, 88-91 (2014)
   PUBMED   24792710
  REMARK    GeneRIF: No pathogenic SGCZ mutations were identified
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Ikeda,M., Okahisa,Y., Aleksic,B., Won,M., Kondo,N., Naruse,N.,
            Aoyama-Uehara,K., Sora,I., Iyo,M., Hashimoto,R., Kawamura,Y.,
            Nishida,N., Miyagawa,T., Takeda,M., Sasaki,T., Tokunaga,K.,
            Ozaki,N., Ujike,H. and Iwata,N.
  TITLE     Evidence for shared genetic risk between methamphetamine-induced
            psychosis and schizophrenia
  JOURNAL   Neuropsychopharmacology 38 (10), 1864-1870 (2013)
   PUBMED   23594818
REFERENCE   3  (residues 1 to 271)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   4  (residues 1 to 271)
  AUTHORS   Zhao,W., Wineinger,N.E., Tiwari,H.K., Mosley,T.H., Broeckel,U.,
            Arnett,D.K., Kardia,S.L., Kabagambe,E.K. and Sun,Y.V.
  TITLE     Copy number variations associated with obesity-related traits in
            African Americans: a joint analysis between GENOA and HyperGEN
  JOURNAL   Obesity (Silver Spring) 20 (12), 2431-2437 (2012)
   PUBMED   22836685
  REMARK    GeneRIF: three CNVs associated with BMI, obesity, and other
            obesity-related traits after adjusting for multiple testing. These
            CNVs overlap the PARK2, GYPA, and SGCZ genes
REFERENCE   5  (residues 1 to 271)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 271)
  AUTHORS   Pilgram,G.S., Potikanond,S., Baines,R.A., Fradkin,L.G. and
            Noordermeer,J.N.
  TITLE     The roles of the dystrophin-associated glycoprotein complex at the
            synapse
  JOURNAL   Mol Neurobiol 41 (1), 1-21 (2010)
   PUBMED   19899002
  REMARK    Review article
REFERENCE   7  (residues 1 to 271)
  AUTHORS   Aurino,S., Piluso,G., Saccone,V., Cacciottolo,M., D'Amico,F.,
            Dionisi,M., Totaro,A., Belsito,A., Di Vicino,U. and Nigro,V.
  TITLE     Candidate-gene testing for orphan limb-girdle muscular dystrophies
  JOURNAL   Acta Myol 27 (3), 90-97 (2008)
   PUBMED   19472918
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 271)
  AUTHORS   Baulac,S., Gourfinkel-An,I., Couarch,P., Depienne,C., Kaminska,A.,
            Dulac,O., Baulac,M., LeGuern,E. and Nabbout,R.
  TITLE     A novel locus for generalized epilepsy with febrile seizures plus
            in French families
  JOURNAL   Arch Neurol 65 (7), 943-951 (2008)
   PUBMED   18625863
REFERENCE   9  (residues 1 to 271)
  AUTHORS   Anastasi,G., Cutroneo,G., Sidoti,A., Rinaldi,C., Bruschetta,D.,
            Rizzo,G., D'Angelo,R., Tarone,G., Amato,A. and Favaloro,A.
  TITLE     Sarcoglycan subcomplex expression in normal human smooth muscle
  JOURNAL   J Histochem Cytochem 55 (8), 831-843 (2007)
   PUBMED   17438352
REFERENCE   10 (residues 1 to 271)
  AUTHORS   Wheeler,M.T., Zarnegar,S. and McNally,E.M.
  TITLE     Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is
            reduced in muscular dystrophy
  JOURNAL   Hum Mol Genet 11 (18), 2147-2154 (2002)
   PUBMED   12189167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020992.10, AY502063.1,
            AY028700.1, AC023538.7 and AI580904.1.
            
            Summary: The zeta-sarcoglycan gene measures over 465 kb and
            localizes to 8p22. This protein is part of the sarcoglycan complex,
            a group of 6 proteins. The sarcoglycans are all N-glycosylated
            transmembrane proteins with a short intra-cellular domain, a single
            transmembrane region and a large extra-cellular domain containing a
            carboxyl-terminal cluster with several conserved cysteine residues.
            The sarcoglycan complex is part of the dystrophin-associated
            glycoprotein complex (DGC), which bridges the inner cytoskeleton
            and the extra-cellular matrix. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.85521.1,
                                           SRR1803611.146720.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1970526,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..271
                     /product="zeta-sarcoglycan isoform 3"
                     /note="zeta-sarcoglycan; zeta-SG"
                     /calculated_mol_wt=29927
     Region          38..258
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     CDS             1..271
                     /gene="SGCZ"
                     /gene_synonym="ZSG1"
                     /coded_by="NM_001322880.2:809..1624"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:137868"
                     /db_xref="HGNC:HGNC:14075"
                     /db_xref="MIM:608113"
ORIGIN      
        1 mdrstnldie elkmtreqyi latqqnnlpr tenaqlypvg iygwrkrcly ffvllllvtm
       61 ivnlamtiwi lkvmnftvdg mgnlrvtkkg irlegisefl lplyvkeihs rkdsplvlqs
      121 drnvtvnarn hmgqltgqlt igtegavfgh svetphirae psqdlrlesp trslimeapr
      181 gvqvsaaagd fkatcrkelh lqstegeifl naetiklgnl ptgsfssssp sssssrqtvy
      241 elcvcpngkl ylspagvgst cqsssniclw s
//
LOCUS       NP_647594                550 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 2 [Homo sapiens].
ACCESSION   NP_647594
VERSION     NP_647594.1
DBSOURCE    REFSEQ: accession NM_139344.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 550)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 550)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 550)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 550)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 550)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 550)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 550)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 550)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 550)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 550)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CF594020.1, AF043901.1,
            AC012508.10, AF070576.1 and BM711160.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            coding region, compared to variant 1. Isoform 2, also called IId
            and S1/R3-6, is shorter than isoform 1 and binds dynamin,
            synaptojanin, and clathrin.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043901.1, SRR14372080.4179710.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..550
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..550
                     /product="myc box-dependent-interacting protein 1 isoform
                     2"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=59806
     Region          31..272
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,228,231..232,234,239..240,242..243,246..247,
                     249..250,253..254,256..257,261,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <260..448
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          478..549
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(489..495,514,516..519,542,544..545)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..550
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_139344.3:212..1864"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS2139.1"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakpvsllek
      181 aapqwcqgkl qahlvaqtnl lrnqaeeeli kaqkvfeemn vdlqeelpsl wnsrvgfyvn
      241 tfqsiaglee nfhkemskln qnlndvlvgl ekqhgsntft vkaqpsdnap akgnkspspp
      301 dgspaatpei rvnhepepag gatpgatlpk spsqfeapgp fseqaslldl dfdplppvts
      361 pvkaptpsgq sipwdlwept espagslpsg epsaaegtfa vswpsqtaep gpaqpaease
      421 vaggtqpaag aqepgetaas eaassslpav vvetfpatvn gtveggsgag rldlppgfmf
      481 kvqaqhdyta tdtdelqlka gdvvlvipfq npeeqdegwl mgvkesdwnq hkelekcrgv
      541 fpenftervp
//
LOCUS       NP_694972               1330 aa            linear   PRI 20-NOV-2025
DEFINITION  nephrocystin-3 [Homo sapiens].
ACCESSION   NP_694972 NP_689743
VERSION     NP_694972.3
DBSOURCE    REFSEQ: accession NM_153240.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1330)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1330)
  AUTHORS   Thuy,P.X., Jang,T.K. and Moon,E.Y.
  TITLE     Vinblastine Resistance Is Associated with Nephronophthisis
            3-Mediated Primary Cilia via Intraflagellar Transport Protein 88
            and Apoptosis-Antagonizing Transcription Factor
  JOURNAL   Int J Mol Sci 25 (19), 10369 (2024)
   PUBMED   39408701
  REMARK    GeneRIF: Vinblastine Resistance Is Associated with Nephronophthisis
            3-Mediated Primary Cilia via Intraflagellar Transport Protein 88
            and Apoptosis-Antagonizing Transcription Factor.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1330)
  AUTHORS   Lee,J.W., Cho,J.Y., Thuy,P.X. and Moon,E.Y.
  TITLE     HeLa Cervical Cancer Cells Are Maintained by Nephronophthisis
            3-Associated Primary Cilium Formation via ROS-Induced ERK and
            HIF-1alpha Activation under Serum-Deprived Normoxic Condition
  JOURNAL   Int J Mol Sci 23 (23), 14500 (2022)
   PUBMED   36498831
  REMARK    GeneRIF: HeLa Cervical Cancer Cells Are Maintained by
            Nephronophthisis 3-Associated Primary Cilium Formation via
            ROS-Induced ERK and HIF-1alpha Activation under Serum-Deprived
            Normoxic Condition.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1330)
  AUTHORS   Olinger,E., Alawi,I.A., Al Riyami,M.S., Salmi,I.A., Molinari,E.,
            Faqeih,E.A., Al-Hamed,M.H., Barroso-Gil,M., Powell,L.,
            Al-Hussaini,A.A., Rahim,K.A., Almontashiri,N.A.M., Miles,C.,
            Shril,S., Hildebrandt,F., Consortium,G.E.R., Wilson,I.J. and
            Sayer,J.A.
  TITLE     A discarded synonymous variant in NPHP3 explains nephronophthisis
            and congenital hepatic fibrosis in several families
  JOURNAL   Hum Mutat 42 (10), 1221-1228 (2021)
   PUBMED   34212438
  REMARK    GeneRIF: A discarded synonymous variant in NPHP3 explains
            nephronophthisis and congenital hepatic fibrosis in several
            families.
REFERENCE   5  (residues 1 to 1330)
  AUTHORS   Olbrich,H., Fliegauf,M., Hoefele,J., Kispert,A., Otto,E., Volz,A.,
            Wolf,M.T., Sasmaz,G., Trauer,U., Reinhardt,R., Sudbrak,R.,
            Antignac,C., Gretz,N., Walz,G., Schermer,B., Benzing,T.,
            Hildebrandt,F. and Omran,H.
  TITLE     Mutations in a novel gene, NPHP3, cause adolescent
            nephronophthisis, tapeto-retinal degeneration and hepatic fibrosis
  JOURNAL   Nat Genet 34 (4), 455-459 (2003)
   PUBMED   12872122
  REMARK    GeneRIF: Mutations in a novel gene, NPHP3, cause adolescent
            nephronophthisis, tapeto-retinal degeneration and hepatic fibrosis.
REFERENCE   6  (residues 1 to 1330)
  AUTHORS   Omran,H., Sasmaz,G., Haffner,K., Volz,A., Olbrich,H., Melkaoui,R.,
            Otto,E., Wienker,T.F., Korinthenberg,R., Brandis,M., Antignac,C.
            and Hildebrandt,F.
  TITLE     Identification of a gene locus for Senior-Loken syndrome in the
            region of the nephronophthisis type 3 gene
  JOURNAL   J Am Soc Nephrol 13 (1), 75-79 (2002)
   PUBMED   11752023
REFERENCE   7  (residues 1 to 1330)
  AUTHORS   Omran,H., Haffner,K., Burth,S., Fernandez,C., Fargier,B.,
            Villaquiran,A., Nothwang,H.G., Schnittger,S., Lehrach,H., Woo,D.,
            Brandis,M., Sudbrak,R. and Hildebrandt,F.
  TITLE     Human adolescent nephronophthisis: gene locus synteny with
            polycystic kidney disease in pcy mice
  JOURNAL   J Am Soc Nephrol 12 (1), 107-113 (2001)
   PUBMED   11134256
REFERENCE   8  (residues 1 to 1330)
  AUTHORS   Omran,H., Fernandez,C., Jung,M., Haffner,K., Fargier,B.,
            Villaquiran,A., Waldherr,R., Gretz,N., Brandis,M., Ruschendorf,F.,
            Reis,A. and Hildebrandt,F.
  TITLE     Identification of a new gene locus for adolescent nephronophthisis,
            on chromosome 3q22 in a large Venezuelan pedigree
  JOURNAL   Am J Hum Genet 66 (1), 118-127 (2000)
   PUBMED   10631142
REFERENCE   9  (residues 1 to 1330)
  AUTHORS   Stokman,M., Lilien,M. and Knoers,N.
  TITLE     Nephronophthisis-Related Ciliopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   27336129
REFERENCE   10 (residues 1 to 1330)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB114822.1, AY257864.1,
            AC055732.16 and EB387619.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Jun 13, 2008 this sequence version replaced
            NP_689743.1, NP_694972.2.
            
            Summary: This gene encodes a protein containing a coiled-coil (CC)
            domain, a tubulin-tyrosine ligase (TTL) domain, and a tetratrico
            peptide repeat (TPR) domain. The encoded protein interacts with
            nephrocystin, it is required for normal ciliary development, and it
            functions in renal tubular development. Mutations in this gene are
            associated with nephronophthisis type 3, and also with
            renal-hepatic-pancreatic dysplasia, and Meckel syndrome type 7.
            Naturally occurring read-through transcripts exist between this
            gene and the downstream ACAD11 (acyl-CoA dehydrogenase family,
            member 11) gene. [provided by RefSeq, Feb 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY257864.1, SRR14038196.2431912.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337331.10/ ENSP00000338766.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.1"
     Protein         1..1330
                     /product="nephrocystin-3"
                     /note="Meckel syndrome, type 7; cilia and flagella
                     associated protein 31; nephronophthisis 3 (adolescent)"
                     /calculated_mol_wt=150734
     Region          <81..>202
                     /region_name="PRK03918"
                     /note="DNA double-strand break repair ATPase Rad50"
                     /db_xref="CDD:235175"
     Region          471..504
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          885..918
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          920..942
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          943..976
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          943..971
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <951..1289
                     /region_name="FxSxx_TPR"
                     /note="FxSxx-COOH system tetratricopeptide repeat protein;
                     NF040586"
                     /db_xref="CDD:468560"
     Region          985..1018
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          985..1013
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1027..1079
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1027..1060
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1093..1126
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1093..1121
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1135..1168
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1135..1163
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(1136,1139..1140,1143..1144,1146,1175,1178,1182,
                     1185..1186,1188..1189,1220,1223..1224,1227..1228,1231)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          1173..1206
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1177..1210
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1219..1252
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1219..1247
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1261..1294
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     Region          1261..1289
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1296..1330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z494.1)"
     CDS             1..1330
                     /gene="NPHP3"
                     /gene_synonym="CFAP31; MKS7; NPH3; RHPD; RHPD1; SLSN3"
                     /coded_by="NM_153240.5:55..4047"
                     /db_xref="CCDS:CCDS3078.1"
                     /db_xref="GeneID:27031"
                     /db_xref="HGNC:HGNC:7907"
                     /db_xref="MIM:608002"
ORIGIN      
        1 mgtasslvsp aggeviedty gagggeacei pvevkpkarl lrnsfrrgag aaagagpgsl
       61 prgvgaggll gasfkstgss vpeleyaaae yerlrkeyei frvsknqell smgrreakld
      121 tenkrlrael qalqktyqki lrekesalea kyqameraat fehdrdkvkr qfkifretke
      181 neiqdllrak relesklqrl qaqgiqvfdp gesdsddnct dvtaagtqce ywtggalgse
      241 psigsmiqlq qsfrgpefah ssidvegpfa nvnrddwdia vasllqvtpl fshslwsntv
      301 rcyliytdet qpemdlflkd yspklkrmce tmgyffhavy fpidvenqyl tvrkweieks
      361 slvilfihlt lpsllledce eaflknpegk prlifhrled gkvssdsvqq lidqvsnlnk
      421 tskakiidhs gdpaegvykt yicvekiikq dilgfentdl etkdlgseds ipeeddfgdv
      481 lwdihdeqeq metfqqasns ahelgfekyy qrlndlvaap apippllvsg gpgsgkslll
      541 skwiqlqqkn spntlilshf vgrpmstsse ssliikrltl klmqhswsvs altldpakll
      601 eefprwlekl sarhqgsiii vidsidqvqq vekhmkwlid plpvnvrviv svnvetcppa
      661 wrlwptlhld plspkdaksi iiaechsvdi klskeqekkl erhcrsattc nalyvtlfgk
      721 miaragragn ldkilhqcfq cqdtlslyrl vlhsiresma ndvdkelmkq ilclvnvshn
      781 gvseselmel ypemswtflt slihslykmc lltygcgllr fqhlqawetv rleylegptv
      841 tssyrqklin yftlqlsqdr vtwrsadelp wlfqqqgskq klhdcllnlf vsqnlykrgh
      901 faellsywqf vgkdksamat eyfdslkqye kncegednms cladlyetlg rflkdlglls
      961 qaivplqrsl eiretaldpd hprvaqslhq lasvyvqwkk fgnaeqlykq aleisenayg
     1021 adhpytarel ealatlyqkq nkyeqaehfr kksfkihqka ikkkgnlygf allrrralql
     1081 eeltlgkdtp dnartlnelg vlyylqnnle tadqflkrsl emrervlgpd hpdcaqslnn
     1141 laalcnekkq ydkaeelyer aldirrrala pdhpslaytv khlailykkm gkldkavply
     1201 elaveirqks fgpkhpsvat alvnlavlys qmkkhvealp lyeralkiye dslgrmhprv
     1261 getlknlavl syeggdfeka aelykramei keaetsllgg kapsrhsssg dtfslktahs
     1321 pnvflqqgqr
//
LOCUS       NP_060440               1164 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear exosome regulator NRDE2 [Homo sapiens].
ACCESSION   NP_060440
VERSION     NP_060440.2
DBSOURCE    REFSEQ: accession NM_017970.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1164)
  AUTHORS   Wang,Y., Liu,X., Zuo,X., Wang,C., Zhang,Z., Zhang,H., Zeng,T.,
            Chen,S., Liu,M., Chen,H., Song,Q., Li,Q., Yang,C., Le,Y., Xing,J.,
            Zhang,H., An,J., Jia,W., Kang,L., Zhang,H., Xie,H., Ye,J., Wu,T.,
            He,F., Zhang,X., Li,Y. and Zhou,G.
  TITLE     NRDE2 deficiency impairs homologous recombination repair and
            sensitizes hepatocellular carcinoma to PARP inhibitors
  JOURNAL   Cell Genom 4 (5), 100550 (2024)
   PUBMED   38697125
  REMARK    GeneRIF: NRDE2 deficiency impairs homologous recombination repair
            and sensitizes hepatocellular carcinoma to PARP inhibitors.
REFERENCE   3  (residues 1 to 1164)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 1164)
  AUTHORS   Wang,J., Chen,J., Wu,G., Zhang,H., Du,X., Chen,S., Zhang,L.,
            Wang,K., Fan,J., Gao,S., Wu,X., Zhang,S., Kuai,B., Zhao,P., Chi,B.,
            Wang,L., Li,G., Wong,C.C.L., Zhou,Y., Li,J., Yun,C. and Cheng,H.
  TITLE     NRDE2 negatively regulates exosome functions by inhibiting MTR4
            recruitment and exosome interaction
  JOURNAL   Genes Dev 33 (9-10), 536-549 (2019)
   PUBMED   30842217
  REMARK    GeneRIF: NRDE2 interacts with MTR4's key residues, locks MTR4 in a
            closed conformation, and inhibits MTR4 interaction with the exosome
            as well as proteins important for MTR4 recruitment
REFERENCE   5  (residues 1 to 1164)
  AUTHORS   Jiao,A.L., Perales,R., Umbreit,N.T., Haswell,J.R., Piper,M.E.,
            Adams,B.D., Pellman,D., Kennedy,S. and Slack,F.J.
  TITLE     Human nuclear RNAi-defective 2 (NRDE2) is an essential RNA splicing
            factor
  JOURNAL   RNA 25 (3), 352-363 (2019)
   PUBMED   30538148
  REMARK    GeneRIF: Our work establishes a conserved role for human NRDE2 in
            RNA splicing, characterizes the severe genomic instability
            phenotypes observed upon loss of NRDE2, and highlights the direct
            regulation of CEP131 splicing as one of multiple mechanisms through
            which such phenotypes might be explained.
REFERENCE   6  (residues 1 to 1164)
  AUTHORS   Richard,P., Ogami,K., Chen,Y., Feng,S., Moresco,J.J., Yates,J.R.
            3rd and Manley,J.L.
  TITLE     NRDE-2, the human homolog of fission yeast Nrl1, prevents DNA
            damage accumulation in human cells
  JOURNAL   RNA Biol 15 (7), 868-876 (2018)
   PUBMED   29902117
  REMARK    GeneRIF: this study found that Mtr4 association with the human
            homolog of fission yeast Nrl1, NRDE-2, defines a novel function for
            Mtr4 in the DNA damage response pathway.
REFERENCE   7  (residues 1 to 1164)
  AUTHORS   Yashin,A.I., Wu,D., Arbeev,K.G. and Ukraintseva,S.V.
  TITLE     Joint influence of small-effect genetic variants on human longevity
  JOURNAL   Aging (Albany NY) 2 (9), 612-620 (2010)
   PUBMED   20834067
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK294958.1, BC008925.2, AW196499.1, AL161662.6 and AL355074.5.
            
            On Dec 16, 2003 this sequence version replaced NP_060440.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK294958.1, SRR1803616.261501.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000354366.8/ ENSP00000346335.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.11"
     Protein         1..1164
                     /product="nuclear exosome regulator NRDE2"
                     /note="UPF0614 protein C14orf102; protein NRDE2 homolog"
                     /calculated_mol_wt=132542
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          39..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          162..258
                     /region_name="NRDE2_MID"
                     /note="MTR4-interacting domain (MID) found in nuclear
                     exosome regulator NRDE2 and similar proteins; cd22200"
                     /db_xref="CDD:412062"
     Site            order(162..170,173..174,178..179,181,183..197,200..202,
                     204..206,214..216,220..221,223..224,227..233,242..245,
                     249..258)
                     /site_type="other"
                     /note="MTR4 binding site [polypeptide binding]"
                     /db_xref="CDD:412062"
     Region          163..266
                     /region_name="MID/MTR4-interacting domain.
                     /evidence=ECO:0000269|PubMed:30842217"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          279..305
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          305..337
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          313..645
                     /region_name="NRDE-2"
                     /note="necessary for RNA interference; pfam08424"
                     /db_xref="CDD:462472"
     Region          395..427
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          758..792
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          978..1010
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     Region          1067..1101
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H7Z3.3)"
     CDS             1..1164
                     /gene="NRDE2"
                     /gene_synonym="C14orf102"
                     /coded_by="NM_017970.4:38..3532"
                     /db_xref="CCDS:CCDS9890.1"
                     /db_xref="GeneID:55051"
                     /db_xref="HGNC:HGNC:20186"
                     /db_xref="MIM:618631"
ORIGIN      
        1 malfpafagl seapdggssr keldwlsnps fcvgsitsls qqteaapahv seglpltrsh
       61 lksessdesd tnkklkqtsr kkkkekkkkr khqhhkktkr khgpssssrs etdtdsekdk
      121 psrgvggskk eseepnqgnn aaadtghrfv wlediqavtg etfrtdkkpd panweyksly
      181 rgdiarykrk gdsclginpk kqciswegts tekkhsrkqv eryftkksvg lmnidgvais
      241 skteppssep isfipvkdle daapvttwln plgiydqstt hwlqgqgppe qeskqpdaqp
      301 dsesaalkak veefnrrvre nprdtqlwma fvafqdevmk spglyaieeg eqekrkrslk
      361 lilekklail eraiesnqss vdlklaklkl ctefwepstl vkewqklifl hpnntalwqk
      421 yllfcqsqfs tfsiskihsl ygkclstlsa vkdgsilshp alpgteeamf alflqqchfl
      481 rqaghsekai slfqamvdft ffkpdsvkdl ptkgqveffe pfwdsgepra gekgargwka
      541 wmhqqerggw vvinpdeddd epeeddqeik dktlprwqiw laaersrdqr hwrpwrpdkt
      601 kkqteedced perqvlfddi gqslirlssh dlqfqlveaf lqflgvpsgf tppasclyla
      661 mdensifdng lydekpltff nplfsgascv grmdrlgypr wtrgqnrege efirnvfhlv
      721 mplfsgkeks qlcfswlqye iakviwclht knkkrlksqg knckklaknl lkepencnnf
      781 clwkqyahle wllgntedar kvfdtalgma gsrelkdsdl celsllyael evelspevrr
      841 aataravhil tkltesspyg pytgqvlavh ilkarkayeh alqdclgdsc vsnpaptdsc
      901 srlislakcf mlfqyltigi daavqiyeqv faklnssvfp egsgegdsas sqswtsvlea
      961 itlmhtsllr fhmkvsvypl aplrealsqa lklypgnqvl wrsyvqiqnk shsasktrrf
     1021 fdtitrsakp lepwlfaiea eklrkrlvet vqrldgreih atipetglmh riqalfenam
     1081 rsdsgsqcpl lwrmylnflv slgnkerskg vfykalqncp wakvlyldav eyfpdemqei
     1141 ldlmtekelr vrlpleelel lled
//
LOCUS       NP_001300882             312 aa            linear   PRI 20-NOV-2025
DEFINITION  aurora kinase B isoform 5 [Homo sapiens].
ACCESSION   NP_001300882 XP_011522372
VERSION     NP_001300882.1
DBSOURCE    REFSEQ: accession NM_001313953.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Zhang,T., Liu,S., Durojaye,O., Xiong,F., Fang,Z., Ullah,T., Fu,C.,
            Sun,B., Jiang,H., Xia,P., Wang,Z., Yao,X. and Liu,X.
  TITLE     Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic
            gene reactivation
  JOURNAL   Cell Rep 43 (9), 114739 (2024)
   PUBMED   39276350
  REMARK    GeneRIF: Dynamic phosphorylation of FOXA1 by Aurora B guides
            post-mitotic gene reactivation.
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Zhu,G., Luo,L., He,Y., Xiao,Y., Cai,Z., Tong,W., Deng,W., Xie,J.,
            Zhong,Y., Hu,Z. and Shan,R.
  TITLE     AURKB targets DHX9 to promote hepatocellular carcinoma progression
            via PI3K/AKT/mTOR pathway
  JOURNAL   Mol Carcinog 63 (9), 1814-1826 (2024)
   PUBMED   38874176
  REMARK    GeneRIF: AURKB targets DHX9 to promote hepatocellular carcinoma
            progression via PI3K/AKT/mTOR pathway.
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Li,L., Jiang,P., Hu,W., Zou,F., Li,M., Rao,T., Ruan,Y., Yu,W.,
            Ning,J. and Cheng,F.
  TITLE     AURKB promotes bladder cancer progression by deregulating the p53
            DNA damage response pathway via MAD2L2
  JOURNAL   J Transl Med 22 (1), 295 (2024)
   PUBMED   38515112
  REMARK    GeneRIF: AURKB promotes bladder cancer progression by deregulating
            the p53 DNA damage response pathway via MAD2L2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Katayama,H., Ota,T., Morita,K., Terada,Y., Suzuki,F., Katoh,O. and
            Tatsuka,M.
  TITLE     Human AIM-1: cDNA cloning and reduced expression during endomitosis
            in megakaryocyte-lineage cells
  JOURNAL   Gene 224 (1-2), 1-7 (1998)
   PUBMED   9931403
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Li,F., Ambrosini,G., Chu,E.Y., Plescia,J., Tognin,S.,
            Marchisio,P.C. and Altieri,D.C.
  TITLE     Control of apoptosis and mitotic spindle checkpoint by survivin
  JOURNAL   Nature 396 (6711), 580-584 (1998)
   PUBMED   9859993
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Tatsuka,M., Katayama,H., Ota,T., Tanaka,T., Odashima,S., Suzuki,F.
            and Terada,Y.
  TITLE     Multinuclearity and increased ploidy caused by overexpression of
            the aurora- and Ipl1-like midbody-associated protein mitotic kinase
            in human cancer cells
  JOURNAL   Cancer Res 58 (21), 4811-4816 (1998)
   PUBMED   9809983
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Shindo,M., Nakano,H., Kuroyanagi,H., Shirasawa,T., Mihara,M.,
            Gilbert,D.J., Jenkins,N.A., Copeland,N.G., Yagita,H. and Okumura,K.
  TITLE     cDNA cloning, expression, subcellular localization, and chromosomal
            assignment of mammalian aurora homologues, aurora-related kinase
            (ARK) 1 and 2
  JOURNAL   Biochem Biophys Res Commun 244 (1), 285-292 (1998)
   PUBMED   9514916
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Kimura,M., Matsuda,Y., Yoshioka,T., Sumi,N. and Okano,Y.
  TITLE     Identification and characterization of STK12/Aik2: a human gene
            related to aurora of Drosophila and yeast IPL1
  JOURNAL   Cytogenet Cell Genet 82 (3-4), 147-152 (1998)
   PUBMED   9858806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC135178.13, BU153790.1 and
            BC009751.2.
            
            On Aug 4, 2017 this sequence version replaced XP_011522372.1.
            
            Summary: This gene encodes a member of the aurora kinase subfamily
            of serine/threonine kinases. The genes encoding the other two
            members of this subfamily are located on chromosomes 19 and 20.
            These kinases participate in the regulation of alignment and
            segregation of chromosomes during mitosis and meiosis through
            association with microtubules. A pseudogene of this gene is located
            on chromosome 8. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (7) uses alternate in-frame donor
            and acceptor splices sites in the mid-coding region compared to
            variant 1. The resulting isoform (5) is shorter containing a 16 aa
            protein segment not found in isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU153790.1, SRR5189658.29688.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..312
                     /product="aurora kinase B isoform 5"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine kinase 12; aurora-B; aurora-1;
                     aurora kinase B-Sv1; aurora kinase B-Sv2; aurora-related
                     kinase 2; aurora/IPL1-related kinase 2;
                     serine/threonine-protein kinase aurora-B; aurora- and
                     Ipl1-like midbody-associated protein 1;
                     serine/threonine-protein kinase 5; protein phosphatase 1,
                     regulatory subunit 48; serine/threonine-protein kinase 12;
                     aurora- and Ipl1-like midbody-associated protein 1
                     homolog"
                     /calculated_mol_wt=35171
     Region          70..307
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(83..85,86,88,106,122..125,168,172..173,175,185..186)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..312
                     /gene="AURKB"
                     /gene_synonym="AIK2; AIM-1; AIM1; ARK-2; ARK2; AurB;
                     aurkb-sv1; aurkb-sv2; IPL1; PPP1R48; STK-1; STK12; STK5"
                     /coded_by="NM_001313953.3:72..1010"
                     /note="isoform 5 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS82065.1"
                     /db_xref="GeneID:9212"
                     /db_xref="HGNC:HGNC:11390"
                     /db_xref="MIM:604970"
ORIGIN      
        1 maqkensypw pygrqtapsg lstlpqrvlr kepvtpsalv lmsrsnvqpt aapgqkvmen
       61 ssgtpdiltr hftiddfeig rplgkallcl wpeassvssp shpnilrlyn yfydrrriyl
      121 ileyaprgel ykelqksctf deqrtatime eladalmych gkkvihrdik penlllglkg
      181 elkiadfgws vhapslrrkt mcgtldylpp emiegrmhne kvdlwcigvl cyellvgnpp
      241 fesashnety rrivkvdlkf pasvpmgaqd liskllrhnp serlplaqvs ahpwvransr
      301 rvlppsalqs va
//
LOCUS       NP_000710               2138 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent L-type calcium channel subunit alpha-1C isoform
            18 [Homo sapiens].
ACCESSION   NP_000710
VERSION     NP_000710.5
DBSOURCE    REFSEQ: accession NM_000719.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2138)
  AUTHORS   Zhang,X., Liang,X., Cheng,X., Chen,J., Deng,W., Zhang,Y., Cui,L.,
            Cheng,X., Li,X., Yang,C., Ye,B. and Cao,L.
  TITLE     [CACNA1C rs58619945 genotype influences the cortical thickness of
            attention network among patients with Bipolar disorder]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 41 (9), 1045-1052 (2024)
   PUBMED   39217481
  REMARK    GeneRIF: [CACNA1C rs58619945 genotype influences the cortical
            thickness of attention network among patients with Bipolar
            disorder].
REFERENCE   2  (residues 1 to 2138)
  AUTHORS   Yang,Y., Zhu,Z., Hui,L. and Sun,P.
  TITLE     Effects of CACNA1C and ANK3 on cognitive function in patients with
            bipolar disorder
  JOURNAL   Prog Neuropsychopharmacol Biol Psychiatry 133, 111016 (2024)
   PUBMED   38657895
  REMARK    GeneRIF: Effects of CACNA1C and ANK3 on cognitive function in
            patients with bipolar disorder.
REFERENCE   3  (residues 1 to 2138)
  AUTHORS   Almodovar-Paya,C., Guardiola-Ripoll,M., Giralt-Lopez,M.,
            Oscoz-Irurozqui,M., Canales-Rodriguez,E.J., Madre,M.,
            Soler-Vidal,J., Ramiro,N., Callado,L.F., Arias,B., Gallego,C.,
            Pomarol-Clotet,E. and Fatjo-Vilas,M.
  TITLE     NRN1 epistasis with BDNF and CACNA1C: mediation effects on symptom
            severity through neuroanatomical changes in schizophrenia
  JOURNAL   Brain Struct Funct 229 (5), 1299-1315 (2024)
   PUBMED   38720004
  REMARK    GeneRIF: NRN1 epistasis with BDNF and CACNA1C: mediation effects on
            symptom severity through neuroanatomical changes in schizophrenia.
REFERENCE   4  (residues 1 to 2138)
  AUTHORS   Gao,S., Yao,X., Chen,J., Huang,G., Fan,X., Xue,L., Li,Z., Wu,T.,
            Zheng,Y., Huang,J., Jin,X., Wang,Y., Wang,Z., Yu,Y., Liu,L.,
            Pan,X., Song,C. and Yan,N.
  TITLE     Structural basis for human Cav1.2 inhibition by multiple drugs and
            the neurotoxin calciseptine
  JOURNAL   Cell 186 (24), 5363-5374 (2023)
   PUBMED   37972591
  REMARK    GeneRIF: Structural basis for human Cav1.2 inhibition by multiple
            drugs and the neurotoxin calciseptine.
REFERENCE   5  (residues 1 to 2138)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   6  (residues 1 to 2138)
  AUTHORS   Napolitano,C. and Priori,S.G.
  TITLE     CACNA1C-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301577
REFERENCE   7  (residues 1 to 2138)
  AUTHORS   Groffen,A.J., Bikker,H. and Christiaans,I.
  TITLE     Long QT Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301308
REFERENCE   8  (residues 1 to 2138)
  AUTHORS   Sun,W., McPherson,J.D., Hoang,D.Q., Wasmuth,J.J., Evans,G.A. and
            Montal,M.
  TITLE     Mapping of a human brain voltage-gated calcium channel to human
            chromosome 12p13-pter
  JOURNAL   Genomics 14 (4), 1092-1094 (1992)
   PUBMED   1335957
REFERENCE   9  (residues 1 to 2138)
  AUTHORS   Powers,P.A., Gregg,R.G. and Hogan,K.
  TITLE     Linkage mapping of the human gene for the alpha 1 subunit of the
            cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome
            12p13.2-pter using a dinucleotide repeat
  JOURNAL   Genomics 14 (1), 206-207 (1992)
   PUBMED   1330882
REFERENCE   10 (residues 1 to 2138)
  AUTHORS   Soldatov,N.M.
  TITLE     Molecular diversity of L-type Ca2+ channel transcripts in human
            fibroblasts
  JOURNAL   Proc Natl Acad Sci U S A 89 (10), 4628-4632 (1992)
   PUBMED   1316612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005342.1, Z34810.1 and
            AC007618.21.
            
            On Dec 29, 2006 this sequence version replaced NP_000710.4.
            
            Summary: This gene encodes an alpha-1 subunit of a
            voltage-dependent calcium channel. Calcium channels mediate the
            influx of calcium ions into the cell upon membrane polarization.
            The alpha-1 subunit consists of 24 transmembrane segments and forms
            the pore through which ions pass into the cell. The calcium channel
            consists of a complex of alpha-1, alpha-2/delta, beta, and gamma
            subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of
            these proteins, either encoded by different genes or the result of
            alternative splicing of transcripts. The protein encoded by this
            gene binds to and is inhibited by dihydropyridine. Alternative
            splicing results in many transcript variants encoding different
            proteins. Some of the predicted proteins may not produce functional
            ion channel subunits. [provided by RefSeq, Oct 2012].
            
            Transcript Variant: This variant (18), also referred to as HLCC70,
            lacks three alternate in-frame exons, compared to variant 1,
            resulting in a shorter protein (isoform 18), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF465484.1, Z34810.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399655.6/ ENSP00000382563.1
            RefSeq Select criteria :: based on manual assertion, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2138
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..2138
                     /product="voltage-dependent L-type calcium channel subunit
                     alpha-1C isoform 18"
                     /note="calcium channel, cardic dihydropyridine-sensitive,
                     alpha-1 subunit; DHPR, alpha-1 subunit; voltage-dependent
                     L-type Ca2+ channel alpha 1 subunit; calcium channel,
                     voltage-dependent, L type, alpha 1C subunit; CACNA1C
                     intronic transcript 2; CACNA1C intronic transcript 2
                     (non-protein coding)"
                     /calculated_mol_wt=239508
     Region          123..416
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          523..764
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          899..1176
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1218..1487
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Region          1496..1549
                     /region_name="GPHH"
                     /note="Voltage-dependent L-type calcium channel,
                     IQ-associated; pfam16905"
                     /db_xref="CDD:465306"
     Region          1559..1633
                     /region_name="Ca_chan_IQ"
                     /note="Voltage gated calcium channel IQ domain; pfam08763"
                     /db_xref="CDD:462591"
     Region          1653..2088
                     /region_name="CAC1F_C"
                     /note="Voltage-gated calcium channel subunit alpha,
                     C-term; pfam16885"
                     /db_xref="CDD:465298"
     CDS             1..2138
                     /gene="CACNA1C"
                     /gene_synonym="CACH2; CACN2; CACNA1C-IT2; CACNL1A1;
                     CaV1.2; CCHL1A1; LQT8; NEDHLSS; TS; TS. LQT8"
                     /coded_by="NM_000719.7:577..6993"
                     /note="isoform 18 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS44794.1"
                     /db_xref="GeneID:775"
                     /db_xref="HGNC:HGNC:1390"
                     /db_xref="MIM:114205"
ORIGIN      
        1 mvnentrmyi peenhqgsny gsprpahanm nanaaaglap ehiptpgaal swqaaidaar
       61 qaklmgsagn atistvsstq rkrqqygkpk kqgsttatrp prallcltlk npirracisi
      121 vewkpfeiii lltifancva laiyipfped dsnatnsnle rveylfliif tveaflkvia
      181 ygllfhpnay lrngwnlldf iivvvglfsa ileqatkadg analggkgag fdvkalrafr
      241 vlrplrlvsg vpslqvvlns iikamvpllh iallvlfvii iyaiiglelf mgkmhktcyn
      301 qegiadvpae ddpspcalet ghgrqcqngt vckpgwdgpk hgitnfdnfa famltvfqci
      361 tmegwtdvly wvndavgrdw pwiyfvtlii igsffvlnlv lgvlsgefsk erekakargd
      421 fqklrekqql eedlkgyldw itqaedidpe nedegmdeek prnmsmptse tesvntenva
      481 ggdiegencg arlahrisks kfsrywrrwn rfcrrkcraa vksnvfywlv iflvflntlt
      541 iasehynqpn wltevqdtan kallalftae mllkmyslgl qayfvslfnr fdcfvvcggi
      601 letilvetki msplgisvlr cvrllrifki trywnslsnl vasllnsvrs iaslllllfl
      661 fiiifsllgm qlfggkfnfd emqtrrstfd nfpqslltvf qiltgedwns vmydgimayg
      721 gpsfpgmlvc iyfiilficg nyillnvfla iavdnladae sltsaqkeee eekerkklar
      781 taspekkqel vekpavgesk eekielksit adgesppatk inmddlqpne nedkspypnp
      841 ettgeedeee pempvgprpr plselhlkek avpmpeasaf fifssnnrfr lqchrivndt
      901 iftnlilffi llssislaae dpvqhtsfrn hilfyfdivf ttiftieial kmtaygaflh
      961 kgsfcrnyfn ildllvvsvs lisfgiqssa invvkilrvl rvlrplrain rakglkhvvq
     1021 cvfvairtig nivivttllq fmfacigvql fkgklytcsd sskqteaeck gnyitykdge
     1081 vdhpiiqprs wenskfdfdn vlaammalft vstfegwpel lyrsidshte dkgpiynyrv
     1141 eisiffiiyi iiiaffmmni fvgfvivtfq eqgeqeyknc eldknqrqcv eyalkarplr
     1201 ryipknqhqy kvwyvvnsty feylmfvlil lnticlamqh ygqsclfkia mnilnmlftg
     1261 lftvemilkl iafkpkhyfc dawntfdali vvgsivdiai tevnpaehtq cspsmnaeen
     1321 srisitffrl frvmrlvkll srgegirtll wtfiksfqal pyvallivml ffiyavigmq
     1381 vfgkialndt teinrnnnfq tfpqavlllf rcatgeawqd imlacmpgkk capesepsns
     1441 tegetpcgss favfyfisfy mlcafliinl fvavimdnfd yltrdwsilg phhldefkri
     1501 waeydpeakg rikhldvvtl lrriqpplgf gklcphrvac krlvsmnmpl nsdgtvmfna
     1561 tlfalvrtal riktegnleq aneelraiik kiwkrtsmkl ldqvvppagd devtvgkfya
     1621 tfliqeyfrk fkkrkeqglv gkpsqrnals lqaglrtlhd igpeirrais gdltaeeeld
     1681 kamkeavsaa seddifrrag glfgnhvsyy qsdgrsafpq tfttqrplhi nkagssqgdt
     1741 espsheklvd stftpssyss tgsnaninna nntalgrlpr pagypstvst veghgpplsp
     1801 airvqevawk lssnrchsre sqaamagqee tsqdetyevk mnhdteacse psllstemls
     1861 yqddenrqlt lpeedkrdir qspkrgflrs aslgrrasfh leclkrqkdr ggdisqktvl
     1921 plhlvhhqal avaglspllq rshspasfpr pfatppatpg srgwppqpvp tlrlegvess
     1981 eklnssfpsi hcgswaettp ggggssaarr vrpvslmvps qagapgrqfh gsasslveav
     2041 liseglgqfa qdpkfievtt qeladacdmt ieemesaadn ilsggapqsp ngallpfvnc
     2101 rdagqdragg eedagcvrar grpseeelqd srvyvssl
//
LOCUS       NP_001269606            1226 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisomal ATPase PEX1 isoform 2 [Homo sapiens].
ACCESSION   NP_001269606 XP_005250487
VERSION     NP_001269606.1
DBSOURCE    REFSEQ: accession NM_001282677.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1226)
  AUTHORS   Karuntu,J.S., Klouwer,F.C.C., Engelen,M. and Boon,C.J.F.
  TITLE     Systematic study of ophthalmological findings in 10 patients with
            PEX1-mediated Zellweger spectrum disorder
  JOURNAL   Ophthalmic Genet 45 (4), 351-362 (2024)
   PUBMED   38664000
  REMARK    GeneRIF: Systematic study of ophthalmological findings in 10
            patients with PEX1-mediated Zellweger spectrum disorder.
REFERENCE   2  (residues 1 to 1226)
  AUTHORS   Miranda,V., Cortez,L., Rosmaninho-Salgado,J., Ramos,F. and Paiva,C.
  TITLE     Ophthalmic Manifestations of Heimler Syndrome in Two Siblings With
            PEX1 Variants
  JOURNAL   J Pediatr Ophthalmol Strabismus 61 (1), 59-66 (2024)
   PUBMED   37092661
  REMARK    GeneRIF: Ophthalmic Manifestations of Heimler Syndrome in Two
            Siblings With PEX1 Variants.
            Review article
REFERENCE   3  (residues 1 to 1226)
  AUTHORS   Liang,J.S., Hung,K.L., Lin,L.J., Ong,W.P., Keng,W.T. and Lu,J.F.
  TITLE     Novel PEX1 mutations in fibroblasts from children with Zellweger
            spectrum disorders exhibit temperature sensitive characteristics
  JOURNAL   Epilepsy Behav 145, 109266 (2023)
   PUBMED   37385119
  REMARK    GeneRIF: Novel PEX1 mutations in fibroblasts from children with
            Zellweger spectrum disorders exhibit temperature sensitive
            characteristics.
REFERENCE   4  (residues 1 to 1226)
  AUTHORS   Ott,J., Sehr,J., Schmidt,N., Schliebs,W. and Erdmann,R.
  TITLE     Comparison of human PEX knockout cell lines suggests a dual role of
            PEX1 in peroxisome biogenesis
  JOURNAL   Biol Chem 404 (2-3), 209-219 (2022)
   PUBMED   36534601
  REMARK    GeneRIF: Comparison of human PEX knockout cell lines suggests a
            dual role of PEX1 in peroxisome biogenesis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1226)
  AUTHORS   Faber,K.N., Heyman,J.A. and Subramani,S.
  TITLE     Two AAA family peroxins, PpPex1p and PpPex6p, interact with each
            other in an ATP-dependent manner and are associated with different
            subcellular membranous structures distinct from peroxisomes
  JOURNAL   Mol Cell Biol 18 (2), 936-943 (1998)
   PUBMED   9447990
REFERENCE   6  (residues 1 to 1226)
  AUTHORS   Portsteffen,H., Beyer,A., Becker,E., Epplen,C., Pawlak,A.,
            Kunau,W.H. and Dodt,G.
  TITLE     Human PEX1 is mutated in complementation group 1 of the peroxisome
            biogenesis disorders
  JOURNAL   Nat Genet 17 (4), 449-452 (1997)
   PUBMED   9398848
REFERENCE   7  (residues 1 to 1226)
  AUTHORS   Reuber,B.E., Germain-Lee,E., Collins,C.S., Morrell,J.C.,
            Ameritunga,R., Moser,H.W., Valle,D. and Gould,S.J.
  TITLE     Mutations in PEX1 are the most common cause of peroxisome
            biogenesis disorders
  JOURNAL   Nat Genet 17 (4), 445-448 (1997)
   PUBMED   9398847
REFERENCE   8  (residues 1 to 1226)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   9  (residues 1 to 1226)
  AUTHORS   Steinberg,S.J., Raymond,G.V., Braverman,N.E. and Moser,A.B.
  TITLE     Zellweger Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301621
REFERENCE   10 (residues 1 to 1226)
  AUTHORS   Naritomi,K., Izumikawa,Y., Ohshiro,S., Yoshida,K., Shimozawa,N.,
            Suzuki,Y., Orii,T. and Hirayama,K.
  TITLE     Gene assignment of Zellweger syndrome to 7q11.23: report of the
            second case associated with a pericentric inversion of chromosome 7
  JOURNAL   Hum Genet 84 (1), 79-80 (1989)
   PUBMED   2606480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA313282.1, AB052090.1,
            DB461678.1 and BC035575.1.
            
            On Sep 18, 2013 this sequence version replaced XP_005250487.1.
            
            Summary: This gene encodes a member of the AAA ATPase family, a
            large group of ATPases associated with diverse cellular activities.
            This protein is cytoplasmic but is often anchored to a peroxisomal
            membrane where it forms a heteromeric complex and plays a role in
            the import of proteins into peroxisomes and peroxisome biogenesis.
            Mutations in this gene have been associated with complementation
            group 1 peroxisomal disorders such as neonatal
            adrenoleukodystrophy, infantile Refsum disease, and Zellweger
            syndrome. Alternatively spliced transcript variants have been found
            for this gene. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (2) is missing an in-frame coding
            exon compared to variant 1. The resulting shorter isoform (2) lacks
            an internal protein segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB052090.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..1226
                     /product="peroxisomal ATPase PEX1 isoform 2"
                     /note="peroxisome biogenesis disorder protein 1;
                     peroxin-1; Zellweger syndrome; peroxisomal ATPase PEX1"
                     /calculated_mol_wt=136454
     Region          17..98
                     /region_name="PEX-2N"
                     /note="Peroxisome biogenesis factor 1, N-terminal;
                     pfam09263"
                     /db_xref="CDD:462730"
     Region          104..179
                     /region_name="PEX-1N"
                     /note="Peroxisome biogenesis factor 1, N-terminal;
                     pfam09262"
                     /db_xref="CDD:462729"
     Region          397..762
                     /region_name="SpoVK"
                     /note="AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell
                     wall/membrane/envelope biogenesis, Cell cycle control,
                     cell division, chromosome partitioning, Signal
                     transduction mechanisms]; COG0464"
                     /db_xref="CDD:440232"
     Region          <595..1008
                     /region_name="CDC48"
                     /note="AAA family ATPase, CDC48 subfamily; TIGR01243"
                     /db_xref="CDD:273521"
     Region          791..948
                     /region_name="RecA-like_PEX1_r2"
                     /note="second of two ATPase domains of Peroxisomal
                     biogenesis factor 1 (PEX1); cd19526"
                     /db_xref="CDD:410934"
     Site            order(825..832,927)
                     /site_type="other"
                     /note="putative ATP binding site [chemical binding]"
                     /db_xref="CDD:410934"
     CDS             1..1226
                     /gene="PEX1"
                     /gene_synonym="HMLR1; PBD1A; PBD1B; ZWS; ZWS1"
                     /coded_by="NM_001282677.2:86..3766"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64710.1"
                     /db_xref="GeneID:5189"
                     /db_xref="HGNC:HGNC:8850"
                     /db_xref="MIM:602136"
ORIGIN      
        1 mwgsdrlaga ggggaavtva ftnardcflh lprrlvaqlh llqnqaievv wshqpaflsw
       61 vegrhfsdqg envaeinrqv gqklglsngg qvflkpcshv vscqqvevep lsaddweile
      121 lhavsleqhl ldqirivfpk aifpvwvdqq tyifiqival ipaasygrle tdtklliqpk
      181 trrakentfs kadaeykklh sygrdqkgmm kelqtkqlqs ntvgitesne neseipvdss
      241 svaslwtmig sifsfqsekk qetswgltei nafknmqskv vpldnifrvc ksqppsiyna
      301 satsvfhkhc aihvfpwdqe yfdvepsftv tygklvklls pkqqqsktkq nvlspekekq
      361 msepldqkki rsdhneedek acvlqvvwng leelnnaiky tknvevlhlg kvwipddlrk
      421 rlniemhavv ritpvevtpk iprslklqpr enlpkdisee diktvfyswl qqstttmlpl
      481 viseeefikl etkdglkefs lsivhsweke kdknifllsp nllqkttiqv lldpmvkeen
      541 seeidfilpf lklsslggvn slgvsslehi thsllgrpls rqlmslvagl rngallltgg
      601 kgsgkstlak aickeafdkl dahvervdck alralndmik efismgslva liatsqsqqs
      661 lhpllvsaqg vhifqcvqhi qppnqeqrce ilcnviknkl dcdinkftdl dlqhvaketg
      721 gfvardftvl vdraihsrls rqsistrekl vlttldfqka lrgflpaslr svnlhkprdl
      781 gwdkigglhe vrqilmdtiq lpakypelfa nlpirqrtgi llygppgtgk tllagviare
      841 srmnfisvkg pellskyiga seqavrdifi raqaakpcil ffdefesiap rrghdntgvt
      901 drvvnqlltq ldgveglqgv yvlaatsrpd lidpallrpg rldkcvycpp pdqvsrleil
      961 nvlsdslpla ddvdlqhvas vtdsftgadl kallynaqle alhgmllssg lqdgssssds
     1021 dlslssmvfl nhssgsddsa gdgecgldqs lvslemseil pdeskfnmyr lyfgssyese
     1081 lgngtssdls sqclsapssm tqdlpgvpgk dqlfsqppvl rtasqegcqe ltqeqrdqlr
     1141 adisiikgry rsqsgedesm nqpgpiktrl aisqshlmta lghtrpsise ddwknfaely
     1201 esfqnpkrrk nqsgtmfrpg qkvtla
//
LOCUS       NP_005048                538 aa            linear   PRI 20-NOV-2025
DEFINITION  retinoblastoma-binding protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_005048
VERSION     NP_005048.2
DBSOURCE    REFSEQ: accession NM_005057.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Patel,A., Dharmarajan,V., Vought,V.E. and Cosgrove,M.S.
  TITLE     On the mechanism of multiple lysine methylation by the human mixed
            lineage leukemia protein-1 (MLL1) core complex
  JOURNAL   J Biol Chem 284 (36), 24242-24256 (2009)
   PUBMED   19556245
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Southall,S.M., Wong,P.S., Odho,Z., Roe,S.M. and Wilson,J.R.
  TITLE     Structural basis for the requirement of additional factors for MLL1
            SET domain activity and recognition of epigenetic marks
  JOURNAL   Mol Cell 33 (2), 181-191 (2009)
   PUBMED   19187761
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Lee,J.H., Tate,C.M., You,J.S. and Skalnik,D.G.
  TITLE     Identification and characterization of the human Set1B histone
            H3-Lys4 methyltransferase complex
  JOURNAL   J Biol Chem 282 (18), 13419-13428 (2007)
   PUBMED   17355966
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Scacheri,P.C., Davis,S., Odom,D.T., Crawford,G.E., Perkins,S.,
            Halawi,M.J., Agarwal,S.K., Marx,S.J., Spiegel,A.M., Meltzer,P.S.
            and Collins,F.S.
  TITLE     Genome-wide analysis of menin binding provides insights into MEN1
            tumorigenesis
  JOURNAL   PLoS Genet 2 (4), e51 (2006)
   PUBMED   16604156
  REMARK    GeneRIF: analysis of menin's role as a tumor suppressor and binding
            sites of Rbbp5 and MLL1
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Goo,Y.H., Sohn,Y.C., Kim,D.H., Kim,S.W., Kang,M.J., Jung,D.J.,
            Kwak,E., Barlev,N.A., Berger,S.L., Chow,V.T., Roeder,R.G.,
            Azorsa,D.O., Meltzer,P.S., Suh,P.G., Song,E.J., Lee,K.J., Lee,Y.C.
            and Lee,J.W.
  TITLE     Activating signal cointegrator 2 belongs to a novel steady-state
            complex that contains a subset of trithorax group proteins
  JOURNAL   Mol Cell Biol 23 (1), 140-149 (2003)
   PUBMED   12482968
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Saijo,M., Sakai,Y., Kishino,T., Niikawa,N., Matsuura,Y., Morino,K.,
            Tamai,K. and Taya,Y.
  TITLE     Molecular cloning of a human protein that binds to the
            retinoblastoma protein and chromosomal mapping
  JOURNAL   Genomics 27 (3), 511-519 (1995)
   PUBMED   7558034
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA797022.1, BC075059.2,
            AL583832.14 and BQ020418.1.
            
            On Oct 4, 2004 this sequence version replaced NP_005048.1.
            
            Summary: This gene encodes a ubiquitously expressed nuclear protein
            which belongs to a highly conserved subfamily of WD-repeat
            proteins. The encoded protein binds directly to retinoblastoma
            protein, which regulates cell proliferation. It interacts
            preferentially with the underphosphorylated retinoblastoma protein
            via the E1A-binding pocket B. Three alternatively spliced
            transcript variants that encode different protein isoforms have
            been described for this gene. [provided by RefSeq, Jul 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest protein (isoform 1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC053856.1, X85134.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264515.11/ ENSP00000264515.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..538
                     /product="retinoblastoma-binding protein 5 isoform 1"
                     /note="SWD1, Set1c WD40 repeat protein, homolog; RBBP-5;
                     retinoblastoma-binding protein RBQ-3;
                     retinoblastoma-binding protein 5"
                     /calculated_mol_wt=59022
     Region          22..63
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          29..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <31..321
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          64..103
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          70..106
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..188
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          154..190
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          196..235
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          201..246
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          249..291
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7558034; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          254..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          293..331
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          298..321
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..366
                     /region_name="Interaction with ASH2L.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Region          344..377
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          371..380
                     /region_name="Interaction with WDR5.
                     /evidence=ECO:0000269|PubMed:21220120"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            388
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Region          408..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15291.2)"
     Site            497
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:7558034; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15291.2)"
     CDS             1..538
                     /gene="RBBP5"
                     /gene_synonym="RBQ3; SWD1"
                     /coded_by="NM_005057.4:106..1722"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS30983.1"
                     /db_xref="GeneID:5929"
                     /db_xref="HGNC:HGNC:9888"
                     /db_xref="MIM:600697"
ORIGIN      
        1 mnlellesfg qnypeeadgt ldcismaltc tfnrwgtlla vgcndgrivi wdfltrgiak
       61 iisahihpvc slcwsrdghk lvsastdniv sqwdvlsgdc dqrfrfpspi lkvqyhprdq
      121 nkvlvcpmks apvmltlsds khvvlpvddd sdlnvvasfd rrgeyiytgn akgkilvlkt
      181 dsqdlvasfr vttgtsntta iksiefarkg scflintadr iirvydgrei ltcgrdgepe
      241 pmqklqdlvn rtpwkkccfs gdgeyivags arqhalyiwe ksignlvkil hgtrgellld
      301 vawhpvrpii asissgvvsi waqnqvenws afapdfkeld enveyeeres efdiededks
      361 epeqtgadaa edeevdvtsv dpiaafcssd eeledskall ylpiapeved peenpygppp
      421 davqtslmde gassekkrqs sadgsqppkk kpkttnielq gvpndevhpl lgvkgdgksk
      481 kkqagrpkgs kgkekdspfk pklykgdrgl plegsakgkv qaelsqplta ggaisell
//
LOCUS       NP_002609                403 aa            linear   PRI 20-NOV-2025
DEFINITION  peroxisome biogenesis factor 13 [Homo sapiens].
ACCESSION   NP_002609
VERSION     NP_002609.1
DBSOURCE    REFSEQ: accession NM_002618.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Gaussmann,S., Peschel,R., Ott,J., Zak,K.M., Sastre,J.,
            Delhommel,F., Popowicz,G.M., Boekhoven,J., Schliebs,W., Erdmann,R.
            and Sattler,M.
  TITLE     Modulation of peroxisomal import by the PEX13 SH3 domain and a
            proximal FxxxF binding motif
  JOURNAL   Nat Commun 15 (1), 3317 (2024)
   PUBMED   38632234
  REMARK    GeneRIF: Modulation of peroxisomal import by the PEX13 SH3 domain
            and a proximal FxxxF binding motif.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Ravindran,R., Bacellar,I.O.L., Castellanos-Girouard,X., Wahba,H.M.,
            Zhang,Z., Omichinski,J.G., Kisley,L. and Michnick,S.W.
  TITLE     Peroxisome biogenesis initiated by protein phase separation
  JOURNAL   Nature 617 (7961), 608-615 (2023)
   PUBMED   37165185
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Borgia,P., Baldassari,S., Pedemonte,N., Alkhunaizi,E.,
            D'Onofrio,G., Tortora,D., Cali,E., Scudieri,P., Balagura,G.,
            Musante,I., Diana,M.C., Pedemonte,M., Vari,M.S., Iacomino,M.,
            Riva,A., Chimenz,R., Mangano,G.D., Mohammadi,M.H., Toosi,M.B.,
            Ashrafzadeh,F., Imannezhad,S., Karimiani,E.G., Accogli,A.,
            Schiaffino,M.C., Maghnie,M., Soler,M.A., Echiverri,K., Abrams,C.K.,
            Striano,P., Fortuna,S., Maroofian,R., Houlden,H., Zara,F.,
            Fiorillo,C. and Salpietro,V.
  TITLE     Genotype-phenotype correlations and disease mechanisms in
            PEX13-related Zellweger spectrum disorders
  JOURNAL   Orphanet J Rare Dis 17 (1), 286 (2022)
   PUBMED   35854306
  REMARK    GeneRIF: Genotype-phenotype correlations and disease mechanisms in
            PEX13-related Zellweger spectrum disorders.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Feng,P., Wu,X., Erramilli,S.K., Paulo,J.A., Knejski,P., Gygi,S.P.,
            Kossiakoff,A.A. and Rapoport,T.A.
  TITLE     A peroxisomal ubiquitin ligase complex forms a retrotranslocation
            channel
  JOURNAL   Nature 607 (7918), 374-380 (2022)
   PUBMED   35768507
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Bjorkman,J., Stetten,G., Moore,C.S., Gould,S.J. and Crane,D.I.
  TITLE     Genomic structure of PEX13, a candidate peroxisome biogenesis
            disorder gene
  JOURNAL   Genomics 54 (3), 521-528 (1998)
   PUBMED   9878256
REFERENCE   6  (residues 1 to 403)
  AUTHORS   Fransen,M., Terlecky,S.R. and Subramani,S.
  TITLE     Identification of a human PTS1 receptor docking protein directly
            required for peroxisomal protein import
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 8087-8092 (1998)
   PUBMED   9653144
REFERENCE   7  (residues 1 to 403)
  AUTHORS   Albertini,M., Rehling,P., Erdmann,R., Girzalsky,W., Kiel,J.A.,
            Veenhuis,M. and Kunau,W.H.
  TITLE     Pex14p, a peroxisomal membrane protein binding both receptors of
            the two PTS-dependent import pathways
  JOURNAL   Cell 89 (1), 83-92 (1997)
   PUBMED   9094717
REFERENCE   8  (residues 1 to 403)
  AUTHORS   Gould,S.J., Kalish,J.E., Morrell,J.C., Bjorkman,J., Urquhart,A.J.
            and Crane,D.I.
  TITLE     Pex13p is an SH3 protein of the peroxisome membrane and a docking
            factor for the predominantly cytoplasmic PTs1 receptor
  JOURNAL   J Cell Biol 135 (1), 85-95 (1996)
   PUBMED   8858165
REFERENCE   9  (residues 1 to 403)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 403)
  AUTHORS   Steinberg,S.J., Raymond,G.V., Braverman,N.E. and Moser,A.B.
  TITLE     Zellweger Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301621
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB102467.1, AB022192.1,
            AC010733.8 and CN288682.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a peroxisomal membrane protein that
            binds the type 1 peroxisomal targeting signal receptor via a SH3
            domain located in the cytoplasm. Mutations and deficiencies in
            peroxisomal protein importing and peroxisome assembly lead to
            peroxisomal biogenesis disorders, an example of which is Zellweger
            syndrome. [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.353160.1,
                                           SRR1660805.7239.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000295030.6/ ENSP00000295030.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..403
                     /product="peroxisome biogenesis factor 13"
                     /note="peroxisomal membrane protein PEX13; peroxin-13"
                     /calculated_mol_wt=43999
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Region          117..254
                     /region_name="Peroxin-13_N"
                     /note="Peroxin 13, N-terminal region; pfam04088"
                     /db_xref="CDD:461167"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Region          145..233
                     /region_name="Targeting to peroxisomes.
                     /evidence=ECO:0000269|PubMed:11390669"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Region          175..196
                     /region_name="Interaction with PEX19.
                     /evidence=ECO:0000269|PubMed:11390669"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Site            175..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Site            234..254
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92968.2)"
     Region          276..333
                     /region_name="SH3_PEX13_eumet"
                     /note="Src Homology 3 domain of eumetazoan Peroxisomal
                     biogenesis factor 13; cd11864"
                     /db_xref="CDD:212798"
     Site            order(281,283,286,290,312..313,327,329..330)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212798"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9D0K1; propagated from
                     UniProtKB/Swiss-Prot (Q92968.2)"
     CDS             1..403
                     /gene="PEX13"
                     /gene_synonym="NALD; PBD11A; PBD11B; ZWS"
                     /coded_by="NM_002618.4:41..1252"
                     /db_xref="CCDS:CCDS1866.1"
                     /db_xref="GeneID:5194"
                     /db_xref="HGNC:HGNC:8855"
                     /db_xref="MIM:601789"
ORIGIN      
        1 masqpppppk pwetrripga gpgpgpgptf qsadlgptlm trpgqpaltr vpppilprps
       61 qqtgsssvnt frpayssfss gygaygnsfy ggyspysygy nglgynrlrv ddlppsrfvq
      121 qaeessrgaf qsiesivhaf asvsmmmdat fsavynsfra vldvanhfsr lkihftkvfs
      181 afalvrtiry lyrrlqrmlg lrrgsenedl waesegtvac lgaedraats akswpiflff
      241 avilggpyli wkllsthsde vtdsinwasg eddhvvarae ydfaavseee isfragdmln
      301 lalkeqqpkv rgwllasldg qttglipany vkilgkrkgr ktvesskvsk qqqsftnptl
      361 tkgatvadsl deqeaafesv fvetnkvpva pdsigkdgek qdl
//
LOCUS       NP_009160                486 aa            linear   PRI 20-NOV-2025
DEFINITION  protein kinase C and casein kinase substrate in neurons protein 2
            isoform A [Homo sapiens].
ACCESSION   NP_009160
VERSION     NP_009160.2
DBSOURCE    REFSEQ: accession NM_007229.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wint,H., Li,J., Abe,T., Yamada,H., Higaki,T., Nasu,Y., Watanabe,M.,
            Takei,K. and Takeda,T.
  TITLE     Pacsin 2-dependent N-cadherin internalization regulates the
            migration behaviour of malignant cancer cells
  JOURNAL   J Cell Sci 136 (10) (2023)
   PUBMED   37132654
  REMARK    GeneRIF: Pacsin 2-dependent N-cadherin internalization regulates
            the migration behaviour of malignant cancer cells.
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Zudeh,G., Franca,R., Lucafo,M., Bonten,E.J., Bramuzzo,M.,
            Sgarra,R., Lagatolla,C., Franzin,M., Evans,W.E., Decorti,G. and
            Stocco,G.
  TITLE     PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells
  JOURNAL   Life Sci Alliance 6 (3), e202201610 (2023)
   PUBMED   36596605
  REMARK    GeneRIF: PACSIN2 as a modulator of autophagy and mercaptopurine
            cytotoxicity: mechanisms in lymphoid and intestinal cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Park,K., Yoo,H.S., Oh,C.K., Lee,J.R., Chung,H.J., Kim,H.N.,
            Kim,S.H., Kee,K.M., Kim,T.Y., Kim,M., Kim,B.G., Ra,J.S., Myung,K.,
            Kim,H., Han,S.H., Seo,M.D., Lee,Y. and Kim,D.W.
  TITLE     Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate
            drug resistance in chronic myeloid leukemia
  JOURNAL   Cancer Med 11 (21), 4005-4020 (2022)
   PUBMED   35352878
  REMARK    GeneRIF: Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1
            regulate drug resistance in chronic myeloid leukemia.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Kessels,M.M. and Qualmann,B.
  TITLE     The syndapin protein family: linking membrane trafficking with the
            cytoskeleton
  JOURNAL   J Cell Sci 117 (Pt 15), 3077-3086 (2004)
   PUBMED   15226389
  REMARK    Review article
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Ghadimi,M.P., Sanzenbacher,R., Thiede,B., Wenzel,J., Jing,Q.,
            Plomann,M., Borkhardt,A., Kabelitz,D. and Janssen,O.
  TITLE     Identification of interaction partners of the cytosolic polyproline
            region of CD95 ligand (CD178)
  JOURNAL   FEBS Lett 519 (1-3), 50-58 (2002)
   PUBMED   12023017
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Sumoy,L., Pluvinet,R., Andreu,N., Estivill,X. and Escarceller,M.
  TITLE     PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
            pacsin-syndapin-FAP52 gene family
  JOURNAL   Gene 262 (1-2), 199-205 (2001)
   PUBMED   11179684
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Modregger,J., Ritter,B., Witter,B., Paulsson,M. and Plomann,M.
  TITLE     All three PACSIN isoforms bind to endocytic proteins and inhibit
            endocytosis
  JOURNAL   J Cell Sci 113 Pt 24, 4511-4521 (2000)
   PUBMED   11082044
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Ritter,B., Modregger,J., Paulsson,M. and Plomann,M.
  TITLE     PACSIN 2, a novel member of the PACSIN family of cytoplasmic
            adapter proteins
  JOURNAL   FEBS Lett 454 (3), 356-362 (1999)
   PUBMED   10431838
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008037.2, AF128536.1 and
            BI964045.1.
            
            On Jun 10, 2007 this sequence version replaced NP_009160.1.
            
            Summary: This gene is a member of the protein kinase C and casein
            kinase substrate in neurons family. The encoded protein is involved
            in linking the actin cytoskeleton with vesicle formation by
            regulating tubulin polymerization. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Both variants 1 and 2 encode the same isoform (A).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008037.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..486
                     /product="protein kinase C and casein kinase substrate in
                     neurons protein 2 isoform A"
                     /note="syndapin2; syndapin-II; syndapin-2; cytoplasmic
                     phosphoprotein PACSIN2"
                     /calculated_mol_wt=55608
     Region          1..362
                     /region_name="(Microbial infection) Interaction with HCV
                     NS5A. /evidence=ECO:0000269|PubMed:31801866"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          18..275
                     /region_name="F-BAR_PACSIN2"
                     /note="The F-BAR (FES-CIP4 Homology and
                     Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein
                     kinase Substrate in Neurons 2 (PACSIN2); cd07679"
                     /db_xref="CDD:153363"
     Site            order(18..20,26..27,30,33,36..37,40..41,43..44,47..48,
                     51..52,54..55,58..59,62,65..66,74..75,79,83,86..87,89,97,
                     145,149,212,227,230,234,237..238,240..242,245,248..249,
                     251..252,255..258,263..264,267,270..271,274..275)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153363"
     Site            order(25,29,36,46,50,53,65,101,113,132,139..140,147..148,
                     150,203,207,210)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153363"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          314..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          <338..428
                     /region_name="NPF"
                     /note="Rabosyn-5 repeating NPF sequence-motif; pfam16601"
                     /db_xref="CDD:406900"
     Region          362..364
                     /region_name="NPF1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WVE8; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          405..407
                     /region_name="NPF2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          417..419
                     /region_name="NPF3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNF0.2)"
     Region          429..484
                     /region_name="SH3_PACSIN1-2"
                     /note="Src homology 3 domain of Protein kinase C and
                     Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN
                     2; cd11998"
                     /db_xref="CDD:212931"
     Site            order(435,437,440,444,463..464,478,480..481)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212931"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNF0.2)"
     CDS             1..486
                     /gene="PACSIN2"
                     /gene_synonym="SDPII"
                     /coded_by="NM_007229.3:223..1683"
                     /note="isoform A is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43023.1"
                     /db_xref="GeneID:11252"
                     /db_xref="HGNC:HGNC:8571"
                     /db_xref="MIM:604960"
ORIGIN      
        1 msvtyddsvg vevssdsfwe vgnykrtvkr iddghrlcsd lmnclherar iekayaqqlt
       61 ewarrwrqlv ekgpqygtve kawmafmsea ervselhlev kaslmnddfe kiknwqkeaf
      121 hkqmmggfke tkeaedgfrk aqkpwakklk eveaakkahh aackeeklai sreanskadp
      181 slnpeqlkkl qdkiekckqd vlktkekyek slkeldqgtp qymenmeqvf eqcqqfeekr
      241 lrffrevlle vqkhldlsnv agykaiyhdl eqsiraadav edlrwfranh gpgmamnwpq
      301 feewsadlnr tlsrrekkka tdgvtltgin qtgdqslpsk psstlnvpsn paqsaqsqss
      361 ynpfededdt gstvsekddt kaknvssyek tqsyptdwsd desnnpfsst dangdsnpfd
      421 ddatsgtevr vralydyegq ehdelsfkag deltkmeded eqgwckgrld ngqvglypan
      481 yveaiq
//
LOCUS       NP_001307752             349 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 54 isoform a [Homo sapiens].
ACCESSION   NP_001307752 XP_006712174
VERSION     NP_001307752.1
DBSOURCE    REFSEQ: accession NM_001320823.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 349)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 349)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 349)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 349)
  AUTHORS   Yuan,Y., Qi,G., Shen,H., Guo,A., Cao,F., Zhu,Y., Xiao,C., Chang,W.
            and Zheng,S.
  TITLE     Clinical significance and biological function of WD repeat domain
            54 as an oncogene in colorectal cancer
  JOURNAL   Int J Cancer 144 (7), 1584-1595 (2019)
   PUBMED   29987896
  REMARK    GeneRIF: WDR54 was found to be elevated and associated with
            prognosis in patients with colorectal cancer (CRC). Functional
            assays showed that WDR54 facilitates the aggressiveness of CRC
            cells and promotes tumor growth in mice. Knockdown of WDR54
            sensitizes CRC cells to the proliferation-inhibitory effect of SHP2
            inhibitor, an effect involving their common function in regulating
            AKT and ERK signaling.
REFERENCE   5  (residues 1 to 349)
  AUTHORS   Maeda,A., Nishino,T., Matsunaga,R., Yokoyama,A., Suga,H., Yagi,T.
            and Konishi,H.
  TITLE     Transglutaminase-mediated cross-linking of WDR54 regulates EGF
            receptor-signaling
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1866 (2), 285-295 (2019)
   PUBMED   30458214
REFERENCE   6  (residues 1 to 349)
  AUTHORS   Rush,J., Moritz,A., Lee,K.A., Guo,A., Goss,V.L., Spek,E.J.,
            Zhang,H., Zha,X.M., Polakiewicz,R.D. and Comb,M.J.
  TITLE     Immunoaffinity profiling of tyrosine phosphorylation in cancer
            cells
  JOURNAL   Nat Biotechnol 23 (1), 94-101 (2005)
   PUBMED   15592455
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG024606.1, BI855898.1, AK023015.1 and AI203710.1.
            
            On Mar 5, 2016 this sequence version replaced XP_006712174.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.265491.1,
                                           SRR5189667.302648.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..349
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.1"
     Protein         1..349
                     /product="WD repeat-containing protein 54 isoform a"
                     /note="WD repeat-containing protein 54"
                     /calculated_mol_wt=37346
     Region          87..128
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <127..297
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          134..177
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..223
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          231..264
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          270..307
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..349
                     /gene="WDR54"
                     /coded_by="NM_001320823.2:22..1071"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:84058"
                     /db_xref="HGNC:HGNC:25770"
                     /db_xref="MIM:620826"
ORIGIN      
        1 mvaadlegpy epgvrmfrwe rsiplrgsaa alcnnlsvlq lparnltyfg vvhgpsaqll
       61 saapegvpla qrqlhakega gvspplitqv hwcvlpfrvl lvltshrgiq myesngytmv
      121 ywhaldsgda spvqavfarg iaasghficv gtwsgrvlvf dipakgpniv lseelaghqm
      181 pitdiatepa qgqdcvadmv taddsgllcv wrsgpeftll tripgfgvpc psvqlwqgii
      241 aagygngqvh lyeattgnlh vqinaharai caldlasevg kllsagedtf vhiwklsrnp
      301 esgyievehc hgecvadtql cgarfcdssg nsfavtgydl aeirrfssv
//
LOCUS       NP_001357592             776 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-1 [Homo sapiens].
ACCESSION   NP_001357592 XP_011514934
VERSION     NP_001357592.1
DBSOURCE    REFSEQ: accession NM_001370663.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Yang,T., Hu,J., Zhang,L., Liu,L., Pan,X., Zhou,Y., Wu,Y., Shi,X.,
            Obiegbusi,C.N. and Dong,X.
  TITLE     CircCUL1 inhibits trophoblast cell migration and invasion and
            promotes cell autophagy by sponging hsa-miR-30e-3p in fetal growth
            restriction via the ANXA1/PI3K/AKT axis
  JOURNAL   J Biochem Mol Toxicol 38 (7), e23759 (2024)
   PUBMED   39003567
  REMARK    GeneRIF: CircCUL1 inhibits trophoblast cell migration and invasion
            and promotes cell autophagy by sponging hsa-miR-30e-3p in fetal
            growth restriction via the ANXA1/PI3K/AKT axis.
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,Y., Huang,X., Wang,Y., Lei,Y., Yu,J., Yu,S., Gao,Y., Yang,J.,
            Zhao,F., Yu,H., Zeng,J., Chu,Y., Yang,M., Li,G., Xie,X. and
            Zhang,J.
  TITLE     NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer by
            Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins
  JOURNAL   Adv Sci (Weinh) 11 (9), e2305907 (2024)
   PUBMED   38126621
  REMARK    GeneRIF: NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer
            by Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Khalil,M.I., Yang,C., Vu,L., Chadha,S., Nabors,H., James,C.D.,
            Morgan,I.M. and Pyeon,D.
  TITLE     The membrane-associated ubiquitin ligase MARCHF8 stabilizes the
            human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in
            head and neck cancer
  JOURNAL   J Virol 98 (2), e0172623 (2024)
   PUBMED   38226814
  REMARK    GeneRIF: The membrane-associated ubiquitin ligase MARCHF8
            stabilizes the human papillomavirus oncoprotein E7 by degrading
            CUL1 and UBE2L3 in head and neck cancer.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Winston,J.T., Strack,P., Beer-Romero,P., Chu,C.Y., Elledge,S.J. and
            Harper,J.W.
  TITLE     The SCFbeta-TRCP-ubiquitin ligase complex associates specifically
            with phosphorylated destruction motifs in IkappaBalpha and
            beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
  JOURNAL   Genes Dev 13 (3), 270-283 (1999)
   PUBMED   9990852
  REMARK    Erratum:[Genes Dev 1999 Apr 15;13(8):1050]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Ng,R.W., Arooz,T., Yam,C.H., Chan,I.W., Lau,A.W. and Poon,R.Y.
  TITLE     Characterization of the cullin and F-box protein partner Skp1
  JOURNAL   FEBS Lett 438 (3), 183-189 (1998)
   PUBMED   9827542
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005229.2 and AC006323.3.
            
            On May 21, 2019 this sequence version replaced XP_011514934.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.64857.1,
                                           SRR1803616.142043.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..776
                     /product="cullin-1"
                     /note="CUL-1"
                     /calculated_mol_wt=89548
     Region          21..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Site            63
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13616.2)"
     Region          706..768
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..776
                     /gene="CUL1"
                     /coded_by="NM_001370663.1:230..2560"
                     /db_xref="CCDS:CCDS34772.1"
                     /db_xref="GeneID:8454"
                     /db_xref="HGNC:HGNC:2551"
                     /db_xref="MIM:603134"
ORIGIN      
        1 msstrsqnph glkqigldqi wddlragiqq vytrqsmaks rymelythvy nyctsvhqsn
       61 qargagvpps kskkgqtpgg aqfvglelyk rlkeflknyl tnllkdgedl mdesvlkfyt
      121 qqwedyrfss kvlngicayl nrhwvrrecd egrkgiyeiy slalvtwrdc lfrplnkqvt
      181 navlklieke rngetintrl isgvvqsyve lglneddafa kgptltvyke sfesqfladt
      241 erfytreste flqqnpvtey mkkaearlle eqrrvqvylh estqdelark ceqvliekhl
      301 eifhtefqnl ldadknedlg rmynlvsriq dglgelkkll ethihnqgla aiekcgeaal
      361 ndpkmyvqtv ldvhkkynal vmsafnndag fvaaldkacg rfinnnavtk maqssskspe
      421 llarycdsll kkssknpeea eledtlnqvm vvfkyiedkd vfqkfyakml akrlvhqnsa
      481 sddaeasmis klkqacgfey tsklqrmfqd igvskdlneq fkkhltnsep ldldfsiqvl
      541 ssgswpfqqs ctfalpsele rsyqrftafy asrhsgrklt wlyqlskgel vtncfknryt
      601 lqastfqmai llqynteday tvqqltdstq ikmdilaqvl qillkskllv ledenanvde
      661 velkpdtlik lylgyknkkl rvninvpmkt eqkqeqetth knieedrkll iqaaivrimk
      721 mrkvlkhqql lgevltqlss rfkprvpvik kcidilieke ylervdgekd tysyla
//
LOCUS       NP_001315                431 aa            linear   PRI 20-NOV-2025
DEFINITION  cleavage stimulation factor subunit 1 [Homo sapiens].
ACCESSION   NP_001315
VERSION     NP_001315.1
DBSOURCE    REFSEQ: accession NM_001324.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 431)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 431)
  AUTHORS   Tu,Y.X.I., Sydor,A.M., Coyaud,E., Laurent,E.M.N., Dyer,D.,
            Mellouk,N., St-Germain,J., Vernon,R.M., Forman-Kay,J.D., Li,T.,
            Hua,R., Zhao,K., Ridgway,N.D., Kim,P.K., Raught,B. and Brumell,J.H.
  TITLE     Global Proximity Interactome of the Human Macroautophagy Pathway
  JOURNAL   Autophagy 18 (5), 1174-1186 (2022)
   PUBMED   34524948
REFERENCE   3  (residues 1 to 431)
  AUTHORS   Boreikaite,V., Elliott,T.S., Chin,J.W. and Passmore,L.A.
  TITLE     RBBP6 activates the pre-mRNA 3' end processing machinery in humans
  JOURNAL   Genes Dev 36 (3-4), 210-224 (2022)
   PUBMED   35177536
REFERENCE   4  (residues 1 to 431)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 431)
  AUTHORS   Yang,W., Hsu,P.L., Yang,F., Song,J.E. and Varani,G.
  TITLE     Reconstitution of the CstF complex unveils a regulatory role for
            CstF-50 in recognition of 3'-end processing signals
  JOURNAL   Nucleic Acids Res 46 (2), 493-503 (2018)
   PUBMED   29186539
REFERENCE   6  (residues 1 to 431)
  AUTHORS   Ruegsegger,U., Beyer,K. and Keller,W.
  TITLE     Purification and characterization of human cleavage factor Im
            involved in the 3' end processing of messenger RNA precursors
  JOURNAL   J Biol Chem 271 (11), 6107-6113 (1996)
   PUBMED   8626397
REFERENCE   7  (residues 1 to 431)
  AUTHORS   Murthy,K.G. and Manley,J.L.
  TITLE     The 160-kD subunit of human cleavage-polyadenylation specificity
            factor coordinates pre-mRNA 3'-end formation
  JOURNAL   Genes Dev 9 (21), 2672-2683 (1995)
   PUBMED   7590244
REFERENCE   8  (residues 1 to 431)
  AUTHORS   Takagaki,Y. and Manley,J.L.
  TITLE     A polyadenylation factor subunit is the human homologue of the
            Drosophila suppressor of forked protein
  JOURNAL   Nature 372 (6505), 471-474 (1994)
   PUBMED   7984242
REFERENCE   9  (residues 1 to 431)
  AUTHORS   Takagaki,Y. and Manley,J.L.
  TITLE     A human polyadenylation factor is a G protein beta-subunit
            homologue
  JOURNAL   J Biol Chem 267 (33), 23471-23474 (1992)
   PUBMED   1358884
REFERENCE   10 (residues 1 to 431)
  AUTHORS   Takagaki,Y., MacDonald,C.C., Shenk,T. and Manley,J.L.
  TITLE     The human 64-kDa polyadenylylation factor contains a
            ribonucleoprotein-type RNA binding domain and unusual auxiliary
            motifs
  JOURNAL   Proc Natl Acad Sci U S A 89 (4), 1403-1407 (1992)
   PUBMED   1741396
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU189971.1, L02547.1,
            BE958524.1, BU189431.1 and AL121914.31.
            
            Summary: This gene encodes one of three subunits which combine to
            form cleavage stimulation factor (CSTF). CSTF is involved in the
            polyadenylation and 3'end cleavage of pre-mRNAs. Similar to
            mammalian G protein beta subunits, this protein contains
            transducin-like repeats. Several transcript variants with different
            5' UTR, but encoding the same protein, have been found for this
            gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.195462.1,
                                           SRR1803613.171534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000217109.9/ ENSP00000217109.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..431
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.2-q13.31"
     Protein         1..431
                     /product="cleavage stimulation factor subunit 1"
                     /note="CSTF 50 kDa subunit; CF-1 50 kDa subunit; cleavage
                     stimulation factor 50 kDa subunit; cleavage stimulation
                     factor, 3' pre-RNA, subunit 1, 50kD; cleavage stimulation
                     factor, 3' pre-RNA, subunit 1, 50kDa"
                     /calculated_mol_wt=48227
     Region          8..59
                     /region_name="CSTF1_dimer"
                     /note="Cleavage stimulation factor subunit 1, dimerization
                     domain; pfam16699"
                     /db_xref="CDD:465240"
     Region          14..35
                     /region_name="Hydrophobic"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          100..424
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          106..145
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Site            order(107,125,129,135..136,171..172,190,194,200..201,
                     215..216,233,238,244..245,261,278,283,289..290,303..304,
                     323,327,333..334,346,355,369,375,381..382,395..396,414,
                     418,424)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          116..171
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          171..210
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          177..215
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..254
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          220..259
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          260..301
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          266..301
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          303..343
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          309..345
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          356..393
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          395..430
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q05048.1)"
     Region          400..424
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..431
                     /gene="CSTF1"
                     /gene_synonym="CstF-50; CstFp50"
                     /coded_by="NM_001324.3:102..1397"
                     /db_xref="CCDS:CCDS13452.1"
                     /db_xref="GeneID:1477"
                     /db_xref="HGNC:HGNC:2483"
                     /db_xref="MIM:600369"
ORIGIN      
        1 myrtkvglkd rqqlykliis qllydgyisi anglineikp qsvcapseql lhliklgmen
       61 ddtavqyaig rsdtvapgtg idlefdadvq tmspeaseye tcyvtshkgp crvatysrdg
      121 qliatgsada sikildterm laksampiev mmnetaqqnm enhpvirtly dhvdevtcla
      181 fhpteqilas gsrdytlklf dyskpsakra fkyiqeaeml rsisfhpsgd filvgtqhpt
      241 lrlydintfq cfvscnpqdq htdaicsvny nssanmyvtg skdgciklwd gvsnrcittf
      301 ekahdgaevc saifsknsky ilssgkdsva klweistgrt lvrytgagls grqvhrtqav
      361 fnhtedyvll pdertislcc wdsrtaerrn llslghnniv rcivhsptnp gfmtcsddfr
      421 arfwyrrstt d
//
LOCUS       NP_001159830             483 aa            linear   PRI 20-NOV-2025
DEFINITION  serine hydroxymethyltransferase, mitochondrial isoform 3 [Homo
            sapiens].
ACCESSION   NP_001159830
VERSION     NP_001159830.1
DBSOURCE    REFSEQ: accession NM_001166358.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Qiao,Z., Li,Y., Li,S., Liu,S. and Cheng,Y.
  TITLE     Hypoxia-induced SHMT2 protein lactylation facilitates glycolysis
            and stemness of esophageal cancer cells
  JOURNAL   Mol Cell Biochem 479 (11), 3063-3076 (2024)
   PUBMED   38175377
  REMARK    GeneRIF: Hypoxia-induced SHMT2 protein lactylation facilitates
            glycolysis and stemness of esophageal cancer cells.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Han,T., Wang,Y., Cheng,M., Hu,Q., Wan,X., Huang,M., Liu,Y., Xun,W.,
            Xu,J., Wang,L., Luo,R., Yuan,Y., Wang,K. and Wang,J.
  TITLE     Phosphorylated SHMT2 Regulates Oncogenesis Through m6A Modification
            in Lung Adenocarcinoma
  JOURNAL   Adv Sci (Weinh) 11 (18), e2307834 (2024)
   PUBMED   38460155
  REMARK    GeneRIF: Phosphorylated SHMT2 Regulates Oncogenesis Through m[6]A
            Modification in Lung Adenocarcinoma.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Malatesta,M., Fornasier,E., Di Salvo,M.L., Tramonti,A.,
            Zangelmi,E., Peracchi,A., Secchi,A., Polverini,E., Giachin,G.,
            Battistutta,R., Contestabile,R. and Percudani,R.
  TITLE     One substrate many enzymes virtual screening uncovers missing genes
            of carnitine biosynthesis in human and mouse
  JOURNAL   Nat Commun 15 (1), 3199 (2024)
   PUBMED   38615009
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Shan,Y., Liu,D., Li,Y., Wu,C. and Ye,Y.
  TITLE     The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer
  JOURNAL   PeerJ 12, e16594 (2024)
   PUBMED   38188143
  REMARK    GeneRIF: The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Bennett,F.I. and Jackson,A.A.
  TITLE     Glycine is not formed through the amino transferase reaction in
            human or rat placenta
  JOURNAL   Placenta 19 (4), 329-331 (1998)
   PUBMED   9639330
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Girgis,S., Nasrallah,I.M., Suh,J.R., Oppenheim,E., Zanetti,K.A.,
            Mastri,M.G. and Stover,P.J.
  TITLE     Molecular cloning, characterization and alternative splicing of the
            human cytoplasmic serine hydroxymethyltransferase gene
  JOURNAL   Gene 210 (2), 315-324 (1998)
   PUBMED   9573390
  REMARK    GeneRIF: This paper compares the mitochondrial and cytoplasmic
            forms of this enzyme and suggests that the two genes are a result
            of a single gene duplication.
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Trakatellis,A., Dimitriadou,A. and Trakatelli,M.
  TITLE     Pyridoxine deficiency: new approaches in immunosuppression and
            chemotherapy
  JOURNAL   Postgrad Med J 73 (864), 617-622 (1997)
   PUBMED   9497969
  REMARK    Review article
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Stover,P.J., Chen,L.H., Suh,J.R., Stover,D.M., Keyomarsi,K. and
            Shane,B.
  TITLE     Molecular cloning, characterization, and regulation of the human
            mitochondrial serine hydroxymethyltransferase gene
  JOURNAL   J Biol Chem 272 (3), 1842-1848 (1997)
   PUBMED   8999870
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Garrow,T.A., Brenner,A.A., Whitehead,V.M., Chen,X.N., Duncan,R.G.,
            Korenberg,J.R. and Shane,B.
  TITLE     Cloning of human cDNAs encoding mitochondrial and cytosolic serine
            hydroxymethyltransferases and chromosomal localization
  JOURNAL   J Biol Chem 268 (16), 11910-11916 (1993)
   PUBMED   8505317
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Waziri,R., Baruah,S. and Sherman,A.D.
  TITLE     Abnormal serine-glycine metabolism in the brains of schizophrenics
  JOURNAL   Schizophr Res 8 (3), 233-243 (1993)
   PUBMED   8435385
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647711.1, AC137834.9 and
            BC091501.1.
            
            Summary: This gene encodes the mitochondrial form of a pyridoxal
            phosphate-dependent enzyme that catalyzes the reversible reaction
            of serine and tetrahydrofolate to glycine and 5,10-methylene
            tetrahydrofolate. The encoded product is primarily responsible for
            glycine synthesis. The activity of the encoded protein has been
            suggested to be the primary source of intracellular glycine. The
            gene which encodes the cytosolic form of this enzyme is located on
            chromosome 17. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus, compared to isoform 1. Variants 3, 4,
            and 5 encode the same isoform 3. Translation efficiency is
            uncertain from this alternative start codon, and there is rapid
            turnover of the mitochondrial protein in the cytoplasm prior to
            mitochondrial import due to its shortened import presequence (PMID
            8999870).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.132004.1,
                                           SRR1803617.84139.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..483
                     /product="serine hydroxymethyltransferase, mitochondrial
                     isoform 3"
                     /EC_number="2.1.2.1"
                     /note="glycine hydroxymethyltransferase; serine aldolase;
                     serine hydroxymethylase; threonine aldolase; GLY A+;
                     glycine auxotroph A, human complement for hamster; serine
                     methylase; epididymis secretory sperm binding protein Li
                     51e; serine hydroxymethyltransferase 2 (mitochondrial);
                     mitochondrial serine hydroxymethyltransferase"
                     /calculated_mol_wt=53324
     Region          24..481
                     /region_name="PLN03226"
                     /note="serine hydroxymethyltransferase; Provisional"
                     /db_xref="CDD:215639"
     Site            order(32,34,41..42,51,56,74,92..93,101,120,127,167..168,
                     307,325)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(55,75,85,122..123,150,205,230,233,258..259,265,404)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(55,150,259,404)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(77,84,145,149,151,299,389)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
     CDS             1..483
                     /gene="SHMT2"
                     /gene_synonym="GLYA; HEL-S-51e; mSHMT; NEDCASB; SHMT"
                     /coded_by="NM_001166358.2:134..1585"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53805.1"
                     /db_xref="GeneID:6472"
                     /db_xref="HGNC:HGNC:10852"
                     /db_xref="MIM:138450"
ORIGIN      
        1 mairaqhsna aqtqtgeanr gwtgqeslsd sdpemwellq rekdrqcrgl eliasenfcs
       61 raalealgsc lnnkysegyp gkryyggaev vdeiellcqr raleafdldp aqwgvnvqpy
      121 sgspanlavy tallqphdri mgldlpdggh lthgymsdvk risatsiffe smpyklnpkt
      181 glidynqlal tarlfrprli iagtsayarl idyarmrevc devkahllad mahisglvaa
      241 kvipspfkha divtttthkt lrgarsglif yrkgvkavdp ktgreipytf edrinfavfp
      301 slqggphnha iaavavalkq actpmfreys lqvlknaram adallergys lvsggtdnhl
      361 vlvdlrpkgl dgaraervle lvsitanknt cpgdrsaitp gglrlgapal tsrqfreddf
      421 rrvvdfideg vniglevksk taklqdfksf llkdsetsqr lanlrqrveq farafpmpgf
      481 deh
//
LOCUS       NP_001104268             429 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 16, NatA auxiliary subunit isoform 3
            [Homo sapiens].
ACCESSION   NP_001104268
VERSION     NP_001104268.1
DBSOURCE    REFSEQ: accession NM_001110798.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Arnesen,T., Gromyko,D., Kagabo,D., Betts,M.J., Starheim,K.K.,
            Varhaug,J.E., Anderson,D. and Lillehaug,J.R.
  TITLE     A novel human NatA Nalpha-terminal acetyltransferase complex:
            hNaa16p-hNaa10p (hNat2-hArd1)
  JOURNAL   BMC Biochem 10, 15 (2009)
   PUBMED   19480662
  REMARK    GeneRIF: hNaa16p (NARG1L) interacts with hNaa10p (hArd1) making a
            distinct ribosome associated human NatA N-terminal
            acetyltransferase complex. hNAA16 is expressed in a variety of
            human cell lines and specific knockdown of hNAA16 induces cell
            death.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Arnesen,T., Betts,M.J., Pendino,F., Liberles,D.A., Anderson,D.,
            Caro,J., Kong,X., Varhaug,J.E. and Lillehaug,J.R.
  TITLE     Characterization of hARD2, a processed hARD1 gene duplicate,
            encoding a human protein N-alpha-acetyltransferase
  JOURNAL   BMC Biochem 7, 13 (2006)
   PUBMED   16638120
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Dunham,A., Matthews,L.H., Burton,J., Ashurst,J.L., Howe,K.L.,
            Ashcroft,K.J., Beare,D.M., Burford,D.C., Hunt,S.E.,
            Griffiths-Jones,S., Jones,M.C., Keenan,S.J., Oliver,K., Scott,C.E.,
            Ainscough,R., Almeida,J.P., Ambrose,K.D., Andrews,D.T.,
            Ashwell,R.I., Babbage,A.K., Bagguley,C.L., Bailey,J., Bannerjee,R.,
            Barlow,K.F., Bates,K., Beasley,H., Bird,C.P., Bray-Allen,S.,
            Brown,A.J., Brown,J.Y., Burrill,W., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M.E., Clark,S.Y., Clarke,G., Clee,C.M.,
            Clegg,S.C., Cobley,V., Collins,J.E., Corby,N., Coville,G.J.,
            Deloukas,P., Dhami,P., Dunham,I., Dunn,M., Earthrowl,M.E.,
            Ellington,A.G., Faulkner,L., Frankish,A.G., Frankland,J.,
            French,L., Garner,P., Garnett,J., Gilbert,J.G., Gilson,C.J.,
            Ghori,J., Grafham,D.V., Gribble,S.M., Griffiths,C., Hall,R.E.,
            Hammond,S., Harley,J.L., Hart,E.A., Heath,P.D., Howden,P.J.,
            Huckle,E.J., Hunt,P.J., Hunt,A.R., Johnson,C., Johnson,D., Kay,M.,
            Kimberley,A.M., King,A., Laird,G.K., Langford,C.J., Lawlor,S.,
            Leongamornlert,D.A., Lloyd,D.M., Lloyd,C., Loveland,J.E.,
            Lovell,J., Martin,S., Mashreghi-Mohammadi,M., McLaren,S.J.,
            McMurray,A., Milne,S., Moore,M.J., Nickerson,T., Palmer,S.A.,
            Pearce,A.V., Peck,A.I., Pelan,S., Phillimore,B., Porter,K.M.,
            Rice,C.M., Searle,S., Sehra,H.K., Shownkeen,R., Skuce,C.D.,
            Smith,M., Steward,C.A., Sycamore,N., Tester,J., Thomas,D.W.,
            Tracey,A., Tromans,A., Tubby,B., Wall,M., Wallis,J.M., West,A.P.,
            Whitehead,S.L., Willey,D.L., Wilming,L., Wray,P.W., Wright,M.W.,
            Young,L., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E., Beck,S.,
            Bentley,D.R., Rogers,J. and Ross,M.T.
  TITLE     The DNA sequence and analysis of human chromosome 13
  JOURNAL   Nature 428 (6982), 522-528 (2004)
   PUBMED   15057823
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB078940.1, BC064592.1, AL590665.9 and BE501152.1.
            
            Transcript Variant: This variant (3) lacks several coding exons and
            differs in the 3' UTR, compared to variant 1, resulting in a
            shorter protein (isoform 3) with a unique C-terminus, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064592.1, SRR1660807.222020.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.11"
     Protein         1..429
                     /product="N-alpha-acetyltransferase 16, NatA auxiliary
                     subunit isoform 3"
                     /note="NMDA receptor-regulated 1-like protein; NARG1-like
                     protein"
                     /calculated_mol_wt=50430
     Region          13..38
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          21..243
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          46..79
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          47..74
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          80..113
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          82..108
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(84..85,88..89,91,115,118..119,122..123,125..126,149,
                     152..153,156..157,160)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          113..143
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          148..184
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          148..173
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          187..>419
                     /region_name="NatA_aux_su"
                     /note="N-terminal acetyltransferase A, auxiliary subunit;
                     pfam12569"
                     /db_xref="CDD:463630"
     Region          224..257
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     Region          374..407
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6N069.2)"
     CDS             1..429
                     /gene="NAA16"
                     /gene_synonym="NARG1L"
                     /coded_by="NM_001110798.2:263..1552"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45044.1"
                     /db_xref="GeneID:79612"
                     /db_xref="HGNC:HGNC:26164"
                     /db_xref="MIM:619497"
ORIGIN      
        1 mpnvllppke snlfkrilkc yeqkqykngl kfckmilsnp kfaehgetla mkgltlnclg
       61 kkeeayefvr kglrndvksh vcwhvygllq rsdkkydeai kcyrnalkld kdnlqilrdl
      121 sllqiqmrdl egyretryql lqlrptqras wigyaiayhl lkdydmalkl leefrqtqqv
      181 ppnkidyeys elilyqnqvm readllqesl ehiemyekqi cdkllveeik geillklgrl
      241 keasevfknl idrnaenwcy yeglekalqi stleerlqiy eeiskqhpka itprrlpltl
      301 vpgerfrelm dkflrvnfsk gcpplfttlk slyyntekvs iiqelvtnye aslktcdffs
      361 pyengekepp ttllwvqyfl aqhfdklgqy slaldyinaa iastptliel fymkakiykv
      421 ksescflss
//
LOCUS       NP_001159831             483 aa            linear   PRI 20-NOV-2025
DEFINITION  serine hydroxymethyltransferase, mitochondrial isoform 3 [Homo
            sapiens].
ACCESSION   NP_001159831
VERSION     NP_001159831.1
DBSOURCE    REFSEQ: accession NM_001166359.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 483)
  AUTHORS   Qiao,Z., Li,Y., Li,S., Liu,S. and Cheng,Y.
  TITLE     Hypoxia-induced SHMT2 protein lactylation facilitates glycolysis
            and stemness of esophageal cancer cells
  JOURNAL   Mol Cell Biochem 479 (11), 3063-3076 (2024)
   PUBMED   38175377
  REMARK    GeneRIF: Hypoxia-induced SHMT2 protein lactylation facilitates
            glycolysis and stemness of esophageal cancer cells.
REFERENCE   2  (residues 1 to 483)
  AUTHORS   Han,T., Wang,Y., Cheng,M., Hu,Q., Wan,X., Huang,M., Liu,Y., Xun,W.,
            Xu,J., Wang,L., Luo,R., Yuan,Y., Wang,K. and Wang,J.
  TITLE     Phosphorylated SHMT2 Regulates Oncogenesis Through m6A Modification
            in Lung Adenocarcinoma
  JOURNAL   Adv Sci (Weinh) 11 (18), e2307834 (2024)
   PUBMED   38460155
  REMARK    GeneRIF: Phosphorylated SHMT2 Regulates Oncogenesis Through m[6]A
            Modification in Lung Adenocarcinoma.
REFERENCE   3  (residues 1 to 483)
  AUTHORS   Malatesta,M., Fornasier,E., Di Salvo,M.L., Tramonti,A.,
            Zangelmi,E., Peracchi,A., Secchi,A., Polverini,E., Giachin,G.,
            Battistutta,R., Contestabile,R. and Percudani,R.
  TITLE     One substrate many enzymes virtual screening uncovers missing genes
            of carnitine biosynthesis in human and mouse
  JOURNAL   Nat Commun 15 (1), 3199 (2024)
   PUBMED   38615009
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 483)
  AUTHORS   Shan,Y., Liu,D., Li,Y., Wu,C. and Ye,Y.
  TITLE     The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer
  JOURNAL   PeerJ 12, e16594 (2024)
   PUBMED   38188143
  REMARK    GeneRIF: The expression and clinical significance of serine
            hydroxymethyltransferase2 in gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 483)
  AUTHORS   Bennett,F.I. and Jackson,A.A.
  TITLE     Glycine is not formed through the amino transferase reaction in
            human or rat placenta
  JOURNAL   Placenta 19 (4), 329-331 (1998)
   PUBMED   9639330
REFERENCE   6  (residues 1 to 483)
  AUTHORS   Girgis,S., Nasrallah,I.M., Suh,J.R., Oppenheim,E., Zanetti,K.A.,
            Mastri,M.G. and Stover,P.J.
  TITLE     Molecular cloning, characterization and alternative splicing of the
            human cytoplasmic serine hydroxymethyltransferase gene
  JOURNAL   Gene 210 (2), 315-324 (1998)
   PUBMED   9573390
  REMARK    GeneRIF: This paper compares the mitochondrial and cytoplasmic
            forms of this enzyme and suggests that the two genes are a result
            of a single gene duplication.
REFERENCE   7  (residues 1 to 483)
  AUTHORS   Trakatellis,A., Dimitriadou,A. and Trakatelli,M.
  TITLE     Pyridoxine deficiency: new approaches in immunosuppression and
            chemotherapy
  JOURNAL   Postgrad Med J 73 (864), 617-622 (1997)
   PUBMED   9497969
  REMARK    Review article
REFERENCE   8  (residues 1 to 483)
  AUTHORS   Stover,P.J., Chen,L.H., Suh,J.R., Stover,D.M., Keyomarsi,K. and
            Shane,B.
  TITLE     Molecular cloning, characterization, and regulation of the human
            mitochondrial serine hydroxymethyltransferase gene
  JOURNAL   J Biol Chem 272 (3), 1842-1848 (1997)
   PUBMED   8999870
REFERENCE   9  (residues 1 to 483)
  AUTHORS   Garrow,T.A., Brenner,A.A., Whitehead,V.M., Chen,X.N., Duncan,R.G.,
            Korenberg,J.R. and Shane,B.
  TITLE     Cloning of human cDNAs encoding mitochondrial and cytosolic serine
            hydroxymethyltransferases and chromosomal localization
  JOURNAL   J Biol Chem 268 (16), 11910-11916 (1993)
   PUBMED   8505317
REFERENCE   10 (residues 1 to 483)
  AUTHORS   Waziri,R., Baruah,S. and Sherman,A.D.
  TITLE     Abnormal serine-glycine metabolism in the brains of schizophrenics
  JOURNAL   Schizophr Res 8 (3), 233-243 (1993)
   PUBMED   8435385
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN395976.1, AK296183.1,
            AC137834.9 and BC091501.1.
            
            Summary: This gene encodes the mitochondrial form of a pyridoxal
            phosphate-dependent enzyme that catalyzes the reversible reaction
            of serine and tetrahydrofolate to glycine and 5,10-methylene
            tetrahydrofolate. The encoded product is primarily responsible for
            glycine synthesis. The activity of the encoded protein has been
            suggested to be the primary source of intracellular glycine. The
            gene which encodes the cytosolic form of this enzyme is located on
            chromosome 17. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (5) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (3) has a shorter N-terminus, compared to isoform 1. Variants 3, 4,
            and 5 encode the same isoform 3. Translation efficiency is
            uncertain from this alternative start codon, and there is rapid
            turnover of the mitochondrial protein in the cytoplasm prior to
            mitochondrial import due to its shortened import presequence (PMID
            8999870).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296183.1, SRR14038194.1165986.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..483
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..483
                     /product="serine hydroxymethyltransferase, mitochondrial
                     isoform 3"
                     /EC_number="2.1.2.1"
                     /note="glycine hydroxymethyltransferase; serine aldolase;
                     serine hydroxymethylase; threonine aldolase; GLY A+;
                     glycine auxotroph A, human complement for hamster; serine
                     methylase; epididymis secretory sperm binding protein Li
                     51e; serine hydroxymethyltransferase 2 (mitochondrial);
                     mitochondrial serine hydroxymethyltransferase"
                     /calculated_mol_wt=53324
     Region          24..481
                     /region_name="PLN03226"
                     /note="serine hydroxymethyltransferase; Provisional"
                     /db_xref="CDD:215639"
     Site            order(32,34,41..42,51,56,74,92..93,101,120,127,167..168,
                     307,325)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(55,75,85,122..123,150,205,230,233,258..259,265,404)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(55,150,259,404)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(77,84,145,149,151,299,389)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
     CDS             1..483
                     /gene="SHMT2"
                     /gene_synonym="GLYA; HEL-S-51e; mSHMT; NEDCASB; SHMT"
                     /coded_by="NM_001166359.1:124..1575"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS53805.1"
                     /db_xref="GeneID:6472"
                     /db_xref="HGNC:HGNC:10852"
                     /db_xref="MIM:138450"
ORIGIN      
        1 mairaqhsna aqtqtgeanr gwtgqeslsd sdpemwellq rekdrqcrgl eliasenfcs
       61 raalealgsc lnnkysegyp gkryyggaev vdeiellcqr raleafdldp aqwgvnvqpy
      121 sgspanlavy tallqphdri mgldlpdggh lthgymsdvk risatsiffe smpyklnpkt
      181 glidynqlal tarlfrprli iagtsayarl idyarmrevc devkahllad mahisglvaa
      241 kvipspfkha divtttthkt lrgarsglif yrkgvkavdp ktgreipytf edrinfavfp
      301 slqggphnha iaavavalkq actpmfreys lqvlknaram adallergys lvsggtdnhl
      361 vlvdlrpkgl dgaraervle lvsitanknt cpgdrsaitp gglrlgapal tsrqfreddf
      421 rrvvdfideg vniglevksk taklqdfksf llkdsetsqr lanlrqrveq farafpmpgf
      481 deh
//
LOCUS       NP_036391                337 aa            linear   PRI 20-NOV-2025
DEFINITION  hairy/enhancer-of-split related with YRPW motif protein 2 [Homo
            sapiens].
ACCESSION   NP_036391
VERSION     NP_036391.1
DBSOURCE    REFSEQ: accession NM_012259.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 337)
  AUTHORS   van Walree,E.S., Dombrowsky,G., Jansen,I.E., Mirkov,M.U., Zwart,R.,
            Ilgun,A., Guo,D., Clur,S.B., Amin,A.S., Savage,J.E., van der
            Wal,A.C., Waisfisz,Q., Maugeri,A., Wilsdon,A., Bu'Lock,F.A.,
            Hurles,M.E., Dittrich,S., Berger,F., Audain Martinez,E.,
            Christoffels,V.M., Hitz,M.P., Milewicz,D.M., Posthuma,D.,
            Meijers-Heijboer,H., Postma,A.V. and Mathijssen,I.B.
  TITLE     Germline variants in HEY2 functional domains lead to congenital
            heart defects and thoracic aortic aneurysms
  JOURNAL   Genet Med 23 (1), 103-110 (2021)
   PUBMED   32820247
  REMARK    GeneRIF: Germline variants in HEY2 functional domains lead to
            congenital heart defects and thoracic aortic aneurysms.
            Erratum:[Genet Med. 2022 Apr;24(4):965. doi:
            10.1016/j.gim.2022.01.018. PMID: 35394427]
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Yu,H., Hu,W., Song,X. and Zhao,Y.
  TITLE     Notch-HEY2 signaling pathway contributes to the differentiation of
            CD34+ hematopoietic-like stem cells from adult peripheral blood
            insulin-producing cells after the treatment with platelet-derived
            mitochondria
  JOURNAL   Mol Biol Rep 47 (10), 8347-8352 (2020)
   PUBMED   32997309
  REMARK    GeneRIF: Notch-HEY2 signaling pathway contributes to the
            differentiation of CD34(+) hematopoietic-like stem cells from adult
            peripheral blood insulin-producing cells after the treatment with
            platelet-derived mitochondria.
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Firulli,B.A., Hadzic,D.B., McDaid,J.R. and Firulli,A.B.
  TITLE     The basic helix-loop-helix transcription factors dHAND and eHAND
            exhibit dimerization characteristics that suggest complex
            regulation of function
  JOURNAL   J Biol Chem 275 (43), 33567-33573 (2000)
   PUBMED   10924525
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Steidl,C., Leimeister,C., Klamt,B., Maier,M., Nanda,I., Dixon,M.,
            Clarke,R., Schmid,M. and Gessler,M.
  TITLE     Characterization of the human and mouse HEY1, HEY2, and HEYL genes:
            cloning, mapping, and mutation screening of a new bHLH gene family
  JOURNAL   Genomics 66 (2), 195-203 (2000)
   PUBMED   10860664
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Zhong,T.P., Rosenberg,M., Mohideen,M.A., Weinstein,B. and
            Fishman,M.C.
  TITLE     gridlock, an HLH gene required for assembly of the aorta in
            zebrafish
  JOURNAL   Science 287 (5459), 1820-1824 (2000)
   PUBMED   10710309
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Chin,M.T., Maemura,K., Fukumoto,S., Jain,M.K., Layne,M.D.,
            Watanabe,M., Hsieh,C.M. and Lee,M.E.
  TITLE     Cardiovascular basic helix loop helix factor 1, a novel
            transcriptional repressor expressed preferentially in the
            developing and adult cardiovascular system
  JOURNAL   J Biol Chem 275 (9), 6381-6387 (2000)
   PUBMED   10692439
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Leimeister,C., Externbrink,A., Klamt,B. and Gessler,M.
  TITLE     Hey genes: a novel subfamily of hairy- and Enhancer of split
            related genes specifically expressed during mouse embryogenesis
  JOURNAL   Mech Dev 85 (1-2), 173-177 (1999)
   PUBMED   10415358
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI549391.1, BC007707.2 and
            AJ249545.1.
            
            Summary: This gene encodes a member of the hairy and enhancer of
            split-related (HESR) family of basic helix-loop-helix (bHLH)-type
            transcription factors. The encoded protein forms homo- or
            hetero-dimers that localize to the nucleus and interact with a
            histone deacetylase complex to repress transcription. Expression of
            this gene is induced by the Notch signal transduction pathway. Two
            similar and redundant genes in mouse are required for embryonic
            cardiovascular development, and are also implicated in neurogenesis
            and somitogenesis. Alternatively spliced transcript variants have
            been found, but their biological validity has not been determined.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.90043.1,
                                           SRR1660809.152616.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368364.4/ ENSP00000357348.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..337
                     /product="hairy/enhancer-of-split related with YRPW motif
                     protein 2"
                     /note="HES-related repressor protein 1; cardiovascular
                     basic helix-loop-helix factor 1; hairy-related
                     transcription factor 2; HRT-2; hCHF1; hHRT2; HESR-2;
                     protein gridlock homolog; HES-related repressor protein 2;
                     cardiovascular helix-loop-helix factor 1; class B basic
                     helix-loop-helix protein 32; hairy and enhancer of
                     split-related protein 2; hairy/enhancer-of-split related
                     with YRPW motif 2"
                     /calculated_mol_wt=35677
     Region          1..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBP5.1)"
     Region          40..121
                     /region_name="bHLH-O_HEY2"
                     /note="basic helix-loop-helix-orange (bHLH-O) domain found
                     in hairy/enhancer-of-split related with YRPW motif protein
                     2 (HEY2) and similar proteins; cd18920"
                     /db_xref="CDD:381490"
     Region          47..116
                     /region_name="Transcriptional repression and interaction
                     with NCOR1 and SIN3A. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBP5.1)"
     Site            order(53..55,58,60..61,65,88..89)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381490"
     Site            order(60..61,63..65,67..68,70..71,74..75,78,86,88..90,
                     93..94,96..97,99..101,103..104,107)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381490"
     Region          119..165
                     /region_name="ORANGE"
                     /note="Orange domain; smart00511"
                     /db_xref="CDD:128787"
     Region          307..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBP5.1)"
     Region          327..330
                     /region_name="YRPW motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBP5.1)"
     CDS             1..337
                     /gene="HEY2"
                     /gene_synonym="bHLHb32; CHF1; GRIDLOCK; GRL; HERP1; HESR2;
                     HRT2"
                     /coded_by="NM_012259.3:146..1159"
                     /db_xref="CCDS:CCDS5131.1"
                     /db_xref="GeneID:23493"
                     /db_xref="HGNC:HGNC:4881"
                     /db_xref="MIM:604674"
ORIGIN      
        1 mkrpceetts esdmdetidv gsennysgqs tssvirlnsp tttsqimark krrgiiekrr
       61 rdrinnslse lrrlvptafe kqgsakleka eilqmtvdhl kmlqatggkg yfdahalamd
      121 fmsigfrecl tevarylssv egldssdplr vrlvshlstc atqreaaamt ssmahhhhpl
      181 hphhwaaafh hlpaallqpn glhasestpc rlsttsevpp ahgsalltat fahadsalrm
      241 pstgsvapcv pplstsllsl satvhaaaaa ataaahsfpl sfagafpmlp pnaaaavaaa
      301 taispplsvs atsspqqtss gtnnkpyrpw gtevgaf
//
LOCUS       NP_055929                938 aa            linear   PRI 20-NOV-2025
DEFINITION  ankyrin repeat and LEM domain-containing protein 2 [Homo sapiens].
ACCESSION   NP_055929 XP_931084
VERSION     NP_055929.1
DBSOURCE    REFSEQ: accession NM_015114.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 938)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 938)
  AUTHORS   Thomas,A.X., Link,N., Robak,L.A., Demmler-Harrison,G., Pao,E.C.,
            Squire,A.E., Michels,S., Cohen,J.S., Comi,A., Prontera,P., Verrotti
            di Pianella,A., Di Cara,G., Garavelli,L., Caraffi,S.G., Fusco,C.,
            Zuntini,R., Parks,K.C., Sherr,E.H., Hashem,M.O., Maddirevula,S.,
            Alkuraya,F.S., Contractar,I.A.F., Neil,J.E., Walsh,C.A.,
            Bellen,H.J., Chao,H.T., Clark,R.D. and Mirzaa,G.M.
  TITLE     ANKLE2-related microcephaly: A variable microcephaly syndrome
            resembling Zika infection
  JOURNAL   Ann Clin Transl Neurol 9 (8), 1276-1288 (2022)
   PUBMED   35871307
  REMARK    GeneRIF: ANKLE2-related microcephaly: A variable microcephaly
            syndrome resembling Zika infection.
REFERENCE   3  (residues 1 to 938)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 938)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 938)
  AUTHORS   Link,N., Chung,H., Jolly,A., Withers,M., Tepe,B., Arenkiel,B.R.,
            Shah,P.S., Krogan,N.J., Aydin,H., Geckinli,B.B., Tos,T., Isikay,S.,
            Tuysuz,B., Mochida,G.H., Thomas,A.X., Clark,R.D., Mirzaa,G.M.,
            Lupski,J.R. and Bellen,H.J.
  TITLE     Mutations in ANKLE2, a ZIKA Virus Target, Disrupt an Asymmetric
            Cell Division Pathway in Drosophila Neuroblasts to Cause
            Microcephaly
  JOURNAL   Dev Cell 51 (6), 713-729 (2019)
   PUBMED   31735666
  REMARK    GeneRIF: that NS4A, ANKLE2, VRK1, and LLGL1 define a pathway
            impinging on asymmetric determinants of neural stem cell division
REFERENCE   6  (residues 1 to 938)
  AUTHORS   Yamamoto,S., Jaiswal,M., Charng,W.L., Gambin,T., Karaca,E.,
            Mirzaa,G., Wiszniewski,W., Sandoval,H., Haelterman,N.A., Xiong,B.,
            Zhang,K., Bayat,V., David,G., Li,T., Chen,K., Gala,U., Harel,T.,
            Pehlivan,D., Penney,S., Vissers,L.E.L.M., de Ligt,J.,
            Jhangiani,S.N., Xie,Y., Tsang,S.H., Parman,Y., Sivaci,M.,
            Battaloglu,E., Muzny,D., Wan,Y.W., Liu,Z., Lin-Moore,A.T.,
            Clark,R.D., Curry,C.J., Link,N., Schulze,K.L., Boerwinkle,E.,
            Dobyns,W.B., Allikmets,R., Gibbs,R.A., Chen,R., Lupski,J.R.,
            Wangler,M.F. and Bellen,H.J.
  TITLE     A drosophila genetic resource of mutants to study mechanisms
            underlying human genetic diseases
  JOURNAL   Cell 159 (1), 200-214 (2014)
   PUBMED   25259927
REFERENCE   7  (residues 1 to 938)
  AUTHORS   Asencio,C., Davidson,I.F., Santarella-Mellwig,R., Ly-Hartig,T.B.,
            Mall,M., Wallenfang,M.R., Mattaj,I.W. and Gorjanacz,M.
  TITLE     Coordination of kinase and phosphatase activities by Lem4 enables
            nuclear envelope reassembly during mitosis
  JOURNAL   Cell 150 (1), 122-135 (2012)
   PUBMED   22770216
  REMARK    GeneRIF: By coordinating VRK-1- and PP2A-mediated signaling on BAF,
            Lem4 and LEM-4L (Y55F3BR.8) controls postmitotic nuclear envelope
            formation in a function conserved from worms to humans.
REFERENCE   8  (residues 1 to 938)
  AUTHORS   Ovsyannikova,I.G., Kennedy,R.B., O'Byrne,M., Jacobson,R.M.,
            Pankratz,V.S. and Poland,G.A.
  TITLE     Genome-wide association study of antibody response to smallpox
            vaccine
  JOURNAL   Vaccine 30 (28), 4182-4189 (2012)
   PUBMED   22542470
REFERENCE   9  (residues 1 to 938)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   10 (residues 1 to 938)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB453975.1, DB451935.1,
            BC043157.1, AB014592.1, AK293028.1, BC062373.1, R59085.1 and
            AC135586.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 8, 2007 this sequence version replaced XP_931084.2.
            
            Summary: This gene encodes a member of the LEM family of inner
            nuclear membrane proteins. The encoded protein functions as a
            mitotic regulator through postmitotic formation of the nuclear
            envelope. Mutations in this gene cause morphology defects in the
            nuclear envelope and BAF hyperphosphorylation. [provided by RefSeq,
            Mar 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1179574.1,
                                           SRR18074967.2377414.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357997.10/ ENSP00000350686.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..938
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.33"
     Protein         1..938
                     /product="ankyrin repeat and LEM domain-containing protein
                     2"
                     /note="LEM domain containing 7; LEM domain-containing
                     protein 4; LEM-domain protein 4"
                     /calculated_mol_wt=103984
     Site            13..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XL3.4)"
     Region          71..113
                     /region_name="LEM_ANKL2"
                     /note="LEM (Lap2/Emerin/Man1) domain found in ankyrin
                     repeat and LEM domain-containing protein 2 (ANKL2);
                     cd12944"
                     /db_xref="CDD:240591"
     Site            order(77..78,90..95,97..98,101..102,104..105)
                     /site_type="other"
                     /note="putative polypeptide substrate binding site
                     [polypeptide binding]"
                     /db_xref="CDD:240591"
     Region          199..249
                     /region_name="Cauli_VI"
                     /note="Caulimovirus viroplasmin; pfam01693"
                     /db_xref="CDD:460297"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            268
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Region          <303..467
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          355..386
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          410..443
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          411..440
                     /region_name="ANK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            488
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            512
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Region          609..636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            662
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            804
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Region          870..924
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            896
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     Site            914
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q86XL3.4)"
     CDS             1..938
                     /gene="ANKLE2"
                     /gene_synonym="KIAA0692; Lem4; LEMD7; MCPH16"
                     /coded_by="NM_015114.3:35..2851"
                     /db_xref="CCDS:CCDS41869.1"
                     /db_xref="GeneID:23141"
                     /db_xref="HGNC:HGNC:29101"
                     /db_xref="MIM:616062"
ORIGIN      
        1 mlwprlaaae waalawellg asvlliavrw lvrrlgprpg glgrsgtpvp ppsaaaapas
       61 gemtmdalla rlkllnpddl reeivkaglk cgpitsttrf ifekklaqal leqggrlssf
      121 yhheagvtal sqdpqrilkp aegnptdqag fsedrdfgys vglnppeeea vtsktcsvpp
      181 sdtdtyraga taskepplyy gvcpvyedvp arneriyvye nkkealqavk mikgsrfkaf
      241 stredaekfa rgicdyfpsp sktslplspv ktaplfsndr lkdglclses etvnkerans
      301 yknprtqdlt aklrkavekg eedtfsdliw snpryligsg dnptivqegc rynvmhvaak
      361 enqasicqlt ldvlenpdfm rlmypdddea mlqkriryvv dlylntpdkm gydtplhfac
      421 kfgnadvvnv lsshhlivkn srnkydktpe dvicersknk svelkerire ylkghyyvpl
      481 lraeetsspv igelwspdqt aeashvsryg gsprdpvltl rafagplspa kaedfrklwk
      541 tpprekagfl hhvkksdper gfervgrela helgypwvey weflgcfvdl ssqeglqrle
      601 eyltqqeigk kaqqetgere ascrdkatts gsnsisvraf ldeddmslee iknrqnaarn
      661 nspptvgafg htrcsafple qeadlieaae pggphssrng lchplnhsrt lagkrpkapr
      721 geeahlppvs dltvefdkln lqnigrsvsk tpdestktkd qiltsrinav erdllepspa
      781 dqlgnghrrt esemsariak mslspssprh edqlevtrep arrlflfgee pskldqdvla
      841 alecadvdph qfpavhrwks avlcyspsdr qswpspavkg rfksqlpdls gphsyspgrn
      901 svagsnpakp glgspgrysp vhgsqlrrma rlaelaal
//
LOCUS       NP_004799                498 aa            linear   PRI 20-NOV-2025
DEFINITION  glycylpeptide N-tetradecanoyltransferase 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_004799
VERSION     NP_004799.1
DBSOURCE    REFSEQ: accession NM_004808.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 498)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 498)
  AUTHORS   Zhang,T., Goel,A., Xu,X., Wu,Y., Tang,E., Zhang,F., Li,Y., Li,H.,
            Cai,Y. and Weng,W.
  TITLE     N-mytistoyltransferase 1 and 2 are potential tumor suppressors and
            novel targets of miR-182 in human non-small cell lung carcinomas
  JOURNAL   Lung Cancer 171, 70-81 (2022)
   PUBMED   35930829
  REMARK    GeneRIF: N-mytistoyltransferase 1 and 2 are potential tumor
            suppressors and novel targets of miR-182 in human non-small cell
            lung carcinomas.
REFERENCE   3  (residues 1 to 498)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 498)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 498)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 498)
  AUTHORS   Seaton,K.E. and Smith,C.D.
  TITLE     N-Myristoyltransferase isozymes exhibit differential specificity
            for human immunodeficiency virus type 1 Gag and Nef
  JOURNAL   J Gen Virol 89 (Pt 1), 288-296 (2008)
   PUBMED   18089753
  REMARK    GeneRIF: Nef is preferentially myristoylated by NMT2, suggesting
            that selective inhibition of NMT2 may provide a novel means of
            blocking HIV virulence.
REFERENCE   7  (residues 1 to 498)
  AUTHORS   Pal,R., Reitz,M.S. Jr., Tschachler,E., Gallo,R.C.,
            Sarngadharan,M.G. and Veronese,F.D.
  TITLE     Myristoylation of gag proteins of HIV-1 plays an important role in
            virus assembly
  JOURNAL   AIDS Res Hum Retroviruses 6 (6), 721-730 (1990)
   PUBMED   2194551
REFERENCE   8  (residues 1 to 498)
  AUTHORS   Bryant,M. and Ratner,L.
  TITLE     Myristoylation-dependent replication and assembly of human
            immunodeficiency virus 1
  JOURNAL   Proc Natl Acad Sci U S A 87 (2), 523-527 (1990)
   PUBMED   2405382
REFERENCE   9  (residues 1 to 498)
  AUTHORS   Tashiro,A., Shoji,S. and Kubota,Y.
  TITLE     Antimyristoylation of the gag proteins in the human
            immunodeficiency virus-infected cells with N-myristoyl glycinal
            diethylacetal resulted in inhibition of virus production
  JOURNAL   Biochem Biophys Res Commun 165 (3), 1145-1154 (1989)
   PUBMED   2692561
REFERENCE   10 (residues 1 to 498)
  AUTHORS   Goddard,C., Aquino,A., Glazer,R.I. and Felsted,R.L.
  TITLE     Chemical characterization of p17gag from human immunodeficiency
            virus as an N-terminally myristoylated protein
  JOURNAL   Eur J Biochem 182 (2), 323-326 (1989)
   PUBMED   2737204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590365.14 and AF043325.1.
            
            Summary: This gene encodes one of two N-myristoyltransferase
            proteins. N-terminal myristoylation is a lipid modification that is
            involved in regulating the function and localization of signaling
            proteins. The encoded protein catalyzes the addition of a myristoyl
            group to the N-terminal glycine residue of many signaling proteins,
            including the human immunodeficiency virus type 1 (HIV-1) proteins,
            Gag and Nef. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Apr 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF043325.1, BC006376.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000378165.9/ ENSP00000367407.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..498
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p13"
     Protein         1..498
                     /product="glycylpeptide N-tetradecanoyltransferase 2
                     isoform 1"
                     /EC_number="2.3.1.97"
                     /note="NMT 2; type II N-myristoyltransferase; peptide
                     N-myristoyltransferase 2; myristoyl-CoA:protein
                     N-myristoyltransferase 2; protein-lysine
                     myristoyltransferase NMT2"
                     /calculated_mol_wt=56849
     Region          1..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60551.1)"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O60551.1)"
     Region          119..486
                     /region_name="NMT1"
                     /note="N-myristoyl transferase [Lipid metabolism];
                     COG5092"
                     /db_xref="CDD:227423"
     CDS             1..498
                     /gene="NMT2"
                     /coded_by="NM_004808.3:82..1578"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS7109.1"
                     /db_xref="GeneID:9397"
                     /db_xref="HGNC:HGNC:7858"
                     /db_xref="MIM:603801"
ORIGIN      
        1 maedsesaas qqslelddqd tcgidgdnee etehakgspg gylgakkkkk kqkrkkekpn
       61 sggtksdsas dsqeikiqqp sknpsvpmqk lqdiqramel lsacqgparn ideaakhryq
      121 fwdtqpvpkl devitshgai epdkdnvrqe pyslpqgfmw dtldlsdaev lkelytllne
      181 nyvedddnmf rfdyspefll walrppgwll qwhcgvrvss nkklvgfisa ipaniriyds
      241 vkkmveinfl cvhkklrskr vapvlireit rrvnlegifq avytagvvlp kpiatcrywh
      301 rslnprklve vkfshlsrnm tlqrtmklyr lpdvtktsgl rpmepkdiks vrelintylk
      361 qfhlapvmde eevahwflpr ehiidtfvve spngkltdfl sfytlpstvm hhpahkslka
      421 aysfynihte tplldlmsda lilakskgfd vfnaldlmen ktfleklkfg igdgnlqyyl
      481 ynwrcpgtds ekvglvlq
//
LOCUS       NP_001091873             865 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger and BTB domain-containing protein 21 isoform S [Homo
            sapiens].
ACCESSION   NP_001091873
VERSION     NP_001091873.1
DBSOURCE    REFSEQ: accession NM_001098403.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 865)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 865)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 865)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 865)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 865)
  AUTHORS   Heckerman,D., Traynor,B.J., Picca,A., Calvani,R., Marzetti,E.,
            Hernandez,D., Nalls,M., Arepali,S., Ferrucci,L. and Landi,F.
  TITLE     Genetic variants associated with physical performance and
            anthropometry in old age: a genome-wide association study in the
            ilSIRENTE cohort
  JOURNAL   Sci Rep 7 (1), 15879 (2017)
   PUBMED   29158487
  REMARK    GeneRIF: Genotyping was accomplished on Infinium Human610-QUAD
            version 1. In the ilSIRENTE population, genetic variants in ZNF295
            and C2CD2 (rs928874 and rs1788355) on chromosome 21q22.3, were
            significantly associated with the 4-meter gait speed
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 865)
  AUTHORS   Bartke,T., Vermeulen,M., Xhemalce,B., Robson,S.C., Mann,M. and
            Kouzarides,T.
  TITLE     Nucleosome-interacting proteins regulated by DNA and histone
            methylation
  JOURNAL   Cell 143 (3), 470-484 (2010)
   PUBMED   21029866
REFERENCE   7  (residues 1 to 865)
  AUTHORS   Wang,J., Kudoh,J., Takayanagi,A. and Shimizu,N.
  TITLE     Novel human BTB/POZ domain-containing zinc finger protein ZNF295 is
            directly associated with ZFP161
  JOURNAL   Biochem Biophys Res Commun 327 (2), 615-627 (2005)
   PUBMED   15629158
  REMARK    GeneRIF: ZNF295 may be involved in the bi-directional control of
            gene expression in concert with ZFP161
REFERENCE   8  (residues 1 to 865)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 865)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 865)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP230048.1 and AB041015.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks an in-frame segment in the coding region compared to variant
            5. Variants 3 and 4 encode isoform S, which is shorter than isoform
            L.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB041015.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..865
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..865
                     /product="zinc finger and BTB domain-containing protein 21
                     isoform S"
                     /note="zinc finger and BTB domain-containing protein 21;
                     zinc finger protein 295"
                     /calculated_mol_wt=95677
     Region          12..123
                     /region_name="BTB_POZ_ZBTB21_ZNF295"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in zinc finger and
                     BTB domain-containing protein 21 (ZBTB21); cd18209"
                     /db_xref="CDD:349518"
     Region          545..572
                     /region_name="zf_C2H2_6"
                     /note="Zinc Finger domain; pfam18450"
                     /db_xref="CDD:408245"
     Region          710..730
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Site            order(715,717,719,721..722,725..726,729,743,745..747,
                     753..754,758)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275370"
     Region          738..759
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275370"
     Region          842..864
                     /region_name="zf-C2H2"
                     /note="Zinc finger, C2H2 type; pfam00096"
                     /db_xref="CDD:395048"
     CDS             1..865
                     /gene="ZBTB21"
                     /gene_synonym="ZNF295"
                     /coded_by="NM_001098403.2:188..2785"
                     /note="isoform S is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS42934.1"
                     /db_xref="GeneID:49854"
                     /db_xref="HGNC:HGNC:13083"
                     /db_xref="MIM:616485"
ORIGIN      
        1 megllhyinp ahaisllsal neerlkgqlc dvllivgdqk frahknvlaa sseyfqslft
       61 nkenesqtvf qldfcepdaf dnvlnyiyss slfvekssla avqelgyslg isfltnivsk
      121 tpqapfptcp nrkkvfvedd enssqkrsvi vcqsrneaqg ktvsqnqpdv shtsrpspsi
      181 avkantnkph vpkpieplhn lsltekswpk dssvvyaksl ehsgslddpn rislvkrnav
      241 lpskplqdre amddkpgvsg qlpkgkalel alkrprppvl svcsssetpy llketnkgng
      301 qgedrnllyy sklglvipss gsgsgnqsid rsgplvksll rrslsmdsqv pvyspsidlk
      361 ssqgsssvss dapgnvlcal sqksslkdcs ektalddrpq vlqphrlrsf sasqstdreg
      421 aspvtevrik tepssplsdp sdiirvtvgd aattaaasss svtrdlslkt eddqkdmsrl
      481 pakrrfqadr rlpfkklkvn ehgspvsedn feegssptll dadfpdsdln kdefeqgshe
      541 rlcrnaavcp ycslrffspe lkqeheskce ykkltclecm rtfkssfsiw rhqvevhnqn
      601 nmaptenfsl pvldhngdvt gssrpqsqpe pnkvnhivtt kddnvfsdss eqvnfdseds
      661 sclpedlsls kqlkiqvkee pveeaeeeap eastapkeag pskeaslwpc ekcgkmftvh
      721 kqlerhqell csvkpfichv cnkafrtnfr lwshfqshms qaseesahke sevcpvptns
      781 psppplpppp plpkiqplep dsptglsenp tpateklfvp qesdtlfyha pplsaitfkr
      841 qfmcklchrt fktafslwsh eqthn
//
LOCUS       NP_904319                224 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 44 isoform 2 [Homo sapiens].
ACCESSION   NP_904319
VERSION     NP_904319.1
DBSOURCE    REFSEQ: accession NM_183412.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Thompson,L.L., Rutherford,K.A., Lepage,C.C. and McManus,K.J.
  TITLE     The SCF Complex Is Essential to Maintain Genome and Chromosome
            Stability
  JOURNAL   Int J Mol Sci 22 (16), 8544 (2021)
   PUBMED   34445249
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Shen,J.Z., Qiu,Z., Wu,Q., Finlay,D., Garcia,G., Sun,D., Rantala,J.,
            Barshop,W., Hope,J.L., Gimple,R.C., Sangfelt,O., Bradley,L.M.,
            Wohlschlegel,J., Rich,J.N. and Spruck,C.
  TITLE     FBXO44 promotes DNA replication-coupled repetitive element
            silencing in cancer cells
  JOURNAL   Cell 184 (2), 352-369 (2021)
   PUBMED   33357448
  REMARK    GeneRIF: FBXO44 promotes DNA replication-coupled repetitive element
            silencing in cancer cells.
REFERENCE   4  (residues 1 to 224)
  AUTHORS   McNabb,H.J., Gonzalez,S., Muli,C.S. and Sjogren,B.
  TITLE     N-Terminal Targeting of Regulator of G Protein Signaling Protein 2
            for F-Box Only Protein 44-Mediated Proteasomal Degradation
  JOURNAL   Mol Pharmacol 98 (6), 677-685 (2020)
   PUBMED   33008920
  REMARK    GeneRIF: N-Terminal Targeting of Regulator of G Protein Signaling
            Protein 2 for F-Box Only Protein 44-Mediated Proteasomal
            Degradation.
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Glenn,K.A., Nelson,R.F., Wen,H.M., Mallinger,A.J. and Paulson,H.L.
  TITLE     Diversity in tissue expression, substrate binding, and SCF complex
            formation for a lectin family of ubiquitin ligases
  JOURNAL   J Biol Chem 283 (19), 12717-12729 (2008)
   PUBMED   18203720
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Ilyin,G.P., Serandour,A.L., Pigeon,C., Rialland,M., Glaise,D. and
            Guguen-Guillouzo,C.
  TITLE     A new subfamily of structurally related human F-box proteins
  JOURNAL   Gene 296 (1-2), 11-20 (2002)
   PUBMED   12383498
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055344.1 and AL031731.44.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbxs class. It is also a member of the NFB42 (neural
            F Box 42 kDa) family, similar to F-box only protein 2 and F-box
            only protein 6. Several alternatively spliced transcript variants
            encoding two distinct isoforms have been found for this gene.
            [provided by RefSeq, Feb 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, uses an
            alternate splice junction at the 3' end of an internal exon, and
            lacks an alternate internal exon compared to variant 1, that causes
            a frameshift. The resulting isoform (2) has a shorter and distinct
            C-terminus compared to isoform 1. Variants 2, 3, and 5 all encode
            the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055344.1, SRR3476690.261442.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.22"
     Protein         1..224
                     /product="F-box only protein 44 isoform 2"
                     /note="F-box protein FBX30; F-box gene 3; F-box only
                     protein 44; F-box/G-domain protein 3"
                     /calculated_mol_wt=25567
     Region          3..85
                     /region_name="F-box_FBXO6-like"
                     /note="F-box domain found in F-box only proteins FBXO6,
                     FBXO44 and similar proteins; cd22168"
                     /db_xref="CDD:438939"
     Site            order(3,5..7,9..10,13,17,20,22,24..25,27,30..35,37..38,70)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438939"
     Region          72..>124
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     CDS             1..224
                     /gene="FBXO44"
                     /gene_synonym="FBG3; FBX30; Fbx44; FBX6A; Fbxo6a"
                     /coded_by="NM_183412.3:206..880"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS131.1"
                     /db_xref="GeneID:93611"
                     /db_xref="HGNC:HGNC:24847"
                     /db_xref="MIM:609111"
ORIGIN      
        1 mavgninelp enillelfth vparqlllnc rlvcslwrdl idlvtlwkrk clregfited
       61 wdqpvadwki fyflrslhrn llhnpcaeeg fefwsldvng gdewkvedls rdqrkefpnd
      121 qvrsqarlrv qvpavrsapv vrarasgdlp arpgdhpaee rcqvegglph ilqlparrpl
      181 hlvsarrrgh sllgrlvrpe ghqqqhhhra paaltppepp saep
//
LOCUS       NP_001316525             520 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 10 isoform 2 [Homo sapiens].
ACCESSION   NP_001316525
VERSION     NP_001316525.1
DBSOURCE    REFSEQ: accession NM_001329596.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Qiu,Q.M., Liu,G., Li,W.N., Shi,Q.W., Zhu,F.X. and Lu,G.X.
  TITLE     [Mutation of KLHL-10 in idiopathic infertile males with
            azoospermia, oligospermia or asthenospermia]
  JOURNAL   Zhonghua Nan Ke Xue 15 (11), 974-979 (2009)
   PUBMED   20218307
  REMARK    GeneRIF: The KLHL-10 gene is not a major contributor to
            azoospermia, oligospermia or asthenospermia in Chinese population.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Yatsenko,A.N., Roy,A., Chen,R., Ma,L., Murthy,L.J., Yan,W.,
            Lamb,D.J. and Matzuk,M.M.
  TITLE     Non-invasive genetic diagnosis of male infertility using
            spermatozoal RNA: KLHL10 mutations in oligozoospermic patients
            impair homodimerization
  JOURNAL   Hum Mol Genet 15 (23), 3411-3419 (2006)
   PUBMED   17047026
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Yan,W., Ma,L., Burns,K.H. and Matzuk,M.M.
  TITLE     Haploinsufficiency of kelch-like protein homolog 10 causes
            infertility in male mice
  JOURNAL   Proc Natl Acad Sci U S A 101 (20), 7793-7798 (2004)
   PUBMED   15136734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB021233.1, AK301797.1,
            AY495339.1 and AC125257.4.
            
            Summary: The protein encoded by this gene belongs to the kelch
            repeat-containing family, and contains an N-terminal BTB/POZ domain
            a BACK domain and six C-terminal kelch repeats. Kelch domains are
            thought to form a four stranded beta-sheet blade structure that can
            fold into a beta-propeller domain when multiple kelch repeats are
            found together. Mutations in this gene have been associated with
            oligozoospermia in some infertile males. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and uses
            an alternate splice site in its 5' terminal exon compared to
            variant 1. This variant represents translation initiation at a
            downstream start codon compared to variant 1; the 5'-most
            initiation codon, as used in variant 1, is associated with a
            truncated ORF that would render the transcript a candidate for
            nonsense-mediated decay (NMD). Leaky scanning may allow translation
            initiation at the downstream start codon to encode an isoform (2)
            that has a shorter N-terminus, compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301797.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..520
                     /product="kelch-like protein 10 isoform 2"
                     /note="kelch-like protein 10; testicular tissue protein Li
                     104"
                     /calculated_mol_wt=58833
     Region          5..484
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          241..284
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          288..332
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          335..378
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          382..425
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          429..472
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..520
                     /gene="KLHL10"
                     /gene_synonym="SPGF11"
                     /coded_by="NM_001329596.2:311..1873"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:317719"
                     /db_xref="HGNC:HGNC:18829"
                     /db_xref="MIM:608778"
ORIGIN      
        1 mmkliieyay trtvpitpdn vekllaaadq fnimgivrgc ceflkselcl dncigickft
       61 dyyycpelrq kaymfilhnf eemvkvsaef lelsvtelkd iiekdelnvk qedavfeail
      121 kwishdpqnr kqhisillpk vrlalmhaey fmnnvkmndy vkdseeckpv iinalkamyd
      181 lnmngpsnsd ftnpltrprl pyailfaigg wsggsptnai eaydaradrw vnvtceeesp
      241 rayhgaaylk gyvyiiggfd svdyfnsvkr fdpvkktwhq vapmhsrrcy vsvtvlgnfi
      301 yamggfdgyv rlntaeryep etnqwtliap mheqrsdasa ttlygkvyic ggfngneclf
      361 taevyntesn qwtviapmrs rrsgigviay gehvyavggf dganrlrsae ayspvantwr
      421 tiptmfnprs nfgievvddl lfvvggfngf tttfnvecyd ektdewydah dmsiyrsals
      481 ccvvpglanv eeyaarrdnf pglalrdevk ysaststlpv
//
LOCUS       NP_066568                729 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 15 member 2 isoform a [Homo sapiens].
ACCESSION   NP_066568
VERSION     NP_066568.3
DBSOURCE    REFSEQ: accession NM_021082.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 729)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 729)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 729)
  AUTHORS   Kudo,M., Kobayashi-Nakamura,K., Kitajima,N. and Tsuji-Naito,K.
  TITLE     Alternate expression of PEPT1 and PEPT2 in epidermal
            differentiation is required for NOD2 immune responses by
            bacteria-derived muramyl dipeptide
  JOURNAL   Biochem Biophys Res Commun 522 (1), 151-156 (2020)
   PUBMED   31757425
  REMARK    GeneRIF: Alternate expression of PEPT1 and PEPT2 in epidermal
            differentiation is required for NOD2 immune responses by
            bacteria-derived muramyl dipeptide.
REFERENCE   4  (residues 1 to 729)
  AUTHORS   Oppermann,H., Heinrich,M., Birkemeyer,C., Meixensberger,J. and
            Gaunitz,F.
  TITLE     The proton-coupled oligopeptide transporters PEPT2, PHT1 and PHT2
            mediate the uptake of carnosine in glioblastoma cells
  JOURNAL   Amino Acids 51 (7), 999-1008 (2019)
   PUBMED   31073693
  REMARK    GeneRIF: The transporters PEPT2, PHT1, and PHT2 are responsible for
            the uptake of carnosine into glioblastoma cells and full function
            of all three transporters is required for maximum uptake.
REFERENCE   5  (residues 1 to 729)
  AUTHORS   Sweeney,M.D., Zhao,Z., Montagne,A., Nelson,A.R. and Zlokovic,B.V.
  TITLE     Blood-Brain Barrier: From Physiology to Disease and Back
  JOURNAL   Physiol Rev 99 (1), 21-78 (2019)
   PUBMED   30280653
  REMARK    Review article
REFERENCE   6  (residues 1 to 729)
  AUTHORS   Daniel,H. and Kottra,G.
  TITLE     The proton oligopeptide cotransporter family SLC15 in physiology
            and pharmacology
  JOURNAL   Pflugers Arch 447 (5), 610-618 (2004)
   PUBMED   12905028
  REMARK    Review article
REFERENCE   7  (residues 1 to 729)
  AUTHORS   Groneberg,D.A.
  TITLE     [Expression, localization and functional aspects of the peptide
            transporter PEPT2 in the normal respiratory tract and in cystic
            fibrosis]
  JOURNAL   Pneumologie 57 (2), 104-105 (2003)
   PUBMED   12579467
  REMARK    GeneRIF: expression, localization and functional aspects of this
            protein in the normal respiratory tract and in cystic fibrosis
REFERENCE   8  (residues 1 to 729)
  AUTHORS   Alcorn,J., Lu,X., Moscow,J.A. and McNamara,P.J.
  TITLE     Transporter gene expression in lactating and nonlactating human
            mammary epithelial cells using real-time reverse
            transcription-polymerase chain reaction
  JOURNAL   J Pharmacol Exp Ther 303 (2), 487-496 (2002)
   PUBMED   12388627
REFERENCE   9  (residues 1 to 729)
  AUTHORS   Doring,F., Martini,C., Walter,J. and Daniel,H.
  TITLE     Importance of a small N-terminal region in mammalian peptide
            transporters for substrate affinity and function
  JOURNAL   J Membr Biol 186 (2), 55-62 (2002)
   PUBMED   11944083
  REMARK    GeneRIF: the two identified aminoterminal regions in mammalian
            peptide carriers play an important role in determining the
            substrate affinity and also other characteristic features of the
            two transporter subtypes.
REFERENCE   10 (residues 1 to 729)
  AUTHORS   Liu,W., Liang,R., Ramamoorthy,S., Fei,Y.J., Ganapathy,M.E.,
            Hediger,M.A., Ganapathy,V. and Leibach,F.H.
  TITLE     Molecular cloning of PEPT 2, a new member of the H+/peptide
            cotransporter family, from human kidney
  JOURNAL   Biochim Biophys Acta 1235 (2), 461-466 (1995)
   PUBMED   7756356
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC072031.18.
            
            On Apr 4, 2009 this sequence version replaced NP_066568.2.
            
            Summary: The mammalian kidney expresses a proton-coupled peptide
            transporter that is responsible for the absorption of small
            peptides, as well as beta-lactam antibiotics and other peptide-like
            drugs, from the tubular filtrate. This transporter, SLC15A2,
            belongs to the same gene family as SLC15A1 (MIM 600544), the
            proton-coupled peptide transporter found in the small intestine
            (Liu et al, 1995 [PubMed 7756356]).[supplied by OMIM, Feb 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.250269.1,
                                           SRR1660803.238045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000489711.6/ ENSP00000417085.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..729
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..729
                     /product="solute carrier family 15 member 2 isoform a"
                     /note="kidney H(+)/peptide cotransporter; peptide
                     transporter 2; solute carrier family 15 (H+/peptide
                     transporter), member 2; solute carrier family 15
                     (oligopeptide transporter), member 2"
                     /calculated_mol_wt=81653
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES07; propagated from
                     UniProtKB/Swiss-Prot (Q16348.2)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9ES07; propagated from
                     UniProtKB/Swiss-Prot (Q16348.2)"
     Site            28
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63424; propagated from
                     UniProtKB/Swiss-Prot (Q16348.2)"
     Region          58..696
                     /region_name="2A1704"
                     /note="Peptide:H+ symporter (also transports b-lactam
                     antibiotics, the antitumor agent, bestatin, and various
                     protease inhibitors); TIGR00926"
                     /db_xref="CDD:273343"
     Site            58..78
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            84..104
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            114..134
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            140..160
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            218..238
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            296..316
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            344..364
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            381..401
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Region          402..611
                     /region_name="Extracellular domain (ECD).
                     /evidence=ECO:0000250|UniProtKB:Q63424"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            435
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            472
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            528
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            567
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            587
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00498; propagated
                     from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            612..632
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            644..664
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     Site            675..695
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16348.2)"
     CDS             1..729
                     /gene="SLC15A2"
                     /gene_synonym="PEPT2"
                     /coded_by="NM_021082.4:77..2266"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3007.1"
                     /db_xref="GeneID:6565"
                     /db_xref="HGNC:HGNC:10921"
                     /db_xref="MIM:602339"
ORIGIN      
        1 mnpfqknesk etlfspvsie evpprppspp kkpspticgs nyplsiafiv vnefcerfsy
       61 ygmkavlily flyflhwned tstsiyhafs slcyftpilg aaiadswlgk fktiiylslv
      121 yvlghviksl galpilggqv vhtvlsligl slialgtggi kpcvaafggd qfeekhaeer
      181 tryfsvfyls inagslistf itpmlrgdvq cfgedcyala fgvpgllmvi alvvfamgsk
      241 iynkpppegn ivaqvfkciw faisnrfknr sgdipkrqhw ldwaaekypk qlimdvkalt
      301 rvlflyiplp mfwalldqqg srwtlqairm nrnlgffvlq pdqmqvlnpl lvlifiplfd
      361 fviyrlvskc ginfsslrkm avgmilacla favaaaveik inemapaqpg pqevflqvln
      421 laddevkvtv vgnennslli esiksfqktp hysklhlktk sqdfhfhlky hnlslytehs
      481 vqeknwyslv iredgnsiss mmvkdtesrt tngmttvrfv ntlhkdvnis lstdtslnvg
      541 edygvsayrt vqrgeypavh crtedknfsl nlglldfgaa ylfvitnntn qglqawkied
      601 ipankmsiaw qlpqyalvta gevmfsvtgl efsysqapss mksvlqaawl ltiavgniiv
      661 lvvaqfsglv qwaefilfsc lllviclifs imgyyyvpvk tedmrgpadk hiphiqgnmi
      721 kletkktkl
//
LOCUS       NP_001161401             570 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-1 receptor accessory protein isoform 1 precursor [Homo
            sapiens].
ACCESSION   NP_001161401
VERSION     NP_001161401.1
DBSOURCE    REFSEQ: accession NM_001167929.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 570)
  AUTHORS   Mulholland,M., Depuydt,M.A.C., Jakobsson,G., Ljungcrantz,I.,
            Grentzmann,A., To,F., Bengtsson,E., Jaensson Gyllenback,E.,
            Gronberg,C., Rattik,S., Liberg,D., Schiopu,A., Bjorkbacka,H.,
            Kuiper,J., Bot,I., Slutter,B. and Engelbertsen,D.
  TITLE     Interleukin-1 receptor accessory protein blockade limits the
            development of atherosclerosis and reduces plaque inflammation
  JOURNAL   Cardiovasc Res 120 (6), 581-595 (2024)
   PUBMED   38563353
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein blockade limits
            the development of atherosclerosis and reduces plaque inflammation.
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Zarezadeh Mehrabadi,A., Shahba,F., Khorramdelazad,H.,
            Aghamohammadi,N., Karimi,M., Bagherzadeh,K., Khoshmirsafa,M.,
            Massoumi,R. and Falak,R.
  TITLE     Interleukin-1 receptor accessory protein (IL-1RAP): A magic bullet
            candidate for immunotherapy of human malignancies
  JOURNAL   Crit Rev Oncol Hematol 193, 104200 (2024)
   PUBMED   37981104
  REMARK    GeneRIF: Interleukin-1 receptor accessory protein (IL-1RAP): A
            magic bullet candidate for immunotherapy of human malignancies.
            Review article
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Cao,K., Liu,Z., Liu,J., Hu,Q., Shan,W., Hu,B., Shi,H. and Zhang,B.
  TITLE     Constitutive photomorphogenic protein 1 ubiquitinates interleukin-1
            receptor accessory protein in human liver cancer
  JOURNAL   J Cancer Res Clin Oncol 149 (18), 16247-16260 (2023)
   PUBMED   37700160
  REMARK    GeneRIF: Constitutive photomorphogenic protein 1 ubiquitinates
            interleukin-1 receptor accessory protein in human liver cancer.
REFERENCE   4  (residues 1 to 570)
  AUTHORS   Yu,F., Xing,J., Li,L. and Xiang,M.
  TITLE     CircCRIM1 mediates proliferation, migration, and invasion of
            trophoblast cell through regulating miR-942-5p/IL1RAP axis
  JOURNAL   Am J Reprod Immunol 90 (1), e13699 (2023)
   PUBMED   37382169
  REMARK    GeneRIF: CircCRIM1 mediates proliferation, migration, and invasion
            of trophoblast cell through regulating miR-942-5p/IL1RAP axis.
REFERENCE   5  (residues 1 to 570)
  AUTHORS   Agerstam,H., Lilljebjorn,H., Rissler,M., Sanden,C. and Fioretos,T.
  TITLE     IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models
  JOURNAL   Haematologica 108 (2), 599-604 (2023)
   PUBMED   36226493
  REMARK    GeneRIF: IL1RAP is expressed in several subtypes of pediatric acute
            lymphoblastic leukemia and can be used as a target to eliminate
            ETV6::RUNX1-positive leukemia cells in preclinical models.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 570)
  AUTHORS   Huang,J., Gao,X., Li,S. and Cao,Z.
  TITLE     Recruitment of IRAK to the interleukin 1 receptor complex requires
            interleukin 1 receptor accessory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (24), 12829-12832 (1997)
   PUBMED   9371760
REFERENCE   7  (residues 1 to 570)
  AUTHORS   Wesche,H., Korherr,C., Kracht,M., Falk,W., Resch,K. and Martin,M.U.
  TITLE     The interleukin-1 receptor accessory protein (IL-1RAcP) is
            essential for IL-1-induced activation of interleukin-1
            receptor-associated kinase (IRAK) and stress-activated protein
            kinases (SAP kinases)
  JOURNAL   J Biol Chem 272 (12), 7727-7731 (1997)
   PUBMED   9065432
REFERENCE   8  (residues 1 to 570)
  AUTHORS   Cao,Z., Xiong,J., Takeuchi,M., Kurama,T. and Goeddel,D.V.
  TITLE     TRAF6 is a signal transducer for interleukin-1
  JOURNAL   Nature 383 (6599), 443-446 (1996)
   PUBMED   8837778
REFERENCE   9  (residues 1 to 570)
  AUTHORS   Parnet,P., Garka,K.E., Bonnert,T.P., Dower,S.K. and Sims,J.E.
  TITLE     IL-1Rrp is a novel receptor-like molecule similar to the type I
            interleukin-1 receptor and its homologues T1/ST2 and IL-1R AcP
  JOURNAL   J Biol Chem 271 (8), 3967-3970 (1996)
   PUBMED   8626725
REFERENCE   10 (residues 1 to 570)
  AUTHORS   Greenfeder,S.A., Nunes,P., Kwee,L., Labow,M., Chizzonite,R.A. and
            Ju,G.
  TITLE     Molecular cloning and characterization of a second subunit of the
            interleukin 1 receptor complex
  JOURNAL   J Biol Chem 270 (23), 13757-13765 (1995)
   PUBMED   7775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA024801.1, AF538733.1,
            BM194193.1 and BM973472.1.
            
            Summary: This gene encodes a component of the interleukin 1
            receptor complex, which initiates signalling events that result in
            the activation of interleukin 1-responsive genes. Alternative
            splicing of this gene results in membrane-bound and soluble
            isoforms differing in their C-terminus. The ratio of soluble to
            membrane-bound forms increases during acute-phase induction or
            stress. [provided by RefSeq, Jul 2018].
            
            Transcript Variant: This variant (4) differs in the 5' UTR,
            compared to variant 1. It encodes the membrane-bound isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.241098.1,
                                           SRR1803611.37684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q28"
     Protein         1..570
                     /product="interleukin-1 receptor accessory protein isoform
                     1 precursor"
                     /EC_number="3.2.2.6"
                     /note="interleukin-1 receptor accessory protein beta;
                     interleukin-1 receptor 3; IL-1 receptor accessory protein"
                     /calculated_mol_wt=63114
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2323
     mat_peptide     21..570
                     /product="Interleukin-1 receptor accessory protein.
                     /id=PRO_0000015450"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
                     /calculated_mol_wt=63114
     Region          25..132
                     /region_name="Ig1_IL1R_like"
                     /note="First immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20992"
                     /db_xref="CDD:409584"
     Region          26..29
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409584"
     Site            order(27,29..36)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409584"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409584"
     Region          42..47
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409584"
     Site            57
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          67..71
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409584"
     Region          69..85
                     /region_name="Essential for interaction with PTPRD.
                     /evidence=ECO:0000250|UniProtKB:Q61730"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          80..82
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409584"
     Region          91..95
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409584"
     Region          97..101
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409584"
     Site            107
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          110..118
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409584"
     Site            111
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          121..132
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409584"
     Region          143..235
                     /region_name="Ig2_IL-1RAP_like"
                     /note="Second immunoglobulin (Ig)-like domain of
                     interleukin-1 receptor (IL1R), and similar domains;
                     cd20993"
                     /db_xref="CDD:409585"
     Site            order(143..145,147..150,157,162,164,196,234)
                     /site_type="other"
                     /note="antagonist binding site [polypeptide binding]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          145..150
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          174..179
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          182..184
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          189..193
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Region          195..200
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409585"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Region          209..218
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409585"
     Site            209
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:20802483; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          221..234
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409585"
     Region          243..349
                     /region_name="Ig3_IL1RAP"
                     /note="Third immunoglobulin domain of interleukin-1
                     receptor accessory protein (IL1RAP); cd20931"
                     /db_xref="CDD:409525"
     Region          243..246
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409525"
     Region          254..258
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409525"
     Region          260..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409525"
     Region          278..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409525"
     Region          286..288
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409525"
     Region          296..304
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409525"
     Site            299
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          310..318
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409525"
     Region          329..335
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409525"
     Region          339..345
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409525"
     Site            368..388
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Region          405..552
                     /region_name="TIR"
                     /note="TIR domain; pfam01582"
                     /db_xref="CDD:396246"
     Region          549..570
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NPH3.2)"
     Site            557
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NPH3.2)"
     CDS             1..570
                     /gene="IL1RAP"
                     /gene_synonym="C3orf13; IL-1RAcP; IL1R3"
                     /coded_by="NM_001167929.2:137..1849"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS3298.1"
                     /db_xref="GeneID:3556"
                     /db_xref="HGNC:HGNC:5995"
                     /db_xref="MIM:602626"
ORIGIN      
        1 mtllwcvvsl yfygilqsda sercddwgld tmrqiqvfed eparikcplf ehflkfnyst
       61 ahsagltliw ywtrqdrdle epinfrlpen riskekdvlw frptllndtg nytcmlrntt
      121 ycskvafple vvqkdscfns pmklpvhkly ieygiqritc pnvdgyfpss vkptitwymg
      181 cykiqnfnnv ipegmnlsfl ialisnngny tcvvtypeng rtfhltrtlt vkvvgspkna
      241 vppvihspnd hvvyekepge ellipctvyf sflmdsrnev wwtidgkkpd ditidvtine
      301 sishsrtede trtqilsikk vtsedlkrsy vcharsakge vakaakvkqk vpaprytvel
      361 acgfgatvll vvilivvyhv ywlemvlfyr ahfgtdetil dgkeydiyvs yarnaeeeef
      421 vlltlrgvle nefgyklcif drdslpggiv tdetlsfiqk srrllvvlsp nyvlqgtqal
      481 lelkaglenm asrgninvil vqykavketk vkelkraktv ltvikwkgek skypqgrfwk
      541 qlqvampvkk sprrsssdeq glsysslknv
//
LOCUS       NP_001528                 76 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock factor-binding protein 1 [Homo sapiens].
ACCESSION   NP_001528
VERSION     NP_001528.1
DBSOURCE    REFSEQ: accession NM_001537.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 76)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 76)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 76)
  AUTHORS   Zhong,Y., Cao,L., Ma,H., Wang,Q., Wei,P., Yang,J., Mo,Y., Cao,L.,
            Shuai,C. and Peng,S.
  TITLE     Lin28A Regulates Stem-like Properties of Ovarian Cancer Cells by
            Enriching RAN and HSBP1 mRNA and Up-regulating its Protein
            Expression
  JOURNAL   Int J Biol Sci 16 (11), 1941-1953 (2020)
   PUBMED   32398961
  REMARK    GeneRIF: Lin28A Regulates Stem-like Properties of Ovarian Cancer
            Cells by Enriching RAN and HSBP1 mRNA and Up-regulating its Protein
            Expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 76)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 76)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 76)
  AUTHORS   Yashin,D.V., Dukhanina,E.A., Kabanova,O.D., Romanova,E.A.,
            Lukyanova,T.I., Tonevitskii,A.G., Raynes,D.A., Gnuchev,N.V.,
            Guerriero,V., Georgiev,G.P. and Sashchenko,L.P.
  TITLE     The heat shock-binding protein (HspBP1) protects cells against the
            cytotoxic action of the Tag7-Hsp70 complex
  JOURNAL   J Biol Chem 286 (12), 10258-10264 (2011)
   PUBMED   21247889
  REMARK    GeneRIF: HspBP1 inhibited the cytotoxic activity of the Tag7-Hsp70
            complex secreted by lymphocytes. HspBP1
REFERENCE   7  (residues 1 to 76)
  AUTHORS   Liu,X., Xu,L., Liu,Y., Tong,X., Zhu,G., Zhang,X.C., Li,X. and
            Rao,Z.
  TITLE     Crystal structure of the hexamer of human heat shock factor binding
            protein 1
  JOURNAL   Proteins 75 (1), 1-11 (2009)
   PUBMED   18767159
  REMARK    GeneRIF: This study reports the crystal structure of a
            degradation-resistant fragment of HSBP1. A continuous, long-helix
            conformation of HSBP1 assembles into a coiled-coil three-helix
            bundle and subsequently into an elongated, symmetrical hexamer.
REFERENCE   8  (residues 1 to 76)
  AUTHORS   Tai,L.J., McFall,S.M., Huang,K., Demeler,B., Fox,S.G., Brubaker,K.,
            Radhakrishnan,I. and Morimoto,R.I.
  TITLE     Structure-function analysis of the heat shock factor-binding
            protein reveals a protein composed solely of a highly conserved and
            dynamic coiled-coil trimerization domain
  JOURNAL   J Biol Chem 277 (1), 735-745 (2002)
   PUBMED   11679589
  REMARK    GeneRIF: HSBP likely mediates its function through its
            trimerization domain.
REFERENCE   9  (residues 1 to 76)
  AUTHORS   Satyal,S.H., Chen,D., Fox,S.G., Kramer,J.M. and Morimoto,R.I.
  TITLE     Negative regulation of the heat shock transcriptional response by
            HSBP1
  JOURNAL   Genes Dev 12 (13), 1962-1974 (1998)
   PUBMED   9649501
REFERENCE   10 (residues 1 to 76)
  AUTHORS   Morimoto,R.I., Kline,M.P., Bimston,D.N. and Cotto,J.J.
  TITLE     The heat-shock response: regulation and function of heat-shock
            proteins and molecular chaperones
  JOURNAL   Essays Biochem 32, 17-29 (1997)
   PUBMED   9493008
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009119.10, BC007515.2,
            AK172732.1 and DB519225.1.
            
            Summary: The heat-shock response is elicited by exposure of cells
            to thermal and chemical stress and through the activation of HSFs
            (heat shock factors) results in the elevated expression of
            heat-shock induced genes.  Heat shock factor binding protein 1
            (HSBP1), is a 76-amino-acid protein that binds to heat shock factor
            1(HSF1), which is a transcription factor involved in the HS
            response.  During HS response, HSF1 undergoes conformational
            transition from an inert non-DNA-binding monomer to active
            functional trimers. HSBP1 is nuclear-localized and interacts  with
            the active trimeric state of HSF1 to negatively regulate HSF1
            DNA-binding activity. Overexpression of HSBP1 in mammalian cells
            represses the transactivation activity of HSF1. When overexpressed
            in C.elegans HSBP1 has severe effects on survival of the animals
            after thermal and chemical stress consistent with a role of HSBP1
            as a negative regulator of heat shock response. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.38835.1,
                                           SRR1803613.41892.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000433866.7/ ENSP00000392896.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..76
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q23.3"
     Protein         1..76
                     /product="heat shock factor-binding protein 1"
                     /note="nasopharyngeal carcinoma-associated antigen 13"
                     /calculated_mol_wt=8412
     Region          10..60
                     /region_name="HSBP1"
                     /note="Heat shock factor binding protein 1; pfam06825"
                     /db_xref="CDD:429139"
     CDS             1..76
                     /gene="HSBP1"
                     /gene_synonym="NPC-A-13"
                     /coded_by="NM_001537.4:100..330"
                     /db_xref="CCDS:CCDS45534.1"
                     /db_xref="GeneID:3281"
                     /db_xref="HGNC:HGNC:5203"
                     /db_xref="MIM:604553"
ORIGIN      
        1 maetdpktvq dltsvvqtll qqmqdkfqtm sdqiigridd mssriddlek niadlmtqag
       61 veelesenki patqks
//
LOCUS       NP_001353141             871 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 8 [Homo sapiens].
ACCESSION   NP_001353141 XP_016861305
VERSION     NP_001353141.1
DBSOURCE    REFSEQ: accession NM_001366212.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 871)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 871)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 871)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 871)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 871)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 871)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 871)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 871)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 871)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 871)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861305.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.22313.1,
                                           SRR11853565.21617.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..871
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..871
                     /product="disks large homolog 1 isoform 8"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=96945
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          680..858
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..871
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366212.1:624..3239"
                     /note="isoform 8 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS93452.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgeipdd mgskglkhvt snasdsessy
      661 rgqeeyvlsy epvnqqevny trpviilgpm kdrinddlis efpdkfgscv phttrpkrdy
      721 evdgrdyhfv tsreqmekdi qehkfieagq ynnhlygtsv qsvrevaekg khcildvsgn
      781 aikrlqiaql ypisifikpk smenimemnk rlteeqarkt feramkleqe ftehftaivq
      841 gdtlediynq vkqiieeqsg syiwvpakek l
//
LOCUS       NP_060817                200 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-5 complex subunit sigma-1 [Homo sapiens].
ACCESSION   NP_060817
VERSION     NP_060817.1
DBSOURCE    REFSEQ: accession NM_018347.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Mai,X., Wang,Y., Wang,X., Liu,M., Teng,F., Liu,Z., Su,M.Y. and
            Stjepanovic,G.
  TITLE     Structural basis for membrane remodeling by the AP5-SPG11-SPG15
            complex
  JOURNAL   Nat Struct Mol Biol 32 (8), 1334-1346 (2025)
   PUBMED   40175557
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Hirst,J., Barlow,L.D., Francisco,G.C., Sahlender,D.A., Seaman,M.N.,
            Dacks,J.B. and Robinson,M.S.
  TITLE     The fifth adaptor protein complex
  JOURNAL   PLoS Biol 9 (10), e1001170 (2011)
   PUBMED   22022230
  REMARK    Erratum:[PLoS Biol. 2012 Mar;10(3). doi:
            10.1371/annotation/89dff893-c156-44bb-a731-bfcc91843583]
REFERENCE   3  (residues 1 to 200)
  AUTHORS   Slabicki,M., Theis,M., Krastev,D.B., Samsonov,S., Mundwiller,E.,
            Junqueira,M., Paszkowski-Rogacz,M., Teyra,J., Heninger,A.K.,
            Poser,I., Prieur,F., Truchetto,J., Confavreux,C., Marelli,C.,
            Durr,A., Camdessanche,J.P., Brice,A., Shevchenko,A.,
            Pisabarro,M.T., Stevanin,G. and Buchholz,F.
  TITLE     A genome-scale DNA repair RNAi screen identifies SPG48 as a novel
            gene associated with hereditary spastic paraplegia
  JOURNAL   PLoS Biol 8 (6), e1000408 (2010)
   PUBMED   20613862
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 200)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA253969.1, BC043344.1, AK002030.1 and AL109804.41.
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 3 encode the same
            protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.400910.1, AK002030.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000615891.2/ ENSP00000481750.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..200
                     /product="AP-5 complex subunit sigma-1"
                     /note="protein C20orf29; sigma5; adapter-related protein
                     complex 5 sigma subunit; adaptor-related protein complex 5
                     sigma subunit; adaptor related protein complex 5 sigma 1
                     subunit"
                     /calculated_mol_wt=22391
     Region          1..195
                     /region_name="AP-5_subunit_s1"
                     /note="AP-5 complex subunit sigma-1; pfam15001"
                     /db_xref="CDD:434380"
     CDS             1..200
                     /gene="AP5S1"
                     /gene_synonym="C20orf29"
                     /coded_by="NM_018347.3:229..831"
                     /db_xref="CCDS:CCDS13070.1"
                     /db_xref="GeneID:55317"
                     /db_xref="HGNC:HGNC:15875"
                     /db_xref="MIM:614824"
ORIGIN      
        1 mvhaflihtl rapntedtgl crvlyscvfg aekspddprp hgaerdrllr keqilavarq
       61 vesmcrlqqq asgrppmdlq pqssdeqvpl heaprgafrl aaenpfqepr tvvwlgvlsl
      121 gfalvldahe nlllaegtlr lltrllldhl rllapstsll lradriegil trflphgqll
      181 flndqfvqgl ekefsaawpr
//
LOCUS       NP_000983                159 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL29 [Homo sapiens].
ACCESSION   NP_000983
VERSION     NP_000983.1
DBSOURCE    REFSEQ: accession NM_000992.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Babaylova,E.S., Kolobova,A.V., Gopanenko,A.V., Tupikin,A.E.,
            Kabilov,M.R., Malygin,A.A. and Karpova,G.G.
  TITLE     The human ribosomal protein eL29 binds in vivo to the cognate mRNA
            by interacting with its coding sequence, as revealed from in-cell
            cross-linking data
  JOURNAL   Biochimie 177, 68-77 (2020)
   PUBMED   32798643
  REMARK    GeneRIF: The human ribosomal protein eL29 binds in vivo to the
            cognate mRNA by interacting with its coding sequence, as revealed
            from in-cell cross-linking data.
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Li,J. and Peng,Y.
  TITLE     Knockdown RPL29 Gene Can Inhibit the Proliferation, Invasion of
            Squamous Cell Carcinomas
  JOURNAL   Ann Clin Lab Sci 49 (6), 763-769 (2019)
   PUBMED   31882427
  REMARK    GeneRIF: RPL29 is upregulated in the gingival squamous cell
            carcinoma.RPL29 role in the cell proliferation of the gingival
            squamous cell carcinoma.
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Rohde,L.H., Julian,J., Babaknia,A. and Carson,D.D.
  TITLE     Cell surface expression of HIP, a novel heparin/heparan sulfate
            binding protein, of human uterine epithelial cells and cell lines
  JOURNAL   J Biol Chem 271 (20), 11824-11830 (1996)
   PUBMED   8662617
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Liu,S., Smith,S.E., Julian,J., Rohde,L.H., Karin,N.J. and
            Carson,D.D.
  TITLE     cDNA cloning and expression of HIP, a novel cell surface heparan
            sulfate/heparin-binding protein of human uterine epithelial cells
            and cell lines
  JOURNAL   J Biol Chem 271 (20), 11817-11823 (1996)
   PUBMED   8662616
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Law,P.T., Tsui,S.K., Lam,W.Y., Luk,S.C., Hwang,D.M., Liew,C.C.,
            Lee,C.Y., Fung,K.P. and Waye,M.M.
  TITLE     A novel cDNA encoding a human homologue of ribosomal protein L29
  JOURNAL   Biochim Biophys Acta 1305 (3), 105-108 (1996)
   PUBMED   8597591
REFERENCE   9  (residues 1 to 159)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   10 (residues 1 to 159)
  AUTHORS   Nika,H. and Hultin,T.
  TITLE     Location of the sulfhydryl groups involved in disulfide interaction
            between the neighboring proteins L6 and L29 in mammalian ribosomes.
            S-cleavage of the cyanylated proteins in polyacrylamide gels after
            separation by dodecylsulfate gel electrophoresis
  JOURNAL   Eur J Biochem 142 (3), 521-526 (1984)
   PUBMED   6468376
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from BC008926.2 and AC115284.4.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a cytoplasmic
            ribosomal protein that is a component of the 60S subunit. The
            protein belongs to the L29E family of ribosomal proteins. The
            protein is also a peripheral membrane protein expressed on the cell
            surface that directly binds heparin. Although this gene was
            previously reported to map to 3q29-qter, it is believed that it is
            located at 3p21.3-p21.2. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD249111.1, CD247488.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294189.11/ ENSP00000294189.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.2"
     Protein         1..159
                     /product="large ribosomal subunit protein eL29"
                     /note="heparin/heparan sulfate-interacting protein;
                     HP/HS-interacting protein; heparin/heparan sulfate-binding
                     protein; cell surface heparin-binding protein HIP; 60S
                     ribosomal protein L29; ribosomal protein YL43 homologue"
                     /calculated_mol_wt=17621
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47914.2)"
     Region          4..42
                     /region_name="Ribosomal_L29e"
                     /note="Ribosomal L29e protein family; pfam01779"
                     /db_xref="CDD:460324"
     Site            5
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0000269|PubMed:12962325,
                     ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P47914.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P47914.2)"
     Site            33
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P47914.2)"
     Region          117..159
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P47914.2)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P47914.2)"
     CDS             1..159
                     /gene="RPL29"
                     /gene_synonym="eL29; HIP; HUMRPL29; L29; RPL29P10;
                     RPL29_3_370"
                     /coded_by="NM_000992.3:48..527"
                     /db_xref="CCDS:CCDS2845.1"
                     /db_xref="GeneID:6159"
                     /db_xref="HGNC:HGNC:10331"
                     /db_xref="MIM:601832"
ORIGIN      
        1 maksknhtth nqsrkwhrng ikkprsqrye slkgvdpkfl rnmrfakkhn kkglkkmqan
       61 nakamsarae aikalvkpke vkpkipkgvs rkldrlayia hpklgkrara riakglrlcr
      121 pkakakakak dqtkaqaaap asvpaqapkr tqaptkase
//
LOCUS       NP_001186779             364 aa            linear   PRI 20-NOV-2025
DEFINITION  small ribosomal subunit protein mS29 isoform 2 [Homo sapiens].
ACCESSION   NP_001186779
VERSION     NP_001186779.1
DBSOURCE    REFSEQ: accession NM_001199850.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Smith,T.B., Kopajtich,R., Demain,L.A.M., Rea,A., Thomas,H.B.,
            Schiff,M., Beetz,C., Joss,S., Conway,G.S., Shukla,A., Yeole,M.,
            Radhakrishnan,P., Azzouz,H., Ben Chehida,A., Elmaleh-Berges,M.,
            Glasgow,R.I.C., Thompson,K., Olahova,M., He,L., Jenkinson,E.M.,
            Jahic,A., Belyantseva,I.A., Barzik,M., Urquhart,J.E.,
            O'Sullivan,J., Williams,S.G., Bhaskar,S.S., Carrera,S.,
            Blakes,A.J.M., Banka,S., Yue,W.W., Ellingford,J.M., Houlden,H.,
            Munro,K.J., Friedman,T.B., Taylor,R.W., Prokisch,H., O'Keefe,R.T.
            and Newman,W.G.
  CONSRTM   DDD Study
  TITLE     Bi-allelic variants in DAP3 result in reduced assembly of the
            mitoribosomal small subunit with altered apoptosis and a
            Perrault-syndrome-spectrum phenotype
  JOURNAL   Am J Hum Genet 112 (1), 59-74 (2025)
   PUBMED   39701103
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Tan,S., Zhang,X., Guo,X., Pan,G., Yan,L., Ding,Z., Li,R., Wang,D.,
            Yan,Y., Dong,Z. and Li,T.
  TITLE     DAP3 promotes mitochondrial activity and tumour progression in
            hepatocellular carcinoma by regulating MT-ND5 expression
  JOURNAL   Cell Death Dis 15 (7), 540 (2024)
   PUBMED   39080251
  REMARK    GeneRIF: DAP3 promotes mitochondrial activity and tumour
            progression in hepatocellular carcinoma by regulating MT-ND5
            expression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Sui,L., Zeng,J., Zhao,H., Ye,L., Martin,T.A., Sanders,A.J.,
            Ruge,F., Jiang,A., Dou,Q.P., Hargest,R., Song,X. and Jiang,W.G.
  TITLE     Death associated protein-3 (DAP3) and DAP3 binding cell death
            enhancer-1 (DELE1) in human colorectal cancer, and their impacts on
            clinical outcome and chemoresistance
  JOURNAL   Int J Oncol 62 (1) (2023)
   PUBMED   36382667
  REMARK    GeneRIF: Death associated protein3 (DAP3) and DAP3 binding cell
            death enhancer1 (DELE1) in human colorectal cancer, and their
            impacts on clinical outcome and chemoresistance.
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Han,M.J., Chiu,D.T. and Koc,E.C.
  TITLE     Regulation of mitochondrial ribosomal protein S29 (MRPS29)
            expression by a 5'-upstream open reading frame
  JOURNAL   Mitochondrion 10 (3), 274-283 (2010)
   PUBMED   20079882
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Morgan,C.J., Jacques,C., Savagner,F., Tourmen,Y., Mirebeau,D.P.,
            Malthiery,Y. and Reynier,P.
  TITLE     A conserved N-terminal sequence targets human DAP3 to mitochondria
  JOURNAL   Biochem Biophys Res Commun 280 (1), 177-181 (2001)
   PUBMED   11162496
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Hulkko,S.M., Wakui,H. and Zilliacus,J.
  TITLE     The pro-apoptotic protein death-associated protein 3 (DAP3)
            interacts with the glucocorticoid receptor and affects the receptor
            function
  JOURNAL   Biochem J 349 Pt 3 (Pt 3), 885-893 (2000)
   PUBMED   10903152
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Kissil,J.L. and Kimchi,A.
  TITLE     Assignment of death associated protein 3 (DAP3) to human chromosome
            1q21 by in situ hybridization
  JOURNAL   Cytogenet Cell Genet 77 (3-4), 252 (1997)
   PUBMED   9284927
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Kissil,J.L., Deiss,L.P., Bayewitch,M., Raveh,T., Khaspekov,G. and
            Kimchi,A.
  TITLE     Isolation of DAP3, a novel mediator of interferon-gamma-induced
            cell death
  JOURNAL   J Biol Chem 270 (46), 27932-27936 (1995)
   PUBMED   7499268
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK302281.1, AK298201.1,
            AL162734.15 and BQ183744.1.
            
            Summary: Mammalian mitochondrial ribosomal proteins are encoded by
            nuclear genes and help in protein synthesis within the
            mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a
            small 28S subunit and a large 39S subunit. They have an estimated
            75% protein to rRNA composition compared to prokaryotic ribosomes,
            where this ratio is reversed. Another difference between mammalian
            mitoribosomes and prokaryotic ribosomes is that the latter contain
            a 5S rRNA. Among different species, the proteins comprising the
            mitoribosome differ greatly in sequence, and sometimes in
            biochemical properties, which prevents easy recognition by sequence
            homology. This gene encodes a 28S subunit protein that also
            participates in apoptotic pathways which are initiated by tumor
            necrosis factor-alpha, Fas ligand, and gamma interferon. This
            protein potentially binds ATP/GTP and might be a functional partner
            of the mitoribosomal protein S27. Multiple alternatively spliced
            transcript variants encoding distinct isoforms have been found for
            this gene. Pseudogenes corresponding to this gene are found on
            chromosomes 1q and 2q. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (4) lacks an in-frame exon in the
            CDS, as compared to variant 2. The resulting isoform (2) lacks an
            internal segment, as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302281.1, SRR1803611.230837.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..364
                     /product="small ribosomal subunit protein mS29 isoform 2"
                     /note="mitochondrial 28S ribosomal protein S29; 28S
                     ribosomal protein S29, mitochondrial; ionizing radiation
                     resistance conferring protein; mitochondrial small
                     ribosomal subunit protein mS29"
                     /calculated_mol_wt=41542
     Region          65..359
                     /region_name="DAP3"
                     /note="Mitochondrial ribosomal death-associated protein 3;
                     pfam10236"
                     /db_xref="CDD:431160"
     CDS             1..364
                     /gene="DAP3"
                     /gene_synonym="bMRP-10; DAP-3; MRP-S29; MRPS29; mS29;
                     PRLTS7; S29mt"
                     /coded_by="NM_001199850.1:92..1186"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55646.1"
                     /db_xref="GeneID:7818"
                     /db_xref="HGNC:HGNC:2673"
                     /db_xref="MIM:602074"
ORIGIN      
        1 mmlkgitrli srihkldpgr flhmgtqarq siaahldnqv pvespraisr tnendpvktf
       61 seaclmvrkp alellhylkn tsfaypairy llygekgtgk tlslchvihf cakqdwlilh
      121 ipdahlwvkn crdllqssyn kqrfdqplea stwlknfktt nerflnqikv qekyvwnkre
      181 stekgsplge vveqgitrvr natdavgivl kelkrqsslg mfhllvavdg inalwgrttl
      241 kredkspiap eelalvhnlr kmmkndwhgg aivsalsqtg slfkprkayl pqellgkegf
      301 daldpfipil vsnynpkefe sciqyylenn wlqhekapte egkkellfls nanpsllerh
      361 cayl
//
LOCUS       NP_001353515             791 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 19 [Homo
            sapiens].
ACCESSION   NP_001353515 XP_016855522
VERSION     NP_001353515.1
DBSOURCE    REFSEQ: accession NM_001366586.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 791)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 791)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 791)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 791)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 791)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 791)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 791)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 791)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 791)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 791)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855522.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.15411.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..791
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..791
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 19"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=88809
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <38..126
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <493..>627
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..791
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366586.1:2055..4430"
                     /note="isoform 19 is encoded by transcript variant 24"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rtksrspspa pekkektpel pepsvkvkep
      121 svqeatstsd ilkvpkpepi pepkepspek nskkekekek trprsrsrsk srsrtrsrsp
      181 shtrprrrhr srsrsysprr rpsprrrpsp rrrtpprrmp ppprhrrsrs pvrrrrrssa
      241 slsgssssss ssrsrsppkk ppkrtssppr ktrrlspsas pprrrhrpsp patpppktrh
      301 sptpqqsnrt rksrvsvspg rtsgkvtkhk gtekrespsp apkprkvels eseedkggkm
      361 aaadsvqqrr qyrrqnqqss sdsgssssse derpkrshvk ngevgrrrrh spsrsaspsp
      421 rkrqketspr grrrrspspp ptrrrrspsp appprrrrtp tppprrrtps ppprrrspsp
      481 rrysppiqrr yspspppkrr taspppppkr raspspppkr rvshspppkq rsspvtkrrs
      541 pslsskhrkg sspsrstrea rspqpnkrhs psprprapqt ssspppvrrg assspqrrqs
      601 pspstrpirr vsrtpepkki kkaaspspqs vrrvsssrsv sgspepaakk ppappspvqs
      661 qspstnwspa vpvkkakspt pspspprnsd qegggkkkkk kkdkkhkkdk khkkhkkhkk
      721 ekavaaaaaa avtpaaiaaa tttlaqeepv aapepkkete seaednlddl ekhlrekalr
      781 smrkaqvspq s
//
LOCUS       NP_001229306             385 aa            linear   PRI 20-NOV-2025
DEFINITION  m7GpppN-mRNA hydrolase isoform 2 [Homo sapiens].
ACCESSION   NP_001229306
VERSION     NP_001229306.1
DBSOURCE    REFSEQ: accession NM_001242377.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 385)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 385)
  AUTHORS   Mei,Y., Lv,Q., Tan,Z., Zhang,Z., Ji,Y., Chen,S. and Shen,X.
  TITLE     Decapping enzyme 2 is a novel immune-related biomarker that
            predicts poor prognosis in glioma
  JOURNAL   Biotechnol Genet Eng Rev 40 (4), 4262-4283 (2024)
   PUBMED   37191010
  REMARK    GeneRIF: Decapping enzyme 2 is a novel immune-related biomarker
            that predicts poor prognosis in glioma.
REFERENCE   3  (residues 1 to 385)
  AUTHORS   Liu,Q., Yi,D., Ding,J., Mao,Y., Wang,S., Ma,L., Li,Q., Wang,J.,
            Zhang,Y., Zhao,J., Guo,S., Liu,Z., Guo,F., Zhao,D., Liang,C.,
            Li,X., Peng,X. and Cen,S.
  TITLE     MOV10 recruits DCP2 to decap human LINE-1 RNA by forming large
            cytoplasmic granules with phase separation properties
  JOURNAL   EMBO Rep 24 (9), e56512 (2023)
   PUBMED   37437058
  REMARK    GeneRIF: MOV10 recruits DCP2 to decap human LINE-1 RNA by forming
            large cytoplasmic granules with phase separation properties.
REFERENCE   4  (residues 1 to 385)
  AUTHORS   Maciej,V.D., Mateva,N., Schwarz,J., Dittmers,T., Mallick,M.,
            Urlaub,H. and Chakrabarti,S.
  TITLE     Intrinsically disordered regions of tristetraprolin and DCP2
            directly interact to mediate decay of ARE-mRNA
  JOURNAL   Nucleic Acids Res 50 (18), 10665-10679 (2022)
   PUBMED   36130271
  REMARK    GeneRIF: Intrinsically disordered regions of tristetraprolin and
            DCP2 directly interact to mediate decay of ARE-mRNA.
REFERENCE   5  (residues 1 to 385)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 385)
  AUTHORS   van Dijk,E., Cougot,N., Meyer,S., Babajko,S., Wahle,E. and
            Seraphin,B.
  TITLE     Human Dcp2: a catalytically active mRNA decapping enzyme located in
            specific cytoplasmic structures
  JOURNAL   EMBO J 21 (24), 6915-6924 (2002)
   PUBMED   12486012
  REMARK    GeneRIF: Human Dcp2 is a catalytically active mRNA decapping enzyme
            that localizes to the cytoplasm
REFERENCE   7  (residues 1 to 385)
  AUTHORS   Ingelfinger,D., Arndt-Jovin,D.J., Luhrmann,R. and Achsel,T.
  TITLE     The human LSm1-7 proteins colocalize with the mRNA-degrading
            enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
  JOURNAL   RNA 8 (12), 1489-1501 (2002)
   PUBMED   12515382
  REMARK    GeneRIF: LSm1-7 proteins colocalize with DCP1,DCP2 and Xrn1 in
            cytoplasmic foci
REFERENCE   8  (residues 1 to 385)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
  REMARK    GeneRIF: These data suggest that a human decapping complex
            containing decapping enzymes hDcp1a and hDcp2 may be recruited to
            mRNAs containing premature termination codons by the hUpf proteins.
REFERENCE   9  (residues 1 to 385)
  AUTHORS   Wang,Z., Jiao,X., Carr-Schmid,A. and Kiledjian,M.
  TITLE     The hDcp2 protein is a mammalian mRNA decapping enzyme
  JOURNAL   Proc Natl Acad Sci U S A 99 (20), 12663-12668 (2002)
   PUBMED   12218187
  REMARK    GeneRIF: an mRNA decapping enzyme demonstrated to contain intrinsic
            decapping activity
REFERENCE   10 (residues 1 to 385)
  AUTHORS   Ueno,K., Kumagai,T., Kijima,T., Kishimoto,T. and Hosoe,S.
  TITLE     Cloning and tissue expression of cDNAs from chromosome 5q21-22
            which is frequently deleted in advanced lung cancer
  JOURNAL   Hum Genet 102 (1), 63-68 (1998)
   PUBMED   9490301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY146650.1, BC064593.1,
            AY135173.1, BC045596.1, DB146225.1, BX648838.1, BX537716.1,
            AL135390.1, AC008536.7, CF994730.1 and AA837315.1.
            
            Summary: The protein encoded by this gene is a key component of an
            mRNA-decapping complex required for degradation of mRNAs, both in
            normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). It
            removes the 7-methyl guanine cap structure from mRNA, prior to its
            degradation from the 5' end. Alternatively spliced transcript
            variants encoding different isoforms have been noted for this
            gene.[provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            compared to variant 1. This results in a shorter isoform (2)
            missing an internal protein segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.270553.1,
                                           SRR1803612.219692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..385
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.2"
     Protein         1..385
                     /product="m7GpppN-mRNA hydrolase isoform 2"
                     /EC_number="3.6.1.62"
                     /note="nudix (nucleoside diphosphate linked moiety X)-type
                     motif 20; mRNA-decapping enzyme 2; hDpc; m7GpppN-mRNA
                     hydrolase; DCP2 decapping enzyme homolog"
                     /calculated_mol_wt=44278
     Region          12..93
                     /region_name="DCP2"
                     /note="Dcp2, box A domain; pfam05026"
                     /db_xref="CDD:428265"
     Region          97..246
                     /region_name="NUDIX_Dcp2p_Nudt20"
                     /note="mRNA decapping enzyme 2; cd03672"
                     /db_xref="CDD:467540"
     CDS             1..385
                     /gene="DCP2"
                     /gene_synonym="NUDT20"
                     /coded_by="NM_001242377.2:137..1294"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56377.1"
                     /db_xref="GeneID:167227"
                     /db_xref="HGNC:HGNC:24452"
                     /db_xref="MIM:609844"
ORIGIN      
        1 metkrveipg svlddlcsrf ilhipseerd nairvcfqie lahwfyldfy mqntpglpqc
       61 girdfakavf shcpfllpqg edvekvldew keykmgvpty gaiildetle nvllvqgyla
      121 ksgwgfpkgk vnkeeaphdc aarevfeetg fdikdyickd dyielrindq larlyiipgi
      181 pkdtkfnpkt rreirniewf sieklpchrn dmtpksklgl apnkffmaip firplrdwls
      241 rrfgdssdsd ngfsstgstp akptveklsr tkfrhsqqlf pdgspgdqwv khrqplqqkp
      301 ynnhsemsdl lkgkkcekkl hprklqdnfe tdavydlpss sedqllehae gqpvacnghc
      361 kfpfssrafl sfkfdhnaim kildl
//
LOCUS       NP_001307948             128 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-ribosomal protein eL40 fusion protein isoform 1 precursor
            [Homo sapiens].
ACCESSION   NP_001307948
VERSION     NP_001307948.1
DBSOURCE    REFSEQ: accession NM_001321019.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 128)
  AUTHORS   Park,J., Wu,J., Szkop,K.J., Jeong,J., Jovanovic,P., Husmann,D.,
            Flores,N.M., Francis,J.W., Chen,Y.C., Benitez,A.M., Zahn,E.,
            Song,S., Ajani,J.A., Wang,L., Singh,K., Larsson,O., Garcia,B.A.,
            Topisirovic,I., Gozani,O. and Mazur,P.K.
  TITLE     SMYD5 methylation of rpL40 links ribosomal output to gastric cancer
  JOURNAL   Nature 632 (8025), 656-663 (2024)
   PUBMED   39048817
  REMARK    GeneRIF: SMYD5 methylation of rpL40 links ribosomal output to
            gastric cancer.
REFERENCE   2  (residues 1 to 128)
  AUTHORS   Tong,L., Zheng,X., Wang,T., Gu,W., Shen,T., Yuan,W., Wang,S.,
            Xing,S., Liu,X., Zhang,C. and Zhang,C.
  TITLE     Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression
  JOURNAL   J Cell Mol Med 28 (6), e18164 (2024)
   PUBMED   38445807
  REMARK    GeneRIF: Inhibition of UBA52 induces autophagy via EMC6 to suppress
            hepatocellular carcinoma tumorigenesis and progression.
REFERENCE   3  (residues 1 to 128)
  AUTHORS   Lee,S.O., Kelliher,J.L., Song,W., Tengler,K., Sarkar,A., Dray,E.
            and Leung,J.W.C.
  TITLE     UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination
            and DNA repair
  JOURNAL   J Biol Chem 299 (8), 105043 (2023)
   PUBMED   37451480
  REMARK    GeneRIF: UBA80 and UBA52 fine-tune RNF168-dependent histone
            ubiquitination and DNA repair.
REFERENCE   4  (residues 1 to 128)
  AUTHORS   Eastham,M.J., Pelava,A., Wells,G.R., Watkins,N.J. and Schneider,C.
  TITLE     RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion Proteins,
            Are Not Essential for p53 Signalling
  JOURNAL   Biomolecules 13 (6), 898 (2023)
   PUBMED   37371478
  REMARK    GeneRIF: RPS27a and RPL40, Which Are Produced as Ubiquitin Fusion
            Proteins, Are Not Essential for p53 Signalling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 128)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   6  (residues 1 to 128)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   7  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin/52-residue ribosomal protein fusion gene
            subfamily (UbA52) is composed primarily of processed pseudogenes
  JOURNAL   Genomics 14 (2), 520-522 (1992)
   PUBMED   1330885
REFERENCE   8  (residues 1 to 128)
  AUTHORS   Baker,R.T. and Board,P.G.
  TITLE     The human ubiquitin-52 amino acid fusion protein gene shares
            several structural features with mammalian ribosomal protein genes
  JOURNAL   Nucleic Acids Res 19 (5), 1035-1040 (1991)
   PUBMED   1850507
REFERENCE   9  (residues 1 to 128)
  AUTHORS   Monia,B.P., Ecker,D.J., Jonnalagadda,S., Marsh,J., Gotlib,L.,
            Butt,T.R. and Crooke,S.T.
  TITLE     Gene synthesis, expression, and processing of human ubiquitin
            carboxyl extension proteins
  JOURNAL   J Biol Chem 264 (7), 4093-4103 (1989)
   PUBMED   2537304
REFERENCE   10 (residues 1 to 128)
  AUTHORS   Salvesen,G., Lloyd,C. and Farley,D.
  TITLE     cDNA encoding a human homolog of yeast ubiquitin 1
  JOURNAL   Nucleic Acids Res 15 (13), 5485 (1987)
   PUBMED   3037496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005253.1, BG035502.1,
            CD385706.1, BQ428515.1, AF545864.1 and BU677484.1.
            
            Summary: Ubiquitin is a highly conserved nuclear and cytoplasmic
            protein that has a major role in targeting cellular proteins for
            degradation by the 26S proteosome. It is also involved in the
            maintenance of chromatin structure, the regulation of gene
            expression, and the stress response. Ubiquitin is synthesized as a
            precursor protein consisting of either polyubiquitin chains or a
            single ubiquitin moiety fused to an unrelated protein. This gene
            encodes a fusion protein consisting of ubiquitin at the N terminus
            and ribosomal protein L40 at the C terminus, a C-terminal extension
            protein (CEP). Multiple processed pseudogenes derived from this
            gene are present in the genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CD385706.1, DRR138524.331983.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..128
                     /product="ubiquitin-ribosomal protein eL40 fusion protein
                     isoform 1 precursor"
                     /note="ubiquitin-52 amino acid fusion protein; ubiquitin
                     carboxyl extension protein 52; ubiquitin-CEP52;
                     ubiquitin-60S ribosomal protein L40; ubiquitin-ribosomal
                     protein eL40 fusion protein"
                     /calculated_mol_wt=14597
     mat_peptide     1..76
                     /product="Ubiquitin. /id=PRO_0000396433"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=8565
     Region          1..76
                     /region_name="Ubl_ubiquitin"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin;
                     cd01803"
                     /db_xref="CDD:340501"
     Site            order(6..9,11,34..37,40,42,44,46..49,68..76)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            order(8..12,31..35,40,42,44,46..49,68,70..76)
                     /site_type="other"
                     /note="E1 interaction site [polypeptide binding]"
                     /db_xref="CDD:340501"
     Site            54
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000269|PubMed:24660806,
                     ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
                     ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291;
                     propagated from UniProtKB/Swiss-Prot (P62987.2)"
     Site            68
                     /site_type="other"
                     /note="Essential for function; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     Site            72
                     /site_type="other"
                     /note="Interacts with activating enzyme; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     mat_peptide     77..128
                     /product="Large ribosomal subunit protein eL40.
                     /id=PRO_0000396434"
                     /note="propagated from UniProtKB/Swiss-Prot (P62987.2)"
                     /calculated_mol_wt=6182
     Region          79..126
                     /region_name="Ribosomal_L40e"
                     /note="Ribosomal L40e family; pfam01020"
                     /db_xref="CDD:395807"
     Site            98
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000269|PubMed:39048817,
                     ECO:0000269|PubMed:39103523; propagated from
                     UniProtKB/Swiss-Prot (P62987.2)"
     CDS             1..128
                     /gene="UBA52"
                     /gene_synonym="CEP52; HUBCEP52; L40; RPL40"
                     /coded_by="NM_001321019.2:298..684"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 5"
                     /db_xref="CCDS:CCDS12382.1"
                     /db_xref="GeneID:7311"
                     /db_xref="HGNC:HGNC:12458"
                     /db_xref="MIM:191321"
ORIGIN      
        1 mqifvktltg ktitleveps dtienvkaki qdkegippdq qrlifagkql edgrtlsdyn
       61 iqkestlhlv lrlrggiiep slrqlaqkyn cdkmicrkcy arlhpravnc rkkkcghtnn
      121 lrpkkkvk
//
LOCUS       NP_001356508             646 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform 28 [Homo sapiens].
ACCESSION   NP_001356508 XP_016881424
VERSION     NP_001356508.1
DBSOURCE    REFSEQ: accession NM_001369579.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881424.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.27446.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..646
                     /product="transcription factor 4 isoform 28"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68896
     Region          537..621
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(545,549,551..553,555,560,581..582)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(558..559,562..563,565..566,569,573,583,586,590,593,
                     596..601)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..646
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369579.1:156..2096"
                     /note="isoform 28 is encoded by transcript variant 39"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsgtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit rsrssnndde dltpeqkaer
      541 ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv
      601 rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_000777                509 aa            linear   PRI 20-NOV-2025
DEFINITION  lanosterol 14-alpha demethylase isoform 1 [Homo sapiens].
ACCESSION   NP_000777
VERSION     NP_000777.1
DBSOURCE    REFSEQ: accession NM_000786.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 509)
  AUTHORS   Kaluzhskiy,L., Yablokov,E., Gnedenko,O., Burkatovskii,D.,
            Maslov,I., Bogorodskiy,A., Ershov,P., Tsybruk,T., Zelepuga,E.,
            Rutckova,T., Kozlovskaya,E., Dmitrenok,P., Gilep,A.,
            Borshchevskiy,V., Strushkevich,N. and Ivanov,A.
  TITLE     The effect of membrane composition on the interaction between human
            CYP51 and its flavonoid inhibitor - luteolin 7,3'-disulfate
  JOURNAL   Biochim Biophys Acta Biomembr 1866 (3), 184286 (2024)
   PUBMED   38272204
  REMARK    GeneRIF: The effect of membrane composition on the interaction
            between human CYP51 and its flavonoid inhibitor - luteolin
            7,3'-disulfate.
REFERENCE   2  (residues 1 to 509)
  AUTHORS   Yin,J., Fu,J., Shao,Y., Xu,J., Li,H., Chen,C., Zhao,Y., Zheng,Z.,
            Yu,C., Zheng,L. and Wang,B.
  TITLE     CYP51-mediated cholesterol biosynthesis is required for the
            proliferation of CD4+ T cells in Sjogren's syndrome
  JOURNAL   Clin Exp Med 23 (5), 1691-1711 (2023)
   PUBMED   36413274
  REMARK    GeneRIF: CYP51-mediated cholesterol biosynthesis is required for
            the proliferation of CD4[+] T cells in Sjogren's syndrome.
REFERENCE   3  (residues 1 to 509)
  AUTHORS   McCarty,K.D., Sullivan,M.E., Tateishi,Y., Hargrove,T.Y.,
            Lepesheva,G.I. and Guengerich,F.P.
  TITLE     Processive kinetics in the three-step lanosterol
            14alpha-demethylation reaction catalyzed by human cytochrome P450
            51A1
  JOURNAL   J Biol Chem 299 (7), 104841 (2023)
   PUBMED   37209823
  REMARK    GeneRIF: Processive kinetics in the three-step lanosterol
            14alpha-demethylation reaction catalyzed by human cytochrome P450
            51A1.
REFERENCE   4  (residues 1 to 509)
  AUTHORS   Jing,Y., Usai,R., Liu,Y. and Kincaid,J.R.
  TITLE     Revealing substrate-induced structural changes in active site of
            human CYP51 in the presence of its physiological substrates
  JOURNAL   J Inorg Biochem 242, 112167 (2023)
   PUBMED   36870163
  REMARK    GeneRIF: Revealing substrate-induced structural changes in active
            site of human CYP51 in the presence of its physiological
            substrates.
REFERENCE   5  (residues 1 to 509)
  AUTHORS   Lamb,D.C., Hargrove,T.Y., Zhao,B., Wawrzak,Z., Goldstone,J.V.,
            Nes,W.D., Kelly,S.L., Waterman,M.R., Stegeman,J.J. and
            Lepesheva,G.I.
  TITLE     Concerning P450 Evolution: Structural Analyses Support Bacterial
            Origin of Sterol 14alpha-Demethylases
  JOURNAL   Mol Biol Evol 38 (3), 952-967 (2021)
   PUBMED   33031537
  REMARK    GeneRIF: Concerning P450 Evolution: Structural Analyses Support
            Bacterial Origin of Sterol 14alpha-Demethylases.
REFERENCE   6  (residues 1 to 509)
  AUTHORS   Nelson,D.R., Zeldin,D.C., Hoffman,S.M., Maltais,L.J., Wain,H.M. and
            Nebert,D.W.
  TITLE     Comparison of cytochrome P450 (CYP) genes from the mouse and human
            genomes, including nomenclature recommendations for genes,
            pseudogenes and alternative-splice variants
  JOURNAL   Pharmacogenetics 14 (1), 1-18 (2004)
   PUBMED   15128046
  REMARK    Review article
REFERENCE   7  (residues 1 to 509)
  AUTHORS   Stromstedt,M., Rozman,D. and Waterman,M.R.
  TITLE     The ubiquitously expressed human CYP51 encodes lanosterol 14
            alpha-demethylase, a cytochrome P450 whose expression is regulated
            by oxysterols
  JOURNAL   Arch Biochem Biophys 329 (1), 73-81 (1996)
   PUBMED   8619637
REFERENCE   8  (residues 1 to 509)
  AUTHORS   Aoyama,Y., Noshiro,M., Gotoh,O., Imaoka,S., Funae,Y., Kurosawa,N.,
            Horiuchi,T. and Yoshida,Y.
  TITLE     Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient
            and conserved P450 species
  JOURNAL   J Biochem 119 (5), 926-933 (1996)
   PUBMED   8797093
REFERENCE   9  (residues 1 to 509)
  AUTHORS   Aoyama,Y., Funae,Y., Noshiro,M., Horiuchi,T. and Yoshida,Y.
  TITLE     Occurrence of a P450 showing high homology to yeast lanosterol
            14-demethylase (P450(14DM)) in the rat liver
  JOURNAL   Biochem Biophys Res Commun 201 (3), 1320-1326 (1994)
   PUBMED   8024575
REFERENCE   10 (residues 1 to 509)
  AUTHORS   Sonoda,Y., Endo,M., Ishida,K., Sato,Y., Fukusen,N. and Fukuhara,M.
  TITLE     Purification of a human cytochrome P-450 isozyme catalyzing
            lanosterol 14 alpha-demethylation
  JOURNAL   Biochim Biophys Acta 1170 (1), 92-97 (1993)
   PUBMED   8399332
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U23942.1 and AC000120.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the cytochrome P450
            superfamily of enzymes. The cytochrome P450 proteins are
            monooxygenases which catalyze many reactions involved in drug
            metabolism and synthesis of cholesterol, steroids and other lipids.
            This endoplasmic reticulum protein participates in the synthesis of
            cholesterol by catalyzing the removal of the 14alpha-methyl group
            from lanosterol. Homologous genes are found in all three eukaryotic
            phyla, fungi, plants, and animals, suggesting that this is one of
            the oldest cytochrome P450 genes. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Mar 2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.163286.1, U23942.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000003100.13/ ENSP00000003100.8
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..509
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..509
                     /product="lanosterol 14-alpha demethylase isoform 1"
                     /EC_number="1.14.14.154"
                     /note="sterol 14-alpha demethylase; cytochrome P450, 51
                     (lanosterol 14-alpha-demethylase); lanosterol 14-alpha
                     demethylase; CYPLI; cytochrome P450LI; cytochrome
                     P45014DM; cytochrome P450 51A1; cytochrome P450-14DM;
                     cytochrome P450, family 51, subfamily A, polypeptide 1"
                     /calculated_mol_wt=57147
     Site            30..50
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16850.4)"
     Region          94..505
                     /region_name="CYP51-like"
                     /note="cytochrome P450 family 51 and similar cytochrome
                     P450s; cd11042"
                     /db_xref="CDD:410668"
     Site            order(137,159,162,169,314,317..318,321..322,325,377,382,
                     386,388,447..449,452..457,460..461)
                     /site_type="other"
                     /note="heme binding site [chemical binding]"
                     /db_xref="CDD:410668"
     Site            order(137,139..140,144,240,313,316..317,320..321,385,387)
                     /site_type="other"
                     /note="chemical substrate binding pocket [chemical
                     binding]"
                     /db_xref="CDD:410668"
     CDS             1..509
                     /gene="CYP51A1"
                     /gene_synonym="CP51; CYP51; CYPL1; LDM; P450-14DM; P450L1"
                     /coded_by="NM_000786.4:114..1643"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5623.1"
                     /db_xref="GeneID:1595"
                     /db_xref="HGNC:HGNC:2649"
                     /db_xref="MIM:601637"
ORIGIN      
        1 maaaagmlll gllqaggsvl gqamekvtgg nllsmlliac aftlslvyli rlaaghlvql
       61 pagvksppyi fspipflgha iafgkspief lenayekygp vfsftmvgkt ftyllgsdaa
      121 allfnskned lnaedvysrl ttpvfgkgva ydvpnpvfle qkkmlksgln iahfkqhvsi
      181 ieketkeyfe swgesgeknv fealseliil tashclhgke irsqlnekva qlyadldggf
      241 shaawllpgw lplpsfrrrd rahreikdif ykaiqkrrqs qekiddilqt lldatykdgr
      301 pltddevagm liglllagqh tssttsawmg fflardktlq kkcyleqktv cgenlpplty
      361 dqlkdlnlld rciketlrlr ppimimmrma rtpqtvagyt ippghqvcvs ptvnqrlkds
      421 wverldfnpd rylqdnpasg ekfayvpfga grhrcigenf ayvqiktiws tmlrlyefdl
      481 idgyfptvny ttmihtpenp virykrrsk
//
LOCUS       NP_612402                184 aa            linear   PRI 20-NOV-2025
DEFINITION  receptor expression-enhancing protein 6 isoform 2 [Homo sapiens].
ACCESSION   NP_612402
VERSION     NP_612402.1
DBSOURCE    REFSEQ: accession NM_138393.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Zhou,Y., Liu,Y., Gupta,S., Paramo,M.I., Hou,Y., Mao,C., Luo,Y.,
            Judd,J., Wierbowski,S., Bertolotti,M., Nerkar,M., Jehi,L.,
            Drayman,N., Nicolaescu,V., Gula,H., Tay,S., Randall,G., Wang,P.,
            Lis,J.T., Feschotte,C., Erzurum,S.C., Cheng,F. and Yu,H.
  TITLE     A comprehensive SARS-CoV-2-human protein-protein interactome
            reveals COVID-19 pathobiology and potential host therapeutic
            targets
  JOURNAL   Nat Biotechnol 41 (1), 128-139 (2023)
   PUBMED   36217030
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Zhang,L., Li,Y., Qin,L., Wu,Y. and Lei,B.
  TITLE     Autosomal Recessive Retinitis Pigmentosa Associated with Three
            Novel REEP6 Variants in Chinese Population
  JOURNAL   Genes (Basel) 12 (4), 537 (2021)
   PUBMED   33917198
  REMARK    GeneRIF: Autosomal Recessive Retinitis Pigmentosa Associated with
            Three Novel REEP6 Variants in Chinese Population.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Wellmann,A., Fogt,F., Hollerbach,S., Hahne,J., Koenig-Hoffmann,K.,
            Smeets,D. and Brinkmann,U.
  TITLE     Polymorphisms of the apoptosis-associated gene DP1L1 (deleted in
            polyposis 1-like 1) in colon cancer and inflammatory bowel disease
  JOURNAL   J Cancer Res Clin Oncol 136 (6), 795-802 (2010)
   PUBMED   19924442
  REMARK    GeneRIF: DP1L1 polymorphisms are associated with colon cancer and
            IBD. This indicates that DP1L1 plays a functional role in these
            conditions. Thus DP1L1 may be a diagnostic and therapeutic target
            for colon cancer and IBD.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Saito,H., Kubota,M., Roberts,R.W., Chi,Q. and Matsunami,H.
  TITLE     RTP family members induce functional expression of mammalian
            odorant receptors
  JOURNAL   Cell 119 (5), 679-691 (2004)
   PUBMED   15550249
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Ray,S., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human retina for the NEIBank
            Project: retbindin, an abundant, novel retinal cDNA and alternative
            splicing of other retina-preferred gene transcripts
  JOURNAL   Mol Vis 8, 196-204 (2002)
   PUBMED   12107411
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC008201.1 and BU728980.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene may be involved in the
            transport of receptors from the endoplasmic reticulum (ER) to the
            cell surface. The encoded protein may also play a role in
            regulating ER membrane structure. This gene is required for the
            proper development of retinal rods and photoreceptors, with defects
            in this gene being associated with retinitis pigmentosa 77.
            [provided by RefSeq, May 2017].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (2) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.102880.1, BC008201.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000233596.8/ ENSP00000233596.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..184
                     /product="receptor expression-enhancing protein 6 isoform
                     2"
                     /note="deleted in polyposis 1-like 1; polyposis locus
                     protein 1-like 1; receptor expression-enhancing protein 6"
                     /calculated_mol_wt=20602
     Region          66..143
                     /region_name="TB2_DP1_HVA22"
                     /note="TB2/DP1, HVA22 family; pfam03134"
                     /db_xref="CDD:460820"
     CDS             1..184
                     /gene="REEP6"
                     /gene_synonym="C19orf32; DP1L1; REEP6.1; REEP6.2; RP77;
                     TB1; TB2L1; Yip2f"
                     /coded_by="NM_138393.4:90..644"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12070.1"
                     /db_xref="GeneID:92840"
                     /db_xref="HGNC:HGNC:30078"
                     /db_xref="MIM:609346"
ORIGIN      
        1 mdglrqrveh fleqrnlvte vlgaleaktg vekrylaaga vtllslyllf gygasllcnl
       61 igfvypayas ikaiespskd ddtvwltywv vyalfglaef fsdlllswfp fyyvgkcafl
      121 lfcmaprpwn galmlyqrvv rplflrhhga vdrimndlsg raldaaagit rnvkpsqtpq
      181 pkdk
//
LOCUS       NP_858064                432 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform d [Homo sapiens].
ACCESSION   NP_858064
VERSION     NP_858064.1
DBSOURCE    REFSEQ: accession NM_181678.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA365141.1, BI669304.1,
            BC031790.1 and AI621232.1.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..432
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform d"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=50240
     Region          13..427
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          16..64
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          82..159
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..201
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          215..266
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          273..309
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..365
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          404..427
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..432
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_181678.2:276..1574"
                     /note="isoform d is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS43380.1"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 mnypdentyg nkadiistve fnhtgellat gdkggrvvif qreqesknqv hrrgeynvys
       61 tfqshepefd ylksleieek inkirwlpqq naayfllstn dktvklwkvs erdkrpegyn
      121 lkdeegrlrd patittlrvp vlrpmdlmve atprrvfana htyhinsisv nsdyetymsa
      181 ddlrinlwnf eitnqsfniv dikpanmeel tevitaaefh phhcntfvys sskgtirlcd
      241 mrasalcdrh tkffeepedp snrsffseii ssisdvkfsh sgryimtrdy ltvkvwdlnm
      301 enrpietyqv hdylrsklcs lyendcifdk fecvwngsds vimtgsynnf frmfdrntkr
      361 dvtleasren skprailkpr kvcvggkrrk deisvdsldf skkilhtawh pseniiavaa
      421 tnnlyifqdk vn
//
LOCUS       NP_277048                290 aa            linear   PRI 20-NOV-2025
DEFINITION  tubulin polyglutamylase complex subunit 1 [Homo sapiens].
ACCESSION   NP_277048 XP_042012
VERSION     NP_277048.2
DBSOURCE    REFSEQ: accession NM_033513.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 290)
  AUTHORS   Ruse,C.I., Chin,H.G. and Pradhan,S.
  TITLE     Polyglutamylation: biology and analysis
  JOURNAL   Amino Acids 54 (4), 529-542 (2022)
   PUBMED   35357568
  REMARK    Review article
REFERENCE   2  (residues 1 to 290)
  AUTHORS   Wang,L., Paudyal,S.C., Kang,Y., Owa,M., Liang,F.X., Spektor,A.,
            Knaut,H., Sanchez,I. and Dynlacht,B.D.
  TITLE     Regulators of tubulin polyglutamylation control nuclear shape and
            cilium disassembly by balancing microtubule and actin assembly
  JOURNAL   Cell Res 32 (2), 190-209 (2022)
   PUBMED   34782749
REFERENCE   3  (residues 1 to 290)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   4  (residues 1 to 290)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   5  (residues 1 to 290)
  AUTHORS   Regnard,C., Fesquet,D., Janke,C., Boucher,D., Desbruyeres,E.,
            Koulakoff,A., Insina,C., Travo,P. and Edde,B.
  TITLE     Characterisation of PGs1, a subunit of a protein complex
            co-purifying with tubulin polyglutamylase
  JOURNAL   J Cell Sci 116 (Pt 20), 4181-4190 (2003)
   PUBMED   12972506
  REMARK    GeneRIF: Isolation and functional characterization of the mouse
            PGs1 ortholog, and comparison to the human protein.
REFERENCE   6  (residues 1 to 290)
  AUTHORS   Kitazawa,H., Iida,J., Uchida,A., Haino-Fukushima,K., Itoh,T.J.,
            Hotani,H., Ookata,K., Murofushi,H., Bulinski,J.C., Kishimoto,T. and
            Hisanaga,S.
  TITLE     Ser787 in the proline-rich region of human MAP4 is a critical
            phosphorylation site that reduces its activity to promote tubulin
            polymerization
  JOURNAL   Cell Struct Funct 25 (1), 33-39 (2000)
   PUBMED   10791892
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM846833.1 and BC009520.1.
            
            On Jan 19, 2007 this sequence version replaced NP_277048.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.92786.1,
                                           SRR1163655.241914.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000359315.6/ ENSP00000352265.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..290
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..290
                     /product="tubulin polyglutamylase complex subunit 1"
                     /note="gene trap ROSA b-geo 22; polyglutamylase subunit 1"
                     /calculated_mol_wt=31144
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZTW0.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6ZTW0.2)"
     Region          37..75
                     /region_name="DD_TPGS1"
                     /note="dimerization/docking (D/D) domain found in tubulin
                     polyglutamylase complex subunit 1 (TPGS1) and similar
                     proteins; cd22960"
                     /db_xref="CDD:438529"
     Site            266
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99MS8; propagated from
                     UniProtKB/Swiss-Prot (Q6ZTW0.2)"
     CDS             1..290
                     /gene="TPGS1"
                     /gene_synonym="C19orf20; GTRGEO22; PGs1"
                     /coded_by="NM_033513.3:11..883"
                     /db_xref="CCDS:CCDS42454.1"
                     /db_xref="GeneID:91978"
                     /db_xref="HGNC:HGNC:25058"
                     /db_xref="MIM:620709"
ORIGIN      
        1 maavekrrqa vpppagftds grqsvsraag aaeseedflr qvgvtemlra allkvlearp
       61 eepiaflahy fenmglrspv nggageppgq lllqqqrlgr alwhlrlahh sqraafnnnv
      121 svayeclsag grrkrpgldg rtysellrri crdgqapeev vapllrkvqc rdheavplsv
      181 fragtltcfv llefvaraga lfqlledsaa avadrrvgqa vldtlegalq asdaaaparf
      241 leagsrlgpd slalaldrav ggrrpsapmt reefleraaa lfiakvkpvg
//
LOCUS       NP_001242970            1043 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-Ia [Homo sapiens].
ACCESSION   NP_001242970
VERSION     NP_001242970.1
DBSOURCE    REFSEQ: accession NM_001256041.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1043)
  AUTHORS   Gaibee,Z., Warner,N., Bugda Gwilt,K., Li,W., Guan,R., Yourshaw,M.,
            Whittaker Hawkins,R., Zorbas,C., St-Germain,J., Tabatabaie,M.,
            Mao,S., Pinsk,V., Yerushalmi,B., Wang,L.K., Nelson,S.F.,
            Wozniak,L., Shouval,D.S., Matar,M., Assa,A., Frost,N., Jimenez,L.,
            Acra,S., Walters,T., Mouat,S., Li,M., Lafontaine,D.L.J., Tyska,M.,
            Raught,B., Avitzur,Y., Lencer,W.I., Goldenring,J.R., Martin,M.G.,
            Thiagarajah,J.R. and Muise,A.M.
  TITLE     The Genetic Architecture of Congenital Diarrhea and Enteropathy
  JOURNAL   N Engl J Med 392 (13), 1297-1309 (2025)
   PUBMED   40174224
REFERENCE   2  (residues 1 to 1043)
  AUTHORS   Braathen,G.J., Hoyer,H., Busk,O.L., Tveten,K., Skjelbred,C.F. and
            Russell,M.B.
  TITLE     Variants in the genes DCTN2, DNAH10, LRIG3, and MYO1A are
            associated with intermediate Charcot-Marie-Tooth disease in a
            Norwegian family
  JOURNAL   Acta Neurol Scand 134 (1), 67-75 (2016)
   PUBMED   26517670
  REMARK    GeneRIF: This is the first time a haplotype on chromosome 12
            containing sequence variants in the genes DCTN2, DNAH10, LRIG3, and
            MYO1A has been linked to an inherited neuropathy in humans.
REFERENCE   3  (residues 1 to 1043)
  AUTHORS   Patton,J., Brewer,C., Chien,W., Johnston,J.J., Griffith,A.J. and
            Biesecker,L.G.
  TITLE     A genotypic ascertainment approach to refute the association of
            MYO1A variants with non-syndromic deafness
  JOURNAL   Eur J Hum Genet 25 (1), 147-149 (2016)
   PUBMED   27759032
  REMARK    GeneRIF: These data do not support a causal relationship of
            variants in MYO1A to sensorineural hearing loss. We suggest that
            the genotypic ascertainment method is useful to objectively
            evaluate gene-phenotype associations.
REFERENCE   4  (residues 1 to 1043)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   5  (residues 1 to 1043)
  AUTHORS   Kwon,T.J., Oh,S.K., Park,H.J., Sato,O., Venselaar,H., Choi,S.Y.,
            Kim,S., Lee,K.Y., Bok,J., Lee,S.H., Vriend,G., Ikebe,M., Kim,U.K.
            and Choi,J.Y.
  TITLE     The effect of novel mutations on the structure and enzymatic
            activity of unconventional myosins associated with autosomal
            dominant non-syndromic hearing loss
  JOURNAL   Open Biol 4 (7) (2014)
   PUBMED   25080041
  REMARK    GeneRIF: One missense variant, p.R544W, was found in the MYO1A
            gene, and in silico analysis suggested that this variant has
            deleterious effects on protein function.
REFERENCE   6  (residues 1 to 1043)
  AUTHORS   Durrbach,A., Collins,K., Matsudaira,P., Louvard,D. and Coudrier,E.
  TITLE     Brush border myosin-I truncated in the motor domain impairs the
            distribution and the function of endocytic compartments in an
            hepatoma cell line
  JOURNAL   Proc Natl Acad Sci U S A 93 (14), 7053-7058 (1996)
   PUBMED   8692943
REFERENCE   7  (residues 1 to 1043)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   8  (residues 1 to 1043)
  AUTHORS   Okubo,K., Yoshii,J., Yokouchi,H., Kameyama,M. and Matsubara,K.
  TITLE     An expression profile of active genes in human colonic mucosa
  JOURNAL   DNA Res 1 (1), 37-45 (1994)
   PUBMED   7584027
REFERENCE   9  (residues 1 to 1043)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
REFERENCE   10 (residues 1 to 1043)
  AUTHORS   Hoshimaru,M., Fujio,Y., Sobue,K., Sugimoto,T. and Nakanishi,S.
  TITLE     Immunochemical evidence that myosin I heavy chain-like protein is
            identical to the 110-kilodalton brush-border protein
  JOURNAL   J Biochem 106 (3), 455-459 (1989)
   PUBMED   2606897
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC026120.33, AK312431.1,
            AF105424.1 and D25786.1.
            
            Summary: This gene encodes a member of the myosin superfamily. The
            protein represents an unconventional myosin; it should not be
            confused with the conventional skeletal muscle myosin-1 (MYH1).
            Unconventional myosins contain the basic domains characteristic of
            conventional myosins and are further distinguished from class
            members by their tail domains. They function as actin-based
            molecular motors. Mutations in this gene have been associated with
            autosomal dominant deafness. Alternatively spliced variants have
            been found for this gene. [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK312431.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1043
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..1043
                     /product="unconventional myosin-Ia"
                     /note="myosin I heavy chain; myosin, heavy
                     polypeptide-like (100kD); brush border myosin I; myosin,
                     heavy polypeptide-like 110kDa"
                     /calculated_mol_wt=118270
     Region          22..681
                     /region_name="MYSc_Myo1"
                     /note="class I myosin, motor domain; cd01378"
                     /db_xref="CDD:276829"
     Site            order(49..52,57,101..108,148..158,380..385)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276829"
     Site            order(49..52,57)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276829"
     Site            101..108
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276829"
     Site            148..158
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276829"
     Site            380..385
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276829"
     Site            order(409..420,423..430,432)
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276829"
     Region          571..593
                     /region_name="Actin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBC5.1)"
     Site            613..623
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276829"
     Site            order(625..651,668..681)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276829"
     Region          742..764
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          847..1042
                     /region_name="Myosin_TH1"
                     /note="Unconventional myosin tail, actin- and
                     lipid-binding; pfam06017"
                     /db_xref="CDD:461801"
     CDS             1..1043
                     /gene="MYO1A"
                     /gene_synonym="BBMI; DFNA48; DIAR15; MIHC; MYHL"
                     /coded_by="NM_001256041.2:722..3853"
                     /db_xref="CCDS:CCDS8929.1"
                     /db_xref="GeneID:4640"
                     /db_xref="HGNC:HGNC:7595"
                     /db_xref="MIM:601478"
ORIGIN      
        1 mpllegsvgv edlvlleplv eesllknlql ryenkeiyty ignvvisvnp yqqlpiygpe
       61 fiakyqdytf yelkphiyal anvayqslrd rdrdqcilit gesgsgktea sklvmsyvaa
      121 vcgkgeqvns vkeqllqsnp vleafgnakt irnnnssrfg kymdiefdfk gsplggvitn
      181 ylleksrlvk qlkgernfhi fyqllagade qllkalkler dttgyaylnh evsrvdgmdd
      241 assfravqsa mavigfseee irqvlevtsm vlklgnvlva defqasgipa sgirdgrgvr
      301 eigemvglns eeveralcsr tmetakekvv talnvmqaqy ardalakniy srlfdwivnr
      361 inesikvgig ekkkvmgvld iygfeiledn sfeqfvinyc neklqqvfie mtlkeeqeey
      421 kregipwtkv dyfdngiick liehnqrgil amldeeclrp gvvsdstfla klnqlfskhg
      481 hyeskvtqna qrqydhtmgl scfrichyag kvtynvtsfi dknndllfrd llqamwkaqh
      541 pllrslfpeg npkqaslkrp ptagaqfkss vailmknlys kspnyircik pnehqqrgqf
      601 ssdlvatqar ylgllenvrv rragyahrqg ygpfleryrl lsrstwphwn ggdregvekv
      661 lgelsmssge lafgktkifi rspktlfyle eqrrlrlqql atliqkiyrg wrcrthyqlm
      721 rksqilissw frgnmqkkcy gkikasvlli qafvrgwkar knyrkyfrse aaltladfiy
      781 ksmvqkfllg lknnlpstnv ldktwpaapy kclstanqel qqlfyqwkck rfrdqlspkq
      841 veilreklca selfkgkkas ypqsvpipfc gdyiglqgnp klqklkggee gpvlmaeavk
      901 kvnrgngkts srillltkgh viltdtkksq akivigldnv agvsvtslkd glfslhlsem
      961 ssvgskgdfl lvsehviell tkmyravlda tqrqltvtvt ekfsvrfken svavkvvqgp
     1021 aggdnsklry kkkgshclev tvq
//
LOCUS       NP_001265117             182 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform 6 [Homo sapiens].
ACCESSION   NP_001265117
VERSION     NP_001265117.1
DBSOURCE    REFSEQ: accession NM_001278188.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 182)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 182)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 182)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 182)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 182)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK298678.1, AL590431.11 and
            AA863064.1.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (6) lacks an exon in the 5' coding
            region, compared to variant Tpm3.1, and initiates translation at an
            alternate upstream start codon. The encoded isoform (6) is shorter
            and has a distinct N-terminus, compared to isoform Tpm3.1cy.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.200485.1,
                                           SRR1803612.180813.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..182
                     /product="tropomyosin alpha-3 chain isoform 6"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=21222
     Region          <23..180
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..182
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001278188.2:164..712"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 mmqrselsas seklrekggp gnrgmkvien ralkdeekme lqeiqlkeak hiaeeadrky
       61 eevarklvii egdlerteer aelaesrcre mdeqirlmdq nlkclsaaee kysqkedkye
      121 eeikiltdkl keaetraefa ersvaklekt iddledklkc tkeehlctqr mldqtlldln
      181 em
//
LOCUS       NP_006459                534 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase III subunit RPC3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_006459
VERSION     NP_006459.3
DBSOURCE    REFSEQ: accession NM_006468.8
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Hou,H., Li,Y., Wang,M., Liu,A., Yu,Z., Chen,K., Zhao,D. and Xu,Y.
  TITLE     Structural insights into RNA polymerase III-mediated transcription
            termination through trapping poly-deoxythymidine
  JOURNAL   Nat Commun 12 (1), 6135 (2021)
   PUBMED   34675218
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Girbig,M., Misiaszek,A.D., Vorlander,M.K., Lafita,A., Grotsch,H.,
            Baudin,F., Bateman,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase III in its unbound and
            transcribing states
  JOURNAL   Nat Struct Mol Biol 28 (2), 210-219 (2021)
   PUBMED   33558764
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Mertens,C., Hofmann,I., Wang,Z., Teichmann,M., Sepehri Chong,S.,
            Schnolzer,M. and Franke,W.W.
  TITLE     Nuclear particles containing RNA polymerase III complexes
            associated with the junctional plaque protein plakophilin 2
  JOURNAL   Proc Natl Acad Sci U S A 98 (14), 7795-7800 (2001)
   PUBMED   11416169
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Hsieh,Y.J., Kundu,T.K., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     The TFIIIC90 subunit of TFIIIC interacts with multiple components
            of the RNA polymerase III machinery and contains a histone-specific
            acetyltransferase activity
  JOURNAL   Mol Cell Biol 19 (11), 7697-7704 (1999)
   PUBMED   10523658
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Hsieh,Y.J., Wang,Z., Kovelman,R. and Roeder,R.G.
  TITLE     Cloning and characterization of two evolutionarily conserved
            subunits (TFIIIC102 and TFIIIC63) of human TFIIIC and their
            involvement in functional interactions with TFIIIB and RNA
            polymerase III
  JOURNAL   Mol Cell Biol 19 (7), 4944-4952 (1999)
   PUBMED   10373544
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Three human RNA polymerase III-specific subunits form a subcomplex
            with a selective function in specific transcription initiation
  JOURNAL   Genes Dev 11 (10), 1315-1326 (1997)
   PUBMED   9171375
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Jang,K.L., Collins,M.K. and Latchman,D.S.
  TITLE     The human immunodeficiency virus tat protein increases the
            transcription of human Alu repeated sequences by increasing the
            activity of the cellular transcription factor TFIIIC
  JOURNAL   J Acquir Immune Defic Syndr (1988) 5 (11), 1142-1147 (1992)
   PUBMED   1403646
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI831011.1, BC002586.1, DA291657.1, BE258456.1, BQ932484.1 and
            BC053590.1.
            
            On Jun 9, 2002 this sequence version replaced NP_006459.2.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.2101243.1, BC002586.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334163.4/ ENSP00000334564.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.1"
     Protein         1..534
                     /product="DNA-directed RNA polymerase III subunit RPC3
                     isoform 1"
                     /note="DNA-directed RNA polymerase III subunit RPC3; RNA
                     polymerase III subunit C3; DNA-directed III 62 kDa
                     polypeptide; polymerase (RNA) III (DNA directed)
                     polypeptide C (62kD); DNA-directed RNA polymerase III
                     subunit C; RNA polymerase III 62 kDa subunit; polymerase
                     (RNA) III subunit C"
                     /calculated_mol_wt=60481
     Region          7..65
                     /region_name="HTH_9"
                     /note="RNA polymerase III subunit RPC82 helix-turn-helix
                     domain; pfam08221"
                     /db_xref="CDD:400500"
     Region          146..345
                     /region_name="RNA_pol_Rpc82"
                     /note="RNA polymerase III subunit RPC82; pfam05645"
                     /db_xref="CDD:398977"
     Region          161..181
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUI4.1)"
     Site            194
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BUI4.1)"
     Region          197..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUI4.1)"
     CDS             1..534
                     /gene="POLR3C"
                     /gene_synonym="C82; RPC3; RPC62"
                     /coded_by="NM_006468.8:191..1795"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS72864.1"
                     /db_xref="GeneID:10623"
                     /db_xref="HGNC:HGNC:30076"
                     /db_xref="MIM:617454"
ORIGIN      
        1 mtqaeiklcs lllqehfgei vekigvhlir tgsqplrvia hdtgtsldqv kkalcvlvqh
       61 nlvsyqvhkr gvveyeaqcs rvlrmlrypr yiyttktlys dtgeliveel llngkltmsa
      121 vvkkvadrlt etmedgktmd yaevsntfvr ladthfvqrc psvpttensd pgppppaptl
      181 vinekdmylv pklsligkgk rrrssdedaa gepkakrpky ttdnkepipd dgiywqanld
      241 rfhqhfrdqa ivsavanrmd qtsseivrtm lrmseittss sapftqplss neifrslpvg
      301 yniskqvldq yltlladdpl efvgksgdsg ggmyvinlhk alaslatatl esvvqerfgs
      361 rcarifrlvl qkkhieqkqv edfamipake akdmlykmls enfmslqeip ktpdhapsrt
      421 fylytvnils aarmllhrcy ksianlierr qfetkenkrl leksqrveai iasmqatgae
      481 eaqlqeieem itaperqqle tlkrnvnkld aseiqvdeti fllesyiect mkrq
//
LOCUS       NP_067004                335 aa            linear   PRI 20-NOV-2025
DEFINITION  SLAM family member 7 isoform a precursor [Homo sapiens].
ACCESSION   NP_067004
VERSION     NP_067004.3
DBSOURCE    REFSEQ: accession NM_021181.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Chu,E., Wu,J., Kang,S.S. and Kang,Y.
  TITLE     SLAMF7 as a Promising Immunotherapeutic Target in Multiple Myeloma
            Treatments
  JOURNAL   Curr Oncol 30 (9), 7891-7903 (2023)
   PUBMED   37754488
  REMARK    GeneRIF: SLAMF7 as a Promising Immunotherapeutic Target in Multiple
            Myeloma Treatments.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Choe,U., Pham,Q., Kim,Y.S., Yu,L. and Wang,T.T.Y.
  TITLE     Identification and elucidation of cross talk between SLAM Family
            Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages
  JOURNAL   Sci Rep 13 (1), 11007 (2023)
   PUBMED   37420084
  REMARK    GeneRIF: Identification and elucidation of cross talk between SLAM
            Family Member 7 (SLAMF7) and Toll-like receptor (TLR) pathways in
            monocytes and macrophages.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 335)
  AUTHORS   O'Connell,P., Blake,M.K., Godbehere,S., Amalfitano,A. and
            Aldhamen,Y.A.
  TITLE     SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity
  JOURNAL   J Neuroinflammation 19 (1), 241 (2022)
   PUBMED   36199066
  REMARK    GeneRIF: SLAMF7 modulates B cells and adaptive immunity to regulate
            susceptibility to CNS autoimmunity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Simmons,D.P., Nguyen,H.N., Gomez-Rivas,E., Jeong,Y., Jonsson,A.H.,
            Chen,A.F., Lange,J.K., Dyer,G.S., Blazar,P., Earp,B.E.,
            Coblyn,J.S., Massarotti,E.M., Sparks,J.A., Todd,D.J., Rao,D.A.,
            Kim,E.Y. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership (AMP) RA/SLE Network
  TITLE     SLAMF7 engagement superactivates macrophages in acute and chronic
            inflammation
  JOURNAL   Sci Immunol 7 (68), eabf2846 (2022)
   PUBMED   35148199
  REMARK    GeneRIF: SLAMF7 engagement superactivates macrophages in acute and
            chronic inflammation.
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Lee,J.K., Boles,K.S. and Mathew,P.A.
  TITLE     Molecular and functional characterization of a CS1 (CRACC) splice
            variant expressed in human NK cells that does not contain
            immunoreceptor tyrosine-based switch motifs
  JOURNAL   Eur J Immunol 34 (10), 2791-2799 (2004)
   PUBMED   15368295
  REMARK    GeneRIF: CS1-L and CS1-S may differentially regulate human NK cell
            functions
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Tovar,V., del Valle,J., Zapater,N., Martin,M., Romero,X.,
            Pizcueta,P., Bosch,J., Terhorst,C. and Engel,P.
  TITLE     Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family
            of leukocyte cell-surface receptors
  JOURNAL   Immunogenetics 54 (6), 394-402 (2002)
   PUBMED   12242590
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Murphy,J.J., Hobby,P., Vilarino-Varela,J., Bishop,B.,
            Iordanidou,P., Sutton,B.J. and Norton,J.D.
  TITLE     A novel immunoglobulin superfamily receptor (19A) related to CD2 is
            expressed on activated lymphocytes and promotes homotypic B-cell
            adhesion
  JOURNAL   Biochem J 361 (Pt 3), 431-436 (2002)
   PUBMED   11802771
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Bouchon,A., Cella,M., Grierson,H.L., Cohen,J.I. and Colonna,M.
  TITLE     Activation of NK cell-mediated cytotoxicity by a SAP-independent
            receptor of the CD2 family
  JOURNAL   J Immunol 167 (10), 5517-5521 (2001)
   PUBMED   11698418
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Boles,K.S. and Mathew,P.A.
  TITLE     Molecular cloning of CS1, a novel human natural killer cell
            receptor belonging to the CD2 subset of the immunoglobulin
            superfamily
  JOURNAL   Immunogenetics 52 (3-4), 302-307 (2001)
   PUBMED   11220635
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC388332.1, AB027233.1, AL121985.13 and BQ000581.1.
            
            On Apr 4, 2002 this sequence version replaced NP_067004.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a, also known as
            CS1-L).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.315385.1, AB027233.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368043.8/ ENSP00000357022.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..335
                     /product="SLAM family member 7 isoform a precursor"
                     /note="CD2-like receptor activating cytotoxic cells; 19A24
                     protein; novel LY9 (lymphocyte antigen 9) like protein;
                     protein 19A; CD2 subset 1; membrane protein FOAP-12"
                     /calculated_mol_wt=35128
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2311
     mat_peptide     23..335
                     /product="SLAM family member 7. /id=PRO_0000014963"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ25.1)"
                     /calculated_mol_wt=35128
     Region          27..125
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          37..41
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          50..54
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          88..92
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Region          102..107
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          117..120
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            142
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            148
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            204
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Site            227..247
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Region          278..296
                     /region_name="Interaction with FYN when phosphorylated at
                     Tyr-284. /evidence=ECO:0000250|UniProtKB:Q8BHK6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ25.1)"
     Region          302..307
                     /region_name="ITSM.
                     /evidence=ECO:0000250|UniProtKB:Q13291,
                     ECO:0000250|UniProtKB:Q8BHK6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQ25.1)"
     CDS             1..335
                     /gene="SLAMF7"
                     /gene_synonym="19A; CD319; CRACC; CS1"
                     /coded_by="NM_021181.5:56..1063"
                     /note="isoform a precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1209.1"
                     /db_xref="GeneID:57823"
                     /db_xref="HGNC:HGNC:21394"
                     /db_xref="MIM:606625"
ORIGIN      
        1 magsptcltl iyilwqltgs aasgpvkelv gsvggavtfp lkskvkqvds ivwtfnttpl
       61 vtiqpeggti ivtqnrnrer vdfpdggysl klsklkknds giyyvgiyss slqqpstqey
      121 vlhvyehlsk pkvtmglqsn kngtcvtnlt ccmehgeedv iytwkalgqa aneshngsil
      181 piswrwgesd mtficvarnp vsrnfsspil arklcegaad dpdssmvllc lllvplllsl
      241 fvlglflwfl krerqeeyie ekkrvdicre tpnicphsge nteydtipht nrtilkedpa
      301 ntvystveip kkmenphsll tmpdtprlfa yenvi
//
LOCUS       NP_149105                217 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger CCHC-type and RNA-binding motif-containing protein 1
            [Homo sapiens].
ACCESSION   NP_149105
VERSION     NP_149105.3
DBSOURCE    REFSEQ: accession NM_033114.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 217)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 217)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   4  (residues 1 to 217)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   5  (residues 1 to 217)
  AUTHORS   Tan,Y.W., Hong,W. and Liu,D.X.
  TITLE     Binding of the 5'-untranslated region of coronavirus RNA to zinc
            finger CCHC-type and RNA-binding motif 1 enhances viral replication
            and transcription
  JOURNAL   Nucleic Acids Res 40 (11), 5065-5077 (2012)
   PUBMED   22362731
  REMARK    GeneRIF: Using small interfering RNA against MADP1, defective viral
            RNA synthesis was observed in the knockdown cells, therefore
            indicating the importance of the protein in coronaviral RNA
            synthesis.
REFERENCE   6  (residues 1 to 217)
  AUTHORS   Wang,H., Gao,M.X., Li,L., Wang,B., Hori,N. and Sato,K.
  TITLE     Isolation, expression, and characterization of the human ZCRB1 gene
            mapped to 12q12
  JOURNAL   Genomics 89 (1), 59-69 (2007)
   PUBMED   16959469
  REMARK    GeneRIF: The 5'-flanking region contains an enhancer core motif and
            binding sites for AP-1, AP-2, and LF-A1. ZCRB1 is characterized by
            an RNA-binding motif and a CCHC zinc finger motif.
REFERENCE   7  (residues 1 to 217)
  AUTHORS   Golas,M.M., Sander,B., Will,C.L., Luhrmann,R. and Stark,H.
  TITLE     Major conformational change in the complex SF3b upon integration
            into the spliceosomal U11/U12 di-snRNP as revealed by electron
            cryomicroscopy
  JOURNAL   Mol Cell 17 (6), 869-883 (2005)
   PUBMED   15780942
REFERENCE   8  (residues 1 to 217)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB062361.1, BC022543.1 and
            BI666919.1.
            
            On Aug 16, 2004 this sequence version replaced NP_149105.2.
            
            Summary: Pre-mRNA splicing is catalyzed by the spliceosome.
            U12-type spliceosome binds U12-type pre-mRNAs and recognizes the 5'
            splice site and branch-point sequence. U11 and U12 snRNPs are
            components of U12-type spliceosome and function as a molecular
            bridge connecting both ends of the intron. The protein encoded by
            this gene contains a RNA recognition motif. It was identified as
            one of the protein components of U11/U12 snRNPs. This protein and
            many other U11/U12 snRNP proteins are highly conserved in organisms
            known to contain U12-type introns. These proteins have been shown
            to be essential for cell viability, suggesting the key roles in
            U12-type splicing. [provided by RefSeq, Jul 2008].
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC022543.1, SRR1660803.213590.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467147, SAMEA2467148
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266529.8/ ENSP00000266529.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..217
                     /product="zinc finger CCHC-type and RNA-binding
                     motif-containing protein 1"
                     /note="U11/U12 snRNP 31K; zinc finger CCHC-type and RNA
                     binding motif 1; U11/U12-31K; U11/U12 snRNP 31 kDa
                     protein; U11/U12 small nuclear ribonucleoprotein 31 kDa
                     protein"
                     /calculated_mol_wt=24461
     Region          9..84
                     /region_name="RRM_ZCRB1"
                     /note="RNA recognition motif (RRM) found in Zinc finger
                     CCHC-type and RNA-binding motif-containing protein 1
                     (ZCRB1) and similar proteins; cd12393"
                     /db_xref="CDD:409827"
     Region          <97..123
                     /region_name="PTZ00368"
                     /note="universal minicircle sequence binding protein
                     (UMSBP); Provisional"
                     /db_xref="CDD:173561"
     Region          120..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TBF4.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8TBF4.2)"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TBF4.2)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TBF4.2)"
     CDS             1..217
                     /gene="ZCRB1"
                     /gene_synonym="MADP-1; MADP1; RBM36; SNRNP31; ZCCHC19"
                     /coded_by="NM_033114.4:174..827"
                     /db_xref="CCDS:CCDS8740.1"
                     /db_xref="GeneID:85437"
                     /db_xref="HGNC:HGNC:29620"
                     /db_xref="MIM:610750"
ORIGIN      
        1 msgglapsks tvyvsnlpfs ltnndlyrif skygkvvkvt imkdkdtrks kgvafilfld
       61 kdsaqnctra innkqlfgrv ikasiaidng raaefirrrn yfdkskcyec gesghlsyac
      121 pknmlgerep pkkkekkkkk kapepeeeie eveesedege dpaldslsqa iafqqakiee
      181 eqkkwkpssg vpstsddsrr prikkstyfs deeelsd
//
LOCUS       NP_001299602             367 aa            linear   PRI 20-NOV-2025
DEFINITION  choline-phosphate cytidylyltransferase A [Homo sapiens].
ACCESSION   NP_001299602
VERSION     NP_001299602.1
DBSOURCE    REFSEQ: accession NM_001312673.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 367)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 367)
  AUTHORS   Mao,Z., Li,T., Zhao,H., Wang,X., Kang,Y. and Kang,Y.
  TITLE     Methylome and transcriptome profiling revealed epigenetic silencing
            of LPCAT1 and PCYT1A associated with lipidome alterations in
            polycystic ovary syndrome
  JOURNAL   J Cell Physiol 236 (9), 6362-6375 (2021)
   PUBMED   33521992
  REMARK    GeneRIF: Methylome and transcriptome profiling revealed epigenetic
            silencing of LPCAT1 and PCYT1A associated with lipidome alterations
            in polycystic ovary syndrome.
REFERENCE   3  (residues 1 to 367)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 367)
  AUTHORS   Yu,J., Wu,C., Wu,Q., Huang,J., Fu,W., Xie,X., Li,W., Tang,W., Xu,C.
            and Jin,G.
  TITLE     PCYT1A suppresses proliferation and migration via inhibiting mTORC1
            pathway in lung adenocarcinoma
  JOURNAL   Biochem Biophys Res Commun 529 (2), 353-361 (2020)
   PUBMED   32703435
  REMARK    GeneRIF: PCYT1A suppresses proliferation and migration via
            inhibiting mTORC1 pathway in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 367)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 367)
  AUTHORS   Weinhold,P.A. and Feldman,D.A.
  TITLE     Fatty acids promote the formation of complexes between
            choline-phosphate cytidylyltransferase and cytidylyltransferase
            binding protein
  JOURNAL   Arch Biochem Biophys 318 (1), 147-156 (1995)
   PUBMED   7726555
REFERENCE   7  (residues 1 to 367)
  AUTHORS   Kalmar,G.B., Kay,R.J., LaChance,A.C. and Cornell,R.B.
  TITLE     Primary structure and expression of a human CTP:phosphocholine
            cytidylyltransferase
  JOURNAL   Biochim Biophys Acta 1219 (2), 328-334 (1994)
   PUBMED   7918629
REFERENCE   8  (residues 1 to 367)
  AUTHORS   Johnson,J.E. and Cornell,R.B.
  TITLE     Membrane-binding amphipathic alpha-helical peptide derived from
            CTP:phosphocholine cytidylyltransferase
  JOURNAL   Biochemistry 33 (14), 4327-4335 (1994)
   PUBMED   8155650
REFERENCE   9  (residues 1 to 367)
  AUTHORS   Hunt,A.N., Normand,C.S. and Postle,A.D.
  TITLE     CTP:cholinephosphate cytidylyltransferase in human and rat lung:
            association in vitro with cytoskeletal actin
  JOURNAL   Biochim Biophys Acta 1043 (1), 19-26 (1990)
   PUBMED   2155660
REFERENCE   10 (residues 1 to 367)
  AUTHORS   Vance,J.E. and Vance,D.E.
  TITLE     Does rat liver Golgi have the capacity to synthesize phospholipids
            for lipoprotein secretion?
  JOURNAL   J Biol Chem 263 (12), 5898-5909 (1988)
   PUBMED   2833521
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK309073.1, L28957.1,
            AK304534.1, DB223595.1 and AC069257.28.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the cytidylyltransferase family and
            is involved in the regulation of phosphatidylcholine biosynthesis.
            Mutations in this gene are associated with spondylometaphyseal
            dysplasia with cone-rod dystrophy. Alternatively spliced transcript
            variants have been found for this gene. [provided by RefSeq, Aug
            2015].
            
            Transcript Variant: This variant (2) lacks a 5' non-coding exon,
            thus has a shorter 5' UTR compared to variant 1. Variants 1 and 2
            encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.80988.1,
                                           SRR1803616.271858.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000431016.6/ ENSP00000394617.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..367
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..367
                     /product="choline-phosphate cytidylyltransferase A"
                     /EC_number="2.7.7.15"
                     /note="phosphorylcholine transferase A; CTP:phosphocholine
                     cytidylyltransferase A; CT A; CCT A; CCT-alpha;
                     CTP:phosphocholine cytidylyltransferase-alpha;
                     choline-phosphate cytidylyltransferase alpha;
                     phosphorylcholine transferase alpha; phosphate
                     cytidylyltransferase 1, choline, alpha"
                     /calculated_mol_wt=41600
     Region          1..33
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Region          75..224
                     /region_name="CCT"
                     /note="CTP:phosphocholine cytidylyltransferase; cd02174"
                     /db_xref="CDD:173925"
     Site            order(82..85,89,91..92,95,113,122,150..151,168..169,182,
                     195..197,200)
                     /site_type="active"
                     /db_xref="CDD:173925"
     Site            89..92
                     /site_type="other"
                     /note="(T/H)XGH motif"
                     /db_xref="CDD:173925"
     Region          228..287
                     /region_name="Amphipathic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            233
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Region          272..293
                     /region_name="Autoinhibitory (AI).
                     /evidence=ECO:0000250|UniProtKB:P19836"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Region          298..315
                     /region_name="Amphipathic. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Region          313..367
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49585.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            323
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49586; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            325
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P49586; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P19836; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P49585.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P49585.2)"
     CDS             1..367
                     /gene="PCYT1A"
                     /gene_synonym="CCTA; CCTalpha; CGL5; CT; CTA; CTPCT;
                     PCYT1; SMDCRD"
                     /coded_by="NM_001312673.2:123..1226"
                     /db_xref="CCDS:CCDS3315.1"
                     /db_xref="GeneID:5130"
                     /db_xref="HGNC:HGNC:8754"
                     /db_xref="MIM:123695"
ORIGIN      
        1 mdaqcsakvn arkrrkeapg pngateedgv pskvqrcavg lrqpapfsde ievdfskpyv
       61 rvtmeeasrg tpcerpvrvy adgifdlfhs gharalmqak nlfpntyliv gvcsdelthn
      121 fkgftvmnen erydavqhcr yvdevvrnap wtltpeflae hridfvahdd ipyssagsdd
      181 vykhikeagm faptqrtegi stsdiitriv rdydvyarrn lqrgytakel nvsfinekky
      241 hlqervdkvk kkvkdveeks kefvqkveek sidliqkwee ksrefigsfl emfgpegalk
      301 hmlkegkgrm lqaispkqsp sssptrersp spsfrwpfsg ktsppcspan lsrhkaaayd
      361 isedeed
//
LOCUS       NP_001357162             260 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein RFXANK isoform a [Homo sapiens].
ACCESSION   NP_001357162 XP_016882904
VERSION     NP_001357162.1
DBSOURCE    REFSEQ: accession NM_001370233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 260)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 260)
  AUTHORS   Mousavi Khorshidi,M.S., Seeleuthner,Y., Chavoshzadeh,Z., Behfar,M.,
            Hamidieh,A.A., Alimadadi,H., Sherkat,R., Momen,T., Behniafard,N.,
            Eskandarzadeh,S., Mansouri,M., Behnam,M., Mahdavi,M., Heydarazad
            Zadeh,M., Shokri,M., Alizadeh,F., Movahedi,M., Momenilandi,M.,
            Keramatipour,M., Casanova,J.L., Cobat,A., Abel,L., Shahrooei,M. and
            Parvaneh,N.
  TITLE     Clinical, Immunological, and Genetic Findings in Iranian Patients
            with MHC-II Deficiency: Confirmation of c.162delG RFXANK Founder
            Mutation in the Iranian Population
  JOURNAL   J Clin Immunol 43 (8), 1941-1952 (2023)
   PUBMED   37584719
  REMARK    GeneRIF: Clinical, Immunological, and Genetic Findings in Iranian
            Patients with MHC-II Deficiency: Confirmation of c.162delG RFXANK
            Founder Mutation in the Iranian Population.
REFERENCE   3  (residues 1 to 260)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 260)
  AUTHORS   Gao,J. and Xu,C.
  TITLE     Structural basis for the recognition of RFX7 by ANKRA2 and RFXANK
  JOURNAL   Biochem Biophys Res Commun 523 (1), 263-266 (2020)
   PUBMED   31864703
  REMARK    GeneRIF: Structural basis for the recognition of RFX7 by ANKRA2 and
            RFXANK.
REFERENCE   5  (residues 1 to 260)
  AUTHORS   Abolnezhadian,F., Saeedi-Boroujeni,A. and Iranparast,S.
  TITLE     MHC Class II Deficiency with Normal CD4+ T Cell Counts: A Case
            Report
  JOURNAL   Iran J Allergy Asthma Immunol 17 (6), 594-600 (2018)
   PUBMED   30644704
  REMARK    GeneRIF: this study reports an 8 month-old girl with MHC class II
            deficiency with a novel homozygous mutation in RFXANK gene and
            normal CD4+ T cell counts, diagnosed by whole exome sequencing and
            negative HLA-DR proteins on peripheral blood mononuclear cell in
            flow cytometry
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Peijnenburg,A., Gobin,S.J., Boss,J.M. and van den
            elsen,P.J.
  TITLE     Novel mutations within the RFX-B gene and partial rescue of MHC and
            related genes through exogenous class II transactivator in
            RFX-B-deficient cells
  JOURNAL   J Immunol 164 (7), 3666-3674 (2000)
   PUBMED   10725724
REFERENCE   7  (residues 1 to 260)
  AUTHORS   Wiszniewski,W., Fondaneche,M.C., Lambert,N., Masternak,K.,
            Picard,C., Notarangelo,L., Schwartz,K., Bal,J., Reith,W.,
            Alcaide,C., de Saint Basile,G., Fischer,A. and
            Lisowska-Grospierre,B.
  TITLE     Founder effect for a 26-bp deletion in the RFXANK gene in North
            African major histocompatibility complex class II-deficient
            patients belonging to complementation group B
  JOURNAL   Immunogenetics 51 (4-5), 261-267 (2000)
   PUBMED   10803838
REFERENCE   8  (residues 1 to 260)
  AUTHORS   Lin,J.H., Makris,A., McMahon,C., Bear,S.E., Patriotis,C.,
            Prasad,V.R., Brent,R., Golemis,E.A. and Tsichlis,P.N.
  TITLE     The ankyrin repeat-containing adaptor protein Tvl-1 is a novel
            substrate and regulator of Raf-1
  JOURNAL   J Biol Chem 274 (21), 14706-14715 (1999)
   PUBMED   10329666
REFERENCE   9  (residues 1 to 260)
  AUTHORS   Nagarajan,U.M., Louis-Plence,P., DeSandro,A., Nilsen,R., Bushey,A.
            and Boss,J.M.
  TITLE     RFX-B is the gene responsible for the most common cause of the bare
            lymphocyte syndrome, an MHC class II immunodeficiency
  JOURNAL   Immunity 10 (2), 153-162 (1999)
   PUBMED   10072068
  REMARK    Erratum:[Immunity 1999 Mar;10(3):399]
REFERENCE   10 (residues 1 to 260)
  AUTHORS   Masternak,K., Barras,E., Zufferey,M., Conrad,B., Corthals,G.,
            Aebersold,R., Sanchez,J.C., Hochstrasser,D.F., Mach,B. and Reith,W.
  TITLE     A gene encoding a novel RFX-associated transactivator is mutated in
            the majority of MHC class II deficiency patients
  JOURNAL   Nat Genet 20 (3), 273-277 (1998)
   PUBMED   9806546
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002126.1 and AC003110.1.
            
            On May 2, 2019 this sequence version replaced XP_016882904.1.
            
            Summary: Major histocompatibility (MHC) class II molecules are
            transmembrane proteins that have a central role in development and
            control of the immune system. The protein encoded by this gene,
            along with regulatory factor X-associated protein and regulatory
            factor-5, forms a complex that binds to the X box motif of certain
            MHC class II gene promoters and activates their transcription. Once
            bound to the promoter, this complex associates with the
            non-DNA-binding factor MHC class II transactivator, which controls
            the cell type specificity and inducibility of MHC class II gene
            expression. This protein contains ankyrin repeats involved in
            protein-protein interactions. Mutations in this gene have been
            linked to bare lymphocyte syndrome type II, complementation group
            B. Multiple alternatively spliced transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Jul 2013].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.461382.1,
                                           SRR1163657.93631.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..260
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..260
                     /product="DNA-binding protein RFXANK isoform a"
                     /note="ankyrin repeat-containing regulatory factor
                     X-associated protein; regulatory factor X subunit B;
                     RFX-Bdelta4; DNA-binding protein RFXANK; ankyrin repeat
                     family A protein 1"
                     /calculated_mol_wt=27971
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          89..118
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          <94..249
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          94..121
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(123,125,129..130,133..135,137..138,142,145,154,156,
                     158,162..163,166..168,170..171,175,178,187,189,191,
                     195..196,199..201,203..204,208,211)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          123..154
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          123..152
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          156..187
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          156..185
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..218
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     Region          189..217
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          222..251
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O14593.2)"
     CDS             1..260
                     /gene="RFXANK"
                     /gene_synonym="ANKRA1; BLS; F14150_1; MHC2D2; RFX-B"
                     /coded_by="NM_001370233.1:175..957"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS12395.1"
                     /db_xref="GeneID:8625"
                     /db_xref="HGNC:HGNC:9987"
                     /db_xref="MIM:603200"
ORIGIN      
        1 meltqpaedl iqtqqtpase lgdpedpgee aadgsdtvvl slfpctpepv npepdasvss
       61 pqagsslkhs ttltnrqrgn evsalpatld slsihqlaaq geldqlkehl rkgdnlvnkp
      121 dergftpliw asafgeietv rfllewgadp hilakeresa lslastggyt divglllerd
      181 vdiniydwng gtpllyavrg nhvkcveall argadlttea dsgytpmdla valgyrkvqq
      241 vienhilklf qsnlvpadpe
//
LOCUS       NP_001036162             140 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger SWIM domain-containing protein 7 [Homo sapiens].
ACCESSION   NP_001036162
VERSION     NP_001036162.1
DBSOURCE    REFSEQ: accession NM_001042697.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 140)
  AUTHORS   Hengel,S.R., Oppenheimer,K.G., Smith,C.M., Schaich,M.A., Rein,H.L.,
            Martino,J., Darrah,K.E., Witham,M., Ezekwenna,O.C., Burton,K.R.,
            Van Houten,B., Spies,M. and Bernstein,K.A.
  TITLE     The human Shu complex promotes RAD51 activity by modulating RPA
            dynamics on ssDNA
  JOURNAL   Nat Commun 15 (1), 7197 (2024)
   PUBMED   39169038
  REMARK    GeneRIF: The human Shu complex promotes RAD51 activity by
            modulating RPA dynamics on ssDNA.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 140)
  AUTHORS   Hussain,S., Nawaz,S., Khan,I., Khan,N., Hussain,S., Ullah,I.,
            Fakhro,K.A. and Ahmad,W.
  TITLE     A novel homozygous variant in homologous recombination repair gene
            ZSWIM7 causes azoospermia in males and primary ovarian
            insufficiency in females
  JOURNAL   Eur J Med Genet 65 (11), 104629 (2022)
   PUBMED   36202298
  REMARK    GeneRIF: A novel homozygous variant in homologous recombination
            repair gene ZSWIM7 causes azoospermia in males and primary ovarian
            insufficiency in females.
            Review article
REFERENCE   3  (residues 1 to 140)
  AUTHORS   Yatsenko,S.A., Gurbuz,F., Topaloglu,A.K., Berman,A.J., Martin,P.M.,
            Rodrigue-Escriba,M., Qin,Y. and Rajkovic,A.
  TITLE     Pathogenic Variants in ZSWIM7 Cause Primary Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 107 (6), e2359-e2364 (2022)
   PUBMED   35218660
  REMARK    GeneRIF: Pathogenic Variants in ZSWIM7 Cause Primary Ovarian
            Insufficiency.
            Erratum:[J Clin Endocrinol Metab. 2022 Aug 18;107(9):e3969. doi:
            10.1210/clinem/dgac345. PMID: 35689663]
REFERENCE   4  (residues 1 to 140)
  AUTHORS   McGlacken-Byrne,S.M., Le Quesne Stabej,P., Del Valle,I., Ocaka,L.,
            Gagunashvili,A., Crespo,B., Moreno,N., James,C., Bacchelli,C.,
            Dattani,M.T., Williams,H.J., Kelberman,D., Achermann,J.C. and
            Conway,G.S.
  TITLE     ZSWIM7 Is Associated With Human Female Meiosis and Familial Primary
            Ovarian Insufficiency
  JOURNAL   J Clin Endocrinol Metab 107 (1), e254-e263 (2022)
   PUBMED   34402903
  REMARK    GeneRIF: ZSWIM7 Is Associated With Human Female Meiosis and
            Familial Primary Ovarian Insufficiency.
REFERENCE   5  (residues 1 to 140)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   6  (residues 1 to 140)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
REFERENCE   7  (residues 1 to 140)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 140)
  AUTHORS   Sung,Y.J., de las Fuentes,L., Schwander,K.L., Simino,J. and
            Rao,D.C.
  TITLE     Gene-smoking interactions identify several novel blood pressure
            loci in the Framingham Heart Study
  JOURNAL   Am J Hypertens 28 (3), 343-354 (2015)
   PUBMED   25189868
REFERENCE   9  (residues 1 to 140)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   10 (residues 1 to 140)
  AUTHORS   Martin,V., Chahwan,C., Gao,H., Blais,V., Wohlschlegel,J.,
            Yates,J.R. 3rd, McGowan,C.H. and Russell,P.
  TITLE     Sws1 is a conserved regulator of homologous recombination in
            eukaryotic cells
  JOURNAL   EMBO J 25 (11), 2564-2574 (2006)
   PUBMED   16710300
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC006251.3, BU075283.1 and DQ530600.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA593990.1, SRR1660803.219346.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399277.6/ ENSP00000382218.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..140
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..140
                     /product="zinc finger SWIM domain-containing protein 7"
                     /note="SWIM domain-containing and Srs2-interacting protein
                     1 homolog; SWIM-type zinc finger domain-containing protein
                     7"
                     /calculated_mol_wt=15255
     Region          23..133
                     /region_name="COG5431"
                     /note="Predicted nucleic acid-binding protein, contains
                     SWIM-type Zn-finger domain [General function prediction
                     only]"
                     /db_xref="CDD:444183"
     CDS             1..140
                     /gene="ZSWIM7"
                     /gene_synonym="ODG10; SPGF71; SWS1"
                     /coded_by="NM_001042697.2:111..533"
                     /db_xref="CCDS:CCDS42266.1"
                     /db_xref="GeneID:125150"
                     /db_xref="HGNC:HGNC:26993"
                     /db_xref="MIM:614535"
ORIGIN      
        1 mavvlpavve ellsemaaav qesaripdey llslkflfgs satqaldlvd rqsitlissp
       61 sgrrvyqvlg sssktytcla schycscpaf afsvlrksds ilckhllavy lsqvmrtcqq
      121 lsvsdkqltd illmekkqea
//
LOCUS       NP_149115                484 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 2 isoform 1 [Homo sapiens].
ACCESSION   NP_149115
VERSION     NP_149115.2
DBSOURCE    REFSEQ: accession NM_033124.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Jreijiri,F., Cavarocchi,E., Amiri-Yekta,A., Cazin,C.,
            Hosseini,S.H., El Khouri,E., Patrat,C., Thierry-Mieg,N., Ray,P.F.,
            Dulioust,E., Whitfield,M. and Toure,A.
  TITLE     CCDC65, encoding a component of the axonemal Nexin-Dynein
            regulatory complex, is required for sperm flagellum structure in
            humans
  JOURNAL   Clin Genet 105 (3), 317-322 (2024)
   PUBMED   37975235
  REMARK    GeneRIF: CCDC65, encoding a component of the axonemal Nexin-Dynein
            regulatory complex, is required for sperm flagellum structure in
            humans.
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Zhang,J., He,X., Wu,H., Zhang,X., Yang,S., Liu,C., Liu,S., Hua,R.,
            Zhou,S., Zhao,S., Hu,F., Zhang,J., Liu,W., Cheng,H., Gao,Y.,
            Zhang,F., Cao,Y. and Liu,M.
  TITLE     Loss of DRC1 function leads to multiple morphological abnormalities
            of the sperm flagella and male infertility in human and mouse
  JOURNAL   Hum Mol Genet 30 (21), 1996-2011 (2021)
   PUBMED   34169321
REFERENCE   4  (residues 1 to 484)
  AUTHORS   Deng,T., Shen,P., Li,A., Zhang,Z., Yang,H., Deng,X., Peng,X.,
            Hu,Z., Tang,Z., Liu,J., Hou,R., Liu,Z. and Fang,W.
  TITLE     CCDC65 as a new potential tumor suppressor induced by metformin
            inhibits activation of AKT1 via ubiquitination of ENO1 in gastric
            cancer
  JOURNAL   Theranostics 11 (16), 8112-8128 (2021)
   PUBMED   34335983
  REMARK    GeneRIF: CCDC65 as a new potential tumor suppressor induced by
            metformin inhibits activation of AKT1 via ubiquitination of ENO1 in
            gastric cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 484)
  AUTHORS   Sigg,M.A., Menchen,T., Lee,C., Johnson,J., Jungnickel,M.K.,
            Choksi,S.P., Garcia,G. 3rd, Busengdal,H., Dougherty,G.W.,
            Pennekamp,P., Werner,C., Rentzsch,F., Florman,H.M., Krogan,N.,
            Wallingford,J.B., Omran,H. and Reiter,J.F.
  TITLE     Evolutionary Proteomics Uncovers Ancient Associations of Cilia with
            Signaling Pathways
  JOURNAL   Dev Cell 43 (6), 744-762 (2017)
   PUBMED   29257953
REFERENCE   6  (residues 1 to 484)
  AUTHORS   Austin-Tse,C., Halbritter,J., Zariwala,M.A., Gilberti,R.M.,
            Gee,H.Y., Hellman,N., Pathak,N., Liu,Y., Panizzi,J.R.,
            Patel-King,R.S., Tritschler,D., Bower,R., O'Toole,E., Porath,J.D.,
            Hurd,T.W., Chaki,M., Diaz,K.A., Kohl,S., Lovric,S., Hwang,D.Y.,
            Braun,D.A., Schueler,M., Airik,R., Otto,E.A., Leigh,M.W.,
            Noone,P.G., Carson,J.L., Davis,S.D., Pittman,J.E., Ferkol,T.W.,
            Atkinson,J.J., Olivier,K.N., Sagel,S.D., Dell,S.D., Rosenfeld,M.,
            Milla,C.E., Loges,N.T., Omran,H., Porter,M.E., King,S.M.,
            Knowles,M.R., Drummond,I.A. and Hildebrandt,F.
  TITLE     Zebrafish Ciliopathy Screen Plus Human Mutational Analysis
            Identifies C21orf59 and CCDC65 Defects as Causing Primary Ciliary
            Dyskinesia
  JOURNAL   Am J Hum Genet 93 (4), 672-686 (2013)
   PUBMED   24094744
REFERENCE   7  (residues 1 to 484)
  AUTHORS   Horani,A., Brody,S.L., Ferkol,T.W., Shoseyov,D., Wasserman,M.G.,
            Ta-shma,A., Wilson,K.S., Bayly,P.V., Amirav,I.,
            Cohen-Cymberknoh,M., Dutcher,S.K., Elpeleg,O. and Kerem,E.
  TITLE     CCDC65 mutation causes primary ciliary dyskinesia with normal
            ultrastructure and hyperkinetic cilia
  JOURNAL   PLoS One 8 (8), e72299 (2013)
   PUBMED   23991085
  REMARK    GeneRIF: Mutation in CCDC65, a nexin-dynein regulatory complex
            member, resulted in a frameshift mutation and PCD
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 484)
  AUTHORS   Lin,J., Tritschler,D., Song,K., Barber,C.F., Cobb,J.S., Porter,M.E.
            and Nicastro,D.
  TITLE     Building blocks of the nexin-dynein regulatory complex in
            Chlamydomonas flagella
  JOURNAL   J Biol Chem 286 (33), 29175-29191 (2011)
   PUBMED   21700706
REFERENCE   9  (residues 1 to 484)
  AUTHORS   Zheng,Y., Zhang,J., Wang,L., Zhou,Z., Xu,M., Li,J. and Sha,J.H.
  TITLE     Cloning and characterization of a novel sperm tail protein,
            NYD-SP28
  JOURNAL   Int J Mol Med 18 (6), 1119-1125 (2006)
   PUBMED   17089017
  REMARK    GeneRIF: NYD-SP28, a sperm tail protein, was cloned and
            characterized.
REFERENCE   10 (residues 1 to 484)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB026303.1, BC039317.1 and
            CA314956.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 6, 2009 this sequence version replaced NP_149115.1.
            
            Summary: This gene encodes a sperm tail protein that is highly
            expressed in adult testis, spermatocytes and spermatids. The
            protein plays a critical role in the assembly of the nexin-dynein
            regulatory complex. Mutations in this gene result in primary
            ciliary dyskinesia. [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.205939.1,
                                           SRR5189667.322978.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000320516.5/ ENSP00000312706.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..484
                     /product="dynein regulatory complex subunit 2 isoform 1"
                     /note="testis development protein NYD-SP28; coiled-coil
                     domain containing 65"
                     /calculated_mol_wt=57166
     Region          27..124
                     /region_name="NYD-SP28"
                     /note="Sperm tail; pfam14772"
                     /db_xref="CDD:464307"
     CDS             1..484
                     /gene="DRC2"
                     /gene_synonym="CCDC65; CFAP250; FAP250; NYD-SP28"
                     /coded_by="NM_033124.5:205..1659"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8772.1"
                     /db_xref="GeneID:85478"
                     /db_xref="HGNC:HGNC:29937"
                     /db_xref="MIM:611088"
ORIGIN      
        1 mpkkekmakt plsdekqlll fqqkllaeee makkkerlls qflkdklake ehnsalnlnk
       61 intqwrtvlr evktrelhkd ieilsqtfer vvdckdnvik slakdlseae eqyahalrsh
      121 lhnvdqllal qrhrlsllee synmelealt kefeterkti idqhekeihy lqdifmameq
      181 nyidseyesk lefqsmwndl knmnleekhf lrlhlenrve dlwrkfqdvl knytdatedr
      241 kaafetlqvk deksskeiev qmkkiqklqd aitiskgkim ihsreseden ryirndkelv
      301 lvqlrklkaq rtqaraasqk nlvrltlesn atlkalrkiv dkgekilkla eicrkfetee
      361 ekvlpfyssv ltpkeqegiq knnleeltee ltkvmvdyig menfwkrynk vkleqlslqh
      421 rraqllding klremlkqyl dgisvsdevl sqlnplfivn yqsnllqpls iriahpgdkq
      481 hptt
//
LOCUS       NP_001159526             210 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform d
            [Homo sapiens].
ACCESSION   NP_001159526
VERSION     NP_001159526.1
DBSOURCE    REFSEQ: accession NM_001166054.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 210)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC372060.1, DC377357.1,
            CX782504.1, AC131953.1 and AL080130.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (7) differs in the presence and
            absence of exons in the 5' UTR and 5' coding region, and uses a
            downstream translational start codon, compared to variant 1. The
            resulting isoform (d) is significantly shorter at the N-terminus,
            compared to isoform a. Variants 4, 5, 6 and 7 encode the same
            isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.241451.1,
                                           SRR1660803.83685.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..210
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform d"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=23357
     Region          34..160
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(45,119,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(56,58,106..107,109..116,118,126,132,142,144,147,151,
                     154..155,157..158)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..210
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001166054.1:286..918"
                     /note="isoform d is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS54760.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 maerknakal acsslqeran vnldvplqvd fptpktelvq kfhvqylgml pvdkpvgmdi
       61 lnsaienlmt ssnkedwlsv nmnvadatvt visekneeev lvecrvrfls fmgvgkdvht
      121 fafimdtgnq rfechvfwce pnagnvseav qaacmlryqk clvarppsqk vrpppppads
      181 vtrrvttnvk rgvlslidtl kqkrpvtemp
//
LOCUS       NP_004238                972 aa            linear   PRI 20-NOV-2025
DEFINITION  116 kDa U5 small nuclear ribonucleoprotein component isoform a
            [Homo sapiens].
ACCESSION   NP_004238
VERSION     NP_004238.3
DBSOURCE    REFSEQ: accession NM_004247.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 972)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 972)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 972)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 972)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   5  (residues 1 to 972)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   6  (residues 1 to 972)
  AUTHORS   Jurica,M.S., Licklider,L.J., Gygi,S.R., Grigorieff,N. and
            Moore,M.J.
  TITLE     Purification and characterization of native spliceosomes suitable
            for three-dimensional structural analysis
  JOURNAL   RNA 8 (4), 426-439 (2002)
   PUBMED   11991638
REFERENCE   7  (residues 1 to 972)
  AUTHORS   Makarov,E.M., Makarova,O.V., Achsel,T. and Luhrmann,R.
  TITLE     The human homologue of the yeast splicing factor prp6p contains
            multiple TPR elements and is stably associated with the U5 snRNP
            via protein-protein interactions
  JOURNAL   J Mol Biol 298 (4), 567-575 (2000)
   PUBMED   10788320
REFERENCE   8  (residues 1 to 972)
  AUTHORS   Achsel,T., Ahrens,K., Brahms,H., Teigelkamp,S. and Luhrmann,R.
  TITLE     The human U5-220kD protein (hPrp8) forms a stable RNA-free complex
            with several U5-specific proteins, including an RNA unwindase, a
            homologue of ribosomal elongation factor EF-2, and a novel WD-40
            protein
  JOURNAL   Mol Cell Biol 18 (11), 6756-6766 (1998)
   PUBMED   9774689
REFERENCE   9  (residues 1 to 972)
  AUTHORS   Fabrizio,P., Laggerbauer,B., Lauber,J., Lane,W.S. and Luhrmann,R.
  TITLE     An evolutionarily conserved U5 snRNP-specific protein is a
            GTP-binding factor closely related to the ribosomal translocase
            EF-2
  JOURNAL   EMBO J 16 (13), 4092-4106 (1997)
   PUBMED   9233818
REFERENCE   10 (residues 1 to 972)
  AUTHORS   Lines,M., Hartley,T., MacDonald,S.K. and Boycott,K.M.
  TITLE     Mandibulofacial Dysostosis with Microcephaly
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24999515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC353274.1, BC002360.2,
            AK126464.1 and AC015936.14.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 11, 2008 this sequence version replaced NP_004238.2.
            
            Summary: This gene encodes a GTPase which is a component of the
            spliceosome complex which processes precursor mRNAs to produce
            mature mRNAs. Mutations in this gene are associated with
            mandibulofacial dysostosis with microcephaly. Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Both variants 1 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.45034.1,
                                           SRR1803614.32410.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000426333.7/ ENSP00000392094.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..972
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..972
                     /product="116 kDa U5 small nuclear ribonucleoprotein
                     component isoform a"
                     /note="116 kDa U5 small nuclear ribonucleoprotein
                     component; hSNU114; SNU114 homolog; U5 snRNP-specific
                     protein, 116 kDa; elongation factor Tu GTP-binding
                     domain-containing protein 2"
                     /calculated_mol_wt=109305
     Region          1..54
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15029.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Region          4..110
                     /region_name="EFTUD2"
                     /note="116 kDa U5 small nuclear ribonucleoprotein
                     component N-terminus; pfam16004"
                     /db_xref="CDD:464968"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15029.1)"
     Region          122..954
                     /region_name="PRK13351"
                     /note="elongation factor G-like protein; cl46912"
                     /db_xref="CDD:481252"
     CDS             1..972
                     /gene="EFTUD2"
                     /gene_synonym="MFDGA; MFDM; SNRNP116; Snrp116; Snu114;
                     U5-116KD"
                     /coded_by="NM_004247.4:82..3000"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11489.1"
                     /db_xref="GeneID:9343"
                     /db_xref="HGNC:HGNC:30858"
                     /db_xref="MIM:603892"
ORIGIN      
        1 mdtdlydefg nyigpeldsd edddelgret kdldemdddd ddddvgdhdd dhpgmevvlh
       61 edkkyyptae evygpeveti vqeedtqplt epiikpvktk kftlmeqtlp vtvyemdfla
      121 dlmdnselir nvtlcghlhh gktcfvdcli eqthpeirkr ydqdlcytdi lfteqergvg
      181 ikstpvtvvl pdtkgksylf nimdtpghvn fsdevtaglr isdgvvlfid aaegvmlnte
      241 rlikhavqer lavtvcinki drlilelklp ptdayyklrh ivdevnglis mystdenlil
      301 spllgnvcfs ssqysicftl gsfakiyadt fgdinyqefa krlwgdiyfn pktrkftkka
      361 ptsssqrsfv efileplyki laqvvgdvdt slprtldelg ihltkeelkl nirpllrlvc
      421 kkffgeftgf vdmcvqhips pkvgakpkie htytggvdsd lgeamsdcdp dgplmchttk
      481 mystddgvqf hafgrvlsgt ihagqpvkvl genytledee dsqictvgrl wisvaryhie
      541 vnrvpagnwv liegvdqpiv ktatiteprg neeaqifrpl kfnttsviki avepvnpsel
      601 pkmldglrkv nksypslttk veesgehvil gtgelyldcv mhdlrkmyse idikvadpvv
      661 tfcetvvets slkcfaetpn kknkitmiae plekglaedi enevvqitwn rkklgeffqt
      721 kydwdllaar siwafgpdat gpnilvddtl psevdkallg svkdsivqgf qwgtregplc
      781 delirnvkfk ildavvaqep lhrgggqiip tarrvvysaf lmatprlmep yyfvevqapa
      841 dcvsavytvl arrrghvtqd apipgsplyt ikafipaids fgfetdlrth tqgqafslsv
      901 fhhwqivpgd pldksivirp lepqpaphla refmiktrrr kglsedvsis kffddpmlle
      961 lakqdvvlny pm
//
LOCUS       NP_001357402             552 aa            linear   PRI 20-NOV-2025
DEFINITION  CCR4-NOT transcription complex subunit 6 isoform 2 [Homo sapiens].
ACCESSION   NP_001357402 XP_011532907
VERSION     NP_001357402.1
DBSOURCE    REFSEQ: accession NM_001370473.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 552)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 552)
  AUTHORS   Chen,Y., Khazina,E., Izaurralde,E. and Weichenrieder,O.
  TITLE     Crystal structure and functional properties of the human CCR4-CAF1
            deadenylase complex
  JOURNAL   Nucleic Acids Res 49 (11), 6489-6510 (2021)
   PUBMED   34038562
  REMARK    GeneRIF: Crystal structure and functional properties of the human
            CCR4-CAF1 deadenylase complex.
REFERENCE   3  (residues 1 to 552)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 552)
  AUTHORS   Raisch,T., Chang,C.T., Levdansky,Y., Muthukumar,S., Raunser,S. and
            Valkov,E.
  TITLE     Reconstitution of recombinant human CCR4-NOT reveals molecular
            insights into regulated deadenylation
  JOURNAL   Nat Commun 10 (1), 3173 (2019)
   PUBMED   31320642
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 552)
  AUTHORS   Morita,M., Siddiqui,N., Katsumura,S., Rouya,C., Larsson,O.,
            Nagashima,T., Hekmatnejad,B., Takahashi,A., Kiyonari,H., Zang,M.,
            St-Arnaud,R., Oike,Y., Giguere,V., Topisirovic,I.,
            Okada-Hatakeyama,M., Yamamoto,T. and Sonenberg,N.
  TITLE     Hepatic posttranscriptional network comprised of CCR4-NOT
            deadenylase and FGF21 maintains systemic metabolic homeostasis
  JOURNAL   Proc Natl Acad Sci U S A 116 (16), 7973-7981 (2019)
   PUBMED   30926667
  REMARK    GeneRIF: Studied hepatic role in metabolic homeostasis of
            fibroblast growth factor 21(FGF21) and the 'CCR4-NOT complex' (a
            multisubunit protein complex composed of 'CCR4-NOT transcription
            complex subunit 6 like' (CNOT6L) and 'CCR4-NOT transcription
            complex subunit 6' (CNOT6). Results show CNOT6L plays a major role
            in regulation FGF21 levels.
REFERENCE   6  (residues 1 to 552)
  AUTHORS   Morel,A.P., Sentis,S., Bianchin,C., Le Romancer,M., Jonard,L.,
            Rostan,M.C., Rimokh,R. and Corbo,L.
  TITLE     BTG2 antiproliferative protein interacts with the human CCR4
            complex existing in vivo in three cell-cycle-regulated forms
  JOURNAL   J Cell Sci 116 (Pt 14), 2929-2936 (2003)
   PUBMED   12771185
  REMARK    GeneRIF: CCR4 and BTG2 interact and have a role in cell-cycle
            regulation
REFERENCE   7  (residues 1 to 552)
  AUTHORS   Chen,J., Chiang,Y.C. and Denis,C.L.
  TITLE     CCR4, a 3'-5' poly(A) RNA and ssDNA exonuclease, is the catalytic
            component of the cytoplasmic deadenylase
  JOURNAL   EMBO J 21 (6), 1414-1426 (2002)
   PUBMED   11889047
REFERENCE   8  (residues 1 to 552)
  AUTHORS   Dupressoir,A., Morel,A.P., Barbot,W., Loireau,M.P., Corbo,L. and
            Heidmann,T.
  TITLE     Identification of four families of yCCR4- and Mg2+-dependent
            endonuclease-related proteins in higher eukaryotes, and
            characterization of orthologs of yCCR4 with a conserved
            leucine-rich repeat essential for hCAF1/hPOP2 binding
  JOURNAL   BMC Genomics 2, 9 (2001)
   PUBMED   11747467
REFERENCE   9  (residues 1 to 552)
  AUTHORS   Albert,T.K., Lemaire,M., van Berkum,N.L., Gentz,R., Collart,M.A.
            and Timmers,H.T.
  TITLE     Isolation and characterization of human orthologs of yeast CCR4-NOT
            complex subunits
  JOURNAL   Nucleic Acids Res 28 (3), 809-817 (2000)
   PUBMED   10637334
REFERENCE   10 (residues 1 to 552)
  AUTHORS   Okubo,K., Itoh,K., Fukushima,A., Yoshii,J. and Matsubara,K.
  TITLE     Monitoring cell physiology by expression profiles and discovering
            cell type-specific genes by compiled expression profiles
  JOURNAL   Genomics 30 (2), 178-186 (1995)
   PUBMED   8586417
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC034213.5 and AC122714.2.
            
            On May 8, 2019 this sequence version replaced XP_011532907.1.
            
            Summary: This gene encodes the catalytic component of the CCR4-NOT
            core transcriptional regulation complex. The encoded protein has a
            3'-5' RNase activity and prefers polyadenylated substrates. The
            CCR4-NOT complex plays a role in many cellular processes, including
            miRNA-mediated repression, mRNA degradation, and transcriptional
            regulation. [provided by RefSeq, Dec 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.188923.1,
                                           SRR1660803.189404.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..552
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..552
                     /product="CCR4-NOT transcription complex subunit 6 isoform
                     2"
                     /EC_number="3.1.13.4"
                     /note="carbon catabolite repression 4 protein; cytoplasmic
                     deadenylase; carbon catabolite repressor protein 4
                     homolog"
                     /calculated_mol_wt=62648
     Region          <33..>133
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          33..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          53..75
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          75..96
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          76..98
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          98..120
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          99..121
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          121..143
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULM6.2)"
     Region          122..133
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          186..535
                     /region_name="Deadenylase_CCR4a"
                     /note="C-terminal deadenylase domain of CCR4a, also known
                     as CCR4-NOT transcription complex subunit 6; cd10313"
                     /db_xref="CDD:197340"
     Site            order(190,235,356,359,361,367,407,409,411,476,481,
                     485..486,526)
                     /site_type="active"
                     /db_xref="CDD:197340"
     Site            order(190,235,356,359,361,367,407,409,411,476,481,485,526)
                     /site_type="other"
                     /note="poly(A) RNA binding site [nucleotide binding]"
                     /db_xref="CDD:197340"
     Site            order(190,235,356,407,409,486,525..526)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197340"
     Site            order(190,235,525)
                     /site_type="other"
                     /note="Mg binding site A [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(356,409,526)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197340"
     Site            order(407,409,526)
                     /site_type="other"
                     /note="Mg binding site B [ion binding]"
                     /db_xref="CDD:197340"
     CDS             1..552
                     /gene="CNOT6"
                     /gene_synonym="CCR4; Ccr4a"
                     /coded_by="NM_001370473.1:388..2046"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:57472"
                     /db_xref="HGNC:HGNC:14099"
                     /db_xref="MIM:608951"
ORIGIN      
        1 mpkekyeppd prrmytimss eeaangkksh waeleisgkv rslsaslwsl thltalhlsd
       61 nslsripsdi aklhnlvyld lssnkirslp aelgnmvslr elhlnnnllr vlpfelgklf
      121 qlqtlglkgn pltqdilnly qepdgtrrll nylldnlsvt teqppprswi mlqepdrtrp
      181 talfsvmcyn vlcdkyatrq lygycpswal nwdyrkkaii qeilscnadi vslqeveteq
      241 yysfflvelk ergyngffsp ksrartmseq erkhvdgcai ffktekftlv qkhtvefnql
      301 amansegsea mlnrvmtkdn igvavllelr kesiempsgk phlgtekqli lvanahmhwd
      361 peysdvklvq tmmflsevkn iidkasrnlk ssvlgefgti plvlcadlns lpdsgvveyl
      421 stggvetnhk dfkelrynes ltnfschgkn gttngrithg fklqsayesg lmpytnytfd
      481 fkgiidyify skpqlntlgi lgpldhhwlv ennisgcphp lipsdhfslf aqlelllpfl
      541 pqvngihlpg rr
//
LOCUS       NP_001171657             522 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase component PIGT isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001171657
VERSION     NP_001171657.1
DBSOURCE    REFSEQ: accession NM_001184728.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Ben Ayed,I., Jallouli,O., Murakami,Y., Souissi,A., Mallouli,S.,
            Bouzid,A., Kamoun,F., Elloumi,I., Frikha,F., Tlili,A.,
            Weckhuysen,S., Kinoshita,T., Triki,C.C. and Masmoudi,S.
  TITLE     Case report: Functional analysis of the p.Arg507Trp variant of the
            PIGT gene supporting the moderate epilepsy phenotype of mutations
            in the C-terminal region
  JOURNAL   Front Neurol 14, 1092887 (2023)
   PUBMED   36970549
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Ohishi,K., Nagamune,K., Maeda,Y. and Kinoshita,T.
  TITLE     Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and
            PIG-T, form a functionally important intermolecular disulfide
            bridge
  JOURNAL   J Biol Chem 278 (16), 13959-13967 (2003)
   PUBMED   12582175
  REMARK    GeneRIF: GPI8 and PIG-T form a functionally important
            intermolecular disulfide bridge
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Vainauskas,S., Maeda,Y., Kurniawan,H., Kinoshita,T. and Menon,A.K.
  TITLE     Structural requirements for the recruitment of Gaa1 into a
            functional glycosylphosphatidylinositol transamidase complex
  JOURNAL   J Biol Chem 277 (34), 30535-30542 (2002)
   PUBMED   12052837
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Ohishi,K., Inoue,N. and Kinoshita,T.
  TITLE     PIG-S and PIG-T, essential for GPI anchor attachment to proteins,
            form a complex with GAA1 and GPI8
  JOURNAL   EMBO J 20 (15), 4088-4098 (2001)
   PUBMED   11483512
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Fossey,S.C., Mychaleckyj,J.C., Pendleton,J.K., Snyder,J.R.,
            Bensen,J.T., Hirakawa,S., Rich,S.S., Freedman,B.I. and Bowden,D.W.
  TITLE     A high-resolution 6.0-megabase transcript map of the type 2
            diabetes susceptibility region on human chromosome 20
  JOURNAL   Genomics 76 (1-3), 45-57 (2001)
   PUBMED   11549316
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC399420.1, AK296139.1 and
            AL121742.1.
            
            Summary: This gene encodes a protein that is involved in
            glycosylphosphatidylinositol (GPI)-anchor biosynthesis. The
            GPI-anchor is a glycolipid found on many blood cells and serves to
            anchor proteins to the cell surface. This protein is an essential
            component of the multisubunit enzyme, GPI transamidase. GPI
            transamidase mediates GPI anchoring in the endoplasmic reticulum,
            by catalyzing the transfer of fully assembled GPI units to
            proteins. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. [provided by
            RefSeq, May 2012].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, but maintains the reading frame, compared to variant 1. The
            encoded isoform (2) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296139.1, DRR138513.2320.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.12"
     Protein         1..522
                     /product="GPI-anchor transamidase component PIGT isoform 2
                     precursor"
                     /note="neurotrophin-regulated neuronal
                     development-associated protein; GPI transamidase subunit;
                     GPI transamidase component PIG-T; GPI-anchor transamidase
                     component PIGT; phosphatidylinositol-glycan biosynthesis
                     class T protein"
                     /calculated_mol_wt=57489
     sig_peptide     1..21
                     /calculated_mol_wt=2111
     mat_peptide     22..522
                     /product="GPI-anchor transamidase component PIGT isoform
                     2"
                     /calculated_mol_wt=57489
     Region          32..495
                     /region_name="Gpi16"
                     /note="Gpi16 subunit, GPI transamidase component;
                     pfam04113"
                     /db_xref="CDD:461180"
     CDS             1..522
                     /gene="PIGT"
                     /gene_synonym="CGI-06; MCAHS3; NDAP; PIG-T; PNH2"
                     /coded_by="NM_001184728.3:17..1585"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS54464.1"
                     /db_xref="GeneID:51604"
                     /db_xref="HGNC:HGNC:14938"
                     /db_xref="MIM:610272"
ORIGIN      
        1 maaamplall vllllgpggw claepprdsl reelvitplp sgdvaatfqf rtrwdselqr
       61 egvshyrlfp kalgqlisky slrelhlsft qgfwrtrywg ppflqapsdt dhyflryavl
      121 prevvctenl tpwkkllpcs skaglsvllk adrlfhtsyh sqavhirpvc rnarctsisw
      181 elrqtlsvvf dafitgqgkk dwslfrmfsr tltepcplas esrvyvditt ynqdnetlev
      241 hppptttyqd vilgtrktya iydlldtami nnsrnlniql kwkrppenea ppvpflhaqr
      301 yvsgyglqkg elstllynth pyrafpvlll dtvpwylrly vhtltitskg kenkpsyihy
      361 qpaqdrlqph llemliqlpa nsvtkvsiqf erallkwtey tpdpnhgfyv spsvlsalvp
      421 smvaakpvdw eesplfnslf pvsdgsnyfv rlytepllvn lptpdfsmpy nvicltctvv
      481 avcygsfynl ltrtfhieep rtgglakrla nlirrargvp pl
//
LOCUS       NP_065902                745 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin superfamily containing leucine-rich repeat protein 2
            precursor [Homo sapiens].
ACCESSION   NP_065902 XP_027396
VERSION     NP_065902.1
DBSOURCE    REFSEQ: accession NM_020851.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 745)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 745)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 745)
  AUTHORS   Alazami,A.M., Maddirevula,S., Seidahmed,M.Z., Albhlal,L.A. and
            Alkuraya,F.S.
  TITLE     A novel ISLR2-linked autosomal recessive syndrome of congenital
            hydrocephalus, arthrogryposis and abdominal distension
  JOURNAL   Hum Genet 138 (1), 105-107 (2019)
   PUBMED   30483960
  REMARK    GeneRIF: Deletion in ISLR2 gene is associated with autosomal
            recessive syndrome of congenital hydrocephalus, arthrogryposis and
            abdominal distension.
REFERENCE   4  (residues 1 to 745)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA911394.1 and BC152429.1.
            
            On Dec 18, 2003 this sequence version replaced XP_027396.4.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All four transcripts encode the same protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358316.1, AK092297.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000453268.3/ ENSP00000411834.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..745
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..745
                     /product="immunoglobulin superfamily containing
                     leucine-rich repeat protein 2 precursor"
                     /note="immunoglobulin superfamily containing leucine-rich
                     repeat protein 2; leucine-rich repeat domain and
                     immunoglobulin domain-containing axon extension protein"
                     /calculated_mol_wt=76995
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2014
     mat_peptide     19..745
                     /product="Immunoglobulin superfamily containing
                     leucine-rich repeat protein 2. /id=PRO_0000317498"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
                     /calculated_mol_wt=76995
     Region          36..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <51..>183
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          52..73
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            52
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          53..76
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          76..97
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          100..123
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            121
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..169
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          154..>228
                     /region_name="PCC"
                     /note="polycystin cation channel protein; TIGR00864"
                     /db_xref="CDD:188093"
     Region          232..359
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Region          287..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          375..466
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            474
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            563
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            590..610
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Region          656..722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     Site            720
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKR3; propagated from
                     UniProtKB/Swiss-Prot (Q6UXK2.1)"
     CDS             1..745
                     /gene="ISLR2"
                     /gene_synonym="LINX"
                     /coded_by="NM_020851.3:155..2392"
                     /db_xref="CCDS:CCDS10259.1"
                     /db_xref="GeneID:57611"
                     /db_xref="HGNC:HGNC:29286"
                     /db_xref="MIM:614179"
ORIGIN      
        1 mfplralwlv wallgvagsc pepcacvdky ahqfadcayk elrevpeglp anvttlslsa
       61 nkitvlrrga fadvtqvtsl wlahnevrtv epgalavlsq lknldlshnf issfpwsdlr
      121 nlsalqllkm nhnrlgslpr dalgalpdlr slrinnnrlr tlapgtfdal salshlqlyh
      181 npfhcgcglv wlqawaastr vslpepdsia casppalqgv pvyrlpalpc appsvhlsae
      241 ppleapgtpl raglafvlhc iadghptprl qwqlqipggt vvleppvlsg eddgvgaeeg
      301 egegdgdllt qtqaqtptpa pawpappatp rflalangsl lvpllsakea gvytcrahne
      361 lganstsirv avaatgppkh apgaggepdg qaptserkst akgrgnsvlp skpegkikgq
      421 glakvsilge tetepeedts egeeaedqil adpaeeqrcg ngdpsryvsn hafnqsaelk
      481 phvfelgvia ldvaerearv qltplaarwg pgpggaggap rpgrrplrll ylcpagggaa
      541 vqwsrveegv naywfrglrp gtnysvclal ageachvqvv fstkkelpsl lvivavsvfl
      601 lvlatvpllg aacchllakh pgkpyrlilr pqapdpmekr iaadfdpras yleseksypa
      661 ggeaggeepe dvqgeglded aeqgdpsgdl qreeslaacs lvesqskanq eefeagseys
      721 drlplgaeav niaqeingny rqtag
//
LOCUS       NP_001489                637 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamate--cysteine ligase catalytic subunit isoform a [Homo
            sapiens].
ACCESSION   NP_001489
VERSION     NP_001489.1
DBSOURCE    REFSEQ: accession NM_001498.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 637)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 637)
  AUTHORS   Xu,C., Bian,Z., Wang,X., Niu,N., Liu,L., Xiao,Y., Zhu,J., Huang,N.,
            Zhang,Y., Chen,Y., Wu,Q., Sun,F., Zhu,X. and Pan,Q.
  TITLE     SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 331 (2023)
   PUBMED   38049865
  REMARK    GeneRIF: SNORA56-mediated pseudouridylation of 28 S rRNA inhibits
            ferroptosis and promotes colorectal cancer proliferation by
            enhancing GCLC translation.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 637)
  AUTHORS   Liu,C., Wu,X., Bing,X., Qi,W., Zhu,F., Guo,N., Li,C., Gao,X.,
            Cao,X., Zhao,M. and Xia,M.
  TITLE     H1N1 influenza virus infection through NRF2-KEAP1-GCLC pathway
            induces ferroptosis in nasal mucosal epithelial cells
  JOURNAL   Free Radic Biol Med 204, 226-242 (2023)
   PUBMED   37146698
  REMARK    GeneRIF: H1N1 influenza virus infection through NRF2-KEAP1-GCLC
            pathway induces ferroptosis in nasal mucosal epithelial cells.
REFERENCE   4  (residues 1 to 637)
  AUTHORS   Luo,L., Zhang,Z., Weng,Y. and Zeng,J.
  TITLE     Ferroptosis-Related Gene GCLC Is a Novel Prognostic Molecular and
            Correlates with Immune Infiltrates in Lung Adenocarcinoma
  JOURNAL   Cells 11 (21), 3371 (2022)
   PUBMED   36359768
  REMARK    GeneRIF: Ferroptosis-Related Gene GCLC Is a Novel Prognostic
            Molecular and Correlates with Immune Infiltrates in Lung
            Adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 637)
  AUTHORS   Bykanova,M.A., Solodilova,M.A., Azarova,I.E., Klyosova,E.Y.,
            Bushueva,O.Y., Polonikova,A.A., Churnosov,M.I. and Polonikov,A.V.
  TITLE     Genetic variation at the catalytic subunit of glutamate cysteine
            ligase contributes to the susceptibility to sporadic colorectal
            cancer: a pilot study
  JOURNAL   Mol Biol Rep 49 (7), 6145-6154 (2022)
   PUBMED   35386070
  REMARK    GeneRIF: Genetic variation at the catalytic subunit of glutamate
            cysteine ligase contributes to the susceptibility to sporadic
            colorectal cancer: a pilot study.
REFERENCE   6  (residues 1 to 637)
  AUTHORS   Mulcahy,R.T. and Gipp,J.J.
  TITLE     Identification of a putative antioxidant response element in the
            5'-flanking region of the human gamma-glutamylcysteine synthetase
            heavy subunit gene
  JOURNAL   Biochem Biophys Res Commun 209 (1), 227-233 (1995)
   PUBMED   7726839
REFERENCE   7  (residues 1 to 637)
  AUTHORS   Gipp,J.J., Chang,C. and Mulcahy,R.T.
  TITLE     Cloning and nucleotide sequence of a full-length cDNA for human
            liver gamma-glutamylcysteine synthetase
  JOURNAL   Biochem Biophys Res Commun 185 (1), 29-35 (1992)
   PUBMED   1350904
REFERENCE   8  (residues 1 to 637)
  AUTHORS   Beutler,E., Moroose,R., Kramer,L., Gelbart,T. and Forman,L.
  TITLE     Gamma-glutamylcysteine synthetase deficiency and hemolytic anemia
  JOURNAL   Blood 75 (1), 271-273 (1990)
   PUBMED   2294991
REFERENCE   9  (residues 1 to 637)
  AUTHORS   Lebo,R.V. and Kredich,N.M.
  TITLE     Inactivation of human gamma-glutamylcysteine synthetase by
            cystamine. Demonstration and quantification of enzyme-ligand
            complexes
  JOURNAL   J Biol Chem 253 (8), 2615-2623 (1978)
   PUBMED   24639
REFERENCE   10 (residues 1 to 637)
  AUTHORS   Konrad,P.N., Richards,F. 2nd, Valentine,W.N. and Paglia,D.E.
  TITLE     -Glutamyl-cysteine synthetase deficiency. A cause of hereditary
            hemolytic anemia
  JOURNAL   N Engl J Med 286 (11), 557-561 (1972)
   PUBMED   5058793
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI550814.1, AL531593.3,
            AK313480.1, AB262176.1 and BC039894.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Glutamate-cysteine ligase, also known as
            gamma-glutamylcysteine synthetase is the first rate-limiting enzyme
            of glutathione synthesis. The enzyme consists of two subunits, a
            heavy catalytic subunit and a light regulatory subunit. This locus
            encodes the catalytic subunit, while the regulatory subunit is
            derived from a different gene located on chromosome 1p22-p21.
            Mutations at this locus have been associated with hemolytic anemia
            due to deficiency of gamma-glutamylcysteine synthetase and
            susceptibility to myocardial infarction.[provided by RefSeq, Oct
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.95345.1, AB262176.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000650454.1/ ENSP00000497574.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..637
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12.1"
     Protein         1..637
                     /product="glutamate--cysteine ligase catalytic subunit
                     isoform a"
                     /EC_number="6.3.2.2"
                     /note="gamma-glutamylcysteine synthetase; gamma-ECS; GCS
                     heavy chain"
                     /calculated_mol_wt=72635
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48506.2)"
     Region          <22..76
                     /region_name="PRK00087"
                     /note="bifunctional 4-hydroxy-3-methylbut-2-enyl
                     diphosphate reductase/30S ribosomal protein S1"
                     /db_xref="CDD:234623"
     Region          236..608
                     /region_name="GCS"
                     /note="Glutamate-cysteine ligase; pfam03074"
                     /db_xref="CDD:460796"
     CDS             1..637
                     /gene="GCLC"
                     /gene_synonym="CNSHA7; GCL; GCS; GLCL; GLCLC"
                     /coded_by="NM_001498.4:457..2370"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4952.1"
                     /db_xref="GeneID:2729"
                     /db_xref="HGNC:HGNC:4311"
                     /db_xref="MIM:606857"
ORIGIN      
        1 mgllsqgspl sweetkrhad hvrrhgilqf lhiyhavkdr hkdvlkwgde veymlvsfdh
       61 enkkvrlvls gekvletlqe kgertnpnhp tlwrpeygsy miegtpgqpy ggtmsefntv
      121 eanmrkrrke atsileenqa lctitsfprl gcpgftlpev kpnpveggas kslffpdeai
      181 nkhprfstlt rnirhrrgek vvinvpifkd kntpspfiet fteddeasra skpdhiymda
      241 mgfgmgnccl qvtfqacsis earylydqla ticpivmals aaspfyrgyv sdidcrwgvi
      301 sasvddrtre ergleplknn nyrisksryd sidsylskcg ekyndidlti dkeiyeqllq
      361 egidhllaqh vahlfirdpl tlfeekihld danesdhfen iqstnwqtmr fkppppnsdi
      421 gwrvefrpme vqltdfensa yvvfvvlltr vilsykldfl iplskvdenm kvaqkrdavl
      481 qgmfyfrkdi ckggnavvdg cgkaqnstel aaeeytlmsi dtiingkegv fpglipilns
      541 ylenmevdvd trcsilnylk likkrasgel mtvarwmref ianhpdykqd svitdemnys
      601 lilkcnqian elcecpellg safrkvkysg sktdssn
//
LOCUS       NP_001274669             407 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase 32A isoform 3 [Homo sapiens].
ACCESSION   NP_001274669 XP_005268442
VERSION     NP_001274669.1
DBSOURCE    REFSEQ: accession NM_001287740.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Takamitsu,E., Fukunaga,K., Iio,Y., Moriya,K. and Utsumi,T.
  TITLE     Cell-free identification of novel N-myristoylated proteins from
            complementary DNA resources using bioorthogonal myristic acid
            analogues
  JOURNAL   Anal Biochem 464, 83-93 (2014)
   PUBMED   25043870
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Orvedahl,A., Sumpter,R. Jr., Xiao,G., Ng,A., Zou,Z., Tang,Y.,
            Narimatsu,M., Gilpin,C., Sun,Q., Roth,M., Forst,C.V., Wrana,J.L.,
            Zhang,Y.E., Luby-Phelps,K., Xavier,R.J., Xie,Y. and Levine,B.
  TITLE     Image-based genome-wide siRNA screen identifies selective autophagy
            factors
  JOURNAL   Nature 480 (7375), 113-117 (2011)
   PUBMED   22020285
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Koskinen,L.L., Einarsdottir,E., Korponay-Szabo,I.R., Kurppa,K.,
            Kaukinen,K., Sistonen,P., Pocsai,Z., Szeles,G., Adany,R., Maki,M.,
            Kere,J. and Saavalainen,P.
  TITLE     Fine mapping of the CELIAC2 locus on chromosome 5q31-q33 in the
            Finnish and Hungarian populations
  JOURNAL   Tissue Antigens 74 (5), 408-416 (2009)
   PUBMED   19845895
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Schmutz,J., Martin,J., Terry,A., Couronne,O., Grimwood,J.,
            Lowry,S., Gordon,L.A., Scott,D., Xie,G., Huang,W., Hellsten,U.,
            Tran-Gyamfi,M., She,X., Prabhakar,S., Aerts,A., Altherr,M.,
            Bajorek,E., Black,S., Branscomb,E., Caoile,C., Challacombe,J.F.,
            Chan,Y.M., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Glavina,T., Gomez,M., Gonzales,E., Goodstein,D.,
            Grigoriev,I., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Israni,S.,
            Jett,J., Kadner,K., Kimball,H., Kobayashi,A., Lopez,F., Lou,Y.,
            Martinez,D., Medina,C., Morgan,J., Nandkeshwar,R., Noonan,J.P.,
            Pitluck,S., Pollard,M., Predki,P., Priest,J., Ramirez,L.,
            Retterer,J., Rodriguez,A., Rogers,S., Salamov,A., Salazar,A.,
            Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N., Wheeler,J.,
            Wu,K., Yang,J., Dickson,M., Cheng,J.F., Eichler,E.E., Olsen,A.,
            Pennacchio,L.A., Rokhsar,D.S., Richardson,P., Lucas,S.M.,
            Myers,R.M. and Rubin,E.M.
  TITLE     The DNA sequence and comparative analysis of human chromosome 5
  JOURNAL   Nature 431 (7006), 268-274 (2004)
   PUBMED   15372022
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Manning,G., Whyte,D.B., Martinez,R., Hunter,T. and Sudarsanam,S.
  TITLE     The protein kinase complement of the human genome
  JOURNAL   Science 298 (5600), 1912-1934 (2002)
   PUBMED   12471243
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK315942.1 and AC009189.6.
            
            On Dec 19, 2013 this sequence version replaced XP_005268442.1.
            
            Transcript Variant: This variant (3) represents the longest
            transcript and encodes the longest isoform (3).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.59330.1,
                                           SRR1803611.69045.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..407
                     /product="serine/threonine-protein kinase 32A isoform 3"
                     /EC_number="2.7.11.1"
                     /note="A930015B13Rik; serine/threonine-protein kinase 32A;
                     yet another novel kinase 1; CTB-108O6.2"
                     /calculated_mol_wt=47409
     Region          22..281
                     /region_name="STKc_Yank1"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Yank1; cd05578"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,100..101,103,107,109,146,148,
                     150..151,153,163..164,167,180..185,215,221,224)
                     /site_type="active"
                     /db_xref="CDD:270730"
     Site            order(29..33,37,50,52,84,101..103,107,146,148,150..151,
                     153,163..164)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270730"
     Site            order(33,107,109,146,148,150,167,180..185,215,221,224)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270730"
     Site            order(163..173,177..185)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270730"
     CDS             1..407
                     /gene="STK32A"
                     /gene_synonym="YANK1"
                     /coded_by="NM_001287740.2:271..1494"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75351.1"
                     /db_xref="GeneID:202374"
                     /db_xref="HGNC:HGNC:28317"
                     /db_xref="MIM:621310"
ORIGIN      
        1 mgantsrkpp vfdenedvnf dhfeilraig kgsfgkvciv qkndtkkmya mkymnkqkcv
       61 ernevrnvfk elqimqgleh pflvnlwysf qdeedmfmvv dlllggdlry hlqqnvhfke
      121 etvklficel vmaldylqnq riihrdmkpd nilldehghv hitdfniaam lpretqittm
      181 agtkpymape mfssrkgagy sfavdwwslg vtayellrgr rpyhirssts skeivhtfet
      241 tvvtypsaws qemvsllkkl lepnpdqrfs qlsdvqnfpy mndinwdavf qkrlipgfip
      301 nkgrlncdpt feleemiles kplhkkkkrl akkekdmrkc dssqtcllqe hldsvqkefi
      361 ifnrekvnrd fnkrqpnlal eqtkdpqvtn gqmdtglset fqtskvs
//
LOCUS       NP_976030                458 aa            linear   PRI 20-NOV-2025
DEFINITION  nectin-1 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_976030
VERSION     NP_976030.1
DBSOURCE    REFSEQ: accession NM_203285.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 458)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 458)
  AUTHORS   Kite,J., Hill,M., Preston,N., Rubina,A., Kollnberger,S.,
            Wang,E.C.Y. and Elliott,G.
  TITLE     Downregulation of endogenous nectin1 in human keratinocytes by
            herpes simplex virus 1 glycoprotein D excludes superinfection but
            does not affect NK cell function
  JOURNAL   J Gen Virol 105 (3) (2024)
   PUBMED   38471041
  REMARK    GeneRIF: Downregulation of endogenous nectin1 in human
            keratinocytes by herpes simplex virus 1 glycoprotein D excludes
            superinfection but does not affect NK cell function.
REFERENCE   3  (residues 1 to 458)
  AUTHORS   Park,J.W., Kang,G., Baek,S.H. and Kim,Y.H.
  TITLE     Genetic associations and parent-of-origin effects of PVRL1 in
            non-syndromic cleft lip with or without cleft palate across
            multiple ethnic populations
  JOURNAL   Epidemiol Health 46, e2024069 (2024)
   PUBMED   39139080
  REMARK    GeneRIF: Genetic associations and parent-of-origin effects of PVRL1
            in non-syndromic cleft lip with or without cleft palate across
            multiple ethnic populations.
REFERENCE   4  (residues 1 to 458)
  AUTHORS   De La Cruz,N.C., Mockel,M., Niehues,H., Rubsam,M., Malter,W.,
            Zinser,M., Krummenacher,C. and Knebel-Morsdorf,D.
  TITLE     Ex Vivo Infection of Human Skin Models with Herpes Simplex Virus 1:
            Accessibility of the Receptor Nectin-1 during Formation or
            Impairment of Epidermal Barriers Is Restricted by Tight Junctions
  JOURNAL   J Virol 97 (6), e0026223 (2023)
   PUBMED   37289055
  REMARK    GeneRIF: Ex Vivo Infection of Human Skin Models with Herpes Simplex
            Virus 1: Accessibility of the Receptor Nectin-1 during Formation or
            Impairment of Epidermal Barriers Is Restricted by Tight Junctions.
REFERENCE   5  (residues 1 to 458)
  AUTHORS   Ablain,J., Al Mahi,A., Rothschild,H., Prasad,M., Aires,S., Yang,S.,
            Dokukin,M.E., Xu,S., Dang,M., Sokolov,I., Lian,C.G. and Zon,L.I.
  TITLE     Loss of NECTIN1 triggers melanoma dissemination upon local IGF1
            depletion
  JOURNAL   Nat Genet 54 (12), 1839-1852 (2022)
   PUBMED   36229674
  REMARK    GeneRIF: Loss of NECTIN1 triggers melanoma dissemination upon local
            IGF1 depletion.
REFERENCE   6  (residues 1 to 458)
  AUTHORS   Krummenacher,C., Nicola,A.V., Whitbeck,J.C., Lou,H., Hou,W.,
            Lambris,J.D., Geraghty,R.J., Spear,P.G., Cohen,G.H. and
            Eisenberg,R.J.
  TITLE     Herpes simplex virus glycoprotein D can bind to poliovirus
            receptor-related protein 1 or herpesvirus entry mediator, two
            structurally unrelated mediators of virus entry
  JOURNAL   J Virol 72 (9), 7064-7074 (1998)
   PUBMED   9696799
REFERENCE   7  (residues 1 to 458)
  AUTHORS   Geraghty,R.J., Krummenacher,C., Cohen,G.H., Eisenberg,R.J. and
            Spear,P.G.
  TITLE     Entry of alphaherpesviruses mediated by poliovirus receptor-related
            protein 1 and poliovirus receptor
  JOURNAL   Science 280 (5369), 1618-1620 (1998)
   PUBMED   9616127
REFERENCE   8  (residues 1 to 458)
  AUTHORS   Lopez,M., Eberle,F., Mattei,M.G., Gabert,J., Birg,F., Bardin,F.,
            Maroc,C. and Dubreuil,P.
  TITLE     Complementary DNA characterization and chromosomal localization of
            a human gene related to the poliovirus receptor-encoding gene
  JOURNAL   Gene 155 (2), 261-265 (1995)
   PUBMED   7721102
REFERENCE   9  (residues 1 to 458)
  AUTHORS   Bustos,T., Simosa,V., Pinto-Cisternas,J., Abramovits,W., Jolay,L.,
            Rodriguez,L., Fernandez,L. and Ramela,M.
  TITLE     Autosomal recessive ectodermal dysplasia: I. An undescribed
            dysplasia/malformation syndrome
  JOURNAL   Am J Med Genet 41 (4), 398-404 (1991)
   PUBMED   1776626
REFERENCE   10 (residues 1 to 458)
  AUTHORS   Carritt,B. and Goldfarb,P.
  TITLE     A human chromosomal determinant for susceptibility to herpes
            simplex virus
  JOURNAL   Nature 264 (5586), 556-558 (1976)
   PUBMED   1034214
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP003390.1, AI819997.1 and
            AF110314.1.
            
            Summary: This gene encodes an adhesion protein that plays a role in
            the organization of adherens junctions and tight junctions in
            epithelial and endothelial cells. The protein is a
            calcium(2+)-independent cell-cell adhesion molecule that belongs to
            the immunoglobulin superfamily and has 3 extracellular
            immunoglobulin-like loops, a single transmembrane domain (in some
            isoforms), and a cytoplasmic region. This protein acts as a
            receptor for glycoprotein D (gD) of herpes simplex viruses 1 and 2
            (HSV-1, HSV-2), and pseudorabies virus (PRV) and mediates viral
            entry into epithelial and neuronal cells. Mutations in this gene
            cause cleft lip and palate/ectodermal dysplasia 1 syndrome (CLPED1)
            as well as non-syndromic cleft lip with or without cleft palate
            (CL/P). Alternative splicing results in multiple transcript
            variants encoding proteins with distinct C-termini. [provided by
            RefSeq, Oct 2009].
            
            Transcript Variant: This variant (2) uses alternate exons for its
            3' end, compared to variant 1, resulting in a protein (isoform 2;
            also known as isoform Alpha, beta, or HIgR) with a shorter and
            distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF110314.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..458
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..458
                     /product="nectin-1 isoform 2 precursor"
                     /note="nectin 1; poliovirus receptor-related 1
                     (herpesvirus entry mediator C); ectodermal dysplasia 4
                     (Margarita Island type); poliovirus receptor-like 1;
                     poliovirus receptor-related protein 1; herpesvirus Ig-like
                     receptor; herpes virus entry mediator C; herpes simplex
                     virus type 1 sensitivity"
                     /calculated_mol_wt=47624
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3116
     mat_peptide     31..458
                     /product="nectin-1 isoform 2"
                     /calculated_mol_wt=47624
     Region          31..143
                     /region_name="IgV_1_Nectin-1_like"
                     /note="First immunoglobulin variable (IgV) domain of
                     nectin-1, and similar domains; cd05886"
                     /db_xref="CDD:409469"
     Region          31..54
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409469"
     Region          31..35
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409469"
     Region          37..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409469"
     Site            order(45..52,62..70,77..89,107..113,118..132,135..143)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409469"
     Region          46..54
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409469"
     Region          55..62
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409469"
     Region          63..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409469"
     Region          64..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409469"
     Region          70..89
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409469"
     Region          79..84
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409469"
     Region          86..90
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409469"
     Region          90..128
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409469"
     Region          97..101
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409469"
     Region          106..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409469"
     Region          120..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409469"
     Region          129..132
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409469"
     Region          132..142
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409469"
     Region          133..143
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409469"
     Region          146..243
                     /region_name="IgC1_2_Nectin-1_like"
                     /note="Second immunoglobulin (Ig) domain of nectin-1, and
                     similar domains; member of the C1-set of Ig superfamily
                     (IgSF) domains; cd05890"
                     /db_xref="CDD:143298"
     Region          146..152
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:143298"
     Region          168..175
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:143298"
     Region          180..186
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:143298"
     Region          188..190
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:143298"
     Region          191..199
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:143298"
     Region          205..213
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:143298"
     Region          223..230
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:143298"
     Region          234..240
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:143298"
     Region          247..325
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          265..269
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409524"
     Region          279..283
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409524"
     Region          298..302
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409524"
     Region          313..318
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409524"
     CDS             1..458
                     /gene="NECTIN1"
                     /gene_synonym="CD111; CLPED1; ED4; HIgR; HV1S; HVEC;
                     nectin-1; OFC7; PRR; PRR1; PVRL1; PVRR; PVRR1; SK-12"
                     /coded_by="NM_203285.2:648..2024"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:5818"
                     /db_xref="HGNC:HGNC:9706"
                     /db_xref="MIM:600644"
ORIGIN      
        1 marmglagaa grwwglalgl tafflpgvhs qvvqvndsmy gfigtdvvlh csfanplpsv
       61 kitqvtwqks tngskqnvai ynpsmgvsvl apyrervefl rpsftdgtir lsrleledeg
      121 vyicefatfp tgnresqlnl tvmakptnwi egtqavlrak kgqddkvlva tctsangkpp
      181 svvswetrlk geaeyqeirn pngtvtvisr yrlvpsreah qqslacivny hmdrfkeslt
      241 lnvqyepevt iegfdgnwyl qrmdvkltck adanppatey hwttlngslp kgveaqnrtl
      301 ffkgpinysl agtyiceatn pigtrsgqve vnitekprpq rglgsaarll agtvavflil
      361 vavltvffly nrqqksppet dgagtdqpls qkpepspsrq sslvpediqv vhldpgrqqq
      421 qeeedlqkls lqppyydlgv spsyhpsvrt teprgecp
//
LOCUS       NP_057467                313 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine zipper protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_057467
VERSION     NP_057467.1
DBSOURCE    REFSEQ: accession NM_016383.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 313)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 313)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   4  (residues 1 to 313)
  AUTHORS   Viphakone,N., Cumberbatch,M.G., Livingstone,M.J., Heath,P.R.,
            Dickman,M.J., Catto,J.W. and Wilson,S.A.
  TITLE     Luzp4 defines a new mRNA export pathway in cancer cells
  JOURNAL   Nucleic Acids Res 43 (4), 2353-2366 (2015)
   PUBMED   25662211
  REMARK    GeneRIF: Luzp4 is an RNA-binding protein which associates with the
            TREX mRNA export complex subunit Uap56. Luzp4 also binds the
            principal mRNA export receptor Nxf1, enhances its RNA binding
            activity and complements Alyref knockdown in vivo. Luzp4 displays
            all features of an mRNA export adaptor. Whilst Luzp4 is
            up-regulated in a range of tumours, it appears preferentially
            expressed in melanoma cells where it is required for growth.
REFERENCE   5  (residues 1 to 313)
  AUTHORS   Tureci,O., Sahin,U., Koslowski,M., Buss,B., Bell,C., Ballweber,P.,
            Zwick,C., Eberle,T., Zuber,M., Villena-Heinsen,C., Seitz,G. and
            Pfreundschuh,M.
  TITLE     A novel tumour associated leucine zipper protein targeting to sites
            of gene transcription and splicing
  JOURNAL   Oncogene 21 (24), 3879-3888 (2002)
   PUBMED   12032826
  REMARK    GeneRIF: A novel tumour associated leucine zipper protein targeting
            to sites of gene transcription and splicing.
REFERENCE   6  (residues 1 to 313)
  AUTHORS   Sahin,U., Koslowski,M., Tureci,O., Eberle,T., Zwick,C., Romeike,B.,
            Moringlane,J.R., Schwechheimer,K., Feiden,W. and Pfreundschuh,M.
  TITLE     Expression of cancer testis genes in human brain tumors
  JOURNAL   Clin Cancer Res 6 (10), 3916-3922 (2000)
   PUBMED   11051238
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC239923.3, DB035084.1,
            AF124430.1 and AK093369.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a leucine-zipper protein that was first
            defined as a cancer testis antigens. The encoded protein is an RNA
            binding protein that interacts with the mRNA export receptor
            nuclear RNA export factor 2. Alternate splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.364378.1,
                                           SRR5189667.137125.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000371920.4/ ENSP00000360988.3
            RefSeq Select criteria :: based on expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..313
                     /product="leucine zipper protein 4 isoform 1"
                     /note="HOM-TES-85 tumor antigen; cancer/testis antigen 28;
                     tumor antigen HOM-TES-85"
                     /calculated_mol_wt=35806
     Region          1..238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          1..119
                     /region_name="Interaction with DDX39B/UAP56.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          22..40
                     /region_name="UAP56-binding motif (UBM), required for
                     proper nuclear localization.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          51..80
                     /region_name="Arg-rich, required for RNA-binding.
                     /evidence=ECO:0000303|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          <110..>255
                     /region_name="PHA00430"
                     /note="tail fiber protein"
                     /db_xref="CDD:222790"
     Region          178..236
                     /region_name="RS-containing His-rich (RS-H), necessary for
                     nuclear localization.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          238..287
                     /region_name="Leucine-zipper, required for RNA-binding and
                     for its relocalization to the cytoplasm during cell
                     division. /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          241..313
                     /region_name="Interaction with NXF1.
                     /evidence=ECO:0000269|PubMed:25662211"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     Region          290..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P127.1)"
     CDS             1..313
                     /gene="LUZP4"
                     /gene_synonym="CT-28; CT-8; CT28; HOM-TES-85"
                     /coded_by="NM_016383.5:46..987"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14567.1"
                     /db_xref="GeneID:51213"
                     /db_xref="HGNC:HGNC:24971"
                     /db_xref="MIM:300616"
ORIGIN      
        1 masfrkltls ekvppnhpsr kkvnfldmsl ddiiiykele gtnaeeeknk rqnhskkesp
       61 srqqskahrh rhrrgysrcr snseegnhdk kpsqkpsgfk sgqhplngqp lieqekcsdn
      121 yeaqaeknqg qsegnqhqse gnpdkseesq gqpeenhhse rsrnhlersl sqsdrsqgql
      181 krhhpqyers hgqykrshgq sershghser shghsershg hsershghsk rsrsqgdlvd
      241 tqsdliatqr dliatqkdli atqrdliatq rdlivtqrdl vaterdlinq sgrshgqser
      301 hqrystgknt itt
//
LOCUS       NP_036524                284 aa            linear   PRI 20-NOV-2025
DEFINITION  peflin isoform 1 [Homo sapiens].
ACCESSION   NP_036524
VERSION     NP_036524.1
DBSOURCE    REFSEQ: accession NM_012392.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 284)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 284)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 284)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 284)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 284)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 284)
  AUTHORS   Hansen,C., Tarabykina,S., la Cour,J.M., Lollike,K. and
            Berchtold,M.W.
  TITLE     The PEF family proteins sorcin and grancalcin interact in vivo and
            in vitro
  JOURNAL   FEBS Lett 545 (2-3), 151-154 (2003)
   PUBMED   12804766
REFERENCE   7  (residues 1 to 284)
  AUTHORS   Satoh,H., Nakano,Y., Shibata,H. and Maki,M.
  TITLE     The penta-EF-hand domain of ALG-2 interacts with amino-terminal
            domains of both annexin VII and annexin XI in a Ca2+-dependent
            manner
  JOURNAL   Biochim Biophys Acta 1600 (1-2), 61-67 (2002)
   PUBMED   12445460
REFERENCE   8  (residues 1 to 284)
  AUTHORS   Kitaura,Y., Satoh,H., Takahashi,H., Shibata,H. and Maki,M.
  TITLE     Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
            by dimerization through their fifth EF-hand regions
  JOURNAL   Arch Biochem Biophys 399 (1), 12-18 (2002)
   PUBMED   11883899
  REMARK    GeneRIF: peflin is stabilized by dimerization through its fifth
            EF-hand region
REFERENCE   9  (residues 1 to 284)
  AUTHORS   Kitaura,Y., Matsumoto,S., Satoh,H., Hitomi,K. and Maki,M.
  TITLE     Peflin and ALG-2, members of the penta-EF-hand protein family, form
            a heterodimer that dissociates in a Ca2+-dependent manner
  JOURNAL   J Biol Chem 276 (17), 14053-14058 (2001)
   PUBMED   11278427
REFERENCE   10 (residues 1 to 284)
  AUTHORS   Kitaura,Y., Watanabe,M., Satoh,H., Kawai,T., Hitomi,K. and Maki,M.
  TITLE     Peflin, a novel member of the five-EF-hand-protein family, is
            similar to the apoptosis-linked gene 2 (ALG-2) protein but
            possesses nonapeptide repeats in the N-terminal hydrophobic region
  JOURNAL   Biochem Biophys Res Commun 263 (1), 68-75 (1999)
   PUBMED   10486255
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012561.1, AC114488.3 and
            CA307778.1.
            
            Summary: This gene encodes a calcium-binding protein belonging to
            the penta-EF-hand protein family. The encoded protein has been
            shown to form a heterodimer with the programmed cell death 6 gene
            product and may modulate its function in Ca(2+) signaling.
            Alternative splicing results in multiple transcript variants and a
            pseudogene has been identified on chromosome 1.[provided by RefSeq,
            May 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.142956.1,
                                           SRR3476690.202122.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373703.5/ ENSP00000362807.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..284
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..284
                     /product="peflin isoform 1"
                     /note="PEF protein with a long N-terminal hydrophobic
                     domain; epididymis secretory sperm binding protein"
                     /calculated_mol_wt=30250
     Region          1..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBV8.1)"
     Region          21..109
                     /region_name="9 X 9 AA approximate tandem repeat of
                     [AP]-P-G-G-P-Y-G-G-P-P. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBV8.1)"
     Region          118..283
                     /region_name="EFh_PEF_peflin"
                     /note="EF-hand, calcium binding motif, found in peflin and
                     similar proteins; cd16184"
                     /db_xref="CDD:320059"
     Region          118..147
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Site            order(127,129,131,138,194,196,198,205)
                     /site_type="other"
                     /note="putative Ca binding site [ion binding]"
                     /db_xref="CDD:320059"
     Region          155..184
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          185..215
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          204..284
                     /region_name="Required for interaction with PDCD6.
                     /evidence=ECO:0000269|PubMed:11883899"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBV8.1)"
     Region          221..251
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     Region          252..283
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320059"
     CDS             1..284
                     /gene="PEF1"
                     /gene_synonym="ABP32; PEF1A"
                     /coded_by="NM_012392.4:13..867"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS345.1"
                     /db_xref="GeneID:553115"
                     /db_xref="HGNC:HGNC:30009"
                     /db_xref="MIM:610033"
ORIGIN      
        1 masypyrqgc pgaagqapga ppgsyypgpp nsggqygsgl ppgggyggpa pggpygppag
       61 ggpyghpnpg mfpsgtpggp yggaapggpy gqpppssyga qqpglygqgg appnvdpeay
      121 swfqsvdsdh sgyismkelk qalvncnwss fndetclmmi nmfdktksgr idvygfsalw
      181 kfiqqwknlf qqydrdrsgs isytelqqal sqmgynlspq ftqllvsryc prsanpamql
      241 drfiqvctql qvlteafrek dtavqgnirl sfedfvtmta srml
//
LOCUS       NP_000975                156 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL23 [Homo sapiens].
ACCESSION   NP_000975 XP_208300
VERSION     NP_000975.2
DBSOURCE    REFSEQ: accession NM_000984.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 156)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 156)
  AUTHORS   Zhang,Z., Wu,Q., Fang,M., Liu,Y., Jiang,J., Feng,Q., Hu,R. and
            Xu,J.
  TITLE     HERC3 directly targets RPL23A for ubiquitination degradation and
            further regulates Colorectal Cancer proliferation and the cell
            cycle
  JOURNAL   Int J Biol Sci 18 (8), 3282-3297 (2022)
   PUBMED   35637966
  REMARK    GeneRIF: HERC3 directly targets RPL23A for ubiquitination
            degradation and further regulates Colorectal Cancer proliferation
            and the cell cycle.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 156)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 156)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 156)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 156)
  AUTHORS   Jakel,S. and Gorlich,D.
  TITLE     Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear
            import of ribosomal proteins in mammalian cells
  JOURNAL   EMBO J 17 (15), 4491-4502 (1998)
   PUBMED   9687515
REFERENCE   7  (residues 1 to 156)
  AUTHORS   Fan,W., Christensen,M., Eichler,E., Zhang,X. and Lennon,G.
  TITLE     Cloning, sequencing, gene organization, and localization of the
            human ribosomal protein RPL23A gene
  JOURNAL   Genomics 46 (2), 234-239 (1997)
   PUBMED   9417910
REFERENCE   8  (residues 1 to 156)
  AUTHORS   Jiang,H., Lin,J.J., Tao,J. and Fisher,P.B.
  TITLE     Suppression of human ribosomal protein L23A expression during cell
            growth inhibition by interferon-beta
  JOURNAL   Oncogene 14 (4), 473-480 (1997)
   PUBMED   9053844
REFERENCE   9  (residues 1 to 156)
  AUTHORS   Fan,W., Cai,W., Parimoo,S., Schwarz,D.C., Lennon,G.G. and
            Weissman,S.M.
  TITLE     Identification of seven new human MHC class I region genes around
            the HLA-F locus
  JOURNAL   Immunogenetics 44 (2), 97-103 (1996)
   PUBMED   8662070
  REMARK    Erratum:[Immunogenetics 1997;46(2):169]
REFERENCE   10 (residues 1 to 156)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from U43701.1, BC058041.1, BE464375.1 and AC010761.10.
            
            On or before Apr 21, 2005 this sequence version replaced
            XP_208300.2, NP_000975.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L23P family of ribosomal proteins. It is located in the
            cytoplasm. The protein may be one of the target molecules involved
            in mediating growth inhibition by interferon. In yeast, the
            corresponding protein binds to a specific site on the 26S rRNA.
            This gene is co-transcribed with the U42A, U42B, U101A, and U101B
            small nucleolar RNA genes, which are located in its third, first,
            second, and fourth introns, respectively. As is typical for genes
            encoding ribosomal proteins, there are multiple processed
            pseudogenes of this gene dispersed through the genome. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.26679.1,
                                           SRR5189661.13134.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000422514.7/ ENSP00000389103.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..156
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..156
                     /product="large ribosomal subunit protein uL23"
                     /note="60S ribosomal protein L23a; melanoma
                     differentiation-associated gene 20"
                     /calculated_mol_wt=17564
     Region          1..67
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62750.1)"
     Site            2
                     /site_type="methylation"
                     /note="N,N,N-trimethylalanine.
                     /evidence=ECO:0000250|UniProtKB:P62751; propagated from
                     UniProtKB/Swiss-Prot (P62750.1)"
     Region          32..74
                     /region_name="Beta-like import receptor binding (BIB)
                     domain. /evidence=ECO:0000269|PubMed:9687515"
                     /note="propagated from UniProtKB/Swiss-Prot (P62750.1)"
     Region          36..156
                     /region_name="PTZ00191"
                     /note="60S ribosomal protein L23a; Provisional"
                     /db_xref="CDD:185507"
     Site            43
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P62750.1)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P62750.1)"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P62751; propagated from
                     UniProtKB/Swiss-Prot (P62750.1)"
     CDS             1..156
                     /gene="RPL23A"
                     /gene_synonym="L23A; MDA20; uL23"
                     /coded_by="NM_000984.6:22..492"
                     /db_xref="CCDS:CCDS11241.1"
                     /db_xref="GeneID:6147"
                     /db_xref="HGNC:HGNC:10317"
                     /db_xref="MIM:602326"
ORIGIN      
        1 mapkakkeap appkaeakak alkakkavlk gvhshkkkki rtsptfrrpk tlrlrrqpky
       61 prksaprrnk ldhyaiikfp lttesamkki ednntlvfiv dvkankhqik qavkklydid
      121 vakvntlirp dgekkayvrl apdydaldva nkigii
//
LOCUS       NP_001131026             182 aa            linear   PRI 20-NOV-2025
DEFINITION  malignant T-cell-amplified sequence 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001131026
VERSION     NP_001131026.1
DBSOURCE    REFSEQ: accession NM_001137554.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 182)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 182)
  AUTHORS   Bohlen,J., Zhou,Q., Philippot,Q., Ogishi,M., Rinchai,D.,
            Nieminen,T., Seyedpour,S., Parvaneh,N., Rezaei,N., Yazdanpanah,N.,
            Momenilandi,M., Conil,C., Neehus,A.L., Schmidt,C.,
            Arango-Franco,C.A., Voyer,T.L., Khan,T., Yang,R., Puchan,J.,
            Erazo,L., Roiuk,M., Vatovec,T., Janda,Z., Bagaric,I., Materna,M.,
            Gervais,A., Li,H., Rosain,J., Peel,J.N., Seeleuthner,Y., Han,J.E.,
            L'Honneur,A.S., Moncada-Velez,M., Martin-Fernandez,M., Horesh,M.E.,
            Kochetkov,T., Schmidt,M., AlShehri,M.A., Salo,E., Saxen,H.,
            ElGhazali,G., Yatim,A., Soudee,C., Sallusto,F., Ensser,A., Marr,N.,
            Zhang,P., Bogunovic,D., Cobat,A., Shahrooei,M., Beziat,V., Abel,L.,
            Wang,X., Boisson-Dupuis,S., Teleman,A.A., Bustamante,J., Zhang,Q.
            and Casanova,J.L.
  TITLE     Human MCTS1-dependent translation of JAK2 is essential for
            IFN-gamma immunity to mycobacteria
  JOURNAL   Cell 186 (23), 5114-5134 (2023)
   PUBMED   37875108
  REMARK    GeneRIF: Human MCTS1-dependent translation of JAK2 is essential for
            IFN-gamma immunity to mycobacteria.
REFERENCE   3  (residues 1 to 182)
  AUTHORS   Ma,B., Wei,X., Zhou,S. and Yang,M.
  TITLE     MCTS1 enhances the proliferation of laryngeal squamous cell
            carcinoma via promoting OTUD6B-1 mediated LIN28B deubiquitination
  JOURNAL   Biochem Biophys Res Commun 678, 128-134 (2023)
   PUBMED   37634410
  REMARK    GeneRIF: MCTS1 enhances the proliferation of laryngeal squamous
            cell carcinoma via promoting OTUD6B-1 mediated LIN28B
            deubiquitination.
REFERENCE   4  (residues 1 to 182)
  AUTHORS   Yang,M., Ma,B. and Liu,X.
  TITLE     MCTS1 promotes laryngeal squamous cell carcinoma cell growth via
            enhancing LARP7 stability
  JOURNAL   Clin Exp Pharmacol Physiol 49 (6), 652-660 (2022)
   PUBMED   35274760
  REMARK    GeneRIF: MCTS1 promotes laryngeal squamous cell carcinoma cell
            growth via enhancing LARP7 stability.
REFERENCE   5  (residues 1 to 182)
  AUTHORS   Zhu,J., Wang,X., Shao,Z., Sun,W. and Wu,T.
  TITLE     Prognostic value of malignant T cell-amplified sequence 1 in head
            and neck squamous cell carcinoma
  JOURNAL   Biomark Med 15 (17), 1623-1639 (2021)
   PUBMED   34704820
  REMARK    GeneRIF: Prognostic value of malignant T cell-amplified sequence 1
            in head and neck squamous cell carcinoma.
REFERENCE   6  (residues 1 to 182)
  AUTHORS   Stelzl,U., Worm,U., Lalowski,M., Haenig,C., Brembeck,F.H.,
            Goehler,H., Stroedicke,M., Zenkner,M., Schoenherr,A., Koeppen,S.,
            Timm,J., Mintzlaff,S., Abraham,C., Bock,N., Kietzmann,S.,
            Goedde,A., Toksoz,E., Droege,A., Krobitsch,S., Korn,B.,
            Birchmeier,W., Lehrach,H. and Wanker,E.E.
  TITLE     A human protein-protein interaction network: a resource for
            annotating the proteome
  JOURNAL   Cell 122 (6), 957-968 (2005)
   PUBMED   16169070
REFERENCE   7  (residues 1 to 182)
  AUTHORS   Shi,B., Levenson,V. and Gartenhaus,R.B.
  TITLE     Identification and characterization of a novel enhancer for the
            human MCT-1 oncogene promoter
  JOURNAL   J Cell Biochem 90 (1), 68-79 (2003)
   PUBMED   12938157
  REMARK    GeneRIF: demonstrated the presence of sequence-specific DNA-binding
            protein in nuclear extracts designated as LMBF; the 26-mer
            oligonucleotide containing the LMBF binding site is required for
            maximum transcriptional activity of the MCT-1 promoter
REFERENCE   8  (residues 1 to 182)
  AUTHORS   Shi,B., Hsu,H.L., Evens,A.M., Gordon,L.I. and Gartenhaus,R.B.
  TITLE     Expression of the candidate MCT-1 oncogene in B- and T-cell
            lymphoid malignancies
  JOURNAL   Blood 102 (1), 297-302 (2003)
   PUBMED   12637315
  REMARK    GeneRIF: tumor cell lines overexpressing MCT-1 exhibited increased
            growth rates and displayed increased protection against apoptosis
            induced by serum starvation
REFERENCE   9  (residues 1 to 182)
  AUTHORS   Herbert,G.B., Shi,B. and Gartenhaus,R.B.
  TITLE     Expression and stabilization of the MCT-1 protein by DNA damaging
            agents
  JOURNAL   Oncogene 20 (46), 6777-6783 (2001)
   PUBMED   11709712
REFERENCE   10 (residues 1 to 182)
  AUTHORS   Prosniak,M., Dierov,J., Okami,K., Tilton,B., Jameson,B.,
            Sawaya,B.E. and Gartenhaus,R.B.
  TITLE     A novel candidate oncogene, MCT-1, is involved in cell cycle
            progression
  JOURNAL   Cancer Res 58 (19), 4233-4237 (1998)
   PUBMED   9766643
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AA375691.1, AW957695.1, AK294834.1, AC011890.4 and BM671542.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at an
            alternate start codon, compared to variant 1. The encoded isoform
            (2) is longer and has a distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.134015.1,
                                           SRR1803616.76982.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..182
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq24"
     Protein         1..182
                     /product="malignant T-cell-amplified sequence 1 isoform 2"
                     /note="multiple copies T-cell malignancies; malignant
                     T-cell amplified sequence 1; multiple copies in T-cell
                     lymphoma-1"
                     /calculated_mol_wt=20419
     Region          5..81
                     /region_name="MCT1_N"
                     /note="N-terminal domain of multiple copies T cell
                     malignancies 1 and related proteins; cd11609"
                     /db_xref="CDD:211422"
     Site            order(33..34,72,74,78..81)
                     /site_type="other"
                     /note="PUA domain interface [polypeptide binding]"
                     /db_xref="CDD:211422"
     Region          81..176
                     /region_name="PUA_MCTS-1-like"
                     /note="PUA RNA-binding domain of malignant T
                     cell-amplified sequence 1 and related proteins; cd21155"
                     /db_xref="CDD:409297"
     Site            order(99,105,107..109,111..113,162..163,167..170)
                     /site_type="other"
                     /note="putative RNA binding site [nucleotide binding]"
                     /db_xref="CDD:409297"
     CDS             1..182
                     /gene="MCTS1"
                     /gene_synonym="IMD118; MCT-1; MCT1"
                     /coded_by="NM_001137554.2:156..704"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS48160.1"
                     /db_xref="GeneID:28985"
                     /db_xref="HGNC:HGNC:23357"
                     /db_xref="MIM:300587"
ORIGIN      
        1 mgkgrfdeke nvsnciqlkt svikgiknql ieqfpgiepw lnqimpkkdp vkivrchehi
       61 eiltvngell ffrqregpfy ptlrllhkyp filphqqvdk gaikfvlsga nimcpgltsp
      121 gaklypaavd tivaimaegk qhalcvgvmk msaediekvn kgigienihy lndglwhmkt
      181 yk
//
LOCUS       NP_001316601             194 aa            linear   PRI 20-NOV-2025
DEFINITION  arrestin domain-containing protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001316601
VERSION     NP_001316601.1
DBSOURCE    REFSEQ: accession NM_001329672.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Chen,M., Yin,B., Liu,Y., Li,M., Shen,S., Wu,J., Li,W. and Fan,J.
  TITLE     ARRDC3 regulates the targeted therapy sensitivity of clear cell
            renal cell carcinoma by promoting AXL degradation
  JOURNAL   Cell Cycle 23 (1), 56-69 (2024)
   PUBMED   38389126
  REMARK    GeneRIF: ARRDC3 regulates the targeted therapy sensitivity of clear
            cell renal cell carcinoma by promoting AXL degradation.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Long,M. and Wang,S.
  TITLE     Hsa_circ_0001740 mediates trophoblast cell function via regulating
            miR-188-3p/ARRDC3
  JOURNAL   Mol Reprod Dev 90 (6), 406-416 (2023)
   PUBMED   37436094
  REMARK    GeneRIF: Hsa_circ_0001740 mediates trophoblast cell function via
            regulating miR-188-3p/ARRDC3.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Huang,C.N., Huang,S.P., Pao,J.B., Chang,T.Y., Lan,Y.H., Lu,T.L.,
            Lee,H.Z., Juang,S.H., Wu,P.P., Pu,Y.S., Hsieh,C.J. and Bao,B.Y.
  TITLE     Genetic polymorphisms in androgen receptor-binding sites predict
            survival in prostate cancer patients receiving androgen-deprivation
            therapy
  JOURNAL   Ann Oncol 23 (3), 707-713 (2012)
   PUBMED   21652578
  REMARK    GeneRIF: single-nucleotide polymorphisms in ARRDC3, FLT1, and SKAP1
            were significant predictors for survival androgen-deprivation
            therapy in prostate cancer patients.
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Draheim,K.M., Chen,H.B., Tao,Q., Moore,N., Roche,M. and Lyle,S.
  TITLE     ARRDC3 suppresses breast cancer progression by negatively
            regulating integrin beta4
  JOURNAL   Oncogene 29 (36), 5032-5047 (2010)
   PUBMED   20603614
  REMARK    GeneRIF: ARRDC3 directly binds to a phosphorylated form of ITGbeta4
            leading to its internalization, ubiquitination and ultimate
            degradation, and suppress breast cancer progression.
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Nabhan,J.F., Pan,H. and Lu,Q.
  TITLE     Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase
            to mediate ubiquitination of the beta2-adrenergic receptor
  JOURNAL   EMBO Rep 11 (8), 605-611 (2010)
   PUBMED   20559325
  REMARK    GeneRIF: Data show that ARRDC3 interacts with NEDD4 through two
            conserved PPXY motifs and recruits NEDD4 to the activated
            beta2-adrenergic receptor.
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Patwari,P., Chutkow,W.A., Cummings,K., Verstraeten,V.L.,
            Lammerding,J., Schreiter,E.R. and Lee,R.T.
  TITLE     Thioredoxin-independent regulation of metabolism by the
            alpha-arrestin proteins
  JOURNAL   J Biol Chem 284 (37), 24996-25003 (2009)
   PUBMED   19605364
  REMARK    GeneRIF: Txnip regulates cellular metabolism independent of its
            binding to thioredoxin and the arrestin domains are crucial
            structural elements in metabolic functions of alpha-arrestin
            proteins
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Oka,S., Masutani,H., Liu,W., Horita,H., Wang,D., Kizaka-Kondoh,S.
            and Yodoi,J.
  TITLE     Thioredoxin-binding protein-2-like inducible membrane protein is a
            novel vitamin D3 and peroxisome proliferator-activated receptor
            (PPAR)gamma ligand target protein that regulates PPARgamma
            signaling
  JOURNAL   Endocrinology 147 (2), 733-743 (2006)
   PUBMED   16269462
  REMARK    GeneRIF: [Thioredoxin-binding protein-2-like inducible membrane
            protein, TLIMP] TLIMP, a novel VD3- or PPARgamma ligand-inducible
            membrane-associated protein, plays a regulatory role in cell
            proliferation and PPARgamma activation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008799.6.
            
            Summary: This gene encodes a member of the arrestin family of
            proteins, which regulate G protein-mediated signaling. The encoded
            protein is thought to act as a regulator of breast cancer growth
            and progression by binding to a phosphorylated form of integrin
            beta4, a tumor-related antigen, targeting the integrin for
            internalization and degradation. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: Variants 2, 3 and 4 encode the same isoform
            (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853566.22500.1,
                                           SRR11853564.22265.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..194
                     /product="arrestin domain-containing protein 3 isoform b"
                     /note="TBP-2-like inducible membrane protein;
                     alpha-arrestin 3"
                     /calculated_mol_wt=21418
     Region          <5..94
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     smart01017"
                     /db_xref="CDD:214976"
     CDS             1..194
                     /gene="ARRDC3"
                     /gene_synonym="TLIMP"
                     /coded_by="NM_001329672.2:738..1322"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="GeneID:57561"
                     /db_xref="HGNC:HGNC:29263"
                     /db_xref="MIM:612464"
ORIGIN      
        1 mvvpkaaiyq tqafyakgkm kevkqlvanl rgeslssgkt etwngkllki ppvspsildc
       61 siirveyslm vyvdipgamd lflnlplvig tiplhpfgsr tssvssqcsm nmnwlslslp
      121 erpeappsya evvteeqrrn nlapvsacdd feralqgplf ayiqefrflp pplyseidpn
      181 pdqsaddrps cpsr
//
LOCUS       NP_001316599             194 aa            linear   PRI 20-NOV-2025
DEFINITION  arrestin domain-containing protein 3 isoform b [Homo sapiens].
ACCESSION   NP_001316599
VERSION     NP_001316599.1
DBSOURCE    REFSEQ: accession NM_001329670.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 194)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 194)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 194)
  AUTHORS   Chen,M., Yin,B., Liu,Y., Li,M., Shen,S., Wu,J., Li,W. and Fan,J.
  TITLE     ARRDC3 regulates the targeted therapy sensitivity of clear cell
            renal cell carcinoma by promoting AXL degradation
  JOURNAL   Cell Cycle 23 (1), 56-69 (2024)
   PUBMED   38389126
  REMARK    GeneRIF: ARRDC3 regulates the targeted therapy sensitivity of clear
            cell renal cell carcinoma by promoting AXL degradation.
REFERENCE   4  (residues 1 to 194)
  AUTHORS   Long,M. and Wang,S.
  TITLE     Hsa_circ_0001740 mediates trophoblast cell function via regulating
            miR-188-3p/ARRDC3
  JOURNAL   Mol Reprod Dev 90 (6), 406-416 (2023)
   PUBMED   37436094
  REMARK    GeneRIF: Hsa_circ_0001740 mediates trophoblast cell function via
            regulating miR-188-3p/ARRDC3.
REFERENCE   5  (residues 1 to 194)
  AUTHORS   Huang,C.N., Huang,S.P., Pao,J.B., Chang,T.Y., Lan,Y.H., Lu,T.L.,
            Lee,H.Z., Juang,S.H., Wu,P.P., Pu,Y.S., Hsieh,C.J. and Bao,B.Y.
  TITLE     Genetic polymorphisms in androgen receptor-binding sites predict
            survival in prostate cancer patients receiving androgen-deprivation
            therapy
  JOURNAL   Ann Oncol 23 (3), 707-713 (2012)
   PUBMED   21652578
  REMARK    GeneRIF: single-nucleotide polymorphisms in ARRDC3, FLT1, and SKAP1
            were significant predictors for survival androgen-deprivation
            therapy in prostate cancer patients.
REFERENCE   6  (residues 1 to 194)
  AUTHORS   Davis,O.S., Butcher,L.M., Docherty,S.J., Meaburn,E.L., Curtis,C.J.,
            Simpson,M.A., Schalkwyk,L.C. and Plomin,R.
  TITLE     A three-stage genome-wide association study of general cognitive
            ability: hunting the small effects
  JOURNAL   Behav Genet 40 (6), 759-767 (2010)
   PUBMED   20306291
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
REFERENCE   7  (residues 1 to 194)
  AUTHORS   Draheim,K.M., Chen,H.B., Tao,Q., Moore,N., Roche,M. and Lyle,S.
  TITLE     ARRDC3 suppresses breast cancer progression by negatively
            regulating integrin beta4
  JOURNAL   Oncogene 29 (36), 5032-5047 (2010)
   PUBMED   20603614
  REMARK    GeneRIF: ARRDC3 directly binds to a phosphorylated form of ITGbeta4
            leading to its internalization, ubiquitination and ultimate
            degradation, and suppress breast cancer progression.
REFERENCE   8  (residues 1 to 194)
  AUTHORS   Nabhan,J.F., Pan,H. and Lu,Q.
  TITLE     Arrestin domain-containing protein 3 recruits the NEDD4 E3 ligase
            to mediate ubiquitination of the beta2-adrenergic receptor
  JOURNAL   EMBO Rep 11 (8), 605-611 (2010)
   PUBMED   20559325
  REMARK    GeneRIF: Data show that ARRDC3 interacts with NEDD4 through two
            conserved PPXY motifs and recruits NEDD4 to the activated
            beta2-adrenergic receptor.
REFERENCE   9  (residues 1 to 194)
  AUTHORS   Patwari,P., Chutkow,W.A., Cummings,K., Verstraeten,V.L.,
            Lammerding,J., Schreiter,E.R. and Lee,R.T.
  TITLE     Thioredoxin-independent regulation of metabolism by the
            alpha-arrestin proteins
  JOURNAL   J Biol Chem 284 (37), 24996-25003 (2009)
   PUBMED   19605364
  REMARK    GeneRIF: Txnip regulates cellular metabolism independent of its
            binding to thioredoxin and the arrestin domains are crucial
            structural elements in metabolic functions of alpha-arrestin
            proteins
REFERENCE   10 (residues 1 to 194)
  AUTHORS   Oka,S., Masutani,H., Liu,W., Horita,H., Wang,D., Kizaka-Kondoh,S.
            and Yodoi,J.
  TITLE     Thioredoxin-binding protein-2-like inducible membrane protein is a
            novel vitamin D3 and peroxisome proliferator-activated receptor
            (PPAR)gamma ligand target protein that regulates PPARgamma
            signaling
  JOURNAL   Endocrinology 147 (2), 733-743 (2006)
   PUBMED   16269462
  REMARK    GeneRIF: [Thioredoxin-binding protein-2-like inducible membrane
            protein, TLIMP] TLIMP, a novel VD3- or PPARgamma ligand-inducible
            membrane-associated protein, plays a regulatory role in cell
            proliferation and PPARgamma activation.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008799.6.
            
            Summary: This gene encodes a member of the arrestin family of
            proteins, which regulate G protein-mediated signaling. The encoded
            protein is thought to act as a regulator of breast cancer growth
            and progression by binding to a phosphorylated form of integrin
            beta4, a tumor-related antigen, targeting the integrin for
            internalization and degradation. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: Variants 2, 3 and 4 encode the same isoform
            (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.1795576.1,
                                           SRR14372080.2357320.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.3"
     Protein         1..194
                     /product="arrestin domain-containing protein 3 isoform b"
                     /note="TBP-2-like inducible membrane protein;
                     alpha-arrestin 3"
                     /calculated_mol_wt=21418
     Region          <5..94
                     /region_name="Arrestin_C"
                     /note="Arrestin (or S-antigen), C-terminal domain;
                     smart01017"
                     /db_xref="CDD:214976"
     CDS             1..194
                     /gene="ARRDC3"
                     /gene_synonym="TLIMP"
                     /coded_by="NM_001329670.2:1031..1615"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:57561"
                     /db_xref="HGNC:HGNC:29263"
                     /db_xref="MIM:612464"
ORIGIN      
        1 mvvpkaaiyq tqafyakgkm kevkqlvanl rgeslssgkt etwngkllki ppvspsildc
       61 siirveyslm vyvdipgamd lflnlplvig tiplhpfgsr tssvssqcsm nmnwlslslp
      121 erpeappsya evvteeqrrn nlapvsacdd feralqgplf ayiqefrflp pplyseidpn
      181 pdqsaddrps cpsr
//
LOCUS       NP_001349447             505 aa            linear   PRI 20-NOV-2025
DEFINITION  rab proteins geranylgeranyltransferase component A 1 isoform c
            [Homo sapiens].
ACCESSION   NP_001349447 XP_016884733
VERSION     NP_001349447.1
DBSOURCE    REFSEQ: accession NM_001362518.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 505)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 505)
  AUTHORS   Sarkar,H., Tracey-White,D., Hagag,A.M., Burgoyne,T., Nair,N.,
            Jensen,L.D., Edwards,M.M. and Moosajee,M.
  TITLE     Loss of REP1 impacts choroidal melanogenesis and vasculogenesis in
            choroideremia
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (2), 166963 (2024)
   PUBMED   37989423
  REMARK    GeneRIF: Loss of REP1 impacts choroidal melanogenesis and
            vasculogenesis in choroideremia.
REFERENCE   3  (residues 1 to 505)
  AUTHORS   Iwagawa,T., Masumoto,H., Tabuchi,H., Tani,K., Conklin,B.R. and
            Watanabe,S.
  TITLE     Evaluation of CRISPR/Cas9 exon-skipping vector for choroideremia
            using human induced pluripotent stem cell-derived RPE
  JOURNAL   J Gene Med 25 (2), e3464 (2023)
   PUBMED   36413603
  REMARK    GeneRIF: Evaluation of CRISPR/Cas9 exon-skipping vector for
            choroideremia using human induced pluripotent stem cell-derived
            RPE.
REFERENCE   4  (residues 1 to 505)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 505)
  AUTHORS   van Bokhoven,H., van den Hurk,J.A., Bogerd,L., Philippe,C.,
            Gilgenkrantz,S., de Jong,P., Ropers,H.H. and Cremers,F.P.
  TITLE     Cloning and characterization of the human choroideremia gene
  JOURNAL   Hum Mol Genet 3 (7), 1041-1046 (1994)
   PUBMED   7981670
REFERENCE   6  (residues 1 to 505)
  AUTHORS   MacDonald,I.M., Hume,S., Zhai,Y. and Xu,M.
  TITLE     Choroideremia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301511
REFERENCE   7  (residues 1 to 505)
  AUTHORS   van den Hurk,J.A., van de Pol,T.J., Molloy,C.M., Brunsmann,F.,
            Ruther,K., Zrenner,E., Pinckers,A.J., Pawlowitzki,I.H.,
            Bleeker-Wagemakers,E.M., Wieringa,B. et al.
  TITLE     Detection and characterization of point mutations in the
            choroideremia candidate gene by PCR-SSCP analysis and direct DNA
            sequencing
  JOURNAL   Am J Hum Genet 50 (6), 1195-1202 (1992)
   PUBMED   1598901
REFERENCE   8  (residues 1 to 505)
  AUTHORS   Sankila,E.M., Tolvanen,R., van den Hurk,J.A., Cremers,F.P. and de
            la Chapelle,A.
  TITLE     Aberrant splicing of the CHM gene is a significant cause of
            choroideremia
  JOURNAL   Nat Genet 1 (2), 109-113 (1992)
   PUBMED   1302003
REFERENCE   9  (residues 1 to 505)
  AUTHORS   Molloy,C.M., van de Pol,T.J., Brohet,R.M., Ropers,H.H. and
            Cremers,F.P.
  TITLE     Three RFLPs for pZ11 (DXS540) in the choroideremia gene at Xq21.2
  JOURNAL   Nucleic Acids Res 20 (6), 1434 (1992)
   PUBMED   1373238
REFERENCE   10 (residues 1 to 505)
  AUTHORS   Merry,D.E., Janne,P.A., Landers,J.E., Lewis,R.A. and Nussbaum,R.L.
  TITLE     Isolation of a candidate gene for choroideremia
  JOURNAL   Proc Natl Acad Sci U S A 89 (6), 2135-2139 (1992)
   PUBMED   1549574
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL035451.6, AL009175.2 and
            AL022401.2.
            
            On Apr 20, 2018 this sequence version replaced XP_016884733.1.
            
            Summary: This gene encodes component A of the RAB geranylgeranyl
            transferase holoenzyme. In the dimeric holoenzyme, this subunit
            binds unprenylated Rab GTPases and then presents them to the
            catalytic Rab GGTase subunit for the geranylgeranyl transfer
            reaction. Rab GTPases need to be geranylgeranyled on either one or
            two cysteine residues in their C-terminus to localize to the
            correct intracellular membrane. Mutations in this gene are a cause
            of choroideremia; also known as tapetochoroidal dystrophy (TCD).
            This X-linked disease is characterized by progressive dystrophy of
            the choroid, retinal pigment epithelium and retina. Alternatively
            spliced transcript variants have been found for this gene.
            [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (5) contains an alternate 5'
            terminal exon and 5' splice site, which results in translation
            initiation at an in-frame downstream start codon compared to
            variant 1. The resulting isoform (c) has a shorter N-terminus
            compared to isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.104018.1,
                                           SRR18074969.103226.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..505
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq21.2"
     Protein         1..505
                     /product="rab proteins geranylgeranyltransferase component
                     A 1 isoform c"
                     /note="rab proteins geranylgeranyltransferase component A
                     1; choroideremia (Rab escort protein 1); CHM, Rab escort
                     protein 1"
                     /calculated_mol_wt=57134
     Region          77..394
                     /region_name="Rossmann-fold NAD(P)(+)-binding proteins"
                     /note="A large family of proteins that share a
                     Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The
                     NADB domain is found in numerous dehydrogenases of
                     metabolic pathways such as glycolysis, and many other
                     redox enzymes. NAD binding involves numerous...; cl21454"
                     /db_xref="CDD:473865"
     CDS             1..505
                     /gene="CHM"
                     /gene_synonym="DXS540; GGTA; HSD-32; REP-1; TCD"
                     /coded_by="NM_001362518.2:452..1969"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="GeneID:1121"
                     /db_xref="HGNC:HGNC:1940"
                     /db_xref="MIM:300390"
ORIGIN      
        1 mscemlteqt pssdpenale vngaevtgek enhcddktcv pstsaedmse nvpiaedtte
       61 qpkknritys qiikegrrfn idlvskllys rgllidllik snvsryaefk nitrilafre
      121 grveqvpcsr advfnskqlt mvekrmlmkf ltfcmeyeky pdeykgyeei tfyeylktqk
      181 ltpnlqyivm hsiamtseta sstidglkat knflhclgry gntpflfply gqgelpqcfc
      241 rmcavfggiy clrhsvqclv vdkesrkcka iidqfgqrii sehflvedsy fpenmcsrvq
      301 yrqisravli tdrsvlktds dqqisiltvp aeepgtfavr vielcsstmt cmkgtylvhl
      361 tctssktare dlesvvqklf vpytemeien eqvekprilw alyfnmrdss disrscyndl
      421 psnvyvcsgp dcglgndnav kqaetlfqei cpnedfcppp pnpediildg dslqpeases
      481 saipeanset fkestnlgnl eesse
//
LOCUS       NP_055184                460 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 18 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055184
VERSION     NP_055184.2
DBSOURCE    REFSEQ: accession NM_014369.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Zhou,Z., Yu,W., Li,H., Shi,J., Meng,S., Yan,Y., Chen,R., Liu,H.,
            Wang,J., Sun,J., Xiao,Z. and Zhang,J.
  TITLE     Hepatitis B Virus X Protein Represses Expression of Tumor
            Suppressor PTPN18 in Hepatocellular Carcinoma
  JOURNAL   Mol Cancer Res 22 (9), 891-901 (2024)
   PUBMED   38787319
  REMARK    GeneRIF: Hepatitis B Virus X Protein Represses Expression of Tumor
            Suppressor PTPN18 in Hepatocellular Carcinoma.
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Wang,T., Yu,Y., Ba,X., Zhang,X., Zhang,N., Wang,G., Bai,B., Li,T.,
            Zhao,J., Zhao,Y. and Wang,B.
  TITLE     PTPN18 Serves as a Potential Oncogene for Glioblastoma by Enhancing
            Immune Suppression
  JOURNAL   Oxid Med Cell Longev 2023, 2994316 (2023)
   PUBMED   36846716
  REMARK    GeneRIF: PTPN18 Serves as a Potential Oncogene for Glioblastoma by
            Enhancing Immune Suppression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Manso,J.A., Marcos,T., Ruiz-Martin,V., Casas,J., Alcon,P., Sanchez
            Crespo,M., Bayon,Y., de Pereda,J.M. and Alonso,A.
  TITLE     PSTPIP1-LYP phosphatase interaction: structural basis and
            implications for autoinflammatory disorders
  JOURNAL   Cell Mol Life Sci 79 (2), 131 (2022)
   PUBMED   35152348
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Held,M.A., Greenfest-Allen,E., Su,S., Stoeckert,C.J., Stokes,M.P.
            and Wojchowski,D.M.
  TITLE     Phospho-PTM proteomic discovery of novel EPO- modulated kinases and
            phosphatases, including PTPN18 as a positive regulator of EPOR/JAK2
            Signaling
  JOURNAL   Cell Signal 69, 109554 (2020)
   PUBMED   32027948
  REMARK    GeneRIF: Phospho-PTM proteomic discovery of novel EPO- modulated
            kinases and phosphatases, including PTPN18 as a positive regulator
            of EPOR/JAK2 Signaling.
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Blanchetot,C., Chagnon,M., Dube,N., Halle,M. and Tremblay,M.L.
  TITLE     Substrate-trapping techniques in the identification of cellular PTP
            targets
  JOURNAL   Methods 35 (1), 44-53 (2005)
   PUBMED   15588985
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Gandhi,T.K., Chandran,S., Peri,S., Saravana,R., Amanchy,R.,
            Prasad,T.S. and Pandey,A.
  TITLE     A bioinformatics analysis of protein tyrosine phosphatases in
            humans
  JOURNAL   DNA Res 12 (2), 79-89 (2005)
   PUBMED   16303740
  REMARK    GeneRIF: novel isoform of PTPN18 based on analysis of expressed
            sequence tags was discovered; deletion of 4 exons in the catalytic
            domain of the isoform may alter enzymatic activity; 2 of the novel
            isoform predictions were experimentally validated through RT-PCR
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Gensler,M., Buschbeck,M. and Ullrich,A.
  TITLE     Negative regulation of HER2 signaling by the PEST-type
            protein-tyrosine phosphatase BDP1
  JOURNAL   J Biol Chem 279 (13), 12110-12116 (2004)
   PUBMED   14660651
  REMARK    GeneRIF: BDP1 has a role in negative regulation of HER2 signaling
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Wang,B., Lemay,S., Tsai,S. and Veillette,A.
  TITLE     SH2 domain-mediated interaction of inhibitory protein tyrosine
            kinase Csk with protein tyrosine phosphatase-HSCF
  JOURNAL   Mol Cell Biol 21 (4), 1077-1088 (2001)
   PUBMED   11158295
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Kim,Y.W., Wang,H., Sures,I., Lammers,R., Martell,K.J. and
            Ullrich,A.
  TITLE     Characterization of the PEST family protein tyrosine phosphatase
            BDP1
  JOURNAL   Oncogene 13 (10), 2275-2279 (1996)
   PUBMED   8950995
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DN995571.1, X79568.1,
            AK303804.1, AC132479.2, BM789073.1 and CA310199.1.
            
            On Jan 25, 2002 this sequence version replaced NP_055184.1.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, the mitotic cycle, and
            oncogenic transformation. This PTP contains a PEST motif, which
            often serves as a protein-protein interaction domain, and may be
            related to protein intracellular half-live. This protein can
            differentially dephosphorylate autophosphorylated tyrosine kinases
            that are overexpressed in tumor tissues, and it appears to regulate
            HER2, a member of the epidermal growth factor receptor family of
            receptor tyrosine kinases. Two transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Nov 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X79568.1, SRR1163658.227597.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000175756.10/ ENSP00000175756.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..460
                     /product="tyrosine-protein phosphatase non-receptor type
                     18 isoform 1"
                     /EC_number="3.1.3.48"
                     /note="brain-derived phosphatase; tyrosine-protein
                     phosphatase non-receptor type 18; protein tyrosine
                     phosphatase, non-receptor type 18 (brain-derived)"
                     /calculated_mol_wt=50351
     Region          27..292
                     /region_name="PTPc-N18"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 18; cd14603"
                     /db_xref="CDD:350451"
     Region          361..460
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99952.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61152; propagated from
                     UniProtKB/Swiss-Prot (Q99952.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99952.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q61152; propagated from
                     UniProtKB/Swiss-Prot (Q99952.2)"
     CDS             1..460
                     /gene="PTPN18"
                     /gene_synonym="BDP1; PTP-HSCF"
                     /coded_by="NM_014369.4:53..1435"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2161.1"
                     /db_xref="GeneID:26469"
                     /db_xref="HGNC:HGNC:9649"
                     /db_xref="MIM:606587"
ORIGIN      
        1 msrsldsars flerleargg regavlagef sdiqacsaaw kadgvcstva gsrpenvrkn
       61 rykdvlpydq trvilsllqe eghsdyingn firgvdgsla yiatqgplph tlldfwrlvw
      121 efgvkvilma creiengrkr cerywaqeqe plqtglfcit likekwlned imlrtlkvtf
      181 qkesrsvyql qymswpdrgv psspdhmlam veearrlqgs gpeplcvhcs agcgrtgvlc
      241 tvdyvrqlll tqmippdfsl fdvvlkmrkq rpaavqteeq yrflyhtvaq mfcstlqnas
      301 phyqnikenc aplyddalfl rtpqallaip rppggvlrsi svpgspgham adtyavvqkr
      361 gapagagsgt qtgtgtgtga rsaeeaplys kvtpraqrpg ahaedargtl pgrvpadqsp
      421 agsgayedva ggaqtgglgf nlrigrpkgp rdppaewtrv
//
LOCUS       NP_001275710             531 aa            linear   PRI 20-NOV-2025
DEFINITION  tetratricopeptide repeat protein 8 isoform D [Homo sapiens].
ACCESSION   NP_001275710
VERSION     NP_001275710.1
DBSOURCE    REFSEQ: accession NM_001288781.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 531)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 531)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 531)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 531)
  AUTHORS   Ullah,A., Umair,M., Yousaf,M., Khan,S.A., Nazim-Ud-Din,M., Shah,K.,
            Ahmad,F., Azeem,Z., Ali,G., Alhaddad,B., Rafique,A., Jan,A.,
            Haack,T.B., Strom,T.M., Meitinger,T., Ghous,T. and Ahmad,W.
  TITLE     Sequence variants in four genes underlying Bardet-Biedl syndrome in
            consanguineous families
  JOURNAL   Mol Vis 23, 482-494 (2017)
   PUBMED   28761321
  REMARK    GeneRIF: Two novel mutations and three previously reported
            variants, identified in the present study, further extend the body
            of evidence implicating BBS6, BBS7, BBS8, and BBS10 in causing
            Bardet-Biedl Syndrome.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 531)
  AUTHORS   Nachury,M.V., Loktev,A.V., Zhang,Q., Westlake,C.J., Peranen,J.,
            Merdes,A., Slusarski,D.C., Scheller,R.H., Bazan,J.F.,
            Sheffield,V.C. and Jackson,P.K.
  TITLE     A core complex of BBS proteins cooperates with the GTPase Rab8 to
            promote ciliary membrane biogenesis
  JOURNAL   Cell 129 (6), 1201-1213 (2007)
   PUBMED   17574030
REFERENCE   6  (residues 1 to 531)
  AUTHORS   Badano,J.L., Leitch,C.C., Ansley,S.J., May-Simera,H., Lawson,S.,
            Lewis,R.A., Beales,P.L., Dietz,H.C., Fisher,S. and Katsanis,N.
  TITLE     Dissection of epistasis in oligogenic Bardet-Biedl syndrome
  JOURNAL   Nature 439 (7074), 326-330 (2006)
   PUBMED   16327777
REFERENCE   7  (residues 1 to 531)
  AUTHORS   Ansley,S.J., Badano,J.L., Blacque,O.E., Hill,J., Hoskins,B.E.,
            Leitch,C.C., Kim,J.C., Ross,A.J., Eichers,E.R., Teslovich,T.M.,
            Mah,A.K., Johnsen,R.C., Cavender,J.C., Lewis,R.A., Leroux,M.R.,
            Beales,P.L. and Katsanis,N.
  TITLE     Basal body dysfunction is a likely cause of pleiotropic
            Bardet-Biedl syndrome
  JOURNAL   Nature 425 (6958), 628-633 (2003)
   PUBMED   14520415
  REMARK    GeneRIF: A homozygous null BBS8 mutation leads to Bardet-Biedl
            syndrome with randomization of left-right body axis symmetry, a
            known defect of the nodal cilium
REFERENCE   8  (residues 1 to 531)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   9  (residues 1 to 531)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
REFERENCE   10 (residues 1 to 531)
  AUTHORS   Forsyth,R. and Gunay-Aygun,M.
  TITLE     Bardet-Biedl Syndrome Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301537
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX247959.1, BC026351.1 and
            BU738965.1.
            
            Summary: This gene encodes a protein that has been directly linked
            to Bardet-Biedl syndrome. The primary features of this syndrome
            include retinal dystrophy, obesity, polydactyly, renal
            abnormalities and learning disabilities. Experimentation in
            non-human eukaryotes suggests that this gene is expressed in
            ciliated cells and that it is involved in the formation of cilia. A
            mutation in this gene has also been implicated in nonsyndromic
            retinitis pigmentosa. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (4) includes an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            encoded isoform (D) is longer, compared to isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC026351.1, SRR1803615.169262.1
                                    [ECO:0000331]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..531
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q31.3"
     Protein         1..531
                     /product="tetratricopeptide repeat protein 8 isoform D"
                     /note="Bardet-Biedl syndrome type 8; TPR repeat protein 8"
                     /calculated_mol_wt=60261
     Region          30..169
                     /region_name="TTC8_N"
                     /note="N-terminal domain of tetratricopeptide repeat
                     domain 8; cd21341"
                     /db_xref="CDD:411061"
     Region          108..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          241..274
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Site            order(246,249..250,252,275,278..279,282..283,285..286,309,
                     312..313,316..317,320)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          246..269
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          248..527
                     /region_name="LapB"
                     /note="Lipopolysaccharide biosynthesis regulator
                     YciM/LapB, contains six TPR domains and a C-terminal
                     metal-binding domain [Cell wall/membrane/envelope
                     biogenesis]; COG2956"
                     /db_xref="CDD:442196"
     Region          273..303
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          275..307
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          308..341
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          308..336
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          342..375
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          342..370
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          376..409
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Site            order(377,380..381,384..385,387,414,417..418,421..422,
                     424..425,448,451..452,455..456,459)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          377..404
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          409..442
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          413..446
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          447..480
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAM2.2)"
     Region          447..473
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          481..506
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..531
                     /gene="TTC8"
                     /gene_synonym="BBS8; RP51"
                     /coded_by="NM_001288781.1:197..1792"
                     /note="isoform D is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS73674.1"
                     /db_xref="GeneID:123016"
                     /db_xref="HGNC:HGNC:20087"
                     /db_xref="MIM:608132"
ORIGIN      
        1 mssemeplll awsyfrrrkf qlcadlctqm lekspydqaa wilkaralte mvyideidvd
       61 qegiaemmld enaiaqvprp gtslklpgtn qtggpsqavr pitqagrpit gflrpstqsg
      121 rpgtmeqair tprtaytarp itsssgrfvr lgtasmltsp dgpfinlsrl nltkysqkpk
      181 lakalfeyif hhendvktih ledvvlhlgi ypfllrnknh ieknaldlaa lstehsqykd
      241 wwwkvqigkc yyrlgmyrea ekqfksalkq qemvdtflyl akvyvsldqp vtalnlfkqg
      301 ldkfpgevtl lcgiariyee mnnmssaaey ykevlkqdnt hveaiacigs nhfysdqpei
      361 alrfyrrllq mgiyngqlfn nlglccfyaq qydmtltsfe ralslaenee eaadvwynlg
      421 hvavgigdtn lahqcfrlal vnnnnhaeay nnlavlemrk ghveqarall qtasslaphm
      481 yephfnfati sdkigdlqrs yvaaqkseaa fpdhvdtqhl ikqlrqhfam l
//
LOCUS       NP_001278936             437 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 8 isoform 3 [Homo sapiens].
ACCESSION   NP_001278936 XP_005263210
VERSION     NP_001278936.1
DBSOURCE    REFSEQ: accession NM_001292007.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Mena,E.L., Kjolby,R.A.S., Saxton,R.A., Werner,A., Lew,B.G.,
            Boyle,J.M., Harland,R. and Rape,M.
  TITLE     Dimerization quality control ensures neuronal development and
            survival
  JOURNAL   Science 362 (6411) (2018)
   PUBMED   30190310
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Bennett,E.J., Rush,J., Gygi,S.P. and Harper,J.W.
  TITLE     Dynamics of cullin-RING ubiquitin ligase network revealed by
            systematic quantitative proteomics
  JOURNAL   Cell 143 (6), 951-965 (2010)
   PUBMED   21145461
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Flachsbart,F., Franke,A., Kleindorp,R., Caliebe,A., Blanche,H.,
            Schreiber,S. and Nebel,A.
  TITLE     Investigation of genetic susceptibility factors for human longevity
            - a targeted nonsynonymous SNP study
  JOURNAL   Mutat Res 694 (1-2), 13-19 (2010)
   PUBMED   20800603
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Teslovich,T.M., Musunuru,K., Smith,A.V., Edmondson,A.C.,
            Stylianou,I.M., Koseki,M., Pirruccello,J.P., Ripatti,S.,
            Chasman,D.I., Willer,C.J., Johansen,C.T., Fouchier,S.W., Isaacs,A.,
            Peloso,G.M., Barbalic,M., Ricketts,S.L., Bis,J.C., Aulchenko,Y.S.,
            Thorleifsson,G., Feitosa,M.F., Chambers,J., Orho-Melander,M.,
            Melander,O., Johnson,T., Li,X., Guo,X., Li,M., Shin Cho,Y., Jin
            Go,M., Jin Kim,Y., Lee,J.Y., Park,T., Kim,K., Sim,X., Twee-Hee
            Ong,R., Croteau-Chonka,D.C., Lange,L.A., Smith,J.D., Song,K., Hua
            Zhao,J., Yuan,X., Luan,J., Lamina,C., Ziegler,A., Zhang,W.,
            Zee,R.Y., Wright,A.F., Witteman,J.C., Wilson,J.F., Willemsen,G.,
            Wichmann,H.E., Whitfield,J.B., Waterworth,D.M., Wareham,N.J.,
            Waeber,G., Vollenweider,P., Voight,B.F., Vitart,V.,
            Uitterlinden,A.G., Uda,M., Tuomilehto,J., Thompson,J.R., Tanaka,T.,
            Surakka,I., Stringham,H.M., Spector,T.D., Soranzo,N., Smit,J.H.,
            Sinisalo,J., Silander,K., Sijbrands,E.J., Scuteri,A., Scott,J.,
            Schlessinger,D., Sanna,S., Salomaa,V., Saharinen,J., Sabatti,C.,
            Ruokonen,A., Rudan,I., Rose,L.M., Roberts,R., Rieder,M.,
            Psaty,B.M., Pramstaller,P.P., Pichler,I., Perola,M., Penninx,B.W.,
            Pedersen,N.L., Pattaro,C., Parker,A.N., Pare,G., Oostra,B.A.,
            O'Donnell,C.J., Nieminen,M.S., Nickerson,D.A., Montgomery,G.W.,
            Meitinger,T., McPherson,R., McCarthy,M.I., McArdle,W., Masson,D.,
            Martin,N.G., Marroni,F., Mangino,M., Magnusson,P.K., Lucas,G.,
            Luben,R., Loos,R.J., Lokki,M.L., Lettre,G., Langenberg,C.,
            Launer,L.J., Lakatta,E.G., Laaksonen,R., Kyvik,K.O., Kronenberg,F.,
            Konig,I.R., Khaw,K.T., Kaprio,J., Kaplan,L.M., Johansson,A.,
            Jarvelin,M.R., Janssens,A.C., Ingelsson,E., Igl,W., Kees
            Hovingh,G., Hottenga,J.J., Hofman,A., Hicks,A.A., Hengstenberg,C.,
            Heid,I.M., Hayward,C., Havulinna,A.S., Hastie,N.D., Harris,T.B.,
            Haritunians,T., Hall,A.S., Gyllensten,U., Guiducci,C., Groop,L.C.,
            Gonzalez,E., Gieger,C., Freimer,N.B., Ferrucci,L., Erdmann,J.,
            Elliott,P., Ejebe,K.G., Doring,A., Dominiczak,A.F., Demissie,S.,
            Deloukas,P., de Geus,E.J., de Faire,U., Crawford,G., Collins,F.S.,
            Chen,Y.D., Caulfield,M.J., Campbell,H., Burtt,N.P.,
            Bonnycastle,L.L., Boomsma,D.I., Boekholdt,S.M., Bergman,R.N.,
            Barroso,I., Bandinelli,S., Ballantyne,C.M., Assimes,T.L.,
            Quertermous,T., Altshuler,D., Seielstad,M., Wong,T.Y., Tai,E.S.,
            Feranil,A.B., Kuzawa,C.W., Adair,L.S., Taylor,H.A. Jr.,
            Borecki,I.B., Gabriel,S.B., Wilson,J.G., Holm,H.,
            Thorsteinsdottir,U., Gudnason,V., Krauss,R.M., Mohlke,K.L.,
            Ordovas,J.M., Munroe,P.B., Kooner,J.S., Tall,A.R., Hegele,R.A.,
            Kastelein,J.J., Schadt,E.E., Rotter,J.I., Boerwinkle,E.,
            Strachan,D.P., Mooser,V., Stefansson,K., Reilly,M.P., Samani,N.J.,
            Schunkert,H., Cupples,L.A., Sandhu,M.S., Ridker,P.M., Rader,D.J.,
            van Duijn,C.M., Peltonen,L., Abecasis,G.R., Boehnke,M. and
            Kathiresan,S.
  TITLE     Biological, clinical and population relevance of 95 loci for blood
            lipids
  JOURNAL   Nature 466 (7307), 707-713 (2010)
   PUBMED   20686565
REFERENCE   9  (residues 1 to 437)
  AUTHORS   Nam,S., Min,K., Hwang,H., Lee,H.O., Lee,J.H., Yoon,J., Lee,H.,
            Park,S. and Lee,J.
  TITLE     Control of rapsyn stability by the CUL-3-containing E3 ligase
            complex
  JOURNAL   J Biol Chem 284 (12), 8195-8206 (2009)
   PUBMED   19158078
REFERENCE   10 (residues 1 to 437)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092658.2, CN290430.1, BX640744.1, CR749265.1, BX647454.1,
            BX538173.1 and AA878129.1.
            
            On May 15, 2014 this sequence version replaced XP_005263210.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            lacks an alternate in-frame exon in the 5' coding region, compared
            to variant 1. It encodes isoform 3, which lacks an internal segment
            and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749265.1, SRR1660803.78173.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q22.1"
     Protein         1..437
                     /product="kelch-like protein 8 isoform 3"
                     /note="kelch-like protein 8; kelch-like 8"
                     /calculated_mol_wt=47828
     Region          52..>73
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Region          <73..111
                     /region_name="BACK"
                     /note="BACK (BTB and C-terminal Kelch) domain; cl28903"
                     /db_xref="CDD:475122"
     Region          128..382
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          173..216
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          220..264
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          267..312
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          314..359
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          361..403
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          372..416
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..437
                     /gene="KLHL8"
                     /coded_by="NM_001292007.2:353..1666"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS75163.1"
                     /db_xref="GeneID:57563"
                     /db_xref="HGNC:HGNC:18644"
                     /db_xref="MIM:611967"
ORIGIN      
        1 masdsmsskq arnhitkgkr qqqhqqiknr ssisdgdged sfifeaneaw kdfhgsllrf
       61 yengelcdvt lkvrlpllpv dflmgvvake qivkqnlkcr dlldearnyh lhlssravpd
      121 feysirttpr khtagvlfcv ggrggsgdpf rsiecysink nswffgpemn srrrhvgvis
      181 vegkvyavgg hdgnehlgsm emfdpltnkw mmkasmntkr rgialaslgg piyaiggldd
      241 ntcfndvery diesdqwstv apmntprggv gsvalvnhvy avggndgmas lssverydph
      301 ldkwievkem gqrragngvs klhgclyvvg gfddnsplss verydprsnk wdyvaalttp
      361 rggvgiatvm gkifavgghn gnaylntvea fdpvlnrwel vgsvshcrag agvavcsclt
      421 sqirdvghgs nnvvdcm
//
LOCUS       NP_001307941             445 aa            linear   PRI 20-NOV-2025
DEFINITION  C-terminal-binding protein 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001307941 XP_005269622
VERSION     NP_001307941.1
DBSOURCE    REFSEQ: accession NM_001321012.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Pastoors,D., Havermans,M., Mulet-Lazaro,R., Brian,D., Noort,W.,
            Grasel,J., Hoogenboezem,R., Smeenk,L., Demmers,J.A.A., Milsom,M.D.,
            Enver,T., Groen,R.W.J., Bindels,E. and Delwel,R.
  TITLE     Oncogene EVI1 drives acute myeloid leukemia via a targetable
            interaction with CTBP2
  JOURNAL   Sci Adv 10 (20), eadk9076 (2024)
   PUBMED   38748792
  REMARK    GeneRIF: Oncogene EVI1 drives acute myeloid leukemia via a
            targetable interaction with CTBP2.
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Cheung,C.H.Y., Cheng,C.K., Leung,K.T., Zhang,C., Ho,C.Y., Luo,X.,
            Kam,A.Y.F., Xia,T., Wan,T.S.K., Pitts,H.A., Chan,N.P.H.,
            Cheung,J.S., Wong,R.S.M., Zhang,X.B. and Ng,M.H.L.
  TITLE     C-terminal binding protein 2 is a novel tumor suppressor targeting
            the MYC-IRF4 axis in multiple myeloma
  JOURNAL   Blood Adv 8 (9), 2217-2234 (2024)
   PUBMED   38457926
  REMARK    GeneRIF: C-terminal binding protein 2 is a novel tumor suppressor
            targeting the MYC-IRF4 axis in multiple myeloma.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Sekiya,M., Ma,Y., Kainoh,K., Saito,K., Yamazaki,D., Tsuyuzaki,T.,
            Chen,W., Adi Putri,P.I.P., Ohno,H., Miyamoto,T., Takeuchi,Y.,
            Murayama,Y., Sugano,Y., Osaki,Y., Iwasaki,H., Yahagi,N., Suzuki,H.,
            Motomura,K., Matsuzaka,T., Murata,K., Mizuno,S., Takahashi,S. and
            Shimano,H.
  TITLE     Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function
  JOURNAL   Cell Rep 42 (8), 112914 (2023)
   PUBMED   37557182
  REMARK    GeneRIF: Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Holmes,M., Turner,J., Fox,A., Chisholm,O., Crossley,M. and Chong,B.
  TITLE     hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
            and modulates GATA-mediated activation
  JOURNAL   J Biol Chem 274 (33), 23491-23498 (1999)
   PUBMED   10438528
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and
            Otte,A.P.
  TITLE     C-Terminal binding protein is a transcriptional repressor that
            interacts with a specific class of vertebrate Polycomb proteins
  JOURNAL   Mol Cell Biol 19 (1), 777-787 (1999)
   PUBMED   9858600
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Turner,J. and Crossley,M.
  TITLE     Cloning and characterization of mCtBP2, a co-repressor that
            associates with basic Kruppel-like factor and other mammalian
            transcriptional regulators
  JOURNAL   EMBO J 17 (17), 5129-5140 (1998)
   PUBMED   9724649
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB200827.1, CX165167.1,
            AL731571.3 and BE671217.1.
            
            On Mar 12, 2016 this sequence version replaced XP_005269622.1.
            
            Summary: This gene produces alternative transcripts encoding two
            distinct proteins. One protein is a transcriptional repressor,
            while the other isoform is a major component of specialized
            synapses known as synaptic ribbons. Both proteins contain a NAD+
            binding domain similar to NAD+-dependent 2-hydroxyacid
            dehydrogenases. A portion of the 3' untranslated region was used to
            map this gene to chromosome 21q21.3; however, it was noted that
            similar loci elsewhere in the genome are likely. Blast analysis
            shows that this gene is present on chromosome 10. Several
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Feb 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2057229.1,
                                           SRR18074967.3936560.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..445
                     /product="C-terminal-binding protein 2 isoform 1"
                     /note="ribeye"
                     /calculated_mol_wt=48814
     Site            22
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     Region          34..352
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(103,106..107,272,321,324)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(106,134,186..187,189..191,209..213,242..244,246,249,
                     270..272,296..297,321,323..324)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Region          414..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P56545.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P56545.1)"
     CDS             1..445
                     /gene="CTBP2"
                     /coded_by="NM_001321012.2:307..1644"
                     /note="isoform 1 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS7643.1"
                     /db_xref="GeneID:1488"
                     /db_xref="HGNC:HGNC:2495"
                     /db_xref="MIM:602619"
ORIGIN      
        1 malvdkhkvk rqrldriceg irpqimngpl hprplvalld grdctvempi lkdlatvafc
       61 daqstqeihe kvlneavgam myhtitltre dlekfkalrv ivrigsgydn vdikaagelg
      121 iavcnipsaa veetadstic hilnlyrrnt wlyqalregt rvqsveqire vasgaarirg
      181 etlgligfgr tgqavavrak afgfsvifyd pylqdgiers lgvqrvytlq dllyqsdcvs
      241 lhcnlnehnh hlindftikq mrqgaflvna argglvdeka laqalkegri rgaaldvhes
      301 epfsfaqgpl kdapnlictp htawyseqas lemreaaate irraitgrip eslrncvnke
      361 ffvtsapwsv idqqaihpel ngatyryppg ivgvapgglp aamegiipgg ipvthnlptv
      421 ahpsqapspn qptkhgdnre hpneq
//
LOCUS       NP_005183                212 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase inhibitor 3 isoform 1 [Homo sapiens].
ACCESSION   NP_005183
VERSION     NP_005183.2
DBSOURCE    REFSEQ: accession NM_005192.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Qin,H., Wang,Q., Xu,J., Zeng,H., Liu,J., Yu,F. and Yang,J.
  TITLE     Integrative analysis of anoikis-related genes prognostic signature
            with immunotherapy and identification of CDKN3 as a key oncogene in
            lung adenocarcinoma
  JOURNAL   Int Immunopharmacol 143 (Pt 1), 113282 (2024)
   PUBMED   39383787
  REMARK    GeneRIF: Integrative analysis of anoikis-related genes prognostic
            signature with immunotherapy and identification of CDKN3 as a key
            oncogene in lung adenocarcinoma.
            Erratum:[Int Immunopharmacol. 2024 Dec 25;143(Pt 3):113584. doi:
            10.1016/j.intimp.2024.113584. PMID: 39580329]
REFERENCE   3  (residues 1 to 212)
  AUTHORS   Zhang,J., Zhang,Y. and Zhang,J.
  TITLE     N6-Methyladenosine modified circ-NAB1 modulates cell cycle and
            epithelial-mesenchymal transition via CDKN3 in endometrial cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 161-169 (2024)
   PUBMED   38814199
  REMARK    GeneRIF: N6-Methyladenosine modified circ-NAB1 modulates cell cycle
            and epithelial-mesenchymal transition via CDKN3 in endometrial
            cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Chen,Y., Li,D., Sha,K., Zhang,X. and Liu,T.
  TITLE     Human pan-cancer analysis of the predictive biomarker for the CDKN3
  JOURNAL   Eur J Med Res 29 (1), 272 (2024)
   PUBMED   38720365
  REMARK    GeneRIF: Human pan-cancer analysis of the predictive biomarker for
            the CDKN3.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Zhu,S. and Fang,Z.
  TITLE     MicroRNA-127-3p Inhibits Cardiomyocyte Inflammation and Apoptosis
            after Acute Myocardial Infarction via Targeting CDKN3
  JOURNAL   Int Heart J 64 (6), 1133-1139 (2023)
   PUBMED   38030294
  REMARK    GeneRIF: MicroRNA-127-3p Inhibits Cardiomyocyte Inflammation and
            Apoptosis after Acute Myocardial Infarction via Targeting CDKN3.
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Poon,R.Y. and Hunter,T.
  TITLE     Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent
            kinase-interacting phosphatase KAP in the absence of cyclin
  JOURNAL   Science 270 (5233), 90-93 (1995)
   PUBMED   7569954
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Demetrick,D.J., Matsumoto,S., Hannon,G.J., Okamoto,K., Xiong,Y.,
            Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the genes for the human cell cycle proteins
            cyclin C (CCNC), cyclin E (CCNE), p21 (CDKN1) and KAP (CDKN3)
  JOURNAL   Cytogenet Cell Genet 69 (3-4), 190-192 (1995)
   PUBMED   7698009
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Hannon,G.J., Casso,D. and Beach,D.
  TITLE     KAP: a dual specificity phosphatase that interacts with
            cyclin-dependent kinases
  JOURNAL   Proc Natl Acad Sci U S A 91 (5), 1731-1735 (1994)
   PUBMED   8127873
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Harper,J.W., Adami,G.R., Wei,N., Keyomarsi,K. and Elledge,S.J.
  TITLE     The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1
            cyclin-dependent kinases
  JOURNAL   Cell 75 (4), 805-816 (1993)
   PUBMED   8242751
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Gyuris,J., Golemis,E., Chertkov,H. and Brent,R.
  TITLE     Cdi1, a human G1 and S phase protein phosphatase that associates
            with Cdk2
  JOURNAL   Cell 75 (4), 791-803 (1993)
   PUBMED   8242750
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK098653.1 and BC064965.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 27, 2001 this sequence version replaced NP_005183.1.
            
            Summary: The protein encoded by this gene belongs to the dual
            specificity protein phosphatase family. It was identified as a
            cyclin-dependent kinase inhibitor, and has been shown to interact
            with, and dephosphorylate CDK2 kinase, thus prevent the activation
            of CDK2 kinase. This gene was reported to be deleted, mutated, or
            overexpressed in several kinds of cancers. Alternatively spliced
            transcript variants encoding different isoforms have been found for
            this gene. [provided by RefSeq, Aug 2008].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.434556.1,
                                           SRR1163655.602463.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000335183.11/ ENSP00000335357.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.2"
     Protein         1..212
                     /product="cyclin-dependent kinase inhibitor 3 isoform 1"
                     /EC_number="3.1.3.16"
                     /EC_number="3.1.3.48"
                     /note="cyclin-dependent kinase interactor 1;
                     cyclin-dependent kinase interacting protein 2;
                     CDK2-associated dual specificity phosphatase;
                     cyclin-dependent kinase inhibitor; kinase-associated
                     phosphatase; Cdk-associated protein phosphatase"
                     /calculated_mol_wt=23674
     Region          1..168
                     /region_name="CDKN3"
                     /note="Cyclin-dependent kinase inhibitor 3 (CDKN3);
                     pfam05706"
                     /db_xref="CDD:399018"
     Region          1..34
                     /region_name="Interaction with CDK2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16667.1)"
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16667.1)"
     CDS             1..212
                     /gene="CDKN3"
                     /gene_synonym="CDI1; CIP2; KAP; KAP1"
                     /coded_by="NM_005192.4:63..701"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9716.1"
                     /db_xref="GeneID:1033"
                     /db_xref="HGNC:HGNC:1791"
                     /db_xref="MIM:123832"
ORIGIN      
        1 mkppssiqts efdssdeepi edeqtpihis wlslsrvncs qflglcalpg ckfkdvrrnv
       61 qkdteelksc giqdifvfct rgelskyrvp nlldlyqqcg iithhhpiad ggtpdiascc
      121 eimeelttcl knyrktlihc ygglgrsclv aaclllylsd tispeqaids lrdlrgsgai
      181 qtikqynylh efrdklaahl ssrdsqsrsv sr
//
LOCUS       NP_009075                344 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb group RING finger protein 2 [Homo sapiens].
ACCESSION   NP_009075
VERSION     NP_009075.1
DBSOURCE    REFSEQ: accession NM_007144.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wang,K., Li,M., Duan,H., Fan,M., Xu,C. and Yu,F.
  TITLE     SLCO4A1-AS1 triggers the malignant behaviours of melanoma cells via
            sponging miR-1306-5p to enhance PCGF2
  JOURNAL   Exp Dermatol 31 (8), 1220-1233 (2022)
   PUBMED   35427425
  REMARK    GeneRIF: SLCO4A1-AS1 triggers the malignant behaviours of melanoma
            cells via sponging miR-1306-5p to enhance PCGF2.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Mai,J., Peng,X.D., Tang,J., Du,T., Chen,Y.H., Wang,Z.F.,
            Zhang,H.L., Huang,J.H., Zhong,Z.Y., Yang,D., Li,Z.L., Huang,Y.,
            Feng,G.K., Zhu,X.F. and Deng,R.
  TITLE     AKT-mediated regulation of chromatin ubiquitylation and
            tumorigenesis through Mel18 phosphorylation
  JOURNAL   Oncogene 40 (13), 2422-2436 (2021)
   PUBMED   33664452
  REMARK    GeneRIF: AKT-mediated regulation of chromatin ubiquitylation and
            tumorigenesis through Mel18 phosphorylation.
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Miyazaki,K., Inoue,H., Onai,N., Ishihara,H. and Kanno,M.
  TITLE     Chemokine-mediated thymopoiesis is regulated by a mammalian
            Polycomb group gene, mel-18
  JOURNAL   Immunol Lett 80 (2), 139-143 (2002)
   PUBMED   11750047
  REMARK    GeneRIF: The mouse counterpart of this gene regulates the
            expression of various chemokines and chemokine receptors, which may
            be important for T cell migration and differentiation.
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Matsuo,F., Yano,K., Saito,H., Morotomi,K., Kato,M., Yoshimoto,M.,
            Kasumi,F., Akiyama,F., Sakamoto,G. and Miki,Y.
  TITLE     Mutation analysis of the mel-18 gene that shows decreased
            expression in human breast cancer cell lines
  JOURNAL   Breast Cancer 9 (1), 33-38 (2002)
   PUBMED   12196719
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Kimura,M., Koseki,Y., Yamashita,M., Watanabe,N., Shimizu,C.,
            Katsumoto,T., Kitamura,T., Taniguchi,M., Koseki,H. and Nakayama,T.
  TITLE     Regulation of Th2 cell differentiation by mel-18, a mammalian
            polycomb group gene
  JOURNAL   Immunity 15 (2), 275-287 (2001)
   PUBMED   11520462
  REMARK    GeneRIF: The mouse counterpart of this gene regulates the
            expression of Th2 cytokines, and plays a critical role in Th2 cell
            differentiation and Th-2 dependent immune responses.
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Ishida,A., Asano,H., Hasegawa,M., Koseki,H., Ono,T., Yoshida,M.C.,
            Taniguchi,M. and Kanno,M.
  TITLE     Cloning and chromosome mapping of the human Mel-18 gene which
            encodes a DNA-binding protein with a new 'RING-finger' motif
  JOURNAL   Gene 129 (2), 249-255 (1993)
   PUBMED   8325509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006449.19.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif and is similar to the polycomb group (PcG) gene products. PcG
            gene products form complexes via protein-protein interaction and
            maintain the transcription repression of genes involved in
            embryogenesis, cell cycles, and tumorigenesis. This protein was
            shown to act as a negative regulator of transcription and has tumor
            suppressor activity. The expression of this gene was detected in
            various tumor cells, but is limited in neural organs in normal
            tissues. Knockout studies in mice suggested that this protein may
            negatively regulate the expression of different cytokines,
            chemokines, and chemokine receptors, and thus plays an important
            role in lymphocyte differentiation and migration, as well as in
            immune responses. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.883288.1, BC024255.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000620225.5/ ENSP00000482815.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..344
                     /product="polycomb group RING finger protein 2"
                     /note="ring finger protein 110; zinc finger protein 144;
                     DNA-binding protein Mel-18"
                     /calculated_mol_wt=37657
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35227.1)"
     Region          130..228
                     /region_name="RAWUL_PCGF2"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     2 (PCGF2); cd17164"
                     /db_xref="CDD:340684"
     Region          <236..328
                     /region_name="PLN02217"
                     /note="probable pectinesterase/pectinesterase inhibitor"
                     /db_xref="CDD:215130"
     Region          240..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35227.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35227.1)"
     CDS             1..344
                     /gene="PCGF2"
                     /gene_synonym="MEL-18; RNF110; TPFS; ZNF144"
                     /coded_by="NM_007144.3:275..1309"
                     /db_xref="CCDS:CCDS32638.1"
                     /db_xref="GeneID:7703"
                     /db_xref="HGNC:HGNC:12929"
                     /db_xref="MIM:600346"
ORIGIN      
        1 mhrttrikit elnphlmcal cggyfidatt iveclhsfck tcivryletn kycpmcdvqv
       61 hktrpllsir sdktlqdivy klvpglfkde mkrrrdfyaa ypltevpngs nedrgevleq
      121 ekgalsddei vslsiefyeg ardrdekkgp lengdgdkek tgvrflrcpa amtvmhlakf
      181 lrnkmdvpsk ykvevlyede plkeyytlmd iayiypwrrn gplplkyrvq packrltlat
      241 vptpsegtnt sgasecesvs dkapspatlp atssslpspa tpshgspssh gppathptsp
      301 tppstasgat taanggslnc lqtpsstsrg rkmtvngapv pplt
//
LOCUS       NP_001340976             710 aa            linear   PRI 20-NOV-2025
DEFINITION  rho guanine nucleotide exchange factor 7 isoform j [Homo sapiens].
ACCESSION   NP_001340976 XP_016876306
VERSION     NP_001340976.1
DBSOURCE    REFSEQ: accession NM_001354047.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 710)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 710)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 710)
  AUTHORS   Kawase,N., Sugihara,A., Kajiwara,K., Hiroshima,M., Akamatsu,K.,
            Nada,S., Matsumoto,K., Ueda,M. and Okada,M.
  TITLE     SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells
  JOURNAL   J Biol Chem 298 (3), 101630 (2022)
   PUBMED   35085554
  REMARK    GeneRIF: SRC kinase activator CDCP1 promotes hepatocyte growth
            factor-induced cell migration/invasion of a subset of breast cancer
            cells.
REFERENCE   4  (residues 1 to 710)
  AUTHORS   Keum,S., Yang,S.J., Park,E., Kang,T., Choi,J.H., Jeong,J.,
            Hwang,Y.E., Kim,J.W., Park,D. and Rhee,S.
  TITLE     Beta-Pix-dynamin 2 complex promotes colorectal cancer progression
            by facilitating membrane dynamics
  JOURNAL   Cell Oncol (Dordr) 44 (6), 1287-1305 (2021)
   PUBMED   34582006
  REMARK    GeneRIF: Beta-Pix-dynamin 2 complex promotes colorectal cancer
            progression by facilitating membrane dynamics.
REFERENCE   5  (residues 1 to 710)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 710)
  AUTHORS   Turner,C.E., Brown,M.C., Perrotta,J.A., Riedy,M.C.,
            Nikolopoulos,S.N., McDonald,A.R., Bagrodia,S., Thomas,S. and
            Leventhal,P.S.
  TITLE     Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin
            repeat, ARF-GAP protein: A role in cytoskeletal remodeling
  JOURNAL   J Cell Biol 145 (4), 851-863 (1999)
   PUBMED   10330411
REFERENCE   7  (residues 1 to 710)
  AUTHORS   Aghazadeh,B., Zhu,K., Kubiseski,T.J., Liu,G.A., Pawson,T., Zheng,Y.
            and Rosen,M.K.
  TITLE     Structure and mutagenesis of the Dbl homology domain
  JOURNAL   Nat Struct Biol 5 (12), 1098-1107 (1998)
   PUBMED   9846881
REFERENCE   8  (residues 1 to 710)
  AUTHORS   Bagrodia,S., Taylor,S.J., Jordon,K.A., Van Aelst,L. and
            Cerione,R.A.
  TITLE     A novel regulator of p21-activated kinases
  JOURNAL   J Biol Chem 273 (37), 23633-23636 (1998)
   PUBMED   9726964
REFERENCE   9  (residues 1 to 710)
  AUTHORS   Manser,E., Loo,T.H., Koh,C.G., Zhao,Z.S., Chen,X.Q., Tan,L.,
            Tan,I., Leung,T. and Lim,L.
  TITLE     PAK kinases are directly coupled to the PIX family of nucleotide
            exchange factors
  JOURNAL   Mol Cell 1 (2), 183-192 (1998)
   PUBMED   9659915
REFERENCE   10 (residues 1 to 710)
  AUTHORS   Oh,W.K., Yoo,J.C., Jo,D., Song,Y.H., Kim,M.G. and Park,D.
  TITLE     Cloning of a SH3 domain-containing proline-rich protein, p85SPR,
            and its localization in focal adhesion
  JOURNAL   Biochem Biophys Res Commun 235 (3), 794-798 (1997)
   PUBMED   9207241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353704.10, AL390754.18 and
            AL139086.12.
            
            On Aug 4, 2017 this sequence version replaced XP_016876306.1.
            
            Summary: This gene encodes a protein that belongs to a family of
            cytoplasmic proteins that activate the Ras-like family of Rho
            proteins by exchanging bound GDP for GTP. It forms a complex with
            the small GTP binding protein Rac1 and recruits Rac1 to membrane
            ruffles and to focal adhesions. Multiple alternatively spliced
            transcript variants encoding different isoforms have been observed
            for this gene. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.27240.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..710
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..710
                     /product="rho guanine nucleotide exchange factor 7 isoform
                     j"
                     /note="SH3 domain-containing proline-rich protein;
                     PAK-interacting exchange factor beta; Rho guanine
                     nucleotide exchange factor (GEF) 7"
                     /calculated_mol_wt=79750
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q14155.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q14155.2)"
     Region          3..>89
                     /region_name="CH_SF"
                     /note="calponin homology (CH) domain superfamily; cl00030"
                     /db_xref="CDD:469584"
     Region          95..148
                     /region_name="SH3_betaPIX"
                     /note="Src Homology 3 domain of beta-Pak Interactive
                     eXchange factor; cd12061"
                     /db_xref="CDD:212994"
     Site            order(100,102,105,108..109,124,126..128,139,141,143..144)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212994"
     Region          179..356
                     /region_name="RhoGEF"
                     /note="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous
                     (DH) domain. It appears that PH domains invariably occur
                     C-terminal to RhoGEF/DH domains; cd00160"
                     /db_xref="CDD:238091"
     Site            order(185,189,283,307..308,311..312,314..315,318..319,
                     322..323,326,352,356)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238091"
     Region          387..485
                     /region_name="PH_Cool_Pix"
                     /note="Cloned out of library/PAK-interactive exchange
                     factor pleckstrin homology (PH) domain; cd01225"
                     /db_xref="CDD:269932"
     Region          545..635
                     /region_name="RhoGEF67_u2"
                     /note="Unstructured region two on RhoGEF 6 and 7;
                     pfam16614"
                     /db_xref="CDD:465200"
     CDS             1..710
                     /gene="ARHGEF7"
                     /gene_synonym="BETA-PIX; COOL-1; COOL1; Nbla10314; P50;
                     P50BP; P85; P85COOL1; P85SPR; PAK3; PIXB"
                     /coded_by="NM_001354047.1:909..3041"
                     /note="isoform j is encoded by transcript variant 13"
                     /db_xref="GeneID:8874"
                     /db_xref="HGNC:HGNC:15607"
                     /db_xref="MIM:605477"
ORIGIN      
        1 mnsaeqtvtw litlgvlesp kktisdpegf lqaslkdgvv lcrllerllp gtiekvypep
       61 rseseclsni reflrgcgas lrledmtdns nnqlvvrakf nfqqtnedel sfskgdvihv
      121 trveeggwwe gtlngrtgwf psnyvrevka sekpvspksg tlksppkgfd ttainksyyn
      181 vvlqnilete neyskelqtv lstylrplqt seklssanis ylmgnleeic sfqqmlvqsl
      241 eectklpeaq qrvggcflnl mpqmktlylt ycanhpsavn vltehseelg efmetkgass
      301 pgilvlttgl skpfmrldky ptllkelerh medyhtdrqd iqksmaafkn lsaqcqevrk
      361 rkelelqilt eairnwegdd iktlgnvtym sqvliqcags eeknerylll fpnvllmlsa
      421 sprmsgfiyq gklpttgmti tkledsenhr nafeisgsmi erilvscnnq qdlqewvehl
      481 qkqtkvtsvg nptikphsvp shtlpshpvt psskhadskp apltpayhtl phpshhgtph
      541 ttinwgplep pktpkpwsls clrpapplrp saalcykedl skspktmkkl lpkrkperkp
      601 sdeefasrks taaleedaqi lkvieaycts aktrqtlnst wqgtdlmhnh vladddqpsl
      661 dslgrrssls rlepsdlsed sdydsiwtah syrmgstsrk sccsyishqn
//
LOCUS       NP_006328                462 aa            linear   PRI 20-NOV-2025
DEFINITION  microspherule protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_006328
VERSION     NP_006328.2
DBSOURCE    REFSEQ: accession NM_006337.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Huang,C.J., Lyu,X. and Kang,J.
  TITLE     The molecular characteristics and functional roles of microspherule
            protein 1 (MCRS1) in gene expression, cell proliferation, and
            organismic development
  JOURNAL   Cell Cycle 22 (6), 619-632 (2023)
   PUBMED   36384428
  REMARK    GeneRIF: The molecular characteristics and functional roles of
            microspherule protein 1 (MCRS1) in gene expression, cell
            proliferation, and organismic development.
            Review article
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Laguillo-Diego,A., Kiewisz,R., Marti-Gomez,C., Baum,D.,
            Muller-Reichert,T. and Vernos,I.
  TITLE     MCRS1 modulates the heterogeneity of microtubule minus-end
            morphologies in mitotic spindles
  JOURNAL   Mol Biol Cell 34 (1), ar1 (2023)
   PUBMED   36350698
  REMARK    GeneRIF: MCRS1 modulates the heterogeneity of microtubule minus-end
            morphologies in mitotic spindles.
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Song,H., Li,Y., Chen,G., Xing,Z., Zhao,J., Yokoyama,K.K., Li,T. and
            Zhao,M.
  TITLE     Human MCRS2, a cell-cycle-dependent protein, associates with
            LPTS/PinX1 and reduces the telomere length
  JOURNAL   Biochem Biophys Res Commun 316 (4), 1116-1123 (2004)
   PUBMED   15044100
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Lin,D.Y. and Shih,H.M.
  TITLE     Essential role of the 58-kDa microspherule protein in the
            modulation of Daxx-dependent transcriptional repression as revealed
            by nucleolar sequestration
  JOURNAL   J Biol Chem 277 (28), 25446-25456 (2002)
   PUBMED   11948183
  REMARK    GeneRIF: role in the modulation of Daxx-dependent transcriptional
            repression
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Bruni,R. and Roizman,B.
  TITLE     Herpes simplex virus 1 regulatory protein ICP22 interacts with a
            new cell cycle-regulated factor and accumulates in a cell
            cycle-dependent fashion in infected cells
  JOURNAL   J Virol 72 (11), 8525-8531 (1998)
   PUBMED   9765390
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Ren,Y., Busch,R.K., Perlaky,L. and Busch,H.
  TITLE     The 58-kDa microspherule protein (MSP58), a nucleolar protein,
            interacts with nucleolar protein p120
  JOURNAL   Eur J Biochem 253 (3), 734-742 (1998)
   PUBMED   9654073
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY078747.1, BC011794.2 and R66413.1.
            
            On Apr 16, 2003 this sequence version replaced NP_006328.1.
            
            Transcript Variant: This variant (1) has an alternate 5' coding
            sequence, compared to variant 2. The resulting isoform (1) is
            shorter and has a distinct N-terminus, compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC011794.2, SRR14038194.4502291.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000343810.9/ ENSP00000345358.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..462
                     /product="microspherule protein 1 isoform 1"
                     /note="INO80 complex subunit Q; cell cycle-regulated
                     factor (78 kDa); INO80 complex subunit J; 58 kDa
                     microspherule protein; cell cycle-regulated factor p78"
                     /calculated_mol_wt=51672
     Region          1..130
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q99L90; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            103
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            108
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Region          113..123
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Site            130
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Region          134..331
                     /region_name="MCRS_N"
                     /note="N-terminal region of micro-spherule protein;
                     pfam13325"
                     /db_xref="CDD:463845"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96EZ8.1)"
     Region          341..445
                     /region_name="FHA_MCRS1"
                     /note="forkhead associated (FHA) domain found in
                     microspherule protein 1 (MCRS1) and similar proteins;
                     cd22687"
                     /db_xref="CDD:438739"
     Site            order(366..367,388..389,391,408,410..411)
                     /site_type="other"
                     /note="putative phosphopeptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438739"
     Region          389..396
                     /region_name="UBR5-degron.
                     /evidence=ECO:0000269|PubMed:37478862"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96EZ8.1)"
     CDS             1..462
                     /gene="MCRS1"
                     /gene_synonym="ICP22BP; INO80Q; MCRS2; MSP58; P78"
                     /coded_by="NM_006337.5:206..1594"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8787.1"
                     /db_xref="GeneID:10445"
                     /db_xref="HGNC:HGNC:6960"
                     /db_xref="MIM:609504"
ORIGIN      
        1 mdkdsqglld sslmasgtas rsedeeslag qkrassqalg tipkrrsssr fikrkkfdde
       61 lvesslakss trakgasgve pgrcsgseps ssekkkvska pstpvppspa papgltkrvk
      121 kskqplqvtk dlgrwkpadd lllinavlqt ndltsvhlgv kfscrftlre vqerwyally
      181 dpvisklacq amrqlhpeai aaiqskalfs kaeeqllskv gstsqptlet fqdllhrhpd
      241 afylartaka lqahwqlmkq yylledqtvq plpkgdqvln fsdaedlidd sklkdmrdev
      301 lehelmvadr rqkreirqle qelhkwqvlv dsitgmsspd fdnqtlavlr grmvrylmrs
      361 reitlgratk dnqidvdlsl egpawkisrk qgviklknng dffianegrr piyidgrpvl
      421 cgskwrlsnn svveiaslrf vflinqdlia liraeaakit pq
//
LOCUS       NP_001354474             533 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 38 [Homo sapiens].
ACCESSION   NP_001354474 XP_024303983
VERSION     NP_001354474.1
DBSOURCE    REFSEQ: accession NM_001367545.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 533)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 533)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 533)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 533)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 533)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 533)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 533)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_024303983.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.608923.1,
                                           SRR3476690.1061220.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..533
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 38"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=59629
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          401..528
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..533
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367545.1:95..1696"
                     /note="isoform 38 is encoded by transcript variant 38"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk epqttvvhna tdgikgstes cntttededl
      361 kaaplrtgng ssvpegrssr drtapsagmq pqpslcssam rkqeiikite qlieainngd
      421 feaytkicdp gltsfepeal gnlvegmdfh kfyfenllsk nskpihttil nphvhviged
      481 aaciayirlt qyidgqgrpr tsqseetrvw hrrdgkwlnv hyhcsgapaa plq
//
LOCUS       NP_000739                502 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit beta-2 precursor [Homo
            sapiens].
ACCESSION   NP_000739
VERSION     NP_000739.1
DBSOURCE    REFSEQ: accession NM_000748.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 502)
  AUTHORS   Mazzaferro,S., Kang,G., Natarajan,K., Hibbs,R.E. and Sine,S.M.
  TITLE     Structural bases for stoichiometry-selective calcium potentiation
            of a neuronal nicotinic receptor
  JOURNAL   Br J Pharmacol 181 (13), 1973-1992 (2024)
   PUBMED   38454578
REFERENCE   2  (residues 1 to 502)
  AUTHORS   George,A.A., John,S.J., Lucero,L.M., Eaton,J.B., Jaiswal,E.,
            Christensen,S.B., Gajewiak,J., Watkins,M., Cao,Y., Olivera,B.M.,
            Im,W., McIntosh,J.M. and Whiteaker,P.
  TITLE     Analogs of alpha-conotoxin PnIC selectively inhibit alpha7beta2-
            over alpha7-only subtype nicotinic acetylcholine receptors via a
            novel allosteric mechanism
  JOURNAL   FASEB J 38 (1), e23374 (2024)
   PUBMED   38161283
REFERENCE   3  (residues 1 to 502)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 502)
  AUTHORS   Weltzin,M.M., George,A.A., Lukas,R.J. and Whiteaker,P.
  TITLE     Sleep-related hypermotor epilepsy associated mutations uncover
            important kinetic roles of alpha4beta2- nicotinic acetylcholine
            receptor intracellular structures
  JOURNAL   PLoS One 16 (3), e0247825 (2021)
   PUBMED   33657187
  REMARK    GeneRIF: Sleep-related hypermotor epilepsy associated mutations
            uncover important kinetic roles of alpha4beta2- nicotinic
            acetylcholine receptor intracellular structures.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 502)
  AUTHORS   Luijerink,L.L.M., Vivekanandarajah,A., Waters,K.A. and
            Machaalani,R.
  TITLE     The alpha7 and beta2 nicotinic acetylcholine receptor subunits
            regulate apoptosis in the infant hippocampus, and in sudden infant
            death syndrome (SIDS)
  JOURNAL   Apoptosis 25 (7-8), 574-589 (2020)
   PUBMED   32577853
  REMARK    GeneRIF: The alpha7 and beta2 nicotinic acetylcholine receptor
            subunits regulate apoptosis in the infant hippocampus, and in
            sudden infant death syndrome (SIDS).
REFERENCE   6  (residues 1 to 502)
  AUTHORS   Wang,F., Gerzanich,V., Wells,G.B., Anand,R., Peng,X., Keyser,K. and
            Lindstrom,J.
  TITLE     Assembly of human neuronal nicotinic receptor alpha5 subunits with
            alpha3, beta2, and beta4 subunits
  JOURNAL   J Biol Chem 271 (30), 17656-17665 (1996)
   PUBMED   8663494
REFERENCE   7  (residues 1 to 502)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
REFERENCE   8  (residues 1 to 502)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
REFERENCE   9  (residues 1 to 502)
  AUTHORS   Anand,R. and Lindstrom,J.
  TITLE     Chromosomal localization of seven neuronal nicotinic acetylcholine
            receptor subunit genes in humans
  JOURNAL   Genomics 13 (4), 962-967 (1992)
   PUBMED   1505988
REFERENCE   10 (residues 1 to 502)
  AUTHORS   Anand,R. and Lindstrom,J.
  TITLE     Nucleotide sequence of the human nicotinic acetylcholine receptor
            beta 2 subunit gene
  JOURNAL   Nucleic Acids Res 18 (14), 4272 (1990)
   PUBMED   2377478
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL592078.10, U62437.1 and
            R40506.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Neuronal acetylcholine receptors are homo- or
            heteropentameric complexes composed of homologous alpha and beta
            subunits. They belong to a superfamily of ligand-gated ion channels
            which allow the flow of sodium and potassium across the plasma
            membrane in response to ligands such as acetylcholine and nicotine.
            This gene encodes one of several beta subunits. Mutations in this
            gene are associated with autosomal dominant nocturnal frontal lobe
            epilepsy. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.46094.1,
                                           SRR1803616.245182.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368476.4/ ENSP00000357461.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..502
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..502
                     /product="neuronal acetylcholine receptor subunit beta-2
                     precursor"
                     /note="cholinergic receptor, nicotinic, beta polypeptide 2
                     (neuronal); neuronal nicotinic acetylcholine receptor beta
                     2; neuronal acetylcholine receptor subunit beta-2;
                     acetylcholine receptor, nicotinic, beta 2 (neuronal);
                     cholinergic receptor, nicotinic beta 2; beta2 human
                     neuronal nicotinic acetylcholine receptor; cholinergic
                     receptor, nicotinic, beta 2 (neuronal)"
                     /calculated_mol_wt=54391
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2646
     mat_peptide     26..502
                     /product="neuronal acetylcholine receptor subunit beta-2"
                     /calculated_mol_wt=54391
     Region          29..479
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          31..234
                     /region_name="LGIC_ECD_nAChR_B2"
                     /note="extracellular domain of nicotinic acetylcholine
                     receptor subunit beta 2 (CHRNB2); cd19025"
                     /db_xref="CDD:349826"
     Site            51
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:27698419,
                     ECO:0007744|PDB:5KXI; propagated from UniProtKB/Swiss-Prot
                     (P17787.1)"
     Site            order(66,68,74..75,82,104,106,115..116,118,120..121,125,
                     127..128,132..134,136,146,148,150,154,176,233)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349826"
     Site            84
                     /site_type="other"
                     /note="Key residue that may interfere with effective
                     access of the conotoxin BuIA to the channel binding site.
                     /evidence=ECO:0000250|UniProtKB:P12390; propagated from
                     UniProtKB/Swiss-Prot (P17787.1)"
     Site            136
                     /site_type="other"
                     /note="Key residue for a rapid dissociation (K(off)) from
                     the conotoxin BuIA.
                     /evidence=ECO:0000250|UniProtKB:P12390; propagated from
                     UniProtKB/Swiss-Prot (P17787.1)"
     Site            144
                     /site_type="other"
                     /note="Key residue for a rapid dissociation (K(off)) from
                     the conotoxin BuIA.
                     /evidence=ECO:0000250|UniProtKB:P12390; propagated from
                     UniProtKB/Swiss-Prot (P17787.1)"
     Region          155..169
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349826"
     Site            168
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17787.1)"
     Site            239..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17787.1)"
     Site            266..282
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17787.1)"
     Site            297..321
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17787.1)"
     Site            459..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P17787.1)"
     Site            485
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P17787.1)"
     CDS             1..502
                     /gene="CHRNB2"
                     /gene_synonym="EFNL3; nAChRB2"
                     /coded_by="NM_000748.3:268..1776"
                     /db_xref="CCDS:CCDS1070.1"
                     /db_xref="GeneID:1141"
                     /db_xref="HGNC:HGNC:1962"
                     /db_xref="MIM:118507"
ORIGIN      
        1 marrcgpval llgfgllrlc sgvwgtdtee rlvehlldps rynklirpat ngselvtvql
       61 mvslaqlisv hereqimttn vwltqewedy rltwkpeefd nmkkvrlpsk hiwlpdvvly
      121 nnadgmyevs fysnavvsyd gsifwlppai yksackievk hfpfdqqnct mkfrswtydr
      181 teidlvlkse vaslddftps gewdivalpg rrnenpddst yvditydfii rrkplfytin
      241 liipcvlits lailvfylps dcgekmtlci svllaltvfl lliskivppt sldvplvgky
      301 lmftmvlvtf sivtsvcvln vhhrspttht mapwvkvvfl eklpallfmq qprhhcarqr
      361 lrlrrrqrer egagalffre apgadsctcf vnrasvqgla gafgaepapv agpgrsgepc
      421 gcglreavdg vrfiadhmrs edddqsvsed wkyvamvidr lflwifvfvc vfgtigmflq
      481 plfqnytttt flhsdhsaps sk
//
LOCUS       NP_000713               1091 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-1 isoform 1
            preproprotein [Homo sapiens].
ACCESSION   NP_000713
VERSION     NP_000713.2
DBSOURCE    REFSEQ: accession NM_000722.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Inoue,H., Shiozaki,A., Kosuga,T., Shimizu,H., Kudou,M., Arita,T.,
            Konishi,H., Komatsu,S., Kuriu,Y., Kubota,T., Fujiwara,H.,
            Morinaga,Y., Konishi,E. and Otsuji,E.
  TITLE     CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer
  JOURNAL   J Gastroenterol 59 (7), 556-571 (2024)
   PUBMED   38536483
  REMARK    GeneRIF: CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer.
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Chen,Z., Mondal,A., Abderemane-Ali,F., Jang,S., Niranjan,S.,
            Montano,J.L., Zaro,B.W. and Minor,D.L. Jr.
  TITLE     EMC chaperone-CaV structure reveals an ion channel assembly
            intermediate
  JOURNAL   Nature 619 (7969), 410-419 (2023)
   PUBMED   37196677
  REMARK    GeneRIF: EMC chaperone-CaV structure reveals an ion channel
            assembly intermediate.
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Dahimene,S., von Elsner,L., Holling,T., Mattas,L.S., Pickard,J.,
            Lessel,D., Pilch,K.S., Kadurin,I., Pratt,W.S., Zhulin,I.B., Dai,H.,
            Hempel,M., Ruzhnikov,M.R.Z., Kutsche,K. and Dolphin,A.C.
  TITLE     Biallelic CACNA2D1 loss-of-function variants cause early-onset
            developmental epileptic encephalopathy
  JOURNAL   Brain 145 (8), 2721-2729 (2022)
   PUBMED   35293990
  REMARK    GeneRIF: Biallelic CACNA2D1 loss-of-function variants cause
            early-onset developmental epileptic encephalopathy.
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Schleithoff,L., Mehrke,G., Reutlinger,B. and Lehmann-Horn,F.
  TITLE     Genomic structure and functional expression of a human
            alpha(2)/delta calcium channel subunit gene (CACNA2)
  JOURNAL   Genomics 61 (2), 201-209 (1999)
   PUBMED   10534405
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Iles,D.E., Lehmann-Horn,F., Scherer,S.W., Tsui,L.C., Olde
            Weghuis,D., Suijkerbuijk,R.F., Heytens,L., Mikala,G., Schwartz,A.,
            Ellis,F.R. et al.
  TITLE     Localization of the gene encoding the alpha 2/delta-subunits of the
            L-type voltage-dependent calcium channel to chromosome 7q and
            analysis of the segregation of flanking markers in malignant
            hyperthermia susceptible families
  JOURNAL   Hum Mol Genet 3 (6), 969-975 (1994)
   PUBMED   7951247
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Powers,P.A., Scherer,S.W., Tsui,L.C., Gregg,R.G. and Hogan,K.
  TITLE     Localization of the gene encoding the alpha 2/delta subunit
            (CACNL2A) of the human skeletal muscle voltage-dependent Ca2+
            channel to chromosome 7q21-q22 by somatic cell hybrid analysis
  JOURNAL   Genomics 19 (1), 192-193 (1994)
   PUBMED   8188232
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Brust,P.F., Simerson,S., McCue,A.F., Deal,C.R., Schoonmaker,S.,
            Williams,M.E., Velicelebi,G., Johnson,E.C., Harpold,M.M. and
            Ellis,S.B.
  TITLE     Human neuronal voltage-dependent calcium channels: studies on
            subunit structure and role in channel assembly
  JOURNAL   Neuropharmacology 32 (11), 1089-1102 (1993)
   PUBMED   8107964
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Ellis,S.B., Williams,M.E., Ways,N.R., Brenner,R., Sharp,A.H.,
            Leung,A.T., Campbell,K.P., McKenna,E., Koch,W.J., Hui,A.,
            Schwartz,A. and Harpold,M.M.
  TITLE     Sequence and expression of mRNAs encoding the alpha 1 and alpha 2
            subunits of a DHP-sensitive calcium channel
  JOURNAL   Science 241 (4873), 1661-1664 (1988)
   PUBMED   2458626
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP258070.1, BC051339.1,
            M76559.1, BG055272.1, AL707206.1, AC006145.2, AL833141.1 and
            AI924415.1.
            
            On Oct 13, 2004 this sequence version replaced NP_000713.1.
            
            Summary: The preproprotein encoded by this gene is cleaved into
            multiple chains that comprise the alpha-2 and delta subunits of the
            voltage-dependent calcium channel complex. Calcium channels mediate
            the influx of calcium ions into the cell upon membrane
            polarization. Mutations in this gene can cause cardiac
            deficiencies, including Brugada syndrome and short QT syndrome.
            Alternate splicing results in multiple transcript variants, some of
            which may lack the delta subunit portion. [provided by RefSeq, Nov
            2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.256576.1,
                                           SRR1660805.49818.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356860.8/ ENSP00000349320.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..1091
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-1 isoform 1 preproprotein"
                     /note="calcium channel, L type, alpha 2 polypeptide;
                     dihydropyridine-sensitive L-type, calcium channel
                     alpha-2/delta subunit; voltage-gated calcium channel
                     subunit alpha-2/delta-1; calcium channel,
                     voltage-dependent, alpha 2/delta subunit 1; alpha2delta-1"
                     /calculated_mol_wt=120752
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     Region          104..223
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Region          239..417
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(259,261,263,331,363)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          509..606
                     /region_name="HK_sensor"
                     /note="Sensor domains of Histidine Kinase receptors;
                     cl38916"
                     /db_xref="CDD:365792"
     Region          632..1060
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     CDS             1..1091
                     /gene="CACNA2D1"
                     /gene_synonym="CACNA2; CACNL2A; CCHL2A; DEE110; LINC01112;
                     lncRNA-N3"
                     /coded_by="NM_000722.4:319..3594"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS5598.1"
                     /db_xref="GeneID:781"
                     /db_xref="HGNC:HGNC:1399"
                     /db_xref="MIM:114204"
ORIGIN      
        1 maagcllalt ltlfqsllig psseepfpsa vtikswvdkm qedlvtlakt asgvnqlvdi
       61 yekyqdlytv epnnarqlve iaardiekll snrskalvrl aleaekvqaa hqwredfasn
      121 evvyynakdd ldpekndsep gsqrikpvfi edanfgrqis yqhaavhipt diyegstivl
      181 nelnwtsald evfkknreed psllwqvfgs atglaryypa spwvdnsrtp nkidlydvrr
      241 rpwyiqgaas pkdmlilvdv sgsvsgltlk lirtsvseml etlsdddfvn vasfnsnaqd
      301 vscfqhlvqa nvrnkkvlkd avnnitakgi tdykkgfsfa feqllnynvs rancnkiiml
      361 ftdggeeraq eifnkynkdk kvrvftfsvg qhnydrgpiq wmacenkgyy yeipsigair
      421 intqeyldvl grpmvlagdk akqvqwtnvy ldalelglvi tgtlpvfnit gqfenktnlk
      481 nqlilgvmgv dvsledikrl tprftlcpng yyfaidpngy vllhpnlqpk npksqepvtl
      541 dfldaelend ikveirnkmi dgesgektfr tlvksqdery idkgnrtytw tpvngtdysl
      601 alvlptysfy yikakleeti tqarskkgkm kdsetlkpdn feesgytfia prdycndlki
      661 sdnnteflln fnefidrktp nnpscnadli nrvlldagft nelvqnywsk qknikgvkar
      721 fvvtdggitr vypkeagenw qenpetyeds fykrsldndn yvftapyfnk sgpgayesgi
      781 mvskaveiyi qgkllkpavv gikidvnswi enftktsird pcagpvcdck rnsdvmdcvi
      841 lddggfllma nhddytnqig rffgeidpsl mrhlvnisvy afnksydyqs vcepgaapkq
      901 gaghrsayvp svadilqigw wataaawsil qqfllsltfp rlleavemed ddftaslskq
      961 sciteqtqyf fdndsksfsg vldcgncsri fhgeklmntn lifimveskg tcpcdtrlli
     1021 qaeqtsdgpn pcdmvkqpry rkgpdvcfdn nvledytdcg gvsglnpslw yiigiqflll
     1081 wlvsgsthrl l
//
LOCUS       NP_001307695            1752 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase listerin isoform 2 [Homo sapiens].
ACCESSION   NP_001307695 XP_011527827
VERSION     NP_001307695.2
DBSOURCE    REFSEQ: accession NM_001320766.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1752)
  AUTHORS   Qin,F., Cai,B., Wang,P., Cao,R., Zhang,Y., Wen,H., Zheng,Y.,
            Zhao,W., Gao,C. and Liu,B.
  TITLE     LTN1 promotes RLR degradation to inhibit immune response to RNA
            virus through the ESCRT pathway
  JOURNAL   Autophagy 20 (6), 1270-1285 (2024)
   PUBMED   38060409
  REMARK    GeneRIF: LTN1 promotes RLR degradation to inhibit immune response
            to RNA virus through the ESCRT pathway.
REFERENCE   2  (residues 1 to 1752)
  AUTHORS   Filbeck,S., Cerullo,F., Pfeffer,S. and Joazeiro,C.A.P.
  TITLE     Ribosome-associated quality-control mechanisms from bacteria to
            humans
  JOURNAL   Mol Cell 82 (8), 1451-1466 (2022)
   PUBMED   35452614
  REMARK    Review article
REFERENCE   3  (residues 1 to 1752)
  AUTHORS   Farhang,S., Sabaie,H., Gharesouran,J., Asadi,M.R., Arsang-Jang,S.,
            Ghafouri-Fard,S., Taheri,M. and Rezazadeh,M.
  TITLE     Expression Analysis of Ermin and Listerin E3 Ubiquitin Protein
            Ligase 1 Genes in the Periphery of Patients with Schizophrenia
  JOURNAL   J Mol Neurosci 72 (2), 246-254 (2022)
   PUBMED   34676516
  REMARK    GeneRIF: Expression Analysis of Ermin and Listerin E3 Ubiquitin
            Protein Ligase 1 Genes in the Periphery of Patients with
            Schizophrenia.
REFERENCE   4  (residues 1 to 1752)
  AUTHORS   Matsuo,Y., Ikeuchi,K., Saeki,Y., Iwasaki,S., Schmidt,C.,
            Udagawa,T., Sato,F., Tsuchiya,H., Becker,T., Tanaka,K.,
            Ingolia,N.T., Beckmann,R. and Inada,T.
  TITLE     Ubiquitination of stalled ribosome triggers ribosome-associated
            quality control
  JOURNAL   Nat Commun 8 (1), 159 (2017)
   PUBMED   28757607
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1752)
  AUTHORS   von der Malsburg,K., Shao,S. and Hegde,R.S.
  TITLE     The ribosome quality control pathway can access nascent
            polypeptides stalled at the Sec61 translocon
  JOURNAL   Mol Biol Cell 26 (12), 2168-2180 (2015)
   PUBMED   25877867
  REMARK    GeneRIF: E3 ligase listerin accesses nascent polypeptides stalled
            at the Sec61 translocon via a gap in the ribosome-translocon
            junction near the Sec61 lateral gate.
REFERENCE   6  (residues 1 to 1752)
  AUTHORS   Shao,S., Brown,A., Santhanam,B. and Hegde,R.S.
  TITLE     Structure and assembly pathway of the ribosome quality control
            complex
  JOURNAL   Mol Cell 57 (3), 433-444 (2015)
   PUBMED   25578875
  REMARK    GeneRIF: Results show that Listerin specificity for nascent
            chain-60S complexes depends on nuclear export mediator factor.
REFERENCE   7  (residues 1 to 1752)
  AUTHORS   Li,S., Wang,L., Berman,M., Kong,Y.Y. and Dorf,M.E.
  TITLE     Mapping a dynamic innate immunity protein interaction network
            regulating type I interferon production
  JOURNAL   Immunity 35 (3), 426-440 (2011)
   PUBMED   21903422
  REMARK    Erratum:[Immunity. 2011 Oct 28;35(4):647-8]
REFERENCE   8  (residues 1 to 1752)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1752)
  AUTHORS   Bengtson,M.H. and Joazeiro,C.A.
  TITLE     Role of a ribosome-associated E3 ubiquitin ligase in protein
            quality control
  JOURNAL   Nature 467 (7314), 470-473 (2010)
   PUBMED   20835226
REFERENCE   10 (residues 1 to 1752)
  AUTHORS   Chu,J., Hong,N.A., Masuda,C.A., Jenkins,B.V., Nelms,K.A.,
            Goodnow,C.C., Glynne,R.J., Wu,H., Masliah,E., Joazeiro,C.A. and
            Kay,S.A.
  TITLE     A mouse forward genetics screen identifies LISTERIN as an E3
            ubiquitin ligase involved in neurodegeneration
  JOURNAL   Proc Natl Acad Sci U S A 106 (7), 2097-2103 (2009)
   PUBMED   19196968
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY001556.1, BC029371.1, AF260011.2, BC140790.1, AB018257.2 and
            BF059116.1.
            
            On Sep 13, 2018 this sequence version replaced NP_001307695.1.
            
            Summary: Like most RING finger proteins, LTN1 functions as an E3
            ubiquitin ligase (Chu et al., 2009 [PubMed 19196968]).[supplied by
            OMIM, Nov 2010].
            
            Transcript Variant: This variant (2) lacks an alternate, in-frame
            exon in the central coding region compared to variant 1. It encodes
            isoform 2, which is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.1355802.1,
                                           SRR11853567.19369.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..1752
                     /product="E3 ubiquitin-protein ligase listerin isoform 2"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 160; zinc finger protein 294;
                     E3 ubiquitin-protein ligase listerin; RING-type E3
                     ubiquitin transferase listerin"
                     /calculated_mol_wt=198741
     Region          59..>262
                     /region_name="COG5219"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227544"
     Region          59..96
                     /region_name="HEAT 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          100..138
                     /region_name="HEAT 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          273..314
                     /region_name="HEAT 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          335..372
                     /region_name="HEAT 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          380..418
                     /region_name="HEAT 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          433..473
                     /region_name="HEAT 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          513..551
                     /region_name="HEAT 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          611..658
                     /region_name="HEAT 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          754..796
                     /region_name="HEAT 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          897..935
                     /region_name="HEAT 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1054..1091
                     /region_name="HEAT 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1170..1213
                     /region_name="HEAT 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1300..1338
                     /region_name="HEAT 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1363..1400
                     /region_name="HEAT 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1461..1498
                     /region_name="HEAT 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          <1463..1751
                     /region_name="COG5219"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227544"
     CDS             1..1752
                     /gene="LTN1"
                     /gene_synonym="C21orf10; C21orf98; RNF160; ZNF294"
                     /coded_by="NM_001320766.2:73..5331"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:26046"
                     /db_xref="HGNC:HGNC:13082"
                     /db_xref="MIM:613083"
ORIGIN      
        1 mggknkqrtk gnlrpsnsgr aaellakeqg tvpgfigfgt sqsdlgyvpa iqgaeeidsl
       61 vdsdfrmvlr klskkdvttk lkamqefgtm cterdtetvk gvlpywprif ckisldhdrr
      121 vreatqqafe klilkvkkql apylkslmgy wlmaqcdtyt paafaakdaf eaafppskqp
      181 eaiafckdei tsvlqdhlik etpdtlsdpq tvpeeereak fyrvvtcsll alkrllcllp
      241 dneldsleek fksllsqnkf wkygkhsvpq irsayfelvs alcqripqlm keeaskvsps
      301 vllsiddsdp ivcpalweav lytlttiedc wlhvnakksv fpklstvire ggrglatviy
      361 pyllpfiskl pqsitnpkld ffknfltslv aglstertkt sslessavis affeclrfim
      421 qqnlgeeeie qmlvndqlip fidavlkdpg lqhgqlfnhl aetlssweak adtekdekta
      481 hnlenvlihf werlseicva kisepeadve svlgvsnllq vlqkpksslk sskkkngkvr
      541 fadeilesnk enekcvsseg ekiegweltt epslthnssg llsplrkkpl edlvckladi
      601 sinyvnerks eqhlrflstl ldsfsssrvf kmllgdekqs ivqakpleia klvqknpavq
      661 flyqkligwl nedqrkdfgf lvdilysalr ccdndmerkk vlddltkacp ssdkhalvtp
      721 wlkgdilgek lvnladclcn edlesrvsse shfserwtll slvlsqhvkn dyligdvyve
      781 riivrlhetl fktkklseae ssdssvsfic dvaynyfssa kgcllmpsse dllltlfqlc
      841 aqskekthlp dflicklknt wlsgvnllvh qtdssykest flhlsalwlk nqvqassldi
      901 nslqvllsav ddllntlles edsylmgvyi gsvmpndsew ekmrqslpmq wlhrpllegr
      961 lslnyecfkt dfkeqdiktl pshlctsall skmvlialrk etvlennele kiiaellysl
     1021 qwceeldnpp ifligfceil qkmnitydnl rvlgntsgll qllfnrsreh gtlwsliiak
     1081 lilsrsissd evkphykrke sffpltegnl htiqslcpfl skeekkefsa qcipallgwt
     1141 kkdlcstngg fghlaifnsc lqtksiddge llhgilkiii swkkehedif lfscnlseas
     1201 pevlgvniei irflslflky cssplaesew dfimcsmlaw lettsenqal ysiplvqlfa
     1261 cvscdlacdl saffdsttld tignlpvnli sewkeffsqg ihslllpilv tvtgenkdvs
     1321 etsfqnamlk pmcetltyis keqllshklp arlvadqktn lpeylqtlln tlaplllfra
     1381 rpvqiavyhm lyklmpelpq ydqdnlksyg deeeepalsp paalmsllsi qedllenvlg
     1441 cipvgqivti kplsedfcyv lgylltwkli ltffkaassq lralysmylr ktkslnklly
     1501 hlfrlmpenp tyaetavevp nkdpktffte elqlsirett mlpyhiphla csvyhmtlkd
     1561 lpamvrlwwn ssekrvfniv drftskyvss vlsfqeissv qtstqlfngm tvkarattre
     1621 vmatytiedi vieliiqlps nyplgsiive sgkrvgvavq qwrnwmlqls tylthqngsi
     1681 meglalwknn vdkrfegved cmicfsvihg fnyslpkkac rtckkkfhsa clykwftssn
     1741 kstcplcret ff
//
LOCUS       NP_001193639             299 aa            linear   PRI 20-NOV-2025
DEFINITION  5'-AMP-activated protein kinase subunit gamma-1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001193639
VERSION     NP_001193639.1
DBSOURCE    REFSEQ: accession NM_001206710.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 299)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 299)
  AUTHORS   Bai,W., Guo,T., Wang,H., Li,B., Sun,Q., Wu,W., Zhang,J., Zhou,J.,
            Luo,J., Zhu,M., Lu,J., Li,P., Dong,B., Han,S., Pang,X., Zhang,G.,
            Bai,Y. and Wang,S.
  TITLE     S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming
  JOURNAL   EMBO Rep 25 (1), 128-143 (2024)
   PUBMED   38177907
  REMARK    GeneRIF: S-nitrosylation of AMPKgamma impairs coronary collateral
            circulation and disrupts VSMC reprogramming.
REFERENCE   3  (residues 1 to 299)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 299)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 299)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 299)
  AUTHORS   Dyck,J.R., Gao,G., Widmer,J., Stapleton,D., Fernandez,C.S.,
            Kemp,B.E. and Witters,L.A.
  TITLE     Regulation of 5'-AMP-activated protein kinase activity by the
            noncatalytic beta and gamma subunits
  JOURNAL   J Biol Chem 271 (30), 17798-17803 (1996)
   PUBMED   8663446
REFERENCE   7  (residues 1 to 299)
  AUTHORS   Woods,A., Cheung,P.C., Smith,F.C., Davison,M.D., Scott,J.,
            Beri,R.K. and Carling,D.
  TITLE     Characterization of AMP-activated protein kinase beta and gamma
            subunits. Assembly of the heterotrimeric complex in vitro
  JOURNAL   J Biol Chem 271 (17), 10282-10290 (1996)
   PUBMED   8626596
REFERENCE   8  (residues 1 to 299)
  AUTHORS   Gao,G., Fernandez,C.S., Stapleton,D., Auster,A.S., Widmer,J.,
            Dyck,J.R., Kemp,B.E. and Witters,L.A.
  TITLE     Non-catalytic beta- and gamma-subunit isoforms of the
            5'-AMP-activated protein kinase
  JOURNAL   J Biol Chem 271 (15), 8675-8681 (1996)
   PUBMED   8621499
REFERENCE   9  (residues 1 to 299)
  AUTHORS   Stapleton,D., Mitchelhill,K.I., Gao,G., Widmer,J., Michell,B.J.,
            Teh,T., House,C.M., Fernandez,C.S., Cox,T., Witters,L.A. and
            Kemp,B.E.
  TITLE     Mammalian AMP-activated protein kinase subfamily
  JOURNAL   J Biol Chem 271 (2), 611-614 (1996)
   PUBMED   8557660
REFERENCE   10 (residues 1 to 299)
  AUTHORS   Hofmann,B., Nishanian,P., Nguyen,T., Insixiengmay,P. and Fahey,J.L.
  TITLE     Human immunodeficiency virus proteins induce the inhibitory
            cAMP/protein kinase A pathway in normal lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6676-6680 (1993)
   PUBMED   7688126
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011603.37, AK293332.1,
            BC000358.2 and BM667691.1.
            
            Summary: The protein encoded by this gene is a regulatory subunit
            of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer
            consisting of an alpha catalytic subunit, and non-catalytic beta
            and gamma subunits. AMPK is an important energy-sensing enzyme that
            monitors cellular energy status. In response to cellular metabolic
            stresses, AMPK is activated, and thus phosphorylates and
            inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy
            beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in
            regulating de novo biosynthesis of fatty acid and cholesterol. This
            subunit is one of the gamma regulatory subunits of AMPK.
            Alternatively spliced transcript variants encoding distinct
            isoforms have been observed. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and uses
            a downstream in-frame start codon, compared to variant 1. The
            encoded isoform (4) is shorter at the N-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293332.1, SRR5189652.93171.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..299
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.12"
     Protein         1..299
                     /product="5'-AMP-activated protein kinase subunit gamma-1
                     isoform 4"
                     /note="AMPK gamma-1 chain; 5'-AMP-activated protein
                     kinase, gamma-1 subunit; AMPK gamma1; protein kinase,
                     AMP-activated, gamma 1 non-catalytic subunit"
                     /calculated_mol_wt=33953
     Region          6..142
                     /region_name="CBS_euAMPK_gamma-like_repeat1"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains found in AMP-activated
                     protein kinase gamma-like proteins, repeat 1; cd04618"
                     /db_xref="CDD:341388"
     Site            order(13,15..17,39..41,120,134,136,138..139,142)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341388"
     Region          13..86
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Site            order(39,53,57..58,61,98,120..122,138)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341388"
     Region          98..142
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341388"
     Region          168..291
                     /region_name="CBS_euAMPK_gamma-like_repeat2"
                     /note="CBS pair domain found in 5'-AMP (adenosine
                     monophosphate)-activated protein kinase; cd04641"
                     /db_xref="CDD:341399"
     Site            order(169,171..173,195..197,267,280,282,284..285,288)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341399"
     Region          169..234
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     Site            order(195,208,212..213,216,245,267..269,284)
                     /site_type="other"
                     /note="ligand binding site I [chemical binding]"
                     /db_xref="CDD:341399"
     Region          245..288
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341399"
     CDS             1..299
                     /gene="PRKAG1"
                     /gene_synonym="AMPKG"
                     /coded_by="NM_001206710.2:341..1240"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS55824.1"
                     /db_xref="GeneID:5571"
                     /db_xref="HGNC:HGNC:9385"
                     /db_xref="MIM:602742"
ORIGIN      
        1 mkshrcydli ptssklvvfd tslqvkkaff alvtngvraa plwdskkqsf vgmltitdfi
       61 nilhryyksa lvqiyeleeh kietwrevyl qdsfkplvci spnaslfdav sslirnkihr
      121 lpvidpesgn tlyilthkri lkflklfite fpkpefmsks leelqigtya niamvrtttp
      181 vyvalgifvq hrvsalpvvd ekgrvvdiys kfdvinlaae ktynnldvsv tkalqhrshy
      241 fegvlkcylh etletiinrl veaevhrlvv vdendvvkgi vslsdilqal vltggekkp
//
LOCUS       NP_001340923             571 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001340923 XP_016885411
VERSION     NP_001340923.1
DBSOURCE    REFSEQ: accession NM_001353994.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 571)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 571)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 571)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 571)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 571)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 571)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 571)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 571)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 571)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            
            On Aug 3, 2017 this sequence version replaced XP_016885411.1.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (8), as well as variants 5-7, 9,
            and 10, encodes isoform 5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.114904.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..571
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..571
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 5"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=65207
     Region          13..112
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          129..455
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     CDS             1..571
                     /gene="MTMR1"
                     /coded_by="NM_001353994.1:296..2011"
                     /note="isoform 5 is encoded by transcript variant 8"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 meeaplfpge sikaivkdvm yicpfmgavs gtltvtdfkl yfknverdph fildvplgvi
       61 srvekigaqs hgdnscgiei vckdmrnlrl aykqeeqskl gifenlnkha fplsngqalf
      121 afsykekfpi ngwkvydpvs eykrqglpne swkiskinsn yefcdtypai ivvptsvkdd
      181 dlskvaafra kgrvpvlswi hpesqatitr csqplvgpnd krckedekyl qtimdanaqs
      241 hkliifdarq nsvadtnktk gggyesesay pnaelvflei hnihvmresl rklkeivyps
      301 idearwlsnv dgthwleyir mllagavria dkiesgktsv vvhcsdgwdr taqltslaml
      361 mldsyyrtik gfetlvekew isfghrfalr vghgndnhad adrspiflqf vdcvwqmtrq
      421 fpsafefnel flitildhly sclfgtflcn ceqqrfkedv ytktislwsy insqldefsn
      481 pffvnyenhv lypvaslshl elwvnyyvrw nprmrpqmpi hqnlkellav raelqkrveg
      541 lqrevatrav ssssergssp shsatsvhts v
//
LOCUS       NP_077271                251 aa            linear   PRI 20-NOV-2025
DEFINITION  derlin-1 isoform a [Homo sapiens].
ACCESSION   NP_077271 NP_061100
VERSION     NP_077271.1
DBSOURCE    REFSEQ: accession NM_024295.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Wang,T., Wang,D., Kuang,G., Gong,X., Zhang,L., Wan,J. and Li,K.
  TITLE     Derlin-1 promotes diet-induced non-alcoholic fatty liver disease
            via increasing RIPK3-mediated necroptosis
  JOURNAL   Free Radic Biol Med 217, 29-47 (2024)
   PUBMED   38522486
  REMARK    GeneRIF: Derlin-1 promotes diet-induced non-alcoholic fatty liver
            disease via increasing RIPK3-mediated necroptosis.
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Rao,B., Wang,Q., Yao,D., Xia,Y., Li,W., Xie,Y., Li,S., Cao,M.,
            Shen,Y., Qin,A., Zhao,J. and Cao,Y.
  TITLE     The cryo-EM structure of the human ERAD retrotranslocation complex
  JOURNAL   Sci Adv 9 (41), eadi5656 (2023)
   PUBMED   37831771
REFERENCE   3  (residues 1 to 251)
  AUTHORS   You,H., Wen,X., Wang,X., Zhu,C., Chen,H., Bu,L., Zhang,J. and Qu,S.
  TITLE     Derlin-1 ameliorates nonalcoholic hepatic steatosis by promoting
            ubiquitylation and degradation of FABP1
  JOURNAL   Free Radic Biol Med 207, 260-271 (2023)
   PUBMED   37499886
  REMARK    GeneRIF: Derlin-1 ameliorates nonalcoholic hepatic steatosis by
            promoting ubiquitylation and degradation of FABP1.
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Miyano,K., Okamoto,S., Kajikawa,M., Kiyohara,T., Kawai,C.,
            Yamauchi,A. and Kuribayashi,F.
  TITLE     Regulation of Derlin-1-mediated degradation of NADPH oxidase
            partner p22phox by thiol modification
  JOURNAL   Redox Biol 56, 102479 (2022)
   PUBMED   36122532
  REMARK    GeneRIF: Regulation of Derlin-1-mediated degradation of NADPH
            oxidase partner p22(phox) by thiol modification.
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Schulze,A., Standera,S., Buerger,E., Kikkert,M., van Voorden,S.,
            Wiertz,E., Koning,F., Kloetzel,P.M. and Seeger,M.
  TITLE     The ubiquitin-domain protein HERP forms a complex with components
            of the endoplasmic reticulum associated degradation pathway
  JOURNAL   J Mol Biol 354 (5), 1021-1027 (2005)
   PUBMED   16289116
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Ye,Y., Shibata,Y., Kikkert,M., van Voorden,S., Wiertz,E. and
            Rapoport,T.A.
  TITLE     Recruitment of the p97 ATPase and ubiquitin ligases to the site of
            retrotranslocation at the endoplasmic reticulum membrane
  JOURNAL   Proc Natl Acad Sci U S A 102 (40), 14132-14138 (2005)
   PUBMED   16186510
  REMARK    GeneRIF: Derlin-1 is part of a retrotranslocation channel that is
            associated with both the polyubiquitination and p97-ATPase
            machineries at the endoplasmic reticulum membrane.
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Lilley,B.N. and Ploegh,H.L.
  TITLE     Multiprotein complexes that link dislocation, ubiquitination, and
            extraction of misfolded proteins from the endoplasmic reticulum
            membrane
  JOURNAL   Proc Natl Acad Sci U S A 102 (40), 14296-14301 (2005)
   PUBMED   16186509
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Katiyar,S., Joshi,S. and Lennarz,W.J.
  TITLE     The retrotranslocation protein Derlin-1 binds peptide:N-glycanase
            to the endoplasmic reticulum
  JOURNAL   Mol Biol Cell 16 (10), 4584-4594 (2005)
   PUBMED   16055502
  REMARK    GeneRIF: Derlin-1 interacts with the N-terminal domain of PNGase
            via its cytosolic C-terminus. PNGase distributed in two
            populations; ER-associated and free in the cytosol, which suggests
            the deglycosylation process can proceed at either site
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Ye,Y., Shibata,Y., Yun,C., Ron,D. and Rapoport,T.A.
  TITLE     A membrane protein complex mediates retro-translocation from the ER
            lumen into the cytosol
  JOURNAL   Nature 429 (6994), 841-847 (2004)
   PUBMED   15215856
  REMARK    GeneRIF: Derlin-1 interacts with US11, a virally encoded ER protein
            that specifically targets MHC class I heavy chains for export from
            the ER, as well as with VIMP, a novel membrane protein that
            recruits the p97 ATPase and its cofactor
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Lilley,B.N. and Ploegh,H.L.
  TITLE     A membrane protein required for dislocation of misfolded proteins
            from the ER
  JOURNAL   Nature 429 (6994), 834-840 (2004)
   PUBMED   15215855
  REMARK    GeneRIF: Derlin-1 is an important factor for the extraction of
            certain aberrantly folded proteins from the mammalian ER
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA800358.1, AY358818.1,
            AK023846.1, AF131854.1 and AA976062.1.
            
            On Apr 9, 2003 this sequence version replaced NP_061100.1.
            
            Summary: The protein encoded by this gene is a member of the derlin
            family. Members of this family participate in the ER-associated
            degradation response and retrotranslocate misfolded or unfolded
            proteins from the ER lumen to the cytosol for proteasomal
            degradation. This protein recognizes substrate in the ER and works
            in a complex to retrotranslocate it across the ER membrane into the
            cytosol. This protein may select cystic fibrosis transmembrane
            conductance regulator protein (CFTR) for degradation as well as
            unfolded proteins in Alzheimer's disease. Alternative splicing
            results in multiple transcript variants that encode different
            protein isoforms. [provided by RefSeq, Aug 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.95145.1,
                                           SRR1660809.180544.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000259512.9/ ENSP00000259512.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.13"
     Protein         1..251
                     /product="derlin-1 isoform a"
                     /note="DERtrin-1; degradation in endoplasmic reticulum
                     protein 1; Der1-like domain family, member 1"
                     /calculated_mol_wt=28670
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Region          11..204
                     /region_name="DER1"
                     /note="Der1-like family; pfam04511"
                     /db_xref="CDD:427988"
     Site            16..31
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            70..89
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            95..115
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            123..137
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            155..166
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            171..189
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Region          229..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     Region          241..248
                     /region_name="SHP-box.
                     /evidence=ECO:0000305|PubMed:27714797"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BUN8.1)"
     CDS             1..251
                     /gene="DERL1"
                     /gene_synonym="DER-1; DER1; derlin-1"
                     /coded_by="NM_024295.6:181..936"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6337.1"
                     /db_xref="GeneID:79139"
                     /db_xref="HGNC:HGNC:28454"
                     /db_xref="MIM:608813"
ORIGIN      
        1 msdigdwfrs ipaitrywfa atvavplvgk lglispaylf lwpeaflyrf qiwrpitatf
       61 yfpvgpgtgf lylvnlyfly qystrletga fdgrpadylf mllfnwiciv itglamdmql
      121 lmiplimsvl yvwaqlnrdm ivsfwfgtrf kacylpwvil gfnyiiggsv inelignlvg
      181 hlyfflmfry pmdlggrnfl stpqflyrwl psrrggvsgf gvppasmrra adqnggggrh
      241 nwgqgfrlgd q
//
LOCUS       NP_006347                161 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP synthase peripheral stalk subunit d, mitochondrial isoform a
            [Homo sapiens].
ACCESSION   NP_006347
VERSION     NP_006347.1
DBSOURCE    REFSEQ: accession NM_006356.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Katz Shroitman,N., Yitzhaky,A., Ben Shachar,D., Gurwitz,D. and
            Hertzberg,L.
  TITLE     Meta-analysis of brain samples of individuals with schizophrenia
            detects down-regulation of multiple ATP synthase encoding genes in
            both females and males
  JOURNAL   J Psychiatr Res 158, 350-359 (2023)
   PUBMED   36640659
  REMARK    GeneRIF: Meta-analysis of brain samples of individuals with
            schizophrenia detects down-regulation of multiple ATP synthase
            encoding genes in both females and males.
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Song,K.H., Kim,J.H., Lee,Y.H., Bae,H.C., Lee,H.J., Woo,S.R.,
            Oh,S.J., Lee,K.M., Yee,C., Kim,B.W., Cho,H., Chung,E.J.,
            Chung,J.Y., Hewitt,S.M., Chung,T.W., Ha,K.T., Bae,Y.K., Mao,C.P.,
            Yang,A., Wu,T.C. and Kim,T.W.
  TITLE     Mitochondrial reprogramming via ATP5H loss promotes multimodal
            cancer therapy resistance
  JOURNAL   J Clin Invest 128 (9), 4098-4114 (2018)
   PUBMED   30124467
  REMARK    GeneRIF: ATP5H loss in the tumor is strongly linked to failure of
            therapy, disease progression, and poor survival in patients with
            cancer.
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Aggeler,R., Coons,J., Taylor,S.W., Ghosh,S.S., Garcia,J.J.,
            Capaldi,R.A. and Marusich,M.F.
  TITLE     A functionally active human F1F0 ATPase can be purified by
            immunocapture from heart tissue and fibroblast cell lines. Subunit
            structure and activity studies
  JOURNAL   J Biol Chem 277 (37), 33906-33912 (2002)
   PUBMED   12110673
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Wang,H. and Oster,G.
  TITLE     Energy transduction in the F1 motor of ATP synthase
  JOURNAL   Nature 396 (6708), 279-282 (1998)
   PUBMED   9834036
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Elston,T., Wang,H. and Oster,G.
  TITLE     Energy transduction in ATP synthase
  JOURNAL   Nature 391 (6666), 510-513 (1998)
   PUBMED   9461222
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Higuti,T., Kuroiwa,K., Miyazaki,S., Yoshihara,Y., Toda,H.,
            Kakuno,T. and Sakiyama,F.
  TITLE     The complete amino acid sequence of subunit d of rat liver
            mitochondrial H(+)-ATP synthase
  JOURNAL   J Biochem 114 (5), 714-717 (1993)
   PUBMED   7509337
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Boyer,P.D., Cross,R.L. and Momsen,W.
  TITLE     A new concept for energy coupling in oxidative phosphorylation
            based on a molecular explanation of the oxygen exchange reactions
  JOURNAL   Proc Natl Acad Sci U S A 70 (10), 2837-2839 (1973)
   PUBMED   4517936
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC032245.1, BC029392.1,
            BC038092.2 and AA608885.1.
            
            Summary: Mitochondrial ATP synthase catalyzes ATP synthesis,
            utilizing an electrochemical gradient of protons across the inner
            membrane during oxidative phosphorylation. It is composed of two
            linked multi-subunit complexes: the soluble catalytic core, F1, and
            the membrane-spanning component, Fo, which comprises the proton
            channel. The F1 complex consists of 5 different subunits (alpha,
            beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3
            beta, and a single representative of the other 3. The Fo seems to
            have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene
            encodes the d subunit of the Fo complex. Alternatively spliced
            transcript variants encoding different isoforms have been
            identified for this gene. In addition, three pseudogenes are
            located on chromosomes 9, 12 and 15. [provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript, and it encodes the longer isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BG706786.1, CD175322.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142680
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000301587.9/
                                                  ENSP00000301587.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..161
                     /product="ATP synthase peripheral stalk subunit d,
                     mitochondrial isoform a"
                     /EC_number="3.6.1.14"
                     /note="ATP synthase, H+ transporting, mitochondrial F0
                     complex, subunit d; ATP synthase, H+ transporting,
                     mitochondrial F1F0, subunit d; ATP synthase peripheral
                     stalk subunit d, mitochondrial; ATP synthase, H+
                     transporting, mitochondrial Fo complex, subunit d; My032
                     protein; ATP synthase D chain, mitochondrial; ATP synthase
                     subunit d, mitochondrial; ATPase subunit d; ATP synthase,
                     H+ transporting, mitochondrial Fo complex subunit D"
                     /calculated_mol_wt=18360
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Region          3..155
                     /region_name="Mt_ATP-synt_D"
                     /note="ATP synthase D chain, mitochondrial (ATP5H);
                     pfam05873"
                     /db_xref="CDD:461764"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCX2; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            63
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCX2; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            72
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCX2; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DCX2; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            85
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            95
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            117
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q9DCX2; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     Site            149
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75947.3)"
     CDS             1..161
                     /gene="ATP5PD"
                     /gene_synonym="APT5H; ATP5H; ATPQ"
                     /coded_by="NM_006356.3:55..540"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11712.1"
                     /db_xref="GeneID:10476"
                     /db_xref="HGNC:HGNC:845"
                     /db_xref="MIM:618121"
ORIGIN      
        1 magrklalkt idwvafaeii pqnqkaiass lkswnetlts rlaalpenpp aidwayykan
       61 vakaglvddf ekkfnalkvp vpedkytaqv daeekedvks caewvslska riveyekeme
      121 kmknlipfdq mtiedlneaf petkldkkky pywphqpien l
//
LOCUS       NP_066943                817 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 3 isoform a [Homo sapiens].
ACCESSION   NP_066943
VERSION     NP_066943.2
DBSOURCE    REFSEQ: accession NM_021120.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Huyghebaert,J., Mateiu,L., Elinck,E., Van Rossem,K.E.,
            Christiaenssen,B., D'Incal,C.P., McCormack,M.K., Lazzarini,A.,
            Vandeweyer,G. and Kooy,R.F.
  TITLE     Identification of a DLG3 stop mutation in the MRX20 family
  JOURNAL   Eur J Hum Genet 32 (3), 317-323 (2024)
   PUBMED   38273165
  REMARK    GeneRIF: Identification of a DLG3 stop mutation in the MRX20
            family.
REFERENCE   3  (residues 1 to 817)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     DLG3, the gene encoding human neuroendocrine Dlg (NE-Dlg), is
            located within the 1.8-Mb dystonia-parkinsonism region at Xq13.1
  JOURNAL   Genomics 49 (2), 310-313 (1998)
   PUBMED   9598320
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Makino,K., Kuwahara,H., Masuko,N., Nishiyama,Y., Morisaki,T.,
            Sasaki,J., Nakao,M., Kuwano,A., Nakata,M., Ushio,Y. and Saya,H.
  TITLE     Cloning and characterization of NE-dlg: a novel human homolog of
            the Drosophila discs large (dlg) tumor suppressor protein interacts
            with the APC protein
  JOURNAL   Oncogene 14 (20), 2425-2433 (1997)
   PUBMED   9188857
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Takeuchi,M., Hata,Y., Hirao,K., Toyoda,A., Irie,M. and Takai,Y.
  TITLE     SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
            postsynaptic density
  JOURNAL   J Biol Chem 272 (18), 11943-11951 (1997)
   PUBMED   9115257
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Lau,L.F., Mammen,A., Ehlers,M.D., Kindler,S., Chung,W.J.,
            Garner,C.C. and Huganir,R.L.
  TITLE     Interaction of the N-methyl-D-aspartate receptor complex with a
            novel synapse-associated protein, SAP102
  JOURNAL   J Biol Chem 271 (35), 21622-21628 (1996)
   PUBMED   8702950
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Muller,B.M., Kistner,U., Kindler,S., Chung,W.J., Kuhlendahl,S.,
            Fenster,S.D., Lau,L.F., Veh,R.W., Huganir,R.L., Gundelfinger,E.D.
            and Garner,C.C.
  TITLE     SAP102, a novel postsynaptic protein that interacts with NMDA
            receptor complexes in vivo
  JOURNAL   Neuron 17 (2), 255-265 (1996)
   PUBMED   8780649
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL139398.20, AB209328.1,
            BC093866.1, AB033058.1 and CK300381.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 25, 2006 this sequence version replaced NP_066943.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase protein family. The encoded protein may play a
            role in clustering of NMDA receptors at excitatory synapses. It may
            also negatively regulate cell proliferation through interaction
            with the C-terminal region of the adenomatosis polyposis coli tumor
            suppressor protein. Mutations in this gene have been associated
            with X-linked cognitive disability. Alternatively spliced
            transcript variants have been described. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.216999.1, U49089.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374360.8/ ENSP00000363480.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..817
                     /product="disks large homolog 3 isoform a"
                     /note="disks large homolog 3; neuroendocrine-DLG; protein
                     phosphatase 1, regulatory subunit 82; synapse-associated
                     protein 102; discs, large homolog 3"
                     /calculated_mol_wt=90183
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92796.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q92796.2)"
     Region          33..101
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92796.2)"
     Region          129..208
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70175; propagated from
                     UniProtKB/Swiss-Prot (Q92796.2)"
     Site            order(140..146,163,166,196,200,203..204)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          226..310
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(235..241,258,261,291,295,298..299)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          311..385
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          383..473
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(395..401,412,415,445,449,452..453)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          502..568
                     /region_name="SH3_DLG3"
                     /note="Src Homology 3 domain of Disks Large homolog 3;
                     cd12029"
                     /db_xref="CDD:212962"
     Site            order(507,529..530)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212962"
     Site            order(510,512,515,524,542..543,562,564..565)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212962"
     Region          626..804
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     Site            673
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P70175; propagated from
                     UniProtKB/Swiss-Prot (Q92796.2)"
     CDS             1..817
                     /gene="DLG3"
                     /gene_synonym="MRX; MRX90; NEDLG; PPP1R82; SAP102; XLID90;
                     XLMR"
                     /coded_by="NM_021120.4:368..2821"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14403.1"
                     /db_xref="GeneID:1741"
                     /db_xref="HGNC:HGNC:2902"
                     /db_xref="MIM:300189"
ORIGIN      
        1 mhkhqhcckc pecyevtrla alrrleppgy gdwqvpdpyg pgggngasag yggyssqtlp
       61 sqagatptpr tkakliptgr dvgpvppkpv pgkstpklng sgpswwpect ctnrdwyeqv
      121 ngsdgmfkye eivlergnsg lgfsiaggid nphvpddpgi fitkiipgga aamdgrlgvn
      181 dcvlrvnevd vsevvhsrav ealkeagpvv rlvvrrrqpp petimevnll kgpkglgfsi
      241 aggignqhip gdnsiyitki ieggaaqkdg rlqigdrlla vnntnlqdvr heeavaslkn
      301 tsdmvylkva kpgslhlndm yappdyastf taladnhish nsslgylgav eskvsypapp
      361 qvpptryspi prhmlaeedf treprkiilh kgstglgfni vggedgegif vsfilaggpa
      421 dlsgelrrgd rilsvngvnl rnatheqaaa alkragqsvt ivaqyrpeey srfeskihdl
      481 reqmmnssms sgsgslrtse krslyvralf dydrtrdscl psqglsfsyg dilhvinasd
      541 dewwqarlvt phgeseqigv ipskkrvekk erarlktvkf hartgmiesn rdfpglsddy
      601 ygaknlkgqe dailsyepvt rqeihyarpv iilgpmkdrv nddlisefph kfgscvphtt
      661 rprrdnevdg qdyhfvvsre qmekdiqdnk fieagqfndn lygtsiqsvr avaergkhci
      721 ldvsgnaikr lqqaqlypia ifikpksiea lmemnrrqty eqankiydka mkleqefgey
      781 ftaivqgdsl eeiynkikqi iedqsghyiw vpspekl
//
LOCUS       NP_076999                393 aa            linear   PRI 20-NOV-2025
DEFINITION  sister chromatid cohesion protein DCC1 [Homo sapiens].
ACCESSION   NP_076999
VERSION     NP_076999.2
DBSOURCE    REFSEQ: accession NM_024094.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   He,Q., Wang,F., O'Donnell,M.E. and Li,H.
  TITLE     Cryo-EM reveals a nearly complete PCNA loading process and unique
            features of the human alternative clamp loader CTF18-RFC
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2319727121 (2024)
   PUBMED   38669181
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Liu,H., Cui,Z., Wang,R., Wang,L., Wang,L., Cheng,F., Pan,R. and
            Yang,X.
  TITLE     Characterization of the prognostic, diagnostic, and immunological
            roles of DSCC1 and its genomic alteration and instability in human
            cancers
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (4), 202-211 (2024)
   PUBMED   38678604
  REMARK    GeneRIF: Characterization of the prognostic, diagnostic, and
            immunological roles of DSCC1 and its genomic alteration and
            instability in human cancers.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 393)
  AUTHORS   Jin,G., Wang,W., Cheng,P., Tian,Y., Zhang,L. and Niu,H.U.
  TITLE     DNA replication and sister chromatid cohesion 1 promotes breast
            carcinoma progression by modulating the Wnt/beta-catenin signaling
            and p53 protein
  JOURNAL   J Biosci 45 (2020)
   PUBMED   33184243
  REMARK    GeneRIF: DNA replication and sister chromatid cohesion 1 promotes
            breast carcinoma progression by modulating the Wnt/beta-catenin
            signaling and p53 protein.
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Terret,M.E., Sherwood,R., Rahman,S., Qin,J. and Jallepalli,P.V.
  TITLE     Cohesin acetylation speeds the replication fork
  JOURNAL   Nature 462 (7270), 231-234 (2009)
   PUBMED   19907496
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Farina,A., Shin,J.H., Kim,D.H., Bermudez,V.P., Kelman,Z., Seo,Y.S.
            and Hurwitz,J.
  TITLE     Studies with the human cohesin establishment factor, ChlR1.
            Association of ChlR1 with Ctf18-RFC and Fen1
  JOURNAL   J Biol Chem 283 (30), 20925-20936 (2008)
   PUBMED   18499658
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Watrin,E., Schleiffer,A., Tanaka,K., Eisenhaber,F., Nasmyth,K. and
            Peters,J.M.
  TITLE     Human Scc4 is required for cohesin binding to chromatin,
            sister-chromatid cohesion, and mitotic progression
  JOURNAL   Curr Biol 16 (9), 863-874 (2006)
   PUBMED   16682347
REFERENCE   9  (residues 1 to 393)
  AUTHORS   Bermudez,V.P., Maniwa,Y., Tappin,I., Ozato,K., Yokomori,K. and
            Hurwitz,J.
  TITLE     The alternative Ctf18-Dcc1-Ctf8-replication factor C complex
            required for sister chromatid cohesion loads proliferating cell
            nuclear antigen onto DNA
  JOURNAL   Proc Natl Acad Sci U S A 100 (18), 10237-10242 (2003)
   PUBMED   12930902
  REMARK    GeneRIF: The alternative Ctf18-Dcc1-Ctf8-replication factor C
            complex required for sister chromatid cohesion loads proliferating
            cell nuclear antigen onto DNA.
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Merkle,C.J., Karnitz,L.M., Henry-Sanchez,J.T. and Chen,J.
  TITLE     Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human
            homologs of a Saccharomyces cerevisiae complex involved in sister
            chromatid cohesion establishment
  JOURNAL   J Biol Chem 278 (32), 30051-30056 (2003)
   PUBMED   12766176
  REMARK    GeneRIF: hCTF18, hCTF8, and hDCC1 interact with each other as well
            as with the p38 subunit of RFC
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA346021.1, BC001531.2 and AK058129.1.
            
            On Feb 13, 2009 this sequence version replaced NP_076999.1.
            
            Summary: CHTF18 (MIM 613201), CHTF8 (MIM 613202), and DSCC1 are
            components of an alternative replication factor C (RFC) (see MIM
            600404) complex that loads PCNA (MIM 176740) onto DNA during S
            phase of the cell cycle (Merkle et al., 2003 [PubMed 12766176];
            Bermudez et al., 2003 [PubMed 12930902]).[supplied by OMIM, Dec
            2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC001316.1, SRR1660803.155311.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313655.5/ ENSP00000322180.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.12"
     Protein         1..393
                     /product="sister chromatid cohesion protein DCC1"
                     /note="defective in sister chromatid cohesion protein 1
                     homolog; defective in sister chromatid cohesion 1 homolog"
                     /calculated_mol_wt=44694
     Region          43..357
                     /region_name="Dcc1"
                     /note="Sister chromatid cohesion protein Dcc1; pfam09724"
                     /db_xref="CDD:462857"
     CDS             1..393
                     /gene="DSCC1"
                     /gene_synonym="DCC1"
                     /coded_by="NM_024094.3:100..1281"
                     /db_xref="CCDS:CCDS6330.1"
                     /db_xref="GeneID:79075"
                     /db_xref="HGNC:HGNC:24453"
                     /db_xref="MIM:613203"
ORIGIN      
        1 mkrtrdevda tlqiaklnaa ellpavhclg fgpgasgaaa gdfcllelep tlcqqledgh
       61 slvirgdkde qavlcskdkt ydlkiadtsn mllfipgckt pdqlkkedsh cniihteifg
      121 fsnnywelrr rrpklkklkk llmenpyegp dsqkekdsns skyttedlld qiqaseeeim
      181 tqlqvlnack iggywrilef dyemkllnhv tqlvdsesws fgkvplntcl qelgplepee
      241 miehclkcyg kkyvdegevy feldadkicr aaarmllqna vkfnlaefqe vwqqsvpegm
      301 vtsldqlkgl alvdrhsrpe iifllkvddl pednqerfns lfslrekwte ediapyiqdl
      361 cgekqtigal ltkyshssmq ngvkvynsrr pis
//
LOCUS       NP_776247                291 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding Raly-like protein isoform 2 [Homo sapiens].
ACCESSION   NP_776247
VERSION     NP_776247.3
DBSOURCE    REFSEQ: accession NM_173848.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 291)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 291)
  AUTHORS   Xia,Y., Ye,S., Yang,Y., Liu,Y. and Tong,G.
  TITLE     Over-expression of RALYL suppresses the progression of ovarian
            clear cell carcinoma through inhibiting MAPK and CDH1 signaling
            pathways
  JOURNAL   Int J Med Sci 18 (3), 785-791 (2021)
   PUBMED   33437214
  REMARK    GeneRIF: Over-expression of RALYL suppresses the progression of
            ovarian clear cell carcinoma through inhibiting MAPK and CDH1
            signaling pathways.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 291)
  AUTHORS   Zhang,Y., Wang,J., Liu,X. and Liu,H.
  TITLE     Exploring the role of RALYL in Alzheimer's disease reserve by
            network-based approaches
  JOURNAL   Alzheimers Res Ther 12 (1), 165 (2020)
   PUBMED   33298176
  REMARK    GeneRIF: Exploring the role of RALYL in Alzheimer's disease reserve
            by network-based approaches.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 291)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 291)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   7  (residues 1 to 291)
  AUTHORS   Cobb,J., Cule,E., Moncrieffe,H., Hinks,A., Ursu,S., Patrick,F.,
            Kassoumeri,L., Flynn,E., Bulatovic,M., Wulffraat,N., van Zelst,B.,
            de Jonge,R., Bohm,M., Dolezalova,P., Hirani,S., Newman,S.,
            Whitworth,P., Southwood,T.R., De Iorio,M., Wedderburn,L.R. and
            Thomson,W.
  CONSRTM   Childhood Arthritis Response to Medication Study (CHARMS);
            Childhood Arthritis Prospective Study (CAPS); BSPAR study group
  TITLE     Genome-wide data reveal novel genes for methotrexate response in a
            large cohort of juvenile idiopathic arthritis cases
  JOURNAL   Pharmacogenomics J 14 (4), 356-364 (2014)
   PUBMED   24709693
REFERENCE   8  (residues 1 to 291)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   9  (residues 1 to 291)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 291)
  AUTHORS   Ji,C.N., Chen,J.Z., Xie,Y., Wang,S., Qian,J., Zhao,E., Jin,W.,
            Wu,X.Z., Xu,W.X., Ying,K. and Mao,Y.M.
  TITLE     A novel cDNA encodes a putative hRALY-like protein, hRALYL
  JOURNAL   Mol Biol Rep 30 (1), 61-67 (2003)
   PUBMED   12688537
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC012400.11, AC027043.7, AC087368.7 and AC009901.6.
            
            On Jul 31, 2007 this sequence version replaced NP_776247.2.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region and initiates translation at a
            downstream start codon, compared to variant 1. Variants 2 through 4
            encode the same isoform (2), which has a shorter N-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.165454.1,
                                           SRR1803617.268874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145544, SAMEA2154665
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000521268.6/ ENSP00000430367.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q21.2"
     Protein         1..291
                     /product="RNA-binding Raly-like protein isoform 2"
                     /note="RNA-binding Raly-like protein; hnRNP core protein
                     C-like 3; heterogeneous nuclear ribonucleoprotein C-like
                     3"
                     /calculated_mol_wt=32199
     Region          15..97
                     /region_name="RRM_SF"
                     /note="RNA recognition motif (RRM) superfamily; cl17169"
                     /db_xref="CDD:473069"
     Region          171..192
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     Region          199..>244
                     /region_name="XhlA"
                     /note="Haemolysin XhlA; pfam10779"
                     /db_xref="CDD:402419"
     Region          249..291
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86SE5.2)"
     CDS             1..291
                     /gene="RALYL"
                     /gene_synonym="HNRPCL3"
                     /coded_by="NM_173848.7:1175..2050"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55253.1"
                     /db_xref="GeneID:138046"
                     /db_xref="HGNC:HGNC:27036"
                     /db_xref="MIM:614648"
ORIGIN      
        1 mtgktqtsnv tnkndpksin srvfignlnt aivkkvdiea ifskygkivg csvhkgyafv
       61 qymserhara avagenarvi agqpldinma gepkpyrpkp gnkrplsaly rleskepfls
      121 vggyvfdydy yrddfynrlf dyhgrvpppp raviplkrpr vavtttrrgk gvfsmkggsr
      181 stasgstgsk lksdelqtik keltqiktki dsllgrleki ekqqkaeaea qkkqleeslv
      241 liqeecvsei adhsteepae ggpdadgeem tdgieedfde dgghelflqi k
//
LOCUS       NP_001310464             358 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing regulatory glutamine/lysine-rich protein 1 isoform h [Homo
            sapiens].
ACCESSION   NP_001310464
VERSION     NP_001310464.1
DBSOURCE    REFSEQ: accession NM_001323535.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Chang,C., Rajasekaran,M., Qiao,Y., Dong,H., Wang,Y., Xia,H.,
            Deivasigamani,A., Wu,M., Sekar,K., Gao,H., Sun,M., Niu,Y., Li,Q.,
            Tao,L., Yan,Z., Wang,M., Chen,S., Zhao,S., Chen,D., Li,L., Yang,F.,
            Gao,H., Chen,B., Su,L., Xu,L., Chen,Y., Seshachalam,V.P., Chen,G.,
            Gunaratne,J., Hong,W., Shi,J., Chen,G., Grierson,D.S., Chabot,B.,
            Xie,T., Hui,K.M. and Chen,J.
  TITLE     The aberrant upregulation of exon 10-inclusive SREK1 through SRSF10
            acts as an oncogenic driver in human hepatocellular carcinoma
  JOURNAL   Nat Commun 13 (1), 1363 (2022)
   PUBMED   35296659
  REMARK    GeneRIF: The aberrant upregulation of exon 10-inclusive SREK1
            through SRSF10 acts as an oncogenic driver in human hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Abudureheman,Z., Li,L., Zhong,X., Xu,J., Gong,H., Yilamujiang,S.,
            Ren,J., Xie,C., Zheng,A., Tuerxun,D., Abudukadeer,A., Aini,P.,
            Xu,A. and Zou,X.
  TITLE     The rs74794265 SNP of the SREK1 Gene is Associated with COPD in
            Kashi, China
  JOURNAL   Int J Chron Obstruct Pulmon Dis 16, 2631-2636 (2021)
   PUBMED   34556983
  REMARK    GeneRIF: The rs74794265 SNP of the SREK1 Gene is Associated with
            COPD in Kashi, China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Heese,K., Fujita,M., Akatsu,H., Yamamoto,T., Kosaka,K., Nagai,Y.
            and Sawada,T.
  TITLE     The splicing regulatory protein p18SRP is down-regulated in
            Alzheimer's disease brain
  JOURNAL   J Mol Neurosci 24 (2), 269-276 (2004)
   PUBMED   15456940
  REMARK    GeneRIF: p18SRP is a lysine-rich zinc finger domain-containing
            protein that interacts with the serine-arginine-rich splicing
            regulatory protein SRrp86; it is downregulated in brain of
            Alzheimer disease patients.
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   8  (residues 1 to 358)
  AUTHORS   Li,J., Barnard,D.C. and Patton,J.G.
  TITLE     A unique glutamic acid-lysine (EK) domain acts as a splicing
            inhibitor
  JOURNAL   J Biol Chem 277 (42), 39485-39492 (2002)
   PUBMED   12183448
  REMARK    GeneRIF: the unique glutamic acid-lysine domain of SRrp86 plays a
            modulatory role controlling serine-arginine domain function
REFERENCE   9  (residues 1 to 358)
  AUTHORS   Barnard,D.C., Li,J., Peng,R. and Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 through coactivation
            and repression of specific SR proteins
  JOURNAL   RNA 8 (4), 526-533 (2002)
   PUBMED   11991645
  REMARK    GeneRIF: SRrp86 can activate SRp20 and repress SC35 in a
            dose-dependent manner both in vitro and in vivo
REFERENCE   10 (residues 1 to 358)
  AUTHORS   Barnard,D.C. and Patton,J.G.
  TITLE     Identification and characterization of a novel serine-arginine-rich
            splicing regulatory protein
  JOURNAL   Mol Cell Biol 20 (9), 3049-3057 (2000)
   PUBMED   10757789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025442.6 and AC008772.6.
            
            Summary: This gene encodes a member of a family of
            serine/arginine-rich (SR) splicing proteins containing RNA
            recognition motif (RRM) domains. The encoded protein interacts with
            other SR proteins to modulate splice site selection. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.136614.1,
                                           SRR1803615.154640.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..358
                     /product="splicing regulatory glutamine/lysine-rich
                     protein 1 isoform h"
                     /note="splicing factor, arginine/serine-rich 12;
                     serine-arginine-rich splicing regulatory protein 508;
                     serine/arginine-rich-splicing regulatory protein 86;
                     splicing regulatory glutamine/lysine-rich protein 1;
                     splicing regulatory glutamic acid/lysine-rich protein 1"
                     /calculated_mol_wt=43224
     CDS             1..358
                     /gene="SREK1"
                     /gene_synonym="SFRS12; SRrp508; SRrp86"
                     /coded_by="NM_001323535.2:764..1840"
                     /note="isoform h is encoded by transcript variant 9"
                     /db_xref="GeneID:140890"
                     /db_xref="HGNC:HGNC:17882"
                     /db_xref="MIM:609268"
ORIGIN      
        1 mtpqaaakel eevmkrvrea qsfisaaiep esgksnerkg grsrshtrsk srssskshsr
       61 rkrsqskhrs rshnrsrsrq kdrrrsksph kkrsksrerr ksrsrshsrd krkdtrekik
      121 ekervkekdr ekerereker ekekergknk drdkerekdr ekdkekdrer erekehekdr
      181 dkekekeqdk ekerekdrsk eidekrkkdk ksrtpprsyn asrrsrsssr errrrrsrss
      241 srsprtskti krkssrspsp rrnkkdkkre kerdhiserr ererstsmrk ssndrdgkek
      301 leknstslke kehnkepdss vskevddkda prteenkiqh ngncqlneen lstkteav
//
LOCUS       NP_001011713             362 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 30 [Homo sapiens].
ACCESSION   NP_001011713 XP_058661
VERSION     NP_001011713.2
DBSOURCE    REFSEQ: accession NM_001011713.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 362)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 362)
  AUTHORS   Haakonsen,D.L., Heider,M., Ingersoll,A.J., Vodehnal,K., Witus,S.R.,
            Uenaka,T., Wernig,M. and Rape,M.
  TITLE     Stress response silencing by an E3 ligase mutated in
            neurodegeneration
  JOURNAL   Nature 626 (8000), 874-880 (2024)
   PUBMED   38297121
REFERENCE   3  (residues 1 to 362)
  AUTHORS   Varland,S., Silva,R.D., Kjosas,I., Faustino,A., Bogaert,A.,
            Billmann,M., Boukhatmi,H., Kellen,B., Costanzo,M., Drazic,A.,
            Osberg,C., Chan,K., Zhang,X., Tong,A.H.Y., Andreazza,S., Lee,J.J.,
            Nedyalkova,L., Usaj,M., Whitworth,A.J., Andrews,B.J., Moffat,J.,
            Myers,C.L., Gevaert,K., Boone,C., Martinho,R.G. and Arnesen,T.
  TITLE     N-terminal acetylation shields proteins from degradation and
            promotes age-dependent motility and longevity
  JOURNAL   Nat Commun 14 (1), 6774 (2023)
   PUBMED   37891180
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 362)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 362)
  AUTHORS   Varland,S., Myklebust,L.M., Goksoyr,S.O., Glomnes,N., Torsvik,J.,
            Varhaug,J.E. and Arnesen,T.
  TITLE     Identification of an alternatively spliced nuclear isoform of human
            N-terminal acetyltransferase Naa30
  JOURNAL   Gene 644, 27-37 (2018)
   PUBMED   29247799
  REMARK    GeneRIF: Overexpression of full-length Naa30 increased cell
            viability.
REFERENCE   6  (residues 1 to 362)
  AUTHORS   Mughal,A.A., Grieg,Z., Skjellegrind,H., Fayzullin,A.,
            Lamkhannat,M., Joel,M., Ahmed,M.S., Murrell,W., Vik-Mo,E.O.,
            Langmoen,I.A. and Stangeland,B.
  TITLE     Knockdown of NAT12/NAA30 reduces tumorigenic features of
            glioblastoma-initiating cells
  JOURNAL   Mol Cancer 14, 160 (2015)
   PUBMED   26292663
  REMARK    GeneRIF: NAT12/NAA30 plays an important role in growth and survival
            of GICs possibly by regulating hypoxia response (HIF1a), levels of
            p-MTOR (Ser2448) and the p53 pathway.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 362)
  AUTHORS   Aksnes,H., Van Damme,P., Goris,M., Starheim,K.K., Marie,M.,
            Stove,S.I., Hoel,C., Kalvik,T.V., Hole,K., Glomnes,N., Furnes,C.,
            Ljostveit,S., Ziegler,M., Niere,M., Gevaert,K. and Arnesen,T.
  TITLE     An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic
            N termini of transmembrane proteins and maintains Golgi integrity
  JOURNAL   Cell Rep 10 (8), 1362-1374 (2015)
   PUBMED   25732826
REFERENCE   8  (residues 1 to 362)
  AUTHORS   Anger,A.M., Armache,J.P., Berninghausen,O., Habeck,M., Subklewe,M.,
            Wilson,D.N. and Beckmann,R.
  TITLE     Structures of the human and Drosophila 80S ribosome
  JOURNAL   Nature 497 (7447), 80-85 (2013)
   PUBMED   23636399
REFERENCE   9  (residues 1 to 362)
  AUTHORS   Polevoda,B., Arnesen,T. and Sherman,F.
  TITLE     A synopsis of eukaryotic Nalpha-terminal acetyltransferases:
            nomenclature, subunits and substrates
  JOURNAL   BMC Proc 3 Suppl 6 (Suppl 6), S2 (2009)
   PUBMED   19660095
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 362)
  AUTHORS   Starheim,K.K., Gromyko,D., Evjenth,R., Ryningen,A., Varhaug,J.E.,
            Lillehaug,J.R. and Arnesen,T.
  TITLE     Knockdown of human N alpha-terminal acetyltransferase complex C
            leads to p53-dependent apoptosis and aberrant human Arl8b
            localization
  JOURNAL   Mol Cell Biol 29 (13), 3569-3581 (2009)
   PUBMED   19398576
  REMARK    GeneRIF: Human Naa30 (MAK3) is the catalytic subunit of the human
            NatC N-terminal acetyltransferase complex. NatC acetylates
            hydrophobic Met-starting N-termini, and NatC knockdown induces
            p53-dependent apoptosis.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK092674.1, BC118589.1, BC048983.1 and AL355834.4.
            
            On Jun 13, 2008 this sequence version replaced NP_001011713.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.151325.1,
                                           SRR1660805.250676.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000556492.6/ ENSP00000452521.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.3"
     Protein         1..362
                     /product="N-alpha-acetyltransferase 30"
                     /EC_number="2.3.1.256"
                     /note="N-acetyltransferase 12 (GCN5-related, putative);
                     N-acetyltransferase MAK3 homolog; putative
                     N-acetyltransferase; natC catalytic subunit"
                     /calculated_mol_wt=39189
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q147X3.1)"
     Region          38..88
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            39
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Region          113..182
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            117
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Region          224..338
                     /region_name="Acetyltransf_1"
                     /note="Acetyltransferase (GNAT) family; pfam00583"
                     /db_xref="CDD:395465"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q147X3.1)"
     Site            order(287..289,299..300)
                     /site_type="other"
                     /note="Coenzyme A binding pocket [chemical binding]"
                     /db_xref="CDD:173926"
     CDS             1..362
                     /gene="NAA30"
                     /gene_synonym="C14orf35; MAK3; Mak3p; NAT12; NAT12P"
                     /coded_by="NM_001011713.3:122..1210"
                     /db_xref="CCDS:CCDS32088.1"
                     /db_xref="GeneID:122830"
                     /db_xref="HGNC:HGNC:19844"
                     /db_xref="MIM:617989"
ORIGIN      
        1 maevppgpss llpppappap aaveprcpfp agaalaccse deeddeeheg ggsrspagge
       61 satvaakghp clrcpqppqe qqqlnglisp elrhlraaas lkskvlsvae vaattatpdg
      121 gpratatkga gvhsgerpph slssnartav pspveaaaas dpaaarngla egteqeeeee
      181 deqvrllsss ltadcslrsp sgrevepged rtiryvryes elqmpdimrl itkdlsepys
      241 iytyryfihn wpqlcflamv geecvgaivc kldmhkkmfr rgyiamlavd skyrrngigt
      301 nlvkkaiyam vegdcdevvl eteitnksal klyenlgfvr dkrlfryyln gvdalrlklw
      361 lr
//
LOCUS       NP_079422                169 aa            linear   PRI 20-NOV-2025
DEFINITION  N-alpha-acetyltransferase 50 isoform 1 [Homo sapiens].
ACCESSION   NP_079422
VERSION     NP_079422.1
DBSOURCE    REFSEQ: accession NM_025146.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Reddi,R., Saddanapu,V., Chinthapalli,D.K., Sankoju,P., Sripadi,P.
            and Addlagatta,A.
  TITLE     Human Naa50 Protein Displays Broad Substrate Specificity for
            Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL
            ANALYSIS USING TETRAPEPTIDE LIBRARY
  JOURNAL   J Biol Chem 291 (39), 20530-20538 (2016)
   PUBMED   27484799
  REMARK    GeneRIF: Because Naa10 is reported to acetylate all amino termini
            that are devoid of methionine and Naa50 acetylates all other
            peptides that are followed by methionine
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Starheim,K.K., Gromyko,D., Evjenth,R., Ryningen,A., Varhaug,J.E.,
            Lillehaug,J.R. and Arnesen,T.
  TITLE     Knockdown of human N alpha-terminal acetyltransferase complex C
            leads to p53-dependent apoptosis and aberrant human Arl8b
            localization
  JOURNAL   Mol Cell Biol 29 (13), 3569-3581 (2009)
   PUBMED   19398576
  REMARK    GeneRIF: Data show that with MAK3 knockdown, p53 is stabilized and
            phosphorylated and there is a significant transcriptional
            activation of proapoptotic genes downstream of p53, and that
            localization of Arl8b is altered, suggesting that Arl8b is a Mak3
            substrate.
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Hou,F., Chu,C.W., Kong,X., Yokomori,K. and Zou,H.
  TITLE     The acetyltransferase activity of San stabilizes the mitotic
            cohesin at the centromeres in a shugoshin-independent manner
  JOURNAL   J Cell Biol 177 (4), 587-597 (2007)
   PUBMED   17502424
  REMARK    GeneRIF: May be specifically required for the maintenance of
            centromeric cohesion in mitosis.
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Arnesen,T., Anderson,D., Torsvik,J., Halseth,H.B., Varhaug,J.E. and
            Lillehaug,J.R.
  TITLE     Cloning and characterization of hNAT5/hSAN: an evolutionarily
            conserved component of the NatA protein N-alpha-acetyltransferase
            complex
  JOURNAL   Gene 371 (2), 291-295 (2006)
   PUBMED   16507339
  REMARK    GeneRIF: The first description of the human homologue of Nat5p/San,
            hNAT5, the third component of the human NatA
            N-alpha-acetyltransferase complex
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM831426.1, BC012731.2, DB198553.1, DB096143.1, DA408894.1,
            DA599265.1, HX784836.1, AW954963.1, H15889.1, H39948.1, BX102492.1
            and AC108693.5.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023256.1, SRR1803612.19842.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000240922.8/ ENSP00000240922.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.31"
     Protein         1..169
                     /product="N-alpha-acetyltransferase 50 isoform 1"
                     /EC_number="2.3.1.258"
                     /note="N-acetyltransferase 5; N-acetyltransferase 13
                     (GCN5-related); N-acetyltransferase san homolog; natE
                     catalytic subunit; N-epsilon-acetyltransferase 50"
                     /calculated_mol_wt=19267
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; N6-acetyllysine, by
                     autocatalysis. /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            37
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929,
                     ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Region          57..155
                     /region_name="RimI"
                     /note="Ribosomal protein S18 acetylase RimI and related
                     acetyltransferases [Translation, ribosomal structure and
                     biogenesis]; COG0456"
                     /db_xref="CDD:440224"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:19744929; propagated from
                     UniProtKB/Swiss-Prot (Q9GZZ1.1)"
     CDS             1..169
                     /gene="NAA50"
                     /gene_synonym="hNaa50p; MAK3; NAT13; NAT13P; NAT5; NAT5P;
                     SAN"
                     /coded_by="NM_025146.4:301..810"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2975.1"
                     /db_xref="GeneID:80218"
                     /db_xref="HGNC:HGNC:29533"
                     /db_xref="MIM:610834"
ORIGIN      
        1 mkgsrielgd vtphnikqlk rlnqvifpvs yndkfykdvl evgelaklay fndiavgavc
       61 crvdhsqnqk rlyimtlgcl apyrrlgigt kmlnhvlnic ekdgtfdniy lhvqisnesa
      121 idfyrkfgfe iietkknyyk riepadahvl qknlkvpsgq nadvqktdn
//
LOCUS       NP_001307570             562 aa            linear   PRI 20-NOV-2025
DEFINITION  myc box-dependent-interacting protein 1 isoform 12 [Homo sapiens].
ACCESSION   NP_001307570 XP_005263701
VERSION     NP_001307570.1
DBSOURCE    REFSEQ: accession NM_001320641.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 562)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 562)
  AUTHORS   Saha,O., Melo de Farias,A.R., Pelletier,A., Siedlecki-Wullich,D.,
            Landeira,B.S., Gadaut,J., Carrier,A., Vreulx,A.C., Guyot,K.,
            Shen,Y., Bonnefond,A., Amouyel,P., Tcw,J., Kilinc,D., Queiroz,C.M.,
            Delahaye,F., Lambert,J.C. and Costa,M.R.
  TITLE     The Alzheimer's disease risk gene BIN1 regulates activity-dependent
            gene expression in human-induced glutamatergic neurons
  JOURNAL   Mol Psychiatry 29 (9), 2634-2646 (2024)
   PUBMED   38514804
  REMARK    GeneRIF: The Alzheimer's disease risk gene BIN1 regulates
            activity-dependent gene expression in human-induced glutamatergic
            neurons.
REFERENCE   3  (residues 1 to 562)
  AUTHORS   Picas,L., Andre-Arpin,C., Comunale,F., Bousquet,H., Tsai,F.C.,
            Rico,F., Maiuri,P., Pernier,J., Bodin,S., Nicot,A.S., Laporte,J.,
            Bassereau,P., Goud,B., Gauthier-Rouviere,C. and Miserey,S.
  TITLE     BIN1 regulates actin-membrane interactions during IRSp53-dependent
            filopodia formation
  JOURNAL   Commun Biol 7 (1), 549 (2024)
   PUBMED   38724689
  REMARK    GeneRIF: BIN1 regulates actin-membrane interactions during
            IRSp53-dependent filopodia formation.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 562)
  AUTHORS   Garcia-Agudo,L.F., Shi,Z., Smith,I.F., Kramar,E.A., Tran,K.,
            Kawauchi,S., Wang,S., Collins,S., Walker,A., Shi,K.X., Neumann,J.,
            Liang,H.Y., Da Cunha,C., Milinkeviciute,G., Morabito,S.,
            Miyoshi,E., Rezaie,N., Gomez-Arboledas,A., Arvilla,A.M.,
            Ghaemi,D.I., Tenner,A.J., LaFerla,F.M., Wood,M.A., Mortazavi,A.,
            Swarup,V., MacGregor,G.R. and Green,K.N.
  TITLE     BIN1K358R suppresses glial response to plaques in mouse model of
            Alzheimer's disease
  JOURNAL   Alzheimers Dement 20 (4), 2922-2942 (2024)
   PUBMED   38460121
  REMARK    GeneRIF: BIN1[K358R] suppresses glial response to plaques in mouse
            model of Alzheimer's disease.
REFERENCE   5  (residues 1 to 562)
  AUTHORS   Kaur,I., Behl,T., Sundararajan,G., Panneerselvam,P.,
            Vijayakumar,A.R., Senthilkumar,G.P., Venkatachalam,T., Jaglan,D.,
            Yadav,S., Anwer,K., Fuloria,N.K., Sehgal,A., Gulati,M. and
            Chigurupati,S.
  TITLE     BIN1 in the Pursuit of Ousting the Alzheimer's Reign: Impact on
            Amyloid and Tau Neuropathology
  JOURNAL   Neurotox Res 41 (6), 698-707 (2023)
   PUBMED   37847429
  REMARK    GeneRIF: BIN1 in the Pursuit of Ousting the Alzheimer's Reign:
            Impact on Amyloid and Tau Neuropathology.
            Review article
REFERENCE   6  (residues 1 to 562)
  AUTHORS   Ramjaun,A.R., Micheva,K.D., Bouchelet,I. and McPherson,P.S.
  TITLE     Identification and characterization of a nerve terminal-enriched
            amphiphysin isoform
  JOURNAL   J Biol Chem 272 (26), 16700-16706 (1997)
   PUBMED   9195986
REFERENCE   7  (residues 1 to 562)
  AUTHORS   Butler,M.H., David,C., Ochoa,G.C., Freyberg,Z., Daniell,L.,
            Grabs,D., Cremona,O. and De Camilli,P.
  TITLE     Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs
            family, is concentrated in the cortical cytomatrix of axon initial
            segments and nodes of ranvier in brain and around T tubules in
            skeletal muscle
  JOURNAL   J Cell Biol 137 (6), 1355-1367 (1997)
   PUBMED   9182667
REFERENCE   8  (residues 1 to 562)
  AUTHORS   Leprince,C., Romero,F., Cussac,D., Vayssiere,B., Berger,R.,
            Tavitian,A. and Camonis,J.H.
  TITLE     A new member of the amphiphysin family connecting endocytosis and
            signal transduction pathways
  JOURNAL   J Biol Chem 272 (24), 15101-15105 (1997)
   PUBMED   9182529
REFERENCE   9  (residues 1 to 562)
  AUTHORS   Sakamuro,D., Elliott,K.J., Wechsler-Reya,R. and Prendergast,G.C.
  TITLE     BIN1 is a novel MYC-interacting protein with features of a tumour
            suppressor
  JOURNAL   Nat Genet 14 (1), 69-77 (1996)
   PUBMED   8782822
  REMARK    GeneRIF: A nucleocytosolic myc-interacting isoform of Bin1 has
            properties of a tumor suppressor.
REFERENCE   10 (residues 1 to 562)
  AUTHORS   Negorev,D., Riethman,H., Wechsler-Reya,R., Sakamuro,D.,
            Prendergast,G.C. and Simon,D.
  TITLE     The Bin1 gene localizes to human chromosome 2q14 by PCR analysis of
            somatic cell hybrids and fluorescence in situ hybridization
  JOURNAL   Genomics 33 (2), 329-331 (1996)
   PUBMED   8725406
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL713697.1, BM742027.1,
            AC012508.10, AW411140.1, BE047931.1, BM805510.1, BC004101.2 and
            BM711160.1.
            
            On Mar 2, 2016 this sequence version replaced XP_005263701.1.
            
            Summary: This gene encodes several isoforms of a nucleocytoplasmic
            adaptor protein, one of which was initially identified as a
            MYC-interacting protein with features of a tumor suppressor.
            Isoforms that are expressed in the central nervous system may be
            involved in synaptic vesicle endocytosis and may interact with
            dynamin, synaptojanin, endophilin, and clathrin. Isoforms that are
            expressed in muscle and ubiquitously expressed isoforms localize to
            the cytoplasm and nucleus and activate a caspase-independent
            apoptotic process. Studies in mouse suggest that this gene plays an
            important role in cardiac muscle development. Alternate splicing of
            the gene results in several transcript variants encoding different
            isoforms. Aberrant splice variants expressed in tumor cell lines
            have also been described. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (12) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (12) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.81185.1,
                                           SRR14038195.2436253.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..562
                     /product="myc box-dependent-interacting protein 1 isoform
                     12"
                     /note="amphiphysin II; box dependant MYC interacting
                     protein 1; amphiphysin-like protein; box-dependent
                     myc-interacting protein 1; amphiphysin 2"
                     /calculated_mol_wt=61130
     Region          31..241
                     /region_name="BAR_Amphiphysin_I_II"
                     /note="The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin
                     I and II; cd07611"
                     /db_xref="CDD:153295"
     Site            order(50,53..54,58,61,64..65,68,78..79,81..82,85..86,
                     88..89,92,100,197,200..201,203,208..209,211..212,215..216,
                     218..219,222..223,225..226,230,233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:153295"
     Site            order(73,80,139,142,145..146,170)
                     /site_type="other"
                     /note="putative membrane interaction site"
                     /db_xref="CDD:153295"
     Region          <245..476
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          490..561
                     /region_name="SH3_Bin1"
                     /note="Src Homology 3 domain of Bridging integrator 1
                     (Bin1), also called Amphiphysin-2; cd12139"
                     /db_xref="CDD:213015"
     Site            order(501..507,526,528..531,554,556..557)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:213015"
     CDS             1..562
                     /gene="BIN1"
                     /gene_synonym="AMPH2; AMPHL; CNM2; SH3P9"
                     /coded_by="NM_001320641.2:212..1900"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="GeneID:274"
                     /db_xref="HGNC:HGNC:1052"
                     /db_xref="MIM:601248"
ORIGIN      
        1 maemgskgvt agkiasnvqk kltraqekvl qklgkadetk deqfeqcvqn fnkqltegtr
       61 lqkdlrtyla svkamheask klneclqevy epdwpgrdea nkiaenndll wmdyhqklvd
      121 qalltmdtyl gqfpdiksri akrgrklvdy dsarhhyesl qtakkkdeak iakaeeelik
      181 aqkvfeemnv dlqeelpslw nsrvgfyvnt fqsiagleen fhkemsklnq nlndvlvgle
      241 kqhgsntftv kaqpsdnapa kgnkspsppd gspaatpeir vnhepepagg atpgatlpks
      301 psqlrkgppv ppppkhtpsk evkqeqilsl fedtfvpeis vttpsqfeap gpfseqasll
      361 dldfdplppv tspvkaptps gqsipwdlwe ptespagslp sgepsaaegt favswpsqta
      421 epgpaqpaea sevaggtqpa agaqepgeta aseaassslp avvvetfpat vngtveggsg
      481 agrldlppgf mfkvqaqhdy tatdtdelql kagdvvlvip fqnpeeqdeg wlmgvkesdw
      541 nqhkelekcr gvfpenfter vp
//
LOCUS       NP_001311317             418 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox-containing protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001311317
VERSION     NP_001311317.1
DBSOURCE    REFSEQ: accession NM_001324388.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Chen,X., Zha,G., Li,C. and Wang,K.
  TITLE     High expression of HMBOX1 promotes the progression of lung squamous
            cell carcinoma
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (5), 198-203 (2024)
   PUBMED   38814216
  REMARK    GeneRIF: High expression of HMBOX1 promotes the progression of lung
            squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Zhou,C., Wei,W., Ma,J., Yang,Y., Liang,L., Zhang,Y., Wang,Z.,
            Chen,X., Huang,L., Wang,W. and Wu,S.
  TITLE     Cancer-secreted exosomal miR-1468-5p promotes tumor immune escape
            via the immunosuppressive reprogramming of lymphatic vessels
  JOURNAL   Mol Ther 29 (4), 1512-1528 (2021)
   PUBMED   33388421
  REMARK    GeneRIF: Cancer-secreted exosomal miR-1468-5p promotes tumor immune
            escape via the immunosuppressive reprogramming of lymphatic
            vessels.
            Erratum:[Mol Ther. 2022 Feb 2;30(2):976-977. doi:
            10.1016/j.ymthe.2021.12.014. PMID: 34982969]
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Dai,J., Wu,L., Zhang,C., Zheng,X., Tian,Z. and Zhang,J.
  TITLE     Recombinant expression of a novel human transcriptional repressor
            HMBOX1 and preparation of anti-HMBOX1 monoclonal antibody
  JOURNAL   Cell Mol Immunol 6 (4), 261-268 (2009)
   PUBMED   19728927
  REMARK    GeneRIF: decreased expression in hepatic carcinoma
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Dejardin,J. and Kingston,R.E.
  TITLE     Purification of proteins associated with specific genomic Loci
  JOURNAL   Cell 136 (1), 175-186 (2009)
   PUBMED   19135898
REFERENCE   8  (residues 1 to 418)
  AUTHORS   De Marco,A., Biancotto,C., Knezevich,A., Maiuri,P., Vardabasso,C.
            and Marcello,A.
  TITLE     Intragenic transcriptional cis-activation of the human
            immunodeficiency virus 1 does not result in allele-specific
            inhibition of the endogenous gene
  JOURNAL   Retrovirology 5, 98 (2008)
   PUBMED   18983639
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Chen,S., Saiyin,H., Zeng,X., Xi,J., Liu,X., Li,X. and Yu,L.
  TITLE     Isolation and functional analysis of human HMBOX1, a homeobox
            containing protein with transcriptional repressor activity
  JOURNAL   Cytogenet Genome Res 114 (2), 131-136 (2006)
   PUBMED   16825764
  REMARK    GeneRIF: Hmbox1 is widely expressed in pancreas and the expression
            of this gene can also be detected in pallium, hippocampus and
            hypothalamus
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC040975.8, DC395744.1, DC358620.1, AK290683.1, DQ153248.1,
            AC108449.5 and BQ019252.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.249946.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.1-p12"
     Protein         1..418
                     /product="homeobox-containing protein 1 isoform 5"
                     /note="homeobox-containing protein 1; homeobox
                     telomere-binding protein 1; homeobox-containing protein
                     PBHNF; telomere-associated homeobox-containing protein 1"
                     /calculated_mol_wt=46947
     Region          25..227
                     /region_name="HNF-1_N"
                     /note="Hepatocyte nuclear factor 1 (HNF-1), N terminus;
                     pfam04814"
                     /db_xref="CDD:461440"
     Region          56..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Site            170
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          268..340
                     /region_name="homeodomain"
                     /note="Homeodomain; DNA binding domains involved in the
                     transcriptional regulation of key eukaryotic developmental
                     processes; may bind to DNA as monomers or as homo- and/or
                     heterodimers, in a sequence-specific manner; cd00086"
                     /db_xref="CDD:238039"
     Site            order(268..272,274,291,297,325,327..328,331..332,334..336,
                     338..339)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            order(270,273,328,331..332,335)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Site            335
                     /site_type="other"
                     /note="Critical for recognition and binding of
                     5'-TTAGGG-3' motifs in telomeric DNA.
                     /evidence=ECO:0000269|PubMed:23685356; propagated from
                     UniProtKB/Swiss-Prot (Q6NT76.1)"
     Region          351..383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NT76.1)"
     CDS             1..418
                     /gene="HMBOX1"
                     /gene_synonym="HNF1LA; HOT1; PBHNF; TAH1"
                     /coded_by="NM_001324388.2:229..1485"
                     /note="isoform 5 is encoded by transcript variant 9"
                     /db_xref="GeneID:79618"
                     /db_xref="HGNC:HGNC:26137"
                     /db_xref="MIM:618610"
ORIGIN      
        1 mlssfpvvll etmshytdep rftieqidll qrlrrtgmtk heilhaletl drldqehsdk
       61 fgrrssyggs sygnstnnvp assstatast qtqhsgmsps psnsydtspq pcttnqngre
      121 nnerlstsng kmsptryhan smgqrsysfe aseedldvdd kveelmrrds svikeeikaf
      181 lanrrisqav vaqvtgisqs rishwllqqg sdlseqkkra fyrwyqlekt npgatlsmrp
      241 apipiedpew rqtpppvsat sgtfrlrrgs rftwrkecla vmesyfnenq ypdeakreei
      301 anacnaviqk pgkklsdler vtslkvynwf anrrkeikrr aniaileshg idvqspgghs
      361 nsddvdgndy seqddstshs dhqdpislav emaavnhtil alarqganei ktealddd
//
LOCUS       NP_001646                511 aa            linear   PRI 20-NOV-2025
DEFINITION  coatomer subunit delta isoform 1 [Homo sapiens].
ACCESSION   NP_001646
VERSION     NP_001646.2
DBSOURCE    REFSEQ: accession NM_001655.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 511)
  AUTHORS   O'Donoghue,L., Comer,S.P., Hiebner,D.W., Schoen,I., von
            Kriegsheim,A. and Smolenski,A.
  TITLE     RhoGAP6 interacts with COPI to regulate protein transport
  JOURNAL   Biochem J 480 (14), 1109-1127 (2023)
   PUBMED   37409526
REFERENCE   2  (residues 1 to 511)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 511)
  AUTHORS   Tidwell,T., Deshotel,M., Palumbos,J., Miller,C., Bayrak-Toydemir,P.
            and Carey,J.C.
  TITLE     Novel de novo ARCN1 intronic variant causes rhizomelic short
            stature with microretrognathia and developmental delay
  JOURNAL   Cold Spring Harb Mol Case Stud 6 (6), a005728 (2020)
   PUBMED   33154040
  REMARK    GeneRIF: Novel de novo ARCN1 intronic variant causes rhizomelic
            short stature with microretrognathia and developmental delay.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 511)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 511)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 511)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   7  (residues 1 to 511)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   8  (residues 1 to 511)
  AUTHORS   Radice,P., Pensotti,V., Jones,C., Perry,H., Pierotti,M.A. and
            Tunnacliffe,A.
  TITLE     The human archain gene, ARCN1, has highly conserved homologs in
            rice and Drosophila
  JOURNAL   Genomics 26 (1), 101-106 (1995)
   PUBMED   7782067
REFERENCE   9  (residues 1 to 511)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
REFERENCE   10 (residues 1 to 511)
  AUTHORS   Waters,M.G., Serafini,T. and Rothman,J.E.
  TITLE     'Coatomer': a cytosolic protein complex containing subunits of
            non-clathrin-coated Golgi transport vesicles
  JOURNAL   Nature 349 (6306), 248-251 (1991)
   PUBMED   1898986
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB216489.1, BC093636.1,
            CR988766.1, AU125652.1, BC080638.1 and AA856562.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 15, 2000 this sequence version replaced NP_001646.1.
            
            Summary: This gene maps in a region, which include the mixed
            lineage leukemia and Friend leukemia virus integration 1 genes,
            where multiple disease-associated chromosome translocations occur.
            It is an intracellular protein. Archain sequences are well
            conserved among eukaryotes and this protein may play a fundamental
            role in eukaryotic cell biology. It has similarities to heat shock
            proteins and clathrin-associated proteins, and may be involved in
            vesicle structure or trafficking. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.157670.1,
                                           SRR1803616.34747.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000264028.5/ ENSP00000264028.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..511
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..511
                     /product="coatomer subunit delta isoform 1"
                     /note="coatomer protein delta-COP; coatomer protein
                     complex, subunit delta; archain vesicle transport protein
                     1; coatomer delta subunit; delta-coat protein; COPI coat
                     complex subunit delta"
                     /calculated_mol_wt=57079
     Region          4..133
                     /region_name="Delta_COP_N"
                     /note="delta subunit of the F-COPI complex, N-terminal
                     domain; cd14830"
                     /db_xref="CDD:341434"
     Region          168..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P48444.1)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Region          272..508
                     /region_name="AP_delta-COPI_MHD"
                     /note="Mu homology domain (MHD) of adaptor protein (AP)
                     coat protein I (COPI) delta subunit; cd09254"
                     /db_xref="CDD:271162"
     Site            309
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            351
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q5XJY5; propagated from
                     UniProtKB/Swiss-Prot (P48444.1)"
     Site            493
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P48444.1)"
     CDS             1..511
                     /gene="ARCN1"
                     /gene_synonym="COPD; SRMMD; SSMG"
                     /coded_by="NM_001655.5:140..1675"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8400.1"
                     /db_xref="GeneID:372"
                     /db_xref="HGNC:HGNC:649"
                     /db_xref="MIM:600820"
ORIGIN      
        1 mvllaaavct kagkaivsrq fvemtrtrie gllaafpklm ntgkqhtfve tesvryvyqp
       61 meklymvlit tknsniledl etlrlfsrvi peycraleen eisehcfdli fafdeivalg
      121 yrenvnlaqi rtftemdshe ekvfravret qereakaemr rkakelqqar rdaerqgkka
      181 pgfggfgssa vsggstaami tetiietdkp kvapaparps gpskalklga kgkevdnfvd
      241 klksegetim sssmgkrtse atkmhappin mesvhmkiee kitltcgrdg glqnmelhgm
      301 imlrisddky grirlhvene dkkgvqlqth pnvdkklfta esliglknpe ksfpvnsdvg
      361 vlkwrlqtte esfipltinc wpsesgngcd vnieyelqed nlelndvvit iplpsgvgap
      421 vigeidgeyr hdsrrntlew clpvidaknk sgslefsiag qpndffpvqv sfvskknycn
      481 iqvtkvtqvd gnspvrfste ttflvdkyei l
//
LOCUS       NP_006775                943 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 3 [Homo sapiens].
ACCESSION   NP_006775
VERSION     NP_006775.1
DBSOURCE    REFSEQ: accession NM_006784.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 943)
  AUTHORS   Liu,W., Xie,A., Xiong,J., Li,S., Yang,L. and Liu,W.
  TITLE     WDR3 promotes stem cell-like properties in prostate cancer by
            inhibiting USF2-mediated transcription of RASSF1A
  JOURNAL   J Gene Med 25 (7), e3498 (2023)
   PUBMED   36905106
  REMARK    GeneRIF: WDR3 promotes stem cell-like properties in prostate cancer
            by inhibiting USF2-mediated transcription of RASSF1A.
REFERENCE   2  (residues 1 to 943)
  AUTHORS   Moraleva,A.A., Deryabin,A.S., Rubtsov,Y.P., Rubtsova,M.P. and
            Dontsova,O.A.
  TITLE     Eukaryotic Ribosome Biogenesis: The 40S Subunit
  JOURNAL   Acta Naturae 14 (1), 14-30 (2022)
   PUBMED   35441050
REFERENCE   3  (residues 1 to 943)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 943)
  AUTHORS   Su,W., Zhu,S., Chen,K., Yang,H., Tian,M., Fu,Q., Shi,G., Feng,S.,
            Ren,D., Jin,X. and Yang,C.
  TITLE     Overexpressed WDR3 induces the activation of Hippo pathway by
            interacting with GATA4 in pancreatic cancer
  JOURNAL   J Exp Clin Cancer Res 40 (1), 88 (2021)
   PUBMED   33648545
  REMARK    GeneRIF: Overexpressed WDR3 induces the activation of Hippo pathway
            by interacting with GATA4 in pancreatic cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 943)
  AUTHORS   Kobayashi,M., Jitoku,D., Iwayama,Y., Yamamoto,N., Toyota,T.,
            Suzuki,K., Kikuchi,M., Hashimoto,T., Kanahara,N., Kurumaji,A.,
            Yoshikawa,T. and Nishikawa,T.
  TITLE     Association studies of WD repeat domain 3 and
            chitobiosyldiphosphodolichol beta-mannosyltransferase genes with
            schizophrenia in a Japanese population
  JOURNAL   PLoS One 13 (1), e0190991 (2018)
   PUBMED   29309433
  REMARK    GeneRIF: evaluated the genetic association of WDR3 and ALG1 in
            schizophrenia. We examined 21 single nucleotide polymorphisms
            [SNPs; W1 (rs1812607)-W16 (rs6656360), A1 (rs8053916)-A10
            (rs9673733)] from these genes using the Japanese case-control
            sample (1,808 schizophrenics and 2,170 matched controls). No
            significant genetic associations of these SNPs were identified.
            However, we detected a significant association of W4 (rs319471)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 943)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   7  (residues 1 to 943)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   8  (residues 1 to 943)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   9  (residues 1 to 943)
  AUTHORS   Claudio,J.O., Liew,C.C., Ma,J., Heng,H.H., Stewart,A.K. and
            Hawley,R.G.
  TITLE     Cloning and expression analysis of a novel WD repeat gene, WDR3,
            mapping to 1p12-p13
  JOURNAL   Genomics 59 (1), 85-89 (1999)
   PUBMED   10395803
REFERENCE   10 (residues 1 to 943)
  AUTHORS   Claudio,J.O., Liew,C.C., Dempsey,A.A., Cukerman,E., Stewart,A.K.,
            Na,E., Atkins,H.L., Iscove,N.N. and Hawley,R.G.
  TITLE     Identification of sequence-tagged transcripts differentially
            expressed within the human hematopoietic hierarchy
  JOURNAL   Genomics 50 (1), 44-52 (1998)
   PUBMED   9628821
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121993.7, BP281064.1,
            AK292438.1, AF083217.1, BU685597.1 and AA258068.1.
            
            Summary: This gene encodes a nuclear protein containing 10 WD
            repeats. WD repeats are approximately 30- to 40-amino acid domains
            containing several conserved residues, which usually include a
            trp-asp at the C-terminal end. Proteins belonging to the WD repeat
            family are involved in a variety of cellular processes, including
            cell cycle progression, signal transduction, apoptosis, and gene
            regulation. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.27264.1,
                                           SRR1660807.233060.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000349139.6/ ENSP00000308179.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..943
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..943
                     /product="WD repeat-containing protein 3"
                     /note="dJ776P7.2 (WD repeat domain 3)"
                     /calculated_mol_wt=105968
     Region          21..60
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          49..621
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          63..102
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          68..104
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          105..144
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          111..146
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          147..186
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          152..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          189..228
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          194..220
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Site            257
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          277..316
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          326..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          407..703
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          413..451
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Site            order(414,432,436,441..442,471,475,481..482,494..495,512,
                     517,523..524,565,570,576..577,589..590,608,612,618..619,
                     631..632,649,654,660..661,673..674,692,696,702..703)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          420..454
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          453..493
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          462..494
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          494..533
                     /region_name="WD 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          500..548
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..586
                     /region_name="WD 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          552..588
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          589..630
                     /region_name="WD 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          595..630
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          631..670
                     /region_name="WD 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          636..672
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          673..712
                     /region_name="WD 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Site            726
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNX4.1)"
     Region          804..907
                     /region_name="Utp12"
                     /note="Dip2/Utp12 Family; pfam04003"
                     /db_xref="CDD:461125"
     CDS             1..943
                     /gene="WDR3"
                     /gene_synonym="DIP2; UTP12"
                     /coded_by="NM_006784.3:77..2908"
                     /db_xref="CCDS:CCDS898.1"
                     /db_xref="GeneID:10885"
                     /db_xref="HGNC:HGNC:12755"
                     /db_xref="MIM:604737"
ORIGIN      
        1 mgltkqylry vasavfgvig sqkgnivfvt lrgekgryva vpacehvfiw dlrkgekili
       61 lqglkqevtc lcpspdglhl avgyedgsir ifsllsgegn vtfnghkaai ttlkydqlgg
      121 rlasgskdtd iivwdvines glyrlkghkd aitqalflre knllvtsgkd tmvkwwdldt
      181 qhcfktmvgh rtevwglvll seekrlitga sdselrvwdi aylqeiedpe epdpkkikgs
      241 spgiqdtlea edgafetdea pedrilscrk agsimregrd rvvnlavdkt grilachgtd
      301 svlelfcils kkeiqkkmdk kmkkarkkak lhsskgeeed pevnvemslq deiqrvtnik
      361 tsakiksfdl ihsphgelka vfllqnnlve lyslnpslpt pqpvrtsrit igghrsdvrt
      421 lsfssdniav lsaaadsiki wnrstlqcir tmtceyalcs ffvpgdrqvv igtktgklql
      481 ydlasgnlle tidahdgalw smslspdqrg fvtggadksv kfwdfelvkd enstqkrlsv
      541 kqtrtlqlde dvlcvsyspn qkllavslld ctvkifyvdt lkfflslygh klpvicmdis
      601 hdgaliatgs adrnvkiwgl dfgdchkslf ahddsvmylq fvpkshlfft agkdhkikqw
      661 dadkfehiqt leghhqeiwc lavspsgdyv vssshdkslr lwertrepli leeeremere
      721 aeyeesvake dqpavpgetq gdsyftgkkt ietvkaaeri meaielyree takmkehkai
      781 ckaagkevpl psnpilmayg sispsayvle ifkgikssel eesllvlpfs yvpdilklfn
      841 efiqlgsdve licrclffll rihfgqitsn qmlvpviekl rettiskvsq vrdvigfnma
      901 gldylkrece aksevmffad atshleekkr krkkreklil tlt
//
LOCUS       NP_940927               1343 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF7 [Homo sapiens].
ACCESSION   NP_940927 XP_351009
VERSION     NP_940927.2
DBSOURCE    REFSEQ: accession NM_198525.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1343)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1343)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 1343)
  AUTHORS   Blasius,T.L., Yue,Y., Prasad,R., Liu,X., Gennerich,A. and
            Verhey,K.J.
  TITLE     Sequences in the stalk domain regulate auto-inhibition and ciliary
            tip localization of the immotile kinesin-4 KIF7
  JOURNAL   J Cell Sci 134 (13) (2021)
   PUBMED   34114033
  REMARK    GeneRIF: Sequences in the stalk domain regulate auto-inhibition and
            ciliary tip localization of the immotile kinesin-4 KIF7.
REFERENCE   4  (residues 1 to 1343)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 1343)
  AUTHORS   Katoh,Y. and Katoh,M.
  TITLE     KIF27 is one of orthologs for Drosophila Costal-2
  JOURNAL   Int J Oncol 25 (6), 1875-1880 (2004)
   PUBMED   15547729
REFERENCE   6  (residues 1 to 1343)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   7  (residues 1 to 1343)
  AUTHORS   Miki,H., Setou,M., Kaneshiro,K. and Hirokawa,N.
  TITLE     All kinesin superfamily protein, KIF, genes in mouse and human
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7004-7011 (2001)
   PUBMED   11416179
  REMARK    Review article
REFERENCE   8  (residues 1 to 1343)
  AUTHORS   Bayoumi,R., Saar,K., Lee,Y.A., Nurnberg,G., Reis,A., Nur-E-Kamal,M.
            and Al-Gazali,L.I.
  TITLE     Localisation of a gene for an autosomal recessive syndrome of
            macrocephaly, multiple epiphyseal dysplasia, and distinctive facies
            to chromosome 15q26
  JOURNAL   J Med Genet 38 (6), 369-373 (2001)
   PUBMED   11389160
REFERENCE   9  (residues 1 to 1343)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 1343)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC013787.15, BC042063.1,
            BC104044.1, BC112273.1, AY358384.1 and AW451733.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 17, 2008 this sequence version replaced NP_940927.1.
            
            Summary: This gene encodes a cilia-associated protein belonging to
            the kinesin family. This protein plays a role in the sonic hedgehog
            (SHH) signaling pathway through the regulation of GLI transcription
            factors. It functions as a negative regulator of the SHH pathway by
            preventing inappropriate activation of GLI2 in the absence of
            ligand, and as a positive regulator by preventing the processing of
            GLI3 into its repressor form. Mutations in this gene have been
            associated with various ciliopathies. [provided by RefSeq, Oct
            2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.3183965.1,
                                           SRR14038193.1406546.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000394412.8/ ENSP00000377934.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1343
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..1343
                     /product="kinesin-like protein KIF7"
                     /note="EQYK340"
                     /calculated_mol_wt=150457
     Region          15..350
                     /region_name="KISc_KIF4"
                     /note="Kinesin motor domain, KIF4-like subfamily; cd01372"
                     /db_xref="CDD:276823"
     Site            order(23,94,97,99..102,252)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276823"
     Site            order(302,305,308)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276823"
     Region          356..382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          358..1206
                     /region_name="Interaction with SMO.
                     /evidence=ECO:0000250|UniProtKB:B7ZNG0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          358..479
                     /region_name="Interaction with DLG5.
                     /evidence=ECO:0000250|UniProtKB:B7ZNG0"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          451..483
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          513..775
                     /region_name="Sufficient for interaction with NPHP1.
                     /evidence=ECO:0000269|PubMed:21633164"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          611..639
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          <702..>1198
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     Site            898
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B7ZNG0; propagated from
                     UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          1219..1238
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     Region          1310..1343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2M1P5.2)"
     CDS             1..1343
                     /gene="KIF7"
                     /gene_synonym="ACLS; AGBK; HLS2; JBTS12; MMEDF; UNQ340"
                     /coded_by="NM_198525.3:94..4125"
                     /db_xref="CCDS:CCDS32325.2"
                     /db_xref="GeneID:374654"
                     /db_xref="HGNC:HGNC:30497"
                     /db_xref="MIM:611254"
ORIGIN      
        1 mgleaqrlpg aeeapvrval rvrpllpkel lhghqsclqv epglgrvtlg rdrhfgfhvv
       61 laedagqeav yqacvqplle affegfnatv faygqtgsgk tytmgeasva slledeqgiv
      121 pramaeafkl idendlldcl vhvsylevyk eefrdllevg tasrdiqlre dergnvvlcg
      181 vkevdvegld evlsllemgn aarhtgathl nhlssrshtv ftvtleqrgr apsrlprpap
      241 gqllvskfhf vdlagservl ktgstgerlk esiqinssll algnvisalg dpqrrgship
      301 yrdskitril kdslggnakt vmiacvspss sdfdetlntl nyasraqnir nratvnwrpe
      361 aerppeetas gargpprhrs etriihrgrr apgpatasaa aamrlgaeca ryractdaay
      421 sllrelqaep glpgaaarkv rdwlcavege rsalssasgp dsgiesasve dqaaqgaggr
      481 kedegaqqll tlqnqvarle eenrdflaal edameqyklq sdrlreqqee mvelrlrlel
      541 vrpgwggprl lnglppgsfv prphtaplgg ahahvlgmvp paclpgdevg seqrgeqvtn
      601 greagaellt evnrlgsgss aaseeeeeee epprrtlhlr rnrisncsqr agarpgslpe
      661 rkgpelclee ldaaipgsra vggskarvqa rqvppatase wrlaqaqqki relainirmk
      721 eeligelvrt gkaaqalnrq hsqrireleq eaeqvraels egqrqlrele gkelqdager
      781 srlqefrrrv aaaqsqvqvl kekkqaterl vslsaqsekr lqelernvql mrqqqgqlqr
      841 rlreeteqkr rleaemskrq hrvkelelkh eqqqkilkik teeiaafqrk rrsgsngsvv
      901 sleqqqkiee qkkwldqeme kvlqqrrale elgeelhkre ailakkealm qektgleskr
      961 lrssqalned ivrvssrleh lekelseksg qlrqgsaqsq qqirgeidsl rqekdsllkq
     1021 rleidgklrq gsllspeeer tlfqldeaie aldaaieykn eaitcrqrvl rasasllsqc
     1081 emnlmaklsy lsssetrall ckyfdkvvtl reeqhqqqia fselemqlee qqrlvywlev
     1141 alerqrlemd rqltlqqkeh eqnmqlllqq srdhlgegla dsrrqyeari qalekelgry
     1201 mwinqelkqk lggvnavghs rggekrslcs egrqapgned elhlapellw lspltegapr
     1261 treetrdlvh aplpltwkrs slcgeeqgsp eelrqreaae plvgrvlpvg eaglpwnfgp
     1321 lskprrelrr aspgmidvrk npl
//
LOCUS       NP_001157565             275 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 7a [Homo sapiens].
ACCESSION   NP_001157565
VERSION     NP_001157565.1
DBSOURCE    REFSEQ: accession NM_001164093.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 275)
  AUTHORS   Poh,J., Ponsford,A.H., Boyd,J., Woodsmith,J., Stelzl,U., Wanker,E.,
            Harper,N., MacEwan,D. and Sanderson,C.M.
  TITLE     A functionally defined high-density NRF2 interactome reveals new
            conditional regulators of ARE transactivation
  JOURNAL   Redox Biol 37, 101686 (2020)
   PUBMED   32911434
REFERENCE   4  (residues 1 to 275)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 275)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 275)
  AUTHORS   Wei,N., Serino,G. and Deng,X.W.
  TITLE     The COP9 signalosome: more than a protease
  JOURNAL   Trends Biochem Sci 33 (12), 592-600 (2008)
   PUBMED   18926707
  REMARK    Review article
REFERENCE   7  (residues 1 to 275)
  AUTHORS   Lyapina,S., Cope,G., Shevchenko,A., Serino,G., Tsuge,T., Zhou,C.,
            Wolf,D.A., Wei,N., Shevchenko,A. and Deshaies,R.J.
  TITLE     Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome
  JOURNAL   Science 292 (5520), 1382-1385 (2001)
   PUBMED   11337588
REFERENCE   8  (residues 1 to 275)
  AUTHORS   Bech-Otschir,D., Kraft,R., Huang,X., Henklein,P., Kapelari,B.,
            Pollmann,C. and Dubiel,W.
  TITLE     COP9 signalosome-specific phosphorylation targets p53 to
            degradation by the ubiquitin system
  JOURNAL   EMBO J 20 (7), 1630-1639 (2001)
   PUBMED   11285227
REFERENCE   9  (residues 1 to 275)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 275)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC355036.1, AK292621.1,
            BC011789.2 and BQ008460.1.
            
            Summary: This gene encodes a component of the COP9 signalosome, an
            evolutionarily conserved multi-subunit protease that regulates the
            activity of the ubiquitin conjugation pathway. Alternatively
            spliced transcript variants that encode the same protein have been
            described. [provided by RefSeq, Mar 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1070662.1, AK292621.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.31"
     Protein         1..275
                     /product="COP9 signalosome complex subunit 7a"
                     /note="COP9 complex subunit 7a; COP9 constitutive
                     photomorphogenic homolog subunit 7A; dermal
                     papilla-derived protein 10; JAB1-containing signalosome
                     subunit 7a"
                     /calculated_mol_wt=30146
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:18850735; propagated from
                     UniProtKB/Swiss-Prot (Q9UBW8.1)"
     Region          87..177
                     /region_name="PINT"
                     /note="motif in proteasome subunits, Int-6, Nip-1 and
                     TRIP-15; smart00088"
                     /db_xref="CDD:214509"
     Region          166..215
                     /region_name="CSN7a_helixI"
                     /note="COP9 signalosome complex subunit 7a helix I domain;
                     pfam18392"
                     /db_xref="CDD:465740"
     Region          227..275
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBW8.1)"
     CDS             1..275
                     /gene="COPS7A"
                     /gene_synonym="CSN7; CSN7A; SGN7a"
                     /coded_by="NM_001164093.2:371..1198"
                     /db_xref="CCDS:CCDS8558.1"
                     /db_xref="GeneID:50813"
                     /db_xref="HGNC:HGNC:16758"
                     /db_xref="MIM:616009"
ORIGIN      
        1 msaevkvtgq nqeqflllak sakgaalatl ihqvleapgv yvfgelldmp nvrelaesdf
       61 astfrlltvf aygtyadyla earnlpplte aqknklrhls vvtlaakvkc ipyavlleal
      121 alrnvrqled lvieavyadv lrgsldqrnq rlevdysigr diqrqdlsai artlqewcvg
      181 cevvlsgiee qvsranqhke qqlglkqqie sevanlkkti kvttaaaaaa tsqdpeqhlt
      241 elrepapgtn qrqpskkask gkglrgsaki wsksn
//
LOCUS       NP_001317437             579 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 40 isoform 3 [Homo sapiens].
ACCESSION   NP_001317437 XP_005257549
VERSION     NP_001317437.1
DBSOURCE    REFSEQ: accession NM_001330508.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 579)
  AUTHORS   Wilken,A., Hoben,I.M., Wolter,A., Loges,N.T., Olbrich,H., Aprea,I.,
            Dworniczak,B., Raidt,J. and Omran,H.
  TITLE     Primary Ciliary Dyskinesia Associated Disease-Causing Variants in
            CCDC39 and CCDC40 Cause Axonemal Absence of Inner Dynein Arm Heavy
            Chains DNAH1, DNAH6, and DNAH7
  JOURNAL   Cells 13 (14), 1200 (2024)
   PUBMED   39056782
  REMARK    GeneRIF: Primary Ciliary Dyskinesia Associated Disease-Causing
            Variants in CCDC39 and CCDC40 Cause Axonemal Absence of Inner
            Dynein Arm Heavy Chains DNAH1, DNAH6, and DNAH7.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 579)
  AUTHORS   Liu,L., Zhou,K., Song,Y. and Liu,X.
  TITLE     CCDC40 mutation as a cause of infertility in a Chinese family with
            primary ciliary dyskinesia
  JOURNAL   Medicine (Baltimore) 100 (51), e28275 (2021)
   PUBMED   34941110
  REMARK    GeneRIF: CCDC40 mutation as a cause of infertility in a Chinese
            family with primary ciliary dyskinesia.
REFERENCE   3  (residues 1 to 579)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 579)
  AUTHORS   Fassad,M.R., Shoman,W.I., Morsy,H., Patel,M.P., Radwan,N.,
            Jenkins,L., Cullup,T., Fouda,E., Mitchison,H.M. and Fasseeh,N.
  TITLE     Clinical and genetic spectrum in 33 Egyptian families with
            suspected primary ciliary dyskinesia
  JOURNAL   Clin Genet 97 (3), 509-515 (2020)
   PUBMED   31650533
  REMARK    GeneRIF: Clinical and genetic spectrum in 33 Egyptian families with
            suspected primary ciliary dyskinesia.
REFERENCE   5  (residues 1 to 579)
  AUTHORS   Antony,D., Becker-Heck,A., Zariwala,M.A., Schmidts,M.,
            Onoufriadis,A., Forouhan,M., Wilson,R., Taylor-Cox,T., Dewar,A.,
            Jackson,C., Goggin,P., Loges,N.T., Olbrich,H., Jaspers,M.,
            Jorissen,M., Leigh,M.W., Wolf,W.E., Daniels,M.L., Noone,P.G.,
            Ferkol,T.W., Sagel,S.D., Rosenfeld,M., Rutman,A., Dixit,A.,
            O'Callaghan,C., Lucas,J.S., Hogg,C., Scambler,P.J., Emes,R.D.,
            Chung,E.M., Shoemark,A., Knowles,M.R., Omran,H. and Mitchison,H.M.
  CONSRTM   Uk10k
  TITLE     Mutations in CCDC39 and CCDC40 are the major cause of primary
            ciliary dyskinesia with axonemal disorganization and absent inner
            dynein arms
  JOURNAL   Hum Mutat 34 (3), 462-472 (2013)
   PUBMED   23255504
  REMARK    GeneRIF: This study shows that CCDC39 and CCDC40 mutations are the
            major cause of Primary ciliary dyskinesia in patients with the
            previously termed 'radial spoke defect'.
REFERENCE   6  (residues 1 to 579)
  AUTHORS   Blanchon,S., Legendre,M., Copin,B., Duquesnoy,P., Montantin,G.,
            Kott,E., Dastot,F., Jeanson,L., Cachanado,M., Rousseau,A.,
            Papon,J.F., Beydon,N., Brouard,J., Crestani,B., Deschildre,A.,
            Desir,J., Dollfus,H., Leheup,B., Tamalet,A., Thumerelle,C.,
            Vojtek,A.M., Escalier,D., Coste,A., de Blic,J., Clement,A.,
            Escudier,E. and Amselem,S.
  TITLE     Delineation of CCDC39/CCDC40 mutation spectrum and associated
            phenotypes in primary ciliary dyskinesia
  JOURNAL   J Med Genet 49 (6), 410-416 (2012)
   PUBMED   22693285
  REMARK    GeneRIF: Aiming to delineate the CCDC39/CCDC40 mutation spectrum
            and associated phenotypes, a large cohort of patients with IDA
            defects were screened. Biallelic CCDC39 or CCDC40 mutations were
            identified in 30/34 unrelated families with IDA defects.
REFERENCE   7  (residues 1 to 579)
  AUTHORS   Nakhleh,N., Francis,R., Giese,R.A., Tian,X., Li,Y., Zariwala,M.A.,
            Yagi,H., Khalifa,O., Kureshi,S., Chatterjee,B., Sabol,S.L.,
            Swisher,M., Connelly,P.S., Daniels,M.P., Srinivasan,A., Kuehl,K.,
            Kravitz,N., Burns,K., Sami,I., Omran,H., Barmada,M., Olivier,K.,
            Chawla,K.K., Leigh,M., Jonas,R., Knowles,M., Leatherbury,L. and
            Lo,C.W.
  TITLE     High prevalence of respiratory ciliary dysfunction in congenital
            heart disease patients with heterotaxy
  JOURNAL   Circulation 125 (18), 2232-2242 (2012)
   PUBMED   22499950
REFERENCE   8  (residues 1 to 579)
  AUTHORS   Becker-Heck,A., Zohn,I.E., Okabe,N., Pollock,A., Lenhart,K.B.,
            Sullivan-Brown,J., McSheene,J., Loges,N.T., Olbrich,H.,
            Haeffner,K., Fliegauf,M., Horvath,J., Reinhardt,R., Nielsen,K.G.,
            Marthin,J.K., Baktai,G., Anderson,K.V., Geisler,R., Niswander,L.,
            Omran,H. and Burdine,R.D.
  TITLE     The coiled-coil domain containing protein CCDC40 is essential for
            motile cilia function and left-right axis formation
  JOURNAL   Nat Genet 43 (1), 79-84 (2011)
   PUBMED   21131974
  REMARK    GeneRIF: CCDC40 mutations in humans result in a variant of primary
            ciliary dyskinesia characterized by misplacement of the central
            pair of microtubules and defective assembly of inner dynein arms
            and dynein regulatory complexes.
REFERENCE   9  (residues 1 to 579)
  AUTHORS   Wang,J., Lin,J., Chang,Y., Li,P. and Yang,Y.
  TITLE     MCM3AP, a novel HBV integration site in hepatocellular carcinoma
            and its implication in hepatocarcinogenesis
  JOURNAL   J Huazhong Univ Sci Technolog Med Sci 30 (4), 425-429 (2010)
   PUBMED   20714864
REFERENCE   10 (residues 1 to 579)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC116025.21.
            
            On Aug 29, 2016 this sequence version replaced XP_005257549.1.
            
            Summary: This gene encodes a protein that is necessary for motile
            cilia function. It functions in correct left-right axis formation
            by regulating the assembly of the inner dynein arm and the dynein
            regulatory complexes, which control ciliary beat. Mutations in this
            gene cause ciliary dyskinesia type 15, a disorder due to defects in
            cilia motility. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Aug 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK000760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2145240
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..579
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     Protein         1..579
                     /product="coiled-coil domain-containing protein 40 isoform
                     3"
                     /note="coiled-coil domain-containing protein 40;
                     coiled-coil domain containing 40"
                     /calculated_mol_wt=63877
     Region          1..197
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Region          251..274
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Site            252
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8BI79; propagated from
                     UniProtKB/Swiss-Prot (Q4G0X9.2)"
     Region          <299..>481
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..579
                     /gene="CCDC40"
                     /gene_synonym="CFAP172; CILD15; FAP172"
                     /coded_by="NM_001330508.2:22..1761"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82212.1"
                     /db_xref="GeneID:55036"
                     /db_xref="HGNC:HGNC:26090"
                     /db_xref="MIM:613799"
ORIGIN      
        1 maepggaagr shpedgsase gekegnnesh mvsppekddg qkgeeavgst ehpeevttqa
       61 eaaieegeve tegeaavege eeavsygdae seeeyyytet sspegqisaa dttypyfspp
      121 qelpgeeayd svsgeaglqg fqqeatgppe srerrvtspe pshgvlgpse qmgqvtsgpa
      181 vgrltgstee pqgqvlpmgv qhrfrlshgs diessdleef vsqepvippg vpdahpregd
      241 lpvfqdqiqq psteegamae rvesegsdee aedegsqlvv ldpdhplmvr fqaalknyln
      301 rqieklkldl qelvvatkqs raqrqelgvn lyevqqhlvh lqkllekshd rhamasserr
      361 qkeeelqaar alytktcaaa neerkklaal qtemenlalh lfymqnidqd mrddirvmtq
      421 vvkkaeteri raeiekkkqd lyvdqlttra qqleedialf eaqylaqaed trilrkavse
      481 acteidaisv ekrrimqqwa sslvgmkhrd eahravleal svslerfpsq nintarsrls
      541 ttwhsagill rgsflpgasr afasvcygga avdnrirec
//
LOCUS       NP_003481                580 aa            linear   PRI 20-NOV-2025
DEFINITION  synapsin-3 isoform IIIa [Homo sapiens].
ACCESSION   NP_003481 XP_011528708
VERSION     NP_003481.3
DBSOURCE    REFSEQ: accession NM_003490.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 580)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 580)
  AUTHORS   Baris,R.O., Sahin,N., Bilgic,A.D., Ozdemir,C. and Edgunlu,T.G.
  TITLE     Molecular and in silico analyses of SYN III gene variants in autism
            spectrum disorder
  JOURNAL   Ir J Med Sci 192 (6), 2887-2895 (2023)
   PUBMED   37166614
  REMARK    GeneRIF: Molecular and in silico analyses of SYN III gene variants
            in autism spectrum disorder.
REFERENCE   3  (residues 1 to 580)
  AUTHORS   Bolat,H., Unsel-Bolat,G., Ozgul,S., Pariltay,E., Tahillioglu,A.,
            Rohde,L.A., Akin,H. and Ercan,E.S.
  TITLE     Investigation of possible associations of the BDNF, SNAP-25 and SYN
            III genes with the neurocognitive measures: BDNF and SNAP-25 genes
            might be involved in attention domain, SYN III gene in executive
            function
  JOURNAL   Nord J Psychiatry 76 (8), 610-615 (2022)
   PUBMED   35077325
  REMARK    GeneRIF: Investigation of possible associations of the BDNF,
            SNAP-25 and SYN III genes with the neurocognitive measures: BDNF
            and SNAP-25 genes might be involved in attention domain, SYN III
            gene in executive function.
REFERENCE   4  (residues 1 to 580)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 580)
  AUTHORS   Longhena,F., Faustini,G., Varanita,T., Zaltieri,M., Porrini,V.,
            Tessari,I., Poliani,P.L., Missale,C., Borroni,B., Padovani,A.,
            Bubacco,L., Pizzi,M., Spano,P. and Bellucci,A.
  TITLE     Synapsin III is a key component of alpha-synuclein fibrils in Lewy
            bodies of PD brains
  JOURNAL   Brain Pathol 28 (6), 875-888 (2018)
   PUBMED   29330884
  REMARK    GeneRIF: Synapsin III is a crucial alpha-synuclein interactant and
            a key component of Lewy bodies fibrils in the brain of patients
            affected by Parkinson's disease.
REFERENCE   6  (residues 1 to 580)
  AUTHORS   Porton,B., Ferreira,A., DeLisi,L.E. and Kao,H.T.
  TITLE     A rare polymorphism affects a mitogen-activated protein kinase site
            in synapsin III: possible relationship to schizophrenia
  JOURNAL   Biol Psychiatry 55 (2), 118-125 (2004)
   PUBMED   14732590
  REMARK    GeneRIF: A missense polymorphism, S470N, was identified in the
            synapsin III gene and appeared more frequently in individuals with
            schizophrenia. The site affected by the polymorphism, Ser470, was
            determined to be a substrate for mitogen-activated protein kinase.
REFERENCE   7  (residues 1 to 580)
  AUTHORS   Tsai,M.T., Hung,C.C., Tsai,C.Y., Liu,M.Y., Su,Y.C., Chen,Y.H.,
            Hsiao,K.J. and Chen,C.H.
  TITLE     Mutation analysis of synapsin III gene in schizophrenia
  JOURNAL   Am J Med Genet 114 (1), 79-83 (2002)
   PUBMED   11840510
  REMARK    GeneRIF: Evidence is not in favor of a large effect of synapsin III
            gene in the pathogenesis of schizophrenia.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Hilfiker,S., Stefani,G., Pieribone,V.A.,
            DeSalle,R. and Greengard,P.
  TITLE     Molecular evolution of the synapsin gene family
  JOURNAL   J Exp Zool 285 (4), 360-377 (1999)
   PUBMED   10578110
REFERENCE   9  (residues 1 to 580)
  AUTHORS   Porton,B., Kao,H.T. and Greengard,P.
  TITLE     Characterization of transcripts from the synapsin III gene locus
  JOURNAL   J Neurochem 73 (6), 2266-2271 (1999)
   PUBMED   10582583
REFERENCE   10 (residues 1 to 580)
  AUTHORS   Kao,H.T., Porton,B., Czernik,A.J., Feng,J., Yiu,G., Haring,M.,
            Benfenati,F. and Greengard,P.
  TITLE     A third member of the synapsin gene family
  JOURNAL   Proc Natl Acad Sci U S A 95 (8), 4667-4672 (1998)
   PUBMED   9539796
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z83846.1, Z98256.1, Z82246.2,
            Z80902.2, Z82181.2 and Z71183.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Apr 24, 2019 this sequence version replaced
            XP_011528708.1, NP_003481.2.
            
            Summary: This gene is a member of the synapsin gene family.
            Synapsins encode neuronal phosphoproteins which associate with the
            cytoplasmic surface of synaptic vesicles. Family members are
            characterized by common protein domains, and they are implicated in
            synaptogenesis and the modulation of neurotransmitter release,
            suggesting a potential role in several neuropsychiatric diseases.
            The protein encoded by this gene shares the synapsin family domain
            model, with domains A, C, and E exhibiting the highest degree of
            conservation. The protein contains a unique domain J, located
            between domains C and E. Based on this gene's localization to
            22q12.3, a possible schizophrenia susceptibility locus, and the
            established neurobiological roles of the synapsins, this family
            member may represent a candidate gene for schizophrenia. The TIMP3
            gene is located within an intron of this gene and is transcribed in
            the opposite direction. Alternative splicing of this gene results
            in multiple splice variants that encode different isoforms.
            [provided by RefSeq, Oct 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.158655.1,
                                           SRR1803611.24598.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358763.7/ ENSP00000351614.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..580
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..580
                     /product="synapsin-3 isoform IIIa"
                     /note="synapsin-3; cN28H9.2 (synapsin III)"
                     /calculated_mol_wt=63172
     Region          1..29
                     /region_name="Synapsin_N"
                     /note="Synapsin N-terminal; pfam10581"
                     /db_xref="CDD:463155"
     Region          1..28
                     /region_name="A"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and CaMK1.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          19..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          28..90
                     /region_name="B, linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          91..399
                     /region_name="C, actin-binding and synaptic-vesicle
                     binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          92..191
                     /region_name="Synapsin"
                     /note="N-terminal domain; pfam02078"
                     /db_xref="CDD:460438"
     Region          193..395
                     /region_name="CPSase_L_D2"
                     /note="Carbamoyl-phosphate synthase L chain, ATP binding
                     domain; cl17255"
                     /db_xref="CDD:473076"
     Region          <394..536
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Region          395..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Region          400..531
                     /region_name="J, Pro-rich linker"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            455
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            462
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            470
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1 and MAPK.
                     /evidence=ECO:0000269|PubMed:14732590; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O70441; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     Region          532..580
                     /region_name="E"
                     /note="propagated from UniProtKB/Swiss-Prot (O14994.2)"
     Site            541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8JZP2; propagated from
                     UniProtKB/Swiss-Prot (O14994.2)"
     CDS             1..580
                     /gene="SYN3"
                     /coded_by="NM_003490.4:253..1995"
                     /note="isoform IIIa is encoded by transcript variant IIIa"
                     /db_xref="CCDS:CCDS13908.1"
                     /db_xref="GeneID:8224"
                     /db_xref="HGNC:HGNC:11496"
                     /db_xref="MIM:602705"
ORIGIN      
        1 mnflrrrlsd ssfmanlpng ymtdlqrpds stsspaspam errhpqplaa sfsspgsslf
       61 sslssamkqa pqatsglmep pgpstpivqr prillvidda htdwskyfhg kkvngeieir
      121 veqaefseln laayvtggcm vdmqvvrngt kvvsrsfkpd filvrqhays malgedyrsl
      181 viglqygglp avnslysvyn fcskpwvfsq likifhslgp ekfplveqtf fpnhkpmvta
      241 phfpvvvklg hahagmgkik venqldfqdi tsvvamakty atteafidsk ydiriqkigs
      301 nykaymrtsi sgnwkantgs amleqvamte ryrlwvdscs emfggldica vkavhskdgr
      361 dyiievmdss mpligehvee drqlmadlvv skmsqlpmpg gtapsplrpw apqiksaksp
      421 gqaqlgpqlg qpqprpppqg gprqaqspqp qrsgspsqqr lspqgqqpls pqsgspqqqr
      481 spgspqlsra ssgsspnqas kpgatlasqp rppvqgrsts qqgeeskkpa pphphlnksq
      541 sltnslstsd tsqrgtpsed eakaetirnl rksfaslfsd
//
LOCUS       NP_060504                654 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 70 isoform 1 [Homo sapiens].
ACCESSION   NP_060504
VERSION     NP_060504.1
DBSOURCE    REFSEQ: accession NM_018034.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 654)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 654)
  AUTHORS   Mao,X., Wu,J., Zhang,Q., Zhang,S., Chen,X., Liu,X., Wei,M., Wan,X.,
            Qiu,L., Zeng,M., Lei,X., Liu,C. and Han,J.
  TITLE     Requirement of WDR70 for POLE3-mediated DNA double-strand breaks
            repair
  JOURNAL   Sci Adv 9 (36), eadh2358 (2023)
   PUBMED   37682991
  REMARK    GeneRIF: Requirement of WDR70 for POLE3-mediated DNA double-strand
            breaks repair.
REFERENCE   3  (residues 1 to 654)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   4  (residues 1 to 654)
  AUTHORS   Tang,Z.Z., Wang,H.B., Zeng,M., Liu,C. and Li,D.H.
  TITLE     [DNA Repair Function and Mutation of an H2B Monoubiquitination
            Factor WDR70 in Ovarian Cancer]
  JOURNAL   Sichuan Da Xue Xue Bao Yi Xue Ban 48 (5), 693-698 (2017)
   PUBMED   29130659
  REMARK    GeneRIF: Ovarian cancer had different expression of WDR70 and H2B
            monoubiquitination compared with normal tissue
REFERENCE   5  (residues 1 to 654)
  AUTHORS   Guo,L.D., Wang,D., Yang,F., Liang,Y.J., Yang,X.Q., Qin,Y.Y.,
            Ren,L.F., Zeng,M., Tang,Z.Z., Wang,X.J., Wang,S., Liu,C., Lou,J.Y.
            and Chen,J.
  TITLE     [Functional Analysis of DNA Damage Repair Factor WDR70 and Its
            Mutation in Ovarian Cancer]
  JOURNAL   Sichuan Da Xue Xue Bao Yi Xue Ban 47 (4), 501-506 (2016)
   PUBMED   28591950
REFERENCE   6  (residues 1 to 654)
  AUTHORS   Zeng,M., Ren,L., Mizuno,K., Nestoras,K., Wang,H., Tang,Z., Guo,L.,
            Kong,D., Hu,Q., He,Q., Du,L., Carr,A.M. and Liu,C.
  TITLE     CRL4(Wdr70) regulates H2B monoubiquitination and facilitates
            Exo1-dependent resection
  JOURNAL   Nat Commun 7, 11364 (2016)
   PUBMED   27098497
  REMARK    GeneRIF: CRL4(Wdr70) regulates H2B monoubiquitination and
            facilitates Exo1-dependent DNA repair resection.
            Publication Status: Online-Only
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC009648.1 and AC093269.3.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.247246.1,
                                           SRR1803613.219462.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265107.9/ ENSP00000265107.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..654
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..654
                     /product="WD repeat-containing protein 70 isoform 1"
                     /note="WD repeat-containing protein 70"
                     /calculated_mol_wt=73070
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          43..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          177..498
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          180..219
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            order(181,199,203,209..210,226,230,246,250,256..257,269,
                     282,305,311..312,331,348,353,359..360,374..375,395,399,
                     405..406,416..417,439,450,456..457,469..470,488,492,498)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          185..227
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          227..268
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          233..281
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          281..321
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          286..324
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          330..369
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          336..376
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          376..415
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          382..418
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          421..466
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          426..470
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            452
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          469..508
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          474..498
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          540..579
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NW82.1)"
     Region          630..654
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9NW82.1)"
     CDS             1..654
                     /gene="WDR70"
                     /coded_by="NM_018034.4:51..2015"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34147.1"
                     /db_xref="GeneID:55100"
                     /db_xref="HGNC:HGNC:25495"
                     /db_xref="MIM:617233"
ORIGIN      
        1 mersgpsevt gsdasgpdpq lavtmgftgf gkkartfdle amfeqtrrta versrktlea
       61 rekeeemnre kelrrqnedi eptssrsnvv rdcsksssrd tssseseqss dssddeligp
      121 plppkmvgkp vnfmeedilg plppplneee eeaeeeeeee eeeenpvhki pdsheitlkh
      181 gtktvsalgl dpsgarlvtg gydydvkfwd fagmdasfka frslqpcech qikslqysnt
      241 gdmilvvsgs sqakvidrdg fevmecikgd qyivdmantk ghtamlhtgs whpkikgefm
      301 tcsndatvrt wevenpkkqk svfkprtmqg kkvipttcty srdgnliaaa cqngsiqiwd
      361 rnltvhpkfh ykqahdsgtd tscvtfsydg nvlasrggdd slklwdirqf nkplfsasgl
      421 ptmfpmtdcc fspddklivt gtsiqrgcgs gklvfferrt fqrvyeidit dasvvrclwh
      481 pklnqimvgt gnglakvyyd pnksqrgakl cvvktqrkak qaetltqdyi itphalpmfr
      541 eprqrstrkq lekdrldplk shkpeppvag pgrggrvgth ggtlssyivk nialdktdds
      601 npreailrha kaaedspywv spaysktqpk tmfaqvesdd eeaknepewk krki
//
LOCUS       NP_001350587             307 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerases I and III subunit RPAC1 isoform 3
            [Homo sapiens].
ACCESSION   NP_001350587 XP_011513302
VERSION     NP_001350587.1
DBSOURCE    REFSEQ: accession NM_001363658.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 307)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 307)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 307)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 307)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   5  (residues 1 to 307)
  AUTHORS   Jansa,P., Mason,S.W., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Cloning and functional characterization of PTRF, a novel protein
            which induces dissociation of paused ternary transcription
            complexes
  JOURNAL   EMBO J 17 (10), 2855-2864 (1998)
   PUBMED   9582279
REFERENCE   6  (residues 1 to 307)
  AUTHORS   Dammann,R. and Pfeifer,G.P.
  TITLE     Cloning and characterization of the human RNA polymerase I subunit
            hRPA40
  JOURNAL   Biochim Biophys Acta 1396 (2), 153-157 (1998)
   PUBMED   9540830
REFERENCE   7  (residues 1 to 307)
  AUTHORS   Seither,P., Zatsepina,O., Hoffmann,M. and Grummt,I.
  TITLE     Constitutive and strong association of PAF53 with RNA polymerase I
  JOURNAL   Chromosoma 106 (4), 216-225 (1997)
   PUBMED   9254723
REFERENCE   8  (residues 1 to 307)
  AUTHORS   Yao,Y., Yamamoto,K., Nishi,Y., Nogi,Y. and Muramatsu,M.
  TITLE     Mouse RNA polymerase I 16-kDa subunit able to associate with 40-kDa
            subunit is a homolog of yeast AC19 subunit of RNA polymerases I and
            III
  JOURNAL   J Biol Chem 271 (51), 32881-32885 (1996)
   PUBMED   8955128
REFERENCE   9  (residues 1 to 307)
  AUTHORS   Bernard,G. and Vanderver,A.
  TITLE     POLR3-Related Leukodystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22855961
REFERENCE   10 (residues 1 to 307)
  AUTHORS   Barbosa,M., Jabs,E.W. and Huston,S.
  TITLE     Treacher Collins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301704
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355802.13.
            
            On May 24, 2018 this sequence version replaced XP_011513302.1.
            
            Summary: The protein encoded by this gene is a subunit of both RNA
            polymerase I and RNA polymerase III complexes. The encoded protein
            is part of the Pol core element. Mutations in this gene have been
            associated with Treacher Collins syndrome (TCS) and hypomyelinating
            leukodystrophy 11. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) differs in the 3' UTR and
            coding sequence compared to variant 1. The resulting isoform (3)
            has a shorter and distinct C-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.226239.1,
                                           SRR5189655.110295.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145245, SAMEA2147596
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..307
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..307
                     /product="DNA-directed RNA polymerases I and III subunit
                     RPAC1 isoform 3"
                     /note="DNA-directed RNA polymerases I and III subunit
                     RPAC1; RNA polymerase I subunit C; RNA polymerases I and
                     III subunit AC1; DNA-directed RNA polymerase I subunit C;
                     DNA-directed RNA polymerases I and III 40 kDa polypeptide;
                     polymerase (RNA) I polypeptide C, 30kDa; polymerase (RNA)
                     I subunit C"
                     /calculated_mol_wt=34828
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O15160.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15160.1)"
     Region          49..307
                     /region_name="RNAP_I_II_AC40"
                     /note="AC40 subunit of Eukaryotic RNA polymerase (RNAP) I
                     and RNAP III; cd07032"
                     /db_xref="CDD:132910"
     Site            order(74,77..78,82,102,104..105,108..109,222..223,
                     228..230,232..233,235..236)
                     /site_type="other"
                     /note="AC40 - A135(C128) interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:132910"
     Site            order(89..95,103,108,221..222,224)
                     /site_type="other"
                     /note="AC40 - RPB12 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:132910"
     Site            order(100,109,112,167,169,196..198,201,203,224,229..230)
                     /site_type="other"
                     /note="AC40 - RPB10 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:132910"
     CDS             1..307
                     /gene="POLR1C"
                     /gene_synonym="AC40; HLD11; RPA39; RPA40; RPA5; RPAC1;
                     RPC40; TCS3"
                     /coded_by="NM_001363658.2:22..945"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS87408.1"
                     /db_xref="GeneID:9533"
                     /db_xref="HGNC:HGNC:20194"
                     /db_xref="MIM:610060"
ORIGIN      
        1 maasqaveem rsrvvlgefg vrnvhttdfp gnysgyddaw dqdrfeknfr vdvvhmdens
       61 lefdmvgida aianafrril laevptmave kvlvynntsi vqdeilahrl glipihadpr
      121 lfeyrnqgde egteidtlqf rlqvrctrnp haakdssdpn elyvnhkvyt rhmtwiplgn
      181 qadlfpegti rpvhddilia qlrpgqeidl lmhcvkgigk dhakfspvat asyrllpdit
      241 llepvegeaa eelsrcfspg vievqevqgk kvarvanprl dtfsreifrn eklkkvvrla
      301 rvrdhyi
//
LOCUS       NP_001354605             846 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform mm [Homo sapiens].
ACCESSION   NP_001354605
VERSION     NP_001354605.1
DBSOURCE    REFSEQ: accession NM_001367676.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 846)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 846)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 846)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 846)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 846)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 846)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 846)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 846)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 846)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 846)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.118508.1,
                                           SRR1803612.232897.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..846
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..846
                     /product="SUN domain-containing protein 1 isoform mm"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=94315
     Region          62..352
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          478..531
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(478,481..482,485,488..489,492..493,495..496,
                     499..500,502..503,506..507,509..510,513,516..517,520,
                     523..524,527..528,530..531)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          490..>623
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          608..666
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          709..844
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..846
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367676.1:52..2592"
                     /note="isoform mm is encoded by transcript variant 39"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc gasfyvnril wlarytassf
      241 ssflvqlfqv vlmklsyese nyklkthesk dcesesyksk sheskahasy ygrmnvrevl
      301 redghlsvng ealwkaasgv fwwlgigwyq fvtliswlnv flltrclrni ckflvllipl
      361 flllaglslr gqgnffsflp vlnwasmhrt qrvddpqdvf kpttsrlkqp lqgdseafpw
      421 hwmsgveqqv aslsgqchhh genlrelttl lqklqarvdq meggaagpsa svrdavgqpp
      481 retdfmafhq ehevrmshle dilgklreks eaiqkeleqt kqktisavge qllptvehlq
      541 leldqlksel sswrhvktgc etvdavqerv dvqvremvkl lfsedqqggs leqllqrfss
      601 qfvskgdlqt mlrdlqlqil rnvthhvsvt kqlptseavv savseagasg iteaqaraiv
      661 nsalklysqd ktgmvdfale sgggsilstr csetyetkta lmslfgiplw yfsqsprvvi
      721 qpdiypgncw afkgsqgylv vrlsmmihpa aftlehipkt lsptgnissa pkdfavygle
      781 neyqeegqll gqftydqdge slqmfqalkr pddtafqive lrifsnwghp eytclyrfrv
      841 hgepvk
//
LOCUS       NP_001287998             428 aa            linear   PRI 20-NOV-2025
DEFINITION  U1 small nuclear ribonucleoprotein 70 kDa isoform 2 [Homo sapiens].
ACCESSION   NP_001287998 XP_005259234
VERSION     NP_001287998.1
DBSOURCE    REFSEQ: accession NM_001301069.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 428)
  AUTHORS   Kumari,S., Adhikary,A. and Singh,K.K.
  TITLE     BioID proximity mapping reveals novel SAP18 interactions in the
            prespliceosomal complex
  JOURNAL   Biochem Biophys Res Commun 738, 150944 (2024)
   PUBMED   39522233
REFERENCE   3  (residues 1 to 428)
  AUTHORS   Paul,T., Zhang,P., Zhang,Z., Fargason,T., De Silva,N.I.U.,
            Powell,E., Ekpenyong,E., Jamal,S., Yu,Y., Prevelige,P., Lu,R. and
            Zhang,J.
  TITLE     The U1-70K and SRSF1 interaction is modulated by phosphorylation
            during the early stages of spliceosome assembly
  JOURNAL   Protein Sci 33 (8), e5117 (2024)
   PUBMED   39023093
  REMARK    GeneRIF: The U1-70K and SRSF1 interaction is modulated by
            phosphorylation during the early stages of spliceosome assembly.
REFERENCE   4  (residues 1 to 428)
  AUTHORS   Jiang,D., Zhu,X.L., An,Y. and Li,Y.R.
  TITLE     Clinical significance of small nuclear ribonucleoprotein U1 subunit
            70 in patients with hepatocellular carcinoma
  JOURNAL   PeerJ 12, e16876 (2024)
   PUBMED   38500533
  REMARK    GeneRIF: Clinical significance of small nuclear ribonucleoprotein
            U1 subunit 70 in patients with hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 428)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   6  (residues 1 to 428)
  AUTHORS   Wilk,H.E., Schaefer,K.P., Agris,P.F., Boak,A.M. and Kovacs,S.A.
  TITLE     U1 SnRNP association with HnRNP involves an initial non-specific
            splice-site independent interaction of U1 SnRNP protein with HnRNA
  JOURNAL   Mol Cell Biochem 106 (1), 55-66 (1991)
   PUBMED   1833625
REFERENCE   7  (residues 1 to 428)
  AUTHORS   Spritz,R.A., Strunk,K., Surowy,C.S. and Mohrenweiser,H.W.
  TITLE     Human U1-70K ribonucleoprotein antigen gene: organization,
            nucleotide sequence, and mapping to locus 19q13.3
  JOURNAL   Genomics 8 (2), 371-379 (1990)
   PUBMED   2147422
REFERENCE   8  (residues 1 to 428)
  AUTHORS   Du Clos,T.W.
  TITLE     C-reactive protein reacts with the U1 small nuclear
            ribonucleoprotein
  JOURNAL   J Immunol 143 (8), 2553-2559 (1989)
   PUBMED   2477447
REFERENCE   9  (residues 1 to 428)
  AUTHORS   Query,C.C., Bentley,R.C. and Keene,J.D.
  TITLE     A common RNA recognition motif identified within a defined U1 RNA
            binding domain of the 70K U1 snRNP protein
  JOURNAL   Cell 57 (1), 89-101 (1989)
   PUBMED   2467746
REFERENCE   10 (residues 1 to 428)
  AUTHORS   Spritz,R.A., Strunk,K., Surowy,C.S., Hoch,S.O., Barton,D.E. and
            Francke,U.
  TITLE     The human U1-70K snRNP protein: cDNA cloning, chromosomal
            localization, expression, alternative splicing and RNA-binding
  JOURNAL   Nucleic Acids Res 15 (24), 10373-10391 (1987)
   PUBMED   2447561
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB189176.1, AL560281.3, BC001315.1 and X06815.1.
            
            On Jul 19, 2014 this sequence version replaced XP_005259234.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. It
            encodes isoform 2, which lacks an internal segment and is shorter,
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410571.176042.1,
                                           SRR3476690.992195.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..428
                     /product="U1 small nuclear ribonucleoprotein 70 kDa
                     isoform 2"
                     /note="U1 small nuclear ribonucleoprotein 70 kDa; U1 snRNP
                     70 kDa; small nuclear ribonucleoprotein 70kDa (U1); small
                     nuclear ribonucleoprotein, U1 70kDa subunit"
                     /calculated_mol_wt=50487
     Region          3..94
                     /region_name="U1snRNP70_N"
                     /note="U1 small nuclear ribonucleoprotein of 70kDa MW N
                     terminal; pfam12220"
                     /db_xref="CDD:432406"
     Region          102..187
                     /region_name="RRM_snRNP70"
                     /note="RNA recognition motif (RRM) found in U1 small
                     nuclear ribonucleoprotein 70 kDa (U1-70K) and similar
                     proteins; cd12236"
                     /db_xref="CDD:409682"
     CDS             1..428
                     /gene="SNRNP70"
                     /gene_synonym="RNPU1Z; RPU1; Snp1; SNRP70; U1-70K; U170K;
                     U1AP; U1RNP"
                     /coded_by="NM_001301069.2:197..1483"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS74417.1"
                     /db_xref="GeneID:6625"
                     /db_xref="HGNC:HGNC:11150"
                     /db_xref="MIM:180740"
ORIGIN      
        1 mtqflppnll alfaprdpip ylppleklph ekhhnqpycg iapyirefed prdappptra
       61 etreermerk rrekierrqq evetelkmwd phndpnaqgd afktlfvarv nydttesklr
      121 refevygpik rihmvyskrs gkprgyafie yeherdmhsa ykhadgkkid grrvlvdver
      181 grtvkgwrpr rlggglggtr rggadvnirh sgrddtsryd erdrdrdrer errersrerd
      241 kererrrsrs rdrrrrsrsr dkeerrrsre rskdkdrdrk rrssrsrera rrererkeel
      301 rggggdmaep seagdappdd gppgelgpdg pdgpeekgrd rdrerrrshr sererrrdrd
      361 rdrdrdrehk rgergsergr deargggggq dngleglgnd srdmymeseg gdgylapeng
      421 ylmeaape
//
LOCUS       NP_001308444             422 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-10 isoform 21 [Homo sapiens].
ACCESSION   NP_001308444
VERSION     NP_001308444.1
DBSOURCE    REFSEQ: accession NM_001321515.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Weiler,S.M.E., Bissinger,M., Rose,F., von Bubnoff,F., Lutz,T.,
            Ori,A., Schirmacher,P. and Breuhahn,K.
  TITLE     SEPTIN10-mediated crosstalk between cytoskeletal networks controls
            mechanotransduction and oncogenic YAP/TAZ signaling
  JOURNAL   Cancer Lett 584, 216637 (2024)
   PUBMED   38242197
  REMARK    GeneRIF: SEPTIN10-mediated crosstalk between cytoskeletal networks
            controls mechanotransduction and oncogenic YAP/TAZ signaling.
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Shen,B., Gao,H., Zhang,D., Yu,H., Chen,J., Huang,S., Gu,P. and
            Zhong,Y.
  TITLE     miR-124-3p regulates the proliferation and differentiation of
            retinal progenitor cells through SEPT10
  JOURNAL   Cell Tissue Res 392 (3), 689-704 (2023)
   PUBMED   36802303
  REMARK    GeneRIF: miR-124-3p regulates the proliferation and differentiation
            of retinal progenitor cells through SEPT10.
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Zhu,H., Tang,X., Zhang,H., Zhou,M., Liu,H., Chu,H. and Zhang,Z.
  TITLE     Exosomal circCLIP1 regulates PM2.5-induced airway obstruction via
            targeting SEPT10 in vitro
  JOURNAL   Ecotoxicol Environ Saf 254, 114750 (2023)
   PUBMED   36950992
  REMARK    GeneRIF: Exosomal circCLIP1 regulates PM2.5-induced airway
            obstruction via targeting SEPT10 in vitro.
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Xu,M., Takanashi,M., Oikawa,K., Nishi,H., Isaka,K., Yoshimoto,T.,
            Ohyashiki,J. and Kuroda,M.
  TITLE     Identification of a novel role of Septin 10 in
            paclitaxel-resistance in cancers through a functional genomics
            screen
  JOURNAL   Cancer Sci 103 (4), 821-827 (2012)
   PUBMED   22320903
  REMARK    GeneRIF: we found that paclitaxel-resistant tumors had decreased
            expression of SEPT10.
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Liu,M., Shen,S., Chen,F., Yu,W. and Yu,L.
  TITLE     Linking the septin expression with carcinogenesis
  JOURNAL   Mol Biol Rep 37 (7), 3601-3608 (2010)
   PUBMED   20195767
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Benedetti,D., Bomben,R., Dal-Bo,M., Marconi,D., Zucchetto,A.,
            Degan,M., Forconi,F., Del-Poeta,G., Gaidano,G. and Gattei,V.
  TITLE     Are surrogates of IGHV gene mutational status useful in B-cell
            chronic lymphocytic leukemia? The example of Septin-10
  JOURNAL   Leukemia 22 (1), 224-226 (2008)
   PUBMED   17657217
  REMARK    GeneRIF: Lack of SEPT10 transcript is associated with B-cell
            chronic lymphocytic leukemia
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Sui,L., Zhang,W., Liu,Q., Chen,T., Li,N., Wan,T., Yu,M. and Cao,X.
  TITLE     Cloning and functional characterization of human septin 10, a novel
            member of septin family cloned from dendritic cells
  JOURNAL   Biochem Biophys Res Commun 304 (2), 393-398 (2003)
   PUBMED   12711328
  REMARK    GeneRIF: Cloning and functional characterization of septin 10.
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Macara,I.G., Baldarelli,R., Field,C.M., Glotzer,M., Hayashi,Y.,
            Hsu,S.C., Kennedy,M.B., Kinoshita,M., Longtine,M., Low,C.,
            Maltais,L.J., McKenzie,L., Mitchison,T.J., Nishikawa,T., Noda,M.,
            Petty,E.M., Peifer,M., Pringle,J.R., Robinson,P.J., Roth,D.,
            Russell,S.E., Stuhlmann,H., Tanaka,M., Tanaka,T., Trimble,W.S.,
            Ware,J., Zeleznik-Le,N.J. and Zieger,B.
  TITLE     Mammalian septins nomenclature
  JOURNAL   Mol Biol Cell 13 (12), 4111-4113 (2002)
   PUBMED   12475938
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011753.6 and AC140485.3.
            
            Summary: This gene encodes a member of the septin family of
            cytoskeletal proteins with GTPase activity. This protein localizes
            to the cytoplasm and nucleus and displays GTP-binding and GTPase
            activity. A pseudogene for this gene is located on chromosome 8.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Apr 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.189551.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..422
                     /product="septin-10 isoform 21"
                     /calculated_mol_wt=48983
     Region          31..299
                     /region_name="CDC_Septin"
                     /note="CDC/Septin GTPase family; cd01850"
                     /db_xref="CDD:206649"
     Site            41..48
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(43..49,93,96,176..177,179,231..232)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            93..96
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(95..133,135..142)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            176..179
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            231..233
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..422
                     /gene="SEPTIN10"
                     /gene_synonym="SEPT10; Septin-10"
                     /coded_by="NM_001321515.2:554..1822"
                     /note="isoform 21 is encoded by transcript variant 21"
                     /db_xref="GeneID:151011"
                     /db_xref="HGNC:HGNC:14349"
                     /db_xref="MIM:611737"
ORIGIN      
        1 mkrenirslt msghvgfesl pdqlvnrsiq qgfcfnilcv getgigkstl idtlfntnfe
       61 dyesshfcpn vklkaqtyel qesnvqlklt ivntvgfgdq inkeesyqpi vdyidaqfea
      121 ylqeelkikr slftyhdsri hvclyfispt ghslktldll tmknldskvn iipviakadt
      181 vsktelqkfk iklmselvsn gvqiyqfptd ddtiakvnaa mngqlpfavv gsmdevkvgn
      241 kmvkarqypw gvvqvenenh cdfvklreml ictnmedlre qthtrhyely rrckleemgf
      301 tdvgpenkpv svqetyeakr hefhgerqrk eeemkqmfvq rvkekeailk eaerelqakf
      361 ehlkrlhqee rmkleekrrl leeeiiafsk kkatseifhs qsflatgsnl rkdkdrknsn
      421 fl
//
LOCUS       NP_001003675             251 aa            linear   PRI 20-NOV-2025
DEFINITION  low-density lipoprotein receptor class A domain-containing protein
            4 isoform gamma 2 [Homo sapiens].
ACCESSION   NP_001003675
VERSION     NP_001003675.1
DBSOURCE    REFSEQ: accession NM_001003675.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Xie,W., Xiao,H., Luo,J., Zhao,L., Jin,F., Ma,J., Li,J., Xiong,K.,
            Chen,C. and Wang,G.
  TITLE     Identification of low-density lipoprotein receptor class A domain
            containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors
  JOURNAL   Curr Probl Cancer 44 (6), 100593 (2020)
   PUBMED   32507364
  REMARK    GeneRIF: Identification of low-density lipoprotein receptor class A
            domain containing 4 (LDLRAD4) as a prognostic indicator in primary
            gastrointestinal stromal tumors.
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Meerabux,J.M., Ohba,H., Iwayama,Y., Maekawa,M.,
            Detera-Wadleigh,S.D., DeLisi,L.E. and Yoshikawa,T.
  TITLE     Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
            schizophrenia
  JOURNAL   J Hum Genet 54 (7), 386-391 (2009)
   PUBMED   19461657
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Kikuchi,M., Yamada,K., Toyota,T. and Yoshikawa,T.
  TITLE     C18orf1 located on chromosome 18p11.2 may confer susceptibility to
            schizophrenia
  JOURNAL   J Med Dent Sci 50 (3), 225-229 (2003)
   PUBMED   15074360
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E. and Detera-Wadleigh,S.D.
  TITLE     Multiple transcriptional variants and RNA editing in C18orf1, a
            novel gene with LDLRA and transmembrane domains on 18p11.2
  JOURNAL   Genomics 47 (2), 246-257 (1998)
   PUBMED   9479497
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Esterling,L.E., Cox Matise,T., Sanders,A.R., Yoshikawa,T.,
            Overhauser,J., Gershon,E.S., Moskowitz,M.T. and
            Detera-Wadleigh,S.D.
  TITLE     An integrated physical map of 18p11.2: a susceptibility region for
            bipolar disorder
  JOURNAL   Mol Psychiatry 2 (6), 501-504 (1997)
   PUBMED   9399696
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Yoshikawa,T., Sanders,A.R., Esterling,L.E., Overhauser,J.,
            Garnes,J.A., Lennon,G., Grewal,R. and Detera-Wadleigh,S.D.
  TITLE     Isolation of chromosome 18-specific brain transcripts as positional
            candidates for bipolar disorder
  JOURNAL   Am J Med Genet 74 (2), 140-149 (1997)
   PUBMED   9129712
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA246476.1, DA126127.1, BC047093.1, DA276009.1, HY115972.1,
            BX114947.1, BM991627.1, AI878844.1, BC066971.1, AF009424.1 and
            AP001010.4.
            
            Transcript Variant: This variant (4) contains an alternate 5'
            terminal exon, differs in its 5' UTR, lacks a portion of the 5'
            coding region, initiates translation at an alternate start codon,
            and lacks an alternate in-frame exon in the central coding region,
            compared to variant a1. The encoded isoform (gamma 2) is shorter
            and has a distinct N-terminus, compared to isoform alpha 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.209584.1,
                                           SRR1803617.136812.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.21"
     Protein         1..251
                     /product="low-density lipoprotein receptor class A
                     domain-containing protein 4 isoform gamma 2"
                     /note="clone 22; low-density lipoprotein receptor class A
                     domain-containing protein 4"
                     /calculated_mol_wt=28116
     CDS             1..251
                     /gene="LDLRAD4"
                     /gene_synonym="C18orf1"
                     /coded_by="NM_001003675.3:1242..1997"
                     /note="isoform gamma 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS42415.1"
                     /db_xref="GeneID:753"
                     /db_xref="HGNC:HGNC:1224"
                     /db_xref="MIM:606571"
ORIGIN      
        1 mssdhlnnst lkeaqfkdlf lkkaelefaq iiiivvvvtv mvvvivclln hykvstrsfi
       61 nrpnqsrrre dglpqimhap rsrdrftaps fiqrdrfsrf qptypyvqhe idlpptisls
      121 dgeepppyqg pctlqlrdpe qqmelnresv rappnrtifd sdlidiamys ggpcppssns
      181 gisastcssn grmegpppty sevmghhpga sflhhqrsna hrgsrlqfqq nnaestivpi
      241 kgkdrkpgnl v
//
LOCUS       NP_071426                653 aa            linear   PRI 20-NOV-2025
DEFINITION  leucine-rich repeat-containing protein 4 precursor [Homo sapiens].
ACCESSION   NP_071426
VERSION     NP_071426.1
DBSOURCE    REFSEQ: accession NM_022143.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Deng,K. and Wu,M.
  TITLE     Leucine-rich repeats containing 4 protein (LRRC4) in memory,
            psychoneurosis, and glioblastoma
  JOURNAL   Chin Med J (Engl) 136 (1), 4-12 (2023)
   PUBMED   36780420
  REMARK    GeneRIF: Leucine-rich repeats containing 4 protein (LRRC4) in
            memory, psychoneurosis, and glioblastoma.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Feng,J., Zhang,Y., Ren,X., Li,D., Fu,H., Liu,C., Zhou,W., Liu,Q.,
            Liu,Q. and Wu,M.
  TITLE     Leucine-rich repeat containing 4 act as an autophagy inhibitor that
            restores sensitivity of glioblastoma to temozolomide
  JOURNAL   Oncogene 39 (23), 4551-4566 (2020)
   PUBMED   32372061
  REMARK    GeneRIF: Leucine-rich repeat containing 4 act as an autophagy
            inhibitor that restores sensitivity of glioblastoma to
            temozolomide.
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Aoyama,T., Takasawa,A., Takasawa,K., Ono,Y., Emori,M., Murata,M.,
            Hayasaka,T., Fujitani,N., Osanai,M., Yamashita,T., Hasegawa,T. and
            Sawada,N.
  TITLE     Identification of Coiled-Coil Domain-Containing Protein 180 and
            Leucine-Rich Repeat-Containing Protein 4 as Potential
            Immunohistochemical Markers for Liposarcoma Based on Proteomic
            Analysis Using Formalin-Fixed, Paraffin-Embedded Tissue
  JOURNAL   Am J Pathol 189 (5), 1015-1028 (2019)
   PUBMED   30790560
  REMARK    GeneRIF: High LRRC4 expression is associated with Liposarcoma .
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Wang,Z., Guo,Q., Wang,R., Xu,G., Li,P., Sun,Y., She,X., Liu,Q.,
            Chen,Q., Yu,Z., Liu,C., Xiong,J., Li,G. and Wu,M.
  TITLE     The D Domain of LRRC4 anchors ERK1/2 in the cytoplasm and
            competitively inhibits MEK/ERK activation in glioma cells
  JOURNAL   J Hematol Oncol 9 (1), 130 (2016)
   PUBMED   27884160
  REMARK    GeneRIF: Following EGF stimuli, the D domain of LRRC4 anchors
            ERK1/2 in the cytoplasm and abrogates ERK1/2 activation and nuclear
            translocation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Zhang,Q.H., Wang,L.L., Cao,L., Peng,C., Li,X.L., Tang,K., Li,W.F.,
            Liao,P., Wang,J.R. and Li,G.Y.
  TITLE     Study of a novel brain relatively specific gene LRRC4 involved in
            glioma tumorigenesis suppression using the Tet-on system
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 37 (8), 532-540 (2005)
   PUBMED   16077900
REFERENCE   7  (residues 1 to 653)
  AUTHORS   Zhang,Q., Wang,J., Fan,S., Wang,L., Cao,L., Tang,K., Peng,C.,
            Li,Z., Li,W., Gan,K., Liu,Z., Li,X., Shen,S. and Li,G.
  TITLE     Expression and functional characterization of LRRC4, a novel
            brain-specific member of the LRR superfamily
  JOURNAL   FEBS Lett 579 (17), 3674-3682 (2005)
   PUBMED   15967442
  REMARK    GeneRIF: LRRC4 may play an important role in maintaining normal
            function and suppressing tumorigenesis in the central nervous
            system.
REFERENCE   8  (residues 1 to 653)
  AUTHORS   Lin,J.C., Ho,W.H., Gurney,A. and Rosenthal,A.
  TITLE     The netrin-G1 ligand NGL-1 promotes the outgrowth of
            thalamocortical axons
  JOURNAL   Nat Neurosci 6 (12), 1270-1276 (2003)
   PUBMED   14595443
REFERENCE   9  (residues 1 to 653)
  AUTHORS   Wang,J.R., Li,X.L., Fan,S.Q., Tan,C., Xiang,J.J., Tang,K., Wang,R.
            and Li,G.Y.
  TITLE     Expression of LRRC4 has the potential to decrease the growth rate
            and tumorigenesis of glioblastoma cell line U251
  JOURNAL   Ai Zheng 22 (9), 897-902 (2003)
   PUBMED   12969517
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Nakashiba,T., Ikeda,T., Nishimura,S., Tashiro,K., Honjo,T.,
            Culotti,J.G. and Itohara,S.
  TITLE     Netrin-G1: a novel glycosyl phosphatidylinositol-linked mammalian
            netrin that is functionally divergent from classical netrins
  JOURNAL   J Neurosci 20 (17), 6540-6550 (2000)
   PUBMED   10964959
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008039.1, AF196976.4, BC111745.1 and BU682120.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF196976.4, BC111561.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000249363.4/ ENSP00000249363.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32.1"
     Protein         1..653
                     /product="leucine-rich repeat-containing protein 4
                     precursor"
                     /note="brain tumor associated protein LRRC4; leucine-rich
                     repeat-containing protein 4; netrin-G2 ligand; brain
                     tumor-associated protein BAG; nasopharyngeal
                     carcinoma-associated gene 14 protein; netrin-G ligand-2"
                     /calculated_mol_wt=68391
     sig_peptide     1..38
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
                     /calculated_mol_wt=4344
     mat_peptide     39..653
                     /product="Leucine-rich repeat-containing protein 4.
                     /id=PRO_0000014833"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
                     /calculated_mol_wt=68391
     Region          46..79
                     /region_name="LRRNT"
                     /note="Leucine rich repeat N-terminal domain; smart00013"
                     /db_xref="CDD:214470"
     Region          <75..323
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          76..97
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          77..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          100..121
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          124..145
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          125..148
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          148..169
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          149..172
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          172..194
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          173..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          197..218
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          198..219
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          219..240
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          220..243
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          243..264
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          244..267
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          267..288
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          268..289
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            277
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          300..351
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            322
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          359..441
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Site            363
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          370..374
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409367"
     Region          381..385
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409367"
     Site            388
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          407..411
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409367"
     Site            410
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Region          421..426
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409367"
     Region          434..437
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409367"
     Site            434
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Site            440
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Site            447
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Site            450
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9HBW1.2)"
     Site            528..548
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9HBW1.2)"
     CDS             1..653
                     /gene="LRRC4"
                     /gene_synonym="NAG14; NGL-2"
                     /coded_by="NM_022143.5:626..2587"
                     /db_xref="CCDS:CCDS5799.1"
                     /db_xref="GeneID:64101"
                     /db_xref="HGNC:HGNC:15586"
                     /db_xref="MIM:610486"
ORIGIN      
        1 mkllwqvtvh hhtwnaillp fvyltaqvwi lcaaiaaaas agpqncpsvc scsnqfskvv
       61 ctrrglsevp qgipsntryl nlmenniqmi qadtfrhlhh levlqlgrns irqievgafn
      121 glaslntlel fdnwltvips gafeylsklr elwlrnnpie sipsyafnrv pslmrldlge
      181 lkkleyiseg afeglfnlky lnlgmcnikd mpnltplvgl eelemsgnhf peirpgsfhg
      241 lsslkklwvm nsqvsliern afdglaslve lnlahnnlss lphdlftplr ylvelhlhhn
      301 pwncdcdilw lawwlreyip tnstccgrch apmhmrgryl vevdqasfqc sapfimdapr
      361 dlnisegrma elkcrtppms svkwllpngt vlshasrhpr isvlndgtln fshvllsdtg
      421 vytcmvtnva gnsnasayln vstaelntsn ysffttvtve tteispedtt rkykpvptts
      481 tgyqpaytts ttvliqttrv pkqvavpatd ttdkmqtsld evmkttkiii gcfvavtlla
      541 aamlivfykl rkrhqqrstv taartveiiq vdedipaats aaataapsgv sgegavvlpt
      601 ihdhinynty kpahgahwte nslgnslhpt vttisepyii qthtkdkvqe tqi
//
LOCUS       NP_001028                218 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel regulatory subunit beta-1 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001028 XP_945148
VERSION     NP_001028.1
DBSOURCE    REFSEQ: accession NM_001037.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Popa-Fotea,N.M., Oprescu,N., Scafa-Udriste,A. and Micheu,M.M.
  TITLE     Impact of rs1805127 and rs55742440 Variants on Atrial Remodeling in
            Hypertrophic Cardiomyopathy Patients with Atrial Fibrillation: A
            Romanian Cohort Study
  JOURNAL   Int J Mol Sci 24 (24), 17244 (2023)
   PUBMED   38139087
  REMARK    GeneRIF: Impact of rs1805127 and rs55742440 Variants on Atrial
            Remodeling in Hypertrophic Cardiomyopathy Patients with Atrial
            Fibrillation: A Romanian Cohort Study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Li,Y., Yuan,T., Huang,B., Zhou,F., Peng,C., Li,X., Qiu,Y., Yang,B.,
            Zhao,Y., Huang,Z. and Jiang,D.
  TITLE     Structure of human NaV1.6 channel reveals Na+ selectivity and pore
            blockade by 4,9-anhydro-tetrodotoxin
  JOURNAL   Nat Commun 14 (1), 1030 (2023)
   PUBMED   36823201
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Fan,X., Huang,J., Jin,X. and Yan,N.
  TITLE     Cryo-EM structure of human voltage-gated sodium channel Nav1.6
  JOURNAL   Proc Natl Acad Sci U S A 120 (5), e2220578120 (2023)
   PUBMED   36696443
REFERENCE   4  (residues 1 to 218)
  AUTHORS   Alghamdi,M.A., Al-Eitan,L.N., Asiri,A., Rababa'h,D.M.,
            Alqahtani,S.A., Aldarami,M.S., Alsaeedi,M.A., Almuidh,R.S.,
            Alzahrani,A.A., Sakah,A.H., El Nashar,E.M., Otaif,M.Y. and Abdel
            Ghaffar,N.F.
  TITLE     Association of sodium voltage-gated channel genes polymorphisms
            with epilepsy risk and prognosis in the Saudi population
  JOURNAL   Ann Med 54 (1), 1938-1951 (2022)
   PUBMED   35801810
  REMARK    GeneRIF: Association of sodium voltage-gated channel genes
            polymorphisms with epilepsy risk and prognosis in the Saudi
            population.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Qin,N., D'Andrea,M.R., Lubin,M.L., Shafaee,N., Codd,E.E. and
            Correa,A.M.
  TITLE     Molecular cloning and functional expression of the human sodium
            channel beta1B subunit, a novel splicing variant of the beta1
            subunit
  JOURNAL   Eur J Biochem 270 (23), 4762-4770 (2003)
   PUBMED   14622265
  REMARK    GeneRIF: identification and characterization of a novel splicing
            variant; functional studies in oocytes demonstrate that the beta1B
            subunit increases the ionic current when coexpressed with the
            tetrodotoxin sensitive channel, NaV1.2
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Makita,N., Sloan-Brown,K., Weghuis,D.O., Ropers,H.H. and
            George,A.L. Jr.
  TITLE     Genomic organization and chromosomal assignment of the human
            voltage-gated Na+ channel beta 1 subunit gene (SCN1B)
  JOURNAL   Genomics 23 (3), 628-634 (1994)
   PUBMED   7851891
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Makita,N., Bennett,P.B. Jr. and George,A.L. Jr.
  TITLE     Voltage-gated Na+ channel beta 1 subunit mRNA expressed in adult
            human skeletal muscle, heart, and brain is encoded by a single gene
  JOURNAL   J Biol Chem 269 (10), 7571-7578 (1994)
   PUBMED   8125980
REFERENCE   8  (residues 1 to 218)
  AUTHORS   McClatchey,A.I., Cannon,S.C., Slaugenhaupt,S.A. and Gusella,J.F.
  TITLE     The cloning and expression of a sodium channel beta 1-subunit cDNA
            from human brain
  JOURNAL   Hum Mol Genet 2 (6), 745-749 (1993)
   PUBMED   8394762
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 218)
  AUTHORS   Hartshorne,R.P. and Catterall,W.A.
  TITLE     The sodium channel from rat brain. Purification and subunit
            composition
  JOURNAL   J Biol Chem 259 (3), 1667-1675 (1984)
   PUBMED   6319405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020907.6 and BC067122.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_945148.1.
            
            Summary: Voltage-gated sodium channels are heteromeric proteins
            that function in the generation and propagation of action
            potentials in muscle and neuronal cells. They are composed of one
            alpha and two beta subunits, where the alpha subunit provides
            channel activity and the beta-1 subunit modulates the kinetics of
            channel inactivation. This gene encodes a sodium channel beta-1
            subunit. Mutations in this gene result in generalized epilepsy with
            febrile seizures plus, Brugada syndrome 5, and defects in cardiac
            conduction. Multiple transcript variants encoding different
            isoforms have been found for this gene.[provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (a) represents the longer
            transcript but encodes the shorter isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.62069.1,
                                           SRR3476690.943038.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262631.11/ ENSP00000262631.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..218
                     /product="sodium channel regulatory subunit beta-1 isoform
                     a precursor"
                     /note="sodium channel subunit beta-1; sodium channel,
                     voltage-gated, type I, beta; sodium channel, voltage
                     gated, type I beta subunit; sodium channel regulatory
                     subunit beta-1"
                     /calculated_mol_wt=22994
     sig_peptide     1..18
                     /note="/evidence=ECO:0000250|UniProtKB:Q00954; propagated
                     from UniProtKB/Swiss-Prot (Q07699.1)"
                     /calculated_mol_wt=1731
     mat_peptide     19..218
                     /product="Sodium channel regulatory subunit beta-1.
                     /id=PRO_0000014926"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07699.1)"
                     /calculated_mol_wt=22994
     Region          23..147
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30765606,
                     ECO:0000269|PubMed:36696443, ECO:0007744|PDB:6J8G,
                     ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I,
                     ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD; propagated
                     from UniProtKB/Swiss-Prot (Q07699.1)"
     Site            110
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30190309,
                     ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:36696443,
                     ECO:0007744|PDB:6AGF, ECO:0007744|PDB:6J8G,
                     ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I,
                     ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD; propagated
                     from UniProtKB/Swiss-Prot (Q07699.1)"
     Site            114
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30190309,
                     ECO:0000269|PubMed:30765606, ECO:0000269|PubMed:36696443,
                     ECO:0007744|PDB:6AGF, ECO:0007744|PDB:6J8G,
                     ECO:0007744|PDB:6J8H, ECO:0007744|PDB:6J8I,
                     ECO:0007744|PDB:6J8J, ECO:0007744|PDB:8FHD; propagated
                     from UniProtKB/Swiss-Prot (Q07699.1)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:30765606,
                     ECO:0000269|PubMed:36696443, ECO:0000269|PubMed:36823201,
                     ECO:0007744|PDB:6J8G, ECO:0007744|PDB:6J8H,
                     ECO:0007744|PDB:6J8I, ECO:0007744|PDB:6J8J,
                     ECO:0007744|PDB:8FHD, ECO:0007744|PDB:8GZ1,
                     ECO:0007744|PDB:8GZ2; propagated from UniProtKB/Swiss-Prot
                     (Q07699.1)"
     Site            158..179
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q07699.1)"
     CDS             1..218
                     /gene="SCN1B"
                     /gene_synonym="ATFB13; BRGDA5; DEE52; EIEE52; GEFSP1"
                     /coded_by="NM_001037.5:352..1008"
                     /note="isoform a precursor is encoded by transcript
                     variant a"
                     /db_xref="CCDS:CCDS12441.1"
                     /db_xref="GeneID:6324"
                     /db_xref="HGNC:HGNC:10586"
                     /db_xref="MIM:600235"
ORIGIN      
        1 mgrllalvvg aalvssacgg cvevdsetea vygmtfkilc isckrrsetn aetftewtfr
       61 qkgteefvki lryenevlql eederfegrv vwngsrgtkd lqdlsifitn vtynhsgdye
      121 chvyrllffe nyehntsvvk kihievvdka nrdmasivse immyvlivvl tiwlvaemiy
      181 cykkiaaate taaqenasey laitsesken ctgvqvae
//
LOCUS       NP_003600                556 aa            linear   PRI 20-NOV-2025
DEFINITION  HIRA-interacting protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_003600
VERSION     NP_003600.2
DBSOURCE    REFSEQ: accession NM_003609.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 556)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 556)
  AUTHORS   Ignatyeva,M., Patel,A.K.M., Ibrahim,A., Albiheyri,R.S., Zari,A.T.,
            Bahieldin,A., Bronner,C., Sabir,J.S.M. and Hamiche,A.
  TITLE     Identification and Characterization of HIRIP3 as a Histone H2A
            Chaperone
  JOURNAL   Cells 13 (3), 273 (2024)
   PUBMED   38334665
  REMARK    GeneRIF: Identification and Characterization of HIRIP3 as a Histone
            H2A Chaperone.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 556)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 556)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 556)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 556)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 556)
  AUTHORS   Kim,J.E., Tannenbaum,S.R. and White,F.M.
  TITLE     Global phosphoproteome of HT-29 human colon adenocarcinoma cells
  JOURNAL   J Proteome Res 4 (4), 1339-1346 (2005)
   PUBMED   16083285
REFERENCE   8  (residues 1 to 556)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   9  (residues 1 to 556)
  AUTHORS   Lorain,S., Quivy,J.P., Monier-Gavelle,F., Scamps,C., Lecluse,Y.,
            Almouzni,G. and Lipinski,M.
  TITLE     Core histones and HIRIP3, a novel histone-binding protein, directly
            interact with WD repeat protein HIRA
  JOURNAL   Mol Cell Biol 18 (9), 5546-5556 (1998)
   PUBMED   9710638
REFERENCE   10 (residues 1 to 556)
  AUTHORS   Auffray,C., Behar,G., Bois,F., Bouchier,C., Da Silva,C.,
            Devignes,M.D., Duprat,S., Houlgatte,R., Jumeau,M.N., Lamy,B. et al.
  TITLE     [IMAGE: molecular integration of the analysis of the human genome
            and its expression]
  JOURNAL   C R Acad Sci III 318 (2), 263-272 (1995)
   PUBMED   7757816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000588.2, Z25386.1,
            BU629222.1 and BX101682.1.
            
            On Jun 12, 2002 this sequence version replaced NP_003600.1.
            
            Summary: The HIRA protein shares sequence similarity with Hir1p and
            Hir2p, the two corepressors of histone gene transcription
            characterized in the yeast, Saccharomyces cerevisiae. The
            structural features of the HIRA protein suggest that it may
            function as part of a multiprotein complex. Several cDNAs encoding
            HIRA-interacting proteins, or HIRIPs, have been identified. In
            vitro, the protein encoded by this gene binds HIRA, as well as H2B
            and H3 core histones, indicating that a complex containing
            HIRA-HIRIP3 could function in some aspects of chromatin and histone
            metabolism. Alternatively spliced transcript variants encoding
            distinct isoforms have been found for this gene.[provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.104665.1,
                                           SRR3476690.866475.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2145245
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279392.8/ ENSP00000279392.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..556
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..556
                     /product="HIRA-interacting protein 3 isoform 1"
                     /calculated_mol_wt=61826
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Region          64..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            87
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            359
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            370
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Region          403..527
                     /region_name="Interaction with the histone H2A-H2B
                     complex. /evidence=ECO:0000269|PubMed:38334665"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Region          484..520
                     /region_name="CHZ"
                     /note="Histone chaperone domain CHZ; smart01082"
                     /db_xref="CDD:198150"
     Region          502..556
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            551
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     Site            555
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9BW71.3)"
     CDS             1..556
                     /gene="HIRIP3"
                     /coded_by="NM_003609.5:13..1683"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10664.1"
                     /db_xref="GeneID:8479"
                     /db_xref="HGNC:HGNC:4917"
                     /db_xref="MIM:603365"
ORIGIN      
        1 marekemqef trsffrgrpd lstlthsivr rrylahsgrs hlepeekqal krlveeellk
       61 mqvdeaasre dkldltkkgk rpptpcsdpe rkrfrfnses esgseasspd yfgppakngv
      121 aaevspakee nprraskave essdeerqrd lpaqrgeess eeeekgykgk trkkpvvkkq
      181 apgkasvsrk qareeseese aepvqrtakk vegnkgtksl keseqeseee ilaqkkeqre
      241 eeveeeekee deekgdwkpr trsngrrksa reersckqks qakrllgdsd seeeqkeaas
      301 sgddsgrdre ppvqrksedr tqlkggkrls gssedeedsg kgeptakgsr kmarlgstsg
      361 eesdlerevs dseagggpqg erknrsskks srkgrtrsss sssdgspeak ggkagsgrrg
      421 edhpavmrlk ryiracgahr nykkllgscc shkerlsilr aelealgmkg tpslgkcral
      481 keqreeaaev asldvaniis gsgrprrrta wnplgeaapp gelyrrtlds deerprpapp
      541 dwshmrgiis sdgesn
//
LOCUS       NP_001180381             192 aa            linear   PRI 20-NOV-2025
DEFINITION  tudor-interacting repair regulator protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001180381
VERSION     NP_001180381.1
DBSOURCE    REFSEQ: accession NM_001193452.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Parnandi,N., Rendo,V., Cui,G., Botuyan,M.V., Remisova,M.,
            Nguyen,H., Drane,P., Beroukhim,R., Altmeyer,M., Mer,G. and
            Chowdhury,D.
  TITLE     TIRR inhibits the 53BP1-p53 complex to alter cell-fate programs
  JOURNAL   Mol Cell 81 (12), 2583-2595 (2021)
   PUBMED   33961797
  REMARK    GeneRIF: TIRR inhibits the 53BP1-p53 complex to alter cell-fate
            programs.
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Zhang,A., Peng,B., Huang,P., Chen,J. and Gong,Z.
  TITLE     The p53-binding protein 1-Tudor-interacting repair regulator
            complex participates in the DNA damage response
  JOURNAL   J Biol Chem 292 (16), 6461-6467 (2017)
   PUBMED   28213517
  REMARK    GeneRIF: TIRR is a novel 53BP1-interacting protein that
            participates in the DNA damage response
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Song,M.G., Li,Y. and Kiledjian,M.
  TITLE     Multiple mRNA decapping enzymes in mammalian cells
  JOURNAL   Mol Cell 40 (3), 423-432 (2010)
   PUBMED   21070968
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Taylor,M.J. and Peculis,B.A.
  TITLE     Evolutionary conservation supports ancient origin for Nudt16, a
            nuclear-localized, RNA-binding, RNA-decapping enzyme
  JOURNAL   Nucleic Acids Res 36 (18), 6021-6034 (2008)
   PUBMED   18820299
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA607298.1, BQ923183.1, AC023830.9 and BU739233.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 2, which has a shorter and distinct
            C-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.422753.1,
                                           SRR1163658.227366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..192
                     /product="tudor-interacting repair regulator protein
                     isoform 2"
                     /note="protein syndesmos; NUDT16-like protein 1; nudix
                     (nucleoside diphosphate linked moiety X)-type motif
                     16-like 1; tudor-interacting repair regulator protein"
                     /calculated_mol_wt=20896
     Site            10
                     /site_type="other"
                     /note="Required for interaction with TP53BP1.
                     /evidence=ECO:0000269|PubMed:28241136; propagated from
                     UniProtKB/Swiss-Prot (Q9BRJ7.1)"
     Region          23..>139
                     /region_name="NUDIX_Hydrolase"
                     /note="NUDIX hydrolase superfamily; cl00447"
                     /db_xref="CDD:469772"
     CDS             1..192
                     /gene="NUDT16L1"
                     /gene_synonym="SDOS; TIRR"
                     /coded_by="NM_001193452.1:35..613"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS59257.1"
                     /db_xref="GeneID:84309"
                     /db_xref="HGNC:HGNC:28154"
                     /db_xref="MIM:617338"
ORIGIN      
        1 mstaavpelk qisrveamrl gpgwshscha mlyaanpgql fgripmrfsv lmqmrfdgll
       61 gfpggfvdrr fwsledglnr vlglglgclr lteadylssh ltegphrvva hlyarqltle
      121 qlhaveisav hsrdhglevg pppgprpppr glalapwkap mgagpragpa vhpegpsrrl
      181 pqlpeqrlre hg
//
LOCUS       NP_060941                426 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger CCCH domain-containing protein 15 [Homo sapiens].
ACCESSION   NP_060941
VERSION     NP_060941.2
DBSOURCE    REFSEQ: accession NM_018471.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 426)
  AUTHORS   Hou,J., Xu,M., Gu,H., Pei,D., Liu,Y., Huang,P., Chang,H. and Cui,H.
  TITLE     ZC3H15 promotes glioblastoma progression through regulating EGFR
            stability
  JOURNAL   Cell Death Dis 13 (1), 55 (2022)
   PUBMED   35027542
  REMARK    GeneRIF: ZC3H15 promotes glioblastoma progression through
            regulating EGFR stability.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 426)
  AUTHORS   Li,Q., Hou,J., Guo,C., Zhang,Y., Liu,L., Hu,H., Shi,S., Ji,Y.,
            Guo,L., Shi,Y., Liu,Y. and Cui,H.
  TITLE     ZC3H15 Correlates with a Poor Prognosis and Tumor Progression in
            Melanoma
  JOURNAL   Biomed Res Int 2021, 8305299 (2021)
   PUBMED   34988227
  REMARK    GeneRIF: ZC3H15 Correlates with a Poor Prognosis and Tumor
            Progression in Melanoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 426)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 426)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   7  (residues 1 to 426)
  AUTHORS   Capalbo,G., Muller-Kuller,T., Dietrich,U., Hoelzer,D., Ottmann,O.G.
            and Scheuring,U.J.
  TITLE     Inhibition of X4-tropic HIV type 1 replication by knockdown of the
            cellular protein LEREPO4
  JOURNAL   AIDS Res Hum Retroviruses 26 (10), 1155-1161 (2010)
   PUBMED   20925576
  REMARK    GeneRIF: down-regulation of LEREPO4 expression caused a significant
            inhibition of HIV replication
REFERENCE   8  (residues 1 to 426)
  AUTHORS   Ishikawa,K., Akiyama,T., Ito,K., Semba,K. and Inoue,J.
  TITLE     Independent stabilizations of polysomal Drg1/Dfrp1 complex and
            non-polysomal Drg2/Dfrp2 complex in mammalian cells
  JOURNAL   Biochem Biophys Res Commun 390 (3), 552-556 (2009)
   PUBMED   19819225
REFERENCE   9  (residues 1 to 426)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
REFERENCE   10 (residues 1 to 426)
  AUTHORS   Gregory,R.C., Lord,K.A., Panek,L.B., Gaines,P., Dillon,S.B. and
            Wojchowski,D.M.
  TITLE     Subtraction cloning and initial characterization of novel
            epo-immediate response genes
  JOURNAL   Cytokine 12 (7), 845-857 (2000)
   PUBMED   10880228
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL040058.1 and BC021102.1.
            
            On Nov 19, 2006 this sequence version replaced NP_060941.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.288403.1, AF289586.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000337859.11/ ENSP00000338788.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q32.1"
     Protein         1..426
                     /product="zinc finger CCCH domain-containing protein 15"
                     /note="DRG family-regulatory protein 1; likely ortholog of
                     mouse immediate early response erythropoietin 4"
                     /calculated_mol_wt=48472
     Region          1..325
                     /region_name="COG5252"
                     /note="Uncharacterized conserved protein, contains
                     CCCH-type Zn-finger protein [General function prediction
                     only]"
                     /db_xref="CDD:227577"
     Region          1..30
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          53..74
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            231
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          236..260
                     /region_name="Required for interaction with DRG1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          299..326
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Region          358..411
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8WU90.1)"
     Site            381
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8WU90.1)"
     CDS             1..426
                     /gene="ZC3H15"
                     /gene_synonym="DFRP1; HT010; LEREPO4; MSTP012"
                     /coded_by="NM_018471.3:124..1404"
                     /db_xref="CCDS:CCDS42791.1"
                     /db_xref="GeneID:55854"
                     /db_xref="HGNC:HGNC:29528"
                     /db_xref="MIM:619704"
ORIGIN      
        1 mppkkqaqag gskkaeqkkk ekiiedktfg lknkkgakqq kfikavthqv kfgqqnprqv
       61 aqseaekklk kddkkkelqe lnelfkpvva aqkiskgadp ksvvcaffkq gqctkgdkck
      121 fshdltlerk cekrsvyida rdeelekdtm dnwdekklee vvnkkhgeae kkkpktqivc
      181 khfleaienn kygwfwvcpg ggdicmyrha lppgfvlkkd kkkeekedei sledlierer
      241 salgpnvtki tlesflawkk rkrqekidkl eqdmerrkad fkagkalvis grevfefrpe
      301 lvndddeead dtrytqgtgg devddsvsvn didlslyipr dvdetgitva slerfstyts
      361 dkdenklsea sggraenger sdleednere gtengaidav pvdenlftge dldeleeeln
      421 tldlee
//
LOCUS       NP_877419                499 aa            linear   PRI 20-NOV-2025
DEFINITION  thioredoxin reductase 1, cytoplasmic isoform 1 [Homo sapiens].
ACCESSION   NP_877419
VERSION     NP_877419.1
DBSOURCE    REFSEQ: accession NM_182742.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Hsieh,M.S., Ling,H.H., Setiawan,S.A., Hardianti,M.S., Fong,I.H.,
            Yeh,C.T. and Chen,J.H.
  TITLE     Therapeutic targeting of thioredoxin reductase 1 causes ferroptosis
            while potentiating anti-PD-1 efficacy in head and neck cancer
  JOURNAL   Chem Biol Interact 395, 111004 (2024)
   PUBMED   38636790
  REMARK    GeneRIF: Therapeutic targeting of thioredoxin reductase 1 causes
            ferroptosis while potentiating anti-PD-1 efficacy in head and neck
            cancer.
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Shen,X., Xia,Y., Lu,H., Zheng,P., Wang,J., Chen,Y., Xu,C., Qiu,C.,
            Zhang,Y., Xiao,Z., Zou,P., Cui,R. and Ni,D.
  TITLE     Synergistic targeting of TrxR1 and ATM/AKT pathway in human colon
            cancer cells
  JOURNAL   Biomed Pharmacother 174, 116507 (2024)
   PUBMED   38565059
  REMARK    GeneRIF: Synergistic targeting of TrxR1 and ATM/AKT pathway in
            human colon cancer cells.
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Nalvarte,I., Damdimopoulos,A.E., Ruegg,J. and Spyrou,G.
  TITLE     The expression and activity of thioredoxin reductase 1 splice
            variants v1 and v2 regulate the expression of genes associated with
            differentiation and adhesion
  JOURNAL   Biosci Rep 35 (6), e00269 (2015)
   PUBMED   26464515
  REMARK    GeneRIF: TXNRD1_v1 and TXNRD1_v2 have distinct roles in
            differentiation, possibly by altering the expression of the genes
            associated with differentiation, and further emphasize the
            importance in distinguishing each unique action of different TrxR1
            splice forms
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Dammeyer,P., Damdimopoulos,A.E., Nordman,T., Jimenez,A.,
            Miranda-Vizuete,A. and Arner,E.S.
  TITLE     Induction of cell membrane protrusions by the N-terminal
            glutaredoxin domain of a rare splice variant of human thioredoxin
            reductase 1
  JOURNAL   J Biol Chem 283 (5), 2814-2821 (2008)
   PUBMED   18042542
  REMARK    GeneRIF: the Grx domain of TXNRD1_v3 localizes first in the
            emerging cell membrane protrusion and is then followed into the
            protrusions by actin and subsequently by tubulin
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Gladyshev,V.N., Jeang,K.T. and Stadtman,T.C.
  TITLE     Selenocysteine, identified as the penultimate C-terminal residue in
            human T-cell thioredoxin reductase, corresponds to TGA in the human
            placental gene
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 6146-6151 (1996)
   PUBMED   8650234
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Tamura,T. and Stadtman,T.C.
  TITLE     A new selenoprotein from human lung adenocarcinoma cells:
            purification, properties, and thioredoxin reductase activity
  JOURNAL   Proc Natl Acad Sci U S A 93 (3), 1006-1011 (1996)
   PUBMED   8577704
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Cha,M.K. and Kim,I.H.
  TITLE     Thioredoxin-linked peroxidase from human red blood cell: evidence
            for the existence of thioredoxin and thioredoxin reductase in human
            red blood cell
  JOURNAL   Biochem Biophys Res Commun 217 (3), 900-907 (1995)
   PUBMED   8554614
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Gasdaska,P.Y., Gasdaska,J.R., Cochran,S. and Powis,G.
  TITLE     Cloning and sequencing of a human thioredoxin reductase
  JOURNAL   FEBS Lett 373 (1), 5-9 (1995)
   PUBMED   7589432
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Schallreuter,K.U., Grebe,T., Pittelkow,M.R. and Wood,J.M.
  TITLE     [3H]-13-cis-retinoic acid covalently binds to thioredoxin reductase
            in human keratinocytes
  JOURNAL   Skin Pharmacol 4 (1), 14-20 (1991)
   PUBMED   2064786
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA238692.1, AK226071.1,
            BC018122.1 and AI097548.1.
            
            Summary: The protein encoded by this gene belongs to the pyridine
            nucleotide-disulfide oxidoreductase family, and is a member of the
            thioredoxin (Trx) system. Three thioredoxin reductase (TrxR)
            isozymes are found in mammals. TrxRs are selenocysteine-containing
            flavoenzymes, which reduce thioredoxins, as well as other
            substrates, and play a key role in redox homoeostasis. This gene
            encodes an ubiquitously expressed, cytosolic form of TrxR, which
            functions as a homodimer containing FAD, and selenocysteine (Sec)
            at the active site. Sec is encoded by UGA codon that normally
            signals translation termination. The 3' UTRs of selenoprotein mRNAs
            contain a conserved stem-loop structure, the Sec insertion sequence
            (SECIS) element, which is necessary for the recognition of UGA as a
            Sec codon rather than as a stop signal. Alternative splicing,
            primarily at the 5' end, results in transcript variants encoding
            same or different isoforms, including a glutaredoxin-containing
            isoform that is predominantly expressed in testis. [provided by
            RefSeq, May 2017].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1-3 encode the same isoform (1, also known
            as TXNRD1_v1), which is thought to regulate expression of genes
            associated with differentiation and adhesion (PMID:26464515).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.240223.1,
                                           SRR1660805.6794.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            protein contains selenocysteine :: PMID: 7589432, 8650234
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..499
                     /product="thioredoxin reductase 1, cytoplasmic isoform 1"
                     /EC_number="1.8.1.9"
                     /EC_number="1.11.1.2"
                     /note="KM-102-derived reductase-like factor; thioredoxin
                     reductase GRIM-12; thioredoxin reductase 1, cytoplasmic;
                     oxidoreductase; thioredoxin reductase TR1; gene associated
                     with retinoic and IFN-induced mortality 12 protein;
                     selenoprotein TXNRD1; gene associated with retinoic and
                     interferon-induced mortality 12 protein; testis tissue
                     sperm-binding protein Li 46a; peroxidase TXNRD1"
                     /calculated_mol_wt=54623
     Region          11..499
                     /region_name="TGR"
                     /note="thioredoxin and glutathione reductase
                     selenoprotein; TIGR01438"
                     /db_xref="CDD:273624"
     Site            498
                     /site_type="other"
                     /note="Selenocysteine"
     CDS             1..499
                     /gene="TXNRD1"
                     /gene_synonym="GRIM-12; TR; TR1; TRXR1; TXNR; TXNR1"
                     /coded_by="NM_182742.3:352..1851"
                     /note="UGA stop codon recoded as selenocysteine; isoform 1
                     is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53823.1"
                     /db_xref="GeneID:7296"
                     /db_xref="HGNC:HGNC:12437"
                     /db_xref="MIM:601112"
ORIGIN      
        1 mngpedlpks ydydliiigg gsgglaaake aaqygkkvmv ldfvtptplg trwglggtcv
       61 nvgcipkklm hqaallgqal qdsrnygwkv eetvkhdwdr mieavqnhig slnwgyrval
      121 rekkvvyena ygqfigphri katnnkgkek iysaerflia tgerprylgi pgdkeyciss
      181 ddlfslpycp gktlvvgasy valecagfla gigldvtvmv rsillrgfdq dmankigehm
      241 eehgikfirq fvpikveqie agtpgrlrvv aqstnseeii egeyntvmla igrdactrki
      301 gletvgvkin ektgkipvtd eeqtnvpyiy aigdiledkv eltpvaiqag rllaqrlyag
      361 stvkcdyenv pttvftpley gacglseeka vekfgeenie vyhsyfwple wtipsrdnnk
      421 cyakiicntk dnervvgfhv lgpnagevtq gfaaalkcgl tkkqldstig ihpvcaevft
      481 tlsvtkrsga silqagcug
//
LOCUS       NP_001352683             222 aa            linear   PRI 20-NOV-2025
DEFINITION  MIF4G domain-containing protein isoform 4 [Homo sapiens].
ACCESSION   NP_001352683 XP_016880382
VERSION     NP_001352683.1
DBSOURCE    REFSEQ: accession NM_001365754.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 222)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 222)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 222)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 222)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 222)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 222)
  AUTHORS   Cakmakci,N.G., Lerner,R.S., Wagner,E.J., Zheng,L. and Marzluff,W.F.
  TITLE     SLIP1, a factor required for activation of histone mRNA translation
            by the stem-loop binding protein
  JOURNAL   Mol Cell Biol 28 (3), 1182-1194 (2008)
   PUBMED   18025107
  REMARK    GeneRIF: downregulation of endogenous SLIP1 reduces the rate of
            translation of endogenous histone mRNA and also reduces cell
            viability.
REFERENCE   8  (residues 1 to 222)
  AUTHORS   Miele,A., Medina,R., van Wijnen,A.J., Stein,G.S. and Stein,J.L.
  TITLE     The interactome of the histone gene regulatory factor HiNF-P
            suggests novel cell cycle related roles in transcriptional control
            and RNA processing
  JOURNAL   J Cell Biochem 102 (1), 136-148 (2007)
   PUBMED   17577209
REFERENCE   9  (residues 1 to 222)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 222)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC022211.5.
            
            On Sep 12, 2018 this sequence version replaced XP_016880382.1.
            
            Summary: This gene encodes a protein which interacts with the
            N-terminus of the stem-loop binding protein (SLBP) and the 3' end
            of histone mRNA. This interaction facilitates the activation of
            histone mRNA translation. Alternative splicing results in multiple
            transcript variants encoding different isoforms. [provided by
            RefSeq, Jun 2011].
            
            Transcript Variant: This variant (9), as well as variants 4, 7, 8,
            and 10, encodes isoform (4).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: CX870572.1, BM560704.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..222
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.1"
     Protein         1..222
                     /product="MIF4G domain-containing protein isoform 4"
                     /note="SLBP (stem loop binding protein)-interacting
                     protein 1; MIF4G domain-containing protein;
                     SLBP-interacting protein 1"
                     /calculated_mol_wt=25292
     Region          8..179
                     /region_name="MIF4G"
                     /note="MIF4G domain; cl02652"
                     /db_xref="CDD:413423"
     CDS             1..222
                     /gene="MIF4GD"
                     /gene_synonym="AD023; MIFD; SLIP1"
                     /coded_by="NM_001365754.1:207..875"
                     /note="isoform 4 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS56044.1"
                     /db_xref="GeneID:57409"
                     /db_xref="HGNC:HGNC:24030"
                     /db_xref="MIM:612072"
ORIGIN      
        1 mgepsreeyk iqsfdaetqq llktalkdpg avdlekvanv ivdhslqdcv fskeagrmcy
       61 aiiqaeskqa gqsvfrrgll nrlqqeyqar eqlrarslqg wvcyvtficn ifdylrvnnm
      121 pmmalvnpvy dclfrlaqpd slskeeevdc lvlqlhrvge qlekmngqrm delfvlirdg
      181 fllptglssl aqlllleiie fraagwkttp aahkyyysev sd
//
LOCUS       NP_001950                225 aa            linear   PRI 20-NOV-2025
DEFINITION  elongation factor 1-beta [Homo sapiens].
ACCESSION   NP_001950
VERSION     NP_001950.1
DBSOURCE    REFSEQ: accession NM_001959.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 225)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 225)
  AUTHORS   Negrutskii,B.S., Shalak,V.F., Novosylna,O.V., Porubleva,L.V.,
            Lozhko,D.M. and El'skaya,A.V.
  TITLE     The eEF1 family of mammalian translation elongation factors
  JOURNAL   BBA Adv 3, 100067 (2022)
   PUBMED   37082266
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 225)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 225)
  AUTHORS   He,C., Guo,J., Tian,W. and Wong,C.C.L.
  TITLE     Proteogenomics Integrating Novel Junction Peptide Identification
            Strategy Discovers Three Novel Protein Isoforms of Human NHSL1 and
            EEF1B2
  JOURNAL   J Proteome Res 20 (12), 5294-5303 (2021)
   PUBMED   34420305
  REMARK    GeneRIF: Proteogenomics Integrating Novel Junction Peptide
            Identification Strategy Discovers Three Novel Protein Isoforms of
            Human NHSL1 and EEF1B2.
REFERENCE   5  (residues 1 to 225)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 225)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R. et
            al.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
   PUBMED   1286669
REFERENCE   7  (residues 1 to 225)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   8  (residues 1 to 225)
  AUTHORS   Sanders,J., Maassen,J.A., Amons,R. and Moller,W.
  TITLE     Nucleotide sequence of human elongation factor-1 beta cDNA
  JOURNAL   Nucleic Acids Res 19 (16), 4551 (1991)
   PUBMED   1886777
REFERENCE   9  (residues 1 to 225)
  AUTHORS   von der Kammer,H., Klaudiny,J., Zimmer,M. and Scheit,K.H.
  TITLE     Human elongation factor 1 beta: cDNA and derived amino acid
            sequence
  JOURNAL   Biochem Biophys Res Commun 177 (1), 312-317 (1991)
   PUBMED   1710449
REFERENCE   10 (residues 1 to 225)
  AUTHORS   Bec,G., Kerjan,P., Zha,X.D. and Waller,J.P.
  TITLE     Valyl-tRNA synthetase from rabbit liver. I. Purification as a
            heterotypic complex in association with elongation factor 1
  JOURNAL   J Biol Chem 264 (35), 21131-21137 (1989)
   PUBMED   2556394
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from X60489.1.
            
            Summary: This gene encodes a translation elongation factor. The
            protein is a guanine nucleotide exchange factor involved in the
            transfer of aminoacylated tRNAs to the ribosome. Alternative
            splicing results in three transcript variants which differ only in
            the 5' UTR. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This predominant variant (1) has a distinct 5'
            UTR. Variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X60489.1, SRR1163655.11650.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392222.7/ ENSP00000376056.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..225
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33.3"
     Protein         1..225
                     /product="elongation factor 1-beta"
                     /note="eukaryotic translation elongation factor 1 beta 1;
                     EF-1-beta; eEF-1B alpha"
                     /calculated_mol_wt=24633
     Region          <3..62
                     /region_name="GST_C_eEF1b_like"
                     /note="Glutathione S-transferase C-terminal-like, alpha
                     helical domain of eukaryotic translation Elongation Factor
                     1 beta; cd10308"
                     /db_xref="CDD:198341"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Site            order(19..23,50..51,53..54,58,61..62)
                     /site_type="other"
                     /note="putative protein interface 2 [polypeptide binding]"
                     /db_xref="CDD:198341"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Region          78..115
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P24534.3)"
     Site            88
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O70251; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P24534.3)"
     Region          103..130
                     /region_name="EF-1_beta_acid"
                     /note="Eukaryotic elongation factor 1 beta central acidic
                     region; pfam10587"
                     /db_xref="CDD:463158"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17693683,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     Region          142..225
                     /region_name="EF1_GNE"
                     /note="EF-1 guanine nucleotide exchange domain; pfam00736"
                     /db_xref="CDD:459919"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P24534.3)"
     CDS             1..225
                     /gene="EEF1B2"
                     /gene_synonym="EEF1B; EEF1B1; EF1B"
                     /coded_by="NM_001959.4:86..763"
                     /db_xref="CCDS:CCDS2367.1"
                     /db_xref="GeneID:1933"
                     /db_xref="HGNC:HGNC:3208"
                     /db_xref="MIM:600655"
ORIGIN      
        1 mgfgdlkspa glqvlndyla dksyiegyvp sqadvavfea vsspppadlc halrwynhik
       61 syekekaslp gvkkalgkyg padvedttgs gatdskdddd idlfgsddee eseeakrlre
      121 erlaqyeskk akkpalvaks silldvkpwd detdmaklee cvrsiqadgl vwgssklvpv
      181 gygikklqiq cvveddkvgt dmleeqitaf edyvqsmdva afnki
//
LOCUS       NP_055991                368 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 28 isoform a [Homo sapiens].
ACCESSION   NP_055991
VERSION     NP_055991.1
DBSOURCE    REFSEQ: accession NM_015176.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Song,G., Sun,Z., Chu,M., Zhang,Z., Chen,J., Wang,Z. and Zhu,X.
  TITLE     FBXO28 promotes cell proliferation, migration and invasion via
            upregulation of the TGF-beta1/SMAD2/3 signaling pathway in ovarian
            cancer
  JOURNAL   BMC Cancer 24 (1), 122 (2024)
   PUBMED   38267923
  REMARK    GeneRIF: FBXO28 promotes cell proliferation, migration and invasion
            via upregulation of the TGF-beta1/SMAD2/3 signaling pathway in
            ovarian cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Qiao,X., Lin,J., Shen,J., Chen,Y., Zheng,L., Ren,H., Zhao,X.,
            Yang,H., Li,P. and Wang,Z.
  TITLE     FBXO28 suppresses liver cancer invasion and metastasis by promoting
            PKA-dependent SNAI2 degradation
  JOURNAL   Oncogene 42 (39), 2878-2891 (2023)
   PUBMED   37596321
  REMARK    GeneRIF: FBXO28 suppresses liver cancer invasion and metastasis by
            promoting PKA-dependent SNAI2 degradation.
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Liu,S., Liu,P., Zhu,C., Yang,R., He,Z., Li,Y., Li,Y., Fei,X.,
            Hou,J., Wang,X. and Pan,Y.
  TITLE     FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination
  JOURNAL   Aging (Albany NY) 15 (12), 5381-5398 (2023)
   PUBMED   37348029
  REMARK    GeneRIF: FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination.
            Erratum:[Aging (Albany NY). 2023 Sep 14;15(17):9230-9232. doi:
            10.18632/aging.205071. PMID: 37708091]
REFERENCE   6  (residues 1 to 368)
  AUTHORS   D'Angiolella,V., Donato,V., Forrester,F.M., Jeong,Y.T.,
            Pellacani,C., Kudo,Y., Saraf,A., Florens,L., Washburn,M.P. and
            Pagano,M.
  TITLE     Cyclin F-mediated degradation of ribonucleotide reductase M2
            controls genome integrity and DNA repair
  JOURNAL   Cell 149 (5), 1023-1034 (2012)
   PUBMED   22632967
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Ohta,S., Bukowski-Wills,J.C., Sanchez-Pulido,L., Alves Fde,L.,
            Wood,L., Chen,Z.A., Platani,M., Fischer,L., Hudson,D.F.,
            Ponting,C.P., Fukagawa,T., Earnshaw,W.C. and Rappsilber,J.
  TITLE     The protein composition of mitotic chromosomes determined using
            multiclassifier combinatorial proteomics
  JOURNAL   Cell 142 (5), 810-821 (2010)
   PUBMED   20813266
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Prashar,Y. and Weissman,S.M.
  TITLE     Analysis of differential gene expression by display of 3' end
            restriction fragments of cDNAs
  JOURNAL   Proc Natl Acad Sci U S A 93 (2), 659-663 (1996)
   PUBMED   8570611
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL390122.16.
            
            Summary: Members of the F-box protein family, such as FBXO28, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001628.1, SRR1803615.245511.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000366862.10/ ENSP00000355827.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.11"
     Protein         1..368
                     /product="F-box only protein 28 isoform a"
                     /note="F-box only protein 28; centromere protein 30"
                     /calculated_mol_wt=41018
     Region          1..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVF7.1)"
     Region          64..108
                     /region_name="F-box_FBXO28"
                     /note="F-box domain found in F-box only protein 28
                     (FBXO28) and similar proteins; cd22100"
                     /db_xref="CDD:438872"
     Site            order(67,71,74..75,78..79,83,85..86,90..92,94)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438872"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NVF7.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NVF7.1)"
     Site            270
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q9NVF7.1)"
     Region          328..368
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVF7.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVF7.1)"
     CDS             1..368
                     /gene="FBXO28"
                     /gene_synonym="CENP-30; DEE100; Fbx28"
                     /coded_by="NM_015176.4:20..1126"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1539.1"
                     /db_xref="GeneID:23219"
                     /db_xref="HGNC:HGNC:29046"
                     /db_xref="MIM:609100"
ORIGIN      
        1 maaaaeerma eeggggqgdg gsslasgstq rqppppapqh pqpgsqalpa palapdqlpq
       61 nntlvalpiv aienilsfms ydeisqlrlv ckrmdlvcqr mlnqgflkve ryhnlcqkqv
      121 kaqlprrese rrnhslarha dilaavetrl sllnmtfmky vdsnlccfip gkvideiyrv
      181 lryvnstrap qrahevlqel rdissmamey fdekivpilk rklpgsdvsg rlmgsppvpg
      241 psaalttmql fskqnpsrqe vtklqqqvkt ngagvtvlrr eiselrtkvq eqqkqlqdqd
      301 qklleqtqii geqnarlael erklrevmes avgnssgsgq neesprkrkk ateaidslrk
      361 skrlrnrk
//
LOCUS       NP_001353517             902 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 21 [Homo
            sapiens].
ACCESSION   NP_001353517 XP_005245778
VERSION     NP_001353517.1
DBSOURCE    REFSEQ: accession NM_001366588.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 902)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 902)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 902)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 902)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 902)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 902)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 902)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 902)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 902)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 902)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_005245778.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.156801.1,
                                           SRR1803617.44368.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..902
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..902
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 21"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=102019
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            549
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            558
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            570
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            579
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            581
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            594
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            603
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <604..>738
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            605
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            624
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            692
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            694
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            703
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            705
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            711
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            713
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            716
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            736
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            746
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            754
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            771
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            773
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            775
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            776
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            779
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            800
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            870
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..902
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366588.1:26..2734"
                     /note="isoform 21 is encoded by transcript variant 26"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsvtkh kgtekresps papkprkvel seseedkggk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssss ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rgrrrrspsp pptrrrrsps pappprrrrt ptppprrrtp sppprrrsps prrysppiqr
      601 ryspspppkr rtaspppppk rraspspppk rrvshspppk qrsspvtkrr spslsskhrk
      661 gsspsrstre arspqpnkrh spsprprapq tssspppvrr gassspqrrq spspstrpir
      721 rvsrtpepkk ikkaaspspq svrrvsssrs vsgspepaak kppappspvq sqspstnwsp
      781 avpvkkaksp tpspspprns dqegggkkkk kkkdkkhkkd kkhkkhkkhk kekavaaaaa
      841 aavtpaaiaa atttlaqeep vaapepkket eseaednldd lekhlrekal rsmrkaqvsp
      901 qs
//
LOCUS       NP_006353                619 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear RNA export factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_006353
VERSION     NP_006353.2
DBSOURCE    REFSEQ: accession NM_006362.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 619)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 619)
  AUTHORS   Ebara,S., Yoshida,M., Yamakawa,H., Shimokawa,K., Inoue,Y.,
            Tauchi,H. and Morishita,D.
  TITLE     Interaction of CDK12 with NXF1 is a new node for the linking
            mechanism between transcription and transportation of mRNA
  JOURNAL   Biochem Biophys Res Commun 735, 150608 (2024)
   PUBMED   39270556
  REMARK    GeneRIF: Interaction of CDK12 with NXF1 is a new node for the
            linking mechanism between transcription and transportation of mRNA.
REFERENCE   3  (residues 1 to 619)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 619)
  AUTHORS   Jin,T., Yang,L., Chang,C., Luo,H., Wang,R., Gan,Y., Sun,Y., Guo,Y.,
            Tang,R., Chen,S., Meng,D., Dai,P. and Liu,M.
  TITLE     HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective Export via
            ALYREF/NXF1 Complex to Foster Breast Cancer Development
  JOURNAL   Adv Sci (Weinh) 11 (24), e2307639 (2024)
   PUBMED   38626369
  REMARK    GeneRIF: HnRNPA2B1 ISGylation Regulates m6A-Tagged mRNA Selective
            Export via ALYREF/NXF1 Complex to Foster Breast Cancer Development.
REFERENCE   5  (residues 1 to 619)
  AUTHORS   Luo,F., Zou,P., Liao,Y., Luo,J., Luo,D., Hu,K., Zhang,K. and
            Wang,B.
  TITLE     Association between TAP gene polymorphisms and tuberculosis
            susceptibility in a Han Chinese population in Guangdong
  JOURNAL   Mol Genet Genomics 297 (3), 779-790 (2022)
   PUBMED   35325275
  REMARK    GeneRIF: Association between TAP gene polymorphisms and
            tuberculosis susceptibility in a Han Chinese population in
            Guangdong.
REFERENCE   6  (residues 1 to 619)
  AUTHORS   Li,Y., Bor,Y.C., Misawa,Y., Xue,Y., Rekosh,D. and Hammarskjold,M.L.
  TITLE     An intron with a constitutive transport element is retained in a
            Tap messenger RNA
  JOURNAL   Nature 443 (7108), 234-237 (2006)
   PUBMED   16971948
  REMARK    GeneRIF: results indicate that Tap regulates expression of its own
            intron-containing RNA through a CTE (constitutive transport
            element)-mediated mechanism
REFERENCE   7  (residues 1 to 619)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   8  (residues 1 to 619)
  AUTHORS   Gruter,P., Tabernero,C., von Kobbe,C., Schmitt,C., Saavedra,C.,
            Bachi,A., Wilm,M., Felber,B.K. and Izaurralde,E.
  TITLE     TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export
            from the nucleus
  JOURNAL   Mol Cell 1 (5), 649-659 (1998)
   PUBMED   9660949
REFERENCE   9  (residues 1 to 619)
  AUTHORS   Arai,Y., Hosoda,F., Kobayashi,H., Arai,K., Hayashi,Y., Kamada,N.,
            Kaneko,Y. and Ohki,M.
  TITLE     The inv(11)(p15q22) chromosome translocation of de novo and
            therapy-related myeloid malignancies results in fusion of the
            nucleoporin gene, NUP98, with the putative RNA helicase gene, DDX10
  JOURNAL   Blood 89 (11), 3936-3944 (1997)
   PUBMED   9166830
REFERENCE   10 (residues 1 to 619)
  AUTHORS   Yoon,D.W., Lee,H., Seol,W., DeMaria,M., Rosenzweig,M. and Jung,J.U.
  TITLE     Tap: a novel cellular protein that interacts with tip of
            herpesvirus saimiri and induces lymphocyte aggregation
  JOURNAL   Immunity 6 (5), 571-582 (1997)
   PUBMED   9175835
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001160.4, BC004904.2 and
            BC028041.1.
            
            On Sep 7, 2001 this sequence version replaced NP_006353.1.
            
            Summary: This gene is one member of a family of nuclear RNA export
            factor genes. Common domain features of this family are a
            noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich
            repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain
            that allows heterodimerization with NTF2-related export protein-1
            (NXT1), and a ubiquitin-associated domain that mediates
            interactions with nucleoporins. The LRRs and NTF2-like domains are
            required for export activity. Alternative splicing seems to be a
            common mechanism in this gene family. The encoded protein of this
            gene shuttles between the nucleus and the cytoplasm and binds in
            vivo to poly(A)+ RNA. It is the vertebrate homologue of the yeast
            protein Mex67p. The encoded protein overcomes the mRNA export block
            caused by the presence of saturating amounts of CTE (constitutive
            transport element) RNA of type D retroviruses. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC028041.1, AF112880.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294172.7/ ENSP00000294172.2
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..619
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..619
                     /product="nuclear RNA export factor 1 isoform 1"
                     /note="tip associating protein; mRNA export factor TAP;
                     tip-associated protein"
                     /calculated_mol_wt=70052
     Region          1..85
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          2..118
                     /region_name="RNA-binding (RBD)"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          2..60
                     /region_name="Minor non-specific RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Site            42
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99JX7;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q99JX7; propagated from
                     UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          61..118
                     /region_name="Major non-specific RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          67..100
                     /region_name="Nuclear localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          83..110
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBU9.1)"
     Region          119..198
                     /region_name="Tap-RNA_bind"
                     /note="Tap, RNA-binding; pfam09162"
                     /db_xref="CDD:462696"
     Region          121..198
                     /region_name="noncanonical RNP-type RNA-binding (RBD)
                     domain"
     Region          199..371
                     /region_name="leucine-rich repeat (LRR) domains"
     Region          224..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          <263..>389
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          267..292
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          293..316
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          317..347
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275382"
     Region          382..538
                     /region_name="NTF2"
                     /note="Nuclear transport factor 2 (NTF2) domain plays an
                     important role in the trafficking of macromolecules, ions
                     and small molecules between the cytoplasm and nucleus.
                     This bi-directional transport of macromolecules across the
                     nuclear envelope requires many...; cd00780"
                     /db_xref="CDD:238403"
     Site            order(411,417,457,482,484..485,494,520,531..533,535,537)
                     /site_type="active"
                     /note="TAP/p15 interaction [active]"
                     /db_xref="CDD:238403"
     Site            order(415,417..418,477..478,482,484..485,492,496..498,502,
                     508..511,514,520,531..533,535..538)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238403"
     Site            order(418..419,469,472,497,499,501..502,508,511,534,536,
                     538)
                     /site_type="active"
                     /note="RanGDP-NTF2 interaction [active]"
                     /db_xref="CDD:238403"
     Region          556..618
                     /region_name="TAP_C"
                     /note="C-terminal domain of vertebrate Tap protein;
                     smart00804"
                     /db_xref="CDD:197882"
     Site            order(580,584,587..588,590..593,598,602,606,611,613)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270527"
     CDS             1..619
                     /gene="NXF1"
                     /gene_synonym="MEX67; TAP"
                     /coded_by="NM_006362.5:85..1944"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8037.1"
                     /db_xref="GeneID:10482"
                     /db_xref="HGNC:HGNC:8071"
                     /db_xref="MIM:602647"
ORIGIN      
        1 madegksyse hddervnfpq rkkkgrgpfr wkygegnrrs grggsgirss rleeddgdva
       61 msdaqdgprv rynpyttrpn rrgdtwhdrd rihvtvrrdr apperggagt sqdgtsknwf
      121 kitipygrky dkawllsmiq skcsvpftpi efhyentraq ffvedastas alkavnykil
      181 drenrrisii inssapphti lnelkpeqve qlklimskry dgsqqaldlk glrsdpdlva
      241 qnidvvlnrr scmaatlrii eenipellsl nlsnnrlyrl ddmssivqka pnlkilnlsg
      301 nelksereld kikglkleel wldgnslcdt frdqstyisa irerfpkllr ldghelpppi
      361 afdveapttl ppckgsyfgt enlkslvlhf lqqyyaiyds gdrqgllday hdgaccslsi
      421 pfipqnpars slaeyfkdsr nvkklkdptl rfrllkhtrl nvvaflnelp ktqhdvnsfv
      481 vdisaqtstl lcfsvngvfk evdgksrdsl raftrtfiav pasnsglciv ndelfvrnas
      541 seeiqrafam paptpssspv ptlspeqqem lqafstqsgm nlewsqkclq dnnwdytrsa
      601 qafthlkakg eipevafmk
//
LOCUS       NP_001340537             329 aa            linear   PRI 20-NOV-2025
DEFINITION  lysosomal cobalamin transporter ABCD4 isoform l [Homo sapiens].
ACCESSION   NP_001340537 XP_016877032
VERSION     NP_001340537.1
DBSOURCE    REFSEQ: accession NM_001353608.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Pillai,N.R., Miller,D., Pierpont,E.I., Berry,S.A. and Aggarwal,A.
  TITLE     Cobalamin J disease detected on newborn screening: Novel variant
            and normal neurodevelopmental course
  JOURNAL   Am J Med Genet A 185 (6), 1870-1874 (2021)
   PUBMED   33729671
  REMARK    GeneRIF: Cobalamin J disease detected on newborn screening: Novel
            variant and normal neurodevelopmental course.
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Kitai,K., Kawaguchi,K., Tomohiro,T., Morita,M., So,T. and
            Imanaka,T.
  TITLE     The lysosomal protein ABCD4 can transport vitamin B12 across
            liposomal membranes in vitro
  JOURNAL   J Biol Chem 296, 100654 (2021)
   PUBMED   33845046
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Xu,D., Feng,Z., Hou,W.T., Jiang,Y.L., Wang,L., Sun,L., Zhou,C.Z.
            and Chen,Y.
  TITLE     Cryo-EM structure of human lysosomal cobalamin exporter ABCD4
  JOURNAL   Cell Res 29 (12), 1039-1041 (2019)
   PUBMED   31467407
  REMARK    GeneRIF: Cryo-EM structure of human lysosomal cobalamin exporter
            ABCD4.
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Holzinger,A., Roscher,A.A., Landgraf,P., Lichtner,P. and
            Kammerer,S.
  TITLE     Genomic organization and chromosomal localization of the human
            peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding
            a peroxisomal ABC transporter
  JOURNAL   FEBS Lett 426 (2), 238-242 (1998)
   PUBMED   9599016
REFERENCE   7  (residues 1 to 329)
  AUTHORS   Gartner,J., Jimenez-Sanchez,G., Roerig,P. and Valle,D.
  TITLE     Genomic organization of the 70-kDa peroxisomal membrane protein
            gene (PXMP1)
  JOURNAL   Genomics 48 (2), 203-208 (1998)
   PUBMED   9521874
REFERENCE   8  (residues 1 to 329)
  AUTHORS   Shani,N., Jimenez-Sanchez,G., Steel,G., Dean,M. and Valle,D.
  TITLE     Identification of a fourth half ABC transporter in the human
            peroxisomal membrane
  JOURNAL   Hum Mol Genet 6 (11), 1925-1931 (1997)
   PUBMED   9302272
REFERENCE   9  (residues 1 to 329)
  AUTHORS   Holzinger,A., Kammerer,S. and Roscher,A.A.
  TITLE     Primary structure of human PMP69, a putative peroxisomal
            ABC-transporter
  JOURNAL   Biochem Biophys Res Commun 237 (1), 152-157 (1997)
   PUBMED   9266848
REFERENCE   10 (residues 1 to 329)
  AUTHORS   Sloan,J.L., Carrillo,N., Adams,D. and Venditti,C.P.
  TITLE     Disorders of Intracellular Cobalamin Metabolism
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301503
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005519.4.
            
            On Jul 19, 2017 this sequence version replaced XP_016877032.1.
            
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the ALD subfamily, which is involved in
            peroxisomal import of fatty acids and/or fatty acyl-CoAs in the
            organelle. All known peroxisomal ABC transporters are half
            transporters which require a partner half transporter molecule to
            form a functional homodimeric or heterodimeric transporter. The
            function of this peroxisomal membrane protein is unknown. However,
            it is speculated that it may function as a heterodimer for another
            peroxisomal ABC transporter and, therefore, may modify the
            adrenoleukodystrophy phenotype. It may also play a role in the
            process of peroxisome biogenesis. Alternative splicing results in
            several protein-coding and non-protein-coding variants. [provided
            by RefSeq, Jul 2017].
            
            Transcript Variant: This variant (23), as well as variants 21, 22,
            and 24, encodes isoform l.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.20845.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..329
                     /product="lysosomal cobalamin transporter ABCD4 isoform l"
                     /EC_number="7.6.2.8"
                     /note="ATP-binding cassette sub-family D member 4;
                     peroxisomal membrane protein 69; 69 kDa peroxisomal
                     ABC-transporter; PMP70-related protein; PXMP1-L;
                     ATP-binding cassette, sub-family D (ALD), member 4;
                     lysosomal cobalamin transporter ABCD4"
                     /calculated_mol_wt=36114
     Region          <1..321
                     /region_name="YddA"
                     /note="ABC-type uncharacterized transport system, permease
                     and ATPase components [General function prediction only];
                     COG4178"
                     /db_xref="CDD:443337"
     Region          124..321
                     /region_name="ABCD_peroxisomal_ALDP"
                     /note="ATP-binding cassette domain of peroxisomal
                     transporter, subfamily D; cd03223"
                     /db_xref="CDD:213190"
     CDS             1..329
                     /gene="ABCD4"
                     /gene_synonym="ABC41; EST352188; MAHCJ; P70R; P79R; PMP69;
                     PXMP1L"
                     /coded_by="NM_001353608.2:572..1561"
                     /note="isoform l is encoded by transcript variant 23"
                     /db_xref="GeneID:5826"
                     /db_xref="HGNC:HGNC:68"
                     /db_xref="MIM:603214"
ORIGIN      
        1 mrslllstvg intfdylgsi lsyvviaipi fsgvygdlsp aelstlvskn afvciylisc
       61 ftqlidlstt lsdvagythr igqlretlld mslksqdcei lgesewgldt ppgwpaaepa
      121 dtafllervs isapssdkpl ikdlslkise gqsllitgnt gtgktsllrv lgglwtstrg
      181 svqmltdfgp hgvlflpqkp fftdgtlreq viyplkevyp dsgsadderi lrflelagls
      241 nlvartegld qqvdwnwydv lspgemqrls farlfylqpk yavldeatsa lteevesely
      301 rigqqlgmtf isvghrqsle kvpvltrma
//
LOCUS       NP_001240309             204 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL15 isoform 1 [Homo sapiens].
ACCESSION   NP_001240309
VERSION     NP_001240309.1
DBSOURCE    REFSEQ: accession NM_001253380.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 204)
  AUTHORS   Wang,G., Qin,M., Zhang,B., Yan,Y., Yang,F., Chen,Q., Liu,Y.,
            Qiao,F. and Ni,Y.
  TITLE     Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification
  JOURNAL   Cell Biol Int 47 (10), 1749-1759 (2023)
   PUBMED   37431269
  REMARK    GeneRIF: Decreased expression of RPL15 and RPL18 exacerbated the
            calcification of valve interstitial cells during aortic valve
            calcification.
REFERENCE   2  (residues 1 to 204)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 204)
  AUTHORS   Xu,C., He,X.Y., Ren,X.H., Han,D. and Cheng,S.X.
  TITLE     Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin in
            Living Circulating Tumor Cells at Single Cell Resolution To Study
            Tumor Heterogeneity
  JOURNAL   Anal Chem 94 (30), 10610-10616 (2022)
   PUBMED   35856393
  REMARK    GeneRIF: Detection of mRNAs of Ribosomal Protein L15 and E-Cadherin
            in Living Circulating Tumor Cells at Single Cell Resolution To
            Study Tumor Heterogeneity.
REFERENCE   4  (residues 1 to 204)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   5  (residues 1 to 204)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   6  (residues 1 to 204)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
REFERENCE   7  (residues 1 to 204)
  AUTHORS   Wang,Q., Yang,C., Zhou,J., Wang,X., Wu,M. and Liu,Z.
  TITLE     Cloning and characterization of full-length human ribosomal protein
            L15 cDNA which was overexpressed in esophageal cancer
  JOURNAL   Gene 263 (1-2), 205-209 (2001)
   PUBMED   11223259
REFERENCE   8  (residues 1 to 204)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 204)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 204)
  AUTHORS   Sieff,C.
  TITLE     DBA Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124914.3, DB461802.1,
            AY347528.1 and AI886077.1.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of four RNA species and approximately
            80 structurally distinct proteins. This gene encodes a member of
            the L15E family of ribosomal proteins and a component of the 60S
            subunit. This gene shares sequence similarity with the yeast
            ribosomal protein YL10 gene. Elevated expression of this gene has
            been observed in esophageal tumors and gastric cancer tissues, and
            deletion of this gene has been observed in a Diamond-Blackfan
            anemia (DBA) patient. As is typical for genes encoding ribosomal
            proteins, there are multiple processed pseudogenes of this gene
            dispersed through the genome. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1-5 encode the same isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.143557.1,
                                           SRR1803613.135180.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..204
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.2"
     Protein         1..204
                     /product="large ribosomal subunit protein eL15 isoform 1"
                     /note="60S ribosomal protein L15; large ribosomal subunit
                     protein eL15"
                     /calculated_mol_wt=24015
     Region          2..191
                     /region_name="Ribosomal_L15e"
                     /note="Ribosomal L15; pfam00827"
                     /db_xref="CDD:459950"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P61314; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P61313.2)"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P61313.2)"
     Region          165..186
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P61313.2)"
     CDS             1..204
                     /gene="RPL15"
                     /gene_synonym="DBA12; EC45; eL15; L15; RPL10; RPLY10;
                     RPYL10"
                     /coded_by="NM_001253380.2:763..1377"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2640.1"
                     /db_xref="GeneID:6138"
                     /db_xref="HGNC:HGNC:10306"
                     /db_xref="MIM:604174"
ORIGIN      
        1 mgaykyiqel wrkkqsdvmr fllrvrcwqy rqlsalhrap rptrpdkarr lgykakqgyv
       61 iyrirvrrgg rkrpvpkgat ygkpvhhgvn qlkfarslqs vaeeragrhc galrvlnsyw
      121 vgedstykff evilidpfhk airrnpdtqw itkpvhkhre mrgltsagrk srglgkghkf
      181 hhtiggsrra awrrrntlql hryr
//
LOCUS       NP_001278847             305 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional adapter 2-alpha isoform b [Homo sapiens].
ACCESSION   NP_001278847
VERSION     NP_001278847.1
DBSOURCE    REFSEQ: accession NM_001291918.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Cochino,A.V., Ioan,A., Farkas,O.M., Liu,M. and Lee,P.Y.
  TITLE     Novel ADA2 Variants in a Romanian Case Series of DADA2
  JOURNAL   J Clin Immunol 43 (8), 1788-1791 (2023)
   PUBMED   37783985
  REMARK    GeneRIF: Novel ADA2 Variants in a Romanian Case Series of DADA2.
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Zhang,X., Lei,G., Zhao,K., Zhang,X. and Dang,C.
  TITLE     CircTADA2A up-regulates MAPK8 by targeting MiR-214-3p and
            recruiting EIF4A3 to promote the invasion and migration of
            non-small cell lung cancer cells
  JOURNAL   Histol Histopathol 38 (7), 837-848 (2023)
   PUBMED   36193940
  REMARK    GeneRIF: CircTADA2A up-regulates MAPK8 by targeting MiR-214-3p and
            recruiting EIF4A3 to promote the invasion and migration of
            non-small cell lung cancer cells.
REFERENCE   4  (residues 1 to 305)
  AUTHORS   Ehlers,L., Bucciol,G., Beysen,D. and Meyts,I.
  CONSRTM   KU Leuven - UZA DADA2 team
  TITLE     ADA2 Deficiency Mimicking Acute Disseminated Encephalomyelitis
  JOURNAL   J Clin Immunol 43 (3), 536-539 (2023)
   PUBMED   36472692
  REMARK    GeneRIF: ADA2 Deficiency Mimicking Acute Disseminated
            Encephalomyelitis.
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Zhang,Y., Yao,H., Li,Y., Yang,L., Zhang,L., Chen,J., Wang,Y. and
            Li,X.
  TITLE     Circular RNA TADA2A promotes proliferation and migration via
            modulating of miR-638/KIAA0101 signal in non-small cell lung cancer
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296306
  REMARK    GeneRIF: Circular RNA TADA2A promotes proliferation and migration
            via modulating of miR638/KIAA0101 signal in nonsmall cell lung
            cancer.
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Henriksson,A., Almlof,T., Ford,J., McEwan,I.J., Gustafsson,J.A. and
            Wright,A.P.
  TITLE     Role of the Ada adaptor complex in gene activation by the
            glucocorticoid receptor
  JOURNAL   Mol Cell Biol 17 (6), 3065-3073 (1997)
   PUBMED   9154805
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Carter,K.C., Wang,L., Shell,B.K., Zamir,I., Berger,S.L. and
            Moore,P.A.
  TITLE     The human transcriptional adaptor genes TADA2L and GCN5L2
            colocalize to chromosome 17q12-q21 and display a similar tissue
            expression pattern
  JOURNAL   Genomics 40 (3), 497-500 (1997)
   PUBMED   9073520
REFERENCE   9  (residues 1 to 305)
  AUTHORS   Wang,L., Mizzen,C., Ying,C., Candau,R., Barlev,N., Brownell,J.,
            Allis,C.D. and Berger,S.L.
  TITLE     Histone acetyltransferase activity is conserved between yeast and
            human GCN5 and is required for complementation of growth and
            transcriptional activation
  JOURNAL   Mol Cell Biol 17 (1), 519-527 (1997)
   PUBMED   8972232
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Candau,R., Moore,P.A., Wang,L., Barlev,N., Ying,C.Y., Rosen,C.A.
            and Berger,S.L.
  TITLE     Identification of human proteins functionally conserved with the
            yeast putative adaptors ADA2 and GCN5
  JOURNAL   Mol Cell Biol 16 (2), 593-602 (1996)
   PUBMED   8552087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA244842.1, BC001172.1 and
            AC243654.3.
            
            Summary: Many DNA-binding transcriptional activator proteins
            enhance the initiation rate of RNA polymerase II-mediated gene
            transcription by interacting functionally with the general
            transcription machinery bound at the basal promoter. Adaptor
            proteins are usually required for this activation, possibly to
            acetylate and destabilize nucleosomes, thereby relieving chromatin
            constraints at the promoter. The protein encoded by this gene is a
            transcriptional activator adaptor and has been found to be part of
            the PCAF histone acetylase complex. Several alternatively spliced
            transcript variants encoding different isoforms of this gene have
            been described, but the full-length nature of some of these
            variants has not been determined. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            represents an alternate transcript termination and polyadenylation
            site compared to variant 1. This results in a shorter isoform (b)
            which has a distinct C-terminus compared to isoform a. Variants 2
            and 4 both encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.128953.1, BC001172.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..305
                     /product="transcriptional adapter 2-alpha isoform b"
                     /note="transcriptional adaptor 2 alpha; transcriptional
                     adapter 2-alpha; ADA2-like protein"
                     /calculated_mol_wt=35913
     Region          28..>272
                     /region_name="COG5114"
                     /note="Histone acetyltransferase complex SAGA/ADA, subunit
                     ADA2 [Chromatin structure and dynamics]"
                     /db_xref="CDD:227445"
     CDS             1..305
                     /gene="TADA2A"
                     /gene_synonym="ADA2; ADA2A; hADA2; KL04P; TADA2L"
                     /coded_by="NM_001291918.2:162..1079"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45656.1"
                     /db_xref="GeneID:6871"
                     /db_xref="HGNC:HGNC:11531"
                     /db_xref="MIM:602276"
ORIGIN      
        1 mdrlgsfsnd psdkppcrgc ssylmepyik caecgpppff lclqcftrgf eykkhqsdht
       61 yeimtsdfpv ldpswtaqee malleavmdc gfgnwqdvan qmctktkeec ekhymkhfin
      121 nplfastlln lkqaeeakta dtaipfhstd dpprptfdsl lsrdmagymp aradfieefd
      181 nyaewdlrdi dfveddsdil halkmavvdi yhsrlkerqr rkkiirdhgl inlrkfqlme
      241 rrypkevqdl yetmrrfari vgpvehdkfi eshacrwfls leqylcvyiy inrrdngvfy
      301 vkfyk
//
LOCUS       NP_001002926             338 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase I subunit RPA43 [Homo sapiens].
ACCESSION   NP_001002926 XP_166508 XP_379792
VERSION     NP_001002926.1
DBSOURCE    REFSEQ: accession NM_001002926.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Daiss,J.L., Pilsl,M., Straub,K., Bleckmann,A., Hocherl,M.,
            Heiss,F.B., Abascal-Palacios,G., Ramsay,E.P., Tluckova,K.,
            Mars,J.C., Furtges,T., Bruckmann,A., Rudack,T., Bernecky,C.,
            Lamour,V., Panov,K., Vannini,A., Moss,T. and Engel,C.
  TITLE     The human RNA polymerase I structure reveals an HMG-like docking
            domain specific to metazoans
  JOURNAL   Life Sci Alliance 5 (11), e202201568 (2022)
   PUBMED   36271492
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 338)
  AUTHORS   Misiaszek,A.D., Girbig,M., Grotsch,H., Baudin,F., Murciano,B.,
            Lafita,A. and Muller,C.W.
  TITLE     Cryo-EM structures of human RNA polymerase I
  JOURNAL   Nat Struct Mol Biol 28 (12), 997-1008 (2021)
   PUBMED   34887565
REFERENCE   3  (residues 1 to 338)
  AUTHORS   Zhao,D., Liu,W., Chen,K., Wu,Z., Yang,H. and Xu,Y.
  TITLE     Structure of the human RNA polymerase I elongation complex
  JOURNAL   Cell Discov 7 (1), 97 (2021)
   PUBMED   34671025
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 338)
  AUTHORS   He,M., Xu,M., Zhang,B., Liang,J., Chen,P., Lee,J.Y., Johnson,T.A.,
            Li,H., Yang,X., Dai,J., Liang,L., Gui,L., Qi,Q., Huang,J., Li,Y.,
            Adair,L.S., Aung,T., Cai,Q., Cheng,C.Y., Cho,M.C., Cho,Y.S.,
            Chu,M., Cui,B., Gao,Y.T., Go,M.J., Gu,D., Gu,W., Guo,H., Hao,Y.,
            Hong,J., Hu,Z., Hu,Y., Huang,J., Hwang,J.Y., Ikram,M.K., Jin,G.,
            Kang,D.H., Khor,C.C., Kim,B.J., Kim,H.T., Kubo,M., Lee,J., Lee,J.,
            Lee,N.R., Li,R., Li,J., Liu,J., Longe,J., Lu,W., Lu,X., Miao,X.,
            Okada,Y., Ong,R.T., Qiu,G., Seielstad,M., Sim,X., Song,H.,
            Takeuchi,F., Tanaka,T., Taylor,P.R., Wang,L., Wang,W., Wang,Y.,
            Wu,C., Wu,Y., Xiang,Y.B., Yamamoto,K., Yang,H., Liao,M., Yokota,M.,
            Young,T., Zhang,X., Kato,N., Wang,Q.K., Zheng,W., Hu,F.B., Lin,D.,
            Shen,H., Teo,Y.Y., Mo,Z., Wong,T.Y., Lin,X., Mohlke,K.L., Ning,G.,
            Tsunoda,T., Han,B.G., Shu,X.O., Tai,E.S., Wu,T. and Qi,L.
  TITLE     Meta-analysis of genome-wide association studies of adult height in
            East Asians identifies 17 novel loci
  JOURNAL   Hum Mol Genet 24 (6), 1791-1800 (2015)
   PUBMED   25429064
REFERENCE   5  (residues 1 to 338)
  AUTHORS   Foroud,T., Lai,D., Koller,D., Van't Hof,F., Kurki,M.I.,
            Anderson,C.S., Brown,R.D. Jr., Connolly,E.S., Eriksson,J.G.,
            Flaherty,M., Fornage,M., von Und Zu Fraunberg,M., Gaal,E.I.,
            Laakso,A., Hernesniemi,J., Huston,J., Jaaskelainen,J.E.,
            Kiemeney,L.A., Kivisaari,R., Kleindorfer,D., Ko,N., Lehto,H.,
            Mackey,J., Meissner,I., Moomaw,C.J., Mosley,T.H., Moskala,M.,
            Niemela,M., Palotie,A., Pera,J., Rinkel,G., Ripke,S., Rouleau,G.,
            Ruigrok,Y., Sauerbeck,L., Slowik,A., Vermeulen,S.H., Woo,D.,
            Worrall,B.B. and Broderick,J.
  CONSRTM   Familial Intracranial Aneurysm Study Investigators
  TITLE     Genome-wide association study of intracranial aneurysm identifies a
            new association on chromosome 7
  JOURNAL   Stroke 45 (11), 3194-3199 (2014)
   PUBMED   25256182
REFERENCE   6  (residues 1 to 338)
  AUTHORS   Goodfellow,S.J. and Zomerdijk,J.C.
  TITLE     Basic mechanisms in RNA polymerase I transcription of the ribosomal
            RNA genes
  JOURNAL   Subcell Biochem 61, 211-236 (2013)
   PUBMED   23150253
  REMARK    Review article
REFERENCE   7  (residues 1 to 338)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   8  (residues 1 to 338)
  AUTHORS   Yuan,X., Zhao,J., Zentgraf,H., Hoffmann-Rohrer,U. and Grummt,I.
  TITLE     Multiple interactions between RNA polymerase I, TIF-IA and TAF(I)
            subunits regulate preinitiation complex assembly at the ribosomal
            gene promoter
  JOURNAL   EMBO Rep 3 (11), 1082-1087 (2002)
   PUBMED   12393749
REFERENCE   9  (residues 1 to 338)
  AUTHORS   Kosan,C. and Kunz,J.
  TITLE     Identification and characterisation of the gene TWIST NEIGHBOR
            (TWISTNB) located in the microdeletion syndrome 7p21 region
  JOURNAL   Cytogenet Genome Res 97 (3-4), 167-170 (2002)
   PUBMED   12438708
  REMARK    GeneRIF: describe the localisation and characterisation of the
            TWIST NEIGHBOR (TWISTNB) gene
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC056267.1, AK090846.1 and AC004940.1.
            
            On or before Aug 30, 2004 this sequence version replaced
            XP_379792.1, XP_166508.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.167769.1,
                                           SRR1660805.17726.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2159607 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222567.6/ ENSP00000222567.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.1"
     Protein         1..338
                     /product="DNA-directed RNA polymerase I subunit RPA43"
                     /note="twist neighbor protein; DNA-directed RNA polymerase
                     I subunit F"
                     /calculated_mol_wt=37301
     Region          40..126
                     /region_name="RNAP_I_Rpa43_N"
                     /note="Rpa43, N-terminal ribonucleoprotein (RNP) domain.
                     Rpa43 is a subunit of eukaryotic RNA polymerase (RNAP) I
                     that is homologous to Rpb7 of eukaryotic RNAP II, Rpc25 of
                     eukaryotic RNP III, and RpoE of archaeal RNAP. Rpa43 has
                     two domains, an N-terminal RNP...; cd04328"
                     /db_xref="CDD:239820"
     Site            order(48..52,54,81,87,91..93,119,124,126)
                     /site_type="other"
                     /note="putative Rpa14 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239820"
     Region          125..>157
                     /region_name="RPA43_OB"
                     /note="RPA43 OB domain in RNA Pol I; pfam17875"
                     /db_xref="CDD:465545"
     Region          209..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B726.1)"
     Site            242
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q3B726.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q3B726.1)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q3B726.1)"
     Site            322
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q3B726.1)"
     Site            328
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q3B726.1)"
     CDS             1..338
                     /gene="POLR1F"
                     /gene_synonym="A43; RPA43; TWISTNB"
                     /coded_by="NM_001002926.2:22..1038"
                     /db_xref="CCDS:CCDS34606.1"
                     /db_xref="GeneID:221830"
                     /db_xref="HGNC:HGNC:18027"
                     /db_xref="MIM:608312"
ORIGIN      
        1 maagcseapr paaasdgslv gqagvlpcle lptyaaacal vnsrysclva gphqrhials
       61 prylnrkrtg ireqldaell rysesllgvp iaydnikvvg elgdiyddqg hihlnieadf
      121 vifcpepgqk lmgivnkvss shigclvhgc fnasipkpeq lsaeqwqtme inmgdelefe
      181 vfrldsdaag vfcirgklni tslqfkrsev seevtengte eaakkpkkkk kkkdpetyev
      241 dsgttkladd addtpmeesa lqntnnangi weeepkkkkk kkkhqevqdq dpvfqgsdss
      301 gyqsdhkkkk kkrkhseeae ftpplkcspk rkgksnfl
//
LOCUS       NP_001258764             630 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 120 isoform 3 [Homo sapiens].
ACCESSION   NP_001258764
VERSION     NP_001258764.1
DBSOURCE    REFSEQ: accession NM_001271835.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 630)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 630)
  AUTHORS   Mo,X., Niu,Q., Ivanov,A.A., Tsang,Y.H., Tang,C., Shu,C., Li,Q.,
            Qian,K., Wahafu,A., Doyle,S.P., Cicka,D., Yang,X., Fan,D.,
            Reyna,M.A., Cooper,L.A.D., Moreno,C.S., Zhou,W., Owonikoko,T.K.,
            Lonial,S., Khuri,F.R., Du,Y., Ramalingam,S.S., Mills,G.B. and Fu,H.
  TITLE     Systematic discovery of mutation-directed neo-protein-protein
            interactions in cancer
  JOURNAL   Cell 185 (11), 1974-1985 (2022)
   PUBMED   35512704
REFERENCE   3  (residues 1 to 630)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 630)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 630)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 630)
  AUTHORS   Huang,N., Xia,Y., Zhang,D., Wang,S., Bao,Y., He,R., Teng,J. and
            Chen,J.
  TITLE     Hierarchical assembly of centriole subdistal appendages via
            centrosome binding proteins CCDC120 and CCDC68
  JOURNAL   Nat Commun 8, 15057 (2017)
   PUBMED   28422092
  REMARK    GeneRIF: centrosome-binding proteins, coiled-coil domain containing
            (CCDC) 120 and CCDC68 are two novel subdistal appendages (SDA)
            components required for hierarchical SDA assembly in human cells.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 630)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 630)
  AUTHORS   Torii,T., Miyamoto,Y., Tago,K., Sango,K., Nakamura,K., Sanbe,A.,
            Tanoue,A. and Yamauchi,J.
  TITLE     Arf6 guanine nucleotide exchange factor cytohesin-2 binds to
            CCDC120 and is transported along neurites to mediate neurite growth
  JOURNAL   J Biol Chem 289 (49), 33887-33903 (2014)
   PUBMED   25326380
  REMARK    GeneRIF: Arf6 guanine nucleotide exchange factor cytohesin-2 binds
            to CCDC120 and is transported along neurites to mediate neurite
            growth.
REFERENCE   9  (residues 1 to 630)
  AUTHORS   Xin,X., Rual,J.F., Hirozane-Kishikawa,T., Hill,D.E., Vidal,M.,
            Boone,C. and Thierry-Mieg,N.
  TITLE     Shifted Transversal Design smart-pooling for high coverage
            interactome mapping
  JOURNAL   Genome Res 19 (7), 1262-1269 (2009)
   PUBMED   19447967
REFERENCE   10 (residues 1 to 630)
  AUTHORS   Tarpey,P.S., Smith,R., Pleasance,E., Whibley,A., Edkins,S.,
            Hardy,C., O'Meara,S., Latimer,C., Dicks,E., Menzies,A.,
            Stephens,P., Blow,M., Greenman,C., Xue,Y., Tyler-Smith,C.,
            Thompson,D., Gray,K., Andrews,J., Barthorpe,S., Buck,G., Cole,J.,
            Dunmore,R., Jones,D., Maddison,M., Mironenko,T., Turner,R.,
            Turrell,K., Varian,J., West,S., Widaa,S., Wray,P., Teague,J.,
            Butler,A., Jenkinson,A., Jia,M., Richardson,D., Shepherd,R.,
            Wooster,R., Tejada,M.I., Martinez,F., Carvill,G., Goliath,R., de
            Brouwer,A.P., van Bokhoven,H., Van Esch,H., Chelly,J., Raynaud,M.,
            Ropers,H.H., Abidi,F.E., Srivastava,A.K., Cox,J., Luo,Y.,
            Mallya,U., Moon,J., Parnau,J., Mohammed,S., Tolmie,J.L.,
            Shoubridge,C., Corbett,M., Gardner,A., Haan,E., Rujirabanjerd,S.,
            Shaw,M., Vandeleur,L., Fullston,T., Easton,D.F., Boyle,J.,
            Partington,M., Hackett,A., Field,M., Skinner,C., Stevenson,R.E.,
            Bobrow,M., Turner,G., Schwartz,C.E., Gecz,J., Raymond,F.L.,
            Futreal,P.A. and Stratton,M.R.
  TITLE     A systematic, large-scale resequencing screen of X-chromosome
            coding exons in mental retardation
  JOURNAL   Nat Genet 41 (5), 535-543 (2009)
   PUBMED   19377476
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA102343.1, AK315837.1 and
            BC008769.2.
            
            Summary: This gene encodes a protein that contains a coiled-coil
            domain. Several alternatively spliced transcript variants encoding
            multiple isoforms have been found for this gene. [provided by
            RefSeq, Nov 2012].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and
            coding sequence and differs in the 3' UTR and coding sequence
            compared to variant 1. The resulting isoform (3) is shorter at the
            N-terminus and has a shorter and distinct C-terminus compared to
            isoform 1. Variants 3, 5, and 6 all encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BC008769.2, AK291370.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1968540,
                                    SAMEA2142348 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..630
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..630
                     /product="coiled-coil domain-containing protein 120
                     isoform 3"
                     /note="coiled-coil domain-containing protein 120"
                     /calculated_mol_wt=67437
     Region          2..141
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     Region          31..70
                     /region_name="Involved in CYTH2-binding.
                     /evidence=ECO:0000269|PubMed:25326380"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HB5.1)"
     Region          212..435
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HB5.1)"
     Site            358
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96HB5.1)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96HB5.1)"
     Site            435
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:A2AEV7; propagated from
                     UniProtKB/Swiss-Prot (Q96HB5.1)"
     Region          457..534
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HB5.1)"
     CDS             1..630
                     /gene="CCDC120"
                     /gene_synonym="JM11"
                     /coded_by="NM_001271835.1:296..2188"
                     /note="isoform 3 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS14316.1"
                     /db_xref="GeneID:90060"
                     /db_xref="HGNC:HGNC:28910"
                     /db_xref="MIM:300947"
ORIGIN      
        1 mevkgqliss ptfnapaalf geaapqvkse rlrglldrqr tlqealslkl qelrkvclqe
       61 aeltgqlppe cplepgerpq lvrrrpptar ayppphpnqa hhslcpaeel alealerevs
      121 vqqqiaaaar rlalapdlst eqrrrrrqvq adalrrlhel eeqlrdvrar lglpvlplpq
      181 plplstgsvi ttqgvclgmr laqlsqedvv lhsessslse sgashdneep hgcfslaerp
      241 sppkawdqlr avsggsperr tpwkpppsdl ygdlksrrns vasptsptrs lprsassfeg
      301 rsvpatpvlt rgagpqlckp eglhsrqwsg sqdsqmgfpr adpasdrasl fvartrrsns
      361 seallvdraa gggagsppap lapsasgppv ckssevlyer pqptpafssr tagppdppra
      421 arpssaapas rgaprlppvc gdflldysld rglprsgggt gwgelppaae vpgplsrrdg
      481 lltmlpgppp vyaadsnspl lrtkdphtra trtkpcglpp eaaegpevhp npllwmpppt
      541 ripsagersg hknlaleglr dwyirnsgla agpqrrpvlp svgpphppfl harcyevgqa
      601 lygapsqapl phsrsftapp vsgryggcfy
//
LOCUS       NP_149122                352 aa            linear   PRI 20-NOV-2025
DEFINITION  protein Wnt-3a precursor [Homo sapiens].
ACCESSION   NP_149122
VERSION     NP_149122.1
DBSOURCE    REFSEQ: accession NM_033131.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Zuo,X., Wang,X., Ma,T., Chen,S., Cao,P., Cheng,H., Yang,N., Han,X.,
            Gao,W., Liu,X. and Sun,Y.
  TITLE     TNFRSF19 within the 13q12.12 Risk Locus Functions as a Lung Cancer
            Suppressor by Binding Wnt3a to Inhibit Wnt/beta-Catenin Signaling
  JOURNAL   Mol Cancer Res 22 (3), 227-239 (2024)
   PUBMED   38047807
  REMARK    GeneRIF: TNFRSF19 within the 13q12.12 Risk Locus Functions as a
            Lung Cancer Suppressor by Binding Wnt3a to Inhibit Wnt/beta-Catenin
            Signaling.
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Meng,X. and Zhu,H.
  TITLE     SOX9 Inhibits the Progression of Osteonecrosis of the Femoral Head
            via the Activation of the Wnt/Beta-Catenin Pathway
  JOURNAL   J Invest Surg 36 (1), 2197054 (2023)
   PUBMED   37076124
  REMARK    GeneRIF: SOX9 Inhibits the Progression of Osteonecrosis of the
            Femoral Head via the Activation of the Wnt/Beta-Catenin Pathway.
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Wang,J., Shen,D., Li,S., Li,Q., Zuo,Q., Lu,J., Tang,D., Feng,Y.,
            Yin,P., Chen,C. and Chen,T.
  TITLE     LINC00665 activating Wnt3a/beta-catenin signaling by bond with YBX1
            promotes gastric cancer proliferation and metastasis
  JOURNAL   Cancer Gene Ther 30 (11), 1530-1542 (2023)
   PUBMED   37563362
  REMARK    GeneRIF: LINC00665 activating Wnt3a/beta-catenin signaling by bond
            with YBX1 promotes gastric cancer proliferation and metastasis.
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Bitencourt Reis,C.L., Nakane Matsumoto,M.A., Baratto-Filho,F.,
            Scariot,R., Sasso Stuani,M.B., Lourenco Romano,F., Della
            Coletta,R., Silva Barroso de Oliveira,D., Proff,P., Kirschneck,C.
            and Calvano Kuchler,E.
  TITLE     Impact of genetic variations in the WNT family members and RUNX2 on
            dental and skeletal maturation: a cross-sectional study
  JOURNAL   Head Face Med 19 (1), 26 (2023)
   PUBMED   37400934
  REMARK    GeneRIF: Impact of genetic variations in the WNT family members and
            RUNX2 on dental and skeletal maturation: a cross-sectional study.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Tanaka,K., Okabayashi,K., Asashima,M., Perrimon,N. and Kadowaki,T.
  TITLE     The evolutionarily conserved porcupine gene family is involved in
            the processing of the Wnt family
  JOURNAL   Eur J Biochem 267 (13), 4300-4311 (2000)
   PUBMED   10866835
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Lee,C.S., Buttitta,L.A., May,N.R., Kispert,A. and Fan,C.M.
  TITLE     SHH-N upregulates Sfrp2 to mediate its competitive interaction with
            WNT1 and WNT4 in the somitic mesoderm
  JOURNAL   Development 127 (1), 109-118 (2000)
   PUBMED   10654605
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Gazit,A., Yaniv,A., Bafico,A., Pramila,T., Igarashi,M.,
            Kitajewski,J. and Aaronson,S.A.
  TITLE     Human frizzled 1 interacts with transforming Wnts to transduce a
            TCF dependent transcriptional response
  JOURNAL   Oncogene 18 (44), 5959-5966 (1999)
   PUBMED   10557084
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Huguet,E.L., McMahon,J.A., McMahon,A.P., Bicknell,R. and
            Harris,A.L.
  TITLE     Differential expression of human Wnt genes 2, 3, 4, and 7B in human
            breast cell lines and normal and disease states of human breast
            tissue
  JOURNAL   Cancer Res 54 (10), 2615-2621 (1994)
   PUBMED   8168088
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Smolich,B.D., McMahon,J.A., McMahon,A.P. and Papkoff,J.
  TITLE     Wnt family proteins are secreted and associated with the cell
            surface
  JOURNAL   Mol Biol Cell 4 (12), 1267-1275 (1993)
   PUBMED   8167409
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL136379.19, DA742143.1,
            AB060284.1, AK056278.1 and CA437424.1.
            
            Summary: The WNT gene family consists of structurally related genes
            which encode secreted signaling proteins. These proteins have been
            implicated in oncogenesis and in several developmental processes,
            including regulation of cell fate and patterning during
            embryogenesis. This gene is a member of the WNT gene family. It
            encodes a protein which shows 96% amino acid identity to mouse
            Wnt3A protein, and 84% to human WNT3 protein, another WNT gene
            product. This gene is clustered with WNT14 gene, another family
            member, in chromosome 1q42 region. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056278.1, SRR14038193.3009024.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000284523.2/ ENSP00000284523.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..352
                     /product="protein Wnt-3a precursor"
                     /note="protein Wnt-3a; wingless-type MMTV integration site
                     family, member 3A"
                     /calculated_mol_wt=37445
     sig_peptide     1..18
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1938
     mat_peptide     19..352
                     /product="Protein Wnt-3a. /id=PRO_0000041418"
                     /note="propagated from UniProtKB/Swiss-Prot (P56704.2)"
                     /calculated_mol_wt=37445
     Site            26..27
                     /site_type="cleavage"
                     /note="Cleavage, by TIKI1 and TIKI2.
                     /evidence=ECO:0000250|UniProtKB:P27467; propagated from
                     UniProtKB/Swiss-Prot (P56704.2)"
     Region          39..352
                     /region_name="Wnt_Wnt3_Wnt3a"
                     /note="Wnt domain found in proto-oncogene Wnt-3 and
                     similar proteins; cd19335"
                     /db_xref="CDD:381709"
     Site            87
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21244856; propagated from
                     UniProtKB/Swiss-Prot (P56704.2)"
     Site            order(204..205,208..210,218,331,333,335,337)
                     /site_type="other"
                     /note="Frizzled receptor binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381709"
     Site            298
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:21244856; propagated from
                     UniProtKB/Swiss-Prot (P56704.2)"
     CDS             1..352
                     /gene="WNT3A"
                     /coded_by="NM_033131.4:132..1190"
                     /db_xref="CCDS:CCDS1564.1"
                     /db_xref="GeneID:89780"
                     /db_xref="HGNC:HGNC:15983"
                     /db_xref="MIM:606359"
ORIGIN      
        1 maplgyflll cslkqalgsy piwwslavgp qysslgsqpi lcasipglvp kqlrfcrnyv
       61 eimpsvaegi kigiqecqhq frgrrwnctt vhdslaifgp vldkatresa fvhaiasagv
      121 afavtrscae gtaaicgcss rhqgspgkgw kwggcsedie fggmvsrefa darenrpdar
      181 samnrhnnea grqaiashmh lkckchglsg scevktcwws qpdfraigdf lkdkydsase
      241 mvvekhresr gwvetlrpry tyfkvpterd lvyyeaspnf cepnpetgsf gtrdrtcnvs
      301 shgidgcdll ccgrghnara errrekcrcv fhwccyvscq ectrvydvht ck
//
LOCUS       NP_009194                308 aa            linear   PRI 20-NOV-2025
DEFINITION  coatomer subunit epsilon isoform a [Homo sapiens].
ACCESSION   NP_009194
VERSION     NP_009194.2
DBSOURCE    REFSEQ: accession NM_007263.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 308)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 308)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 308)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 308)
  AUTHORS   Shima,D.T., Scales,S.J., Kreis,T.E. and Pepperkok,R.
  TITLE     Segregation of COPI-rich and anterograde-cargo-rich domains in
            endoplasmic-reticulum-to-Golgi transport complexes
  JOURNAL   Curr Biol 9 (15), 821-824 (1999)
   PUBMED   10469566
REFERENCE   7  (residues 1 to 308)
  AUTHORS   Faulstich,D., Auerbach,S., Orci,L., Ravazzola,M., Wegchingel,S.,
            Lottspeich,F., Stenbeck,G., Harter,C., Wieland,F.T. and
            Tschochner,H.
  TITLE     Architecture of coatomer: molecular characterization of delta-COP
            and protein interactions within the complex
  JOURNAL   J Cell Biol 135 (1), 53-61 (1996)
   PUBMED   8858162
REFERENCE   8  (residues 1 to 308)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   9  (residues 1 to 308)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   10 (residues 1 to 308)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI520280.1 and AI680336.1.
            
            On Jun 9, 2003 this sequence version replaced NP_009194.1.
            
            Summary: The product of this gene is an epsilon subunit of coatomer
            protein complex. Coatomer is a cytosolic protein complex that binds
            to dilysine motifs and reversibly associates with Golgi
            non-clathrin-coated vesicles. It is required for budding from Golgi
            membranes, and is essential for the retrograde Golgi-to-ER
            transport of dilysine-tagged proteins. Coatomer complex consists of
            at least the alpha, beta, beta', gamma, delta, epsilon and zeta
            subunits. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222584.1, SRR1163657.39938.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262812.9/ ENSP00000262812.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..308
                     /product="coatomer subunit epsilon isoform a"
                     /note="coatomer epsilon subunit; epsilon coat protein;
                     coatomer subunit epsilon; coatomer protein complex subunit
                     epsilon; COPI coat complex subunit epsilon"
                     /calculated_mol_wt=34351
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O14579.3)"
     Region          17..305
                     /region_name="Coatomer_E"
                     /note="Coatomer epsilon subunit; pfam04733"
                     /db_xref="CDD:398419"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14579.3)"
     Site            99
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O14579.3)"
     Region          215..245
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..308
                     /gene="COPE"
                     /gene_synonym="epsilon-COP"
                     /coded_by="NM_007263.4:40..966"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12387.1"
                     /db_xref="GeneID:11316"
                     /db_xref="HGNC:HGNC:2234"
                     /db_xref="MIM:606942"
ORIGIN      
        1 mappapgpas ggsgevdelf dvknafyigs yqqcineaqr vklssperdv erdvflyray
       61 laqrkfgvvl deikpssape lqavrmfady lahesrrdsi vaeldremsr svdvtnttfl
      121 lmaasiylhd qnpdaalral hqgdslecta mtvqillkld rldlarkelk rmqdldedat
      181 ltqlatawvs latggeklqd ayyifqemad kcsptlllln gqaachmaqg rweaaegllq
      241 ealdkdsgyp etlvnlivls qhlgkppevt nrylsqlkda hrshpfikey qakendfdrl
      301 vlqyapsa
//
LOCUS       NP_003755                287 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-11 [Homo sapiens].
ACCESSION   NP_003755
VERSION     NP_003755.2
DBSOURCE    REFSEQ: accession NM_003764.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 287)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 287)
  AUTHORS   Kogl,T., Chang,H.F., Staniek,J., Chiang,S.C.C., Thoulass,G.,
            Lao,J., Weissert,K., Dettmer-Monaco,V., Geiger,K., Manna,P.T.,
            Beziat,V., Momenilandi,M., Tu,S.M., Keppler,S.J., Pattu,V.,
            Wolf,P., Kupferschmid,L., Tholen,S., Covill,L.E., Ebert,K.,
            Straub,T., Gross,M., Gather,R., Engel,H., Salzer,U., Schell,C.,
            Maier,S., Lehmberg,K., Cornu,T.I., Pircher,H., Shahrooei,M.,
            Parvaneh,N., Elling,R., Rizzi,M., Bryceson,Y.T., Ehl,S., Aichele,P.
            and Ammann,S.
  TITLE     Patients and mice with deficiency in the SNARE protein SYNTAXIN-11
            have a secondary B cell defect
  JOURNAL   J Exp Med 221 (7) (2024)
   PUBMED   38722309
  REMARK    GeneRIF: Patients and mice with deficiency in the SNARE protein
            SYNTAXIN-11 have a secondary B cell defect.
            Erratum:[J Exp Med. 2024 Jul 1;221(7):e2022112205142024c. doi:
            10.1084/jem.2022112205142024c. PMID: 38771261]
REFERENCE   3  (residues 1 to 287)
  AUTHORS   Wang,J., Li,D.L., Zheng,L.F., Ren,S., Huang,Z.Q., Tao,Y., Liu,Z.,
            Shang,Y., Pang,D., Guo,H., Zeng,T., Wang,H.R., Huang,H., Du,X.,
            Ye,H., Zhou,H.M., Li,P. and Zhao,T.J.
  TITLE     Dynamic palmitoylation of STX11 controls injury-induced fatty acid
            uptake to promote muscle regeneration
  JOURNAL   Dev Cell 59 (3), 384-399 (2024)
   PUBMED   38198890
  REMARK    GeneRIF: Dynamic palmitoylation of STX11 controls injury-induced
            fatty acid uptake to promote muscle regeneration.
REFERENCE   4  (residues 1 to 287)
  AUTHORS   Ganesan,S., Alvarez,N.N., Steiner,S., Fowler,K.M., Corona,A.K. and
            Roy,C.R.
  TITLE     Syntaxin 11 Contributes to the Interferon-Inducible Restriction of
            Coxiella burnetii Intracellular Infection
  JOURNAL   mBio 14 (1), e0354522 (2023)
   PUBMED   36728431
  REMARK    GeneRIF: Syntaxin 11 Contributes to the Interferon-Inducible
            Restriction of Coxiella burnetii Intracellular Infection.
REFERENCE   5  (residues 1 to 287)
  AUTHORS   zur Stadt,U., Schmidt,S., Kasper,B., Beutel,K., Diler,A.S.,
            Henter,J.I., Kabisch,H., Schneppenheim,R., Nurnberg,P., Janka,G.
            and Hennies,H.C.
  TITLE     Linkage of familial hemophagocytic lymphohistiocytosis (FHL) type-4
            to chromosome 6q24 and identification of mutations in syntaxin 11
  JOURNAL   Hum Mol Genet 14 (6), 827-834 (2005)
   PUBMED   15703195
REFERENCE   6  (residues 1 to 287)
  AUTHORS   Martin-Martin,B., Nabokina,S.M., Lazo,P.A. and Mollinedo,F.
  TITLE     Co-expression of several human syntaxin genes in neutrophils and
            differentiating HL-60 cells: variant isoforms and detection of
            syntaxin 1
  JOURNAL   J Leukoc Biol 65 (3), 397-406 (1999)
   PUBMED   10080545
REFERENCE   7  (residues 1 to 287)
  AUTHORS   Valdez,A.C., Cabaniols,J.P., Brown,M.J. and Roche,P.A.
  TITLE     Syntaxin 11 is associated with SNAP-23 on late endosomes and the
            trans-Golgi network
  JOURNAL   J Cell Sci 112 (Pt 6), 845-854 (1999)
   PUBMED   10036234
REFERENCE   8  (residues 1 to 287)
  AUTHORS   Advani,R.J., Bae,H.R., Bock,J.B., Chao,D.S., Doung,Y.C.,
            Prekeris,R., Yoo,J.S. and Scheller,R.H.
  TITLE     Seven novel mammalian SNARE proteins localize to distinct membrane
            compartments
  JOURNAL   J Biol Chem 273 (17), 10317-10324 (1998)
   PUBMED   9553086
REFERENCE   9  (residues 1 to 287)
  AUTHORS   Tang,B.L., Low,D.Y. and Hong,W.
  TITLE     Syntaxin 11: a member of the syntaxin family without a carboxyl
            terminal transmembrane domain
  JOURNAL   Biochem Biophys Res Commun 245 (2), 627-632 (1998)
   PUBMED   9571206
REFERENCE   10 (residues 1 to 287)
  AUTHORS   Zhang,K., Astigarraga,I., Bryceson,Y., Lehmberg,K., Machowicz,R.,
            Marsh,R., Sieni,E., Wang,Z. and Nichols,K.E.
  TITLE     Familial Hemophagocytic Lymphohistiocytosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301617
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM150302.1, BC033519.1,
            BQ030324.1, AL135917.15, CR739089.1, AI791689.1 and BF941242.1.
            
            On Aug 15, 2003 this sequence version replaced NP_003755.1.
            
            Summary: This gene encodes a member of the syntaxin family.
            Syntaxins have been implicated in the targeting and fusion of
            intracellular transport vesicles. This family member may regulate
            protein transport among late endosomes and the trans-Golgi network.
            Mutations in this gene have been associated with familial
            hemophagocytic lymphohistiocytosis. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.380161.1,
                                           SRR1660809.237270.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000367568.5/ ENSP00000356540.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..287
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q24.2"
     Protein         1..287
                     /product="syntaxin-11"
                     /calculated_mol_wt=33065
     Region          43..238
                     /region_name="Syntaxin"
                     /note="pfam00804"
                     /db_xref="CDD:459942"
     Region          207..273
                     /region_name="SNARE"
                     /note="SNARE motif; cl22856"
                     /db_xref="CDD:473982"
     Site            order(235,242,245)
                     /site_type="other"
                     /note="flanking leucine-zipper layers"
                     /db_xref="CDD:277192"
     Site            238
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277192"
     CDS             1..287
                     /gene="STX11"
                     /gene_synonym="FHL4; HLH4; HPLH4"
                     /coded_by="NM_003764.4:193..1056"
                     /db_xref="CCDS:CCDS5205.1"
                     /db_xref="GeneID:8676"
                     /db_xref="HGNC:HGNC:11429"
                     /db_xref="MIM:605014"
ORIGIN      
        1 mkdrlaelld lskqydqqfp dgddefdsph edivfetdhi leslyrdird iqdenqllva
       61 dvkrlgkqna rfltsmrrls sikrdtnsia kaikargevi hcklramkel seaaeaqhgp
      121 hsavarisra qynaltltfq ramhdynqae mkqrdnckir iqrqleimgk evsgdqiedm
      181 feqgkwdvfs enlladvkga raalneiesr hrellrlesr irdvhelflq mavlvekqad
      241 tlnvielnvq ktvdytgqak aqvrkavqye eknpcrtlcc fccpclk
//
LOCUS       NP_150596                192 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptidase complex catalytic subunit SEC11C isoform 1 [Homo
            sapiens].
ACCESSION   NP_150596
VERSION     NP_150596.1
DBSOURCE    REFSEQ: accession NM_033280.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Zhang,N., Cao,S., Sun,R., Wang,Y., Liu,L., Wang,W. and Meng,X.
  TITLE     Signal peptidase 21 suppresses cell proliferation, migration, and
            invasion via the PTEN-PI3K/Akt signaling pathway in lung
            adenocarcinoma
  JOURNAL   PeerJ 10, e14206 (2022)
   PUBMED   36275477
  REMARK    GeneRIF: Signal peptidase 21 suppresses cell proliferation,
            migration, and invasion via the PTEN-PI3K/Akt signaling pathway in
            lung adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
  REMARK    GeneRIF: Structure of the human signal peptidase complex reveals
            the determinants for signal peptide cleavage.
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 192)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 192)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 192)
  AUTHORS   Oue,N., Naito,Y., Hayashi,T., Takigahira,M., Kawano-Nagatsuma,A.,
            Sentani,K., Sakamoto,N., Zarni Oo,H., Uraoka,N., Yanagihara,K.,
            Ochiai,A., Sasaki,H. and Yasui,W.
  TITLE     Signal peptidase complex 18, encoded by SEC11A, contributes to
            progression via TGF-alpha secretion in gastric cancer
  JOURNAL   Oncogene 33 (30), 3918-3926 (2014)
   PUBMED   23995782
  REMARK    Erratum:[Oncogene. 2019 Jul;38(28):5748. doi:
            10.1038/s41388-019-0837-z. PMID: 31175341]
REFERENCE   8  (residues 1 to 192)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 192)
  AUTHORS   Dodson,G. and Steiner,D.
  TITLE     The role of assembly in insulin's biosynthesis
  JOURNAL   Curr Opin Struct Biol 8 (2), 189-194 (1998)
   PUBMED   9631292
  REMARK    Review article
REFERENCE   10 (residues 1 to 192)
  AUTHORS   Shelness,G.S. and Blobel,G.
  TITLE     Two subunits of the canine signal peptidase complex are homologous
            to yeast SEC11 protein
  JOURNAL   J Biol Chem 265 (16), 9512-9519 (1990)
   PUBMED   2188978
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM789622.1 and AF212233.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279839.6784.1,
                                           SRR3476690.136078.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000587834.6/ ENSP00000468633.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.32"
     Protein         1..192
                     /product="signal peptidase complex catalytic subunit
                     SEC11C isoform 1"
                     /EC_number="3.4.21.89"
                     /note="signal peptidase complex catalytic subunit SEC11C;
                     SEC11-like protein 3; SPase 21 kDa subunit; microsomal
                     signal peptidase 21 kDa subunit; SEC11-like 3; signal
                     peptidase complex 21"
                     /calculated_mol_wt=21411
     Site            29..48
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY50.3)"
     Region          34..167
                     /region_name="Peptidase_S24_S26"
                     /note="The S24, S26 LexA/signal peptidase superfamily
                     contains LexA-related and type I signal peptidase
                     families. The S24 LexA protein domains include: the lambda
                     repressor CI/C2 family and related bacterial prophage
                     repressor proteins; LexA (EC 3.4.21.88), the...; cl10465"
                     /db_xref="CDD:447902"
     Site            order(68,108)
                     /site_type="active"
                     /note="Catalytic site [active]"
                     /db_xref="CDD:119398"
     Region          177..188
                     /region_name="C-terminal short (CTS) helix.
                     /evidence=ECO:0000269|PubMed:34388369"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BY50.3)"
     CDS             1..192
                     /gene="SEC11C"
                     /gene_synonym="SEC11L3; SPC21; SPCS4C"
                     /coded_by="NM_033280.4:66..644"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11970.1"
                     /db_xref="GeneID:90701"
                     /db_xref="HGNC:HGNC:23400"
ORIGIN      
        1 mvragavgah lpasgldifg dlkkmnkrql yyqvlnfami vssalmiwkg livltgsesp
       61 ivvvlsgsme pafhrgdllf ltnfredpir ageivvfkve grdipivhrv ikvhekdngd
      121 ikfltkgdnn evddrglyke gqnwlekkdv vgrargflpy vgmvtiimnd ypkfkyalla
      181 vmgayvllkr es
//
LOCUS       NP_055144               1401 aa            linear   PRI 20-NOV-2025
DEFINITION  enhancer of mRNA-decapping protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_055144
VERSION     NP_055144.3
DBSOURCE    REFSEQ: accession NM_014329.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1401)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1401)
  AUTHORS   Bloch,D.B., Sinow,C.O., Sauer,A.J. and Corman,B.H.P.
  TITLE     Assembly and regulation of the mammalian mRNA processing body
  JOURNAL   PLoS One 18 (3), e0282496 (2023)
   PUBMED   36877681
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1401)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 1401)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 1401)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1401)
  AUTHORS   Bloch,D.B., Gulick,T., Bloch,K.D. and Yang,W.H.
  TITLE     Processing body autoantibodies reconsidered
  JOURNAL   RNA 12 (5), 707-709 (2006)
   PUBMED   16641511
REFERENCE   7  (residues 1 to 1401)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 1401)
  AUTHORS   Yu,J.H., Yang,W.H., Gulick,T., Bloch,K.D. and Bloch,D.B.
  TITLE     Ge-1 is a central component of the mammalian cytoplasmic mRNA
            processing body
  JOURNAL   RNA 11 (12), 1795-1802 (2005)
   PUBMED   16314453
REFERENCE   9  (residues 1 to 1401)
  AUTHORS   Garcia-Lozano,J.R., Gonzalez-Escribano,M.F., Wichmann,I. and
            Nunez-Roldan,A.
  TITLE     Cytoplasmic detection of a novel protein containing a nuclear
            localization sequence by human autoantibodies
  JOURNAL   Clin Exp Immunol 107 (3), 501-506 (1997)
   PUBMED   9067524
REFERENCE   10 (residues 1 to 1401)
  AUTHORS   Bloch,D.B., Rabkina,D., Quertermous,T. and Bloch,K.D.
  TITLE     The immunoreactive region in a novel autoantigen contains a nuclear
            localization sequence
  JOURNAL   Clin Immunol Immunopathol 72 (3), 380-389 (1994)
   PUBMED   7520377
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC403765.1 and BC064567.1.
            
            On Mar 30, 2004 this sequence version replaced NP_055144.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043616.1, SRR1803615.133095.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358933.10/ ENSP00000351811.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1401
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..1401
                     /product="enhancer of mRNA-decapping protein 4 isoform 2"
                     /note="enhancer of mRNA-decapping protein 4; autoantigen
                     Ge-1; autoantigen RCD-8; human enhancer of decapping large
                     subunit"
                     /calculated_mol_wt=151531
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          23..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          114..441
                     /region_name="Ge1_WD40"
                     /note="WD40 region of Ge1, enhancer of mRNA-decapping
                     protein; pfam16529"
                     /db_xref="CDD:465162"
     Region          121..164
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          167..206
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          180..219
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          217..269
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          232..288
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          287..326
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          300..341
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          335..385
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          348..393
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          389..426
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          432..475
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          <525..982
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          545..565
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            565
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            583
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            585
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          603..628
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          662..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            676
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            693
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          717..741
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            723
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            729
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            741
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          778..808
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            844
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          868..946
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            879
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UJB9; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            892
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Region          913..934
                     /region_name="Sufficient for nuclear localization"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            967
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     Site            1380
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q6P2E9.1)"
     CDS             1..1401
                     /gene="EDC4"
                     /gene_synonym="Ge-1; GE1; HEDL5; HEDLS; RCD-8; RCD8"
                     /coded_by="NM_014329.5:211..4416"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10849.1"
                     /db_xref="GeneID:23644"
                     /db_xref="HGNC:HGNC:17157"
                     /db_xref="MIM:606030"
ORIGIN      
        1 mascasidie datqhlrdil kldrpaggps aesprpssay ngdlngllvp dplcsgdsts
       61 anktglrtmp pinlqekqvi clsgddsstc igilakevei vassdssiss kargsnkvki
      121 qpvakydweq kyyygnliav snsflayair aanngsamvr visvstsert llkgftgsva
      181 dlafahlnsp qlacldeagn lfvwrlalvn gkiqeeilvh irqpegtpln hfrriiwcpf
      241 ipeesedcce essptvallh edraevwdld mlrsshstwp vdvsqikqgf ivvkghstcl
      301 segalspdgt vlatashdgy vkfwqiyieg qdeprclhew kphdgrplsc llfcdnhkkq
      361 dpdvpfwrfl itgadqnrel kmwctvswtc lqtirfspdi fssvsvppsl kvcldlsaey
      421 lilsdvqrkv lyvmellqnq eeghacfssi sefllthpvl sfgiqvvsrc rlrhtevlpa
      481 eeendslgad gthgagames aagvliklfc vhtkalqdvq irfqpqlnpd vvaplpthta
      541 hedftfgesr pelgseglgs aahgsqpdlr rivelpapad flslssetkp klmtpdafmt
      601 psaslqqita spsssssgss sssssssssl tavsamssts avdpsltrpp eeltlspklq
      661 ldgsltmsss gslqasprgl lpgllpapad kltpkgpgqv ptatsalsle lqeveplglp
      721 qaspsrtrsp dvissastal sqdipeiase alsrgfgssa peglepdsma saasalhlls
      781 prprpgpelg pqlgldggpg dgdrhntpsl leaaltqeas tpdsqvwpta pditretcst
      841 laesprnglq ekhkslafhr ppyhllqqrd sqdasaeqsd hddevaslas asggfgtkvp
      901 aprlpakdwk tkgsprtspk lkrkskkddg daamgsrlte hqvaeppedw paliwqqqre
      961 laelrhsqee llqrlctqle glqstvtghv eraletrheq eqrrlerala egqqrggqlq
     1021 eqltqqlsqa lssavagrle rsirdeikkt vppcvsrsle pmagqlsnsv atkltavegs
     1081 mkeniskllk sknltdaiar aaadtlqgpm qaayreafqs vvlpafeksc qamfqqinds
     1141 frlgtqeylq qleshmksrk areqearepv laqlrglvst lqsateqmaa tvagsvraev
     1201 qhqlhvavgs lqesilaqvq rivkgevsva lkeqqaavts simqamrsaa gtpvpsahld
     1261 cqaqqahilq llqqghlnqa fqqaltaadl nlvlyvcetv dpaqvfgqpp cplsqpvlls
     1321 liqqlasdlg trtdlklsyl eeavmhldhs dpitrdhmgs vmaqvrqklf qflqaephns
     1381 lgkaarrlsl mlhglvtpsl p
//
LOCUS       NP_005493               2261 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid-transporting ATPase ABCA1 [Homo sapiens].
ACCESSION   NP_005493
VERSION     NP_005493.2
DBSOURCE    REFSEQ: accession NM_005502.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2261)
  AUTHORS   Boh,J., Suligoj,E., Mankoc Ramus,S. and Petrovic,D.
  TITLE     The ABCA1 gene polymorphisms rs1800977 and rs2230806 are
            differentially associated with the risk for myocardial infarction
            in Slovenian subjects with type 2 diabetes mellitus
  JOURNAL   Gene 927, 148705 (2024)
   PUBMED   38901534
  REMARK    GeneRIF: The ABCA1 gene polymorphisms rs1800977 and rs2230806 are
            differentially associated with the risk for myocardial infarction
            in Slovenian subjects with type 2 diabetes mellitus.
REFERENCE   2  (residues 1 to 2261)
  AUTHORS   Torres-Paz,Y.E., Gamboa,R., Fuentevilla-Alvarez,G.,
            Cardoso-Saldana,G., Martinez-Alvarado,R., Soto,M.E. and
            Huesca-Gomez,C.
  TITLE     Involvement of Expression of miR33-5p and ABCA1 in Human Peripheral
            Blood Mononuclear Cells in Coronary Artery Disease
  JOURNAL   Int J Mol Sci 25 (16), 8605 (2024)
   PUBMED   39201292
  REMARK    GeneRIF: Involvement of Expression of miR33-5p and ABCA1 in Human
            Peripheral Blood Mononuclear Cells in Coronary Artery Disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2261)
  AUTHORS   Majeed,A., Baig,Z.A. and Rashid,A.
  TITLE     Identification and Molecular Simulation of Genetic Variants in
            ABCA1 Gene Associated with Susceptibility to Dyslipidemia in Type 2
            Diabetes
  JOURNAL   Int J Mol Sci 25 (12), 6796 (2024)
   PUBMED   38928502
  REMARK    GeneRIF: Identification and Molecular Simulation of Genetic
            Variants in ABCA1 Gene Associated with Susceptibility to
            Dyslipidemia in Type 2 Diabetes.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2261)
  AUTHORS   Kumari,A., Saini,V. and Kumar,V.
  TITLE     Decreased mRNA expression of NR1H3 and ABCA1 in pulmonary
            tuberculosis patients from population of Punjab, India
  JOURNAL   Mol Biol Rep 51 (1), 657 (2024)
   PUBMED   38740636
  REMARK    GeneRIF: Decreased mRNA expression of NR1H3 and ABCA1 in pulmonary
            tuberculosis patients from population of Punjab, India.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2261)
  AUTHORS   Zhuo,S., Song,S., Wang,C., Wang,Z., Zhang,M., Lin,D. and Chen,K.
  TITLE     Inflammatory corpuscle AIM2 facilitates macrophage foam cell
            formation by inhibiting cholesterol efflux protein ABCA1
  JOURNAL   Sci Rep 14 (1), 10782 (2024)
   PUBMED   38734775
  REMARK    GeneRIF: Inflammatory corpuscle AIM2 facilitates macrophage foam
            cell formation by inhibiting cholesterol efflux protein ABCA1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2261)
  AUTHORS   Rust,S., Walter,M., Funke,H., von Eckardstein,A., Cullen,P.,
            Kroes,H.Y., Hordijk,R., Geisel,J., Kastelein,J., Molhuizen,H.O.,
            Schreiner,M., Mischke,A., Hahmann,H.W. and Assmann,G.
  TITLE     Assignment of Tangier disease to chromosome 9q31 by a graphical
            linkage exclusion strategy
  JOURNAL   Nat Genet 20 (1), 96-98 (1998)
   PUBMED   9731541
  REMARK    Erratum:[Nat Genet 1998 Nov;20(3):312]
REFERENCE   7  (residues 1 to 2261)
  AUTHORS   Becq,F., Hamon,Y., Bajetto,A., Gola,M., Verrier,B. and Chimini,G.
  TITLE     ABC1, an ATP binding cassette transporter required for phagocytosis
            of apoptotic cells, generates a regulated anion flux after
            expression in Xenopus laevis oocytes
  JOURNAL   J Biol Chem 272 (5), 2695-2699 (1997)
   PUBMED   9006906
REFERENCE   8  (residues 1 to 2261)
  AUTHORS   Allikmets,R., Gerrard,B., Glavac,D., Ravnik-Glavac,M.,
            Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Modi,W. and Dean,M.
  TITLE     Characterization and mapping of three new mammalian ATP-binding
            transporter genes from an EST database
  JOURNAL   Mamm Genome 6 (2), 114-117 (1995)
   PUBMED   7766993
REFERENCE   9  (residues 1 to 2261)
  AUTHORS   Luciani,M.F., Denizot,F., Savary,S., Mattei,M.G. and Chimini,G.
  TITLE     Cloning of two novel ABC transporters mapping on human chromosome 9
  JOURNAL   Genomics 21 (1), 150-159 (1994)
   PUBMED   8088782
REFERENCE   10 (residues 1 to 2261)
  AUTHORS   Burnett,J.R., Hooper,A.J., McCormick,S.P.A. and Hegele,R.A.
  TITLE     Tangier Disease
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31751110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX955241.1, AB445477.1,
            BC146856.1, AL359846.11 and BU753834.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 21, 2002 this sequence version replaced NP_005493.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intracellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the ABC1 subfamily. Members of
            the ABC1 subfamily comprise the only major ABC subfamily found
            exclusively in multicellular eukaryotes. With cholesterol as its
            substrate, this protein functions as a cholesteral efflux pump in
            the cellular lipid removal pathway. Mutations in both alleles of
            this gene cause Tangier disease and familial high-density
            lipoprotein (HDL) deficiency. [provided by RefSeq, Sep 2019].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF285167.1, BC146856.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374736.8/ ENSP00000363868.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..2261
                     /product="phospholipid-transporting ATPase ABCA1"
                     /EC_number="7.6.2.1"
                     /note="cholesterol efflux regulatory protein; ATP-binding
                     cassette sub-family A member 1; ATP-binding cassette
                     transporter A1; membrane-bound; ATP-binding cassette,
                     sub-family A (ABC1), member 1"
                     /calculated_mol_wt=254172
     Region          6..2236
                     /region_name="rim_protein"
                     /note="retinal-specific rim ABC transporter; TIGR01257"
                     /db_xref="CDD:130324"
     Site            14
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            22..42
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Region          69..80
                     /region_name="Annulus domain 1.
                     /evidence=ECO:0000305|PubMed:35974019"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            151
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            161
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            196
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            244
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            292
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            337
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            349
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Region          368..379
                     /region_name="Annulus domain 2.
                     /evidence=ECO:0000305|PubMed:35974019"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            400
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            478
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            489
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            521
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Region          564..594
                     /region_name="Gateway domain.
                     /evidence=ECO:0000305|PubMed:35974019"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            640..660
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            683..703
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            716..736
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            745..765
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            777..797
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            820
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            827..847
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1041..1057
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1042
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:12196520; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Region          1283..1312
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1294
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1296
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41233; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1351..1371
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1453
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1504
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1637
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            1657..1677
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1703..1723
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1735..1755
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1768..1788
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1802..1822
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            1852..1872
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95477.3)"
     Site            2044
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            2054
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000269|PubMed:12196520; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     Site            2238
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O95477.3)"
     CDS             1..2261
                     /gene="ABCA1"
                     /gene_synonym="ABC-1; ABC1; CERP; HDLCQTL13; HDLDT1;
                     HPALP1; TGD"
                     /coded_by="NM_005502.4:314..7099"
                     /db_xref="CCDS:CCDS6762.1"
                     /db_xref="GeneID:19"
                     /db_xref="HGNC:HGNC:29"
                     /db_xref="MIM:600046"
ORIGIN      
        1 macwpqlrll lwknltfrrr qtcqllleva wplfiflili svrlsyppye qhechfpnka
       61 mpsagtlpwv qgiicnannp cfryptpgea pgvvgnfnks ivarlfsdar rlllysqkdt
      121 smkdmrkvlr tlqqikksss nlklqdflvd netfsgflyh nlslpkstvd kmlradvilh
      181 kvflqgyqlh ltslcngsks eemiqlgdqe vselcglpre klaaaervlr snmdilkpil
      241 rtlnstspfp skelaeatkt llhslgtlaq elfsmrswsd mrqevmfltn vnssssstqi
      301 yqavsrivcg hpeggglkik slnwyednny kalfggngte edaetfydns ttpycndlmk
      361 nlessplsri iwkalkpllv gkilytpdtp atrqvmaevn ktfqelavfh dlegmweels
      421 pkiwtfmens qemdlvrmll dsrdndhfwe qqldgldwta qdivaflakh pedvqssngs
      481 vytwreafne tnqairtisr fmecvnlnkl epiatevwli nksmellder kfwagivftg
      541 itpgsielph hvkykirmdi dnvertnkik dgywdpgpra dpfedmryvw ggfaylqdvv
      601 eqaiirvltg tekktgvymq qmpypcyvdd iflrvmsrsm plfmtlawiy svaviikgiv
      661 yekearlket mrimgldnsi lwfswfissl ipllvsagll vvilklgnll pysdpsvvfv
      721 flsvfavvti lqcflistlf sranlaaacg giiyftlylp yvlcvawqdy vgftlkifas
      781 llspvafgfg ceyfalfeeq gigvqwdnlf espveedgfn lttsvsmmlf dtflygvmtw
      841 yieavfpgqy giprpwyfpc tksywfgees dekshpgsnq kriseicmee epthlklgvs
      901 iqnlvkvyrd gmkvavdgla lnfyegqits flghngagkt ttmsiltglf pptsgtayil
      961 gkdirsemst irqnlgvcpq hnvlfdmltv eehiwfyarl kglsekhvka emeqmaldvg
     1021 lpssklkskt sqlsggmqrk lsvalafvgg skvvildept agvdpysrrg iwelllkyrq
     1081 grtiilsthh mdeadvlgdr iaiishgklc cvgsslflkn qlgtgyyltl vkkdvessls
     1141 scrnssstvs ylkkedsvsq sssdaglgsd hesdtltidv saisnlirkh vsearlvedi
     1201 gheltyvlpy eaakegafve lfheiddrls dlgissygis ettleeiflk vaeesgvdae
     1261 tsdgtlparr nrrafgdkqs clrpftedda adpndsdidp esretdllsg mdgkgsyqvk
     1321 gwkltqqqfv allwkrllia rrsrkgffaq ivlpavfvci alvfslivpp fgkypslelq
     1381 pwmyneqytf vsndapedtg tlellnaltk dpgfgtrcme gnpipdtpcq ageeewttap
     1441 vpqtimdlfq ngnwtmqnps pacqcssdki kkmlpvcppg agglpppqrk qntadilqdl
     1501 tgrnisdylv ktyvqiiaks lknkiwvnef ryggfslgvs ntqalppsqe vndaikqmkk
     1561 hlklakdssa drflnslgrf mtgldtknnv kvwfnnkgwh aissflnvin nailranlqk
     1621 genpshygit afnhplnltk qqlsevalmt tsvdvlvsic vifamsfvpa sfvvfliqer
     1681 vskakhlqfi sgvkpviywl snfvwdmcny vvpatlviii ficfqqksyv sstnlpvlal
     1741 llllygwsit plmypasfvf kipstayvvl tsvnlfigin gsvatfvlel ftdnklnnin
     1801 dilksvflif phfclgrgli dmvknqamad alerfgenrf vsplswdlvg rnlfamaveg
     1861 vvfflitvli qyrffirprp vnaklsplnd ededvrrerq rildgggqnd ileikeltki
     1921 yrrkrkpavd ricvgippge cfgllgvnga gksstfkmlt gdttvtrgda flnknsilsn
     1981 ihevhqnmgy cpqfdaitel ltgrehveff allrgvpeke vgkvgewair klglvkygek
     2041 yagnysggnk rklstamali ggppvvflde pttgmdpkar rflwncalsv vkegrsvvlt
     2101 shsmeeceal ctrmaimvng rfrclgsvqh lknrfgdgyt ivvriagsnp dlkpvqdffg
     2161 lafpgsvlke khrnmlqyql psslsslari fsilsqskkr lhiedysvsq ttldqvfvnf
     2221 akdqsdddhl kdlslhknqt vvdvavltsf lqdekvkesy v
//
LOCUS       NP_001353506             888 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 13 [Homo
            sapiens].
ACCESSION   NP_001353506 XP_005245779
VERSION     NP_001353506.1
DBSOURCE    REFSEQ: accession NM_001366577.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_005245779.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.119023.1,
                                           SRR1660807.24938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..888
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 13"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=100132
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <121..209
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          <590..>724
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..888
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366577.1:26..2692"
                     /note="isoform 13 is encoded by transcript variant 17"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrtksrsp
      181 spapekkekt pelpepsvkv kepsvqeats tsdilkvpkp epipepkeps peknskkeke
      241 kektrprsrs rsksrsrtrs rspshtrprr rhrsrsrsys prrrpsprrr psprrrtppr
      301 rmpppprhrr srspvrrrrr ssaslsgsss sssssrsrsp pkkppkrtss pprktrrlsp
      361 saspprrrhr psppatpppk trhsptpqqs nrtrksrvsv spgrtsgkvt khkgtekres
      421 pspapkprkv elseseedkg gkmaaadsvq qrrqyrrqnq qsssdsgsss ssederpkrs
      481 hvkngevgrr rrhspsrsas psprkrqket sprmqmgkrw qspvtksgrr rrspsppptr
      541 rrrspspapp prrrrtptpp prrrtpsppp rrrspsprry sppiqrrysp spppkrrtas
      601 pppppkrras pspppkrrvs hspppkqrss pvtkrrspsl sskhrkgssp srstrearsp
      661 qpnkrhspsp rprapqtsss pppvrrgass spqrrqspsp strpirrvsr tpepkkikka
      721 aspspqsvrr vsssrsvsgs pepaakkppa ppspvqsqsp stnwspavpv kkaksptpsp
      781 spprnsdqeg ggkkkkkkkd kkhkkdkkhk khkkhkkeka vaaaaaaavt paaiaaattt
      841 laqeepvaap epkketesea ednlddlekh lrekalrsmr kaqvspqs
//
LOCUS       NP_057116                364 aa            linear   PRI 20-NOV-2025
DEFINITION  palmitoyltransferase ZDHHC9 [Homo sapiens].
ACCESSION   NP_057116
VERSION     NP_057116.2
DBSOURCE    REFSEQ: accession NM_016032.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 364)
  AUTHORS   Du,G., Healy,L.B., David,L., Walker,C., El-Baba,T.J.,
            Lutomski,C.A., Goh,B., Gu,B., Pi,X., Devant,P., Fontana,P.,
            Dong,Y., Ma,X., Miao,R., Balasubramanian,A., Puthenveetil,R.,
            Banerjee,A., Luo,H.R., Kagan,J.C., Oh,S.F., Robinson,C.V.,
            Lieberman,J. and Wu,H.
  TITLE     ROS-dependent S-palmitoylation activates cleaved and intact
            gasdermin D
  JOURNAL   Nature 630 (8016), 437-446 (2024)
   PUBMED   38599239
REFERENCE   2  (residues 1 to 364)
  AUTHORS   Balasubramanian,A., Hsu,A.Y., Ghimire,L., Tahir,M., Devant,P.,
            Fontana,P., Du,G., Liu,X., Fabin,D., Kambara,H., Xie,X., Liu,F.,
            Hasegawa,T., Xu,R., Yu,H., Chen,M., Kolakowski,S., Trauger,S.,
            Larsen,M.R., Wei,W., Wu,H., Kagan,J.C., Lieberman,J. and Luo,H.R.
  TITLE     The palmitoylation of gasdermin D directs its membrane
            translocation and pore formation during pyroptosis
  JOURNAL   Sci Immunol 9 (94), eadn1452 (2024)
   PUBMED   38530158
REFERENCE   3  (residues 1 to 364)
  AUTHORS   Yang,A., Liu,S., Zhang,Y., Chen,J., Fan,Y., Wang,F., Zou,Y.,
            Feng,S., Wu,J. and Hu,Q.
  TITLE     Regulation of RAS palmitoyltransferases by accessory proteins and
            palmitoylation
  JOURNAL   Nat Struct Mol Biol 31 (3), 436-446 (2024)
   PUBMED   38182928
REFERENCE   4  (residues 1 to 364)
  AUTHORS   Fan,Y., Gao,Y., Nie,L., Hou,T., Dan,W., Wang,Z., Liu,T., Wei,Y.,
            Wang,Y., Liu,B., Que,T., Lei,Y., Zeng,J., Ma,J., Wei,W. and Li,L.
  TITLE     Targeting LYPLAL1-mediated cGAS depalmitoylation enhances the
            response to anti-tumor immunotherapy
  JOURNAL   Mol Cell 83 (19), 3520-3532 (2023)
   PUBMED   37802025
REFERENCE   5  (residues 1 to 364)
  AUTHORS   Raymond,F.L., Tarpey,P.S., Edkins,S., Tofts,C., O'Meara,S.,
            Teague,J., Butler,A., Stevens,C., Barthorpe,S., Buck,G., Cole,J.,
            Dicks,E., Gray,K., Halliday,K., Hills,K., Hinton,J., Jones,D.,
            Menzies,A., Perry,J., Raine,K., Shepherd,R., Small,A., Varian,J.,
            Widaa,S., Mallya,U., Moon,J., Luo,Y., Shaw,M., Boyle,J., Kerr,B.,
            Turner,G., Quarrell,O., Cole,T., Easton,D.F., Wooster,R.,
            Bobrow,M., Schwartz,C.E., Gecz,J., Stratton,M.R. and Futreal,P.A.
  TITLE     Mutations in ZDHHC9, which encodes a palmitoyltransferase of NRAS
            and HRAS, cause X-linked mental retardation associated with a
            Marfanoid habitus
  JOURNAL   Am J Hum Genet 80 (5), 982-987 (2007)
   PUBMED   17436253
REFERENCE   6  (residues 1 to 364)
  AUTHORS   Omura,T., Kaneko,M., Okuma,Y., Orba,Y., Nagashima,K., Takahashi,R.,
            Fujitani,N., Matsumura,S., Hata,A., Kubota,K., Murahashi,K.,
            Uehara,T. and Nomura,Y.
  TITLE     A ubiquitin ligase HRD1 promotes the degradation of Pael receptor,
            a substrate of Parkin
  JOURNAL   J Neurochem 99 (6), 1456-1469 (2006)
   PUBMED   17059562
REFERENCE   7  (residues 1 to 364)
  AUTHORS   Ohno,Y., Kihara,A., Sano,T. and Igarashi,Y.
  TITLE     Intracellular localization and tissue-specific distribution of
            human and yeast DHHC cysteine-rich domain-containing proteins
  JOURNAL   Biochim Biophys Acta 1761 (4), 474-483 (2006)
   PUBMED   16647879
REFERENCE   8  (residues 1 to 364)
  AUTHORS   Zhu,C., Anderson,A.C., Schubart,A., Xiong,H., Imitola,J.,
            Khoury,S.J., Zheng,X.X., Strom,T.B. and Kuchroo,V.K.
  TITLE     The Tim-3 ligand galectin-9 negatively regulates T helper type 1
            immunity
  JOURNAL   Nat Immunol 6 (12), 1245-1252 (2005)
   PUBMED   16286920
REFERENCE   9  (residues 1 to 364)
  AUTHORS   Swarthout,J.T., Lobo,S., Farh,L., Croke,M.R., Greentree,W.K.,
            Deschenes,R.J. and Linder,M.E.
  TITLE     DHHC9 and GCP16 constitute a human protein fatty acyltransferase
            with specificity for H- and N-Ras
  JOURNAL   J Biol Chem 280 (35), 31141-31148 (2005)
   PUBMED   16000296
  REMARK    GeneRIF: Data show that H- and N-Ras are palmitoylated by a human
            protein palmitoyltransferase encoded by the ZDHHC9 and GCP16 genes.
REFERENCE   10 (residues 1 to 364)
  AUTHORS   Kaneko,M., Ishiguro,M., Niinuma,Y., Uesugi,M. and Nomura,Y.
  TITLE     Human HRD1 protects against ER stress-induced apoptosis through
            ER-associated degradation
  JOURNAL   FEBS Lett 532 (1-2), 147-152 (2002)
   PUBMED   12459480
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA493628.1, BC003128.1 and
            AL359542.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 16, 2004 this sequence version replaced NP_057116.1.
            
            Summary: This gene encodes an integral membrane protein that is a
            member of the zinc finger DHHC domain-containing protein family.
            The encoded protein forms a complex with golgin subfamily A member
            7 and functions as a palmitoyltransferase. This protein
            specifically palmitoylates HRAS and NRAS. Mutations in this gene
            are associated with X-linked cognitive disability. Alternate
            splicing results in multiple transcript variants that encode the
            same protein.[provided by RefSeq, May 2010].
            
            Transcript Variant: This variant (1) is the longer transcript and
            both variants 1 and 2 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853562.33890.1,
                                           SRR11853563.35554.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357166.11/ ENSP00000349689.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..364
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26.1"
     Protein         1..364
                     /product="palmitoyltransferase ZDHHC9"
                     /EC_number="2.3.1.225"
                     /note="Asp-His-His-Cys domain containing protein 9; zinc
                     finger, DHHC domain containing 10; antigen MMSA-1; zinc
                     finger protein 379; zinc finger protein 380; zinc finger
                     DHHC-type containing 9; zinc finger DHHC-type
                     palmitoyltransferase 9"
                     /calculated_mol_wt=40785
     Site            36..56
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y397.2)"
     Site            64..84
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y397.2)"
     Region          138..261
                     /region_name="DHHC"
                     /note="DHHC palmitoyltransferase; pfam01529"
                     /db_xref="CDD:396215"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y397.2)"
     Site            229..249
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y397.2)"
     Region          303..364
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y397.2)"
     CDS             1..364
                     /gene="ZDHHC9"
                     /gene_synonym="CGI89; CXorf11; DHHC9; MMSA1; MRXSR; MRXSZ;
                     ZDHHC10; ZNF379; ZNF380"
                     /coded_by="NM_016032.4:395..1489"
                     /db_xref="CCDS:CCDS35395.1"
                     /db_xref="GeneID:51114"
                     /db_xref="HGNC:HGNC:18475"
                     /db_xref="MIM:300646"
ORIGIN      
        1 msvmvvrkkv trkweklpgr ntfccdgrvm marqkgifyl tlflilgtct lffafecryl
       61 avqlspaipv faamlflfsm atllrtsfsd pgvipralpd eaafiemeie atngavpqgq
      121 rpppriknfq innqivklky cytckifrpp rashcsicdn cverfdhhcp wvgncvgkrn
      181 yryfylfils lslltiyvfa fnivyvalks lkigfletlk etpgtvlevl icfftlwsvv
      241 gltgfhtflv alnqttnedi kgswtgknrv qnpyshgniv knccevlcgp lppsvldrrg
      301 ilpleesgsr ppstqetsss llpqspapte hlnsnemped sstpeemppp eppeppqeaa
      361 eaek
//
LOCUS       NP_001300927             450 aa            linear   PRI 20-NOV-2025
DEFINITION  beclin-1 isoform a [Homo sapiens].
ACCESSION   NP_001300927 XP_005257815
VERSION     NP_001300927.1
DBSOURCE    REFSEQ: accession NM_001313998.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Chen,M., Nguyen,T.N., Ren,X., Khuu,G., Cook,A.S.I., Zhao,Y.,
            Yildiz,A., Lazarou,M. and Hurley,J.H.
  TITLE     Structure and activation of the human autophagy-initiating
            ULK1C:PI3KC3-C1 supercomplex
  JOURNAL   Nat Struct Mol Biol 32 (9), 1596-1605 (2025)
   PUBMED   40442316
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Baek,S., Chang,J.W., Yoo,S.M., Choo,J., Jung,S., Nah,J. and
            Jung,Y.K.
  TITLE     TMEM9 activates Rab9-dependent alternative autophagy through
            interaction with Beclin1
  JOURNAL   Cell Mol Life Sci 81 (1), 322 (2024)
   PUBMED   39078420
  REMARK    GeneRIF: TMEM9 activates Rab9-dependent alternative autophagy
            through interaction with Beclin1.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Oberstein,A., Jeffrey,P.D. and Shi,Y.
  TITLE     Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1
            is a novel BH3-only protein
  JOURNAL   J Biol Chem 282 (17), 13123-13132 (2007)
   PUBMED   17337444
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Furuya,N., Yu,J., Byfield,M., Pattingre,S. and Levine,B.
  TITLE     The evolutionarily conserved domain of Beclin 1 is required for
            Vps34 binding, autophagy and tumor suppressor function
  JOURNAL   Autophagy 1 (1), 46-52 (2005)
   PUBMED   16874027
  REMARK    GeneRIF: Evolutionarily conserved domain of Beclin 1 is essential
            for Vps34 interaction, autophagy function, and tumor suppressor
            function.
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Aita,V.M., Liang,X.H., Murty,V.V., Pincus,D.L., Yu,W., Cayanis,E.,
            Kalachikov,S., Gilliam,T.C. and Levine,B.
  TITLE     Cloning and genomic organization of beclin 1, a candidate tumor
            suppressor gene on chromosome 17q21
  JOURNAL   Genomics 59 (1), 59-65 (1999)
   PUBMED   10395800
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Liang,X.H., Kleeman,L.K., Jiang,H.H., Gordon,G., Goldman,J.E.,
            Berry,G., Herman,B. and Levine,B.
  TITLE     Protection against fatal Sindbis virus encephalitis by beclin, a
            novel Bcl-2-interacting protein
  JOURNAL   J Virol 72 (11), 8586-8596 (1998)
   PUBMED   9765397
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Panaretou,C., Domin,J., Cockcroft,S. and Waterfield,M.D.
  TITLE     Characterization of p150, an adaptor protein for the human
            phosphatidylinositol (PtdIns) 3-kinase. Substrate presentation by
            phosphatidylinositol transfer protein to the p150.Ptdins 3-kinase
            complex
  JOURNAL   J Biol Chem 272 (4), 2477-2485 (1997)
   PUBMED   8999962
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Rommens,J.M., Durocher,F., McArthur,J., Tonin,P., LeBlanc,J.F.,
            Allen,T., Samson,C., Ferri,L., Narod,S., Morgan,K. et al.
  TITLE     Generation of a transcription map at the HSD17B locus centromeric
            to BRCA1 at 17q21
  JOURNAL   Genomics 28 (3), 530-542 (1995)
   PUBMED   7490091
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC354547.1, AK312651.1,
            AC016889.28 and BC010276.1.
            
            On Sep 22, 2015 this sequence version replaced XP_005257815.1.
            
            Summary: This gene encodes a protein that regulates autophagy, a
            catabolic process of degradation induced by starvation. The encoded
            protein is a component of the phosphatidylinositol-3-kinase (PI3K)
            complex which mediates vesicle-trafficking processes. This protein
            is thought to play a role in multiple cellular processes, including
            tumorigenesis, neurodegeneration and apoptosis. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2015].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.667136.1,
                                           SRR1660803.21025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000590099.6/ ENSP00000465364.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.31"
     Protein         1..450
                     /product="beclin-1 isoform a"
                     /note="beclin 1 (coiled-coil, moesin-like BCL2-interacting
                     protein); beclin1-gamma; beclin1-beta; ATG6 autophagy
                     related 6 homolog; coiled-coil myosin-like
                     BCL2-interacting protein; testis secretory sperm-binding
                     protein Li 215e; beclin 1, autophagy related"
                     /calculated_mol_wt=51765
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:31123703; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          48..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            93
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:23878393,
                     ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AMPK.
                     /evidence=ECO:0000269|PubMed:25891078; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     Region          105..129
                     /region_name="BH3"
                     /note="Beclin-1 BH3 domain, Bcl-2-interacting; pfam15285"
                     /db_xref="CDD:464614"
     Region          108..127
                     /region_name="BH3. /evidence=ECO:0000269|PubMed:17337444"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Region          112..159
                     /region_name="Interaction with BCL2 and BCL2L1 isoform
                     Bcl-X(L). /evidence=ECO:0000269|PubMed:17446862"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by DAPK1.
                     /evidence=ECO:0000269|PubMed:19180116; propagated from
                     UniProtKB/Swiss-Prot (Q14457.2)"
     mat_peptide     134..450
                     /product="Beclin-1-C 37 kDa.
                     /evidence=ECO:0000305|PubMed:21364619. /id=PRO_0000435036"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
                     /calculated_mol_wt=37303
     Region          135..261
                     /region_name="APG6_N"
                     /note="Apg6 coiled-coil region; pfam17675"
                     /db_xref="CDD:465452"
     mat_peptide     150..450
                     /product="Beclin-1-C 35 kDa.
                     /evidence=ECO:0000305|PubMed:21364619,
                     ECO:0000305|PubMed:26263979. /id=PRO_0000435037"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
                     /calculated_mol_wt=35476
     Region          245..450
                     /region_name="Evolutionary conserved domain (ECD).
                     /evidence=ECO:0000305|PubMed:28445460"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     Region          267..445
                     /region_name="APG6"
                     /note="Apg6 BARA domain; pfam04111"
                     /db_xref="CDD:461178"
     Region          425..450
                     /region_name="Required for membrane-association.
                     /evidence=ECO:0000269|PubMed:23878393"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14457.2)"
     CDS             1..450
                     /gene="BECN1"
                     /gene_synonym="ATG6; beclin1; VPS30"
                     /coded_by="NM_001313998.2:131..1483"
                     /note="isoform a is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11441.1"
                     /db_xref="GeneID:8678"
                     /db_xref="HGNC:HGNC:1034"
                     /db_xref="MIM:604378"
ORIGIN      
        1 megsktsnns tmqvsfvcqr csqplkldts fkildrvtiq eltaplltta qakpgetqee
       61 etnsgeepfi etprqdgvsr rfipparmms tesansftli geasdggtme nlsrrlkvtg
      121 dlfdimsgqt dvdhplceec tdtlldqldt qlnvtenecq nykrcleile qmneddseql
      181 qmelkelale eerliqeled veknrkivae nlekvqaeae rldqeeaqyq reysefkrqq
      241 lelddelksv enqmryaqtq ldklkktnvf natfhiwhsg qfgtinnfrl grlpsvpvew
      301 neinaawgqt vlllhalank mglkfqryrl vpygnhsyle sltdkskelp lycsgglrff
      361 wdnkfdhamv afldcvqqfk eevekgetrf clpyrmdvek gkiedtggsg gsysiktqfn
      421 seeqwtkalk fmltnlkwgl awvssqfynk
//
LOCUS       NP_001290377             916 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001290377 XP_005245776
VERSION     NP_001290377.1
DBSOURCE    REFSEQ: accession NM_001303448.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 916)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 916)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 916)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 916)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 916)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 916)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 916)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 916)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 916)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 916)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK302498.1, AF419855.1, AW958761.1, AA744578.1, CX782666.1 and
            BG178896.1.
            
            On Jan 4, 2015 this sequence version replaced XP_005245776.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.103050.1,
                                           SRR1803615.250029.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..916
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..916
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 1"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=103665
     Region          1..156
                     /region_name="Necessary for mRNA 3'-end cleavage and
                     cytoplasmic accumulation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          1..151
                     /region_name="Necessary for DNA and RNA-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          46..115
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Site            140
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            227
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            234
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            420
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            522
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            524
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            526
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            528
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            530
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            567
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            572
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            574
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            586
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            595
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            608
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            617
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Region          <618..>752
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            638
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            706
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            707
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            717
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            719
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            727
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            750
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            752
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            760
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            766
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            768
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            781
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            789
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            790
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q52KI8; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            793
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            803
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            807
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            809
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8IYB3.2)"
     Site            913
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IYB3.2)"
     CDS             1..916
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001303448.2:26..2776"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mdagffrgts aeqdnrfsnk qkkllkqlkf aeclekkvdm skvnlevikp witkrvteil
       61 gfeddvvief ifnqlevknp dskmmqinlt gflngknare fmgelwplll saqeniagip
      121 saflelkkee ikqrqieqek lasmkkqded kdkrdkeeke ssrekrersr sprrrksrsp
      181 sprrrsspvr rerkrshsrs prhrtksrsp spapekkekt pelpepsvkv kepsvqeats
      241 tsdilkvpkp epipepkeps peknskkeke kektrprsrs rsksrsrtrs rspshtrprr
      301 rhrsrsrsys prrrpsprrr psprrrtppr rmpppprhrr srspvrrrrr ssaslsgsss
      361 sssssrsrsp pkkppkrtss pprktrrlsp saspprrrhr psppatpppk trhsptpqqs
      421 nrtrksrvsv spgrtsvtkh kgtekresps papkprkvel seseedkggk maaadsvqqr
      481 rqyrrqnqqs ssdsgsssss ederpkrshv kngevgrrrr hspsrsasps prkrqketsp
      541 rmqmgkrwqs pvtksgrrrr spsppptrrr rspspapppr rrrtptpppr rrtpsppprr
      601 rspsprrysp piqrryspsp ppkrrtaspp pppkrrasps pppkrrvshs pppkqrsspv
      661 tkrrspslss khrkgsspsr strearspqp nkrhspsprp rapqtssspp pvrrgasssp
      721 qrrqspspst rpirrvsrtp epkkikkaas pspqsvrrvs ssrsvsgspe paakkppapp
      781 spvqsqspst nwspavpvkk aksptpspsp prnsdqeggg kkkkkkkdkk hkkdkkhkkh
      841 kkhkkekava aaaaaavtpa aiaaatttla qeepvaapep kketeseaed nlddlekhlr
      901 ekalrsmrka qvspqs
//
LOCUS       NP_000963                266 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein eL8 [Homo sapiens].
ACCESSION   NP_000963
VERSION     NP_000963.1
DBSOURCE    REFSEQ: accession NM_000972.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 266)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   2  (residues 1 to 266)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   3  (residues 1 to 266)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 266)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 266)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 266)
  AUTHORS   Burris,T.P., Nawaz,Z., Tsai,M.J. and O'Malley,B.W.
  TITLE     A nuclear hormone receptor-associated protein that inhibits
            transactivation by the thyroid hormone and retinoic acid receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (21), 9525-9529 (1995)
   PUBMED   7568167
REFERENCE   7  (residues 1 to 266)
  AUTHORS   Colombo,P., Yon,J. and Fried,M.
  TITLE     The organization and expression of the human L7a ribosomal protein
            gene
  JOURNAL   Biochim Biophys Acta 1129 (1), 93-95 (1991)
   PUBMED   1756182
REFERENCE   8  (residues 1 to 266)
  AUTHORS   Ben-Ishai,R., Scharf,R., Sharon,R. and Kapten,I.
  TITLE     A human cellular sequence implicated in trk oncogene activation is
            DNA damage inducible
  JOURNAL   Proc Natl Acad Sci U S A 87 (16), 6039-6043 (1990)
   PUBMED   1696715
REFERENCE   9  (residues 1 to 266)
  AUTHORS   Ziemiecki,A., Muller,R.G., Fu,X.C., Hynes,N.E. and Kozma,S.
  TITLE     Oncogenic activation of the human trk proto-oncogene by
            recombination with the ribosomal large subunit protein L7a
  JOURNAL   EMBO J 9 (1), 191-196 (1990)
   PUBMED   2403926
REFERENCE   10 (residues 1 to 266)
  AUTHORS   Kozma,S.C., Redmond,S.M., Fu,X.C., Saurer,S.M., Groner,B. and
            Hynes,N.E.
  TITLE     Activation of the receptor kinase domain of the trk oncogene by
            recombination with two different cellular sequences
  JOURNAL   EMBO J 7 (1), 147-154 (1988)
   PUBMED   2966065
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AL772161.10 and AL593848.15.
            
            Summary: Cytoplasmic ribosomes, organelles that catalyze protein
            synthesis, consist of a small 40S subunit and a large 60S subunit.
            Together these subunits are composed of 4 RNA species and
            approximately 80 structurally distinct proteins. This gene encodes
            a ribosomal protein that is a component of the 60S subunit. The
            protein belongs to the L7AE family of ribosomal proteins. It can
            interact with a subclass of nuclear hormone receptors, including
            thyroid hormone receptor, and inhibit their ability to
            transactivate by preventing their binding to their DNA response
            elements. This gene is included in the surfeit gene cluster, a
            group of very tightly linked genes that do not share sequence
            similarity. It is co-transcribed with the U24, U36a, U36b, and U36c
            small nucleolar RNA genes, which are located in its second, fifth,
            fourth, and sixth introns, respectively. This gene rearranges with
            the trk proto-oncogene to form the chimeric oncogene trk-2h, which
            encodes an oncoprotein consisting of the N terminus of ribosomal
            protein L7a fused to the receptor tyrosine kinase domain of trk. As
            is typical for genes encoding ribosomal proteins, there are
            multiple processed pseudogenes of this gene dispersed through the
            genome. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.152640.1,
                                           SRR5189655.22992.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323345.11/ ENSP00000361076.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..266
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
     Protein         1..266
                     /product="large ribosomal subunit protein eL8"
                     /note="surfeit 3; surfeit locus protein 3; PLA-X
                     polypeptide; 60S ribosomal protein L7a; thyroid hormone
                     receptor uncoupling protein"
                     /calculated_mol_wt=29865
     Region          16..266
                     /region_name="SNU13"
                     /note="U4/U6.U5 small nuclear ribonucleoprotein SNU13;
                     cl42391"
                     /db_xref="CDD:455736"
     Site            34
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     Site            order(141,144..145,148,163,165..166,168..169,172)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:411046"
     Site            217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P62424.2)"
     CDS             1..266
                     /gene="RPL7A"
                     /gene_synonym="eL8; L7A; SURF3; TRUP"
                     /coded_by="NM_000972.3:27..827"
                     /db_xref="CCDS:CCDS6965.1"
                     /db_xref="GeneID:6130"
                     /db_xref="HGNC:HGNC:10364"
                     /db_xref="MIM:185640"
ORIGIN      
        1 mpkgkkakgk kvapapavvk kqeakkvvnp lfekrpknfg igqdiqpkrd ltrfvkwpry
       61 irlqrqrail ykrlkvppai nqftqaldrq tatqllklah kyrpetkqek kqrllaraek
      121 kaagkgdvpt krppvlragv ntvttlvenk kaqlvviahd vdpielvvfl palcrkmgvp
      181 yciikgkarl grlvhrktct tvaftqvnse dkgalaklve airtnyndry deirrhwggn
      241 vlgpksvari aklekakake latklg
//
LOCUS       NP_115818               1562 aa            linear   PRI 20-NOV-2025
DEFINITION  neuralized-like protein 4 isoform 1 [Homo sapiens].
ACCESSION   NP_115818
VERSION     NP_115818.2
DBSOURCE    REFSEQ: accession NM_032442.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1562)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1562)
  AUTHORS   Cardamone,M.D., Gao,Y., Kwan,J., Hayashi,V., Sheeran,M., Xu,J.,
            English,J., Orofino,J., Emili,A. and Perissi,V.
  TITLE     Neuralized-like protein 4 (NEURL4) mediates ADP-ribosylation of
            mitochondrial proteins
  JOURNAL   J Cell Biol 221 (3) (2022)
   PUBMED   35157000
  REMARK    GeneRIF: Neuralized-like protein 4 (NEURL4) mediates
            ADP-ribosylation of mitochondrial proteins.
REFERENCE   3  (residues 1 to 1562)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 1562)
  AUTHORS   Loukil,A., Tormanen,K. and Sutterlin,C.
  TITLE     The daughter centriole controls ciliogenesis by regulating Neurl-4
            localization at the centrosome
  JOURNAL   J Cell Biol 216 (5), 1287-1300 (2017)
   PUBMED   28385950
  REMARK    GeneRIF: The data support a model in which the daughter centriole
            promotes ciliogenesis through Neurl-4-dependent regulation of CP110
            levels at the mother centriole.
REFERENCE   5  (residues 1 to 1562)
  AUTHORS   Li,J., Kim,S., Kobayashi,T., Liang,F.X., Korzeniewski,N.,
            Duensing,S. and Dynlacht,B.D.
  TITLE     Neurl4, a novel daughter centriole protein, prevents formation of
            ectopic microtubule organizing centres
  JOURNAL   EMBO Rep 13 (6), 547-553 (2012)
   PUBMED   22441691
  REMARK    GeneRIF: Neurl4 counteracts accumulation of CP110, thereby
            maintaining normal centriolar homeostasis and preventing formation
            of ectopic microtubular organizing centres
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1562)
  AUTHORS   Al-Hakim,A.K., Bashkurov,M., Gingras,A.C., Durocher,D. and
            Pelletier,L.
  TITLE     Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2
            as novel modulators of centrosome architecture
  JOURNAL   Mol Cell Proteomics 11 (6), M111.014233 (2012)
   PUBMED   22261722
  REMARK    GeneRIF: the NEURL4-HERC2 complex participates in the
            ubiquitin-dependent regulation of centrosome architecture
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026954.14, AB058690.1 and AL136870.1.
            
            On Oct 6, 2004 this sequence version replaced NP_115818.1.
            
            Summary: The protein encoded by this gene is predicted and it
            includes two isoforms resulting from two alternatively spliced
            transcript variants. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB058690.1, SRR1803613.12439.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000399464.7/ ENSP00000382390.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..1562
                     /product="neuralized-like protein 4 isoform 1"
                     /note="neuralized-like protein 4; neuralized homolog 4"
                     /calculated_mol_wt=166777
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          43..205
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          207..236
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          320..482
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Site            502
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          523..684
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          691..716
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          718..882
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Site            907
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          915..1084
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     Region          1086..1123
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JN8.2)"
     Region          1133..1292
                     /region_name="SPRY_NHR_like"
                     /note="SPRY domain in neuralized homology repeat; cd12887"
                     /db_xref="CDD:293945"
     CDS             1..1562
                     /gene="NEURL4"
                     /coded_by="NM_032442.3:24..4712"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42251.1"
                     /db_xref="GeneID:84461"
                     /db_xref="HGNC:HGNC:34410"
                     /db_xref="MIM:615865"
ORIGIN      
        1 maagsggsgg sgggpgpgpg ggggpsgsgs gpgsngglgs ggelhprtgr lvslsacgrt
       61 arrqqpgqef nhglvlsrep lrdgrvftvr idrkvnswsg sieigvtald psvldfpssa
      121 tglkggswvv sgcsvlrdgr svleeygqdl dqlgegdrvg vertvagelr lwvngrdcgv
      181 aatglpprvw avvdlygkct qitvlppepg fspptpiptp pleplapted salaeqgtsa
      241 deafmvspaq arpetfpnsl eshndfanme lsevvsntil saynggllnv nlssppageg
      301 lgssgaatsp iltsndallf hekcgtlikl snnnktaerr rpldefnngv vmtnrplrdn
      361 emfeiridkl vdkwsgsiei gvtthnpnsl eypatmtnlq sgtimmsgcg iltngkgtrr
      421 eycefsldel qegdhigltr ksnsalhffi ngidqgvatp ltppvvygvv dlygmavkvt
      481 ivhnnnhsdr lrrnnailra lspegalrra apaaqaeper llfhpncgqk aaithegrta
      541 lrphatddfn hgvvlssral rdgevfqvri dkmvdkwags ieigvtthnp aylqlpstmt
      601 nlrsgtwmmt gngvmhngtt ildeyghnld rlkagdtvgv vrredgtlhf fvngmtqgpa
      661 awnvppgvya vvdlygqaaq ativddveva pvpeplpegn nqvspsspss gaggsdlrfh
      721 qlhgsnavit nggrtalrhn crsefndaiv isnralrdge lfeiviqkmv drwsgsieag
      781 vtairpedle fpntmtdidy dtwmlsgtai mqdgntmrnn ygcdldalgt garigmmrta
      841 kgdlhyfing qdqgaacsgl ppgkevyavv dlygqcvqvs itnatgpmdn slatsntate
      901 ksfplhspva gvahrfhstc gknvtleedg travraagya hglvfstkel raeevfevkv
      961 eeldekwags lrlglttlap gemgpgaggg gpglppslpe lrtkttwmvs scevrrdgql
     1021 qrmnygrnle rlgvgsrvgv rrgaddtmhi lvdgedmgpa atgiaknvwa vldlygpvrg
     1081 vsivsstrle esegtqppsp ssdtgsegee ddegeehglg gqnevgiipt tleflenhgk
     1141 nillsngnrt atrvasynqg ivvinqplvp qllvqvridf lnrqwtsslv lgvitcaper
     1201 lnfpasacal kraawllrgr gvfhnglkic ekfgpnldtc pegtilglrl dssgglhlhv
     1261 ngvdqgvavp dvpqpchalv dlygqceqvt ivnpepgaas gksagtqgdm ekadmvdgik
     1321 esvcwgpppa asplksceyh alcsrfqell llpedyfmpp pkrslcyces crklrgdeah
     1381 rrrgepprey alpfgwcrfn lrvnprleag tltkkwhmay hgsnvaavrr vldrgelgag
     1441 tasilscrpl kgepgvgfee pgencappre eqpppvllsp slqyagaetl askvqfrdpk
     1501 sqrthqaqva fqvcvrpgsy tpgppsaalg eppdphfspa elewvtkekg atllcallvr
     1561 ve
//
LOCUS       NP_001276680             486 aa            linear   PRI 20-NOV-2025
DEFINITION  dihydrolipoyl dehydrogenase, mitochondrial isoform 3 [Homo
            sapiens].
ACCESSION   NP_001276680
VERSION     NP_001276680.1
DBSOURCE    REFSEQ: accession NM_001289751.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 486)
  AUTHORS   Lin,J., Wang,G., Cheng,S., Hu,Y., Li,H., Feng,W., Liu,X. and Xu,C.
  TITLE     Pan-Cancer Analysis of the Cuproptosis-Related Gene DLD
  JOURNAL   Mediators Inflamm 2023, 5533444 (2023)
   PUBMED   38077227
  REMARK    GeneRIF: Pan-Cancer Analysis of the Cuproptosis-Related Gene DLD.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 486)
  AUTHORS   Wongkittichote,P., Cuddapah,S.R., Master,S.R., Grange,D.K.,
            Dietzen,D., Roper,S.M. and Ganetzky,R.D.
  TITLE     Biochemical characterization of patients with dihydrolipoamide
            dehydrogenase deficiency
  JOURNAL   JIMD Rep 64 (5), 367-374 (2023)
   PUBMED   37701333
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 486)
  AUTHORS   Hevler,J.F., Albanese,P., Cabrera-Orefice,A., Potter,A.,
            Jankevics,A., Misic,J., Scheltema,R.A., Brandt,U., Arnold,S. and
            Heck,A.J.R.
  TITLE     MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
            dehydrogenase complex
  JOURNAL   Open Biol 13 (3), 220363 (2023)
   PUBMED   36854377
REFERENCE   4  (residues 1 to 486)
  AUTHORS   Babady,N.E., Pang,Y.P., Elpeleg,O. and Isaya,G.
  TITLE     Cryptic proteolytic activity of dihydrolipoamide dehydrogenase
  JOURNAL   Proc Natl Acad Sci U S A 104 (15), 6158-6163 (2007)
   PUBMED   17404228
  REMARK    GeneRIF: Certain DLD mutations can simultaneously induce the loss
            of a primary metabolic activity and the gain of a moonlighting
            proteolytic activity thus contributing to the metabolic derangement
            associated with DLD deficiency.
            GeneRIF: Human, mouse, and pig Dld has moonlighting function as a
            protease in addition to its canonical function as a a
            dehydrogenase.
REFERENCE   5  (residues 1 to 486)
  AUTHORS   Ganetzky,R., McCormick,E.M. and Falk,M.J.
  TITLE     Primary Pyruvate Dehydrogenase Complex Deficiency Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   34138529
REFERENCE   6  (residues 1 to 486)
  AUTHORS   Rahman,S., Thorburn,D.R. and Ball,M.
  TITLE     Nuclear Gene-Encoded Leigh Syndrome Spectrum Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26425749
REFERENCE   7  (residues 1 to 486)
  AUTHORS   Quinonez,S.C. and Thoene,J.G.
  TITLE     Dihydrolipoamide Dehydrogenase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25032271
REFERENCE   8  (residues 1 to 486)
  AUTHORS   Johanning,G.L., Morris,J.I., Madhusudhan,K.T., Samols,D. and
            Patel,M.S.
  TITLE     Characterization of the transcriptional regulatory region of the
            human dihydrolipoamide dehydrogenase gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (22), 10964-10968 (1992)
   PUBMED   1332063
REFERENCE   9  (residues 1 to 486)
  AUTHORS   Kume,A., Koyata,H., Sakakibara,T., Ishiguro,Y., Kure,S. and
            Hiraga,K.
  TITLE     The glycine cleavage system. Molecular cloning of the chicken and
            human glycine decarboxylase cDNAs and some characteristics involved
            in the deduced protein structures
  JOURNAL   J Biol Chem 266 (5), 3323-3329 (1991)
   PUBMED   1993704
REFERENCE   10 (residues 1 to 486)
  AUTHORS   Scherer,S.W., Otulakowski,G., Robinson,B.H. and Tsui,L.C.
  TITLE     Localization of the human dihydrolipoamide dehydrogenase gene (DLD)
            to 7q31----q32
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 176-177 (1991)
   PUBMED   2055113
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC354209.1, AK312346.1,
            BC018648.2 and AC005046.3.
            
            Summary: This gene encodes a member of the class-I pyridine
            nucleotide-disulfide oxidoreductase family. The encoded protein has
            been identified as a moonlighting protein based on its ability to
            perform mechanistically distinct functions. In homodimeric form,
            the encoded protein functions as a dehydrogenase and is found in
            several multi-enzyme complexes that regulate energy metabolism.
            However, as a monomer, this protein can function as a protease.
            Mutations in this gene have been identified in patients with
            E3-deficient maple syrup urine disease and lipoamide dehydrogenase
            deficiency. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2014].
            
            Transcript Variant: This variant (3) lacks an in-frame exon in the
            5' coding region, compared to variant 1. The encoded isoform (3) is
            shorter, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297508.1, SRR3476690.1045787.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            multifunctional gene product(s)    :: PMID: 17404228
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..486
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..486
                     /product="dihydrolipoyl dehydrogenase, mitochondrial
                     isoform 3"
                     /EC_number="1.8.1.4"
                     /note="E3 component of pyruvate dehydrogenase complex,
                     2-oxo-glutarate complex, branched chain keto acid
                     dehydrogenase complex; dihydrolipoyl dehydrogenase,
                     mitochondrial; glycine cleavage system protein L;
                     lipoamide reductase; lipoamide dehydrogenase; lipoyl
                     dehydrogenase; diaphorase; glycine cleavage system L
                     protein; epididymis secretory sperm binding protein;
                     pyruvate dehydrogenase complex subunit E3, 2-oxo-glutarate
                     complex, branched chain keto acid dehydrogenase complex,
                     glycine cleavage system protein L"
                     /calculated_mol_wt=51685
     Region          40..478
                     /region_name="Lpd"
                     /note="Dihydrolipoamide dehydrogenase (E3) component of
                     pyruvate/2-oxoglutarate dehydrogenase complex or
                     glutathione oxidoreductase [Energy production and
                     conversion]; COG1249"
                     /db_xref="CDD:440861"
     CDS             1..486
                     /gene="DLD"
                     /gene_synonym="DLDD; DLDH; E3; GCSL; LAD; OGDC-E3; PHE3"
                     /coded_by="NM_001289751.1:145..1605"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS78269.1"
                     /db_xref="GeneID:1738"
                     /db_xref="HGNC:HGNC:2898"
                     /db_xref="MIM:238331"
ORIGIN      
        1 mqswsrvycs lakrghfnri shglqglsav plrtyadqpi dadvtvigsg pggyvaaika
       61 aqlgfkalln nshyyhmahg kdfasrgiem sevrlnldkm meqkstavka ltggiahlfk
      121 qnkvvhvngy gkitgknqvt atkadggtqv idtkniliat gsevtpfpgi tidedtivss
      181 tgalslkkvp ekmvvigagv igvelgsvwq rlgadvtave flghvggvgi dmeisknfqr
      241 ilqkqgfkfk lntkvtgatk ksdgkidvsi eaasggkaev itcdvllvci grrpftknlg
      301 leelgieldp rgripvntrf qtkipniyai gdvvagpmla hkaedegiic vegmaggavh
      361 idyncvpsvi ythpevawvg kseeqlkeeg ieykvgkfpf aansraktna dtdgmvkilg
      421 qkstdrvlga hilgpgagem vneaalaley gascediarv chahptlsea freanlaasf
      481 gksinf
//
LOCUS       NP_001229411             165 aa            linear   PRI 20-NOV-2025
DEFINITION  probable RNA-binding protein EIF1AD [Homo sapiens].
ACCESSION   NP_001229411
VERSION     NP_001229411.1
DBSOURCE    REFSEQ: accession NM_001242482.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 165)
  AUTHORS   Yu,J. and Marintchev,A.
  TITLE     Comparative sequence and structure analysis of eIF1A and eIF1AD
  JOURNAL   BMC Struct Biol 18 (1), 11 (2018)
   PUBMED   30180896
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 165)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 165)
  AUTHORS   Smirnova,E.V., Rakitina,T.V., Bogatova,O.V., Ivanova,D.L.,
            Vorobyeva,E.E., Lipkin,A.V., Kostanyan,I.A. and Lipkin,V.M.
  TITLE     Novel protein haponin regulates cellular response to oxidative
            stress
  JOURNAL   Dokl Biochem Biophys 440, 225-227 (2011)
   PUBMED   22095125
  REMARK    GeneRIF: Novel protein haponin regulates cellular response to
            oxidative stress.
REFERENCE   8  (residues 1 to 165)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   9  (residues 1 to 165)
  AUTHORS   Vonarshenko,A.V., Radchenko,V.V., Gapon,M.V., Rodionov,I.L.,
            Babichenko,I.I., Kakuev,D.L., Artamonov,I.D., Garkovenko,A.V.,
            D'iachkova,L.G., Lipkin,V.M. and Kostanian,I.A.
  TITLE     [Identification and expression of haponin, a new protein from HL-60
            cells]
  JOURNAL   Bioorg Khim 33 (6), 653-656 (2007)
   PUBMED   18173130
REFERENCE   10 (residues 1 to 165)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP328412.1, BE791453.1, BU790195.1, BE669813.1 and AP006287.2.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 5' UTR, compared to variant 1, but encodes the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.14482.1,
                                           SRR1803611.244534.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2152719, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..165
                     /product="probable RNA-binding protein EIF1AD"
                     /note="eukaryotic translation initiation factor 1A
                     domain-containing protein"
                     /calculated_mol_wt=18922
     Region          6..12
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          25..102
                     /region_name="S1_eIF1AD_like"
                     /note="eukaryotic translation initiation factor 1A domain
                     containing protein (eIF1AD)-like, S1-like RNA-binding
                     domain. eIF1AD is also known as MGC11102 protein. Little
                     is known about the function of eIF1AD. S1-like RNA-binding
                     domains are found in a wide...; cd05792"
                     /db_xref="CDD:240218"
     Site            order(33..34,38,52..55,58,63)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:240218"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          56..65
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Region          112..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3THJ3; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            137
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5RKI6; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8N9N8.1)"
     CDS             1..165
                     /gene="EIF1AD"
                     /gene_synonym="haponin; OBELIX"
                     /coded_by="NM_001242482.2:341..838"
                     /db_xref="CCDS:CCDS8124.1"
                     /db_xref="GeneID:84285"
                     /db_xref="HGNC:HGNC:28147"
                     /db_xref="MIM:618473"
ORIGIN      
        1 msqatkrkhv vkevlgehiv psdqqqivrv lrtpgnnlhe vetaqgqrfl vsmpskyrkn
       61 iwikrgdfli vdpieegekv kaeisfvlck dhvrslqkeg fwpeafseva ekhnnrnrqt
      121 qpelpaepql sgeesssedd sdlfvntnrr qyheseeese eeeaa
//
LOCUS       NP_001229338             876 aa            linear   PRI 20-NOV-2025
DEFINITION  GRB2-associated and regulator of MAPK protein 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_001229338
VERSION     NP_001229338.1
DBSOURCE    REFSEQ: accession NM_001242409.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 876)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 876)
  AUTHORS   Nishino,T., Abe,T., Kaneko,M., Yokohira,M., Yamakawa,K., Imaida,K.
            and Konishi,H.
  TITLE     GAREM1 is involved in controlling body mass in mice and humans
  JOURNAL   Biochem Biophys Res Commun 628, 91-97 (2022)
   PUBMED   36084556
  REMARK    GeneRIF: GAREM1 is involved in controlling body mass in mice and
            humans.
REFERENCE   3  (residues 1 to 876)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   4  (residues 1 to 876)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 876)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 876)
  AUTHORS   Taniguchi,T., Tanaka,S., Ishii,A., Watanabe,M., Fujitani,N.,
            Sugeo,A., Gotoh,S., Ohta,T., Hiyoshi,M., Matsuzaki,H., Sakai,N. and
            Konishi,H.
  TITLE     A brain-specific Grb2-associated regulator of extracellular
            signal-regulated kinase (Erk)/mitogen-activated protein kinase
            (MAPK) (GAREM) subtype, GAREM2, contributes to neurite outgrowth of
            neuroblastoma cells by regulating Erk signaling
  JOURNAL   J Biol Chem 288 (41), 29934-29942 (2013)
   PUBMED   24003223
  REMARK    GeneRIF: Data indicate that a subtype of GAREM, GAREM2, is
            specifically expressed in the mouse, rat, and human brain.
REFERENCE   7  (residues 1 to 876)
  AUTHORS   Wang,J., Huo,K., Ma,L., Tang,L., Li,D., Huang,X., Yuan,Y., Li,C.,
            Wang,W., Guan,W., Chen,H., Jin,C., Wei,J., Zhang,W., Yang,Y.,
            Liu,Q., Zhou,Y., Zhang,C., Wu,Z., Xu,W., Zhang,Y., Liu,T., Yu,D.,
            Zhang,Y., Chen,L., Zhu,D., Zhong,X., Kang,L., Gan,X., Yu,X., Ma,Q.,
            Yan,J., Zhou,L., Liu,Z., Zhu,Y., Zhou,T., He,F. and Yang,X.
  TITLE     Toward an understanding of the protein interaction network of the
            human liver
  JOURNAL   Mol Syst Biol 7, 536 (2011)
   PUBMED   21988832
  REMARK    Erratum:[Mol Syst Biol. 2017 Dec 18;13(12):965. doi:
            10.15252/msb.20178107. PMID: 29254952]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 876)
  AUTHORS   Bisson,N., James,D.A., Ivosev,G., Tate,S.A., Bonner,R., Taylor,L.
            and Pawson,T.
  TITLE     Selected reaction monitoring mass spectrometry reveals the dynamics
            of signaling through the GRB2 adaptor
  JOURNAL   Nat Biotechnol 29 (7), 653-658 (2011)
   PUBMED   21706016
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 876)
  AUTHORS   Bandyopadhyay,S., Chiang,C.Y., Srivastava,J., Gersten,M., White,S.,
            Bell,R., Kurschner,C., Martin,C., Smoot,M., Sahasrabudhe,S.,
            Barber,D.L., Chanda,S.K. and Ideker,T.
  TITLE     A human MAP kinase interactome
  JOURNAL   Nat Methods 7 (10), 801-805 (2010)
   PUBMED   20936779
REFERENCE   10 (residues 1 to 876)
  AUTHORS   Tashiro,K., Tsunematsu,T., Okubo,H., Ohta,T., Sano,E., Yamauchi,E.,
            Taniguchi,H. and Konishi,H.
  TITLE     GAREM, a novel adaptor protein for growth factor receptor-bound
            protein 2, contributes to cellular transformation through the
            activation of extracellular signal-regulated kinase signaling
  JOURNAL   J Biol Chem 284 (30), 20206-20214 (2009)
   PUBMED   19509291
  REMARK    GeneRIF: Extracellular signal-regulated kinase activation in
            response to epidermal growth factor stimulation is regulated by the
            expression of GAREM in COS-7 and HeLa cells.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC009835.14, AK025263.1,
            BC121068.1, AK025660.1, AC015563.11 and AI479499.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an adaptor protein which functions in
            the epidermal growth factor (EGF) receptor-mediated signaling
            pathway. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Oct 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.258763.1,
                                           SRR1803617.223086.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467150 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269209.7/ ENSP00000269209.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..876
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..876
                     /product="GRB2-associated and regulator of MAPK protein 1
                     isoform 1"
                     /note="Grb2-associated and regulator of Erk/MAPK; protein
                     FAM59A; family with sequence similarity 59, member A;
                     GRB2-associated and regulator of MAPK1; GRB2 associated,
                     regulator of MAPK1; GRB2 associated regulator of MAPK1 1;
                     GRB2-associated and regulator of MAPK protein 1"
                     /calculated_mol_wt=97055
     Region          12..320
                     /region_name="CABIT"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          32..323
                     /region_name="CABIT"
                     /note="Cell-cycle sustaining, positive selection;
                     pfam12736"
                     /db_xref="CDD:463686"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19509291; propagated from
                     UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          414..>766
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     Site            453
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:19509291; propagated from
                     UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          496..572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          498..550
                     /region_name="Necessary for interaction with GRB2.
                     /evidence=ECO:0000269|PubMed:19509291"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H706.2)"
     Site            610
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H706.2)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          626..664
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          738..763
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H706.2)"
     Region          808..874
                     /region_name="SAM_GAREM"
                     /note="SAM domain of GAREM subfamily; cd09525"
                     /db_xref="CDD:188924"
     CDS             1..876
                     /gene="GAREM1"
                     /gene_synonym="C18orf11; FAM59A; GAREM; Gm944"
                     /coded_by="NM_001242409.2:455..3085"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56057.1"
                     /db_xref="GeneID:64762"
                     /db_xref="HGNC:HGNC:26136"
                     /db_xref="MIM:617998"
ORIGIN      
        1 mdpapslgcs lkdvkwssva vpldllvsty rlpqiarldn gecveglren dyllihscrq
       61 wttitahsle eghyvigpki eipvhyagqf klleqdrdik epvqyfnsve evakafperv
      121 yvmeditfnv kvasgecned tevynitlct gdeltlmgqa eilyaktfke ksrlntifkk
      181 igklnsiskl gkgkmpclic mnhrtnesis lpfqckgrfs trsplelqmq egehtirniv
      241 ektrlpvnvt vpsppprnpy dlhfireghr ykfvniqtkt vvvccvlrnn kilpmhfplh
      301 ltvpkfslpe hlvkgeswpe tlvhhwlgic qeqfdideys ravrdvktdw neeckspkkg
      361 rcsghnhvpn slsyardelt qsfhrlsvcv ygnnlhgnse vnlhgcrdlg gdwapfphdi
      421 lpyqdsgdsg sdylfpease esagipgkse lpyeelwlee gkpshqpltr slseknrcdq
      481 frgsvrskca tsplpipgtl gaavkssdta lppppvppks eavreecrll nappvpprsa
      541 kplstspsip prtvkparqq trspsptlsy yssglhnisv tktdtnpses tpvscypcnr
      601 vktdsvdlks pfgspsaeav ssrlswpnhy sgasesqtrs dflldpsrsy syprqktpgt
      661 pkrncpapfd fdgcellasp tspvtaefss svsgcpksas yslestdvks laagvtkqst
      721 scpalpprap klveekvase tsplplkidg aeedpksgsp dlsedqyfvk kgmqdifsas
      781 ypfssplhlq laprscgdgs pwqppadlsg lsieevsksl rfiglsedvi sffvtekidg
      841 nllvqlteei lsedfklskl qvkkimqfin gwrpki
//
LOCUS       NP_001336191             676 aa            linear   PRI 20-NOV-2025
DEFINITION  KAT8 regulatory NSL complex subunit 3 isoform 7 [Homo sapiens].
ACCESSION   NP_001336191
VERSION     NP_001336191.1
DBSOURCE    REFSEQ: accession NM_001349262.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 676)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 676)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 676)
  AUTHORS   Wu,D., Zhao,L., Feng,Z., Yu,C., Ding,J., Wang,L., Wang,F., Liu,D.,
            Zhu,H., Xing,F., Conaway,J.W., Conaway,R.C., Cai,Y. and Jin,J.
  TITLE     O-Linked N-acetylglucosamine transferase 1 regulates global histone
            H4 acetylation via stabilization of the nonspecific lethal protein
            NSL3
  JOURNAL   J Biol Chem 292 (24), 10014-10025 (2017)
   PUBMED   28450392
  REMARK    GeneRIF: Data suggest that O-GlcNAc transferase 1 (OGT1)
            specifically binds to, O-GlcNAcylates, and stabilizes nonspecific
            lethal protein3 (NSL3); stabilization of NSL3 by OGT1 up-regulates
            global acetylation levels of histone 4 at Lys-5, Lys-8, and Lys-16.
REFERENCE   4  (residues 1 to 676)
  AUTHORS   Chatterjee,A., Seyfferth,J., Lucci,J., Gilsbach,R., Preissl,S.,
            Bottinger,L., Martensson,C.U., Panhale,A., Stehle,T., Kretz,O.,
            Sahyoun,A.H., Avilov,S., Eimer,S., Hein,L., Pfanner,N., Becker,T.
            and Akhtar,A.
  TITLE     MOF Acetyl Transferase Regulates Transcription and Respiration in
            Mitochondria
  JOURNAL   Cell 167 (3), 722-738 (2016)
   PUBMED   27768893
REFERENCE   5  (residues 1 to 676)
  AUTHORS   Meunier,S., Shvedunova,M., Van Nguyen,N., Avila,L., Vernos,I. and
            Akhtar,A.
  TITLE     An epigenetic regulator emerges as microtubule minus-end binding
            and stabilizing factor in mitosis
  JOURNAL   Nat Commun 6, 7889 (2015)
   PUBMED   26243146
  REMARK    GeneRIF: microtubule minus-end-binding protein, essential for
            spindle assembly and chromosome segregation
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 676)
  AUTHORS   Zhao,X., Su,J., Wang,F., Liu,D., Ding,J., Yang,Y., Conaway,J.W.,
            Conaway,R.C., Cao,L., Wu,D., Wu,M., Cai,Y. and Jin,J.
  TITLE     Crosstalk between NSL histone acetyltransferase and MLL/SET
            complexes: NSL complex functions in promoting histone H3K4
            di-methylation activity by MLL/SET complexes
  JOURNAL   PLoS Genet 9 (11), e1003940 (2013)
   PUBMED   24244196
REFERENCE   7  (residues 1 to 676)
  AUTHORS   Cai,Y., Jin,J., Swanson,S.K., Cole,M.D., Choi,S.H., Florens,L.,
            Washburn,M.P., Conaway,J.W. and Conaway,R.C.
  TITLE     Subunit composition and substrate specificity of a MOF-containing
            histone acetyltransferase distinct from the male-specific lethal
            (MSL) complex
  JOURNAL   J Biol Chem 285 (7), 4268-4272 (2010)
   PUBMED   20018852
REFERENCE   8  (residues 1 to 676)
  AUTHORS   Rea,S., Xouri,G. and Akhtar,A.
  TITLE     Males absent on the first (MOF): from flies to humans
  JOURNAL   Oncogene 26 (37), 5385-5394 (2007)
   PUBMED   17694080
  REMARK    Review article
REFERENCE   9  (residues 1 to 676)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 676)
  AUTHORS   Mendjan,S., Taipale,M., Kind,J., Holz,H., Gebhardt,P., Schelder,M.,
            Vermeulen,M., Buscaino,A., Duncan,K., Mueller,J., Wilm,M.,
            Stunnenberg,H.G., Saumweber,H. and Akhtar,A.
  TITLE     Nuclear pore components are involved in the transcriptional
            regulation of dosage compensation in Drosophila
  JOURNAL   Mol Cell 21 (6), 811-823 (2006)
   PUBMED   16543150
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC079754.4.
            
            Transcript Variant: This variant (14) differs in the 5' UTR,
            contains an alternate exon in the 3' coding region, and initiates
            translation from a downstream start codon, compared to variant 1.
            The encoded isoform (7) is shorter than isoform 1. Both variants 13
            and 14 encode the same isoform (7).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.628327.1,
                                           SRR1660809.62694.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..676
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..676
                     /product="KAT8 regulatory NSL complex subunit 3 isoform 7"
                     /note="serum inhibited-related protein; testis development
                     protein PRTD; NSL complex protein NSL3; non-specific
                     lethal 3 homolog"
                     /calculated_mol_wt=69914
     Region          <95..244
                     /region_name="COG3571"
                     /note="Predicted hydrolase of the alpha/beta-hydrolase
                     fold [General function prediction only]"
                     /db_xref="CDD:442792"
     CDS             1..676
                     /gene="KANSL3"
                     /gene_synonym="KIAA1310; NSL3; Rcd1"
                     /coded_by="NM_001349262.2:488..2518"
                     /note="isoform 7 is encoded by transcript variant 14"
                     /db_xref="GeneID:55683"
                     /db_xref="HGNC:HGNC:25473"
                     /db_xref="MIM:617742"
ORIGIN      
        1 mlvssntktg aagaealsll lkrpwdpavg vlshnkpskl pgsplilias sgpsssvfpt
       61 srrhrfwqsq lsclgkvipv athllnngsg vgvlqclehm igavrskvle ihshfphkpi
      121 iligwntgal vachvsvmey vtavvclgfp lltvdgprgd vddplldmkt pvlfvigqns
      181 lqchpeamed frekiraens lvvvggaddn lriskakkks egltqsmvdr ciqdeivdfl
      241 tgvltraegh mgseprdqda ekkkkprdva rrdlafevpe rgsrpaspaa klpaspsgse
      301 dlssvssspt sspktkvttv tsaqkssqig ssqllkrhvq rteavlthkq aqaqfaaflk
      361 qnmlvrkalp pgtssclfvp isseppeege kedlrvqlkr hhpssplpgs ktskrpkikv
      421 slisqgdtag gpcapsqgsa peaaggkpit mtlgqasaga keltglltta ksssseggvs
      481 aspvpsvvss stapsalhtl qsrlvatspg sslpgatsas sllqglsfsl qdissktsgl
      541 panpspgpap qatsvklptp mqslgaittg tstivrtipv attlsslgat pggkptaihq
      601 lltngglakl asslpglaqi snqasglkvp ttitltlrgq psrittlspm gsgaapsees
      661 ssqvlpsssq rlppap
//
LOCUS       NP_001304113             821 aa            linear   PRI 20-NOV-2025
DEFINITION  cadherin-1 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001304113
VERSION     NP_001304113.1
DBSOURCE    REFSEQ: accession NM_001317184.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Si,W., Liu,J., Wang,Y., Mao,Y., Zhang,Y., Xu,S., Guo,K., Zhang,Y.,
            Hu,Y. and Zhang,F.
  TITLE     IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway
  JOURNAL   Int Immunopharmacol 142 (Pt A), 113074 (2024)
   PUBMED   39244903
  REMARK    GeneRIF: IL-8 promotes lens capsular residual cells migration by
            down-regulates expression of E-cadherin and ZO-1 via the
            CXCR1/2-NF-kappaB-RhoA signal pathway.
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Dash,S., Biswas,J., Goswami,S., Mukherjee,S., Ganguli,N.,
            Duraivelan,K., Mondal,S., Mukhopadhyay,R. and Samanta,D.
  TITLE     Molecular Crosstalk Between Adherens Junction Proteins, E-cadherin
            and Nectin-4
  JOURNAL   J Mol Biol 436 (18), 168709 (2024)
   PUBMED   39009071
  REMARK    GeneRIF: Molecular Crosstalk Between Adherens Junction Proteins,
            E-cadherin and Nectin-4.
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Peng,Y., Zhang,Y., Fang,R., Jiang,H., Lan,G., Xu,Z., Liu,Y.,
            Nie,Z., Ren,L., Wang,F., Zhang,S.D., Ma,Y., Yang,P., Ge,H.H.,
            Zhang,W.D., Luo,C., Li,A. and He,W.
  TITLE     Target Identification and Mechanistic Characterization of Indole
            Terpenoid Mimics: Proper Spindle Microtubule Assembly Is Essential
            for Cdh1-Mediated Proteolysis of CENP-A
  JOURNAL   Adv Sci (Weinh) 11 (29), e2305593 (2024)
   PUBMED   38873820
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Yim,I.S. and Laronde,D.M.
  TITLE     Biomarkers of epithelial-mesenchymal transition: E-cadherin and
            beta-catenin in malignant transformation of oral lesions
  JOURNAL   Can J Dent Hyg 58 (2), 111-119 (2024)
   PUBMED   38974823
  REMARK    GeneRIF: Biomarkers of epithelial-mesenchymal transition:
            E-cadherin and beta-catenin in malignant transformation of oral
            lesions.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Lecuit,T. and Yap,A.S.
  TITLE     E-cadherin junctions as active mechanical integrators in tissue
            dynamics
  JOURNAL   Nat Cell Biol 17 (5), 533-539 (2015)
   PUBMED   25925582
  REMARK    Review article
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Barbosa-Matos,R., Cordova,L., Schrader,K. and Oliveira,C.
  TITLE     Diffuse Gastric and Lobular Breast Cancer Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301318
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Knudsen,K.A. and Wheelock,M.J.
  TITLE     Plakoglobin, or an 83-kD homologue distinct from beta-catenin,
            interacts with E-cadherin and N-cadherin
  JOURNAL   J Cell Biol 118 (3), 671-679 (1992)
   PUBMED   1639850
REFERENCE   8  (residues 1 to 821)
  AUTHORS   La Vecchia,C., Negri,E., Franceschi,S. and Gentile,A.
  TITLE     Family history and the risk of stomach and colorectal cancer
  JOURNAL   Cancer 70 (1), 50-55 (1992)
   PUBMED   1606546
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Zanghieri,G., Di Gregorio,C., Sacchetti,C., Fante,R.,
            Sassatelli,R., Cannizzo,G., Carriero,A. and Ponz de Leon,M.
  TITLE     Familial occurrence of gastric cancer in the 2-year experience of a
            population-based registry
  JOURNAL   Cancer 66 (9), 2047-2051 (1990)
   PUBMED   2224804
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Mansouri,A., Spurr,N., Goodfellow,P.N. and Kemler,R.
  TITLE     Characterization and chromosomal localization of the gene encoding
            the human cell adhesion molecule uvomorulin
  JOURNAL   Differentiation 38 (1), 67-71 (1988)
   PUBMED   3263290
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK312551.1, AB025105.1 and
            EU709494.1.
            
            Summary: This gene encodes a classical cadherin of the cadherin
            superfamily. Alternative splicing results in multiple transcript
            variants, at least one of which encodes a preproprotein that is
            proteolytically processed to generate the mature glycoprotein. This
            calcium-dependent cell-cell adhesion protein is comprised of five
            extracellular cadherin repeats, a transmembrane region and a highly
            conserved cytoplasmic tail. Mutations in this gene are correlated
            with gastric, breast, colorectal, thyroid and ovarian cancer. Loss
            of function of this gene is thought to contribute to cancer
            progression by increasing proliferation, invasion, and/or
            metastasis. The ectodomain of this protein mediates bacterial
            adhesion to mammalian cells and the cytoplasmic domain is required
            for internalization. This gene is present in a gene cluster with
            other members of the cadherin family on chromosome 16. [provided by
            RefSeq, Nov 2015].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            central coding region compared to variant 1. The encoded isoform
            (2) is shorter than isoform 1. This isoform (2) may undergo
            proteolytic processing similar to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB025105.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..821
                     /product="cadherin-1 isoform 2 precursor"
                     /note="calcium-dependent adhesion protein, epithelial;
                     cadherin 1, E-cadherin (epithelial); cell-CAM 120/80;
                     uvomorulin; epithelial cadherin; cadherin 1, type 1,
                     E-cadherin (epithelial); E-cadherin 1; epididymis
                     secretory sperm binding protein"
                     /calculated_mol_wt=88499
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2461
     Region          27..116
                     /region_name="Cadherin_pro"
                     /note="Cadherin prodomain like; pfam08758"
                     /db_xref="CDD:462590"
     Region          158..258
                     /region_name="CA_like"
                     /note="Cadherin repeat-like domain; cd00031"
                     /db_xref="CDD:206635"
     Site            order(165..166,221,223,254,256..257)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206635"
     Region          266..371
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(273..274,334,336,367,369..370)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Site            280
                     /site_type="glycosylation"
                     /note="O-linked (Man...) serine.
                     /evidence=ECO:0000250|UniProtKB:P09803; propagated from
                     UniProtKB/Swiss-Prot (P12830.3)"
     Site            285
                     /site_type="glycosylation"
                     /note="O-linked (Man...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P09803; propagated from
                     UniProtKB/Swiss-Prot (P12830.3)"
     Site            358
                     /site_type="glycosylation"
                     /note="O-linked (Man...) threonine.
                     /evidence=ECO:0000250|UniProtKB:P09803; propagated from
                     UniProtKB/Swiss-Prot (P12830.3)"
     Site            364..365
                     /site_type="cleavage"
                     /note="Cleavage, by S.pyogenes SpeB.
                     /evidence=ECO:0000269|PubMed:23532847; propagated from
                     UniProtKB/Swiss-Prot (P12830.3)"
     Region          431..530
                     /region_name="Cadherin_repeat"
                     /note="Cadherin tandem repeat domain; cd11304"
                     /db_xref="CDD:206637"
     Site            order(436..437,488,490,526,528..529)
                     /site_type="other"
                     /note="Ca2+ binding site [ion binding]"
                     /db_xref="CDD:206637"
     Region          537..625
                     /region_name="Cadherin"
                     /note="Cadherin domain; pfam00028"
                     /db_xref="CDD:394985"
     Region          757..816
                     /region_name="CADH_Y-type_LIR"
                     /note="Cadherin, Y-type LIR-motif; pfam01049"
                     /db_xref="CDD:460041"
     CDS             1..821
                     /gene="CDH1"
                     /gene_synonym="Arc-1; BCDS1; CD324; CDHE; ECAD; LCAM; UVO"
                     /coded_by="NM_001317184.2:125..2590"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS82005.1"
                     /db_xref="GeneID:999"
                     /db_xref="HGNC:HGNC:1748"
                     /db_xref="MIM:192090"
ORIGIN      
        1 mgpwsrslsa lllllqvssw lcqepepchp gfdaesytft vprrhlergr vlgrvnfedc
       61 tgrqrtayfs ldtrfkvgtd gvitvkrplr fhnpqihflv yawdstyrkf stkvtlntvg
      121 hhhrppphqa svsgiqaell tfpnsspglr rqkrdwvipp iscpenekgp fpknlvqiks
      181 nkdkegkvfy sitgqgadtp pvgvfiiere tgwlkvtepl dreriatytl fshavssngn
      241 avedpmeili tvtdqndnkp eftqevfkgs vmegalpgts vmevtatdad ddvntynaai
      301 aytilsqdpe lpdknmftin rntgvisvvt tgldresfpt ytlvvqaadl qgeglsttat
      361 avitvtdtnd nppifnpttg ldfeakqqyi lhvavtnvvp fevslttsta tvtvdvldvn
      421 eapifvppek rvevsedfgv gqeitsytaq epdtfmeqki tyriwrdtan wleinpdtga
      481 istraeldre dfehvknsty taliiatdng spvatgtgtl llilsdvndn apipeprtif
      541 fcernpkpqv iniidadlpp ntspftaelt hgasanwtiq yndptqesii lkpkmalevg
      601 dykinlklmd nqnkdqvttl evsvcdcega agvcrkaqpv eaglqipail gilggilall
      661 ililllllfl rrravvkepl lppeddtrdn vyyydeeggg eedqdfdlsq lhrgldarpe
      721 vtrndvaptl msvprylprp anpdeignfi denlkaadtd ptappydsll vfdyegsgse
      781 aaslsslnss esdkdqdydy lnewgnrfkk ladmyggged d
//
LOCUS       NP_001736                296 aa            linear   PRI 20-NOV-2025
DEFINITION  guided entry of tail-anchored proteins factor CAMLG [Homo sapiens].
ACCESSION   NP_001736
VERSION     NP_001736.1
DBSOURCE    REFSEQ: accession NM_001745.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 296)
  AUTHORS   McDowell,M.A., Heimes,M., Fiorentino,F., Mehmood,S., Farkas,A.,
            Coy-Vergara,J., Wu,D., Bolla,J.R., Schmid,V., Heinze,R., Wild,K.,
            Flemming,D., Pfeffer,S., Schwappach,B., Robinson,C.V. and
            Sinning,I.
  TITLE     Structural Basis of Tail-Anchored Membrane Protein Biogenesis by
            the GET Insertase Complex
  JOURNAL   Mol Cell 80 (1), 72-86 (2020)
   PUBMED   32910895
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Inglis,A.J., Page,K.R., Guna,A. and Voorhees,R.M.
  TITLE     Differential Modes of Orphan Subunit Recognition for the WRB/CAML
            Complex
  JOURNAL   Cell Rep 30 (11), 3691-3698 (2020)
   PUBMED   32187542
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Tovey,S.C., Bootman,M.D., Lipp,P., Berridge,M.J. and Bram,R.J.
  TITLE     Calcium-modulating cyclophilin ligand desensitizes hormone-evoked
            calcium release
  JOURNAL   Biochem Biophys Res Commun 276 (1), 97-100 (2000)
   PUBMED   11006089
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Holloway,M.P. and Bram,R.J.
  TITLE     Co-localization of calcium-modulating cyclophilin ligand with
            intracellular calcium pools
  JOURNAL   J Biol Chem 273 (26), 16346-16350 (1998)
   PUBMED   9632697
REFERENCE   8  (residues 1 to 296)
  AUTHORS   von Bulow,G.U. and Bram,R.J.
  TITLE     NF-AT activation induced by a CAML-interacting member of the tumor
            necrosis factor receptor superfamily
  JOURNAL   Science 278 (5335), 138-141 (1997)
   PUBMED   9311921
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Bram,R.J., Valentine,V., Shapiro,D.N., Jenkins,N.A., Gilbert,D.J.
            and Copeland,N.G.
  TITLE     The gene for calcium-modulating cyclophilin ligand (CAMLG) is
            located on human chromosome 5q23 and a syntenic region of mouse
            chromosome 13
  JOURNAL   Genomics 31 (2), 257-260 (1996)
   PUBMED   8824814
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Bram,R.J. and Crabtree,G.R.
  TITLE     Calcium signalling in T cells stimulated by a cyclophilin B-binding
            protein
  JOURNAL   Nature 371 (6495), 355-358 (1994)
   PUBMED   7522304
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA727548.1, U18242.1,
            AC010301.7 and BX111055.1.
            
            Summary: The immunosuppressant drug cyclosporin A blocks a
            calcium-dependent signal from the T-cell receptor (TCR) that
            normally leads to T-cell activation. When bound to cyclophilin B,
            cyclosporin A binds and inactivates the key signaling intermediate
            calcineurin. The protein encoded by this gene functions similarly
            to cyclosporin A, binding to cyclophilin B and acting downstream of
            the TCR and upstream of calcineurin by causing an influx of
            calcium. This integral membrane protein appears to be a new
            participant in the calcium signal transduction pathway, implicating
            cyclophilin B in calcium signaling, even in the absence of
            cyclosporin. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.480092.1,
                                           SRR3476690.273731.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297156.4/ ENSP00000297156.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..296
                     /product="guided entry of tail-anchored proteins factor
                     CAMLG"
                     /note="cyclophilin B-binding protein; calcium-modulating
                     cyclophilin ligand; calcium signal-modulating cyclophilin
                     ligand"
                     /calculated_mol_wt=32822
     Region          1..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P49069.1)"
     Region          23..292
                     /region_name="Get2_like"
                     /note="Get2-like; pfam14963"
                     /db_xref="CDD:464408"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P49069.1)"
     Site            190..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49069.1)"
     Site            213..231
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49069.1)"
     Site            270..288
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P49069.1)"
     CDS             1..296
                     /gene="CAMLG"
                     /gene_synonym="CAML; CDG2Z; GET2"
                     /coded_by="NM_001745.4:74..964"
                     /db_xref="CCDS:CCDS4178.1"
                     /db_xref="GeneID:819"
                     /db_xref="HGNC:HGNC:1471"
                     /db_xref="MIM:601118"
ORIGIN      
        1 mesmavatdg gerpgvpags glsasqrrae lrrrkllmns eqrinrimgf hrpgsgaeee
       61 sqtkskqqds dklnslsvps vskrvvlgds vstgttdqqg gvaevkgtql gdkldsfikp
      121 pecssdvnle lrqrnrgdlt adsvqrgsrh gleqylsrfe eamklrkqli sekpsqedgn
      181 tteefdsfri frlvgcalla lgvrafvcky lsifapfltl qlaymglyky fpksekkikt
      241 tvltaallls gipaevinrs mdtyskmgev ftdlcvyfft fifchelldy wgsevp
//
LOCUS       NP_056235                445 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 13 isoform 1 [Homo sapiens].
ACCESSION   NP_056235 NP_054875
VERSION     NP_056235.5
DBSOURCE    REFSEQ: accession NM_015420.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Tang,Z.Y., Wang,X.M., Xu,C.W., Sun,Q.Q., Hua,Y.X., Zhou,Q.Y.,
            Hu,H.Y., Liu,S.B., Guo,Y.J., Ao,L., Che,X., Zhang,X.C., Heger,M.,
            Zheng,X., Liu,A.J., Wang,Q., Zhan,Z.J., Cheng,S.Q. and Pan,W.W.
  TITLE     DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway
  JOURNAL   Cell Mol Life Sci 81 (1), 421 (2024)
   PUBMED   39367995
  REMARK    GeneRIF: DCAF13 promotes ovarian cancer progression by activating
            FRAS1-mediated FAK signaling pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 445)
  AUTHORS   Ren,P., Tong,X., Li,J., Jiang,H., Liu,S., Li,X., Lai,M., Yang,W.,
            Rong,Y., Zhang,Y., Jin,J., Ma,Y., Pan,W., Fan,H.Y., Zhang,S. and
            Zhang,Y.L.
  TITLE     CRL4DCAF13 E3 ubiquitin ligase targets MeCP2 for degradation to
            prevent DNA hypermethylation and ensure normal transcription in
            growing oocytes
  JOURNAL   Cell Mol Life Sci 81 (1), 165 (2024)
   PUBMED   38578457
  REMARK    GeneRIF: CRL4[DCAF13] E3 ubiquitin ligase targets MeCP2 for
            degradation to prevent DNA hypermethylation and ensure normal
            transcription in growing oocytes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 445)
  AUTHORS   Manzoor,H., Zahid,H., Emerling,C.A., Kumar,K.R., Hussain,H.M.J.,
            Seo,G.H., Wajid,M. and Naz,S.
  TITLE     A biallelic variant of DCAF13 implicated in a neuromuscular
            disorder in humans
  JOURNAL   Eur J Hum Genet 31 (6), 629-637 (2023)
   PUBMED   36797467
  REMARK    GeneRIF: A biallelic variant of DCAF13 implicated in a
            neuromuscular disorder in humans.
REFERENCE   4  (residues 1 to 445)
  AUTHORS   Wei,S., Lu,K., Xing,J. and Yu,W.
  TITLE     A multidimensional pan-cancer analysis of DCAF13 and its
            protumorigenic effect in lung adenocarcinoma
  JOURNAL   FASEB J 37 (4), e22849 (2023)
   PUBMED   36884358
  REMARK    GeneRIF: A multidimensional pan-cancer analysis of DCAF13 and its
            protumorigenic effect in lung adenocarcinoma.
REFERENCE   5  (residues 1 to 445)
  AUTHORS   Yan,X., Rong,M., Zhou,Q. and Zhang,C.
  TITLE     DCAF13 is essential for the pathogenesis of preeclampsia through
            its involvement in endometrial decidualization
  JOURNAL   Mol Cell Endocrinol 556, 111741 (2022)
   PUBMED   35932979
  REMARK    GeneRIF: DCAF13 is essential for the pathogenesis of preeclampsia
            through its involvement in endometrial decidualization.
REFERENCE   6  (residues 1 to 445)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   7  (residues 1 to 445)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   8  (residues 1 to 445)
  AUTHORS   Urano,T., Shiraki,M., Usui,T., Sasaki,N., Ouchi,Y. and Inoue,S.
  TITLE     Identification of non-synonymous polymorphisms in the WDSOF1 gene
            as novel susceptibility markers for low bone mineral density in
            Japanese postmenopausal women
  JOURNAL   Bone 47 (3), 636-642 (2010)
   PUBMED   20601284
  REMARK    GeneRIF: This study suggests that non-synonymous WDSOF1
            polymorphisms play a role in the genetic susceptibility to
            osteoporosis.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 445)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   10 (residues 1 to 445)
  AUTHORS   Andersen,J.S., Lyon,C.E., Fox,A.H., Leung,A.K., Lam,Y.W., Steen,H.,
            Mann,M. and Lamond,A.I.
  TITLE     Directed proteomic analysis of the human nucleolus
  JOURNAL   Curr Biol 12 (1), 1-11 (2002)
   PUBMED   11790298
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK027799.1, AC012213.8 and CA429438.1.
            
            On Jul 12, 2018 this sequence version replaced NP_056235.4.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.743504.1,
                                           SRR1803613.2471.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000612750.5/ ENSP00000484962.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q22.3"
     Protein         1..445
                     /product="DDB1- and CUL4-associated factor 13 isoform 1"
                     /note="WD repeats and SOF1 domain containing; WD repeat
                     and SOF domain-containing protein 1"
                     /calculated_mol_wt=51271
     Region          59..353
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Site            order(65,84,88,94..95,107..108,126,130,136..137,155,172,
                     177,183..184,212,218,224..225,236..237,255,260,266..267,
                     280..281,298,303,309..310,321,342,346,352..353)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          70..107
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          112..154
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          162..197
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          199..236
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          244..278
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          285..309
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          328..364
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          354..435
                     /region_name="Sof1"
                     /note="Sof1-like domain; pfam04158"
                     /db_xref="CDD:427753"
     CDS             1..445
                     /gene="DCAF13"
                     /gene_synonym="GM83; HSPC064; Sof1; WDSOF1"
                     /coded_by="NM_015420.7:62..1399"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34934.2"
                     /db_xref="GeneID:25879"
                     /db_xref="HGNC:HGNC:24535"
                     /db_xref="MIM:616196"
ORIGIN      
        1 mkvkmlsrnp dnyvretkld lqrvprnydp alhpfevpre yiralnatkl ervfakpfla
       61 sldghrdgvn clakhpekla tvlsgacdge vriwnltqrn cirtiqaheg fvrgictrfc
      121 gtsfftvgdd ktvkqwkmdg pgygdeeepl htilgktvyt gidhhwkeav fatcgqqvdi
      181 wdeqrtnpic smtwgfdsis svkfnpietf llgscasdrn ivlydmrqat plkkvildmr
      241 tnticwnpme afiftaaned ynlytfdmra ldtpvmvhmd hvsavldvdy sptgkefvsa
      301 sfdksirifp vdksrsrevy htkrmqhvic vkwtsdskyi mcgsdemnir lwkanasekl
      361 gvltsrekaa kdynqklkek fqhyphikri arhrhlpksi ysqiqeqrim kearrrkevn
      421 rikhskpgsv plvsekkkhv vavvk
//
LOCUS       NP_056273                549 aa            linear   PRI 20-NOV-2025
DEFINITION  myotubularin-related protein 9 [Homo sapiens].
ACCESSION   NP_056273
VERSION     NP_056273.2
DBSOURCE    REFSEQ: accession NM_015458.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 549)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 549)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 549)
  AUTHORS   Shi,Z., Jia,X., Tian,Y., Liu,X., Bai,J., Liu,Y., Zhang,F., Li,J.,
            Gao,X. and Zhang,K.
  TITLE     Genetic Variants of the MTMR9 Gene Are Associated with Nonspecific
            Intellectual Disability: A Family-Based Association Study
  JOURNAL   Genet Test Mol Biomarkers 24 (10), 625-631 (2020)
   PUBMED   32991201
  REMARK    GeneRIF: Genetic Variants of the MTMR9 Gene Are Associated with
            Nonspecific Intellectual Disability: A Family-Based Association
            Study.
REFERENCE   4  (residues 1 to 549)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 549)
  AUTHORS   Doubravska,L., Dostal,V., Knop,F., Libusova,L. and Macurkova,M.
  TITLE     Human myotubularin-related protein 9 regulates ER-to-Golgi
            trafficking and modulates WNT3A secretion
  JOURNAL   Exp Cell Res 386 (1), 111709 (2020)
   PUBMED   31704058
  REMARK    GeneRIF: MTMR9 localizes to the intermediate compartment and to the
            Golgi apparatus. MTMR9 modulates WNT3A signalling by interfering
            with WNT3A secretion.
REFERENCE   6  (residues 1 to 549)
  AUTHORS   Lorenzo,O., Urbe,S. and Clague,M.J.
  TITLE     Systematic analysis of myotubularins: heteromeric interactions,
            subcellular localisation and endosome related functions
  JOURNAL   J Cell Sci 119 (Pt 14), 2953-2959 (2006)
   PUBMED   16787938
REFERENCE   7  (residues 1 to 549)
  AUTHORS   Mochizuki,Y. and Majerus,P.W.
  TITLE     Characterization of myotubularin-related protein 7 and its binding
            partner, myotubularin-related protein 9
  JOURNAL   Proc Natl Acad Sci U S A 100 (17), 9768-9773 (2003)
   PUBMED   12890864
REFERENCE   8  (residues 1 to 549)
  AUTHORS   Appel,S., Filter,M., Reis,A., Hennies,H.C., Bergheim,A.,
            Ogilvie,E., Arndt,S., Simmons,A., Lovett,M., Hide,W., Ramsay,M.,
            Reichwald,K., Zimmermann,W. and Rosenthal,A.
  TITLE     Physical and transcriptional map of the critical region for
            keratolytic winter erythema (KWE) on chromosome 8p22-p23 between
            D8S550 and D8S1759
  JOURNAL   Eur J Hum Genet 10 (1), 17-25 (2002)
   PUBMED   11896452
REFERENCE   9  (residues 1 to 549)
  AUTHORS   Appel,S., Reichwald,K., Zimmermann,W., Reis,A., Rosenthal,A. and
            Hennies,H.C.
  TITLE     Identification and localization of a new human myotubularin-related
            protein gene, mtmr8, on 8p22-p23
  JOURNAL   Genomics 75 (1-3), 6-8 (2001)
   PUBMED   11472061
REFERENCE   10 (residues 1 to 549)
  AUTHORS   Wang,J.C., Radford,D.M., Holt,M.S., Helms,C., Goate,A., Brandt,W.,
            Parik,M., Phillips,N.J., DeSchryver,K., Schuh,M.E., Fair,K.L.,
            Ritter,J.H., Marshall,P. and Donis-Keller,H.
  TITLE     Sequence-ready contig for the 1.4-cM ductal carcinoma in situ loss
            of heterozygosity region on chromosome 8p22-p23
  JOURNAL   Genomics 60 (1), 1-11 (1999)
   PUBMED   10458905
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ297823.1 and BU631532.1.
            
            On Apr 4, 2002 this sequence version replaced NP_056273.1.
            
            Summary: This gene encodes a myotubularin-related protein that is
            atypical to most other members of the myotubularin-related protein
            family because it has no dual-specificity phosphatase domain. The
            encoded protein contains a double-helical motif similar to the SET
            interaction domain, which is thought to have a role in the control
            of cell proliferation. In mouse, a protein similar to the encoded
            protein binds with MTMR7, and together they dephosphorylate
            phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ297823.1, BC034990.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000221086.8/ ENSP00000221086.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..549
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..549
                     /product="myotubularin-related protein 9"
                     /note="myotubularin related protein 8; inactive
                     phosphatidylinositol 3-phosphatase 9"
                     /calculated_mol_wt=63331
     Region          1..97
                     /region_name="PH-GRAM_MTMR9"
                     /note="Myotubularian (MTM) related 9 protein (MTMR9)
                     Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase
                     activators and Myotubularins (PH-GRAM) domain; cd13211"
                     /db_xref="CDD:275398"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q96QG7.1)"
     Region          121..446
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96QG7.1)"
     CDS             1..549
                     /gene="MTMR9"
                     /gene_synonym="C8orf9; LIP-STYX; MTMR8"
                     /coded_by="NM_015458.4:74..1723"
                     /db_xref="CCDS:CCDS5979.1"
                     /db_xref="GeneID:66036"
                     /db_xref="HGNC:HGNC:14596"
                     /db_xref="MIM:606260"
ORIGIN      
        1 mefaeliktp rvdnvvlhrp fypavegtlc ltghhlilss rqdnteelwl lhsnidaidk
       61 rfvgslgtii ikckdfriiq ldipgmeecl niassieals tldsitlmyp ffyrpmfevi
      121 edgwhsflpe qefelyssat sewrlsyvnk efavcpsypp ivtvpksidd ealrkvatfr
      181 hggrfpvlsy yhkkngmvim rsgqpltgtn grrckedekl inatlragkr gyiidtrsln
      241 vaqqtrakgg gfeqeahypq wrrihksier yhilqeslik lveacndqth nmdrwlskle
      301 asnwlthike ilttaclaaq cidregasil ihgtegtdst lqvtslaqii leprsrtirg
      361 fealierewl qaghpfqqrc aqsaycntkq kweapvfllf ldcvwqilrq fpcsfefnen
      421 flimlfehay asqfgtflgn nesercklkl qqktmslwsw vnqpselskf tnplfeannl
      481 viwpsvapqs lplwegiflr wnrsskylde ayeemvniie ynkelqakvn ilrrqlaele
      541 tedgmqesp
//
LOCUS       NP_008896                368 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 24 isoform 1 [Homo sapiens].
ACCESSION   NP_008896
VERSION     NP_008896.2
DBSOURCE    REFSEQ: accession NM_006965.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Meng,F., Ai,C., Yan,G. and Wang,G.
  TITLE     Tumor-suppressive zinc finger protein 24 (ZNF24) sensitizes
            colorectal cancer cells to 5-fluorouracil by inhibiting the Wnt
            pathway and activating the p53 signaling
  JOURNAL   Exp Cell Res 433 (1), 113796 (2023)
   PUBMED   37774763
  REMARK    GeneRIF: Tumor-suppressive zinc finger protein 24 (ZNF24)
            sensitizes colorectal cancer cells to 5-fluorouracil by inhibiting
            the Wnt pathway and activating the p53 signaling.
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Liu,Y., Cheng,H., Cheng,C., Zheng,F., Zhao,Z., Chen,Q., Zeng,W.,
            Zhang,P., Huang,C., Jiang,W., Liu,X. and Liu,G.
  TITLE     ZNF191 alters DNA methylation and activates the PI3K-AKT pathway in
            hepatoma cells via transcriptional regulation of DNMT1
  JOURNAL   Cancer Med 11 (5), 1269-1280 (2022)
   PUBMED   35092191
  REMARK    GeneRIF: ZNF191 alters DNA methylation and activates the PI3K-AKT
            pathway in hepatoma cells via transcriptional regulation of DNMT1.
REFERENCE   4  (residues 1 to 368)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Liu,Y., Wu,D., Cheng,H., Chen,L., Zhang,W., Zou,L., Gao,Q.,
            Zhao,Z., Chen,Q., Zeng,W., Zhang,Z., Jiang,W., Huang,C. and Liu,G.
  TITLE     Wnt8B, transcriptionally regulated by ZNF191, promotes cell
            proliferation of hepatocellular carcinoma via Wnt signaling
  JOURNAL   Cancer Sci 112 (2), 629-640 (2021)
   PUBMED   33197287
  REMARK    GeneRIF: Wnt8B, transcriptionally regulated by ZNF191, promotes
            cell proliferation of hepatocellular carcinoma via Wnt signaling.
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Albanese,V., Biguet,N.F., Kiefer,H., Bayard,E., Mallet,J. and
            Meloni,R.
  TITLE     Quantitative effects on gene silencing by allelic variation at a
            tetranucleotide microsatellite
  JOURNAL   Hum Mol Genet 10 (17), 1785-1792 (2001)
   PUBMED   11532988
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Han,Z.G., Zhang,Q.H., Ye,M., Kan,L.X., Gu,B.W., He,K.L., Shi,S.L.,
            Zhou,J., Fu,G., Mao,M., Chen,S.J., Yu,L. and Chen,Z.
  TITLE     Molecular cloning of six novel Kruppel-like zinc finger genes from
            hematopoietic cells and identification of a novel transregulatory
            domain KRNB
  JOURNAL   J Biol Chem 274 (50), 35741-35748 (1999)
   PUBMED   10585455
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Williams,A.J., Blacklow,S.C. and Collins,T.
  TITLE     The zinc finger-associated SCAN box is a conserved oligomerization
            domain
  JOURNAL   Mol Cell Biol 19 (12), 8526-8535 (1999)
   PUBMED   10567577
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Rousseau-Merck,M.F., Huebner,K., Berger,R. and Thiesen,H.J.
  TITLE     Chromosomal localization of two human zinc finger protein genes,
            ZNF24 (KOX17) and ZNF29 (KOX26), to 18q12 and 17p13-p12,
            respectively
  JOURNAL   Genomics 9 (1), 154-161 (1991)
   PUBMED   2004757
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Thiesen,H.J.
  TITLE     Multiple genes encoding zinc finger domains are expressed in human
            T cells
  JOURNAL   New Biol 2 (4), 363-374 (1990)
   PUBMED   2288909
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC116447.10.
            
            On Jun 18, 2008 this sequence version replaced NP_008896.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.15229.1,
                                           SRR1660805.7258.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261332.11/ ENSP00000261332.5
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..368
                     /product="zinc finger protein 24 isoform 1"
                     /note="zinc finger protein 191; zinc finger protein 24
                     (KOX 17); zinc finger protein KOX17; retinoic acid
                     suppression protein A; zinc finger and SCAN
                     domain-containing protein 3"
                     /calculated_mol_wt=42024
     Region          48..160
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Site            142
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          <249..329
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          251..301
                     /region_name="Necessary and sufficient for nuclear
                     localization"
                     /note="propagated from UniProtKB/Swiss-Prot (P17028.4)"
     Region          253..273
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(258,260,262,264..265,268..269,272,286,288,292..293,
                     296..297,300,314,316,318,320..321,324..325,328)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Site            274
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          281..301
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          305..>358
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          309..329
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (P17028.4)"
     Region          337..357
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..368
                     /gene="ZNF24"
                     /gene_synonym="KOX17; RSG-A; Zfp191; ZNF191; ZSCAN3"
                     /coded_by="NM_006965.4:145..1251"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11912.1"
                     /db_xref="GeneID:7572"
                     /db_xref="HGNC:HGNC:13032"
                     /db_xref="MIM:194534"
ORIGIN      
        1 msaqsveeds iliiptpdee ekilrvklee dpdgeegssi pwnhlpdpei frqrfrqfgy
       61 qdspgpreav sqlrelcrlw lrpethtkeq ilelvvleqf vailpkelqt wvrdhhpeng
      121 eeavtvledl eselddpgqp vslrrrkrev lvedmvsqee aqglpsseld avenqlkwas
      181 welhslrhcd ddgrtengal apkqelpsal eshevpgtln mgvpqifkyg etcfpkgrfe
      241 rkrnpsrkkq hicdecgkhf sqgsalilhq rihsgekpyg cvecgkafsr ssilvqhqrv
      301 htgekpykcl ecgkafsqns glinhqriht gekpyecvqc gksysqssnl frhqrrhnae
      361 kllnvvkv
//
LOCUS       NP_060434                461 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 6 isoform 2 [Homo sapiens].
ACCESSION   NP_060434
VERSION     NP_060434.2
DBSOURCE    REFSEQ: accession NM_017964.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 461)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 461)
  AUTHORS   Song,C.C., Liu,T., Hogstrand,C., Zhong,C.C., Zheng,H., Sun,L.H. and
            Luo,Z.
  TITLE     SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409 involved
            in the regulation of zinc metabolism in Golgi apparatus
  JOURNAL   Cell Mol Life Sci 81 (1), 422 (2024)
   PUBMED   39367979
  REMARK    GeneRIF: SENP1 mediates zinc-induced ZnT6 deSUMOylation at Lys-409
            involved in the regulation of zinc metabolism in Golgi apparatus.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 461)
  AUTHORS   Aktay,I., Billur,D., Tuncay,E. and Turan,B.
  TITLE     An Overexpression of SLC30A6 Gene Contributes to Cardiomyocyte
            Dysfunction via Affecting Mitochondria and Inducing Activations in
            K-Acetylation and Epigenetic Proteins
  JOURNAL   Biochem Genet 62 (4), 3198-3214 (2024)
   PUBMED   38091184
  REMARK    GeneRIF: An Overexpression of SLC30A6 Gene Contributes to
            Cardiomyocyte Dysfunction via Affecting Mitochondria and Inducing
            Activations in K-Acetylation and Epigenetic Proteins.
REFERENCE   4  (residues 1 to 461)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 461)
  AUTHORS   Zhu,B., Huo,R., Zhi,Q., Zhan,M., Chen,X. and Hua,Z.C.
  TITLE     Increased expression of zinc transporter ZIP4, ZIP11, ZnT1, and
            ZnT6 predicts poor prognosis in pancreatic cancer
  JOURNAL   J Trace Elem Med Biol 65, 126734 (2021)
   PUBMED   33631610
  REMARK    GeneRIF: Increased expression of zinc transporter ZIP4, ZIP11,
            ZnT1, and ZnT6 predicts poor prognosis in pancreatic cancer.
REFERENCE   6  (residues 1 to 461)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   7  (residues 1 to 461)
  AUTHORS   Smith,J.L., Xiong,S., Markesbery,W.R. and Lovell,M.A.
  TITLE     Altered expression of zinc transporters-4 and -6 in mild cognitive
            impairment, early and late Alzheimer's disease brain
  JOURNAL   Neuroscience 140 (3), 879-888 (2006)
   PUBMED   16580781
  REMARK    GeneRIF: Our results show that Zn transporter-4 and Zn
            transporter-6 are significantly (P<0.05) increased in
            hippocampus/parahippocampal gyrus of early Alzheimer's disease and
            Alzheimer's disease subjects.
REFERENCE   8  (residues 1 to 461)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   9  (residues 1 to 461)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 461)
  AUTHORS   Huang,L., Kirschke,C.P. and Gitschier,J.
  TITLE     Functional characterization of a novel mammalian zinc transporter,
            ZnT6
  JOURNAL   J Biol Chem 277 (29), 26389-26395 (2002)
   PUBMED   11997387
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055663.1, BC032525.1,
            BG527678.1 and AA594503.1.
            
            On Jul 3, 2002 this sequence version replaced NP_060434.1.
            
            Summary: This gene encodes a member of a family of proteins that
            function as zinc transporters. This protein can regulate
            subcellular levels of zinc in the Golgi and vesicles. Expression of
            this gene is altered in the Alzheimer's disease brain plaques.
            [provided by RefSeq, Aug 2016].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon compared to variant 1. The resulting protein (isoform 2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK055663.1, SRR1803611.92922.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000282587.9/ ENSP00000282587.5
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..461
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p22.3"
     Protein         1..461
                     /product="zinc transporter 6 isoform 2"
                     /note="zinc transporter 6; solute carrier family 30 (zinc
                     transporter), member 6"
                     /calculated_mol_wt=50985
     Site            34..54
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Region          43..255
                     /region_name="Cation_efflux"
                     /note="Cation efflux family; pfam01545"
                     /db_xref="CDD:426316"
     Site            65..85
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Site            99..119
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Site            201..221
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Site            224..244
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     Region          371..392
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NXT4.2)"
     CDS             1..461
                     /gene="SLC30A6"
                     /gene_synonym="MST103; MSTP103; ZNT6"
                     /coded_by="NM_017964.5:38..1423"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS1780.1"
                     /db_xref="GeneID:55676"
                     /db_xref="HGNC:HGNC:19305"
                     /db_xref="MIM:611148"
ORIGIN      
        1 mgtihlfrkp qrsffgkllr efrlvaadrr swkillfgvi nlictgfllm wcsstnsial
       61 taytyltifd lfslmtclis ywvtlrkpsp vysfgferle vlavfastvl aqlgalfilk
      121 esaerfleqp eihtgrllvg tfvalcfnlf tmlsirnkpf ayvseaasts wlqehvadls
      181 rslcgiipgl ssiflprmnp fvlidlagaf alcitymlie innyfavdta saiaialmtf
      241 gtmypmsvys gkvllqttpp hvigqldkli revstldgvl evrnehfwtl gfgslagsvh
      301 vrirrdaneq mvlahvtnrl ytlvstltvq ifkddwirpa llsgpvaanv lnfsdhhvip
      361 mpllkgtddl npvtstpakp sspppefsfn tpgknvnpvi llntqtrpyg fglnhghtpy
      421 ssmlnqglgv pgigatqglr tgftnipsry gtnnrigqpr p
//
LOCUS       NP_001357118             640 aa            linear   PRI 20-NOV-2025
DEFINITION  transforming growth factor beta activator LRRC32 isoform b [Homo
            sapiens].
ACCESSION   NP_001357118 XP_005273960
VERSION     NP_001357118.1
DBSOURCE    REFSEQ: accession NM_001370189.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 640)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 640)
  AUTHORS   Ma,J., Chen,Y., Li,T., Cao,Y., Hu,B., Liu,Y., Zhang,Y., Li,X.,
            Liu,J., Zhang,W., Niu,H., Gao,J., Zhang,Z., Yue,K., Wang,J.,
            Bao,G., Wang,C., Wang,P.G., Zou,T. and Xie,S.
  TITLE     Suppression of lysosome metabolism-meditated GARP/TGF-beta1
            complexes specifically depletes regulatory T cells to inhibit
            breast cancer metastasis
  JOURNAL   Oncogene 43 (25), 1930-1940 (2024)
   PUBMED   38698265
  REMARK    GeneRIF: Suppression of lysosome metabolism-meditated
            GARP/TGF-beta1 complexes specifically depletes regulatory T cells
            to inhibit breast cancer metastasis.
REFERENCE   3  (residues 1 to 640)
  AUTHORS   Zhang,X., Sharma,P., Maschmeyer,P., Hu,Y., Lou,M., Kim,J.,
            Fujii,H., Unutmaz,D., Schwabe,R.F. and Winau,F.
  TITLE     GARP on hepatic stellate cells is essential for the development of
            liver fibrosis
  JOURNAL   J Hepatol 79 (5), 1214-1225 (2023)
   PUBMED   37348791
  REMARK    GeneRIF: GARP on hepatic stellate cells is essential for the
            development of liver fibrosis.
REFERENCE   4  (residues 1 to 640)
  AUTHORS   Cai,H., Liu,Y., Dong,X., Jiang,F., Li,H., Ouyang,S., Yin,W., He,T.,
            Zeng,Q. and Yang,H.
  TITLE     Analysis of LAP+ and GARP+ Treg subsets in peripheral blood of
            patients with neuromyelitis optica spectrum disorders
  JOURNAL   Neurol Sci 44 (5), 1739-1747 (2023)
   PUBMED   36683084
  REMARK    GeneRIF: Analysis of LAP[+] and GARP[+] Treg subsets in peripheral
            blood of patients with neuromyelitis optica spectrum disorders.
REFERENCE   5  (residues 1 to 640)
  AUTHORS   Lahimchi,M.R., Eslami,M. and Yousefi,B.
  TITLE     New insight into GARP striking role in cancer progression:
            application for cancer therapy
  JOURNAL   Med Oncol 40 (1), 33 (2022)
   PUBMED   36460874
  REMARK    GeneRIF: New insight into GARP striking role in cancer progression:
            application for cancer therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 640)
  AUTHORS   Macaulay,I.C., Tijssen,M.R., Thijssen-Timmer,D.C., Gusnanto,A.,
            Steward,M., Burns,P., Langford,C.F., Ellis,P.D., Dudbridge,F.,
            Zwaginga,J.J., Watkins,N.A., van der Schoot,C.E. and Ouwehand,W.H.
  TITLE     Comparative gene expression profiling of in vitro differentiated
            megakaryocytes and erythroblasts identifies novel activatory and
            inhibitory platelet membrane proteins
  JOURNAL   Blood 109 (8), 3260-3269 (2007)
   PUBMED   17192395
REFERENCE   7  (residues 1 to 640)
  AUTHORS   Maire,G., Forus,A., Foa,C., Bjerkehagen,B., Mainguene,C.,
            Kresse,S.H., Myklebost,O. and Pedeutour,F.
  TITLE     11q13 alterations in two cases of hibernoma: large heterozygous
            deletions and rearrangement breakpoints near GARP in 11q13.5
  JOURNAL   Genes Chromosomes Cancer 37 (4), 389-395 (2003)
   PUBMED   12800150
REFERENCE   8  (residues 1 to 640)
  AUTHORS   Roubin,R., Pizette,S., Ollendorff,V., Planche,J., Birnbaum,D. and
            Delapeyriere,O.
  TITLE     Structure and developmental expression of mouse Garp, a gene
            encoding a new leucine-rich repeat-containing protein
  JOURNAL   Int J Dev Biol 40 (3), 545-555 (1996)
   PUBMED   8840187
REFERENCE   9  (residues 1 to 640)
  AUTHORS   Ollendorff,V., Noguchi,T., deLapeyriere,O. and Birnbaum,D.
  TITLE     The GARP gene encodes a new member of the family of leucine-rich
            repeat-containing proteins
  JOURNAL   Cell Growth Differ 5 (2), 213-219 (1994)
   PUBMED   8180135
REFERENCE   10 (residues 1 to 640)
  AUTHORS   Ollendorff,V., Szepetowski,P., Mattei,M.G., Gaudray,P. and
            Birnbaum,D.
  TITLE     New gene in the homologous human 11q13-q14 and mouse 7F chromosomal
            regions
  JOURNAL   Mamm Genome 2 (3), 195-200 (1992)
   PUBMED   1543912
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001189.5 and KF455417.1.
            
            On May 2, 2019 this sequence version replaced XP_005273960.2.
            
            Summary: This gene encodes a type I membrane protein which contains
            20 leucine-rich repeats. Alterations in the chromosomal region
            11q13-11q14 are involved in several pathologies. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.206164.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..640
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.5"
     Protein         1..640
                     /product="transforming growth factor beta activator LRRC32
                     isoform b"
                     /note="garpin; glycoprotein A repetitions predominant;
                     leucine-rich repeat-containing protein 32; transforming
                     growth factor beta activator LRRC32"
                     /calculated_mol_wt=69466
     Region          7..255
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Site            order(9,11,14,16,29,32,34,37,39,53,56,58,61,63,77,80,82,
                     85,87,104,107,109,112,114,129,132,134,137,139,153,156,158,
                     161,163,177,180,182,185,187,198,201,203,206,208,223,226,
                     228,231,233,245,248,250,253,255)
                     /site_type="active"
                     /note="Leucine-rich repeats [active]"
                     /db_xref="CDD:238064"
     Region          9..28
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            order(12..13,60,111,136,184,202,204,227,249)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:238064"
     Region          29..52
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          53..76
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          77..103
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          104..128
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          129..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          177..197
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          198..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          223..244
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          268..>552
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          295..318
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          319..342
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          343..365
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          366..389
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          390..422
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          423..441
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          446..470
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          471..493
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          <474..632
                     /region_name="PLN03150"
                     /note="hypothetical protein; Provisional"
                     /db_xref="CDD:178695"
     Region          494..515
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          516..537
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          541..553
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     CDS             1..640
                     /gene="LRRC32"
                     /gene_synonym="CPPRDD; D11S833E; GARP"
                     /coded_by="NM_001370189.1:271..2193"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="GeneID:2615"
                     /db_xref="HGNC:HGNC:4161"
                     /db_xref="MIM:137207"
ORIGIN      
        1 mlcpdrvdkk vscqvlgllq vpsvlppdte tldlsgnqlr silasplgfy talrhldlst
       61 neisflqpga fqalthlehl slahnrlama talsagglgp lprvtsldls gnslysglle
      121 rllgeapslh tlslaenslt rltrhtfrdm paleqldlhs nvlmdiedga feglprlthl
      181 nlsrnsltci sdfslqqlrv ldlscnsiea fqtasqpqae fqltwldlre nkllhfpdla
      241 alprliylnl snnlirlptg ppqdskgiha psegwsalpl sapsgnasgr plsqllnldl
      301 syneielipd sflehltslc flnlsrnclr tfearrlgsl pclmlldlsh naletlelga
      361 ralgslrtll lqgnalrdlp pytfanlasl qrlnlqgnrv spcggpdepg psgcvafsgi
      421 tslrslslvd neiellraga flhtplteld lssnpgleva tgalggleas levlalqgng
      481 lmvlqvdlpc ficlkrlnla enrlshlpaw tqavslevld lrnnsfsllp gsamgglets
      541 lrrlylqgnp lsccgngwla aqlhqgrvdv datqdlicrf ssqeevslsh vrpedcekgg
      601 lkninliiil tfilvsaill ttlaacccvr rqkfnqqyka
//
LOCUS       NP_002783                248 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-7 [Homo sapiens].
ACCESSION   NP_002783
VERSION     NP_002783.1
DBSOURCE    REFSEQ: accession NM_002792.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 248)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 248)
  AUTHORS   Sheng,G., Li,F., Jin,W. and Wang,K.
  TITLE     Pan-caner analysis identifies PSMA7 as a targets for amplification
            at 20q13.33 in tumorigenesis
  JOURNAL   Sci Rep 14 (1), 3034 (2024)
   PUBMED   38321088
  REMARK    GeneRIF: Pan-caner analysis identifies PSMA7 as a targets for
            amplification at 20q13.33 in tumorigenesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 248)
  AUTHORS   Xu,X., Pei,M., Kim,K.Y., Xi,H., Lee,S.G., Chung,K.Y., Roh,M.R. and
            Jin,Z.
  TITLE     Proteasome Subunit Alpha Type-7 Expression Suppresses Cutaneous
            Squamous Cell Carcinoma Progression by Inhibiting Cancer-associated
            Cytokines
  JOURNAL   In Vivo 37 (4), 1584-1592 (2023)
   PUBMED   37369480
  REMARK    GeneRIF: Proteasome Subunit Alpha Type-7 Expression Suppresses
            Cutaneous Squamous Cell Carcinoma Progression by Inhibiting
            Cancer-associated Cytokines.
REFERENCE   4  (residues 1 to 248)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   5  (residues 1 to 248)
  AUTHORS   Du,H., Huang,X., Wang,S., Wu,Y., Xu,W. and Li,M.
  TITLE     PSMA7, a potential biomarker of diseases
  JOURNAL   Protein Pept Lett 16 (5), 486-489 (2009)
   PUBMED   19442227
  REMARK    Review article
REFERENCE   6  (residues 1 to 248)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   7  (residues 1 to 248)
  AUTHORS   Huang,J., Kwong,J., Sun,E.C. and Liang,T.J.
  TITLE     Proteasome complex as a potential cellular target of hepatitis B
            virus X protein
  JOURNAL   J Virol 70 (8), 5582-5591 (1996)
   PUBMED   8764072
REFERENCE   8  (residues 1 to 248)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   9  (residues 1 to 248)
  AUTHORS   Akioka,H., Forsberg,N.E., Ishida,N., Okumura,K., Nogami,M.,
            Taguchi,H., Noda,C. and Tanaka,K.
  TITLE     Isolation and characterization of the HC8 subunit gene of the human
            proteasome
  JOURNAL   Biochem Biophys Res Commun 207 (1), 318-323 (1995)
   PUBMED   7857283
REFERENCE   10 (residues 1 to 248)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG575009.1, AF054185.1 and
            BU632089.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. Proteasomes are
            distributed throughout eukaryotic cells at a high concentration and
            cleave peptides in an ATP/ubiquitin-dependent process in a
            non-lysosomal pathway. This gene encodes a member of the peptidase
            T1A family that functions as a 20S core alpha subunit. The encoded
            protein interacts with the hepatitis B virus X protein and plays a
            role in regulating hepatitis C virus internal ribosome entry site
            (IRES) activity, an activity essential for viral replication. The
            encoded protein also plays a role in the cellular stress response
            by regulating hypoxia-inducible factor-1alpha. A pseudogene of this
            gene is located on the long arm of chromosome 9. [provided by
            RefSeq, Jul 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.498155.1,
                                           SRR1163657.409375.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370873.9/ ENSP00000359910.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..248
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..248
                     /product="proteasome subunit alpha type-7"
                     /EC_number="3.4.25.1"
                     /note="proteasome subunit alpha 4; proteasome subunit
                     RC6-1; proteasome subunit XAPC7; proteasome subunit alpha
                     7; proteasome (prosome, macropain) subunit, alpha type, 7;
                     alpha-4; epididymis secretory protein Li 276; testicular
                     tissue protein Li 151"
                     /calculated_mol_wt=27756
     Region          3..211
                     /region_name="proteasome_alpha_type_7"
                     /note="The 20S proteasome, multisubunit proteolytic
                     complex, is the central enzyme of nonlysosomal protein
                     degradation in both the cytosol and nucleus. It is
                     composed of 28 subunits arranged as four homoheptameric
                     rings that stack on top of one another forming...;
                     cd03755"
                     /db_xref="CDD:239724"
     Site            order(5..8,10..11,13..14,18,21,24..25,28,36,51,53..54,
                     77..79,81..82,113,116,119..120,123..127,145,150..151,153,
                     155..156,158)
                     /site_type="other"
                     /note="alpha subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239724"
     Site            order(30,46,48,61,163)
                     /site_type="active"
                     /db_xref="CDD:239724"
     Site            130
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (O14818.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and ABL2.
                     /evidence=ECO:0000269|PubMed:16678104; propagated from
                     UniProtKB/Swiss-Prot (O14818.1)"
     Site            227
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O14818.1)"
     CDS             1..248
                     /gene="PSMA7"
                     /gene_synonym="C6; HEL-S-276; HSPC; RC6-1; XAPC7"
                     /coded_by="NM_002792.4:92..838"
                     /db_xref="CCDS:CCDS13489.1"
                     /db_xref="GeneID:5688"
                     /db_xref="HGNC:HGNC:9536"
                     /db_xref="MIM:606607"
ORIGIN      
        1 msydraitvf spdghlfqve yaqeavkkgs tavgvrgrdi vvlgvekksv aklqdertvr
       61 kicalddnvc mafagltada rivinrarve cqshrltved pvtveyitry iaslkqrytq
      121 sngrrpfgis alivgfdfdg tprlyqtdps gtyhawkana igrgaksvre fleknytdea
      181 ietddltikl vikallevvq sggknielav mrrdqslkil npeeiekyva eiekekeene
      241 kkkqkkas
//
LOCUS       NP_001335141             537 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform i [Homo sapiens].
ACCESSION   NP_001335141
VERSION     NP_001335141.1
DBSOURCE    REFSEQ: accession NM_001348212.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 537)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 537)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 537)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 537)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 537)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 537)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 537)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 537)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 537)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 537)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC358599.1, AK300612.1 and
            AC091103.4.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (18) differs in the 5' UTR, lacks
            a portion of the 5' coding region, initiates translation at a
            downstream start codon, and uses an alternate in-frame splice site
            in the 3' coding region, compared to variant 3. The resulting
            isoform (i) is shorter at the N-terminus and lacks a small internal
            segment compared to isoform c. Variants 9 and 18 encode the same
            isoform (i).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.191556.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..537
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..537
                     /product="transcription factor 4 isoform i"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=57294
     Region          428..512
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(436,440,442..444,446,451,472..473)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(449..450,453..454,456..457,460,464,474,477,481,484,
                     487..492)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..537
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001348212.2:190..1803"
                     /note="isoform i is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS58626.1"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mdmgnpgtls ptkpgsqyyq yssnnprrrp lhssamevqt kkvrkvppgl pssvyapsas
       61 tadynrdspg ypsskpatst fpssffmqdg hhssdpwsss sgmnqpgyag mlgnsshipq
      121 sssycslhph erlsypshss adinsslppm stfhrsgtnh ystssctppa ngtdsimanr
      181 gsgaagssqt gdalgkalas iyspdhtnns fssnpstpvg sppslsagta vwsrnggqas
      241 sspnyegplh slqsriedrl erlddaihvl rnhavgpsta mpgghgdmhg iigpshngam
      301 gglgsgygtg llsanrhslm vgthredgva lrgshsllpn qvpvpqlpvq satspdlnpp
      361 qdpyrgmppg lqgqsvssgs seiksddegd enlqdtksse dkkldddkkd iksitsnndd
      421 edltpeqkae rekerrmann arerlrvrdi neafkelgrm vqlhlksdkp qtkllilhqa
      481 vavilsleqq vrernlnpka aclkrreeek vsseppplsl agphpgmgda snhmgqm
//
LOCUS       NP_001310868             920 aa            linear   PRI 20-NOV-2025
DEFINITION  DIS3-like exonuclease 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001310868
VERSION     NP_001310868.1
DBSOURCE    REFSEQ: accession NM_001323939.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 920)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 920)
  AUTHORS   Huntzinger,E., Sinteff,J., Morlet,B. and Seraphin,B.
  TITLE     HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of
            the RNB family is expressed from a non-canonical initiation codon
  JOURNAL   Nucleic Acids Res 51 (17), 9279-9293 (2023)
   PUBMED   37602378
REFERENCE   3  (residues 1 to 920)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 920)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 920)
  AUTHORS   Lee,J.Y., Moon,S., Kim,Y.K., Lee,S.H., Lee,B.S., Park,M.Y.,
            Park,J.E., Jang,Y. and Han,B.G.
  TITLE     Genome-based exome sequencing analysis identifies GYG1, DIS3L and
            DDRGK1 are associated with myocardial infarction in Koreans
  JOURNAL   J Genet 96 (6), 1041-1046 (2017)
   PUBMED   29321365
  REMARK    GeneRIF: we screened the susceptibility loci for Myocardial
            infarction (MI) using exome sequencing and validated candidate
            variants in replication sets. We identified that three genes (GYG1,
            DIS3L and DDRGK1) were associated with MI at the discovery and
            replication stages.
REFERENCE   6  (residues 1 to 920)
  AUTHORS   Li,L., Fridley,B.L., Kalari,K., Niu,N., Jenkins,G., Batzler,A.,
            Abo,R.P., Schaid,D. and Wang,L.
  TITLE     Discovery of genetic biomarkers contributing to variation in drug
            response of cytidine analogues using human lymphoblastoid cell
            lines
  JOURNAL   BMC Genomics 15, 93 (2014)
   PUBMED   24483146
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 920)
  AUTHORS   Lubas,M., Damgaard,C.K., Tomecki,R., Cysewski,D., Jensen,T.H. and
            Dziembowski,A.
  TITLE     Exonuclease hDIS3L2 specifies an exosome-independent 3'-5'
            degradation pathway of human cytoplasmic mRNA
  JOURNAL   EMBO J 32 (13), 1855-1868 (2013)
   PUBMED   23756462
REFERENCE   8  (residues 1 to 920)
  AUTHORS   Staals,R.H., Bronkhorst,A.W., Schilders,G., Slomovic,S.,
            Schuster,G., Heck,A.J., Raijmakers,R. and Pruijn,G.J.
  TITLE     Dis3-like 1: a novel exoribonuclease associated with the human
            exosome
  JOURNAL   EMBO J 29 (14), 2358-2367 (2010)
   PUBMED   20531389
  REMARK    GeneRIF: Data indicate that hDis3L1 is a novel exosome-associated
            exoribonuclease in the cytoplasm of human cells.
REFERENCE   9  (residues 1 to 920)
  AUTHORS   Tomecki,R., Kristiansen,M.S., Lykke-Andersen,S., Chlebowski,A.,
            Larsen,K.M., Szczesny,R.J., Drazkowska,K., Pastula,A.,
            Andersen,J.S., Stepien,P.P., Dziembowski,A. and Jensen,T.H.
  TITLE     The human core exosome interacts with differentially localized
            processive RNases: hDIS3 and hDIS3L
  JOURNAL   EMBO J 29 (14), 2342-2357 (2010)
   PUBMED   20531386
  REMARK    GeneRIF: Data show that hDIS3 and hDIS3L are active exonucleases,
            but only hDIS3 has retained endonucleolytic activity, and suggest
            that three different ribonucleases can serve as catalytic subunits
            for the exosome in human cells.
REFERENCE   10 (residues 1 to 920)
  AUTHORS   Slomovic,S., Fremder,E., Staals,R.H., Pruijn,G.J. and Schuster,G.
  TITLE     Addition of poly(A) and poly(A)-rich tails during RNA degradation
            in the cytoplasm of human cells
  JOURNAL   Proc Natl Acad Sci U S A 107 (16), 7407-7412 (2010)
   PUBMED   20368444
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC055855.9.
            
            Summary: The cytoplasmic RNA exosome complex degrades unstable
            mRNAs and is involved in the regular turnover of other mRNAs. The
            protein encoded by this gene contains 3'-5' exoribonuclease
            activity and is a catalytic component of this complex. [provided by
            RefSeq, May 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.56410.1,
                                           SRR1803616.228445.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..920
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..920
                     /product="DIS3-like exonuclease 1 isoform 3"
                     /EC_number="3.1.13.1"
                     /note="DIS3-like exonuclease 1; DIS3 mitotic control
                     homolog-like"
                     /calculated_mol_wt=104881
     Region          <1..54
                     /region_name="PIN_SF"
                     /note="PIN (PilT N terminus) domain: Superfamily; cl28905"
                     /db_xref="CDD:475124"
     Region          104..732
                     /region_name="VacB"
                     /note="Exoribonuclease R [Transcription]; COG0557"
                     /db_xref="CDD:440323"
     Region          747..822
                     /region_name="Rrp44_S1"
                     /note="S1 domain; pfam17215"
                     /db_xref="CDD:435792"
     CDS             1..920
                     /gene="DIS3L"
                     /gene_synonym="DIS3L1"
                     /coded_by="NM_001323939.2:556..3318"
                     /note="isoform 3 is encoded by transcript variant 6"
                     /db_xref="GeneID:115752"
                     /db_xref="HGNC:HGNC:28698"
                     /db_xref="MIM:614183"
ORIGIN      
        1 mekwqtrsiy naavwyyhhc qdrmpivmvt edeeaiqqyg setegvfvit fknyldnfwp
       61 dlkaahelcd silqsrrere nesqeshgke ypehlplevl eagiksgryi qgilnvnkhr
      121 aqieafvrlq gasskdsdlv sdilihgmka rnrsihgdvv vvellpknew kgrtvalcen
      181 dcddkasges psepmptgrv vgilqknwrd yvvtfpskee vqsqgknaqk ilvtpwdyri
      241 pkiristqqa etlqdfrvvv ridswestsv ypnghfvrvl grigdlegei atilvensis
      301 vipfseaqmc empvntpesp wkvspeeeqk rkdlrkshlv fsidpkgced vddtlsvrtl
      361 nngnlelgvh iadvthfvap nsyidieart rattyyladr rydmlpsvls adlcsllggv
      421 dryavsimwe ldkasyeikk vwygrtiirs ayklfyeaaq elldgnlsvv ddipefkdld
      481 eksrqaklee lvwaigkltd iarhvrakrd gcgalelegv evcvqlddkk nihdlipkqp
      541 levhetvaec milanhwvak kiwesfphqa llrqhppphq effselreca kakgffidtr
      601 snktladsld nandphdpiv nrllrsmatq amsnalyfst gscaeeefhh yglaldkyth
      661 ftspirrysd ivvhrllmaa iskdkkmeik gnlfsnkdle elcrhinnrn qaaqhsqkqs
      721 telfqcmyfk dkdpateerc isdgviysir tngvllfipr fgikgaaylk nkdglviscg
      781 pdscsewkpg slqrfqnkit stttdgesvt fhlfdhvtvr isiqasrchs dtirleiisn
      841 kpykipntel ihqsspllks elvkevtksv eeaqlaqevk vniiqeeyqe yrqtkgrsly
      901 tlleeirdla lldvsnnygi
//
LOCUS       NP_001336349             600 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform b [Homo sapiens].
ACCESSION   NP_001336349 XP_005247610
VERSION     NP_001336349.1
DBSOURCE    REFSEQ: accession NM_001349420.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 600)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 600)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 600)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 600)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 600)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 600)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 600)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 600)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_005247610.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (9), as well as variants 7, 8, and
            10-15, encodes isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.47657.1,
                                           SRR1660807.149279.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..600
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..600
                     /product="kelch-like protein 24 isoform b"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=68230
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          314..363
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          365..407
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          397..441
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          408..454
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          444..489
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          456..502
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          492..529
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          504..544
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     Region          536..578
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          545..591
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     Region          546..592
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6TFL4.1)"
     CDS             1..600
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349420.1:341..2143"
                     /note="isoform b is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS3246.1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkvy vvggydgqnr
      421 lssvecydsf snrwtevapl keavsspavt scvgklfvig ggpddntcsd kvqsydpetn
      481 swllraaipi akrcitavsl nnliyvaggl tkaiycydpv edywmhvqnt fsrqencgms
      541 vcngkiyilg grrengeatd tilcydpats iitgvaampr pvsyhgcvti hrynekcfkl
//
LOCUS       NP_001035829             534 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein RO60 isoform 3 [Homo sapiens].
ACCESSION   NP_001035829
VERSION     NP_001035829.2
DBSOURCE    REFSEQ: accession NM_001042370.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Song,Y., Wei,F., Liu,Y., Han,F., Ma,L., Zhuang,Y., Pan,C., Jia,Z.
            and Gong,A.
  TITLE     IL-33/ST2 Activation Is involved in Ro60-Regulated Photosensitivity
            in Cutaneous Lupus Erythematosus
  JOURNAL   Mediators Inflamm 2022, 4955761 (2022)
   PUBMED   35909659
  REMARK    GeneRIF: IL-33/ST2 Activation Is involved in Ro60-Regulated
            Photosensitivity in Cutaneous Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Lee,A.Y.S., Beroukas,D., Brown,L., Lucchesi,C., Kaur,A., Gyedu,L.,
            Hughes,N., Ng,Y.H., Saran,O., Gordon,T.P. and Wang,J.J.
  TITLE     Identification of a unique anti-Ro60 subset with restricted
            serological and molecular profiles
  JOURNAL   Clin Exp Immunol 203 (1), 13-21 (2021)
   PUBMED   32852779
  REMARK    GeneRIF: Identification of a unique anti-Ro60 subset with
            restricted serological and molecular profiles.
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Leng,Y., Sim,S., Magidson,V. and Wolin,S.L.
  TITLE     Noncoding Y RNAs regulate the levels, subcellular distribution and
            protein interactions of their Ro60 autoantigen partner
  JOURNAL   Nucleic Acids Res 48 (12), 6919-6930 (2020)
   PUBMED   32469055
  REMARK    GeneRIF: Noncoding Y RNAs regulate the levels, subcellular
            distribution and protein interactions of their Ro60 autoantigen
            partner.
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Barcellos,K.S., Nonogaki,S., Enokihara,M.M., Teixeira,M.S. and
            Andrade,L.E.
  TITLE     Differential expression of Ro/SSA 60 kDa and La/SSB, but not Ro/SSA
            52 kDa, mRNA and protein in minor salivary glands from patients
            with primary Sjogren's syndrome
  JOURNAL   J Rheumatol 34 (6), 1283-1292 (2007)
   PUBMED   17552056
  REMARK    GeneRIF: Increased Ro/SSA 60 and La/SSB mRNA expression in minor
            salivary glands in primary Sjogren's syndrome (pSS) suggest that
            these 2 autoantigens, but not Ro/SSA 52, are involved in
            tissue-specific autoimmune response in pSS.
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Pruijn,G.J., Slobbe,R.L. and van Venrooij,W.J.
  TITLE     Analysis of protein--RNA interactions within Ro ribonucleoprotein
            complexes
  JOURNAL   Nucleic Acids Res 19 (19), 5173-5180 (1991)
   PUBMED   1833722
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Jitsukawa,T., Nakajima,S., Usui,J. and Watanabe,H.
  TITLE     Detection of anti-nuclear antibodies from patients with systemic
            rheumatic diseases by ELISA using HEp-2 cell nuclei
  JOURNAL   J Clin Lab Anal 5 (1), 49-53 (1991)
   PUBMED   1999763
REFERENCE   8  (residues 1 to 534)
  AUTHORS   James,J.A., Dickey,W.D., Fujisaku,A., O'Brien,C.A., Deutscher,S.L.,
            Keene,J.D. and Harley,J.B.
  TITLE     Antigenicity of a recombinant Ro (SS-A) fusion protein
  JOURNAL   Arthritis Rheum 33 (1), 102-106 (1990)
   PUBMED   1689160
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Ben-Chetrit,E., Gandy,B.J., Tan,E.M. and Sullivan,K.F.
  TITLE     Isolation and characterization of a cDNA clone encoding the 60-kD
            component of the human SS-A/Ro ribonucleoprotein autoantigen
  JOURNAL   J Clin Invest 83 (4), 1284-1292 (1989)
   PUBMED   2649513
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Deutscher,S.L., Harley,J.B. and Keene,J.D.
  TITLE     Molecular analysis of the 60-kDa human Ro ribonucleoprotein
  JOURNAL   Proc Natl Acad Sci U S A 85 (24), 9479-9483 (1988)
   PUBMED   3200833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX761715.1, AY205315.1, AL136370.4 and AI433657.1.
            
            On Mar 16, 2010 this sequence version replaced NP_001035829.1.
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the 3' coding region, which results in a frameshift, compared to
            variant 1. It encodes isoform 3, which has a longer and distinct
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY205315.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.2"
     Protein         1..534
                     /product="RNA-binding protein RO60 isoform 3"
                     /note="Sjogren syndrome antigen A2 (60kD,
                     ribonucleoprotein autoantigen SS-A/Ro); gastric cancer
                     multi-drug resistance protein; TROVE domain family member
                     2; 60 kDa ribonucleoprotein Ro; sjoegren syndrome type A
                     antigen; Ro/SSA 60kDa; ro60 autoantigen; RNA-binding
                     protein RO60"
                     /calculated_mol_wt=60038
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          17..369
                     /region_name="TROVE"
                     /note="TROVE domain; pfam05731"
                     /db_xref="CDD:461724"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          120..284
                     /region_name="RNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          <363..489
                     /region_name="ViaA"
                     /note="Uncharacterized conserved protein, contains a von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG2425"
                     /db_xref="CDD:441973"
     CDS             1..534
                     /gene="RO60"
                     /gene_synonym="RORNP; SSA2; TROVE2"
                     /coded_by="NM_001042370.2:371..1975"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS41450.2"
                     /db_xref="GeneID:6738"
                     /db_xref="HGNC:HGNC:11313"
                     /db_xref="MIM:600063"
ORIGIN      
        1 meesvnqmqp lnekqiansq dgyvwqvtdm nrlhrflcfg seggtyyike qklglenaea
       61 lirliedgrg ceviqeiksf sqegrttkqe pmlfalaics qcsdistkqa afkavsevcr
      121 ipthlftfiq fkkdlkesmk cgmwgralrk aiadwynekg gmalalavtk ykqrngwshk
      181 dllrlshlkp sseglaivtk yitkgwkevh elykekalsv etekllkyle avekvkrtrd
      241 elevihliee hrlvrehllt nhlkskevwk allqemplta llrnlgkmta nsvlepgnse
      301 vslvceklcn ekllkkarih pfhilialet yktghglrgk lkwrpdeeil kaldaafykt
      361 fktveptgkr fllavdvsas mnqrvlgsil nastvaaamc mvvtrtekds yvvafsdemv
      421 pcpvttdmtl qqvlmamsqi paggtdcslp miwaqktntp advfivftdn etfaggvhpa
      481 ialreyrkkm dipaklivcg mtsngftiad pddrgmldmc gfdtgaldpc kipy
//
LOCUS       NP_001356709             232 aa            linear   PRI 20-NOV-2025
DEFINITION  protein lin-37 homolog isoform 2 [Homo sapiens].
ACCESSION   NP_001356709
VERSION     NP_001356709.1
DBSOURCE    REFSEQ: accession NM_001369780.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 232)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 232)
  AUTHORS   Uxa,S., Bernhart,S.H., Mages,C.F.S., Fischer,M., Kohler,R.,
            Hoffmann,S., Stadler,P.F., Engeland,K. and Muller,G.A.
  TITLE     DREAM and RB cooperate to induce gene repression and cell-cycle
            arrest in response to p53 activation
  JOURNAL   Nucleic Acids Res 47 (17), 9087-9103 (2019)
   PUBMED   31400114
  REMARK    GeneRIF: Abrogation of DREAM function by knockout of the DREAM
            component LIN37 results in a reduced repression of cell-cycle
            genes.
REFERENCE   5  (residues 1 to 232)
  AUTHORS   Sadasivam,S. and DeCaprio,J.A.
  TITLE     The DREAM complex: master coordinator of cell cycle-dependent gene
            expression
  JOURNAL   Nat Rev Cancer 13 (8), 585-595 (2013)
   PUBMED   23842645
  REMARK    Review article
            Erratum:[Nat Rev Cancer. 2013 Oct;13(10):752]
REFERENCE   6  (residues 1 to 232)
  AUTHORS   Sadasivam,S., Duan,S. and DeCaprio,J.A.
  TITLE     The MuvB complex sequentially recruits B-Myb and FoxM1 to promote
            mitotic gene expression
  JOURNAL   Genes Dev 26 (5), 474-489 (2012)
   PUBMED   22391450
REFERENCE   7  (residues 1 to 232)
  AUTHORS   Litovchick,L., Florens,L.A., Swanson,S.K., Washburn,M.P. and
            DeCaprio,J.A.
  TITLE     DYRK1A protein kinase promotes quiescence and senescence through
            DREAM complex assembly
  JOURNAL   Genes Dev 25 (8), 801-813 (2011)
   PUBMED   21498570
REFERENCE   8  (residues 1 to 232)
  AUTHORS   Litovchick,L., Sadasivam,S., Florens,L., Zhu,X., Swanson,S.K.,
            Velmurugan,S., Chen,R., Washburn,M.P., Liu,X.S. and DeCaprio,J.A.
  TITLE     Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
            complex represses human cell cycle-dependent genes in quiescence
  JOURNAL   Mol Cell 26 (4), 539-551 (2007)
   PUBMED   17531812
REFERENCE   9  (residues 1 to 232)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 232)
  AUTHORS   Grimwood,J., Gordon,L.A., Olsen,A., Terry,A., Schmutz,J.,
            Lamerdin,J., Hellsten,U., Goodstein,D., Couronne,O.,
            Tran-Gyamfi,M., Aerts,A., Altherr,M., Ashworth,L., Bajorek,E.,
            Black,S., Branscomb,E., Caenepeel,S., Carrano,A., Caoile,C.,
            Chan,Y.M., Christensen,M., Cleland,C.A., Copeland,A., Dalin,E.,
            Dehal,P., Denys,M., Detter,J.C., Escobar,J., Flowers,D.,
            Fotopulos,D., Garcia,C., Georgescu,A.M., Glavina,T., Gomez,M.,
            Gonzales,E., Groza,M., Hammon,N., Hawkins,T., Haydu,L., Ho,I.,
            Huang,W., Israni,S., Jett,J., Kadner,K., Kimball,H., Kobayashi,A.,
            Larionov,V., Leem,S.H., Lopez,F., Lou,Y., Lowry,S., Malfatti,S.,
            Martinez,D., McCready,P., Medina,C., Morgan,J., Nelson,K.,
            Nolan,M., Ovcharenko,I., Pitluck,S., Pollard,M., Popkie,A.P.,
            Predki,P., Quan,G., Ramirez,L., Rash,S., Retterer,J., Rodriguez,A.,
            Rogers,S., Salamov,A., Salazar,A., She,X., Smith,D., Slezak,T.,
            Solovyev,V., Thayer,N., Tice,H., Tsai,M., Ustaszewska,A., Vo,N.,
            Wagner,M., Wheeler,J., Wu,K., Xie,G., Yang,J., Dubchak,I.,
            Furey,T.S., DeJong,P., Dickson,M., Gordon,D., Eichler,E.E.,
            Pennacchio,L.A., Richardson,P., Stubbs,L., Rokhsar,D.S.,
            Myers,R.M., Rubin,E.M. and Lucas,S.M.
  TITLE     The DNA sequence and biology of human chromosome 19
  JOURNAL   Nature 428 (6982), 529-535 (2004)
   PUBMED   15057824
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AD000671.1, AC002398.1, KC877720.1 and KC877725.1.
            
            Summary: This gene encodes a protein expressed in the eye.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (2) is
            shorter at the N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.267253.1,
                                           SRR7410570.653592.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..232
                     /product="protein lin-37 homolog isoform 2"
                     /note="protein F25965; protein lin-37 homolog;
                     antolefinin"
                     /calculated_mol_wt=26607
     Region          70..226
                     /region_name="LIN37"
                     /note="pfam15306"
                     /db_xref="CDD:464632"
     CDS             1..232
                     /gene="LIN37"
                     /gene_synonym="F25965; lin-37; ZK418.4"
                     /coded_by="NM_001369780.1:206..904"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:55957"
                     /db_xref="HGNC:HGNC:33234"
                     /db_xref="MIM:621287"
ORIGIN      
        1 makarnqlda vlqclleksh mdrerldeea gktpsdthnk dcsiaatgkr psarfphqrr
       61 kkrremddgl aeggpqrsnt yviklfdrsv dlaqfsentp lypicrawmr nspsvrerec
      121 spssplpplp edeegsevtn sksrdvyklp pptppgppgd acrsripspl qpemqgtpdd
      181 epsepepsps tliyrnmqrw krirqrwkea shrnqlryse smkilremye rq
//
LOCUS       NP_689853                617 aa            linear   PRI 20-NOV-2025
DEFINITION  mRNA-decapping enzyme 1B isoform 1 [Homo sapiens].
ACCESSION   NP_689853
VERSION     NP_689853.3
DBSOURCE    REFSEQ: accession NM_152640.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 617)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 617)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 617)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 617)
  AUTHORS   Na,Z., Luo,Y., Schofield,J.A., Smelyansky,S., Khitun,A.,
            Muthukumar,S., Valkov,E., Simon,M.D. and Slavoff,S.A.
  TITLE     The NBDY Microprotein Regulates Cellular RNA Decapping
  JOURNAL   Biochemistry 59 (42), 4131-4142 (2020)
   PUBMED   33059440
REFERENCE   5  (residues 1 to 617)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 617)
  AUTHORS   Tritschler,F., Braun,J.E., Motz,C., Igreja,C., Haas,G.,
            Truffault,V., Izaurralde,E. and Weichenrieder,O.
  TITLE     DCP1 forms asymmetric trimers to assemble into active mRNA
            decapping complexes in metazoa
  JOURNAL   Proc Natl Acad Sci U S A 106 (51), 21591-21596 (2009)
   PUBMED   19966221
REFERENCE   7  (residues 1 to 617)
  AUTHORS   Fenger-Gron,M., Fillman,C., Norrild,B. and Lykke-Andersen,J.
  TITLE     Multiple processing body factors and the ARE binding protein TTP
            activate mRNA decapping
  JOURNAL   Mol Cell 20 (6), 905-915 (2005)
   PUBMED   16364915
REFERENCE   8  (residues 1 to 617)
  AUTHORS   Lehner,B. and Sanderson,C.M.
  TITLE     A protein interaction framework for human mRNA degradation
  JOURNAL   Genome Res 14 (7), 1315-1323 (2004)
   PUBMED   15231747
REFERENCE   9  (residues 1 to 617)
  AUTHORS   Cougot,N., Babajko,S. and Seraphin,B.
  TITLE     Cytoplasmic foci are sites of mRNA decay in human cells
  JOURNAL   J Cell Biol 165 (1), 31-40 (2004)
   PUBMED   15067023
REFERENCE   10 (residues 1 to 617)
  AUTHORS   Lykke-Andersen,J.
  TITLE     Identification of a human decapping complex associated with hUpf
            proteins in nonsense-mediated decay
  JOURNAL   Mol Cell Biol 22 (23), 8114-8121 (2002)
   PUBMED   12417715
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AY146652.1, AK299203.1,
            BC015368.3 and AW204088.1.
            
            On Jan 2, 2004 this sequence version replaced NP_689853.2.
            
            Summary: This gene encodes a member of a family of proteins that
            function in removing the 5' cap from mRNAs, which is a step in
            regulated mRNA decay. This protein localizes to cytoplasmic foci
            which are the site of mRNA breakdown and turnover. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056200.1, SRR1660805.203232.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000280665.11/ ENSP00000280665.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..617
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.33"
     Protein         1..617
                     /product="mRNA-decapping enzyme 1B isoform 1"
                     /EC_number="3.6.1.62"
                     /note="decapping enzyme hDcp1b; mRNA-decapping enzyme 1B;
                     DCP1 decapping enzyme homolog B"
                     /calculated_mol_wt=67592
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          16..131
                     /region_name="Dcp1"
                     /note="mRNA decapping enzyme 1 (Dcp1); cd09804"
                     /db_xref="CDD:197362"
     Site            order(17,19..20,23..24,34,36,58,75..77,80,82)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:197362"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Site            191
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          195..222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          243..266
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Site            275
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          <279..576
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          362..426
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Site            448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Site            511
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZD4.2)"
     Region          574..615
                     /region_name="mRNA_decap_C"
                     /note="mRNA-decapping enzyme C-terminus; pfam16741"
                     /db_xref="CDD:465253"
     CDS             1..617
                     /gene="DCP1B"
                     /gene_synonym="DCP1"
                     /coded_by="NM_152640.5:27..1880"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31727.1"
                     /db_xref="GeneID:196513"
                     /db_xref="HGNC:HGNC:24451"
                     /db_xref="MIM:609843"
ORIGIN      
        1 maavaagglv gkgrdislaa lqrhdpyinr ivdvasqval ytfghranew ektdvegtlf
       61 vytrsaspkh gftimnrlsm enrtepitkd ldfqlqdpfl lyrnarlsiy giwfydkeec
      121 qriaelmknl tqyeqlkahq gtgagispvi lnsgegkevd ilrmlikakd eytkcktcse
      181 pkkitsssai ydnpnlikpi pvkpsenqqq ripqpnqtld pepqhlslta lfgkqdkatc
      241 qetveppqtl hqqqqqqqqq qeklpirqgv vrslsyeepr rhsppiekql cpaiqklmvr
      301 sadlhplsel penrpcengs thsagefftg pvqpgsphni gtsrgvqnas rtqnlfeklq
      361 stpgaankcd pstpapassa alnrsrapts vtpvapgkgl aqppqayfng slppqtvghq
      421 ahgreqstlp rqtlpisgsq tgssgvispq ellkklqivq qeqqlhasnr palaakfpvl
      481 aqssgtgkpl eswinktpnt eqqtplfqvi spqripataa psllmspmvf aqptsvppke
      541 resgllpvgg qeppaaatsl llpiqspeps vitsspltkl qlqeallyli qnddnflnii
      601 yeaylfsmtq aamkktm
//
LOCUS       NP_006833                895 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing factor 3B subunit 2 [Homo sapiens].
ACCESSION   NP_006833 XP_290506
VERSION     NP_006833.2
DBSOURCE    REFSEQ: accession NM_006842.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 895)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 895)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 895)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 895)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 895)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   6  (residues 1 to 895)
  AUTHORS   Das,B.K., Xia,L., Palandjian,L., Gozani,O., Chyung,Y. and Reed,R.
  TITLE     Characterization of a protein complex containing spliceosomal
            proteins SAPs 49, 130, 145, and 155
  JOURNAL   Mol Cell Biol 19 (10), 6796-6802 (1999)
   PUBMED   10490618
REFERENCE   7  (residues 1 to 895)
  AUTHORS   Neubauer,G., King,A., Rappsilber,J., Calvio,C., Watson,M., Ajuh,P.,
            Sleeman,J., Lamond,A. and Mann,M.
  TITLE     Mass spectrometry and EST-database searching allows
            characterization of the multi-protein spliceosome complex
  JOURNAL   Nat Genet 20 (1), 46-50 (1998)
   PUBMED   9731529
REFERENCE   8  (residues 1 to 895)
  AUTHORS   Agell,N., Aligue,R., Alemany,V., Castro,A., Jaime,M., Pujol,M.J.,
            Rius,E., Serratosa,J., Taules,M. and Bachs,O.
  TITLE     New nuclear functions for calmodulin
  JOURNAL   Cell Calcium 23 (2-3), 115-121 (1998)
   PUBMED   9601606
  REMARK    Review article
REFERENCE   9  (residues 1 to 895)
  AUTHORS   Gozani,O., Feld,R. and Reed,R.
  TITLE     Evidence that sequence-independent binding of highly conserved U2
            snRNP proteins upstream of the branch site is required for assembly
            of spliceosomal complex A
  JOURNAL   Genes Dev 10 (2), 233-243 (1996)
   PUBMED   8566756
REFERENCE   10 (residues 1 to 895)
  AUTHORS   Champion-Arnaud,P. and Reed,R.
  TITLE     The prespliceosome components SAP 49 and SAP 145 interact in a
            complex implicated in tethering U2 snRNP to the branch site
  JOURNAL   Genes Dev 8 (16), 1974-1983 (1994)
   PUBMED   7958871
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF311442.1, BC053577.1,
            BC014125.2, BE677116.1 and AP006287.2.
            
            On or before Nov 22, 2004 this sequence version replaced
            XP_290506.3, NP_006833.1.
            
            Summary: This gene encodes subunit 2 of the splicing factor 3b
            protein complex. Splicing factor 3b, together with splicing factor
            3a and a 12S RNA unit, forms the U2 small nuclear
            ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a
            complex binds pre-mRNA upstream of the intron's branch site in a
            sequence-independent manner and may anchor the U2 snRNP to the
            pre-mRNA. Splicing factor 3b is also a component of the minor
            U12-type spliceosome. Subunit 2 associates with pre-mRNA upstream
            of the branch site at the anchoring site. Subunit 2 also interacts
            directly with subunit 4 of the splicing factor 3b complex. Subunit
            2 is a highly hydrophilic protein with a proline-rich N-terminus
            and a glutamate-rich stretch in the C-terminus. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.488926.1,
                                           SRR7410570.488925.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000322535.11/ ENSP00000318861.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..895
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..895
                     /product="splicing factor 3B subunit 2"
                     /note="spliceosome associated protein 145; pre-mRNA
                     splicing factor SF3b 145 kDa subunit; SAP 145; splicing
                     factor 3b, subunit 2, 145kD; splicing factor 3b, subunit
                     2, 145kDa"
                     /calculated_mol_wt=100097
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Region          24..57
                     /region_name="SAP"
                     /note="SAP domain; pfam02037"
                     /db_xref="CDD:460424"
     Region          65..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Region          197..373
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            222
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            245
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            247
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            298
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Region          400..453
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Region          401..550
                     /region_name="Required for interaction with PRMT9.
                     /evidence=ECO:0000269|PubMed:25737013"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Region          <442..706
                     /region_name="CUS1"
                     /note="Splicing factor 3b, subunit 2 [RNA processing and
                     modification]; COG5182"
                     /db_xref="CDD:227509"
     Region          471..596
                     /region_name="DUF382"
                     /note="Domain of unknown function (DUF382); pfam04037"
                     /db_xref="CDD:461140"
     Site            508
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, by PRMT9, alternate.
                     /evidence=ECO:0000269|PubMed:25737013; Symmetric
                     dimethylarginine, by PRMT9, alternate.
                     /evidence=ECO:0000269|PubMed:25737013; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Site            515
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Region          691..757
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            780
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     Region          844..895
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13435.2)"
     Site            861
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13435.2)"
     CDS             1..895
                     /gene="SF3B2"
                     /gene_synonym="CFM; Cus1; HFM; SAP145; SF3b1; SF3B145;
                     SF3b150"
                     /coded_by="NM_006842.3:22..2709"
                     /db_xref="CCDS:CCDS31612.1"
                     /db_xref="GeneID:10992"
                     /db_xref="HGNC:HGNC:10769"
                     /db_xref="MIM:605591"
ORIGIN      
        1 matehpeppk aelqlppppp pghygawaaq elqaklaeig apiqgnreel verlqsytrq
       61 tgivlnrpvl rgedgdkaap ppmsaqlpgi pmpppplglp plqppppppp pppglglgfp
      121 mahppnlgpp pplrvgepva lseeerlkla qqqaallmqq eerakqqgdh slkehelleq
      181 qkraavlleq erqqeiakmg tpvprppqdm gqigvrtplg prvaapvgpv gptptvlpmg
      241 apvprprgpp pppgdenrem ddpsvgpkip qalekilqlk esrqeemnsq qeeeemetda
      301 rsslgqsase teedtvsvsk keknrkrrnr kkkkkpqrvr gvssessgdr ekdstrsrgs
      361 dspaadveie yvteepeiye pnfiffkrif eafkltddvk kekekepekl dklensaapk
      421 kkgfeeehkd sdddssddeq ekkpeapkls kkklrrmnrf tvaelkqlva rpdvvemhdv
      481 taqdpkllvh lkatrnsvpv prhwcfkrky lqgkrgiekp pfelpdfikr tgiqemreal
      541 qekeeqktmk skmrekvrpk mgkididyqk lhdaffkwqt kpkltihgdl yyegkefetr
      601 lkekkpgdls delrislgmp vgpnahkvpp pwliamqryg pppsypnlki pglnspipes
      661 csfgyhaggw gkppvdetgk plygdvfgtn aaefqtktee eeidrtpwge lepsdeesse
      721 eeeeeesded kpdetgfitp adsglitpgg fssvpagmet pelielrkkk ieeamdgset
      781 pqlftvlpek rtatvggamm gsthiydmst vmsrkgpape lqgvevalap eeleldpmam
      841 tqkyeehvre qqaqvekedf sdmvaehaak qkqkkrkaqp qdsrggskky kefkf
//
LOCUS       NP_079133               1844 aa            linear   PRI 20-NOV-2025
DEFINITION  ATPase family AAA domain-containing protein 5 [Homo sapiens].
ACCESSION   NP_079133 XP_947519 XP_951057
VERSION     NP_079133.3
DBSOURCE    REFSEQ: accession NM_024857.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1844)
  AUTHORS   Wang,F., He,Q., Yao,N.Y., O'Donnell,M.E. and Li,H.
  TITLE     The human ATAD5 has evolved unique structural elements to function
            exclusively as a PCNA unloader
  JOURNAL   Nat Struct Mol Biol 31 (11), 1680-1691 (2024)
   PUBMED   38871854
REFERENCE   2  (residues 1 to 1844)
  AUTHORS   Park,S.H., Kim,N., Kang,N., Ryu,E., Lee,E.A., Ra,J.S., Gartner,A.,
            Kang,S., Myung,K. and Lee,K.Y.
  TITLE     Short-range end resection requires ATAD5-mediated PCNA unloading
            for faithful homologous recombination
  JOURNAL   Nucleic Acids Res 51 (19), 10519-10535 (2023)
   PUBMED   37739427
  REMARK    GeneRIF: Short-range end resection requires ATAD5-mediated PCNA
            unloading for faithful homologous recombination.
REFERENCE   3  (residues 1 to 1844)
  AUTHORS   Itzkovich,Z., Choudhary,K., Arbel,M. and Kupiec,M.
  TITLE     Effects of Defective Unloading and Recycling of PCNA Revealed by
            the Analysis of ELG1 Mutants
  JOURNAL   Int J Mol Sci 24 (2), 1568 (2023)
   PUBMED   36675081
  REMARK    GeneRIF: Effects of Defective Unloading and Recycling of PCNA
            Revealed by the Analysis of ELG1 Mutants.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1844)
  AUTHORS   Park,S.H., Kim,Y., Ra,J.S., Wie,M.W., Kang,M.S., Kang,S., Myung,K.
            and Lee,K.Y.
  TITLE     Timely termination of repair DNA synthesis by ATAD5 is important in
            oxidative DNA damage-induced single-strand break repair
  JOURNAL   Nucleic Acids Res 49 (20), 11746-11764 (2021)
   PUBMED   34718749
  REMARK    GeneRIF: Timely termination of repair DNA synthesis by ATAD5 is
            important in oxidative DNA damage-induced single-strand break
            repair.
REFERENCE   5  (residues 1 to 1844)
  AUTHORS   Kim,S.J., Wie,M., Park,S.H., Kim,T.M., Park,J.H., Kim,S., Myung,K.
            and Lee,K.Y.
  TITLE     ATAD5 suppresses centrosome over-duplication by regulating UAF1 and
            ID1
  JOURNAL   Cell Cycle 19 (15), 1952-1968 (2020)
   PUBMED   32594826
  REMARK    GeneRIF: ATAD5 suppresses centrosome over-duplication by regulating
            UAF1 and ID1.
REFERENCE   6  (residues 1 to 1844)
  AUTHORS   Gudbjartsson,D.F., Walters,G.B., Thorleifsson,G., Stefansson,H.,
            Halldorsson,B.V., Zusmanovich,P., Sulem,P., Thorlacius,S.,
            Gylfason,A., Steinberg,S., Helgadottir,A., Ingason,A.,
            Steinthorsdottir,V., Olafsdottir,E.J., Olafsdottir,G.H.,
            Jonsson,T., Borch-Johnsen,K., Hansen,T., Andersen,G., Jorgensen,T.,
            Pedersen,O., Aben,K.K., Witjes,J.A., Swinkels,D.W., den Heijer,M.,
            Franke,B., Verbeek,A.L., Becker,D.M., Yanek,L.R., Becker,L.C.,
            Tryggvadottir,L., Rafnar,T., Gulcher,J., Kiemeney,L.A., Kong,A.,
            Thorsteinsdottir,U. and Stefansson,K.
  TITLE     Many sequence variants affecting diversity of adult human height
  JOURNAL   Nat Genet 40 (5), 609-615 (2008)
   PUBMED   18391951
REFERENCE   7  (residues 1 to 1844)
  AUTHORS   Douglas,J., Cilliers,D., Coleman,K., Tatton-Brown,K., Barker,K.,
            Bernhard,B., Burn,J., Huson,S., Josifova,D., Lacombe,D., Malik,M.,
            Mansour,S., Reid,E., Cormier-Daire,V., Cole,T. and Rahman,N.
  CONSRTM   Childhood Overgrowth Collaboration
  TITLE     Mutations in RNF135, a gene within the NF1 microdeletion region,
            cause phenotypic abnormalities including overgrowth
  JOURNAL   Nat Genet 39 (8), 963-965 (2007)
   PUBMED   17632510
REFERENCE   8  (residues 1 to 1844)
  AUTHORS   Ishii,H., Inageta,T., Mimori,K., Saito,T., Sasaki,H., Isobe,M.,
            Mori,M., Croce,C.M., Huebner,K., Ozawa,K. and Furukawa,Y.
  TITLE     Frag1, a homolog of alternative replication factor C subunits,
            links replication stress surveillance with apoptosis
  JOURNAL   Proc Natl Acad Sci U S A 102 (27), 9655-9660 (2005)
   PUBMED   15983387
  REMARK    GeneRIF: The Frag1 signal pathway, by linking replication stress
            surveillance with apoptosis induction, plays a central role in
            determining whether DNA damage is compatible with cell survival or
            whether it requires cell elimination by apoptosis.
REFERENCE   9  (residues 1 to 1844)
  AUTHORS   Jenne,D.E., Tinschert,S., Reimann,H., Lasinger,W., Thiel,G.,
            Hameister,H. and Kehrer-Sawatzki,H.
  TITLE     Molecular characterization and gene content of breakpoint
            boundaries in patients with neurofibromatosis type 1 with 17q11.2
            microdeletions
  JOURNAL   Am J Hum Genet 69 (3), 516-527 (2001)
   PUBMED   11468690
REFERENCE   10 (residues 1 to 1844)
  AUTHORS   Jenne,D.E., Tinschert,S., Stegmann,E., Reimann,H., Nurnberg,P.,
            Horn,D., Naumann,I., Buske,A. and Thiel,G.
  TITLE     A common set of at least 11 functional genes is lost in the
            majority of NF1 patients with gross deletions
  JOURNAL   Genomics 66 (1), 93-97 (2000)
   PUBMED   10843809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127024.4, AL832103.1, AJ314648.2, DR159473.1 and DB527289.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_947519.1, XP_951057.1, NP_079133.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AJ314648.2, AY557611.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321990.5/ ENSP00000313171.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1844
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..1844
                     /product="ATPase family AAA domain-containing protein 5"
                     /note="enhanced level of genomic instability 1 homolog;
                     chromosome fragility-associated gene 1 protein; chromosome
                     fragility associated gene 1"
                     /calculated_mol_wt=207440
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          178..204
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            354
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q4QY64; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          368..384
                     /region_name="Interaction with WDR48.
                     /evidence=ECO:0000269|PubMed:20147293"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          477..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          580..623
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            602
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            614
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          658..700
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            817
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          987..1047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1051..>1167
                     /region_name="PRK04195"
                     /note="replication factor C large subunit; Provisional"
                     /db_xref="CDD:235250"
     Region          1092..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Site            1116
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1203..1235
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1272..1292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1428..1432
                     /region_name="LXCXE motif"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1591..1635
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     Region          1630..1719
                     /region_name="Interaction with RAD51 and RFC5.
                     /evidence=ECO:0000269|PubMed:31844045"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96QE3.4)"
     CDS             1..1844
                     /gene="ATAD5"
                     /gene_synonym="C17orf41; ELG1; FRAG1"
                     /coded_by="NM_024857.5:383..5917"
                     /db_xref="CCDS:CCDS11260.1"
                     /db_xref="GeneID:79915"
                     /db_xref="HGNC:HGNC:25752"
                     /db_xref="MIM:609534"
ORIGIN      
        1 mvgvlamaaa aapppvkdce iepckkrkkd ddtstcktit kylsplgktr drvfappkps
       61 nildyfrkts ptnektqlgk eckikspesv pvdsnkdctt plemfsnvef kkkrkrvnls
      121 hqlnnikten eapieissdd skedyslnnd fvesstsvlr ykkqvevlae niqdtksqpn
      181 tmtslqnskk vnpkqgttkn dfkklrkrkc rdvvdlsesl plaeelnllk kdgkdtkqme
      241 nttshansrd nvteaaqlnd siitvsyeef lkshkenkve eipdstmsic vpsetvdeiv
      301 ksgyisesen seisqqvrfk tvtvlaqvhp ippkktgkip riflkqkqfe menslsdpen
      361 eqtvqkrksn vviqeeelel avleagssea vkpkctleer qqfmkafrqp asdalkngvk
      421 kssdkqkdln ekclyevgrd dnskkimens giqmvskngn lqlhtdkgsf lkeknkklkk
      481 knkktldtga ipgknregnt qkkettfflk ekqyqnrmsl rqrkteffks stlfnneslv
      541 yedianddll kvsslcnnnk lsrktsipvk dikltqskae seasllnvst pkstrrsgri
      601 sstpttetir gidsddvqdn sqlkastqka anlsekhsly taelitvpfd sespirmkft
      661 ristpkkskk ksnkrsekse atdggftsqi rkasntskni skakqlieka kalhisrskv
      721 teeiaiplrr ssrhqtlper kklsetedsv iiidssptal khpeknqkkl qclndvlgkk
      781 lntstknvpg kmkvaplflv rkaqkaadpv psfdessqdt seksqdcdvq ckakrdflms
      841 glpdllkrqi akkaaaldvy navstsfqrv vhvqqkddgc clwhlkppsc plltkfkeln
      901 tkvidlskcg ialgefstln sklksgnsaa vfmrtrkeft eevrnlllee irwsnpefsl
      961 kkyfplllkk qiehqvlsse chskqelead vshketkrkl veaenskskr kkpneysknl
     1021 ektnrkseel skrnnssgik ldsskdsgte dmlwtekyqp qtaseligne laikklhswl
     1081 kdwkrraele erqnlkgkrd ekhedfsggi dfkgssddee esrlcntvli tgptgvgkta
     1141 avyacaqelg fkifevnass qrsgrqilsq lkeatqshqv dkqgvnsqkp cffnsyyigk
     1201 spkkisspkk vvtsprkvpp pspkssgpkr alppktlany fkvspkpknn eeigmllenn
     1261 kgiknsfeqk qitqtkstna tnsnvkdvga eepsrknats lilfeevdvi fdedagflna
     1321 iktfmattkr pvilttsdpt fslmfdgcfe eikfstpsll nvasylqmic ltenfrtdvk
     1381 dfvtlltant cdirksilyl qfwirsgggv leerpltlyr gnsrnvqlvc sehgldnkiy
     1441 pkntkkkrvd lpkcdsgcae tlfglknifs psedlfsflk hkitmkeewh kfiqlltefq
     1501 mrnvdflysn lefilplpvd tipetknfcg psvtvdasaa tksmnclark hsereqplkk
     1561 sqkkkqkktl vilddsdlfd tdldfpdqsi slssvssssn aeesktgdee skardkgnnp
     1621 etkksipcpp kttagkkcsa lvshclnsls efmdnmsfld alltdvreqn kygrndfswt
     1681 ngkvtsglcd efslesndgw tsqssgelka aaealsftkc ssaiskalet lnsckklgrd
     1741 ptndltfyvs qkrnnvyfsq saanldnawk risviksvfs srsllyvgnr qasiieylpt
     1801 lrnicktekl keqgkskrrf lhyfegihld ipketvntla adfp
//
LOCUS       NP_060898                597 aa            linear   PRI 20-NOV-2025
DEFINITION  U3 small nucleolar RNA-associated protein 6 homolog [Homo sapiens].
ACCESSION   NP_060898
VERSION     NP_060898.2
DBSOURCE    REFSEQ: accession NM_018428.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 597)
  AUTHORS   Moraleva,A.A., Deryabin,A.S., Rubtsov,Y.P., Rubtsova,M.P. and
            Dontsova,O.A.
  TITLE     Eukaryotic Ribosome Biogenesis: The 40S Subunit
  JOURNAL   Acta Naturae 14 (1), 14-30 (2022)
   PUBMED   35441050
REFERENCE   2  (residues 1 to 597)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 597)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 597)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 597)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 597)
  AUTHORS   Venturin,M., Bentivegna,A., Moroni,R., Larizza,L. and Riva,P.
  TITLE     Evidence by expression analysis of candidate genes for congenital
            heart defects in the NF1 microdeletion interval
  JOURNAL   Ann Hum Genet 69 (Pt 5), 508-516 (2005)
   PUBMED   16138909
REFERENCE   7  (residues 1 to 597)
  AUTHORS   Andersen,J.S., Lam,Y.W., Leung,A.K., Ong,S.E., Lyon,C.E.,
            Lamond,A.I. and Mann,M.
  TITLE     Nucleolar proteome dynamics
  JOURNAL   Nature 433 (7021), 77-83 (2005)
   PUBMED   15635413
REFERENCE   8  (residues 1 to 597)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   9  (residues 1 to 597)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   10 (residues 1 to 597)
  AUTHORS   Jenne,D.E., Tinschert,S., Stegmann,E., Reimann,H., Nurnberg,P.,
            Horn,D., Naumann,I., Buske,A. and Thiel,G.
  TITLE     A common set of at least 11 functional genes is lost in the
            majority of NF1 patients with gross deletions
  JOURNAL   Genomics 66 (1), 93-97 (2000)
   PUBMED   10843809
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF334386.1, BC035325.1, BC015454.1 and AC004253.2.
            
            On Jul 1, 2004 this sequence version replaced NP_060898.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.209100.1,
                                           SRR1803613.129859.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000261708.9/ ENSP00000261708.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..597
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..597
                     /product="U3 small nucleolar RNA-associated protein 6
                     homolog"
                     /note="hepatocellular carcinoma-associated antigen 66;
                     multiple hat domains protein; UTP6, small subunit (SSU)
                     processome component, homolog"
                     /calculated_mol_wt=70063
     Region          1..>222
                     /region_name="COG5191"
                     /note="Uncharacterized conserved protein, contains HAT
                     (Half-A-TPR) repeat [General function prediction only]"
                     /db_xref="CDD:227518"
     Region          121..153
                     /region_name="HAT 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYH9.2)"
     Region          156..188
                     /region_name="HAT 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYH9.2)"
     Region          304..335
                     /region_name="HAT 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYH9.2)"
     Region          488..520
                     /region_name="HAT 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYH9.2)"
     Region          524..557
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NYH9.2)"
     CDS             1..597
                     /gene="UTP6"
                     /gene_synonym="C17orf40; HCA66"
                     /coded_by="NM_018428.3:82..1875"
                     /db_xref="CCDS:CCDS11269.1"
                     /db_xref="GeneID:55813"
                     /db_xref="HGNC:HGNC:18279"
                     /db_xref="MIM:620948"
ORIGIN      
        1 maeiiqerie drlpeleqle riglfshaei kaiikkasdl eykiqrrtlf kedfinyvqy
       61 einlleliqr rrtrigysfk kdeiensivh rvqgvfqras akwkddvqlw lsyvafckkw
      121 atktrlskvf samlaihsnk palwimaakw emedrlsses arqlflralr fhpecpklyk
      181 eyfrmelmha eklrkekeef ekasmdvenp dyseeilkge lawiiyknsv siikgaefhv
      241 sllsiaqlfd fakdlqkeiy ddlqalhtdd pltwdyvarr eleiesqtee qpttkqakav
      301 evgrkeercc avyeeavktl pteamwkcyi tfclerftkk snsgflrgkr lertmtvfrk
      361 ahelkllsec qykqlsvsll cynflreale vavagtelfr dsgtmwqlkl qvlieskspd
      421 iamlfeeafv hlkpqvclpl wiswaewseg aksqedteav fkkallavig adsvtlknky
      481 ldwayrsggy kkaravfksl qesrpfsvdf frkmiqfeke qescnmanir eyyeralref
      541 gsadsdlwmd ymkeelnhpl grpencgqiy wramkmlqge saeafvakha mhqtghl
//
LOCUS       NP_001355069             281 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-VI isoform 6 [Homo sapiens].
ACCESSION   NP_001355069
VERSION     NP_001355069.1
DBSOURCE    REFSEQ: accession NM_001368140.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 281)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109897.30 and AL136093.8.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (7), as well as variant 6, encodes
            isoform 6.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.1818900.1,
                                           SRR1803613.103576.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..281
                     /product="unconventional myosin-VI isoform 6"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=31610
     Region          71..>263
                     /region_name="Motor_domain"
                     /note="Myosin and Kinesin motor domain; cl22853"
                     /db_xref="CDD:473979"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     CDS             1..281
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_001368140.1:233..1078"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveanplle afgnaktvrn nnssrfgkfv eihfnekssv vggfvshyll eksricvqgk
      241 eernyhifyr lcagasedir eklhlsspdn frvgqkkrnf i
//
LOCUS       NP_001350903             159 aa            linear   PRI 20-NOV-2025
DEFINITION  calaxin isoform b [Homo sapiens].
ACCESSION   NP_001350903
VERSION     NP_001350903.1
DBSOURCE    REFSEQ: accession NM_001363974.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Hjeij,R., Aprea,I., Poeta,M., Nothe-Menchen,T., Bracht,D.,
            Raidt,J., Honecker,B.I., Dougherty,G.W., Olbrich,H., Schwartz,O.,
            Keller,U., Nusse,H., Diderich,K.E.M., Vogelberg,C., Santamaria,F.
            and Omran,H.
  TITLE     Pathogenic variants in CLXN encoding the outer dynein arm
            docking-associated calcium-binding protein calaxin cause primary
            ciliary dyskinesia
  JOURNAL   Genet Med 25 (5), 100798 (2023)
   PUBMED   36727596
  REMARK    GeneRIF: Pathogenic variants in CLXN encoding the outer dynein arm
            docking-associated calcium-binding protein calaxin cause primary
            ciliary dyskinesia.
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Braschi,B., Omran,H., Witman,G.B., Pazour,G.J., Pfister,K.K.,
            Bruford,E.A. and King,S.M.
  TITLE     Consensus nomenclature for dyneins and associated assembly factors
  JOURNAL   J Cell Biol 221 (2) (2022)
   PUBMED   35006274
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Gui,M., Farley,H., Anujan,P., Anderson,J.R., Maxwell,D.W.,
            Whitchurch,J.B., Botsch,J.J., Qiu,T., Meleppattu,S., Singh,S.K.,
            Zhang,Q., Thompson,J., Lucas,J.S., Bingle,C.D., Norris,D.P., Roy,S.
            and Brown,A.
  TITLE     De novo identification of mammalian ciliary motility proteins using
            cryo-EM
  JOURNAL   Cell 184 (23), 5791-5806 (2021)
   PUBMED   34715025
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Pineau,C., Hikmet,F., Zhang,C., Oksvold,P., Chen,S., Fagerberg,L.,
            Uhlen,M. and Lindskog,C.
  TITLE     Cell Type-Specific Expression of Testis Elevated Genes Based on
            Transcriptomics and Antibody-Based Proteomics
  JOURNAL   J Proteome Res 18 (12), 4215-4230 (2019)
   PUBMED   31429579
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Sasaki,K., Shiba,K., Nakamura,A., Kawano,N., Satouh,Y.,
            Yamaguchi,H., Morikawa,M., Shibata,D., Yanase,R., Jokura,K.,
            Nomura,M., Miyado,M., Takada,S., Ueno,H., Nonaka,S., Baba,T.,
            Ikawa,M., Kikkawa,M., Miyado,K. and Inaba,K.
  TITLE     Calaxin is required for cilia-driven determination of vertebrate
            laterality
  JOURNAL   Commun Biol 2, 226 (2019)
   PUBMED   31240264
  REMARK    Erratum:[Commun Biol. 2019 Jul 4;2:254. doi:
            10.1038/s42003-019-0512-5. PMID: 31286071]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 159)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 159)
  AUTHORS   Takeuchi,F., Isono,M., Katsuya,T., Yamamoto,K., Yokota,M.,
            Sugiyama,T., Nabika,T., Fujioka,A., Ohnaka,K., Asano,H., Yamori,Y.,
            Yamaguchi,S., Kobayashi,S., Takayanagi,R., Ogihara,T. and Kato,N.
  TITLE     Blood pressure and hypertension are associated with 7 loci in the
            Japanese population
  JOURNAL   Circulation 121 (21), 2302-2309 (2010)
   PUBMED   20479155
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 159)
  AUTHORS   Zariwala,M.A., Despotes,K.A. and Davis,S.D.
  TITLE     Primary Ciliary Dyskinesia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301301
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB204697.1, DC414358.1, AK316037.1, BC025676.1, CB250588.1,
            DB536362.1 and AC022915.14.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.2323711.1, AK316037.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..159
                     /product="calaxin isoform b"
                     /note="EF-hand calcium-binding domain-containing protein
                     1; EF-hand calcium binding domain 1; outer dynein arm
                     docking complex subunit 5"
                     /calculated_mol_wt=18367
     Region          <17..124
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     CDS             1..159
                     /gene="CLXN"
                     /gene_synonym="CILD53; EFCAB1; ODAD5"
                     /coded_by="NM_001363974.2:118..597"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS47853.1"
                     /db_xref="GeneID:79645"
                     /db_xref="HGNC:HGNC:25678"
                     /db_xref="MIM:619564"
ORIGIN      
        1 mnrkklqklt dtltknckhl frgfdkdndg cvnvlewihg lslflrgsle ekmkycfevf
       61 dlngdgfisk eemfhmlkns llkqpseedp degikdlvei tlkkmdhdhd gklsfadyel
      121 avreetllle afgpclpdpk sqmefeaqvf kdpnefndm
//
LOCUS       NP_001002269             164 aa            linear   PRI 20-NOV-2025
DEFINITION  exosome complex component RRP40 isoform 2 [Homo sapiens].
ACCESSION   NP_001002269
VERSION     NP_001002269.1
DBSOURCE    REFSEQ: accession NM_001002269.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Lu,G., Liu,H., Wang,H., Tang,X., Luo,S., Du,M., Christiani,D.C. and
            Wei,Q.
  TITLE     Potentially functional variants of INPP5D and EXOSC3 in immunity B
            cell-related genes are associated with non-small cell lung cancer
            survival
  JOURNAL   Front Immunol 15, 1440454 (2024)
   PUBMED   39176091
  REMARK    GeneRIF: Potentially functional variants of INPP5D and EXOSC3 in
            immunity B cell-related genes are associated with non-small cell
            lung cancer survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Van Quekelberghe,C., Latta,K., Kunzmann,S., Grohmann,M. and
            Hansen,M.
  TITLE     Atypical hemolytic uremic syndrome induced by SARS-CoV2 infection
            in infants with EXOSC3 mutation
  JOURNAL   Pediatr Nephrol 37 (11), 2781-2784 (2022)
   PUBMED   35522339
  REMARK    GeneRIF: Atypical hemolytic uremic syndrome induced by SARS-CoV2
            infection in infants with EXOSC3 mutation.
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Tsuda,M., Noguchi,M., Kurai,T., Ichihashi,Y., Ise,K., Wang,L.,
            Ishida,Y., Tanino,M., Hirano,S., Asaka,M. and Tanaka,S.
  TITLE     Aberrant expression of MYD88 via RNA-controlling CNOT4 and EXOSC3
            in colonic mucosa impacts generation of colonic cancer
  JOURNAL   Cancer Sci 112 (12), 5100-5113 (2021)
   PUBMED   34626022
  REMARK    GeneRIF: Aberrant expression of MYD88 via RNA-controlling CNOT4 and
            EXOSC3 in colonic mucosa impacts generation of colonic cancer.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Mukherjee,D., Gao,M., O'Connor,J.P., Raijmakers,R., Pruijn,G.,
            Lutz,C.S. and Wilusz,J.
  TITLE     The mammalian exosome mediates the efficient degradation of mRNAs
            that contain AU-rich elements
  JOURNAL   EMBO J 21 (1-2), 165-174 (2002)
   PUBMED   11782436
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Chen,C.Y., Gherzi,R., Ong,S.E., Chan,E.L., Raijmakers,R.,
            Pruijn,G.J., Stoecklin,G., Moroni,C., Mann,M. and Karin,M.
  TITLE     AU binding proteins recruit the exosome to degrade ARE-containing
            mRNAs
  JOURNAL   Cell 107 (4), 451-464 (2001)
   PUBMED   11719186
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Brouwer,R., Allmang,C., Raijmakers,R., van Aarssen,Y.,
            Egberts,W.V., Petfalski,E., van Venrooij,W.J., Tollervey,D. and
            Pruijn,G.J.
  TITLE     Three novel components of the human exosome
  JOURNAL   J Biol Chem 276 (9), 6177-6184 (2001)
   PUBMED   11110791
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Allmang,C., Petfalski,E., Podtelejnikov,A., Mann,M., Tollervey,D.
            and Mitchell,P.
  TITLE     The yeast exosome and human PM-Scl are related complexes of 3' -->
            5' exonucleases
  JOURNAL   Genes Dev 13 (16), 2148-2158 (1999)
   PUBMED   10465791
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Baas,F. and van Dijk,T.
  TITLE     EXOSC3 Pontocerebellar Hypoplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   25144110
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP237222.1, DA352003.1,
            AF229833.1, AK290864.1 and BE048144.1.
            
            Summary: This gene encodes a non-catalytic component of the human
            exosome, a complex with 3'-5' exoribonuclease activity that plays a
            role in numerous RNA processing and degradation activities. Related
            pseudogenes of this gene are found on chromosome 19 and 21.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2012].
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region that causes a frameshift and leads to an early stop codon
            compared to variant 1. The resulting protein (isoform 2) is shorter
            and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.215204.1,
                                           SRR1660803.107687.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.2"
     Protein         1..164
                     /product="exosome complex component RRP40 isoform 2"
                     /note="exosome complex exonuclease RRP40; exosome complex
                     component RRP40; ribosomal RNA-processing protein 40"
                     /calculated_mol_wt=17117
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9NQT5.3)"
     Region          108..>159
                     /region_name="S1_like"
                     /note="Ribosomal protein S1-like RNA-binding domain. Found
                     in a wide variety of RNA-associated proteins. Originally
                     identified in S1 ribosomal protein. This superfamily also
                     contains the Cold Shock Domain (CSD), which is a homolog
                     of the S1 domain. Both domains...; cl09927"
                     /db_xref="CDD:471952"
     Site            order(122,130,140,142)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:238094"
     CDS             1..164
                     /gene="EXOSC3"
                     /gene_synonym="bA3J10.7; CGI-102; hRrp-40; p10; PCH1B;
                     RRP40; Rrp40p"
                     /coded_by="NM_001002269.2:49..543"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43805.1"
                     /db_xref="GeneID:51010"
                     /db_xref="HGNC:HGNC:17944"
                     /db_xref="MIM:606489"
ORIGIN      
        1 maepasvaae slagsraraa rtvlgqvvlp geelllpeqe daegpggave rplslnarac
       61 srvrvvcgpg lrrcgdrllv tkcgrlrhke pgsgsgggvy wvdsqqkryv pvkgdhvigi
      121 vtaksgdifk vdvggsepas lsylsfegat krnrpnvqai ssrl
//
LOCUS       NP_705717                462 aa            linear   PRI 20-NOV-2025
DEFINITION  TGF-beta-activated kinase 1 and MAP3K7-binding protein 1 isoform
            beta [Homo sapiens].
ACCESSION   NP_705717
VERSION     NP_705717.1
DBSOURCE    REFSEQ: accession NM_153497.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 462)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 462)
  AUTHORS   Zhang,J., Teng,P., Sun,B., Zhang,J., Zhou,X. and Chen,W.
  TITLE     Down-regulated TAB1 suppresses the replication of Coxsackievirus B5
            via activating the NF-kappaB pathways through interaction with
            viral 3D polymerase
  JOURNAL   Virol J 20 (1), 291 (2023)
   PUBMED   38072991
  REMARK    GeneRIF: Down-regulated TAB1 suppresses the replication of
            Coxsackievirus B5 via activating the NF-kappaB pathways through
            interaction with viral 3D polymerase.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 462)
  AUTHORS   Ma,M., Dang,Y., Chang,B., Wang,F., Xu,J., Chen,L., Su,H., Li,J.,
            Ge,B., Chen,C. and Liu,H.
  TITLE     TAK1 is an essential kinase for STING trafficking
  JOURNAL   Mol Cell 83 (21), 3885-3903 (2023)
   PUBMED   37832545
REFERENCE   4  (residues 1 to 462)
  AUTHORS   Maddali,P., Ambesi,A. and McKeown-Longo,P.J.
  TITLE     Induction of pro-inflammatory genes by fibronectin DAMPs in three
            fibroblast cell lines: Role of TAK1 and MAP kinases
  JOURNAL   PLoS One 18 (5), e0286390 (2023)
   PUBMED   37228128
  REMARK    GeneRIF: Induction of pro-inflammatory genes by fibronectin DAMPs
            in three fibroblast cell lines: Role of TAK1 and MAP kinases.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 462)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 462)
  AUTHORS   Yamaguchi,K., Nagai,S., Ninomiya-Tsuji,J., Nishita,M., Tamai,K.,
            Irie,K., Ueno,N., Nishida,E., Shibuya,H. and Matsumoto,K.
  TITLE     XIAP, a cellular member of the inhibitor of apoptosis protein
            family, links the receptors to TAB1-TAK1 in the BMP signaling
            pathway
  JOURNAL   EMBO J 18 (1), 179-187 (1999)
   PUBMED   9878061
REFERENCE   7  (residues 1 to 462)
  AUTHORS   Arch,R.H., Gedrich,R.W. and Thompson,C.B.
  TITLE     Tumor necrosis factor receptor-associated factors (TRAFs)--a family
            of adapter proteins that regulates life and death
  JOURNAL   Genes Dev 12 (18), 2821-2830 (1998)
   PUBMED   9744859
  REMARK    Review article
REFERENCE   8  (residues 1 to 462)
  AUTHORS   Kurozumi,K., Nishita,M., Yamaguchi,K., Fujita,T., Ueno,N. and
            Shibuya,H.
  TITLE     BRAM1, a BMP receptor-associated molecule involved in BMP
            signalling
  JOURNAL   Genes Cells 3 (4), 257-264 (1998)
   PUBMED   9663660
REFERENCE   9  (residues 1 to 462)
  AUTHORS   Deacon,K. and Blank,J.L.
  TITLE     Characterization of the mitogen-activated protein kinase kinase 4
            (MKK4)/c-Jun NH2-terminal kinase 1 and MKK3/p38 pathways regulated
            by MEK kinases 2 and 3. MEK kinase 3 activates MKK3 but does not
            cause activation of p38 kinase in vivo
  JOURNAL   J Biol Chem 272 (22), 14489-14496 (1997)
   PUBMED   9162092
REFERENCE   10 (residues 1 to 462)
  AUTHORS   Shibuya,H., Yamaguchi,K., Shirakabe,K., Tonegawa,A., Gotoh,Y.,
            Ueno,N., Irie,K., Nishida,E. and Matsumoto,K.
  TITLE     TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal
            transduction
  JOURNAL   Science 272 (5265), 1179-1182 (1996)
   PUBMED   8638164
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC050554.1, AF425640.1,
            AI827837.1 and Z83845.14.
            
            Summary: The protein encoded by this gene was identified as a
            regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is
            known to mediate various intracellular signaling pathways, such as
            those induced by TGF beta, interleukin 1, and WNT-1. This protein
            interacts and thus activates TAK1 kinase. It has been shown that
            the C-terminal portion of this protein is sufficient for binding
            and activation of TAK1, while a portion of the N-terminus acts as a
            dominant-negative inhibitor of TGF beta, suggesting that this
            protein may function as a mediator between TGF beta receptors and
            TAK1. This protein can also interact with and activate the
            mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus
            represents an alternative activation pathway, in addition to the
            MAPKK pathways, which contributes to the biological responses of
            MAPK14 to various stimuli. Alternatively spliced transcript
            variants encoding distinct isoforms have been reported. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (beta) uses an alternate exon at
            the 3' end compared to variant 1, which includes a part of the
            coding region. The resulting isoform (beta) has a distinct and
            shorter C-terminus, as compared to isoform alpha. The beta isoform
            can interact with and activate MAPK14/p38alpha, but it does not
            bind or activate MAP3K7/TAK1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF425640.1, SRR3476690.4350.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..462
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..462
                     /product="TGF-beta-activated kinase 1 and MAP3K7-binding
                     protein 1 isoform beta"
                     /note="TAK1-binding protein 1; transforming growth factor
                     beta-activated kinase-binding protein 1; mitogen-activated
                     protein kinase kinase kinase 7-interacting protein 1"
                     /calculated_mol_wt=49786
     Region          1..22
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15750.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            order(46,50..51,69..71,290)
                     /site_type="active"
                     /db_xref="CDD:238083"
     Region          69..334
                     /region_name="PP2C"
                     /note="Protein phosphatase 2C; pfam00481"
                     /db_xref="CDD:395385"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            395
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:22307082,
                     ECO:0000269|PubMed:28939839; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:14592977; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK14.
                     /evidence=ECO:0000269|PubMed:14592977; propagated from
                     UniProtKB/Swiss-Prot (Q15750.1)"
     CDS             1..462
                     /gene="TAB1"
                     /gene_synonym="3'-Tab1; MAP3K7IP1"
                     /coded_by="NM_153497.3:24..1412"
                     /note="isoform beta is encoded by transcript variant beta"
                     /db_xref="CCDS:CCDS13992.1"
                     /db_xref="GeneID:10454"
                     /db_xref="HGNC:HGNC:18157"
                     /db_xref="MIM:602615"
ORIGIN      
        1 maaqrrsllq seqqpswtdd lplchlsgvg sasnrsysad gkgteshppe dswlkfrsen
       61 ncflygvfng ydgnrvtnfv aqrlsaelll gqlnaehaea dvrrvllqaf dvversfles
      121 iddalaekas lqsqlpegvp qhqlppqyqk ilerlktler eisggamavv avllnnklyv
      181 anvgtnrall ckstvdglqv tqlnvdhtte nedelfrlsq lgldagkikq vgiicgqest
      241 rrigdykvky gytdidllsa akskpiiaep eihgaqpldg vtgflvlmse glykaleaah
      301 gpgqanqeia amidtefakq tsldavaqav vdrvkrihsd tfasggerar fcprhedmtl
      361 lvrnfgyplg emsqptpspa paaggrvypv svpyssaqst sktsvtlslv mpsqgqmvng
      421 ahsastldea tptltkdpsr pasdltaipq cqlnllgslt pg
//
LOCUS       NP_001357593             776 aa            linear   PRI 20-NOV-2025
DEFINITION  cullin-1 [Homo sapiens].
ACCESSION   NP_001357593 XP_011514931
VERSION     NP_001357593.1
DBSOURCE    REFSEQ: accession NM_001370664.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 776)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 776)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   3  (residues 1 to 776)
  AUTHORS   Yang,T., Hu,J., Zhang,L., Liu,L., Pan,X., Zhou,Y., Wu,Y., Shi,X.,
            Obiegbusi,C.N. and Dong,X.
  TITLE     CircCUL1 inhibits trophoblast cell migration and invasion and
            promotes cell autophagy by sponging hsa-miR-30e-3p in fetal growth
            restriction via the ANXA1/PI3K/AKT axis
  JOURNAL   J Biochem Mol Toxicol 38 (7), e23759 (2024)
   PUBMED   39003567
  REMARK    GeneRIF: CircCUL1 inhibits trophoblast cell migration and invasion
            and promotes cell autophagy by sponging hsa-miR-30e-3p in fetal
            growth restriction via the ANXA1/PI3K/AKT axis.
REFERENCE   4  (residues 1 to 776)
  AUTHORS   Ma,Y., Huang,X., Wang,Y., Lei,Y., Yu,J., Yu,S., Gao,Y., Yang,J.,
            Zhao,F., Yu,H., Zeng,J., Chu,Y., Yang,M., Li,G., Xie,X. and
            Zhang,J.
  TITLE     NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer by
            Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins
  JOURNAL   Adv Sci (Weinh) 11 (9), e2305907 (2024)
   PUBMED   38126621
  REMARK    GeneRIF: NNMT/1-MNA Promote Cell-Cycle Progression of Breast Cancer
            by Targeting UBC12/Cullin-1-Mediated Degradation of P27 Proteins.
REFERENCE   5  (residues 1 to 776)
  AUTHORS   Khalil,M.I., Yang,C., Vu,L., Chadha,S., Nabors,H., James,C.D.,
            Morgan,I.M. and Pyeon,D.
  TITLE     The membrane-associated ubiquitin ligase MARCHF8 stabilizes the
            human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in
            head and neck cancer
  JOURNAL   J Virol 98 (2), e0172623 (2024)
   PUBMED   38226814
  REMARK    GeneRIF: The membrane-associated ubiquitin ligase MARCHF8
            stabilizes the human papillomavirus oncoprotein E7 by degrading
            CUL1 and UBE2L3 in head and neck cancer.
REFERENCE   6  (residues 1 to 776)
  AUTHORS   Winston,J.T., Strack,P., Beer-Romero,P., Chu,C.Y., Elledge,S.J. and
            Harper,J.W.
  TITLE     The SCFbeta-TRCP-ubiquitin ligase complex associates specifically
            with phosphorylated destruction motifs in IkappaBalpha and
            beta-catenin and stimulates IkappaBalpha ubiquitination in vitro
  JOURNAL   Genes Dev 13 (3), 270-283 (1999)
   PUBMED   9990852
  REMARK    Erratum:[Genes Dev 1999 Apr 15;13(8):1050]
REFERENCE   7  (residues 1 to 776)
  AUTHORS   Ng,R.W., Arooz,T., Yam,C.H., Chan,I.W., Lau,A.W. and Poon,R.Y.
  TITLE     Characterization of the cullin and F-box protein partner Skp1
  JOURNAL   FEBS Lett 438 (3), 183-189 (1998)
   PUBMED   9827542
REFERENCE   8  (residues 1 to 776)
  AUTHORS   Michel,J.J. and Xiong,Y.
  TITLE     Human CUL-1, but not other cullin family members, selectively
            interacts with SKP1 to form a complex with SKP2 and cyclin A
  JOURNAL   Cell Growth Differ 9 (6), 435-449 (1998)
   PUBMED   9663463
REFERENCE   9  (residues 1 to 776)
  AUTHORS   Lisztwan,J., Marti,A., Sutterluty,H., Gstaiger,M., Wirbelauer,C.
            and Krek,W.
  TITLE     Association of human CUL-1 and ubiquitin-conjugating enzyme CDC34
            with the F-box protein p45(SKP2): evidence for evolutionary
            conservation in the subunit composition of the CDC34-SCF pathway
  JOURNAL   EMBO J 17 (2), 368-383 (1998)
   PUBMED   9430629
REFERENCE   10 (residues 1 to 776)
  AUTHORS   Kipreos,E.T., Lander,L.E., Wing,J.P., He,W.W. and Hedgecock,E.M.
  TITLE     cul-1 is required for cell cycle exit in C. elegans and identifies
            a novel gene family
  JOURNAL   Cell 85 (6), 829-839 (1996)
   PUBMED   8681378
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005229.2 and AC006323.3.
            
            On May 21, 2019 this sequence version replaced XP_011514931.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.166539.1,
                                           SRR1660807.74492.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..776
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..776
                     /product="cullin-1"
                     /note="CUL-1"
                     /calculated_mol_wt=89548
     Region          21..660
                     /region_name="Cullin"
                     /note="Cullin family; pfam00888"
                     /db_xref="CDD:459983"
     Site            63
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13616.2)"
     Region          706..768
                     /region_name="Cullin_Nedd8"
                     /note="Cullin protein neddylation domain; pfam10557"
                     /db_xref="CDD:463146"
     CDS             1..776
                     /gene="CUL1"
                     /coded_by="NM_001370664.1:583..2913"
                     /db_xref="CCDS:CCDS34772.1"
                     /db_xref="GeneID:8454"
                     /db_xref="HGNC:HGNC:2551"
                     /db_xref="MIM:603134"
ORIGIN      
        1 msstrsqnph glkqigldqi wddlragiqq vytrqsmaks rymelythvy nyctsvhqsn
       61 qargagvpps kskkgqtpgg aqfvglelyk rlkeflknyl tnllkdgedl mdesvlkfyt
      121 qqwedyrfss kvlngicayl nrhwvrrecd egrkgiyeiy slalvtwrdc lfrplnkqvt
      181 navlklieke rngetintrl isgvvqsyve lglneddafa kgptltvyke sfesqfladt
      241 erfytreste flqqnpvtey mkkaearlle eqrrvqvylh estqdelark ceqvliekhl
      301 eifhtefqnl ldadknedlg rmynlvsriq dglgelkkll ethihnqgla aiekcgeaal
      361 ndpkmyvqtv ldvhkkynal vmsafnndag fvaaldkacg rfinnnavtk maqssskspe
      421 llarycdsll kkssknpeea eledtlnqvm vvfkyiedkd vfqkfyakml akrlvhqnsa
      481 sddaeasmis klkqacgfey tsklqrmfqd igvskdlneq fkkhltnsep ldldfsiqvl
      541 ssgswpfqqs ctfalpsele rsyqrftafy asrhsgrklt wlyqlskgel vtncfknryt
      601 lqastfqmai llqynteday tvqqltdstq ikmdilaqvl qillkskllv ledenanvde
      661 velkpdtlik lylgyknkkl rvninvpmkt eqkqeqetth knieedrkll iqaaivrimk
      721 mrkvlkhqql lgevltqlss rfkprvpvik kcidilieke ylervdgekd tysyla
//
LOCUS       NP_001356543             344 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb group RING finger protein 2 [Homo sapiens].
ACCESSION   NP_001356543 XP_005257699
VERSION     NP_001356543.1
DBSOURCE    REFSEQ: accession NM_001369614.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 344)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 344)
  AUTHORS   Wang,K., Li,M., Duan,H., Fan,M., Xu,C. and Yu,F.
  TITLE     SLCO4A1-AS1 triggers the malignant behaviours of melanoma cells via
            sponging miR-1306-5p to enhance PCGF2
  JOURNAL   Exp Dermatol 31 (8), 1220-1233 (2022)
   PUBMED   35427425
  REMARK    GeneRIF: SLCO4A1-AS1 triggers the malignant behaviours of melanoma
            cells via sponging miR-1306-5p to enhance PCGF2.
REFERENCE   3  (residues 1 to 344)
  AUTHORS   Flora,P., Dalal,G., Cohen,I. and Ezhkova,E.
  TITLE     Polycomb Repressive Complex(es) and Their Role in Adult Stem Cells
  JOURNAL   Genes (Basel) 12 (10), 1485 (2021)
   PUBMED   34680880
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 344)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 344)
  AUTHORS   Mai,J., Peng,X.D., Tang,J., Du,T., Chen,Y.H., Wang,Z.F.,
            Zhang,H.L., Huang,J.H., Zhong,Z.Y., Yang,D., Li,Z.L., Huang,Y.,
            Feng,G.K., Zhu,X.F. and Deng,R.
  TITLE     AKT-mediated regulation of chromatin ubiquitylation and
            tumorigenesis through Mel18 phosphorylation
  JOURNAL   Oncogene 40 (13), 2422-2436 (2021)
   PUBMED   33664452
  REMARK    GeneRIF: AKT-mediated regulation of chromatin ubiquitylation and
            tumorigenesis through Mel18 phosphorylation.
REFERENCE   6  (residues 1 to 344)
  AUTHORS   Levine,S.S., Weiss,A., Erdjument-Bromage,H., Shao,Z., Tempst,P. and
            Kingston,R.E.
  TITLE     The core of the polycomb repressive complex is compositionally and
            functionally conserved in flies and humans
  JOURNAL   Mol Cell Biol 22 (17), 6070-6078 (2002)
   PUBMED   12167701
REFERENCE   7  (residues 1 to 344)
  AUTHORS   Miyazaki,K., Inoue,H., Onai,N., Ishihara,H. and Kanno,M.
  TITLE     Chemokine-mediated thymopoiesis is regulated by a mammalian
            Polycomb group gene, mel-18
  JOURNAL   Immunol Lett 80 (2), 139-143 (2002)
   PUBMED   11750047
  REMARK    GeneRIF: The mouse counterpart of this gene regulates the
            expression of various chemokines and chemokine receptors, which may
            be important for T cell migration and differentiation.
REFERENCE   8  (residues 1 to 344)
  AUTHORS   Matsuo,F., Yano,K., Saito,H., Morotomi,K., Kato,M., Yoshimoto,M.,
            Kasumi,F., Akiyama,F., Sakamoto,G. and Miki,Y.
  TITLE     Mutation analysis of the mel-18 gene that shows decreased
            expression in human breast cancer cell lines
  JOURNAL   Breast Cancer 9 (1), 33-38 (2002)
   PUBMED   12196719
REFERENCE   9  (residues 1 to 344)
  AUTHORS   Kimura,M., Koseki,Y., Yamashita,M., Watanabe,N., Shimizu,C.,
            Katsumoto,T., Kitamura,T., Taniguchi,M., Koseki,H. and Nakayama,T.
  TITLE     Regulation of Th2 cell differentiation by mel-18, a mammalian
            polycomb group gene
  JOURNAL   Immunity 15 (2), 275-287 (2001)
   PUBMED   11520462
  REMARK    GeneRIF: The mouse counterpart of this gene regulates the
            expression of Th2 cytokines, and plays a critical role in Th2 cell
            differentiation and Th-2 dependent immune responses.
REFERENCE   10 (residues 1 to 344)
  AUTHORS   Ishida,A., Asano,H., Hasegawa,M., Koseki,H., Ono,T., Yoshida,M.C.,
            Taniguchi,M. and Kanno,M.
  TITLE     Cloning and chromosome mapping of the human Mel-18 gene which
            encodes a DNA-binding protein with a new 'RING-finger' motif
  JOURNAL   Gene 129 (2), 249-255 (1993)
   PUBMED   8325509
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006449.19.
            
            On Apr 13, 2019 this sequence version replaced XP_005257699.1.
            
            Summary: The protein encoded by this gene contains a RING finger
            motif and is similar to the polycomb group (PcG) gene products. PcG
            gene products form complexes via protein-protein interaction and
            maintain the transcription repression of genes involved in
            embryogenesis, cell cycles, and tumorigenesis. This protein was
            shown to act as a negative regulator of transcription and has tumor
            suppressor activity. The expression of this gene was detected in
            various tumor cells, but is limited in neural organs in normal
            tissues. Knockout studies in mice suggested that this protein may
            negatively regulate the expression of different cytokines,
            chemokines, and chemokine receptors, and thus plays an important
            role in lymphocyte differentiation and migration, as well as in
            immune responses. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.870921.1,
                                           SRR7346977.805242.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..344
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..344
                     /product="polycomb group RING finger protein 2"
                     /note="ring finger protein 110; zinc finger protein 144;
                     DNA-binding protein Mel-18"
                     /calculated_mol_wt=37657
     Region          5..101
                     /region_name="RING-HC_PCGF4"
                     /note="RING finger found in polycomb group RING finger
                     protein 4 (PCGF4) and similar proteins; cd16736"
                     /db_xref="CDD:438394"
     Site            order(5..13,15,17,21,23..24,26..27,29..30,32..36,39..42,
                     44..45,66,69..72,74,78,81..82,84,86,89..90,93..94,97)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:438394"
     Region          81..95
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P35227.1)"
     Region          130..228
                     /region_name="RAWUL_PCGF2"
                     /note="RING finger- and WD40-associated ubiquitin-like
                     (RAWUL) domain found in polycomb group RING finger protein
                     2 (PCGF2); cd17164"
                     /db_xref="CDD:340684"
     Region          <236..328
                     /region_name="PLN02217"
                     /note="probable pectinesterase/pectinesterase inhibitor"
                     /db_xref="CDD:215130"
     Region          240..344
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35227.1)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P35227.1)"
     CDS             1..344
                     /gene="PCGF2"
                     /gene_synonym="MEL-18; RNF110; TPFS; ZNF144"
                     /coded_by="NM_001369614.1:182..1216"
                     /db_xref="CCDS:CCDS32638.1"
                     /db_xref="GeneID:7703"
                     /db_xref="HGNC:HGNC:12929"
                     /db_xref="MIM:600346"
ORIGIN      
        1 mhrttrikit elnphlmcal cggyfidatt iveclhsfck tcivryletn kycpmcdvqv
       61 hktrpllsir sdktlqdivy klvpglfkde mkrrrdfyaa ypltevpngs nedrgevleq
      121 ekgalsddei vslsiefyeg ardrdekkgp lengdgdkek tgvrflrcpa amtvmhlakf
      181 lrnkmdvpsk ykvevlyede plkeyytlmd iayiypwrrn gplplkyrvq packrltlat
      241 vptpsegtnt sgasecesvs dkapspatlp atssslpspa tpshgspssh gppathptsp
      301 tppstasgat taanggslnc lqtpsstsrg rkmtvngapv pplt
//
LOCUS       NP_003788                441 aa            linear   PRI 20-NOV-2025
DEFINITION  polycomb protein EED isoform a [Homo sapiens].
ACCESSION   NP_003788
VERSION     NP_003788.2
DBSOURCE    REFSEQ: accession NM_003797.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Goel,H., O'Donnell,S. and Edwards,M.
  TITLE     EED related overgrowth: First report of multiple members in a
            single family
  JOURNAL   Am J Med Genet A 194 (2), 374-382 (2024)
   PUBMED   37840385
  REMARK    GeneRIF: EED related overgrowth: First report of multiple members
            in a single family.
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Liu,X. and Liu,X.
  TITLE     PRC2, Chromatin Regulation, and Human Disease: Insights From
            Molecular Structure and Function
  JOURNAL   Front Oncol 12, 894585 (2022)
   PUBMED   35800061
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 441)
  AUTHORS   Shaliman,D., Takenobu,H., Sugino,R.P., Ohira,M. and Kamijo,T.
  TITLE     The PRC2 molecule EED is a target of epigenetic therapy for
            neuroblastoma
  JOURNAL   Eur J Cell Biol 101 (3), 151238 (2022)
   PUBMED   35636260
  REMARK    GeneRIF: The PRC2 molecule EED is a target of epigenetic therapy
            for neuroblastoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 441)
  AUTHORS   Alerasool,N., Leng,H., Lin,Z.Y., Gingras,A.C. and Taipale,M.
  TITLE     Identification and functional characterization of transcriptional
            activators in human cells
  JOURNAL   Mol Cell 82 (3), 677-695 (2022)
   PUBMED   35016035
REFERENCE   6  (residues 1 to 441)
  AUTHORS   Rietzler,M., Bittner,M., Kolanus,W., Schuster,A. and Holzmann,B.
  TITLE     The human WD repeat protein WAIT-1 specifically interacts with the
            cytoplasmic tails of beta7-integrins
  JOURNAL   J Biol Chem 273 (42), 27459-27466 (1998)
   PUBMED   9765275
REFERENCE   7  (residues 1 to 441)
  AUTHORS   Denisenko,O., Shnyreva,M., Suzuki,H. and Bomsztyk,K.
  TITLE     Point mutations in the WD40 domain of Eed block its interaction
            with Ezh2
  JOURNAL   Mol Cell Biol 18 (10), 5634-5642 (1998)
   PUBMED   9742080
REFERENCE   8  (residues 1 to 441)
  AUTHORS   Sewalt,R.G., van der Vlag,J., Gunster,M.J., Hamer,K.M., den
            Blaauwen,J.L., Satijn,D.P., Hendrix,T., van Driel,R. and Otte,A.P.
  TITLE     Characterization of interactions between the mammalian
            polycomb-group proteins Enx1/EZH2 and EED suggests the existence of
            different mammalian polycomb-group protein complexes
  JOURNAL   Mol Cell Biol 18 (6), 3586-3595 (1998)
   PUBMED   9584199
REFERENCE   9  (residues 1 to 441)
  AUTHORS   van Lohuizen,M., Tijms,M., Voncken,J.W., Schumacher,A., Magnuson,T.
            and Wientjens,E.
  TITLE     Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2
            with Eed: indication for separate Pc-G complexes
  JOURNAL   Mol Cell Biol 18 (6), 3572-3579 (1998)
   PUBMED   9584197
REFERENCE   10 (residues 1 to 441)
  AUTHORS   Sequerra Amram Cohen,A. and Gibson,W.T.
  TITLE     EED-Related Overgrowth
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   30973693
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB086430.1, AL546955.3,
            AK292120.1, AA811323.1 and AW263732.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 16, 2002 this sequence version replaced NP_003788.1.
            
            Summary: This gene encodes a member of the Polycomb-group (PcG)
            family. PcG family members form multimeric protein complexes, which
            are involved in maintaining the transcriptional repressive state of
            genes over successive cell generations. This protein interacts with
            enhancer of zeste 2, the cytoplasmic tail of integrin beta7,
            immunodeficiency virus type 1 (HIV-1) MA protein, and histone
            deacetylase proteins. This protein mediates repression of gene
            activity through histone deacetylation, and may act as a specific
            regulator of integrin function. Two transcript variants encoding
            distinct isoforms have been identified for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) lacks an in-frame exon in the
            3' coding region compared to variant 3. It encodes isoform a, which
            is shorter than isoform c.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.878030.1, AK292120.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263360.11/ ENSP00000263360.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.2"
     Protein         1..441
                     /product="polycomb protein EED isoform a"
                     /note="polycomb protein EED; WD protein associating with
                     integrin cytoplasmic tails 1; embryonic ectoderm
                     development protein"
                     /calculated_mol_wt=50067
     Region          1..72
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q921E6; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O75530.2)"
     Site            66
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          81..441
                     /region_name="Interaction with EZH2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          96..140
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <109..439
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          148..188
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          149..303
                     /region_name="Required for interaction with the matrix
                     protein MA of HIV-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          193..230
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            197
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          240..302
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            268
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Site            284
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:20974918; N6-methyllysine,
                     alternate. /evidence=ECO:0000269|PubMed:20974918;
                     propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          301..441
                     /region_name="Required for interaction with the matrix
                     protein MA of HIV-1"
                     /note="propagated from UniProtKB/Swiss-Prot (O75530.2)"
     Region          309..357
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          365..405
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          413..437
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..441
                     /gene="EED"
                     /gene_synonym="COGIS; HEED; WAIT1"
                     /coded_by="NM_003797.5:478..1803"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8273.1"
                     /db_xref="GeneID:8726"
                     /db_xref="HGNC:HGNC:3188"
                     /db_xref="MIM:605984"
ORIGIN      
        1 mserevstap agtdmpaakk qklssdensn pdlsgdendd avsiesgtnt erpdtptntp
       61 napgrkswgk gkwkskkcky sfkcvnslke dhnqplfgvq fnwhskegdp lvfatvgsnr
      121 vtlyechsqg eirllqsyvd adadenfytc awtydsntsh pllavagsrg iiriinpitm
      181 qcikhyvghg nainelkfhp rdpnlllsvs kdhalrlwni qtdtlvaifg gveghrdevl
      241 sadydllgek imscgmdhsl klwrinskrm mnaikesydy npnktnrpfi sqkihfpdfs
      301 trdihrnyvd cvrwlgdlil skscenaivc wkpgkmeddi dkikpsesnv tilgrfdysq
      361 cdiwymrfsm dfwqkmlalg nqvgklyvwd levedphkak cttlthhkcg aairqtsfsr
      421 dssiliavcd dasiwrwdrl r
//
LOCUS       NP_001287912             852 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 2 isoform 6 [Homo sapiens].
ACCESSION   NP_001287912 XP_005273866
VERSION     NP_001287912.1
DBSOURCE    REFSEQ: accession NM_001300983.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 852)
  AUTHORS   Li,H., Zhu,J., Liu,X., Liu,L., Huang,S., Wu,A., Xu,Z., Zhang,X.,
            Li,Z., Ni,F., Liu,L. and Dong,J.
  TITLE     Glioma stem cell-derived exosomes induce the transformation of
            astrocytes via the miR-3065-5p/DLG2 signaling axis
  JOURNAL   Glia 72 (5), 857-871 (2024)
   PUBMED   38234042
  REMARK    GeneRIF: Glioma stem cell-derived exosomes induce the
            transformation of astrocytes via the miR-3065-5p/DLG2 signaling
            axis.
REFERENCE   2  (residues 1 to 852)
  AUTHORS   Chen,Y., Karaca,E., Robin,N.H., Goodloe,D., Al-Beshri,A.,
            Dean,S.J., Hurst,A.C.E., Carroll,A.J. and Mikhail,F.M.
  TITLE     DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism
  JOURNAL   Genet Med 26 (1), 101010 (2024)
   PUBMED   37860969
  REMARK    GeneRIF: DLG2 intragenic exonic deletions reinforce the link to
            neurodevelopmental disorders and suggest a potential association
            with congenital anomalies and dysmorphism.
REFERENCE   3  (residues 1 to 852)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 852)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 852)
  AUTHORS   Stathakis,D.G., Lee,D. and Bryant,P.J.
  TITLE     Fine-scale physical map of the 11q21 region surrounding the human
            DLG2 locus, the gene encoding Chapsyn-110
  JOURNAL   Genomics 54 (1), 186-188 (1998)
   PUBMED   9806853
REFERENCE   6  (residues 1 to 852)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
REFERENCE   7  (residues 1 to 852)
  AUTHORS   Hsueh,Y.P., Kim,E. and Sheng,M.
  TITLE     Disulfide-linked head-to-head multimerization in the mechanism of
            ion channel clustering by PSD-95
  JOURNAL   Neuron 18 (5), 803-814 (1997)
   PUBMED   9182804
REFERENCE   8  (residues 1 to 852)
  AUTHORS   Kim,E., Cho,K.O., Rothschild,A. and Sheng,M.
  TITLE     Heteromultimerization and NMDA receptor-clustering activity of
            Chapsyn-110, a member of the PSD-95 family of proteins
  JOURNAL   Neuron 17 (1), 103-113 (1996)
   PUBMED   8755482
REFERENCE   9  (residues 1 to 852)
  AUTHORS   Brenman,J.E., Chao,D.S., Gee,S.H., McGee,A.W., Craven,S.E.,
            Santillano,D.R., Wu,Z., Huang,F., Xia,H., Peters,M.F.,
            Froehner,S.C. and Bredt,D.S.
  TITLE     Interaction of nitric oxide synthase with the postsynaptic density
            protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
  JOURNAL   Cell 84 (5), 757-767 (1996)
   PUBMED   8625413
REFERENCE   10 (residues 1 to 852)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295094.1 and AP003026.2.
            
            On Jul 17, 2014 this sequence version replaced XP_005273866.1.
            
            Summary: This gene encodes a member of the membrane-associated
            guanylate kinase (MAGUK) family. The encoded protein forms a
            heterodimer with a related family member that may interact at
            postsynaptic sites to form a multimeric scaffold for the clustering
            of receptors, ion channels, and associated signaling proteins.
            Multiple transcript variants encoding different isoforms have been
            found for this gene. Additional transcript variants have been
            described, but their full-length nature is not known. [provided by
            RefSeq, Dec 2008].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and
            coding sequence compared to variant 1. The resulting isoform (6)
            has a shorter and distinct N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK295094.1, BC143964.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..852
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..852
                     /product="disks large homolog 2 isoform 6"
                     /note="channel-associated protein of synapses, 110kDa;
                     postsynaptic density protein PSD-93; channel-associated
                     protein of synapse-110; discs, large homolog 2,
                     chapsyn-110; protein phosphatase 1, regulatory subunit 58;
                     disks large homolog 2"
                     /calculated_mol_wt=94870
     Region          15..97
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          96..184
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(107..113,130,133,163,167,170..171)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          193..277
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(202..208,225,228,258,262,265..266)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          278..345
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          418..508
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(430..436,447,450,480,484,487..488)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          534..607
                     /region_name="SH3_DLG2"
                     /note="Src Homology 3 domain of Disks Large homolog 2;
                     cd12032"
                     /db_xref="CDD:212965"
     Site            order(542,564..565)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212965"
     Site            order(545,547,550,559,577..578,597,599..600)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212965"
     Region          661..839
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..852
                     /gene="DLG2"
                     /gene_synonym="chapsyn-110; PPP1R58; PSD-93; PSD93"
                     /coded_by="NM_001300983.1:304..2862"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS73357.1"
                     /db_xref="GeneID:1740"
                     /db_xref="HGNC:HGNC:2901"
                     /db_xref="MIM:603583"
ORIGIN      
        1 mffacycalr tnvkkyryqd edaphdhslp rlthevrgpe lvhvseknls qienvhgyvl
       61 qshisplkas papiivntdt ldtipyvngt eieyefeeit lergnsglgf siaggtdnph
      121 igddpgifit kiipggaaae dgrlrvndci lrvnevdvse vshskaveal keagsivrly
      181 vrrrrpilet vveiklfkgp kglgfsiagg vgnqhipgdn siyvtkiidg gaaqkdgrlq
      241 vgdrllmvnn ysleevthee availkntse vvylkvgkpt tiymtdpygp pdithsyspp
      301 menhllsgnn gtleyktslp pispgryspi pkhmlvdddy trppepvyst vnklcdkpas
      361 prhyspvecd ksfllsapys hyhlgllpds emtshsqhst atrqpsmtlq ravslegepr
      421 kvvlhkgstg lgfnivgged gegifvsfil aggpadlsge lqrgdqilsv ngidlrgash
      481 eqaaaalkga gqtvtiiaqy qpedyarfea kihdlreqmm nhsmssgsgs lrtnqkrsly
      541 vramfdydks kdsglpsqgl sfkygdilhv inasddewwq arrvmlegds eemgvipskr
      601 rverkerarl ktvkfnakpg vidskgdipg lgddgygtkt lrgqedlils yepvtrqein
      661 ytrpviilgp mkdrinddli sefpdkfgsc vphttrpkrd yevdgrdyhf visreqmekd
      721 iqehkfieag qyndnlygts vqsvrfvaer gkhcildvsg naikrlqvaq lypiaifikp
      781 rsleplmemn krlteeqakk tydraikleq efgeyftaiv qgdtlediyn qcklvieeqs
      841 gpfiwipske kl
//
LOCUS       NP_598003                376 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc transporter 7 [Homo sapiens].
ACCESSION   NP_598003
VERSION     NP_598003.2
DBSOURCE    REFSEQ: accession NM_133496.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Yu,W., Gui,S., Xie,J., Peng,L., Xiao,J., Luo,H., Tao,Z. and
            Cheng,Z.
  TITLE     Investigation of cuproptosis regulator-mediated modification
            patterns and SLC30A7 function in GBM
  JOURNAL   Aging (Albany NY) 16 (4), 3554-3582 (2024)
   PUBMED   38393693
  REMARK    GeneRIF: Investigation of cuproptosis regulator-mediated
            modification patterns and SLC30A7 function in GBM.
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Bui,H.B., Watanabe,S., Nomura,N., Liu,K., Uemura,T., Inoue,M.,
            Tsutsumi,A., Fujita,H., Kinoshita,K., Kato,Y., Iwata,S., Kikkawa,M.
            and Inaba,K.
  TITLE     Cryo-EM structures of human zinc transporter ZnT7 reveal the
            mechanism of Zn2+ uptake into the Golgi apparatus
  JOURNAL   Nat Commun 14 (1), 4770 (2023)
   PUBMED   37553324
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Huang,L., Yang,Z., Kirschke,C.P., Prouteau,C., Copin,M.C.,
            Bonneau,D., Pellier,I., Coutant,R., Miot,C. and Ziegler,A.
  TITLE     Identification of novel compound heterozygous variants in the
            SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure
  JOURNAL   Hum Mol Genet 32 (12), 2016-2031 (2023)
   PUBMED   36821639
  REMARK    GeneRIF: Identification of novel compound heterozygous variants in
            the SLC30A7 (ZNT7) gene in two French brothers with stunted growth,
            testicular hypoplasia and bone marrow failure.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Penon-Portmann,M., Eldomery,M.K., Potocki,L., Marafi,D.,
            Posey,J.E., Coban-Akdemir,Z., Harel,T., Grochowski,C.M., Loucks,H.,
            Devine,W.P., Van Ziffle,J., Doherty,D., Lupski,J.R. and Shieh,J.T.
  TITLE     De novo heterozygous variants in SLC30A7 are a candidate cause for
            Joubert syndrome
  JOURNAL   Am J Med Genet A 188 (8), 2360-2366 (2022)
   PUBMED   35751429
  REMARK    GeneRIF: De novo heterozygous variants in SLC30A7 are a candidate
            cause for Joubert syndrome.
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Li,W., Yang,S., Chen,G. and He,S.
  TITLE     MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in diabetic
            retinopathy
  JOURNAL   Hum Exp Toxicol 41, 9603271221099589 (2022)
   PUBMED   35607288
  REMARK    GeneRIF: MiR-200c-3p regulates pyroptosis by targeting SLC30A7 in
            diabetic retinopathy.
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Matsuura,W., Kohda,A.,
            Okumura,K., Nagao,M., Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Zinc transporters, ZnT5 and ZnT7, are required for the activation
            of alkaline phosphatases, zinc-requiring enzymes that are
            glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
  JOURNAL   J Biol Chem 280 (1), 637-643 (2005)
   PUBMED   15525635
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Devergnas,S., Chimienti,F., Naud,N., Pennequin,A., Coquerel,Y.,
            Chantegrel,J., Favier,A. and Seve,M.
  TITLE     Differential regulation of zinc efflux transporters ZnT-1, ZnT-5
            and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
  JOURNAL   Biochem Pharmacol 68 (4), 699-709 (2004)
   PUBMED   15276077
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Seve,M., Chimienti,F., Devergnas,S. and Favier,A.
  TITLE     In silico identification and expression of SLC30 family genes: an
            expressed sequence tag data mining strategy for the
            characterization of zinc transporters' tissue expression
  JOURNAL   BMC Genomics 5 (1), 32 (2004)
   PUBMED   15154973
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 376)
  AUTHORS   Kirschke,C.P. and Huang,L.
  TITLE     ZnT7, a novel mammalian zinc transporter, accumulates zinc in the
            Golgi apparatus
  JOURNAL   J Biol Chem 278 (6), 4096-4102 (2003)
   PUBMED   12446736
REFERENCE   10 (residues 1 to 376)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA997188.1, BC064692.1, AL732465.6 and BX648884.1.
            
            On Dec 20, 2003 this sequence version replaced NP_598003.1.
            
            Summary: Zinc functions as a cofactor for numerous enzymes, nuclear
            factors, and hormones and as an intra- and intercellular signal
            ion. Members of the zinc transporter (ZNT)/SLC30 subfamily of the
            cation diffusion facilitator family, such as SLC30A7, permit
            cellular efflux of zinc (Seve et al., 2004 [PubMed
            15154973]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) is the longer transcript.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.17968.1, BC064692.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000357650.9/ ENSP00000350278.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21.2"
     Protein         1..376
                     /product="zinc transporter 7"
                     /note="zinc transporter like 2; zinc transporter ZnT-7;
                     znt-like transporter 2; solute carrier family 30 (zinc
                     transporter), member 7"
                     /calculated_mol_wt=41495
     Region          31..354
                     /region_name="CzcD"
                     /note="Co/Zn/Cd efflux system component [Inorganic ion
                     transport and metabolism]; COG1230"
                     /db_xref="CDD:440843"
     Site            38..58
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            103..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          161..218
                     /region_name="His-rich loop"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Region          <182..219
                     /region_name="ureE"
                     /note="urease accessory protein UreE; Provisional;
                     PRK13263"
                     /db_xref="CDD:237323"
     Region          194..226
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            237..257
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     Site            263..283
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEW0.1)"
     CDS             1..376
                     /gene="SLC30A7"
                     /gene_synonym="ZHS; ZnT-7; ZNT7; ZnTL2"
                     /coded_by="NM_133496.5:174..1304"
                     /db_xref="CCDS:CCDS776.1"
                     /db_xref="GeneID:148867"
                     /db_xref="HGNC:HGNC:19306"
                     /db_xref="MIM:611149"
ORIGIN      
        1 mlplsikdde ykppkfnlfg kisgwfrsil sdktsrnlff flclnlsfaf vellygiwsn
       61 clglisdsfh mffdstaila glaasviskw rdndafsygy vraevlagfv nglfliftaf
      121 fifsegvera lappdvhher lllvsilgfv vnligifvfk hgghghshgs ghghshslfn
      181 galdqahghv dhchshevkh gaahshdhah ghghfhshdg pslkettgps rqilqgvflh
      241 iladtlgsig viasaimmqn fglmiadpic siliailivv svipllresv gilmqrtppl
      301 lenslpqcyq rvqqlqgvys lqeqhfwtlc sdvyvgtlkl ivapdadarw ilsqthnift
      361 qagvrqlyvq idfaam
//
LOCUS       NP_001357122             339 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin-binding protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001357122
VERSION     NP_001357122.1
DBSOURCE    REFSEQ: accession NM_001370193.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Liu,J., Prickett,T.D., Elliott,E., Meroni,G. and Brautigan,D.L.
  TITLE     Phosphorylation and microtubule association of the Opitz syndrome
            protein mid-1 is regulated by protein phosphatase 2A via binding to
            the regulatory subunit alpha 4
  JOURNAL   Proc Natl Acad Sci U S A 98 (12), 6650-6655 (2001)
   PUBMED   11371618
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Scanlan,M.J., Gordan,J.D., Williamson,B., Stockert,E., Bander,N.H.,
            Jongeneel,V., Gure,A.O., Jager,D., Jager,E., Knuth,A., Chen,Y.T.
            and Old,L.J.
  TITLE     Antigens recognized by autologous antibody in patients with
            renal-cell carcinoma
  JOURNAL   Int J Cancer 83 (4), 456-464 (1999)
   PUBMED   10508479
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Chung,H., Nairn,A.C., Murata,K. and Brautigan,D.L.
  TITLE     Mutation of Tyr307 and Leu309 in the protein phosphatase 2A
            catalytic subunit favors association with the alpha 4 subunit which
            promotes dephosphorylation of elongation factor-2
  JOURNAL   Biochemistry 38 (32), 10371-10376 (1999)
   PUBMED   10441131
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Chen,J., Peterson,R.T. and Schreiber,S.L.
  TITLE     Alpha 4 associates with protein phosphatases 2A, 4, and 6
  JOURNAL   Biochem Biophys Res Commun 247 (3), 827-832 (1998)
   PUBMED   9647778
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Onda,M., Inui,S., Maeda,K., Suzuki,M., Takahashi,E. and
            Sakaguchi,N.
  TITLE     Expression and chromosomal localization of the human alpha 4/IGBP1
            gene, the structure of which is closely related to the yeast TAP42
            protein of the rapamycin-sensitive signal transduction pathway
  JOURNAL   Genomics 46 (3), 373-378 (1997)
   PUBMED   9441740
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158141.14 and AL139111.20.
            
            Summary: The proliferation and differentiation of B cells is
            dependent upon a B-cell antigen receptor (BCR) complex. Binding of
            antigens to specific B-cell receptors results in a tyrosine
            phosphorylation reaction through the BCR complex and leads to
            multiple signal transduction pathways. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.643739.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153307, SAMEA2159080
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
     Protein         1..339
                     /product="immunoglobulin-binding protein 1 isoform 1"
                     /note="protein phosphatase 2A, regulatory subunit alpha-4;
                     B cell signal transduction molecule alpha 4; bA351K23.1
                     (immunoglobulin binding protein 1 (CD79A)); protein
                     alpha-4; CD79a-binding protein 1; immunoglobulin (CD79A)
                     binding protein 1; renal carcinoma antigen NY-REN-16;
                     protein phosphatase 2/4/6 regulatory subunit"
                     /calculated_mol_wt=39091
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          12..329
                     /region_name="TAP42"
                     /note="TAP42-like family; pfam04177"
                     /db_xref="CDD:461209"
     Region          98..202
                     /region_name="Interaction with PPP2CA"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          221..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Region          225..290
                     /region_name="Interaction with MID1.
                     /evidence=ECO:0000269|PubMed:11806752"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     Site            241
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Site            255..256
                     /site_type="cleavage"
                     /note="Cleavage, by calpain; propagated from
                     UniProtKB/Swiss-Prot (P78318.1)"
     Region          289..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78318.1)"
     CDS             1..339
                     /gene="IGBP1"
                     /gene_synonym="ALPHA-4; alpha4; IBP1; MRXS28"
                     /coded_by="NM_001370193.1:95..1114"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14396.1"
                     /db_xref="GeneID:3476"
                     /db_xref="HGNC:HGNC:5461"
                     /db_xref="MIM:300139"
ORIGIN      
        1 maaedelqlp rlpelfetgr qlldevevat epagsrivqe kvfkgldlle kaaemlsqld
       61 lfsrnedlee iastdlkyll vpafqgaltm kqvnpskrld hlqrarehfi nyltqchcyh
      121 vaefelpktm nnsaenhtan ssmaypslva masqrqakiq rykqkkeleh rlsamksave
      181 sgqaddervr eyyllhlqrw idisleeies idqeikilre rdssreasts nssrqerppv
      241 kpfiltrnma qakvfgagyp slptmtvsdw yeqhrkygal pdqgiakaap eefrkaaqqq
      301 eeqeekeeed deqtlhrare wddwkdthpr gygnrqnmg
//
LOCUS       NP_001354761             170 aa            linear   PRI 20-NOV-2025
DEFINITION  phospholipid hydroperoxide glutathione peroxidase GPX4 isoform D
            [Homo sapiens].
ACCESSION   NP_001354761
VERSION     NP_001354761.1
DBSOURCE    REFSEQ: accession NM_001367832.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Ye,H., Ding,X., Lv,X., Du,Y., Guo,R., Qiu,J., Li,R. and Cao,L.
  TITLE     KLF14 directly downregulates the expression of GPX4 to exert
            antitumor effects by promoting ferroptosis in cervical cancer
  JOURNAL   J Transl Med 22 (1), 923 (2024)
   PUBMED   39390559
  REMARK    GeneRIF: KLF14 directly downregulates the expression of GPX4 to
            exert antitumor effects by promoting ferroptosis in cervical
            cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Sok,S.P.M., Pipkin,K., Popescu,N.I., Reidy,M., Li,B., Van
            Remmen,H., Kinter,M., Sun,X.H., Fan,Z. and Zhao,M.
  TITLE     Gpx4 Regulates Invariant NKT Cell Homeostasis and Function by
            Preventing Lipid Peroxidation and Ferroptosis
  JOURNAL   J Immunol 213 (7), 941-951 (2024)
   PUBMED   39158281
  REMARK    GeneRIF: Gpx4 Regulates Invariant NKT Cell Homeostasis and Function
            by Preventing Lipid Peroxidation and Ferroptosis.
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Li,X., He,J., Gao,X., Zheng,G., Chen,C., Chen,Y., Xing,Z., Wang,T.,
            Tang,J., Guo,Y. and He,Y.
  TITLE     GPX4 restricts ferroptosis of NKp46+ILC3s to control intestinal
            inflammation
  JOURNAL   Cell Death Dis 15 (9), 687 (2024)
   PUBMED   39300068
  REMARK    GeneRIF: GPX4 restricts ferroptosis of NKp46[+]ILC3s to control
            intestinal inflammation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Sneddon,A.A., Wu,H.C., Farquharson,A., Grant,I., Arthur,J.R.,
            Rotondo,D., Choe,S.N. and Wahle,K.W.
  TITLE     Regulation of selenoprotein GPx4 expression and activity in human
            endothelial cells by fatty acids, cytokines and antioxidants
  JOURNAL   Atherosclerosis 171 (1), 57-65 (2003)
   PUBMED   14642406
  REMARK    GeneRIF: lipids, cytokines and antioxidants modulate GPx4 in a
            complex manner that in the presence of adequate selenium, may
            favour protection against potentially proatherogenic processes.
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Roveri,A., Flohe,L., Maiorino,M. and Ursini,F.
  TITLE     Phospholipid-hydroperoxide glutathione peroxidase in sperm
  JOURNAL   Methods Enzymol 347, 208-212 (2002)
   PUBMED   11898409
  REMARK    GeneRIF: Glutathione peroxidase is a moonlighting protein that
            functions both as a peroxidase as well as a structural protein in
            mature spermatozoa.
REFERENCE   7  (residues 1 to 170)
  AUTHORS   Kelner,M.J. and Montoya,M.A.
  TITLE     Structural organization of the human selenium-dependent
            phospholipid hydroperoxide glutathione peroxidase gene (GPX4):
            chromosomal localization to 19p13.3
  JOURNAL   Biochem Biophys Res Commun 249 (1), 53-55 (1998)
   PUBMED   9705830
REFERENCE   8  (residues 1 to 170)
  AUTHORS   Opalenik,S.R., Ding,Q., Mallery,S.R. and Thompson,J.A.
  TITLE     Glutathione depletion associated with the HIV-1 TAT protein
            mediates the extracellular appearance of acidic fibroblast growth
            factor
  JOURNAL   Arch Biochem Biophys 351 (1), 17-26 (1998)
   PUBMED   9501919
REFERENCE   9  (residues 1 to 170)
  AUTHORS   Esworthy,R.S., Doan,K., Doroshow,J.H. and Chu,F.F.
  TITLE     Cloning and sequencing of the cDNA encoding a human testis
            phospholipid hydroperoxide glutathione peroxidase
  JOURNAL   Gene 144 (2), 317-318 (1994)
   PUBMED   8039723
REFERENCE   10 (residues 1 to 170)
  AUTHORS   Chu,F.F.
  TITLE     The human glutathione peroxidase genes GPX2, GPX3, and GPX4 map to
            chromosomes 14, 5, and 19, respectively
  JOURNAL   Cytogenet Cell Genet 66 (2), 96-98 (1994)
   PUBMED   8287691
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC039849.1.
            
            Summary: The protein encoded by this gene belongs to the
            glutathione peroxidase family, members of which catalyze the
            reduction of hydrogen peroxide, organic hydroperoxides and lipid
            hydroperoxides, and thereby protect cells against oxidative damage.
            Several isozymes of this gene family exist in vertebrates, which
            vary in cellular location and substrate specificity. This isozyme
            has a high preference for lipid hydroperoxides and protects cells
            against membrane lipid peroxidation and cell death. It is also
            required for normal sperm development; thus, it has been identified
            as a 'moonlighting' protein because of its ability to serve dual
            functions as a peroxidase, as well as a structural protein in
            mature spermatozoa. Mutations in this gene are associated with
            Sedaghatian type of spondylometaphyseal dysplasia (SMDS). This
            isozyme is also a selenoprotein, containing the rare amino acid
            selenocysteine (Sec) at its active site. Sec is encoded by the UGA
            codon, which normally signals translation termination. The 3' UTRs
            of selenoprotein mRNAs contain a conserved stem-loop structure,
            designated the Sec insertion sequence (SECIS) element, that is
            necessary for the recognition of UGA as a Sec codon, rather than as
            a stop signal. Transcript variants resulting from alternative
            splicing or use of alternate promoters have been described to
            encode isoforms with different subcellular localization. [provided
            by RefSeq, Dec 2018].
            
            Transcript Variant: This variant (4) uses an alternate promoter,
            which results in translation initiation from an in-frame downstream
            AUG start codon compared to variant 1. The encoded isoform (D) has
            a shorter N-terminus compared to isoform A. A similar isoform in
            rat (S-form) has been reported to be localized to the cytoplasm
            (PMID:9988735).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC039849.1, AK225859.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            multifunctional gene product(s)    :: PMID: 11898409
            protein contains selenocysteine    :: PMID: 8039723
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..170
                     /product="phospholipid hydroperoxide glutathione
                     peroxidase GPX4 isoform D"
                     /EC_number="1.11.1.9"
                     /EC_number="1.11.1.12"
                     /note="phospholipid hydroperoxidase; sperm nucleus
                     glutathione peroxidase; phospholipid hydroperoxide
                     glutathione peroxidase, mitochondrial; epididymis
                     secretory sperm binding protein; selenoprotein GPX4;
                     phospholipid hydroperoxide glutathione peroxidase GPX4"
                     /calculated_mol_wt=19394
     Region          13..166
                     /region_name="GSH_Peroxidase"
                     /note="Glutathione (GSH) peroxidase family; tetrameric
                     selenoenzymes that catalyze the reduction of a variety of
                     hydroperoxides including lipid peroxidases, using GSH as a
                     specific electron donor substrate. GSH peroxidase contains
                     one selenocysteine residue per...; cd00340"
                     /db_xref="CDD:238207"
     Site            order(46,81,136)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            46
                     /site_type="other"
                     /note="Selenocysteine"
     Site            order(80,83,85,88,91,95)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
     CDS             1..170
                     /gene="GPX4"
                     /gene_synonym="GPx-4; GSHPx-4; MCSP; PHGPx; SMDS; snGPx;
                     snPHGPx"
                     /coded_by="NM_001367832.1:69..581"
                     /note="UGA stop codon recoded as selenocysteine; isoform D
                     is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS92476.1"
                     /db_xref="GeneID:2879"
                     /db_xref="HGNC:HGNC:4556"
                     /db_xref="MIM:138322"
ORIGIN      
        1 mcasrddwrc arsmhefsak didghmvnld kyrgfvcivt nvasqugkte vnytqlvdlh
       61 aryaecglri lafpcnqfgk qepgsneeik efaagynvkf dmfskicvng ddahplwkwm
      121 kiqpkgkgil gnaikwnftk flidkngcvv krygpmeepl viekdlphyf
//
LOCUS       NP_001356491             146 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform b [Homo sapiens].
ACCESSION   NP_001356491
VERSION     NP_001356491.1
DBSOURCE    REFSEQ: accession NM_001369562.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 146)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 146)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 146)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 146)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 146)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 146)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 146)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 146)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 146)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 146)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.388648.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..146
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..146
                     /product="large ribosomal subunit protein uL22 isoform b"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=16963
     Region          <1..127
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     CDS             1..146
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369562.1:110..550"
                     /note="isoform b is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS56070.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mhirkatkyl kdvtlqkqcv pfrrynggvg rcaqakqwgw tqgrwpkksa efllhmlkna
       61 esnaelkgld vdslviehiq vnkapkmrrr tyrahgrinp ymsspchiem iltekeqivp
      121 kpeeevaqkk kisqkklkkq klmare
//
LOCUS       NP_001271307             113 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 4 isoform 3 [Homo sapiens].
ACCESSION   NP_001271307 XP_005254572
VERSION     NP_001271307.1
DBSOURCE    REFSEQ: accession NM_001284378.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 113)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 113)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 113)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 113)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 113)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 113)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   7  (residues 1 to 113)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   8  (residues 1 to 113)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   9  (residues 1 to 113)
  AUTHORS   Uys,G.M., Ramburan,A., Loos,B., Kinnear,C.J., Korkie,L.J.,
            Mouton,J., Riedemann,J. and Moolman-Smook,J.C.
  TITLE     Myomegalin is a novel A-kinase anchoring protein involved in the
            phosphorylation of cardiac myosin binding protein C
  JOURNAL   BMC Cell Biol 12, 18 (2011)
   PUBMED   21569246
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 113)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI829264.1 and AW117823.1.
            
            On Oct 1, 2013 this sequence version replaced XP_005254572.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons in the 3' coding region, compared to variant 1. The encoded
            isoform (3) is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM714514.1, CN255954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..113
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.2"
     Protein         1..113
                     /product="COMM domain-containing protein 4 isoform 3"
                     /note="COMM domain-containing protein 4"
                     /calculated_mol_wt=12160
     Region          25..>101
                     /region_name="Commd"
                     /note="COMM_Domain, a family of domains found at the
                     C-terminus of HCarG, the copper metabolism gene MURR1
                     product, and related proteins. Presumably all COMM_Domain
                     containing proteins are located in the nucleus and the
                     COMM domain plays a role in...; cl06336"
                     /db_xref="CDD:471425"
     CDS             1..113
                     /gene="COMMD4"
                     /coded_by="NM_001284378.2:28..369"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS66835.1"
                     /db_xref="GeneID:54939"
                     /db_xref="HGNC:HGNC:26027"
                     /db_xref="MIM:616701"
ORIGIN      
        1 mrfrfcgdld cpdwvlaeis tlakmssvkl rllcsqvlke llgqgidyek ilkltadakf
       61 esgdvkatva vlsfilssaa khsvdgesls selqqlglpk elkqaqtlms slg
//
LOCUS       NP_001353865             429 aa            linear   PRI 20-NOV-2025
DEFINITION  protein prenyltransferase alpha subunit repeat-containing protein 1
            isoform 3 [Homo sapiens].
ACCESSION   NP_001353865 XP_005252033
VERSION     NP_001353865.1
DBSOURCE    REFSEQ: accession NM_001366936.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Shirakawa,R., Goto-Ito,S., Goto,K., Wakayama,S., Kubo,H.,
            Sakata,N., Trinh,D.A., Yamagata,A., Sato,Y., Masumoto,H., Cheng,J.,
            Fujimoto,T., Fukai,S. and Horiuchi,H.
  TITLE     A SNARE geranylgeranyltransferase essential for the organization of
            the Golgi apparatus
  JOURNAL   EMBO J 39 (8), e104120 (2020)
   PUBMED   32128853
  REMARK    GeneRIF: A SNARE geranylgeranyltransferase essential for the
            organization of the Golgi apparatus.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Kuchay,S., Wang,H., Marzio,A., Jain,K., Homer,H., Fehrenbacher,N.,
            Philips,M.R., Zheng,N. and Pagano,M.
  TITLE     GGTase3 is a newly identified geranylgeranyltransferase targeting a
            ubiquitin ligase
  JOURNAL   Nat Struct Mol Biol 26 (7), 628-636 (2019)
   PUBMED   31209342
  REMARK    GeneRIF: This study reports the identification of a previously
            unknown human prenyltransferase complex consisting of an orphan
            prenyltransferase alpha subunit, PTAR1, and the catalytic
            beta-subunit of GGTase2, RabGGTB.
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL162412.11.
            
            On Oct 26, 2018 this sequence version replaced XP_005252033.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.86697.1,
                                           SRR1803615.71611.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.12"
     Protein         1..429
                     /product="protein prenyltransferase alpha subunit
                     repeat-containing protein 1 isoform 3"
                     /note="protein prenyltransferase alpha subunit
                     repeat-containing protein 1"
                     /calculated_mol_wt=49088
     Region          82..>208
                     /region_name="PLN02789"
                     /note="farnesyltranstransferase"
                     /db_xref="CDD:215423"
     Region          216..247
                     /region_name="PPTA"
                     /note="Protein prenyltransferase alpha subunit repeat;
                     pfam01239"
                     /db_xref="CDD:460128"
     Region          292..320
                     /region_name="PPTA"
                     /note="Protein prenyltransferase alpha subunit repeat;
                     pfam01239"
                     /db_xref="CDD:460128"
     CDS             1..429
                     /gene="PTAR1"
                     /coded_by="NM_001366936.1:74..1363"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:375743"
                     /db_xref="HGNC:HGNC:30449"
                     /db_xref="MIM:621024"
ORIGIN      
        1 maetseevav lvqrvvkdit nafrrnphid eiglipcpea rynrspivlv enklgveswc
       61 vkfllpyvhn klllyrtrkq wlnrdelidv tctllllnpd fttawnvrke lilsgtlnpi
      121 kdlhlgklal tkfpkspetw ihrrwvlqql iqetslpsfv tkgnlgtipt eraqrliqee
      181 mevcgeaagr ypsnynawsh riwvlqhlak ldvkilldel sstkhwasmh vsdhsgfhyr
      241 qfllkslisq tvidssvmeq nplrsepalv ppkdeeaavs teeprinlph lleeevefst
      301 dlidsypghe tlwchrrhif ylqhhlngrf phsmtqlspa dspggtlsdl hlipagsqls
      361 qamevdglnd sskqgysqet krlkrtpvpd slglemehrf idqvlstcrn veqarfasay
      421 rkwlvtlsq
//
LOCUS       NP_001265389            1174 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001265389
VERSION     NP_001265389.1
DBSOURCE    REFSEQ: accession NM_001278460.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1174)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1174)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1174)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1174)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1174)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1174)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1174)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1174)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1174)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1174)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK294937.1, AK225849.1, AB023194.1, AC019181.4 and AI261693.1.
            
            Transcript Variant: This variant (3) lacks three alternate in-frame
            exons compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.171625.1, AK225849.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1174
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1174
                     /product="cordon-bleu protein-like 1 isoform 3"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=128485
     Region          106..172
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Region          190..268
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Region          <835..1072
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          1123..1148
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1127..1128,1130..1132,1134..1136,1144..1147)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1144..1147
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     CDS             1..1174
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001278460.2:33..3557"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS92884.1"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mppswsplmc graaeaaass rtpgremgqa vtrrlgagar aaprramdgr tprpqdapar
       61 rkpkakaplp paetkytdvs saadsvesta fimeqkenmi dkdvelsvvl pgdiiksttv
      121 hgskpmmdll iflcaqyhln pssytidlls aeqnhikfkp ntpigmleve kvilkpkmld
      181 kkkptpiipe ktvrvvinfk ktqktivrvs phaslqelap iicskcefdp lhtlllkdyq
      241 sqepldltks lndlglrely amdvnrescq isqnldimke kenkgffsff qrskkkrdqt
      301 asapatplvn khrptftrsn tiskpyisnt lpsdapkkrr aplppmpasq svpqdlahiq
      361 erpascivks msvdetdksp ceagrvrags lqlssmsagn sslrrtkrka psppskipph
      421 qsdensrvta lqpvdgvppd saseanspee lsspagissd ysleeideke elsevpkvea
      481 enispksqdi pfvstdiint lkndpdsalg ngsgefsqns meekqetkst dgqephsvvy
      541 dtsngkkvvd sirnlkslgp nqenvvqnei ivypentedn mkngvkktei nvegvaknnn
      601 idmeverpsn seahetdtai sykenhlaas svpdqklnqp saektkdaai qttpscnsfd
      661 gkhqdhnlsd skveecvqts nnnistqhsc lssqdsvnts refrsqgtli ihsedpltvk
      721 dpicahgndd llppvdridk nstasylkny plyrqdynpk pkpsneitre yipkigmtty
      781 kivppkslei skdwqsetie ykddqdmhal gkkhthenvk etaiqtedsa isespeeplp
      841 nlkpkpnlrt ehqvpssvss pddamvsplk papkmtrdtg tapfapnlee innileskfk
      901 srasnaqakp ssfflqmqkr vsghyvtsaa aksvhaapnp apkeltnkea erdmlpspeq
      961 tlsplskmph svpqplvekt dddvigqapa easpppiapk pvtipasqvs tqnlktlktf
     1021 gaprpysssg pspfalavvk rsqsfskert espsasalvq ppanteegkt hsvnkfvdip
     1081 qlgvsdkenn sahneqnsqi ptptdgpsft vmrqssltfq ssdpeqmrqs lltairsgea
     1141 aaklkrvtip sntisvngrs rlshsmspda qdgh
//
LOCUS       NP_055220                327 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel gamma-4 subunit [Homo sapiens].
ACCESSION   NP_055220 NP_116048
VERSION     NP_055220.1
DBSOURCE    REFSEQ: accession NM_014405.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 327)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 327)
  AUTHORS   Guan,F., Zhang,T., Liu,X., Han,W., Lin,H., Li,L., Chen,G. and Li,T.
  TITLE     Evaluation of voltage-dependent calcium channel gamma gene families
            identified several novel potential susceptible genes to
            schizophrenia
  JOURNAL   Sci Rep 6, 24914 (2016)
   PUBMED   27102562
  REMARK    GeneRIF: These results indicate that CACNG4, CACNG5, CACNG6 and
            CACNG8 may contribute to the risk of SCZ. The statistical epistasis
            identified between CACNG5 and CACNG6 suggests that there may be an
            underlying biological interaction between the two genes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 327)
  AUTHORS   Yang,L., Katchman,A., Morrow,J.P., Doshi,D. and Marx,S.O.
  TITLE     Cardiac L-type calcium channel (Cav1.2) associates with gamma
            subunits
  JOURNAL   FASEB J 25 (3), 928-936 (2011)
   PUBMED   21127204
REFERENCE   4  (residues 1 to 327)
  AUTHORS   Kato,A.S., Gill,M.B., Ho,M.T., Yu,H., Tu,Y., Siuda,E.R., Wang,H.,
            Qian,Y.W., Nisenbaum,E.S., Tomita,S. and Bredt,D.S.
  TITLE     Hippocampal AMPA receptor gating controlled by both TARP and
            cornichon proteins
  JOURNAL   Neuron 68 (6), 1082-1096 (2010)
   PUBMED   21172611
REFERENCE   5  (residues 1 to 327)
  AUTHORS   Sager,C., Tapken,D., Kott,S. and Hollmann,M.
  TITLE     Functional modulation of AMPA receptors by transmembrane AMPA
            receptor regulatory proteins
  JOURNAL   Neuroscience 158 (1), 45-54 (2009)
   PUBMED   18304745
  REMARK    Review article
REFERENCE   6  (residues 1 to 327)
  AUTHORS   Chen,R.S., Deng,T.C., Garcia,T., Sellers,Z.M. and Best,P.M.
  TITLE     Calcium channel gamma subunits: a functionally diverse protein
            family
  JOURNAL   Cell Biochem Biophys 47 (2), 178-186 (2007)
   PUBMED   17652770
  REMARK    Review article
REFERENCE   7  (residues 1 to 327)
  AUTHORS   Moss,F.J., Dolphin,A.C. and Clare,J.J.
  TITLE     Human neuronal stargazin-like proteins, gamma2, gamma3 and gamma4;
            an investigation of their specific localization in human brain and
            their influence on CaV2.1 voltage-dependent calcium channels
            expressed in Xenopus oocytes
  JOURNAL   BMC Neurosci 4, 23 (2003)
   PUBMED   14505496
  REMARK    GeneRIF: examined distribution of the stargazin-like proteins
            gamma2, gamma3, and gamma4 in human CNS: gamma2 is expressed in
            cerebellum, cerebral cortex, hippocampus and thalamus, whereas
            gamma3 abounds in cerebral cortex & amygdala and gamma4 in basal
            ganglia
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 327)
  AUTHORS   Chu,P.J., Robertson,H.M. and Best,P.M.
  TITLE     Calcium channel gamma subunits provide insights into the evolution
            of this gene family
  JOURNAL   Gene 280 (1-2), 37-48 (2001)
   PUBMED   11738816
REFERENCE   9  (residues 1 to 327)
  AUTHORS   Burgess,D.L., Gefrides,L.A., Foreman,P.J. and Noebels,J.L.
  TITLE     A cluster of three novel Ca2+ channel gamma subunit genes on
            chromosome 19q13.4: evolution and expression profile of the gamma
            subunit gene family
  JOURNAL   Genomics 71 (3), 339-350 (2001)
   PUBMED   11170751
REFERENCE   10 (residues 1 to 327)
  AUTHORS   Burgess,D.L., Davis,C.F., Gefrides,L.A. and Noebels,J.L.
  TITLE     Identification of three novel Ca(2+) channel gamma subunit genes
            reveals molecular diversification by tandem and chromosome
            duplication
  JOURNAL   Genome Res 9 (12), 1204-1213 (1999)
   PUBMED   10613843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005988.1, BC034532.1 and
            AC005544.1.
            
            On Nov 4, 2002 this sequence version replaced NP_116048.1.
            
            Summary: The protein encoded by this gene is a type I transmembrane
            AMPA receptor regulatory protein (TARP). TARPs regulate both
            trafficking and channel gating of the AMPA receptors. This gene is
            part of a functionally diverse eight-member protein subfamily of
            the PMP-22/EMP/MP20 family and is located in a cluster with two
            family members, a type II TARP and a calcium channel gamma subunit.
            [provided by RefSeq, Dec 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC034532.1, AF162692.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142348, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000262138.4/ ENSP00000262138.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..327
                     /product="voltage-dependent calcium channel gamma-4
                     subunit"
                     /note="neuronal voltage-gated calcium channel gamma-4
                     subunit; TARP gamma-4; transmembrane AMPAR regulatory
                     protein gamma-4; calcium channel, voltage-dependent, gamma
                     subunit 4"
                     /calculated_mol_wt=36448
     Region          6..202
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            10..30
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            42
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            108..128
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            137..157
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            187..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Region          235..261
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN1.1)"
     Site            259
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JJV4; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN1.1)"
     CDS             1..327
                     /gene="CACNG4"
                     /coded_by="NM_014405.4:206..1189"
                     /db_xref="CCDS:CCDS11667.1"
                     /db_xref="GeneID:27092"
                     /db_xref="HGNC:HGNC:1408"
                     /db_xref="MIM:606404"
ORIGIN      
        1 mvrcdrglqm llttagafaa fslmaiaigt dywlyssahi cngtnltmdd gppprrargd
       61 lthsglwrvc ciegiykghc frinhfpedn dydhdsseyl lrivrassvf pilstillll
      121 gglcigagri ysrknnivls agilfvaagl sniigiivyi ssntgdpsdk rdedkknhyn
      181 ygwsfyfgal sfivaetvgv lavniyiekn kelrfktkre flkasssspy armpsyryrr
      241 rrsrsssrst easpsrdvsp mglkitgaip mgelsmytls replkvttaa syspdqeasf
      301 lqvhdffqqd lkegfhvsml nrrttpv
//
LOCUS       NP_056173                939 aa            linear   PRI 20-NOV-2025
DEFINITION  MORC family CW-type zinc finger protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_056173
VERSION     NP_056173.1
DBSOURCE    REFSEQ: accession NM_015358.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 939)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 939)
  AUTHORS   Champion,A., Rowland,A., Yee,L., van den Boomen,D., Reeves,M.,
            Lehner,P., Sinclair,J. and Poole,E.
  TITLE     MORC3 represses the HCMV major immediate early promoter in myeloid
            cells in the absence of PML nuclear bodies
  JOURNAL   J Med Virol 95 (11), e29227 (2023)
   PUBMED   38009611
  REMARK    GeneRIF: MORC3 represses the HCMV major immediate early promoter in
            myeloid cells in the absence of PML nuclear bodies.
REFERENCE   3  (residues 1 to 939)
  AUTHORS   Ma,X.H., Yao,Y.X., Wang,X.Z., Zhou,Y.P., Huang,S.N., Li,D.,
            Mei,M.J., Wu,J.P., Pan,Y.T., Cheng,S., Jiang,X., Sun,J.Y.,
            Zeng,W.B., Gong,S., Cheng,H., Luo,M.H. and Yang,B.
  TITLE     MORC3 restricts human cytomegalovirus infection by suppressing the
            major immediate-early promoter activity
  JOURNAL   J Med Virol 94 (11), 5492-5506 (2022)
   PUBMED   35879101
  REMARK    GeneRIF: MORC3 restricts human cytomegalovirus infection by
            suppressing the major immediate-early promoter activity.
REFERENCE   4  (residues 1 to 939)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 939)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 939)
  AUTHORS   Takahashi,K., Yoshida,N., Murakami,N., Kawata,K., Ishizaki,H.,
            Tanaka-Okamoto,M., Miyoshi,J., Zinn,A.R., Shime,H. and Inoue,N.
  TITLE     Dynamic regulation of p53 subnuclear localization and senescence by
            MORC3
  JOURNAL   Mol Biol Cell 18 (5), 1701-1709 (2007)
   PUBMED   17332504
  REMARK    GeneRIF: MORC3 (microrchidia3)-ATPase activated p53 and induced
            cellular senescence in normal fibroblasts but not p53-/-
            fibroblasts
REFERENCE   7  (residues 1 to 939)
  AUTHORS   Rosendorff,A., Sakakibara,S., Lu,S., Kieff,E., Xuan,Y., DiBacco,A.,
            Shi,Y., Shi,Y. and Gill,G.
  TITLE     NXP-2 association with SUMO-2 depends on lysines required for
            transcriptional repression
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5308-5313 (2006)
   PUBMED   16567619
  REMARK    GeneRIF: When tethered to a promoter by fusion to Gal4, NXP-2
            repressed transcription, consistent with a role for NXP-2 in
            SUMO-mediated repression
REFERENCE   8  (residues 1 to 939)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   9  (residues 1 to 939)
  AUTHORS   Perry,J. and Zhao,Y.
  TITLE     The CW domain, a structural module shared amongst vertebrates,
            vertebrate-infecting parasites and higher plants
  JOURNAL   Trends Biochem Sci 28 (11), 576-580 (2003)
   PUBMED   14607086
  REMARK    Review article
REFERENCE   10 (residues 1 to 939)
  AUTHORS   Kimura,Y., Sakai,F., Nakano,O., Kisaki,O., Sugimoto,H.,
            Sawamura,T., Sadano,H. and Osumi,T.
  TITLE     The newly identified human nuclear protein NXP-2 possesses three
            distinct domains, the nuclear matrix-binding, RNA-binding, and
            coiled-coil domains
  JOURNAL   J Biol Chem 277 (23), 20611-20617 (2002)
   PUBMED   11927593
  REMARK    GeneRIF: determination of nuclear matrix-binding, RNA-binding, and
            coiled-coil domans
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA702537.1, D50926.2 and
            BC094779.1.
            
            Summary: This gene encodes a protein that localizes to the nuclear
            matrix and forms nuclear bodies via an ATP-dependent mechanism. The
            protein is predicted to have coiled-coil and zinc finger domains
            and has RNA binding activity. Alternative splicing produces
            multiple transcript variants encoding distinct isoforms. [provided
            by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longer protein
            (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094779.1, SRR1660805.178161.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000400485.6/ ENSP00000383333.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..939
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.12"
     Protein         1..939
                     /product="MORC family CW-type zinc finger protein 3
                     isoform 1"
                     /note="zinc finger, CW type with coiled-coil domain 3;
                     nuclear matrix protein NXP2; MORC family CW-type zinc
                     finger protein 3; zinc finger CW-type coiled-coil domain
                     protein 3; nuclear matrix protein 2"
                     /calculated_mol_wt=106982
     Region          18..135
                     /region_name="HATPase_MORC-like"
                     /note="Histidine kinase-like ATPase domain of human
                     microrchidia (MORC) family CW-type zinc finger proteins
                     MORC1-4, and related domains; cd16931"
                     /db_xref="CDD:340408"
     Site            order(35,39,42,65,67,69,71..72,101..104,117,119,128..129,
                     131)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:340408"
     Site            order(82,104)
                     /site_type="other"
                     /note="ATP-lid"
                     /db_xref="CDD:340408"
     Region          249..382
                     /region_name="Morc6_S5"
                     /note="Morc6 ribosomal protein S5 domain 2-like;
                     pfam17942"
                     /db_xref="CDD:465579"
     Region          326..353
                     /region_name="Nuclear matrix binding.
                     /evidence=ECO:0000269|PubMed:11927593"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14149.3)"
     Region          409..446
                     /region_name="zf-CW"
                     /note="CW-type Zinc Finger; pfam07496"
                     /db_xref="CDD:462181"
     Region          500..591
                     /region_name="RNA binding domain"
     Site            503
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14149.3)"
     Site            514
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14149.3)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14149.3)"
     Site            560
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14149.3)"
     Region          613..640
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14149.3)"
     Region          673..>866
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Site            765
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14149.3)"
     Region          <808..>936
                     /region_name="ClpA"
                     /note="ATP-dependent Clp protease, ATP-binding subunit
                     ClpA [Posttranslational modification, protein turnover,
                     chaperones]; COG0542"
                     /db_xref="CDD:440308"
     CDS             1..939
                     /gene="MORC3"
                     /gene_synonym="NXP2; ZCW5; ZCWCC3"
                     /coded_by="NM_015358.3:69..2888"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42924.1"
                     /db_xref="GeneID:23515"
                     /db_xref="HGNC:HGNC:23572"
                     /db_xref="MIM:610078"
ORIGIN      
        1 maaqpprgir lsalcpkflh tnstshtwpf savaelidna ydpdvnakqi widktvindh
       61 icltftdngn gmtsdklhkm lsfgfsdkvt mnghvpvgly gngfksgsmr lgkdaivftk
      121 ngesmsvgll sqtylevika ehvvvpivaf nkhrqminla eskaslaail ehslfsteqk
      181 llaeldaiig kkgtriiiwn lrsyknatef dfekdkydir ipedldeitg kkgykkqerm
      241 dqiapesdys lraycsilyl kprmqiilrg qkvktqlvsk slayierdvy rpkflsktvr
      301 itfgfncrnk dhygimmyhr nrlikayekv gcqlrannmg vgvvgiiecn flkpthnkqd
      361 fdytneyrlt italgeklnd ywnemkvkkn teyplnlpve diqkrpdqtw vqcdaclkwr
      421 klpdgmdqlp ekwycsnnpd pqfrncevpe epededlvhp tyektykktn kekfrirqpe
      481 miprinaell frptalstps fsspkesvpr rhlsegtnsy atrllnnhqv ppqsepesns
      541 lkrrlstrss ilnaknrrls sqfensvykg ddddedviil eenstpkpav dhdidmkseq
      601 shveqggvqv efvgdsepcg qtgststsss rcdqgntaat qtevpslvvk keetvedeid
      661 vrndavilps cveaeakihe tqettdksad dagcqlqelr nqlllvteek enykrqchmf
      721 tdqikvlqqr ilemndkyvk ketchqstet davfllesin gksespdhmv sqyqqaleei
      781 erlkkqcsal qhvkaecsqc snnesksemd emavqlddvf rqldkcsier dqyksevell
      841 emeksqirsq ceelkteveq lkstnqqtat dvstssniee svnhmdgesl klrslrvnvg
      901 qllamivpdl dlqqvnydvd vvdeilgqvv eqmseisst
//
LOCUS       NP_001356484             189 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform c [Homo sapiens].
ACCESSION   NP_001356484
VERSION     NP_001356484.1
DBSOURCE    REFSEQ: accession NM_001369555.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 189)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 189)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 189)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 189)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 189)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 189)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 189)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 189)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 189)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 189)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..189
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..189
                     /product="large ribosomal subunit protein uL22 isoform c"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21826
     Region          1..170
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(20..21,43..45,47..48,50..51,104..109,117..122,
                     154..155)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(23,25,28,30..32,35,39,42,102,106,109,121,123..125,
                     127,130,142..147)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     CDS             1..189
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369555.1:22..591"
                     /note="isoform c is encoded by transcript variant 9"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkckwtgac ksrgsnlrvh fkntretaqa ikgmhirkat kylkdvtlqk
       61 qcvpfrryng gvgrcaqakq wgwtqgrwpk ksaefllhml knaesnaelk gldvdslvie
      121 hiqvnkapkm rrrtyrahgr inpymsspch iemiltekeq ivpkpeeeva qkkkisqkkl
      181 kkqklmare
//
LOCUS       NP_003066               1214 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF complex subunit SMARCC2 isoform a [Homo sapiens].
ACCESSION   NP_003066
VERSION     NP_003066.2
DBSOURCE    REFSEQ: accession NM_003075.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1214)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1214)
  AUTHORS   Bosch,E., Popp,B., Guse,E., Skinner,C., van der Sluijs,P.J.,
            Maystadt,I., Pinto,A.M., Renieri,A., Bruno,L.P., Granata,S.,
            Marcelis,C., Baysal,O., Hartwich,D., Holthofer,L., Isidor,B.,
            Cogne,B., Wieczorek,D., Capra,V., Scala,M., De Marco,P.,
            Ognibene,M., Jamra,R.A., Platzer,K., Carter,L.B., Kuismin,O., van
            Haeringen,A., Maroofian,R., Valenzuela,I., Cusco,I.,
            Martinez-Agosto,J.A., Rabani,A.M., Mefford,H.C., Pereira,E.M.,
            Close,C., Anyane-Yeboa,K., Wagner,M., Hannibal,M.C., Zacher,P.,
            Thiffault,I., Beunders,G., Umair,M., Bhola,P.T., McGinnis,E.,
            Millichap,J., van de Kamp,J.M., Prijoles,E.J., Dobson,A.,
            Shillington,A., Graham,B.H., Garcia,E.J., Galindo,M.K.,
            Ropers,F.G., Nibbeling,E.A.R., Hubbard,G., Karimov,C., Goj,G.,
            Bend,R., Rath,J., Morrow,M.M., Millan,F., Salpietro,V., Torella,A.,
            Nigro,V., Kurki,M., Stevenson,R.E., Santen,G.W.E., Zweier,M.,
            Campeau,P.M., Severino,M., Reis,A., Accogli,A. and Vasileiou,G.
  TITLE     Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals
  JOURNAL   Genet Med 25 (11), 100950 (2023)
   PUBMED   37551667
  REMARK    GeneRIF: Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals.
REFERENCE   3  (residues 1 to 1214)
  AUTHORS   Liu,S., Liu,P., Zhu,C., Yang,R., He,Z., Li,Y., Li,Y., Fei,X.,
            Hou,J., Wang,X. and Pan,Y.
  TITLE     FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination
  JOURNAL   Aging (Albany NY) 15 (12), 5381-5398 (2023)
   PUBMED   37348029
  REMARK    GeneRIF: FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination.
            Erratum:[Aging (Albany NY). 2023 Sep 14;15(17):9230-9232. doi:
            10.18632/aging.205071. PMID: 37708091]
REFERENCE   4  (residues 1 to 1214)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1214)
  AUTHORS   Li,C., Wang,T., Gu,J., Qi,S., Li,J., Chen,L., Wu,H., Shi,L.,
            Song,C., Li,H., Zhu,L., Lu,Y. and Zhou,Q.
  TITLE     SMARCC2 mediates the regulation of DKK1 by the transcription factor
            EGR1 through chromatin remodeling to reduce the proliferative
            capacity of glioblastoma
  JOURNAL   Cell Death Dis 13 (11), 990 (2022)
   PUBMED   36418306
  REMARK    GeneRIF: SMARCC2 mediates the regulation of DKK1 by the
            transcription factor EGR1 through chromatin remodeling to reduce
            the proliferative capacity of glioblastoma.
            Erratum:[Cell Death Dis. 2022 Dec 12;13(12):1033. doi:
            10.1038/s41419-022-05498-x. PMID: 36509739]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1214)
  AUTHORS   Wang,W., Chi,T., Xue,Y., Zhou,S., Kuo,A. and Crabtree,G.R.
  TITLE     Architectural DNA binding by a high-mobility-group/kinesin-like
            subunit in mammalian SWI/SNF-related complexes
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 492-498 (1998)
   PUBMED   9435219
REFERENCE   7  (residues 1 to 1214)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   8  (residues 1 to 1214)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   9  (residues 1 to 1214)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   10 (residues 1 to 1214)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY118539.1, AK315153.1,
            BC009067.1, CX165574.1 and BM875330.1.
            
            On May 28, 2002 this sequence version replaced NP_003066.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and contains a predicted
            leucine zipper motif typical of many transcription factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (1) encodes isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026222.3, SRR11853560.7021.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1214
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..1214
                     /product="SWI/SNF complex subunit SMARCC2 isoform a"
                     /note="chromatin remodeling complex BAF170 subunit;
                     SWI3-like protein; SWI/SNF complex 170 kDa subunit;
                     mammalian chromatin remodeling complex BRG1-associated
                     factor 170; SWI/SNF complex subunit SMARCC2; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin subfamily c member 2"
                     /calculated_mol_wt=132749
     Region          1..274
                     /region_name="MarR-like, BRCT and chromo domains module.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01376"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          4..420
                     /region_name="SWIRM-assoc_2"
                     /note="SWIRM-associated domain at the N-terminal;
                     pfam16496"
                     /db_xref="CDD:465143"
     Region          257..413
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            283
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            326
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          379..>708
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Site            387
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PDG5; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          684..750
                     /region_name="SWIRM-assoc_3"
                     /note="SWIRM-associated domain at the C-terminal;
                     pfam16498"
                     /db_xref="CDD:465145"
     Region          <690..947
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          724..852
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          <880..946
                     /region_name="SWIRM-assoc_1"
                     /note="SWIRM-associated region 1; pfam16495"
                     /db_xref="CDD:465142"
     Region          947..983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          <968..1203
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          997..1092
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     Region          1182..1214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAQ2.1)"
     CDS             1..1214
                     /gene="SMARCC2"
                     /gene_synonym="BAF170; CRACC2; CSS8; Rsc8"
                     /coded_by="NM_003075.5:23..3667"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8907.1"
                     /db_xref="GeneID:6601"
                     /db_xref="HGNC:HGNC:11105"
                     /db_xref="MIM:601734"
ORIGIN      
        1 mavrkkdggp nvkyyeaadt vtqfdnvrlw lgknykkyiq aepptnksls slvvqllqfq
       61 eevfgkhvsn apltklpikc fldfkaggsl chilaaaykf ksdqgwrryd fqnpsrmdrn
      121 vemfmtieks lvqnnclsrp niflcpeiep kllgklkdii krhqgtvted knnashvvyp
      181 vpgnleeeew vrpvmkrdkq vllhwgyypd sydtwipase ieasvedapt pekprkvhak
      241 wildtdtfne wmneedyevn ddknpvsrrk kisaktltde vnspdsdrrd kkggnykkrk
      301 rspspsptpe akkknakkgp stpytkskrg hreeeqedlt kdmdepspvp nveevtlpkt
      361 vntkkdsesa pvkggtmtdl deqedesmet tgkdedenst gnkgeqtknp dlhednvteq
      421 thhiiipsya awfdynsvha ierralpeff ngknksktpe iylayrnfmi dtyrlnpqey
      481 ltstacrrnl agdvcaimrv hafleqwgli nyqvdaesrp tpmgppptsh fhvladtpsg
      541 lvplqpktpq qtsasqqmln fpdkgkekpt dmqnfglrtd mytkknvpsk skaaasatre
      601 wteqetllll ealemykddw nkvsehvgsr tqdecilhfl rlpiedpyle dseaslgpla
      661 yqpipfsqsg npvmstvafl asvvdprvas aaaksaleef skmkeevpta lveahvrkve
      721 eaakvtgkad pafglessgi agttsdeper ieesgndear vegqatdekk epkepreggg
      781 aieeeakekt seapkkdeek gkegdsekes eksdgdpivd pekekepkeg qeevlkevve
      841 segerktkve rdigegnlst aaaaalaaaa vkakhlaave erkikslval lvetqmkkle
      901 iklrhfeele timdrereal eyqrqqllad rqafhmeqlk yaemrarqqh fqqmhqqqqq
      961 pppalppgsq pipptgaagp pavhglavap asvvpapags gappgslgps eqigqagsta
     1021 gpqqqqpaga pqpgavppgv pppgphgpsp fpnqqtppsm mpgavpgsgh pgvagnaplg
     1081 lpfgmppppp ppapsiipfg sladsisinl pappnlhghh hhlpfapgtl pppnlpvsma
     1141 nplhpnlpat ttmpsslplg pglgsaaaqs paivaavqgn llpsasplpd pgtplppdpt
     1201 apspgtvtpv pppq
//
LOCUS       NP_001340208             178 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 2 [Homo sapiens].
ACCESSION   NP_001340208 XP_016869048
VERSION     NP_001340208.1
DBSOURCE    REFSEQ: accession NM_001353279.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869048.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.232953.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..178
                     /product="CYFIP-related Rac1 interactor B isoform 2"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=20062
     Region          <1..174
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..178
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353279.1:682..1218"
                     /note="isoform 2 is encoded by transcript variant 41"
                     /db_xref="CCDS:CCDS83327.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mtnpaiqndf syyrrtlsrm rinnvpaege nevnnelanr mslfyaeatp mlktlsdatt
       61 kfvsenknlp ienttdclst masvcrvmle tpeyrsrftn eetvsfclrv mvgviilydh
      121 vhpvgafakt skidmkgcik vlkdqppnsv egllnalryt tkhlndetts kqiksmlq
//
LOCUS       NP_620614               1572 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF-related matrix-associated actin-dependent regulator of
            chromatin subfamily A member 2 isoform b [Homo sapiens].
ACCESSION   NP_620614
VERSION     NP_620614.2
DBSOURCE    REFSEQ: accession NM_139045.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1572)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1572)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z., Liu,Q., Zhang,Y., Xiong,S.
            and Zhang,S.
  TITLE     Expression of SMARCA2 and SMARCA4 in gastric adenocarcinoma and
            construction of a nomogram prognostic model
  JOURNAL   Int J Clin Oncol 28 (11), 1487-1500 (2023)
   PUBMED   37634210
  REMARK    GeneRIF: Expression of SMARCA2 and SMARCA4 in gastric
            adenocarcinoma and construction of a nomogram prognostic model.
REFERENCE   3  (residues 1 to 1572)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1572)
  AUTHORS   Zhang,Z., Li,Q., Sun,S., Li,Z., Cui,Z.G., Zhang,M., Liu,Q.,
            Zhang,Y., Xiong,S. and Zhang,S.
  TITLE     Clinicopathological and prognostic significance of SWI/SNF complex
            subunits in undifferentiated gastric carcinoma
  JOURNAL   World J Surg Oncol 20 (1), 383 (2022)
   PUBMED   36464671
  REMARK    GeneRIF: Clinicopathological and prognostic significance of SWI/SNF
            complex subunits in undifferentiated gastric carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1572)
  AUTHORS   Zhang,X., Chen,H., Song,Y., Chen,Z., Liu,X., Rong,P. and Ma,R.
  TITLE     Ten-year follow-up of Nicolaides-Baraitser syndrome with a de novo
            mutation and analysis of 58 gene loci of SMARCA2-associated NCBRS
  JOURNAL   Mol Genet Genomic Med 10 (9), e2009 (2022)
   PUBMED   35811451
  REMARK    GeneRIF: Ten-year follow-up of Nicolaides-Baraitser syndrome with a
            de novo mutation and analysis of 58 gene loci of SMARCA2-associated
            NCBRS.
REFERENCE   6  (residues 1 to 1572)
  AUTHORS   Aves,S.J., Hindley,J., Phear,G.A. and Tongue,N.
  TITLE     A fission yeast gene mapping close to suc1 encodes a protein
            containing two bromodomains
  JOURNAL   Mol Gen Genet 248 (4), 491-498 (1995)
   PUBMED   7565614
REFERENCE   7  (residues 1 to 1572)
  AUTHORS   Chiba,H., Muramatsu,M., Nomoto,A. and Kato,H.
  TITLE     Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
            Drosophila brahma are transcriptional coactivators cooperating with
            the estrogen receptor and the retinoic acid receptor
  JOURNAL   Nucleic Acids Res 22 (10), 1815-1820 (1994)
   PUBMED   8208605
REFERENCE   8  (residues 1 to 1572)
  AUTHORS   Muchardt,C., Yaniv,M. and Mattei,M.G.
  TITLE     Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2
            and Drosophila brm genes, to chromosome region 9p23-p24, by in situ
            hybridization
  JOURNAL   Mamm Genome 5 (4), 241-243 (1994)
   PUBMED   8012116
REFERENCE   9  (residues 1 to 1572)
  AUTHORS   Muchardt,C. and Yaniv,M.
  TITLE     A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and
            Drosophila brm genes potentiates transcriptional activation by the
            glucocorticoid receptor
  JOURNAL   EMBO J 12 (11), 4279-4290 (1993)
   PUBMED   8223438
REFERENCE   10 (residues 1 to 1572)
  AUTHORS   Abdul-Rahman,O. and May,F.
  TITLE     SMARCA2-Related Nicolaides-Baraitser Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26468571
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC040029.1, BC068252.1,
            X72889.1, BC066596.1 and AK094076.1.
            
            On Jun 4, 2004 this sequence version replaced NP_620614.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins and is highly similar to the brahma
            protein of Drosophila. Members of this family have helicase and
            ATPase activities and are thought to regulate transcription of
            certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI, which is required for
            transcriptional activation of genes normally repressed by
            chromatin. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene, which contains a
            trinucleotide repeat (CAG) length polymorphism. [provided by
            RefSeq, Jan 2014].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1965299,
                              SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1572
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p24.3"
     Protein         1..1572
                     /product="SWI/SNF-related matrix-associated
                     actin-dependent regulator of chromatin subfamily A member
                     2 isoform b"
                     /note="global transcription activator homologous sequence;
                     SNF2-alpha; sucrose nonfermenting 2-like protein 2;
                     SNF2/SWI2-like protein 2; SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     a2; brahma homolog; probable global transcription
                     activator SNF2L2; BAF190B; protein brahma homolog;
                     BRG1-associated factor 190B; ATP-dependent helicase
                     SMARCA2; putative global transcription activator SNF2L2;
                     SWI/SNF related, matrix associated, actin dependent
                     regulator of chromatin, subfamily a, member 2"
                     /calculated_mol_wt=179151
     Region          1..71
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          <46..>450
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          95..176
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            172
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          173..207
                     /region_name="QLQ"
                     /note="pfam08880"
                     /db_xref="CDD:462622"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            190
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          212..334
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            316
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Region          436..508
                     /region_name="HSA"
                     /note="domain in helicases and associated with SANT
                     domains; smart00573"
                     /db_xref="CDD:214727"
     Region          551..592
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          589..632
                     /region_name="BRK"
                     /note="BRK domain; pfam07533"
                     /db_xref="CDD:462196"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            604
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6DIC0; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          627..672
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            666
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            670
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P51532; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          701..951
                     /region_name="DEXHc_SMARCA2"
                     /note="DEXH-box helicase domain of SMARCA2; cd18063"
                     /db_xref="CDD:350821"
     Region          720..>1202
                     /region_name="PLN03142"
                     /note="Probable chromatin-remodeling complex ATPase chain;
                     Provisional"
                     /db_xref="CDD:215601"
     Site            order(751..757,791,851..852)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350821"
     Region          851..854
                     /region_name="DEGH box"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            997
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            999
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1259..1326
                     /region_name="SnAC"
                     /note="Snf2-ATP coupling, chromatin remodelling complex;
                     pfam14619"
                     /db_xref="CDD:464219"
     Region          1333..>1395
                     /region_name="Bromodomain"
                     /note="Bromodomains are found in many chromatin-associated
                     proteins and in nuclear histone acetyltransferases. They
                     interact specifically with acetylated lysine; cl02556"
                     /db_xref="CDD:445827"
     Region          1344..1383
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Region          1382..1488
                     /region_name="Bromo_SNF2L2"
                     /note="Bromodomain, SNF2L2-like subfamily, specific to
                     animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related
                     matrix-associated actin-dependent regulator of chromatin
                     subfamily A member 2 is a global transcriptional
                     activator, which cooperates with nuclear hormone...;
                     cd05516"
                     /db_xref="CDD:99947"
     Site            order(1413,1418,1421,1460,1464,1470)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99947"
     Region          1488..1572
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1510
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     Site            1550
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P51531.2)"
     Site            1554
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P51531.2)"
     CDS             1..1572
                     /gene="SMARCA2"
                     /gene_synonym="BAF190; BIS; BRM; hBRM; hSNF2a; NCBRS;
                     SAMRCA2; SNF2; SNF2L2; SNF2LA; Sth1p; SWI2"
                     /coded_by="NM_139045.4:95..4813"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS34978.1"
                     /db_xref="GeneID:6595"
                     /db_xref="HGNC:HGNC:11098"
                     /db_xref="MIM:600014"
ORIGIN      
        1 mstptdpgam phpgpspgpg pspgpilgps pgpgpspgsv hsmmgpspgp psvshpmptm
       61 gstdfpqegm hqmhkpidgi hdkgivedih cgsmkgtgmr pphpgmgppq spmdqhsqgy
      121 msphpsplga pehvsspmsg ggptppqmpp sqpgalipgd pqamsqpnrg pspfspvqlh
      181 qlraqilayk mlargqplpe tlqlavqgkr tlpglqqqqq qqqqqqqqqq qqqqqqqqpq
      241 qqppqpqtqq qqqpalvnyn rpsgpgpels gpstpqklpv papggrpspa ppaaaqppaa
      301 avpgpsvpqp apgqpspvlq lqqkqsrisp iqkpqgldpv eilqereyrl qariahriqe
      361 lenlpgslpp dlrtkatvel kalrllnfqr qlrqevvacm rrdttletal nskaykrskr
      421 qtlrearmte klekqqkieq erkrrqkhqe ylnsilqhak dfkeyhrsva gkiqklskav
      481 atwhantere qkketeriek ermrrlmaed eegyrklidq kkdrrlayll qqtdeyvanl
      541 tnlvwehkqa qaakekkkrr rrkkkaeena eggesalgpd gepidessqm sdlpvkvtht
      601 etgkvlfgpe apkasqldaw lemnpgyeva prsdseesds dyeeedeeee ssrqeteeki
      661 lldpnseevs ekdakqiiet akqdvddeys mqysargsqs yytvahaise rvekqsalli
      721 ngtlkhyqlq glewmvslyn nnlngilade mglgktiqti alitylmehk rlngpyliiv
      781 plstlsnwty efdkwapsvv kisykgtpam rrslvpqlrs gkfnvlltty eyiikdkhil
      841 akirwkymiv deghrmknhh ckltqvlnth yvaprrillt gtplqnklpe lwallnfllp
      901 tifkscstfe qwfnapfamt gervdlneee tiliirrlhk vlrpfllrrl kkevesqlpe
      961 kveyvikcdm salqkilyrh mqakgilltd gsekdkkgkg gaktlmntim qlrkicnhpy
     1021 mfqhieesfa ehlgysngvi ngaelyrasg kfelldrilp klratnhrvl lfcqmtslmt
     1081 imedyfafrn flylrldgtt ksedraallk kfnepgsqyf ifllstragg lglnlqaadt
     1141 vvifdsdwnp hqdlqaqdra hrigqqnevr vlrlctvnsv eekilaaaky klnvdqkviq
     1201 agmfdqksss herraflqai leheeeneee devpddetln qmiarreeef dlfmrmdmdr
     1261 rredarnpkr kprlmeedel pswiikddae verltceeee ekifgrgsrq rrdvdysdal
     1321 tekqwlraie dgnleemeee vrlkkrkrrr nvdkdpaked vekakkrrgr ppaeklspnp
     1381 pkltkqmnai idtvinykds sgrqlsevfi qlpsrkelpe yyelirkpvd fkkikerirn
     1441 hkyrslgdle kdvmllchna qtfnlegsqi yedsivlqsv fksarqkiak eeesedesne
     1501 eeeeedeees eseaksvkvk iklnkkddkg rdkgkgkkrp nrgkakpvvs dfdsdeeqde
     1561 reqsegsgtd de
//
LOCUS       NP_001275645             888 aa            linear   PRI 20-NOV-2025
DEFINITION  catenin delta-2 isoform 3 [Homo sapiens].
ACCESSION   NP_001275645 XP_005248312
VERSION     NP_001275645.1
DBSOURCE    REFSEQ: accession NM_001288716.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Assendorp,N., Fossati,M., Libe-Philippot,B., Christopoulou,E.,
            Depp,M., Rapone,R., Dingli,F., Loew,D., Vanderhaeghen,P. and
            Charrier,C.
  TITLE     CTNND2 moderates the pace of synaptic maturation and links human
            evolution to synaptic neoteny
  JOURNAL   Cell Rep 43 (10), 114797 (2024)
   PUBMED   39352808
  REMARK    GeneRIF: CTNND2 moderates the pace of synaptic maturation and links
            human evolution to synaptic neoteny.
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Pauly,M., Krumbiegel,M., Trumpp,S., Braig,S., Rupprecht,T.,
            Kraus,C., Uebe,S., Reis,A. and Vasileiou,G.
  TITLE     Severe manifestation of Rauch-Azzarello syndrome associated with
            biallelic deletion of CTNND2
  JOURNAL   Clin Genet 106 (2), 180-186 (2024)
   PUBMED   38604781
  REMARK    GeneRIF: Severe manifestation of Rauch-Azzarello syndrome
            associated with biallelic deletion of CTNND2.
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Li,M., Nopparat,J., Aguilar,B.J., Chen,Y.H., Zhang,J., Du,J.,
            Ai,X., Luo,Y., Jiang,Y., Boykin,C. and Lu,Q.
  TITLE     Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression
  JOURNAL   Oncogene 39 (22), 4358-4374 (2020)
   PUBMED   32313227
  REMARK    GeneRIF: Intratumor delta-catenin heterogeneity driven by genomic
            rearrangement dictates growth factor dependent prostate cancer
            progression.
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Lu,Q., Paredes,M., Medina,M., Zhou,J., Cavallo,R., Peifer,M.,
            Orecchio,L. and Kosik,K.S.
  TITLE     delta-catenin, an adhesive junction-associated protein which
            promotes cell scattering
  JOURNAL   J Cell Biol 144 (3), 519-532 (1999)
   PUBMED   9971746
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Paffenholz,R. and Franke,W.W.
  TITLE     Identification and localization of a neurally expressed member of
            the plakoglobin/armadillo multigene family
  JOURNAL   Differentiation 61 (5), 293-304 (1997)
   PUBMED   9342840
REFERENCE   9  (residues 1 to 888)
  AUTHORS   Zhou,J., Liyanage,U., Medina,M., Ho,C., Simmons,A.D., Lovett,M. and
            Kosik,K.S.
  TITLE     Presenilin 1 interaction in the brain with a novel member of the
            Armadillo family
  JOURNAL   Neuroreport 8 (8), 2085-2090 (1997)
   PUBMED   9223106
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Simmons,A.D., Overhauser,J. and Lovett,M.
  TITLE     Isolation of cDNAs from the Cri-du-chat critical region by direct
            screening of a chromosome 5-specific cDNA library
  JOURNAL   Genome Res 7 (2), 118-127 (1997)
   PUBMED   9049630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC332925.1, AK299300.1,
            AF035302.1, DB571461.1, AI680877.1 and AC010626.6.
            
            On Jan 1, 2014 this sequence version replaced XP_005248312.1.
            
            Summary: This gene encodes an adhesive junction associated protein
            of the armadillo/beta-catenin superfamily and is implicated in
            brain and eye development and cancer formation. The protein encoded
            by this gene promotes the disruption of E-cadherin based adherens
            junction to favor cell spreading upon stimulation by hepatocyte
            growth factor. This gene is overexpressed in prostate
            adenocarcinomas and is associated with decreased expression of
            tumor suppressor E-cadherin in this tissue. This gene resides in a
            region of the short arm of chromosome 5 that is deleted in Cri du
            Chat syndrome. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Dec
            2013].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            coding region, uses a downstream start codon, and lacks two
            alternate exons in the 5' coding region, compared to variant 1.
            The resulting protein (isoform 3) has a shorter and distinct
            N-terminus compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.9060.1,
                                           SRR1803614.205907.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p15.2"
     Protein         1..888
                     /product="catenin delta-2 isoform 3"
                     /note="catenin (cadherin-associated protein), delta 2
                     (neural plakophilin-related arm-repeat protein); T-cell
                     delta-catenin; neurojungin"
                     /calculated_mol_wt=97849
     Region          213..>386
                     /region_name="PLN03200"
                     /note="cellulose synthase-interactive protein;
                     Provisional"
                     /db_xref="CDD:215629"
     Region          215..240
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(231,235,239,273,277,281,318,322,326)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          244..284
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          248..284
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          288..329
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          292..327
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          334..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          497..538
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          501..538
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          548..583
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          548..582
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          589..635
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          637..681
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          641..676
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     CDS             1..888
                     /gene="CTNND2"
                     /gene_synonym="GT24; NPRAP"
                     /coded_by="NM_001288716.1:272..2938"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75227.1"
                     /db_xref="GeneID:1501"
                     /db_xref="HGNC:HGNC:2516"
                     /db_xref="MIM:604275"
ORIGIN      
        1 mssmssaeeq fqwqsqdgqk diedelttgl elvdscirsl qesgildpqd ystgetgsra
       61 syssqhghlg pelralqspe hhidpiyedr vyqkppmrsl sqsqgdplpp ahtgtyrtst
      121 apsspgvdsv plqrtgsqhg pqnaaaatfq rasyaagpas nyadpyrqlq ycpsvespys
      181 ksgpalppeg tlarspsids iqkdprefgw rdpelpeviq mlqhqfpsvq snaaaylqhl
      241 cfgdnkikae irrqggiqll vdlldhrmte vhrsacgalr nlvygkandd nkialkncgg
      301 ipalvrllrk ttdleirelv tgvlwnlssc dalkmpiiqd alavltnavi iphsgwensp
      361 lqddrkiqlh ssqvlrnatg clrnvssage earrrmrecd gltdallyvi qsalgsseid
      421 sktvencvci lrnlsyrlaa etsqgqhmgt deldgllcge angkdaessg cwgkkkkkkk
      481 sqdqwdgvgp lpdcaeppkg iqmlwhpsiv kpyltllsec snpdtlegaa galqnlaags
      541 wkwsvyiraa vrkekglpil vellridndr vvcavatalr nmaldvrnke ligkyamrdl
      601 vhrlpggnns nntaskamsd dtvtavcctl hevitknmen akalrdaggi eklvgisksk
      661 gdkhspkvvk aasqvlnsmw qyrdlrslyk kdgwsqyhfv assstierdr qrpysssrtp
      721 sispvrvspn nrsasapasp remislkerk tdyectgsna tyhgakgeht srkdamtaqn
      781 tgistlyrns ygapaedikh nqvsaqpvpq epsrkdyety qpfqnstrny desffedqvh
      841 hrppaseytm hlglkstgny vdfysaarpy selnyetshy paspdswv
//
LOCUS       NP_001350918             489 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit alpha
            isoform 1 [Homo sapiens].
ACCESSION   NP_001350918
VERSION     NP_001350918.1
DBSOURCE    REFSEQ: accession NM_001363989.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Lin,J., Xia,H., Yu,J., Wang,Y., Wang,H., Xie,D., Cheng,C., Lu,L.,
            Bian,T., Wu,Y. and Liu,Q.
  TITLE     circADAMTS6 via stabilizing CAMK2A is involved in smoking-induced
            emphysema through driving M2 macrophage polarization
  JOURNAL   Environ Int 190, 108832 (2024)
   PUBMED   38936066
  REMARK    GeneRIF: circADAMTS6 via stabilizing CAMK2A is involved in
            smoking-induced emphysema through driving M2 macrophage
            polarization.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,Y., Xia,M., Zhao,T., Zhang,Q., Li,R. and Yang,L.
  TITLE     Camk2a suppresses denervated muscle atrophy by maintaining the Ca2+
            homeostasis in muscle cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (11), 25-29 (2023)
   PUBMED   38015546
  REMARK    GeneRIF: Camk2a suppresses denervated muscle atrophy by maintaining
            the Ca2+ homeostasis in muscle cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Alphonse,N., Wanford,J.J., Voak,A.A., Gay,J., Venkhaya,S.,
            Burroughs,O., Mathew,S., Lee,T., Evans,S.L., Zhao,W., Frowde,K.,
            Alrehaili,A., Dickenson,R.E., Munk,M., Panina,S., Mahmood,I.F.,
            Llorian,M., Stanifer,M.L., Boulant,S., Berchtold,M.W.,
            Bergeron,J.R.C., Wack,A., Lesser,C.F. and Odendall,C.
  TITLE     A family of conserved bacterial virulence factors dampens
            interferon responses by blocking calcium signaling
  JOURNAL   Cell 185 (13), 2354-2369 (2022)
   PUBMED   35568036
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Bredt,D.S., Ferris,C.D. and Snyder,S.H.
  TITLE     Nitric oxide synthase regulatory sites. Phosphorylation by cyclic
            AMP-dependent protein kinase, protein kinase C, and
            calcium/calmodulin protein kinase; identification of flavin and
            calmodulin binding sites
  JOURNAL   J Biol Chem 267 (16), 10976-10981 (1992)
   PUBMED   1375933
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Wegner,M., Cao,Z. and Rosenfeld,M.G.
  TITLE     Calcium-regulated phosphorylation within the leucine zipper of
            C/EBP beta
  JOURNAL   Science 256 (5055), 370-373 (1992)
   PUBMED   1314426
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Tokui,T., Yamauchi,T., Yano,T., Nishi,Y., Kusagawa,M., Yatani,R.
            and Inagaki,M.
  TITLE     Ca2(+)-calmodulin-dependent protein kinase II phosphorylates
            various types of non-epithelial intermediate filament proteins
  JOURNAL   Biochem Biophys Res Commun 169 (3), 896-904 (1990)
   PUBMED   2114109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011372.7.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinases family, and to the Ca(2+)/calmodulin-dependent
            protein kinases subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. This calcium
            calmodulin-dependent protein kinase is composed of four different
            chains: alpha, beta, gamma, and delta. The alpha chain encoded by
            this gene is required for hippocampal long-term potentiation (LTP)
            and spatial learning. In addition to its calcium-calmodulin
            (CaM)-dependent activity, this protein can undergo
            autophosphorylation, resulting in CaM-independent activity. Several
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.162921.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..489
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit alpha isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II alpha; CaM-kinase II alpha chain;
                     calcium/calmodulin-dependent protein kinase II alpha-B
                     subunit; CaM kinase II alpha subunit; CaMK-II alpha
                     subunit; calcium/calmodulin-dependent protein kinase type
                     II alpha chain; calcium/calmodulin-dependent protein
                     kinase type II subunit alpha; caMK-II subunit alpha; caM
                     kinase II subunit alpha"
                     /calculated_mol_wt=55189
     Region          11..302
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(19..23,27,40,42,73,89..92,96,98,134..135,137,
                     139..140,142,155..156,159,174..178,180)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(19..22,27,40,42,73,89..92,96,139..140,142,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(23,96,98,134..135,137,139,159,174..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(155..165,168..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(293,295..302)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          357..484
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..489
                     /gene="CAMK2A"
                     /gene_synonym="CAMKA; CaMKIIalpha; CaMKIINalpha; MRD53;
                     MRT63"
                     /coded_by="NM_001363989.1:335..1804"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS43387.1"
                     /db_xref="GeneID:815"
                     /db_xref="HGNC:HGNC:1460"
                     /db_xref="MIM:114078"
ORIGIN      
        1 matitctrft eeyqlfeelg kgafsvvrrc vkvlagqeya akiintkkls ardhqklere
       61 aricrllkhp nivrlhdsis eeghhylifd lvtggelfed ivareyysea dashciqqil
      121 eavlhchqmg vvhrdlkpen lllasklkga avkladfgla ievegeqqaw fgfagtpgyl
      181 spevlrkdpy gkpvdlwacg vilyillvgy ppfwdedqhr lyqqikagay dfpspewdtv
      241 tpeakdlink mltinpskri taaealkhpw ishrstvasc mhrqetvdcl kkfnarrklk
      301 gailttmlat rnfsggksgg nkksdgvkkr kssssvqlme ssestnttie dedtkvrkqe
      361 iikvteqlie aisngdfesy tkmcdpgmta fepealgnlv egldfhrfyf enlwsrnskp
      421 vhttilnphi hlmgdesaci ayiritqyld aggiprtaqs eetrvwhrrd gkwqivhfhr
      481 sgapsvlph
//
LOCUS       NP_001288073             296 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase TRIM69 isoform c [Homo sapiens].
ACCESSION   NP_001288073 XP_005254220
VERSION     NP_001288073.1
DBSOURCE    REFSEQ: accession NM_001301144.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Sun,L., Chen,Y., Xia,L., Wang,J., Zhu,J., Li,J., Wang,K., Shen,K.,
            Zhang,D., Zhang,G., Shi,T. and Chen,W.
  TITLE     TRIM69 suppressed the anoikis resistance and metastasis of gastric
            cancer through ubiquitin-proteasome-mediated degradation of PRKCD
  JOURNAL   Oncogene 42 (49), 3619-3632 (2023)
   PUBMED   37864033
  REMARK    GeneRIF: TRIM69 suppressed the anoikis resistance and metastasis of
            gastric cancer through ubiquitin-proteasome-mediated degradation of
            PRKCD.
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Wang,Y., Risteski,P., Yang,Y., Chen,H., Droby,G., Walens,A.,
            Jayaprakash,D., Troester,M., Herring,L., Chernoff,J., Tolic,I.M.,
            Bowser,J. and Vaziri,C.
  TITLE     The TRIM69-MST2 signaling axis regulates centrosome dynamics and
            chromosome segregation
  JOURNAL   Nucleic Acids Res 51 (19), 10568-10589 (2023)
   PUBMED   37739411
  REMARK    GeneRIF: The TRIM69-MST2 signaling axis regulates centrosome
            dynamics and chromosome segregation.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Yuan,J., Lv,T., Yang,J., Wu,Z., Yan,L., Yang,J. and Shi,Y.
  TITLE     HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability by
            diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma
  JOURNAL   Redox Biol 58, 102546 (2022)
   PUBMED   36423520
  REMARK    GeneRIF: HDLBP-stabilized lncFAL inhibits ferroptosis vulnerability
            by diminishing Trim69-dependent FSP1 degradation in hepatocellular
            carcinoma.
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Song,Y., Nguyen,X.N., Kumar,A., da Silva,C., Picard,L., Etienne,L.
            and Cimarelli,A.
  TITLE     Trim69 is a microtubule regulator that acts as a pantropic viral
            inhibitor
  JOURNAL   Proc Natl Acad Sci U S A 119 (43), e2211467119 (2022)
   PUBMED   36251989
  REMARK    GeneRIF: Trim69 is a microtubule regulator that acts as a pantropic
            viral inhibitor.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Han,Y., Li,R., Gao,J., Miao,S. and Wang,L.
  TITLE     Characterisation of human RING finger protein TRIM69, a novel
            testis E3 ubiquitin ligase and its subcellular localisation
  JOURNAL   Biochem Biophys Res Commun 429 (1-2), 6-11 (2012)
   PUBMED   23131556
  REMARK    GeneRIF: hTRIM69 is a novel E3 ubiquitin ligase identified from
            human testis and may function to ubiquitinate its particular
            substrates during spermatogenesis.
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Bahmanyar,S., Kaplan,D.D., Deluca,J.G., Giddings,T.H. Jr.,
            O'Toole,E.T., Winey,M., Salmon,E.D., Casey,P.J., Nelson,W.J. and
            Barth,A.I.
  TITLE     beta-Catenin is a Nek2 substrate involved in centrosome separation
  JOURNAL   Genes Dev 22 (1), 91-105 (2008)
   PUBMED   18086858
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     Forced expression of RNF36 induces cell apoptosis
  JOURNAL   Exp Cell Res 287 (2), 301-313 (2003)
   PUBMED   12837286
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Shyu,H.W., Hsu,S.H., Hsieh-Li,H.M. and Li,H.
  TITLE     A novel member of the RBCC family, Trif, expressed specifically in
            the spermatids of mouse testis
  JOURNAL   Mech Dev 108 (1-2), 213-216 (2001)
   PUBMED   11578878
  REMARK    GeneRIF: Gene and protein analysis of the mouse counterpart.
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI827618.1, AF302088.1,
            AC122108.2 and DB524904.1.
            
            On Jul 23, 2014 this sequence version replaced XP_005254220.1.
            
            Summary: This gene encodes a member of the RING-B-box-coiled-coil
            (RBCC) family and encodes a protein with an N-terminal RING finger
            motif, a PRY domain and a C-terminal SPRY domain. The mouse
            ortholog of this gene is specifically expressed in germ cells at
            the round spermatid stages during spermatogenesis and, when
            overexpressed, induces apoptosis. Alternatively spliced transcript
            variants encoding distinct isoforms have been described. [provided
            by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (c) lacks an alternate exon and
            uses an alternate splice site, and it thus differs in its 5' UTR
            and initiates translation at a downstream in-frame start codon,
            compared to variant a. The encoded isoform (c, also known as
            TRIMLESS alpha) is shorter at the N-terminus, compared to isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.49591.1, AF302088.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..296
                     /product="E3 ubiquitin-protein ligase TRIM69 isoform c"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 36; RFP-like domain-containing
                     protein trimless; E3 ubiquitin-protein ligase TRIM69;
                     RING-type E3 ubiquitin transferase TRIM69"
                     /calculated_mol_wt=33902
     Region          107..293
                     /region_name="SPRY_PRY_TRIM69"
                     /note="PRY/SPRY domain in tripartite motif-binding protein
                     69 (TRIM69), also known as RING finger protein 36 (RNF36);
                     cd15818"
                     /db_xref="CDD:293990"
     CDS             1..296
                     /gene="TRIM69"
                     /gene_synonym="HSD-34; HSD34; RNF36; Trif"
                     /coded_by="NM_001301144.2:321..1211"
                     /note="isoform c is encoded by transcript variant c"
                     /db_xref="CCDS:CCDS73719.1"
                     /db_xref="GeneID:140691"
                     /db_xref="HGNC:HGNC:17857"
                     /db_xref="MIM:616017"
ORIGIN      
        1 meflklhqfl hskekdilte lreegkalne emelnlsqlq eqcllakdml vsiqakteqq
       61 nsfdflkdit tllhsleqgm kvlatrelis rklnlgqykg piqymvwrem qdtlcpglsp
      121 ltldpktahp nlvlsksqts vwhgdikkim pddperfdss vavlgsrgft sgkwywevev
      181 akktkwtvgv vresiirkgs cpltpeqgfw llrlrnqtdl kaldlpsfsl tltnnldkvg
      241 iyldyeggql sfynaktmth iytfsntfme klypyfcpcl ndggenkepl hilhpq
//
LOCUS       NP_001157974             811 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 4E transporter isoform b
            [Homo sapiens].
ACCESSION   NP_001157974
VERSION     NP_001157974.1
DBSOURCE    REFSEQ: accession NM_001164502.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 811)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 811)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 811)
  AUTHORS   Ding,Y., Chen,S., Jin,J., Sun,Y., Chu,C., Kee,K., Xin,M. and Li,L.
  TITLE     POI-associated EIF4ENIF1 mutations exhibit impaired translation
            regulation abilities
  JOURNAL   Gene 917, 148456 (2024)
   PUBMED   38604507
  REMARK    GeneRIF: POI-associated EIF4ENIF1 mutations exhibit impaired
            translation regulation abilities.
REFERENCE   4  (residues 1 to 811)
  AUTHORS   Zuberek,J., Warzecha,M., Dobrowolski,M. and Modrak-Wojcik,A.
  TITLE     An intramolecular disulphide bond in human 4E-T affects its binding
            to eIF4E1a protein
  JOURNAL   Eur Biophys J 52 (6-7), 497-510 (2023)
   PUBMED   37798395
  REMARK    GeneRIF: An intramolecular disulphide bond in human 4E-T affects
            its binding to eIF4E1a protein.
REFERENCE   5  (residues 1 to 811)
  AUTHORS   Shang,L., Ren,S., Yang,X., Zhang,F., Jin,L., Zhang,X. and Wu,Y.
  TITLE     EIF4ENIF1 variants in two patients with non-syndromic premature
            ovarian insufficiency
  JOURNAL   Eur J Med Genet 65 (10), 104597 (2022)
   PUBMED   36030004
  REMARK    GeneRIF: EIF4ENIF1 variants in two patients with non-syndromic
            premature ovarian insufficiency.
REFERENCE   6  (residues 1 to 811)
  AUTHORS   Andrei,M.A., Ingelfinger,D., Heintzmann,R., Achsel,T.,
            Rivera-Pomar,R. and Luhrmann,R.
  TITLE     A role for eIF4E and eIF4E-transporter in targeting mRNPs to
            mammalian processing bodies
  JOURNAL   RNA 11 (5), 717-727 (2005)
   PUBMED   15840819
  REMARK    GeneRIF: human P bodies contain the cap-binding protein eIF4E and
            the related factor eIF4E-transporter (eIF4E-T), suggesting novel
            roles for these proteins in targeting mRNAs for 5' --> 3'
            degradation
REFERENCE   7  (residues 1 to 811)
  AUTHORS   Ballif,B.A., Villen,J., Beausoleil,S.A., Schwartz,D. and Gygi,S.P.
  TITLE     Phosphoproteomic analysis of the developing mouse brain
  JOURNAL   Mol Cell Proteomics 3 (11), 1093-1101 (2004)
   PUBMED   15345747
REFERENCE   8  (residues 1 to 811)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   9  (residues 1 to 811)
  AUTHORS   Warner,D.R., Roberts,E.A., Greene,R.M. and Pisano,M.M.
  TITLE     Identification of novel Smad binding proteins
  JOURNAL   Biochem Biophys Res Commun 312 (4), 1185-1190 (2003)
   PUBMED   14651998
REFERENCE   10 (residues 1 to 811)
  AUTHORS   Dostie,J., Ferraiuolo,M., Pause,A., Adam,S.A. and Sonenberg,N.
  TITLE     A novel shuttling protein, 4E-T, mediates the nuclear import of the
            mRNA 5' cap-binding protein, eIF4E
  JOURNAL   EMBO J 19 (12), 3142-3156 (2000)
   PUBMED   10856257
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK314636.1 and BC032941.1.
            
            Summary: The protein encoded by this gene is a nucleocytoplasmic
            shuttle protein for the translation initiation factor eIF4E. This
            shuttle protein interacts with the importin alpha-beta complex to
            mediate nuclear import of eIF4E. It is predominantly cytoplasmic;
            its own nuclear import is regulated by a nuclear localization
            signal and nuclear export signals. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2009].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            segment in the coding region compared to variant 1. The resulting
            isoform (b) has the same N- and C-termini but is shorter compared
            to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032941.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..811
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..811
                     /product="eukaryotic translation initiation factor 4E
                     transporter isoform b"
                     /note="2610509L04Rik; eukaryotic translation initiation
                     factor 4E transporter; eIF4E transporter; 4E-transporter"
                     /calculated_mol_wt=88095
     Region          <100..537
                     /region_name="EIF4E-T"
                     /note="Nucleocytoplasmic shuttling protein for mRNA
                     cap-binding EIF4E; pfam10477"
                     /db_xref="CDD:371079"
     Region          574..>761
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     CDS             1..811
                     /gene="EIF4ENIF1"
                     /gene_synonym="4E-T; Clast4"
                     /coded_by="NM_001164502.2:177..2612"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS54520.1"
                     /db_xref="GeneID:56478"
                     /db_xref="HGNC:HGNC:16687"
                     /db_xref="MIM:607445"
ORIGIN      
        1 mdrrsmgete sgdafldlkk ppaskcphry tkeelldike lphskqrpsc lsekydsdgv
       61 wdpekwhasl ypasgrsspv eslkkeldtd rpslvrrivg ivecnggvae edevevilaq
      121 epaadqevpr davlpeqspg dfdfneffnl dkvpclasmi edvlgegsvs asrfsrwfsn
      181 psrsgsrsss lgstpheele rlagleqail spgqnsgnyf apipledhae nkvdilemlq
      241 kakvdlkpll sslsankekl kesshsgvvl sveeveaglk glkvdqqvkn stpfmaehle
      301 etlsavtnnr qlkkdgdmta fnklvstmkr nleshlmspa eipgqpvpkn ilqellgqpv
      361 qrpassnlls glmgsleptt sllgqrapsp plsqvfqtra asadylrpri pspigftpgp
      421 qqllgdpfqg mrkpmspita qqmsqlelqq aaleglalph dlavqaanfy qpgfgkpqvd
      481 rtrdgfrnrq qrvtkspapv hrgnssspap aasitsmlsp sftptsvirk myeskekske
      541 epasgkaalg dskedtqkas eenllssssv psadrdsspt tnsklsalqr sscstplsqa
      601 nrytkeqdyr pkatgrktpt laspvpttpf lrpvhqvplv phvpmvrpah qlhpglvqrm
      661 laqgvhpqhl psllqtgvlp pgmdlshlqg isgpilgqpf yplpaashpl lnprpgtplh
      721 lamvqqqlqr svlhppgsgs haaavsvqtt pqnvpsrsgl phmhsqlehr psqrssspvg
      781 lakwfgsdvl qqplpsmpak visvdeleyr q
//
LOCUS       NP_620135                730 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 5 isoform 1 [Homo sapiens].
ACCESSION   NP_620135
VERSION     NP_620135.1
DBSOURCE    REFSEQ: accession NM_138780.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Huang,D., Zeng,Y., Deng,H.Y., Fu,B.D., Ke,Y., Luo,J.Y., Yu,J.C. and
            Yu,S.T.
  TITLE     SYTL5 Promotes Papillary Thyroid Carcinoma Progression by Enhancing
            Activation of the NF-kappaB Signaling Pathway
  JOURNAL   Endocrinology 164 (1) (2022)
   PUBMED   36378561
  REMARK    GeneRIF: SYTL5 Promotes Papillary Thyroid Carcinoma Progression by
            Enhancing Activation of the NF-kappaB Signaling Pathway.
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   8  (residues 1 to 730)
  AUTHORS   Colvin,R.A., Means,T.K., Diefenbach,T.J., Moita,L.F., Friday,R.P.,
            Sever,S., Campanella,G.S., Abrazinski,T., Manice,L.A., Moita,C.,
            Andrews,N.W., Wu,D., Hacohen,N. and Luster,A.D.
  TITLE     Synaptotagmin-mediated vesicle fusion regulates cell migration
  JOURNAL   Nat Immunol 11 (6), 495-502 (2010)
   PUBMED   20473299
REFERENCE   9  (residues 1 to 730)
  AUTHORS   Saxena,S.K., Horiuchi,H. and Fukuda,M.
  TITLE     Rab27a regulates epithelial sodium channel (ENaC) activity through
            synaptotagmin-like protein (SLP-5) and Munc13-4 effector mechanism
  JOURNAL   Biochem Biophys Res Commun 344 (2), 651-657 (2006)
   PUBMED   16630545
  REMARK    GeneRIF: These observations decisively prove that Rab27a inhibits
            ENaC function through a complex mechanism that involves GTP/GDP
            status, and protein-protein interactions involving Munc13-4 and
            SLP-5 effector proteins.
REFERENCE   10 (residues 1 to 730)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     Synaptotagmin-like protein 5: a novel Rab27A effector with
            C-terminal tandem C2 domains
  JOURNAL   Biochem Biophys Res Commun 293 (3), 899-906 (2002)
   PUBMED   12051743
  REMARK    GeneRIF: molecular cloning of slp5:a novel Rab27A effector with
            C-terminal tandem C2 domains
            GeneRIF: Synaptotagmin-like protein 5 (Slp5) contains an N-terminal
            Slp homology domain (SHD) (PMID: 11327731). The SHD of Slp5
            specifically and directly binds the GTP-bound form of Rab27A.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121578.1, BX647688.1,
            AK125106.1, AB080222.1 and AL135038.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the
            synaptotagmin-like (Slp) protein family, which contains a unique
            homology domain at the N-terminus, referred to as the Slp homology
            domain (SHD). The SHD functions as a binding site for Rab27A, which
            plays a role in protein transport. Expression of this gene is
            restricted to placenta and liver, suggesting that it might be
            involved in Rab27A-dependent membrane trafficking in specific
            tissues. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2009].
            
            Transcript Variant: This variant (1) encodes the shorter isoform
            (1). Variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AB080222.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968540, SAMEA2142348 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000297875.7/ ENSP00000297875.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..730
                     /product="synaptotagmin-like protein 5 isoform 1"
                     /note="exophilin 9; synaptotagmin-like protein 5"
                     /calculated_mol_wt=81392
     Region          11..123
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          62..108
                     /region_name="FYVE_Slp5"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 5 (Slp5) and similar proteins; cd15766"
                     /db_xref="CDD:277305"
     Region          147..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDW5.1)"
     Site            147
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80T23; propagated from
                     UniProtKB/Swiss-Prot (Q8TDW5.1)"
     Region          217..271
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDW5.1)"
     Region          <218..>392
                     /region_name="AF-4"
                     /note="AF-4 proto-oncoprotein N-terminal region;
                     pfam05110"
                     /db_xref="CDD:461550"
     Region          294..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TDW5.1)"
     Region          407..530
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Region          544..722
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..730
                     /gene="SYTL5"
                     /gene_synonym="slp5"
                     /coded_by="NM_138780.3:473..2665"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14244.1"
                     /db_xref="GeneID:94122"
                     /db_xref="HGNC:HGNC:15589"
                     /db_xref="MIM:301126"
ORIGIN      
        1 msknsefinl sflldhekem ilgvlkrdey lkkvedkrir klknelleak rrsgktqqea
       61 srvcvhchrn lglifdrgdp cqacslrvcr ecrvagpngs wkctvcdkia qlriitgewf
      121 feekakrfkq vnvlgtdvvr qsilrrspga eevqsqeqtr qdaeksdtsp vagkkashdg
      181 pkrkgfllsk frsatrgeii tpktdtgrsy sldldgqhfr slksppgsdr gstgssdlnd
      241 qepgprtpks srsngvtpgt qsspapstrt vtsvisreyg fensmdlaai egtsqeltks
      301 hrrntsgtps iavsgtslss dqsrseldls esftedsedt vsirsksvpg aldkdsleet
      361 eesidalvss qlstnthrla sglsttslns mmsvysetgd ygnvkvsgei llhisycykt
      421 gglyifvknc rnlaigdekk qrtdayvksy llpdksrnnk rktkirtgtn pefnetlkyt
      481 ishtqletrt lqlsvwhydr fgrnsflgev eipfdswnfe nptdewfvlq pkvefapdig
      541 lqykgeltvv lryippeenl mlppeqlqgn ktfkkgkkke spvisggile vfikeaknlt
      601 avksggtsds fvkgyllpdd skatkhktlv ikksvnpqwn htfmfsgihp qdiknvclel
      661 tiwdkeafss niflggvrln sgsgvshgkn vdwmdsqgee qrlwqkmann pgtpfegvlm
      721 lrssmgkcrl
//
LOCUS       NP_001243237             545 aa            linear   PRI 20-NOV-2025
DEFINITION  dystrobrevin beta isoform 8 [Homo sapiens].
ACCESSION   NP_001243237
VERSION     NP_001243237.1
DBSOURCE    REFSEQ: accession NM_001256308.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 545)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 545)
  AUTHORS   Prokopenko,D., Lee,S., Hecker,J., Mullin,K., Morgan,S.,
            Katsumata,Y., Weiner,M.W., Fardo,D.W., Laird,N., Bertram,L.,
            Hide,W., Lange,C. and Tanzi,R.E.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative (ADNI)
  TITLE     Region-based analysis of rare genomic variants in whole-genome
            sequencing datasets reveal two novel Alzheimer's disease-associated
            genes: DTNB and DLG2
  JOURNAL   Mol Psychiatry 27 (4), 1963-1969 (2022)
   PUBMED   35246634
  REMARK    GeneRIF: Region-based analysis of rare genomic variants in
            whole-genome sequencing datasets reveal two novel Alzheimer's
            disease-associated genes: DTNB and DLG2.
REFERENCE   3  (residues 1 to 545)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 545)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 545)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 545)
  AUTHORS   Piluso,G., Mirabella,M., Ricci,E., Belsito,A., Abbondanza,C.,
            Servidei,S., Puca,A.A., Tonali,P., Puca,G.A. and Nigro,V.
  TITLE     Gamma1- and gamma2-syntrophins, two novel dystrophin-binding
            proteins localized in neuronal cells
  JOURNAL   J Biol Chem 275 (21), 15851-15860 (2000)
   PUBMED   10747910
REFERENCE   7  (residues 1 to 545)
  AUTHORS   Blake,D.J., Hawkes,R., Benson,M.A. and Beesley,P.W.
  TITLE     Different dystrophin-like complexes are expressed in neurons and
            glia
  JOURNAL   J Cell Biol 147 (3), 645-658 (1999)
   PUBMED   10545507
REFERENCE   8  (residues 1 to 545)
  AUTHORS   Puca,A.A., Nigro,V., Piluso,G., Belsito,A., Sampaolo,S.,
            Quaderi,N., Rossi,E., Di Iorio,G., Ballabio,A. and Franco,B.
  TITLE     Identification and characterization of a novel member of the
            dystrobrevin gene family
  JOURNAL   FEBS Lett 425 (1), 7-13 (1998)
   PUBMED   9540997
REFERENCE   9  (residues 1 to 545)
  AUTHORS   Peters,M.F., O'Brien,K.F., Sadoulet-Puccio,H.M., Kunkel,L.M.,
            Adams,M.E. and Froehner,S.C.
  TITLE     beta-dystrobrevin, a new member of the dystrophin family.
            Identification, cloning, and protein associations
  JOURNAL   J Biol Chem 272 (50), 31561-31569 (1997)
   PUBMED   9395493
REFERENCE   10 (residues 1 to 545)
  AUTHORS   Straub,V. and Campbell,K.P.
  TITLE     Muscular dystrophies and the dystrophin-glycoprotein complex
  JOURNAL   Curr Opin Neurol 10 (2), 168-175 (1997)
   PUBMED   9146999
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK301386.1, AC010150.3,
            AC019144.9 and BC016655.1.
            
            Summary: This gene encodes dystrobrevin beta, a component of the
            dystrophin-associated protein complex (DPC). The DPC consists of
            dystrophin and several integral and peripheral membrane proteins,
            including dystroglycans, sarcoglycans, syntrophins and dystrobrevin
            alpha and beta. The DPC localizes to the sarcolemma and its
            disruption is associated with various forms of muscular dystrophy.
            Dystrobrevin beta is thought to interact with syntrophin and the
            DP71 short form of dystrophin. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK301386.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..545
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..545
                     /product="dystrobrevin beta isoform 8"
                     /note="DTN-B; beta-dystrobrevin"
                     /calculated_mol_wt=61408
     Region          1..157
                     /region_name="EFh_DMD_DYTN_DTN"
                     /note="EF-hand-like motif found in the
                     dystrophin/dystrobrevin/dystrotelin family; cl07621"
                     /db_xref="CDD:352774"
     Region          1..37
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:319999"
     Region          47..81
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:319999"
     Region          87..123
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:319999"
     Region          134..157
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:319999"
     Region          184..232
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(186,189,201,204,210,213,223,227)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(186,189,210,213)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(187,198,200,206,208)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(199,214,229,232)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(201,204,223,227)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     Region          <343..>485
                     /region_name="EnvC"
                     /note="Septal ring factor EnvC, activator of murein
                     hydrolases AmiA and AmiB [Cell cycle control, cell
                     division, chromosome partitioning]; COG4942"
                     /db_xref="CDD:443969"
     CDS             1..545
                     /gene="DTNB"
                     /coded_by="NM_001256308.2:306..1943"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:1838"
                     /db_xref="HGNC:HGNC:3058"
                     /db_xref="MIM:602415"
ORIGIN      
        1 mieafrdngl ntldhtteis vsrletviss iyyqlnkrlp sthqisveqs islllnfmia
       61 aydsegrgkl tvfsvkamla tmcggkmldk lryvfsqmsd snglmifskf dqflkevlkl
      121 ptavfegpsf gytehsvrtc fpqqrkimln mfldtmmadp ppqclvwlpl mhrlahvenv
      181 fhpvecsycr cesmmgfryr cqqchnyqlc qncfwrghag gphsnqhqmk ehsswkspak
      241 klshaisksl gcvptrepph pvfpeqpekp ldlahivppr pltnmndtmv shmssgvptp
      301 tkrlqysqdi pshladehal iasyvarlqh carvldspsr ldeehrliar yaarlaaeag
      361 nvtrpptdls fnfdankqqr qliaelenkn reilqeiqrl rleheqasqp tpekaqqnpt
      421 llaelrllrq rkdeleqrms alqesrrelm vqleelmkll kaqatgspht spthgggrpm
      481 pmpvrstsag stpthcpqds lsgvggdvqe afaqgtrrnl rndllvaads itntmsslvk
      541 elhsg
//
LOCUS       NP_003330                147 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D2 isoform 1 [Homo sapiens].
ACCESSION   NP_003330
VERSION     NP_003330.1
DBSOURCE    REFSEQ: accession NM_003339.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Yan,R., Zeng,S., Gao,F., Li,L. and Xiao,X.
  TITLE     CircUBE2D2 regulates HMGB1 through miR-885-5p to promote ovarian
            cancer malignancy
  JOURNAL   Clinics (Sao Paulo) 79, 100391 (2024)
   PUBMED   38848634
  REMARK    GeneRIF: CircUBE2D2 regulates HMGB1 through miR-885-5p to promote
            ovarian cancer malignancy.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Critchley,W.R., Smith,G.A., Zachary,I.C., Harrison,M.A. and
            Ponnambalam,S.
  TITLE     The E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2D2 regulate
            VEGFR2 dynamics and endothelial function
  JOURNAL   J Cell Sci 136 (10) (2023)
   PUBMED   37226882
  REMARK    GeneRIF: The E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2D2
            regulate VEGFR2 dynamics and endothelial function.
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Hatakeyama,S., Jensen,J.P. and Weissman,A.M.
  TITLE     Subcellular localization and ubiquitin-conjugating enzyme (E2)
            interactions of mammalian HECT family ubiquitin protein ligases
  JOURNAL   J Biol Chem 272 (24), 15085-15092 (1997)
   PUBMED   9182527
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Jensen,J.P., Bates,P.W., Yang,M., Vierstra,R.D. and Weissman,A.M.
  TITLE     Identification of a family of closely related human ubiquitin
            conjugating enzymes
  JOURNAL   J Biol Chem 270 (51), 30408-30414 (1995)
   PUBMED   8530467
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Rolfe,M., Beer-Romero,P., Glass,S., Eckstein,J., Berdo,I.,
            Theodoras,A., Pagano,M. and Draetta,G.
  TITLE     Reconstitution of p53-ubiquitinylation reactions from purified
            components: the role of human ubiquitin-conjugating enzyme UBC4 and
            E6-associated protein (E6AP)
  JOURNAL   Proc Natl Acad Sci U S A 92 (8), 3264-3268 (1995)
   PUBMED   7724550
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Scheffner,M., Huibregtse,J.M. and Howley,P.M.
  TITLE     Identification of a human ubiquitin-conjugating enzyme that
            mediates the E6-AP-dependent ubiquitination of p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 8797-8801 (1994)
   PUBMED   8090726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC033349.1, AK001311.1,
            AK001428.1 and AF317220.1.
            
            Summary: Regulated degradation of misfolded, damaged or short-lived
            proteins in eukaryotes occurs via the ubiquitin (Ub)-proteasome
            system (UPS). An integral part of the UPS system is the
            ubiquitination of target proteins and covalent linkage of
            Ub-containing proteins to form polymeric chains, marking them as
            targets for 26S proteasome-mediated degradation. Ubiquitination of
            proteins is mediated by a cascade of enzymes which includes E1
            (ubiquitin activating), E2 (ubiquitin conjugating), and E3
            (ubiquitin ligases) enzymes. This gene encodes a member of the E2
            enzyme family. Substrates of this enzyme include the tumor
            suppressor protein p53 and peroxisomal biogenesis factor 5 (PEX5).
            Alternative splicing results in multiple transcript variants of
            this gene. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001428.1, SRR3476690.977885.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398733.8/ ENSP00000381717.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D2 isoform 1"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2D 2 (homologous to
                     yeast UBC4/5); ubiquitin-conjugating enzyme E2-17 kDa 2;
                     ubiquitin conjugating enzyme E2D 2; ubiquitin-protein
                     ligase D2; ubiquitin carrier protein D2; E2
                     ubiquitin-conjugating enzyme D2; p53-regulated
                     ubiquitin-conjugating enzyme 1; (E3-independent) E2
                     ubiquitin-conjugating enzyme D2"
                     /calculated_mol_wt=16604
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="UBE2D2"
                     /gene_synonym="E2(17)KB2; PUBC1; UBC4; UBC4/5; UBCH4;
                     UBCH5B"
                     /coded_by="NM_003339.3:454..897"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43369.1"
                     /db_xref="GeneID:7322"
                     /db_xref="HGNC:HGNC:12475"
                     /db_xref="MIM:602962"
ORIGIN      
        1 malkrihkel ndlardppaq csagpvgddm fhwqatimgp ndspyqggvf fltihfptdy
       61 pfkppkvaft triyhpnins ngsicldilr sqwspaltis kvllsicsll cdpnpddplv
      121 peiariyktd rekynriare wtqkyam
//
LOCUS       NP_001338571             960 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            6 [Homo sapiens].
ACCESSION   NP_001338571 XP_016884614
VERSION     NP_001338571.1
DBSOURCE    REFSEQ: accession NM_001351642.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 960)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 960)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 960)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 960)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 960)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 960)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 960)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 960)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 960)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 960)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, AL954743.9,
            AL671545.13 and AL096767.14.
            
            On May 17, 2017 this sequence version replaced XP_016884614.1.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.160895.1,
                                           SRR1803611.119132.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..960
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..960
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 6"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=104175
     Region          128..532
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Site            289
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          408..436
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          657..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Region          <701..955
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            772
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8R3Q2; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     Region          813..850
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75170.2)"
     Site            822
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75170.2)"
     CDS             1..960
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001351642.2:372..3254"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesqdcveq llknmfdgdr tesclvsgtq vlltlletrr vgteglvdsf sqglersyav
      301 sssvlhgiep rlkdfhqlll nppkkkailt tigvleeplg narlhgarlm aallhtntps
      361 inqelcrlnt mdllldlffk ytwnnflhfq velciaails haareertea sgsesrvepp
      421 hengnrslet pqpaaslpdn tmvthlfqkc clvqrileaw eandhtqaag gmrrgnmghl
      481 trianavvqn lergpvqthi sevirglpad crgrwesfve etltetnrrn tvdlvsthhl
      541 hsssededie gafpnelslq qafsdyqiqq mtanfvdqfg fndeefadqd dninapfdri
      601 aeinfnidad edspsaalfe accsdriqpf dddedediwe dsdtrcaarv marprfgaph
      661 asescskngp erggqdgkas leahrdapga gappapgkke appvegdsea gamwtavfde
      721 panstptapg vvrdvgssvw aagtsapeek gwakftdfqp fccsesgprc sspvdtecsh
      781 aegsrsqgpe kafspaspca wnvcvtrkap llasdssssg gshsedgdqk aasamdavsr
      841 gpgreapplp tvarteeavg rvgcadsrll spacpapkev taapavavpp eatvaittal
      901 skagpaiptp avssalavav plgpimavta apamvatlgt vtkdgktdap pegaalngpv
//
LOCUS       NP_079067                491 aa            linear   PRI 20-NOV-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF4 isoform 2 [Homo
            sapiens].
ACCESSION   NP_079067
VERSION     NP_079067.3
DBSOURCE    REFSEQ: accession NM_024791.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Pouly,D., Chenaux,S., Martin,V., Babis,M., Koch,R., Nagoshi,E.,
            Katanaev,V.L., Gachon,F. and Staub,O.
  TITLE     USP2-45 Is a Circadian Clock Output Effector Regulating Calcium
            Absorption at the Post-Translational Level
  JOURNAL   PLoS One 11 (1), e0145155 (2016)
   PUBMED   26756164
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Reid,H.M., Turner,E.C., Mulvaney,E.P., Hyland,P.B., McLean,C. and
            Kinsella,B.T.
  TITLE     Interaction of the human prostacyclin receptor and the NHERF4
            family member intestinal and kidney enriched PDZ protein (IKEPP)
  JOURNAL   Biochim Biophys Acta 1823 (10), 1998-2012 (2012)
   PUBMED   22884631
  REMARK    GeneRIF: IKEPP was also found to be expressed in vascular
            endothelial cells where it co-localizes and complexes with the hIP
            Erratum:[Biochim Biophys Acta. 2015 Jan;1853(1):63-4]
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Zachos,N.C., Hodson,C., Kovbasnjuk,O., Li,X., Thelin,W.R., Cha,B.,
            Milgram,S. and Donowitz,M.
  TITLE     Elevated intracellular calcium stimulates NHE3 activity by an IKEPP
            (NHERF4) dependent mechanism
  JOURNAL   Cell Physiol Biochem 22 (5-6), 693-704 (2008)
   PUBMED   19088451
  REMARK    GeneRIF: Regulation of NHE3 depends on the nature of the NHERF
            family member associating with NHE3 and the accompanying NHE3
            complexes.
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Thelin,W.R., Hodson,C.A. and Milgram,S.L.
  TITLE     Beyond the brush border: NHERF4 blazes new NHERF turf
  JOURNAL   J Physiol 567 (Pt 1), 13-19 (2005)
   PUBMED   15994182
  REMARK    Review article
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Kato,Y., Sai,Y., Yoshida,K., Watanabe,C., Hirata,T. and Tsuji,A.
  TITLE     PDZK1 directly regulates the function of organic cation/carnitine
            transporter OCTN2
  JOURNAL   Mol Pharmacol 67 (3), 734-743 (2005)
   PUBMED   15523054
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Hegedus,T., Sessler,T., Scott,R., Thelin,W., Bakos,E., Varadi,A.,
            Szabo,K., Homolya,L., Milgram,S.L. and Sarkadi,B.
  TITLE     C-terminal phosphorylation of MRP2 modulates its interaction with
            PDZ proteins
  JOURNAL   Biochem Biophys Res Commun 302 (3), 454-461 (2003)
   PUBMED   12615054
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Scott,R.O., Thelin,W.R. and Milgram,S.L.
  TITLE     A novel PDZ protein regulates the activity of guanylyl cyclase C,
            the heat-stable enterotoxin receptor
  JOURNAL   J Biol Chem 277 (25), 22934-22941 (2002)
   PUBMED   11950846
  REMARK    GeneRIF: A novel PDZ protein regulates the activity of guanylyl
            cyclase C, the heat-stable enterotoxin receptor.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA381610.1, BC029042.1, AP002956.1 and AB094096.1.
            
            On Dec 10, 2009 this sequence version replaced NP_079067.2.
            
            Summary: Guanylyl cyclase C (GCC, or GUCY2C; MIM 601330) produces
            cGMP following the binding of either endogenous ligands or
            heat-stable enterotoxins secreted by E. coli and other enteric
            bacteria. Activation of GCC initiates a signaling cascade that
            leads to phosphorylation of the cystic fibrosis transmembrane
            conductance regulator (CFTR; MIM 602421), followed by a net efflux
            of ions and water into the intestinal lumen. IKEPP is a regulatory
            protein that associates with GCC and regulates the amount of cGMP
            produced following receptor stimulation (Scott et al., 2002 [PubMed
            11950846]).[supplied by OMIM, Mar 2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1.
            This results in a shorter protein (isoform 2), compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029042.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..491
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF4
                     isoform 2"
                     /note="PDZ domain containing 2; natrium-phosphate
                     cotransporter IIa C-terminal-associated protein 2;
                     sodium-hydrogen exchanger regulatory factor 4; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF4; intestinal and
                     kidney enriched PDZ protein; NHERF-4; naPi-Cap2; PDZ
                     domain-containing protein 2; PDZ domain-containing protein
                     3; PDZ domain containing 3; na/Pi cotransporter
                     C-terminal-associated protein 2; Na(+)/H(+) exchange
                     regulatory cofactor 4"
                     /calculated_mol_wt=52417
     Region          48..127
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(59..65,76,79,108,112,115..116)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          156..219
                     /region_name="PDZ_canonical"
                     /note="canonical PDZ domain; cl49608"
                     /db_xref="CDD:483948"
     Region          248..330
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(258..264,278,281,310,314,317..318)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          395..464
                     /region_name="PDZ"
                     /note="Domain present in PSD-95, Dlg, and ZO-1/2;
                     smart00228"
                     /db_xref="CDD:214570"
     CDS             1..491
                     /gene="NHERF4"
                     /gene_synonym="IKEPP; PDZD3; PDZK2"
                     /coded_by="NM_024791.4:21..1496"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8417.1"
                     /db_xref="GeneID:79849"
                     /db_xref="HGNC:HGNC:19891"
                     /db_xref="MIM:607146"
ORIGIN      
        1 mekaadlqdt asltlkfkfn pklgidnpvl slaedhdpyd pwslerprfc llskeegksf
       61 gfhlqqelgr aghvvcrvdp gtsaqrqglq egdrilavnn dvvehedyav vvrrirassp
      121 rvlltvlarh ahdvaraqlg edahlcptlg pgvrprlchi vkdeggfgfs vthgnqgpfw
      181 lvlstggaae ragvppgarl levnglwqsg qqvtllvagp eveeqcrqlg lplaaplaeg
      241 walptkprcl hlekgpqgfg fllreekgld grpgqflwev dpglpakkag mqagdrlvav
      301 agesveglgh eetvsriqgq gscvsltvvd peadrffsmv rlspllflen teapasprgs
      361 ssaslveted psledtsvps vplgsrqcfl ypgpggsygf rlscvasgpr lfisqvtpgg
      421 saaraglqvg dvilevngyp vggqndlerl qqlpeaeppl clklaarslr gleawippga
      481 aedwalasdl l
//
LOCUS       NP_573571                440 aa            linear   PRI 20-NOV-2025
DEFINITION  WAS/WASL-interacting protein family member 2 [Homo sapiens].
ACCESSION   NP_573571
VERSION     NP_573571.1
DBSOURCE    REFSEQ: accession NM_133264.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Kennedy,S.A., Jarboui,M.A., Srihari,S., Raso,C., Bryan,K.,
            Dernayka,L., Charitou,T., Bernal-Llinares,M., Herrera-Montavez,C.,
            Krstic,A., Matallanas,D., Kotlyar,M., Jurisica,I., Curak,J.,
            Wong,V., Stagljar,I., LeBihan,T., Imrie,L., Pillai,P., Lynn,M.A.,
            Fasterius,E., Al-Khalili Szigyarto,C., Breen,J., Kiel,C.,
            Serrano,L., Rauch,N., Rukhlenko,O., Kholodenko,B.N.,
            Iglesias-Martinez,L.F., Ryan,C.J., Pilkington,R., Cammareri,P.,
            Sansom,O., Shave,S., Auer,M., Horn,N., Klose,F., Ueffing,M.,
            Boldt,K., Lynn,D.J. and Kolch,W.
  TITLE     Extensive rewiring of the EGFR network in colorectal cancer cells
            expressing transforming levels of KRASG13D
  JOURNAL   Nat Commun 11 (1), 499 (2020)
   PUBMED   31980649
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Girard,A., Sachidanandam,R., Hannon,G.J. and Carmell,M.A.
  TITLE     A germline-specific class of small RNAs binds mammalian Piwi
            proteins
  JOURNAL   Nature 442 (7099), 199-202 (2006)
   PUBMED   16751776
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Salazar,M.A., Kwiatkowski,A.V., Pellegrini,L., Cestra,G.,
            Butler,M.H., Rossman,K.L., Serna,D.M., Sondek,J., Gertler,F.B. and
            De Camilli,P.
  TITLE     Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl
            homology domains, links dynamin to regulation of the actin
            cytoskeleton
  JOURNAL   J Biol Chem 278 (49), 49031-49043 (2003)
   PUBMED   14506234
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Aspenstrom,P.
  TITLE     The WASP-binding protein WIRE has a role in the regulation of the
            actin filament system downstream of the platelet-derived growth
            factor receptor
  JOURNAL   Exp Cell Res 279 (1), 21-33 (2002)
   PUBMED   12213210
  REMARK    GeneRIF: The WASP-binding protein WIRE has a role in the regulation
            of the actin filament system downstream of the platelet-derived
            growth factor receptor
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Kato,M., Miki,H., Kurita,S., Endo,T., Nakagawa,H., Miyamoto,S. and
            Takenawa,T.
  TITLE     WICH, a novel verprolin homology domain-containing protein that
            functions cooperatively with N-WASP in actin-microspike formation
  JOURNAL   Biochem Biophys Res Commun 291 (1), 41-47 (2002)
   PUBMED   11829459
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068669.21, CN404607.1, BC065551.1, BC043408.1, AU138315.1,
            BC019706.1, CB240594.1 and AC080112.15.
            
            Summary: This gene encodes a WASP interacting protein (WIP)-related
            protein. It has been shown that this protein has a role in the
            WASP-mediated organization of the actin cytoskeleton and that this
            protein is a potential link between the activated platelet-derived
            growth factor receptor and the actin polymerization machinery.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.375701.1, BC065551.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000323571.9/ ENSP00000320924.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..440
                     /product="WAS/WASL-interacting protein family member 2"
                     /note="WASP-binding protein; WIP-related protein; WIP- and
                     CR16-homologous protein; WASP-interacting protein-related
                     protein"
                     /calculated_mol_wt=46158
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF74.1)"
     Region          33..62
                     /region_name="WH2_WAS_WASL-2_3"
                     /note="Wiskott Aldrich syndrome homology region 2 (WH2
                     motif) in WAS/WASL-interacting protein (WIP) family
                     members 2 and 3; cd22077"
                     /db_xref="CDD:409220"
     Site            order(36..37,39..41,43..45,50..53)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409220"
     Site            37
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q6PEV3; propagated from
                     UniProtKB/Swiss-Prot (Q8TF74.1)"
     Region          49..52
                     /region_name="Binds actin. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF74.1)"
     Region          50..53
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409220"
     Region          56..387
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF74.1)"
     Region          <96..308
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          419..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TF74.1)"
     CDS             1..440
                     /gene="WIPF2"
                     /gene_synonym="WICH; WIRE"
                     /coded_by="NM_133264.5:259..1581"
                     /db_xref="CCDS:CCDS11364.1"
                     /db_xref="GeneID:147179"
                     /db_xref="HGNC:HGNC:30923"
                     /db_xref="MIM:609692"
ORIGIN      
        1 mpippppppp pgppppptfh qanteqpkls rdeqrgrgal lqdickgtkl kkvtnindrs
       61 apilekpkgs sggygsggaa lqpkgglfqg gvlklrpvga kdgsenlagk palqipssra
      121 aaprppvsaa sgrpqddtds sraslpelpr mqrpslpdls rpnttsstgm khsssapppp
      181 ppgrranapp tplpmhsska paynrekplp ptpgqrlhpg regppapppv kpppspvnir
      241 tgpsgqslap ppppyrqppg vpngpssptn esapelpqrh nslhrktpgp vrglappppt
      301 saspsllsnr ppppardpps rgaapppppp virngardap pppppyrmhg seppsrgkpp
      361 pppsrtpagp ppppppplrn ghrdsittvr sflddfesky sfhpvedfpa peeykhfqri
      421 ypsktnraar gapplppilr
//
LOCUS       NP_001124180             538 aa            linear   PRI 20-NOV-2025
DEFINITION  uncharacterized protein C14orf93 isoform a precursor [Homo
            sapiens].
ACCESSION   NP_001124180
VERSION     NP_001124180.1
DBSOURCE    REFSEQ: accession NM_001130708.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Yu,Y., Liu,C., Zhang,J., Zhang,M., Wen,W., Ruan,X., Li,D.,
            Zhang,S., Gao,M. and Chen,L.
  TITLE     Rtfc (4931414P19Rik) Regulates in vitro Thyroid Differentiation and
            in vivo Thyroid Function
  JOURNAL   Sci Rep 7, 43396 (2017)
   PUBMED   28230092
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Liu,C., Yu,Y., Yin,G., Zhang,J., Wen,W., Ruan,X., Li,D., Zhang,S.,
            Cai,W., Gao,M. and Chen,L.
  TITLE     C14orf93 (RTFC) is identified as a novel susceptibility gene for
            familial nonmedullary thyroid cancer
  JOURNAL   Biochem Biophys Res Commun 482 (4), 590-596 (2017)
   PUBMED   27864143
  REMARK    GeneRIF: RTFC promotes thyroid cancer cell survival under starving
            conditions, and thyroid cancer cell migration. The R115Q, V205M and
            G209D RTFC mutants enhance the colony forming capacity of thyroid
            cancer cells, and are able to transform normal thyroid cells. In
            summary, our data suggest the roles of RTFC in thyroid
            carcinogenesis.
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Fatemifar,G., Hoggart,C.J., Paternoster,L., Kemp,J.P.,
            Prokopenko,I., Horikoshi,M., Wright,V.J., Tobias,J.H., Richmond,S.,
            Zhurov,A.I., Toma,A.M., Pouta,A., Taanila,A., Sipila,K.,
            Lahdesmaki,R., Pillas,D., Geller,F., Feenstra,B., Melbye,M.,
            Nohr,E.A., Ring,S.M., St Pourcain,B., Timpson,N.J., Davey Smith,G.,
            Jarvelin,M.R. and Evans,D.M.
  TITLE     Genome-wide association study of primary tooth eruption identifies
            pleiotropic loci associated with height and craniofacial distances
  JOURNAL   Hum Mol Genet 22 (18), 3807-3817 (2013)
   PUBMED   23704328
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA891690.1, AK023026.1, BC014299.2 and AL132780.5.
            
            Transcript Variant: This variant (4) differs in in the 5' UTR,
            compared to variant 1. Variants 1, 2, and 4 encode the same isoform
            (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023026.1, SRR3476690.415443.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..538
                     /product="uncharacterized protein C14orf93 isoform a
                     precursor"
                     /note="uncharacterized protein C14orf93; regulator of
                     thyroid function and cancer"
                     /calculated_mol_wt=56986
     sig_peptide     1..17
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H972.1)"
                     /calculated_mol_wt=1729
     Region          2..538
                     /region_name="DUF4616"
                     /note="Domain of unknown function (DUF4616); pfam15394"
                     /db_xref="CDD:464701"
     mat_peptide     18..538
                     /product="Uncharacterized protein C14orf93.
                     /id=PRO_0000020950"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H972.1)"
                     /calculated_mol_wt=56986
     Region          101..131
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H972.1)"
     Site            224
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H972.1)"
     Region          233..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H972.1)"
     Site            285
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H972.1)"
     Site            428
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2W9; propagated from
                     UniProtKB/Swiss-Prot (Q9H972.1)"
     Region          488..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H972.1)"
     CDS             1..538
                     /gene="C14orf93"
                     /gene_synonym="RTFC"
                     /coded_by="NM_001130708.3:177..1793"
                     /note="isoform a precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS9583.1"
                     /db_xref="GeneID:60686"
                     /db_xref="HGNC:HGNC:20162"
ORIGIN      
        1 msfsatilfs ppsgsearcc ccacksetng gntgsqggnp ppstpitvtg hglavqsseq
       61 llhviyqrvd kavglaeaal glarannell krlqeevgdl rqgkvsipde dgesrahssp
      121 peepgplkes pgeafkalsa veeecdsvgs gvqvvieelr qlgaasvgpg plgfpatqrd
      181 mrlpgctlaa seaapllnpl vddyvasega vqrvlvpaya kqlspatqla iqratpetgp
      241 engtklpppr pedmlnaaaa ldsaleesgp gstgelrhsl gltvspcrtr gsgqknsrrk
      301 rdlvlsklvh nvhnhitndk rfngsesiks swnisvvkfl leklkqelvt sphnytdkel
      361 kgacvayflt krreyrnsln pfkglkekee kklrsrryrl fanrssimrh fgpedqrlwn
      421 dvteelmsde edslnepgvw varpprfraq rltelcyhld anskhgtkan rvygppsdrl
      481 psaeaqllpp elynpnfqee edeggdenap gspsfdqphk tccpdlnsfi eikvekde
//
LOCUS       NP_001307470             422 aa            linear   PRI 20-NOV-2025
DEFINITION  phagosome assembly factor 1 isoform a [Homo sapiens].
ACCESSION   NP_001307470 XP_005256234
VERSION     NP_001307470.1
DBSOURCE    REFSEQ: accession NM_001320541.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 422)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 422)
  AUTHORS   Franco-Romero,A., Morbidoni,V., Milan,G., Sartori,R., Wulff,J.,
            Romanello,V., Armani,A., Salviati,L., Conte,M., Salvioli,S.,
            Franceschi,C., Buonomo,V., Swoboda,C.O., Grumati,P., Pannone,L.,
            Martinelli,S., Jefferies,H.B., Dikic,I., van der Laan,J.,
            Cabreiro,F., Millay,D.P., Tooze,S.A., Trevisson,E. and Sandri,M.
  TITLE     C16ORF70/MYTHO promotes healthy aging in C.elegans and prevents
            cellular senescence in mammals
  JOURNAL   J Clin Invest 134 (15), e165814 (2024)
   PUBMED   38869949
  REMARK    GeneRIF: C16ORF70/MYTHO promotes healthy aging in C.elegans and
            prevents cellular senescence in mammals.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 422)
  AUTHORS   Kojima,W., Yamano,K., Kosako,H., Imai,K., Kikuchi,R., Tanaka,K. and
            Matsuda,N.
  TITLE     Mammalian BCAS3 and C16orf70 associate with the phagophore assembly
            site in response to selective and non-selective autophagy
  JOURNAL   Autophagy 17 (8), 2011-2036 (2021)
   PUBMED   33499712
REFERENCE   4  (residues 1 to 422)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 422)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 422)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 422)
  AUTHORS   Hosgood,H.D. 3rd, Zhang,L., Shen,M., Berndt,S.I., Vermeulen,R.,
            Li,G., Yin,S., Yeager,M., Yuenger,J., Rothman,N., Chanock,S.,
            Smith,M. and Lan,Q.
  TITLE     Association between genetic variants in VEGF, ERCC3 and
            occupational benzene haematotoxicity
  JOURNAL   Occup Environ Med 66 (12), 848-853 (2009)
   PUBMED   19773279
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 422)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 422)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   10 (residues 1 to 422)
  AUTHORS   Setou,M., Nakagawa,T., Seog,D.H. and Hirokawa,N.
  TITLE     Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA
            receptor-containing vesicle transport
  JOURNAL   Science 288 (5472), 1796-1802 (2000)
   PUBMED   10846156
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY157930.1, CB997191.1, BC004556.2 and AA127668.1.
            
            On Feb 27, 2016 this sequence version replaced XP_005256234.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1, 2, 3, and 4 all encode the same isoform
            (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.241314.1,
                                           SRR7346977.1276475.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..422
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..422
                     /product="phagosome assembly factor 1 isoform a"
                     /note="UPF0183 protein C16orf70; macro-autophagy and youth
                     optimizer; phagosome assembly factor 1"
                     /calculated_mol_wt=47394
     Region          15..407
                     /region_name="PHAF1"
                     /note="Phagosome assembly factor 1; pfam03676"
                     /db_xref="CDD:461013"
     CDS             1..422
                     /gene="PHAF1"
                     /gene_synonym="C16orf6; C16orf70; lin-10; LIN10; MYTHO"
                     /coded_by="NM_001320541.2:122..1390"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS10828.1"
                     /db_xref="GeneID:80262"
                     /db_xref="HGNC:HGNC:29564"
ORIGIN      
        1 mldlevvper slgneqweft lgmplaqava ilqkhcriik nvqvlyseqs plshdlilnl
       61 tqdgiklmfd afnqrlkvie vcdltkvklk ycgvhfnsqa iaptieqidq sfgathpgvy
      121 nsaeqlfhln frglsfsfql dswteapkye pnfahglasl qiphgatvkr myiysgnslq
      181 dtkapmmpls cflgnvyaes vdvlrdgtgp aglrlrllaa gcgpgllada kmrvfersvy
      241 fgdscqdvls mlgsphkvfy ksedkmkihs psphkqvpsk cndyffnyft lgvdilfdan
      301 thkvkkfvlh tnypghynfn iyhrcefkip laikkenadg qtetcttysk wdniqellgh
      361 pvekpvvlhr ssspnntnpf gstfcfglqr mifevmqnnh iasvtlygpp rpgshlrtae
      421 lp
//
LOCUS       NP_006854                489 aa            linear   PRI 20-NOV-2025
DEFINITION  leukocyte immunoglobulin-like receptor subfamily A member 1 isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_006854
VERSION     NP_006854.1
DBSOURCE    REFSEQ: accession NM_006863.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Wang,K.S., Liu,X., Aragam,N., Mullersman,J.E., Jian,X., Pan,Y. and
            Liu,Y.
  TITLE     Polymorphisms in ABLIM1 are associated with personality traits and
            alcohol dependence
  JOURNAL   J Mol Neurosci 46 (2), 265-271 (2012)
   PUBMED   21547531
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Ryu,M., Chen,Y., Qi,J., Liu,J., Fan,Z., Nam,G., Shi,Y., Cheng,H.
            and Gao,G.F.
  TITLE     LILRA3 binds both classical and non-classical HLA class I molecules
            but with reduced affinities compared to LILRB1/LILRB2: structural
            evidence
  JOURNAL   PLoS One 6 (4), e19245 (2011)
   PUBMED   21559424
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Tedla,N., An,H., Borges,L., Vollmer-Conna,U., Bryant,K., Geczy,C.
            and McNeil,H.P.
  TITLE     Expression of activating and inhibitory leukocyte
            immunoglobulin-like receptors in rheumatoid synovium: correlations
            to disease activity
  JOURNAL   Tissue Antigens 77 (4), 305-316 (2011)
   PUBMED   21388353
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Jones,D.C., Kosmoliaptsis,V., Apps,R., Lapaque,N., Smith,I.,
            Kono,A., Chang,C., Boyle,L.H., Taylor,C.J., Trowsdale,J. and
            Allen,R.L.
  TITLE     HLA class I allelic sequence and conformation regulate leukocyte
            Ig-like receptor binding
  JOURNAL   J Immunol 186 (5), 2990-2997 (2011)
   PUBMED   21270408
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Brown,D., Trowsdale,J. and Allen,R.
  TITLE     The LILR family: modulators of innate and adaptive immune pathways
            in health and disease
  JOURNAL   Tissue Antigens 64 (3), 215-225 (2004)
   PUBMED   15304001
  REMARK    Review article
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Allen,R.L., Raine,T., Haude,A., Trowsdale,J. and Wilson,M.J.
  TITLE     Leukocyte receptor complex-encoded immunomodulatory receptors show
            differing specificity for alternative HLA-B27 structures
  JOURNAL   J Immunol 167 (10), 5543-5547 (2001)
   PUBMED   11698424
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Liu,W.R., Kim,J., Nwankwo,C., Ashworth,L.K. and Arm,J.P.
  TITLE     Genomic organization of the human leukocyte immunoglobulin-like
            receptors within the leukocyte receptor complex on chromosome
            19q13.4
  JOURNAL   Immunogenetics 51 (8-9), 659-669 (2000)
   PUBMED   10941837
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Wilson,M.J., Torkar,M., Haude,A., Milne,S., Jones,T., Sheer,D.,
            Beck,S. and Trowsdale,J.
  TITLE     Plasticity in the organization and sequences of human KIR/ILT gene
            families
  JOURNAL   Proc Natl Acad Sci U S A 97 (9), 4778-4783 (2000)
   PUBMED   10781084
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Borges,L., Hsu,M.L., Fanger,N., Kubin,M. and Cosman,D.
  TITLE     A family of human lymphoid and myeloid Ig-like receptors, some of
            which bind to MHC class I molecules
  JOURNAL   J Immunol 159 (11), 5192-5196 (1997)
   PUBMED   9548455
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA999265.1, AF025530.1,
            BC101514.1 and AC245036.3.
            
            Summary: This gene encodes an activating member of the leukocyte
            immunoglobulin-like receptor (LIR) family, which is found in a gene
            cluster at chromosomal region 19q13.4. The encoded protein is
            predominantly expressed in B cells, interacts with major
            histocompatibility complex class I ligands, and contributes to the
            regulation of immune responses. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (1, also known as LIR6a)
            represents the longest transcript and encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290919.1, AF025530.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: downstream AUG is associated
                                                with N-terminal localization
                                                signal (PMID:9548455)
            MANE Ensembl match               :: ENST00000251372.8/
                                                ENSP00000251372.3
            RefSeq Select criteria           :: based on expression, longest
                                                protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.42"
     Protein         1..489
                     /product="leukocyte immunoglobulin-like receptor subfamily
                     A member 1 isoform 1 precursor"
                     /note="leukocyte immunoglobulin-like receptor 6; CD85
                     antigen-like family member I; leukocyte
                     immunoglobulin-like receptor, subfamily A (with TM
                     domain), member 1; leucocyte Ig-like receptor A1;
                     leukocyte immunoglobulin-like receptor subfamily A member
                     1"
                     /calculated_mol_wt=51564
     sig_peptide     1..16
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
                     /calculated_mol_wt=1729
     mat_peptide     17..489
                     /product="Leukocyte immunoglobulin-like receptor subfamily
                     A member 1. /id=PRO_0000014816"
                     /note="propagated from UniProtKB/Swiss-Prot (O75019.1)"
                     /calculated_mol_wt=51564
     Region          28..118
                     /region_name="IgC2_D1_LILR_KIR_like"
                     /note="First immunoglobulin (Ig)-like domain found in
                     Leukocyte Ig-like receptors (LILRs), Natural killer
                     inhibitory receptors (KIRs) and similar domains; member of
                     Immunoglobulin Constant-2 set of IgSF domains; cd05751"
                     /db_xref="CDD:409409"
     Region          29..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409409"
     Region          37..40
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409409"
     Region          43..50
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409409"
     Region          57..62
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409409"
     Site            order(61,99,107)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:409409"
     Region          70..73
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409409"
     Region          82..86
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409409"
     Region          94..100
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409409"
     Region          111..118
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409409"
     Region          124..219
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            140
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          141..145
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          153..157
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          180..184
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          194..199
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          212..215
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          225..318
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          242..246
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          254..258
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          280..284
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            281
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          294..299
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Site            302
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          311..314
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          325..419
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Site            341
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Region          342..346
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          354..358
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          380..384
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          394..399
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          412..415
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          425..453
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75019.1)"
     Site            431
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Site            448
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O75019.1)"
     Site            462..482
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75019.1)"
     CDS             1..489
                     /gene="LILRA1"
                     /gene_synonym="CD85I; LIR-6; LIR6"
                     /coded_by="NM_006863.4:199..1668"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS12901.1"
                     /db_xref="GeneID:11024"
                     /db_xref="HGNC:HGNC:6602"
                     /db_xref="MIM:604810"
ORIGIN      
        1 mtpivtvlic lrlslgprth vqagtlpkpt lwaepgsvit qgspvtlwcq giletqeyrl
       61 yrekktapwi tripqeivkk gqfpipsitw ehtgryrcfy gshtagwsep sdplelvvtg
      121 ayikptlsal pspvvtsggn vtlhcvsqva fgsfilckeg edehpqclns qprthgwsra
      181 ifsvgpvsps rrwsyrcyay dsnsphvwsl psdllellvl gvskkpslsv qpgpivapge
      241 sltlqcvsdv sydrfvlyke gerdflqlpg pqpqaglsqa nftlgpvsrs yggqyrcsga
      301 ynlssewsap sdpldiliag qfrgrpfisv hpgptvasge nvtllcqswg pfhtflltka
      361 gaadaplrlr siheypkyqa efpmspvtsa hsgtyrcygs lssnpyllsh psdslelmvs
      421 gaaetlsppq nksdskagaa ntlspsqnkt ashpqdytve nlirmgiagl vlvvlgillf
      481 eaqhsqrsl
//
LOCUS       NP_001350927             591 aa            linear   PRI 20-NOV-2025
DEFINITION  calnexin isoform e precursor [Homo sapiens].
ACCESSION   NP_001350927
VERSION     NP_001350927.1
DBSOURCE    REFSEQ: accession NM_001363998.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 591)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 591)
  AUTHORS   Ye,Y., Zhang,J., Guo,Y., Zhu,J., Tang,B. and Fan,P.
  TITLE     PON2 ameliorates Ang II-induced cardiomyocyte injury by targeting
            the CANX/NOX4 signaling pathway
  JOURNAL   Immun Inflamm Dis 11 (2), e765 (2023)
   PUBMED   36840500
  REMARK    GeneRIF: PON2 ameliorates Ang II-induced cardiomyocyte injury by
            targeting the CANX/NOX4 signaling pathway.
REFERENCE   3  (residues 1 to 591)
  AUTHORS   Yan,G., Li,X., Zheng,Z., Gao,W., Chen,C., Wang,X., Cheng,Z., Yu,J.,
            Zou,G., Farooq,M.Z., Zhu,X., Zhu,W., Zhong,Q. and Yan,X.
  TITLE     KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity
  JOURNAL   Autophagy 18 (12), 2799-2816 (2022)
   PUBMED   35266843
  REMARK    GeneRIF: KAT7-mediated CANX (calnexin) crotonylation regulates
            leucine-stimulated MTORC1 activity.
REFERENCE   4  (residues 1 to 591)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 591)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 591)
  AUTHORS   Lenter,M. and Vestweber,D.
  TITLE     The integrin chains beta 1 and alpha 6 associate with the chaperone
            calnexin prior to integrin assembly
  JOURNAL   J Biol Chem 269 (16), 12263-12268 (1994)
   PUBMED   8163531
REFERENCE   7  (residues 1 to 591)
  AUTHORS   Tjoelker,L.W., Seyfried,C.E., Eddy,R.L. Jr., Byers,M.G.,
            Shows,T.B., Calderon,J., Schreiber,R.B. and Gray,P.W.
  TITLE     Human, mouse, and rat calnexin cDNA cloning: identification of
            potential calcium binding motifs and gene localization to human
            chromosome 5
  JOURNAL   Biochemistry 33 (11), 3229-3236 (1994)
   PUBMED   8136357
REFERENCE   8  (residues 1 to 591)
  AUTHORS   Honore,B., Rasmussen,H.H., Celis,A., Leffers,H., Madsen,P. and
            Celis,J.E.
  TITLE     The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin
            exhibit strikingly different levels in quiescent keratinocytes as
            compared to their proliferating normal and transformed
            counterparts: cDNA cloning and expression of calnexin
  JOURNAL   Electrophoresis 15 (3-4), 482-490 (1994)
   PUBMED   8055875
REFERENCE   9  (residues 1 to 591)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   10 (residues 1 to 591)
  AUTHORS   Galvin,K., Krishna,S., Ponchel,F., Frohlich,M., Cummings,D.E.,
            Carlson,R., Wands,J.R., Isselbacher,K.J., Pillai,S. and Ozturk,M.
  TITLE     The major histocompatibility complex class I antigen-binding
            protein p88 is the product of the calnexin gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (18), 8452-8456 (1992)
   PUBMED   1326756
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC113426.2.
            
            Summary: This gene encodes a member of the calnexin family of
            molecular chaperones. The encoded protein is a calcium-binding,
            endoplasmic reticulum (ER)-associated protein that interacts
            transiently with newly synthesized N-linked glycoproteins,
            facilitating protein folding and assembly. It may also play a
            central role in the quality control of protein folding by retaining
            incorrectly folded protein subunits within the ER for degradation.
            Alternatively spliced transcript variants encoding different
            isoforms have been described. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.210532.1,
                                           SRR1803613.16649.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..591
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..591
                     /product="calnexin isoform e precursor"
                     /note="major histocompatibility complex class I
                     antigen-binding protein p88; epididymis secretory sperm
                     binding protein"
                     /calculated_mol_wt=65267
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2191
     Region          71..440
                     /region_name="Calreticulin"
                     /note="Calreticulin family; pfam00262"
                     /db_xref="CDD:459737"
     Site            137
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P27824.2)"
     Region          260..345
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          276..409
                     /region_name="P domain (Extended arm).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          278..345
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          326..359
                     /region_name="Interaction with PPIB.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Region          348..405
                     /region_name="4 X approximate repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            482..502
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            553
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK3.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     Site            582
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P27824.2)"
     CDS             1..591
                     /gene="CANX"
                     /gene_synonym="CNX; IP90; P90"
                     /coded_by="NM_001363998.1:178..1953"
                     /note="isoform e precursor is encoded by transcript
                     variant 8"
                     /db_xref="CCDS:CCDS93838.1"
                     /db_xref="GeneID:821"
                     /db_xref="HGNC:HGNC:1473"
                     /db_xref="MIM:114217"
ORIGIN      
        1 megkwllcml lvlgtaivea hdghdddvid ieddlddvie evedskpdtt appsspkvty
       61 kapvptgevy fadsfdrgtl sgwilskakk ddtddeiaky dgkweveemk esklpgdkgl
      121 vlmsrakhha isaklnkpfl fdtkplivqy evnfqngiec ggayvkllsk tpelnldqfh
      181 dktpytimfg pdkcgedykl hfifrhknpk tgiyeekhak rpdadlktyf tdkkthlytl
      241 ilnpdnsfei lvdqsvvnsg nllndmtppv npsreiedpe drkpedwder pkipdpeavk
      301 pddwdedapa kipdeeatkp egwlddepey vpdpdaekpe dwdedmdgew eapqianprc
      361 esapgcgvwq rpvidnpnyk gkwkppmidn psyqgiwkpr kipnpdffed lepfrmtpfs
      421 aiglelwsmt sdiffdnfii cadrrivddw andgwglkka adgaaepgvv gqmieaaeer
      481 pwlwvvyilt valpvflvil fccsgkkqts gmeykktdap qpdvkeeeee keeekdkgde
      541 eeegeeklek qksdaeedgg tvsqeeedrk pkaeedeiln rsprnrkprr e
//
LOCUS       NP_001258863             216 aa            linear   PRI 20-NOV-2025
DEFINITION  thymidine kinase 2 isoform 5 [Homo sapiens].
ACCESSION   NP_001258863
VERSION     NP_001258863.1
DBSOURCE    REFSEQ: accession NM_001271934.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Aoki,H., Higashi,M., Okita,M., Ando,N., Murayama,S., Ishikawa,K.
            and Yokota,T.
  TITLE     Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n
  JOURNAL   Cerebellum 22 (1), 70-84 (2023)
   PUBMED   35084690
  REMARK    GeneRIF: Thymidine Kinase 2 and Mitochondrial Protein COX I in the
            Cerebellum of Patients with Spinocerebellar Ataxia Type 31 Caused
            by Penta-nucleotide Repeats (TTCCA)n.
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Dominguez-Gonzalez,C., Hernandez-Voth,A., de Fuenmayor-Fernandez de
            la Hoz,C.P., Guerrero,L.B., Moris,G., Garcia-Garcia,J., Muelas,N.,
            Leon Hernandez,J.C., Rabasa,M., Lora,D., Blazquez,A., Arenas,J. and
            Martin,M.A.
  TITLE     Metrics of progression and prognosis in untreated adults with
            thymidine kinase 2 deficiency: An observational study
  JOURNAL   Neuromuscul Disord 32 (9), 728-735 (2022)
   PUBMED   35907766
  REMARK    GeneRIF: Metrics of progression and prognosis in untreated adults
            with thymidine kinase 2 deficiency: An observational study.
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Wang,L. and Eriksson,S.
  TITLE     Mutational analyses of human thymidine kinase 2 reveal key residues
            in ATP-Mg2+ binding and catalysis
  JOURNAL   Nucleosides Nucleotides Nucleic Acids 41 (3), 264-272 (2022)
   PUBMED   34758700
  REMARK    GeneRIF: Mutational analyses of human thymidine kinase 2 reveal key
            residues in ATP-Mg(2+) binding and catalysis.
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Kierdaszuk,B., Krawiec,K., Kazimierczuk,Z., Jacobsson,U.,
            Johansson,N.G., Munch-Petersen,B., Eriksson,S. and Shugar,D.
  TITLE     Substrate/inhibitor specificities of human deoxycytidine kinase
            (dCK) and thymidine kinases (TK1 and TK2)
  JOURNAL   Adv Exp Med Biol 431, 623-627 (1998)
   PUBMED   9598140
REFERENCE   7  (residues 1 to 216)
  AUTHORS   Johansson,M. and Karlsson,A.
  TITLE     Cloning of the cDNA and chromosome localization of the gene for
            human thymidine kinase 2
  JOURNAL   J Biol Chem 272 (13), 8454-8458 (1997)
   PUBMED   9079672
REFERENCE   8  (residues 1 to 216)
  AUTHORS   Wang,J., El-Hattab,A.W. and Wong,L.J.C.
  TITLE     TK2-Related Mitochondrial DNA Maintenance Defect, Myopathic Form
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23230576
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Jansson,O., Bohman,C., Munch-Petersen,B. and Eriksson,S.
  TITLE     Mammalian thymidine kinase 2. Direct photoaffinity labeling with
            [32P]dTTP of the enzyme from spleen, liver, heart and brain
  JOURNAL   Eur J Biochem 206 (2), 485-490 (1992)
   PUBMED   1597187
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Willecke,K., Teber,T., Kucherlapati,R.S. and Ruddle,F.H.
  TITLE     Human mitochondrial thymidine kinase is coded for by a gene on
            chromosome 16 of the nucleus
  JOURNAL   Somatic Cell Genet 3 (3), 237-245 (1977)
   PUBMED   605384
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF521891.1, AK303590.1,
            BC142970.1, AC010542.7 and AL038860.1.
            
            Summary: This gene encodes a deoxyribonucleoside kinase that
            specifically phosphorylates thymidine, deoxycytidine, and
            deoxyuridine. The encoded enzyme localizes to the mitochondria and
            is required for mitochondrial DNA synthesis. Mutations in this gene
            are associated with a myopathic form of mitochondrial DNA depletion
            syndrome. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms, some of which lack transit
            peptide, so are not localized to mitochondria. [provided by RefSeq,
            Dec 2012].
            
            Transcript Variant: This variant (5) has an additional exon in the
            5' region, which results in an alternate translation start codon,
            compared to variant 1. The encoded isoform (5) is not localized to
            mitochondria, and it has a distinct N-terminus and is shorter than
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC142970.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..216
                     /product="thymidine kinase 2 isoform 5"
                     /EC_number="2.7.1.74"
                     /EC_number="2.7.1.21"
                     /note="mt-TK; thymidine kinase 2, mitochondrial;
                     deoxycytidine kinase TK2; 2'-deoxyuridine kinase TK2;
                     mitochondrial thymidine kinase"
                     /calculated_mol_wt=25355
     Region          4..211
                     /region_name="dNK"
                     /note="Deoxynucleoside kinase; pfam01712"
                     /db_xref="CDD:396326"
     Site            order(12,14..15,50,60..61,94,147,152)
                     /site_type="other"
                     /note="Substrate-binding site [chemical binding]"
                     /db_xref="CDD:238836"
     Site            68
                     /site_type="other"
                     /note="Substrate specificity [chemical binding]"
                     /db_xref="CDD:238836"
     CDS             1..216
                     /gene="TK2"
                     /gene_synonym="MTDPS2; MTTK; PEOB3; SCA31; TK2-EXT"
                     /coded_by="NM_001271934.2:304..954"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="GeneID:7084"
                     /db_xref="HGNC:HGNC:11831"
                     /db_xref="MIM:188250"
ORIGIN      
        1 mtsicvegni asgkttclef fsnatdvevl tepvskwrnv rghnplglmy hdasrwgltl
       61 qtyvqltmld rhtrpqvssv rlmersihsa ryifvenlyr sgkmpevdyv vlsewfdwil
      121 rnmdvsvdli vylrtnpetc yqrlkkrcre eekvipleyl eaihhlheew likgslfpma
      181 apvlvieadh hmermlelfe qnrdriltpe nrkhcp
//
LOCUS       NP_002568                524 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase PAK 2 [Homo sapiens].
ACCESSION   NP_002568 XP_941604
VERSION     NP_002568.2
DBSOURCE    REFSEQ: accession NM_002577.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Kervarrec,T., Westphal,D., Pissaloux,D., Legrand,M., Tirode,F.,
            Neuhart,A., Drouot,F., Becker,J.C., Macagno,N., Seris,A.,
            Jouary,T., Beltzung,F., Jullie,M.L., Harms,P.W., Cribier,B.,
            Mourah,S., Jouenne,F., Fromont,G., Louveau,B., Mancini,M.,
            Kazakov,D.V., de la Fouchardiere,A. and Battistella,M.
  TITLE     Porocarcinomas with PAK1/2/3 fusions: a series of 12 cases
  JOURNAL   Histopathology 85 (4), 566-578 (2024)
   PUBMED   38785043
  REMARK    GeneRIF: Porocarcinomas with PAK1/2/3 fusions: a series of 12
            cases.
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Wu,D., Zuo,Z., Sun,X., Li,X., Yin,F. and Yin,W.
  TITLE     ACSL4 promotes malignant progression of Hepatocellular carcinoma by
            targeting PAK2 transcription
  JOURNAL   Biochem Pharmacol 224, 116206 (2024)
   PUBMED   38615921
  REMARK    GeneRIF: ACSL4 promotes malignant progression of Hepatocellular
            carcinoma by targeting PAK2 transcription.
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Sannigrahi,M.K., Cao,A.C., Rajagopalan,P., Sun,L., Brody,R.M.,
            Raghav,L., Gimotty,P.A. and Basu,D.
  TITLE     A novel pipeline for prioritizing cancer type-specific therapeutic
            vulnerabilities using DepMap identifies PAK2 as a target in head
            and neck squamous cell carcinomas
  JOURNAL   Mol Oncol 18 (2), 336-349 (2024)
   PUBMED   37997254
  REMARK    GeneRIF: A novel pipeline for prioritizing cancer type-specific
            therapeutic vulnerabilities using DepMap identifies PAK2 as a
            target in head and neck squamous cell carcinomas.
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Yang,H., Li,Z., Zhu,S., Wang,W., Zhang,J., Zhao,D., Zhang,M.,
            Zhu,W., Xu,W. and Xu,C.
  TITLE     Molecular mechanisms of pancreatic cancer liver metastasis: the
            role of PAK2
  JOURNAL   Front Immunol 15, 1347683 (2024)
   PUBMED   38343537
  REMARK    GeneRIF: Molecular mechanisms of pancreatic cancer liver
            metastasis: the role of PAK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 524)
  AUTHORS   Benner,G.E., Dennis,P.B. and Masaracchia,R.A.
  TITLE     Activation of an S6/H4 kinase (PAK 65) from human placenta by
            intramolecular and intermolecular autophosphorylation
  JOURNAL   J Biol Chem 270 (36), 21121-21128 (1995)
   PUBMED   7673144
REFERENCE   7  (residues 1 to 524)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (17), 4385 (1995)
   PUBMED   7556080
  REMARK    Correction to:[EMBO J. 1995 May 1;14(9):1970-8. doi:
            10.1002/j.1460-2075.1995.tb07189.x. PMID: 7744004]
REFERENCE   8  (residues 1 to 524)
  AUTHORS   Knaus,U.G., Morris,S., Dong,H.J., Chernoff,J. and Bokoch,G.M.
  TITLE     Regulation of human leukocyte p21-activated kinases through G
            protein--coupled receptors
  JOURNAL   Science 269 (5221), 221-223 (1995)
   PUBMED   7618083
REFERENCE   9  (residues 1 to 524)
  AUTHORS   Martin,G.A., Bollag,G., McCormick,F. and Abo,A.
  TITLE     A novel serine kinase activated by rac1/CDC42Hs-dependent
            autophosphorylation is related to PAK65 and STE20
  JOURNAL   EMBO J 14 (9), 1970-1978 (1995)
   PUBMED   7744004
  REMARK    Erratum:[EMBO J. 1995 Sep 1;14(17):4385. doi:
            10.1002/j.1460-2075.1995.tb00113.x. PMID: 7556080]
REFERENCE   10 (residues 1 to 524)
  AUTHORS   Brandon,S.D. and Masaracchia,R.A.
  TITLE     Multisite phosphorylation of a synthetic peptide derived from the
            carboxyl terminus of the ribosomal protein S6
  JOURNAL   J Biol Chem 266 (1), 380-385 (1991)
   PUBMED   1985906
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB164364.1, AK291339.1,
            BC069613.1 and AC127904.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_941604.1, NP_002568.1.
            
            Summary: The p21 activated kinases (PAK) are critical effectors
            that link Rho GTPases to cytoskeleton reorganization and nuclear
            signaling. The PAK proteins are a family of serine/threonine
            kinases that serve as targets for the small GTP binding proteins,
            CDC42 and RAC1, and have been implicated in a wide range of
            biological activities. The protein encoded by this gene is
            activated by proteolytic cleavage during caspase-mediated
            apoptosis, and may play a role in regulating the apoptotic events
            in the dying cell. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.141172.1,
                                           SRR1660803.20636.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327134.7/ ENSP00000314067.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..524
                     /product="serine/threonine-protein kinase PAK 2"
                     /EC_number="2.7.11.1"
                     /note="p21 (CDKN1A)-activated kinase 2; S6/H4 kinase; p58;
                     PAK-2; gamma-PAK; p21-activated kinase 2; p21 protein
                     (Cdc42/Rac)-activated kinase 2"
                     /calculated_mol_wt=57912
     Region          1..81
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            55
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            58
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            60
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            62
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q8CIN4; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Region          69..137
                     /region_name="Autoregulatory region.
                     /evidence=ECO:0000250|UniProtKB:Q13153"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Region          69..112
                     /region_name="GTPase-binding.
                     /evidence=ECO:0000250|UniProtKB:Q13153"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Region          73..130
                     /region_name="PBD"
                     /note="P21-Rho-binding domain; pfam00786"
                     /db_xref="CDD:395634"
     Site            order(74,77,80,82,85,102,106)
                     /site_type="other"
                     /note="GTPase interaction site [polypeptide binding]"
                     /db_xref="CDD:238526"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            141
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:33693784,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Region          143..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Site            143
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8CIN4; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Region          169..188
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Site            197
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Site            212..213
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 or caspase-3-like proteases.
                     /evidence=ECO:0000269|PubMed:9171063,
                     ECO:0000269|PubMed:9786869; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     Region          229..524
                     /region_name="STKc_PAK2"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     p21-activated kinase 2; cd06655"
                     /db_xref="CDD:132986"
     Region          245..251
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000269|PubMed:12853446"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13177.3)"
     Site            order(255..259,263,276,278,307,323..327,329..330,333,368,
                     370..373,375,385..386,389,402..406,408,435,444..446)
                     /site_type="active"
                     /db_xref="CDD:132986"
     Site            order(255..259,263,276,278,307,323..327,329..330,333,
                     372..373,375,385..386)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:132986"
     Site            order(258..259,368,370..372,389,402..406,408,435,444..446)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:132986"
     Site            order(260,294,363,365..368,386..387,414..415,417,422,447,
                     450,453)
                     /site_type="other"
                     /note="AID interaction site [polypeptide binding]"
                     /db_xref="CDD:132986"
     Site            385..408
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:132986"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305|PubMed:9786869; propagated from
                     UniProtKB/Swiss-Prot (Q13177.3)"
     CDS             1..524
                     /gene="PAK2"
                     /gene_synonym="KNO2; PAK65; PAKgamma"
                     /coded_by="NM_002577.4:323..1897"
                     /db_xref="CCDS:CCDS3321.1"
                     /db_xref="GeneID:5062"
                     /db_xref="HGNC:HGNC:8591"
                     /db_xref="MIM:605022"
ORIGIN      
        1 msdngeledk ppappvrmss tifstggkdp lsanhslkpl psvpeekkpr hkiisifsgt
       61 ekgskkkeke rpeisppsdf ehtihvgfda vtgeftgmpe qwarllqtsn itkleqkknp
      121 qavldvlkfy dsntvkqkyl sftppekdgf psgtpalnak gteapavvte eedddeetap
      181 pviaprpdht ksiytrsvid pvpapvgdsh vdgaaksldk qkkktkmtde eimeklrtiv
      241 sigdpkkkyt ryekigqgas gtvftatdva lgqevaikqi nlqkqpkkel iineilvmke
      301 lknpnivnfl dsylvgdelf vvmeylaggs ltdvvtetcm deaqiaavcr eclqaleflh
      361 anqvihrdik sdnvllgmeg svkltdfgfc aqitpeqskr stmvgtpywm apevvtrkay
      421 gpkvdiwslg imaiemvege ppylnenplr alyliatngt pelqnpekls pifrdflnrc
      481 lemdvekrgs akellqhpfl klakplsslt plimaakeam ksnr
//
LOCUS       NP_001309786             406 aa            linear   PRI 20-NOV-2025
DEFINITION  NIPA-like protein 3 isoform a [Homo sapiens].
ACCESSION   NP_001309786
VERSION     NP_001309786.1
DBSOURCE    REFSEQ: accession NM_001322857.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Grzmil,P., Konietzko,J., Boehm,D., Holter,S.M.,
            Aguilar-Pimentel,A., Javaheri,A., Kalaydjiev,S., Adler,T.,
            Bolle,I., Adham,I., Dixkens,C., Wolf,S., Fuchs,H.,
            Gailus-Durner,V., Wurst,W., Ollert,M., Busch,D.H., Schulz,H., de
            Angelis,M.H. and Burfeind,P.
  TITLE     Targeted disruption of the mouse Npal3 gene leads to deficits in
            behavior, increased IgE levels, and impaired lung function
  JOURNAL   Cytogenet Genome Res 125 (3), 186-200 (2009)
   PUBMED   19738379
  REMARK    GeneRIF: Study demonstrates that both human NPAL3 and mouse NPAL3
            are ubiquitously expressed and encode highly conserved proteins
            Erratum:[Cytogenet Genome Res. 2009;125(4):285. Hoelter, S M
            [corrected to Holter, S M]; Aguilar, A [corrected to
            Aguilar-Pimentel, A]; Gailus-Durne, V [corrected to Gailus-Durner,
            V]; Busch, D [corrected to Busch, D H]]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL031431.8.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.99107.1,
                                           SRR1660805.89182.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..406
                     /product="NIPA-like protein 3 isoform a"
                     /note="NIPA-like protein 3"
                     /calculated_mol_wt=44611
     Region          32..326
                     /region_name="EamA"
                     /note="EamA-like transporter family; cl23754"
                     /db_xref="CDD:474045"
     Site            33..53
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            76..96
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            101..121
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            166
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            171..191
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            202..222
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            240..260
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            271..291
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            300..320
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P499.1)"
     Site            372
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q6P499.1)"
     CDS             1..406
                     /gene="NIPAL3"
                     /gene_synonym="DJ462O23.2; NPAL3; SLC57A5"
                     /coded_by="NM_001322857.1:466..1686"
                     /note="isoform a is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS30631.1"
                     /db_xref="GeneID:57185"
                     /db_xref="HGNC:HGNC:25233"
                     /db_xref="MIM:620034"
ORIGIN      
        1 mdgshsaalk lqqlpptsss savseasfsy kenligalla ifghlvvsia lnlqkychir
       61 lagskdpray fktktwwlgl flmllgelgv fasyafapls livplsavsv iasaiigiif
      121 ikekwkpkdf lrryvlsfvg cglavvgtyl lvtfapnshe kmtgenvtrh lvswpfllym
      181 lveiilfcll lyfykeknan nivvilllva llgsmtvvtv kavagmlvls iqgnlqldyp
      241 ifyvmfvcmv atavyqaafl sqasqmydss liasvgyils ttiaitagai fyldfigedv
      301 lhicmfalgc liaflgvfli trnrkkpipf epyismdamp gmqnmhdkgm tvqpelkasf
      361 sygalenndn iseiyapatl pvmqeehgsr sasgvpyrvl ehtkke
//
LOCUS       NP_001340051             495 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 63 kDa isoform c [Homo sapiens].
ACCESSION   NP_001340051
VERSION     NP_001340051.1
DBSOURCE    REFSEQ: accession NM_001353122.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 495)
  AUTHORS   Kodani,A., Knopp,K.A., Di Lullo,E., Retallack,H., Kriegstein,A.R.,
            DeRisi,J.L. and Reiter,J.F.
  TITLE     Zika virus alters centrosome organization to suppress the innate
            immune response
  JOURNAL   EMBO Rep 23 (9), e52211 (2022)
   PUBMED   35793002
REFERENCE   2  (residues 1 to 495)
  AUTHORS   Ling,H., Cao,C.H., Han,K., Lv,Y.R., Ma,X.D., Cao,J.H., Chen,J.W.,
            Li,S., Lin,J.L., Fang,Y.J., Pan,Z.Z., Xie,D. and Wang,F.W.
  TITLE     CEP63 upregulates YAP1 to promote colorectal cancer progression
            through stabilizing RNA binding protein FXR1
  JOURNAL   Oncogene 41 (39), 4433-4445 (2022)
   PUBMED   35989368
  REMARK    GeneRIF: CEP63 upregulates YAP1 to promote colorectal cancer
            progression through stabilizing RNA binding protein FXR1.
REFERENCE   3  (residues 1 to 495)
  AUTHORS   O'Neill,A.C., Uzbas,F., Antognolli,G., Merino,F., Draganova,K.,
            Jack,A., Zhang,S., Pedini,G., Schessner,J.P., Cramer,K.,
            Schepers,A., Metzger,F., Esgleas,M., Smialowski,P., Guerrini,R.,
            Falk,S., Feederle,R., Freytag,S., Wang,Z., Bahlo,M., Jungmann,R.,
            Bagni,C., Borner,G.H.H., Robertson,S.P., Hauck,S.M. and Gotz,M.
  TITLE     Spatial centrosome proteome of human neural cells uncovers
            disease-relevant heterogeneity
  JOURNAL   Science 376 (6599), eabf9088 (2022)
   PUBMED   35709258
REFERENCE   4  (residues 1 to 495)
  AUTHORS   Liu,C., Yu,F., Ma,R., Zhang,L., Du,G., Niu,D. and Yin,D.
  TITLE     Cep63 knockout inhibits the malignant phenotypes of papillary
            thyroid cancer cell line TPC-1
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296302
  REMARK    GeneRIF: Cep63 knockout inhibits the malignant phenotypes of
            papillary thyroid cancer cell line TPC1.
REFERENCE   5  (residues 1 to 495)
  AUTHORS   Mahjabeen,I., Maqsood,Y., Abbasi,R., Ahmed,M.W. and Kayani,M.A.
  TITLE     Polymorphism in miRNA target sites of CEP-63 and CEP-152 ring
            complex influences expression of CEP genes and favors tumorigenesis
            in glioma
  JOURNAL   Future Oncol 17 (25), 3355-3372 (2021)
   PUBMED   34156311
  REMARK    GeneRIF: Polymorphism in miRNA target sites of CEP-63 and CEP-152
            ring complex influences expression of CEP genes and favors
            tumorigenesis in glioma.
REFERENCE   6  (residues 1 to 495)
  AUTHORS   Morris,J.A., Kandpal,G., Ma,L. and Austin,C.P.
  TITLE     DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated
            protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL:
            regulation and loss of interaction with mutation
  JOURNAL   Hum Mol Genet 12 (13), 1591-1608 (2003)
   PUBMED   12812986
REFERENCE   7  (residues 1 to 495)
  AUTHORS   Takahashi,M., Yamagiwa,A., Nishimura,T., Mukai,H. and Ono,Y.
  TITLE     Centrosomal proteins CG-NAP and kendrin provide microtubule
            nucleation sites by anchoring gamma-tubulin ring complex
  JOURNAL   Mol Biol Cell 13 (9), 3235-3245 (2002)
   PUBMED   12221128
REFERENCE   8  (residues 1 to 495)
  AUTHORS   Mayor,T., Stierhof,Y.D., Tanaka,K., Fry,A.M. and Nigg,E.A.
  TITLE     The centrosomal protein C-Nap1 is required for cell cycle-regulated
            centrosome cohesion
  JOURNAL   J Cell Biol 151 (4), 837-846 (2000)
   PUBMED   11076968
REFERENCE   9  (residues 1 to 495)
  AUTHORS   Golsteyn,R.M., Mundt,K.E., Fry,A.M. and Nigg,E.A.
  TITLE     Cell cycle regulation of the activity and subcellular localization
            of Plk1, a human protein kinase implicated in mitotic spindle
            function
  JOURNAL   J Cell Biol 129 (6), 1617-1628 (1995)
   PUBMED   7790358
REFERENCE   10 (residues 1 to 495)
  AUTHORS   Verloes,A., Drunat,S., Gressens,P. and Passemard,S.
  TITLE     Primary Autosomal Recessive Microcephalies and Seckel Syndrome
            Spectrum Disorders - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301772
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC010207.18, AC026117.15,
            AC139764.5, AC109912.10 and BC014050.2.
            
            Summary: This gene encodes a protein with six coiled-coil domains.
            The protein is localized to the centrosome, a non-membraneous
            organelle that functions as the major microtubule-organizing center
            in animal cells. Several alternatively spliced transcript variants
            have been found, but their biological validity has not been
            determined. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803614.148122.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA2148093, SAMEA2151119 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..495
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.2"
     Protein         1..495
                     /product="centrosomal protein of 63 kDa isoform c"
                     /note="centrosome protein CEP63; centrosomal protein
                     63kDa"
                     /calculated_mol_wt=57777
     Region          18..280
                     /region_name="CEP63"
                     /note="Centrosomal protein of 63 kDa; pfam17045"
                     /db_xref="CDD:465338"
     Region          <163..>441
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..495
                     /gene="CEP63"
                     /gene_synonym="SCKL6"
                     /coded_by="NM_001353122.1:427..1914"
                     /note="isoform c is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS43154.1"
                     /db_xref="GeneID:80254"
                     /db_xref="HGNC:HGNC:25815"
                     /db_xref="MIM:614724"
ORIGIN      
        1 meallegiqn rghgggflts ceaelqelmk qidimvahkk sewegrthal etclkireqe
       61 lkslrsqldv thkevgmlhq qveehekikq emtmeykqel kklheelcil krsyeklqkk
      121 qmrefrgntk nhredrseie rltakieefr qksldwekqr liyqqqvssl eaqrkalaeq
      181 seiiqaqlvn rkqklesvel ssqseiqhls sklerandti caneleierl tmrvndlvgt
      241 smtvlqeqqq keeklresek llealqeekr elkaalqsqe nliheariqk eklqekvkat
      301 ntqhaveais lesvsatckq lsqelmekye elkrmeahnn eykaeikklk eqilqgeqsy
      361 ssalegmkme ishltqelhq rditiastkg sssdmekrlr aemqkaedka vehkeildql
      421 eslklenrhl semvmklelg lhecslpvsp lgsiatrfle eeelrshhil erldahieel
      481 kresektvrq ftalk
//
LOCUS       NP_061861                390 aa            linear   PRI 20-NOV-2025
DEFINITION  glucose-fructose oxidoreductase domain-containing protein 1 isoform
            1 precursor [Homo sapiens].
ACCESSION   NP_061861
VERSION     NP_061861.1
DBSOURCE    REFSEQ: accession NM_018988.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 390)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 390)
  AUTHORS   Shi,J., Guo,X., Liu,C., Wang,Y., Chen,X., Wu,G., Ding,J. and
            Zhang,T.
  TITLE     Molecular insight into the potential functional role of
            pseudoenzyme GFOD1 via interaction with NKIRAS2
  JOURNAL   Acta Biochim Biophys Sin (Shanghai) 56 (9), 1256-1266 (2024)
   PUBMED   38946427
REFERENCE   3  (residues 1 to 390)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 390)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 390)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 390)
  AUTHORS   Liu,Z., Ma,C., Gu,J. and Yu,M.
  TITLE     Potential biomarkers of acute myocardial infarction based on
            weighted gene co-expression network analysis
  JOURNAL   Biomed Eng Online 18 (1), 9 (2019)
   PUBMED   30683112
  REMARK    GeneRIF: three overlapping genes (FGFBP2, GFOD1 and MLC1) between
            two modules could potentially have a role in acute myocardial
            infarction and have diagnostic potential
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 390)
  AUTHORS   Wu,X.R., Chen,Y.H., Chen,W., Kong,W., Huang,J.W., Zhang,J., Xue,W.,
            Liu,D.M. and Huang,Y.R.
  TITLE     GFOD1 and peejar are promising markers for clear-cell renal cell
            carcinoma disease progression
  JOURNAL   Oncotarget 7 (25), 38004-38009 (2016)
   PUBMED   27191742
  REMARK    GeneRIF: Authors found the expression of peejar was positively
            correlated with the expression of GFOD1 in ccRCC tissue, with
            Pearson correlation coefficiency reaching 0.939 (p < 0.001). GFOD1
            and peejar were novel genes correlated with ccRCC disease
            progression and patients' poor prognosis.
REFERENCE   8  (residues 1 to 390)
  AUTHORS   Lasky-Su,J., Neale,B.M., Franke,B., Anney,R.J., Zhou,K.,
            Maller,J.B., Vasquez,A.A., Chen,W., Asherson,P., Buitelaar,J.,
            Banaschewski,T., Ebstein,R., Gill,M., Miranda,A., Mulas,F.,
            Oades,R.D., Roeyers,H., Rothenberger,A., Sergeant,J.,
            Sonuga-Barke,E., Steinhausen,H.C., Taylor,E., Daly,M., Laird,N.,
            Lange,C. and Faraone,S.V.
  TITLE     Genome-wide association scan of quantitative traits for attention
            deficit hyperactivity disorder identifies novel associations and
            confirms candidate gene associations
  JOURNAL   Am J Med Genet B Neuropsychiatr Genet 147B (8), 1345-1354 (2008)
   PUBMED   18821565
  REMARK    GeneRIF: Observational study and genome-wide association study of
            gene-disease association. (HuGE Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL583828.4 and AL589984.7.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.865191.1,
                                           SRR3476690.852885.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379287.4/ ENSP00000368589.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..390
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.1-p23"
     Protein         1..390
                     /product="glucose-fructose oxidoreductase
                     domain-containing protein 1 isoform 1 precursor"
                     /note="glucose-fructose oxidoreductase domain-containing
                     protein 1; glucose-fructose oxidoreductase domain
                     containing 1; gfo/Idh/MocA-like oxidoreductase
                     domain-containing protein 1"
                     /calculated_mol_wt=41022
     sig_peptide     1..21
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9NXC2.1)"
                     /calculated_mol_wt=2155
     Region          4..260
                     /region_name="MviM"
                     /note="Predicted dehydrogenase [General function
                     prediction only]; COG0673"
                     /db_xref="CDD:440437"
     mat_peptide     22..390
                     /product="Glucose-fructose oxidoreductase
                     domain-containing protein 1. /id=PRO_0000282968"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXC2.1)"
                     /calculated_mol_wt=41022
     CDS             1..390
                     /gene="GFOD1"
                     /gene_synonym="ADG-90; C6orf114"
                     /coded_by="NM_018988.4:711..1883"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS4524.1"
                     /db_xref="GeneID:54438"
                     /db_xref="HGNC:HGNC:21096"
                     /db_xref="MIM:619932"
ORIGIN      
        1 mlpgvgvfgt sltarviipl lkdegfavka lwgrtqeeae elakemsvpf ytsridevll
       61 hqdvdlvcin lpppltrqia vktlgigknv icdrtatpld afrmtsaahy ypklmsimgn
      121 vlrflpafvr mkqlieegyv geplvcevqv hggsllgkky nwscddlmgg gglhsvgtyi
      181 idlltfltgq kavkvhgllk tfvkqtdhik girqitsddf ctfqmvlegg vcctvtlnfn
      241 vpgefkqdvt vvgsagrlla vgtdlygqrn sapeqellvq datpvsnsll pekafsdips
      301 pylrgtikmm qavrqafqdq ddrrtwdgrp ltmaatfddc lyalcvvdti krssqtgewq
      361 niaimteepe lspaylisea mrrsrmslyc
//
LOCUS       NP_001015000             161 aa            linear   PRI 20-NOV-2025
DEFINITION  structure-specific endonuclease subunit SLX1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001015000
VERSION     NP_001015000.1
DBSOURCE    REFSEQ: accession NM_001015000.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Payliss,B.J., Patel,A., Sheppard,A.C. and Wyatt,H.D.M.
  TITLE     Exploring the Structures and Functions of Macromolecular
            SLX4-Nuclease Complexes in Genome Stability
  JOURNAL   Front Genet 12, 784167 (2021)
   PUBMED   34804132
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 161)
  AUTHORS   Garribba,L., Bjerregaard,V.A., Goncalves Dinis,M.M., Ozer,O.,
            Wu,W., Sakellariou,D., Pena-Diaz,J., Hickson,I.D. and Liu,Y.
  TITLE     Folate stress induces SLX1- and RAD51-dependent mitotic DNA
            synthesis at the fragile X locus in human cells
  JOURNAL   Proc Natl Acad Sci U S A 117 (28), 16527-16536 (2020)
   PUBMED   32601218
  REMARK    GeneRIF: Folate stress induces SLX1- and RAD51-dependent mitotic
            DNA synthesis at the fragile X locus in human cells.
REFERENCE   3  (residues 1 to 161)
  AUTHORS   Zhou,X., DeLucia,M. and Ahn,J.
  TITLE     SLX4-SLX1 Protein-independent Down-regulation of MUS81-EME1 Protein
            by HIV-1 Viral Protein R (Vpr)
  JOURNAL   J Biol Chem 291 (33), 16936-16947 (2016)
   PUBMED   27354282
  REMARK    GeneRIF: SLX4-SLX1 Protein-independent Down-regulation of
            MUS81-EME1 Protein by HIV-1 Viral Protein R (Vpr).
REFERENCE   4  (residues 1 to 161)
  AUTHORS   Wyatt,H.D., Sarbajna,S., Matos,J. and West,S.C.
  TITLE     Coordinated actions of SLX1-SLX4 and MUS81-EME1 for Holliday
            junction resolution in human cells
  JOURNAL   Mol Cell 52 (2), 234-247 (2013)
   PUBMED   24076221
  REMARK    GeneRIF: Data show that three structure-selective endonucleases,
            SLX1-SLX4, MUS81-EME1, and GEN1, define two pathways of Holliday
            junctions (HJs) resolution in HeLa cells.
REFERENCE   5  (residues 1 to 161)
  AUTHORS   Wan,B., Yin,J., Horvath,K., Sarkar,J., Chen,Y., Wu,J., Wan,K.,
            Lu,J., Gu,P., Yu,E.Y., Lue,N.F., Chang,S., Liu,Y. and Lei,M.
  TITLE     SLX4 assembles a telomere maintenance toolkit by bridging multiple
            endonucleases with telomeres
  JOURNAL   Cell Rep 4 (5), 861-869 (2013)
   PUBMED   24012755
REFERENCE   6  (residues 1 to 161)
  AUTHORS   Svendsen,J.M., Smogorzewska,A., Sowa,M.E., O'Connell,B.C.,
            Gygi,S.P., Elledge,S.J. and Harper,J.W.
  TITLE     Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and
            is required for DNA repair
  JOURNAL   Cell 138 (1), 63-77 (2009)
   PUBMED   19596235
REFERENCE   7  (residues 1 to 161)
  AUTHORS   Andersen,S.L., Bergstralh,D.T., Kohl,K.P., LaRocque,J.R.,
            Moore,C.B. and Sekelsky,J.
  TITLE     Drosophila MUS312 and the vertebrate ortholog BTBD12 interact with
            DNA structure-specific endonucleases in DNA repair and
            recombination
  JOURNAL   Mol Cell 35 (1), 128-135 (2009)
   PUBMED   19595722
REFERENCE   8  (residues 1 to 161)
  AUTHORS   Munoz,I.M., Hain,K., Declais,A.C., Gardiner,M., Toh,G.W.,
            Sanchez-Pulido,L., Heuckmann,J.M., Toth,R., Macartney,T.,
            Eppink,B., Kanaar,R., Ponting,C.P., Lilley,D.M. and Rouse,J.
  TITLE     Coordination of structure-specific nucleases by human SLX4/BTBD12
            is required for DNA repair
  JOURNAL   Mol Cell 35 (1), 116-127 (2009)
   PUBMED   19595721
REFERENCE   9  (residues 1 to 161)
  AUTHORS   Hildebrandt,M.A., Salavaggione,O.E., Martin,Y.N., Flynn,H.C.,
            Jalal,S., Wieben,E.D. and Weinshilboum,R.M.
  TITLE     Human SULT1A3 pharmacogenetics: gene duplication and functional
            genomic studies
  JOURNAL   Biochem Biophys Res Commun 321 (4), 870-878 (2004)
   PUBMED   15358107
REFERENCE   10 (residues 1 to 161)
  AUTHORS   Wistow,G., Bernstein,S.L., Ray,S., Wyatt,M.K., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human iris for the NEIBank
            Project: steroid-response factors and similarities with retinal
            pigment epithelium
  JOURNAL   Mol Vis 8, 185-195 (2002)
   PUBMED   12107412
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI757439.1, BC144462.1 and
            AI885276.1.
            
            Summary: This gene encodes a protein that is an important regulator
            of genome stability. The protein represents the catalytic subunit
            of the SLX1-SLX4 structure-specific endonuclease, which can resolve
            DNA secondary structures that are formed during repair and
            recombination processes. Two identical copies of this gene are
            located on the p arm of chromosome 16 due to a segmental
            duplication; this record represents the more centromeric copy.
            Alternative splicing results in multiple transcript variants.
            Read-through transcription also occurs between this gene and the
            downstream SULT1A3 (sulfotransferase family, cytosolic, 1A,
            phenol-preferring, member 3) gene. [provided by RefSeq, Nov 2010].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1, resulting
            in an isoform (2) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.328305.1, AI383477.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..161
                     /product="structure-specific endonuclease subunit SLX1
                     isoform 2"
                     /note="GIY-YIG domain-containing protein 1; SLX1
                     structure-specific endonuclease subunit homolog A; SLX1
                     homolog A, structure-specific endonuclease subunit"
                     /calculated_mol_wt=17881
     Region          13..82
                     /region_name="GIY-YIG_SLX1"
                     /note="Catalytic GIY-YIG domain of yeast
                     structure-specific endonuclease subunit SLX1 and its
                     eukaryotic homologs; cd10455"
                     /db_xref="CDD:198402"
     Site            order(15..17,31..33)
                     /site_type="other"
                     /note="GIY-YIG motif/motif A"
                     /db_xref="CDD:198402"
     Site            order(17,31,33,41,45,82)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:198402"
     Site            82
                     /site_type="other"
                     /note="putative metal binding site [ion binding]"
                     /db_xref="CDD:198402"
     CDS             1..161
                     /gene="SLX1A"
                     /gene_synonym="GIYD1"
                     /coded_by="NM_001015000.2:243..728"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS32432.1"
                     /db_xref="GeneID:548593"
                     /db_xref="HGNC:HGNC:20922"
                     /db_xref="MIM:615822"
ORIGIN      
        1 mgpagvaarp grffgvylly clnpryrgrv yvgftvntar rvqqhnggrk kggawrtsgr
       61 gpwemvlvvh gfpssvaalr deegplccph pgcllrahvi claeeflqee pgqllplegq
      121 cpcceksllw gdliwlcqmd tekevedsel eeahwtdlle t
//
LOCUS       NP_001352603            1141 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001352603
VERSION     NP_001352603.1
DBSOURCE    REFSEQ: accession NM_001365674.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1141)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1141)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1141)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1141)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1141)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1141)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1141)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.182639.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1141
                     /product="cordon-bleu protein-like 1 isoform 7"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=125074
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          60..126
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          144..222
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          262..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          304..309
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          338..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          373..378
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          467..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          793..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          <802..1039
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          895..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1008..1094
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1090..1115
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1094..1095,1097..1099,1101..1103,1111..1114)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1111..1114
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     Region          1116..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     CDS             1..1141
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001365674.2:165..3590"
                     /note="isoform 7 is encoded by transcript variant 9"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mdgrtprpqd aparrkpkak aplppaetky tdvssaadsv estafimeqk enmidkdvel
       61 svvlpgdiik sttvhgskpm mdlliflcaq yhlnpssyti dllsaeqnhi kfkpntpigm
      121 levekvilkp kmldkkkptp iipektvrvv infkktqkti vrvsphaslq elapiicskc
      181 efdplhtlll kdyqsqepld ltkslndlgl relyamdvnr atsvtvfsks slqescqisq
      241 nldimkeken kgffsffqrs kkkrdqtasa patplvnkhr ptftrsntis kpyisntlps
      301 dapkkrrapl ppmpasqsvp qdlahiqerp ascivksmsv detdkspcea grvragslql
      361 ssmsagnssl rrtkrkapsp pskipphqsd ensrvtalqp vdgvppdsas eanspeelss
      421 pagissdysl eeidekeels evpkveaeni spksqdipfv stdiintlkn dpdsalgngs
      481 gefsqnsmee kqetkstdgq ephsvvydts ngkkvvdsir nlkslgpnqe nvvqneiivy
      541 pentednmkn gvkkteinve gvaknnnidm everpsnsea hetdtaisyk enhlaassvp
      601 dqklnqpsae ktkdaaiqtt pscnsfdgkh qdhnlsdskv eecvqtsnnn istqhsclss
      661 qdsvntsref rsqgtliihs edpltvkdpi cahgnddllp pvdridknst asylknyply
      721 rqdynpkpkp sneitreyip kigmttykiv ppksleiskd wqsetieykd dqdmhalgkk
      781 hthenvketa iqtedsaise speeplpnlk pkpnlrtehq vpssvsspdd amvsplkpap
      841 kmtrdtgtap fapnleeinn ileskfksra snaqakpssf flqmqkrvsg hyvtsaaaks
      901 vhaapnpapk eltnkeaerd mlpspeqtls plskmphsvp qplvektddd vigqapaeas
      961 pppiapkpvt ipasqvstqn lktlktfgap rpysssgpsp falavvkrsq sfskertesp
     1021 sasalvqppa nteegkthsv nkfvdipqlg vsdkennsah neqnsqiptp tdgpsftvmr
     1081 qssltfqssd peqmrqsllt airsgeaaak lkrvtipsnt isvngrsrls hsmspdaqdg
     1141 h
//
LOCUS       NP_775858                523 aa            linear   PRI 20-NOV-2025
DEFINITION  REST corepressor 2 isoform 1 [Homo sapiens].
ACCESSION   NP_775858
VERSION     NP_775858.2
DBSOURCE    REFSEQ: accession NM_173587.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 523)
  AUTHORS   Rivera,C., Verbel-Vergara,D., Arancibia,D., Lappala,A.,
            Gonzalez,M., Guzman,F., Merello,G., Lee,J.T. and Andres,M.E.
  TITLE     Revealing RCOR2 as a regulatory component of nuclear speckles
  JOURNAL   Epigenetics Chromatin 14 (1), 51 (2021)
   PUBMED   34819154
  REMARK    GeneRIF: Revealing RCOR2 as a regulatory component of nuclear
            speckles.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 523)
  AUTHORS   Song,Y., Dagil,L., Fairall,L., Robertson,N., Wu,M., Ragan,T.J.,
            Savva,C.G., Saleh,A., Morone,N., Kunze,M.B.A., Jamieson,A.G.,
            Cole,P.A., Hansen,D.F. and Schwabe,J.W.R.
  TITLE     Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1
            Deacetylase in the CoREST Complex
  JOURNAL   Cell Rep 30 (8), 2699-2711 (2020)
   PUBMED   32101746
REFERENCE   3  (residues 1 to 523)
  AUTHORS   Hiramatsu,H., Kobayashi,K., Kobayashi,K., Haraguchi,T., Ino,Y.,
            Todo,T. and Iba,H.
  TITLE     The role of the SWI/SNF chromatin remodeling complex in maintaining
            the stemness of glioma initiating cells
  JOURNAL   Sci Rep 7 (1), 889 (2017)
   PUBMED   28420882
  REMARK    Erratum:[Sci Rep. 2018 Oct 25;8(1):16079. doi:
            10.1038/s41598-018-31444-z. PMID: 30356171]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 523)
  AUTHORS   Monaghan,C.E., Nechiporuk,T., Jeng,S., McWeeney,S.K., Wang,J.,
            Rosenfeld,M.G. and Mandel,G.
  TITLE     REST corepressors RCOR1 and RCOR2 and the repressor INSM1 regulate
            the proliferation-differentiation balance in the developing brain
  JOURNAL   Proc Natl Acad Sci U S A 114 (3), E406-E415 (2017)
   PUBMED   28049845
REFERENCE   5  (residues 1 to 523)
  AUTHORS   Suva,M.L., Rheinbay,E., Gillespie,S.M., Patel,A.P., Wakimoto,H.,
            Rabkin,S.D., Riggi,N., Chi,A.S., Cahill,D.P., Nahed,B.V.,
            Curry,W.T., Martuza,R.L., Rivera,M.N., Rossetti,N., Kasif,S.,
            Beik,S., Kadri,S., Tirosh,I., Wortman,I., Shalek,A.K.,
            Rozenblatt-Rosen,O., Regev,A., Louis,D.N. and Bernstein,B.E.
  TITLE     Reconstructing and reprogramming the tumor-propagating potential of
            glioblastoma stem-like cells
  JOURNAL   Cell 157 (3), 580-594 (2014)
   PUBMED   24726434
REFERENCE   6  (residues 1 to 523)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 523)
  AUTHORS   Yang,P., Wang,Y., Chen,J., Li,H., Kang,L., Zhang,Y., Chen,S.,
            Zhu,B. and Gao,S.
  TITLE     RCOR2 is a subunit of the LSD1 complex that regulates ESC property
            and substitutes for SOX2 in reprogramming somatic cells to
            pluripotency
  JOURNAL   Stem Cells 29 (5), 791-801 (2011)
   PUBMED   21433225
  REMARK    GeneRIF: Ectopic expression of Rcor2 in both mouse and human
            somatic cells effectively substituted the requirement for exogenous
            Sox2 expression in somatic cell reprogramming.
REFERENCE   8  (residues 1 to 523)
  AUTHORS   Vaquerizas,J.M., Kummerfeld,S.K., Teichmann,S.A. and Luscombe,N.M.
  TITLE     A census of human transcription factors: function, expression and
            evolution
  JOURNAL   Nat Rev Genet 10 (4), 252-263 (2009)
   PUBMED   19274049
  REMARK    Review article
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003780.3 and BC023587.2.
            
            On Nov 24, 2009 this sequence version replaced NP_775858.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC023587.2, AB593132.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301459.5/ ENSP00000301459.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..523
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..523
                     /product="REST corepressor 2 isoform 1"
                     /calculated_mol_wt=57881
     Region          1..43
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          46..98
                     /region_name="ELM2"
                     /note="ELM2 domain; pfam01448"
                     /db_xref="CDD:460214"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          134..178
                     /region_name="SANT"
                     /note="'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains.
                     Tandem copies of the domain bind telomeric DNA tandem
                     repeatsas part of the capping complex. Binding is sequence
                     dependent for repeats which contain the G/C rich motif
                     [C2-3 A (CA)1-6]. The domain is...; cl21498"
                     /db_xref="CDD:473887"
     Site            order(135,164..165,167..168,170..172,174..176)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:212559"
     Region          185..264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5FWT8; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          331..374
                     /region_name="Myb_DNA-binding"
                     /note="Myb-like DNA-binding domain; pfam00249"
                     /db_xref="CDD:459731"
     Region          387..523
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZ40.2)"
     Region          <466..520
                     /region_name="Gag_MA"
                     /note="Matrix protein (MA), p15; pfam01140"
                     /db_xref="CDD:426076"
     Site            479
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q8C796; propagated from
                     UniProtKB/Swiss-Prot (Q8IZ40.2)"
     CDS             1..523
                     /gene="RCOR2"
                     /coded_by="NM_173587.4:709..2280"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS8052.1"
                     /db_xref="GeneID:283248"
                     /db_xref="HGNC:HGNC:27455"
                     /db_xref="MIM:616019"
ORIGIN      
        1 mpsvmekpsa gsgilsrsra ktvpnggqph seddsseeeh shdsmirvgt nyqavipeck
       61 pesparysnk elkgmlvwsp nhcvsdakld kyiamakekh gynieqalgm llwhkhdvek
      121 sladlanftp fpdewtvedk vlfeqafgfh gkcfqriqqm lpdklipslv kyyyswkktr
      181 srtsvmdrqa rrlggrkdke dsdeleegrg gvsegepdpa dpkreplpsr plnarpgpgk
      241 kevqvsqyrh hplrtrrrpp kgmylspegl tavsgspdla nltlrgldsq lislkrqvqs
      301 mkqtnsslrq aleggidplr ppeantkfns rwttdeqlla vqairrygkd fgaiaevign
      361 ktltqvktff vsyrrrfnle evlqeweaeq dgapgapvpm eearrgaplp apaleeddev
      421 qitsvstsvp rsvppapppp ppptslsqpp pllrpplpta ptllrqpppl qqgrflqprl
      481 apnqppppli rpalaaprhs arpgpqpppt ligtpleppa psl
//
LOCUS       NP_001287731             765 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-4 isoform c [Homo sapiens].
ACCESSION   NP_001287731 XP_005274436
VERSION     NP_001287731.1
DBSOURCE    REFSEQ: accession NM_001300802.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 765)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 765)
  AUTHORS   Wu,S., Jin,J., Huang,J., Chen,G. and Chen,Y.
  TITLE     Comprehensive analysis of the RSK gene family in acute myeloid
            leukemia determines a prognostic signature for the prediction of
            clinical prognosis and treatment responses
  JOURNAL   Hematology 28 (1), 2235833 (2023)
   PUBMED   37462338
  REMARK    GeneRIF: Comprehensive analysis of the RSK gene family in acute
            myeloid leukemia determines a prognostic signature for the
            prediction of clinical prognosis and treatment responses.
REFERENCE   3  (residues 1 to 765)
  AUTHORS   Qiu,M., Lin,Q., Liu,Y., Chen,P., Zhou,Y., Jiang,Y., Zhou,Z.,
            Wen,Q., Zhou,X., Liang,X., Gan,H. and Yu,H.
  TITLE     Potentially functional genetic variants in RPS6KA4 and MAP2K5 in
            the MAPK signaling pathway predict HBV-related hepatocellular
            carcinoma survival
  JOURNAL   Mol Carcinog 62 (9), 1378-1387 (2023)
   PUBMED   37278562
  REMARK    GeneRIF: Potentially functional genetic variants in RPS6KA4 and
            MAP2K5 in the MAPK signaling pathway predict HBV-related
            hepatocellular carcinoma survival.
REFERENCE   4  (residues 1 to 765)
  AUTHORS   Sattarifard,H., Safaei,A., Khazeeva,E., Rastegar,M. and Davie,J.R.
  TITLE     Mitogen- and stress-activated protein kinase (MSK1/2) regulated
            gene expression in normal and disease states
  JOURNAL   Biochem Cell Biol 101 (3), 204-219 (2023)
   PUBMED   36812480
  REMARK    GeneRIF: Mitogen- and stress-activated protein kinase (MSK1/2)
            regulated gene expression in normal and disease states.
            Review article
REFERENCE   5  (residues 1 to 765)
  AUTHORS   Akbar,N., Forteath,C., Hussain,M.S., Reyskens,K., Belch,J.J.F.,
            Lang,C.C., Mordi,I.R., Bhalraam,U., Arthur,J.S.C. and Khan,F.
  TITLE     Mitogen and Stress-Activated Kinases 1 and 2 Mediate Endothelial
            Dysfunction
  JOURNAL   Int J Mol Sci 22 (16), 8655 (2021)
   PUBMED   34445361
  REMARK    GeneRIF: Mitogen and Stress-Activated Kinases 1 and 2 Mediate
            Endothelial Dysfunction.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 765)
  AUTHORS   Du,K. and Montminy,M.
  TITLE     CREB is a regulatory target for the protein kinase Akt/PKB
  JOURNAL   J Biol Chem 273 (49), 32377-32379 (1998)
   PUBMED   9829964
REFERENCE   7  (residues 1 to 765)
  AUTHORS   Zhu,S. and Gerhard,D.S.
  TITLE     A transcript map of an 800-kb region on human chromosome 11q13,
            part of the candidate region for SCA5 and BBS1
  JOURNAL   Hum Genet 103 (6), 674-680 (1998)
   PUBMED   9921902
REFERENCE   8  (residues 1 to 765)
  AUTHORS   Pierrat,B., Correia,J.S., Mary,J.L., Tomas-Zuber,M. and
            Lesslauer,W.
  TITLE     RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase
            under dominant control of p38alpha mitogen-activated protein kinase
            (p38alphaMAPK)
  JOURNAL   J Biol Chem 273 (45), 29661-29671 (1998)
   PUBMED   9792677
REFERENCE   9  (residues 1 to 765)
  AUTHORS   Deak,M., Clifton,A.D., Lucocq,L.M. and Alessi,D.R.
  TITLE     Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
            activated by MAPK and SAPK2/p38, and may mediate activation of CREB
  JOURNAL   EMBO J 17 (15), 4426-4441 (1998)
   PUBMED   9687510
REFERENCE   10 (residues 1 to 765)
  AUTHORS   Xing,J., Ginty,D.D. and Greenberg,M.E.
  TITLE     Coupling of the RAS-MAPK pathway to gene activation by RSK2, a
            growth factor-regulated CREB kinase
  JOURNAL   Science 273 (5277), 959-963 (1996)
   PUBMED   8688081
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223561.1, AK313567.1,
            AP003774.4 and AJ010119.1.
            
            On Jul 12, 2014 this sequence version replaced XP_005274436.1.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            non-identical kinase catalytic domains and phosphorylates various
            substrates, including CREB1 and ATF1. The encoded protein can also
            phosphorylate histone H3 to regulate certain inflammatory genes.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) uses an alternate in-frame
            splice site in the coding region, compared to variant 1, resulting
            in a shorter protein (isoform c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK223561.1, AK313567.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..765
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..765
                     /product="ribosomal protein S6 kinase alpha-4 isoform c"
                     /EC_number="2.7.11.1"
                     /note="ribosomal protein kinase B; mitogen- and
                     stress-activated protein kinase 2; ribosomal protein S6
                     kinase, 90kDa, polypeptide 4; ribosomal protein S6 kinase
                     alpha-4; 90 kDa ribosomal protein S6 kinase 4; nuclear
                     mitogen- and stress-activated protein kinase 2"
                     /calculated_mol_wt=84625
     Region          32..364
                     /region_name="STKc_MSK2_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, Mitogen and stress-activated kinase 2; cd05614"
                     /db_xref="CDD:270765"
     Site            order(39..43,47,63,65,99,115..116,118,122,124,161,163,
                     165..166,168,178..179,182,197..202,230,236,239)
                     /site_type="active"
                     /db_xref="CDD:270765"
     Site            order(39..43,47,63,65,99,116..118,122,161,163,165..166,
                     168,178..179)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270765"
     Site            order(43,122,124,161,163,165,182,197..202,230,236,239)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270765"
     Site            order(178..188,191..202)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270765"
     Site            196
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            344
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270765"
     Site            347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            356..361
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270765"
     Site            360
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            365
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Region          400..707
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(410..413,416,418,431,433,460,476..479,523,527..528,
                     530,543..544)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271082"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            561
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1, MAPK3 and MAPK14.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Region          666..689
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            680
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Region          718..765
                     /region_name="Required for nuclear targeting and
                     association with MAPK14"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Region          721..765
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75676.1)"
     Site            730
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     Site            738
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O75676.1)"
     CDS             1..765
                     /gene="RPS6KA4"
                     /gene_synonym="MSK2; RSK-B; S6K-alpha-4"
                     /coded_by="NM_001300802.2:75..2372"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS73313.1"
                     /db_xref="GeneID:8986"
                     /db_xref="HGNC:HGNC:10433"
                     /db_xref="MIM:603606"
ORIGIN      
        1 mgdedddesc avelritean ltgheekvsv enfellkvlg tgaygkvflv rkagghdagk
       61 lyamkvlrka alvqraktqe htrtersvle lvrqapflvt lhyafqtdak lhlildyvsg
      121 gemfthlyqr qyfkeaevrv yggeivlale hlhklgiiyr dlklenvlld seghivltdf
      181 glskefltee kertfsfcgt ieymapeiir sktghgkavd wwslgillfe lltgaspftl
      241 egerntqaev srrilkcspp fpprigpvaq dllqrllckd pkkrlgagpq gaqevrnhpf
      301 fqgldwvala arkipapfrp qirseldvgn faeeftrlep vysppgsppp gdprifqgys
      361 fvapsilfdh nnavmtdgle apgagdrpgr aavarsammq yeldlrepal gqgsfsvcrr
      421 crqrqsgqef avkilsrrle antqrevaal rlcqshpnvv nlhevhhdql htylvlellr
      481 ggellehirk krhfseseas qilrslvsav sfmheeagvv hrdlkpenil yaddtpgapv
      541 kiidfgfarl rpqspgvpmq tpcftlqyaa pellaqqgyd escdlwslgv ilymmlsgqv
      601 pfqgasgqgg qsqaaeimck iregrfsldg eawqgvseea kelvrglltv dpakrlkleg
      661 lrgsswlqdg sarsspplrt pdvlessgpa vrsglnatfm afnrgkregf flksvenapl
      721 akrrkqklrs atasrrgspa panpgrapva skgaprrang plpps
//
LOCUS       NP_001191039              82 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 15 [Homo sapiens].
ACCESSION   NP_001191039
VERSION     NP_001191039.1
DBSOURCE    REFSEQ: accession NM_001204110.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 82)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 82)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 82)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 82)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 82)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 82)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 82)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 82)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 82)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 82)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            DQ849200.1 and AI268146.1.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (15) uses an alternate in-frame
            splice site in the 5' coding region, contains an alternate internal
            exon, and differs in the 3' coding region and UTR, compared to
            variant 1. The resulting isoform (15) is shorter and has a distinct
            C-terminus, compared to isoform 1. This record was created to
            support clinical studies, but the encoded isoform currently lacks
            experimental evidence.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: DQ849200.1 [ECO:0000331]
            RNAseq introns       :: single sample supports all introns
                                    SAMEA1968968, SAMEA2145313 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            NMD candidate             :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..82
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..82
                     /product="bcl-2-like protein 11 isoform 15"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=9230
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     Region          46..76
                     /region_name="Bclx_interact"
                     /note="Bcl-x interacting, BH3 domain; pfam08945"
                     /db_xref="CDD:462643"
     CDS             1..82
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_001204110.2:289..537"
                     /note="isoform 15 is encoded by transcript variant 15"
                     /db_xref="CCDS:CCDS56133.1"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qasmrqaepa dmrpeiwiaq
       61 elrrigdefn ayyarrmplp pd
//
LOCUS       NP_001188472             716 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM161A isoform 1 [Homo sapiens].
ACCESSION   NP_001188472
VERSION     NP_001188472.1
DBSOURCE    REFSEQ: accession NM_001201543.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 716)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 716)
  AUTHORS   Arslanhan,M.D., Cengiz-Emek,S., Odabasi,E., Steib,E., Hamel,V.,
            Guichard,P. and Firat-Karalar,E.N.
  TITLE     CCDC15 localizes to the centriole inner scaffold and controls
            centriole length and integrity
  JOURNAL   J Cell Biol 222 (12) (2023)
   PUBMED   37934472
REFERENCE   3  (residues 1 to 716)
  AUTHORS   Liu,Y., Chen,J., Sager,R., Sasaki,E. and Hu,H.
  TITLE     Interactions between C8orf37 and FAM161A, Two Ciliary Proteins
            Essential for Photoreceptor Survival
  JOURNAL   Int J Mol Sci 23 (19), 12033 (2022)
   PUBMED   36233334
  REMARK    GeneRIF: Interactions between C8orf37 and FAM161A, Two Ciliary
            Proteins Essential for Photoreceptor Survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 716)
  AUTHORS   Mercey,O., Kostic,C., Bertiaux,E., Giroud,A., Sadian,Y.,
            Gaboriau,D.C.A., Morrison,C.G., Chang,N., Arsenijevic,Y.,
            Guichard,P. and Hamel,V.
  TITLE     The connecting cilium inner scaffold provides a structural
            foundation that protects against retinal degeneration
  JOURNAL   PLoS Biol 20 (6), e3001649 (2022)
   PUBMED   35709082
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 716)
  AUTHORS   Zach,F., Grassmann,F., Langmann,T., Sorusch,N., Wolfrum,U. and
            Stohr,H.
  TITLE     The retinitis pigmentosa 28 protein FAM161A is a novel ciliary
            protein involved in intermolecular protein interaction and
            microtubule association
  JOURNAL   Hum Mol Genet 21 (21), 4573-4586 (2012)
   PUBMED   22791751
  REMARK    GeneRIF: FAM161A is a microtubule-associated ciliary protein
            presumably involved in microtubule stabilization to maintain the
            microtubule tracks and/or in transport processes along microtubules
            in photoreceptors and other retinal cell types.
REFERENCE   6  (residues 1 to 716)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 716)
  AUTHORS   Bandah-Rozenfeld,D., Mizrahi-Meissonnier,L., Farhy,C.,
            Obolensky,A., Chowers,I., Pe'er,J., Merin,S., Ben-Yosef,T.,
            Ashery-Padan,R., Banin,E. and Sharon,D.
  TITLE     Homozygosity mapping reveals null mutations in FAM161A as a cause
            of autosomal-recessive retinitis pigmentosa
  JOURNAL   Am J Hum Genet 87 (3), 382-391 (2010)
   PUBMED   20705279
  REMARK    GeneRIF: These data suggest a pivotal role for FAM161A in
            photoreceptors and reveal that FAM161A loss-of-function mutations
            are a major cause of autosomal-recessive Retinitis pigmentosa.
REFERENCE   8  (residues 1 to 716)
  AUTHORS   Langmann,T., Di Gioia,S.A., Rau,I., Stohr,H., Maksimovic,N.S.,
            Corbo,J.C., Renner,A.B., Zrenner,E., Kumaramanickavel,G.,
            Karlstetter,M., Arsenijevic,Y., Weber,B.H., Gal,A. and Rivolta,C.
  TITLE     Nonsense mutations in FAM161A cause RP28-associated recessive
            retinitis pigmentosa
  JOURNAL   Am J Hum Genet 87 (3), 376-381 (2010)
   PUBMED   20705278
  REMARK    GeneRIF: Null mutations in FAM161A are responsible for the
            RP28-associated autosomal-recessive retinitis pigmentosa.
REFERENCE   9  (residues 1 to 716)
  AUTHORS   Gu,S., Kumaramanickavel,G., Srikumari,C.R., Denton,M.J. and Gal,A.
  TITLE     Autosomal recessive retinitis pigmentosa locus RP28 maps between
            D2S1337 and D2S286 on chromosome 2p11-p15 in an Indian family
  JOURNAL   J Med Genet 36 (9), 705-707 (1999)
   PUBMED   10507729
REFERENCE   10 (residues 1 to 716)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107081.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene belongs to the FAM161 family. It is expressed
            mainly in the retina. Mouse studies suggested that this gene is
            involved in development of retinal progenitors during
            embryogenesis, and that its activity is restricted to mature
            photoreceptors after birth. Mutations in this gene cause autosomal
            recessive retinitis pigmentosa-28. Alternatively spliced transcript
            variants have been identified.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.88349.1, BX648834.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000404929.6/ ENSP00000385158.1
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..716
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..716
                     /product="protein FAM161A isoform 1"
                     /note="retinitis pigmentosa 28 (autosomal recessive);
                     protein FAM161A; family with sequence similarity 161
                     member A; FAM161A, centrosomal protein"
                     /calculated_mol_wt=83361
     Region          234..595
                     /region_name="UPF0564"
                     /note="Uncharacterized protein family UPF0564; pfam10595"
                     /db_xref="CDD:431382"
     CDS             1..716
                     /gene="FAM161A"
                     /gene_synonym="RP28"
                     /coded_by="NM_001201543.2:20..2170"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS56120.1"
                     /db_xref="GeneID:84140"
                     /db_xref="HGNC:HGNC:25808"
                     /db_xref="MIM:613596"
ORIGIN      
        1 matshrvakl vasslqtpvn pitgarvaqy eredplkala aaeailedee eekvaqpaga
       61 sadlntsfsg vdehapisye dfvnfpdihh sneeyfkkve elkaahietm aklekmyqdk
      121 lhlkevqpvv iredslsdss rsvseknsyh pvslmtsfse pdlgqsssly vssseeelpn
      181 lekeyprknr mmtyakelin nmwtdfcved yirckdtgfh aaekrrkkrk ewvptitvpe
      241 pfqmmireqk kkeesmksks diemvhkalk kqeedpeykk kfranpvpas vflplyhdlv
      301 kqkeerrrsl kekskealla sqkpfkfiar eeqkraarek qlrdflkykk ktnrfkarpi
      361 prstygsttn dklkeeelyr nlrtqlraqe hlqnssplpc rsacgcrnpr cpeqavklkc
      421 khkvrcptpd fedlperyqk hlsehkspkl ltvckpfdlh asphasikre kiladieade
      481 enlketrwpy lsprrkspvr cagvnpvpcn cnppvptvss rgreqavrrs leekkmleee
      541 rnriltkqkq rmkelqkllt trakaydshq slaqisksrv kclrkseker mreyqrelee
      601 reeklkkrpl lfervaqkna rmaaekhysn tlkalgisde fvskkgqsgk vleyfnnqet
      661 ksvtedkesf neeekieere ngeenyfidt nsqdsykekd eaneeseeek sveesh
//
LOCUS       NP_001271226            1181 aa            linear   PRI 20-NOV-2025
DEFINITION  1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
            isoform 2 [Homo sapiens].
ACCESSION   NP_001271226 XP_005254503
VERSION     NP_001271226.1
DBSOURCE    REFSEQ: accession NM_001284297.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1181)
  AUTHORS   Phoenix,K.N., Yue,Z., Yue,L., Cronin,C.G., Liang,B.T.,
            Hoeppner,L.H. and Claffey,K.P.
  TITLE     PLCbeta2 Promotes VEGF-Induced Vascular Permeability
  JOURNAL   Arterioscler Thromb Vasc Biol 42 (10), 1229-1241 (2022)
   PUBMED   35861069
  REMARK    GeneRIF: PLCbeta2 Promotes VEGF-Induced Vascular Permeability.
REFERENCE   2  (residues 1 to 1181)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1181)
  AUTHORS   Zhang,H., Xie,T., Shui,Y. and Qi,Y.
  TITLE     Knockdown of PLCB2 expression reduces melanoma cell viability and
            promotes melanoma cell apoptosis by altering Ras/Raf/MAPK signals
  JOURNAL   Mol Med Rep 21 (1), 420-428 (2020)
   PUBMED   31746389
  REMARK    GeneRIF: Knockdown of PLCB2 expression reduces melanoma cell
            viability and promotes melanoma cell apoptosis by altering
            Ras/Raf/MAPK signals.
REFERENCE   4  (residues 1 to 1181)
  AUTHORS   Bertagnolo,V., Grassilli,S., Volinia,S., Al-Qassab,Y., Brugnoli,F.,
            Vezzali,F., Lambertini,E., Palomba,M., Piubello,Q., Orvieto,E.,
            Natali,C., Piva,R., Croce,C.M. and Capitani,S.
  TITLE     Ectopic expression of PLC-beta2 in non-invasive breast tumor cells
            plays a protective role against malignant progression and is
            correlated with the deregulation of miR-146a
  JOURNAL   Mol Carcinog 58 (5), 708-721 (2019)
   PUBMED   30582225
  REMARK    GeneRIF: High PLCB2 expression is associated with breast cancer.
REFERENCE   5  (residues 1 to 1181)
  AUTHORS   Brugnoli,F., Grassilli,S., Lanuti,P., Marchisio,M., Al-Qassab,Y.,
            Vezzali,F., Capitani,S. and Bertagnolo,V.
  TITLE     Up-modulation of PLC-beta2 reduces the number and malignancy of
            triple-negative breast tumor cells with a CD133+/EpCAM+ phenotype:
            a promising target for preventing progression of TNBC
  JOURNAL   BMC Cancer 17 (1), 617 (2017)
   PUBMED   28870198
  REMARK    GeneRIF: this work adds substantial information about the role of
            PLC-beta2 in invasive breast tumors, demonstrating that its
            up-regulation in cells with a basal-B triple-negative phenotype is
            sufficient to down-modulate the expression of surface antigens
            crucial for malignancy and to reduce the number of cells with a
            stem-like phenotype.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1181)
  AUTHORS   Zauli,G., Previati,M., Caramelli,E., Bassini,A., Falcieri,E.,
            Gibellini,D., Bertolaso,L., Bosco,D., Robuffo,I. and Capitani,S.
  TITLE     Exogenous human immunodeficiency virus type-1 Tat protein
            selectively stimulates a phosphatidylinositol-specific
            phospholipase C nuclear pathway in the Jurkat T cell line
  JOURNAL   Eur J Immunol 25 (9), 2695-2700 (1995)
   PUBMED   7589147
REFERENCE   7  (residues 1 to 1181)
  AUTHORS   Buhl,A.M., Osawa,S. and Johnson,G.L.
  TITLE     Mitogen-activated protein kinase activation requires two signal
            inputs from the human anaphylatoxin C5a receptor
  JOURNAL   J Biol Chem 270 (34), 19828-19832 (1995)
   PUBMED   7649993
REFERENCE   8  (residues 1 to 1181)
  AUTHORS   Park,D., Jhon,D.Y., Kriz,R., Knopf,J. and Rhee,S.G.
  TITLE     Cloning, sequencing, expression, and Gq-independent activation of
            phospholipase C-beta 2
  JOURNAL   J Biol Chem 267 (23), 16048-16055 (1992)
   PUBMED   1644792
REFERENCE   9  (residues 1 to 1181)
  AUTHORS   Berstein,G., Blank,J.L., Jhon,D.Y., Exton,J.H., Rhee,S.G. and
            Ross,E.M.
  TITLE     Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11,
            its physiologic regulator
  JOURNAL   Cell 70 (3), 411-418 (1992)
   PUBMED   1322796
REFERENCE   10 (residues 1 to 1181)
  AUTHORS   Banno,Y., Yada,Y. and Nozawa,Y.
  TITLE     Purification and characterization of membrane-bound phospholipase C
            specific for phosphoinositides from human platelets
  JOURNAL   J Biol Chem 263 (23), 11459-11465 (1988)
   PUBMED   2841328
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA981116.1, M95678.1 and
            AB209583.1.
            
            On Sep 27, 2013 this sequence version replaced XP_005254503.1.
            
            Summary: The protein encoded by this gene is a phosphodiesterase
            that catalyzes the hydrolysis of phosphatidylinositol
            4,5-bisphosphate to the second messengers inositol
            1,4,5-trisphosphate (IP3) and diacylglycerol. The encoded protein
            is activated by G proteins and has been shown to be involved in the
            type 2 taste receptor signal transduction pathway. In addition,
            nuclear factor kappa B can regulate the transcription of this gene,
            whose protein product is also an important regulator of platelet
            responses. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site, compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M95678.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..1181
                     /product="1-phosphatidylinositol 4,5-bisphosphate
                     phosphodiesterase beta-2 isoform 2"
                     /EC_number="3.1.4.11"
                     /note="phosphoinositide phospholipase C-beta-2;
                     1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
                     beta-2"
                     /calculated_mol_wt=133550
     Region          12..141
                     /region_name="PH_14"
                     /note="PH domain; pfam17787"
                     /db_xref="CDD:465506"
     Region          149..299
                     /region_name="EFh_PI-PLCbeta2"
                     /note="EF-hand motif found in phosphoinositide
                     phospholipase C beta 2 (PI-PLC-beta2); cd16209"
                     /db_xref="CDD:320039"
     Region          149..178
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          182..211
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          220..249
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          266..299
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:320039"
     Region          311..645
                     /region_name="PI-PLCc_beta2"
                     /note="Catalytic domain of metazoan
                     phosphoinositide-specific phospholipase C-beta2; cd08624"
                     /db_xref="CDD:176561"
     Site            order(327..328,357,359,374,408,461,463,571,598,600)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:176561"
     Site            order(327,374)
                     /site_type="active"
                     /note="catalytic site [active]"
                     /db_xref="CDD:176561"
     Site            order(328,357,359,408)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:176561"
     Region          677..798
                     /region_name="C2_PLC_like"
                     /note="C2 domain present in Phosphoinositide-specific
                     phospholipases C (PLC); cd00275"
                     /db_xref="CDD:175974"
     Site            order(696,721,753,757,759)
                     /site_type="other"
                     /note="Ca2+ binding pocket [ion binding]"
                     /db_xref="CDD:175974"
     Region          855..884
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Region          875..>1070
                     /region_name="YhaN"
                     /note="Uncharacterized conserved protein YhaN, contains
                     AAA domain [Function unknown]; COG4717"
                     /db_xref="CDD:443752"
     Region          939..975
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00722.2)"
     Site            949
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q00722.2)"
     Region          974..1149
                     /region_name="PLC-beta_C"
                     /note="PLC-beta C terminal; pfam08703"
                     /db_xref="CDD:462571"
     CDS             1..1181
                     /gene="PLCB2"
                     /gene_synonym="PLC-beta-2"
                     /coded_by="NM_001284297.2:264..3809"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS61592.1"
                     /db_xref="GeneID:5330"
                     /db_xref="HGNC:HGNC:9055"
                     /db_xref="MIM:604114"
ORIGIN      
        1 msllnpvllp pkvkaylsqg erfikwddet tvaspvilrv dpkgyylywt yqskemefld
       61 itsirdtrfg kfakmpksqk lrdvfnmdfp dnsfllktlt vvsgpdmvdl tfhnfvsyke
      121 nvgkawaedv lalvkhplta nasrstfldk ilvklkmqln segkipvknf fqmfpadrkr
      181 veaalsachl pkgkndainp edfpepvyks flmslcprpe ideiftsyha kakpymtkeh
      241 ltkfinqkqr dsrlnsllfp parpdqvqgl idkyepsgin aqrgqlspeg mvwflcgpen
      301 svlaqdklll hhdmtqplnh yfinsshnty ltagqfsgls saemyrqvll sgcrcveldc
      361 wkgkppdeep iithgftmtt diffkeaiea iaesafktsp ypiilsfenh vdsprqqakm
      421 aeycrtifgd mllteplekf plkpgvplps pedlrgkili knkknqfsgp tssskdtgge
      481 aegssppsap avwageegte leeeeveeee eeesgnldee eikkmqsdeg taglevtaye
      541 emsslvnyiq ptkfvsfefs aqknrsyvis sftelkaydl lskasvqfvd ynkrqmsriy
      601 pkgtrmdssn ympqmfwnag cqmvalnfqt mdlpmqqnma vfefngqsgy llkhefmrrp
      661 dkqfnpfsvd ridvvvattl sitvisgqfl sersvrtyve velfglpgdp krryrtklsp
      721 stnsinpvwk eepfvfekil mpelaslrva vmeegnkflg hriipinaln sgyhhlclhs
      781 esnmpltmpa lfiflemkdy ipgawadltv alanpikffs ahdtksvklk eamgglpekp
      841 fplaspvasq vngalaptsn gspaaragar eeamkeaaep rtasleelre lkgvvklqrr
      901 hekelreler rgarrweell qrgaaqlael gppgvggvga cklgpgkgsr kkrslprees
      961 agaapgegpe gvdgrvrelk drlelellrq geeqyecvlk rkeqhvaeqi skmmelarek
     1021 qaaelkalke tsendtkemk kkletkrler iqgmtkvttd kmaqerlkre innshiqevv
     1081 qvikqmtenl erhqekleek qaacleqire mekqfqkeal aeyearmkgl eaevkesvra
     1141 clrtcfpsea kdkperacec ppelceqdpl iakadaqesr l
//
LOCUS       NP_001352355             647 aa            linear   PRI 20-NOV-2025
DEFINITION  conserved oligomeric Golgi complex subunit 4 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001352355 XP_011521283
VERSION     NP_001352355.1
DBSOURCE    REFSEQ: accession NM_001365426.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 647)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 647)
  AUTHORS   Ferreira,C.R., Niiler,T., Duker,A.L., Jackson,A.P. and Bober,M.B.
  TITLE     Growth in individuals with Saul-Wilson syndrome
  JOURNAL   Am J Med Genet A 182 (9), 2110-2116 (2020)
   PUBMED   32652690
  REMARK    GeneRIF: Growth in individuals with Saul-Wilson syndrome.
REFERENCE   4  (residues 1 to 647)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 647)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   6  (residues 1 to 647)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   7  (residues 1 to 647)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   8  (residues 1 to 647)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   9  (residues 1 to 647)
  AUTHORS   Ferreira,C.
  TITLE     Saul-Wilson Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32078278
REFERENCE   10 (residues 1 to 647)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106804.4.
            
            On Jan 26, 2019 this sequence version replaced XP_011521283.1.
            
            Summary: The protein encoded by this gene is a component of an
            oligomeric protein complex involved in the structure and function
            of the Golgi apparatus. Defects in this gene may be a cause of
            congenital disorder of glycosylation type IIj. Two transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.103057.1,
                                           SRR1803614.239512.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..647
                     /product="conserved oligomeric Golgi complex subunit 4
                     isoform 3"
                     /note="complexed with Dor1p; conserved oligomeric Golgi
                     complex protein 4; COG complex subunit 4"
                     /calculated_mol_wt=73651
     Region          50..359
                     /region_name="COG4"
                     /note="COG4 transport protein; pfam08318"
                     /db_xref="CDD:462425"
     CDS             1..647
                     /gene="COG4"
                     /gene_synonym="CDG2J; COD1; SWILS"
                     /coded_by="NM_001365426.1:611..2554"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:25839"
                     /db_xref="HGNC:HGNC:18620"
                     /db_xref="MIM:606976"
ORIGIN      
        1 mdgvqtalrs edyeqaaaht hrylcldksv ielsrqgkeg smidanlkll qeaeqrlkai
       61 vaekfaiatk egdlpqverf fkifpllglh eeglrkfsey lckqvaskae enllmvlgtd
      121 msdrraavif adtltllfeg iarivethqp ivetyygpgr lytlikylqv ecdrqvekvv
      181 dkfikqrdyh qqfrhvqnnl mrnsttekie preldpilte vtlmnarsel ylrflkkris
      241 sdfevgdsma seevkqehqk cldkllnncl lsctmqelig lyvtmeeyfm retvnkaval
      301 dtyekgqlts smvddvfyiv kkcigralss ssidclcami nlattelesd frdvlcnklr
      361 mgfpattfqd iqrgvtsavn imhsslqqgk fdtkgiestd eakmsflvtl nnvevcseni
      421 stlkktlesd ctklfsqgig geqaqakfds clsdlaavsn kfrdllqegl telnstaikp
      481 qvqpwinsff svshnieeee fndyeandpw vqqfilnleq qmaefkasls pviydsltgl
      541 mtslvavele kvvlkstfnr lgglqfdkel rsliaylttv ttwtirdkfa rlsqmatiln
      601 lervteildy wgpnsgpltw rltpaevrqv lalridfrse dikrlrl
//
LOCUS       NP_001182192            1033 aa            linear   PRI 20-NOV-2025
DEFINITION  PDZ domain-containing protein 7 isoform 1 [Homo sapiens].
ACCESSION   NP_001182192
VERSION     NP_001182192.1
DBSOURCE    REFSEQ: accession NM_001195263.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1033)
  AUTHORS   Nouri,Z., Sarmadi,A., Narrei,S., Kianersi,H., Kianersi,F. and
            Tabatabaiefar,M.A.
  TITLE     Clinical characterizations and molecular genetic study of two
            co-segregating variants in PDZD7 and PDE6C genes leading
            simultaneously to non-syndromic hearing loss and achromatopsia
  JOURNAL   BMC Med Genomics 17 (1), 173 (2024)
   PUBMED   38956522
  REMARK    GeneRIF: Clinical characterizations and molecular genetic study of
            two co-segregating variants in PDZD7 and PDE6C genes leading
            simultaneously to non-syndromic hearing loss and achromatopsia.
            Erratum:[BMC Med Genomics. 2025 Aug 4;18(1):126. doi:
            10.1186/s12920-025-02197-2. PMID: 40760435]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1033)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1033)
  AUTHORS   Du,Q., Sun,Q., Gu,X., Wang,J., Li,W., Guo,L. and Li,H.
  TITLE     Novel homozygous variant in the PDZD7 gene in a family with
            nonsyndromic sensorineural hearing loss
  JOURNAL   BMC Med Genomics 15 (1), 135 (2022)
   PUBMED   35715776
  REMARK    GeneRIF: Novel homozygous variant in the PDZD7 gene in a family
            with nonsyndromic sensorineural hearing loss.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1033)
  AUTHORS   Lee,S.Y., Han,J.H., Kim,B.J., Oh,S.H., Lee,S., Oh,D.Y. and
            Choi,B.Y.
  TITLE     Identification of a Potential Founder Effect of a Novel PDZD7
            Variant Involved in Moderate-to-Severe Sensorineural Hearing Loss
            in Koreans
  JOURNAL   Int J Mol Sci 20 (17), 4174 (2019)
   PUBMED   31454969
  REMARK    GeneRIF: PDZD7 can be an important causative gene for moderate to
            severe ARNSHL in Koreans. Moreover, at least some, if not all,
            p.Arg164Trp alleles in Koreans could exert a potential founder
            effect and arise from diverse haplotypes as a mutational hot spot.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1033)
  AUTHORS   Luo,H., Hassan,R.N., Yan,J., Xie,J., Du,P., Hu,Q., Zhu,Y. and
            Jiang,W.
  TITLE     Novel recessive PDZD7 biallelic mutations associated with
            hereditary hearing loss in a Chinese pedigree
  JOURNAL   Gene 709, 65-74 (2019)
   PUBMED   31129248
  REMARK    GeneRIF: Three mutations in PDZD7 gene linked to autosomal
            recessive non-syndromic hearing loss (ARNSHL) were identified in a
            Chinese pedigree. The findings expand not only our knowledge of
            genetic causes of ARNSHL, but also PDZD7 genes mutation spectrum of
            the disease. They will aid personalized genetic counseling,
            molecular diagnostics and clinical management of this condition.
REFERENCE   6  (residues 1 to 1033)
  AUTHORS   Yoshimura,H., Iwasaki,S., Nishio,S.Y., Kumakawa,K., Tono,T.,
            Kobayashi,Y., Sato,H., Nagai,K., Ishikawa,K., Ikezono,T., Naito,Y.,
            Fukushima,K., Oshikawa,C., Kimitsuki,T., Nakanishi,H. and Usami,S.
  TITLE     Massively parallel DNA sequencing facilitates diagnosis of patients
            with Usher syndrome type 1
  JOURNAL   PLoS One 9 (3), e90688 (2014)
   PUBMED   24618850
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1033)
  AUTHORS   Grati,M., Shin,J.B., Weston,M.D., Green,J., Bhat,M.A.,
            Gillespie,P.G. and Kachar,B.
  TITLE     Localization of PDZD7 to the stereocilia ankle-link associates this
            scaffolding protein with the Usher syndrome protein network
  JOURNAL   J Neurosci 32 (41), 14288-14293 (2012)
   PUBMED   23055499
  REMARK    GeneRIF: PDZD7 is a scaffolding component of the ankle-link complex
            in stereocilia and is associated with the Usher syndrome protein
            network.
REFERENCE   8  (residues 1 to 1033)
  AUTHORS   Bohm,D., Keller,K., Pieter,J., Boehm,N., Wolters,D., Siggelkow,W.,
            Lebrecht,A., Schmidt,M., Kolbl,H., Pfeiffer,N. and Grus,F.H.
  TITLE     Comparison of tear protein levels in breast cancer patients and
            healthy controls using a de novo proteomic approach
  JOURNAL   Oncol Rep 28 (2), 429-438 (2012)
   PUBMED   22664934
REFERENCE   9  (residues 1 to 1033)
  AUTHORS   Ebermann,I., Phillips,J.B., Liebau,M.C., Koenekoop,R.K.,
            Schermer,B., Lopez,I., Schafer,E., Roux,A.F., Dafinger,C.,
            Bernd,A., Zrenner,E., Claustres,M., Blanco,B., Nurnberg,G.,
            Nurnberg,P., Ruland,R., Westerfield,M., Benzing,T. and Bolz,H.J.
  TITLE     PDZD7 is a modifier of retinal disease and a contributor to digenic
            Usher syndrome
  JOURNAL   J Clin Invest 120 (6), 1812-1823 (2010)
   PUBMED   20440071
  REMARK    GeneRIF: PDZD7 is a modifier of retinal disease and a contributor
            to digenic Usher syndrome.
REFERENCE   10 (residues 1 to 1033)
  AUTHORS   Schneider,E., Marker,T., Daser,A., Frey-Mahn,G., Beyer,V.,
            Farcas,R., Schneider-Ratzke,B., Kohlschmidt,N., Grossmann,B.,
            Bauss,K., Napiontek,U., Keilmann,A., Bartsch,O., Zechner,U.,
            Wolfrum,U. and Haaf,T.
  TITLE     Homozygous disruption of PDZD7 by reciprocal translocation in a
            consanguineous family: a new member of the Usher syndrome protein
            interactome causing congenital hearing impairment
  JOURNAL   Hum Mol Genet 18 (4), 655-666 (2009)
   PUBMED   19028668
  REMARK    GeneRIF: PDZD7 is a new autosomal-recessive deafness-causing gene
            and a prime candidate gene for Usher syndrome.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA197280.1, FJ617449.1,
            AK026862.1 and AL133215.17.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a ciliary protein homologous to proteins
            which are mutated in Usher syndrome patients, and mutations and
            translocations involving this gene have been associated with two
            types of Usher syndrome. Multiple transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: FJ617449.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000619208.6/ ENSP00000480489.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1033
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24.31"
     Protein         1..1033
                     /product="PDZ domain-containing protein 7 isoform 1"
                     /note="PDZ domain-containing protein 7; deafness,
                     autosomal recessive 57"
                     /calculated_mol_wt=111621
     Region          84..167
                     /region_name="PDZ1_PDZD7-like"
                     /note="PDZ domain 1 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd10833"
                     /db_xref="CDD:467269"
     Site            order(96..102,114,117,146,150,153..154)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467269"
     Region          208..292
                     /region_name="PDZ2_PDZD7-like"
                     /note="PDZ domain 2 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd10834"
                     /db_xref="CDD:467270"
     Site            order(221..227,239,242,271,275,278..279)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467270"
     Region          323..380
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          444..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          554..630
                     /region_name="HN_PDZD7_like"
                     /note="harmonin_N_like domain, a protein-binding module of
                     PDZ domain-containing protein 7 and related proteins;
                     cd07358"
                     /db_xref="CDD:259824"
     Site            order(555,558,562,575,578,581..582,585)
                     /site_type="other"
                     /note="putative protein binding site [polypeptide
                     binding]"
                     /db_xref="CDD:259824"
     Region          754..864
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     Region          860..948
                     /region_name="PDZ3_PDZD7-like"
                     /note="PDZ domain 3 of the canonical isoform 1 of PDZ
                     domain containing 7 (PDZD7), and related domains; cd06751"
                     /db_xref="CDD:467233"
     Site            order(871..877,891,894,924,928,931..932)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467233"
     Region          943..1033
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H5P4.2)"
     CDS             1..1033
                     /gene="PDZD7"
                     /gene_synonym="DFNB57; PDZK7"
                     /coded_by="NM_001195263.2:223..3324"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS73182.1"
                     /db_xref="GeneID:79955"
                     /db_xref="HGNC:HGNC:26257"
                     /db_xref="MIM:612971"
ORIGIN      
        1 maqgfavgfd plglgdlssg slsslssrgh lgsdsgstat ryllrkqqrl lngpprgira
       61 sspmgrvili nspieansde sdiihsvrve kspagrlgfs vrggsehglg ifvskveegs
      121 saeraglcvg dkitevngls lesttmgsav kvltsssrlh mmvrrmgrvp gikfskektt
      181 wvdvvnrrlv vekcgstpsd tssedgvrri vhlyttsddf clgfnirggk efglgiyvsk
      241 vdhgglaeen gikvgdqvla angvrfddis hsqavevlkg qthimltike tgrypaykem
      301 vseycwldrl sngvlqqlsp asessssvss cassapyssg slpsdrmdic lgqeepgsrg
      361 pgwgradtam qtepdaggrv etwcsvrptv ilrdtairsd gphpgrrlds alsespktal
      421 llalsrprpp itrsqsyltl weekqqrkke ksgspgekga lqrsktlmnl ffkggrqgrl
      481 ardgrreawt ldsgslakty prldiekagg vgpvqkfvtw rlrrdqergr allsarsgsp
      541 ssqlpnvdeq vqawesrrpl iqdlaqrllt ddevlavtrh csryvheggi edlvrpllai
      601 ldrpekllll qdirsvvapt dlgrfdsmvm lveleafeal ksravrppal rparqdtppk
      661 rhlitpvpds rggfyllpvn gfpeeednge lrerlgalkv spsasaprhp hkgipplqdv
      721 pvdaftplri actpppqlpp vaprplrpnw llteplsreh ppqsqirgra qsrsrsrsrs
      781 rsrssrgqgk spgrrspspv ptpapsmtng ryhkprkarp plprpldgea akvgakqgps
      841 esgtegtake aamknpsgel ktvtlskmkq slgisisggi eskvqpmvki ekifpggaaf
      901 lsgalqagfe lvavdgenle qvthqravdt irrayrnkar epmelvvrvp gpsprpspsd
      961 ssaltdgglp adhlpahqpl daapvpahwl pepptnpqtp ptdarllqpt pspapspalq
     1021 tpdskpapsp rip
//
LOCUS       NP_067038                326 aa            linear   PRI 20-NOV-2025
DEFINITION  regulation of nuclear pre-mRNA domain-containing protein 1B [Homo
            sapiens].
ACCESSION   NP_067038
VERSION     NP_067038.1
DBSOURCE    REFSEQ: accession NM_021215.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Jia,Y., Yan,Q., Zheng,Y., Li,L., Zhang,B., Chang,Z., Wang,Z.,
            Tang,H., Qin,Y. and Guan,X.Y.
  TITLE     Long non-coding RNA NEAT1 mediated RPRD1B stability facilitates
            fatty acid metabolism and lymph node metastasis via
            c-Jun/c-Fos/SREBP1 axis in gastric cancer
  JOURNAL   J Exp Clin Cancer Res 41 (1), 287 (2022)
   PUBMED   36171622
  REMARK    GeneRIF: Long non-coding RNA NEAT1 mediated RPRD1B stability
            facilitates fatty acid metabolism and lymph node metastasis via
            c-Jun/c-Fos/SREBP1 axis in gastric cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Siril,Y.J., Kouketsu,A., Saito,H., Takahashi,T. and Kumamoto,H.
  TITLE     Immunohistochemical expression levels of cyclin D1 and CREPT
            reflect the course and prognosis in oral precancerous lesions and
            squamous cell carcinoma
  JOURNAL   Int J Oral Maxillofac Surg 51 (1), 27-32 (2022)
   PUBMED   33838964
  REMARK    GeneRIF: Immunohistochemical expression levels of cyclin D1 and
            CREPT reflect the course and prognosis in oral precancerous lesions
            and squamous cell carcinoma.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Zhai,W., Ye,X., Wang,Y., Feng,Y., Wang,Y., Lin,Y., Ding,L.,
            Yang,L., Wang,X., Kuang,Y., Fu,X., Eugene Chin,Y., Jia,B., Zhu,B.,
            Ren,F. and Chang,Z.
  TITLE     CREPT/RPRD1B promotes tumorigenesis through STAT3-driven gene
            transcription in a p300-dependent manner
  JOURNAL   Br J Cancer 124 (8), 1437-1448 (2021)
   PUBMED   33531691
  REMARK    GeneRIF: CREPT/RPRD1B promotes tumorigenesis through STAT3-driven
            gene transcription in a p300-dependent manner.
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Wang,Y., Qiu,H., Hu,W., Li,S. and Yu,J.
  TITLE     RPRD1B promotes tumor growth by accelerating the cell cycle in
            endometrial cancer
  JOURNAL   Oncol Rep 31 (3), 1389-1395 (2014)
   PUBMED   24452636
  REMARK    GeneRIF: RPRD1B overexpression promotes tumor growth and
            accelerates cell cycle progression.
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Lu,D., Wu,Y., Wang,Y., Ren,F., Wang,D., Su,F., Zhang,Y., Yang,X.,
            Jin,G., Hao,X., He,D., Zhai,Y., Irwin,D.M., Hu,J., Sung,J.J.,
            Yu,J., Jia,B. and Chang,Z.
  TITLE     CREPT accelerates tumorigenesis by regulating the transcription of
            cell-cycle-related genes
  JOURNAL   Cancer Cell 21 (1), 92-104 (2012)
   PUBMED   22264791
  REMARK    GeneRIF: CREPT increases cyclin D1 transcription during
            tumorigenesis.
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Ni,Z., Olsen,J.B., Guo,X., Zhong,G., Ruan,E.D., Marcon,E.,
            Young,P., Guo,H., Li,J., Moffat,J., Emili,A. and Greenblatt,J.F.
  TITLE     Control of the RNA polymerase II phosphorylation state in promoter
            regions by CTD interaction domain-containing proteins RPRD1A and
            RPRD1B
  JOURNAL   Transcription 2 (5), 237-242 (2011)
   PUBMED   22231121
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G.,
            Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L.,
            Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M.,
            Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J.,
            Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P.,
            Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y.,
            Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R.,
            Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P.,
            Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L.,
            Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R.,
            Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L.,
            Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K.,
            Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A.,
            Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M.,
            Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L.,
            McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D.,
            Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A.,
            Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J.,
            Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T.,
            Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D.,
            Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M.,
            Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A.,
            Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L.,
            Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L.,
            Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and
            Rogers,J.
  TITLE     The DNA sequence and comparative analysis of human chromosome 20
  JOURNAL   Nature 414 (6866), 865-871 (2001)
   PUBMED   11780052
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP359144.1, BC033629.1 and AK092567.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033629.1, SRR1660805.10487.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373433.9/ ENSP00000362532.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.23"
     Protein         1..326
                     /product="regulation of nuclear pre-mRNA domain-containing
                     protein 1B"
                     /note="cell-cycle related and expression-elevated protein
                     in tumor; Ku70-binding protein 5-Hera"
                     /calculated_mol_wt=36769
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Region          3..131
                     /region_name="CID_RPRD1B"
                     /note="CID (CTD-Interacting Domain) of Regulation of
                     nuclear pre-mRNA domain-containing protein 1B; cd17012"
                     /db_xref="CDD:340809"
     Site            order(18..20,23,61,64..65,68..69,106,110,113..114)
                     /site_type="other"
                     /note="CTD binding site [polypeptide binding]"
                     /db_xref="CDD:340809"
     Region          127..149
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Site            161
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9NQG5.1)"
     Region          178..324
                     /region_name="CREPT"
                     /note="Cell-cycle alteration and expression-elevated
                     protein in tumour; pfam16566"
                     /db_xref="CDD:465181"
     Site            299
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q96P16; propagated from
                     UniProtKB/Swiss-Prot (Q9NQG5.1)"
     CDS             1..326
                     /gene="RPRD1B"
                     /gene_synonym="C20orf77; CREPT; dJ1057B20.2; K-H;
                     Kub5-Hera; NET60"
                     /coded_by="NM_021215.4:203..1183"
                     /db_xref="CCDS:CCDS13301.1"
                     /db_xref="GeneID:58490"
                     /db_xref="HGNC:HGNC:16209"
                     /db_xref="MIM:614694"
ORIGIN      
        1 mssfsesale kklselsnsq qsvqtlslwl ihhrkhagpi vsvwhrelrk aksnrkltfl
       61 ylandviqns krkgpeftre fesvlvdafs hvareadegc kkplerllni wqersvygge
      121 fiqqlklsme dskspppkat eekkslkrtf qqiqeeeddd ypgsyspqdp sagpllteel
      181 ikalqdlena asgdatvrqk iaslpqevqd vsllekitdk eaaerlsktv deaclllaey
      241 ngrlaaeled rrqlarmlve ytqnqkdvls ekekkleeyk qklarvtqvr kelkshiqsl
      301 pdlsllpnvt gglaplpsag dlfstd
//
LOCUS       NP_001287784             135 aa            linear   PRI 20-NOV-2025
DEFINITION  fos-related antigen 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001287784
VERSION     NP_001287784.1
DBSOURCE    REFSEQ: accession NM_001300855.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 135)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 135)
  AUTHORS   Li,L., Li,D., Jin,J., Xu,F., He,N., Ren,Y., Wang,X., Tian,L.,
            Chen,B., Li,X., Chen,Z., Zhang,L., Qiao,L., Wang,L. and Wang,J.
  TITLE     FOSL1-mediated LINC01566 negatively regulates CD4+ T-cell
            activation in myasthenia gravis
  JOURNAL   J Neuroinflammation 21 (1), 197 (2024)
   PUBMED   39113081
  REMARK    GeneRIF: FOSL1-mediated LINC01566 negatively regulates CD4[+]
            T-cell activation in myasthenia gravis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 135)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 135)
  AUTHORS   Ramar,V., Guo,S., Hudson,B., Khedri,A., Guo,A.A., Li,J. and Liu,M.
  TITLE     Interaction of NF-kappaB and FOSL1 drives glioma stemness
  JOURNAL   Cell Mol Life Sci 81 (1), 255 (2024)
   PUBMED   38856747
  REMARK    GeneRIF: Interaction of NF-kappaB and FOSL1 drives glioma stemness.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 135)
  AUTHORS   Luo,X., Wang,J., Chen,Y., Zhou,X., Shao,Z., Liu,K. and Shang,Z.
  TITLE     Melatonin inhibits the stemness of head and neck squamous cell
            carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis
  JOURNAL   J Pineal Res 76 (2), e12940 (2024)
   PUBMED   38402581
  REMARK    GeneRIF: Melatonin inhibits the stemness of head and neck squamous
            cell carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis.
REFERENCE   6  (residues 1 to 135)
  AUTHORS   Arts,J., Herr,I., Lansink,M., Angel,P. and Kooistra,T.
  TITLE     Cell-type specific DNA-protein interactions at the tissue-type
            plasminogen activator promoter in human endothelial and HeLa cells
            in vivo and in vitro
  JOURNAL   Nucleic Acids Res 25 (2), 311-317 (1997)
   PUBMED   9016559
REFERENCE   7  (residues 1 to 135)
  AUTHORS   Courseaux,A., Grosgeorge,J., Gaudray,P., Pannett,A.A., Forbes,S.A.,
            Williamson,C., Bassett,D., Thakker,R.V., Teh,B.T., Farnebo,F.,
            Shepherd,J., Skogseid,B., Larsson,C., Giraud,S., Zhang,C.X.,
            Salandre,J. and Calender,A.
  TITLE     Definition of the minimal MEN1 candidate area based on a 5-Mb
            integrated map of proximal 11q13. The European Consortium on Men1,
            (GENEM 1; Groupe d'Etude des Neoplasies Endocriniennes Multiples de
            type 1)
  JOURNAL   Genomics 37 (3), 354-365 (1996)
   PUBMED   8938448
REFERENCE   8  (residues 1 to 135)
  AUTHORS   Tsuchiya,H., Fujii,M., Niki,T., Tokuhara,M., Matsui,M. and Seiki,M.
  TITLE     Human T-cell leukemia virus type 1 Tax activates transcription of
            the human fra-1 gene through multiple cis elements responsive to
            transmembrane signals
  JOURNAL   J Virol 67 (12), 7001-7007 (1993)
   PUBMED   8230424
REFERENCE   9  (residues 1 to 135)
  AUTHORS   Sinke,R.J., Tanigami,A., Nakamura,Y. and Geurts van Kessel,A.
  TITLE     Reverse mapping of the gene encoding the human fos-related
            antigen-1 (fra-1) within chromosome band 11q13
  JOURNAL   Genomics 18 (1), 165 (1993)
   PUBMED   8276409
REFERENCE   10 (residues 1 to 135)
  AUTHORS   Matsui,M., Tokuhara,M., Konuma,Y., Nomura,N. and Ishizaki,R.
  TITLE     Isolation of human fos-related genes and their expression during
            monocyte-macrophage differentiation
  JOURNAL   Oncogene 5 (3), 249-255 (1990)
   PUBMED   2107490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ937004.1, BP222547.1,
            BC016648.1, AA120824.1 and AP006287.2.
            
            Summary: The Fos gene family consists of 4 members: FOS, FOSB,
            FOSL1, and FOSL2. These genes encode leucine zipper proteins that
            can dimerize with proteins of the JUN family, thereby forming the
            transcription factor complex AP-1. As such, the FOS proteins have
            been implicated as regulators of cell proliferation,
            differentiation, and transformation. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (3) uses an alternate splice
            junction at the 5' end of an exon compared to variant 1, that
            causes a frameshift. The resulting isoform (3) has a shorter and
            distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BP222547.1, CB150816.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145122
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..135
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..135
                     /product="fos-related antigen 1 isoform 3"
                     /note="FOS-like antigen-1; fos-related antigen 1; FOS like
                     1, AP-1 trancription factor subunit"
                     /calculated_mol_wt=14020
     CDS             1..135
                     /gene="FOSL1"
                     /gene_synonym="FRA; fra-1; FRA1"
                     /coded_by="NM_001300855.2:50..457"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS76437.1"
                     /db_xref="GeneID:8061"
                     /db_xref="HGNC:HGNC:13718"
                     /db_xref="MIM:136515"
ORIGIN      
        1 mfrdfgepgp ssgngggygg paqppaaaqa aqqkfhlvps intmsgsqel qwmvqphflg
       61 pssyprplty pqysppqprp gviralgppp gvrrrpceqp ggrgappska raeqagcgqv
      121 qepeegtdrl paggd
//
LOCUS       NP_004694                862 aa            linear   PRI 20-NOV-2025
DEFINITION  rab GTPase-binding effector protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004694
VERSION     NP_004694.2
DBSOURCE    REFSEQ: accession NM_004703.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 862)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 862)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 862)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 862)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 862)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 862)
  AUTHORS   Swanton,E., Bishop,N. and Woodman,P.
  TITLE     Human rabaptin-5 is selectively cleaved by caspase-3 during
            apoptosis
  JOURNAL   J Biol Chem 274 (53), 37583-37590 (1999)
   PUBMED   10608812
REFERENCE   7  (residues 1 to 862)
  AUTHORS   Neve,R.L., Coopersmith,R., McPhie,D.L., Santeufemio,C., Pratt,K.G.,
            Murphy,C.J. and Lynn,S.D.
  TITLE     The neuronal growth-associated protein GAP-43 interacts with
            rabaptin-5 and participates in endocytosis
  JOURNAL   J Neurosci 18 (19), 7757-7767 (1998)
   PUBMED   9742146
REFERENCE   8  (residues 1 to 862)
  AUTHORS   Vitale,G., Rybin,V., Christoforidis,S., Thornqvist,P.,
            McCaffrey,M., Stenmark,H. and Zerial,M.
  TITLE     Distinct Rab-binding domains mediate the interaction of Rabaptin-5
            with GTP-bound Rab4 and Rab5
  JOURNAL   EMBO J 17 (7), 1941-1951 (1998)
   PUBMED   9524117
REFERENCE   9  (residues 1 to 862)
  AUTHORS   Xiao,G.H., Shoarinejad,F., Jin,F., Golemis,E.A. and Yeung,R.S.
  TITLE     The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5
            GTPase activating protein (GAP) in modulating endocytosis
  JOURNAL   J Biol Chem 272 (10), 6097-6100 (1997)
   PUBMED   9045618
REFERENCE   10 (residues 1 to 862)
  AUTHORS   Stenmark,H., Vitale,G., Ullrich,O. and Zerial,M.
  TITLE     Rabaptin-5 is a direct effector of the small GTPase Rab5 in
            endocytic membrane fusion
  JOURNAL   Cell 83 (3), 423-432 (1995)
   PUBMED   8521472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB169027.1, BC041700.1, AK314183.1, AF098638.1, DB124187.1,
            AL157499.1, EB387308.1 and BM678290.1.
            
            On Jun 4, 2003 this sequence version replaced NP_004694.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.122092.1,
                                           SRR1803616.41935.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000537505.6/ ENSP00000445408.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..862
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..862
                     /product="rab GTPase-binding effector protein 1 isoform 1"
                     /note="rab GTPase-binding effector protein 1; rabaptin-5;
                     neurocrescin; rabaptin-4; rabaptin-5alpha; renal carcinoma
                     antigen NY-REN-17"
                     /calculated_mol_wt=99160
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q15276.2)"
     Region          9..495
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     Site            282
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15276.2)"
     Region          315..338
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15276.2)"
     Site            374
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15276.2)"
     Site            377
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15276.2)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15276.2)"
     Site            408
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15276.2)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q15276.2)"
     Region          435..447
                     /region_name="Interaction with AP1G1, AP1G2, GGA1, GGA2
                     and GGA3. /evidence=ECO:0000269|PubMed:14665628"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15276.2)"
     Region          533..839
                     /region_name="Rab5-bind"
                     /note="Rabaptin-like protein; pfam09311"
                     /db_xref="CDD:462752"
     CDS             1..862
                     /gene="RABEP1"
                     /gene_synonym="RAB5EP; RABPT5"
                     /coded_by="NM_004703.6:204..2792"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45592.1"
                     /db_xref="GeneID:9135"
                     /db_xref="HGNC:HGNC:17677"
                     /db_xref="MIM:603616"
ORIGIN      
        1 maqpgpasqp dvslqqrvae lekinaeflr aqqqleqefn qkrakfkely lakeedlkrq
       61 navlqaaqdd lghlrtqlwe aqaemenika iatvsentkq eaidevkrqw reevaslqav
      121 mketvrdyeh qfhlrleqer tqwaqyresa ereiadlrrr lsegqeeenl enemkkaqed
      181 aeklrsvvmp mekeiaalkd klteaedkik eleaskvkel nhyleaeksc rtdlemyvav
      241 lntqksvlqe daeklrkelh evchlleqer qqhnqlkhtw qkandqfles qrllmrdmqr
      301 meivltseql rqveelkkkd qeddeqqrln krkdhkkadv eeeikipvvc altqeessaq
      361 lsneeehlds trgsvhslda glllpsgdpf sksdndmfkd glrraqstds lgtsgslqsk
      421 algynykaks agnldesdfg plvgadsvse nfdtaslgsl qmpsgfmltk dqeraikamt
      481 peqeetasll ssvtqgmesa yvspsgyrlv setewnllqk evhnagnklg rrcdmcsnye
      541 kqlqgiqiqe aetrdqvkkl qlmlrqandq lektmkdkqe ledfikqsse dsshqisalv
      601 lraqaseill eelqqglsqa krdvqeqmav lmqsreqvse elvrlqkdnd slqgkhslhv
      661 slqqaedfil pdttealrel vlkyrediin vrtaadhvee klkaeilflk eqiqaeqclk
      721 enleetlqle ienckeeias isslkaeler ikvekgqles tlreksqqle slqeikisle
      781 eqlkketaak atveqlmfee knkaqrlqte ldvseqvqrd fvklsqtlqv qlerirqads
      841 lerirailnd tkltdinqlp et
//
LOCUS       NP_055054                351 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit beta [Homo sapiens].
ACCESSION   NP_055054
VERSION     NP_055054.1
DBSOURCE    REFSEQ: accession NM_014239.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Norris,K., Hodgson,R.E., Dornelles,T., Allen,K.E., Abell,B.M.,
            Ashe,M.P. and Campbell,S.G.
  TITLE     Mutational analysis of the alpha subunit of eIF2B provides insights
            into the role of eIF2B bodies in translational control and VWM
            disease
  JOURNAL   J Biol Chem 296, 100207 (2021)
   PUBMED   33334879
  REMARK    GeneRIF: Mutational analysis of the alpha subunit of eIF2B provides
            insights into the role of eIF2B bodies in translational control and
            VWM disease.
REFERENCE   3  (residues 1 to 351)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 351)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 351)
  AUTHORS   Gomez,E. and Pavitt,G.D.
  TITLE     Identification of domains and residues within the epsilon subunit
            of eukaryotic translation initiation factor 2B (eIF2Bepsilon)
            required for guanine nucleotide exchange reveals a novel activation
            function promoted by eIF2B complex formation
  JOURNAL   Mol Cell Biol 20 (11), 3965-3976 (2000)
   PUBMED   10805739
REFERENCE   6  (residues 1 to 351)
  AUTHORS   Kimball,S.R., Heinzinger,N.K., Horetsky,R.L. and Jefferson,L.S.
  TITLE     Identification of interprotein interactions between the subunits of
            eukaryotic initiation factors eIF2 and eIF2B
  JOURNAL   J Biol Chem 273 (5), 3039-3044 (1998)
   PUBMED   9446619
REFERENCE   7  (residues 1 to 351)
  AUTHORS   Yang,W. and Hinnebusch,A.G.
  TITLE     Identification of a regulatory subcomplex in the guanine nucleotide
            exchange factor eIF2B that mediates inhibition by phosphorylated
            eIF2
  JOURNAL   Mol Cell Biol 16 (11), 6603-6616 (1996)
   PUBMED   8887689
REFERENCE   8  (residues 1 to 351)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   9  (residues 1 to 351)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   10 (residues 1 to 351)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AL049780.4, BC011750.2 and AI265790.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes the beta subunit of eukaryotic
            initiation factor-2B (EIF2B). EIF2B is involved in protein
            synthesis and exchanges GDP and GTP for its activation and
            deactivation. [provided by RefSeq, Aug 2011].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.384109.1,
                                           SRR1803613.254333.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266126.10/ ENSP00000266126.5
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.3"
     Protein         1..351
                     /product="translation initiation factor eIF2B subunit
                     beta"
                     /note="translation initiation factor eIF-2B subunit beta;
                     S20I15; S20III15; eIF-2B GDP-GTP exchange factor subunit
                     beta; eukaryotic translation initiation factor 2B, subunit
                     2 beta, 39kDa; eIF2B GDP-GTP exchange factor subunit beta"
                     /calculated_mol_wt=38859
     Region          29..333
                     /region_name="IF-2B"
                     /note="Initiation factor 2 subunit family; pfam01008"
                     /db_xref="CDD:395798"
     CDS             1..351
                     /gene="EIF2B2"
                     /gene_synonym="EIF-2Bbeta; EIF2B; EIF2Bbeta; VWM2"
                     /coded_by="NM_014239.4:71..1126"
                     /db_xref="CCDS:CCDS9836.1"
                     /db_xref="GeneID:8892"
                     /db_xref="HGNC:HGNC:3258"
                     /db_xref="MIM:606454"
ORIGIN      
        1 mpgsaakgse lseriesfve tlkrgggprs seemaretlg llrqiitdhr wsnagelmel
       61 irregrrmta aqpsettvgn mvrrvlkiir eeygrlhgrs desdqqeslh klltsgglne
      121 dfsfhyaqlq sniieainel lvelegtmen iaaqalehih snevimtigf srtveaflke
      181 aarkrkfhvi vaecapfcqg hemavnlska giettvmtda aifavmsrvn kviigtktil
      241 angalravtg thtlalaakh hstplivcap mfklspqfpn eedsfhkfva peevlpfteg
      301 dilekvsvhc pvfdyvppel itlfisnigg napsyiyrlm selyhpddhv l
//
LOCUS       NP_001352289             427 aa            linear   PRI 20-NOV-2025
DEFINITION  elongation factor Tu, mitochondrial isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001352289 XP_011544230
VERSION     NP_001352289.1
DBSOURCE    REFSEQ: accession NM_001365360.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Zhang,J., Zhou,X.Y., Wang,A., Lai,Y.H., Zhang,X.F., Liu,X.T.,
            Wang,Z., Liu,Y.D., Tang,S.Y. and Chen,S.L.
  TITLE     Novel Tu translation elongation factor, mitochondrial (TUFM)
            homozygous variant in a consanguineous family with premature
            ovarian insufficiency
  JOURNAL   Clin Genet 104 (5), 516-527 (2023)
   PUBMED   37461298
  REMARK    GeneRIF: Novel Tu translation elongation factor, mitochondrial
            (TUFM) homozygous variant in a consanguineous family with premature
            ovarian insufficiency.
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Cipullo,M., Gese,G.V., Khawaja,A., Hallberg,B.M. and Rorbach,J.
  TITLE     Structural basis for late maturation steps of the human
            mitoribosomal large subunit
  JOURNAL   Nat Commun 12 (1), 3673 (2021)
   PUBMED   34135318
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Zhong,B.R., Zhou,G.F., Song,L., Wen,Q.X., Deng,X.J., Ma,Y.L.,
            Hu,L.T. and Chen,G.J.
  TITLE     TUFM is involved in Alzheimer's disease-like pathologies that are
            associated with ROS
  JOURNAL   FASEB J 35 (5), e21445 (2021)
   PUBMED   33774866
  REMARK    GeneRIF: TUFM is involved in Alzheimer's disease-like pathologies
            that are associated with ROS.
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Girodat,D., Blanchard,S.C., Wieden,H.J. and Sanbonmatsu,K.Y.
  TITLE     Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA
            Selection
  JOURNAL   J Mol Biol 432 (9), 3064-3077 (2020)
   PUBMED   32061931
  REMARK    GeneRIF: Elongation Factor Tu Switch I Element is a Gate for
            Aminoacyl-tRNA Selection.
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Chang,S.Y., Park,S.G., Kim,S. and Kang,C.Y.
  TITLE     Interaction of the C-terminal domain of p43 and the alpha subunit
            of ATP synthase. Its functional implication in endothelial cell
            proliferation
  JOURNAL   J Biol Chem 277 (10), 8388-8394 (2002)
   PUBMED   11741979
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Shah,Z.H., Migliosi,V., Miller,S.C., Wang,A., Friedman,T.B. and
            Jacobs,H.T.
  TITLE     Chromosomal locations of three human nuclear genes (RPSM12, TUFM,
            and AFG3L1) specifying putative components of the mitochondrial
            gene expression apparatus
  JOURNAL   Genomics 48 (3), 384-388 (1998)
   PUBMED   9545647
REFERENCE   8  (residues 1 to 427)
  AUTHORS   Ling,M., Merante,F., Chen,H.S., Duff,C., Duncan,A.M. and
            Robinson,B.H.
  TITLE     The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA
            sequence, genomic localization, genomic structure, and
            identification of a pseudogene
  JOURNAL   Gene 197 (1-2), 325-336 (1997)
   PUBMED   9332382
REFERENCE   9  (residues 1 to 427)
  AUTHORS   Woriax,V.L., Burkhart,W. and Spremulli,L.L.
  TITLE     Cloning, sequence analysis and expression of mammalian
            mitochondrial protein synthesis elongation factor Tu
  JOURNAL   Biochim Biophys Acta 1264 (3), 347-356 (1995)
   PUBMED   8547323
REFERENCE   10 (residues 1 to 427)
  AUTHORS   Wells,J., Henkler,F., Leversha,M. and Koshy,R.
  TITLE     A mitochondrial elongation factor-like protein is over-expressed in
            tumours and differentially expressed in normal tissues
  JOURNAL   FEBS Lett 358 (2), 119-125 (1995)
   PUBMED   7828719
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC133550.2.
            
            On Aug 20, 2018 this sequence version replaced XP_011544230.1.
            
            Summary: This gene encodes a protein which participates in protein
            translation in mitochondria. Mutations in this gene have been
            associated with combined oxidative phosphorylation deficiency
            resulting in lactic acidosis and fatal encephalopathy. A pseudogene
            has been identified on chromosome 17. [provided by RefSeq, Jul
            2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.551915.1,
                                           SRR5189667.403990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..427
                     /product="elongation factor Tu, mitochondrial isoform 2
                     precursor"
                     /EC_number="3.6.5.3"
                     /note="elongation factor Tu, mitochondrial; EF-Tu;
                     epididymis secretory sperm binding protein"
                     /calculated_mol_wt=46694
     Region          50..416
                     /region_name="TufA"
                     /note="Translation elongation factor EF-Tu, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0050"
                     /db_xref="CDD:439820"
     CDS             1..427
                     /gene="TUFM"
                     /gene_synonym="COXPD4; EF-TuMT; EFTU; P43"
                     /coded_by="NM_001365360.2:80..1363"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="GeneID:7284"
                     /db_xref="HGNC:HGNC:12420"
                     /db_xref="MIM:602389"
ORIGIN      
        1 mttmaaatll ratphfsgla agrtfllqgl lrllkapalp llcrglavea kktyvrdkph
       61 vnvgtighvd hgkttltaai tkilaeggga kfkkyeeidn apeerargit inaahveyst
      121 aarhyahtdc pghadyvknm itgtapldgc ilvvaandgp mpqtrehlll arqigvehvv
      181 vyvnkadavq dsemvelvel eirelltefg ykgeetpviv gsalcalegr dpelglksvq
      241 klldavdtyi pvpardlekp fllpveavys vpgrgtvvtg iemfhksler aeagdnlgal
      301 vrglkredlr rglvmvkpgs ikphqkveaq vyilskeegg rhkpfvshfm pvmfsltwdm
      361 acriilppek elampgedlk fnlilrqpmi lekgqrftlr dgnrtigtgl vtntlamtee
      421 eknikwg
//
LOCUS       NP_065836                122 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil and C2 domain-containing protein 2A isoform b [Homo
            sapiens].
ACCESSION   NP_065836
VERSION     NP_065836.2
DBSOURCE    REFSEQ: accession NM_020785.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Harion,M., Qebibo,L., Riquet,A., Rougeot,C., Afenjar,A., Garel,C.,
            Louha,M., Lacaze,E., Audic-Gerard,F., Barth,M., Berquin,P.,
            Bonneau,D., Bourdain,F., Busa,T., Colin,E., Cuisset,J.M., Des
            Portes,V., Dorison,N., Francannet,C., Heron,B., Laroche,C.,
            Lebrun,M., Metreau,J., Odent,S., Pasquier,L., Trujillo,Y.P.,
            Perrin,L., Pinson,L., Rivier,F., Sigaudy,S., Thauvin-Robinet,C.,
            Louvier,U.W., Labayle,O., Rodriguez,D., Valence,S. and Burglen,L.
  TITLE     New insights into CC2D2A-related Joubert syndrome
  JOURNAL   J Med Genet 60 (6), 578-586 (2023)
   PUBMED   36319078
  REMARK    GeneRIF: New insights into CC2D2A-related Joubert syndrome.
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Cabrita Pinto,R.L., Viaggi,S., Canale,E., Martinez Popple,M.,
            Capra,V., Conteduca,G., Testa,B., Coviello,D. and Covone,A.E.
  TITLE     Exome Analysis Reveals Novel Missense and Deletion Variants in the
            CC2D2A Gene as Causative of Joubert Syndrome
  JOURNAL   Genes (Basel) 14 (4), 810 (2023)
   PUBMED   37107568
  REMARK    GeneRIF: Exome Analysis Reveals Novel Missense and Deletion
            Variants in the CC2D2A Gene as Causative of Joubert Syndrome.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Barroso-Gil,M., Olinger,E., Ramsbottom,S.A., Molinari,E.,
            Miles,C.G. and Sayer,J.A.
  TITLE     Update of genetic variants in CEP120 and CC2D2A-With an emphasis on
            genotype-phenotype correlations, tissue specific transcripts and
            exploring mutation specific exon skipping therapies
  JOURNAL   Mol Genet Genomic Med 9 (12), e1603 (2021)
   PUBMED   33486889
  REMARK    GeneRIF: Update of genetic variants in CEP120 and CC2D2A-With an
            emphasis on genotype-phenotype correlations, tissue specific
            transcripts and exploring mutation specific exon skipping
            therapies.
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Khan,M.I., Latif,M., Saif,M., Ahmad,H., Khan,A.U., Naseer,M.I.,
            Hussain,H.M.J. and Jelani,M.
  TITLE     Whole exome sequencing identified a novel missense alteration in
            CC2D2A causing Joubert syndrome 9 in a Pakhtun family
  JOURNAL   J Gene Med 23 (1), e3279 (2021)
   PUBMED   32989887
  REMARK    GeneRIF: Whole exome sequencing identified a novel missense
            alteration in CC2D2A causing Joubert syndrome 9 in a Pakhtun
            family.
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Paterson,A.D., Lutufullah,M., Doherty,D.,
            Vincent,J.B. and Ayub,M.
  TITLE     Addendum. CC2D2A, encoding a coiled-coil and C2 domain protein,
            causes autosomal-recessive mental retardation with retinitis
            pigmentosa
  JOURNAL   Am J Hum Genet 83 (5), 656 (2008)
   PUBMED   19068953
  REMARK    GeneRIF: CC2D2A causes autosomal-recessive mental retardation with
            retinitis pigmentosa.
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Gorden,N.T., Arts,H.H., Parisi,M.A., Coene,K.L., Letteboer,S.J.,
            van Beersum,S.E., Mans,D.A., Hikida,A., Eckert,M., Knutzen,D.,
            Alswaid,A.F., Ozyurek,H., Dibooglu,S., Otto,E.A., Liu,Y.,
            Davis,E.E., Hutter,C.M., Bammler,T.K., Farin,F.M., Dorschner,M.,
            Topcu,M., Zackai,E.H., Rosenthal,P., Owens,K.N., Katsanis,N.,
            Vincent,J.B., Hildebrandt,F., Rubel,E.W., Raible,D.W., Knoers,N.V.,
            Chance,P.F., Roepman,R., Moens,C.B., Glass,I.A. and Doherty,D.
  TITLE     CC2D2A is mutated in Joubert syndrome and interacts with the
            ciliopathy-associated basal body protein CEP290
  JOURNAL   Am J Hum Genet 83 (5), 559-571 (2008)
   PUBMED   18950740
  REMARK    GeneRIF: CC2D2A is mutated in Joubert syndrome and interacts with
            the ciliopathy-associated basal body protein CEP290.
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Tallila,J., Jakkula,E., Peltonen,L., Salonen,R. and Kestila,M.
  TITLE     Identification of CC2D2A as a Meckel syndrome gene adds an
            important piece to the ciliopathy puzzle
  JOURNAL   Am J Hum Genet 82 (6), 1361-1367 (2008)
   PUBMED   18513680
  REMARK    GeneRIF: CC2D2A appears to have at least two cilia-related
            functions: the molecule seems to be a part of the basal body
            complex where the cilium is assembled from and also seems to act as
            a sensor for the intracellular calcium.
REFERENCE   8  (residues 1 to 122)
  AUTHORS   Noor,A., Windpassinger,C., Patel,M., Stachowiak,B., Mikhailov,A.,
            Azam,M., Irfan,M., Siddiqui,Z.K., Naeem,F., Paterson,A.D.,
            Lutfullah,M., Vincent,J.B. and Ayub,M.
  TITLE     CC2D2A, encoding a coiled-coil and C2 domain protein, causes
            autosomal-recessive mental retardation with retinitis pigmentosa
  JOURNAL   Am J Hum Genet 82 (4), 1011-1018 (2008)
   PUBMED   18387594
  REMARK    GeneRIF: A homozygous splice-site mutation segregating in the
            family with autosomal-recessive mental retardation, within a
            coiled-coil and C2 domain-containing gene, CC2D2A was identified.
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from N35522.1, DA860072.1,
            BC070395.1, BC053865.1 and AI376394.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 12, 2009 this sequence version replaced NP_065836.1.
            
            Summary: This gene encodes a coiled-coil and calcium binding domain
            protein that appears to play a critical role in cilia formation.
            Mutations in this gene cause Meckel syndrome type 6, as well as
            Joubert syndrome type 9. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region that results in a frameshift, and differs in the
            presence and absence of exons at its 3' end, compared to variant 1.
            The encoded isoform (b) has a distinct and significantly shorter
            C-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC070395.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155974, SAMEA2158188
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.32"
     Protein         1..122
                     /product="coiled-coil and C2 domain-containing protein 2A
                     isoform b"
                     /note="coiled-coil and C2 domain-containing protein 2A"
                     /calculated_mol_wt=13510
     CDS             1..122
                     /gene="CC2D2A"
                     /gene_synonym="COACH2; JBTS9; MKS6; RP93"
                     /coded_by="NM_020785.2:246..614"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS47027.2"
                     /db_xref="GeneID:57545"
                     /db_xref="HGNC:HGNC:29253"
                     /db_xref="MIM:612013"
ORIGIN      
        1 mnpreekvki iteefiende dadmgrqnkn skvrrqprkk qkptpfsrac wqilphlsag
       61 vpllgwehpv qgksfqatnc cpqgngvrki ppwqppgaca ggaqdpppey dsperptera
      121 gc
//
LOCUS       NP_068805                124 aa            linear   PRI 20-NOV-2025
DEFINITION  ragulator complex protein LAMTOR3 isoform 1 [Homo sapiens].
ACCESSION   NP_068805 XP_001723353 XP_001723417 XP_001724602
VERSION     NP_068805.1
DBSOURCE    REFSEQ: accession NM_021970.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 124)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 124)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 124)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 124)
  AUTHORS   Jansen,R.M., Peruzzo,R., Fromm,S.A., Yokom,A.L., Zoncu,R. and
            Hurley,J.H.
  TITLE     Structural basis for FLCN RagC GAP activation in MiT-TFE
            substrate-selective mTORC1 regulation
  JOURNAL   Sci Adv 8 (37), eadd2926 (2022)
   PUBMED   36103527
REFERENCE   5  (residues 1 to 124)
  AUTHORS   Gong,Y., Lv,Y., Xu,F., Xiu,Y., Lu,Y., Liu,Z. and Deng,L.
  TITLE     LAMTOR3 is a prognostic biomarker in kidney renal clear cell
            carcinoma
  JOURNAL   J Clin Lab Anal 36 (9), e24648 (2022)
   PUBMED   36082464
  REMARK    GeneRIF: LAMTOR3 is a prognostic biomarker in kidney renal clear
            cell carcinoma.
REFERENCE   6  (residues 1 to 124)
  AUTHORS   Lunin,V.V., Munger,C., Wagner,J., Ye,Z., Cygler,M. and Sacher,M.
  TITLE     The structure of the MAPK scaffold, MP1, bound to its partner, p14.
            A complex with a critical role in endosomal map kinase signaling
  JOURNAL   J Biol Chem 279 (22), 23422-23430 (2004)
   PUBMED   15016825
REFERENCE   7  (residues 1 to 124)
  AUTHORS   Paces-Fessy,M., Boucher,D., Petit,E., Paute-Briand,S. and
            Blanchet-Tournier,M.F.
  TITLE     The negative regulator of Gli, Suppressor of fused (Sufu),
            interacts with SAP18, Galectin3 and other nuclear proteins
  JOURNAL   Biochem J 378 (Pt 2), 353-362 (2004)
   PUBMED   14611647
REFERENCE   8  (residues 1 to 124)
  AUTHORS   Teis,D., Wunderlich,W. and Huber,L.A.
  TITLE     Localization of the MP1-MAPK scaffold complex to endosomes is
            mediated by p14 and required for signal transduction
  JOURNAL   Dev Cell 3 (6), 803-814 (2002)
   PUBMED   12479806
REFERENCE   9  (residues 1 to 124)
  AUTHORS   Wunderlich,W., Fialka,I., Teis,D., Alpi,A., Pfeifer,A.,
            Parton,R.G., Lottspeich,F. and Huber,L.A.
  TITLE     A novel 14-kilodalton protein interacts with the mitogen-activated
            protein kinase scaffold mp1 on a late endosomal/lysosomal
            compartment
  JOURNAL   J Cell Biol 152 (4), 765-776 (2001)
   PUBMED   11266467
REFERENCE   10 (residues 1 to 124)
  AUTHORS   Schaeffer,H.J., Catling,A.D., Eblen,S.T., Collier,L.S., Krauss,A.
            and Weber,M.J.
  TITLE     MP1: a MEK binding partner that enhances enzymatic activation of
            the MAP kinase cascade
  JOURNAL   Science 281 (5383), 1668-1671 (1998)
   PUBMED   9733512
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC026245.1, AF201947.1,
            AK022313.1, DA300823.1 and AP001962.2.
            
            On or before Mar 17, 2009 this sequence version replaced
            XP_001723417.1, XP_001723353.1, XP_001724602.1.
            
            Summary: This gene encodes a scaffold protein that functions in the
            extracellular signal-regulated kinase (ERK) cascade. The protein is
            localized to late endosomes by the mitogen-activated
            protein-binding protein-interacting protein, and binds specifically
            to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP
            kinase MAPK1/ERK2. Studies of the orthologous gene in mouse
            indicate that it regulates late endosomal traffic and cell
            proliferation. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. A pseudogene of
            this gene is located on the long arm of chromosome 13. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.47431.1,
                                           SRR1660807.249589.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000499666.7/ ENSP00000424183.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..124
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..124
                     /product="ragulator complex protein LAMTOR3 isoform 1"
                     /note="MAPK scaffold protein 1; mitogen-activated protein
                     kinase kinase 1 interacting protein 1; MEK binding partner
                     1; mitogen-activated protein kinase scaffold protein 1;
                     ragulator complex protein LAMTOR3; late
                     endosomal/lysosomal adaptor and MAPK and MTOR activator 3"
                     /calculated_mol_wt=13492
     Region          3..121
                     /region_name="MAPKK1_Int"
                     /note="Mitogen-activated protein kinase kinase 1
                     interacting; pfam08923"
                     /db_xref="CDD:462635"
     Region          57..70
                     /region_name="Required for interaction with LAMTOR2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHA4.1)"
     CDS             1..124
                     /gene="LAMTOR3"
                     /gene_synonym="MAP2K1IP1; MAPBP; MAPKSP1; MP1; PRO0633;
                     Ragulator3"
                     /coded_by="NM_021970.4:131..505"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3652.1"
                     /db_xref="GeneID:8649"
                     /db_xref="HGNC:HGNC:15606"
                     /db_xref="MIM:603296"
ORIGIN      
        1 maddlkrfly kklpsveglh aivvsdrdgv pvikvandna pehalrpgfl stfalatdqg
       61 sklglsknks iicyyntyqv vqfnrlplvv sfiasssant glivslekel aplfeelrqv
      121 vevs
//
LOCUS       NP_001159577             443 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional adapter 2-alpha isoform a [Homo sapiens].
ACCESSION   NP_001159577
VERSION     NP_001159577.2
DBSOURCE    REFSEQ: accession NM_001166105.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Cochino,A.V., Ioan,A., Farkas,O.M., Liu,M. and Lee,P.Y.
  TITLE     Novel ADA2 Variants in a Romanian Case Series of DADA2
  JOURNAL   J Clin Immunol 43 (8), 1788-1791 (2023)
   PUBMED   37783985
  REMARK    GeneRIF: Novel ADA2 Variants in a Romanian Case Series of DADA2.
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Zhang,X., Lei,G., Zhao,K., Zhang,X. and Dang,C.
  TITLE     CircTADA2A up-regulates MAPK8 by targeting MiR-214-3p and
            recruiting EIF4A3 to promote the invasion and migration of
            non-small cell lung cancer cells
  JOURNAL   Histol Histopathol 38 (7), 837-848 (2023)
   PUBMED   36193940
  REMARK    GeneRIF: CircTADA2A up-regulates MAPK8 by targeting MiR-214-3p and
            recruiting EIF4A3 to promote the invasion and migration of
            non-small cell lung cancer cells.
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Ehlers,L., Bucciol,G., Beysen,D. and Meyts,I.
  CONSRTM   KU Leuven - UZA DADA2 team
  TITLE     ADA2 Deficiency Mimicking Acute Disseminated Encephalomyelitis
  JOURNAL   J Clin Immunol 43 (3), 536-539 (2023)
   PUBMED   36472692
  REMARK    GeneRIF: ADA2 Deficiency Mimicking Acute Disseminated
            Encephalomyelitis.
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Zhang,Y., Yao,H., Li,Y., Yang,L., Zhang,L., Chen,J., Wang,Y. and
            Li,X.
  TITLE     Circular RNA TADA2A promotes proliferation and migration via
            modulating of miR-638/KIAA0101 signal in non-small cell lung cancer
  JOURNAL   Oncol Rep 46 (3) (2021)
   PUBMED   34296306
  REMARK    GeneRIF: Circular RNA TADA2A promotes proliferation and migration
            via modulating of miR638/KIAA0101 signal in nonsmall cell lung
            cancer.
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Ogryzko,V.V., Kotani,T., Zhang,X., Schiltz,R.L., Howard,T.,
            Yang,X.J., Howard,B.H., Qin,J. and Nakatani,Y.
  TITLE     Histone-like TAFs within the PCAF histone acetylase complex
  JOURNAL   Cell 94 (1), 35-44 (1998)
   PUBMED   9674425
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Henriksson,A., Almlof,T., Ford,J., McEwan,I.J., Gustafsson,J.A. and
            Wright,A.P.
  TITLE     Role of the Ada adaptor complex in gene activation by the
            glucocorticoid receptor
  JOURNAL   Mol Cell Biol 17 (6), 3065-3073 (1997)
   PUBMED   9154805
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Carter,K.C., Wang,L., Shell,B.K., Zamir,I., Berger,S.L. and
            Moore,P.A.
  TITLE     The human transcriptional adaptor genes TADA2L and GCN5L2
            colocalize to chromosome 17q12-q21 and display a similar tissue
            expression pattern
  JOURNAL   Genomics 40 (3), 497-500 (1997)
   PUBMED   9073520
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Wang,L., Mizzen,C., Ying,C., Candau,R., Barlev,N., Brownell,J.,
            Allis,C.D. and Berger,S.L.
  TITLE     Histone acetyltransferase activity is conserved between yeast and
            human GCN5 and is required for complementation of growth and
            transcriptional activation
  JOURNAL   Mol Cell Biol 17 (1), 519-527 (1997)
   PUBMED   8972232
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Candau,R., Moore,P.A., Wang,L., Barlev,N., Ying,C.Y., Rosen,C.A.
            and Berger,S.L.
  TITLE     Identification of human proteins functionally conserved with the
            yeast putative adaptors ADA2 and GCN5
  JOURNAL   Mol Cell Biol 16 (2), 593-602 (1996)
   PUBMED   8552087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA244842.1, AK225918.1,
            BC011753.2 and AC243654.3.
            
            On May 9, 2014 this sequence version replaced NP_001159577.1.
            
            Summary: Many DNA-binding transcriptional activator proteins
            enhance the initiation rate of RNA polymerase II-mediated gene
            transcription by interacting functionally with the general
            transcription machinery bound at the basal promoter. Adaptor
            proteins are usually required for this activation, possibly to
            acetylate and destabilize nucleosomes, thereby relieving chromatin
            constraints at the promoter. The protein encoded by this gene is a
            transcriptional activator adaptor and has been found to be part of
            the PCAF histone acetylase complex. Several alternatively spliced
            transcript variants encoding different isoforms of this gene have
            been described, but the full-length nature of some of these
            variants has not been determined. [provided by RefSeq, Oct 2009].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 both encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.30005.1,
                                           SRR1803617.101202.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000615182.5/ ENSP00000481091.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..443
                     /product="transcriptional adapter 2-alpha isoform a"
                     /note="transcriptional adaptor 2 alpha; transcriptional
                     adapter 2-alpha; ADA2-like protein"
                     /calculated_mol_wt=51365
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine, in variant Ser-6.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75478.3)"
     Region          28..440
                     /region_name="COG5114"
                     /note="Histone acetyltransferase complex SAGA/ADA, subunit
                     ADA2 [Chromatin structure and dynamics]"
                     /db_xref="CDD:227445"
     Region          348..372
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75478.3)"
     CDS             1..443
                     /gene="TADA2A"
                     /gene_synonym="ADA2; ADA2A; hADA2; KL04P; TADA2L"
                     /coded_by="NM_001166105.3:162..1493"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS11319.1"
                     /db_xref="GeneID:6871"
                     /db_xref="HGNC:HGNC:11531"
                     /db_xref="MIM:602276"
ORIGIN      
        1 mdrlgsfsnd psdkppcrgc ssylmepyik caecgpppff lclqcftrgf eykkhqsdht
       61 yeimtsdfpv ldpswtaqee malleavmdc gfgnwqdvan qmctktkeec ekhymkhfin
      121 nplfastlln lkqaeeakta dtaipfhstd dpprptfdsl lsrdmagymp aradfieefd
      181 nyaewdlrdi dfveddsdil halkmavvdi yhsrlkerqr rkkiirdhgl inlrkfqlme
      241 rrypkevqdl yetmrrfari vgpvehdkfi eshalefelr reikrlqeyr tagitnfcsa
      301 rtydhlkktr eeerlkrtml sevlqyiqds sacqqwlrrq adidsglsps ipmasnsgrr
      361 sapplnltgl pgteklneke kelcqmvrlv pgayleyksa llnecnkqgg lrlaqarali
      421 kidvnktrki ydfliregyi tkg
//
LOCUS       NP_004435                987 aa            linear   PRI 20-NOV-2025
DEFINITION  ephrin type-B receptor 4 precursor [Homo sapiens].
ACCESSION   NP_004435
VERSION     NP_004435.3
DBSOURCE    REFSEQ: accession NM_004444.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 987)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 987)
  AUTHORS   Vanden Broek,K., Ryu,J.R., Perrier,R., Tyndall,A.V., Childs,S.J.
            and Au,P.Y.B.
  TITLE     SAM domain variants of EPHB4 associated with aberrant signaling are
            linked to lymphatic-related fetal hydrops and facial dysmorphology
  JOURNAL   Clin Genet 105 (4), 386-396 (2024)
   PUBMED   38151336
  REMARK    GeneRIF: SAM domain variants of EPHB4 associated with aberrant
            signaling are linked to lymphatic-related fetal hydrops and facial
            dysmorphology.
            Erratum:[Clin Genet. 2024 Nov;106(5):664. doi: 10.1111/cge.14597.
            PMID: 39073083]
REFERENCE   3  (residues 1 to 987)
  AUTHORS   Ullah,A., Razzaq,A., Zhou,C., Ullah,N., Shehzadi,S., Aziz,T.,
            Alfaifi,M.Y., Elbehairi,S.E.I. and Iqbal,H.
  TITLE     Biological Significance of EphB4 Expression in Cancer
  JOURNAL   Curr Protein Pept Sci 25 (3), 244-255 (2024)
   PUBMED   37909437
  REMARK    GeneRIF: Biological Significance of EphB4 Expression in Cancer.
            Review article
REFERENCE   4  (residues 1 to 987)
  AUTHORS   Sesen,J., Ghalali,A., Driscoll,J., Martinez,T., Lupieri,A.,
            Zurakowski,D., Alexandrescu,S., Smith,E.R. and Fehnel,K.P.
  TITLE     Discovery and Characterization of Ephrin B2 and EphB4 Dysregulation
            and Novel Mutations in Cerebral Cavernous Malformations: In Vitro
            and Patient-Derived Evidence of Ephrin-Mediated Endothelial Cell
            Pathophysiology
  JOURNAL   Cell Mol Neurobiol 44 (1), 12 (2023)
   PUBMED   38150042
  REMARK    GeneRIF: Discovery and Characterization of Ephrin B2 and EphB4
            Dysregulation and Novel Mutations in Cerebral Cavernous
            Malformations: In Vitro and Patient-Derived Evidence of
            Ephrin-Mediated Endothelial Cell Pathophysiology.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 987)
  AUTHORS   Vish,K.J., Stiegler,A.L. and Boggon,T.J.
  TITLE     Diverse p120RasGAP interactions with doubly phosphorylated partners
            EphB4, p190RhoGAP, and Dok1
  JOURNAL   J Biol Chem 299 (9), 105098 (2023)
   PUBMED   37507023
  REMARK    GeneRIF: Diverse p120RasGAP interactions with doubly phosphorylated
            partners EphB4, p190RhoGAP, and Dok1.
REFERENCE   6  (residues 1 to 987)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   7  (residues 1 to 987)
  AUTHORS   Berclaz,G., Andres,A.C., Albrecht,D., Dreher,E., Ziemiecki,A.,
            Gusterson,B.A. and Crompton,M.R.
  TITLE     Expression of the receptor protein tyrosine kinase myk-1/htk in
            normal and malignant mammary epithelium
  JOURNAL   Biochem Biophys Res Commun 226 (3), 869-875 (1996)
   PUBMED   8831703
REFERENCE   8  (residues 1 to 987)
  AUTHORS   Bennett,B.D., Wang,Z., Kuang,W.J., Wang,A., Groopman,J.E.,
            Goeddel,D.V. and Scadden,D.T.
  TITLE     Cloning and characterization of HTK, a novel transmembrane tyrosine
            kinase of the EPH subfamily
  JOURNAL   J Biol Chem 269 (19), 14211-14218 (1994)
   PUBMED   8188704
REFERENCE   9  (residues 1 to 987)
  AUTHORS   Andres,A.C., Reid,H.H., Zurcher,G., Blaschke,R.J., Albrecht,D. and
            Ziemiecki,A.
  TITLE     Expression of two novel eph-related receptor protein tyrosine
            kinases in mammary gland development and carcinogenesis
  JOURNAL   Oncogene 9 (5), 1461-1467 (1994)
   PUBMED   8152808
  REMARK    Erratum:[Oncogene 1994 Aug;9(8):2431]
REFERENCE   10 (residues 1 to 987)
  AUTHORS   Bayrak-Toydemir,P. and Stevenson,D.A.
  TITLE     Capillary Malformation-Arteriovenous Malformation Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   21348050
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011895.4, CB962032.1,
            BC052804.1 and AY056048.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 11, 2003 this sequence version replaced NP_004435.2.
            
            Summary: Ephrin receptors and their ligands, the ephrins, mediate
            numerous developmental processes, particularly in the nervous
            system. Based on their structures and sequence relationships,
            ephrins are divided into the ephrin-A (EFNA) class, which are
            anchored to the membrane by a glycosylphosphatidylinositol linkage,
            and the ephrin-B (EFNB) class, which are transmembrane proteins.
            The Eph family of receptors are divided into 2 groups based on the
            similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. Ephrin
            receptors make up the largest subgroup of the receptor tyrosine
            kinase (RTK) family. The protein encoded by this gene binds to
            ephrin-B2 and plays an essential role in vascular development.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052804.1, U07695.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358173.8/ ENSP00000350896.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..987
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..987
                     /product="ephrin type-B receptor 4 precursor"
                     /EC_number="2.7.10.1"
                     /note="hepatoma transmembrane kinase; ephrin type-B
                     receptor 4; ephrin receptor EphB4; tyrosine-protein kinase
                     TYRO11; tyrosine-protein kinase receptor HTK"
                     /calculated_mol_wt=106642
     sig_peptide     1..15
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1647
     mat_peptide     16..987
                     /product="ephrin type-B receptor 4"
                     /calculated_mol_wt=106642
     Region          17..196
                     /region_name="EphR_LBD_B4"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 4;
                     cd10474"
                     /db_xref="CDD:198442"
     Site            order(27,29,43..46,48..50,52,54,56,59..60,93,95,147,149,
                     155..157,159,184..186,188)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198442"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Region          <321..>514
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Site            335
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Site            426
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Region          434..526
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(434,499,514)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Site            order(515..516,518..519)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Site            540..560
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54760.2)"
     Region          <564..612
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          610..878
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(621..625,629,645,647,693..694,696,700,740,744..745,
                     747,758,779..783,792,826)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(621..623,625,629,645,647,693..694,696,700,745,747,
                     758)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(740,744,779..783,792,826)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            757..785
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Site            770
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Region          907..973
                     /region_name="SAM_EPH-B4"
                     /note="SAM domain of EPH-B4 subfamily of tyrosine kinase
                     receptors; cd09554"
                     /db_xref="CDD:188953"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Site            order(924,957)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188953"
     Site            943
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Region          965..987
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P54760.2)"
     Site            976
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     Region          985..987
                     /region_name="PDZ-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P54760.2)"
     Site            987
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P54760.2)"
     CDS             1..987
                     /gene="EPHB4"
                     /gene_synonym="CMAVM2; HFASD; HTK; LMPHM7; MYK1; TYRO11"
                     /coded_by="NM_004444.5:494..3457"
                     /db_xref="CCDS:CCDS5706.1"
                     /db_xref="GeneID:2050"
                     /db_xref="HGNC:HGNC:3395"
                     /db_xref="MIM:600011"
ORIGIN      
        1 melrvllcwa slaaaleetl lntkletadl kwvtfpqvdg qweelsglde eqhsvrtyev
       61 cdvqrapgqa hwlrtgwvpr rgavhvyatl rftmleclsl pragrscket ftvfyyesda
      121 dtataltpaw menpyikvdt vaaehltrkr pgaeatgkvn vktlrlgpls kagfylafqd
      181 qgacmallsl hlfykkcaql tvnltrfpet vprelvvpva gscvvdavpa pgpspslycr
      241 edgqwaeqpv tgcscapgfe aaegntkcra caqgtfkpls gegscqpcpa nshsntigsa
      301 vcqcrvgyfr artdprgapc ttppsaprsv vsrlngsslh lewsaplesg gredltyalr
      361 crecrpggsc apcggdltfd pgprdlvepw vvvrglrpdf tytfevtaln gvsslatgpv
      421 pfepvnvttd revppavsdi rvtrsspssl slawavprap sgavldyevk yhekgaegps
      481 svrflktsen raelrglkrg asylvqvrar seagygpfgq ehhsqtqlde segwreqlal
      541 iagtavvgvv lvlvvivvav lclrkqsngr eaeysdkhgq ylighgtkvy idpftyedpn
      601 eavrefakei dvsyvkieev igagefgevc rgrlkapgkk escvaiktlk ggyterqrre
      661 flseasimgq fehpniirle gvvtnsmpvm iltefmenga ldsflrlndg qftviqlvgm
      721 lrgiasgmry laemsyvhrd laarnilvns nlvckvsdfg lsrfleenss dptytsslgg
      781 kipirwtape aiafrkftsa sdawsygivm wevmsfgerp ywdmsnqdvi naieqdyrlp
      841 pppdcptslh qlmldcwqkd rnarprfpqv vsaldkmirn paslkivare nggashplld
      901 qrqphysafg svgewlraik mgryeesfaa agfgsfelvs qisaedllri gvtlaghqkk
      961 ilasvqhmks qakpgtpggt ggpapqy
//
LOCUS       NP_001338638             792 aa            linear   PRI 20-NOV-2025
DEFINITION  trafficking protein particle complex subunit 10 isoform b [Homo
            sapiens].
ACCESSION   NP_001338638 XP_016855341 XP_016883944
VERSION     NP_001338638.1
DBSOURCE    REFSEQ: accession NM_001351709.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 792)
  AUTHORS   Rawlins,L.E., Almousa,H., Khan,S., Collins,S.C., Milev,M.P.,
            Leslie,J., Saint-Dic,D., Khan,V., Hincapie,A.M., Day,J.O.,
            McGavin,L., Rowley,C., Harlalka,G.V., Vancollie,V.E., Ahmad,W.,
            Lelliott,C.J., Gul,A., Yalcin,B., Crosby,A.H., Sacher,M. and
            Baple,E.L.
  TITLE     Biallelic variants in TRAPPC10 cause a microcephalic TRAPPopathy
            disorder in humans and mice
  JOURNAL   PLoS Genet 18 (3), e1010114 (2022)
   PUBMED   35298461
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 792)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 792)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 792)
  AUTHORS   Cuenca,A., Insinna,C., Zhao,H., John,P., Weiss,M.A., Lu,Q.,
            Walia,V., Specht,S., Manivannan,S., Stauffer,J., Peden,A.A. and
            Westlake,C.J.
  TITLE     The C7orf43/TRAPPC14 component links the TRAPPII complex to Rabin8
            for preciliary vesicle tethering at the mother centriole during
            ciliogenesis
  JOURNAL   J Biol Chem 294 (42), 15418-15434 (2019)
   PUBMED   31467083
REFERENCE   5  (residues 1 to 792)
  AUTHORS   Lafreniere,R.G., Kibar,Z., Rochefort,D.L., Han,F.Y., Fon,E.A.,
            Dube,M.P., Kang,X., Baird,S., Korneluk,R.G., Rommens,J.M. and
            Rouleau,G.A.
  TITLE     Genomic structure of the human GT334 (EHOC-1) gene mapping to
            21q22.3
  JOURNAL   Gene 198 (1-2), 313-321 (1997)
   PUBMED   9370297
REFERENCE   6  (residues 1 to 792)
  AUTHORS   Nagamine,K., Kudoh,J., Minoshima,S., Kawasaki,K., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Genomic organization and complete nucleotide sequence of the human
            PWP2 gene on chromosome 21
  JOURNAL   Genomics 42 (3), 528-531 (1997)
   PUBMED   9205129
REFERENCE   7  (residues 1 to 792)
  AUTHORS   Nagamine,K., Kudoh,J., Kawasaki,K., Minoshima,S., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Genomic organization and complete nucleotide sequence of the TMEM1
            gene on human chromosome 21q22.3
  JOURNAL   Biochem Biophys Res Commun 235 (1), 185-190 (1997)
   PUBMED   9196060
REFERENCE   8  (residues 1 to 792)
  AUTHORS   Nagamine,K., Kudoh,J., Minoshima,S., Kawasaki,K., Asakawa,S.,
            Ito,F. and Shimizu,N.
  TITLE     Isolation of cDNA for a novel human protein KNP-I that is
            homologous to the E. coli SCRP-27A protein from the autoimmune
            polyglandular disease type I (APECED) region of chromosome 21q22.3
  JOURNAL   Biochem Biophys Res Commun 225 (2), 608-616 (1996)
   PUBMED   8753807
REFERENCE   9  (residues 1 to 792)
  AUTHORS   Yamakawa,K., Mitchell,S., Hubert,R., Chen,X.N., Colbern,S.,
            Huo,Y.K., Gadomski,C., Kim,U.J. and Korenberg,J.R.
  TITLE     Isolation and characterization of a candidate gene for progressive
            myoclonus epilepsy on 21q22.3
  JOURNAL   Hum Mol Genet 4 (4), 709-716 (1995)
   PUBMED   7633421
REFERENCE   10 (residues 1 to 792)
  AUTHORS   Tekendo-Ngongang,C., Muenke,M. and Kruszka,P.
  TITLE     Holoprosencephaly Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301702
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB001523.1 and AB001517.1.
            
            On or before May 23, 2017 this sequence version replaced
            XP_016883944.1, XP_016855341.1.
            
            Summary: The protein encoded by this gene is a transmembrane
            protein found in the cis-Golgi complex. The encoded protein is part
            of the multisubunit transport protein particle (TRAPP) complex and
            may be involved in vesicular transport from the endoplasmic
            reticulum to the Golgi. Mutations in this gene could be responsible
            for the Unverricht-Lundborg type of progressive myoclonus epilepsy,
            or for autoimmune polyglandular disease type 1. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks
            several coding exons at the 5' end, and uses a novel splice in an
            internal exon, resulting in the use of a downstream start codon
            compared to variant1. The encoded isoform (b) has a shorter
            N-terminus compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2301607.1,
                                           SRR1803613.116146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..792
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..792
                     /product="trafficking protein particle complex subunit 10
                     isoform b"
                     /note="transmembrane protein 1; TRAPP 130 kDa subunit;
                     trafficking protein particle complex subunit 130; epilepsy
                     holoprosencephaly candidate-1 protein; trafficking protein
                     particle complex 10; transport protein particle subunit
                     TMEM1; TRAPP subunit TMEM1; trafficking protein particle
                     complex subunit TMEM1"
                     /calculated_mol_wt=88257
     Region          602..779
                     /region_name="TRAPPC10"
                     /note="Trafficking protein particle complex subunit 10,
                     TRAPPC10; pfam12584"
                     /db_xref="CDD:403698"
     CDS             1..792
                     /gene="TRAPPC10"
                     /gene_synonym="EHOC-1; EHOC1; GT334; NEDMISS; TMEM1;
                     TRS130; TRS30"
                     /coded_by="NM_001351709.1:467..2845"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:7109"
                     /db_xref="HGNC:HGNC:11868"
                     /db_xref="MIM:602103"
ORIGIN      
        1 mytsigrirs akfvgkdlae fymrkkapqk aeiylqgalk nylaegwalp ithtrkqlae
       61 cqkhlgqien ylqtssllas dhhlteeerk hfcqeildfa sqpsdspghk ivlpmhsfaq
      121 lrdlhfdpsn avvhvggvlc veitmysqmp vpvhveqivv nvhfsiekns yrktaewltk
      181 hktsngiinf ppetapfpvs qnslpalely emferspsdn slnttgiicr nvhmllrrqe
      241 sssslempsg valeegahvl rcshvtlepg anqitfrtqa kepgtytlrq lcasvgsvwf
      301 vlphiypivq ydvysqepql hvepladsll agipqrvkft vttghytikn gdslqlsnae
      361 amlilcqaes ravvysntre qsseaalriq ssdkvtsisl pvapayhvie felevlslps
      421 apalggesdm lgmaephrkh kdkqrtgrcm vttdhkvsid cpwsiystvi altfsvpfrt
      481 thsllssgtr kyvqvcvqnl seldfqlsds ylvdtgdstd lqlvplntqs qqpiyskqsv
      541 ffvwelkwte epppslhcrf svgfspasee qlsislkpyt yefkvenfft lynvkaeifp
      601 psgmeycrtg slcslevlit rlsdllevdk dealtesdeh fstklmyevv dnssnwavcg
      661 kscgvismpv aarathrvhm evmplfagyl plpdvrlfky lphhsahssq ldadswiend
      721 slsvdkhgdd qpdssslksr gsvhsacsse hkglpmprlq alpagqvfns ssgtqvlvip
      781 sqddhvlevs vt
//
LOCUS       NP_001229526             175 aa            linear   PRI 20-NOV-2025
DEFINITION  BOS complex subunit TMEM147 isoform 2 [Homo sapiens].
ACCESSION   NP_001229526
VERSION     NP_001229526.1
DBSOURCE    REFSEQ: accession NM_001242597.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   Ghorashi,T., Darvish,H., Bakhtiari,S., Tafakhori,A., Kruer,M.C. and
            Mozdarani,H.
  TITLE     A biallelic loss-of-function variant in TMEM147 causes profound
            intellectual disability and spasticity
  JOURNAL   Neurogenetics 24 (4), 311-316 (2023)
   PUBMED   37668766
  REMARK    GeneRIF: A biallelic loss-of-function variant in TMEM147 causes
            profound intellectual disability and spasticity.
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Cheng,S., Li,J., Xu,M., Bao,Q., Wu,J., Sun,P. and Han,B.
  TITLE     TMEM147 Correlates with Immune Infiltration and Serve as a
            Potential Prognostic Biomarker in Hepatocellular Carcinoma
  JOURNAL   Anal Cell Pathol (Amst) 2023, 4413049 (2023)
   PUBMED   37305689
  REMARK    GeneRIF: TMEM147 Correlates with Immune Infiltration and Serve as a
            Potential Prognostic Biomarker in Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Sundaram,A., Yamsek,M., Zhong,F., Hooda,Y., Hegde,R.S. and
            Keenan,R.J.
  TITLE     Substrate-driven assembly of a translocon for multipass membrane
            proteins
  JOURNAL   Nature 611 (7934), 167-172 (2022)
   PUBMED   36261522
REFERENCE   4  (residues 1 to 175)
  AUTHORS   Thomas,Q., Motta,M., Gautier,T., Zaki,M.S., Ciolfi,A., Paccaud,J.,
            Girodon,F., Boespflug-Tanguy,O., Besnard,T., Kerkhof,J.,
            McConkey,H., Masson,A., Denomme-Pichon,A.S., Cogne,B., Trochu,E.,
            Vignard,V., El It,F., Rodan,L.H., Alkhateeb,M.A., Jamra,R.A.,
            Duplomb,L., Tisserant,E., Duffourd,Y., Bruel,A.L., Jackson,A.,
            Banka,S., McEntagart,M., Saggar,A., Gleeson,J.G., Sievert,D.,
            Bae,H., Lee,B.H., Kwon,K., Seo,G.H., Lee,H., Saeed,A., Anjum,N.,
            Cheema,H., Alawbathani,S., Khan,I., Pinto-Basto,J., Teoh,J.,
            Wong,J., Sahari,U.B.M., Houlden,H., Zhelcheska,K., Pannetier,M.,
            Awad,M.A., Lesieur-Sebellin,M., Barcia,G., Amiel,J., Delanne,J.,
            Philippe,C., Faivre,L., Odent,S., Bertoli-Avella,A., Thauvin,C.,
            Sadikovic,B., Reversade,B., Maroofian,R., Govin,J., Tartaglia,M.
            and Vitobello,A.
  TITLE     Bi-allelic loss-of-function variants in TMEM147 cause moderate to
            profound intellectual disability with facial dysmorphism and
            pseudo-Pelger-Huet anomaly
  JOURNAL   Am J Hum Genet 109 (10), 1909-1922 (2022)
   PUBMED   36044892
  REMARK    GeneRIF: Bi-allelic loss-of-function variants in TMEM147 cause
            moderate to profound intellectual disability with facial
            dysmorphism and pseudo-Pelger-Huet anomaly.
REFERENCE   5  (residues 1 to 175)
  AUTHORS   Maimaris,G., Christodoulou,A., Santama,N. and Lederer,C.W.
  TITLE     Regulation of ER Composition and Extent, and Putative Action in
            Protein Networks by ER/NE Protein TMEM147
  JOURNAL   Int J Mol Sci 22 (19), 10231 (2021)
   PUBMED   34638576
  REMARK    GeneRIF: Regulation of ER Composition and Extent, and Putative
            Action in Protein Networks by ER/NE Protein TMEM147.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 175)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   7  (residues 1 to 175)
  AUTHORS   Rosemond,E., Rossi,M., McMillin,S.M., Scarselli,M., Donaldson,J.G.
            and Wess,J.
  TITLE     Regulation of M muscarinic receptor expression and function by
            transmembrane protein 147
  JOURNAL   Mol Pharmacol 79 (2), 251-261 (2011)
   PUBMED   21056967
REFERENCE   8  (residues 1 to 175)
  AUTHORS   Dettmer,U., Kuhn,P.H., Abou-Ajram,C., Lichtenthaler,S.F.,
            Kruger,M., Kremmer,E., Haass,C. and Haffner,C.
  TITLE     Transmembrane protein 147 (TMEM147) is a novel component of the
            Nicalin-NOMO protein complex
  JOURNAL   J Biol Chem 285 (34), 26174-26181 (2010)
   PUBMED   20538592
  REMARK    GeneRIF: TMEM147 is a novel core component of the Nicalin-NOMO
            complex, further emphasizing its similarity with gamma-secretase.
REFERENCE   9  (residues 1 to 175)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   10 (residues 1 to 175)
  AUTHORS   Lehner,B., Semple,J.I., Brown,S.E., Counsell,D., Campbell,R.D. and
            Sanderson,C.M.
  TITLE     Analysis of a high-throughput yeast two-hybrid system and its use
            to predict the function of intracellular proteins encoded within
            the human MHC class III region
  JOURNAL   Genomics 83 (1), 153-167 (2004)
   PUBMED   14667819
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM423809.1, BG697070.1, AW473288.1 and AW130399.1.
            
            Transcript Variant: This variant (2) lacks a splice site in the 5'
            coding region and initiates translation at a downstream, in-frame
            start codon, compared to variant 1. The encoded isoform (2) has a
            shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.226436.1,
                                           SRR1163657.26227.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.12"
     Protein         1..175
                     /product="BOS complex subunit TMEM147 isoform 2"
                     /note="seven transmembrane domain protein; protein NIFIE
                     14; BOS complex subunit TMEM147"
                     /calculated_mol_wt=19412
     Region          <1..106
                     /region_name="DUF2053"
                     /note="Predicted membrane protein (DUF2053); pfam09767"
                     /db_xref="CDD:462890"
     CDS             1..175
                     /gene="TMEM147"
                     /gene_synonym="NEDFLPH; NIFIE14"
                     /coded_by="NM_001242597.2:333..860"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56091.1"
                     /db_xref="GeneID:10430"
                     /db_xref="HGNC:HGNC:30414"
                     /db_xref="MIM:613585"
ORIGIN      
        1 mlflatffpt weggiydfig efmkasvdva dliglnlvms rnagkgeyki mvaalgwata
       61 elimsrcipl wvgargiefd wkyiqmsids nislvhyiva saqvwmitry dlyhtfrpav
      121 lllmflsvyk afvmetfvhl cslgswaall aravvtglla lstlalyvav vnvhs
//
LOCUS       NP_689504                377 aa            linear   PRI 20-NOV-2025
DEFINITION  mucin-7 precursor [Homo sapiens].
ACCESSION   NP_689504
VERSION     NP_689504.2
DBSOURCE    REFSEQ: accession NM_152291.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 377)
  AUTHORS   Zhang,J. and Li,Z.
  TITLE     Diagnostic accuracy of MUC7 expression for bladder cancer: A
            systematic review and meta-analysis
  JOURNAL   Medicine (Baltimore) 102 (35), e34828 (2023)
   PUBMED   37657056
  REMARK    GeneRIF: Diagnostic accuracy of MUC7 expression for bladder cancer:
            A systematic review and meta-analysis.
REFERENCE   2  (residues 1 to 377)
  AUTHORS   Ghosh,S., Ahearn,C.P., Isabella,C.R., Marando,V.M., Dodge,G.J.,
            Bartlett,H., McPherson,R.L., Dugan,A.E., Jain,S., Neznanova,L.,
            Tettelin,H., Putnik,R., Grimes,C.L., Ruhl,S., Kiessling,L.L. and
            Imperiali,B.
  TITLE     Human oral lectin ZG16B acts as a cell wall polysaccharide probe to
            decode host-microbe interactions with oral commensals
  JOURNAL   Proc Natl Acad Sci U S A 120 (22), e2216304120 (2023)
   PUBMED   37216558
REFERENCE   3  (residues 1 to 377)
  AUTHORS   Saad,E.A., Elsaid,A.M., Shoaib,R.M.S., Megahed,K.F. and
            Elsharawy,A.N.
  TITLE     MUC7 VNTR polymorphism and association with bronchial asthma in
            Egyptian children
  JOURNAL   Sci Rep 12 (1), 18910 (2022)
   PUBMED   36344553
  REMARK    GeneRIF: MUC7 VNTR polymorphism and association with bronchial
            asthma in Egyptian children.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 377)
  AUTHORS   Chahal,G., Quintana-Hayashi,M.P., Gaytan,M.O., Benktander,J.,
            Padra,M., King,S.J. and Linden,S.K.
  TITLE     Streptococcus oralis Employs Multiple Mechanisms of Salivary Mucin
            Binding That Differ Between Strains
  JOURNAL   Front Cell Infect Microbiol 12, 889711 (2022)
   PUBMED   35782137
  REMARK    GeneRIF: Streptococcus oralis Employs Multiple Mechanisms of
            Salivary Mucin Binding That Differ Between Strains.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 377)
  AUTHORS   Hertel,S., Hannig,M., Hannig,C. and Sterzenbach,T.
  TITLE     Mucins 5b and 7 and secretory IgA in the oral acquired pellicle of
            children with caries and caries-free children
  JOURNAL   Arch Oral Biol 134, 105314 (2022)
   PUBMED   34861462
  REMARK    GeneRIF: Mucins 5b and 7 and secretory IgA in the oral acquired
            pellicle of children with caries and caries-free children.
REFERENCE   6  (residues 1 to 377)
  AUTHORS   Bobek,L.A. and Situ,H.
  TITLE     MUC7 20-Mer: investigation of antimicrobial activity, secondary
            structure, and possible mechanism of antifungal action
  JOURNAL   Antimicrob Agents Chemother 47 (2), 643-652 (2003)
   PUBMED   12543672
  REMARK    GeneRIF: MUC7 is a salivary mucin with antimicrobial activity
            against bacteria and fungi.
REFERENCE   7  (residues 1 to 377)
  AUTHORS   Prakobphol,A., Thomsson,K.A., Hansson,G.C., Rosen,S.D.,
            Singer,M.S., Phillips,N.J., Medzihradszky,K.F., Burlingame,A.L.,
            Leffler,H. and Fisher,S.J.
  TITLE     Human low-molecular-weight salivary mucin expresses the sialyl
            lewisx determinant and has L-selectin ligand activity
  JOURNAL   Biochemistry 37 (14), 4916-4927 (1998)
   PUBMED   9538010
REFERENCE   8  (residues 1 to 377)
  AUTHORS   Troxler,R.F., Iontcheva,I., Oppenheim,F.G., Nunes,D.P. and
            Offner,G.D.
  TITLE     Molecular characterization of a major high molecular weight mucin
            from human sublingual gland
  JOURNAL   Glycobiology 7 (7), 965-973 (1997)
   PUBMED   9363439
REFERENCE   9  (residues 1 to 377)
  AUTHORS   Bobek,L.A., Liu,J., Sait,S.N., Shows,T.B., Bobek,Y.A. and
            Levine,M.J.
  TITLE     Structure and chromosomal localization of the human salivary mucin
            gene, MUC7
  JOURNAL   Genomics 31 (3), 277-282 (1996)
   PUBMED   8838308
REFERENCE   10 (residues 1 to 377)
  AUTHORS   Bobek,L.A., Tsai,H., Biesbrock,A.R. and Levine,M.J.
  TITLE     Molecular cloning, sequence, and specificity of expression of the
            gene encoding the low molecular weight human salivary mucin (MUC7)
  JOURNAL   J Biol Chem 268 (27), 20563-20569 (1993)
   PUBMED   7690757
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC108518.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 3, 2009 this sequence version replaced NP_689504.1.
            
            Summary: This gene encodes a small salivary mucin, which is thought
            to play a role in facilitating the clearance of bacteria in the
            oral cavity and to aid in mastication, speech, and swallowing. The
            central domain of this glycoprotein contains tandem repeats, each
            composed of 23 amino acids. This antimicrobial protein has
            antibacterial and antifungal activity. The most common allele
            contains 6 repeats, and some alleles may be associated with
            susceptibility to asthma. Alternatively spliced transcript variants
            with different 5' UTR, but encoding the same protein, have been
            found for this gene. [provided by RefSeq, Oct 2014].
            
            Transcript Variant: This variant (3) represents the shortest
            transcript and has a different 5' UTR compared to transcript
            variant 1. Transcript variants 1, 2 and 3 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025688.1, AK312855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA2142853
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000304887.6/
                                                  ENSP00000302021.5
            Protein has antimicrobial activity :: PMID: 12543672
            RefSeq Select criteria             :: based on expression, longest
                                                  protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..377
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q13.3"
     Protein         1..377
                     /product="mucin-7 precursor"
                     /note="mucin 7, salivary; mucin-7; MUC-7; apo-MG2;
                     salivary mucin-7; mucin MG2"
                     /calculated_mol_wt=36809
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2368
     mat_peptide     23..377
                     /product="mucin-7"
                     /calculated_mol_wt=36809
     mat_peptide     52..71
                     /product="MUC7 20-Mer"
                     /experiment="DESCRIPTION:antimicrobial peptide[PMID:
                     12543672]"
                     /calculated_mol_wt=2513
     Region          70..100
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            97
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            128
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Region          <141..358
                     /region_name="PRK12323"
                     /note="DNA polymerase III subunit gamma/tau; cl46901"
                     /db_xref="CDD:481241"
     Site            146
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Region          150..355
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            182
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) serine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            183
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) serine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            188
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc) threonine, by GALNT13.
                     /evidence=ECO:0000269|PubMed:12407114; propagated from
                     UniProtKB/Swiss-Prot (Q8TAX7.2)"
     CDS             1..377
                     /gene="MUC7"
                     /gene_synonym="MG2"
                     /coded_by="NM_152291.3:111..1244"
                     /db_xref="CCDS:CCDS3541.1"
                     /db_xref="GeneID:4589"
                     /db_xref="HGNC:HGNC:7518"
                     /db_xref="MIM:158375"
ORIGIN      
        1 mktlplfvci calsacfsfs egrerdhelr hrrhhhqspk shfelphypg llahqkpfir
       61 ksykclhkrc rpklppspnn ppkfpnphqp pkhpdknssv vnptlvattq ipsvtfpsas
      121 tkittlpnvt flpqnattis srenvntsss vatlapvnsp apqdttaapp tpsattpapp
      181 sssappetta apptpsattq appsssappe ttaapptppa ttpappsssa ppettaappt
      241 psattpapls ssappettav pptpsattld pssasappet taapptpsat tpappsspap
      301 qettaapitt pnsspttlap dtsetsaapt hqtttsvttq ttttkqptsa pgqnkisrfl
      361 lymknllnri iddmveq
//
LOCUS       NP_009148                212 aa            linear   PRI 20-NOV-2025
DEFINITION  programmed cell death protein 10 [Homo sapiens].
ACCESSION   NP_009148
VERSION     NP_009148.2
DBSOURCE    REFSEQ: accession NM_007217.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 212)
  AUTHORS   Li,Y., Liu,Y., Liu,K., Tao,T., Yang,L., Liu,R., Zhou,H., Liang,D.,
            Zhang,Y., Huang,D. and Sun,Y.
  TITLE     Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units
  JOURNAL   Ecotoxicol Environ Saf 277, 116269 (2024)
   PUBMED   38657460
  REMARK    GeneRIF: Study on the role of CCM3 gene and lead exposure induced
            neurotoxicity through neurovascular units.
REFERENCE   3  (residues 1 to 212)
  AUTHORS   da Fontoura Galvao,G., da Silva,E.V., Trefilio,L.M.,
            Alves-Leon,S.V., Fontes-Dantas,F.L. and de Souza,J.M.
  TITLE     Comprehensive CCM3 Mutational Analysis in Two Patients with
            Syndromic Cerebral Cavernous Malformation
  JOURNAL   Transl Stroke Res 15 (2), 411-421 (2024)
   PUBMED   36723700
  REMARK    GeneRIF: Comprehensive CCM3 Mutational Analysis in Two Patients
            with Syndromic Cerebral Cavernous Malformation.
REFERENCE   4  (residues 1 to 212)
  AUTHORS   Tang,L., Zhou,M., Xu,Y., Peng,B., Gao,Y. and Mo,Y.
  TITLE     Knockdown of CCM3 promotes angiogenesis through activation and
            nuclear translocation of YAP/TAZ
  JOURNAL   Biochem Biophys Res Commun 701, 149525 (2024)
   PUBMED   38320423
  REMARK    GeneRIF: Knockdown of CCM3 promotes angiogenesis through activation
            and nuclear translocation of YAP/TAZ.
REFERENCE   5  (residues 1 to 212)
  AUTHORS   Ni,W.J. and Leng,X.M.
  TITLE     Programmed cell death 10 can be used as a potential biomarker for
            ankylosing spondylitis diagnosis and treatment
  JOURNAL   Spinal Cord 62 (3), 99-103 (2024)
   PUBMED   38158408
  REMARK    GeneRIF: Programmed cell death 10 can be used as a potential
            biomarker for ankylosing spondylitis diagnosis and treatment.
REFERENCE   6  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Bilguvar,K., Shin,D.,
            O'Roak,B.J. and Gunel,M.
  TITLE     Mutations in apoptosis-related gene, PDCD10, cause cerebral
            cavernous malformation 3
  JOURNAL   Neurosurgery 57 (5), 1008-1013 (2005)
   PUBMED   16284570
  REMARK    GeneRIF: Mutations in apoptosis-related gene, PDCD10, cause
            cerebral cavernous malformation 3.
REFERENCE   7  (residues 1 to 212)
  AUTHORS   Guclu,B., Ozturk,A.K., Pricola,K.L., Seker,A., Ozek,M. and Gunel,M.
  TITLE     Cerebral venous malformations have distinct genetic origin from
            cerebral cavernous malformations
  JOURNAL   Stroke 36 (11), 2479-2480 (2005)
   PUBMED   16239636
  REMARK    GeneRIF: KRIT1, Malcavernin, and PDCD10 are differentially
            expressed in cerebral venous malformations and cerebral cavernous
            malformations
REFERENCE   8  (residues 1 to 212)
  AUTHORS   Bergametti,F., Denier,C., Labauge,P., Arnoult,M., Boetto,S.,
            Clanet,M., Coubes,P., Echenne,B., Ibrahim,R., Irthum,B.,
            Jacquet,G., Lonjon,M., Moreau,J.J., Neau,J.P., Parker,F.,
            Tremoulet,M. and Tournier-Lasserve,E.
  CONSRTM   Societe Francaise de Neurochirurgie
  TITLE     Mutations within the programmed cell death 10 gene cause cerebral
            cavernous malformations
  JOURNAL   Am J Hum Genet 76 (1), 42-51 (2005)
   PUBMED   15543491
  REMARK    GeneRIF: We report herein the identification of PDCD10 (programmed
            cell death 10) as the CCM3 gene.
REFERENCE   9  (residues 1 to 212)
  AUTHORS   Craig,H.D., Gunel,M., Cepeda,O., Johnson,E.W., Ptacek,L.,
            Steinberg,G.K., Ogilvy,C.S., Berg,M.J., Crawford,S.C., Scott,R.M.,
            Steichen-Gersdorf,E., Sabroe,R., Kennedy,C.T., Mettler,G.,
            Beis,M.J., Fryer,A., Awad,I.A. and Lifton,R.P.
  TITLE     Multilocus linkage identifies two new loci for a mendelian form of
            stroke, cerebral cavernous malformation, at 7p15-13 and 3q25.2-27
  JOURNAL   Hum Mol Genet 7 (12), 1851-1858 (1998)
   PUBMED   9811928
REFERENCE   10 (residues 1 to 212)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079822.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 10, 2002 this sequence version replaced NP_009148.1.
            
            Summary: This gene encodes an evolutionarily conserved protein
            associated with cell apoptosis. The protein interacts with the
            serine/threonine protein kinase MST4 to modulate the extracellular
            signal-regulated kinase (ERK) pathway. It also interacts with and
            is phosphoryated by serine/threonine kinase 25, and is thought to
            function in a signaling pathway essential for vascular developent.
            Mutations in this gene are one cause of cerebral cavernous
            malformations, which are vascular malformations that cause seizures
            and cerebral hemorrhages. Multiple alternatively spliced variants,
            encoding the same protein, have been identified. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript. Variants 1, 2, and 3 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC002506.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000392750.7/ ENSP00000376506.2
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q26.1"
     Protein         1..212
                     /product="programmed cell death protein 10"
                     /note="apoptosis-related protein 15; TF-1 cell
                     apoptosis-related protein 15; cerebral cavernous
                     malformations 3 protein"
                     /calculated_mol_wt=24571
     Region          14..161
                     /region_name="DUF1241"
                     /note="Protein of unknown function (DUF1241); pfam06840"
                     /db_xref="CDD:462018"
     Site            179
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9BUL8.1)"
     CDS             1..212
                     /gene="PDCD10"
                     /gene_synonym="CCM3; TFAR15"
                     /coded_by="NM_007217.4:485..1123"
                     /db_xref="CCDS:CCDS3202.1"
                     /db_xref="GeneID:11235"
                     /db_xref="HGNC:HGNC:8761"
                     /db_xref="MIM:609118"
ORIGIN      
        1 mrmtmeemkn eaettsmvsm plyavmypvf nelervnlsa aqtlraafik aekenpgltq
       61 diimkilekk svevnftesl lrmaaddvee ymierpepef qdlnekaral kqilskipde
      121 indrvrflqt ikdiasaike lldtvnnvfk kyqyqnrral ehqkkefvky sksfsdtlkt
      181 yfkdgkainv fvsanrlihq tnlilqtfkt va
//
LOCUS       NP_001280018             823 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 3 [Homo sapiens].
ACCESSION   NP_001280018 XP_005257949
VERSION     NP_001280018.1
DBSOURCE    REFSEQ: accession NM_001293089.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 823)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 823)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 823)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 823)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 823)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 823)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 823)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 823)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 823)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 823)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY023336.1, U00001.1,
            AC002558.2 and AA927469.1.
            
            On May 28, 2014 this sequence version replaced XP_005257949.1.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (3) uses two alternate in-frame
            splice sites in the central coding region, compared to variant 1,
            resulting in an isoform (3) that is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038195.999443.1,
                                           SRR1803614.245793.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..823
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..823
                     /product="cell division cycle protein 27 homolog isoform
                     3"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=91608
     Region          6..35
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          17..92
                     /region_name="ANAPC3"
                     /note="Anaphase-promoting complex, cyclosome, subunit 3;
                     pfam12895"
                     /db_xref="CDD:463743"
     Region          38..65
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          67..99
                     /region_name="TPR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          115..145
                     /region_name="TPR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Region          287..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            291
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            313
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            366
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            379
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            386
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            430
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            435
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:14657031; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:14657031,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          464..494
                     /region_name="TPR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          498..605
                     /region_name="NrfG"
                     /note="Cytochrome c-type biogenesis protein CcmH/NrfG
                     [Energy production and conversion, Posttranslational
                     modification, protein turnover, chaperones]; COG4235"
                     /db_xref="CDD:443378"
     Region          498..527
                     /region_name="TPR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          500..526
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          532..562
                     /region_name="TPR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          560..>730
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          566..597
                     /region_name="TPR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          566..594
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(567,570..571,574..575,577,601,604..605,608..609,
                     611..612,635,638..639,642..643,646)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          599..629
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          600..630
                     /region_name="TPR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          634..666
                     /region_name="TPR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          634..662
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <664..803
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          668..695
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          669..701
                     /region_name="TPR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          702..730
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          703..733
                     /region_name="TPR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          736..767
                     /region_name="TPR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Region          736..764
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          780..823
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P30260.2)"
     Site            820
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22139841; propagated from
                     UniProtKB/Swiss-Prot (P30260.2)"
     CDS             1..823
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001293089.3:124..2595"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS74090.1"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mtvlqepvqa aiwqalnhya yrdavflaer lyaevhseea lfllatcyyr sgkaykayrl
       61 lkghscttpq ckyllakccv dlsklaegeq ilsggvfnkq kshddivtef gdsacftlsl
      121 lghvycktdr lakgsecyqk slslnpflws pfeslceige kpdpdqtfkf tslqnfsncl
      181 pnscttqvpn hslshrqpet vltetpqdti elnrlnless nskyslntds svsyidsavi
      241 spdtvplgtg tsilskqvqn kpktgrsllg gpaalspltp sfgilpletp spgdgsylqn
      301 ytntppvidv pstgapskks varigqtgtk svfsqsgnsr evtpilaqtq ssgpqtsttp
      361 qvlsptitsp pnalprrssr lftsdssttk enskklkmkf ppkipnrktk sktnkggitq
      421 pnindsleit kldssiiseg kistitpqiq afnlqkaaag lmsllremgk gylalcsync
      481 keainilshl pshhyntgwv lcqigrayfe lseymqaeri fsevrrieny rvegmeiyst
      541 tlwhlqkdva lsvlskdltd mdknspeawc aagncfslqr ehdiaikffq raiqvdpnya
      601 yaytllghef vlteeldkal acfrnairvn prhynawygl gmiyykqekf slaemhfqka
      661 ldinpqssvl lchigvvqha lkksekaldt lnkaividpk nplckfhras vlfanekyks
      721 alqeleelkq ivpkeslvyf ligkvykklg qthlalmnfs wamdldpkga nnqikeaidk
      781 rylpddeepi tqeeqimgtd esqessmtda ddtqlhaaes def
//
LOCUS       NP_055946                677 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 43 [Homo sapiens].
ACCESSION   NP_055946
VERSION     NP_055946.1
DBSOURCE    REFSEQ: accession NM_015131.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 677)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 677)
  AUTHORS   Yang,X., Luo,T., Liu,Z., Liu,J. and Yang,Z.
  TITLE     WD repeat domain 43 as a new predictive indicator and its
            connection with tumor immune cell infiltration in pan-cancer
  JOURNAL   Medicine (Baltimore) 103 (31), e39153 (2024)
   PUBMED   39093744
  REMARK    GeneRIF: WD repeat domain 43 as a new predictive indicator and its
            connection with tumor immune cell infiltration in pan-cancer.
REFERENCE   3  (residues 1 to 677)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 677)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   5  (residues 1 to 677)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 677)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   7  (residues 1 to 677)
  AUTHORS   Prieto,J.L. and McStay,B.
  TITLE     Recruitment of factors linking transcription and processing of
            pre-rRNA to NOR chromatin is UBF-dependent and occurs independent
            of transcription in human cells
  JOURNAL   Genes Dev 21 (16), 2041-2054 (2007)
   PUBMED   17699751
REFERENCE   8  (residues 1 to 677)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   9  (residues 1 to 677)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   10 (residues 1 to 677)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA654485.1, D26488.1, AC097720.5 and AW593733.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.166644.1, D26488.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000407426.8/ ENSP00000384302.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..677
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.2"
     Protein         1..677
                     /product="WD repeat-containing protein 43"
                     /note="UTP5, small subunit (SSU) processome component,
                     homolog; U3 small nucleolar RNA-associated protein 5
                     homolog"
                     /calculated_mol_wt=74760
     Region          11..51
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          19..57
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <20..300
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          57..119
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          63..124
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          124..163
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          129..165
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          166..205
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          172..205
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          207..259
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          211..262
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          267..309
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Region          271..320
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Site            399
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Region          414..445
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Site            437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Region          473..577
                     /region_name="Utp12"
                     /note="Dip2/Utp12 Family; pfam04003"
                     /db_xref="CDD:461125"
     Region          582..677
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15061.3)"
     Site            590
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Site            656
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     Site            658
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q15061.3)"
     CDS             1..677
                     /gene="WDR43"
                     /gene_synonym="NET12; UTP5"
                     /coded_by="NM_015131.3:33..2066"
                     /db_xref="CCDS:CCDS46251.1"
                     /db_xref="GeneID:23160"
                     /db_xref="HGNC:HGNC:28945"
                     /db_xref="MIM:616195"
ORIGIN      
        1 maaggggscd plapagvpca fsphsqayfa lastdghlrv wetannrlhq eyvpsahlsg
       61 tctclawapa rlqakespqr kkrkseavgm snqtdllalg tavgsillys tvkgelhskl
      121 isgghdnrvn ciqwhqdsgc lyscsddkhi vewnvqtckv kckwkgdnss vsslcispdg
      181 kmllsagrti klwvletkev yrhftghatp vsslmfttir ppnesqpfdg itglyflsga
      241 vhdrllnvwq vrsenkeksa vmsftvtdep vyidltlsen keepvklavv crdgqvhlfe
      301 hilngyckkp ltsnctiqia tpgkgkkstp kpipilaagf csdkmslllv ygswfqptie
      361 rvalnsreph mclvrdisnc wapkvetait kvrtpvmnse akvlvpgipg hhaaikpapp
      421 qteqveskrk sggnevsiee rlgamdidth kkgkedlqtn sfpvlltqgl esndfemlnk
      481 vlqtrnvnli kktvlrmplh tiipllqelt krlqghpnsa vlmvqwlkcv ltvhasylst
      541 lpdlvpqlgt lyqlmesrvk tfqklshlhg klillitqvt asektkgats pgqkaklvye
      601 eesseeesdd eiadkdsedn wdedeeeses ekdedveeed edaegkdeen gedrdtasek
      661 elngdsdldp eneseee
//
LOCUS       NP_001264006             224 aa            linear   PRI 20-NOV-2025
DEFINITION  homer protein homolog 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001264006
VERSION     NP_001264006.1
DBSOURCE    REFSEQ: accession NM_001277077.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 224)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 224)
  AUTHORS   Singer,A., Ramos,A. and Keating,A.E.
  TITLE     Elaboration of the Homer1 recognition landscape reveals incomplete
            divergence of paralogous EVH1 domains
  JOURNAL   Protein Sci 33 (8), e5094 (2024)
   PUBMED   38989636
  REMARK    GeneRIF: Elaboration of the Homer1 recognition landscape reveals
            incomplete divergence of paralogous EVH1 domains.
REFERENCE   3  (residues 1 to 224)
  AUTHORS   Shu,S., Xu,Z., Lu,H., Li,Z. and Zhang,Y.
  TITLE     CircHOMER1 aggravates oxidative stress, inflammation and
            extracellular matrix deposition in high glucose-induced human
            mesangial cells
  JOURNAL   Nephrology (Carlton) 27 (12), 983-993 (2022)
   PUBMED   36181383
  REMARK    GeneRIF: CircHOMER1 aggravates oxidative stress, inflammation and
            extracellular matrix deposition in high glucose-induced human
            mesangial cells.
REFERENCE   4  (residues 1 to 224)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 224)
  AUTHORS   Lin,R., Learman,L.N., Bangash,M.A., Melnikova,T., Leyder,E.,
            Reddy,S.C., Naidoo,N., Park,J.M., Savonenko,A. and Worley,P.F.
  TITLE     Homer1a regulates Shank3 expression and underlies behavioral
            vulnerability to stress in a model of Phelan-McDermid syndrome
  JOURNAL   Cell Rep 37 (7), 110014 (2021)
   PUBMED   34788607
  REMARK    GeneRIF: Homer1a regulates Shank3 expression and underlies
            behavioral vulnerability to stress in a model of Phelan-McDermid
            syndrome.
REFERENCE   6  (residues 1 to 224)
  AUTHORS   Roche,K.W., Tu,J.C., Petralia,R.S., Xiao,B., Wenthold,R.J. and
            Worley,P.F.
  TITLE     Homer 1b regulates the trafficking of group I metabotropic
            glutamate receptors
  JOURNAL   J Biol Chem 274 (36), 25953-25957 (1999)
   PUBMED   10464340
REFERENCE   7  (residues 1 to 224)
  AUTHORS   Tu,J.C., Xiao,B., Naisbitt,S., Yuan,J.P., Petralia,R.S.,
            Brakeman,P., Doan,A., Aakalu,V.K., Lanahan,A.A., Sheng,M. and
            Worley,P.F.
  TITLE     Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
            postsynaptic density proteins
  JOURNAL   Neuron 23 (3), 583-592 (1999)
   PUBMED   10433269
REFERENCE   8  (residues 1 to 224)
  AUTHORS   Tu,J.C., Xiao,B., Yuan,J.P., Lanahan,A.A., Leoffert,K., Li,M.,
            Linden,D.J. and Worley,P.F.
  TITLE     Homer binds a novel proline-rich motif and links group 1
            metabotropic glutamate receptors with IP3 receptors
  JOURNAL   Neuron 21 (4), 717-726 (1998)
   PUBMED   9808459
REFERENCE   9  (residues 1 to 224)
  AUTHORS   Xiao,B., Tu,J.C., Petralia,R.S., Yuan,J.P., Doan,A., Breder,C.D.,
            Ruggiero,A., Lanahan,A.A., Wenthold,R.J. and Worley,P.F.
  TITLE     Homer regulates the association of group 1 metabotropic glutamate
            receptors with multivalent complexes of homer-related, synaptic
            proteins
  JOURNAL   Neuron 21 (4), 707-716 (1998)
   PUBMED   9808458
REFERENCE   10 (residues 1 to 224)
  AUTHORS   Brakeman,P.R., Lanahan,A.A., O'Brien,R., Roche,K., Barnes,C.A.,
            Huganir,R.L. and Worley,P.F.
  TITLE     Homer: a protein that selectively binds metabotropic glutamate
            receptors
  JOURNAL   Nature 386 (6622), 284-288 (1997)
   PUBMED   9069287
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC093270.3, AY189939.1 and AC020898.6.
            
            Summary: This gene encodes a member of the homer family of
            dendritic proteins. Members of this family regulate group 1
            metabotrophic glutamate receptor function. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2, also known as HOMER1E) lacks
            three consecutive coding exons compared to variant 1. The missing
            segment is in-frame, so the resulting isoform (2) has the same N-
            and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154665
                              [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..224
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q14.1"
     Protein         1..224
                     /product="homer protein homolog 1 isoform 2"
                     /note="homer, neuronal immediate early gene, 1; homer
                     protein homolog 1; homer-1; homer homolog 1; homer
                     scaffolding protein 1"
                     /calculated_mol_wt=25712
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylglycine.
                     /evidence=ECO:0000269|PubMed:25489052; propagated from
                     UniProtKB/Swiss-Prot (Q86YM7.2)"
     Region          3..101
                     /region_name="EVH1_Homer_Vesl"
                     /note="Homer/Vesl family proteins EVH1 domain; cd01206"
                     /db_xref="CDD:269917"
     Site            order(24,70,74,89)
                     /site_type="other"
                     /note="proline-rich peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269917"
     Region          137..>222
                     /region_name="PRK12704"
                     /note="phosphodiesterase; Provisional"
                     /db_xref="CDD:237177"
     CDS             1..224
                     /gene="HOMER1"
                     /gene_synonym="HOMER; HOMER1A; HOMER1B; HOMER1C; SYN47;
                     Ves-1"
                     /coded_by="NM_001277077.1:1063..1737"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS64188.1"
                     /db_xref="GeneID:9456"
                     /db_xref="HGNC:HGNC:17512"
                     /db_xref="MIM:604798"
ORIGIN      
        1 mgeqpifstr ahvfqidpnt kknwvptskh avtvsyfyds trnvyriisl dgskaiinst
       61 itpnmtftkt sqkfgqwads rantvyglgf ssehhlskvt elecvssqan avhthkteln
      121 qtiqeleetl klkeeeierl kqeidnarel qeqrdsltqk lqeveirnkd legqlsdleq
      181 rleksqneqe afrnnlktll eildgkifel telrdnlakl lecs
//
LOCUS       NP_001166902            1543 aa            linear   PRI 20-NOV-2025
DEFINITION  obscurin-like protein 1 isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001166902
VERSION     NP_001166902.1
DBSOURCE    REFSEQ: accession NM_001173431.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1543)
  AUTHORS   Tuysuz,B., Alp Unkar,Z., Turan,H., Gezdirici,A., Uludag Alkaya,D.,
            Kasap,B., Yesil,G., Vural,M. and Ercan,O.
  TITLE     Natural history of facial and skeletal features from neonatal
            period to adulthood in a 3M syndrome cohort with biallelic CUL7 or
            OBSL1 variants
  JOURNAL   Eur J Med Genet 64 (12), 104346 (2021)
   PUBMED   34597859
  REMARK    GeneRIF: Natural history of facial and skeletal features from
            neonatal period to adulthood in a 3M syndrome cohort with biallelic
            CUL7 or OBSL1 variants.
REFERENCE   2  (residues 1 to 1543)
  AUTHORS   Isik,E., Arican,D., Atik,T., Ooi,J.E., Darcan,S., Ozen,S., Simsek
            Kiper,P.O., Utine,E., Cogulu,O. and Ozkinay,F.
  TITLE     A rare cause of syndromic short stature: 3M syndrome in three
            families
  JOURNAL   Am J Med Genet A 185 (2), 461-468 (2021)
   PUBMED   33258289
  REMARK    GeneRIF: A rare cause of syndromic short stature: 3M syndrome in
            three families.
REFERENCE   3  (residues 1 to 1543)
  AUTHORS   Jacob,P. and Girisha,K.M.
  TITLE     Three M syndrome 2 in two Indian patients
  JOURNAL   Am J Med Genet A 185 (2), 614-616 (2021)
   PUBMED   33135300
  REMARK    GeneRIF: Three M syndrome 2 in two Indian patients.
REFERENCE   4  (residues 1 to 1543)
  AUTHORS   Wang,P., Yan,F., Li,Z., Yu,Y., Parnell,S.E. and Xiong,Y.
  TITLE     Impaired plasma membrane localization of ubiquitin ligase complex
            underlies 3-M syndrome development
  JOURNAL   J Clin Invest 129 (10), 4393-4407 (2019)
   PUBMED   31343991
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1543)
  AUTHORS   Simsek-Kiper,P.O., Taskiran,E., Kosukcu,C., Arslan,U.E.,
            Cormier-Daire,V., Gonc,N., Ozon,A., Alikasifoglu,A., Kandemir,N.,
            Utine,G.E., Alanay,Y., Alikasifoglu,M. and Boduroglu,K.
  TITLE     Further expanding the mutational spectrum and investigation of
            genotype-phenotype correlation in 3M syndrome
  JOURNAL   Am J Med Genet A 179 (7), 1157-1172 (2019)
   PUBMED   30980518
  REMARK    GeneRIF: The mutational spectrum of CUL7, OBSL1, and investigation
            of genotype-phenotype correlation in 3M syndrome has been reported.
REFERENCE   6  (residues 1 to 1543)
  AUTHORS   Hanson,D., Murray,P.G., Sud,A., Temtamy,S.A., Aglan,M.,
            Superti-Furga,A., Holder,S.E., Urquhart,J., Hilton,E., Manson,F.D.,
            Scambler,P., Black,G.C. and Clayton,P.E.
  TITLE     The primordial growth disorder 3-M syndrome connects ubiquitination
            to the cytoskeletal adaptor OBSL1
  JOURNAL   Am J Hum Genet 84 (6), 801-806 (2009)
   PUBMED   19481195
  REMARK    GeneRIF: Loss of OBSL1 leads to downregulation of CUL7 and results
            in primordial growth disorder 3-M syndrome.
REFERENCE   7  (residues 1 to 1543)
  AUTHORS   Fukuzawa,A., Lange,S., Holt,M., Vihola,A., Carmignac,V.,
            Ferreiro,A., Udd,B. and Gautel,M.
  TITLE     Interactions with titin and myomesin target obscurin and
            obscurin-like 1 to the M-band: implications for hereditary
            myopathies
  JOURNAL   J Cell Sci 121 (11), 1841-1851 (2008)
   PUBMED   18477606
  REMARK    GeneRIF: N-terminal Ig-domains of Obsl1 and Obscurin (Obsc) bind to
            titin-M10 and myomesin. Titin mutations, linked to limb-girdle
            muscular dystrophy 2J (LGMD2J) or Salih myopathy, weaken or
            abrogate titin-Obsc and titin-Obsl1 binding.
REFERENCE   8  (residues 1 to 1543)
  AUTHORS   Geisler,S.B., Robinson,D., Hauringa,M., Raeker,M.O., Borisov,A.B.,
            Westfall,M.V. and Russell,M.W.
  TITLE     Obscurin-like 1, OBSL1, is a novel cytoskeletal protein related to
            obscurin
  JOURNAL   Genomics 89 (4), 521-531 (2007)
   PUBMED   17289344
  REMARK    GeneRIF: report the cloning and characterization of OBSL1; OBSL1 is
            located on human chromosome 2q35 within 100 kb of SPEG, another
            gene related to obscurin
REFERENCE   9  (residues 1 to 1543)
  AUTHORS   Lanfranchi,G., Muraro,T., Caldara,F., Pacchioni,B., Pallavicini,A.,
            Pandolfo,D., Toppo,S., Trevisan,S., Scarso,S. and Valle,G.
  TITLE     Identification of 4370 expressed sequence tags from a
            3'-end-specific cDNA library of human skeletal muscle by DNA
            sequencing and filter hybridization
  JOURNAL   Genome Res 6 (1), 35-42 (1996)
   PUBMED   8681137
REFERENCE   10 (residues 1 to 1543)
  AUTHORS   Akilapa,R., Irving,M. and Holder-Espinasse,M.
  TITLE     3-M Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB475523.1, CK904385.1,
            EF063637.1, AK023854.1 and AC009955.4.
            
            Summary: Cytoskeletal adaptor proteins function in linking the
            internal cytoskeleton of cells to the cell membrane. This gene
            encodes a cytoskeletal adaptor protein, which is a member of the
            Unc-89/obscurin family. The protein contains multiple N- and
            C-terminal immunoglobulin (Ig)-like domains and a central
            fibronectin type 3 domain. Mutations in this gene cause 3M syndrome
            type 2. Alternatively spliced transcript variants encoding
            different isoforms have been found in this gene. [provided by
            RefSeq, Mar 2010].
            
            Transcript Variant: This variant (2) lacks multiple 3' exons but
            has an alternate 3' sequence, as compared to variant 1. The
            resulting isoform (2, also known as isoform C) is shorter and has a
            different C-terminus, as compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1543
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q35"
     Protein         1..1543
                     /product="obscurin-like protein 1 isoform 2 precursor"
                     /EC_number="2.7.11.18"
                     /note="obscurin-like protein 1; obscurin like 1"
                     /calculated_mol_wt=165493
     sig_peptide     1..29
                     /calculated_mol_wt=3048
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O75147.4)"
     Region          12..88
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          17..19
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          29..33
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     mat_peptide     30..1543
                     /product="obscurin-like protein 1 isoform 2"
                     /calculated_mol_wt=165493
     Region          42..46
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          67..71
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          81..86
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          85..94
                     /region_name="Interaction with TTN"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          106..127
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O75147.4)"
     Region          134..226
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          145..149
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          158..162
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          182..196
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          206..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          219..222
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          257..336
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          263..267
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          276..280
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          302..306
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          316..321
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          329..332
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          342..426
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          358..362
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          371..374
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          395..399
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          409..414
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          423..426
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          518..602
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(518,584,599)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          736..801
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          746..750
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          771..775
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          785..790
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          794..797
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          827..892
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          837..841
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          862..866
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          876..881
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          885..888
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          918..983
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          928..932
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          953..957
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          967..972
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          976..979
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1009..1074
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1019..1023
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1044..1048
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1058..1063
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1067..1070
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1097..1164
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1099..1103
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1111..1115
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1136..1140
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1150..1155
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1159..1162
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1178..1265
                     /region_name="Ig_Semaphorin_C"
                     /note="Immunoglobulin (Ig)-like domain at the C-terminus
                     of semaphorins; cd04979"
                     /db_xref="CDD:409368"
     Region          1178..1184
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409368"
     Region          1188..1196
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409368"
     Site            order(1190,1233)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409368"
     Region          1202..1208
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409368"
     Region          1210..1213
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409368"
     Region          1218..1222
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409368"
     Region          1228..1235
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409368"
     Region          1241..1250
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409368"
     Region          1252..1265
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409368"
     Region          1273..1354
                     /region_name="IgI_C2_MyBP-C-like"
                     /note="Domain C2 of human cardiac Myosin Binding Protein C
                     and similar domains; a member of the I-set of IgSF
                     domains; cd20967"
                     /db_xref="CDD:409559"
     Region          1273..1275
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409559"
     Region          1278..1282
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409559"
     Region          1286..1292
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409559"
     Region          1299..1304
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409559"
     Region          1307..1310
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409559"
     Region          1315..1320
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409559"
     Region          1323..1328
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409559"
     Region          1337..1343
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409559"
     Region          1346..1354
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409559"
     Region          1361..1444
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1377..1381
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1389..1393
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1414..1418
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1428..1433
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1437..1440
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          1451..1522
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          1466..1470
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          1480..1484
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          1505..1509
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          1519..1524
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          1528..1531
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..1543
                     /gene="OBSL1"
                     /coded_by="NM_001173431.2:308..4939"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS63134.1"
                     /db_xref="GeneID:23363"
                     /db_xref="HGNC:HGNC:29092"
                     /db_xref="MIM:610991"
ORIGIN      
        1 mkassgdqgs ppcflrfprp vrvvsgaeae lkcvvlgepp pvvvwekggq qlaaserlsf
       61 padgaehgll ltaalptdag vyvcrarnaa geayaaaavt vleppasdpe lqpaerplps
      121 pgsgegapvf ltgprsqwvl rgaevvltcr agglpeptly wekdgmalde vwdsshfalq
      181 pgraedgpga slalrilaar lpdsgvyvch arnahghaqa gallqvhqpp esppadpdea
      241 papvveplkc apktfwvneg khakfrcyvm gkpepeiewh wegrpllpdr rrlmyrdrdg
      301 gfvlkvlycq akdrglyvca arnsagqtls avqlhvkepr lrftrplqdv egrehgiavl
      361 eckvpnsrip tawfredqrl lpcrkyeqie egtvrrliih rlkadddgiy lcemrgrvrt
      421 vanvtvkgpi lkrlprkldv legenavllv etleagvegr wsrdgeelpv icqsssghmh
      481 alvlpgvtre dagevtfslg nsrtttllrv kcvkhsppgp pilaemfkgh kntvlltwkp
      541 pepapetpfi yrlerqevgs edwiqcfsie kagavevpgd cvpsegdyrf rictvsghgr
      601 sphvvfhgsa hlvptarlva gledvqvydg edavfsldls tiiqgtwfln geelksnepe
      661 gqvepgalry rieqkglqhr lilhavkhqd sgalvgfscp gvqdsaalti qespvhilsp
      721 qdrvsltftt servvltcel srvdfpatwy kdgqkveese llvvkmdgrk hrlilpeakv
      781 qdsgefecrt egvsaffgvt vqdppvhivd prehvfvhai tsecvmlace vdredapvrw
      841 ykdgqevees dfvvlenegp hrrlvlpatq psdggefqcv agdecayftv titdvsswiv
      901 ypsgkvyvaa vrlervvltc elcrpwaevr wtkdgeevve spalllqked tvrrlvlpav
      961 qledsgeylc eiddesasft vtvteppvri iyprdevtli avtlecvvlm celsredapv
     1021 rwykdgleve esealvlerd gprcrlvlpa aqpedggefv cdagddsaff tvtvtapper
     1081 ivhpaarsld lhfgapgrve lrcevapags qvrwykdgle veasdalqlg aegptrtltl
     1141 phaqpedage yvcetrheai tfnvilaepp vqflalettp splcvapgep vvlscelsra
     1201 gapvvwshng rpvqegegle lhaegprrvl ciqaagpaha glytcqsgaa pgapslsftv
     1261 qvaeppvrvv apeaaqtrvr stpggdlelv vhlsgpggpv rwykdgerla sqgrvqleqa
     1321 garqvlrvqg arsgdageyl cdapqdsrif lvsveepllv klvseltplt vhegddatfr
     1381 cevsppdadv twlrngavvt pgpqvemaqn gssriltlrg cqlgdagtvt lragstatsa
     1441 rlhvretell flrrlqdvra eegqdvclev etgrvgaaga vrwvrggqpl phdsrlsmaq
     1501 dghihrlfih gviladqgty gceshhdrtl arlsvrrecp vls
//
LOCUS       NP_060957                235 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 176A [Homo sapiens].
ACCESSION   NP_060957
VERSION     NP_060957.2
DBSOURCE    REFSEQ: accession NM_018487.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 235)
  AUTHORS   Li,H., Yang,W., Zhang,M., He,T., Zhou,F., G Herman,J., Hu,L. and
            Guo,M.
  TITLE     Methylation of TMEM176A, a key ERK signaling regulator, is a novel
            synthetic lethality marker of ATM inhibitors in human lung cancer
  JOURNAL   Epigenomics 13 (17), 1403-1419 (2021)
   PUBMED   34558311
  REMARK    GeneRIF: Methylation of TMEM176A, a key ERK signaling regulator, is
            a novel synthetic lethality marker of ATM inhibitors in human lung
            cancer.
REFERENCE   2  (residues 1 to 235)
  AUTHORS   Guo,Y., Cao,F., Hu,S., Liu,S., Sun,H., Li,A. and Li,F.
  TITLE     TMEM176A acts as a tumor suppressor gene in pancreatic cancer by
            inhibiting ERK signaling
  JOURNAL   Discov Med 30 (161), 145-153 (2020)
   PUBMED   33593482
  REMARK    GeneRIF: TMEM176A acts as a tumor suppressor gene in pancreatic
            cancer by inhibiting ERK signaling.
REFERENCE   3  (residues 1 to 235)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 235)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 235)
  AUTHORS   Picotto,G., Morse,L.R., Nguyen,N., Saltzman,J. and Battaglino,R.
  TITLE     TMEM176A and TMEM176B Are Candidate Regulators of Inhibition of
            Dendritic Cell Maturation and Function after Chronic Spinal Cord
            Injury
  JOURNAL   J Neurotrauma 37 (3), 528-533 (2020)
   PUBMED   31354034
  REMARK    GeneRIF: TMEM176A and TMEM176B Are Candidate Regulators of
            Inhibition of Dendritic Cell Maturation and Function after Chronic
            Spinal Cord Injury.
REFERENCE   6  (residues 1 to 235)
  AUTHORS   Berndt,S.I., Gustafsson,S., Magi,R., Ganna,A., Wheeler,E.,
            Feitosa,M.F., Justice,A.E., Monda,K.L., Croteau-Chonka,D.C.,
            Day,F.R., Esko,T., Fall,T., Ferreira,T., Gentilini,D.,
            Jackson,A.U., Luan,J., Randall,J.C., Vedantam,S., Willer,C.J.,
            Winkler,T.W., Wood,A.R., Workalemahu,T., Hu,Y.J., Lee,S.H.,
            Liang,L., Lin,D.Y., Min,J.L., Neale,B.M., Thorleifsson,G., Yang,J.,
            Albrecht,E., Amin,N., Bragg-Gresham,J.L., Cadby,G., den Heijer,M.,
            Eklund,N., Fischer,K., Goel,A., Hottenga,J.J., Huffman,J.E.,
            Jarick,I., Johansson,A., Johnson,T., Kanoni,S., Kleber,M.E.,
            Konig,I.R., Kristiansson,K., Kutalik,Z., Lamina,C., Lecoeur,C.,
            Li,G., Mangino,M., McArdle,W.L., Medina-Gomez,C.,
            Muller-Nurasyid,M., Ngwa,J.S., Nolte,I.M., Paternoster,L.,
            Pechlivanis,S., Perola,M., Peters,M.J., Preuss,M., Rose,L.M.,
            Shi,J., Shungin,D., Smith,A.V., Strawbridge,R.J., Surakka,I.,
            Teumer,A., Trip,M.D., Tyrer,J., Van Vliet-Ostaptchouk,J.V.,
            Vandenput,L., Waite,L.L., Zhao,J.H., Absher,D., Asselbergs,F.W.,
            Atalay,M., Attwood,A.P., Balmforth,A.J., Basart,H., Beilby,J.,
            Bonnycastle,L.L., Brambilla,P., Bruinenberg,M., Campbell,H.,
            Chasman,D.I., Chines,P.S., Collins,F.S., Connell,J.M.,
            Cookson,W.O., de Faire,U., de Vegt,F., Dei,M., Dimitriou,M.,
            Edkins,S., Estrada,K., Evans,D.M., Farrall,M., Ferrario,M.M.,
            Ferrieres,J., Franke,L., Frau,F., Gejman,P.V., Grallert,H.,
            Gronberg,H., Gudnason,V., Hall,A.S., Hall,P., Hartikainen,A.L.,
            Hayward,C., Heard-Costa,N.L., Heath,A.C., Hebebrand,J., Homuth,G.,
            Hu,F.B., Hunt,S.E., Hypponen,E., Iribarren,C., Jacobs,K.B.,
            Jansson,J.O., Jula,A., Kahonen,M., Kathiresan,S., Kee,F.,
            Khaw,K.T., Kivimaki,M., Koenig,W., Kraja,A.T., Kumari,M.,
            Kuulasmaa,K., Kuusisto,J., Laitinen,J.H., Lakka,T.A.,
            Langenberg,C., Launer,L.J., Lind,L., Lindstrom,J., Liu,J.,
            Liuzzi,A., Lokki,M.L., Lorentzon,M., Madden,P.A., Magnusson,P.K.,
            Manunta,P., Marek,D., Marz,W., Mateo Leach,I., McKnight,B.,
            Medland,S.E., Mihailov,E., Milani,L., Montgomery,G.W., Mooser,V.,
            Muhleisen,T.W., Munroe,P.B., Musk,A.W., Narisu,N., Navis,G.,
            Nicholson,G., Nohr,E.A., Ong,K.K., Oostra,B.A., Palmer,C.N.,
            Palotie,A., Peden,J.F., Pedersen,N., Peters,A., Polasek,O.,
            Pouta,A., Pramstaller,P.P., Prokopenko,I., Putter,C.,
            Radhakrishnan,A., Raitakari,O., Rendon,A., Rivadeneira,F.,
            Rudan,I., Saaristo,T.E., Sambrook,J.G., Sanders,A.R., Sanna,S.,
            Saramies,J., Schipf,S., Schreiber,S., Schunkert,H., Shin,S.Y.,
            Signorini,S., Sinisalo,J., Skrobek,B., Soranzo,N., Stancakova,A.,
            Stark,K., Stephens,J.C., Stirrups,K., Stolk,R.P., Stumvoll,M.,
            Swift,A.J., Theodoraki,E.V., Thorand,B., Tregouet,D.A., Tremoli,E.,
            Van der Klauw,M.M., van Meurs,J.B., Vermeulen,S.H., Viikari,J.,
            Virtamo,J., Vitart,V., Waeber,G., Wang,Z., Widen,E., Wild,S.H.,
            Willemsen,G., Winkelmann,B.R., Witteman,J.C., Wolffenbuttel,B.H.,
            Wong,A., Wright,A.F., Zillikens,M.C., Amouyel,P., Boehm,B.O.,
            Boerwinkle,E., Boomsma,D.I., Caulfield,M.J., Chanock,S.J.,
            Cupples,L.A., Cusi,D., Dedoussis,G.V., Erdmann,J., Eriksson,J.G.,
            Franks,P.W., Froguel,P., Gieger,C., Gyllensten,U., Hamsten,A.,
            Harris,T.B., Hengstenberg,C., Hicks,A.A., Hingorani,A., Hinney,A.,
            Hofman,A., Hovingh,K.G., Hveem,K., Illig,T., Jarvelin,M.R.,
            Jockel,K.H., Keinanen-Kiukaanniemi,S.M., Kiemeney,L.A., Kuh,D.,
            Laakso,M., Lehtimaki,T., Levinson,D.F., Martin,N.G., Metspalu,A.,
            Morris,A.D., Nieminen,M.S., Njolstad,I., Ohlsson,C.,
            Oldehinkel,A.J., Ouwehand,W.H., Palmer,L.J., Penninx,B., Power,C.,
            Province,M.A., Psaty,B.M., Qi,L., Rauramaa,R., Ridker,P.M.,
            Ripatti,S., Salomaa,V., Samani,N.J., Snieder,H., Sorensen,T.I.,
            Spector,T.D., Stefansson,K., Tonjes,A., Tuomilehto,J.,
            Uitterlinden,A.G., Uusitupa,M., van der Harst,P., Vollenweider,P.,
            Wallaschofski,H., Wareham,N.J., Watkins,H., Wichmann,H.E.,
            Wilson,J.F., Abecasis,G.R., Assimes,T.L., Barroso,I., Boehnke,M.,
            Borecki,I.B., Deloukas,P., Fox,C.S., Frayling,T., Groop,L.C.,
            Haritunian,T., Heid,I.M., Hunter,D., Kaplan,R.C., Karpe,F.,
            Moffatt,M.F., Mohlke,K.L., O'Connell,J.R., Pawitan,Y., Schadt,E.E.,
            Schlessinger,D., Steinthorsdottir,V., Strachan,D.P.,
            Thorsteinsdottir,U., van Duijn,C.M., Visscher,P.M., Di Blasio,A.M.,
            Hirschhorn,J.N., Lindgren,C.M., Morris,A.P., Meyre,D., Scherag,A.,
            McCarthy,M.I., Speliotes,E.K., North,K.E., Loos,R.J. and
            Ingelsson,E.
  TITLE     Genome-wide meta-analysis identifies 11 new loci for anthropometric
            traits and provides insights into genetic architecture
  JOURNAL   Nat Genet 45 (5), 501-512 (2013)
   PUBMED   23563607
REFERENCE   7  (residues 1 to 235)
  AUTHORS   Cuajungco,M.P., Podevin,W., Valluri,V.K., Bui,Q., Nguyen,V.H. and
            Taylor,K.
  TITLE     Abnormal accumulation of human transmembrane (TMEM)-176A and 176B
            proteins is associated with cancer pathology
  JOURNAL   Acta Histochem 114 (7), 705-712 (2012)
   PUBMED   22244448
  REMARK    GeneRIF: human TMEM176A and 176B protein levels are significantly
            elevated in lymphoma, but not in normal tissues
REFERENCE   8  (residues 1 to 235)
  AUTHORS   Lango Allen,H., Estrada,K., Lettre,G., Berndt,S.I., Weedon,M.N.,
            Rivadeneira,F., Willer,C.J., Jackson,A.U., Vedantam,S.,
            Raychaudhuri,S., Ferreira,T., Wood,A.R., Weyant,R.J., Segre,A.V.,
            Speliotes,E.K., Wheeler,E., Soranzo,N., Park,J.H., Yang,J.,
            Gudbjartsson,D., Heard-Costa,N.L., Randall,J.C., Qi,L., Vernon
            Smith,A., Magi,R., Pastinen,T., Liang,L., Heid,I.M., Luan,J.,
            Thorleifsson,G., Winkler,T.W., Goddard,M.E., Sin Lo,K., Palmer,C.,
            Workalemahu,T., Aulchenko,Y.S., Johansson,A., Zillikens,M.C.,
            Feitosa,M.F., Esko,T., Johnson,T., Ketkar,S., Kraft,P., Mangino,M.,
            Prokopenko,I., Absher,D., Albrecht,E., Ernst,F., Glazer,N.L.,
            Hayward,C., Hottenga,J.J., Jacobs,K.B., Knowles,J.W., Kutalik,Z.,
            Monda,K.L., Polasek,O., Preuss,M., Rayner,N.W., Robertson,N.R.,
            Steinthorsdottir,V., Tyrer,J.P., Voight,B.F., Wiklund,F., Xu,J.,
            Zhao,J.H., Nyholt,D.R., Pellikka,N., Perola,M., Perry,J.R.,
            Surakka,I., Tammesoo,M.L., Altmaier,E.L., Amin,N., Aspelund,T.,
            Bhangale,T., Boucher,G., Chasman,D.I., Chen,C., Coin,L.,
            Cooper,M.N., Dixon,A.L., Gibson,Q., Grundberg,E., Hao,K., Juhani
            Junttila,M., Kaplan,L.M., Kettunen,J., Konig,I.R., Kwan,T.,
            Lawrence,R.W., Levinson,D.F., Lorentzon,M., McKnight,B.,
            Morris,A.P., Muller,M., Suh Ngwa,J., Purcell,S., Rafelt,S.,
            Salem,R.M., Salvi,E., Sanna,S., Shi,J., Sovio,U., Thompson,J.R.,
            Turchin,M.C., Vandenput,L., Verlaan,D.J., Vitart,V., White,C.C.,
            Ziegler,A., Almgren,P., Balmforth,A.J., Campbell,H., Citterio,L.,
            De Grandi,A., Dominiczak,A., Duan,J., Elliott,P., Elosua,R.,
            Eriksson,J.G., Freimer,N.B., Geus,E.J., Glorioso,N., Haiqing,S.,
            Hartikainen,A.L., Havulinna,A.S., Hicks,A.A., Hui,J., Igl,W.,
            Illig,T., Jula,A., Kajantie,E., Kilpelainen,T.O., Koiranen,M.,
            Kolcic,I., Koskinen,S., Kovacs,P., Laitinen,J., Liu,J., Lokki,M.L.,
            Marusic,A., Maschio,A., Meitinger,T., Mulas,A., Pare,G.,
            Parker,A.N., Peden,J.F., Petersmann,A., Pichler,I.,
            Pietilainen,K.H., Pouta,A., Ridderstrale,M., Rotter,J.I.,
            Sambrook,J.G., Sanders,A.R., Schmidt,C.O., Sinisalo,J., Smit,J.H.,
            Stringham,H.M., Bragi Walters,G., Widen,E., Wild,S.H.,
            Willemsen,G., Zagato,L., Zgaga,L., Zitting,P., Alavere,H.,
            Farrall,M., McArdle,W.L., Nelis,M., Peters,M.J., Ripatti,S., van
            Meurs,J.B., Aben,K.K., Ardlie,K.G., Beckmann,J.S., Beilby,J.P.,
            Bergman,R.N., Bergmann,S., Collins,F.S., Cusi,D., den Heijer,M.,
            Eiriksdottir,G., Gejman,P.V., Hall,A.S., Hamsten,A., Huikuri,H.V.,
            Iribarren,C., Kahonen,M., Kaprio,J., Kathiresan,S., Kiemeney,L.,
            Kocher,T., Launer,L.J., Lehtimaki,T., Melander,O., Mosley,T.H. Jr.,
            Musk,A.W., Nieminen,M.S., O'Donnell,C.J., Ohlsson,C., Oostra,B.,
            Palmer,L.J., Raitakari,O., Ridker,P.M., Rioux,J.D., Rissanen,A.,
            Rivolta,C., Schunkert,H., Shuldiner,A.R., Siscovick,D.S.,
            Stumvoll,M., Tonjes,A., Tuomilehto,J., van Ommen,G.J., Viikari,J.,
            Heath,A.C., Martin,N.G., Montgomery,G.W., Province,M.A., Kayser,M.,
            Arnold,A.M., Atwood,L.D., Boerwinkle,E., Chanock,S.J., Deloukas,P.,
            Gieger,C., Gronberg,H., Hall,P., Hattersley,A.T., Hengstenberg,C.,
            Hoffman,W., Lathrop,G.M., Salomaa,V., Schreiber,S., Uda,M.,
            Waterworth,D., Wright,A.F., Assimes,T.L., Barroso,I., Hofman,A.,
            Mohlke,K.L., Boomsma,D.I., Caulfield,M.J., Cupples,L.A.,
            Erdmann,J., Fox,C.S., Gudnason,V., Gyllensten,U., Harris,T.B.,
            Hayes,R.B., Jarvelin,M.R., Mooser,V., Munroe,P.B., Ouwehand,W.H.,
            Penninx,B.W., Pramstaller,P.P., Quertermous,T., Rudan,I.,
            Samani,N.J., Spector,T.D., Volzke,H., Watkins,H., Wilson,J.F.,
            Groop,L.C., Haritunians,T., Hu,F.B., Kaplan,R.C., Metspalu,A.,
            North,K.E., Schlessinger,D., Wareham,N.J., Hunter,D.J.,
            O'Connell,J.R., Strachan,D.P., Wichmann,H.E., Borecki,I.B., van
            Duijn,C.M., Schadt,E.E., Thorsteinsdottir,U., Peltonen,L.,
            Uitterlinden,A.G., Visscher,P.M., Chatterjee,N., Loos,R.J.,
            Boehnke,M., McCarthy,M.I., Ingelsson,E., Lindgren,C.M.,
            Abecasis,G.R., Stefansson,K., Frayling,T.M. and Hirschhorn,J.N.
  TITLE     Hundreds of variants clustered in genomic loci and biological
            pathways affect human height
  JOURNAL   Nature 467 (7317), 832-838 (2010)
   PUBMED   20881960
REFERENCE   9  (residues 1 to 235)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   10 (residues 1 to 235)
  AUTHORS   Nakajima,H., Takenaka,M., Kaimori,J.Y., Nagasawa,Y., Kosugi,A.,
            Kawamoto,S., Imai,E., Hori,M. and Okubo,K.
  TITLE     Gene expression profile of renal proximal tubules regulated by
            proteinuria
  JOURNAL   Kidney Int 61 (5), 1577-1587 (2002)
   PUBMED   11967007
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC008303.1.
            
            On Jul 9, 2003 this sequence version replaced NP_060957.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008303.1, AF258340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000004103.8/ ENSP00000004103.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..235
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q36.1"
     Protein         1..235
                     /product="transmembrane protein 176A"
                     /note="likley ortholog of mouse GS188; hepatocellular
                     carcinoma-associated antigen 112"
                     /calculated_mol_wt=25985
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DCS1; propagated from
                     UniProtKB/Swiss-Prot (Q96HP8.1)"
     Site            55..75
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP8.1)"
     Region          56..194
                     /region_name="CD20"
                     /note="CD20-like family; pfam04103"
                     /db_xref="CDD:461174"
     Site            86..106
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP8.1)"
     Site            113..133
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP8.1)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96HP8.1)"
     CDS             1..235
                     /gene="TMEM176A"
                     /gene_synonym="GS188; HCA112; MS4B1"
                     /coded_by="NM_018487.3:76..783"
                     /db_xref="CCDS:CCDS5909.1"
                     /db_xref="GeneID:55365"
                     /db_xref="HGNC:HGNC:24930"
                     /db_xref="MIM:610334"
ORIGIN      
        1 mgtadsdema peapqhthid vhihqesala kllltccsal rpratqargs srllvaswvm
       61 qivlgilsav lggffyirdy tllvtsgaai wtgavavlag aaafiyekrg gtywallrtl
      121 ltlaafstai aalklwnedf rygysyynsa crissssdwn tpaptqspee vrrlhlctsf
      181 mdmlkalfrt lqamllgvwi llllasltpl wlycwrmfpt kgkrdqkeml evsgi
//
LOCUS       NP_620706               1130 aa            linear   PRI 20-NOV-2025
DEFINITION  SWI/SNF complex subunit SMARCC2 isoform b [Homo sapiens].
ACCESSION   NP_620706
VERSION     NP_620706.1
DBSOURCE    REFSEQ: accession NM_139067.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1130)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1130)
  AUTHORS   Bosch,E., Popp,B., Guse,E., Skinner,C., van der Sluijs,P.J.,
            Maystadt,I., Pinto,A.M., Renieri,A., Bruno,L.P., Granata,S.,
            Marcelis,C., Baysal,O., Hartwich,D., Holthofer,L., Isidor,B.,
            Cogne,B., Wieczorek,D., Capra,V., Scala,M., De Marco,P.,
            Ognibene,M., Jamra,R.A., Platzer,K., Carter,L.B., Kuismin,O., van
            Haeringen,A., Maroofian,R., Valenzuela,I., Cusco,I.,
            Martinez-Agosto,J.A., Rabani,A.M., Mefford,H.C., Pereira,E.M.,
            Close,C., Anyane-Yeboa,K., Wagner,M., Hannibal,M.C., Zacher,P.,
            Thiffault,I., Beunders,G., Umair,M., Bhola,P.T., McGinnis,E.,
            Millichap,J., van de Kamp,J.M., Prijoles,E.J., Dobson,A.,
            Shillington,A., Graham,B.H., Garcia,E.J., Galindo,M.K.,
            Ropers,F.G., Nibbeling,E.A.R., Hubbard,G., Karimov,C., Goj,G.,
            Bend,R., Rath,J., Morrow,M.M., Millan,F., Salpietro,V., Torella,A.,
            Nigro,V., Kurki,M., Stevenson,R.E., Santen,G.W.E., Zweier,M.,
            Campeau,P.M., Severino,M., Reis,A., Accogli,A. and Vasileiou,G.
  TITLE     Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals
  JOURNAL   Genet Med 25 (11), 100950 (2023)
   PUBMED   37551667
  REMARK    GeneRIF: Elucidating the clinical and molecular spectrum of
            SMARCC2-associated NDD in a cohort of 65 affected individuals.
REFERENCE   3  (residues 1 to 1130)
  AUTHORS   Liu,S., Liu,P., Zhu,C., Yang,R., He,Z., Li,Y., Li,Y., Fei,X.,
            Hou,J., Wang,X. and Pan,Y.
  TITLE     FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination
  JOURNAL   Aging (Albany NY) 15 (12), 5381-5398 (2023)
   PUBMED   37348029
  REMARK    GeneRIF: FBXO28 promotes proliferation, invasion, and metastasis of
            pancreatic cancer cells through regulation of SMARCC2
            ubiquitination.
            Erratum:[Aging (Albany NY). 2023 Sep 14;15(17):9230-9232. doi:
            10.18632/aging.205071. PMID: 37708091]
REFERENCE   4  (residues 1 to 1130)
  AUTHORS   Pintacuda,G., Hsu,Y.H., Tsafou,K., Li,K.W., Martin,J.M.,
            Riseman,J., Biagini,J.C., Ching,J.K.T., Mena,D.,
            Gonzalez-Lozano,M.A., Egri,S.B., Jaffe,J., Smit,A.B., Fornelos,N.,
            Eggan,K.C. and Lage,K.
  TITLE     Protein interaction studies in human induced neurons indicate
            convergent biology underlying autism spectrum disorders
  JOURNAL   Cell Genom 3 (3), 100250 (2023)
   PUBMED   36950384
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1130)
  AUTHORS   Li,C., Wang,T., Gu,J., Qi,S., Li,J., Chen,L., Wu,H., Shi,L.,
            Song,C., Li,H., Zhu,L., Lu,Y. and Zhou,Q.
  TITLE     SMARCC2 mediates the regulation of DKK1 by the transcription factor
            EGR1 through chromatin remodeling to reduce the proliferative
            capacity of glioblastoma
  JOURNAL   Cell Death Dis 13 (11), 990 (2022)
   PUBMED   36418306
  REMARK    GeneRIF: SMARCC2 mediates the regulation of DKK1 by the
            transcription factor EGR1 through chromatin remodeling to reduce
            the proliferative capacity of glioblastoma.
            Erratum:[Cell Death Dis. 2022 Dec 12;13(12):1033. doi:
            10.1038/s41419-022-05498-x. PMID: 36509739]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1130)
  AUTHORS   Wang,W., Chi,T., Xue,Y., Zhou,S., Kuo,A. and Crabtree,G.R.
  TITLE     Architectural DNA binding by a high-mobility-group/kinesin-like
            subunit in mammalian SWI/SNF-related complexes
  JOURNAL   Proc Natl Acad Sci U S A 95 (2), 492-498 (1998)
   PUBMED   9435219
REFERENCE   7  (residues 1 to 1130)
  AUTHORS   Reyes,J.C., Muchardt,C. and Yaniv,M.
  TITLE     Components of the human SWI/SNF complex are enriched in active
            chromatin and are associated with the nuclear matrix
  JOURNAL   J Cell Biol 137 (2), 263-274 (1997)
   PUBMED   9128241
REFERENCE   8  (residues 1 to 1130)
  AUTHORS   Wang,W., Cote,J., Xue,Y., Zhou,S., Khavari,P.A., Biggar,S.R.,
            Muchardt,C., Kalpana,G.V., Goff,S.P., Yaniv,M., Workman,J.L. and
            Crabtree,G.R.
  TITLE     Purification and biochemical heterogeneity of the mammalian SWI-SNF
            complex
  JOURNAL   EMBO J 15 (19), 5370-5382 (1996)
   PUBMED   8895581
REFERENCE   9  (residues 1 to 1130)
  AUTHORS   Wang,W., Xue,Y., Zhou,S., Kuo,A., Cairns,B.R. and Crabtree,G.R.
  TITLE     Diversity and specialization of mammalian SWI/SNF complexes
  JOURNAL   Genes Dev 10 (17), 2117-2130 (1996)
   PUBMED   8804307
REFERENCE   10 (residues 1 to 1130)
  AUTHORS   Schrier Vergano,S., Santen,G., Wieczorek,D. and Matsumoto,N.
  TITLE     Coffin-Siris Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   23556151
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB209006.1, CX165574.1 and
            BM875330.1.
            
            Summary: The protein encoded by this gene is a member of the
            SWI/SNF family of proteins, whose members display helicase and
            ATPase activities and which are thought to regulate transcription
            of certain genes by altering the chromatin structure around those
            genes. The encoded protein is part of the large ATP-dependent
            chromatin remodeling complex SNF/SWI and contains a predicted
            leucine zipper motif typical of many transcription factors.
            Alternatively spliced transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) contains an alternate in-frame
            exon in the central coding region and uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1. The
            encoded isoform (b), contains a novel internal segment, lacks a
            segment near the C-terminus, and is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013045.1, BT009924.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1130
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.2"
     Protein         1..1130
                     /product="SWI/SNF complex subunit SMARCC2 isoform b"
                     /note="chromatin remodeling complex BAF170 subunit;
                     SWI3-like protein; SWI/SNF complex 170 kDa subunit;
                     mammalian chromatin remodeling complex BRG1-associated
                     factor 170; SWI/SNF complex subunit SMARCC2; SWI/SNF
                     related, matrix associated, actin dependent regulator of
                     chromatin subfamily c member 2"
                     /calculated_mol_wt=124710
     Region          4..420
                     /region_name="SWIRM-assoc_2"
                     /note="SWIRM-associated domain at the N-terminal;
                     pfam16496"
                     /db_xref="CDD:465143"
     Region          379..>739
                     /region_name="RSC8"
                     /note="RSC chromatin remodeling complex subunit RSC8
                     [Chromatin structure and dynamics / Transcription];
                     COG5259"
                     /db_xref="CDD:227584"
     Region          715..781
                     /region_name="SWIRM-assoc_3"
                     /note="SWIRM-associated domain at the C-terminal;
                     pfam16498"
                     /db_xref="CDD:465145"
     Region          <721..978
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <911..977
                     /region_name="SWIRM-assoc_1"
                     /note="SWIRM-associated region 1; pfam16495"
                     /db_xref="CDD:465142"
     CDS             1..1130
                     /gene="SMARCC2"
                     /gene_synonym="BAF170; CRACC2; CSS8; Rsc8"
                     /coded_by="NM_139067.4:23..3415"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8908.1"
                     /db_xref="GeneID:6601"
                     /db_xref="HGNC:HGNC:11105"
                     /db_xref="MIM:601734"
ORIGIN      
        1 mavrkkdggp nvkyyeaadt vtqfdnvrlw lgknykkyiq aepptnksls slvvqllqfq
       61 eevfgkhvsn apltklpikc fldfkaggsl chilaaaykf ksdqgwrryd fqnpsrmdrn
      121 vemfmtieks lvqnnclsrp niflcpeiep kllgklkdii krhqgtvted knnashvvyp
      181 vpgnleeeew vrpvmkrdkq vllhwgyypd sydtwipase ieasvedapt pekprkvhak
      241 wildtdtfne wmneedyevn ddknpvsrrk kisaktltde vnspdsdrrd kkggnykkrk
      301 rspspsptpe akkknakkgp stpytkskrg hreeeqedlt kdmdepspvp nveevtlpkt
      361 vntkkdsesa pvkggtmtdl deqedesmet tgkdedenst gnkgeqtknp dlhednvteq
      421 thhiiipsya awfdynsvha ierralpeff ngknksktpe iylayrnfmi dtyrlnpqey
      481 ltstacrrnl agdvcaimrv hafleqwgli nyqvdaesrp tpmgppptsh fhvladtpsg
      541 lvplqpktpq grqvdadtka grkgkelddl vpetakgkpe lqtsasqqml nfpdkgkekp
      601 tdmqnfglrt dmytkknvps kskaaasatr ewteqetlll lealemykdd wnkvsehvgs
      661 rtqdecilhf lrlpiedpyl edseaslgpl ayqpipfsqs gnpvmstvaf lasvvdprva
      721 saaaksalee fskmkeevpt alveahvrkv eeaakvtgka dpafglessg iagttsdepe
      781 rieesgndea rvegqatdek kepkepregg gaieeeakek tseapkkdee kgkegdseke
      841 seksdgdpiv dpekekepke gqeevlkevv esegerktkv erdigegnls taaaaalaaa
      901 avkakhlaav eerkikslva llvetqmkkl eiklrhfeel etimdrerea leyqrqqlla
      961 drqafhmeql kyaemrarqq hfqqmhqqqq qpppalppgs qpipptgaag ppavhglava
     1021 pasvvpapag sgappgslgp seqigqagst agpqqqqpag apqpgavppg vpppgphgps
     1081 pfpnqqtpps mmpgavpgsg hpgvadpgtp lppdptapsp gtvtpvpppq
//
LOCUS       NP_037397                782 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 51 homolog [Homo
            sapiens].
ACCESSION   NP_037397
VERSION     NP_037397.2
DBSOURCE    REFSEQ: accession NM_013265.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Chauhan,M., Betancourt,A., Balakrishnan,M., Mishra,A., Fox,K.,
            Belfort,M. and Yallampalli,C.
  TITLE     Soluble fms-like tyrosine kinase-1 and angiotensin2 target
            calcitonin gene-related peptide family peptides in maternal
            vascular smooth muscle cells in pregnancydagger
  JOURNAL   Biol Reprod 104 (5), 1071-1083 (2021)
   PUBMED   33624744
  REMARK    GeneRIF: Soluble fms-like tyrosine kinase-1 and angiotensin2 target
            calcitonin gene-related peptide family peptides in maternal
            vascular smooth muscle cells in pregnancydagger.
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Uwineza,A., Caberg,J.H., Hitayezu,J., Wenric,S., Mutesa,L.,
            Vial,Y., Drunat,S., Passemard,S., Verloes,A., El Ghouzzi,V. and
            Bours,V.
  TITLE     VPS51 biallelic variants cause microcephaly with brain
            malformations: A confirmatory report
  JOURNAL   Eur J Med Genet 62 (8), 103704 (2019)
   PUBMED   31207318
  REMARK    GeneRIF: This observation supports a pathogenic effect of VPS51
            variants, which has only been reported previously once, in a single
            child with microcephaly. It confirms the key role of membrane
            trafficking in normal brain development and homeostasis.
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Gershlick,D.C., Ishida,M., Jones,J.R., Bellomo,A., Bonifacino,J.S.
            and Everman,D.B.
  TITLE     A neurodevelopmental disorder caused by mutations in the VPS51
            subunit of the GARP and EARP complexes
  JOURNAL   Hum Mol Genet 28 (9), 1548-1560 (2019)
   PUBMED   30624672
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Schindler,C., Chen,Y., Pu,J., Guo,X. and Bonifacino,J.S.
  TITLE     EARP is a multisubunit tethering complex involved in endocytic
            recycling
  JOURNAL   Nat Cell Biol 17 (5), 639-650 (2015)
   PUBMED   25799061
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Abascal-Palacios,G., Schindler,C., Rojas,A.L., Bonifacino,J.S. and
            Hierro,A.
  TITLE     Structural basis for the interaction of the Golgi-Associated
            Retrograde Protein Complex with the t-SNARE Syntaxin 6
  JOURNAL   Structure 21 (9), 1698-1706 (2013)
   PUBMED   23932592
  REMARK    GeneRIF: A dityrosine motif of Ang2 interacts with a highly
            conserved groove in Syntaxin 6.
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Perez-Victoria,F.J., Schindler,C., Magadan,J.G., Mardones,G.A.,
            Delevoye,C., Romao,M., Raposo,G. and Bonifacino,J.S.
  TITLE     Ang2/fat-free is a conserved subunit of the Golgi-associated
            retrograde protein complex
  JOURNAL   Mol Biol Cell 21 (19), 3386-3395 (2010)
   PUBMED   20685960
  REMARK    GeneRIF: Ang2 is the missing component of the Golgi-associated
            retrograde protein complex in most eukaryotes.
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Lemmens,I., Merregaert,J., Van de Ven,W.J., Kas,K., Zhang,C.X.,
            Giraud,S., Wautot,V., Buisson,N., De Witte,K., Salandre,J.,
            Lenoir,G., Calender,A., Parente,F., Quincey,D., Courseaux,A.,
            Carle,G.F., Gaudray,P., De Wit,M.J., Lips,C.J., Hoppener,J.W.,
            Khodaei,S., Grant,A.L., Weber,G., Kytola,S., Thakker,R.V. et al.
  TITLE     Construction of a 1.2-Mb sequence-ready contig of chromosome 11q13
            encompassing the multiple endocrine neoplasia type 1 (MEN1) gene.
            The European Consortium on MEN1
  JOURNAL   Genomics 44 (1), 94-100 (1997)
   PUBMED   9286704
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Canestri,F.
  TITLE     A proposed clinical application of a model of CO2 laser radiation
            induced damage craters
  JOURNAL   J Med Eng Technol 12 (3), 112-117 (1988)
   PUBMED   3172165
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF024631.2, HY270070.1,
            AW007399.1 and AP003068.3.
            
            On Jun 9, 2000 this sequence version replaced NP_037397.1.
            
            Summary: This gene encodes a member of the vacuolar protein
            sorting-associated protein 51 family. The encoded protein is a
            component of the Golgi-associated retrograde protein complex which
            acts as a tethering factor for carriers in retrograde transport
            from the early and late endosomes to the trans-Golgi network.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2012].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the functional protein.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF024631.2, SRR3476690.841371.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279281.8/ ENSP00000279281.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..782
                     /product="vacuolar protein sorting-associated protein 51
                     homolog"
                     /note="protein fat-free homolog; another new gene 2
                     protein; vacuolar protein sorting 51 homolog; VPS51, GARP
                     complex subunit"
                     /calculated_mol_wt=85912
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UID3.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9UID3.2)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UID3.2)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UVL4; propagated from
                     UniProtKB/Swiss-Prot (Q9UID3.2)"
     Region          63..147
                     /region_name="Vps51"
                     /note="Vps51/Vps67; pfam08700"
                     /db_xref="CDD:462568"
     Region          79..>242
                     /region_name="COG2"
                     /note="COG (conserved oligomeric Golgi) complex component,
                     COG2; cl19297"
                     /db_xref="CDD:473160"
     Site            649
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UID3.2)"
     CDS             1..782
                     /gene="VPS51"
                     /gene_synonym="ANG2; ANG3; C11orf2; C11orf3; FFR; PCH13"
                     /coded_by="NM_013265.4:38..2386"
                     /db_xref="CCDS:CCDS8093.1"
                     /db_xref="GeneID:738"
                     /db_xref="HGNC:HGNC:1172"
                     /db_xref="MIM:615738"
ORIGIN      
        1 maaaaaagps pgsgpgdspe gpegeaperr rkahgmlkly yglsegeaag rpagpdpldp
       61 tdlngahfdp evyldklrre cplaqlmdse tdmvrqiral dsdmqtlvye nynkfisatd
      121 tirkmkndfr kmedemdrla tnmavitdfs arisatlqdr heritklagv hallrklqfl
      181 felpsrltkc velgaygqav ryqgraqavl qqyqhlpsfr aiqddcqvit arlaqqlrqr
      241 freggsgape qaecvellla lgepaeelce eflahargrl ekelrnleae lgpsppapdv
      301 leftdhggsg fvgglcqvaa ayqelfaaqg pagaeklaaf arqlgsryfa lverrlaqeq
      361 gggdnsllvr aldrfhrrlr apgallaaag ladaateive rvarerlghh lqglraaflg
      421 cltdvrqala aprvagkegp glaellanva ssilshikas laavhlftak evsfsnkpyf
      481 rgefcsqgvr eglivgfvhs mcqtaqsfcd spgekggatp palllllsrl cldyetatis
      541 yiltltdeqf lvqdqfpvtp vstlcaeare tarrllthyv kvqglvisqm lrksvetrdw
      601 lstleprnvr avmkrvvedt taidvqvgll yeegvrkaqs sdsskrtfsv ysssrqqgry
      661 apsytpsapm dtnllsniqk lfseridvfs pvefnkvsvl tgiikislkt llecvrlrtf
      721 grfglqqvqv dchflqlylw rfvadeelvh llldevvasa alrcpdpvpm epsvvevice
      781 rg
//
LOCUS       NP_001269162             167 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit alpha type-6 isoform b [Homo sapiens].
ACCESSION   NP_001269162 XP_005267927
VERSION     NP_001269162.1
DBSOURCE    REFSEQ: accession NM_001282233.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 167)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   2  (residues 1 to 167)
  AUTHORS   Zhao,J., Makhija,S., Zhou,C., Zhang,H., Wang,Y., Muralidharan,M.,
            Huang,B. and Cheng,Y.
  TITLE     Structural insights into the human PA28-20S proteasome enabled by
            efficient tagging and purification of endogenous proteins
  JOURNAL   Proc Natl Acad Sci U S A 119 (33), e2207200119 (2022)
   PUBMED   35858375
REFERENCE   3  (residues 1 to 167)
  AUTHORS   Thomas,T.A. and Smith,D.M.
  TITLE     Proteasome activator 28gamma (PA28gamma) allosterically activates
            trypsin-like proteolysis by binding to the alpha-ring of the 20S
            proteasome
  JOURNAL   J Biol Chem 298 (8), 102140 (2022)
   PUBMED   35714770
REFERENCE   4  (residues 1 to 167)
  AUTHORS   Zivkovic,D., Sanchez Dafun,A., Menneteau,T., Schahl,A., Lise,S.,
            Kervarrec,C., Toste Rego,A., da Fonseca,P.C.A., Chavent,M.,
            Pineau,C., Burlet-Schiltz,O., Marcoux,J. and Bousquet,M.P.
  TITLE     Proteasome complexes experience profound structural and functional
            rearrangements throughout mammalian spermatogenesis
  JOURNAL   Proc Natl Acad Sci U S A 119 (15), e2116826119 (2022)
   PUBMED   35377789
REFERENCE   5  (residues 1 to 167)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 167)
  AUTHORS   Nederlof,P.M., Wang,H.R. and Baumeister,W.
  TITLE     Nuclear localization signals of human and Thermoplasma proteasomal
            alpha subunits are functional in vitro
  JOURNAL   Proc Natl Acad Sci U S A 92 (26), 12060-12064 (1995)
   PUBMED   8618844
REFERENCE   7  (residues 1 to 167)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   8  (residues 1 to 167)
  AUTHORS   Kato,S., Sekine,S., Oh,S.W., Kim,N.S., Umezawa,Y., Abe,N.,
            Yokoyama-Kobayashi,M. and Aoki,T.
  TITLE     Construction of a human full-length cDNA bank
  JOURNAL   Gene 150 (2), 243-250 (1994)
   PUBMED   7821789
REFERENCE   9  (residues 1 to 167)
  AUTHORS   Bey,F., Silva Pereira,I., Coux,O., Viegas-Pequignot,E., Recillas
            Targa,F., Nothwang,H.G., Dutrillaux,B. and Scherrer,K.
  TITLE     The prosomal RNA-binding protein p27K is a member of the alpha-type
            human prosomal gene family
  JOURNAL   Mol Gen Genet 237 (1-2), 193-205 (1993)
   PUBMED   7681138
REFERENCE   10 (residues 1 to 167)
  AUTHORS   DeMartino,G.N., Orth,K., McCullough,M.L., Lee,L.W., Munn,T.Z.,
            Moomaw,C.R., Dawson,P.A. and Slaughter,C.A.
  TITLE     The primary structures of four subunits of the human,
            high-molecular-weight proteinase, macropain (proteasome), are
            distinct but homologous
  JOURNAL   Biochim Biophys Acta 1079 (1), 29-38 (1991)
   PUBMED   1888762
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU657545.1, BG701535.1,
            AK298920.1 and BQ009843.1.
            
            On Aug 24, 2013 this sequence version replaced XP_005267927.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the peptidase T1A family, that is a 20S core alpha
            subunit. Multiple transcript variants encoding several different
            isoforms have been found for this gene. A pseudogene has been
            identified on the Y chromosome. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) lacks an alternate exon
            compared to variant 1. This difference causes translation
            initiation at a downstream AUG and results in an isoform (b) with a
            shorter N-terminus compared to isoform a. Variants 2 and 3 both
            encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298920.1, SRR1803615.261961.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..167
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.2"
     Protein         1..167
                     /product="proteasome subunit alpha type-6 isoform b"
                     /EC_number="3.4.25.1"
                     /note="macropain subunit iota; prosomal P27K protein;
                     proteasome subunit iota; proteasome iota chain; proteasome
                     subunit alpha 6; proteasome subunit alpha1; macropain iota
                     chain; multicatalytic endopeptidase complex iota chain; 27
                     kDa prosomal protein; PROS-27; proteasome (prosome,
                     macropain) subunit, alpha type, 6; testicular secretory
                     protein Li 44; alpha-1; proteasome subunit alpha-1"
                     /calculated_mol_wt=18684
     Region          <1..141
                     /region_name="Ntn_hydrolase"
                     /note="The Ntn hydrolases (N-terminal nucleophile) are a
                     diverse superfamily of of enzymes that are activated
                     autocatalytically via an N-terminally lcated nucleophilic
                     amino acid. N-terminal nucleophile (NTN-) hydrolase
                     superfamily, which contains a...; cl00467"
                     /db_xref="CDD:469781"
     CDS             1..167
                     /gene="PSMA6"
                     /gene_synonym="IOTA; p27K; PROS27"
                     /coded_by="NM_001282233.1:303..806"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61438.1"
                     /db_xref="GeneID:5687"
                     /db_xref="HGNC:HGNC:9535"
                     /db_xref="MIM:602855"
ORIGIN      
        1 mtgmtadsrs qvqraryeaa nwkykygyei pvdmlckria disqvytqna emrplgccmi
       61 ligideeqgp qvykcdpagy ycgfkataag vkqtestsfl ekkvkkkfdw tfeqtvetai
      121 tclstvlsid fkpseievgv vtvenpkfri lteaeidahl valaerd
//
LOCUS       NP_001298130             179 aa            linear   PRI 20-NOV-2025
DEFINITION  methylosome subunit pICln isoform c [Homo sapiens].
ACCESSION   NP_001298130
VERSION     NP_001298130.1
DBSOURCE    REFSEQ: accession NM_001311201.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 179)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 179)
  AUTHORS   Cui,Z., He,J., Zhu,J., Ni,W., Liu,L., Bian,Z., Mao,S., Gu,S.,
            Shan,Y., Chu,Z., Wu,Q., Lu,J., Liu,Y., Sun,F., Pan,Q., Zhang,Y.,
            Huang,N. and Ma,J.
  TITLE     O-GlcNAcylated LARP1 positively regulated by circCLNS1A facilitates
            hepatoblastoma progression through DKK4/beta-catenin signalling
  JOURNAL   Clin Transl Med 13 (4), e1239 (2023)
   PUBMED   37070251
  REMARK    GeneRIF: O-GlcNAcylated LARP1 positively regulated by circCLNS1A
            facilitates hepatoblastoma progression through DKK4/beta-catenin
            signalling.
REFERENCE   3  (residues 1 to 179)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 179)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 179)
  AUTHORS   Beketova,E., Fang,S., Owens,J.L., Liu,S., Chen,X., Zhang,Q.,
            Asberry,A.M., Deng,X., Malola,J., Huang,J., Li,C., Pili,R.,
            Elzey,B.D., Ratliff,T.L., Wan,J. and Hu,C.D.
  TITLE     Protein Arginine Methyltransferase 5 Promotes pICln-Dependent
            Androgen Receptor Transcription in Castration-Resistant Prostate
            Cancer
  JOURNAL   Cancer Res 80 (22), 4904-4917 (2020)
   PUBMED   32999000
  REMARK    GeneRIF: Protein Arginine Methyltransferase 5 Promotes
            pICln-Dependent Androgen Receptor Transcription in
            Castration-Resistant Prostate Cancer.
REFERENCE   6  (residues 1 to 179)
  AUTHORS   Schwartz,R.S., Rybicki,A.C. and Nagel,R.L.
  TITLE     Molecular cloning and expression of a chloride channel-associated
            protein pICln in human young red blood cells: association with
            actin
  JOURNAL   Biochem J 327 (Pt 2) (Pt 2), 609-616 (1997)
   PUBMED   9359436
REFERENCE   7  (residues 1 to 179)
  AUTHORS   Bekri,S., Adelaide,J., Merscher,S., Grosgeorge,J., Caroli-Bosc,F.,
            Perucca-Lostanlen,D., Kelley,P.M., Pebusque,M.J., Theillet,C.,
            Birnbaum,D. and Gaudray,P.
  TITLE     Detailed map of a region commonly amplified at 11q13-->q14 in human
            breast carcinoma
  JOURNAL   Cytogenet Cell Genet 79 (1-2), 125-131 (1997)
   PUBMED   9533029
REFERENCE   8  (residues 1 to 179)
  AUTHORS   Nagl,U.O., Erdel,M., Schmarda,A., Seri,M., Pinggera,G.M.,
            Gschwentner,M., Duba,C., Galietta,L.J., Deetjen,P., Utermann,G. and
            Paulmichl,M.
  TITLE     Chromosomal localization of the genes (CLNS1A and CLNS1B) coding
            for the swelling-dependent chloride channel ICln
  JOURNAL   Genomics 38 (3), 438-441 (1996)
   PUBMED   8975725
REFERENCE   9  (residues 1 to 179)
  AUTHORS   Buyse,G., de Greef,C., Raeymaekers,L., Droogmans,G., Nilius,B. and
            Eggermont,J.
  TITLE     The ubiquitously expressed pICln protein forms homomeric complexes
            in vitro
  JOURNAL   Biochem Biophys Res Commun 218 (3), 822-827 (1996)
   PUBMED   8579598
REFERENCE   10 (residues 1 to 179)
  AUTHORS   Anguita,J., Chalfant,M.L., Civan,M.M. and Coca-Prados,M.
  TITLE     Molecular cloning of the human volume-sensitive chloride
            conductance regulatory protein, pICln, from ocular ciliary
            epithelium
  JOURNAL   Biochem Biophys Res Commun 208 (1), 89-95 (1995)
   PUBMED   7887970
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA004269.1, BU538016.1,
            U53454.1, AA757599.1 and AP000609.5.
            
            Summary: This gene encodes a protein that functions in multiple
            regulatory pathways. The encoded protein complexes with numerous
            cytosolic proteins and performs diverse functions including
            regulation of small nuclear ribonucleoprotein biosynthesis,
            platelet activation and cytoskeletal organization. The protein is
            also found associated with the plasma membrane where it functions
            as a chloride current regulator. Pseudogenes of this gene are found
            on chromosomes 1, 4 and 6. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2015].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon compared to variant 1. The resulting isoform (c) has the same
            N- and C-termini but is shorter compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BU538016.1, SRR14038195.455884.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..179
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1"
     Protein         1..179
                     /product="methylosome subunit pICln isoform c"
                     /note="chloride channel regulatory protein; reticulocyte
                     protein ICln; chloride ion current inducer protein;
                     methylosome subunit pICln; i(Cln); reticulocyte pICln;
                     chloride channel, nucleotide sensitive 1A; chloride
                     conductance regulatory protein ICln"
                     /calculated_mol_wt=19612
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.10,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P54105.1)"
     Region          35..>137
                     /region_name="Voldacs"
                     /note="Regulator of volume decrease after cellular
                     swelling; pfam03517"
                     /db_xref="CDD:427344"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphoserine. /evidence=ECO:0000269|Ref.10,
                     ECO:0000269|Ref.11, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P54105.1)"
     Site            144
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P54105.1)"
     CDS             1..179
                     /gene="CLNS1A"
                     /gene_synonym="CLCI; CLNS1B; ICln"
                     /coded_by="NM_001311201.2:81..620"
                     /note="isoform c is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS81602.1"
                     /db_xref="GeneID:1207"
                     /db_xref="HGNC:HGNC:2080"
                     /db_xref="MIM:602158"
ORIGIN      
        1 msflksfppp gpaegllrqq pdteavlngk glgtgtlyia esrlswldgs glgfsleypt
       61 islhalsrdr sdclgehlyv mvnakfeees kepvadeeee dsdddvepit efrfvpsdks
      121 aleamftamc ecqalhpdpe dedsddydge eydveahdgm evdttptvag qfedadvdh
//
LOCUS       NP_071381                507 aa            linear   PRI 20-NOV-2025
DEFINITION  xaa-Pro aminopeptidase 3 isoform 1 [Homo sapiens].
ACCESSION   NP_071381
VERSION     NP_071381.1
DBSOURCE    REFSEQ: accession NM_022098.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Kumar,R., Kotapalli,V., Naz,A., Gowrishankar,S., Rao,S.,
            Pollack,J.R. and Bashyam,M.D.
  TITLE     XPNPEP3 is a novel transcriptional target of canonical
            Wnt/beta-catenin signaling
  JOURNAL   Genes Chromosomes Cancer 57 (6), 304-310 (2018)
   PUBMED   29383790
  REMARK    GeneRIF: results therefore suggest XPNPEP3 to be a transcriptional
            target of Wnt/beta-catenin pathway with particular significance for
            CRC
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Singh,R., Jamdar,S.N., Goyal,V.D., Kumar,A., Ghosh,B. and
            Makde,R.D.
  TITLE     Structure of the human aminopeptidase XPNPEP3 and comparison of its
            in vitro activity with Icp55 orthologs: Insights into diverse
            cellular processes
  JOURNAL   J Biol Chem 292 (24), 10035-10047 (2017)
   PUBMED   28476889
  REMARK    GeneRIF: Data suggest that human XPNPEP3, Ashbya gossypii Icp55,
            and Fusarium graminearum Icp55 exhibit structural and functional
            properties of genuine Xaa-Pro specific aminopeptidases; these
            enzymes appear to function in the previously observed mitochondrial
            role of Icp55 in processing of Nfs1 (mitochondrial cysteine
            desulfurase) substrate. [Icp55 = intermediate-cleavage
            metalloexopeptidases 55]
REFERENCE   6  (residues 1 to 507)
  AUTHORS   O'Toole,J.F., Liu,Y., Davis,E.E., Westlake,C.J., Attanasio,M.,
            Otto,E.A., Seelow,D., Nurnberg,G., Becker,C., Nuutinen,M.,
            Karppa,M., Ignatius,J., Uusimaa,J., Pakanen,S., Jaakkola,E., van
            den Heuvel,L.P., Fehrenbach,H., Wiggins,R., Goyal,M., Zhou,W.,
            Wolf,M.T., Wise,E., Helou,J., Allen,S.J., Murga-Zamalloa,C.A.,
            Ashraf,S., Chaki,M., Heeringa,S., Chernin,G., Hoskins,B.E.,
            Chaib,H., Gleeson,J., Kusakabe,T., Suzuki,T., Isaac,R.E.,
            Quarmby,L.M., Tennant,B., Fujioka,H., Tuominen,H., Hassinen,I.,
            Lohi,H., van Houten,J.L., Rotig,A., Sayer,J.A., Rolinski,B.,
            Freisinger,P., Madhavan,S.M., Herzer,M., Madignier,F., Prokisch,H.,
            Nurnberg,P., Jackson,P.K., Khanna,H., Katsanis,N. and
            Hildebrandt,F.
  TITLE     Individuals with mutations in XPNPEP3, which encodes a
            mitochondrial protein, develop a nephronophthisis-like nephropathy
  JOURNAL   J Clin Invest 120 (3), 791-802 (2010)
   PUBMED   20179356
  REMARK    GeneRIF: Individuals with mutations in XPNPEP3, which encodes a
            mitochondrial protein, develop a nephronophthisis-like nephropathy.
            Erratum:[J Clin Invest. 2010 Apr;120(4):1362. Jackson, Peter
            [corrected to Jackson, Peter K]]
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Ersahin,C., Szpaderska,A.M., Orawski,A.T. and Simmons,W.H.
  TITLE     Aminopeptidase P isozyme expression in human tissues and peripheral
            blood mononuclear cell fractions
  JOURNAL   Arch Biochem Biophys 435 (2), 303-310 (2005)
   PUBMED   15708373
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP346902.1, BC004989.1,
            AL365514.1, AI446638.1, AL035450.1, AL080242.11 and BX648018.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the family of
            X-pro-aminopeptidases that utilize a metal cofactor, and remove the
            N-terminal amino acid from peptides with a proline residue in the
            penultimate position. This protein has been shown to localize to
            the mitochondria of renal cells, and have a role in ciliary
            function. Mutations in this gene are associated with
            nephronophthisis-like nephropathy-1. Alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene, however, expression of some of these isoforms in vivo is
            not known.[provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1, also known as APP3m).
            This isoform has been shown to be localized to the mitochondria
            (PMID:20179356).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.148658.1,
                                           SRR1803613.49857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 20179356
            MANE Ensembl match                 :: ENST00000357137.9/
                                                  ENSP00000349658.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..507
                     /product="xaa-Pro aminopeptidase 3 isoform 1"
                     /EC_number="3.4.11.9"
                     /note="probable Xaa-Pro aminopeptidase 3; X-Pro
                     aminopeptidase 3; Intermediate Cleaving Peptidase 55;
                     X-prolyl aminopeptidase 3, mitochondrial; xaa-Pro
                     aminopeptidase 3"
                     /calculated_mol_wt=56903
     Region          54..79
                     /region_name="Interaction with TNFRSF1B.
                     /evidence=ECO:0000269|PubMed:25609706"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NQH7.1)"
     Region          67..210
                     /region_name="AMP_N"
                     /note="Aminopeptidase P, N-terminal domain; smart01011"
                     /db_xref="CDD:198079"
     Region          252..490
                     /region_name="Prolidase"
                     /note="E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase,
                     X-Pro dipeptidase, proline dipeptidase., imidodipeptidase,
                     peptidase D, gamma-peptidase. Catalyses hydrolysis of
                     Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline
                     analogs. No action on Pro-Pro; cd01087"
                     /db_xref="CDD:238520"
     Site            order(314,331,342,424,451,475)
                     /site_type="active"
                     /db_xref="CDD:238520"
     CDS             1..507
                     /gene="XPNPEP3"
                     /gene_synonym="APP3; ICP55; NPHPL1"
                     /coded_by="NM_022098.4:35..1558"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14007.1"
                     /db_xref="GeneID:63929"
                     /db_xref="HGNC:HGNC:28052"
                     /db_xref="MIM:613553"
ORIGIN      
        1 mpwllsapkl vpavanvrgl sgcmlcsqrr yslqpvperr ipnrylgqps pfthphllrp
       61 gevtpglsqv eyalrrhklm sliqkeaqgq sgtdqtvvvl snptyymsnd ipytfhqdnn
      121 flylcgfqep dsilvlqslp gkqlpshkai lfvprrdpsr elwdgprsgt dgaialtgvd
      181 eaytleefqh llpkmkaetn mvwydwmrps haqlhsdymq plteakaksk nkvrgvqqli
      241 qrlrlikspa eiermqiagk ltsqafietm ftskapveea flyakfefec rargadilay
      301 ppvvaggnrs ntlhyvknnq likdgemvll dggcesscyv sditrtwpvn grftapqael
      361 yeavleiqrd clalcfpgts leniysmmlt ligqklkdlg imknikenna fkaarkycph
      421 hvghylgmdv hdtpdmprsl plqpgmviti epgiyipedd kdapekfrgl gvrieddvvv
      481 tqdsplilsa dcpkemndie qicsqas
//
LOCUS       NP_079405                418 aa            linear   PRI 20-NOV-2025
DEFINITION  protein fuzzy homolog isoform 1 [Homo sapiens].
ACCESSION   NP_079405
VERSION     NP_079405.2
DBSOURCE    REFSEQ: accession NM_025129.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Singh,S., Nampoothiri,S., Narayanan,D.L., Chaudhry,C., Salvankar,S.
            and Girisha,K.M.
  TITLE     Biallelic loss of function variants in FUZ result in an
            orofaciodigital syndrome
  JOURNAL   Eur J Hum Genet 32 (8), 1022-1026 (2024)
   PUBMED   38702430
  REMARK    GeneRIF: Biallelic loss of function variants in FUZ result in an
            orofaciodigital syndrome.
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Langousis,G., Cavadini,S., Boegholm,N., Lorentzen,E., Kempf,G. and
            Matthias,P.
  TITLE     Structure of the ciliogenesis-associated CPLANE complex
  JOURNAL   Sci Adv 8 (15), eabn0832 (2022)
   PUBMED   35427153
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 418)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 418)
  AUTHORS   Seo,J.H., Zilber,Y., Babayeva,S., Liu,J., Kyriakopoulos,P., De
            Marco,P., Merello,E., Capra,V., Gros,P. and Torban,E.
  TITLE     Mutations in the planar cell polarity gene, Fuzzy, are associated
            with neural tube defects in humans
  JOURNAL   Hum Mol Genet 20 (22), 4324-4333 (2011)
   PUBMED   21840926
  REMARK    GeneRIF: Data propose that mutations in Fuzzy may account for a
            subset of neural tube defects in humans.
            Erratum:[Hum Mol Genet. 2015 Jul 1;24(13):3893. doi:
            10.1093/hmg/ddv131. PMID: 25954026]
REFERENCE   7  (residues 1 to 418)
  AUTHORS   Heydeck,W. and Liu,A.
  TITLE     PCP effector proteins inturned and fuzzy play nonredundant roles in
            the patterning but not convergent extension of mammalian neural
            tube
  JOURNAL   Dev Dyn 240 (8), 1938-1948 (2011)
   PUBMED   21761479
REFERENCE   8  (residues 1 to 418)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 418)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   10 (residues 1 to 418)
  AUTHORS   Park,T.J., Haigo,S.L. and Wallingford,J.B.
  TITLE     Ciliogenesis defects in embryos lacking inturned or fuzzy function
            are associated with failure of planar cell polarity and Hedgehog
            signaling
  JOURNAL   Nat Genet 38 (3), 303-311 (2006)
   PUBMED   16493421
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB152506.1, AK315445.1 and
            BU073247.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 15, 2002 this sequence version replaced NP_079405.1.
            
            Summary: This gene encodes a planar cell polarity protein that is
            involved in ciliogenesis and directional cell movement. Knockout
            studies in mice exhibit neural tube defects and defective cilia,
            and mutations in this gene are associated with neural tube defects
            in humans. Alternatively spliced transcript variants have been
            found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC016793.2, AK315445.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000313777.9/ ENSP00000313309.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..418
                     /product="protein fuzzy homolog isoform 1"
                     /note="protein fuzzy homolog; ciliogenesis and planar
                     polarity effector 3; ciliogenesis and planar polarity
                     effector complex subunit 3"
                     /calculated_mol_wt=45548
     Region          12..416
                     /region_name="Fuzzy"
                     /note="protein fuzzy and homologs; cd21091"
                     /db_xref="CDD:411043"
     CDS             1..418
                     /gene="FUZ"
                     /gene_synonym="CPLANE3; FY; NTD"
                     /coded_by="NM_025129.5:187..1443"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS12781.1"
                     /db_xref="GeneID:80199"
                     /db_xref="HGNC:HGNC:26219"
                     /db_xref="MIM:610622"
ORIGIN      
        1 mgeegtggtv hllclaassg vplfcrssrg gaparqqlpf svigslngvh mfgqnlevql
       61 ssartenttv vwksfhdsit livlssevgi selrlerllq mvfgamvllv gleeltnirn
      121 verlkkdlra syclidsflg dseligdltq cvdcvippeg sllqealsgf aeaagttfvs
      181 lvvsgrvvaa tegwwrlgtp eavllpwlvg slppqtardy pvylphgspt vphrlltltl
      241 lpslelcllc gpspplsqly pqllerwwqp lldplraclp lgpralpsgf plhtdilgll
      301 llhlelkrcl ftveplgdke pspeqrrrll rnfytlvtst hfppepgppe ktedevyqaq
      361 lpracylvlg teepgtgvrl valqlglrrl llllspqspt hglrslatht lhaltpll
//
LOCUS       NP_001350794             893 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001350794 XP_016861298
VERSION     NP_001350794.1
DBSOURCE    REFSEQ: accession NM_001363865.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 893)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Jun 3, 2018 this sequence version replaced XP_016861298.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853559.24389.1,
                                           SRR14372079.332688.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..893
                     /product="disks large homolog 1 isoform 6"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=99811
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          702..880
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..893
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001363865.1:227..2908"
                     /note="isoform 6 is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS87192.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgqsfnd krkknlfsrk fpfyknkdqs
      661 eqetsdadqh vtsnasdses syrgqeeyvl syepvnqqev nytrpviilg pmkdrinddl
      721 isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt
      781 svqsvrevae kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar
      841 ktferamkle qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_006075                393 aa            linear   PRI 20-NOV-2025
DEFINITION  interferon regulatory factor 9 isoform 2 [Homo sapiens].
ACCESSION   NP_006075
VERSION     NP_006075.3
DBSOURCE    REFSEQ: accession NM_006084.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 393)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 393)
  AUTHORS   Ritter,J., Szelinski,F., Aue,A., Stefanski,A.L., Rincon-Arevalo,H.,
            Chen,Y., Nitschke,E., Dang,V.D., Wiedemann,A., Schrezenmeier,E.,
            Lino,A.C. and Dorner,T.
  TITLE     Elevated unphosphorylated STAT1 and IRF9 in T and B cells of
            primary sjogren's syndrome: Novel biomarkers for disease activity
            and subsets
  JOURNAL   J Autoimmun 147, 103243 (2024)
   PUBMED   38788537
  REMARK    GeneRIF: Elevated unphosphorylated STAT1 and IRF9 in T and B cells
            of primary sjogren's syndrome: Novel biomarkers for disease
            activity and subsets.
REFERENCE   3  (residues 1 to 393)
  AUTHORS   Calvo-Apalategi,A., Nevado,M.L., Bravo-Gallego,L.Y.,
            Gonzalez-Granado,L.I., Allende,L.M., Pena,R.R., Lopez-Granados,E.
            and Reyburn,H.T.
  TITLE     The lack of either IRF9, or STAT2, has surprisingly little effect
            on human natural killer cell development and function
  JOURNAL   Immunology 172 (3), 440-450 (2024)
   PUBMED   38514903
  REMARK    GeneRIF: The lack of either IRF9, or STAT2, has surprisingly little
            effect on human natural killer cell development and function.
REFERENCE   4  (residues 1 to 393)
  AUTHORS   Nowicka,H., Sekrecka,A., Blaszczyk,K., Kluzek,K., Chang,C.Y.,
            Wesoly,J., Lee,C.K. and Bluyssen,H.A.R.
  TITLE     ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced Transcription
            through Genome-Wide Binding of Phosphorylated and Unphosphorylated
            Complexes to Common ISRE-Containing ISGs
  JOURNAL   Int J Mol Sci 24 (24), 17635 (2023)
   PUBMED   38139463
  REMARK    GeneRIF: ISGF3 and STAT2/IRF9 Control Basal and IFN-Induced
            Transcription through Genome-Wide Binding of Phosphorylated and
            Unphosphorylated Complexes to Common ISRE-Containing ISGs.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 393)
  AUTHORS   You,Y., Grasso,E., Alvero,A., Condon,J., Dimova,T., Hu,A., Ding,J.,
            Alexandrova,M., Manchorova,D., Dimitrova,V., Liao,A. and Mor,G.
  TITLE     Twist1-IRF9 Interaction Is Necessary for IFN-Stimulated Gene
            Anti-Zika Viral Infection
  JOURNAL   J Immunol 210 (12), 1899-1912 (2023)
   PUBMED   37144865
  REMARK    GeneRIF: Twist1-IRF9 Interaction Is Necessary for IFN-Stimulated
            Gene Anti-Zika Viral Infection.
REFERENCE   6  (residues 1 to 393)
  AUTHORS   Martinez-Moczygemba,M., Gutch,M.J., French,D.L. and Reich,N.C.
  TITLE     Distinct STAT structure promotes interaction of STAT2 with the p48
            subunit of the interferon-alpha-stimulated transcription factor
            ISGF3
  JOURNAL   J Biol Chem 272 (32), 20070-20076 (1997)
   PUBMED   9242679
REFERENCE   7  (residues 1 to 393)
  AUTHORS   Horvath,C.M., Stark,G.R., Kerr,I.M. and Darnell,J.E. Jr.
  TITLE     Interactions between STAT and non-STAT proteins in the
            interferon-stimulated gene factor 3 transcription complex
  JOURNAL   Mol Cell Biol 16 (12), 6957-6964 (1996)
   PUBMED   8943351
REFERENCE   8  (residues 1 to 393)
  AUTHORS   Robertson,N.G., Khetarpal,U., Gutierrez-Espeleta,G.A., Bieber,F.R.
            and Morton,C.C.
  TITLE     Isolation of novel and known genes from a human fetal cochlear cDNA
            library using subtractive hybridization and differential screening
  JOURNAL   Genomics 23 (1), 42-50 (1994)
   PUBMED   7829101
REFERENCE   9  (residues 1 to 393)
  AUTHORS   David,M., Romero,G., Zhang,Z.Y., Dixon,J.E. and Larner,A.C.
  TITLE     In vitro activation of the transcription factor ISGF3 by interferon
            alpha involves a membrane-associated tyrosine phosphatase and
            tyrosine kinase
  JOURNAL   J Biol Chem 268 (9), 6593-6599 (1993)
   PUBMED   8454630
REFERENCE   10 (residues 1 to 393)
  AUTHORS   Veals,S.A., Schindler,C., Leonard,D., Fu,X.Y., Aebersold,R.,
            Darnell,J.E. Jr. and Levy,D.E.
  TITLE     Subunit of an alpha-interferon-responsive transcription factor is
            related to interferon regulatory factor and Myb families of
            DNA-binding proteins
  JOURNAL   Mol Cell Biol 12 (8), 3315-3324 (1992)
   PUBMED   1630447
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI919023.1, AL136295.3 and BI497082.1.
            
            On Nov 25, 2002 this sequence version replaced NP_006075.2.
            
            Summary: This gene encodes a member of the interferon regulatory
            factor (IRF) family, a group of transcription factors with diverse
            roles, including virus-mediated activation of interferon, and
            modulation of cell growth, differentiation, apoptosis, and immune
            system activity. Members of the IRF family are characterized by a
            conserved N-terminal DNA-binding domain containing tryptophan (W)
            repeats. Mutations in this gene result in Immunodeficiency 65.
            [provided by RefSeq, Jul 2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.559655.1,
                                           SRR1163658.135954.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000396864.8/ ENSP00000380073.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..393
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q12"
     Protein         1..393
                     /product="interferon regulatory factor 9 isoform 2"
                     /note="interferon-stimulated transcription factor 3, gamma
                     48kDa; interferon-stimulated transcription factor 3, gamma
                     (48kD); ISGF-3 gamma; ISGF3 p48 subunit;
                     interferon-stimulated gene factor 3 gamma; transcriptional
                     regulator ISGF3 subunit gamma; IFN-alpha-responsive
                     transcription factor subunit"
                     /calculated_mol_wt=43565
     Region          11..115
                     /region_name="IRF"
                     /note="Interferon regulatory factor transcription factor;
                     pfam00605"
                     /db_xref="CDD:459863"
     Site            order(44,83,85..86,89)
                     /site_type="other"
                     /note="DNA sequence recognition sites [nucleotide
                     binding]"
                     /db_xref="CDD:238051"
     Site            order(88..89,91,94)
                     /site_type="metal-binding"
                     /db_xref="CDD:238051"
     Region          120..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00978.1)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61179; propagated from
                     UniProtKB/Swiss-Prot (Q00978.1)"
     Region          163..202
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00978.1)"
     Region          217..383
                     /region_name="IRF-3"
                     /note="Interferon-regulatory factor 3; pfam10401"
                     /db_xref="CDD:463076"
     CDS             1..393
                     /gene="IRF9"
                     /gene_synonym="IRF-9; ISGF3; ISGF3G; p48"
                     /coded_by="NM_006084.5:76..1257"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS9615.1"
                     /db_xref="GeneID:10379"
                     /db_xref="HGNC:HGNC:6131"
                     /db_xref="MIM:147574"
ORIGIN      
        1 masgrarctr klrnwvveqv esgqfpgvcw ddtaktmfri pwkhagkqdf redqdaaffk
       61 awaifkgkyk egdtggpavw ktrlrcalnk ssefkevper grmdvaepyk vyqllppgiv
      121 sgqpgtqkvp skrqhssvss erkeeedamq nctlspsvlq dslnneeega sggavhsdig
      181 ssssssspep qevtdtteap fqgdqrslef llppepdysl lltfiyngrv vgeaqvqsld
      241 crlvaepsgs essmeqvlfp kpgpleptqr llsqlergil vasnprglfv qrlcpipisw
      301 napqappgpg phllpsnecv elfrtayfcr dlvryfqglg pppkfqvtln fweeshgssh
      361 tpqnlitvkm eqafarylle qtpeqqaail slv
//
LOCUS       NP_001310462             538 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing regulatory glutamine/lysine-rich protein 1 isoform f [Homo
            sapiens].
ACCESSION   NP_001310462 XP_011541472
VERSION     NP_001310462.1
DBSOURCE    REFSEQ: accession NM_001323533.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 538)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 538)
  AUTHORS   Chang,C., Rajasekaran,M., Qiao,Y., Dong,H., Wang,Y., Xia,H.,
            Deivasigamani,A., Wu,M., Sekar,K., Gao,H., Sun,M., Niu,Y., Li,Q.,
            Tao,L., Yan,Z., Wang,M., Chen,S., Zhao,S., Chen,D., Li,L., Yang,F.,
            Gao,H., Chen,B., Su,L., Xu,L., Chen,Y., Seshachalam,V.P., Chen,G.,
            Gunaratne,J., Hong,W., Shi,J., Chen,G., Grierson,D.S., Chabot,B.,
            Xie,T., Hui,K.M. and Chen,J.
  TITLE     The aberrant upregulation of exon 10-inclusive SREK1 through SRSF10
            acts as an oncogenic driver in human hepatocellular carcinoma
  JOURNAL   Nat Commun 13 (1), 1363 (2022)
   PUBMED   35296659
  REMARK    GeneRIF: The aberrant upregulation of exon 10-inclusive SREK1
            through SRSF10 acts as an oncogenic driver in human hepatocellular
            carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 538)
  AUTHORS   Abudureheman,Z., Li,L., Zhong,X., Xu,J., Gong,H., Yilamujiang,S.,
            Ren,J., Xie,C., Zheng,A., Tuerxun,D., Abudukadeer,A., Aini,P.,
            Xu,A. and Zou,X.
  TITLE     The rs74794265 SNP of the SREK1 Gene is Associated with COPD in
            Kashi, China
  JOURNAL   Int J Chron Obstruct Pulmon Dis 16, 2631-2636 (2021)
   PUBMED   34556983
  REMARK    GeneRIF: The rs74794265 SNP of the SREK1 Gene is Associated with
            COPD in Kashi, China.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 538)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 538)
  AUTHORS   Buljan,M., Ciuffa,R., van Drogen,A., Vichalkovski,A., Mehnert,M.,
            Rosenberger,G., Lee,S., Varjosalo,M., Pernas,L.E., Spegg,V.,
            Snijder,B., Aebersold,R. and Gstaiger,M.
  TITLE     Kinase Interaction Network Expands Functional and Disease Roles of
            Human Kinases
  JOURNAL   Mol Cell 79 (3), 504-520 (2020)
   PUBMED   32707033
REFERENCE   6  (residues 1 to 538)
  AUTHORS   Heese,K., Fujita,M., Akatsu,H., Yamamoto,T., Kosaka,K., Nagai,Y.
            and Sawada,T.
  TITLE     The splicing regulatory protein p18SRP is down-regulated in
            Alzheimer's disease brain
  JOURNAL   J Mol Neurosci 24 (2), 269-276 (2004)
   PUBMED   15456940
  REMARK    GeneRIF: p18SRP is a lysine-rich zinc finger domain-containing
            protein that interacts with the serine-arginine-rich splicing
            regulatory protein SRrp86; it is downregulated in brain of
            Alzheimer disease patients.
REFERENCE   7  (residues 1 to 538)
  AUTHORS   Li,J., Hawkins,I.C., Harvey,C.D., Jennings,J.L., Link,A.J. and
            Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 and its interacting
            proteins
  JOURNAL   Mol Cell Biol 23 (21), 7437-7447 (2003)
   PUBMED   14559993
REFERENCE   8  (residues 1 to 538)
  AUTHORS   Li,J., Barnard,D.C. and Patton,J.G.
  TITLE     A unique glutamic acid-lysine (EK) domain acts as a splicing
            inhibitor
  JOURNAL   J Biol Chem 277 (42), 39485-39492 (2002)
   PUBMED   12183448
  REMARK    GeneRIF: the unique glutamic acid-lysine domain of SRrp86 plays a
            modulatory role controlling serine-arginine domain function
REFERENCE   9  (residues 1 to 538)
  AUTHORS   Barnard,D.C., Li,J., Peng,R. and Patton,J.G.
  TITLE     Regulation of alternative splicing by SRrp86 through coactivation
            and repression of specific SR proteins
  JOURNAL   RNA 8 (4), 526-533 (2002)
   PUBMED   11991645
  REMARK    GeneRIF: SRrp86 can activate SRp20 and repress SC35 in a
            dose-dependent manner both in vitro and in vivo
REFERENCE   10 (residues 1 to 538)
  AUTHORS   Barnard,D.C. and Patton,J.G.
  TITLE     Identification and characterization of a novel serine-arginine-rich
            splicing regulatory protein
  JOURNAL   Mol Cell Biol 20 (9), 3049-3057 (2000)
   PUBMED   10757789
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC025442.6 and AC008772.6.
            
            On Apr 22, 2016 this sequence version replaced XP_011541472.1.
            
            Summary: This gene encodes a member of a family of
            serine/arginine-rich (SR) splicing proteins containing RNA
            recognition motif (RRM) domains. The encoded protein interacts with
            other SR proteins to modulate splice site selection. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Jul 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2195613.1,
                                           SRR1803616.77060.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..538
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q12.3"
     Protein         1..538
                     /product="splicing regulatory glutamine/lysine-rich
                     protein 1 isoform f"
                     /note="splicing factor, arginine/serine-rich 12;
                     serine-arginine-rich splicing regulatory protein 508;
                     serine/arginine-rich-splicing regulatory protein 86;
                     splicing regulatory glutamine/lysine-rich protein 1;
                     splicing regulatory glutamic acid/lysine-rich protein 1"
                     /calculated_mol_wt=61466
     Region          20..99
                     /region_name="RRM1_SREK1"
                     /note="RNA recognition motif 1 (RRM1) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12519"
                     /db_xref="CDD:409941"
     Region          178..263
                     /region_name="RRM2_SREK1"
                     /note="RNA recognition motif 2 (RRM2) found in splicing
                     regulatory glutamine/lysine-rich protein 1 (SREK1) and
                     similar proteins; cd12260"
                     /db_xref="CDD:409705"
     CDS             1..538
                     /gene="SREK1"
                     /gene_synonym="SFRS12; SRrp508; SRrp86"
                     /coded_by="NM_001323533.2:78..1694"
                     /note="isoform f is encoded by transcript variant 7"
                     /db_xref="GeneID:140890"
                     /db_xref="HGNC:HGNC:17882"
                     /db_xref="MIM:609268"
ORIGIN      
        1 mnsgggfglg lgfgltptsv iqvtnlssav tseqmrtlfs flgeieelrl yppdnaplaf
       61 sskvcyvkfr dpssvgvaqh ltntvfidra livvpcaegk ipeeskalsl lapaptmtsl
      121 mpgagllpip tpnplttlgv slsslgaipa aaldpniatl geipqpplmg nvdpskidei
      181 rrtvyvgnln sqtttadqll effkqvgevk fvrmagdetq ptrfafvefa dqnsvprala
      241 fngvmfgdrp lkinhsnnai vkppemtpqa aakeleevmk rvreaqsfis aaiepesgks
      301 nerkggrsrs htrsksrsss kshsrrkrsq skhrsrshnr srsrqkdrrr sksphkkrsk
      361 srerrksrsr shsrdkrkdt rekikekerv kekdrekere rekerekeke rgknkdrdke
      421 rekdrekdke kdrerereke hekdrdkeke keqdkekere kdrskeidek rkkdkksrtp
      481 prsynasrrs rsssrerrrr rsrsssrspr tsktikrkss rspsprrrks tiknqiqv
//
LOCUS       NP_001304097              64 aa            linear   PRI 20-NOV-2025
DEFINITION  small nuclear ribonucleoprotein G isoform e [Homo sapiens].
ACCESSION   NP_001304097
VERSION     NP_001304097.1
DBSOURCE    REFSEQ: accession NM_001317168.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 64)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 64)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 64)
  AUTHORS   Schneider,S., Brandina,I., Peter,D., Lagad,S., Fraudeau,A.,
            Portell-Montserrat,J., Tholen,J., Zhao,J. and Galej,W.P.
  TITLE     Structure of the human 20S U5 snRNP
  JOURNAL   Nat Struct Mol Biol 31 (5), 752-756 (2024)
   PUBMED   38467877
REFERENCE   4  (residues 1 to 64)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   5  (residues 1 to 64)
  AUTHORS   Zhang,Z., Kumar,V., Dybkov,O., Will,C.L., Urlaub,H., Stark,H. and
            Luhrmann,R.
  TITLE     Cryo-EM analyses of dimerized spliceosomes provide new insights
            into the functions of B complex proteins
  JOURNAL   EMBO J 43 (6), 1065-1088 (2024)
   PUBMED   38383864
REFERENCE   6  (residues 1 to 64)
  AUTHORS   Fury,M.G., Zhang,W., Christodoulopoulos,I. and Zieve,G.W.
  TITLE     Multiple protein: protein interactions between the snRNP common
            core proteins
  JOURNAL   Exp Cell Res 237 (1), 63-69 (1997)
   PUBMED   9417867
REFERENCE   7  (residues 1 to 64)
  AUTHORS   Liu,Q., Fischer,U., Wang,F. and Dreyfuss,G.
  TITLE     The spinal muscular atrophy disease gene product, SMN, and its
            associated protein SIP1 are in a complex with spliceosomal snRNP
            proteins
  JOURNAL   Cell 90 (6), 1013-1021 (1997)
   PUBMED   9323129
REFERENCE   8  (residues 1 to 64)
  AUTHORS   Plessel,G., Luhrmann,R. and Kastner,B.
  TITLE     Electron microscopy of assembly intermediates of the snRNP core:
            morphological similarities between the RNA-free (E.F.G) protein
            heteromer and the intact snRNP core
  JOURNAL   J Mol Biol 265 (2), 87-94 (1997)
   PUBMED   9020971
REFERENCE   9  (residues 1 to 64)
  AUTHORS   Hermann,H., Fabrizio,P., Raker,V.A., Foulaki,K., Hornig,H.,
            Brahms,H. and Luhrmann,R.
  TITLE     snRNP Sm proteins share two evolutionarily conserved sequence
            motifs which are involved in Sm protein-protein interactions
  JOURNAL   EMBO J 14 (9), 2076-2088 (1995)
   PUBMED   7744013
REFERENCE   10 (residues 1 to 64)
  AUTHORS   Heinrichs,V., Hackl,W. and Luhrmann,R.
  TITLE     Direct binding of small nuclear ribonucleoprotein G to the Sm site
            of small nuclear RNA. Ultraviolet light cross-linking of protein G
            to the AAU stretch within the Sm site (AAUUUGUGG) of U1 small
            nuclear ribonucleoprotein reconstituted in vitro
  JOURNAL   J Mol Biol 227 (1), 15-28 (1992)
   PUBMED   1387914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY168189.1, BC035103.1 and
            AI742299.1.
            
            Summary: The protein encoded by this gene is a component of the U1,
            U2, U4, and U5 small nuclear ribonucleoprotein complexes,
            precursors of the spliceosome. The encoded protein may also be a
            part of the U7 small nuclear ribonucleoprotein complex, which
            participates in the processing of the 3' end of histone
            transcripts. Several transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Nov
            2015].
            
            Transcript Variant: This variant (5) uses an alternate exon in
            place of the first exon compared to variant 1. The resulting
            isoform (e) is shorter at the N-terminus compared to isoform a.
            Variants 5 and 6 both encode the same isoform (e).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC035103.1, AI268598.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..64
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13.3"
     Protein         1..64
                     /product="small nuclear ribonucleoprotein G isoform e"
                     /EC_number="1.8.1.4"
                     /note="small nuclear ribonucleoprotein G; snRNP-G; sm
                     protein G"
                     /calculated_mol_wt=6970
     Region          1..62
                     /region_name="Sm_G"
                     /note="Sm protein G; cd01719"
                     /db_xref="CDD:212466"
     Site            order(5..11,13..25,27..31)
                     /site_type="other"
                     /note="Sm1 motif"
                     /db_xref="CDD:212466"
     Site            order(8,13,26,47,49..50,52,55..59,61)
                     /site_type="other"
                     /note="heptamer interface [polypeptide binding]"
                     /db_xref="CDD:212466"
     Site            order(25,27,51,53)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:212466"
     Site            47..58
                     /site_type="other"
                     /note="Sm2 motif"
                     /db_xref="CDD:212466"
     CDS             1..64
                     /gene="SNRPG"
                     /gene_synonym="Sm-G; SMG"
                     /coded_by="NM_001317168.1:789..983"
                     /note="isoform e is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82461.1"
                     /db_xref="GeneID:6637"
                     /db_xref="HGNC:HGNC:11163"
                     /db_xref="MIM:603542"
ORIGIN      
        1 mdkklslkln ggrhvqgilr gfdpfmnlvi decvematsg qqnnigmvvi rgnsiimlea
       61 lerv
//
LOCUS       NP_001300948             243 aa            linear   PRI 20-NOV-2025
DEFINITION  copine-5 isoform d [Homo sapiens].
ACCESSION   NP_001300948
VERSION     NP_001300948.1
DBSOURCE    REFSEQ: accession NM_001314019.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Zhu,P., Qian,T., Si,C., Liu,Y., Cui,L., Huang,W., Fu,L., Deng,C.
            and Zeng,T.
  TITLE     High expression of CPNE5 and CPNE9 predicts positive prognosis in
            multiple myeloma
  JOURNAL   Cancer Biomark 31 (1), 77-85 (2021)
   PUBMED   33780365
  REMARK    GeneRIF: High expression of CPNE5 and CPNE9 predicts positive
            prognosis in multiple myeloma.
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Umeda,S., Kanda,M., Koike,M., Tanaka,H., Miwa,T., Tanaka,C.,
            Kobayashi,D., Suenaga,M., Hayashi,M., Yamada,S., Nakayama,G. and
            Kodera,Y.
  TITLE     Copine 5 expression predicts prognosis following curative resection
            of esophageal squamous cell carcinoma
  JOURNAL   Oncol Rep 40 (6), 3772-3780 (2018)
   PUBMED   30272363
  REMARK    GeneRIF: Data revealed that CPNE5 mRNA expression was significantly
            lower in ESCC tissues and cell lines and correlated with
            significantly shorter overall survival. Multivariable analysis
            identified low CPNE5 expression to be an independent prognostic
            factor of OS. Analysis of recurrence patterns revealed that
            significantly more patients with local recurrence expressed lower
            levels of CPNE5 mRNA.
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Wang,K.S., Zuo,L., Pan,Y., Xie,C. and Luo,X.
  TITLE     Genetic variants in the CPNE5 gene are associated with alcohol
            dependence and obesity in Caucasian populations
  JOURNAL   J Psychiatr Res 71, 1-7 (2015)
   PUBMED   26522866
  REMARK    GeneRIF: Results provide the first evidence of genetic variants in
            the CPNE5 gene influencing both alcohol dependence and obesity
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Navarini,A.A., Simpson,M.A., Weale,M., Knight,J., Carlavan,I.,
            Reiniche,P., Burden,D.A., Layton,A., Bataille,V., Allen,M.,
            Pleass,R., Pink,A., Creamer,D., English,J., Munn,S., Walton,S.,
            Willis,C., Deret,S., Voegel,J.J., Spector,T., Smith,C.H.,
            Trembath,R.C. and Barker,J.N.
  CONSRTM   Acne Genetic Study Group
  TITLE     Genome-wide association study identifies three novel susceptibility
            loci for severe Acne vulgaris
  JOURNAL   Nat Commun 5, 4020 (2014)
   PUBMED   24927181
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   den Hoed,M., Eijgelsheim,M., Esko,T., Brundel,B.J., Peal,D.S.,
            Evans,D.M., Nolte,I.M., Segre,A.V., Holm,H., Handsaker,R.E.,
            Westra,H.J., Johnson,T., Isaacs,A., Yang,J., Lundby,A., Zhao,J.H.,
            Kim,Y.J., Go,M.J., Almgren,P., Bochud,M., Boucher,G.,
            Cornelis,M.C., Gudbjartsson,D., Hadley,D., van der Harst,P.,
            Hayward,C., den Heijer,M., Igl,W., Jackson,A.U., Kutalik,Z.,
            Luan,J., Kemp,J.P., Kristiansson,K., Ladenvall,C., Lorentzon,M.,
            Montasser,M.E., Njajou,O.T., O'Reilly,P.F., Padmanabhan,S., St
            Pourcain,B., Rankinen,T., Salo,P., Tanaka,T., Timpson,N.J.,
            Vitart,V., Waite,L., Wheeler,W., Zhang,W., Draisma,H.H.,
            Feitosa,M.F., Kerr,K.F., Lind,P.A., Mihailov,E., Onland-Moret,N.C.,
            Song,C., Weedon,M.N., Xie,W., Yengo,L., Absher,D., Albert,C.M.,
            Alonso,A., Arking,D.E., de Bakker,P.I., Balkau,B., Barlassina,C.,
            Benaglio,P., Bis,J.C., Bouatia-Naji,N., Brage,S., Chanock,S.J.,
            Chines,P.S., Chung,M., Darbar,D., Dina,C., Dorr,M., Elliott,P.,
            Felix,S.B., Fischer,K., Fuchsberger,C., de Geus,E.J., Goyette,P.,
            Gudnason,V., Harris,T.B., Hartikainen,A.L., Havulinna,A.S.,
            Heckbert,S.R., Hicks,A.A., Hofman,A., Holewijn,S.,
            Hoogstra-Berends,F., Hottenga,J.J., Jensen,M.K., Johansson,A.,
            Junttila,J., Kaab,S., Kanon,B., Ketkar,S., Khaw,K.T., Knowles,J.W.,
            Kooner,A.S., Kors,J.A., Kumari,M., Milani,L., Laiho,P.,
            Lakatta,E.G., Langenberg,C., Leusink,M., Liu,Y., Luben,R.N.,
            Lunetta,K.L., Lynch,S.N., Markus,M.R., Marques-Vidal,P., Mateo
            Leach,I., McArdle,W.L., McCarroll,S.A., Medland,S.E., Miller,K.A.,
            Montgomery,G.W., Morrison,A.C., Muller-Nurasyid,M., Navarro,P.,
            Nelis,M., O'Connell,J.R., O'Donnell,C.J., Ong,K.K., Newman,A.B.,
            Peters,A., Polasek,O., Pouta,A., Pramstaller,P.P., Psaty,B.M.,
            Rao,D.C., Ring,S.M., Rossin,E.J., Rudan,D., Sanna,S., Scott,R.A.,
            Sehmi,J.S., Sharp,S., Shin,J.T., Singleton,A.B., Smith,A.V.,
            Soranzo,N., Spector,T.D., Stewart,C., Stringham,H.M., Tarasov,K.V.,
            Uitterlinden,A.G., Vandenput,L., Hwang,S.J., Whitfield,J.B.,
            Wijmenga,C., Wild,S.H., Willemsen,G., Wilson,J.F., Witteman,J.C.,
            Wong,A., Wong,Q., Jamshidi,Y., Zitting,P., Boer,J.M., Boomsma,D.I.,
            Borecki,I.B., van Duijn,C.M., Ekelund,U., Forouhi,N.G., Froguel,P.,
            Hingorani,A., Ingelsson,E., Kivimaki,M., Kronmal,R.A., Kuh,D.,
            Lind,L., Martin,N.G., Oostra,B.A., Pedersen,N.L., Quertermous,T.,
            Rotter,J.I., van der Schouw,Y.T., Verschuren,W.M., Walker,M.,
            Albanes,D., Arnar,D.O., Assimes,T.L., Bandinelli,S., Boehnke,M., de
            Boer,R.A., Bouchard,C., Caulfield,W.L., Chambers,J.C., Curhan,G.,
            Cusi,D., Eriksson,J., Ferrucci,L., van Gilst,W.H., Glorioso,N., de
            Graaf,J., Groop,L., Gyllensten,U., Hsueh,W.C., Hu,F.B.,
            Huikuri,H.V., Hunter,D.J., Iribarren,C., Isomaa,B., Jarvelin,M.R.,
            Jula,A., Kahonen,M., Kiemeney,L.A., van der Klauw,M.M.,
            Kooner,J.S., Kraft,P., Iacoviello,L., Lehtimaki,T., Lokki,M.L.,
            Mitchell,B.D., Navis,G., Nieminen,M.S., Ohlsson,C., Poulter,N.R.,
            Qi,L., Raitakari,O.T., Rimm,E.B., Rioux,J.D., Rizzi,F., Rudan,I.,
            Salomaa,V., Sever,P.S., Shields,D.C., Shuldiner,A.R., Sinisalo,J.,
            Stanton,A.V., Stolk,R.P., Strachan,D.P., Tardif,J.C.,
            Thorsteinsdottir,U., Tuomilehto,J., van Veldhuisen,D.J.,
            Virtamo,J., Viikari,J., Vollenweider,P., Waeber,G., Widen,E.,
            Cho,Y.S., Olsen,J.V., Visscher,P.M., Willer,C., Franke,L.,
            Erdmann,J., Thompson,J.R., Pfeufer,A., Sotoodehnia,N.,
            Newton-Cheh,C., Ellinor,P.T., Stricker,B.H., Metspalu,A.,
            Perola,M., Beckmann,J.S., Smith,G.D., Stefansson,K., Wareham,N.J.,
            Munroe,P.B., Sibon,O.C., Milan,D.J., Snieder,H., Samani,N.J. and
            Loos,R.J.
  CONSRTM   Global BPgen Consortium; CARDIoGRAM Consortium; PR GWAS Consortium;
            QRS GWAS Consortium; QT-IGC Consortium; CHARGE-AF Consortium
  TITLE     Identification of heart rate-associated loci and their effects on
            cardiac conduction and rhythm disorders
  JOURNAL   Nat Genet 45 (6), 621-631 (2013)
   PUBMED   23583979
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Tripodis,N., Mason,R., Humphray,S.J., Davies,A.F., Herberg,J.A.,
            Trowsdale,J., Nizetic,D., Senger,G. and Ragoussis,J.
  TITLE     Physical map of human 6p21.2-6p21.3: region flanking the
            centromeric end of the major histocompatibility complex
  JOURNAL   Genome Res 8 (6), 631-643 (1998)
   PUBMED   9647638
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Creutz,C.E., Tomsig,J.L., Snyder,S.L., Gautier,M.C., Skouri,F.,
            Beisson,J. and Cohen,J.
  TITLE     The copines, a novel class of C2 domain-containing,
            calcium-dependent, phospholipid-binding proteins conserved from
            Paramecium to humans
  JOURNAL   J Biol Chem 273 (3), 1393-1402 (1998)
   PUBMED   9430674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC053872.1, BC036840.1 and
            Z85996.1.
            
            Summary: Calcium-dependent membrane-binding proteins may regulate
            molecular events at the interface of the cell membrane and
            cytoplasm. This gene is one of several genes that encode a
            calcium-dependent protein containing two N-terminal type II C2
            domains and an integrin A domain-like sequence in the C-terminus.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. More variants may
            exist, but their full-length natures could not be determined.
            [provided by RefSeq, Sep 2015].
            
            Transcript Variant: This variant (4) lacks several 5' exons and
            contains an alternate 5' terminal exon and internal exon compared
            to variant 1. The resulting isoform (d) is shorter at the
            N-terminus compared to isoform a. Variants 4, 5, and 6 all encode
            the same isoform (d).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036840.1, SRR1163658.498319.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2"
     Protein         1..243
                     /product="copine-5 isoform d"
                     /note="copine V"
                     /calculated_mol_wt=26160
     Region          1..212
                     /region_name="Copine"
                     /note="pfam07002"
                     /db_xref="CDD:462064"
     CDS             1..243
                     /gene="CPNE5"
                     /gene_synonym="COPN5; CPN5"
                     /coded_by="NM_001314019.2:353..1084"
                     /note="isoform d is encoded by transcript variant 4"
                     /db_xref="GeneID:57699"
                     /db_xref="HGNC:HGNC:2318"
                     /db_xref="MIM:604209"
ORIGIN      
        1 mspyqlnaya laltavgeii qhydsdkmfp algfgaklpp dgrvshefpl ngnqenpscc
       61 gidgileayh rslrtvqlyg ptnfapvvth varnaaavqd gsqysvllii tdgvisdmaq
      121 tkeaivnaak lpmsiiivgv gqaefdamve ldgddvriss rgklaerdiv qfvpfrdyvd
      181 rtgnhvlsma rlardvlaei pdqlvsymka qgirprpppa apthspsqsp artppasplh
      241 thi
//
LOCUS       NP_001308506             491 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 17 [Homo sapiens].
ACCESSION   NP_001308506
VERSION     NP_001308506.1
DBSOURCE    REFSEQ: accession NM_001321577.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 491)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Transcript Variant: This variant (18) encodes isoform (17, also
            known as delta 10).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.229085.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..491
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 17"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=55445
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          359..486
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..491
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321577.2:671..2146"
                     /note="isoform 17 is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS93601.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 leavlhchqm gvvhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaksll kkpdgvkepq ttvihnpdgn kestessntt iededvkark
      361 qeiikvteql ieainngdfe aytkicdpgl tafepealgn lvegmdfhrf yfenalsksn
      421 kpihtiilnp hvhlvgddaa ciayirltqy mdgsgmpktm qseetrvwhr rdgkwqnvhf
      481 hrsgsptvpi n
//
LOCUS       NP_001334637             331 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001334637
VERSION     NP_001334637.1
DBSOURCE    REFSEQ: accession NM_001347708.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Demontis,D., Rajagopal,V.M., Thorgeirsson,T.E., Als,T.D., Grove,J.,
            Leppala,K., Gudbjartsson,D.F., Pallesen,J., Hjorthoj,C.,
            Reginsson,G.W., Tyrfingsson,T., Runarsdottir,V., Qvist,P.,
            Christensen,J.H., Bybjerg-Grauholm,J., Baekvad-Hansen,M.,
            Huckins,L.M., Stahl,E.A., Timmermann,A., Agerbo,E., Hougaard,D.M.,
            Werge,T., Mors,O., Mortensen,P.B., Nordentoft,M., Daly,M.J.,
            Stefansson,H., Stefansson,K., Nyegaard,M. and Borglum,A.D.
  TITLE     Genome-wide association study implicates CHRNA2 in cannabis use
            disorder
  JOURNAL   Nat Neurosci 22 (7), 1066-1074 (2019)
   PUBMED   31209380
  REMARK    GeneRIF: The index variant (rs56372821) is a strong expression
            quantitative trait locus for CHRNA2; analyses of the genetically
            regulated gene expression identified a significant association of
            CHRNA2 expression with cannabis use disorder (CUD) in brain tissue.
            At the polygenic level, analyses revealed a significant decrease in
            the risk of CUD with increased load of variants associated with
            cognitive performance.
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Wang,M., Liu,D., Schwender,H., Wang,H., Wang,P., Zhou,Z., Li,J.,
            Wu,T., Zhu,H. and Beaty,T.H.
  TITLE     Evaluating the effect of nicotinic cholinergic receptor genes on
            the risk of nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Oral Dis 24 (6), 1068-1072 (2018)
   PUBMED   29688589
  REMARK    GeneRIF: In our analysis, we found one pair of SNPs in CHRNA1 and
            CHRNA7, plus one pair of SNPs in CHRNA2 and CHRNA3 reached
            corrected significance in tests for GxG interaction. Our study
            suggested evidence of interactions between CHRNs in controlling the
            risk of NSCL/P.
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Jun,H., Yu,H., Gong,J., Jiang,J., Qiao,X., Perkey,E., Kim,D.I.,
            Emont,M.P., Zestos,A.G., Cho,J.S., Liu,J., Kennedy,R.T.,
            Maillard,I., Xu,X.Z.S. and Wu,J.
  TITLE     An immune-beige adipocyte communication via nicotinic acetylcholine
            receptor signaling
  JOURNAL   Nat Med 24 (6), 814-822 (2018)
   PUBMED   29785025
  REMARK    GeneRIF: These results reveal a beige-selective immune-adipose
            interaction mediated through CHRNA2 and identify a novel function
            of nicotinic acetylcholine receptors in energy metabolism.
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Kouvatsos,N., Giastas,P., Chroni-Tzartou,D., Poulopoulou,C. and
            Tzartos,S.J.
  TITLE     Crystal structure of a human neuronal nAChR extracellular domain in
            pentameric assembly: Ligand-bound alpha2 homopentamer
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9635-9640 (2016)
   PUBMED   27493220
  REMARK    GeneRIF: A crystal structure of a human neuronal CHRNA2
            extracellular domain in pentameric assembly has been reported.
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Trivisano,M., Terracciano,A., Milano,T., Cappelletti,S.,
            Pietrafusa,N., Bertini,E.S., Vigevano,F. and Specchio,N.
  TITLE     Mutation of CHRNA2 in a family with benign familial infantile
            seizures: Potential role of nicotinic acetylcholine receptor in
            various phenotypes of epilepsy
  JOURNAL   Epilepsia 56 (5), e53-e57 (2015)
   PUBMED   25847220
  REMARK    GeneRIF: a heterozygous single-nucleotide substitution in CHRNA2
            gene (c.1126 C>T; p. Arg376Trp) in subjects with benign familial
            infantile seizures
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Garcia-Colunga,J. and Miledi,R.
  TITLE     Effects of serotonergic agents on neuronal nicotinic acetylcholine
            receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (7), 2919-2923 (1995)
   PUBMED   7708749
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Wood,S., Schertzer,M. and Yaremko,M.L.
  TITLE     Identification of the human neuronal nicotinic cholinergic alpha 2
            receptor locus, (CHRNA2), within an 8p21 mapped locus, by sequence
            homology with rat DNA
  JOURNAL   Somat Cell Mol Genet 21 (2), 147-150 (1995)
   PUBMED   7570187
REFERENCE   9  (residues 1 to 331)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
REFERENCE   10 (residues 1 to 331)
  AUTHORS   Anand,R. and Lindstrom,J.
  TITLE     Chromosomal localization of seven neuronal nicotinic acetylcholine
            receptor subunit genes in humans
  JOURNAL   Genomics 13 (4), 962-967 (1992)
   PUBMED   1505988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA407151.1, AK314787.1 and
            AF311103.5.
            
            Summary: Nicotinic acetylcholine receptors (nAChRs) are
            ligand-gated ion channels formed by a pentameric arrangement of
            alpha and beta subunits to create distinct muscle and neuronal
            receptors. Neuronal receptors are found throughout the peripheral
            and central nervous system where they are involved in fast synaptic
            transmission. This gene encodes an alpha subunit that is widely
            expressed in the brain. The proposed structure for nAChR subunits
            is a conserved N-terminal extracellular domain followed by three
            conserved transmembrane domains, a variable cytoplasmic loop, a
            fourth conserved transmembrane domain, and a short C-terminal
            extracellular region. Mutations in this gene cause autosomal
            dominant nocturnal frontal lobe epilepsy type 4. Single nucleotide
            polymorphisms (SNPs) in this gene have been associated with
            nicotine dependence. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (6), as well as variant 5, encodes
            isoform 4.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK314787.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465411 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..331
                     /product="neuronal acetylcholine receptor subunit alpha-2
                     isoform 4"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     2 (neuronal); cholinergic receptor, nicotinic alpha 2;
                     neuronal acetylcholine receptor subunit alpha-2;
                     acetylcholine receptor, nicotinic, alpha 2 (neuronal);
                     cholinergic receptor, nicotinic, alpha 2 (neuronal);
                     nicotinic acetylcholine receptor subunit alpha-2"
                     /calculated_mol_wt=37244
     Region          <1..67
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Region          74..322
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     CDS             1..331
                     /gene="CHRNA2"
                     /coded_by="NM_001347708.2:1036..2031"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="GeneID:1135"
                     /db_xref="HGNC:HGNC:1956"
                     /db_xref="MIM:118502"
ORIGIN      
        1 mkfgswtydk akidleqmeq tvdlkdywes gewaivnatg tynskkydcc aeiypdvtya
       61 fvirrlplfy tinliipcll iscltvlvfy lpsdcgekit lcisvllslt vfllliteii
      121 pstslvipli geyllftmif vtlsivitvf vlnvhhrsps thtmphwvrg allgcvprwl
      181 lmnrppppve lchplrlkls psyhwlesnv daeerevvve eedrwacagh vapsvgtlcs
      241 hghlhsgasg pkaeallqeg elllsphmqk alegvhyiad hlrsedadss vkedwkyvam
      301 vidriflwlf iivcflgtig lflppflagm i
//
LOCUS       NP_060633                304 aa            linear   PRI 20-NOV-2025
DEFINITION  dnaJ homolog subfamily C member 17 [Homo sapiens].
ACCESSION   NP_060633
VERSION     NP_060633.1
DBSOURCE    REFSEQ: accession NM_018163.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Nettore,I.C., Desiderio,S., De Nisco,E., Cacace,V., Albano,L.,
            Improda,N., Ungaro,P., Salerno,M., Colao,A. and Macchia,P.E.
  TITLE     High-resolution melting analysis (HRM) for mutational screening of
            Dnajc17 gene in patients affected by thyroid dysgenesis
  JOURNAL   J Endocrinol Invest 41 (6), 711-717 (2018)
   PUBMED   29159607
  REMARK    GeneRIF: DNAJC17 mutations are not frequently present in patients
            with thyroid dysgenesis.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Pascarella,A., Ferrandino,G., Credendino,S.C., Moccia,C.,
            D'Angelo,F., Miranda,B., D'Ambrosio,C., Bielli,P., Spadaro,O.,
            Ceccarelli,M., Scaloni,A., Sette,C., De Felice,M., De Vita,G. and
            Amendola,E.
  TITLE     DNAJC17 is localized in nuclear speckles and interacts with
            splicing machinery components
  JOURNAL   Sci Rep 8 (1), 7794 (2018)
   PUBMED   29773831
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Patel,N., Aldahmesh,M.A., Alkuraya,H., Anazi,S., Alsharif,H.,
            Khan,A.O., Sunker,A., Al-Mohsen,S., Abboud,E.B., Nowilaty,S.R.,
            Alowain,M., Al-Zaidan,H., Al-Saud,B., Alasmari,A.,
            Abdel-Salam,G.M., Abouelhoda,M., Abdulwahab,F.M., Ibrahim,N.,
            Naim,E., Al-Younes,B., E AlMostafa,A., AlIssa,A., Hashem,M.,
            Buzovetsky,O., Xiong,Y., Monies,D., Altassan,N., Shaheen,R.,
            Al-Hazzaa,S.A. and Alkuraya,F.S.
  TITLE     Expanding the clinical, allelic, and locus heterogeneity of retinal
            dystrophies
  JOURNAL   Genet Med 18 (6), 554-562 (2016)
   PUBMED   26355662
  REMARK    GeneRIF: Our study expands the clinical and allelic spectrum of
            known Retinal dystrophies genes, and reveals AGBL5, CDH16, and
            DNAJC17 as novel disease candidates.
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA341962.1, AK001496.1, AA834211.1 and AC012476.8.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853567.9929.1,
                                           SRR11853563.10984.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000220496.9/ ENSP00000220496.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.1"
     Protein         1..304
                     /product="dnaJ homolog subfamily C member 17"
                     /note="DnaJ (Hsp40) homolog, subfamily C, member 17"
                     /calculated_mol_wt=34556
     Region          11..73
                     /region_name="DnaJ"
                     /note="DnaJ domain; pfam00226"
                     /db_xref="CDD:395170"
     Site            order(39..41,50,53..54,57..58)
                     /site_type="other"
                     /note="HSP70 interaction site [polypeptide binding]"
                     /db_xref="CDD:99751"
     Region          79..145
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NVM6.1)"
     Site            112
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NVM6.1)"
     Region          184..247
                     /region_name="RRM_DNAJC17"
                     /note="RNA recognition motif (RRM) found in the DnaJ
                     homolog subfamily C member 17; cd12429"
                     /db_xref="CDD:409863"
     Site            264
                     /site_type="methylation"
                     /note="N6-methyllysine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9NVM6.1)"
     CDS             1..304
                     /gene="DNAJC17"
                     /coded_by="NM_018163.3:28..942"
                     /db_xref="CCDS:CCDS10065.1"
                     /db_xref="GeneID:55192"
                     /db_xref="HGNC:HGNC:25556"
                     /db_xref="MIM:616844"
ORIGIN      
        1 mavtkellqm dlyallgiee kaadkevkka yrqkalschp dknpdnpraa elfhqlsqal
       61 evltdaaara aydkvrkakk qaaertqkld ekrkkvkldl earerqaqaq eseeeeesrs
      121 trtleqeier lreegsrqle eqqrlireqi rqerdqrlrg kaentegqgt pklklkwkck
      181 kedeskggys kdvllrllqk ygevlnlvls skkpgtavve fatvkaaela vqnevglvdn
      241 plkiswlegq pqdavgrshs glskgsvlse rdyeslvmmr mrqaaerqql iarmqqedqe
      301 gppt
//
LOCUS       NP_061981                520 aa            linear   PRI 20-NOV-2025
DEFINITION  nonsense-mediated mRNA decay factor SMG9 [Homo sapiens].
ACCESSION   NP_061981
VERSION     NP_061981.2
DBSOURCE    REFSEQ: accession NM_019108.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Rahikkala,E., Urpa,L., Ghimire,B., Topa,H., Kurki,M.I., Koskela,M.,
            Airavaara,M., Hamalainen,E., Pylkas,K., Korkko,J., Savolainen,H.,
            Suoranta,A., Bertoli-Avella,A., Rolfs,A., Mattila,P., Daly,M.,
            Palotie,A., Pietilainen,O., Moilanen,J. and Kuismin,O.
  TITLE     A novel variant in SMG9 causes intellectual disability, confirming
            a role for nonsense-mediated decay components in neurocognitive
            development
  JOURNAL   Eur J Hum Genet 30 (5), 619-627 (2022)
   PUBMED   35087184
  REMARK    GeneRIF: A novel variant in SMG9 causes intellectual disability,
            confirming a role for nonsense-mediated decay components in
            neurocognitive development.
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Yang,Q., Qin,Z., Zhang,Q., Yi,S., Yi,S. and Luo,J.
  TITLE     Identification of a novel compound heterozygous SMG9 variants in a
            Chinese family with heart and brain malformation syndrome using
            whole exome sequencing
  JOURNAL   BMC Med Genomics 15 (1), 67 (2022)
   PUBMED   35321723
  REMARK    GeneRIF: Identification of a novel compound heterozygous SMG9
            variants in a Chinese family with heart and brain malformation
            syndrome using whole exome sequencing.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Abdel-Salam,G.M.H., Duan,R., Abdel-Hamid,M.S., Sayed,I.S.M.,
            Jhangiani,S.N., Khan,Z., Du,H., Gibbs,R.A., Posey,J.E., Marafi,D.
            and Lupski,J.R.
  TITLE     Expanding the phenotypic and allelic spectrum of SMG8: Clinical
            observations reveal overlap with SMG9-associated disease trait
  JOURNAL   Am J Med Genet A 188 (2), 648-657 (2022)
   PUBMED   34761517
  REMARK    GeneRIF: Expanding the phenotypic and allelic spectrum of SMG8:
            Clinical observations reveal overlap with SMG9-associated disease
            trait.
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Langer,L.M., Bonneau,F., Gat,Y. and Conti,E.
  TITLE     Cryo-EM reconstructions of inhibitor-bound SMG1 kinase reveal an
            autoinhibitory state dependent on SMG8
  JOURNAL   Elife 10, e72353 (2021)
   PUBMED   34698635
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Han,L., Bai,L., Fang,X., Liu,J., Kang,R., Zhou,D., Tang,D. and
            Dai,E.
  TITLE     SMG9 drives ferroptosis by directly inhibiting GPX4 degradation
  JOURNAL   Biochem Biophys Res Commun 567, 92-98 (2021)
   PUBMED   34146907
  REMARK    GeneRIF: SMG9 drives ferroptosis by directly inhibiting GPX4
            degradation.
REFERENCE   6  (residues 1 to 520)
  AUTHORS   Melero,R., Uchiyama,A., Castano,R., Kataoka,N., Kurosawa,H.,
            Ohno,S., Yamashita,A. and Llorca,O.
  TITLE     Structures of SMG1-UPFs complexes: SMG1 contributes to regulate
            UPF2-dependent activation of UPF1 in NMD
  JOURNAL   Structure 22 (8), 1105-1119 (2014)
   PUBMED   25002321
REFERENCE   7  (residues 1 to 520)
  AUTHORS   Takeda,S., Fujimoto,A., Yamauchi,E., Hiyoshi,M., Kido,H.,
            Watanabe,T., Kaibuchi,K., Ohta,T. and Konishi,H.
  TITLE     Role of a tyrosine phosphorylation of SMG-9 in binding of SMG-9 to
            IQGAP and the NMD complex
  JOURNAL   Biochem Biophys Res Commun 410 (1), 29-33 (2011)
   PUBMED   21640080
  REMARK    GeneRIF: IQGAP1 protein, an actin cytoskeleton modifier acts as a
            binding partner with SMG-9 and this binding is regulated by
            phosphorylation of SMG-9 at Tyr-41.
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Fernandez,I.S., Yamashita,A., Arias-Palomo,E., Bamba,Y.,
            Bartolome,R.A., Canales,M.A., Teixido,J., Ohno,S. and Llorca,O.
  TITLE     Characterization of SMG-9, an essential component of the
            nonsense-mediated mRNA decay SMG1C complex
  JOURNAL   Nucleic Acids Res 39 (1), 347-358 (2011)
   PUBMED   20817927
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Yamashita,A., Izumi,N., Kashima,I., Ohnishi,T., Saari,B.,
            Katsuhata,Y., Muramatsu,R., Morita,T., Iwamatsu,A., Hachiya,T.,
            Kurata,R., Hirano,H., Anderson,P. and Ohno,S.
  TITLE     SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate
            remodeling of the mRNA surveillance complex during
            nonsense-mediated mRNA decay
  JOURNAL   Genes Dev 23 (9), 1091-1105 (2009)
   PUBMED   19417104
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY084349.1, AL136606.1,
            AC004780.1 and BQ180848.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 17, 2007 this sequence version replaced NP_061981.1.
            
            Summary: This gene encodes a regulatory subunit of the SMG1
            complex, which plays a critical role in nonsense-mediated mRNA
            decay (NMD). Binding of the encoded protein to the SMG1 complex
            kinase scaffold protein results in the inhibition of its kinase
            activity. Mutations in this gene cause a multiple congenital
            anomaly syndrome in human patients, characterized by brain
            malformation, congenital heart disease and other features.
            [provided by RefSeq, Jul 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1119794.1,
                                           SRR1163655.59815.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000270066.11/ ENSP00000270066.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.31"
     Protein         1..520
                     /product="nonsense-mediated mRNA decay factor SMG9"
                     /note="protein smg-9 homolog"
                     /calculated_mol_wt=57520
     Region          1..94
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            53
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Region          108..143
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Region          341..360
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H0W8.1)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H0W8.1)"
     CDS             1..520
                     /gene="SMG9"
                     /gene_synonym="C19orf61; F17127_1; HBMS; NEDITPO"
                     /coded_by="NM_019108.4:316..1878"
                     /db_xref="CCDS:CCDS33043.2"
                     /db_xref="GeneID:56006"
                     /db_xref="HGNC:HGNC:25763"
                     /db_xref="MIM:613176"
ORIGIN      
        1 msesghsqpg lygierrrrw kepgsggpqn lsgpggrerd yiapwererr daseetstsv
       61 mqktpiilsk ppaerskqpp pptapaappa paplekpivl mkpreegkgp vavtgastpe
      121 gtappppaap appkgekegq rptqpvyqiq nrgmgtaapa amdpvvgqak llppermkhs
      181 iklvddqmnw cdsaieylld qtdvlvvgvl glqgtgksmv msllsantpe edqrtyvfra
      241 qsaemkergg nqtsgidffi tqerivfldt qpilspsild hlinndrklp peynlphtyv
      301 emqslqiaaf lftvchvviv vqdwftdlsl yrflqtaemv kpstpspshe sssssgsdeg
      361 teyyphlvfl qnkarredfc prklrqmhlm idqlmahshl rykgtlsmlq cnvfpglppd
      421 fldsevnlfl vpfmdseaes enppragpgs splfsllpgy rghpsfqslv sklrsqvmsm
      481 arpqlshtil teknwfhyaa riwdgvrkss alaeysrlla
//
LOCUS       NP_001357599             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001357599
VERSION     NP_001357599.1
DBSOURCE    REFSEQ: accession NM_001370670.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.84413.1,
                                           SRR1803616.261546.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001370670.1:377..1141"
                     /note="isoform j is encoded by transcript variant 14"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_004796                142 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB4 [Homo sapiens].
ACCESSION   NP_004796
VERSION     NP_004796.1
DBSOURCE    REFSEQ: accession NM_004805.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 142)
  AUTHORS   Higman,B., Shugar,D.H., Stark,C.P., Ekstrom,G., Koppes,M.N.,
            Lynett,P., Dufresne,A., Haeussler,P.J., Geertsema,M., Gulick,S.,
            Mattox,A., Venditti,J.G., Walton,M.A.L., McCall,N., Mckittrick,E.,
            MacInnes,B., Bilderback,E.L., Tang,H., Willis,M.J., Richmond,B.,
            Reece,R.S., Larsen,C., Olson,B., Capra,J., Ayca,A., Bloom,C.,
            Williams,H., Bonno,D., Weiss,R., Keen,A., Skanavis,V. and Loso,M.
  TITLE     The 2015 landslide and tsunami in Taan Fiord, Alaska
  JOURNAL   Sci Rep 8 (1), 12993 (2018)
   PUBMED   30190595
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 142)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   5  (residues 1 to 142)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 142)
  AUTHORS   Wu-Baer,F., Sigman,D. and Gaynor,R.B.
  TITLE     Specific binding of RNA polymerase II to the human immunodeficiency
            virus trans-activating region RNA is regulated by cellular
            cofactors and Tat
  JOURNAL   Proc Natl Acad Sci U S A 92 (16), 7153-7157 (1995)
   PUBMED   7638159
REFERENCE   7  (residues 1 to 142)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   8  (residues 1 to 142)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   9  (residues 1 to 142)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
REFERENCE   10 (residues 1 to 142)
  AUTHORS   Conaway,R.C. and Conaway,J.W.
  TITLE     ATP activates transcription initiation from promoters by RNA
            polymerase II in a reversible step prior to RNA synthesis
  JOURNAL   J Biol Chem 263 (6), 2962-2968 (1988)
   PUBMED   2449431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC093795.1, AC006011.2 and
            AA775787.1.
            
            Summary: This gene encodes the fourth largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. In yeast, this polymerase subunit is
            associated with the polymerase under suboptimal growth conditions
            and may have a stress protective role. A sequence for a ribosomal
            pseudogene is contained within the 3' untranslated region of the
            transcript from this gene. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093795.1, SRR1163655.112702.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968968,
                                           SAMEA2150385 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000272645.9/ ENSP00000272645.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14.3"
     Protein         1..142
                     /product="DNA-directed RNA polymerase II subunit RPB4"
                     /EC_number="2.7.7.6"
                     /note="RNA polymerase II subunit hsRBP4; RNA polymerase II
                     subunit B4; DNA-directed RNA polymerase II subunit D;
                     DNA-directed RNA polymerase II 16 kDa polypeptide; RNA
                     polymerase II 16 kDa subunit; polymerase (RNA) II (DNA
                     directed) polypeptide D; polymerase (RNA) II subunit D;
                     RNA polymerase II subunit hsRPB4"
                     /calculated_mol_wt=16180
     Region          24..141
                     /region_name="RPOL4c"
                     /note="DNA-directed RNA-polymerase II subunit; smart00657"
                     /db_xref="CDD:128904"
     CDS             1..142
                     /gene="POLR2D"
                     /gene_synonym="HSRBP4; HSRPB4; RBP4; RPB16; RPB4"
                     /coded_by="NM_004805.4:56..484"
                     /db_xref="CCDS:CCDS2151.1"
                     /db_xref="GeneID:5433"
                     /db_xref="HGNC:HGNC:9191"
                     /db_xref="MIM:606017"
ORIGIN      
        1 maaggsdpra gdveedasql ifpkefetae tllnsevhml lehrkqqnes aedeqelsev
       61 fmktlnytar fsrfknreti asvrslllqk klhkfelacl anlcpetaee skalipsleg
      121 rfedeelqqi lddiqtkrsf qy
//
LOCUS       NP_944493                515 aa            linear   PRI 20-NOV-2025
DEFINITION  gamma-aminobutyric acid receptor subunit gamma-2 isoform 3
            precursor [Homo sapiens].
ACCESSION   NP_944493
VERSION     NP_944493.2
DBSOURCE    REFSEQ: accession NM_198903.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 515)
  AUTHORS   Zhou,J., Noviello,C.M., Teng,J., Moore,H., Lega,B. and Hibbs,R.E.
  TITLE     Resolving native GABAA receptor structures from the human brain
  JOURNAL   Nature 638 (8050), 562-568 (2025)
   PUBMED   39843743
REFERENCE   2  (residues 1 to 515)
  AUTHORS   Sui,J., Zhan,L., Ji,S., Wu,W., Chen,Y., Yun,F., Liang,W., Wang,J.,
            Cao,M., Shen,D. and Zhang,Q.
  TITLE     Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations
  JOURNAL   CNS Neurosci Ther 30 (2), e14583 (2024)
   PUBMED   38357846
  REMARK    GeneRIF: Differential inflammation responses determine the variable
            phenotypes of epilepsy induced by GABRG2 mutations.
REFERENCE   3  (residues 1 to 515)
  AUTHORS   Zhang,Q., Forster-Gibson,C., Bercovici,E., Bernardo,A., Ding,F.,
            Shen,W., Langer,K., Rex,T. and Kang,J.Q.
  TITLE     Epilepsy plus blindness in microdeletion of GABRA1 and GABRG2 in
            mouse and human
  JOURNAL   Exp Neurol 369, 114537 (2023)
   PUBMED   37703949
  REMARK    GeneRIF: Epilepsy plus blindness in microdeletion of GABRA1 and
            GABRG2 in mouse and human.
REFERENCE   4  (residues 1 to 515)
  AUTHORS   Ma,M., Zhao,J., Xie,D. and Chen,J.
  TITLE     Association between GABRG2 Gene Single Nucleotide Polymorphisms and
            Susceptibility to Ischemic Stroke in a Chinese Population
  JOURNAL   J Integr Neurosci 22 (6), 151 (2023)
   PUBMED   38176934
  REMARK    GeneRIF: Association between GABRG2 Gene Single Nucleotide
            Polymorphisms and Susceptibility to Ischemic Stroke in a Chinese
            Population.
REFERENCE   5  (residues 1 to 515)
  AUTHORS   Bengtsson,S.K.S., Sjostedt,J., Malinina,E., Das,R., Doverskog,M.,
            Johansson,M., Haage,D. and Backstrom,T.
  TITLE     Extra-Synaptic GABAA Receptor Potentiation and Neurosteroid-Induced
            Learning Deficits Are Inhibited by GR3027, a GABAA Modulating
            Steroid Antagonist
  JOURNAL   Biomolecules 13 (10), 1496 (2023)
   PUBMED   37892178
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 515)
  AUTHORS   Kostrzewa,M., Kohler,A., Eppelt,K., Hellam,L., Fairweather,N.D.,
            Levy,E.R., Monaco,A.P. and Muller,U.
  TITLE     Assignment of genes encoding GABAA receptor subunits alpha 1, alpha
            6, beta 2, and gamma 2 to a YAC contig of 5q33
  JOURNAL   Eur J Hum Genet 4 (4), 199-204 (1996)
   PUBMED   8875185
REFERENCE   7  (residues 1 to 515)
  AUTHORS   Russek,S.J. and Farb,D.H.
  TITLE     Mapping of the beta 2 subunit gene (GABRB2) to microdissected human
            chromosome 5q34-q35 defines a gene cluster for the most abundant
            GABAA receptor isoform
  JOURNAL   Genomics 23 (3), 528-533 (1994)
   PUBMED   7851879
REFERENCE   8  (residues 1 to 515)
  AUTHORS   Moss,S.J., Doherty,C.A. and Huganir,R.L.
  TITLE     Identification of the cAMP-dependent protein kinase and protein
            kinase C phosphorylation sites within the major intracellular
            domains of the beta 1, gamma 2S, and gamma 2L subunits of the
            gamma-aminobutyric acid type A receptor
  JOURNAL   J Biol Chem 267 (20), 14470-14476 (1992)
   PUBMED   1321150
REFERENCE   9  (residues 1 to 515)
  AUTHORS   Wilcox,A.S., Warrington,J.A., Gardiner,K., Berger,R., Whiting,P.,
            Altherr,M.R., Wasmuth,J.J., Patterson,D. and Sikela,J.M.
  TITLE     Human chromosomal localization of genes encoding the gamma 1 and
            gamma 2 subunits of the gamma-aminobutyric acid receptor indicates
            that members of this gene family are often clustered in the genome
  JOURNAL   Proc Natl Acad Sci U S A 89 (13), 5857-5861 (1992)
   PUBMED   1321425
REFERENCE   10 (residues 1 to 515)
  AUTHORS   Pritchett,D.B., Sontheimer,H., Shivers,B.D., Ymer,S.,
            Kettenmann,H., Schofield,P.R. and Seeburg,P.H.
  TITLE     Importance of a novel GABAA receptor subunit for benzodiazepine
            pharmacology
  JOURNAL   Nature 338 (6216), 582-585 (1989)
   PUBMED   2538761
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008611.6, AC091926.4 and
            AC091984.3.
            
            On May 24, 2008 this sequence version replaced NP_944493.1.
            
            Summary: This gene encodes a gamma-aminobutyric acid (GABA)
            receptor. GABA is the major inhibitory neurotransmitter in the
            mammlian brain, where it acts at GABA-A receptors, which are
            ligand-gated chloride channels. GABA-A receptors are pentameric,
            consisting of proteins from several subunit classes: alpha, beta,
            gamma, delta and rho. Mutations in this gene have been associated
            with epilepsy and febrile seizures. Multiple transcript variants
            encoding different isoforms have been identified for this gene.
            [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (3) encodes the longest isoform
            (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC036030.1, SRR1660805.30896.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..515
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..515
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 3 precursor"
                     /note="gamma-aminobutyric acid receptor subunit gamma-2;
                     GABA(A) receptor subunit gamma-2; GABA(A) receptor, gamma
                     2; gamma-aminobutyric acid (GABA) A receptor, gamma 2;
                     gamma-aminobutyric acid type A receptor gamma2 subunit;
                     GABAAR subunit gamma-2"
                     /calculated_mol_wt=55036
     sig_peptide     1..39
                     /calculated_mol_wt=4327
     mat_peptide     40..515
                     /product="gamma-aminobutyric acid receptor subunit gamma-2
                     isoform 3"
                     /calculated_mol_wt=55036
     Region          69..512
                     /region_name="LIC"
                     /note="Cation transporter family protein; cl42365"
                     /db_xref="CDD:455710"
     Region          90..311
                     /region_name="LGIC_ECD_GABAAR_G"
                     /note="extracellular domain of gamma-aminobutyric acid
                     receptor subunit gamma; cd19000"
                     /db_xref="CDD:349801"
     Site            order(97,116)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:349801"
     Site            order(100,102..103,108..109,116,118..119,136,138..139,
                     148..153,156,158,160..161,167..169,171,181..183,211,311)
                     /site_type="other"
                     /note="pentamer interface [polypeptide binding]"
                     /db_xref="CDD:349801"
     Region          190..204
                     /region_name="Cys-loop"
                     /note="Cys-loop [structural motif]"
                     /db_xref="CDD:349801"
     CDS             1..515
                     /gene="GABRG2"
                     /gene_synonym="CAE2; DEE74; ECA2; EIEE74; FEB8; GEFSP3"
                     /coded_by="NM_198903.2:359..1906"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS47333.1"
                     /db_xref="GeneID:2566"
                     /db_xref="HGNC:HGNC:4087"
                     /db_xref="MIM:137164"
ORIGIN      
        1 msspniwstg ssvystpvfs qkmtvwilll lslypgftsq ksdddyedya snktwvltpk
       61 vpegdvtvil nnllegydnk lrpdigvkpt lihtdmyvns igpvnainme ytidiffaqt
      121 wydrrlkfns tikvlrlnsn mvgkiwipdt ffrnskkada hwittpnrml riwndgrvly
      181 tlrltidaec qlqlhnfpmd ehscplefss wsrsiaqagm csgvisahys lrfwgstdpp
      241 tlasrvagis dgypreeivy qwkrssvevg dtrswrlyqf sfvglrntte vvkttsgdyv
      301 vmsvyfdlsr rmgyftiqty ipctlivvls wvsfwinkda vpartslgit tvltmttlst
      361 iarkslpkvs yvtamdlfvs vcfifvfsal veygtlhyfv snrkpskdkd kkkknpllrm
      421 fsfkaptidi rprsatiqmn nathlqerde eygyecldgk dcasffccfe dcrtgawrhg
      481 rihiriakmd syariffpta fclfnlvywv sylyl
//
LOCUS       NP_004422                976 aa            linear   PRI 20-NOV-2025
DEFINITION  ephrin type-A receptor 2 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_004422
VERSION     NP_004422.2
DBSOURCE    REFSEQ: accession NM_004431.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   de Aguiar,A.C.F., Ferreira,N.C.F.L., Borba,M.A.C.S.M.,
            Filho,D.L.F., Leitao,G.M., Mattos,L.A., Filho,J.L.L. and
            Martins,D.B.G.
  TITLE     TYRO3 and EPHA2 Expression Are Dysregulated in Breast Cancer
  JOURNAL   Cell Biochem Funct 42 (7), e4128 (2024)
   PUBMED   39327735
  REMARK    GeneRIF: TYRO3 and EPHA2 Expression Are Dysregulated in Breast
            Cancer.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Harris,E.D., Sharpe,J.C., Strozen,T., Abdi,S., Kliewer,M.,
            Sanchez,M.G., Hogan,N.S., MacDonald-Dickinson,V., Vizeacoumar,F.J.
            and Toosi,B.M.
  TITLE     The EphA2 Receptor Regulates Invasiveness and Drug Sensitivity in
            Canine and Human Osteosarcoma Cells
  JOURNAL   Cells 13 (14), 1201 (2024)
   PUBMED   39056783
  REMARK    GeneRIF: The EphA2 Receptor Regulates Invasiveness and Drug
            Sensitivity in Canine and Human Osteosarcoma Cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Wirth,D., Ozdemir,E., Wimley,W.C., Pasquale,E.B. and Hristova,K.
  TITLE     Transmembrane helix interactions regulate oligomerization of the
            receptor tyrosine kinase EphA2
  JOURNAL   J Biol Chem 300 (7), 107441 (2024)
   PUBMED   38838777
  REMARK    GeneRIF: Transmembrane helix interactions regulate oligomerization
            of the receptor tyrosine kinase EphA2.
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Bai,J., Chen,Y., Sun,Y., Wang,X., Wang,Y., Guo,S., Shang,Z. and
            Shao,Z.
  TITLE     EphA2 promotes the transcription of KLF4 to facilitate stemness in
            oral squamous cell carcinoma
  JOURNAL   Cell Mol Life Sci 81 (1), 278 (2024)
   PUBMED   38916835
  REMARK    GeneRIF: EphA2 promotes the transcription of KLF4 to facilitate
            stemness in oral squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Sulman,E.P., Tang,X.X., Allen,C., Biegel,J.A., Pleasure,D.E.,
            Brodeur,G.M. and Ikegaki,N.
  TITLE     ECK, a human EPH-related gene, maps to 1p36.1, a common region of
            alteration in human cancers
  JOURNAL   Genomics 40 (2), 371-374 (1997)
   PUBMED   9119409
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Pandey,A., Duan,H. and Dixit,V.M.
  TITLE     Characterization of a novel Src-like adapter protein that
            associates with the Eck receptor tyrosine kinase
  JOURNAL   J Biol Chem 270 (33), 19201-19204 (1995)
   PUBMED   7543898
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Pandey,A., Shao,H., Marks,R.M., Polverini,P.J. and Dixit,V.M.
  TITLE     Role of B61, the ligand for the Eck receptor tyrosine kinase, in
            TNF-alpha-induced angiogenesis
  JOURNAL   Science 268 (5210), 567-569 (1995)
   PUBMED   7536959
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Pandey,A., Lazar,D.F., Saltiel,A.R. and Dixit,V.M.
  TITLE     Activation of the Eck receptor protein tyrosine kinase stimulates
            phosphatidylinositol 3-kinase activity
  JOURNAL   J Biol Chem 269 (48), 30154-30157 (1994)
   PUBMED   7982920
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Davis,S., Gale,N.W., Aldrich,T.H., Maisonpierre,P.C., Lhotak,V.,
            Pawson,T., Goldfarb,M. and Yancopoulos,G.D.
  TITLE     Ligands for EPH-related receptor tyrosine kinases that require
            membrane attachment or clustering for activity
  JOURNAL   Science 266 (5186), 816-819 (1994)
   PUBMED   7973638
REFERENCE   10 (residues 1 to 976)
  AUTHORS   Lindberg,R.A. and Hunter,T.
  TITLE     cDNA cloning and characterization of eck, an epithelial cell
            receptor protein-tyrosine kinase in the eph/elk family of protein
            kinases
  JOURNAL   Mol Cell Biol 10 (12), 6316-6324 (1990)
   PUBMED   2174105
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY005615.1, BC037166.2,
            AL451042.10 and AI302504.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 18, 2003 this sequence version replaced NP_004422.1.
            
            Summary: This gene belongs to the ephrin receptor subfamily of the
            protein-tyrosine kinase family. EPH and EPH-related receptors have
            been implicated in mediating developmental events, particularly in
            the nervous system. Receptors in the EPH subfamily typically have a
            single kinase domain and an extracellular region containing a
            Cys-rich domain and 2 fibronectin type III repeats. The ephrin
            receptors are divided into 2 groups based on the similarity of
            their extracellular domain sequences and their affinities for
            binding ephrin-A and ephrin-B ligands. This gene encodes a protein
            that binds ephrin-A ligands. Mutations in this gene are the cause
            of certain genetically-related cataract disorders.[provided by
            RefSeq, May 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037166.2, M59371.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358432.8/ ENSP00000351209.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.13"
     Protein         1..976
                     /product="ephrin type-A receptor 2 isoform 1 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-A receptor 2; epithelial cell receptor
                     protein tyrosine kinase; tyrosine-protein kinase receptor
                     ECK"
                     /calculated_mol_wt=105891
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2394
     Region          28..201
                     /region_name="EphR_LBD_A2"
                     /note="Ligand Binding Domain of Ephrin type-A Receptor 2;
                     cd10480"
                     /db_xref="CDD:198448"
     Site            order(53,55..59,61,63,65..66,68..70,73,101,103,108,151,
                     155..156,159..161,188..190,192)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198448"
     Site            129..133
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:198448"
     Site            order(329,404,417)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          330..424
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(418..419,421..422)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          438..519
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(515..516,518..519)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          <556..610
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          607..875
                     /region_name="PTKc_EphR_A2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Ephrin Receptor A2; cd05063"
                     /db_xref="CDD:133194"
     Site            order(619,621..623,627,644,646,692..693,695,739,743..744,
                     746,757,776..780,789,823)
                     /site_type="active"
                     /db_xref="CDD:133194"
     Site            order(619,622..623,644,646,692..693,695,744,746,757)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133194"
     Site            order(739,743,776..780,789,823)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133194"
     Site            756..782
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133194"
     Region          902..971
                     /region_name="SAM_EPH-A2"
                     /note="SAM domain of EPH-A2 family of tyrosine kinase
                     receptors; cd09543"
                     /db_xref="CDD:188942"
     Site            order(917,941,956..957,960)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188942"
     Site            order(921,954)
                     /site_type="other"
                     /note="putative phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:188942"
     CDS             1..976
                     /gene="EPHA2"
                     /gene_synonym="ARCC2; CTPA; CTPP1; CTRCT6; ECK"
                     /coded_by="NM_004431.5:138..3068"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS169.1"
                     /db_xref="GeneID:1969"
                     /db_xref="HGNC:HGNC:3386"
                     /db_xref="MIM:176946"
ORIGIN      
        1 melqaaracf allwgcalaa aaaaqgkevv lldfaaagge lgwlthpygk gwdlmqnimn
       61 dmpiymysvc nvmsgdqdnw lrtnwvyrge aerifielkf tvrdcnsfpg gasscketfn
      121 lyyaesdldy gtnfqkrlft kidtiapdei tvssdfearh vklnveersv gpltrkgfyl
      181 afqdigacva llsvrvyykk cpellqglah fpetiagsda pslatvagtc vdhavvppgg
      241 eeprmhcavd gewlvpigqc lcqagyekve dacqacspgf fkfeasespc lecpehtlps
      301 pegatscece egffrapqdp asmpctrpps aphyltavgm gakvelrwtp pqdsggredi
      361 vysvtceqcw pesgecgpce asvrysepph gltrtsvtvs dlephmnytf tvearngvsg
      421 lvtsrsfrta svsinqtepp kvrlegrstt slsvswsipp pqqsrvwkye vtyrkkgdsn
      481 synvrrtegf svtlddlapd ttylvqvqal tqegqgagsk vhefqtlspe gsgnlavigg
      541 vavgvvlllv lagvgffihr rrknqrarqs pedvyfskse qlkplktyvd phtyedpnqa
      601 vlkftteihp scvtrqkvig agefgevykg mlktssgkke vpvaiktlka gytekqrvdf
      661 lgeagimgqf shhniirleg viskykpmmi iteymengal dkflrekdge fsvlqlvgml
      721 rgiaagmkyl anmnyvhrdl aarnilvnsn lvckvsdfgl srvleddpea tyttsggkip
      781 irwtapeais yrkftsasdv wsfgivmwev mtygerpywe lsnhevmkai ndgfrlptpm
      841 dcpsaiyqlm mqcwqqerar rpkfadivsi ldklirapds lktladfdpr vsirlpstsg
      901 segvpfrtvs ewlesikmqq ytehfmaagy taiekvvqmt nddikrigvr lpghqkriay
      961 sllglkdqvn tvgipi
//
LOCUS       NP_113651                330 aa            linear   PRI 20-NOV-2025
DEFINITION  inactive hydroxysteroid dehydrogenase-like protein 1 isoform a
            [Homo sapiens].
ACCESSION   NP_113651
VERSION     NP_113651.4
DBSOURCE    REFSEQ: accession NM_031463.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 330)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   2  (residues 1 to 330)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 330)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 330)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   5  (residues 1 to 330)
  AUTHORS   Meier,M., Tokarz,J., Haller,F., Mindnich,R. and Adamski,J.
  TITLE     Human and zebrafish hydroxysteroid dehydrogenase like 1 (HSDL1)
            proteins are inactive enzymes but conserved among species
  JOURNAL   Chem Biol Interact 178 (1-3), 197-205 (2009)
   PUBMED   19026618
  REMARK    GeneRIF: characterized the subcellular localization as well as the
            tissue distribution and performed a screen for putative substrates
            of HSDL1 enzymes
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC306668.1, AK074878.1, BC018084.1, AY028377.1, AK025626.1,
            DB525323.1 and H40440.1.
            
            On Apr 4, 2009 this sequence version replaced NP_113651.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.93034.1,
                                           SRR1660809.193253.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219439.9/ ENSP00000219439.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..330
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.1"
     Protein         1..330
                     /product="inactive hydroxysteroid dehydrogenase-like
                     protein 1 isoform a"
                     /note="inactive hydroxysteroid dehydrogenase-like protein
                     1; steroid dehydrogenase-like protein; short chain
                     dehydrogenase/reductase family 12C member 3"
                     /calculated_mol_wt=36871
     Region          2..82
                     /region_name="Required for mitochondria translocation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3SXM5.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.6;
                     propagated from UniProtKB/Swiss-Prot (Q3SXM5.3)"
     Region          67..309
                     /region_name="17beta-HSD1_like_SDR_c"
                     /note="17-beta-hydroxysteroid dehydrogenases (17beta-HSDs)
                     types -1, -3, and -12, -like, classical (c) SDRs; cd05356"
                     /db_xref="CDD:187614"
     Site            order(74,76..79,98..100,123..125,151..153,176,203..205,
                     218,222,248..251,253..254)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187614"
     Site            order(177,205,218,222)
                     /site_type="active"
                     /db_xref="CDD:187614"
     CDS             1..330
                     /gene="HSDL1"
                     /gene_synonym="SDR12C3"
                     /coded_by="NM_031463.5:167..1159"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10942.1"
                     /db_xref="GeneID:83693"
                     /db_xref="HGNC:HGNC:16475"
                     /db_xref="MIM:619067"
ORIGIN      
        1 maavdsfyll yreiarscnc ymealalvga wytarksitv icdfyslirl hfiprlgsra
       61 dlikqygrwa vvsgatdgig kayaeelasr glniilisrn eeklqvvakd iadtykvetd
      121 iivadfssgr eiylpireal kdkdvgilvn nvgvfypypq yftqlsedkl wdiinvniaa
      181 aslmvhvvlp gmverkkgai vtissgscck ptpqlaafsa skayldhfsr alqyeyaskg
      241 ifvqslipfy vatsmtapsn flhrcswlvp spkvyahhav stlgiskrtt gywshsiqfl
      301 faqympewlw vwganilnrs lrkealscta
//
LOCUS       NP_001355933             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001355933 XP_011516241
VERSION     NP_001355933.1
DBSOURCE    REFSEQ: accession NM_001369004.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_011516241.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.136123.1,
                                           SRR1660807.264788.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369004.1:284..1048"
                     /note="isoform j is encoded by transcript variant 25"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001333211             254 aa            linear   PRI 20-NOV-2025
DEFINITION  syntaxin-18 isoform 3 [Homo sapiens].
ACCESSION   NP_001333211
VERSION     NP_001333211.1
DBSOURCE    REFSEQ: accession NM_001346282.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Guillemyn,B., De Saffel,H., Bek,J.W., Tapaneeyaphan,P., De
            Clercq,A., Jarayseh,T., Debaenst,S., Willaert,A., De Rycke,R.,
            Byers,P.H., Rosseel,T., Coucke,P., Blaumeiser,B., Syx,D.,
            Malfait,F. and Symoens,S.
  TITLE     Syntaxin 18 Defects in Human and Zebrafish Unravel Key Roles in
            Early Cartilage and Bone Development
  JOURNAL   J Bone Miner Res 38 (11), 1718-1730 (2023)
   PUBMED   37718532
  REMARK    GeneRIF: Syntaxin 18 Defects in Human and Zebrafish Unravel Key
            Roles in Early Cartilage and Bone Development.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Bassett,T., Harpur,B., Poon,H.Y., Kuo,K.H. and Lee,C.H.
  TITLE     Effective stimulation of growth in MCF-7 human breast cancer cells
            by inhibition of syntaxin18 by external guide sequence and
            ribonuclease P
  JOURNAL   Cancer Lett 272 (1), 167-175 (2008)
   PUBMED   18722709
  REMARK    GeneRIF: Stx18 in involved in growth of human breast cancer cells
            and may possibly be used as a prognostic marker and a molecular
            target in the treatment of breast cancer.
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Arasaki,K., Taniguchi,M., Tani,K. and Tagaya,M.
  TITLE     RINT-1 regulates the localization and entry of ZW10 to the syntaxin
            18 complex
  JOURNAL   Mol Biol Cell 17 (6), 2780-2788 (2006)
   PUBMED   16571679
  REMARK    GeneRIF: RINT-1 coordinates the localization and function of ZW10
            by serving as a link between ZW10 and the SNARE complex comprising
            syntaxin 18.
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Nakajima,K., Hirose,H., Taniguchi,M., Kurashina,H., Arasaki,K.,
            Nagahama,M., Tani,K., Yamamoto,A. and Tagaya,M.
  TITLE     Involvement of BNIP1 in apoptosis and endoplasmic reticulum
            membrane fusion
  JOURNAL   EMBO J 23 (16), 3216-3226 (2004)
   PUBMED   15272311
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Hirose,H., Arasaki,K., Dohmae,N., Takio,K., Hatsuzawa,K.,
            Nagahama,M., Tani,K., Yamamoto,A., Tohyama,M. and Tagaya,M.
  TITLE     Implication of ZW10 in membrane trafficking between the endoplasmic
            reticulum and Golgi
  JOURNAL   EMBO J 23 (6), 1267-1278 (2004)
   PUBMED   15029241
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Hatsuzawa,K., Hirose,H., Tani,K., Yamamoto,A., Scheller,R.H. and
            Tagaya,M.
  TITLE     Syntaxin 18, a SNAP receptor that functions in the endoplasmic
            reticulum, intermediate compartment, and cis-Golgi vesicle
            trafficking
  JOURNAL   J Biol Chem 275 (18), 13713-13720 (2000)
   PUBMED   10788491
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN364605.1, AB028741.1 and
            AL832867.1.
            
            Summary: This gene encodes a member of the syntaxin family of
            soluble N-ethylmaleimide-sensitive factor attachment protein
            receptors (SNAREs) which is part of a membrane tethering complex
            that includes other SNAREs and several peripheral membrane
            proteins, and is involved in vesicular transport between the
            endoplasmic reticulum (ER) and the Golgi complex. The encoded
            protein is important for the organization of the smooth, rough, and
            exit site ER subdomains. A pseudogene of this gene has been
            identified. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Oct 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.189597.1,
                                           SRR1163657.149965.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3-p16.2"
     Protein         1..254
                     /product="syntaxin-18 isoform 3"
                     /note="cell growth-inhibiting gene 9 protein"
                     /calculated_mol_wt=29475
     Region          165..223
                     /region_name="SNARE_syntaxin18"
                     /note="SNARE motif, subgroup Qa; cd15850"
                     /db_xref="CDD:277203"
     Site            order(166,168..169,171..176,178..180,182..183,185..187,
                     189..190,192..194,196..197,199..204,206..211,213..218,
                     220..222)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277203"
     Site            196
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277203"
     CDS             1..254
                     /gene="STX18"
                     /gene_synonym="Ufe1"
                     /coded_by="NM_001346282.2:260..1024"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:53407"
                     /db_xref="HGNC:HGNC:15942"
                     /db_xref="MIM:606046"
ORIGIN      
        1 mseygrmtdt erdqidqdaq ifmrtcseai qqlrteahke ihsqqvkehr tavldfiedy
       61 lkrvcklyse qrairvkrvv dkkrlsklep epntktrest ssekvsqsps kdseenpate
      121 erpekilaet qpelgtwgdg kgedelspee iqmfeqenqr ligemnslfd evrqiegrvv
      181 eisrlqeift ekvlqqeaei dsihqlvvga tenikegned ireaiknnag frvwilfflv
      241 mcsfsllfld wyds
//
LOCUS       NP_001269403             404 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-1 complex subunit gamma-like 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001269403 XP_005268240
VERSION     NP_001269403.1
DBSOURCE    REFSEQ: accession NM_001282474.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Tavares,L.A., da Silva,E.M., da Silva-Januario,M.E., Januario,Y.C.,
            de Cavalho,J.V., Czernisz,E.S., Mardones,G.A. and daSilva,L.L.
  TITLE     CD4 downregulation by the HIV-1 protein Nef reveals distinct roles
            for the gamma1 and gamma2 subunits of the AP-1 complex in protein
            trafficking
  JOURNAL   J Cell Sci 130 (2), 429-443 (2017)
   PUBMED   27909244
  REMARK    GeneRIF: Depletion of the gamma2 or mu1A (AP1M1) subunits of AP-1,
            but not of gamma1 (AP1G1), precludes Nef-mediated lysosomal
            degradation of CD4.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Jurgens,M.C., Voros,J., Rautureau,G.J., Shepherd,D.A., Pye,V.E.,
            Muldoon,J., Johnson,C.M., Ashcroft,A.E., Freund,S.M. and
            Ferguson,N.
  TITLE     The hepatitis B virus preS1 domain hijacks host trafficking
            proteins by motif mimicry
  JOURNAL   Nat Chem Biol 9 (9), 540-547 (2013)
   PUBMED   23851574
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Mattera,R., Ritter,B., Sidhu,S.S., McPherson,P.S. and
            Bonifacino,J.S.
  TITLE     Definition of the consensus motif recognized by gamma-adaptin ear
            domains
  JOURNAL   J Biol Chem 279 (9), 8018-8028 (2004)
   PUBMED   14665628
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Page,L.J., Sowerby,P.J., Lui,W.W. and Robinson,M.S.
  TITLE     Gamma-synergin: an EH domain-containing protein that interacts with
            gamma-adaptin
  JOURNAL   J Cell Biol 146 (5), 993-1004 (1999)
   PUBMED   10477754
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Lewin,D.A., Sheff,D., Ooi,C.E., Whitney,J.A., Yamamoto,E.,
            Chicione,L.M., Webster,P., Bonifacino,J.S. and Mellman,I.
  TITLE     Cloning, expression, and localization of a novel gamma-adaptin-like
            molecule
  JOURNAL   FEBS Lett 435 (2-3), 263-268 (1998)
   PUBMED   9762922
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Takatsu,H., Sakurai,M., Shin,H.W., Murakami,K. and Nakayama,K.
  TITLE     Identification and characterization of novel clathrin
            adaptor-related proteins
  JOURNAL   J Biol Chem 273 (38), 24693-24700 (1998)
   PUBMED   9733768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG701521.1, BX161425.1 and
            AI497879.1.
            
            On Sep 11, 2013 this sequence version replaced XP_005268240.1.
            
            Summary: Adaptins are important components of clathrin-coated
            vesicles transporting ligand-receptor complexes from the plasma
            membrane or from the trans-Golgi network to lysosomes. The adaptin
            family of proteins is composed of four classes of molecules named
            alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together
            with medium and small subunits, form a heterotetrameric complex
            called an adaptor, whose role is to promote the formation of
            clathrin-coated pits and vesicles. The protein encoded by this gene
            is a gamma-adaptin protein and it belongs to the adaptor complexes
            large subunits family. This protein along with the complex is
            thought to function at some trafficking step in the complex
            pathways between the trans-Golgi network and the cell surface.
            [provided by RefSeq, Aug 2017].
            
            Transcript Variant: This variant (3) uses an alternate 5' exon
            structure and thus differs in the 5' UTR and 5' coding region
            compared to variant 1. These differences cause translation
            initiation at a downstream AUG and result in an isoform (2) with a
            shorter N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX161425.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..404
                     /product="AP-1 complex subunit gamma-like 2 isoform 2"
                     /note="gamma2-adaptin;
                     clathrin-associated/assembly/adaptor protein, large,
                     gamma-2; AP-1 complex subunit gamma-like 2; adaptor
                     related protein complex 1 gamma 2 subunit"
                     /calculated_mol_wt=44407
     Region          <1..194
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          291..399
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     CDS             1..404
                     /gene="AP1G2"
                     /gene_synonym="G2AD"
                     /coded_by="NM_001282474.2:1310..2524"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="GeneID:8906"
                     /db_xref="HGNC:HGNC:556"
                     /db_xref="MIM:603534"
ORIGIN      
        1 mmqelqafle scppdlradc asgillaaer faptkrwhid tilhvlttag thvrddavan
       61 ltqliggaqe lhaysvrrly nalaedisqq plvqvaawci geygdlllag nceeieplqv
      121 deeevlalle kvlqshmslp atrgyaltal mklstrlcgd nnrirqvvsi ygscldvelq
      181 qraveydtlf rkydhmraai lekmplverd gpqadeeake skeaaqlsea apvptepqas
      241 qlldlldlld gasgdvqhpp hldpspggal vhlldlpcvp pppapipdlk vferegvqln
      301 lsfirppenp alllititat nfsegdvthf icqaavpksl qlqlqapsgn tvpargglpi
      361 tqlfrilnpn kaplrlklrl tydhfhqsvq eifevnnlpv eswq
//
LOCUS       NP_036274                360 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-D1-binding protein 1 [Homo sapiens].
ACCESSION   NP_036274
VERSION     NP_036274.3
DBSOURCE    REFSEQ: accession NM_012142.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 360)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 360)
  AUTHORS   Shi,Q., Ruan,J., Yang,Y.C., Shi,X.Q., Liu,S.D., Wang,H.Y.,
            Zhang,S.J., Wang,S.Q., Zhong,L. and Sun,C.
  TITLE     rs66651343 and rs12909095 confer lung cancer risk by regulating
            CCNDBP1 expression
  JOURNAL   PLoS One 18 (4), e0284347 (2023)
   PUBMED   37058478
  REMARK    GeneRIF: rs66651343 and rs12909095 confer lung cancer risk by
            regulating CCNDBP1 expression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 360)
  AUTHORS   Kim,D.K., Weller,B., Lin,C.W., Sheykhkarimli,D., Knapp,J.J.,
            Dugied,G., Zanzoni,A., Pons,C., Tofaute,M.J., Maseko,S.B.,
            Spirohn,K., Laval,F., Lambourne,L., Kishore,N., Rayhan,A.,
            Sauer,M., Young,V., Halder,H., la Rosa,N.M., Pogoutse,O.,
            Strobel,A., Schwehn,P., Li,R., Rothballer,S.T., Altmann,M.,
            Cassonnet,P., Cote,A.G., Vergara,L.E., Hazelwood,I., Liu,B.B.,
            Nguyen,M., Pandiarajan,R., Dohai,B., Coloma,P.A.R., Poirson,J.,
            Giuliana,P., Willems,L., Taipale,M., Jacob,Y., Hao,T., Hill,D.E.,
            Brun,C., Twizere,J.C., Krappmann,D., Heinig,M., Falter,C., Aloy,P.,
            Demeret,C., Vidal,M., Calderwood,M.A., Roth,F.P. and
            Falter-Braun,P.
  TITLE     A proteome-scale map of the SARS-CoV-2-human contactome
  JOURNAL   Nat Biotechnol 41 (1), 140-149 (2023)
   PUBMED   36217029
REFERENCE   4  (residues 1 to 360)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 360)
  AUTHORS   Dgany,O., Avidan,N., Delaunay,J., Krasnov,T., Shalmon,L.,
            Shalev,H., Eidelitz-Markus,T., Kapelushnik,J., Cattan,D.,
            Pariente,A., Tulliez,M., Cretien,A., Schischmanoff,P.O.,
            Iolascon,A., Fibach,E., Koren,A., Rossler,J., Le Merrer,M.,
            Yaniv,I., Zaizov,R., Ben-Asher,E., Olender,T., Lancet,D.,
            Beckmann,J.S. and Tamary,H.
  TITLE     Congenital dyserythropoietic anemia type I is caused by mutations
            in codanin-1
  JOURNAL   Am J Hum Genet 71 (6), 1467-1474 (2002)
   PUBMED   12434312
REFERENCE   6  (residues 1 to 360)
  AUTHORS   Chang,M.S., Chen,C.Y., Yeh,H.I., Fan,C.C., Huang,C.J. and Yang,Y.C.
  TITLE     Cloning, expression, and genomic organization of mouse mp29 gene
  JOURNAL   Biochem Biophys Res Commun 299 (2), 241-246 (2002)
   PUBMED   12437976
REFERENCE   7  (residues 1 to 360)
  AUTHORS   Chang,M.S., Chang,C.L., Huang,C.J. and Yang,Y.C.
  TITLE     p29, a novel GCIP-interacting protein, localizes in the nucleus
  JOURNAL   Biochem Biophys Res Commun 279 (2), 732-737 (2000)
   PUBMED   11118353
REFERENCE   8  (residues 1 to 360)
  AUTHORS   Terai,S., Aoki,H., Ashida,K. and Thorgeirsson,S.S.
  TITLE     Human homologue of maid: A dominant inhibitory helix-loop-helix
            protein associated with liver-specific gene expression
  JOURNAL   Hepatology 32 (2), 357-366 (2000)
   PUBMED   10915743
REFERENCE   9  (residues 1 to 360)
  AUTHORS   Xia,C., Bao,Z., Tabassam,F., Ma,W., Qiu,M., Hua,S. and Liu,M.
  TITLE     GCIP, a novel human grap2 and cyclin D interacting protein,
            regulates E2F-mediated transcriptional activity
  JOURNAL   J Biol Chem 275 (27), 20942-20948 (2000)
   PUBMED   10801854
REFERENCE   10 (residues 1 to 360)
  AUTHORS   Yao,Y., Doki,Y., Jiang,W., Imoto,M., Venkatraj,V.S., Warburton,D.,
            Santella,R.M., Lu,B., Yan,L., Sun,X.H., Su,T., Luo,J. and
            Weinstein,I.B.
  TITLE     Cloning and characterization of DIP1, a novel protein that is
            related to the Id family of proteins
  JOURNAL   Exp Cell Res 257 (1), 22-32 (2000)
   PUBMED   10854051
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA210890.1, AF132034.1,
            AC068724.7 and AI953224.1.
            
            On Apr 25, 2009 this sequence version replaced NP_036274.2.
            
            Summary: This gene was identified by the interaction of its gene
            product with Grap2, a leukocyte-specific adaptor protein important
            for immune cell signaling. The protein encoded by this gene was
            shown to interact with cyclin D. Transfection of this gene in cells
            was reported to reduce the phosphorylation of Rb gene product by
            cyclin D-dependent protein kinase, and inhibit E2F1-mediated
            transcription activity. This protein was also found to interact
            with helix-loop-helix protein E12 and is thought to be a negative
            regulator of liver-specific gene expression. Several alternatively
            spliced variants have been found for this gene. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the supported protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.484140.1,
                                           SRR1803613.266684.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300213.9/ ENSP00000300213.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..360
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.2"
     Protein         1..360
                     /product="cyclin-D1-binding protein 1"
                     /note="human homolog of Maid; grap2 and
                     cyclin-D-interacting protein; cyclin D-type
                     binding-protein 1; D-type cyclin-interacting protein 1"
                     /calculated_mol_wt=40131
     Region          2..208
                     /region_name="Required for interaction with CCND1"
                     /note="propagated from UniProtKB/Swiss-Prot (O95273.2)"
     Region          2..190
                     /region_name="Interaction with RPLP0.
                     /evidence=ECO:0000269|PubMed:17621266"
                     /note="propagated from UniProtKB/Swiss-Prot (O95273.2)"
     Region          2..184
                     /region_name="Interaction with TCF3.
                     /evidence=ECO:0000269|PubMed:10915743"
                     /note="propagated from UniProtKB/Swiss-Prot (O95273.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (O95273.2)"
     Region          55..320
                     /region_name="GCIP"
                     /note="Grap2 and cyclin-D-interacting; pfam13324"
                     /db_xref="CDD:463844"
     Region          150..360
                     /region_name="Interaction with TCF3.
                     /evidence=ECO:0000269|PubMed:10915743"
                     /note="propagated from UniProtKB/Swiss-Prot (O95273.2)"
     Region          240..360
                     /region_name="Interaction with RPLP0.
                     /evidence=ECO:0000269|PubMed:17621266"
                     /note="propagated from UniProtKB/Swiss-Prot (O95273.2)"
     CDS             1..360
                     /gene="CCNDBP1"
                     /gene_synonym="DIP1; GCIP; HHM"
                     /coded_by="NM_012142.5:97..1179"
                     /db_xref="CCDS:CCDS10092.1"
                     /db_xref="GeneID:23582"
                     /db_xref="HGNC:HGNC:1587"
                     /db_xref="MIM:607089"
ORIGIN      
        1 masatapaaa vptlaspleq lrhlaeelrl llprvrvgea qetteefnre mfwrrlneaa
       61 vtvsreattl tivfsqlplp spqetqkfce qvhaaikafi avyyllpkdq gitlrklvrg
      121 atldivdgma qlmevlsvtp tqspenndli synsvwvacq qmpqiprdnk aaallmltkn
      181 vdfvkdahee meqaveecdp ysgllndtee nnsdnhnhed dvlgfpsnqd lywseddqel
      241 iipclalvra skaclkkirm lvaengkkdq vaqlddivdi sdeispsvdd lalsiyppmc
      301 hltvrinsak lvsvlkkale itkashvtpq pedswiplli naidhcmnri keltqselel
//
LOCUS       NP_004590               1141 aa            linear   PRI 20-NOV-2025
DEFINITION  sterol regulatory element-binding protein 2 [Homo sapiens].
ACCESSION   NP_004590
VERSION     NP_004590.2
DBSOURCE    REFSEQ: accession NM_004599.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Moulton,M.J., Atala,K., Zheng,Y., Dutta,D., Grange,D.K., Lin,W.W.,
            Wegner,D.J., Wambach,J.A., Duker,A.L., Bober,M.B., Kratz,L.,
            Wise,C.A., Oxendine,I., Khanshour,A., Wangler,M.F., Yamamoto,S.,
            Cole,F.S., Rios,J. and Bellen,H.J.
  CONSRTM   Undiagnosed Diseases Network
  TITLE     Dominant missense variants in SREBF2 are associated with complex
            dermatological, neurological, and skeletal abnormalities
  JOURNAL   Genet Med 26 (9), 101174 (2024)
   PUBMED   38847193
  REMARK    GeneRIF: Dominant missense variants in SREBF2 are associated with
            complex dermatological, neurological, and skeletal abnormalities.
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Li,J., Sun,J., Xu,M., Yang,L., Yang,N., Deng,J., Ma,Y., Qi,Y.,
            Liu,Z., Ruan,Q., Liu,Y. and Huang,Y.
  TITLE     Human cytomegalovirus infection impairs neural differentiation via
            repressing sterol regulatory element binding protein 2-mediated
            cholesterol biosynthesis
  JOURNAL   Cell Mol Life Sci 81 (1), 289 (2024)
   PUBMED   38970696
  REMARK    GeneRIF: Human cytomegalovirus infection impairs neural
            differentiation via repressing sterol regulatory element binding
            protein 2-mediated cholesterol biosynthesis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Xiong,Y., Luo,J., Hong,Z.Y., Zhu,W.Z., Hu,A. and Song,B.L.
  TITLE     Hyperactivation of SREBP induces pannexin-1-dependent lytic cell
            death
  JOURNAL   J Lipid Res 65 (7), 100579 (2024)
   PUBMED   38880128
  REMARK    GeneRIF: Hyperactivation of SREBP induces pannexin-1-dependent
            lytic cell death.
REFERENCE   4  (residues 1 to 1141)
  AUTHORS   Plebanek,M.P., Xue,Y., Nguyen,Y.V., DeVito,N.C., Wang,X.,
            Holtzhausen,A., Beasley,G.M., Theivanthiran,B. and Hanks,B.A.
  TITLE     A lactate-SREBP2 signaling axis drives tolerogenic dendritic cell
            maturation and promotes cancer progression
  JOURNAL   Sci Immunol 9 (95), eadi4191 (2024)
   PUBMED   38728412
  REMARK    GeneRIF: A lactate-SREBP2 signaling axis drives tolerogenic
            dendritic cell maturation and promotes cancer progression.
REFERENCE   5  (residues 1 to 1141)
  AUTHORS   Miserez,A.R., Cao,G., Probst,L.C. and Hobbs,H.H.
  TITLE     Structure of the human gene encoding sterol regulatory element
            binding protein 2 (SREBF2)
  JOURNAL   Genomics 40 (1), 31-40 (1997)
   PUBMED   9070916
REFERENCE   6  (residues 1 to 1141)
  AUTHORS   Hua,X., Sakai,J., Brown,M.S. and Goldstein,J.L.
  TITLE     Regulated cleavage of sterol regulatory element binding proteins
            requires sequences on both sides of the endoplasmic reticulum
            membrane
  JOURNAL   J Biol Chem 271 (17), 10379-10384 (1996)
   PUBMED   8626610
REFERENCE   7  (residues 1 to 1141)
  AUTHORS   Wang,X., Zelenski,N.G., Yang,J., Sakai,J., Brown,M.S. and
            Goldstein,J.L.
  TITLE     Cleavage of sterol regulatory element binding proteins (SREBPs) by
            CPP32 during apoptosis
  JOURNAL   EMBO J 15 (5), 1012-1020 (1996)
   PUBMED   8605870
REFERENCE   8  (residues 1 to 1141)
  AUTHORS   Hua,X., Wu,J., Goldstein,J.L., Brown,M.S. and Hobbs,H.H.
  TITLE     Structure of the human gene encoding sterol regulatory element
            binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to
            chromosomes 17p11.2 and 22q13
  JOURNAL   Genomics 25 (3), 667-673 (1995)
   PUBMED   7759101
REFERENCE   9  (residues 1 to 1141)
  AUTHORS   Hua,X., Yokoyama,C., Wu,J., Briggs,M.R., Brown,M.S., Goldstein,J.L.
            and Wang,X.
  TITLE     SREBP-2, a second basic-helix-loop-helix-leucine zipper protein
            that stimulates transcription by binding to a sterol regulatory
            element
  JOURNAL   Proc Natl Acad Sci U S A 90 (24), 11603-11607 (1993)
   PUBMED   7903453
REFERENCE   10 (residues 1 to 1141)
  AUTHORS   Yokoyama,C., Wang,X., Briggs,M.R., Admon,A., Wu,J., Hua,X.,
            Goldstein,J.L. and Brown,M.S.
  TITLE     SREBP-1, a basic-helix-loop-helix-leucine zipper protein that
            controls transcription of the low density lipoprotein receptor gene
  JOURNAL   Cell 75 (1), 187-197 (1993)
   PUBMED   8402897
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL021453.1, BC051799.1,
            Z99716.4 and AA035591.1.
            
            On Jan 3, 2003 this sequence version replaced NP_004590.1.
            
            Summary: This gene encodes a member of the a ubiquitously expressed
            transcription factor that controls cholesterol homeostasis by
            regulating transcription of sterol-regulated genes. The encoded
            protein contains a basic helix-loop-helix-leucine zipper (bHLH-Zip)
            domain and binds the sterol regulatory element 1 motif. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) encodes the functional
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC051799.1, BC056158.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361204.9/ ENSP00000354476.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.2"
     Protein         1..1141
                     /product="sterol regulatory element-binding protein 2"
                     /note="class D basic helix-loop-helix protein 2"
                     /calculated_mol_wt=123557
     mat_peptide     1..484
                     /product="Processed sterol regulatory element-binding
                     protein 2. /evidence=ECO:0000305|PubMed:10805775,
                     ECO:0000305|PubMed:9651382. /id=PRO_0000314033"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
                     /calculated_mol_wt=51777
     Region          1..50
                     /region_name="Transcriptional activation (acidic).
                     /evidence=ECO:0000269|PubMed:35120642"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Region          48..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Region          237..491
                     /region_name="Interaction with LMNA.
                     /evidence=ECO:0000250|UniProtKB:Q3U1N2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Region          326..402
                     /region_name="bHLHzip_SREBP2"
                     /note="basic Helix-Loop-Helix-zipper (bHLHzip) domain
                     found in sterol regulatory element-binding protein 2
                     (SREBP2) and similar proteins; cd18922"
                     /db_xref="CDD:381492"
     Site            order(326,332,334..336,338..339,341..343,347,365..366)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381492"
     Site            order(342,345..346,349..350,352..353,356,366..367,
                     370..371,374,376..378,380..381,383..384,387..388,390..391,
                     394..395,398)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381492"
     Region          380..401
                     /region_name="Leucine-zipper"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Site            468..469
                     /site_type="cleavage"
                     /note="Cleavage, by caspase-3 and caspase-7.
                     /evidence=ECO:0000269|PubMed:8643593; propagated from
                     UniProtKB/Swiss-Prot (Q12772.2)"
     Site            480..500
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Site            484..485
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS2.
                     /evidence=ECO:0000269|PubMed:10805775,
                     ECO:0000269|PubMed:9651382; propagated from
                     UniProtKB/Swiss-Prot (Q12772.2)"
     Site            522..523
                     /site_type="cleavage"
                     /note="Cleavage, by MBTPS1.
                     /evidence=ECO:0000269|PubMed:10805775; propagated from
                     UniProtKB/Swiss-Prot (Q12772.2)"
     Site            534..554
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12772.2)"
     Site            855
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12772.2)"
     Site            1098
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q12772.2)"
     CDS             1..1141
                     /gene="SREBF2"
                     /gene_synonym="bHLHd2; SREBP-2; SREBP2"
                     /coded_by="NM_004599.4:167..3592"
                     /db_xref="CCDS:CCDS14023.1"
                     /db_xref="GeneID:6721"
                     /db_xref="HGNC:HGNC:11290"
                     /db_xref="MIM:600481"
ORIGIN      
        1 mddsgelggl etmetltelg deltlgdide mlqfvsnqvg efpdlfseql cssfpgsggs
       61 gsssgssgss ssssngrgss sgavdpsvqr sftqvtlpsf spsaaspqap tlqvkvspts
      121 vpttpratpi lqprpqpqpq pqtqlqqqtv mitptfsttp qtriiqqpli yqnaatsfqv
      181 lqpqvqslvt ssqvqpvtiq qqvqtvqaqr vltqtangtl qtlapatvqt vaapqvqqvp
      241 vlvqpqiikt dslvlttlkt dgspvmaavq npaltalttp iqtaalqvpt lvgssgtilt
      301 tmpvmmgqek vpikqvpggv kqleppkege rrtthniiek ryrssindki ielkdlvmgt
      361 dakmhksgvl rkaidyikyl qqvnhklrqe nmvlklanqk nkllkgidlg slvdnevdlk
      421 iedfnqnvll msppasdsgs qagfspysid sepgsplldd akvkdepdsp pvalgmvdrs
      481 rillcvltfl clsfnpltsl lqwggahdsd qhphsgsgrs vlsfesgsgg wfdwmmptll
      541 lwlvngvivl svfvkllvhg epvirphsrs svtfwrhrkq adldlargdf aaaagnlqtc
      601 lavlgralpt srldlacsls wnviryslqk lrlvrwllkk vfqcrratpa teagfedeak
      661 tsardaalay hrlhqlhitg klpagsacsd vhmalcavnl aecaeekipp stlveihlta
      721 amglktrcgg klgflasyfl sraqslcgpe hsavpdslrw lchplgqkff merswsvksa
      781 akeslycaqr npadpiaqvh qafcknller aieslvkpqa kkkagdqeee scefssaley
      841 lkllhsfvds vgvmspplsr ssvlksalgp diicrwwtsa itvaiswlqg ddaavrshft
      901 kveripkale vtesplvkai fhacramhas lpgkadgqqs sfchcerasg hlwsslnvsg
      961 atsdpalnhv vqlltcdlll slrtalwqkq asasqavget yhasgaelag fqrdlgslrr
     1021 lahsfrpayr kvflheatvr lmagasptrt hqllehslrr rttqstkhge vdawpgqrer
     1081 ataillacrh lplsflsspg qravllaeaa rtlekvgdrr scndcqqmiv klgggtaiaa
     1141 s
//
LOCUS       NP_003644                423 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 3 isoform 1 [Homo sapiens].
ACCESSION   NP_003644
VERSION     NP_003644.2
DBSOURCE    REFSEQ: accession NM_003653.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Niu,J., Yan,T., Guo,W., Wang,W., Ren,T., Huang,Y., Zhao,Z., Yu,Y.,
            Chen,C., Huang,Q., Lou,J. and Guo,L.
  TITLE     The COPS3-FOXO3 positive feedback loop regulates autophagy to
            promote cisplatin resistance in osteosarcoma
  JOURNAL   Autophagy 19 (6), 1693-1710 (2023)
   PUBMED   36451342
  REMARK    GeneRIF: The COPS3-FOXO3 positive feedback loop regulates autophagy
            to promote cisplatin resistance in osteosarcoma.
REFERENCE   3  (residues 1 to 423)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 423)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 423)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (residues 1 to 423)
  AUTHORS   Liu,W., Nichols,A.F., Graham,J.A., Dualan,R., Abbas,A. and Linn,S.
  TITLE     Nuclear transport of human DDB protein induced by ultraviolet light
  JOURNAL   J Biol Chem 275 (28), 21429-21434 (2000)
   PUBMED   10777491
REFERENCE   7  (residues 1 to 423)
  AUTHORS   Bianchi,E., Denti,S., Granata,A., Bossi,G., Geginat,J., Villa,A.,
            Rogge,L. and Pardi,R.
  TITLE     Integrin LFA-1 interacts with the transcriptional co-activator JAB1
            to modulate AP-1 activity
  JOURNAL   Nature 404 (6778), 617-621 (2000)
   PUBMED   10766246
REFERENCE   8  (residues 1 to 423)
  AUTHORS   Potocki,L., Chen,K.S. and Lupski,J.R.
  TITLE     Subunit 3 of the COP9 signal transduction complex is conserved from
            plants to humans and maps within the smith-magenis syndrome
            critical region in 17p11.2
  JOURNAL   Genomics 57 (1), 180-182 (1999)
   PUBMED   10191102
REFERENCE   9  (residues 1 to 423)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   10 (residues 1 to 423)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC001891.1, AC055811.20 and
            BU952436.1.
            
            On Sep 20, 2002 this sequence version replaced NP_003644.1.
            
            Summary: The protein encoded by this gene possesses kinase activity
            that phosphorylates regulators involved in signal transduction. It
            phosphorylates I kappa-Balpha, p105, and c-Jun. It acts as a
            docking site for complex-mediated phosphorylation. The gene is
            located within the Smith-Magenis syndrome region on chromosome 17.
            Several transcript variants encoding different isoforms have been
            found for this gene. [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.110326.1,
                                           SRR1660805.212192.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000268717.10/ ENSP00000268717.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p11.2"
     Protein         1..423
                     /product="COP9 signalosome complex subunit 3 isoform 1"
                     /note="COP9 complex subunit 3; JAB1-containing signalosome
                     subunit 3; COP9 signalosome complex subunit 3; COP9
                     constitutive photomorphogenic homolog subunit 3"
                     /calculated_mol_wt=47742
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:18850735, ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UNS2.3)"
     Region          259..362
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     Region          402..423
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UNS2.3)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O88543; propagated from
                     UniProtKB/Swiss-Prot (Q9UNS2.3)"
     Site            410
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UNS2.3)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:18850735,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q9UNS2.3)"
     CDS             1..423
                     /gene="COPS3"
                     /gene_synonym="CSN3; SGN3"
                     /coded_by="NM_003653.4:61..1332"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11183.1"
                     /db_xref="GeneID:8533"
                     /db_xref="HGNC:HGNC:2239"
                     /db_xref="MIM:604665"
ORIGIN      
        1 masaleqfvn svrqlsaqgq mtqlcelink sgellaknls hldtvlgald vqehslgvla
       61 vlfvkfsmps vpdfetlfsq vqlfistcng ehiryatdtf aglchqltna lverkqplrg
      121 igilkqaidk mqmntnqlts ihadlcqlcl lakcfkpalp yldvdmmdic kengaydakh
      181 flcyyyyggm iytglknfer alyfyeqait tpamavshim lesykkyilv slillgkvqq
      241 lpkytsqivg rfikplsnay helaqvystn npselrnlvn khsetftrdn nmglvkqcls
      301 slykkniqrl tktfltlslq dmasrvqlsg pqeaekyvlh miedgeifas inqkdgmvsf
      361 hdnpekynnp amlhnidqem lkcielderl kamdqeitvn pqfvqksmgs qeddsgnkps
      421 sys
//
LOCUS       NP_001009939             346 aa            linear   PRI 20-NOV-2025
DEFINITION  septin-5 isoform 2 [Homo sapiens].
ACCESSION   NP_001009939
VERSION     NP_001009939.1
DBSOURCE    REFSEQ: accession NM_001009939.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Marttinen,M., Ferreira,C.B., Paldanius,K.M.A., Takalo,M.,
            Natunen,T., Makinen,P., Leppanen,L., Leinonen,V., Tanigaki,K.,
            Kang,G., Hiroi,N., Soininen,H., Rilla,K., Haapasalo,A. and
            Hiltunen,M.
  TITLE     Presynaptic Vesicle Protein SEPTIN5 Regulates the Degradation of
            APP C-Terminal Fragments and the Levels of Abeta
  JOURNAL   Cells 9 (11), 2482 (2020)
   PUBMED   33203136
  REMARK    GeneRIF: Presynaptic Vesicle Protein SEPTIN5 Regulates the
            Degradation of APP C-Terminal Fragments and the Levels of Abeta.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Caltagarone,J., Rhodes,J., Honer,W.G. and Bowser,R.
  TITLE     Localization of a novel septin protein, hCDCrel-1, in neurons of
            human brain
  JOURNAL   Neuroreport 9 (12), 2907-2912 (1998)
   PUBMED   9760144
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Yagi,M., Zieger,B., Roth,G.J. and Ware,J.
  TITLE     Structure and expression of the human septin gene HCDCREL-1
  JOURNAL   Gene 212 (2), 229-236 (1998)
   PUBMED   9611266
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Hsu,S.C., Hazuka,C.D., Roth,R., Foletti,D.L., Heuser,J. and
            Scheller,R.H.
  TITLE     Subunit composition, protein interactions, and structures of the
            mammalian brain sec6/8 complex and septin filaments
  JOURNAL   Neuron 20 (6), 1111-1122 (1998)
   PUBMED   9655500
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Megonigal,M.D., Rappaport,E.F., Jones,D.H., Williams,T.M.,
            Lovett,B.D., Kelly,K.M., Lerou,P.H., Moulton,T., Budarf,M.L. and
            Felix,C.A.
  TITLE     t(11;22)(q23;q11.2) In acute myeloid leukemia of infant twins fuses
            MLL with hCDCrel, a cell division cycle gene in the genomic region
            of deletion in DiGeorge and velocardiofacial syndromes
  JOURNAL   Proc Natl Acad Sci U S A 95 (11), 6413-6418 (1998)
   PUBMED   9600980
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Aug 18;95(17):10344]
REFERENCE   9  (residues 1 to 346)
  AUTHORS   McKie,J.M., Sutherland,H.F., Harvey,E., Kim,U.J. and Scambler,P.J.
  TITLE     A human gene similar to Drosophila melanogaster peanut maps to the
            DiGeorge syndrome region of 22q11
  JOURNAL   Hum Genet 101 (1), 6-12 (1997)
   PUBMED   9385360
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Zieger,B., Hashimoto,Y. and Ware,J.
  TITLE     Alternative expression of platelet glycoprotein Ib(beta) mRNA from
            an adjacent 5' gene with an imperfect polyadenylation signal
            sequence
  JOURNAL   J Clin Invest 99 (3), 520-525 (1997)
   PUBMED   9022087
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI601927.1, AK056273.1 and
            AC000093.5.
            
            Summary: This gene is a member of the septin gene family of
            nucleotide binding proteins, originally described in yeast as cell
            division cycle regulatory proteins. Septins are highly conserved in
            yeast, Drosophila, and mouse and appear to regulate cytoskeletal
            organization. Disruption of septin function disturbs cytokinesis
            and results in large multinucleate or polyploid cells. This gene is
            mapped to 22q11, the region frequently deleted in DiGeorge and
            velocardiofacial syndromes. A translocation involving the MLL gene
            and this gene has also been reported in patients with acute myeloid
            leukemia. Alternative splicing results in multiple transcript
            variants. The presence of a non-consensus polyA signal (AACAAT) in
            this gene also results in read-through transcription into the
            downstream neighboring gene (GP1BB; platelet glycoprotein Ib),
            whereby larger, non-coding transcripts are produced. [provided by
            RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and uses an alternate start codon,
            compared to variant 1. The encoded isoform 2 has a shorter and
            distinct N-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK056273.1, SRR1803614.236440.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..346
                     /product="septin-5 isoform 2"
                     /EC_number="3.1.5.1"
                     /note="peanut-like 1; cell division control related
                     protein 1; platelet glycoprotein Ib beta chain"
                     /calculated_mol_wt=39201
     Region          51..280
                     /region_name="Septin"
                     /note="pfam00735"
                     /db_xref="CDD:395596"
     Site            60..67
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206649"
     Site            order(62..68,117,120,198..199,201,257..258)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206649"
     Site            92..100
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206649"
     Site            94
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206649"
     Site            117..120
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206649"
     Site            order(119..154,155..164)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206649"
     Site            198..201
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206649"
     Site            257..259
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206649"
     CDS             1..346
                     /gene="SEPTIN5"
                     /gene_synonym="CDCREL; CDCREL-1; CDCREL1; H5; HCDCREL-1;
                     PNUTL1; SEPT5; Septin-5"
                     /coded_by="NM_001009939.3:296..1336"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56224.1"
                     /db_xref="GeneID:5413"
                     /db_xref="HGNC:HGNC:9164"
                     /db_xref="MIM:602724"
ORIGIN      
        1 mdslaapqdr lveqllsprt qaqrrlkdid kqyvgfatlp nqvhrksvkk gfdftlmvag
       61 esglgkstlv hslfltdlyk drkllsaeer isqtveilkh tvdieekgvk lkltivdtpg
      121 fgdavnntec wkpitdyvdq qfeqyfrdes glnrkniqdn rvhcclyfis pfghglrpvd
      181 vgfmkalhek vnivpliaka dclvpseirk lkerireeid kfgihvyqfp ecdsdededf
      241 kqqdrelkes apfavigsnt vveakgqrvr grlypwgive galrlreaaq hahphayarp
      301 qgrdvrralr elpralhpad dqqtdpgqph gephpdpaaa hpgrrd
//
LOCUS       NP_000930                267 aa            linear   PRI 20-NOV-2025
DEFINITION  pro-opiomelanocortin preproprotein [Homo sapiens].
ACCESSION   NP_000930
VERSION     NP_000930.1
DBSOURCE    REFSEQ: accession NM_000939.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 267)
  AUTHORS   Santana,C.V.N., Magno,L.A.V., Ramos,A.V., Rios,M.A., Sandrim,V.C.,
            De Marco,L.A., de Miranda,D.M. and Romano-Silva,M.A.
  TITLE     Genetic Variations in AMPK, FOXO3A, and POMC Increase the Risk of
            Extreme Obesity
  JOURNAL   J Obes 2024, 3813621 (2024)
   PUBMED   39484290
  REMARK    GeneRIF: Genetic Variations in AMPK, FOXO3A, and POMC Increase the
            Risk of Extreme Obesity.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 267)
  AUTHORS   Bando,H., Yamamoto,M., Urai,S., Motomura,Y., Sasaki,Y., Ohmachi,Y.,
            Kobatake,M., Tsujimoto,Y., Oi-Yo,Y., Suzuki,M., Yamamoto,N.,
            Takahashi,M., Fukuoka,H., Iguchi,G. and Ogawa,W.
  TITLE     Fluctuations in plasma adrenocorticotropic hormone concentration
            may predict the onset of immune checkpoint inhibitor-related
            hypophysitis
  JOURNAL   J Immunother Cancer 12 (2), e008634 (2024)
   PUBMED   38418395
  REMARK    GeneRIF: Fluctuations in serum adrenocorticotropic hormone
            concentration may predict the onset of immune checkpoint
            inhibitor-related hypophysitis.
            Erratum:[J Immunother Cancer. 2024 Mar 29;12(3):e008634corr1. doi:
            10.1136/jitc-2023-008634corr1. PMID: 38553010]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 267)
  AUTHORS   Singh,M. and Mukhopadhyay,K.
  TITLE     Alpha-melanocyte stimulating hormone: an emerging anti-inflammatory
            antimicrobial peptide
  JOURNAL   Biomed Res Int 2014, 874610 (2014)
   PUBMED   25140322
  REMARK    Review article
REFERENCE   4  (residues 1 to 267)
  AUTHORS   Pritchard,L.E. and White,A.
  TITLE     Neuropeptide processing and its impact on melanocortin pathways
  JOURNAL   Endocrinology 148 (9), 4201-4207 (2007)
   PUBMED   17584964
  REMARK    Review article
REFERENCE   5  (residues 1 to 267)
  AUTHORS   Raffin-Sanson,M.L., de Keyzer,Y. and Bertagna,X.
  TITLE     Proopiomelanocortin, a polypeptide precursor with multiple
            functions: from physiology to pathological conditions
  JOURNAL   Eur J Endocrinol 149 (2), 79-90 (2003)
   PUBMED   12887283
  REMARK    GeneRIF: POMC has become a paradigmatic polypeptide precursor model
            illustrating the variable roles of a single gene and its various
            products in different localities--review
            Review article
REFERENCE   6  (residues 1 to 267)
  AUTHORS   Challis,B.G. and Millington,G.W.M.
  TITLE     Proopiomelanocortin Deficiency - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24354022
REFERENCE   7  (residues 1 to 267)
  AUTHORS   Mountjoy,K.G., Robbins,L.S., Mortrud,M.T. and Cone,R.D.
  TITLE     The cloning of a family of genes that encode the melanocortin
            receptors
  JOURNAL   Science 257 (5074), 1248-1251 (1992)
   PUBMED   1325670
REFERENCE   8  (residues 1 to 267)
  AUTHORS   Takahashi,H., Hakamata,Y., Watanabe,Y., Kikuno,R., Miyata,T. and
            Numa,S.
  TITLE     Complete nucleotide sequence of the human
            corticotropin-beta-lipotropin precursor gene
  JOURNAL   Nucleic Acids Res 11 (19), 6847-6858 (1983)
   PUBMED   6314261
REFERENCE   9  (residues 1 to 267)
  AUTHORS   Dragon,N., Seidah,N.G., Lis,M., Routhier,R. and Chretien,M.
  TITLE     Primary structure and morphine-like activity of human
            beta-endorphin
  JOURNAL   Can J Biochem 55 (6), 666-670 (1977)
   PUBMED   195688
REFERENCE   10 (residues 1 to 267)
  AUTHORS   Li,C.H. and Chung,D.
  TITLE     Primary structure of human beta-lipotropin
  JOURNAL   Nature 260 (5552), 622-624 (1976)
   PUBMED   1264228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY050419.1, CD108235.1,
            BC065832.1 and T29537.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a preproprotein that undergoes
            extensive, tissue-specific, post-translational processing via
            cleavage by subtilisin-like enzymes known as prohormone
            convertases. There are eight potential cleavage sites within the
            preproprotein and, depending on tissue type and the available
            convertases, processing may yield as many as ten biologically
            active peptides involved in diverse cellular functions. The encoded
            protein is synthesized mainly in corticotroph cells of the anterior
            pituitary where four cleavage sites are used; adrenocorticotrophin,
            essential for normal steroidogenesis and the maintenance of normal
            adrenal weight, and lipotropin beta are the major end products. In
            other tissues, including the hypothalamus, placenta, and
            epithelium, all cleavage sites may be used, giving rise to peptides
            with roles in pain and energy homeostasis, melanocyte stimulation,
            and immune modulation. These include several distinct
            melanotropins, lipotropins, and endorphins that are contained
            within the adrenocorticotrophin and beta-lipotropin peptides. The
            antimicrobial melanotropin alpha peptide exhibits antibacterial and
            antifungal activity. Mutations in this gene have been associated
            with early onset obesity, adrenal insufficiency, and red hair
            pigmentation. Alternatively spliced transcript variants encoding
            the same protein have been described. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 3. Variants 1-4 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.394204.1, CD513772.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000395826.7/
                                                  ENSP00000379170.2
            Protein has antimicrobial activity :: PMID: 25140322
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..267
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p23.3"
     Protein         1..267
                     /product="pro-opiomelanocortin preproprotein"
                     /note="met-enkephalin; melanotropin gamma; gamma-MSH;
                     adrenocorticotropic hormone; melanotropin alpha;
                     alpha-MSH; corticotropin-like intermediary peptide;
                     lipotropin beta; beta-LPH; lipotropin gamma; gamma-LPH;
                     melanotropin beta; beta-MSH; beta-endorphin;
                     alpha-melanocyte-stimulating hormone; pro-ACTH-endorphin;
                     beta-melanocyte-stimulating hormone; adrenocorticotropin;
                     proopiomelanocortin preproprotein;
                     corticotropin-lipotropin; opiomelanocortin prepropeptide"
                     /calculated_mol_wt=26679
     sig_peptide     1..26
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2763
     mat_peptide     27..102
                     /product="NPP. /id=PRO_0000024966"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=8469
     Region          28..70
                     /region_name="NPP"
                     /note="Pro-opiomelanocortin, N-terminal region; pfam08384"
                     /db_xref="CDD:429962"
     Site            71
                     /site_type="glycosylation"
                     /note="O-linked (HexNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:6267033; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Region          74..91
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     mat_peptide     77..87
                     /product="Melanotropin gamma.
                     /evidence=ECO:0000269|PubMed:2839146. /id=PRO_0000024967"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=1514
     Site            87
                     /site_type="amidation"
                     /note="Phenylalanine amide. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P01189.2)"
     Region          88..175
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     Site            91
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     105..134
                     /product="Potential peptide. /id=PRO_0000024968"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=3006
     Site            134
                     /site_type="amidation"
                     /note="Glutamic acid 1-amide.
                     /evidence=ECO:0000269|PubMed:6272808; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Region          136..154
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     mat_peptide     138..176
                     /product="Corticotropin. /id=PRO_0000024969"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=4541
     mat_peptide     138..150
                     /product="Melanotropin alpha"
                     /experiment="DESCRIPTION:antimicrobial
                     peptide[PMID:25140322]"
                     /exception="alternative processing"
                     /note="occurs in cells other than corticotroph cells of
                     the anterior pituitary"
                     /calculated_mol_wt=1624
     Site            138
                     /site_type="acetylation"
                     /note="N-acetylserine, in Corticotropin.
                     /evidence=ECO:0000250|UniProtKB:P01191; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     Site            150
                     /site_type="amidation"
                     /note="Valine amide. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     156..176
                     /product="Corticotropin-like intermediary peptide.
                     /id=PRO_0000024971"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=2310
     Site            168
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16807684; propagated from
                     UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     179..267
                     /product="Lipotropin beta. /id=PRO_0000024972"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=9806
     mat_peptide     179..234
                     /product="Lipotropin gamma. /id=PRO_0000024973"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=6075
     Region          181..200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     217..234
                     /product="Melanocyte-stimulating hormone beta.
                     /id=PRO_0000024974"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=2204
     Region          218..236
                     /region_name="ACTH_domain"
                     /note="Corticotropin ACTH domain; pfam00976"
                     /db_xref="CDD:460014"
     Region          222..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
     mat_peptide     237..267
                     /product="Beta-endorphin. /id=PRO_0000024975"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=3465
     Region          237..264
                     /region_name="Op_neuropeptide"
                     /note="Opioids neuropeptide; pfam08035"
                     /db_xref="CDD:462343"
     mat_peptide     237..241
                     /product="Met-enkephalin. /id=PRO_0000024976"
                     /note="propagated from UniProtKB/Swiss-Prot (P01189.2)"
                     /calculated_mol_wt=574
     CDS             1..267
                     /gene="POMC"
                     /gene_synonym="ACTH; CLIP; LPH; MSH; NPP; OBAIRH; POC"
                     /coded_by="NM_000939.4:104..907"
                     /db_xref="CCDS:CCDS1717.1"
                     /db_xref="GeneID:5443"
                     /db_xref="HGNC:HGNC:9201"
                     /db_xref="MIM:176830"
ORIGIN      
        1 mprsccsrsg alllalllqa smevrgwcle ssqcqdltte snllecirac kpdlsaetpm
       61 fpgngdeqpl tenprkyvmg hfrwdrfgrr nssssgssga gqkredvsag edcgplpegg
      121 peprsdgakp gpregkrsys mehfrwgkpv gkkrrpvkvy pngaedesae afplefkrel
      181 tgqrlregdg pdgpaddgag aqadlehsll vaaekkdegp yrmehfrwgs ppkdkryggf
      241 mtseksqtpl vtlfknaiik naykkge
//
LOCUS       NP_001120650             983 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI ethanolamine phosphate transferase 2, catalytic subunit isoform
            1 [Homo sapiens].
ACCESSION   NP_001120650
VERSION     NP_001120650.1
DBSOURCE    REFSEQ: accession NM_001127178.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 983)
  AUTHORS   Tremblay-Laganiere,C., Maroofian,R., Nguyen,T.T.M., Karimiani,E.G.,
            Kirmani,S., Akbar,F., Ibrahim,S., Afroze,B., Doosti,M.,
            Ashrafzadeh,F., Babaei,M., Efthymiou,S., Christoforou,M.,
            Sultan,T., Ladda,R.L., McLaughlin,H.M., Truty,R., Mahida,S.,
            Cohen,J.S., Baranano,K., Ismail,F.Y., Patel,M.S., Lehman,A.,
            Edmondson,A.C., Nagy,A., Walker,M.A., Mercimek-Andrews,S., Maki,Y.,
            Sachdev,R., Macintosh,R., Palmer,E.E., Mancini,G.M.S.,
            Barakat,T.S., Steinfeld,R., Rusch,C.T., Stettner,G.M., Wagner,M.,
            Wortmann,S.B., Kini,U., Brady,A.F., Stals,K.L., Ismayilova,N.,
            Ellard,S., Bernardo,D., Nugent,K., McLean,S.D., Antonarakis,S.E.,
            Houlden,H., Kinoshita,T., Campeau,P.M. and Murakami,Y.
  TITLE     PIGG variant pathogenicity assessment reveals characteristic
            features within 19 families
  JOURNAL   Genet Med 23 (10), 1873-1881 (2021)
   PUBMED   34113002
  REMARK    GeneRIF: PIGG variant pathogenicity assessment reveals
            characteristic features within 19 families.
REFERENCE   2  (residues 1 to 983)
  AUTHORS   Kinoshita,T.
  TITLE     Biosynthesis and biology of mammalian GPI-anchored proteins
  JOURNAL   Open Biol 10 (3), 190290 (2020)
   PUBMED   32156170
  REMARK    Review article
REFERENCE   3  (residues 1 to 983)
  AUTHORS   Parsamanesh,N., Safarpour,H., Etesam,S., Shadmehri,A.A. and
            Miri-Moghaddam,E.
  TITLE     Identification and In Silico Characterization of a Novel Point
            Mutation within the Phosphatidylinositol Glycan Anchor Biosynthesis
            Class G Gene in an Iranian Family with Intellectual Disability
  JOURNAL   J Mol Neurosci 69 (4), 538-545 (2019)
   PUBMED   31414351
  REMARK    GeneRIF: Arg658Gln mutation segregates with nonsyndromic
            intellectual disability in Iranian family.
REFERENCE   4  (residues 1 to 983)
  AUTHORS   Zhao,J.J., Halvardson,J., Knaus,A., Georgii-Hemming,P., Baeck,P.,
            Krawitz,P.M., Thuresson,A.C. and Feuk,L.
  TITLE     Reduced cell surface levels of GPI-linked markers in a new case
            with PIGG loss of function
  JOURNAL   Hum Mutat 38 (10), 1394-1401 (2017)
   PUBMED   28581210
  REMARK    GeneRIF: Based on genetic and functional evidence, we confirm that
            pathogenic variants in PIGG cause an intellectual disability
            syndrome, and we find that loss of function of PIGG is associated
            with Glycosylphosphatidylinositol deficiency
REFERENCE   5  (residues 1 to 983)
  AUTHORS   Huang,X., Dai,F.F., Gaisano,G., Giglou,K., Han,J., Zhang,M.,
            Kittanakom,S., Wong,V., Wei,L., Showalter,A.D., Sloop,K.W.,
            Stagljar,I. and Wheeler,M.B.
  TITLE     The identification of novel proteins that interact with the GLP-1
            receptor and restrain its activity
  JOURNAL   Mol Endocrinol 27 (9), 1550-1563 (2013)
   PUBMED   23864651
REFERENCE   6  (residues 1 to 983)
  AUTHORS   Yoshida,T., Kato,K., Yokoi,K., Oguri,M., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Association of genetic variants with hemorrhagic stroke in Japanese
            individuals
  JOURNAL   Int J Mol Med 25 (4), 649-656 (2010)
   PUBMED   20198315
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   7  (residues 1 to 983)
  AUTHORS   Oguri,M., Kato,K., Yokoi,K., Yoshida,T., Watanabe,S., Metoki,N.,
            Yoshida,H., Satoh,K., Aoyagi,Y., Nozawa,Y. and Yamada,Y.
  TITLE     Assessment of a polymorphism of SDK1 with hypertension in Japanese
            Individuals
  JOURNAL   Am J Hypertens 23 (1), 70-77 (2010)
   PUBMED   19851296
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 983)
  AUTHORS   Shishioh,N., Hong,Y., Ohishi,K., Ashida,H., Maeda,Y. and
            Kinoshita,T.
  TITLE     GPI7 is the second partner of PIG-F and involved in modification of
            glycosylphosphatidylinositol
  JOURNAL   J Biol Chem 280 (10), 9728-9734 (2005)
   PUBMED   15632136
REFERENCE   9  (residues 1 to 983)
  AUTHORS   Kinoshita,T. and Inoue,N.
  TITLE     Dissecting and manipulating the pathway for
            glycosylphos-phatidylinositol-anchor biosynthesis
  JOURNAL   Curr Opin Chem Biol 4 (6), 632-638 (2000)
   PUBMED   11102867
  REMARK    Review article
REFERENCE   10 (residues 1 to 983)
  AUTHORS   Battaglia,A., Carey,J.C. and South,S.T.
  TITLE     Wolf-Hirschhorn Syndrome - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301362
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA548833.1, AB162713.1,
            AL162084.1 and AC116565.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an enzyme involved in
            glycosylphosphatidylinositol-anchor biosynthesis. The encoded
            protein, which is localized to the endoplasmic reticulum, is
            involved in transferring ethanoloamine phosphate to mannose 2 of
            glycosylphosphatidylinositol species H7 to form species H8. Allelic
            variants of this gene have been associated with intellectual
            disability, hypotonia, and early-onset seizures. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Sep 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.43729.1,
                                           SRR1803617.104413.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000453061.7/ ENSP00000415203.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..983
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..983
                     /product="GPI ethanolamine phosphate transferase 2,
                     catalytic subunit isoform 1"
                     /note="GPI ethanolamine phosphate transferase 2;
                     phosphatidylinositol-glycan biosynthesis class G protein;
                     EMM blood group antigen; LAS21 (GPI7) homolog; GPI
                     ethanolamine phosphate transferase 2, catalytic subunit"
                     /calculated_mol_wt=108042
     Region          62..335
                     /region_name="GPI_EPT_2"
                     /note="GPI ethanolamine phosphate transferase 2; PIG-G;
                     cd16024"
                     /db_xref="CDD:293748"
     Site            order(74..75,115,219,268..269)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:293748"
     Site            order(74,115,219,269)
                     /site_type="other"
                     /note="putative substrate binding site [chemical binding]"
                     /db_xref="CDD:293748"
     Site            194
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            432..452
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            471..491
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            506..526
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            552..572
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            699..719
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            721..741
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            752..772
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            789..809
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Region          <803..965
                     /region_name="PIGO_PIGG"
                     /note="GPI ethanolamine phosphate transferase membrane
                     region; pfam19316"
                     /db_xref="CDD:437148"
     Site            812..832
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            879..899
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            919..939
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     Site            955..975
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5H8A4.1)"
     CDS             1..983
                     /gene="PIGG"
                     /gene_synonym="EMM; GPI7; LAS21; MRT53; NEDHSCA; PRO4405;
                     RLGS1930"
                     /coded_by="NM_001127178.3:127..3078"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS46992.1"
                     /db_xref="GeneID:54872"
                     /db_xref="HGNC:HGNC:25985"
                     /db_xref="MIM:616918"
ORIGIN      
        1 mrlgsgtfat ccvaievlgi avflrgffpa pvrssaraeh gaeppapeps agassnwttl
       61 ppplfskvvi vlidalrddf vfgskgvkfm pyttylvekg ashsfvaeak pptvtmprik
      121 almtgslpgf vdvirnlnsp alledsvirq akaagkrivf ygdetwvklf pkhfveydgt
      181 tsffvsdyte vdnnvtrhld kvlkrgdwdi lilhylgldh ighisgpnsp ligqklsemd
      241 svlmkihtsl qskeretplp nllvlcgdhg msetgshgas steevntpli lissaferkp
      301 gdirhpkhvq qtdvaatlai alglpipkds vgsllfpvve grpmreqlrf lhlntvqlsk
      361 llqenvpsye kdpgfeqfkm serlhgnwir lyleekhsev lfnlgskvlr qyldalktls
      421 lslsaqvaqy diysmmvgtv vvlevltlll lsvpqalrrk aelevplssp gfsllfylvi
      481 lvlsavhviv ctsaesscyf cglswlaagg vmvlasallc vivsvltnvl vggntprknp
      541 mhpssrwsel dllillgtag hvlslgassf veeehqtwyf lvntlclals qetyrnyflg
      601 ddgeppcglc veqghdgata awqdgpgcdv lerdkghgsp stsevlrgre kwmvlaspwl
      661 ilaccrllrs lnqtgvqwah rpdlghwlts sdhkaelsvl aalsllvvfv lvqrgcspvs
      721 kaalalgllg vycyraaigs vrfpwrpdsk diskgiiear fvyvfvlgil ftgtkdllks
      781 qviaadfklk tvglweiysg lvllaallfr phnlpvlafs lliqtlmtkf iwkplrhdaa
      841 eitvmhywfg qaffyfqgns nniatvdisa gfvgldtyve ipavlltafg tyagpvlwas
      901 hlvhflsset rsgsalshac fcyalicsip vftyivlvts lryhlfiwsv fspkllyegm
      961 hllitaavcv fftamdqtrl tqs
//
LOCUS       NP_001076007             592 aa            linear   PRI 20-NOV-2025
DEFINITION  tectonic-1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_001076007
VERSION     NP_001076007.1
DBSOURCE    REFSEQ: accession NM_001082538.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Xu,X., Gao,F., Wang,J., Long,C., Tao,L., Ding,L. and Ji,Y.
  TITLE     microRNA-216a-5p inhibits the development of gastric cancer through
            target combination with TCTN1
  JOURNAL   Minerva Med 114 (3), 323-331 (2023)
   PUBMED   32486612
  REMARK    GeneRIF: microRNA-216a-5p inhibits the development of gastric
            cancer through target combination with TCTN1.
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Bai,G., Wei,N., Li,F., Zhao,P., Meng,Z., Zou,B., Liu,Y., Xu,K.,
            Li,K., Yao,C. and Yang,P.
  TITLE     Function and transcriptional regulation of TCTN1 in oral squamous
            cell carcinoma
  JOURNAL   Oncol Rep 47 (2) (2022)
   PUBMED   34859261
  REMARK    GeneRIF: Function and transcriptional regulation of TCTN1 in oral
            squamous cell carcinoma.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Wang,H., Jiang,W., Dai,M., Xiao,B., Xu,Y., Sun,Y., Liu,Y., Ying,X.,
            Sun,Y., Wei,W. and Ji,X.
  TITLE     [Diagnosis of two cases from one family with Joubert syndrome
            caused by novel mutations of TCTN1 gene by whole exome sequencing]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 36 (7), 686-689 (2019)
   PUBMED   31302911
  REMARK    GeneRIF: Two novel TCTN1 mutations were identified in a family with
            Joubert syndrome
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Alazami,A.M., Alshammari,M.J., Salih,M.A., Alzahrani,F., Hijazi,H.,
            Seidahmed,M.Z., Abu Safieh,L., Aldosary,M., Khan,A.O. and
            Alkuraya,F.S.
  TITLE     Molecular characterization of Joubert syndrome in Saudi Arabia
  JOURNAL   Hum Mutat 33 (10), 1423-1428 (2012)
   PUBMED   22693042
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Chih,B., Liu,P., Chinn,Y., Chalouni,C., Komuves,L.G., Hass,P.E.,
            Sandoval,W. and Peterson,A.S.
  TITLE     A ciliopathy complex at the transition zone protects the cilia as a
            privileged membrane domain
  JOURNAL   Nat Cell Biol 14 (1), 61-72 (2011)
   PUBMED   22179047
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Garcia-Gonzalo,F.R., Corbit,K.C., Sirerol-Piquer,M.S.,
            Ramaswami,G., Otto,E.A., Noriega,T.R., Seol,A.D., Robinson,J.F.,
            Bennett,C.L., Josifova,D.J., Garcia-Verdugo,J.M., Katsanis,N.,
            Hildebrandt,F. and Reiter,J.F.
  TITLE     A transition zone complex regulates mammalian ciliogenesis and
            ciliary membrane composition
  JOURNAL   Nat Genet 43 (8), 776-784 (2011)
   PUBMED   21725307
  REMARK    GeneRIF: Mutations in Tctn1 is associated with ciliopathies.
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Reiter,J.F. and Skarnes,W.C.
  TITLE     Tectonic, a novel regulator of the Hedgehog pathway required for
            both activation and inhibition
  JOURNAL   Genes Dev 20 (1), 22-27 (2006)
   PUBMED   16357211
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Gunay-Aygun,M., Gahl,W.A. and Heller,T.
  TITLE     Congenital Hepatic Fibrosis Overview horizontal line RETIRED
            CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301743
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Glass,I.A., Dempsey,J.C., Parisi,M. and Doherty,D.
  TITLE     Joubert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301500
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK295514.1, AY358184.1,
            CA419765.1 and AC144522.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of a family of secreted and
            transmembrane proteins. The orthologous gene in mouse functions
            downstream of smoothened and rab23 to modulate hedgehog signal
            transduction. This protein is a component of the tectonic-like
            complex, which forms a barrier between the ciliary axoneme and the
            basal body. A mutation in this gene was found in a family with
            Joubert syndrome-13. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Feb 2016].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358184.1, SRR1803613.81979.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000397659.9/ ENSP00000380779.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.11"
     Protein         1..592
                     /product="tectonic-1 isoform 1 precursor"
                     /calculated_mol_wt=61877
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2336
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2MV58.2)"
     Region          46..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q2MV58.2)"
     Region          78..387
                     /region_name="TCTN_DUF1619"
                     /note="Tectonic domain DUF1619; pfam07773"
                     /db_xref="CDD:462260"
     Site            295
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2MV58.2)"
     Site            533
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q2MV58.2)"
     CDS             1..592
                     /gene="TCTN1"
                     /gene_synonym="JBTS13; TECT1"
                     /coded_by="NM_001082538.3:55..1833"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS41834.1"
                     /db_xref="GeneID:79600"
                     /db_xref="HGNC:HGNC:26113"
                     /db_xref="MIM:609863"
ORIGIN      
        1 mrprglppll vvllgcwasv saqtdatpav tteglnstea alatfgtfps trppgtprap
       61 gpssgprptp vtdvavlcvc dlspaqcdin cccdpdcssv dfsvfsacsv pvvtgdsqfc
      121 sqkaviysln ftanppqrvf elvdqinpsi fcihitnykp alsfinpevp dennfdtlmk
      181 tsdgftlnae syvsfttkld iptaakyeyg vplqtsdsfl rfpssltssl ctdnnpaafl
      241 vnqavkctrk inleqceeie alsmafyssp eilrvpdsrk kvpitvqsiv iqslnktltr
      301 redtdvlqpt lvnaghfslc vnvvlevkys ltytdagevt kadlsfvlgt vssvvvplqq
      361 kfeihflqen tqpvplsgnp gyvvglplaa gfqphkgsgi iqttnrygql tilhstteqd
      421 clalegvrtp vlfgytmqsg cklrltgalp cqlvaqkvks llwgqgfpdy vapfgnsqaq
      481 dmldwvpihf itqsfnrkhf vlqdscqlpg alvievkwtk ygsllnpqak ivnvtanlis
      541 ssfpeansgn ertilistav tfvdvsapae agfrappain arlpfnfffp fv
//
LOCUS       NP_001354645             858 aa            linear   PRI 20-NOV-2025
DEFINITION  la-related protein 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001354645 XP_016864772
VERSION     NP_001354645.1
DBSOURCE    REFSEQ: accession NM_001367716.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 858)
  AUTHORS   Ma,J., Dong,D., Qi,H., Li,J., Yu,H., Hu,X., Sun,L. and Shen,L.
  TITLE     LARP1, an RNA-binding protein, participates in ovarian cancer cell
            survival by regulating mitochondrial oxidative phosphorylation in
            response to the influence of the PI3K/mTOR pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (8), 167453 (2024)
   PUBMED   39111634
  REMARK    GeneRIF: LARP1, an RNA-binding protein, participates in ovarian
            cancer cell survival by regulating mitochondrial oxidative
            phosphorylation in response to the influence of the PI3K/mTOR
            pathway.
REFERENCE   2  (residues 1 to 858)
  AUTHORS   Chettle,J., Louie,R.J., Larner,O., Best,R., Chen,K., Morris,J.,
            Dedeic,Z., Childers,A., Rogers,R.C., DuPont,B.R., Skinner,C.,
            Kury,S., Uguen,K., Planes,M., Monteil,D., Li,M., Eliyahu,A.,
            Greenbaum,L., Mor,N., Besnard,T., Isidor,B., Cogne,B., Blesson,A.,
            Comi,A., Wentzensen,I.M., Vuocolo,B., Lalani,S.R., Sierra,R.,
            Berry,L., Carter,K., Sanders,S.J. and Blagden,S.P.
  TITLE     LARP1 haploinsufficiency is associated with an autosomal dominant
            neurodevelopmental disorder
  JOURNAL   HGG Adv 5 (4), 100345 (2024)
   PUBMED   39182167
  REMARK    GeneRIF: LARP1 haploinsufficiency is associated with an autosomal
            dominant neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 858)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 858)
  AUTHORS   Smith,B.C. and Silvers,R.
  TITLE     1H, 13C, and 15N resonance assignments of the La Motif of the human
            La-related protein 1
  JOURNAL   Biomol NMR Assign 18 (1), 111-118 (2024)
   PUBMED   38691336
  REMARK    GeneRIF: [1]H, [13]C, and [15]N resonance assignments of the La
            Motif of the human La-related protein 1.
REFERENCE   5  (residues 1 to 858)
  AUTHORS   Kozlov,G., Jiang,J., Rutherford,T., Noronha,A.M., Wilds,C.J. and
            Gehring,K.
  TITLE     Enhanced binding of guanylated poly(A) RNA by the LaM domain of
            LARP1
  JOURNAL   RNA Biol 21 (1), 7-16 (2024)
   PUBMED   39016322
  REMARK    GeneRIF: Enhanced binding of guanylated poly(A) RNA by the LaM
            domain of LARP1.
REFERENCE   6  (residues 1 to 858)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 858)
  AUTHORS   Burrows,C., Abd Latip,N., Lam,S.J., Carpenter,L., Sawicka,K.,
            Tzolovsky,G., Gabra,H., Bushell,M., Glover,D.M., Willis,A.E. and
            Blagden,S.P.
  TITLE     The RNA binding protein Larp1 regulates cell division, apoptosis
            and cell migration
  JOURNAL   Nucleic Acids Res 38 (16), 5542-5553 (2010)
   PUBMED   20430826
REFERENCE   8  (residues 1 to 858)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 858)
  AUTHORS   Horke,S., Reumann,K., Schweizer,M., Will,H. and Heise,T.
  TITLE     Nuclear trafficking of La protein depends on a newly identified
            nucleolar localization signal and the ability to bind RNA
  JOURNAL   J Biol Chem 279 (25), 26563-26570 (2004)
   PUBMED   15060081
  REMARK    GeneRIF: Nuclear trafficking of La protein depends on a newly
            identified nucleolar localization signal and the ability to bind
            RNA
REFERENCE   10 (residues 1 to 858)
  AUTHORS   Chauvet,S., Maurel-Zaffran,C., Miassod,R., Jullien,N., Pradel,J.
            and Aragnol,D.
  TITLE     dlarp, a new candidate Hox target in Drosophila whose orthologue in
            mouse is expressed at sites of epithelium/mesenchymal interactions
  JOURNAL   Dev Dyn 218 (3), 401-413 (2000)
   PUBMED   10878606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008379.7 and AC112169.2.
            
            On Dec 13, 2018 this sequence version replaced XP_016864772.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.7204.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..858
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..858
                     /product="la-related protein 1 isoform 5"
                     /note="la-related protein 1; La ribonucleoprotein domain
                     family member 1"
                     /calculated_mol_wt=98992
     Region          166..238
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Region          <169..317
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Site            order(172,175..176,181,184..185,187,206..208)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153396"
     Region          647..687
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          688..726
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     CDS             1..858
                     /gene="LARP1"
                     /gene_synonym="Lar1; LARP; Lhp1"
                     /coded_by="NM_001367716.1:239..2815"
                     /note="isoform 5 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS93806.1"
                     /db_xref="GeneID:23367"
                     /db_xref="HGNC:HGNC:29531"
                     /db_xref="MIM:612059"
ORIGIN      
        1 mkeqekgegs dskespktks desgeekngd edcqrggqkk kgnkhkwvpl qidmkpevpr
       61 eklasrptrp peprhipanr geikgsesat yvpvapptpa wqpeikpepa whdqdetsth
      121 fdyqfgyrkf dgvegprtpk ymnnityyfd nvsstelysv dqellkdyik rqieyyfsvd
      181 nlerdfflrr kmdadgflpi tliasfhrvq alttdislif aalkdskvve ivdekvrrre
      241 epekwplppi vdysqtdfsq llncpefvpr qhyqketesa pgspravtpv ptkteevsnl
      301 ktlpkglsas lpdldsenwi evkkrprpsp arpkkseesr fshltslpqq lpsqqlmskd
      361 qdeqeeldfl fdeemeqmdg rkntftawsd eesdyeiddr dvnkilivtq tphymrrhpg
      421 gdrtgnhtsr akmsaelakv indglfyyeq dlwaekfepe ysqikqeven fkkvnmisre
      481 qfdtltpepp vdpnqevppg pprfqqvptd alanklfgap epstiarslp ttvpespnyr
      541 ntrtprtprt pqlkdssqts rfypvvkegr tldakmprkr ktrhssnppl eshvgwvmds
      601 rehrprtasi ssspsegtpt vgsygctpqs lpkfqhpshe llkengftqh vyhkyrrrcl
      661 nerkrlgigq sqemntlfrf wsfflrdhfn kkmyeefkql aledakegyr ygleclfryy
      721 syglekkfrl difkdfqeet vkdyeagqly glekfwaflk yskaknldid pklqeylgkf
      781 rrledfrvdp pmgeegnhkr hsvvaggggg egrkrcpsqs ssrpaamisq pptpptgqpv
      841 redakwtsqh sntqtlgk
//
LOCUS       NP_001337341             150 aa            linear   PRI 20-NOV-2025
DEFINITION  regulating synaptic membrane exocytosis protein 1 isoform 8 [Homo
            sapiens].
ACCESSION   NP_001337341
VERSION     NP_001337341.1
DBSOURCE    REFSEQ: accession NM_001350412.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 150)
  AUTHORS   Hsu,Y.H., Pintacuda,G., Liu,R., Nacu,E., Kim,A., Tsafou,K.,
            Petrossian,N., Crotty,W., Suh,J.M., Riseman,J., Martin,J.M.,
            Biagini,J.C., Mena,D., Ching,J.K.T., Malolepsza,E., Li,T.,
            Singh,T., Ge,T., Egri,S.B., Tanenbaum,B., Stanclift,C.R.,
            Apffel,A.M., Carr,S.A., Schenone,M., Jaffe,J., Fornelos,N.,
            Huang,H., Eggan,K.C. and Lage,K.
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium;
            Stanley Global Asia Initiatives
  TITLE     Using brain cell-type-specific protein interactomes to interpret
            neurodevelopmental genetic signals in schizophrenia
  JOURNAL   iScience 26 (5), 106701 (2023)
   PUBMED   37207277
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 150)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 150)
  AUTHORS   Caillet-Saguy,C., Durbesson,F., Rezelj,V.V., Gogl,G., Tran,Q.D.,
            Twizere,J.C., Vignuzzi,M., Vincentelli,R. and Wolff,N.
  TITLE     Host PDZ-containing proteins targeted by SARS-CoV-2
  JOURNAL   FEBS J 288 (17), 5148-5162 (2021)
   PUBMED   33864728
REFERENCE   4  (residues 1 to 150)
  AUTHORS   Hirano,M., Takada,Y., Wong,C.F., Yamaguchi,K., Kotani,H.,
            Kurokawa,T., Mori,M.X., Snutch,T.P., Ronjat,M., De Waard,M. and
            Mori,Y.
  TITLE     C-terminal splice variants of P/Q-type Ca2+ channel CaV2.1 alpha1
            subunits are differentially regulated by Rab3-interacting molecule
            proteins
  JOURNAL   J Biol Chem 292 (22), 9365-9381 (2017)
   PUBMED   28377503
  REMARK    GeneRIF: Electrophysiological characterization of VDCC currents
            revealed that the suppressive effect of RIM2alpha on
            voltage-dependent inactivation (VDI) was stronger than that of
            RIM1alpha for the CaV2.1 variant containing the region encoded by
            exons 44 and 47.
REFERENCE   5  (residues 1 to 150)
  AUTHORS   Ruhle,F., Witten,A., Barysenka,A., Huge,A., Arning,A., Heller,C.,
            Krumpel,A., Mesters,R., Franke,A., Lieb,W., Riemenschneider,M.,
            Hiersche,M., Limperger,V., Nowak-Gottl,U. and Stoll,M.
  TITLE     Rare genetic variants in SMAP1, B3GAT2, and RIMS1 contribute to
            pediatric venous thromboembolism
  JOURNAL   Blood 129 (6), 783-790 (2017)
   PUBMED   28011674
  REMARK    GeneRIF: The study identified a region on chromosome 6 comprising
            the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus
            for pediatric venous thromboembolism.
REFERENCE   6  (residues 1 to 150)
  AUTHORS   Wang,Y., Liu,X., Biederer,T. and Sudhof,T.C.
  TITLE     A family of RIM-binding proteins regulated by alternative splicing:
            Implications for the genesis of synaptic active zones
  JOURNAL   Proc Natl Acad Sci U S A 99 (22), 14464-14469 (2002)
   PUBMED   12391317
REFERENCE   7  (residues 1 to 150)
  AUTHORS   Ohtsuka,T., Takao-Rikitsu,E., Inoue,E., Inoue,M., Takeuchi,M.,
            Matsubara,K., Deguchi-Tawarada,M., Satoh,K., Morimoto,K.,
            Nakanishi,H. and Takai,Y.
  TITLE     Cast: a novel protein of the cytomatrix at the active zone of
            synapses that forms a ternary complex with RIM1 and munc13-1
  JOURNAL   J Cell Biol 158 (3), 577-590 (2002)
   PUBMED   12163476
REFERENCE   8  (residues 1 to 150)
  AUTHORS   Schoch,S., Castillo,P.E., Jo,T., Mukherjee,K., Geppert,M., Wang,Y.,
            Schmitz,F., Malenka,R.C. and Sudhof,T.C.
  TITLE     RIM1alpha forms a protein scaffold for regulating neurotransmitter
            release at the active zone
  JOURNAL   Nature 415 (6869), 321-326 (2002)
   PUBMED   11797009
REFERENCE   9  (residues 1 to 150)
  AUTHORS   Coppola,T., Magnin-Luthi,S., Perret-Menoud,V., Gattesco,S.,
            Schiavo,G. and Regazzi,R.
  TITLE     Direct interaction of the Rab3 effector RIM with Ca2+ channels,
            SNAP-25, and synaptotagmin
  JOURNAL   J Biol Chem 276 (35), 32756-32762 (2001)
   PUBMED   11438518
REFERENCE   10 (residues 1 to 150)
  AUTHORS   Betz,A., Thakur,P., Junge,H.J., Ashery,U., Rhee,J.S., Scheuss,V.,
            Rosenmund,C., Rettig,J. and Brose,N.
  TITLE     Functional interaction of the active zone proteins Munc13-1 and
            RIM1 in synaptic vesicle priming
  JOURNAL   Neuron 30 (1), 183-196 (2001)
   PUBMED   11343654
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL390056.7 and AL590011.5.
            
            Summary: The protein encoded by this gene is a RAS gene superfamily
            member that regulates synaptic vesicle exocytosis. This gene also
            plays a role in the regulation of voltage-gated calcium channels
            during neurotransmitter and insulin release. Mutations have
            suggested a role cognition and have been identified as the cause of
            cone-rod dystrophy type 7. Multiple transcript variants encoding
            different isoforms have been described for this gene. [provided by
            RefSeq, Mar 2012].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.56708.1,
                                           SRR1803612.145040.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2157437
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..150
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q13"
     Protein         1..150
                     /product="regulating synaptic membrane exocytosis protein
                     1 isoform 8"
                     /note="RAB3-interacting protein 2; rab3-interacting
                     molecule 1; rab-3-interacting protein 2"
                     /calculated_mol_wt=17143
     CDS             1..150
                     /gene="RIMS1"
                     /gene_synonym="CORD7; RAB3IP2; RIM; RIM1"
                     /coded_by="NM_001350412.1:322..774"
                     /note="isoform 8 is encoded by transcript variant 8"
                     /db_xref="GeneID:22999"
                     /db_xref="HGNC:HGNC:17282"
                     /db_xref="MIM:606629"
ORIGIN      
        1 mssavgprgp rpptvpppmq elpdlshlte eerniimavm drqkeeeeke eamlkrlhqq
       61 fesykeqvrk igeearryqg ehkddaptcg ichktkfadg cghlcsycrt kfcarcggrv
      121 slrsnnedkv vrihtffsii cycivvnfik
//
LOCUS       NP_001124490             818 aa            linear   PRI 20-NOV-2025
DEFINITION  cip1-interacting zinc finger protein isoform 4 [Homo sapiens].
ACCESSION   NP_001124490
VERSION     NP_001124490.1
DBSOURCE    REFSEQ: accession NM_001131018.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 818)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 818)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 818)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 818)
  AUTHORS   Chen,Y.R., Wu,Y.S., Wang,W.S., Zhang,J.S. and Wu,Q.G.
  TITLE     Upregulation of lncRNA DANCR functions as an oncogenic role in
            non-small lung cancer by regulating miR-214-5p/CIZ1 axis
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (5), 2539-2547 (2020)
   PUBMED   32196604
  REMARK    GeneRIF: Upregulation of lncRNA DANCR functions as an oncogenic
            role in non-small lung cancer by regulating miR-214-5p/CIZ1 axis.
REFERENCE   5  (residues 1 to 818)
  AUTHORS   Chen,X., Wang,P., Wang,S., Li,J., Ou,T. and Zeng,X.
  TITLE     CIZ1 knockdown suppresses the proliferation of bladder cancer cells
            by inducing apoptosis
  JOURNAL   Gene 719, 143946 (2019)
   PUBMED   31252164
  REMARK    GeneRIF: silencing of CIZ1 suppressed bladder cancer cell
            proliferation through inducing apoptosis and reducing cell cycle
            progression
REFERENCE   6  (residues 1 to 818)
  AUTHORS   Oh,J.H., Yang,J.O., Hahn,Y., Kim,M.R., Byun,S.S., Jeon,Y.J.,
            Kim,J.M., Song,K.S., Noh,S.M., Kim,S., Yoo,H.S., Kim,Y.S. and
            Kim,N.S.
  TITLE     Transcriptome analysis of human gastric cancer
  JOURNAL   Mamm Genome 16 (12), 942-954 (2005)
   PUBMED   16341674
REFERENCE   7  (residues 1 to 818)
  AUTHORS   Coverley,D., Marr,J. and Ainscough,J.
  TITLE     Ciz1 promotes mammalian DNA replication
  JOURNAL   J Cell Sci 118 (Pt 1), 101-112 (2005)
   PUBMED   15585571
REFERENCE   8  (residues 1 to 818)
  AUTHORS   Warder,D.E. and Keherly,M.J.
  TITLE     Ciz1, Cip1 interacting zinc finger protein 1 binds the consensus
            DNA sequence ARYSR(0-2)YYAC
  JOURNAL   J Biomed Sci 10 (4), 406-417 (2003)
   PUBMED   12824700
  REMARK    GeneRIF: data indicate that Ciz1 is localized in the nucleus and is
            expressed in a wide range of tissues, especially the pancreas and
            the brain; formulated a consensus DNA sequence, ARYSR(0-2)YYAC,
            recognized by Ciz1
REFERENCE   9  (residues 1 to 818)
  AUTHORS   Mitsui,K., Matsumoto,A., Ohtsuka,S., Ohtsubo,M. and Yoshimura,A.
  TITLE     Cloning and characterization of a novel p21(Cip1/Waf1)-interacting
            zinc finger protein, ciz1
  JOURNAL   Biochem Biophys Res Commun 264 (2), 457-464 (1999)
   PUBMED   10529385
REFERENCE   10 (residues 1 to 818)
  AUTHORS   Gilley,J. and Fried,M.
  TITLE     Extensive gene order differences within regions of conserved
            synteny between the Fugu and human genomes: implications for
            chromosomal evolution and the cloning of disease genes
  JOURNAL   Hum Mol Genet 8 (7), 1313-1320 (1999)
   PUBMED   10369878
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM757318.1 and BC021163.2.
            
            Summary: The protein encoded by this gene is a zinc finger DNA
            binding protein that interacts with CIP1, part of a complex with
            cyclin E. The encoded protein may regulate the cellular
            localization of CIP1. Several transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Apr 2012].
            
            Transcript Variant: This variant (4) has an alternate exon in place
            of the first exon, lacks two alternate in-frame exons, and lacks an
            alternate in-frame segment compared to variant 6. The resulting
            isoform (4) is shorter at the N-terminus and lacks three alternate
            internal segments compared to isoform 5.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC021163.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..818
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.11"
     Protein         1..818
                     /product="cip1-interacting zinc finger protein isoform 4"
                     /note="zinc finger protein 356; nuclear protein NP94;
                     Cip1-interacting zinc finger protein"
                     /calculated_mol_wt=91023
     Region          <111..402
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          512..541
                     /region_name="ZnF_U1"
                     /note="U1-like zinc finger; smart00451"
                     /db_xref="CDD:197732"
     Region          576..596
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     Site            order(583..585,586,590,595,612,615..619,621..622)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275371"
     Region          <586..>637
                     /region_name="UFD2"
                     /note="U1-like Zn-finger-containing protein [General
                     function prediction only]; COG5112"
                     /db_xref="CDD:227443"
     Region          606..630
                     /region_name="zf-C2H2_jaz"
                     /note="Zinc-finger double-stranded RNA-binding; pfam12171"
                     /db_xref="CDD:432381"
     Region          607..629
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275371"
     CDS             1..818
                     /gene="CIZ1"
                     /gene_synonym="LSFR1; NP94; ZNF356"
                     /coded_by="NM_001131018.2:147..2603"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS48033.1"
                     /db_xref="GeneID:25792"
                     /db_xref="HGNC:HGNC:16744"
                     /db_xref="MIM:611420"
ORIGIN      
        1 mfsqqqqqql qqqqqqlqql qqqqlqqqql qqqqllqlqq llqqsppqap lpmavsrglp
       61 pqqpqqplln lqgtnsasll ngsmlqrall lqqlqgnlrg ygmaspglaa psltppqlat
      121 pnlqqffpqa trqsllgppp vgvpmnpsqf nlsgrnpqkq artsssttpn rkdsssqtmp
      181 vedksdppeg seeaaeprmd tpedqdlppc pediakekrt papepepcea selpakrlrs
      241 seeptekepp gqlqvkaqpq armtvpkqtq tpdllpeale aqvlprfqpr vlqvqaqvqs
      301 qtqpripstd tqvqpklqkq aqtqtspehl vlqqkqvqpq lqqeaepqkq vqpqvhtqaq
      361 psvqpqehpp aqvsvqppeq theqphtqpq vsllapeqtp vvvhvcglem ppdaveaggg
      421 mektlpepvg tqvsmeeiqn esacgldvge cenrarempg vwgaggslkv tilqssdsra
      481 fstvpltpvp rpsdsvsstp aatstpskqa lqffcyicka scssqqefqd hmsepqhqqr
      541 lgeiqhmsqa cllsllpvpr dvletedeep pprrwcntcq lyymgdliqh rrtqdhkiak
      601 qslrpfctvc nryfktprkf vehvksqghk dkakelksle keiagqdedh fitvdavgcf
      661 egdeeeeedd edeeeievee elckqvrsrd isreewkgse tyspntaygv dflvpvmgyi
      721 crichkfyhs nsgaqlshck slghfenlqk ykaaknpspt trpvsrrcai narnaltalf
      781 tssgrppsqp ntqdktpskv tarpsqpplp rrstrlkt
//
LOCUS       NP_003738               1327 aa            linear   PRI 20-NOV-2025
DEFINITION  poly [ADP-ribose] polymerase tankyrase-1 [Homo sapiens].
ACCESSION   NP_003738
VERSION     NP_003738.2
DBSOURCE    REFSEQ: accession NM_003747.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1327)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1327)
  AUTHORS   Morino,S., Mashima,T., Shirai,F., Nagayama,S., Katayama,R. and
            Seimiya,H.
  TITLE     BET protein-dependent E2F pathway activity confers bell-shaped type
            resistance to tankyrase inhibitors in APC-mutated colorectal cancer
  JOURNAL   Cancer Lett 584, 216632 (2024)
   PUBMED   38216082
  REMARK    GeneRIF: BET protein-dependent E2F pathway activity confers
            bell-shaped type resistance to tankyrase inhibitors in APC-mutated
            colorectal cancer.
REFERENCE   3  (residues 1 to 1327)
  AUTHORS   Ma,N., Wibowo,Y.C., Wirtz,P., Baltus,D., Wieland,T. and Jansen,S.
  TITLE     Tankyrase inhibition interferes with junction remodeling, induces
            leakiness, and disturbs YAP1/TAZ signaling in the endothelium
  JOURNAL   Naunyn Schmiedebergs Arch Pharmacol 397 (3), 1763-1789 (2024)
   PUBMED   37741944
  REMARK    GeneRIF: Tankyrase inhibition interferes with junction remodeling,
            induces leakiness, and disturbs YAP1/TAZ signaling in the
            endothelium.
REFERENCE   4  (residues 1 to 1327)
  AUTHORS   Duan,X., Huang,T., Zhang,D., Wei,Y., Li,L., Yao,W., Cui,L.,
            Zhou,X., Yang,Y., Wang,W. and Zhao,J.
  TITLE     Effect and interaction of TNKS genetic polymorphisms and
            environmental factors on telomere damage in COEs-exposure workers
  JOURNAL   Ecotoxicol Environ Saf 250, 114489 (2023)
   PUBMED   36603485
  REMARK    GeneRIF: Effect and interaction of TNKS genetic polymorphisms and
            environmental factors on telomere damage in COEs-exposure workers.
REFERENCE   5  (residues 1 to 1327)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   6  (residues 1 to 1327)
  AUTHORS   Lyons,R.J., Deane,R., Lynch,D.K., Ye,Z.S., Sanderson,G.M.,
            Eyre,H.J., Sutherland,G.R. and Daly,R.J.
  TITLE     Identification of a novel human tankyrase through its interaction
            with the adaptor protein Grb14
  JOURNAL   J Biol Chem 276 (20), 17172-17180 (2001)
   PUBMED   11278563
REFERENCE   7  (residues 1 to 1327)
  AUTHORS   Chi,N.W. and Lodish,H.F.
  TITLE     Tankyrase is a golgi-associated mitogen-activated protein kinase
            substrate that interacts with IRAP in GLUT4 vesicles
  JOURNAL   J Biol Chem 275 (49), 38437-38444 (2000)
   PUBMED   10988299
REFERENCE   8  (residues 1 to 1327)
  AUTHORS   Smith,S. and de Lange,T.
  TITLE     Cell cycle dependent localization of the telomeric PARP, tankyrase,
            to nuclear pore complexes and centrosomes
  JOURNAL   J Cell Sci 112 (Pt 21), 3649-3656 (1999)
   PUBMED   10523501
REFERENCE   9  (residues 1 to 1327)
  AUTHORS   Zhu,L., Smith,S., de Lange,T. and Seldin,M.F.
  TITLE     Chromosomal mapping of the tankyrase gene in human and mouse
  JOURNAL   Genomics 57 (2), 320-321 (1999)
   PUBMED   10198177
REFERENCE   10 (residues 1 to 1327)
  AUTHORS   Smith,S., Giriat,I., Schmitt,A. and de Lange,T.
  TITLE     Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
  JOURNAL   Science 282 (5393), 1484-1487 (1998)
   PUBMED   9822378
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC021242.10, AC103877.2, AC103834.2 and AC104052.9.
            
            On Feb 14, 2006 this sequence version replaced NP_003738.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC098394.1, SRR1803611.228164.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000310430.11/ ENSP00000311579.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1327
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p23.1"
     Protein         1..1327
                     /product="poly [ADP-ribose] polymerase tankyrase-1"
                     /EC_number="2.4.2.30"
                     /note="tankyrase-1; TANK1; TNKS-1; tankyrase I; poly
                     [ADP-ribose] polymerase 5A; tankyrase, TRF1-interacting
                     ankyrin-related ADP-ribose polymerase;
                     ADP-ribosyltransferase diphtheria toxin-like 5;
                     TRF1-interacting ankyrin-related ADP-ribose polymerase 1;
                     protein poly-ADP-ribosyltransferase tankyrase-1"
                     /calculated_mol_wt=141909
     Region          1..91
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          112..173
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          181..209
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          182..504
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          215..244
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          218..246
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(221..222,225..227,229..230,234,237,246,248,250,
                     254..255,258..260,262..263,267,270,279,281,283,287..288,
                     291..293,295..296,300,303,312)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          248..279
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          248..277
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          281..312
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          281..310
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          288..628
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          335..364
                     /region_name="ANK 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          368..397
                     /region_name="ANK 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          371..399
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(374..375,378..380,382..383,387,390,399,401,403,
                     407..408,411..413,415..416,420,423,432,434,436,440..441,
                     444..446,448..449,453,456,465)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          401..432
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          401..430
                     /region_name="ANK 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          434..465
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          434..463
                     /region_name="ANK 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          521..553
                     /region_name="ANK 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Site            order(523,527..528,531..533,535,539,543,546,555,557,559,
                     563..564,567..569,571..572,576,579,588,590,592,596..597,
                     600..602,604..605,609,612)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          523..555
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          557..588
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          557..586
                     /region_name="ANK 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          590..619
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          590..619
                     /region_name="ANK 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          621..647
                     /region_name="ANK 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          632..953
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          649..679
                     /region_name="ANK 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          683..712
                     /region_name="ANK 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          686..714
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(689..690,693..695,697..698,702,705,714,716,718,
                     722..723,726..728,730..731,735,738,747,749,751,755..756,
                     759..761,763..764,768,771,780)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          716..747
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          716..745
                     /region_name="ANK 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          749..780
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          749..778
                     /region_name="ANK 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          782..810
                     /region_name="ANK 17. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          806..857
                     /region_name="Ank_4"
                     /note="Ankyrin repeats (many copies); pfam13637"
                     /db_xref="CDD:372654"
     Site            order(836,838,842..843,846..848,850..851,855,858,867,869,
                     871,875..876,879..881,883..884,888,891,900,902,904,
                     908..909,912..914,916..917,921,924,933)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          836..867
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          836..865
                     /region_name="ANK 18. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          869..900
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          869..898
                     /region_name="ANK 19. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          902..933
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          902..931
                     /region_name="ANK 20. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          935..964
                     /region_name="ANK 21. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O95271.2)"
     Region          1024..1089
                     /region_name="SAM_tankyrase1,2"
                     /note="SAM domain of tankyrase1,2 subfamily; cd09524"
                     /db_xref="CDD:188923"
     Region          1091..1313
                     /region_name="tankyrase_like"
                     /note="Tankyrases interact with the telomere reverse
                     transcriptase complex (TERT). Tankyrase 1
                     poly-ADP-ribosylates Telomere Repeat Binding Factor 1
                     (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or
                     TRF1. The tankyrases also contain multiple ankyrin...;
                     cd01438"
                     /db_xref="CDD:238718"
     CDS             1..1327
                     /gene="TNKS"
                     /gene_synonym="ARTD5; PARP-5a; PARP5A; PARPL; pART5; TIN1;
                     TINF1; TNKS1"
                     /coded_by="NM_003747.3:29..4012"
                     /db_xref="CCDS:CCDS5974.1"
                     /db_xref="GeneID:8658"
                     /db_xref="HGNC:HGNC:11941"
                     /db_xref="MIM:603303"
ORIGIN      
        1 maasrrsqhh hhhhqqqlqp apgasapppp pppplspgla pgttpaspta sglapfaspr
       61 hglalpegdg srdppdrprs pdpvdgtscc sttstictva aapvvpavst ssaagvapnp
      121 agsgsnnsps ssssptssss sspsspgssl aespeaagvs staplgpgaa gpgtgvpavs
      181 galrelleac rngdvsrvkr lvdaanvnak dmagrksspl hfaagfgrkd vvehllqmga
      241 nvharddggl iplhnacsfg haevvslllc qgadpnardn wnytplheaa ikgkidvciv
      301 llqhgadpni rntdgksald ladpsakavl tgeykkdell eaarsgneek lmalltplnv
      361 nchasdgrks tplhlaagyn rvrivqlllq hgadvhakdk gglvplhnac syghyevtel
      421 llkhgacvna mdlwqftplh eaasknrvev cslllshgad ptlvnchgks avdmaptpel
      481 rerltyefkg hsllqaarea dlakvkktla leiinfkqpq shetalhcav aslhpkrkqv
      541 telllrkgan vneknkdfmt plhvaaerah ndvmevlhkh gakmnaldtl gqtalhraal
      601 aghlqtcrll lsygsdpsii slqgftaaqm gneavqqils estpirtsdv dyrlleaska
      661 gdletvkqlc ssqnvncrdl egrhstplhf aagynrvsvv eyllhhgadv hakdkgglvp
      721 lhnacsyghy evaellvrhg asvnvadlwk ftplheaaak gkyeicklll khgadptkkn
      781 rdgntpldlv kegdtdiqdl lrgdaallda akkgclarvq klctpeninc rdtqgrnstp
      841 lhlaagynnl evaeyllehg advnaqdkgg liplhnaasy ghvdiaalli kyntcvnatd
      901 kwaftplhea aqkgrtqlca lllahgadpt mknqegqtpl dlataddira llidamppea
      961 lptcfkpqat vvsaslispa stpsclsaas sidnltgpla elavggasna gdgaagterk
     1021 egevagldmn isqflkslgl ehlrdifete qitldvladm gheelkeigi nayghrhkli
     1081 kgverllggq qgtnpyltfh cvnqgtilld lapedkeyqs veeemqstir ehrdggnagg
     1141 ifnrynviri qkvvnkklre rfchrqkevs eenhnhhner mlfhgspfin aiihkgfder
     1201 hayiggmfga giyfaenssk snqyvygigg gtgcpthkdr scyichrqml fcrvtlgksf
     1261 lqfstmkmah appghhsvig rpsvnglaya eyviyrgeqa ypeylityqi mkpeapsqta
     1321 taaeqkt
//
LOCUS       NP_004875                814 aa            linear   PRI 20-NOV-2025
DEFINITION  immunoglobulin superfamily DCC subclass member 3 precursor [Homo
            sapiens].
ACCESSION   NP_004875
VERSION     NP_004875.2
DBSOURCE    REFSEQ: accession NM_004884.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Salbaum,J.M.
  TITLE     Genomic structure and chromosomal localization of the mouse gene
            Punc
  JOURNAL   Mamm Genome 10 (2), 107-111 (1999)
   PUBMED   9922388
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC067107.1, AC105129.4 and AI740721.1.
            
            On Mar 28, 2007 this sequence version replaced NP_004875.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042054.1, SRR9304715.358223.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000327987.9/ ENSP00000332773.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..814
                     /product="immunoglobulin superfamily DCC subclass member 3
                     precursor"
                     /note="putative neuronal cell adhesion molecule"
                     /calculated_mol_wt=82930
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3812
     mat_peptide     36..814
                     /product="Immunoglobulin superfamily DCC subclass member
                     3. /id=PRO_0000014920"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVU1.2)"
                     /calculated_mol_wt=82930
     Region          41..135
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          59..63
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          72..76
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            93
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Region          94..98
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          114..119
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          128..131
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          143..227
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          156..160
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          169..173
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          192..196
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          206..211
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          220..223
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Region          238..310
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            246
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Region          331..417
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          347..351
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          360..364
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          <371..>624
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain [General function
                     prediction only]; COG3401"
                     /db_xref="CDD:442628"
     Region          381..387
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            381
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Site            382
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Region          397..402
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          410..413
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            580
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Site            604
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Site            634
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Site            641..661
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Region          722..743
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVU1.2)"
     Region          762..814
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IVU1.2)"
     CDS             1..814
                     /gene="IGDCC3"
                     /gene_synonym="HsT18880; PUNC"
                     /coded_by="NM_004884.4:215..2659"
                     /db_xref="CCDS:CCDS10205.1"
                     /db_xref="GeneID:9543"
                     /db_xref="HGNC:HGNC:9700"
                     /db_xref="MIM:604184"
ORIGIN      
        1 mavqraaspr rppaplwprl llpllllllp apseglghsa elafavepsd dvavpgqpiv
       61 ldcrvegtpp vritwrkngv elpesthstl langslmirh frlepggsps degdyecvaq
      121 nrfglvvsrk ariqaatmsd fhvhpqatvg eeggvarfqc qihglpkpli tweknrvpid
      181 tdnerytllp kgvlqitglr aedggifhcv asniasiris hgarltvsgs gsgaykepai
      241 lvgpenltlt vhqtavlecv atgnprpivs wsrldgrpig vegiqvlgtg nliisdvtvq
      301 hsgvyvcaan rpgtrvrrta qgrlvvqapa efvqhpqsis rpagttamft cqaqgeppph
      361 vtwlkngqvl gpgghvrlkn nnstltisgi gpedeaiyqc vaensagssq asarltvlwa
      421 eglpgpprnv ravsvsstev rvswseplan tkeiigyvlh irkaadppel eyqeavskst
      481 fqhlvsdlep staysfyika ytprgassas vptlastlge apappplsvr vlgssslqll
      541 wepwprlaqh eggfklfyrp asktsftgpi llpgtvssyn lsqldptavy evkllaynqh
      601 gdgnatvrfv slrgaserta lsppcdcrke eaanqtsttg ivigihigvt ciifcvlfll
      661 fgqrgrvllc kdvenqlspp qgprsqrdpg ilalngarrg qrgqlgrdek rvdmkeleql
      721 fppasaagqp dprptqdpaa papceetqls vlplqgcglm egktteaktt eatapcagla
      781 aappppdggp gllsegqasr paaarvtqpa hseq
//
LOCUS       NP_001308470             288 aa            linear   PRI 20-NOV-2025
DEFINITION  sphingolipid delta(4)-desaturase DES1 isoform 2 [Homo sapiens].
ACCESSION   NP_001308470 XP_011542619
VERSION     NP_001308470.1
DBSOURCE    REFSEQ: accession NM_001321541.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Dei Cas,M., Montavoci,L., Pasini,C., Caretti,A., Penati,S.,
            Martinelli,C., Gianelli,U., Casati,S., Nardecchia,F., Torella,A.,
            Brunetti-Pierri,N. and Trinchera,M.
  TITLE     Loss of function and reduced levels of sphingolipid desaturase
            DEGS1 variants are both relevant in disease mechanism
  JOURNAL   J Lipid Res 65 (3), 100517 (2024)
   PUBMED   38342436
  REMARK    GeneRIF: Loss of function and reduced levels of sphingolipid
            desaturase DEGS1 variants are both relevant in disease mechanism.
REFERENCE   2  (residues 1 to 288)
  AUTHORS   Hulsmeier,A.J., Toelle,S.P., Bellstedt,P., Wentzel,C., Bahr,A.,
            Kolokotronis,K. and Hornemann,T.
  TITLE     The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker for DEGS1
            related hypomyelinating leukodystrophy
  JOURNAL   J Lipid Res 64 (12), 100464 (2023)
   PUBMED   37890668
  REMARK    GeneRIF: The atypical sphingolipid SPB 18:1(14Z);O2 is a biomarker
            for DEGS1 related hypomyelinating leukodystrophy.
REFERENCE   3  (residues 1 to 288)
  AUTHORS   Planas-Serra,L., Launay,N., Goicoechea,L., Heron,B., Jou,C.,
            Julia-Palacios,N., Ruiz,M., Fourcade,S., Casasnovas,C., De La
            Torre,C., Gelot,A., Marsal,M., Loza-Alvarez,P., Garcia-Cazorla,A.,
            Fatemi,A., Ferrer,I., Portero-Otin,M., Area-Gomez,E. and Pujol,A.
  TITLE     Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity
  JOURNAL   J Clin Invest 133 (10), e162957 (2023)
   PUBMED   36951944
  REMARK    GeneRIF: Sphingolipid desaturase DEGS1 is essential for
            mitochondria-associated membrane integrity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 288)
  AUTHORS   Hayashi,Y., Matsuda,K., Tanigawa,K., Tanikawa,T., Maeda,K. and
            Tsuchiya,K.
  TITLE     Dihydroceramide Delta4-Desaturase 1 Is Not Involved in SARS-CoV-2
            Infection
  JOURNAL   Biol Pharm Bull 45 (10), 1559-1563 (2022)
   PUBMED   36184516
  REMARK    GeneRIF: Dihydroceramide Delta4-Desaturase 1 Is Not Involved in
            SARS-CoV-2 Infection.
REFERENCE   5  (residues 1 to 288)
  AUTHORS   Devlin,C.M., Lahm,T., Hubbard,W.C., Van Demark,M., Wang,K.C.,
            Wu,X., Bielawska,A., Obeid,L.M., Ivan,M. and Petrache,I.
  TITLE     Dihydroceramide-based response to hypoxia
  JOURNAL   J Biol Chem 286 (44), 38069-38078 (2011)
   PUBMED   21914808
  REMARK    GeneRIF: overexpression of DEGS1 or DEGS2 attenuates the DHC
            accumulation and increased cell proliferation during hypoxia
            Erratum:[J Biol Chem. 2012 May 18;287(21):17425]
REFERENCE   6  (residues 1 to 288)
  AUTHORS   Idkowiak-Baldys,J., Apraiz,A., Li,L., Rahmaniyan,M., Clarke,C.J.,
            Kraveka,J.M., Asumendi,A. and Hannun,Y.A.
  TITLE     Dihydroceramide desaturase activity is modulated by oxidative
            stress
  JOURNAL   Biochem J 427 (2), 265-274 (2010)
   PUBMED   20105137
  REMARK    GeneRIF: oxidative stress leads to potent inhibition of
            dihydroceramide desaturase resulting in significant elevation in
            dihydroceramide levels in vivo
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 288)
  AUTHORS   Kraveka,J.M., Li,L., Szulc,Z.M., Bielawski,J., Ogretmen,B.,
            Hannun,Y.A., Obeid,L.M. and Bielawska,A.
  TITLE     Involvement of dihydroceramide desaturase in cell cycle progression
            in human neuroblastoma cells
  JOURNAL   J Biol Chem 282 (23), 16718-16728 (2007)
   PUBMED   17283068
  REMARK    GeneRIF: partial loss of DEGS-1 inhibited cell growth, with cell
            cycle arrest at G(0)/G(1). This was accompanied by a significant
            decrease in the amount of phosphorylated retinoblastoma protein
REFERENCE   8  (residues 1 to 288)
  AUTHORS   Inuzuka,M., Hayakawa,M. and Ingi,T.
  TITLE     Serinc, an activity-regulated protein family, incorporates serine
            into membrane lipid synthesis
  JOURNAL   J Biol Chem 280 (42), 35776-35783 (2005)
   PUBMED   16120614
REFERENCE   9  (residues 1 to 288)
  AUTHORS   Ternes,P., Franke,S., Zahringer,U., Sperling,P. and Heinz,E.
  TITLE     Identification and characterization of a sphingolipid delta
            4-desaturase family
  JOURNAL   J Biol Chem 277 (28), 25512-25518 (2002)
   PUBMED   11937514
  REMARK    GeneRIF: identification of sphingolipid delta 4-desaturase family
REFERENCE   10 (residues 1 to 288)
  AUTHORS   Cadena,D.L., Kurten,R.C. and Gill,G.N.
  TITLE     The product of the MLD gene is a member of the membrane fatty acid
            desaturase family: overexpression of MLD inhibits EGF receptor
            biosynthesis
  JOURNAL   Biochemistry 36 (23), 6960-6967 (1997)
   PUBMED   9188692
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092809.2.
            
            On Mar 26, 2016 this sequence version replaced XP_011542619.1.
            
            Summary: This gene encodes a member of the membrane fatty acid
            desaturase family which is responsible for inserting double bonds
            into specific positions in fatty acids. This protein contains three
            His-containing consensus motifs that are characteristic of a group
            of membrane fatty acid desaturases. It is predicted to be a
            multiple membrane-spanning protein localized to the endoplasmic
            reticulum. Overexpression of this gene inhibited biosynthesis of
            the EGF receptor, suggesting a possible role of a fatty acid
            desaturase in regulating biosynthetic processing of the EGF
            receptor. [provided by RefSeq, Mar 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.126676.1,
                                           SRR1660803.238931.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.11"
     Protein         1..288
                     /product="sphingolipid delta(4)-desaturase DES1 isoform 2"
                     /EC_number="1.14.19.17"
                     /note="membrane fatty acid (lipid) desaturase;
                     sphingolipid delta 4 desaturase; migration-inducing gene
                     15 protein; membrane lipid desaturase; cell
                     migration-inducing gene 15 protein; degenerative
                     spermatocyte homolog 1, lipid desaturase; sphingolipid
                     delta(4)-desaturase 1; dihydroceramide desaturase 1;
                     degenerative spermatocyte homolog, lipid desaturase;
                     retinol isomerase"
                     /calculated_mol_wt=33279
     Region          6..42
                     /region_name="Lipid_DES"
                     /note="Sphingolipid Delta4-desaturase (DES); pfam08557"
                     /db_xref="CDD:462517"
     Region          26..275
                     /region_name="Delta4-sphingolipid-FADS-like"
                     /note="The Delta4-sphingolipid Fatty Acid Desaturase
                     (Delta4-sphingolipid-FADS)-like CD includes the
                     integral-membrane enzymes, dihydroceramide Delta-4
                     desaturase, involved in the synthesis of sphingosine; and
                     the human membrane fatty acid (lipid) desaturase...;
                     cd03508"
                     /db_xref="CDD:239585"
     Site            41..61
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            68..88
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            order(89,93,128,131..132,259,262..263)
                     /site_type="other"
                     /note="putative di-iron ligands [ion binding]"
                     /db_xref="CDD:239585"
     Region          89..93
                     /region_name="Histidine box-1. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            102..122
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          128..132
                     /region_name="Histidine box-2. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            152..172
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            184..204
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Site            209..229
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     Region          259..263
                     /region_name="Histidine box-3. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (O15121.1)"
     CDS             1..288
                     /gene="DEGS1"
                     /gene_synonym="DEGS; DEGS-1; Des-1; DES1; FADS7; HLD18;
                     MIG15; MLD"
                     /coded_by="NM_001321541.2:98..964"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:8560"
                     /db_xref="HGNC:HGNC:13709"
                     /db_xref="MIM:615843"
ORIGIN      
        1 mgsrvsredf ewvytdqpha drrreilaky peikslmkpd pnliwiiimm vltqlgafyi
       61 vkdldwkwvi fgayafgsci nhsmtlaihe iahnaafgnc kamwnrwfgm fanlpigipy
      121 sisfkryhmd hhrylgadgv dvdiptdfeg wffctafrkf iwvilqplfy afrplfinpk
      181 pitylevint vaqvtfdili yyflgikslv ymlaasllgl glhpisghfi aehymflkgh
      241 etysyygpln lltfnvgyhn ehhdfpnipg kslplswsfl dgcsgshl
//
LOCUS       NP_001147057             122 aa            linear   PRI 20-NOV-2025
DEFINITION  short coiled-coil protein isoform 4 [Homo sapiens].
ACCESSION   NP_001147057
VERSION     NP_001147057.1
DBSOURCE    REFSEQ: accession NM_001153585.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Wirth,M., Mouilleron,S., Zhang,W., Sjottem,E., Princely Abudu,Y.,
            Jain,A., Lauritz Olsvik,H., Bruun,J.A., Razi,M., Jefferies,H.B.J.,
            Lee,R., Joshi,D., O'Reilly,N., Johansen,T. and Tooze,S.A.
  TITLE     Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding
            Affinity and Specificity
  JOURNAL   J Mol Biol 433 (13), 166987 (2021)
   PUBMED   33845085
  REMARK    GeneRIF: Phosphorylation of the LIR Domain of SCOC Modulates ATG8
            Binding Affinity and Specificity.
            Erratum:[J Mol Biol. 2021 Jul 23;433(15):167049. doi:
            10.1016/j.jmb.2021.167049. PMID: 34052024]
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Stringer,S., Minica,C.C., Verweij,K.J., Mbarek,H., Bernard,M.,
            Derringer,J., van Eijk,K.R., Isen,J.D., Loukola,A.,
            Maciejewski,D.F., Mihailov,E., van der Most,P.J., Sanchez-Mora,C.,
            Roos,L., Sherva,R., Walters,R., Ware,J.J., Abdellaoui,A.,
            Bigdeli,T.B., Branje,S.J., Brown,S.A., Bruinenberg,M., Casas,M.,
            Esko,T., Garcia-Martinez,I., Gordon,S.D., Harris,J.M.,
            Hartman,C.A., Henders,A.K., Heath,A.C., Hickie,I.B., Hickman,M.,
            Hopfer,C.J., Hottenga,J.J., Huizink,A.C., Irons,D.E., Kahn,R.S.,
            Korhonen,T., Kranzler,H.R., Krauter,K., van Lier,P.A., Lubke,G.H.,
            Madden,P.A., Magi,R., McGue,M.K., Medland,S.E., Meeus,W.H.,
            Miller,M.B., Montgomery,G.W., Nivard,M.G., Nolte,I.M.,
            Oldehinkel,A.J., Pausova,Z., Qaiser,B., Quaye,L.,
            Ramos-Quiroga,J.A., Richarte,V., Rose,R.J., Shin,J.,
            Stallings,M.C., Stiby,A.I., Wall,T.L., Wright,M.J., Koot,H.M.,
            Paus,T., Hewitt,J.K., Ribases,M., Kaprio,J., Boks,M.P., Snieder,H.,
            Spector,T., Munafo,M.R., Metspalu,A., Gelernter,J., Boomsma,D.I.,
            Iacono,W.G., Martin,N.G., Gillespie,N.A., Derks,E.M. and Vink,J.M.
  TITLE     Genome-wide association study of lifetime cannabis use based on a
            large meta-analytic sample of 32 330 subjects from the
            International Cannabis Consortium
  JOURNAL   Transl Psychiatry 6 (3), e769 (2016)
   PUBMED   27023175
  REMARK    GeneRIF: SCOC SNPs were associated with lifetime cannabis use, but
            the association did not reach genome-wide significance.
            [Meta-Analysis]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Alborghetti,M.R., Furlan Ada,S., da Silva,J.C., Sforca,M.L.,
            Honorato,R.V., Granato,D.C., dos Santos Migueleti,D.L., Neves,J.L.,
            de Oliveira,P.S., Paes-Leme,A.F., Zeri,A.C., de Torriani,I.C. and
            Kobarg,J.
  TITLE     Structural analysis of intermolecular interactions in the kinesin
            adaptor complex fasciculation and elongation protein zeta 1/ short
            coiled-coil protein (FEZ1/SCOCO)
  JOURNAL   PLoS One 8 (10), e76602 (2013)
   PUBMED   24116125
  REMARK    GeneRIF: Studies indicate that FEZ1 (fasciculation and elongation
            protein zeta 1), SCOCO (short coiled-coil protein) and kinesins
            (kinesin heavy chain) are involved in biological transport process.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Behrens,C., Binotti,B., Schmidt,C., Robinson,C.V., Chua,J.J. and
            Kuhnel,K.
  TITLE     Crystal structure of the human short coiled coil protein and
            insights into SCOC-FEZ1 complex formation
  JOURNAL   PLoS One 8 (10), e76355 (2013)
   PUBMED   24098481
  REMARK    GeneRIF: SCOC forms a stable homogeneous complex with the coiled
            coil domain of FEZ1. SCOC dimerization and the SCOC surface residue
            R117 are important for this interaction.
            Erratum:[PLoS One. 2013;8(10).
            doi:10.1371/annotation/cb60d973-58aa-45e0-bbb3-1c7f5a42a8d2]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 122)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
  REMARK    GeneRIF: The identification of SCOC and WAC as novel regulatory
            proteins with diverse functions in autophagy contributes towards a
            fuller understanding of autophagosome formation.
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Van Valkenburgh,H., Shern,J.F., Sharer,J.D., Zhu,X. and Kahn,R.A.
  TITLE     ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
            specific and shared effectors: characterizing ARL1-binding proteins
  JOURNAL   J Biol Chem 276 (25), 22826-22837 (2001)
   PUBMED   11303027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA625782.1, BC016511.1 and
            AA213765.1.
            
            Summary: This gene encodes a short coiled-coiled domain-containing
            protein that localizes to the Golgi apparatus. The encoded protein
            interacts with ADP-ribosylation factor-like proteins. Pseudogenes
            of this gene are found on chromosomes 1 and 14. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (5) differs in the 5' UTR and 5'
            coding region, compared to variant 1, resulting in an isoform (4)
            with a distinct and shorter N-terminus, compared to isoform 1.
            Variants 4, 5 and 6 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA625782.1, SRR1660805.196764.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..122
                     /product="short coiled-coil protein isoform 4"
                     /calculated_mol_wt=13797
     Region          53..113
                     /region_name="DUF2205"
                     /note="Short coiled-coil protein; pfam10224"
                     /db_xref="CDD:431150"
     CDS             1..122
                     /gene="SCOC"
                     /gene_synonym="HRIHFB2072; SCOCO; UNC-69"
                     /coded_by="NM_001153585.1:179..547"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS3750.1"
                     /db_xref="GeneID:60592"
                     /db_xref="HGNC:HGNC:20335"
ORIGIN      
        1 mdgsrkeeee dstftnisla ddidhssril yprpksllpk mmnadmdavd aenqveleek
       61 trlinqvlel qhtledlsar vdavkeenlk lksenqvlgq yienlmsass vfqttdtksk
      121 rk
//
LOCUS       NP_001265390            1128 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001265390
VERSION     NP_001265390.1
DBSOURCE    REFSEQ: accession NM_001278461.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1128)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1128)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1128)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1128)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1128)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1128)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1128)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1128)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1128)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1128)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4, BC071588.1, AB023194.1 and AI261693.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            coding sequence and lacks two alternate in-frame exons compared to
            variant 1. The resulting isoform (4) is shorter at the N-terminus
            and lacks two alternate internal segments compared to variant 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.31175.1,
                                           SRR1660803.55148.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1128
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1128
                     /product="cordon-bleu protein-like 1 isoform 4"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=123737
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          60..126
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          144..222
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          249..309
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            260
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            284
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          291..296
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          325..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            344
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            356
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          360..365
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            438
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            441
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          454..499
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            461
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            471
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            584
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          780..840
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            786
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          <789..1026
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            813
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            814
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            821
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          882..964
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            911
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            917
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            947
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          995..1081
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1069
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1070
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1077..1102
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1081..1082,1084..1086,1088..1090,1098..1101)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1098..1101
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     Region          1103..1128
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1121
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     CDS             1..1128
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001278461.2:237..3623"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS63045.1"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mdgrtprpqd aparrkpkak aplppaetky tdvssaadsv estafimeqk enmidkdvel
       61 svvlpgdiik sttvhgskpm mdlliflcaq yhlnpssyti dllsaeqnhi kfkpntpigm
      121 levekvilkp kmldkkkptp iipektvrvv infkktqkti vrvsphaslq elapiicskc
      181 efdplhtlll kdyqsqepld ltkslndlgl relyamdvnr escqisqnld imkekenkgf
      241 fsffqrskkk rdqtasapat plvnkhrptf trsntiskpy isntlpsdap kkrraplppm
      301 pasqsvpqdl ahiqerpasc ivksmsvdet dkspceagrv ragslqlssm sagnsslrrt
      361 krkapsppsk ipphqsdens rvtalqpvdg vppdsasean speelsspag issdysleei
      421 dekeelsevp kveaenispk sqdipfvstd iintlkndpd salgngsgef sqnsmeekqe
      481 tkstdgqeph svvydtsngk kvvdsirnlk slgpnqenvv qneiivypen tednmkngvk
      541 kteinvegva knnnidmeve rpsnseahet dtaisykenh laassvpdqk lnqpsaektk
      601 daaiqttpsc nsfdgkhqdh nlsdskveec vqtsnnnist qhsclssqds vntsrefrsq
      661 gtliihsedp ltvkdpicah gnddllppvd ridknstasy lknyplyrqd ynpkpkpsne
      721 itreyipkig mttykivppk sleiskdwqs etieykddqd mhalgkkhth envketaiqt
      781 edsaisespe eplpnlkpkp nlrtehqvps svsspddamv splkpapkmt rdtgtapfap
      841 nleeinnile skfksrasna qakpssfflq mqkrvsghyv tsaaaksvha apnpapkelt
      901 nkeaerdmlp speqtlspls kmphsvpqpl vektdddvig qapaeasppp iapkpvtipa
      961 sqvstqnlkt lktfgaprpy sssgpspfal avvkrsqsfs kertespsas alvqppante
     1021 egkthsvnkf vdipqlgvsd kennsahneq nsqiptptdg psftvmrqss ltfqssdpeq
     1081 mrqslltair sgeaaaklkr vtipsntisv ngrsrlshsm spdaqdgh
//
LOCUS       NP_001269779             817 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 4 regulatory subunit 3B
            isoform 3 [Homo sapiens].
ACCESSION   NP_001269779 XP_005264500
VERSION     NP_001269779.1
DBSOURCE    REFSEQ: accession NM_001282850.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 817)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 817)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 817)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   4  (residues 1 to 817)
  AUTHORS   Kristiansson,K., Perola,M., Tikkanen,E., Kettunen,J., Surakka,I.,
            Havulinna,A.S., Stancakova,A., Barnes,C., Widen,E., Kajantie,E.,
            Eriksson,J.G., Viikari,J., Kahonen,M., Lehtimaki,T.,
            Raitakari,O.T., Hartikainen,A.L., Ruokonen,A., Pouta,A., Jula,A.,
            Kangas,A.J., Soininen,P., Ala-Korpela,M., Mannisto,S.,
            Jousilahti,P., Bonnycastle,L.L., Jarvelin,M.R., Kuusisto,J.,
            Collins,F.S., Laakso,M., Hurles,M.E., Palotie,A., Peltonen,L.,
            Ripatti,S. and Salomaa,V.
  TITLE     Genome-wide screen for metabolic syndrome susceptibility Loci
            reveals strong lipid gene contribution but no evidence for common
            genetic basis for clustering of metabolic syndrome traits
  JOURNAL   Circ Cardiovasc Genet 5 (2), 242-249 (2012)
   PUBMED   22399527
REFERENCE   5  (residues 1 to 817)
  AUTHORS   Chen,G.I., Tisayakorn,S., Jorgensen,C., D'Ambrosio,L.M.,
            Goudreault,M. and Gingras,A.C.
  TITLE     PP4R4/KIAA1622 forms a novel stable cytosolic complex with
            phosphoprotein phosphatase 4
  JOURNAL   J Biol Chem 283 (43), 29273-29284 (2008)
   PUBMED   18715871
REFERENCE   6  (residues 1 to 817)
  AUTHORS   Chowdhury,D., Xu,X., Zhong,X., Ahmed,F., Zhong,J., Liao,J.,
            Dykxhoorn,D.M., Weinstock,D.M., Pfeifer,G.P. and Lieberman,J.
  TITLE     A PP4-phosphatase complex dephosphorylates gamma-H2AX generated
            during DNA replication
  JOURNAL   Mol Cell 31 (1), 33-46 (2008)
   PUBMED   18614045
  REMARK    GeneRIF: A three-protein PP4 phosphatase complex in mammalian
            cells, containing PP4C, PP4R2, and PP4R3beta, specifically
            dephosphorylates ATR-mediated gamma-H2AX generated during DNA
            replication.
REFERENCE   7  (residues 1 to 817)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   8  (residues 1 to 817)
  AUTHORS   Gingras,A.C., Caballero,M., Zarske,M., Sanchez,A., Hazbun,T.R.,
            Fields,S., Sonenberg,N., Hafen,E., Raught,B. and Aebersold,R.
  TITLE     A novel, evolutionarily conserved protein phosphatase complex
            involved in cisplatin sensitivity
  JOURNAL   Mol Cell Proteomics 4 (11), 1725-1740 (2005)
   PUBMED   16085932
REFERENCE   9  (residues 1 to 817)
  AUTHORS   Mendoza,M.C., Du,F., Iranfar,N., Tang,N., Ma,H., Loomis,W.F. and
            Firtel,R.A.
  TITLE     Loss of SMEK, a novel, conserved protein, suppresses MEK1 null cell
            polarity, chemotaxis, and gene expression defects
  JOURNAL   Mol Cell Biol 25 (17), 7839-7853 (2005)
   PUBMED   16107728
REFERENCE   10 (residues 1 to 817)
  AUTHORS   Kittler,R., Putz,G., Pelletier,L., Poser,I., Heninger,A.K.,
            Drechsel,D., Fischer,S., Konstantinova,I., Habermann,B.,
            Grabner,H., Yaspo,M.L., Himmelbauer,H., Korn,B., Neugebauer,K.,
            Pisabarro,M.T. and Buchholz,F.
  TITLE     An endoribonuclease-prepared siRNA screen in human cells identifies
            genes essential for cell division
  JOURNAL   Nature 432 (7020), 1036-1040 (2004)
   PUBMED   15616564
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB261776.1, BC006215.2, AC015982.9 and BE535214.1.
            
            On Sep 20, 2013 this sequence version replaced XP_005264500.1.
            
            Transcript Variant: This variant (3) lacks an in-frame exon in the
            coding region, compared to variant 1. The resulting isoform (3)
            lacks an internal segment, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.17569.1,
                                           SRR1803616.191752.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..817
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..817
                     /product="serine/threonine-protein phosphatase 4
                     regulatory subunit 3B isoform 3"
                     /note="serine/threonine-protein phosphatase 4 regulatory
                     subunit 3B; SMEK homolog 2, suppressor of mek1"
                     /calculated_mol_wt=93587
     Region          7..>65
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          168..359
                     /region_name="PP4R3"
                     /note="Phosphatase 4 regulatory subunit 3; pfam04802"
                     /db_xref="CDD:461435"
     CDS             1..817
                     /gene="PPP4R3B"
                     /gene_synonym="FLFL2; PP4R3B; PSY2; SMEK2; smk1"
                     /coded_by="NM_001282850.2:338..2791"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS62913.1"
                     /db_xref="GeneID:57223"
                     /db_xref="HGNC:HGNC:29267"
                     /db_xref="MIM:610352"
ORIGIN      
        1 msdtrrrvkv ytlnedrqwd drgtghvsst yveelkgmsl lvraesdgsl lleskinpnt
       61 ayqkqqdtli vwseaenydl alsfqekagc deiwekicqv qgkdpsvevt qdlideseee
      121 rfeempetsh lidlptceln kleeiadlvt svlsspirre klalaleneg yikkllqlfq
      181 acenlenteg lhhlyeiirg ilflnkatlf evmfsdecim dvvgcleydp alaqpkrhre
      241 fltktakfke vipitdselr qkihqtyrvq yiqdiilptp svfeenflst ltsfiffnkv
      301 eivsmlqede kflsevfaql tdeatdddkr relvnffkef cafsqtlqpq nrdaffktla
      361 klgilpalei vmgmddlqvr saatdifsyl vefspsmvre fvmqeaqqsd ddillinvvi
      421 eqmicdtdpe lggavqlmgl lrtlidpenm lattnkteks eflnffynhc mhvltapllt
      481 ntsedkcekd nivgsnknnt icpdnyqtaq llalilellt fcvehhtyhi knyimnkdll
      541 rrvlvlmnsk htflalcalr fmrriiglkd efynryitkg nlfepvinal ldngtrynll
      601 nsavielfef irvedikslt ahivenfyka lesieyvqtf kglktkyeqe kdrqnqklns
      661 vpsilrsnrf rrdakaleed eemwfnedee eegkavvapv ekpkpeddfp dnyekfmetk
      721 kakesedken lpkrtspggf kftfshsasa angtnsksvv aqippatsng ssskttnlpt
      781 svtatkgslv glvdypddee edeeeesspr krprlgs
//
LOCUS       NP_001273991             491 aa            linear   PRI 20-NOV-2025
DEFINITION  rab5 GDP/GTP exchange factor isoform c [Homo sapiens].
ACCESSION   NP_001273991 XP_005250336
VERSION     NP_001273991.1
DBSOURCE    REFSEQ: accession NM_001287062.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Fan,H., Xin,T., Dong,X., Yang,F., Zhang,R., Feng,S., He,D., Guo,H.
            and Pang,Q.
  TITLE     RabGEF1 functions as an oncogene in U251 glioblastoma cells and is
            involved in regulating AKT and Erk pathways
  JOURNAL   Exp Mol Pathol 118, 104571 (2021)
   PUBMED   33166495
  REMARK    GeneRIF: RabGEF1 functions as an oncogene in U251 glioblastoma
            cells and is involved in regulating AKT and Erk pathways.
REFERENCE   6  (residues 1 to 491)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   7  (residues 1 to 491)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
  REMARK    GeneRIF: GGAs, a family of Arf-dependent clathrin adaptors involved
            in selection of TGN cargo, interact with the Rabaptin-5-Rabex-5
            complex, a Rab4/Rab5 effector regulating endosome fusion
REFERENCE   8  (residues 1 to 491)
  AUTHORS   Lippe,R., Miaczynska,M., Rybin,V., Runge,A. and Zerial,M.
  TITLE     Functional synergy between Rab5 effector Rabaptin-5 and exchange
            factor Rabex-5 when physically associated in a complex
  JOURNAL   Mol Biol Cell 12 (7), 2219-2228 (2001)
   PUBMED   11452015
REFERENCE   9  (residues 1 to 491)
  AUTHORS   Nimmrich,I., Erdmann,S., Melchers,U., Finke,U., Hentsch,S.,
            Moyer,M.P., Hoffmann,I. and Muller,O.
  TITLE     Seven genes that are differentially transcribed in colorectal tumor
            cell lines
  JOURNAL   Cancer Lett 160 (1), 37-43 (2000)
   PUBMED   11098082
REFERENCE   10 (residues 1 to 491)
  AUTHORS   Horiuchi,H., Lippe,R., McBride,H.M., Rubino,M., Woodman,P.,
            Stenmark,H., Rybin,V., Wilm,M., Ashman,K., Mann,M. and Zerial,M.
  TITLE     A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links
            nucleotide exchange to effector recruitment and function
  JOURNAL   Cell 90 (6), 1149-1159 (1997)
   PUBMED   9323142
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC027644.9.
            
            On Nov 23, 2013 this sequence version replaced XP_005250336.1.
            
            Summary: RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM
            603616) that is required for endocytic membrane fusion, and it
            serves as a specific guanine nucleotide exchange factor (GEF) for
            RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997 [PubMed
            9323142]).[supplied by OMIM, Mar 2010].
            
            Transcript Variant: This variant (3) contains alternate 5' exon
            structure and includes an additional internal exon, and it thus
            differs in its 5' UTR and initiates translation at an alternate
            start codon, compared to variant 1. The encoded isoform (c) is
            longer at the N-terminus, compared to isoform a. Variants 3, 4, and
            9-20 all encode the same isoform (c).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK290678.1, SRR1803613.273835.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.21"
     Protein         1..491
                     /product="rab5 GDP/GTP exchange factor isoform c"
                     /note="Rab5 GDP/GTP exchange factor; rabaptin-5-associated
                     exchange factor for Rab5; RAB guanine nucleotide exchange
                     factor (GEF) 1"
                     /calculated_mol_wt=56760
     Region          17..40
                     /region_name="zf-A20"
                     /note="A20-like zinc finger; pfam01754"
                     /db_xref="CDD:460313"
     Region          158..220
                     /region_name="DUF5601"
                     /note="Domain of unknown function (DUF5601); pfam18151"
                     /db_xref="CDD:465668"
     Region          270..370
                     /region_name="VPS9"
                     /note="Vacuolar sorting protein 9 (VPS9) domain;
                     pfam02204"
                     /db_xref="CDD:460489"
     CDS             1..491
                     /gene="RABGEF1"
                     /gene_synonym="rabex-5; RABEX5; RAP1"
                     /coded_by="NM_001287062.2:273..1748"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS5535.1"
                     /db_xref="GeneID:27342"
                     /db_xref="HGNC:HGNC:17676"
                     /db_xref="MIM:609700"
ORIGIN      
        1 mslkserrgi hvdqsdllck kgcgyygnpa wqgfcskcwr eeyhkarqkq iqedwelaer
       61 lqreeeeafa ssqssqgaqs ltfskfeekk tnektrkvtt vkkffsassr vgskkeiqea
      121 kapspsinrq tsietdrvsk efieflktfh ktgqeiykqt klflegmhyk rdlsieeqse
      181 caqdfyhnva ermqtrgkvp pervekimdq iekyimtrly kyvfcpettd dekkdlaiqk
      241 riralrwvtp qmlcvpvned ipevsdmvvk aitdiiemds krvprdklac itkcskhifn
      301 aikitknepa saddflptli yivlkgnppr lqsniqyitr fcnpsrlmtg edgyyftnlc
      361 cavafiekld aqslnlsqed fdrymsgqts prkqeaesws pdaclgvkqm yknldllsql
      421 nerqerimne akklekdlid wtdgiarevq divekyplei kppnqplaai dsenvendkl
      481 ppplqpqvya g
//
LOCUS       NP_001354567             821 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform i [Homo sapiens].
ACCESSION   NP_001354567
VERSION     NP_001354567.1
DBSOURCE    REFSEQ: accession NM_001367638.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 821)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 821)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 821)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 821)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 821)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 821)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 821)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 821)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 821)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 821)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.19945.1,
                                           SRR1803612.108942.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..821
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..821
                     /product="SUN domain-containing protein 1 isoform i"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=90911
     Region          62..328
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          453..506
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(453,456..457,460,463..464,467..468,470..471,
                     474..475,477..478,481..482,484..485,488,491..492,495,
                     498..499,502..503,505..506)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          465..>598
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          583..641
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          684..819
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..821
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367638.1:52..2517"
                     /note="isoform i is encoded by transcript variant 9"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc ddckgkrhld ahtaahsqsp
      241 rlpgragtlw hiwacagyfl lqilrrigav gqavsrtaws alwlavvapg kaasgvfwwl
      301 gigwyqfvtl iswlnvfllt rclrnickfl vlliplflll glslrgqgnf fsflpvlnwa
      361 smhrtqrvdd pqdvfkptts rlkqplqgds eafpwhwmsg veqqvaslsg qchhhgenlr
      421 elttllqklq arvdqmegga agpsasvrda vgqppretdf mafhqehevr mshledilgk
      481 lrekseaiqk eleqtkqkti savgeqllpt vehlqleldq lkselsswrh vktgcetvda
      541 vqervdvqvr emvkllfsed qqggsleqll qrfssqfvsk gdlqtmlrdl qlqilrnvth
      601 hvsvtkqlpt seavvsavse agasgiteaq araivnsalk lysqdktgmv dfalesgggs
      661 ilstrcsety etktalmslf giplwyfsqs prvviqpdiy pgncwafkgs qgylvvrlsm
      721 mihpaaftle hipktlsptg nissapkdfa vygleneyqe egqllgqfty dqdgeslqmf
      781 qalkrpddta fqivelrifs nwghpeytcl yrfrvhgepv k
//
LOCUS       NP_001191036              85 aa            linear   PRI 20-NOV-2025
DEFINITION  bcl-2-like protein 11 isoform 12 [Homo sapiens].
ACCESSION   NP_001191036
VERSION     NP_001191036.1
DBSOURCE    REFSEQ: accession NM_001204107.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 85)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 85)
  AUTHORS   Wang,Y., Zeng,H., Li,L., Liu,J., Lin,J., Bie,Y., Wang,S., Cheng,X.,
            Nashun,B., Yao,Y., Hu,X. and Zhao,Y.
  TITLE     Pokemon inhibits Bim transcription to promote the proliferation,
            anti-anoikis, invasion, histological grade, and dukes stage of
            colorectal neoplasms
  JOURNAL   J Cancer Res Clin Oncol 150 (8), 380 (2024)
   PUBMED   39095579
  REMARK    GeneRIF: Pokemon inhibits Bim transcription to promote the
            proliferation, anti-anoikis, invasion, histological grade, and
            dukes stage of colorectal neoplasms.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 85)
  AUTHORS   Zhang,Q., Wu,Q., Huan,X.J., Song,S.S., Bao,X.B., Miao,Z.H. and
            Wang,Y.Q.
  TITLE     Co-inhibition of BET and NAE enhances BIM-dependent apoptosis with
            augmented cancer therapeutic efficacy
  JOURNAL   Biochem Pharmacol 223, 116198 (2024)
   PUBMED   38588830
  REMARK    GeneRIF: Co-inhibition of BET and NAE enhances BIM-dependent
            apoptosis with augmented cancer therapeutic efficacy.
REFERENCE   4  (residues 1 to 85)
  AUTHORS   Lu,L., Ma,D. and Xi,Z.
  TITLE     Coexpression of TP53, BIM, and PTEN Enhances the Therapeutic
            Efficacy of Non-Small-Cell Lung Cancer
  JOURNAL   Biomacromolecules 25 (2), 792-808 (2024)
   PUBMED   38237562
  REMARK    GeneRIF: Coexpression of TP53, BIM, and PTEN Enhances the
            Therapeutic Efficacy of Non-Small-Cell Lung Cancer.
REFERENCE   5  (residues 1 to 85)
  AUTHORS   Matsumoto,M., Ogawa,N., Fukuda,T., Bando,Y., Nishimura,T. and
            Usuda,J.
  TITLE     Protein interaction networks characterizing the A549 cells Klotho
            transfected are associated with activated pro-apoptotic Bim and
            suppressed Wnt/beta-catenin signaling pathway
  JOURNAL   Sci Rep 14 (1), 2130 (2024)
   PUBMED   38267588
  REMARK    GeneRIF: Protein interaction networks characterizing the A549 cells
            Klotho transfected are associated with activated pro-apoptotic Bim
            and suppressed Wnt/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 85)
  AUTHORS   Ng,K.P., Hillmer,A.M., Chuah,C.T., Juan,W.C., Ko,T.K., Teo,A.S.,
            Ariyaratne,P.N., Takahashi,N., Sawada,K., Fei,Y., Soh,S., Lee,W.H.,
            Huang,J.W., Allen,J.C. Jr., Woo,X.Y., Nagarajan,N., Kumar,V.,
            Thalamuthu,A., Poh,W.T., Ang,A.L., Mya,H.T., How,G.F., Yang,L.Y.,
            Koh,L.P., Chowbay,B., Chang,C.T., Nadarajan,V.S., Chng,W.J.,
            Than,H., Lim,L.C., Goh,Y.T., Zhang,S., Poh,D., Tan,P., Seet,J.E.,
            Ang,M.K., Chau,N.M., Ng,Q.S., Tan,D.S., Soda,M., Isobe,K.,
            Nothen,M.M., Wong,T.Y., Shahab,A., Ruan,X., Cacheux-Rataboul,V.,
            Sung,W.K., Tan,E.H., Yatabe,Y., Mano,H., Soo,R.A., Chin,T.M.,
            Lim,W.T., Ruan,Y. and Ong,S.T.
  TITLE     A common BIM deletion polymorphism mediates intrinsic resistance
            and inferior responses to tyrosine kinase inhibitors in cancer
  JOURNAL   Nat Med 18 (4), 521-528 (2012)
   PUBMED   22426421
  REMARK    GeneRIF: the heterogeneity of tyrosine kinase inhibitors responses
            across individuals and suggest the possibility of personalizing
            therapy with BH3 mimetics to overcome BIM-polymorphism-associated
            tyrosine kinase inhibitors resistance.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 85)
  AUTHORS   Huang,D.C., Adams,J.M. and Cory,S.
  TITLE     The conserved N-terminal BH4 domain of Bcl-2 homologues is
            essential for inhibition of apoptosis and interaction with CED-4
  JOURNAL   EMBO J 17 (4), 1029-1039 (1998)
   PUBMED   9463381
REFERENCE   8  (residues 1 to 85)
  AUTHORS   O'Connor,L., Strasser,A., O'Reilly,L.A., Hausmann,G., Adams,J.M.,
            Cory,S. and Huang,D.C.
  TITLE     Bim: a novel member of the Bcl-2 family that promotes apoptosis
  JOURNAL   EMBO J 17 (2), 384-395 (1998)
   PUBMED   9430630
REFERENCE   9  (residues 1 to 85)
  AUTHORS   Zha,J., Harada,H., Yang,E., Jockel,J. and Korsmeyer,S.J.
  TITLE     Serine phosphorylation of death agonist BAD in response to survival
            factor results in binding to 14-3-3 not BCL-X(L)
  JOURNAL   Cell 87 (4), 619-628 (1996)
   PUBMED   8929531
REFERENCE   10 (residues 1 to 85)
  AUTHORS   Wang,K., Yin,X.M., Chao,D.T., Milliman,C.L. and Korsmeyer,S.J.
  TITLE     BID: a novel BH3 domain-only death agonist
  JOURNAL   Genes Dev 10 (22), 2859-2869 (1996)
   PUBMED   8918887
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC096670.1, AK290377.1,
            AY423442.1 and AI268146.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene belongs to the BCL-2
            protein family. BCL-2 family members form hetero- or homodimers and
            act as anti- or pro-apoptotic regulators that are involved in a
            wide variety of cellular activities. The protein encoded by this
            gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to
            interact with other members of the BCL-2 protein family and to act
            as an apoptotic activator. The expression of this gene can be
            induced by nerve growth factor (NGF), as well as by the forkhead
            transcription factor FKHR-L1, which suggests a role of this gene in
            neuronal and lymphocyte apoptosis. Transgenic studies of the mouse
            counterpart suggested that this gene functions as an essential
            initiator of apoptosis in thymocyte-negative selection. Several
            alternatively spliced transcript variants of this gene have been
            identified. [provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (12) uses an alternate in-frame
            splice site in the 5' coding region, contains two alternate
            internal exons, and differs in the 3' coding region and UTR,
            compared to variant 1. The resulting isoform (12) is shorter and
            has a distinct C-terminus, compared to isoform 1. This record was
            created to support clinical studies, but the encoded isoform
            currently lacks experimental evidence.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AY423442.1 [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1965299,
                                    SAMEA1968540 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            NMD candidate             :: translation inferred
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..85
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q13"
     Protein         1..85
                     /product="bcl-2-like protein 11 isoform 12"
                     /note="bcl-2 interacting protein Bim; bcl-2 interacting
                     mediator of cell death; bcl-2-related ovarian death
                     agonist; BCL2-like 11 (apoptosis facilitator)"
                     /calculated_mol_wt=9465
     Region          4..40
                     /region_name="Bim_N"
                     /note="Bim protein N-terminus; pfam06773"
                     /db_xref="CDD:429111"
     Region          46..76
                     /region_name="Bclx_interact"
                     /note="Bcl-x interacting, BH3 domain; pfam08945"
                     /db_xref="CDD:462643"
     CDS             1..85
                     /gene="BCL2L11"
                     /gene_synonym="BAM; BIM; BOD"
                     /coded_by="NM_001204107.1:289..546"
                     /note="isoform 12 is encoded by transcript variant 12"
                     /db_xref="CCDS:CCDS56132.1"
                     /db_xref="GeneID:10018"
                     /db_xref="HGNC:HGNC:994"
                     /db_xref="MIM:603827"
ORIGIN      
        1 makqpsdvss ecdregrqlq paerppqlrp gaptslqtep qasmrqaepa dmrpeiwiaq
       61 elrrigdefn ayyarrlakl lasst
//
LOCUS       NP_071762                761 aa            linear   PRI 20-NOV-2025
DEFINITION  semaphorin-4A isoform 1 precursor [Homo sapiens].
ACCESSION   NP_071762
VERSION     NP_071762.2
DBSOURCE    REFSEQ: accession NM_022367.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 761)
  AUTHORS   Hou,T., Zhang,P., Tian,H., Luo,Y., Li,J., Zhang,K. and Li,Y.
  TITLE     Semaphorin 4A Maintains Trophoblastic Function via Activating the
            STAT3 Pathway
  JOURNAL   Biomolecules 14 (7), 826 (2024)
   PUBMED   39062540
  REMARK    GeneRIF: Semaphorin 4A Maintains Trophoblastic Function via
            Activating the STAT3 Pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 761)
  AUTHORS   Wei,X., Liu,Z., Shen,Y., Dong,H., Chen,K., Shi,X., Chen,Y., Wang,B.
            and Dong,S.
  TITLE     Semaphorin4A promotes lung cancer by activation of NF-kappaB
            pathway mediated by PlexinB1
  JOURNAL   PeerJ 11, e16292 (2023)
   PUBMED   37901456
  REMARK    GeneRIF: Semaphorin4A promotes lung cancer by activation of
            NF-kappaB pathway mediated by PlexinB1.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 761)
  AUTHORS   Naito,Y., Koyama,S., Masuhiro,K., Hirai,T., Uenami,T., Inoue,T.,
            Osa,A., Machiyama,H., Watanabe,G., Sax,N., Villa,J.,
            Kinugasa-Katayama,Y., Nojima,S., Yaga,M., Hosono,Y., Okuzaki,D.,
            Satoh,S., Tsuda,T., Nakanishi,Y., Suga,Y., Morita,T., Fukushima,K.,
            Nishide,M., Shiroyama,T., Miyake,K., Iwahori,K., Hirata,H.,
            Nagatomo,I., Yano,Y., Tamiya,M., Kumagai,T., Takemoto,N.,
            Inohara,H., Yamasaki,S., Yamashita,K., Aoshi,T., Akbay,E.A.,
            Hosen,N., Shintani,Y., Takamatsu,H., Mori,M., Takeda,Y. and
            Kumanogoh,A.
  TITLE     Tumor-derived semaphorin 4A improves PD-1-blocking antibody
            efficacy by enhancing CD8+ T cell cytotoxicity and proliferation
  JOURNAL   Sci Adv 9 (20), eade0718 (2023)
   PUBMED   37205755
  REMARK    GeneRIF: Tumor-derived semaphorin 4A improves PD-1-blocking
            antibody efficacy by enhancing CD8[+] T cell cytotoxicity and
            proliferation.
REFERENCE   4  (residues 1 to 761)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 761)
  AUTHORS   Eiza,N., Garty,M., Staun-Ram,E., Miller,A. and Vadasz,Z.
  TITLE     The possible involvement of sema3A and sema4A in the pathogenesis
            of multiple sclerosis
  JOURNAL   Clin Immunol 238, 109017 (2022)
   PUBMED   35460904
  REMARK    GeneRIF: The possible involvement of sema3A and sema4A in the
            pathogenesis of multiple sclerosis.
REFERENCE   6  (residues 1 to 761)
  AUTHORS   Kumanogoh,A. and Kikutani,H.
  TITLE     Immune semaphorins: a new area of semaphorin research
  JOURNAL   J Cell Sci 116 (Pt 17), 3463-3470 (2003)
   PUBMED   12893810
  REMARK    Review article
REFERENCE   7  (residues 1 to 761)
  AUTHORS   Kikutani,H. and Kumanogoh,A.
  TITLE     Semaphorins in interactions between T cells and antigen-presenting
            cells
  JOURNAL   Nat Rev Immunol 3 (2), 159-167 (2003)
   PUBMED   12563299
  REMARK    Review article
REFERENCE   8  (residues 1 to 761)
  AUTHORS   Kumanogoh,A., Marukawa,S., Suzuki,K., Takegahara,N., Watanabe,C.,
            Ch'ng,E., Ishida,I., Fujimura,H., Sakoda,S., Yoshida,K. and
            Kikutani,H.
  TITLE     Class IV semaphorin Sema4A enhances T-cell activation and interacts
            with Tim-2
  JOURNAL   Nature 419 (6907), 629-633 (2002)
   PUBMED   12374982
REFERENCE   9  (residues 1 to 761)
  AUTHORS   Puschel,A.W., Adams,R.H. and Betz,H.
  TITLE     Murine semaphorin D/collapsin is a member of a diverse gene family
            and creates domains inhibitory for axonal extension
  JOURNAL   Neuron 14 (5), 941-948 (1995)
   PUBMED   7748561
REFERENCE   10 (residues 1 to 761)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA409501.1, BC020974.1 and
            AY358531.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 10, 2002 this sequence version replaced NP_071762.1.
            
            Summary: This gene encodes a member of the semaphorin family of
            soluble and transmembrane proteins. Semaphorins are involved in
            numerous functions, including axon guidance, morphogenesis,
            carcinogenesis, and immunomodulation. The encoded protein is a
            single-pass type I membrane protein containing an
            immunoglobulin-like C2-type domain, a PSI domain and a sema domain.
            It inhibits axonal extension by providing local signals to specify
            territories inaccessible for growing axons. It is an activator of
            T-cell-mediated immunity and suppresses vascular endothelial growth
            factor (VEGF)-mediated endothelial cell migration and proliferation
            in vitro and angiogenesis in vivo. Mutations in this gene are
            associated with retinal degenerative diseases including retinitis
            pigmentosa type 35 (RP35) and cone-rod dystrophy type 10 (CORD10).
            Multiple alternatively spliced transcript variants encoding
            different isoforms have been identified.[provided by RefSeq, Sep
            2010].
            
            Transcript Variant: This variant (1) is the longest transcript.
            Variants 1-3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC020974.1, SRR1660803.161175.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368285.8/ ENSP00000357268.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..761
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..761
                     /product="semaphorin-4A isoform 1 precursor"
                     /note="sema B; semaphorin-B; sema domain, immunoglobulin
                     domain (Ig), transmembrane domain (TM) and short
                     cytoplasmic domain, (semaphorin) 4A"
                     /calculated_mol_wt=80167
     sig_peptide     1..32
                     /calculated_mol_wt=3425
     mat_peptide     33..761
                     /product="semaphorin-4A isoform 1"
                     /calculated_mol_wt=80167
     Region          55..495
                     /region_name="Sema_4A"
                     /note="The Sema domain, a protein interacting module, of
                     semaphorin 4A (Sema4A); cd11256"
                     /db_xref="CDD:200517"
     Site            order(115..117,178,199,201..202,204,219,222,224,229,252,
                     276..280,282,361..362,386,390,393)
                     /site_type="other"
                     /note="plexin binding site [polypeptide binding]"
                     /db_xref="CDD:200517"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            135
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Site            order(253..254,256,259..261,295,297..299,301,303,326..328,
                     334..335,399,411)
                     /site_type="other"
                     /note="putative homodimer interface [polypeptide binding]"
                     /db_xref="CDD:200517"
     Region          496..540
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            496
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          566..638
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          576..580
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409456"
     Region          588..592
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409456"
     Region          607..611
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409456"
     Site            607
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          621..626
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409456"
     Site            684..704
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     Region          722..749
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S1.2)"
     CDS             1..761
                     /gene="SEMA4A"
                     /gene_synonym="CORD10; RP35; SEMAB; SEMB"
                     /coded_by="NM_022367.4:210..2495"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS1132.1"
                     /db_xref="GeneID:64218"
                     /db_xref="HGNC:HGNC:10729"
                     /db_xref="MIM:607292"
ORIGIN      
        1 malpalgldp wsllglflfq llqlllpttt aggggqgpmp rvryyagder ralsffhqkg
       61 lqdfdtllls gdgntlyvga reailaldiq dpgvprlknm ipwpasdrkk secafkkksn
      121 etqcfnfirv lvsynvthly tcgtfafspa ctfielqdsy llpisedkvm egkgqspfdp
      181 ahkhtavlvd gmlysgtmnn flgsepilmr tlgsqpvlkt dnflrwlhhd asfvaaipst
      241 qvvyfffeet asefdfferl htsrvarvck ndvggekllq kkwttflkaq llctqpgqlp
      301 fnvirhavll padsptaphi yavftsqwqv ggtrssavca fslldiervf kgkykelnke
      361 tsrwttyrgp etnprpgscs vgpssdkalt fmkdhflmde qvvgtpllvk sgveytrlav
      421 etaqgldghs hlvmylgttt gslhkavvsg dssahlveei qlfpdpepvr nlqlaptqga
      481 vfvgfsggvw rvprancsvy escvdcvlar dphcawdpes rtccllsapn lnswkqdmer
      541 gnpewacasg pmsrslrpqs rpqiikevla vpnsilelpc phlsalasyy wshgpaavpe
      601 asstvyngsl llivqdgvgg lyqcwateng fsypvisywv dsqdqtlald pelagipreh
      661 vkvpltrvsg gaalaaqqsy wphfvtvtvl falvlsgali ilvasplral rargkvqgce
      721 tlrpgekapl sreqhlqspk ecrtsasdvd adnnclgtev a
//
LOCUS       NP_001269898             358 aa            linear   PRI 20-NOV-2025
DEFINITION  uncharacterized protein C14orf93 isoform b [Homo sapiens].
ACCESSION   NP_001269898 XP_005268033
VERSION     NP_001269898.1
DBSOURCE    REFSEQ: accession NM_001282969.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 358)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 358)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 358)
  AUTHORS   Yu,Y., Liu,C., Zhang,J., Zhang,M., Wen,W., Ruan,X., Li,D.,
            Zhang,S., Gao,M. and Chen,L.
  TITLE     Rtfc (4931414P19Rik) Regulates in vitro Thyroid Differentiation and
            in vivo Thyroid Function
  JOURNAL   Sci Rep 7, 43396 (2017)
   PUBMED   28230092
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 358)
  AUTHORS   Liu,C., Yu,Y., Yin,G., Zhang,J., Wen,W., Ruan,X., Li,D., Zhang,S.,
            Cai,W., Gao,M. and Chen,L.
  TITLE     C14orf93 (RTFC) is identified as a novel susceptibility gene for
            familial nonmedullary thyroid cancer
  JOURNAL   Biochem Biophys Res Commun 482 (4), 590-596 (2017)
   PUBMED   27864143
  REMARK    GeneRIF: RTFC promotes thyroid cancer cell survival under starving
            conditions, and thyroid cancer cell migration. The R115Q, V205M and
            G209D RTFC mutants enhance the colony forming capacity of thyroid
            cancer cells, and are able to transform normal thyroid cells. In
            summary, our data suggest the roles of RTFC in thyroid
            carcinogenesis.
REFERENCE   5  (residues 1 to 358)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 358)
  AUTHORS   Fatemifar,G., Hoggart,C.J., Paternoster,L., Kemp,J.P.,
            Prokopenko,I., Horikoshi,M., Wright,V.J., Tobias,J.H., Richmond,S.,
            Zhurov,A.I., Toma,A.M., Pouta,A., Taanila,A., Sipila,K.,
            Lahdesmaki,R., Pillas,D., Geller,F., Feenstra,B., Melbye,M.,
            Nohr,E.A., Ring,S.M., St Pourcain,B., Timpson,N.J., Davey Smith,G.,
            Jarvelin,M.R. and Evans,D.M.
  TITLE     Genome-wide association study of primary tooth eruption identifies
            pleiotropic loci associated with height and craniofacial distances
  JOURNAL   Hum Mol Genet 22 (18), 3807-3817 (2013)
   PUBMED   23704328
REFERENCE   7  (residues 1 to 358)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BX161474.1, CN309429.1 and BC014299.2.
            
            On Sep 24, 2013 this sequence version replaced XP_005268033.1.
            
            Transcript Variant: This variant (6) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (b) has a shorter N-terminus than isoform a. Variants 5 and
            6 encode the same isoform (b).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX161474.1, SRR9304715.254775.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..358
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..358
                     /product="uncharacterized protein C14orf93 isoform b"
                     /note="uncharacterized protein C14orf93; regulator of
                     thyroid function and cancer"
                     /calculated_mol_wt=40005
     Region          <11..358
                     /region_name="DUF4616"
                     /note="Domain of unknown function (DUF4616); pfam15394"
                     /db_xref="CDD:464701"
     CDS             1..358
                     /gene="C14orf93"
                     /gene_synonym="RTFC"
                     /coded_by="NM_001282969.1:441..1517"
                     /note="isoform b is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS61399.1"
                     /db_xref="GeneID:60686"
                     /db_xref="HGNC:HGNC:20162"
ORIGIN      
        1 mrlpgctlaa seaapllnpl vddyvasega vqrvlvpaya kqlspatqla iqratpetgp
       61 engtklpppr pedmlnaaaa ldsaleesgp gstgelrhsl gltvspcrtr gsgqknsrrk
      121 rdlvlsklvh nvhnhitndk rfngsesiks swnisvvkfl leklkqelvt sphnytdkel
      181 kgacvayflt krreyrnsln pfkglkekee kklrsrryrl fanrssimrh fgpedqrlwn
      241 dvteelmsde edslnepgvw varpprfraq rltelcyhld anskhgtkan rvygppsdrl
      301 psaeaqllpp elynpnfqee edeggdenap gspsfdqphk tccpdlnsfi eikvekde
//
LOCUS       NP_001356334             507 aa            linear   PRI 20-NOV-2025
DEFINITION  runt-related transcription factor 2 isoform e [Homo sapiens].
ACCESSION   NP_001356334 NP_004339
VERSION     NP_001356334.1
DBSOURCE    REFSEQ: accession NM_001369405.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 507)
  AUTHORS   Komori,T.
  TITLE     Regulation of Skeletal Development and Maintenance by Runx2 and Sp7
  JOURNAL   Int J Mol Sci 25 (18), 10102 (2024)
   PUBMED   39337587
  REMARK    GeneRIF: Regulation of Skeletal Development and Maintenance by
            Runx2 and Sp7.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 507)
  AUTHORS   Vitale,E., Manicardi,V., Gugnoni,M., Torricelli,F., Donati,B.,
            Muccioli,S., Salviato,E., Rossi,T., Manzotti,G., Piana,S. and
            Ciarrocchi,A.
  TITLE     Exploring the transcriptional cooperation between RUNX2 and its
            associated elncRNA RAIN
  JOURNAL   Cell Death Dis 15 (9), 673 (2024)
   PUBMED   39271656
  REMARK    GeneRIF: Exploring the transcriptional cooperation between RUNX2
            and its associated elncRNA RAIN.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 507)
  AUTHORS   Yalaev,B., Tyurin,A., Akhiiarova,K. and Khusainova,R.
  TITLE     Hypomethylation of the RUNX2 Gene Is a New Potential Biomarker of
            Primary Osteoporosis in Men and Women
  JOURNAL   Int J Mol Sci 25 (13), 7312 (2024)
   PUBMED   39000419
  REMARK    GeneRIF: Hypomethylation of the RUNX2 Gene Is a New Potential
            Biomarker of Primary Osteoporosis in Men and Women.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 507)
  AUTHORS   Drissi,H., Luc,Q., Shakoori,R., Chuva De Sousa Lopes,S., Choi,J.Y.,
            Terry,A., Hu,M., Jones,S., Neil,J.C., Lian,J.B., Stein,J.L., Van
            Wijnen,A.J. and Stein,G.S.
  TITLE     Transcriptional autoregulation of the bone related CBFA1/RUNX2 gene
  JOURNAL   J Cell Physiol 184 (3), 341-350 (2000)
   PUBMED   10911365
REFERENCE   5  (residues 1 to 507)
  AUTHORS   Geoffroy,V., Corral,D.A., Zhou,L., Lee,B. and Karsenty,G.
  TITLE     Genomic organization, expression of the human CBFA1 gene, and
            evidence for an alternative splicing event affecting protein
            function
  JOURNAL   Mamm Genome 9 (1), 54-57 (1998)
   PUBMED   9434946
REFERENCE   6  (residues 1 to 507)
  AUTHORS   Mundlos,S., Otto,F., Mundlos,C., Mulliken,J.B., Aylsworth,A.S.,
            Albright,S., Lindhout,D., Cole,W.G., Henn,W., Knoll,J.H.,
            Owen,M.J., Mertelsmann,R., Zabel,B.U. and Olsen,B.R.
  TITLE     Mutations involving the transcription factor CBFA1 cause
            cleidocranial dysplasia
  JOURNAL   Cell 89 (5), 773-779 (1997)
   PUBMED   9182765
REFERENCE   7  (residues 1 to 507)
  AUTHORS   Feldman,G.J., Robin,N.H., Brueton,L.A., Robertson,E.,
            Thompson,E.M., Siegel-Bartelt,J., Gasser,D.L., Bailey,L.C.,
            Zackai,E.H. and Muenke,M.
  TITLE     A gene for cleidocranial dysplasia maps to the short arm of
            chromosome 6
  JOURNAL   Am J Hum Genet 56 (4), 938-943 (1995)
   PUBMED   7717404
REFERENCE   8  (residues 1 to 507)
  AUTHORS   Levanon,D., Negreanu,V., Bernstein,Y., Bar-Am,I., Avivi,L. and
            Groner,Y.
  TITLE     AML1, AML2, and AML3, the human members of the runt domain
            gene-family: cDNA structure, expression, and chromosomal
            localization
  JOURNAL   Genomics 23 (2), 425-432 (1994)
   PUBMED   7835892
REFERENCE   9  (residues 1 to 507)
  AUTHORS   Ogawa,E., Maruyama,M., Kagoshima,H., Inuzuka,M., Lu,J., Satake,M.,
            Shigesada,K. and Ito,Y.
  TITLE     PEBP2/PEA2 represents a family of transcription factors homologous
            to the products of the Drosophila runt gene and the human AML1 gene
  JOURNAL   Proc Natl Acad Sci U S A 90 (14), 6859-6863 (1993)
   PUBMED   8341710
REFERENCE   10 (residues 1 to 507)
  AUTHORS   Machol,K., Mendoza-Londono,R. and Lee,B.
  TITLE     Cleidocranial Dysplasia Spectrum Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301686
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL096865.28, AL358135.19 and
            AL161907.17.
            
            On Jul 29, 2022 this sequence version replaced NP_004339.3.
            
            Summary: This gene is a member of the RUNX family of transcription
            factors and encodes a nuclear protein with an Runt DNA-binding
            domain. This protein is essential for osteoblastic differentiation
            and skeletal morphogenesis and acts as a scaffold for nucleic acids
            and regulatory factors involved in skeletal gene expression. The
            protein can bind DNA both as a monomer or, with more affinity, as a
            subunit of a heterodimeric complex. Two regions of potential
            trinucleotide repeat expansions are present in the N-terminal
            region of the encoded protein, and these and other mutations in
            this gene have been associated with the bone development disorder
            cleidocranial dysplasia (CCD). Transcript variants that encode
            different protein isoforms result from the use of alternate
            promoters as well as alternate splicing. [provided by RefSeq, Jul
            2016].
            
            Transcript Variant: This variant (7) contains an alternate 5'-most
            exon and initiates translation at an alternate start codon,
            compared to variant 1. The encoded isoform (e) has a distinct and
            shorter N-terminus, compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.113774.1,
                                           SRR6380200.18551.9 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..507
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.1"
     Protein         1..507
                     /product="runt-related transcription factor 2 isoform e"
                     /note="core-binding factor, runt domain, alpha subunit 1;
                     acute myeloid leukemia 3 protein; SL3-3 enhancer factor 1
                     alpha A subunit; runt related transcription factor 2;
                     SL3/AKV core-binding factor alpha A subunit;
                     osteoblast-specific transcription factor 2; PEA2-alpha A;
                     PEBP2-alpha A; oncogene AML-3; polyomavirus
                     enhancer-binding protein 2 alpha A subunit"
                     /calculated_mol_wt=54923
     Region          88..216
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <252..467
                     /region_name="Herpes_BLLF1"
                     /note="Herpes virus major outer envelope glycoprotein
                     (BLLF1); pfam05109"
                     /db_xref="CDD:282904"
     Region          416..507
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..507
                     /gene="RUNX2"
                     /gene_synonym="AML3; CBF-alpha-1; CBFA1; CCD; CCD1; CLCD;
                     OSF-2; OSF2; PEA2aA; PEBP2aA"
                     /coded_by="NM_001369405.1:303..1826"
                     /note="isoform e is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS4913.1"
                     /db_xref="GeneID:860"
                     /db_xref="HGNC:HGNC:10472"
                     /db_xref="MIM:600211"
ORIGIN      
        1 mripvdpsts rrfsppsssl qpgkmsdvsp vvaaqqqqqq qqqqqqqqqq qqqqqqqeaa
       61 aaaaaaaaaa aaaaavprlr pphdnrtmve iiadhpaelv rtdspnflcs vlpshwrcnk
      121 tlpvafkvva lgevpdgtvv tvmagndeny saelrnasav mknqvarfnd lrfvgrsgrg
      181 ksftltitvf tnppqvatyh raikvtvdgp reprrhrqkl ddskpslfsd rlsdlgriph
      241 psmrvgvppq nprpslnsap spfnpqgqsq itdprqaqss ppwsydqsyp sylsqmtsps
      301 ihsttplsst rgtglpaitd vprrisdddt atsdfclwps tlskksqaga selgpfsdpr
      361 qfpsisslte srfsnprmhy patftytppv tsgmslgmsa tthyhtylpp pypgssqsqs
      421 gpfqtsstpy lyygtssgsy qfpmvpggdr spsrmlppct ttsngstlln pnlpnqndgv
      481 dadgshsssp tvlnssgrmd esvwrpy
//
LOCUS       NP_001303868             273 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform c [Homo sapiens].
ACCESSION   NP_001303868 XP_005260022
VERSION     NP_001303868.1
DBSOURCE    REFSEQ: accession NM_001316939.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BM019575.1 and AK000195.1.
            
            On Nov 4, 2015 this sequence version replaced XP_005260022.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (5) uses an alternate splice
            junction, contains an alternate exon, and uses a downstream AUG
            start codon compared to variant 1. The resulting isoform (c) is
            shorter at the N-terminus compared to isoform a. Variants 3, 4, 5,
            6, 7, and 8 all encode the same isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.492920.1,
                                           SRR1163658.515837.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151741, SAMEA2153031
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..273
                     /product="F-box/LRR-repeat protein 12 isoform c"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=30360
     Region          51..72
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          68..>173
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          100..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <114..238
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          125..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          151..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          231..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..273
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_001316939.2:444..1265"
                     /note="isoform c is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS82287.1"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 mrpkvmwhll rrymasrlhs lrmggylfsg sqapqlspal lralgqkcpn lkrlclhvad
       61 lsmvpitslp stlrtlelhs ceismawlhk qqdptvlpll ecivldrvpa frdehlqglt
      121 rfralrslvl ggtyrvtetg ldaglqelsy lqrlevlgct lsadstllai srhlrdvrki
      181 rltvrglsap glavlegmpa leslclqgpl vtpempspte ilsscltmpk lrvlelqglg
      241 wegqeaekil ckglphcmvi vracpkesmd wwm
//
LOCUS       NP_001354568             632 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform j [Homo sapiens].
ACCESSION   NP_001354568
VERSION     NP_001354568.1
DBSOURCE    REFSEQ: accession NM_001367639.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 632)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 632)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 632)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 632)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 632)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 632)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 632)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 632)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 632)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.247307.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155550 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..632
                     /product="SUN domain-containing protein 1 isoform j"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=70751
     Region          <1..139
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          264..317
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(264,267..268,271,274..275,278..279,281..282,
                     285..286,288..289,292..293,295..296,299,302..303,306,
                     309..310,313..314,316..317)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          276..>409
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          394..452
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          495..630
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..632
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367639.1:333..2231"
                     /note="isoform j is encoded by transcript variant 10"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mlserkdvlt ahpaapgpvs rvysrdrnqk cddckgkrhl dahtaahsqs prlpgragtl
       61 whiwacagyf llqilrriga vgqavsrtaw salwlavvap gkaasgvfww lgigwyqfvt
      121 liswlnvfll trclrnickf lvlliplfll lglslrgqgn ffsflpvlnw asmhrtqrvd
      181 dpqdvfkptt srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl relttllqkl
      241 qarvdqmegg aagpsasvrd avgqppretd fmafhqehev rmshledilg klrekseaiq
      301 keleqtkqkt isavgeqllp tvehlqleld qlkselsswr hvktgcetvd avqervdvqv
      361 remvkllfse dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt hhvsvtkqlp
      421 tseavvsavs eagasgitea qaraivnsal klysqdktgm vdfalesggg silstrcset
      481 yetktalmsl fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls mmihpaaftl
      541 ehipktlspt gnissapkdf avygleneyq eegqllgqft ydqdgeslqm fqalkrpddt
      601 afqivelrif snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_001229780             359 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase RNF146 isoform b [Homo sapiens].
ACCESSION   NP_001229780
VERSION     NP_001229780.1
DBSOURCE    REFSEQ: accession NM_001242851.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Li,W., Han,Q., Zhu,Y., Zhou,Y., Zhang,J., Wu,W., Li,Y., Liu,L.,
            Qiu,Y., Hu,K. and Yin,D.
  TITLE     SUMOylation of RNF146 results in Axin degradation and activation of
            Wnt/beta-catenin signaling to promote the progression of
            hepatocellular carcinoma
  JOURNAL   Oncogene 42 (21), 1728-1740 (2023)
   PUBMED   37029301
  REMARK    GeneRIF: SUMOylation of RNF146 results in Axin degradation and
            activation of Wnt/beta-catenin signaling to promote the progression
            of hepatocellular carcinoma.
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 359)
  AUTHORS   Xu,Y.R., Shi,M.L., Zhang,Y., Kong,N., Wang,C., Xiao,Y.F., Du,S.S.,
            Zhu,Q.Y. and Lei,C.Q.
  TITLE     Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation
  JOURNAL   Proc Natl Acad Sci U S A 119 (26), e2122805119 (2022)
   PUBMED   35733260
  REMARK    GeneRIF: Tankyrases inhibit innate antiviral response by PARylating
            VISA/MAVS and priming it for RNF146-mediated ubiquitination and
            degradation.
REFERENCE   5  (residues 1 to 359)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 359)
  AUTHORS   Zhang,Y., Liu,S., Mickanin,C., Feng,Y., Charlat,O., Michaud,G.A.,
            Schirle,M., Shi,X., Hild,M., Bauer,A., Myer,V.E., Finan,P.M.,
            Porter,J.A., Huang,S.M. and Cong,F.
  TITLE     RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin
            degradation and Wnt signalling
  JOURNAL   Nat Cell Biol 13 (5), 623-629 (2011)
   PUBMED   21478859
REFERENCE   7  (residues 1 to 359)
  AUTHORS   Menachem,T.D., Laitman,Y., Kaufman,B. and Friedman,E.
  TITLE     The RNF146 and ECHDC1 genes as candidates for inherited breast and
            ovarian cancer in Jewish Ashkenazi women
  JOURNAL   Fam Cancer 8 (4), 399-402 (2009)
   PUBMED   19517271
  REMARK    GeneRIF: Mutations in the coding regions of the RNF146 and ECHDC1
            genes do not contribute to the burden of inherited predisposition
            of breast cancer in Ashkenazi high risk women.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 359)
  AUTHORS   Gold,B., Kirchhoff,T., Stefanov,S., Lautenberger,J., Viale,A.,
            Garber,J., Friedman,E., Narod,S., Olshen,A.B., Gregersen,P.,
            Kosarin,K., Olsh,A., Bergeron,J., Ellis,N.A., Klein,R.J.,
            Clark,A.G., Norton,L., Dean,M., Boyd,J. and Offit,K.
  TITLE     Genome-wide association study provides evidence for a breast cancer
            risk locus at 6q22.33
  JOURNAL   Proc Natl Acad Sci U S A 105 (11), 4340-4345 (2008)
   PUBMED   18326623
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   9  (residues 1 to 359)
  AUTHORS   von Rotz,R.C., Kins,S., Hipfel,R., von der Kammer,H. and
            Nitsch,R.M.
  TITLE     The novel cytosolic RING finger protein dactylidin is up-regulated
            in brains of patients with Alzheimer's disease
  JOURNAL   Eur J Neurosci 21 (5), 1289-1298 (2005)
   PUBMED   15813938
  REMARK    GeneRIF: Dactylidin may function early in the progression of
            Alzheimer's disease.
REFERENCE   10 (residues 1 to 359)
  AUTHORS   Mungall,A.J., Palmer,S.A., Sims,S.K., Edwards,C.A., Ashurst,J.L.,
            Wilming,L., Jones,M.C., Horton,R., Hunt,S.E., Scott,C.E.,
            Gilbert,J.G., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            Babbage,A.K., Bagguley,C.L., Bailey,J., Banerjee,R., Barker,D.J.,
            Barlow,K.F., Bates,K., Beare,D.M., Beasley,H., Beasley,O.,
            Bird,C.P., Blakey,S., Bray-Allen,S., Brook,J., Brown,A.J.,
            Brown,J.Y., Burford,D.C., Burrill,W., Burton,J., Carder,C.,
            Carter,N.P., Chapman,J.C., Clark,S.Y., Clark,G., Clee,C.M.,
            Clegg,S., Cobley,V., Collier,R.E., Collins,J.E., Colman,L.K.,
            Corby,N.R., Coville,G.J., Culley,K.M., Dhami,P., Davies,J.,
            Dunn,M., Earthrowl,M.E., Ellington,A.E., Evans,K.A., Faulkner,L.,
            Francis,M.D., Frankish,A., Frankland,J., French,L., Garner,P.,
            Garnett,J., Ghori,M.J., Gilby,L.M., Gillson,C.J., Glithero,R.J.,
            Grafham,D.V., Grant,M., Gribble,S., Griffiths,C., Griffiths,M.,
            Hall,R., Halls,K.S., Hammond,S., Harley,J.L., Hart,E.A.,
            Heath,P.D., Heathcott,R., Holmes,S.J., Howden,P.J., Howe,K.L.,
            Howell,G.R., Huckle,E., Humphray,S.J., Humphries,M.D., Hunt,A.R.,
            Johnson,C.M., Joy,A.A., Kay,M., Keenan,S.J., Kimberley,A.M.,
            King,A., Laird,G.K., Langford,C., Lawlor,S., Leongamornlert,D.A.,
            Leversha,M., Lloyd,C.R., Lloyd,D.M., Loveland,J.E., Lovell,J.,
            Martin,S., Mashreghi-Mohammadi,M., Maslen,G.L., Matthews,L.,
            McCann,O.T., McLaren,S.J., McLay,K., McMurray,A., Moore,M.J.,
            Mullikin,J.C., Niblett,D., Nickerson,T., Novik,K.L., Oliver,K.,
            Overton-Larty,E.K., Parker,A., Patel,R., Pearce,A.V., Peck,A.I.,
            Phillimore,B., Phillips,S., Plumb,R.W., Porter,K.M., Ramsey,Y.,
            Ranby,S.A., Rice,C.M., Ross,M.T., Searle,S.M., Sehra,H.K.,
            Sheridan,E., Skuce,C.D., Smith,S., Smith,M., Spraggon,L.,
            Squares,S.L., Steward,C.A., Sycamore,N., Tamlyn-Hall,G., Tester,J.,
            Theaker,A.J., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.,
            Tubby,B., Wall,M., Wallis,J.M., West,A.P., White,S.S.,
            Whitehead,S.L., Whittaker,H., Wild,A., Willey,D.J., Wilmer,T.E.,
            Wood,J.M., Wray,P.W., Wyatt,J.C., Young,L., Younger,R.M.,
            Bentley,D.R., Coulson,A., Durbin,R., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI771613.1, BG708628.1 and AJ420549.1.
            
            Transcript Variant: This variant (10) contains an alternate 5'
            terminal exon and lacks two alternate internal exons, which results
            in the use of an upstream start codon, compared to variant 1. The
            encoded isoform (b) has a longer N-terminus than isoform a.
            Variants 8-10 encode the same isoform (b).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI771613.1, ERR3218375.662966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2146982
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.33"
     Protein         1..359
                     /product="E3 ubiquitin-protein ligase RNF146 isoform b"
                     /EC_number="2.3.2.27"
                     /note="dactylidin; RING-type E3 ubiquitin transferase
                     RNF146; E3 ubiquitin-protein ligase RNF146; iduna"
                     /calculated_mol_wt=38819
     Region          35..84
                     /region_name="RING-HC_RNF146"
                     /note="RING finger, HC subclass, found in RING finger
                     protein 146 (RNF146) and similar proteins; cd16546"
                     /db_xref="CDD:438208"
     Site            order(38..39,41,70,72..73)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438208"
     Region          104..176
                     /region_name="WWE"
                     /note="Domain in Deltex and TRIP12 homologues. Possibly
                     involved in regulation of ubiquitin-mediated proteolysis;
                     smart00678"
                     /db_xref="CDD:128922"
     Region          254..359
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTX7.1)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5XIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NTX7.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q5XIK5; propagated from
                     UniProtKB/Swiss-Prot (Q9NTX7.1)"
     CDS             1..359
                     /gene="RNF146"
                     /coded_by="NM_001242851.1:137..1216"
                     /note="isoform b is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS56449.1"
                     /db_xref="GeneID:81847"
                     /db_xref="HGNC:HGNC:21336"
                     /db_xref="MIM:612137"
ORIGIN      
        1 mmagcgeidh sinmlptnrk anescsntap sltvpecaic lqtcvhpvsl pckhvfcylc
       61 vkgaswlgkr calcrqeipe dfldkptlls peelkaasrg ngeyawyyeg rngwwqyder
      121 tsreledafs kgkkntemli agflyvadle nmvqyrrneh grrrkikrdi idipkkgvag
      181 lrldcdantv nlaressadg adsvsaqsga svqplvssvr pltsvdgqlt spatpspdas
      241 tsledsfahl qlsgdntaer shrgegeedh espssgrvpa pdtsieetes dassdsedvs
      301 avvaqhsltq qrllvsnanq tvpdrsdrsg tdrsvagggt vsvsvrsrrp dgqctvtev
//
LOCUS       NP_996318                435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_996318
VERSION     NP_996318.1
DBSOURCE    REFSEQ: accession NM_206595.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK291028.1, AB020639.1 and
            BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (3) lacks the 5' exon but has two
            alternate 5' exons and uses a downstream AUG start codon, compared
            to variant 1. The resulting isoform (2) is shorter at the
            N-terminus, compared to isoform 1. Variants 2-4, 9-15, and 17-21
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.92746.1,
                                           SRR1803614.233037.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_206595.3:218..1525"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_077324                176 aa            linear   PRI 20-NOV-2025
DEFINITION  dynactin subunit 3 isoform 2 [Homo sapiens].
ACCESSION   NP_077324
VERSION     NP_077324.1
DBSOURCE    REFSEQ: accession NM_024348.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 176)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 176)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 176)
  AUTHORS   Su,X., Li,H., Chen,S. and Qin,C.
  TITLE     Study on the Prognostic Values of Dynactin Genes in Low-Grade
            Glioma
  JOURNAL   Technol Cancer Res Treat 20, 15330338211010143 (2021)
   PUBMED   33896271
  REMARK    GeneRIF: Study on the Prognostic Values of Dynactin Genes in
            Low-Grade Glioma.
REFERENCE   4  (residues 1 to 176)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 176)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 176)
  AUTHORS   Gupta,G.D., Coyaud,E., Goncalves,J., Mojarad,B.A., Liu,Y., Wu,Q.,
            Gheiratmand,L., Comartin,D., Tkach,J.M., Cheung,S.W., Bashkurov,M.,
            Hasegan,M., Knight,J.D., Lin,Z.Y., Schueler,M., Hildebrandt,F.,
            Moffat,J., Gingras,A.C., Raught,B. and Pelletier,L.
  TITLE     A Dynamic Protein Interaction Landscape of the Human
            Centrosome-Cilium Interface
  JOURNAL   Cell 163 (6), 1484-1499 (2015)
   PUBMED   26638075
REFERENCE   7  (residues 1 to 176)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 176)
  AUTHORS   Mills,D.R. and Jackson,C.L.
  TITLE     Assignment of p22 dynactin light chain (DCTN3) to human chromosome
            region 9p13 by radiation hybrid mapping
  JOURNAL   Cytogenet Cell Genet 92 (1-2), 166 (2001)
   PUBMED   11306820
REFERENCE   9  (residues 1 to 176)
  AUTHORS   Karki,S., Tokito,M.K. and Holzbaur,E.L.
  TITLE     A dynactin subunit with a highly conserved cysteine-rich motif
            interacts directly with Arp1
  JOURNAL   J Biol Chem 275 (7), 4834-4839 (2000)
   PUBMED   10671518
REFERENCE   10 (residues 1 to 176)
  AUTHORS   Karki,S., LaMonte,B. and Holzbaur,E.L.
  TITLE     Characterization of the p22 subunit of dynactin reveals the
            localization of cytoplasmic dynein and dynactin to the midbody of
            dividing cells
  JOURNAL   J Cell Biol 142 (4), 1023-1034 (1998)
   PUBMED   9722614
  REMARK    Erratum:[J Cell Biol 1998 Oct 19;143(2):following 560]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA212054.1, BC000319.2 and
            CN257020.1.
            
            Summary: This gene encodes the smallest subunit of dynactin, a
            macromolecular complex consisting of 10 subunits ranging in size
            from 22 to 150 kD. Dynactin binds to both microtubules and
            cytoplasmic dynein. It is involved in a diverse array of cellular
            functions, including ER-to-Golgi transport, the centripetal
            movement of lysosomes and endosomes, spindle formation,
            cytokinesis, chromosome movement, nuclear positioning, and
            axonogenesis. This subunit, like most other dynactin subunits,
            exists only as a part of the dynactin complex. It is primarily an
            alpha-helical protein with very little coiled coil, and binds
            directly to the largest subunit (p150) of dynactin. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region, which results in a translational
            frameshift, compared to variant 1. The encoded isoform (2) has a
            shorter and distinct C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.308100.1, BC000319.2
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p13.3"
     Protein         1..176
                     /product="dynactin subunit 3 isoform 2"
                     /note="dynactin light chain; dynactin complex subunit 22
                     kDa subunit; dynactin 3 (p22)"
                     /calculated_mol_wt=19337
     Region          10..155
                     /region_name="Dynactin_p22"
                     /note="Dynactin subunit p22; pfam07426"
                     /db_xref="CDD:462162"
     CDS             1..176
                     /gene="DCTN3"
                     /gene_synonym="DCTN-22; DCTN22"
                     /coded_by="NM_024348.4:32..562"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS6561.1"
                     /db_xref="GeneID:11258"
                     /db_xref="HGNC:HGNC:2713"
                     /db_xref="MIM:607387"
ORIGIN      
        1 magltdlqrl qarveelerw vygpggargs rkvadglvkv qvalgnissk rervkilykk
       61 iedlikyldp eyidriaipd asklqfilae eqfilsqval leqvnalvpm ldsahikavp
      121 ehaarlqrla qihiqqqapw gvgvrdeags lvedvgfaqf lsvlhfgptg pvcgnh
//
LOCUS       NP_001340184             324 aa            linear   PRI 20-NOV-2025
DEFINITION  CYFIP-related Rac1 interactor B isoform 1 [Homo sapiens].
ACCESSION   NP_001340184 XP_016869033
VERSION     NP_001340184.1
DBSOURCE    REFSEQ: accession NM_001353255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 324)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 324)
  AUTHORS   Nikolaou,S., Juin,A., Whitelaw,J.A., Paul,N.R., Fort,L., Nixon,C.,
            Spence,H.J., Bryson,S. and Machesky,L.M.
  TITLE     CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake
  JOURNAL   Elife 13, e83712 (2024)
   PUBMED   38712822
  REMARK    GeneRIF: CYRI-B-mediated macropinocytosis drives metastasis via
            lysophosphatidic acid receptor uptake.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 324)
  AUTHORS   Huang,H., Tsui,Y.M., Ho,D.W., Chung,C.Y., Sze,K.M., Lee,E.,
            Cheung,G.C., Zhang,V.X., Wang,X., Lyu,X. and Ng,I.O.
  TITLE     LANCL1, a cell surface protein, promotes liver tumor initiation
            through FAM49B-Rac1 axis to suppress oxidative stress
  JOURNAL   Hepatology 79 (2), 323-340 (2024)
   PUBMED   37540188
  REMARK    GeneRIF: LANCL1, a cell surface protein, promotes liver tumor
            initiation through FAM49B-Rac1 axis to suppress oxidative stress.
REFERENCE   4  (residues 1 to 324)
  AUTHORS   Kuiper,J.W.P., Krause,J., Potgeter,L., Adrian,J. and Hauck,C.R.
  TITLE     A genome-wide genetic screen identifies CYRI-B as a negative
            regulator of CEACAM3-mediated phagocytosis
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37264948
  REMARK    GeneRIF: A genome-wide genetic screen identifies CYRI-B as a
            negative regulator of CEACAM3-mediated phagocytosis.
REFERENCE   5  (residues 1 to 324)
  AUTHORS   Xi,Y., Zhang,T., Sun,W., Liang,R., Ganesh,S. and Chen,H.
  TITLE     GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis
  JOURNAL   Int J Mol Sci 23 (23), 15433 (2022)
   PUBMED   36499755
  REMARK    GeneRIF: GOLM1 and FAM49B: Potential Biomarkers in HNSCC Based on
            Bioinformatics and Immunohistochemical Analysis.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 324)
  AUTHORS   Nalls,M.A., Couper,D.J., Tanaka,T., van Rooij,F.J., Chen,M.H.,
            Smith,A.V., Toniolo,D., Zakai,N.A., Yang,Q., Greinacher,A.,
            Wood,A.R., Garcia,M., Gasparini,P., Liu,Y., Lumley,T., Folsom,A.R.,
            Reiner,A.P., Gieger,C., Lagou,V., Felix,J.F., Volzke,H.,
            Gouskova,N.A., Biffi,A., Doring,A., Volker,U., Chong,S.,
            Wiggins,K.L., Rendon,A., Dehghan,A., Moore,M., Taylor,K.,
            Wilson,J.G., Lettre,G., Hofman,A., Bis,J.C., Pirastu,N., Fox,C.S.,
            Meisinger,C., Sambrook,J., Arepalli,S., Nauck,M., Prokisch,H.,
            Stephens,J., Glazer,N.L., Cupples,L.A., Okada,Y., Takahashi,A.,
            Kamatani,Y., Matsuda,K., Tsunoda,T., Tanaka,T., Kubo,M.,
            Nakamura,Y., Yamamoto,K., Kamatani,N., Stumvoll,M., Tonjes,A.,
            Prokopenko,I., Illig,T., Patel,K.V., Garner,S.F., Kuhnel,B.,
            Mangino,M., Oostra,B.A., Thein,S.L., Coresh,J., Wichmann,H.E.,
            Menzel,S., Lin,J., Pistis,G., Uitterlinden,A.G., Spector,T.D.,
            Teumer,A., Eiriksdottir,G., Gudnason,V., Bandinelli,S.,
            Frayling,T.M., Chakravarti,A., van Duijn,C.M., Melzer,D.,
            Ouwehand,W.H., Levy,D., Boerwinkle,E., Singleton,A.B.,
            Hernandez,D.G., Longo,D.L., Soranzo,N., Witteman,J.C., Psaty,B.M.,
            Ferrucci,L., Harris,T.B., O'Donnell,C.J. and Ganesh,S.K.
  TITLE     Multiple loci are associated with white blood cell phenotypes
  JOURNAL   PLoS Genet 7 (6), e1002113 (2011)
   PUBMED   21738480
REFERENCE   7  (residues 1 to 324)
  AUTHORS   Buschow,S.I., van Balkom,B.W., Aalberts,M., Heck,A.J., Wauben,M.
            and Stoorvogel,W.
  TITLE     MHC class II-associated proteins in B-cell exosomes and potential
            functional implications for exosome biogenesis
  JOURNAL   Immunol Cell Biol 88 (8), 851-856 (2010)
   PUBMED   20458337
REFERENCE   8  (residues 1 to 324)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 324)
  AUTHORS   Melzer,D., Perry,J.R., Hernandez,D., Corsi,A.M., Stevens,K.,
            Rafferty,I., Lauretani,F., Murray,A., Gibbs,J.R., Paolisso,G.,
            Rafiq,S., Simon-Sanchez,J., Lango,H., Scholz,S., Weedon,M.N.,
            Arepalli,S., Rice,N., Washecka,N., Hurst,A., Britton,A., Henley,W.,
            van de Leemput,J., Li,R., Newman,A.B., Tranah,G., Harris,T.,
            Panicker,V., Dayan,C., Bennett,A., McCarthy,M.I., Ruokonen,A.,
            Jarvelin,M.R., Guralnik,J., Bandinelli,S., Frayling,T.M.,
            Singleton,A. and Ferrucci,L.
  TITLE     A genome-wide association study identifies protein quantitative
            trait loci (pQTLs)
  JOURNAL   PLoS Genet 4 (5), e1000072 (2008)
   PUBMED   18464913
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 324)
  AUTHORS   Petroziello,J., Yamane,A., Westendorf,L., Thompson,M., McDonagh,C.,
            Cerveny,C., Law,C.L., Wahl,A. and Carter,P.
  TITLE     Suppression subtractive hybridization and expression profiling
            identifies a unique set of genes overexpressed in non-small-cell
            lung cancer
  JOURNAL   Oncogene 23 (46), 7734-7745 (2004)
   PUBMED   15334068
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC131568.5 and AC022973.5.
            
            On Jul 1, 2017 this sequence version replaced XP_016869033.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1803616.345540.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..324
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.21"
     Protein         1..324
                     /product="CYFIP-related Rac1 interactor B isoform 1"
                     /note="protein FAM49B; FAM49B/JPH1 fusion; MTSS1/FAM49B
                     fusion; family with sequence similarity 49 member B"
                     /calculated_mol_wt=36617
     Region          18..320
                     /region_name="CYRIA-B_Rac1-bd"
                     /note="CYRIA/CYRIB Rac1 binding domain; pfam07159"
                     /db_xref="CDD:462106"
     CDS             1..324
                     /gene="CYRIB"
                     /gene_synonym="BM-009; CYRI; CYRI-B; FAM49B; L1"
                     /coded_by="NM_001353255.1:387..1361"
                     /note="isoform 1 is encoded by transcript variant 17"
                     /db_xref="CCDS:CCDS6361.1"
                     /db_xref="GeneID:51571"
                     /db_xref="HGNC:HGNC:25216"
                     /db_xref="MIM:617978"
ORIGIN      
        1 mgnllkvltc tdleqgpnff ldfenaqpte sekeiynqvn vvlkdaegil edlqsyrgag
       61 heireaiqhp adeklqekaw gavvplvgkl kkfyefsqrl eaalrgllga ltstpysptq
      121 hlereqalak qfaeilhftl rfdelkmtnp aiqndfsyyr rtlsrmrinn vpaegenevn
      181 nelanrmslf yaeatpmlkt lsdattkfvs enknlpient tdclstmasv crvmletpey
      241 rsrftneetv sfclrvmvgv iilydhvhpv gafaktskid mkgcikvlkd qppnsvegll
      301 nalryttkhl ndettskqik smlq
//
LOCUS       NP_001308717             982 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform b [Homo sapiens].
ACCESSION   NP_001308717 XP_005247910
VERSION     NP_001308717.1
DBSOURCE    REFSEQ: accession NM_001321788.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 982)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 982)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 982)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 982)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 982)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 982)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 982)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 982)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 982)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 982)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            On Mar 31, 2016 this sequence version replaced XP_005247910.1.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Variants 2 and 3 encode the same isoform (b).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.106942.1,
                                           SRR18074969.1537377.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..982
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..982
                     /product="E3 ubiquitin-protein ligase CBL-B isoform b"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=109319
     Region          35..167
                     /region_name="4H"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Region          41..167
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          168..240
                     /region_name="EF-hand-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Region          171..254
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          241..343
                     /region_name="SH2-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Region          248..344
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(266,286,288..291,296,308,310)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC/PRKCQ.
                     /evidence=ECO:0000269|PubMed:19549985; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            order(311..314,327..329)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          344..372
                     /region_name="Linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Region          351..426
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(362..363,366,390,409..412)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            363
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000305|PubMed:20525694; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            order(366..368,374..377,396,399..400,403,409..410,412)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          466..571
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Site            476
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K4S7; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            521
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            529
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Region          543..568
                     /region_name="Interaction with VAV1.
                     /evidence=ECO:0000269|PubMed:9399639"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K4S7; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Site            665
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10022120; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Region          688..731
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Site            709
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:10022120; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Region          769..929
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Site            889
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q3TTA7; propagated from
                     UniProtKB/Swiss-Prot (Q13191.2)"
     Region          891..927
                     /region_name="Interaction with SH3KBP1.
                     /evidence=ECO:0000269|PubMed:12177062"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13191.2)"
     Region          931..971
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(933..934,936..938,940..941,946,950)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..982
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321788.2:116..3064"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS2948.1"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr rnltklslif shmlaeikai fpngqfqgdn fritkadaae
      181 fwrkffgdkt ivpwkvfrqc lhevhqissg leamalksti dltcndyisv fefdiftrlf
      241 qpwgsilrnw nflavthpgy mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv
      301 tgdgnilqti phnkplfqal idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy
      361 elycemgstf qlckicaend kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep
      421 iivdpfdprd egsrccsiid pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts
      481 pgssplaqrr kpqpdplqip hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq
      541 dkplpapppp lrdppppppe rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg
      601 tnqlvgcrll gegspkpgit assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl
      661 gseeydvppr lsppppvttl lpsikctgpl anslsektrd pveedddeyk ipsshpvsln
      721 sqpshchnvk ppvrscdngh cmlngthgps sekksnipdl siylkgdvfd sasdpvplpp
      781 arpptrdnpk hgsslnrtps dydllipplg edafdalpps lpppppparh sliehskppg
      841 sssrpssgqd lfllpsdpfv dlasgqvplp parrlpgenv ktnrtsqdyd qlpscsdgsq
      901 aparppkprp rrtapeihhr kphgpeaale nvdakiaklm gegyafeevk raleiaqnnv
      961 evarsilref afpppvsprl nl
//
LOCUS       NP_068747                180 aa            linear   PRI 20-NOV-2025
DEFINITION  signal peptidase complex subunit 3 [Homo sapiens].
ACCESSION   NP_068747
VERSION     NP_068747.1
DBSOURCE    REFSEQ: accession NM_021928.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Liaci,A.M., Steigenberger,B., Telles de Souza,P.C., Tamara,S.,
            Grollers-Mulderij,M., Ogrissek,P., Marrink,S.J., Scheltema,R.A. and
            Forster,F.
  TITLE     Structure of the human signal peptidase complex reveals the
            determinants for signal peptide cleavage
  JOURNAL   Mol Cell 81 (19), 3934-3948 (2021)
   PUBMED   34388369
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Hosp,F., Vossfeldt,H., Heinig,M., Vasiljevic,D., Arumughan,A.,
            Wyler,E., Landthaler,M., Hubner,N., Wanker,E.E., Lannfelt,L.,
            Ingelsson,M., Lalowski,M., Voigt,A. and Selbach,M.
  CONSRTM   Genetic and Environmental Risk for Alzheimer's Disease GERAD1
            Consortium
  TITLE     Quantitative interaction proteomics of neurodegenerative disease
            proteins
  JOURNAL   Cell Rep 11 (7), 1134-1146 (2015)
   PUBMED   25959826
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Argente,J., Flores,R., Gutierrez-Arumi,A., Verma,B.,
            Martos-Moreno,G.A., Cusco,I., Oghabian,A., Chowen,J.A.,
            Frilander,M.J. and Perez-Jurado,L.A.
  TITLE     Defective minor spliceosome mRNA processing results in isolated
            familial growth hormone deficiency
  JOURNAL   EMBO Mol Med 6 (3), 299-306 (2014)
   PUBMED   24480542
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Kalies,K.U. and Hartmann,E.
  TITLE     Membrane topology of the 12- and the 25-kDa subunits of the
            mammalian signal peptidase complex
  JOURNAL   J Biol Chem 271 (7), 3925-3929 (1996)
   PUBMED   8632014
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK026302.1 and AC019163.8.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.97109.1,
                                           SRR1660807.2266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000503362.2/ ENSP00000427463.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q34.2"
     Protein         1..180
                     /product="signal peptidase complex subunit 3"
                     /note="SPase 22 kDa subunit; microsomal signal peptidase
                     23 kDa subunit; SPase 22/23 kDa subunit; microsomal signal
                     peptidase 22/23 kDa subunit; signal peptidase complex
                     subunit 3 homolog"
                     /calculated_mol_wt=20182
     Region          1..173
                     /region_name="SPC22"
                     /note="Signal peptidase subunit; pfam04573"
                     /db_xref="CDD:461357"
     Site            12..32
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P61009.1)"
     Site            141
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218,
                     ECO:0000269|PubMed:34388369; propagated from
                     UniProtKB/Swiss-Prot (P61009.1)"
     CDS             1..180
                     /gene="SPCS3"
                     /gene_synonym="PRO3567; SPC22; SPC22/23; SPC23; SPC3;
                     YLR066W"
                     /coded_by="NM_021928.4:112..654"
                     /db_xref="CCDS:CCDS54823.1"
                     /db_xref="GeneID:60559"
                     /db_xref="HGNC:HGNC:26212"
                     /db_xref="MIM:618854"
ORIGIN      
        1 mntvlsrans lfafslsvma altfgcfitt afkdrsvpvr lhvsrimlkn vedftgprer
       61 sdlgfitfdi tadlenifdw nvkqlflyls aeystknnal nqvvlwdkiv lrgdnpklll
      121 kdmktkyfff ddgnglkgnr nvtltlswnv vpnagilplv tgsghvsvpf pdtyeitksy
//
LOCUS       NP_001120822             208 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 18 [Homo
            sapiens].
ACCESSION   NP_001120822
VERSION     NP_001120822.1
DBSOURCE    REFSEQ: accession NM_001127350.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 208)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 208)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 208)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 208)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 208)
  AUTHORS   Xuan,Y. and Wang,Y.
  TITLE     Long non-coding RNA SNHG3 promotes progression of gastric cancer by
            regulating neighboring MED18 gene methylation
  JOURNAL   Cell Death Dis 10 (10), 694 (2019)
   PUBMED   31534128
  REMARK    GeneRIF: Long non-coding RNA SNHG3 promotes progression of gastric
            cancer by regulating neighboring MED18 gene methylation.
            Erratum:[Cell Death Dis. 2022 Mar 11;13(3):226. doi:
            10.1038/s41419-022-04698-9. PMID: 35277490]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Parmely,T.J., Florens,L., Zybailov,B.,
            Swanson,S.K., Banks,C.A., Jin,J., Cai,Y., Washburn,M.P.,
            Conaway,J.W. and Conaway,R.C.
  TITLE     A set of consensus mammalian mediator subunits identified by
            multidimensional protein identification technology
  JOURNAL   Mol Cell 14 (5), 685-691 (2004)
   PUBMED   15175163
REFERENCE   7  (residues 1 to 208)
  AUTHORS   Tomomori-Sato,C., Sato,S., Parmely,T.J., Banks,C.A., Sorokina,I.,
            Florens,L., Zybailov,B., Washburn,M.P., Brower,C.S., Conaway,R.C.
            and Conaway,J.W.
  TITLE     A mammalian mediator subunit that shares properties with
            Saccharomyces cerevisiae mediator subunit Cse2
  JOURNAL   J Biol Chem 279 (7), 5846-5851 (2004)
   PUBMED   14638676
REFERENCE   8  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Parmely,T.J., Sorokina,I.,
            Brower,C.S., Conaway,R.C. and Conaway,J.W.
  TITLE     A mammalian homolog of Drosophila melanogaster transcriptional
            coactivator intersex is a subunit of the mammalian Mediator complex
  JOURNAL   J Biol Chem 278 (50), 49671-49674 (2003)
   PUBMED   14576168
REFERENCE   9  (residues 1 to 208)
  AUTHORS   Sato,S., Tomomori-Sato,C., Banks,C.A., Sorokina,I., Parmely,T.J.,
            Kong,S.E., Jin,J., Cai,Y., Lane,W.S., Brower,C.S., Conaway,R.C. and
            Conaway,J.W.
  TITLE     Identification of mammalian Mediator subunits with similarities to
            yeast Mediator subunits Srb5, Srb6, Med11, and Rox3
  JOURNAL   J Biol Chem 278 (17), 15123-15127 (2003)
   PUBMED   12584197
REFERENCE   10 (residues 1 to 208)
  AUTHORS   Mittler,G., Kremmer,E., Timmers,H.T. and Meisterernst,M.
  TITLE     Novel critical role of a human Mediator complex for basal RNA
            polymerase II transcription
  JOURNAL   EMBO Rep 2 (9), 808-813 (2001)
   PUBMED   11559591
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG752399.1 and AL353622.33.
            
            Summary: MED18 is a component of the Mediator complex, which is a
            coactivator for DNA-binding factors that activate transcription via
            RNA polymerase II (Sato et al., 2003 [PubMed 12584197]).[supplied
            by OMIM, Oct 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 both encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.129010.1,
                                           DRR138512.679939.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..208
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..208
                     /product="mediator of RNA polymerase II transcription
                     subunit 18"
                     /note="TRAP/mediator complex subunit p28b; mediator of RNA
                     polymerase II transcription, subunit 18 homolog"
                     /calculated_mol_wt=23532
     Region          19..203
                     /region_name="Med18"
                     /note="Med18 protein; pfam09637"
                     /db_xref="CDD:462845"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BUE0.1)"
     CDS             1..208
                     /gene="MED18"
                     /gene_synonym="p28b; SRB5"
                     /coded_by="NM_001127350.2:152..778"
                     /db_xref="CCDS:CCDS322.1"
                     /db_xref="GeneID:54797"
                     /db_xref="HGNC:HGNC:25944"
                     /db_xref="MIM:612384"
ORIGIN      
        1 meappvtmmp vtggtinmme yllqgsvldh sleslihrlr glcdnmepet fldhemvfll
       61 kgqqaspfvl rarrsmdrag apwhlrylgq pemgdknrha lvrncvdiat senltdflme
      121 mgfrmdhefv akghlfrkgi mkimvykifr ilvpgntdst ealslsylve lsvvapagqd
      181 mvsddmknfa eqlkplvhle kidpkrlm
//
LOCUS       NP_001280020             763 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001280020 XP_005257952
VERSION     NP_001280020.1
DBSOURCE    REFSEQ: accession NM_001293091.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 763)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 763)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 763)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 763)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 763)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 763)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 763)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 763)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 763)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 763)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY023336.1, AK296881.1,
            AC002558.2 and AA927469.1.
            
            On May 28, 2014 this sequence version replaced XP_005257952.1.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Transcript Variant: This variant (4) lacks an alternate exon in the
            5' region and it thus differs in its 5' UTR and initiates
            translation at an alternate start codon, and it also uses an
            alternate in-frame splice site in the central coding region,
            compared to variant 1. The encoded isoform (4) has a distinct
            N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK296881.1, SRR18074969.1162834.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..763
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..763
                     /product="cell division cycle protein 27 homolog isoform
                     4"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=84758
     Region          387..>610
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          440..466
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          500..>670
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          506..534
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(507,510..511,514..515,517,541,544..545,548..549,
                     551..552,575,578..579,582..583,586)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          539..569
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          574..602
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          <604..743
                     /region_name="NlpI"
                     /note="Lipoprotein NlpI, contains TPR repeats [Cell
                     wall/membrane/envelope biogenesis]; COG4785"
                     /db_xref="CDD:443815"
     Region          608..635
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          642..670
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          676..704
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..763
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001293091.3:159..2450"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mastkplclp rcgfprrtpl crrlaegeqi lsggvfnkqk shddivtefg dsacftlsll
       61 ghvycktdrl akgsecyqks lslnpflwsp feslceigek pdpdqtfkft slqnfsnclp
      121 nscttqvpnh slshrqpetv ltetpqdtie lnrlnlessn skyslntdss vsyidsavis
      181 pdtvplgtgt silskqvqnk pktgrsllgg paalspltps fgilpletps pgdgsylqny
      241 tntppvidvp stgapskksv arigqtgtks vfsqsgnsre vtpilaqtqs sgpqtsttpq
      301 vlsptitspp nalprrssrl ftsdssttke nskklkmkfp pkipnrktks ktnkggitqp
      361 nindsleitk ldssiisegk istitpqiqa fnlqkaaaeg lmsllremgk gylalcsync
      421 keainilshl pshhyntgwv lcqigrayfe lseymqaeri fsevrrieny rvegmeiyst
      481 tlwhlqkdva lsvlskdltd mdknspeawc aagncfslqr ehdiaikffq raiqvdpnya
      541 yaytllghef vlteeldkal acfrnairvn prhynawygl gmiyykqekf slaemhfqka
      601 ldinpqssvl lchigvvqha lkksekaldt lnkaividpk nplckfhras vlfanekyks
      661 alqeleelkq ivpkeslvyf ligkvykklg qthlalmnfs wamdldpkga nnqikeaidk
      721 rylpddeepi tqeeqimgtd esqessmtda ddtqlhaaes def
//
LOCUS       NP_001241680             592 aa            linear   PRI 20-NOV-2025
DEFINITION  T-cell differentiation antigen CD6 isoform 3 precursor [Homo
            sapiens].
ACCESSION   NP_001241680
VERSION     NP_001241680.1
DBSOURCE    REFSEQ: accession NM_001254751.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 592)
  AUTHORS   Do,J.S., Arribas-Layton,D., Juan,J., Garcia,I., Saraswathy,S.,
            Qi,M., Montero,E. and Reijonen,H.
  TITLE     The CD318/CD6 axis limits type 1 diabetes islet
            autoantigen-specific human T cell activation
  JOURNAL   J Autoimmun 146, 103228 (2024)
   PUBMED   38642507
  REMARK    GeneRIF: The CD318/CD6 axis limits type 1 diabetes islet
            autoantigen-specific human T cell activation.
REFERENCE   2  (residues 1 to 592)
  AUTHORS   Wagner,M., Sobczynski,M., Wisniewski,A., Matusiak,L.,
            Kusnierczyk,P. and Jasek,M.
  TITLE     Polymorphisms in the CD6-ALCAM axis may modulate psoriasis risk and
            outcomes
  JOURNAL   Hum Immunol 85 (3), 110797 (2024)
   PUBMED   38580538
  REMARK    GeneRIF: Polymorphisms in the CD6-ALCAM axis may modulate psoriasis
            risk and outcomes.
REFERENCE   3  (residues 1 to 592)
  AUTHORS   Gurrea-Rubio,M., Wu,Q., Amin,M.A., Tsou,P.S., Campbell,P.L.,
            Amarista,C.I., Ikari,Y., Brodie,W.D., Mattichak,M.N., Muraoka,S.,
            Randon,P.M., Lind,M.E., Ruth,J.H., Mao-Draayer,Y., Ding,S.,
            Shen,X., Cooney,L.A., Lin,F. and Fox,D.A.
  TITLE     Activation of cytotoxic lymphocytes through CD6 enhances killing of
            cancer cells
  JOURNAL   Cancer Immunol Immunother 73 (2), 34 (2024)
   PUBMED   38280067
  REMARK    GeneRIF: Activation of cytotoxic lymphocytes through CD6 enhances
            killing of cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 592)
  AUTHORS   Aragon-Serrano,L., Carrillo-Serradell,L., Planells-Romeo,V.,
            Isamat,M., Velasco-de Andres,M. and Lozano,F.
  TITLE     CD6 and Its Interacting Partners: Newcomers to the Block of Cancer
            Immunotherapies
  JOURNAL   Int J Mol Sci 24 (24), 17510 (2023)
   PUBMED   38139340
  REMARK    GeneRIF: CD6 and Its Interacting Partners: Newcomers to the Block
            of Cancer Immunotherapies.
            Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 592)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   6  (residues 1 to 592)
  AUTHORS   Robinson,W.H., Neuman de Vegvar,H.E., Prohaska,S.S., Rhee,J.W. and
            Parnes,J.R.
  TITLE     Human CD6 possesses a large, alternatively spliced cytoplasmic
            domain
  JOURNAL   Eur J Immunol 25 (10), 2765-2769 (1995)
   PUBMED   7589069
REFERENCE   7  (residues 1 to 592)
  AUTHORS   Whitney,G.S., Starling,G.C., Bowen,M.A., Modrell,B., Siadak,A.W.
            and Aruffo,A.
  TITLE     The membrane-proximal scavenger receptor cysteine-rich domain of
            CD6 contains the activated leukocyte cell adhesion molecule binding
            site
  JOURNAL   J Biol Chem 270 (31), 18187-18190 (1995)
   PUBMED   7543097
REFERENCE   8  (residues 1 to 592)
  AUTHORS   Aruffo,A., Melnick,M.B., Linsley,P.S. and Seed,B.
  TITLE     The lymphocyte glycoprotein CD6 contains a repeated domain
            structure characteristic of a new family of cell surface and
            secreted proteins
  JOURNAL   J Exp Med 174 (4), 949-952 (1991)
   PUBMED   1919444
REFERENCE   9  (residues 1 to 592)
  AUTHORS   Swack,J.A., Mier,J.W., Romain,P.L., Hull,S.R. and Rudd,C.E.
  TITLE     Biosynthesis and post-translational modification of CD6, a T cell
            signal-transducing molecule
  JOURNAL   J Biol Chem 266 (11), 7137-7143 (1991)
   PUBMED   2016320
REFERENCE   10 (residues 1 to 592)
  AUTHORS   Tsuge,I., Utsumi,K.R., Ueda,R., Takamoto,S. and Takahashi,T.
  TITLE     Assignment of gene coding human T-cell differentiation antigen,
            Tp120, to chromosome 11
  JOURNAL   Somat Cell Mol Genet 11 (3), 217-222 (1985)
   PUBMED   3923629
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AP003721.3, U66146.1 and AI657093.1.
            
            Summary: This gene encodes a protein found on the outer membrane of
            T-lymphocytes as well as some other immune cells. The encoded
            protein contains three scavenger receptor cysteine-rich (SRCR)
            domains and a binding site for an activated leukocyte cell adhesion
            molecule. The gene product is important for continuation of T cell
            activation. This gene may be associated with susceptibility to
            multiple sclerosis (PMID: 19525953, 21849685). Multiple transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2011].
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 3' coding region compared to variant 1. The resulting
            protein (isoform 3) is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U66146.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..592
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.2"
     Protein         1..592
                     /product="T-cell differentiation antigen CD6 isoform 3
                     precursor"
                     /note="CD6 antigen; T-cell differentiation antigen CD6;
                     T12"
                     /calculated_mol_wt=61772
     sig_peptide     1..17
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1798
     Region          50..156
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     Region          161..260
                     /region_name="SR"
                     /note="Scavenger receptor Cys-rich; smart00202"
                     /db_xref="CDD:214555"
     Region          270..361
                     /region_name="SRCR"
                     /note="Scavenger receptor cysteine-rich domain; pfam00530"
                     /db_xref="CDD:459844"
     CDS             1..592
                     /gene="CD6"
                     /gene_synonym="TP120"
                     /coded_by="NM_001254751.2:187..1965"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS58137.1"
                     /db_xref="GeneID:923"
                     /db_xref="HGNC:HGNC:1691"
                     /db_xref="MIM:186720"
ORIGIN      
        1 mwlffgitgl ltaalsghps pappdqlnts saeselwepg erlpvrltng ssscsgtvev
       61 rleaswepac galwdsraae avcralgcgg aeaasqlapp tpelppppaa gntsvaanat
      121 lagapallcs gaewrlcevv ehacrsdgrr arvtcaenra lrlvdgggac agrvemlehg
      181 ewgsvcddtw dledahvvcr qlgcgwavqa lpglhftpgr gpihrdqvnc sgaeaylwdc
      241 pglpgqhycg hkedagavcs ehqswrltgg adrcegqvev hfrgvwntvc dsewypseak
      301 vlcqslgcgt averpkglph slsgrmyysc ngeeltlsnc swrfnnsnlc sqslaarvlc
      361 sasrslhnls tpevpasvqt vtiessvtvk ienkesrelm llipsivlgi lllgslifia
      421 fillrikgky alpvmvnhqh lpttipagsn syqpvpitip kedsqrhrvt deevqqsrfq
      481 mppleeglee lhashiptan pghcitdpps lgpqyhprsn sesstssged ycnspksklp
      541 pwnpqvfsse rssfleqppn lelagtqpaf sgspspqpds tdnddyddis aa
//
LOCUS       NP_694881                493 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock cognate 71 kDa protein isoform 2 [Homo sapiens].
ACCESSION   NP_694881 XP_005271595
VERSION     NP_694881.1
DBSOURCE    REFSEQ: accession NM_153201.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 493)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 493)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 493)
  AUTHORS   Yang,S., Li,M., Lian,G., Wu,Y., Cui,J. and Wang,L.
  TITLE     ABHD8 antagonizes inflammation by facilitating chaperone-mediated
            autophagy-mediated degradation of NLRP3
  JOURNAL   Autophagy 21 (2), 338-351 (2025)
   PUBMED   39225180
REFERENCE   4  (residues 1 to 493)
  AUTHORS   Chaari,A., Saikia,N., Paul,P., Yousef,M., Ding,F. and Ladjimi,M.
  TITLE     Experimental and computational investigation of the effect of Hsc70
            structural variants on inhibiting amylin aggregation
  JOURNAL   Biophys Chem 309, 107235 (2024)
   PUBMED   38608617
  REMARK    GeneRIF: Experimental and computational investigation of the effect
            of Hsc70 structural variants on inhibiting amylin aggregation.
REFERENCE   5  (residues 1 to 493)
  AUTHORS   Rafiq,S., Mungure,I., Banz,Y., Niklaus,N.J., Kaufmann,T.,
            Muller,S., Jacquel,A., Robert,G., Auberger,P., Torbett,B.E.,
            Muller,S., Tschan,M.P. and Humbert,M.
  TITLE     HSPA8 Chaperone Complex Drives Chaperone-Mediated Autophagy
            Regulation in Acute Promyelocytic Leukemia Cell Differentiation
  JOURNAL   Pharmacology 109 (4), 216-230 (2024)
   PUBMED   38569476
  REMARK    GeneRIF: HSPA8 Chaperone Complex Drives Chaperone-Mediated
            Autophagy Regulation in Acute Promyelocytic Leukemia Cell
            Differentiation.
REFERENCE   6  (residues 1 to 493)
  AUTHORS   Rasmussen,H.H., van Damme,J., Puype,M., Gesser,B., Celis,J.E. and
            Vandekerckhove,J.
  TITLE     Microsequences of 145 proteins recorded in the two-dimensional gel
            protein database of normal human epidermal keratinocytes
  JOURNAL   Electrophoresis 13 (12), 960-969 (1992)
   PUBMED   1286667
REFERENCE   7  (residues 1 to 493)
  AUTHORS   Hattori,H., Liu,Y.C., Tohnai,I., Ueda,M., Kaneda,T., Kobayashi,T.,
            Tanabe,K. and Ohtsuka,K.
  TITLE     Intracellular localization and partial amino acid sequence of a
            stress-inducible 40-kDa protein in HeLa cells
  JOURNAL   Cell Struct Funct 17 (1), 77-86 (1992)
   PUBMED   1586970
REFERENCE   8  (residues 1 to 493)
  AUTHORS   DeLuca-Flaherty,C., McKay,D.B., Parham,P. and Hill,B.L.
  TITLE     Uncoating protein (hsc70) binds a conformationally labile domain of
            clathrin light chain LCa to stimulate ATP hydrolysis
  JOURNAL   Cell 62 (5), 875-887 (1990)
   PUBMED   1975516
REFERENCE   9  (residues 1 to 493)
  AUTHORS   Lim,M.Y., Davis,N., Zhang,J.Y. and Bose,H.R. Jr.
  TITLE     The v-rel oncogene product is complexed with cellular proteins
            including its proto-oncogene product and heat shock protein 70
  JOURNAL   Virology 175 (1), 149-160 (1990)
   PUBMED   2155506
REFERENCE   10 (residues 1 to 493)
  AUTHORS   Chiang,H.L., Terlecky,S.R., Plant,C.P. and Dice,J.F.
  TITLE     A role for a 70-kilodalton heat shock protein in lysosomal
            degradation of intracellular proteins
  JOURNAL   Science 246 (4928), 382-385 (1989)
   PUBMED   2799391
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC395565.1, AB034951.1,
            AK222628.1 and AP000926.6.
            
            On Aug 31, 2013 this sequence version replaced XP_005271595.1.
            
            Summary: This gene encodes a member of the heat shock protein 70
            family, which contains both heat-inducible and constitutively
            expressed members. This protein belongs to the latter group, which
            are also referred to as heat-shock cognate proteins. It functions
            as a chaperone, and binds to nascent polypeptides to facilitate
            correct folding. It also functions as an ATPase in the disassembly
            of clathrin-coated vesicles during transport of membrane components
            through the cell. Alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (2) uses alternate splice sites,
            and is missing an exon in the 3' coding region compared to variant
            1. However, it maintains the reading frame, and encodes a shorter
            isoform (2) missing an internal protein segment compared to isoform
            1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222628.1, AB034951.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..493
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q24.1"
     Protein         1..493
                     /product="heat shock cognate 71 kDa protein isoform 2"
                     /EC_number="3.6.4.10"
                     /note="heat shock 70kd protein 10; constitutive heat shock
                     protein 70; lipopolysaccharide-associated protein 1;
                     LPS-associated protein 1; heat shock cognate protein 54;
                     heat shock cognate 71 kDa protein; N-myristoyltransferase
                     inhibitor protein 71; epididymis luminal protein 33;
                     epididymis secretory sperm binding protein Li 72p; heat
                     shock 70kDa protein 8; heat shock protein family A member
                     8"
                     /calculated_mol_wt=53387
     Region          2..386
                     /region_name="Nucleotide-binding domain (NBD).
                     /evidence=ECO:0000305|PubMed:27474739"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine. /evidence=ECO:0000269|Ref.5,
                     ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330; propagated
                     from UniProtKB/Swiss-Prot (P11142.1)"
     Region          6..380
                     /region_name="ASKHA_NBD_HSP70_HSPA1"
                     /note="nucleotide-binding domain (NBD) of 70-kDa heat
                     shock protein 1 (HSPA1) and similar proteins; cd10233"
                     /db_xref="CDD:466831"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            153
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Region          186..377
                     /region_name="Interaction with BAG1"
                     /note="propagated from UniProtKB/Swiss-Prot (P11142.1)"
     Site            246
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            319
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            328
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63017; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            362
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     Site            470
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P11142.1)"
     CDS             1..493
                     /gene="HSPA8"
                     /gene_synonym="HEL-33; HEL-S-72p; HSC54; HSC70; HSC71;
                     HSP71; HSP73; HSPA10; LAP-1; LAP1; NIP71"
                     /coded_by="NM_153201.4:79..1560"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44754.1"
                     /db_xref="GeneID:3312"
                     /db_xref="HGNC:HGNC:5241"
                     /db_xref="MIM:600816"
ORIGIN      
        1 mskgpavgid lgttyscvgv fqhgkveiia ndqgnrttps yvaftdterl igdaaknqva
       61 mnptntvfda krligrrfdd avvqsdmkhw pfmvvndagr pkvqveykge tksfypeevs
      121 smvltkmkei aeaylgktvt navvtvpayf ndsqrqatkd agtiaglnvl riineptaaa
      181 iaygldkkvg aernvlifdl gggtfdvsil tiedgifevk stagdthlgg edfdnrmvnh
      241 fiaefkrkhk kdisenkrav rrlrtacera krtlssstqa sieidslyeg idfytsitra
      301 rfeelnadlf rgtldpveka lrdakldksq ihdivlvggs tripkiqkll qdffngkeln
      361 ksinpdeava ygaavqaail sgdksenvqd lllldvtpls lgietaggvm tvlikrntti
      421 ptkqtqtftt ysdnqpgvli qvyegeramt kdnnllgkfe ltgmpggmpg gfpgggapps
      481 ggassgptie evd
//
LOCUS       NP_056380               1766 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase listerin isoform 1 [Homo sapiens].
ACCESSION   NP_056380
VERSION     NP_056380.3
DBSOURCE    REFSEQ: accession NM_015565.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1766)
  AUTHORS   Qin,F., Cai,B., Wang,P., Cao,R., Zhang,Y., Wen,H., Zheng,Y.,
            Zhao,W., Gao,C. and Liu,B.
  TITLE     LTN1 promotes RLR degradation to inhibit immune response to RNA
            virus through the ESCRT pathway
  JOURNAL   Autophagy 20 (6), 1270-1285 (2024)
   PUBMED   38060409
  REMARK    GeneRIF: LTN1 promotes RLR degradation to inhibit immune response
            to RNA virus through the ESCRT pathway.
REFERENCE   2  (residues 1 to 1766)
  AUTHORS   Filbeck,S., Cerullo,F., Pfeffer,S. and Joazeiro,C.A.P.
  TITLE     Ribosome-associated quality-control mechanisms from bacteria to
            humans
  JOURNAL   Mol Cell 82 (8), 1451-1466 (2022)
   PUBMED   35452614
  REMARK    Review article
REFERENCE   3  (residues 1 to 1766)
  AUTHORS   Farhang,S., Sabaie,H., Gharesouran,J., Asadi,M.R., Arsang-Jang,S.,
            Ghafouri-Fard,S., Taheri,M. and Rezazadeh,M.
  TITLE     Expression Analysis of Ermin and Listerin E3 Ubiquitin Protein
            Ligase 1 Genes in the Periphery of Patients with Schizophrenia
  JOURNAL   J Mol Neurosci 72 (2), 246-254 (2022)
   PUBMED   34676516
  REMARK    GeneRIF: Expression Analysis of Ermin and Listerin E3 Ubiquitin
            Protein Ligase 1 Genes in the Periphery of Patients with
            Schizophrenia.
REFERENCE   4  (residues 1 to 1766)
  AUTHORS   Matsuo,Y., Ikeuchi,K., Saeki,Y., Iwasaki,S., Schmidt,C.,
            Udagawa,T., Sato,F., Tsuchiya,H., Becker,T., Tanaka,K.,
            Ingolia,N.T., Beckmann,R. and Inada,T.
  TITLE     Ubiquitination of stalled ribosome triggers ribosome-associated
            quality control
  JOURNAL   Nat Commun 8 (1), 159 (2017)
   PUBMED   28757607
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1766)
  AUTHORS   von der Malsburg,K., Shao,S. and Hegde,R.S.
  TITLE     The ribosome quality control pathway can access nascent
            polypeptides stalled at the Sec61 translocon
  JOURNAL   Mol Biol Cell 26 (12), 2168-2180 (2015)
   PUBMED   25877867
  REMARK    GeneRIF: E3 ligase listerin accesses nascent polypeptides stalled
            at the Sec61 translocon via a gap in the ribosome-translocon
            junction near the Sec61 lateral gate.
REFERENCE   6  (residues 1 to 1766)
  AUTHORS   Shao,S., Brown,A., Santhanam,B. and Hegde,R.S.
  TITLE     Structure and assembly pathway of the ribosome quality control
            complex
  JOURNAL   Mol Cell 57 (3), 433-444 (2015)
   PUBMED   25578875
  REMARK    GeneRIF: Results show that Listerin specificity for nascent
            chain-60S complexes depends on nuclear export mediator factor.
REFERENCE   7  (residues 1 to 1766)
  AUTHORS   Li,S., Wang,L., Berman,M., Kong,Y.Y. and Dorf,M.E.
  TITLE     Mapping a dynamic innate immunity protein interaction network
            regulating type I interferon production
  JOURNAL   Immunity 35 (3), 426-440 (2011)
   PUBMED   21903422
  REMARK    Erratum:[Immunity. 2011 Oct 28;35(4):647-8]
REFERENCE   8  (residues 1 to 1766)
  AUTHORS   Oshikawa,M., Tsutsui,C., Ikegami,T., Fuchida,Y., Matsubara,M.,
            Toyama,S., Usami,R., Ohtoko,K. and Kato,S.
  TITLE     Full-length transcriptome analysis of human retina-derived cell
            lines ARPE-19 and Y79 using the vector-capping method
  JOURNAL   Invest Ophthalmol Vis Sci 52 (9), 6662-6670 (2011)
   PUBMED   21697133
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1766)
  AUTHORS   Bengtson,M.H. and Joazeiro,C.A.
  TITLE     Role of a ribosome-associated E3 ubiquitin ligase in protein
            quality control
  JOURNAL   Nature 467 (7314), 470-473 (2010)
   PUBMED   20835226
REFERENCE   10 (residues 1 to 1766)
  AUTHORS   Chu,J., Hong,N.A., Masuda,C.A., Jenkins,B.V., Nelms,K.A.,
            Goodnow,C.C., Glynne,R.J., Wu,H., Masliah,E., Joazeiro,C.A. and
            Kay,S.A.
  TITLE     A mouse forward genetics screen identifies LISTERIN as an E3
            ubiquitin ligase involved in neurodegeneration
  JOURNAL   Proc Natl Acad Sci U S A 106 (7), 2097-2103 (2009)
   PUBMED   19196968
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB452437.1, BC140790.1, AB018257.2 and BF059116.1.
            
            On Sep 13, 2018 this sequence version replaced NP_056380.2.
            
            Summary: Like most RING finger proteins, LTN1 functions as an E3
            ubiquitin ligase (Chu et al., 2009 [PubMed 19196968]).[supplied by
            OMIM, Nov 2010].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.19104.1,
                                           SRR11853559.21293.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000361371.10/ ENSP00000354977.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1766
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..1766
                     /product="E3 ubiquitin-protein ligase listerin isoform 1"
                     /EC_number="2.3.2.27"
                     /note="ring finger protein 160; zinc finger protein 294;
                     E3 ubiquitin-protein ligase listerin; RING-type E3
                     ubiquitin transferase listerin"
                     /calculated_mol_wt=200422
     Region          59..>262
                     /region_name="COG5219"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227544"
     Region          59..96
                     /region_name="HEAT 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          100..138
                     /region_name="HEAT 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          273..314
                     /region_name="HEAT 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          335..372
                     /region_name="HEAT 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          380..418
                     /region_name="HEAT 5. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          433..473
                     /region_name="HEAT 6. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          513..551
                     /region_name="HEAT 7. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          611..658
                     /region_name="HEAT 8. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          676..714
                     /region_name="HEAT 9. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          768..810
                     /region_name="HEAT 10. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          911..949
                     /region_name="HEAT 11. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1068..1105
                     /region_name="HEAT 12. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1184..1227
                     /region_name="HEAT 13. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1314..1352
                     /region_name="HEAT 14. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1377..1414
                     /region_name="HEAT 15. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          1475..1512
                     /region_name="HEAT 16. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O94822.6)"
     Region          <1477..1765
                     /region_name="COG5219"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227544"
     CDS             1..1766
                     /gene="LTN1"
                     /gene_synonym="C21orf10; C21orf98; RNF160; ZNF294"
                     /coded_by="NM_015565.3:73..5373"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33527.3"
                     /db_xref="GeneID:26046"
                     /db_xref="HGNC:HGNC:13082"
                     /db_xref="MIM:613083"
ORIGIN      
        1 mggknkqrtk gnlrpsnsgr aaellakeqg tvpgfigfgt sqsdlgyvpa iqgaeeidsl
       61 vdsdfrmvlr klskkdvttk lkamqefgtm cterdtetvk gvlpywprif ckisldhdrr
      121 vreatqqafe klilkvkkql apylkslmgy wlmaqcdtyt paafaakdaf eaafppskqp
      181 eaiafckdei tsvlqdhlik etpdtlsdpq tvpeeereak fyrvvtcsll alkrllcllp
      241 dneldsleek fksllsqnkf wkygkhsvpq irsayfelvs alcqripqlm keeaskvsps
      301 vllsiddsdp ivcpalweav lytlttiedc wlhvnakksv fpklstvire ggrglatviy
      361 pyllpfiskl pqsitnpkld ffknfltslv aglstertkt sslessavis affeclrfim
      421 qqnlgeeeie qmlvndqlip fidavlkdpg lqhgqlfnhl aetlssweak adtekdekta
      481 hnlenvlihf werlseicva kisepeadve svlgvsnllq vlqkpksslk sskkkngkvr
      541 fadeilesnk enekcvsseg ekiegweltt epslthnssg llsplrkkpl edlvckladi
      601 sinyvnerks eqhlrflstl ldsfsssrvf kmllgdekqs ivqakpleia klvqknpavq
      661 flyqkligwl nedqrkdfgf lvdilysalr ccdndmerkk vlddltkvdl kwnsllkiie
      721 kacpssdkha lvtpwlkgdi lgeklvnlad clcnedlesr vsseshfser wtllslvlsq
      781 hvkndyligd vyveriivrl hetlfktkkl seaessdssv sficdvayny fssakgcllm
      841 pssedllltl fqlcaqskek thlpdflick lkntwlsgvn llvhqtdssy kestflhlsa
      901 lwlknqvqas sldinslqvl lsavddllnt llesedsylm gvyigsvmpn dsewekmrqs
      961 lpmqwlhrpl legrlslnye cfktdfkeqd iktlpshlct sallskmvli alrketvlen
     1021 nelekiiael lyslqwceel dnppifligf ceilqkmnit ydnlrvlgnt sgllqllfnr
     1081 srehgtlwsl iiaklilsrs issdevkphy krkesffplt egnlhtiqsl cpflskeekk
     1141 efsaqcipal lgwtkkdlcs tnggfghlai fnsclqtksi ddgellhgil kiiiswkkeh
     1201 ediflfscnl seaspevlgv nieiirflsl flkycsspla esewdfimcs mlawlettse
     1261 nqalysiplv qlfacvscdl acdlsaffds ttldtignlp vnlisewkef fsqgihslll
     1321 pilvtvtgen kdvsetsfqn amlkpmcetl tyiskeqlls hklparlvad qktnlpeylq
     1381 tllntlapll lfrarpvqia vyhmlyklmp elpqydqdnl ksygdeeeep alsppaalms
     1441 llsiqedlle nvlgcipvgq ivtikplsed fcyvlgyllt wkliltffka assqlralys
     1501 mylrktksln kllyhlfrlm penptyaeta vevpnkdpkt ffteelqlsi rettmlpyhi
     1561 phlacsvyhm tlkdlpamvr lwwnssekrv fnivdrftsk yvssvlsfqe issvqtstql
     1621 fngmtvkara ttrevmatyt iedivielii qlpsnyplgs iivesgkrvg vavqqwrnwm
     1681 lqlstylthq ngsimeglal wknnvdkrfe gvedcmicfs vihgfnyslp kkacrtckkk
     1741 fhsaclykwf tssnkstcpl cretff
//
LOCUS       NP_006776                824 aa            linear   PRI 20-NOV-2025
DEFINITION  mucosa-associated lymphoid tissue lymphoma translocation protein 1
            isoform a [Homo sapiens].
ACCESSION   NP_006776
VERSION     NP_006776.1
DBSOURCE    REFSEQ: accession NM_006785.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Kondreddy,V., Banerjee,R., Devi,B.L.A.P., Muralidharan,K. and
            Piramanayagam,S.
  TITLE     Inhibition of the MALT1-LPCAT3 axis protects cartilage degeneration
            and osteoarthritis
  JOURNAL   Cell Commun Signal 22 (1), 189 (2024)
   PUBMED   38519981
  REMARK    GeneRIF: Inhibition of the MALT1-LPCAT3 axis protects cartilage
            degeneration and osteoarthritis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Iwamuro,M., Takenaka,R., Miyahara,K., Okanoue,S., Yoshioka,M.,
            Sakaguchi,C., Yamamoto,K., Kawai,Y., Toyokawa,T., Tanaka,T. and
            Otsuka,M.
  TITLE     Long-term monitoring of gastric mucosa-associated lymphoid tissue
            lymphoma in patients with extra copies of the MALT1 gene
  JOURNAL   Sci Rep 14 (1), 4953 (2024)
   PUBMED   38418651
  REMARK    GeneRIF: Long-term monitoring of gastric mucosa-associated lymphoid
            tissue lymphoma in patients with extra copies of the MALT1 gene.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Maghe,C., Trillet,K., Andre-Gregoire,G., Kerherve,M., Merlet,L.,
            Jacobs,K.A., Schauer,K., Bidere,N. and Gavard,J.
  TITLE     The paracaspase MALT1 controls cholesterol homeostasis in
            glioblastoma stem-like cells through lysosome proteome shaping
  JOURNAL   Cell Rep 43 (1), 113631 (2024)
   PUBMED   38183651
  REMARK    GeneRIF: The paracaspase MALT1 controls cholesterol homeostasis in
            glioblastoma stem-like cells through lysosome proteome shaping.
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Liu,C., Zhu,J., Zhao,L., Li,G., Sun,J., Zhang,S. and Liang,X.
  TITLE     Blood MALT1 reflects acute exacerbation risk and inflammation in
            elderly chronic obstructive pulmonary disease patients
  JOURNAL   Biomark Med 18 (10-12), 513-521 (2024)
   PUBMED   39136445
  REMARK    GeneRIF: Blood MALT1 reflects acute exacerbation risk and
            inflammation in elderly chronic obstructive pulmonary disease
            patients.
REFERENCE   6  (residues 1 to 824)
  AUTHORS   Hulpiau,P., Driege,Y., Staal,J. and Beyaert,R.
  TITLE     MALT1 is not alone after all: identification of novel paracaspases
  JOURNAL   Cell Mol Life Sci 73 (5), 1103-1116 (2016)
   PUBMED   26377317
  REMARK    GeneRIF: Comparative analysis of the active site suggests that
            paracaspases constitute one of the several subclasses of
            metacaspases that have evolved several times independently.
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Suzuki,H., Motegi,M., Akagi,T., Hosokawa,Y. and Seto,M.
  TITLE     API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue
            lymphoma with t(11;18)(q21;q21)
  JOURNAL   Blood 94 (9), 3270-3271 (1999)
   PUBMED   10610122
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Akagi,T., Motegi,M., Tamura,A., Suzuki,R., Hosokawa,Y., Suzuki,H.,
            Ota,H., Nakamura,S., Morishima,Y., Taniwaki,M. and Seto,M.
  TITLE     A novel gene, MALT1 at 18q21, is involved in t(11;18) (q21;q21)
            found in low-grade B-cell lymphoma of mucosa-associated lymphoid
            tissue
  JOURNAL   Oncogene 18 (42), 5785-5794 (1999)
   PUBMED   10523859
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Hosaka,S., Akamatsu,T., Nakamura,S., Kaneko,T., Kitano,K.,
            Kiyosawa,K., Ota,H., Hosaka,N., Miyabayashi,H. and Katsuyama,T.
  TITLE     Mucosa-associated lymphoid tissue (MALT) lymphoma of the rectum
            with chromosomal translocation of the t(11;18)(q21;q21) and an
            additional aberration of trisomy 3
  JOURNAL   Am J Gastroenterol 94 (7), 1951-1954 (1999)
   PUBMED   10406266
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Dierlamm,J., Baens,M., Wlodarska,I., Stefanova-Ouzounova,M.,
            Hernandez,J.M., Hossfeld,D.K., De Wolf-Peeters,C., Hagemeijer,A.,
            Van den Berghe,H. and Marynen,P.
  TITLE     The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are
            recurrently rearranged in the t(11;18)(q21;q21) associated with
            mucosa-associated lymphoid tissue lymphomas
  JOURNAL   Blood 93 (11), 3601-3609 (1999)
   PUBMED   10339464
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF316597.1, AC104365.4 and
            AK026459.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a caspase-like protease that plays a
            role in BCL10-induced activation of NF-kappaB. The protein is a
            component of the CARMA1-BCL10-MALT1 (CBM) signalosome that triggers
            NF-kappaB signaling and lymphoctye activation following
            antigen-receptor stimulation. Mutations in this gene result in
            immunodeficiency 12 (IMD12). This gene has been found to be
            recurrently rearranged in chromosomal translocations with other
            genes in mucosa-associated lymphoid tissue lymphomas, including a
            t(11;18)(q21;q21) translocation with the baculoviral IAP
            repeat-containing protein 3 (also known as apoptosis inhibitor 2)
            locus [BIRC3(API2)-MALT1], and a t(14;18)(q32;q21) translocation
            with the immunoglobulin heavy chain locus (IGH-MALT1).
            Alternatively spliced transcript variants have been described for
            this gene. [provided by RefSeq, May 2018].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.156357.1,
                                           SRR1803612.156996.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000649217.2/ ENSP00000497997.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.32"
     Protein         1..824
                     /product="mucosa-associated lymphoid tissue lymphoma
                     translocation protein 1 isoform a"
                     /EC_number="3.4.22.-"
                     /note="caspase-like protein; paracaspase-1;
                     mucosa-associated lymphoid tissue lymphoma translocation
                     protein 1; mucosa associated lymphoid tissue lymphoma
                     translocation gene 1; MALT1 protease"
                     /calculated_mol_wt=92142
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Region          42..126
                     /region_name="Death_MALT1"
                     /note="Death domain similar to that found in
                     Mucosa-associated lymphoid tissue-lymphoma-translocation
                     gene 1; cd08783"
                     /db_xref="CDD:260053"
     Region          124..194
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            126..127
                     /site_type="other"
                     /note="Breakpoint for translocation to form BIRC2-MALT1;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Site            135
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Site            216..217
                     /site_type="other"
                     /note="Breakpoint for translocation to form BIRC2-MALT1;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Region          226..294
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            320..321
                     /site_type="other"
                     /note="Breakpoint for translocation to form BIRC2-MALT1;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Site            323..324
                     /site_type="other"
                     /note="Breakpoint for translocation to form BIRC2-MALT1;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Site            329..330
                     /site_type="other"
                     /note="Breakpoint for translocation to form BIRC2-MALT1;
                     propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Region          334..557
                     /region_name="COG4249"
                     /note="Uncharacterized conserved protein, contains caspase
                     domain [General function prediction only]"
                     /db_xref="CDD:443391"
     Region          348..562
                     /region_name="Caspase-like"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Region          369..376
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UDY8.1)"
     Region          583..719
                     /region_name="MALT1_Ig"
                     /note="MALT1 Ig-like domain; pfam18703"
                     /db_xref="CDD:465840"
     CDS             1..824
                     /gene="MALT1"
                     /gene_synonym="IMD12; MLT; MLT1; PCASP1"
                     /coded_by="NM_006785.4:180..2654"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11967.1"
                     /db_xref="GeneID:10892"
                     /db_xref="HGNC:HGNC:6819"
                     /db_xref="MIM:604860"
ORIGIN      
        1 msllgdplqa lppsaaptgp llappagatl nrlrepllrr lselldqape grgwrrlael
       61 agsrgrlrls cldleqcslk vlepegspsl cllklmgekg ctvtelsdfl qamehtevlq
      121 llsppgikit vnpeskavla gqfvklccra tghpfvqyqw fkmnkeipng ntselifnav
      181 hvkdagfyvc rvnnnftfef sqwsqldvcd ipesfqrsvd gvsesklqic veptsqklmp
      241 gstlvlqcva vgspiphyqw fknelplthe tkklymvpyv dlehqgtywc hvyndrdsqd
      301 skkveiiigr tdeavected elnnlghpdn keqttdqpla kdkvallign mnyrehpklk
      361 aplvdvyelt nllrqldfkv vslldlteye mrnavdefll lldkgvygll yyaghgyenf
      421 gnsfmvpvda pnpyrsencl cvqnilklmq eketglnvfl ldmcrkrndy ddtipildal
      481 kvtanivfgy atcqgaeafe iqhsglangi fmkflkdrll edkkitvlld evaedmgkch
      541 ltkgkqalei rsslsekral tdpiqgteys aeslvrnlqw akahelpesm clkfdcgvqi
      601 qlgfaaefsn vmiiytsivy kppeiimcda yvtdfpldld idpkdankgt peetgsylvs
      661 kdlpkhclyt rlsslqklke hlvftvclsy qysgledtve dkqevnvgkp liakldmhrg
      721 lgrktcfqtc lmsngpyqss aatsggaghy hslqdpfhgv yhshpgnpsn vtpadschcs
      781 rtpdafissf ahhaschfsr snvpvettde ipfsfsdrlr isek
//
LOCUS       NP_115557                152 aa            linear   PRI 20-NOV-2025
DEFINITION  protein eva-1 homolog A [Homo sapiens].
ACCESSION   NP_115557
VERSION     NP_115557.1
DBSOURCE    REFSEQ: accession NM_032181.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 152)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 152)
  AUTHORS   Chen,Y., Wang,D., Yin,J., Krafft,P.R., Luo,X., Hao,D., Li,C.,
            Liu,Y., Li,L., Zhang,Y. and Zhu,C.
  TITLE     Increased TMEM166 Level in Patients with Postoperative Stroke after
            Carotid Endarterectomy
  JOURNAL   Neuroscience 549, 138-144 (2024)
   PUBMED   38734302
  REMARK    GeneRIF: Increased TMEM166 Level in Patients with Postoperative
            Stroke after Carotid Endarterectomy.
REFERENCE   3  (residues 1 to 152)
  AUTHORS   Canham,L., Sendac,S., Diagbouga,M.R., Wolodimeroff,E., Pirri,D.,
            Tardajos Ayllon,B., Feng,S., Souilhol,C., Chico,T.J.A., Evans,P.C.
            and Serbanovic-Canic,J.
  TITLE     EVA1A (Eva-1 Homolog A) Promotes Endothelial Apoptosis and
            Inflammatory Activation Under Disturbed Flow Via Regulation of
            Autophagy
  JOURNAL   Arterioscler Thromb Vasc Biol 43 (4), 547-561 (2023)
   PUBMED   36794585
  REMARK    GeneRIF: EVA1A (Eva-1 Homolog A) Promotes Endothelial Apoptosis and
            Inflammatory Activation Under Disturbed Flow Via Regulation of
            Autophagy.
            Erratum:[Arterioscler Thromb Vasc Biol. 2023 Jun;43(6):e230. doi:
            10.1161/ATV.0000000000000163. PMID: 37224275]
REFERENCE   4  (residues 1 to 152)
  AUTHORS   Xu,Q., Liao,Z., Gong,Z., Liu,X., Yang,Y., Wang,Z., Yang,W., Hou,L.,
            Yang,J., Song,J., Liu,W., Wang,B., Hua,J., Pu,M. and Li,N.
  TITLE     Down-regulation of EVA1A by miR-103a-3p promotes hepatocellular
            carcinoma cells proliferation and migration
  JOURNAL   Cell Mol Biol Lett 27 (1), 93 (2022)
   PUBMED   36273122
  REMARK    GeneRIF: Down-regulation of EVA1A by miR-103a-3p promotes
            hepatocellular carcinoma cells proliferation and migration.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 152)
  AUTHORS   Liao,Z., Gong,Z., Wang,Z., Yang,W., Liu,W., Hou,L., Liu,X., Hua,J.,
            Wang,B. and Li,N.
  TITLE     The Degradation of TMEM166 by Autophagy Promotes AMPK Activation to
            Protect SH-SY5Y Cells Exposed to MPP
  JOURNAL   Cells 11 (17), 2706 (2022)
   PUBMED   36078115
  REMARK    GeneRIF: The Degradation of TMEM166 by Autophagy Promotes AMPK
            Activation to Protect SH-SY5Y Cells Exposed to MPP().
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 152)
  AUTHORS   Xu,D., Yang,F., He,H., Hu,J., Lv,X., Ma,D. and Chen,Y.Y.
  TITLE     Expression of TMEM166 protein in human normal and tumor tissues
  JOURNAL   Appl Immunohistochem Mol Morphol 21 (6), 543-552 (2013)
   PUBMED   22495369
  REMARK    GeneRIF: TMEM166 expression was widely down-regulated in the cancer
            tissues.
REFERENCE   7  (residues 1 to 152)
  AUTHORS   Li,L., Khatibi,N.H., Hu,Q., Yan,J., Chen,C., Han,J., Ma,D., Chen,Y.
            and Zhou,C.
  TITLE     Transmembrane protein 166 regulates autophagic and apoptotic
            activities following focal cerebral ischemic injury in rats
  JOURNAL   Exp Neurol 234 (1), 181-190 (2012)
   PUBMED   22227058
REFERENCE   8  (residues 1 to 152)
  AUTHORS   Sun,W., Ma,X.M., Bai,J.P., Zhang,G.Q., Zhu,Y.J., Ma,H.M., Guo,H.,
            Chen,Y.Y. and Ding,J.B.
  TITLE     Transmembrane protein 166 expression in esophageal squamous cell
            carcinoma in Xinjiang, China
  JOURNAL   Asian Pac J Cancer Prev 13 (8), 3713-3716 (2012)
   PUBMED   23098460
  REMARK    GeneRIF: Low TMEM166 mRNA and protein expression is associated with
            esophageal squamous cell carcinoma.
REFERENCE   9  (residues 1 to 152)
  AUTHORS   Wang,L., Yu,C., Lu,Y., He,P., Guo,J., Zhang,C., Song,Q., Ma,D.,
            Shi,T. and Chen,Y.
  TITLE     TMEM166, a novel transmembrane protein, regulates cell autophagy
            and apoptosis
  JOURNAL   Apoptosis 12 (8), 1489-1502 (2007)
   PUBMED   17492404
  REMARK    GeneRIF: TMEM166 is a novel regulator involved in both autophagy
            and apoptosis.
REFERENCE   10 (residues 1 to 152)
  AUTHORS   Wan,D., Gong,Y., Qin,W., Zhang,P., Li,J., Wei,L., Zhou,X., Li,H.,
            Qiu,X., Zhong,F., He,L., Yu,J., Yao,G., Jiang,H., Qian,L., Yu,Y.,
            Shu,H., Chen,X., Xu,H., Guo,M., Pan,Z., Chen,Y., Ge,C., Yang,S. and
            Gu,J.
  TITLE     Large-scale cDNA transfection screening for genes related to cancer
            development and progression
  JOURNAL   Proc Natl Acad Sci U S A 101 (44), 15724-15729 (2004)
   PUBMED   15498874
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2004 Dec 14:101(50):17565]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023453.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023453.1, BI761625.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1970526,
                                           SAMEA2142853 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..152
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p12"
     Protein         1..152
                     /product="protein eva-1 homolog A"
                     /note="transmembrane protein 166; protein FAM176A; family
                     with sequence similarity 176, member A"
                     /calculated_mol_wt=17339
     Region          1..60
                     /region_name="Necessary for the localization and
                     biological activity"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Region          13..152
                     /region_name="FAM176"
                     /note="FAM176 family; pfam14851"
                     /db_xref="CDD:464347"
     Site            35..55
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Region          70..97
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91WM6; propagated from
                     UniProtKB/Swiss-Prot (Q9H8M9.1)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (Q9H8M9.1)"
     CDS             1..152
                     /gene="EVA1A"
                     /gene_synonym="FAM176A; TMEM166"
                     /coded_by="NM_032181.3:436..894"
                     /db_xref="CCDS:CCDS1959.1"
                     /db_xref="GeneID:84141"
                     /db_xref="HGNC:HGNC:25816"
                     /db_xref="MIM:618990"
ORIGIN      
        1 mrlplshspe hvemallsni laaysfvsen peraalyfvs gvciglvltl aalvirisch
       61 tdcrrrpgkk flqdresssd ssdsedgsed tvsdlsvrrh rrfertlnkn vftsaeeler
      121 aqrleereri ireiwmngqp evpgtrslnr yy
//
LOCUS       NP_001191439             347 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic initiation factor 4A-I isoform 2 [Homo sapiens].
ACCESSION   NP_001191439
VERSION     NP_001191439.1
DBSOURCE    REFSEQ: accession NM_001204510.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 347)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 347)
  AUTHORS   Shi,J.Y., Wen,R., Chen,J.Y., Feng,Y.Q., Zhang,Y.Y., Hou,S.J.,
            Xi,Y.J., Wang,J.F. and Zhang,Y.F.
  TITLE     Genetic evidence supporting potential causal roles of EIF4 family
            in breast cancer: a two-sample randomized Mendelian study
  JOURNAL   Sci Rep 14 (1), 20191 (2024)
   PUBMED   39215053
  REMARK    GeneRIF: Genetic evidence supporting potential causal roles of EIF4
            family in breast cancer: a two-sample randomized Mendelian study.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 347)
  AUTHORS   Jiao,D., Sun,H., Zhao,X., Chen,Y., Lv,Z., Shi,Q., Li,Y., Wang,C.
            and Gao,K.
  TITLE     mTORC1/S6K1 signaling promotes sustained oncogenic translation
            through modulating CRL3IBTK-mediated ubiquitination of eIF4A1 in
            cancer cells
  JOURNAL   Elife 12, 92236 (2024)
   PUBMED   38738857
  REMARK    GeneRIF: mTORC1/S6K1 signaling promotes sustained oncogenic
            translation through modulating CRL3[IBTK]-mediated ubiquitination
            of eIF4A1 in cancer cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 347)
  AUTHORS   Schmidt,T., Dabrowska,A., Waldron,J.A., Hodge,K., Koulouras,G.,
            Gabrielsen,M., Munro,J., Tack,D.C., Harris,G., McGhee,E., Scott,D.,
            Carlin,L.M., Huang,D., Le Quesne,J., Zanivan,S., Wilczynska,A. and
            Bushell,M.
  TITLE     eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences to
            activate localised eIF4A1-unwinding through eIF4A1-multimerisation
            to facilitate translation
  JOURNAL   Nucleic Acids Res 51 (4), 1859-1879 (2023)
   PUBMED   36727461
  REMARK    GeneRIF: eIF4A1-dependent mRNAs employ purine-rich 5'UTR sequences
            to activate localised eIF4A1-unwinding through
            eIF4A1-multimerisation to facilitate translation.
REFERENCE   5  (residues 1 to 347)
  AUTHORS   Steinmann,S.M., Sanchez-Martin,A., Tanzer,E., Cigliano,A.,
            Pes,G.M., Simile,M.M., Desaubry,L., Marin,J.J.G., Evert,M. and
            Calvisi,D.F.
  TITLE     eIF4A1 Is a Prognostic Marker and Actionable Target in Human
            Hepatocellular Carcinoma
  JOURNAL   Int J Mol Sci 24 (3), 2055 (2023)
   PUBMED   36768380
  REMARK    GeneRIF: eIF4A1 Is a Prognostic Marker and Actionable Target in
            Human Hepatocellular Carcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 347)
  AUTHORS   Imataka,H. and Sonenberg,N.
  TITLE     Human eukaryotic translation initiation factor 4G (eIF4G) possesses
            two separate and independent binding sites for eIF4A
  JOURNAL   Mol Cell Biol 17 (12), 6940-6947 (1997)
   PUBMED   9372926
REFERENCE   7  (residues 1 to 347)
  AUTHORS   Kukimoto,I., Watanabe,S., Taniguchi,K., Ogata,T., Yoshiike,K. and
            Kanda,T.
  TITLE     Characterization of the cloned promoter of the human initiation
            factor 4AI gene
  JOURNAL   Biochem Biophys Res Commun 233 (3), 844-847 (1997)
   PUBMED   9168945
REFERENCE   8  (residues 1 to 347)
  AUTHORS   Kim,N.S., Kato,T., Abe,N. and Kato,S.
  TITLE     Nucleotide sequence of human cDNA encoding eukaryotic initiation
            factor 4AI
  JOURNAL   Nucleic Acids Res 21 (8), 2012 (1993)
   PUBMED   8493113
REFERENCE   9  (residues 1 to 347)
  AUTHORS   Yoder-Hill,J., Pause,A., Sonenberg,N. and Merrick,W.C.
  TITLE     The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges
            with eIF-4A
  JOURNAL   J Biol Chem 268 (8), 5566-5573 (1993)
   PUBMED   8449919
REFERENCE   10 (residues 1 to 347)
  AUTHORS   Reddy,N.S., Roth,W.W., Bragg,P.W. and Wahba,A.J.
  TITLE     Isolation and mapping of a gene for protein synthesis initiation
            factor 4A and its expression during differentiation of murine
            erythroleukemia cells
  JOURNAL   Gene 70 (2), 231-243 (1988)
   PUBMED   3215517
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BG284868.1, AC016876.10, BC006210.2 and AA446856.1.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            that causes a frameshift in the 3' coding region, compared to
            variant 1, resulting in an isoform (2) with a distinct and shorter
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1171492.1, BC006210.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..347
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.1"
     Protein         1..347
                     /product="eukaryotic initiation factor 4A-I isoform 2"
                     /EC_number="3.6.4.13"
                     /note="eukaryotic translation initiation factor 4A;
                     eukaryotic initiation factor 4A-I; eukaryotic initiation
                     factor 4AI; ATP-dependent RNA helicase eIF4A-1"
                     /calculated_mol_wt=39417
     Region          1..21
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P60842.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:37316325,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Region          20..334
                     /region_name="DEAD-like_helicase_N"
                     /note="N-terminal helicase domain of the DEAD-box helicase
                     superfamily; cl28899"
                     /db_xref="CDD:475120"
     Region          32..60
                     /region_name="Q motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P60842.1)"
     Site            order(34,52,54,59,78..84)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:350804"
     Site            order(35,45,48,53)
                     /site_type="other"
                     /note="eIF4G interface [polypeptide binding]"
                     /db_xref="CDD:350804"
     Site            118
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Site            174
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Region          182..185
                     /region_name="DEAD box"
                     /note="propagated from UniProtKB/Swiss-Prot (P60842.1)"
     Site            193
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P60843; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     Site            238
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P60843; propagated from
                     UniProtKB/Swiss-Prot (P60842.1)"
     CDS             1..347
                     /gene="EIF4A1"
                     /gene_synonym="DDX2A; EIF-4A; eIF-4A-I; EIF4A; eIF4A-I"
                     /coded_by="NM_001204510.2:18..1061"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS58511.1"
                     /db_xref="GeneID:1973"
                     /db_xref="HGNC:HGNC:3282"
                     /db_xref="MIM:602641"
ORIGIN      
        1 msasqdsrsr dngpdgmepe gviesnwnei vdsfddmnls esllrgiyay gfekpsaiqq
       61 railpcikgy dviaqaqsgt gktatfaisi lqqieldlka tqalvlaptr elaqqiqkvv
      121 malgdymgas chaciggtnv raevqklqme aphiivgtpg rvfdmlnrry lspkyikmfv
      181 ldeademlsr gfkdqiydif qklnsntqvv llsatmpsdv levtkkfmrd pirilvkkee
      241 ltlegirqfy invereewkl dtlcdlyetl titqavifin trrkvdwlte kmhardftvs
      301 amhgdmdqke rdvimrefrs gssrvlittd llgklypqnr srwtvwp
//
LOCUS       NP_005473                395 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase precursor [Homo sapiens].
ACCESSION   NP_005473
VERSION     NP_005473.1
DBSOURCE    REFSEQ: accession NM_005482.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 395)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 395)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 395)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 395)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   5  (residues 1 to 395)
  AUTHORS   Liu,S.S., Jin,F., Liu,Y.S., Murakami,Y., Sugita,Y., Kato,T.,
            Gao,X.D., Kinoshita,T., Hattori,M. and Fujita,M.
  TITLE     Functional Analysis of the GPI Transamidase Complex by Screening
            for Amino Acid Mutations in Each Subunit
  JOURNAL   Molecules 26 (18), 5462 (2021)
   PUBMED   34576938
  REMARK    GeneRIF: Functional Analysis of the GPI Transamidase Complex by
            Screening for Amino Acid Mutations in Each Subunit.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 395)
  AUTHORS   Ohishi,K., Inoue,N., Maeda,Y., Takeda,J., Riezman,H. and
            Kinoshita,T.
  TITLE     Gaa1p and gpi8p are components of a glycosylphosphatidylinositol
            (GPI) transamidase that mediates attachment of GPI to proteins
  JOURNAL   Mol Biol Cell 11 (5), 1523-1533 (2000)
   PUBMED   10793132
REFERENCE   7  (residues 1 to 395)
  AUTHORS   Meyer,U., Benghezal,M., Imhof,I. and Conzelmann,A.
  TITLE     Active site determination of Gpi8p, a caspase-related enzyme
            required for glycosylphosphatidylinositol anchor addition to
            proteins
  JOURNAL   Biochemistry 39 (12), 3461-3471 (2000)
   PUBMED   10727241
REFERENCE   8  (residues 1 to 395)
  AUTHORS   Yu,J., Nagarajan,S., Knez,J.J., Udenfriend,S., Chen,R. and
            Medof,M.E.
  TITLE     The affected gene underlying the class K
            glycosylphosphatidylinositol (GPI) surface protein defect codes for
            the GPI transamidase
  JOURNAL   Proc Natl Acad Sci U S A 94 (23), 12580-12585 (1997)
   PUBMED   9356492
REFERENCE   9  (residues 1 to 395)
  AUTHORS   Benghezal,M., Benachour,A., Rusconi,S., Aebi,M. and Conzelmann,A.
  TITLE     Yeast Gpi8p is essential for GPI anchor attachment onto proteins
  JOURNAL   EMBO J 15 (23), 6575-6583 (1996)
   PUBMED   8978684
REFERENCE   10 (residues 1 to 395)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC093433.2, AC113935.2 and
            AL035409.15.
            
            Summary: This gene encodes a member of the cysteine protease family
            C13 that is involved in glycosylphosphatidylinositol (GPI)-anchor
            biosynthesis. The GPI-anchor is a glycolipid found on many blood
            cells and serves to anchor proteins to the cell surface. This
            protein is a member of the multisubunit enzyme, GPI transamidase
            and is thought to be its enzymatic component. GPI transamidase
            mediates GPI anchoring in the endoplasmic reticulum, by catalyzing
            the transfer of fully assembled GPI units to proteins. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.9613.1,
                                           SRR1660805.144577.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000370812.8/ ENSP00000359848.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..395
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p31.1"
     Protein         1..395
                     /product="GPI-anchor transamidase precursor"
                     /EC_number="3.-.-.-"
                     /note="GPI transamidase subunit; phosphatidylinositol
                     glycan, class K; GPI-anchor transamidase;
                     phosphatidylinositol-glycan biosynthesis class K protein;
                     PIG-K; GPI8 homolog; GPI-anchor transamidase component
                     PIGK, catalytic subunit"
                     /calculated_mol_wt=42605
     sig_peptide     1..27
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2665
     mat_peptide     28..395
                     /product="GPI-anchor transamidase"
                     /calculated_mol_wt=42605
     Region          45..273
                     /region_name="CASc"
                     /note="Caspase, interleukin-1 beta converting enzyme (ICE)
                     homologues; Cysteine-dependent aspartate-directed
                     proteases that mediate programmed cell death (apoptosis).
                     Caspases are synthesized as inactive zymogens and
                     activated by proteolysis of the peptide...; cl00042"
                     /db_xref="CDD:444667"
     Region          231..236
                     /region_name="Autoinhibitory loop.
                     /evidence=ECO:0000269|PubMed:37684232"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92643.2)"
     Site            369..385
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92643.2)"
     CDS             1..395
                     /gene="PIGK"
                     /gene_synonym="GPI8; NEDHCAS"
                     /coded_by="NM_005482.3:29..1216"
                     /db_xref="CCDS:CCDS674.1"
                     /db_xref="GeneID:10026"
                     /db_xref="HGNC:HGNC:8965"
                     /db_xref="MIM:605087"
ORIGIN      
        1 mavtdslsra atvlatvlll sfgsvaashi edqaeqffrs ghtnnwavlv ctsrfwfnyr
       61 hvantlsvyr svkrlgipds hivlmladdm acnprnpkpa tvfshknmel nvygddvevd
      121 yrsyevtven flrvltgrip pstprskrll sddrsniliy mtghggngfl kfqdseeitn
      181 ieladafeqm wqkrrynell fiidtcqgas myerfyspni malassqvge dslshqpdpa
      241 igvhlmdryt fyvlefleei npasqtnmnd lfqvcpkslc vstpghrtdl fqrdpknvli
      301 tdffgsvrkv eittetiklq qdseimessy kedqmdeklm eplkyaeqlp vaqiihqkpk
      361 lkdwhppggf ilglwaliim vffktygikh mkfif
//
LOCUS       NP_060735                663 aa            linear   PRI 20-NOV-2025
DEFINITION  innate immunity activator protein isoform 1 [Homo sapiens].
ACCESSION   NP_060735
VERSION     NP_060735.4
DBSOURCE    REFSEQ: accession NM_018265.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 663)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 663)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   3  (residues 1 to 663)
  AUTHORS   Chang,D., Luong,P., Li,Q., LeBarron,J., Anderson,M., Barrett,L. and
            Lencer,W.I.
  TITLE     Small-molecule modulators of INAVA cytosolic condensate and
            cell-cell junction assemblies
  JOURNAL   J Cell Biol 220 (9) (2021)
   PUBMED   34251416
  REMARK    GeneRIF: Small-molecule modulators of INAVA cytosolic condensate
            and cell-cell junction assemblies.
REFERENCE   4  (residues 1 to 663)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 663)
  AUTHORS   Manzanillo,P., Mouchess,M., Ota,N., Dai,B., Ichikawa,R., Wuster,A.,
            Haley,B., Alvarado,G., Kwon,Y., Caothien,R., Roose-Girma,M.,
            Warming,S., McKenzie,B.S., Keir,M.E., Scherl,A., Ouyang,W. and
            Yi,T.
  TITLE     Inflammatory Bowel Disease Susceptibility Gene C1ORF106 Regulates
            Intestinal Epithelial Permeability
  JOURNAL   Immunohorizons 2 (5), 164-171 (2018)
   PUBMED   31022698
  REMARK    GeneRIF: Study identifies C1ORF106 as an epithelial cell junction
            protein, and the loss of C1ORF106 augments TNF-alpha-induced
            intestinal epithelial leakage and diarrhea that may play a critical
            role in the development of inflammatory bowel disease.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 663)
  AUTHORS   Jostins,L., Ripke,S., Weersma,R.K., Duerr,R.H., McGovern,D.P.,
            Hui,K.Y., Lee,J.C., Schumm,L.P., Sharma,Y., Anderson,C.A.,
            Essers,J., Mitrovic,M., Ning,K., Cleynen,I., Theatre,E.,
            Spain,S.L., Raychaudhuri,S., Goyette,P., Wei,Z., Abraham,C.,
            Achkar,J.P., Ahmad,T., Amininejad,L., Ananthakrishnan,A.N.,
            Andersen,V., Andrews,J.M., Baidoo,L., Balschun,T., Bampton,P.A.,
            Bitton,A., Boucher,G., Brand,S., Buning,C., Cohain,A., Cichon,S.,
            D'Amato,M., De Jong,D., Devaney,K.L., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Ferguson,L.R., Franchimont,D., Fransen,K.,
            Gearry,R., Georges,M., Gieger,C., Glas,J., Haritunians,T., Hart,A.,
            Hawkey,C., Hedl,M., Hu,X., Karlsen,T.H., Kupcinskas,L.,
            Kugathasan,S., Latiano,A., Laukens,D., Lawrance,I.C., Lees,C.W.,
            Louis,E., Mahy,G., Mansfield,J., Morgan,A.R., Mowat,C., Newman,W.,
            Palmieri,O., Ponsioen,C.Y., Potocnik,U., Prescott,N.J.,
            Regueiro,M., Rotter,J.I., Russell,R.K., Sanderson,J.D., Sans,M.,
            Satsangi,J., Schreiber,S., Simms,L.A., Sventoraityte,J.,
            Targan,S.R., Taylor,K.D., Tremelling,M., Verspaget,H.W., De Vos,M.,
            Wijmenga,C., Wilson,D.C., Winkelmann,J., Xavier,R.J., Zeissig,S.,
            Zhang,B., Zhang,C.K., Zhao,H., Silverberg,M.S., Annese,V.,
            Hakonarson,H., Brant,S.R., Radford-Smith,G., Mathew,C.G.,
            Rioux,J.D., Schadt,E.E., Daly,M.J., Franke,A., Parkes,M.,
            Vermeire,S., Barrett,J.C. and Cho,J.H.
  CONSRTM   International IBD Genetics Consortium (IIBDGC)
  TITLE     Host-microbe interactions have shaped the genetic architecture of
            inflammatory bowel disease
  JOURNAL   Nature 491 (7422), 119-124 (2012)
   PUBMED   23128233
REFERENCE   7  (residues 1 to 663)
  AUTHORS   Sawcer,S., Hellenthal,G., Pirinen,M., Spencer,C.C.,
            Patsopoulos,N.A., Moutsianas,L., Dilthey,A., Su,Z., Freeman,C.,
            Hunt,S.E., Edkins,S., Gray,E., Booth,D.R., Potter,S.C., Goris,A.,
            Band,G., Oturai,A.B., Strange,A., Saarela,J., Bellenguez,C.,
            Fontaine,B., Gillman,M., Hemmer,B., Gwilliam,R., Zipp,F.,
            Jayakumar,A., Martin,R., Leslie,S., Hawkins,S., Giannoulatou,E.,
            D'alfonso,S., Blackburn,H., Martinelli Boneschi,F., Liddle,J.,
            Harbo,H.F., Perez,M.L., Spurkland,A., Waller,M.J., Mycko,M.P.,
            Ricketts,M., Comabella,M., Hammond,N., Kockum,I., McCann,O.T.,
            Ban,M., Whittaker,P., Kemppinen,A., Weston,P., Hawkins,C.,
            Widaa,S., Zajicek,J., Dronov,S., Robertson,N., Bumpstead,S.J.,
            Barcellos,L.F., Ravindrarajah,R., Abraham,R., Alfredsson,L.,
            Ardlie,K., Aubin,C., Baker,A., Baker,K., Baranzini,S.E.,
            Bergamaschi,L., Bergamaschi,R., Bernstein,A., Berthele,A.,
            Boggild,M., Bradfield,J.P., Brassat,D., Broadley,S.A., Buck,D.,
            Butzkueven,H., Capra,R., Carroll,W.M., Cavalla,P., Celius,E.G.,
            Cepok,S., Chiavacci,R., Clerget-Darpoux,F., Clysters,K., Comi,G.,
            Cossburn,M., Cournu-Rebeix,I., Cox,M.B., Cozen,W., Cree,B.A.,
            Cross,A.H., Cusi,D., Daly,M.J., Davis,E., de Bakker,P.I.,
            Debouverie,M., D'hooghe,M.B., Dixon,K., Dobosi,R., Dubois,B.,
            Ellinghaus,D., Elovaara,I., Esposito,F., Fontenille,C., Foote,S.,
            Franke,A., Galimberti,D., Ghezzi,A., Glessner,J., Gomez,R.,
            Gout,O., Graham,C., Grant,S.F., Guerini,F.R., Hakonarson,H.,
            Hall,P., Hamsten,A., Hartung,H.P., Heard,R.N., Heath,S., Hobart,J.,
            Hoshi,M., Infante-Duarte,C., Ingram,G., Ingram,W., Islam,T.,
            Jagodic,M., Kabesch,M., Kermode,A.G., Kilpatrick,T.J., Kim,C.,
            Klopp,N., Koivisto,K., Larsson,M., Lathrop,M., Lechner-Scott,J.S.,
            Leone,M.A., Leppa,V., Liljedahl,U., Bomfim,I.L., Lincoln,R.R.,
            Link,J., Liu,J., Lorentzen,A.R., Lupoli,S., Macciardi,F., Mack,T.,
            Marriott,M., Martinelli,V., Mason,D., McCauley,J.L., Mentch,F.,
            Mero,I.L., Mihalova,T., Montalban,X., Mottershead,J., Myhr,K.M.,
            Naldi,P., Ollier,W., Page,A., Palotie,A., Pelletier,J., Piccio,L.,
            Pickersgill,T., Piehl,F., Pobywajlo,S., Quach,H.L., Ramsay,P.P.,
            Reunanen,M., Reynolds,R., Rioux,J.D., Rodegher,M., Roesner,S.,
            Rubio,J.P., Ruckert,I.M., Salvetti,M., Salvi,E., Santaniello,A.,
            Schaefer,C.A., Schreiber,S., Schulze,C., Scott,R.J., Sellebjerg,F.,
            Selmaj,K.W., Sexton,D., Shen,L., Simms-Acuna,B., Skidmore,S.,
            Sleiman,P.M., Smestad,C., Sorensen,P.S., Sondergaard,H.B.,
            Stankovich,J., Strange,R.C., Sulonen,A.M., Sundqvist,E.,
            Syvanen,A.C., Taddeo,F., Taylor,B., Blackwell,J.M., Tienari,P.,
            Bramon,E., Tourbah,A., Brown,M.A., Tronczynska,E., Casas,J.P.,
            Tubridy,N., Corvin,A., Vickery,J., Jankowski,J., Villoslada,P.,
            Markus,H.S., Wang,K., Mathew,C.G., Wason,J., Palmer,C.N.,
            Wichmann,H.E., Plomin,R., Willoughby,E., Rautanen,A.,
            Winkelmann,J., Wittig,M., Trembath,R.C., Yaouanq,J.,
            Viswanathan,A.C., Zhang,H., Wood,N.W., Zuvich,R., Deloukas,P.,
            Langford,C., Duncanson,A., Oksenberg,J.R., Pericak-Vance,M.A.,
            Haines,J.L., Olsson,T., Hillert,J., Ivinson,A.J., De Jager,P.L.,
            Peltonen,L., Stewart,G.J., Hafler,D.A., Hauser,S.L., McVean,G.,
            Donnelly,P. and Compston,A.
  CONSRTM   International Multiple Sclerosis Genetics Consortium; Wellcome
            Trust Case Control Consortium 2
  TITLE     Genetic risk and a primary role for cell-mediated immune mechanisms
            in multiple sclerosis
  JOURNAL   Nature 476 (7359), 214-219 (2011)
   PUBMED   21833088
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 663)
  AUTHORS   Anderson,C.A., Boucher,G., Lees,C.W., Franke,A., D'Amato,M.,
            Taylor,K.D., Lee,J.C., Goyette,P., Imielinski,M., Latiano,A.,
            Lagace,C., Scott,R., Amininejad,L., Bumpstead,S., Baidoo,L.,
            Baldassano,R.N., Barclay,M., Bayless,T.M., Brand,S., Buning,C.,
            Colombel,J.F., Denson,L.A., De Vos,M., Dubinsky,M., Edwards,C.,
            Ellinghaus,D., Fehrmann,R.S., Floyd,J.A., Florin,T.,
            Franchimont,D., Franke,L., Georges,M., Glas,J., Glazer,N.L.,
            Guthery,S.L., Haritunians,T., Hayward,N.K., Hugot,J.P., Jobin,G.,
            Laukens,D., Lawrance,I., Lemann,M., Levine,A., Libioulle,C.,
            Louis,E., McGovern,D.P., Milla,M., Montgomery,G.W., Morley,K.I.,
            Mowat,C., Ng,A., Newman,W., Ophoff,R.A., Papi,L., Palmieri,O.,
            Peyrin-Biroulet,L., Panes,J., Phillips,A., Prescott,N.J.,
            Proctor,D.D., Roberts,R., Russell,R., Rutgeerts,P., Sanderson,J.,
            Sans,M., Schumm,P., Seibold,F., Sharma,Y., Simms,L.A.,
            Seielstad,M., Steinhart,A.H., Targan,S.R., van den Berg,L.H.,
            Vatn,M., Verspaget,H., Walters,T., Wijmenga,C., Wilson,D.C.,
            Westra,H.J., Xavier,R.J., Zhao,Z.Z., Ponsioen,C.Y., Andersen,V.,
            Torkvist,L., Gazouli,M., Anagnou,N.P., Karlsen,T.H., Kupcinskas,L.,
            Sventoraityte,J., Mansfield,J.C., Kugathasan,S., Silverberg,M.S.,
            Halfvarson,J., Rotter,J.I., Mathew,C.G., Griffiths,A.M., Gearry,R.,
            Ahmad,T., Brant,S.R., Chamaillard,M., Satsangi,J., Cho,J.H.,
            Schreiber,S., Daly,M.J., Barrett,J.C., Parkes,M., Annese,V.,
            Hakonarson,H., Radford-Smith,G., Duerr,R.H., Vermeire,S.,
            Weersma,R.K. and Rioux,J.D.
  TITLE     Meta-analysis identifies 29 additional ulcerative colitis risk
            loci, increasing the number of confirmed associations to 47
  JOURNAL   Nat Genet 43 (3), 246-252 (2011)
   PUBMED   21297633
  REMARK    Erratum:[Nat Genet. 2011 Sep;43(9):919]
REFERENCE   9  (residues 1 to 663)
  AUTHORS   Franke,A., McGovern,D.P., Barrett,J.C., Wang,K.,
            Radford-Smith,G.L., Ahmad,T., Lees,C.W., Balschun,T., Lee,J.,
            Roberts,R., Anderson,C.A., Bis,J.C., Bumpstead,S., Ellinghaus,D.,
            Festen,E.M., Georges,M., Green,T., Haritunians,T., Jostins,L.,
            Latiano,A., Mathew,C.G., Montgomery,G.W., Prescott,N.J.,
            Raychaudhuri,S., Rotter,J.I., Schumm,P., Sharma,Y., Simms,L.A.,
            Taylor,K.D., Whiteman,D., Wijmenga,C., Baldassano,R.N., Barclay,M.,
            Bayless,T.M., Brand,S., Buning,C., Cohen,A., Colombel,J.F.,
            Cottone,M., Stronati,L., Denson,T., De Vos,M., D'Inca,R.,
            Dubinsky,M., Edwards,C., Florin,T., Franchimont,D., Gearry,R.,
            Glas,J., Van Gossum,A., Guthery,S.L., Halfvarson,J.,
            Verspaget,H.W., Hugot,J.P., Karban,A., Laukens,D., Lawrance,I.,
            Lemann,M., Levine,A., Libioulle,C., Louis,E., Mowat,C., Newman,W.,
            Panes,J., Phillips,A., Proctor,D.D., Regueiro,M., Russell,R.,
            Rutgeerts,P., Sanderson,J., Sans,M., Seibold,F., Steinhart,A.H.,
            Stokkers,P.C., Torkvist,L., Kullak-Ublick,G., Wilson,D.,
            Walters,T., Targan,S.R., Brant,S.R., Rioux,J.D., D'Amato,M.,
            Weersma,R.K., Kugathasan,S., Griffiths,A.M., Mansfield,J.C.,
            Vermeire,S., Duerr,R.H., Silverberg,M.S., Satsangi,J.,
            Schreiber,S., Cho,J.H., Annese,V., Hakonarson,H., Daly,M.J. and
            Parkes,M.
  TITLE     Genome-wide meta-analysis increases to 71 the number of confirmed
            Crohn's disease susceptibility loci
  JOURNAL   Nat Genet 42 (12), 1118-1125 (2010)
   PUBMED   21102463
REFERENCE   10 (residues 1 to 663)
  AUTHORS   Barrett,J.C., Lee,J.C., Lees,C.W., Prescott,N.J., Anderson,C.A.,
            Phillips,A., Wesley,E., Parnell,K., Zhang,H., Drummond,H.,
            Nimmo,E.R., Massey,D., Blaszczyk,K., Elliott,T., Cotterill,L.,
            Dallal,H., Lobo,A.J., Mowat,C., Sanderson,J.D., Jewell,D.P.,
            Newman,W.G., Edwards,C., Ahmad,T., Mansfield,J.C., Satsangi,J.,
            Parkes,M., Mathew,C.G., Donnelly,P., Peltonen,L., Blackwell,J.M.,
            Bramon,E., Brown,M.A., Casas,J.P., Corvin,A., Craddock,N.,
            Deloukas,P., Duncanson,A., Jankowski,J., Markus,H.S., Mathew,C.G.,
            McCarthy,M.I., Palmer,C.N., Plomin,R., Rautanen,A., Sawcer,S.J.,
            Samani,N., Trembath,R.C., Viswanathan,A.C., Wood,N., Spencer,C.C.,
            Barrett,J.C., Bellenguez,C., Davison,D., Freeman,C., Strange,A.,
            Donnelly,P., Langford,C., Hunt,S.E., Edkins,S., Gwilliam,R.,
            Blackburn,H., Bumpstead,S.J., Dronov,S., Gillman,M., Gray,E.,
            Hammond,N., Jayakumar,A., McCann,O.T., Liddle,J., Perez,M.L.,
            Potter,S.C., Ravindrarajah,R., Ricketts,M., Waller,M., Weston,P.,
            Widaa,S., Whittaker,P., Deloukas,P., Peltonen,L., Mathew,C.G.,
            Blackwell,J.M., Brown,M.A., Corvin,A., McCarthy,M.I., Spencer,C.C.,
            Attwood,A.P., Stephens,J., Sambrook,J., Ouwehand,W.H.,
            McArdle,W.L., Ring,S.M. and Strachan,D.P.
  CONSRTM   UK IBD Genetics Consortium; Wellcome Trust Case Control Consortium
            2
  TITLE     Genome-wide association study of ulcerative colitis identifies
            three new susceptibility loci, including the HNF4A region
  JOURNAL   Nat Genet 41 (12), 1330-1334 (2009)
   PUBMED   19915572
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP357953.1, AK001763.1, AK001583.1 and AC099756.2.
            
            On Nov 20, 2018 this sequence version replaced NP_060735.3.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK001763.1, SRR7346977.1767260.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..663
                     /product="innate immunity activator protein isoform 1"
                     /note="uncharacterized protein C1orf106; innate immunity
                     activator protein"
                     /calculated_mol_wt=72783
     Region          1..68
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          87..216
                     /region_name="CUPID"
                     /note="Cytohesin Ubiquitin Protein Inducing Domain;
                     pfam11819"
                     /db_xref="CDD:463360"
     Region          164..170
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000269|PubMed:28436939"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          242..362
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          332..338
                     /region_name="Nuclear localization signal (NLS) 2.
                     /evidence=ECO:0000269|PubMed:28436939"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          378..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          422..428
                     /region_name="Nuclear localization signal (NLS) 3.
                     /evidence=ECO:0000269|PubMed:28436939"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     Region          444..493
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3KP66.2)"
     CDS             1..663
                     /gene="INAVA"
                     /gene_synonym="C1orf106"
                     /coded_by="NM_018265.4:11..2002"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:55765"
                     /db_xref="HGNC:HGNC:25599"
                     /db_xref="MIM:618051"
ORIGIN      
        1 mlqmpklnei ppgragrrea rgegrwpgqt gpeaarlewr aqgqaggara pwdswgssrl
       61 ptqpgpgwsr cppsllcals fqkstmeskd evsdtdsgii lqsgpdspvs pmkelthavh
      121 kqqralearl eacleelrrl clreaeltgt lpaeyplkpg ekapkvrrri gaayklddwa
      181 lhredplssl erqlalqlqi teaarrlcle enlsrqarrq rkhsmlqeek klqelqrclv
      241 errrnseppp aaalplgrel sasddsslsd gllleeeesq vpkpppespa ppsrplppqt
      301 leglqptgpe agsperapvq nspwketsld hpyekprkss epwsessspa ttpqdgpsas
      361 slwllepasy hvvpirgvpg qwqgrtsapa tpeiqgrrgq sqslrvdsfr agpegrgrsa
      421 fprrrpthyt vtvpdscfpa tkpplphaac hscsedsgsd vssishptsp gssspdisfl
      481 qplsppkthr hrgawvpags relvahhpkl llppgyfpag ryvvvaespl ppgewelrra
      541 apgpayeeeg tplryqrlvp srsrivrtps lkdspagrgl skaavseelk wwherarlrs
      601 trphsldrqg afrvrslplg regfgralgp raqvptvcvl rrspdgapvq vfvpekgeii
      661 sqv
//
LOCUS       NP_004078                926 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 2 [Homo sapiens].
ACCESSION   NP_004078
VERSION     NP_004078.2
DBSOURCE    REFSEQ: accession NM_004087.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 926)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 926)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 926)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 926)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 926)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 926)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 926)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 926)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 926)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 926)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8, U13896.1 and
            AC068302.18.
            
            On Jun 2, 2007 this sequence version replaced NP_004078.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Transcript Variant: This variant (2) contains an alternate in-frame
            coding exon compared to variant 1, resulting in a longer isoform
            (2) compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U13896.1, BC140841.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..926
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..926
                     /product="disks large homolog 1 isoform 2"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=103190
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..223
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          222..310
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(233..239,256,259,289,293,296..297)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          319..403
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(328..334,351,354,384,388,391..392)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          404..465
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          463..553
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(475..481,492,495,525,529,532..533)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          582..648
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(587,609..610,631)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(590,592,595,604,622..623,642,644..645)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          735..913
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..926
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_004087.2:191..2971"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS3327.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kpteavlpsp ptvpvipvlp
      181 vpaentvilp tipqanpppv lvntdsletp tyvngtdady eyeeitlerg nsglgfsiag
      241 gtdnphigdd ssifitkiit ggaaaqdgrl rvndcilrvn evdvrdvths kavealkeag
      301 sivrlyvkrr kpvsekimei klikgpkglg fsiaggvgnq hipgdnsiyv tkiieggaah
      361 kdgklqigdk llavnnvcle evtheeavta lkntsdfvyl kvakptsmym ndgyappdit
      421 nsssqpvdnh vspssflgqt pasparyspv skavlgddei treprkvvlh rgstglgfni
      481 vggedgegif isfilaggpa dlsgelrkgd riisvnsvdl raasheqaaa alknagqavt
      541 ivaqyrpeey srfeakihdl reqmmnssis sgsgslrtsq krslyvralf dydktkdsgl
      601 psqglnfkfg dilhvinasd dewwqarqvt pdgesdevgv ipskrrvekk erarlktvkf
      661 nsktrdkgqs fndkrkknlf srkfpfyknk dqseqetsda dqhvtsnasd sessyrgqee
      721 yvlsyepvnq qevnytrpvi ilgpmkdrin ddlisefpdk fgscvphttr pkrdyevdgr
      781 dyhfvtsreq mekdiqehkf ieagqynnhl ygtsvqsvre vaekgkhcil dvsgnaikrl
      841 qiaqlypisi fikpksmeni memnkrltee qarktferam kleqeftehf taivqgdtle
      901 diynqvkqii eeqsgsyiwv pakekl
//
LOCUS       NP_001278510             819 aa            linear   PRI 20-NOV-2025
DEFINITION  rab GTPase-binding effector protein 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001278510
VERSION     NP_001278510.1
DBSOURCE    REFSEQ: accession NM_001291581.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Swanton,E., Bishop,N. and Woodman,P.
  TITLE     Human rabaptin-5 is selectively cleaved by caspase-3 during
            apoptosis
  JOURNAL   J Biol Chem 274 (53), 37583-37590 (1999)
   PUBMED   10608812
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Neve,R.L., Coopersmith,R., McPhie,D.L., Santeufemio,C., Pratt,K.G.,
            Murphy,C.J. and Lynn,S.D.
  TITLE     The neuronal growth-associated protein GAP-43 interacts with
            rabaptin-5 and participates in endocytosis
  JOURNAL   J Neurosci 18 (19), 7757-7767 (1998)
   PUBMED   9742146
REFERENCE   8  (residues 1 to 819)
  AUTHORS   Vitale,G., Rybin,V., Christoforidis,S., Thornqvist,P.,
            McCaffrey,M., Stenmark,H. and Zerial,M.
  TITLE     Distinct Rab-binding domains mediate the interaction of Rabaptin-5
            with GTP-bound Rab4 and Rab5
  JOURNAL   EMBO J 17 (7), 1941-1951 (1998)
   PUBMED   9524117
REFERENCE   9  (residues 1 to 819)
  AUTHORS   Xiao,G.H., Shoarinejad,F., Jin,F., Golemis,E.A. and Yeung,R.S.
  TITLE     The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5
            GTPase activating protein (GAP) in modulating endocytosis
  JOURNAL   J Biol Chem 272 (10), 6097-6100 (1997)
   PUBMED   9045618
REFERENCE   10 (residues 1 to 819)
  AUTHORS   Stenmark,H., Vitale,G., Ullrich,O. and Zerial,M.
  TITLE     Rabaptin-5 is a direct effector of the small GTPase Rab5 in
            endocytic membrane fusion
  JOURNAL   Cell 83 (3), 423-432 (1995)
   PUBMED   8521472
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB169027.1, AK297535.1, BC041700.1, AK314183.1, AF098638.1,
            DB124187.1, AL157499.1, EB387308.1 and BM678290.1.
            
            Transcript Variant: This variant (3) lacks an alternate in-frame
            exon in the 5' coding region, compared to variant 1, resulting in
            an isoform (3) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.4827.1,
                                           SRR1660807.146879.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13.2"
     Protein         1..819
                     /product="rab GTPase-binding effector protein 1 isoform 3"
                     /note="rab GTPase-binding effector protein 1; rabaptin-5;
                     neurocrescin; rabaptin-4; rabaptin-5alpha; renal carcinoma
                     antigen NY-REN-17"
                     /calculated_mol_wt=93984
     Region          11..452
                     /region_name="Rabaptin"
                     /note="pfam03528"
                     /db_xref="CDD:367545"
     Region          490..796
                     /region_name="Rab5-bind"
                     /note="Rabaptin-like protein; pfam09311"
                     /db_xref="CDD:462752"
     CDS             1..819
                     /gene="RABEP1"
                     /gene_synonym="RAB5EP; RABPT5"
                     /coded_by="NM_001291581.2:204..2663"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:9135"
                     /db_xref="HGNC:HGNC:17677"
                     /db_xref="MIM:603616"
ORIGIN      
        1 maqpgpasqp dedlkrqnav lqaaqddlgh lrtqlweaqa emenikaiat vsentkqeai
       61 devkrqwree vaslqavmke tvrdyehqfh lrleqertqw aqyresaere iadlrrrlse
      121 gqeeenlene mkkaqedaek lrsvvmpmek eiaalkdklt eaedkikele askvkelnhy
      181 leaekscrtd lemyvavlnt qksvlqedae klrkelhevc hlleqerqqh nqlkhtwqka
      241 ndqflesqrl lmrdmqrmei vltseqlrqv eelkkkdqed deqqrlnkrk dhkkadveee
      301 ikipvvcalt qeessaqlsn eeehldstrg svhsldagll lpsgdpfsks dndmfkdglr
      361 raqstdslgt sgslqskalg ynykaksagn ldesdfgplv gadsvsenfd taslgslqmp
      421 sgfmltkdqe raikamtpeq eetasllssv tqgmesayvs psgyrlvset ewnllqkevh
      481 nagnklgrrc dmcsnyekql qgiqiqeaet rdqvkklqlm lrqandqlek tmkdkqeled
      541 fikqssedss hqisalvlra qaseilleel qqglsqakrd vqeqmavlmq sreqvseelv
      601 rlqkdndslq gkhslhvslq qaedfilpdt tealrelvlk yrediinvrt aadhveeklk
      661 aeilflkeqi qaeqclkenl eetlqleien ckeeiasiss lkaelerikv ekgqlestlr
      721 eksqqleslq eikisleeql kketaakatv eqlmfeeknk aqrlqteldv seqvqrdfvk
      781 lsqtlqvqle rirqadsler irailndtkl tdinqlpet
//
LOCUS       NP_006471                566 aa            linear   PRI 20-NOV-2025
DEFINITION  regulator of G-protein signaling 14 isoform 1 [Homo sapiens].
ACCESSION   NP_006471
VERSION     NP_006471.2
DBSOURCE    REFSEQ: accession NM_006480.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 566)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 566)
  AUTHORS   Sneddon,W.B., Ramineni,S., Van Doorn,G.E., Hepler,J.R. and
            Friedman,P.A.
  TITLE     Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport
  JOURNAL   Biochem Biophys Res Commun 733, 150700 (2024)
   PUBMED   39293332
  REMARK    GeneRIF: Distinct and overlapping RGS14 and RGS12 actions regulate
            NPT2A-mediated phosphate transport.
REFERENCE   3  (residues 1 to 566)
  AUTHORS   Wang,J., Guo,Y., He,Y., Qin,Y., Li,X., Yang,L., Liu,K. and Xiao,L.
  TITLE     Hepatic regulator of G protein signaling 14 ameliorates NAFLD
            through activating cAMP-AMPK signaling by targeting Gialpha1/3
  JOURNAL   Mol Metab 80, 101882 (2024)
   PUBMED   38237897
  REMARK    GeneRIF: Hepatic regulator of G protein signaling 14 ameliorates
            NAFLD through activating cAMP-AMPK signaling by targeting
            Gialpha1/3.
REFERENCE   4  (residues 1 to 566)
  AUTHORS   Montanez-Miranda,C., Bramlett,S.N. and Hepler,J.R.
  TITLE     RGS14 expression in CA2 hippocampus, amygdala, and basal ganglia:
            Implications for human brain physiology and disease
  JOURNAL   Hippocampus 33 (3), 166-181 (2023)
   PUBMED   36541898
  REMARK    GeneRIF: RGS14 expression in CA2 hippocampus, amygdala, and basal
            ganglia: Implications for human brain physiology and disease.
            Review article
REFERENCE   5  (residues 1 to 566)
  AUTHORS   Friedman,P.A., Sneddon,W.B., Mamonova,T., Montanez-Miranda,C.,
            Ramineni,S., Harbin,N.H., Squires,K.E., Gefter,J.V., Magyar,C.E.,
            Emlet,D.R. and Hepler,J.R.
  TITLE     RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated renal
            phosphate uptake via binding to the NHERF1 scaffolding protein
  JOURNAL   J Biol Chem 298 (5), 101836 (2022)
   PUBMED   35307350
  REMARK    GeneRIF: RGS14 regulates PTH- and FGF23-sensitive NPT2A-mediated
            renal phosphate uptake via binding to the NHERF1 scaffolding
            protein.
REFERENCE   6  (residues 1 to 566)
  AUTHORS   Sierra,D.A., Gilbert,D.J., Householder,D., Grishin,N.V., Yu,K.,
            Ukidwe,P., Barker,S.A., He,W., Wensel,T.G., Otero,G., Brown,G.,
            Copeland,N.G., Jenkins,N.A. and Wilkie,T.M.
  TITLE     Evolution of the regulators of G-protein signaling multigene family
            in mouse and human
  JOURNAL   Genomics 79 (2), 177-185 (2002)
   PUBMED   11829488
REFERENCE   7  (residues 1 to 566)
  AUTHORS   Kimple,R.J., De Vries,L., Tronchere,H., Behe,C.I., Morris,R.A.,
            Gist Farquhar,M. and Siderovski,D.P.
  TITLE     RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
            guanine nucleotide dissociation inhibitor Activity
  JOURNAL   J Biol Chem 276 (31), 29275-29281 (2001)
   PUBMED   11387333
REFERENCE   8  (residues 1 to 566)
  AUTHORS   Cho,H., Kozasa,T., Takekoshi,K., De Gunzburg,J. and Kehrl,J.H.
  TITLE     RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha-
            and G13alpha-mediated signaling pathways
  JOURNAL   Mol Pharmacol 58 (3), 569-576 (2000)
   PUBMED   10953050
REFERENCE   9  (residues 1 to 566)
  AUTHORS   Traver,S., Bidot,C., Spassky,N., Baltauss,T., De Tand,M.F.,
            Thomas,J.L., Zalc,B., Janoueix-Lerosey,I. and Gunzburg,J.D.
  TITLE     RGS14 is a novel Rap effector that preferentially regulates the
            GTPase activity of galphao
  JOURNAL   Biochem J 350 Pt 1 (Pt 1), 19-29 (2000)
   PUBMED   10926822
REFERENCE   10 (residues 1 to 566)
  AUTHORS   Snow,B.E., Antonio,L., Suggs,S., Gutstein,H.B. and Siderovski,D.P.
  TITLE     Molecular cloning and expression analysis of rat Rgs12 and Rgs14
  JOURNAL   Biochem Biophys Res Commun 233 (3), 770-777 (1997)
   PUBMED   9168931
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014094.2.
            
            On Jun 10, 2002 this sequence version replaced NP_006471.1.
            
            Summary: This gene encodes a member of the regulator of G-protein
            signaling family. This protein contains one RGS domain, two
            Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The
            protein attenuates the signaling activity of G-proteins by binding,
            through its GoLoco domain, to specific types of activated,
            GTP-bound G alpha subunits. Acting as a GTPase activating protein
            (GAP), the protein increases the rate of conversion of the GTP to
            GDP. This hydrolysis allows the G alpha subunits to bind G
            beta/gamma subunit heterodimers, forming inactive G-protein
            heterotrimers, thereby terminating the signal. Alternate
            transcriptional splice variants of this gene have been observed but
            have not been thoroughly characterized. [provided by RefSeq, Jul
            2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014094.2, SRR1660809.255985.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA2145893
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000408923.8/ ENSP00000386229.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..566
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..566
                     /product="regulator of G-protein signaling 14 isoform 1"
                     /calculated_mol_wt=61316
     Region          19..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            45
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          58..186
                     /region_name="RGS_RGS14"
                     /note="Regulator of G protein signaling (RGS) domain found
                     in the RGS14 protein; cd08743"
                     /db_xref="CDD:188697"
     Site            order(88..90,92..93,130..135,137..138,165,167..169,173)
                     /site_type="other"
                     /note="putative G-alpha-3 interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:188697"
     Region          192..243
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P97492; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            203
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            218
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O08773; propagated from
                     UniProtKB/Swiss-Prot (O43566.4)"
     Region          299..425
                     /region_name="Necessary for interaction with RABGEF1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Region          302..371
                     /region_name="RBD1_RGS14"
                     /note="Ras-binding domain (RBD) 1 of regulator of G
                     protein signaling 14 (RGS14); cd17137"
                     /db_xref="CDD:340657"
     Site            order(334,351)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340657"
     Region          372..443
                     /region_name="RBD2_RGS14"
                     /note="Ras-binding domain (RBD) 2 of regulator of G
                     protein signaling 14 (RGS14); cd17139"
                     /db_xref="CDD:340659"
     Site            order(384,406)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340659"
     Region          451..490
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     Region          499..520
                     /region_name="GoLoco"
                     /note="GoLoco motif; pfam02188"
                     /db_xref="CDD:460481"
     Region          530..566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O43566.4)"
     CDS             1..566
                     /gene="RGS14"
                     /coded_by="NM_006480.5:102..1802"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43405.1"
                     /db_xref="GeneID:10636"
                     /db_xref="HGNC:HGNC:9996"
                     /db_xref="MIM:602513"
ORIGIN      
        1 mpgkpkhlgv pngrmvlavs dgelssttgp qgqgegrgss lsihslpsgp sspfpteeqp
       61 vaswalsfer llqdplglay fteflkkefs aenvtfwkac erfqqipasd tqqlaqearn
      121 iyqeflssqa lspvnidrqa wlgeevlaep rpdmfraqql qifnlmkfds yarfvksply
      181 recllaeaeg rplrepgssr lgspdatrkk pklkpgkslp lgveelgqlp pvegpggrpl
      241 rksfrrelgg tanaalrres qgslnssasl dlgflafvss kseshrkslg stegesesrp
      301 gkyccvylpd gtaslalarp gltirdmlag icekrglslp dikvylvgne qalvldqdct
      361 vladqevrle nritfelelt alervvrisa kptkrlqeal qpilekhgls plevvlhrpg
      421 ekqpldlgkl vssvaaqrlv ldtlpgvkis kardkspcrs qgcpprtqdk athpppasps
      481 slvkvpssat gkrqtcdieg lvellnrvqs sgahdqrgll rkedlvlpef lqlpaqgpss
      541 eetppqtksa aqpiggslns ttdsal
//
LOCUS       NP_001230447             470 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 6 [Homo sapiens].
ACCESSION   NP_001230447
VERSION     NP_001230447.1
DBSOURCE    REFSEQ: accession NM_001243518.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC064700.1, AB020639.1 and
            BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (16) has an additional exon in the
            5' region, which includes an AUG start codon, and an additional
            segment in the middle region, compared to variant 1. The resulting
            isoform (6) has a longer and distinct N-terminus and an additional
            internal segment, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC064700.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..470
                     /product="estrogen-related receptor gamma isoform 6"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=52332
     Region          127..223
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(131,143..146,151..152,154..156,158..159,162,
                     182..183,186,189,203..204,207..214)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(133,136,150,153,169,175,185,188)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          249..468
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(277,280,284,287,325,338,342,352..354,447,450,452)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(292,306,309..310,313..314,460..461,464..465)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            388
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..470
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243518.2:244..1656"
                     /note="isoform 6 is encoded by transcript variant 16"
                     /db_xref="CCDS:CCDS58061.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 mwrecdwglg avksdlacvp sakrllcrms nkdrhidssc ssfiktepss pasltdsvnh
       61 hspggssdas gsysstmngh qngldspply psapilggsg pvrklyddcs stivedpqtk
      121 ceymlnsmpk rlclvcgdia sgyhygvasc eackaffkrt iqgnieyscp atneceitkr
      181 rrkscqacrf mkclkvgmlk egvrldrvrg grqkykrrid aenspylnpq lvqpakkpll
      241 wsdpadnkiv shllvaepek iyampdptvp dsdikalttl cdladrelvv iigwakhipg
      301 fstlsladqm sllqsawmei lilgvvyrsl sfedelvyad dyimdedqsk laglldlnna
      361 ilqlvkkyks mklekeefvt lkaialansd smhiedveav qklqdvlhea lqdyeagqhm
      421 edprragkml mtlpllrqts tkavqhfyni klegkvpmhk lflemleakv
//
LOCUS       NP_001290038             467 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 12 isoform 3 [Homo sapiens].
ACCESSION   NP_001290038
VERSION     NP_001290038.1
DBSOURCE    REFSEQ: accession NM_001303109.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Lee,K.T., Pranoto,I.K.A., Kim,S.Y., Choi,H.J., To,N.B., Chae,H.,
            Lee,J.Y., Kim,J.E., Kwon,Y.V. and Nam,J.W.
  TITLE     Comparative interactome analysis of alpha-arrestin families in
            human and Drosophila
  JOURNAL   Elife 12, 88328 (2024)
   PUBMED   38270169
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Rondou,P., Haegeman,G., Vanhoenacker,P. and Van Craenenbroeck,K.
  TITLE     BTB Protein KLHL12 targets the dopamine D4 receptor for
            ubiquitination by a Cul3-based E3 ligase
  JOURNAL   J Biol Chem 283 (17), 11083-11096 (2008)
   PUBMED   18303015
  REMARK    GeneRIF: KLHL12 specifically interacts with the D4 polymorphism,
            thereby building up a Cul3-E3 ligase complex with substrate
            specificity toward the D4 receptor
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Sumara,I., Quadroni,M., Frei,C., Olma,M.H., Sumara,G., Ricci,R. and
            Peter,M.
  TITLE     A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes,
            regulating mitotic progression and completion of cytokinesis in
            human cells
  JOURNAL   Dev Cell 12 (6), 887-900 (2007)
   PUBMED   17543862
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Angers,S., Thorpe,C.J., Biechele,T.L., Goldenberg,S.J., Zheng,N.,
            MacCoss,M.J. and Moon,R.T.
  TITLE     The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the
            Wnt-beta-catenin pathway by targeting Dishevelled for degradation
  JOURNAL   Nat Cell Biol 8 (4), 348-357 (2006)
   PUBMED   16547521
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Uchida,K., Akita,Y., Matsuo,K., Fujiwara,S., Nakagawa,A.,
            Kazaoka,Y., Hachiya,H., Naganawa,Y., Oh-Iwa,I., Ohura,K., Saga,S.,
            Kawai,T., Matsumoto,Y., Shimozato,K. and Kozaki,K.
  TITLE     Identification of specific autoantigens in Sjogren's syndrome by
            SEREX
  JOURNAL   Immunology 116 (1), 53-63 (2005)
   PUBMED   16108817
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Mai,A., Jung,S.K. and Yonehara,S.
  TITLE     hDKIR, a human homologue of the Drosophila kelch protein, involved
            in a ring-like structure
  JOURNAL   Exp Cell Res 300 (1), 72-83 (2004)
   PUBMED   15383316
  REMARK    GeneRIF: molecular cloning and characterization of a novel gene,
            encoded a human kelch protein containing 568 amino acid residues,
            termed hDKIR.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK027656.1, AF306689.1,
            AK301791.1 and AK024412.1.
            
            Summary: This gene encodes a member of the KLHL (Kelch-like) family
            of proteins. This protein has been identified as an autoantigen in
            the autoimmune disease Sjogren's syndrome and as a potential
            biomarker in primary biliary cirrhosis. This protein may act as a
            substrate adaptor of the Cullin-3 ubiquitin ligase complex to
            promote substrate-specific ubiquitylation. Ubiquitylation by this
            complex has been shown to regulate the Wnt signaling pathway as
            well as COPII vesicle coat size. A pseudogene has been identified
            on chromosome 22. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (3) uses an alternate 5' terminal
            exon, resulting in a distinct 5' UTR and an in-frame downstream
            translational start site, and lacks two alternate internal exons in
            the 3' coding region, compared to variant 1. This results in
            isoform 3, which is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.104813.1,
                                           SRR1803615.248301.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32.1"
     Protein         1..467
                     /product="kelch-like protein 12 isoform 3"
                     /note="kelch-like protein C3IP1; CUL3-interacting protein
                     1; DKIR homolog"
                     /calculated_mol_wt=52065
     Region          12..135
                     /region_name="BTB_POZ_KLHL12_C3IP1_DKIR"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 12 (KLHL12); cd18242"
                     /db_xref="CDD:349551"
     Region          130..265
                     /region_name="BACK_KLHL12"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 12 (KLHL12); cd18452"
                     /db_xref="CDD:350527"
     Region          278..464
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          315..358
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          362..406
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          409..454
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..467
                     /gene="KLHL12"
                     /gene_synonym="C3IP1; DKIR"
                     /coded_by="NM_001303109.2:192..1595"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:59349"
                     /db_xref="HGNC:HGNC:19360"
                     /db_xref="MIM:614522"
ORIGIN      
        1 mggimapkdi mtnthaksil nsmnslrksn tlcdvtlrve qkdfpahriv laacsdyfca
       61 mftselsekg kpyvdiqglt astmeilldf vytetvhvtv envqellpaa cllqlkgvkq
      121 acceflesql dpsnclgird faethncvdl mqaaevfsqk hfpevvqhee fillsqgeve
      181 klikcdeiqv dseepvfeav inwvkhakke reeslpnllq yvrmplltpr yitdvidaep
      241 fircslqcrd lvdeakkfhl rpelrsqmqg prtrarldmi yvsggfdgsr rhtsmerydp
      301 nidqwsmlgd mqtaregagl vvasgviycl ggydglniln svekydphtg hwtnvtpmat
      361 krsgagvall ndhiyvvggf dgtahlssve aynirtdswt tvtsmttprc yvgatvlrgr
      421 lyaiagydgn sllssiecyd piidswevvt smgtqrcdag vcvlrek
//
LOCUS       NP_001350076             525 aa            linear   PRI 20-NOV-2025
DEFINITION  methylcrotonoyl-CoA carboxylase beta chain, mitochondrial isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_001350076 XP_005248624
VERSION     NP_001350076.1
DBSOURCE    REFSEQ: accession NM_001363147.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   He,J., Yi,J., Ji,L., Dai,L., Chen,Y. and Xue,W.
  TITLE     ECHDC2 inhibits the proliferation of gastric cancer cells by
            binding with NEDD4 to degrade MCCC2 and reduce aerobic glycolysis
  JOURNAL   Mol Med 30 (1), 69 (2024)
   PUBMED   38783226
  REMARK    GeneRIF: ECHDC2 inhibits the proliferation of gastric cancer cells
            by binding with NEDD4 to degrade MCCC2 and reduce aerobic
            glycolysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Liu,W., Chen,S., Xie,W., Wang,Q., Luo,Q., Huang,M., Gu,M., Lan,P.
            and Chen,D.
  TITLE     MCCC2 is a novel mediator between mitochondria and telomere and
            functions as an oncogene in colorectal cancer
  JOURNAL   Cell Mol Biol Lett 28 (1), 80 (2023)
   PUBMED   37828426
  REMARK    GeneRIF: MCCC2 is a novel mediator between mitochondria and
            telomere and functions as an oncogene in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Lim,S.H., Snider,J., Birimberg-Schwartz,L., Ip,W., Serralha,J.C.,
            Botelho,H.M., Lopes-Pacheco,M., Pinto,M.C., Moutaoufik,M.T.,
            Zilocchi,M., Laselva,O., Esmaeili,M., Kotlyar,M., Lyakisheva,A.,
            Tang,P., Lopez Vazquez,L., Akula,I., Aboualizadeh,F., Wong,V.,
            Grozavu,I., Opacak-Bernardi,T., Yao,Z., Mendoza,M., Babu,M.,
            Jurisica,I., Gonska,T., Bear,C.E., Amaral,M.D. and Stagljar,I.
  TITLE     CFTR interactome mapping using the mammalian membrane two-hybrid
            high-throughput screening system
  JOURNAL   Mol Syst Biol 18 (2), e10629 (2022)
   PUBMED   35156780
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Holzinger,A., Roschinger,W., Lagler,F., Mayerhofer,P.U.,
            Lichtner,P., Kattenfeld,T., Thuy,L.P., Nyhan,W.L., Koch,H.G.,
            Muntau,A.C. and Roscher,A.A.
  TITLE     Cloning of the human MCCA and MCCB genes and mutations therein
            reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase
            deficiency
  JOURNAL   Hum Mol Genet 10 (12), 1299-1306 (2001)
   PUBMED   11406611
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Obata,K., Fukuda,T., Morishita,R., Abe,S., Asakawa,S.,
            Yamaguchi,S., Yoshino,M., Ihara,K., Murayama,K., Shigemoto,K.,
            Shimizu,N. and Kondo,I.
  TITLE     Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
            gene (MCCA): cDNA sequence, genomic organization, localization to
            chromosomal band 3q27, and expression
  JOURNAL   Genomics 72 (2), 145-152 (2001)
   PUBMED   11401427
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Baumgartner,M.R., Almashanu,S., Suormala,T., Obie,C., Cole,R.N.,
            Packman,S., Baumgartner,E.R. and Valle,D.
  TITLE     The molecular basis of human 3-methylcrotonyl-CoA carboxylase
            deficiency
  JOURNAL   J Clin Invest 107 (4), 495-504 (2001)
   PUBMED   11181649
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Gallardo,M.E., Desviat,L.R., Rodriguez,J.M., Esparza-Gordillo,J.,
            Perez-Cerda,C., Perez,B., Rodriguez-Pombo,P., Criado,O., Sanz,R.,
            Morton,D.H., Gibson,K.M., Le,T.P., Ribes,A., de Cordoba,S.R.,
            Ugarte,M. and Penalva,M.A.
  TITLE     The molecular basis of 3-methylcrotonylglycinuria, a disorder of
            leucine catabolism
  JOURNAL   Am J Hum Genet 68 (2), 334-346 (2001)
   PUBMED   11170888
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Gibson,K.M., Bennett,M.J., Naylor,E.W. and Morton,D.H.
  TITLE     3-Methylcrotonyl-coenzyme A carboxylase deficiency in
            Amish/Mennonite adults identified by detection of increased
            acylcarnitines in blood spots of their children
  JOURNAL   J Pediatr 132 (3 Pt 1), 519-523 (1998)
   PUBMED   9544913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC138832.2 and AC143336.1.
            
            On May 9, 2018 this sequence version replaced XP_005248624.1.
            
            Summary: This gene encodes the small subunit of
            3-methylcrotonyl-CoA carboxylase. This enzyme functions as a
            heterodimer and catalyzes the carboxylation of 3-methylcrotonyl-CoA
            to form 3-methylglutaconyl-CoA. Mutations in this gene are
            associated with 3-Methylcrotonylglycinuria, an autosomal recessive
            disorder of leucine catabolism. Alternative splicing results in
            multiple transcript variants encoding distinct isoforms. [provided
            by RefSeq, May 2018].
            
            Transcript Variant: This variant (2) lacks an in-frame exon
            compared to variant 1 and encodes a shorter isoform (2) compared to
            isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.155055.1,
                                           SRR1803617.244069.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..525
                     /product="methylcrotonoyl-CoA carboxylase beta chain,
                     mitochondrial isoform 2 precursor"
                     /EC_number="6.4.1.4"
                     /note="biotin carboxylase; methylcrotonoyl-Coenzyme A
                     carboxylase 2 (beta); non-biotin containing subunit of
                     3-methylcrotonyl-CoA carboxylase; methylcrotonoyl-CoA
                     carboxylase beta chain, mitochondrial; MCCase subunit
                     beta; 3-methylcrotonyl-CoA carboxylase 2;
                     3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
                     3-methylcrotonyl-CoA carboxylase non-biotin-containing
                     subunit; methylcrotonoyl-CoA carboxylase 2 (beta);
                     testicular secretory protein Li 29"
                     /calculated_mol_wt=57388
     Region          36..525
                     /region_name="Carboxyl_trans"
                     /note="Carboxyl transferase domain; cl47203"
                     /db_xref="CDD:481543"
     CDS             1..525
                     /gene="MCCC2"
                     /gene_synonym="MCCB; MCCCbeta"
                     /coded_by="NM_001363147.1:87..1664"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS93731.1"
                     /db_xref="GeneID:64087"
                     /db_xref="HGNC:HGNC:6937"
                     /db_xref="MIM:609014"
ORIGIN      
        1 mwavlrlalr pcaraspagp rayhgdsvas lgtqpdlgsa lyqenykqmk alvnqlherv
       61 ehiklgggek aralhisrgk llpreridnl idpgspflel sqfagyqlyd neevpgggii
      121 tgigrvsgve cmiiandatv kggayypvtv kkqlraqeia mqnrlpciyl vdsggaylpr
      181 qadvfpdrdh fgrtfynqai msskniaqvk aatgeevsae dlggadlhcr ksgvsdhwal
      241 ddhhalhltr kvvrnlnyqk kldvtiepse eplfpadely givganlkrs fdvreviari
      301 vdgsrftefk afygdtlvtg farifgypvg ivgnngvlfs esakkgthfv qlccqrnipl
      361 lflqnitgfm vgreyeaegi akdgakmvaa vacaqvpkit liiggsygag nygmcgrays
      421 prflyiwpna risvmggeqa anvlatitkd qraregkqfs sadeaalkep iikkfeeegn
      481 pyyssarvwd dgiidpadtr lvlglsfsaa lnapiektdf gifrm
//
LOCUS       NP_001191315             892 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 3 [Homo sapiens].
ACCESSION   NP_001191315
VERSION     NP_001191315.1
DBSOURCE    REFSEQ: accession NM_001204386.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 892)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 892)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 892)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 892)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 892)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 892)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 892)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 892)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 892)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 892)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U13897.1, BC144651.1,
            AK293967.1, BM728664.1, EF553524.1, AC068302.18, BC042118.1,
            AI223994.1 and AA837080.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Transcript Variant: This variant (3) is missing an in-frame coding
            exon, and contains an alternate in-frame coding exon compared to
            variant 1. This results in a shorter isoform (3) compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144651.1, SRR11853564.20532.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            regulatory uORF :: PMID: 21595829
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..892
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..892
                     /product="disks large homolog 1 isoform 3"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=99683
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          701..879
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..892
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001204386.1:191..2869"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS75072.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgsfndk rkknlfsrkf pfyknkdqse
      661 qetsdadqhv tsnasdsess yrgqeeyvls yepvnqqevn ytrpviilgp mkdrinddli
      721 sefpdkfgsc vphttrpkrd yevdgrdyhf vtsreqmekd iqehkfieag qynnhlygts
      781 vqsvrevaek gkhcildvsg naikrlqiaq lypisifikp ksmenimemn krlteeqark
      841 tferamkleq eftehftaiv qgdtlediyn qvkqiieeqs gsyiwvpake kl
//
LOCUS       NP_733821                664 aa            linear   PRI 20-NOV-2025
DEFINITION  lamin isoform A [Homo sapiens].
ACCESSION   NP_733821
VERSION     NP_733821.1
DBSOURCE    REFSEQ: accession NM_170707.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 664)
  AUTHORS   McClintock,D., Ratner,D., Lokuge,M., Owens,D.M., Gordon,L.B.,
            Collins,F.S. and Djabali,K.
  TITLE     The mutant form of lamin A that causes Hutchinson-Gilford progeria
            is a biomarker of cellular aging in human skin
  JOURNAL   PLoS One 2 (12), e1269 (2007)
   PUBMED   18060063
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 664)
  AUTHORS   Scaffidi,P. and Misteli,T.
  TITLE     Lamin A-dependent nuclear defects in human aging
  JOURNAL   Science 312 (5776), 1059-1063 (2006)
   PUBMED   16645051
  REMARK    GeneRIF: observations implicate lamin A in physiological aging
REFERENCE   3  (residues 1 to 664)
  AUTHORS   De Sandre-Giovannoli,A., Bernard,R., Cau,P., Navarro,C., Amiel,J.,
            Boccaccio,I., Lyonnet,S., Stewart,C.L., Munnich,A., Le Merrer,M.
            and Levy,N.
  TITLE     Lamin a truncation in Hutchinson-Gilford progeria
  JOURNAL   Science 300 (5628), 2055 (2003)
   PUBMED   12702809
  REMARK    GeneRIF: Hutchinson-Gilford progeria appears to represent a novel
            laminopathy, caused by a single heterozygous splicing mutation in
            the LMNA gene, leading to a major loss of Lamin A expression,
            intimately associated to nuclear alterations
REFERENCE   4  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     LMNA-Related Dilated Cardiomyopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301717
REFERENCE   5  (residues 1 to 664)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
REFERENCE   6  (residues 1 to 664)
  AUTHORS   Pegoraro,E. and Hoffman,E.P.
  TITLE     Limb-Girdle Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301582
REFERENCE   7  (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   8  (residues 1 to 664)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   9  (residues 1 to 664)
  AUTHORS   Sparks,S.E., Quijano-Roy,S., Harper,A., Rutkowski,A., Gordon,E.,
            Hoffman,E.P. and Pegoraro,E.
  TITLE     Congenital Muscular Dystrophy Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301468
REFERENCE   10 (residues 1 to 664)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   11 (residues 1 to 664)
  AUTHORS   Gordon,L.B., Brown,W.T. and Collins,F.S.
  TITLE     Hutchinson-Gilford Progeria Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301300
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG822820.1, BC014507.1,
            AL135927.14 and AI872233.1.
            
            Summary: The protein encoded by this gene is part of the nuclear
            lamina, a two-dimensional matrix of proteins located next to the
            inner nuclear membrane. The lamin family of proteins make up the
            matrix and are highly conserved in evolution. During mitosis, the
            lamina matrix is reversibly disassembled as the lamin proteins are
            phosphorylated. Lamin proteins are thought to be involved in
            nuclear stability, chromatin structure and gene expression.
            Vertebrate lamins consist of two types, A and B. Alternative
            splicing results in multiple transcript variants. Mutations in this
            gene lead to several diseases: Emery-Dreifuss muscular dystrophy,
            familial partial lipodystrophy, limb girdle muscular dystrophy,
            dilated cardiomyopathy, Charcot-Marie-Tooth disease, and
            Hutchinson-Gilford progeria syndrome. [provided by RefSeq, May
            2022].
            
            Transcript Variant: This variant (1) encodes isoform A.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK026584.1, SRR11853563.2122.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368300.9/ ENSP00000357283.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..664
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     Protein         1..664
                     /product="lamin isoform A"
                     /note="lamin A/C-like 1; 70 kDa lamin; prelamin-A/C; lamin
                     C; progerin; renal carcinoma antigen NY-REN-32;
                     mandibuloacral dysplasia type A; epididymis secretory
                     sperm binding protein"
                     /calculated_mol_wt=74009
     mat_peptide     1..661
                     /product="Prelamin-A/C. /id=PRO_0000398835"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=73808
     mat_peptide     1..646
                     /product="Lamin-A/C. /id=PRO_0000063810"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
                     /calculated_mol_wt=72225
     Region          1..130
                     /region_name="Interaction with MLIP.
                     /evidence=ECO:0000269|PubMed:21498514"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..33
                     /region_name="Head"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          30..386
                     /region_name="Filament"
                     /note="Intermediate filament protein; pfam00038"
                     /db_xref="CDD:459643"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          34..70
                     /region_name="Coil 1A"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            51
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            66
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          71..80
                     /region_name="Linker 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            71
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            78
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          81..218
                     /region_name="Coil 1B"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            97
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            107
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            108
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            114
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            144
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            155
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            171
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            180
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            201
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            208
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            212
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          219..242
                     /region_name="Linker 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            233
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          243..383
                     /region_name="Coil 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          259..331
                     /region_name="Necessary and sufficient for the interaction
                     with IFFO1. /evidence=ECO:0000269|PubMed:31548606"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            260
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            266
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            270
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            277
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37832547; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            301
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            311
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            316
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            325
                     /site_type="other"
                     /note="Stutter. /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            330
                     /site_type="other"
                     /note="Heptad change of phase; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            341
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..664
                     /region_name="Tail"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Region          384..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            392
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066,
                     ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATR.
                     /evidence=ECO:0000269|PubMed:37788673,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            398
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:2188730,
                     ECO:0000269|PubMed:24741066, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            407
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            414
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          417..422
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            417
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            429
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          434..541
                     /region_name="LTD"
                     /note="Lamin Tail Domain; pfam00932"
                     /db_xref="CDD:460003"
     Site            450
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            457
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            486
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            496
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            505
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            510
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48679; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            546
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            548
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          552..576
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            568
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            571
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Region          598..619
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            612
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            613
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P48678; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            619
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            625
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:26237509; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17924679,
                     ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            632
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            636
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            646..647
                     /site_type="cleavage"
                     /note="Cleavage, by endoprotease; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     Site            652
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:24741066,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P02545.1)"
     Site            661
                     /site_type="methylation"
                     /note="Cysteine methyl ester.
                     /evidence=ECO:0000269|PubMed:8175923,
                     ECO:0000269|PubMed:9030603; propagated from
                     UniProtKB/Swiss-Prot (P02545.1)"
     CDS             1..664
                     /gene="LMNA"
                     /gene_synonym="CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL;
                     FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC;
                     LMNL1; MADA; PRO1"
                     /coded_by="NM_170707.4:209..2203"
                     /note="isoform A is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1129.1"
                     /db_xref="GeneID:4000"
                     /db_xref="HGNC:HGNC:6636"
                     /db_xref="MIM:150330"
ORIGIN      
        1 metpsqrrat rsgaqasstp lsptritrlq ekedlqelnd rlavyidrvr sletenaglr
       61 lriteseevv srevsgikaa yeaelgdark tldsvakera rlqlelskvr eefkelkarn
      121 tkkegdliaa qarlkdleal lnskeaalst alsekrtleg elhdlrgqva kleaalgeak
      181 kqlqdemlrr vdaenrlqtm keeldfqkni yseelretkr rhetrlveid ngkqrefesr
      241 ladalqelra qhedqveqyk kelektysak ldnarqsaer nsnlvgaahe elqqsririd
      301 slsaqlsqlq kqlaakeakl rdledslare rdtsrrllae keremaemra rmqqqldeyq
      361 elldiklald meihayrkll egeeerlrls psptsqrsrg rasshssqtq gggsvtkkrk
      421 lestesrssf sqhartsgrv aveevdeegk fvrlrnksne dqsmgnwqik rqngddpllt
      481 yrfppkftlk agqvvtiwaa gagathsppt dlvwkaqntw gcgnslrtal instgeevam
      541 rklvrsvtvv eddededgdd llhhhhgshc sssgdpaeyn lrsrtvlcgt cgqpadkasa
      601 sgsgaqvggp issgssassv tvtrsyrsvg gsgggsfgdn lvtrsyllgn ssprtqspqn
      661 csim
//
LOCUS       NP_001353144             893 aa            linear   PRI 20-NOV-2025
DEFINITION  disks large homolog 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001353144 XP_016861296
VERSION     NP_001353144.1
DBSOURCE    REFSEQ: accession NM_001366215.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 893)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 893)
  AUTHORS   Yang,Z.Y., Zhao,C., Liu,S.L., Pan,L.J., Zhu,Y.D., Zhao,J.W.,
            Wang,H.K., Ye,Y.Y., Qiang,J., Shi,L.Q., Mei,J.W., Xie,Y., Gong,W.,
            Shu,Y.J., Dong,P. and Xiang,S.S.
  TITLE     NONO promotes gallbladder cancer cell proliferation by enhancing
            oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14
  JOURNAL   Cancer Lett 587, 216703 (2024)
   PUBMED   38341127
  REMARK    GeneRIF: NONO promotes gallbladder cancer cell proliferation by
            enhancing oncogenic RNA splicing of DLG1 through interaction with
            IGF2BP3/RBM14.
REFERENCE   3  (residues 1 to 893)
  AUTHORS   Xu,X., Luo,S., Wang,X., Wen,X., Yin,J., Luo,X., He,B., Liang,C.,
            Xiong,S., Zhu,D., Lv,D., Dai,Z., Lin,J., Li,Y., Lin,Z., Chen,W.,
            Luo,Z., Wang,Y. and Ma,G.
  TITLE     Genetic contribution of synapse-associated protein 97 to cerebellar
            functional connectivity changes in first-episode schizophrenia
  JOURNAL   BMC Psychiatry 23 (1), 630 (2023)
   PUBMED   37644438
  REMARK    GeneRIF: Genetic contribution of synapse-associated protein 97 to
            cerebellar functional connectivity changes in first-episode
            schizophrenia.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 893)
  AUTHORS   Scott,H., Dong,L., Stevenson,A., MacDonald,A.I., Srinivasan,S.,
            Massimi,P., Banks,L., Martin,P.E., Johnstone,S.R. and Graham,S.V.
  TITLE     The human discs large protein 1 interacts with and maintains
            connexin 43 at the plasma membrane in keratinocytes
  JOURNAL   J Cell Sci 136 (11) (2023)
   PUBMED   37288673
  REMARK    GeneRIF: The human discs large protein 1 interacts with and
            maintains connexin 43 at the plasma membrane in keratinocytes.
REFERENCE   5  (residues 1 to 893)
  AUTHORS   Cavatorta,A.L., Facciuto,F., Valdano,M.B., Marziali,F., Giri,A.A.,
            Banks,L. and Gardiol,D.
  TITLE     Regulation of translational efficiency by different splice variants
            of the Disc large 1 oncosuppressor 5'-UTR
  JOURNAL   FEBS J 278 (14), 2596-2608 (2011)
   PUBMED   21595829
  REMARK    GeneRIF: Studies represent first analyses of 5'-UTR of DLG1
            transcripts; data suggest that differential expression of
            alternatively spliced 5'-UTRs with different translational
            properties result in changes in DLG1 expression.
REFERENCE   6  (residues 1 to 893)
  AUTHORS   McLaughlin,M., Hale,R., Ellston,D., Gaudet,S., Lue,R.A. and Viel,A.
  TITLE     The distribution and function of alternatively spliced insertions
            in hDlg
  JOURNAL   J Biol Chem 277 (8), 6406-6412 (2002)
   PUBMED   11723125
  REMARK    GeneRIF: We identify the functions of the two alternatively spliced
            regions. The N-terminal alternatively spliced region is capable of
            binding several SH3 domains and also moderates the level of protein
            oligomerization.
REFERENCE   7  (residues 1 to 893)
  AUTHORS   Mori,K., Iwao,K., Miyoshi,Y., Nakagawara,A., Kofu,K., Akiyama,T.,
            Arita,N., Hayakawa,T. and Nakamura,Y.
  TITLE     Identification of brain-specific splicing variants of the hDLG1
            gene and altered splicing in neuroblastoma cell lines
  JOURNAL   J Hum Genet 43 (2), 123-127 (1998)
   PUBMED   9621517
REFERENCE   8  (residues 1 to 893)
  AUTHORS   Kim,E., Niethammer,M., Rothschild,A., Jan,Y.N. and Sheng,M.
  TITLE     Clustering of Shaker-type K+ channels by interaction with a family
            of membrane-associated guanylate kinases
  JOURNAL   Nature 378 (6552), 85-88 (1995)
   PUBMED   7477295
REFERENCE   9  (residues 1 to 893)
  AUTHORS   Lue,R.A., Marfatia,S.M., Branton,D. and Chishti,A.H.
  TITLE     Cloning and characterization of hdlg: the human homologue of the
            Drosophila discs large tumor suppressor binds to protein 4.1
  JOURNAL   Proc Natl Acad Sci U S A 91 (21), 9818-9822 (1994)
   PUBMED   7937897
REFERENCE   10 (residues 1 to 893)
  AUTHORS   Mukherjee,A., Varma,S.K. and Natarajan,K.
  TITLE     Ankle joint instability in poliomyelitis
  JOURNAL   Indian J Pediatr 39 (289), 37-38 (1972)
   PUBMED   5024025
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC092937.8 and AC068302.18.
            
            On Sep 26, 2018 this sequence version replaced XP_016861296.1.
            
            Summary: This gene encodes a multi-domain scaffolding protein that
            is required for normal development. This protein may have a role in
            septate junction formation, signal transduction, cell
            proliferation, synaptogenesis and lymphocyte activation. A
            multitude of transcript variants deriving from alternative splicing
            and the use of multiple alternate promoter have been observed,
            including some splice variants that may be specific to brain and
            other tissues. An upstream uORF may regulate translation at some
            splice variants of this gene. [provided by RefSeq, Sep 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.21611.1,
                                           SRR11853566.20756.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..893
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..893
                     /product="disks large homolog 1 isoform 6"
                     /note="presynaptic protein SAP97; synapse-associated
                     protein 97; discs large homolog 1, scribble cell polarity
                     complex component; dJ1061C18.1.1"
                     /calculated_mol_wt=99811
     Region          6..64
                     /region_name="L27_1"
                     /note="pfam09058"
                     /db_xref="CDD:462665"
     Region          107..190
                     /region_name="MAGUK_N_PEST"
                     /note="Polyubiquitination (PEST) N-terminal domain of
                     MAGUK; pfam10608"
                     /db_xref="CDD:431391"
     Region          189..277
                     /region_name="PDZ1_Dlg1-2-4-like"
                     /note="PDZ domain 1 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06723"
                     /db_xref="CDD:467206"
     Site            order(200..206,223,226,256,260,263..264)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467206"
     Region          286..370
                     /region_name="PDZ2_Dlg1-2-4-like"
                     /note="PDZ domain 2 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06724"
                     /db_xref="CDD:467207"
     Site            order(295..301,318,321,351,355,358..359)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467207"
     Region          371..432
                     /region_name="PDZ_assoc"
                     /note="PDZ-associated domain of NMDA receptors; pfam10600"
                     /db_xref="CDD:463164"
     Region          430..520
                     /region_name="PDZ3_Dlg1-2-4-like"
                     /note="PDZ domain 3 of human discs large homolog 1 (Dlg1),
                     Dlg2, and Dlg4, Drosophila disc large (Dlg), and related
                     domains; cd06795"
                     /db_xref="CDD:467257"
     Site            order(442..448,459,462,492,496,499..500)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467257"
     Region          549..615
                     /region_name="SH3_DLG1"
                     /note="Src Homology 3 domain of Disks Large homolog 1;
                     cd12031"
                     /db_xref="CDD:212964"
     Site            order(554,576..577,598)
                     /site_type="other"
                     /note="GuK domain interface [polypeptide binding]"
                     /db_xref="CDD:212964"
     Site            order(557,559,562,571,589..590,609,611..612)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212964"
     Region          702..880
                     /region_name="Guanylate_kin"
                     /note="Guanylate kinase; pfam00625"
                     /db_xref="CDD:395500"
     CDS             1..893
                     /gene="DLG1"
                     /gene_synonym="DLGH1; hdlg; SAP-97; SAP97"
                     /coded_by="NM_001366215.1:624..3305"
                     /note="isoform 6 is encoded by transcript variant 20"
                     /db_xref="CCDS:CCDS87192.1"
                     /db_xref="GeneID:1739"
                     /db_xref="HGNC:HGNC:2900"
                     /db_xref="MIM:601014"
ORIGIN      
        1 mpvrkqdtqr alhlleeyrs klsqtedrql rssiervini fqsnlfqali diqefyevtl
       61 ldnpkcidrs kpsepiqpvn tweisslpss tvtsetlpss lspsvekyry qdedtppqeh
      121 ispqitnevi gpelvhvsek nlseienvhg fvshshispi kanpppvlvn tdsletptyv
      181 ngtdadyeye eitlergnsg lgfsiaggtd nphigddssi fitkiitgga aaqdgrlrvn
      241 dcilrvnevd vrdvthskav ealkeagsiv rlyvkrrkpv sekimeikli kgpkglgfsi
      301 aggvgnqhip gdnsiyvtki ieggaahkdg klqigdklla vnnvcleevt heeavtalkn
      361 tsdfvylkva kptsmymndg yappditnss sqpvdnhvsp ssflgqtpas paryspvska
      421 vlgddeitre prkvvlhrgs tglgfnivgg edgegifisf ilaggpadls gelrkgdrii
      481 svnsvdlraa sheqaaaalk nagqavtiva qyrpeeysrf eakihdlreq mmnssissgs
      541 gslrtsqkrs lyvralfdyd ktkdsglpsq glnfkfgdil hvinasddew wqarqvtpdg
      601 esdevgvips krrvekkera rlktvkfnsk trdkgqsfnd krkknlfsrk fpfyknkdqs
      661 eqetsdadqh vtsnasdses syrgqeeyvl syepvnqqev nytrpviilg pmkdrinddl
      721 isefpdkfgs cvphttrpkr dyevdgrdyh fvtsreqmek diqehkfiea gqynnhlygt
      781 svqsvrevae kgkhcildvs gnaikrlqia qlypisifik pksmenimem nkrlteeqar
      841 ktferamkle qeftehftai vqgdtlediy nqvkqiieeq sgsyiwvpak ekl
//
LOCUS       NP_874365               1655 aa            linear   PRI 20-NOV-2025
DEFINITION  protein scribble homolog isoform a [Homo sapiens].
ACCESSION   NP_874365
VERSION     NP_874365.3
DBSOURCE    REFSEQ: accession NM_182706.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1655)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 1655)
  AUTHORS   Edamana,S., Login,F.H., Riishede,A., Dam,V.S., Kirkegaard,T. and
            Nejsum,L.N.
  TITLE     The water channels aquaporin-1 and aquaporin-3 interact with and
            affect the cell polarity protein Scribble in 3D in vitro models of
            breast cancer
  JOURNAL   Am J Physiol Cell Physiol 327 (5), C1323-C1334 (2024)
   PUBMED   39279492
  REMARK    GeneRIF: The water channels aquaporin-1 and aquaporin-3 interact
            with and affect the cell polarity protein Scribble in 3D in vitro
            models of breast cancer.
REFERENCE   3  (residues 1 to 1655)
  AUTHORS   Lulic,L., Simic,I., Bozinovic,K., Pesut,E., Manojlovic,L., Grce,M.,
            Dediol,E., Sabol,I. and Tomaic,V.
  TITLE     Moderate SCRIB Expression Levels Correlate with Worse Prognosis in
            OPSCC Patients Regardless of HPV Status
  JOURNAL   Cells 13 (12), 1002 (2024)
   PUBMED   38920638
  REMARK    GeneRIF: Moderate SCRIB Expression Levels Correlate with Worse
            Prognosis in OPSCC Patients Regardless of HPV Status.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1655)
  AUTHORS   Chen,Y., Su,H., Zhao,J., Na,Z., Jiang,K., Bacchiocchi,A., Loh,K.H.,
            Halaban,R., Wang,Z., Cao,X. and Slavoff,S.A.
  TITLE     Unannotated microprotein EMBOW regulates the interactome and
            chromatin and mitotic functions of WDR5
  JOURNAL   Cell Rep 42 (9), 113145 (2023)
   PUBMED   37725512
REFERENCE   5  (residues 1 to 1655)
  AUTHORS   Almeida,S.M., Ivantsiv,S., Niibori,R., Dunham,W.H., Green,B.A.,
            Zhao,L., Gingras,A.C. and Cordes,S.P.
  TITLE     An interaction between OTULIN and SCRIB uncovers roles for linear
            ubiquitination in planar cell polarity
  JOURNAL   Dis Model Mech 16 (8) (2023)
   PUBMED   37589075
  REMARK    GeneRIF: An interaction between OTULIN and SCRIB uncovers roles for
            linear ubiquitination in planar cell polarity.
REFERENCE   6  (residues 1 to 1655)
  AUTHORS   Audebert,S., Navarro,C., Nourry,C., Chasserot-Golaz,S., Lecine,P.,
            Bellaiche,Y., Dupont,J.L., Premont,R.T., Sempere,C., Strub,J.M.,
            Van Dorsselaer,A., Vitale,N. and Borg,J.P.
  TITLE     Mammalian Scribble forms a tight complex with the betaPIX exchange
            factor
  JOURNAL   Curr Biol 14 (11), 987-995 (2004)
   PUBMED   15182672
REFERENCE   7  (residues 1 to 1655)
  AUTHORS   Brill,L.M., Salomon,A.R., Ficarro,S.B., Mukherji,M.,
            Stettler-Gill,M. and Peters,E.C.
  TITLE     Robust phosphoproteomic profiling of tyrosine phosphorylation sites
            from human T cells using immobilized metal affinity chromatography
            and tandem mass spectrometry
  JOURNAL   Anal Chem 76 (10), 2763-2772 (2004)
   PUBMED   15144186
REFERENCE   8  (residues 1 to 1655)
  AUTHORS   Nakagawa,S., Yano,T., Nakagawa,K., Takizawa,S., Suzuki,Y.,
            Yasugi,T., Huibregtse,J.M. and Taketani,Y.
  TITLE     Analysis of the expression and localisation of a LAP protein, human
            scribble, in the normal and neoplastic epithelium of uterine cervix
  JOURNAL   Br J Cancer 90 (1), 194-199 (2004)
   PUBMED   14710229
  REMARK    GeneRIF: Degradation by human papilloma virus E6 may cause
            progressive decrease of hScrib expression during disease
            progression from low-grade squamous intraepithelial lesions (SIL)
            to high-grade SIL
REFERENCE   9  (residues 1 to 1655)
  AUTHORS   Dow,L.E., Brumby,A.M., Muratore,R., Coombe,M.L., Sedelies,K.A.,
            Trapani,J.A., Russell,S.M., Richardson,H.E. and Humbert,P.O.
  TITLE     hScrib is a functional homologue of the Drosophila tumour
            suppressor Scribble
  JOURNAL   Oncogene 22 (58), 9225-9230 (2003)
   PUBMED   14681682
  REMARK    GeneRIF: hScrib is a functional homologue of DmScrib and therefore
            predict an important role for hScrib in the suppression of
            mammalian tumorigenesis
REFERENCE   10 (residues 1 to 1655)
  AUTHORS   Nakagawa,S. and Huibregtse,J.M.
  TITLE     Human scribble (Vartul) is targeted for ubiquitin-mediated
            degradation by the high-risk papillomavirus E6 proteins and the
            E6AP ubiquitin-protein ligase
  JOURNAL   Mol Cell Biol 20 (21), 8244-8253 (2000)
   PUBMED   11027293
  REMARK    GeneRIF: KIAA0147 encodes the human homolog of Drosophila Scribble.
            hScrib is targeted for ubiquitin-mediated degradation by the HPV E6
            oncoprotein, and mutations in Dros. scrib result in loss of
            polarity and growth control of epithelial cells.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC105219.6 and KF458881.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 3, 2011 this sequence version replaced NP_874365.2.
            
            Summary: This gene encodes a protein that was identified as being
            similar to the Drosophila scribble protein. The mammalian protein
            is involved in tumor suppression pathways. As a scaffold protein
            involved in cell polarization processes, this protein binds to many
            other proteins. The encoded protein binds to papillomavirus E6
            protein via its PDZ domain and the C-terminus of E6. Two
            alternatively spliced transcript variants that encode different
            protein isoforms have been found for this gene. [provided by
            RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR4352443.181440.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356994.7/ ENSP00000349486.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1655
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..1655
                     /product="protein scribble homolog isoform a"
                     /note="protein scribble homolog; scribbled homolog;
                     scribbled planar cell polarity protein"
                     /calculated_mol_wt=177594
     Region          1..818
                     /region_name="Sufficient for targeting to adherens
                     junction and to inhibit cell proliferation"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          14..37
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          36..94
                     /region_name="LRR_8"
                     /note="Leucine rich repeat; pfam13855"
                     /db_xref="CDD:404697"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          38..60
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          61..83
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          84..106
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          87..>396
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          107..129
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          130..152
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          153..175
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          176..198
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          199..221
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          268..290
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          291..313
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          314..336
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          360..381
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            378
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          417..440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          459..606
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            475
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            504
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          628..702
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            689
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            708
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          717..1229
                     /region_name="Interaction with ARHGEF7.
                     /evidence=ECO:0000269|PubMed:15182672"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          727..813
                     /region_name="PDZ1_Scribble-like"
                     /note="PDZ domain 1 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06704"
                     /db_xref="CDD:467188"
     Region          728..1194
                     /region_name="Required for interaction with VIM.
                     /evidence=ECO:0000269|PubMed:19386766"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            order(737..743,761,764,793,797,800..801)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467188"
     Site            764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Region          827..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            835
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            853
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          859..950
                     /region_name="PDZ2_Scribble-like"
                     /note="PDZ domain 2 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06703"
                     /db_xref="CDD:467187"
     Site            order(871..877,895,898,928,932,935..936)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467187"
     Site            875
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            939
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1003..1091
                     /region_name="PDZ3_Scribble-like"
                     /note="PDZ domain 3 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06702"
                     /db_xref="CDD:467186"
     Site            order(1013..1019,1039,1042,1071,1075,1078..1079)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467186"
     Region          1095..1192
                     /region_name="PDZ4_Scribble-like"
                     /note="PDZ domain 4 of Drosophila Scribble, human Scribble
                     homolog, and related domains; cd06701"
                     /db_xref="CDD:467185"
     Region          1105..1117
                     /region_name="Interaction with tick-borne encephalitis
                     virus RNA-directed RNA polymerase NS5.
                     /evidence=ECO:0000269|PubMed:18042258"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            order(1110..1116,1137,1140,1170,1174,1177..1178)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467185"
     Site            1140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1220
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1227..1246
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1232
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1276
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1277..1489
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1279
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1295
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1298
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1306
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1309
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1348
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1378
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1437
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1445
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1448
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1475
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1508
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1520..1568
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1541
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1545
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1547
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1555..>1630
                     /region_name="AbLIM_anchor"
                     /note="Putative adherens-junction anchoring region of
                     AbLIM; pfam16182"
                     /db_xref="CDD:465046"
     Site            1561
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Site            1591
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14160.6)"
     Region          1622..1655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14160.6)"
     CDS             1..1655
                     /gene="SCRIB"
                     /gene_synonym="CRIB1; oSCRIB; SCRB1; SCRIB1; Vartul"
                     /coded_by="NM_182706.5:402..5369"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6412.1"
                     /db_xref="GeneID:23513"
                     /db_xref="HGNC:HGNC:30377"
                     /db_xref="MIM:607733"
ORIGIN      
        1 mlkciplwrc nrhvesvdkr hcslqavpee iyrysrslee llldanqlre lpkpffrlln
       61 lrklglsdne iqrlppevan fmqlveldvs rndipeipes ikfckaleia dfsgnplsrl
      121 pdgftqlrsl ahlalndvsl qalpgdvgnl anlvtlelre nllkslpasl sflvkleqld
      181 lggndlevlp dtlgalpnlr elwldrnqls alppelgnlr rlvcldvsen rleelpaelg
      241 glvlltdlll sqnllrrlpd gigqlkqlsi lkvdqnrlce vteaigdcen lseliltenl
      301 lmalprslgk ltkltnlnvd rnhlealppe iggcvalsvl slrdnrlavl ppelahttel
      361 hvldvagnrl qslpfalthl nlkalwlaen qaqpmlrfqt eddartgekv ltcyllpqqp
      421 ppsledagqq gslsetwsda ppsrvsviqf leapigdeda eeaaaekrgl qrratphpse
      481 lkvmkrsieg rrseacpcqp dsgsplpaee ekrlsaesgl sedsrpsast vseaepegps
      541 aeaqggsqqe attaggeeda eedyqeptvh faedallpgd dreieegqpe apwtlpggrq
      601 rlirkdtphy kkhfkisklp qpeavvallq gmqpdgegpv apggwhngph apwapraqke
      661 eeeeeegspq eeeeeeeeen raeeeeaste eedkegavvs apsvkgvsfd qannlliepa
      721 rieeeeltlt ilrqtgglgi siaggkgstp ykgddegifi srvseegpaa ragvrvgdkl
      781 levngvalqg aehheaveal rgagtavqmr vwrermvepe navtitplrp eddysprerr
      841 ggglrlpllp pespgplrqr hvaclarser glgfsiaggk gstpyragda gifvsriaeg
      901 gaahragtlq vgdrvlsing vdvtearhdh avslltaasp tialllerea ggplppsplp
      961 hsspptaava ttsittatpg vpglpslaps llaaalegpy pveeirlpra ggplglsivg
     1021 gsdhsshpfg vqepgvfisk vlprglaars glrvgdrila vngqdvrdat hqeavsallr
     1081 pclelsllvr rdpappglre lciqkapger lgisirggar ghagnprdpt degifiskvs
     1141 ptgaagrdgr lrvglrllev nqqsllglth geavqllrsv gdtltvlvcd gfeastdaal
     1201 evspgvianp faagighrns lesissidre lspegpgkek elpgqtlhwg peateaagrg
     1261 lqplkldyra laavpsagsv qrvpsgaagg kmaespcsps gqqppsppsp delpanvkqa
     1321 yrafaavpts hppedapaqp ptpgpaaspe qlsfrerqky felevrvpqa egppkrvslv
     1381 gaddlrkmqe eearklqqkr aqmlreaaea gaearlaldg etlgeeeqed eqppwaspsp
     1441 tsrqspaspp plgggapvrt akaerrhqer lrvqspeppa peralspael raleaekral
     1501 wraarmksle qdalraqmvl srsqegrgtr gplerlaeap spaptpsptp vedlgpqtst
     1561 spgrlplsgk kfdyrafaal pssrpvydiq spdfaeelrs lepspspgpq eedgevalvl
     1621 lgrpspgavg pedvalcssr rpvrpgrrgl gpvps
//
LOCUS       NP_001129472            1064 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein kinase ABL2 isoform d [Homo sapiens].
ACCESSION   NP_001129472
VERSION     NP_001129472.1
DBSOURCE    REFSEQ: accession NM_001136000.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1064)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1064)
  AUTHORS   Miao,Y. and Liu,J.
  TITLE     Tumor-suppressive action of miR-30a-5p in lung adenocarcinoma
            correlates with ABL2 inhibition and PI3K/AKT pathway inactivation
  JOURNAL   Clin Transl Oncol 26 (2), 398-413 (2024)
   PUBMED   37479901
  REMARK    GeneRIF: Tumor-suppressive action of miR-30a-5p in lung
            adenocarcinoma correlates with ABL2 inhibition and PI3K/AKT pathway
            inactivation.
REFERENCE   3  (residues 1 to 1064)
  AUTHORS   Kabirova,M., Reichenstein,M., Borovok,N., Sheinin,A., Gorobets,D.
            and Michaelevski,I.
  TITLE     Abl2 Kinase Differentially Regulates iGluRs Current Activity and
            Synaptic Localization
  JOURNAL   Cell Mol Neurobiol 43 (6), 2785-2799 (2023)
   PUBMED   36689065
  REMARK    GeneRIF: Abl2 Kinase Differentially Regulates iGluRs Current
            Activity and Synaptic Localization.
REFERENCE   4  (residues 1 to 1064)
  AUTHORS   Wu,K., Wu,H., Lyu,W., Kim,Y., Furdui,C.M., Anderson,K.S. and
            Koleske,A.J.
  TITLE     Platelet-derived growth factor receptor beta activates Abl2 via
            direct binding and phosphorylation
  JOURNAL   J Biol Chem 297 (1), 100883 (2021)
   PUBMED   34144039
  REMARK    GeneRIF: Platelet-derived growth factor receptor beta activates
            Abl2 via direct binding and phosphorylation.
REFERENCE   5  (residues 1 to 1064)
  AUTHORS   Bianchi,C., Torsello,B., Angeloni,V., Bombelli,S., Soldi,M.,
            Invernizzi,L., Brambilla,P. and Perego,R.A.
  TITLE     Eight full-length abelson related gene (Arg) isoforms are
            constitutively expressed in caki-1 cell line and cell distribution
            of two isoforms has been analyzed after transfection
  JOURNAL   J Cell Biochem 105 (5), 1219-1227 (2008)
   PUBMED   18810762
REFERENCE   6  (residues 1 to 1064)
  AUTHORS   Perego,R.A., Corizzato,M., Bianchi,C., Eroini,B. and Bosari,S.
  TITLE     N- and C-terminal isoforms of Arg quantified by real-time PCR are
            specifically expressed in human normal and neoplastic cells, in
            neoplastic cell lines, and in HL-60 cell differentiation
  JOURNAL   Mol Carcinog 42 (4), 229-239 (2005)
   PUBMED   15765532
REFERENCE   7  (residues 1 to 1064)
  AUTHORS   Wang,B. and Kruh,G.D.
  TITLE     Subcellular localization of the Arg protein tyrosine kinase
  JOURNAL   Oncogene 13 (1), 193-197 (1996)
   PUBMED   8700546
REFERENCE   8  (residues 1 to 1064)
  AUTHORS   Muller,A.J., Pendergast,A.M., Havlik,M.H., Puil,L., Pawson,T. and
            Witte,O.N.
  TITLE     A limited set of SH2 domains binds BCR through a high-affinity
            phosphotyrosine-independent interaction
  JOURNAL   Mol Cell Biol 12 (11), 5087-5093 (1992)
   PUBMED   1383690
REFERENCE   9  (residues 1 to 1064)
  AUTHORS   Kruh,G.D., Perego,R., Miki,T. and Aaronson,S.A.
  TITLE     The complete coding sequence of arg defines the Abelson subfamily
            of cytoplasmic tyrosine kinases
  JOURNAL   Proc Natl Acad Sci U S A 87 (15), 5802-5806 (1990)
   PUBMED   2198571
REFERENCE   10 (residues 1 to 1064)
  AUTHORS   Kruh,G.D., King,C.R., Kraus,M.H., Popescu,N.C., Amsbaugh,S.C.,
            McBride,W.O. and Aaronson,S.A.
  TITLE     A novel human gene closely related to the abl proto-oncogene
  JOURNAL   Science 234 (4783), 1545-1548 (1986)
   PUBMED   3787260
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX538317.1, AL139132.16 and
            BQ014912.1.
            
            Summary: This gene encodes a member of the Abelson family of
            nonreceptor tyrosine protein kinases. The protein is highly similar
            to the c-abl oncogene 1 protein, including the tyrosine kinase, SH2
            and SH3 domains, and it plays a role in cytoskeletal rearrangements
            through its C-terminal F-actin- and microtubule-binding sequences.
            This gene is expressed in both normal and tumor cells, and is
            involved in translocation with the ets variant 6 gene in leukemia.
            Multiple alternatively spliced transcript variants encoding
            different protein isoforms have been found for this gene. [provided
            by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (d) differs in the 5' UTR and 5'
            coding region, and lacks an alternate in-frame segment in the 3'
            coding region, compared to variant b. The resulting isoform (d,
            also known as 1ALCTS) has a distinct N-terminus and is shorter than
            isoform b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX538317.1, DRR138512.549194.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1064
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q25.2"
     Protein         1..1064
                     /product="tyrosine-protein kinase ABL2 isoform d"
                     /EC_number="2.7.10.2"
                     /note="tyrosine-protein kinase ARG; abelson-related gene
                     protein; Abelson tyrosine-protein kinase 2; c-abl oncogene
                     2, non-receptor tyrosine kinase; v-abl Abelson murine
                     leukemia viral oncogene homolog 2"
                     /calculated_mol_wt=116152
     Region          96..149
                     /region_name="SH3_Abl"
                     /note="Src homology 3 domain of the Protein Tyrosine
                     Kinase, Abelson kinase; cd11850"
                     /db_xref="CDD:212784"
     Site            order(101,103,106..108,110,125,129..130,141,143,145..146)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212784"
     Site            order(105..108,127,129)
                     /site_type="other"
                     /note="PTKc domain interface [polypeptide binding]"
                     /db_xref="CDD:212784"
     Region          154..247
                     /region_name="SH2_ABL"
                     /note="Src homology 2 (SH2) domain found in Abelson murine
                     lymphosarcoma virus (ABL) proteins; cd09935"
                     /db_xref="CDD:198189"
     Site            order(165,193,206)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198189"
     Region          266..528
                     /region_name="PTKc_Abl"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Abelson kinase; cd05052"
                     /db_xref="CDD:270645"
     Site            order(279,281..283,300,302,347,349,353,401,412,430..432,
                     434,442,476,480)
                     /site_type="active"
                     /db_xref="CDD:270645"
     Site            order(279,281,284,300,302,317,321,330,346..347,349,353,
                     401,411..412)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            order(294..295,325..327,331,373,405..406,524..525)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:270645"
     Site            order(371..372,375,460,463..464,493..494)
                     /site_type="other"
                     /note="myristoyl binding site [chemical binding]"
                     /db_xref="CDD:270645"
     Site            411..435
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270645"
     Site            order(430..432,434,442,476,480)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270645"
     Region          945..1064
                     /region_name="FABD"
                     /note="F-actin binding domain (FABD); smart00808"
                     /db_xref="CDD:197885"
     CDS             1..1064
                     /gene="ABL2"
                     /gene_synonym="ABLL; ARG"
                     /coded_by="NM_001136000.3:33..3227"
                     /note="isoform d is encoded by transcript variant d"
                     /db_xref="CCDS:CCDS44282.1"
                     /db_xref="GeneID:27"
                     /db_xref="HGNC:HGNC:77"
                     /db_xref="MIM:164690"
ORIGIN      
        1 mvlgtvllpp nsygrdqdts lcclctease salpdltdhf ascvedgfeg dktggsspea
       61 lhrpygcdve pqalneairw sskenllgat esdpnlfval ydfvasgdnt lsitkgeklr
      121 vlgynqngew sevrskngqg wvpsnyitpv nslekhswyh gpvsrsaaey llsslingsf
      181 lvresesspg qlsislryeg rvyhyrintt adgkvyvtae srfstlaelv hhhstvadgl
      241 vttlhypapk cnkptvygvs pihdkwemer tditmkhklg ggqygevyvg vwkkysltva
      301 vktlkedtme veeflkeaav mkeikhpnlv qllgvctlep pfyivteymp ygnlldylre
      361 cnreevtavv llymatqiss ameylekknf ihrdlaarnc lvgenhvvkv adfglsrlmt
      421 gdtytahaga kfpikwtape slayntfsik sdvwafgvll weiatygmsp ypgidlsqvy
      481 dllekgyrme qpegcppkvy elmracwkws padrpsfaet hqafetmfhd ssiseevaee
      541 lgraassssv vpylprlpil psktrtlkkq venkeniega qdatensass lapgfirgaq
      601 assgspalpr kqrdkspssl ledaketcft rdrkggffss fmkkrnaptp pkrsssfrem
      661 enqphkkyel tglpeqdrma mtlprncqrs klqlertvst ssqpeenvdr andmlpkkse
      721 esaapsrerp kakllprgat alplrtpsgd laitekdppg vgvagvaaap kgkeknggar
      781 lgmagvpedg eqpgwpspak aapvlptthn hkvpvlispt lkhtpadvql igtdsqgnkf
      841 kllsehqvts sgdkdrprrv kpkcappppp vmrllqhpsi csdpteepta ltagqstset
      901 qeggkkaalg avpisgkagr pvmpppqvpl ptssispakm angtagtkva lrktkqaaek
      961 isadkiskea llecadllss altepvpnsq lvdtghqlld ycsgyvdcip qtrnkfafre
     1021 avsklelslq elqvssaaag vpgtnpvlnn llscvqeisd vvqr
//
LOCUS       NP_001298184             177 aa            linear   PRI 20-NOV-2025
DEFINITION  biogenesis of lysosome-related organelles complex 1 subunit 6
            isoform 1 [Homo sapiens].
ACCESSION   NP_001298184
VERSION     NP_001298184.1
DBSOURCE    REFSEQ: accession NM_001311255.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 177)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 177)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 177)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 177)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 177)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 177)
  AUTHORS   Huang,L., Kuo,Y.M. and Gitschier,J.
  TITLE     The pallid gene encodes a novel, syntaxin 13-interacting protein
            involved in platelet storage pool deficiency
  JOURNAL   Nat Genet 23 (3), 329-332 (1999)
   PUBMED   10610180
REFERENCE   7  (residues 1 to 177)
  AUTHORS   Risinger,M.A., Korsgren,C. and Cohen,C.M.
  TITLE     Role of N-myristylation in targeting of band 4.2 (pallidin) in
            nonerythroid cells
  JOURNAL   Exp Cell Res 229 (2), 421-431 (1996)
   PUBMED   8986625
REFERENCE   8  (residues 1 to 177)
  AUTHORS   Azim,A.C., Marfatia,S.M., Korsgren,C., Dotimas,E., Cohen,C.M. and
            Chishti,A.H.
  TITLE     Human erythrocyte dematin and protein 4.2 (pallidin) are ATP
            binding proteins
  JOURNAL   Biochemistry 35 (9), 3001-3006 (1996)
   PUBMED   8608138
REFERENCE   9  (residues 1 to 177)
  AUTHORS   Introne,W.J., Huizing,M., Malicdan,M.C.V., O'Brien,K.J. and
            Gahl,W.A.
  TITLE     Hermansky-Pudlak Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301464
REFERENCE   10 (residues 1 to 177)
  AUTHORS   Korsgren,C. and Cohen,C.M.
  TITLE     Associations of human erythrocyte band 4.2. Binding to ankyrin and
            to the cytoplasmic domain of band 3
  JOURNAL   J Biol Chem 263 (21), 10212-10218 (1988)
   PUBMED   2968981
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA230439.1, AL596952.1,
            AK128626.1, BC026289.1 and BP423071.1.
            
            Summary: The protein encoded by this gene may play a role in
            intracellular vesicle trafficking. It interacts with Syntaxin 13
            which mediates intracellular membrane fusion. Mutations in this
            gene cause symptoms associated with Hermansky-Pudlak syndrome-9.
            Alternative splicing results in multiple transcript variants. A
            pseudogene related to this gene is located on the X chromosome.
            [provided by RefSeq, Aug 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.14950.1,
                                           SRR1803615.48563.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..177
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..177
                     /product="biogenesis of lysosome-related organelles
                     complex 1 subunit 6 isoform 1"
                     /note="syntaxin 13-interacting protein pallid; biogenesis
                     of lysosomal organelles complex-1, subunit 6, pallidin;
                     syntaxin 13 binding protein 1; pallid protein homolog;
                     biogenesis of lysosomal organelles complex-1, subunit 5,
                     pallidin; BLOC-1 subunit 6; biogenesis of lysosome-related
                     organelles complex 1 subunit 6; BLOC-1 subunit pallidin"
                     /calculated_mol_wt=20134
     Region          55..145
                     /region_name="Snapin_Pallidin"
                     /note="Snapin/Pallidin; pfam14712"
                     /db_xref="CDD:464275"
     CDS             1..177
                     /gene="BLOC1S6"
                     /gene_synonym="BLOS6; HPS9; PA; PALLID; PLDN"
                     /coded_by="NM_001311255.1:141..674"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS81878.1"
                     /db_xref="GeneID:26258"
                     /db_xref="HGNC:HGNC:8549"
                     /db_xref="MIM:604310"
ORIGIN      
        1 mggtevprgs fvlgvqlkav dgeailslcv dsglsdtspd egliedltie dkaveqlaeg
       61 llshylpdlq rskqalqelt qnqvvlldtl eqeiskfkec hsmldinalf aeakhyhakl
      121 vnirkemlml hektsklkkr alklqqkrqk eelereqqre keferekqlt arpakrm
//
LOCUS       NP_001340919             682 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphate phosphatase MTMR1 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001340919 XP_005274824
VERSION     NP_001340919.1
DBSOURCE    REFSEQ: accession NM_001353990.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Chui,A.J., Griswold,A.R., Taabazuing,C.Y., Orth,E.L., Gai,K.,
            Rao,S.D., Ball,D.P., Hsiao,J.C. and Bachovchin,D.A.
  TITLE     Activation of the CARD8 Inflammasome Requires a Disordered Region
  JOURNAL   Cell Rep 33 (2), 108264 (2020)
   PUBMED   33053349
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Sundell,G.N., Arnold,R., Ali,M., Naksukpaiboon,P., Orts,J.,
            Guntert,P., Chi,C.N. and Ivarsson,Y.
  TITLE     Proteome-wide analysis of phospho-regulated PDZ domain interactions
  JOURNAL   Mol Syst Biol 14 (8), e8129 (2018)
   PUBMED   30126976
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Bong,S.M., Son,K.B., Yang,S.W., Park,J.W., Cho,J.W., Kim,K.T.,
            Kim,H., Kim,S.J., Kim,Y.J. and Lee,B.I.
  TITLE     Crystal Structure of Human Myotubularin-Related Protein 1 Provides
            Insight into the Structural Basis of Substrate Specificity
  JOURNAL   PLoS One 11 (3), e0152611 (2016)
   PUBMED   27018598
  REMARK    Erratum:[PLoS One. 2018 Jan 2;13(1):e0190844. doi:
            10.1371/journal.pone.0190844. PMID: 29293653]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Santoro,M., Modoni,A., Masciullo,M., Gidaro,T., Broccolini,A.,
            Ricci,E., Tonali,P.A. and Silvestri,G.
  TITLE     Analysis of MTMR1 expression and correlation with muscle
            pathological features in juvenile/adult onset myotonic dystrophy
            type 1 (DM1) and in myotonic dystrophy type 2 (DM2)
  JOURNAL   Exp Mol Pathol 89 (2), 158-168 (2010)
   PUBMED   20685272
  REMARK    GeneRIF: an aberrant MTMR1 expression and signs of altered myofiber
            maturation were documented in both DM1 and in DM2 muscle tissues.
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Kim,S.A., Taylor,G.S., Torgersen,K.M. and Dixon,J.E.
  TITLE     Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
            in myotubular myopathy and type 4B Charcot-Marie-Tooth disease
  JOURNAL   J Biol Chem 277 (6), 4526-4531 (2002)
   PUBMED   11733541
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A. and Mandel,J.L.
  TITLE     The myotubularin family: from genetic disease to phosphoinositide
            metabolism
  JOURNAL   Trends Genet 17 (4), 221-228 (2001)
   PUBMED   11275328
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Kioschis,P., Wiemann,S., Heiss,N.S., Francis,F., Gotz,C.,
            Poustka,A., Taudien,S., Platzer,M., Wiehe,T., Beckmann,G.,
            Weber,J., Nordsiek,G. and Rosenthal,A.
  TITLE     Genomic organization of a 225-kb region in Xq28 containing the gene
            for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)
  JOURNAL   Genomics 54 (2), 256-266 (1998)
   PUBMED   9828128
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Laporte,J., Blondeau,F., Buj-Bello,A., Tentler,D., Kretz,C.,
            Dahl,N. and Mandel,J.L.
  TITLE     Characterization of the myotubularin dual specificity phosphatase
            gene family from yeast to human
  JOURNAL   Hum Mol Genet 7 (11), 1703-1712 (1998)
   PUBMED   9736772
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Laporte,J., Hu,L.J., Kretz,C., Mandel,J.L., Kioschis,P., Coy,J.F.,
            Klauck,S.M., Poustka,A. and Dahl,N.
  TITLE     A gene mutated in X-linked myotubular myopathy defines a new
            putative tyrosine phosphatase family conserved in yeast
  JOURNAL   Nat Genet 13 (2), 175-182 (1996)
   PUBMED   8640223
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF002223.2.
            
            On Aug 3, 2017 this sequence version replaced XP_005274824.1.
            
            Summary: This gene encodes a member of the myotubularin related
            family of proteins. Members of this family contain the consensus
            sequence for the active site of protein tyrosine phosphatases.
            Alternatively spliced variants have been described but their
            biological validity has not been determined. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (4) represents the longest
            transcript and encodes the longest isoform (4).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.146874.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145743
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..682
                     /product="phosphatidylinositol-3-phosphate phosphatase
                     MTMR1 isoform 4"
                     /EC_number="3.1.3.95"
                     /note="phosphatidylinositol-3-phosphate phosphatase;
                     phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
                     phosphatidylinositol-3-phosphate phosphatase MTMR1"
                     /calculated_mol_wt=76475
     Region          124..223
                     /region_name="PH-GRAM_MTMR1"
                     /note="Myotubularian related 1 protein (MTMR1) Pleckstrin
                     Homology-Glucosyltransferases, Rab-like GTPase activators
                     and Myotubularins (PH-GRAM) domain; cd13358"
                     /db_xref="CDD:270165"
     Region          240..566
                     /region_name="Myotub-related"
                     /note="Myotubularin-like phosphatase domain; pfam06602"
                     /db_xref="CDD:461958"
     CDS             1..682
                     /gene="MTMR1"
                     /coded_by="NM_001353990.2:136..2184"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS94687.1"
                     /db_xref="GeneID:8776"
                     /db_xref="HGNC:HGNC:7449"
                     /db_xref="MIM:300171"
ORIGIN      
        1 mdrpaaaaaa gceggggpnp gpaggrrppr aaggatagsr qpsvetldsp tgshvewckq
       61 liaatissqi sgsvtsenvs rdykeiqeeh ngypseaead qalrdgnkla qmeeaplfpg
      121 esikaivkdv myicpfmgav sgtltvtdfk lyfknverdp hfildvplgv isrvekigaq
      181 shgdnscgie ivckdmrnlr laykqeeqsk lgifenlnkh afplsngqal fafsykekfp
      241 ingwkvydpv seykrqglpn eswkiskins nyefcdtypa iivvptsvkd ddlskvaafr
      301 akgrvpvlsw ihpesqatit rcsqplvgpn dkrckedeky lqtimdanaq shkliifdar
      361 qnsvadtnkt kgggyesesa ypnaelvfle ihnihvmres lrklkeivyp sidearwlsn
      421 vdgthwleyi rmllagavri adkiesgkts vvvhcsdgwd rtaqltslam lmldsyyrti
      481 kgfetlveke wisfghrfal rvghgndnha dadrspiflq fvdcvwqmtr qfpsafefne
      541 lflitildhl ysclfgtflc nceqqrfked vytktislws yinsqldefs npffvnyenh
      601 vlypvaslsh lelwvnyyvr wnprmrpqmp ihqnlkella vraelqkrve glqrevatra
      661 vssssergss pshsatsvht sv
//
LOCUS       NP_002845                110 aa            linear   PRI 20-NOV-2025
DEFINITION  parvalbumin alpha [Homo sapiens].
ACCESSION   NP_002845
VERSION     NP_002845.1
DBSOURCE    REFSEQ: accession NM_002854.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 110)
  AUTHORS   O'Malley,A., Ray,J.M., Kitlas,P., Ruethers,T., Kapingidza,A.B.,
            Cierpicki,T., Lopata,A., Kowal,K. and Chruszcz,M.
  TITLE     Comparative studies of seafood and reptile alpha- and
            beta-parvalbumins
  JOURNAL   Protein Sci 33 (12), e5226 (2024)
   PUBMED   39584689
REFERENCE   2  (residues 1 to 110)
  AUTHORS   O'Brien,J.T., Jalilvand,S.P., Suji,N.A., Jupelly,R.K., Phensy,A.,
            Mwirigi,J.M., Elahi,H., Price,T.J. and Kroener,S.
  TITLE     Elevations in the Mitochondrial Matrix Protein Cyclophilin D
            Correlate With Reduced Parvalbumin Expression in the Prefrontal
            Cortex of Patients With Schizophrenia
  JOURNAL   Schizophr Bull 50 (5), 1197-1207 (2024)
   PUBMED   38412332
  REMARK    GeneRIF: Elevations in the Mitochondrial Matrix Protein Cyclophilin
            D Correlate With Reduced Parvalbumin Expression in the Prefrontal
            Cortex of Patients With Schizophrenia.
REFERENCE   3  (residues 1 to 110)
  AUTHORS   Dienel,S.J., Fish,K.N. and Lewis,D.A.
  TITLE     The Nature of Prefrontal Cortical GABA Neuron Alterations in
            Schizophrenia: Markedly Lower Somatostatin and Parvalbumin Gene
            Expression Without Missing Neurons
  JOURNAL   Am J Psychiatry 180 (7), 495-507 (2023)
   PUBMED   37073488
  REMARK    GeneRIF: The Nature of Prefrontal Cortical GABA Neuron Alterations
            in Schizophrenia: Markedly Lower Somatostatin and Parvalbumin Gene
            Expression Without Missing Neurons.
REFERENCE   4  (residues 1 to 110)
  AUTHORS   Vologzhannikova,A.A., Shevelyova,M.P., Kazakov,A.S., Sokolov,A.S.,
            Borisova,N.I., Permyakov,E.A., Kircheva,N., Nikolova,V., Dudev,T.
            and Permyakov,S.E.
  TITLE     Strontium Binding to alpha-Parvalbumin, a Canonical Calcium-Binding
            Protein of the 'EF-Hand' Family
  JOURNAL   Biomolecules 11 (8), 1158 (2021)
   PUBMED   34439824
  REMARK    GeneRIF: Strontium Binding to alpha-Parvalbumin, a Canonical
            Calcium-Binding Protein of the ''EF-Hand'' Family.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 110)
  AUTHORS   Craig,M.M., Misic,B., Pappas,I., Adapa,R.M., Menon,D.K. and
            Stamatakis,E.A.
  TITLE     Propofol sedation-induced alterations in brain connectivity reflect
            parvalbumin interneurone distribution in human cerebral cortex
  JOURNAL   Br J Anaesth 126 (4), 835-844 (2021)
   PUBMED   33386125
  REMARK    GeneRIF: Propofol sedation-induced alterations in brain
            connectivity reflect parvalbumin interneurone distribution in human
            cerebral cortex.
REFERENCE   6  (residues 1 to 110)
  AUTHORS   Winsky,L. and Kuznicki,J.
  TITLE     Distribution of calretinin, calbindin D28k, and parvalbumin in
            subcellular fractions of rat cerebellum: effects of calcium
  JOURNAL   J Neurochem 65 (1), 381-388 (1995)
   PUBMED   7790883
REFERENCE   7  (residues 1 to 110)
  AUTHORS   Fohr,U.G., Weber,B.R., Muntener,M., Staudenmann,W., Hughes,G.J.,
            Frutiger,S., Banville,D., Schafer,B.W. and Heizmann,C.W.
  TITLE     Human alpha and beta parvalbumins. Structure and tissue-specific
            expression
  JOURNAL   Eur J Biochem 215 (3), 719-727 (1993)
   PUBMED   8354278
REFERENCE   8  (residues 1 to 110)
  AUTHORS   Ritzler,J.M. and Berchtold,M.W.
  TITLE     An STS in the human parvalbumin gene (PVALB)
  JOURNAL   Nucleic Acids Res 20 (6), 1428 (1992)
   PUBMED   1561106
REFERENCE   9  (residues 1 to 110)
  AUTHORS   Ritzler,J.M., Sawhney,R., Geurts van Kessel,A.H., Grzeschik,K.H.,
            Schinzel,A. and Berchtold,M.W.
  TITLE     The genes for the highly homologous Ca(2+)-binding proteins
            oncomodulin and parvalbumin are not linked in the human genome
  JOURNAL   Genomics 12 (3), 567-572 (1992)
   PUBMED   1559707
REFERENCE   10 (residues 1 to 110)
  AUTHORS   Berchtold,M.W.
  TITLE     Parvalbumin genes from human and rat are identical in intron/exon
            organization and contain highly homologous regulatory elements and
            coding sequences
  JOURNAL   J Mol Biol 210 (3), 417-427 (1989)
   PUBMED   2614829
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z82185.1, BC069300.1,
            AI262242.1 and AA771973.1.
            
            Summary: The protein encoded by this gene is a high affinity
            calcium ion-binding protein that is structurally and functionally
            similar to calmodulin and troponin C. The encoded protein is
            thought to be involved in muscle relaxation. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2015].
            
            Transcript Variant: This variant (1) represents the longer
            transcript. Both variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: X63070.1, BC096112.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465402, SAMN03465403
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..110
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.3"
     Protein         1..110
                     /product="parvalbumin alpha"
                     /note="alpha-PV; alpha-parvalbumin"
                     /calculated_mol_wt=11928
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000269|PubMed:10036163; propagated from
                     UniProtKB/Swiss-Prot (P20472.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02625; propagated from
                     UniProtKB/Swiss-Prot (P20472.2)"
     Region          9..109
                     /region_name="EFh_parvalbumin_alpha"
                     /note="EF-hand, calcium binding motif, found in
                     alpha-parvalbumin; cd16254"
                     /db_xref="CDD:319997"
     Region          9..38
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:319997"
     Site            24
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02625; propagated from
                     UniProtKB/Swiss-Prot (P20472.2)"
     Region          43..72
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:319997"
     Site            order(52,54,56,60,63,91,93,95,102)
                     /site_type="other"
                     /note="Ca binding site [ion binding]"
                     /db_xref="CDD:319997"
     Region          82..109
                     /region_name="EF-hand motif"
                     /note="EF-hand motif [structural motif]"
                     /db_xref="CDD:319997"
     CDS             1..110
                     /gene="PVALB"
                     /gene_synonym="D22S749"
                     /coded_by="NM_002854.3:77..409"
                     /db_xref="CCDS:CCDS13933.1"
                     /db_xref="GeneID:5816"
                     /db_xref="HGNC:HGNC:9704"
                     /db_xref="MIM:168890"
ORIGIN      
        1 msmtdllnae dikkavgafs atdsfdhkkf fqmvglkkks addvkkvfhm ldkdksgfie
       61 edelgfilkg fspdardlsa ketkmlmaag dkdgdgkigv defstlvaes
//
LOCUS       NP_066960                316 aa            linear   PRI 20-NOV-2025
DEFINITION  BTB/POZ domain-containing adapter for CUL3-mediated RhoA
            degradation protein 2 [Homo sapiens].
ACCESSION   NP_066960
VERSION     NP_066960.1
DBSOURCE    REFSEQ: accession NM_021137.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 316)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 316)
  AUTHORS   Lv,D., Chen,Y., Tang,L., Tian,Y., Ren,D., Jian,N. and Shen,T.
  TITLE     HECTD2/TNFAIP1 Axis Regulating the p38/JNK Pathway to Promote an
            Inflammatory Response in Renal Cell Carcinoma Cells
  JOURNAL   In Vivo 38 (3), 1094-1103 (2024)
   PUBMED   38688591
  REMARK    GeneRIF: HECTD2/TNFAIP1 Axis Regulating the p38/JNK Pathway to
            Promote an Inflammatory Response in Renal Cell Carcinoma Cells.
REFERENCE   3  (residues 1 to 316)
  AUTHORS   Wang,W., Gao,W., Gong,P., Song,W., Bu,X., Hou,J., Zhang,L. and
            Zhao,B.
  TITLE     Neuronal-specific TNFAIP1 ablation attenuates postoperative
            cognitive dysfunction via targeting SNAP25 for K48-linked
            ubiquitination
  JOURNAL   Cell Commun Signal 21 (1), 356 (2023)
   PUBMED   38102610
  REMARK    GeneRIF: Neuronal-specific TNFAIP1 ablation attenuates
            postoperative cognitive dysfunction via targeting SNAP25 for
            K48-linked ubiquitination.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 316)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   5  (residues 1 to 316)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 316)
  AUTHORS   Suzuki,H., Fukunishi,Y., Kagawa,I., Saito,R., Oda,H., Endo,T.,
            Kondo,S., Bono,H., Okazaki,Y. and Hayashizaki,Y.
  TITLE     Protein-protein interaction panel using mouse full-length cDNAs
  JOURNAL   Genome Res 11 (10), 1758-1765 (2001)
   PUBMED   11591653
REFERENCE   7  (residues 1 to 316)
  AUTHORS   Pandey,A., Shao,H., Marks,R.M., Polverini,P.J. and Dixit,V.M.
  TITLE     Role of B61, the ligand for the Eck receptor tyrosine kinase, in
            TNF-alpha-induced angiogenesis
  JOURNAL   Science 268 (5210), 567-569 (1995)
   PUBMED   7536959
REFERENCE   8  (residues 1 to 316)
  AUTHORS   Wolf,F.W., Marks,R.M., Sarma,V., Byers,M.G., Katz,R.W., Shows,T.B.
            and Dixit,V.M.
  TITLE     Characterization of a novel tumor necrosis factor-alpha-induced
            endothelial primary response gene
  JOURNAL   J Biol Chem 267 (2), 1317-1326 (1992)
   PUBMED   1370465
REFERENCE   9  (residues 1 to 316)
  AUTHORS   Holzman,L.B., Marks,R.M. and Dixit,V.M.
  TITLE     A novel immediate-early response gene of endothelium is induced by
            cytokines and encodes a secreted protein
  JOURNAL   Mol Cell Biol 10 (11), 5830-5838 (1990)
   PUBMED   2233719
REFERENCE   10 (residues 1 to 316)
  AUTHORS   Dixit,V.M., Green,S., Sarma,V., Holzman,L.B., Wolf,F.W.,
            O'Rourke,K., Ward,P.A., Prochownik,E.V. and Marks,R.M.
  TITLE     Tumor necrosis factor-alpha induction of novel gene products in
            human endothelial cells including a macrophage-specific chemotaxin
  JOURNAL   J Biol Chem 265 (5), 2973-2978 (1990)
   PUBMED   2406243
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC003694.2.
            
            Summary: This gene was identified as a gene whose expression can be
            induced by the tumor necrosis factor alpha (TNF) in umbilical vein
            endothelial cells. Studies of a similar gene in mouse suggest that
            the expression of this gene is developmentally regulated in a
            tissue-specific manner. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC003694.2, SRR1803611.75799.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000226225.7/ ENSP00000226225.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..316
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..316
                     /product="BTB/POZ domain-containing adapter for
                     CUL3-mediated RhoA degradation protein 2"
                     /note="BTB/POZ domain-containing protein TNFAIP1; tumor
                     necrosis factor, alpha-induced protein 1 (endothelial);
                     tumor necrosis factor, alpha induced protein 1"
                     /calculated_mol_wt=36073
     Region          26..129
                     /region_name="BTB_POZ_TNFAIP1_BACURD2"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in tumor necrosis
                     factor, alpha-induced protein 1, endothelial (TNFAIP1);
                     cd18401"
                     /db_xref="CDD:349709"
     Site            order(28..29,33,35..41,45,66,68,70,72,82,85,88..89,100)
                     /site_type="other"
                     /note="putative tetramer interface [polypeptide binding]"
                     /db_xref="CDD:349709"
     Region          268..287
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13829.1)"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13829.1)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:19851886,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13829.1)"
     CDS             1..316
                     /gene="TNFAIP1"
                     /gene_synonym="B12; B61; BTBD34; EDP1; hBACURD2"
                     /coded_by="NM_021137.5:211..1161"
                     /db_xref="CCDS:CCDS11227.1"
                     /db_xref="GeneID:7126"
                     /db_xref="HGNC:HGNC:11894"
                     /db_xref="MIM:191161"
ORIGIN      
        1 msgdtclcpa sgakpklsgf kggglgnkyv qlnvggslyy ttvraltrhd tmlkamfsgr
       61 mevltdkegw ilidrcgkhf gtilnylrdd titlpqnrqe ikelmaeaky yliqglvnmc
      121 qsalqdkkds yqpvcnipii tslkeeerli esstkpvvkl lynrsnnkys ytsnsddhll
      181 knielfdkls lrfngrvlfi kdvigdeicc wsfygqgrkl aevcctsivy atekkqtkve
      241 fpeariyeet lnvllyetpr vpdnslleat srsrsqasps edeetfelrd rvrrihvkry
      301 styddrqlgh qsthrd
//
LOCUS       NP_001308514             296 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 18 [Homo sapiens].
ACCESSION   NP_001308514
VERSION     NP_001308514.1
DBSOURCE    REFSEQ: accession NM_001321585.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 296)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.37683.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..296
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 18"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=33493
     Region          <1..107
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          164..291
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..296
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321585.2:1353..2243"
                     /note="isoform 18 is encoded by transcript variant 26"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mwacgvilyi llvgyppfwd edqhrlyqqi kagaydfpsp ewdtvtpeak dlinkmltin
       61 pakritasea lkhpwicqrs tvasmmhrqe tvdclkkfna rrklkgailt tmlatrnfsa
      121 aksllkkpdg vkepqttvih npdgnkeste ssnttieded vkarkqeiik vteqlieain
      181 ngdfeaytki cdpgltafep ealgnlvegm dfhrfyfena lsksnkpiht iilnphvhlv
      241 gddaaciayi rltqymdgsg mpktmqseet rvwhrrdgkw qnvhfhrsgs ptvpin
//
LOCUS       NP_057065                489 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit alpha
            isoform 1 [Homo sapiens].
ACCESSION   NP_057065
VERSION     NP_057065.2
DBSOURCE    REFSEQ: accession NM_015981.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 489)
  AUTHORS   Zheng,P., Hu,Z., Shen,Y., Gu,L., Ouyang,Y., Duan,Y., Ji,G.,
            Dong,B., Lin,Y., Wen,T., Tian,Q., Hou,Y., Zhou,Q., Sun,X., Chen,X.,
            Wang,K.L., Luo,S., Wu,S., Sun,Y., Li,M., Xiao,L., Wu,Q., Meng,Y.,
            Liu,G., Wang,Z., Bai,X., Duan,S., Ding,Y., Bi,Y., Wang,Y., Li,G.,
            Liu,X., Lu,Z., Wu,X., Tang,Z. and Xu,D.
  TITLE     PSAT1 impairs ferroptosis and reduces immunotherapy efficacy via
            GPX4 hydroxylation
  JOURNAL   Nat Chem Biol 21 (9), 1420-1432 (2025)
   PUBMED   40281343
REFERENCE   2  (residues 1 to 489)
  AUTHORS   Lin,J., Xia,H., Yu,J., Wang,Y., Wang,H., Xie,D., Cheng,C., Lu,L.,
            Bian,T., Wu,Y. and Liu,Q.
  TITLE     circADAMTS6 via stabilizing CAMK2A is involved in smoking-induced
            emphysema through driving M2 macrophage polarization
  JOURNAL   Environ Int 190, 108832 (2024)
   PUBMED   38936066
  REMARK    GeneRIF: circADAMTS6 via stabilizing CAMK2A is involved in
            smoking-induced emphysema through driving M2 macrophage
            polarization.
REFERENCE   3  (residues 1 to 489)
  AUTHORS   Zhang,Y., Xia,M., Zhao,T., Zhang,Q., Li,R. and Yang,L.
  TITLE     Camk2a suppresses denervated muscle atrophy by maintaining the Ca2+
            homeostasis in muscle cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (11), 25-29 (2023)
   PUBMED   38015546
  REMARK    GeneRIF: Camk2a suppresses denervated muscle atrophy by maintaining
            the Ca2+ homeostasis in muscle cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 489)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 489)
  AUTHORS   Alphonse,N., Wanford,J.J., Voak,A.A., Gay,J., Venkhaya,S.,
            Burroughs,O., Mathew,S., Lee,T., Evans,S.L., Zhao,W., Frowde,K.,
            Alrehaili,A., Dickenson,R.E., Munk,M., Panina,S., Mahmood,I.F.,
            Llorian,M., Stanifer,M.L., Boulant,S., Berchtold,M.W.,
            Bergeron,J.R.C., Wack,A., Lesser,C.F. and Odendall,C.
  TITLE     A family of conserved bacterial virulence factors dampens
            interferon responses by blocking calcium signaling
  JOURNAL   Cell 185 (13), 2354-2369 (2022)
   PUBMED   35568036
REFERENCE   6  (residues 1 to 489)
  AUTHORS   Bredt,D.S., Ferris,C.D. and Snyder,S.H.
  TITLE     Nitric oxide synthase regulatory sites. Phosphorylation by cyclic
            AMP-dependent protein kinase, protein kinase C, and
            calcium/calmodulin protein kinase; identification of flavin and
            calmodulin binding sites
  JOURNAL   J Biol Chem 267 (16), 10976-10981 (1992)
   PUBMED   1375933
REFERENCE   7  (residues 1 to 489)
  AUTHORS   Omary,M.B., Baxter,G.T., Chou,C.F., Riopel,C.L., Lin,W.Y. and
            Strulovici,B.
  TITLE     PKC epsilon-related kinase associates with and phosphorylates
            cytokeratin 8 and 18
  JOURNAL   J Cell Biol 117 (3), 583-593 (1992)
   PUBMED   1374067
REFERENCE   8  (residues 1 to 489)
  AUTHORS   Wegner,M., Cao,Z. and Rosenfeld,M.G.
  TITLE     Calcium-regulated phosphorylation within the leucine zipper of
            C/EBP beta
  JOURNAL   Science 256 (5055), 370-373 (1992)
   PUBMED   1314426
REFERENCE   9  (residues 1 to 489)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   10 (residues 1 to 489)
  AUTHORS   Tokui,T., Yamauchi,T., Yano,T., Nishi,Y., Kusagawa,M., Yatani,R.
            and Inagaki,M.
  TITLE     Ca2(+)-calmodulin-dependent protein kinase II phosphorylates
            various types of non-epithelial intermediate filament proteins
  JOURNAL   Biochem Biophys Res Commun 169 (3), 896-904 (1990)
   PUBMED   2114109
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK289776.1, BF951952.1,
            AC011372.7 and BC040457.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 29, 2002 this sequence version replaced NP_057065.1.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinases family, and to the Ca(2+)/calmodulin-dependent
            protein kinases subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. This calcium
            calmodulin-dependent protein kinase is composed of four different
            chains: alpha, beta, gamma, and delta. The alpha chain encoded by
            this gene is required for hippocampal long-term potentiation (LTP)
            and spatial learning. In addition to its calcium-calmodulin
            (CaM)-dependent activity, this protein can undergo
            autophosphorylation, resulting in CaM-independent activity. Several
            transcript variants encoding distinct isoforms have been identified
            for this gene. [provided by RefSeq, Jun 2018].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.208418.1,
                                           SRR1660809.257351.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1966682,
                                           SAMEA1968189 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000671881.1/ ENSP00000500386.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..489
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..489
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit alpha isoform 1"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II alpha; CaM-kinase II alpha chain;
                     calcium/calmodulin-dependent protein kinase II alpha-B
                     subunit; CaM kinase II alpha subunit; CaMK-II alpha
                     subunit; calcium/calmodulin-dependent protein kinase type
                     II alpha chain; calcium/calmodulin-dependent protein
                     kinase type II subunit alpha; caMK-II subunit alpha; caM
                     kinase II subunit alpha"
                     /calculated_mol_wt=55189
     Region          11..302
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(19..23,27,40,42,73,89..92,96,98,134..135,137,
                     139..140,142,155..156,159,174..178,180)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(19..22,27,40,42,73,89..92,96,139..140,142,155..156)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(23,96,98,134..135,137,139,159,174..178,180)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(155..165,168..178)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(293,295..302)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          357..484
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..489
                     /gene="CAMK2A"
                     /gene_synonym="CAMKA; CaMKIIalpha; CaMKIINalpha; MRD53;
                     MRT63"
                     /coded_by="NM_015981.4:149..1618"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43387.1"
                     /db_xref="GeneID:815"
                     /db_xref="HGNC:HGNC:1460"
                     /db_xref="MIM:114078"
ORIGIN      
        1 matitctrft eeyqlfeelg kgafsvvrrc vkvlagqeya akiintkkls ardhqklere
       61 aricrllkhp nivrlhdsis eeghhylifd lvtggelfed ivareyysea dashciqqil
      121 eavlhchqmg vvhrdlkpen lllasklkga avkladfgla ievegeqqaw fgfagtpgyl
      181 spevlrkdpy gkpvdlwacg vilyillvgy ppfwdedqhr lyqqikagay dfpspewdtv
      241 tpeakdlink mltinpskri taaealkhpw ishrstvasc mhrqetvdcl kkfnarrklk
      301 gailttmlat rnfsggksgg nkksdgvkkr kssssvqlme ssestnttie dedtkvrkqe
      361 iikvteqlie aisngdfesy tkmcdpgmta fepealgnlv egldfhrfyf enlwsrnskp
      421 vhttilnphi hlmgdesaci ayiritqyld aggiprtaqs eetrvwhrrd gkwqivhfhr
      481 sgapsvlph
//
LOCUS       NP_004434                998 aa            linear   PRI 20-NOV-2025
DEFINITION  ephrin type-B receptor 3 precursor [Homo sapiens].
ACCESSION   NP_004434
VERSION     NP_004434.2
DBSOURCE    REFSEQ: accession NM_004443.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 998)
  AUTHORS   Gao,X., Zhang,R., He,Y., Wang,X., Bao,W., Feng,X., Chai,J. and
            Wang,J.
  TITLE     EphB3 protein is a potential ancillary diagnostic biomarker for
            thyroid cancers
  JOURNAL   Ann Diagn Pathol 69, 152262 (2024)
   PUBMED   38150866
  REMARK    GeneRIF: EphB3 protein is a potential ancillary diagnostic
            biomarker for thyroid cancers.
REFERENCE   2  (residues 1 to 998)
  AUTHORS   Zhang,F., Shi,H., Xue,H., Li,H., Li,C. and Han,Q.
  TITLE     Up-regulated lncRNA SNHG9 mediates the pathogenesis of dilated
            cardiomyopathy via miR-326/EPHB3 axis
  JOURNAL   J Thromb Thrombolysis 55 (4), 634-648 (2023)
   PUBMED   37004604
  REMARK    GeneRIF: Up-regulated lncRNA SNHG9 mediates the pathogenesis of
            dilated cardiomyopathy via miR-326/EPHB3 axis.
REFERENCE   3  (residues 1 to 998)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 998)
  AUTHORS   Lee,T.H., Heo,J.H., Jeong,J.Y., Lee,G.H., Park,D.S. and Kim,T.H.
  TITLE     Low Expression of EphB2, EphB3, and EphB4 in Bladder Cancer: Novel
            Potential Indicators of Muscular Invasion
  JOURNAL   Yonsei Med J 62 (8), 679-690 (2021)
   PUBMED   34296545
  REMARK    GeneRIF: Low Expression of EphB2, EphB3, and EphB4 in Bladder
            Cancer: Novel Potential Indicators of Muscular Invasion.
REFERENCE   5  (residues 1 to 998)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 998)
  AUTHORS   Zhou,R.
  TITLE     The Eph family receptors and ligands
  JOURNAL   Pharmacol Ther 77 (3), 151-181 (1998)
   PUBMED   9576626
  REMARK    Review article
REFERENCE   7  (residues 1 to 998)
  AUTHORS   Bergemann,A.D., Zhang,L., Chiang,M.K., Brambilla,R., Klein,R. and
            Flanagan,J.G.
  TITLE     Ephrin-B3, a ligand for the receptor EphB3, expressed at the
            midline of the developing neural tube
  JOURNAL   Oncogene 16 (4), 471-480 (1998)
   PUBMED   9484836
REFERENCE   8  (residues 1 to 998)
  AUTHORS   Flanagan,J.G. and Vanderhaeghen,P.
  TITLE     The ephrins and Eph receptors in neural development
  JOURNAL   Annu Rev Neurosci 21, 309-345 (1998)
   PUBMED   9530499
  REMARK    Review article
REFERENCE   9  (residues 1 to 998)
  AUTHORS   Bohme,B., VandenBos,T., Cerretti,D.P., Park,L.S., Holtrich,U.,
            Rubsamen-Waigmann,H. and Strebhardt,K.
  TITLE     Cell-cell adhesion mediated by binding of membrane-anchored ligand
            LERK-2 to the EPH-related receptor human embryonal kinase 2
            promotes tyrosine kinase activity
  JOURNAL   J Biol Chem 271 (40), 24747-24752 (1996)
   PUBMED   8798744
REFERENCE   10 (residues 1 to 998)
  AUTHORS   Bohme,B., Holtrich,U., Wolf,G., Luzius,H., Grzeschik,K.H.,
            Strebhardt,K. and Rubsamen-Waigmann,H.
  TITLE     PCR mediated detection of a new human receptor-tyrosine-kinase, HEK
            2
  JOURNAL   Oncogene 8 (10), 2857-2862 (1993)
   PUBMED   8397371
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112643.12, CB993133.1,
            BC052968.1 and X75208.1.
            
            On Dec 21, 2001 this sequence version replaced NP_004434.1.
            
            Summary: Ephrin receptors and their ligands, the ephrins, mediate
            numerous developmental processes, particularly in the nervous
            system. Based on their structures and sequence relationships,
            ephrins are divided into the ephrin-A (EFNA) class, which are
            anchored to the membrane by a glycosylphosphatidylinositol linkage,
            and the ephrin-B (EFNB) class, which are transmembrane proteins.
            The Eph family of receptors are divided into two groups based on
            the similarity of their extracellular domain sequences and their
            affinities for binding ephrin-A and ephrin-B ligands. Ephrin
            receptors make up the largest subgroup of the receptor tyrosine
            kinase (RTK) family. This gene encodes a receptor for ephrin-B
            family members. [provided by RefSeq, Mar 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC052968.1, X75208.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330394.3/ ENSP00000332118.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..998
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..998
                     /product="ephrin type-B receptor 3 precursor"
                     /EC_number="2.7.10.1"
                     /note="ephrin type-B receptor 3; human embryo kinase 2;
                     tyrosine-protein kinase TYRO6; embryonic kinase 2;
                     EPH-like tyrosine kinase 2"
                     /calculated_mol_wt=106522
     sig_peptide     1..37
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3827
     Region          39..211
                     /region_name="EphR_LBD_B3"
                     /note="Ligand Binding Domain of Ephrin type-B Receptor 3;
                     cd10478"
                     /db_xref="CDD:198446"
     Site            order(47..49,51,63..66,68,72,74,76,79,112..114,118,120,
                     166,168,170..171,173..174,199,201,203)
                     /site_type="other"
                     /note="ephrin binding site [polypeptide binding]"
                     /db_xref="CDD:198446"
     Region          272..316
                     /region_name="Ephrin_rec_like"
                     /note="Tyrosine-protein kinase ephrin type A/B
                     receptor-like; pfam07699"
                     /db_xref="CDD:429604"
     Site            order(340,417,433)
                     /site_type="active"
                     /note="Interdomain contacts [active]"
                     /db_xref="CDD:238020"
     Region          341..436
                     /region_name="fn3"
                     /note="Fibronectin type III domain; pfam00041"
                     /db_xref="CDD:394996"
     Site            order(434..435,437..438)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          <473..542
                     /region_name="FN3"
                     /note="Fibronectin type 3 domain; One of three types of
                     internal repeats found in the plasma protein fibronectin.
                     Its tenth fibronectin type III repeat contains an RGD cell
                     recognition sequence in a flexible loop between 2 strands.
                     Approximately 2% of all...; cd00063"
                     /db_xref="CDD:238020"
     Site            order(531..532,534..535)
                     /site_type="active"
                     /note="Cytokine receptor motif [active]"
                     /db_xref="CDD:238020"
     Region          560..630
                     /region_name="EphA2_TM"
                     /note="Ephrin type-A receptor 2 transmembrane domain;
                     pfam14575"
                     /db_xref="CDD:464211"
     Region          628..896
                     /region_name="PTKc_EphR_B"
                     /note="Catalytic domain of the Protein Tyrosine Kinases,
                     Class EphB Ephrin Receptors; cd05065"
                     /db_xref="CDD:173638"
     Site            order(639..643,647,663,665,711..712,714,718,758,762..763,
                     765,776,797..801,810,844)
                     /site_type="active"
                     /db_xref="CDD:173638"
     Site            order(639..641,643,647,663,665,711..712,714,718,763,765,
                     776)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:173638"
     Site            order(758,762,797..801,810,844)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:173638"
     Site            775..803
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:173638"
     Region          922..990
                     /region_name="SAM_superfamily"
                     /note="SAM (Sterile alpha motif); cl15755"
                     /db_xref="CDD:472832"
     CDS             1..998
                     /gene="EPHB3"
                     /gene_synonym="EK2; ETK2; HEK2; TYRO6"
                     /coded_by="NM_004443.4:452..3448"
                     /db_xref="CCDS:CCDS3268.1"
                     /db_xref="GeneID:2049"
                     /db_xref="HGNC:HGNC:3394"
                     /db_xref="MIM:601839"
ORIGIN      
        1 mararppppp spppgllpll ppllllplll lpagcralee tlmdtkwvts elawtshpes
       61 gweevsgyde amnpirtyqv cnvressqnn wlrtgfiwrr dvqrvyvelk ftvrdcnsip
      121 nipgscketf nlfyyeadsd vasasspfwm enpyvkvdti apdesfsrld agrvntkvrs
      181 fgplskagfy lafqdqgacm slisvrafyk kcasttagfa lfpetltgae ptslviapgt
      241 cipnavevsv plklycngdg ewmvpvgact catghepaak esqcrpcppg sykakqgegp
      301 clpcppnsrt tspaasictc hnnfyradsd sadsacttvp spprgvisnv netslilews
      361 eprdlggrdd llynvickkc hgaggasacs rcddnvefvp rqlglterrv hishllahtr
      421 ytfevqavng vsgksplppr yaavnittnq aapsevptlr lhsssgsslt lswapperpn
      481 gvildyemky feksegiast vtsqmnsvql dglrpdaryv vqvrartvag ygqysrpaef
      541 ettsergsga qqlqeqlpli vgsataglvf vvavvviaiv clrkqrhgsd seyteklqqy
      601 iapgmkvyid pftyedpnea vrefakeidv scvkieevig agefgevcrg rlkqpgrrev
      661 fvaiktlkvg yterqrrdfl seasimgqfd hpniirlegv vtksrpvmil tefmencald
      721 sflrlndgqf tviqlvgmlr giaagmkyls emnyvhrdla arnilvnsnl vckvsdfgls
      781 rfleddpsdp tytsslggki pirwtapeai ayrkftsasd vwsygivmwe vmsygerpyw
      841 dmsnqdvina veqdyrlppp mdcptalhql mldcwvrdrn lrpkfsqivn tldklirnaa
      901 slkviasaqs gmsqplldrt vpdyttfttv gdwldaikmg rykesfvsag fasfdlvaqm
      961 taedllrigv tlaghqkkil ssiqdmrlqm nqtlpvqv
//
LOCUS       NP_002687                172 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-directed RNA polymerase II subunit RPB7 [Homo sapiens].
ACCESSION   NP_002687
VERSION     NP_002687.1
DBSOURCE    REFSEQ: accession NM_002696.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Zhang,Y., Zhang,T. and Chen,Y.
  TITLE     Comprehensive Analysis of Gene Expression Profiles and DNA
            Methylome reveals Oas1, Ppie, Polr2g as Pathogenic Target Genes of
            Gestational Diabetes Mellitus
  JOURNAL   Sci Rep 8 (1), 16244 (2018)
   PUBMED   30389953
  REMARK    GeneRIF: Study of datasets analyzing the gene expression profiles
            and DNA methylation data of gestational Diabetes Mellitus (GDM) and
            confirmed through real time PCR in placenta tissue of three GDM
            samples and three normal samples identified Oas1, Ppie, Polr2g as
            possible pathogenic target genes of GDM by combining
            protein-protein interaction analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Higman,B., Shugar,D.H., Stark,C.P., Ekstrom,G., Koppes,M.N.,
            Lynett,P., Dufresne,A., Haeussler,P.J., Geertsema,M., Gulick,S.,
            Mattox,A., Venditti,J.G., Walton,M.A.L., McCall,N., Mckittrick,E.,
            MacInnes,B., Bilderback,E.L., Tang,H., Willis,M.J., Richmond,B.,
            Reece,R.S., Larsen,C., Olson,B., Capra,J., Ayca,A., Bloom,C.,
            Williams,H., Bonno,D., Weiss,R., Keen,A., Skanavis,V. and Loso,M.
  TITLE     The 2015 landslide and tsunami in Taan Fiord, Alaska
  JOURNAL   Sci Rep 8 (1), 12993 (2018)
   PUBMED   30190595
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Jishage,M., Yu,X., Shi,Y., Ganesan,S.J., Chen,W.Y., Sali,A.,
            Chait,B.T., Asturias,F.J. and Roeder,R.G.
  TITLE     Architecture of Pol II(G) and molecular mechanism of transcription
            regulation by Gdown1
  JOURNAL   Nat Struct Mol Biol 25 (9), 859-867 (2018)
   PUBMED   30190596
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Ujvari,A. and Luse,D.S.
  TITLE     RNA emerging from the active site of RNA polymerase II interacts
            with the Rpb7 subunit
  JOURNAL   Nat Struct Mol Biol 13 (1), 49-54 (2006)
   PUBMED   16327806
  REMARK    GeneRIF: the emerging transcript cross-links to the Rpb7 subunit of
            RNA polymerase II in various complexes containing 26- to 32-nt
            transcripts
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Cramer,P., Bushnell,D.A., Fu,J., Gnatt,A.L., Maier-Davis,B.,
            Thompson,N.E., Burgess,R.R., Edwards,A.M., David,P.R. and
            Kornberg,R.D.
  TITLE     Architecture of RNA polymerase II and implications for the
            transcription mechanism
  JOURNAL   Science 288 (5466), 640-649 (2000)
   PUBMED   10784442
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Schoen,T.J., Chandrasekharappa,S.C., Guru,S.C., Mazuruk,K.,
            Chader,G.J. and Rodriguez,I.R.
  TITLE     Human gene for the RNA polymerase II seventh subunit (hsRPB7):
            structure, expression and chromosomal localization
  JOURNAL   Biochim Biophys Acta 1353 (1), 39-49 (1997)
   PUBMED   9256063
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Kato,H., Sumimoto,H., Pognonec,P., Chen,C.H., Rosen,C.A. and
            Roeder,R.G.
  TITLE     HIV-1 Tat acts as a processivity factor in vitro in conjunction
            with cellular elongation factors
  JOURNAL   Genes Dev 6 (4), 655-666 (1992)
   PUBMED   1559613
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Jacob,G.A., Luse,S.W. and Luse,D.S.
  TITLE     Abortive initiation is increased only for the weakest members of a
            set of down mutants of the adenovirus 2 major late promoter
  JOURNAL   J Biol Chem 266 (33), 22537-22544 (1991)
   PUBMED   1939271
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Southgate,C., Zapp,M.L. and Green,M.R.
  TITLE     Activation of transcription by HIV-1 Tat protein tethered to
            nascent RNA through another protein
  JOURNAL   Nature 345 (6276), 640-642 (1990)
   PUBMED   2190099
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BG530809.1, BC112162.1 and
            AW016747.1.
            
            Summary: This gene encodes the seventh largest subunit of RNA
            polymerase II, the polymerase responsible for synthesizing
            messenger RNA in eukaryotes. The protein functions in transcription
            initiation, and is also thought to help stabilize transcribing
            polyermase molecules during elongation. [provided by RefSeq, Jan
            2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.238328.1,
                                           SRR1163655.390074.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000301788.12/ ENSP00000301788.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3"
     Protein         1..172
                     /product="DNA-directed RNA polymerase II subunit RPB7"
                     /EC_number="2.7.7.6"
                     /note="DNA directed RNA polymerase II 19 kda polypeptide;
                     RNA polymerase II seventh subunit; RNA polymerase II
                     subunit B7; DNA-directed RNA polymerase II subunit G;
                     polymerase (RNA) II subunit G; DNA-directed RNA polymerase
                     II 19 kDa polypeptide; RNA polymerase II 19 kDa subunit;
                     polymerase (RNA) II (DNA directed) polypeptide G"
                     /calculated_mol_wt=19163
     Region          1..169
                     /region_name="PTZ00162"
                     /note="DNA-directed RNA polymerase II subunit 7;
                     Provisional"
                     /db_xref="CDD:240298"
     CDS             1..172
                     /gene="POLR2G"
                     /gene_synonym="hRPB19; hsRPB7; RPB19; RPB7"
                     /coded_by="NM_002696.3:70..588"
                     /db_xref="CCDS:CCDS31585.1"
                     /db_xref="GeneID:5436"
                     /db_xref="HGNC:HGNC:9194"
                     /db_xref="MIM:602013"
ORIGIN      
        1 mfyhislehe illhpryfgp nllntvkqkl ftevegtctg kygfviavtt idnigagviq
       61 pgrgfvlypv kykaivfrpf kgevvdavvt qvnkvglfte igpmscfisr hsipsemefd
      121 pnsnppcykt mdediviqqd deirlkivgt rvdkndifai gslmddylgl vs
//
LOCUS       NP_001229828             933 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 6 regulatory subunit 2 isoform
            2 [Homo sapiens].
ACCESSION   NP_001229828
VERSION     NP_001229828.1
DBSOURCE    REFSEQ: accession NM_001242899.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Marquez,J., Kohli,M., Arteta,B., Chang,S., Li,W.B., Goldblatt,M.
            and Vidal-Vanaclocha,F.
  TITLE     Identification of hepatic microvascular adhesion-related genes of
            human colon cancer cells using random homozygous gene perturbation
  JOURNAL   Int J Cancer 133 (9), 2113-2122 (2013)
   PUBMED   23629598
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Zeng,K., Bastos,R.N., Barr,F.A. and Gruneberg,U.
  TITLE     Protein phosphatase 6 regulates mitotic spindle formation by
            controlling the T-loop phosphorylation state of Aurora A bound to
            its activator TPX2
  JOURNAL   J Cell Biol 191 (7), 1315-1332 (2010)
   PUBMED   21187329
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Stefansson,B., Ohama,T., Daugherty,A.E. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 regulatory subunits composed of ankyrin
            repeat domains
  JOURNAL   Biochemistry 47 (5), 1442-1451 (2008)
   PUBMED   18186651
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Stefansson,B. and Brautigan,D.L.
  TITLE     Protein phosphatase 6 subunit with conserved Sit4-associated
            protein domain targets IkappaBepsilon
  JOURNAL   J Biol Chem 281 (32), 22624-22634 (2006)
   PUBMED   16769727
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX545851.6, BC032664.1 and
            AL096767.14.
            
            Summary: The protein encoded by this gene is a regulatory protein
            for the protein phosphatase-6 catalytic subunit. Together, these
            proteins act as a significant T-loop phosphatase for Aurora A, an
            essential mitotic kinase. Loss of function of either the regulatory
            or catalytic subunit of protein phosphatase-6 interferes with
            spindle formation and chromosome alignment. [provided by RefSeq,
            May 2017].
            
            Transcript Variant: This variant (2) lacks a coding exon and uses
            an alternate splice site in the coding region, but maintains the
            reading frame, compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.33"
     Protein         1..933
                     /product="serine/threonine-protein phosphatase 6
                     regulatory subunit 2 isoform 2"
                     /note="SAPS domain family, member 2;
                     serine/threonine-protein phosphatase 6 regulatory subunit
                     2"
                     /calculated_mol_wt=101271
     Region          128..533
                     /region_name="SAPS"
                     /note="SIT4 phosphatase-associated protein; pfam04499"
                     /db_xref="CDD:398279"
     Region          <677..928
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..933
                     /gene="PPP6R2"
                     /gene_synonym="KIAA0685; PP6R2; SAP190; SAPS2"
                     /coded_by="NM_001242899.2:372..3173"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS56235.1"
                     /db_xref="GeneID:9701"
                     /db_xref="HGNC:HGNC:19253"
                     /db_xref="MIM:610877"
ORIGIN      
        1 mfwkfdlntt shvdklldke hvtlqelmde ddilqeckaq nqklldflcr qqcmeelvsl
       61 itqdppldme ekvrfkypnt acelltcdvp qisdrlggde sllsllydfl dhepplnpll
      121 asffsktign liarkteqvi tflkkkdkfi slvlkhigts almdlllrlv scvepaglrq
      181 dvlhwlneek viqrlvelih psqdedrqsn asqtlcdivr lgrdqgsqlq ealepdpllt
      241 alesrqdcve qllknmfdgd rtesclvsgt qvlltlletr rvgteglvds fsqglersya
      301 vsssvlhgie prlkdfhqll lnppkkkail ttigvleepl gnarlhgarl maallhtntp
      361 sinqelcrln tmdllldlff kytwnnflhf qvelciaail shaareerte asgsesrvep
      421 phengnrsle tpqpaaslpd ntmvthlfqk cclvqrilea weandhtqaa ggmrrgnmgh
      481 ltrianavvq nlergpvqth isevirglpa dcrgrwesfv eetltetnrr ntvdlafsdy
      541 qiqqmtanfv dqfgfndeef adqddninap fdriaeinfn idadedspsa alfeaccsdr
      601 iqpfdddede diwedsdtrc aarvmarprf gaphasescs kngperggqd gkasleahrd
      661 apgagappap gkkeappveg dsegamwtav fdepanstpt apgvvrdvgs svwaagtsap
      721 eekgwakftd fqpfccsesg prcsspvdte cshaegsrsq gpekafspas pcawnvcvtr
      781 kapllasdss ssggshsedg dqkaasamda vsrgpgreap plptvartee avgrvgcads
      841 rllspacpap kevtaapava vppeatvait talskagpai ptpavssala vavplgpima
      901 vtaapamvat lgtvtkdgkt dappegaaln gpv
//
LOCUS       NP_001138516             692 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier organic anion transporter family member 3A1 isoform
            2 [Homo sapiens].
ACCESSION   NP_001138516
VERSION     NP_001138516.1
DBSOURCE    REFSEQ: accession NM_001145044.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 692)
  AUTHORS   Surrer,D.B., Schusser,S., Konig,J., Fromm,M.F. and Gessner,A.
  TITLE     Transport of aromatic amino acids l-tryptophan, l-tyrosine, and
            l-phenylalanine by the organic anion transporting polypeptide
            (OATP) 3A1
  JOURNAL   FEBS J 291 (21), 4732-4743 (2024)
   PUBMED   39206635
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Bakos,E., Nemet,O., Kucsma,N., Tokesi,N., Stieger,B., Rushing,E.,
            Tokes,A.M., Kele,P., Tusnady,G.E. and Ozvegy-Laczka,C.
  TITLE     Cloning and characterization of a novel functional organic anion
            transporting polypeptide 3A1 isoform highly expressed in the human
            brain and testis
  JOURNAL   Front Pharmacol 13, 958023 (2022)
   PUBMED   36120371
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Hau,R.K., Klein,R.R., Wright,S.H. and Cherrington,N.J.
  TITLE     Localization of Xenobiotic Transporters Expressed at the Human
            Blood-Testis Barrier
  JOURNAL   Drug Metab Dispos 50 (6), 770-780 (2022)
   PUBMED   35307651
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Li,M., Wang,W., Cheng,Y., Zhang,X., Zhao,N., Tan,Y., Xie,Q.,
            Chai,J. and Pan,Q.
  TITLE     Tumor necrosis factor alpha upregulates the bile acid efflux
            transporter OATP3A1 via multiple signaling pathways in cholestasis
  JOURNAL   J Biol Chem 298 (2), 101543 (2022)
   PUBMED   34971708
  REMARK    GeneRIF: Tumor necrosis factor alpha upregulates the bile acid
            efflux transporter OATP3A1 via multiple signaling pathways in
            cholestasis.
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 692)
  AUTHORS   Hagenbuch,B. and Meier,P.J.
  TITLE     Organic anion transporting polypeptides of the OATP/ SLC21 family:
            phylogenetic classification as OATP/ SLCO superfamily, new
            nomenclature and molecular/functional properties
  JOURNAL   Pflugers Arch 447 (5), 653-665 (2004)
   PUBMED   14579113
  REMARK    Review article
REFERENCE   7  (residues 1 to 692)
  AUTHORS   Adachi,H., Suzuki,T., Abe,M., Asano,N., Mizutamari,H., Tanemoto,M.,
            Nishio,T., Onogawa,T., Toyohara,T., Kasai,S., Satoh,F., Suzuki,M.,
            Tokui,T., Unno,M., Shimosegawa,T., Matsuno,S., Ito,S. and Abe,T.
  TITLE     Molecular characterization of human and rat organic anion
            transporter OATP-D
  JOURNAL   Am J Physiol Renal Physiol 285 (6), F1188-F1197 (2003)
   PUBMED   14631946
  REMARK    GeneRIF: OATP-D plays an important role in translocating
            prostaglandins in specialized tissues and cells.
REFERENCE   8  (residues 1 to 692)
  AUTHORS   Schiffer,R., Neis,M., Holler,D., Rodriguez,F., Geier,A.,
            Gartung,C., Lammert,F., Dreuw,A., Zwadlo-Klarwasser,G., Merk,H.,
            Jugert,F. and Baron,J.M.
  TITLE     Active influx transport is mediated by members of the organic anion
            transporting polypeptide family in human epidermal keratinocytes
  JOURNAL   J Invest Dermatol 120 (2), 285-291 (2003)
   PUBMED   12542534
REFERENCE   9  (residues 1 to 692)
  AUTHORS   Patel,P., Weerasekera,N., Hitchins,M., Boyd,C.A., Johnston,D.G. and
            Williamson,C.
  TITLE     Semi quantitative expression analysis of MDR3, FIC1, BSEP, OATP-A,
            OATP-C,OATP-D, OATP-E and NTCP gene transcripts in 1st and 3rd
            trimester human placenta
  JOURNAL   Placenta 24 (1), 39-44 (2003)
   PUBMED   12495658
REFERENCE   10 (residues 1 to 692)
  AUTHORS   Tamai,I., Nezu,J., Uchino,H., Sai,Y., Oku,A., Shimane,M. and
            Tsuji,A.
  TITLE     Molecular identification and characterization of novel members of
            the human organic anion transporter (OATP) family
  JOURNAL   Biochem Biophys Res Commun 273 (1), 251-260 (2000)
   PUBMED   10873595
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC104020.10, AF205074.1, AC113190.8, BC000585.2 and AC116903.3.
            
            Transcript Variant: This variant (2) uses an alternate splice site
            in the 3' coding region and contains an alternate 3' terminal exon
            compared to variant 1. The encoded protein (isoform 2) is shorter
            and has a distinct C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000585.2, SRR1660805.515.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..692
                     /product="solute carrier organic anion transporter family
                     member 3A1 isoform 2"
                     /note="solute carrier family 21 (organic anion
                     transporter), member 11; PGE1 transporter; solute carrier
                     family 21 member 11; organic anion-transporting
                     polypeptide D; sodium-independent organic anion
                     transporter D; organic anion transporter
                     polypeptide-related protein 3"
                     /calculated_mol_wt=74242
     Region          39..563
                     /region_name="MFS_SLCO3_OATP3"
                     /note="Solute carrier organic anion transporter 3 family
                     of the Major Facilitator Superfamily of transporters;
                     cd17402"
                     /db_xref="CDD:340960"
     Site            order(53..54,57..58,61,93,191..192,194..196,199,219,
                     222..223,226,358,361..362,365..367,370,399,403,444..445,
                     449,453,506,509..510,513..514,517)
                     /site_type="other"
                     /note="putative chemical substrate binding pocket
                     [chemical binding]"
                     /db_xref="CDD:340960"
     CDS             1..692
                     /gene="SLCO3A1"
                     /gene_synonym="OATP-D; OATP-RP3; OATP3A1; OATPD; OATPRP3;
                     SLC21A11"
                     /coded_by="NM_001145044.1:202..2280"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS45354.1"
                     /db_xref="GeneID:28232"
                     /db_xref="HGNC:HGNC:10952"
                     /db_xref="MIM:612435"
ORIGIN      
        1 mqgkkpggss gggrsgelqg deaqrnkkkk kkvscfsnik iflvsecalm laqgtvgayl
       61 vsvlttlerr fnlqsadvgv iassfeignl alilfvsyfg arghrprlig cggivmalga
      121 llsalpeflt hqykyeagei rwgaegrdvc aangsggdeg pdpdlicrnr tatnmmylll
      181 igaqvllgig atpvqplgvs yiddhvrrkd sslyigilft mlvfgpacgf ilgsfctkiy
      241 vdavfidtsn lditpddprw igawwggfll cgallffssl lmfgfpqslp phsepamese
      301 qamlsereye rpkpsngvlr hplepdssas cfqqlrvipk vtkhllsnpv ftciilaacm
      361 eiavvagfaa flgkyleqqf nlttssanql lgmtaipcac lgiflggllv kklslsalga
      421 irmamlvnlv stacyvsflf lgcdtgpvag vtvpygnsta pgsaldpysp cnnncecqtd
      481 sftpvcgadg itylsacfag cnstnltgca clttvpaena tvvpgkcpsp gcqeafltfl
      541 cvmcicslig amaqtpsvii lirtvspelk syalgvlfll lrllgfippp lifgagidst
      601 clfwstfcge qgacvlydnv vyrylyvsia ialksfafil ytttwqclrk nykryiknhe
      661 gglststeyq dietektcpe shspsedsfv rs
//
LOCUS       NP_742126                478 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 2 [Homo sapiens].
ACCESSION   NP_742126
VERSION     NP_742126.1
DBSOURCE    REFSEQ: accession NM_172128.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 478)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 478)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 478)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 478)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 478)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 478)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 478)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 478)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 478)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 478)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AI057019.1, DA113081.1,
            AB209288.1, AK055642.1 and AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The extend of this RefSeq
            trasncript is supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.76748.1, AK055642.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..478
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..478
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 2"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=53983
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Region          283..292
                     /region_name="Autoinhibitory domain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13557.3)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:16690701; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          291..301
                     /region_name="Calmodulin-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13557.3)"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Site            306
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            307
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000305; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            318
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            330
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            331
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q6PHZ2; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     Region          346..473
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     Site            404
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (Q13557.3)"
     CDS             1..478
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_172128.3:671..2107"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS43263.1"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkes tessnttied edvkarkqei ikvteqliea
      361 inngdfeayt kicdpgltaf epealgnlve gmdfhrfyfe nalsksnkpi htiilnphvh
      421 lvgddaacia yirltqymdg sgmpktmqse etrvwhrrdg kwqnvhfhrs gsptvpin
//
LOCUS       NP_036455                164 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor MafF isoform a [Homo sapiens].
ACCESSION   NP_036455
VERSION     NP_036455.1
DBSOURCE    REFSEQ: accession NM_012323.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 164)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 164)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 164)
  AUTHORS   Moon,E.J., Mello,S.S., Li,C.G., Chi,J.T., Thakkar,K.,
            Kirkland,J.G., Lagory,E.L., Lee,I.J., Diep,A.N., Miao,Y., Rafat,M.,
            Vilalta,M., Castellini,L., Krieg,A.J., Graves,E.E., Attardi,L.D.
            and Giaccia,A.J.
  TITLE     The HIF target MAFF promotes tumor invasion and metastasis through
            IL11 and STAT3 signaling
  JOURNAL   Nat Commun 12 (1), 4308 (2021)
   PUBMED   34262028
  REMARK    GeneRIF: The HIF target MAFF promotes tumor invasion and metastasis
            through IL11 and STAT3 signaling.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 164)
  AUTHORS   Ibrahim,M.K., Abdelhafez,T.H., Takeuchi,J.S., Wakae,K.,
            Sugiyama,M., Tsuge,M., Ito,M., Watashi,K., El Kassas,M., Kato,T.,
            Murayama,A., Suzuki,T., Chayama,K., Shimotohno,K., Muramatsu,M.,
            Aly,H.H. and Wakita,T.
  TITLE     MafF Is an Antiviral Host Factor That Suppresses Transcription from
            Hepatitis B Virus Core Promoter
  JOURNAL   J Virol 95 (15), e0076721 (2021)
   PUBMED   33980595
  REMARK    GeneRIF: MafF Is an Antiviral Host Factor That Suppresses
            Transcription from Hepatitis B Virus Core Promoter.
REFERENCE   5  (residues 1 to 164)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 164)
  AUTHORS   Kataoka,K., Yoshitomo-Nakagawa,K., Shioda,S. and Nishizawa,M.
  TITLE     A set of Hox proteins interact with the Maf oncoprotein to inhibit
            its DNA binding, transactivation, and transforming activities
  JOURNAL   J Biol Chem 276 (1), 819-826 (2001)
   PUBMED   11036080
REFERENCE   7  (residues 1 to 164)
  AUTHORS   Kimura,T., Ivell,R., Rust,W., Mizumoto,Y., Ogita,K., Kusui,C.,
            Matsumura,Y., Azuma,C. and Murata,Y.
  TITLE     Molecular cloning of a human MafF homologue, which specifically
            binds to the oxytocin receptor gene in term myometrium
  JOURNAL   Biochem Biophys Res Commun 264 (1), 86-92 (1999)
   PUBMED   10527846
REFERENCE   8  (residues 1 to 164)
  AUTHORS   Johnsen,O., Skammelsrud,N., Luna,L., Nishizawa,M., Prydz,H. and
            Kolsto,A.B.
  TITLE     Small Maf proteins interact with the human transcription factor
            TCF11/Nrf1/LCR-F1
  JOURNAL   Nucleic Acids Res 24 (21), 4289-4297 (1996)
   PUBMED   8932385
REFERENCE   9  (residues 1 to 164)
  AUTHORS   Armstrong,J.A. and Emerson,B.M.
  TITLE     NF-E2 disrupts chromatin structure at human beta-globin locus
            control region hypersensitive site 2 in vitro
  JOURNAL   Mol Cell Biol 16 (10), 5634-5644 (1996)
   PUBMED   8816476
REFERENCE   10 (residues 1 to 164)
  AUTHORS   Igarashi,K., Kataoka,K., Itoh,K., Hayashi,N., Nishizawa,M. and
            Yamamoto,M.
  TITLE     Regulation of transcription by dimerization of erythroid factor
            NF-E2 p45 with small Maf proteins
  JOURNAL   Nature 367 (6463), 568-572 (1994)
   PUBMED   8107826
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA209378.1, DA654696.1,
            AK002001.1, DB319587.1, AJ010857.1 and AI610651.1.
            
            Summary: The protein encoded by this gene is a basic leucine zipper
            (bZIP) transcription factor that lacks a transactivation domain. It
            is known to bind the US-2 DNA element in the promoter of the
            oxytocin receptor (OTR) gene and most likely heterodimerizes with
            other leucine zipper-containing proteins to enhance expression of
            the OTR gene during term pregnancy. The encoded protein can also
            form homodimers, and since it lacks a transactivation domain, the
            homodimer may act as a repressor of transcription. This gene may
            also be involved in the cellular stress response. Multiple
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Jun 2009].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 3. Variants 1, 3, and 4 encode the same isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC067751.1, AJ010857.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000338483.7/ ENSP00000345393.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..164
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..164
                     /product="transcription factor MafF isoform a"
                     /note="v-maf avian musculoaponeurotic fibrosarcoma
                     oncogene family protein F; transcription factor MAFF;
                     v-maf avian musculoaponeurotic fibrosarcoma oncogene
                     homolog F"
                     /calculated_mol_wt=17629
     Region          47..115
                     /region_name="bZIP_Maf_small"
                     /note="Basic leucine zipper (bZIP) domain of small
                     musculoaponeurotic fibrosarcoma (Maf) proteins: a
                     DNA-binding and dimerization domain; cd14717"
                     /db_xref="CDD:269865"
     Region          47..115
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269865"
     Region          51..76
                     /region_name="Basic motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     Site            order(56..58,60..62,64..65,68..69,71..72)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269865"
     Site            order(72,75..76,79..80,82..83,86..87,89..90,93,96..97,100,
                     103..104,107..108)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269865"
     Region          78..>162
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     Region          79..93
                     /region_name="Leucine-zipper.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00978"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     Region          141..164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9ULX9.2)"
     CDS             1..164
                     /gene="MAFF"
                     /gene_synonym="hMafF; U-MAF"
                     /coded_by="NM_012323.4:251..745"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13968.1"
                     /db_xref="GeneID:23764"
                     /db_xref="HGNC:HGNC:6780"
                     /db_xref="MIM:604877"
ORIGIN      
        1 msvdplsska lkikrelsen tphlsdealm glsvrelnrh lrglsaeevt rlkqrrrtlk
       61 nrgyaascrv krvcqkeelq kqkselerev dklarenaam rleldalrgk cealqgfars
      121 vaaargpatl vapasvitiv kstpgsgsgp ahgpdpahgp ascs
//
LOCUS       NP_002798                953 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 1 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002798
VERSION     NP_002798.2
DBSOURCE    REFSEQ: accession NM_002807.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Tang,D., Zhao,L., Huang,S., Li,W., He,Q. and Wang,A.
  TITLE     Mitochondrial outer membrane protein MTUS1/ATIP1 exerts antitumor
            effects through ROS-induced mitochondrial pyroptosis in head and
            neck squamous cell carcinoma
  JOURNAL   Int J Biol Sci 20 (7), 2576-2591 (2024)
   PUBMED   38725862
  REMARK    GeneRIF: Mitochondrial outer membrane protein MTUS1/ATIP1 exerts
            antitumor effects through ROS-induced mitochondrial pyroptosis in
            head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Kim,M.Y., Park,E.R., Cho,E.H., Park,S.H., Han,C.J., Kim,S.B.,
            Gu,M.B., Shin,H.J. and Lee,K.H.
  TITLE     Depletion of proteasome subunit PSMD1 induces cancer cell death via
            protein ubiquitination and DNA damage, irrespective of p53 status
  JOURNAL   Sci Rep 14 (1), 7997 (2024)
   PUBMED   38580756
  REMARK    GeneRIF: Depletion of proteasome subunit PSMD1 induces cancer cell
            death via protein ubiquitination and DNA damage, irrespective of
            p53 status.
            Erratum:[Sci Rep. 2024 May 3;14(1):10202. doi:
            10.1038/s41598-024-60634-1. PMID: 38702504]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Park,H.C., Kim,H., Kim,J.Y., Lee,H.Y., Lee,J., Cha,W., Ahn,S.H. and
            Jeong,W.J.
  TITLE     PSMD1 as a prognostic marker and potential target in oropharyngeal
            cancer
  JOURNAL   BMC Cancer 23 (1), 1242 (2023)
   PUBMED   38104103
  REMARK    GeneRIF: PSMD1 as a prognostic marker and potential target in
            oropharyngeal cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Simon,J.H., Gaddis,N.C., Fouchier,R.A. and Malim,M.H.
  TITLE     Evidence for a newly discovered cellular anti-HIV-1 phenotype
  JOURNAL   Nat Med 4 (12), 1397-1400 (1998)
   PUBMED   9846577
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Yokota,K., Kagawa,S., Shimizu,Y., Akioka,H., Tsurumi,C., Noda,C.,
            Fujimuro,M., Yokosawa,H., Fujiwara,T., Takahashi,E., Ohba,M.,
            Yamasaki,M., DeMartino,G.N., Slaughter,C.A., Toh-e,A. and Tanaka,K.
  TITLE     CDNA cloning of p112, the largest regulatory subunit of the human
            26s proteasome, and functional analysis of its yeast homologue,
            sen3p
  JOURNAL   Mol Biol Cell 7 (6), 853-870 (1996)
   PUBMED   8816993
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA385817.1, BC094720.1,
            AC009407.8 and AA169719.1.
            
            On Nov 27, 2002 this sequence version replaced NP_002798.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes the
            largest non-ATPase subunit of the 19S regulator lid, which is
            responsible for substrate recognition and binding. There is
            evidence that this proteasome and its subunits interact with viral
            proteins, including those of coronaviruses. Alternatively spliced
            transcript variants have been found for this gene.[provided by
            RefSeq, Aug 2020].
            
            Transcript Variant: This variant (1) is the longest transcript and
            encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.86949.1,
                                           SRR1660803.13938.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000308696.11/ ENSP00000309474.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.1"
     Protein         1..953
                     /product="26S proteasome non-ATPase regulatory subunit 1
                     isoform 1"
                     /note="26S proteasome non-ATPase regulatory subunit 1; 26S
                     proteasome subunit p112; 26S proteasome regulatory subunit
                     S1; 26S proteasome regulatory subunit RPN2; proteasome
                     (prosome, macropain) 26S subunit, non-ATPase, 1"
                     /calculated_mol_wt=105706
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Region          2..934
                     /region_name="RPN2"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5116"
                     /db_xref="CDD:227446"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17323924,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Region          279..318
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17323924; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Site            310
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Site            311
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:17323924,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Site            315
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17323924,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          403..436
                     /region_name="PC 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          441..474
                     /region_name="PC 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          476..510
                     /region_name="PC 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          511..545
                     /region_name="PC 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          547..580
                     /region_name="PC 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          565..590
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          581..616
                     /region_name="PC 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          601..624
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          617..649
                     /region_name="PC 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          651..685
                     /region_name="PC 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          667..697
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     Region          686..726
                     /region_name="PC 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Site            720
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q3TXS7; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Region          729..761
                     /region_name="PC 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Site            830
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99460.2)"
     Region          839..881
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     Region          930..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99460.2)"
     CDS             1..953
                     /gene="PSMD1"
                     /gene_synonym="P112; Rpn2; S1"
                     /coded_by="NM_002807.4:160..3021"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2482.1"
                     /db_xref="GeneID:5707"
                     /db_xref="HGNC:HGNC:9554"
                     /db_xref="MIM:617842"
ORIGIN      
        1 mitsaagiis lldedepqlk efalhklnav vndfwaeise svdkievlye degfrsrqfa
       61 alvaskvfyh lgafeeslny algagdlfnv ndnseyveti iakcidhytk qcvenadlpe
      121 gekkpidqrl egivnkmfqr clddhkykqa igialetrrl dvfektiles ndvpgmlays
      181 lklcmslmqn kqfrnkvlrv lvkiymnlek pdfinvcqcl iflddpqavs dileklvked
      241 nllmayqicf dlyesasqqf lssviqnlrt vgtpiasvpg stntgtvpgs ekdsdsmete
      301 ektssafvgk tpeaspepkd qtlkmikils gemaielhlq flirnnntdl milkntkdav
      361 rnsvchtatv iansfmhcgt tsdqflrdnl ewlaratnwa kftataslgv ihkghekeal
      421 qlmatylpkd tspgsayqeg gglyalglih anhggdiidy llnqlknasn divrhggslg
      481 lglaamgtar qdvydllktn lyqddavtge aaglalglvm lgsknaqaie dmvgyaqetq
      541 hekilrglav gialvmygrm eeadaliesl crdkdpilrr sgmytvamay cgsgnnkair
      601 rllhvavsdv nddvrraave slgfilfrtp eqcpsvvsll sesynphvry gaamalgicc
      661 agtgnkeain llepmtndpv nyvrqgalia salimiqqte itcpkvnqfr qlyskvindk
      721 hddvmakfga ilaqgildag ghnvtislqs rtghthmpsv vgvlvftqfw fwfplshfls
      781 laytptcvig lnkdlkmpkv qyksnckpst faypaplevp kekekekvst avlsitakak
      841 kkekekekke eekmevdeae kkeekekkke pepnfqlldn parvmpaqlk vltmpetcry
      901 qpfkplsigg iiilkdtsed ieelvepvaa hgpkieeeeq epeppepfey idd
//
LOCUS       NP_008933                407 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasomal ubiquitin receptor ADRM1 isoform 1 [Homo sapiens].
ACCESSION   NP_008933
VERSION     NP_008933.2
DBSOURCE    REFSEQ: accession NM_007002.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 407)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 407)
  AUTHORS   Shao,Z., Wang,Y., He,Y., Zhang,C., Zhao,Y., Zhang,M., Li,Q. and
            Wang,J.
  TITLE     The high expression of ADRM1 in hepatocellular carcinoma is closely
            related to tumor immune infiltration and is regulated by
            miR-891a-5p
  JOURNAL   Sci Rep 14 (1), 14002 (2024)
   PUBMED   38890391
  REMARK    GeneRIF: The high expression of ADRM1 in hepatocellular carcinoma
            is closely related to tumor immune infiltration and is regulated by
            miR-891a-5p.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 407)
  AUTHORS   Osei-Amponsa,V., Chandravanshi,M., Lu,X., Magidson,V., Das,S.,
            Andresson,T., Dyba,M., Sabbasani,V.R., Swenson,R.E., Fromont,C.,
            Shrestha,B., Zhao,Y., Clapp,M.E., Chari,R. and Walters,K.J.
  TITLE     hRpn13 shapes the proteome and transcriptome through epigenetic
            factors HDAC8, PADI4, and transcription factor NF-kappaB p50
  JOURNAL   Mol Cell 84 (3), 522-537 (2024)
   PUBMED   38151017
  REMARK    GeneRIF: hRpn13 shapes the proteome and transcriptome through
            epigenetic factors HDAC8, PADI4, and transcription factor NF-kappaB
            p50.
REFERENCE   4  (residues 1 to 407)
  AUTHORS   Zhu,D. and Zhong,Q.
  TITLE     Potential of adhesion-regulating molecule 1 (ADRM1) as a biomarker
            for patients with renal clear-cell carcinoma or papillary-cell
            carcinoma
  JOURNAL   Asian J Surg 46 (10), 4666-4668 (2023)
   PUBMED   37268471
  REMARK    GeneRIF: Potential of adhesion-regulating molecule 1 (ADRM1) as a
            biomarker for patients with renal clear-cell carcinoma or
            papillary-cell carcinoma.
REFERENCE   5  (residues 1 to 407)
  AUTHORS   Xiao,J., Xie,Y., Duan,Q., Liu,T., Ye,R., Duan,X., Le,Z., Deng,N.
            and Liu,F.
  TITLE     LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models
  JOURNAL   Int Heart J 64 (4), 750-758 (2023)
   PUBMED   37518356
  REMARK    GeneRIF: LIM Homeobox 2 Increases Adhesion-Regulating Molecule 1
            Transcription to Facilitate the Pathological Progression of
            Oxidized Low-Density Lipoprotein-Stimulated Atherosclerotic Cell
            Models.
REFERENCE   6  (residues 1 to 407)
  AUTHORS   Jorgensen,J.P., Lauridsen,A.M., Kristensen,P., Dissing,K.,
            Johnsen,A.H., Hendil,K.B. and Hartmann-Petersen,R.
  TITLE     Adrm1, a putative cell adhesion regulating protein, is a novel
            proteasome-associated factor
  JOURNAL   J Mol Biol 360 (5), 1043-1052 (2006)
   PUBMED   16815440
  REMARK    GeneRIF: Adrm1 has a specialised role in proteasome function.
            Identified Adrm1 as a novel component of the regulatory ATPase
            complex of the 26 S proteasome
REFERENCE   7  (residues 1 to 407)
  AUTHORS   Lamerant,N. and Kieda,C.
  TITLE     Adhesion properties of adhesion-regulating molecule 1 protein on
            endothelial cells
  JOURNAL   FEBS J 272 (8), 1833-1844 (2005)
   PUBMED   15819879
  REMARK    GeneRIF: ARM-1 is a cytosolic protein associated with the plasma
            membrane. However, no cell surface expression of the protein was
            observed. These results suggest an indirect role of ARM-1 in
            adhesion rather than a direct role as an adhesion molecule
            itself.[ARM-1]
REFERENCE   8  (residues 1 to 407)
  AUTHORS   Cascio,P., Call,M., Petre,B.M., Walz,T. and Goldberg,A.L.
  TITLE     Properties of the hybrid form of the 26S proteasome containing both
            19S and PA28 complexes
  JOURNAL   EMBO J 21 (11), 2636-2645 (2002)
   PUBMED   12032076
REFERENCE   9  (residues 1 to 407)
  AUTHORS   Simins,A.B., Weighardt,H., Weidner,K.M., Weidle,U.H. and
            Holzmann,B.
  TITLE     Functional cloning of ARM-1, an adhesion-regulating molecule
            upregulated in metastatic tumor cells
  JOURNAL   Clin Exp Metastasis 17 (8), 641-648 (1999)
   PUBMED   10919708
REFERENCE   10 (residues 1 to 407)
  AUTHORS   Shimada,S., Ogawa,M., Takahashi,M., Schlom,J. and Greiner,J.W.
  TITLE     Molecular cloning and characterization of the complementary DNA of
            an M(r) 110,000 antigen expressed by human gastric carcinoma cells
            and upregulated by gamma-interferon
  JOURNAL   Cancer Res 54 (14), 3831-3836 (1994)
   PUBMED   8033103
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354836.13.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 13, 2003 this sequence version replaced NP_008933.1.
            
            Summary: This gene encodes a member of the adhesion regulating
            molecule 1 protein family. The encoded protein is a component of
            the proteasome where it acts as a ubiquitin receptor and recruits
            the deubiquitinating enzyme, ubiquitin carboxyl-terminal hydrolase
            L5. Increased levels of the encoded protein are associated with
            increased cell adhesion, which is likely an indirect effect of this
            intracellular protein. Dysregulation of this gene has been
            implicated in carcinogenesis. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (1). Variants 1 and 2
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC093021.1, SRR3476690.381698.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253003.7/ ENSP00000253003.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..407
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.33"
     Protein         1..407
                     /product="proteasomal ubiquitin receptor ADRM1 isoform 1"
                     /note="110 kDa cell membrane glycoprotein; M(r) 110,000
                     surface antigen; proteasomal ubiquitin receptor ADRM1;
                     rpn13 homolog; proteasome regulatory particle non-ATPase
                     13; proteasome ubiquitin receptor; adhesion regulating
                     molecule 1"
                     /calculated_mol_wt=42022
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylthreonine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          24..128
                     /region_name="PH_Rpn13"
                     /note="Pleckstrin homology-like domain of Regulatory
                     Particle Non-ATPase 13; cd13314"
                     /db_xref="CDD:270124"
     Site            order(53..54,56,73..80,98..100,103)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:270124"
     Site            127
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Region          194..259
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            211
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          253..407
                     /region_name="Interaction with UCHL5.
                     /evidence=ECO:0000269|PubMed:20471946"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Region          274..381
                     /region_name="RPN13_C"
                     /note="UCH-binding domain; pfam16550"
                     /db_xref="CDD:465170"
     Region          379..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16186.2)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JMB5; propagated from
                     UniProtKB/Swiss-Prot (Q16186.2)"
     CDS             1..407
                     /gene="ADRM1"
                     /gene_synonym="ARM-1; ARM1; GP110; PSMD16"
                     /coded_by="NM_007002.4:55..1278"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13496.1"
                     /db_xref="GeneID:11047"
                     /db_xref="HGNC:HGNC:15759"
                     /db_xref="MIM:610650"
ORIGIN      
        1 mttsgalfps lvpgsrgasn kylvefragk mslkgttvtp dkrkglvyiq qtddslihfc
       61 wkdrtsgnve ddliifpddc efkrvpqcps grvyvlkfka gskrlffwmq epktdqdeeh
      121 crkvneylnn ppmpgalgas gssghelsal ggegglqsll gnmshsqlmq ligpaglggl
      181 gglgaltgpg lasllgssgp pgsssssssr sqsaavtpss ttsstratpa psapaaasat
      241 spspapssgn gastaasptq piqlsdlqsi latmnvpagp aggqqvdlas vltpeimapi
      301 lanadvqerl lpylpsgesl pqtadeiqnt ltspqfqqal gmfsaalasg qlgplmcqfg
      361 lpaeaveaan kgdveafaka mqnnakpeqk egdtkdkkde eedmsld
//
LOCUS       NP_001138844             581 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 3 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001138844
VERSION     NP_001138844.1
DBSOURCE    REFSEQ: accession NM_001145372.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 581)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 581)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 581)
  AUTHORS   Masuda,S., Onishi,H., Iwamoto,N., Imaizumi,A., Koga,S., Nagao,S.,
            Sakanashi,K., Itoyama,S., Fujimura,A., Komune,N., Kogo,R.,
            Umebayashi,M., Morisaki,T. and Nakagawa,T.
  TITLE     Inhibition of PTPN3 Expressed in Activated Lymphocytes Enhances the
            Antitumor Effects of Anti-PD-1 Therapy in Head and Neck Cancer,
            Especially in Hypoxic Environments
  JOURNAL   J Immunother 47 (3), 89-97 (2024)
   PUBMED   38297883
  REMARK    GeneRIF: Inhibition of PTPN3 Expressed in Activated Lymphocytes
            Enhances the Antitumor Effects of Anti-PD-1 Therapy in Head and
            Neck Cancer, Especially in Hypoxic Environments.
REFERENCE   4  (residues 1 to 581)
  AUTHORS   Zhou,Z., Lin,Z., Wang,M., Wang,L., Ji,Y., Yang,J., Yang,Y., Zhu,G.
            and Liu,T.
  TITLE     Identification and verification of PTPN3 as a novel biomarker in
            predicting cancer prognosis, immunity, and immunotherapeutic
            efficacy
  JOURNAL   Eur J Med Res 29 (1), 12 (2024)
   PUBMED   38173048
  REMARK    GeneRIF: Identification and verification of PTPN3 as a novel
            biomarker in predicting cancer prognosis, immunity, and
            immunotherapeutic efficacy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 581)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   6  (residues 1 to 581)
  AUTHORS   Zhang,S.H., Kobayashi,R., Graves,P.R., Piwnica-Worms,H. and
            Tonks,N.K.
  TITLE     Serine phosphorylation-dependent association of the band
            4.1-related protein-tyrosine phosphatase PTPH1 with 14-3-3beta
            protein
  JOURNAL   J Biol Chem 272 (43), 27281-27287 (1997)
   PUBMED   9341175
REFERENCE   7  (residues 1 to 581)
  AUTHORS   Ikuta,S., Itoh,F., Hinoda,Y., Toyota,M., Makiguchi,Y., Imai,K. and
            Yachi,A.
  TITLE     Expression of cytoskeletal-associated protein tyrosine phosphatase
            PTPH1 mRNA in human hepatocellular carcinoma
  JOURNAL   J Gastroenterol 29 (6), 727-732 (1994)
   PUBMED   7874267
REFERENCE   8  (residues 1 to 581)
  AUTHORS   Itoh,F., Ikuta,S., Hinoda,Y., Arimura,Y., Ohe,M., Adachi,M.,
            Ariyama,T., Inazawa,J., Imai,K. and Yachi,A.
  TITLE     Expression and chromosomal assignment of PTPH1 gene encoding a
            cytosolic protein tyrosine phosphatase homologous to
            cytoskeletal-associated proteins
  JOURNAL   Int J Cancer 55 (6), 947-951 (1993)
   PUBMED   8253532
REFERENCE   9  (residues 1 to 581)
  AUTHORS   Arimura,Y., Hinoda,Y., Itoh,F., Takekawa,M., Tsujisaki,M.,
            Adachi,M., Imai,K. and Yachi,A.
  TITLE     cDNA cloning of new protein tyrosine phosphatases in the human
            colon
  JOURNAL   Tumour Biol 13 (3), 180-186 (1992)
   PUBMED   1626183
REFERENCE   10 (residues 1 to 581)
  AUTHORS   Yang,Q. and Tonks,N.K.
  TITLE     Isolation of a cDNA clone encoding a human protein-tyrosine
            phosphatase with homology to the cytoskeletal-associated proteins
            band 4.1, ezrin, and talin
  JOURNAL   Proc Natl Acad Sci U S A 88 (14), 5949-5953 (1991)
   PUBMED   1648725
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC342461.1, AK316118.1,
            BC033716.1, DB173093.1, AK096975.1 and AL359963.29.
            
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This protein contains a C-terminal PTP
            domain and an N-terminal domain homologous to the band 4.1
            superfamily of cytoskeletal-associated proteins. P97, a cell cycle
            regulator involved in a variety of membrane related functions, has
            been shown to be a substrate of this PTP. This PTP was also found
            to interact with, and be regulated by adaptor protein 14-3-3 beta.
            Several alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Feb 2009].
            
            Transcript Variant: This variant (6) differs in the 5' UTR, and is
            missing an in-frame coding exon compared to transcript variant 1,
            resulting in an isoform (6) with a shorter N-terminus and lacking
            an internal protein segment compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.226653.1,
                                           SRR1803615.248962.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.3"
     Protein         1..581
                     /product="tyrosine-protein phosphatase non-receptor type 3
                     isoform 6"
                     /EC_number="3.1.3.48"
                     /note="cytoskeletal-associated protein tyrosine
                     phosphatase; protein-tyrosine phosphatase H1"
                     /calculated_mol_wt=65758
     Region          <1..22
                     /region_name="PH-like"
                     /note="Pleckstrin homology-like domain; cl17171"
                     /db_xref="CDD:473070"
     Region          174..263
                     /region_name="PDZ_PTPN3-4-like"
                     /note="PDZ domain of tyrosine-protein phosphatase
                     non-receptor type 3 (PTPN3), tyrosine-protein phosphatase
                     non-receptor type 4 (PTNP4), and related domains; cd06706"
                     /db_xref="CDD:467190"
     Site            order(188..194,206,209,240,244,247..248)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467190"
     Region          299..572
                     /region_name="PTPc-N3"
                     /note="catalytic domain of tyrosine-protein phosphatase
                     non-receptor type 3; cd14600"
                     /db_xref="CDD:350448"
     CDS             1..581
                     /gene="PTPN3"
                     /gene_synonym="PTP-H1; PTPH1"
                     /coded_by="NM_001145372.2:386..2131"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:5774"
                     /db_xref="HGNC:HGNC:9655"
                     /db_xref="MIM:176877"
ORIGIN      
        1 mlnyrscknl wkscvehhtf fqakkllpqe knvlsqywtm gsrntkkrsp rlrheirkpr
       61 hssadnlane mtyitetedv fytykgslap qdsdsevsqn rsphqeslse nnpaqsyltq
      121 kssssvspss napgscspdg vdqqllddfh rvtkggsted asqyycdknd ngdsylvlir
      181 itpdedgkfg fnlkggvdqk mplvvsrinp espadtcipk lnegdqivli ngrdisehth
      241 dqvvmfikas reshsrelal virrravrsf adfksedeln qlfpeaifpm cpeggdtleg
      301 smaqlkkgle sgtvliqfeq lyrkkpglai tfaklpqnld knrykdvlpy dttrvllqgn
      361 edyinasyvn meipaanlvn kyiatqgplp htcaqfwqvv wdqklslivm lttltergrt
      421 kchqywpdpp dvmnhggfhi qcqsedctia yvsremlvtn tqtgeehtvt hlqyvawpdh
      481 gvpddssdfl efvnyvrslr vdsepvlvhc sagigrtgvl vtmetamclt ernlpiypld
      541 ivrkmrdqra mmvqtssqyk fvceailrvy eeglvqmldp s
//
LOCUS       NP_659469                735 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box and leucine-rich repeat protein 13 isoform 1 [Homo sapiens].
ACCESSION   NP_659469
VERSION     NP_659469.3
DBSOURCE    REFSEQ: accession NM_145032.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 735)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 735)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   3  (residues 1 to 735)
  AUTHORS   Fung,E., Richter,C., Yang,H.B., Schaffer,I., Fischer,R.,
            Kessler,B.M., Bassermann,F. and D'Angiolella,V.
  TITLE     FBXL13 directs the proteolysis of CEP192 to regulate centrosome
            homeostasis and cell migration
  JOURNAL   EMBO Rep 19 (3) (2018)
   PUBMED   29348145
REFERENCE   4  (residues 1 to 735)
  AUTHORS   He,J., Kelly,T.N., Zhao,Q., Li,H., Huang,J., Wang,L., Jaquish,C.E.,
            Sung,Y.J., Shimmin,L.C., Lu,F., Mu,J., Hu,D., Ji,X., Shen,C.,
            Guo,D., Ma,J., Wang,R., Shen,J., Li,S., Chen,J., Mei,H., Chen,C.S.,
            Chen,S., Chen,J., Li,J., Cao,J., Lu,X., Wu,X., Rice,T.K., Gu,C.C.,
            Schwander,K., Hamm,L.L., Liu,D., Rao,D.C., Hixson,J.E. and Gu,D.
  TITLE     Genome-wide association study identifies 8 novel loci associated
            with blood pressure responses to interventions in Han Chinese
  JOURNAL   Circ Cardiovasc Genet 6 (6), 598-607 (2013)
   PUBMED   24165912
REFERENCE   5  (residues 1 to 735)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 735)
  AUTHORS   Curtiss,N.P., Bonifas,J.M., Lauchle,J.O., Balkman,J.D., Kratz,C.P.,
            Emerling,B.M., Green,E.D., Le Beau,M.M. and Shannon,K.M.
  TITLE     Isolation and analysis of candidate myeloid tumor suppressor genes
            from a commonly deleted segment of 7q22
  JOURNAL   Genomics 85 (5), 600-607 (2005)
   PUBMED   15820312
REFERENCE   7  (residues 1 to 735)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK097537.1, AY359239.1, BP378950.1 and AK095387.1.
            
            On Nov 29, 2007 this sequence version replaced NP_659469.2.
            
            Summary: Members of the F-box protein family, such as FBXL13, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK097537.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..735
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..735
                     /product="F-box and leucine-rich repeat protein 13 isoform
                     1"
                     /note="F-box/LRR-repeat protein 13; dynein regulatory
                     complex subunit 6; cilia and flagella associated protein
                     169"
                     /calculated_mol_wt=83793
     Region          <22..>134
                     /region_name="Sfi1"
                     /note="Sfi1 spindle body protein; pfam08457"
                     /db_xref="CDD:430007"
     Region          155..196
                     /region_name="F-box_FBXL13"
                     /note="F-box domain found in F-box/LRR-repeat protein 13
                     (FBXL13) and similar proteins; cd22124"
                     /db_xref="CDD:438896"
     Site            order(158,162,165..166,169..170,174,176..177,181..183,185)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438896"
     Region          195..222
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          222..407
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          223..246
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          230..254
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          247..272
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          255..280
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          273..297
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          281..305
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          298..316
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          306..333
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          326..351
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          334..359
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          352..401
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          360..385
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          378..400
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          386..406
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          402..425
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          410..435
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          428..452
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          436..460
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          439..647
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          453..480
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          461..488
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          481..506
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          489..514
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          507..555
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          515..538
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          539..563
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          556..581
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          564..589
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          582..607
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          590..615
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          608..633
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          616..641
                     /region_name="LRR 16"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          634..659
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          642..667
                     /region_name="LRR 17"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     Region          682..703
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NEE6.3)"
     CDS             1..735
                     /gene="FBXL13"
                     /gene_synonym="CFAP169; DRC6; Fbl13"
                     /coded_by="NM_145032.3:428..2635"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5726.1"
                     /db_xref="GeneID:222235"
                     /db_xref="HGNC:HGNC:21658"
                     /db_xref="MIM:609080"
ORIGIN      
        1 mtpelmikac sfytghlvkt hfctwrdiar tnenvvlaek mnravtcynf rlqksvfhhw
       61 hsymedqkek lknillriqq iiychkltii ltkwrntarh kskkkedeli lkhelqlkkw
      121 knrlilkraa aeesnfpers ssevflvdet lkcdisllpe railqiffyl slkdviicgq
      181 vnhawmlmtq lnslwnaidf ssvknvipdk yivstlqrwr lnvlrlnfrg cllrpktfrs
      241 vshcrnlqel nvsdcptftd esmrhisegc pgvlclnlsn ttitnrtmrl lprhfhnlqn
      301 lslaycrrft dkglqylnlg ngchkliyld lsgctqisvq gfryiansct gimhltindm
      361 ptltdncvka lvekcsrits lvftgaphis dctfralsac klrkirfegn krvtdasfkf
      421 idknypnlsh iymadckgit dsslrslspl kqltvlnlan cvrigdmglk qfldgpasmr
      481 irelnlsncv rlsdasvmkl sercpnlnyl slrncehlta qgigyivnif slvsidlsgt
      541 disneglnvl srhkklkels vsecyritdd giqafckssl ilehldvsyc sqlsdmiika
      601 laiycinlts lsiagcpkit dsamemlsak chylhildis gcvlltdqil edlqigckql
      661 rilkmqyctn iskkaaqrms skvqqqeynt ndpprwfgyd regnpvteld nitsskgale
      721 ltvkkstyss edqaa
//
LOCUS       NP_001243506             216 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL16 isoform b [Homo sapiens].
ACCESSION   NP_001243506
VERSION     NP_001243506.2
DBSOURCE    REFSEQ: accession NM_001256577.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Wang,K., Chen,S., Wu,Y., Wang,Y., Lu,Y., Sun,Y. and Chen,Y.
  TITLE     The ufmylation modification of ribosomal protein L10 in the
            development of pancreatic adenocarcinoma
  JOURNAL   Cell Death Dis 14 (6), 350 (2023)
   PUBMED   37280198
  REMARK    GeneRIF: The ufmylation modification of ribosomal protein L10 in
            the development of pancreatic adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Farmer,A.A., Johnsen,J.I., Loftus,T.M., Smith,K.P. and
            Stanbridge,E.J.
  TITLE     Isolation and characterization of the QM promoter
  JOURNAL   Nucleic Acids Res 24 (11), 2158-2165 (1996)
   PUBMED   8668549
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Farmer,A.A., Loftus,T.M., Mills,A.A., Sato,K.Y., Neill,J.D.,
            Tron,T., Yang,M., Trumpower,B.L. and Stanbridge,E.J.
  TITLE     Extreme evolutionary conservation of QM, a novel c-Jun associated
            transcription factor
  JOURNAL   Hum Mol Genet 3 (5), 723-728 (1994)
   PUBMED   8081358
REFERENCE   6  (residues 1 to 216)
  AUTHORS   Kaneko,K., Kobayashi,H., Onodera,O., Miyatake,T. and Tsuji,S.
  TITLE     Genomic organization of a cDNA (QM) demonstrating an altered mRNA
            level in nontumorigenic Wilms' microcell hybrid cells and its
            localization to Xq28
  JOURNAL   Hum Mol Genet 1 (7), 529-533 (1992)
   PUBMED   1339145
REFERENCE   7  (residues 1 to 216)
  AUTHORS   van den Ouweland,A.M., Verdijk,M., Mannens,M.M. and van Oost,B.A.
  TITLE     The QM gene is X-linked and therefore not involved in suppression
            of tumorigenesis in Wilms' tumor
  JOURNAL   Hum Genet 90 (1-2), 144-146 (1992)
   PUBMED   1330878
REFERENCE   8  (residues 1 to 216)
  AUTHORS   van den Ouweland,A.M., Kioschis,P., Verdijk,M., Tamanini,F.,
            Toniolo,D., Poustka,A. and van Oost,B.A.
  TITLE     Identification and characterization of a new gene in the human Xq28
            region
  JOURNAL   Hum Mol Genet 1 (4), 269-273 (1992)
   PUBMED   1303197
REFERENCE   9  (residues 1 to 216)
  AUTHORS   Bignon,C., Roux-Dosseto,M., Zeigler,M.E., Wicha,M.S. and
            Martin,P.M.
  TITLE     cDNA cloning and genomic analysis of a new multigene family sharing
            common phylogenetic and expression profiles with the laminin
            receptor gene
  JOURNAL   Biochem Biophys Res Commun 184 (3), 1165-1172 (1992)
   PUBMED   1534224
REFERENCE   10 (residues 1 to 216)
  AUTHORS   Dowdy,S.F., Lai,K.M., Weissman,B.E., Matsui,Y., Hogan,B.L. and
            Stanbridge,E.J.
  TITLE     The isolation and characterization of a novel cDNA demonstrating an
            altered mRNA level in nontumorigenic Wilms' microcell hybrid cells
  JOURNAL   Nucleic Acids Res 19 (20), 5763-5769 (1991)
   PUBMED   1658743
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA589764.1, AK307511.1,
            BC003358.1 and AC245140.2.
            
            On Jan 13, 2015 this sequence version replaced NP_001243506.1.
            
            Summary: This gene encodes a ribosomal protein that is a component
            of the 60S ribosome subunit. The related protein in chicken can
            bind to c-Jun and can repress c-Jun-mediated transcriptional
            activation. Some studies have detected an association between
            variation in this gene and autism spectrum disorders, though others
            do not detect this relationship. There are multiple pseudogenes of
            this gene dispersed throughout the genome. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Jan
            2015].
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            3' coding region, which results in a frameshift, compared to
            variant 1. The encoded isoform (b) has a distinct, longer
            C-terminus than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CB112798.1, CD389911.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
     Protein         1..216
                     /product="large ribosomal subunit protein uL16 isoform b"
                     /EC_number="3.6.5.3"
                     /note="60S ribosomal protein L10; tumor suppressor QM;
                     Wilms tumor-related protein; laminin receptor homolog;
                     large ribosomal subunit protein uL16"
                     /calculated_mol_wt=24034
     Region          1..>110
                     /region_name="Ribosomal_L16_L10e"
                     /note="L16 is an essential protein in the large ribosomal
                     subunit of bacteria, mitochondria, and chloroplasts. Large
                     subunits that lack L16 are defective in peptidyl
                     transferase activity, peptidyl-tRNA hydrolysis activity,
                     association with the 30S subunit; cl00353"
                     /db_xref="CDD:469737"
     Site            56..57
                     /site_type="other"
                     /note="5S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238714"
     Site            order(68..70,73..74)
                     /site_type="other"
                     /note="putative antibiotic binding site [chemical
                     binding]"
                     /db_xref="CDD:238714"
     Site            order(77,85..86,88)
                     /site_type="other"
                     /note="L25 interface [polypeptide binding]"
                     /db_xref="CDD:238714"
     CDS             1..216
                     /gene="RPL10"
                     /gene_synonym="AUTSX5; DXS648; DXS648E; L10; MRXS35; NOV;
                     QM; uL16"
                     /coded_by="NM_001256577.2:354..1004"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="GeneID:6134"
                     /db_xref="HGNC:HGNC:10298"
                     /db_xref="MIM:312173"
ORIGIN      
        1 mgrrparcyr ycknkpypks rfcrgvpdak irifdlgrkk akvdefplcg hmvsdeyeql
       61 ssealeaari cankymvksc gkdgfhirvr lhpfhvirin kmlscagadr stsqrsgasp
      121 ssmlmnlktw wlksgssqma vgsstspvva lwtsggpcth egfqcaapll iltnkfyfls
      181 tyvfvstflt gkelplgtfg slpfhfrnrl ttqpcs
//
LOCUS       NP_001354469             300 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 33 [Homo sapiens].
ACCESSION   NP_001354469
VERSION     NP_001354469.1
DBSOURCE    REFSEQ: accession NM_001367540.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..300
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 33"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=33065
     Region          <11..81
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          141..>196
                     /region_name="NTF2_like"
                     /note="Nuclear transport factor 2 (NTF2-like) superfamily.
                     This family includes members of the NTF2 family,
                     Delta-5-3-ketosteroid isomerases, Scytalone Dehydratases,
                     and the beta subunit of Ring hydroxylating dioxygenases.
                     This family is a classic example of...; cl09109"
                     /db_xref="CDD:471850"
     CDS             1..300
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367540.1:666..1568"
                     /note="isoform 33 is encoded by transcript variant 33"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 menlwisgpa fpspewdtvt peaknlinqm ltinpakrit adqalkhpwv cqrstvasmm
       61 hrqetveclr kfnarrklkg ailttmlvsr nfsaakslln kksdggvkep qttvvhnatd
      121 gikgstescn tttededlkv rkqeiikite qlieainngd feaytkicdp gltsfepeal
      181 gnlvegmdfh kfyfenrewv raadillpap lplclclllt fssqlptfpl fdlraalllc
      241 mlvplcpdgc rqaplkalll sskchsfcsc fvavpvttik ltyflpgava yacnpntlgg
//
LOCUS       NP_001558               1258 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 isoform 2
            [Homo sapiens].
ACCESSION   NP_001558
VERSION     NP_001558.3
DBSOURCE    REFSEQ: accession NM_001567.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1258)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1258)
  AUTHORS   Ji,X., Wu,Q., Cao,X., Liu,S., Zhang,J., Chen,S., Shan,J., Zhang,Y.,
            Li,B. and Zhao,H.
  TITLE     Helicobacter pylori East Asian type CagA hijacks more SHIP2 by its
            EPIYA-D motif to potentiate the oncogenicity
  JOURNAL   Virulence 15 (1), 2375549 (2024)
   PUBMED   38982595
  REMARK    GeneRIF: Helicobacter pylori East Asian type CagA hijacks more
            SHIP2 by its EPIYA-D motif to potentiate the oncogenicity.
REFERENCE   3  (residues 1 to 1258)
  AUTHORS   Ando,K., Kucukali,F., Doeraene,E., Nagaraj,S., Antonelli,E.M.,
            Thazin Htut,M., Yilmaz,Z., Kosa,A.C., Lopez-Guitierrez,L.,
            Quintanilla-Sanchez,C., Aydin,E., Ramos,A.R., Mansour,S.,
            Turbant,S., Schurmans,S., Sleegers,K., Erneux,C., Brion,J.P. and
            Leroy,K.
  CONSRTM   Brain Bank NeuroCEB Neuropathology Network
  TITLE     Alteration of gene expression and protein solubility of the PI
            5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression
  JOURNAL   Acta Neuropathol 147 (1), 94 (2024)
   PUBMED   38833073
  REMARK    GeneRIF: Alteration of gene expression and protein solubility of
            the PI 5-phosphatase SHIP2 are correlated with Alzheimer's disease
            pathology progression.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1258)
  AUTHORS   Bradshaw,W.J., Kennedy,E.C., Moreira,T., Smith,L.A., Chalk,R.,
            Katis,V.L., Benesch,J.L.P., Brennan,P.E., Murphy,E.J. and
            Gileadi,O.
  TITLE     Regulation of inositol 5-phosphatase activity by the C2 domain of
            SHIP1 and SHIP2
  JOURNAL   Structure 32 (4), 453-466 (2024)
   PUBMED   38309262
  REMARK    GeneRIF: Regulation of inositol 5-phosphatase activity by the C2
            domain of SHIP1 and SHIP2.
REFERENCE   5  (residues 1 to 1258)
  AUTHORS   Habib,T., Hejna,J.A., Moses,R.E. and Decker,S.J.
  TITLE     Growth factors and insulin stimulate tyrosine phosphorylation of
            the 51C/SHIP2 protein
  JOURNAL   J Biol Chem 273 (29), 18605-18609 (1998)
   PUBMED   9660833
REFERENCE   6  (residues 1 to 1258)
  AUTHORS   Le Drean,E., Vely,F., Olcese,L., Cambiaggi,A., Guia,S., Krystal,G.,
            Gervois,N., Moretta,A., Jotereau,F. and Vivier,E.
  TITLE     Inhibition of antigen-induced T cell response and antibody-induced
            NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and
            SHP-2 protein-tyrosine phosphatases
  JOURNAL   Eur J Immunol 28 (1), 264-276 (1998)
   PUBMED   9485206
  REMARK    Erratum:[Eur J Immunol 1998 Mar;28(3):1122]
REFERENCE   7  (residues 1 to 1258)
  AUTHORS   Pesesse,X., Deleu,S., De Smedt,F., Drayer,L. and Erneux,C.
  TITLE     Identification of a second SH2-domain-containing protein closely
            related to the phosphatidylinositol polyphosphate 5-phosphatase
            SHIP
  JOURNAL   Biochem Biophys Res Commun 239 (3), 697-700 (1997)
   PUBMED   9367831
REFERENCE   8  (residues 1 to 1258)
  AUTHORS   Hejna,J.A., Saito,H., Merkens,L.S., Tittle,T.V., Jakobs,P.M.,
            Whitney,M.A., Grompe,M., Friedberg,A.S. and Moses,R.E.
  TITLE     Cloning and characterization of a human cDNA (INPPL1) sharing
            homology with inositol polyphosphate phosphatases
  JOURNAL   Genomics 29 (1), 285-287 (1995)
   PUBMED   8530088
REFERENCE   9  (residues 1 to 1258)
  AUTHORS   Huang,S., Earl,D. and White,K.
  TITLE     INPPL1-Related Opsismodysplasia
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   40504975
REFERENCE   10 (residues 1 to 1258)
  AUTHORS   Slama,V. and Dudek,J.
  TITLE     [Stability of diluted solutions of peracetic acid]
  JOURNAL   Cesk Farm 17 (1), 40-41 (1968)
   PUBMED   5668240
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000593.4, BC140853.1,
            Y14385.1 and BG236320.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 29, 2009 this sequence version replaced NP_001558.2.
            
            Summary: The protein encoded by this gene is an SH2-containing
            5'-inositol phosphatase that is involved in the regulation of
            insulin function. The encoded protein also plays a role in the
            regulation of epidermal growth factor receptor turnover and actin
            remodelling. Additionally, this gene supports metastatic growth in
            breast cancer and is a valuable biomarker for breast cancer.
            [provided by RefSeq, Jan 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: Y14385.1, BC140853.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000298229.7/ ENSP00000298229.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1258
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.4"
     Protein         1..1258
                     /product="phosphatidylinositol 3,4,5-trisphosphate
                     5-phosphatase 2 isoform 2"
                     /EC_number="3.1.3.86"
                     /note="SH2 domain-containing inositol-5'-phosphatase 2;
                     51C protein; protein 51C; phosphatidylinositol
                     3,4,5-trisphosphate 5-phosphatase 2"
                     /calculated_mol_wt=138468
     Region          17..119
                     /region_name="SH2_SHIP"
                     /note="Src homology 2 (SH2) domain found in SH2-containing
                     inositol-5'-phosphatase (SHIP) and SLAM-associated protein
                     (SAP); cd10343"
                     /db_xref="CDD:198206"
     Site            order(28,47,68,70)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198206"
     Site            order(68..69,81..82,87,90,106..108)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198206"
     Region          119..180
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            132
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            165
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            241
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            352
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          424..727
                     /region_name="INPP5c_SHIP2-INPPL1"
                     /note="Catalytic inositol polyphosphate 5-phosphatase
                     (INPP5c) domain of SH2 domain containing inositol
                     5-phosphatase-2 and related proteins; cd09101"
                     /db_xref="CDD:197335"
     Site            order(432,434,473,540..541,561,564..565,607,609,611,
                     661..662,684,690,717..718)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:197335"
     Site            order(432,473,561,607,609,690,717..718)
                     /site_type="active"
                     /note="putative catalytic site [active]"
                     /db_xref="CDD:197335"
     Site            order(473,540..541,561,564..565,611,661..662,684,717)
                     /site_type="other"
                     /note="putative PI/IP binding site [chemical binding]"
                     /db_xref="CDD:197335"
     Site            order(473,717)
                     /site_type="other"
                     /note="putative Mg binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            order(561,609,718)
                     /site_type="other"
                     /note="putative phosphate binding site [ion binding]"
                     /db_xref="CDD:197335"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          897..1118
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Region          <899..1214
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          944..949
                     /region_name="SH3-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            958
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:17219406,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          983..986
                     /region_name="NPXY motif"
                     /note="propagated from UniProtKB/Swiss-Prot (O15357.2)"
     Site            986
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by SRC.
                     /evidence=ECO:0000269|PubMed:11349134,
                     ECO:0000269|PubMed:12235291; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1135
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Site            1162
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:11687594,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     Region          1194..1256
                     /region_name="SAM_Ship2"
                     /note="SAM domain of Ship2 lipid phosphatase proteins;
                     cd09491"
                     /db_xref="CDD:188890"
     Site            order(1222..1224,1226..1227,1230,1235)
                     /site_type="other"
                     /note="heterodimer interface ML [polypeptide binding]"
                     /db_xref="CDD:188890"
     Site            1257
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O15357.2)"
     CDS             1..1258
                     /gene="INPPL1"
                     /gene_synonym="OPSMD; SHIP2"
                     /coded_by="NM_001567.4:219..3995"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS8213.1"
                     /db_xref="GeneID:3636"
                     /db_xref="HGNC:HGNC:6080"
                     /db_xref="MIM:600829"
ORIGIN      
        1 masacgapgp ggalgsqaps wyhrdlsraa aeellaragr dgsflvrdse svagafalcv
       61 lyqkhvhtyr ilpdgedfla vqtsqgvpvr rfqtlgelig lyaqpnqglv calllpvege
      121 repdppddrd asdgedekpp lpprsgstsi saptgpsspl papetptapa aesapnglst
      181 vshdylkgsy gldleavrgg ashlphltrt latscrrlhs evdkvlsgle ilskvfdqqs
      241 spmvtrllqq qnlpqtgeqe leslvlklsv lkdflsgiqk kalkalqdms stappapqps
      301 trkaktipvq afevkldvtl gdltkigksq kftlsvdveg grlvllrrqr dsqedwttft
      361 hdrirqliks qrvqnklgvv fekekdrtqr kdfifvsark reafcqllql mknkhskqde
      421 pdmisvfigt wnmgsvpppk nvtswftskg lgktldevtv tiphdiyvfg tqensvgdre
      481 wldllrgglk eltdldyrpi amqslwnikv avlvkpehen rishvstssv ktgiantlgn
      541 kgavgvsfmf ngtsfgfvnc hltsgnekta rrnqnyldil rllslgdrql nafdislrft
      601 hlfwfgdlny rldmdiqeil nyisrkefep llrvdqlnle rekhkvflrf seeeisfppt
      661 yryergsrdt yawhkqkptg vrtnvpswcd rilwksypet hiicnsygct ddivtsdhsp
      721 vfgtfevgvt sqfiskkgls ktsdqayief esieaivkta srtkffiefy stcleeykks
      781 fendaqssdn inflkvqwss rqlptlkpil adieylqdqh llltvksmdg yesygecvva
      841 lksmigstaq qfltflshrg eetgnirgsm kvrvpterlg trerlyewis idkdeagaks
      901 kapsvsrgsq eprsgsrkpa fteascplsr lfeepekppp tgrppappra apreepltpr
      961 lkpegapepe gvaapppkns fnnpayyvle gvphqllppe ppsparapvp satknkvait
     1021 vpapqlghhr hprvgegsss deesggtlpp pdfpppplpd saiflppsld plpgpvvrgr
     1081 ggaeargppp pkahprpplp pgpspastfl gevasgddrs csvlqmaktl sevdyapagp
     1141 arsallpgpl elqpprglps dygrplsfpp priresiqed laeeapclqg grasglgeag
     1201 msawlraigl eryeeglvhn gwddleflsd iteedleeag vqdpahkrll ldtlqlsk
//
LOCUS       NP_060899               2624 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor TFIIIB component B'' homolog [Homo sapiens].
ACCESSION   NP_060899
VERSION     NP_060899.2
DBSOURCE    REFSEQ: accession NM_018429.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2624)
  AUTHORS   Son,H.J., Mo,H.Y., Yoo,N.J. and Lee,S.H.
  TITLE     Somatic mutations of cancer-related genes PELP1 and BDP1 in
            colorectal cancers
  JOURNAL   Pathol Res Pract 216 (10), 153107 (2020)
   PUBMED   32853945
  REMARK    GeneRIF: Somatic mutations of cancer-related genes PELP1 and BDP1
            in colorectal cancers.
REFERENCE   2  (residues 1 to 2624)
  AUTHORS   Kramm,K., Schroder,T., Gouge,J., Vera,A.M., Gupta,K., Heiss,F.B.,
            Liedl,T., Engel,C., Berger,I., Vannini,A., Tinnefeld,P. and
            Grohmann,D.
  TITLE     DNA origami-based single-molecule force spectroscopy elucidates RNA
            Polymerase III pre-initiation complex stability
  JOURNAL   Nat Commun 11 (1), 2828 (2020)
   PUBMED   32504003
  REMARK    GeneRIF: DNA origami-based single-molecule force spectroscopy
            elucidates RNA Polymerase III pre-initiation complex stability.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2624)
  AUTHORS   Gouge,J., Guthertz,N., Kramm,K., Dergai,O., Abascal-Palacios,G.,
            Satia,K., Cousin,P., Hernandez,N., Grohmann,D. and Vannini,A.
  TITLE     Molecular mechanisms of Bdp1 in TFIIIB assembly and RNA polymerase
            III transcription initiation
  JOURNAL   Nat Commun 8 (1), 130 (2017)
   PUBMED   28743884
  REMARK    GeneRIF: Data indicate the crystal structure of a Brf2-TBP-Bdp1
            complex bound to a DNA promoter.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2624)
  AUTHORS   Girotto,G., Abdulhadi,K., Buniello,A., Vozzi,D., Licastro,D.,
            d'Eustacchio,A., Vuckovic,D., Alkowari,M.K., Steel,K.P., Badii,R.
            and Gasparini,P.
  TITLE     Linkage study and exome sequencing identify a BDP1 mutation
            associated with hereditary hearing loss
  JOURNAL   PLoS One 8 (12), e80323 (2013)
   PUBMED   24312468
  REMARK    GeneRIF: Linkage study and exome sequencing identify a BDP1
            mutation associated with hereditary hearing loss.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2624)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 2624)
  AUTHORS   Teichmann,M., Wang,Z. and Roeder,R.G.
  TITLE     A stable complex of a novel transcription factor IIB- related
            factor, human TFIIIB50, and associated proteins mediate selective
            transcription by RNA polymerase III of genes with upstream promoter
            elements
  JOURNAL   Proc Natl Acad Sci U S A 97 (26), 14200-14205 (2000)
   PUBMED   11121026
REFERENCE   7  (residues 1 to 2624)
  AUTHORS   Kelter,A.R., Herchenbach,J. and Wirth,B.
  TITLE     The transcription factor-like nuclear regulator (TFNR) contains a
            novel 55-amino-acid motif repeated nine times and maps closely to
            SMN1
  JOURNAL   Genomics 70 (3), 315-326 (2000)
   PUBMED   11161782
REFERENCE   8  (residues 1 to 2624)
  AUTHORS   Schramm,L., Pendergrast,P.S., Sun,Y. and Hernandez,N.
  TITLE     Different human TFIIIB activities direct RNA polymerase III
            transcription from TATA-containing and TATA-less promoters
  JOURNAL   Genes Dev 14 (20), 2650-2663 (2000)
   PUBMED   11040218
REFERENCE   9  (residues 1 to 2624)
  AUTHORS   Chu,W.M., Wang,Z., Roeder,R.G. and Schmid,C.W.
  TITLE     RNA polymerase III transcription repressed by Rb through its
            interactions with TFIIIB and TFIIIC2
  JOURNAL   J Biol Chem 272 (23), 14755-14761 (1997)
   PUBMED   9169441
REFERENCE   10 (residues 1 to 2624)
  AUTHORS   Wang,Z. and Roeder,R.G.
  TITLE     Three human RNA polymerase III-specific subunits form a subcomplex
            with a selective function in specific transcription initiation
  JOURNAL   Genes Dev 11 (10), 1315-1326 (1997)
   PUBMED   9171375
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP246483.1, BP347992.1,
            AB051476.3, AC138832.2 and AI537645.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 23, 2006 this sequence version replaced NP_060899.1.
            
            Summary: The product of this gene is a subunit of the TFIIIB
            transcription initiation complex, which recruits RNA polymerase III
            to target promoters in order to initiate transcription. The encoded
            protein localizes to concentrated aggregates in the nucleus, and is
            required for transcription from all three types of polymerase III
            promoters. It is phosphorylated by casein kinase II during mitosis,
            resulting in its release from chromatin and suppression of
            polymerase III transcription. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC146792.1, AB051476.3 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000358731.9/ ENSP00000351575.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2624
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..2624
                     /product="transcription factor TFIIIB component B''
                     homolog"
                     /note="TATA box binding protein (TBP)-associated factor,
                     RNA polymerase III, GTF3B subunit 1; transcription
                     factor-like nuclear regulator; transcription factor IIIB
                     150; RNA polymerase III transcription initiation factor
                     B''; B double prime 1, subunit of RNA polymerase III
                     transcription initiation factor IIIB"
                     /calculated_mol_wt=293755
     Region          1..299
                     /region_name="Interaction with ZBTB43.
                     /evidence=ECO:0000269|PubMed:16542149"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1..142
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          193..241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          293..377
                     /region_name="Myb_DNA-bind_7"
                     /note="Myb DNA-binding like; pfam15963"
                     /db_xref="CDD:464956"
     Region          355..470
                     /region_name="Required for phosphorylation by CSNK2A1"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          379..449
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          544..567
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          606..663
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          729..759
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          823..1327
                     /region_name="9 X 55 AA repeats of
                     G-R-R-X-I-S-P-X-E-N-G-X-E-E-V-K-P-X-X-E-M-E-T-D-L-K-X-T-G-
                     R-E-X-X-X-R-E-K-T-X-E-X-X-D-A-X-E-E-I-D-X-D-L-E-E-T"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          <824..>1336
                     /region_name="PRK02224"
                     /note="DNA double-strand break repair Rad50 ATPase"
                     /db_xref="CDD:179385"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          930..1222
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1306..1348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1365..1440
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1519..1543
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1684..1722
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          1819..1863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          2130..2164
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          2181..2200
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          2207..2241
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          2444..2501
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     Region          2519..2566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6H8Y1.3)"
     CDS             1..2624
                     /gene="BDP1"
                     /gene_synonym="DFNB112; HSA238520; TAF3B1; TFC5; TFIIIB'';
                     TFIIIB150; TFIIIB90; TFNR"
                     /coded_by="NM_018429.3:228..8102"
                     /db_xref="CCDS:CCDS43328.1"
                     /db_xref="GeneID:55814"
                     /db_xref="HGNC:HGNC:13652"
                     /db_xref="MIM:607012"
ORIGIN      
        1 mfrrarlsvk pnvrpgvgar gstasnpqrg resprppdpa tdsaskpaep tdvptvdfgg
       61 aepqekaprs stektggdnd veessrssst vsqrrkriss tsslvkssvs vpseshplst
      121 inqeapqpta tstkekqpcs dryriykaqk lremlkeelr kekkqwknky ainesqrppd
      181 rskmtmrdfi yylpdnnpmt ssleqekkte kpstpvqtre qegkstpnae dnemeeetdd
      241 gpllvprvkv aedgsiilde esltvevlrt kgpcvveend pifergsttt yssfrknyys
      301 kpwsnketdm fflaismvgt dfsmigqlfp hrarieiknk fkreektngw ridkafqekr
      361 pfdfdffahl lqkvlaeeek rkqksvknhs lkekkstkpr knvkvkkvac egvnndpdes
      421 mssrisdter sqkdaqtvee esltlsreda eqvalevdln qkkrrrkkqd ganelgvnnl
      481 lenatvqagp skgekhknkc qairpelkeg ecskeqmlsc tqnidgivgf astekvekrt
      541 dpilslsnqq datsvatess esstsdlpsf evgiralcev nnaegsciee rnvdlknnsl
      601 eidqtenvkp mlrgrfqrpk pnlsragkks vlsqgktese sknshsktsv eknhvekdkm
      661 ntldilrmet terenpeaet vsvlgekncl qegsqlkalr pvqvrgrlqk pkpnagkaae
      721 rkeilisqee iganveknen escadrdtpq hmedqsrkdf eeedvilqpe kndsfqnvqp
      781 depkvlnecl svqennkank lnqvpilrtr fqkpkpnigr gtgrreissk eevlekilvs
      841 gemaaalret vrldtspkem vpaeintkem qsdlketgrr aisprekild viddtiemet
      901 glkamgreic lrektpevid ateeidkdle eagrreispq kngpeevkpl gevetdlkat
      961 gnessprekt pevtdateei dknleetgrr kisprengpe evkpvdemet dlnatgress
     1021 prektpevid ateeidleet erevspqeng leevkplgem etdlkatgrd sfprgktpev
     1081 idaieeieid leetereisp qengleevkp lgemqtdlka tgreisprek tpevidatee
     1141 idkdleetgr reispeengp eevkpvdeme tdlkttgreg ssrektrevi daaevietdl
     1201 eetereispq engpeevkpv gkmetdlkei reeisqrekv laefsairek eidlketgkr
     1261 dipimekvsg kmavveemea dlketgkenf rergseeicv teekvaelkq tgktdispre
     1321 neleetstsr qtdthlmqsg sndfsavpsl diqnissevl smmhtpveek rnsekevssh
     1381 fshfkissqt hesdktevqg iqspdvpeqf sdinlskslp qeqkpleikp apfvrsrfkr
     1441 pkpnlaraal kretteseky iyekksetkk metivmqenn eqtdtlpsqh deaslmisre
     1501 kdtlghrnee avilpctqte rnlspsnsce pkeesqsapv qkndsvvsvg tnnvntfqqe
     1561 mkesviqtar qvrgrlqrpr pnirktgqrq ivdkgeakgi ikegrtilpk detekkvltv
     1621 snsqieteie vpssavpehr myenqsqvvl venlhvnktn etirhenkpy vpssaqmtrr
     1681 kfqkakpnlg rahskkeepv lekvttdqsk egkpedhllq kgasntqlll kekaelltsl
     1741 evsarkdcvg skesalakid aeleevgpsr rvgeetvgdn spssvveeqy lnkltscpqp
     1801 lnetsyskia ldgkttisst seyernrger rshkkfkpnv trgrgskrvr gktskkepra
     1861 skamlvtlra sqeedddadd fesdyeeesy hlapeevnka pvfvpvglrs pepvsaqiee
     1921 tmeeleitvn vpdvgciavv ehelpntdvt teemkqeenl svpfemttse hiqdepgtnd
     1981 gsteaaitll tmgdlvlqse isseqgdvgv ciiphvhskd kshipssldn vnhkivhecq
     2041 elsspvitts pasfeenkiv leeqssreei slmekvkena tptrntiskv tsnlrirsrl
     2101 akpkpnlekt lgtnrlddyq evsslcvtkg aemetqrete knaskatele nknlgpvtta
     2161 enkdqsklac vhgikgtsis sevnlterne nqeessqevh mlsvapvass etgpctlgld
     2221 rglgensvee pqikdskgds vltlpvpeyt ptsipevqqe niinpqdltv nlvanvpqdg
     2281 edeqafiltl veipanavee ftdataqfmp npllpapilv ksvnteergd msiclpatsv
     2341 gqdamglsis grdnskkppd nldlvsrkrf qcrldkndhi ppakkrsltl rddcqeytte
     2401 vhskeltnvf eetgeshkgq difltsgstl ttpepqrqqv eaafqsrgsr spdacmdknv
     2461 pqlpqdemiv sdkeertdaa pksqqmdsrt ssskaslsrp grrplgflsl icsknslesd
     2521 epmqvhskkr lkplipglrk klkrsnpfne sqeknressd llpspsvitt qsenisssat
     2581 qvscdqpllk egyksaqkra pqgeattvse yffndifiev dete
//
LOCUS       NP_612405                346 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF9 [Homo sapiens].
ACCESSION   NP_612405
VERSION     NP_612405.2
DBSOURCE    REFSEQ: accession NM_138396.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Zhang,J., Jiao,Q. and Chen,Z.
  TITLE     Investigating the Prognostic and Oncogenic Roles of
            Membrane-Associated Ring-CH-Type Finger 9 in Colorectal Cancer
  JOURNAL   Genet Res (Camb) 2024, 9279653 (2024)
   PUBMED   39185021
  REMARK    GeneRIF: Investigating the Prognostic and Oncogenic Roles of
            Membrane-Associated Ring-CH-Type Finger 9 in Colorectal Cancer.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Tan,C., Byrne,E.F.X., Ah-Cann,C., Call,M.J. and Call,M.E.
  TITLE     A serine in the first transmembrane domain of the human E3
            ubiquitin ligase MARCH9 is critical for down-regulation of its
            protein substrates
  JOURNAL   J Biol Chem 294 (7), 2470-2485 (2019)
   PUBMED   30554144
  REMARK    GeneRIF: biochemical and structural findings demonstrate that
            specific sequences in the alpha-helical MARCH9 TM domains make
            crucial contributions to its ability to down-regulate its protein
            substrates.
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Luoto,S., Hermelo,I., Vuorinen,E.M., Hannus,P., Kesseli,J.,
            Nykter,M. and Granberg,K.J.
  TITLE     Computational Characterization of Suppressive Immune
            Microenvironments in Glioblastoma
  JOURNAL   Cancer Res 78 (19), 5574-5585 (2018)
   PUBMED   29921698
  REMARK    GeneRIF: analysis of glioblastoma alterations such as IDH mutation,
            NF1 inactivation, and CDK4-MARCH9 locus amplification
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Shen,Q.M., Wang,H.Y. and Xu,S.
  TITLE     MARCH9 Suppresses Lung Adenocarcinoma Progression by Downregulating
            ICAM-1
  JOURNAL   Cell Physiol Biochem 50 (1), 92-107 (2018)
   PUBMED   30278450
  REMARK    GeneRIF: Overexpression of MARCH9 was found to attenuate the
            oncogenic effect of ICAM-1, suggesting that MARCH9 may inhibit
            tumor progression by downregulating ICAM-1 signaling.
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Nice,T.J., Deng,W., Coscoy,L. and Raulet,D.H.
  TITLE     Stress-regulated targeting of the NKG2D ligand Mult1 by a
            membrane-associated RING-CH family E3 ligase
  JOURNAL   J Immunol 185 (9), 5369-5376 (2010)
   PUBMED   20870941
  REMARK    GeneRIF: Downregulation of Mult1 by MARCH9 was reversed by
            heat-shock treatment, which resulted in the dissociation of the two
            proteins and increased the amount of Mult1 at the cell surface.
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Hoer,S., Smith,L. and Lehner,P.J.
  TITLE     MARCH-IX mediates ubiquitination and downregulation of ICAM-1
  JOURNAL   FEBS Lett 581 (1), 45-51 (2007)
   PUBMED   17174307
  REMARK    GeneRIF: MARCH-IX expression causes ubiquitination and
            downregulation of ICAM-1
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC050397.1, AC025165.27 and AK093897.1.
            
            On Dec 20, 2003 this sequence version replaced NP_612405.1.
            
            Summary: MARCH9 is a member of the MARCH family of membrane-bound
            E3 ubiquitin ligases (EC 6.3.2.19). MARCH enzymes add ubiquitin
            (see MIM 191339) to target lysines in substrate proteins, thereby
            signaling their vesicular transport between membrane compartments.
            MARCH9 induces internalization of several membrane glycoproteins
            and directs them to the endosomal compartment (Bartee et al., 2004
            [PubMed 14722266]; Hoer et al., 2007 [PubMed 17174307]).[supplied
            by OMIM, Apr 2010].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.240481.1, BC050397.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000266643.6/ ENSP00000266643.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..346
                     /product="E3 ubiquitin-protein ligase MARCHF9"
                     /EC_number="2.3.2.27"
                     /note="membrane-associated RING-CH protein IX; E3
                     ubiquitin-protein ligase MARCH9; RING finger protein 179;
                     membrane-associated RING finger protein 9;
                     membrane-associated ring finger (C3HC4) 9; membrane
                     associated ring finger 9; RING-type E3 ubiquitin
                     transferase MARCH9; RING-type E3 ubiquitin transferase
                     MARCHF9"
                     /calculated_mol_wt=37641
     Region          20..39
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     Region          47..92
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     Region          109..159
                     /region_name="RING_CH-C4HC3_MARCH4_9"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING finger protein MARCH4, MARCH9,
                     and similar proteins; cd16811"
                     /db_xref="CDD:319725"
     Site            185..205
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     Site            219..239
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     Region          273..301
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     Region          326..346
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86YJ5.2)"
     CDS             1..346
                     /gene="MARCHF9"
                     /gene_synonym="MARCH-IX; MARCH9; RNF179"
                     /coded_by="NM_138396.6:427..1467"
                     /db_xref="CCDS:CCDS31847.1"
                     /db_xref="GeneID:92979"
                     /db_xref="HGNC:HGNC:25139"
                     /db_xref="MIM:613336"
ORIGIN      
        1 mlksrlrmfl nelkllvltg ggrpraepqp rggrgggcgw apfagcstrd gdgdeeeyyg
       61 seprarglag dkepragplp ppapplpppg aldalslsss ldsglrtpqc ricfqgpeqg
      121 ellspcrcdg svrcthqpcl irwisergsw scelcyfkyq vlaistknpl qwqaisltvi
      181 ekvqiaaivl gslflvasis wliwsslsps akwqrqdllf qicygmygfm dvvcigliih
      241 egssvyrifk rwqavnqqwk vlnydktkdi ggdagggtag ksgprnsrtg ptsgatsrpp
      301 aaqrmrtllp qrcgytilhl lgqlrppdar ssshsgrevv mrvttv
//
LOCUS       NP_001303992             340 aa            linear   PRI 20-NOV-2025
DEFINITION  methylosome protein WDR77 isoform 3 [Homo sapiens].
ACCESSION   NP_001303992
VERSION     NP_001303992.1
DBSOURCE    REFSEQ: accession NM_001317063.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 340)
  AUTHORS   Xu,W., Huang,Z., Xiao,Y., Li,W., Xu,M., Zhao,Q. and Yi,P.
  TITLE     HNRNPC promotes estrogen receptor-positive breast cancer cell cycle
            by stabilizing WDR77 mRNA in an m6A-dependent manner
  JOURNAL   Mol Carcinog 63 (5), 859-873 (2024)
   PUBMED   38353359
  REMARK    GeneRIF: HNRNPC promotes estrogen receptor-positive breast cancer
            cell cycle by stabilizing WDR77 mRNA in an m6A-dependent manner.
REFERENCE   2  (residues 1 to 340)
  AUTHORS   Ichikawa,T., Suekane,A., Nakahata,S., Iha,H., Shimoda,K.,
            Murakami,T. and Morishita,K.
  TITLE     Inhibition of PRMT5/MEP50 Arginine Methyltransferase Activity
            Causes Cancer Vulnerability in NDRG2low Adult T-Cell
            Leukemia/Lymphoma
  JOURNAL   Int J Mol Sci 25 (5), 2842 (2024)
   PUBMED   38474089
  REMARK    GeneRIF: Inhibition of PRMT5/MEP50 Arginine Methyltransferase
            Activity Causes Cancer Vulnerability in NDRG2[low] Adult T-Cell
            Leukemia/Lymphoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 340)
  AUTHORS   Mulvaney,K.M., Blomquist,C., Acharya,N., Li,R., Ranaghan,M.J.,
            O'Keefe,M., Rodriguez,D.J., Young,M.J., Kesar,D., Pal,D.,
            Stokes,M., Nelson,A.J., Jain,S.S., Yang,A., Mullin-Bernstein,Z.,
            Columbus,J., Bozal,F.K., Skepner,A., Raymond,D., LaRussa,S.,
            McKinney,D.C., Freyzon,Y., Baidi,Y., Porter,D., Aguirre,A.J.,
            Ianari,A., McMillan,B. and Sellers,W.R.
  TITLE     Molecular basis for substrate recruitment to the PRMT5 methylosome
  JOURNAL   Mol Cell 81 (17), 3481-3495 (2021)
   PUBMED   34358446
REFERENCE   4  (residues 1 to 340)
  AUTHORS   Zhao,Y., Yu,T., Sun,J., Wang,F., Cheng,C., He,S., Chen,L., Xie,D.,
            Fu,L., Guan,X., Yan,A., Li,Y., Miao,G. and Zhu,X.
  TITLE     Germ-line mutations in WDR77 predispose to familial papillary
            thyroid cancer
  JOURNAL   Proc Natl Acad Sci U S A 118 (31) (2021)
   PUBMED   34326253
  REMARK    GeneRIF: Germ-line mutations in WDR77 predispose to familial
            papillary thyroid cancer.
REFERENCE   5  (residues 1 to 340)
  AUTHORS   Yuan,H., Zhao,L., Yuan,Y., Yun,H., Zheng,W., Geng,Y., Yang,G.,
            Wang,Y., Zhao,M. and Zhang,X.
  TITLE     HBx represses WDR77 to enhance HBV replication by DDB1-mediated
            WDR77 degradation in the liver
  JOURNAL   Theranostics 11 (17), 8362-8378 (2021)
   PUBMED   34373747
  REMARK    GeneRIF: HBx represses WDR77 to enhance HBV replication by
            DDB1-mediated WDR77 degradation in the liver.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 340)
  AUTHORS   Yamada,S., Ohira,M., Horie,H., Ando,K., Takayasu,H., Suzuki,Y.,
            Sugano,S., Hirata,T., Goto,T., Matsunaga,T., Hiyama,E., Hayashi,Y.,
            Ando,H., Suita,S., Kaneko,M., Sasaki,F., Hashizume,K., Ohnuma,N.
            and Nakagawara,A.
  TITLE     Expression profiling and differential screening between
            hepatoblastomas and the corresponding normal livers: identification
            of high expression of the PLK1 oncogene as a poor-prognostic
            indicator of hepatoblastomas
  JOURNAL   Oncogene 23 (35), 5901-5911 (2004)
   PUBMED   15221005
REFERENCE   7  (residues 1 to 340)
  AUTHORS   Yong,J., Wan,L. and Dreyfuss,G.
  TITLE     Why do cells need an assembly machine for RNA-protein complexes?
  JOURNAL   Trends Cell Biol 14 (5), 226-232 (2004)
   PUBMED   15130578
  REMARK    Review article
REFERENCE   8  (residues 1 to 340)
  AUTHORS   Hosohata,K., Li,P., Hosohata,Y., Qin,J., Roeder,R.G. and Wang,Z.
  TITLE     Purification and identification of a novel complex which is
            involved in androgen receptor-dependent transcription
  JOURNAL   Mol Cell Biol 23 (19), 7019-7029 (2003)
   PUBMED   12972618
REFERENCE   9  (residues 1 to 340)
  AUTHORS   Licciardo,P., Amente,S., Ruggiero,L., Monti,M., Pucci,P., Lania,L.
            and Majello,B.
  TITLE     The FCP1 phosphatase interacts with RNA polymerase II and with
            MEP50 a component of the methylosome complex involved in the
            assembly of snRNP
  JOURNAL   Nucleic Acids Res 31 (3), 999-1005 (2003)
   PUBMED   12560496
REFERENCE   10 (residues 1 to 340)
  AUTHORS   Friesen,W.J., Wyce,A., Paushkin,S., Abel,L., Rappsilber,J., Mann,M.
            and Dreyfuss,G.
  TITLE     A novel WD repeat protein component of the methylosome binds Sm
            proteins
  JOURNAL   J Biol Chem 277 (10), 8243-8247 (2002)
   PUBMED   11756452
  REMARK    GeneRIF: Here, we describe a novel component of the methylosome, a
            50-kilodalton WD repeat protein termed methylosome protein 50
            (MEP50).
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB105102.1, AL557974.3,
            AL390195.10 and BC016946.1.
            
            Summary: The protein encoded by this gene is an androgen receptor
            coactivator that forms a complex with protein arginine
            methyltransferase 5, which modifies specific arginines to
            dimethylarginines in several spliceosomal Sm proteins. The encoded
            protein may be involved in the early stages of prostate cancer,
            with most of the protein being nuclear-localized in benign cells
            but cytoplasmic in cancer cells. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Nov 2015].
            
            Transcript Variant: This variant (3) uses two alternate in-frame
            splice junctions in the 3' end compared to variant 1. The resulting
            isoform (3) has the same N- and C-termini but is shorter compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7410570.21635.1, AL557974.3
                                           [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..340
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..340
                     /product="methylosome protein WDR77 isoform 3"
                     /note="methylosome protein 50; androgen receptor cofactor
                     p44; WD repeat-containing protein 77; testis tissue
                     sperm-binding protein Li 44a; methylosome protein WDR77"
                     /calculated_mol_wt=36290
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000269|Ref.8,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          22..75
                     /region_name="WD 1.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          78..116
                     /region_name="WD 2.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          80..317
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          123..162
                     /region_name="WD 3.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          128..164
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          165..205
                     /region_name="WD 4.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          171..207
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          209..250
                     /region_name="WD 5.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     Region          214..252
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          258..291
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          293..328
                     /region_name="WD 7.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00221,
                     ECO:0000269|PubMed:23071334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BQA1.1)"
     CDS             1..340
                     /gene="WDR77"
                     /gene_synonym="HKMT1069; MEP-50; MEP50; Nbla10071; p44;
                     p44/Mep50"
                     /coded_by="NM_001317063.2:88..1110"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:79084"
                     /db_xref="HGNC:HGNC:29652"
                     /db_xref="MIM:611734"
ORIGIN      
        1 mrketppplv ppaarewnlp pnapacmerq leaaryrsdg alllgassls grcwagslwl
       61 fkdpcaapne gfcsagvqte agvadltwvg ergilvasds gavelwelde netlivskfc
      121 kyehddivst vsvlssgtqa vsgskdicik vwdlaqqvvl ssyrahaaqv tcvaasphkd
      181 svflscsedn rillwdtrcp kpasqigcsa pgylptslaw hpqqsevfvf gdengtvslv
      241 dtkstscvls savhsqcvtg lvfsphsvpf laslsedcsl avldsslsel sqahrdfvrd
      301 atwsplnhsl lttvgwdhqv vhhvvptepl papgpasvte
//
LOCUS       NP_001334634             370 aa            linear   PRI 20-NOV-2025
DEFINITION  neuronal acetylcholine receptor subunit alpha-2 isoform 3 [Homo
            sapiens].
ACCESSION   NP_001334634 XP_016868492
VERSION     NP_001334634.1
DBSOURCE    REFSEQ: accession NM_001347705.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 370)
  AUTHORS   Demontis,D., Rajagopal,V.M., Thorgeirsson,T.E., Als,T.D., Grove,J.,
            Leppala,K., Gudbjartsson,D.F., Pallesen,J., Hjorthoj,C.,
            Reginsson,G.W., Tyrfingsson,T., Runarsdottir,V., Qvist,P.,
            Christensen,J.H., Bybjerg-Grauholm,J., Baekvad-Hansen,M.,
            Huckins,L.M., Stahl,E.A., Timmermann,A., Agerbo,E., Hougaard,D.M.,
            Werge,T., Mors,O., Mortensen,P.B., Nordentoft,M., Daly,M.J.,
            Stefansson,H., Stefansson,K., Nyegaard,M. and Borglum,A.D.
  TITLE     Genome-wide association study implicates CHRNA2 in cannabis use
            disorder
  JOURNAL   Nat Neurosci 22 (7), 1066-1074 (2019)
   PUBMED   31209380
  REMARK    GeneRIF: The index variant (rs56372821) is a strong expression
            quantitative trait locus for CHRNA2; analyses of the genetically
            regulated gene expression identified a significant association of
            CHRNA2 expression with cannabis use disorder (CUD) in brain tissue.
            At the polygenic level, analyses revealed a significant decrease in
            the risk of CUD with increased load of variants associated with
            cognitive performance.
REFERENCE   2  (residues 1 to 370)
  AUTHORS   Wang,M., Liu,D., Schwender,H., Wang,H., Wang,P., Zhou,Z., Li,J.,
            Wu,T., Zhu,H. and Beaty,T.H.
  TITLE     Evaluating the effect of nicotinic cholinergic receptor genes on
            the risk of nonsyndromic cleft lip with or without cleft palate
  JOURNAL   Oral Dis 24 (6), 1068-1072 (2018)
   PUBMED   29688589
  REMARK    GeneRIF: In our analysis, we found one pair of SNPs in CHRNA1 and
            CHRNA7, plus one pair of SNPs in CHRNA2 and CHRNA3 reached
            corrected significance in tests for GxG interaction. Our study
            suggested evidence of interactions between CHRNs in controlling the
            risk of NSCL/P.
REFERENCE   3  (residues 1 to 370)
  AUTHORS   Jun,H., Yu,H., Gong,J., Jiang,J., Qiao,X., Perkey,E., Kim,D.I.,
            Emont,M.P., Zestos,A.G., Cho,J.S., Liu,J., Kennedy,R.T.,
            Maillard,I., Xu,X.Z.S. and Wu,J.
  TITLE     An immune-beige adipocyte communication via nicotinic acetylcholine
            receptor signaling
  JOURNAL   Nat Med 24 (6), 814-822 (2018)
   PUBMED   29785025
  REMARK    GeneRIF: These results reveal a beige-selective immune-adipose
            interaction mediated through CHRNA2 and identify a novel function
            of nicotinic acetylcholine receptors in energy metabolism.
REFERENCE   4  (residues 1 to 370)
  AUTHORS   Kouvatsos,N., Giastas,P., Chroni-Tzartou,D., Poulopoulou,C. and
            Tzartos,S.J.
  TITLE     Crystal structure of a human neuronal nAChR extracellular domain in
            pentameric assembly: Ligand-bound alpha2 homopentamer
  JOURNAL   Proc Natl Acad Sci U S A 113 (34), 9635-9640 (2016)
   PUBMED   27493220
  REMARK    GeneRIF: A crystal structure of a human neuronal CHRNA2
            extracellular domain in pentameric assembly has been reported.
REFERENCE   5  (residues 1 to 370)
  AUTHORS   Trivisano,M., Terracciano,A., Milano,T., Cappelletti,S.,
            Pietrafusa,N., Bertini,E.S., Vigevano,F. and Specchio,N.
  TITLE     Mutation of CHRNA2 in a family with benign familial infantile
            seizures: Potential role of nicotinic acetylcholine receptor in
            various phenotypes of epilepsy
  JOURNAL   Epilepsia 56 (5), e53-e57 (2015)
   PUBMED   25847220
  REMARK    GeneRIF: a heterozygous single-nucleotide substitution in CHRNA2
            gene (c.1126 C>T; p. Arg376Trp) in subjects with benign familial
            infantile seizures
REFERENCE   6  (residues 1 to 370)
  AUTHORS   Elliott,K.J., Ellis,S.B., Berckhan,K.J., Urrutia,A.,
            Chavez-Noriega,L.E., Johnson,E.C., Velicelebi,G. and Harpold,M.M.
  TITLE     Comparative structure of human neuronal alpha 2-alpha 7 and beta
            2-beta 4 nicotinic acetylcholine receptor subunits and functional
            expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and
            beta 4 subunits
  JOURNAL   J Mol Neurosci 7 (3), 217-228 (1996)
   PUBMED   8906617
REFERENCE   7  (residues 1 to 370)
  AUTHORS   Garcia-Colunga,J. and Miledi,R.
  TITLE     Effects of serotonergic agents on neuronal nicotinic acetylcholine
            receptors
  JOURNAL   Proc Natl Acad Sci U S A 92 (7), 2919-2923 (1995)
   PUBMED   7708749
REFERENCE   8  (residues 1 to 370)
  AUTHORS   Wood,S., Schertzer,M. and Yaremko,M.L.
  TITLE     Identification of the human neuronal nicotinic cholinergic alpha 2
            receptor locus, (CHRNA2), within an 8p21 mapped locus, by sequence
            homology with rat DNA
  JOURNAL   Somat Cell Mol Genet 21 (2), 147-150 (1995)
   PUBMED   7570187
REFERENCE   9  (residues 1 to 370)
  AUTHORS   Kurahashi,H. and Hirose,S.
  TITLE     Autosomal Dominant Sleep-Related Hypermotor (Hyperkinetic) Epilepsy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301348
REFERENCE   10 (residues 1 to 370)
  AUTHORS   Anand,R. and Lindstrom,J.
  TITLE     Chromosomal localization of seven neuronal nicotinic acetylcholine
            receptor subunit genes in humans
  JOURNAL   Genomics 13 (4), 962-967 (1992)
   PUBMED   1505988
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF311103.5.
            
            On Dec 9, 2016 this sequence version replaced XP_016868492.1.
            
            Summary: Nicotinic acetylcholine receptors (nAChRs) are
            ligand-gated ion channels formed by a pentameric arrangement of
            alpha and beta subunits to create distinct muscle and neuronal
            receptors. Neuronal receptors are found throughout the peripheral
            and central nervous system where they are involved in fast synaptic
            transmission. This gene encodes an alpha subunit that is widely
            expressed in the brain. The proposed structure for nAChR subunits
            is a conserved N-terminal extracellular domain followed by three
            conserved transmembrane domains, a variable cytoplasmic loop, a
            fourth conserved transmembrane domain, and a short C-terminal
            extracellular region. Mutations in this gene cause autosomal
            dominant nocturnal frontal lobe epilepsy type 4. Single nucleotide
            polymorphisms (SNPs) in this gene have been associated with
            nicotine dependence. [provided by RefSeq, Nov 2009].
            
            Transcript Variant: This variant (3), as well as variant 4, encodes
            isoform 3.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.194490.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153427, SAMEA2155984
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..370
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.2"
     Protein         1..370
                     /product="neuronal acetylcholine receptor subunit alpha-2
                     isoform 3"
                     /note="cholinergic receptor, nicotinic, alpha polypeptide
                     2 (neuronal); cholinergic receptor, nicotinic alpha 2;
                     neuronal acetylcholine receptor subunit alpha-2;
                     acetylcholine receptor, nicotinic, alpha 2 (neuronal);
                     cholinergic receptor, nicotinic, alpha 2 (neuronal);
                     nicotinic acetylcholine receptor subunit alpha-2"
                     /calculated_mol_wt=41659
     Region          <1..106
                     /region_name="LGIC_ECD"
                     /note="extracellular domain (ECD) of Cys-loop
                     neurotransmitter-gated ion channels (also known as
                     ligand-gated ion channel (LGIC)); cl28912"
                     /db_xref="CDD:475126"
     Region          113..361
                     /region_name="Neur_chan_memb"
                     /note="Neurotransmitter-gated ion-channel transmembrane
                     region; pfam02932"
                     /db_xref="CDD:460753"
     CDS             1..370
                     /gene="CHRNA2"
                     /coded_by="NM_001347705.2:1002..2114"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="GeneID:1135"
                     /db_xref="HGNC:HGNC:1956"
                     /db_xref="MIM:118502"
ORIGIN      
        1 mtkahlfstg tvhwvppaiy ksscsidvtf fpfdqqnckm kfgswtydka kidleqmeqt
       61 vdlkdywesg ewaivnatgt ynskkydcca eiypdvtyaf virrlplfyt inliipclli
      121 scltvlvfyl psdcgekitl cisvllsltv fllliteiip stslviplig eyllftmifv
      181 tlsivitvfv lnvhhrspst htmphwvrga llgcvprwll mnrppppvel chplrlklsp
      241 syhwlesnvd aeerevvvee edrwacaghv apsvgtlcsh ghlhsgasgp kaeallqege
      301 lllsphmqka legvhyiadh lrsedadssv kedwkyvamv idriflwlfi ivcflgtigl
      361 flppflagmi
//
LOCUS       NP_001357268             158 aa            linear   PRI 20-NOV-2025
DEFINITION  high mobility group protein B1 isoform 2 [Homo sapiens].
ACCESSION   NP_001357268 XP_024305111
VERSION     NP_001357268.1
DBSOURCE    REFSEQ: accession NM_001370339.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Wang,S., Cheng,T., Chen,X., Zeng,C., Qin,W. and Xu,Y.
  TITLE     IFN-gamma induces acute graft-versus-host disease by promoting
            HMGB1-mediated nuclear-to-cytoplasm translocation and autophagic
            degradation of p53
  JOURNAL   Clin Sci (Lond) 138 (20), 1287-1304 (2024)
   PUBMED   39312196
  REMARK    GeneRIF: IFN-gamma induces acute graft-versus-host disease by
            promoting HMGB1-mediated nuclear-to-cytoplasm translocation and
            autophagic degradation of p53.
REFERENCE   3  (residues 1 to 158)
  AUTHORS   De Luca,G., Goette,N.P., Lev,P.R., Baroni Pietto,M.C., Marin
            Oyarzun,C.P., Castro Rios,M.A., Moiraghi,B., Sackmann,F.,
            Kamiya,L.J., Verri,V., Caula,V., Fernandez,V., Vicente,A., Pose
            Cabarcos,J., Caruso,V., Camacho,M.F., Larripa,I.B., Khoury,M.,
            Marta,R.F., Glembotsky,A.C. and Heller,P.G.
  TITLE     Elevated levels of damage-associated molecular patterns HMGB1 and
            S100A8/A9 coupled with toll-like receptor-triggered monocyte
            activation are associated with inflammation in patients with
            myelofibrosis
  JOURNAL   Front Immunol 15, 1365015 (2024)
   PUBMED   39391311
  REMARK    GeneRIF: Elevated levels of damage-associated molecular patterns
            HMGB1 and S100A8/A9 coupled with toll-like receptor-triggered
            monocyte activation are associated with inflammation in patients
            with myelofibrosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Ozbay Kurt,F.G., Cicortas,B.A., Balzasch,B.M., De la Torre,C.,
            Ast,V., Tavukcuoglu,E., Ak,C., Wohlfeil,S.A., Cerwenka,A.,
            Utikal,J. and Umansky,V.
  TITLE     S100A9 and HMGB1 orchestrate MDSC-mediated immunosuppression in
            melanoma through TLR4 signaling
  JOURNAL   J Immunother Cancer 12 (9), e009552 (2024)
   PUBMED   39266214
  REMARK    GeneRIF: S100A9 and HMGB1 orchestrate MDSC-mediated
            immunosuppression in melanoma through TLR4 signaling.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Ferrari,S., Finelli,P., Rocchi,M. and Bianchi,M.E.
  TITLE     The active gene that encodes human high mobility group 1 protein
            (HMG1) contains introns and maps to chromosome 13
  JOURNAL   Genomics 35 (2), 367-371 (1996)
   PUBMED   8661151
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Ge,H. and Roeder,R.G.
  TITLE     The high mobility group protein HMG1 can reversibly inhibit class
            II gene transcription by interaction with the TATA-binding protein
  JOURNAL   J Biol Chem 269 (25), 17136-17140 (1994)
   PUBMED   8006019
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Paull,T.T., Haykinson,M.J. and Johnson,R.C.
  TITLE     The nonspecific DNA-binding and -bending proteins HMG1 and HMG2
            promote the assembly of complex nucleoprotein structures
  JOURNAL   Genes Dev 7 (8), 1521-1534 (1993)
   PUBMED   8339930
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Parkkinen,J. and Rauvala,H.
  TITLE     Interactions of plasminogen and tissue plasminogen activator (t-PA)
            with amphoterin. Enhancement of t-PA-catalyzed plasminogen
            activation by amphoterin
  JOURNAL   J Biol Chem 266 (25), 16730-16735 (1991)
   PUBMED   1909331
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Wen,L., Huang,J.K., Johnson,B.H. and Reeck,G.R.
  TITLE     A human placental cDNA clone that encodes nonhistone chromosomal
            protein HMG-1
  JOURNAL   Nucleic Acids Res 17 (3), 1197-1214 (1989)
   PUBMED   2922262
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Bernues,J., Espel,E. and Querol,E.
  TITLE     Identification of the core-histone-binding domains of HMG1 and HMG2
  JOURNAL   Biochim Biophys Acta 866 (4), 242-251 (1986)
   PUBMED   3697355
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL353648.27.
            
            On May 7, 2019 this sequence version replaced XP_024305111.1.
            
            Summary: This gene encodes a protein that belongs to the High
            Mobility Group-box superfamily. The encoded non-histone, nuclear
            DNA-binding protein regulates transcription, and is involved in
            organization of DNA. This protein plays a role in several cellular
            processes, including inflammation, cell differentiation and tumor
            cell migration. Multiple pseudogenes of this gene have been
            identified. Alternative splicing results in multiple transcript
            variants that encode the same protein. [provided by RefSeq, Sep
            2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074967.225312.1,
                                           SRR14038191.2124332.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146411, SAMEA2149004
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.3"
     Protein         1..158
                     /product="high mobility group protein B1 isoform 2"
                     /note="Sulfoglucuronyl carbohydrate binding protein;
                     Amphoterin; high-mobility group (nonhistone chromosomal)
                     protein 1; high mobility group protein B1"
                     /calculated_mol_wt=18180
     Region          1..97
                     /region_name="Sufficient for interaction with HAVCR2.
                     /evidence=ECO:0000250|UniProtKB:P63158"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          3..15
                     /region_name="LPS binding (delipidated).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            3
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            7
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          8..76
                     /region_name="HMG-box_HMGB_rpt1"
                     /note="first high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21978"
                     /db_xref="CDD:438794"
     Site            order(8..10,13,16..17,19..21,25,28,35..36,38..39,41..43,
                     45..46,50)
                     /site_type="other"
                     /note="p53 binding site [polypeptide binding]"
                     /db_xref="CDD:438794"
     Site            order(8,10..11,13..17,20..21,36,38..39,41..43,46,49)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438794"
     Site            8
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            10..11
                     /site_type="cleavage"
                     /note="Cleavage, by thrombin:thrombomodulin.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          27..43
                     /region_name="Nuclear localization signal (NLS) 1.
                     /evidence=ECO:0000250|UniProtKB:P63159"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            28
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            29
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            30
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            35
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            43
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            67..68
                     /site_type="cleavage"
                     /note="Cleavage, by CASP1.
                     /evidence=ECO:0000269|PubMed:24474694; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          76..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          80..96
                     /region_name="LPS binding (Lipid A).
                     /evidence=ECO:0000269|PubMed:21660935"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Region          89..108
                     /region_name="Cytokine-stimulating activity.
                     /evidence=ECO:0000269|PubMed:12765338"
                     /note="propagated from UniProtKB/Swiss-Prot (P09429.3)"
     Site            90
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Region          93..157
                     /region_name="HMG-box_HMGB_rpt2"
                     /note="second high mobility group (HMG)-box found in the
                     high mobility group protein B (HMGB) family; cd21979"
                     /db_xref="CDD:438795"
     Site            order(94..100,102..104,106..107,110,122..123,125..127,130,
                     133,152,155..156)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:438795"
     Site            100
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            127
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            128
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P10103; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     Site            141
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P63158; propagated from
                     UniProtKB/Swiss-Prot (P09429.3)"
     CDS             1..158
                     /gene="HMGB1"
                     /gene_synonym="HMG-1; HMG1; HMG3; SBP-1"
                     /coded_by="NM_001370339.1:156..632"
                     /note="isoform 2 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS86347.1"
                     /db_xref="GeneID:3146"
                     /db_xref="HGNC:HGNC:4983"
                     /db_xref="MIM:163905"
ORIGIN      
        1 mgkgdpkkpr gkmssyaffv qtcreehkkk hpdasvnfse fskkcserwk tmsakekgkf
       61 edmakadkar yeremktyip pkgetkkkfk dpnapkrpps afflfcseyr pkikgehpgl
      121 sigdvakklg emwnntaadd kqpyekkaak lkekyekf
//
LOCUS       NP_001284584             684 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF2C isoform 2 [Homo sapiens].
ACCESSION   NP_001284584 XP_005270452
VERSION     NP_001284584.1
DBSOURCE    REFSEQ: accession NM_001297655.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Kalkan,B.M., Ozcan,S.C., Cicek,E., Gonen,M. and Acilan,C.
  TITLE     Nek2A prevents centrosome clustering and induces cell death in
            cancer cells via KIF2C interaction
  JOURNAL   Cell Death Dis 15 (3), 222 (2024)
   PUBMED   38493150
  REMARK    GeneRIF: Nek2A prevents centrosome clustering and induces cell
            death in cancer cells via KIF2C interaction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Deng,H., Gong,X., Ji,G., Li,C. and Cheng,S.
  TITLE     KIF2C promotes clear cell renal cell carcinoma progression via
            activating JAK2/STAT3 signaling pathway
  JOURNAL   Mol Cell Probes 72, 101938 (2023)
   PUBMED   37863123
  REMARK    GeneRIF: KIF2C promotes clear cell renal cell carcinoma progression
            via activating JAK2/STAT3 signaling pathway.
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Li,S., Ma,Y., Wu,C. and Hou,X.
  TITLE     Knockdown of kinesin family member 2C restricts cell proliferation
            and induces cell cycle arrest in gastric cancer
  JOURNAL   Histol Histopathol 38 (8), 907-916 (2023)
   PUBMED   36448588
  REMARK    GeneRIF: Knockdown of kinesin family member 2C restricts cell
            proliferation and induces cell cycle arrest in gastric cancer.
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Cheng,L.J., Zhou,Z.M., Li,J.M., Zhu,H., Zhu,H., Zhou,Y.D.,
            Wang,L.R., Lin,M. and Sha,J.H.
  TITLE     Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in
            human testis
  JOURNAL   Life Sci 71 (23), 2741-2757 (2002)
   PUBMED   12383881
  REMARK    GeneRIF: identification as a candidate gene for the testis-specific
            KRPs and its specific expression in the testis was correlated with
            spermatogenesis and may be correlated with male infertility
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Miki,H., Setou,M., Kaneshiro,K. and Hirokawa,N.
  TITLE     All kinesin superfamily protein, KIF, genes in mouse and human
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7004-7011 (2001)
   PUBMED   11416179
  REMARK    Review article
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Sugata,N., Li,S., Earnshaw,W.C., Yen,T.J., Yoda,K., Masumoto,H.,
            Munekata,E., Warburton,P.E. and Todokoro,K.
  TITLE     Human CENP-H multimers colocalize with CENP-A and CENP-C at active
            centromere--kinetochore complexes
  JOURNAL   Hum Mol Genet 9 (19), 2919-2926 (2000)
   PUBMED   11092768
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Wordeman,L., Wagenbach,M. and Maney,T.
  TITLE     Mutations in the ATP-binding domain affect the subcellular
            distribution of mitotic centromere-associated kinesin (MCAK)
  JOURNAL   Cell Biol Int 23 (4), 275-286 (1999)
   PUBMED   10600236
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Maney,T., Hunter,A.W., Wagenbach,M. and Wordeman,L.
  TITLE     Mitotic centromere-associated kinesin is important for anaphase
            chromosome segregation
  JOURNAL   J Cell Biol 142 (3), 787-801 (1998)
   PUBMED   9700166
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Kim,I.G., Jun,D.Y., Sohn,U. and Kim,Y.H.
  TITLE     Cloning and expression of human mitotic centromere-associated
            kinesin gene
  JOURNAL   Biochim Biophys Acta 1359 (3), 181-186 (1997)
   PUBMED   9434124
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB264115.1, AK300756.1 and
            BU615368.1.
            
            On Jul 10, 2014 this sequence version replaced XP_005270452.1.
            
            Summary: This gene encodes a kinesin-like protein that functions as
            a microtubule-dependent molecular motor. The encoded protein can
            depolymerize microtubules at the plus end, thereby promoting
            mitotic chromosome segregation. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1. The encoded isoform (2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.246864.1, AK300756.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..684
                     /product="kinesin-like protein KIF2C isoform 2"
                     /note="mitotic centromere-associated kinesin; kinesin-like
                     protein KIF2C; kinesin-like protein 6; testis tissue
                     sperm-binding protein Li 68n"
                     /calculated_mol_wt=76852
     Region          217..545
                     /region_name="KISc_KIF2_like"
                     /note="Kinesin motor domain, KIF2-like group; cd01367"
                     /db_xref="CDD:276818"
     Site            order(225,307,310,312..315,451)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276818"
     Site            order(499,502,505)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276818"
     CDS             1..684
                     /gene="KIF2C"
                     /gene_synonym="CT139; KNSL6; MCAK"
                     /coded_by="NM_001297655.2:97..2151"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:11004"
                     /db_xref="HGNC:HGNC:6393"
                     /db_xref="MIM:604538"
ORIGIN      
        1 mamdsslqar lfpglaikiq rsnglihsan vrtvnleksc vsvewaegga tkgkeidfdd
       61 vaainpellq llplhpkdnl plqenvtiqk qkrrsvnski papkeslrsr strmstvsel
      121 ritaqendme velpaaansr kqfsvplrrk sclvkevekm knkreekkaq nsemrmkraq
      181 eydssfpnwe farmikefra tlechpltmt dpieehricv cvrkrplnkq elakkeidvi
      241 sipskclllv hepklkvdlt kylenqafcf dfafdetasn evvyrftarp lvqtifeggk
      301 atcfaygqtg sgkthtmggd lsgkaqnask giyamasrdv fllknqpcyr klglevyvtf
      361 feiyngklfd llnkkaklrv ledgkqqvqv vglqehlvns addvikmidm gsacrtsgqt
      421 fansnssrsh acfqiilrak grmhgkfslv dlagnergad tssadrqtrm egaeinksll
      481 alkeciralg qnkahtpfre skltqvlrds figensrtcm iatispgiss ceytlntlry
      541 adrvkelsph sgpsgeqliq meteemeacs ngalipgnls keeeelssqm ssfneamtqi
      601 releekamee lkeiiqqgpd wlelsemteq pdydletfvn kaesalaqqa khfsalrdvi
      661 kalrlamqle eqasrqissk krpq
//
LOCUS       NP_001308737             678 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform k [Homo sapiens].
ACCESSION   NP_001308737
VERSION     NP_001308737.1
DBSOURCE    REFSEQ: accession NM_001321808.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 678)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 678)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 678)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 678)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 678)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 678)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 678)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 678)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 678)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 678)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4, AC126185.2 and
            AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.2343247.1,
                                           SRR1660807.184451.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..678
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..678
                     /product="E3 ubiquitin-protein ligase CBL-B isoform k"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=74470
     Region          1..81
                     /region_name="Cbl_N3"
                     /note="CBL proto-oncogene N-terminus, SH2-like domain;
                     pfam02762"
                     /db_xref="CDD:460682"
     Region          91..166
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(102..103,106,130,149..152)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(106..108,114..117,136,139..140,143,149..150,152)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          627..667
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(629..630,632..634,636..637,642,646)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..678
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321808.2:1040..3076"
                     /note="isoform k is encoded by transcript variant 16"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mafltydevk arlqkystkp gsyifrlsct rlgqwaigyv tgdgnilqti phnkplfqal
       61 idgsregfyl ypdgrsynpd ltglceptph dhikvtqeqy elycemgstf qlckicaend
      121 kdvkiepcgh lmctscltaw qesdgqgcpf crceikgtep iivdpfdprd egsrccsiid
      181 pfgmpmldld ddddreeslm mnrlanvrkc tdrqnspvts pgssplaqrr kpqpdplqip
      241 hlslppvppr ldliqkgivr spcgsptgsp ksspcmvrkq dkplpapppp lrdppppppe
      301 rpppippdnr lsrhihhves vpsrdppmpl eawcprdvfg tnqlvgcrll gegspkpgit
      361 assnvngrhs rvgsdpvlmr khrrhdlple gakvfsnghl gseeydvppr lsppppvttl
      421 lpsikctgpl anslsektrd pveedddeyk ipsshpvsln sqpshchnvk ppvrscdngh
      481 cmlngthgps sekksnipdl siylkgedaf dalppslppp ppparhslie hskppgsssr
      541 pssgqdlfll psdpfvdlas gqvplpparr lpgenvktnr tsqdydqlps csdgsqapar
      601 ppkprprrta peihhrkphg peaalenvda kiaklmgegy afeevkrale iaqnnvevar
      661 silrefafpp pvsprlnl
//
LOCUS       NP_001405                305 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor eIF2B subunit alpha [Homo sapiens].
ACCESSION   NP_001405
VERSION     NP_001405.1
DBSOURCE    REFSEQ: accession NM_001414.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 305)
  AUTHORS   Wuerth,J.D. and Weber,F.
  TITLE     Shielding the mRNA-translation factor eIF2B from inhibitory p-eIF2
            as a viral strategy to evade protein kinase R-mediated innate
            immunity
  JOURNAL   Curr Opin Immunol 78, 102251 (2022)
   PUBMED   36242870
  REMARK    GeneRIF: Shielding the mRNA-translation factor eIF2B from
            inhibitory p-eIF2 as a viral strategy to evade protein kinase
            R-mediated innate immunity.
            Review article
REFERENCE   2  (residues 1 to 305)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 305)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 305)
  AUTHORS   De Franco,E., Caswell,R., Johnson,M.B., Wakeling,M.N., Zung,A.,
            Dung,V.C., Bich Ngoc,C.T., Goonetilleke,R., Vivanco Jury,M.,
            El-Khateeb,M., Ellard,S., Flanagan,S.E., Ron,D. and Hattersley,A.T.
  TITLE     De Novo Mutations in EIF2B1 Affecting eIF2 Signaling Cause
            Neonatal/Early-Onset Diabetes and Transient Hepatic Dysfunction
  JOURNAL   Diabetes 69 (3), 477-483 (2020)
   PUBMED   31882561
  REMARK    GeneRIF: Our results establish de novo EIF2B1 mutations as a novel
            cause of permanent diabetes and liver dysfunction. These findings
            confirm the importance of cell stress regulation for beta-cells and
            highlight EIF2B1's fundamental role within this pathway.
REFERENCE   5  (residues 1 to 305)
  AUTHORS   Yang,W. and Hinnebusch,A.G.
  TITLE     Identification of a regulatory subcomplex in the guanine nucleotide
            exchange factor eIF2B that mediates inhibition by phosphorylated
            eIF2
  JOURNAL   Mol Cell Biol 16 (11), 6603-6616 (1996)
   PUBMED   8887689
REFERENCE   6  (residues 1 to 305)
  AUTHORS   Welsh,G.I., Miyamoto,S., Price,N.T., Safer,B. and Proud,C.G.
  TITLE     T-cell activation leads to rapid stimulation of translation
            initiation factor eIF2B and inactivation of glycogen synthase
            kinase-3
  JOURNAL   J Biol Chem 271 (19), 11410-11413 (1996)
   PUBMED   8626696
REFERENCE   7  (residues 1 to 305)
  AUTHORS   Flowers,K.M., Mellor,H., Kimball,S.R. and Jefferson,L.S.
  TITLE     Structure and sequence of the gene encoding the alpha-subunit of
            rat translation initiation factor-2B
  JOURNAL   Biochim Biophys Acta 1264 (2), 163-167 (1995)
   PUBMED   7495858
REFERENCE   8  (residues 1 to 305)
  AUTHORS   Vanderver,A., Tonduti,D., Schiffmann,R., Schmidt,J. and van der
            Knaap,M.S.
  TITLE     Leukodystrophy Overview - RETIRED CHAPTER, FOR HISTORICAL REFERENCE
            ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   24501781
REFERENCE   9  (residues 1 to 305)
  AUTHORS   van der Knaap,M.S., Fogli,A., Boespflug-Tanguy,O., Abbink,T.E.M.
            and Schiffmann,R.
  TITLE     Childhood Ataxia with Central Nervous System Hypomyelination /
            Vanishing White Matter
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301435
REFERENCE   10 (residues 1 to 305)
  AUTHORS   Hershey,J.W.
  TITLE     Translational control in mammalian cells
  JOURNAL   Annu Rev Biochem 60, 717-755 (1991)
   PUBMED   1883206
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff in
            collaboration with Francesco Amaldi. The reference sequence was
            derived from AC117503.8.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes one of five subunits of eukaryotic
            translation initiation factor 2B (EIF2B), a GTP exchange factor for
            eukaryotic initiation factor 2 and an essential regulator for
            protein synthesis. Mutations in this gene and the genes encoding
            other EIF2B subunits have been associated with leukoencephalopathy
            with vanishing white matter. [provided by RefSeq, Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.5290.1,
                                           SRR1660807.189405.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424014.7/ ENSP00000416250.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..305
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..305
                     /product="translation initiation factor eIF2B subunit
                     alpha"
                     /note="eukaryotic translation initiation factor 2B,
                     subunit 1 alpha, 26kDa; eIF-2B GDP-GTP exchange factor
                     subunit alpha; eIF2B GDP-GTP exchange factor subunit
                     alpha"
                     /calculated_mol_wt=33581
     Region          15..293
                     /region_name="IF-2B"
                     /note="Initiation factor 2 subunit family; pfam01008"
                     /db_xref="CDD:395798"
     Site            35
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14232.1)"
     CDS             1..305
                     /gene="EIF2B1"
                     /gene_synonym="EIF2B; EIF2BA; EIF2Balpha; VWM1"
                     /coded_by="NM_001414.4:130..1047"
                     /db_xref="CCDS:CCDS31924.1"
                     /db_xref="GeneID:1967"
                     /db_xref="HGNC:HGNC:3257"
                     /db_xref="MIM:606686"
ORIGIN      
        1 mddkelieyf ksqmkedpdm asavaairtl leflkrdkge tiqglranlt saietlcgvd
       61 ssvavssgge lflrfislas leysdyskck kimiergelf lrrislsrnk iadlchtfik
      121 dgatilthay srvvlrvlea avaakkrfsv yvtesqpdls gkkmakalch lnvpvtvvld
      181 aavgyimeka dlvivgaegv venggiinki gtnqmavcak aqnkpfyvva esfkfvrlfp
      241 lnqqdvpdkf kykadtlkva qtgqdlkeeh pwvdytapsl itllftdlgv ltpsavsdel
      301 iklyl
//
LOCUS       NP_003852                942 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 5 isoform 1 [Homo sapiens].
ACCESSION   NP_003852 XP_031102
VERSION     NP_003852.1
DBSOURCE    REFSEQ: accession NM_003861.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 942)
  AUTHORS   Radko-Juettner,S., Yue,H., Myers,J.A., Carter,R.D., Robertson,A.N.,
            Mittal,P., Zhu,Z., Hansen,B.S., Donovan,K.A., Hunkeler,M.,
            Rosikiewicz,W., Wu,Z., McReynolds,M.G., Roy Burman,S.S.,
            Schmoker,A.M., Mageed,N., Brown,S.A., Mobley,R.J., Partridge,J.F.,
            Stewart,E.A., Pruett-Miller,S.M., Nabet,B., Peng,J., Gray,N.S.,
            Fischer,E.S. and Roberts,C.W.M.
  TITLE     Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing
            SWI/SNF
  JOURNAL   Nature 628 (8007), 442-449 (2024)
   PUBMED   38538798
  REMARK    GeneRIF: Targeting DCAF5 suppresses SMARCB1-mutant cancer by
            stabilizing SWI/SNF.
            Erratum:[Nature. 2024 May;629(8012):E12. doi:
            10.1038/s41586-024-07402-3. PMID: 38684813]
REFERENCE   2  (residues 1 to 942)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 942)
  AUTHORS   Zhang,C., Leng,F., Saxena,L., Hoang,N., Yu,J., Alejo,S., Lee,L.,
            Qi,D., Lu,F., Sun,H. and Zhang,H.
  TITLE     Proteolysis of methylated SOX2 protein is regulated by L3MBTL3 and
            CRL4DCAF5 ubiquitin ligase
  JOURNAL   J Biol Chem 294 (2), 476-489 (2019)
   PUBMED   30442713
REFERENCE   4  (residues 1 to 942)
  AUTHORS   Leng,F., Yu,J., Zhang,C., Alejo,S., Hoang,N., Sun,H., Lu,F. and
            Zhang,H.
  TITLE     Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3
            and CRL4DCAF5 ubiquitin ligase
  JOURNAL   Nat Commun 9 (1), 1641 (2018)
   PUBMED   29691401
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 942)
  AUTHORS   Li,T., Robert,E.I., van Breugel,P.C., Strubin,M. and Zheng,N.
  TITLE     A promiscuous alpha-helical motif anchors viral hijackers and
            substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
  JOURNAL   Nat Struct Mol Biol 17 (1), 105-111 (2010)
   PUBMED   19966799
REFERENCE   6  (residues 1 to 942)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
REFERENCE   7  (residues 1 to 942)
  AUTHORS   Lynch,R.A., Piper,M., Bankier,A., Bhugra,B., Surti,U., Liu,J.,
            Buckler,A., Dear,P.H. and Menon,A.G.
  TITLE     Genomic and functional map of the chromosome 14 t(12;14) breakpoint
            cluster region in uterine leiomyoma
  JOURNAL   Genomics 52 (1), 17-26 (1998)
   PUBMED   9740667
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA058347.1, AB058727.1, BX648006.1, BC136632.1, BC013239.1,
            R41943.1 and AL391262.3.
            
            On Nov 22, 2004 this sequence version replaced XP_031102.4.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.45730.1,
                                           SRR1660803.91249.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000341516.10/
                                                  ENSP00000341351.5
            RefSeq Select criteria             :: based on conservation,
                                                  expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..942
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q24.1"
     Protein         1..942
                     /product="DDB1- and CUL4-associated factor 5 isoform 1"
                     /note="breakpoint cluster region protein, uterine
                     leiomyoma, 2; WD repeat-containing protein 22"
                     /calculated_mol_wt=103833
     Region          <49..362
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          51..91
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          57..98
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          99..139
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          104..139
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          140..180
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          146..187
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          185..225
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          191..228
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          236..323
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          277..317
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          331..370
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          336..360
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          449..478
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          490..509
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            500
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q80T85; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80T85; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            533
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80T85; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          544..655
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            626
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80T85; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            628
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80T85; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            645
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            648
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            651
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          676..824
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     Site            794
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96JK2.2)"
     Region          889..942
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96JK2.2)"
     CDS             1..942
                     /gene="DCAF5"
                     /gene_synonym="BCRG2; BCRP2; D14S1461E; WDR22"
                     /coded_by="NM_003861.3:142..2970"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32106.1"
                     /db_xref="GeneID:8816"
                     /db_xref="HGNC:HGNC:20224"
                     /db_xref="MIM:603812"
ORIGIN      
        1 mkrraglggs mrsvvgflsq rglhgdpllt qdfqrrrlrg crnlykkdll ghfgcvnaie
       61 fsnnggqwlv sggddrrvll whmeqaihsr vkpiqlkgeh hsnifclafn sgntkvfsgg
      121 ndeqvilhdv essetldvfa hedavyglsv spvndnifas ssddgrvliw diresphgep
      181 fclanypsaf hsvmfnpvep rllatanske gvglwdirkp qssllryggn lslqsamsvr
      241 fnsngtqlla lrrrlppvly dihsrlpvfq fdnqgyfnsc tmksccfagd rdqyilsgsd
      301 dfnlymwrip adpeaggigr vvngafmvlk ghrsivnqvr fnphtymics sgvekiikiw
      361 spykqpgctg dldgriedds rclytheeyi slvlnsgsgl shdyanqsvq edprmmaffd
      421 slvrreiegw ssdsdsdlse stilqlhagv sersgytdse ssaslprspp ptvdesadna
      481 fhlgplrvtt tntvastppt ptcedaasrq qrlsalrryq dkrllalsne sdseenvcev
      541 eldtdlfprp rspspedess ssssssssed eeelnerras twqrnamrrr qkttredkps
      601 apikptntyi gednydypqi kvddlssspt ssperststl eiqpsraspt sdiesverki
      661 ykaykwlrys yisysnnkdg etslvtgead egragtshkd npapssskea clniamaqrn
      721 qdlppegcsk dtfkeetprt psngpghehs shawaevpeg tsqdtgnsgs vehpfetkkl
      781 ngkalssrae eppsppvpka sgstlnsgsg ncprtqsdds eersletica nhnngrlhpr
      841 pphphnngqn lgelevvays spghsdtdrd nssltgtllh kdccgsemac etpnagtred
      901 ptdtpatdss ravhghsglk rqrieledtd sensssekkl kt
//
LOCUS       NP_001273499             355 aa            linear   PRI 20-NOV-2025
DEFINITION  junctional adhesion molecule-like isoform 3 [Homo sapiens].
ACCESSION   NP_001273499 XP_005271465
VERSION     NP_001273499.1
DBSOURCE    REFSEQ: accession NM_001286570.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 355)
  AUTHORS   Hao,Z., Xin,Z., Chen,Y., Shao,Z., Lin,W., Wu,W., Lin,M., Liu,Q.,
            Chen,D., Wu,D. and Wu,P.
  TITLE     JAML promotes the antitumor role of tumor-resident CD8+ T cells by
            facilitating their innate-like function in human lung cancer
  JOURNAL   Cancer Lett 590, 216839 (2024)
   PUBMED   38570084
  REMARK    GeneRIF: JAML promotes the antitumor role of tumor-resident CD8[+]
            T cells by facilitating their innate-like function in human lung
            cancer.
REFERENCE   2  (residues 1 to 355)
  AUTHORS   Cheng,S., Li,M., Li,C., Dai,Y., Zhuo,J., Wang,J., Qian,J. and
            Hao,Z.
  TITLE     JAML inhibits colorectal carcinogenesis by modulating the tumor
            immune microenvironment
  JOURNAL   In Vitro Cell Dev Biol Anim 60 (4), 382-396 (2024)
   PUBMED   38625487
  REMARK    GeneRIF: JAML inhibits colorectal carcinogenesis by modulating the
            tumor immune microenvironment.
REFERENCE   3  (residues 1 to 355)
  AUTHORS   Wu,Q., Wang,Y.B., Che,X.W., Wang,H. and Wang,W.
  TITLE     Junctional adhesion molecule-like protein as a novel target for
            kaempferol to ameliorate lung adenocarcinoma
  JOURNAL   J Integr Med 21 (3), 268-276 (2023)
   PUBMED   37069006
  REMARK    GeneRIF: Junctional adhesion molecule-like protein as a novel
            target for kaempferol to ameliorate lung adenocarcinoma.
REFERENCE   4  (residues 1 to 355)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 355)
  AUTHORS   Wu,Q., Li,R., Wang,Q.X., Zhang,M.Y., Liu,T.T. and Qu,Y.Q.
  TITLE     Junctional adhesion molecule-like protein promotes tumor
            progression via the Wnt/beta-catenin signaling pathway in lung
            adenocarcinoma
  JOURNAL   J Transl Med 20 (1), 260 (2022)
   PUBMED   35672776
  REMARK    GeneRIF: Junctional adhesion molecule-like protein promotes tumor
            progression via the Wnt/beta-catenin signaling pathway in lung
            adenocarcinoma.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 355)
  AUTHORS   Ramani,S.R., Tom,I., Lewin-Koh,N., Wranik,B., Depalatis,L.,
            Zhang,J., Eaton,D. and Gonzalez,L.C.
  TITLE     A secreted protein microarray platform for extracellular protein
            interaction discovery
  JOURNAL   Anal Biochem 420 (2), 127-138 (2012)
   PUBMED   21982860
REFERENCE   7  (residues 1 to 355)
  AUTHORS   Guo,Y.L., Bai,R., Chen,C.X., Liu,D.Q., Liu,Y., Zhang,C.Y. and
            Zen,K.
  TITLE     Role of junctional adhesion molecule-like protein in mediating
            monocyte transendothelial migration
  JOURNAL   Arterioscler Thromb Vasc Biol 29 (1), 75-83 (2009)
   PUBMED   18948633
REFERENCE   8  (residues 1 to 355)
  AUTHORS   Luissint,A.C., Lutz,P.G., Calderwood,D.A., Couraud,P.O. and
            Bourdoulous,S.
  TITLE     JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
            in cis by alpha4beta1 integrin activation
  JOURNAL   J Cell Biol 183 (6), 1159-1173 (2008)
   PUBMED   19064666
  REMARK    GeneRIF: Integrin activation is required for the dissociation of
            JAM-L-VLA-4 complexes and the accumulation of functional JAM-L
            dimers, which indicates that the leukocyte integrin VLA-4 controls
            JAM-L function in cis by controlling its dimerization state.
REFERENCE   9  (residues 1 to 355)
  AUTHORS   Zen,K., Liu,Y., McCall,I.C., Wu,T., Lee,W., Babbin,B.A., Nusrat,A.
            and Parkos,C.A.
  TITLE     Neutrophil migration across tight junctions is mediated by adhesive
            interactions between epithelial coxsackie and adenovirus receptor
            and a junctional adhesion molecule-like protein on neutrophils
  JOURNAL   Mol Biol Cell 16 (6), 2694-2703 (2005)
   PUBMED   15800062
REFERENCE   10 (residues 1 to 355)
  AUTHORS   Moog-Lutz,C., Cave-Riant,F., Guibal,F.C., Breau,M.A., Di Gioia,Y.,
            Couraud,P.O., Cayre,Y.E., Bourdoulous,S. and Lutz,P.G.
  TITLE     JAML, a novel protein with characteristics of a junctional adhesion
            molecule, is induced during differentiation of myeloid leukemia
            cells
  JOURNAL   Blood 102 (9), 3371-3378 (2003)
   PUBMED   12869515
  REMARK    GeneRIF: expressed on leukocytes with a possible role in leukocyte
            transmigration
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK298722.1, BC100797.1, AK097285.1 and AP002800.4.
            
            On Nov 8, 2013 this sequence version replaced XP_005271465.1.
            
            Transcript Variant: This variant (3) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream in-frame start codon, compared to variant 1. The encoded
            isoform (3) has a shorter N-terminus than isoform 1. Variants 3 and
            4 encode the same isoform (3).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK298722.1, DRR138524.537060.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q23.3"
     Protein         1..355
                     /product="junctional adhesion molecule-like isoform 3"
                     /note="adhesion molecule AMICA; dendritic-cell specific
                     protein CREA7-1; adhesion molecule, interacts with CXADR
                     antigen 1; dendritic-cell specific protein CREA7-4;
                     adhesion molecule interacting with CXADR antigen 1"
                     /calculated_mol_wt=40005
     Region          3..97
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     Region          99..212
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     CDS             1..355
                     /gene="JAML"
                     /gene_synonym="AMICA; AMICA1; CREA7-1; CREA7-4; Gm638"
                     /coded_by="NM_001286570.2:146..1213"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS66240.1"
                     /db_xref="GeneID:120425"
                     /db_xref="HGNC:HGNC:19084"
                     /db_xref="MIM:609770"
ORIGIN      
        1 mgcvfqsted kcifkidwtl spgehakdey vlyyysnlsv pigrfqnrvh lmgdilcndg
       61 slllqdvqea dqgtyiceir lkgesqvfkk avvlhvlpee pkelmvhvgg liqmgcvfqs
      121 tevkhvtkve wifsgrrake eivfryyhkl rmsveysqsw ghfqnrvnlv gdifrndgsi
      181 mlqgvresdg gnytcsihlg nlvfkktivl hvspeeprtl vtpaalrplv lggnqlviiv
      241 givcatilll pvlilivkkt cgnkssvnst vlvkntkktn peikekpchf ercegekhiy
      301 spiivrevie eeepseksea tymtmhpvwp slrsdrnnsl ekksgggmpk tqqaf
//
LOCUS       NP_115556                660 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM161A isoform 2 [Homo sapiens].
ACCESSION   NP_115556 XP_291019 XP_935352 XP_939624 XP_939626 XP_939628
            XP_939631 XP_939634 XP_939637 XP_947241 XP_950841 XP_950842
            XP_950843 XP_950844 XP_950845 XP_950847 XP_950849
VERSION     NP_115556.2
DBSOURCE    REFSEQ: accession NM_032180.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Arslanhan,M.D., Cengiz-Emek,S., Odabasi,E., Steib,E., Hamel,V.,
            Guichard,P. and Firat-Karalar,E.N.
  TITLE     CCDC15 localizes to the centriole inner scaffold and controls
            centriole length and integrity
  JOURNAL   J Cell Biol 222 (12) (2023)
   PUBMED   37934472
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Liu,Y., Chen,J., Sager,R., Sasaki,E. and Hu,H.
  TITLE     Interactions between C8orf37 and FAM161A, Two Ciliary Proteins
            Essential for Photoreceptor Survival
  JOURNAL   Int J Mol Sci 23 (19), 12033 (2022)
   PUBMED   36233334
  REMARK    GeneRIF: Interactions between C8orf37 and FAM161A, Two Ciliary
            Proteins Essential for Photoreceptor Survival.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Mercey,O., Kostic,C., Bertiaux,E., Giroud,A., Sadian,Y.,
            Gaboriau,D.C.A., Morrison,C.G., Chang,N., Arsenijevic,Y.,
            Guichard,P. and Hamel,V.
  TITLE     The connecting cilium inner scaffold provides a structural
            foundation that protects against retinal degeneration
  JOURNAL   PLoS Biol 20 (6), e3001649 (2022)
   PUBMED   35709082
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Zach,F., Grassmann,F., Langmann,T., Sorusch,N., Wolfrum,U. and
            Stohr,H.
  TITLE     The retinitis pigmentosa 28 protein FAM161A is a novel ciliary
            protein involved in intermolecular protein interaction and
            microtubule association
  JOURNAL   Hum Mol Genet 21 (21), 4573-4586 (2012)
   PUBMED   22791751
  REMARK    GeneRIF: FAM161A is a microtubule-associated ciliary protein
            presumably involved in microtubule stabilization to maintain the
            microtubule tracks and/or in transport processes along microtubules
            in photoreceptors and other retinal cell types.
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Bandah-Rozenfeld,D., Mizrahi-Meissonnier,L., Farhy,C.,
            Obolensky,A., Chowers,I., Pe'er,J., Merin,S., Ben-Yosef,T.,
            Ashery-Padan,R., Banin,E. and Sharon,D.
  TITLE     Homozygosity mapping reveals null mutations in FAM161A as a cause
            of autosomal-recessive retinitis pigmentosa
  JOURNAL   Am J Hum Genet 87 (3), 382-391 (2010)
   PUBMED   20705279
  REMARK    GeneRIF: These data suggest a pivotal role for FAM161A in
            photoreceptors and reveal that FAM161A loss-of-function mutations
            are a major cause of autosomal-recessive Retinitis pigmentosa.
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Langmann,T., Di Gioia,S.A., Rau,I., Stohr,H., Maksimovic,N.S.,
            Corbo,J.C., Renner,A.B., Zrenner,E., Kumaramanickavel,G.,
            Karlstetter,M., Arsenijevic,Y., Weber,B.H., Gal,A. and Rivolta,C.
  TITLE     Nonsense mutations in FAM161A cause RP28-associated recessive
            retinitis pigmentosa
  JOURNAL   Am J Hum Genet 87 (3), 376-381 (2010)
   PUBMED   20705278
  REMARK    GeneRIF: Null mutations in FAM161A are responsible for the
            RP28-associated autosomal-recessive retinitis pigmentosa.
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Gu,S., Kumaramanickavel,G., Srikumari,C.R., Denton,M.J. and Gal,A.
  TITLE     Autosomal recessive retinitis pigmentosa locus RP28 maps between
            D2S1337 and D2S286 on chromosome 2p11-p15 in an Indian family
  JOURNAL   J Med Genet 36 (9), 705-707 (1999)
   PUBMED   10507729
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Fahim,A.T., Daiger,S.P. and Weleber,R.G.
  TITLE     Nonsyndromic Retinitis Pigmentosa Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301590
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC107081.5.
            
            On May 10, 2008 this sequence version replaced NP_115556.1.
            
            Summary: This gene belongs to the FAM161 family. It is expressed
            mainly in the retina. Mouse studies suggested that this gene is
            involved in development of retinal progenitors during
            embryogenesis, and that its activity is restricted to mature
            photoreceptors after birth. Mutations in this gene cause autosomal
            recessive retinitis pigmentosa-28. Alternatively spliced transcript
            variants have been identified.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (2) lacks an in-frame coding exon
            and encodes a shorter isoform (2), as compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX649029.1, SRR1660805.160821.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p15"
     Protein         1..660
                     /product="protein FAM161A isoform 2"
                     /note="retinitis pigmentosa 28 (autosomal recessive);
                     protein FAM161A; family with sequence similarity 161
                     member A; FAM161A, centrosomal protein"
                     /calculated_mol_wt=76621
     Region          234..570
                     /region_name="UPF0564"
                     /note="Uncharacterized protein family UPF0564; pfam10595"
                     /db_xref="CDD:431382"
     Region          341..525
                     /region_name="Required for interaction with CFAP418.
                     /evidence=ECO:0000269|PubMed:36233334"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B820.2)"
     Region          605..660
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B820.2)"
     CDS             1..660
                     /gene="FAM161A"
                     /gene_synonym="RP28"
                     /coded_by="NM_032180.3:20..2002"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS42687.2"
                     /db_xref="GeneID:84140"
                     /db_xref="HGNC:HGNC:25808"
                     /db_xref="MIM:613596"
ORIGIN      
        1 matshrvakl vasslqtpvn pitgarvaqy eredplkala aaeailedee eekvaqpaga
       61 sadlntsfsg vdehapisye dfvnfpdihh sneeyfkkve elkaahietm aklekmyqdk
      121 lhlkevqpvv iredslsdss rsvseknsyh pvslmtsfse pdlgqsssly vssseeelpn
      181 lekeyprknr mmtyakelin nmwtdfcved yirckdtgfh aaekrrkkrk ewvptitvpe
      241 pfqmmireqk kkeesmksks diemvhkalk kqeedpeykk kfranpvpas vflplyhdlv
      301 kqkeerrrsl kekskealla sqkpfkfiar eeqkraarek qlrdflkykk ktnrfkarpi
      361 prstygsttn dklkeeelyr nlrtqlraqe hlqnssplpc rsacgcrnpr cpeqavklkc
      421 khkvrcptpd fedlperyqk hlsehkspkl ltvckpfdlh asphasikre kiladieade
      481 enlketrwpy lsprrkspvr cagvnpvpcn cnppvptvss rgreqavrks ekermreyqr
      541 eleereeklk krpllferva qknarmaaek hysntlkalg isdefvskkg qsgkvleyfn
      601 nqetksvted kesfneeeki eerengeeny fidtnsqdsy kekdeanees eeeksveesh
//
LOCUS       NP_001263194             438 aa            linear   PRI 20-NOV-2025
DEFINITION  dual oxidase maturation factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001263194
VERSION     NP_001263194.1
DBSOURCE    REFSEQ: accession NM_001276265.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 438)
  AUTHORS   Kohda,A., Kamakura,S., Hayase,J. and Sumimoto,H.
  TITLE     The NADPH oxidases DUOX1 and DUOX2 are sorted to the apical plasma
            membrane in epithelial cells via their respective maturation
            factors DUOXA1 and DUOXA2
  JOURNAL   Genes Cells 29 (10), 921-930 (2024)
   PUBMED   39126279
REFERENCE   2  (residues 1 to 438)
  AUTHORS   Wu,J.X., Liu,R., Song,K. and Chen,L.
  TITLE     Structures of human dual oxidase 1 complex in low-calcium and
            high-calcium states
  JOURNAL   Nat Commun 12 (1), 155 (2021)
   PUBMED   33420071
  REMARK    GeneRIF: Structures of human dual oxidase 1 complex in low-calcium
            and high-calcium states.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 438)
  AUTHORS   Meng,Y., Chen,C.W., Yung,M.M.H., Sun,W., Sun,J., Li,Z., Li,J.,
            Li,Z., Zhou,W., Liu,S.S., Cheung,A.N.Y., Ngan,H.Y.S.,
            Braisted,J.C., Kai,Y., Peng,W., Tzatsos,A., Li,Y., Dai,Z.,
            Zheng,W., Chan,D.W. and Zhu,W.
  TITLE     DUOXA1-mediated ROS production promotes cisplatin resistance by
            activating ATR-Chk1 pathway in ovarian cancer
  JOURNAL   Cancer Lett 428, 104-116 (2018)
   PUBMED   29704517
  REMARK    GeneRIF: Study shows that DUOXA1 is overexpressed in
            platinum-resistant ovarian cancer (OC) cells, resulting in over
            production of reactive oxygen species (ROS). Elevated ROS level
            sustains the activation of ATR-Chk1 pathway, leading to resistance
            to cisplatin in OC cells. Clinical studies also confirm the
            activation of ATR and DOUXA1 in OC patients, and elevated DOUXA1 or
            ATR-Chk1 pathway correlates with poor prognosis.
REFERENCE   4  (residues 1 to 438)
  AUTHORS   Ostrakhovitch,E.A. and Semenikhin,O.A.
  TITLE     p53-mediated regulation of neuronal differentiation via regulation
            of dual oxidase maturation factor 1
  JOURNAL   Neurosci Lett 494 (1), 80-85 (2011)
   PUBMED   21362455
REFERENCE   5  (residues 1 to 438)
  AUTHORS   Christophe-Hobertus,C. and Christophe,D.
  TITLE     Delimitation and functional characterization of the bidirectional
            THOX-DUOXA promoter regions in thyrocytes
  JOURNAL   Mol Cell Endocrinol 317 (1-2), 161-167 (2010)
   PUBMED   20060878
REFERENCE   6  (residues 1 to 438)
  AUTHORS   Ostrakhovitch,E.A. and Li,S.S.
  TITLE     NIP1/DUOXA1 expression in epithelial breast cancer cells:
            regulation of cell adhesion and actin dynamics
  JOURNAL   Breast Cancer Res Treat 119 (3), 773-786 (2010)
   PUBMED   19322654
  REMARK    GeneRIF: DUOXA1 transient overexpression affected the cell-cell
            adhesion by modulating the actin cytoskeleton
REFERENCE   7  (residues 1 to 438)
  AUTHORS   Luxen,S., Noack,D., Frausto,M., Davanture,S., Torbett,B.E. and
            Knaus,U.G.
  TITLE     Heterodimerization controls localization of Duox-DuoxA NADPH
            oxidases in airway cells
  JOURNAL   J Cell Sci 122 (Pt 8), 1238-1247 (2009)
   PUBMED   19339556
  REMARK    GeneRIF: Heterodimerization controls localization of Duox-DuoxA
            NADPH oxidases in airway cells.
REFERENCE   8  (residues 1 to 438)
  AUTHORS   Morand,S., Ueyama,T., Tsujibe,S., Saito,N., Korzeniowska,A. and
            Leto,T.L.
  TITLE     Duox maturation factors form cell surface complexes with Duox
            affecting the specificity of reactive oxygen species generation
  JOURNAL   FASEB J 23 (4), 1205-1218 (2009)
   PUBMED   19074510
REFERENCE   9  (residues 1 to 438)
  AUTHORS   Grasberger,H. and Refetoff,S.
  TITLE     Identification of the maturation factor for dual oxidase. Evolution
            of an eukaryotic operon equivalent
  JOURNAL   J Biol Chem 281 (27), 18269-18272 (2006)
   PUBMED   16651268
REFERENCE   10 (residues 1 to 438)
  AUTHORS   Qin,H., Percival-Smith,A., Li,C., Jia,C.Y., Gloor,G. and Li,S.S.
  TITLE     A novel transmembrane protein recruits numb to the plasma membrane
            during asymmetric cell division
  JOURNAL   J Biol Chem 279 (12), 11304-11312 (2004)
   PUBMED   14670962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC029819.1, EU927397.1 and
            CB850544.1.
            
            Summary: Dual oxidases DUOX1 and DUOX2 are NADPH oxidases which are
            involved in hydrogen peroxide production necessary for thyroid
            hormonogenesis. They form a heterodimer with specific maturation
            factors DUOXA1 and DUOXA2, respectively, which is essential for the
            maturation and function of the DUOX enzyme complexes. This gene
            encodes the DUOX1 activator or maturation factor DUOXA1. Rat
            studies identified a bidirectional promoter which controls the
            transcription of the DUOX1 and DUOXA1 genes. This protein is
            cotransported to the cell surface when coexpressed with DUOX1 and
            is retained in the endoplasmic reticulum when expressed without
            DUOX1 protein. The expression of this gene or the DUOX1 gene is not
            suppressed by thyroglobulin (Tg), a macromolecular precursor in
            thyroid hormone synthesis, while the expression of the DUOX2 and
            DUOXA2 are significantly suppressed by the Tg. This protein is also
            a p53-regulated neurogenic factor involved in p53 dependent
            neuronal differentiation. Multiple alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jan 2013].
            
            Transcript Variant: This variant (3) lacks an in-frame coding exon
            compared to variant 1. The resulting isoform (2, also known as
            delta) lacks an internal segment, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: EU927397.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144335
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..438
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..438
                     /product="dual oxidase maturation factor 1 isoform 2"
                     /note="homolog of Drosophila Numb-interacting protein;
                     dual oxidase activator 1; dual oxidase maturation factor 1
                     gamma; dual oxidase maturation factor 1 delta; dual
                     oxidase maturation factor 1 alpha; dual oxidase maturation
                     factor 1 beta"
                     /calculated_mol_wt=48684
     Region          10..242
                     /region_name="DuoxA"
                     /note="Dual oxidase maturation factor; pfam10204"
                     /db_xref="CDD:462995"
     CDS             1..438
                     /gene="DUOXA1"
                     /gene_synonym="mol; NIP; NUMBIP"
                     /coded_by="NM_001276265.1:30..1346"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS61620.1"
                     /db_xref="GeneID:90527"
                     /db_xref="HGNC:HGNC:26507"
                     /db_xref="MIM:612771"
ORIGIN      
        1 matlghtfpf yagpkptfpm dttlasiimi fltalatfiv ilpgirgktr lfwllrvvts
       61 lfigaailgt pvqqlnetin yneeftwrlg enyaeeyaka lekglpdpvl ylaekftprs
      121 pcglyrqyrl aghytsamlw vaflcwllan vmlsmpvlvy ggymllatgi fqllallffs
      181 matsltspcp lhlgasvlht hhgpafwitl ttgllcvllg lamavahrmq phrlkaffnq
      241 svdedpmlew speeggllsp ryrsmadspk sqdiplseas stkayyrprr lslvpadvrg
      301 lapaalsalp gallaqawra llpglrcpka gkesrlgpph spwrfgpegc eerwaehtgd
      361 sprplrgrgt grlwrwgske rracgvraml prlvsnsglk rpscldlpkc wdyrrdaraf
      421 fhlleptpcv tsrhtpli
//
LOCUS       NP_079011                539 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box only protein 31 isoform 1 [Homo sapiens].
ACCESSION   NP_079011
VERSION     NP_079011.3
DBSOURCE    REFSEQ: accession NM_024735.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Zhang,N., Meng,Y., Mao,S., Ni,H., Huang,C., Shen,L., Fu,K., Lv,L.,
            Yu,C., Meekrathok,P., Kuang,C., Chen,F., Zhang,Y. and Yuan,K.
  TITLE     FBXO31-mediated ubiquitination of OGT maintains O-GlcNAcylation
            homeostasis to restrain endometrial malignancy
  JOURNAL   Nat Commun 16 (1), 1274 (2025)
   PUBMED   39894887
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Muhar,M.F., Farnung,J., Cernakova,M., Hofmann,R., Henneberg,L.T.,
            Pfleiderer,M.M., Denoth-Lippuner,A., Kalcic,F., Nievergelt,A.S.,
            Peters Al-Bayati,M., Sidiropoulos,N.D., Beier,V., Mann,M.,
            Jessberger,S., Jinek,M., Schulman,B.A., Bode,J.W. and Corn,J.E.
  TITLE     C-terminal amides mark proteins for degradation via SCF-FBXO31
  JOURNAL   Nature 638 (8050), 519-527 (2025)
   PUBMED   39880951
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Vadhvani,M., Schwedhelm-Domeyer,N., Mukherjee,C. and Stegmuller,J.
  TITLE     The centrosomal E3 ubiquitin ligase FBXO31-SCF regulates neuronal
            morphogenesis and migration
  JOURNAL   PLoS One 8 (2), e57530 (2013)
   PUBMED   23469015
  REMARK    GeneRIF: ascribe a role for FBXO31 in dendrite growth and neuronal
            migration in the developing cerebellar cortex. Taken together, we
            uncovered the centrosomal E3 ligase FBXO31-SCF as a novel regulator
            of neuronal development
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Santra,M.K., Wajapeyee,N. and Green,M.R.
  TITLE     F-box protein FBXO31 mediates cyclin D1 degradation to induce G1
            arrest after DNA damage
  JOURNAL   Nature 459 (7247), 722-725 (2009)
   PUBMED   19412162
  REMARK    GeneRIF: ectopic expression of FBXO31 acts through a
            proteasome-directed pathway to mediate the degradation of cyclin
            D1, an important regulator of progression from G1 to S phase,
            resulting in arrest in G1
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Kumar,R., Neilsen,P.M., Crawford,J., McKirdy,R., Lee,J.,
            Powell,J.A., Saif,Z., Martin,J.M., Lombaerts,M., Cornelisse,C.J.,
            Cleton-Jansen,A.M. and Callen,D.F.
  TITLE     FBXO31 is the chromosome 16q24.3 senescence gene, a candidate
            breast tumor suppressor, and a component of an SCF complex
  JOURNAL   Cancer Res 65 (24), 11304-11313 (2005)
   PUBMED   16357137
  REMARK    GeneRIF: Loss of FBXO31 is associated with breast cancer
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Powell,J.A., Gardner,A.E., Bais,A.J., Hinze,S.J., Baker,E.,
            Whitmore,S., Crawford,J., Kochetkova,M., Spendlove,H.E.,
            Doggett,N.A., Sutherland,G.R., Callen,D.F. and Kremmidiotis,G.
  TITLE     Sequencing, transcript identification, and quantitative gene
            expression profiling in the breast cancer loss of heterozygosity
            region 16q24.3 reveal three potential tumor-suppressor genes
  JOURNAL   Genomics 80 (3), 303-310 (2002)
   PUBMED   12213200
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Wang,C., Deng,L., Hong,M., Akkaraju,G.R., Inoue,J. and Chen,Z.J.
  TITLE     TAK1 is a ubiquitin-dependent kinase of MKK and IKK
  JOURNAL   Nature 412 (6844), 346-351 (2001)
   PUBMED   11460167
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Yang,S.H., Galanis,A. and Sharrocks,A.D.
  TITLE     Targeting of p38 mitogen-activated protein kinases to MEF2
            transcription factors
  JOURNAL   Mol Cell Biol 19 (6), 4028-4038 (1999)
   PUBMED   10330143
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI596608.1, BC012748.1,
            AF318348.1, BM151642.1, BI914636.1, DA493744.1, BX329100.2,
            AL576585.3, BX106211.1 and BE465371.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 3, 2005 this sequence version replaced NP_079011.2.
            
            Summary: This gene is a member of the F-box family. Members are
            classified into three classes according to the substrate
            interaction domain, FBW for WD40 repeats, FBL for leucing-rich
            repeats, and FBXO for other domains. This protein, classified into
            the last category because of the lack of a recognizable substrate
            binding domain, has been proposed to be a component of the SCF
            ubiquitination complex. It is thought to bind and recruit substrate
            for ubiquitination and degradation. This protein may have a role in
            regulating the cell cycle as well as dendrite growth and neuronal
            migration. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Sep 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853563.13165.1,
                                           SRR11853564.11287.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311635.12/ ENSP00000310841.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.2"
     Protein         1..539
                     /product="F-box only protein 31 isoform 1"
                     /note="putative breast cancer tumor-suppressor; F-box only
                     protein 31; SCF ubiquitin ligase specificity factor"
                     /calculated_mol_wt=60533
     Region          11..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Site            33
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3TQF0; Phosphoserine, by
                     PKB/AKT1. /evidence=ECO:0000269|PubMed:29343641;
                     propagated from UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3TQF0; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Region          64..69
                     /region_name="D box.
                     /evidence=ECO:0000269|PubMed:29343641"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Region          76..114
                     /region_name="F-box_SF"
                     /note="F-box domain superfamily; cl45894"
                     /db_xref="CDD:459239"
     Site            order(77..78,81..82,86,88..89,93..95,97)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438852"
     Site            278
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:19412162; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Region          286..512
                     /region_name="Cyclin_D1_bind"
                     /note="Cyclin D1 binding domain; pfam12014"
                     /db_xref="CDD:463431"
     Region          297..299
                     /region_name="DDL motif.
                     /evidence=ECO:0000269|PubMed:31413110"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Region          377..446
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Site            419
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MTOR.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX0.2)"
     Site            480
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:30171069; propagated from
                     UniProtKB/Swiss-Prot (Q5XUX0.2)"
     CDS             1..539
                     /gene="FBXO31"
                     /gene_synonym="FBX14; Fbx31; FBXO14; MRT45; pp2386"
                     /coded_by="NM_024735.5:33..1652"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32501.1"
                     /db_xref="GeneID:79791"
                     /db_xref="HGNC:HGNC:16510"
                     /db_xref="MIM:609102"
ORIGIN      
        1 mavcarlcgv gpsrgcrrrq qrrgpaetaa adsepdtdpe eerieasagv ggglcagpsp
       61 ppprcsllel ppellveifa slpgtdlpsl aqvctkfrri lhtdtiwrrr creeygvcen
      121 lrkleitgvs crdvyakllh ryrhilglwq pdigpyggll nvvvdglfii gwmylpphdp
      181 hvddpmrfkp lfrihlmerk aatvecmygh kgphhghiqi vkkdefstkc nqtdhhrmsg
      241 grqeefrtwl reewgrtled ifhehmqeli lmkfiytsqy dncltyrriy lppsrpddli
      301 kpglfkgtyg shgleivmls fhgrrargtk itgdpnipag qqtveidlrh riqlpdlenq
      361 rnfnelsriv levrervrqe qqeggheage grgrqgpres qpspaqprae apskgpdgtp
      421 gedggepgda vaaaeqpaqc gqgqpfvlpv gvssrnedyp rtcrmcfygt gliaghgfts
      481 pertpgvfil fdedrfgfvw lelksfslys rvqatfrnad apspqafdem lkniqslts
//
LOCUS       NP_001186094             955 aa            linear   PRI 20-NOV-2025
DEFINITION  centrosomal protein of 112 kDa isoform a [Homo sapiens].
ACCESSION   NP_001186094
VERSION     NP_001186094.1
DBSOURCE    REFSEQ: accession NM_001199165.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 955)
  AUTHORS   Zhang,X., Huang,G., Jiang,T., Meng,L., Li,T., Zhang,G., Wu,N.,
            Chen,X., Zhao,B., Li,N., Wu,S., Guo,J., Zheng,R., Ji,Z., Xu,Z.,
            Wang,Z., Deng,D., Tan,Y. and Xu,W.
  TITLE     CEP112 coordinates translational regulation of essential fertility
            genes during spermiogenesis through phase separation in humans and
            mice
  JOURNAL   Nat Commun 15 (1), 8465 (2024)
   PUBMED   39349455
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 955)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 955)
  AUTHORS   Sha,Y., Wang,X., Yuan,J., Zhu,X., Su,Z., Zhang,X., Xu,X. and Wei,X.
  TITLE     Loss-of-function mutations in centrosomal protein 112 is associated
            with human acephalic spermatozoa phenotype
  JOURNAL   Clin Genet 97 (2), 321-328 (2020)
   PUBMED   31654588
  REMARK    GeneRIF: Loss-of-function mutations in centrosomal protein 112 is
            associated with human acephalic spermatozoa phenotype.
REFERENCE   4  (residues 1 to 955)
  AUTHORS   Gopalakrishnan,C., Kamaraj,B. and Purohit,R.
  TITLE     Mutations in microRNA binding sites of CEP genes involved in cancer
  JOURNAL   Cell Biochem Biophys 70 (3), 1933-1942 (2014)
   PUBMED   25115610
REFERENCE   5  (residues 1 to 955)
  AUTHORS   Liu,X., Zheng,Y., Zhang,W., Zhang,X., Lioyd-Jones,D.M.,
            Baccarelli,A.A., Ning,H., Fornage,M., He,K., Liu,K. and Hou,L.
  TITLE     Blood methylomics in response to arsenic exposure in a low-exposed
            US population
  JOURNAL   J Expo Sci Environ Epidemiol 24 (2), 145-149 (2014)
   PUBMED   24368509
REFERENCE   6  (residues 1 to 955)
  AUTHORS   Kumar,A., Rajendran,V., Sethumadhavan,R. and Purohit,R.
  TITLE     CEP proteins: the knights of centrosome dynasty
  JOURNAL   Protoplasma 250 (5), 965-983 (2013)
   PUBMED   23456457
  REMARK    Review article
REFERENCE   7  (residues 1 to 955)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   8  (residues 1 to 955)
  AUTHORS   Smith,K.R., Oliver,P.L., Lumb,M.J., Arancibia-Carcamo,I.L.,
            Revilla-Sanchez,R., Brandon,N.J., Moss,S.J. and Kittler,J.T.
  TITLE     Identification and characterisation of a Maf1/Macoco protein
            complex that interacts with GABAA receptors in neurons
  JOURNAL   Mol Cell Neurosci 44 (4), 330-341 (2010)
   PUBMED   20417281
  REMARK    GeneRIF: We report that Maf1 interacts with a novel coiled-coil
            domain containing protein that we have called Macoco.
REFERENCE   9  (residues 1 to 955)
  AUTHORS   Sombekke,M.H., Arteta,D., van de Wiel,M.A., Crusius,J.B.,
            Tejedor,D., Killestein,J., Martinez,A., Pena,A.S., Polman,C.H. and
            Uitdehaag,B.M.
  TITLE     Analysis of multiple candidate genes in association with phenotypes
            of multiple sclerosis
  JOURNAL   Mult Scler 16 (6), 652-659 (2010)
   PUBMED   20378664
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Erratum:[Mult Scler. 2010 Jun;16(6):765]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006120.1, AC087302.7,
            AC007716.8, AC006440.9, AC105028.4, AC004805.1 and AA723963.1.
            
            Summary: This gene encodes a coiled-coil domain containing protein
            that belongs to the cell division control protein 42 effector
            protein family. In neurons, it localizes to the cytoplasm of
            dendrites and is also enriched in the nucleus where it interacts
            with the RNA polymerase III transcriptional repressor Maf1 to
            regulate gamma-aminobutyric acid A receptor surface expression. In
            addition, the protein has been identified as a component of the
            human centrosome. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Nov 2014].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.129980.1, AK299075.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000535342.7/ ENSP00000442784.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..955
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.1"
     Protein         1..955
                     /product="centrosomal protein of 112 kDa isoform a"
                     /note="centrosomal protein of 112 kDa; coiled-coil
                     domain-containing protein 46; centrosomal protein 112kDa"
                     /calculated_mol_wt=112618
     Region          13..98
                     /region_name="DUF4485"
                     /note="Domain of unknown function (DUF4485); pfam14846"
                     /db_xref="CDD:464345"
     Region          301..>933
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..955
                     /gene="CEP112"
                     /gene_synonym="CCDC46; MACOCO; SPGF44"
                     /coded_by="NM_001199165.4:146..3013"
                     /note="isoform a is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS32710.1"
                     /db_xref="GeneID:201134"
                     /db_xref="HGNC:HGNC:28514"
                     /db_xref="MIM:618980"
ORIGIN      
        1 mevgseeekw ekldaefdhf vvdmkpfvlk lphrterqrc alwirklcep sgtgagimgr
       61 knrnlyakll lhmlkrgale gpfthrpepg tlkilpsyms iyfdepnpar akgsspeglp
      121 awvlgelets ehklneswkl ssgedntlvq sptdvysreq ytgklrvrsh slspthredg
      181 qnitpkicev yskkspvsld dsdiearlns wnlgienpry lrqkpipvsl mtpkfslrks
      241 ssfhddhfls rirekeldmk tkmmeakfhe eklklqqkhd advqkilerk nneieelktl
      301 yrskqhetee tirklekkvq tlirdcqvir etkedqiael kkiceqstes lnndwekklh
      361 navaemeqek fdlqkqhten iqelledtnv rlnkmeseym aqtqstnhmi kelearvqql
      421 tgeaensnlq rqkliqekae lercyqitcs elqevkarrn tlhkekdhlv ndyeqnmkll
      481 qtkydadinl lkqehalsas kassmieele qnvcqlkqql qeselqrkqq lrdqenkfqm
      541 ekshlkhiye kkahdlqsel dkgkedtqkk ihkfeealke keeqltrvte vqrlqaqqad
      601 aaleefkrqv elnsekvyae mkeqmekvea dltrskslre kqskeflwql edirqryeqq
      661 ivelkleheq ekthllqqhn aekdslvrdh ereienlekq lraanmehen qiqefkkrda
      721 qviadmeaqv hklreelinv nsqrkqqlve lgllreeekq ratreheivv nklkaesekm
      781 kielkkthaa etemtlekan sklkqiekey tqklakssqi iaelqttiss lkeensqqql
      841 aaerrlqdvr qkfedekkql irdndqaikv lqdelenrsn qvrcaekklq hkelesqeqi
      901 tyirqeyetk lkglmpaslr qeledtissl ksqvnflqkr asilqeeltt yqgrr
//
LOCUS       NP_001350871             631 aa            linear   PRI 20-NOV-2025
DEFINITION  armadillo repeat-containing protein 8 isoform 7 [Homo sapiens].
ACCESSION   NP_001350871 XP_011510935
VERSION     NP_001350871.1
DBSOURCE    REFSEQ: accession NM_001363942.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 631)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 631)
  AUTHORS   Zhan,T., Chen,M., Liu,W., Han,Z., Zhu,Q., Liu,M., Tan,J., Liu,J.,
            Chen,X., Tian,X. and Huang,X.
  TITLE     MiR-455-3p inhibits gastric cancer progression by repressing
            Wnt/beta-catenin signaling through binding to ARMC8
  JOURNAL   BMC Med Genomics 16 (1), 155 (2023)
   PUBMED   37400847
  REMARK    GeneRIF: MiR-455-3p inhibits gastric cancer progression by
            repressing Wnt/beta-catenin signaling through binding to ARMC8.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 631)
  AUTHORS   Maitland,M.E.R., Lajoie,G.A., Shaw,G.S. and Schild-Poulter,C.
  TITLE     Structural and Functional Insights into GID/CTLH E3 Ligase
            Complexes
  JOURNAL   Int J Mol Sci 23 (11), 5863 (2022)
   PUBMED   35682545
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 631)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 631)
  AUTHORS   Li,X., Zhang,C., Yuan,Y., Wang,Y., Lu,S., Zhou,Z., Zhen,P. and
            Zhou,M.
  TITLE     Downregulation of ARMC8 promotes tumorigenesis through activating
            Wnt/beta-catenin pathway and EMT in cutaneous squamous cell
            carcinomas
  JOURNAL   J Dermatol Sci 102 (3), 184-192 (2021)
   PUBMED   34016486
  REMARK    GeneRIF: Downregulation of ARMC8 promotes tumorigenesis through
            activating Wnt/beta-catenin pathway and EMT in cutaneous squamous
            cell carcinomas.
REFERENCE   6  (residues 1 to 631)
  AUTHORS   Jiang,G., Zhang,Y., Zhang,X., Fan,C., Wang,L., Xu,H., Yu,J. and
            Wang,E.
  TITLE     ARMc8 indicates aggressive colon cancers and promotes invasiveness
            and migration of colon cancer cells
  JOURNAL   Tumour Biol 36 (11), 9005-9013 (2015)
   PUBMED   26081621
  REMARK    GeneRIF: invasiveness and migration capacity of HT29 cells
            transfected with ARMc8 were significantly greater than those of
            control cells (p < 0.001), while ARMc8 siRNA treatment
            significantly reduced cell invasion and migration in LoVo cells
REFERENCE   7  (residues 1 to 631)
  AUTHORS   Jiang,G., Yang,D., Wang,L., Zhang,X., Xu,H., Miao,Y., Wang,E. and
            Zhang,Y.
  TITLE     A novel biomarker ARMc8 promotes the malignant progression of
            ovarian cancer
  JOURNAL   Hum Pathol 46 (10), 1471-1479 (2015)
   PUBMED   26232863
  REMARK    GeneRIF: ARMc8 may enhance the invasion and metastasis of ovarian
            cancer cells
REFERENCE   8  (residues 1 to 631)
  AUTHORS   Fan,C., Zhao,Y., Mao,X., Miao,Y., Lin,X., Jiang,G., Zhang,X.,
            Han,Q., Luan,L. and Wang,E.
  TITLE     Armc8 expression was elevated during atypia-to-carcinoma
            progression and associated with cancer development of breast
            carcinoma
  JOURNAL   Tumour Biol 35 (11), 11337-11343 (2014)
   PUBMED   25119601
  REMARK    GeneRIF: Armc8 expression was elevated during atypia-to-carcinoma
            progression and associated with cancer development of breast
            carcinoma.
REFERENCE   9  (residues 1 to 631)
  AUTHORS   Xie,C., Jiang,G., Fan,C., Zhang,X., Zhang,Y., Miao,Y., Lin,X.,
            Wu,J., Wang,L., Liu,Y., Yu,J., Yang,L., Zhang,D., Xu,K. and Wang,E.
  TITLE     ARMC8alpha promotes proliferation and invasion of non-small cell
            lung cancer cells by activating the canonical Wnt signaling pathway
  JOURNAL   Tumour Biol 35 (9), 8903-8911 (2014)
   PUBMED   24894675
  REMARK    GeneRIF: Data suggest that armadillo repeat containing protein 8
            (ARMC8) might serve as a therapeutic target in non-small cell lung
            cancer (NSCLC).
REFERENCE   10 (residues 1 to 631)
  AUTHORS   Kobayashi,N., Yang,J., Ueda,A., Suzuki,T., Tomaru,K., Takeno,M.,
            Okuda,K. and Ishigatsubo,Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC068777.19 and AC022337.24.
            
            On Jun 3, 2018 this sequence version replaced XP_011510935.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.192207.1,
                                           SRR1660809.95720.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..631
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q22.3"
     Protein         1..631
                     /product="armadillo repeat-containing protein 8 isoform 7"
                     /note="armadillo repeat-containing protein 8; GID complex
                     subunit 5, VID28 homolog"
                     /calculated_mol_wt=70665
     Region          <7..170
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          15..48
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          56..92
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          <332..565
                     /region_name="COG5369"
                     /note="Uncharacterized conserved protein [Function
                     unknown]"
                     /db_xref="CDD:227663"
     Site            order(402,406,410,444,448,452,487,491,495)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          419..455
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          461..496
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          511..541
                     /region_name="HEAT repeat"
                     /note="HEAT repeat [structural motif]"
                     /db_xref="CDD:293787"
     CDS             1..631
                     /gene="ARMC8"
                     /gene_synonym="GID5; HSPC056; S863-2; VID28"
                     /coded_by="NM_001363942.1:434..2329"
                     /note="isoform 7 is encoded by transcript variant 8"
                     /db_xref="CCDS:CCDS87140.1"
                     /db_xref="GeneID:25852"
                     /db_xref="HGNC:HGNC:24999"
                     /db_xref="MIM:618521"
ORIGIN      
        1 mknavignnk qkanlivlga vprllyllqq etsstelkte cavvlgslam gtennvksll
       61 dchiipallq gllspdlkfi eaclrclrti ftspvtpeel lytdatviph lmallsrsry
      121 tqeyicqifs hcckgpdhqt ilfnhgavqn iahlltslsy kvrmqalkcf svlafenpqv
      181 smtlvnvlvd gellpqifvk mlqrdkpiem qltsakclty mcragairtd dncivlktlp
      241 clvrmcsker lleervegae tlayliepdv elqriasitd hliamladyf kypssvsait
      301 dikrldhdlk hahelrqaaf klyaslgand edirkkiiet enmmdrivtg lsessvkvrl
      361 aavrclhsls rsvqqlrtsf qdhavwkplm kvlqnapdei lvvassmlcn lllefspske
      421 pilesgavel lcgltqsenp alrvngiwal mnmafqaeqk ikadilrsls teqlfrllsd
      481 sdlnvlmktl gllrnllstr phidkimsth gkqimqavtl ilegehniev keqtlcilan
      541 iadgttakdl imtnddilqk ikyymghshv klqlaamfci snliwneeeg sqerqdklrd
      601 mgivdilhkl sqspdsnlcd kakmalqqyl a
//
LOCUS       NP_001355932             254 aa            linear   PRI 20-NOV-2025
DEFINITION  aprataxin isoform j [Homo sapiens].
ACCESSION   NP_001355932 XP_024303349
VERSION     NP_001355932.1
DBSOURCE    REFSEQ: accession NM_001369003.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Imamura,R., Saito,M., Shimada,M., Kobayashi,J., Ishiai,M. and
            Matsumoto,Y.
  TITLE     APTX acts in DNA double-strand break repair in a manner distinct
            from XRCC4
  JOURNAL   J Radiat Res 64 (3), 485-495 (2023)
   PUBMED   36940705
  REMARK    GeneRIF: APTX acts in DNA double-strand break repair in a manner
            distinct from XRCC4.
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Hirano,M., Nishiwaki,T., Kariya,S., Furiya,Y., Kawahara,M. and
            Ueno,S.
  TITLE     Novel splice variants increase molecular diversity of aprataxin,
            the gene responsible for early-onset ataxia with ocular motor
            apraxia and hypoalbuminemia
  JOURNAL   Neurosci Lett 366 (2), 120-125 (2004)
   PUBMED   15276230
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Shimazaki,H., Takiyama,Y., Sakoe,K., Ikeguchi,K., Niijima,K.,
            Kaneko,J., Namekawa,M., Ogawa,T., Date,H., Tsuji,S., Nakano,I. and
            Nishizawa,M.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia:
            the aprataxin gene mutations
  JOURNAL   Neurology 59 (4), 590-595 (2002)
   PUBMED   12196655
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Brenner,C.
  TITLE     Hint, Fhit, and GalT: function, structure, evolution, and mechanism
            of three branches of the histidine triad superfamily of nucleotide
            hydrolases and transferases
  JOURNAL   Biochemistry 41 (29), 9003-9014 (2002)
   PUBMED   12119013
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Uchida,E., Gibson,T.,
            Mendonca,P., Costa,M., Barros,J., Yanagisawa,T., Watanabe,M.,
            Ikeda,Y., Aoki,M., Nagata,T., Coutinho,P., Sequeiros,J. and
            Koenig,M.
  TITLE     The gene mutated in ataxia-ocular apraxia 1 encodes the new
            HIT/Zn-finger protein aprataxin
  JOURNAL   Nat Genet 29 (2), 189-193 (2001)
   PUBMED   11586300
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Date,H., Onodera,O., Tanaka,H., Iwabuchi,K., Uekawa,K.,
            Igarashi,S., Koike,R., Hiroi,T., Yuasa,T., Awaya,Y., Sakai,T.,
            Takahashi,T., Nagatomo,H., Sekijima,Y., Kawachi,I., Takiyama,Y.,
            Nishizawa,M., Fukuhara,N., Saito,K., Sugano,S. and Tsuji,S.
  TITLE     Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is
            caused by mutations in a new HIT superfamily gene
  JOURNAL   Nat Genet 29 (2), 184-188 (2001)
   PUBMED   11586299
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Moreira,M.C., Barbot,C., Tachi,N., Kozuka,N., Mendonca,P.,
            Barros,J., Coutinho,P., Sequeiros,J. and Koenig,M.
  TITLE     Homozygosity mapping of Portuguese and Japanese forms of
            ataxia-oculomotor apraxia to 9p13, and evidence for genetic
            heterogeneity
  JOURNAL   Am J Hum Genet 68 (2), 501-508 (2001)
   PUBMED   11170899
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Coutinho,P., Barbot,C. and Coutinho,P.
  TITLE     Ataxia with Oculomotor Apraxia Type 1 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301629
REFERENCE   10 (residues 1 to 254)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL162590.15 and AL353717.13.
            
            On Mar 11, 2019 this sequence version replaced XP_024303349.1.
            
            Summary: This gene encodes a member of the histidine triad (HIT)
            superfamily. The encoded protein may play a role in single-stranded
            DNA repair through its nucleotide-binding activity and its
            diadenosine polyphosphate hydrolase activity. Mutations in this
            gene have been associated with ataxia-ocular apraxia. Alternatively
            spliced transcript variants have been identified for this
            gene.[provided by RefSeq, Aug 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.131150.1,
                                           SRR1803613.137189.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9p21.1"
     Protein         1..254
                     /product="aprataxin isoform j"
                     /EC_number="3.6.1.72"
                     /EC_number="3.6.1.71"
                     /note="forkhead-associated domain histidine triad-like
                     protein"
                     /calculated_mol_wt=28977
     Region          76..177
                     /region_name="aprataxin_related"
                     /note="aprataxin related: Aprataxin, a HINT family
                     hydrolase is mutated in ataxia oculomotor apraxia
                     syndrome. All the members of this subgroup have the
                     conserved HxHxHxx (where x is a hydrophobic residue)
                     signature motif. Members of this subgroup are...; cd01278"
                     /db_xref="CDD:238609"
     Site            order(170,172,174..176)
                     /site_type="active"
                     /note="HIT family signature motif [active]"
                     /db_xref="CDD:238609"
     Site            172
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238609"
     Region          195..254
                     /region_name="zf-C2HE"
                     /note="C2HE / C2H2 / C2HC zinc-binding finger; pfam16278"
                     /db_xref="CDD:465082"
     CDS             1..254
                     /gene="APTX"
                     /gene_synonym="AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT"
                     /coded_by="NM_001369003.1:581..1345"
                     /note="isoform j is encoded by transcript variant 24"
                     /db_xref="CCDS:CCDS47957.1"
                     /db_xref="GeneID:54840"
                     /db_xref="HGNC:HGNC:15984"
                     /db_xref="MIM:606350"
ORIGIN      
        1 mvnelypyiv efeeeaknpg lethrkrkrs gnsdsierda aqeaeagtgl epgsnsgqcs
       61 vplkkgkdap ikkeslghws qglkismqdp kmqvykdeqv vvikdkypka ryhwlvlpwt
      121 sisslkavar ehlellkhmh tvgekvivdf agssklrfrl gyhaipsmsh vhlhvisqdf
      181 dspclknkkh wnsfnteyfl esqaviemvq eagrvtvrdg mpellklplr checqqllps
      241 ipqlkehlrk hwtq
//
LOCUS       NP_001354207             694 aa            linear   PRI 20-NOV-2025
DEFINITION  interleukin-17 receptor C isoform 7 precursor [Homo sapiens].
ACCESSION   NP_001354207 XP_016862833
VERSION     NP_001354207.1
DBSOURCE    REFSEQ: accession NM_001367278.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 694)
  AUTHORS   Arikan,S., Ozturk,O., Duygulu,S., Atalay,E.O. and Atalay,A.
  TITLE     Associations of IL-17 and IL-17 receptor polymorphisms with
            Behcet's disease in Denizli Province of Turkey
  JOURNAL   Immunol Res 71 (4), 600-608 (2023)
   PUBMED   36701075
  REMARK    GeneRIF: Associations of IL-17 and IL-17 receptor polymorphisms
            with Behcet's disease in Denizli Province of Turkey.
REFERENCE   2  (residues 1 to 694)
  AUTHORS   Kang,J.H., Park,S., Rho,J., Hong,E.J., Cho,Y.E., Won,Y.S. and
            Kwon,H.J.
  TITLE     IL-17A promotes Helicobacter pylori-induced gastric carcinogenesis
            via interactions with IL-17RC
  JOURNAL   Gastric Cancer 26 (1), 82-94 (2023)
   PUBMED   36125689
  REMARK    GeneRIF: IL-17A promotes Helicobacter pylori-induced gastric
            carcinogenesis via interactions with IL-17RC.
REFERENCE   3  (residues 1 to 694)
  AUTHORS   Goepfert,A., Barske,C., Lehmann,S., Wirth,E., Willemsen,J.,
            Gudjonsson,J.E., Ward,N.L., Sarkar,M.K., Hemmig,R., Kolbinger,F.
            and Rondeau,J.M.
  TITLE     IL-17-induced dimerization of IL-17RA drives the formation of the
            IL-17 signalosome to potentiate signaling
  JOURNAL   Cell Rep 41 (3), 111489 (2022)
   PUBMED   36260993
REFERENCE   4  (residues 1 to 694)
  AUTHORS   Huang,X., Li,Z., Shen,X., Nie,N. and Shen,Y.
  TITLE     IL-17 upregulates MCP-1 expression via Act1 / TRAF6 / TAK1 in
            experimental autoimmune myocarditis
  JOURNAL   Cytokine 152, 155823 (2022)
   PUBMED   35183823
  REMARK    Erratum:[Cytokine. 2022 Jun;154:155879. doi:
            10.1016/j.cyto.2022.155879. PMID: 35413623]
REFERENCE   5  (residues 1 to 694)
  AUTHORS   Schmidt,T., Luebbe,J., Kilian,C., Riedel,J.H., Hiekmann,S.,
            Asada,N., Ginsberg,P., Robben,L., Song,N., Kaffke,A., Peters,A.,
            Borchers,A., Flavell,R.A., Gagliani,N., Pelzcar,P., Huber,S.,
            Huber,T.B., Turner,J.E., Paust,H.J., Krebs,C.F. and Panzer,U.
  TITLE     IL-17 Receptor C Signaling Controls CD4+ TH17 Immune Responses and
            Tissue Injury in Immune-Mediated Kidney Diseases
  JOURNAL   J Am Soc Nephrol 32 (12), 3081-3098 (2021)
   PUBMED   35167487
  REMARK    GeneRIF: IL-17 Receptor C Signaling Controls CD4(+) TH17 Immune
            Responses and Tissue Injury in Immune-Mediated Kidney Diseases.
REFERENCE   6  (residues 1 to 694)
  AUTHORS   Haudenschild,D.R., Curtiss,S.B., Moseley,T.A. and Reddi,A.H.
  TITLE     Generation of interleukin-17 receptor-like protein (IL-17RL) in
            prostate by alternative splicing of RNA
  JOURNAL   Prostate 66 (12), 1268-1274 (2006)
   PUBMED   16688746
  REMARK    GeneRIF: IL-17RL exists as multiple isoforms due to extensive
            alternative splicing. Changes in RNA IL-17RL splicing occur in
            advanced cancers.
REFERENCE   7  (residues 1 to 694)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   8  (residues 1 to 694)
  AUTHORS   Gerritsen,M.E., Tomlinson,J.E., Zlot,C., Ziman,M. and Hwang,S.
  TITLE     Using gene expression profiling to identify the molecular basis of
            the synergistic actions of hepatocyte growth factor and vascular
            endothelial growth factor in human endothelial cells
  JOURNAL   Br J Pharmacol 140 (4), 595-610 (2003)
   PUBMED   14504135
  REMARK    Review article
REFERENCE   9  (residues 1 to 694)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 694)
  AUTHORS   Haudenschild,D., Moseley,T., Rose,L. and Reddi,A.H.
  TITLE     Soluble and transmembrane isoforms of novel interleukin-17
            receptor-like protein by RNA splicing and expression in prostate
            cancer
  JOURNAL   J Biol Chem 277 (6), 4309-4316 (2002)
   PUBMED   11706037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018809.5.
            
            On Nov 16, 2018 this sequence version replaced XP_016862833.1.
            
            Summary: This gene encodes a single-pass type I membrane protein
            that shares similarity with the interleukin-17 receptor (IL-17RA).
            Unlike IL-17RA, which is predominantly expressed in hemopoietic
            cells, and binds with high affinity to only IL-17A, this protein is
            expressed in nonhemopoietic tissues, and binds both IL-17A and
            IL-17F with similar affinities. The proinflammatory cytokines,
            IL-17A and IL-17F, have been implicated in the progression of
            inflammatory and autoimmune diseases. Multiple alternatively
            spliced transcript variants encoding different isoforms have been
            detected for this gene, and it has been proposed that soluble,
            secreted proteins lacking transmembrane and intracellular domains
            may function as extracellular antagonists to cytokine signaling.
            [provided by RefSeq, Feb 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.83162.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..694
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.3"
     Protein         1..694
                     /product="interleukin-17 receptor C isoform 7 precursor"
                     /note="IL17F receptor; IL-17RL; IL17Rhom; zcytoR14; IL-17
                     receptor C; interleukin-17 receptor homolog;
                     interleukin-17 receptor-like protein"
                     /calculated_mol_wt=73476
     sig_peptide     1..20
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2183
     Region          71..446
                     /region_name="IL17_R_N"
                     /note="Interleukin-17 receptor extracellular region;
                     pfam15037"
                     /db_xref="CDD:464460"
     Region          493..640
                     /region_name="SEFIR"
                     /note="SEFIR domain; pfam08357"
                     /db_xref="CDD:254756"
     CDS             1..694
                     /gene="IL17RC"
                     /gene_synonym="CANDF9; IL17-RL; IL17RL"
                     /coded_by="NM_001367278.1:219..2303"
                     /note="isoform 7 precursor is encoded by transcript
                     variant 8"
                     /db_xref="CCDS:CCDS93201.1"
                     /db_xref="GeneID:84818"
                     /db_xref="HGNC:HGNC:18358"
                     /db_xref="MIM:610925"
ORIGIN      
        1 mpvpwfllsl algrspvvls lerlvgpqda thcspglscr lwdsdilclp gdivpapgpv
       61 lapthlqtel vlrcqketdc dlclrvavhl avhghweepe deekfggaad sgveeprnas
      121 lqaqvvlsfq ayptarcvll evqvpaalvq fgqsvgsvvy dcfeaalgse vriwsytqpr
      181 yekelnhtqq lpdcrglevw nsipscwalp wlnvsadgdn vhlvlnvsee qhfglslywn
      241 qtgpqiitln htdlvpclci qvwplepdsv rtnicpfred prahqnlwqa arlqlltlqs
      301 wlldapcslp aeaalcwrap ggdpcqplvp plswenvtvd kvlefpllkg hpnlcvqvns
      361 seklqlqecl wadslgplkd dvllletrgp qdnrslcale psgctslpsk astraarlge
      421 yllqdlqsgq clqlwdddlg alwacpmdky ihkrwalvwl acllfaaals lilllkkdha
      481 kaaargraal llysaddsgf erlvgalasa lcqlplrvav dlwsrrelsa qgpvawfhaq
      541 rrqtlqeggv vvllfspgav alcsewlqdg vsgpgahgph dafraslscv lpdflqgrap
      601 gsyvgacfdr llhpdavpal frtvpvftlp sqlpdflgal qqpraprsgr lqeraeqvsr
      661 alqpaldsyf hppgtpapgr gvgpgagpga gdgt
//
LOCUS       NP_851849                816 aa            linear   PRI 20-NOV-2025
DEFINITION  neuroligin-4, X-linked precursor [Homo sapiens].
ACCESSION   NP_851849
VERSION     NP_851849.1
DBSOURCE    REFSEQ: accession NM_181332.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 816)
  AUTHORS   Schorghofer,D., Vock,L., Mirea,M.A., Eckel,O., Gschwendtner,A.,
            Neesen,J., Richtig,E., Hengstschlager,M. and Mikula,M.
  TITLE     Late stage melanoma is hallmarked by low NLGN4X expression leading
            to HIF1A accumulation
  JOURNAL   Br J Cancer 131 (3), 468-480 (2024)
   PUBMED   38902533
  REMARK    GeneRIF: Late stage melanoma is hallmarked by low NLGN4X expression
            leading to HIF1A accumulation.
REFERENCE   2  (residues 1 to 816)
  AUTHORS   Benner,O., Cast,T.P., Minamide,L.S., Lenninger,Z., Bamburg,J.R. and
            Chanda,S.
  TITLE     Multiple N-linked glycosylation sites critically modulate the
            synaptic abundance of neuroligin isoforms
  JOURNAL   J Biol Chem 299 (12), 105361 (2023)
   PUBMED   37865312
REFERENCE   3  (residues 1 to 816)
  AUTHORS   Toya,A., Fukada,M., Aoki,E., Matsuki,T., Ueda,M., Eda,S.,
            Hashizume,Y., Iio,A., Masaki,S. and Nakayama,A.
  TITLE     The distribution of neuroligin4, an autism-related postsynaptic
            molecule, in the human brain
  JOURNAL   Mol Brain 16 (1), 20 (2023)
   PUBMED   36747195
  REMARK    GeneRIF: The distribution of neuroligin4, an autism-related
            postsynaptic molecule, in the human brain.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 816)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 816)
  AUTHORS   Roundhill,E.A., Chicon-Bosch,M., Jeys,L., Parry,M., Rankin,K.S.,
            Droop,A. and Burchill,S.A.
  TITLE     RNA sequencing and functional studies of patient-derived cells
            reveal that neurexin-1 and regulators of this pathway are
            associated with poor outcomes in Ewing sarcoma
  JOURNAL   Cell Oncol (Dordr) 44 (5), 1065-1085 (2021)
   PUBMED   34403115
  REMARK    GeneRIF: RNA sequencing and functional studies of patient-derived
            cells reveal that neurexin-1 and regulators of this pathway are
            associated with poor outcomes in Ewing sarcoma.
REFERENCE   6  (residues 1 to 816)
  AUTHORS   Laumonnier,F., Bonnet-Brilhault,F., Gomot,M., Blanc,R., David,A.,
            Moizard,M.P., Raynaud,M., Ronce,N., Lemonnier,E., Calvas,P.,
            Laudier,B., Chelly,J., Fryns,J.P., Ropers,H.H., Hamel,B.C.,
            Andres,C., Barthelemy,C., Moraine,C. and Briault,S.
  TITLE     X-linked mental retardation and autism are associated with a
            mutation in the NLGN4 gene, a member of the neuroligin family
  JOURNAL   Am J Hum Genet 74 (3), 552-557 (2004)
   PUBMED   14963808
REFERENCE   7  (residues 1 to 816)
  AUTHORS   Jamain,S., Quach,H., Betancur,C., Rastam,M., Colineaux,C.,
            Gillberg,I.C., Soderstrom,H., Giros,B., Leboyer,M., Gillberg,C. and
            Bourgeron,T.
  CONSRTM   Paris Autism Research International Sibpair Study
  TITLE     Mutations of the X-linked genes encoding neuroligins NLGN3 and
            NLGN4 are associated with autism
  JOURNAL   Nat Genet 34 (1), 27-29 (2003)
   PUBMED   12669065
  REMARK    GeneRIF: report mutations in two X-linked genes encoding
            neuroligins NLGN3 and NLGN4 in siblings with autism-spectrum
            disorders
REFERENCE   8  (residues 1 to 816)
  AUTHORS   Bolliger,M.F., Frei,K., Winterhalter,K.H. and Gloor,S.M.
  TITLE     Identification of a novel neuroligin in humans which binds to
            PSD-95 and has a widespread expression
  JOURNAL   Biochem J 356 (Pt 2), 581-588 (2001)
   PUBMED   11368788
REFERENCE   9  (residues 1 to 816)
  AUTHORS   Cantallops,I. and Cline,H.T.
  TITLE     Synapse formation: if it looks like a duck and quacks like a duck
            ...
  JOURNAL   Curr Biol 10 (17), R620-R623 (2000)
   PUBMED   10996085
  REMARK    Review article
REFERENCE   10 (residues 1 to 816)
  AUTHORS   Irie,M., Hata,Y., Takeuchi,M., Ichtchenko,K., Toyoda,A., Hirao,K.,
            Takai,Y., Rosahl,T.W. and Sudhof,T.C.
  TITLE     Binding of neuroligins to PSD-95
  JOURNAL   Science 277 (5331), 1511-1515 (1997)
   PUBMED   9278515
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN357526.1, AB033086.1 and
            AC078989.22.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the type-B
            carboxylesterase/lipase protein family. The encoded protein belongs
            to a family of neuronal cell surface proteins. Members of this
            family may act as splice site-specific ligands for beta-neurexins
            and may be involved in the formation and remodeling of central
            nervous system synapses. The encoded protein interacts with discs
            large homolog 4 (DLG4). Mutations in this gene have been associated
            with autism and Asperger syndrome. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (2) differs in the 5' UTR,
            compared to variant 3. Variants 1, 2, 3, and 4 encode the same
            protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.174330.1,
                                           SRR1803611.266722.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2157437 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000381095.8/ ENSP00000370485.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..816
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.32-p22.31"
     Protein         1..816
                     /product="neuroligin-4, X-linked precursor"
                     /calculated_mol_wt=87304
     sig_peptide     1..41
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=4630
     Region          44..590
                     /region_name="COesterase"
                     /note="Carboxylesterase family; pfam00135"
                     /db_xref="CDD:395084"
     Site            order(174..176,253..255,258,399,405..406,444,490,493)
                     /site_type="other"
                     /note="substrate binding pocket [chemical binding]"
                     /db_xref="CDD:238191"
     Site            order(254,375,489)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238191"
     CDS             1..816
                     /gene="NLGN4X"
                     /gene_synonym="ASPGX2; AUTSX2; HLNX; HNL4X; NLGN4"
                     /coded_by="NM_181332.3:633..3083"
                     /db_xref="CCDS:CCDS14126.1"
                     /db_xref="GeneID:57502"
                     /db_xref="HGNC:HGNC:14287"
                     /db_xref="MIM:300427"
ORIGIN      
        1 msrpqgllwl pllftpvcvm lnsnvllwlt alaikftlid sqaqypvvnt nygkirglrt
       61 plpneilgpv eqylgvpyas pptgerrfqp peppsswtgi rnttqfaavc pqhldersll
      121 hdmlpiwfta nldtlmtyvq dqnedclyln iyvpteddih dqnskkpvmv yihggsymeg
      181 tgnmidgsil asygnvivit inyrlgilgf lstgdqaakg nyglldqiqa lrwieenvga
      241 fggdpkrvti fgsgagascv slltlshyse glfqkaiiqs gtalsswavn yqpakytril
      301 adkvgcnmld ttdmveclrn knykeliqqt itpatyhiaf gpvidgdvip ddpqilmeqg
      361 eflnydimlg vnqgeglkfv dgivdnedgv tpndfdfsvs nfvdnlygyp egkdtlreti
      421 kfmytdwadk enpetrrktl valftdhqwv apavatadlh aqygsptyfy afyhhcqsem
      481 kpswadsahg devpyvfgip migptelfsc nfskndvmls avvmtywtnf aktgdpnqpv
      541 pqdtkfihtk pnrfeevaws kynpkdqlyl higlkprvrd hyratkvafw lelvphlhnl
      601 neifqyvstt tkvpppdmts fpygtrrspa kiwpttkrpa itpannpkhs kdphktgped
      661 ttvlietkrd ystelsvtia vgasllflni lafaalyykk dkrrhethrr pspqrnttnd
      721 iahiqneeim slqmkqlehd heceslqahd tlrltcppdy tltlrrspdd iplmtpntit
      781 mipntltgmq plhtfntfsg gqnstnlphg hsttrv
//
LOCUS       NP_001230439             435 aa            linear   PRI 20-NOV-2025
DEFINITION  estrogen-related receptor gamma isoform 2 [Homo sapiens].
ACCESSION   NP_001230439
VERSION     NP_001230439.1
DBSOURCE    REFSEQ: accession NM_001243510.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 435)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 435)
  AUTHORS   Sato,K., Takayama,K.I., Saito,Y. and Inoue,S.
  TITLE     ERRalpha and ERRgamma coordinate expression of genes associated
            with Alzheimer's disease, inhibiting DKK1 to suppress tau
            phosphorylation
  JOURNAL   Proc Natl Acad Sci U S A 121 (37), e2406854121 (2024)
   PUBMED   39231208
  REMARK    GeneRIF: ERRalpha and ERRgamma coordinate expression of genes
            associated with Alzheimer's disease, inhibiting DKK1 to suppress
            tau phosphorylation.
REFERENCE   3  (residues 1 to 435)
  AUTHORS   Adkins-Threats,M., Arimura,S., Huang,Y.Z., Divenko,M., To,S.,
            Mao,H., Zeng,Y., Hwang,J.Y., Burclaff,J.R., Jain,S. and Mills,J.C.
  TITLE     Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells
  JOURNAL   Cell Stem Cell 31 (6), 886-903 (2024)
   PUBMED   38733994
  REMARK    GeneRIF: Metabolic regulator ERRgamma governs gastric stem cell
            differentiation into acid-secreting parietal cells.
REFERENCE   4  (residues 1 to 435)
  AUTHORS   Jung,Y.S., Radhakrishnan,K., Hammad,S., Muller,S., Muller,J.,
            Noh,J.R., Kim,J., Lee,I.K., Cho,S.J., Kim,D.K., Kim,Y.H., Lee,C.H.,
            Dooley,S. and Choi,H.S.
  TITLE     ERRgamma-inducible FGF23 promotes alcoholic liver injury through
            enhancing CYP2E1 mediated hepatic oxidative stress
  JOURNAL   Redox Biol 71, 103107 (2024)
   PUBMED   38479224
  REMARK    GeneRIF: ERRgamma-inducible FGF23 promotes alcoholic liver injury
            through enhancing CYP2E1 mediated hepatic oxidative stress.
REFERENCE   5  (residues 1 to 435)
  AUTHORS   Lee,C.Y., Hubrich,D., Varga,J.K., Schafer,C., Welzel,M.,
            Schumbera,E., Djokic,M., Strom,J.M., Schonfeld,J., Geist,J.L.,
            Polat,F., Gibson,T.J., Keller Valsecchi,C.I., Kumar,M.,
            Schueler-Furman,O. and Luck,K.
  TITLE     Systematic discovery of protein interaction interfaces using
            AlphaFold and experimental validation
  JOURNAL   Mol Syst Biol 20 (2), 75-97 (2024)
   PUBMED   38225382
REFERENCE   6  (residues 1 to 435)
  AUTHORS   Greschik,H., Wurtz,J.M., Sanglier,S., Bourguet,W., van
            Dorsselaer,A., Moras,D. and Renaud,J.P.
  TITLE     Structural and functional evidence for ligand-independent
            transcriptional activation by the estrogen-related receptor 3
  JOURNAL   Mol Cell 9 (2), 303-313 (2002)
   PUBMED   11864604
  REMARK    GeneRIF: Transcriptional activation by ERR3 can be
            ligand-independent.
REFERENCE   7  (residues 1 to 435)
  AUTHORS   Heard,D.J., Norby,P.L., Holloway,J. and Vissing,H.
  TITLE     Human ERRgamma, a third member of the estrogen receptor-related
            receptor (ERR) subfamily of orphan nuclear receptors:
            tissue-specific isoforms are expressed during development and in
            the adult
  JOURNAL   Mol Endocrinol 14 (3), 382-392 (2000)
   PUBMED   10707956
REFERENCE   8  (residues 1 to 435)
  AUTHORS   Hong,H., Yang,L. and Stallcup,M.R.
  TITLE     Hormone-independent transcriptional activation and coactivator
            binding by novel orphan nuclear receptor ERR3
  JOURNAL   J Biol Chem 274 (32), 22618-22626 (1999)
   PUBMED   10428842
REFERENCE   9  (residues 1 to 435)
  AUTHORS   Chen,F., Zhang,Q., McDonald,T., Davidoff,M.J., Bailey,W., Bai,C.,
            Liu,Q. and Caskey,C.T.
  TITLE     Identification of two hERR2-related novel nuclear receptors
            utilizing bioinformatics and inverse PCR
  JOURNAL   Gene 228 (1-2), 101-109 (1999)
   PUBMED   10072763
REFERENCE   10 (residues 1 to 435)
  AUTHORS   Eudy,J.D., Yao,S., Weston,M.D., Ma-Edmonds,M., Talmadge,C.B.,
            Cheng,J.J., Kimberling,W.J. and Sumegi,J.
  TITLE     Isolation of a gene encoding a novel member of the nuclear receptor
            superfamily from the critical region of Usher syndrome type IIa at
            1q41
  JOURNAL   Genomics 50 (3), 382-384 (1998)
   PUBMED   9676434
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX647076.1, AY388457.1,
            DA293919.1, AB020639.1 and BU752915.1.
            
            Summary: This gene encodes a member of the estrogen
            receptor-related receptor (ESRR) family, which belongs to the
            nuclear hormone receptor superfamily. All members of the ESRR
            family share an almost identical DNA binding domain, which is
            composed of two C4-type zinc finger motifs. The ESRR members are
            orphan nuclear receptors; they bind to the estrogen response
            element and steroidogenic factor 1 response element, and activate
            genes controlled by both response elements in the absence of any
            ligands. The ESRR family is closely related to the estrogen
            receptor (ER) family. They share target genes, co-regulators and
            promoters, and by targeting the same set of genes, the ESRRs seem
            to interfere with the ER-mediated estrogen response in various
            ways. It has been reported that the family member encoded by this
            gene functions as a transcriptional activator of DNA
            cytosine-5-methyltransferases 1 (Dnmt1) expression by direct
            binding to its response elements in the DNMT1 promoters, modulates
            cell proliferation and estrogen signaling in breast cancer, and
            negatively regulates bone morphogenetic protein 2-induced
            osteoblast differentiation and bone formation. Multiple
            alternatively spliced transcript variants have been identified,
            which mainly differ at the 5' end and some of which encode protein
            isoforms differing in the N-terminal region. [provided by RefSeq,
            Aug 2011].
            
            Transcript Variant: This variant (10) uses an alternate exon
            structure in the 5' UTR and 5' coding region, compared to variant
            1. This results in a distinct 5' UTR and use of a downstream
            in-frame start codon. The encoded isoform (2) has a shorter
            N-terminus compared to isoform 1. Variants 2-4, 9-15, and 17-21
            encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: CR749497.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..435
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..435
                     /product="estrogen-related receptor gamma isoform 2"
                     /note="estrogen receptor-related protein 3; nuclear
                     receptor subfamily 3 group B member 3; ERR gamma-2"
                     /calculated_mol_wt=48450
     Region          99..195
                     /region_name="NR_DBD_ERR"
                     /note="DNA-binding domain of estrogen related receptors
                     (ERR) is composed of two C4-type zinc fingers; cd07170"
                     /db_xref="CDD:143544"
     Site            order(103,115..118,123..124,126..128,130..131,134,
                     154..155,158,161,175..176,179..186)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143544"
     Site            order(105,108,122,125,141,147,157,160)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143544"
     Region          214..433
                     /region_name="NR_LBD_ERR"
                     /note="The ligand binding domain of estrogen
                     receptor-related nuclear receptors; cd06946"
                     /db_xref="CDD:132744"
     Site            order(242,245,249,252,290,303,307,317..319,412,415,417)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:132744"
     Site            order(257,271,274..275,278..279,425..426,429..430)
                     /site_type="other"
                     /note="coactivator recognition site [polypeptide binding]"
                     /db_xref="CDD:132744"
     Site            353
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:132744"
     CDS             1..435
                     /gene="ESRRG"
                     /gene_synonym="ERR-gamma; ERR3; ERRg; ERRgamma; NR3B3"
                     /coded_by="NM_001243510.3:260..1567"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS1517.1"
                     /db_xref="GeneID:2104"
                     /db_xref="HGNC:HGNC:3474"
                     /db_xref="MIM:602969"
ORIGIN      
        1 msnkdrhids scssfiktep sspasltdsv nhhspggssd asgsysstmn ghqngldspp
       61 lypsapilgg sgpvrklydd csstivedpq tkceymlnsm pkrlclvcgd iasgyhygva
      121 sceackaffk rtiqgnieys cpatneceit krrrkscqac rfmkclkvgm lkegvrldrv
      181 rggrqkykrr idaenspyln pqlvqpakkp ynkivshllv aepekiyamp dptvpdsdik
      241 alttlcdlad relvviigwa khipgfstls ladqmsllqs awmeililgv vyrslsfede
      301 lvyaddyimd edqsklagll dlnnailqlv kkyksmklek eefvtlkaia lansdsmhie
      361 dveavqklqd vlhealqdye agqhmedprr agkmlmtlpl lrqtstkavq hfyniklegk
      421 vpmhklflem leakv
//
LOCUS       NP_001278767             432 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA-binding protein Ikaros isoform 3 [Homo sapiens].
ACCESSION   NP_001278767
VERSION     NP_001278767.1
DBSOURCE    REFSEQ: accession NM_001291838.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 432)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 432)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 432)
  AUTHORS   Song,Y., Zhang,Y., Wang,Z., Lin,Y., Cao,X., Han,X., Li,G., Hou,A.
            and Han,S.
  TITLE     CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway
  JOURNAL   Oncogene 43 (36), 2737-2749 (2024)
   PUBMED   39112517
  REMARK    GeneRIF: CCL2 mediated IKZF1 expression promotes M2 polarization of
            glioma-associated macrophages through CD84-SHP2 pathway.
REFERENCE   4  (residues 1 to 432)
  AUTHORS   Ezzat,S., Yu,S. and Asa,S.L.
  TITLE     Ikaros isoforms in human pituitary tumors: distinct localization,
            histone acetylation, and activation of the 5' fibroblast growth
            factor receptor-4 promoter
  JOURNAL   Am J Pathol 163 (3), 1177-1184 (2003)
   PUBMED   12937159
REFERENCE   5  (residues 1 to 432)
  AUTHORS   Payne,K.J., Nicolas,J.H., Zhu,J.Y., Barsky,L.W. and Crooks,G.M.
  TITLE     Cutting edge: predominant expression of a novel Ikaros isoform in
            normal human hemopoiesis
  JOURNAL   J Immunol 167 (4), 1867-1870 (2001)
   PUBMED   11489963
  REMARK    GeneRIF: A novel Ikaros isoform 'Ikx' is the predominant Ikaros
            protein present in normal cord blood and bone marrow cells, but not
            in leukemia cell lines.
REFERENCE   6  (residues 1 to 432)
  AUTHORS   Nakayama,H., Ishimaru,F., Avitahl,N., Sezaki,N., Fujii,N.,
            Nakase,K., Ninomiya,Y., Harashima,A., Minowada,J., Tsuchiyama,J.,
            Imajoh,K., Tsubota,T., Fukuda,S., Sezaki,T., Kojima,K., Hara,M.,
            Takimoto,H., Yorimitsu,S., Takahashi,I., Miyata,A., Taniguchi,S.,
            Tokunaga,Y., Gondo,H., Niho,Y., Harada,M. et al.
  TITLE     Decreases in Ikaros activity correlate with blast crisis in
            patients with chronic myelogenous leukemia
  JOURNAL   Cancer Res 59 (16), 3931-3934 (1999)
   PUBMED   10463586
REFERENCE   7  (residues 1 to 432)
  AUTHORS   Sun,L., Heerema,N., Crotty,L., Wu,X., Navara,C., Vassilev,A.,
            Sensel,M., Reaman,G.H. and Uckun,F.M.
  TITLE     Expression of dominant-negative and mutant isoforms of the
            antileukemic transcription factor Ikaros in infant acute
            lymphoblastic leukemia
  JOURNAL   Proc Natl Acad Sci U S A 96 (2), 680-685 (1999)
   PUBMED   9892693
REFERENCE   8  (residues 1 to 432)
  AUTHORS   Molnar,A., Wu,P., Largespada,D.A., Vortkamp,A., Scherer,S.,
            Copeland,N.G., Jenkins,N.A., Bruns,G. and Georgopoulos,K.
  TITLE     The Ikaros gene encodes a family of lymphocyte-restricted zinc
            finger DNA binding proteins, highly conserved in human and mouse
  JOURNAL   J Immunol 156 (2), 585-592 (1996)
   PUBMED   8543809
REFERENCE   9  (residues 1 to 432)
  AUTHORS   Hahm,K., Ernst,P., Lo,K., Kim,G.S., Turck,C. and Smale,S.T.
  TITLE     The lymphoid transcription factor LyF-1 is encoded by specific,
            alternatively spliced mRNAs derived from the Ikaros gene
  JOURNAL   Mol Cell Biol 14 (11), 7111-7123 (1994)
   PUBMED   7935426
REFERENCE   10 (residues 1 to 432)
  AUTHORS   Georgopoulos,K., Moore,D.D. and Derfler,B.
  TITLE     Ikaros, an early lymphoid-specific transcription factor and a
            putative mediator for T cell commitment
  JOURNAL   Science 258 (5083), 808-812 (1992)
   PUBMED   1439790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB122945.1, AK303586.1 and
            JX459579.1.
            
            Summary: This gene encodes a transcription factor that belongs to
            the family of zinc-finger DNA-binding proteins associated with
            chromatin remodeling. The expression of this protein is restricted
            to the fetal and adult hemo-lymphopoietic system, and it functions
            as a regulator of lymphocyte differentiation. Several alternatively
            spliced transcript variants encoding different isoforms have been
            described for this gene. Most isoforms share a common C-terminal
            domain, which contains two zinc finger motifs that are required for
            hetero- or homo-dimerization, and for interactions with other
            proteins. The isoforms, however, differ in the number of N-terminal
            zinc finger motifs that bind DNA and in nuclear localization signal
            presence, resulting in members with and without DNA-binding
            properties. Only a few isoforms contain the requisite three or more
            N-terminal zinc motifs that confer high affinity binding to a
            specific core DNA sequence element in the promoters of target
            genes. The non-DNA-binding isoforms are largely found in the
            cytoplasm, and are thought to function as dominant-negative
            factors. Overexpression of some dominant-negative isoforms have
            been associated with B-cell malignancies, such as acute
            lymphoblastic leukemia (ALL). [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (Ik-2) differs in the 5' UTR, and
            lacks an alternate in-frame exon in the 5' coding region, compared
            to variant 1. The encoded isoform (3, also known as Ik-2) is
            shorter than isoform 1, and is localized to the nucleus and
            contains three N-terminal zinc finger motifs for high affinity DNA
            binding (PMID:9892693).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038191.2733846.1,
                                           SRR14038193.4575310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..432
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12.2"
     Protein         1..432
                     /product="DNA-binding protein Ikaros isoform 3"
                     /note="zinc finger protein, subfamily 1A, 1 (Ikaros);
                     DNA-binding protein Ikaros; CLL-associated antigen KW-6;
                     ikaros family zinc finger protein 1; protein phosphatase
                     1, regulatory subunit 92; lymphoid transcription factor
                     LyF-1"
                     /calculated_mol_wt=48158
     Region          <1..>131
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          60..80
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(65,67,69,71..72,75..76,79,93,95,99..100,103..104,
                     107,121,123,125,127..128,131..132,136)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          88..108
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          116..137
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..432
                     /gene="IKZF1"
                     /gene_synonym="CVID13; Hs.54452; IK1; IKAROS; LyF-1; LYF1;
                     PPP1R92; PRO0758; ZNFN1A1"
                     /coded_by="NM_001291838.2:222..1520"
                     /note="isoform 3 is encoded by transcript variant Ik-2"
                     /db_xref="CCDS:CCDS78233.1"
                     /db_xref="GeneID:10320"
                     /db_xref="HGNC:HGNC:13176"
                     /db_xref="MIM:603023"
ORIGIN      
        1 mdadegqdms qvsgkesppv sdtpdegdep mpipedlstt sggqqssksd rvvgerpfqc
       61 nqcgasftqk gnllrhiklh sgekpfkchl cnyacrrrda ltghlrthsv gkphkcgycg
      121 rsykqrssle ehkerchnyl esmglpgtly pvikeetnhs emaedlckig serslvldrl
      181 asnvakrkss mpqkflgdkg lsdtpydssa syekenemmk shvmdqainn ainylgaesl
      241 rplvqtppgg sevvpvispm yqlhkplaeg tprsnhsaqd savenlllls kaklvpsere
      301 aspsnscqds tdtesnneeq rsgliyltnh iapharngls lkeehraydl lraasensqd
      361 alrvvstsge qmkvykcehc rvlfldhvmy tihmgchgfr dpfecnmcgy hsqdryefss
      421 hitrgehrfh ms
//
LOCUS       NP_001265120             158 aa            linear   PRI 20-NOV-2025
DEFINITION  tropomyosin alpha-3 chain isoform 9 [Homo sapiens].
ACCESSION   NP_001265120
VERSION     NP_001265120.1
DBSOURCE    REFSEQ: accession NM_001278191.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Geeves,M.A., Hitchcock-DeGregori,S.E. and Gunning,P.W.
  TITLE     A systematic nomenclature for mammalian tropomyosin isoforms
  JOURNAL   J Muscle Res Cell Motil 36 (2), 147-153 (2015)
   PUBMED   25369766
  REMARK    Review article
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Takeuchi,K., Soda,M., Togashi,Y., Suzuki,R., Sakata,S., Hatano,S.,
            Asaka,R., Hamanaka,W., Ninomiya,H., Uehara,H., Lim Choi,Y.,
            Satoh,Y., Okumura,S., Nakagawa,K., Mano,H. and Ishikawa,Y.
  TITLE     RET, ROS1 and ALK fusions in lung cancer
  JOURNAL   Nat Med 18 (3), 378-381 (2012)
   PUBMED   22327623
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Gunning,P.W., Schevzov,G., Kee,A.J. and Hardeman,E.C.
  TITLE     Tropomyosin isoforms: divining rods for actin cytoskeleton function
  JOURNAL   Trends Cell Biol 15 (6), 333-341 (2005)
   PUBMED   15953552
  REMARK    Review article
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Lin,J.L., Geng,X., Bhattacharya,S.D., Yu,J.R., Reiter,R.S.,
            Sastri,B., Glazier,K.D., Mirza,Z.K., Wang,K.K., Amenta,P.S.,
            Das,K.M. and Lin,J.J.
  TITLE     Isolation and sequencing of a novel tropomyosin isoform
            preferentially associated with colon cancer
  JOURNAL   Gastroenterology 123 (1), 152-162 (2002)
   PUBMED   12105844
  REMARK    GeneRIF: cloned and sequenced a novel nonmuscle tropomyosin (hTM)
            isoform, TC22, which is strongly associated with colonic neoplasia
            and carcinoma
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Lamant,L., Dastugue,N., Pulford,K., Delsol,G. and Mariame,B.
  TITLE     A new fusion gene TPM3-ALK in anaplastic large cell lymphoma
            created by a (1;2)(q25;p23) translocation
  JOURNAL   Blood 93 (9), 3088-3095 (1999)
   PUBMED   10216106
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Laing,N.G., Wilton,S.D., Akkari,P.A., Dorosz,S., Boundy,K.,
            Kneebone,C., Blumbergs,P., White,S., Watkins,H., Love,D.R. et al.
  TITLE     A mutation in the alpha tropomyosin gene TPM3 associated with
            autosomal dominant nemaline myopathy
  JOURNAL   Nat Genet 9 (1), 75-79 (1995)
   PUBMED   7704029
  REMARK    Erratum:[Nat Genet. 1995 Jun;10(2):249. doi: 10.1038/ng0695-249.
            PMID: 7663526]
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Wilton,S.D., Eyre,H., Akkari,P.A., Watkins,H.C., MacRae,C.,
            Laing,N.G. and Callen,D.C.
  TITLE     Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by
            fluorescence in situ hybridisation
  JOURNAL   Cytogenet Cell Genet 68 (1-2), 122-124 (1995)
   PUBMED   7956350
REFERENCE   8  (residues 1 to 158)
  AUTHORS   North,K.N. and Ryan,M.M.
  TITLE     Nemaline Myopathy - RETIRED CHAPTER, FOR HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301465
REFERENCE   9  (residues 1 to 158)
  AUTHORS   DeChene,E.T., Kang,P.B. and Beggs,A.H.
  TITLE     Congenital Fiber-Type Disproportion - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301436
REFERENCE   10 (residues 1 to 158)
  AUTHORS   Clayton,L., Reinach,F.C., Chumbley,G.M. and MacLeod,A.R.
  TITLE     Organization of the hTMnm gene. Implications for the evolution of
            muscle and non-muscle tropomyosins
  JOURNAL   J Mol Biol 201 (3), 507-515 (1988)
   PUBMED   3418707
REFERENCE   11 (residues 1 to 158)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C. and Talbot,K.
  TITLE     The mRNA and RNA-copy pseudogenes encoding TM30nm, a human
            cytoskeletal tropomyosin
  JOURNAL   Nucleic Acids Res 14 (21), 8413-8426 (1986)
   PUBMED   3024106
REFERENCE   12 (residues 1 to 158)
  AUTHORS   Martin-Zanca,D., Hughes,S.H. and Barbacid,M.
  TITLE     A human oncogene formed by the fusion of truncated tropomyosin and
            protein tyrosine kinase sequences
  JOURNAL   Nature 319 (6056), 743-748 (1986)
   PUBMED   2869410
REFERENCE   13 (residues 1 to 158)
  AUTHORS   MacLeod,A.R., Houlker,C., Reinach,F.C., Smillie,L.B., Talbot,K.,
            Modi,G. and Walsh,F.S.
  TITLE     A muscle-type tropomyosin in human fibroblasts: evidence for
            expression by an alternative RNA splicing mechanism
  JOURNAL   Proc Natl Acad Sci U S A 82 (23), 7835-7839 (1985)
   PUBMED   3865200
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA209890.1, BF967161.1,
            BC000771.2, AL590431.11 and AA863064.1.
            
            Summary: This gene encodes a member of the tropomyosin family of
            actin-binding proteins. Tropomyosins are dimers of coiled-coil
            proteins that provide stability to actin filaments and regulate
            access of other actin-binding proteins. Mutations in this gene
            result in autosomal dominant nemaline myopathy and other muscle
            disorders. This locus is involved in translocations with other
            loci, including anaplastic lymphoma receptor tyrosine kinase (ALK)
            and neurotrophic tyrosine kinase receptor type 1 (NTRK1), which
            result in the formation of fusion proteins that act as oncogenes.
            There are numerous pseudogenes for this gene on different
            chromosomes. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, May 2013].
            
            Transcript Variant: This variant (9) differs in the 5' UTR and
            contains multiple differences in the coding region, compared to
            variant Tpm3.1. It initiates translation at a downstream in-frame
            start codon. The encoded isoform (9) is shorter than isoform
            Tpm3.1cy.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.273860.1,
                                           SRR1660805.53929.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.3"
     Protein         1..158
                     /product="tropomyosin alpha-3 chain isoform 9"
                     /note="heat-stable cytoskeletal protein 30 kDa;
                     cytoskeletal tropomyosin TM30; tropomyosin alpha-3 chain;
                     tropomyosin gamma; tropomyosin-5; alpha-tropomyosin, slow
                     skeletal; epididymis secretory sperm binding protein Li
                     82p; epididymis luminal protein 189; tropomyosin 3 nu"
                     /calculated_mol_wt=18472
     Region          <1..156
                     /region_name="Tropomyosin"
                     /note="pfam00261"
                     /db_xref="CDD:459736"
     CDS             1..158
                     /gene="TPM3"
                     /gene_synonym="CAPM1; CFTD; CMYO4A; CMYO4B; CMYP4A;
                     CMYP4B; HEL-189; HEL-S-82p; hscp30; NEM1; OK/SW-cl.5;
                     TM-5; TM3; TM30; TM30nm; TM5; TPM3nu; TPMsk3; TRK"
                     /coded_by="NM_001278191.2:230..706"
                     /note="isoform 9 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS60274.1"
                     /db_xref="GeneID:7170"
                     /db_xref="HGNC:HGNC:12012"
                     /db_xref="MIM:191030"
ORIGIN      
        1 mkvienralk deekmelqei qlkeakhiae eadrkyeeva rklviiegdl erteeraela
       61 eskcseleee lknvtnnlks leaqaekysq kedkyeeeik iltdklkeae traefaersv
      121 aklektiddl edklkctkee hlctqrmldq tlldlnem
//
LOCUS       NP_001350437             513 aa            linear   PRI 20-NOV-2025
DEFINITION  C-terminal-binding protein 2 isoform 3 [Homo sapiens].
ACCESSION   NP_001350437 XP_011537651
VERSION     NP_001350437.1
DBSOURCE    REFSEQ: accession NM_001363508.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 513)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 513)
  AUTHORS   Pastoors,D., Havermans,M., Mulet-Lazaro,R., Brian,D., Noort,W.,
            Grasel,J., Hoogenboezem,R., Smeenk,L., Demmers,J.A.A., Milsom,M.D.,
            Enver,T., Groen,R.W.J., Bindels,E. and Delwel,R.
  TITLE     Oncogene EVI1 drives acute myeloid leukemia via a targetable
            interaction with CTBP2
  JOURNAL   Sci Adv 10 (20), eadk9076 (2024)
   PUBMED   38748792
  REMARK    GeneRIF: Oncogene EVI1 drives acute myeloid leukemia via a
            targetable interaction with CTBP2.
REFERENCE   3  (residues 1 to 513)
  AUTHORS   Cheung,C.H.Y., Cheng,C.K., Leung,K.T., Zhang,C., Ho,C.Y., Luo,X.,
            Kam,A.Y.F., Xia,T., Wan,T.S.K., Pitts,H.A., Chan,N.P.H.,
            Cheung,J.S., Wong,R.S.M., Zhang,X.B. and Ng,M.H.L.
  TITLE     C-terminal binding protein 2 is a novel tumor suppressor targeting
            the MYC-IRF4 axis in multiple myeloma
  JOURNAL   Blood Adv 8 (9), 2217-2234 (2024)
   PUBMED   38457926
  REMARK    GeneRIF: C-terminal binding protein 2 is a novel tumor suppressor
            targeting the MYC-IRF4 axis in multiple myeloma.
REFERENCE   4  (residues 1 to 513)
  AUTHORS   Li,K., Chen,J., Zhang,C., Cheng,M., Chen,S., Song,W., Yang,C.,
            Ling,R., Chen,Z., Wang,X., Xiong,G., Ma,J., Zhu,Y., Yuan,Q.,
            Liu,Q., Peng,L., Chen,Q. and Chen,D.
  TITLE     The CTBP2-PCIF1 complex regulates m6Am modification of mRNA in head
            and neck squamous cell carcinoma
  JOURNAL   J Clin Invest 133 (20), e170173 (2023)
   PUBMED   37643007
  REMARK    GeneRIF: The CTBP2-PCIF1 complex regulates m6Am modification of
            mRNA in head and neck squamous cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 513)
  AUTHORS   Sekiya,M., Ma,Y., Kainoh,K., Saito,K., Yamazaki,D., Tsuyuzaki,T.,
            Chen,W., Adi Putri,P.I.P., Ohno,H., Miyamoto,T., Takeuchi,Y.,
            Murayama,Y., Sugano,Y., Osaki,Y., Iwasaki,H., Yahagi,N., Suzuki,H.,
            Motomura,K., Matsuzaka,T., Murata,K., Mizuno,S., Takahashi,S. and
            Shimano,H.
  TITLE     Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function
  JOURNAL   Cell Rep 42 (8), 112914 (2023)
   PUBMED   37557182
  REMARK    GeneRIF: Loss of CtBP2 may be a mechanistic link between metabolic
            derangements and progressive impairment of pancreatic beta cell
            function.
REFERENCE   6  (residues 1 to 513)
  AUTHORS   Holmes,M., Turner,J., Fox,A., Chisholm,O., Crossley,M. and Chong,B.
  TITLE     hFOG-2, a novel zinc finger protein, binds the co-repressor mCtBP2
            and modulates GATA-mediated activation
  JOURNAL   J Biol Chem 274 (33), 23491-23498 (1999)
   PUBMED   10438528
REFERENCE   7  (residues 1 to 513)
  AUTHORS   Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and
            Otte,A.P.
  TITLE     C-Terminal binding protein is a transcriptional repressor that
            interacts with a specific class of vertebrate Polycomb proteins
  JOURNAL   Mol Cell Biol 19 (1), 777-787 (1999)
   PUBMED   9858600
REFERENCE   8  (residues 1 to 513)
  AUTHORS   Turner,J. and Crossley,M.
  TITLE     Cloning and characterization of mCtBP2, a co-repressor that
            associates with basic Kruppel-like factor and other mammalian
            transcriptional regulators
  JOURNAL   EMBO J 17 (17), 5129-5140 (1998)
   PUBMED   9724649
REFERENCE   9  (residues 1 to 513)
  AUTHORS   Katsanis,N. and Fisher,E.M.
  TITLE     A novel C-terminal binding protein (CTBP2) is closely related to
            CTBP1, an adenovirus E1A-binding protein, and maps to human
            chromosome 21q21.3
  JOURNAL   Genomics 47 (2), 294-299 (1998)
   PUBMED   9479502
REFERENCE   10 (residues 1 to 513)
  AUTHORS   Schaeper,U., Boyd,J.M., Verma,S., Uhlmann,E., Subramanian,T. and
            Chinnadurai,G.
  TITLE     Molecular cloning and characterization of a cellular phosphoprotein
            that interacts with a conserved C-terminal domain of adenovirus E1A
            involved in negative modulation of oncogenic transformation
  JOURNAL   Proc Natl Acad Sci U S A 92 (23), 10467-10471 (1995)
   PUBMED   7479821
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL731571.3.
            
            On May 24, 2018 this sequence version replaced XP_011537651.1.
            
            Summary: This gene produces alternative transcripts encoding two
            distinct proteins. One protein is a transcriptional repressor,
            while the other isoform is a major component of specialized
            synapses known as synaptic ribbons. Both proteins contain a NAD+
            binding domain similar to NAD+-dependent 2-hydroxyacid
            dehydrogenases. A portion of the 3' untranslated region was used to
            map this gene to chromosome 21q21.3; however, it was noted that
            similar loci elsewhere in the genome are likely. Blast analysis
            shows that this gene is present on chromosome 10. Several
            transcript variants encoding two different isoforms have been found
            for this gene. [provided by RefSeq, Feb 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037900.2, SRR1803615.97554.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..513
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..513
                     /product="C-terminal-binding protein 2 isoform 3"
                     /note="ribeye"
                     /calculated_mol_wt=55971
     Region          102..420
                     /region_name="CtBP_dh"
                     /note="C-terminal binding protein (CtBP),
                     D-isomer-specific 2-hydroxyacid dehydrogenases related
                     repressor; cd05299"
                     /db_xref="CDD:240624"
     Site            order(171,174..175,340,389,392)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:240624"
     Site            order(174,202,254..255,257..259,277..281,310..312,314,317,
                     338..340,364..365,389,391..392)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:240624"
     CDS             1..513
                     /gene="CTBP2"
                     /coded_by="NM_001363508.2:211..1752"
                     /note="isoform 3 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS86154.1"
                     /db_xref="GeneID:1488"
                     /db_xref="HGNC:HGNC:2495"
                     /db_xref="MIM:602619"
ORIGIN      
        1 mrpglpgptg lcaqtssrgq ksvlkqkesc giwqlyhfls rkqeprwepc vsgsssgdga
       61 vadladelrg ypalcctlpv hsyrswagir pqimngplhp rplvalldgr dctvempilk
      121 dlatvafcda qstqeihekv lneavgammy htitltredl ekfkalrviv rigsgydnvd
      181 ikaagelgia vcnipsaave etadstichi lnlyrrntwl yqalregtrv qsveqireva
      241 sgaarirget lgligfgrtg qavavrakaf gfsvifydpy lqdgierslg vqrvytlqdl
      301 lyqsdcvslh cnlnehnhhl indftikqmr qgaflvnaar gglvdekala qalkegrirg
      361 aaldvhesep fsfaqgplkd apnlictpht awyseqasle mreaaateir raitgripes
      421 lrncvnkeff vtsapwsvid qqaihpelng atyryppgiv gvapgglpaa megiipggip
      481 vthnlptvah psqapspnqp tkhgdnrehp neq
//
LOCUS       NP_001354562             785 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform a [Homo sapiens].
ACCESSION   NP_001354562
VERSION     NP_001354562.1
DBSOURCE    REFSEQ: accession NM_001367633.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 785)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 785)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 785)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 785)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 785)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 785)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 785)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 785)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 785)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 785)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (73), as well as variants 1 and
            72, encodes isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.10628.1,
                                           SRR1660803.123117.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..785
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..785
                     /product="SUN domain-containing protein 1 isoform a"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=86979
     Region          62..291
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <365..>589
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          417..470
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(417,420..421,424,427..428,431..432,434..435,
                     438..439,441..442,445..446,448..449,452,455..456,459,
                     462..463,466..467,469..470)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          547..605
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          648..783
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..785
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367633.1:52..2409"
                     /note="isoform a is encoded by transcript variant 73"
                     /db_xref="CCDS:CCDS47525.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng dvgaaaatah
      181 ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri gavgqavsrt
      241 awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic kflvlliplf
      301 lllaglslrg qgnffsflpv lnwasmhrtq rvddpqdvfk pttsrlkqpl qgdseafpwh
      361 wmsgveqqva slsgqchhhg enlrelttll qklqarvdqm eggaagpsas vrdavgqppr
      421 etdfmafhqe hevrmshled ilgklrekse aiqkeleqtk qktisavgeq llptvehlql
      481 eldqlksels swrhvktgce tvdavqervd vqvremvkll fsedqqggsl eqllqrfssq
      541 fvskgdlqtm lrdlqlqilr nvthhvsvtk qlptseavvs avseagasgi teaqaraivn
      601 salklysqdk tgmvdfales gggsilstrc setyetktal mslfgiplwy fsqsprvviq
      661 pdiypgncwa fkgsqgylvv rlsmmihpaa ftlehipktl sptgnissap kdfavyglen
      721 eyqeegqllg qftydqdges lqmfqalkrp ddtafqivel rifsnwghpe ytclyrfrvh
      781 gepvk
//
LOCUS       NP_001129513             296 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 11 isoform 2 [Homo sapiens].
ACCESSION   NP_001129513
VERSION     NP_001129513.1
DBSOURCE    REFSEQ: accession NM_001136041.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 296)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 296)
  AUTHORS   Shi,J.Q., Liu,X.F. and Wang,C.
  TITLE     [Progress on the involvement of HDAC11 in the regulation of
            mammalian oocyte maturation and early embryonic development]
  JOURNAL   Sheng Li Xue Bao 76 (3), 438-446 (2024)
   PUBMED   38939938
  REMARK    GeneRIF: [Progress on the involvement of HDAC11 in the regulation
            of mammalian oocyte maturation and early embryonic development].
            Review article
REFERENCE   3  (residues 1 to 296)
  AUTHORS   Byeon,H.E., Choi,S.E., Kim,Y., Choi,S., Lee,S.J., Kim,D.H., Mo,J.S.
            and Jeon,J.Y.
  TITLE     HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome Activation by
            Inducing YAP Expression in THP-1 Cells and PBMCs
  JOURNAL   Endocrinology 165 (3) (2024)
   PUBMED   38366363
  REMARK    GeneRIF: HDAC11 Regulates Palmitate-induced NLRP3 Inflammasome
            Activation by Inducing YAP Expression in THP-1 Cells and PBMCs.
REFERENCE   4  (residues 1 to 296)
  AUTHORS   Liu,Y., Tong,X., Hu,W. and Chen,D.
  TITLE     HDAC11: A novel target for improved cancer therapy
  JOURNAL   Biomed Pharmacother 166, 115418 (2023)
   PUBMED   37659201
  REMARK    GeneRIF: HDAC11: A novel target for improved cancer therapy.
            Review article
REFERENCE   5  (residues 1 to 296)
  AUTHORS   Wu,H., Yin,X., Zhao,X., Wu,Z., Xiao,Y., Di,Q., Sun,P., Tang,H.,
            Quan,J. and Chen,W.
  TITLE     HDAC11 negatively regulates antifungal immunity by inhibiting Nos2
            expression via binding with transcriptional repressor STAT3
  JOURNAL   Redox Biol 56, 102461 (2022)
   PUBMED   36087429
  REMARK    GeneRIF: HDAC11 negatively regulates antifungal immunity by
            inhibiting Nos2 expression via binding with transcriptional
            repressor STAT3.
REFERENCE   6  (residues 1 to 296)
  AUTHORS   Feng,W., Lu,Z., Luo,R.Z., Zhang,X., Seto,E., Liao,W.S. and Yu,Y.
  TITLE     Multiple histone deacetylases repress tumor suppressor gene ARHI in
            breast cancer
  JOURNAL   Int J Cancer 120 (8), 1664-1668 (2007)
   PUBMED   17230502
REFERENCE   7  (residues 1 to 296)
  AUTHORS   Lindberg,D., Akerstrom,G. and Westin,G.
  TITLE     Mutational analyses of WNT7A and HDAC11 as candidate tumour
            suppressor genes in sporadic malignant pancreatic endocrine tumours
  JOURNAL   Clin Endocrinol (Oxf) 66 (1), 110-114 (2007)
   PUBMED   17201809
  REMARK    GeneRIF: the absence of tumour-specific somatic events in WNT7A and
            HDAC11 suggests that these genes are unlikely to have a classical
            tumour suppressor gene role in sporadic malignant pancreatic
            endocrine tumours
REFERENCE   8  (residues 1 to 296)
  AUTHORS   Voelter-Mahlknecht,S., Ho,A.D. and Mahlknecht,U.
  TITLE     Chromosomal organization and localization of the novel class IV
            human histone deacetylase 11 gene
  JOURNAL   Int J Mol Med 16 (4), 589-598 (2005)
   PUBMED   16142391
  REMARK    GeneRIF: Fluorescence in situ hybridization analysis localized
            HDAC11 gene to chromosome 3p25, a region characterized by frequent
            gains and losses of chromosomal material in a number of various
            types of cancer.
REFERENCE   9  (residues 1 to 296)
  AUTHORS   Bradbury,C.A., Khanim,F.L., Hayden,R., Bunce,C.M., White,D.A.,
            Drayson,M.T., Craddock,C. and Turner,B.M.
  TITLE     Histone deacetylases in acute myeloid leukaemia show a distinctive
            pattern of expression that changes selectively in response to
            deacetylase inhibitors
  JOURNAL   Leukemia 19 (10), 1751-1759 (2005)
   PUBMED   16121216
REFERENCE   10 (residues 1 to 296)
  AUTHORS   Gao,L., Cueto,M.A., Asselbergs,F. and Atadja,P.
  TITLE     Cloning and functional characterization of HDAC11, a novel member
            of the human histone deacetylase family
  JOURNAL   J Biol Chem 277 (28), 25748-25755 (2002)
   PUBMED   11948178
  REMARK    GeneRIF: cloning and functional characterization
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC027124.5, BG708402.1,
            AK293223.1 and AW291816.1.
            
            Summary: This gene encodes a class IV histone deacetylase. The
            encoded protein is localized to the nucleus and may be involved in
            regulating the expression of interleukin 10. Alternative splicing
            results in multiple transcript variants.[provided by RefSeq, Apr
            2009].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and
            coding region, and initiates translation at an alternate start
            codon, compared to variant 1. The encoded isoform (2) has a
            distinct N-terminus and is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK293223.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2147975, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..296
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..296
                     /product="histone deacetylase 11 isoform 2"
                     /EC_number="3.5.1.98"
                     /calculated_mol_wt=32993
     Region          7..268
                     /region_name="HDAC_classIV"
                     /note="Histone deacetylase class IV also known as histone
                     deacetylase 11; cd09993"
                     /db_xref="CDD:212519"
     Site            order(13,89..92,100..102,130,132,206,210,250..251,253)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:212519"
     CDS             1..296
                     /gene="HDAC11"
                     /gene_synonym="HD11"
                     /coded_by="NM_001136041.3:224..1114"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS46760.1"
                     /db_xref="GeneID:79885"
                     /db_xref="HGNC:HGNC:19086"
                     /db_xref="MIM:607226"
ORIGIN      
        1 mgleklhpfd agkwgkvinf lkeekllsds mlvearease edllvvhtrr ylnelkrkvl
       61 rplrtqtggt imagklaver gwainvgggf hhcssdrggg fcayaditla ikflferveg
      121 isratiidld ahqgngherd fmddkrvyim dvynrhiypg drfakqairr kvelewgted
      181 deyldkvern ikkslqehlp dvvvynagtd ilegdrlggl sispagivkr delvfrmvrg
      241 rrvpilmvts ggyqkrtari iadsilnlfg lgligpesps vsaqnsdtpl lppavp
//
LOCUS       NP_001350477             406 aa            linear   PRI 20-NOV-2025
DEFINITION  sialic acid-binding Ig-like lectin 8 isoform 2 precursor [Homo
            sapiens].
ACCESSION   NP_001350477 XP_011525037
VERSION     NP_001350477.1
DBSOURCE    REFSEQ: accession NM_001363548.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Li,T.A., Gonzalez-Gil,A., Awol,A.K., Ackerman,S.J., Orsburn,B.C.
            and Schnaar,R.L.
  TITLE     Sialylated keratan sulfates on MUC5B are Siglec-8 ligands in the
            human esophagus
  JOURNAL   Glycobiology 34 (10) (2024)
   PUBMED   39173029
  REMARK    GeneRIF: Sialylated keratan sulfates on MUC5B are Siglec-8 ligands
            in the human esophagus.
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Lee,H.S., Gonzalez-Gil,A., Drake,V., Li,T.A., Schnaar,R.L. and
            Kim,J.
  TITLE     Induction of the endogenous sialoglycan ligand for eosinophil death
            receptor Siglec-8 in chronic rhinosinusitis with hyperplastic nasal
            polyposis
  JOURNAL   Glycobiology 31 (8), 1026-1036 (2021)
   PUBMED   33755113
  REMARK    GeneRIF: Induction of the endogenous sialoglycan ligand for
            eosinophil death receptor Siglec-8 in chronic rhinosinusitis with
            hyperplastic nasal polyposis.
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Trebo,A., Ditsch,N., Degenhardt,T., Kuhn,C., Rahmeh,M.,
            Schmoeckel,E., Mayr,D., Czogalla,B., Kolben,T., Meister,S.,
            Mahner,S., Jeschke,U. and Hester,A.
  TITLE     First Evidence for a Role of Siglec-8 in Breast Cancer
  JOURNAL   Int J Mol Sci 22 (4), 2000 (2021)
   PUBMED   33670444
  REMARK    GeneRIF: First Evidence for a Role of Siglec-8 in Breast Cancer.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 406)
  AUTHORS   Wojtowicz,W.M., Vielmetter,J., Fernandes,R.A., Siepe,D.H.,
            Eastman,C.L., Chisholm,G.B., Cox,S., Klock,H., Anderson,P.W.,
            Rue,S.M., Miller,J.J., Glaser,S.M., Bragstad,M.L., Vance,J.,
            Lam,A.W., Lesley,S.A., Zinn,K. and Garcia,K.C.
  TITLE     A Human IgSF Cell-Surface Interactome Reveals a Complex Network of
            Protein-Protein Interactions
  JOURNAL   Cell 182 (4), 1027-1043 (2020)
   PUBMED   32822567
REFERENCE   5  (residues 1 to 406)
  AUTHORS   Sajay-Asbaghi,M., Sadeghi-Shabestrai,M., Monfaredan,A.,
            Seyfizadeh,N., Razavi,A. and Kazemi,T.
  TITLE     Promoter region single nucleotide polymorphism of siglec-8 gene
            associates with susceptibility to allergic asthma
  JOURNAL   Per Med 17 (3), 195-201 (2020)
   PUBMED   32077788
  REMARK    GeneRIF: Promoter region single nucleotide polymorphism of siglec-8
            gene associates with susceptibility to allergic asthma.
REFERENCE   6  (residues 1 to 406)
  AUTHORS   Nutku,E., Aizawa,H., Hudson,S.A. and Bochner,B.S.
  TITLE     Ligation of Siglec-8: a selective mechanism for induction of human
            eosinophil apoptosis
  JOURNAL   Blood 101 (12), 5014-5020 (2003)
   PUBMED   12609831
  REMARK    GeneRIF: Sialic acid binding immunoglobulin-like lectin 8
            (Siglec-8) cross-linking with antibodies rapidly generated
            caspase-3-like activity and reduced eosinophil viability through
            induction of apoptosis
REFERENCE   7  (residues 1 to 406)
  AUTHORS   Munday,J., Kerr,S., Ni,J., Cornish,A.L., Zhang,J.Q., Nicoll,G.,
            Floyd,H., Mattei,M.G., Moore,P., Liu,D. and Crocker,P.R.
  TITLE     Identification, characterization and leucocyte expression of
            Siglec-10, a novel human sialic acid-binding receptor
  JOURNAL   Biochem J 355 (Pt 2), 489-497 (2001)
   PUBMED   11284738
REFERENCE   8  (residues 1 to 406)
  AUTHORS   Foussias,G., Yousef,G.M. and Diamandis,E.P.
  TITLE     Molecular characterization of a Siglec8 variant containing
            cytoplasmic tyrosine-based motifs, and mapping of the Siglec8 gene
  JOURNAL   Biochem Biophys Res Commun 278 (3), 775-781 (2000)
   PUBMED   11095983
REFERENCE   9  (residues 1 to 406)
  AUTHORS   Kikly,K.K., Bochner,B.S., Freeman,S.D., Tan,K.B., Gallagher,K.T.,
            D'alessio,K.J., Holmes,S.D., Abrahamson,J.A., Erickson-Miller,C.L.,
            Murdock,P.R., Tachimoto,H., Schleimer,R.P. and White,J.R.
  TITLE     Identification of SAF-2, a novel siglec expressed on eosinophils,
            mast cells, and basophils
  JOURNAL   J Allergy Clin Immunol 105 (6 Pt 1), 1093-1100 (2000)
   PUBMED   10856141
REFERENCE   10 (residues 1 to 406)
  AUTHORS   Floyd,H., Ni,J., Cornish,A.L., Zeng,Z., Liu,D., Carter,K.C.,
            Steel,J. and Crocker,P.R.
  TITLE     Siglec-8. A novel eosinophil-specific member of the immunoglobulin
            superfamily
  JOURNAL   J Biol Chem 275 (2), 861-866 (2000)
   PUBMED   10625619
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA388103.1, BC053319.1, BP309940.1 and AF195092.1.
            
            On May 24, 2018 this sequence version replaced XP_011525037.1.
            
            Summary: Sialic acid-binding immunoglobulin (Ig)-like lectins, or
            SIGLECs (e.g., CD33 (MIM 159590)), are a family of type 1
            transmembrane proteins each having a unique expression pattern,
            mostly in hemopoietic cells. SIGLEC8 is a member of the CD33-like
            subgroup of SIGLECs, which are localized to 19q13.3-q13.4 and have
            2 conserved cytoplasmic tyrosine-based motifs: an immunoreceptor
            tyrosine-based inhibitory motif, or ITIM (see MIM 604964), and a
            motif homologous to one identified in signaling lymphocyte
            activation molecule (SLAM; MIM 603492) that mediates an association
            with SLAM-associated protein (SAP; MIM 300490) (summarized by
            Foussias et al., 2000 [PubMed 11095983]).[supplied by OMIM, May
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.592987.1,
                                           SRR1803613.128924.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..406
                     /product="sialic acid-binding Ig-like lectin 8 isoform 2
                     precursor"
                     /note="SAF-2; CDw329; sialoadhesin family member 2"
                     /calculated_mol_wt=42584
     sig_peptide     1..16
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1794
     Region          27..151
                     /region_name="IgV_CD33"
                     /note="Immunoglobulin Variable (IgV) domain at the
                     N-terminus of CD33 and related Siglecs (sialic
                     acid-binding Ig-like lectins); cd05712"
                     /db_xref="CDD:409377"
     Region          27..51
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          27..31
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409377"
     Region          34..38
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409377"
     Region          40..51
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409377"
     Region          52..61
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          62..69
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409377"
     Region          70..93
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409377"
     Region          80..83
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409377"
     Region          94..127
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          95..99
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409377"
     Region          105..113
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409377"
     Region          120..128
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409377"
     Site            order(125,133..134)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409377"
     Region          128..131
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409377"
     Region          132..151
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409377"
     Region          175..253
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          186..190
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          199..203
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Region          221..225
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          232..237
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          247..250
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..406
                     /gene="SIGLEC8"
                     /gene_synonym="SAF2; SIGLEC-8; SIGLEC8L"
                     /coded_by="NM_001363548.1:68..1288"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS86797.1"
                     /db_xref="GeneID:27181"
                     /db_xref="HGNC:HGNC:10877"
                     /db_xref="MIM:605639"
ORIGIN      
        1 mlllllllpl lwgtkgmegd rqygdgyllq vqelvtvqeg lcvhvpcsfs ypqdgwtdsd
       61 pvhgywfrag drpyqdapva tnnpdrevqa etqgrfqllg diwsndcsls irdarkrdkg
      121 syffrlergs mkwsyksqln yktkqlsvfv tdppwnltmt vfqgdatast algngsslsv
      181 legqslrlvc avnsnpparl swtrgsltlc psrssnpgll elprvhvrde geftcraqna
      241 qgsqhislsl slqnegtgts rpvsqvtlaa vggagatala flsfciifii vrscrkksar
      301 paagvgdtgm edakairgsa sqgplteswk dgnplkkppp avapssgeeg elhyatlsfh
      361 kvkpqdpqgq eatdseysei kihkretaet qaclrnhnps skevrg
//
LOCUS       NP_036294                539 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 6 isoform 1 [Homo sapiens].
ACCESSION   NP_036294
VERSION     NP_036294.2
DBSOURCE    REFSEQ: accession NM_012162.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 539)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 539)
  AUTHORS   Lavie,J., Lalou,C., Mahfouf,W., Dupuy,J.W., Lacaule,A.,
            Cywinska,A.A., Lacombe,D., Duchene,A.M., Raymond,A.A.,
            Rezvani,H.R., Ngondo,R.P. and Benard,G.
  TITLE     The E3 ubiquitin ligase FBXL6 controls the quality of newly
            synthesized mitochondrial ribosomal proteins
  JOURNAL   Cell Rep 42 (6), 112579 (2023)
   PUBMED   37267103
  REMARK    GeneRIF: The E3 ubiquitin ligase FBXL6 controls the quality of
            newly synthesized mitochondrial ribosomal proteins.
REFERENCE   3  (residues 1 to 539)
  AUTHORS   Feng,G., Sun,H. and Piao,M.
  TITLE     FBXL6 is dysregulated in keloids and promotes keloid fibroblast
            growth by inducing c-Myc expression
  JOURNAL   Int Wound J 20 (1), 131-139 (2023)
   PUBMED   35606330
  REMARK    GeneRIF: FBXL6 is dysregulated in keloids and promotes keloid
            fibroblast growth by inducing c-Myc expression.
REFERENCE   4  (residues 1 to 539)
  AUTHORS   Li,Y., Cui,K., Zhang,Q., Li,X., Lin,X., Tang,Y., Prochownik,E.V.
            and Li,Y.
  TITLE     FBXL6 degrades phosphorylated p53 to promote tumor growth
  JOURNAL   Cell Death Differ 28 (7), 2112-2125 (2021)
   PUBMED   33568778
  REMARK    GeneRIF: FBXL6 degrades phosphorylated p53 to promote tumor growth.
REFERENCE   5  (residues 1 to 539)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 539)
  AUTHORS   Lievens,S., Vanderroost,N., Van der Heyden,J., Gesellchen,V.,
            Vidal,M. and Tavernier,J.
  TITLE     Array MAPPIT: high-throughput interactome analysis in mammalian
            cells
  JOURNAL   J Proteome Res 8 (2), 877-886 (2009)
   PUBMED   19159283
REFERENCE   7  (residues 1 to 539)
  AUTHORS   Roukens,M.G., Alloul-Ramdhani,M., Moghadasi,S., Op den Brouw,M. and
            Baker,D.A.
  TITLE     Downregulation of vertebrate Tel (ETV6) and Drosophila Yan is
            facilitated by an evolutionarily conserved mechanism of
            F-box-mediated ubiquitination
  JOURNAL   Mol Cell Biol 28 (13), 4394-4406 (2008)
   PUBMED   18426905
  REMARK    GeneRIF: Fbl6 regulates Tel/Yan protein stability and allows
            appropriate spatiotemporal control of gene expression by these
            repressors.
REFERENCE   8  (residues 1 to 539)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   9  (residues 1 to 539)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
REFERENCE   10 (residues 1 to 539)
  AUTHORS   Cenciarelli,C., Chiaur,D.S., Guardavaccaro,D., Parks,W., Vidal,M.
            and Pagano,M.
  TITLE     Identification of a family of human F-box proteins
  JOURNAL   Curr Biol 9 (20), 1177-1179 (1999)
   PUBMED   10531035
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM761056.1, BC033066.1 and
            AC233992.5.
            
            On Jul 19, 2013 this sequence version replaced NP_036294.1.
            
            Summary: This gene encodes a member of a family of proteins that
            are characterized by an F-box motif. The encoded protein also
            contains leucine-rich repeats. F-box-containing proteins comprise
            one of the subunits of the SCF (SKP1-cullin-F-box) complex, which
            functions in phosphorylation-dependent ubiquitination. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jul 2013].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC033066.1, SRR1163658.178162.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000331890.6/ ENSP00000330098.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..539
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..539
                     /product="F-box/LRR-repeat protein 6 isoform 1"
                     /note="F-box protein Fbl6; F-box/LRR-repeat protein 6"
                     /calculated_mol_wt=58427
     Region          1..27
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          49..111
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          112..158
                     /region_name="F-box_FBXL6"
                     /note="F-box domain found in F-box/LRR-repeat protein 6
                     (FBXL6) and similar proteins; cd22119"
                     /db_xref="CDD:438891"
     Site            order(115,119,122..123,126..127,136,138..139,143..145,147)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438891"
     Region          177..203
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          185..398
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          196..221
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          204..229
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          222..247
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          230..255
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          248..299
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          281..307
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          300..329
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          312..337
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          330..357
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          341..365
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          <357..508
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          358..385
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          368..393
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          386..409
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          394..419
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          423..449
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          442..474
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          453..481
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     Region          475..499
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          482..507
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N531.2)"
     CDS             1..539
                     /gene="FBXL6"
                     /gene_synonym="FBL6; FBL6A; PP14630"
                     /coded_by="NM_012162.4:26..1645"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS6422.1"
                     /db_xref="GeneID:26233"
                     /db_xref="HGNC:HGNC:13603"
                     /db_xref="MIM:609076"
ORIGIN      
        1 maapasrqvr rraraaprpr saedwwwdrl aprgsgyhll qsdsmllvls epgparpraq
       61 rrasrrtprq pprgpsaaak pkaglrseaa aapapapapt ptpeegpdag wgdripleil
      121 vqifgllvaa dgpmpflgra arvcrrwqea asqpalwhtv tlssplvgrp akggvkaekk
      181 llaslewlmp nrfsqlqrlt lihwksqvhp vlklvgeccp rltflklsgc hgvtadalvm
      241 lakaccqlhs ldlqhsmves tavvsfleea gsrmrklwlt yssqttailg allgsccpql
      301 qvlevstgin rnsiplqlpv ealqkgcpql qvlrllnlmw lpkppgrgva pgpgfpslee
      361 lclasstcnf vsnevlgrll hgspnlrlld lrgcaritpa glqdlpcrel eqlhlglygt
      421 sdrltlakeg spfltqkwch tlreldlsgq gfsekdleqa laaflstpgg shpalcslnl
      481 rgtrvtpstv ssvisgcpgl lylnlescrc lprglkrayr gleevqwcle qlltspsps
//
LOCUS       NP_001182068             764 aa            linear   PRI 20-NOV-2025
DEFINITION  conserved oligomeric Golgi complex subunit 4 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001182068
VERSION     NP_001182068.2
DBSOURCE    REFSEQ: accession NM_001195139.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Ferreira,C.R., Niiler,T., Duker,A.L., Jackson,A.P. and Bober,M.B.
  TITLE     Growth in individuals with Saul-Wilson syndrome
  JOURNAL   Am J Med Genet A 182 (9), 2110-2116 (2020)
   PUBMED   32652690
  REMARK    GeneRIF: Growth in individuals with Saul-Wilson syndrome.
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Hillman,R.T., Green,R.E. and Brenner,S.E.
  TITLE     An unappreciated role for RNA surveillance
  JOURNAL   Genome Biol 5 (2), R8 (2004)
   PUBMED   14759258
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Loh,E. and Hong,W.
  TITLE     Sec34 is implicated in traffic from the endoplasmic reticulum to
            the Golgi and exists in a complex with GTC-90 and ldlBp
  JOURNAL   J Biol Chem 277 (24), 21955-21961 (2002)
   PUBMED   11929878
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Ungar,D., Oka,T., Brittle,E.E., Vasile,E., Lupashin,V.V.,
            Chatterton,J.E., Heuser,J.E., Krieger,M. and Waters,M.G.
  TITLE     Characterization of a mammalian Golgi-localized protein complex,
            COG, that is required for normal Golgi morphology and function
  JOURNAL   J Cell Biol 157 (3), 405-415 (2002)
   PUBMED   11980916
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Whyte,J.R. and Munro,S.
  TITLE     The Sec34/35 Golgi transport complex is related to the exocyst,
            defining a family of complexes involved in multiple steps of
            membrane traffic
  JOURNAL   Dev Cell 1 (4), 527-537 (2001)
   PUBMED   11703943
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Ferreira,C.
  TITLE     Saul-Wilson Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32078278
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Sparks,S.E. and Krasnewich,D.M.
  TITLE     Congenital Disorders of N-Linked Glycosylation and Multiple Pathway
            Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301507
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK096557.1, BP282697.1,
            AU125729.1, AL050101.1 and AC106804.4.
            
            On Jan 26, 2019 this sequence version replaced NP_001182068.1.
            
            Summary: The protein encoded by this gene is a component of an
            oligomeric protein complex involved in the structure and function
            of the Golgi apparatus. Defects in this gene may be a cause of
            congenital disorder of glycosylation type IIj. Two transcript
            variants encoding different isoforms have been found for this
            gene.[provided by RefSeq, Aug 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.20250.1,
                                           SRR1803612.259815.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: upstream AUG and CDS extension
                                                is not conserved
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..764
                     /product="conserved oligomeric Golgi complex subunit 4
                     isoform 2"
                     /note="complexed with Dor1p; conserved oligomeric Golgi
                     complex protein 4; COG complex subunit 4"
                     /calculated_mol_wt=86636
     Region          188..497
                     /region_name="COG4"
                     /note="COG4 transport protein; pfam08318"
                     /db_xref="CDD:462425"
     CDS             1..764
                     /gene="COG4"
                     /gene_synonym="CDG2J; COD1; SWILS"
                     /coded_by="NM_001195139.2:24..2318"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS73909.2"
                     /db_xref="GeneID:25839"
                     /db_xref="HGNC:HGNC:18620"
                     /db_xref="MIM:606976"
ORIGIN      
        1 madldsppkl sgvqqpsegv gggrcseisa elirsltelq eleavyerlc geekvverel
       61 dalleqqnti eskmvtlhrm gpnlqliegd akqlagmitf tcnlaenvss kvrqldlakn
      121 rlyqaiqrad dildlkfcmd gvqtalrsed yeqaaahthr ylcldksvie lsrqgkegsm
      181 idanlkllqe aeqrlkaiva ekfaiatkeg dlpqverffk ifpllglhee glrkfseylc
      241 kqvaskaeen llmvlgtdms drraavifad tltllfegia rivethqpiv etyygpgrly
      301 tlikylqvec drqvekvvdk fikqrdyhqq frhvqnnlmr nsttekiepr eldpiltevt
      361 lmnarselyl rflkkrissd fevgdsmase evkqehqkcl dkllnnclls ctmqeligly
      421 vtmeeyfmre tvnkavaldt yekgqltssm vddvfyivkk cigralssss idclcaminl
      481 attelesdfr dvlcnklrmg fpattfqdiq rgvtsavnim hsslqqgkfd tkgiestdea
      541 kmsflsdctk lfsqgiggeq aqakfdscls dlaavsnkfr dllqegltel nstaikpqvq
      601 pwinsffsvs hnieeeefnd yeandpwvqq filnleqqma efkaslspvi ydsltglmts
      661 lvavelekvv lkstfnrlgg lqfdkelrsl iaylttvttw tirdkfarls qmatilnler
      721 vteildywgp nsgpltwrlt paevrqvlal ridfrsedik rlrl
//
LOCUS       NP_001836               1669 aa            linear   PRI 20-NOV-2025
DEFINITION  collagen alpha-1(IV) chain isoform 1 preproprotein [Homo sapiens].
ACCESSION   NP_001836
VERSION     NP_001836.3
DBSOURCE    REFSEQ: accession NM_001845.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1669)
  AUTHORS   Kuo,D.S., Labelle-Dumais,C. and Gould,D.B.
  TITLE     COL4A1 and COL4A2 mutations and disease: insights into pathogenic
            mechanisms and potential therapeutic targets
  JOURNAL   Hum Mol Genet 21 (R1), R97-R110 (2012)
   PUBMED   22914737
  REMARK    Review article
REFERENCE   2  (residues 1 to 1669)
  AUTHORS   Plaisier,E. and Ronco,P.
  TITLE     COL4A1-Related Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301768
REFERENCE   3  (residues 1 to 1669)
  AUTHORS   Soininen,R., Huotari,M., Ganguly,A., Prockop,D.J. and Tryggvason,K.
  TITLE     Structural organization of the gene for the alpha 1 chain of human
            type IV collagen
  JOURNAL   J Biol Chem 264 (23), 13565-13571 (1989)
   PUBMED   2701944
REFERENCE   4  (residues 1 to 1669)
  AUTHORS   Soininen,R., Huotari,M., Hostikka,S.L., Prockop,D.J. and
            Tryggvason,K.
  TITLE     The structural genes for alpha 1 and alpha 2 chains of human type
            IV collagen are divergently encoded on opposite DNA strands and
            have an overlapping promoter region
  JOURNAL   J Biol Chem 263 (33), 17217-17220 (1988)
   PUBMED   3182844
REFERENCE   5  (residues 1 to 1669)
  AUTHORS   Poschl,E., Pollner,R. and Kuhn,K.
  TITLE     The genes for the alpha 1(IV) and alpha 2(IV) chains of human
            basement membrane collagen type IV are arranged head-to-head and
            separated by a bidirectional promoter of unique structure
  JOURNAL   EMBO J 7 (9), 2687-2695 (1988)
   PUBMED   2846280
REFERENCE   6  (residues 1 to 1669)
  AUTHORS   Soininen,R., Haka-Risku,T., Prockop,D.J. and Tryggvason,K.
  TITLE     Complete primary structure of the alpha 1-chain of human basement
            membrane (type IV) collagen
  JOURNAL   FEBS Lett 225 (1-2), 188-194 (1987)
   PUBMED   3691802
REFERENCE   7  (residues 1 to 1669)
  AUTHORS   Brazel,D., Oberbaumer,I., Dieringer,H., Babel,W., Glanville,R.W.,
            Deutzmann,R. and Kuhn,K.
  TITLE     Completion of the amino acid sequence of the alpha 1 chain of human
            basement membrane collagen (type IV) reveals 21 non-triplet
            interruptions located within the collagenous domain
  JOURNAL   Eur J Biochem 168 (3), 529-536 (1987)
   PUBMED   3311751
REFERENCE   8  (residues 1 to 1669)
  AUTHORS   Glanville,R.W., Qian,R.Q., Siebold,B., Risteli,J. and Kuhn,K.
  TITLE     Amino acid sequence of the N-terminal aggregation and cross-linking
            region (7S domain) of the alpha 1 (IV) chain of human basement
            membrane collagen
  JOURNAL   Eur J Biochem 152 (1), 213-219 (1985)
   PUBMED   4043082
REFERENCE   9  (residues 1 to 1669)
  AUTHORS   Pihlajaniemi,T., Tryggvason,K., Myers,J.C., Kurkinen,M., Lebo,R.,
            Cheung,M.C., Prockop,D.J. and Boyd,C.D.
  TITLE     cDNA clones coding for the pro-alpha1(IV) chain of human type IV
            procollagen reveal an unusual homology of amino acid sequences in
            two halves of the carboxyl-terminal domain
  JOURNAL   J Biol Chem 260 (12), 7681-7687 (1985)
   PUBMED   2581969
REFERENCE   10 (residues 1 to 1669)
  AUTHORS   Brinker,J.M., Gudas,L.J., Loidl,H.R., Wang,S.Y., Rosenbloom,J.,
            Kefalides,N.A. and Myers,J.C.
  TITLE     Restricted homology between human alpha 1 type IV and other
            procollagen chains
  JOURNAL   Proc Natl Acad Sci U S A 82 (11), 3649-3653 (1985)
   PUBMED   2582422
REFERENCE   11 (residues 1 to 1669)
  AUTHORS   Babel,W. and Glanville,R.W.
  TITLE     Structure of human-basement-membrane (type IV) collagen. Complete
            amino-acid sequence of a 914-residue-long pepsin fragment from the
            alpha 1(IV) chain
  JOURNAL   Eur J Biochem 143 (3), 545-556 (1984)
   PUBMED   6434307
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL161773.21, X05561.1,
            BC151220.1, Y00706.1, AL390755.5, BC047305.1 and AA678474.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Dec 18, 2014 this sequence version replaced NP_001836.2.
            
            Summary: This gene encodes a type IV collagen alpha protein. Type
            IV collagen proteins are integral components of basement membranes.
            This gene shares a bidirectional promoter with a paralogous gene on
            the opposite strand. The protein consists of an amino-terminal 7S
            domain, a triple-helix forming collagenous domain, and a
            carboxy-terminal non-collagenous domain. It functions as part of a
            heterotrimer and interacts with other extracellular matrix
            components such as perlecans, proteoglycans, and laminins. In
            addition, proteolytic cleavage of the non-collagenous
            carboxy-terminal domain results in a biologically active fragment
            known as arresten, which has anti-angiogenic and tumor suppressor
            properties. Mutations in this gene cause porencephaly,
            cerebrovascular disease, and renal and muscular defects.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC151220.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2147920
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000375820.10/ ENSP00000364979.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1669
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..1669
                     /product="collagen alpha-1(IV) chain isoform 1
                     preproprotein"
                     /note="collagen of basement membrane, alpha-1 chain;
                     collagen IV, alpha-1 polypeptide; collagen alpha-1(IV)
                     chain; COL4A1 NC1 domain; arresten"
                     /calculated_mol_wt=157664
     sig_peptide     1..27
                     /note="/evidence=ECO:0000269|PubMed:4043082; propagated
                     from UniProtKB/Swiss-Prot (P02462.4)"
                     /calculated_mol_wt=2966
     Region          <42..>361
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          48..459
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     mat_peptide     173..1669
                     /product="Collagen alpha-1(IV) chain. /id=PRO_0000005749"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
                     /calculated_mol_wt=144012
     Region          173..1440
                     /region_name="Triple-helical region"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
     Site            204
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            207
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            210
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Region          <267..>577
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          504..1382
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
     Region          <506..>766
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            587
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            602
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            603
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            605
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            606
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            623
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            626
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            629
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            632
                     /site_type="hydroxylation"
                     /note="4-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:P02463; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Site            647
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Region          <777..>1047
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <948..>1179
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          <1088..>1335
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Site            1214
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     Region          <1229..>1443
                     /region_name="gly_rich_SclB"
                     /note="LPXTG-anchored collagen-like adhesin Scl2/SclB;
                     NF038329"
                     /db_xref="CDD:468478"
     Region          1404..1431
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
     Site            1424
                     /site_type="hydroxylation"
                     /note="3-hydroxyproline.
                     /evidence=ECO:0000250|UniProtKB:Q7SIB2; propagated from
                     UniProtKB/Swiss-Prot (P02462.4)"
     mat_peptide     1445..1669
                     /product="Arresten. /id=PRO_0000390482"
                     /note="propagated from UniProtKB/Swiss-Prot (P02462.4)"
                     /calculated_mol_wt=24893
     Region          1446..1553
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     Region          1556..1667
                     /region_name="C4"
                     /note="C-terminal tandem repeated domain in type 4
                     procollagen; pfam01413"
                     /db_xref="CDD:460201"
     CDS             1..1669
                     /gene="COL4A1"
                     /gene_synonym="BSVD; BSVD1; COL4A1s; PADMAL; RATOR"
                     /coded_by="NM_001845.6:131..5140"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS9511.1"
                     /db_xref="GeneID:1282"
                     /db_xref="HGNC:HGNC:2202"
                     /db_xref="MIM:120130"
ORIGIN      
        1 mgprlsvwll llpaalllhe ehsraaakgg cagsgcgkcd chgvkgqkge rglpglqgvi
       61 gfpgmqgpeg pqgppgqkgd tgepglpgtk gtrgppgasg ypgnpglpgi pgqdgppgpp
      121 gipgcngtkg ergplgppgl pgfagnpgpp glpgmkgdpg eilghvpgml lkgergfpgi
      181 pgtpgppglp glqgpvgppg ftgppgppgp pgppgekgqm glsfqgpkgd kgdqgvsgpp
      241 gvpgqaqvqe kgdfatkgek gqkgepgfqg mpgvgekgep gkpgprgkpg kdgdkgekgs
      301 pgfpgepgyp gligrqgpqg ekgeagppgp pgivigtgpl gekgergypg tpgprgepgp
      361 kgfpglpgqp gppglpvpgq agapgfpger gekgdrgfpg tslpgpsgrd glpgppgspg
      421 ppgqpgytng ivecqpgppg dqgppgipgq pgfigeigek gqkgesclic didgyrgppg
      481 pqgppgeigf pgqpgakgdr glpgrdgvag vpgpqgtpgl igqpgakgep gefyfdlrlk
      541 gdkgdpgfpg qpgmpgrags pgrdghpglp gpkgspgsvg lkgergppgg vgfpgsrgdt
      601 gppgppgygp agpigdkgqa gfpggpgspg lpgpkgepgk ivplpgppga eglpgspgfp
      661 gpqgdrgfpg tpgrpglpge kgavgqpgig fpgppgpkgv dglpgdmgpp gtpgrpgfng
      721 lpgnpgvqgq kgepgvglpg lkglpglpgi pgtpgekgsi gvpgvpgehg aigppglqgi
      781 rgepgppglp gsvgspgvpg igppgargpp ggqgppglsg ppgikgekgf pgfpgldmpg
      841 pkgdkgaqgl pgitgqsglp glpgqqgapg ipgfpgskge mgvmgtpgqp gspgpvgapg
      901 lpgekgdhgf pgssgprgdp glkgdkgdvg lpgkpgsmdk vdmgsmkgqk gdqgekgqig
      961 pigekgsrgd pgtpgvpgkd gqagqpgqpg pkgdpgisgt pgapglpgpk gsvggmglpg
     1021 tpgekgvpgi pgpqgspglp gdkgakgekg qagppgigip glrgekgdqg iagfpgspge
     1081 kgekgsigip gmpgspglkg spgsvgypgs pglpgekgdk glpgldgipg vkgeaglpgt
     1141 pgptgpagqk gepgsdgipg sagekgepgl pgrgfpgfpg akgdkgskge vgfpglagsp
     1201 gipgskgeqg fmgppgpqgq pglpgspgha tegpkgdrgp qgqpglpglp gpmgppglpg
     1261 idgvkgdkgn pgwpgapgvp gpkgdpgfqg mpgiggspgi tgskgdmgpp gvpgfqgpkg
     1321 lpglqgikgd qgdqgvpgak glpgppgppg pydiikgepg lpgpegppgl kglqglpgpk
     1381 gqqgvtglvg ipgppgipgf dgapgqkgem gpagptgprg fpgppgpdgl pgsmgppgtp
     1441 svdhgflvtr hsqtiddpqc psgtkilyhg ysllyvqgne rahgqdlgta gsclrkfstm
     1501 pflfcninnv cnfasrndys ywlstpepmp msmapitgen irpfisrcav ceapamvmav
     1561 hsqtiqippc psgwsslwig ysfvmhtsag aegsgqalas pgscleefrs apfiechgrg
     1621 tcnyyanays fwlatierse mfkkptpstl kagelrthvs rcqvcmrrt
//
LOCUS       NP_005838                598 aa            linear   PRI 20-NOV-2025
DEFINITION  solute carrier family 23 member 1 isoform a [Homo sapiens].
ACCESSION   NP_005838
VERSION     NP_005838.3
DBSOURCE    REFSEQ: accession NM_005847.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 598)
  AUTHORS   Kobayashi,T.A., Shimada,H., Sano,F.K., Itoh,Y., Enoki,S., Okada,Y.,
            Kusakizako,T. and Nureki,O.
  TITLE     Dimeric transport mechanism of human vitamin C transporter SVCT1
  JOURNAL   Nat Commun 15 (1), 5569 (2024)
   PUBMED   38956111
  REMARK    GeneRIF: Dimeric transport mechanism of human vitamin C transporter
            SVCT1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 598)
  AUTHORS   Toyoda,Y., Miyata,H., Uchida,N., Morimoto,K., Shigesawa,R.,
            Kassai,H., Nakao,K., Tomioka,N.H., Matsuo,H., Ichida,K.,
            Hosoyamada,M., Aiba,A., Suzuki,H. and Takada,T.
  TITLE     Vitamin C transporter SVCT1 serves a physiological role as a urate
            importer: functional analyses and in vivo investigations
  JOURNAL   Pflugers Arch 475 (4), 489-504 (2023)
   PUBMED   36749388
  REMARK    GeneRIF: Vitamin C transporter SVCT1 serves a physiological role as
            a urate importer: functional analyses and in vivo investigations.
REFERENCE   3  (residues 1 to 598)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 598)
  AUTHORS   Hou,H., Zhang,Y., Wu,H., Huang,Z., Liu,S., Liang,H. and Xu,Y.
  TITLE     Impact of SLC23A1 and SLC23A2 Polymorphisms on the Risk for
            Preeclampsia in a Chinese Han Population
  JOURNAL   J Nutr Sci Vitaminol (Tokyo) 68 (5), 368-374 (2022)
   PUBMED   36310070
  REMARK    GeneRIF: Impact of SLC23A1 and SLC23A2 Polymorphisms on the Risk
            for Preeclampsia in a Chinese Han Population.
REFERENCE   5  (residues 1 to 598)
  AUTHORS   Hayashi,K., Noguchi-Shinohara,M., Sato,T., Hosomichi,K., Kannon,T.,
            Abe,C., Domoto,C., Yuki-Nozaki,S., Mori,A., Horimoto,M.,
            Yokogawa,M., Sakai,K., Iwasa,K., Komai,K., Ishimiya,M.,
            Nakamura,H., Ishida,N., Suga,Y., Ishizaki,J., Ishigami,A.,
            Tajima,A. and Yamada,M.
  TITLE     Effects of functional variants of vitamin C transporter genes on
            apolipoprotein E E4-associated risk of cognitive decline: The
            Nakajima study
  JOURNAL   PLoS One 16 (11), e0259663 (2021)
   PUBMED   34780525
  REMARK    GeneRIF: Effects of functional variants of vitamin C transporter
            genes on apolipoprotein E E4-associated risk of cognitive decline:
            The Nakajima study.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 598)
  AUTHORS   Wang,H., Dutta,B., Huang,W., Devoe,L.D., Leibach,F.H., Ganapathy,V.
            and Prasad,P.D.
  TITLE     Human Na(+)-dependent vitamin C transporter 1 (hSVCT1): primary
            structure, functional characteristics and evidence for a
            non-functional splice variant
  JOURNAL   Biochim Biophys Acta 1461 (1), 1-9 (1999)
   PUBMED   10556483
REFERENCE   7  (residues 1 to 598)
  AUTHORS   Rajan,D.P., Huang,W., Dutta,B., Devoe,L.D., Leibach,F.H.,
            Ganapathy,V. and Prasad,P.D.
  TITLE     Human placental sodium-dependent vitamin C transporter (SVCT2):
            molecular cloning and transport function
  JOURNAL   Biochem Biophys Res Commun 262 (3), 762-768 (1999)
   PUBMED   10471399
REFERENCE   8  (residues 1 to 598)
  AUTHORS   Hogue,D.L. and Ling,V.
  TITLE     A human nucleobase transporter-like cDNA (SLC23A1): member of a
            transporter family conserved from bacteria to mammals
  JOURNAL   Genomics 59 (1), 18-23 (1999)
   PUBMED   10395795
REFERENCE   9  (residues 1 to 598)
  AUTHORS   Tsukaguchi,H., Tokui,T., Mackenzie,B., Berger,U.V., Chen,X.Z.,
            Wang,Y., Brubaker,R.F. and Hediger,M.A.
  TITLE     A family of mammalian Na+-dependent L-ascorbic acid transporters
  JOURNAL   Nature 399 (6731), 70-75 (1999)
   PUBMED   10331392
REFERENCE   10 (residues 1 to 598)
  AUTHORS   Faaland,C.A., Race,J.E., Ricken,G., Warner,F.J., Williams,W.J. and
            Holtzman,E.J.
  TITLE     Molecular characterization of two novel transporters from human and
            mouse kidney and from LLC-PK1 cells reveals a novel conserved
            family that is homologous to bacterial and Aspergillus nucleobase
            transporters
  JOURNAL   Biochim Biophys Acta 1442 (2-3), 353-360 (1998)
   PUBMED   9804989
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA385445.1, AJ250807.1,
            BC050261.1 and AI478520.1.
            
            On Feb 27, 2004 this sequence version replaced NP_005838.2.
            
            Summary: The absorption of vitamin C into the body and its
            distribution to organs requires two sodium-dependent vitamin C
            transporters. This gene encodes one of the two transporters. The
            encoded protein is active in bulk vitamin C transport involving
            epithelial surfaces. Previously, this gene had an official symbol
            of SLC23A2. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Dec 2008].
            
            Transcript Variant: This variant (1) represents the more
            predominant transcript and encodes the shorter isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF098277.1, AF170911.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000348729.8/ ENSP00000302701.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..598
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..598
                     /product="solute carrier family 23 member 1 isoform a"
                     /note="sodium-dependent vitamin C transporter-1; yolk sac
                     permease-like molecule 3; solute carrier family 23
                     (nucleobase transporters), member 2; Na(+)/L-ascorbic acid
                     transporter 1; hSVCT1; solute carrier family 23
                     (nucleobase transporters), member 1; solute carrier family
                     23 (ascorbic acid transporter), member 1"
                     /calculated_mol_wt=64684
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Region          30..522
                     /region_name="UraA"
                     /note="Xanthine/uracil permease [Nucleotide transport and
                     metabolism]; COG2233"
                     /db_xref="CDD:441834"
     Site            53..73
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            104..124
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            138
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19379732; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            144
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19379732; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            160..180
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            208..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            251..271
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            313..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            359..379
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            403..423
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            427..447
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            458..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            491..511
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Region          579..598
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            591
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2J0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2J0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI7.4)"
     Site            596
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2J0; propagated from
                     UniProtKB/Swiss-Prot (Q9UHI7.4)"
     CDS             1..598
                     /gene="SLC23A1"
                     /gene_synonym="SLC23A2; SVCT1; YSPL3"
                     /coded_by="NM_005847.5:45..1841"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4212.1"
                     /db_xref="GeneID:9963"
                     /db_xref="HGNC:HGNC:10974"
                     /db_xref="MIM:603790"
ORIGIN      
        1 mraqedlegr tqhettrdps tplptepkfd mlykiedvpp wylcillgfq hyltcfsgti
       61 avpfllaeal cvghdqhmvs qligtiftcv gittliqttv girlplfqas afaflvpaka
      121 ilalerwkcp peeeiygnws lplntshiwh prirevqgai mvssvvevvi gllglpgall
      181 nyigpltvtp tvsliglsvf qaagdragsh wgisacsill iilfsqylrn ltfllpvyrw
      241 gkgltllriq ifkmfpimla imtvwllcyv ltltdvlptd pkaygfqart dargdimaia
      301 pwiripypcq wglptvtaaa vlgmfsatla giiesigdyy acarlagapp ppvhainrgi
      361 ftegicciia gllgtgngst ssspnigvlg itkvgsrrvv qygaaimlvl gtigkftalf
      421 aslpdpilgg mfctlfgmit avglsnlqfv dmnssrnlfv lgfsmffglt lpnylesnpg
      481 aintgilevd qilivlltte mfvggclafi ldntvpgspe ergliqwkag ahansdmsss
      541 lksydfpigm givkritflk yipicpvfkg fsssskdqia ipedtpente tasvctkv
//
LOCUS       NP_001352604            1141 aa            linear   PRI 20-NOV-2025
DEFINITION  cordon-bleu protein-like 1 isoform 7 [Homo sapiens].
ACCESSION   NP_001352604
VERSION     NP_001352604.1
DBSOURCE    REFSEQ: accession NM_001365675.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1141)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1141)
  AUTHORS   Glunk,V., Laber,S., Sinnott-Armstrong,N., Sobreira,D.R.,
            Strobel,S.M., Batista,T.M., Kubitz,P., Moud,B.N., Ebert,H.,
            Huang,Y., Brandl,B., Garbo,G., Honecker,J., Stirling,D.R.,
            Abdennur,N., Calabuig-Navarro,V., Skurk,T., Ocvirk,S., Stemmer,K.,
            Cimini,B.A., Carpenter,A.E., Dankel,S.N., Lindgren,C.M., Hauner,H.,
            Nobrega,M.A. and Claussnitzer,M.
  TITLE     A non-coding variant linked to metabolic obesity with normal weight
            affects actin remodelling in subcutaneous adipocytes
  JOURNAL   Nat Metab 5 (5), 861-879 (2023)
   PUBMED   37253881
  REMARK    GeneRIF: A non-coding variant linked to metabolic obesity with
            normal weight affects actin remodelling in subcutaneous adipocytes.
REFERENCE   3  (residues 1 to 1141)
  AUTHORS   Kwak,J. and Shin,D.
  TITLE     Gene-Nutrient Interactions in Obesity: COBLL1 Genetic Variants
            Interact with Dietary Fat Intake to Modulate the Incidence of
            Obesity
  JOURNAL   Int J Mol Sci 24 (4), 3758 (2023)
   PUBMED   36835164
  REMARK    GeneRIF: Gene-Nutrient Interactions in Obesity: COBLL1 Genetic
            Variants Interact with Dietary Fat Intake to Modulate the Incidence
            of Obesity.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1141)
  AUTHORS   Lansdon,L.A., Dickinson,A., Arlis,S., Liu,H., Hlas,A., Hahn,A.,
            Bonde,G., Long,A., Standley,J., Tyryshkina,A., Wehby,G., Lee,N.R.,
            Daack-Hirsch,S., Mohlke,K., Girirajan,S., Darbro,B.W.,
            Cornell,R.A., Houston,D.W., Murray,J.C. and Manak,J.R.
  TITLE     Genome-wide analysis of copy-number variation in humans with cleft
            lip and/or cleft palate identifies COBLL1, RIC1, and ARHGEF38 as
            clefting genes
  JOURNAL   Am J Hum Genet 110 (1), 71-91 (2023)
   PUBMED   36493769
  REMARK    GeneRIF: Genome-wide analysis of copy-number variation in humans
            with cleft lip and/or cleft palate identifies COBLL1, RIC1, and
            ARHGEF38 as clefting genes.
REFERENCE   5  (residues 1 to 1141)
  AUTHORS   Sun,C., Forster,F., Gutsmann,B., Moulla,Y., Stroh,C., Dietrich,A.,
            Schon,M.R., Gartner,D., Lohmann,T., Dressler,M., Stumvoll,M.,
            Bluher,M., Kovacs,P., Breitfeld,J. and Guiu-Jurado,E.
  TITLE     Metabolic Effects of the Waist-To-Hip Ratio Associated Locus
            GRB14/COBLL1 Are Related to GRB14 Expression in Adipose Tissue
  JOURNAL   Int J Mol Sci 23 (15), 8558 (2022)
   PUBMED   35955692
  REMARK    GeneRIF: Metabolic Effects of the Waist-To-Hip Ratio Associated
            Locus GRB14/COBLL1 Are Related to GRB14 Expression in Adipose
            Tissue.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1141)
  AUTHORS   Barber,M.J., Mangravite,L.M., Hyde,C.L., Chasman,D.I., Smith,J.D.,
            McCarty,C.A., Li,X., Wilke,R.A., Rieder,M.J., Williams,P.T.,
            Ridker,P.M., Chatterjee,A., Rotter,J.I., Nickerson,D.A.,
            Stephens,M. and Krauss,R.M.
  TITLE     Genome-wide association of lipid-lowering response to statins in
            combined study populations
  JOURNAL   PLoS One 5 (3), e9763 (2010)
   PUBMED   20339536
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1141)
  AUTHORS   Gordon,G.J., Dong,L., Yeap,B.Y., Richards,W.G., Glickman,J.N.,
            Edenfield,H., Mani,M., Colquitt,R., Maulik,G., Van Oss,B.,
            Sugarbaker,D.J. and Bueno,R.
  TITLE     Four-gene expression ratio test for survival in patients undergoing
            surgery for mesothelioma
  JOURNAL   J Natl Cancer Inst 101 (9), 678-686 (2009)
   PUBMED   19401544
  REMARK    GeneRIF: The gene ratio test with the COBLL1/ARHGDIA genes for
            survival of patients with malignant pleural mesothelioma has robust
            predictive value.
REFERENCE   8  (residues 1 to 1141)
  AUTHORS   Gonzales,P.A., Pisitkun,T., Hoffert,J.D., Tchapyjnikov,D.,
            Star,R.A., Kleta,R., Wang,N.S. and Knepper,M.A.
  TITLE     Large-scale proteomics and phosphoproteomics of urinary exosomes
  JOURNAL   J Am Soc Nephrol 20 (2), 363-379 (2009)
   PUBMED   19056867
REFERENCE   9  (residues 1 to 1141)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   10 (residues 1 to 1141)
  AUTHORS   Carroll,E.A., Gerrelli,D., Gasca,S., Berg,E., Beier,D.R., Copp,A.J.
            and Klingensmith,J.
  TITLE     Cordon-bleu is a conserved gene involved in neural tube formation
  JOURNAL   Dev Biol 262 (1), 16-31 (2003)
   PUBMED   14512015
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC019181.4.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.187068.1,
                                           SRR1803614.263748.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1141
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.3"
     Protein         1..1141
                     /product="cordon-bleu protein-like 1 isoform 7"
                     /note="cordon-bleu protein-like 1; COBL-like 1"
                     /calculated_mol_wt=125074
     Region          1..35
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          60..126
                     /region_name="RBD"
                     /note="Raf-like Ras-binding domain; pfam02196"
                     /db_xref="CDD:460485"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          144..222
                     /region_name="Cobl"
                     /note="Cordon-bleu ubiquitin-like domain; pfam09469"
                     /db_xref="CDD:462810"
     Site            204
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          262..322
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            286
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          304..309
                     /region_name="KKRRAP 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          338..454
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            339
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            357
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            369
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          373..378
                     /region_name="KKRRAP 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            451
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            454
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          467..512
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            474
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            484
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            487
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            576
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            597
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          793..853
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            799
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          <802..1039
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            826
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            827
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            834
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          895..977
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            924
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            930
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            960
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1008..1094
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1082
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1083
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q3UMF0; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     Region          1090..1115
                     /region_name="WH2_Wc_Cobl"
                     /note="third Wiskott Aldrich syndrome homology region 2
                     (WH2 motif) repeat (called Wc) found in protein
                     Cordon-Bleu (Cobl) and similar proteins; cd21801"
                     /db_xref="CDD:409199"
     Site            order(1094..1095,1097..1099,1101..1103,1111..1114)
                     /site_type="other"
                     /note="actin-binding motif [polypeptide binding]"
                     /db_xref="CDD:409199"
     Region          1111..1114
                     /region_name="actin-binding sequence"
                     /note="actin-binding sequence [structural motif]"
                     /db_xref="CDD:409199"
     Region          1116..1141
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q53SF7.3)"
     Site            1134
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q53SF7.3)"
     CDS             1..1141
                     /gene="COBLL1"
                     /gene_synonym="COBLR1"
                     /coded_by="NM_001365675.2:136..3561"
                     /note="isoform 7 is encoded by transcript variant 10"
                     /db_xref="GeneID:22837"
                     /db_xref="HGNC:HGNC:23571"
                     /db_xref="MIM:610318"
ORIGIN      
        1 mdgrtprpqd aparrkpkak aplppaetky tdvssaadsv estafimeqk enmidkdvel
       61 svvlpgdiik sttvhgskpm mdlliflcaq yhlnpssyti dllsaeqnhi kfkpntpigm
      121 levekvilkp kmldkkkptp iipektvrvv infkktqkti vrvsphaslq elapiicskc
      181 efdplhtlll kdyqsqepld ltkslndlgl relyamdvnr atsvtvfsks slqescqisq
      241 nldimkeken kgffsffqrs kkkrdqtasa patplvnkhr ptftrsntis kpyisntlps
      301 dapkkrrapl ppmpasqsvp qdlahiqerp ascivksmsv detdkspcea grvragslql
      361 ssmsagnssl rrtkrkapsp pskipphqsd ensrvtalqp vdgvppdsas eanspeelss
      421 pagissdysl eeidekeels evpkveaeni spksqdipfv stdiintlkn dpdsalgngs
      481 gefsqnsmee kqetkstdgq ephsvvydts ngkkvvdsir nlkslgpnqe nvvqneiivy
      541 pentednmkn gvkkteinve gvaknnnidm everpsnsea hetdtaisyk enhlaassvp
      601 dqklnqpsae ktkdaaiqtt pscnsfdgkh qdhnlsdskv eecvqtsnnn istqhsclss
      661 qdsvntsref rsqgtliihs edpltvkdpi cahgnddllp pvdridknst asylknyply
      721 rqdynpkpkp sneitreyip kigmttykiv ppksleiskd wqsetieykd dqdmhalgkk
      781 hthenvketa iqtedsaise speeplpnlk pkpnlrtehq vpssvsspdd amvsplkpap
      841 kmtrdtgtap fapnleeinn ileskfksra snaqakpssf flqmqkrvsg hyvtsaaaks
      901 vhaapnpapk eltnkeaerd mlpspeqtls plskmphsvp qplvektddd vigqapaeas
      961 pppiapkpvt ipasqvstqn lktlktfgap rpysssgpsp falavvkrsq sfskertesp
     1021 sasalvqppa nteegkthsv nkfvdipqlg vsdkennsah neqnsqiptp tdgpsftvmr
     1081 qssltfqssd peqmrqsllt airsgeaaak lkrvtipsnt isvngrsrls hsmspdaqdg
     1141 h
//
LOCUS       NP_659498                412 aa            linear   PRI 20-NOV-2025
DEFINITION  spindle and kinetochore-associated protein 3 isoform 1 [Homo
            sapiens].
ACCESSION   NP_659498
VERSION     NP_659498.4
DBSOURCE    REFSEQ: accession NM_145061.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 412)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 412)
  AUTHORS   Liang,G., Duan,C., He,J. and Shi,L.
  TITLE     Spindle and kinetochore-related complex subunit 3 has a protumour
            function in osteosarcoma by activating the Notch pathway
  JOURNAL   Toxicol Appl Pharmacol 483, 116826 (2024)
   PUBMED   38228236
  REMARK    GeneRIF: Spindle and kinetochore-related complex subunit 3 has a
            protumour function in osteosarcoma by activating the Notch pathway.
REFERENCE   3  (residues 1 to 412)
  AUTHORS   Deng,J., Liao,S., Chen,C., Han,F., Lei,S., Lai,X., Ye,K., Han,Q.,
            E,F., Lu,C., Lai,M., Liu,F. and Zhang,H.
  TITLE     Specific intracellular retention of circSKA3 promotes colorectal
            cancer metastasis by attenuating ubiquitination and degradation of
            SLUG
  JOURNAL   Cell Death Dis 14 (11), 750 (2023)
   PUBMED   37973787
  REMARK    GeneRIF: Specific intracellular retention of circSKA3 promotes
            colorectal cancer metastasis by attenuating ubiquitination and
            degradation of SLUG.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 412)
  AUTHORS   Chen,Y., Xu,X., Wang,Y., Zhang,Y., Zhou,T., Jiang,W., Wang,Z.,
            Chang,J., Liu,S., Chen,R., Shan,J., Wang,J., Wang,Y., Li,C. and
            Li,X.
  TITLE     Hypoxia-induced SKA3 promoted cholangiocarcinoma progression and
            chemoresistance by enhancing fatty acid synthesis via the
            regulation of PAR-dependent HIF-1a deubiquitylation
  JOURNAL   J Exp Clin Cancer Res 42 (1), 265 (2023)
   PUBMED   37821935
  REMARK    GeneRIF: Hypoxia-induced SKA3 promoted cholangiocarcinoma
            progression and chemoresistance by enhancing fatty acid synthesis
            via the regulation of PAR-dependent HIF-1a deubiquitylation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 412)
  AUTHORS   Ning,G., Lu,C., Chen,Y., Jiang,M., Si,P. and Zhang,R.
  TITLE     Transcription factor ZEB1 regulates PLK1-mediated SKA3
            phosphorylation to promote lung cancer cell proliferation,
            migration and cell cycle
  JOURNAL   Anticancer Drugs 34 (7), 866-876 (2023)
   PUBMED   36728910
  REMARK    GeneRIF: Transcription factor ZEB1 regulates PLK1-mediated SKA3
            phosphorylation to promote lung cancer cell proliferation,
            migration and cell cycle.
REFERENCE   6  (residues 1 to 412)
  AUTHORS   Raaijmakers,J.A., Tanenbaum,M.E., Maia,A.F. and Medema,R.H.
  TITLE     RAMA1 is a novel kinetochore protein involved in
            kinetochore-microtubule attachment
  JOURNAL   J Cell Sci 122 (Pt 14), 2436-2445 (2009)
   PUBMED   19549680
  REMARK    GeneRIF: RAMA1 is a novel kinetochore protein involved in
            kinetochore-microtubule attachment.
REFERENCE   7  (residues 1 to 412)
  AUTHORS   Guimaraes,G.J. and Deluca,J.G.
  TITLE     Connecting with Ska, a key complex at the kinetochore-microtubule
            interface
  JOURNAL   EMBO J 28 (10), 1375-1377 (2009)
   PUBMED   19458608
REFERENCE   8  (residues 1 to 412)
  AUTHORS   Theis,M., Slabicki,M., Junqueira,M., Paszkowski-Rogacz,M.,
            Sontheimer,J., Kittler,R., Heninger,A.K., Glatter,T., Kruusmaa,K.,
            Poser,I., Hyman,A.A., Pisabarro,M.T., Gstaiger,M., Aebersold,R.,
            Shevchenko,A. and Buchholz,F.
  TITLE     Comparative profiling identifies C13orf3 as a component of the Ska
            complex required for mammalian cell division
  JOURNAL   EMBO J 28 (10), 1453-1465 (2009)
   PUBMED   19387489
  REMARK    GeneRIF: These data identify C13orf3 (Ska3) as an important factor
            for metaphase to anaphase progression and highlight the potential
            of combined RNAi screening and protein localisation analyses.
REFERENCE   9  (residues 1 to 412)
  AUTHORS   Gaitanos,T.N., Santamaria,A., Jeyaprakash,A.A., Wang,B., Conti,E.
            and Nigg,E.A.
  TITLE     Stable kinetochore-microtubule interactions depend on the Ska
            complex and its new component Ska3/C13Orf3
  JOURNAL   EMBO J 28 (10), 1442-1452 (2009)
   PUBMED   19360002
  REMARK    GeneRIF: C13Orf3 (now termed Ska3) localizes to the spindle and
            kinetochore throughout mitosis and its depletion markedly delays
            anaphase transition.
REFERENCE   10 (residues 1 to 412)
  AUTHORS   Welburn,J.P., Grishchuk,E.L., Backer,C.B., Wilson-Kubalek,E.M.,
            Yates,J.R. 3rd and Cheeseman,I.M.
  TITLE     The human kinetochore Ska1 complex facilitates microtubule
            depolymerization-coupled motility
  JOURNAL   Dev Cell 16 (3), 374-385 (2009)
   PUBMED   19289083
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL158032.32 and AF361358.1.
            
            On Oct 8, 2009 this sequence version replaced NP_659498.3.
            
            Summary: This gene encodes a component of the spindle and
            kinetochore-associated protein complex that regulates microtubule
            attachment to the kinetochores during mitosis. The encoded protein
            localizes to the outer kinetechore and may be required for normal
            chromosome segregation and cell division. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF361358.1, SRR1803611.270606.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000314759.6/ ENSP00000319417.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..412
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.11"
     Protein         1..412
                     /product="spindle and kinetochore-associated protein 3
                     isoform 1"
                     /note="spindle and kinetochore-associated protein 3"
                     /calculated_mol_wt=46228
     Region          3..101
                     /region_name="SKA3_N"
                     /note="Spindle and kinetochore-associated protein 3,
                     N-terminal domain; cd12957"
                     /db_xref="CDD:240570"
     Site            order(3..8,10..12,15..16,19)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:240570"
     Site            order(10,14,17,21,25,28..29,40..41,44,47..48,51..52,
                     54..55,58..59,61..62,65..66,68..69,73,76,79)
                     /site_type="other"
                     /note="SKA1 interface [polypeptide binding]"
                     /db_xref="CDD:240570"
     Site            order(11,14,18,22,25..26,29,47,51,54,57..58,61,68,72,75,
                     78..79,81..82,89,93,96)
                     /site_type="other"
                     /note="SKA2 interface [polypeptide binding]"
                     /db_xref="CDD:240570"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Region          132..156
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            155
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:15144186,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            265
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     Site            384
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q8IX90.2)"
     CDS             1..412
                     /gene="SKA3"
                     /gene_synonym="C13orf3; RAMA1"
                     /coded_by="NM_145061.6:76..1314"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31946.1"
                     /db_xref="GeneID:221150"
                     /db_xref="HGNC:HGNC:20262"
                     /db_xref="MIM:619247"
ORIGIN      
        1 mdpirsfcgk lrslastldc etarlqrald geesdfedyp mrilydlhse vqtlkddvni
       61 lldkarlenq egidfikatk vlmeknsmdi mkireyfqky gysprvkkns vheqeainsd
      121 pelsncenfq ktdvkddlsd ppvasscise ksprspqlsd fgleryivsq vlpnppqavn
      181 nykeepvivt pptkqslvkv lktpkcalkm ddfecvtpkl ehfgiseytm clnedytmgl
      241 knarnnksee aidtesrlnd nvfatpspii qqleksdaey tnsplvptfc tpglkipstk
      301 nsialvstny plsktnsssn dlevedrtsl vlnsdtcfen ltdpssptis syenllrtpt
      361 ppevtkiped ilqllskyns nlatpiaika vppskrflkh gqnirdvsnk en
//
LOCUS       NP_001351756             470 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 14 [Homo sapiens].
ACCESSION   NP_001351756 XP_011536767
VERSION     NP_001351756.1
DBSOURCE    REFSEQ: accession NM_001364827.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 470)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 470)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 470)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 470)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 470)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 470)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 470)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 470)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 470)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 470)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC079684.16 and AC079601.25.
            
            On Jul 12, 2018 this sequence version replaced XP_011536767.1.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.72464.1,
                                           SRR1660809.126306.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..470
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..470
                     /product="periphilin-1 isoform 14"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=53813
     Region          266..>322
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Region          <421..>456
                     /region_name="HERV-K_REC"
                     /note="Rec (regulator of expression encoded by corf) of
                     HERV-K-113; pfam15695"
                     /db_xref="CDD:292323"
     CDS             1..470
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001364827.2:84..1496"
                     /note="isoform 14 is encoded by transcript variant 14"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdgynrl vnivpkkppl ldrpgegsyn ryyshvdyrd
       61 ydegrsfshd rrsgpphrgd esgyrwtrdd hsasrqpeyr dmrdgfrrks fysshyarer
      121 spykrdntff respvgrkds phsrsgssvs srsyspersk sysfhqsqhr nkerpvqslk
      181 tsrdtspssg savssskvld kpsrltekel aeaaskwaae kleksdesnl peiseyeags
      241 taplftdqpe epesntthgi elfedsqltt rskaiasktk eieqvyrqdc etfgmvvkml
      301 iekdpsleks iqfalrqnlh eiesagqtwq qvppvrntem dhdgtpeneg eetaqsalfg
      361 fqhdasnhti vglgpnqvpe mkettlqapq ppqapqplqp rkkrvrrttq lrrttgapdi
      421 twgmlkkttq eaerillrtq tpftpenlfl amlsvvhcns rkdvkpenkq
//
LOCUS       NP_001273897             304 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor JunD isoform deltaJunD [Homo sapiens].
ACCESSION   NP_001273897
VERSION     NP_001273897.1
DBSOURCE    REFSEQ: accession NM_001286968.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 304)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 304)
  AUTHORS   Schnoegl,D., Hiesinger,A., Huntington,N.D. and Gotthardt,D.
  TITLE     AP-1 transcription factors in cytotoxic lymphocyte development and
            antitumor immunity
  JOURNAL   Curr Opin Immunol 85, 102397 (2023)
   PUBMED   37931499
  REMARK    GeneRIF: AP-1 transcription factors in cytotoxic lymphocyte
            development and antitumor immunity.
            Review article
REFERENCE   3  (residues 1 to 304)
  AUTHORS   Chang,Y., Chen,L., Tang,J., Chen,G., Ji,J. and Xu,M.
  TITLE     USP7-mediated JUND suppresses RCAN2 transcription and elevates
            NFATC1 to enhance stem cell property in colorectal cancer
  JOURNAL   Cell Biol Toxicol 39 (6), 3121-3140 (2023)
   PUBMED   37535148
  REMARK    GeneRIF: USP7-mediated JUND suppresses RCAN2 transcription and
            elevates NFATC1 to enhance stem cell property in colorectal cancer.
REFERENCE   4  (residues 1 to 304)
  AUTHORS   Zhang,D., Pan,G., Cheng,N., Sun,L., Zhou,X., Li,C. and Zhao,J.
  TITLE     JUND facilitates proliferation and angiogenesis of esophageal
            squamous cell carcinoma cell via MAPRE2 up-regulation
  JOURNAL   Tissue Cell 81, 102010 (2023)
   PUBMED   36608637
  REMARK    GeneRIF: JUND facilitates proliferation and angiogenesis of
            esophageal squamous cell carcinoma cell via MAPRE2 up-regulation.
REFERENCE   5  (residues 1 to 304)
  AUTHORS   Goos,H., Kinnunen,M., Salokas,K., Tan,Z., Liu,X., Yadav,L.,
            Zhang,Q., Wei,G.H. and Varjosalo,M.
  TITLE     Human transcription factor protein interaction networks
  JOURNAL   Nat Commun 13 (1), 766 (2022)
   PUBMED   35140242
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 304)
  AUTHORS   Short,J.D. and Pfarr,C.M.
  TITLE     Translational regulation of the JunD messenger RNA
  JOURNAL   J Biol Chem 277 (36), 32697-32705 (2002)
   PUBMED   12105216
  REMARK    GeneRIF: Translation initiation from alternative AUG and non-AUG
            sites in human, mouse and rat.
REFERENCE   7  (residues 1 to 304)
  AUTHORS   Franklin,C.C., McCulloch,A.V. and Kraft,A.S.
  TITLE     In vitro association between the Jun protein family and the general
            transcription factors, TBP and TFIIB
  JOURNAL   Biochem J 305 (Pt 3) (Pt 3), 967-974 (1995)
   PUBMED   7848298
REFERENCE   8  (residues 1 to 304)
  AUTHORS   Berger,I. and Shaul,Y.
  TITLE     Structure and function of human jun-D
  JOURNAL   Oncogene 6 (4), 561-566 (1991)
   PUBMED   1903194
REFERENCE   9  (residues 1 to 304)
  AUTHORS   Mollinedo,F., Vaquerizo,M.J. and Naranjo,J.R.
  TITLE     Expression of c-jun, jun B and jun D proto-oncogenes in human
            peripheral-blood granulocytes
  JOURNAL   Biochem J 273(Pt 2) (Pt 2), 477-479 (1991)
   PUBMED   1899335
REFERENCE   10 (residues 1 to 304)
  AUTHORS   Nomura,N., Ide,M., Sasamoto,S., Matsui,M., Date,T. and Ishizaki,R.
  TITLE     Isolation of human cDNA clones of jun-related genes, jun-B and
            jun-D
  JOURNAL   Nucleic Acids Res 18 (10), 3047-3048 (1990)
   PUBMED   2112242
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK223630.1, CB050506.1,
            BQ130444.1 and AW027337.1.
            
            Summary: The protein encoded by this intronless gene is a member of
            the JUN family, and a functional component of the AP1 transcription
            factor complex. This protein has been proposed to protect cells
            from p53-dependent senescence and apoptosis. Alternative
            translation initiation site usage results in the production of
            different isoforms (PMID:12105216). [provided by RefSeq, Nov 2013].
            
            Transcript Variant: This variant (1) encodes two isoforms resulting
            from the use of alternative in-frame translation initiation codons.
            The longer isoform (JunD-FL) is derived from an upstream AUG (S1
            ORF, PMID:12105216), while the shorter isoform (deltaJunD) is
            derived from a downstream AUG (S3 ORF, PMID:12105216). This RefSeq
            represents the shorter isoform (deltaJunD).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: AK223630.1, SRR1163657.559005.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: experimental evidence
                                                (PMID:12105216)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..304
                     /product="transcription factor JunD isoform deltaJunD"
                     /note="transcription factor jun-D; activator protein 1;
                     jun D proto-oncogene; transcription factor AP-1 subunit
                     JunD; transcription factor JunD"
                     /calculated_mol_wt=31103
     Region          1..213
                     /region_name="Jun"
                     /note="Jun-like transcription factor; pfam03957"
                     /db_xref="CDD:461108"
     Region          227..286
                     /region_name="bZIP_Jun"
                     /note="Basic leucine zipper (bZIP) domain of Jun proteins
                     and similar proteins: a DNA-binding and dimerization
                     domain; cd14696"
                     /db_xref="CDD:269844"
     Region          228..279
                     /region_name="coiled coil"
                     /note="coiled coil [structural motif]"
                     /db_xref="CDD:269844"
     Site            order(232,234..236,238..243,245..247)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:269844"
     Site            order(246..247,249..250,252..254,256..257,260..261,
                     263..264,266..268,270..271,274..275,278,281,284..286)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:269844"
     CDS             1..304
                     /gene="JUND"
                     /gene_synonym="AP-1"
                     /coded_by="NM_001286968.2:268..1182"
                     /note="isoform deltaJunD is encoded by transcript variant
                     1"
                     /db_xref="GeneID:3727"
                     /db_xref="HGNC:HGNC:6206"
                     /db_xref="MIM:165162"
ORIGIN      
        1 mmkkdaltls lseqvaaalk paaappptpl radgapsaap pdgllaspdl gllklaspel
       61 erliiqsngl vtttptssqf lypkvaasee qefaegfvka ledlhkqnql gagaaaaaaa
      121 aaaggpsgta tgsappgela paaaapeapv yanlssyagg aggaggaatv afaaepvpfp
      181 pppppgalgp prlaalkdep qtvpdvpsfg espplspidm dtqerikaer krlrnriaas
      241 kcrkrkleri srleekvktl ksqntelast asllreqvaq lkqkvlshvn sgcqllpqhq
      301 vpay
//
LOCUS       NP_004765               1581 aa            linear   PRI 20-NOV-2025
DEFINITION  mediator of RNA polymerase II transcription subunit 1 [Homo
            sapiens].
ACCESSION   NP_004765
VERSION     NP_004765.2
DBSOURCE    REFSEQ: accession NM_004774.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1581)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1581)
  AUTHORS   Li,Z., Sun,M., Yang,R., Wang,Z., Zhu,Q., Zhang,Y., Yang,H.,
            Meng,Z., Hu,L. and Sui,L.
  TITLE     Mediator complex subunit 1 promotes oral squamous cell carcinoma
            progression by activating MMP9 transcription and suppressing CD8+ T
            cell antitumor immunity
  JOURNAL   J Exp Clin Cancer Res 43 (1), 270 (2024)
   PUBMED   39343952
  REMARK    GeneRIF: Mediator complex subunit 1 promotes oral squamous cell
            carcinoma progression by activating MMP9 transcription and
            suppressing CD8[+] T cell antitumor immunity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1581)
  AUTHORS   Chaudhuri,S.M., Weinberg,S.E., Wang,D., Yalom,L.K., Montauti,E.,
            Iyer,R., Tang,A.Y., Torres Acosta,M.A., Shen,J., Mani,N.L.,
            Wang,S., Liu,K., Lu,W., Bui,T.M., Manzanares,L.D., Dehghani,Z.,
            Wai,C.M., Gao,B., Wei,J., Yue,F., Cui,W., Singer,B.D., Sumagin,R.,
            Zhang,Y. and Fang,D.
  TITLE     Mediator complex subunit 1 architects a tumorigenic Treg cell
            program independent of inflammation
  JOURNAL   Cell Rep Med 5 (3), 101441 (2024)
   PUBMED   38428427
  REMARK    GeneRIF: Mediator complex subunit 1 architects a tumorigenic Treg
            cell program independent of inflammation.
REFERENCE   4  (residues 1 to 1581)
  AUTHORS   Shen,Y., Zhou,L., Xu,M., Tan,Z., Yao,K. and Wang,W.
  TITLE     MED1 induces M2 polarization of tumor-associated macrophages to
            aggravate breast cancer
  JOURNAL   Genes Genomics 45 (12), 1517-1525 (2023)
   PUBMED   37594664
  REMARK    GeneRIF: MED1 induces M2 polarization of tumor-associated
            macrophages to aggravate breast cancer.
REFERENCE   5  (residues 1 to 1581)
  AUTHORS   Gao,J., Bao,M., Xing,Y., Ding,Y., Han,T., Wen,E., Liu,J., Yue,S.,
            Wang,R., Wang,L., Liu,J., Zhao,S., Huang,J., Liu,E. and Bai,L.
  TITLE     Mediator subunit MED1 deficiency prevents carbon
            tetrachloride-induced hepatic fibrosis in mice
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 325 (5), G418-G428 (2023)
   PUBMED   37668531
  REMARK    GeneRIF: Mediator subunit MED1 deficiency prevents carbon
            tetrachloride-induced hepatic fibrosis in mice.
REFERENCE   6  (residues 1 to 1581)
  AUTHORS   Yuan,C.X., Ito,M., Fondell,J.D., Fu,Z.Y. and Roeder,R.G.
  TITLE     The TRAP220 component of a thyroid hormone receptor- associated
            protein (TRAP) coactivator complex interacts directly with nuclear
            receptors in a ligand-dependent fashion
  JOURNAL   Proc Natl Acad Sci U S A 95 (14), 7939-7944 (1998)
   PUBMED   9653119
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Nov 24;95(24):14584]
REFERENCE   7  (residues 1 to 1581)
  AUTHORS   Drane,P., Barel,M., Balbo,M. and Frade,R.
  TITLE     Identification of RB18A, a 205 kDa new p53 regulatory protein which
            shares antigenic and functional properties with p53
  JOURNAL   Oncogene 15 (25), 3013-3024 (1997)
   PUBMED   9444950
REFERENCE   8  (residues 1 to 1581)
  AUTHORS   Zhu,Y., Qi,C., Jain,S., Rao,M.S. and Reddy,J.K.
  TITLE     Isolation and characterization of PBP, a protein that interacts
            with peroxisome proliferator-activated receptor
  JOURNAL   J Biol Chem 272 (41), 25500-25506 (1997)
   PUBMED   9325263
REFERENCE   9  (residues 1 to 1581)
  AUTHORS   Fondell,J.D., Ge,H. and Roeder,R.G.
  TITLE     Ligand induction of a transcriptionally active thyroid hormone
            receptor coactivator complex
  JOURNAL   Proc Natl Acad Sci U S A 93 (16), 8329-8333 (1996)
   PUBMED   8710870
REFERENCE   10 (residues 1 to 1581)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP357374.1, BC131783.1 and
            AC005288.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 25, 2003 this sequence version replaced NP_004765.1.
            
            Summary: The activation of gene transcription is a multistep
            process that is triggered by factors that recognize transcriptional
            enhancer sites in DNA. These factors work with co-activators to
            direct transcriptional initiation by the RNA polymerase II
            apparatus. The protein encoded by this gene is a subunit of the
            CRSP (cofactor required for SP1 activation) complex, which, along
            with TFIID, is required for efficient activation by SP1. This
            protein is also a component of other multisubunit complexes e.g.
            thyroid hormone receptor-(TR-) associated proteins which interact
            with TR and facilitate TR function on DNA templates in conjunction
            with initiation factors and cofactors. It also regulates
            p53-dependent apoptosis and it is essential for adipogenesis. This
            protein is known to have the ability to self-oligomerize. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC131783.1, Y13467.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300651.11/ ENSP00000300651.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1581
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..1581
                     /product="mediator of RNA polymerase II transcription
                     subunit 1"
                     /note="thyroid receptor interacting protein 2; PPARG
                     binding protein; vitamin D receptor-interacting protein
                     complex component DRIP205; thyroid hormone
                     receptor-associated protein complex component TRAP220;
                     vitamin D receptor-interacting protein 230 kD; ARC205;
                     TRIP-2; PPAR-binding protein; TR-interacting protein 2;
                     p53 regulatory protein RB18A; activator-recruited cofactor
                     205 kDa component; peroxisome proliferator-activated
                     receptor-binding protein; thyroid hormone
                     receptor-associated protein complex 220 kDa component"
                     /calculated_mol_wt=168348
     Region          1..670
                     /region_name="Interaction with the Mediator complex and
                     THRA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          16..590
                     /region_name="Interaction with ESR1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          60..426
                     /region_name="Med1"
                     /note="Mediator of RNA polymerase II transcription subunit
                     1; pfam10744"
                     /db_xref="CDD:463183"
     Region          108..212
                     /region_name="Interaction with the Mediator complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          215..390
                     /region_name="Interaction with the Mediator complex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          405..644
                     /region_name="Interaction with THRA"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          542..789
                     /region_name="Interaction with VDR"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            588
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Region          604..608
                     /region_name="LXXLL motif 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          609..705
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          622..701
                     /region_name="Interaction with PPARGC1A and THRA.
                     /evidence=ECO:0000269|PubMed:14636573"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          645..649
                     /region_name="LXXLL motif 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          656..1066
                     /region_name="Interaction with ESR1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            664
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Region          681..715
                     /region_name="Interaction with GATA1.
                     /evidence=ECO:0000269|PubMed:24245781"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          792..820
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            805
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          874..893
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Region          875..902
                     /region_name="Integrase domain-binding motif (IBM).
                     /evidence=ECO:0000269|PubMed:29997176"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            887
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29997176; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Region          <942..>1079
                     /region_name="PTZ00449"
                     /note="104 kDa microneme/rhoptry antigen; Provisional"
                     /db_xref="CDD:185628"
     Region          948..1566
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            953
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925J9; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1032
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1 or MAPK3.
                     /evidence=ECO:0000269|PubMed:16314496; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1051
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1057
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1156
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1177
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1215
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1223
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Region          1249..1421
                     /region_name="Interaction with TP53.
                     /evidence=ECO:0000269|PubMed:9444950"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1302
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1347
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1403
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1433
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1440
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1457
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by MAPK1 or MAPK3.
                     /evidence=ECO:0000269|PubMed:16314496; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1463
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1465
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q925J9; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1479
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1481
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1482
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q15648.4)"
     Site            1529
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q15648.4)"
     CDS             1..1581
                     /gene="MED1"
                     /gene_synonym="CRSP1; CRSP200; DRIP205; DRIP230; PBP;
                     PPARBP; PPARGBP; RB18A; TRAP220; TRIP2"
                     /coded_by="NM_004774.4:202..4947"
                     /db_xref="CCDS:CCDS11336.1"
                     /db_xref="GeneID:5469"
                     /db_xref="HGNC:HGNC:9234"
                     /db_xref="MIM:604311"
ORIGIN      
        1 mkaqgetees eklskmssll erlhakfnqn rpwsetiklv rqvmekrvvm ssgghqhlvs
       61 cletlqkalk vtslpamtdr lesiarqngl gshlsasgte cyitsdmfyv evqldpagql
      121 cdvkvahhge npvscpelvq qlreknfdef skhlkglvnl ynlpgdnklk tkmylalqsl
      181 eqdlskmaim ywkatnagpl dkilhgsvgy ltprsgghlm nlkyyvspsd llddktaspi
      241 ilhennvsrs lgmnasvtie gtsavyklpi aplimgshpv dnkwtpsfss itsansvdlp
      301 acfflkfpqp ipvsrafvqk lqnctgiplf etqptyaply elitqfelsk dpdpiplnhn
      361 mrfyaalpgq qhcyflnkda plpdgrslqg tlvskitfqh pgrvplilnl irhqvayntl
      421 igscvkrtil kedspgllqf evcplsesrf svsfqhpvnd slvcvvmdvq dsthvsckly
      481 kglsdalict ddfiakvvqr cmsipvtmra irrkaetiqa dtpalsliae tvedmvkknl
      541 ppasspgygm ttgnnpmsgt ttptntfpgg pittlfnmsm sikdrhesvg hgedfskvsq
      601 npiltsllqi tgnggstigs sptpphhtpp pvssmagntk nhpmlmnllk dnpaqdfstl
      661 ygssplerqn sssgsprmei csgsnktkkk kssrlppekp khqteddfqr elfsmdvdsq
      721 npifdvnmta dtldtphitp apsqcstppt typqpvphpq psiqrmvrls ssdsigpdvt
      781 dilsdiaeea sklpstsddc paigtplrds sssghsqstl fdsdvfqtnn nenpytdpad
      841 liadaagsps sdsptnhffh dgvdfnpdll nsqsqsgfge eyfdessqsg dnddfkgfas
      901 qalntlgvpm lggdngetkf kgnnqadtvd fsiisvagka lapadlmehh sgsqgplltt
      961 gdlgkektqk rvkegngtsn stlsgpglds kpgkrsrtps ndgkskdkpp krkkadtegk
     1021 spshsssnrp ftpptstggs kspgsagrsq tppgvatppi pkitiqipkg tvmvgkpssh
     1081 sqytssgsvs ssgskshhsh sssssssast sgkmksskse gssssklsss myssqgssgs
     1141 sqsknssqsg gkpgsspitk hglssgssst kmkpqgkpss lmnpslskpn ispshsrppg
     1201 gsdklaspmk pvpgtppssk akspissgsg gshmsgtsss sgmksssglg ssgslsqktp
     1261 pssnsctass ssfsssgssm sssqnqhgss kgkspsrnkk psltavidkl khgvvtsgpg
     1321 gedpldgqmg vstnssshpm sskhnmsgge fqgkreksdk dkskvstsgs svdsskktse
     1381 sknvgstgva kiiiskhdgg spsikakvtl qkpgessgeg lrpqmasskn ygsplisgst
     1441 pkhergspsh skspaytpqn ldsesesgss iaeksyqnsp ssddgirplp eystekhkkh
     1501 kkekkkvkdk drdrdrdkdr dkkkshsikp eswskspiss dqslsmtsnt ilsadrpsrl
     1561 spdfmigeed ddlmdvalig n
//
LOCUS       NP_001354398            1119 aa            linear   PRI 20-NOV-2025
DEFINITION  activating molecule in BECN1-regulated autophagy protein 1 isoform
            6 [Homo sapiens].
ACCESSION   NP_001354398 XP_006718323
VERSION     NP_001354398.1
DBSOURCE    REFSEQ: accession NM_001367469.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1119)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1119)
  AUTHORS   Gottlieb,S., Shang,W., Ye,D., Kubo,S., Jiang,P.D., Shafer,S.,
            Xu,L., Zheng,L., Park,A.Y., Song,J., Chan,W., Zeng,Z., He,T.,
            Schwarz,B., Haupl,B., Oellerich,T., Lenardo,M.J. and Yao,Y.
  TITLE     AMBRA1 controls the translation of immune-specific genes in T
            lymphocytes
  JOURNAL   Proc Natl Acad Sci U S A 121 (44), e2416722121 (2024)
   PUBMED   39436665
  REMARK    GeneRIF: AMBRA1 controls the translation of immune-specific genes
            in T lymphocytes.
REFERENCE   3  (residues 1 to 1119)
  AUTHORS   Sankar,D.S., Kaeser-Pebernard,S., Vionnet,C., Favre,S., de Oliveira
            Marchioro,L., Pillet,B., Zhou,J., Stumpe,M., Kovacs,W.J.,
            Kressler,D., Antonioli,M., Fimia,G.M. and Dengjel,J.
  TITLE     The ULK1 effector BAG2 regulates autophagy initiation by modulating
            AMBRA1 localization
  JOURNAL   Cell Rep 43 (9), 114689 (2024)
   PUBMED   39207901
  REMARK    GeneRIF: The ULK1 effector BAG2 regulates autophagy initiation by
            modulating AMBRA1 localization.
REFERENCE   4  (residues 1 to 1119)
  AUTHORS   Di Leo,L., Pagliuca,C., Kishk,A., Rizza,S., Tsiavou,C.,
            Pecorari,C., Dahl,C., Pacheco,M.P., Tholstrup,R., Brewer,J.R.,
            Berico,P., Hernando,E., Cecconi,F., Ballotti,R., Bertolotto,C.,
            Filomeni,G., Gjerstorff,M.F., Sauter,T., Lovat,P., Guldberg,P. and
            De Zio,D.
  TITLE     AMBRA1 levels predict resistance to MAPK inhibitors in melanoma
  JOURNAL   Proc Natl Acad Sci U S A 121 (25), e2400566121 (2024)
   PUBMED   38870061
  REMARK    GeneRIF: AMBRA1 levels predict resistance to MAPK inhibitors in
            melanoma.
REFERENCE   5  (residues 1 to 1119)
  AUTHORS   Qu,X., Li,X.Y., Feng,Y., Wang,X., Li,L., Wang,Y.P. and Chu,Y.L.
  TITLE     sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to reduce
            autophagy in gestational diabetes
  JOURNAL   Endokrynol Pol 75 (1), 61-70 (2024)
   PUBMED   38497391
  REMARK    GeneRIF: sh- Ambra1 inhibits IRS-1/PI3K/Akt signalling pathway to
            reduce autophagy in gestational diabetes.
REFERENCE   6  (residues 1 to 1119)
  AUTHORS   Cecconi,F., Di Bartolomeo,S., Nardacci,R., Fuoco,C., Corazzari,M.,
            Giunta,L., Romagnoli,A., Stoykova,A., Chowdhury,K., Fimia,G.M. and
            Piacentini,M.
  TITLE     A novel role for autophagy in neurodevelopment
  JOURNAL   Autophagy 3 (5), 506-508 (2007)
   PUBMED   17622796
REFERENCE   7  (residues 1 to 1119)
  AUTHORS   Le Bot,N.
  TITLE     Autophagy: a new regulator of development
  JOURNAL   Nat Cell Biol 9 (7), 741 (2007)
   PUBMED   17603510
REFERENCE   8  (residues 1 to 1119)
  AUTHORS   Fimia,G.M., Stoykova,A., Romagnoli,A., Giunta,L., Di Bartolomeo,S.,
            Nardacci,R., Corazzari,M., Fuoco,C., Ucar,A., Schwartz,P.,
            Gruss,P., Piacentini,M., Chowdhury,K. and Cecconi,F.
  TITLE     Ambra1 regulates autophagy and development of the nervous system
  JOURNAL   Nature 447 (7148), 1121-1125 (2007)
   PUBMED   17589504
REFERENCE   9  (residues 1 to 1119)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 1119)
  AUTHORS   Meyerson,M. and Harlow,E.
  TITLE     Identification of G1 kinase activity for cdk6, a novel cyclin D
            partner
  JOURNAL   Mol Cell Biol 14 (3), 2077-2086 (1994)
   PUBMED   8114739
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC127035.6, AC115097.6, AC024293.18 and AC116021.5.
            
            On Dec 1, 2018 this sequence version replaced XP_006718323.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.151930.1,
                                           SRR1660809.19725.1 [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p11.2"
     Protein         1..1119
                     /product="activating molecule in BECN1-regulated autophagy
                     protein 1 isoform 6"
                     /note="WD repeat domain 94; DDB1 and CUL4 associated
                     factor 3; activating molecule in BECN1-regulated autophagy
                     protein 1; activating molecule in beclin-1-regulated
                     autophagy; autophagy/beclin-1 regulator 1"
                     /calculated_mol_wt=122489
     Region          1..22
                     /region_name="Interaction with DDB1.
                     /evidence=ECO:0000269|PubMed:30166453"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          51..90
                     /region_name="WD 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MTOR.
                     /evidence=ECO:0000269|PubMed:23524951; propagated from
                     UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          56..92
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          <59..198
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          93..133
                     /region_name="WD 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          99..135
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          135..175
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9C0C7.2)"
     Region          140..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..1119
                     /gene="AMBRA1"
                     /gene_synonym="DCAF3; WDR94"
                     /coded_by="NM_001367469.1:317..3676"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="GeneID:55626"
                     /db_xref="HGNC:HGNC:25990"
                     /db_xref="MIM:611359"
ORIGIN      
        1 mkvvpeknav rilwgrerga ramgaqrllq elvedktrwm kwegkrvelp dsprstflla
       61 fspdrtllas thvnhniyit evktgkcvhs lighrrtpwc vtfhptisgl iasgcldgev
      121 riwdlhggse swftdsnnai aslafhptaq llliatanei hfwdwsrrep favvktasem
      181 ervrlvrfdp lghylltaiv npsnqqgdde peipidgtel shyrqrallq sqpvrrtpll
      241 hnflhmlssr ssgiqtepfh ppeqasstqq dqgllnrpsa fstvqsstag ntlrnlslgp
      301 trrslggpls shpsryhrei apgltgsewt rtvlslnsrs eaesmppprt sassvsllsv
      361 lrqqeggsqa svytsategr gfpasglate sdggngssqn nsgsirhelq cdlrrffley
      421 drlqeldqsl sgeapqtqqa qemlnnnies erpgpshqpt phssennsnl srghlnrcra
      481 chnlltfnnd tlrwerttpn yssgeasssw qvpssfesvp ssgsqlpple rtegqtpsss
      541 rlelsssasp qeertvgvaf nqetghweri ytqssrsgtv sqealhqdmp eesseedslr
      601 rdngdrsrhr aprnarmsap slgrfvprrf llpeylpyag ifhergqpgl athssvnrvl
      661 agavigdgqs avasniantt yrlqwwdftk fdlpeisnas vnvlvqncki yndascdisa
      721 dgqllaafip ssqrgfpdeg ilavyslaph nlgemlytkr fgpnaisvsl spmgryvmvg
      781 lasrrillhp stehmvaqvf rlqqahgget smrrvfnvly pmpadqrrhv sinsarwlpe
      841 pglglaygtn kgdlvicrpe alnsgveyyw dqlnetvftv hsnsrsserp gtsratwrtd
      901 rdmglmnaig lqprnpatsv tsqgtqtlal qlqnaetqte revpepgtaa sgpgegegse
      961 ygasgedals riqrlmaegg mtavvqreqs ttmasmggfg nniivshrih rssqtgtepg
     1021 aahtsspqps tsrgllpeag qlaerglspr taswdqpgtp greptqptlp ssspvpipvs
     1081 lpsaegptlh celtnnnhll dggssrgdaa gprgeprnr
//
LOCUS       NP_002791                219 aa            linear   PRI 20-NOV-2025
DEFINITION  proteasome subunit beta type-9 precursor [Homo sapiens].
ACCESSION   NP_002791
VERSION     NP_002791.1
DBSOURCE    REFSEQ: accession NM_002800.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Hu,X., Hu,Z., Zhang,H., Zhang,N., Feng,H., Jia,X., Zhang,C. and
            Cheng,Q.
  TITLE     Deciphering the tumor-suppressive role of PSMB9 in melanoma through
            multi-omics and single-cell transcriptome analyses
  JOURNAL   Cancer Lett 581, 216466 (2024)
   PUBMED   37944578
  REMARK    GeneRIF: Deciphering the tumor-suppressive role of PSMB9 in
            melanoma through multi-omics and single-cell transcriptome
            analyses.
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Rutkowska,J., Kasacka,I., Rogowski,M. and Olszewska,E.
  TITLE     Immunohistochemical Identification and Assessment of the Location
            of Immunoproteasome Subunits LMP2 and LMP7 in Acquired
            Cholesteatoma
  JOURNAL   Int J Mol Sci 24 (18), 14137 (2023)
   PUBMED   37762439
  REMARK    GeneRIF: Immunohistochemical Identification and Assessment of the
            Location of Immunoproteasome Subunits LMP2 and LMP7 in Acquired
            Cholesteatoma.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Kim,M., Serwa,R.A., Samluk,L., Suppanz,I., Kodron,A.,
            Stepkowski,T.M., Elancheliyan,P., Tsegaye,B., Oeljeklaus,S.,
            Wasilewski,M., Warscheid,B. and Chacinska,A.
  TITLE     Immunoproteasome-specific subunit PSMB9 induction is required to
            regulate cellular proteostasis upon mitochondrial dysfunction
  JOURNAL   Nat Commun 14 (1), 4092 (2023)
   PUBMED   37433777
  REMARK    GeneRIF: Immunoproteasome-specific subunit PSMB9 induction is
            required to regulate cellular proteostasis upon mitochondrial
            dysfunction.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Shani,S., Goldstein,O., Gana-Weisz,M., Bar-Shira,A., Thaler,A.,
            Gurevich,T., Mirelman,A., Giladi,N., Alcalay,R.N. and
            Orr-Urtreger,A.
  TITLE     Variants in PSMB9 and FGR differentially affect Parkinson's disease
            risk in GBA and LRRK2 mutation carriers
  JOURNAL   Parkinsonism Relat Disord 111, 105398 (2023)
   PUBMED   37116292
  REMARK    GeneRIF: Variants in PSMB9 and FGR differentially affect
            Parkinson's disease risk in GBA and LRRK2 mutation carriers.
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Kristensen,P., Johnsen,A.H., Uerkvitz,W., Tanaka,K. and Hendil,K.B.
  TITLE     Human proteasome subunits from 2-dimensional gels identified by
            partial sequencing
  JOURNAL   Biochem Biophys Res Commun 205 (3), 1785-1789 (1994)
   PUBMED   7811265
  REMARK    Erratum:[Biochem Biophys Res Commun. 1995 Feb 27;207(3):1059. doi:
            10.1006/bbrc.1995.1294. PMID: 7864893]
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Beck,S., Kelly,A., Radley,E., Khurshid,F., Alderton,R.P. and
            Trowsdale,J.
  TITLE     DNA sequence analysis of 66 kb of the human MHC class II region
            encoding a cluster of genes for antigen processing
  JOURNAL   J Mol Biol 228 (2), 433-441 (1992)
   PUBMED   1453454
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Fruh,K., Yang,Y., Arnold,D., Chambers,J., Wu,L., Waters,J.B.,
            Spies,T. and Peterson,P.A.
  TITLE     Alternative exon usage and processing of the major
            histocompatibility complex-encoded proteasome subunits
  JOURNAL   J Biol Chem 267 (31), 22131-22140 (1992)
   PUBMED   1429565
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Kelly,A., Powis,S.H., Glynne,R., Radley,E., Beck,S. and
            Trowsdale,J.
  TITLE     Second proteasome-related gene in the human MHC class II region
  JOURNAL   Nature 353 (6345), 667-668 (1991)
   PUBMED   1922385
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Martinez,C.K. and Monaco,J.J.
  TITLE     Homology of proteasome subunits to a major histocompatibility
            complex-linked LMP gene
  JOURNAL   Nature 353 (6345), 664-667 (1991)
   PUBMED   1681432
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BF513693.1, BC065513.1 and
            AI310206.1.
            
            Summary: The proteasome is a multicatalytic proteinase complex with
            a highly ordered ring-shaped 20S core structure. The core structure
            is composed of 4 rings of 28 non-identical subunits; 2 rings are
            composed of 7 alpha subunits and 2 rings are composed of 7 beta
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            member of the proteasome B-type family, also known as the T1B
            family, that is a 20S core beta subunit. This gene is located in
            the class II region of the MHC (major histocompatibility complex).
            Expression of this gene is induced by gamma interferon and this
            gene product replaces catalytic subunit 1 (proteasome beta 6
            subunit) in the immunoproteasome. Proteolytic processing is
            required to generate a mature subunit. [provided by RefSeq, Mar
            2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.229991.1,
                                           SRR5189658.127609.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000374859.3/ ENSP00000363993.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.32"
     Protein         1..219
                     /product="proteasome subunit beta type-9 precursor"
                     /EC_number="3.4.25.1"
                     /note="proteasome-related gene 2; proteasome chain 7;
                     macropain chain 7; low molecular mass protein 2;
                     multicatalytic endopeptidase complex chain 7; proteasome
                     catalytic subunit 1i; proteasome subunit beta 6i;
                     proteasome subunit beta type-9; proteasome subunit
                     beta-1i; really interesting new gene 12 protein;
                     proteasome (prosome, macropain) subunit, beta type, 9
                     (large multifunctional peptidase 2); proteasome subunit
                     beta 9; proteasome subunit beta1i"
                     /calculated_mol_wt=23133
     Site            20..21
                     /site_type="cleavage"
                     /note="Cleavage, by autolysis.
                     /evidence=ECO:0000250|UniProtKB:O35955; propagated from
                     UniProtKB/Swiss-Prot (P28065.2)"
     mat_peptide     21..219
                     /product="Proteasome subunit beta type-9.
                     /id=PRO_0000026620"
                     /note="propagated from UniProtKB/Swiss-Prot (P28065.2)"
                     /calculated_mol_wt=21276
     Region          21..207
                     /region_name="proteasome_beta_type_6"
                     /note="proteasome beta type-6 subunit. The 20S proteasome,
                     multisubunit proteolytic complex, is the central enzyme of
                     nonlysosomal protein degradation in both the cytosol and
                     nucleus. It is composed of 28 subunits arranged as four
                     homoheptameric rings that...; cd03762"
                     /db_xref="CDD:239731"
     Site            order(21,37,39,53,149,186,189..190)
                     /site_type="active"
                     /db_xref="CDD:239731"
     Site            order(39,42,44..49,69,71,86,98,101..102,104..105,108,111,
                     134,136,138..141,144,152..153,155..156,159..161,177,
                     184..187,190..191)
                     /site_type="other"
                     /note="beta subunit interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:239731"
     Site            53
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P28065.2)"
     Site            109
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P28065.2)"
     CDS             1..219
                     /gene="PSMB9"
                     /gene_synonym="beta1i; LMP2; PRAAS3; PRAAS6; PSMB6i;
                     RING12"
                     /coded_by="NM_002800.5:39..698"
                     /db_xref="CCDS:CCDS4759.1"
                     /db_xref="GeneID:5698"
                     /db_xref="HGNC:HGNC:9546"
                     /db_xref="MIM:177045"
ORIGIN      
        1 mlragaptgd lpragevhtg ttimavefdg gvvmgsdsrv sageavvnrv fdklsplher
       61 iycalsgsaa daqavadmaa yqlelhgiel eepplvlaaa nvvrnisyky redlsahlmv
      121 agwdqreggq vygtlggmlt rqpfaiggsg stfiygyvda aykpgmspee crrfttdaia
      181 lamsrdgssg gviylvtita agvdhrvilg nelpkfyde
//
LOCUS       NP_001337619             736 aa            linear   PRI 20-NOV-2025
DEFINITION  krev interaction trapped protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001337619
VERSION     NP_001337619.1
DBSOURCE    REFSEQ: accession NM_001350690.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 736)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 736)
  AUTHORS   Croft,J., Sandoval,D.F., Cistola,D. and Zhang,J.
  TITLE     Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation
  JOURNAL   Metab Brain Dis 39 (5), 885-893 (2024)
   PUBMED   38795261
  REMARK    GeneRIF: Plasma water T2 detects age-stratified differences in
            cardiometabolic health among familial CCM patients with Hispanic
            CCM1 mutation.
REFERENCE   3  (residues 1 to 736)
  AUTHORS   Li,C., Liu,P., Huang,W., Wang,H., Ma,K., Zhuo,L., Kang,Y., He,Q.,
            Lin,Y., Kang,D. and Lin,F.
  TITLE     A novel KRIT1/CCM1 mutation accompanied by a NOTCH3 mutation in a
            Chinese family with multiple cerebral cavernous malformations
  JOURNAL   Neurogenetics 24 (2), 137-146 (2023)
   PUBMED   36892712
  REMARK    GeneRIF: A novel KRIT1/CCM1 mutation accompanied by a NOTCH3
            mutation in a Chinese family with multiple cerebral cavernous
            malformations.
REFERENCE   4  (residues 1 to 736)
  AUTHORS   He,Q., Ye,A., Ye,W., Liao,X., Qin,G., Xu,Y., Yin,Y., Luo,H., Yi,M.,
            Xian,L., Zhang,S., Qin,X., Zhu,W. and Li,Y.
  TITLE     Cancer-secreted exosomal miR-21-5p induces angiogenesis and
            vascular permeability by targeting KRIT1
  JOURNAL   Cell Death Dis 12 (6), 576 (2021)
   PUBMED   34088891
  REMARK    GeneRIF: Cancer-secreted exosomal miR-21-5p induces angiogenesis
            and vascular permeability by targeting KRIT1.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 736)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 736)
  AUTHORS   Laberge-le Couteulx,S., Jung,H.H., Labauge,P., Houtteville,J.P.,
            Lescoat,C., Cecillon,M., Marechal,E., Joutel,A., Bach,J.F. and
            Tournier-Lasserve,E.
  TITLE     Truncating mutations in CCM1, encoding KRIT1, cause hereditary
            cavernous angiomas
  JOURNAL   Nat Genet 23 (2), 189-193 (1999)
   PUBMED   10508515
REFERENCE   7  (residues 1 to 736)
  AUTHORS   Serebriiskii,I., Estojak,J., Sonoda,G., Testa,J.R. and Golemis,E.A.
  TITLE     Association of Krev-1/rap1a with Krit1, a novel ankyrin
            repeat-containing protein encoded by a gene mapping to 7q21-22
  JOURNAL   Oncogene 15 (9), 1043-1049 (1997)
   PUBMED   9285558
REFERENCE   8  (residues 1 to 736)
  AUTHORS   Marchuk,D.A., Gallione,C.J., Morrison,L.A., Clericuzio,C.L.,
            Hart,B.L., Kosofsky,B.E., Louis,D.N., Gusella,J.F., Davis,L.E. and
            Prenger,V.L.
  TITLE     A locus for cerebral cavernous malformations maps to chromosome 7q
            in two families
  JOURNAL   Genomics 28 (2), 311-314 (1995)
   PUBMED   8530042
REFERENCE   9  (residues 1 to 736)
  AUTHORS   Gunel,M., Awad,I.A., Anson,J. and Lifton,R.P.
  TITLE     Mapping a gene causing cerebral cavernous malformation to
            7q11.2-q21
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6620-6624 (1995)
   PUBMED   7604043
REFERENCE   10 (residues 1 to 736)
  AUTHORS   Flemming,K.D., Smith,E., Marchuk,D. and Derry,W.B.
  TITLE     Familial Cerebral Cavernous Malformations
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC000120.1.
            
            Summary: This gene encodes a protein containing four ankyrin
            repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and
            multiple NPXY sequences. The encoded protein is localized in the
            nucleus and cytoplasm. It binds to integrin cytoplasmic
            domain-associated protein-1 alpha (ICAP1alpha), and plays a
            critical role in beta1-integrin-mediated cell proliferation. It
            associates with junction proteins and RAS-related protein 1A
            (Rap1A), which requires the encoded protein for maintaining the
            integrity of endothelial junctions. It is also a
            microtubule-associated protein and may play a role in microtubule
            targeting. Mutations in this gene result in cerebral cavernous
            malformations. Multiple alternatively spliced transcript variants
            have been found for this gene. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (26), as well as variants 1-4,
            9-25, and 27-34, encodes isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.133016.1,
                                           SRR1803615.185001.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..736
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.2"
     Protein         1..736
                     /product="krev interaction trapped protein 1 isoform 1"
                     /note="ankyrin repeat-containing protein Krit1; krev
                     interaction trapped protein 1; krev interaction trapped 1;
                     cerebral cavernous malformations 1 protein"
                     /calculated_mol_wt=84217
     Region          1..170
                     /region_name="N-terminal domain similar to Nudix hydrolase
                     domain"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          30..198
                     /region_name="NUDIX_5"
                     /note="NUDIX, or N-terminal NPxY motif-rich, region of
                     KRIT; pfam16705"
                     /db_xref="CDD:465241"
     Region          172..195
                     /region_name="Interaction with ITGB1BP1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          287..316
                     /region_name="ANK 1. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          <291..>414
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          291..318
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(293..294,297..299,301..302,306,309,318,320,322,
                     326..327,330..332,334..335,339,342,352,354,356,360..361,
                     364..366,368..369,373,376)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          320..352
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          320..350
                     /region_name="ANK 2. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          354..383
                     /region_name="ANK 3. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          388..419
                     /region_name="ANK 4. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          421..640
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          430..452
                     /region_name="Interaction with RAP1B.
                     /evidence=ECO:0000269|PubMed:22577140"
                     /note="propagated from UniProtKB/Swiss-Prot (O00522.2)"
     Region          636..735
                     /region_name="FERM_C_CCM1"
                     /note="FERM domain C-lobe of Cerebral cavernous
                     malformation 1; cd13197"
                     /db_xref="CDD:270018"
     Site            order(650,669,671,677)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270018"
     Site            order(681,686..689,723,727,730..731)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     Site            723..734
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270018"
     CDS             1..736
                     /gene="KRIT1"
                     /gene_synonym="CAM; CCM1"
                     /coded_by="NM_001350690.1:584..2794"
                     /note="isoform 1 is encoded by transcript variant 26"
                     /db_xref="CCDS:CCDS5624.1"
                     /db_xref="GeneID:889"
                     /db_xref="HGNC:HGNC:1573"
                     /db_xref="MIM:604214"
ORIGIN      
        1 mgnpenieda yvavirpknt aslnsreyra ksyeillhev piegqkkkrk kvlletklqg
       61 nseitqgild yvvettkpis panqgirgkr vvlmkkfpld gekmgreasl fivpsvvkdn
      121 tkytytpgcp ifyclqdimr vcsessthfa tltarmlial dkwlderhaq shfipalfrp
      181 spleriktnv inpayatesg qtenslhmgy saleikskml alekadtciy nplfgsdlqy
      241 tnrvdkvvin pyfglgapdy skiqipkqek wqrsmssvte dkerqwvddf plhrsacegd
      301 sellsrllse rfsvnqldsd hwapihyacw ygkveatril lekgkcnpnl lngqlssplh
      361 faaggghaei vqillnhpet drhitdqqgr splniceenk qnnweeaakl lkeainkpye
      421 kvriyrmdgs yrsvelkhgn nttvqqimeg mrlsqetqqy ftiwicsenl slqlkpyhkp
      481 lqhvrdwpei laeltnldpq retpqlflrr dvrlplevek qiedplaili lfdearynll
      541 kgfytapdak litlaslllq ivygnyeskk hkqgflneen lksivpvtkl kskaphwtnr
      601 ilheyknlst segvskemhh lqrmflqncw eiptygaaff tgqiftkasp snhkvipvyv
      661 gvnikglhll nmetkallis lkygcfmwql gdtdtcfqih smenkmsfiv htkqaglvvk
      721 llmklngqlm pterns
//
LOCUS       NP_569122                529 aa            linear   PRI 20-NOV-2025
DEFINITION  dual specificity tyrosine-phosphorylation-regulated kinase 1A
            isoform 5 [Homo sapiens].
ACCESSION   NP_569122
VERSION     NP_569122.1
DBSOURCE    REFSEQ: accession NM_130438.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 529)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 529)
  AUTHORS   Wang,P., Sarkar,S., Zhang,M., Xiao,T., Kong,F., Zhang,Z.,
            Balasubramanian,D., Jayaram,N., Datta,S., He,R., Wu,P., Chao,P.,
            Zhang,Y., Washburn,M., Florens,L.A., Nagarkar-Jaiswal,S.,
            Jaiswal,M. and Mohan,M.
  TITLE     DYRK1A interacts with the tuberous sclerosis complex and promotes
            mTORC1 activity
  JOURNAL   Elife 12, 88318 (2024)
   PUBMED   39436397
  REMARK    GeneRIF: DYRK1A interacts with the tuberous sclerosis complex and
            promotes mTORC1 activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 529)
  AUTHORS   Pastor,F., Charles,E., Di Vona,C., Chapelle,M., Rivoire,M.,
            Passot,G., Chabot,B., de la Luna,S., Lucifora,J., Durantel,D. and
            Salvetti,A.
  TITLE     The dual-specificity kinase DYRK1A interacts with the Hepatitis B
            virus genome and regulates the production of viral RNA
  JOURNAL   PLoS One 19 (10), e0311655 (2024)
   PUBMED   39405283
  REMARK    GeneRIF: The dual-specificity kinase DYRK1A interacts with the
            Hepatitis B virus genome and regulates the production of viral RNA.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 529)
  AUTHORS   Guimera,J., Casas,C., Estivill,X. and Pritchard,M.
  TITLE     Human minibrain homologue (MNBH/DYRK1): characterization,
            alternative splicing, differential tissue expression, and
            overexpression in Down syndrome
  JOURNAL   Genomics 57 (3), 407-418 (1999)
   PUBMED   10329007
REFERENCE   5  (residues 1 to 529)
  AUTHORS   Wang,J., Kudoh,J., Shintani,A., Minoshima,S. and Shimizu,N.
  TITLE     Identification of two novel 5' noncoding exons in human MNB/DYRK
            gene and alternatively spliced transcripts
  JOURNAL   Biochem Biophys Res Commun 250 (3), 704-710 (1998)
   PUBMED   9784410
REFERENCE   6  (residues 1 to 529)
  AUTHORS   Song,W.J., Sternberg,L.R., Kasten-Sportes,C., Keuren,M.L.,
            Chung,S.H., Slack,A.C., Miller,D.E., Glover,T.W., Chiang,P.W.,
            Lou,L. and Kurnit,D.M.
  TITLE     Isolation of human and murine homologues of the Drosophila
            minibrain gene: human homologue maps to 21q22.2 in the Down
            syndrome 'critical region'
  JOURNAL   Genomics 38 (3), 331-339 (1996)
   PUBMED   8975710
REFERENCE   7  (residues 1 to 529)
  AUTHORS   Guimera,J., Casas,C., Pucharcos,C., Solans,A., Domenech,A.,
            Planas,A.M., Ashley,J., Lovett,M., Estivill,X. and Pritchard,M.A.
  TITLE     A human homologue of Drosophila minibrain (MNB) is expressed in the
            neuronal regions affected in Down syndrome and maps to the critical
            region
  JOURNAL   Hum Mol Genet 5 (9), 1305-1310 (1996)
   PUBMED   8872470
REFERENCE   8  (residues 1 to 529)
  AUTHORS   Shindoh,N., Kudoh,J., Maeda,H., Yamaki,A., Minoshima,S., Shimizu,Y.
            and Shimizu,N.
  TITLE     Cloning of a human homolog of the Drosophila minibrain/rat Dyrk
            gene from 'the Down syndrome critical region' of chromosome 21
  JOURNAL   Biochem Biophys Res Commun 225 (1), 92-99 (1996)
   PUBMED   8769099
REFERENCE   9  (residues 1 to 529)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
REFERENCE   10 (residues 1 to 529)
  AUTHORS   van Bon,B.W.M., Coe,B.P., de Vries,B.B.A. and Eichler,E.E.
  TITLE     DYRK1A Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   26677511
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF108830.1 and AP001421.1.
            
            Summary: This gene encodes a member of the Dual-specificity
            tyrosine phosphorylation-regulated kinase (DYRK) family. This
            member contains a nuclear targeting signal sequence, a protein
            kinase domain, a leucine zipper motif, and a highly conservative
            13-consecutive-histidine repeat. It catalyzes its
            autophosphorylation on serine/threonine and tyrosine residues. It
            may play a significant role in a signaling pathway regulating cell
            proliferation and may be involved in brain development. This gene
            is a homolog of Drosophila mnb (minibrain) gene and rat Dyrk gene.
            It is localized in the Down syndrome critical region of chromosome
            21, and is considered to be a strong candidate gene for learning
            defects associated with Down syndrome. Alternative splicing of this
            gene generates several transcript variants differing from each
            other either in the 5' UTR or in the 3' coding region. These
            variants encode at least five different isoforms. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (5) lacks a 3' coding exon, as
            compared to variant 1. It encodes a 234 aa shorter isoform which
            lacks the poly-His domain and has a different C-terminus, compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed/partial sample support SAMEA1965299,
                              SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..529
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..529
                     /product="dual specificity
                     tyrosine-phosphorylation-regulated kinase 1A isoform 5"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.12.1"
                     /note="dual specificity YAK1-related kinase;
                     serine/threonine-specific protein kinase; mnb protein
                     kinase homolog hp86; serine/threonine kinase MNB; MNB/DYRK
                     protein kinase; protein kinase minibrain homolog; dual
                     specificity tyrosine-(Y)-phosphorylation regulated kinase
                     1A"
                     /calculated_mol_wt=60199
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          32..57
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          115..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Region          117..134
                     /region_name="Bipartite nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            140
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          148..484
                     /region_name="PKc_DYRK1"
                     /note="Catalytic domain of the protein kinase,
                     Dual-specificity tYrosine-phosphorylated and -Regulated
                     Kinase 1; cd14226"
                     /db_xref="CDD:271128"
     Site            159
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(165..169,173,186,188,202,222,238..241,244,246..247,
                     287,289,291..292,294,307,310,319,321..324,326,363)
                     /site_type="active"
                     /db_xref="CDD:271128"
     Site            order(165..169,173,186,188,222,238..241,244,287,289,
                     291..292,294,307)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271128"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            order(202,246,287,289,310,319,321..324,326,363)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271128"
     Site            219
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q63470; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            306..326
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271128"
     Site            310
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            321
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Site            402
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     Region          408..442
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13627.2)"
     Site            449
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:23665168; propagated from
                     UniProtKB/Swiss-Prot (Q13627.2)"
     CDS             1..529
                     /gene="DYRK1A"
                     /gene_synonym="DYRK; DYRK1; HP86; MNB; MNBH; MRD7"
                     /coded_by="NM_130438.2:77..1666"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS13654.1"
                     /db_xref="GeneID:1859"
                     /db_xref="HGNC:HGNC:3091"
                     /db_xref="MIM:600855"
ORIGIN      
        1 mhtggetsac kpssvrlaps fsfhaaglqm agqmphshqy sdrrqpnisd qqvsalsysd
       61 qiqqpltnqv mpdivmlqrr mpqtfrdpat aplrklsvdl iktykhinev yyakkkrrhq
      121 qgqgddsshk kerkvyndgy dddnydyivk ngekwmdrye idsligkgsf gqvvkaydrv
      181 eqewvaikii knkkaflnqa qievrllelm nkhdtemkyy ivhlkrhfmf rnhlclvfem
      241 lsynlydllr ntnfrgvsln ltrkfaqqmc tallflatpe lsiihcdlkp enillcnpkr
      301 saikivdfgs scqlgqriyq yiqsrfyrsp evllgmpydl aidmwslgci lvemhtgepl
      361 fsganevdqm nkivevlgip pahildqapk arkffeklpd gtwnlkktkd gkreykppgt
      421 rklhnilgve tggpggrrag esghtvadyl kfkdlilrml dydpktriqp yyalqhsffk
      481 ktadegtnts nsvstspame qsqssgttss tssssgasai scsswlvrh
//
LOCUS       NP_001230665             117 aa            linear   PRI 20-NOV-2025
DEFINITION  ragulator complex protein LAMTOR3 isoform 2 [Homo sapiens].
ACCESSION   NP_001230665
VERSION     NP_001230665.1
DBSOURCE    REFSEQ: accession NM_001243736.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 117)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 117)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   3  (residues 1 to 117)
  AUTHORS   Trepte,P., Secker,C., Kostova,S., Maseko,S.B., Choi,S.G.,
            Blavier,J., Minia,I., Ramos,E.S., Cassonnet,P., Golusik,S.,
            Zenkner,M., Beetz,S., Liebich,M.J., Scharek,N., Schutz,A.,
            Sperling,M., Lisurek,M., Wang,Y., Spirohn,K., Hao,T.,
            Calderwood,M.A., Hill,D.E., Landthaler,M., Olivet,J., Twizere,J.C.,
            Vidal,M. and Wanker,E.E.
  TITLE     AI-guided pipeline for protein-protein interaction drug discovery
            identifies a SARS-CoV-2 inhibitor
  JOURNAL   bioRxiv (2023)
   PUBMED   37398436
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 117)
  AUTHORS   Jansen,R.M., Peruzzo,R., Fromm,S.A., Yokom,A.L., Zoncu,R. and
            Hurley,J.H.
  TITLE     Structural basis for FLCN RagC GAP activation in MiT-TFE
            substrate-selective mTORC1 regulation
  JOURNAL   Sci Adv 8 (37), eadd2926 (2022)
   PUBMED   36103527
REFERENCE   5  (residues 1 to 117)
  AUTHORS   Gong,Y., Lv,Y., Xu,F., Xiu,Y., Lu,Y., Liu,Z. and Deng,L.
  TITLE     LAMTOR3 is a prognostic biomarker in kidney renal clear cell
            carcinoma
  JOURNAL   J Clin Lab Anal 36 (9), e24648 (2022)
   PUBMED   36082464
  REMARK    GeneRIF: LAMTOR3 is a prognostic biomarker in kidney renal clear
            cell carcinoma.
REFERENCE   6  (residues 1 to 117)
  AUTHORS   Lunin,V.V., Munger,C., Wagner,J., Ye,Z., Cygler,M. and Sacher,M.
  TITLE     The structure of the MAPK scaffold, MP1, bound to its partner, p14.
            A complex with a critical role in endosomal map kinase signaling
  JOURNAL   J Biol Chem 279 (22), 23422-23430 (2004)
   PUBMED   15016825
REFERENCE   7  (residues 1 to 117)
  AUTHORS   Paces-Fessy,M., Boucher,D., Petit,E., Paute-Briand,S. and
            Blanchet-Tournier,M.F.
  TITLE     The negative regulator of Gli, Suppressor of fused (Sufu),
            interacts with SAP18, Galectin3 and other nuclear proteins
  JOURNAL   Biochem J 378 (Pt 2), 353-362 (2004)
   PUBMED   14611647
REFERENCE   8  (residues 1 to 117)
  AUTHORS   Teis,D., Wunderlich,W. and Huber,L.A.
  TITLE     Localization of the MP1-MAPK scaffold complex to endosomes is
            mediated by p14 and required for signal transduction
  JOURNAL   Dev Cell 3 (6), 803-814 (2002)
   PUBMED   12479806
REFERENCE   9  (residues 1 to 117)
  AUTHORS   Wunderlich,W., Fialka,I., Teis,D., Alpi,A., Pfeifer,A.,
            Parton,R.G., Lottspeich,F. and Huber,L.A.
  TITLE     A novel 14-kilodalton protein interacts with the mitogen-activated
            protein kinase scaffold mp1 on a late endosomal/lysosomal
            compartment
  JOURNAL   J Cell Biol 152 (4), 765-776 (2001)
   PUBMED   11266467
REFERENCE   10 (residues 1 to 117)
  AUTHORS   Schaeffer,H.J., Catling,A.D., Eblen,S.T., Collier,L.S., Krauss,A.
            and Weber,M.J.
  TITLE     MP1: a MEK binding partner that enhances enzymatic activation of
            the MAP kinase cascade
  JOURNAL   Science 281 (5383), 1668-1671 (1998)
   PUBMED   9733512
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI562630.1, AL544981.3 and
            AP001962.2.
            
            Summary: This gene encodes a scaffold protein that functions in the
            extracellular signal-regulated kinase (ERK) cascade. The protein is
            localized to late endosomes by the mitogen-activated
            protein-binding protein-interacting protein, and binds specifically
            to MAP kinase kinase MAP2K1/MEK1, MAP kinase MAPK3/ERK1, and MAP
            kinase MAPK1/ERK2. Studies of the orthologous gene in mouse
            indicate that it regulates late endosomal traffic and cell
            proliferation. Alternatively spliced transcript variants encoding
            multiple isoforms have been observed for this gene. A pseudogene of
            this gene is located on the long arm of chromosome 13. [provided by
            RefSeq, Aug 2011].
            
            Transcript Variant: This variant (3) uses an alternate splice site
            in the coding region, but maintains the reading frame, compared to
            variant 1. The encoded isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL544981.3 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..117
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q23"
     Protein         1..117
                     /product="ragulator complex protein LAMTOR3 isoform 2"
                     /note="MAPK scaffold protein 1; mitogen-activated protein
                     kinase kinase 1 interacting protein 1; MEK binding partner
                     1; mitogen-activated protein kinase scaffold protein 1;
                     ragulator complex protein LAMTOR3; late
                     endosomal/lysosomal adaptor and MAPK and MTOR activator 3"
                     /calculated_mol_wt=12810
     Region          3..114
                     /region_name="MAPKK1_Int"
                     /note="Mitogen-activated protein kinase kinase 1
                     interacting; pfam08923"
                     /db_xref="CDD:462635"
     CDS             1..117
                     /gene="LAMTOR3"
                     /gene_synonym="MAP2K1IP1; MAPBP; MAPKSP1; MP1; PRO0633;
                     Ragulator3"
                     /coded_by="NM_001243736.1:250..603"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58920.1"
                     /db_xref="GeneID:8649"
                     /db_xref="HGNC:HGNC:15606"
                     /db_xref="MIM:603296"
ORIGIN      
        1 maddlkrfly kklpsveglh aivvsdrdgv pvikehalrp gflstfalat dqgsklglsk
       61 nksiicyynt yqvvqfnrlp lvvsfiasss antglivsle kelaplfeel rqvvevs
//
LOCUS       NP_919339                246 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase NRDP1 isoform 2 [Homo sapiens].
ACCESSION   NP_919339
VERSION     NP_919339.1
DBSOURCE    REFSEQ: accession NM_194358.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 246)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 246)
  AUTHORS   Xiong,S., Li,S., Li,Z., Song,Y., Yang,L., Yang,H., Xiong,J.,
            Pan,W., Guo,J., Fu,B. and Xu,S.
  TITLE     A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C stability
            promotes prostate cancer metastasis by inducing actin remodeling
  JOURNAL   Oncogene 43 (36), 2696-2707 (2024)
   PUBMED   39112516
  REMARK    GeneRIF: A noncanonical E3 ubiquitin ligase RNF41-mediated MYO1C
            stability promotes prostate cancer metastasis by inducing actin
            remodeling.
REFERENCE   3  (residues 1 to 246)
  AUTHORS   Li,Q.Q., Guo,M., He,G.H., Xi,K.H., Zhou,M.Y., Shi,R.Y. and
            Chen,G.Q.
  TITLE     VEGF-induced Nrdp1 deficiency in vascular endothelial cells
            promotes cancer metastasis by degrading vascular basement membrane
  JOURNAL   Oncogene 43 (24), 1836-1851 (2024)
   PUBMED   38654108
  REMARK    GeneRIF: VEGF-induced Nrdp1 deficiency in vascular endothelial
            cells promotes cancer metastasis by degrading vascular basement
            membrane.
REFERENCE   4  (residues 1 to 246)
  AUTHORS   Zong,C.Y., Ji,Q.Q., Chen,F.F., Yang,J.J., Zhou,H., Zhu,B.F. and
            Zhou,G.X.
  TITLE     Correlation between neuregulin receptor degradation protein-1 and
            Crohn's disease
  JOURNAL   J Physiol Pharmacol 75 (1) (2024)
   PUBMED   38583443
  REMARK    GeneRIF: Correlation between neuregulin receptor degradation
            protein-1 and Crohn's disease.
REFERENCE   5  (residues 1 to 246)
  AUTHORS   Zeng,W., Zhu,J.F., Guo,J., Huang,G.J., Ai,L.S., Zeng,Y. and
            Liao,W.J.
  TITLE     m6A-modified circFNDC3B inhibits colorectal cancer stemness and
            metastasis via RNF41-dependent ASB6 degradation
  JOURNAL   Cell Death Dis 13 (11), 1008 (2022)
   PUBMED   36446779
  REMARK    GeneRIF: m[6]A-modified circFNDC3B inhibits colorectal cancer
            stemness and metastasis via RNF41-dependent ASB6 degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 246)
  AUTHORS   Brajenovic,M., Joberty,G., Kuster,B., Bouwmeester,T. and Drewes,G.
  TITLE     Comprehensive proteomic analysis of human Par protein complexes
            reveals an interconnected protein network
  JOURNAL   J Biol Chem 279 (13), 12804-12811 (2004)
   PUBMED   14676191
REFERENCE   7  (residues 1 to 246)
  AUTHORS   Qiu,X.B., Markant,S.L., Yuan,J. and Goldberg,A.L.
  TITLE     Nrdp1-mediated degradation of the gigantic IAP, BRUCE, is a novel
            pathway for triggering apoptosis
  JOURNAL   EMBO J 23 (4), 800-810 (2004)
   PUBMED   14765125
  REMARK    GeneRIF: Nrdp1 can be important in the initiation of apoptosis by
            catalyzing ubiquitination and degradation of BRUCE.
REFERENCE   8  (residues 1 to 246)
  AUTHORS   Qiu,X.B. and Goldberg,A.L.
  TITLE     Nrdp1/FLRF is a ubiquitin ligase promoting ubiquitination and
            degradation of the epidermal growth factor receptor family member,
            ErbB3
  JOURNAL   Proc Natl Acad Sci U S A 99 (23), 14843-14848 (2002)
   PUBMED   12411582
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):17220.]
REFERENCE   9  (residues 1 to 246)
  AUTHORS   Diamonti,A.J., Guy,P.M., Ivanof,C., Wong,K., Sweeney,C. and
            Carraway,K.L. 3rd.
  TITLE     An RBCC protein implicated in maintenance of steady-state
            neuregulin receptor levels
  JOURNAL   Proc Natl Acad Sci U S A 99 (5), 2866-2871 (2002)
   PUBMED   11867753
REFERENCE   10 (residues 1 to 246)
  AUTHORS   Abdullah,J.M., Li,X., Nachtman,R.G. and Jurecic,R.
  TITLE     FLRF, a novel evolutionarily conserved RING finger gene, is
            differentially expressed in mouse fetal and adult hematopoietic
            stem cells and progenitors
  JOURNAL   Blood Cells Mol Dis 27 (1), 320-333 (2001)
   PUBMED   11358394
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB989647.1, BC024284.1 and
            AC073896.41.
            
            Summary: This gene encodes an E3 ubiquitin ligase. The encoded
            protein plays a role in type 1 cytokine receptor signaling by
            controlling the balance between JAK2-associated cytokine receptor
            degradation and ectodomain shedding. Alternative splicing results
            in multiple transcript variants. [provided by RefSeq, Jun 2011].
            
            Transcript Variant: This variant (2) includes an alternate exon in
            the 5' region and uses a downstream start codon compared to variant
            1. The resulting isoform (2) has a shorter N-terminus compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1577908.1,
                                           SRR14038192.1231141.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..246
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..246
                     /product="E3 ubiquitin-protein ligase NRDP1 isoform 2"
                     /EC_number="2.3.2.27"
                     /note="neuregulin receptor degradation protein-1; fetal
                     liver ring finger; E3 ubiquitin-protein ligase NRDP1; ring
                     finger protein 41, E3 ubiquitin protein ligase; RING-type
                     E3 ubiquitin transferase NRDP1"
                     /calculated_mol_wt=27834
     Region          6..>90
                     /region_name="Sina"
                     /note="Seven in absentia protein family; pfam03145"
                     /db_xref="CDD:460824"
     Region          66..244
                     /region_name="USP8_interact"
                     /note="USP8 interacting; pfam08941"
                     /db_xref="CDD:430333"
     CDS             1..246
                     /gene="RNF41"
                     /gene_synonym="FLRF; NRDP1; SBBI03"
                     /coded_by="NM_194358.3:728..1468"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS8910.1"
                     /db_xref="GeneID:10193"
                     /db_xref="HGNC:HGNC:18401"
                     /db_xref="MIM:620051"
ORIGIN      
        1 mrnmlsklqi acdnavfgcs avvrldnlms hlsdcehnpk rpvtceqgcg lempkdelpn
       61 hncikhlrsv vqqqqtriae lektsaehkh qlaeqkrdiq llkaymrair svnpnlqnle
      121 etieyneile wvnslqparv trwggmistp davlqavikr slvesgcpas ivnelienah
      181 erswpqglat letrqmnrry yenyvakrip gkqavvvmac enqhmgddmv qepglvmifa
      241 hgveei
//
LOCUS       NP_001238898              77 aa            linear   PRI 20-NOV-2025
DEFINITION  proton-coupled zinc antiporter SLC30A5 isoform 3 [Homo sapiens].
ACCESSION   NP_001238898
VERSION     NP_001238898.1
DBSOURCE    REFSEQ: accession NM_001251969.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 77)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 77)
  AUTHORS   Wagatsuma,T., Shimotsuma,K., Sogo,A., Sato,R., Kubo,N., Ueda,S.,
            Uchida,Y., Kinoshita,M. and Kambe,T.
  TITLE     Zinc transport via ZNT5-6 and ZNT7 is critical for cell surface
            glycosylphosphatidylinositol-anchored protein expression
  JOURNAL   J Biol Chem 298 (6), 102011 (2022)
   PUBMED   35525268
REFERENCE   3  (residues 1 to 77)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 77)
  AUTHORS   Lieberwirth,J.K., Joset,P., Heinze,A., Hentschel,J., Stein,A.,
            Iannaccone,A., Steindl,K., Kuechler,A. and Abou Jamra,R.
  TITLE     Bi-allelic loss of function variants in SLC30A5 as cause of
            perinatal lethal cardiomyopathy
  JOURNAL   Eur J Hum Genet 29 (5), 808-815 (2021)
   PUBMED   33547425
  REMARK    GeneRIF: Bi-allelic loss of function variants in SLC30A5 as cause
            of perinatal lethal cardiomyopathy.
            Erratum:[Eur J Hum Genet. 2021 May;29(5):887. doi:
            10.1038/s41431-021-00843-8. PMID: 33750920]
REFERENCE   5  (residues 1 to 77)
  AUTHORS   Falcon-Perez,J.M. and Dell'Angelica,E.C.
  TITLE     Zinc transporter 2 (SLC30A2) can suppress the vesicular zinc defect
            of adaptor protein 3-depleted fibroblasts by promoting zinc
            accumulation in lysosomes
  JOURNAL   Exp Cell Res 313 (7), 1473-1483 (2007)
   PUBMED   17349999
REFERENCE   6  (residues 1 to 77)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Ishihara,K., Nagao,M.,
            Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Two different zinc transport complexes of cation diffusion
            facilitator proteins localized in the secretory pathway operate to
            activate alkaline phosphatases in vertebrate cells
  JOURNAL   J Biol Chem 280 (35), 30956-30962 (2005)
   PUBMED   15994300
REFERENCE   7  (residues 1 to 77)
  AUTHORS   Suzuki,T., Ishihara,K., Migaki,H., Matsuura,W., Kohda,A.,
            Okumura,K., Nagao,M., Yamaguchi-Iwai,Y. and Kambe,T.
  TITLE     Zinc transporters, ZnT5 and ZnT7, are required for the activation
            of alkaline phosphatases, zinc-requiring enzymes that are
            glycosylphosphatidylinositol-anchored to the cytoplasmic membrane
  JOURNAL   J Biol Chem 280 (1), 637-643 (2005)
   PUBMED   15525635
REFERENCE   8  (residues 1 to 77)
  AUTHORS   Devergnas,S., Chimienti,F., Naud,N., Pennequin,A., Coquerel,Y.,
            Chantegrel,J., Favier,A. and Seve,M.
  TITLE     Differential regulation of zinc efflux transporters ZnT-1, ZnT-5
            and ZnT-7 gene expression by zinc levels: a real-time RT-PCR study
  JOURNAL   Biochem Pharmacol 68 (4), 699-709 (2004)
   PUBMED   15276077
REFERENCE   9  (residues 1 to 77)
  AUTHORS   Cragg,R.A., Christie,G.R., Phillips,S.R., Russi,R.M., Kury,S.,
            Mathers,J.C., Taylor,P.M. and Ford,D.
  TITLE     A novel zinc-regulated human zinc transporter, hZTL1, is localized
            to the enterocyte apical membrane
  JOURNAL   J Biol Chem 277 (25), 22789-22797 (2002)
   PUBMED   11937503
  REMARK    GeneRIF: A novel zinc-regulated human zinc transporter, hZTL1, is
            localized to the enterocyte apical membrane
REFERENCE   10 (residues 1 to 77)
  AUTHORS   Kambe,T., Narita,H., Yamaguchi-Iwai,Y., Hirose,J., Amano,T.,
            Sugiura,N., Sasaki,R., Mori,K., Iwanaga,T. and Nagao,M.
  TITLE     Cloning and characterization of a novel mammalian zinc transporter,
            zinc transporter 5, abundantly expressed in pancreatic beta cells
  JOURNAL   J Biol Chem 277 (21), 19049-19055 (2002)
   PUBMED   11904301
  REMARK    GeneRIF: cloning and characterization of ZnT-5 which is expressed
            in pancreatic beta cells
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB090660.1, BC144349.1 and
            BC017441.1.
            
            Summary: This gene encodes a member of the SLC30A/ZnT family of
            zinc transporter proteins. ZnT proteins mediate both cellular zinc
            efflux and zinc sequestration into membrane-bound organelles. The
            encoded protein plays a role in the early secretory pathway as a
            heterodimer with zinc transporter 6, and may also regulate zinc
            sequestration into secretory granules of pancreatic beta cells.
            Alternatively spliced transcript variants encoding multiple
            isoforms have been observed for this gene, and a pseudogene of this
            gene is located on the long arm of chromosome 19. [provided by
            RefSeq, Oct 2011].
            
            Transcript Variant: This variant (3) lacks an exon in the 5' coding
            region, differs in the 3' UTR and lacks a large portion of the
            coding region, compared to variant 1. The encoded isoform (3) is
            significantly shorter and has a distinct C-terminus, compared to
            isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138512.556270.1, BC144349.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..77
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.1-q13.2"
     Protein         1..77
                     /product="proton-coupled zinc antiporter SLC30A5 isoform
                     3"
                     /note="zinc transporter ZTL1; znT-like transporter 1;
                     solute carrier family 30 (zinc transporter), member 5;
                     proton-coupled zinc antiporter SLC30A5"
                     /calculated_mol_wt=8084
     CDS             1..77
                     /gene="SLC30A5"
                     /gene_synonym="ZnT-5; ZNT5; ZNTL1; ZTL1"
                     /coded_by="NM_001251969.2:243..476"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS58955.1"
                     /db_xref="GeneID:64924"
                     /db_xref="HGNC:HGNC:19089"
                     /db_xref="MIM:607819"
ORIGIN      
        1 meekyggdvl agpggggglg pvdvpsarta ffmvlfqkpf ssgktitkhq iigslkipgr
       61 kefkdkklnd prklvgn
//
LOCUS       NP_001339876             665 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 18 [Homo sapiens].
ACCESSION   NP_001339876
VERSION     NP_001339876.1
DBSOURCE    REFSEQ: accession NM_001352947.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 665)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 665)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 665)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 665)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 665)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 665)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 665)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 665)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 665)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 665)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            Transcript Variant: This variant (22), as well as variants 21 and
            23, encodes isoform 18.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.216666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03465410, SAMN03465414
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..665
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..665
                     /product="DNA repair-scaffolding protein isoform 18"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=72443
     Region          <5..119
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          271..655
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..665
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352947.1:594..2591"
                     /note="isoform 18 is encoded by transcript variant 22"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mrscrsfprg glaerlnglq nrersaislw rhqcisyqkt lsgrksgvlt vkilelheec
       61 amqvamceql lgspatsssq svaprpgagl kvlftketag ylrgrpqdtv rifppwqkli
      121 ipsgscpvil ntyfcekvva kedsektcev ycpdiplprr sislaqmfvi kgltnnspei
      181 qvvcsgvatt gtawthghke akqriptstp lrdslldvve sqgaaswpga gvrvvvqrvy
      241 slpsrdstrg qqgassghtd pagtracllv qdacgmfgev hleftmskar qlegkscslv
      301 gmkvlqkvtr grtagifsli dtlwppaipl ktpgrdqpce eikthlpppa lcyiltahpn
      361 lgqidiided piyklyqppv trclrdilqm ndlgtrcsfy atviyqkpql kslllleqre
      421 iwllvtdvtl qtkeerdprl pktllvyvap lcvlgsevle alagaaphsl ffkdalrdqg
      481 rivcaertvl llqkpllsvv sgasscelpg pvmldsldsa tpvnsicsvq gtvvgvdest
      541 afswpvcdmc gngrleqrpe drgafscgdc srvvtspvlk rhlqvfldcr srpqcrvkvk
      601 llqrsissll rfaagedgsy evksvlgkev gllncfvqsv tahptscigl eeiellsagg
      661 asaeh
//
LOCUS       NP_054735                587 aa            linear   PRI 20-NOV-2025
DEFINITION  phosphatidylinositol-3-phosphatase SAC1 isoform 1 [Homo sapiens].
ACCESSION   NP_054735
VERSION     NP_054735.3
DBSOURCE    REFSEQ: accession NM_014016.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Frommelt,F., Ladurner,R., Goldmann,U., Wolf,G., Ingles-Prieto,A.,
            Lineiro-Retes,E., Gelova,Z., Hopp,A.K., Christodoulaki,E.,
            Teoh,S.T., Leippe,P., Santini,B.L., Rebsamen,M., Lindinger,S.,
            Serrano,I., Onstein,S., Klimek,C., Barbosa,B., Pantielieieva,A.,
            Dvorak,V., Hannich,T.J., Schoenbett,J., Sansig,G., Mocking,T.A.M.,
            Ooms,J.F., IJzerman,A.P., Heitman,L.H., Sykacek,P., Reinhardt,J.,
            Muller,A.C., Wiedmer,T. and Superti-Furga,G.
  TITLE     The solute carrier superfamily interactome
  JOURNAL   Mol Syst Biol 21 (6), 632-675 (2025)
   PUBMED   40355756
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Popescu,M.A., Patriche,D., Dobrica,M.O., Pantazica,A.M., Flintoaca
            Alexandru,P.R., Rouille,Y., Popescu,C.I. and Branza-Nichita,N.
  TITLE     Sac1 phosphatidylinositol 4-phosphate phosphatase is a novel host
            cell factor regulating hepatitis B virus particles assembly and
            release
  JOURNAL   FEBS J 289 (23), 7486-7499 (2022)
   PUBMED   35816160
  REMARK    GeneRIF: Sac1 phosphatidylinositol 4-phosphate phosphatase is a
            novel host cell factor regulating hepatitis B virus particles
            assembly and release.
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Loughran,G., Chou,M.Y., Ivanov,I.P., Jungreis,I., Kellis,M.,
            Kiran,A.M., Baranov,P.V. and Atkins,J.F.
  TITLE     Evidence of efficient stop codon readthrough in four mammalian
            genes
  JOURNAL   Nucleic Acids Res 42 (14), 8928-8938 (2014)
   PUBMED   25013167
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Liu,Y., Boukhelifa,M., Tribble,E., Morin-Kensicki,E., Uetrecht,A.,
            Bear,J.E. and Bankaitis,V.A.
  TITLE     The Sac1 phosphoinositide phosphatase regulates Golgi membrane
            morphology and mitotic spindle organization in mammals
  JOURNAL   Mol Biol Cell 19 (7), 3080-3096 (2008)
   PUBMED   18480408
  REMARK    GeneRIF: Sac1 executes an essential household function in mammals
            that involves organization of both Golgi membranes and mitotic
            spindles
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Rohde,H.M., Cheong,F.Y., Konrad,G., Paiha,K., Mayinger,P. and
            Boehmelt,G.
  TITLE     The human phosphatidylinositol phosphatase SAC1 interacts with the
            coatomer I complex
  JOURNAL   J Biol Chem 278 (52), 52689-52699 (2003)
   PUBMED   14527956
  REMARK    GeneRIF: the enzymatic function of hSAC1 provides a switch for
            accessibility of the COPI interaction motif
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Kiss,H., Kedra,D., Kiss,C., Kost-Alimova,M., Yang,Y., Klein,G.,
            Imreh,S. and Dumanski,J.P.
  TITLE     The LZTFL1 gene is a part of a transcriptional map covering 250 kb
            within the common eliminated region 1 (C3CER1) in 3p21.3
  JOURNAL   Genomics 73 (1), 10-19 (2001)
   PUBMED   11352561
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Nemoto,Y., Kearns,B.G., Wenk,M.R., Chen,H., Mori,K., Alb,J.G. Jr.,
            De Camilli,P. and Bankaitis,V.A.
  TITLE     Functional characterization of a mammalian Sac1 and mutants
            exhibiting substrate-specific defects in phosphoinositide
            phosphatase activity
  JOURNAL   J Biol Chem 275 (44), 34293-34305 (2000)
   PUBMED   10887188
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC322649.1, AB020658.1 and
            CA335989.1.
            
            On Jun 11, 2008 this sequence version replaced NP_054735.2.
            
            Summary: This gene encodes an integral membrane protein, which is
            localized to the endoplasmic reticulum, and functions as a
            phosphoinositide phosphatase that hydrolyzes phosphatidylinositol
            3-phosphate, phosphatidylinositol 4-phosphate, and
            phosphatidylinositol 3,5-bisphosphate. Deletion of this gene in
            mouse results in preimplantation lethality. Other studies suggest
            that this gene is also involved in the organization of golgi
            membranes and mitotic spindles. Alternatively spliced transcript
            variants have been found for this gene. A C-terminally extended
            isoform is also predicted to be produced by the use of an
            alternative in-frame, downstream translation termination codon via
            a stop codon readthrough mechanism.[provided by RefSeq, Dec 2017].
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes two isoforms, which result from the use of
            alternative in-frame translation termination codons. The shorter
            isoform (1) results from translation termination at the upstream
            UGA stop codon, while the longer isoform (1x) results from UGA stop
            codon readthrough to the downstream UGA termination codon. This
            RefSeq represents the shorter isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.276687.1,
                                           SRR1660809.52292.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000389061.10/ ENSP00000373713.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..587
                     /product="phosphatidylinositol-3-phosphatase SAC1 isoform
                     1"
                     /EC_number="3.1.3.64"
                     /note="suppressor of actin 1; phosphatidylinositide
                     phosphatase SAC1; suppressor of actin mutations 1-like
                     protein; SAC1 suppressor of actin mutations 1 like;
                     phosphatidylinositol-4-phosphate phosphatase;
                     phosphatidylinositol-3-phosphatase SAC1"
                     /calculated_mol_wt=66836
     Region          57..513
                     /region_name="COG5329"
                     /note="Phosphoinositide polyphosphatase (Sac family)
                     [Signal transduction mechanisms]"
                     /db_xref="CDD:227637"
     Region          452..587
                     /region_name="Essential for
                     phosphatidylinositol-4-phosphate phosphatase activity.
                     /evidence=ECO:0000269|PubMed:29461204"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTJ5.2)"
     Site            456
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NTJ5.2)"
     Site            521..541
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTJ5.2)"
     Site            549..569
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NTJ5.2)"
     CDS             1..587
                     /gene="SACM1L"
                     /gene_synonym="SAC1"
                     /coded_by="NM_014016.5:71..1834"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS33745.1"
                     /db_xref="GeneID:22908"
                     /db_xref="HGNC:HGNC:17059"
                     /db_xref="MIM:606569"
ORIGIN      
        1 mataayeqlk lhitpekfyv eacddgaddv ltidrvstev tlavkkdvpp savtrpifgi
       61 lgtihlvagn ylivitkkik vgeffshvvw katdfdvlsy kktmlhltdi qlqdnktfla
      121 mlnhvlnvdg fyfsttydlt htlqrlsnts pefqemslle radqrfvwng hllrelsaqp
      181 evhrfalpvl hgfitmhscs ingkyfdwil isrrscfrag vryyvrgids eghaanfvet
      241 eqivhyngsk asfvqtrgsi pvfwsqrpnl kykplpqisk vanhmdgfqr hfdsqviiyg
      301 kqviinlinq kgsekpleqt fatmvsslgs gmmryiafdf hkecknmrwd rlsilldqva
      361 emqdelsyfl vdsagqvvan qegvfrsncm dcldrtnviq sllarrslqa qlqrlgvlhv
      421 gqkleeqdef ekiyknawad nanacakqya gtgalktdft rtgkrthlgl imdgwnsmir
      481 yyknnfsdgf rqdsidlflg nysvdelesh splsvprdwk flalpiimvv afsmciicll
      541 magdtwtetl ayvlfwgvas igtffiilyn gkdfvdaprl vqkekid
//
LOCUS       NP_997186               1379 aa            linear   PRI 20-NOV-2025
DEFINITION  attractin-like protein 1 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_997186
VERSION     NP_997186.1
DBSOURCE    REFSEQ: accession NM_207303.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1379)
  AUTHORS   Fang,M., Zhou,Y., Li,Z. and Li,X.
  TITLE     Transcriptional factor CCAAT enhancer binding protein beta inhibits
            epithelial-mesenchymal transition in cervical cancer via regulating
            attractin-like 1
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 69 (13), 1-7 (2023)
   PUBMED   38158696
  REMARK    GeneRIF: Transcriptional factor CCAAT enhancer binding protein beta
            inhibits epithelial-mesenchymal transition in cervical cancer via
            regulating attractin-like 1.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1379)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1379)
  AUTHORS   Luciano,M., Hansell,N.K., Lahti,J., Davies,G., Medland,S.E.,
            Raikkonen,K., Tenesa,A., Widen,E., McGhee,K.A., Palotie,A.,
            Liewald,D., Porteous,D.J., Starr,J.M., Montgomery,G.W.,
            Martin,N.G., Eriksson,J.G., Wright,M.J. and Deary,I.J.
  TITLE     Whole genome association scan for genetic polymorphisms influencing
            information processing speed
  JOURNAL   Biol Psychol 86 (3), 193-202 (2011)
   PUBMED   21130836
REFERENCE   4  (residues 1 to 1379)
  AUTHORS   Cota,C.D., Liu,R.R., Sumberac,T.M., Jung,S., Vencato,D.,
            Millet,Y.H. and Gunn,T.M.
  TITLE     Genetic and phenotypic studies of the dark-like mutant mouse
  JOURNAL   Genesis 46 (10), 562-573 (2008)
   PUBMED   18821597
  REMARK    GeneRIF: Transgenic overexpression of Attractin-like-1 (Atrnl1),
            which compensates for loss of ATRN, does not rescue dark-like
            mutant phenotypes.
REFERENCE   5  (residues 1 to 1379)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 1379)
  AUTHORS   Haqq,A.M., Rene,P., Kishi,T., Khong,K., Lee,C.E., Liu,H.,
            Friedman,J.M., Elmquist,J.K. and Cone,R.D.
  TITLE     Characterization of a novel binding partner of the melanocortin-4
            receptor: attractin-like protein
  JOURNAL   Biochem J 376 (Pt 3), 595-605 (2003)
   PUBMED   14531729
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC035157.1, AY442317.1 and AC022542.5.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.231188.1,
                                           SRR1660809.112260.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355044.8/ ENSP00000347152.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1379
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q25.3"
     Protein         1..1379
                     /product="attractin-like protein 1 isoform 1 precursor"
                     /note="attractin-like protein 1"
                     /calculated_mol_wt=147349
     sig_peptide     1..52
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
                     /calculated_mol_wt=5309
     Region          1..23
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     mat_peptide     53..1379
                     /product="Attractin-like protein 1. /id=PRO_0000334650"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
                     /calculated_mol_wt=147349
     Site            76
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          93..208
                     /region_name="CUB"
                     /note="CUB domain; extracellular domain; present in
                     proteins mostly known to be involved in development; not
                     found in prokaryotes, plants and yeast; cd00041"
                     /db_xref="CDD:238001"
     Site            order(103,105,107,132,137,179,203,205,207..208)
                     /site_type="other"
                     /note="heterodimerization interface [polypeptide binding]"
                     /db_xref="CDD:238001"
     Site            174
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Site            198
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          235..281
                     /region_name="DSL"
                     /note="Delta serrate ligand; cl19567"
                     /db_xref="CDD:473190"
     Region          303..598
                     /region_name="NanM"
                     /note="N-acetylneuraminic acid mutarotase [Cell
                     wall/membrane/envelope biogenesis]; COG3055"
                     /db_xref="CDD:442289"
     Region          305..349
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          316..365
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          355..408
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          367..415
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Site            380
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          427..475
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          480..531
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          521..574
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          533..591
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          592..638
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          748..874
                     /region_name="CLECT_attractin_like"
                     /note="C-type lectin-like domain (CTLD) of the type found
                     in human and mouse attractin (AtrN) and attractin-like
                     protein (ALP); cd03597"
                     /db_xref="CDD:153067"
     Site            763
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Site            778
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Site            order(845,849,851,857,859..862,866..868)
                     /site_type="other"
                     /note="ligand binding surface [chemical binding]"
                     /db_xref="CDD:153067"
     Region          889..938
                     /region_name="PSI"
                     /note="Plexin repeat; pfam01437"
                     /db_xref="CDD:396154"
     Site            898
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          1013..1058
                     /region_name="EGF_Lam"
                     /note="Laminin-type epidermal growth factor-like domain;
                     laminins are the major noncollagenous components of
                     basement membranes that mediate cell adhesion, growth
                     migration, and differentiation; the laminin-type epidermal
                     growth factor-like module occurs in...; cd00055"
                     /db_xref="CDD:238012"
     Site            order(1014,1016,1028,1031,1040)
                     /site_type="active"
                     /note="EGF-like motif [active]"
                     /db_xref="CDD:238012"
     Site            1157
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q5VV63.2)"
     Site            1231..1251
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     Region          1354..1379
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5VV63.2)"
     CDS             1..1379
                     /gene="ATRNL1"
                     /gene_synonym="ALP; bA338L11.1; bA454H24.1"
                     /coded_by="NM_207303.4:387..4526"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7592.1"
                     /db_xref="GeneID:26033"
                     /db_xref="HGNC:HGNC:29063"
                     /db_xref="MIM:612869"
ORIGIN      
        1 metggrartg tpqpaapgvw rarpaggggg gasswlldgn swllcygfly lalyaqvsqs
       61 kpcertgscf sgrcvnstcl cdpgwvgdqc qhcqgrfklt epsgyltdgp inykyktkct
      121 wliegypnav lrlrfnhfat ecswdhmyvy dgdsiyapli avlsglivpe irgnetvpev
      181 vttsgyallh ffsdaaynlt gfnifysins cpnncsghgk cttsvsvpsq vycecdkywk
      241 geacdipyck ancgspdhgy cdltgeklcv cndswqgpdc slnvpstesy wilpnvkpfs
      301 psvgrashka vlhgkfmwvi ggytfnyssf qmvlnynles siwnvgtpsr gplqryghsl
      361 alyqenifmy ggrietndgn vtdelwvfni hsqswstktp tvlghgqqya veghsahime
      421 ldsrdvvmii ifgysaiygy tssiqeyhis sntwlvpetk gaivqggygh tsvydeitks
      481 iyvhggykal pgnkyglvdd lykyevntkt wtilkesgfa rylhsavlin gamlifggnt
      541 hndtslsnga kcfsadflay diacdewkil pkpnlhrdvn rfghsavvin gsmyifggfs
      601 svllndilvy kppnckafrd eelcknagpg ikcvwnknhc eswesgntnn ilrakcppkt
      661 aasddrcyry adcasctant ngcqwcddkk cisansncsm svknytkchv rneqicnklt
      721 sckscslnln cqwdqrqqec qalpahlcge gwshigdacl rvnssrenyd naklycynls
      781 gnlaslttsk evefvldeiq kytqqkvspw vglrkinisy wgwedmspft nttlqwlpge
      841 pndsgfcayl eraavaglka npctsmangl vcekpvvspn qnarpckkpc slrtscsnct
      901 sngmecmwcs stkrcvdsna yiisfpygqc lewqtatcsp qncsglrtcg qcleqpgcgw
      961 cndpsntgrg hciegssrgp mkligmhhse mvldtnlcpk eknyewsfiq cpacqcnghs
     1021 tcinnnvceq cknlttgkqc qdcmpgyygd ptnggqctac tcsghanich lhtgkcfctt
     1081 kgikgdqcql cdsenryvgn plrgtcyysl lidyqftfsl lqeddrhhta infianpeqs
     1141 nknldisina snnfnlnitw svgstagtis geetsivskn nikeyrdsfs yekfnfrsnp
     1201 nitfyvyvsn fswpikiqia fsqhntimdl vqffvtffsc flslllvaav vwkikqtcwa
     1261 srrreqllre rqqmasrpfa svdvalevga eqteflrgpl egapkpiaie pcagnraavl
     1321 tvflclprgs sgapppgqsg laiasalidi sqqkasdskd ktsgvrnrkh lstrqgtcv
//
LOCUS       NP_001137259             434 aa            linear   PRI 20-NOV-2025
DEFINITION  periphilin-1 isoform 6 [Homo sapiens].
ACCESSION   NP_001137259
VERSION     NP_001137259.1
DBSOURCE    REFSEQ: accession NM_001143787.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Bloor,S., Wit,N. and Lehner,P.J.
  TITLE     RNA binding by Periphilin plays an essential role in initiating
            silencing by the HUSH complex
  JOURNAL   Nucleic Acids Res 53 (2) (2025)
   PUBMED   39658355
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Jensvold,Z.D., Flood,J.R., Christenson,A.E. and Lewis,P.W.
  TITLE     Interplay between Two Paralogous Human Silencing Hub (HuSH)
            Complexes in Regulating LINE-1 Element Silencing
  JOURNAL   Nat Commun 15 (1), 9492 (2024)
   PUBMED   39489739
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Danac,J.M.C., Matthews,R.E., Gungi,A., Qin,C., Parsons,H.,
            Antrobus,R., Timms,R.T. and Tchasovnikarova,I.A.
  TITLE     Competition between two HUSH complexes orchestrates the immune
            response to retroelement invasion
  JOURNAL   Mol Cell 84 (15), 2870-2881 (2024)
   PUBMED   39013473
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Tunbak,H., Enriquez-Gasca,R., Tie,C.H.C., Gould,P.A., Mlcochova,P.,
            Gupta,R.K., Fernandes,L., Holt,J., van der Veen,A.G.,
            Giampazolias,E., Burns,K.H., Maillard,P.V. and Rowe,H.M.
  TITLE     The HUSH complex is a gatekeeper of type I interferon through
            epigenetic regulation of LINE-1s
  JOURNAL   Nat Commun 11 (1), 5387 (2020)
   PUBMED   33144593
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Prigozhin,D.M., Douse,C.H., Farleigh,L.E., Albecka,A.,
            Tchasovnikarova,I.A., Timms,R.T., Oda,S.I., Adolf,F.,
            Freund,S.M.V., Maslen,S., Lehner,P.J. and Modis,Y.
  TITLE     Periphilin self-association underpins epigenetic silencing by the
            HUSH complex
  JOURNAL   Nucleic Acids Res 48 (18), 10313-10328 (2020)
   PUBMED   32976585
  REMARK    GeneRIF: Periphilin self-association underpins epigenetic silencing
            by the HUSH complex.
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Kurita,M., Suzuki,H., Masai,H., Mizumoto,K., Ogata,E.,
            Nishimoto,I., Aiso,S. and Matsuoka,M.
  TITLE     Overexpression of CR/periphilin downregulates Cdc7 expression and
            induces S-phase arrest
  JOURNAL   Biochem Biophys Res Commun 324 (2), 554-561 (2004)
   PUBMED   15474462
  REMARK    GeneRIF: CR (periphilin) retards S-phase progression by modifying
            expression of Cdc7 and other genes involved in progression of DNA
            replication
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Goehler,H., Lalowski,M., Stelzl,U., Waelter,S., Stroedicke,M.,
            Worm,U., Droege,A., Lindenberg,K.S., Knoblich,M., Haenig,C.,
            Herbst,M., Suopanki,J., Scherzinger,E., Abraham,C., Bauer,B.,
            Hasenbank,R., Fritzsche,A., Ludewig,A.H., Bussow,K., Coleman,S.H.,
            Gutekunst,C.A., Landwehrmeyer,B.G., Lehrach,H. and Wanker,E.E.
  TITLE     A protein interaction network links GIT1, an enhancer of huntingtin
            aggregation, to Huntington's disease
  JOURNAL   Mol Cell 15 (6), 853-865 (2004)
   PUBMED   15383276
  REMARK    Erratum:[Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad
            [corrected to Bussow, Konrad]]
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Kazerounian,S. and Aho,S.
  TITLE     Characterization of periphilin, a widespread, highly insoluble
            nuclear protein and potential constituent of the keratinocyte
            cornified envelope
  JOURNAL   J Biol Chem 278 (38), 36707-36717 (2003)
   PUBMED   12853457
  REMARK    GeneRIF: periphilin is potentially involved in epithelial
            differentiation and contributes to epidermal integrity and barrier
            formation
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Kazerounian,S., Uitto,J. and Aho,S.
  TITLE     Unique role for the periplakin tail in intermediate filament
            association: specific binding to keratin 8 and vimentin
  JOURNAL   Exp Dermatol 11 (5), 428-438 (2002)
   PUBMED   12366696
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Line,A., Stengrevics,A., Slucka,Z., Li,G., Jankevics,E. and
            Rees,R.C.
  TITLE     Serological identification and expression analysis of gastric
            cancer-associated genes
  JOURNAL   Br J Cancer 86 (11), 1824-1830 (2002)
   PUBMED   12087473
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK129910.1, BC025306.1 and
            AC079601.25.
            
            Summary: The protein encoded by this gene is one of the several
            proteins that become sequentially incorporated into the cornified
            cell envelope during the terminal differentiation of keratinocyte
            at the outer layers of epidermis. This protein interacts with
            periplakin, which is known as a precursor of the cornified cell
            envelope. The cellular localization pattern and insolubility of
            this protein suggest that it may play a role in epithelial
            differentiation and contribute to epidermal integrity and barrier
            formation. Multiple alternatively spliced transcript variants
            encoding distinct isoforms have been observed. [provided by RefSeq,
            Jul 2008].
            
            Transcript Variant: This variant (6) lacks an alternate in-frame
            exon and uses an alternate in-frame splice junction compared to
            variant 1. The resulting isoform (6) has the same N- and C-termini
            but is shorter compared to isoform 1.z.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC025306.1, SRR1163657.429106.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..434
                     /product="periphilin-1 isoform 6"
                     /note="gastric cancer antigen Ga50; CDC7 expression
                     repressor"
                     /calculated_mol_wt=49524
     Region          230..>286
                     /region_name="periphilin-like"
                     /note="Vertebrate periphilin-1 and similar proteins;
                     cd22896"
                     /db_xref="CDD:439377"
     Region          <385..>420
                     /region_name="HERV-K_REC"
                     /note="Rec (regulator of expression encoded by corf) of
                     HERV-K-113; pfam15695"
                     /db_xref="CDD:292323"
     CDS             1..434
                     /gene="PPHLN1"
                     /gene_synonym="CR; HSPC206; HSPC232"
                     /coded_by="NM_001143787.2:84..1388"
                     /note="isoform 6 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS44860.1"
                     /db_xref="GeneID:51535"
                     /db_xref="HGNC:HGNC:19369"
                     /db_xref="MIM:608150"
ORIGIN      
        1 mwsegryeye riprerappr shpsdesgyr wtrddhsasr qpeyrdmrdg frrksfyssh
       61 yarerspykr dntffrespv grkdsphsrs gssvssrsys persksysfh qsqhrksvrp
      121 gasykrqneg nperdkerpv qslktsrdts pssgsavsss kvldkpsrlt ekelaeaask
      181 waaekleksd esnlpeisey eagstaplft dqpeepesnt thgielfeds qlttrskaia
      241 sktkeieqvy rqdcetfgmv vkmliekdps leksiqfalr qnlheiesag qtwqqvppvr
      301 ntemdhdgtp enegeetaqs alfgfqhdas nhtivglgpn qvpemkettl qapqppqapq
      361 plqprkkrvr rttqlrrttg apditwgmlk kttqeaeril lrtqtpftpe nlflamlsvv
      421 hcnsrkdvkp enkq
//
LOCUS       NP_001354600             734 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform hh [Homo sapiens].
ACCESSION   NP_001354600
VERSION     NP_001354600.1
DBSOURCE    REFSEQ: accession NM_001367671.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 734)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 734)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 734)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 734)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 734)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 734)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 734)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 734)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 734)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 734)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.94631.1,
                                           SRR1660805.72650.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..734
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..734
                     /product="SUN domain-containing protein 1 isoform hh"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=81193
     Region          12..241
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          <314..>538
                     /region_name="SMC_N"
                     /note="RecF/RecN/SMC N terminal domain; cl47134"
                     /db_xref="CDD:481474"
     Region          366..419
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(366,369..370,373,376..377,380..381,383..384,
                     387..388,390..391,394..395,397..398,401,404..405,408,
                     411..412,415..416,418..419)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          496..554
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          597..732
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..734
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367671.1:105..2309"
                     /note="isoform hh is encoded by transcript variant 34"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gldddgdlkg gnkaaiqgng
      121 dvgaaaatah ngfscsncsm lserkdvlta hpaapgpvsr vysrdrnqkc yfllqilrri
      181 gavgqavsrt awsalwlavv apgkaasgvf wwlgigwyqf vtliswlnvf lltrclrnic
      241 kflvlliplf lllglslrgq gnffsflpvl nwasmhrtqr vddpqdvfkp ttsrlkqplq
      301 gdseafpwhw msgveqqvas lsgqchhhge nlrelttllq klqarvdqme ggaagpsasv
      361 rdavgqppre tdfmafhqeh evrmshledi lgklreksea iqkeleqtkq ktisavgeql
      421 lptvehlqle ldqlkselss wrhvktgcet vdavqervdv qvremvkllf sedqqggsle
      481 qllqrfssqf vskgdlqtml rdlqlqilrn vthhvsvtkq lptseavvsa vseagasgit
      541 eaqaraivns alklysqdkt gmvdfalesg ggsilstrcs etyetktalm slfgiplwyf
      601 sqsprvviqp diypgncwaf kgsqgylvvr lsmmihpaaf tlehipktls ptgnissapk
      661 dfavyglene yqeegqllgq ftydqdgesl qmfqalkrpd dtafqivelr ifsnwghpey
      721 tclyrfrvhg epvk
//
LOCUS       NP_848545                253 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase MARCHF3 [Homo sapiens].
ACCESSION   NP_848545 XP_943102
VERSION     NP_848545.1
DBSOURCE    REFSEQ: accession NM_178450.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 253)
  AUTHORS   Zhou,J., Tu,D., Peng,R., Tang,Y., Deng,Q., Su,B., Wang,S., Tang,H.,
            Jin,S., Jiang,G., Wang,Q., Jin,X., Zhang,C., Cao,J. and Bai,D.
  TITLE     RNF173 suppresses RAF/MEK/ERK signaling to regulate invasion and
            metastasis via GRB2 ubiquitination in Hepatocellular Carcinoma
  JOURNAL   Cell Commun Signal 21 (1), 224 (2023)
   PUBMED   37626338
  REMARK    GeneRIF: RNF173 suppresses RAF/MEK/ERK signaling to regulate
            invasion and metastasis via GRB2 ubiquitination in Hepatocellular
            Carcinoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 253)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 253)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 253)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 253)
  AUTHORS   Leclair,H.M., Andre-Gregoire,G., Treps,L., Azzi,S., Bidere,N. and
            Gavard,J.
  TITLE     The E3 ubiquitin ligase MARCH3 controls the endothelial barrier
  JOURNAL   FEBS Lett 590 (20), 3660-3668 (2016)
   PUBMED   27616439
  REMARK    GeneRIF: Report shows that silencing MARCH3 protects the
            endothelial barrier and upregulates OCLN in MARCH3-depleted cells.
            MARCH3 silencing results in the strengthening of cell-cell contacts
            and inactivates FoxO1.
REFERENCE   6  (residues 1 to 253)
  AUTHORS   Fatehchand,K., Ren,L., Elavazhagan,S., Fang,H., Mo,X.,
            Vasilakos,J.P., Dietsch,G.N., Hershberg,R.M., Tridandapani,S. and
            Butchar,J.P.
  TITLE     Toll-like Receptor 4 Ligands Down-regulate Fcgamma Receptor IIb
            (FcgammaRIIb) via MARCH3 Protein-mediated Ubiquitination
  JOURNAL   J Biol Chem 291 (8), 3895-3904 (2016)
   PUBMED   26694610
  REMARK    GeneRIF: LPS activation of TLR4 significantly increased MARCH3
            expression and that siRNA against MARCH3 prevented the decrease in
            FcgammaRIIb following LPS treatment.
REFERENCE   7  (residues 1 to 253)
  AUTHORS   Ivarsson,Y., Arnold,R., McLaughlin,M., Nim,S., Joshi,R., Ray,D.,
            Liu,B., Teyra,J., Pawson,T., Moffat,J., Li,S.S., Sidhu,S.S. and
            Kim,P.M.
  TITLE     Large-scale interaction profiling of PDZ domains through proteomic
            peptide-phage display using human and viral phage peptidomes
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2542-2547 (2014)
   PUBMED   24550280
REFERENCE   8  (residues 1 to 253)
  AUTHORS   Fukuda,H., Nakamura,N. and Hirose,S.
  TITLE     MARCH-III Is a novel component of endosomes with properties similar
            to those of MARCH-II
  JOURNAL   J Biochem 139 (1), 137-145 (2006)
   PUBMED   16428329
REFERENCE   9  (residues 1 to 253)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB455278.1, BC047569.1,
            AC093532.2 and AC137794.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Mar 4, 2006 this sequence version replaced XP_943102.1.
            
            Summary: This gene encodes a member of the membrane-associated
            RING-CH (MARCH) family. The encoded protein is an E3
            ubiquitin-protein ligase that may be involved in regulation of the
            endosomal transport pathway. [provided by RefSeq, Mar 2013].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.62941.1,
                                           SRR1803613.34973.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000308660.6/ ENSP00000309141.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..253
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..253
                     /product="E3 ubiquitin-protein ligase MARCHF3"
                     /EC_number="2.3.2.27"
                     /note="membrane-associated RING-CH protein III; E3
                     ubiquitin-protein ligase MARCH3; RING finger protein 173;
                     membrane-associated ring finger (C3HC4) 3, E3 ubiquitin
                     protein ligase; membrane associated ring finger 3;
                     RING-type E3 ubiquitin transferase MARCH3; RING-type E3
                     ubiquitin transferase MARCHF3"
                     /calculated_mol_wt=28373
     Region          65..120
                     /region_name="RING_CH-C4HC3_MARCH3"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH3 (MARCH3); cd16809"
                     /db_xref="CDD:438459"
     Site            145..165
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UD3.1)"
     Site            182..202
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86UD3.1)"
     Site            237
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UD3.1)"
     Site            243
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86UD3.1)"
     CDS             1..253
                     /gene="MARCHF3"
                     /gene_synonym="MARCH-III; MARCH3; RNF173"
                     /coded_by="NM_178450.5:266..1027"
                     /db_xref="CCDS:CCDS4141.1"
                     /db_xref="GeneID:115123"
                     /db_xref="HGNC:HGNC:28728"
                     /db_xref="MIM:613333"
ORIGIN      
        1 mttsrcshlp evlpdctssa apvvktvedc gslvngqpqy vmqvsakdgq llstvvrtla
       61 tqspfndrpm crichegssq edllspcect gtlgtihrsc lehwlsssnt sycelchfrf
      121 averkprplv ewlrnpgpqh ekrtlfgdmv cflfitplat isgwlclrga vdhlhfssrl
      181 eavglialtv alftiylfwt lvsfryhcrl ynewrrtnqr villipksvn vpsnqpsllg
      241 lhsvkrnske tvv
//
LOCUS       NP_001295151             372 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-gated potassium channel subunit beta-1 isoform 5 [Homo
            sapiens].
ACCESSION   NP_001295151 XP_005247811
VERSION     NP_001295151.1
DBSOURCE    REFSEQ: accession NM_001308222.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 372)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 372)
  AUTHORS   Quintanilha,J.C.F., Wang,J., Sibley,A.B., Jiang,C., Etheridge,A.S.,
            Shen,F., Jiang,G., Mulkey,F., Patel,J.N., Hertz,D.L., Dees,E.C.,
            McLeod,H.L., Bertagnolli,M., Rugo,H., Kindler,H.L., Kelly,W.K.,
            Ratain,M.J., Kroetz,D.L., Owzar,K., Schneider,B.P., Lin,D. and
            Innocenti,F.
  TITLE     Bevacizumab-induced hypertension and proteinuria: a genome-wide
            study of more than 1000 patients
  JOURNAL   Br J Cancer 126 (2), 265-274 (2022)
   PUBMED   34616010
  REMARK    GeneRIF: Bevacizumab-induced hypertension and proteinuria: a
            genome-wide study of more than 1000 patients.
            Erratum:[Br J Cancer. 2022 Jan;126(1):162. doi:
            10.1038/s41416-021-01617-1. PMID: 34853435]
REFERENCE   3  (residues 1 to 372)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 372)
  AUTHORS   Macias,A., de la Cruz,A., Peraza,D.A., Benito-Bueno,A., Gonzalez,T.
            and Valenzuela,C.
  TITLE     KV1.5-KVbeta1.3 Recycling Is PKC-Dependent
  JOURNAL   Int J Mol Sci 22 (3), 1336 (2021)
   PUBMED   33572906
  REMARK    GeneRIF: KV1.5-KVbeta1.3 Recycling Is PKC-Dependent.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 372)
  AUTHORS   Cho,I.H., Panzera,L.C., Chin,M., Alpizar,S.A., Olveda,G.E.,
            Hill,R.A. and Hoppa,M.B.
  TITLE     The potassium channel subunit Kvbeta1 serves as a major control
            point for synaptic facilitation
  JOURNAL   Proc Natl Acad Sci U S A 117 (47), 29937-29947 (2020)
   PUBMED   33168717
  REMARK    GeneRIF: The potassium channel subunit Kvbeta1 serves as a major
            control point for synaptic facilitation.
REFERENCE   6  (residues 1 to 372)
  AUTHORS   England,S.K., Uebele,V.N., Kodali,J., Bennett,P.B. and Tamkun,M.M.
  TITLE     A novel K+ channel beta-subunit (hKv beta 1.3) is produced via
            alternative mRNA splicing
  JOURNAL   J Biol Chem 270 (48), 28531-28534 (1995)
   PUBMED   7499366
REFERENCE   7  (residues 1 to 372)
  AUTHORS   McCormack,K., McCormack,T., Tanouye,M., Rudy,B. and Stuhmer,W.
  TITLE     Alternative splicing of the human Shaker K+ channel beta 1 gene and
            functional expression of the beta 2 gene product
  JOURNAL   FEBS Lett 370 (1-2), 32-36 (1995)
   PUBMED   7649300
REFERENCE   8  (residues 1 to 372)
  AUTHORS   England,S.K., Uebele,V.N., Shear,H., Kodali,J., Bennett,P.B. and
            Tamkun,M.M.
  TITLE     Characterization of a voltage-gated K+ channel beta subunit
            expressed in human heart
  JOURNAL   Proc Natl Acad Sci U S A 92 (14), 6309-6313 (1995)
   PUBMED   7603988
REFERENCE   9  (residues 1 to 372)
  AUTHORS   Morales,M.J., Castellino,R.C., Crews,A.L., Rasmusson,R.L. and
            Strauss,H.C.
  TITLE     A novel beta subunit increases rate of inactivation of specific
            voltage-gated potassium channel alpha subunits
  JOURNAL   J Biol Chem 270 (11), 6272-6277 (1995)
   PUBMED   7890764
REFERENCE   10 (residues 1 to 372)
  AUTHORS   Majumder,K., De Biasi,M., Wang,Z. and Wible,B.A.
  TITLE     Molecular cloning and functional expression of a novel potassium
            channel beta-subunit from human atrium
  JOURNAL   FEBS Lett 361 (1), 13-16 (1995)
   PUBMED   7890032
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC043166.2, AC022013.3,
            AY780786.1, AC069413.14 and AC092927.5.
            
            On Apr 28, 2015 this sequence version replaced XP_005247811.1.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member includes distinct isoforms
            which are encoded by alternatively spliced transcript variants of
            this gene. Some of these isoforms are beta subunits, which form
            heteromultimeric complexes with alpha subunits and modulate the
            activity of the pore-forming alpha subunits. [provided by RefSeq,
            Apr 2015].
            
            Transcript Variant: This variant (5) lacks a 5' exon, uses an
            alternate 5' terminal, initiates translation at an alternate start
            codon, and lacks an alternate in-frame exon in the 3' coding
            region, compared to variant 1. It encodes isoform 5 which has a
            distinct N-terminus and is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.92635.1, AY780786.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144120, SAMEA2144333
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..372
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.31"
     Protein         1..372
                     /product="voltage-gated potassium channel subunit beta-1
                     isoform 5"
                     /note="potassium channel beta 3 chain; potassium channel
                     beta3 subunit; potassium channel shaker chain beta 1a;
                     K(+) channel subunit beta-1; potassium voltage-gated
                     channel, shaker-related subfamily, beta member 1; K+
                     channel Beta1a chain; potassium voltage-gated channel
                     subfamily A member regulatory beta subunit 1; potassium
                     channel, voltage gated subfamily A regulatory beta subunit
                     1"
                     /calculated_mol_wt=41319
     Region          71..364
                     /region_name="AKR_SF"
                     /note="Aldo-keto reductase (AKR) superfamily; cl00470"
                     /db_xref="CDD:444925"
     Site            order(89..91,119,124,152,193..194,219,248..254,309,
                     326..329,334,337..338)
                     /site_type="active"
                     /db_xref="CDD:381296"
     CDS             1..372
                     /gene="KCNAB1"
                     /gene_synonym="AKR6A3; hKvb3; hKvBeta3; KCNA1B; KV-BETA-1;
                     Kvb1.3"
                     /coded_by="NM_001308222.1:872..1990"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS77845.1"
                     /db_xref="GeneID:7881"
                     /db_xref="HGNC:HGNC:6228"
                     /db_xref="MIM:601141"
ORIGIN      
        1 mqvsiacteh nlksrngedr llskqsstap nvvnaarakf rtvaiiarsl gtftpqhhis
       61 lkestakqtg mkyrnlgksg lrvsclglgt wvtfggqisd evaerlmtia yesgvnlfdt
      121 aevyaagkae vilgsiikkk gwrrsslvit tklywggkae terglsrkhi ieeivramth
      181 vinqgmamyw gtsrwsamei meaysvarqf nmippvceqa eyhlfqrekv evqlpelyhk
      241 igvgamtwsp lacgiisgky gngvpessra slkcyqwlke rivseegrkq qnklkdlspi
      301 aerlgctlpq lavawclrne gvssvllgss tpeqlienlg aiqvlpkmts hvvneidnil
      361 rnkpyskkdy rs
//
LOCUS       NP_001335050             434 aa            linear   PRI 20-NOV-2025
DEFINITION  tripartite motif-containing protein 16 isoform b [Homo sapiens].
ACCESSION   NP_001335050
VERSION     NP_001335050.1
DBSOURCE    REFSEQ: accession NM_001348121.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Guo,D., Zhang,M., Wei,T., Zhang,X., Shi,X., Tang,H., Ding,M.,
            Li,J., Zhang,S. and Guo,W.
  TITLE     NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16
  JOURNAL   Cell Mol Life Sci 81 (1), 167 (2024)
   PUBMED   38581570
  REMARK    GeneRIF: NFKBIZ regulates NFkappaB signaling pathway to mediate
            tumorigenesis and metastasis of hepatocellular carcinoma by direct
            interaction with TRIM16.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Li,S., Wang,J., Chen,H., Hou,J., Shen,T., Li,J., Zhou,B., Zhang,B.,
            Liu,H. and Jiang,D.K.
  TITLE     TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin pathway
  JOURNAL   Mol Carcinog 62 (11), 1686-1699 (2023)
   PUBMED   37477507
  REMARK    GeneRIF: TRIM16 E121D variant affects the risk and prognosis of
            hepatocellular carcinoma by modulating the Wnt/beta-catenin
            pathway.
REFERENCE   4  (residues 1 to 434)
  AUTHORS   Roshanazadeh,M.R., Adelipour,M., Sanaei,A., Chenane,H. and
            Rashidi,M.
  TITLE     TRIM3 and TRIM16 as potential tumor suppressors in breast cancer
            patients
  JOURNAL   BMC Res Notes 15 (1), 312 (2022)
   PUBMED   36180926
  REMARK    GeneRIF: TRIM3 and TRIM16 as potential tumor suppressors in breast
            cancer patients.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 434)
  AUTHORS   Wang,Y., Wu,Y. and Xie,S.
  TITLE     CircPTK2 inhibits cell cisplatin (CDDP) resistance by targeting
            miR-942/TRIM16 axis in non-small cell lung cancer (NSCLC)
  JOURNAL   Bioengineered 13 (2), 3651-3664 (2022)
   PUBMED   35230201
  REMARK    GeneRIF: CircPTK2 inhibits cell cisplatin (CDDP) resistance by
            targeting miR-942/TRIM16 axis in non-small cell lung cancer
            (NSCLC).
REFERENCE   6  (residues 1 to 434)
  AUTHORS   Gwinn,M.R., Whipkey,D.L., Tennant,L.B. and Weston,A.
  TITLE     Differential gene expression in normal human mammary epithelial
            cells treated with malathion monitored by DNA microarrays
  JOURNAL   Environ Health Perspect 113 (8), 1046-1051 (2005)
   PUBMED   16079077
REFERENCE   7  (residues 1 to 434)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   8  (residues 1 to 434)
  AUTHORS   Beer,H.D., Munding,C., Dubois,N., Mamie,C., Hohl,D. and Werner,S.
  TITLE     The estrogen-responsive B box protein: a novel regulator of
            keratinocyte differentiation
  JOURNAL   J Biol Chem 277 (23), 20740-20749 (2002)
   PUBMED   11919186
  REMARK    GeneRIF: role in regulating keratinocyte differentiation
REFERENCE   9  (residues 1 to 434)
  AUTHORS   Reymond,A., Meroni,G., Fantozzi,A., Merla,G., Cairo,S., Luzi,L.,
            Riganelli,D., Zanaria,E., Messali,S., Cainarca,S., Guffanti,A.,
            Minucci,S., Pelicci,P.G. and Ballabio,A.
  TITLE     The tripartite motif family identifies cell compartments
  JOURNAL   EMBO J 20 (9), 2140-2151 (2001)
   PUBMED   11331580
REFERENCE   10 (residues 1 to 434)
  AUTHORS   Liu,H.L., Golder-Novoselsky,E., Seto,M.H., Webster,L., McClary,J.
            and Zajchowski,D.A.
  TITLE     The novel estrogen-responsive B-box protein (EBBP) gene is
            tamoxifen-regulated in cells expressing an estrogen receptor
            DNA-binding domain mutant
  JOURNAL   Mol Endocrinol 12 (11), 1733-1748 (1998)
   PUBMED   9817599
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005324.1.
            
            Summary: The protein encoded by this gene is a tripartite motif
            (TRIM) family member that contains two B box domains and a
            coiled-coiled region that are characteristic of the B box zinc
            finger protein family. While it lacks a RING domain found in other
            TRIM proteins, the encoded protein can homodimerize or
            heterodimerize with other TRIM proteins and has E3 ubiquitin ligase
            activity. This gene is also a tumor suppressor and is involved in
            secretory autophagy. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (4), as well as variant 5, encodes
            isoform b.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.122162.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p12"
     Protein         1..434
                     /product="tripartite motif-containing protein 16 isoform
                     b"
                     /EC_number="2.3.2.27"
                     /note="estrogen-responsive B box protein; tripartite
                     motif-containing protein 16; E3 ubiquitin-protein ligase
                     TRIM16"
                     /calculated_mol_wt=49899
     Region          235..416
                     /region_name="SPRY_PRY_TRIM16"
                     /note="PRY/SPRY domain in tripartite motif-containing
                     protein 16 (TRIM16); cd12890"
                     /db_xref="CDD:293948"
     CDS             1..434
                     /gene="TRIM16"
                     /gene_synonym="EBBP"
                     /coded_by="NM_001348121.1:189..1493"
                     /note="isoform b is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS86579.1"
                     /db_xref="GeneID:10626"
                     /db_xref="HGNC:HGNC:17241"
                     /db_xref="MIM:609505"
ORIGIN      
        1 mimedwtckl qnrvlpsedp alsqkgylkk enmaalcrta esqaelqctq ldlerklkln
       61 enaisrlqan qksvlvsvse vkavaemqfg ellaavrkaq anvmlfleek eqaalsqang
      121 ikahleyrsa emekskqele rmaaisntvq fleeyckfkn teditfpsvy vglkdklsgi
      181 rkvitestvh liqllenykk klqefskeee ydirtqvsav vqrkywtskp epstreqflq
      241 yayditfdpd tahkylrlqe enrkvtnttp wehpypdlps rflhwrqvls qqslylhryy
      301 feveifgagt yvgltckgid rkgeernsci sgnnfswslq wngkeftawy sdmetplkag
      361 pfrrlgvyid fpggilsfyg veydtmtlvh kfackfsepv yaafwlskke nairivdlge
      421 epekpapslv gtap
//
LOCUS       NP_001186251             123 aa            linear   PRI 20-NOV-2025
DEFINITION  biogenesis of lysosome-related organelles complex 1 subunit 5
            isoform 2 [Homo sapiens].
ACCESSION   NP_001186251
VERSION     NP_001186251.1
DBSOURCE    REFSEQ: accession NM_001199322.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 123)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 123)
  AUTHORS   Zhong,Z., Wu,Z., Zhang,J. and Chen,J.
  TITLE     A novel BLOC1S5-related HPS-11 patient and zebrafish with bloc1s5
            disruption
  JOURNAL   Pigment Cell Melanoma Res 34 (6), 1112-1119 (2021)
   PUBMED   34058075
  REMARK    GeneRIF: A novel BLOC1S5-related HPS-11 patient and zebrafish with
            bloc1s5 disruption.
REFERENCE   3  (residues 1 to 123)
  AUTHORS   Boeckelmann,D., Wolter,M., Kasmann-Kellner,B., Koehler,U.,
            Schieber-Nakamura,L. and Zieger,B.
  TITLE     A Novel Likely Pathogenic Variant in the BLOC1S5 Gene Associated
            with Hermansky-Pudlak Syndrome Type 11 and an Overview of Human
            BLOC-1 Deficiencies
  JOURNAL   Cells 10 (10), 2630 (2021)
   PUBMED   34685610
  REMARK    GeneRIF: A Novel Likely Pathogenic Variant in the BLOC1S5 Gene
            Associated with Hermansky-Pudlak Syndrome Type 11 and an Overview
            of Human BLOC-1 Deficiencies.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 123)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 123)
  AUTHORS   Pennamen,P., Le,L., Tingaud-Sequeira,A., Fiore,M., Bauters,A., Van
            Duong Beatrice,N., Coste,V., Bordet,J.C., Plaisant,C., Diallo,M.,
            Michaud,V., Trimouille,A., Lacombe,D., Lasseaux,E., Delevoye,C.,
            Picard,F.M., Delobel,B., Marks,M.S. and Arveiler,B.
  TITLE     BLOC1S5 pathogenic variants cause a new type of Hermansky-Pudlak
            syndrome
  JOURNAL   Genet Med 22 (10), 1613-1622 (2020)
   PUBMED   32565547
  REMARK    GeneRIF: BLOC1S5 pathogenic variants cause a new type of
            Hermansky-Pudlak syndrome.
REFERENCE   6  (residues 1 to 123)
  AUTHORS   Ciciotte,S.L., Gwynn,B., Moriyama,K., Huizing,M., Gahl,W.A.,
            Bonifacino,J.S. and Peters,L.L.
  TITLE     Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a
            novel protein that is part of the pallidin-muted complex (BLOC-1)
  JOURNAL   Blood 101 (11), 4402-4407 (2003)
   PUBMED   12576321
REFERENCE   7  (residues 1 to 123)
  AUTHORS   Moriyama,K. and Bonifacino,J.S.
  TITLE     Pallidin is a component of a multi-protein complex involved in the
            biogenesis of lysosome-related organelles
  JOURNAL   Traffic 3 (9), 666-677 (2002)
   PUBMED   12191018
REFERENCE   8  (residues 1 to 123)
  AUTHORS   Falcon-Perez,J.M., Starcevic,M., Gautam,R. and Dell'Angelica,E.C.
  TITLE     BLOC-1, a novel complex containing the pallidin and muted proteins
            involved in the biogenesis of melanosomes and platelet-dense
            granules
  JOURNAL   J Biol Chem 277 (31), 28191-28199 (2002)
   PUBMED   12019270
REFERENCE   9  (residues 1 to 123)
  AUTHORS   Zhang,Q., Li,W., Novak,E.K., Karim,A., Mishra,V.S., Kingsmore,S.F.,
            Roe,B.A., Suzuki,T. and Swank,R.T.
  TITLE     The gene for the muted (mu) mouse, a model for Hermansky-Pudlak
            syndrome, defines a novel protein which regulates vesicle
            trafficking
  JOURNAL   Hum Mol Genet 11 (6), 697-706 (2002)
   PUBMED   11912185
REFERENCE   10 (residues 1 to 123)
  AUTHORS   Introne,W.J., Huizing,M., Malicdan,M.C.V., O'Brien,K.J. and
            Gahl,W.A.
  TITLE     Hermansky-Pudlak Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301464
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA635930.1, BC119645.1,
            AL096800.20 and AA653396.1.
            
            Summary: This gene encodes a component of BLOC-1 (biogenesis of
            lysosome-related organelles complex 1). Components of this complex
            are involved in the biogenesis of organelles such as melanosomes
            and platelet-dense granules. A mouse model for Hermansky-Pudlak
            Syndrome is mutated in the murine version of this gene. Alternative
            splicing results in multiple transcript variants. Read-through
            transcription exists between this gene and the upstream EEF1E1
            (eukaryotic translation elongation factor 1 epsilon 1) gene, as
            well as with the downstream TXNDC5 (thioredoxin domain containing
            5) gene. [provided by RefSeq, Dec 2010].
            
            Transcript Variant: This variant (2) includes an additional
            internal exon, resulting in the use of an alternate start codon,
            compared to variant 1. The encoded isoform (2) has a distinct and
            shorter N-terminus, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR18074969.2583776.1,
                                           SRR14038191.221947.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..123
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..123
                     /product="biogenesis of lysosome-related organelles
                     complex 1 subunit 5 isoform 2"
                     /note="protein Muted homolog; muted homolog; BLOC-1
                     subunit 5; biogenesis of lysosome-related organelles
                     complex 1 subunit 5; biogenesis of lysosomal organelles
                     complex-1, subunit 5, muted"
                     /calculated_mol_wt=14762
     Region          <2..117
                     /region_name="Muted"
                     /note="Organelle biogenesis, Muted-like protein;
                     pfam14942"
                     /db_xref="CDD:464390"
     CDS             1..123
                     /gene="BLOC1S5"
                     /gene_synonym="BLOS5; HPS11; MU; MUTED"
                     /coded_by="NM_001199322.1:334..705"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:63915"
                     /db_xref="HGNC:HGNC:18561"
                     /db_xref="MIM:607289"
ORIGIN      
        1 mekrglremr vlenlknmih etnehtlpkc rdtmrdslsq vlqrlqaand svcrlqqreq
       61 erkkihsdhl vasekqhmlq wdnfmkeqpn kraevdeehr kamerlkeqy aemekdlakf
      121 stf
//
LOCUS       NP_001257337             312 aa            linear   PRI 20-NOV-2025
DEFINITION  junctional adhesion molecule B isoform 3 precursor [Homo sapiens].
ACCESSION   NP_001257337
VERSION     NP_001257337.1
DBSOURCE    REFSEQ: accession NM_001270408.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Khojasteh,M., Soleimani,P., Ghasemi,A., Taghizadeh,P., Rohani,M.
            and Alavi,A.
  TITLE     JAM2 variants can be more common in primary familial brain
            calcification (PFBC) cases than those appear; may be due to a
            founder mutation
  JOURNAL   Neurol Sci 45 (8), 3829-3844 (2024)
   PUBMED   38441788
  REMARK    GeneRIF: JAM2 variants can be more common in primary familial brain
            calcification (PFBC) cases than those appear; may be due to a
            founder mutation.
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Dong,Y., Zhang,J., Xie,S., Di,S., Fan,B. and Gong,T.
  TITLE     JAM2 is a prognostic biomarker and inhibits proliferation,
            metastasis and epithelial-mesenchymal transition in lung
            adenocarcinoma
  JOURNAL   J Gene Med 26 (2), e3679 (2024)
   PUBMED   38404047
  REMARK    GeneRIF: JAM2 is a prognostic biomarker and inhibits proliferation,
            metastasis and epithelial-mesenchymal transition in lung
            adenocarcinoma.
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Peng,Y., Li,H., Fu,Y., Guo,S., Qu,C., Zhang,Y., Zong,B. and Liu,S.
  TITLE     JAM2 predicts a good prognosis and inhibits invasion and migration
            by suppressing EMT pathway in breast cancer
  JOURNAL   Int Immunopharmacol 103, 108430 (2022)
   PUBMED   34923424
  REMARK    GeneRIF: JAM2 predicts a good prognosis and inhibits invasion and
            migration by suppressing EMT pathway in breast cancer.
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Liang,T.W., Chiu,H.H., Gurney,A., Sidle,A., Tumas,D.B., Schow,P.,
            Foster,J., Klassen,T., Dennis,K., DeMarco,R.A., Pham,T., Frantz,G.
            and Fong,S.
  TITLE     Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2
            interacts with T, NK, and dendritic cells through JAM 3
  JOURNAL   J Immunol 168 (4), 1618-1626 (2002)
   PUBMED   11823489
  REMARK    GeneRIF: role as an adhesive ligand for interacting with a variety
            of immune cell types
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Arrate,M.P., Rodriguez,J.M., Tran,T.M., Brock,T.A. and
            Cunningham,S.A.
  TITLE     Cloning of human junctional adhesion molecule 3 (JAM3) and its
            identification as the JAM2 counter-receptor
  JOURNAL   J Biol Chem 276 (49), 45826-45832 (2001)
   PUBMED   11590146
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Cunningham,S.A., Arrate,M.P., Rodriguez,J.M., Bjercke,R.J.,
            Vanderslice,P., Morris,A.P. and Brock,T.A.
  TITLE     A novel protein with homology to the junctional adhesion molecule.
            Characterization of leukocyte interactions
  JOURNAL   J Biol Chem 275 (44), 34750-34756 (2000)
   PUBMED   10945976
  REMARK    GeneRIF: Cloning and discovery as adhesion receptor for T cells
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Palmeri,D., van Zante,A., Huang,C.C., Hemmerich,S. and Rosen,S.D.
  TITLE     Vascular endothelial junction-associated molecule, a novel member
            of the immunoglobulin superfamily, is localized to intercellular
            boundaries of endothelial cells
  JOURNAL   J Biol Chem 275 (25), 19139-19145 (2000)
   PUBMED   10779521
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Balck,A., Klein,C. and Westenberger,A.
  TITLE     Primary Familial Brain Calcification Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301594
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000223.1, BM921497.1,
            AY358361.1 and AP000226.2.
            
            Summary: This gene belongs to the immunoglobulin superfamily, and
            the junctional adhesion molecule (JAM) family. The protein encoded
            by this gene is a type I membrane protein that is localized at the
            tight junctions of both epithelial and endothelial cells. It acts
            as an adhesive ligand for interacting with a variety of immune cell
            types, and may play a role in lymphocyte homing to secondary
            lymphoid organs. Alternatively spliced transcript variants have
            been found for this gene. [provided by RefSeq, Jul 2012].
            
            Transcript Variant: This variant (3) contains an alternate 3'
            terminal exon compared to variant 1, which results in a
            frame-shift, and a longer isoform (3) with a distinct C-terminus
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358361.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..312
                     /product="junctional adhesion molecule B isoform 3
                     precursor"
                     /note="vascular endothelial junction-associated molecule;
                     junctional adhesion molecule B; JAM-IT/VE-JAM; JAM-2"
                     /calculated_mol_wt=31233
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3340
     mat_peptide     29..312
                     /product="junctional adhesion molecule B isoform 3"
                     /calculated_mol_wt=31233
     Region          30..131
                     /region_name="IgV_1_JAM1-like"
                     /note="First Ig-like domain of Junctional adhesion
                     molecule-1 (JAM1)and similar domains; a member of the
                     V-set of IgSF domains; cd20946"
                     /db_xref="CDD:409538"
     Region          30..52
                     /region_name="FR1"
                     /note="FR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          30..33
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409538"
     Region          37..41
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409538"
     Region          44..53
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409538"
     Region          53..59
                     /region_name="CDR1"
                     /note="CDR1 [structural motif]"
                     /db_xref="CDD:409538"
     Region          59..67
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409538"
     Region          60..67
                     /region_name="FR2"
                     /note="FR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          70..83
                     /region_name="CDR2"
                     /note="CDR2 [structural motif]"
                     /db_xref="CDD:409538"
     Region          70..75
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409538"
     Region          84..112
                     /region_name="FR3"
                     /note="FR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          86..90
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409538"
     Region          92..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409538"
     Site            98
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Region          105..113
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409538"
     Region          113..121
                     /region_name="CDR3"
                     /note="CDR3 [structural motif]"
                     /db_xref="CDD:409538"
     Region          121..130
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409538"
     Region          122..131
                     /region_name="FR4"
                     /note="FR4 [structural motif]"
                     /db_xref="CDD:409538"
     Region          137..232
                     /region_name="Ig"
                     /note="Immunoglobulin domain; cl11960"
                     /db_xref="CDD:472250"
     Region          151..155
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          165..169
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            187
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Region          197..201
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          211..216
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          225..228
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            236
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P57087.1)"
     Site            239..259
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P57087.1)"
     CDS             1..312
                     /gene="JAM2"
                     /gene_synonym="C21orf43; CD322; IBGC8; JAM-B; JAMB;
                     PRO245; VE-JAM; VEJAM"
                     /coded_by="NM_001270408.2:565..1503"
                     /note="isoform 3 precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS58787.1"
                     /db_xref="GeneID:58494"
                     /db_xref="HGNC:HGNC:14686"
                     /db_xref="MIM:606870"
ORIGIN      
        1 marrsrhrll llllrylvva lgyhkaygfs apkdqqvvta veyqeailac ktpkktvssr
       61 lewkklgrsv sfvyyqqtlq gdfknraemi dfniriknvt rsdagkyrce vsapseqgqn
      121 leedtvtlev lvapavpsce vpssalsgtv velrcqdkeg npapeytwfk dgirllenpr
      181 lgsqstnssy tmntktgtlq fntvskldtg eyscearnsv gyrrcpgkrm qvddlnisgi
      241 iaavvvvalv isvcglgvcy aqrkgyfske tsfqksnsss kattmsenvq wltpvipalw
      301 kaaaggsrgq ef
//
LOCUS       NP_001271359             499 aa            linear   PRI 20-NOV-2025
DEFINITION  U3 small nucleolar RNA-associated protein 15 homolog isoform 2
            [Homo sapiens].
ACCESSION   NP_001271359 XP_005248671
VERSION     NP_001271359.1
DBSOURCE    REFSEQ: accession NM_001284430.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 499)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 499)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   3  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 499)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 499)
  AUTHORS   Wada,K., Sato,M., Araki,N., Kumeta,M., Hirai,Y., Takeyasu,K.,
            Furukawa,K. and Horigome,T.
  TITLE     Dynamics of WD-repeat containing proteins in SSU processome
            components
  JOURNAL   Biochem Cell Biol 92 (3), 191-199 (2014)
   PUBMED   24754225
REFERENCE   6  (residues 1 to 499)
  AUTHORS   Prieto,J.L. and McStay,B.
  TITLE     Recruitment of factors linking transcription and processing of
            pre-rRNA to NOR chromatin is UBF-dependent and occurs independent
            of transcription in human cells
  JOURNAL   Genes Dev 21 (16), 2041-2054 (2007)
   PUBMED   17699751
REFERENCE   7  (residues 1 to 499)
  AUTHORS   Tsuritani,K., Irie,T., Yamashita,R., Sakakibara,Y., Wakaguri,H.,
            Kanai,A., Mizushima-Sugano,J., Sugano,S., Nakai,K. and Suzuki,Y.
  TITLE     Distinct class of putative 'non-conserved' promoters in humans:
            comparative studies of alternative promoters of human and mouse
            genes
  JOURNAL   Genome Res 17 (7), 1005-1014 (2007)
   PUBMED   17567985
REFERENCE   8  (residues 1 to 499)
  AUTHORS   Van Hooser,A.A., Yuh,P. and Heald,R.
  TITLE     The perichromosomal layer
  JOURNAL   Chromosoma 114 (6), 377-388 (2005)
   PUBMED   16136320
  REMARK    Review article
REFERENCE   9  (residues 1 to 499)
  AUTHORS   Scherl,A., Coute,Y., Deon,C., Calle,A., Kindbeiter,K.,
            Sanchez,J.C., Greco,A., Hochstrasser,D. and Diaz,J.J.
  TITLE     Functional proteomic analysis of human nucleolus
  JOURNAL   Mol Biol Cell 13 (11), 4100-4109 (2002)
   PUBMED   12429849
REFERENCE   10 (residues 1 to 499)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP872156.1, AK302021.1, AK022849.1, AL520195.3 and AC010279.5.
            
            On Oct 1, 2013 this sequence version replaced XP_005248671.1.
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            acceptor splice site in the 5' coding region compared to variant 1.
            The resulting shorter isoform (2) lacks an internal protein segment
            compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302021.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2161674
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..499
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.2"
     Protein         1..499
                     /product="U3 small nucleolar RNA-associated protein 15
                     homolog isoform 2"
                     /note="Src-associated protein SAW; U3 small nucleolar
                     RNA-associated protein 15 homolog; UTP15, U3 small
                     nucleolar ribonucleoprotein, homolog; UTP15 SSU processome
                     component"
                     /calculated_mol_wt=56225
     Region          <31..288
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          65..101
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          107..143
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          148..185
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          191..226
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          232..268
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          273..311
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          324..471
                     /region_name="UTP15_C"
                     /note="UTP15 C terminal; pfam09384"
                     /db_xref="CDD:462782"
     CDS             1..499
                     /gene="UTP15"
                     /gene_synonym="NET21"
                     /coded_by="NM_001284430.1:256..1755"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS68893.1"
                     /db_xref="GeneID:84135"
                     /db_xref="HGNC:HGNC:25758"
                     /db_xref="MIM:616194"
ORIGIN      
        1 magykpvaiq typilgekit qdtlywnnyk ppynyavtas srihiygrys qepiktfsrf
       61 kdtaycatfr qdgrllvags edggvqlfdi sgraplrqfe ghtkavhtvd ftadkyhvvs
      121 gaddytvklw dipnskeilt fkehsdyvrc gcasklnpdl fitgsydhtv kmfdartses
      181 vlsvehgqpv esvllfpsgg llvsaggryv kvwdmlkggq llvslknhhk tvtclclsss
      241 gqrllsgsld rkvkvystts ykvvhsfdya asilslalah edetivvgmt ngilsvkhrk
      301 seakkeslpr rrrpayrtfi kgknymkqrd dilinrpakk hlelydrdlk hfriskaldr
      361 vldptctikt peitvsiike lnrrgvlana lagrdekeis hvlnflirnl sqprfapvli
      421 naaeiiidiy lpvigqspvv dkkflllqgl vekeidyqre lletlgmmdm lfatmrrkeg
      481 tsvlehtsdg fpenkkies
//
LOCUS       NP_054880                180 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL18m isoform 1 [Homo sapiens].
ACCESSION   NP_054880
VERSION     NP_054880.2
DBSOURCE    REFSEQ: accession NM_014161.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 180)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 180)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 180)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 180)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 180)
  AUTHORS   Brown,A., Rathore,S., Kimanius,D., Aibara,S., Bai,X.C., Rorbach,J.,
            Amunts,A. and Ramakrishnan,V.
  TITLE     Structures of the human mitochondrial ribosome in native states of
            assembly
  JOURNAL   Nat Struct Mol Biol 24 (10), 866-869 (2017)
   PUBMED   28892042
REFERENCE   6  (residues 1 to 180)
  AUTHORS   Smirnov,A., Entelis,N., Martin,R.P. and Tarassov,I.
  TITLE     Biological significance of 5S rRNA import into human mitochondria:
            role of ribosomal protein MRP-L18
  JOURNAL   Genes Dev 25 (12), 1289-1305 (2011)
   PUBMED   21685364
REFERENCE   7  (residues 1 to 180)
  AUTHORS   Zhang,Z. and Gerstein,M.
  TITLE     Identification and characterization of over 100 mitochondrial
            ribosomal protein pseudogenes in the human genome
  JOURNAL   Genomics 81 (5), 468-480 (2003)
   PUBMED   12706105
REFERENCE   8  (residues 1 to 180)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Behal,A., Touchman,J.W.,
            Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of adult human lens for the NEIBank
            Project: over 2000 non-redundant transcripts, novel genes and
            splice variants
  JOURNAL   Mol Vis 8, 171-184 (2002)
   PUBMED   12107413
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 180)
  AUTHORS   Koc,E.C., Burkhart,W., Blackburn,K., Moyer,M.B., Schlatzer,D.M.,
            Moseley,A. and Spremulli,L.L.
  TITLE     The large subunit of the mammalian mitochondrial ribosome. Analysis
            of the complement of ribosomal proteins present
  JOURNAL   J Biol Chem 276 (47), 43958-43969 (2001)
   PUBMED   11551941
REFERENCE   10 (residues 1 to 180)
  AUTHORS   Kenmochi,N., Suzuki,T., Uechi,T., Magoori,M., Kuniba,M., Higa,S.,
            Watanabe,K. and Tanaka,T.
  TITLE     The human mitochondrial ribosomal protein genes: mapping of 54
            genes to the chromosomes and implications for human disorders
  JOURNAL   Genomics 77 (1-2), 65-70 (2001)
   PUBMED   11543634
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BU932963.1, AF161556.1 and
            BC001623.1.
            
            On May 30, 2002 this sequence version replaced NP_054880.1.
            
            Summary: This nuclear gene encodes a protein component of the
            larger 39S subunit of mitochondrial ribosome. This protein may also
            aid in the import of nuclear-encoded 5S rRNA into mitochondria.
            Alternative splicing results in multiple transcript variants, most
            of which are not predicted to encode a protein. A pseudogene of
            this gene is found on chromosome 16. [provided by RefSeq, Jan
            2016].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163658.506051.1,
                                           SRR5189661.14037.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000367034.5/
                                                  ENSP00000356001.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..180
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..180
                     /product="large ribosomal subunit protein uL18m isoform 1"
                     /note="39S ribosomal protein L18, mitochondrial;
                     mitochondrial large ribosomal subunit protein uL18m"
                     /calculated_mol_wt=20445
     Region          68..170
                     /region_name="Ribosomal_L18_L5e"
                     /note="Ribosomal L18/L5e: L18 (L5e) is a ribosomal protein
                     found in the central protuberance (CP) of the large
                     subunit. L18 binds 5S rRNA and induces a conformational
                     change that stimulates the binding of L5 to 5S rRNA.
                     Association of 5S rRNA with 23S rRNA...; cd00432"
                     /db_xref="CDD:238246"
     Site            order(68,71..72,146,149,166)
                     /site_type="other"
                     /note="23S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238246"
     Site            68
                     /site_type="other"
                     /note="L21e interface [polypeptide binding]"
                     /db_xref="CDD:238246"
     Site            order(70,72..73,75,80,84..89,91,93,99..101,104,145,157)
                     /site_type="other"
                     /note="5S rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238246"
     Site            order(70,73..74)
                     /site_type="other"
                     /note="L27 interface [polypeptide binding]"
                     /db_xref="CDD:238246"
     Site            151
                     /site_type="other"
                     /note="L5 interface [polypeptide binding]"
                     /db_xref="CDD:238246"
     CDS             1..180
                     /gene="MRPL18"
                     /gene_synonym="HSPC071; L18mt; MRP-L18; uL18m"
                     /coded_by="NM_014161.5:122..664"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5270.1"
                     /db_xref="GeneID:29074"
                     /db_xref="HGNC:HGNC:14477"
                     /db_xref="MIM:611831"
ORIGIN      
        1 malrsrfwgl fsvcrnpgcr faalstssep aakpevdpve neavapeftn rnprnlells
       61 varkergwrt vfpsrefwhr lrvirtqhhv ealvehqngk vvvsastrew aikkhlystr
      121 nvvacesigr vlaqrcleag infmvyqptp weaasdsmkr lqsamteggv vlrepqriye
//
LOCUS       NP_002224                653 aa            linear   PRI 20-NOV-2025
DEFINITION  potassium voltage-gated channel subfamily A member 4 [Homo
            sapiens].
ACCESSION   NP_002224
VERSION     NP_002224.1
DBSOURCE    REFSEQ: accession NM_002233.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 653)
  AUTHORS   Kang,G.J., Xie,A., Kim,E. and Dudley,S.C. Jr.
  TITLE     miR-448 regulates potassium voltage-gated channel subfamily A
            member 4 (KCNA4) in ischemia and heart failure
  JOURNAL   Heart Rhythm 20 (5), 730-736 (2023)
   PUBMED   36693615
  REMARK    GeneRIF: miR-448 regulates potassium voltage-gated channel
            subfamily A member 4 (KCNA4) in ischemia and heart failure.
REFERENCE   2  (residues 1 to 653)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 653)
  AUTHORS   Nilsson,M., Lindstrom,S.H., Kaneko,M., Wang,K., Minguez-Vinas,T.,
            Angelini,M., Steccanella,F., Holder,D., Ottolia,M., Olcese,R. and
            Pantazis,A.
  TITLE     An epilepsy-associated KV1.2 charge-transfer-center mutation
            impairs KV1.2 and KV1.4 trafficking
  JOURNAL   Proc Natl Acad Sci U S A 119 (17), e2113675119 (2022)
   PUBMED   35439054
  REMARK    GeneRIF: An epilepsy-associated KV1.2 charge-transfer-center
            mutation impairs KV1.2 and KV1.4 trafficking.
REFERENCE   4  (residues 1 to 653)
  AUTHORS   Enyeart,J.J. and Enyeart,J.A.
  TITLE     Human adrenal glomerulosa cells express K2P and GIRK potassium
            channels that are inhibited by ANG II and ACTH
  JOURNAL   Am J Physiol Cell Physiol 321 (1), C158-C175 (2021)
   PUBMED   34038243
  REMARK    GeneRIF: Human adrenal glomerulosa cells express K2P and GIRK
            potassium channels that are inhibited by ANG II and ACTH.
REFERENCE   5  (residues 1 to 653)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 653)
  AUTHORS   Gessler,M., Grupe,A., Grzeschik,K.H. and Pongs,O.
  TITLE     The potassium channel gene HK1 maps to human chromosome 11p14.1,
            close to the FSHB gene
  JOURNAL   Hum Genet 90 (3), 319-321 (1992)
   PUBMED   1487251
REFERENCE   7  (residues 1 to 653)
  AUTHORS   Scott,H.S., Litjens,T., Hopwood,J.J. and Morris,C.P.
  TITLE     PCR detection of two RFLPs in exon I of the alpha-L-iduronidase
            (IDUA) gene
  JOURNAL   Hum Genet 90 (3), 327 (1992)
   PUBMED   1362562
REFERENCE   8  (residues 1 to 653)
  AUTHORS   Tamkun,M.M., Knoth,K.M., Walbridge,J.A., Kroemer,H., Roden,D.M. and
            Glover,D.M.
  TITLE     Molecular cloning and characterization of two voltage-gated K+
            channel cDNAs from human ventricle
  JOURNAL   FASEB J 5 (3), 331-337 (1991)
   PUBMED   2001794
REFERENCE   9  (residues 1 to 653)
  AUTHORS   Philipson,L.H., Hice,R.E., Schaefer,K., LaMendola,J., Bell,G.I.,
            Nelson,D.J. and Steiner,D.F.
  TITLE     Sequence and functional expression in Xenopus oocytes of a human
            insulinoma and islet potassium channel
  JOURNAL   Proc Natl Acad Sci U S A 88 (1), 53-57 (1991)
   PUBMED   1986382
REFERENCE   10 (residues 1 to 653)
  AUTHORS   Philipson,L.H., Schaefer,K., LaMendola,J., Bell,G.I. and
            Steiner,D.F.
  TITLE     Sequence of a human fetal skeletal muscle potassium channel cDNA
            related to RCK4
  JOURNAL   Nucleic Acids Res 18 (23), 7160 (1990)
   PUBMED   2263489
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA328650.1, AK311228.1,
            M60450.1, BE467209.1 and AC124657.5.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Potassium channels represent the most complex class of
            voltage-gated ion channels from both functional and structural
            standpoints. Their diverse functions include regulating
            neurotransmitter release, heart rate, insulin secretion, neuronal
            excitability, epithelial electrolyte transport, smooth muscle
            contraction, and cell volume. Four sequence-related potassium
            channel genes - shaker, shaw, shab, and shal - have been identified
            in Drosophila, and each has been shown to have human homolog(s).
            This gene encodes a member of the potassium channel, voltage-gated,
            shaker-related subfamily. This member contains six
            membrane-spanning domains with a shaker-type repeat in the fourth
            segment. It belongs to the A-type potassium current class, the
            members of which may be important in the regulation of the fast
            repolarizing phase of action potentials in heart and thus may
            influence the duration of cardiac action potential.[provided by
            RefSeq, Mar 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DA328650.1, SRR1660803.27947.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2142363
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000328224.7/ ENSP00000328511.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..653
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p14.1"
     Protein         1..653
                     /product="potassium voltage-gated channel subfamily A
                     member 4"
                     /note="shaker-related potassium channel Kv1.4; type A
                     potassium channel; rapidly inactivating potassium channel;
                     potassium channel, voltage gated shaker related subfamily
                     A, member 4; fetal skeletal muscle potassium channel;
                     cardiac potassium channel; potassium channel 2;
                     voltage-gated K(+) channel HuKII; voltage-gated potassium
                     channel HK1; voltage-gated potassium channel HBK4;
                     voltage-gated potassium channel subunit Kv1.4"
                     /calculated_mol_wt=73127
     Region          1..>37
                     /region_name="K_channel_TID"
                     /note="Potassium channel Kv1.4 tandem inactivation domain;
                     pfam07941"
                     /db_xref="CDD:429748"
     Region          24..148
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            90
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q61423; propagated from
                     UniProtKB/Swiss-Prot (P22459.2)"
     Region          176..303
                     /region_name="BTB_POZ"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain superfamily; cl38908"
                     /db_xref="CDD:453885"
     Site            305..326
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Region          306..570
                     /region_name="Ion_trans"
                     /note="Ion transport protein; pfam00520"
                     /db_xref="CDD:459842"
     Site            352
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P22459.2)"
     Site            371..392
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            404..424
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            440..460
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Region          462..475
                     /region_name="S4-S5 linker.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            476..497
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Region          524..529
                     /region_name="Selectivity filter.
                     /evidence=ECO:0000250|UniProtKB:P63142"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            539..567
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Site            599
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Region          629..653
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     Region          651..653
                     /region_name="PDZ-binding.
                     /evidence=ECO:0000250|UniProtKB:P15385"
                     /note="propagated from UniProtKB/Swiss-Prot (P22459.2)"
     CDS             1..653
                     /gene="KCNA4"
                     /gene_synonym="HBK4; HK1; HPCN2; HUKII; KCNA4L; KCNA8;
                     KV1.4; MCIDDS; PCN2"
                     /coded_by="NM_002233.4:1242..3203"
                     /db_xref="CCDS:CCDS41629.1"
                     /db_xref="GeneID:3739"
                     /db_xref="HGNC:HGNC:6222"
                     /db_xref="MIM:176266"
ORIGIN      
        1 mevamvsaes sgcnshmpyg yaaqararer erlahsraaa aaavaaataa vegsggsggg
       61 shhhhqsrga ctshdpqssr gsrrrrrqrs ekkkahyrqs sfphcsdlmp sgseekilre
      121 lseeeedeee eeeeeeegrf yyseddhgde csytdllpqd eggggyssvr ysdccervvi
      181 nvsglrfetq mktlaqfpet llgdpekrtq yfdplrneyf fdrnrpsfda ilyyyqsggr
      241 lkrpvnvpfd ifteevkfyq lgeeallkfr edegfvreee dralpenefk kqiwllfeyp
      301 essspargia ivsvlvilis ivifcletlp efrddrdlvm alsagghggl lndtsaphle
      361 nsghtifndp ffivetvciv wfsfefvvrc facpsqalff knimniidiv silpyfitlg
      421 tdlaqqqggg ngqqqqamsf ailriirlvr vfrifklsrh skglqilght lrasmrelgl
      481 lifflfigvi lfssavyfae adeptthfqs ipdafwwavv tmttvgygdm kpitvggkiv
      541 gslcaiagvl tialpvpviv snfnyfyhre teneeqtqlt qnavscpylp snllkkfrss
      601 tssslgdkse ylemeegvke slcakeekcq gkgddsetdk nncsnakave tdv
//
LOCUS       NP_690610                314 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 6 isoform 2
            precursor [Homo sapiens].
ACCESSION   NP_690610
VERSION     NP_690610.1
DBSOURCE    REFSEQ: accession NM_152871.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 314)
  AUTHORS   Bartels,N., van der Voort,N.T.M., Opanasyuk,O., Felekyan,S.,
            Greife,A., Shang,X., Bister,A., Wiek,C., Seidel,C.A.M. and
            Monzel,C.
  TITLE     Advanced multiparametric image spectroscopy and super-resolution
            microscopy reveal a minimal model of CD95 signal initiation
  JOURNAL   Sci Adv 10 (35), eadn3238 (2024)
   PUBMED   39213362
  REMARK    GeneRIF: Advanced multiparametric image spectroscopy and
            super-resolution microscopy reveal a minimal model of CD95 signal
            initiation.
REFERENCE   2  (residues 1 to 314)
  AUTHORS   Liu,Y., Sardana,R., Nemirovsky,D., Frosina,D., Jungbluth,A.,
            Johnson,W.T., Vardhana,S., Arcila,M., Horwitz,S.M., Derkach,A.,
            Dogan,A. and Xiao,W.
  TITLE     Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma
  JOURNAL   Blood Adv 8 (12), 3064-3075 (2024)
   PUBMED   38593227
  REMARK    GeneRIF: Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma.
REFERENCE   3  (residues 1 to 314)
  AUTHORS   Yang,Z., Zhang,X., Zhang,X., Liu,Y., Zhang,J. and Yuan,X.
  TITLE     [Porphyromonas gingivalis infection facilitates immune escape of
            esophageal cancer by enhancing YTHDF2-mediated Fas degradation]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (6), 1159-1165 (2024)
   PUBMED   38977346
  REMARK    GeneRIF: [Porphyromonas gingivalis infection facilitates immune
            escape of esophageal cancer by enhancing YTHDF2-mediated Fas
            degradation].
REFERENCE   4  (residues 1 to 314)
  AUTHORS   Staniek,J., Kalina,T., Andrieux,G., Boerries,M., Janowska,I.,
            Fuentes,M., Diez,P., Bakardjieva,M., Stancikova,J., Raabe,J.,
            Neumann,J., Schwenk,S., Arpesella,L., Stuchly,J., Benes,V., Garcia
            Valiente,R., Fernandez Garcia,J., Carsetti,R., Piano Mortari,E.,
            Catala,A., de la Calle,O., Sogkas,G., Neven,B., Rieux-Laucat,F.,
            Magerus,A., Neth,O., Olbrich,P., Voll,R.E., Alsina,L.,
            Allende,L.M., Gonzalez-Granado,L.I., Bohler,C., Thiel,J.,
            Venhoff,N., Lorenzetti,R., Warnatz,K., Unger,S., Seidl,M.,
            Mielenz,D., Schneider,P., Ehl,S., Rensing-Ehl,A., Smulski,C.R. and
            Rizzi,M.
  TITLE     Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells
  JOURNAL   Sci Immunol 9 (91), eadj5948 (2024)
   PUBMED   38215192
  REMARK    GeneRIF: Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells.
REFERENCE   5  (residues 1 to 314)
  AUTHORS   Jenkins,M., Keir,M. and McCune,J.M.
  TITLE     A membrane-bound Fas decoy receptor expressed by human thymocytes
  JOURNAL   J Biol Chem 275 (11), 7988-7993 (2000)
   PUBMED   10713117
REFERENCE   6  (residues 1 to 314)
  AUTHORS   Cascino,I., Papoff,G., Eramo,A. and Ruberti,G.
  TITLE     Soluble Fas/Apo-1 splicing variants and apoptosis
  JOURNAL   Front Biosci 1, d12-d18 (1996)
   PUBMED   9159204
  REMARK    GeneRIF: A review of alternative spliced APO-1 variants and their
            possible biological roles.
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 314)
  AUTHORS   Cheng,J., Zhou,T., Liu,C., Shapiro,J.P., Brauer,M.J., Kiefer,M.C.,
            Barr,P.J. and Mountz,J.D.
  TITLE     Protection from Fas-mediated apoptosis by a soluble form of the Fas
            molecule
  JOURNAL   Science 263 (5154), 1759-1762 (1994)
   PUBMED   7510905
REFERENCE   8  (residues 1 to 314)
  AUTHORS   Bleesing,J.J.H., Nagaraj,C.B. and Zhang,K.
  TITLE     Autoimmune Lymphoproliferative Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301287
REFERENCE   9  (residues 1 to 314)
  AUTHORS   Inazawa,J., Itoh,N., Abe,T. and Nagata,S.
  TITLE     Assignment of the human Fas antigen gene (Fas) to 10q24.1
  JOURNAL   Genomics 14 (3), 821-822 (1992)
   PUBMED   1385309
REFERENCE   10 (residues 1 to 314)
  AUTHORS   Oehm,A., Behrmann,I., Falk,W., Pawlita,M., Maier,G., Klas,C.,
            Li-Weber,M., Richards,S., Dhein,J., Trauth,B.C. et al.
  TITLE     Purification and molecular cloning of the APO-1 cell surface
            antigen, a member of the tumor necrosis factor/nerve growth factor
            receptor superfamily. Sequence identity with the Fas antigen
  JOURNAL   J Biol Chem 267 (15), 10709-10715 (1992)
   PUBMED   1375228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA699562.1, Z47993.1,
            AK290978.1, BC012479.1, AL157394.15, AK026195.1 and BU620333.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains a death domain. It
            has been shown to play a central role in the physiological
            regulation of programmed cell death, and has been implicated in the
            pathogenesis of various malignancies and diseases of the immune
            system. The interaction of this receptor with its ligand allows the
            formation of a death-inducing signaling complex that includes
            Fas-associated death domain protein (FADD), caspase 8, and caspase
            10. The autoproteolytic processing of the caspases in the complex
            triggers a downstream caspase cascade, and leads to apoptosis. This
            receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and
            MAPK8/JNK, and is found to be involved in transducing the
            proliferating signals in normal diploid fibroblast and T cells.
            Several alternatively spliced transcript variants have been
            described, some of which are candidates for nonsense-mediated mRNA
            decay (NMD). The isoforms lacking the transmembrane domain may
            negatively regulate the apoptosis mediated by the full length
            isoform. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (2), also known as FasdeltaTM or
            soluble FAS, lacks an alternate in-frame exon in the 3' coding
            region, compared to variant 1. The resulting isoform (2) lacks an
            internal region, compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660807.106226.1,
                                           SRR1803616.29670.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..314
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..314
                     /product="tumor necrosis factor receptor superfamily
                     member 6 isoform 2 precursor"
                     /note="tumor necrosis factor receptor superfamily, member
                     6; APO-1 cell surface antigen; apoptosis antigen 1; Fas
                     AMA; CD95 antigen; FASLG receptor; apoptosis-mediating
                     surface antigen FAS; apoptosis signaling receptor FAS; Fas
                     (TNF receptor superfamily, member 6); TNF receptor
                     superfamily member 6; mutant tumor necrosis receptor
                     superfamily member 6"
                     /calculated_mol_wt=32734
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2670
     Region          39..167
                     /region_name="TNFRSF6"
                     /note="Tumor necrosis factor receptor superfamily member 6
                     (TNFRSF6), also known as fas cell surface death receptor
                     (Fas); cd10579"
                     /db_xref="CDD:276905"
     Region          48..82
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276905"
     Site            order(59..65,94..97,102)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276905"
     Region          85..127
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276905"
     Region          129..149
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276905"
     Region          205..298
                     /region_name="Death_FAS_TNFRSF6"
                     /note="Death domain of FAS or TNF receptor superfamily
                     member 6; cd08316"
                     /db_xref="CDD:260028"
     Site            order(207..208,210..211,214..215,217..218,230,263..265,
                     267..268,270,273..275,277..279,281,284..288,290,293..294)
                     /site_type="other"
                     /note="FAS-FADD heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:260028"
     Site            order(230,286..287,290,294,297..298)
                     /site_type="other"
                     /note="octamer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     Site            order(275,278,282,285..286,293,296..297)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     CDS             1..314
                     /gene="FAS"
                     /gene_synonym="ALPS1A; APO-1; APT1; CD95; FAS1; FASTM;
                     TNFRSF6"
                     /coded_by="NM_152871.4:80..1024"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS7394.1"
                     /db_xref="GeneID:355"
                     /db_xref="HGNC:HGNC:11920"
                     /db_xref="MIM:134637"
ORIGIN      
        1 mlgiwtllpl vltsvarlss ksvnaqvtdi nskglelrkt vttvetqnle glhhdgqfch
       61 kpcppgerka rdctvngdep dcvpcqegke ytdkahfssk crrcrlcdeg hgleveinct
      121 rtqntkcrck pnffcnstvc ehcdpctkce hgiikectlt sntkckeevk rkevqktcrk
      181 hrkenqgshe sptlnpetva inlsdvdlsk yittiagvmt lsqvkgfvrk ngvneakide
      241 ikndnvqdta eqkvqllrnw hqlhgkkeay dtlikdlkka nlctlaekiq tiilkditsd
      301 sensnfrnei qslv
//
LOCUS       NP_001531                205 aa            linear   PRI 20-NOV-2025
DEFINITION  heat shock protein beta-1 [Homo sapiens].
ACCESSION   NP_001531
VERSION     NP_001531.1
DBSOURCE    REFSEQ: accession NM_001540.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Meng,J., Fang,J., Bao,Y., Chen,H., Hu,X., Wang,Z., Li,M., Cheng,Q.,
            Dong,Y., Yang,X., Zou,Y., Zhao,D., Tang,J., Zhang,W. and Chen,C.
  TITLE     The biphasic role of Hspb1 on ferroptotic cell death in Parkinson's
            disease
  JOURNAL   Theranostics 14 (12), 4643-4666 (2024)
   PUBMED   39239519
  REMARK    GeneRIF: The biphasic role of Hspb1 on ferroptotic cell death in
            Parkinson's disease.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 205)
  AUTHORS   Tieliwaerdi,A., Aini,A., Amuti,M., Aierken,Y., Nijiati,M. and
            Luo,B.
  TITLE     STUB1 promotes the degradation of HSPB1 and induces ferroptosis in
            lung cancer cells
  JOURNAL   Environ Toxicol 39 (8), 4156-4170 (2024)
   PUBMED   38661247
  REMARK    GeneRIF: STUB1 promotes the degradation of HSPB1 and induces
            ferroptosis in lung cancer cells.
REFERENCE   4  (residues 1 to 205)
  AUTHORS   Homa,K. and Zur-Wyrozumska,K.
  TITLE     HSPB1 mutation causing distal Hereditary Motor Neuropathy type 2B
            in a Polish family
  JOURNAL   Folia Med Cracov 63 (4), 57-61 (2023)
   PUBMED   38578345
  REMARK    GeneRIF: HSPB1 mutation causing distal Hereditary Motor Neuropathy
            type 2B in a Polish family.
REFERENCE   5  (residues 1 to 205)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Hereditary Neuropathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301532
REFERENCE   6  (residues 1 to 205)
  AUTHORS   Bird,T.D.
  TITLE     Charcot-Marie-Tooth Neuropathy Type 2 - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301462
REFERENCE   7  (residues 1 to 205)
  AUTHORS   Stokoe,D., Engel,K., Campbell,D.G., Cohen,P. and Gaestel,M.
  TITLE     Identification of MAPKAP kinase 2 as a major enzyme responsible for
            the phosphorylation of the small mammalian heat shock proteins
  JOURNAL   FEBS Lett 313 (3), 307-313 (1992)
   PUBMED   1332886
REFERENCE   8  (residues 1 to 205)
  AUTHORS   Dawson,S.J. and White,L.A.
  TITLE     Treatment of Haemophilus aphrophilus endocarditis with
            ciprofloxacin
  JOURNAL   J Infect 24 (3), 317-320 (1992)
   PUBMED   1602151
REFERENCE   9  (residues 1 to 205)
  AUTHORS   Kato,K., Shinohara,H., Goto,S., Inaguma,Y., Morishita,R. and
            Asano,T.
  TITLE     Copurification of small heat shock protein with alpha B crystallin
            from human skeletal muscle
  JOURNAL   J Biol Chem 267 (11), 7718-7725 (1992)
   PUBMED   1560006
REFERENCE   10 (residues 1 to 205)
  AUTHORS   Landry,J., Lambert,H., Zhou,M., Lavoie,J.N., Hickey,E., Weber,L.A.
            and Anderson,C.W.
  TITLE     Human HSP27 is phosphorylated at serines 78 and 82 by heat shock
            and mitogen-activated kinases that recognize the same amino acid
            motif as S6 kinase II
  JOURNAL   J Biol Chem 267 (2), 794-803 (1992)
   PUBMED   1730670
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP231480.1 and BC012768.2.
            
            Summary: This gene encodes a member of the small heat shock protein
            (HSP20) family of proteins. In response to environmental stress,
            the encoded protein translocates from the cytoplasm to the nucleus
            and functions as a molecular chaperone that promotes the correct
            folding of other proteins. This protein plays an important role in
            the differentiation of a wide variety of cell types. Expression of
            this gene is correlated with poor clinical outcome in multiple
            human cancers, and the encoded protein may promote cancer cell
            proliferation and metastasis, while protecting cancer cells from
            apoptosis. Mutations in this gene have been identified in human
            patients with Charcot-Marie-Tooth disease and distal hereditary
            motor neuropathy. [provided by RefSeq, Aug 2017].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012292.1, X54079.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000248553.7/ ENSP00000248553.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..205
                     /product="heat shock protein beta-1"
                     /note="heat shock 27kD protein 1; stress-responsive
                     protein 27; epididymis secretory protein Li 102;
                     estrogen-regulated 24 kDa protein; 28 kDa heat shock
                     protein; heat shock 27 kDa protein; heat shock 27kDa
                     protein 1; heat shock protein family B member 1"
                     /calculated_mol_wt=22651
     Site            12
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2 and MAPKAPK3.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:8774846,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P42930; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            65
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Region          70..205
                     /region_name="Interaction with TGFB1I1.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2, MAPKAPK3 and MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
                     ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
                     ECO:0000269|PubMed:8774846, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     Site            82
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by MAPKAPK2, MAPKAPK3 and MAPKAPK5.
                     /evidence=ECO:0000269|PubMed:10383393,
                     ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:15976317,
                     ECO:0000269|PubMed:1730670, ECO:0000269|PubMed:19166925,
                     ECO:0000269|PubMed:8774846, ECO:0000269|Ref.14,
                     ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Region          84..169
                     /region_name="ACD_HspB1_like"
                     /note="Alpha crystallin domain (ACD) found in mammalian
                     small (s)heat shock protein (Hsp)-27 (also denoted HspB1
                     in human) and similar proteins. sHsps are molecular
                     chaperones that suppress protein aggregation and protect
                     against cell stress, and are generally...; cd06475"
                     /db_xref="CDD:107230"
     Site            order(84..88,98,100,102..103,140,161..162)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:107230"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            98
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            123
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            174
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            176
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P04792.2)"
     Site            199
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (P04792.2)"
     CDS             1..205
                     /gene="HSPB1"
                     /gene_synonym="CMT2F; HEL-S-102; HMN2B; HMND3; HS.76067;
                     Hsp25; HSP27; HSP28; SRP27"
                     /coded_by="NM_001540.5:41..658"
                     /db_xref="CCDS:CCDS5583.1"
                     /db_xref="GeneID:3315"
                     /db_xref="HGNC:HGNC:5246"
                     /db_xref="MIM:602195"
ORIGIN      
        1 mterrvpfsl lrgpswdpfr dwyphsrlfd qafglprlpe ewsqwlggss wpgyvrplpp
       61 aaiespavaa paysralsrq lssgvseirh tadrwrvsld vnhfapdelt vktkdgvvei
      121 tgkheerqde hgyisrcftr kytlppgvdp tqvssslspe gtltveapmp klatqsneit
      181 ipvtfesraq lggpeaaksd etaak
//
LOCUS       NP_001258828             449 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B
            beta isoform isoform g [Homo sapiens].
ACCESSION   NP_001258828
VERSION     NP_001258828.1
DBSOURCE    REFSEQ: accession NM_001271899.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 449)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 449)
  AUTHORS   Shen,D. and Kang,S.
  TITLE     Comprehensive analysis of mitochondria-related genes indicates that
            PPP2R2B is a novel biomarker and promotes the progression of
            bladder cancer via Wnt signaling pathway
  JOURNAL   Biol Direct 19 (1), 17 (2024)
   PUBMED   38409085
  REMARK    GeneRIF: Comprehensive analysis of mitochondria-related genes
            indicates that PPP2R2B is a novel biomarker and promotes the
            progression of bladder cancer via Wnt signaling pathway.
            Erratum:[Biol Direct. 2024 Apr 18;19(1):27. doi:
            10.1186/s13062-024-00474-1. PMID: 38637864]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 449)
  AUTHORS   Zhou,C., Liu,H.B., Jahanbakhsh,F., Deng,L., Wu,B., Ying,M.,
            Margolis,R.L. and Li,P.P.
  TITLE     Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12
  JOURNAL   Mov Disord 38 (12), 2230-2240 (2023)
   PUBMED   37735923
  REMARK    GeneRIF: Bidirectional Transcription at the PPP2R2B Gene Locus in
            Spinocerebellar Ataxia Type 12.
REFERENCE   4  (residues 1 to 449)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 449)
  AUTHORS   Ruediger,R., Brewis,N., Ohst,K. and Walter,G.
  TITLE     Increasing the ratio of PP2A core enzyme to holoenzyme inhibits
            Tat-stimulated HIV-1 transcription and virus production
  JOURNAL   Virology 238 (2), 432-443 (1997)
   PUBMED   9400615
REFERENCE   6  (residues 1 to 449)
  AUTHORS   Tung,H.Y., De Rocquigny,H., Zhao,L.J., Cayla,X., Roques,B.P. and
            Ozon,R.
  TITLE     Direct activation of protein phosphatase-2A0 by HIV-1 encoded
            protein complex NCp7:vpr
  JOURNAL   FEBS Lett 401 (2-3), 197-201 (1997)
   PUBMED   9013886
REFERENCE   7  (residues 1 to 449)
  AUTHORS   Schalling,M., Hudson,T.J., Buetow,K.H. and Housman,D.E.
  TITLE     Direct detection of novel expanded trinucleotide repeats in the
            human genome
  JOURNAL   Nat Genet 4 (2), 135-139 (1993)
   PUBMED   8348150
REFERENCE   8  (residues 1 to 449)
  AUTHORS   Margolis,R.L., Holmes,S.E., Srivastava,A.K., Mukherji,M. and
            Sinha,K.K.
  TITLE     Spinocerebellar Ataxia Type 12 - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301381
REFERENCE   9  (residues 1 to 449)
  AUTHORS   Perlman,S.
  TITLE     Hereditary Ataxia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301317
REFERENCE   10 (residues 1 to 449)
  AUTHORS   Mayer,R.E., Hendrix,P., Cron,P., Matthies,R., Stone,S.R., Goris,J.,
            Merlevede,W., Hofsteenge,J. and Hemmings,B.A.
  TITLE     Structure of the 55-kDa regulatory subunit of protein phosphatase
            2A: evidence for a neuronal-specific isoform
  JOURNAL   Biochemistry 30 (15), 3589-3597 (1991)
   PUBMED   1849734
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX464346.2, AK295347.1,
            BC031790.1 and AI621232.1.
            
            Summary: The product of this gene belongs to the phosphatase 2
            regulatory subunit B family. Protein phosphatase 2 is one of the
            four major Ser/Thr phosphatases, and it is implicated in the
            negative control of cell growth and division. It consists of a
            common heteromeric core enzyme, which is composed of a catalytic
            subunit and a constant regulatory subunit, that associates with a
            variety of regulatory subunits. The B regulatory subunit might
            modulate substrate selectivity and catalytic activity. This gene
            encodes a beta isoform of the regulatory subunit B55 subfamily.
            Defects in this gene cause autosomal dominant spinocerebellar
            ataxia 12 (SCA12), a disease caused by degeneration of the
            cerebellum, sometimes involving the brainstem and spinal cord, and
            in resulting in poor coordination of speech and body movements.
            Multiple alternatively spliced variants, which encode different
            isoforms, have been identified for this gene. The 5' UTR of some of
            these variants includes a CAG trinucleotide repeat sequence (7-28
            copies) that can be expanded to 55-78 copies in cases of SCA12.
            [provided by RefSeq, Jul 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.199111.1,
                                           SRR1803611.83434.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..449
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..449
                     /product="serine/threonine-protein phosphatase 2A 55 kDa
                     regulatory subunit B beta isoform isoform g"
                     /EC_number="3.1.3.16"
                     /note="protein phosphatase 2, regulatory subunit B, beta"
                     /calculated_mol_wt=51935
     Region          14..444
                     /region_name="CDC55"
                     /note="Serine/threonine protein phosphatase 2A, regulatory
                     subunit [Signal transduction mechanisms]; COG5170"
                     /db_xref="CDD:227498"
     Region          33..81
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          99..176
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          182..218
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          232..283
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          290..326
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          347..382
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          421..444
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..449
                     /gene="PPP2R2B"
                     /gene_synonym="B55BETA; PP2AB55BETA; PP2ABBETA; PP2APR55B;
                     PP2APR55BETA; PR2AB55BETA; PR2ABBETA; PR2APR55BETA; PR52B;
                     PR55-BETA; PR55BETA; SCA12"
                     /coded_by="NM_001271899.1:255..1604"
                     /note="isoform g is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS64282.1"
                     /db_xref="GeneID:5521"
                     /db_xref="HGNC:HGNC:9305"
                     /db_xref="MIM:604325"
ORIGIN      
        1 mipgigtltq dtlwcfsqvk gtieigttea diistvefnh tgellatgdk ggrvvifqre
       61 qesknqvhrr geynvystfq shepefdylk sleieekink irwlpqqnaa yfllstndkt
      121 vklwkvserd krpegynlkd eegrlrdpat ittlrvpvlr pmdlmveatp rrvfanahty
      181 hinsisvnsd yetymsaddl rinlwnfeit nqsfnivdik panmeeltev itaaefhphh
      241 cntfvysssk gtirlcdmra salcdrhtkf feepedpsnr sffseiissi sdvkfshsgr
      301 yimtrdyltv kvwdlnmenr pietyqvhdy lrsklcslye ndcifdkfec vwngsdsvim
      361 tgsynnffrm fdrntkrdvt leasrenskp railkprkvc vggkrrkdei svdsldfskk
      421 ilhtawhpse niiavaatnn lyifqdkvn
//
LOCUS       NP_113611                464 aa            linear   PRI 20-NOV-2025
DEFINITION  kinetochore protein Nuf2 [Homo sapiens].
ACCESSION   NP_113611
VERSION     NP_113611.2
DBSOURCE    REFSEQ: accession NM_031423.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Bao,L., Gong,Y., Che,Y., Li,Y., Xu,T., Chen,J., Wang,S., Tan,Z.,
            Huang,P., Pan,Z. and Ge,M.
  TITLE     Maintenance of magnesium homeostasis by NUF2 promotes protein
            synthesis and anaplastic thyroid cancer progression
  JOURNAL   Cell Death Dis 15 (9), 656 (2024)
   PUBMED   39242581
  REMARK    GeneRIF: Maintenance of magnesium homeostasis by NUF2 promotes
            protein synthesis and anaplastic thyroid cancer progression.
            Erratum:[Cell Death Dis. 2024 Nov 18;15(11):842. doi:
            10.1038/s41419-024-07174-8. PMID: 39557824]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Aimaier,R., Chung,M.H., Gu,Y., Yu,Q., Wei,C., Li,H., Guo,Z.,
            Long,M., Li,Y., Wang,W., Li,Q. and Wang,Z.
  TITLE     FOXM1 promotes neurofibromatosis type 1-associated malignant
            peripheral nerve sheath tumor progression in a NUF2-dependent
            manner
  JOURNAL   Cancer Gene Ther 30 (10), 1390-1402 (2023)
   PUBMED   37488294
  REMARK    GeneRIF: FOXM1 promotes neurofibromatosis type 1-associated
            malignant peripheral nerve sheath tumor progression in a
            NUF2-dependent manner.
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Zheng,B., Wang,S., Yuan,X., Zhang,J., Shen,Z. and Ge,C.
  TITLE     NUF2 is correlated with a poor prognosis and immune infiltration in
            clear cell renal cell carcinoma
  JOURNAL   BMC Urol 23 (1), 82 (2023)
   PUBMED   37138262
  REMARK    GeneRIF: NUF2 is correlated with a poor prognosis and immune
            infiltration in clear cell renal cell carcinoma.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Shan,J., Jiang,W., Chang,J., Zhou,T., Chen,Y., Zhang,Y., Wang,J.,
            Wang,Y., Wang,Y., Xu,X., Liu,S., Shi,X., Fan,S., Chen,R., Li,C. and
            Li,X.
  TITLE     NUF2 Drives Cholangiocarcinoma Progression and Migration via
            Inhibiting Autophagic Degradation of TFR1
  JOURNAL   Int J Biol Sci 19 (5), 1336-1351 (2023)
   PUBMED   37056930
  REMARK    GeneRIF: NUF2 Drives Cholangiocarcinoma Progression and Migration
            via Inhibiting Autophagic Degradation of TFR1.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Tien,A.C., Lin,M.H., Su,L.J., Hong,Y.R., Cheng,T.S., Lee,Y.C.,
            Lin,W.J., Still,I.H. and Huang,C.Y.
  TITLE     Identification of the substrates and interaction proteins of aurora
            kinases from a protein-protein interaction model
  JOURNAL   Mol Cell Proteomics 3 (1), 93-104 (2004)
   PUBMED   14602875
REFERENCE   7  (residues 1 to 464)
  AUTHORS   DeLuca,J.G., Howell,B.J., Canman,J.C., Hickey,J.M., Fang,G. and
            Salmon,E.D.
  TITLE     Nuf2 and Hec1 are required for retention of the checkpoint proteins
            Mad1 and Mad2 to kinetochores
  JOURNAL   Curr Biol 13 (23), 2103-2109 (2003)
   PUBMED   14654001
REFERENCE   8  (residues 1 to 464)
  AUTHORS   DeLuca,J.G., Moree,B., Hickey,J.M., Kilmartin,J.V. and Salmon,E.D.
  TITLE     hNuf2 inhibition blocks stable kinetochore-microtubule attachment
            and induces mitotic cell death in HeLa cells
  JOURNAL   J Cell Biol 159 (4), 549-555 (2002)
   PUBMED   12438418
  REMARK    GeneRIF: Data highlight a specific role for hNuf2 in
            kinetochore-microtubule attachment and suggest that hNuf2 is part
            of a molecular linker between the kinetochore attachment site and
            tubulin subunits within the lattice of attached plus ends.
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Nabetani,A., Koujin,T., Tsutsumi,C., Haraguchi,T. and Hiraoka,Y.
  TITLE     A conserved protein, Nuf2, is implicated in connecting the
            centromere to the spindle during chromosome segregation: a link
            between the kinetochore function and the spindle checkpoint
  JOURNAL   Chromosoma 110 (5), 322-334 (2001)
   PUBMED   11685532
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Wigge,P.A. and Kilmartin,J.V.
  TITLE     The Ndc80p complex from Saccharomyces cerevisiae contains conserved
            centromere components and has a function in chromosome segregation
  JOURNAL   J Cell Biol 152 (2), 349-360 (2001)
   PUBMED   11266451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL592435.2 and BC008489.1.
            
            On Nov 15, 2006 this sequence version replaced NP_113611.1.
            
            Summary: This gene encodes a protein that is highly similar to
            yeast Nuf2, a component of a conserved protein complex associated
            with the centromere. Yeast Nuf2 disappears from the centromere
            during meiotic prophase when centromeres lose their connection to
            the spindle pole body, and plays a regulatory role in chromosome
            segregation. The encoded protein is found to be associated with
            centromeres of mitotic HeLa cells, which suggests that this protein
            is a functional homolog of yeast Nuf2. Alternatively spliced
            transcript variants that encode the same protein have been
            described. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. Variants 1 and 2 encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC008489.1, AF326731.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23.3"
     Protein         1..464
                     /product="kinetochore protein Nuf2"
                     /note="cancer/testis antigen 106; cell division cycle
                     associated 1; hNuf2; hNuf2R; hsNuf2; cell division
                     cycle-associated protein 1; NUF2, NDC80 kinetochore
                     complex component, homolog; NDC80 kinetochore complex
                     component NUF2"
                     /calculated_mol_wt=54173
     Region          1..385
                     /region_name="Interaction with the N-terminus of NDC80"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD4.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9BZD4.2)"
     Region          3..146
                     /region_name="Nuf2"
                     /note="Nuf2 family; pfam03800"
                     /db_xref="CDD:461057"
     Region          144..>370
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZD4.2)"
     Site            247
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9BZD4.2)"
     Region          309..>458
                     /region_name="DR0291"
                     /note="Predicted nucleic acid-binding protein DR0291,
                     contains C4-type Zn-ribbon domain [General function
                     prediction only]; COG1579"
                     /db_xref="CDD:441187"
     Region          386..464
                     /region_name="Interaction with the C-terminus of NDC80 and
                     the SPBC24-SPBC25 subcomplex"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9BZD4.2)"
     CDS             1..464
                     /gene="NUF2"
                     /gene_synonym="CDCA1; CT106; NUF2R"
                     /coded_by="NM_031423.4:134..1528"
                     /db_xref="CCDS:CCDS1245.1"
                     /db_xref="GeneID:83540"
                     /db_xref="HGNC:HGNC:14621"
                     /db_xref="MIM:611772"
ORIGIN      
        1 metlsfpryn vaeivihirn kiltgadgkn ltkndlypnp kpevlhmiym ralqivygir
       61 lehfymmpvn sevmyphlme gflpfsnlvt hldsflpicr vndfetadil cpkakrtsrf
      121 lsgiinfihf reacretyme flwqykssad kmqqlnaahq ealmklerld svpveeqeef
      181 kqlsdgiqel qqslnqdfhq ktivlqegns qkksnisekt krlnelklsv vslkeiqesl
      241 ktkivdspek lknykekmkd tvqklknarq evvekyeiyg dsvdclpscq levqlyqkki
      301 qdlsdnrekl asilkeslnl edqiesdese lkklkteens fkrlmivkke klataqfkin
      361 kkhedvkqyk rtviedcnkv qekrgavyer vttinqeiqk iklgiqqlkd aaereklksq
      421 eiflnlktal ekyhdgieka aedsyakide ktaelkrkmf kmst
//
LOCUS       NP_001317449            1913 aa            linear   PRI 20-NOV-2025
DEFINITION  trinucleotide repeat-containing gene 6A protein isoform 2 [Homo
            sapiens].
ACCESSION   NP_001317449 XP_005255311
VERSION     NP_001317449.1
DBSOURCE    REFSEQ: accession NM_001330520.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1913)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1913)
  AUTHORS   Li,M., Zhai,P., Mu,X., Song,J., Zhang,H. and Su,J.
  TITLE     Hypoxic BMSC-derived exosomal miR-652-3p promotes proliferation and
            metastasis of hepatocarcinoma cancer cells via targeting TNRC6A
  JOURNAL   Aging (Albany NY) 15 (22), 12780-12793 (2023)
   PUBMED   37976119
  REMARK    GeneRIF: Hypoxic BMSC-derived exosomal miR-652-3p promotes
            proliferation and metastasis of hepatocarcinoma cancer cells via
            targeting TNRC6A.
REFERENCE   3  (residues 1 to 1913)
  AUTHORS   Majerciak,V., Zhou,T., Kruhlak,M.J. and Zheng,Z.M.
  TITLE     RNA helicase DDX6 and scaffold protein GW182 in P-bodies promote
            biogenesis of stress granules
  JOURNAL   Nucleic Acids Res 51 (17), 9337-9355 (2023)
   PUBMED   37427791
  REMARK    GeneRIF: RNA helicase DDX6 and scaffold protein GW182 in P-bodies
            promote biogenesis of stress granules.
REFERENCE   4  (residues 1 to 1913)
  AUTHORS   Yang,R., Han,J. and Zhao,S.
  TITLE     LINC01082 Inhibits Non-Small Cell Lung Cancer by Targeting the
            miR-543/TNRC6A Axis
  JOURNAL   Biochem Genet 61 (4), 1585-1605 (2023)
   PUBMED   36719626
  REMARK    GeneRIF: LINC01082 Inhibits Non-Small Cell Lung Cancer by Targeting
            the miR-543/TNRC6A Axis.
REFERENCE   5  (residues 1 to 1913)
  AUTHORS   Chen,W., Ru,J., Wu,T., Man,D., Wu,J., Wu,L., Sun,Y., Yu,H., Li,M.,
            Zhang,G., Zhu,X., Tong,R., Xiao,H., Li,Y. and Yang,B.
  TITLE     MiR-652-3p promotes malignancy and metastasis of cancer cells via
            inhibiting TNRC6A in hepatocellular carcinoma
  JOURNAL   Biochem Biophys Res Commun 640, 1-11 (2023)
   PUBMED   36495604
  REMARK    GeneRIF: MiR-652-3p promotes malignancy and metastasis of cancer
            cells via inhibiting TNRC6A in hepatocellular carcinoma.
REFERENCE   6  (residues 1 to 1913)
  AUTHORS   Eystathioy,T., Jakymiw,A., Chan,E.K., Seraphin,B., Cougot,N. and
            Fritzler,M.J.
  TITLE     The GW182 protein colocalizes with mRNA degradation associated
            proteins hDcp1 and hLSm4 in cytoplasmic GW bodies
  JOURNAL   RNA 9 (10), 1171-1173 (2003)
   PUBMED   13130130
REFERENCE   7  (residues 1 to 1913)
  AUTHORS   Eystathioy,T., Chan,E.K., Mahler,M., Luft,L.M., Fritzler,M.L. and
            Fritzler,M.J.
  TITLE     A panel of monoclonal antibodies to cytoplasmic GW bodies and the
            mRNA binding protein GW182
  JOURNAL   Hybrid Hybridomics 22 (2), 79-86 (2003)
   PUBMED   12831532
REFERENCE   8  (residues 1 to 1913)
  AUTHORS   Eystathioy,T., Chan,E.K., Tenenbaum,S.A., Keene,J.D., Griffith,K.
            and Fritzler,M.J.
  TITLE     A phosphorylated cytoplasmic autoantigen, GW182, associates with a
            unique population of human mRNAs within novel cytoplasmic speckles
  JOURNAL   Mol Biol Cell 13 (4), 1338-1351 (2002)
   PUBMED   11950943
  REMARK    GeneRIF: GW ribonucleoprotein complex is involved in the
            posttranscriptional regulation of gene expression
REFERENCE   9  (residues 1 to 1913)
  AUTHORS   Margolis,R.L., Abraham,M.R., Gatchell,S.B., Li,S.H., Kidwai,A.S.,
            Breschel,T.S., Stine,O.C., Callahan,C., McInnis,M.G. and Ross,C.A.
  TITLE     cDNAs with long CAG trinucleotide repeats from human brain
  JOURNAL   Hum Genet 100 (1), 114-122 (1997)
   PUBMED   9225980
REFERENCE   10 (residues 1 to 1913)
  AUTHORS   Yamagata,K., Takeda,J., Menzel,S., Chen,X., Eng,S., Lim,L.R.,
            Concannon,P., Hanis,C.L., Spielman,R.S., Cox,N.J. and Bell,G.I.
  TITLE     Searching for NIDDM susceptibility genes: studies of genes with
            triplet repeats expressed in skeletal muscle
  JOURNAL   Diabetologia 39 (6), 725-730 (1996)
   PUBMED   8781769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002565.1, AC008731.8 and
            BU743266.1.
            
            On Aug 26, 2016 this sequence version replaced XP_005255311.1.
            
            Summary: This gene encodes a member of the trinucleotide repeat
            containing 6 protein family. The protein functions in
            post-transcriptional gene silencing through the RNA interference
            (RNAi) and microRNA pathways. The protein associates with messenger
            RNAs and Argonaute proteins in cytoplasmic bodies known as
            GW-bodies or P-bodies. Inhibiting expression of this gene
            delocalizes other GW-body proteins and impairs RNAi and
            microRNA-induced gene silencing. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the 3' coding region, compared to variant 1. The encoded
            isoform (2) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.53998.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..1913
                     /product="trinucleotide repeat-containing gene 6A protein
                     isoform 2"
                     /note="CAG repeat protein 26; glycine-tryptophan protein
                     of 182 kDa; trinucleotide repeat-containing gene 6A
                     protein; EDIE; GW182 autoantigen; EMSY interactor protein;
                     CTD-2540M10.1; trinucleotide repeat containing 6A"
                     /calculated_mol_wt=205021
     Region          <405..>693
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          <622..>860
                     /region_name="ser_rich_anae_1"
                     /note="serine-rich protein; NF033849"
                     /db_xref="CDD:468206"
     Region          1075..1202
                     /region_name="Ago_hook"
                     /note="Argonaute hook; pfam10427"
                     /db_xref="CDD:463088"
     Region          <1280..1432
                     /region_name="M_domain"
                     /note="M domain of GW182; pfam12938"
                     /db_xref="CDD:432890"
     Region          1457..1718
                     /region_name="TNRC6-PABC_bdg"
                     /note="TNRC6-PABC binding domain; pfam16608"
                     /db_xref="CDD:465195"
     Region          1726..1817
                     /region_name="RRM_TNRC6A"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     GW182 autoantigen; cd12711"
                     /db_xref="CDD:410110"
     CDS             1..1913
                     /gene="TNRC6A"
                     /gene_synonym="CAGH26; FAME6; GW1; GW182; TNRC6"
                     /coded_by="NM_001330520.3:192..5933"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81959.1"
                     /db_xref="GeneID:27327"
                     /db_xref="HGNC:HGNC:11969"
                     /db_xref="MIM:610739"
ORIGIN      
        1 mreleakatk dvernlsrdl vqeeeqlmee kkkkkddkkk keaaqkkate qkikvpeqik
       61 psvsqpqpan snngtstats tnnnakrata nnqqpqqqqq qqqpqqqqpq qqpqpqpqqq
      121 qpqqqpqalp ryprevpprf rhqehkqllk rgqhfpviaa nlgsavkvln sqsessaltn
      181 qqpqnngevq nsknqsdinh stsgshyens qrgpvsstsd sstncknavv sdlsekeawp
      241 sapgsdpela secmdadsas sseserniti masgntggek dglrnstglg sqnkfvvgss
      301 snnvghgsst gpwgfshgai istcqvsvda pesksessnn rmnawgtvss ssngglnpst
      361 lnsasnhgaw pvlennglal kgpvgsgssg iniqcstigq mpnnqsinsk vsggsthgtw
      421 gslqetcese vsgtqkvsfs gqpqnittem tgpnnttnfm tsslpnsgsv qnnelpssnt
      481 gawrvstmnh pqmqapsgmn gtslshlsng esksggsygt twgaygsnys gdkcsgpngq
      541 angdtvnatl mqpgvngpmg tnfqvntnkg ggvwesgaan sqstswgsgn gansggsrrg
      601 wgtpaqntgt nlpsvewnkl psnqhsndsa ngngktftng wksteeedqg satsqtneqs
      661 svwaktggtv esdgstestg rleekgtges qsrdrrkidq htllqsivnr tdldprvlsn
      721 sgwgqtpikq ntawdtetsp rgerktdngt eawgssatqt fnsgacidkt spngndtssv
      781 sgwgdpkpal rwgdskgsnc qggweddsaa tgmvksnqwg nckeekaawn dsqknkqgwg
      841 dgqkssqgws vsasdnwget srnnhwgean kksssggsds drsvsgwnel gktssftwgn
      901 ninpnnssgw desskptpsq gwgdppksnq slgwgdsskp vsspdwnkqq divgswgipp
      961 atgkppgtgw lggpipapak eeeptgweep spesirrkme iddgtsawgd pskynyknvn
     1021 mwnknvpngn srsdqqaqvh qlltpasais nkeassgsgw gepwgepstp attvdngtsa
     1081 wgkpidsgps wgepiaaass tstwgsssvg pqalsksgpk smqdgwcgdd mplpgnrptg
     1141 weeeedveig mwnsnssqel nsslnwppyt kkmsskglsg kkrrrergmm kggnkqeeaw
     1201 inpfvkqfsn isfsrdspee nvqsnkmdls ggmlqdkrme idkhslnigd ynrtvgkgpg
     1261 srpqiskess mernpyfdkn gnpsmfgvgn taaqprgmqq ppaqplsssq pnlraqvppp
     1321 llspqvpvsl lkyapnnggl nplfgpqqva mlnqlsqlnq lsqisqlqrl laqqqraqsq
     1381 rsvpsgnrpq qdqqgrplsv qqqmmqqsrq ldpnllvkqq tppsqqqplh qpamksfldn
     1441 vmphttpelq kgpspinafs nfpiglnsnl nvnmdmnsik epqsrlrkwt tvdsisvnts
     1501 ldqnsskhga issgfrlees pfvpydfmns stspasppgs igdgwpraks pngsssvnwp
     1561 pefrpgepwk gypnidpetd pyvtpgsvin nlsintvrev dhlrdrnsgs ssslnttlps
     1621 tsawssiras nynvplssta qstsarnsds kltwspgsvt ntslahelwk vplppknita
     1681 psrpppgltg qkpplstwdn splrigggwg nsdarytpgs swgesssgri tnwlvlknlt
     1741 pqidgstlrt lcmqhgplit fhlnlphgna lvrysskeev vkaqkslhmc vlgnttilae
     1801 faseeeisrf faqsqsltps pgwqslgssq srlgsldcsh sfssrtdlnh wngaglsgtn
     1861 cgdlhgtslw gtphystslw gppsssdprg isspspinaf lsvdhlgggg esm
//
LOCUS       NP_003792                621 aa            linear   PRI 20-NOV-2025
DEFINITION  GPI-anchor transamidase component GPAA1 [Homo sapiens].
ACCESSION   NP_003792
VERSION     NP_003792.1
DBSOURCE    REFSEQ: accession NM_003801.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 621)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 621)
  AUTHORS   Xu,Y., Li,T., Zhou,Z., Hong,J., Chao,Y., Zhu,Z., Zhang,Y., Qu,Q.
            and Li,D.
  TITLE     Structures of liganded glycosylphosphatidylinositol transamidase
            illuminate GPI-AP biogenesis
  JOURNAL   Nat Commun 14 (1), 5520 (2023)
   PUBMED   37684232
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 621)
  AUTHORS   Xu,Y., Jia,G., Li,T., Zhou,Z., Luo,Y., Chao,Y., Bao,J., Su,Z.,
            Qu,Q. and Li,D.
  TITLE     Molecular insights into biogenesis of glycosylphosphatidylinositol
            anchor proteins
  JOURNAL   Nat Commun 13 (1), 2617 (2022)
   PUBMED   35551457
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 621)
  AUTHORS   Zhang,H., Su,J., Li,B., Gao,Y., Liu,M., He,L., Xu,H., Dong,Y.,
            Zhang,X.C. and Zhao,Y.
  TITLE     Structure of human glycosylphosphatidylinositol transamidase
  JOURNAL   Nat Struct Mol Biol 29 (3), 203-209 (2022)
   PUBMED   35165458
REFERENCE   5  (residues 1 to 621)
  AUTHORS   Liu,S.S., Jin,F., Liu,Y.S., Murakami,Y., Sugita,Y., Kato,T.,
            Gao,X.D., Kinoshita,T., Hattori,M. and Fujita,M.
  TITLE     Functional Analysis of the GPI Transamidase Complex by Screening
            for Amino Acid Mutations in Each Subunit
  JOURNAL   Molecules 26 (18), 5462 (2021)
   PUBMED   34576938
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 621)
  AUTHORS   Ohishi,K., Inoue,N., Maeda,Y., Takeda,J., Riezman,H. and
            Kinoshita,T.
  TITLE     Gaa1p and gpi8p are components of a glycosylphosphatidylinositol
            (GPI) transamidase that mediates attachment of GPI to proteins
  JOURNAL   Mol Biol Cell 11 (5), 1523-1533 (2000)
   PUBMED   10793132
REFERENCE   7  (residues 1 to 621)
  AUTHORS   Inoue,N., Ohishi,K., Endo,Y., Fujita,T., Takeda,J. and Kinoshita,T.
  TITLE     Human and mouse GPAA1 (Glycosylphosphatidylinositol anchor
            attachment 1) genes: genomic structures, chromosome loci and the
            presence of a minor class intron
  JOURNAL   Cytogenet Cell Genet 84 (3-4), 199-205 (1999)
   PUBMED   10393431
REFERENCE   8  (residues 1 to 621)
  AUTHORS   Hiroi,Y., Komuro,I., Matsushita,I., Aburatani,H., Hosoda,T.,
            Nakahori,Y., Medof,M.E. and Yazaki,Y.
  TITLE     Assignment of the human GPAA1 gene, which encodes a product
            required for the attachment of glycosylphosphatidylinositols to
            proteins, at 8q24
  JOURNAL   Genomics 54 (2), 354-355 (1998)
   PUBMED   9828142
REFERENCE   9  (residues 1 to 621)
  AUTHORS   Hiroi,Y., Komuro,I., Chen,R., Hosoda,T., Mizuno,T., Kudoh,S.,
            Georgescu,S.P., Medof,M.E. and Yazaki,Y.
  TITLE     Molecular cloning of human homolog of yeast GAA1 which is required
            for attachment of glycosylphosphatidylinositols to proteins
  JOURNAL   FEBS Lett 421 (3), 252-258 (1998)
   PUBMED   9468317
REFERENCE   10 (residues 1 to 621)
  AUTHORS   Ploug,M., Ronne,E., Behrendt,N., Jensen,A.L., Blasi,F. and Dano,K.
  TITLE     Cellular receptor for urokinase plasminogen activator.
            Carboxyl-terminal processing and membrane anchoring by
            glycosyl-phosphatidylinositol
  JOURNAL   J Biol Chem 266 (3), 1926-1933 (1991)
   PUBMED   1846368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC004129.2 and BC003171.1.
            
            Summary: Posttranslational glycosylphosphatidylinositol (GPI)
            anchor attachment serves as a general mechanism for linking
            proteins to the cell surface membrane. The protein encoded by this
            gene presumably functions in GPI anchoring at the GPI transfer
            step. The mRNA transcript is ubiquitously expressed in both fetal
            and adult tissues. The anchor attachment protein 1 contains an
            N-terminal signal sequence, 1 cAMP- and cGMP-dependent protein
            kinase phosphorylation site, 1 leucine zipper pattern, 2 potential
            N-glycosylation sites, and 8 putative transmembrane domains.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.301001.1,
                                           SRR3476690.350575.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000355091.9/ ENSP00000347206.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..621
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q24.3"
     Protein         1..621
                     /product="GPI-anchor transamidase component GPAA1"
                     /note="glycophosphatidylinositol anchor attachment 1; GPI
                     transamidase subunit; anchor attachment protein 1 (Gaa1p,
                     yeast) homolog; glycosylphosphatidylinositol anchor
                     attachment 1 protein; GAA1 protein homolog; GPI anchor
                     attachment protein 1; GPAA1P anchor attachment protein 1
                     homolog; glycosylphosphatidylinositol anchor attachment
                     protein 1 homolog"
                     /calculated_mol_wt=67492
     Site            20..41
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Region          125..615
                     /region_name="Gaa1"
                     /note="Gaa1-like, GPI transamidase component; pfam04114"
                     /db_xref="CDD:461181"
     Site            203
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:35165458,
                     ECO:0000269|PubMed:37684232, ECO:0007744|PDB:8IMX,
                     ECO:0007744|PDB:8IMY; propagated from UniProtKB/Swiss-Prot
                     (O43292.3)"
     Site            371..393
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            426..450
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            463..483
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            496..519
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            520..536
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            541..563
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     Site            598..619
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43292.3)"
     CDS             1..621
                     /gene="GPAA1"
                     /gene_synonym="GAA1; GPIBD15; hGAA1"
                     /coded_by="NM_003801.4:98..1963"
                     /db_xref="CCDS:CCDS43776.1"
                     /db_xref="GeneID:8733"
                     /db_xref="HGNC:HGNC:4446"
                     /db_xref="MIM:603048"
ORIGIN      
        1 mgllsdpvrr ralarlvlrl naplcvlsyv agiawflalv fppltqrtym senamgstmv
       61 eeqfaggdra rafardfaah rkksgalpva wlertmrsvg levytqsfsr klpfpdethe
      121 rymvsgtnvy gilrapraas teslvltvpc gsdstnsqav glllalaahf rgqiywakdi
      181 vflvtehdll gteawleayh dvnvtgmqss plqgragaiq aavalelssd vvtsldvave
      241 glngqlpnld llnlfqtfcq kggllctlqg klqpedwtsl dgplqglqtl llmvlrqasg
      301 rphgshglfl ryrvealtlr ginsfrqyky dlvavgkale gmfrklnhll erlhqsffly
      361 llpglsrfvs iglympavgf lllvlglkal elwmqlheag mgleepggap gpsvplppsq
      421 gvglaslvap llisqamgla lyvlpvlgqh vatqhfpvae aeavvltlla iyaaglalph
      481 nthrvvstqa pdrgwmalkl valiylalql gcialtnfsl gfllattmvp taalakphgp
      541 rtlyaallvl tspaatllgs lflwrelqea plslaegwql flaalaqgvl ehhtygallf
      601 pllslglypc wllfwnvlfw k
//
LOCUS       NP_620308                186 aa            linear   PRI 20-NOV-2025
DEFINITION  diablo IAP-binding mitochondrial protein isoform 2 [Homo sapiens].
ACCESSION   NP_620308
VERSION     NP_620308.1
DBSOURCE    REFSEQ: accession NM_138930.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 186)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 186)
  AUTHORS   Zhang,D. and Yang,N.
  TITLE     In vivo and in vitro studies on the role of regulating Smac
            expression in the occurrence and development of colon cancer
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (6), 206-210 (2024)
   PUBMED   38836659
  REMARK    GeneRIF: In vivo and in vitro studies on the role of regulating
            Smac expression in the occurrence and development of colon cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 186)
  AUTHORS   Li,Y., Song,Y. and Liang,Y.
  TITLE     AREL1 resists the apoptosis induced by TGF-beta by inhibiting SMAC
            in vascular endothelial cells
  JOURNAL   J Biochem Mol Toxicol 37 (10), e23439 (2023)
   PUBMED   37522329
  REMARK    GeneRIF: AREL1 resists the apoptosis induced by TGF-beta by
            inhibiting SMAC in vascular endothelial cells.
REFERENCE   4  (residues 1 to 186)
  AUTHORS   Fu,J., Jin,Y. and Arend,L.J.
  TITLE     Smac3, a novel Smac/DIABLO splicing variant, attenuates the
            stability and apoptosis-inhibiting activity of X-linked inhibitor
            of apoptosis protein
  JOURNAL   J Biol Chem 278 (52), 52660-52672 (2003)
   PUBMED   14523016
  REMARK    GeneRIF: Smac3 is a novel Smac/DIABLO splicing variant and
            attenuates the stability and apoptosis-inhibiting activity of XIAP
REFERENCE   5  (residues 1 to 186)
  AUTHORS   Roberts,D.L., Merrison,W., MacFarlane,M. and Cohen,G.M.
  TITLE     The inhibitor of apoptosis protein-binding domain of Smac is not
            essential for its proapoptotic activity
  JOURNAL   J Cell Biol 153 (1), 221-228 (2001)
   PUBMED   11285287
REFERENCE   6  (residues 1 to 186)
  AUTHORS   Liu,Z., Sun,C., Olejniczak,E.T., Meadows,R.P., Betz,S.F., Oost,T.,
            Herrmann,J., Wu,J.C. and Fesik,S.W.
  TITLE     Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
  JOURNAL   Nature 408 (6815), 1004-1008 (2000)
   PUBMED   11140637
REFERENCE   7  (residues 1 to 186)
  AUTHORS   Srinivasula,S.M., Datta,P., Fan,X.J., Fernandes-Alnemri,T.,
            Huang,Z. and Alnemri,E.S.
  TITLE     Molecular determinants of the caspase-promoting activity of
            Smac/DIABLO and its role in the death receptor pathway
  JOURNAL   J Biol Chem 275 (46), 36152-36157 (2000)
   PUBMED   10950947
REFERENCE   8  (residues 1 to 186)
  AUTHORS   Chai,J., Du,C., Wu,J.W., Kyin,S., Wang,X. and Shi,Y.
  TITLE     Structural and biochemical basis of apoptotic activation by
            Smac/DIABLO
  JOURNAL   Nature 406 (6798), 855-862 (2000)
   PUBMED   10972280
REFERENCE   9  (residues 1 to 186)
  AUTHORS   Verhagen,A.M., Ekert,P.G., Pakusch,M., Silke,J., Connolly,L.M.,
            Reid,G.E., Moritz,R.L., Simpson,R.J. and Vaux,D.L.
  TITLE     Identification of DIABLO, a mammalian protein that promotes
            apoptosis by binding to and antagonizing IAP proteins
  JOURNAL   Cell 102 (1), 43-53 (2000)
   PUBMED   10929712
REFERENCE   10 (residues 1 to 186)
  AUTHORS   Du,C., Fang,M., Li,Y., Li,L. and Wang,X.
  TITLE     Smac, a mitochondrial protein that promotes cytochrome c-dependent
            caspase activation by eliminating IAP inhibition
  JOURNAL   Cell 102 (1), 33-42 (2000)
   PUBMED   10929711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA877400.1, BC046209.1,
            BC095468.1, AK057778.1 and N66735.1.
            
            Summary: This gene encodes an inhibitor of apoptosis protein
            (IAP)-binding protein. The encoded mitochondrial protein enters the
            cytosol when cells undergo apoptosis, and allows activation of
            caspases by binding to inhibitor of apoptosis proteins.
            Overexpression of the encoded protein sensitizes tumor cells to
            apoptosis. A mutation in this gene is associated with young-adult
            onset of nonsyndromic deafness-64. Alternative splicing results in
            multiple transcript variants encoding different isoforms. [provided
            by RefSeq, May 2013].
            
            Transcript Variant: This variant (2) differs in its 5' UTR and 5'
            coding region, and uses an alternate start codon, compared to
            variant 1. The encoded isoform (2, also known as Smac-beta and
            Smac/DIABLO-S) has a shorter and distinct N-terminus, compared to
            isoform 1. Isoform 2 has a cortical, instead of a mitochondrial,
            subcellular distribution, and lacks the inhibitor of apoptosis
            protein-binding domain but maintains the ability to potentiate
            apoptosis (PMID: 11285287). Variants 2 and 7 encode the same
            isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC095468.1, SRR1660809.311907.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 10929711; reported by
                                                  MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..186
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..186
                     /product="diablo IAP-binding mitochondrial protein isoform
                     2"
                     /note="second mitochondria-derived activator of caspase;
                     direct IAP-binding protein with low pI; diablo homolog,
                     mitochondrial; diablo-like protein; second
                     mitochondria-derived activator of caspases"
                     /calculated_mol_wt=21102
     Region          8..186
                     /region_name="Smac_DIABLO"
                     /note="Second Mitochondria-derived Activator of Caspases;
                     pfam09057"
                     /db_xref="CDD:462664"
     CDS             1..186
                     /gene="DIABLO"
                     /gene_synonym="DFNA64; SMAC"
                     /coded_by="NM_138930.3:685..1245"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:56616"
                     /db_xref="HGNC:HGNC:21528"
                     /db_xref="MIM:605219"
ORIGIN      
        1 mksdfyfqks ephslsseal mrravslvtd ststflsqtt yalieaitey tkavytltsl
       61 yrqytsllgk mnseeedevw qviigaraem tskhqeylkl ettwmtavgl semaaeaayq
      121 tgadqasita rnhiqlvklq veevhqlsrk aetklaeaqi eelrqktqee geeraeseqe
      181 aylred
//
LOCUS       NP_055742               1034 aa            linear   PRI 20-NOV-2025
DEFINITION  connector enhancer of kinase suppressor of ras 2 isoform 1 [Homo
            sapiens].
ACCESSION   NP_055742
VERSION     NP_055742.2
DBSOURCE    REFSEQ: accession NM_014927.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1034)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1034)
  AUTHORS   Ito,H. and Nagata,K.I.
  TITLE     Functions of CNKSR2 and Its Association with Neurodevelopmental
            Disorders
  JOURNAL   Cells 11 (2), 303 (2022)
   PUBMED   35053419
  REMARK    GeneRIF: Functions of CNKSR2 and Its Association with
            Neurodevelopmental Disorders.
            Review article
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1034)
  AUTHORS   Toraman,B., Bilginer,S.C., Hesapcioglu,S.T., Goker,Z., Soykam,H.O.,
            Erguner,B., Dincer,T., Yildiz,G., Unsal,S., Kasap,B.K., Kandil,S.
            and Kalay,E.
  TITLE     Finding underlying genetic mechanisms of two patients with autism
            spectrum disorder carrying familial apparently balanced chromosomal
            translocations
  JOURNAL   J Gene Med 23 (4), e3322 (2021)
   PUBMED   33591602
  REMARK    GeneRIF: Finding underlying genetic mechanisms of two patients with
            autism spectrum disorder carrying familial apparently balanced
            chromosomal translocations.
REFERENCE   4  (residues 1 to 1034)
  AUTHORS   Zhang,Y., Yu,T., Li,N., Wang,J., Wang,J., Ge,Y. and Yao,R.
  TITLE     Psychomotor development and attention problems caused by a splicing
            variant of CNKSR2
  JOURNAL   BMC Med Genomics 13 (1), 182 (2020)
   PUBMED   33298018
  REMARK    GeneRIF: Psychomotor development and attention problems caused by a
            splicing variant of CNKSR2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1034)
  AUTHORS   Daoqi,M., Guohong,C., Yuan,W., Zhixiao,Y., Kaili,X. and Shiyue,M.
  TITLE     Exons deletion of CNKSR2 gene identified in X-linked syndromic
            intellectual disability
  JOURNAL   BMC Med Genet 21 (1), 69 (2020)
   PUBMED   32245427
  REMARK    GeneRIF: This study enhances our knowledge of the CNKSR2 gene
            mutation spectrum and provides further information about the
            phenotypic characteristics of X-linked syndromic intellectual
            disability.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1034)
  AUTHORS   Wang,X., Patel,R. and Studzinski,G.P.
  TITLE     hKSR-2, a vitamin D-regulated gene, inhibits apoptosis in
            arabinocytosine-treated HL60 leukemia cells
  JOURNAL   Mol Cancer Ther 7 (9), 2798-2806 (2008)
   PUBMED   18790760
REFERENCE   7  (residues 1 to 1034)
  AUTHORS   Rajakulendran,T., Sahmi,M., Kurinov,I., Tyers,M., Therrien,M. and
            Sicheri,F.
  TITLE     CNK and HYP form a discrete dimer by their SAM domains to mediate
            RAF kinase signaling
  JOURNAL   Proc Natl Acad Sci U S A 105 (8), 2836-2841 (2008)
   PUBMED   18287031
  REMARK    GeneRIF: CNK and HYP form a discrete dimer by their SAM domains to
            mediate RAF kinase signaling.
REFERENCE   8  (residues 1 to 1034)
  AUTHORS   Bumeister,R., Rosse,C., Anselmo,A., Camonis,J. and White,M.A.
  TITLE     CNK2 couples NGF signal propagation to multiple regulatory cascades
            driving cell differentiation
  JOURNAL   Curr Biol 14 (5), 439-445 (2004)
   PUBMED   15028221
REFERENCE   9  (residues 1 to 1034)
  AUTHORS   Lanigan,T.M., Liu,A., Huang,Y.Z., Mei,L., Margolis,B. and Guan,K.L.
  TITLE     Human homologue of Drosophila CNK interacts with Ras effector
            proteins Raf and Rlf
  JOURNAL   FASEB J 17 (14), 2048-2060 (2003)
   PUBMED   14597674
  REMARK    GeneRIF: CNK2 through interaction with Raf and Rlf may function as
            a regulator of Ras signaling.
REFERENCE   10 (residues 1 to 1034)
  AUTHORS   Ohtakara,K., Nishizawa,M., Izawa,I., Hata,Y., Matsushima,S.,
            Taki,W., Inada,H., Takai,Y. and Inagaki,M.
  TITLE     Densin-180, a synaptic protein, links to PSD-95 through its direct
            interaction with MAGUIN-1
  JOURNAL   Genes Cells 7 (11), 1149-1160 (2002)
   PUBMED   12390249
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL807781.6, BC136289.1 and
            AL772392.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 30, 2004 this sequence version replaced NP_055742.1.
            
            Summary: This gene encodes a multidomain protein that functions as
            a scaffold protein to mediate the mitogen-activated protein kinase
            pathways downstream from Ras. This gene product is induced by
            vitamin D and inhibits apoptosis in certain cancer cells. It may
            also play a role in ternary complex assembly of synaptic proteins
            at the postsynaptic membrane and coupling of signal transduction to
            membrane/cytoskeletal remodeling. Multiple transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Dec 2009].
            
            Transcript Variant: This variant (1, also known as CNK2A and
            MAGUIN-1) represents the longest transcript and encodes the longest
            isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.36477.1,
                                           SRR1803611.255113.1 [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA2144333 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000379510.5/ ENSP00000368824.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1034
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..1034
                     /product="connector enhancer of kinase suppressor of ras 2
                     isoform 1"
                     /note="connector enhancer of KSR2; membrane-associated
                     guanylate kinase-interacting protein; CNK homolog protein
                     2"
                     /calculated_mol_wt=117404
     Region          8..76
                     /region_name="SAM_CNK1,2,3-suppressor"
                     /note="SAM domain of CNK1,2,3-suppressor subfamily;
                     cd09511"
                     /db_xref="CDD:188910"
     Site            12
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            order(24,49,53,58..65,67..68,71)
                     /site_type="other"
                     /note="heterodimer interface EH [polypeptide binding]"
                     /db_xref="CDD:188910"
     Region          84..176
                     /region_name="CRIC_ras_sig"
                     /note="Connector enhancer of kinase suppressor of ras;
                     pfam10534"
                     /db_xref="CDD:463138"
     Region          214..294
                     /region_name="PDZ_CNK1_2_3-like"
                     /note="PDZ domain of connector enhancer of kinase
                     suppressor of ras 1 (CNK1), CNK2, CNK3, and related
                     domains; cd06748"
                     /db_xref="CDD:467230"
     Site            order(226..232,242,245,275,279,282..283)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467230"
     Region          324..349
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          339..>487
                     /region_name="CNK2_3_dom"
                     /note="Connector enhancer of kinase suppressor of ras 2/3
                     domain; pfam06663"
                     /db_xref="CDD:461979"
     Site            390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          480..510
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          539..559
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          559..672
                     /region_name="PH_CNK_mammalian-like"
                     /note="Connector enhancer of KSR (Kinase suppressor of
                     ras) (CNK) pleckstrin homology (PH) domain; cd01260"
                     /db_xref="CDD:269962"
     Region          682..766
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            683
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            685
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80YA9; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            756
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T4; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            767
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z1T4; propagated from
                     UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Region          864..905
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     Site            908
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8WXI2.1)"
     CDS             1..1034
                     /gene="CNKSR2"
                     /gene_synonym="CNK2; KSR2; MAGUIN; MRXSHG"
                     /coded_by="NM_014927.5:481..3585"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS14198.1"
                     /db_xref="GeneID:22866"
                     /db_xref="HGNC:HGNC:19701"
                     /db_xref="MIM:300724"
ORIGIN      
        1 malimepvsk wspsqvvdwm kglddclqqy iknferekis gdqllrithq eledlgvsri
       61 ghqelileav dllcalnygl etenlktlsh klnasaknlq nfitgrrrsg hydgrtsrkl
      121 pndfltsvvd ligaakslla wldrspfaav tdysvtrnnv iqlcleltti vqqdctvyet
      181 enkilhvckt lsgvcdhiis lssdplvsqs ahleviqlan ikpseglgmy ikstydglhv
      241 itgttenspa drckkihagd eviqvnhqtv vgwqlknlvn alredpsgvi ltlkkrpqsm
      301 ltsapallkn mrwkplalqp liprsptssv atpsstistp tkrdssalqd lyippppaep
      361 yiprdekgnl pcedlrghmv gkpvhkgses pnsfldqeyr krfniveedt vlycyeyekg
      421 rsssqgrres tptygklrpi smpveynwvg dyedpnkmkr dsrrensllr ymsnekiaqe
      481 eymfqrnskk dtgkkskkkg dksnspthys llpslqmdal rqdimgtpvp ettlyhtfqq
      541 sslqhkskkk nkgpiagksk rrisckdlgr gdcegwlwkk kdaksyfsqk wkkywfvlkd
      601 aslywyinee dekaegfisl pefkidrase crkkyafkac hpkiksfyfa aehlddmnrw
      661 lnrinmltag yaererikqe qdywsesdke eadtpstpkq dsppppydty prppsmscas
      721 pyveakhsrl sstetsqsqs sheefrqevt gssavspirk tasqrrswqd lietpltssg
      781 lhylqtlple dsvfsdsaai spehrrqstl ptqkchlqdh ygpyplaese rmqvlngngg
      841 kprsftlprd sgfnhcclna pvsacdpqdd vqppeveeee eeeeeegeaa genigekses
      901 reeklgdslq dlyraleqas lsplgehris tkmeyklsfi krcndpvmne klhrlrilks
      961 tlkaregeva iidkvldnpd ltskefqqwk qmyldlfldi cqnttsndpl sissevdvit
     1021 sslahthsyi ethv
//
LOCUS       NP_001138386             709 aa            linear   PRI 20-NOV-2025
DEFINITION  fibroblast growth factor receptor 2 isoform 4 precursor [Homo
            sapiens].
ACCESSION   NP_001138386
VERSION     NP_001138386.1
DBSOURCE    REFSEQ: accession NM_001144914.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 709)
  AUTHORS   Chen,C.P., Huang,J.P., Huang,K.S., Chen,Y.Y., Wu,F.T., Pan,Y.T.,
            Chiu,C.L. and Wang,W.
  TITLE     Perinatal imaging findings of a fetus with Pfeiffer syndrome and a
            heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation in FGFR2
            presenting a cloverleaf skull, craniosynostosis and short limbs on
            prenatal ultrasound mimicking thanatophoric dysplasia type II
  JOURNAL   Taiwan J Obstet Gynecol 63 (3), 387-390 (2024)
   PUBMED   38802203
  REMARK    GeneRIF: Perinatal imaging findings of a fetus with Pfeiffer
            syndrome and a heterozygous c.1019A>G, p.Tyr340Cys (Y340C) mutation
            in FGFR2 presenting a cloverleaf skull, craniosynostosis and short
            limbs on prenatal ultrasound mimicking thanatophoric dysplasia type
            II.
REFERENCE   2  (residues 1 to 709)
  AUTHORS   Lian,Y., Bodian,D. and Shehu,A.
  TITLE     Elucidating the Role of Wildtype and Variant FGFR2 Structural
            Dynamics in (Dys)Function and Disorder
  JOURNAL   Int J Mol Sci 25 (8), 4523 (2024)
   PUBMED   38674107
  REMARK    GeneRIF: Elucidating the Role of Wildtype and Variant FGFR2
            Structural Dynamics in (Dys)Function and Disorder.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 709)
  AUTHORS   Xu,N., Hung,K.L., Gong,X., Fan,D., Tian,Y., Yan,M., Wei,Y. and
            Wang,S.
  TITLE     Genetic insights into the 'sandwich fusion' subtype of Klippel-Feil
            syndrome: novel FGFR2 mutations identified by 21 cases of
            whole-exome sequencing
  JOURNAL   Orphanet J Rare Dis 19 (1), 141 (2024)
   PUBMED   38561822
  REMARK    GeneRIF: Genetic insights into the 'sandwich fusion' subtype of
            Klippel-Feil syndrome: novel FGFR2 mutations identified by 21 cases
            of whole-exome sequencing.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 709)
  AUTHORS   Wenger,T.L., Hing,A.V. and Evans,K.N.
  TITLE     Apert Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31145570
REFERENCE   5  (residues 1 to 709)
  AUTHORS   Wenger,T., Miller,D. and Evans,K.
  TITLE     FGFR Craniosynostosis Syndromes Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301628
REFERENCE   6  (residues 1 to 709)
  AUTHORS   Longoni,M., Pober,B.R. and High,F.A.
  TITLE     Congenital Diaphragmatic Hernia Overview - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301533
REFERENCE   7  (residues 1 to 709)
  AUTHORS   Dell,K.R. and Williams,L.T.
  TITLE     A novel form of fibroblast growth factor receptor 2. Alternative
            splicing of the third immunoglobulin-like domain confers ligand
            binding specificity
  JOURNAL   J Biol Chem 267 (29), 21225-21229 (1992)
   PUBMED   1400433
REFERENCE   8  (residues 1 to 709)
  AUTHORS   Luqmani,Y.A., Graham,M. and Coombes,R.C.
  TITLE     Expression of basic fibroblast growth factor, FGFR1 and FGFR2 in
            normal and malignant human breast, and comparison with other normal
            tissues
  JOURNAL   Br J Cancer 66 (2), 273-280 (1992)
   PUBMED   1380281
REFERENCE   9  (residues 1 to 709)
  AUTHORS   Katoh,M., Hattori,Y., Sasaki,H., Tanaka,M., Sugano,K., Yazaki,Y.,
            Sugimura,T. and Terada,M.
  TITLE     K-sam gene encodes secreted as well as transmembrane receptor
            tyrosine kinase
  JOURNAL   Proc Natl Acad Sci U S A 89 (7), 2960-2964 (1992)
   PUBMED   1313574
REFERENCE   10 (residues 1 to 709)
  AUTHORS   Miki,T., Bottaro,D.P., Fleming,T.P., Smith,C.L., Burgess,W.H.,
            Chan,A.M. and Aaronson,S.A.
  TITLE     Determination of ligand-binding specificity by alternative
            splicing: two distinct growth factor receptors encoded by a single
            gene
  JOURNAL   Proc Natl Acad Sci U S A 89 (1), 246-250 (1992)
   PUBMED   1309608
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M97193.1, U11814.1, AB084153.1,
            BC037338.2 and CB305736.1.
            
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member is a high-affinity receptor for acidic, basic and/or
            keratinocyte growth factor, depending on the isoform. Mutations in
            this gene are associated with Crouzon syndrome, Pfeiffer syndrome,
            Craniosynostosis, Apert syndrome, Jackson-Weiss syndrome,
            Beare-Stevenson cutis gyrata syndrome, Saethre-Chotzen syndrome,
            and syndromic craniosynostosis. Multiple alternatively spliced
            transcript variants encoding different isoforms have been noted for
            this gene. [provided by RefSeq, Jan 2009].
            
            Transcript Variant: This variant (4) is missing two consecutive
            in-frame coding exons compared to transcript variant 1. This
            results in a shorter isoform (4) lacking an internal protein
            segment compared to isoform 1.
            
            Sequence Note: A downstream AUG translation start codon is selected
            for this RefSeq based on the presence of a strong Kozak consensus
            signal, a strong community standard for the use of the downstream
            start codon, and on a higher probability of an N-terminal signal
            peptide being present in the resulting protein. The use of an
            alternative in-frame upstream AUG start codon would result in a
            protein that is 19 aa longer at the N-terminus. Translation from
            the annotated downstream start codon is likely to occur via leaky
            scanning and/or reinitiation.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB084153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG :: community standard (PMID:
                                                15863034)
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..709
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q26.13"
     Protein         1..709
                     /product="fibroblast growth factor receptor 2 isoform 4
                     precursor"
                     /EC_number="2.7.10.1"
                     /note="protein tyrosine kinase, receptor like 14;
                     bacteria-expressed kinase; keratinocyte growth factor
                     receptor; BEK fibroblast growth factor receptor"
                     /calculated_mol_wt=77554
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2298
     mat_peptide     22..709
                     /product="fibroblast growth factor receptor 2 isoform 4"
                     /calculated_mol_wt=77554
     Region          31..124
                     /region_name="IgI_1_FGFR"
                     /note="First immunoglobulin (Ig)-like domain of fibroblast
                     growth factor receptor (FGFR); member of the I-set of Ig
                     superfamily (IgSF) domains; cd04973"
                     /db_xref="CDD:409362"
     Region          31..34
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409362"
     Region          47..53
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409362"
     Region          56..66
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409362"
     Region          69..74
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409362"
     Region          77..79
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409362"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21802.1)"
     Region          84..88
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409362"
     Region          91..96
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409362"
     Region          102..111
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409362"
     Region          114..124
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409362"
     Site            123
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21802.1)"
     Region          131..151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P21802.1)"
     Region          154..248
                     /region_name="IgI_2_FGFR"
                     /note="Second immunoglobulin (Ig)-like domain of
                     fibroblast growth factor (FGF) receptor; member of the
                     I-set of IgSF domains; cd05857"
                     /db_xref="CDD:409443"
     Region          154..157
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409443"
     Region          161..178
                     /region_name="Heparin-binding"
                     /note="propagated from UniProtKB/Swiss-Prot (P21802.1)"
     Region          165..170
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409443"
     Site            order(166,168,170)
                     /site_type="other"
                     /note="FGF binding site [polypeptide binding]"
                     /db_xref="CDD:409443"
     Site            order(167,174..176,178)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:409443"
     Region          174..182
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409443"
     Region          188..193
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409443"
     Region          196..198
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409443"
     Region          207..210
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409443"
     Region          214..219
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409443"
     Region          228..235
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409443"
     Site            228
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21802.1)"
     Region          238..248
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409443"
     Site            241
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P21802.1)"
     Region          344..656
                     /region_name="PTKc_FGFR2"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     Fibroblast Growth Factor Receptor 2; cd05101"
                     /db_xref="CDD:270679"
     Site            order(375..376,378,383,403,405,422,452..455,459,514,
                     518..519,521,532,550..554,563,597)
                     /site_type="active"
                     /db_xref="CDD:270679"
     Site            order(375..376,378,383,403,405,422,452..455,459,518..519,
                     521,532)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270679"
     Site            order(514,518,550..554,563,597)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270679"
     Site            531..556
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270679"
     CDS             1..709
                     /gene="FGFR2"
                     /gene_synonym="BBDS; BEK; BFR-1; CD332; CEK3; CFD1; ECT1;
                     JWS; K-SAM; KGFR; TK14; TK25"
                     /coded_by="NM_001144914.1:151..2280"
                     /note="isoform 4 precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS44486.1"
                     /db_xref="GeneID:2263"
                     /db_xref="HGNC:HGNC:3689"
                     /db_xref="MIM:176943"
ORIGIN      
        1 mvswgrficl vvvtmatlsl arpsfslved ttlepeeppt kyqisqpevy vaapgeslev
       61 rcllkdaavi swtkdgvhlg pnnrtvlige ylqikgatpr dsglyactas rtvdsetwyf
      121 mvnvtdaiss gddeddtdga edfvsensnn krapywtnte kmekrlhavp aantvkfrcp
      181 aggnpmptmr wlkngkefkq ehriggykvr nqhwslimes vvpsdkgnyt cvveneygsi
      241 nhtyhldvva pgrekeitas pdyleiaiyc igvfliacmv vtvilcrmkn ttkkpdfssq
      301 pavhkltkri plrrqvtvsa essssmnsnt plvrittrls stadtpmlag vseyelpedp
      361 kwefprdklt lgkplgegcf gqvvmaeavg idkdkpkeav tvavkmlkdd atekdlsdlv
      421 sememmkmig khkniinllg actqdgplyv iveyaskgnl reylrarrpp gmeysydinr
      481 vpeeqmtfkd lvsctyqlar gmeylasqkc ihrdlaarnv lvtennvmki adfglardin
      541 nidyykkttn grlpvkwmap ealfdrvyth qsdvwsfgvl mweiftlggs pypgipveel
      601 fkllkeghrm dkpanctnel ymmmrdcwha vpsqrptfkq lvedldrilt lttneeyldl
      661 sqpleqysps ypdtrsscss gddsvfspdp mpyepclpqy phingsvkt
//
LOCUS       NP_001303866             273 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 12 isoform c [Homo sapiens].
ACCESSION   NP_001303866 XP_005260021
VERSION     NP_001303866.1
DBSOURCE    REFSEQ: accession NM_001316937.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 273)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 273)
  AUTHORS   Brunner,A., Li,Q., Fisicaro,S., Kourtesakis,A., Viiliainen,J.,
            Johansson,H.J., Pandey,V., Mayank,A.K., Lehtio,J.,
            Wohlschlegel,J.A., Spruck,C., Rantala,J.K., Orre,L.M. and
            Sangfelt,O.
  TITLE     FBXL12 degrades FANCD2 to regulate replication recovery and promote
            cancer cell survival under conditions of replication stress
  JOURNAL   Mol Cell 83 (20), 3720-3739 (2023)
   PUBMED   37591242
  REMARK    GeneRIF: FBXL12 degrades FANCD2 to regulate replication recovery
            and promote cancer cell survival under conditions of replication
            stress.
REFERENCE   3  (residues 1 to 273)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 273)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   5  (residues 1 to 273)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 273)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   7  (residues 1 to 273)
  AUTHORS   Kim,M., Nakamoto,T., Nishimori,S., Tanaka,K. and Chiba,T.
  TITLE     A new ubiquitin ligase involved in p57KIP2 proteolysis regulates
            osteoblast cell differentiation
  JOURNAL   EMBO Rep 9 (9), 878-884 (2008)
   PUBMED   18660753
REFERENCE   8  (residues 1 to 273)
  AUTHORS   Barrios-Rodiles,M., Brown,K.R., Ozdamar,B., Bose,R., Liu,Z.,
            Donovan,R.S., Shinjo,F., Liu,Y., Dembowy,J., Taylor,I.W., Luga,V.,
            Przulj,N., Robinson,M., Suzuki,H., Hayashizaki,Y., Jurisica,I. and
            Wrana,J.L.
  TITLE     High-throughput mapping of a dynamic signaling network in mammalian
            cells
  JOURNAL   Science 307 (5715), 1621-1625 (2005)
   PUBMED   15761153
REFERENCE   9  (residues 1 to 273)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
REFERENCE   10 (residues 1 to 273)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB127388.1, AC008752.6 and AK000195.1.
            
            On Nov 5, 2015 this sequence version replaced XP_005260021.1.
            
            Summary: Members of the F-box protein family, such as FBXL12, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (Jin et al., 2004 [PubMed 15520277]).[supplied
            by OMIM, Mar 2008].
            
            Transcript Variant: This variant (3) uses an alternate splice
            junction and a downstream AUG start codon compared to variant 1.
            The resulting isoform (c) is shorter at the N-terminus compared to
            isoform a. Variants 3, 4, 5, 6, 7, and 8 all encode the same
            isoform (c).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.68037.1, AK093760.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2151358, SAMEA2156099
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..273
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..273
                     /product="F-box/LRR-repeat protein 12 isoform c"
                     /note="F-box/LRR-repeat protein 12; F-box protein FBL12"
                     /calculated_mol_wt=30360
     Region          51..72
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          68..>173
                     /region_name="AMN1"
                     /note="Antagonist of mitotic exit network protein 1;
                     cd09293"
                     /db_xref="CDD:187754"
     Region          100..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <114..238
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          125..150
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          151..176
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          177..200
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          231..266
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..273
                     /gene="FBXL12"
                     /gene_synonym="Fbl12"
                     /coded_by="NM_001316937.2:400..1221"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS82287.1"
                     /db_xref="GeneID:54850"
                     /db_xref="HGNC:HGNC:13611"
                     /db_xref="MIM:609079"
ORIGIN      
        1 mrpkvmwhll rrymasrlhs lrmggylfsg sqapqlspal lralgqkcpn lkrlclhvad
       61 lsmvpitslp stlrtlelhs ceismawlhk qqdptvlpll ecivldrvpa frdehlqglt
      121 rfralrslvl ggtyrvtetg ldaglqelsy lqrlevlgct lsadstllai srhlrdvrki
      181 rltvrglsap glavlegmpa leslclqgpl vtpempspte ilsscltmpk lrvlelqglg
      241 wegqeaekil ckglphcmvi vracpkesmd wwm
//
LOCUS       NP_001307084             298 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-L2 isoform C [Homo sapiens].
ACCESSION   NP_001307084
VERSION     NP_001307084.1
DBSOURCE    REFSEQ: accession NM_001320155.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 298)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 298)
  AUTHORS   Wang,C., Xu,L., Du,C., Yun,H., Wang,K., Liu,H., Ye,M., Fan,J.,
            Zhou,Y. and Cheng,H.
  TITLE     CDK11 requires a critical activator SAP30BP to regulate pre-mRNA
            splicing
  JOURNAL   EMBO J 42 (24), e114051 (2023)
   PUBMED   38059508
REFERENCE   3  (residues 1 to 298)
  AUTHORS   Hluchy,M., Gajduskova,P., Ruiz de Los Mozos,I., Rajecky,M.,
            Kluge,M., Berger,B.T., Slaba,Z., Potesil,D., Weiss,E., Ule,J.,
            Zdrahal,Z., Knapp,S., Paruch,K., Friedel,C.C. and Blazek,D.
  TITLE     CDK11 regulates pre-mRNA splicing by phosphorylation of SF3B1
  JOURNAL   Nature 609 (7928), 829-834 (2022)
   PUBMED   36104565
REFERENCE   4  (residues 1 to 298)
  AUTHORS   Wu,C., Zhu,Q., Yao,Y., Shi,Z., Jin,C. and Chen,L.
  TITLE     Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription
  JOURNAL   Dev Neurosci 44 (3), 121-130 (2022)
   PUBMED   34937039
  REMARK    GeneRIF: Exosome miR-23a-3p from Osteoblast Alleviates Spinal Cord
            Ischemia/Reperfusion Injury by Down-Regulating KLF3-Activated CCNL2
            Transcription.
REFERENCE   5  (residues 1 to 298)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 298)
  AUTHORS   Loyer,P., Trembley,J.H., Grenet,J.A., Busson,A., Corlu,A., Zhao,W.,
            Kocak,M., Kidd,V.J. and Lahti,J.M.
  TITLE     Characterization of cyclin L1 and L2 interactions with CDK11 and
            splicing factors: influence of cyclin L isoforms on splice site
            selection
  JOURNAL   J Biol Chem 283 (12), 7721-7732 (2008)
   PUBMED   18216018
  REMARK    GeneRIF: CDK11(p110) interacts physically and functionally with
            cyclin Lalpha and -beta isoforms and SR proteins to regulate
            splicing.
REFERENCE   7  (residues 1 to 298)
  AUTHORS   de Graaf,K., Hekerman,P., Spelten,O., Herrmann,A., Packman,L.C.,
            Bussow,K., Muller-Newen,G. and Becker,W.
  TITLE     Characterization of cyclin L2, a novel cyclin with an
            arginine/serine-rich domain: phosphorylation by DYRK1A and
            colocalization with splicing factors
  JOURNAL   J Biol Chem 279 (6), 4612-4624 (2004)
   PUBMED   14623875
  REMARK    GeneRIF: characterize cyclin L2 as a highly mobile component of
            nuclear speckles and suggest that DYRK1A may regulate splicing by
            phosphorylation of cyclin L2
REFERENCE   8  (residues 1 to 298)
  AUTHORS   Edelheit,S. and Meiri,N.
  TITLE     Cyclin S: a new member of the cyclin family plays a role in
            long-term memory
  JOURNAL   Eur J Neurosci 19 (2), 365-375 (2004)
   PUBMED   14725631
REFERENCE   9  (residues 1 to 298)
  AUTHORS   Cheng,H. and Bjerknes,M.
  TITLE     Patterns of gene expression along the crypt-villus axis in mouse
            jejunal epithelium
  JOURNAL   Anat Rec 244 (1), 78-94 (1996)
   PUBMED   8838426
REFERENCE   10 (residues 1 to 298)
  AUTHORS   Bunnell,B.A., Heath,L.S., Adams,D.E., Lahti,J.M. and Kidd,V.J.
  TITLE     Increased expression of a 58-kDa protein kinase leads to changes in
            the CHO cell cycle
  JOURNAL   Proc Natl Acad Sci U S A 87 (19), 7467-7471 (1990)
   PUBMED   2217177
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2612]
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY002650.1, AY116620.1,
            CR628411.1, AK074112.1 and AK000685.1.
            
            Summary: The protein encoded by this gene belongs to the cyclin
            family. Through its interaction with several proteins, such as RNA
            polymerase II, splicing factors, and cyclin-dependent kinases, this
            protein functions as a regulator of the pre-mRNA splicing process,
            as well as in inducing apoptosis by modulating the expression of
            apoptotic and antiapoptotic proteins. Alternatively spliced
            transcript variants encoding different isoforms have been described
            for this gene. [provided by RefSeq, Aug 2011].
            
            Transcript Variant: This variant (4) contains an alternate exon
            compared to variant 1. The resulting isoform (C) is shorter at the
            N-terminus compared to isoform A. Variants 3, 4, 6, and 7 encode
            the same isoform (C).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.912323.1,
                                           SRR7346977.921918.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2153932 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..298
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.33"
     Protein         1..298
                     /product="cyclin-L2 isoform C"
                     /note="cyclin M; paneth cell-enhanced expression protein;
                     cyclin S"
                     /calculated_mol_wt=33708
     Region          <1..95
                     /region_name="CYCLIN_SF"
                     /note="Cyclin box fold superfamily; cl40454"
                     /db_xref="CDD:477360"
     CDS             1..298
                     /gene="CCNL2"
                     /gene_synonym="ANIA-6B; CCNM; CCNS; HCLA-ISO; HLA-ISO;
                     PCEE; SB138"
                     /coded_by="NM_001320155.3:710..1606"
                     /note="isoform C is encoded by transcript variant 4"
                     /db_xref="GeneID:81669"
                     /db_xref="HGNC:HGNC:20570"
                     /db_xref="MIM:613482"
ORIGIN      
        1 mndslrtdvf vrfqpesiac aciylaartl eiplpnrphw fllfgateee iqeiclkilq
       61 lyarkkvdlt hlegevekrk haieeakaqa rgllpggtqv ldgtsgfspa pklvespkeg
      121 kgskpsplsv kntkrrlega kkakadspvn glpkgresrs rsrsreqsys rspsrsaspk
      181 rrksdsgsts ggsksqsrsr srsdspprqa prsapykgse irgsrkskdc kypqkphksr
      241 srsssrsrsr sreradnpgk ykkkshyyrd qrrersrsye rtgrryerdh pghsrhrr
//
LOCUS       NP_057049                144 aa            linear   PRI 20-NOV-2025
DEFINITION  NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 [Homo
            sapiens].
ACCESSION   NP_057049
VERSION     NP_057049.5
DBSOURCE    REFSEQ: accession NM_015965.7
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Wang,B., Yang,Y., Ye,J., Han,X., Yang,L., Huang,Y. and Chao,L.
  TITLE     GRIM-19 deficiency promotes macrophage polarization to the M1
            phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger
  JOURNAL   Biol Reprod 110 (4), 739-749 (2024)
   PUBMED   38206868
  REMARK    GeneRIF: GRIM-19 deficiency promotes macrophage polarization to the
            M1 phenotype partly through glycolysis in unexplained recurrent
            spontaneous abortiondagger.
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Yang,L., Yang,Y., Han,X., Huang,C., Wang,Y., Jiang,D. and Chao,L.
  TITLE     GRIM19 deficiency aggravates metabolic disorder and ovarian
            dysfunction in PCOS
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (4), 167063 (2024)
   PUBMED   38360073
  REMARK    GeneRIF: GRIM19 deficiency aggravates metabolic disorder and
            ovarian dysfunction in PCOS.
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Lu,H. and Cao,X.
  TITLE     GRIM-19 is essential for maintenance of mitochondrial membrane
            potential
  JOURNAL   Mol Biol Cell 19 (5), 1893-1902 (2008)
   PUBMED   18287540
  REMARK    GeneRIF: GRIM-19 is required for electron transfer activity of
            complex I, and disruption of mitochondrial transmembrane potential
            by GRIM-19 mutants enhances the cells' sensitivity to apoptotic
            stimuli.
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Yeo,W.M., Isegawa,Y. and Chow,V.T.
  TITLE     The U95 protein of human herpesvirus 6B interacts with human
            GRIM-19: silencing of U95 expression reduces viral load and
            abrogates loss of mitochondrial membrane potential
  JOURNAL   J Virol 82 (2), 1011-1020 (2008)
   PUBMED   17928352
  REMARK    GeneRIF: results indicate that the high affinity between U95 early
            viral protein and GRIM-19 may be closely linked to the detrimental
            effect of HHV-6B infection on mitochondria.
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Kalakonda,S., Nallar,S.C., Lindner,D.J., Hu,J., Reddy,S.P. and
            Kalvakolanu,D.V.
  TITLE     Tumor-suppressive activity of the cell death activator GRIM-19 on a
            constitutively active signal transducer and activator of
            transcription 3
  JOURNAL   Cancer Res 67 (13), 6212-6220 (2007)
   PUBMED   17616678
  REMARK    GeneRIF: GRIM-19 suppresses constitutive STAT3-induced cellular
            transformation in vitro and in vivo by down-regulating the
            expression of a number of cellular genes involved in cell
            proliferation and apoptosis
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Murray,J., Zhang,B., Taylor,S.W., Oglesbee,D., Fahy,E.,
            Marusich,M.F., Ghosh,S.S. and Capaldi,R.A.
  TITLE     The subunit composition of the human NADH dehydrogenase obtained by
            rapid one-step immunopurification
  JOURNAL   J Biol Chem 278 (16), 13619-13622 (2003)
   PUBMED   12611891
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Angell,J.E., Lindner,D.J., Shapiro,P.S., Hofmann,E.R. and
            Kalvakolanu,D.V.
  TITLE     Identification of GRIM-19, a novel cell death-regulatory gene
            induced by the interferon-beta and retinoic acid combination, using
            a genetic approach
  JOURNAL   J Biol Chem 275 (43), 33416-33426 (2000)
   PUBMED   10924506
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Hu,R.M., Han,Z.G., Song,H.D., Peng,Y.D., Huang,Q.H., Ren,S.X.,
            Gu,Y.J., Huang,C.H., Li,Y.B., Jiang,C.L., Fu,G., Zhang,Q.H.,
            Gu,B.W., Dai,M., Mao,Y.F., Gao,G.F., Rong,R., Ye,M., Zhou,J.,
            Xu,S.H., Gu,J., Shi,J.X., Jin,W.R., Zhang,C.K., Wu,T.M.,
            Huang,G.Y., Chen,Z., Chen,M.D. and Chen,J.L.
  TITLE     Gene expression profiling in the human
            hypothalamus-pituitary-adrenal axis and full-length cDNA cloning
  JOURNAL   Proc Natl Acad Sci U S A 97 (17), 9543-9548 (2000)
   PUBMED   10931946
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Chidambaram,N.V., Angell,J.E., Ling,W., Hofmann,E.R. and
            Kalvakolanu,D.V.
  TITLE     Chromosomal localization of human GRIM-19, a novel IFN-beta and
            retinoic acid-activated regulator of cell death
  JOURNAL   J Interferon Cytokine Res 20 (7), 661-665 (2000)
   PUBMED   10926209
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC009189.2 and BG705222.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 8, 2009 this sequence version replaced NP_057049.4.
            
            Summary: This gene encodes a subunit of the mitochondrial membrane
            respiratory chain NADH dehydrogenase (Complex I), which functions
            in the transfer of electrons from NADH to the respiratory chain.
            The protein is required for complex I assembly and electron
            transfer activity. The protein binds the signal transducers and
            activators of transcription 3 (STAT3) transcription factor, and can
            function as a tumor suppressor. The human protein purified from
            mitochondria migrates at approximately 16 kDa. Transcripts
            originating from an upstream promoter and capable of expressing a
            protein with a longer N-terminus have been found, but their
            biological validity has not been determined. [provided by RefSeq,
            Oct 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF261134.1, SRR5189667.105639.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: PMID: 12611891, 17928352;
                                                  reported by MitoCarta
            MANE Ensembl match                 :: ENST00000507754.9/
                                                  ENSP00000423673.1
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..144
                     /product="NADH dehydrogenase [ubiquinone] 1 alpha
                     subcomplex subunit 13"
                     /EC_number="7.1.1.2"
                     /note="complex I B16.6 subunit; cell death-regulatory
                     protein GRIM19; CI-B16.6; complex I-B16.6; cell death
                     regulatory protein GRIM-19; NADH-ubiquinone oxidoreductase
                     B16.6 subunit; gene associated with retinoic and
                     IFN-induced mortality 19 protein; gene associated with
                     retinoic and interferon-induced mortality 19 protein; NADH
                     dehydrogenase (ubiquinone) 1 alpha subcomplex, 13"
                     /calculated_mol_wt=16567
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q95KV7; propagated from
                     UniProtKB/Swiss-Prot (Q9P0J0.3)"
     Region          5..128
                     /region_name="GRIM-19"
                     /note="GRIM-19 protein; pfam06212"
                     /db_xref="CDD:461852"
     Site            30..51
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J0.3)"
     Region          102..144
                     /region_name="Important for inducing cell death"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9P0J0.3)"
     CDS             1..144
                     /gene="NDUFA13"
                     /gene_synonym="B16.6; CDA016; CGI-39; GRIM-19; GRIM19;
                     MC1DN28"
                     /coded_by="NM_015965.7:15..449"
                     /db_xref="CCDS:CCDS12404.2"
                     /db_xref="GeneID:51079"
                     /db_xref="HGNC:HGNC:17194"
                     /db_xref="MIM:609435"
ORIGIN      
        1 maaskvkqdm pppggygpid ykrnlprrgl sgysmlaigi gtliyghwsi mkwnrerrrl
       61 qiedfearia llpllqaetd rrtlqmlren leeeaiimkd vpdwkvgesv fhttrwvppl
      121 igelyglrtt eealhashgf mwyt
//
LOCUS       NP_003901                144 aa            linear   PRI 20-NOV-2025
DEFINITION  protein BUD31 homolog [Homo sapiens].
ACCESSION   NP_003901
VERSION     NP_003901.2
DBSOURCE    REFSEQ: accession NM_003910.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Wu,X., Fan,R., Zhang,Y., Duan,C., Yao,X., Liu,K., Lin,D. and
            Chen,Z.
  TITLE     The role of BUD31 in clear cell renal cell carcinoma: prognostic
            significance, alternative splicing, and tumor immune environment
  JOURNAL   Clin Exp Med 24 (1), 191 (2024)
   PUBMED   39136845
  REMARK    GeneRIF: The role of BUD31 in clear cell renal cell carcinoma:
            prognostic significance, alternative splicing, and tumor immune
            environment.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Choudhry,M., Gamallat,Y., Khosh Kish,E., Seyedi,S., Gotto,G.,
            Ghosh,S. and Bismar,T.A.
  TITLE     Downregulation of BUD31 Promotes Prostate Cancer Cell Proliferation
            and Migration via Activation of p-AKT and Vimentin In Vitro
  JOURNAL   Int J Mol Sci 24 (7), 6055 (2023)
   PUBMED   37047027
  REMARK    GeneRIF: Downregulation of BUD31 Promotes Prostate Cancer Cell
            Proliferation and Migration via Activation of p-AKT and Vimentin In
            Vitro.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Zhang,X., Yan,C., Zhan,X., Li,L., Lei,J. and Shi,Y.
  TITLE     Structure of the human activated spliceosome in three
            conformational states
  JOURNAL   Cell Res 28 (3), 307-322 (2018)
   PUBMED   29360106
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Bertram,K., Agafonov,D.E., Liu,W.T., Dybkov,O., Will,C.L.,
            Hartmuth,K., Urlaub,H., Kastner,B., Stark,H. and Luhrmann,R.
  TITLE     Cryo-EM structure of a human spliceosome activated for step 2 of
            splicing
  JOURNAL   Nature 542 (7641), 318-323 (2017)
   PUBMED   28076346
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Xu,W., Huang,H., Yu,L. and Cao,L.
  TITLE     Meta-analysis of gene expression profiles indicates genes in
            spliceosome pathway are up-regulated in hepatocellular carcinoma
            (HCC)
  JOURNAL   Med Oncol 32 (4), 96 (2015)
   PUBMED   25731616
  REMARK    GeneRIF: High BUD31 expression is associated with hepatocellular
            carcinoma.
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Hsu,C.L., Liu,J.S., Wu,P.L., Guan,H.H., Chen,Y.L., Lin,A.C.,
            Ting,H.J., Pang,S.T., Yeh,S.D., Ma,W.L., Chen,C.J., Wu,W.G. and
            Chang,C.
  TITLE     Identification of a new androgen receptor (AR) co-regulator BUD31
            and related peptides to suppress wild-type and mutated AR-mediated
            prostate cancer growth via peptide screening and X-ray structure
            analysis
  JOURNAL   Mol Oncol 8 (8), 1575-1587 (2014)
   PUBMED   25091737
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Hla,T., Jackson,A.Q., Appleby,S.B. and Maciag,T.
  TITLE     Characterization of edg-2, a human homologue of the Xenopus
            maternal transcript G10 from endothelial cells
  JOURNAL   Biochim Biophys Acta 1260 (2), 227-229 (1995)
   PUBMED   7841202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004922.2 and BC022821.1.
            
            On Jun 24, 2003 this sequence version replaced NP_003901.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.677472.1,
                                           SRR1163658.123835.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000222969.10/ ENSP00000222969.5
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22.1"
     Protein         1..144
                     /product="protein BUD31 homolog"
                     /note="maternal G10 transcript; functional
                     spliceosome-associated protein 17; protein EDG-2; protein
                     G10 homolog; G10 maternal transcript homolog; BUD31
                     homolog"
                     /calculated_mol_wt=16869
     Region          1..143
                     /region_name="G10"
                     /note="G10 protein; pfam01125"
                     /db_xref="CDD:426066"
     Region          2..10
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Region          59..67
                     /region_name="Interaction with AR.
                     /evidence=ECO:0000269|PubMed:28076346"
                     /note="propagated from UniProtKB/Swiss-Prot (P41223.2)"
     Site            125
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P41223.2)"
     CDS             1..144
                     /gene="BUD31"
                     /gene_synonym="Cwc14; EDG-2; EDG2; fSAP17; G10; YCR063W"
                     /coded_by="NM_003910.4:443..877"
                     /db_xref="CCDS:CCDS5663.1"
                     /db_xref="GeneID:8896"
                     /db_xref="HGNC:HGNC:29629"
                     /db_xref="MIM:603477"
ORIGIN      
        1 mpkvkrsrka ppdgweliep tldeldqkmr eaetephegk rkveslwpif rihhqktryi
       61 fdlfykrkai srelyeycik egyadknlia kwkkqgyenl cclrciqtrd tnfgtncicr
      121 vpksklevgr iiecthcgcr gcsg
//
LOCUS       NP_001003396             144 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor protein D53 isoform 3 [Homo sapiens].
ACCESSION   NP_001003396
VERSION     NP_001003396.1
DBSOURCE    REFSEQ: accession NM_001003396.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 144)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 144)
  AUTHORS   Couzens,A.L., Knight,J.D., Kean,M.J., Teo,G., Weiss,A.,
            Dunham,W.H., Lin,Z.Y., Bagshaw,R.D., Sicheri,F., Pawson,T.,
            Wrana,J.L., Choi,H. and Gingras,A.C.
  TITLE     Protein interaction network of the mammalian Hippo pathway reveals
            mechanisms of kinase-phosphatase interactions
  JOURNAL   Sci Signal 6 (302), rs15 (2013)
   PUBMED   24255178
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 144)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   6  (residues 1 to 144)
  AUTHORS   Nourse,C.R., Mattei,M.G., Gunning,P. and Byrne,J.A.
  TITLE     Cloning of a third member of the D52 gene family indicates
            alternative coding sequence usage in D52-like transcripts
  JOURNAL   Biochim Biophys Acta 1443 (1-2), 155-168 (1998)
   PUBMED   9838088
REFERENCE   7  (residues 1 to 144)
  AUTHORS   Byrne,J.A., Nourse,C.R., Basset,P. and Gunning,P.
  TITLE     Identification of homo- and heteromeric interactions between
            members of the breast carcinoma-associated D52 protein family using
            the yeast two-hybrid system
  JOURNAL   Oncogene 16 (7), 873-881 (1998)
   PUBMED   9484778
REFERENCE   8  (residues 1 to 144)
  AUTHORS   Byrne,J.A., Mattei,M.G., Basset,P. and Gunning,P.
  TITLE     Identification and in situ hybridization mapping of a mouse Tpd52l1
            (D53) orthologue to chromosome 10A4-B2
  JOURNAL   Cytogenet Cell Genet 81 (3-4), 199-201 (1998)
   PUBMED   9730602
REFERENCE   9  (residues 1 to 144)
  AUTHORS   Byrne,J.A., Mattei,M.G. and Basset,P.
  TITLE     Definition of the tumor protein D52 (TPD52) gene family through
            cloning of D52 homologues in human (hD53) and mouse (mD52)
  JOURNAL   Genomics 35 (3), 523-532 (1996)
   PUBMED   8812487
REFERENCE   10 (residues 1 to 144)
  AUTHORS   Byrne,J.A., Tomasetto,C., Garnier,J.M., Rouyer,N., Mattei,M.G.,
            Bellocq,J.P., Rio,M.C. and Basset,P.
  TITLE     A screening method to identify genes commonly overexpressed in
            carcinomas and the identification of a novel complementary DNA
            sequence
  JOURNAL   Cancer Res 55 (13), 2896-2903 (1995)
   PUBMED   7796418
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB114736.1, U44427.1, U44429.1,
            AL121938.10 and AI222450.1.
            
            Summary: This gene encodes a member of a family of proteins that
            contain coiled-coil domains and may form hetero- or homomers. The
            encoded protein is involved in cell proliferation and calcium
            signaling. It also interacts with the mitogen-activated protein
            kinase kinase kinase 5 (MAP3K5/ASK1) and positively regulates
            MAP3K5-induced apoptosis. Multiple alternatively spliced transcript
            variants have been observed. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (3) lacks an exon in the 3' coding
            region, which results in a frameshift, compared to variant 1. The
            resulting isoform (3) has a distinct and shorter C-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.278612.1, BC002375.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.31"
     Protein         1..144
                     /product="tumor protein D53 isoform 3"
                     /note="tumor protein D53; tumor protein D52 like 1"
                     /calculated_mol_wt=16045
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q16890.1)"
     Site            29
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Region          44..131
                     /region_name="TPD52"
                     /note="Tumour protein D52 family; pfam04201"
                     /db_xref="CDD:461225"
     Site            86
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            131
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     Site            133
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q16890.1)"
     CDS             1..144
                     /gene="TPD52L1"
                     /gene_synonym="D53; TPD53"
                     /coded_by="NM_001003396.3:180..614"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS34527.1"
                     /db_xref="GeneID:7164"
                     /db_xref="HGNC:HGNC:12006"
                     /db_xref="MIM:604069"
ORIGIN      
        1 meaqaqglle teplqgtded avasadfssm lseeekeelk aelvqledei ttlrqvlsak
       61 erhlveikqk lgmnlmnelk qnfskswhdm qtttaykkth etlshagqka taafsnvgta
      121 iskkfgdmsy sirhsismpa mrrk
//
LOCUS       NP_001317947             172 aa            linear   PRI 20-NOV-2025
DEFINITION  vacuolar protein sorting-associated protein 26C isoform 2 [Homo
            sapiens].
ACCESSION   NP_001317947 XP_005260968
VERSION     NP_001317947.1
DBSOURCE    REFSEQ: accession NM_001331018.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 172)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   2  (residues 1 to 172)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 172)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 172)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 172)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 172)
  AUTHORS   Koumandou,V.L., Klute,M.J., Herman,E.K., Nunez-Miguel,R.,
            Dacks,J.B. and Field,M.C.
  TITLE     Evolutionary reconstruction of the retromer complex and its
            function in Trypanosoma brucei
  JOURNAL   J Cell Sci 124 (Pt 9), 1496-1509 (2011)
   PUBMED   21502137
REFERENCE   7  (residues 1 to 172)
  AUTHORS   Aubry,L., Guetta,D. and Klein,G.
  TITLE     The arrestin fold: variations on a theme
  JOURNAL   Curr Genomics 10 (2), 133-142 (2009)
   PUBMED   19794886
REFERENCE   8  (residues 1 to 172)
  AUTHORS   Hu,Y.H., Warnatz,H.J., Vanhecke,D., Wagner,F., Fiebitz,A.,
            Thamm,S., Kahlem,P., Lehrach,H., Yaspo,M.L. and Janitz,M.
  TITLE     Cell array-based intracellular localization screening reveals novel
            functional features of human chromosome 21 proteins
  JOURNAL   BMC Genomics 7, 155 (2006)
   PUBMED   16780588
  REMARK    Publication Status: Online-Only
REFERENCE   9  (residues 1 to 172)
  AUTHORS   Dahmane,N., Ghezala,G.A., Gosset,P., Chamoun,Z.,
            Dufresne-Zacharia,M.C., Lopes,C., Rabatel,N.,
            Gassanova-Maugenre,S., Chettouh,Z., Abramowski,V., Fayet,E.,
            Yaspo,M.L., Korn,B., Blouin,J.L., Lehrach,H., Poutska,A.,
            Antonarakis,S.E., Sinet,P.M., Creau,N. and Delabar,J.M.
  TITLE     Transcriptional map of the 2.5-Mb CBR-ERG region of chromosome 21
            involved in Down syndrome
  JOURNAL   Genomics 48 (1), 12-23 (1998)
   PUBMED   9503011
REFERENCE   10 (residues 1 to 172)
  AUTHORS   Nakamura,A., Hattori,M. and Sakaki,Y.
  TITLE     Isolation of a novel human gene from the Down syndrome critical
            region of chromosome 21q22.2
  JOURNAL   J Biochem 122 (4), 872-877 (1997)
   PUBMED   9399594
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP001412.2, DB286372.1,
            DA311783.1, AK303624.1, D87343.1 and BX648191.1.
            
            On Sep 3, 2016 this sequence version replaced XP_005260968.1.
            
            Summary: The region of chromosome 21 between genes CBR and ERG
            (CBR-ERG region), which spans 2.5 Mb on 21q22.2, has been defined
            by analysis of patients with partial trisomy 21. It contributes
            significantly to the pathogenesis of many characteristics of Down
            syndrome, including morphological features, hypotonia, and
            cognitive disability. The DSCR3 (Down syndrome critical region gene
            3) gene is found in this region and is predictated to contain eight
            exons. DSCR3 is expressed in most tissues examined. [provided by
            RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.217128.1,
                                           SRR1660805.11901.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..172
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..172
                     /product="vacuolar protein sorting-associated protein 26C
                     isoform 2"
                     /note="Down syndrome critical region protein A; Down
                     syndrome critical region protein 3; Down syndrome critical
                     region gene 3; Down syndrome critical region 3; DSCR3
                     arrestin fold containing; vacuolar protein
                     sorting-associated protein 26C"
                     /calculated_mol_wt=19019
     Region          <31..158
                     /region_name="Arrestin_N"
                     /note="Arrestin (or S-antigen), N-terminal domain;
                     cl22903"
                     /db_xref="CDD:451447"
     CDS             1..172
                     /gene="VPS26C"
                     /gene_synonym="DCRA; DSCR3; DSCRA"
                     /coded_by="NM_001331018.1:816..1334"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS82671.1"
                     /db_xref="GeneID:10311"
                     /db_xref="HGNC:HGNC:3044"
                     /db_xref="MIM:605298"
ORIGIN      
        1 mgtaldikik rankvyhagp qkgkftpspv dftitpetlq nvkerallpk fllrghlnst
       61 ncvitqpltg elvvesseaa irsvelqlvr vetcgcaegy ardateiqni qiadgdvcrg
      121 lsvpiymvfp rlftcptlet tnfkvefevn ivvllhpdhl itenfplklc ri
//
LOCUS       NP_919307                136 aa            linear   PRI 20-NOV-2025
DEFINITION  active regulator of SIRT1 [Homo sapiens].
ACCESSION   NP_919307 XP_039373
VERSION     NP_919307.1
DBSOURCE    REFSEQ: accession NM_194326.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 136)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 136)
  AUTHORS   Weiss,S., Adolph,R.S., Schweimer,K., DiFonzo,A., Meleshin,M.,
            Schutkowski,M. and Steegborn,C.
  TITLE     Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein
  JOURNAL   Int J Mol Sci 23 (21), 12764 (2022)
   PUBMED   36361557
  REMARK    GeneRIF: Molecular Mechanism of Sirtuin 1 Modulation by the AROS
            Protein.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 136)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 136)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 136)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 136)
  AUTHORS   Kim,E.J., Kho,J.H., Kang,M.R. and Um,S.J.
  TITLE     Active regulator of SIRT1 cooperates with SIRT1 and facilitates
            suppression of p53 activity
  JOURNAL   Mol Cell 28 (2), 277-290 (2007)
   PUBMED   17964266
  REMARK    GeneRIF: Active regulator of SIRT1 (AROS) is the first direct SIRT1
            regulator to be identified that modulates p53-mediated growth
            regulation.
            Erratum:[Mol Cell. 2007 Nov 9;28(3):513]
REFERENCE   7  (residues 1 to 136)
  AUTHORS   Wang,A.G., Yoon,S.Y., Oh,J.H., Jeon,Y.J., Kim,M., Kim,J.M.,
            Byun,S.S., Yang,J.O., Kim,J.H., Kim,D.G., Yeom,Y.I., Yoo,H.S.,
            Kim,Y.S. and Kim,N.S.
  TITLE     Identification of intrahepatic cholangiocarcinoma related genes by
            comparison with normal liver tissues using expressed sequence tags
  JOURNAL   Biochem Biophys Res Commun 345 (3), 1022-1032 (2006)
   PUBMED   16712791
REFERENCE   8  (residues 1 to 136)
  AUTHORS   Maeda,N., Toku,S., Kenmochi,N. and Tanaka,T.
  TITLE     A novel nucleolar protein interacts with ribosomal protein S19
  JOURNAL   Biochem Biophys Res Commun 339 (1), 41-46 (2006)
   PUBMED   16289379
REFERENCE   9  (residues 1 to 136)
  AUTHORS   Collins,J.E., Wright,C.L., Edwards,C.A., Davis,M.P., Grinham,J.A.,
            Cole,C.G., Goward,M.E., Aguado,B., Mallya,M., Mokrab,Y.,
            Huckle,E.J., Beare,D.M. and Dunham,I.
  TITLE     A genome annotation-driven approach to cloning the human ORFeome
  JOURNAL   Genome Biol 5 (10), R84 (2004)
   PUBMED   15461802
REFERENCE   10 (residues 1 to 136)
  AUTHORS   Dunham,I., Shimizu,N., Roe,B.A., Chissoe,S., Hunt,A.R.,
            Collins,J.E., Bruskiewich,R., Beare,D.M., Clamp,M., Smink,L.J.,
            Ainscough,R., Almeida,J.P., Babbage,A., Bagguley,C., Bailey,J.,
            Barlow,K., Bates,K.N., Beasley,O., Bird,C.P., Blakey,S.,
            Bridgeman,A.M., Buck,D., Burgess,J., Burrill,W.D., O'Brien,K.P. et
            al.
  TITLE     The DNA sequence of human chromosome 22
  JOURNAL   Nature 402 (6761), 489-495 (1999)
   PUBMED   10591208
  REMARK    Erratum:[Nature 2000 Apr 20;404(6780):904]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC037573.1.
            
            On Dec 17, 2003 this sequence version replaced XP_039373.1.
            
            Transcript Variant: This variant (1) represents the predominant
            transcript and encodes the functional protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037573.1, BU175572.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968832,
                                           SAMEA2142680 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334678.8/ ENSP00000333948.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..136
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..136
                     /product="active regulator of SIRT1"
                     /note="homolog of mouse S19 binding protein; RPS19-binding
                     protein 1; 40S ribosomal protein S19-binding protein 1"
                     /calculated_mol_wt=15303
     Region          13..58
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86WX3.1)"
     Region          20..133
                     /region_name="AROS"
                     /note="Active regulator of SIRT1, or 40S ribosomal protein
                     S19-binding 1; pfam15684"
                     /db_xref="CDD:464802"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q86WX3.1)"
     CDS             1..136
                     /gene="RPS19BP1"
                     /gene_synonym="AROS; S19BP"
                     /coded_by="NM_194326.4:11..421"
                     /db_xref="CCDS:CCDS13997.1"
                     /db_xref="GeneID:91582"
                     /db_xref="HGNC:HGNC:28749"
                     /db_xref="MIM:610225"
ORIGIN      
        1 msaallrrgl ellaaseapr dppgqakprg apvkrprktk aiqaqklrns akgkvpksal
       61 deyrkrecrd hlrvnlkflt rtrstvaesv sqqilrqnrg rkacdrpvak tkkkkaegtv
      121 fteedfqkfq qeyfgs
//
LOCUS       NP_001354459             506 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 23 [Homo sapiens].
ACCESSION   NP_001354459 XP_016872224
VERSION     NP_001354459.1
DBSOURCE    REFSEQ: accession NM_001367530.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 506)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 506)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 506)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 506)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 506)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 506)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 506)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 506)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 506)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 506)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_016872224.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1150351.1,
                                           SRR3476690.370411.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..506
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..506
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 23"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=57071
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          374..501
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..506
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367530.1:95..1615"
                     /note="isoform 23 is encoded by transcript variant 23"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsaaksl lnkksdggvk krkssssvhl mepqttvvhn atdgikgste
      361 scnttteded lkvrkqeiik iteqlieain ngdfeaytki cdpgltsfep ealgnlvegm
      421 dfhkfyfenl lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg rprtsqseet
      481 rvwhrrdgkw lnvhyhcsga paaplq
//
LOCUS       NP_066190                295 aa            linear   PRI 20-NOV-2025
DEFINITION  aquaporin-9 isoform 1 [Homo sapiens].
ACCESSION   NP_066190
VERSION     NP_066190.2
DBSOURCE    REFSEQ: accession NM_020980.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 295)
  AUTHORS   Thon,P., Rahmel,T., Ziehe,D., Palmowski,L., Marko,B., Nowak,H.,
            Wolf,A., Witowski,A., Orlowski,J., Ellger,B., Wappler,F.,
            Schwier,E., Henzler,D., Kohler,T., Zarbock,A., Ehrentraut,S.F.,
            Putensen,C., Frey,U.H., Anft,M., Babel,N., Sitek,B., Adamzik,M.,
            Bergmann,L., Unterberg,M., Koos,B. and Rump,K.
  CONSRTM   SepsisDataNet.NRW Research Group
  TITLE     AQP3 and AQP9-Contrary Players in Sepsis?
  JOURNAL   Int J Mol Sci 25 (2), 1209 (2024)
   PUBMED   38279209
  REMARK    GeneRIF: AQP3 and AQP9-Contrary Players in Sepsis?
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 295)
  AUTHORS   Dong,Y., Li,J., Cao,D., Zhong,J., Liu,X., Duan,Y.G., Lee,K.F.,
            Yeung,W.S.B., Lee,C.L. and Chiu,P.C.N.
  TITLE     Integrated MicroRNA and Secretome Analysis of Human Endometrial
            Organoids Reveal the miR-3194-5p/Aquaporin/S100A9 Module in
            Regulating Trophoblast Functions
  JOURNAL   Mol Cell Proteomics 22 (4), 100526 (2023)
   PUBMED   36889440
REFERENCE   3  (residues 1 to 295)
  AUTHORS   Olmez,F., Oglak,S.C. and Can,E.
  TITLE     The Implication of Aquaporin-9 in the Pathogenesis of Preterm
            Premature Rupture of Membranes
  JOURNAL   Z Geburtshilfe Neonatol 226 (4), 233-239 (2022)
   PUBMED   35508193
  REMARK    GeneRIF: The Implication of Aquaporin-9 in the Pathogenesis of
            Preterm Premature Rupture of Membranes.
            Erratum:[Z Geburtshilfe Neonatol. 2022 Aug;226(4):e40. doi:
            10.1055/a-1845-2928. PMID: 35580619]
REFERENCE   4  (residues 1 to 295)
  AUTHORS   Ren,L., Li,P., Li,Z. and Chen,Q.
  TITLE     AQP9 and ZAP70 as immune-related prognostic biomarkers suppress
            proliferation, migration and invasion of laryngeal cancer cells
  JOURNAL   BMC Cancer 22 (1), 465 (2022)
   PUBMED   35477402
  REMARK    GeneRIF: AQP9 and ZAP70 as immune-related prognostic biomarkers
            suppress proliferation, migration and invasion of laryngeal cancer
            cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 295)
  AUTHORS   He,S., Yang,M., Yang,Y., Wang,F., Wang,X., Lu,T., Jiao,M. and Li,Y.
  TITLE     [Association study of single nucleotide polymorphisms of AQP7 and
            AQP9 genes with type 2 diabetes mellitus among ethnic Han Chinese
            population]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 39 (2), 234-239 (2022)
   PUBMED   35076928
  REMARK    GeneRIF: [Association study of single nucleotide polymorphisms of
            AQP7 and AQP9 genes with type 2 diabetes mellitus among ethnic Han
            Chinese population].
REFERENCE   6  (residues 1 to 295)
  AUTHORS   Kuriyama,H., Kawamoto,S., Ishida,N., Ohno,I., Mita,S.,
            Matsuzawa,Y., Matsubara,K. and Okubo,K.
  TITLE     Molecular cloning and expression of a novel human aquaporin from
            adipose tissue with glycerol permeability
  JOURNAL   Biochem Biophys Res Commun 241 (1), 53-58 (1997)
   PUBMED   9405233
REFERENCE   7  (residues 1 to 295)
  AUTHORS   Kuwahara,M., Gu,Y., Ishibashi,K., Marumo,F. and Sasaki,S.
  TITLE     Mercury-sensitive residues and pore site in AQP3 water channel
  JOURNAL   Biochemistry 36 (46), 13973-13978 (1997)
   PUBMED   9369468
REFERENCE   8  (residues 1 to 295)
  AUTHORS   Raina,S., Preston,G.M., Guggino,W.B. and Agre,P.
  TITLE     Molecular cloning and characterization of an aquaporin cDNA from
            salivary, lacrimal, and respiratory tissues
  JOURNAL   J Biol Chem 270 (4), 1908-1912 (1995)
   PUBMED   7530250
REFERENCE   9  (residues 1 to 295)
  AUTHORS   Zeidel,M.L., Ambudkar,S.V., Smith,B.L. and Agre,P.
  TITLE     Reconstitution of functional water channels in liposomes containing
            purified red cell CHIP28 protein
  JOURNAL   Biochemistry 31 (33), 7436-7440 (1992)
   PUBMED   1510932
REFERENCE   10 (residues 1 to 295)
  AUTHORS   Preston,G.M., Carroll,T.P., Guggino,W.B. and Agre,P.
  TITLE     Appearance of water channels in Xenopus oocytes expressing red cell
            CHIP28 protein
  JOURNAL   Science 256 (5055), 385-387 (1992)
   PUBMED   1373524
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB008775.1 and AC066616.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 14, 2007 this sequence version replaced NP_066190.1.
            
            Summary: The aquaporins are a family of water-selective membrane
            channels. This gene encodes a member of a subset of aquaporins
            called the aquaglyceroporins. This protein allows passage of a
            broad range of noncharged solutes and also stimulates urea
            transport and osmotic water permeability. This protein may also
            facilitate the uptake of glycerol in hepatic tissue . The encoded
            protein may also play a role in specialized leukocyte functions
            such as immunological response and bactericidal activity. Alternate
            splicing results in multiple transcript variants. [provided by
            RefSeq, Mar 2016].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.1295416.1,
                                           SRR1803612.80663.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000219919.9/ ENSP00000219919.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..295
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.3"
     Protein         1..295
                     /product="aquaporin-9 isoform 1"
                     /note="small solute channel 1; aquaglyceroporin-9"
                     /calculated_mol_wt=31300
     Region          21..267
                     /region_name="GlpF"
                     /note="Glycerol uptake facilitator or related aquaporin
                     (Major Intrinsic protein Family) [Carbohydrate transport
                     and metabolism]; COG0580"
                     /db_xref="CDD:440345"
     Site            25..43
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Site            58..77
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Region          84..86
                     /region_name="NPA 1.
                     /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Site            99..123
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Site            161..178
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Site            191..207
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Region          216..218
                     /region_name="NPA 2.
                     /evidence=ECO:0000250|UniProtKB:Q96PS8"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     Site            244..264
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O43315.2)"
     CDS             1..295
                     /gene="AQP9"
                     /gene_synonym="AQP-9; HsT17287; SSC1; T17287"
                     /coded_by="NM_020980.5:186..1073"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10165.1"
                     /db_xref="GeneID:366"
                     /db_xref="HGNC:HGNC:643"
                     /db_xref="MIM:602914"
ORIGIN      
        1 mqpegaekgk sfkqrlvlks slaketlsef lgtfilivlg cgcvaqails rgrfggviti
       61 nvgfsmavam aiyvaggvsg ghinpavsla mclfgrmkwf klpfyvgaqf lgafvgaatv
      121 fgiyydglms faggkllivg enatahifat ypapylslan afadqvvatm illiivfaif
      181 dsrnlgaprg lepiaiglli iviasslgln sgcamnpard lsprlftala gwgfevfrag
      241 nnfwwipvvg plvgaviggl iyvlvieihh pepdsvfkte qsedkpekye lsvim
//
LOCUS       NP_071888                268 aa            linear   PRI 20-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_071888
VERSION     NP_071888.1
DBSOURCE    REFSEQ: accession NM_022443.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 268)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 268)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 268)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 268)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 268)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 268)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 268)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 268)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 268)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 268)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK315402.1, KU178186.1,
            AC025033.20 and AA707847.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.223641.1,
                                           SRR1803617.54855.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..268
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..268
                     /product="myeloid leukemia factor 1 isoform 1"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=30496
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P58340.1)"
     Site            16..17
                     /site_type="other"
                     /note="Breakpoint for translocation to form NPM-MLF1;
                     propagated from UniProtKB/Swiss-Prot (P58340.1)"
     Region          26..202
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P58340.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:22151054; propagated from
                     UniProtKB/Swiss-Prot (P58340.1)"
     Region          44..66
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58340.1)"
     Region          50..125
                     /region_name="Interaction with COPS3.
                     /evidence=ECO:0000269|PubMed:15861129"
                     /note="propagated from UniProtKB/Swiss-Prot (P58340.1)"
     Region          209..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P58340.1)"
     CDS             1..268
                     /gene="MLF1"
                     /coded_by="NM_022443.5:108..914"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS3182.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mfrmlnssfe ddpffsesil ahrenmrqmi rsfsepfgrd llsisdgrgr ahnrrghndg
       61 edslthtdvs sfqtmdqmvs nmrnymqkle rnfgqlsvdp nghsfcsssv mtyskigdep
      121 pkvfqastqt rrapggiket rkamrdsdsg lekmaighhi hdrahvikks knkktgdeev
      181 nqefinmnes dahafdeewq sevlkykpgr hnlgntrmrs vghenpgsre lkrrekpqqs
      241 paiehgrrsn vlgdklhikg ssvksnkk
//
LOCUS       NP_000034                335 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 6 isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_000034
VERSION     NP_000034.1
DBSOURCE    REFSEQ: accession NM_000043.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 335)
  AUTHORS   Bartels,N., van der Voort,N.T.M., Opanasyuk,O., Felekyan,S.,
            Greife,A., Shang,X., Bister,A., Wiek,C., Seidel,C.A.M. and
            Monzel,C.
  TITLE     Advanced multiparametric image spectroscopy and super-resolution
            microscopy reveal a minimal model of CD95 signal initiation
  JOURNAL   Sci Adv 10 (35), eadn3238 (2024)
   PUBMED   39213362
  REMARK    GeneRIF: Advanced multiparametric image spectroscopy and
            super-resolution microscopy reveal a minimal model of CD95 signal
            initiation.
REFERENCE   2  (residues 1 to 335)
  AUTHORS   Liu,Y., Sardana,R., Nemirovsky,D., Frosina,D., Jungbluth,A.,
            Johnson,W.T., Vardhana,S., Arcila,M., Horwitz,S.M., Derkach,A.,
            Dogan,A. and Xiao,W.
  TITLE     Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma
  JOURNAL   Blood Adv 8 (12), 3064-3075 (2024)
   PUBMED   38593227
  REMARK    GeneRIF: Somatic mutations in FAS pathway increase hemophagocytic
            lymphohistiocytosis risk in patients with T- and/or NK-cell
            lymphoma.
REFERENCE   3  (residues 1 to 335)
  AUTHORS   Yang,Z., Zhang,X., Zhang,X., Liu,Y., Zhang,J. and Yuan,X.
  TITLE     [Porphyromonas gingivalis infection facilitates immune escape of
            esophageal cancer by enhancing YTHDF2-mediated Fas degradation]
  JOURNAL   Nan Fang Yi Ke Da Xue Xue Bao 44 (6), 1159-1165 (2024)
   PUBMED   38977346
  REMARK    GeneRIF: [Porphyromonas gingivalis infection facilitates immune
            escape of esophageal cancer by enhancing YTHDF2-mediated Fas
            degradation].
REFERENCE   4  (residues 1 to 335)
  AUTHORS   Staniek,J., Kalina,T., Andrieux,G., Boerries,M., Janowska,I.,
            Fuentes,M., Diez,P., Bakardjieva,M., Stancikova,J., Raabe,J.,
            Neumann,J., Schwenk,S., Arpesella,L., Stuchly,J., Benes,V., Garcia
            Valiente,R., Fernandez Garcia,J., Carsetti,R., Piano Mortari,E.,
            Catala,A., de la Calle,O., Sogkas,G., Neven,B., Rieux-Laucat,F.,
            Magerus,A., Neth,O., Olbrich,P., Voll,R.E., Alsina,L.,
            Allende,L.M., Gonzalez-Granado,L.I., Bohler,C., Thiel,J.,
            Venhoff,N., Lorenzetti,R., Warnatz,K., Unger,S., Seidl,M.,
            Mielenz,D., Schneider,P., Ehl,S., Rensing-Ehl,A., Smulski,C.R. and
            Rizzi,M.
  TITLE     Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells
  JOURNAL   Sci Immunol 9 (91), eadj5948 (2024)
   PUBMED   38215192
  REMARK    GeneRIF: Non-apoptotic FAS signaling controls mTOR activation and
            extrafollicular maturation in human B cells.
REFERENCE   5  (residues 1 to 335)
  AUTHORS   Jenkins,M., Keir,M. and McCune,J.M.
  TITLE     A membrane-bound Fas decoy receptor expressed by human thymocytes
  JOURNAL   J Biol Chem 275 (11), 7988-7993 (2000)
   PUBMED   10713117
REFERENCE   6  (residues 1 to 335)
  AUTHORS   Cascino,I., Papoff,G., Eramo,A. and Ruberti,G.
  TITLE     Soluble Fas/Apo-1 splicing variants and apoptosis
  JOURNAL   Front Biosci 1, d12-d18 (1996)
   PUBMED   9159204
  REMARK    GeneRIF: A review of alternative spliced APO-1 variants and their
            possible biological roles.
            Review article
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 335)
  AUTHORS   Cheng,J., Zhou,T., Liu,C., Shapiro,J.P., Brauer,M.J., Kiefer,M.C.,
            Barr,P.J. and Mountz,J.D.
  TITLE     Protection from Fas-mediated apoptosis by a soluble form of the Fas
            molecule
  JOURNAL   Science 263 (5154), 1759-1762 (1994)
   PUBMED   7510905
REFERENCE   8  (residues 1 to 335)
  AUTHORS   Bleesing,J.J.H., Nagaraj,C.B. and Zhang,K.
  TITLE     Autoimmune Lymphoproliferative Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301287
REFERENCE   9  (residues 1 to 335)
  AUTHORS   Inazawa,J., Itoh,N., Abe,T. and Nagata,S.
  TITLE     Assignment of the human Fas antigen gene (Fas) to 10q24.1
  JOURNAL   Genomics 14 (3), 821-822 (1992)
   PUBMED   1385309
REFERENCE   10 (residues 1 to 335)
  AUTHORS   Oehm,A., Behrmann,I., Falk,W., Pawlita,M., Maier,G., Klas,C.,
            Li-Weber,M., Richards,S., Dhein,J., Trauth,B.C. et al.
  TITLE     Purification and molecular cloning of the APO-1 cell surface
            antigen, a member of the tumor necrosis factor/nerve growth factor
            receptor superfamily. Sequence identity with the Fas antigen
  JOURNAL   J Biol Chem 267 (15), 10709-10715 (1992)
   PUBMED   1375228
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012479.1, AK290978.1,
            AL157394.15, AK026195.1 and BU620333.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains a death domain. It
            has been shown to play a central role in the physiological
            regulation of programmed cell death, and has been implicated in the
            pathogenesis of various malignancies and diseases of the immune
            system. The interaction of this receptor with its ligand allows the
            formation of a death-inducing signaling complex that includes
            Fas-associated death domain protein (FADD), caspase 8, and caspase
            10. The autoproteolytic processing of the caspases in the complex
            triggers a downstream caspase cascade, and leads to apoptosis. This
            receptor has been also shown to activate NF-kappaB, MAPK3/ERK1, and
            MAPK8/JNK, and is found to be involved in transducing the
            proliferating signals in normal diploid fibroblast and T cells.
            Several alternatively spliced transcript variants have been
            described, some of which are candidates for nonsense-mediated mRNA
            decay (NMD). The isoforms lacking the transmembrane domain may
            negatively regulate the apoptosis mediated by the full length
            isoform. [provided by RefSeq, Mar 2011].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.69751.1,
                                           SRR1163657.562566.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000652046.1/ ENSP00000498466.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..335
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.31"
     Protein         1..335
                     /product="tumor necrosis factor receptor superfamily
                     member 6 isoform 1 precursor"
                     /note="tumor necrosis factor receptor superfamily, member
                     6; APO-1 cell surface antigen; apoptosis antigen 1; Fas
                     AMA; CD95 antigen; FASLG receptor; apoptosis-mediating
                     surface antigen FAS; apoptosis signaling receptor FAS; Fas
                     (TNF receptor superfamily, member 6); TNF receptor
                     superfamily member 6; mutant tumor necrosis receptor
                     superfamily member 6"
                     /calculated_mol_wt=35080
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2670
     mat_peptide     26..335
                     /product="Tumor necrosis factor receptor superfamily
                     member 6. /id=PRO_0000034563"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
                     /calculated_mol_wt=35080
     Site            28
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          39..167
                     /region_name="TNFRSF6"
                     /note="Tumor necrosis factor receptor superfamily member 6
                     (TNFRSF6), also known as fas cell surface death receptor
                     (Fas); cd10579"
                     /db_xref="CDD:276905"
     Region          47..83
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          48..82
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276905"
     Site            order(59..65,94..97,102)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276905"
     Region          84..127
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          85..127
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276905"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19159218; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          128..166
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Region          129..149
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276905"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            174..190
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          212..317
                     /region_name="Interaction with HIPK3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            214
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P25446; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            225
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Region          226..319
                     /region_name="Death_FAS_TNFRSF6"
                     /note="Death domain of FAS or TNF receptor superfamily
                     member 6; cd08316"
                     /db_xref="CDD:260028"
     Site            order(228..229,231..232,235..236,238..239,251,284..286,
                     288..289,291,294..296,298..300,302,305..309,311,314..315)
                     /site_type="other"
                     /note="FAS-FADD heterodimer interface [polypeptide
                     binding]"
                     /db_xref="CDD:260028"
     Region          230..254
                     /region_name="Interaction with CALM.
                     /evidence=ECO:0000269|PubMed:24914971"
                     /note="propagated from UniProtKB/Swiss-Prot (P25445.1)"
     Site            250
                     /site_type="glycosylation"
                     /note="(Microbial infection) N-beta-linked (GlcNAc)
                     arginine. /evidence=ECO:0000269|PubMed:30979585,
                     ECO:0000305|PubMed:23955153; propagated from
                     UniProtKB/Swiss-Prot (P25445.1)"
     Site            order(251,307..308,311,315,318..319)
                     /site_type="other"
                     /note="octamer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     Site            order(296,299,303,306..307,314,317..318)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:260028"
     CDS             1..335
                     /gene="FAS"
                     /gene_synonym="ALPS1A; APO-1; APT1; CD95; FAS1; FASTM;
                     TNFRSF6"
                     /coded_by="NM_000043.6:80..1087"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS7393.1"
                     /db_xref="GeneID:355"
                     /db_xref="HGNC:HGNC:11920"
                     /db_xref="MIM:134637"
ORIGIN      
        1 mlgiwtllpl vltsvarlss ksvnaqvtdi nskglelrkt vttvetqnle glhhdgqfch
       61 kpcppgerka rdctvngdep dcvpcqegke ytdkahfssk crrcrlcdeg hgleveinct
      121 rtqntkcrck pnffcnstvc ehcdpctkce hgiikectlt sntkckeegs rsnlgwlcll
      181 llpiplivwv krkevqktcr khrkenqgsh esptlnpetv ainlsdvdls kyittiagvm
      241 tlsqvkgfvr kngvneakid eikndnvqdt aeqkvqllrn whqlhgkkea ydtlikdlkk
      301 anlctlaeki qtiilkdits dsensnfrne iqslv
//
LOCUS       NP_001353529             835 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 6 [Homo
            sapiens].
ACCESSION   NP_001353529 XP_011538783
VERSION     NP_001353529.1
DBSOURCE    REFSEQ: accession NM_001366600.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 835)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 835)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 835)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 835)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 835)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 835)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 835)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 835)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 835)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_011538783.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.86290.1,
                                           SRR1803617.229666.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..835
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..835
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 6"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=94173
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <537..>671
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..835
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366600.1:405..2912"
                     /note="isoform 6 is encoded by transcript variant 41"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels eseedkggkm aaadsvqqrr qyrrqnqqss sdsgssssse
      421 derpkrshvk ngevgrrrrh spsrsaspsp rkrqketspr mqmgkrwqsp vtksgrrrrs
      481 psppptrrrr spspappprr rrtptppprr rtpsppprrr spsprryspp iqrryspspp
      541 pkrrtasppp ppkrraspsp ppkrrvshsp ppkqrsspvt krrspslssk hrkgsspsrs
      601 trearspqpn krhspsprpr apqtsssppp vrrgassspq rrqspspstr pirrvsrtpe
      661 pkkikkaasp spqsvrrvss srsvsgspep aakkppapps pvqsqspstn wspavpvkka
      721 ksptpspspp rnsdqegggk kkkkkkdkkh kkdkkhkkhk khkkekavaa aaaaavtpaa
      781 iaaatttlaq eepvaapepk keteseaedn lddlekhlre kalrsmrkaq vspqs
//
LOCUS       NP_004001               3562 aa            linear   PRI 20-NOV-2025
DEFINITION  dystrophin isoform Dp427p2 [Homo sapiens].
ACCESSION   NP_004001
VERSION     NP_004001.1
DBSOURCE    REFSEQ: accession NM_004010.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3562)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 3562)
  AUTHORS   Chen,L., Luo,X., Wang,H., Tian,Y. and Liu,Y.
  TITLE     Identifying inversions with breakpoints in the Dystrophin gene
            through long-read sequencing: report of two cases
  JOURNAL   BMC Med Genomics 17 (1), 227 (2024)
   PUBMED   39251998
  REMARK    GeneRIF: Identifying inversions with breakpoints in the Dystrophin
            gene through long-read sequencing: report of two cases.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 3562)
  AUTHORS   Davies,K.E. and Vogt,J.
  TITLE     Long-term clinical follow-up of a family with Becker muscular
            dystrophy associated with a large deletion in the DMD gene
  JOURNAL   Neuromuscul Disord 39, 5-9 (2024)
   PUBMED   38653179
  REMARK    GeneRIF: Long-term clinical follow-up of a family with Becker
            muscular dystrophy associated with a large deletion in the DMD
            gene.
            Erratum:[Neuromuscul Disord. 2024 Jun;39:54. doi:
            10.1016/j.nmd.2024.05.010. PMID: 38801812]
REFERENCE   4  (residues 1 to 3562)
  AUTHORS   Achermann,J.C. and Vilain,E.J.
  TITLE     NR0B1-Related Adrenal Hypoplasia Congenita
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301604
REFERENCE   5  (residues 1 to 3562)
  AUTHORS   Hershberger,R.E. and Jordan,E.
  TITLE     Dilated Cardiomyopathy Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301486
REFERENCE   6  (residues 1 to 3562)
  AUTHORS   Darras,B.T., Urion,D.K. and Ghosh,P.S.
  TITLE     Dystrophinopathies
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301298
REFERENCE   7  (residues 1 to 3562)
  AUTHORS   Nigro,V., Politano,L., Nigro,G., Romano,S.C., Molinari,A.M. and
            Puca,G.A.
  TITLE     Detection of a nonsense mutation in the dystrophin gene by multiple
            SSCP
  JOURNAL   Hum Mol Genet 1 (7), 517-520 (1992)
   PUBMED   1307253
REFERENCE   8  (residues 1 to 3562)
  AUTHORS   Gorecki,D.C., Monaco,A.P., Derry,J.M., Walker,A.P., Barnard,E.A.
            and Barnard,P.J.
  TITLE     Expression of four alternative dystrophin transcripts in brain
            regions regulated by different promoters
  JOURNAL   Hum Mol Genet 1 (7), 505-510 (1992)
   PUBMED   1307251
REFERENCE   9  (residues 1 to 3562)
  AUTHORS   Lederfein,D., Levy,Z., Augier,N., Mornet,D., Morris,G., Fuchs,O.,
            Yaffe,D. and Nudel,U.
  TITLE     A 71-kilodalton protein is a major product of the Duchenne muscular
            dystrophy gene in brain and other nonmuscle tissues
  JOURNAL   Proc Natl Acad Sci U S A 89 (12), 5346-5350 (1992)
   PUBMED   1319059
REFERENCE   10 (residues 1 to 3562)
  AUTHORS   Koenig,M., Monaco,A.P. and Kunkel,L.M.
  TITLE     The complete sequence of dystrophin predicts a rod-shaped
            cytoskeletal protein
  JOURNAL   Cell 53 (2), 219-228 (1988)
   PUBMED   3282674
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL049643.12, S64152.1,
            M18533.1, AL109609.5 and BC028720.1.
            
            Summary: This gene spans a genomic range of greater than 2 Mb and
            encodes a large protein containing an N-terminal actin-binding
            domain and multiple spectrin repeats. The encoded protein forms a
            component of the dystrophin-glycoprotein complex (DGC), which
            bridges the inner cytoskeleton and the extracellular matrix.
            Deletions, duplications, and point mutations at this gene locus may
            cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy
            (BMD), or cardiomyopathy. Alternative promoter usage and
            alternative splicing result in numerous distinct transcript
            variants and protein isoforms for this gene. [provided by RefSeq,
            Dec 2016].
            
            Transcript Variant: The first exon of transcript Dp427p2 is 84 nt
            longer than the first exon of transcript Dp427p1. The additional
            length in Dp427p2 introduces a premature translational stop codon
            downstream of the ATG start codon used in the Dp427p1 transcript.
            The Dp427p2 transcript uses a downstream start codon compared to
            Dp427p1, and has unknown coding capacity.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: partial sample support SAMEA1965299, SAMEA1966682
                              [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..3562
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp21.2-p21.1"
     Protein         1..3562
                     /product="dystrophin isoform Dp427p2"
                     /note="mutant dystrophin"
                     /calculated_mol_wt=412271
     Region          13..123
                     /region_name="CH_DMD_rpt2"
                     /note="second calponin homology (CH) domain found in
                     dystrophin and similar proteins; cd21233"
                     /db_xref="CDD:409082"
     Site            order(13,17,68,70..71,74..75,77,86..94,101,103..104,
                     106..107,110..111,114)
                     /site_type="other"
                     /note="putative actin binding site [polypeptide binding]"
                     /db_xref="CDD:409082"
     Site            order(16..17,87..91,94,97,99..104,107,110..111,113..114,
                     118..123)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:409082"
     Region          218..435
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            325..330
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          437..704
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            545..550
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          <640..>1815
                     /region_name="235kDa-fam"
                     /note="reticulocyte binding/rhoptry protein; TIGR01612"
                     /db_xref="CDD:130673"
     Region          926..1140
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            1032..1037
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1755..1979
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cl02488"
                     /db_xref="CDD:413338"
     Site            1871..1876
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          1982..2197
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            order(2086..2088,2090..2092)
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2349..2565
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            2455..2460
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2567..2810
                     /region_name="SPEC"
                     /note="Spectrin repeats, found in several proteins
                     involved in cytoskeletal structure; family members include
                     spectrin, alpha-actinin and dystrophin; the spectrin
                     repeat forms a three helix bundle with the second helix
                     interrupted by proline in some sequences; cd00176"
                     /db_xref="CDD:238103"
     Site            2680..2685
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2811..2917
                     /region_name="Spectrin"
                     /note="Spectrin repeat; pfam00435"
                     /db_xref="CDD:395348"
     Site            2918..2922
                     /site_type="active"
                     /note="linker region [active]"
                     /db_xref="CDD:238103"
     Region          2936..2965
                     /region_name="WW"
                     /note="Two conserved tryptophans domain; also known as the
                     WWP or rsp5 domain; around 40 amino acids; functions as an
                     interaction module in a diverse set of signalling
                     proteins; binds specific proline-rich sequences but at low
                     affinities compared to other...; cd00201"
                     /db_xref="CDD:238122"
     Site            order(2949,2960)
                     /site_type="active"
                     /note="binding pocket [active]"
                     /db_xref="CDD:238122"
     Region          3002..3163
                     /region_name="EFh_DMD"
                     /note="EF-hand-like motif found in dystrophin; cd16246"
                     /db_xref="CDD:320004"
     Site            order(3002..3003,3005..3006,3024,3028,3032,3034..3035,
                     3038,3049..3055,3057..3058,3061,3067,3080,3121..3122,3124)
                     /site_type="other"
                     /note="Domain interface"
                     /db_xref="CDD:320004"
     Region          3002..3041
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3048..3082
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Site            3065..3067
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:320004"
     Region          3088..3124
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3137..3163
                     /region_name="EF-hand-like motif"
                     /note="EF-hand-like motif [structural motif]"
                     /db_xref="CDD:320004"
     Region          3188..3236
                     /region_name="ZZ_dystrophin"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     dystrophin and dystrobrevin. The ZZ motif coordinates two
                     zinc ions and most likely participates in ligand binding
                     or molecular scaffolding. Dystrophin attaches actin
                     filaments to an integral membrane...; cd02334"
                     /db_xref="CDD:239074"
     Site            order(3190,3193,3205,3208,3214,3217,3227,3231)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(3190,3193,3214,3217)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239074"
     Site            order(3191,3202,3204,3210,3212)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(3203,3218,3233,3236)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239074"
     Site            order(3205,3208,3227,3231)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239074"
     CDS             1..3562
                     /gene="DMD"
                     /gene_synonym="BMD; CMD3B; DXS142; DXS164; DXS206; DXS230;
                     DXS239; DXS268; DXS269; DXS270; DXS272; MRX85"
                     /coded_by="NM_004010.3:704..11392"
                     /note="isoform Dp427p2 is encoded by transcript variant
                     Dp427p2"
                     /db_xref="GeneID:1756"
                     /db_xref="HGNC:HGNC:2928"
                     /db_xref="MIM:300377"
ORIGIN      
        1 mknimaglqq tnsekillsw vrqstrnypq vnvinfttsw sdglalnali hshrpdlfdw
       61 nsvvcqqsat qrlehafnia ryqlgiekll dpedvdttyp dkksilmyit slfqvlpqqv
      121 sieaiqevem lprppkvtke ehfqlhhqmh ysqqitvsla qgyertsspk prfksyaytq
      181 aayvttsdpt rspfpsqhle apedksfgss lmesevnldr yqtaleevls wllsaedtlq
      241 aqgeisndve vvkdqfhthe gymmdltahq grvgnilqlg skligtgkls edeetevqeq
      301 mnllnsrwec lrvasmekqs nlhrvlmdlq nqklkelndw ltkteertrk meeeplgpdl
      361 edlkrqvqqh kvlqedleqe qvrvnslthm vvvvdessgd hataaleeql kvlgdrwani
      421 crwtedrwvl lqdillkwqr lteeqclfsa wlsekedavn kihttgfkdq nemlsslqkl
      481 avlkadlekk kqsmgklysl kqdllstlkn ksvtqkteaw ldnfarcwdn lvqkleksta
      541 qisqavtttq psltqttvme tvttvttreq ilvkhaqeel pppppqkkrq itvdseirkr
      601 ldvditelhs witrseavlq spefaifrke gnfsdlkekv naierekaek frklqdasrs
      661 aqalveqmvn egvnadsikq aseqlnsrwi efcqllserl nwleyqnnii afynqlqqle
      721 qmtttaenwl kiqpttpsep taiksqlkic kdevnrlsgl qpqierlkiq sialkekgqg
      781 pmfldadfva ftnhfkqvfs dvqarekelq tifdtlppmr yqetmsairt wvqqsetkls
      841 ipqlsvtdye imeqrlgelq alqsslqeqq sglyylsttv kemskkapse isrkyqsefe
      901 eiegrwkkls sqlvehcqkl eeqmnklrki qnhiqtlkkw maevdvflke ewpalgdsei
      961 lkkqlkqcrl lvsdiqtiqp slnsvneggq kikneaepef asrletelke lntqwdhmcq
     1021 qvyarkealk gglektvslq kdlsemhewm tqaeeeyler dfeyktpdel qkaveemkra
     1081 keeaqqkeak vklltesvns viaqappvaq ealkkeletl ttnyqwlctr lngkcktlee
     1141 vwacwhells ylekankwln evefklktte nipggaeeis evldslenlm rhsednpnqi
     1201 rilaqtltdg gvmdelinee letfnsrwre lheeavrrqk lleqsiqsaq etekslhliq
     1261 esltfidkql aayiadkvda aqmpqeaqki qsdltsheis leemkkhnqg keaaqrvlsq
     1321 idvaqkklqd vsmkfrlfqk panfeqrlqe skmildevkm hlpaletksv eqevvqsqln
     1381 hcvnlyksls evksevemvi ktgrqivqkk qtenpkelde rvtalklhyn elgakvterk
     1441 qqlekclkls rkmrkemnvl tewlaatdme ltkrsavegm psnldsevaw gkatqkeiek
     1501 qkvhlksite vgealktvlg kketlvedkl sllnsnwiav tsraeewlnl lleyqkhmet
     1561 fdqnvdhitk wiiqadtlld esekkkpqqk edvlkrlkae lndirpkvds trdqaanlma
     1621 nrgdhcrklv epqiselnhr faaishrikt gkasiplkel eqfnsdiqkl lepleaeiqq
     1681 gvnlkeedfn kdmnednegt vkellqrgdn lqqritderk reeikikqql lqtkhnalkd
     1741 lrsqrrkkal eishqwyqyk rqaddllkcl ddiekklasl peprderkik eidrelqkkk
     1801 eelnavrrqa eglsedgaam aveptqiqls krwreieskf aqfrrlnfaq ihtvreetmm
     1861 vmtedmplei syvpstylte ithvsqalle veqllnapdl cakdfedlfk qeeslknikd
     1921 slqqssgrid iihskktaal qsatpvervk lqealsqldf qwekvnkmyk drqgrfdrsv
     1981 ekwrrfhydi kifnqwltea eqflrktqip enwehakykw ylkelqdgig qrqtvvrtln
     2041 atgeeiiqqs sktdasilqe klgslnlrwq evckqlsdrk krleeqknil sefqrdlnef
     2101 vlwleeadni asiplepgke qqlkekleqv kllveelplr qgilkqlnet ggpvlvsapi
     2161 speeqdklen klkqtnlqwi kvsralpekq geieaqikdl gqlekkledl eeqlnhlllw
     2221 lspirnqlei ynqpnqegpf dvqeteiavq akqpdveeil skgqhlykek patqpvkrkl
     2281 edlssewkav nrllqelrak qpdlapgltt igasptqtvt lvtqpvvtke taisklemps
     2341 slmlevpala dfnrawtelt dwlslldqvi ksqrvmvgdl edinemiikq katmqdleqr
     2401 rpqleelita aqnlknktsn qeartiitdr ieriqnqwde vqehlqnrrq qlnemlkdst
     2461 qwleakeeae qvlgqarakl eswkegpytv daiqkkitet kqlakdlrqw qtnvdvandl
     2521 alkllrdysa ddtrkvhmit eninaswrsi hkrvsereaa leethrllqq fpldlekfla
     2581 wlteaettan vlqdatrker lledskgvke lmkqwqdlqg eieahtdvyh nldensqkil
     2641 rslegsddav llqrrldnmn fkwselrkks lnirshleas sdqwkrlhls lqellvwlql
     2701 kddelsrqap iggdfpavqk qndvhrafkr elktkepvim stletvrifl teqpleglek
     2761 lyqeprelpp eeraqnvtrl lrkqaeevnt eweklnlhsa dwqrkidetl erlqelqeat
     2821 deldlklrqa evikgswqpv gdllidslqd hlekvkalrg eiaplkenvs hvndlarqlt
     2881 tlgiqlspyn lstledlntr wkllqvaved rvrqlheahr dfgpasqhfl stsvqgpwer
     2941 aispnkvpyy inhetqttcw dhpkmtelyq sladlnnvrf sayrtamklr rlqkalcldl
     3001 lslsaacdal dqhnlkqndq pmdilqiinc lttiydrleq ehnnlvnvpl cvdmclnwll
     3061 nvydtgrtgr irvlsfktgi islckahled kyrylfkqva sstgfcdqrr lglllhdsiq
     3121 iprqlgevas fggsniepsv rscfqfannk peieaalfld wmrlepqsmv wlpvlhrvaa
     3181 aetakhqakc nickecpiig fryrslkhfn ydicqscffs grvakghkmh ypmveyctpt
     3241 tsgedvrdfa kvlknkfrtk ryfakhprmg ylpvqtvleg dnmetpvtli nfwpvdsapa
     3301 sspqlshddt hsriehyasr laemensngs ylndsispne siddehlliq hycqslnqds
     3361 plsqprspaq ilisleseer geleriladl eeenrnlqae ydrlkqqheh kglsplpspp
     3421 emmptspqsp rdaeliaeak llrqhkgrle armqiledhn kqlesqlhrl rqlleqpqae
     3481 akvngttvss pstslqrsds sqpmllrvvg sqtsdsmgee dllsppqdts tgleevmeql
     3541 nnsfpssrgr ntpgkpmred tm
//
LOCUS       NP_075065                455 aa            linear   PRI 20-NOV-2025
DEFINITION  adrenocortical dysplasia protein homolog isoform 2 [Homo sapiens].
ACCESSION   NP_075065
VERSION     NP_075065.3
DBSOURCE    REFSEQ: accession NM_022914.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 455)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 455)
  AUTHORS   Wang,Q.L., Gong,C., Meng,X.Y., Fu,M., Yang,H., Zhou,F., Wu,Q. and
            Zhou,Y.
  TITLE     TPP1 is associated with risk of advanced precursors and cervical
            cancer survival
  JOURNAL   PLoS One 19 (5), e0298118 (2024)
   PUBMED   38722833
  REMARK    GeneRIF: TPP1 is associated with risk of advanced precursors and
            cervical cancer survival.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 455)
  AUTHORS   Bertrand,A., Ba,I., Kermasson,L., Pirabakaran,V., Chable,N.,
            Lainey,E., Menard,C., Kallel,F., Picard,C., Hadiji,S.,
            Coolen-Allou,N., Blanchard,E., de Villartay,J.P., Moshous,D.,
            Roelens,M., Callebaut,I., Kannengiesser,C. and Revy,P.
  TITLE     Characterization of novel mutations in the TEL-patch domain of the
            telomeric factor TPP1 associated with telomere biology disorders
  JOURNAL   Hum Mol Genet 33 (7), 612-623 (2024)
   PUBMED   38176734
  REMARK    GeneRIF: Characterization of novel mutations in the TEL-patch
            domain of the telomeric factor TPP1 associated with telomere
            biology disorders.
REFERENCE   4  (residues 1 to 455)
  AUTHORS   Wang,H., Ma,T., Zhang,X., Chen,W., Lan,Y., Kuang,G., Hsu,S.J.,
            He,Z., Chen,Y., Stewart,J., Bhattacharjee,A., Luo,Z., Price,C. and
            Feng,X.
  TITLE     CTC1 OB-B interaction with TPP1 terminates telomerase and prevents
            telomere overextension
  JOURNAL   Nucleic Acids Res 51 (10), 4914-4928 (2023)
   PUBMED   37021555
  REMARK    GeneRIF: CTC1 OB-B interaction with TPP1 terminates telomerase and
            prevents telomere overextension.
REFERENCE   5  (residues 1 to 455)
  AUTHORS   Lambert-Lanteigne,P., Young,A. and Autexier,C.
  TITLE     Complex interaction network revealed by mutation of human
            telomerase 'insertion in fingers' and essential N-terminal domains
            and the telomere protein TPP1
  JOURNAL   J Biol Chem 299 (3), 102916 (2023)
   PUBMED   36649908
  REMARK    GeneRIF: Complex interaction network revealed by mutation of human
            telomerase 'insertion in fingers' and essential N-terminal domains
            and the telomere protein TPP1.
REFERENCE   6  (residues 1 to 455)
  AUTHORS   Liu,D., O'Connor,M.S., Qin,J. and Songyang,Z.
  TITLE     Telosome, a mammalian telomere-associated complex formed by
            multiple telomeric proteins
  JOURNAL   J Biol Chem 279 (49), 51338-51342 (2004)
   PUBMED   15383534
REFERENCE   7  (residues 1 to 455)
  AUTHORS   Houghtaling,B.R., Cuttonaro,L., Chang,W. and Smith,S.
  TITLE     A dynamic molecular link between the telomere length regulator TRF1
            and the chromosome end protector TRF2
  JOURNAL   Curr Biol 14 (18), 1621-1631 (2004)
   PUBMED   15380063
  REMARK    GeneRIF: TINT1 localized to telomeres via TIN2, where it functions
            as a negative regulator of telomerase-mediated telomere elongation.
REFERENCE   8  (residues 1 to 455)
  AUTHORS   Ye,J.Z., Hockemeyer,D., Krutchinsky,A.N., Loayza,D., Hooper,S.M.,
            Chait,B.T. and de Lange,T.
  TITLE     POT1-interacting protein PIP1: a telomere length regulator that
            recruits POT1 to the TIN2/TRF1 complex
  JOURNAL   Genes Dev 18 (14), 1649-1654 (2004)
   PUBMED   15231715
REFERENCE   9  (residues 1 to 455)
  AUTHORS   Liu,D., Safari,A., O'Connor,M.S., Chan,D.W., Laegeler,A., Qin,J.
            and Songyang,Z.
  TITLE     PTOP interacts with POT1 and regulates its localization to
            telomeres
  JOURNAL   Nat Cell Biol 6 (7), 673-680 (2004)
   PUBMED   15181449
  REMARK    GeneRIF: a paper that firstly reported cloning of human TTP1 (PTOP)
            and its biological function at telomere. TPP1 interacts with both
            POT1 and TIN2, heterodimerizes with POT1 and regulates POT1
            telomeric recruitment and telomere length.
REFERENCE   10 (residues 1 to 455)
  AUTHORS   Savage,S.A. and Niewisch,M.R.
  TITLE     Dyskeratosis Congenita and Related Telomere Biology Disorders
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK023726.1 and AF070535.1.
            
            On Jun 21, 2018 this sequence version replaced NP_075065.2.
            
            Summary: This gene encodes a protein that is involved in telomere
            function. This protein is one of six core proteins in the
            telosome/shelterin telomeric complex, which functions to maintain
            telomere length and to protect telomere ends. Through its
            interaction with other components, this protein plays a key role in
            the assembly and stabilization of this complex, and it mediates the
            access of telomerase to the telomere. Multiple transcript variants
            encoding different isoforms have been found for this gene. This
            gene, which is also referred to as TPP1, is distinct from the
            unrelated TPP1 gene on chromosome 11, which encodes
            tripeptidyl-peptidase I. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1,
            resulting in a shorter protein (isoform 2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK023726.1, SRR14038197.1831501.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..455
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..455
                     /product="adrenocortical dysplasia protein homolog isoform
                     2"
                     /note="TIN2 interacting protein 1; POT1 and
                     TIN2-interacting protein; adrenocortical dysplasia
                     homolog"
                     /calculated_mol_wt=48496
     Region          11..117
                     /region_name="TPP1"
                     /note="Shelterin complex subunit, TPP1/ACD; pfam10341"
                     /db_xref="CDD:431220"
     Region          11..13
                     /region_name="PWI"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP0.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q96AP0.4)"
     Region          155..248
                     /region_name="Interaction with POT1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP0.4)"
     Region          227..>437
                     /region_name="Atrophin-1"
                     /note="Atrophin-1 family; pfam03154"
                     /db_xref="CDD:460830"
     Region          262..365
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP0.4)"
     Region          283..>378
                     /region_name="PRK13042"
                     /note="superantigen-like protein SSL4; Reviewed"
                     /db_xref="CDD:183854"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q96AP0.4)"
     Region          384..403
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96AP0.4)"
     CDS             1..455
                     /gene="ACD"
                     /gene_synonym="DKCA6; DKCB7; PIP1; PTOP; TINT1; TPP1"
                     /coded_by="NM_022914.3:41..1408"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS10842.2"
                     /db_xref="GeneID:65057"
                     /db_xref="HGNC:HGNC:25070"
                     /db_xref="MIM:609377"
ORIGIN      
        1 magsgrlvlr pwirelilgs etpsspragq lledaeaava gpshapdtsd vgatllvsdg
       61 thsvrclvtr ealdtsdwee kefgfrgteg rllllqdcgv hvqvaeggap aefylqvdrf
      121 sllpteqprl rvpgcnqdld vqkklydcle ehlsestssn aglslsqlld emredqehqg
      181 alvclaescl tlegpctapp vthwaasrck atgeavytvp ssmlcisend qlilsslgpc
      241 qrtqgpelpp pdpalqdlsl tliasppssp sssgtpalpg hmsseesgts isllpalsla
      301 apdpgqrsss qpspaicsap atltprspha srtpssplqs ctpslsprsh vpsphqalvt
      361 rpqkpslefk efvglpcknr ppfprtgatr gaqepcsvwe ppkrhrdgsa fqyeyeppct
      421 slcarvqavr lppqlmawal hflmdaqpgs eptpm
//
LOCUS       NP_001263219             337 aa            linear   PRI 20-NOV-2025
DEFINITION  cAMP-dependent protein kinase type I-alpha regulatory subunit
            isoform b [Homo sapiens].
ACCESSION   NP_001263219
VERSION     NP_001263219.1
DBSOURCE    REFSEQ: accession NM_001276290.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Calvo,S.E., Pagliarini,D.J. and Mootha,V.K.
  TITLE     Upstream open reading frames cause widespread reduction of protein
            expression and are polymorphic among humans
  JOURNAL   Proc Natl Acad Sci U S A 106 (18), 7507-7512 (2009)
   PUBMED   19372376
  REMARK    GeneRIF: Includes the study of a disease-related upstream ORF in
            this gene, and shows that it functions to reduce protein levels by
            ~95%.
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Gupte,R.S., Pozarowski,P., Grabarek,J., Traganos,F.,
            Darzynkiewicz,Z. and Lee,M.Y.
  TITLE     RIalpha influences cellular proliferation in cancer cells by
            transporting RFC40 into the nucleus
  JOURNAL   Cancer Biol Ther 4 (4), 429-437 (2005)
   PUBMED   15846072
  REMARK    GeneRIF: A nonconventional nuclear localization sequence (NLS) has
            been found for PRKAR1A. This suggests a new function for PRKAR1A as
            a nuclear transport protein for the second subunit of RFC40.
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Bossis,I. and Stratakis,C.A.
  TITLE     Minireview: PRKAR1A: normal and abnormal functions
  JOURNAL   Endocrinology 145 (12), 5452-5458 (2004)
   PUBMED   15331577
  REMARK    GeneRIF: PRKAR1A might function as a tumor suppressor gene
            Review article
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Stergiopoulos,S.G. and Stratakis,C.A.
  TITLE     Human tumors associated with Carney complex and germline PRKAR1A
            mutations: a protein kinase A disease!
  JOURNAL   FEBS Lett 546 (1), 59-64 (2003)
   PUBMED   12829237
  REMARK    Review article
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Stratakis,C.A.
  TITLE     Carney Complex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301463
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Jones,K.W., Shapero,M.H., Chevrette,M. and Fournier,R.E.
  TITLE     Subtractive hybridization cloning of a tissue-specific
            extinguisher: TSE1 encodes a regulatory subunit of protein kinase A
  JOURNAL   Cell 66 (5), 861-872 (1991)
   PUBMED   1889088
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Boshart,M., Weih,F., Nichols,M. and Schutz,G.
  TITLE     The tissue-specific extinguisher locus TSE1 encodes a regulatory
            subunit of cAMP-dependent protein kinase
  JOURNAL   Cell 66 (5), 849-859 (1991)
   PUBMED   1832337
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Sandberg,M., Skalhegg,B. and Jahnsen,T.
  TITLE     The two mRNA forms for the type I alpha regulatory subunit of
            cAMP-dependent protein kinase from human testis are due to the use
            of different polyadenylation site signals
  JOURNAL   Biochem Biophys Res Commun 167 (1), 323-330 (1990)
   PUBMED   2310396
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Sandberg,M., Tasken,K., Oyen,O., Hansson,V. and Jahnsen,T.
  TITLE     Molecular cloning, cDNA structure and deduced amino acid sequence
            for a type I regulatory subunit of cAMP-dependent protein kinase
            from human testis
  JOURNAL   Biochem Biophys Res Commun 149 (3), 939-945 (1987)
   PUBMED   3426618
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Geahlen,R.L., Carmichael,D.F., Hashimoto,E. and Krebs,E.G.
  TITLE     Phosphorylation of cAMP-dependent protein kinase subunits
  JOURNAL   Adv Enzyme Regul 20, 195-209 (1982)
   PUBMED   6287816
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC093042.1 and AW732104.1.
            
            Summary: cAMP is a signaling molecule important for a variety of
            cellular functions. cAMP exerts its effects by activating the
            cAMP-dependent protein kinase, which transduces the signal through
            phosphorylation of different target proteins. The inactive kinase
            holoenzyme is a tetramer composed of two regulatory and two
            catalytic subunits. cAMP causes the dissociation of the inactive
            holoenzyme into a dimer of regulatory subunits bound to four cAMP
            and two free monomeric catalytic subunits. Four different
            regulatory subunits and three catalytic subunits have been
            identified in humans. This gene encodes one of the regulatory
            subunits. This protein was found to be a tissue-specific
            extinguisher that down-regulates the expression of seven liver
            genes in hepatoma x fibroblast hybrids. Mutations in this gene
            cause Carney complex (CNC). This gene can fuse to the RET
            protooncogene by gene rearrangement and form the thyroid
            tumor-specific chimeric oncogene known as PTC2. A nonconventional
            nuclear localization sequence (NLS) has been found for this protein
            which suggests a role in DNA replication via the protein serving as
            a nuclear transport protein for the second subunit of the
            Replication Factor C (RFC40). Several alternatively spliced
            transcript variants encoding two different isoforms have been
            observed. [provided by RefSeq, Jan 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.304768.1, BX438028.2
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..337
                     /product="cAMP-dependent protein kinase type I-alpha
                     regulatory subunit isoform b"
                     /EC_number="2.7.11.1"
                     /note="tissue-specific extinguisher 1; cAMP-dependent
                     protein kinase type I-alpha regulatory chain;
                     cAMP-dependent protein kinase regulatory subunit RIalpha;
                     protein kinase A type 1a regulatory subunit; epididymis
                     secretory sperm binding protein; protein kinase,
                     cAMP-dependent, regulatory, type I, alpha; Carney complex
                     type 1; protein kinase, cAMP-dependent, regulatory subunit
                     type I alpha"
                     /calculated_mol_wt=37872
     Region          1..136
                     /region_name="Dimerization and phosphorylation"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          14..63
                     /region_name="DD_RIalpha_PKA"
                     /note="dimerization/docking (D/D) domain of the Type I
                     alpha Regulatory subunit of cAMP-dependent protein kinase;
                     cd12101"
                     /db_xref="CDD:438522"
     Site            order(15,18..19,28..29,31..32,35..36)
                     /site_type="other"
                     /note="AKAP interaction site [polypeptide binding]"
                     /db_xref="CDD:438522"
     Site            order(18,21..22,27,30..31,34..35,38..39,43,45..48,50..51,
                     54..55,58)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:438522"
     Region          64..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            75
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            77
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          96..100
                     /region_name="Pseudophosphorylation motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P10644.1)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBC7; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     Region          137..246
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            order(201..202,211..213)
                     /site_type="other"
                     /note="ligand binding site [chemical binding]"
                     /db_xref="CDD:237999"
     Site            order(233..235,239..241)
                     /site_type="other"
                     /note="flexible hinge region"
                     /db_xref="CDD:237999"
     Region          255..>329
                     /region_name="CAP_ED"
                     /note="effector domain of the CAP family of transcription
                     factors; members include CAP (or cAMP receptor protein
                     (CRP)), which binds cAMP, FNR (fumarate and nitrate
                     reduction), which uses an iron-sulfur cluster to sense
                     oxygen) and CooA, a heme containing CO...; cd00038"
                     /db_xref="CDD:237999"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P09456; propagated from
                     UniProtKB/Swiss-Prot (P10644.1)"
     CDS             1..337
                     /gene="PRKAR1A"
                     /gene_synonym="ACRDYS1; ADOHR; CAR; CNC; CNC1; PKR1;
                     PPNAD1; PRKAR1; Prkar1alpha; TSE1"
                     /coded_by="NM_001276290.1:7..1020"
                     /note="isoform b is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS62307.1"
                     /db_xref="GeneID:5573"
                     /db_xref="HGNC:HGNC:9388"
                     /db_xref="MIM:188830"
ORIGIN      
        1 mesgstaase earslrecel yvqkhniqal lkdsivqlct arperpmafl reyferleke
       61 eakqiqnlqk agtrtdsred eisppppnpv vkgrrrrgai saevyteeda asyvrkvipk
      121 dyktmaalak aieknvlfsh lddnersdif damfsvsfia getviqqgde gdnfyvidqg
      181 etdvyvnnew atsvgeggsf gelaliygtp raatvkaktn vklwgidrds yrrilmgstl
      241 rkrkmyeefl skvsilesld kwerltvada lepvqfedgq kivvqgepgd effiilegsa
      301 avlqrrsene efvevgrlgp sdyfghliis rrsiplg
//
LOCUS       NP_004028                825 aa            linear   PRI 20-NOV-2025
DEFINITION  AMP deaminase 2 isoform 1 [Homo sapiens].
ACCESSION   NP_004028
VERSION     NP_004028.4
DBSOURCE    REFSEQ: accession NM_004037.9
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Flores-Mendez,M., Ohl,L., Roule,T., Zhou,Y., Tintos-Hernandez,J.A.,
            Walsh,K., Ortiz-Gonzalez,X.R. and Akizu,N.
  TITLE     IMPDH2 filaments protect from neurodegeneration in AMPD2 deficiency
  JOURNAL   EMBO Rep 25 (9), 3990-4012 (2024)
   PUBMED   39075237
  REMARK    GeneRIF: IMPDH2 filaments protect from neurodegeneration in AMPD2
            deficiency.
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Gilboa,T., Elefant,N., Meiner,V. and Hacohen,N.
  TITLE     Delineating the phenotype and genetic basis of AMPD2-related
            pontocerebellar hypoplasia
  JOURNAL   Neurogenetics 24 (1), 61-66 (2023)
   PUBMED   36445597
  REMARK    GeneRIF: Delineating the phenotype and genetic basis of
            AMPD2-related pontocerebellar hypoplasia.
REFERENCE   4  (residues 1 to 825)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   5  (residues 1 to 825)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 825)
  AUTHORS   Van den Bergh,F. and Sabina,R.L.
  TITLE     Characterization of human AMP deaminase 2 (AMPD2) gene expression
            reveals alternative transcripts encoding variable N-terminal
            extensions of isoform L
  JOURNAL   Biochem J 312 (Pt 2) (Pt 2), 401-410 (1995)
   PUBMED   8526848
REFERENCE   7  (residues 1 to 825)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
REFERENCE   8  (residues 1 to 825)
  AUTHORS   Bausch-Jurken,M.T., Mahnke-Zizelman,D.K., Morisaki,T. and
            Sabina,R.L.
  TITLE     Molecular cloning of AMP deaminase isoform L. Sequence and
            bacterial expression of human AMPD2 cDNA
  JOURNAL   J Biol Chem 267 (31), 22407-22413 (1992)
   PUBMED   1429593
REFERENCE   9  (residues 1 to 825)
  AUTHORS   Mahnke-Zizelman,D.K. and Sabina,R.L.
  TITLE     Cloning of human AMP deaminase isoform E cDNAs. Evidence for a
            third AMPD gene exhibiting alternatively spliced 5'-exons
  JOURNAL   J Biol Chem 267 (29), 20866-20877 (1992)
   PUBMED   1400401
REFERENCE   10 (residues 1 to 825)
  AUTHORS   Ashby,B. and Holmsen,H.
  TITLE     Platelet AMP deaminase. Purification and kinetic studies
  JOURNAL   J Biol Chem 256 (20), 10519-10523 (1981)
   PUBMED   7287721
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355310.20.
            
            On Mar 1, 2019 this sequence version replaced NP_004028.3.
            
            Summary: The protein encoded by this gene is important in purine
            metabolism by converting AMP to IMP. The encoded protein, which
            acts as a homotetramer, is one of three AMP deaminases found in
            mammals. Several transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Apr 2012].
            
            Transcript Variant: This variant (1) differs in the 5' UTR compared
            to variant 4. Variants 1 and 4 both encode the longest isoform (1).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660809.214359.1,
                                           SRR1660805.1620.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.3"
     Protein         1..825
                     /product="AMP deaminase 2 isoform 1"
                     /EC_number="3.5.4.6"
                     /note="adenosine monophosphate deaminase 2 (isoform L);
                     AMP deaminase 2"
                     /calculated_mol_wt=94759
     Region          1..49
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q01433.3)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            45
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            46
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            64
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            80
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBT5; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            97
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            114
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            134
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            136
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Site            138
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q01433.3)"
     Region          163..806
                     /region_name="AMP_deaminase"
                     /note="AMP deaminase; pfam19326"
                     /db_xref="CDD:437158"
     CDS             1..825
                     /gene="AMPD2"
                     /gene_synonym="AMPD; PCH9; SPG63"
                     /coded_by="NM_004037.9:35..2512"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS805.2"
                     /db_xref="GeneID:271"
                     /db_xref="HGNC:HGNC:469"
                     /db_xref="MIM:102771"
ORIGIN      
        1 masypsgsgk pkakypfkkr aslqastaap eargglgapp lqsarslpgp apclkhfpld
       61 lrtsmdgkck eiaeelftrs laeselrsap yefpeespie qleerrqrle rqisqdvkle
      121 pdillrakqd flktdsdsdl qlykeqgegq gdrslrerdv lerefqrvti sgeekcgvpf
      181 tdlldaaksv vralfireky malslqsfcp ttrrylqqla ekpletrtye qgpdtpvsad
      241 apvhppaleq hpyehcepst mpgdlglglr mvrgvvhvyt rrepdehcse velpypdlqe
      301 fvadvnvlma liingpiksf cyrrlqylss kfqmhvllne mkelaaqkkv phrdfynirk
      361 vdthihassc mnqkhllrfi kramkrhlee ivhveqgreq tlrevfesmn ltaydlsvdt
      421 ldvhadrntf hrfdkfnaky npigesvlre ifiktdnrvs gkyfahiike vmsdleesky
      481 qnaelrlsiy grsrdewdkl arwavmhrvh spnvrwlvqv prlfdvyrtk gqlanfqeml
      541 eniflplfea tvhpashpel hlflehvdgf dsvddeskpe nhvfnlespl peawveednp
      601 pyayylyytf anmamlnhlr rqrgfhtfvl rphcgeagpi hhlvsafmla enishglllr
      661 kapvlqylyy laqigiamsp lsnnslflsy hrnplpeyls rglmvslstd dplqfhftke
      721 plmeeysiat qvwklsscdm celarnsvlm sgfshkvksh wlgpnytkeg pegndirrtn
      781 vpdirvgyry etlcqelali tqavqsemle tipeeagitm spgpq
//
LOCUS       NP_001271344             518 aa            linear   PRI 20-NOV-2025
DEFINITION  2-hydroxyacyl-CoA lyase 1 isoform c [Homo sapiens].
ACCESSION   NP_001271344 XP_005265097
VERSION     NP_001271344.1
DBSOURCE    REFSEQ: accession NM_001284415.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 518)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 518)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 518)
  AUTHORS   Kitamura,T., Seki,N. and Kihara,A.
  TITLE     Phytosphingosine degradation pathway includes fatty acid
            alpha-oxidation reactions in the endoplasmic reticulum
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), E2616-E2623 (2017)
   PUBMED   28289220
REFERENCE   4  (residues 1 to 518)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 518)
  AUTHORS   Mezzar,S., de Schryver,E. and Van Veldhoven,P.P.
  TITLE     RP-HPLC-fluorescence analysis of aliphatic aldehydes: application
            to aldehyde-generating enzymes HACL1 and SGPL1
  JOURNAL   J Lipid Res 55 (3), 573-582 (2014)
   PUBMED   24323699
  REMARK    GeneRIF: Data show that a easy assay for 2-hydroxyacyl-CoA lyase
            (HACL1) and sphingosine-1-phosphate lyase (SGPL1) activities was
            developed.
REFERENCE   6  (residues 1 to 518)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   7  (residues 1 to 518)
  AUTHORS   Wanders,R.J. and Waterham,H.R.
  TITLE     Biochemistry of mammalian peroxisomes revisited
  JOURNAL   Annu Rev Biochem 75, 295-332 (2006)
   PUBMED   16756494
  REMARK    Review article
REFERENCE   8  (residues 1 to 518)
  AUTHORS   Foulon,V., Sniekers,M., Huysmans,E., Asselberghs,S., Mahieu,V.,
            Mannaerts,G.P., Van Veldhoven,P.P. and Casteels,M.
  TITLE     Breakdown of 2-hydroxylated straight chain fatty acids via
            peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the
            alpha-oxidation of straight chain fatty acids
  JOURNAL   J Biol Chem 280 (11), 9802-9812 (2005)
   PUBMED   15644336
  REMARK    GeneRIF: 2-hydroxyphytanoyl-CoA lyase has a role in the breakdown
            of long chain 2-hydroxyfatty acids
REFERENCE   9  (residues 1 to 518)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   10 (residues 1 to 518)
  AUTHORS   Foulon,V., Antonenkov,V.D., Croes,K., Waelkens,E., Mannaerts,G.P.,
            Van Veldhoven,P.P. and Casteels,M.
  TITLE     Purification, molecular cloning, and expression of
            2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine
            pyrophosphate-dependent enzyme that catalyzes the carbon-carbon
            bond cleavage during alpha-oxidation of 3-methyl-branched fatty
            acids
  JOURNAL   Proc Natl Acad Sci U S A 96 (18), 10039-10044 (1999)
   PUBMED   10468558
  REMARK    GeneRIF: peroxisomal thiamine-pyrophosphate depending enzyme
            required for the degradation of phytanic acid, catalyzing the
            cleavage of 2-hydroxyphytanoyl-CoA lyase into formyl-CoA and
            pristanal
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA609383.1, AK302086.1, BC001627.1, AJ131753.1, AA643224.1 and
            AC027129.6.
            
            On Oct 1, 2013 this sequence version replaced XP_005265097.1.
            
            Transcript Variant: This variant (3) lacks two alternate in-frame
            exons in the central coding region, compared to variant 1,
            resulting in an isoform (c) that is shorter than isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302086.1, SRR9304716.317558.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2146236, SAMEA2151741
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..518
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..518
                     /product="2-hydroxyacyl-CoA lyase 1 isoform c"
                     /EC_number="4.1.2.63"
                     /note="2-hydroxyphytanol-CoA lyase; phytanoyl-CoA
                     2-hydroxylase 2; 1600020H07Rik; phytanoyl-CoA hydroxylase
                     2; 2-hydroxyphytanoyl-CoA lyase"
                     /calculated_mol_wt=56530
     Region          7..503
                     /region_name="PRK09259"
                     /note="putative oxalyl-CoA decarboxylase; Validated"
                     /db_xref="CDD:236433"
     CDS             1..518
                     /gene="HACL1"
                     /gene_synonym="2-HPCL; HPCL; HPCL2; PHYH2"
                     /coded_by="NM_001284415.2:107..1663"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS68362.1"
                     /db_xref="GeneID:26061"
                     /db_xref="HGNC:HGNC:17856"
                     /db_xref="MIM:604300"
ORIGIN      
        1 mpdsnfaers eeqvsgakvi aqalktqdve yifgivgipv teiaiaaqql gikyigmrne
       61 qaacyaasai gyltsrpgvc lvvsgpglih alggmananm ncwpllvigg ssernqetmg
      121 afqefpqavr ssiygrpgac yvdipadfvn lqvnvnsiky mercmsppis maetsavcta
      181 asvirnakqp lliigkgaay ahaeesikkl veqyklpflp tpmgkgvvpd nhpycvgaar
      241 sralqfadvi vlfgarlnwi lhfglppryq pdvkfiqvdi caeelgnnvk pavtllgnih
      301 avtkqelask kslpmnyytv fyhvqeqlpr dcfvvsegan tmdigrtvlq nylprhrlda
      361 gtfgtmgvgl gfaiaaavva kdrspgqwii cvegdsafgf sgmeveticr ynlpiillvv
      421 nnngiyqgfd tdtwkemlkf qdatavvppm cllpnshyeq vmtafggkgy fvqtpeelqk
      481 slrqsladtt kpslinimie pqatrkaqdf hwltrsnm
//
LOCUS       NP_004990               1285 aa            linear   PRI 20-NOV-2025
DEFINITION  unconventional myosin-VI isoform 1 [Homo sapiens].
ACCESSION   NP_004990 XP_376516
VERSION     NP_004990.3
DBSOURCE    REFSEQ: accession NM_004999.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1285)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1285)
  AUTHORS   Zheng,S., Hong,Z., Tan,Y., Wang,Y., Li,J., Zhang,Z., Feng,T.,
            Hong,Z., Lin,G. and Ye,D.
  TITLE     MYO6 contributes to tumor progression and enzalutamide resistance
            in castration-resistant prostate cancer by activating the focal
            adhesion signaling pathway
  JOURNAL   Cell Commun Signal 22 (1), 517 (2024)
   PUBMED   39449086
  REMARK    GeneRIF: MYO6 contributes to tumor progression and enzalutamide
            resistance in castration-resistant prostate cancer by activating
            the focal adhesion signaling pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1285)
  AUTHORS   Raghuvanshi,R., Panda,K.C., Ray,C.S. and Ramchander,P.V.
  TITLE     Targeted Next-Generation Sequencing Analysis Reveals a Novel
            Genetic Variant in MYO6 Gene in an Indian Family with Postlingual
            Nonsyndromic Hearing Loss
  JOURNAL   Genet Test Mol Biomarkers 28 (8), 328-336 (2024)
   PUBMED   39019031
  REMARK    GeneRIF: Targeted Next-Generation Sequencing Analysis Reveals a
            Novel Genetic Variant in MYO6 Gene in an Indian Family with
            Postlingual Nonsyndromic Hearing Loss.
REFERENCE   4  (residues 1 to 1285)
  AUTHORS   Canon,L., Kikuti,C., Planelles-Herrero,V.J., Lin,T., Mayeux,F.,
            Sirkia,H., Lee,Y.I., Heidsieck,L., Velikovsky,L., David,A., Liu,X.,
            Moussaoui,D., Forest,E., Hook,P., Petersen,K.J., Morgan,T.E., Di
            Cicco,A., Sires-Campos,J., Derivery,E., Levy,D., Delevoye,C.,
            Sweeney,H.L. and Houdusse,A.
  TITLE     How myosin VI traps its off-state, is activated and dimerizes
  JOURNAL   Nat Commun 14 (1), 6732 (2023)
   PUBMED   37872146
  REMARK    GeneRIF: How myosin VI traps its off-state, is activated and
            dimerizes.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1285)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 1285)
  AUTHORS   Avraham,K.B., Hasson,T., Sobe,T., Balsara,B., Testa,J.R.,
            Skvorak,A.B., Morton,C.C., Copeland,N.G. and Jenkins,N.A.
  TITLE     Characterization of unconventional MYO6, the human homologue of the
            gene responsible for deafness in Snell's waltzer mice
  JOURNAL   Hum Mol Genet 6 (8), 1225-1231 (1997)
   PUBMED   9259267
REFERENCE   7  (residues 1 to 1285)
  AUTHORS   Avraham,K.B., Hasson,T., Steel,K.P., Kingsley,D.M., Russell,L.B.,
            Mooseker,M.S., Copeland,N.G. and Jenkins,N.A.
  TITLE     The mouse Snell's waltzer deafness gene encodes an unconventional
            myosin required for structural integrity of inner ear hair cells
  JOURNAL   Nat Genet 11 (4), 369-375 (1995)
   PUBMED   7493015
REFERENCE   8  (residues 1 to 1285)
  AUTHORS   Hasson,T. and Mooseker,M.S.
  TITLE     Porcine myosin-VI: characterization of a new mammalian
            unconventional myosin
  JOURNAL   J Cell Biol 127 (2), 425-440 (1994)
   PUBMED   7929586
REFERENCE   9  (residues 1 to 1285)
  AUTHORS   Bement,W.M., Hasson,T., Wirth,J.A., Cheney,R.E. and Mooseker,M.S.
  TITLE     Identification and overlapping expression of multiple
            unconventional myosin genes in vertebrate cell types
  JOURNAL   Proc Natl Acad Sci U S A 91 (14), 6549-6553 (1994)
   PUBMED   8022818
  REMARK    Erratum:[Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11767. doi:
            10.1073/pnas.91.24.11767-c. PMID: 7972138]
REFERENCE   10 (residues 1 to 1285)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB088907.1, AB002387.1,
            AL136093.8 and AL392166.19.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 19, 2006 this sequence version replaced NP_004990.2.
            
            Summary: This gene encodes a reverse-direction motor protein that
            moves toward the minus end of actin filaments and plays a role in
            intracellular vesicle and organelle transport. The protein consists
            of a motor domain containing an ATP- and an actin-binding site and
            a globular tail which interacts with other proteins. This protein
            maintains the structural integrity of inner ear hair cells and
            mutations in this gene cause non-syndromic autosomal dominant and
            recessive hearing loss. Alternative splicing results in multiple
            transcript variants encoding distinct isoforms. [provided by
            RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) encodes isoform (1). Isoforms
            1 and 8 are the same length but differ in sequence.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.189978.1,
                                           SRR1660807.103545.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2144335, SAMEA2155770
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369977.8/ ENSP00000358994.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1285
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q14.1"
     Protein         1..1285
                     /product="unconventional myosin-VI isoform 1"
                     /note="unconventional myosin-6; unconventional myosin-VI"
                     /calculated_mol_wt=148584
     Region          71..759
                     /region_name="MYSc_Myo6"
                     /note="class VI myosin, motor domain; cd01382"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107,151..158,195..205,456..461)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276833"
     Site            order(98..100,102..107)
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276833"
     Site            151..158
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276833"
     Site            195..205
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276833"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          273..317
                     /region_name="Responsible for slow ATPase activity.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            405
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            456..461
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276833"
     Site            order(485..496,499..508)
                     /site_type="active"
                     /note="relay loop [active]"
                     /db_xref="CDD:276833"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64331; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          665..672
                     /region_name="Actin-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            693..703
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276833"
     Site            705..759
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276833"
     Region          770..917
                     /region_name="CBD_MYO6-like"
                     /note="calmodulin binding domain found in unconventional
                     myosin-VI and similar proteins; cd21759"
                     /db_xref="CDD:409646"
     Region          782..810
                     /region_name="Required for binding calmodulin.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            order(786,789..790,792..810,812..813,816..831,833,
                     836..837,840..841,886)
                     /site_type="other"
                     /note="calmodulin binding site [polypeptide binding]"
                     /db_xref="CDD:409646"
     Site            820..830
                     /site_type="other"
                     /note="IQ motif"
                     /db_xref="CDD:409646"
     Region          835..916
                     /region_name="Three-helix bundle.
                     /evidence=ECO:0000250|UniProtKB:Q29122"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          917..984
                     /region_name="SAH. /evidence=ECO:0000269|PubMed:18511944"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          934..955
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          999..1059
                     /region_name="MYO6_MIU_linker"
                     /note="MIU-linker domain found in unconventional
                     myosin-VI; cd22294"
                     /db_xref="CDD:412090"
     Site            999..1024
                     /site_type="other"
                     /note="MIU motif"
                     /db_xref="CDD:412090"
     Site            1025
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64331; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1051..1276
                     /region_name="Interaction with TAX1BP1 and CALCOCO2/NDP52.
                     /evidence=ECO:0000269|PubMed:31371777"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1073..1113
                     /region_name="MyUb_Myo6"
                     /note="myosin VI ubiquitin-binding domain (MyUb) found in
                     unconventional myosin-VI and similar proteins; cd21958"
                     /db_xref="CDD:439319"
     Site            order(1078..1079,1081..1082,1108..1109,1111..1112)
                     /site_type="other"
                     /note="clathrin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Site            order(1081..1083,1086..1087,1089..1093,1095,1098..1099,
                     1102,1105..1106)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:439319"
     Region          1107..1109
                     /region_name="Interaction with OPTN.
                     /evidence=ECO:0000250|UniProtKB:Q9I8D1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Site            1146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q64331; propagated from
                     UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1148..1276
                     /region_name="Interaction with TOM1.
                     /evidence=ECO:0000269|PubMed:31371777"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UM54.4)"
     Region          1168..1258
                     /region_name="Myosin-VI_CBD"
                     /note="Myosin VI cargo binding domain; pfam16521"
                     /db_xref="CDD:465157"
     CDS             1..1285
                     /gene="MYO6"
                     /gene_synonym="DFNA22; DFNB37"
                     /coded_by="NM_004999.4:233..4090"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS34487.1"
                     /db_xref="GeneID:4646"
                     /db_xref="HGNC:HGNC:7605"
                     /db_xref="MIM:600970"
ORIGIN      
        1 medgkpvwap hptdgfqmgn ivdigpdslt ieplnqkgkt flalinqvfp aeedskkdve
       61 dncslmylne atllhnikvr yskdriytyv aniliavnpy fdipkiysse aiksyqgksl
      121 gtrpphvfai adkafrdmkv lkmsqsiivs gesgagkten tkfvlrylte sygtgqdidd
      181 riveanplle afgnaktvrn nnssrfgkfv eihfnekssv vggfvshyll eksricvqgk
      241 eernyhifyr lcagasedir eklhlsspdn frylnrgctr yfanketdkq ilqnrkspey
      301 lkagsmkdpl lddhgdfirm ctamkkigld deekldlfrv vagvlhlgni dfeeagstsg
      361 gcnlknksaq sleycaellg ldqddlrvsl ttrvmlttag gtkgtvikvp lkveqannar
      421 dalaktvysh lfdhvvnrvn qcfpfetssy figvldiagf eyfehnsfeq fcinycnekl
      481 qqffnerilk eeqelyqkeg lgvnevhyvd nqdcidliea klvgildild eenrlpqpsd
      541 qhftsavhqk hkdhfrltip rksklavhrn irddegfiir hfagavcyet tqfveknnda
      601 lhmsleslic esrdkfirel fesstnnnkd tkqkagklsf isvgnkfktq lnllldklrs
      661 tgasfircik pnlkmtshhf egaqilsqlq csgmvsvldl mqggypsras fhelynmykk
      721 ympdklarld prlfckalfk alglnendyk fgltkvffrp gkfaefdqim ksdpdhlael
      781 vkrvnhwltc srwkkvqwcs lsviklknki kyraeacikm qktirmwlck rrhkpridgl
      841 vkvgtlkkrl dkfnevvsvl kdgkpemnkq iknleisidt lmakikstmm tqeqiqkeyd
      901 alvksseell salqkkkqqe eeaerlrriq eemekerkrr eedekrrrke eeerrmklem
      961 eakrkqeeee rkkreddekr iqaeveaqla rqkeeesqqq avleqerrdr elalriaqse
     1021 aelisdeaqa dlalrrndgt rpkmtpeqma kemseflsrg pavlatkaaa gtkkydlskw
     1081 kyaelrdtin tscdiellaa creefhrrlk vyhawksknk krnteteqra pksvtdydfa
     1141 pflnnspqqn paaqiparqr eiemnrqqrf fripfirpad qykdpqskkk gwwyahfdgp
     1201 wiarqmelhp dkppillvag kddmemceln leetgltrkr gaeilprqfe eiwercggiq
     1261 ylqnaiesrq arptyataml qsllk
//
LOCUS       NP_004227                443 aa            linear   PRI 20-NOV-2025
DEFINITION  COP9 signalosome complex subunit 2 isoform 1 [Homo sapiens].
ACCESSION   NP_004227
VERSION     NP_004227.1
DBSOURCE    REFSEQ: accession NM_004236.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 443)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 443)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 443)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 443)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 443)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 443)
  AUTHORS   Dressel,U., Thormeyer,D., Altincicek,B., Paululat,A., Eggert,M.,
            Schneider,S., Tenbaum,S.P., Renkawitz,R. and Baniahmad,A.
  TITLE     Alien, a highly conserved protein with characteristics of a
            corepressor for members of the nuclear hormone receptor superfamily
  JOURNAL   Mol Cell Biol 19 (5), 3383-3394 (1999)
   PUBMED   10207062
REFERENCE   7  (residues 1 to 443)
  AUTHORS   Schaefer,L., Beermann,M.L. and Miller,J.B.
  TITLE     Coding sequence, genomic organization, chromosomal localization,
            and expression pattern of the signalosome component Cops2: the
            mouse homologue of Drosophila alien
  JOURNAL   Genomics 56 (3), 310-316 (1999)
   PUBMED   10087198
REFERENCE   8  (residues 1 to 443)
  AUTHORS   Wei,N., Tsuge,T., Serino,G., Dohmae,N., Takio,K., Matsui,M. and
            Deng,X.W.
  TITLE     The COP9 complex is conserved between plants and mammals and is
            related to the 26S proteasome regulatory complex
  JOURNAL   Curr Biol 8 (16), 919-922 (1998)
   PUBMED   9707402
REFERENCE   9  (residues 1 to 443)
  AUTHORS   Seeger,M., Kraft,R., Ferrell,K., Bech-Otschir,D., Dumdey,R.,
            Schade,R., Gordon,C., Naumann,M. and Dubiel,W.
  TITLE     A novel protein complex involved in signal transduction possessing
            similarities to 26S proteasome subunits
  JOURNAL   FASEB J 12 (6), 469-478 (1998)
   PUBMED   9535219
REFERENCE   10 (residues 1 to 443)
  AUTHORS   Lee,J.W., Choi,H.S., Gyuris,J., Brent,R. and Moore,D.D.
  TITLE     Two classes of proteins dependent on either the presence or absence
            of thyroid hormone for interaction with the thyroid hormone
            receptor
  JOURNAL   Mol Endocrinol 9 (2), 243-254 (1995)
   PUBMED   7776974
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB059510.1, BC012629.1, CN287009.1, BX648602.1, CN281648.1,
            BM667648.1 and AC013452.9.
            
            Transcript Variant: This variant (1) has an exon with an
            alternative splice acceptor site in the 5' coding region, compared
            to variant 2, which results in a shorter protein (isoform 1),
            compared to isoform 2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222590.1, BC012629.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000388901.10/ ENSP00000373553.5
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..443
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.1"
     Protein         1..443
                     /product="COP9 signalosome complex subunit 2 isoform 1"
                     /note="COP9 signalosome complex subunit 2; JAB1-containing
                     signalosome subunit 2; TRIP-15; alien homolog;
                     TR-interacting protein 15; thyroid receptor-interacting
                     protein 15; COP9 constitutive photomorphogenic homolog
                     subunit 2"
                     /calculated_mol_wt=51466
     Region          1..275
                     /region_name="Mediates interaction with NIF3L1.
                     /evidence=ECO:0000250|UniProtKB:P61203"
                     /note="propagated from UniProtKB/Swiss-Prot (P61201.1)"
     Region          40..434
                     /region_name="RPN6"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5159"
                     /db_xref="CDD:227488"
     Region          309..413
                     /region_name="PCI"
                     /note="PCI domain; pfam01399"
                     /db_xref="CDD:460195"
     CDS             1..443
                     /gene="COPS2"
                     /gene_synonym="ALIEN; CSN2; SGN2; TRIP15"
                     /coded_by="NM_004236.4:22..1353"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32235.1"
                     /db_xref="GeneID:9318"
                     /db_xref="HGNC:HGNC:30747"
                     /db_xref="MIM:604508"
ORIGIN      
        1 msdmeddfmc ddeedydley sedsnsepnv dlenqyynsk alkeddpkaa lssfqkvlel
       61 egekgewgfk alkqmikinf kltnfpemmn rykqlltyir savtrnysek sinsildyis
      121 tskqmdllqe fyettlealk dakndrlwfk tntklgklyl ereeygklqk ilrqlhqscq
      181 tddgeddlkk gtqlleiyal eiqmytaqkn nkklkalyeq slhiksaiph plimgvirec
      241 ggkmhlrege fekahtdffe afknydesgs prrttclkyl vlanmlmksg inpfdsqeak
      301 pykndpeila mtnlvsayqn nditefekil ktnhsnimdd pfirehieel lrnirtqvli
      361 klikpytrih ipfiskelni dvadvesllv qcildntihg ridqvnqlle ldhqkrggar
      421 ytaldkwtnq lnslnqavvs kla
//
LOCUS       NP_001287786             169 aa            linear   PRI 20-NOV-2025
DEFINITION  fos-related antigen 1 isoform 5 [Homo sapiens].
ACCESSION   NP_001287786
VERSION     NP_001287786.1
DBSOURCE    REFSEQ: accession NM_001300857.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Li,L., Li,D., Jin,J., Xu,F., He,N., Ren,Y., Wang,X., Tian,L.,
            Chen,B., Li,X., Chen,Z., Zhang,L., Qiao,L., Wang,L. and Wang,J.
  TITLE     FOSL1-mediated LINC01566 negatively regulates CD4+ T-cell
            activation in myasthenia gravis
  JOURNAL   J Neuroinflammation 21 (1), 197 (2024)
   PUBMED   39113081
  REMARK    GeneRIF: FOSL1-mediated LINC01566 negatively regulates CD4[+]
            T-cell activation in myasthenia gravis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Wang,H., Shi,Y., Zhou,X., Zhang,L., Yang,A., Zhou,D. and Ma,T.
  TITLE     HNRNPA2B1 stabilizes NFATC3 levels to potentiate its combined
            actions with FOSL1 to mediate vasculogenic mimicry in GBM cells
  JOURNAL   Cell Biol Toxicol 40 (1), 44 (2024)
   PUBMED   38862832
  REMARK    GeneRIF: HNRNPA2B1 stabilizes NFATC3 levels to potentiate its
            combined actions with FOSL1 to mediate vasculogenic mimicry in GBM
            cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Ramar,V., Guo,S., Hudson,B., Khedri,A., Guo,A.A., Li,J. and Liu,M.
  TITLE     Interaction of NF-kappaB and FOSL1 drives glioma stemness
  JOURNAL   Cell Mol Life Sci 81 (1), 255 (2024)
   PUBMED   38856747
  REMARK    GeneRIF: Interaction of NF-kappaB and FOSL1 drives glioma stemness.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 169)
  AUTHORS   Luo,X., Wang,J., Chen,Y., Zhou,X., Shao,Z., Liu,K. and Shang,Z.
  TITLE     Melatonin inhibits the stemness of head and neck squamous cell
            carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis
  JOURNAL   J Pineal Res 76 (2), e12940 (2024)
   PUBMED   38402581
  REMARK    GeneRIF: Melatonin inhibits the stemness of head and neck squamous
            cell carcinoma by modulating HA synthesis via the FOSL1/HAS3 axis.
REFERENCE   6  (residues 1 to 169)
  AUTHORS   Arts,J., Herr,I., Lansink,M., Angel,P. and Kooistra,T.
  TITLE     Cell-type specific DNA-protein interactions at the tissue-type
            plasminogen activator promoter in human endothelial and HeLa cells
            in vivo and in vitro
  JOURNAL   Nucleic Acids Res 25 (2), 311-317 (1997)
   PUBMED   9016559
REFERENCE   7  (residues 1 to 169)
  AUTHORS   Courseaux,A., Grosgeorge,J., Gaudray,P., Pannett,A.A., Forbes,S.A.,
            Williamson,C., Bassett,D., Thakker,R.V., Teh,B.T., Farnebo,F.,
            Shepherd,J., Skogseid,B., Larsson,C., Giraud,S., Zhang,C.X.,
            Salandre,J. and Calender,A.
  TITLE     Definition of the minimal MEN1 candidate area based on a 5-Mb
            integrated map of proximal 11q13. The European Consortium on Men1,
            (GENEM 1; Groupe d'Etude des Neoplasies Endocriniennes Multiples de
            type 1)
  JOURNAL   Genomics 37 (3), 354-365 (1996)
   PUBMED   8938448
REFERENCE   8  (residues 1 to 169)
  AUTHORS   Tsuchiya,H., Fujii,M., Niki,T., Tokuhara,M., Matsui,M. and Seiki,M.
  TITLE     Human T-cell leukemia virus type 1 Tax activates transcription of
            the human fra-1 gene through multiple cis elements responsive to
            transmembrane signals
  JOURNAL   J Virol 67 (12), 7001-7007 (1993)
   PUBMED   8230424
REFERENCE   9  (residues 1 to 169)
  AUTHORS   Sinke,R.J., Tanigami,A., Nakamura,Y. and Geurts van Kessel,A.
  TITLE     Reverse mapping of the gene encoding the human fos-related
            antigen-1 (fra-1) within chromosome band 11q13
  JOURNAL   Genomics 18 (1), 165 (1993)
   PUBMED   8276409
REFERENCE   10 (residues 1 to 169)
  AUTHORS   Matsui,M., Tokuhara,M., Konuma,Y., Nomura,N. and Ishizaki,R.
  TITLE     Isolation of human fos-related genes and their expression during
            monocyte-macrophage differentiation
  JOURNAL   Oncogene 5 (3), 249-255 (1990)
   PUBMED   2107490
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BQ937004.1, BM846271.1,
            BC016648.1, AA120824.1 and AP006287.2.
            
            Summary: The Fos gene family consists of 4 members: FOS, FOSB,
            FOSL1, and FOSL2. These genes encode leucine zipper proteins that
            can dimerize with proteins of the JUN family, thereby forming the
            transcription factor complex AP-1. As such, the FOS proteins have
            been implicated as regulators of cell proliferation,
            differentiation, and transformation. Several transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (5) lacks two alternate in-frame
            exons compared to variant 1. The resulting isoform (5) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK299050.1, SRR5189658.70764.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154405
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.1"
     Protein         1..169
                     /product="fos-related antigen 1 isoform 5"
                     /note="FOS-like antigen-1; fos-related antigen 1; FOS like
                     1, AP-1 trancription factor subunit"
                     /calculated_mol_wt=17428
     Region          <34..66
                     /region_name="bZIP"
                     /note="Basic leucine zipper (bZIP) domain of bZIP
                     transcription factors: a DNA-binding and dimerization
                     domain; cl21462"
                     /db_xref="CDD:473870"
     Region          35..>148
                     /region_name="PRK13729"
                     /note="conjugal transfer pilus assembly protein TraB;
                     Provisional"
                     /db_xref="CDD:184281"
     CDS             1..169
                     /gene="FOSL1"
                     /gene_synonym="FRA; fra-1; FRA1"
                     /coded_by="NM_001300857.2:50..559"
                     /note="isoform 5 is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS76436.1"
                     /db_xref="GeneID:8061"
                     /db_xref="HGNC:HGNC:13718"
                     /db_xref="MIM:136515"
ORIGIN      
        1 mfrdfgepgp ssgngggygg paqppaaaqa aqqetdkled eksglqreie elqkqkerle
       61 lvleahrpic kipegakegd tgstsgtssp papcrpvpci slspgpvlep ealhtptlmt
      121 tpsltpftps lvftypstpe pcasahrkss sssgdpssdp lgsptllal
//
LOCUS       NP_001356713             243 aa            linear   PRI 20-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001356713 XP_011511155
VERSION     NP_001356713.1
DBSOURCE    REFSEQ: accession NM_001369784.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 243)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 243)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 243)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 243)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 243)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 243)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 243)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 243)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 243)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9 and AC025033.20.
            
            On Apr 18, 2019 this sequence version replaced XP_011511155.1.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189667.271460.1,
                                           SRR1803614.308958.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968832
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..243
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..243
                     /product="myeloid leukemia factor 1 isoform 2"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=27494
     Region          1..177
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..243
                     /gene="MLF1"
                     /coded_by="NM_001369784.1:256..987"
                     /note="isoform 2 is encoded by transcript variant 10"
                     /db_xref="CCDS:CCDS46945.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mrqmirsfse pfgrdllsis dgrgrahnrr ghndgedslt htdvssfqtm dqmvsnmrny
       61 mqklernfgq lsvdpnghsf csssvmtysk igdeppkvfq astqtrrapg giketrkamr
      121 dsdsglekma ighhihdrah vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk
      181 ykpgrhnlgn trmrsvghen pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks
      241 nkk
//
LOCUS       NP_001159524             210 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform d
            [Homo sapiens].
ACCESSION   NP_001159524
VERSION     NP_001159524.1
DBSOURCE    REFSEQ: accession NM_001166052.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 210)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 210)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC400218.1, AK299800.1,
            AC131953.1 and AL080130.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (5) differs in the presence and
            absence of exons in the 5' UTR and 5' coding region, and uses a
            downstream translational start codon, compared to variant 1. The
            resulting isoform (d) is significantly shorter at the N-terminus,
            compared to isoform a. Variants 4, 5, 6 and 7 encode the same
            isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038197.1142797.1,
                                           SRR1660803.231546.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..210
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform d"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=23357
     Region          34..160
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(45,119,138)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(56,58,106..107,109..116,118,126,132,142,144,147,151,
                     154..155,157..158)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..210
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001166052.2:290..922"
                     /note="isoform d is encoded by transcript variant 5"
                     /db_xref="CCDS:CCDS54760.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 maerknakal acsslqeran vnldvplqvd fptpktelvq kfhvqylgml pvdkpvgmdi
       61 lnsaienlmt ssnkedwlsv nmnvadatvt visekneeev lvecrvrfls fmgvgkdvht
      121 fafimdtgnq rfechvfwce pnagnvseav qaacmlryqk clvarppsqk vrpppppads
      181 vtrrvttnvk rgvlslidtl kqkrpvtemp
//
LOCUS       NP_001306871             218 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane and immunoglobulin domain-containing protein 1
            isoform 2 precursor [Homo sapiens].
ACCESSION   NP_001306871 XP_005258026
VERSION     NP_001306871.1
DBSOURCE    REFSEQ: accession NM_001319942.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 218)
  AUTHORS   Zhou,L., Zhu,L., Wu,X., Hu,S., Zhang,S., Ning,M., Yu,J. and Chen,M.
  TITLE     Decreased TMIGD1 aggravates colitis and intestinal barrier
            dysfunction via the BANF1-NF-kappaB pathway in Crohn's disease
  JOURNAL   BMC Med 21 (1), 287 (2023)
   PUBMED   37542259
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 218)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 218)
  AUTHORS   Mu,L., Wang,Y., Hu,Y., Shi,C., Alman,B.A., Zhang,C. and She,J.
  TITLE     The Role of TMIGD1 as a Tumor Suppressor in Colorectal Cancer
  JOURNAL   Genet Test Mol Biomarkers 26 (4), 174-183 (2022)
   PUBMED   35481970
  REMARK    GeneRIF: The Role of TMIGD1 as a Tumor Suppressor in Colorectal
            Cancer.
REFERENCE   4  (residues 1 to 218)
  AUTHORS   De La Cena,K.O.C., Ho,R.X., Amraei,R., Woolf,N., Tashjian,J.Y.,
            Zhao,Q., Richards,S., Walker,J., Huang,J., Chitalia,V.C. and
            Rahimi,N.
  TITLE     Transmembrane and Immunoglobulin Domain Containing 1, a Putative
            Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint Arrest in
            Colon Cancer Cells
  JOURNAL   Am J Pathol 191 (1), 157-167 (2021)
   PUBMED   33129760
  REMARK    GeneRIF: Transmembrane and Immunoglobulin Domain Containing 1, a
            Putative Tumor Suppressor, Induces G2/M Cell Cycle Checkpoint
            Arrest in Colon Cancer Cells.
REFERENCE   5  (residues 1 to 218)
  AUTHORS   Zabana,Y., Loren,V., Domenech,E., Aterido,A.,
            Garcia-Jaraquemada,A., Julia,A., Vicario,M., Pedrosa,E.,
            Ferreiro,M., Troya,J., Lozano,J.J., Sarrias,M.R., Cabre,E.,
            Manosa,M. and Manye,J.
  TITLE     Transcriptomic identification of TMIGD1 and its relationship with
            the ileal epithelial cell differentiation in Crohn's disease
  JOURNAL   Am J Physiol Gastrointest Liver Physiol 319 (2), G109-G120 (2020)
   PUBMED   32508154
  REMARK    GeneRIF: Transcriptomic identification of TMIGD1 and its
            relationship with the ileal epithelial cell differentiation in
            Crohn's disease.
REFERENCE   6  (residues 1 to 218)
  AUTHORS   Hartmann,C., Schwietzer,Y.A., Kummer,D., Kirschnick,N., Hoppe,E.,
            Thuring,E.M., Glaesner-Ebnet,M., Brinkmann,F., Gerke,V., Reuter,S.,
            Nakayama,M. and Ebnet,K.
  TITLE     The mitochondrial outer membrane protein SYNJ2BP interacts with the
            cell adhesion molecule TMIGD1 and can recruit it to mitochondria
  JOURNAL   BMC Mol Cell Biol 21 (1), 30 (2020)
   PUBMED   32303178
  REMARK    GeneRIF: The mitochondrial outer membrane protein SYNJ2BP interacts
            with the cell adhesion molecule TMIGD1 and can recruit it to
            mitochondria.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 218)
  AUTHORS   Arafa,E., Bondzie,P.A., Rezazadeh,K., Meyer,R.D., Hartsough,E.,
            Henderson,J.M., Schwartz,J.H., Chitalia,V. and Rahimi,N.
  TITLE     TMIGD1 is a novel adhesion molecule that protects epithelial cells
            from oxidative cell injury
  JOURNAL   Am J Pathol 185 (10), 2757-2767 (2015)
   PUBMED   26342724
  REMARK    GeneRIF: identified TMIGD1 as a novel cell adhesion molecule
            expressed in kidney epithelial cells that protects kidney
            epithelial cells from oxidative cell injury to promote cell
            survival
REFERENCE   8  (residues 1 to 218)
  AUTHORS   Ivarsson,Y., Arnold,R., McLaughlin,M., Nim,S., Joshi,R., Ray,D.,
            Liu,B., Teyra,J., Pawson,T., Moffat,J., Li,S.S., Sidhu,S.S. and
            Kim,P.M.
  TITLE     Large-scale interaction profiling of PDZ domains through proteomic
            peptide-phage display using human and viral phage peptidomes
  JOURNAL   Proc Natl Acad Sci U S A 111 (7), 2542-2547 (2014)
   PUBMED   24550280
REFERENCE   9  (residues 1 to 218)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK172838.1 and AC087644.8.
            
            On Feb 6, 2016 this sequence version replaced XP_005258026.1.
            
            Transcript Variant: This variant (2) lacks an exon in the coding
            region, which results in a frameshift and an early stop codon,
            compared to variant 1. The encoded isoform (2) is shorter and has a
            distinct C-terminus, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK172838.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968540,
                                           SAMEA1970526 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..218
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..218
                     /product="transmembrane and immunoglobulin
                     domain-containing protein 1 isoform 2 precursor"
                     /note="transmembrane and immunoglobulin domain-containing
                     protein 1; AWKS9372"
                     /calculated_mol_wt=21002
     sig_peptide     1..28
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=3299
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXZ0.1)"
     Site            83
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXZ0.1)"
     Site            118
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXZ0.1)"
     Region          131..212
                     /region_name="IG_like"
                     /note="Immunoglobulin like; smart00410"
                     /db_xref="CDD:214653"
     Region          139..143
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          152..156
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            158
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXZ0.1)"
     Region          178..182
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Site            190
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q6UXZ0.1)"
     Region          192..197
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     CDS             1..218
                     /gene="TMIGD1"
                     /gene_synonym="TMIGD; UNQ9372"
                     /coded_by="NM_001319942.2:84..740"
                     /note="isoform 2 precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS82099.1"
                     /db_xref="GeneID:388364"
                     /db_xref="HGNC:HGNC:32431"
                     /db_xref="MIM:621206"
ORIGIN      
        1 mawkssvimq mgrflllvil flpremtssv ltvngkteny ildttpgsqa slicavqnht
       61 reeellwyre egrvdlksgn kinsssvcvs sisendngis ftcrlgrdqs vsvsvvlnvt
      121 fppllsgndf qtveegsnvk lvcnvkanpq aqmmwyknss lldleksrhq iqqtsesfql
      181 sitkvekpdn gtysciakss lktesldfhl ivkalheg
//
LOCUS       NP_001353796            1103 aa            linear   PRI 20-NOV-2025
DEFINITION  voltage-dependent calcium channel subunit alpha-2/delta-1 isoform 3
            preproprotein [Homo sapiens].
ACCESSION   NP_001353796 XP_005250627
VERSION     NP_001353796.1
DBSOURCE    REFSEQ: accession NM_001366867.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Inoue,H., Shiozaki,A., Kosuga,T., Shimizu,H., Kudou,M., Arita,T.,
            Konishi,H., Komatsu,S., Kuriu,Y., Kubota,T., Fujiwara,H.,
            Morinaga,Y., Konishi,E. and Otsuji,E.
  TITLE     CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer
  JOURNAL   J Gastroenterol 59 (7), 556-571 (2024)
   PUBMED   38536483
  REMARK    GeneRIF: CACNA2D1 regulates the progression and influences the
            microenvironment of colon cancer.
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Chen,Z., Mondal,A., Abderemane-Ali,F., Jang,S., Niranjan,S.,
            Montano,J.L., Zaro,B.W. and Minor,D.L. Jr.
  TITLE     EMC chaperone-CaV structure reveals an ion channel assembly
            intermediate
  JOURNAL   Nature 619 (7969), 410-419 (2023)
   PUBMED   37196677
  REMARK    GeneRIF: EMC chaperone-CaV structure reveals an ion channel
            assembly intermediate.
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Dahimene,S., von Elsner,L., Holling,T., Mattas,L.S., Pickard,J.,
            Lessel,D., Pilch,K.S., Kadurin,I., Pratt,W.S., Zhulin,I.B., Dai,H.,
            Hempel,M., Ruzhnikov,M.R.Z., Kutsche,K. and Dolphin,A.C.
  TITLE     Biallelic CACNA2D1 loss-of-function variants cause early-onset
            developmental epileptic encephalopathy
  JOURNAL   Brain 145 (8), 2721-2729 (2022)
   PUBMED   35293990
  REMARK    GeneRIF: Biallelic CACNA2D1 loss-of-function variants cause
            early-onset developmental epileptic encephalopathy.
REFERENCE   4  (residues 1 to 1103)
  AUTHORS   Schleithoff,L., Mehrke,G., Reutlinger,B. and Lehmann-Horn,F.
  TITLE     Genomic structure and functional expression of a human
            alpha(2)/delta calcium channel subunit gene (CACNA2)
  JOURNAL   Genomics 61 (2), 201-209 (1999)
   PUBMED   10534405
REFERENCE   5  (residues 1 to 1103)
  AUTHORS   Iles,D.E., Lehmann-Horn,F., Scherer,S.W., Tsui,L.C., Olde
            Weghuis,D., Suijkerbuijk,R.F., Heytens,L., Mikala,G., Schwartz,A.,
            Ellis,F.R. et al.
  TITLE     Localization of the gene encoding the alpha 2/delta-subunits of the
            L-type voltage-dependent calcium channel to chromosome 7q and
            analysis of the segregation of flanking markers in malignant
            hyperthermia susceptible families
  JOURNAL   Hum Mol Genet 3 (6), 969-975 (1994)
   PUBMED   7951247
REFERENCE   6  (residues 1 to 1103)
  AUTHORS   Powers,P.A., Scherer,S.W., Tsui,L.C., Gregg,R.G. and Hogan,K.
  TITLE     Localization of the gene encoding the alpha 2/delta subunit
            (CACNL2A) of the human skeletal muscle voltage-dependent Ca2+
            channel to chromosome 7q21-q22 by somatic cell hybrid analysis
  JOURNAL   Genomics 19 (1), 192-193 (1994)
   PUBMED   8188232
REFERENCE   7  (residues 1 to 1103)
  AUTHORS   Brust,P.F., Simerson,S., McCue,A.F., Deal,C.R., Schoonmaker,S.,
            Williams,M.E., Velicelebi,G., Johnson,E.C., Harpold,M.M. and
            Ellis,S.B.
  TITLE     Human neuronal voltage-dependent calcium channels: studies on
            subunit structure and role in channel assembly
  JOURNAL   Neuropharmacology 32 (11), 1089-1102 (1993)
   PUBMED   8107964
REFERENCE   8  (residues 1 to 1103)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   9  (residues 1 to 1103)
  AUTHORS   Williams,M.E., Feldman,D.H., McCue,A.F., Brenner,R., Velicelebi,G.,
            Ellis,S.B. and Harpold,M.M.
  TITLE     Structure and functional expression of alpha 1, alpha 2, and beta
            subunits of a novel human neuronal calcium channel subtype
  JOURNAL   Neuron 8 (1), 71-84 (1992)
   PUBMED   1309651
REFERENCE   10 (residues 1 to 1103)
  AUTHORS   Ellis,S.B., Williams,M.E., Ways,N.R., Brenner,R., Sharp,A.H.,
            Leung,A.T., Campbell,K.P., McKenna,E., Koch,W.J., Hui,A.,
            Schwartz,A. and Harpold,M.M.
  TITLE     Sequence and expression of mRNAs encoding the alpha 1 and alpha 2
            subunits of a DHP-sensitive calcium channel
  JOURNAL   Science 241 (4873), 1661-1664 (1988)
   PUBMED   2458626
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004970.2, AC004989.1,
            AC008283.3 and AC006145.2.
            
            On Oct 24, 2018 this sequence version replaced XP_005250627.1.
            
            Summary: The preproprotein encoded by this gene is cleaved into
            multiple chains that comprise the alpha-2 and delta subunits of the
            voltage-dependent calcium channel complex. Calcium channels mediate
            the influx of calcium ions into the cell upon membrane
            polarization. Mutations in this gene can cause cardiac
            deficiencies, including Brugada syndrome and short QT syndrome.
            Alternate splicing results in multiple transcript variants, some of
            which may lack the delta subunit portion. [provided by RefSeq, Nov
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments from orthologous transcript data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMEA1965299, SAMEA1966682
                              [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1103
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.11"
     Protein         1..1103
                     /product="voltage-dependent calcium channel subunit
                     alpha-2/delta-1 isoform 3 preproprotein"
                     /note="calcium channel, L type, alpha 2 polypeptide;
                     dihydropyridine-sensitive L-type, calcium channel
                     alpha-2/delta subunit; voltage-gated calcium channel
                     subunit alpha-2/delta-1; calcium channel,
                     voltage-dependent, alpha 2/delta subunit 1; alpha2delta-1"
                     /calculated_mol_wt=122137
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2450
     mat_peptide     25..1103
                     /product="Voltage-dependent calcium channel subunit
                     alpha-2/delta-1. /id=PRO_0000304633"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
                     /calculated_mol_wt=122137
     mat_peptide     25..956
                     /product="Voltage-dependent calcium channel subunit
                     alpha-2-1. /evidence=ECO:0000250. /id=PRO_0000005001"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
                     /calculated_mol_wt=105689
     Site            92
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          104..223
                     /region_name="VWA_N"
                     /note="VWA N-terminal; pfam08399"
                     /db_xref="CDD:462464"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P54290; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            136
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            184
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          239..417
                     /region_name="vWA_VGCC_like"
                     /note="VWA Voltage gated Calcium channel like:
                     Voltage-gated calcium channels are a complex of five
                     proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The
                     alpha 2 and delta subunits result from proteolytic
                     processing of a single gene product and carries at...;
                     cd01463"
                     /db_xref="CDD:238740"
     Site            order(259,261,263,331,363)
                     /site_type="other"
                     /note="metal ion-dependent adhesion site (MIDAS)"
                     /db_xref="CDD:238740"
     Region          259..263
                     /region_name="MIDAS-like motif"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
     Site            324
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            348
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          <435..>529
                     /region_name="dCache_1"
                     /note="Cache domain; pfam02743"
                     /db_xref="CDD:460673"
     Site            468
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Site            475
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            604
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            613
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Region          644..1072
                     /region_name="VGCC_alpha2"
                     /note="Neuronal voltage-dependent calcium channel alpha
                     2acd; pfam08473"
                     /db_xref="CDD:462488"
     Site            675
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            781
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     Site            824
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            888
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            895
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:34234349,
                     ECO:0007744|PDB:7MIX, ECO:0007744|PDB:7MIY; propagated
                     from UniProtKB/Swiss-Prot (P54289.3)"
     mat_peptide     957..1103
                     /product="Voltage-dependent calcium channel subunit
                     delta-1. /evidence=ECO:0000250. /id=PRO_0000005002"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
                     /calculated_mol_wt=16466
     Site            985
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            998
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P54289.3)"
     Site            1074..1094
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54289.3)"
     CDS             1..1103
                     /gene="CACNA2D1"
                     /gene_synonym="CACNA2; CACNL2A; CCHL2A; DEE110; LINC01112;
                     lncRNA-N3"
                     /coded_by="NM_001366867.1:498..3809"
                     /note="isoform 3 preproprotein is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS94135.1"
                     /db_xref="GeneID:781"
                     /db_xref="HGNC:HGNC:1399"
                     /db_xref="MIM:114204"
ORIGIN      
        1 maagcllalt ltlfqsllig psseepfpsa vtikswvdkm qedlvtlakt asgvnqlvdi
       61 yekyqdlytv epnnarqlve iaardiekll snrskalvrl aleaekvqaa hqwredfasn
      121 evvyynakdd ldpekndsep gsqrikpvfi edanfgrqis yqhaavhipt diyegstivl
      181 nelnwtsald evfkknreed psllwqvfgs atglaryypa spwvdnsrtp nkidlydvrr
      241 rpwyiqgaas pkdmlilvdv sgsvsgltlk lirtsvseml etlsdddfvn vasfnsnaqd
      301 vscfqhlvqa nvrnkkvlkd avnnitakgi tdykkgfsfa feqllnynvs rancnkiiml
      361 ftdggeeraq eifnkynkdk kvrvftfsvg qhnydrgpiq wmacenkgyy yeipsigair
      421 intqeyldvl grpmvlagdk akqvqwtnvy ldalelglvi tgtlpvfnit gqfenktnlk
      481 nqlilgvmgv dvsledikrl tprftlcpng yyfaidpngy vllhpnlqpk pigvgiptin
      541 lrkrrpniqn pksqepvtld fldaelendi kveirnkmid gesgektfrt lvksqderyi
      601 dkgnrtytwt pvngtdysla lvlptysfyy ikakleetit qarysetlkp dnfeesgytf
      661 iaprdycndl kisdnntefl lnfnefidrk tpnnpscnad linrvlldag ftnelvqnyw
      721 skqknikgvk arfvvtdggi trvypkeage nwqenpetye dsfykrsldn dnyvftapyf
      781 nksgpgayes gimvskavei yiqgkllkpa vvgikidvns wienftktsi rdpcagpvcd
      841 ckrnsdvmdc vilddggfll manhddytnq igrffgeidp slmrhlvnis vyafnksydy
      901 qsvcepgaap kqgaghrsay vpsvadilqi gwwataaaws ilqqfllslt fprlleavem
      961 edddftasls kqsciteqtq yffdndsksf sgvldcgncs rifhgeklmn tnlifimves
     1021 kgtcpcdtrl liqaeqtsdg pnpcdmvkqp ryrkgpdvcf dnnvledytd cggvsglnps
     1081 lwyiigiqfl llwlvsgsth rll
//
LOCUS       NP_001276091             874 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein regulatory complex subunit 7 isoform a [Homo sapiens].
ACCESSION   NP_001276091 XP_005256259
VERSION     NP_001276091.1
DBSOURCE    REFSEQ: accession NM_001289162.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Walton,T., Gui,M., Velkova,S., Fassad,M.R., Hirst,R.A., Haarman,E.,
            O'Callaghan,C., Bottier,M., Burgoyne,T., Mitchison,H.M. and
            Brown,A.
  TITLE     Axonemal structures reveal mechanoregulatory and disease mechanisms
  JOURNAL   Nature 618 (7965), 625-633 (2023)
   PUBMED   37258679
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 874)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Dowling,J.K., Becker,C.E., Bourke,N.M., Corr,S.C., Connolly,D.J.,
            Quinn,S.R., Pandolfi,P.P., Mansell,A. and O'Neill,L.A.J.
  TITLE     Promyelocytic leukemia protein interacts with the
            apoptosis-associated speck-like protein to limit inflammasome
            activation
  JOURNAL   J Biol Chem 289 (10), 6429-6437 (2014)
   PUBMED   24407287
REFERENCE   5  (residues 1 to 874)
  AUTHORS   Zhang,D. and Aravind,L.
  TITLE     Novel transglutaminase-like peptidase and C2 domains elucidate the
            structure, biogenesis and evolution of the ciliary compartment
  JOURNAL   Cell Cycle 11 (20), 3861-3875 (2012)
   PUBMED   22983010
REFERENCE   6  (residues 1 to 874)
  AUTHORS   Yang,Y., Cochran,D.A., Gargano,M.D., King,I., Samhat,N.K.,
            Burger,B.P., Sabourin,K.R., Hou,Y., Awata,J., Parry,D.A.,
            Marshall,W.F., Witman,G.B. and Lu,X.
  TITLE     Regulation of flagellar motility by the conserved flagellar protein
            CG34110/Ccdc135/FAP50
  JOURNAL   Mol Biol Cell 22 (7), 976-987 (2011)
   PUBMED   21289096
REFERENCE   7  (residues 1 to 874)
  AUTHORS   Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
            Wiemann,S.
  TITLE     Systematic subcellular localization of novel proteins identified by
            large-scale cDNA sequencing
  JOURNAL   EMBO Rep 1 (3), 287-292 (2000)
   PUBMED   11256614
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB093780.1, BC030661.1, AK292558.1, AK093035.1, BC036667.1 and
            AC018552.6.
            
            On Jan 16, 2014 this sequence version replaced XP_005256259.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Both variants 1 and
            2 encode the same isoform (a).
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC030661.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360716.8/ ENSP00000353942.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q21"
     Protein         1..874
                     /product="dynein regulatory complex subunit 7 isoform a"
                     /note="coiled-coil domain-containing protein 135;
                     coiled-coil domain-containing protein lobo homolog;
                     coiled-coil domain containing 135"
                     /calculated_mol_wt=103366
     Region          <173..>214
                     /region_name="Transglut_core"
                     /note="Transglutaminase-like superfamily; cl17362"
                     /db_xref="CDD:450180"
     Region          386..410
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IY82.3)"
     CDS             1..874
                     /gene="DRC7"
                     /gene_synonym="C16orf50; CCDC135; CFAP50; FAP50"
                     /coded_by="NM_001289162.2:216..2840"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10787.1"
                     /db_xref="GeneID:84229"
                     /db_xref="HGNC:HGNC:25289"
                     /db_xref="MIM:618769"
ORIGIN      
        1 mevlrekvee eeeaereeaa ewaewarmek mmrpvevrke eitlkqetlr dlekklseiq
       61 itvsaelpaf tkdtidiskl pisyktntpk eehllqvadn fsrqyshlcp drvplflhpl
      121 necevpkfvs ttlrptlmpy pelynwdsca qfvsdfltmv plpdplkpps hlyssttvlk
      181 yqkgncfdfs tllcsmligs gydaycvngy gsldlchmdl trevcpltvk pketikkeek
      241 vlpkkytikp prdlcsrfeq eqevkkqqei raqekkrlre eeerlmeaek akpdalhglr
      301 vhswvlvlsg krevpenffi dpftghsyst qdehflgies lwnhknywin mqdcwncckd
      361 lifdlgdpvr weymllgtdk sqlslteedd sgindeddve nlgkededks fdmphswveq
      421 ieispeafet rcpngkkviq ykraklekwa pylnsnglvs rlttyedlqc tnileikewy
      481 qnredmlelk hinkttdlkt dyfkpghpqa lrvhsyksmq pemdrviefy etarvdglmk
      541 reetprtmte yyqgrpdfls yrhasfgprv kkltlssaes nprpivkite rffrnpakpa
      601 eedvaervfl vaeeriqlry hcredhitas kreflrrtev dskgnkiimt pdmcisfeve
      661 pmehtkklly qyeammhlkr eeklsrhqvw eselevleil klreeeeaah tltisiydtk
      721 rnekskeyre amermmheeh lrqvetqldy lapflaqlpp gekltcwqav rlkdeclsdf
      781 kqrlinkanl iqarfeketq elqkkqqwyq enqvtltped edlylsycsq amfririleq
      841 rlnrhkelap lkylaleekl ykdprlgelq kifa
//
LOCUS       NP_001177951             399 aa            linear   PRI 20-NOV-2025
DEFINITION  transcriptional repressor CTCF isoform 2 [Homo sapiens].
ACCESSION   NP_001177951
VERSION     NP_001177951.1
DBSOURCE    REFSEQ: accession NM_001191022.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 399)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 399)
  AUTHORS   Ma,D.B., Zhang,H., Wang,X.L. and Wu,Q.G.
  TITLE     METTL3 aggravates cell damage induced by Streptococcus pneumoniae
            via the NEAT1/CTCF/MUC19 axis
  JOURNAL   Kaohsiung J Med Sci 40 (8), 722-731 (2024)
   PUBMED   38757482
  REMARK    GeneRIF: METTL3 aggravates cell damage induced by Streptococcus
            pneumoniae via the NEAT1/CTCF/MUC19 axis.
REFERENCE   3  (residues 1 to 399)
  AUTHORS   Zhang,J., Hu,G., Lu,Y., Ren,H., Huang,Y., Wen,Y., Ji,B., Wang,D.,
            Wang,H., Liu,H., Ma,N., Zhang,L., Pan,G., Qu,Y., Wang,H., Zhang,W.,
            Miao,Z. and Yao,H.
  TITLE     CTCF mutation at R567 causes developmental disorders via 3D genome
            rearrangement and abnormal neurodevelopment
  JOURNAL   Nat Commun 15 (1), 5524 (2024)
   PUBMED   38951485
  REMARK    GeneRIF: CTCF mutation at R567 causes developmental disorders via
            3D genome rearrangement and abnormal neurodevelopment.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 399)
  AUTHORS   Pandey,A., Kakani,P. and Shukla,S.
  TITLE     CTCF and BORIS-mediated autophagy regulation via alternative
            splicing of BNIP3L in breast cancer
  JOURNAL   J Biol Chem 300 (7), 107416 (2024)
   PUBMED   38810696
  REMARK    GeneRIF: CTCF and BORIS-mediated autophagy regulation via
            alternative splicing of BNIP3L in breast cancer.
REFERENCE   5  (residues 1 to 399)
  AUTHORS   He,T., You,M., Zhu,H., Chen,P. and Fang,S.
  TITLE     CCCTC-binding factor suppresses alpha-2-macroglobulin transcription
            to improve vascular endothelial cell functions in lower extremity
            arteriosclerosis obliterans
  JOURNAL   Gen Physiol Biophys 43 (3), 231-242 (2024)
   PUBMED   38774923
  REMARK    GeneRIF: CCCTC-binding factor suppresses alpha-2-macroglobulin
            transcription to improve vascular endothelial cell functions in
            lower extremity arteriosclerosis obliterans.
REFERENCE   6  (residues 1 to 399)
  AUTHORS   Bell,A.C., West,A.G. and Felsenfeld,G.
  TITLE     The protein CTCF is required for the enhancer blocking activity of
            vertebrate insulators
  JOURNAL   Cell 98 (3), 387-396 (1999)
   PUBMED   10458613
REFERENCE   7  (residues 1 to 399)
  AUTHORS   Filippova,G.N., Lindblom,A., Meincke,L.J., Klenova,E.M.,
            Neiman,P.E., Collins,S.J., Doggett,N.A. and Lobanenkov,V.V.
  TITLE     A widely expressed transcription factor with multiple DNA sequence
            specificity, CTCF, is localized at chromosome segment 16q22.1
            within one of the smallest regions of overlap for common deletions
            in breast and prostate cancers
  JOURNAL   Genes Chromosomes Cancer 22 (1), 26-36 (1998)
   PUBMED   9591631
REFERENCE   8  (residues 1 to 399)
  AUTHORS   Vostrov,A.A. and Quitschke,W.W.
  TITLE     The zinc finger protein CTCF binds to the APBbeta domain of the
            amyloid beta-protein precursor promoter. Evidence for a role in
            transcriptional activation
  JOURNAL   J Biol Chem 272 (52), 33353-33359 (1997)
   PUBMED   9407128
REFERENCE   9  (residues 1 to 399)
  AUTHORS   Filippova,G.N., Fagerlie,S., Klenova,E.M., Myers,C., Dehner,Y.,
            Goodwin,G., Neiman,P.E., Collins,S.J. and Lobanenkov,V.V.
  TITLE     An exceptionally conserved transcriptional repressor, CTCF, employs
            different combinations of zinc fingers to bind diverged promoter
            sequences of avian and mammalian c-myc oncogenes
  JOURNAL   Mol Cell Biol 16 (6), 2802-2813 (1996)
   PUBMED   8649389
REFERENCE   10 (residues 1 to 399)
  AUTHORS   Valverde de Morales,H.G., Wang,H.L., Garber,K., Corces,V. and Li,H.
  TITLE     CTCF-Related Disorder
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   38662876
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB229066.1, AB209793.1 and
            AA814313.1.
            
            Summary: This gene is a member of the BORIS + CTCF gene family and
            encodes a transcriptional regulator protein with 11 highly
            conserved zinc finger (ZF) domains. This nuclear protein is able to
            use different combinations of the ZF domains to bind different DNA
            target sequences and proteins. Depending upon the context of the
            site, the protein can bind a histone acetyltransferase
            (HAT)-containing complex and function as a transcriptional
            activator or bind a histone deacetylase (HDAC)-containing complex
            and function as a transcriptional repressor. If the protein is
            bound to a transcriptional insulator element, it can block
            communication between enhancers and upstream promoters, thereby
            regulating imprinted expression. Mutations in this gene have been
            associated with invasive breast cancers, prostate cancers, and
            Wilms' tumors. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Jul 2010].
            
            Transcript Variant: This variant (2) lacks internal two consecutive
            exons, resulting in a downstream AUG start codon, as compared to
            variant 1. The resulting isoform (2) has a shorter N-terminus, as
            compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB209793.1, SRR1803612.158608.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..399
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..399
                     /product="transcriptional repressor CTCF isoform 2"
                     /note="transcriptional repressor CTCF; CTCFL paralog;
                     11-zinc finger protein; 11 zinc finger transcriptional
                     repressor; CCCTC-binding factor (zinc finger protein)"
                     /calculated_mol_wt=45867
     Region          23..47
                     /region_name="zf-H2C2_5"
                     /note="C2H2-type zinc-finger domain; pfam13909"
                     /db_xref="CDD:404746"
     Region          25..45
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(30,32,34,36..37,40..41,44,58,60,64..65,68..69,72,86,
                     88,90,92..93,96..97)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          <38..172
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          53..73
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          81..98
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          111..129
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          141..161
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(146,148,150,152..153,156..157,160,174,176,180..181,
                     184..185,188,202,204,206,208..209,212..213)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          169..189
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          181..206
                     /region_name="zf-H2C2_2"
                     /note="Zinc-finger double domain; pfam13465"
                     /db_xref="CDD:463886"
     Region          197..213
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          229..245
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..399
                     /gene="CTCF"
                     /gene_synonym="CFAP108; FAP108; MRD21"
                     /coded_by="NM_001191022.2:349..1548"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54029.1"
                     /db_xref="GeneID:10664"
                     /db_xref="HGNC:HGNC:13723"
                     /db_xref="MIM:604167"
ORIGIN      
        1 mafvtsgelv rhrrykhthe kpfkcsmcdy asvevsklkr hirshtgerp fqcslcsyas
       61 rdtyklkrhm rthsgekpye cyicharftq sgtmkmhilq khtenvakfh cphcdtviar
      121 ksdlgvhlrk qhsyieqgkk crycdavfhe ryaliqhqks hknekrfkcd qcdyacrqer
      181 hmimhkrtht gekpyacshc dktfrqkqll dmhfkryhdp nfvpaafvcs kcgktftrrn
      241 tmarhadnca gpdgvegeng getkkskrgr krkmrskked ssdsenaepd lddnedeeep
      301 aveiepepep qpvtpapppa kkrrgrppgr tnqpkqnqpt aiiqvedqnt gaieniivev
      361 kkepdaepae geeeeaqpaa tdapngdltp emilsmmdr
//
LOCUS       NP_001339978             708 aa            linear   PRI 20-NOV-2025
DEFINITION  cell division cycle protein 27 homolog isoform 7 [Homo sapiens].
ACCESSION   NP_001339978 XP_016880976
VERSION     NP_001339978.1
DBSOURCE    REFSEQ: accession NM_001353049.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 708)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 708)
  AUTHORS   Song,W., Xia,X., Fan,Y., Zhang,B. and Chen,X.
  TITLE     Functional and Genetic Analyses Unveil the Implication of CDC27 in
            Hemifacial Microsomia
  JOURNAL   Int J Mol Sci 25 (9), 4707 (2024)
   PUBMED   38731925
  REMARK    GeneRIF: Functional and Genetic Analyses Unveil the Implication of
            CDC27 in Hemifacial Microsomia.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 708)
  AUTHORS   Zhao,C., Sun,J., Dang,Z., Su,Q. and Yang,J.
  TITLE     Circ_0000775 promotes the migration, invasion and EMT of hepatic
            carcinoma cells by recruiting IGF2BP2 to stabilize CDC27
  JOURNAL   Pathol Res Pract 235, 153908 (2022)
   PUBMED   35561648
  REMARK    GeneRIF: Circ_0000775 promotes the migration, invasion and EMT of
            hepatic carcinoma cells by recruiting IGF2BP2 to stabilize CDC27.
REFERENCE   4  (residues 1 to 708)
  AUTHORS   Shang,S., Zhou,Y., Chen,K., Chen,L., Li,P., Li,D., Cui,S.,
            Zhang,M.J., Chen,X. and Li,Q.
  TITLE     A Novel Gene CDC27 Causes SLE and Is Associated With the Disease
            Activity
  JOURNAL   Front Immunol 13, 876963 (2022)
   PUBMED   35418986
  REMARK    GeneRIF: A Novel Gene CDC27 Causes SLE and Is Associated With the
            Disease Activity.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 708)
  AUTHORS   Yu,H., Peters,J.M., King,R.W., Page,A.M., Hieter,P. and
            Kirschner,M.W.
  TITLE     Identification of a cullin homology region in a subunit of the
            anaphase-promoting complex
  JOURNAL   Science 279 (5354), 1219-1222 (1998)
   PUBMED   9469815
REFERENCE   6  (residues 1 to 708)
  AUTHORS   Ollendorff,V. and Donoghue,D.J.
  TITLE     The serine/threonine phosphatase PP5 interacts with CDC16 and
            CDC27, two tetratricopeptide repeat-containing subunits of the
            anaphase-promoting complex
  JOURNAL   J Biol Chem 272 (51), 32011-32018 (1997)
   PUBMED   9405394
REFERENCE   7  (residues 1 to 708)
  AUTHORS   Ho,P.P., Couch,F.J., Brody,L.C., Abel,K.J., Boehnke,M.,
            Shearon,T.H., Chandrasekharappa,S.C., Collins,F.S. and Weber,B.L.
  TITLE     Localization of the human homolog of the yeast cell division
            control 27 gene (CDC27) proximal to ITGB3 on human chromosome
            17q21.3
  JOURNAL   Somat Cell Mol Genet 21 (5), 351-355 (1995)
   PUBMED   8619132
REFERENCE   8  (residues 1 to 708)
  AUTHORS   Tugendreich,S., Tomkiel,J., Earnshaw,W. and Hieter,P.
  TITLE     CDC27Hs colocalizes with CDC16Hs to the centrosome and mitotic
            spindle and is essential for the metaphase to anaphase transition
  JOURNAL   Cell 81 (2), 261-268 (1995)
   PUBMED   7736578
REFERENCE   9  (residues 1 to 708)
  AUTHORS   Chen,P.L., Ueng,Y.C., Durfee,T., Chen,K.C., Yang-Feng,T. and
            Lee,W.H.
  TITLE     Identification of a human homologue of yeast nuc2 which interacts
            with the retinoblastoma protein in a specific manner
  JOURNAL   Cell Growth Differ 6 (2), 199-210 (1995)
   PUBMED   7756179
REFERENCE   10 (residues 1 to 708)
  AUTHORS   Tugendreich,S., Boguski,M.S., Seldin,M.S. and Hieter,P.
  TITLE     Linking yeast genetics to mammalian genomes: identification and
            mapping of the human homolog of CDC27 via the expressed sequence
            tag (EST) data base
  JOURNAL   Proc Natl Acad Sci U S A 90 (21), 10031-10035 (1993)
   PUBMED   8234252
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC002558.2.
            
            On Jun 28, 2017 this sequence version replaced XP_016880976.1.
            
            Summary: The protein encoded by this gene shares strong similarity
            with Saccharomyces cerevisiae protein Cdc27, and the gene product
            of Schizosaccharomyces pombe nuc 2. This protein is a component of
            the anaphase-promoting complex (APC), which is composed of eight
            protein subunits and is highly conserved in eukaryotic cells. This
            complex catalyzes the formation of cyclin B-ubiquitin conjugate,
            which is responsible for the ubiquitin-mediated proteolysis of
            B-type cyclins. The protein encoded by this gene and three other
            members of the APC complex contain tetratricopeptide (TPR) repeats,
            which are important for protein-protein interactions. This protein
            was shown to interact with mitotic checkpoint proteins including
            Mad2, p55CDC and BUBR1, and it may thus be involved in controlling
            the timing of mitosis. Alternative splicing of this gene results in
            multiple transcript variants. Related pseudogenes have been
            identified on chromosomes 2, 22 and Y. [provided by RefSeq, May
            2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.1658081.1,
                                           SRR18074968.1192594.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..708
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.32"
     Protein         1..708
                     /product="cell division cycle protein 27 homolog isoform
                     7"
                     /note="anaphase promoting complex subunit 3; nuc2 homolog;
                     anaphase-promoting complex, protein 3; cell division cycle
                     27 homolog; D0S1430E, D17S978E"
                     /calculated_mol_wt=78710
     Region          387..>610
                     /region_name="Spy"
                     /note="Predicted O-linked N-acetylglucosamine transferase,
                     SPINDLY family [Posttranslational modification, protein
                     turnover, chaperones]; COG3914"
                     /db_xref="CDD:443119"
     Region          440..466
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          500..>670
                     /region_name="TPR"
                     /note="Tetratricopeptide (TPR) repeat [General function
                     prediction only]; COG0457"
                     /db_xref="CDD:440225"
     Region          506..534
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Site            order(507,510..511,514..515,517,541,544..545,548..549,
                     551..552,575,578..579,582..583,586)
                     /site_type="other"
                     /note="putative protein binding surface [polypeptide
                     binding]"
                     /db_xref="CDD:276809"
     Region          539..569
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          574..602
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          608..635
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          642..670
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..708
                     /gene="CDC27"
                     /gene_synonym="ANAPC3; APC3; CDC27Hs; D0S1430E; D17S978E;
                     H-NUC; HNUC; NUC2"
                     /coded_by="NM_001353049.2:159..2285"
                     /note="isoform 7 is encoded by transcript variant 7"
                     /db_xref="GeneID:996"
                     /db_xref="HGNC:HGNC:1728"
                     /db_xref="MIM:116946"
ORIGIN      
        1 mastkplclp rcgfprrtpl crrlaegeqi lsggvfnkqk shddivtefg dsacftlsll
       61 ghvycktdrl akgsecyqks lslnpflwsp feslceigek pdpdqtfkft slqnfsnclp
      121 nscttqvpnh slshrqpetv ltetpqdtie lnrlnlessn skyslntdss vsyidsavis
      181 pdtvplgtgt silskqvqnk pktgrsllgg paalspltps fgilpletps pgdgsylqny
      241 tntppvidvp stgapskksv arigqtgtks vfsqsgnsre vtpilaqtqs sgpqtsttpq
      301 vlsptitspp nalprrssrl ftsdssttke nskklkmkfp pkipnrktks ktnkggitqp
      361 nindsleitk ldssiisegk istitpqiqa fnlqkaaaeg lmsllremgk gylalcsync
      421 keainilshl pshhyntgwv lcqigrayfe lseymqaeri fsevrrieny rvegmeiyst
      481 tlwhlqkdva lsvlskdltd mdknspeawc aagncfslqr ehdiaikffq raiqvdpnya
      541 yaytllghef vlteeldkal acfrnairvn prhynawygl gmiyykqekf slaemhfqka
      601 ldinpqssvl lchigvvqha lkksekaldt lnkaividpk nplckfhras vlfanekyks
      661 alqeleelkq ivpkeslvyf ligkilkepi trlkrqlisv ifqmmrsq
//
LOCUS       NP_001077082             240 aa            linear   PRI 20-NOV-2025
DEFINITION  insulin-like growth factor-binding protein 3 receptor isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_001077082
VERSION     NP_001077082.1
DBSOURCE    REFSEQ: accession NM_001083613.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 240)
  AUTHORS   Xu,W., Chao,R., Xie,X., Mao,Y., Chen,X., Chen,X. and Zhang,S.
  TITLE     IL13Ralpha2 as a crucial receptor for Chi3l1 in osteoclast
            differentiation and bone resorption through the MAPK/AKT pathway
  JOURNAL   Cell Commun Signal 22 (1), 81 (2024)
   PUBMED   38291404
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 240)
  AUTHORS   D'Addio,F., Assi,E., Maestroni,A., Rossi,G., Usuelli,V.,
            Petrazzuolo,A., Nardini,M., Loretelli,C., Ben Nasr,M. and
            Fiorina,P.
  TITLE     TMEM219 regulates the transcription factor expression and
            proliferation of beta cells
  JOURNAL   Front Endocrinol (Lausanne) 15, 1306127 (2024)
   PUBMED   38318298
  REMARK    GeneRIF: TMEM219 regulates the transcription factor expression and
            proliferation of beta cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 240)
  AUTHORS   Knudson,K.M., Hwang,S., McCann,M.S., Joshi,B.H., Husain,S.R. and
            Puri,R.K.
  TITLE     Recent Advances in IL-13Ralpha2-Directed Cancer Immunotherapy
  JOURNAL   Front Immunol 13, 878365 (2022)
   PUBMED   35464460
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 240)
  AUTHORS   D'Addio,F., Maestroni,A., Assi,E., Ben Nasr,M., Amabile,G.,
            Usuelli,V., Loretelli,C., Bertuzzi,F., Antonioli,B., Cardarelli,F.,
            El Essawy,B., Solini,A., Gerling,I.C., Bianchi,C., Becchi,G.,
            Mazzucchelli,S., Corradi,D., Fadini,G.P., Foschi,D., Markmann,J.F.,
            Orsi,E., Skrha,J. Jr., Camboni,M.G., Abdi,R., James Shapiro,A.M.,
            Folli,F., Ludvigsson,J., Del Prato,S., Zuccotti,G. and Fiorina,P.
  TITLE     The IGFBP3/TMEM219 pathway regulates beta cell homeostasis
  JOURNAL   Nat Commun 13 (1), 684 (2022)
   PUBMED   35115561
  REMARK    GeneRIF: The IGFBP3/TMEM219 pathway regulates beta cell
            homeostasis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 240)
  AUTHORS   Joyce,S. and Nour,A.M.
  TITLE     Blocking transmembrane219 protein signaling inhibits autophagy and
            restores normal cell death
  JOURNAL   PLoS One 14 (6), e0218091 (2019)
   PUBMED   31220095
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 240)
  CONSRTM   Schizophrenia Working Group of the Psychiatric Genomics Consortium
  TITLE     Biological insights from 108 schizophrenia-associated genetic loci
  JOURNAL   Nature 511 (7510), 421-427 (2014)
   PUBMED   25056061
REFERENCE   7  (residues 1 to 240)
  AUTHORS   He,C.H., Lee,C.G., Dela Cruz,C.S., Lee,C.M., Zhou,Y., Ahangari,F.,
            Ma,B., Herzog,E.L., Rosenberg,S.A., Li,Y., Nour,A.M., Parikh,C.R.,
            Schmidt,I., Modis,Y., Cantley,L. and Elias,J.A.
  TITLE     Chitinase 3-like 1 regulates cellular and tissue responses via
            IL-13 receptor alpha2
  JOURNAL   Cell Rep 4 (4), 830-841 (2013)
   PUBMED   23972995
  REMARK    Erratum:[Cell Rep. 2013 Nov 27;5(4):1156]
REFERENCE   8  (residues 1 to 240)
  AUTHORS   Baxter,R.C.
  TITLE     Insulin-like growth factor binding protein-3 (IGFBP-3): Novel
            ligands mediate unexpected functions
  JOURNAL   J Cell Commun Signal 7 (3), 179-189 (2013)
   PUBMED   23700234
REFERENCE   9  (residues 1 to 240)
  AUTHORS   Ingermann,A.R., Yang,Y.F., Han,J., Mikami,A., Garza,A.E.,
            Mohanraj,L., Fan,L., Idowu,M., Ware,J.L., Kim,H.S., Lee,D.Y. and
            Oh,Y.
  TITLE     Identification of a novel cell death receptor mediating
            IGFBP-3-induced anti-tumor effects in breast and prostate cancer
  JOURNAL   J Biol Chem 285 (39), 30233-30246 (2010)
   PUBMED   20353938
REFERENCE   10 (residues 1 to 240)
  AUTHORS   Wood,N., Whitters,M.J., Jacobson,B.A., Witek,J., Sypek,J.P.,
            Kasaian,M., Eppihimer,M.J., Unger,M., Tanaka,T., Goldman,S.J.,
            Collins,M., Donaldson,D.D. and Grusby,M.J.
  TITLE     Enhanced interleukin (IL)-13 responses in mice lacking IL-13
            receptor alpha 2
  JOURNAL   J Exp Med 197 (6), 703-709 (2003)
   PUBMED   12642602
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB506492.1 and BC050051.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.18695.1, HM005516.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000279396.11/ ENSP00000279396.6
            RefSeq Select criteria :: based on conservation, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..240
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..240
                     /product="insulin-like growth factor-binding protein 3
                     receptor isoform 1 precursor"
                     /note="insulin-like growth factor-binding protein 3
                     receptor; testicular tissue protein Li 203"
                     /calculated_mol_wt=21870
     sig_peptide     1..38
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
                     /calculated_mol_wt=3872
     mat_peptide     39..240
                     /product="Insulin-like growth factor-binding protein 3
                     receptor. /id=PRO_0000329049"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XT9.1)"
                     /calculated_mol_wt=21870
     Region          48..169
                     /region_name="TMEM219"
                     /note="Transmembrane 219; pfam14940"
                     /db_xref="CDD:464388"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            101
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            167
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q86XT9.1)"
     Site            205..225
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q86XT9.1)"
     CDS             1..240
                     /gene="TMEM219"
                     /gene_synonym="IGFBP-3R; IGFBP3R"
                     /coded_by="NM_001083613.2:92..814"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS42145.1"
                     /db_xref="GeneID:124446"
                     /db_xref="HGNC:HGNC:25201"
                     /db_xref="MIM:620290"
ORIGIN      
        1 mgncqaghnl hlclahhppl vcatlillll glsglglgsf llthrtglrs pdipqdwvsf
       61 lrsfgqltlc prngtvtgkw rgshvvgllt tlnfgdgpdr nktrtfqatv lgsqmglkgs
      121 sagqlvlita rvttertagt clyfsavpgi lpssqppisc seegagnatl sprmgeecvs
      181 vwsheglvlt klltseelal cgsrllvlgs flllfcgllc cvtamcfhpr reshwsrtrl
//
LOCUS       NP_001275926             528 aa            linear   PRI 20-NOV-2025
DEFINITION  protein lin-54 homolog isoform b [Homo sapiens].
ACCESSION   NP_001275926
VERSION     NP_001275926.1
DBSOURCE    REFSEQ: accession NM_001288997.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 528)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   2  (residues 1 to 528)
  AUTHORS   Marceau,A.H., Felthousen,J.G., Goetsch,P.D., Iness,A.N., Lee,H.W.,
            Tripathi,S.M., Strome,S., Litovchick,L. and Rubin,S.M.
  TITLE     Structural basis for LIN54 recognition of CHR elements in cell
            cycle-regulated promoters
  JOURNAL   Nat Commun 7, 12301 (2016)
   PUBMED   27465258
  REMARK    GeneRIF: the DNA-binding properties of LIN54 and the structural
            basis for recognition of a cell cycle genes homology region
            sequence, are described.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 528)
  AUTHORS   Sadasivam,S. and DeCaprio,J.A.
  TITLE     The DREAM complex: master coordinator of cell cycle-dependent gene
            expression
  JOURNAL   Nat Rev Cancer 13 (8), 585-595 (2013)
   PUBMED   23842645
  REMARK    Review article
            Erratum:[Nat Rev Cancer. 2013 Oct;13(10):752]
REFERENCE   4  (residues 1 to 528)
  AUTHORS   Matsuo,T., Kuramoto,H., Kumazaki,T., Mitsui,Y. and Takahashi,T.
  TITLE     LIN54 harboring a mutation in CHC domain is localized to the
            cytoplasm and inhibits cell cycle progression
  JOURNAL   Cell Cycle 11 (17), 3227-3236 (2012)
   PUBMED   22895175
  REMARK    GeneRIF: LIN54 harboring a mutation in CHC domain is localized to
            the cytoplasm and inhibits cell cycle progression.
REFERENCE   5  (residues 1 to 528)
  AUTHORS   Sadasivam,S., Duan,S. and DeCaprio,J.A.
  TITLE     The MuvB complex sequentially recruits B-Myb and FoxM1 to promote
            mitotic gene expression
  JOURNAL   Genes Dev 26 (5), 474-489 (2012)
   PUBMED   22391450
REFERENCE   6  (residues 1 to 528)
  AUTHORS   Litovchick,L., Florens,L.A., Swanson,S.K., Washburn,M.P. and
            DeCaprio,J.A.
  TITLE     DYRK1A protein kinase promotes quiescence and senescence through
            DREAM complex assembly
  JOURNAL   Genes Dev 25 (8), 801-813 (2011)
   PUBMED   21498570
REFERENCE   7  (residues 1 to 528)
  AUTHORS   Schmit,F., Cremer,S. and Gaubatz,S.
  TITLE     LIN54 is an essential core subunit of the DREAM/LINC complex that
            binds to the cdc2 promoter in a sequence-specific manner
  JOURNAL   FEBS J 276 (19), 5703-5716 (2009)
   PUBMED   19725879
  REMARK    GeneRIF: the cysteine-rich CXC domain of LIN54 is a novel
            DNA-binding domain that binds to the cdc2 promoter in a
            sequence-specific manner
REFERENCE   8  (residues 1 to 528)
  AUTHORS   Litovchick,L., Sadasivam,S., Florens,L., Zhu,X., Swanson,S.K.,
            Velmurugan,S., Chen,R., Washburn,M.P., Liu,X.S. and DeCaprio,J.A.
  TITLE     Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein
            complex represses human cell cycle-dependent genes in quiescence
  JOURNAL   Mol Cell 26 (4), 539-551 (2007)
   PUBMED   17531812
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DC335927.1, BX640657.1, BX537919.1, AB111889.1, BX640966.1,
            AC021105.13, BX108765.1, AI208524.1 and CK819664.1.
            
            Summary: LIN54 is a component of the LIN, or DREAM, complex, an
            essential regulator of cell cycle genes (Schmit et al., 2009
            [PubMed 19725879]).[supplied by OMIM, Dec 2010].
            
            Transcript Variant: This variant (7) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1.
            Variants 2, 3 and 7 encode the same isoform (b) which is shorter
            than isoform a.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BX640657.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..528
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21.22"
     Protein         1..528
                     /product="protein lin-54 homolog isoform b"
                     /note="protein lin-54 homolog; CXC domain-containing
                     protein 1"
                     /calculated_mol_wt=56153
     Region          <26..>245
                     /region_name="SP1-4_N"
                     /note="N-terminal domain of transcription factor
                     Specificity Proteins (SP) 1-4; cl41773"
                     /db_xref="CDD:425404"
     Region          301..>324
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     Region          375..410
                     /region_name="TCR"
                     /note="Tesmin/TSO1-like CXC domain, cysteine-rich domain;
                     pfam03638"
                     /db_xref="CDD:461001"
     CDS             1..528
                     /gene="LIN54"
                     /gene_synonym="CXCDC1; JC8.6; MIP120; TCX1"
                     /coded_by="NM_001288997.1:121..1707"
                     /note="isoform b is encoded by transcript variant 7"
                     /db_xref="CCDS:CCDS47089.1"
                     /db_xref="GeneID:132660"
                     /db_xref="HGNC:HGNC:25397"
                     /db_xref="MIM:613367"
ORIGIN      
        1 mevvpaeiak kprtptsgpv itklifakpi nskavtgqtt qvsppviagr vlsqstpgtp
       61 sktitisesg vigstlnstt qtpnkiaisp lkspnkavks tvqtitvggv stsqfktiip
      121 latapnvqqi qvpgskfhyv rlvtatsass stqpvsqnps tntqplqqak pvvvnttpvr
      181 msvpivsaqa vkqvvpkpin ptsqivttsq pqqrlimpat plpqiqpnlt nlppgtvlap
      241 apgtgnvgya vlpaqyvtql qqssyvsias nstftgtsgi qtqarlpfng iipsesasrp
      301 rkpcnctksl clklycdcfa ngefcnncnc tncynnlehe nerqkaikac ldrnpeafkp
      361 kigkgkeges drrhskgcnc krsgclknyc ecyeakimcs sickcigckn feesperktl
      421 mhladaaevr vqqqtaaktk lssqisdllt rptpalnsgg gklpftfvtk evaeatcncl
      481 laqaeqadkk gkskaaaerm ileefgrclm svinsagkak sdpcamnc
//
LOCUS       NP_002478                321 aa            linear   PRI 20-NOV-2025
DEFINITION  necdin [Homo sapiens].
ACCESSION   NP_002478
VERSION     NP_002478.1
DBSOURCE    REFSEQ: accession NM_002487.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Sanderson,M.R., Badior,K.E., Fahlman,R.P. and Wevrick,R.
  TITLE     The necdin interactome: evaluating the effects of amino acid
            substitutions and cell stress using proximity-dependent
            biotinylation (BioID) and mass spectrometry
  JOURNAL   Hum Genet 139 (12), 1513-1529 (2020)
   PUBMED   32529326
  REMARK    GeneRIF: The necdin interactome: evaluating the effects of amino
            acid substitutions and cell stress using proximity-dependent
            biotinylation (BioID) and mass spectrometry.
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Lau,J.C., Hanel,M.L. and Wevrick,R.
  TITLE     Tissue-specific and imprinted epigenetic modifications of the human
            NDN gene
  JOURNAL   Nucleic Acids Res 32 (11), 3376-3382 (2004)
   PUBMED   15247330
  REMARK    GeneRIF: Tissue-specific gene expression regulation and imprinted
            epigenetic modifications of the human NDN gene.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Nakada,Y., Taniura,H., Uetsuki,T., Inazawa,J. and Yoshikawa,K.
  TITLE     The human chromosomal gene for necdin, a neuronal growth
            suppressor, in the Prader-Willi syndrome deletion region
  JOURNAL   Gene 213 (1-2), 65-72 (1998)
   PUBMED   9630521
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Taniura,H., Taniguchi,N., Hara,M. and Yoshikawa,K.
  TITLE     Necdin, a postmitotic neuron-specific growth suppressor, interacts
            with viral transforming proteins and cellular transcription factor
            E2F1
  JOURNAL   J Biol Chem 273 (2), 720-728 (1998)
   PUBMED   9422723
REFERENCE   8  (residues 1 to 321)
  AUTHORS   Jay,P., Rougeulle,C., Massacrier,A., Moncla,A., Mattei,M.G.,
            Malzac,P., Roeckel,N., Taviaux,S., Lefranc,J.L., Cau,P., Berta,P.,
            Lalande,M. and Muscatelli,F.
  TITLE     The human necdin gene, NDN, is maternally imprinted and located in
            the Prader-Willi syndrome chromosomal region
  JOURNAL   Nat Genet 17 (3), 357-361 (1997)
   PUBMED   9354807
REFERENCE   9  (residues 1 to 321)
  AUTHORS   MacDonald,H.R. and Wevrick,R.
  TITLE     The necdin gene is deleted in Prader-Willi syndrome and is
            imprinted in human and mouse
  JOURNAL   Hum Mol Genet 6 (11), 1873-1878 (1997)
   PUBMED   9302265
  REMARK    GeneRIF: The necdin gene is imprinted, with preferential expression
            from the paternal allele in human and mouse.
REFERENCE   10 (residues 1 to 321)
  AUTHORS   Aizawa,T., Maruyama,K., Kondo,H. and Yoshikawa,K.
  TITLE     Expression of necdin, an embryonal carcinoma-derived nuclear
            protein, in developing mouse brain
  JOURNAL   Brain Res Dev Brain Res 68 (2), 265-274 (1992)
   PUBMED   1394972
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC124309.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This intronless gene is located in the Prader-Willi
            syndrome deletion region. It is an imprinted gene and is expressed
            exclusively from the paternal allele. Studies in mouse suggest that
            the protein encoded by this gene may suppress growth in postmitotic
            neurons. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: SRR3476690.434425.1, DRR138527.509882.1
                                        [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            imprinted gene         :: PMID: 9302265
            MANE Ensembl match     :: ENST00000649030.2/ ENSP00000497916.1
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q11.2"
     Protein         1..321
                     /product="necdin"
                     /note="necdin homolog; Prader-Willi syndrome chromosome
                     region; necdin, melanoma antigen (MAGE) family member;
                     necdin-like protein"
                     /calculated_mol_wt=35955
     Region          1..96
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99608.1)"
     Region          105..273
                     /region_name="MAGE"
                     /note="MAGE homology domain; pfam01454"
                     /db_xref="CDD:426270"
     CDS             1..321
                     /gene="NDN"
                     /gene_synonym="HsT16328; PWCR"
                     /coded_by="NM_002487.3:89..1054"
                     /db_xref="CCDS:CCDS10014.1"
                     /db_xref="GeneID:4692"
                     /db_xref="HGNC:HGNC:7675"
                     /db_xref="MIM:602117"
ORIGIN      
        1 mseqskdlsd pnfaaeapns evhsspgvse gvppsatlae pqspplgpta apqaapppqa
       61 pndegdpkal qqaaeegrah qapsaaqpgp appapaqlvq kahelmwyvl vkdqkkmiiw
      121 fpdmvkdvig sykkwcrsil rrtslilarv fglhlrltsl htmefalvka lepeeldrva
      181 lsnrmpmtgl llmilsliyv kgrgaresav wnvlrilglr pwkkhstfgd vrkliteefv
      241 qmnylkyqrv pyveppeyef fwgsrasrei tkmqimefla rvfkkdpqaw psryrealee
      301 aralreanpt ahyprssvse d
//
LOCUS       NP_001243895             302 aa            linear   PRI 20-NOV-2025
DEFINITION  mitochondrial potassium channel isoform 2 [Homo sapiens].
ACCESSION   NP_001243895
VERSION     NP_001243895.1
DBSOURCE    REFSEQ: accession NM_001256966.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 302)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 302)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 302)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 302)
  AUTHORS   Paggio,A., Checchetto,V., Campo,A., Menabo,R., Di Marco,G., Di
            Lisa,F., Szabo,I., Rizzuto,R. and De Stefani,D.
  TITLE     Identification of an ATP-sensitive potassium channel in
            mitochondria
  JOURNAL   Nature 572 (7771), 609-613 (2019)
   PUBMED   31435016
REFERENCE   5  (residues 1 to 302)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 302)
  AUTHORS   Wang,C. and Brennan,W.A. Jr.
  TITLE     Rat skeletal muscle, liver and brain have different fetal and adult
            forms of the glucose transporter
  JOURNAL   Biochim Biophys Acta 946 (1), 11-18 (1988)
   PUBMED   3145016
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BP307614.1, AL533758.3, BQ050243.1, AC134772.2 and BC011993.1.
            
            Transcript Variant: This variant (4) uses an alternate splice site
            in the 5' region and initiates translation at a downstream,
            in-frame start codon, compared to variant 1. Variants 3, 4, 5, 6
            and 7 encode the same isoform (2), which has a shorter N-terminus
            compared to isoform 1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.240374.1,
                                           SRR1163658.117819.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..302
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..302
                     /product="mitochondrial potassium channel isoform 2"
                     /note="coiled-coil domain-containing protein 51;
                     mitochondrial potassium channel"
                     /calculated_mol_wt=33526
     CDS             1..302
                     /gene="CCDC51"
                     /gene_synonym="MITOK"
                     /coded_by="NM_001256966.3:347..1255"
                     /note="isoform 2 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58830.1"
                     /db_xref="GeneID:79714"
                     /db_xref="HGNC:HGNC:25714"
                     /db_xref="MIM:618585"
ORIGIN      
        1 mvarglvrea redlevhqak lkevrdrldr vsredsqyle latlehrmlq eekrlrtayl
       61 raedserekf slfsaavres hekertraer tknwsligsv lgaligvags tyvnrvrlqe
      121 lkallleaqk gpvslqeair eqassysrqq rdlhnlmvdl rglvhaagpg qdsgsqagsp
      181 ptrdrdvdvl saalkeqlsh srqvhscleg lreqldglek tcsqmagvvq lvksaahpgl
      241 vepadgamps flleqgsmil alsdteqrle aqvnrntiys tlvtcvtfva tlpvlymlfk
      301 as
//
LOCUS       NP_001099043             286 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/SPRY domain-containing protein 1 [Homo sapiens].
ACCESSION   NP_001099043 XP_936650 XP_951273
VERSION     NP_001099043.1
DBSOURCE    REFSEQ: accession NM_001105573.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Lin,X., Tao,T., He,X., Mao,L., Pan,L. and Chen,L.
  TITLE     LncRNA MEG8 ameliorates Parkinson's disease neuro-inflammation
            through miR-485-3p/FBXO45 axis
  JOURNAL   Acta Neurol Belg 124 (2), 549-557 (2024)
   PUBMED   37814093
  REMARK    GeneRIF: LncRNA MEG8 ameliorates Parkinson's disease
            neuro-inflammation through miR-485-3p/FBXO45 axis.
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Zhang,F., Wang,Y., He,Y. and Dong,B.
  TITLE     Correlation of FBXO45 Expression Levels with Cancer Severity by
            ZEB1 Ubiquitin in Non-Small-Cell Lung Cancer
  JOURNAL   J Environ Pathol Toxicol Oncol 43 (4), 13-23 (2024)
   PUBMED   39016138
  REMARK    GeneRIF: Correlation of FBXO45 Expression Levels with Cancer
            Severity by ZEB1 Ubiquitin in Non-Small-Cell Lung Cancer.
REFERENCE   3  (residues 1 to 286)
  AUTHORS   Virdee,S.
  TITLE     An atypical ubiquitin ligase at the heart of neural development and
            programmed axon degeneration
  JOURNAL   Neural Regen Res 17 (11), 2347-2350 (2022)
   PUBMED   35535869
  REMARK    Review article
REFERENCE   4  (residues 1 to 286)
  AUTHORS   Wang,Q., Xu,C., Cai,R., An,W., Yuan,H. and Xu,M.
  TITLE     Fbxo45-mediated NP-STEP46 degradation via K6-linked ubiquitination
            sustains ERK activity in lung cancer
  JOURNAL   Mol Oncol 16 (16), 3017-3033 (2022)
   PUBMED   35838331
  REMARK    GeneRIF: Fbxo45-mediated NP-STEP46 degradation via K6-linked
            ubiquitination sustains ERK activity in lung cancer.
REFERENCE   5  (residues 1 to 286)
  AUTHORS   Wu,L., Yu,K., Chen,K., Zhu,X., Yang,Z., Wang,Q., Gao,J., Wang,Y.,
            Cao,T., Xu,H., Pan,X., Wang,L., Xia,J., Li,Y., Wang,Z.P. and Ma,J.
  TITLE     Fbxo45 facilitates pancreatic carcinoma progression by targeting
            USP49 for ubiquitination and degradation
  JOURNAL   Cell Death Dis 13 (3), 231 (2022)
   PUBMED   35279684
  REMARK    GeneRIF: Fbxo45 facilitates pancreatic carcinoma progression by
            targeting USP49 for ubiquitination and degradation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 286)
  AUTHORS   Chen,X., Sahasrabuddhe,A.A., Szankasi,P., Chung,F., Basrur,V.,
            Rangnekar,V.M., Pagano,M., Lim,M.S. and Elenitoba-Johnson,K.S.
  TITLE     Fbxo45-mediated degradation of the tumor-suppressor Par-4 regulates
            cancer cell survival
  JOURNAL   Cell Death Differ 21 (10), 1535-1545 (2014)
   PUBMED   24992930
  REMARK    GeneRIF: Fbxo45 is the substrate-receptor subunit of a functional
            E3 ligase for Par-4 that has a critical role in cancer cell
            survival.
REFERENCE   7  (residues 1 to 286)
  AUTHORS   Wang,C., Koide,T., Kimura,H., Kunimoto,S., Yoshimi,A., Nakamura,Y.,
            Kushima,I., Banno,M., Kawano,N., Takasaki,Y., Xing,J., Noda,Y.,
            Mouri,A., Aleksic,B., Ikeda,M., Okada,T., Iidaka,T., Inada,T.,
            Iwata,N. and Ozaki,N.
  TITLE     Novel rare variants in F-box protein 45 (FBXO45) in schizophrenia
  JOURNAL   Schizophr Res 157 (1-3), 149-156 (2014)
   PUBMED   24878430
  REMARK    GeneRIF: Study found that the R108C mutation in FBXO45 is a rare
            variant with a modest effect on schizophrenia risk that may disrupt
            the structure and function of the FBXO45 protein
REFERENCE   8  (residues 1 to 286)
  AUTHORS   Peschiaroli,A., Scialpi,F., Bernassola,F., Pagano,M. and Melino,G.
  TITLE     The F-box protein FBXO45 promotes the proteasome-dependent
            degradation of p73
  JOURNAL   Oncogene 28 (35), 3157-3166 (2009)
   PUBMED   19581926
  REMARK    GeneRIF: FBXO45 promotes the proteasome-dependent degradation of
            p73.
REFERENCE   9  (residues 1 to 286)
  AUTHORS   Yoshida,K.
  TITLE     Characterization of estrogen-induced F-box protein FBXO45
  JOURNAL   Oncol Rep 14 (2), 531-535 (2005)
   PUBMED   16012741
  REMARK    GeneRIF: FBXO45 gene consisting of 3 exons, and the vicinity of the
            transcriptional start site had several estrogen receptor binding
            consensus sequences.
REFERENCE   10 (residues 1 to 286)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC092933.21, DB636510.1, BE778263.1, CA445163.1 and BE047625.1.
            
            On or before Sep 30, 2007 this sequence version replaced
            XP_936650.2, XP_951273.2.
            
            Summary: Members of the F-box protein family, such as FBXO45, are
            characterized by an approximately 40-amino acid F-box motif. SCF
            complexes, formed by SKP1 (MIM 601434), cullin (see CUL1; MIM
            603134), and F-box proteins, act as protein-ubiquitin ligases.
            F-box proteins interact with SKP1 through the F box, and they
            interact with ubiquitination targets through other protein
            interaction domains (summary by Jin et al., 2004 [PubMed
            15520277]).[supplied by OMIM, Jan 2011].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.155239.1,
                                           SRR1163657.577130.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311630.7/ ENSP00000310332.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q29"
     Protein         1..286
                     /product="F-box/SPRY domain-containing protein 1"
                     /note="hFbxo45; F-box only protein 45"
                     /calculated_mol_wt=30502
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (P0C2W1.1)"
     Region          38..71
                     /region_name="F-box_FBXO45"
                     /note="F-box domain found in F-box only protein 45
                     (FBXO45) and similar proteins; cd22111"
                     /db_xref="CDD:438883"
     Site            order(39,43,46..47,50..51,55,57..58,62..64,66)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438883"
     Region          112..286
                     /region_name="SPRY_Fbox"
                     /note="SPRY domain in the F-box family Fbxo45; cd12907"
                     /db_xref="CDD:293964"
     CDS             1..286
                     /gene="FBXO45"
                     /gene_synonym="Fbx45"
                     /coded_by="NM_001105573.2:326..1186"
                     /db_xref="CCDS:CCDS46985.1"
                     /db_xref="GeneID:200933"
                     /db_xref="HGNC:HGNC:29148"
                     /db_xref="MIM:609112"
ORIGIN      
        1 maapapgaga asggagcsgg gagagagsgs gaagaggrlp srvlelvfsy lelselrsca
       61 lvckhwyrcl hgdensevwr slcarslaee alrtdilcnl psykakiraf qhafstndcs
      121 rnvyikkngf tlhrnpiaqs tdgartkigf segrhawevw wegplgtvav igiatkrapm
      181 qcqgyvallg sddqswgwnl vdnnllhnge vngsfpqcnn apkyqigeri rvildmedkt
      241 lafergyefl gvafrglpkv clypavsavy gntevtlvyl gkpldg
//
LOCUS       NP_001336342             625 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 24 isoform a [Homo sapiens].
ACCESSION   NP_001336342 XP_016862139
VERSION     NP_001336342.1
DBSOURCE    REFSEQ: accession NM_001349413.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 625)
  AUTHORS   Kosykh,A.V., Ryumina,I.I., Botkina,A.S., Evtushenko,N.A.,
            Zhigmitova,E.B., Martynova,A.A., Gurskaya,N.G. and Rebrikov,D.V.
  TITLE     EBS in Children with De Novo Pathogenic Variants Disturbing Krt14
  JOURNAL   Int J Mol Sci 25 (5), 2989 (2024)
   PUBMED   38474236
  REMARK    GeneRIF: EBS in Children with De Novo Pathogenic Variants
            Disturbing Krt14.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 625)
  AUTHORS   Vermeer,M.C.S.C., Al-Shinnag,M., Sillje,H.H.W., Gaytan,A.E.,
            Murrell,D.F., McGaughran,J., Melbourne,W., Cowan,T., van den
            Akker,P.C., van Spaendonck-Zwarts,K.Y., van der Meer,P. and
            Bolling,M.C.
  TITLE     A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation
  JOURNAL   Br J Dermatol 187 (6), 1045-1048 (2022)
   PUBMED   35975634
  REMARK    GeneRIF: A translation re-initiation variant in KLHL24 also causes
            epidermolysis bullosa simplex and dilated cardiomyopathy via
            intermediate filament degradation.
REFERENCE   3  (residues 1 to 625)
  AUTHORS   Vermeer,M.C.S.C., Sillje,H.H.W., Pas,H.H., Andrei,D., van der
            Meer,P. and Bolling,M.C.
  TITLE     Keratin 14 Degradation and Aging in Epidermolysis Bullosa Simplex
            due to KLHL24 Gain-of-Function Variants
  JOURNAL   J Invest Dermatol 142 (8), 2271-2274 (2022)
   PUBMED   35031308
  REMARK    GeneRIF: Keratin 14 Degradation and Aging in Epidermolysis Bullosa
            Simplex due to KLHL24 Gain-of-Function Variants.
REFERENCE   4  (residues 1 to 625)
  AUTHORS   Logli,E., Marzuolo,E., D'Agostino,M., Conti,L.A., Lena,A.M.,
            Diociaiuti,A., Dellambra,E., Has,C., Cianfanelli,V., Zambruno,G.,
            El Hachem,M., Magenta,A., Candi,E. and Condorelli,A.G.
  TITLE     Proteasome-mediated degradation of keratins 7, 8, 17 and 18 by
            mutant KLHL24 in a foetal keratinocyte model: Novel insight in
            congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy
  JOURNAL   Hum Mol Genet 31 (8), 1308-1324 (2022)
   PUBMED   34740256
  REMARK    GeneRIF: Proteasome-mediated degradation of keratins 7, 8, 17 and
            18 by mutant KLHL24 in a foetal keratinocyte model: Novel insight
            in congenital skin defects and fragility of epidermolysis bullosa
            simplex with cardiomyopathy.
REFERENCE   5  (residues 1 to 625)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   6  (residues 1 to 625)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 625)
  AUTHORS   Wu,W., Guo,Z., Zhang,X., Guo,L., Liu,L., Liao,Y., Wang,J., Wang,L.
            and Li,Q.
  TITLE     A microRNA encoded by HSV-1 inhibits a cellular transcriptional
            repressor of viral immediate early and early genes
  JOURNAL   Sci China Life Sci 56 (4), 373-383 (2013)
   PUBMED   23512275
  REMARK    GeneRIF: Data show that a miRNA, hsv1-mir-H27, encoded within the
            genome of herpes simplex virus 1 (HSV-1), targets the mRNA of the
            cellular transcriptional repressor Kelch-like 24 (KLHL24).
REFERENCE   8  (residues 1 to 625)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Craig,A.M. and Huettner,J.E.
  TITLE     The BTB/kelch protein, KRIP6, modulates the interaction of PICK1
            with GluR6 kainate receptors
  JOURNAL   Neuropharmacology 55 (7), 1131-1139 (2008)
   PUBMED   18692513
  REMARK    GeneRIF: KRIP6 regulates kainate receptors by inhibiting PICK1
            modulation via competition or a mutual blocking effect
REFERENCE   9  (residues 1 to 625)
  AUTHORS   Laezza,F., Wilding,T.J., Sequeira,S., Coussen,F., Zhang,X.Z.,
            Hill-Robinson,R., Mulle,C., Huettner,J.E. and Craig,A.M.
  TITLE     KRIP6: a novel BTB/kelch protein regulating function of kainate
            receptors
  JOURNAL   Mol Cell Neurosci 34 (4), 539-550 (2007)
   PUBMED   17254796
REFERENCE   10 (residues 1 to 625)
  AUTHORS   So,J.Y. and Teng,J.
  TITLE     Epidermolysis Bullosa Simplex
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301543
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068769.19.
            
            On Mar 15, 2017 this sequence version replaced XP_016862139.1.
            
            Summary: The protein encoded by this gene is a ubiquitin ligase
            substrate receptor and is regulated by autoubiquitination.
            Variations in the translation initiation codon of this gene have
            been found, which result in an N-terminally truncated but more
            stable protein due to loss of the autoubiquitination function. The
            more stable mutant protein causes an increased ubiquitin and
            degradation of keratin 14, which leads to skin fragility and the
            potentially life-threatening disease epidermolysis bullosa. The
            encoded protein is also involved in the regulation of kainate
            receptors. [provided by RefSeq, Mar 2017].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1-6 all encode the same isoform (a).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.18301.1,
                                           SRR1660803.31962.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..625
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q27.1"
     Protein         1..625
                     /product="kelch-like protein 24 isoform a"
                     /note="kainate receptor interacting protein for GluR6;
                     kelch-like protein 24; kelch-like 24"
                     /calculated_mol_wt=71055
     Region          48..168
                     /region_name="BTB_POZ_KLHL24_KRIP6"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 24 (KLHL24); cd18253"
                     /db_xref="CDD:349562"
     Region          62..591
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          354..393
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          397..466
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          469..514
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          517..556
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          559..604
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          570..616
                     /region_name="Kelch"
                     /note="Kelch domain; smart00612"
                     /db_xref="CDD:128874"
     CDS             1..625
                     /gene="KLHL24"
                     /gene_synonym="CMH29; DRE1; EBS6; EBSSH; KRIP6"
                     /coded_by="NM_001349413.1:296..2173"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="GeneID:54800"
                     /db_xref="HGNC:HGNC:25947"
                     /db_xref="MIM:611295"
ORIGIN      
        1 mvlilgrrln redlgvrdsp atkrkvfemd pksltgheff dfssgsshae nilqifnefr
       61 dsrlftdvii cvegkefpch ravlsacssy framfcndhr esremlvein gilaeamecf
      121 lqyvytgkvk ittenvqylf etsslfqisv lrdacakfle eqldpcnclg iqrfadthsl
      181 ktlftkcknf alqtfedvsq heefleldkd elidyicsde lvigkeemvf eavmrwvyra
      241 vdlrrpllhe llthvrlpll hpnyfvqtve vdqliqnspe cyqllhearr yhilgnemms
      301 prtrprrstg ysevivvvgg cervggfnlp ytecydpvtg ewkslaklpe ftkseyavca
      361 lrndilvsgg rinsrdvwiy nsqlniwirv aslnkgrwrh kmavllgkgf lktsilgqsw
      421 wltpvipalw eakvyvvggy dgqnrlssve cydsfsnrwt evaplkeavs spavtscvgk
      481 lfvigggpdd ntcsdkvqsy dpetnswllr aaipiakrci tavslnnliy vaggltkaiy
      541 cydpvedywm hvqntfsrqe ncgmsvcngk iyilggrren geatdtilcy dpatsiitgv
      601 aamprpvsyh gcvtihryne kcfkl
//
LOCUS       NP_758526                388 aa            linear   PRI 20-NOV-2025
DEFINITION  homeobox protein Meis2 isoform g [Homo sapiens].
ACCESSION   NP_758526
VERSION     NP_758526.1
DBSOURCE    REFSEQ: accession NM_172315.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 388)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 388)
  AUTHORS   Xiao,Y., Liu,Y., Sun,Y., Huang,C. and Zhong,S.
  TITLE     MEIS2 suppresses breast cancer development by downregulating IL10
  JOURNAL   Cancer Rep (Hoboken) 7 (5), e2064 (2024)
   PUBMED   38711262
  REMARK    GeneRIF: MEIS2 suppresses breast cancer development by
            downregulating IL10.
REFERENCE   3  (residues 1 to 388)
  AUTHORS   Li,D. and Hu,A.
  TITLE     LINC-PINT suppresses breast cancer cell proliferation and migration
            via MEIS2/PPP3CC/NF-kappaB pathway by sponging miR-576-5p
  JOURNAL   Am J Med Sci 367 (3), 201-211 (2024)
   PUBMED   37660994
  REMARK    GeneRIF: LINC-PINT suppresses breast cancer cell proliferation and
            migration via MEIS2/PPP3CC/NF-kappaB pathway by sponging
            miR-576-5p.
REFERENCE   4  (residues 1 to 388)
  AUTHORS   Arunachalam,V., Lea,R., Hoy,W., Lee,S., Mott,S., Savige,J.,
            Mathews,J.D., McMorran,B.J. and Nagaraj,S.H.
  TITLE     Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study
  JOURNAL   Genome Med 16 (1), 29 (2024)
   PUBMED   38347632
  REMARK    GeneRIF: Novel genetic markers for chronic kidney disease in a
            geographically isolated population of Indigenous Australians:
            Individual and multiple phenotype genome-wide association study.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 388)
  AUTHORS   Xu,H., Chen,S., Li,J., Weng,S., Ren,Y., Zhang,Y., Wang,L., Liu,L.,
            Guo,C., Xing,Z., Luo,P., Cheng,Q., Han,X. and Liu,Z.
  TITLE     Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a Key
            Factor for the Aggressive Progression and Prognosis in Stage II/III
            Colorectal Cancer
  JOURNAL   J Proteome Res 23 (2), 760-774 (2024)
   PUBMED   38153233
  REMARK    GeneRIF: Cellular Ligand-Receptor Perturbations Unravel MEIS2 as a
            Key Factor for the Aggressive Progression and Prognosis in Stage
            II/III Colorectal Cancer.
REFERENCE   6  (residues 1 to 388)
  AUTHORS   Fujino,T., Yamazaki,Y., Largaespada,D.A., Jenkins,N.A.,
            Copeland,N.G., Hirokawa,K. and Nakamura,T.
  TITLE     Inhibition of myeloid differentiation by Hoxa9, Hoxb8, and Meis
            homeobox genes
  JOURNAL   Exp Hematol 29 (7), 856-863 (2001)
   PUBMED   11438208
REFERENCE   7  (residues 1 to 388)
  AUTHORS   Liu,Y., MacDonald,R.J. and Swift,G.H.
  TITLE     DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b
            trimer and cooperation with a pancreas-specific basic
            helix-loop-helix complex
  JOURNAL   J Biol Chem 276 (21), 17985-17993 (2001)
   PUBMED   11279116
REFERENCE   8  (residues 1 to 388)
  AUTHORS   Yang,Y., Hwang,C.K., D'Souza,U.M., Lee,S.H., Junn,E. and
            Mouradian,M.M.
  TITLE     Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
            differentially regulate transcription
  JOURNAL   J Biol Chem 275 (27), 20734-20741 (2000)
   PUBMED   10764806
REFERENCE   9  (residues 1 to 388)
  AUTHORS   Smith,J.E., Afonja,O., Yee,H.T., Inghirami,G. and Takeshita,K.
  TITLE     Chromosomal mapping to 15q14 and expression analysis of the human
            MEIS2 homeobox gene
  JOURNAL   Mamm Genome 8 (12), 951-952 (1997)
   PUBMED   9383298
REFERENCE   10 (residues 1 to 388)
  AUTHORS   Steelman,S., Moskow,J.J., Muzynski,K., North,C., Druck,T.,
            Montgomery,J.C., Huebner,K., Daar,I.O. and Buchberg,A.M.
  TITLE     Identification of a conserved family of Meis1-related homeobox
            genes
  JOURNAL   Genome Res 7 (2), 142-156 (1997)
   PUBMED   9049632
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC078909.7, DA648763.1,
            AK056038.1, AK226072.1, BM679305.1 and AC018563.7.
            
            Summary: This gene encodes a homeobox protein belonging to the TALE
            ('three amino acid loop extension') family of
            homeodomain-containing proteins. TALE homeobox proteins are highly
            conserved transcription regulators, and several members have been
            shown to be essential contributors to developmental programs.
            Multiple transcript variants encoding distinct isoforms have been
            described for this gene. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (g) differs in the 5' UTR and
            coding sequence compared to variant a. The resulting isoform (g)
            has a shorter N-terminus when compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.106712.1,
                                           SRR1803615.262203.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..388
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q14"
     Protein         1..388
                     /product="homeobox protein Meis2 isoform g"
                     /note="Meis homolog 2; TALE homeobox protein Meis2;
                     Meis1-related gene 1; meis1-related protein 1; Meis1,
                     myeloid ecotropic viral integration site 1 homolog 2"
                     /calculated_mol_wt=42141
     Region          97..181
                     /region_name="Meis_PKNOX_N"
                     /note="N-terminal of Homeobox Meis and PKNOX1; pfam16493"
                     /db_xref="CDD:465140"
     Site            order(269,312,315..316,319)
                     /site_type="other"
                     /note="specific DNA base contacts [nucleotide binding]"
                     /db_xref="CDD:238039"
     Region          282..320
                     /region_name="Homeobox_KN"
                     /note="Homeobox KN domain; pfam05920"
                     /db_xref="CDD:428673"
     CDS             1..388
                     /gene="MEIS2"
                     /gene_synonym="CPCMR; HsT18361; MRG1"
                     /coded_by="NM_172315.3:525..1691"
                     /note="isoform g is encoded by transcript variant g"
                     /db_xref="CCDS:CCDS45219.1"
                     /db_xref="GeneID:4212"
                     /db_xref="HGNC:HGNC:7001"
                     /db_xref="MIM:601740"
ORIGIN      
        1 mdgvgvpasm ygdphaprpi ppvhhlnhgp plhatqhyga haphpnvmpa smgsavndal
       61 krdkdaiygh plfpllalvf ekcelatctp repgvaggdv cssdsfnedi avfakqvrae
      121 kplfssnpel dnlmiqaiqv lrfhllelek vhelcdnfch ryisclkgkm pidlviderd
      181 gssksdheel sgsstnladh npsswrdhdd atsthsagtp gpssgghasq sgdnsseqgd
      241 gldnsvaspg tgddddpdkd kkrqkkrgif pkvatnimra wlfqhlthpy pseeqkkqla
      301 qdtgltilqv nnwfinarrr ivqpmidqsn ragflldpsv sqgaayspeg qpmgsfvldg
      361 qqhmgirpag pmsgmgmnmg mdgqwhym
//
LOCUS       NP_071380                196 aa            linear   PRI 20-NOV-2025
DEFINITION  calcineurin B homologous protein 2 [Homo sapiens].
ACCESSION   NP_071380
VERSION     NP_071380.1
DBSOURCE    REFSEQ: accession NM_022097.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 196)
  AUTHORS   Dong,Y., Li,H., Ilie,A., Gao,Y., Boucher,A., Zhang,X.C.,
            Orlowski,J. and Zhao,Y.
  TITLE     Structural basis of autoinhibition of the human NHE3-CHP1 complex
  JOURNAL   Sci Adv 8 (21), eabn3925 (2022)
   PUBMED   35613257
REFERENCE   2  (residues 1 to 196)
  AUTHORS   Dong,Y., Gao,Y., Ilie,A., Kim,D., Boucher,A., Li,B., Zhang,X.C.,
            Orlowski,J. and Zhao,Y.
  TITLE     Structure and mechanism of the human NHE1-CHP1 complex
  JOURNAL   Nat Commun 12 (1), 3474 (2021)
   PUBMED   34108458
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 196)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 196)
  AUTHORS   Xu,L., Qin,Y., Sun,B., Wang,H., Gu,J., Tang,Z., Zhang,W. and
            Feng,J.
  TITLE     Involvement of CHP2 in the Development of Non-Small Cell Lung
            Cancer and Patients' Poor Prognosis
  JOURNAL   Appl Immunohistochem Mol Morphol 28 (9), 678-686 (2020)
   PUBMED   33030853
  REMARK    GeneRIF: Involvement of CHP2 in the Development of Non-Small Cell
            Lung Cancer and Patients' Poor Prognosis.
REFERENCE   5  (residues 1 to 196)
  AUTHORS   Cottle,W.T., Wallert,C.H., Anderson,K.K., Tran,M.F., Bakker,C.L.,
            Wallert,M.A. and Provost,J.J.
  TITLE     Calcineurin homologous protein isoform 2 supports tumor survival
            via the sodium hydrogen exchanger isoform 1 in non-small cell lung
            cancer
  JOURNAL   Tumour Biol 42 (7), 1010428320937863 (2020)
   PUBMED   32686600
  REMARK    GeneRIF: the data support the tumor-promoting potential of aberrant
            calcineurin B homologous protein 2 expression and position
            calcineurin B homologous protein 2 as a potential therapeutic
            target for the treatment of non-small cell lung cancer.
REFERENCE   6  (residues 1 to 196)
  AUTHORS   Inoue,H., Nakamura,Y., Nagita,M., Takai,T., Masuda,M., Nakamura,N.
            and Kanazawa,H.
  TITLE     Calcineurin homologous protein isoform 2 (CHP2), Na+/H+
            exchangers-binding protein, is expressed in intestinal epithelium
  JOURNAL   Biol Pharm Bull 26 (2), 148-155 (2003)
   PUBMED   12576672
REFERENCE   7  (residues 1 to 196)
  AUTHORS   Pang,T., Wakabayashi,S. and Shigekawa,M.
  TITLE     Expression of calcineurin B homologous protein 2 protects serum
            deprivation-induced cell death by serum-independent activation of
            Na+/H+ exchanger
  JOURNAL   J Biol Chem 277 (46), 43771-43777 (2002)
   PUBMED   12226101
REFERENCE   8  (residues 1 to 196)
  AUTHORS   Wang,Y., Han,K.J., Pang,X.W., Vaughan,H.A., Qu,W., Dong,X.Y.,
            Peng,J.R., Zhao,H.T., Rui,J.A., Leng,X.S., Cebon,J., Burgess,A.W.
            and Chen,W.F.
  TITLE     Large scale identification of human hepatocellular
            carcinoma-associated antigens by autoantibodies
  JOURNAL   J Immunol 169 (2), 1102-1109 (2002)
   PUBMED   12097419
REFERENCE   9  (residues 1 to 196)
  AUTHORS   Loftus,B.J., Kim,U.J., Sneddon,V.P., Kalush,F., Brandon,R.,
            Fuhrmann,J., Mason,T., Crosby,M.L., Barnstead,M., Cronin,L.,
            Deslattes Mays,A., Cao,Y., Xu,R.X., Kang,H.L., Mitchell,S.,
            Eichler,E.E., Harris,P.C., Venter,J.C. and Adams,M.D.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
   PUBMED   10493829
REFERENCE   10 (residues 1 to 196)
  AUTHORS   Lin,X. and Barber,D.L.
  TITLE     A calcineurin homologous protein inhibits GTPase-stimulated Na-H
            exchange
  JOURNAL   Proc Natl Acad Sci U S A 93 (22), 12631-12636 (1996)
   PUBMED   8901634
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF146019.1 and BF197519.1.
            
            Summary: This gene product is a small calcium-binding protein that
            regulates cell pH by controlling plasma membrane-type Na+/H+
            exchange activity. This protein shares sequence similarity with
            calcineurin B and can bind to and stimulate the protein phosphatase
            activity of calcineurin A (CnA) and functions in the
            calcineurin/NFAT (nuclear factor of activated T cells) signaling
            pathway. Another member of the CHP subfamily, Calcineurin B
            homologous protein 1, is located on Chromosome 15 and is an
            inhibitor of calcineurin activity and has a genetic phenotype
            associated with Parkinson's Disease (OMIM:606988). This gene was
            initially identified as a tumor-associated antigen and was
            previously referred to as Hepatocellular carcinoma-associated
            antigen 520. [provided by RefSeq, Jul 2013].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF146019.1, SRR1803612.214828.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300113.3/ ENSP00000300113.2
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..196
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.2"
     Protein         1..196
                     /product="calcineurin B homologous protein 2"
                     /note="hepatocellular carcinoma antigen gene 520;
                     hepatocellular carcinoma-associated antigen 520"
                     /calculated_mol_wt=22321
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q810D1; propagated from
                     UniProtKB/Swiss-Prot (O43745.3)"
     Region          30..184
                     /region_name="FRQ1"
                     /note="Ca2+-binding protein, EF-hand superfamily [Signal
                     transduction mechanisms]; COG5126"
                     /db_xref="CDD:444056"
     Region          137..148
                     /region_name="Nuclear export signal"
                     /note="propagated from UniProtKB/Swiss-Prot (O43745.3)"
     CDS             1..196
                     /gene="CHP2"
                     /coded_by="NM_022097.4:25..615"
                     /db_xref="CCDS:CCDS10617.1"
                     /db_xref="GeneID:63928"
                     /db_xref="HGNC:HGNC:24927"
ORIGIN      
        1 mgsrsshaav ipdgdsirre tgfsqasllr lhhrfraldr nkkgylsrmd lqqigalavn
       61 plgdriiesf fpdgsqrvdf pgfvrvlahf rpvededtet qdpkkpepln srrnklhyaf
      121 qlydldrdgk isrhemlqvl rlmvgvqvte eqleniadrt vqeadedgdg avsfveftks
      181 lekmdveqkm sirilk
//
LOCUS       NP_001254509             525 aa            linear   PRI 20-NOV-2025
DEFINITION  protein regulator of cytokinesis 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001254509
VERSION     NP_001254509.2
DBSOURCE    REFSEQ: accession NM_001267580.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Ciapponi,M., Karlukova,E., Schkolziger,S., Benda,C. and Muller,J.
  TITLE     Structural basis of the histone ubiquitination read-write mechanism
            of RYBP-PRC1
  JOURNAL   Nat Struct Mol Biol 31 (7), 1023-1027 (2024)
   PUBMED   38528151
  REMARK    GeneRIF: Structural basis of the histone ubiquitination read-write
            mechanism of RYBP-PRC1.
            Erratum:[Nat Struct Mol Biol. 2025 Sep;32(9):1840. doi:
            10.1038/s41594-025-01674-7. PMID: 40866579]
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Gluszek-Kustusz,A., Craske,B., Legal,T., McHugh,T. and Welburn,J.P.
  TITLE     Phosphorylation controls spatial and temporal activities of
            motor-PRC1 complexes to complete mitosis
  JOURNAL   EMBO J 42 (21), e113647 (2023)
   PUBMED   37592895
  REMARK    GeneRIF: Phosphorylation controls spatial and temporal activities
            of motor-PRC1 complexes to complete mitosis.
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Walia,G.K., Sharma,P., Agarwal,T., Lal,M., Negandhi,H.,
            Prabhakaran,D., Khadgawat,R., Sachdeva,M.P. and Gupta,V.
  TITLE     Genetic associations of TMEM154, PRC1 and ZFAND6 loci with type 2
            diabetes in an endogamous business community of North India
  JOURNAL   PLoS One 18 (9), e0291339 (2023)
   PUBMED   37738238
  REMARK    GeneRIF: Genetic associations of TMEM154, PRC1 and ZFAND6 loci with
            type 2 diabetes in an endogamous business community of North India.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Li,S., Motino,O., Lambertucci,F., Martins,I., Sun,L. and Kroemer,G.
  TITLE     Protein regulator of cytokinesis 1: a potential oncogenic driver
  JOURNAL   Mol Cancer 22 (1), 128 (2023)
   PUBMED   37563591
  REMARK    GeneRIF: Protein regulator of cytokinesis 1: a potential oncogenic
            driver.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Yi,M., Lv,S., He,Y., Wu,Y., Zhang,J. and Chen,Q.
  TITLE     CircKDM1B promotes hepatocellular carcinoma progression through
            regulating miR-1322/PRC1 axis
  JOURNAL   Environ Toxicol 38 (8), 2031-2040 (2023)
   PUBMED   37227723
  REMARK    GeneRIF: CircKDM1B promotes hepatocellular carcinoma progression
            through regulating miR-1322/PRC1 axis.
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Kurasawa,Y., Earnshaw,W.C., Mochizuki,Y., Dohmae,N. and Todokoro,K.
  TITLE     Essential roles of KIF4 and its binding partner PRC1 in organized
            central spindle midzone formation
  JOURNAL   EMBO J 23 (16), 3237-3248 (2004)
   PUBMED   15297875
  REMARK    GeneRIF: kinesin family member 4 and its binding partner PRC1 play
            essential roles in the organization of central spindles and midzone
            formation
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Ban,R., Irino,Y., Fukami,K. and Tanaka,H.
  TITLE     Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP
            activity toward Cdc42 during the metaphase
  JOURNAL   J Biol Chem 279 (16), 16394-16402 (2004)
   PUBMED   14744859
  REMARK    GeneRIF: contributes to the correct formation of the spindle during
            the metaphase
REFERENCE   8  (residues 1 to 525)
  AUTHORS   Li,C., Shridhar,K. and Liu,J.
  TITLE     Molecular characterization of oncostatin M-induced growth arrest of
            MCF-7 cells expressing a temperature-sensitive mutant of p53
  JOURNAL   Breast Cancer Res Treat 80 (1), 23-37 (2003)
   PUBMED   12889596
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Mollinari,C., Kleman,J.P., Jiang,W., Schoehn,G., Hunter,T. and
            Margolis,R.L.
  TITLE     PRC1 is a microtubule binding and bundling protein essential to
            maintain the mitotic spindle midzone
  JOURNAL   J Cell Biol 157 (7), 1175-1186 (2002)
   PUBMED   12082078
  REMARK    GeneRIF: PRC1 is a microtubule-associated protein required to
            maintain the spindle midzone, and that distinct functions are
            associated with modular elements of the primary sequence.
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Jiang,W., Jimenez,G., Wells,N.J., Hope,T.J., Wahl,G.M., Hunter,T.
            and Fukunaga,R.
  TITLE     PRC1: a human mitotic spindle-associated CDK substrate protein
            required for cytokinesis
  JOURNAL   Mol Cell 2 (6), 877-885 (1998)
   PUBMED   9885575
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC068831.17.
            
            On May 31, 2019 this sequence version replaced NP_001254509.1.
            
            Summary: This gene encodes a protein that is involved in
            cytokinesis. The protein is present at high levels during the S and
            G2/M phases of mitosis but its levels drop dramatically when the
            cell exits mitosis and enters the G1 phase. It is located in the
            nucleus during interphase, becomes associated with mitotic spindles
            in a highly dynamic manner during mitosis, and localizes to the
            cell mid-body during cytokinesis. This protein has been shown to be
            a substrate of several cyclin-dependent kinases (CDKs). It is
            necessary for polarizing parallel microtubules and concentrating
            the factors responsible for contractile ring assembly. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Jun 2012].
            
            Transcript Variant: This variant (4) lacks an alternate in-frame
            exon in the 5' coding region, and uses and alternate splice site
            and lacks an exon that results in a frameshift in the 3' coding
            region, compared to variant 1. The encoded isoform (4) has a
            distinct C-terminus and is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK297117.1, SRR18074969.2239383.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q26.1"
     Protein         1..525
                     /product="protein regulator of cytokinesis 1 isoform 4"
                     /note="protein regulating cytokinesis 1; anaphase spindle
                     elongation 1 homolog"
                     /calculated_mol_wt=61257
     Region          16..436
                     /region_name="MAP65_ASE1"
                     /note="Microtubule associated protein (MAP65/ASE1 family);
                     pfam03999"
                     /db_xref="CDD:427641"
     CDS             1..525
                     /gene="PRC1"
                     /gene_synonym="ASE1; MAP65"
                     /coded_by="NM_001267580.2:119..1696"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS45353.2"
                     /db_xref="GeneID:9055"
                     /db_xref="HGNC:HGNC:9341"
                     /db_xref="MIM:603484"
ORIGIN      
        1 mrrsevlaee sivclqkaln hlreiwelig ipedqrlqrt evvkkhikee gettilqlek
       61 dlrtqvelmr kqkkerkqel kllqeqdqel ceilcmphyd idsasvpsle elnqfrqhvt
      121 tlretkasrr eefvsikrqi ilcmealdht pdtsferdvv cededafcls leniatlqkl
      181 lrqlemqksq neavceglrt qirelwdrlq ipeeereava timsgskakv rkalqlevdr
      241 leelkmqnmk kvieairvel vqywdqcfys qeqrqafapf caedytesll qlhdaeivrl
      301 knyyevhkel fegvqkweet wrlfleferk asdpnrftnr ggnllkeekq raklqkmlpk
      361 leeelkarie lweqehskaf mvngqkfmey vaeqwemhrl ekerakqerq lknkkqtete
      421 mlygsaprtp skrrglapnt pgkarklntt tmsnatanss irpifggtvy hspvsrlpps
      481 gskpvaastc sgkktprtgr hgankenlel ngsilsartf kgfqi
//
LOCUS       NP_871617                147 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-conjugating enzyme E2 D3 isoform 1 [Homo sapiens].
ACCESSION   NP_871617
VERSION     NP_871617.1
DBSOURCE    REFSEQ: accession NM_181888.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Yalcin,Z., Koot,D., Bezstarosti,K., Salas-Lloret,D.,
            Bleijerveld,O.B., Boersma,V., Falcone,M., Gonzalez-Prieto,R.,
            Altelaar,M., Demmers,J.A.A. and Jacobs,J.J.L.
  TITLE     Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control
  JOURNAL   Mol Cell Proteomics 22 (6), 100548 (2023)
   PUBMED   37059365
  REMARK    GeneRIF: Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and
            Implicates UBE2D3 in Protein Quality Control.
REFERENCE   3  (residues 1 to 147)
  AUTHORS   Jiang,C., Dai,X., He,S., Zhou,H., Fang,L., Guo,J., Liu,S.,
            Zhang,T., Pan,W., Yu,H., Fu,T., Li,D., Inuzuka,H., Wang,P., Xiao,J.
            and Wei,W.
  TITLE     Ring domains are essential for GATOR2-dependent mTORC1 activation
  JOURNAL   Mol Cell 83 (1), 74-89 (2023)
   PUBMED   36528027
REFERENCE   4  (residues 1 to 147)
  AUTHORS   Ray,P., Nancarrow,D.J., Ferrer-Torres,D., Wang,Z., San Martinho,M.,
            Hinton,T., Wu,J.H., Wu,A., Turgeon,D.K., Hammer,M.A., Dame,M.K.,
            Lawrence,T.S., O'Brien,P.J., Spence,J.R., Beer,D.G. and Ray,D.
  TITLE     UBCH5 Family Members Differentially Impact Stabilization of Mutant
            p53 via RNF128 Iso1 During Barrett's Progression to Esophageal
            Adenocarcinoma
  JOURNAL   Cell Mol Gastroenterol Hepatol 13 (1), 129-149 (2022)
   PUBMED   34416429
  REMARK    GeneRIF: UBCH5 Family Members Differentially Impact Stabilization
            of Mutant p53 via RNF128 Iso1 During Barrett's Progression to
            Esophageal Adenocarcinoma.
REFERENCE   5  (residues 1 to 147)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 147)
  AUTHORS   Ohta,T., Michel,J.J., Schottelius,A.J. and Xiong,Y.
  TITLE     ROC1, a homolog of APC11, represents a family of cullin partners
            with an associated ubiquitin ligase activity
  JOURNAL   Mol Cell 3 (4), 535-541 (1999)
   PUBMED   10230407
REFERENCE   7  (residues 1 to 147)
  AUTHORS   Anan,T., Nagata,Y., Koga,H., Honda,Y., Yabuki,N., Miyamoto,C.,
            Kuwano,A., Matsuda,I., Endo,F., Saya,H. and Nakao,M.
  TITLE     Human ubiquitin-protein ligase Nedd4: expression, subcellular
            localization and selective interaction with ubiquitin-conjugating
            enzymes
  JOURNAL   Genes Cells 3 (11), 751-763 (1998)
   PUBMED   9990509
REFERENCE   8  (residues 1 to 147)
  AUTHORS   Rogakou,E.P., Pilch,D.R., Orr,A.H., Ivanova,V.S. and Bonner,W.M.
  TITLE     DNA double-stranded breaks induce histone H2AX phosphorylation on
            serine 139
  JOURNAL   J Biol Chem 273 (10), 5858-5868 (1998)
   PUBMED   9488723
REFERENCE   9  (residues 1 to 147)
  AUTHORS   Jensen,J.P., Bates,P.W., Yang,M., Vierstra,R.D. and Weissman,A.M.
  TITLE     Identification of a family of closely related human ubiquitin
            conjugating enzymes
  JOURNAL   J Biol Chem 270 (51), 30408-30414 (1995)
   PUBMED   8530467
REFERENCE   10 (residues 1 to 147)
  AUTHORS   Scheffner,M., Huibregtse,J.M. and Howley,P.M.
  TITLE     Identification of a human ubiquitin-conjugating enzyme that
            mediates the E6-AP-dependent ubiquitination of p53
  JOURNAL   Proc Natl Acad Sci U S A 91 (19), 8797-8801 (1994)
   PUBMED   8090726
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BM750658.1, DA335600.1,
            BC003395.1, AC018797.4 and BM967209.1.
            
            Summary: The modification of proteins with ubiquitin is an
            important cellular mechanism for targeting abnormal or short-lived
            proteins for degradation. Ubiquitination involves at least three
            classes of enzymes: ubiquitin-activating enzymes, or E1s,
            ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein
            ligases, or E3s. This gene encodes a member of the E2
            ubiquitin-conjugating enzyme family. This enzyme functions in the
            ubiquitination of the tumor-suppressor protein p53, which is
            induced by an E3 ubiquitin-protein ligase. [provided by RefSeq, Jan
            2017].
            
            Transcript Variant: This variant (4) lacks a segment in the 5' UTR,
            and encodes the same isoform (1), as compared to variant 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.414420.1, BQ428985.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2142680 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q24"
     Protein         1..147
                     /product="ubiquitin-conjugating enzyme E2 D3 isoform 1"
                     /EC_number="2.3.2.23"
                     /EC_number="2.3.2.24"
                     /note="ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog,
                     yeast); ubiquitin-conjugating enzyme E2-17 kDa 3;
                     ubiquitin-protein ligase D3; ubiquitin carrier protein D3;
                     ubiquitin-conjugating enzyme E2(17)KB 3; ubiquitin
                     conjugating enzyme E2D 3; E2 ubiquitin-conjugating enzyme
                     D3; (E3-independent) E2 ubiquitin-conjugating enzyme D3;
                     ubiquitin-conjugating enzyme E2D 3 (homologous to yeast
                     UBC4/5)"
                     /calculated_mol_wt=16556
     Region          3..145
                     /region_name="UBCc_UBE2D"
                     /note="Ubiquitin-conjugating enzyme E2, catalytic (UBCc)
                     domain of ubiquitin conjugating enzyme E2 D1-D3 and
                     related proteins; cd23792"
                     /db_xref="CDD:467412"
     CDS             1..147
                     /gene="UBE2D3"
                     /gene_synonym="E2(17)KB3; UBC4/5; UBCH5C"
                     /coded_by="NM_181888.3:343..786"
                     /note="isoform 1 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS3660.1"
                     /db_xref="GeneID:7323"
                     /db_xref="HGNC:HGNC:12476"
                     /db_xref="MIM:602963"
ORIGIN      
        1 malkrinkel sdlardppaq csagpvgddm fhwqatimgp ndspyqggvf fltihfptdy
       61 pfkppkvaft triyhpnins ngsicldilr sqwspaltis kvllsicsll cdpnpddplv
      121 peiariyktd rdkynrisre wtqkyam
//
LOCUS       NP_001305297             463 aa            linear   PRI 20-NOV-2025
DEFINITION  cyclin-dependent kinase 8 isoform 2 [Homo sapiens].
ACCESSION   NP_001305297 XP_005266272
VERSION     NP_001305297.1
DBSOURCE    REFSEQ: accession NM_001318368.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Comeau,D., Belliveau,J., Bouhamdani,N. and Amor,M.B.
  TITLE     Expanding the phenotypic spectrum for CDK8-related disease: A case
            report
  JOURNAL   Am J Med Genet A 194 (5), e63537 (2024)
   PUBMED   38193604
  REMARK    GeneRIF: Expanding the phenotypic spectrum for CDK8-related
            disease: A case report.
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Choi,H.Y., Zhu,Y., Zhao,X., Mehta,S., Hernandez,J.C., Lee,J.J.,
            Kou,Y., Machida,R., Giacca,M., Del Sal,G., Ray,R., Eoh,H.,
            Tahara,S.M., Chen,L., Tsukamoto,H. and Machida,K.
  TITLE     NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells
  JOURNAL   Exp Mol Med 56 (2), 461-477 (2024)
   PUBMED   38409448
  REMARK    GeneRIF: NOTCH localizes to mitochondria through the TBC1D15-FIS1
            interaction and is stabilized via blockade of E3 ligase and CDK8
            recruitment to reprogram tumor-initiating cells.
            Erratum:[Exp Mol Med. 2024 Oct;56(10):2323. doi:
            10.1038/s12276-024-01325-9. PMID: 39465353]
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Chen,M., Li,J., Zhang,L., Wang,L., Cheng,C., Ji,H., Altilia,S.,
            Ding,X., Cai,G., Altomare,D., Shtutman,M., Byrum,S.D.,
            Mackintosh,S.G., Feoktistov,A., Soshnikova,N., Mogila,V.A.,
            Tatarskiy,V., Erokhin,M., Chetverina,D., Prawira,A., Ni,Y.,
            Urban,S., McInnes,C., Broude,E.V. and Roninson,I.B.
  TITLE     CDK8 and CDK19: positive regulators of signal-induced transcription
            and negative regulators of Mediator complex proteins
  JOURNAL   Nucleic Acids Res 51 (14), 7288-7313 (2023)
   PUBMED   37378433
  REMARK    GeneRIF: CDK8 and CDK19: positive regulators of signal-induced
            transcription and negative regulators of Mediator complex proteins.
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Rzymski,T., Mikula,M., Wiklik,K. and Brzozka,K.
  TITLE     CDK8 kinase--An emerging target in targeted cancer therapy
  JOURNAL   Biochim Biophys Acta 1854 (10 Pt B), 1617-1629 (2015)
   PUBMED   26006748
  REMARK    GeneRIF: Current state of the art confirms that further development
            of CDK8 inhibitors will translate into targeted therapies in
            oncology
            Review article
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Nemet,J., Jelicic,B., Rubelj,I. and Sopta,M.
  TITLE     The two faces of Cdk8, a positive/negative regulator of
            transcription
  JOURNAL   Biochimie 97, 22-27 (2014)
   PUBMED   24139904
  REMARK    GeneRIF: CDK8 regulates the transcription factors turnover,
            C-terminal domain phosphorylation, and regulates the activator or
            repressor functions. (Review)
            Review article
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Cujec,T.P., Cho,H., Maldonado,E., Meyer,J., Reinberg,D. and
            Peterlin,B.M.
  TITLE     The human immunodeficiency virus transactivator Tat interacts with
            the RNA polymerase II holoenzyme
  JOURNAL   Mol Cell Biol 17 (4), 1817-1823 (1997)
   PUBMED   9121429
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Rickert,P., Seghezzi,W., Shanahan,F., Cho,H. and Lees,E.
  TITLE     Cyclin C/CDK8 is a novel CTD kinase associated with RNA polymerase
            II
  JOURNAL   Oncogene 12 (12), 2631-2640 (1996)
   PUBMED   8700522
REFERENCE   9  (residues 1 to 463)
  AUTHORS   Tassan,J.P., Jaquenoud,M., Leopold,P., Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of human cyclin-dependent kinase 8, a putative
            protein kinase partner for cyclin C
  JOURNAL   Proc Natl Acad Sci U S A 92 (19), 8871-8875 (1995)
   PUBMED   7568034
REFERENCE   10 (residues 1 to 463)
  AUTHORS   Schultz,S.J. and Nigg,E.A.
  TITLE     Identification of 21 novel human protein kinases, including 3
            members of a family related to the cell cycle regulator nimA of
            Aspergillus nidulans
  JOURNAL   Cell Growth Differ 4 (10), 821-830 (1993)
   PUBMED   8274451
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC094784.1, BC069634.1 and
            BM021447.1.
            
            On Jan 5, 2016 this sequence version replaced XP_005266272.1.
            
            Summary: This gene encodes a member of the cyclin-dependent protein
            kinase (CDK) family. CDK family members are known to be important
            regulators of cell cycle progression. This kinase and its
            regulatory subunit, cyclin C, are components of the Mediator
            transcriptional regulatory complex, involved in both
            transcriptional activation and repression by phosphorylation of the
            carboxy-terminal domain of the largest subunit of RNA polymerase
            II. This kinase regulates transcription by targeting the
            cyclin-dependent kinase 7 subunits of the general transcription
            initiation factor IIH, thus providing a link between the Mediator
            complex and the basal transcription machinery. Multiple pseudogenes
            of this gene have been identified. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Oct 2016].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 3' coding region, compared to variant 1, which
            results in a protein (isoform 2) that is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.150001.1,
                                           SRR1163657.282316.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q12.13"
     Protein         1..463
                     /product="cyclin-dependent kinase 8 isoform 2"
                     /EC_number="2.7.11.23"
                     /EC_number="2.7.11.22"
                     /note="CDK8 protein kinase; protein kinase K35; cell
                     division protein kinase 8; mediator complex subunit CDK8;
                     mediator of RNA polymerase II transcription subunit CDK8"
                     /calculated_mol_wt=53025
     Region          1..15
                     /region_name="Interaction with CCNC"
                     /note="propagated from UniProtKB/Swiss-Prot (P49336.1)"
     Region          3..335
                     /region_name="STKc_CDK8"
                     /note="Catalytic domain of the Serine/Threonine Kinase,
                     Cyclin-Dependent protein Kinase 8; cd07868"
                     /db_xref="CDD:270851"
     Site            order(3..6,9,13,58..59,61,64..65,67..69,71..73,84,86..88,
                     91..93,145..147)
                     /site_type="other"
                     /note="CDK/cyclin interface [polypeptide binding]"
                     /db_xref="CDD:270851"
     Site            order(27..30,35,50,52,65,79,97..100,103,105..106,151,153,
                     155..156,158,173,176,191,193..196,198,236..237)
                     /site_type="active"
                     /db_xref="CDD:270851"
     Site            order(27..30,35,50,52,79,97..100,103,106,155..156,158,173)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270851"
     Site            order(65,105,151,153,176,191,193..196,198,236..237)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270851"
     Site            172..198
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270851"
     CDS             1..463
                     /gene="CDK8"
                     /gene_synonym="IDDHBA; K35"
                     /coded_by="NM_001318368.2:514..1905"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:1024"
                     /db_xref="HGNC:HGNC:1779"
                     /db_xref="MIM:603184"
ORIGIN      
        1 mdydfkvkls serervedlf eyegckvgrg tyghvykakr kdgkddkdya lkqiegtgis
       61 msacreiall relkhpnvis lqkvflshad rkvwllfdya ehdlwhiikf hraskankkp
      121 vqlprgmvks llyqildgih ylhanwvlhr dlkpanilvm gegpergrvk iadmgfarlf
      181 nsplkpladl dpvvvtfwyr apelllgarh ytkaidiwai gcifaellts epifhcrqed
      241 iktsnpyhhd qldrifnvmg fpadkdwedi kkmpehstlm kdfrrntytn cslikymekh
      301 kvkpdskafh llqklltmdp ikritseqam qdpyfledpl ptsdvfagcq ipypkreflt
      361 eeepddkgdk nqqqqqgnnh tngtghpgnq dsshtqgppl kkvrvvpptt tsgglimtsd
      421 yqrsnphaay pnpgpstsqp qssmgysats qqppqyshqt hry
//
LOCUS       NP_001268402             480 aa            linear   PRI 20-NOV-2025
DEFINITION  melanophilin isoform 3 [Homo sapiens].
ACCESSION   NP_001268402
VERSION     NP_001268402.1
DBSOURCE    REFSEQ: accession NM_001281473.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Kim,M.Y., Kim,Y.H., Park,E.R., Shin,Y., Kim,G.H., Jeong,J.H.,
            Gu,M.B., Lee,K.H. and Shin,H.J.
  TITLE     MLPH is a novel adipogenic factor controlling redox homeostasis to
            inhibit lipid peroxidation in adipocytes
  JOURNAL   Biochem Biophys Res Commun 734, 150459 (2024)
   PUBMED   39083977
  REMARK    GeneRIF: MLPH is a novel adipogenic factor controlling redox
            homeostasis to inhibit lipid peroxidation in adipocytes.
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 480)
  AUTHORS   Guo,D., Jain,R., Hwang,J.S., Weninger,W., Beaumont,K.A. and
            Tikoo,S.
  TITLE     RAB27A/Melanophilin Blocker Inhibits Melanoma Cell Motility and
            Invasion
  JOURNAL   J Invest Dermatol 140 (7), 1470-1473 (2020)
   PUBMED   31978414
  REMARK    GeneRIF: RAB27A/Melanophilin Blocker Inhibits Melanoma Cell
            Motility and Invasion.
REFERENCE   5  (residues 1 to 480)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 480)
  AUTHORS   Fukuda,M.
  TITLE     Synaptotagmin-like protein (Slp) homology domain 1 of
            Slac2-a/melanophilin is a critical determinant of GTP-dependent
            specific binding to Rab27A
  JOURNAL   J Biol Chem 277 (42), 40118-40124 (2002)
   PUBMED   12189142
  REMARK    GeneRIF: SHD1 of Slac2-a/melanophilin alone is both necessary and
            sufficient for high affinity specific recognition of the GTP-bound
            form of Rab27A
REFERENCE   7  (residues 1 to 480)
  AUTHORS   Strom,M., Hume,A.N., Tarafder,A.K., Barkagianni,E. and Seabra,M.C.
  TITLE     A family of Rab27-binding proteins. Melanophilin links Rab27a and
            myosin Va function in melanosome transport
  JOURNAL   J Biol Chem 277 (28), 25423-25430 (2002)
   PUBMED   11980908
  REMARK    GeneRIF: links rab27a and myosin Va function in melanosome
            transport
REFERENCE   8  (residues 1 to 480)
  AUTHORS   Nagashima,K., Torii,S., Yi,Z., Igarashi,M., Okamoto,K., Takeuchi,T.
            and Izumi,T.
  TITLE     Melanophilin directly links Rab27a and myosin Va through its
            distinct coiled-coil regions
  JOURNAL   FEBS Lett 517 (1-3), 233-238 (2002)
   PUBMED   12062444
  REMARK    GeneRIF: Melanophilin has a role in bridging Rab27a on melanosomes
            and myosin Va on actin filaments during melanosome transport.
REFERENCE   9  (residues 1 to 480)
  AUTHORS   Fukuda,M., Kuroda,T.S. and Mikoshiba,K.
  TITLE     Slac2-a/melanophilin, the missing link between Rab27 and myosin Va:
            implications of a tripartite protein complex for melanosome
            transport
  JOURNAL   J Biol Chem 277 (14), 12432-12436 (2002)
   PUBMED   11856727
  REMARK    GeneRIF: Slac2-a/melanophilin, the missing link between Rab27 and
            myosin Va: implications of a tripartite protein complex for
            melanosome transport
            GeneRIF: Slac2-a/melanophilin contains an N-terminal Slp homology
            domain (SHD) (PMID: 11327731). The SHD of Slac2-a specifically and
            directly binds the GTP-bound form of Rab27A and Rab27B (PMID:
            11773082). The C-terminus of Slac2-a directly binds myosin Va.
REFERENCE   10 (residues 1 to 480)
  AUTHORS   Matesic,L.E., Yip,R., Reuss,A.E., Swing,D.A., O'Sullivan,T.N.,
            Fletcher,C.F., Copeland,N.G. and Jenkins,N.A.
  TITLE     Mutations in Mlph, encoding a member of the Rab effector family,
            cause the melanosome transport defects observed in leaden mice
  JOURNAL   Proc Natl Acad Sci U S A 98 (18), 10238-10243 (2001)
   PUBMED   11504925
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC300186.1, AK225381.1,
            AC112721.3, BC014948.1, BM992819.1 and AC104667.5.
            
            Summary: This gene encodes a member of the exophilin subfamily of
            Rab effector proteins. The protein forms a ternary complex with the
            small Ras-related GTPase Rab27A in its GTP-bound form and the motor
            protein myosin Va. A similar protein complex in mouse functions to
            tether pigment-producing organelles called melanosomes to the actin
            cytoskeleton in melanocytes, and is required for visible
            pigmentation in the hair and skin. A mutation in this gene results
            in Griscelli syndrome type 3, which is characterized by a
            silver-gray hair color and abnormal pigment distribution in the
            hair shaft. Several alternatively spliced transcript variants
            encoding different isoforms have been found for this gene.
            [provided by RefSeq, Jul 2013].
            
            Transcript Variant: This variant (3) lacks three alternate in-frame
            exons compared to variant 1. The resulting isoform (3) has the same
            N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK225381.1, SRR5189664.103562.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37.3"
     Protein         1..480
                     /product="melanophilin isoform 3"
                     /note="exophilin-3; synaptotagmin-like protein 2a; slp
                     homolog lacking C2 domains a; synaptotagmin-like protein
                     homologue lacking C2 domains-a"
                     /calculated_mol_wt=52511
     Region          8..125
                     /region_name="FYVE_2"
                     /note="FYVE-type zinc finger; pfam02318"
                     /db_xref="CDD:426716"
     CDS             1..480
                     /gene="MLPH"
                     /gene_synonym="SLAC2-A"
                     /coded_by="NM_001281473.2:212..1654"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS63173.1"
                     /db_xref="GeneID:79083"
                     /db_xref="HGNC:HGNC:29643"
                     /db_xref="MIM:606526"
ORIGIN      
        1 mgkkldlskl tdeeaqhvle vvqrdfdlrr keeerlealk gkikkesskr ellsdtahln
       61 ethcarclqp yqllvnskrq clecglftck scgrvhpeeq gwicdpchla rvvkigslew
      121 yyehvkarfk rfgsakvirs lhgrlqggag peliseersg dsdqtdedge pgseaqaqaq
      181 pfgsksltde scsekaaphk aegleeadtg asgchshpee qptsispsrh galaelcppg
      241 gshrmalgta aalgsnvirn eqlplqylad vdtsdeesir ahvmashhsk rrgrassesq
      301 glgagvrtea dveeealrrk leeltsnvsd qetsseeeea kdekaepnrd ksvgplpqad
      361 pevsdiesri aalraagltv kpsgkprrks nlpiflprva gklgkrpedp nadpsseaka
      421 mavpyllrrk fsnslksqgk dddsfdrksv yrgsltqrnp narkgmasht fakpvvahqs
//
LOCUS       NP_001350469            1975 aa            linear   PRI 20-NOV-2025
DEFINITION  dedicator of cytokinesis protein 4 isoform 2 [Homo sapiens].
ACCESSION   NP_001350469 XP_006716251
VERSION     NP_001350469.1
DBSOURCE    REFSEQ: accession NM_001363540.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1975)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1975)
  AUTHORS   Wu,C., Wang,C., Xiao,B., Li,S., Sheng,Y., Wang,Q., Tao,J., Zhang,Y.
            and Jiang,X.
  TITLE     Integration analysis of lncRNA and mRNA expression data identifies
            DOCK4 as a potential biomarker for elderly osteoporosis
  JOURNAL   BMC Med Genomics 17 (1), 70 (2024)
   PUBMED   38443923
  REMARK    GeneRIF: Integration analysis of lncRNA and mRNA expression data
            identifies DOCK4 as a potential biomarker for elderly osteoporosis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1975)
  AUTHORS   Herbst,C., Bothe,V., Wegler,M., Axer-Schaefer,S.,
            Audebert-Bellanger,S., Gecz,J., Cogne,B., Feldman,H.B.,
            Horn,A.H.C., Hurst,A.C.E., Kelly,M.A., Kruer,M.C., Kurolap,A.,
            Laquerriere,A., Li,M., Mark,P.R., Morawski,M., Nizon,M.,
            Pastinen,T., Polster,T., Saugier-Veber,P., SeSong,J., Sticht,H.,
            Stieler,J.T., Thifffault,I., van Eyk,C.L., Marcorelles,P.,
            Vezain-Mouchard,M., Abou Jamra,R. and Oppermann,H.
  TITLE     Heterozygous loss-of-function variants in DOCK4 cause
            neurodevelopmental delay and microcephaly
  JOURNAL   Hum Genet 143 (3), 455-469 (2024)
   PUBMED   38526744
  REMARK    GeneRIF: Heterozygous loss-of-function variants in DOCK4 cause
            neurodevelopmental delay and microcephaly.
REFERENCE   4  (residues 1 to 1975)
  AUTHORS   Xu,X., He,B., Zeng,J., Yin,J., Wang,X., Luo,X., Liang,C., Luo,S.,
            Yan,H., Xiong,S., Tan,Z., Lv,D., Dai,Z., Lin,Z., Lin,J., Ye,X.,
            Chen,R., Li,Y., Wang,Y., Chen,W., Luo,Z., Li,K. and Ma,G.
  TITLE     Genetic variations in DOCK4 contribute to schizophrenia
            susceptibility in a Chinese cohort: A genetic neuroimaging study
  JOURNAL   Behav Brain Res 443, 114353 (2023)
   PUBMED   36822513
  REMARK    GeneRIF: Genetic variations in DOCK4 contribute to schizophrenia
            susceptibility in a Chinese cohort: A genetic neuroimaging study.
REFERENCE   5  (residues 1 to 1975)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1975)
  AUTHORS   Hiramoto,K., Negishi,M. and Katoh,H.
  TITLE     Dock4 is regulated by RhoG and promotes Rac-dependent cell
            migration
  JOURNAL   Exp Cell Res 312 (20), 4205-4216 (2006)
   PUBMED   17027967
  REMARK    GeneRIF: Taken together, these results suggest that Dock4 plays an
            important role in the regulation of cell migration through
            activation of Rac1, and that RhoG is a key upstream regulator for
            Dock4.
REFERENCE   7  (residues 1 to 1975)
  AUTHORS   Yan,D., Li,F., Hall,M.L., Sage,C., Hu,W.H., Giallourakis,C.,
            Upadhyay,G., Ouyang,X.M., Du,L.L., Bethea,J.R., Chen,Z.Y.,
            Yajnik,V. and Liu,X.Z.
  TITLE     An isoform of GTPase regulator DOCK4 localizes to the stereocilia
            in the inner ear and binds to harmonin (USH1C)
  JOURNAL   J Mol Biol 357 (3), 755-764 (2006)
   PUBMED   16464467
REFERENCE   8  (residues 1 to 1975)
  AUTHORS   Liang,H., Castro,P.D., Ma,J. and Nagarajan,L.
  TITLE     Finer delineation and transcript map of the 7q31 locus deleted in
            myeloid neoplasms
  JOURNAL   Cancer Genet Cytogenet 162 (2), 151-159 (2005)
   PUBMED   16213364
REFERENCE   9  (residues 1 to 1975)
  AUTHORS   Yajnik,V., Paulding,C., Sordella,R., McClatchey,A.I., Saito,M.,
            Wahrer,D.C., Reynolds,P., Bell,D.W., Lake,R., van den Heuvel,S.,
            Settleman,J. and Haber,D.A.
  TITLE     DOCK4, a GTPase activator, is disrupted during tumorigenesis
  JOURNAL   Cell 112 (5), 673-684 (2003)
   PUBMED   12628187
REFERENCE   10 (residues 1 to 1975)
  AUTHORS   Cote,J.F. and Vuori,K.
  TITLE     Identification of an evolutionarily conserved superfamily of
            DOCK180-related proteins with guanine nucleotide exchange activity
  JOURNAL   J Cell Sci 115 (Pt 24), 4901-4913 (2002)
   PUBMED   12432077
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004111.1, AC003080.1,
            AC003077.1 and AC005047.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On May 24, 2018 this sequence version replaced XP_006716251.1.
            
            Summary: This gene is a member of the dedicator of cytokinesis
            (DOCK) family and encodes a protein with a DHR-1 (CZH-1) domain, a
            DHR-2 (CZH-2) domain and an SH3 domain. This membrane-associated,
            cytoplasmic protein functions as a guanine nucleotide exchange
            factor and is involved in regulation of adherens junctions between
            cells. Mutations in this gene have been associated with ovarian,
            prostate, glioma, and colorectal cancers. Alternatively spliced
            variants which encode different protein isoforms have been
            described, but only one has been fully characterized. [provided by
            RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660805.183757.1,
                                           SRR1660805.74538.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000428084.6/ ENSP00000410746.1
            RefSeq Select criteria :: based on manual assertion, conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1975
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.1"
     Protein         1..1975
                     /product="dedicator of cytokinesis protein 4 isoform 2"
                     /note="dedicator of cytokinesis protein 4"
                     /calculated_mol_wt=226048
     Region          10..65
                     /region_name="SH3_DOCK4_B"
                     /note="Src Homology 3 domain of Class B Dedicator of
                     Cytokinesis 4; cd12049"
                     /db_xref="CDD:212982"
     Site            order(12..16,23,28..30,32,36..37,41..42,44,52,54,56,58,
                     60..61,63,65)
                     /site_type="other"
                     /note="ELMO interaction site [polypeptide binding]"
                     /db_xref="CDD:212982"
     Site            order(15,17,20,24,41..42,58,60..61)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212982"
     Region          73..392
                     /region_name="DOCK_N"
                     /note="DOCK N-terminus; pfam16172"
                     /db_xref="CDD:465040"
     Site            167
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            193
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          400..584
                     /region_name="C2_Dock-B"
                     /note="C2 domains found in Dedicator Of CytoKinesis (Dock)
                     class B proteins; cd08695"
                     /db_xref="CDD:176077"
     Region          1206..1596
                     /region_name="DHR2_DOCK4"
                     /note="Dock Homology Region 2, a GEF domain, of Class B
                     Dedicator of Cytokinesis 4; cd11705"
                     /db_xref="CDD:212578"
     Site            order(1286,1296,1298..1299,1301..1302,1305..1306,
                     1308..1309,1312..1313)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:212578"
     Site            order(1324,1326,1350,1353..1356,1358..1359,1372..1374,
                     1391..1393,1427..1430,1441..1442,1445,1447,1484..1485,
                     1488,1508..1509,1511..1512,1515..1517,1520..1522,
                     1525..1526,1529,1559,1581,1584)
                     /site_type="other"
                     /note="putative Rac/Cdc42 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212578"
     Site            1520..1525
                     /site_type="other"
                     /note="nucleotide sensor"
                     /db_xref="CDD:212578"
     Site            1608
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1616
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1623
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1627
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1629
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1640
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1657..1738
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1751..1975
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Site            1778
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P59764; propagated from
                     UniProtKB/Swiss-Prot (Q8N1I0.3)"
     Region          1797..1803
                     /region_name="SH3-binding. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8N1I0.3)"
     CDS             1..1975
                     /gene="DOCK4"
                     /coded_by="NM_001363540.2:262..6189"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS87541.1"
                     /db_xref="GeneID:9732"
                     /db_xref="HGNC:HGNC:19192"
                     /db_xref="MIM:607679"
ORIGIN      
        1 mwipteheky gvviasfrgt vpyglsleig dtvqilekcd gwyrgfalkn pnikgifpss
       61 yvhlknacvk nkgqfemvip tedsvitemt stlrdwgtmw kqlyvrnegd lfhrlwhimn
      121 eildlrrqvl vghlthdrmk dvkrhitarl dwgneqlgld lvprkeyamv dpedisitel
      181 yrlmehrhrk kdtpvqassh hlfvqmkslm csnlgeelev ifslfdsken rpiserfflr
      241 lnrnglpkap dkperhcslf vdlgsselrk diyitvhiir igrmgagekk nacsvqyrrp
      301 fgcavlsiad lltgetkddl ilkvymcnte sewyqiheni ikklnarynl tgsnaglavs
      361 lqllhgdieq irreyssvfs hgvsitrklg fsniimpgem rndlyitier gefekggksv
      421 arnvevtmfi vdssgqtlkd fisfgsgepp aseyhsfvly hnnsprwsel lklpipvdkf
      481 rgahirfefr hcstkekgek klfgfsfvpl mqedgrtlpd gthelivhkc eentnlqdtt
      541 rylklpfskg iflgnnnqam katkesfcit sflcstkltq ngdmldllkw rthpdkitgc
      601 lsklkeidgs eivkflqdtl dtlfgilden sqkygskvfd slvhiinllq dskfhhfkpv
      661 mdtyieshfa galayrdlik vlkwyvdrit eaerqehiqe vlkaqeyifk yivqsrrlfs
      721 latggqneee frcciqellm svrfflsqes kgsgalsqsq avflssfpav ysellklfdv
      781 revanlvqdt lgslptilhv ddslqaiklq cigktvesql ytnpdsryil lpvvlhhlhi
      841 hlqeqkdlim carilsnvfc likknsseks vleeidviva slldillrti leitsrpqps
      901 ssamrfqfqd vtgefvacll sllrqmtdrh yqqlldsfnt keelrdfllq iftvfrilir
      961 pemfpkdwtv mrlvannvii ttvlylsdal rknflnenfd ykiwdsyfyl avifinqlcl
     1021 qlemftpskk kkvlekygdm rvtmgceifs mwqnlgehkl hfipaligpf levtlipqpd
     1081 lrnvmipifh dmmdweqrrs gnfkqveakl idkldslmse gkgdetyrel fnsiiplfgp
     1141 ypsllkkier etwresgvsl iatvtrlmer lldyrdcmkm gevdgkkigc tvsllnfykt
     1201 elnkeemyir yihklydlhl kaqnfteaay tlllydelle wsdrplrefl typmqtewqr
     1261 kehlhltiiq nfdrgkcwen giilcrkiae qyesyydyrn lskmrmmeas lydkimdqqr
     1321 lepeffrvgf ygkkfpfflr nkefvcrghd yerleafqqr mlnefphaia mqhanqpdet
     1381 ifqaeaqylq iyavtpipes qevlqregvp dniksfykvn hiwkfrydrp fhkgtkdken
     1441 efkslwvert slylvqslpg isrwfevekr evvemsplen aievlenknq qlktlisqcq
     1501 trqmqninpl tmclngvida avnggvsryq eaffvkeyil shpedgekia rlrelmleqa
     1561 qilefglavh ekfvpqdmrp lhkklvdqff vmksslgiqe fsacmqaspv hfpngsprvc
     1621 rnsapasvsp dgtrviprrs plsypavnry sssslssqas aevsnitgqs essdevfnmq
     1681 pspstsslss thsaspnvts sapssarasp llsdkhkhsr ensclsprer pcsaiyptpv
     1741 epsqrmlfnh igdgalprsd pnlsapekav nptpsswsld sgkeaknmsd sgklisppvp
     1801 prptqtaspa rhttsvspsp agrsplkgsv qsftpspvey hspglisnsp vlsgsyssgi
     1861 sslsrcstse tsgfenqvne qsaplpvpvp vpvpsyggee pvrkesktpp pysvyertlr
     1921 rpvplphsls ipvtseppal ppkplaarss hlengarrtd pgprprplpr kvsql
//
LOCUS       NP_059111                587 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 3 isoform 1 [Homo sapiens].
ACCESSION   NP_059111
VERSION     NP_059111.2
DBSOURCE    REFSEQ: accession NM_017415.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 587)
  AUTHORS   Ying,S., Guo,Q. and Zhang,C.
  TITLE     KLHL3-dependent WNK4 degradation affected by potassium through the
            neddylation and autophagy pathway
  JOURNAL   BMC Nephrol 24 (1), 217 (2023)
   PUBMED   37481568
  REMARK    GeneRIF: KLHL3-dependent WNK4 degradation affected by potassium
            through the neddylation and autophagy pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 587)
  AUTHORS   Lin,Y., Li,Q. and Jin,X.
  TITLE     Kelch-like protein 3 in human disease and therapy
  JOURNAL   Mol Biol Rep 49 (10), 9813-9824 (2022)
   PUBMED   35585379
  REMARK    GeneRIF: Kelch-like protein 3 in human disease and therapy.
            Review article
REFERENCE   3  (residues 1 to 587)
  AUTHORS   Chen,Z., Zhang,J., Murillo-de-Ozores,A.R., Castaneda-Bueno,M.,
            D'Amico,F., Heilig,R., Manning,C.E., Sorrell,F.J., D'Angiolella,V.,
            Fischer,R., Mulder,M.P.C., Gamba,G., Alessi,D.R. and Bullock,A.N.
  TITLE     Sequence and structural variations determining the recruitment of
            WNK kinases to the KLHL3 E3 ligase
  JOURNAL   Biochem J 479 (5), 661-675 (2022)
   PUBMED   35179207
REFERENCE   4  (residues 1 to 587)
  AUTHORS   Etges,A., Hellmig,N., Walenda,G., Haddad,B.G., Machtens,J.P.,
            Morosan,T., Rump,L.C. and Scholl,U.I.
  TITLE     A Novel Homozygous KLHL3 Mutation as a Cause of Autosomal Recessive
            Pseudohypoaldosteronism Type II Diagnosed Late in Life
  JOURNAL   Nephron 146 (4), 418-428 (2022)
   PUBMED   35093948
REFERENCE   5  (residues 1 to 587)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 587)
  AUTHORS   Yang,C.L., Zhu,X. and Ellison,D.H.
  TITLE     The thiazide-sensitive Na-Cl cotransporter is regulated by a WNK
            kinase signaling complex
  JOURNAL   J Clin Invest 117 (11), 3403-3411 (2007)
   PUBMED   17975670
REFERENCE   7  (residues 1 to 587)
  AUTHORS   Kahle,K.T., Wilson,F.H., Leng,Q., Lalioti,M.D., O'Connell,A.D.,
            Dong,K., Rapson,A.K., MacGregor,G.G., Giebisch,G., Hebert,S.C. and
            Lifton,R.P.
  TITLE     WNK4 regulates the balance between renal NaCl reabsorption and K+
            secretion
  JOURNAL   Nat Genet 35 (4), 372-376 (2003)
   PUBMED   14608358
REFERENCE   8  (residues 1 to 587)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
REFERENCE   9  (residues 1 to 587)
  AUTHORS   Lai,F., Orelli,B.J., Till,B.G., Godley,L.A., Fernald,A.A.,
            Pamintuan,L. and Le Beau,M.M.
  TITLE     Molecular characterization of KLHL3, a human homologue of the
            Drosophila kelch gene
  JOURNAL   Genomics 66 (1), 65-75 (2000)
   PUBMED   10843806
REFERENCE   10 (residues 1 to 587)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA083147.1, AB032955.1 and
            AC106775.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jan 30, 2008 this sequence version replaced NP_059111.1.
            
            Summary: This gene is ubiquitously expressed and encodes a
            full-length protein which has an N-terminal BTB domain followed by
            a BACK domain and six kelch-like repeats in the C-terminus. These
            kelch-like repeats promote substrate ubiquitination of bound
            proteins via interaction of the BTB domain with the CUL3 (cullin 3)
            component of a cullin-RING E3 ubiquitin ligase (CRL) complex.
            Muatations in this gene cause pseudohypoaldosteronism type IID
            (PHA2D); a rare Mendelian syndrome featuring hypertension,
            hyperkalaemia and metabolic acidosis. Alternative splicing results
            in multiple transcript variants encoding distinct isoforms.
            [provided by RefSeq, Mar 2012].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1; also known as KLHL3a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data because no single transcript was available
            for the full length of the gene. The extent of this transcript is
            supported by transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF208068.1, SRR1660805.258662.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309755.9/ ENSP00000312397.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..587
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.2"
     Protein         1..587
                     /product="kelch-like protein 3 isoform 1"
                     /note="kelch-like protein 3"
                     /calculated_mol_wt=64839
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26435498; propagated from
                     UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          29..149
                     /region_name="BTB_POZ_KLHL3"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 3 (KLHL3); cd18339"
                     /db_xref="CDD:349648"
     Region          47..566
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Site            order(73..74,77..78,82..85,92..95,125,128..129,131,136)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:349648"
     Region          147..276
                     /region_name="BACK_KLHL3"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 3 (KLHL3); cd18513"
                     /db_xref="CDD:350588"
     Site            order(160..163,165)
                     /site_type="other"
                     /note="cullin binding site [polypeptide binding]"
                     /db_xref="CDD:350588"
     Site            295
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26435498; propagated from
                     UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          297..333
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          302..347
                     /region_name="Kelch 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          337..380
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          348..394
                     /region_name="Kelch 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     Site            375
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000269|PubMed:26435498; propagated from
                     UniProtKB/Swiss-Prot (Q9UH77.2)"
     Site            376
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:26435498; propagated from
                     UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          384..428
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          396..441
                     /region_name="Kelch 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          431..476
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Site            433
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA and PKC.
                     /evidence=ECO:0000269|PubMed:25313067,
                     ECO:0000269|PubMed:26435498, ECO:0000269|PubMed:27727489,
                     ECO:0000269|PubMed:30718414; propagated from
                     UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          442..490
                     /region_name="Kelch 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          480..524
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          491..537
                     /region_name="Kelch 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     Region          527..573
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          539..585
                     /region_name="Kelch 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UH77.2)"
     CDS             1..587
                     /gene="KLHL3"
                     /gene_synonym="PHA2D"
                     /coded_by="NM_017415.3:444..2207"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4192.1"
                     /db_xref="GeneID:26249"
                     /db_xref="HGNC:HGNC:6354"
                     /db_xref="MIM:605775"
ORIGIN      
        1 megesvklss qtliqagdde knqrtitvnp ahmgkafkvm nelrskqllc dvmivaedve
       61 ieahrvvlaa cspyfcamft gdmseskakk ieikdvdgqt lsklidyiyt aeievteenv
      121 qvllpaasll qlmdvrqncc dflqsqlhpt nclgirafad vhtctdllqq anayaeqhfp
      181 evmlgeefls lsldqvcsli ssdkltvsse ekvfeavisw inyeketrle hmaklmehvr
      241 lpllprdylv qtveeealik nnntckdfli eamkyhllpl dqrlliknpr tkprtpvslp
      301 kvmivvggqa pkairsvecy dfeedrwdqi aelpsrrcra gvvfmaghvy avggfngslr
      361 vrtvdvydgv kdqwtsiasm qerrstlgaa vlndllyavg gfdgstglas veaysyktne
      421 wffvapmntr rssvgvgvve gklyavggyd gasrqclstv eqynpatnew iyvadmstrr
      481 sgagvgvlsg qlyatgghdg plvrksvevy dpgtntwkqv admnmcrrna gvcavnglly
      541 vvggddgscn lasveyynpv tdkwtllptn mstgrsyagv avihksl
//
LOCUS       NP_001165415             682 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform c [Homo sapiens].
ACCESSION   NP_001165415
VERSION     NP_001165415.1
DBSOURCE    REFSEQ: accession NM_001171944.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Transcript Variant: This variant (3) differs in the 5' UTR and
            lacks three in-frame exons in the middle portion of the coding
            region, compared to variant 1. The resulting isoform (c) is shorter
            than isoform a.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK302896.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..682
                     /product="SUN domain-containing protein 1 isoform c"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=76272
     Region          62..189
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     Region          314..367
                     /region_name="SUN1_cc1"
                     /note="coiled-coil domain 1 of SUN domain-containing
                     protein 1 and similar proteins; cd21439"
                     /db_xref="CDD:410605"
     Site            order(314,317..318,321,324..325,328..329,331..332,
                     335..336,338..339,342..343,345..346,349,352..353,356,
                     359..360,363..364,366..367)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:410605"
     Region          326..>459
                     /region_name="CwlO1"
                     /note="Uncharacterized N-terminal coiled-coil domain of
                     peptidoglycan hydrolase CwlO [Function unknown]; COG3883"
                     /db_xref="CDD:443091"
     Region          444..502
                     /region_name="HTH_SUN2"
                     /note="SUN2 helix-turn-helix domain; pfam18580"
                     /db_xref="CDD:436594"
     Region          545..680
                     /region_name="Sad1_UNC"
                     /note="Sad1 / UNC-like C-terminal; pfam07738"
                     /db_xref="CDD:400199"
     CDS             1..682
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001171944.2:52..2100"
                     /note="isoform c is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55080.1"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 mdfsrlhmys ppqcvpentg ytyalsssys sdaldfeteh kldpvfdspr msrrslrlat
       61 tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq vtssgvshgg
      121 tvslqdavtr rppvldeswi reqttvdhfw gkaasgvfww lgigwyqfvt liswlnvfll
      181 trclrnickf lvlliplfll lglslrgqgn ffsflpvlnw asmhrtqrvd dpqdvfkptt
      241 srlkqplqgd seafpwhwms gveqqvasls gqchhhgenl relttllqkl qarvdqmegg
      301 aagpsasvrd avgqppretd fmafhqehev rmshledilg klrekseaiq keleqtkqkt
      361 isavgeqllp tvehlqleld qlkselsswr hvktgcetvd avqervdvqv remvkllfse
      421 dqqggsleql lqrfssqfvs kgdlqtmlrd lqlqilrnvt hhvsvtkqlp tseavvsavs
      481 eagasgitea qaraivnsal klysqdktgm vdfalesggg silstrcset yetktalmsl
      541 fgiplwyfsq sprvviqpdi ypgncwafkg sqgylvvrls mmihpaaftl ehipktlspt
      601 gnissapkdf avygleneyq eegqllgqft ydqdgeslqm fqalkrpddt afqivelrif
      661 snwghpeytc lyrfrvhgep vk
//
LOCUS       NP_001290380             553 aa            linear   PRI 20-NOV-2025
DEFINITION  kelch-like protein 36 isoform 2 [Homo sapiens].
ACCESSION   NP_001290380
VERSION     NP_001290380.1
DBSOURCE    REFSEQ: accession NM_001303451.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 553)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   2  (residues 1 to 553)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   3  (residues 1 to 553)
  AUTHORS   Dubiel,W., Dubiel,D., Wolf,D.A. and Naumann,M.
  TITLE     Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian
            Cell Differentiation
  JOURNAL   Trends Biochem Sci 43 (2), 95-107 (2018)
   PUBMED   29249570
  REMARK    Review article
REFERENCE   4  (residues 1 to 553)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   5  (residues 1 to 553)
  AUTHORS   Dhanoa,B.S., Cogliati,T., Satish,A.G., Bruford,E.A. and
            Friedman,J.S.
  TITLE     Update on the Kelch-like (KLHL) gene family
  JOURNAL   Hum Genomics 7 (1), 13 (2013)
   PUBMED   23676014
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 553)
  AUTHORS   Croteau-Chonka,D.C., Marvelle,A.F., Lange,E.M., Lee,N.R.,
            Adair,L.S., Lange,L.A. and Mohlke,K.L.
  TITLE     Genome-wide association study of anthropometric traits and evidence
            of interactions with age and study year in Filipino women
  JOURNAL   Obesity (Silver Spring) 19 (5), 1019-1027 (2011)
   PUBMED   20966902
REFERENCE   7  (residues 1 to 553)
  AUTHORS   Furukawa,M., He,Y.J., Borchers,C. and Xiong,Y.
  TITLE     Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin
            ligases
  JOURNAL   Nat Cell Biol 5 (11), 1001-1007 (2003)
   PUBMED   14528312
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA049618.1, BC032400.1, AC009116.8 and AW337439.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            segment compared to variant 1. The resulting isoform (2) has the
            same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC032400.1, SRR14038195.1882604.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2149004, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..553
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.1"
     Protein         1..553
                     /product="kelch-like protein 36 isoform 2"
                     /note="kelch-like protein 36; kelch-like 36"
                     /calculated_mol_wt=62641
     Region          21..155
                     /region_name="BTB_POZ_KLHL36"
                     /note="BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ
                     (poxvirus and zinc finger) domain found in Kelch-like
                     protein 36 (KLHL36); cd18266"
                     /db_xref="CDD:349575"
     Region          45..522
                     /region_name="PHA03098"
                     /note="kelch-like protein; Provisional"
                     /db_xref="CDD:222983"
     Region          143..242
                     /region_name="BACK_KLHL36"
                     /note="BACK (BTB and C-terminal Kelch) domain found in
                     Kelch-like protein 36 (KLHL36); cd18475"
                     /db_xref="CDD:350550"
     Region          372..416
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          420..470
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     Region          473..519
                     /region_name="KELCH repeat"
                     /note="KELCH repeat [structural motif]"
                     /db_xref="CDD:276965"
     CDS             1..553
                     /gene="KLHL36"
                     /gene_synonym="C16orf44"
                     /coded_by="NM_001303451.2:156..1817"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS76909.1"
                     /db_xref="GeneID:79786"
                     /db_xref="HGNC:HGNC:17844"
ORIGIN      
        1 mmegsrqtrv srpykisess kvyrwadhss tvlqrlneqr lrglfcdvvl vadeqrvpah
       61 rnllavcsdy fnsmftigmr eafqkeveli gasyiglkav vdflyggelv ldggnidyvl
      121 etahllqiwt vvdfcceyle qevsednyly lqelasiysl krldafidgf ilnhfgtlsf
      181 tpdflqnvsm qklcvylsss evqrecehdl lqaalqwltq qpereaharq vlenihfpli
      241 pkndllhrvk pavcsllpke ancegfieea vryhnnlaaq pvmqtkrtal rtnqerllfv
      301 ggevsercle lsddtcylda kseqwvketp lparrshhcv avlggfifia ggsfsrdngg
      361 daasnllyrf tyghagtiyk dfvyisgghd yqigpyrknl lcydhrtdvw eerrpmttar
      421 gwhsmcslgd siysiggsdd niesmerfdv lgveayspqc nqwtrvapll hansesgvav
      481 wegriyilgg yswentafsk tvqvydread kwsrgvdlpk aiaggsacvc aleprpedkk
      541 kkgkgkrhqd rgq
//
LOCUS       NP_919248                209 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein with multiple splicing 2 [Homo sapiens].
ACCESSION   NP_919248 XP_496072
VERSION     NP_919248.1
DBSOURCE    REFSEQ: accession NM_194272.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 209)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 209)
  AUTHORS   Cheng,M., Zhan,X., Xu,Y., Wang,S., Zhang,H., Fang,L., Jin,H. and
            Chen,W.
  TITLE     DNA methylation of RNA-binding protein for multiple splicing 2
            functions as diagnosis biomarker in gastric cancer pathogenesis and
            its potential clinical significance
  JOURNAL   Bioengineered 13 (2), 4347-4360 (2022)
   PUBMED   35137653
  REMARK    GeneRIF: DNA methylation of RNA-binding protein for multiple
            splicing 2 functions as diagnosis biomarker in gastric cancer
            pathogenesis and its potential clinical significance.
REFERENCE   3  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 209)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 209)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   6  (residues 1 to 209)
  AUTHORS   Sagnol,S., Yang,Y., Bessin,Y., Allemand,F., Hapkova,I.,
            Notarnicola,C., Guichou,J.F., Faure,S., Labesse,G. and de Santa
            Barbara,P.
  TITLE     Homodimerization of RBPMS2 through a new RRM-interaction motif is
            necessary to control smooth muscle plasticity
  JOURNAL   Nucleic Acids Res 42 (15), 10173-10184 (2014)
   PUBMED   25064856
  REMARK    GeneRIF: The study shows that RBPMS2 homodimerizes through a
            particular sequence motif located in its RNA recognition motif
            domain.
REFERENCE   7  (residues 1 to 209)
  AUTHORS   Farazi,T.A., Leonhardt,C.S., Mukherjee,N., Mihailovic,A., Li,S.,
            Max,K.E., Meyer,C., Yamaji,M., Cekan,P., Jacobs,N.C.,
            Gerstberger,S., Bognanni,C., Larsson,E., Ohler,U. and Tuschl,T.
  TITLE     Identification of the RNA recognition element of the RBPMS family
            of RNA-binding proteins and their transcriptome-wide mRNA targets
  JOURNAL   RNA 20 (7), 1090-1102 (2014)
   PUBMED   24860013
REFERENCE   8  (residues 1 to 209)
  AUTHORS   Hapkova,I., Skarda,J., Rouleau,C., Thys,A., Notarnicola,C.,
            Janikova,M., Bernex,F., Rypka,M., Vanderwinden,J.M., Faure,S.,
            Vesely,J. and de Santa Barbara,P.
  TITLE     High expression of the RNA-binding protein RBPMS2 in
            gastrointestinal stromal tumors
  JOURNAL   Exp Mol Pathol 94 (2), 314-321 (2013)
   PUBMED   23295309
  REMARK    GeneRIF: RBPMS2 is up-regulated in Gastrointestinal stromal tumors
            compared to normal adult gastrointestinal tissues, indicating that
            RBPMS2 might represent a new diagnostic marker for GISTs and a
            potential target for cancer therapy.
REFERENCE   9  (residues 1 to 209)
  AUTHORS   Notarnicola,C., Rouleau,C., Le Guen,L., Virsolvy,A., Richard,S.,
            Faure,S. and De Santa Barbara,P.
  TITLE     The RNA-binding protein RBPMS2 regulates development of
            gastrointestinal smooth muscle
  JOURNAL   Gastroenterology 143 (3), 687-697 (2012)
   PUBMED   22683258
  REMARK    GeneRIF: RBPMS3 transcripts are up-regulation in colons of patients
            with chronic psuedo obstruction syndrome.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091582.17, AK127873.1 and
            AI274305.1.
            
            On May 1, 2005 this sequence version replaced XP_496072.1.
            
            Summary: The protein encoded by this gene is a member of the RNA
            recognition motif (RRM)-containing protein family and is involved
            in the development and dedifferentiation of digestive smooth muscle
            cells. The encoded protein functions as a homodimer and indirectly
            inhibits the bone morphogenetic protein pathway. [provided by
            RefSeq, Aug 2016].
            
            Transcript Variant: This variant (1) represents the protein-coding
            transcript.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY369207.1, AK127873.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300069.5/ ENSP00000300069.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..209
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22.31"
     Protein         1..209
                     /product="RNA-binding protein with multiple splicing 2"
                     /note="RNA binding protein with multiple splicing 2"
                     /calculated_mol_wt=22365
     Region          1..24
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     Region          30..105
                     /region_name="RRM_RBPMS2"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     RNA-binding protein with multiple splicing 2 (RBP-MS2);
                     cd12683"
                     /db_xref="CDD:410084"
     Region          41..51
                     /region_name="Important for homodimerization.
                     /evidence=ECO:0000269|PubMed:25064856"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6ZRY4.1)"
     CDS             1..209
                     /gene="RBPMS2"
                     /coded_by="NM_194272.3:271..900"
                     /db_xref="CCDS:CCDS32271.1"
                     /db_xref="GeneID:348093"
                     /db_xref="HGNC:HGNC:19098"
                     /db_xref="MIM:619034"
ORIGIN      
        1 msnlkpdgeh ggstgtgsga gsggaleeev rtlfvsglpv dikprelyll frpfkgyegs
       61 likltarqpv gfvifdsrag aeaaknalng irfdpenpqt lrlefakant kmaksklmat
      121 pnpsnvhpal gahfiardpy dlmgaalipa speawapypl ytteltpais haaftyptat
      181 aaaaalhaqv rwypssdttq qgwkyrqfc
//
LOCUS       NP_036320                378 aa            linear   PRI 20-NOV-2025
DEFINITION  forkhead box protein I1 isoform a [Homo sapiens].
ACCESSION   NP_036320
VERSION     NP_036320.2
DBSOURCE    REFSEQ: accession NM_012188.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 378)
  AUTHORS   AitRaise,I., Amalou,G., Bakhchane,A., Bousfiha,A., Abdelghaffar,H.,
            Majida,C., Bonnet,C., Petit,C. and Barakat,A.
  TITLE     Homozygous Missense Variants in FOXI1 and TMPRSS3 Genes Associated
            with Non-syndromic Deafness in Moroccan Families
  JOURNAL   Biochem Genet 62 (3), 1914-1924 (2024)
   PUBMED   37777971
  REMARK    GeneRIF: Homozygous Missense Variants in FOXI1 and TMPRSS3 Genes
            Associated with Non-syndromic Deafness in Moroccan Families.
REFERENCE   2  (residues 1 to 378)
  AUTHORS   Huang,L.H., Zhao,X.L., Cheng,X.H., Yu,Y.D., Wen,C., Li,Y.,
            Wang,X.L., Wang,X.Y., Ruan,Y. and En,H.
  TITLE     [Analysis of genotypes on 850 newborns with SLC26A4 single-allele
            mutation and the phenotypes of those with second variant]
  JOURNAL   Zhonghua Er Bi Yan Hou Tou Jing Wai Ke Za Zhi 58 (2), 117-125
            (2023)
   PUBMED   36748152
  REMARK    GeneRIF: [Analysis of genotypes on 850 newborns with SLC26A4
            single-allele mutation and the phenotypes of those with second
            variant].
REFERENCE   3  (residues 1 to 378)
  AUTHORS   Klarov,L.A., Pshennikova,V.G., Romanov,G.P., Cherdonova,A.M.,
            Solovyev,A.V., Teryutin,F.M., Luginov,N.V., Kotlyarov,P.M. and
            Barashkov,N.A.
  TITLE     Analysis of SLC26A4, FOXI1, and KCNJ10 Gene Variants in Patients
            with Incomplete Partition of the Cochlea and Enlarged Vestibular
            Aqueduct (EVA) Anomalies
  JOURNAL   Int J Mol Sci 23 (23), 15372 (2022)
   PUBMED   36499699
  REMARK    GeneRIF: Analysis of SLC26A4, FOXI1, and KCNJ10 Gene Variants in
            Patients with Incomplete Partition of the Cochlea and Enlarged
            Vestibular Aqueduct (EVA) Anomalies.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 378)
  AUTHORS   Li,J., Kang,H. and Kong,X.
  TITLE     [Diagnosis of a Chinese pedigree affected with autosomal recessive
            deafness 4 with enlarged vestibular aqueduct due to compound
            heterozygous variants of FOXI1 gene]
  JOURNAL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 39 (10), 1080-1084 (2022)
   PUBMED   36184087
  REMARK    GeneRIF: [Diagnosis of a Chinese pedigree affected with autosomal
            recessive deafness 4 with enlarged vestibular aqueduct due to
            compound heterozygous variants of FOXI1 gene].
REFERENCE   5  (residues 1 to 378)
  AUTHORS   Overdier,D.G., Ye,H., Peterson,R.S., Clevidence,D.E. and Costa,R.H.
  TITLE     The winged helix transcriptional activator HFH-3 is expressed in
            the distal tubules of embryonic and adult mouse kidney
  JOURNAL   J Biol Chem 272 (21), 13725-13730 (1997)
   PUBMED   9153225
REFERENCE   6  (residues 1 to 378)
  AUTHORS   Larsson,C., Hellqvist,M., Pierrou,S., White,I., Enerback,S. and
            Carlsson,P.
  TITLE     Chromosomal localization of six human forkhead genes, freac-1
            (FKHL5), -3 (FKHL7), -4 (FKHL8), -5 (FKHL9), -6 (FKHL10), and -8
            (FKHL12)
  JOURNAL   Genomics 30 (3), 464-469 (1995)
   PUBMED   8825632
REFERENCE   7  (residues 1 to 378)
  AUTHORS   Pierrou,S., Hellqvist,M., Samuelsson,L., Enerback,S. and
            Carlsson,P.
  TITLE     Cloning and characterization of seven human forkhead proteins:
            binding site specificity and DNA bending
  JOURNAL   EMBO J 13 (20), 5002-5012 (1994)
   PUBMED   7957066
REFERENCE   8  (residues 1 to 378)
  AUTHORS   Clevidence,D.E., Overdier,D.G., Tao,W., Qian,X., Pani,L., Lai,E.
            and Costa,R.H.
  TITLE     Identification of nine tissue-specific transcription factors of the
            hepatocyte nuclear factor 3/forkhead DNA-binding-domain family
  JOURNAL   Proc Natl Acad Sci U S A 90 (9), 3948-3952 (1993)
   PUBMED   7683413
REFERENCE   9  (residues 1 to 378)
  AUTHORS   Alexander,R.T., Gil-Pena,H., Greenbaum,L.A. and Santos,F.
  TITLE     Hereditary Distal Renal Tubular Acidosis
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   31600044
REFERENCE   10 (residues 1 to 378)
  AUTHORS   Smith,R.J.H., Azaiez,H. and Odell,A.M.
  TITLE     SLC26A4-Related Sensorineural Hearing Loss
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301640
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008660.5 and BC029778.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 27, 2002 this sequence version replaced NP_036320.1.
            
            Summary: This gene belongs to the forkhead family of transcription
            factors, which is characterized by a distinct forkhead domain. This
            gene may play an important role in the development of the cochlea
            and vestibulum, as well as in embryogenesis. The encoded protein
            has been found to be required for the transcription of four
            subunits of a proton pump found in the inner ear, the kidney, and
            the epididymis. Mutations in this gene have been associated with
            deafness, autosomal recessive 4. [provided by RefSeq, Jan 2017].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK292176.1, L13203.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968832, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000306268.8/ ENSP00000304286.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..378
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.1"
     Protein         1..378
                     /product="forkhead box protein I1 isoform a"
                     /note="forkhead-related activator 6; forkhead-like 10;
                     hepatocyte nuclear factor 3 forkhead homolog 3;
                     HNF-3/fork-head homolog-3; forkhead box protein I1;
                     forkhead-related protein FKHL10; forkhead-related
                     transcription factor 6"
                     /calculated_mol_wt=40842
     Region          1..26
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12951.3)"
     Region          120..219
                     /region_name="FH_FOXI1"
                     /note="Forkhead (FH) domain found in Forkhead box protein
                     I1 (FOXI1) and similar proteins; cd20053"
                     /db_xref="CDD:410827"
     Site            order(128,146..147,150,169..170,172..173,176,183,193..195,
                     197)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:410827"
     Region          208..278
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q12951.3)"
     CDS             1..378
                     /gene="FOXI1"
                     /gene_synonym="FKH10; FKHL10; FREAC-6; FREAC6; HFH-3;
                     HFH3"
                     /coded_by="NM_012188.5:62..1198"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4372.1"
                     /db_xref="GeneID:2299"
                     /db_xref="HGNC:HGNC:3815"
                     /db_xref="MIM:601093"
ORIGIN      
        1 mssfdlpaps pprcspqfps igqeppemnl yyenffhpqg vpspqrpsfe gggeygatpn
       61 pylwfngptm tpppylpgpn aspflpqayg vqrpllpsvs glggsdlgwl pipsqeelmk
      121 lvrppysysa liamaihgap dkrltlsqiy qyvadnfpfy nkskagwqns irhnlslndc
      181 fkkvprdedd pgkgnywtld pncekmfdng nfrrkrkrks dvssstasla lektesslpv
      241 dspkttepqd ildgaspggt tsspekrpsp ppsgapclns flssmtayvs ggsptshplv
      301 tpglspepsd ktgqnsltfn sfspltnlsn hsgggdwanp mptnmlsygg svlsqfsphf
      361 ynsvntsgvl ypregtev
//
LOCUS       NP_631906                312 aa            linear   PRI 20-NOV-2025
DEFINITION  zeta-sarcoglycan isoform 1 [Homo sapiens].
ACCESSION   NP_631906
VERSION     NP_631906.2
DBSOURCE    REFSEQ: accession NM_139167.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Peall,K.J., Ritz,K., Waite,A.J., Groen,J.L., Morris,H.R., Baas,F.,
            Blake,D.J. and Tijssen,M.A.
  TITLE     SGCZ mutations are unlikely to be associated with myoclonus
            dystonia
  JOURNAL   Neuroscience 272, 88-91 (2014)
   PUBMED   24792710
  REMARK    GeneRIF: No pathogenic SGCZ mutations were identified
REFERENCE   2  (residues 1 to 312)
  AUTHORS   Ikeda,M., Okahisa,Y., Aleksic,B., Won,M., Kondo,N., Naruse,N.,
            Aoyama-Uehara,K., Sora,I., Iyo,M., Hashimoto,R., Kawamura,Y.,
            Nishida,N., Miyagawa,T., Takeda,M., Sasaki,T., Tokunaga,K.,
            Ozaki,N., Ujike,H. and Iwata,N.
  TITLE     Evidence for shared genetic risk between methamphetamine-induced
            psychosis and schizophrenia
  JOURNAL   Neuropsychopharmacology 38 (10), 1864-1870 (2013)
   PUBMED   23594818
REFERENCE   3  (residues 1 to 312)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   4  (residues 1 to 312)
  AUTHORS   Zhao,W., Wineinger,N.E., Tiwari,H.K., Mosley,T.H., Broeckel,U.,
            Arnett,D.K., Kardia,S.L., Kabagambe,E.K. and Sun,Y.V.
  TITLE     Copy number variations associated with obesity-related traits in
            African Americans: a joint analysis between GENOA and HyperGEN
  JOURNAL   Obesity (Silver Spring) 20 (12), 2431-2437 (2012)
   PUBMED   22836685
  REMARK    GeneRIF: three CNVs associated with BMI, obesity, and other
            obesity-related traits after adjusting for multiple testing. These
            CNVs overlap the PARK2, GYPA, and SGCZ genes
REFERENCE   5  (residues 1 to 312)
  AUTHORS   Comuzzie,A.G., Cole,S.A., Laston,S.L., Voruganti,V.S., Haack,K.,
            Gibbs,R.A. and Butte,N.F.
  TITLE     Novel genetic loci identified for the pathophysiology of childhood
            obesity in the Hispanic population
  JOURNAL   PLoS One 7 (12), e51954 (2012)
   PUBMED   23251661
REFERENCE   6  (residues 1 to 312)
  AUTHORS   Pilgram,G.S., Potikanond,S., Baines,R.A., Fradkin,L.G. and
            Noordermeer,J.N.
  TITLE     The roles of the dystrophin-associated glycoprotein complex at the
            synapse
  JOURNAL   Mol Neurobiol 41 (1), 1-21 (2010)
   PUBMED   19899002
  REMARK    Review article
REFERENCE   7  (residues 1 to 312)
  AUTHORS   Aurino,S., Piluso,G., Saccone,V., Cacciottolo,M., D'Amico,F.,
            Dionisi,M., Totaro,A., Belsito,A., Di Vicino,U. and Nigro,V.
  TITLE     Candidate-gene testing for orphan limb-girdle muscular dystrophies
  JOURNAL   Acta Myol 27 (3), 90-97 (2008)
   PUBMED   19472918
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 312)
  AUTHORS   Baulac,S., Gourfinkel-An,I., Couarch,P., Depienne,C., Kaminska,A.,
            Dulac,O., Baulac,M., LeGuern,E. and Nabbout,R.
  TITLE     A novel locus for generalized epilepsy with febrile seizures plus
            in French families
  JOURNAL   Arch Neurol 65 (7), 943-951 (2008)
   PUBMED   18625863
REFERENCE   9  (residues 1 to 312)
  AUTHORS   Anastasi,G., Cutroneo,G., Sidoti,A., Rinaldi,C., Bruschetta,D.,
            Rizzo,G., D'Angelo,R., Tarone,G., Amato,A. and Favaloro,A.
  TITLE     Sarcoglycan subcomplex expression in normal human smooth muscle
  JOURNAL   J Histochem Cytochem 55 (8), 831-843 (2007)
   PUBMED   17438352
REFERENCE   10 (residues 1 to 312)
  AUTHORS   Wheeler,M.T., Zarnegar,S. and McNally,E.M.
  TITLE     Zeta-sarcoglycan, a novel component of the sarcoglycan complex, is
            reduced in muscular dystrophy
  JOURNAL   Hum Mol Genet 11 (18), 2147-2154 (2002)
   PUBMED   12189167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020992.10, AY502063.1,
            AY028700.1, AC023538.7 and AI580904.1.
            
            On May 5, 2006 this sequence version replaced NP_631906.1.
            
            Summary: The zeta-sarcoglycan gene measures over 465 kb and
            localizes to 8p22. This protein is part of the sarcoglycan complex,
            a group of 6 proteins. The sarcoglycans are all N-glycosylated
            transmembrane proteins with a short intra-cellular domain, a single
            transmembrane region and a large extra-cellular domain containing a
            carboxyl-terminal cluster with several conserved cysteine residues.
            The sarcoglycan complex is part of the dystrophin-associated
            glycoprotein complex (DGC), which bridges the inner cytoskeleton
            and the extra-cellular matrix. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY502063.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2155371, SAMN03465402
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000382080.6/ ENSP00000371512.1
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p22"
     Protein         1..312
                     /product="zeta-sarcoglycan isoform 1"
                     /note="zeta-sarcoglycan; zeta-SG"
                     /calculated_mol_wt=34363
     Region          38..299
                     /region_name="Sarcoglycan_1"
                     /note="Sarcoglycan complex subunit protein; pfam04790"
                     /db_xref="CDD:461428"
     CDS             1..312
                     /gene="SGCZ"
                     /gene_synonym="ZSG1"
                     /coded_by="NM_139167.4:809..1747"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5992.2"
                     /db_xref="GeneID:137868"
                     /db_xref="HGNC:HGNC:14075"
                     /db_xref="MIM:608113"
ORIGIN      
        1 mdrstnldie elkmtreqyi latqqnnlpr tenaqlypvg iygwrkrcly ffvllllvtm
       61 ivnlamtiwi lkvmnftvdg mgnlrvtkkg irlegisefl lplyvkeihs rkdsplvlqs
      121 drnvtvnarn hmgqltgqlt igadaveaqc krfevrased grvlfsaded eitigaeklk
      181 vtgtegavfg hsvetphira epsqdlrles ptrslimeap rgvqvsaaag dfkatcrkel
      241 hlqstegeif lnaetiklgn lptgsfssss psssssrqtv yelcvcpngk lylspagvgs
      301 tcqsssnicl ws
//
LOCUS       NP_002807                456 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 12 isoform 1 [Homo
            sapiens].
ACCESSION   NP_002807 XP_947587 XP_951137 XP_951140 XP_951142 XP_951145
            XP_951148 XP_951151
VERSION     NP_002807.1
DBSOURCE    REFSEQ: accession NM_002816.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 456)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 456)
  AUTHORS   Lv,J., Ma,S., Wang,X., Dang,J. and Ma,F.
  TITLE     PSMD12 promotes non-small cell lung cancer progression through
            activating the Nrf2/TrxR1 pathway
  JOURNAL   Genes Genomics 46 (3), 263-277 (2024)
   PUBMED   38243044
  REMARK    GeneRIF: PSMD12 promotes non-small cell lung cancer progression
            through activating the Nrf2/TrxR1 pathway.
REFERENCE   3  (residues 1 to 456)
  AUTHORS   Ma,J., Zhou,W., Yuan,Y., Wang,B. and Meng,X.
  TITLE     PSMD12 interacts with CDKN3 and facilitates pancreatic cancer
            progression
  JOURNAL   Cancer Gene Ther 30 (8), 1072-1083 (2023)
   PUBMED   37037907
  REMARK    GeneRIF: PSMD12 interacts with CDKN3 and facilitates pancreatic
            cancer progression.
REFERENCE   4  (residues 1 to 456)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   5  (residues 1 to 456)
  AUTHORS   Zhang,H., Li,C., Liao,S., Tu,Y., Sun,S., Yao,F., Li,Z. and Wang,Z.
  TITLE     PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer
  JOURNAL   Cancer Biol Ther 23 (1), 1-11 (2022)
   PUBMED   36137220
  REMARK    GeneRIF: PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer.
REFERENCE   6  (residues 1 to 456)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   7  (residues 1 to 456)
  AUTHORS   Saito,A., Watanabe,T.K., Shimada,Y., Fujiwara,T., Slaughter,C.A.,
            DeMartino,G.N., Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p44.5 and p55, two
            regulatory subunits of the 26S proteasome
  JOURNAL   Gene 203 (2), 241-250 (1997)
   PUBMED   9426256
REFERENCE   8  (residues 1 to 456)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 456)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 456)
  AUTHORS   Kanayama,H.O., Tamura,T., Ugai,S., Kagawa,S., Tanahashi,N.,
            Yoshimura,T., Tanaka,K. and Ichihara,A.
  TITLE     Demonstration that a human 26S proteolytic complex consists of a
            proteasome and multiple associated protein components and
            hydrolyzes ATP and ubiquitin-ligated proteins by closely linked
            mechanisms
  JOURNAL   Eur J Biochem 206 (2), 567-578 (1992)
   PUBMED   1317798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC366628.1, BC019062.2,
            AC110921.9 and BU616916.1.
            
            On or before Mar 4, 2006 this sequence version replaced
            XP_951137.1, XP_947587.1, XP_951140.1, XP_951142.1, XP_951145.1,
            XP_951148.1, XP_951151.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. A pseudogene has been
            identified on chromosome 3. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR11853565.13508.1, AK307821.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000356126.8/ ENSP00000348442.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..456
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..456
                     /product="26S proteasome non-ATPase regulatory subunit 12
                     isoform 1"
                     /note="26S proteasome regulatory subunit p55; 26S
                     proteasome regulatory subunit RPN5; proteasome (prosome,
                     macropain) 26S subunit, non-ATPase, 12"
                     /calculated_mol_wt=52774
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:12665801,
                     ECO:0007744|PubMed:19413330; propagated from
                     UniProtKB/Swiss-Prot (O00232.3)"
     Region          14..456
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     Site            221
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00232.3)"
     Site            368
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O00232.3)"
     CDS             1..456
                     /gene="PSMD12"
                     /gene_synonym="p55; Rpn5; STISS"
                     /coded_by="NM_002816.5:59..1429"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS11669.1"
                     /db_xref="GeneID:5718"
                     /db_xref="HGNC:HGNC:9557"
                     /db_xref="MIM:604450"
ORIGIN      
        1 madggserad grivkmevdy satvdqrlpe caklakegrl qevietllsl ekqtrtasdm
       61 vstsrilvav vkmcyeakew dllnenimll skrrsqlkqa vakmvqqcct yveeitdlpi
      121 klrlidtlrm vtegkiyvei erarltktla tikeqngdvk eaasilqelq vetygsmekk
      181 ervefileqm rlclavkdyi rtqiiskkin tkffqeente klklkyynlm iqldqhegsy
      241 lsickhyrai ydtpciqaes ekwqqalksv vlyvilapfd neqsdlvhri sgdkkleeip
      301 kykdllklft tmelmrwstl vedygmelrk gslespatdv fgsteegekr wkdlknrvve
      361 hnirimakyy tritmkrmaq lldlsvdese aflsnlvvnk tifakvdrla giinfqrpkd
      421 pnnllndwsq klnslmslvn ktthliakee mihnlq
//
LOCUS       NP_036392                578 aa            linear   PRI 20-NOV-2025
DEFINITION  2-hydroxyacyl-CoA lyase 1 isoform a [Homo sapiens].
ACCESSION   NP_036392
VERSION     NP_036392.2
DBSOURCE    REFSEQ: accession NM_012260.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 578)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 578)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 578)
  AUTHORS   Kitamura,T., Seki,N. and Kihara,A.
  TITLE     Phytosphingosine degradation pathway includes fatty acid
            alpha-oxidation reactions in the endoplasmic reticulum
  JOURNAL   Proc Natl Acad Sci U S A 114 (13), E2616-E2623 (2017)
   PUBMED   28289220
REFERENCE   4  (residues 1 to 578)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 578)
  AUTHORS   Mezzar,S., de Schryver,E. and Van Veldhoven,P.P.
  TITLE     RP-HPLC-fluorescence analysis of aliphatic aldehydes: application
            to aldehyde-generating enzymes HACL1 and SGPL1
  JOURNAL   J Lipid Res 55 (3), 573-582 (2014)
   PUBMED   24323699
  REMARK    GeneRIF: Data show that a easy assay for 2-hydroxyacyl-CoA lyase
            (HACL1) and sphingosine-1-phosphate lyase (SGPL1) activities was
            developed.
REFERENCE   6  (residues 1 to 578)
  AUTHORS   Ghosh,D. and Berg,J.M.
  TITLE     A proteome-wide perspective on peroxisome targeting signal
            1(PTS1)-Pex5p affinities
  JOURNAL   J Am Chem Soc 132 (11), 3973-3979 (2010)
   PUBMED   20178365
REFERENCE   7  (residues 1 to 578)
  AUTHORS   Wanders,R.J. and Waterham,H.R.
  TITLE     Biochemistry of mammalian peroxisomes revisited
  JOURNAL   Annu Rev Biochem 75, 295-332 (2006)
   PUBMED   16756494
  REMARK    Review article
REFERENCE   8  (residues 1 to 578)
  AUTHORS   Foulon,V., Sniekers,M., Huysmans,E., Asselberghs,S., Mahieu,V.,
            Mannaerts,G.P., Van Veldhoven,P.P. and Casteels,M.
  TITLE     Breakdown of 2-hydroxylated straight chain fatty acids via
            peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the
            alpha-oxidation of straight chain fatty acids
  JOURNAL   J Biol Chem 280 (11), 9802-9812 (2005)
   PUBMED   15644336
  REMARK    GeneRIF: 2-hydroxyphytanoyl-CoA lyase has a role in the breakdown
            of long chain 2-hydroxyfatty acids
REFERENCE   9  (residues 1 to 578)
  AUTHORS   Kikuchi,M., Hatano,N., Yokota,S., Shimozawa,N., Imanaka,T. and
            Taniguchi,H.
  TITLE     Proteomic analysis of rat liver peroxisome: presence of
            peroxisome-specific isozyme of Lon protease
  JOURNAL   J Biol Chem 279 (1), 421-428 (2004)
   PUBMED   14561759
REFERENCE   10 (residues 1 to 578)
  AUTHORS   Foulon,V., Antonenkov,V.D., Croes,K., Waelkens,E., Mannaerts,G.P.,
            Van Veldhoven,P.P. and Casteels,M.
  TITLE     Purification, molecular cloning, and expression of
            2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine
            pyrophosphate-dependent enzyme that catalyzes the carbon-carbon
            bond cleavage during alpha-oxidation of 3-methyl-branched fatty
            acids
  JOURNAL   Proc Natl Acad Sci U S A 96 (18), 10039-10044 (1999)
   PUBMED   10468558
  REMARK    GeneRIF: peroxisomal thiamine-pyrophosphate depending enzyme
            required for the degradation of phytanic acid, catalyzing the
            cleavage of 2-hydroxyphytanoyl-CoA lyase into formyl-CoA and
            pristanal
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA609383.1, BC001627.1, AJ131753.1, AA643224.1 and AC027129.6.
            
            On Apr 20, 2006 this sequence version replaced NP_036392.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.53132.1,
                                           SRR1803616.32893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2152474
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000321169.10/ ENSP00000323811.5
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..578
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p25.1"
     Protein         1..578
                     /product="2-hydroxyacyl-CoA lyase 1 isoform a"
                     /EC_number="4.1.2.63"
                     /note="2-hydroxyphytanol-CoA lyase; phytanoyl-CoA
                     2-hydroxylase 2; 1600020H07Rik; phytanoyl-CoA hydroxylase
                     2; 2-hydroxyphytanoyl-CoA lyase"
                     /calculated_mol_wt=63598
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UJ83.2)"
     Region          7..563
                     /region_name="PRK09259"
                     /note="putative oxalyl-CoA decarboxylase; Validated"
                     /db_xref="CDD:236433"
     Region          401..486
                     /region_name="Thiamine pyrophosphate binding.
                     /evidence=ECO:0000250|UniProtKB:P40149"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ83.2)"
     Region          576..578
                     /region_name="Microbody targeting signal.
                     /evidence=ECO:0000269|PubMed:10468558"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UJ83.2)"
     CDS             1..578
                     /gene="HACL1"
                     /gene_synonym="2-HPCL; HPCL; HPCL2; PHYH2"
                     /coded_by="NM_012260.4:107..1843"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2627.1"
                     /db_xref="GeneID:26061"
                     /db_xref="HGNC:HGNC:17856"
                     /db_xref="MIM:604300"
ORIGIN      
        1 mpdsnfaers eeqvsgakvi aqalktqdve yifgivgipv teiaiaaqql gikyigmrne
       61 qaacyaasai gyltsrpgvc lvvsgpglih alggmananm ncwpllvigg ssernqetmg
      121 afqefpqvea crlytkfsar pssieaipfv iekavrssiy grpgacyvdi padfvnlqvn
      181 vnsikymerc msppismaet savctaasvi rnakqpllii gkgaayahae esikklveqy
      241 klpflptpmg kgvvpdnhpy cvgaarsral qfadvivlfg arlnwilhfg lppryqpdvk
      301 fiqvdicaee lgnnvkpavt llgnihavtk qlleeldktp wqyppeskww ktlrekmksn
      361 eaaskelask kslpmnyytv fyhvqeqlpr dcfvvsegan tmdigrtvlq nylprhrlda
      421 gtfgtmgvgl gfaiaaavva kdrspgqwii cvegdsafgf sgmeveticr ynlpiillvv
      481 nnngiyqgfd tdtwkemlkf qdatavvppm cllpnshyeq vmtafggkgy fvqtpeelqk
      541 slrqsladtt kpslinimie pqatrkaqdf hwltrsnm
//
LOCUS       NP_057211                339 aa            linear   PRI 20-NOV-2025
DEFINITION  store-operated calcium entry-associated regulatory factor isoform 1
            precursor [Homo sapiens].
ACCESSION   NP_057211
VERSION     NP_057211.4
DBSOURCE    REFSEQ: accession NM_016127.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 339)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 339)
  AUTHORS   Dai,Y., Xu,Y., Shen,J., Hu,C., Li,X., Chen,Y., Liu,Y. and Hu,D.
  TITLE     MiR-30a-5p isoform -1|1 promotes the progression of gastric cancer
            by inhibiting TMEM66 and reducing intratumoral cytotoxic T cells
  JOURNAL   Exp Cell Res 439 (2), 114099 (2024)
   PUBMED   38802035
  REMARK    GeneRIF: MiR-30a-5p isoform -1|1 promotes the progression of
            gastric cancer by inhibiting TMEM66 and reducing intratumoral
            cytotoxic T cells.
REFERENCE   3  (residues 1 to 339)
  AUTHORS   Rosado,J.A.
  TITLE     Reduced Ca2+ mobilization in neonatal human platelets involves
            SARAF and pannexin-1
  JOURNAL   Br J Haematol 204 (3), 755-756 (2024)
   PUBMED   38073055
  REMARK    GeneRIF: Reduced Ca[2+] mobilization in neonatal human platelets
            involves SARAF and pannexin-1.
REFERENCE   4  (residues 1 to 339)
  AUTHORS   Zomot,E., Achildiev Cohen,H., Dagan,I., Militsin,R. and Palty,R.
  TITLE     Bidirectional regulation of calcium release-activated calcium
            (CRAC) channel by SARAF
  JOURNAL   J Cell Biol 220 (12) (2021)
   PUBMED   34705029
  REMARK    GeneRIF: Bidirectional regulation of calcium release-activated
            calcium (CRAC) channel by SARAF.
REFERENCE   5  (residues 1 to 339)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 339)
  AUTHORS   Palty,R., Raveh,A., Kaminsky,I., Meller,R. and Reuveny,E.
  TITLE     SARAF inactivates the store operated calcium entry machinery to
            prevent excess calcium refilling
  JOURNAL   Cell 149 (2), 425-438 (2012)
   PUBMED   22464749
  REMARK    GeneRIF: Study shows that SARAF is an endoplasmic reticulum
            resident protein, which responds to cytosolic Ca2+ elevation after
            ER Ca2+ refilling by promoting a slow inactivation process of
            STIM2-dependent basal SOCE activity, as well as STIM1-mediated SOCE
            activity.
REFERENCE   7  (residues 1 to 339)
  AUTHORS   Lodola,F., Laforenza,U., Bonetti,E., Lim,D., Dragoni,S.,
            Bottino,C., Ong,H.L., Guerra,G., Ganini,C., Massa,M., Manzoni,M.,
            Ambudkar,I.S., Genazzani,A.A., Rosti,V., Pedrazzoli,P., Tanzi,F.,
            Moccia,F. and Porta,C.
  TITLE     Store-operated Ca2+ entry is remodelled and controls in vitro
            angiogenesis in endothelial progenitor cells isolated from tumoral
            patients
  JOURNAL   PLoS One 7 (9), e42541 (2012)
   PUBMED   23049731
  REMARK    GeneRIF: Store-operated Ca2+ entry is remodelled and controls in
            vitro angiogenesis in endothelial progenitor cells isolated from
            tumoral patients.
REFERENCE   8  (residues 1 to 339)
  AUTHORS   Zhang,Z. and Henzel,W.J.
  TITLE     Signal peptide prediction based on analysis of experimentally
            verified cleavage sites
  JOURNAL   Protein Sci 13 (10), 2819-2824 (2004)
   PUBMED   15340161
REFERENCE   9  (residues 1 to 339)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
REFERENCE   10 (residues 1 to 339)
  AUTHORS   Chen,J., Sun,M., Lee,S., Zhou,G., Rowley,J.D. and Wang,S.M.
  TITLE     Identifying novel transcripts and novel genes in the human genome
            by using novel SAGE tags
  JOURNAL   Proc Natl Acad Sci U S A 99 (19), 12257-12262 (2002)
   PUBMED   12213963
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC044849.12.
            
            On Feb 9, 2004 this sequence version replaced NP_057211.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.17909.1,
                                           SRR1660809.27298.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000256255.11/ ENSP00000256255.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..339
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p12"
     Protein         1..339
                     /product="store-operated calcium entry-associated
                     regulatory factor isoform 1 precursor"
                     /note="HBV XAg-transactivated protein 3; HBV
                     X-transactivated gene 3 protein; SOCE-associated
                     regulatory factor; transmembrane protein 66; testicular
                     secretory protein Li 59"
                     /calculated_mol_wt=34150
     sig_peptide     1..30
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2843
     Region          24..339
                     /region_name="SARAF"
                     /note="SOCE-associated regulatory factor of calcium
                     homoeostasis; pfam06682"
                     /db_xref="CDD:461985"
     mat_peptide     31..339
                     /product="Store-operated calcium entry-associated
                     regulatory factor. /id=PRO_0000045485"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY9.1)"
                     /calculated_mol_wt=34150
     Site            174..194
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY9.1)"
     Region          318..339
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q96BY9.1)"
     CDS             1..339
                     /gene="SARAF"
                     /gene_synonym="FOAP-7; HSPC035; TMEM66; XTP3"
                     /coded_by="NM_016127.6:116..1135"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS6074.1"
                     /db_xref="GeneID:51669"
                     /db_xref="HGNC:HGNC:28789"
                     /db_xref="MIM:614768"
ORIGIN      
        1 maaacgpgaa gyclllglhl flltagpalg wndpdrmllr dvkaltlhyd ryttsrrldp
       61 ipqlkcvggt agcdsytpkv iqcqnkgwdg ydvqwecktd ldiaykfgkt vvscegyess
      121 edqyvlrgsc gleynldyte lglqklkesg kqhgfasfsd yyykwssads cnmsglitiv
      181 vllgiafvvy klflsdgqys pppyseyppf shryqrftns agppppgfks eftgpqntgh
      241 gatsgfgsaf tgqqgyensg pgfwtglgtg gilgylfgsn raatpfsdsw yypsyppsyp
      301 gtwnrayspl hggsgsysvc snsdtktrta sgyggtrrr
//
LOCUS       NP_036221                738 aa            linear   PRI 20-NOV-2025
DEFINITION  ATP-binding cassette sub-family B member 10, mitochondrial [Homo
            sapiens].
ACCESSION   NP_036221
VERSION     NP_036221.2
DBSOURCE    REFSEQ: accession NM_012089.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Ozdemir,M., Oeljeklaus,S., Schendzielorz,A., Morgenstern,M.,
            Valpadashi,A., Yousefi,R., Warscheid,B. and Dennerlein,S.
  TITLE     Definition of the human mitochondrial TOM interactome reveals TRABD
            as a new interacting protein
  JOURNAL   J Cell Sci 138 (9) (2025)
   PUBMED   40105103
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Do,Y., Yagi,M., Hirai,H., Miki,K., Fukahori,Y., Setoyama,D.,
            Yamamoto,M., Furukawa,T., Kunisaki,Y., Kang,D. and Uchiumi,T.
  TITLE     Cardiomyocyte-specific deletion of the mitochondrial transporter
            Abcb10 causes cardiac dysfunction via lysosomal-mediated
            ferroptosis
  JOURNAL   Biosci Rep 44 (5) (2024)
   PUBMED   38655715
  REMARK    GeneRIF: Cardiomyocyte-specific deletion of the mitochondrial
            transporter Abcb10 causes cardiac dysfunction via
            lysosomal-mediated ferroptosis.
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Miljkovic,M., Seguin,A., Jia,X., Cox,J.E., Catrow,J.L.,
            Bergonia,H., Phillips,J.D., Stephens,W.Z. and Ward,D.M.
  TITLE     Loss of the mitochondrial protein Abcb10 results in altered
            arginine metabolism in MEL and K562 cells and nutrient stress
            signaling through ATF4
  JOURNAL   J Biol Chem 299 (7), 104877 (2023)
   PUBMED   37269954
  REMARK    GeneRIF: Loss of the mitochondrial protein Abcb10 results in
            altered arginine metabolism in MEL and K562 cells and nutrient
            stress signaling through ATF4.
REFERENCE   4  (residues 1 to 738)
  AUTHORS   Cao,S., Yang,Y., He,L., Hang,Y., Yan,X., Shi,H., Wu,J. and
            Ouyang,Z.
  TITLE     Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo
            and biliverdin-bound form
  JOURNAL   Nat Commun 14 (1), 2030 (2023)
   PUBMED   37041204
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 738)
  AUTHORS   Obi,C.D., Dailey,H.A., Jami-Alahmadi,Y., Wohlschlegel,J.A. and
            Medlock,A.E.
  TITLE     Proteomic Analysis of Ferrochelatase Interactome in Erythroid and
            Non-Erythroid Cells
  JOURNAL   Life (Basel) 13 (2), 577 (2023)
   PUBMED   36836934
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 738)
  AUTHORS   Graf,S.A., Haigh,S.E., Corson,E.D. and Shirihai,O.S.
  TITLE     Targeting, import, and dimerization of a mammalian mitochondrial
            ATP binding cassette (ABC) transporter, ABCB10 (ABC-me)
  JOURNAL   J Biol Chem 279 (41), 42954-42963 (2004)
   PUBMED   15215243
  REMARK    GeneRIF: study of ABCB10 targeting, import, and dimerization
REFERENCE   7  (residues 1 to 738)
  AUTHORS   Saito,S., Iida,A., Sekine,A., Miura,Y., Ogawa,C., Kawauchi,S.,
            Higuchi,S. and Nakamura,Y.
  TITLE     Three hundred twenty-six genetic variations in genes encoding nine
            members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the
            Japanese population
  JOURNAL   J Hum Genet 47 (1), 38-50 (2002)
   PUBMED   11829140
REFERENCE   8  (residues 1 to 738)
  AUTHORS   Zhang,F., Hogue,D.L., Liu,L., Fisher,C.L., Hui,D., Childs,S. and
            Ling,V.
  TITLE     M-ABC2, a new human mitochondrial ATP-binding cassette membrane
            protein
  JOURNAL   FEBS Lett 478 (1-2), 89-94 (2000)
   PUBMED   10922475
REFERENCE   9  (residues 1 to 738)
  AUTHORS   Zhang,F., Zhang,W., Liu,L., Fisher,C.L., Hui,D., Childs,S.,
            Dorovini-Zis,K. and Ling,V.
  TITLE     Characterization of ABCB9, an ATP binding cassette protein
            associated with lysosomes
  JOURNAL   J Biol Chem 275 (30), 23287-23294 (2000)
   PUBMED   10748049
REFERENCE   10 (residues 1 to 738)
  AUTHORS   Allikmets,R., Gerrard,B., Glavac,D., Ravnik-Glavac,M.,
            Jenkins,N.A., Gilbert,D.J., Copeland,N.G., Modi,W. and Dean,M.
  TITLE     Characterization and mapping of three new mammalian ATP-binding
            transporter genes from an EST database
  JOURNAL   Mamm Genome 6 (2), 114-117 (1995)
   PUBMED   7766993
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL121990.34, AF216833.1,
            AB013380.1 and BC064930.1.
            
            On Mar 28, 2008 this sequence version replaced NP_036221.1.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters.  ABC proteins transport various molecules across
            extra- and intra-cellular membranes.  ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White).  This protein is a member of the MDR/TAP subfamily.
            Members of the MDR/TAP subfamily are involved in multidrug
            resistance.  The function of this mitochondrial protein is unknown.
            [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB013380.1, AF216833.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000344517.5/
                                                  ENSP00000355637.3
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q42.13"
     Protein         1..738
                     /product="ATP-binding cassette sub-family B member 10,
                     mitochondrial"
                     /note="ATP-binding cassette transporter 10; ABC
                     transporter 10 protein; mitochondrial ATP-binding cassette
                     2; ATP-binding cassette, sub-family B (MDR/TAP), member
                     10; ABC-me protein; ABC-mitochondrial erythroid protein"
                     /calculated_mol_wt=79017
     Region          1..105
                     /region_name="mitochondrial targeting sequence"
     Region          158..734
                     /region_name="MdlB"
                     /note="ABC-type multidrug transport system, ATPase and
                     permease component [Defense mechanisms]; COG1132"
                     /db_xref="CDD:440747"
     Site            169..192
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            214..236
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            265
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            288..310
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            314..333
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            393..416
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     Site            431..452
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NRK6.2)"
     CDS             1..738
                     /gene="ABCB10"
                     /gene_synonym="EST20237; M-ABC2; MTABC2"
                     /coded_by="NM_012089.3:56..2272"
                     /db_xref="CCDS:CCDS1580.1"
                     /db_xref="GeneID:23456"
                     /db_xref="HGNC:HGNC:41"
                     /db_xref="MIM:605454"
ORIGIN      
        1 mrgppawplr lleppspaep grllpvacvw aaasrvpgsl spftglrpar lwgagpallw
       61 gvgaarrwrs gcrgggpgas rgvlglarll glwargpgsc rcgafagpga prlprarfpg
      121 gpaaaawagd eawrrgpaap pgdkgrlrpa aaglpearkl lglayperrr laaavgfltm
      181 ssvismsapf flgkiidviy tnptvdysdn ltrlclglsa vflcgaaana irvylmqtsg
      241 qrivnrlrts lfssilrqev affdktrtge linrlssdta llgrsvtenl sdglragaqa
      301 svgismmffv spnlatfvls vvppvsiiav iygrylrklt kvtqdslaqa tqlaeerign
      361 vrtvrafgke mteiekyask vdhvmqlark eafaragffg atglsgnliv lsvlykggll
      421 mgsahmtvge lssflmyafw vgisigglss fyselmkglg aggrlwelle repklpfneg
      481 vilneksfqg alefknvhfa yparpevpif qdfslsipsg svtalvgpsg sgkstvlsll
      541 lrlydpasgt isldghdirq lnpvwlrski gtvsqepilf scsiaeniay gaddpssvta
      601 eeiqrvaeva navafirnfp qgfntvvgek gvllsggqkq riaiarallk npkillldea
      661 tsaldaeney lvqealdrlm dgrtvlviah rlstiknanm vavldqgkit eygkheells
      721 kpngiyrklm nkqsfisa
//
LOCUS       NP_001308725             933 aa            linear   PRI 20-NOV-2025
DEFINITION  E3 ubiquitin-protein ligase CBL-B isoform g [Homo sapiens].
ACCESSION   NP_001308725
VERSION     NP_001308725.1
DBSOURCE    REFSEQ: accession NM_001321796.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 933)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 933)
  AUTHORS   Jiang,Y., Dai,A., Huang,Y., Li,H., Cui,J., Yang,H., Si,L., Jiao,T.,
            Ren,Z., Zhang,Z., Mou,S., Zhu,H., Guo,W., Huang,Q., Li,Y., Xue,M.,
            Jiang,J., Wang,F., Li,L., Zhong,Q., Wang,K., Liu,B., Wang,J.,
            Fan,G., Guo,J., Chen,L., Workman,C.J., Shen,Z., Kong,Y.,
            Vignali,D.A.A., Xu,C. and Wang,H.
  TITLE     Ligand-induced ubiquitination unleashes LAG3 immune checkpoint
            function by hindering membrane sequestration of signaling motifs
  JOURNAL   Cell 188 (9), 2354-2371 (2025)
   PUBMED   40101708
REFERENCE   3  (residues 1 to 933)
  AUTHORS   Li,X., Sun,W., Huang,M., Gong,L., Zhang,X., Zhong,L., Calderon,V.,
            Bian,Z., He,Y., Suh,W.K., Li,Y., Song,T., Zou,Y., Lian,Z.X. and
            Gu,H.
  TITLE     Deficiency of CBL and CBLB ubiquitin ligases leads to hyper T
            follicular helper cell responses and lupus by reducing BCL6
            degradation
  JOURNAL   Immunity 57 (7), 1603-1617 (2024)
   PUBMED   38761804
  REMARK    GeneRIF: Deficiency of CBL and CBLB ubiquitin ligases leads to
            hyper T follicular helper cell responses and lupus by reducing BCL6
            degradation.
REFERENCE   4  (residues 1 to 933)
  AUTHORS   Li,S., Wan,L., Liu,J., Huang,C., Chen,Y., Cheng,J., Hu,S., Li,F.
            and Zhu,Z.
  TITLE     [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis]
  JOURNAL   Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 40 (2), 106-113 (2024)
   PUBMED   38284251
  REMARK    GeneRIF: [Circular RNA Cbl proto-oncogene B (circCBLB) inhibits
            proliferation, promotes apoptosis, and increases anti-inflammatory
            cytokine levels of fibroblast-like synoviocytes in rheumatoid
            arthritis].
REFERENCE   5  (residues 1 to 933)
  AUTHORS   Wirnsberger,G., Zwolanek,F., Asaoka,T., Kozieradzki,I., Tortola,L.,
            Wimmer,R.A., Kavirayani,A., Fresser,F., Baier,G., Langdon,W.Y.,
            Ikeda,F., Kuchler,K. and Penninger,J.M.
  TITLE     Inhibition of CBLB protects from lethal Candida albicans sepsis
  JOURNAL   Nat Med 22 (8), 915-923 (2016)
   PUBMED   27428901
REFERENCE   6  (residues 1 to 933)
  AUTHORS   Xiao,Y., Tang,J., Guo,H., Zhao,Y., Tang,R., Ouyang,S., Zeng,Q.,
            Rappleye,C.A., Rajaram,M.V., Schlesinger,L.S., Tao,L., Brown,G.D.,
            Langdon,W.Y., Li,B.T. and Zhang,J.
  TITLE     Targeting CBLB as a potential therapeutic approach for disseminated
            candidiasis
  JOURNAL   Nat Med 22 (8), 906-914 (2016)
   PUBMED   27428899
  REMARK    GeneRIF: Silencing CBLB in human monocyte-derived macrophages
            resulted in increased cytokine production and impaired
            down-modulation of dectin-1 and dectin-2 expression after
            C.albicans exposure.
REFERENCE   7  (residues 1 to 933)
  AUTHORS   Liu,Q., Zhou,H., Langdon,W.Y. and Zhang,J.
  TITLE     E3 ubiquitin ligase Cbl-b in innate and adaptive immunity
  JOURNAL   Cell Cycle 13 (12), 1875-1884 (2014)
   PUBMED   24875217
  REMARK    Review article
REFERENCE   8  (residues 1 to 933)
  AUTHORS   Lavagna-Sevenier,C., Marchetto,S., Birnbaum,D. and Rosnet,O.
  TITLE     The CBL-related protein CBLB participates in FLT3 and interleukin-7
            receptor signal transduction in pro-B cells
  JOURNAL   J Biol Chem 273 (24), 14962-14967 (1998)
   PUBMED   9614102
REFERENCE   9  (residues 1 to 933)
  AUTHORS   Bustelo,X.R., Crespo,P., Lopez-Barahona,M., Gutkind,J.S. and
            Barbacid,M.
  TITLE     Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits
            Vav-mediated c-Jun N-terminal kinase activation
  JOURNAL   Oncogene 15 (21), 2511-2520 (1997)
   PUBMED   9399639
REFERENCE   10 (residues 1 to 933)
  AUTHORS   Keane,M.M., Rivero-Lezcano,O.M., Mitchell,J.A., Robbins,K.C. and
            Lipkowitz,S.
  TITLE     Cloning and characterization of cbl-b: a SH3 binding protein with
            homology to the c-cbl proto-oncogene
  JOURNAL   Oncogene 10 (12), 2367-2377 (1995)
   PUBMED   7784085
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC112485.4 and AC016138.8.
            
            Summary: This gene encodes an E3 ubiquitin-protein ligase which
            promotes proteosome-mediated protein degradation by transferring
            ubiquitin from an E2 ubiquitin-conjugating enzyme to a substrate.
            The encoded protein is involved in the regulation of immune
            response by limiting T-cell receptor, B-cell receptor, and high
            affinity immunoglobulin epsilon receptor activation. Studies in
            mouse suggest that this gene is involved in antifungal host defense
            and that its inhibition leads to increased fungal killing.
            Manipulation of this gene may be beneficial in implementing
            immunotherapies for a variety of conditions, including cancer,
            autoimmune diseases, allergies, and infections. [provided by
            RefSeq, Sep 2017].
            
            Transcript Variant: Isoform g is the same length as isoform f but
            differs in the amino acid sequence.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14372080.2091919.1,
                                           SRR14372079.530978.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.11"
     Protein         1..933
                     /product="E3 ubiquitin-protein ligase CBL-B isoform g"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase CBL-B; RING finger
                     protein 56; SH3-binding protein CBL-B; signal transduction
                     protein CBL-B; RING-type E3 ubiquitin transferase CBL-B;
                     Cbl proto-oncogene B, E3 ubiquitin protein ligase; casitas
                     B-lineage lymphoma proto-oncogene b; Cas-Br-M (murine)
                     ecotropic retroviral transforming sequence b; Cbl
                     proto-oncogene, E3 ubiquitin protein ligase B"
                     /calculated_mol_wt=103618
     Region          41..>140
                     /region_name="Cbl_N"
                     /note="CBL proto-oncogene N-terminal domain 1; pfam02262"
                     /db_xref="CDD:426685"
     Region          123..205
                     /region_name="Cbl_N2"
                     /note="CBL proto-oncogene N-terminus, EF hand-like domain;
                     pfam02761"
                     /db_xref="CDD:460681"
     Region          199..295
                     /region_name="SH2_Cbl-b_TKB"
                     /note="Src homology 2 (SH2) domain found in the Cbl-b TKB
                     domain; cd09920"
                     /db_xref="CDD:198176"
     Site            order(217,237,239..242,247,259,261)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198176"
     Site            order(262..265,278..280)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198176"
     Region          302..377
                     /region_name="RING-HC_Cbl-b"
                     /note="RING finger, HC subclass, found in E3
                     ubiquitin-protein ligase Cbl-b and similar proteins;
                     cd16709"
                     /db_xref="CDD:438369"
     Site            order(313..314,317,341,360..363)
                     /site_type="other"
                     /note="ubiquitin binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Site            order(317..319,325..328,347,350..351,354,360..361,363)
                     /site_type="other"
                     /note="E2 binding site [polypeptide binding]"
                     /db_xref="CDD:438369"
     Region          882..922
                     /region_name="UBA_Cbl-b"
                     /note="UBA domain found in E3 ubiquitin-protein ligase
                     Cbl-b and similar proteins; cd14392"
                     /db_xref="CDD:270575"
     Site            order(884..885,887..889,891..892,897,901)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270575"
     CDS             1..933
                     /gene="CBLB"
                     /gene_synonym="ADMIO3; Cbl-b; Nbla00127; RNF56"
                     /coded_by="NM_001321796.2:116..2917"
                     /note="isoform g is encoded by transcript variant 10"
                     /db_xref="GeneID:868"
                     /db_xref="HGNC:HGNC:1542"
                     /db_xref="MIM:604491"
ORIGIN      
        1 mansmngrnp ggrggnprkg rilgiidaiq davgppkqaa adrrtvektw klmdkvvrlc
       61 qnpklqlkns ppyildilpd tyqhlrlils kyddnqklaq lseneyfkiy idslmkkskr
      121 airlfkegke rmyeeqsqdr tivpwkvfrq clhevhqiss gleamalkst idltcndyis
      181 vfefdiftrl fqpwgsilrn wnflavthpg ymafltydev karlqkystk pgsyifrlsc
      241 trlgqwaigy vtgdgnilqt iphnkplfqa lidgsregfy lypdgrsynp dltglceptp
      301 hdhikvtqeq yelycemgst fqlckicaen dkdvkiepcg hlmctsclta wqesdgqgcp
      361 fcrceikgte piivdpfdpr degsrccsii dpfgmpmldl dddddreesl mmnrlanvrk
      421 ctdrqnspvt spgssplaqr rkpqpdplqi phlslppvpp rldliqkgiv rspcgsptgs
      481 pksspcmvrk qdkplpappp plrdpppppp erpppippdn rlsrhihhve svpsrdppmp
      541 leawcprdvf gtnqlvgcrl lgegspkpgi tassnvngrh srvgsdpvlm rkhrrhdlpl
      601 egakvfsngh lgseeydvpp rlsppppvtt llpsikctgp lanslsektr dpveedddey
      661 kipsshpvsl nsqpshchnv kppvrscdng hcmlngthgp ssekksnipd lsiylkgdvf
      721 dsasdpvplp parpptrdnp khgsslnrtp sdydllippl gedafdalpp slppppppar
      781 hsliehskpp gsssrpssgq dlfllpsdpf vdlasgqvpl pparrlpgen vktnrtsqdy
      841 dqlpscsdgs qaparppkpr prrtapeihh rkphgpeaal envdakiakl mgegyafeev
      901 kraleiaqnn vevarsilre fafpppvspr lnl
//
LOCUS       NP_001308534             185 aa            linear   PRI 20-NOV-2025
DEFINITION  sodium channel regulatory subunit beta-1 isoform c [Homo sapiens].
ACCESSION   NP_001308534 XP_005259201
VERSION     NP_001308534.1
DBSOURCE    REFSEQ: accession NM_001321605.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Popa-Fotea,N.M., Oprescu,N., Scafa-Udriste,A. and Micheu,M.M.
  TITLE     Impact of rs1805127 and rs55742440 Variants on Atrial Remodeling in
            Hypertrophic Cardiomyopathy Patients with Atrial Fibrillation: A
            Romanian Cohort Study
  JOURNAL   Int J Mol Sci 24 (24), 17244 (2023)
   PUBMED   38139087
  REMARK    GeneRIF: Impact of rs1805127 and rs55742440 Variants on Atrial
            Remodeling in Hypertrophic Cardiomyopathy Patients with Atrial
            Fibrillation: A Romanian Cohort Study.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Li,Y., Yuan,T., Huang,B., Zhou,F., Peng,C., Li,X., Qiu,Y., Yang,B.,
            Zhao,Y., Huang,Z. and Jiang,D.
  TITLE     Structure of human NaV1.6 channel reveals Na+ selectivity and pore
            blockade by 4,9-anhydro-tetrodotoxin
  JOURNAL   Nat Commun 14 (1), 1030 (2023)
   PUBMED   36823201
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Fan,X., Huang,J., Jin,X. and Yan,N.
  TITLE     Cryo-EM structure of human voltage-gated sodium channel Nav1.6
  JOURNAL   Proc Natl Acad Sci U S A 120 (5), e2220578120 (2023)
   PUBMED   36696443
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Alghamdi,M.A., Al-Eitan,L.N., Asiri,A., Rababa'h,D.M.,
            Alqahtani,S.A., Aldarami,M.S., Alsaeedi,M.A., Almuidh,R.S.,
            Alzahrani,A.A., Sakah,A.H., El Nashar,E.M., Otaif,M.Y. and Abdel
            Ghaffar,N.F.
  TITLE     Association of sodium voltage-gated channel genes polymorphisms
            with epilepsy risk and prognosis in the Saudi population
  JOURNAL   Ann Med 54 (1), 1938-1951 (2022)
   PUBMED   35801810
  REMARK    GeneRIF: Association of sodium voltage-gated channel genes
            polymorphisms with epilepsy risk and prognosis in the Saudi
            population.
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Qin,N., D'Andrea,M.R., Lubin,M.L., Shafaee,N., Codd,E.E. and
            Correa,A.M.
  TITLE     Molecular cloning and functional expression of the human sodium
            channel beta1B subunit, a novel splicing variant of the beta1
            subunit
  JOURNAL   Eur J Biochem 270 (23), 4762-4770 (2003)
   PUBMED   14622265
  REMARK    GeneRIF: identification and characterization of a novel splicing
            variant; functional studies in oocytes demonstrate that the beta1B
            subunit increases the ionic current when coexpressed with the
            tetrodotoxin sensitive channel, NaV1.2
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Makita,N., Sloan-Brown,K., Weghuis,D.O., Ropers,H.H. and
            George,A.L. Jr.
  TITLE     Genomic organization and chromosomal assignment of the human
            voltage-gated Na+ channel beta 1 subunit gene (SCN1B)
  JOURNAL   Genomics 23 (3), 628-634 (1994)
   PUBMED   7851891
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Makita,N., Bennett,P.B. Jr. and George,A.L. Jr.
  TITLE     Voltage-gated Na+ channel beta 1 subunit mRNA expressed in adult
            human skeletal muscle, heart, and brain is encoded by a single gene
  JOURNAL   J Biol Chem 269 (10), 7571-7578 (1994)
   PUBMED   8125980
REFERENCE   8  (residues 1 to 185)
  AUTHORS   McClatchey,A.I., Cannon,S.C., Slaugenhaupt,S.A. and Gusella,J.F.
  TITLE     The cloning and expression of a sodium channel beta 1-subunit cDNA
            from human brain
  JOURNAL   Hum Mol Genet 2 (6), 745-749 (1993)
   PUBMED   8394762
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Brugada,R., Campuzano,O., Sarquella-Brugada,G., Brugada,P.,
            Brugada,J. and Hong,K.
  TITLE     Brugada Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301690
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Hartshorne,R.P. and Catterall,W.A.
  TITLE     The sodium channel from rat brain. Purification and subunit
            composition
  JOURNAL   J Biol Chem 259 (3), 1667-1675 (1984)
   PUBMED   6319405
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC020907.6, DA062026.1 and
            BC067122.1.
            
            On Mar 29, 2016 this sequence version replaced XP_005259201.1.
            
            Summary: Voltage-gated sodium channels are heteromeric proteins
            that function in the generation and propagation of action
            potentials in muscle and neuronal cells. They are composed of one
            alpha and two beta subunits, where the alpha subunit provides
            channel activity and the beta-1 subunit modulates the kinetics of
            channel inactivation. This gene encodes a sodium channel beta-1
            subunit. Mutations in this gene result in generalized epilepsy with
            febrile seizures plus, Brugada syndrome 5, and defects in cardiac
            conduction. Multiple transcript variants encoding different
            isoforms have been found for this gene.[provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (c) encodes an isoform (c) that
            lacks a predicted signal peptide compared to isoforms a and b.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.288786.1,
                                           SRR3476690.535438.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2145313
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.11"
     Protein         1..185
                     /product="sodium channel regulatory subunit beta-1 isoform
                     c"
                     /note="sodium channel subunit beta-1; sodium channel,
                     voltage-gated, type I, beta; sodium channel, voltage
                     gated, type I beta subunit; sodium channel regulatory
                     subunit beta-1"
                     /calculated_mol_wt=21366
     Region          8..114
                     /region_name="V-set"
                     /note="Immunoglobulin V-set domain; pfam07686"
                     /db_xref="CDD:462230"
     CDS             1..185
                     /gene="SCN1B"
                     /gene_synonym="ATFB13; BRGDA5; DEE52; EIEE52; GEFSP1"
                     /coded_by="NM_001321605.2:570..1127"
                     /note="isoform c is encoded by transcript variant c"
                     /db_xref="CCDS:CCDS86744.1"
                     /db_xref="GeneID:6324"
                     /db_xref="HGNC:HGNC:10586"
                     /db_xref="MIM:600235"
ORIGIN      
        1 mtfkilcisc krrsetnaet ftewtfrqkg teefvkilry enevlqleed erfegrvvwn
       61 gsrgtkdlqd lsifitnvty nhsgdyechv yrllffenye hntsvvkkih ievvdkanrd
      121 masivseimm yvlivvltiw lvaemiycyk kiaaatetaa qenaseylai tseskenctg
      181 vqvae
//
LOCUS       NP_001307601             429 aa            linear   PRI 20-NOV-2025
DEFINITION  runt-related transcription factor 3 isoform 1 [Homo sapiens].
ACCESSION   NP_001307601
VERSION     NP_001307601.1
DBSOURCE    REFSEQ: accession NM_001320672.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 429)
  AUTHORS   Samsa,W.E., Zhang,Z. and Gong,Z.
  TITLE     CBFbeta Regulates RUNX3 ADP-Ribosylation to Mediate Homologous
            Recombination Repair
  JOURNAL   J Cell Physiol 240 (1), e31503 (2025)
   PUBMED   39696918
REFERENCE   2  (residues 1 to 429)
  AUTHORS   Wang,J., Wang,J., Zhang,J., Gong,H., Li,J., Song,Y., Huang,Y.,
            Ma,B., Gu,W. and Yang,R.
  TITLE     Association between the methylations of RUNX3 in peripheral blood
            and lung cancer: a case-control study
  JOURNAL   Biomarkers 29 (6), 343-351 (2024)
   PUBMED   38923933
  REMARK    GeneRIF: Association between the methylations of RUNX3 in
            peripheral blood and lung cancer: a case-control study.
REFERENCE   3  (residues 1 to 429)
  AUTHORS   Zhao,B., Xia,Z., Yang,B., Guo,Y., Zhou,R., Gu,M., Liu,M., Li,Q.,
            Bai,W., Huang,J., Zhang,X., Zhu,C., Leung,K.T., Chen,C. and Dong,J.
  TITLE     USP7 promotes IgA class switching through stabilizing RUNX3 for
            germline transcription activation
  JOURNAL   Cell Rep 43 (5), 114194 (2024)
   PUBMED   38735043
  REMARK    GeneRIF: USP7 promotes IgA class switching through stabilizing
            RUNX3 for germline transcription activation.
            Erratum:[Cell Rep. 2024 Jun 25;43(6):114315. doi:
            10.1016/j.celrep.2024.114315. PMID: 38795349]
REFERENCE   4  (residues 1 to 429)
  AUTHORS   Wang,N., Miao,X., Lu,W., Ji,Y., Zheng,Y., Meng,D., Liu,H. and
            Xiang,C.
  TITLE     RUNX3 exerts tumor-suppressive role through inhibiting EXOSC4
            expression
  JOURNAL   Funct Integr Genomics 24 (3), 103 (2024)
   PUBMED   38913281
  REMARK    GeneRIF: RUNX3 exerts tumor-suppressive role through inhibiting
            EXOSC4 expression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 429)
  AUTHORS   Zheng,G., Ye,H., Bai,J. and Zhang,X.
  TITLE     Downregulation of lncRNA MIR17HG reduced tumorigenicity and
            Treg-mediated immune escape of non-small-cell lung cancer cells
            through targeting the miR-17-5p/RUNX3 axis
  JOURNAL   J Biochem Mol Toxicol 38 (5), e23715 (2024)
   PUBMED   38704830
  REMARK    GeneRIF: Downregulation of lncRNA MIR17HG reduced tumorigenicity
            and Treg-mediated immune escape of non-small-cell lung cancer cells
            through targeting the miR-17-5p/RUNX3 axis.
REFERENCE   6  (residues 1 to 429)
  AUTHORS   Levanon,D., Goldstein,R.E., Bernstein,Y., Tang,H., Goldenberg,D.,
            Stifani,S., Paroush,Z. and Groner,Y.
  TITLE     Transcriptional repression by AML1 and LEF-1 is mediated by the
            TLE/Groucho corepressors
  JOURNAL   Proc Natl Acad Sci U S A 95 (20), 11590-11595 (1998)
   PUBMED   9751710
REFERENCE   7  (residues 1 to 429)
  AUTHORS   Bae,S.C., Takahashi,E., Zhang,Y.W., Ogawa,E., Shigesada,K.,
            Namba,Y., Satake,M. and Ito,Y.
  TITLE     Cloning, mapping and expression of PEBP2 alpha C, a third gene
            encoding the mammalian Runt domain
  JOURNAL   Gene 159 (2), 245-248 (1995)
   PUBMED   7622058
REFERENCE   8  (residues 1 to 429)
  AUTHORS   Wijmenga,C., Speck,N.A., Dracopoli,N.C., Hofker,M.H., Liu,P. and
            Collins,F.S.
  TITLE     Identification of a new murine runt domain-containing gene, Cbfa3,
            and localization of the human homolog, CBFA3, to chromosome
            1p35-pter
  JOURNAL   Genomics 26 (3), 611-614 (1995)
   PUBMED   7607690
REFERENCE   9  (residues 1 to 429)
  AUTHORS   Levanon,D., Negreanu,V., Bernstein,Y., Bar-Am,I., Avivi,L. and
            Groner,Y.
  TITLE     AML1, AML2, and AML3, the human members of the runt domain
            gene-family: cDNA structure, expression, and chromosomal
            localization
  JOURNAL   Genomics 23 (2), 425-432 (1994)
   PUBMED   7835892
REFERENCE   10 (residues 1 to 429)
  AUTHORS   Bae,S.C., Yamaguchi-Iwai,Y., Ogawa,E., Maruyama,M., Inuzuka,M.,
            Kagoshima,H., Shigesada,K., Satake,M. and Ito,Y.
  TITLE     Isolation of PEBP2 alpha B cDNA representing the mouse homolog of
            human acute myeloid leukemia gene, AML1
  JOURNAL   Oncogene 8 (3), 809-814 (1993)
   PUBMED   8437866
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL445471.13, BC013362.2 and
            AL023096.1.
            
            Summary: This gene encodes a member of the runt domain-containing
            family of transcription factors. A heterodimer of this protein and
            a beta subunit forms a complex that binds to the core DNA sequence
            5'-PYGPYGGT-3' found in a number of enhancers and promoters, and
            can either activate or suppress transcription. It also interacts
            with other transcription factors. It functions as a tumor
            suppressor, and the gene is frequently deleted or transcriptionally
            silenced in cancer. Alternative splicing results in multiple
            transcript variants. [provided by RefSeq, Mar 2016].
            
            Transcript Variant: This variant (3) differs in the 5' UTR compared
            to variant 1. Variants 1 and 3 encode the same protein.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC013362.2 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMN03465409
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..429
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..429
                     /product="runt-related transcription factor 3 isoform 1"
                     /note="core-binding factor, runt domain, alpha subunit 3;
                     transcription factor AML2; acute myeloid leukemia gene 2;
                     polyomavirus enhancer-binding protein 2 alpha C subunit;
                     PEA2 alpha C; PEBP2 alpha C; CBF-alpha-3; oncogene AML-2;
                     acute myeloid leukemia 2 protein; core-binding factor
                     subunit alpha-3; SL3-3 enhancer factor 1 alpha C subunit;
                     SL3/AKV core-binding factor alpha C subunit; runt related
                     transcription factor 3"
                     /calculated_mol_wt=45791
     Region          69..197
                     /region_name="Runt"
                     /note="Runt domain; pfam00853"
                     /db_xref="CDD:459963"
     Region          <191..325
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          330..429
                     /region_name="RunxI"
                     /note="Runx inhibition domain; pfam08504"
                     /db_xref="CDD:430037"
     CDS             1..429
                     /gene="RUNX3"
                     /gene_synonym="AML2; CBFA3; PEBP2aC"
                     /coded_by="NM_001320672.1:273..1562"
                     /note="isoform 1 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS30633.1"
                     /db_xref="GeneID:864"
                     /db_xref="HGNC:HGNC:10473"
                     /db_xref="MIM:600210"
ORIGIN      
        1 masnsifdsf ptysptfird pstsrrftpp spafpcgggg gkmgensgal saqaavgpgg
       61 rarpevrsmv dvladhagel vrtdspnflc svlpshwrcn ktlpvafkvv algdvpdgtv
      121 vtvmagnden ysaelrnasa vmknqvarfn dlrfvgrsgr gksftltitv ftnptqvaty
      181 hraikvtvdg preprrhrqk ledqtkpfpd rfgdlerlrm rvtpstpspr gslsttshfs
      241 sqpqtpiqgt selnpfsdpr qfdrsfptlp tltesrfpdp rmhypgamsa afpysatpsg
      301 tsisslsvag mpatsrfhht ylpppypgap qnqsgpfqan pspyhlyygt ssgsyqfsmv
      361 agsssggdrs ptrmlascts saasvaagnl mnpslggqsd gveadgshsn sptalstpgr
      421 mdeavwrpy
//
LOCUS       NP_036448                536 aa            linear   PRI 20-NOV-2025
DEFINITION  importin subunit alpha-7 [Homo sapiens].
ACCESSION   NP_036448
VERSION     NP_036448.1
DBSOURCE    REFSEQ: accession NM_012316.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 536)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 536)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 536)
  AUTHORS   Yu,M., Sun,L., Zhang,Z., Zhang,Y., Zhang,H., Na,L. and Wang,X.
  TITLE     KPNA6 is a Cofactor of ANP32A/B in Supporting Influenza Virus
            Polymerase Activity
  JOURNAL   Microbiol Spectr 10 (1), e0207321 (2022)
   PUBMED   35044222
  REMARK    GeneRIF: KPNA6 is a Cofactor of ANP32A/B in Supporting Influenza
            Virus Polymerase Activity.
REFERENCE   4  (residues 1 to 536)
  AUTHORS   Tsimbalyuk,S., Donnelly,C.M. and Forwood,J.K.
  TITLE     Structural characterization of human importin alpha 7 in its
            cargo-free form at 2.5 A resolution
  JOURNAL   Sci Rep 12 (1), 315 (2022)
   PUBMED   35013395
  REMARK    GeneRIF: Structural characterization of human importin alpha 7 in
            its cargo-free form at 2.5 A resolution.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 536)
  AUTHORS   Zhang,Q., Chen,Z., Huang,C., Sun,J., Xue,M., Feng,T., Pan,W.,
            Wang,K. and Dai,J.
  TITLE     Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2)
            Membrane (M) and Spike (S) Proteins Antagonize Host Type I
            Interferon Response
  JOURNAL   Front Cell Infect Microbiol 11, 766922 (2021)
   PUBMED   34950606
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 536)
  AUTHORS   Di Marzio,P., Choe,S., Ebright,M., Knoblauch,R. and Landau,N.R.
  TITLE     Mutational analysis of cell cycle arrest, nuclear localization and
            virion packaging of human immunodeficiency virus type 1 Vpr
  JOURNAL   J Virol 69 (12), 7909-7916 (1995)
   PUBMED   7494303
REFERENCE   7  (residues 1 to 536)
  AUTHORS   Gallay,P., Swingler,S., Song,J., Bushman,F. and Trono,D.
  TITLE     HIV nuclear import is governed by the phosphotyrosine-mediated
            binding of matrix to the core domain of integrase
  JOURNAL   Cell 83 (4), 569-576 (1995)
   PUBMED   7585960
REFERENCE   8  (residues 1 to 536)
  AUTHORS   Freed,E.O., Englund,G. and Martin,M.A.
  TITLE     Role of the basic domain of human immunodeficiency virus type 1
            matrix in macrophage infection
  JOURNAL   J Virol 69 (6), 3949-3954 (1995)
   PUBMED   7745752
REFERENCE   9  (residues 1 to 536)
  AUTHORS   Bukrinsky,M.I., Sharova,N., Dempsey,M.P., Stanwick,T.L.,
            Bukrinskaya,A.G., Haggerty,S. and Stevenson,M.
  TITLE     Active nuclear import of human immunodeficiency virus type 1
            preintegration complexes
  JOURNAL   Proc Natl Acad Sci U S A 89 (14), 6580-6584 (1992)
   PUBMED   1631159
REFERENCE   10 (residues 1 to 536)
  AUTHORS   Sharova,N. and Bukrinskaya,A.
  TITLE     p17 and p17-containing gag precursors of input human
            immunodeficiency virus are transported into the nuclei of infected
            cells
  JOURNAL   AIDS Res Hum Retroviruses 7 (3), 303-306 (1991)
   PUBMED   2064827
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP374991.1, BC020520.1 and
            AL049795.21.
            
            Summary: Nucleocytoplasmic transport, a signal- and
            energy-dependent process, takes place through nuclear pore
            complexes embedded in the nuclear envelope. The import of proteins
            containing a nuclear localization signal (NLS) requires the NLS
            import receptor, a heterodimer of importin alpha and beta subunits
            also known as karyopherins. Importin alpha binds the NLS-containing
            cargo in the cytoplasm and importin beta docks the complex at the
            cytoplasmic side of the nuclear pore complex. In the presence of
            nucleoside triphosphates and the small GTP binding protein Ran, the
            complex moves into the nuclear pore complex and the importin
            subunits dissociate. Importin alpha enters the nucleoplasm with its
            passenger protein and importin beta remains at the pore. The
            protein encoded by this gene is a member of the importin alpha
            family. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK002111.1, BC020520.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373625.8/ ENSP00000362728.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..536
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2"
     Protein         1..536
                     /product="importin subunit alpha-7"
                     /note="importin-alpha-S2; importin alpha 7 subunit;
                     karyopherin alpha 6 (importin alpha 7)"
                     /calculated_mol_wt=59899
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          36..525
                     /region_name="SRP1"
                     /note="Karyopherin (importin) alpha [Intracellular
                     trafficking and secretion]; COG5064"
                     /db_xref="CDD:227396"
     Region          45..54
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          76..115
                     /region_name="ARM 1, truncated"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Site            113
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O60684.1)"
     Region          116..159
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          126..152
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(143,147,151,185,189,193,228,232,236)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          147..239
                     /region_name="NLS binding site (major).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          160..196
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          202..237
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          205..243
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          244..288
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          254..279
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(270,274,278,312,316,320,354,358,362)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          287..323
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          289..328
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          316..404
                     /region_name="NLS binding site (minor).
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          329..363
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          371..410
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          371..407
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          411..453
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     Region          414..448
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          457..502
                     /region_name="ARM 10, atypical"
                     /note="propagated from UniProtKB/Swiss-Prot (O60684.1)"
     CDS             1..536
                     /gene="KPNA6"
                     /gene_synonym="IPOA7"
                     /coded_by="NM_012316.5:76..1686"
                     /db_xref="CCDS:CCDS352.1"
                     /db_xref="GeneID:23633"
                     /db_xref="HGNC:HGNC:6399"
                     /db_xref="MIM:610563"
ORIGIN      
        1 metmaspgkd nyrmksyknn alnpeemrrr reeegiqlrk qkreqqlfkr rnvelineea
       61 amfdsllmds yvssttgesv itremvemlf sddsdlqlat tqkfrkllsk epsppidevi
      121 ntprvvdrfv eflkrnenct lqfeaawalt niasgtsqqt kivieagavp ifiellnsdf
      181 edvqeqavwa lgniagdssv crdyvlncsi lnplltlltk strltmtrna vwalsnlcrg
      241 knpppefakv spclpvlsrl lfssdsdlla dacwalsyls dgpnekiqav idsgvcrrlv
      301 ellmhndykv aspalravgn ivtgddiqtq vilncsalpc llhllsspke sirkeacwti
      361 snitagnraq iqavidanif pvlieilqka efrtrkeaaw aitnatsggt peqirylvsl
      421 gcikplcdll tvmdskivqv alnglenilr lgeqegkrsg sgvnpycgli eeaygldkie
      481 flqshenqei yqkafdlieh yfgvedddss lapqvdetqq qfifqqpeap megfql
//
LOCUS       NP_001290341             276 aa            linear   PRI 20-NOV-2025
DEFINITION  regulation of nuclear pre-mRNA domain-containing protein 1A isoform
            2 [Homo sapiens].
ACCESSION   NP_001290341
VERSION     NP_001290341.1
DBSOURCE    REFSEQ: accession NM_001303412.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 276)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 276)
  AUTHORS   Feng,X., Jiang,T., Yang,C., Pang,S., Ding,Z., Hu,H., Wang,H.,
            Dong,L. and Yang,N.
  TITLE     RPRD1A stabilizes NRF2 and aggravates HCC progression through
            competing with p62 for TRIM21 binding
  JOURNAL   Cell Death Dis 13 (1), 6 (2021)
   PUBMED   34921137
  REMARK    GeneRIF: RPRD1A stabilizes NRF2 and aggravates HCC progression
            through competing with p62 for TRIM21 binding.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 276)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 276)
  AUTHORS   Zouboulis,C.C., Nogueira da Costa,A., Fimmel,S. and Zouboulis,K.C.
  TITLE     Apocrine glands are bystanders in hidradenitis suppurativa and
            their involvement is gender specific
  JOURNAL   J Eur Acad Dermatol Venereol 34 (7), 1555-1563 (2020)
   PUBMED   32031713
REFERENCE   5  (residues 1 to 276)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 276)
  AUTHORS   Behr,E.R., Ritchie,M.D., Tanaka,T., Kaab,S., Crawford,D.C.,
            Nicoletti,P., Floratos,A., Sinner,M.F., Kannankeril,P.J.,
            Wilde,A.A., Bezzina,C.R., Schulze-Bahr,E., Zumhagen,S.,
            Guicheney,P., Bishopric,N.H., Marshall,V., Shakir,S.,
            Dalageorgou,C., Bevan,S., Jamshidi,Y., Bastiaenen,R.,
            Myerburg,R.J., Schott,J.J., Camm,A.J., Steinbeck,G., Norris,K.,
            Altman,R.B., Tatonetti,N.P., Jeffery,S., Kubo,M., Nakamura,Y.,
            Shen,Y., George,A.L. Jr. and Roden,D.M.
  TITLE     Genome wide analysis of drug-induced torsades de pointes: lack of
            common variants with large effect sizes
  JOURNAL   PLoS One 8 (11), e78511 (2013)
   PUBMED   24223155
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 276)
  AUTHORS   Zhang,X., Cao,Q., Liu,X., Liu,S., Wang,J., Sun,S., Wang,O.,
            Tian,Z., Liu,H., Kuang,J. and Zhang,W.
  TITLE     Cellular and molecular evidence for malignancy-inhibitory functions
            of p15RS
  JOURNAL   Cell Cycle 11 (10), 1988-1998 (2012)
   PUBMED   22580456
  REMARK    GeneRIF: The p15RS expression specifically downregulates the
            expression of cathepsin B and MMP-9 at RNA levels, which are known
            to promote cell invasion through degrading extracellular matrix
            proteins.
REFERENCE   8  (residues 1 to 276)
  AUTHORS   Ni,Z., Olsen,J.B., Guo,X., Zhong,G., Ruan,E.D., Marcon,E.,
            Young,P., Guo,H., Li,J., Moffat,J., Emili,A. and Greenblatt,J.F.
  TITLE     Control of the RNA polymerase II phosphorylation state in promoter
            regions by CTD interaction domain-containing proteins RPRD1A and
            RPRD1B
  JOURNAL   Transcription 2 (5), 237-242 (2011)
   PUBMED   22231121
REFERENCE   9  (residues 1 to 276)
  AUTHORS   Wu,Y., Zhang,Y., Zhang,H., Yang,X., Wang,Y., Ren,F., Liu,H.,
            Zhai,Y., Jia,B., Yu,J. and Chang,Z.
  TITLE     p15RS attenuates Wnt/{beta}-catenin signaling by disrupting
            {beta}-catenin.TCF4 Interaction
  JOURNAL   J Biol Chem 285 (45), 34621-34631 (2010)
   PUBMED   20739273
  REMARK    GeneRIF: p15RS inhibits Wnt signaling by interrupting
            beta-catenin.TCF4 complex formation and that Wnt signaling
            initiates downstream gene expression by removing p15RS from
            promoters.
REFERENCE   10 (residues 1 to 276)
  AUTHORS   Liu,J., Liu,H., Zhang,X., Gao,P., Wang,J. and Hu,Z.
  TITLE     Identification and characterization of P15RS, a novel P15(INK4b)
            related gene on G1/S progression
  JOURNAL   Biochem Biophys Res Commun 299 (5), 880-885 (2002)
   PUBMED   12470661
  REMARK    GeneRIF: molecular cloning and characterization of P15RS, a novel
            P15(INK4b) related gene involved in G1/S progression
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB444937.1, BG325568.1 and
            BC000225.1.
            
            Summary: This gene encodes a cell-cycle and transcription
            regulatory protein. The encoded protein interacts with the cell
            cycle inhibitor cyclin-dependent kinase 4 inhibitor B and may
            function as a negative regulator of G(1)/S phase progression. This
            protein also forms homo- and hetrodimers with the protein,
            regulation of nuclear pre-mRNA domain-containing protein 1B, to
            form a scaffold that interacts with the C-terminal domain of RNA
            polymerase II subunit B1 and regulates several aspects of
            transcription. Alternate splicing results in multiple transcript
            variants. A pseudogene of this gene is found on chromosome 16.
            [provided by RefSeq, Dec 2014].
            
            Transcript Variant: This variant (3) uses an alternate exon in the
            5' UTR and 5' coding region uses an alternate splice site in the 3'
            UTR. These differences result in the use of an alternate start
            codon compared to variant 1. The encoded isoform (2) is shorter and
            has a distinct N_terminus compared to isoform 1. Variant 2 and 3
            encode the same isoform (2).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC000225.1, SRR1660805.199384.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..276
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..276
                     /product="regulation of nuclear pre-mRNA domain-containing
                     protein 1A isoform 2"
                     /note="regulation of nuclear pre-mRNA domain-containing
                     protein 1A; cyclin-dependent kinase 2B-inhibitor-related
                     protein; p15INK4B-related protein; CDKN2B-related protein;
                     Cyclin-dependent kinase inhibitor 2B-related protein
                     (p15INK4B-related protein)"
                     /calculated_mol_wt=31494
     Region          <15..95
                     /region_name="VHS_ENTH_ANTH"
                     /note="VHS, ENTH and ANTH domain superfamily; cl02544"
                     /db_xref="CDD:470608"
     Region          129..274
                     /region_name="CREPT"
                     /note="Cell-cycle alteration and expression-elevated
                     protein in tumour; pfam16566"
                     /db_xref="CDD:465181"
     CDS             1..276
                     /gene="RPRD1A"
                     /gene_synonym="HsT3101; P15RS"
                     /coded_by="NM_001303412.2:323..1153"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS77178.1"
                     /db_xref="GeneID:55197"
                     /db_xref="HGNC:HGNC:25560"
                     /db_xref="MIM:610347"
ORIGIN      
        1 mrnsnwrfcq tgiyskpnrk ltflylandv iqnskrkgpe ftkdfapviv eafkhvsset
       61 desckkhlgr vlsiweersv yendvleqlk qalygdkkpr krtyeqikvd enencsslgs
      121 pseppqtldl vralqdlena asgdaavhqr iaslpvevqe vslldkitdk esgerlskmv
      181 edacmllady ngrlaaeidd rkqltrmlad flrcqkeala ekehkleeyk rklarvslvr
      241 kelrsriqsl pdlsrlpnvt gshmhlpfag diysed
//
LOCUS       NP_001294861             185 aa            linear   PRI 20-NOV-2025
DEFINITION  COMM domain-containing protein 9 isoform 3 [Homo sapiens].
ACCESSION   NP_001294861 XP_011518335
VERSION     NP_001294861.1
DBSOURCE    REFSEQ: accession NM_001307932.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 185)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 185)
  AUTHORS   Singla,A., Rogers,C., Touma,M.J., El-Najjar,Y., Colley,A.,
            Boesch,D.J., Billadeau,D.D., Gecz,J., Chen,B. and Burstein,E.
  TITLE     CCDC22 mutations that impair COMMD binding cause attenuated
            3C/Ritscher-Schinzel syndrome
  JOURNAL   BMC Med Genomics 18 (1), 98 (2025)
   PUBMED   40448120
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 185)
  AUTHORS   Healy,M.D., McNally,K.E., Butkovic,R., Chilton,M., Kato,K.,
            Sacharz,J., McConville,C., Moody,E.R.R., Shaw,S.,
            Planelles-Herrero,V.J., Yadav,S.K.N., Ross,J., Borucu,U.,
            Palmer,C.S., Chen,K.E., Croll,T.I., Hall,R.J., Caruana,N.J.,
            Ghai,R., Nguyen,T.H.D., Heesom,K.J., Saitoh,S., Berger,I.,
            Schaffitzel,C., Williams,T.A., Stroud,D.A., Derivery,E.,
            Collins,B.M. and Cullen,P.J.
  TITLE     Structure of the endosomal Commander complex linked to
            Ritscher-Schinzel syndrome
  JOURNAL   Cell 186 (10), 2219-2237 (2023)
   PUBMED   37172566
REFERENCE   4  (residues 1 to 185)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 185)
  AUTHORS   Laulumaa,S. and Varjosalo,M.
  TITLE     Commander Complex-A Multifaceted Operator in Intracellular
            Signaling and Cargo
  JOURNAL   Cells 10 (12), 3447 (2021)
   PUBMED   34943955
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 185)
  AUTHORS   Hein,M.Y., Hubner,N.C., Poser,I., Cox,J., Nagaraj,N., Toyoda,Y.,
            Gak,I.A., Weisswange,I., Mansfeld,J., Buchholz,F., Hyman,A.A. and
            Mann,M.
  TITLE     A human interactome in three quantitative dimensions organized by
            stoichiometries and abundances
  JOURNAL   Cell 163 (3), 712-723 (2015)
   PUBMED   26496610
REFERENCE   7  (residues 1 to 185)
  AUTHORS   Phillips-Krawczak,C.A., Singla,A., Starokadomskyy,P., Deng,Z.,
            Osborne,D.G., Li,H., Dick,C.J., Gomez,T.S., Koenecke,M.,
            Zhang,J.S., Dai,H., Sifuentes-Dominguez,L.F., Geng,L.N.,
            Kaufmann,S.H., Hein,M.Y., Wallis,M., McGaughran,J., Gecz,J.,
            Sluis,Bv., Billadeau,D.D. and Burstein,E.
  TITLE     COMMD1 is linked to the WASH complex and regulates endosomal
            trafficking of the copper transporter ATP7A
  JOURNAL   Mol Biol Cell 26 (1), 91-103 (2015)
   PUBMED   25355947
REFERENCE   8  (residues 1 to 185)
  AUTHORS   Starokadomskyy,P., Gluck,N., Li,H., Chen,B., Wallis,M., Maine,G.N.,
            Mao,X., Zaidi,I.W., Hein,M.Y., McDonald,F.J., Lenzner,S., Zecha,A.,
            Ropers,H.H., Kuss,A.W., McGaughran,J., Gecz,J. and Burstein,E.
  TITLE     CCDC22 deficiency in humans blunts activation of proinflammatory
            NF-kappaB signaling
  JOURNAL   J Clin Invest 123 (5), 2244-2256 (2013)
   PUBMED   23563313
REFERENCE   9  (residues 1 to 185)
  AUTHORS   Mao,X., Gluck,N., Chen,B., Starokadomskyy,P., Li,H., Maine,G.N. and
            Burstein,E.
  TITLE     COMMD1 (copper metabolism MURR1 domain-containing protein 1)
            regulates Cullin RING ligases by preventing CAND1
            (Cullin-associated Nedd8-dissociated protein 1) binding
  JOURNAL   J Biol Chem 286 (37), 32355-32365 (2011)
   PUBMED   21778237
REFERENCE   10 (residues 1 to 185)
  AUTHORS   Burstein,E., Hoberg,J.E., Wilkinson,A.S., Rumble,J.M., Csomos,R.A.,
            Komarck,C.M., Maine,G.N., Wilkinson,J.C., Mayo,M.W. and
            Duckett,C.S.
  TITLE     COMMD proteins, a novel family of structural and functional
            homologs of MURR1
  JOURNAL   J Biol Chem 280 (23), 22222-22232 (2005)
   PUBMED   15799966
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC087277.11.
            
            On Apr 17, 2015 this sequence version replaced XP_011518335.1.
            
            Transcript Variant: This variant (3) lacks an alternate exon in the
            3' coding region, which causes a frameshift compared to variant 1.
            It encodes isoform 3, which is shorter than and has a distinct
            C-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BI668465.1, BI668180.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2154665, SAMEA2467146
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..185
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..185
                     /product="COMM domain-containing protein 9 isoform 3"
                     /note="COMM domain-containing protein 9"
                     /calculated_mol_wt=20557
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q9P000.2)"
     Region          90..>106
                     /region_name="Commd"
                     /note="COMM_Domain, a family of domains found at the
                     C-terminus of HCarG, the copper metabolism gene MURR1
                     product, and related proteins. Presumably all COMM_Domain
                     containing proteins are located in the nucleus and the
                     COMM domain plays a role in...; cl06336"
                     /db_xref="CDD:471425"
     CDS             1..185
                     /gene="COMMD9"
                     /gene_synonym="C11orf55; HSPC166; LINC00610"
                     /coded_by="NM_001307932.2:13..570"
                     /note="isoform 3 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS76395.1"
                     /db_xref="GeneID:29099"
                     /db_xref="HGNC:HGNC:25014"
                     /db_xref="MIM:612299"
ORIGIN      
        1 maaltaehfa alqsllkass kdvvrqlcqe sfsssalglk klldvtcssl svtqeeaeel
       61 lqalhrltrl vafrdlssae ailalfpenf hqnlknlltk iilehvlsat pgrsglesgy
      121 qnllrqhqph grphlpapde dprrsqpmrr qtlhlschrg aeqrntghhv rwpgphprpt
      181 lcrgq
//
LOCUS       NP_001001436             154 aa            linear   PRI 20-NOV-2025
DEFINITION  UPF0547 protein C16orf87 isoform 1 [Homo sapiens].
ACCESSION   NP_001001436
VERSION     NP_001001436.1
DBSOURCE    REFSEQ: accession NM_001001436.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   7  (residues 1 to 154)
  AUTHORS   Joshi,P., Greco,T.M., Guise,A.J., Luo,Y., Yu,F., Nesvizhskii,A.I.
            and Cristea,I.M.
  TITLE     The functional interactome landscape of the human histone
            deacetylase family
  JOURNAL   Mol Syst Biol 9, 672 (2013)
   PUBMED   23752268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC007225.2, BC056676.1 and BX647945.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.300646.1,
                                           SRR1660805.58567.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMN03267769
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000285697.9/ ENSP00000285697.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q11.2"
     Protein         1..154
                     /product="UPF0547 protein C16orf87 isoform 1"
                     /note="UPF0547 protein C16orf87"
                     /calculated_mol_wt=17668
     Region          14..38
                     /region_name="UPF0547"
                     /note="Uncharacterized protein family UPF0547; pfam10571"
                     /db_xref="CDD:402278"
     Region          43..119
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6PH81.1)"
     Site            91
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q6PH81.1)"
     CDS             1..154
                     /gene="C16orf87"
                     /coded_by="NM_001001436.4:32..496"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS10724.1"
                     /db_xref="GeneID:388272"
                     /db_xref="HGNC:HGNC:33754"
ORIGIN      
        1 msatrakkvk matkscpecd qqvpvacksc pcgyifisrk llnakhseks ppstenkhea
       61 krrrtervrr ekinstvnkd lenrkrsrsn shsdhirrgr grpksasakk heeerekqek
      121 eidiyanlsd ekafvfsval aeinrkiinq rlil
//
LOCUS       NP_001480                475 aa            linear   PRI 20-NOV-2025
DEFINITION  nuclear receptor subfamily 6 group A member 1 isoform 2 [Homo
            sapiens].
ACCESSION   NP_001480
VERSION     NP_001480.3
DBSOURCE    REFSEQ: accession NM_001489.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 475)
  AUTHORS   Neelathi,U.M., Ullah,E., George,A., Maftei,M.I., Boobalan,E.,
            Sanchez-Mendoza,D., Adams,C., McGaughey,D., Sergeev,Y.V., Ai
            Rawi,R., Naik,A., Bender,C., Maumenee,I.H., Michaelides,M.,
            Tan,T.G., Lin,S., Villasmil,R., Blain,D., Hufnagel,R.B., Arno,G.,
            Young,R.M., Guan,B. and Brooks,B.P.
  TITLE     Variants in NR6A1 cause a novel oculo vertebral renal syndrome
  JOURNAL   Nat Commun 16 (1), 6111 (2025)
   PUBMED   40610405
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 475)
  AUTHORS   Wu,Q., Li,X., Long,M., Xie,X. and Liu,Q.
  TITLE     Integrated analysis of histone lysine lactylation (Kla)-specific
            genes suggests that NR6A1, OSBP2 and UNC119B are novel therapeutic
            targets for hepatocellular carcinoma
  JOURNAL   Sci Rep 13 (1), 18642 (2023)
   PUBMED   37903971
  REMARK    GeneRIF: Integrated analysis of histone lysine lactylation
            (Kla)-specific genes suggests that NR6A1, OSBP2 and UNC119B are
            novel therapeutic targets for hepatocellular carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 475)
  AUTHORS   Daisuke,H., Kato,H., Fukumura,K., Mayeda,A., Miyagi,Y., Seiki,M.
            and Koshikawa,N.
  TITLE     Novel LAMC2 fusion protein has tumor-promoting properties in
            ovarian carcinoma
  JOURNAL   Cancer Sci 112 (12), 4957-4967 (2021)
   PUBMED   34689384
  REMARK    GeneRIF: Novel LAMC2 fusion protein has tumor-promoting properties
            in ovarian carcinoma.
REFERENCE   4  (residues 1 to 475)
  AUTHORS   Zhou,W., Jiang,R., Wang,Y., Li,Y., Sun,Z. and Zhao,H.
  TITLE     hsa_circ_001653 up-regulates NR6A1 expression and elicits gastric
            cancer progression by binding to microRNA-377
  JOURNAL   Exp Physiol 105 (12), 2141-2153 (2020)
   PUBMED   33006200
  REMARK    GeneRIF: hsa_circ_001653 up-regulates NR6A1 expression and elicits
            gastric cancer progression by binding to microRNA-377.
REFERENCE   5  (residues 1 to 475)
  AUTHORS   Wang,Y., Wan,X., Hao,Y., Zhao,Y., Du,L., Huang,Y., Liu,Z., Wang,Y.,
            Wang,N. and Zhang,P.
  TITLE     NR6A1 regulates lipid metabolism through mammalian target of
            rapamycin complex 1 in HepG2 cells
  JOURNAL   Cell Commun Signal 17 (1), 77 (2019)
   PUBMED   31315616
  REMARK    GeneRIF: the role of NR6A1 in the lipogenesis in HepG2 cells
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 475)
  AUTHORS   Agoulnik,I.Y., Cho,Y., Niederberger,C., Kieback,D.G. and
            Cooney,A.J.
  TITLE     Cloning, expression analysis and chromosomal localization of the
            human nuclear receptor gene GCNF
  JOURNAL   FEBS Lett 424 (1-2), 73-78 (1998)
   PUBMED   9537518
REFERENCE   7  (residues 1 to 475)
  AUTHORS   Kapelle,M., Kratzschmar,J., Husemann,M. and Schleuning,W.D.
  TITLE     cDNA cloning of two closely related forms of human germ cell
            nuclear factor (GCNF)
  JOURNAL   Biochim Biophys Acta 1352 (1), 13-17 (1997)
   PUBMED   9177477
REFERENCE   8  (residues 1 to 475)
  AUTHORS   Yan,Z.H., Medvedev,A., Hirose,T., Gotoh,H. and Jetten,A.M.
  TITLE     Characterization of the response element and DNA binding properties
            of the nuclear orphan receptor germ cell nuclear factor/retinoid
            receptor-related testis-associated receptor
  JOURNAL   J Biol Chem 272 (16), 10565-10572 (1997)
   PUBMED   9099702
REFERENCE   9  (residues 1 to 475)
  AUTHORS   Lei,W., Hirose,T., Zhang,L.X., Adachi,H., Spinella,M.J.,
            Dmitrovsky,E. and Jetten,A.M.
  TITLE     Cloning of the human orphan receptor germ cell nuclear
            factor/retinoid receptor-related testis-associated receptor and its
            differential regulation during embryonal carcinoma cell
            differentiation
  JOURNAL   J Mol Endocrinol 18 (2), 167-176 (1997)
   PUBMED   9134503
REFERENCE   10 (residues 1 to 475)
  AUTHORS   Susens,U. and Borgmeyer,U.
  TITLE     Characterization of the human germ cell nuclear factor gene
  JOURNAL   Biochim Biophys Acta 1309 (3), 179-182 (1996)
   PUBMED   8982251
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354928.9, BC030600.1,
            AL354979.17 and AA467752.1.
            
            On Oct 1, 2004 this sequence version replaced NP_001480.2.
            
            Summary: This gene encodes an orphan nuclear receptor which is a
            member of the nuclear hormone receptor family. Its expression
            pattern suggests that it may be involved in neurogenesis and germ
            cell development. The protein can homodimerize and bind DNA, but in
            vivo targets have not been identified. Alternate splicing results
            in multiple transcript variants.[provided by RefSeq, Jun 2013].
            
            Transcript Variant: This variant (2) uses two alternate in-frame
            splice sites compared to variant 1. The resulting isoform (2) has
            the same N- and C-termini but is shorter compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC042395.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..475
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q33.3"
     Protein         1..475
                     /product="nuclear receptor subfamily 6 group A member 1
                     isoform 2"
                     /note="retinoic acid receptor-related testis-associated
                     receptor; retinoid receptor-related testis-specific
                     receptor"
                     /calculated_mol_wt=53778
     Region          1..32
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          48..137
                     /region_name="NR_DBD_GCNF_like"
                     /note="DNA-binding domain of Germ cell nuclear factor
                     (GCNF) F1 is composed of two C4-type zinc fingers;
                     cd07169"
                     /db_xref="CDD:143543"
     Site            order(56,59,73,76,92,98,108,111)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:143543"
     Site            order(66..68,74..75,77,79,82,85,105..106,109,112,123,126)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:143543"
     Region          127..146
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15406.2)"
     Region          251..462
                     /region_name="NR_LBD_DHR4_like"
                     /note="The ligand binding domain of orphan nuclear
                     receptor Ecdysone-induced receptor DHR4; cd06953"
                     /db_xref="CDD:132751"
     Site            order(281..282,286,320,324,327,341,364)
                     /site_type="other"
                     /note="putative ligand binding site [chemical binding]"
                     /db_xref="CDD:132751"
     Site            order(291,294,298,303,308..309,311..312,315..316)
                     /site_type="active"
                     /note="putative coactivator recognition site [active]"
                     /db_xref="CDD:132751"
     CDS             1..475
                     /gene="NR6A1"
                     /gene_synonym="CT150; GCNF; GCNF1; hGCNF; hRTR; NR61; RTR"
                     /coded_by="NM_001489.5:193..1620"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS55340.1"
                     /db_xref="GeneID:2649"
                     /db_xref="HGNC:HGNC:7985"
                     /db_xref="MIM:602778"
ORIGIN      
        1 merdepppsg ggggggsagf leppaalppp prngfcqdel aeldpgtndr aeqrtclicg
       61 dratglhygi iscegckgff krsicnkrvy rcsrdkncvm srkqrnrcqy crllkclqmg
      121 mnrkairedg mpggrnksig pvqiseeeie rimsgqefee eanhwsnhgd sdhsspgnra
      181 sesnqpspgs tlssrsveln gfmafreqym gmsvpphyqy iphlfsysgh spllpqqars
      241 ldpqsyslih qllsaedlep lgtpmliedg yavtqaelfa llcrladell frqiawikkl
      301 pffcelsikd ytcllsstwq elillssltv yskqifgela dvtakyspsd eelhrfsdeg
      361 mevierliyl yhkfhqlkvs neeyacmkai nflnqdirgl tsasqleqln krywyicqdf
      421 teykythqpn rfpdlmmclp eiryiagkmv nvpleqlpll fkvvlhsckt svgke
//
LOCUS       NP_659486                318 aa            linear   PRI 20-NOV-2025
DEFINITION  ubiquitin-like domain-containing CTD phosphatase 1 [Homo sapiens].
ACCESSION   NP_659486
VERSION     NP_659486.2
DBSOURCE    REFSEQ: accession NM_145049.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 318)
  AUTHORS   Soueid,J., Hamze,Z., Bedran,J., Chahrour,M. and Boustany,R.M.
  TITLE     A novel autism-associated UBLCP1 mutation impacts proteasome
            regulation/activity
  JOURNAL   Transl Psychiatry 13 (1), 404 (2023)
   PUBMED   38129378
  REMARK    GeneRIF: A novel autism-associated UBLCP1 mutation impacts
            proteasome regulation/activity.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 318)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 318)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 318)
  AUTHORS   Liu,X., Xiao,W., Zhang,Y., Wiley,S.E., Zuo,T., Zheng,Y., Chen,N.,
            Chen,L., Wang,X., Zheng,Y., Huang,L., Lin,S., Murphy,A.N.,
            Dixon,J.E., Xu,P. and Guo,X.
  TITLE     Reversible phosphorylation of Rpn1 regulates 26S proteasome
            assembly and function
  JOURNAL   Proc Natl Acad Sci U S A 117 (1), 328-336 (2020)
   PUBMED   31843888
  REMARK    GeneRIF: Study provides evidence that Rpn1-Ser361 is a prevalent
            phosphosite that is required for proper assembly and activity of
            the 26S proteasome and identified multiple kinases, including
            PIM1/2/3, that can phosphorylate Rpn1-S361 and have demonstrated
            that UBLCP1 is a physiologically relevant phosphatase of this site.
            Blocking phosphorylation of Rpn1-S361 leads to slowed proliferation
            and mitochondrial dysfunction.
REFERENCE   6  (residues 1 to 318)
  AUTHORS   Sun,S., Liu,S., Zhang,Z., Zeng,W., Sun,C., Tao,T., Lin,X. and
            Feng,X.H.
  TITLE     Phosphatase UBLCP1 controls proteasome assembly
  JOURNAL   Open Biol 7 (5) (2017)
   PUBMED   28539385
  REMARK    GeneRIF: Data show that UBLCP1 selectively binds to the 26S
            proteasome non-ATPase regulatory subunit 13 (19S regulatory
            particle) in regulating proteasome assembly.
REFERENCE   7  (residues 1 to 318)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   8  (residues 1 to 318)
  AUTHORS   Yun,J.H., Ko,S., Lee,C.K., Cheong,H.K., Cheong,C., Yoon,J.B. and
            Lee,W.
  TITLE     Solution structure and Rpn1 interaction of the UBL domain of human
            RNA polymerase II C-terminal domain phosphatase
  JOURNAL   PLoS One 8 (5), e62981 (2013)
   PUBMED   23667555
  REMARK    GeneRIF: the high-resolution solution structure of the UBL domain
            of human UBLCP1 and its interaction with Rpn1
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 318)
  AUTHORS   Guo,X., Engel,J.L., Xiao,J., Tagliabracci,V.S., Wang,X., Huang,L.
            and Dixon,J.E.
  TITLE     UBLCP1 is a 26S proteasome phosphatase that regulates nuclear
            proteasome activity
  JOURNAL   Proc Natl Acad Sci U S A 108 (46), 18649-18654 (2011)
   PUBMED   21949367
  REMARK    GeneRIF: UBLCP1 is a 26S proteasome phosphatase that regulates
            nuclear proteasome activity
REFERENCE   10 (residues 1 to 318)
  AUTHORS   Zheng,H., Ji,C., Gu,S., Shi,B., Wang,J., Xie,Y. and Mao,Y.
  TITLE     Cloning and characterization of a novel RNA polymerase II
            C-terminal domain phosphatase
  JOURNAL   Biochem Biophys Res Commun 331 (4), 1401-1407 (2005)
   PUBMED   15883030
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA930581.1, AY444562.1 and AC011418.5.
            
            On Jun 27, 2008 this sequence version replaced NP_659486.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY444562.1, SRR3476690.926666.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000296786.8/ ENSP00000296786.6
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.3"
     Protein         1..318
                     /product="ubiquitin-like domain-containing CTD phosphatase
                     1"
                     /EC_number="3.1.3.16"
                     /note="CTD phosphatase-like with ubiquitin domain 1;
                     CTD-like phosphatase domain-containing protein; nuclear
                     proteasome inhibitor UBLCP1"
                     /calculated_mol_wt=36674
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (Q8WVY7.2)"
     Region          3..77
                     /region_name="Ubl_UBLCP1"
                     /note="ubiquitin-like (Ubl) domain found in ubiquitin-like
                     domain-containing CTD phosphatase 1 (UBLCP1) and similar
                     proteins; cd01813"
                     /db_xref="CDD:340511"
     Site            29
                     /site_type="other"
                     /note="key conserved lysine K27"
                     /db_xref="CDD:340511"
     Region          117..311
                     /region_name="HAD_IIID1"
                     /note="HAD-superfamily subfamily IIID hydrolase,
                     TIGR02245"
                     /db_xref="CDD:131299"
     Site            117
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q8WVY7.2)"
     CDS             1..318
                     /gene="UBLCP1"
                     /gene_synonym="CPUB1"
                     /coded_by="NM_145049.5:118..1074"
                     /db_xref="CCDS:CCDS4345.1"
                     /db_xref="GeneID:134510"
                     /db_xref="HGNC:HGNC:28110"
                     /db_xref="MIM:609867"
ORIGIN      
        1 malpiivkwg gqeysvttls eddtvldlkq flktltgvlp erqkllglkv kgkpaendvk
       61 lgalklkpnt kimmmgtree sledvlgppp dnddvvndfd iedevveven reenllkisr
      121 rvkeykveil nppregkkll vldvdytlfd hrscaetgve lmrpylhefl tsayedydiv
      181 iwsatnmkwi eakmkelgvs tnanykitfm ldsaamitvh tprrglidvk plgviwgkfs
      241 efyskkntim fddigrnflm npqnglkirp fmkahlnrdk dkellkltqy lkeiaklddf
      301 ldlnhkywer ylskkqgq
//
LOCUS       NP_001332813             216 aa            linear   PRI 20-NOV-2025
DEFINITION  DDB1- and CUL4-associated factor 16 [Homo sapiens].
ACCESSION   NP_001332813
VERSION     NP_001332813.1
DBSOURCE    REFSEQ: accession NM_001345884.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 216)
  AUTHORS   Pu,C., Tong,Y., Liu,Y., Lan,S., Wang,S., Yan,G., Zhang,H., Luo,D.,
            Ma,X., Yu,S., Huang,Q., Deng,R. and Li,R.
  TITLE     Selective degradation of PARP2 by PROTACs via recruiting DCAF16 for
            triple-negative breast cancer
  JOURNAL   Eur J Med Chem 236, 114321 (2022)
   PUBMED   35430559
  REMARK    GeneRIF: Selective degradation of PARP2 by PROTACs via recruiting
            DCAF16 for triple-negative breast cancer.
REFERENCE   2  (residues 1 to 216)
  AUTHORS   Zhang,Y., Yu,H., Zhang,J., Gao,H., Wang,S., Li,S., Wei,P.,
            Liang,J., Yu,G., Wang,X., Li,X., Li,D. and Yang,W.
  TITLE     Cul4A-DDB1-mediated monoubiquitination of phosphoglycerate
            dehydrogenase promotes colorectal cancer metastasis via increased
            S-adenosylmethionine
  JOURNAL   J Clin Invest 131 (21) (2021)
   PUBMED   34720086
REFERENCE   3  (residues 1 to 216)
  AUTHORS   Zhang,X., Thielert,M., Li,H. and Cravatt,B.F.
  TITLE     SPIN4 Is a Principal Endogenous Substrate of the E3 Ubiquitin
            Ligase DCAF16
  JOURNAL   Biochemistry 60 (9), 637-642 (2021)
   PUBMED   33636084
REFERENCE   4  (residues 1 to 216)
  AUTHORS   Zhang,X., Crowley,V.M., Wucherpfennig,T.G., Dix,M.M. and
            Cravatt,B.F.
  TITLE     Electrophilic PROTACs that degrade nuclear proteins by engaging
            DCAF16
  JOURNAL   Nat Chem Biol 15 (7), 737-746 (2019)
   PUBMED   31209349
REFERENCE   5  (residues 1 to 216)
  AUTHORS   Jin,J., Arias,E.E., Chen,J., Harper,J.W. and Walter,J.C.
  TITLE     A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
            which is required for S phase destruction of the replication factor
            Cdt1
  JOURNAL   Mol Cell 23 (5), 709-721 (2006)
   PUBMED   16949367
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC005768.17.
            
            Transcript Variant: This variant (5) plus variants 1-4 and 6 all
            encode the same protein.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA2154361,
                              SAMEA2156099 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..216
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15.31"
     Protein         1..216
                     /product="DDB1- and CUL4-associated factor 16"
                     /calculated_mol_wt=24062
     Region          1..216
                     /region_name="DCA16"
                     /note="DDB1- and CUL4-associated factor 16; pfam15349"
                     /db_xref="CDD:434656"
     Region          1..42
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NXF7.1)"
     Site            61
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9NXF7.1)"
     CDS             1..216
                     /gene="DCAF16"
                     /gene_synonym="C4orf30"
                     /coded_by="NM_001345884.2:1083..1733"
                     /db_xref="CCDS:CCDS3423.1"
                     /db_xref="GeneID:54876"
                     /db_xref="HGNC:HGNC:25987"
                     /db_xref="MIM:620524"
ORIGIN      
        1 mgprnpspdh lseseseeee nisylnessg eewdsseeed smvpnlsple slawqvkcll
       61 kysttwkpln pnswlyhakl ldpstpvhil reiglrlshc shcvpklepi pewpplascg
      121 vppfqkplts psrlsrdhat lngalqfatk qlsrtlsrat pipeylkqip nscvsgcccg
      181 wltktvkett rtepinttys ytdfqkavnk lltasl
//
LOCUS       NP_001356712             283 aa            linear   PRI 20-NOV-2025
DEFINITION  myeloid leukemia factor 1 isoform 6 [Homo sapiens].
ACCESSION   NP_001356712 XP_005247536
VERSION     NP_001356712.1
DBSOURCE    REFSEQ: accession NM_001369783.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 283)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 283)
  AUTHORS   Tang,Z., Yang,Y., Chen,W. and Liang,T.
  TITLE     Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling
  JOURNAL   Hepatol Commun 7 (8), e0204 (2023)
   PUBMED   37486965
  REMARK    GeneRIF: Epigenetic deregulation of MLF1 drives intrahepatic
            cholangiocarcinoma progression through EGFR/AKT and
            Wnt/beta-catenin signaling.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 283)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 283)
  AUTHORS   Huang,D., Liu,C., Sun,X., Sun,X., Qu,Y., Tang,Y., Li,G. and Tong,T.
  TITLE     CRL4DCAF8 and USP11 oppositely regulate the stability of myeloid
            leukemia factors (MLFs)
  JOURNAL   Biochem Biophys Res Commun 529 (2), 127-132 (2020)
   PUBMED   32703400
  REMARK    GeneRIF: CRL4(DCAF8) and USP11 oppositely regulate the stability of
            myeloid leukemia factors (MLFs).
REFERENCE   5  (residues 1 to 283)
  AUTHORS   Darracq,A., Pak,H., Bourgoin,V., Zmiri,F., Dellaire,G., Affar,E.B.
            and Milot,E.
  TITLE     NPM and NPM-MLF1 interact with chromatin remodeling complexes and
            influence their recruitment to specific genes
  JOURNAL   PLoS Genet 15 (11), e1008463 (2019)
   PUBMED   31675375
  REMARK    GeneRIF: the abnormal gene regulation imposed by NPM-MLF1 can be
            characterized by the enhanced recruitment of NuRD to gene
            regulatory regions. Thus, different mechanisms would orchestrate
            the dysregulation of NPM function in NPMc+- versus
            NPM1-MLF1-associated leukemia.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 283)
  AUTHORS   Yoneda-Kato,N., Tomoda,K., Umehara,M., Arata,Y. and Kato,J.Y.
  TITLE     Myeloid leukemia factor 1 regulates p53 by suppressing COP1 via
            COP9 signalosome subunit 3
  JOURNAL   EMBO J 24 (9), 1739-1749 (2005)
   PUBMED   15861129
REFERENCE   7  (residues 1 to 283)
  AUTHORS   Hanissian,S.H., Akbar,U., Teng,B., Janjetovic,Z., Hoffmann,A.,
            Hitzler,J.K., Iscove,N., Hamre,K., Du,X., Tong,Y., Mukatira,S.,
            Robertson,J.H. and Morris,S.W.
  TITLE     cDNA cloning and characterization of a novel gene encoding the
            MLF1-interacting protein MLF1IP
  JOURNAL   Oncogene 23 (20), 3700-3707 (2004)
   PUBMED   15116101
REFERENCE   8  (residues 1 to 283)
  AUTHORS   Arber,D.A., Chang,K.L., Lyda,M.H., Bedell,V., Spielberger,R. and
            Slovak,M.L.
  TITLE     Detection of NPM/MLF1 fusion in t(3;5)-positive acute myeloid
            leukemia and myelodysplasia
  JOURNAL   Hum Pathol 34 (8), 809-813 (2003)
   PUBMED   14506644
  REMARK    GeneRIF: These findings suggest that an NPM/MLF1 fusion is the
            primary molecular abnormality in t(3;5) MDS and AML with
            multilineage dysplasia, and that cases with NPM/MLF1 may be
            clinically distinct from other MDS-associated disease
REFERENCE   9  (residues 1 to 283)
  AUTHORS   Lim,R., Winteringham,L.N., Williams,J.H., McCulloch,R.K.,
            Ingley,E., Tiao,J.Y., Lalonde,J.P., Tsai,S., Tilbrook,P.A., Sun,Y.,
            Wu,X., Morris,S.W. and Klinken,S.P.
  TITLE     MADM, a novel adaptor protein that mediates phosphorylation of the
            14-3-3 binding site of myeloid leukemia factor 1
  JOURNAL   J Biol Chem 277 (43), 40997-41008 (2002)
   PUBMED   12176995
  REMARK    GeneRIF: phosphorylation of 14-3-3 binding site by MADM
REFERENCE   10 (residues 1 to 283)
  AUTHORS   Yoneda-Kato,N., Look,A.T., Kirstein,M.N., Valentine,M.B.,
            Raimondi,S.C., Cohen,K.J., Carroll,A.J. and Morris,S.W.
  TITLE     The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid
            leukemia produces a novel fusion gene, NPM-MLF1
  JOURNAL   Oncogene 12 (2), 265-275 (1996)
   PUBMED   8570204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC106707.9, KU178187.1 and
            AC025033.20.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Apr 18, 2019 this sequence version replaced XP_005247536.1.
            
            Summary: This gene encodes an oncoprotein which is thought to play
            a role in the phenotypic determination of hemopoetic cells.
            Translocations between this gene and nucleophosmin have been
            associated with myelodysplastic syndrome and acute myeloid
            leukemia. Multiple transcript variants encoding different isoforms
            have been found for this gene. [provided by RefSeq, Sep 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189655.181954.1,
                                           SRR5189655.221586.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2149178
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000466246.7/ ENSP00000417278.2
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..283
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25.32"
     Protein         1..283
                     /product="myeloid leukemia factor 1 isoform 6"
                     /note="myelodysplasia-myeloid leukemia factor 1; testis
                     tissue sperm-binding protein Li 49e"
                     /calculated_mol_wt=31967
     Region          26..217
                     /region_name="Mlf1IP"
                     /note="Myelodysplasia-myeloid leukemia factor
                     1-interacting protein; pfam10248"
                     /db_xref="CDD:463022"
     CDS             1..283
                     /gene="MLF1"
                     /coded_by="NM_001369783.1:108..959"
                     /note="isoform 6 is encoded by transcript variant 9"
                     /db_xref="CCDS:CCDS93414.1"
                     /db_xref="GeneID:4291"
                     /db_xref="HGNC:HGNC:7125"
                     /db_xref="MIM:601402"
ORIGIN      
        1 mfrmlnssfe ddpffsesil ahrenmrqmi rsfsepfgrd llsisdgrgr ahnrrghndg
       61 edsltatscs lvpfgdfggm htdvssfqtm dqmvsnmrny mqklernfgq lsvdpnghsf
      121 csssvmtysk igdeppkvfq astqtrrapg giketrkamr dsdsglekma ighhihdrah
      181 vikksknkkt gdeevnqefi nmnesdahaf deewqsevlk ykpgrhnlgn trmrsvghen
      241 pgsrelkrre kpqqspaieh grrsnvlgdk lhikgssvks nkk
//
LOCUS       NP_001354566             120 aa            linear   PRI 20-NOV-2025
DEFINITION  SUN domain-containing protein 1 isoform h [Homo sapiens].
ACCESSION   NP_001354566
VERSION     NP_001354566.1
DBSOURCE    REFSEQ: accession NM_001367637.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 120)
  AUTHORS   Fan,T., Zhu,J., Liu,W., Qu,R., Khan,A.U., Shi,Y., Liu,J., Zhou,Z.,
            Xu,C., Dai,J. and Ouyang,J.
  TITLE     SUN1 inhibits osteogenesis and promotes adipogenesis of human
            adipose-derived stem cells by regulating alpha-tubulin and CD36
            expression
  JOURNAL   J Cell Mol Med 28 (19), e70143 (2024)
   PUBMED   39383106
  REMARK    GeneRIF: SUN1 inhibits osteogenesis and promotes adipogenesis of
            human adipose-derived stem cells by regulating alpha-tubulin and
            CD36 expression.
REFERENCE   2  (residues 1 to 120)
  AUTHORS   Gurusaran,M., Erlandsen,B.S. and Davies,O.R.
  TITLE     The crystal structure of SUN1-KASH6 reveals an asymmetric LINC
            complex architecture compatible with nuclear membrane insertion
  JOURNAL   Commun Biol 7 (1), 138 (2024)
   PUBMED   38291267
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 120)
  AUTHORS   Baskerville,V., Rapuri,S., Mehlhop,E. and Coyne,A.N.
  TITLE     SUN1 facilitates CHMP7 nuclear influx and injury cascades in
            sporadic amyotrophic lateral sclerosis
  JOURNAL   Brain 147 (1), 109-121 (2024)
   PUBMED   37639327
  REMARK    GeneRIF: SUN1 facilitates CHMP7 nuclear influx and injury cascades
            in sporadic amyotrophic lateral sclerosis.
REFERENCE   4  (residues 1 to 120)
  AUTHORS   Meng,Q., Shao,B., Zhao,D., Fu,X., Wang,J., Li,H., Zhou,Q. and
            Gao,T.
  TITLE     Loss of SUN1 function in spermatocytes disrupts the attachment of
            telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans
  JOURNAL   Hum Genet 142 (4), 531-541 (2023)
   PUBMED   36933034
  REMARK    GeneRIF: Loss of SUN1 function in spermatocytes disrupts the
            attachment of telomeres to the nuclear envelope and contributes to
            non-obstructive azoospermia in humans.
REFERENCE   5  (residues 1 to 120)
  AUTHORS   Crisp,M., Liu,Q., Roux,K., Rattner,J.B., Shanahan,C., Burke,B.,
            Stahl,P.D. and Hodzic,D.
  TITLE     Coupling of the nucleus and cytoplasm: role of the LINC complex
  JOURNAL   J Cell Biol 172 (1), 41-53 (2006)
   PUBMED   16380439
REFERENCE   6  (residues 1 to 120)
  AUTHORS   Padmakumar,V.C., Libotte,T., Lu,W., Zaim,H., Abraham,S.,
            Noegel,A.A., Gotzmann,J., Foisner,R. and Karakesisoglou,I.
  TITLE     The inner nuclear membrane protein Sun1 mediates the anchorage of
            Nesprin-2 to the nuclear envelope
  JOURNAL   J Cell Sci 118 (Pt 15), 3419-3430 (2005)
   PUBMED   16079285
  REMARK    GeneRIF: The Sun1 itself does not require functional A-type lamins
            for its localisation at the inner nuclear membrane in mammalian
            cells.
REFERENCE   7  (residues 1 to 120)
  AUTHORS   Bray,J.D., Chennathukuzhi,V.M. and Hecht,N.B.
  TITLE     Identification and characterization of cDNAs encoding four novel
            proteins that interact with translin associated factor-X
  JOURNAL   Genomics 79 (6), 799-808 (2002)
   PUBMED   12036294
  REMARK    GeneRIF: Isolation of a cDNA encoding a mouse homolog of the human
            SUN1 (UNC84A) gene.
REFERENCE   8  (residues 1 to 120)
  AUTHORS   Dreger,M., Bengtsson,L., Schoneberg,T., Otto,H. and Hucho,F.
  TITLE     Nuclear envelope proteomics: novel integral membrane proteins of
            the inner nuclear membrane
  JOURNAL   Proc Natl Acad Sci U S A 98 (21), 11943-11948 (2001)
   PUBMED   11593002
  REMARK    GeneRIF: KIAA0810 is a novel 100-kDa transmembrane protein with
            similarity to Caenorhabditis elegans Unc-84A and resides in the
            inner nuclear membrane. It is likely to interact with the nuclear
            lamina.
REFERENCE   9  (residues 1 to 120)
  AUTHORS   Malone,C.J., Fixsen,W.D., Horvitz,H.R. and Han,M.
  TITLE     UNC-84 localizes to the nuclear envelope and is required for
            nuclear migration and anchoring during C. elegans development
  JOURNAL   Development 126 (14), 3171-3181 (1999)
   PUBMED   10375507
  REMARK    GeneRIF: Describes cloning and function of C. elegans unc-84 and
            cloning of human orthologs.
REFERENCE   10 (residues 1 to 120)
  AUTHORS   Ben Yaou,R., Leturcq,F. and Bonne,G.
  TITLE     Emery-Dreifuss Muscular Dystrophy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC099731.5.
            
            Summary: This gene is a member of the unc-84 homolog family and
            encodes a nuclear envelope protein with an Unc84 (SUN) domain. The
            protein is involved in nuclear anchorage and migration.
            Alternatively spliced transcript variants have been described.
            [provided by RefSeq, Jan 2019].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB278949.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145240, SAMEA2145544
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..120
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..120
                     /product="SUN domain-containing protein 1 isoform h"
                     /note="Sad1 unc-84 domain protein 1; protein unc-84
                     homolog A; SUN domain-containing protein 1; sad1/unc-84
                     protein-like 1"
                     /calculated_mol_wt=12865
     Region          12..>101
                     /region_name="MRP"
                     /note="Mitochondrial RNA binding protein MRP; pfam09387"
                     /db_xref="CDD:430576"
     CDS             1..120
                     /gene="SUN1"
                     /gene_synonym="UNC84A"
                     /coded_by="NM_001367637.1:105..467"
                     /note="isoform h is encoded by transcript variant 8"
                     /db_xref="GeneID:23353"
                     /db_xref="HGNC:HGNC:18587"
                     /db_xref="MIM:607723"
ORIGIN      
        1 msrrslrlat tactlgdgea vgadsgtssa vslknraart tkqrrstnks afsinhvsrq
       61 vtssgvshgg tvslqdavtr rppvldeswi reqttvdhfw gclnkdnpkt svcfqesskq
//
LOCUS       NP_000505                211 aa            linear   PRI 20-NOV-2025
DEFINITION  glial cell line-derived neurotrophic factor isoform 1 preproprotein
            [Homo sapiens].
ACCESSION   NP_000505
VERSION     NP_000505.1
DBSOURCE    REFSEQ: accession NM_000514.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Guo,X., Zhou,H., Liu,Y., Xu,W., Kanwore,K. and Zhang,L.
  TITLE     Glial-Cell-Line-Derived Neurotrophic Factor Promotes Glioblastoma
            Cell Migration and Invasion via the SMAD2/3-SERPINE1-Signaling Axis
  JOURNAL   Int J Mol Sci 25 (18), 10229 (2024)
   PUBMED   39337713
  REMARK    GeneRIF: Glial-Cell-Line-Derived Neurotrophic Factor Promotes
            Glioblastoma Cell Migration and Invasion via the
            SMAD2/3-SERPINE1-Signaling Axis.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 211)
  AUTHORS   Avenel,I.C.N., Ewald,J.D., Ariey-Bonnet,J., Kristensen,I.H.,
            Petterson,S.A., Thesbjerg,M.N., Burton,M., Thomassen,M.,
            Wennerberg,K., Michaelsen,S.R. and Kristensen,B.W.
  TITLE     GDNF/GFRA1 signaling contributes to chemo- and radioresistance in
            glioblastoma
  JOURNAL   Sci Rep 14 (1), 17639 (2024)
   PUBMED   39085346
  REMARK    GeneRIF: GDNF/GFRA1 signaling contributes to chemo- and
            radioresistance in glioblastoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 211)
  AUTHORS   Keszler,G., Vekony,B., Elek,Z., Nemoda,Z., Angyal,N., Banlaki,Z.,
            Kovacs-Nagy,R., Ronai,Z. and Rethelyi,J.M.
  TITLE     MicroRNA-Mediated Suppression of Glial Cell Line-Derived
            Neurotrophic Factor Expression Is Modulated by a
            Schizophrenia-Associated Non-Coding Polymorphism
  JOURNAL   Int J Mol Sci 25 (8), 4477 (2024)
   PUBMED   38674063
  REMARK    GeneRIF: MicroRNA-Mediated Suppression of Glial Cell Line-Derived
            Neurotrophic Factor Expression Is Modulated by a
            Schizophrenia-Associated Non-Coding Polymorphism.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 211)
  AUTHORS   Alster,P., Otto-Slusarczyk,D., Szlufik,S., Duszynska-Was,K.,
            Drzewinska,A., Wiercinska-Drapalo,A., Struga,M., Kutylowski,M.,
            Friedman,A. and Madetko-Alster,N.
  TITLE     The significance of glial cell line-derived neurotrophic factor
            analysis in Progressive Supranuclear Palsy
  JOURNAL   Sci Rep 14 (1), 2805 (2024)
   PUBMED   38307947
  REMARK    GeneRIF: The significance of glial cell line-derived neurotrophic
            factor analysis in Progressive Supranuclear Palsy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 211)
  AUTHORS   Airavaara,M., Pletnikova,O., Doyle,M.E., Zhang,Y.E., Troncoso,J.C.
            and Liu,Q.R.
  TITLE     Identification of novel GDNF isoforms and cis-antisense GDNFOS gene
            and their regulation in human middle temporal gyrus of Alzheimer
            disease
  JOURNAL   J Biol Chem 286 (52), 45093-45102 (2011)
   PUBMED   22081608
  REMARK    GeneRIF: Identification of novel GDNF isoforms and cis-antisense
            GDNFOS gene and their regulation in human middle temporal gyrus of
            Alzheimer disease
REFERENCE   6  (residues 1 to 211)
  AUTHORS   Schindelhauer,D., Schuffenhauer,S., Gasser,T., Steinkasserer,A. and
            Meitinger,T.
  TITLE     The gene coding for glial cell line derived neurotrophic factor
            (GDNF) maps to chromosome 5p12-p13.1
  JOURNAL   Genomics 28 (3), 605-607 (1995)
   PUBMED   7490108
REFERENCE   7  (residues 1 to 211)
  AUTHORS   Oppenheim,R.W., Houenou,L.J., Johnson,J.E., Lin,L.F., Li,L.,
            Lo,A.C., Newsome,A.L., Prevette,D.M. and Wang,S.
  TITLE     Developing motor neurons rescued from programmed and
            axotomy-induced cell death by GDNF
  JOURNAL   Nature 373 (6512), 344-346 (1995)
   PUBMED   7830769
REFERENCE   8  (residues 1 to 211)
  AUTHORS   Tomac,A., Lindqvist,E., Lin,L.F., Ogren,S.O., Young,D., Hoffer,B.J.
            and Olson,L.
  TITLE     Protection and repair of the nigrostriatal dopaminergic system by
            GDNF in vivo
  JOURNAL   Nature 373 (6512), 335-339 (1995)
   PUBMED   7830766
REFERENCE   9  (residues 1 to 211)
  AUTHORS   Schaar,D.G., Sieber,B.A., Sherwood,A.C., Dean,D., Mendoza,G.,
            Ramakrishnan,L., Dreyfus,C.F. and Black,I.B.
  TITLE     Multiple astrocyte transcripts encode nigral trophic factors in rat
            and human
  JOURNAL   Exp Neurol 130 (2), 387-393 (1994)
   PUBMED   7867768
REFERENCE   10 (residues 1 to 211)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC008869.5, AF053748.1 and
            AY052832.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a secreted ligand of the TGF-beta
            (transforming growth factor-beta) superfamily of proteins. Ligands
            of this family bind various TGF-beta receptors leading to
            recruitment and activation of SMAD family transcription factors
            that regulate gene expression. The encoded preproprotein is
            proteolytically processed to generate each subunit of the
            disulfide-linked homodimer. The recombinant form of this protein, a
            highly conserved neurotrophic factor, was shown to promote the
            survival and differentiation of dopaminergic neurons in culture,
            and was able to prevent apoptosis of motor neurons induced by
            axotomy. This protein is a ligand for the product of the RET
            (rearranged during transfection) protooncogene. Mutations in this
            gene may be associated with Hirschsprung disease and Tourette
            syndrome. This gene encodes multiple protein isoforms that may
            undergo similar proteolytic processing. [provided by RefSeq, Aug
            2016].
            
            Transcript Variant: This variant (1) differs in the 5' UTR,
            represents use of an alternate promoter, and uses a downstream
            start codon, compared to variant 3. The resulting isoform (1) has a
            shorter N-terminus, compared to isoform 3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF053748.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000326524.7/ ENSP00000317145.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.2"
     Protein         1..211
                     /product="glial cell line-derived neurotrophic factor
                     isoform 1 preproprotein"
                     /note="astrocyte-derived trophic factor; glial cell
                     line-derived neurotrophic factor"
                     /calculated_mol_wt=21669
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2070
     Region          21..56
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P39905.1)"
     mat_peptide     78..211
                     /product="Glial cell line-derived neurotrophic factor.
                     /id=PRO_0000034005"
                     /note="propagated from UniProtKB/Swiss-Prot (P39905.1)"
                     /calculated_mol_wt=15068
     Region          78..113
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P39905.1)"
     Region          115..210
                     /region_name="TGF_beta_GDNF"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in glial cell line-derived neurotrophic
                     factor (GDNF) and similar proteins; cd19380"
                     /db_xref="CDD:381650"
     Site            order(123,125,129..132,142..146,155..157,159..160,
                     162..163,175..181,184,201..203)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381650"
     Site            order(124,137..139,141,186..191,193..197,199)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:381650"
     Site            126
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:19478429,
                     ECO:0000269|PubMed:25242331, ECO:0007744|PDB:4UX8;
                     propagated from UniProtKB/Swiss-Prot (P39905.1)"
     Site            162
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P39905.1)"
     CDS             1..211
                     /gene="GDNF"
                     /gene_synonym="ATF; ATF1; ATF2; HFB1-GDNF; HSCR3"
                     /coded_by="NM_000514.4:562..1197"
                     /note="isoform 1 preproprotein is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS3922.1"
                     /db_xref="GeneID:2668"
                     /db_xref="HGNC:HGNC:4232"
                     /db_xref="MIM:600837"
ORIGIN      
        1 mklwdvvavc lvllhtasaf plpagkrppe apaedrslgr rrapfalssd snmpedypdq
       61 fddvmdfiqa tikrlkrspd kqmavlprre rnrqaaaanp ensrgkgrrg qrgknrgcvl
      121 taihlnvtdl glgyetkeel ifrycsgscd aaettydkil knlsrnrrlv sdkvgqaccr
      181 piafdddlsf lddnlvyhil rkhsakrcgc i
//
LOCUS       NP_001012410             561 aa            linear   PRI 20-NOV-2025
DEFINITION  shugoshin 1 isoform EF [Homo sapiens].
ACCESSION   NP_001012410
VERSION     NP_001012410.1
DBSOURCE    REFSEQ: accession NM_001012410.5
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 561)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 561)
  AUTHORS   Yang,Z., Jiang,Y., Wang,L., Yu,B., Cai,H., Fan,J. and Zhang,M.
  TITLE     Prognosis and biological function of SGOL1 in clear cell renal cell
            carcinoma: a multiomics analysis
  JOURNAL   BMC Med Genomics 17 (1), 60 (2024)
   PUBMED   38383432
  REMARK    GeneRIF: Prognosis and biological function of SGOL1 in clear cell
            renal cell carcinoma: a multiomics analysis.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 561)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 561)
  AUTHORS   Chetaille,P., Preuss,C., Burkhard,S., Cote,J.M., Houde,C.,
            Castilloux,J., Piche,J., Gosset,N., Leclerc,S., Wunnemann,F.,
            Thibeault,M., Gagnon,C., Galli,A., Tuck,E., Hickson,G.R., El
            Amine,N., Boufaied,I., Lemyre,E., de Santa Barbara,P., Faure,S.,
            Jonzon,A., Cameron,M., Dietz,H.C., Gallo-McFarlane,E., Benson,D.W.,
            Moreau,C., Labuda,D., Zhan,S.H., Shen,Y., Jomphe,M., Jones,S.J.,
            Bakkers,J. and Andelfinger,G.
  CONSRTM   FORGE Canada Consortium
  TITLE     Mutations in SGOL1 cause a novel cohesinopathy affecting heart and
            gut rhythm
  JOURNAL   Nat Genet 46 (11), 1245-1249 (2014)
   PUBMED   25282101
  REMARK    GeneRIF: Mutations in SGOL1 cause a novel cohesinopathy affecting
            heart and gut rhythm.
REFERENCE   5  (residues 1 to 561)
  AUTHORS   Wang,X., Yang,Y., Duan,Q., Jiang,N., Huang,Y., Darzynkiewicz,Z. and
            Dai,W.
  TITLE     sSgo1, a major splice variant of Sgo1, functions in centriole
            cohesion where it is regulated by Plk1
  JOURNAL   Dev Cell 14 (3), 331-341 (2008)
   PUBMED   18331714
  REMARK    GeneRIF: Centriole splitting induced by Sgo1 depletion or
            expression of a dominant negative mutant is suppressed by ectopic
            expression of sSgo1 or by Plk1 knockdown.
REFERENCE   6  (residues 1 to 561)
  AUTHORS   Kitajima,T.S., Sakuno,T., Ishiguro,K., Iemura,S., Natsume,T.,
            Kawashima,S.A. and Watanabe,Y.
  TITLE     Shugoshin collaborates with protein phosphatase 2A to protect
            cohesin
  JOURNAL   Nature 441 (7089), 46-52 (2006)
   PUBMED   16541025
  REMARK    GeneRIF: a specific subtype of serine/threonine protein phosphatase
            2A (PP2A) associates with human shugoshin
REFERENCE   7  (residues 1 to 561)
  AUTHORS   Wang,X., Yang,Y. and Dai,W.
  TITLE     Differential subcellular localizations of two human Sgo1 isoforms:
            implications in regulation of sister chromatid cohesion and
            microtubule dynamics
  JOURNAL   Cell Cycle 5 (6), 635-640 (2006)
   PUBMED   16582621
REFERENCE   8  (residues 1 to 561)
  AUTHORS   McGuinness,B.E., Hirota,T., Kudo,N.R., Peters,J.M. and Nasmyth,K.
  TITLE     Shugoshin prevents dissociation of cohesin from centromeres during
            mitosis in vertebrate cells
  JOURNAL   PLoS Biol 3 (3), e86 (2005)
   PUBMED   15737064
  REMARK    GeneRIF: A shugoshin-like protein associates with centromeres
            during prophase and disappears at the onset of anaphase
REFERENCE   9  (residues 1 to 561)
  AUTHORS   Tang,Z., Sun,Y., Harley,S.E., Zou,H. and Yu,H.
  TITLE     Human Bub1 protects centromeric sister-chromatid cohesion through
            Shugoshin during mitosis
  JOURNAL   Proc Natl Acad Sci U S A 101 (52), 18012-18017 (2004)
   PUBMED   15604152
  REMARK    GeneRIF: Bub1 protects centromeric cohesion through Shugoshin in
            mitosis
REFERENCE   10 (residues 1 to 561)
  AUTHORS   Scanlan,M.J., Gout,I., Gordon,C.M., Williamson,B., Stockert,E.,
            Gure,A.O., Jager,D., Chen,Y.T., Mackay,A., O'Hare,M.J. and Old,L.J.
  TITLE     Humoral immunity to human breast cancer: antigen definition and
            quantitative analysis of mRNA expression
  JOURNAL   Cancer Immun 1, 4 (2001)
   PUBMED   12747765
  REMARK    Publication Status: Online-Only
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BX494477.1, AB193061.1 and
            AB187578.1.
            
            Summary: The protein encoded by this gene is a member of the
            shugoshin family of proteins. This protein is thought to protect
            centromeric cohesin from cleavage during mitotic prophase by
            preventing phosphorylation of a cohesin subunit. Reduced expression
            of this gene leads to the premature loss of centromeric cohesion,
            mis-segregation of sister chromatids, and mitotic arrest. Evidence
            suggests that this protein also protects a small subset of cohesin
            found along the length of the chromosome arms during mitotic
            prophase. An isoform lacking exon 6 has been shown to play a role
            in the cohesion of centrioles (PMID: 16582621 and PMID:18331714).
            Mutations in this gene have been associated with Chronic Atrial and
            Intestinal Dysrhythmia (CAID) syndrome, characterized by the
            co-occurrence of Sick Sinus Syndrome (SSS) and Chronic Intestinal
            Pseudo-obstruction (CIPO) within the first four decades of life
            (PMID:25282101). Fibroblast cells from CAID patients exhibited both
            increased cell proliferation and higher rates of senescence.
            Pseudogenes of this gene have been found on chromosomes 1 and 7.
            Alternative splicing results in multiple transcript variants.
            [provided by RefSeq, Mar 2015].
            
            Transcript Variant: This variant (Sgo1F, PMID:15737064; also known
            as A2) differs in the 5' UTR and contains an alternate 3' terminal
            segment compared to variant 1, resulting in a novel 3' coding
            region and distinct 3' UTR. It encodes isoform 1EF which is longer
            and has a distinct C-terminus, compared to isoform 1. Both variants
            Sgo1E and Sgo1F encode the same isoform (1EF).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB187578.1, AB193061.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN03267770 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..561
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p24.3"
     Protein         1..561
                     /product="shugoshin 1 isoform EF"
                     /note="shugoshin 1AB protein; shugoshin 1CD protein;
                     shugoshin 1EF protein; shugoshin 1GH protein; shugoshin
                     1KL protein; serologically defined breast cancer antigen
                     NY-BR-85"
                     /calculated_mol_wt=64059
     Region          1..176
                     /region_name="Necessary for interaction with PPP2CA and
                     PPP2R1A. /evidence=ECO:0000269|PubMed:16580887"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          22..66
                     /region_name="Shugoshin_N"
                     /note="Shugoshin N-terminal coiled-coil region; pfam07558"
                     /db_xref="CDD:462208"
     Region          192..200
                     /region_name="D-box 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            256
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          260..331
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          310..312
                     /region_name="KEN box"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          348..441
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18220336,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          438..446
                     /region_name="D-box 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          451..455
                     /region_name="PXVXL/I motif.
                     /evidence=ECO:0000305|PubMed:21346195"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          457..465
                     /region_name="D-box 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     Region          474..495
                     /region_name="Shugoshin_C"
                     /note="Shugoshin C terminus; pfam07557"
                     /db_xref="CDD:462207"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by NEK2.
                     /evidence=ECO:0000269|PubMed:17621308,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q5FBB7.1)"
     CDS             1..561
                     /gene="SGO1"
                     /gene_synonym="CAID; NY-BR-85; SGO; SGOL1"
                     /coded_by="NM_001012410.5:156..1841"
                     /note="isoform EF is encoded by transcript variant Sgo1F"
                     /db_xref="CCDS:CCDS33716.1"
                     /db_xref="GeneID:151648"
                     /db_xref="HGNC:HGNC:25088"
                     /db_xref="MIM:609168"
ORIGIN      
        1 makerclkks fqdsledikk rmkekrnknl aeigkrrsfi aapcqiitnt stllknyqdn
       61 nkmlvlalen ekskvkeaqd iilqlrkecy yltcqlyalk gkltsqqtve paqnqeicss
      121 gmdpnsddss rnlfvkdlpq ipleetelpg qgesfqiedq iptipqdtlg vdfdsgeaks
      181 tdnvlprtvs vrsslkkhcn sicqfdsldd fetshlagks fefervgfld plvnmhipen
      241 vqhnacqwsk dqvnlspkli qpgtftktke dileskseqt kskqrdtqer kreekrkanr
      301 rkskrmskyk enksenkktv pqkkmhksvs sndaynfnle egvhltpfrq kvsndsnree
      361 nnesevslce ssgsgddsdd lylptckyiq nptsnsdrpv trplakralk ytdeketegs
      421 kptktptttp petqqsphls lkditnvsly pvvkirrlsl spkknkaspa valpkrrcta
      481 svnykeptla sklrrgdpft dlcflnspif kqkkdlrrsk kralevspak eaifilyyvr
      541 efvsrfpdcr kcklethicl r
//
LOCUS       NP_001661                962 aa            linear   PRI 20-NOV-2025
DEFINITION  splicing regulator ARVCF isoform 1 [Homo sapiens].
ACCESSION   NP_001661
VERSION     NP_001661.1
DBSOURCE    REFSEQ: accession NM_001670.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 962)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 962)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 962)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 962)
  AUTHORS   Suzuki,N., Idogawa,M., Tange,S., Ohashi,T., Sasaki,Y., Nakase,H.
            and Tokino,T.
  TITLE     p53-induced ARVCF modulates the splicing landscape and supports the
            tumor suppressive function of p53
  JOURNAL   Oncogene 39 (10), 2202-2211 (2020)
   PUBMED   31827232
  REMARK    GeneRIF: p53-induced ARVCF modulates the splicing landscape and
            supports the tumor suppressive function of p53.
REFERENCE   5  (residues 1 to 962)
  AUTHORS   Zhang,D., Tang,N., Liu,Y. and Wang,E.H.
  TITLE     ARVCF expression is significantly correlated with the malignant
            phenotype of non-small cell lung cancer
  JOURNAL   Mol Carcinog 54 Suppl 1, E185-E191 (2015)
   PUBMED   25683624
  REMARK    GeneRIF: observed ARVCF-dependent changes in small GTPase (mainly
            RhoA) activity in lung cancer cells. We confirmed that ARVCF plays
            an important role in the malignant phenotype
REFERENCE   6  (residues 1 to 962)
  AUTHORS   Mariner,D.J., Wang,J. and Reynolds,A.B.
  TITLE     ARVCF localizes to the nucleus and adherens junction and is
            mutually exclusive with p120(ctn) in E-cadherin complexes
  JOURNAL   J Cell Sci 113 (Pt 8), 1481-1490 (2000)
   PUBMED   10725230
REFERENCE   7  (residues 1 to 962)
  AUTHORS   Bonne,S., van Hengel,J. and van Roy,F.
  TITLE     Chromosomal mapping of human armadillo genes belonging to the
            p120(ctn)/plakophilin subfamily
  JOURNAL   Genomics 51 (3), 452-454 (1998)
   PUBMED   9721216
REFERENCE   8  (residues 1 to 962)
  AUTHORS   Sirotkin,H., Morrow,B., Saint-Jore,B., Puech,A., Das Gupta,R.,
            Patanjali,S.R., Skoultchi,A., Weissman,S.M. and Kucherlapati,R.
  TITLE     Identification, characterization, and precise mapping of a human
            gene encoding a novel membrane-spanning protein from the 22q11
            region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 42 (2), 245-251 (1997)
   PUBMED   9192844
REFERENCE   9  (residues 1 to 962)
  AUTHORS   Sirotkin,H., O'Donnell,H., DasGupta,R., Halford,S., St Jore,B.,
            Puech,A., Parimoo,S., Morrow,B., Skoultchi,A., Weissman,S.M.,
            Scambler,P. and Kucherlapati,R.
  TITLE     Identification of a new human catenin gene family member (ARVCF)
            from the region deleted in velo-cardio-facial syndrome
  JOURNAL   Genomics 41 (1), 75-83 (1997)
   PUBMED   9126485
REFERENCE   10 (residues 1 to 962)
  AUTHORS   Lindsay,E.A., Goldberg,R., Jurecic,V., Morrow,B., Carlson,C.,
            Kucherlapati,R.S., Shprintzen,R.J. and Baldini,A.
  TITLE     Velo-cardio-facial syndrome: frequency and extent of 22q11
            deletions
  JOURNAL   Am J Med Genet 57 (3), 514-522 (1995)
   PUBMED   7677167
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC005663.2 and U51269.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: Armadillo Repeat gene deleted in Velo-Cardio-Facial
            syndrome (ARVCF) is a member of the catenin family. This family
            plays an important role in the formation of adherens junction
            complexes, which are thought to facilitate communication between
            the inside and outside environments of a cell. The ARVCF gene was
            isolated in the search for the genetic defect responsible for the
            autosomal dominant Velo-Cardio-Facial syndrome (VCFS), a relatively
            common human disorder with phenotypic features including cleft
            palate, conotruncal heart defects and facial dysmorphology. The
            ARVCF gene encodes a protein containing two motifs, a coiled coil
            domain in the N-terminus and a 10 armadillo repeat sequence in the
            midregion. Since these sequences can facilitate protein-protein
            interactions ARVCF is thought to function in a protein complex. In
            addition, ARVCF contains a predicted nuclear-targeting sequence
            suggesting that it may have a function as a nuclear protein.
            [provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: U51269.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000263207.8/ ENSP00000263207.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..962
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.21"
     Protein         1..962
                     /product="splicing regulator ARVCF isoform 1"
                     /note="armadillo repeat protein deleted in
                     velo-cardio-facial syndrome; armadillo repeat gene deleted
                     in velocardiofacial syndrome; splicing regulator ARVCF"
                     /calculated_mol_wt=104511
     Region          95..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            102
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            170
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P98203; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          186..253
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          266..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            267
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            332
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            335
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            343
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          348..387
                     /region_name="ARM 1"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          360..385
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Site            order(376,380,384,418,422,426,461,466,470)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:293788"
     Region          389..428
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          390..429
                     /region_name="ARM 2"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          393..429
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          432..473
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          433..467
                     /region_name="ARM 3"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          436..471
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          468..508
                     /region_name="ARM 4"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          478..529
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          526..565
                     /region_name="ARM 5"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          575..622
                     /region_name="ARM 6"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          590..614
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            606
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          607..623
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            642
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Region          646..686
                     /region_name="ARM 7"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          656..692
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          656..692
                     /region_name="Arm"
                     /note="Armadillo/beta-catenin-like repeat; pfam00514"
                     /db_xref="CDD:425727"
     Region          699..738
                     /region_name="ARM 8"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          702..737
                     /region_name="ARM"
                     /note="Armadillo/beta-catenin-like repeats; smart00185"
                     /db_xref="CDD:214547"
     Region          702..736
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          739..781
                     /region_name="ARM 9"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          743..788
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          776..962
                     /region_name="Required for interaction with RNA-binding
                     proteins DDX5, HNRNPH2 and SRSF1 and with mRNAs.
                     /evidence=ECO:0000269|PubMed:24644279"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Region          794..826
                     /region_name="armadillo repeat"
                     /note="armadillo repeat [structural motif]"
                     /db_xref="CDD:293788"
     Region          854..962
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            864
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (O00192.1)"
     Site            871
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            872
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     Site            915
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O00192.1)"
     CDS             1..962
                     /gene="ARVCF"
                     /coded_by="NM_001670.3:308..3196"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS13771.1"
                     /db_xref="GeneID:421"
                     /db_xref="HGNC:HGNC:728"
                     /db_xref="MIM:602269"
ORIGIN      
        1 medcnvhsaa silasvkeqe arferltral eqerrhvalq leraqqpgmv sggmgsgqpl
       61 pmawqqlvlq eqspgsqasl atmpeapdvl eetvtveedp gtptshvsiv tsedgttrrt
      121 etkvtktvkt vttrtvrqvp vgpdglplld ggpplgpfad galdrhfllr gggpvatlsr
      181 aylssgggfp egpeprdsps ygslsrglgm rppragplgp gpgdgcftlp ghreafpvgp
      241 epgppggrsl perfqaepyg leddtrslaa ddeggpelep dygtatrrrp ecgrglhtra
      301 yedtaddgge laderpafpm vtaplaqper gsmgsldrlv rrspsvdsar keprwrdpel
      361 pevlamlrhp vdpvkanaaa ylqhlcfene gvkrrvrqlr glpllvalld hpraevrrra
      421 cgalrnlsyg rdtdnkaair dcggvpalvr llraardnev relvtgtlwn lssyeplkmv
      481 iidhglqtlt hevivphsgw erepnedskp rdaewttvfk ntsgclrnvs sdgaearrrl
      541 receglvdal lhalqsavgr kdtdnksven cvcimrnlsy hvhkevpgad ryqeaepgpl
      601 gsavgsqrrr rddascfggk kakeewfhqg kkdgemdrnf dtldlpkrte aakgfellyq
      661 pevvrlylsl ltesrnfntl eaaagalqnl sagnwmwaty iratvrkerg lpvlvellqs
      721 etdkvvrava ialrnlsldr rnkdligsya maelvrnvrn aqapprpgac leedtvvavl
      781 ntiheivsds ldnarsllqa rgvpalvalv assqsvreak aashvlqtvw sykelrgtlq
      841 kdgwtkarfq saaatakgpk galspggfdd stlplvdksl egektgsrdv ipmdalgpdg
      901 ystvdrrerr prgassagea sekeplkldp srkapppgps rpavrlvdav gdakpqpvds
      961 wv
//
LOCUS       NP_001309393             226 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3 domain-binding protein 5-like isoform 3 [Homo sapiens].
ACCESSION   NP_001309393
VERSION     NP_001309393.1
DBSOURCE    REFSEQ: accession NM_001322464.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 226)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 226)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 226)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 226)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 226)
  AUTHORS   Jenkins,M.L., Margaria,J.P., Stariha,J.T.B., Hoffmann,R.M.,
            McPhail,J.A., Hamelin,D.J., Boulanger,M.J., Hirsch,E. and
            Burke,J.E.
  TITLE     Structural determinants of Rab11 activation by the guanine
            nucleotide exchange factor SH3BP5
  JOURNAL   Nat Commun 9 (1), 3772 (2018)
   PUBMED   30217979
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 226)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Paulo,J.A., Cannon,J.R., Ting,L.,
            Baltier,K., Colby,G., Gebreab,F., Gygi,M.P., Parzen,H., Szpyt,J.,
            Tam,S., Zarraga,G., Pontano-Vaites,L., Swarup,S., White,A.E.,
            Schweppe,D.K., Rad,R., Erickson,B.K., Obar,R.A., Guruharsha,K.G.,
            Li,K., Artavanis-Tsakonas,S., Gygi,S.P. and Harper,J.W.
  TITLE     Architecture of the human interactome defines protein communities
            and disease networks
  JOURNAL   Nature 545 (7655), 505-509 (2017)
   PUBMED   28514442
REFERENCE   8  (residues 1 to 226)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   9  (residues 1 to 226)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   10 (residues 1 to 226)
  AUTHORS   Clark,H.F., Gurney,A.L., Abaya,E., Baker,K., Baldwin,D., Brush,J.,
            Chen,J., Chow,B., Chui,C., Crowley,C., Currell,B., Deuel,B.,
            Dowd,P., Eaton,D., Foster,J., Grimaldi,C., Gu,Q., Hass,P.E.,
            Heldens,S., Huang,A., Kim,H.S., Klimowski,L., Jin,Y., Johnson,S.,
            Lee,J., Lewis,L., Liao,D., Mark,M., Robbie,E., Sanchez,C.,
            Schoenfeld,J., Seshagiri,S., Simmons,L., Singh,J., Smith,V.,
            Stinson,J., Vagts,A., Vandlen,R., Watanabe,C., Wieand,D., Woods,K.,
            Xie,M.H., Yansura,D., Yi,S., Yu,G., Yuan,J., Zhang,M., Zhang,Z.,
            Goddard,A., Wood,W.I., Godowski,P. and Gray,A.
  TITLE     The secreted protein discovery initiative (SPDI), a large-scale
            effort to identify novel human secreted and transmembrane proteins:
            a bioinformatics assessment
  JOURNAL   Genome Res 13 (10), 2265-2270 (2003)
   PUBMED   12975309
  REMARK    Erratum:[Genome Res. 2003 Dec;13(12):2759]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL732583.5.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.280496.1,
                                           SRR1803616.177948.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..226
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q44"
     Protein         1..226
                     /product="SH3 domain-binding protein 5-like isoform 3"
                     /note="SH3 domain-binding protein 5-like; SH3BP-5-like"
                     /calculated_mol_wt=24279
     Region          <27..116
                     /region_name="SH3BP5"
                     /note="SH3 domain-binding protein 5 (SH3BP5); pfam05276"
                     /db_xref="CDD:461608"
     CDS             1..226
                     /gene="SH3BP5L"
                     /coded_by="NM_001322464.2:1097..1777"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:80851"
                     /db_xref="HGNC:HGNC:29360"
                     /db_xref="MIM:620652"
ORIGIN      
        1 mgpgsvmcpl gqvneaeeer lrgerehqrv trlcqqaear vqalqktlrr aigksrpyfe
       61 lkaqfsqile ehkakvtele qqvaqaktry svalrnleqi seqiharrrg glpphplgpr
      121 rsspvgaeag pedmedgdsg iegaegagle egsslgpgpa pdtdtlslls lrtvasdlqk
      181 cdsvehlrgl sdhvsldgqe lgtrsggrrg sdggarggrh qrsvsl
//
LOCUS       NP_001177410            1275 aa            linear   PRI 20-NOV-2025
DEFINITION  claspin isoform 2 [Homo sapiens].
ACCESSION   NP_001177410
VERSION     NP_001177410.1
DBSOURCE    REFSEQ: accession NM_001190481.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1275)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1275)
  AUTHORS   Hsieh,M.J., Lo,Y.S., Ho,H.Y., Lin,C.C., Chuang,Y.C. and Chen,M.K.
  TITLE     The Interaction between CLSPN Gene Polymorphisms and Alcohol
            Consumption Contributes to Oral Cancer Progression
  JOURNAL   Int J Mol Sci 25 (2), 1098 (2024)
   PUBMED   38256171
  REMARK    GeneRIF: The Interaction between CLSPN Gene Polymorphisms and
            Alcohol Consumption Contributes to Oral Cancer Progression.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1275)
  AUTHORS   Jia,Y., Cheng,X., Liang,W., Lin,S., Li,P., Yan,Z., Zhang,M., Ma,W.,
            Hu,C., Wang,B. and Liu,Z.
  TITLE     CLSPN is a potential biomarker associated with poor prognosis in
            low-grade gliomas based on a multi-database analysis
  JOURNAL   Curr Res Transl Med 70 (4), 103345 (2022)
   PUBMED   35487167
  REMARK    GeneRIF: CLSPN is a potential biomarker associated with poor
            prognosis in low-grade gliomas based on a multi-database analysis.
REFERENCE   4  (residues 1 to 1275)
  AUTHORS   Benz,C., Ali,M., Krystkowiak,I., Simonetti,L., Sayadi,A.,
            Mihalic,F., Kliche,J., Andersson,E., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Proteome-scale mapping of binding sites in the unstructured regions
            of the human proteome
  JOURNAL   Mol Syst Biol 18 (1), e10584 (2022)
   PUBMED   35044719
REFERENCE   5  (residues 1 to 1275)
  AUTHORS   Hu,T., Lei,D., Zhou,J. and Zhang,B.O.
  TITLE     circRNA derived from CLSPN (circCLSPN) is an oncogene in human
            glioblastoma multiforme by regulating cell growth, migration and
            invasion via ceRNA pathway
  JOURNAL   J Biosci 46 (2021)
   PUBMED   34269180
  REMARK    GeneRIF: circRNA derived from CLSPN (circCLSPN) is an oncogene in
            human glioblastoma multiforme by regulating cell growth, migration
            and invasion via ceRNA pathway.
REFERENCE   6  (residues 1 to 1275)
  AUTHORS   Lin,S.Y., Li,K., Stewart,G.S. and Elledge,S.J.
  TITLE     Human Claspin works with BRCA1 to both positively and negatively
            regulate cell proliferation
  JOURNAL   Proc Natl Acad Sci U S A 101 (17), 6484-6489 (2004)
   PUBMED   15096610
  REMARK    GeneRIF: determination of properties of both a tumor suppressor and
            an oncogene
REFERENCE   7  (residues 1 to 1275)
  AUTHORS   Chini,C.C. and Chen,J.
  TITLE     Human claspin is required for replication checkpoint control
  JOURNAL   J Biol Chem 278 (32), 30057-30062 (2003)
   PUBMED   12766152
  REMARK    GeneRIF: Claspin has a potentially critical role in replication
            checkpoint control in mammalian cells
REFERENCE   8  (residues 1 to 1275)
  AUTHORS   Zou,L. and Elledge,S.J.
  TITLE     Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
  JOURNAL   Science 300 (5625), 1542-1548 (2003)
   PUBMED   12791985
REFERENCE   9  (residues 1 to 1275)
  AUTHORS   Kumagai,A. and Dunphy,W.G.
  TITLE     Claspin, a novel protein required for the activation of Chk1 during
            a DNA replication checkpoint response in Xenopus egg extracts
  JOURNAL   Mol Cell 6 (4), 839-849 (2000)
   PUBMED   11090622
REFERENCE   10 (residues 1 to 1275)
  AUTHORS   Calderari,G.
  TITLE     [Inlays in the prosthetic rehabilitation of the periodontal
            patient]
  JOURNAL   Dent Cadmos 34 (11), 1509-1537 (1966)
   PUBMED   5226314
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL354864.16, AF297866.1,
            BC115025.1 and BC137279.1.
            
            Summary: The product of this gene is an essential upstream
            regulator of checkpoint kinase 1 and triggers a checkpoint arrest
            of the cell cycle in response to replicative stress or DNA damage.
            The protein is also required for efficient DNA replication during a
            normal S phase. Multiple transcript variants encoding different
            isoforms have been found for this gene. [provided by RefSeq, Jun
            2010].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon in the central coding region, compared to variant 1. The
            resulting isoform (2) lacks an internal segment, compared to
            isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC115025.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1275
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.3"
     Protein         1..1275
                     /product="claspin isoform 2"
                     /note="claspin homolog"
                     /calculated_mol_wt=144036
     CDS             1..1275
                     /gene="CLSPN"
                     /coded_by="NM_001190481.2:109..3936"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS53297.1"
                     /db_xref="GeneID:63967"
                     /db_xref="HGNC:HGNC:19715"
                     /db_xref="MIM:605434"
ORIGIN      
        1 mtgevgsevh leindpnvis qeeadspsds gqgsyetigp lsegdsdeei fvskklknrk
       61 vlqdsdsete dtnaspektt ydsaeeenke nlyagkntki kriyktvads desymeksly
      121 qenleaqvkp clelslqsgn stdfttdrks skkhihdkeg tagkakvksk rrlekeerkm
      181 ekirqlkkke tknqeddveq pfndsgcllv dkdlfetgle dennsplede eslesiraav
      241 knkvkkhkkk epslesgvhs feegselskg ttrkerkaar lskealkqlh setqrlires
      301 alnlpyhmpe nktihdffkr kprptchgna mallksskyq sshhkeiidt anttemnsdh
      361 hskgseqttg aenevetnal pvvsketqii tgsdescrkd lvkneeleiq ekqkqsdirp
      421 spgdssvlqq esnflgnnhs eecqvgglva fephalegeg pqnpeetdek veepeqqnks
      481 savgppekvr rftldrlkql gvdvsikprl gadedsfvil epetnrgekl qvlkaklqea
      541 mklrrfeerq krqalfkldn edgfeeeeee eeemtdesee dgeekvekee keeeleeeee
      601 keeeeeeegn qetaefllss eeietkdeke mdkenndgss eigkavgfls vpkslssdst
      661 lllfkdsssk mgyfpteeks etdensgkqp skldeddscs lltkesshns sfeligstip
      721 syqpcnrqtg rgtsffptag gfrspspglf raslvssask ssgklsepsl piedsqdlyn
      781 aspepktlfl gagdfqfcle ddtqsqllda dgflnvrnhr nqyqalkprl plasmdenam
      841 danmdelldl ctgkftsqae khlprksdkk enmeellnlc sgkftsqdas tpasselnkq
      901 ekessmgdpm eealalcsgs fptdkeeede eeefgdfrlv sndnefdsde dehsdsgndl
      961 aledheddde eellkrsekl krqmrlrkyl edeaevsgsd vgsedeydge eideyeedvi
     1021 devlpsdeel qsqikkihmk tmldddkrql rlyqerylad gdlhsdgpgr mrkfrwknid
     1081 dasqmdlfhr dsdddqteeq ldesearwrk eriereqwlr dmaqqgkita eeeeeigeds
     1141 qfmilakkvt akalqknasr pmviqesksl lrnpfeairp gsaqqvktgs llnqpkavlq
     1201 klaalsdhnp saprnsrnfv fhtlspvkae aakessksqv kkrgpsfmts pspkhlktdd
     1261 stsgltrsif kyles
//
LOCUS       NP_001035828             525 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein RO60 isoform 1 [Homo sapiens].
ACCESSION   NP_001035828
VERSION     NP_001035828.1
DBSOURCE    REFSEQ: accession NM_001042369.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 525)
  AUTHORS   Song,Y., Wei,F., Liu,Y., Han,F., Ma,L., Zhuang,Y., Pan,C., Jia,Z.
            and Gong,A.
  TITLE     IL-33/ST2 Activation Is involved in Ro60-Regulated Photosensitivity
            in Cutaneous Lupus Erythematosus
  JOURNAL   Mediators Inflamm 2022, 4955761 (2022)
   PUBMED   35909659
  REMARK    GeneRIF: IL-33/ST2 Activation Is involved in Ro60-Regulated
            Photosensitivity in Cutaneous Lupus Erythematosus.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 525)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 525)
  AUTHORS   Lee,A.Y.S., Beroukas,D., Brown,L., Lucchesi,C., Kaur,A., Gyedu,L.,
            Hughes,N., Ng,Y.H., Saran,O., Gordon,T.P. and Wang,J.J.
  TITLE     Identification of a unique anti-Ro60 subset with restricted
            serological and molecular profiles
  JOURNAL   Clin Exp Immunol 203 (1), 13-21 (2021)
   PUBMED   32852779
  REMARK    GeneRIF: Identification of a unique anti-Ro60 subset with
            restricted serological and molecular profiles.
REFERENCE   4  (residues 1 to 525)
  AUTHORS   Leng,Y., Sim,S., Magidson,V. and Wolin,S.L.
  TITLE     Noncoding Y RNAs regulate the levels, subcellular distribution and
            protein interactions of their Ro60 autoantigen partner
  JOURNAL   Nucleic Acids Res 48 (12), 6919-6930 (2020)
   PUBMED   32469055
  REMARK    GeneRIF: Noncoding Y RNAs regulate the levels, subcellular
            distribution and protein interactions of their Ro60 autoantigen
            partner.
REFERENCE   5  (residues 1 to 525)
  AUTHORS   Barcellos,K.S., Nonogaki,S., Enokihara,M.M., Teixeira,M.S. and
            Andrade,L.E.
  TITLE     Differential expression of Ro/SSA 60 kDa and La/SSB, but not Ro/SSA
            52 kDa, mRNA and protein in minor salivary glands from patients
            with primary Sjogren's syndrome
  JOURNAL   J Rheumatol 34 (6), 1283-1292 (2007)
   PUBMED   17552056
  REMARK    GeneRIF: Increased Ro/SSA 60 and La/SSB mRNA expression in minor
            salivary glands in primary Sjogren's syndrome (pSS) suggest that
            these 2 autoantigens, but not Ro/SSA 52, are involved in
            tissue-specific autoimmune response in pSS.
REFERENCE   6  (residues 1 to 525)
  AUTHORS   Pruijn,G.J., Slobbe,R.L. and van Venrooij,W.J.
  TITLE     Analysis of protein--RNA interactions within Ro ribonucleoprotein
            complexes
  JOURNAL   Nucleic Acids Res 19 (19), 5173-5180 (1991)
   PUBMED   1833722
REFERENCE   7  (residues 1 to 525)
  AUTHORS   Jitsukawa,T., Nakajima,S., Usui,J. and Watanabe,H.
  TITLE     Detection of anti-nuclear antibodies from patients with systemic
            rheumatic diseases by ELISA using HEp-2 cell nuclei
  JOURNAL   J Clin Lab Anal 5 (1), 49-53 (1991)
   PUBMED   1999763
REFERENCE   8  (residues 1 to 525)
  AUTHORS   James,J.A., Dickey,W.D., Fujisaku,A., O'Brien,C.A., Deutscher,S.L.,
            Keene,J.D. and Harley,J.B.
  TITLE     Antigenicity of a recombinant Ro (SS-A) fusion protein
  JOURNAL   Arthritis Rheum 33 (1), 102-106 (1990)
   PUBMED   1689160
REFERENCE   9  (residues 1 to 525)
  AUTHORS   Ben-Chetrit,E., Gandy,B.J., Tan,E.M. and Sullivan,K.F.
  TITLE     Isolation and characterization of a cDNA clone encoding the 60-kD
            component of the human SS-A/Ro ribonucleoprotein autoantigen
  JOURNAL   J Clin Invest 83 (4), 1284-1292 (1989)
   PUBMED   2649513
REFERENCE   10 (residues 1 to 525)
  AUTHORS   Deutscher,S.L., Harley,J.B. and Keene,J.D.
  TITLE     Molecular analysis of the 60-kDa human Ro ribonucleoprotein
  JOURNAL   Proc Natl Acad Sci U S A 85 (24), 9479-9483 (1988)
   PUBMED   3200833
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CX761715.1, M25077.1 and AI433657.1.
            
            Transcript Variant: This variant (1) encodes isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: M25077.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..525
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31.2"
     Protein         1..525
                     /product="RNA-binding protein RO60 isoform 1"
                     /note="Sjogren syndrome antigen A2 (60kD,
                     ribonucleoprotein autoantigen SS-A/Ro); gastric cancer
                     multi-drug resistance protein; TROVE domain family member
                     2; 60 kDa ribonucleoprotein Ro; sjoegren syndrome type A
                     antigen; Ro/SSA 60kDa; ro60 autoantigen; RNA-binding
                     protein RO60"
                     /calculated_mol_wt=59139
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.9,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895;
                     propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            4
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          17..369
                     /region_name="TROVE"
                     /note="TROVE domain; pfam05731"
                     /db_xref="CDD:461724"
     Site            19
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          120..284
                     /region_name="RNA-binding. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P10155.2)"
     Site            224
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Site            359
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P10155.2)"
     Region          <363..489
                     /region_name="ViaA"
                     /note="Uncharacterized conserved protein, contains a von
                     Willebrand factor type A (vWA) domain [Function unknown];
                     COG2425"
                     /db_xref="CDD:441973"
     CDS             1..525
                     /gene="RO60"
                     /gene_synonym="RORNP; SSA2; TROVE2"
                     /coded_by="NM_001042369.2:371..1948"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS41449.1"
                     /db_xref="GeneID:6738"
                     /db_xref="HGNC:HGNC:11313"
                     /db_xref="MIM:600063"
ORIGIN      
        1 meesvnqmqp lnekqiansq dgyvwqvtdm nrlhrflcfg seggtyyike qklglenaea
       61 lirliedgrg ceviqeiksf sqegrttkqe pmlfalaics qcsdistkqa afkavsevcr
      121 ipthlftfiq fkkdlkesmk cgmwgralrk aiadwynekg gmalalavtk ykqrngwshk
      181 dllrlshlkp sseglaivtk yitkgwkevh elykekalsv etekllkyle avekvkrtrd
      241 elevihliee hrlvrehllt nhlkskevwk allqemplta llrnlgkmta nsvlepgnse
      301 vslvceklcn ekllkkarih pfhilialet yktghglrgk lkwrpdeeil kaldaafykt
      361 fktveptgkr fllavdvsas mnqrvlgsil nastvaaamc mvvtrtekds yvvafsdemv
      421 pcpvttdmtl qqvlmamsqi paggtdcslp miwaqktntp advfivftdn etfaggvhpa
      481 ialreyrkkm dipaklivcg mtsngftiad pddralqntl lnksf
//
LOCUS       NP_001128650             534 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 397 isoform 1 [Homo sapiens].
ACCESSION   NP_001128650
VERSION     NP_001128650.1
DBSOURCE    REFSEQ: accession NM_001135178.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 534)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 534)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 534)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 534)
  AUTHORS   Helleboid,P.Y., Heusel,M., Duc,J., Piot,C., Thorball,C.W.,
            Coluccio,A., Pontis,J., Imbeault,M., Turelli,P., Aebersold,R. and
            Trono,D.
  TITLE     The interactome of KRAB zinc finger proteins reveals the
            evolutionary history of their functional diversification
  JOURNAL   EMBO J 38 (18), e101220 (2019)
   PUBMED   31403225
REFERENCE   5  (residues 1 to 534)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 534)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   7  (residues 1 to 534)
  AUTHORS   Ravasi,T., Suzuki,H., Cannistraci,C.V., Katayama,S., Bajic,V.B.,
            Tan,K., Akalin,A., Schmeier,S., Kanamori-Katayama,M., Bertin,N.,
            Carninci,P., Daub,C.O., Forrest,A.R., Gough,J., Grimmond,S.,
            Han,J.H., Hashimoto,T., Hide,W., Hofmann,O., Kamburov,A., Kaur,M.,
            Kawaji,H., Kubosaki,A., Lassmann,T., van Nimwegen,E.,
            MacPherson,C.R., Ogawa,C., Radovanovic,A., Schwartz,A.,
            Teasdale,R.D., Tegner,J., Lenhard,B., Teichmann,S.A., Arakawa,T.,
            Ninomiya,N., Murakami,K., Tagami,M., Fukuda,S., Imamura,K., Kai,C.,
            Ishihara,R., Kitazume,Y., Kawai,J., Hume,D.A., Ideker,T. and
            Hayashizaki,Y.
  TITLE     An atlas of combinatorial transcriptional regulation in mouse and
            man
  JOURNAL   Cell 140 (5), 744-752 (2010)
   PUBMED   20211142
  REMARK    Erratum:[Cell. 2010 Apr 16;141(2):369. Kamburov, Atanas [added];
            Kaur, Mandeep [added]; MacPherson, Cameron Ross [added];
            Radovanovic, Aleksandar [added]; Schwartz, Ariel [added]]
REFERENCE   8  (residues 1 to 534)
  AUTHORS   Bailey,S.L., Chang,S.C., Griffiths,B., Graham,A.N., Saffery,R.,
            Earle,E., Choo,K.H. and Kalitsis,P.
  TITLE     ZNF397, a new class of interphase to early prophase-specific,
            SCAN-zinc-finger, mammalian centromere protein
  JOURNAL   Chromosoma 117 (4), 367-380 (2008)
   PUBMED   18369653
  REMARK    GeneRIF: ZNF397, a new class of interphase to early
            prophase-specific, SCAN-zinc-finger, mammalian centromere protein.
REFERENCE   9  (residues 1 to 534)
  AUTHORS   Wu,Y., Yu,L., Bi,G., Luo,K., Zhou,G. and Zhao,S.
  TITLE     Identification and characterization of two novel human SCAN
            domain-containing zinc finger genes ZNF396 and ZNF397
  JOURNAL   Gene 310, 193-201 (2003)
   PUBMED   12801647
REFERENCE   10 (residues 1 to 534)
  AUTHORS   Lichter,P., Bray,P., Ried,T., Dawid,I.B. and Ward,D.C.
  TITLE     Clustering of C2-H2 zinc finger motif sequences within telomeric
            and fragile site regions of human chromosomes
  JOURNAL   Genomics 13 (4), 999-1007 (1992)
   PUBMED   1505991
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI772202.1, BC006172.1,
            AF533250.2 and AC011815.7.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a protein with a N-terminal SCAN domain,
            and the longer isoform contains nine C2H2-type zinc finger repeats
            in the C-terminal domain. The protein localizes to centromeres
            during interphase and early prophase, and different isoforms can
            repress or activate transcription in transfection studies. Multiple
            transcript variants encoding different isoforms have been found for
            this gene. Additional variants have been described, but their
            biological validity has not been determined. [provided by RefSeq,
            Oct 2009].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1), also known as ZNF397-fu.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF533250.2, SRR5189664.55667.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000330501.12/ ENSP00000331577.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..534
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.2"
     Protein         1..534
                     /product="zinc finger protein 397 isoform 1"
                     /note="zinc finger protein 47; zinc finger and SCAN
                     domain-containing protein 15"
                     /calculated_mol_wt=61008
     Site            31
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NF99.2)"
     Region          46..152
                     /region_name="SCAN"
                     /note="leucine rich region; smart00431"
                     /db_xref="CDD:128708"
     Region          180..217
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NF99.2)"
     Region          <278..527
                     /region_name="COG5048"
                     /note="FOG: Zn-finger [General function prediction only]"
                     /db_xref="CDD:227381"
     Region          287..307
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          315..335
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          343..363
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          371..391
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          399..419
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(404,406,408,410..411,414..415,418,432,434,438..439,
                     442..443,446,460,462,464,466..467,470..471,474)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          427..447
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          455..475
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          483..503
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          511..531
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..534
                     /gene="ZNF397"
                     /gene_synonym="ZNF47; ZSCAN15"
                     /coded_by="NM_001135178.3:157..1761"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45852.1"
                     /db_xref="GeneID:84307"
                     /db_xref="HGNC:HGNC:18818"
                     /db_xref="MIM:609601"
ORIGIN      
        1 mavesgvist lipqdppeqe lilvkvednf swdekfkqng stqscqelfr qqfrkfcyqe
       61 tpgprealsr lqelcyqwlm pelhtkeqil ellvleqfls ilpeelqiwv qqhnpesgee
      121 avtlledler efddpgqqvp aspqgpavpw kdltclrasq estdihlqpl ktqlkswkpc
      181 lspksdcens etatkegise eksqglpqep sfrgisehes nlvwkqgsat geklrspsqg
      241 gsfsqviftn kslgkrdlyd eaercliltt dsimcqkvpp eerpyrcdvc ghsfkqhssl
      301 tqhqrihtge kpykcnqcgk afslrsylii hqrihsgeka yecsecgkaf nqssalirhr
      361 kihtgekack cnecgkafsq ssyliihqri htgekpyecn ecgktfsqss klirhqriht
      421 gerpyecnec gkafrqssel ithqrihsge kpyecsecgk afslssnlir hqrihsgeep
      481 yqcnecgktf krssalvqhq rihsgdeayi cnecgkafrh rsvlmrhqrv htik
//
LOCUS       NP_001159522             758 aa            linear   PRI 20-NOV-2025
DEFINITION  amyloid beta precursor protein binding family B member 2 isoform b
            [Homo sapiens].
ACCESSION   NP_001159522
VERSION     NP_001159522.1
DBSOURCE    REFSEQ: accession NM_001166050.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 758)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 758)
  AUTHORS   Viard,J., Loe-Mie,Y., Daudin,R., Khelfaoui,M., Plancon,C.,
            Boland,A., Tejedor,F., Huganir,R.L., Kim,E., Kinoshita,M., Liu,G.,
            Haucke,V., Moncion,T., Yu,E., Hindie,V., Blehaut,H., Mircher,C.,
            Herault,Y., Deleuze,J.F., Rain,J.C., Simonneau,M. and
            Lepagnol-Bestel,A.M.
  TITLE     Chr21 protein-protein interactions: enrichment in proteins involved
            in intellectual disability, autism, and late-onset Alzheimer's
            disease
  JOURNAL   Life Sci Alliance 5 (12), e202101205 (2022)
   PUBMED   35914814
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 758)
  AUTHORS   Xu,L.B., Xiong,J., Zhang,Y.H., Dai,Y., Ren,X.P., Ren,Y.J., Han,D.,
            Wei,S.H. and Qi,M.
  TITLE     miR-205-3p promotes lung cancer progression by targeting APBB2
  JOURNAL   Mol Med Rep 24 (2) (2021)
   PUBMED   34165160
  REMARK    GeneRIF: miR2053p promotes lung cancer progression by targeting
            APBB2.
REFERENCE   4  (residues 1 to 758)
  AUTHORS   Zhou,K., Cao,D., Wang,Y., Wang,L. and Meng,X.
  TITLE     Hsa-miR-30a-3p attenuates gastric adenocarcinoma proliferation and
            metastasis via APBB2
  JOURNAL   Aging (Albany NY) 13 (12), 16763-16772 (2021)
   PUBMED   34182542
  REMARK    GeneRIF: Hsa-miR-30a-3p attenuates gastric adenocarcinoma
            proliferation and metastasis via APBB2.
REFERENCE   5  (residues 1 to 758)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 758)
  AUTHORS   Chang,Y., Tesco,G., Jeong,W.J., Lindsley,L., Eckman,E.A.,
            Eckman,C.B., Tanzi,R.E. and Guenette,S.Y.
  TITLE     Generation of the beta-amyloid peptide and the amyloid precursor
            protein C-terminal fragment gamma are potentiated by FE65L1
  JOURNAL   J Biol Chem 278 (51), 51100-51107 (2003)
   PUBMED   14527950
  REMARK    GeneRIF: FE65L1 potentiates gamma-secretase processing of APP CTFs.
            This requires binding of FE65L1 to APP and APP CTFs. Enhanced APP
            CTF processing can be detected in early endosome vesicles
REFERENCE   7  (residues 1 to 758)
  AUTHORS   Bruni,P., Minopoli,G., Brancaccio,T., Napolitano,M., Faraonio,R.,
            Zambrano,N., Hansen,U. and Russo,T.
  TITLE     Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein,
            blocks cell cycle progression by down-regulating thymidylate
            synthase expression
  JOURNAL   J Biol Chem 277 (38), 35481-35488 (2002)
   PUBMED   12089154
REFERENCE   8  (residues 1 to 758)
  AUTHORS   Blanco,G., Irving,N.G., Brown,S.D., Miller,C.C. and McLoughlin,D.M.
  TITLE     Mapping of the human and murine X11-like genes (APBA2 and apba2),
            the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2):
            genes encoding phosphotyrosine-binding domain proteins that
            interact with the Alzheimer's disease amyloid precursor protein
  JOURNAL   Mamm Genome 9 (6), 473-475 (1998)
   PUBMED   9585438
REFERENCE   9  (residues 1 to 758)
  AUTHORS   McLoughlin,D.M. and Miller,C.C.
  TITLE     The intracellular cytoplasmic domain of the Alzheimer's disease
            amyloid precursor protein interacts with phosphotyrosine-binding
            domain proteins in the yeast two-hybrid system
  JOURNAL   FEBS Lett 397 (2-3), 197-200 (1996)
   PUBMED   8955346
REFERENCE   10 (residues 1 to 758)
  AUTHORS   Guenette,S.Y., Chen,J., Jondro,P.D. and Tanzi,R.E.
  TITLE     Association of a novel human FE65-like protein with the cytoplasmic
            domain of the beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 93 (20), 10832-10837 (1996)
   PUBMED   8855266
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB236935.1, AK304247.1,
            AK295974.1, BC027946.1, AC131953.1 and AL080130.1.
            
            Summary: The protein encoded by this gene interacts with the
            cytoplasmic domains of amyloid beta (A4) precursor protein and
            amyloid beta (A4) precursor-like protein 2. This protein contains
            two phosphotyrosine binding (PTB) domains, which are thought to
            function in signal transduction. Polymorphisms in this gene have
            been associated with Alzheimer's disease. Alternative splicing
            results in multiple transcript variants. [provided by RefSeq, Oct
            2009].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (b) that is 1 aa shorter than isoform a.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK304247.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..758
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p14-p13"
     Protein         1..758
                     /product="amyloid beta precursor protein binding family B
                     member 2 isoform b"
                     /note="Fe65-like 1; protein Fe65-like 1"
                     /calculated_mol_wt=83243
     Site            123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          134..154
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          176..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Region          206..295
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Region          292..320
                     /region_name="WW"
                     /note="WW domain; pfam00397"
                     /db_xref="CDD:459800"
     Region          326..351
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q92870.3)"
     Site            334
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR4; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Site            412
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9DBR4; propagated from
                     UniProtKB/Swiss-Prot (Q92870.3)"
     Region          416..553
                     /region_name="PTB1_Fe65"
                     /note="Fe65 N-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01272"
                     /db_xref="CDD:269970"
     Site            order(431,499,516)
                     /site_type="other"
                     /note="phosphoinositide binding site [chemical binding]"
                     /db_xref="CDD:269970"
     Site            order(498..503,516,538,542)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:269970"
     Region          582..708
                     /region_name="PTB2_Fe65"
                     /note="Fe65 C-terminal Phosphotyrosine-binding (PTB)
                     domain; cd01271"
                     /db_xref="CDD:269969"
     Site            order(593,667,686)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:269969"
     Site            order(604,606,654..655,657..664,666,674,680,690,692,695,
                     699,702..703,705..706)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:269969"
     CDS             1..758
                     /gene="APBB2"
                     /gene_synonym="FE65L; FE65L1"
                     /coded_by="NM_001166050.2:555..2831"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS54761.1"
                     /db_xref="GeneID:323"
                     /db_xref="HGNC:HGNC:582"
                     /db_xref="MIM:602710"
ORIGIN      
        1 msevlpadsg vdtlavfmas sgttdvtnrn spatppntln lrsshnelln aeikhtetkn
       61 stppkcrkky altniqaamg lsdpaaqpll gngsaniklv kngenqlrka aeqgqqdpnk
      121 nlsptavini tseklegkep hpqdssscei lpsqprrtks flnyyadlet sareleqnrg
      181 nhhgtaeeks qpvqgqasti igngdlllqk pnrpqssped gqvatvsssp etkkdhpktg
      241 aktdcalhri qnlapsdees swttlsqdsa spsspdetdi wsdhsfqtdp dlppgwkrvs
      301 diagtyywhi ptgttqwerp vsipadlqgs rkgslssvtp sptpenekqp wsdfavlngg
      361 kinsdiwkdl haatvnpdps lkefegatlr yaslklrnap hpddddscsi nsdpeakcfa
      421 vrslgwvema eedlapgkss vavnncirql syckndirdt vgiwgegkdm ylilendmls
      481 lvdpmdrsvl hsqpivsirv wgvgrdngrd fayvardkdt rilkchvfrc dtpakaiats
      541 lheicskima erknakalac sslqeranvn ldvplqvdfp tpktelvqkf hvqylgmlpv
      601 dkpvgmdiln saienlmtss nkedwlsvnm nvadatvtvi sekneeevlv ecrvrflsfm
      661 gvgkdvhtfa fimdtgnqrf echvfwcepn agnvseavqa acmlryqkcl varppsqkvr
      721 pppppadsvt rrvttnvkrg vlslidtlkq krpvtemp
//
LOCUS       NP_004955                482 aa            linear   PRI 20-NOV-2025
DEFINITION  histone deacetylase 1 [Homo sapiens].
ACCESSION   NP_004955
VERSION     NP_004955.2
DBSOURCE    REFSEQ: accession NM_004964.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 482)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 482)
  AUTHORS   Chen,W., Chu,J., Miao,Y., Jiang,W., Wang,F., Zhang,N., Jin,J. and
            Cai,Y.
  TITLE     MOF-mediated acetylation of CDK9 promotes global transcription by
            modulating P-TEFb complex formation
  JOURNAL   FEBS J 291 (21), 4796-4812 (2024)
   PUBMED   39250546
REFERENCE   3  (residues 1 to 482)
  AUTHORS   Kanojia,A., Roy,G., Madhubala,R. and Muthuswami,R.
  TITLE     Interplay between DOT1L and HDAC1 regulates Leishmania donovani
            infection in human THP-1 cells
  JOURNAL   Acta Trop 258, 107352 (2024)
   PUBMED   39103111
  REMARK    GeneRIF: Interplay between DOT1L and HDAC1 regulates Leishmania
            donovani infection in human THP-1 cells.
REFERENCE   4  (residues 1 to 482)
  AUTHORS   Di Giorgio,E., Dalla,E., Tolotto,V., D'Este,F., Paluvai,H.,
            Ranzino,L. and Brancolini,C.
  TITLE     HDAC4 influences the DNA damage response and counteracts senescence
            by assembling with HDAC1/HDAC2 to control H2BK120 acetylation and
            homology-directed repair
  JOURNAL   Nucleic Acids Res 52 (14), 8218-8240 (2024)
   PUBMED   38874468
  REMARK    GeneRIF: HDAC4 influences the DNA damage response and counteracts
            senescence by assembling with HDAC1/HDAC2 to control H2BK120
            acetylation and homology-directed repair.
REFERENCE   5  (residues 1 to 482)
  AUTHORS   Kong,Y., Jiang,R., Zhou,H., Ge,M., Lin,H., Wang,Y., Yao,R.,
            Wang,Q., Liang,X., Li,J. and Zhou,X.
  TITLE     PHF12 regulates HDAC1 to promote tumorigenesis via EGFR/AKT
            signaling pathway in non-small cell lung cancer
  JOURNAL   J Transl Med 22 (1), 689 (2024)
   PUBMED   39075515
  REMARK    GeneRIF: PHF12 regulates HDAC1 to promote tumorigenesis via
            EGFR/AKT signaling pathway in non-small cell lung cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 482)
  AUTHORS   Taunton,J., Hassig,C.A. and Schreiber,S.L.
  TITLE     A mammalian histone deacetylase related to the yeast
            transcriptional regulator Rpd3p
  JOURNAL   Science 272 (5260), 408-411 (1996)
   PUBMED   8602529
REFERENCE   7  (residues 1 to 482)
  AUTHORS   Wolffe,A.P.
  TITLE     Histone deacetylase: a regulator of transcription
  JOURNAL   Science 272 (5260), 371-372 (1996)
   PUBMED   8602525
  REMARK    Review article
REFERENCE   8  (residues 1 to 482)
  AUTHORS   Furukawa,Y., Kawakami,T., Sudo,K., Inazawa,J., Matsumine,A.,
            Akiyama,T. and Nakamura,Y.
  TITLE     Isolation and mapping of a human gene (RPD3L1) that is homologous
            to RPD3, a transcription factor in Saccharomyces cerevisiae
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 130-133 (1996)
   PUBMED   8646880
REFERENCE   9  (residues 1 to 482)
  AUTHORS   Hijmans,E.M., Voorhoeve,P.M., Beijersbergen,R.L., van 't Veer,L.J.
            and Bernards,R.
  TITLE     E2F-5, a new E2F family member that interacts with p130 in vivo
  JOURNAL   Mol Cell Biol 15 (6), 3082-3089 (1995)
   PUBMED   7760804
REFERENCE   10 (residues 1 to 482)
  AUTHORS   Margolis,D.M., Somasundaran,M. and Green,M.R.
  TITLE     Human transcription factor YY1 represses human immunodeficiency
            virus type 1 transcription and virion production
  JOURNAL   J Virol 68 (2), 905-910 (1994)
   PUBMED   8289393
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109945.15.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 26, 2001 this sequence version replaced NP_004955.1.
            
            Summary: Histone acetylation and deacetylation, catalyzed by
            multisubunit complexes, play a key role in the regulation of
            eukaryotic gene expression. The protein encoded by this gene
            belongs to the histone deacetylase/acuc/apha family and is a
            component of the histone deacetylase complex. It also interacts
            with retinoblastoma tumor-suppressor protein and this complex is a
            key element in the control of cell proliferation and
            differentiation. Together with metastasis-associated protein-2, it
            deacetylates p53 and modulates its effect on cell growth and
            apoptosis. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163657.10339.1,
                                           SRR1803611.177301.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373548.8/ ENSP00000362649.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..482
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.2-p35.1"
     Protein         1..482
                     /product="histone deacetylase 1"
                     /EC_number="3.5.1.98"
                     /note="reduced potassium dependency, yeast homolog-like 1;
                     protein deacetylase HDAC1; protein decrotonylase HDAC1;
                     protein deacylase HDAC1"
                     /calculated_mol_wt=54972
     Region          4..374
                     /region_name="HDAC1"
                     /note="Histone deacetylase 1 (HDAC1); cd10010"
                     /db_xref="CDD:212534"
     Region          9..321
                     /region_name="Histone deacetylase"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            74
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            order(140..141,149..150,176,178,264,271,301,303)
                     /site_type="active"
                     /db_xref="CDD:212534"
     Site            220
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Region          390..482
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            406
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92769; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            409
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            421
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11602581,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13547.1)"
     Site            423
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:11602581,
                     ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     Site            432
                     /site_type="methylation"
                     /note="N6-methylated lysine, by EHMT2.
                     /evidence=ECO:0000269|PubMed:18438403; propagated from
                     UniProtKB/Swiss-Prot (Q13547.1)"
     CDS             1..482
                     /gene="HDAC1"
                     /gene_synonym="GON-10; HD1; KDAC1; RPD3; RPD3L1"
                     /coded_by="NM_004964.3:88..1536"
                     /db_xref="CCDS:CCDS360.1"
                     /db_xref="GeneID:3065"
                     /db_xref="HGNC:HGNC:4852"
                     /db_xref="MIM:601241"
ORIGIN      
        1 maqtqgtrrk vcyyydgdvg nyyygqghpm kphrirmthn lllnyglyrk meiyrphkan
       61 aeemtkyhsd dyikflrsir pdnmseyskq mqrfnvgedc pvfdglfefc qlstggsvas
      121 avklnkqqtd iavnwagglh hakkseasgf cyvndivlai lellkyhqrv lyididihhg
      181 dgveeafytt drvmtvsfhk ygeyfpgtgd lrdigagkgk yyavnyplrd giddesyeai
      241 fkpvmskvme mfqpsavvlq cgsdslsgdr lgcfnltikg hakcvefvks fnlpmlmlgg
      301 ggytirnvar cwtyetaval dteipnelpy ndyfeyfgpd fklhispsnm tnqntneyle
      361 kikqrlfenl rmlphapgvq mqaipedaip eesgdededd pdkrisicss dkriaceeef
      421 sdseeegegg rknssnfkka krvktedeke kdpeekkevt eeektkeekp eakgvkeevk
      481 la
//
LOCUS       NP_079331                755 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 33 isoform 1 [Homo sapiens].
ACCESSION   NP_079331
VERSION     NP_079331.3
DBSOURCE    REFSEQ: accession NM_025055.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 755)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 755)
  AUTHORS   Daakour,S., Hajingabo,L.J., Kerselidou,D., Devresse,A.,
            Kettmann,R., Simonis,N., Dequiedt,F. and Twizere,J.C.
  TITLE     Systematic interactome mapping of acute lymphoblastic leukemia
            cancer gene products reveals EXT-1 tumor suppressor as a Notch1 and
            FBWX7 common interactor
  JOURNAL   BMC Cancer 16, 335 (2016)
   PUBMED   27229929
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 755)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 755)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   5  (residues 1 to 755)
  AUTHORS   Kaczmarek,K., Niedzialkowska,E., Studencka,M., Schulz,Y. and
            Grzmil,P.
  TITLE     Ccdc33, a predominantly testis-expressed gene, encodes a putative
            peroxisomal protein
  JOURNAL   Cytogenet Genome Res 126 (3), 243-252 (2009)
   PUBMED   20068295
  REMARK    GeneRIF: Data show that CCDC33-dsRED fusion protein co-localized
            with a known peroxisomal protein, namely PXT1, and showed punctuate
            intracellular distribution.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DB049940.1, AC023300.19, AK057417.1, BC031684.1 and AI223423.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 1, 2006 this sequence version replaced NP_079331.2.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK057417.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2148093, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398814.8/ ENSP00000381795.3
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..755
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q24.1"
     Protein         1..755
                     /product="coiled-coil domain-containing protein 33 isoform
                     1"
                     /note="cancer/testis antigen 61; coiled-coil
                     domain-containing protein 33; hypothetical protein
                     HP11097"
                     /calculated_mol_wt=84821
     Region          37..132
                     /region_name="C2"
                     /note="C2 domain; cd00030"
                     /db_xref="CDD:175973"
     Region          <436..>698
                     /region_name="Smc"
                     /note="Chromosome segregation ATPase Smc [Cell cycle
                     control, cell division, chromosome partitioning]; COG1196"
                     /db_xref="CDD:440809"
     CDS             1..755
                     /gene="CCDC33"
                     /gene_synonym="CC2D3; CT61; HP11097"
                     /coded_by="NM_025055.5:395..2662"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS42058.1"
                     /db_xref="GeneID:80125"
                     /db_xref="HGNC:HGNC:26552"
                     /db_xref="MIM:618525"
ORIGIN      
        1 mglknkknte dpeepliasq stepeighls pskketimvt lhgatnlpac kdgsepwpyv
       61 vvkstseekn nqsskavtsv tseptrapiw gdtvnveiqa edagqedvil kvvdnrkkqe
      121 llsykipiky lrvfhpyhfe lvkptesgka deataktqly atvvrkssfi pryigcnhma
      181 leiflrgvne plannpnpiv viarvvpnyk efkvsqanrd lasvglpitp lsfpipsmmn
      241 fdvprvsqng cpqlskpggp peqplwnqsf lfqgrdgats fsedtalvle yysstsmkgs
      301 qpwtlnqplg isvlplksrl yqkmltgkgl dglhverlpi mdtslktind eaptvalsfq
      361 llsserpenf ltpnnskalp tldpkildkk lrtiqeswsk dtvsstmdls tstpreaeee
      421 plvpemshdt emnnyrramq kmaedilslr rqasilegen rilrsrlaqq eeeegqgkas
      481 eaqntvsmkq klllseldmk klrdrvqhlq nelirkndre kellllyqaq qpqaallkqy
      541 qgklqkmkal eetvrhqekv iekmervled rlqdrskppp lnrqqgkpyt gfpmlsasgl
      601 plgsmgenlp velysvllae naklrteldk nrhqqapiil qqqalpdlls gtsdkfnlla
      661 klehaqsril slesqledsa rrwgrekqdl atrlqeqekg frhpsnsiii eqpsalthsm
      721 dlkqpselep llpssdskln kplspqketa nsqqt
//
LOCUS       NP_001307931             727 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor IF-2, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001307931 XP_011531172
VERSION     NP_001307931.1
DBSOURCE    REFSEQ: accession NM_001321002.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Remes,C., Khawaja,A., Pearce,S.F., Dinan,A.M., Gopalakrishna,S.,
            Cipullo,M., Kyriakidis,V., Zhang,J., Dopico,X.C., Yukhnovets,O.,
            Atanassov,I., Firth,A.E., Cooperman,B. and Rorbach,J.
  TITLE     Translation initiation of leaderless and polycistronic transcripts
            in mammalian mitochondria
  JOURNAL   Nucleic Acids Res 51 (2), 891-907 (2023)
   PUBMED   36629253
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Xu,D., Wang,Y., Wu,J., Zhang,Z., Chen,J., Xie,M., Tang,R.,
            Cheng,C., Chen,L., Lin,S., Luo,X. and Zheng,J.
  TITLE     MTIF2 impairs 5 fluorouracil-mediated immunogenic cell death in
            hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance
  JOURNAL   Pharmacol Res 163, 105265 (2021)
   PUBMED   33129983
  REMARK    GeneRIF: MTIF2 impairs 5 fluorouracil-mediated immunogenic cell
            death in hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance.
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Gelernter,J., Kranzler,H.R., Sherva,R., Almasy,L., Koesterer,R.,
            Smith,A.H., Anton,R., Preuss,U.W., Ridinger,M., Rujescu,D.,
            Wodarz,N., Zill,P., Zhao,H. and Farrer,L.A.
  TITLE     Genome-wide association study of alcohol dependence:significant
            findings in African- and European-Americans including novel risk
            loci
  JOURNAL   Mol Psychiatry 19 (1), 41-49 (2014)
   PUBMED   24166409
  REMARK    GeneRIF: This study identified a novel GWS association (1.17 x
            10(-10)) mapped to chromosome 2 at rs1437396, between MTIF2 and
            CCDC88A, across all of the EA and AA cohorts.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Overman,R.G. Jr., Enderle,P.J., Farrow,J.M. 3rd, Wiley,J.E. and
            Farwell,M.A.
  TITLE     The human mitochondrial translation initiation factor 2 gene
            (MTIF2): transcriptional analysis and identification of a
            pseudogene
  JOURNAL   Biochim Biophys Acta 1628 (3), 195-205 (2003)
   PUBMED   12932832
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Koc,E.C. and Spremulli,L.L.
  TITLE     Identification of mammalian mitochondrial translational initiation
            factor 3 and examination of its role in initiation complex
            formation with natural mRNAs
  JOURNAL   J Biol Chem 277 (38), 35541-35549 (2002)
   PUBMED   12095986
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Bonner,D.S., Wiley,J.E. and Farwell,M.A.
  TITLE     Assignment1 of the mitochondrial translational initiation factor 2
            gene (MTIF2) to human chromosome 2 bands p16-->p14 by in situ
            hybridization and with somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 80-81 (1998)
   PUBMED   9925935
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Ma,L. and Spremulli,L.L.
  TITLE     Cloning and sequence analysis of the human mitochondrial
            translational initiation factor 2 cDNA
  JOURNAL   J Biol Chem 270 (4), 1859-1865 (1995)
   PUBMED   7829522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961193.1, BP282053.1,
            AC012358.9, AF494407.1 and BU681583.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011531172.1.
            
            Summary: During the initiation of protein biosynthesis, initiation
            factor-2 (IF-2) promotes the binding of the initiator tRNA to the
            small subunit of the ribosome in a GTP-dependent manner.
            Prokaryotic IF-2 is a single polypeptide, while eukaryotic
            cytoplasmic IF-2 (eIF-2) is a trimeric protein. Bovine liver
            mitochondria contain IF-2(mt), an 85-kD monomeric protein that is
            equivalent to prokaryotic IF-2. The predicted 727-amino acid human
            protein contains a 29-amino acid presequence. Human IF-2(mt) shares
            32 to 38% amino acid sequence identity with yeast IF-2(mt) and
            several prokaryotic IF-2s, with the greatest degree of conservation
            in the G domains of the proteins. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.32778.1,
                                           SRR7346977.1270921.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..727
                     /product="translation initiation factor IF-2,
                     mitochondrial isoform a precursor"
                     /note="IF-2mt; translation initiation factor IF-2,
                     mitochondrial"
                     /calculated_mol_wt=77711
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=3624
     mat_peptide     30..727
                     /product="Translation initiation factor IF-2,
                     mitochondrial. /id=PRO_0000014480"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=77711
     Region          178..720
                     /region_name="InfB"
                     /note="Translation initiation factor IF-2, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0532"
                     /db_xref="CDD:440298"
     Region          187..194
                     /region_name="G1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          212..216
                     /region_name="G2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          234..237
                     /region_name="G3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          288..291
                     /region_name="G4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          324..326
                     /region_name="G5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91YJ5; propagated from
                     UniProtKB/Swiss-Prot (P46199.2)"
     CDS             1..727
                     /gene="MTIF2"
                     /coded_by="NM_001321002.1:245..2428"
                     /note="isoform a precursor is encoded by transcript
                     variant 4"
                     /db_xref="CCDS:CCDS1853.1"
                     /db_xref="GeneID:4528"
                     /db_xref="HGNC:HGNC:7441"
                     /db_xref="MIM:603766"
ORIGIN      
        1 mnqkllklen llrfhtiyrq lhslcqrral rqwrhgfssa ypvwtaqlca wpwptdvltg
       61 aalsqyrllv tkkeegpwks qlsstkskkv vevwigmtie elarameknt dyvyeallnt
      121 dididslead shldevwike vitkagmklk wsklkqdkvr knkdavrrpq adpalltprs
      181 pvvtimghvd hgkttlldkf rktqvaavet ggitqhigaf lvslpsgeki tfldtpghaa
      241 fsamrargaq vtdivvlvva addgvmkqtv esiqhakdaq vpiilavnkc dkaeadpekv
      301 kkellaydvv cedyggdvqa vpvsaltgdn lmalaeatva laemlelkad pngpvegtvi
      361 esftdkgrgl vttaiiqrgt lrkgsvlvag kcwakvrlmf dengktidea ypsmpvgitg
      421 wrdlpsagee ilevesepra revvdwrkye qeqekgqedl kiieekrkeh keahqkarek
      481 yghllwkkrs ilrflerkeq iplkpkekre rdsnvlsvii kgdvdgsvea ilniidtyda
      541 shecelelvh fgvgdvsand vnlaetfdgv iygfnvnagn viqqsaakkg vkiklhkiiy
      601 rlvedlqeel ssrlpcavee hpvgeasila tfsvtegkkk vpvagcrvqk gqlekqkkfk
      661 ltrnghviwk gsltslkhhk ddisivktgm dcglsldedn mefqvgdriv cyeekqiqak
      721 tswdpgf
//
LOCUS       NP_955474                257 aa            linear   PRI 20-NOV-2025
DEFINITION  coatomer subunit epsilon isoform b [Homo sapiens].
ACCESSION   NP_955474
VERSION     NP_955474.1
DBSOURCE    REFSEQ: accession NM_199442.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 257)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   2  (residues 1 to 257)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 257)
  AUTHORS   Li,W., Liang,J., Outeda,P., Turner,S., Wakimoto,B.T. and Watnick,T.
  TITLE     A genetic screen in Drosophila reveals an unexpected role for the
            KIP1 ubiquitination-promoting complex in male fertility
  JOURNAL   PLoS Genet 16 (12), e1009217 (2020)
   PUBMED   33378371
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 257)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 257)
  AUTHORS   Davila,S., Froeling,F.E., Tan,A., Bonnard,C., Boland,G.J.,
            Snippe,H., Hibberd,M.L. and Seielstad,M.
  TITLE     New genetic associations detected in a host response study to
            hepatitis B vaccine
  JOURNAL   Genes Immun 11 (3), 232-238 (2010)
   PUBMED   20237496
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   6  (residues 1 to 257)
  AUTHORS   Shima,D.T., Scales,S.J., Kreis,T.E. and Pepperkok,R.
  TITLE     Segregation of COPI-rich and anterograde-cargo-rich domains in
            endoplasmic-reticulum-to-Golgi transport complexes
  JOURNAL   Curr Biol 9 (15), 821-824 (1999)
   PUBMED   10469566
REFERENCE   7  (residues 1 to 257)
  AUTHORS   Faulstich,D., Auerbach,S., Orci,L., Ravazzola,M., Wegchingel,S.,
            Lottspeich,F., Stenbeck,G., Harter,C., Wieland,F.T. and
            Tschochner,H.
  TITLE     Architecture of coatomer: molecular characterization of delta-COP
            and protein interactions within the complex
  JOURNAL   J Cell Biol 135 (1), 53-61 (1996)
   PUBMED   8858162
REFERENCE   8  (residues 1 to 257)
  AUTHORS   Schekman,R. and Orci,L.
  TITLE     Coat proteins and vesicle budding
  JOURNAL   Science 271 (5255), 1526-1533 (1996)
   PUBMED   8599108
  REMARK    Review article
REFERENCE   9  (residues 1 to 257)
  AUTHORS   Cukierman,E., Huber,I., Rotman,M. and Cassel,D.
  TITLE     The ARF1 GTPase-activating protein: zinc finger motif and Golgi
            complex localization
  JOURNAL   Science 270 (5244), 1999-2002 (1995)
   PUBMED   8533093
REFERENCE   10 (residues 1 to 257)
  AUTHORS   Orcl,L., Palmer,D.J., Amherdt,M. and Rothman,J.E.
  TITLE     Coated vesicle assembly in the Golgi requires only coatomer and ARF
            proteins from the cytosol
  JOURNAL   Nature 364 (6439), 732-734 (1993)
   PUBMED   8355790
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BI520280.1 and AI680336.1.
            
            Summary: The product of this gene is an epsilon subunit of coatomer
            protein complex. Coatomer is a cytosolic protein complex that binds
            to dilysine motifs and reversibly associates with Golgi
            non-clathrin-coated vesicles. It is required for budding from Golgi
            membranes, and is essential for the retrograde Golgi-to-ER
            transport of dilysine-tagged proteins. Coatomer complex consists of
            at least the alpha, beta, beta', gamma, delta, epsilon and zeta
            subunits. Alternatively spliced transcript variants encoding
            different isoforms have been identified. [provided by RefSeq, Jul
            2008].
            
            Transcript Variant: This variant (2) lacks an in-frame segment of
            the coding region, compared to variant 1. It encodes a shorter
            isoform (b), that is missing an internal segment compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR7346977.314741.1,
                                           SRR7346977.352024.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..257
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.11"
     Protein         1..257
                     /product="coatomer subunit epsilon isoform b"
                     /note="coatomer epsilon subunit; epsilon coat protein;
                     coatomer subunit epsilon; coatomer protein complex subunit
                     epsilon; COPI coat complex subunit epsilon"
                     /calculated_mol_wt=28666
     Region          17..254
                     /region_name="Coatomer_E"
                     /note="Coatomer epsilon subunit; pfam04733"
                     /db_xref="CDD:398419"
     Region          164..194
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     CDS             1..257
                     /gene="COPE"
                     /gene_synonym="epsilon-COP"
                     /coded_by="NM_199442.2:40..813"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12388.1"
                     /db_xref="GeneID:11316"
                     /db_xref="HGNC:HGNC:2234"
                     /db_xref="MIM:606942"
ORIGIN      
        1 mappapgpas ggsgevdelf dvknafyigs yqqcineaqr vklssperdv erdvflyray
       61 laqrkfgvvl deikpssape lqavrmfady lahesrstam tvqillkldr ldlarkelkr
      121 mqdldedatl tqlatawvsl atggeklqda yyifqemadk csptllllng qaachmaqgr
      181 weaaegllqe aldkdsgype tlvnlivlsq hlgkppevtn rylsqlkdah rshpfikeyq
      241 akendfdrlv lqyapsa
//
LOCUS       NP_001354473             577 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 37 [Homo sapiens].
ACCESSION   NP_001354473 XP_005270252
VERSION     NP_001354473.1
DBSOURCE    REFSEQ: accession NM_001367544.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 577)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 577)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 577)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 577)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 577)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 577)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 577)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 577)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 577)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 577)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            On Dec 5, 2018 this sequence version replaced XP_005270252.1.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.492485.1,
                                           SRR3476690.634999.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..577
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..577
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 37"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=63870
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          445..572
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..577
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367544.1:95..1828"
                     /note="isoform 37 is encoded by transcript variant 37"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mattatctrf tddyqlfeel gkgafsvvrr cvkktstqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashcihqi
      121 lesvnhihqh divhrdlkpe nlllaskckg aavkladfgl aievqgeqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdiwac gvilyillvg yppfwdedqh klyqqikaga ydfpspewdt
      241 vtpeaknlin qmltinpakr itadqalkhp wvcqrstvas mmhrqetvec lrkfnarrkl
      301 kgailttmlv srnfsvgrqs sapaspaasa aglagqaaks llnkksdggv kpqsnnknsl
      361 vspaqepapl qtamepqttv vhnatdgikg stescnttte dedlkaaplr tgngssvpeg
      421 rssrdrtaps agmqpqpslc ssamrkqeii kiteqlieai nngdfeaytk icdpgltsfe
      481 pealgnlveg mdfhkfyfen llsknskpih ttilnphvhv igedaaciay irltqyidgq
      541 grprtsqsee trvwhrrdgk wlnvhyhcsg apaaplq
//
LOCUS       NP_777561                166 aa            linear   PRI 20-NOV-2025
DEFINITION  protein FAM9C [Homo sapiens].
ACCESSION   NP_777561 XP_001129351 XP_005274518
VERSION     NP_777561.1
DBSOURCE    REFSEQ: accession NM_174901.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 166)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 166)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 166)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 166)
  AUTHORS   Zhou,J.D., Shen,F., Ji,J.S., Zheng,K., Huang,M. and Wu,J.C.
  TITLE     FAM9C plays an anti-apoptotic role through activation of the
            PI3K/Akt pathway in human hepatocellular carcinoma
  JOURNAL   Oncol Rep 30 (3), 1275-1284 (2013)
   PUBMED   23836295
  REMARK    GeneRIF: FAM9C overexpression increased the phosphorylation levels
            of Akt and anti-apoptotic ability in hepatocellular carcinoma.
REFERENCE   5  (residues 1 to 166)
  AUTHORS   Martinez-Garay,I., Jablonka,S., Sutajova,M., Steuernagel,P., Gal,A.
            and Kutsche,K.
  TITLE     A new gene family (FAM9) of low-copy repeats in Xp22.3 expressed
            exclusively in testis: implications for recombinations in this
            region
  JOURNAL   Genomics 80 (3), 259-267 (2002)
   PUBMED   12213195
  REMARK    GeneRIF: Expressed exclusively in testis; protein is located in the
            nucleus.
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF494345.1 and AC139705.4.
            This sequence is a reference standard in the RefSeqGene project.
            
            On or before Aug 31, 2013 this sequence version replaced
            XP_005274518.1, XP_001129351.1.
            
            Summary: This gene is a member of a gene family which arose through
            duplication on the X chromosome. The encoded protein may be
            localized to the nucleus as the protein contains several nuclear
            localization signals, and has similarity to a synaptonemal complex
            protein. [provided by RefSeq, Aug 2011].
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF494345.1, SRR11853559.33520.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1968968 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380625.8/ ENSP00000369999.3
            RefSeq Select criteria :: based on expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..166
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.2"
     Protein         1..166
                     /product="protein FAM9C"
                     /note="testis expressed 39C"
                     /calculated_mol_wt=19079
     Region          17..63
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZT9.1)"
     Region          78..>158
                     /region_name="Cor1"
                     /note="Cor1/Xlr/Xmr conserved region; pfam04803"
                     /db_xref="CDD:461436"
     Region          129..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8IZT9.1)"
     CDS             1..166
                     /gene="FAM9C"
                     /gene_synonym="TEX39C"
                     /coded_by="NM_174901.6:150..650"
                     /db_xref="CCDS:CCDS35203.1"
                     /db_xref="GeneID:171484"
                     /db_xref="HGNC:HGNC:18405"
                     /db_xref="MIM:300479"
ORIGIN      
        1 maakdqlevq vmaaqemela gkdpvshehe erkpvtetke gdvtdehger gsfaetdeht
       61 gvdtkeledi aadikehlaa krkriekiak acseiknrik nvlrttqlkr qkrdyrislk
      121 lpnvleefit deqkdeegdg ekeeqikifq eqqkrwqqdg kgterd
//
LOCUS       NP_001078834             158 aa            linear   PRI 20-NOV-2025
DEFINITION  mitotic-spindle organizing protein 2A [Homo sapiens].
ACCESSION   NP_001078834
VERSION     NP_001078834.1
DBSOURCE    REFSEQ: accession NM_001085365.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 158)
  AUTHORS   Serna,M., Zimmermann,F., Vineethakumari,C., Gonzalez-Rodriguez,N.,
            Llorca,O. and Luders,J.
  TITLE     CDK5RAP2 activates microtubule nucleator gammaTuRC by facilitating
            template formation and actin release
  JOURNAL   Dev Cell 59 (23), 3175-3188 (2024)
   PUBMED   39321809
REFERENCE   2  (residues 1 to 158)
  AUTHORS   Wang,H., Jiang,X., Cheng,Y., Ren,H., Hu,Y., Zhang,Y., Su,H.,
            Zou,Z., Wang,Q., Liu,Z., Zhang,J. and Qiu,X.
  TITLE     MZT2A promotes NSCLC viability and invasion by increasing Akt
            phosphorylation via the MOZART2 domain
  JOURNAL   Cancer Sci 112 (6), 2210-2222 (2021)
   PUBMED   33754417
  REMARK    GeneRIF: MZT2A promotes NSCLC viability and invasion by increasing
            Akt phosphorylation via the MOZART2 domain.
            Erratum:[Cancer Sci. 2025 Nov 18. doi: 10.1111/cas.70271. PMID:
            41254876]
REFERENCE   3  (residues 1 to 158)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 158)
  AUTHORS   Wieczorek,M., Huang,T.L., Urnavicius,L., Hsia,K.C. and Kapoor,T.M.
  TITLE     MZT Proteins Form Multi-Faceted Structural Modules in the
            gamma-Tubulin Ring Complex
  JOURNAL   Cell Rep 31 (13), 107791 (2020)
   PUBMED   32610146
  REMARK    GeneRIF: MZT Proteins Form Multi-Faceted Structural Modules in the
            gamma-Tubulin Ring Complex.
REFERENCE   5  (residues 1 to 158)
  AUTHORS   Jakobsen,L., Vanselow,K., Skogs,M., Toyoda,Y., Lundberg,E.,
            Poser,I., Falkenby,L.G., Bennetzen,M., Westendorf,J., Nigg,E.A.,
            Uhlen,M., Hyman,A.A. and Andersen,J.S.
  TITLE     Novel asymmetrically localizing components of human centrosomes
            identified by complementary proteomics methods
  JOURNAL   EMBO J 30 (8), 1520-1535 (2011)
   PUBMED   21399614
REFERENCE   6  (residues 1 to 158)
  AUTHORS   Teixido-Travesa,N., Villen,J., Lacasa,C., Bertran,M.T.,
            Archinti,M., Gygi,S.P., Caelles,C., Roig,J. and Luders,J.
  TITLE     The gammaTuRC revisited: a comparative analysis of interphase and
            mitotic human gammaTuRC redefines the set of core components and
            identifies the novel subunit GCP8
  JOURNAL   Mol Biol Cell 21 (22), 3963-3972 (2010)
   PUBMED   20861304
  REMARK    GeneRIF: Data show that depletion of GCP8 specifically affects the
            organization of the interphase microtubule network.
REFERENCE   7  (residues 1 to 158)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   8  (residues 1 to 158)
  AUTHORS   Hutchins,J.R., Toyoda,Y., Hegemann,B., Poser,I., Heriche,J.K.,
            Sykora,M.M., Augsburg,M., Hudecz,O., Buschhorn,B.A., Bulkescher,J.,
            Conrad,C., Comartin,D., Schleiffer,A., Sarov,M., Pozniakovsky,A.,
            Slabicki,M.M., Schloissnig,S., Steinmacher,I., Leuschner,M.,
            Ssykor,A., Lawo,S., Pelletier,L., Stark,H., Nasmyth,K.,
            Ellenberg,J., Durbin,R., Buchholz,F., Mechtler,K., Hyman,A.A. and
            Peters,J.M.
  TITLE     Systematic analysis of human protein complexes identifies
            chromosome segregation proteins
  JOURNAL   Science 328 (5978), 593-599 (2010)
   PUBMED   20360068
REFERENCE   9  (residues 1 to 158)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU682101.1 and BM554057.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BM554057.1, SRR1803612.267831.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000309451.7/ ENSP00000311500.6
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..158
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q21.1"
     Protein         1..158
                     /product="mitotic-spindle organizing protein 2A"
                     /note="mitotic-spindle organizing protein associated with
                     a ring of gamma-tubulin 2A; family with sequence
                     similarity 128, member A"
                     /calculated_mol_wt=16089
     Region          9..96
                     /region_name="MOZART2"
                     /note="Mitotic-spindle organizing gamma-tubulin ring
                     associated; pfam12926"
                     /db_xref="CDD:432879"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZ67; propagated from
                     UniProtKB/Swiss-Prot (Q6P582.2)"
     Region          84..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6P582.2)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q6NZ67; propagated from
                     UniProtKB/Swiss-Prot (Q6P582.2)"
     CDS             1..158
                     /gene="MZT2A"
                     /gene_synonym="FAM128A; MOZART2A"
                     /coded_by="NM_001085365.2:22..498"
                     /db_xref="CCDS:CCDS42758.1"
                     /db_xref="GeneID:653784"
                     /db_xref="HGNC:HGNC:33187"
                     /db_xref="MIM:613449"
ORIGIN      
        1 maaqgvgpgp gsaappglea arqklalrrk kvlsteemel yelaqaaggg idpdvfkilv
       61 dllklnvapl avfqmlksmc agqrlasepq dpaavslpts svpetrgrdk gsaalggvla
      121 laersnhegs sqrmprqpsa trlpkgggpg ksptqgst
//
LOCUS       NP_003694                857 aa            linear   PRI 20-NOV-2025
DEFINITION  nucleolar protein 14 isoform 1 [Homo sapiens].
ACCESSION   NP_003694 XP_035572
VERSION     NP_003694.1
DBSOURCE    REFSEQ: accession NM_003703.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 857)
  AUTHORS   Yan,X., Kuang,B.H., Ma,S., Wang,R., Lin,J., Zeng,Y.X., Xie,X. and
            Feng,L.
  TITLE     NOP14-mediated ribosome biogenesis is required for mTORC2
            activation and predicts rapamycin sensitivity
  JOURNAL   J Biol Chem 300 (3), 105681 (2024)
   PUBMED   38272224
  REMARK    GeneRIF: NOP14-mediated ribosome biogenesis is required for mTORC2
            activation and predicts rapamycin sensitivity.
REFERENCE   2  (residues 1 to 857)
  AUTHORS   Lu,C., Liao,W., Huang,Y., Huang,Y. and Luo,Y.
  TITLE     Increased expression of NOP14 is associated with improved prognosis
            due to immune regulation in colorectal cancer
  JOURNAL   BMC Gastroenterol 22 (1), 207 (2022)
   PUBMED   35473611
  REMARK    GeneRIF: Increased expression of NOP14 is associated with improved
            prognosis due to immune regulation in colorectal cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 857)
  AUTHORS   Singh,S., Vanden Broeck,A., Miller,L., Chaker-Margot,M. and
            Klinge,S.
  TITLE     Nucleolar maturation of the human small subunit processome
  JOURNAL   Science 373 (6560), eabj5338 (2021)
   PUBMED   34516797
REFERENCE   4  (residues 1 to 857)
  AUTHORS   Zhu,X., Jia,W., Yan,Y., Huang,Y. and Wang,B.
  TITLE     NOP14 regulates the growth, migration, and invasion of colorectal
            cancer cells by modulating the NRIP1/GSK-3beta/beta-catenin
            signaling pathway
  JOURNAL   Eur J Histochem 65 (3), 3246 (2021)
   PUBMED   34218653
  REMARK    GeneRIF: NOP14 regulates the growth, migration, and invasion of
            colorectal cancer cells by modulating the
            NRIP1/GSK-3beta/beta-catenin signaling pathway.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 857)
  AUTHORS   Ying,Y., Li,J., Xie,H., Yan,H., Jin,K., He,L., Ma,X., Wu,J., Xu,X.,
            Fang,J., Wang,X., Zheng,X., Liu,B. and Xie,L.
  TITLE     CCND1, NOP14 and DNMT3B are involved in miR-502-5p-mediated
            inhibition of cell migration and proliferation in bladder cancer
  JOURNAL   Cell Prolif 53 (2), e12751 (2020)
   PUBMED   31971654
  REMARK    GeneRIF: CCND1, DNMT3B and NOP14 were identified as direct targets
            of miR-502-5p.
REFERENCE   6  (residues 1 to 857)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   7  (residues 1 to 857)
  AUTHORS   Nousiainen,M., Sillje,H.H., Sauer,G., Nigg,E.A. and Korner,R.
  TITLE     Phosphoproteome analysis of the human mitotic spindle
  JOURNAL   Proc Natl Acad Sci U S A 103 (14), 5391-5396 (2006)
   PUBMED   16565220
REFERENCE   8  (residues 1 to 857)
  AUTHORS   Liu,P.C. and Thiele,D.J.
  TITLE     Novel stress-responsive genes EMG1 and NOP14 encode conserved,
            interacting proteins required for 40S ribosome biogenesis
  JOURNAL   Mol Biol Cell 12 (11), 3644-3657 (2001)
   PUBMED   11694595
REFERENCE   9  (residues 1 to 857)
  AUTHORS   Hadano,S., Ishida,Y. and Ikeda,J.E.
  TITLE     The primary structure and genomic organization of five novel
            transcripts located close to the Huntington's disease gene on human
            chromosome 4p16.3
  JOURNAL   DNA Res 5 (3), 177-186 (1998)
   PUBMED   9734812
REFERENCE   10 (residues 1 to 857)
  AUTHORS   Pribill,I., Barnes,G.T., Chen,J., Church,D., Buckler,A.,
            Baxendale,S., Bates,G.P., Lehrach,H., Gusella,M.J., Duyao,M.P.,
            Ambrose,C.M., Gusella,J.F. and MacDonald,M.E.
  TITLE     Exon trapping and sequence-based methods of gene finding in
            transcript mapping of human 4p16.3
  JOURNAL   Somat Cell Mol Genet 23 (6), 413-427 (1997)
   PUBMED   9661704
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK292939.1, AF040965.1 and AK025692.1.
            
            On Nov 22, 2004 this sequence version replaced XP_035572.2.
            
            Summary: This gene encodes a protein that plays a role in pre-18s
            rRNA processing and small ribosomal subunit assembly. The encoded
            protein may be involved in the regulation of pancreatic cancer cell
            proliferation and migration. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, May 2014].
            
            Transcript Variant: This variant (2) differs in the 3' UTR,
            compared to variant 2. Variants 1 and 2 encode the same isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF040965.1, SRR1803615.235344.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..857
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p16.3"
     Protein         1..857
                     /product="nucleolar protein 14 isoform 1"
                     /note="probable nucleolar complex protein 14; NOP14
                     nucleolar protein homolog"
                     /calculated_mol_wt=97538
     Region          1..34
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78316.3)"
     Region          30..846
                     /region_name="Nop14"
                     /note="Nop14-like family; pfam04147"
                     /db_xref="CDD:461196"
     Site            96
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P78316.3)"
     Site            146
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78316.3)"
     Site            148
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P78316.3)"
     Region          162..252
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78316.3)"
     Region          264..422
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P78316.3)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P78316.3)"
     CDS             1..857
                     /gene="NOP14"
                     /gene_synonym="C4orf9; NOL14; RES4-25; RES425; UTP2"
                     /coded_by="NM_003703.3:88..2661"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33945.1"
                     /db_xref="GeneID:8602"
                     /db_xref="HGNC:HGNC:16821"
                     /db_xref="MIM:611526"
ORIGIN      
        1 makakkvgar rkasgapaga rggpakansn pfevkvnrqk fqilgrktrh dvglpgvsra
       61 ralrkrtqtl lkeykerdks nvfrdkrfge ynsnmspeek mmkrfaleqq rhhekksiyn
      121 lnedeelthy gqsladiekh ndivdsdsda edrgtlsael taahfggggg llhkktqqeg
      181 eerekpksrk elieeliaks kqekrerqaq redaleltek ldqdwkeiqt llshktpkse
      241 nrdkkekpkp daydmmvrel gfemkaqpsn rmkteaelak eeqehlrkle aerlrrmlgk
      301 dedenvkkpk hmsaddlndg fvldkddrrl lsykdgkmnv eedvqeeqsk easdpesnee
      361 egdssggedt eesdspdshl dlesnvesee enekpakeqr qtpgkglisg keragkatrd
      421 elpytfaape syeelrslll grsmeeqllv veriqkcnhp slaegnkakl eklfgflley
      481 vgdlatddpp dltvidklvv hlyhlcqmfp esasdaikfv lrdamhemee mietkgraal
      541 pgldvliylk itgllfptsd fwhpvvtpal vclsqlltkc pilslqdvvk glfvcclfle
      601 yvalsqrfip elinfllgil yiatpnkasq gstlvhpfra lgknsellvv saredvatwq
      661 qsslslrwas rlraptstea nhirlsclav glallkrcvl mygslpsfha imgplqallt
      721 dhladcshpq elqelcqstl temesqkqlc rpltcekskp vplklftprl vkvlefgrkq
      781 gsskeeqerk rlihkhkref kgavreirkd nqflarmqls eimerdaerk rkvkqlfnsl
      841 atqegewkal krkkfkk
//
LOCUS       NP_056281               1636 aa            linear   PRI 20-NOV-2025
DEFINITION  tyrosine-protein phosphatase non-receptor type 23 isoform 1 [Homo
            sapiens].
ACCESSION   NP_056281
VERSION     NP_056281.1
DBSOURCE    REFSEQ: accession NM_015466.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1636)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1636)
  AUTHORS   Niu,S., Ma,J., Li,Y., Yue,X., Shi,K., Pan,M., Song,L., Tan,Y.,
            Gu,L., Liu,S. and Chang,J.
  TITLE     PTPN23[Thr] variant reduces susceptibility and tumorigenesis in
            esophageal squamous cell carcinoma through dephosphorylation of
            EGFR
  JOURNAL   Cancer Lett 592, 216936 (2024)
   PUBMED   38704135
  REMARK    GeneRIF: PTPN23[Thr] variant reduces susceptibility and
            tumorigenesis in esophageal squamous cell carcinoma through
            dephosphorylation of EGFR.
REFERENCE   3  (residues 1 to 1636)
  AUTHORS   Singh,S., Yeat,N.Y., Wang,Y.T., Lin,S.Y., Kuo,I.Y., Wu,K.P.,
            Wang,W.J., Wang,W.C., Su,W.C., Wang,Y.C. and Chen,R.H.
  TITLE     PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET degradation
            to define a lung cancer therapeutic target
  JOURNAL   Cell Death Dis 14 (10), 671 (2023)
   PUBMED   37821451
  REMARK    GeneRIF: PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET
            degradation to define a lung cancer therapeutic target.
            Erratum:[Cell Death Dis. 2024 Jul 2;15(7):468. doi:
            10.1038/s41419-024-06747-x. PMID: 38956428]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1636)
  AUTHORS   Pashkova,N., Yu,L., Schnicker,N.J., Tseng,C.C., Gakhar,L.,
            Katzmann,D.J. and Piper,R.C.
  TITLE     Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP
            reveals role for regulation of Vps4 ATPase
  JOURNAL   Mol Biol Cell 32 (22), ar42 (2021)
   PUBMED   34586919
  REMARK    GeneRIF: Interactions of ubiquitin and CHMP5 with the V domain of
            HD-PTP reveals role for regulation of Vps4 ATPase.
REFERENCE   5  (residues 1 to 1636)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 1636)
  AUTHORS   Castiglioni,S., Maier,J.A. and Mariotti,M.
  TITLE     The tyrosine phosphatase HD-PTP: A novel player in endothelial
            migration
  JOURNAL   Biochem Biophys Res Commun 364 (3), 534-539 (2007)
   PUBMED   17959146
  REMARK    GeneRIF: We suggest that HD-PTP contributes to the regulation of
            endothelial motility by modulating the tyrosine phosphorylation of
            FAK.
REFERENCE   7  (residues 1 to 1636)
  AUTHORS   Ichioka,F., Takaya,E., Suzuki,H., Kajigaya,S., Buchman,V.L.,
            Shibata,H. and Maki,M.
  TITLE     HD-PTP and Alix share some membrane-traffic related proteins that
            interact with their Bro1 domains or proline-rich regions
  JOURNAL   Arch Biochem Biophys 457 (2), 142-149 (2007)
   PUBMED   17174262
REFERENCE   8  (residues 1 to 1636)
  AUTHORS   Mariotti,M., Castiglioni,S., Beguinot,L. and Maier,J.A.
  TITLE     The tyrosine phosphatase HD-PTP is regulated by FGF-2 through
            proteasome degradation
  JOURNAL   Front Biosci 11, 2138-2143 (2006)
   PUBMED   16720300
  REMARK    GeneRIF: data suggest that HD-PTP might participate in modulating
            endothelial response to angiogenic factors and play a role in
            regulating the complex events leading to the formation of new
            vessels
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 1636)
  AUTHORS   Mariotti,M., Castiglioni,S. and Maier,J.A.
  TITLE     Expression analysis and modulation by HIV-Tat of the tyrosine
            phosphatase HD-PTP
  JOURNAL   J Cell Biochem 98 (2), 301-308 (2006)
   PUBMED   16408268
  REMARK    GeneRIF: These results suggest that HD-PTP amounts might be
            regulated both at the transcriptional and post-transcriptional
            levels.
REFERENCE   10 (residues 1 to 1636)
  AUTHORS   Toyooka,S., Ouchida,M., Jitsumori,Y., Tsukuda,K., Sakai,A.,
            Nakamura,A., Shimizu,N. and Shimizu,K.
  TITLE     HD-PTP: A novel protein tyrosine phosphatase gene on human
            chromosome 3p21.3
  JOURNAL   Biochem Biophys Res Commun 278 (3), 671-678 (2000)
   PUBMED   11095967
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB040904.2, AF290614.1 and
            BU173747.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the non-receptor type
            protein-tyrosine phosphatase family. The encoded protein may be
            involved in the regulation of small nuclear ribonucleo protein
            assembly and pre-mRNA splicing by modifying the survival motor
            neuron (SMN) complex. The encoded protein additionally plays a role
            in ciliogenesis and is part of endosomal sorting complex required
            for transport (ESCRT) pathways. This gene may serve a tumor
            suppressor function. [provided by RefSeq, Jul 2016].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AB025194.1, AF290614.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265562.5/ ENSP00000265562.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1636
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..1636
                     /product="tyrosine-protein phosphatase non-receptor type
                     23 isoform 1"
                     /EC_number="3.1.3.48"
                     /note="protein tyrosine phosphatase TD14; his
                     domain-containing protein tyrosine phosphatase"
                     /calculated_mol_wt=178843
     Region          2..357
                     /region_name="BRO1_HD-PTP_like"
                     /note="Protein-interacting, N-terminal, Bro1-like domain
                     of mammalian His-Domain type N23 protein tyrosine
                     phosphatase and related domains; cd09239"
                     /db_xref="CDD:185762"
     Site            order(125,128,141,144..145,189,192..193,202,205..206,336,
                     338,340,342)
                     /site_type="other"
                     /note="putative ESCRT-III binding site"
                     /db_xref="CDD:185762"
     Region          250..283
                     /region_name="TPR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          362..700
                     /region_name="V_HD-PTP_like"
                     /note="Protein-interacting V-domain of mammalian
                     His-Domain type N23 protein tyrosine phosphatase and
                     related domains; cd09234"
                     /db_xref="CDD:185747"
     Region          374..407
                     /region_name="TPR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            order(445,504,508,511..512,671,674..675,678,681)
                     /site_type="other"
                     /note="putative YPXnL-motif binding site"
                     /db_xref="CDD:185747"
     Region          701..812
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          <727..1083
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Site            733
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          770..1130
                     /region_name="His"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          888..1151
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            950
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          953..964
                     /region_name="6 X 2 AA approximate tandem repeats of P-Q"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            1122
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            1123
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            1131
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Region          1243..1447
                     /region_name="PTP-N23"
                     /note="PTP-like domain of tyrosine-protein phosphatase
                     non-receptor type 23; cd14539"
                     /db_xref="CDD:350387"
     Region          1513..1636
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H3S7.1)"
     Site            1615
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q9H3S7.1)"
     CDS             1..1636
                     /gene="PTPN23"
                     /gene_synonym="HD-PTP; HDPTP; NEDBASS; PTP-TD14"
                     /coded_by="NM_015466.4:77..4987"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2754.1"
                     /db_xref="GeneID:25930"
                     /db_xref="HGNC:HGNC:14406"
                     /db_xref="MIM:606584"
ORIGIN      
        1 meavprmpmi wldlkeagdf hfqpavkkfv lknygenpea yneelkklel lrqnavrvpr
       61 dfegcsvlrk ylgqlhylqs rvpmgsgqea avpvtwteif sgksvahedi kyeqacilyn
      121 lgalhsmlga mdkrvseegm kvscthfqca agafaylreh fpqaysvdms rqiltlnvnl
      181 mlgqaqecll eksmldnrks flvarisaqv vdyykeacra lenpdtasll griqkdwkkl
      241 vqmkiyyfaa vahlhmgkqa eeqqkfgerv ayfqsaldkl neaiklakgq pdtvqdalrf
      301 tmdviggkyn sakkdndfiy heavpaldtl qpvkgaplvk plpvnptdpa vtgpdifakl
      361 vpmaaheass lyseekakll remmakiedk nevldqfmds mqldpetvdn ldayshippq
      421 lmekcaalsv rpdtvrnlvq smqvlsgvft dveaslkdir dlleedelle qkfqeavgqa
      481 gaisitskae laevrrewak ymevhekasf tnselhramn lhvgnlrlls gpldqvraal
      541 ptpalspedk avlqnlkril akvqemrdqr vsleqqlrel iqkdditasl vttdhsemkk
      601 lfeeqlkkyd qlkvyleqnl aaqdrvlcal teanvqyaav rrvlsdldqk wnstlqtlva
      661 syeayedlmk ksqegrdfya dleskvaall ertqstcqar eaarqqlldr elkkkppprp
      721 tapkpllprr eeseaveagd ppeelrslpp dmvagprlpd tflgsatplh fppspfpsst
      781 gpgphylsgp lppgtysgpt qliqprapgp hampvapgpa lypapaytpe lglvprsspq
      841 hgvvsspyvg vgpappvagl psapppqfsg pelamavrpa tttvdsiqap ipshtaprpn
      901 ptpappppcf pvpppqplpt pytypagakq pipaqhhfss gipagfpapr igpqpqphpq
      961 phpsqafgpq ppqqplplqh phlfppqapg llppqspypy apqpgvlgqp ppplhtqlyp
     1021 gpaqdplpah sgalpfpspg ppqpphppla ygpapstrpm gpqaapltir gpssagqstp
     1081 sphlvpspap spgpgpvppr ppaaepppcl rrgaaaadll ssspesqhgg tqspgggqpl
     1141 lqptkvdaae grrpqalrli erdpyehper lrqlqqelea frgqlgdvga ldtvwrelqd
     1201 aqehdargrs iaiarcyslk nrhqdvmpyd snrvvlrsgk ddyinascve glspycpplv
     1261 atqaplpgta adfwlmvheq kvsvivmlvs eaemekqkva ryfptergqp mvhgalslal
     1321 ssvrstethv ervlslqfrd qslkrslvhl hfptwpelgl pdspsnllrf iqevhahylh
     1381 qrplhtpiiv hcssgvgrtg afallyaavq eveagngipe lpqlvrrmrq qrkhmlqekl
     1441 hlrfcyeavv rhveqvlqrh gvpppckpla sasisqknhl pqdsqdlvlg gdvpissiqa
     1501 tiaklsirpp gglespvasl pgpaeppglp paslpestpi psssppplss plpeapqpke
     1561 eppvpeapss gppssslell asltpeafsl dsslrgkqrm skhnflqahn gqglratrps
     1621 ddplslldpl wtlnkt
//
LOCUS       NP_003831                386 aa            linear   PRI 20-NOV-2025
DEFINITION  tumor necrosis factor receptor superfamily member 10D precursor
            [Homo sapiens].
ACCESSION   NP_003831
VERSION     NP_003831.2
DBSOURCE    REFSEQ: accession NM_003840.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 386)
  AUTHORS   Ghosal,N., Tapadar,P., Biswas,D. and Pal,R.
  TITLE     ELF3 plays an important role in defining TRAIL sensitivity in
            breast cancer by modulating the expression of decoy receptor 2
            (DCR2)
  JOURNAL   Mol Biol Rep 51 (1), 671 (2024)
   PUBMED   38787503
  REMARK    GeneRIF: ELF3 plays an important role in defining TRAIL sensitivity
            in breast cancer by modulating the expression of decoy receptor 2
            (DCR2).
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 386)
  AUTHORS   Shilts,J., Severin,Y., Galaway,F., Muller-Sienerth,N., Chong,Z.S.,
            Pritchard,S., Teichmann,S., Vento-Tormo,R., Snijder,B. and
            Wright,G.J.
  TITLE     A physical wiring diagram for the human immune system
  JOURNAL   Nature 608 (7922), 397-404 (2022)
   PUBMED   35922511
  REMARK    Erratum:[Nature. 2024 Nov;635(8037):E1. doi:
            10.1038/s41586-024-07928-6. PMID: 39433908]
REFERENCE   3  (residues 1 to 386)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 386)
  AUTHORS   Madsen,S.D., Jones,S.H., Tucker,H.A., Giler,M.K., Muller,D.C.,
            Discher,C.T., Russell,K.C., Dobek,G.L., Sammarco,M.C., Bunnell,B.A.
            and O'Connor,K.C.
  TITLE     Survival of aging CD264+ and CD264- populations of human bone
            marrow mesenchymal stem cells is independent of colony-forming
            efficiency
  JOURNAL   Biotechnol Bioeng 117 (1), 223-237 (2020)
   PUBMED   31612990
  REMARK    GeneRIF: Survival of aging CD264(+) and CD264(-) populations of
            human bone marrow mesenchymal stem cells is independent of
            colony-forming efficiency.
REFERENCE   5  (residues 1 to 386)
  AUTHORS   Heilmann,T., Vondung,F., Borzikowsky,C., Szymczak,S., Kruger,S.,
            Alkatout,I., Wenners,A., Bauer,M., Klapper,W., Rocken,C., Maass,N.,
            von Karstedt,S., Schem,C. and Trauzold,A.
  TITLE     Heterogeneous intracellular TRAIL-receptor distribution predicts
            poor outcome in breast cancer patients
  JOURNAL   J Mol Med (Berl) 97 (8), 1155-1167 (2019)
   PUBMED   31183506
  REMARK    GeneRIF: data suggest that the determination of intracellular
            co-expression patterns of TRAIL-R1, TRAIL-R2, and TRAIL-R4 provides
            an innovative and robust method for risk stratification in breast
            cancer patients beyond conventional prognostic markers.
REFERENCE   6  (residues 1 to 386)
  AUTHORS   Zhang,X.D., Franco,A.V., Nguyen,T., Gray,C.P. and Hersey,P.
  TITLE     Differential localization and regulation of death and decoy
            receptors for TNF-related apoptosis-inducing ligand (TRAIL) in
            human melanoma cells
  JOURNAL   J Immunol 164 (8), 3961-3970 (2000)
   PUBMED   10754286
REFERENCE   7  (residues 1 to 386)
  AUTHORS   Phillips,T.A., Ni,J., Pan,G., Ruben,S.M., Wei,Y.F., Pace,J.L. and
            Hunt,J.S.
  TITLE     TRAIL (Apo-2L) and TRAIL receptors in human placentas: implications
            for immune privilege
  JOURNAL   J Immunol 162 (10), 6053-6059 (1999)
   PUBMED   10229846
REFERENCE   8  (residues 1 to 386)
  AUTHORS   Pan,G., Ni,J., Yu,G., Wei,Y.F. and Dixit,V.M.
  TITLE     TRUNDD, a new member of the TRAIL receptor family that antagonizes
            TRAIL signalling
  JOURNAL   FEBS Lett 424 (1-2), 41-45 (1998)
   PUBMED   9537512
REFERENCE   9  (residues 1 to 386)
  AUTHORS   Marsters,S.A., Sheridan,J.P., Pitti,R.M., Huang,A., Skubatch,M.,
            Baldwin,D., Yuan,J., Gurney,A., Goddard,A.D., Godowski,P. and
            Ashkenazi,A.
  TITLE     A novel receptor for Apo2L/TRAIL contains a truncated death domain
  JOURNAL   Curr Biol 7 (12), 1003-1006 (1997)
   PUBMED   9382840
REFERENCE   10 (residues 1 to 386)
  AUTHORS   Degli-Esposti,M.A., Dougall,W.C., Smolak,P.J., Waugh,J.Y.,
            Smith,C.A. and Goodwin,R.G.
  TITLE     The novel receptor TRAIL-R4 induces NF-kappaB and protects against
            TRAIL-mediated apoptosis, yet retains an incomplete death domain
  JOURNAL   Immunity 7 (6), 813-820 (1997)
   PUBMED   9430226
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100861.2, AY358285.1,
            AF021233.1, BU199149.1 and AA743393.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 29, 2002 this sequence version replaced NP_003831.1.
            
            Summary: The protein encoded by this gene is a member of the
            TNF-receptor superfamily. This receptor contains an extracellular
            TRAIL-binding domain, a transmembrane domain, and a truncated
            cytoplamic death domain. This receptor does not induce apoptosis,
            and has been shown to play an inhibitory role in TRAIL-induced cell
            apoptosis. [provided by RefSeq, Jul 2008].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AY358285.1, SRR1660803.35943.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000312584.4/ ENSP00000310263.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..386
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21.3"
     Protein         1..386
                     /product="tumor necrosis factor receptor superfamily
                     member 10D precursor"
                     /note="decoy receptor 2; TNF receptor-related receptor for
                     TRAIL; TRAIL receptor 4; TRAIL receptor with a truncated
                     death domain; tumor necrosis factor receptor superfamily,
                     member 10d, decoy with truncated death domain; tumor
                     necrosis factor receptor superfamily member 10d;
                     TNF-related apoptosis-inducing ligand receptor 4"
                     /calculated_mol_wt=35958
     sig_peptide     1..55
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=5910
     Region          1..25
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     mat_peptide     56..386
                     /product="tumor necrosis factor receptor superfamily
                     member 10D"
                     /calculated_mol_wt=35958
     Region          58..97
                     /region_name="TNFR-Cys 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          62..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          80..180
                     /region_name="TNFRSF10"
                     /note="Tumor necrosis factor receptor superfamily member
                     10 (TNFRSF10), includes TNFRSF10A (DR4), TNFRSF10B (DR5),
                     TNFRSF10C (DcR1) and TNFRSF10D (DcR2); cd10580"
                     /db_xref="CDD:276906"
     Site            order(80..82,89,91,108..109,111..114,116..117,156,177)
                     /site_type="other"
                     /note="Antibody binding [polypeptide binding]"
                     /db_xref="CDD:276906"
     Region          80..96
                     /region_name="CRD1"
                     /note="CRD1 [structural motif]"
                     /db_xref="CDD:276906"
     Region          98..139
                     /region_name="TNFR-Cys 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          99..139
                     /region_name="CRD2"
                     /note="CRD2 [structural motif]"
                     /db_xref="CDD:276906"
     Site            order(114,117,122,153..157)
                     /site_type="other"
                     /note="polypeptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:276906"
     Site            127
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          140..180
                     /region_name="TNFR-Cys 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          141..180
                     /region_name="CRD3"
                     /note="CRD3 [structural motif]"
                     /db_xref="CDD:276906"
     Site            182
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN6.2)"
     Region          <340..369
                     /region_name="DD"
                     /note="Death Domain Superfamily of protein-protein
                     interaction domains; cl14633"
                     /db_xref="CDD:472698"
     CDS             1..386
                     /gene="TNFRSF10D"
                     /gene_synonym="CD264; DCR2; TRAIL-R4; TRAILR4; TRUNDD"
                     /coded_by="NM_003840.5:93..1253"
                     /db_xref="CCDS:CCDS6038.1"
                     /db_xref="GeneID:8793"
                     /db_xref="HGNC:HGNC:11907"
                     /db_xref="MIM:603614"
ORIGIN      
        1 mglwgqsvpt assaragryp gartasgtrp wlldpkilkf vvfivavllp vrvdsatipr
       61 qdevpqqtva pqqqrrslke eecpagshrs eytgacnpct egvdytiasn nlpscllctv
      121 cksgqtnkss ctttrdtvcq cekgsfqdkn spemcrtcrt gcprgmvkvs nctprsdikc
      181 knesaasstg ktpaaeetvt tilgmlaspy hyliiivvlv iilavvvvgf scrkkfisyl
      241 kgicsggggg pervhrvlfr rrscpsrvpg aednarnetl snrylqptqv seqeiqgqel
      301 aeltgvtvel peepqrlleq aeaegcqrrr llvpvndads adistlldas atleeghake
      361 tiqdqlvgse klfyeedeag satscl
//
LOCUS       NP_006836                725 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF2C isoform 1 [Homo sapiens].
ACCESSION   NP_006836
VERSION     NP_006836.2
DBSOURCE    REFSEQ: accession NM_006845.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 725)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 725)
  AUTHORS   Kalkan,B.M., Ozcan,S.C., Cicek,E., Gonen,M. and Acilan,C.
  TITLE     Nek2A prevents centrosome clustering and induces cell death in
            cancer cells via KIF2C interaction
  JOURNAL   Cell Death Dis 15 (3), 222 (2024)
   PUBMED   38493150
  REMARK    GeneRIF: Nek2A prevents centrosome clustering and induces cell
            death in cancer cells via KIF2C interaction.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 725)
  AUTHORS   Deng,H., Gong,X., Ji,G., Li,C. and Cheng,S.
  TITLE     KIF2C promotes clear cell renal cell carcinoma progression via
            activating JAK2/STAT3 signaling pathway
  JOURNAL   Mol Cell Probes 72, 101938 (2023)
   PUBMED   37863123
  REMARK    GeneRIF: KIF2C promotes clear cell renal cell carcinoma progression
            via activating JAK2/STAT3 signaling pathway.
REFERENCE   4  (residues 1 to 725)
  AUTHORS   Li,S., Ma,Y., Wu,C. and Hou,X.
  TITLE     Knockdown of kinesin family member 2C restricts cell proliferation
            and induces cell cycle arrest in gastric cancer
  JOURNAL   Histol Histopathol 38 (8), 907-916 (2023)
   PUBMED   36448588
  REMARK    GeneRIF: Knockdown of kinesin family member 2C restricts cell
            proliferation and induces cell cycle arrest in gastric cancer.
REFERENCE   5  (residues 1 to 725)
  AUTHORS   Cheng,L.J., Zhou,Z.M., Li,J.M., Zhu,H., Zhu,H., Zhou,Y.D.,
            Wang,L.R., Lin,M. and Sha,J.H.
  TITLE     Expression of a novel HsMCAK mRNA splice variant, tsMCAK gene, in
            human testis
  JOURNAL   Life Sci 71 (23), 2741-2757 (2002)
   PUBMED   12383881
  REMARK    GeneRIF: identification as a candidate gene for the testis-specific
            KRPs and its specific expression in the testis was correlated with
            spermatogenesis and may be correlated with male infertility
REFERENCE   6  (residues 1 to 725)
  AUTHORS   Miki,H., Setou,M., Kaneshiro,K. and Hirokawa,N.
  TITLE     All kinesin superfamily protein, KIF, genes in mouse and human
  JOURNAL   Proc Natl Acad Sci U S A 98 (13), 7004-7011 (2001)
   PUBMED   11416179
  REMARK    Review article
REFERENCE   7  (residues 1 to 725)
  AUTHORS   Sugata,N., Li,S., Earnshaw,W.C., Yen,T.J., Yoda,K., Masumoto,H.,
            Munekata,E., Warburton,P.E. and Todokoro,K.
  TITLE     Human CENP-H multimers colocalize with CENP-A and CENP-C at active
            centromere--kinetochore complexes
  JOURNAL   Hum Mol Genet 9 (19), 2919-2926 (2000)
   PUBMED   11092768
REFERENCE   8  (residues 1 to 725)
  AUTHORS   Wordeman,L., Wagenbach,M. and Maney,T.
  TITLE     Mutations in the ATP-binding domain affect the subcellular
            distribution of mitotic centromere-associated kinesin (MCAK)
  JOURNAL   Cell Biol Int 23 (4), 275-286 (1999)
   PUBMED   10600236
REFERENCE   9  (residues 1 to 725)
  AUTHORS   Maney,T., Hunter,A.W., Wagenbach,M. and Wordeman,L.
  TITLE     Mitotic centromere-associated kinesin is important for anaphase
            chromosome segregation
  JOURNAL   J Cell Biol 142 (3), 787-801 (1998)
   PUBMED   9700166
REFERENCE   10 (residues 1 to 725)
  AUTHORS   Kim,I.G., Jun,D.Y., Sohn,U. and Kim,Y.H.
  TITLE     Cloning and expression of human mitotic centromere-associated
            kinesin gene
  JOURNAL   Biochim Biophys Acta 1359 (3), 181-186 (1997)
   PUBMED   9434124
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU130795.1, BC008764.2,
            BC014924.1 and BU615368.1.
            
            On Feb 2, 2008 this sequence version replaced NP_006836.1.
            
            Summary: This gene encodes a kinesin-like protein that functions as
            a microtubule-dependent molecular motor. The encoded protein can
            depolymerize microtubules at the plus end, thereby promoting
            mitotic chromosome segregation. Alternative splicing results in
            multiple transcript variants. [provided by RefSeq, Jul 2014].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: HM005691.1, AB264115.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000372224.9/ ENSP00000361298.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..725
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p34.1"
     Protein         1..725
                     /product="kinesin-like protein KIF2C isoform 1"
                     /note="mitotic centromere-associated kinesin; kinesin-like
                     protein KIF2C; kinesin-like protein 6; testis tissue
                     sperm-binding protein Li 68n"
                     /calculated_mol_wt=81182
     Region          2..254
                     /region_name="Globular. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99661.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Region          89..116
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99661.2)"
     Site            95
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by AURKB.
                     /evidence=ECO:0000269|PubMed:14960279; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Region          98..101
                     /region_name="Microtubule tip localization signal"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99661.2)"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70096; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70096; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            115
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            166
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            175
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            187
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            192
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P70096; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Region          207..238
                     /region_name="Negative regulator of microtubule-binding.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99661.2)"
     Region          258..586
                     /region_name="KISc_KIF2_like"
                     /note="Kinesin motor domain, KIF2-like group; cd01367"
                     /db_xref="CDD:276818"
     Site            order(266,348,351,353..356,492)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276818"
     Region          415..418
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99661.2)"
     Site            519
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            order(540,543,546)
                     /site_type="other"
                     /note="microtubule interaction site [polypeptide binding]"
                     /db_xref="CDD:276818"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     Site            633
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q99661.2)"
     CDS             1..725
                     /gene="KIF2C"
                     /gene_synonym="CT139; KNSL6; MCAK"
                     /coded_by="NM_006845.4:97..2274"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS512.1"
                     /db_xref="GeneID:11004"
                     /db_xref="HGNC:HGNC:6393"
                     /db_xref="MIM:604538"
ORIGIN      
        1 mamdsslqar lfpglaikiq rsnglihsan vrtvnleksc vsvewaegga tkgkeidfdd
       61 vaainpellq llplhpkdnl plqenvtiqk qkrrsvnski papkeslrsr strmstvsel
      121 ritaqendme velpaaansr kqfsvppapt rpscpavaei plrmvseeme eqvhsirgss
      181 sanpvnsvrr ksclvkevek mknkreekka qnsemrmkra qeydssfpnw efarmikefr
      241 atlechpltm tdpieehric vcvrkrplnk qelakkeidv isipskclll vhepklkvdl
      301 tkylenqafc fdfafdetas nevvyrftar plvqtifegg katcfaygqt gsgkthtmgg
      361 dlsgkaqnas kgiyamasrd vfllknqpcy rklglevyvt ffeiyngklf dllnkkaklr
      421 vledgkqqvq vvglqehlvn saddvikmid mgsacrtsgq tfansnssrs hacfqiilra
      481 kgrmhgkfsl vdlagnerga dtssadrqtr megaeinksl lalkeciral gqnkahtpfr
      541 eskltqvlrd sfigensrtc miatispgis sceytlntlr yadrvkelsp hsgpsgeqli
      601 qmeteemeac sngalipgnl skeeeelssq mssfneamtq ireleekame elkeiiqqgp
      661 dwlelsemte qpdydletfv nkaesalaqq akhfsalrdv ikalrlamql eeqasrqiss
      721 kkrpq
//
LOCUS       NP_001353522             834 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 18 [Homo
            sapiens].
ACCESSION   NP_001353522 XP_016855512
VERSION     NP_001353522.1
DBSOURCE    REFSEQ: accession NM_001366593.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 834)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 834)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 834)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 834)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 834)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 834)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 834)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 834)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 834)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 834)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_016855512.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.56473.1,
                                           SRR1803613.25179.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..834
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..834
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 18"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=94044
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <331..660
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..834
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366593.1:2055..4559"
                     /note="isoform 18 is encoded by transcript variant 36"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsgkvtkhk
      361 gtekrespsp apkprkvels esedkggkma aadsvqqrrq yrrqnqqsss dsgsssssed
      421 erpkrshvkn gevgrrrrhs psrsaspspr krqketsprm qmgkrwqspv tksgrrrrsp
      481 sppptrrrrs pspappprrr rtptppprrr tpsppprrrs psprrysppi qrryspsppp
      541 krrtaspppp pkrraspspp pkrrvshspp pkqrsspvtk rrspslsskh rkgsspsrst
      601 rearspqpnk rhspsprpra pqtssspppv rrgassspqr rqspspstrp irrvsrtpep
      661 kkikkaasps pqsvrrvsss rsvsgspepa akkppappsp vqsqspstnw spavpvkkak
      721 sptpspsppr nsdqegggkk kkkkkdkkhk kdkkhkkhkk hkkekavaaa aaaavtpaai
      781 aaatttlaqe epvaapepkk eteseaednl ddlekhlrek alrsmrkaqv spqs
//
LOCUS       NP_001171716            1319 aa            linear   PRI 20-NOV-2025
DEFINITION  partitioning defective 3 homolog isoform 4 [Homo sapiens].
ACCESSION   NP_001171716
VERSION     NP_001171716.1
DBSOURCE    REFSEQ: accession NM_001184787.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1319)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1319)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1319)
  AUTHORS   Zhang,J., Shi,Y., Ding,K., Yu,W., He,J. and Sun,B.
  TITLE     DCAF1 interacts with PARD3 to promote hepatocellular carcinoma
            progression and metastasis by activating the Akt signaling pathway
  JOURNAL   J Exp Clin Cancer Res 43 (1), 136 (2024)
   PUBMED   38711082
  REMARK    GeneRIF: DCAF1 interacts with PARD3 to promote hepatocellular
            carcinoma progression and metastasis by activating the Akt
            signaling pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1319)
  AUTHORS   Wu,J., Tan,H.Y., Chan,Y.T., Lu,Y., Feng,Z., Yuan,H., Zhang,C.,
            Feng,Y. and Wang,N.
  TITLE     PARD3 drives tumorigenesis through activating Sonic Hedgehog
            signalling in tumour-initiating cells in liver cancer
  JOURNAL   J Exp Clin Cancer Res 43 (1), 42 (2024)
   PUBMED   38317186
  REMARK    GeneRIF: PARD3 drives tumorigenesis through activating Sonic
            Hedgehog signalling in tumour-initiating cells in liver cancer.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1319)
  AUTHORS   Gunji,D., Narumi,R., Muraoka,S., Isoyama,J., Ikemoto,N., Ishida,M.,
            Tomonaga,T., Sakai,Y., Obama,K. and Adachi,J.
  TITLE     Integrative analysis of cancer dependency data and comprehensive
            phosphoproteomics data revealed the EPHA2-PARD3 axis as a cancer
            vulnerability in KRAS-mutant colorectal cancer
  JOURNAL   Mol Omics 19 (8), 624-639 (2023)
   PUBMED   37232035
  REMARK    GeneRIF: Integrative analysis of cancer dependency data and
            comprehensive phosphoproteomics data revealed the EPHA2-PARD3 axis
            as a cancer vulnerability in KRAS-mutant colorectal cancer.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1319)
  AUTHORS   Ebnet,K., Suzuki,A., Horikoshi,Y., Hirose,T., Meyer Zu
            Brickwedde,M.K., Ohno,S. and Vestweber,D.
  TITLE     The cell polarity protein ASIP/PAR-3 directly associates with
            junctional adhesion molecule (JAM)
  JOURNAL   EMBO J 20 (14), 3738-3748 (2001)
   PUBMED   11447115
REFERENCE   7  (residues 1 to 1319)
  AUTHORS   Suzuki,A., Yamanaka,T., Hirose,T., Manabe,N., Mizuno,K.,
            Shimizu,M., Akimoto,K., Izumi,Y., Ohnishi,T. and Ohno,S.
  TITLE     Atypical protein kinase C is involved in the evolutionarily
            conserved par protein complex and plays a critical role in
            establishing epithelia-specific junctional structures
  JOURNAL   J Cell Biol 152 (6), 1183-1196 (2001)
   PUBMED   11257119
REFERENCE   8  (residues 1 to 1319)
  AUTHORS   Noda,Y., Takeya,R., Ohno,S., Naito,S., Ito,T. and Sumimoto,H.
  TITLE     Human homologues of the Caenorhabditis elegans cell polarity
            protein PAR6 as an adaptor that links the small GTPases Rac and
            Cdc42 to atypical protein kinase C
  JOURNAL   Genes Cells 6 (2), 107-119 (2001)
   PUBMED   11260256
REFERENCE   9  (residues 1 to 1319)
  AUTHORS   Johansson,A., Driessens,M. and Aspenstrom,P.
  TITLE     The mammalian homologue of the Caenorhabditis elegans polarity
            protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
            Rac1
  JOURNAL   J Cell Sci 113 (Pt 18), 3267-3275 (2000)
   PUBMED   10954424
REFERENCE   10 (residues 1 to 1319)
  AUTHORS   Joberty,G., Petersen,C., Gao,L. and Macara,I.G.
  TITLE     The cell-polarity protein Par6 links Par3 and atypical protein
            kinase C to Cdc42
  JOURNAL   Nat Cell Biol 2 (8), 531-539 (2000)
   PUBMED   10934474
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL450337.24, AL138768.23,
            AL360233.21, AL392123.12, AL390766.16 and AL160409.12.
            
            Summary: This gene encodes a member of the PARD protein family.
            PARD family members interact with other PARD family members and
            other proteins; they affect asymmetrical cell division and direct
            polarized cell growth. Multiple alternatively spliced transcript
            variants have been described for this gene. [provided by RefSeq,
            Oct 2011].
            
            Transcript Variant: This variant (4) lacks an alternate, in-frame
            segment in the coding region, compared to variant 1. The resulting
            protein (isoform 4) is shorter when it is compared to isoform 1.
            This variant has also been called 'variant d'.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF467004.1, SRR9304712.89695.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1319
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.22-p11.21"
     Protein         1..1319
                     /product="partitioning defective 3 homolog isoform 4"
                     /note="partitioning defective 3 homolog; atypical PKC
                     isotype-specific interacting protein; PAR3-alpha; CTCL
                     tumor antigen se2-5; bazooka; par-3 partitioning defective
                     3 homolog; par-3 family cell polarity regulator alpha;
                     protein phosphatase 1, regulatory subunit 118"
                     /calculated_mol_wt=146746
     Region          2..83
                     /region_name="Par3_HAL_N_term"
                     /note="N-terminal of Par3 and HAL proteins; pfam12053"
                     /db_xref="CDD:463446"
     Region          268..364
                     /region_name="PDZ1_Par3-like"
                     /note="PDZ domain 1 of partitioning defective 3 (Par3),
                     and related domains; cd06691"
                     /db_xref="CDD:467178"
     Site            order(283..289,304,307,337,341,344..345)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467178"
     Region          455..547
                     /region_name="PDZ2_Par3-like"
                     /note="PDZ domain 2 of partitioning defective 3 (Par3),
                     and related domains; cd23058"
                     /db_xref="CDD:467271"
     Site            order(470..476,491,494,524,528,531..532)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467271"
     Region          584..683
                     /region_name="PDZ3_Par3-like"
                     /note="PDZ domain 3 of partitioning defective 3 (Par3),
                     and related domains; cd23059"
                     /db_xref="CDD:467272"
     Site            order(600..606,622,625,655,659,662..663)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467272"
     CDS             1..1319
                     /gene="PARD3"
                     /gene_synonym="ASIP; Baz; PAR3; PAR3alpha; PARD-3; PARD3A;
                     PPP1R118; SE2-5L16; SE2-5LT1; SE2-5T2"
                     /coded_by="NM_001184787.2:302..4261"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS53514.1"
                     /db_xref="GeneID:56288"
                     /db_xref="HGNC:HGNC:16051"
                     /db_xref="MIM:606745"
ORIGIN      
        1 mkvtvcfgrt rvvvpcgdgh mkvfsliqqa vtryrkaiak dpnywiqvhr lehgdggild
       61 lddilcdvad dkdrlvavfd eqdphhggdg tsasstgtqs peifgselgt nnvsafqpyq
      121 atseievtps vlranmplhv rrssdpalig lstsvsdsnf sseepsrknp trwsttagfl
      181 kqntagspkt cdrkkdenyr slprdtsnws nqfqrdnars slsashpmvg kwlekqeqde
      241 dgteednsrv epvghadtgl ehipnfsldd mvklvevpnd ggplgihvvp fsarggrtlg
      301 llvkrlekgg kaehenlfre ndcivrindg dlrnrrfeqa qhmfrqamrt piiwfhvvpa
      361 ankeqyeqls qseknnyyss rfspdsqyid nrsvnsaglh tvqraprlnh ppeqidshsr
      421 lphsahpsgk ppsapasapq nvfsttvssg yntkkigkrl niqlkkgteg lgfsitsrdv
      481 tiggsapiyv knilprgaai qdgrlkagdr lievngvdlv gksqeevvsl lrstkmegtv
      541 sllvfrqeda fhprelnaep sqmqipketk aededivltp dgtrefltfe vplndsgsag
      601 lgvsvkgnrs kenhadlgif vksiinggaa skdgrlrvnd qliavngesl lgktnqdame
      661 tlrrsmsteg nkrgmiqliv arriskcnel kspgsppgpe lpietalddr errishslys
      721 giegldesps rnaalsrimg esgkyqlspt vnmpqddtvi ieddrlpvlp phlsdqssss
      781 shddvgfvta dagtwakaai sdsadcslsp dvdpvlafqr egfgrqsmse krtkqfsdas
      841 qldfvktrks ksmdlgiade tklntvddqk agspsrdvgp slglkksssl eslqtavaev
      901 tlngdipfhr prpriirgrg cnesfraaid ksydkpavdd ddegmetlee dteessrsgr
      961 esvstasdqp shslerqmng nqekgdktdr kkdktgkekk kdrdkekdkm kakkgmlkgl
     1021 gdmfriqakt refrerqare rdyaeiqdfh rtfgcddelm yggvssyegs malnarpqsp
     1081 reghmmdaly aqvkkprnsk pspvdsnrst psnhdriqrl rqefqqakqd edvedrrrty
     1141 sfeqpwpnar patqsgrhsv svevqmqrqr qeeressqqa qrqysslprq srknassvsq
     1201 dsweqnyspg egfqsakenp ryssyqgsrn gylgghgfna rvmletqell rqeqrrkeqq
     1261 mkkqppsegp snydsykkvq dpsyappkgp frqdvppsps qvarlnrlqt pekgrpfys
//
LOCUS       NP_001356506             646 aa            linear   PRI 20-NOV-2025
DEFINITION  transcription factor 4 isoform 28 [Homo sapiens].
ACCESSION   NP_001356506 XP_016881434
VERSION     NP_001356506.1
DBSOURCE    REFSEQ: accession NM_001369577.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 646)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 646)
  AUTHORS   Ma,Y., Du,S., Wang,S., Liu,X., Cong,L., Shen,W. and Ye,K.
  TITLE     Circ_0004674 regulation of glycolysis and proliferation mechanism
            of osteosarcoma through miR-140-3p/TCF4 pathway
  JOURNAL   J Biochem Mol Toxicol 38 (9), e23846 (2024)
   PUBMED   39243204
REFERENCE   3  (residues 1 to 646)
  AUTHORS   Honda,T., Nakagawa,T., Yuasa,T., Tokuda,Y., Nakano,M., Tashiro,K.,
            Tourtas,T., Schlotzer-Schrehardt,U., Kruse,F., Yamamoto,K.,
            Koizumi,N. and Okumura,N.
  TITLE     Dysregulation of the TCF4 Isoform in Corneal Endothelial Cells of
            Patients With Fuchs Endothelial Corneal Dystrophy
  JOURNAL   Invest Ophthalmol Vis Sci 65 (6), 27 (2024)
   PUBMED   38884552
  REMARK    GeneRIF: Dysregulation of the TCF4 Isoform in Corneal Endothelial
            Cells of Patients With Fuchs Endothelial Corneal Dystrophy.
REFERENCE   4  (residues 1 to 646)
  AUTHORS   Wang,H., Chen,K., Zong,L., Zhao,X., Wang,J., Fan,S., Shen,B. and
            Zheng,S.
  TITLE     MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood Mesenchymal
            Stem Cells Improve Thin Endometrium Fertility by the Wnt Signaling
            Pathway
  JOURNAL   Cell Transplant 33, 9636897241259552 (2024)
   PUBMED   38847385
  REMARK    GeneRIF: MALAT1/miR-7-5p/TCF4 Axis Regulating Menstrual Blood
            Mesenchymal Stem Cells Improve Thin Endometrium Fertility by the
            Wnt Signaling Pathway.
REFERENCE   5  (residues 1 to 646)
  AUTHORS   Goldfarb,A.N., Lewandowska,K. and Shoham,M.
  TITLE     Determinants of helix-loop-helix dimerization affinity. Random
            mutational analysis of SCL/tal
  JOURNAL   J Biol Chem 271 (5), 2683-2688 (1996)
   PUBMED   8576241
REFERENCE   6  (residues 1 to 646)
  AUTHORS   Sweetser,D.A., Gipson,K.S. and Zar-Kessler,C.
  TITLE     Pitt-Hopkins Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22934316
REFERENCE   7  (residues 1 to 646)
  AUTHORS   Parisi,M.A.
  TITLE     Hirschsprung Disease Overview - RETIRED CHAPTER, FOR HISTORICAL
            REFERENCE ONLY
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301612
REFERENCE   8  (residues 1 to 646)
  AUTHORS   Corneliussen,B., Thornell,A., Hallberg,B. and Grundstrom,T.
  TITLE     Helix-loop-helix transcriptional activators bind to a sequence in
            glucocorticoid response elements of retrovirus enhancers
  JOURNAL   J Virol 65 (11), 6084-6093 (1991)
   PUBMED   1681116
REFERENCE   9  (residues 1 to 646)
  AUTHORS   Henthorn,P., McCarrick-Walmsley,R. and Kadesch,T.
  TITLE     Sequence of the cDNA encoding ITF-2, a positive-acting
            transcription factor
  JOURNAL   Nucleic Acids Res 18 (3), 678 (1990)
   PUBMED   2308860
REFERENCE   10 (residues 1 to 646)
  AUTHORS   Henthorn,P., Kiledjian,M. and Kadesch,T.
  TITLE     Two distinct transcription factors that bind the immunoglobulin
            enhancer microE5/kappa 2 motif
  JOURNAL   Science 247 (4941), 467-470 (1990)
   PUBMED   2105528
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC018994.7, AC090684.6,
            AC013587.10 and AC091103.4.
            
            On Apr 11, 2019 this sequence version replaced XP_016881434.1.
            
            Summary: This gene encodes transcription factor 4, a basic
            helix-loop-helix transcription factor. The encoded protein
            recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a
            motif first identified in immunoglobulin enhancers. This gene is
            broadly expressed, and may play an important role in nervous system
            development. Defects in this gene are a cause of Pitt-Hopkins
            syndrome. In addition, an intronic CTG repeat normally numbering
            10-37 repeat units can expand to >50 repeat units and cause Fuchs
            endothelial corneal dystrophy. Multiple alternatively spliced
            transcript variants that encode different proteins have been
            described. [provided by RefSeq, Jul 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.179324.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..646
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.2"
     Protein         1..646
                     /product="transcription factor 4 isoform 28"
                     /note="immunoglobulin transcription factor 2; SL3-3
                     enhancer factor 2; class B basic helix-loop-helix protein
                     19"
                     /calculated_mol_wt=68896
     Region          537..621
                     /region_name="bHLH_E-protein_TCF4_E2-2"
                     /note="basic helix-loop-helix (bHLH) domain found in
                     transcription factor 4 (TCF-4) and similar proteins;
                     cd18945"
                     /db_xref="CDD:381515"
     Site            order(545,549,551..553,555,560,581..582)
                     /site_type="other"
                     /note="putative DNA binding site [nucleotide binding]"
                     /db_xref="CDD:381515"
     Site            order(558..559,562..563,565..566,569,573,583,586,590,593,
                     596..601)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:381515"
     CDS             1..646
                     /gene="TCF4"
                     /gene_synonym="bHLHb19; CDG2T; E2-2; FCD2; FECD3; ITF-2;
                     ITF2; PTHS; SEF-2; SEF2; SEF2-1; SEF2-1A; SEF2-1B;
                     SEF2-1D; TCF-4"
                     /coded_by="NM_001369577.1:516..2456"
                     /note="isoform 28 is encoded by transcript variant 37"
                     /db_xref="GeneID:6925"
                     /db_xref="HGNC:HGNC:11634"
                     /db_xref="MIM:602272"
ORIGIN      
        1 mfsppvssgk ngptslasgh ftgsnvedrs ssgswgnggh pspsrnygdg tpydhmtsrd
       61 lgshdnlspp fvnsriqskt ergsyssygr esnlqgchqq sllggdmdmg npgtlsptkp
      121 gsqyyqyssn nprrrplhss amevqtkkvr kvppglpssv yapsastady nrdspgypss
      181 kpatstfpss ffmqdghhss dpwssssgmn qpgyagmlgn sshipqsssy cslhpherls
      241 ypshssadin sslppmstfh rsgtnhysts sctppangtd simanrgsga agssqtgdal
      301 gkalasiysp dhtnnsfssn pstpvgspps lsgtavwsrn ggqassspny egplhslqsr
      361 iedrlerldd aihvlrnhav gpstampggh gdmhgiigps hngamgglgs gygtgllsan
      421 rhslmvgthr edgvalrgsh sllpnqvpvp qlpvqsatsp dlnppqdpyr gmppglqgqs
      481 vssgsseiks ddegdenlqd tkssedkkld ddkkdiksit rsrssnndde dltpeqkaer
      541 ekerrmanna rerlrvrdin eafkelgrmv qlhlksdkpq tkllilhqav avilsleqqv
      601 rernlnpkaa clkrreeekv sseppplsla gphpgmgdas nhmgqm
//
LOCUS       NP_055521                963 aa            linear   PRI 20-NOV-2025
DEFINITION  spliceosome associated factor 3, U4/U6 recycling protein isoform 1
            [Homo sapiens].
ACCESSION   NP_055521
VERSION     NP_055521.1
DBSOURCE    REFSEQ: accession NM_014706.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 963)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 963)
  AUTHORS   Wang,Y., Zhou,J., He,W., Fu,R., Shi,L., Dang,N.K., Liu,B., Xu,H.,
            Cheng,X. and Bedford,M.T.
  TITLE     SART3 reads methylarginine-marked glycine- and arginine-rich motifs
  JOURNAL   Cell Rep 43 (7), 114459 (2024)
   PUBMED   38985674
  REMARK    GeneRIF: SART3 reads methylarginine-marked glycine- and
            arginine-rich motifs.
REFERENCE   3  (residues 1 to 963)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   4  (residues 1 to 963)
  AUTHORS   Kim,J., Taketomi,T., Yamada,A., Uematsu,Y., Ueda,K., Chiba,T. and
            Tsuruta,F.
  TITLE     USP4 regulates TUT1 ubiquitination status in concert with SART3
  JOURNAL   Biochem Biophys Res Commun 701, 149557 (2024)
   PUBMED   38310689
  REMARK    GeneRIF: USP4 regulates TUT1 ubiquitination status in concert with
            SART3.
REFERENCE   5  (residues 1 to 963)
  AUTHORS   Ayers,K.L., Eggers,S., Rollo,B.N., Smith,K.R., Davidson,N.M.,
            Siddall,N.A., Zhao,L., Bowles,J., Weiss,K., Zanni,G., Burglen,L.,
            Ben-Shachar,S., Rosensaft,J., Raas-Rothschild,A., Jorgensen,A.,
            Schittenhelm,R.B., Huang,C., Robevska,G., van den Bergen,J.,
            Casagranda,F., Cyza,J., Pachernegg,S., Wright,D.K., Bahlo,M.,
            Oshlack,A., O'Brien,T.J., Kwan,P., Koopman,P., Hime,G.R.,
            Girard,N., Hoffmann,C., Shilon,Y., Zung,A., Bertini,E., Milh,M.,
            Ben Rhouma,B., Belguith,N., Bashamboo,A., McElreavey,K., Banne,E.,
            Weintrob,N., BenZeev,B. and Sinclair,A.H.
  TITLE     Variants in SART3 cause a spliceosomopathy characterised by failure
            of testis development and neuronal defects
  JOURNAL   Nat Commun 14 (1), 3403 (2023)
   PUBMED   37296101
  REMARK    GeneRIF: Variants in SART3 cause a spliceosomopathy characterised
            by failure of testis development and neuronal defects.
            Erratum:[Nat Commun. 2023 Jun 15;14(1):3566. doi:
            10.1038/s41467-023-39372-x. PMID: 37322043]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 963)
  AUTHORS   Tanaka,S., Tsuda,N., Kawano,K., Sakamoto,M., Nishida,T.,
            Hashimoto,T., Shichijo,S., Kamura,T. and Itoh,K.
  TITLE     Expression of tumor-rejection antigens in gynecologic cancers
  JOURNAL   Jpn J Cancer Res 91 (11), 1177-1184 (2000)
   PUBMED   11092984
REFERENCE   7  (residues 1 to 963)
  AUTHORS   Xia,J.H., Yang,Y.F., Deng,H., Tang,B.S., Tang,D.S., He,Y.G.,
            Xia,K., Chen,S.X., Li,Y.X., Pan,Q., Long,Z.G., Dai,H.P., Liao,X.D.,
            Xiao,J.F., Liu,Z.R., Lu,C.Y., Yu,K.P. and Deng,H.X.
  TITLE     Identification of a locus for disseminated superficial actinic
            porokeratosis at chromosome 12q23.2-24.1
  JOURNAL   J Invest Dermatol 114 (6), 1071-1074 (2000)
   PUBMED   10844547
REFERENCE   8  (residues 1 to 963)
  AUTHORS   Harada,K., Yamada,A., Mine,T., Kawagoe,N., Takasu,H. and Itoh,K.
  TITLE     Mouse homologue of the human SART3 gene encoding tumor-rejection
            antigen
  JOURNAL   Jpn J Cancer Res 91 (2), 239-247 (2000)
   PUBMED   10761712
REFERENCE   9  (residues 1 to 963)
  AUTHORS   Nottrott,S., Hartmuth,K., Fabrizio,P., Urlaub,H., Vidovic,I.,
            Ficner,R. and Luhrmann,R.
  TITLE     Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP
            protein with the 5' stem-loop of U4 snRNA
  JOURNAL   EMBO J 18 (21), 6119-6133 (1999)
   PUBMED   10545122
REFERENCE   10 (residues 1 to 963)
  AUTHORS   Yang,D., Nakao,M., Shichijo,S., Sasatomi,T., Takasu,H.,
            Matsumoto,H., Mori,K., Hayashi,A., Yamana,H., Shirouzu,K. and
            Itoh,K.
  TITLE     Identification of a gene coding for a protein possessing shared
            tumor epitopes capable of inducing HLA-A24-restricted cytotoxic T
            lymphocytes in cancer patients
  JOURNAL   Cancer Res 59 (16), 4056-4063 (1999)
   PUBMED   10463607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA391623.1, BC032601.1,
            CN349201.1, BQ231651.1, D63879.1 and AI656011.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The protein encoded by this gene is an RNA-binding nuclear
            protein that is a tumor-rejection antigen. This antigen possesses
            tumor epitopes capable of inducing HLA-A24-restricted and
            tumor-specific cytotoxic T lymphocytes in cancer patients and may
            be useful for specific immunotherapy. This gene product is found to
            be an important cellular factor for HIV-1 gene expression and viral
            replication. It also associates transiently with U6 and U4/U6
            snRNPs during the recycling phase of the spliceosome cycle. This
            encoded protein is thought to be involved in the regulation of mRNA
            splicing. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.224931.1,
                                           SRR1803617.63153.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000546815.6/ ENSP00000449386.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..963
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.3"
     Protein         1..963
                     /product="spliceosome associated factor 3, U4/U6 recycling
                     protein isoform 1"
                     /note="tat-interacting protein of 110 kDa; SART-3;
                     hSART-3; squamous cell carcinoma antigen recognized by T
                     cells 3; p110 nuclear RNA-binding protein; HIV-1
                     Tat-interacting protein of 110kDa; PRP24 homolog"
                     /calculated_mol_wt=109804
     Region          1..36
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          2..351
                     /region_name="Mediates interaction with PRPF3.
                     /evidence=ECO:0000269|PubMed:15314151"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.13,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            10
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          50..90
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          100..>460
                     /region_name="RNA14"
                     /note="Pre-mRNA 3'-end processing (cleavage and
                     polyadenylation) factor [RNA processing and modification];
                     COG5107"
                     /db_xref="CDD:227438"
     Site            215
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          324..356
                     /region_name="HAT 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          359..391
                     /region_name="HAT 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          394..430
                     /region_name="HAT 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          487..520
                     /region_name="Required for interaction with USP4.
                     /evidence=ECO:0000269|PubMed:20595234"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          537..953
                     /region_name="Necessary and sufficient for U6 snRNA
                     binding. /evidence=ECO:0000269|PubMed:15314151"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          590..694
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          600..670
                     /region_name="Required for nuclear localization.
                     /evidence=ECO:0000269|PubMed:11959860"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Region          601..608
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00768"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            650
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            657
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          705..778
                     /region_name="RRM1_SART3"
                     /note="RNA recognition motif 1 (RRM1) found in squamous
                     cell carcinoma antigen recognized by T-cells 3 (SART3) and
                     similar proteins; cd12391"
                     /db_xref="CDD:409825"
     Site            769
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Site            795
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          799..879
                     /region_name="RRM2_SART3"
                     /note="RNA recognition motif 2 (RRM2) found in squamous
                     cell carcinoma antigen recognized by T-cells 3 (SART3) and
                     similar proteins; cd12392"
                     /db_xref="CDD:409826"
     Site            852
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17525332; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          877..933
                     /region_name="LSM_int_assoc"
                     /note="LSM-interacting associated unstructured; pfam16605"
                     /db_xref="CDD:465192"
     Region          878..898
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     Site            906
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q15020.1)"
     Region          920..948
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15020.1)"
     CDS             1..963
                     /gene="SART3"
                     /gene_synonym="DSAP1; P100; p110; p110(nrb); RP11-13G14;
                     TIP110"
                     /coded_by="NM_014706.4:20..2911"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS9117.1"
                     /db_xref="GeneID:9733"
                     /db_xref="HGNC:HGNC:16860"
                     /db_xref="MIM:611684"
ORIGIN      
        1 mataaetsas epeaeskagp kadgeedevk aartrrkvls ravaaatykt mgpawdqqee
       61 gvsesdgdey amassaessp geyeweydee eeknqleier leeqlsinvy dynchvdlir
      121 llrlegeltk vrmarqkmse ifplteelwl ewlhdeisma qdgldrehvy dlfekavkdy
      181 icpniwleyg qysvggigqk gglekvrsvf eralssvglh mtkglalwea yrefesaive
      241 aarlekvhsl frrqlaiply dmeatfaeye ewsedpipes viqnynkalq qlekykpyee
      301 allqaeaprl aeyqayidfe mkigdpariq liferalven clvpdlwiry sqyldrqlkv
      361 kdlvlsvhnr airncpwtva lwsryllame rhgvdhqvis vtfekalnag fiqatdyvei
      421 wqayldylrr rvdfkqdssk eleelraaft raleylkqev eerfnesgdp scvimqnwar
      481 iearlcnnmq karelwdsim trgnakyanm wleyynlera hgdtqhcrka lhravqctsd
      541 ypehvcevll tmertegsle dwdiavqkte trlarvneqr mkaaekeaal vqqeeekaeq
      601 rkraraekka lkkkkkirgp ekrgadedde kewgddeeeq pskrrrvens ipaagetqnv
      661 evaagpagkc aavdveppsk qkekaaslkr dmpkvlhdss kdsitvfvsn lpysmqepdt
      721 klrplfeacg evvqirpifs nrgdfrgycy vefkeeksal qalemdrksv egrpmfvspc
      781 vdksknpdfk vfrystslek hklfisglpf sctkeeleei ckahgtvkdl rlvtnragkp
      841 kglayveyen esqasqavmk mdgmtikeni ikvaisnppq rkvpekpetr kapggpmllp
      901 qtygargkgr tqlsllpral qrpsaaapqa engpaaapav aapaateapk msnadfaklf
      961 lrk
//
LOCUS       NP_055841               1717 aa            linear   PRI 20-NOV-2025
DEFINITION  protein MON2 homolog isoform 1 [Homo sapiens].
ACCESSION   NP_055841 XP_051091
VERSION     NP_055841.2
DBSOURCE    REFSEQ: accession NM_015026.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1717)
  AUTHORS   Li,P., Wu,Q., Yang,X.R. and Sun,T.
  TITLE     MicroRNA-133a-5p inhibiting metastatic capacity of renal clear cell
            carcinoma through regulating MON2
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (11), 5988-5995 (2020)
   PUBMED   32572912
  REMARK    GeneRIF: MicroRNA-133a-5p inhibiting metastatic capacity of renal
            clear cell carcinoma through regulating MON2.
REFERENCE   2  (residues 1 to 1717)
  AUTHORS   Mahajan,D., Tie,H.C., Chen,B. and Lu,L.
  TITLE     Dopey1-Mon2 complex binds to dual-lipids and recruits kinesin-1 for
            membrane trafficking
  JOURNAL   Nat Commun 10 (1), 3218 (2019)
   PUBMED   31324769
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1717)
  AUTHORS   McGough,I.J., de Groot,R.E.A., Jellett,A.P., Betist,M.C.,
            Varandas,K.C., Danson,C.M., Heesom,K.J., Korswagen,H.C. and
            Cullen,P.J.
  TITLE     SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A
            complex to mediate Wntless sorting and Wnt secretion
  JOURNAL   Nat Commun 9 (1), 3737 (2018)
   PUBMED   30213940
  REMARK    GeneRIF: an evolutionary conserved MON2:DOPEY2:ATP9A complex is
            required for SNX3 retromer mediation of Wntless sorting and Wnt
            secretion
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1717)
  AUTHORS   Mahajan,D., Boh,B.K., Zhou,Y., Chen,L., Cornvik,T.C., Hong,W. and
            Lu,L.
  TITLE     Mammalian Mon2/Ysl2 regulates endosome-to-Golgi trafficking but
            possesses no guanine nucleotide exchange activity toward Arl1
            GTPase
  JOURNAL   Sci Rep 3, 3362 (2013)
   PUBMED   24285343
  REMARK    GeneRIF: Mon2 is involved in endosome-to-Golgi trafficking as its
            depletion accelerated the delivery of furin and CI-M6PR to Golgi
            after endocytosis.
            Erratum:[Sci Rep. 2016 Sep 22;6:33619. doi: 10.1038/srep33619.
            PMID: 27654351]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1717)
  AUTHORS   Lauc,G., Huffman,J.E., Pucic,M., Zgaga,L., Adamczyk,B., Muzinic,A.,
            Novokmet,M., Polasek,O., Gornik,O., Kristic,J., Keser,T.,
            Vitart,V., Scheijen,B., Uh,H.W., Molokhia,M., Patrick,A.L.,
            McKeigue,P., Kolcic,I., Lukic,I.K., Swann,O., van Leeuwen,F.N.,
            Ruhaak,L.R., Houwing-Duistermaat,J.J., Slagboom,P.E., Beekman,M.,
            de Craen,A.J., Deelder,A.M., Zeng,Q., Wang,W., Hastie,N.D.,
            Gyllensten,U., Wilson,J.F., Wuhrer,M., Wright,A.F., Rudd,P.M.,
            Hayward,C., Aulchenko,Y., Campbell,H. and Rudan,I.
  TITLE     Loci associated with N-glycosylation of human immunoglobulin G show
            pleiotropy with autoimmune diseases and haematological cancers
  JOURNAL   PLoS Genet 9 (1), e1003225 (2013)
   PUBMED   23382691
REFERENCE   6  (residues 1 to 1717)
  AUTHORS   Tomita,Y., Noda,T., Fujii,K., Watanabe,T., Morikawa,Y. and
            Kawaoka,Y.
  TITLE     The cellular factors Vps18 and Mon2 are required for efficient
            production of infectious HIV-1 particles
  JOURNAL   J Virol 85 (11), 5618-5627 (2011)
   PUBMED   21450827
  REMARK    GeneRIF: Depletion of hVps18 or hMon2 reduced the efficient
            production of infectious HIV-1 virions in human cells.
REFERENCE   7  (residues 1 to 1717)
  AUTHORS   Singer-Kruger,B., Lasic,M., Burger,A.M., Hausser,A., Pipkorn,R. and
            Wang,Y.
  TITLE     Yeast and human Ysl2p/hMon2 interact with Gga adaptors and mediate
            their subcellular distribution
  JOURNAL   EMBO J 27 (10), 1423-1435 (2008)
   PUBMED   18418388
  REMARK    GeneRIF: Ysl2p represents an essential, evolutionarily conserved
            member of a network controlling direct binding and membrane docking
            of Ggas.
REFERENCE   8  (residues 1 to 1717)
  AUTHORS   Gillingham,A.K., Whyte,J.R., Panic,B. and Munro,S.
  TITLE     Mon2, a relative of large Arf exchange factors, recruits Dop1 to
            the Golgi apparatus
  JOURNAL   J Biol Chem 281 (4), 2273-2280 (2006)
   PUBMED   16301316
REFERENCE   9  (residues 1 to 1717)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA125763.1, AB017814.1, AL834320.1 and AC026115.27.
            
            On Sep 14, 2006 this sequence version replaced NP_055841.1.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.120847.1,
                                           SRR1803616.219310.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000393630.8/ ENSP00000377250.4
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1717
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q14.1"
     Protein         1..1717
                     /product="protein MON2 homolog isoform 1"
                     /note="protein MON2 homolog; MON2 homolog, regulator of
                     endosome-to-Golgi trafficking"
                     /calculated_mol_wt=190229
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          9..180
                     /region_name="DCB"
                     /note="dimerization and cyclophilin-binding domain of
                     Mon2; pfam16213"
                     /db_xref="CDD:465072"
     Site            205
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          212..381
                     /region_name="Sec7_N"
                     /note="Guanine nucleotide exchange factor in Golgi
                     transport N-terminal; pfam12783"
                     /db_xref="CDD:463703"
     Region          511..538
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Site            537
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q80TL7; propagated from
                     UniProtKB/Swiss-Prot (Q7Z3U7.3)"
     Region          <872..931
                     /region_name="DUF1981"
                     /note="Domain of unknown function (DUF1981); pfam09324"
                     /db_xref="CDD:462756"
     Region          934..1708
                     /region_name="Mon2_C"
                     /note="C-terminal region of Mon2 protein; pfam16206"
                     /db_xref="CDD:465066"
     CDS             1..1717
                     /gene="MON2"
                     /coded_by="NM_015026.3:383..5536"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31849.1"
                     /db_xref="GeneID:23041"
                     /db_xref="HGNC:HGNC:29177"
                     /db_xref="MIM:616822"
ORIGIN      
        1 msgtsspeav kkllenmqsd lralsleckk kfppvkeaae sgiikvktia arnteilaal
       61 kenssevvqp flmgcgtkep kitqlclaai qrlmshevvs etaagniinm lwqlmensle
      121 elkllqtvlv llttntvvhd ealskaivlc frlhftkdni tnntaaatvr qvvtvvferm
      181 vaederhrdi ieqpvlvqgn snrrsvstlk pcakdaymlf qdlcqlvnad apywlvgmte
      241 mtrtfglell esvlndfpqv flqhqefsfl lkervcplvi klfspnikfr qgsstssspa
      301 pvekpyfpic mrllrvvsvl ikqfysllvt eceiflsllv kfldadkpqw lravavesih
      361 rfcvqpqllr sfcqsydmkq hstkvfrdiv nalgsfiqsl flvpptgnpa tsnqagnnnl
      421 ggsvsapans gmvgigggvt llpafeyrgt wipiltitvq gsakatylem ldkvepptip
      481 egyamsvafh clldlvrgit smiegelgel etecqtttee gssptqsteq qdlqstsdqm
      541 dkeivsravw eemvnacwcg llaalsllld astdeaaten ilkaeltmaa lcgrlglvts
      601 rdafitaick gslpphyalt vlntttaatl snksysvqgq svmmispsse shqqvvavgq
      661 plavqpqgtv mltskniqcm rtllnlahch gavlgtswql vlatlqhlvw ilglkpssgg
      721 alkpgraveg pstvlttavm tdlpvisnil srlfessqyl ddvslhhlin alcslsleam
      781 dmaygnnkep slfavaklle tglvnmhrie ilwrpltghl levcqhpnsr mrewgaealt
      841 slikagltfn hdpplsqnqr lqllllnplk emsninhpdi rlkqlecvlq ilqsqgdslg
      901 pgwplvlgvm gairndqges lirtafqclq lvvtdflptm pctclqivvd vagsfglhnq
      961 elnisltsig llwnisdyff qrgetiekel nkeeaaqqkq aeekgvvlnr pfhpappfdc
     1021 lwlclyaklg elcvdprpav rksagqtlfs tigahgtllq hstwhtviwk vlfhlldrvr
     1081 essttadkek iesgggnili hhsrdtaekq waetwvltla gvarifntrr yllqplgdfs
     1141 rawdvlldhi qsaalsknne vslaalksfq eilqivspvr dsdkpetppv vnvpvpvlig
     1201 pisgmsrpfv rtdsigeklg ryssseppiv tdeledlnlw waawntwyri gsestkppit
     1261 fdkltfipsq pfltaliqif palyqhiktg fnmddlqklg vilhsaisvp issdaspfil
     1321 psyteavlts lqeavltald vlqkaicvgp enmqimypai fdqllafvef sckppqygql
     1381 etkhianaky nqiqlfapae wvalnyvpfa erslevvvdl yqktachkav vnekvlqnii
     1441 ktlrvplslk yscpsestwk lavssllrvl siglpvarqh assgkfdsmw pelantfedf
     1501 lftksippdn lsiqefqrne nidvevvqli sneilpyanf ipkefvgqim tmlnkgsihs
     1561 qsssfteaei dirlreefsk mcfetllqfs fsnkvttpqe gyisrmalsv llkrsqdvlh
     1621 ryiederlsg kcplprqqvt eiifvlkavs tlidslkktq penvdgntwa qvialyptlv
     1681 ecitcsssev csalkealvp fkdfmqppas rvqnges
//
LOCUS       NP_001341024             254 aa            linear   PRI 20-NOV-2025
DEFINITION  PSME3-interacting protein isoform a [Homo sapiens].
ACCESSION   NP_001341024 XP_016879186
VERSION     NP_001341024.1
DBSOURCE    REFSEQ: accession NM_001354095.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 254)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 254)
  AUTHORS   Wu,X., Fang,Y., Gu,Y., Shen,H., Xu,Y., Xu,T., Shi,R., Xu,D.,
            Zhang,J., Leng,K., Shu,Y. and Ma,P.
  TITLE     Fat mass and obesity-associated protein (FTO) mediated m6A
            modification of circFAM192A promoted gastric cancer proliferation
            by suppressing SLC7A5 decay
  JOURNAL   Mol Biomed 5 (1), 11 (2024)
   PUBMED   38556586
  REMARK    GeneRIF: Fat mass and obesity-associated protein (FTO) mediated
            m[6]A modification of circFAM192A promoted gastric cancer
            proliferation by suppressing SLC7A5 decay.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 254)
  AUTHORS   Lipinski,K.A., Senn,K.A., Zeps,N.J. and Hoskins,A.A.
  TITLE     Biochemical and genetic evidence supports Fyv6 as a second-step
            splicing factor in Saccharomyces cerevisiae
  JOURNAL   RNA 29 (11), 1792-1802 (2023)
   PUBMED   37625852
REFERENCE   4  (residues 1 to 254)
  AUTHORS   Zhan,X., Lu,Y., Zhang,X., Yan,C. and Shi,Y.
  TITLE     Mechanism of exon ligation by human spliceosome
  JOURNAL   Mol Cell 82 (15), 2769-2778 (2022)
   PUBMED   35705093
REFERENCE   5  (residues 1 to 254)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 254)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   7  (residues 1 to 254)
  AUTHORS   Gao,X., Wang,Q., Wang,Y., Liu,J., Liu,S., Liu,J., Zhou,X., Zhou,L.,
            Chen,H., Pan,L., Chen,J., Wang,D., Zhang,Q., Shen,S., Xiao,Y.,
            Wu,Z., Cheng,Y., Chen,G., Kubra,S., Qin,J., Huang,L., Zhang,P.,
            Wang,C., Moses,R.E., Lonard,D.M., Malley,B.W.O., Fares,F.,
            Zhang,B., Li,X., Li,L. and Xiao,J.
  TITLE     The REGgamma inhibitor NIP30 increases sensitivity to chemotherapy
            in p53-deficient tumor cells
  JOURNAL   Nat Commun 11 (1), 3904 (2020)
   PUBMED   32764536
  REMARK    GeneRIF: The REGgamma inhibitor NIP30 increases sensitivity to
            chemotherapy in p53-deficient tumor cells.
            Erratum:[Nat Commun. 2020 Sep 23;11(1):4888. doi:
            10.1038/s41467-020-18767-0. PMID: 32968062]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 254)
  AUTHORS   Jonik-Nowak,B., Menneteau,T., Fesquet,D., Baldin,V.,
            Bonne-Andrea,C., Mechali,F., Fabre,B., Boisguerin,P., de Rossi,S.,
            Henriquet,C., Pugniere,M., Ducoux-Petit,M., Burlet-Schiltz,O.,
            Lamond,A.I., Fort,P., Boulon,S., Bousquet,M.P. and Coux,O.
  TITLE     PIP30/FAM192A is a novel regulator of the nuclear proteasome
            activator PA28gamma
  JOURNAL   Proc Natl Acad Sci U S A 115 (28), E6477-E6486 (2018)
   PUBMED   29934401
  REMARK    GeneRIF: data show that PIP30 deeply affects PA28gamma interactions
            with cellular proteins, including the 20S proteasome, demonstrating
            that it is an important regulator of PA28gamma in cells and thus a
            new player in the control of the multiple functions of the
            proteasome within the nucleus.
REFERENCE   9  (residues 1 to 254)
  AUTHORS   Waddell,D.S., Duffin,P.J., Haddock,A.N., Triplett,V.E.,
            Saredy,J.J., Kakareka,K.M. and Eldredge,J.T.
  TITLE     Isolation, expression analysis and characterization of
            NEFA-interacting nuclear protein 30 and RING finger and SPRY domain
            containing 1 in skeletal muscle
  JOURNAL   Gene 576 (1 Pt 2), 319-332 (2016)
   PUBMED   26497270
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC009090.12.
            
            On Sep 13, 2017 this sequence version replaced XP_016879186.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803617.222321.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..254
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13"
     Protein         1..254
                     /product="PSME3-interacting protein isoform a"
                     /note="NEFA-interacting nuclear protein NIP30;
                     PA28G-interacting protein; protein FAM192A; PA28G
                     interacting protein 30kDa; PSME3 interacting protein
                     30kDa; PSME3-interacting protein; family with sequence
                     similarity 192 member A"
                     /calculated_mol_wt=28781
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          15..103
                     /region_name="FAM192A_Fyv6_N"
                     /note="FAM192A/Fyv6, N-terminal domain; pfam10187"
                     /db_xref="CDD:462987"
     Site            17
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          22..52
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            139
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          155..195
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Region          201..254
                     /region_name="Interaction with PSME3.
                     /evidence=ECO:0000269|PubMed:29934401"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            222
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     Site            228
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CK2.
                     /evidence=ECO:0000269|PubMed:29934401; propagated from
                     UniProtKB/Swiss-Prot (Q9GZU8.1)"
     CDS             1..254
                     /gene="PSME3IP1"
                     /gene_synonym="C16orf94; CDA018; CDA10; FAM192A; NIP30;
                     PIP30"
                     /coded_by="NM_001354095.2:378..1142"
                     /note="isoform a is encoded by transcript variant 18"
                     /db_xref="CCDS:CCDS42168.1"
                     /db_xref="GeneID:80011"
                     /db_xref="HGNC:HGNC:29856"
                     /db_xref="MIM:617766"
ORIGIN      
        1 mdggddgnli ikkrfvseae lderrkrrqe ewekvrkped peecpeevyd prslyerlqe
       61 qkdrkqqeye eqfkfknmvr gldedetnfl devsrqqeli ekqrreeelk elkeyrnnlk
      121 kvgisqenkk evekkltvkp ietknkfsqa kllagavkhk ssesgnsvkr lkpdpepddk
      181 nqepsscksl gntslsgpsi hcpsaavcig ilpglgaysg ssdsesssds egtinatgki
      241 vssifrtntf leap
//
LOCUS       NP_001356486             184 aa            linear   PRI 20-NOV-2025
DEFINITION  large ribosomal subunit protein uL22 isoform a [Homo sapiens].
ACCESSION   NP_001356486
VERSION     NP_001356486.1
DBSOURCE    REFSEQ: accession NM_001369557.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 184)
  AUTHORS   Fellmann,F., Saunders,C., O'Donohue,M.F., Reid,D.W., McFadden,K.A.,
            Montel-Lehry,N., Yu,C., Fang,M., Zhang,J., Royer-Bertrand,B.,
            Farinelli,P., Karboul,N., Willer,J.R., Fievet,L., Bhuiyan,Z.A.,
            Kleinhenz,A.L., Jadeau,J., Fulbright,J., Rivolta,C., Renella,R.,
            Katsanis,N., Beckmann,J.S., Nicchitta,C.V., Da Costa,L., Davis,E.E.
            and Gleizes,P.E.
  TITLE     An atypical form of 60S ribosomal subunit in Diamond-Blackfan
            anemia linked to RPL17 variants
  JOURNAL   JCI Insight 9 (17), e172475 (2024)
   PUBMED   39088281
  REMARK    GeneRIF: An atypical form of 60S ribosomal subunit in
            Diamond-Blackfan anemia linked to RPL17 variants.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 184)
  AUTHORS   Li,H., Huo,Y., He,X., Yao,L., Zhang,H., Cui,Y., Xiao,H., Xie,W.,
            Zhang,D., Wang,Y., Zhang,S., Tu,H., Cheng,Y., Guo,Y., Cao,X.,
            Zhu,Y., Jiang,T., Guo,X., Qin,Y. and Sha,J.
  TITLE     A male germ-cell-specific ribosome controls male fertility
  JOURNAL   Nature 612 (7941), 725-731 (2022)
   PUBMED   36517592
REFERENCE   3  (residues 1 to 184)
  AUTHORS   Kao,B.R., Malerba,A., Lu-Nguyen,N.B., Harish,P., McCarthy,J.J.,
            Dickson,G. and Popplewell,L.J.
  TITLE     Knockdown of Muscle-Specific Ribosomal Protein L3-Like Enhances
            Muscle Function in Healthy and Dystrophic Mice
  JOURNAL   Nucleic Acid Ther 31 (6), 457-464 (2021)
   PUBMED   34081545
REFERENCE   4  (residues 1 to 184)
  AUTHORS   Liang,X., Zuo,M.Q., Zhang,Y., Li,N., Ma,C., Dong,M.Q. and Gao,N.
  TITLE     Structural snapshots of human pre-60S ribosomal particles before
            and after nuclear export
  JOURNAL   Nat Commun 11 (1), 3542 (2020)
   PUBMED   32669547
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 184)
  AUTHORS   Hori,H., Nakamura,S., Yoshida,F., Teraishi,T., Sasayama,D., Ota,M.,
            Hattori,K., Kim,Y., Higuchi,T. and Kunugi,H.
  TITLE     Integrated profiling of phenotype and blood transcriptome for
            stress vulnerability and depression
  JOURNAL   J Psychiatr Res 104, 202-210 (2018)
   PUBMED   30103068
  REMARK    GeneRIF: The present study combines an individual-based phenotypic
            profiling with a transdiagnostic approach and shows that several
            ribosomal genes including RPL17 is involved in stress vulnerability
            across nonclinical and clinical conditions.
REFERENCE   6  (residues 1 to 184)
  AUTHORS   Odintsova,T.I., Muller,E.C., Ivanov,A.V., Egorov,T.A., Bienert,R.,
            Vladimirov,S.N., Kostka,S., Otto,A., Wittmann-Liebold,B. and
            Karpova,G.G.
  TITLE     Characterization and analysis of posttranslational modifications of
            the human large cytoplasmic ribosomal subunit proteins by mass
            spectrometry and Edman sequencing
  JOURNAL   J Protein Chem 22 (3), 249-258 (2003)
   PUBMED   12962325
REFERENCE   7  (residues 1 to 184)
  AUTHORS   Yoshihama,M., Uechi,T., Asakawa,S., Kawasaki,K., Kato,S., Higa,S.,
            Maeda,N., Minoshima,S., Tanaka,T., Shimizu,N. and Kenmochi,N.
  TITLE     The human ribosomal protein genes: sequencing and comparative
            analysis of 73 genes
  JOURNAL   Genome Res 12 (3), 379-390 (2002)
   PUBMED   11875025
REFERENCE   8  (residues 1 to 184)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res 8 (5), 509-523 (1998)
   PUBMED   9582194
REFERENCE   9  (residues 1 to 184)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem Cell Biol 73 (11-12), 933-947 (1995)
   PUBMED   8722009
  REMARK    Review article
REFERENCE   10 (residues 1 to 184)
  AUTHORS   Mager,D.L. and Freeman,J.D.
  TITLE     A human gene related to the ribosomal protein L23 gene of
            Halobacterium marismortui
  JOURNAL   Nucleic Acids Res 18 (17), 5301 (1990)
   PUBMED   2402465
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100778.5.
            
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L22P family of ribosomal proteins. It is located in the
            cytoplasm. This gene has been referred to as rpL23 because the
            encoded protein shares amino acid identity with ribosomal protein
            L23 from Halobacterium marismortui; however, its official symbol is
            RPL17. As is typical for genes encoding ribosomal proteins, there
            are multiple processed pseudogenes of this gene dispersed through
            the genome. Alternative splicing results in multiple transcript
            variants. Read-through transcription also exists between this gene
            and the neighboring downstream C18orf32 (chromosome 18 open reading
            frame 32) gene. [provided by RefSeq, Dec 2010].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: BM456137.1, SRR1163658.194424.1
                                    [ECO:0000331]
            RNAseq introns       :: partial sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q21.1"
     Protein         1..184
                     /product="large ribosomal subunit protein uL22 isoform a"
                     /note="60S ribosomal protein L17; large ribosomal subunit
                     protein uL22; gene encoding putative NFkB activating
                     protein; 60S ribosomal protein L23"
                     /calculated_mol_wt=21266
     Region          1..165
                     /region_name="PTZ00178"
                     /note="60S ribosomal protein L17; Provisional"
                     /db_xref="CDD:240306"
     Site            order(15..16,38..40,42..43,45..46,99..104,112..117,
                     149..150)
                     /site_type="active"
                     /note="putative translocon binding site [active]"
                     /db_xref="CDD:238205"
     Site            order(18,20,23,25..27,30,34,37,97,101,104,116,118..120,
                     122,125,137..142)
                     /site_type="other"
                     /note="protein-rRNA interface [nucleotide binding]"
                     /db_xref="CDD:238205"
     Region          160..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P18621.3)"
     CDS             1..184
                     /gene="RPL17"
                     /gene_synonym="DBA22; L17; PD-1; RPL23; uL22"
                     /coded_by="NM_001369557.1:161..715"
                     /note="isoform a is encoded by transcript variant 11"
                     /db_xref="CCDS:CCDS45865.1"
                     /db_xref="GeneID:6139"
                     /db_xref="HGNC:HGNC:10307"
                     /db_xref="MIM:603661"
ORIGIN      
        1 mvrysldpen ptkscksrgs nlrvhfkntr etaqaikgmh irkatkylkd vtlqkqcvpf
       61 rrynggvgrc aqakqwgwtq grwpkksaef llhmlknaes naelkgldvd slviehiqvn
      121 kapkmrrrty rahgrinpym sspchiemil tekeqivpkp eeevaqkkki sqkklkkqkl
      181 mare
//
LOCUS       NP_060093                707 aa            linear   PRI 20-NOV-2025
DEFINITION  metal transporter CNNM3 isoform 1 precursor [Homo sapiens].
ACCESSION   NP_060093
VERSION     NP_060093.3
DBSOURCE    REFSEQ: accession NM_017623.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 707)
  AUTHORS   Bai,Z., Feng,J., Franken,G.A.C., Al'Saadi,N., Cai,N., Yu,A.S.,
            Lou,L., Komiya,Y., Hoenderop,J.G.J., de Baaij,J.H.F., Yue,L. and
            Runnels,L.W.
  TITLE     CNNM proteins selectively bind to the TRPM7 channel to stimulate
            divalent cation entry into cells
  JOURNAL   PLoS Biol 19 (12), e3001496 (2021)
   PUBMED   34928937
  REMARK    GeneRIF: CNNM proteins selectively bind to the TRPM7 channel to
            stimulate divalent cation entry into cells.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 707)
  AUTHORS   Xu,H., Chai,S.S., Lv,P. and Wang,J.J.
  TITLE     CNN3 in glioma: The prognostic factor and a potential
            immunotherapeutic target
  JOURNAL   Medicine (Baltimore) 100 (46), e27931 (2021)
   PUBMED   34797350
  REMARK    GeneRIF: CNN3 in glioma: The prognostic factor and a potential
            immunotherapeutic target.
REFERENCE   3  (residues 1 to 707)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 707)
  AUTHORS   Cai,F., Huang,Y., Wang,M., Sun,M., Zhao,Y. and Hattori,M.
  TITLE     A FRET-based screening method to detect potential inhibitors of the
            binding of CNNM3 to PRL2
  JOURNAL   Sci Rep 10 (1), 12879 (2020)
   PUBMED   32733084
  REMARK    GeneRIF: A FRET-based screening method to detect potential
            inhibitors of the binding of CNNM3 to PRL2.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 707)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 707)
  AUTHORS   Gomez Garcia,I., Oyenarte,I. and Martinez-Cruz,L.A.
  TITLE     Purification, crystallization and preliminary crystallographic
            analysis of the CBS pair of the human metal transporter CNNM4
  JOURNAL   Acta Crystallogr Sect F Struct Biol Cryst Commun 67 (Pt 3), 349-353
            (2011)
   PUBMED   21393841
REFERENCE   7  (residues 1 to 707)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   8  (residues 1 to 707)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   9  (residues 1 to 707)
  AUTHORS   Venkatesan,K., Rual,J.F., Vazquez,A., Stelzl,U., Lemmens,I.,
            Hirozane-Kishikawa,T., Hao,T., Zenkner,M., Xin,X., Goh,K.I.,
            Yildirim,M.A., Simonis,N., Heinzmann,K., Gebreab,F., Sahalie,J.M.,
            Cevik,S., Simon,C., de Smet,A.S., Dann,E., Smolyar,A.,
            Vinayagam,A., Yu,H., Szeto,D., Borick,H., Dricot,A., Klitgord,N.,
            Murray,R.R., Lin,C., Lalowski,M., Timm,J., Rau,K., Boone,C.,
            Braun,P., Cusick,M.E., Roth,F.P., Hill,D.E., Tavernier,J.,
            Wanker,E.E., Barabasi,A.L. and Vidal,M.
  TITLE     An empirical framework for binary interactome mapping
  JOURNAL   Nat Methods 6 (1), 83-90 (2009)
   PUBMED   19060904
REFERENCE   10 (residues 1 to 707)
  AUTHORS   Wang,C.Y., Shi,J.D., Yang,P., Kumar,P.G., Li,Q.Z., Run,Q.G.,
            Su,Y.C., Scott,H.S., Kao,K.J. and She,J.X.
  TITLE     Molecular cloning and characterization of a novel gene family of
            four ancient conserved domain proteins (ACDP)
  JOURNAL   Gene 306, 37-44 (2003)
   PUBMED   12657465
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK126847.1 and AC092636.3.
            
            On Dec 18, 2003 this sequence version replaced NP_060093.2.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC037272.1, AK126847.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000305510.4/ ENSP00000305449.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..707
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q11.2"
     Protein         1..707
                     /product="metal transporter CNNM3 isoform 1 precursor"
                     /note="ancient conserved domain protein 3; metal
                     transporter CNNM3; cyclin-M3; ancient conserved
                     domain-containing protein 3"
                     /calculated_mol_wt=73791
     sig_peptide     1..25
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2347
     Site            11..27
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE01.1)"
     Region          <13..299
                     /region_name="COG3903"
                     /note="Predicted ATPase [General function prediction
                     only]"
                     /db_xref="CDD:443109"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q8NE01.1)"
     Site            193..213
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE01.1)"
     Site            221..241
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE01.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE01.1)"
     Region          313..442
                     /region_name="CBS_pair_CorC_HlyC_assoc"
                     /note="Two tandem repeats of the cystathionine
                     beta-synthase (CBS pair) domains the majority of which are
                     associated with the CorC_HlyC domain; cd04590"
                     /db_xref="CDD:341366"
     Site            order(321,323..325,348..350,413,434,436,438..439,442)
                     /site_type="other"
                     /note="ligand binding site II [chemical binding]"
                     /db_xref="CDD:341366"
     Region          321..387
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Site            order(348,362,366..367,370,391,413..415,438)
                     /site_type="other"
                     /note="putative ligand binding site I [chemical binding]"
                     /db_xref="CDD:341366"
     Region          391..442
                     /region_name="CBS repeat"
                     /note="CBS repeat [structural motif]"
                     /db_xref="CDD:341366"
     Site            661
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE01.1)"
     Region          678..707
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NE01.1)"
     Site            700
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NE01.1)"
     CDS             1..707
                     /gene="CNNM3"
                     /gene_synonym="ACDP3; SLC70A3"
                     /coded_by="NM_017623.5:11..2134"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS2025.1"
                     /db_xref="GeneID:26505"
                     /db_xref="HGNC:HGNC:104"
                     /db_xref="MIM:607804"
ORIGIN      
        1 maaavaaagr lgwlfaalcl gnaageaapg prvlgfclee dgaagagwvr ggaardtpda
       61 tfllrlfgpg fansswswva pegagcreea aspagewral lrlrlraeav rphsallavr
      121 vepgggaaee aappwalglg aagllalaal arglqlsala lapaevqvlr esgseaeraa
      181 arrleparrw agcalgalll laslaqaala vllyraagqr avpavlgsag lvflvgevvp
      241 aavsgrwtla lapralglsr lavlltlpva lpvgqllela arpgrlrerv lelargggdp
      301 ysdlskgvlr crtvedvltp ledcfmldas tvldfgvlas imqsghtrip vyeeersniv
      361 dmlylkdlaf vdpedctpls titrfynhpl hfvfndtkld avleefkrgk shlaivqkvn
      421 negegdpfye vlglvtledv ieeiirseil desedyrdtv vkrkpaslma plkrkeefsl
      481 fkvsddeykv tispqlllat qrflsrevdv fsplrisekv llhllkhpsv nqevrfdesn
      541 rlathhylyq rsqpvdyfil ilqgrvevei gkeglkfeng aftyygvsal tvpssvhqsp
      601 vsslqpirhd lqpdpgdgth ssaycpdytv ralsdlqlik vtrlqylnal latraqnlpq
      661 spentdlqvi pgsqtrllge ktttaagssh srpgvpvegs pgrnpgv
//
LOCUS       NP_005672                450 aa            linear   PRI 20-NOV-2025
DEFINITION  TATA box-binding protein-associated factor RNA polymerase I subunit
            A isoform 1 [Homo sapiens].
ACCESSION   NP_005672
VERSION     NP_005672.1
DBSOURCE    REFSEQ: accession NM_005681.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Zhang,D.L. and Yang,N.
  TITLE     TNFAIP8 regulates cisplatin resistance through TAF-Ialpha and
            promotes malignant progression of esophageal cancer
  JOURNAL   Eur Rev Med Pharmacol Sci 24 (9), 4775-4784 (2020)
   PUBMED   32432789
  REMARK    GeneRIF: TNFAIP8 regulates cisplatin resistance through TAF-Ialpha
            and promotes malignant progression of esophageal cancer.
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Miller,G., Panov,K.I., Friedrich,J.K., Trinkle-Mulcahy,L.,
            Lamond,A.I. and Zomerdijk,J.C.
  TITLE     hRRN3 is essential in the SL1-mediated recruitment of RNA
            Polymerase I to rRNA gene promoters
  JOURNAL   EMBO J 20 (6), 1373-1382 (2001)
   PUBMED   11250903
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Muth,V., Nadaud,S., Grummt,I. and Voit,R.
  TITLE     Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA
            polymerase I transcription
  JOURNAL   EMBO J 20 (6), 1353-1362 (2001)
   PUBMED   11250901
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Zhai,W. and Comai,L.
  TITLE     Repression of RNA polymerase I transcription by the tumor
            suppressor p53
  JOURNAL   Mol Cell Biol 20 (16), 5930-5938 (2000)
   PUBMED   10913176
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Di Pietro,C., Rapisarda,A., Amico,V., Bonaiuto,C., Viola,A.,
            Scalia,M., Motta,S., Amato,A., Engel,H., Messina,A., Sichel,G.,
            Grzeschik,K. and Purrello,M.
  TITLE     Genomic localization of the human genes TAF1A, TAF1B and TAF1C,
            encoding TAF(I)48, TAF(I)63 and TAF(I)110 subunits of class I
            general transcription initiation factor SL1
  JOURNAL   Cytogenet Cell Genet 89 (1-2), 133-136 (2000)
   PUBMED   10894955
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Comai,L., Zomerdijk,J.C., Beckmann,H., Zhou,S., Admon,A. and
            Tjian,R.
  TITLE     Reconstitution of transcription factor SL1: exclusive binding of
            TBP by SL1 or TFIID subunits
  JOURNAL   Science 266 (5193), 1966-1972 (1994)
   PUBMED   7801123
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Rudloff,U., Eberhard,D., Tora,L., Stunnenberg,H. and Grummt,I.
  TITLE     TBP-associated factors interact with DNA and govern species
            specificity of RNA polymerase I transcription
  JOURNAL   EMBO J 13 (11), 2611-2616 (1994)
   PUBMED   8013460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299536.1, AL592148.7,
            BC013808.1 and CN479053.1.
            
            Summary: This gene encodes a subunit of the RNA polymerase I
            complex, Selectivity Factor I (SLI). The encoded protein is a TATA
            box-binding protein-associated factor that plays a role in the
            assembly of the RNA polymerase I preinitiation complex. Alternate
            splicing results in multiple transcript variants encoding multiple
            isoforms.[provided by RefSeq, Jan 2011].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.189608.1,
                                           SRR1660805.235213.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000352967.9/ ENSP00000327072.6
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q41"
     Protein         1..450
                     /product="TATA box-binding protein-associated factor RNA
                     polymerase I subunit A isoform 1"
                     /note="SL1, 48kD subunit; TBP-associated factor 1A;
                     transcription factor SL1; TATA box-binding
                     protein-associated factor 1A; transcription initiation
                     factor SL1/TIF-IB subunit A; RNA polymerase I-specific
                     TBP-associated factor 48 kDa; TATA-box binding protein
                     associated factor, RNA polymerase I, A; TATA box binding
                     protein (TBP)-associated factor, RNA polymerase I, A,
                     48kD; TATA box binding protein (TBP)-associated factor,
                     RNA polymerase I, A, 48kDa"
                     /calculated_mol_wt=52545
     Region          63..423
                     /region_name="TAF1_subA"
                     /note="TAF RNA Polymerase I subunit A; pfam14929"
                     /db_xref="CDD:434323"
     CDS             1..450
                     /gene="TAF1A"
                     /gene_synonym="MGC:17061; RAFI48; SL1; TAFI48"
                     /coded_by="NM_005681.4:210..1562"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS1531.1"
                     /db_xref="GeneID:9015"
                     /db_xref="HGNC:HGNC:11532"
                     /db_xref="MIM:604903"
ORIGIN      
        1 msdfseelkg pvtddeevet svlsgagmhf pwlqtyvetv aiggkrrkdf aqttsaclsf
       61 iqeallkhqw qqaaeymysy fqtledsdsy krqaapeiiw klgseilfyh pksnmesfnt
      121 fanrmknigv mnylkislqh alyllhhgml kdakrnlsea etwrhgents sreilinliq
      181 aykgllqyyt wsekkmelsk ldkddyayna vaqdvfnhsw ktsanisali kipgvwdpfv
      241 ksyvemlefy gdrdgaqevl tnyaydekfp snpnahiyly nflkrqkapr sklisvlkil
      301 yqivpshklm lefhtllrks ekeehrklgl evlfgvldfa gctknitawk ylakylknil
      361 mgnhlawvqe ewnsrknwwp gfhfsyfwak sdwkedtala cekafvagll lgkgcryfry
      421 ilkqdhqilg kkikrmkrsv kkysivnprl
//
LOCUS       NP_001295154            1091 aa            linear   PRI 20-NOV-2025
DEFINITION  zinc finger protein 521 isoform 2 [Homo sapiens].
ACCESSION   NP_001295154 XP_005258298
VERSION     NP_001295154.1
DBSOURCE    REFSEQ: accession NM_001308225.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1091)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1091)
  AUTHORS   Scicchitano,S., Faniello,M.C. and Mesuraca,M.
  TITLE     Zinc Finger 521 Modulates the Nrf2-Notch Signaling Pathway in Human
            Ovarian Carcinoma
  JOURNAL   Int J Mol Sci 24 (19), 14755 (2023)
   PUBMED   37834202
  REMARK    GeneRIF: Zinc Finger 521 Modulates the Nrf2-Notch Signaling Pathway
            in Human Ovarian Carcinoma.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1091)
  AUTHORS   Scicchitano,S., Montalcini,Y., Lucchino,V., Melocchi,V.,
            Gigantino,V., Chiarella,E., Bianchi,F., Weisz,A. and Mesuraca,M.
  TITLE     Enhanced ZNF521 expression induces an aggressive phenotype in human
            ovarian carcinoma cell lines
  JOURNAL   PLoS One 17 (10), e0274785 (2022)
   PUBMED   36191006
  REMARK    GeneRIF: Enhanced ZNF521 expression induces an aggressive phenotype
            in human ovarian carcinoma cell lines.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1091)
  AUTHORS   Chiarella,E., Aloisio,A., Scicchitano,S., Todoerti,K.,
            Cosentino,E.G., Lico,D., Neri,A., Amodio,N., Bond,H.M. and
            Mesuraca,M.
  TITLE     ZNF521 Enhances MLL-AF9-Dependent Hematopoietic Stem Cell
            Transformation in Acute Myeloid Leukemias by Altering the Gene
            Expression Landscape
  JOURNAL   Int J Mol Sci 22 (19), 10814 (2021)
   PUBMED   34639154
  REMARK    GeneRIF: ZNF521 Enhances MLL-AF9-Dependent Hematopoietic Stem Cell
            Transformation in Acute Myeloid Leukemias by Altering the Gene
            Expression Landscape.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1091)
  AUTHORS   Chiarella,E., Aloisio,A., Scicchitano,S., Bond,H.M. and Mesuraca,M.
  TITLE     Regulatory Role of microRNAs Targeting the Transcription Co-Factor
            ZNF521 in Normal Tissues and Cancers
  JOURNAL   Int J Mol Sci 22 (16), 8461 (2021)
   PUBMED   34445164
  REMARK    GeneRIF: Regulatory Role of microRNAs Targeting the Transcription
            Co-Factor ZNF521 in Normal Tissues and Cancers.
            Review article
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1091)
  AUTHORS   Matsubara,E., Sakai,I., Yamanouchi,J., Fujiwara,H., Yakushijin,Y.,
            Hato,T., Shigemoto,K. and Yasukawa,M.
  TITLE     The role of zinc finger protein 521/early hematopoietic zinc finger
            protein in erythroid cell differentiation
  JOURNAL   J Biol Chem 284 (6), 3480-3487 (2009)
   PUBMED   19049973
  REMARK    GeneRIF: ZNF521 modulates erythroid cell differentiation through
            direct binding with GATA-1.
REFERENCE   7  (residues 1 to 1091)
  AUTHORS   Bond,H.M., Mesuraca,M., Amodio,N., Mega,T., Agosti,V., Fanello,D.,
            Pelaggi,D., Bullinger,L., Grieco,M., Moore,M.A., Venuta,S. and
            Morrone,G.
  TITLE     Early hematopoietic zinc finger protein-zinc finger protein 521: a
            candidate regulator of diverse immature cells
  JOURNAL   Int J Biochem Cell Biol 40 (5), 848-854 (2008)
   PUBMED   17543573
  REMARK    GeneRIF: A review of possible roles for ZNF521 in development, stem
            cell regulation and oncogenesis.
            Review article
REFERENCE   8  (residues 1 to 1091)
  AUTHORS   Bond,H.M., Mesuraca,M., Carbone,E., Bonelli,P., Agosti,V.,
            Amodio,N., De Rosa,G., Di Nicola,M., Gianni,A.M., Moore,M.A.,
            Hata,A., Grieco,M., Morrone,G. and Venuta,S.
  TITLE     Early hematopoietic zinc finger protein (EHZF), the human homolog
            to mouse Evi3, is highly expressed in primitive human hematopoietic
            cells
  JOURNAL   Blood 103 (6), 2062-2070 (2004)
   PUBMED   14630787
  REMARK    GeneRIF: EHZF is likely to play a relevant role in the control of
            human hematopoiesis and might be implicated in the development of
            hematopoietic malignancies.
REFERENCE   9  (residues 1 to 1091)
  AUTHORS   Warming,S., Liu,P., Suzuki,T., Akagi,K., Lindtner,S.,
            Pavlakis,G.N., Jenkins,N.A. and Copeland,N.G.
  TITLE     Evi3, a common retroviral integration site in murine B-cell
            lymphoma, encodes an EBFAZ-related Kruppel-like zinc finger protein
  JOURNAL   Blood 101 (5), 1934-1940 (2003)
   PUBMED   12393497
REFERENCE   10 (residues 1 to 1091)
  AUTHORS   Tchernev,V.T., Mansfield,T.A., Giot,L., Kumar,A.M., Nandabalan,K.,
            Li,Y., Mishra,V.S., Detter,J.C., Rothberg,J.M., Wallace,M.R.,
            Southwick,F.S. and Kingsmore,S.F.
  TITLE     The Chediak-Higashi protein interacts with SNARE complex and signal
            transduction proteins
  JOURNAL   Mol Med 8 (1), 56-64 (2002)
   PUBMED   11984006
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA102816.1, BC032869.2, AC110603.7, BC113622.1, AC105114.3,
            AC104961.7 and CA415157.1.
            
            On Apr 28, 2015 this sequence version replaced XP_005258298.1.
            
            Transcript Variant: This variant (2) lacks an alternate exon in the
            5' coding region, resulting in the use of a downstream start codon,
            compared to variant 1. The encoded isoform (2) has a shorter
            N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.3842.1,
                                           SRR1803613.214827.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1968189,
                                           SAMEA1968540 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1091
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q11.2"
     Protein         1..1091
                     /product="zinc finger protein 521 isoform 2"
                     /note="LYST-interacting protein 3; early hematopoietic
                     zinc finger protein"
                     /calculated_mol_wt=122809
     Region          28..49
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(33,35,37,39..40,43..44,48,68,70,74..75,78..79,83,97,
                     99,101,103..104,107..108,111)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          63..84
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          92..112
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          187..208
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(192,195,197,199..200,203..204,207,224,226,230..231,
                     234..235,239,264,266,268,270..271,274..275,278)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          219..240
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          259..278
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          416..436
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(421,423,425,427..428,431..432,435,451,453,457..458,
                     461..462,465,481,483,485,487..488,491..492)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          446..466
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          476..493
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          504..525
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(509,511,513,515..516,519..520,523,539,541,545..546,
                     549..550,553,570,572,574,576..577,580..581,584)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          534..554
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          565..>744
                     /region_name="COG5236"
                     /note="Uncharacterized conserved protein, contains RING
                     Zn-finger [General function prediction only]"
                     /db_xref="CDD:227561"
     Region          565..585
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          591..609
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          668..689
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(673,675,677,679..680,683..684,688,717,719,723..724,
                     727..728,731,746,748,750,752..753,756..757,760)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          712..732
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          741..761
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1007..1027
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Site            order(1012,1014,1016,1018..1019,1022..1023,1026,1043,1045,
                     1049..1050,1053..1054,1058,1073,1075,1077,1079..1080,
                     1083..1084,1087)
                     /site_type="other"
                     /note="putative nucleic acid binding site [nucleotide
                     binding]"
                     /db_xref="CDD:275368"
     Region          1038..1059
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     Region          1068..1087
                     /region_name="C2H2 Zn finger"
                     /note="C2H2 Zn finger [structural motif]"
                     /db_xref="CDD:275368"
     CDS             1..1091
                     /gene="ZNF521"
                     /gene_synonym="EHZF; Evi3"
                     /coded_by="NM_001308225.2:783..4058"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS77167.1"
                     /db_xref="GeneID:25925"
                     /db_xref="HGNC:HGNC:24605"
                     /db_xref="MIM:610974"
ORIGIN      
        1 mqvhernkdg sqsgsrmedw kmkdtqkcsq ceegfdfped lqkhiaechp ecspnedraa
       61 lqcvychelf veetslmnhm eqvhsgekkn scsicsesfh tveelyshmd shqqpescnh
      121 snspslvtvg ytsvssttpd snlsvdsstm veaappipks rgrkraaqqt pdmtgpsskq
      181 akvtysciyc nkqlfsslav lqihlktmhl dkpeqahicq yclevlpsly nlnehlkqvh
      241 eaqdpglivs ampaivyqcn fcsevvndln tlqehircsh gfanpaakds naffcphcym
      301 gfltdsslee hirqvhcdls gsrfgspvlg tpkepvvevy scsyctnspi fnsvlklnkh
      361 ikenhknipl alnyihngkk sralsplspv aieqtslkmm qavggaparp tgeyicnqcg
      421 akytsldsfq thlkthldtv lpkltcpqcn kefpnqesll khvtihfmit styyicescd
      481 kqftsvddlq khlldmhtfv ffrctlcqev fdskvsiqlh lavkhsnekk vyrctscnwd
      541 frnetdlqlh vkhnhlenqg kvhkcifcge sfgtevelqc hitthskkyn ckfcskafha
      601 iillekhlre khcvfetktp ncgtngaseq vqkeevelqt lltnsqeshn shdgseedvd
      661 tsepmygcdi cgaaytmetl lqnhqlrdhn irpgesaivk kkaelikgny kcnvcsrtff
      721 senglrehmq thlgpvkhym cpicgerfps lltltehkvt hsksldtgnc rickmplqse
      781 eeflehcqmh pdlrnsltgf rcvvcmqtvt stlelkihgt fhmqktgngs avqttgrgqh
      841 vqklykcasc lkefrskqdl vkldinglpy glcagcvnls ksaspginvp pgtnrpglgq
      901 nenlsaiegk gkvgglktrc sscnvkfese selqnhiqti hrelvpdsns tqlktpqvsp
      961 mprispsqsd ekktyqcikc qmvfynewdi qvhvanhmid eglnhecklc sqtfdspakl
     1021 qchliehsfe gmggtfkcpv cftvfvqank lqqhifsahg qedkiydctq cpqkfffqte
     1081 lqnhtmtqhs s
//
LOCUS       NP_001354471             326 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit gamma
            isoform 35 [Homo sapiens].
ACCESSION   NP_001354471
VERSION     NP_001354471.1
DBSOURCE    REFSEQ: accession NM_001367542.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 326)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 326)
  AUTHORS   Gurd,B.J., Menezes,E.S., Arhen,B.B. and Islam,H.
  TITLE     Impacts of altered exercise volume, intensity, and duration on the
            activation of AMPK and CaMKII and increases in PGC-1alpha mRNA
  JOURNAL   Semin Cell Dev Biol 143, 17-27 (2023)
   PUBMED   35680515
  REMARK    GeneRIF: Impacts of altered exercise volume, intensity, and
            duration on the activation of AMPK and CaMKII and increases in
            PGC-1alpha mRNA.
            Review article
REFERENCE   3  (residues 1 to 326)
  AUTHORS   Koren,D.T., Shrivastava,R. and Ghosh,S.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II Disrupts the Voltage
            Dependency of the Voltage-Dependent Anion Channel on the Lipid
            Bilayer Membrane
  JOURNAL   J Phys Chem B 127 (15), 3372-3381 (2023)
   PUBMED   37040575
  REMARK    GeneRIF: Ca[2+]/Calmodulin-Dependent Protein Kinase II Disrupts the
            Voltage Dependency of the Voltage-Dependent Anion Channel on the
            Lipid Bilayer Membrane.
REFERENCE   4  (residues 1 to 326)
  AUTHORS   Zhu,S., Zhang,X., Guo,Y., Tang,L., Zhou,Z., Chen,X. and Peng,C.
  TITLE     NETO2 promotes melanoma progression via activation of the
            Ca2+/CaMKII signaling pathway
  JOURNAL   Front Med 17 (2), 263-274 (2023)
   PUBMED   36738427
  REMARK    GeneRIF: NETO2 promotes melanoma progression via activation of the
            Ca[2+]/CaMKII signaling pathway.
REFERENCE   5  (residues 1 to 326)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 326)
  AUTHORS   Wen,Z., Zhong,Z. and Darnell,J.E. Jr.
  TITLE     Maximal activation of transcription by Stat1 and Stat3 requires
            both tyrosine and serine phosphorylation
  JOURNAL   Cell 82 (2), 241-250 (1995)
   PUBMED   7543024
REFERENCE   7  (residues 1 to 326)
  AUTHORS   Countaway,J.L., Nairn,A.C. and Davis,R.J.
  TITLE     Mechanism of desensitization of the epidermal growth factor
            receptor protein-tyrosine kinase
  JOURNAL   J Biol Chem 267 (2), 1129-1140 (1992)
   PUBMED   1309762
REFERENCE   8  (residues 1 to 326)
  AUTHORS   Ikebe,M. and Reardon,S.
  TITLE     Phosphorylation of smooth myosin light chain kinase by smooth
            muscle Ca2+/calmodulin-dependent multifunctional protein kinase
  JOURNAL   J Biol Chem 265 (16), 8975-8978 (1990)
   PUBMED   2160950
REFERENCE   9  (residues 1 to 326)
  AUTHORS   Czernik,A.J., Pang,D.T. and Greengard,P.
  TITLE     Amino acid sequences surrounding the cAMP-dependent and
            calcium/calmodulin-dependent phosphorylation sites in rat and
            bovine synapsin I
  JOURNAL   Proc Natl Acad Sci U S A 84 (21), 7518-7522 (1987)
   PUBMED   3118371
REFERENCE   10 (residues 1 to 326)
  AUTHORS   Vulliet,P.R., Woodgett,J.R. and Cohen,P.
  TITLE     Phosphorylation of tyrosine hydroxylase by calmodulin-dependent
            multiprotein kinase
  JOURNAL   J Biol Chem 259 (22), 13680-13683 (1984)
   PUBMED   6150037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL596247.22, AL713896.9 and
            AC022400.9.
            
            Summary: The product of this gene is one of the four subunits of an
            enzyme which belongs to the serine/threonine protein kinase family,
            and to the Ca(2+)/calmodulin-dependent protein kinase subfamily.
            Calcium signaling is crucial for several aspects of plasticity at
            glutamatergic synapses. In mammalian cells the enzyme is composed
            of four different chains: alpha, beta, gamma, and delta. The
            product of this gene is a gamma chain. Many alternatively spliced
            transcripts encoding different isoforms have been described but the
            full-length nature of all the variants has not been
            determined.[provided by RefSeq, Mar 2011].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR5189652.234430.1, SRR3476690.492485.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..326
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q22.2"
     Protein         1..326
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit gamma isoform 35"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II gamma; calcium/calmodulin-dependent protein
                     kinase type II subunit gamma; caMK-II subunit gamma"
                     /calculated_mol_wt=35338
     Region          <1..52
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Region          194..321
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..326
                     /gene="CAMK2G"
                     /gene_synonym="CAMK; CAMK-II; CAMKG; MRD59"
                     /coded_by="NM_001367542.1:982..1962"
                     /note="isoform 35 is encoded by transcript variant 35"
                     /db_xref="GeneID:818"
                     /db_xref="HGNC:HGNC:1463"
                     /db_xref="MIM:602123"
ORIGIN      
        1 mltinpakri tadqalkhpw vcqrstvasm mhrqetvecl rkfnarrklk gailttmlvs
       61 rnfsvgrqss apaspaasaa glagqaaksl lnkksdggvk pqsnnknslv spaqepaplq
      121 tamepqttvv hnatdgikgs tescnttted edlkaaplrt gngssvpegr ssrdrtapsa
      181 gmqpqpslcs samrkqeiik iteqlieain ngdfeaytki cdpgltsfep ealgnlvegm
      241 dfhkfyfenl lsknskpiht tilnphvhvi gedaaciayi rltqyidgqg rprtsqseet
      301 rvwhrrdgkw lnvhyhcsga paaplq
//
LOCUS       NP_001006666             744 aa            linear   PRI 20-NOV-2025
DEFINITION  ribosomal protein S6 kinase alpha-1 isoform b [Homo sapiens].
ACCESSION   NP_001006666
VERSION     NP_001006666.1
DBSOURCE    REFSEQ: accession NM_001006665.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 744)
  AUTHORS   Zhou,N., Guo,C., Du,J., Xu,Q., Li,J., Huang,D., Zheng,X. and Tu,L.
  TITLE     PPP1R14B-mediated phosphorylation enhances protein stability of
            RPS6KA1 to promote hepatocellular carcinoma tumorigenesis
  JOURNAL   Biochim Biophys Acta Mol Cell Res 1871 (8), 119840 (2024)
   PUBMED   39216602
  REMARK    GeneRIF: PPP1R14B-mediated phosphorylation enhances protein
            stability of RPS6KA1 to promote hepatocellular carcinoma
            tumorigenesis.
REFERENCE   2  (residues 1 to 744)
  AUTHORS   Guo,X., Huang,G., Qiu,D., He,H., Niu,X., Guo,Z. and Ye,Y.
  TITLE     RPS6KA1 is a histone acetylation-related oncoprotein in acute
            myeloid leukemia which is targeted by afzelin
  JOURNAL   BMC Cancer 24 (1), 1189 (2024)
   PUBMED   39333927
  REMARK    GeneRIF: RPS6KA1 is a histone acetylation-related oncoprotein in
            acute myeloid leukemia which is targeted by afzelin.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 744)
  AUTHORS   Wu,S., Jin,J., Huang,J., Chen,G. and Chen,Y.
  TITLE     Comprehensive analysis of the RSK gene family in acute myeloid
            leukemia determines a prognostic signature for the prediction of
            clinical prognosis and treatment responses
  JOURNAL   Hematology 28 (1), 2235833 (2023)
   PUBMED   37462338
  REMARK    GeneRIF: Comprehensive analysis of the RSK gene family in acute
            myeloid leukemia determines a prognostic signature for the
            prediction of clinical prognosis and treatment responses.
REFERENCE   4  (residues 1 to 744)
  AUTHORS   Weidenauer,K., Schmidt,C., Rohde,C., Pauli,C., Blank,M.F., Heid,D.,
            Waclawiczek,A., Corbacioglu,A., Gollner,S., Lotze,M., Vierbaum,L.,
            Renders,S., Krijgsveld,J., Raffel,S., Sauer,T., Trumpp,A.,
            Pabst,C., Muller-Tidow,C. and Janssen,M.
  TITLE     The ribosomal protein S6 kinase alpha-1 (RPS6KA1) induces
            resistance to venetoclax/azacitidine in acute myeloid leukemia
  JOURNAL   Leukemia 37 (8), 1611-1625 (2023)
   PUBMED   37414921
  REMARK    GeneRIF: The ribosomal protein S6 kinase alpha-1 (RPS6KA1) induces
            resistance to venetoclax/azacitidine in acute myeloid leukemia.
REFERENCE   5  (residues 1 to 744)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 744)
  AUTHORS   Moller,D.E., Xia,C.H., Tang,W., Zhu,A.X. and Jakubowski,M.
  TITLE     Human rsk isoforms: cloning and characterization of tissue-specific
            expression
  JOURNAL   Am J Physiol 266 (2 Pt 1), C351-C359 (1994)
   PUBMED   8141249
REFERENCE   7  (residues 1 to 744)
  AUTHORS   Chen,R.H., Abate,C. and Blenis,J.
  TITLE     Phosphorylation of the c-Fos transrepression domain by
            mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
  JOURNAL   Proc Natl Acad Sci U S A 90 (23), 10952-10956 (1993)
   PUBMED   8248197
REFERENCE   8  (residues 1 to 744)
  AUTHORS   Rivera,V.M., Miranti,C.K., Misra,R.P., Ginty,D.D., Chen,R.H.,
            Blenis,J. and Greenberg,M.E.
  TITLE     A growth factor-induced kinase phosphorylates the serum response
            factor at a site that regulates its DNA-binding activity
  JOURNAL   Mol Cell Biol 13 (10), 6260-6273 (1993)
   PUBMED   8413226
REFERENCE   9  (residues 1 to 744)
  AUTHORS   Tratner,I., Ofir,R. and Verma,I.M.
  TITLE     Alteration of a cyclic AMP-dependent protein kinase phosphorylation
            site in the c-Fos protein augments its transforming potential
  JOURNAL   Mol Cell Biol 12 (3), 998-1006 (1992)
   PUBMED   1545828
REFERENCE   10 (residues 1 to 744)
  AUTHORS   Chen,R.H., Sarnecki,C. and Blenis,J.
  TITLE     Nuclear localization and regulation of erk- and rsk-encoded protein
            kinases
  JOURNAL   Mol Cell Biol 12 (3), 915-927 (1992)
   PUBMED   1545823
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL627313.16.
            
            Summary: This gene encodes a member of the RSK (ribosomal S6
            kinase) family of serine/threonine kinases. This kinase contains 2
            nonidentical kinase catalytic domains and phosphorylates various
            substrates, including members of the mitogen-activated kinase
            (MAPK) signalling pathway. The activity of this protein has been
            implicated in controlling cell growth and differentiation.
            Alternate transcriptional splice variants, encoding different
            isoforms, have been characterized. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) differs in the 5' UTR and 5'
            end of the coding region compared to variant 1. These differences
            cause translation initiation at an in-frame AUG of an alternate
            exon and an isoform (b) with a distinct N-terminus compared to
            isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.115812.1,
                                           SRR1803611.103557.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..744
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..744
                     /product="ribosomal protein S6 kinase alpha-1 isoform b"
                     /EC_number="2.7.11.1"
                     /note="p90-RSK 1; ribosomal protein S6 kinase alpha-1;
                     S6K-alpha 1; dJ590P13.1 (ribosomal protein S6 kinase,
                     90kD, polypeptide 1); RSK-1; p90S6K; p90RSK1; MAPKAPK-1a;
                     MAPKAP kinase 1a; ribosomal S6 kinase 1; ribosomal protein
                     S6 kinase, 90kDa, polypeptide 1; MAPK-activated protein
                     kinase 1a; 90 kDa ribosomal protein S6 kinase 1; MAP
                     kinase-activated protein kinase 1a"
                     /calculated_mol_wt=83802
     Region          75..391
                     /region_name="STKc_RSK_N"
                     /note="N-terminal catalytic domain of the Serine/Threonine
                     Kinase, 90 kDa ribosomal protein S6 kinase; cd05582"
                     /db_xref="CDD:270734"
     Site            order(77..81,85,101,103,134,150..151,153,157,159,196,198,
                     200..201,203,213..214,217,231..236,263,269,272)
                     /site_type="active"
                     /db_xref="CDD:270734"
     Site            order(77..81,85,101,103,134,151..153,157,196,198,200..201,
                     203,213..214)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270734"
     Site            order(81,157,159,196,198,200,217,231..236,263,269,272)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270734"
     Site            order(213..224,226..236)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270734"
     Site            372
                     /site_type="other"
                     /note="turn motif phosphorylation site [posttranslational
                     modification]"
                     /db_xref="CDD:270734"
     Site            385..390
                     /site_type="other"
                     /note="hydrophobic motif (HM)"
                     /db_xref="CDD:270734"
     Region          425..715
                     /region_name="STKc_RSK1_C"
                     /note="C-terminal catalytic domain of the Serine/Threonine
                     Kinase, Ribosomal S6 kinase 1 (also called Ribosomal
                     protein S6 kinase alpha-1 or 90kDa ribosomal protein S6
                     kinase 1); cd14175"
                     /db_xref="CDD:271077"
     Site            order(433..437,441,454,456,482,498..501,505,507,543..544,
                     546,548..549,551,565..566,569,584..588,590)
                     /site_type="active"
                     /db_xref="CDD:271077"
     Site            order(433..436,441,454,456,482,498..501,505,548..549,551,
                     565..566)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:271077"
     Site            order(437,505,507,543..544,546,548,569,584..588,590)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:271077"
     Site            565..588
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:271077"
     CDS             1..744
                     /gene="RPS6KA1"
                     /gene_synonym="HU-1; MAPKAPK1; MAPKAPK1A; p90Rsk; RSK;
                     RSK1"
                     /coded_by="NM_001006665.2:60..2294"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS30649.1"
                     /db_xref="GeneID:6195"
                     /db_xref="HGNC:HGNC:10430"
                     /db_xref="MIM:601684"
ORIGIN      
        1 meqdpkpprl rlwalipwlp rkqrprisqt slpvpgpgsg pqrdsdegvl keisithhvk
       61 agsekadpsh fellkvlgqg sfgkvflvrk vtrpdsghly amkvlkkatl kvrdrvrtkm
      121 erdiladvnh pfvvklhyaf qtegklylil dflrggdlft rlskevmfte edvkfylael
      181 algldhlhsl giiyrdlkpe nilldeeghi kltdfglske aidhekkays fcgtveymap
      241 evvnrqghsh sadwwsygvl mfemltgslp fqgkdrketm tlilkaklgm pqflsteaqs
      301 llralfkrnp anrlgsgpdg aeeikrhvfy stidwnklyr reikppfkpa vaqpddtfyf
      361 dteftsrtpk dspgippsag ahqlfrgfsf vatglmeddg kprapqaplh svvqqlhgkn
      421 lvfsdgyvvk etigvgsyse ckrcvhkatn meyavkvidk skrdpseeie illrygqhpn
      481 iitlkdvydd gkhvylvtel mrggelldki lrqkffsere asfvlhtigk tveylhsqgv
      541 vhrdlkpsni lyvdesgnpe clricdfgfa kqlraengll mtpcytanfv apevlkrqgy
      601 degcdiwslg illytmlagy tpfangpsdt peeiltrigs gkftlsggnw ntvsetakdl
      661 vskmlhvdph qrltakqvlq hpwvtqkdkl pqsqlshqdl qlvkgamaat ysalnsskpt
      721 pqlkpiessi laqrrvrklp sttl
//
LOCUS       NP_001354644             824 aa            linear   PRI 20-NOV-2025
DEFINITION  la-related protein 1 isoform 4 [Homo sapiens].
ACCESSION   NP_001354644 XP_016864773
VERSION     NP_001354644.1
DBSOURCE    REFSEQ: accession NM_001367715.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 824)
  AUTHORS   Ma,J., Dong,D., Qi,H., Li,J., Yu,H., Hu,X., Sun,L. and Shen,L.
  TITLE     LARP1, an RNA-binding protein, participates in ovarian cancer cell
            survival by regulating mitochondrial oxidative phosphorylation in
            response to the influence of the PI3K/mTOR pathway
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (8), 167453 (2024)
   PUBMED   39111634
  REMARK    GeneRIF: LARP1, an RNA-binding protein, participates in ovarian
            cancer cell survival by regulating mitochondrial oxidative
            phosphorylation in response to the influence of the PI3K/mTOR
            pathway.
REFERENCE   2  (residues 1 to 824)
  AUTHORS   Chettle,J., Louie,R.J., Larner,O., Best,R., Chen,K., Morris,J.,
            Dedeic,Z., Childers,A., Rogers,R.C., DuPont,B.R., Skinner,C.,
            Kury,S., Uguen,K., Planes,M., Monteil,D., Li,M., Eliyahu,A.,
            Greenbaum,L., Mor,N., Besnard,T., Isidor,B., Cogne,B., Blesson,A.,
            Comi,A., Wentzensen,I.M., Vuocolo,B., Lalani,S.R., Sierra,R.,
            Berry,L., Carter,K., Sanders,S.J. and Blagden,S.P.
  TITLE     LARP1 haploinsufficiency is associated with an autosomal dominant
            neurodevelopmental disorder
  JOURNAL   HGG Adv 5 (4), 100345 (2024)
   PUBMED   39182167
  REMARK    GeneRIF: LARP1 haploinsufficiency is associated with an autosomal
            dominant neurodevelopmental disorder.
REFERENCE   3  (residues 1 to 824)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 824)
  AUTHORS   Smith,B.C. and Silvers,R.
  TITLE     1H, 13C, and 15N resonance assignments of the La Motif of the human
            La-related protein 1
  JOURNAL   Biomol NMR Assign 18 (1), 111-118 (2024)
   PUBMED   38691336
  REMARK    GeneRIF: [1]H, [13]C, and [15]N resonance assignments of the La
            Motif of the human La-related protein 1.
REFERENCE   5  (residues 1 to 824)
  AUTHORS   Kozlov,G., Jiang,J., Rutherford,T., Noronha,A.M., Wilds,C.J. and
            Gehring,K.
  TITLE     Enhanced binding of guanylated poly(A) RNA by the LaM domain of
            LARP1
  JOURNAL   RNA Biol 21 (1), 7-16 (2024)
   PUBMED   39016322
  REMARK    GeneRIF: Enhanced binding of guanylated poly(A) RNA by the LaM
            domain of LARP1.
REFERENCE   6  (residues 1 to 824)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
REFERENCE   7  (residues 1 to 824)
  AUTHORS   Burrows,C., Abd Latip,N., Lam,S.J., Carpenter,L., Sawicka,K.,
            Tzolovsky,G., Gabra,H., Bushell,M., Glover,D.M., Willis,A.E. and
            Blagden,S.P.
  TITLE     The RNA binding protein Larp1 regulates cell division, apoptosis
            and cell migration
  JOURNAL   Nucleic Acids Res 38 (16), 5542-5553 (2010)
   PUBMED   20430826
REFERENCE   8  (residues 1 to 824)
  AUTHORS   Meek,S.E., Lane,W.S. and Piwnica-Worms,H.
  TITLE     Comprehensive proteomic analysis of interphase and mitotic
            14-3-3-binding proteins
  JOURNAL   J Biol Chem 279 (31), 32046-32054 (2004)
   PUBMED   15161933
REFERENCE   9  (residues 1 to 824)
  AUTHORS   Horke,S., Reumann,K., Schweizer,M., Will,H. and Heise,T.
  TITLE     Nuclear trafficking of La protein depends on a newly identified
            nucleolar localization signal and the ability to bind RNA
  JOURNAL   J Biol Chem 279 (25), 26563-26570 (2004)
   PUBMED   15060081
  REMARK    GeneRIF: Nuclear trafficking of La protein depends on a newly
            identified nucleolar localization signal and the ability to bind
            RNA
REFERENCE   10 (residues 1 to 824)
  AUTHORS   Chauvet,S., Maurel-Zaffran,C., Miassod,R., Jullien,N., Pradel,J.
            and Aragnol,D.
  TITLE     dlarp, a new candidate Hox target in Drosophila whose orthologue in
            mouse is expressed at sites of epithelium/mesenchymal interactions
  JOURNAL   Dev Dyn 218 (3), 401-413 (2000)
   PUBMED   10878606
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC008379.7 and AC112169.2.
            
            On Dec 13, 2018 this sequence version replaced XP_016864773.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803611.64464.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..824
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.2"
     Protein         1..824
                     /product="la-related protein 1 isoform 4"
                     /note="la-related protein 1; La ribonucleoprotein domain
                     family member 1"
                     /calculated_mol_wt=95261
     Region          <6..283
                     /region_name="LHP1"
                     /note="La protein, small RNA-binding pol III transcript
                     stabilizing protein and related La-motif-containing
                     proteins involved in translation [Posttranslational
                     modification, protein turnover, chaperones / Translation,
                     ribosomal structure and biogenesis]; COG5193"
                     /db_xref="CDD:227520"
     Region          132..204
                     /region_name="LAM"
                     /note="LA motif RNA-binding domain; cl02755"
                     /db_xref="CDD:470666"
     Site            order(138,141..142,147,150..151,153,172..174)
                     /site_type="other"
                     /note="RNA binding site [nucleotide binding]"
                     /db_xref="CDD:153396"
     Region          613..653
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     Region          654..692
                     /region_name="DM15"
                     /note="Tandem repeat in fly CG14066 (La related protein),
                     human KIAA0731 and worm R144.7. Unknown function;
                     smart00684"
                     /db_xref="CDD:128927"
     CDS             1..824
                     /gene="LARP1"
                     /gene_synonym="Lar1; LARP; Lhp1"
                     /coded_by="NM_001367715.1:239..2713"
                     /note="isoform 4 is encoded by transcript variant 5"
                     /db_xref="GeneID:23367"
                     /db_xref="HGNC:HGNC:29531"
                     /db_xref="MIM:612059"
ORIGIN      
        1 mkeqekgegs dskespktks desgeekngd edcqrggqkk kgnkhkwvpl qidmkpevpr
       61 eklasrptrp peprhipanr geikahfdyq fgyrkfdgve gprtpkymnn ityyfdnvss
      121 telysvdqel lkdyikrqie yyfsvdnler dfflrrkmda dgflpitlia sfhrvqaltt
      181 dislifaalk dskvveivde kvrrreepek wplppivdys qtdfsqllnc pefvprqhyq
      241 ketesapgsp ravtpvptkt eevsnlktlp kglsaslpdl dsenwievkk rprpsparpk
      301 kseesrfshl tslpqqlpsq qlmskdqdeq eeldflfdee meqmdgrknt ftawsdeesd
      361 yeiddrdvnk ilivtqtphy mrrhpggdrt gnhtsrakms aelakvindg lfyyeqdlwa
      421 ekfepeysqi kqevenfkkv nmisreqfdt ltpeppvdpn qevppgpprf qqvptdalan
      481 klfgapepst iarslpttvp espnyrntrt prtprtpqlk dssqtsrfyp vvkegrtlda
      541 kmprkrktrh ssnppleshv gwvmdsrehr prtasisssp segtptvgsy gctpqslpkf
      601 qhpshellke ngftqhvyhk yrrrclnerk rlgigqsqem ntlfrfwsff lrdhfnkkmy
      661 eefkqlaled akegyrygle clfryysygl ekkfrldifk dfqeetvkdy eagqlyglek
      721 fwaflkyska knldidpklq eylgkfrrle dfrvdppmge egnhkrhsvv agggggegrk
      781 rcpsqsssrp aamisqpptp ptgqpvreda kwtsqhsntq tlgk
//
LOCUS       NP_004283                783 aa            linear   PRI 20-NOV-2025
DEFINITION  ras and Rab interactor 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004283
VERSION     NP_004283.2
DBSOURCE    REFSEQ: accession NM_004292.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 783)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 783)
  AUTHORS   Osei Saahene,R., Barnes,P., Yeboah,F.A., Agbo,E., Asante,D.B. and
            Arhin,S.K.
  TITLE     Expression of RAS and RAB interactor 1 (RIN1) in head and neck
            tumors at selected hospital in Ghana
  JOURNAL   PLoS One 19 (4), e0301295 (2024)
   PUBMED   38635569
  REMARK    GeneRIF: Expression of RAS and RAB interactor 1 (RIN1) in head and
            neck tumors at selected hospital in Ghana.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 783)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 783)
  AUTHORS   Swaney,D.L., Ramms,D.J., Wang,Z., Park,J., Goto,Y., Soucheray,M.,
            Bhola,N., Kim,K., Zheng,F., Zeng,Y., McGregor,M., Herrington,K.A.,
            O'Keefe,R., Jin,N., VanLandingham,N.K., Foussard,H., Von Dollen,J.,
            Bouhaddou,M., Jimenez-Morales,D., Obernier,K., Kreisberg,J.F.,
            Kim,M., Johnson,D.E., Jura,N., Grandis,J.R., Gutkind,J.S.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein network map of head and neck cancer reveals PIK3CA mutant
            drug sensitivity
  JOURNAL   Science 374 (6563), eabf2911 (2021)
   PUBMED   34591642
REFERENCE   5  (residues 1 to 783)
  AUTHORS   Kim,M., Park,J., Bouhaddou,M., Kim,K., Rojc,A., Modak,M.,
            Soucheray,M., McGregor,M.J., O'Leary,P., Wolf,D., Stevenson,E.,
            Foo,T.K., Mitchell,D., Herrington,K.A., Munoz,D.P., Tutuncuoglu,B.,
            Chen,K.H., Zheng,F., Kreisberg,J.F., Diolaiti,M.E., Gordan,J.D.,
            Coppe,J.P., Swaney,D.L., Xia,B., van 't Veer,L., Ashworth,A.,
            Ideker,T. and Krogan,N.J.
  TITLE     A protein interaction landscape of breast cancer
  JOURNAL   Science 374 (6563), eabf3066 (2021)
   PUBMED   34591612
REFERENCE   6  (residues 1 to 783)
  AUTHORS   Afar,D.E., Han,L., McLaughlin,J., Wong,S., Dhaka,A., Parmar,K.,
            Rosenberg,N., Witte,O.N. and Colicelli,J.
  TITLE     Regulation of the oncogenic activity of BCR-ABL by a tightly bound
            substrate protein RIN1
  JOURNAL   Immunity 6 (6), 773-782 (1997)
   PUBMED   9208849
REFERENCE   7  (residues 1 to 783)
  AUTHORS   Han,L., Wong,D., Dhaka,A., Afar,D., White,M., Xie,W., Herschman,H.,
            Witte,O. and Colicelli,J.
  TITLE     Protein binding and signaling properties of RIN1 suggest a unique
            effector function
  JOURNAL   Proc Natl Acad Sci U S A 94 (10), 4954-4959 (1997)
   PUBMED   9144171
REFERENCE   8  (residues 1 to 783)
  AUTHORS   Han,L. and Colicelli,J.
  TITLE     A human protein selected for interference with Ras function
            interacts directly with Ras and competes with Raf1
  JOURNAL   Mol Cell Biol 15 (3), 1318-1323 (1995)
   PUBMED   7862125
REFERENCE   9  (residues 1 to 783)
  AUTHORS   Colicelli,J., Nicolette,C., Birchmeier,C., Rodgers,L., Riggs,M. and
            Wigler,M.
  TITLE     Expression of three mammalian cDNAs that interfere with RAS
            function in Saccharomyces cerevisiae
  JOURNAL   Proc Natl Acad Sci U S A 88 (7), 2913-2917 (1991)
   PUBMED   1849280
REFERENCE   10 (residues 1 to 783)
  AUTHORS   Trowbridge,I.S., Lesley,J., Trotter,J. and Hyman,R.
  TITLE     Thymocyte subpopulation enriched for progenitors with an
            unrearranged T-cell receptor beta-chain gene
  JOURNAL   Nature 315 (6021), 666-669 (1985)
   PUBMED   3874369
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            L36463.1, BC014417.1, BQ956294.1, BG163919.1 and AP001107.5.
            
            On Jul 6, 2005 this sequence version replaced NP_004283.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: L36463.1, SRR3476690.1091027.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000311320.9/ ENSP00000310406.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..783
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13.2"
     Protein         1..783
                     /product="ras and Rab interactor 1 isoform 1"
                     /note="ras inhibitor 1; ras inhibitor RIN1; ras inhibitor
                     JC99; ras interaction/interference protein 1"
                     /calculated_mol_wt=83968
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Site            3
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Site            16
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and ABL2.
                     /evidence=ECO:0000269|PubMed:15886098; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Region          58..158
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(76,94,119,121)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198256"
     Site            order(120,147)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198256"
     Site            210
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Region          250..282
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Site            258
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Region          294..727
                     /region_name="Ras and 14-3-3 protein binding region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Region          295..342
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Site            333
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Site            337
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:16964243,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Site            351
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKD/PRKD1.
                     /evidence=ECO:0000269|PubMed:11784866,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     Region          489..607
                     /region_name="VPS9"
                     /note="Domain present in VPS9; smart00167"
                     /db_xref="CDD:128469"
     Site            609
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Site            611
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Region          625..705
                     /region_name="Ubl1_cv_Nsp3_N-like"
                     /note="first ubiquitin-like (Ubl) domain located at the
                     N-terminus of coronavirus SARS-CoV non-structural protein
                     3 (Nsp3) and related proteins; cl28922"
                     /db_xref="CDD:475130"
     Site            692
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q13671.4)"
     Region          709..783
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q13671.4)"
     CDS             1..783
                     /gene="RIN1"
                     /coded_by="NM_004292.3:33..2384"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS31614.1"
                     /db_xref="GeneID:9610"
                     /db_xref="HGNC:HGNC:18749"
                     /db_xref="MIM:605965"
ORIGIN      
        1 mespgesgag spgapspssf ttghlarekp aqdplydvpn asggqaggpq rpgrvvslre
       61 rllltrpvwl qlqanaaaal hmlrteppgt flvrksntrq cqalcmrlpe asgpsfvssh
      121 yilespggvs legselmfpd lvqlicaych trdilllplq lpraihhaat hkeleaishl
      181 giefwsssln ikaqrgpagg pvlpqlkars pqeldqgtga alcffnplfp gdlgptkrek
      241 fkrsfkvrvs tetssplspp avppppvpvl pgavpsqter lppcqllrre ssvgyrvpag
      301 sgpslppmps lqevdcgsps sseeegvpgs rgspatsphl grrrpllrsm saafcsllap
      361 erqvgraaaa lmqdrhtaag qlvqdlltqv ragpepqelq girqalsrar amlsaelgpe
      421 kllspkrleh vlekslhcsv lkplrpilaa rlrrrlaadg slgrlaeglr laraqgpgaf
      481 gshlslpspv eleqvrqkll qllrtyspsa qvkrllqack llymalrtqe gegagadefl
      541 pllslvlahc dlpellleae ymsellepsl ltgeggyylt slsaslalls glgqahtlpl
      601 spvqelrrsl slweqrrlpa thcfqhllrv ayqdpssgct sktlavppea siatlnqlca
      661 tkfrvtqpnt fglflykeqg yhrlppgala hrlpttgylv yrraewpetq gavteeegsg
      721 qsearsrgee qgcqgdgdag vkasprdire qsettaeggq gqaqegpaqp gepeaegsra
      781 aee
//
LOCUS       NP_005617                494 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine-rich splicing factor 4 [Homo sapiens].
ACCESSION   NP_005617
VERSION     NP_005617.2
DBSOURCE    REFSEQ: accession NM_005626.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 494)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 494)
  AUTHORS   Miano,M., Bertola,N., Grossi,A., Dell'Orso,G., Regis,S.,
            Rusmini,M., Uva,P., Vozzi,D., Fioredda,F., Palmisani,E., Lupia,M.,
            Lanciotti,M., Grilli,F., Corsolini,F., Arcuri,L., Giarratana,M.C.,
            Ceccherini,I., Dufour,C., Cappelli,E. and Ravera,S.
  TITLE     Impaired Mitochondrial Function and Marrow Failure in Patients
            Carrying a Variant of the SRSF4 Gene
  JOURNAL   Int J Mol Sci 25 (4), 2083 (2024)
   PUBMED   38396760
  REMARK    GeneRIF: Impaired Mitochondrial Function and Marrow Failure in
            Patients Carrying a Variant of the SRSF4 Gene.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 494)
  AUTHORS   Sun,Y., Liu,X., Wu,Z., Wang,X., Zhang,Y., Yan,W. and You,Y.
  TITLE     SRSF4 Confers Temozolomide Resistance of Glioma via Accelerating
            Double Strand Break Repair
  JOURNAL   J Mol Neurosci 73 (4-5), 259-268 (2023)
   PUBMED   37014544
  REMARK    GeneRIF: SRSF4 Confers Temozolomide Resistance of Glioma via
            Accelerating Double Strand Break Repair.
REFERENCE   4  (residues 1 to 494)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 494)
  AUTHORS   Manley,J.L. and Krainer,A.R.
  TITLE     A rational nomenclature for serine/arginine-rich protein splicing
            factors (SR proteins)
  JOURNAL   Genes Dev 24 (11), 1073-1074 (2010)
   PUBMED   20516191
REFERENCE   6  (residues 1 to 494)
  AUTHORS   Lareau,L.F., Inada,M., Green,R.E., Wengrod,J.C. and Brenner,S.E.
  TITLE     Unproductive splicing of SR genes associated with highly conserved
            and ultraconserved DNA elements
  JOURNAL   Nature 446 (7138), 926-929 (2007)
   PUBMED   17361132
REFERENCE   7  (residues 1 to 494)
  AUTHORS   Zimowska,G., Shi,J., Munguba,G., Jackson,M.R., Alpatov,R.,
            Simmons,M.N., Shi,Y. and Sugrue,S.P.
  TITLE     Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal
            epithelial cells
  JOURNAL   Invest Ophthalmol Vis Sci 44 (11), 4715-4723 (2003)
   PUBMED   14578391
REFERENCE   8  (residues 1 to 494)
  AUTHORS   Ramchatesingh,J., Zahler,A.M., Neugebauer,K.M., Roth,M.B. and
            Cooper,T.A.
  TITLE     A subset of SR proteins activates splicing of the cardiac troponin
            T alternative exon by direct interactions with an exonic enhancer
  JOURNAL   Mol Cell Biol 15 (9), 4898-4907 (1995)
   PUBMED   7651409
REFERENCE   9  (residues 1 to 494)
  AUTHORS   Zahler,A.M., Neugebauer,K.M., Stolk,J.A. and Roth,M.B.
  TITLE     Human SR proteins and isolation of a cDNA encoding SRp75
  JOURNAL   Mol Cell Biol 13 (7), 4023-4028 (1993)
   PUBMED   8321209
REFERENCE   10 (residues 1 to 494)
  AUTHORS   Zahler,A.M., Lane,W.S., Stolk,J.A. and Roth,M.B.
  TITLE     SR proteins: a conserved family of pre-mRNA splicing factors
  JOURNAL   Genes Dev 6 (5), 837-847 (1992)
   PUBMED   1577277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL590729.14, BC002781.2 and
            CV814357.1.
            
            On Jun 10, 2002 this sequence version replaced NP_005617.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.805643.1,
                                           SRR1660803.180030.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2153307
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000373795.7/ ENSP00000362900.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..494
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p35.3"
     Protein         1..494
                     /product="serine/arginine-rich splicing factor 4"
                     /note="SR splicing factor 4; splicing factor,
                     arginine/serine-rich 4; SRP001LB; pre-mRNA-splicing factor
                     SRP75"
                     /calculated_mol_wt=56547
     Region          1..87
                     /region_name="RRM1_SRSF4"
                     /note="RNA recognition motif 1 (RRM1) found in vertebrate
                     serine/arginine-rich splicing factor 4 (SRSF4); cd12594"
                     /db_xref="CDD:410007"
     Region          72..95
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08170.2)"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            84
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Region          104..175
                     /region_name="RRM2_SRSF4_like"
                     /note="RNA recognition motif 2 (RRM2) found in
                     serine/arginine-rich splicing factor 4 (SRSF4) and similar
                     proteins; cd12600"
                     /db_xref="CDD:410012"
     Region          169..494
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q08170.2)"
     Site            288
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            290
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            431
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            446
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            456
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q08170.2)"
     CDS             1..494
                     /gene="SRSF4"
                     /gene_synonym="SFRS4; SRP75"
                     /coded_by="NM_005626.5:149..1633"
                     /db_xref="CCDS:CCDS333.1"
                     /db_xref="GeneID:6429"
                     /db_xref="HGNC:HGNC:10786"
                     /db_xref="MIM:601940"
ORIGIN      
        1 mprvyigrls yqarerdver ffkgygkile vdlkngygfv efddlrdadd avyelngkdl
       61 cgerviveha rgprrdgsyg sgrsgygyrr sgrdkygppt rteyrliven lssrcswqdl
      121 kdymrqagev tyadahkgrk negviefvsy sdmkralekl dgtevngrki rlvedkpgsr
      181 rrrsysrsrs hsrsrsrsrh srksrsrsgs sksshsksrs rsrsgsrsrs ksrsrsqsrs
      241 rskkeksrsp skeksrsrsh sagksrsksk dqaeekiqnn dnvgkpksrs psrhksksks
      301 rsrsqerrve eekrgsvsrg rsqekslrqs rsrsrskggs rsrsrsrsks kdkrkgrkrs
      361 reesrsrsrs rsksersrkr gskrdskags skkkkkedtd rsqsrspsrs vskerehaks
      421 essqregrge senagtnqet rsrsrsnsks kpnlpsesrs rsksasktrs rsksrsrsas
      481 rspsrsrsrs hsrs
//
LOCUS       NP_001014763             346 aa            linear   PRI 20-NOV-2025
DEFINITION  electron transfer flavoprotein subunit beta isoform 2 [Homo
            sapiens].
ACCESSION   NP_001014763
VERSION     NP_001014763.1
DBSOURCE    REFSEQ: accession NM_001014763.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 346)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 346)
  AUTHORS   Chen,F., Ni,C., Wang,X., Cheng,R., Pan,C., Wang,Y., Liang,J.,
            Zhang,J., Cheng,J., Chin,Y.E., Zhou,Y., Wang,Z., Guo,Y., Chen,S.,
            Htun,S., Mathes,E.F., de Alba Campomanes,A.G., Slavotinek,A.M.,
            Zhang,S., Li,M. and Yao,Z.
  TITLE     S1P defects cause a new entity of cataract, alopecia, oral mucosal
            disorder, and psoriasis-like syndrome
  JOURNAL   EMBO Mol Med 14 (5), e14904 (2022)
   PUBMED   35362222
REFERENCE   3  (residues 1 to 346)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 346)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 346)
  AUTHORS   Husen,P., Nielsen,C., Martino,C.F. and Solov'yov,I.A.
  TITLE     Molecular Oxygen Binding in the Mitochondrial Electron Transfer
            Flavoprotein
  JOURNAL   J Chem Inf Model 59 (11), 4868-4879 (2019)
   PUBMED   31665600
  REMARK    GeneRIF: Molecular Oxygen Binding in the Mitochondrial Electron
            Transfer Flavoprotein.
REFERENCE   6  (residues 1 to 346)
  AUTHORS   Colombo,I., Finocchiaro,G., Garavaglia,B., Garbuglio,N.,
            Yamaguchi,S., Frerman,F.E., Berra,B. and DiDonato,S.
  TITLE     Mutations and polymorphisms of the gene encoding the beta-subunit
            of the electron transfer flavoprotein in three patients with
            glutaric acidemia type II
  JOURNAL   Hum Mol Genet 3 (3), 429-435 (1994)
   PUBMED   7912128
REFERENCE   7  (residues 1 to 346)
  AUTHORS   Antonacci,R., Colombo,I., Archidiacono,N., Volta,M., DiDonato,S.,
            Finocchiaro,G. and Rocchi,M.
  TITLE     Assignment of the gene encoding the beta-subunit of the
            electron-transfer flavoprotein (ETFB) to human chromosome 19q13.3
  JOURNAL   Genomics 19 (1), 177-179 (1994)
   PUBMED   8188225
REFERENCE   8  (residues 1 to 346)
  AUTHORS   Finocchiaro,G., Colombo,I., Garavaglia,B., Gellera,C.,
            Valdameri,G., Garbuglio,N. and Didonato,S.
  TITLE     cDNA cloning and mitochondrial import of the beta-subunit of the
            human electron-transfer flavoprotein
  JOURNAL   Eur J Biochem 213 (3), 1003-1008 (1993)
   PUBMED   8504797
REFERENCE   9  (residues 1 to 346)
  AUTHORS   Prasun,P.
  TITLE     Multiple Acyl-CoA Dehydrogenase Deficiency
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   32550677
REFERENCE   10 (residues 1 to 346)
  AUTHORS   Royal,V., Alberts,M.J., Pericak-Vance,M.A., Finocchiaro,G.,
            Bebout,J., Yamaoka,L., Hung,W.Y., Gaskell,P.C. and Roses,A.D.
  TITLE     RsaI RFLP for electron transport flavoprotein-beta(ETFB)
  JOURNAL   Nucleic Acids Res 19 (14), 4021 (1991)
   PUBMED   1677763
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK055285.1, AF370381.1 and
            BG281641.1.
            
            Summary: This gene encodes electron-transfer-flavoprotein, beta
            polypeptide, which shuttles electrons between primary flavoprotein
            dehydrogenases involved in mitochondrial fatty acid and amino acid
            catabolism and the membrane-bound electron transfer flavoprotein
            ubiquinone oxidoreductase. The gene deficiencies have been
            implicated in type II glutaricaciduria. Alternatively spliced
            transcript variants have been found for this gene. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (2) lacks the 5' exon but has an
            alternate 5' segment, as compared to variant 1. The encoded isoform
            (2) has a longer and distinct N-terminus compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1163655.571283.1, AK055285.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1970526
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..346
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.41"
     Protein         1..346
                     /product="electron transfer flavoprotein subunit beta
                     isoform 2"
                     /note="electron transfer flavoprotein, beta polypeptide;
                     electron-transferring-flavoprotein, beta polypeptide;
                     beta-ETF; electron transfer flavoprotein beta subunit"
                     /calculated_mol_wt=37303
     Region          108..346
                     /region_name="FixA"
                     /note="Electron transfer flavoprotein, alpha and beta
                     subunits [Energy production and conversion]; COG2086"
                     /db_xref="CDD:441689"
     CDS             1..346
                     /gene="ETFB"
                     /gene_synonym="FP585; MADD"
                     /coded_by="NM_001014763.1:205..1245"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS33085.1"
                     /db_xref="GeneID:2109"
                     /db_xref="HGNC:HGNC:3482"
                     /db_xref="MIM:130410"
ORIGIN      
        1 mylslwvtin tvnlrntlsg lrgavttvgm iksdvpgtqe wlderrrqgd lplptnsnpv
       61 lslelcdpgq gpapfqavvv liqpgrglal rpppsclfpp dptpsppagq irvkpdrtgv
      121 vtdgvkhsmn pfceiaveea vrlkekklvk eviavscgpa qcqetirtal amgadrgihv
      181 evppaeaerl gplqvarvla klaekekvdl vllgkqaidd dcnqtgqmta gfldwpqgtf
      241 asqvtlegdk lkvereidgg letlrlklpa vvtadlrlne pryatlpnim kakkkkievi
      301 kpgdlgvdlt sklsvisved ppqrtagvkv ettedlvakl keigri
//
LOCUS       NP_001138467             419 aa            linear   PRI 20-NOV-2025
DEFINITION  coiled-coil domain-containing protein 85C [Homo sapiens].
ACCESSION   NP_001138467 XP_001723962 XP_001724885 XP_001726496
VERSION     NP_001138467.1
DBSOURCE    REFSEQ: accession NM_001144995.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 419)
  AUTHORS   Han,Y.W., Xu,S.X., Zhang,J., Li,Y.F., Xu,P., Lee,S.C. and Zhao,J.Z.
  TITLE     Cadmium promotes the binding and centrosomal translocation of
            CCDC85C and PLK4 via ROS-GCLM pathway to trigger centrosome
            amplification in colon cancer cells
  JOURNAL   Toxicol Lett 392, 84-93 (2024)
   PUBMED   38185225
REFERENCE   2  (residues 1 to 419)
  AUTHORS   Yadav,L., Tamene,F., Goos,H., van Drogen,A., Katainen,R.,
            Aebersold,R., Gstaiger,M. and Varjosalo,M.
  TITLE     Systematic Analysis of Human Protein Phosphatase Interactions and
            Dynamics
  JOURNAL   Cell Syst 4 (4), 430-444 (2017)
   PUBMED   28330616
REFERENCE   3  (residues 1 to 419)
  AUTHORS   St-Denis,N., Gupta,G.D., Lin,Z.Y., Gonzalez-Badillo,B., Veri,A.O.,
            Knight,J.D.R., Rajendran,D., Couzens,A.L., Currie,K.W., Tkach,J.M.,
            Cheung,S.W.T., Pelletier,L. and Gingras,A.C.
  TITLE     Phenotypic and Interaction Profiling of the Human Phosphatases
            Identifies Diverse Mitotic Regulators
  JOURNAL   Cell Rep 17 (9), 2488-2501 (2016)
   PUBMED   27880917
REFERENCE   4  (residues 1 to 419)
  AUTHORS   Boldt,K., van Reeuwijk,J., Lu,Q., Koutroumpas,K., Nguyen,T.M.,
            Texier,Y., van Beersum,S.E., Horn,N., Willer,J.R., Mans,D.A.,
            Dougherty,G., Lamers,I.J., Coene,K.L., Arts,H.H., Betts,M.J.,
            Beyer,T., Bolat,E., Gloeckner,C.J., Haidari,K., Hetterschijt,L.,
            Iaconis,D., Jenkins,D., Klose,F., Knapp,B., Latour,B.,
            Letteboer,S.J., Marcelis,C.L., Mitic,D., Morleo,M., Oud,M.M.,
            Riemersma,M., Rix,S., Terhal,P.A., Toedt,G., van Dam,T.J., de
            Vrieze,E., Wissinger,Y., Wu,K.M., Apic,G., Beales,P.L.,
            Blacque,O.E., Gibson,T.J., Huynen,M.A., Katsanis,N., Kremer,H.,
            Omran,H., van Wijk,E., Wolfrum,U., Kepes,F., Davis,E.E., Franco,B.,
            Giles,R.H., Ueffing,M., Russell,R.B. and Roepman,R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 419)
  AUTHORS   Tanaka,N., Izawa,T., Takenaka,S., Yamate,J. and Kuwamura,M.
  TITLE     Ccdc85C, a causative protein for hydrocephalus and subcortical
            heterotopia, is expressed in the systemic epithelia with
            proliferative activity in rats
  JOURNAL   Histol Histopathol 30 (7), 823-832 (2015)
   PUBMED   25644709
REFERENCE   6  (residues 1 to 419)
  AUTHORS   Wang,X., Lopez,O., Sweet,R.A., Becker,J.T., DeKosky,S.T.,
            Barmada,M.M., Feingold,E., Demirci,F.Y. and Kamboh,M.I.
  TITLE     Genetic Determinants of Survival in Patientswith Alzheimer's
            Disease
  JOURNAL   J Alzheimers Dis 45 (2), 651-658 (2015)
   PUBMED   25649651
  REMARK    GeneRIF: Genome-wide SNP analysis identified multiple suggestive
            novel loci and two of them were also significant in gene-based
            analysis (CCDC85C and NARS2) that survived after controlling for
            false-discovery rate at 0.05.
REFERENCE   7  (residues 1 to 419)
  AUTHORS   Markham,N.O., Doll,C.A., Dohn,M.R., Miller,R.K., Yu,H.,
            Coffey,R.J., McCrea,P.D., Gamse,J.T. and Reynolds,A.B.
  TITLE     DIPA-family coiled-coils bind conserved isoform-specific head
            domain of p120-catenin family: potential roles in hydrocephalus and
            heterotopia
  JOURNAL   Mol Biol Cell 25 (17), 2592-2603 (2014)
   PUBMED   25009281
REFERENCE   8  (residues 1 to 419)
  AUTHORS   Mori,N., Kuwamura,M., Tanaka,N., Hirano,R., Nabe,M., Ibuki,M. and
            Yamate,J.
  TITLE     Ccdc85c encoding a protein at apical junctions of radial glia is
            disrupted in hemorrhagic hydrocephalus (hhy) mice
  JOURNAL   Am J Pathol 180 (1), 314-327 (2012)
   PUBMED   22056358
REFERENCE   9  (residues 1 to 419)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL160313.4 and AL110504.6.
            
            On or before Feb 19, 2009 this sequence version replaced
            XP_001724885.1, XP_001723962.1, XP_001726496.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.496694.1, BQ918944.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142670
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000380243.9/ ENSP00000369592.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..419
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.2"
     Protein         1..419
                     /product="coiled-coil domain-containing protein 85C"
                     /calculated_mol_wt=45079
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (A6NKD9.1)"
     Region          12..202
                     /region_name="CCDC85"
                     /note="CCDC85 family; pfam10226"
                     /db_xref="CDD:463009"
     Region          162..268
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NKD9.1)"
     Site            178
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (A6NKD9.1)"
     Site            246
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (A6NKD9.1)"
     Region          307..348
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (A6NKD9.1)"
     CDS             1..419
                     /gene="CCDC85C"
                     /coded_by="NM_001144995.2:249..1508"
                     /db_xref="CCDS:CCDS45161.1"
                     /db_xref="GeneID:317762"
                     /db_xref="HGNC:HGNC:35459"
                     /db_xref="MIM:621283"
ORIGIN      
        1 makpaataaa aseelsqvpd eellrwskee larrlrraeg ekvglmlehg glmrdvnrrl
       61 qqhlleirgl kdvnqrlqdd nqelrelccf ldddrqkgrk larewqrfgr haagavwhev
      121 arsqqklrel earqeallre nlelkelvll ldeeraalaa tgaasggggg gggagsrssi
      181 dsqaslsgpl sggapgagar dvgdgsstss agsggspdhh hhvpppllpp gphkapdgka
      241 gatrrslddl sapphhrsip nglhdpssty irqleskvrl legdkllaqq agsgefrtlr
      301 kgfspyhses qlaslppsyq dslqngpacp apelpsppsa gyspagqkpe avvhamkvle
      361 vhenldrqlq dsceedlsek ekaivremcn vvwrklgdaa sskpsirqhl sgnqfkgpl
//
LOCUS       NP_001075019            1593 aa            linear   PRI 20-NOV-2025
DEFINITION  THO complex subunit 2 isoform 1 [Homo sapiens].
ACCESSION   NP_001075019
VERSION     NP_001075019.1
DBSOURCE    REFSEQ: accession NM_001081550.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1593)
  AUTHORS   Puhringer,T., Hohmann,U., Fin,L., Pacheco-Fiallos,B.,
            Schellhaas,U., Brennecke,J. and Plaschka,C.
  TITLE     Structure of the human core transcription-export complex reveals a
            hub for multivalent interactions
  JOURNAL   Elife 9, e61503 (2020)
   PUBMED   33191911
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1593)
  AUTHORS   Zhou,X., Liu,X., Zhang,G., Zhang,Q., Chen,H., Wang,Y., Fang,F. and
            Sun,J.
  TITLE     Knockdown THOC2 suppresses the proliferation and invasion of
            melanoma
  JOURNAL   Bioengineered 10 (1), 635-645 (2019)
   PUBMED   31680623
  REMARK    GeneRIF: THOC2 reduction repressed melanoma cell proliferation and
            invasion, and induced cell apoptosis.
REFERENCE   3  (residues 1 to 1593)
  AUTHORS   Kumar,R., Gardner,A., Homan,C.C., Douglas,E., Mefford,H.,
            Wieczorek,D., Ludecke,H.J., Stark,Z., Sadedin,S., Nowak,C.B.,
            Douglas,J., Parsons,G., Mark,P., Loidi,L., Herman,G.E., Mihalic
            Mosher,T., Gillespie,M.K., Brady,L., Tarnopolsky,M., Madrigal,I.,
            Eiris,J., Domenech Salgado,L., Rabionet,R., Strom,T.M.,
            Ishihara,N., Inagaki,H., Kurahashi,H., Dudding-Byth,T.,
            Palmer,E.E., Field,M. and Gecz,J.
  CONSRTM   Broad CMG
  TITLE     Severe neurocognitive and growth disorders due to variation in
            THOC2, an essential component of nuclear mRNA export machinery
  JOURNAL   Hum Mutat 39 (8), 1126-1138 (2018)
   PUBMED   29851191
  REMARK    GeneRIF: Study presents detailed clinical assessment and functional
            studies on a de novo variant in a female with an epileptic
            encephalopathy and discuss an additional four families with rare
            variants in THOC2 with supportive evidence for pathogenicity.
REFERENCE   4  (residues 1 to 1593)
  AUTHORS   Kumar,R., Corbett,M.A., van Bon,B.W., Woenig,J.A., Weir,L.,
            Douglas,E., Friend,K.L., Gardner,A., Shaw,M., Jolly,L.A., Tan,C.,
            Hunter,M.F., Hackett,A., Field,M., Palmer,E.E., Leffler,M.,
            Rogers,C., Boyle,J., Bienek,M., Jensen,C., Van Buggenhout,G., Van
            Esch,H., Hoffmann,K., Raynaud,M., Zhao,H., Reed,R., Hu,H.,
            Haas,S.A., Haan,E., Kalscheuer,V.M. and Gecz,J.
  TITLE     THOC2 Mutations Implicate mRNA-Export Pathway in X-Linked
            Intellectual Disability
  JOURNAL   Am J Hum Genet 97 (2), 302-310 (2015)
   PUBMED   26166480
  REMARK    GeneRIF: THOC2 mutations implicate mRNA-export pathway in X-linked
            intellectual disability.
REFERENCE   5  (residues 1 to 1593)
  AUTHORS   Grolimund,L., Aeby,E., Hamelin,R., Armand,F., Chiappe,D.,
            Moniatte,M. and Lingner,J.
  TITLE     A quantitative telomeric chromatin isolation protocol identifies
            different telomeric states
  JOURNAL   Nat Commun 4, 2848 (2013)
   PUBMED   24270157
REFERENCE   6  (residues 1 to 1593)
  AUTHORS   Beausoleil,S.A., Jedrychowski,M., Schwartz,D., Elias,J.E.,
            Villen,J., Li,J., Cohn,M.A., Cantley,L.C. and Gygi,S.P.
  TITLE     Large-scale characterization of HeLa cell nuclear phosphoproteins
  JOURNAL   Proc Natl Acad Sci U S A 101 (33), 12130-12135 (2004)
   PUBMED   15302935
REFERENCE   7  (residues 1 to 1593)
  AUTHORS   Strasser,K., Masuda,S., Mason,P., Pfannstiel,J., Oppizzi,M.,
            Rodriguez-Navarro,S., Rondon,A.G., Aguilera,A., Struhl,K., Reed,R.
            and Hurt,E.
  TITLE     TREX is a conserved complex coupling transcription with messenger
            RNA export
  JOURNAL   Nature 417 (6886), 304-308 (2002)
   PUBMED   11979277
REFERENCE   8  (residues 1 to 1593)
  AUTHORS   Coffey,A.J., Brooksbank,R.A., Brandau,O., Oohashi,T., Howell,G.R.,
            Bye,J.M., Cahn,A.P., Durham,J., Heath,P., Wray,P., Pavitt,R.,
            Wilkinson,J., Leversha,M., Huckle,E., Shaw-Smith,C.J., Dunham,A.,
            Rhodes,S., Schuster,V., Porta,G., Yin,L., Serafini,P., Sylla,B.,
            Zollo,M., Franco,B., Bolino,A., Seri,M., Lanyi,A., Davis,J.R.,
            Webster,D., Harris,A., Lenoir,G., de St Basile,G., Jones,A.,
            Behloradsky,B.H., Achatz,H., Murken,J., Fassler,R., Sumegi,J.,
            Romeo,G., Vaudin,M., Ross,M.T., Meindl,A. and Bentley,D.R.
  TITLE     Host response to EBV infection in X-linked lymphoproliferative
            disease results from mutations in an SH2-domain encoding gene
  JOURNAL   Nat Genet 20 (2), 129-135 (1998)
   PUBMED   9771704
REFERENCE   9  (residues 1 to 1593)
  AUTHORS   Gu,X.X., Decorte,R., Marynen,P., Fryns,J.P., Cassiman,J.J. and
            Raeymaekers,P.
  TITLE     Localisation of a new gene for non-specific mental retardation to
            Xq22-q26 (MRX35)
  JOURNAL   J Med Genet 33 (1), 52-55 (1996)
   PUBMED   8825049
REFERENCE   10 (residues 1 to 1593)
  AUTHORS   Mulley,J.C., Kerr,B., Stevenson,R. and Lubs,H.
  TITLE     Nomenclature guidelines for X-linked mental retardation
  JOURNAL   Am J Med Genet 43 (1-2), 383-391 (1992)
   PUBMED   1605216
  REMARK    Review article
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA504931.1, AW206982.1,
            AF441770.1 and BC054050.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The TREX multiprotein complex binds specifically to
            spliced mRNAs to facilitate mRNA export. The protein encoded by
            this gene is a member of the THO complex, a subset of the TREX
            complex. The encoded protein interacts with the THOC1
            protein.[provided by RefSeq, Jun 2010].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038196.3428918.1,
                                           SRR1660807.247482.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000245838.13/ ENSP00000245838.8
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1593
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq25"
     Protein         1..1593
                     /product="THO complex subunit 2 isoform 1"
                     /note="THO complex 2"
                     /calculated_mol_wt=182644
     Region          1..163
                     /region_name="Anchor domain, interaction with THOC5 and
                     THOC7. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          11..566
                     /region_name="THOC2_N"
                     /note="THO complex subunit 2 N-terminus; pfam16134"
                     /db_xref="CDD:465032"
     Region          164..534
                     /region_name="Bow domain, interaction with THOC1 dock
                     domain and THOC3. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          322..341
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          535..686
                     /region_name="MIF4G domain, interaction with THOC3 and
                     DDX39B. /evidence=ECO:0000269|PubMed:33191911,
                     ECO:0007744|PDB:7APK"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          568..642
                     /region_name="Thoc2"
                     /note="Transcription- and export-related complex subunit;
                     pfam11732"
                     /db_xref="CDD:463334"
     Region          687..1174
                     /region_name="Stern domain.
                     /evidence=ECO:0000269|PubMed:33191911"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          874..1173
                     /region_name="Tho2"
                     /note="Transcription factor/nuclear export subunit protein
                     2; pfam11262"
                     /db_xref="CDD:463251"
     Region          923..928
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1175..1593
                     /region_name="Charged domain.
                     /evidence=ECO:0000269|PubMed:33191911"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1184..1593
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1222
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:B1AZI6; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          <1291..1593
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Site            1385
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1390
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1393
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1417
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1443
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Region          1448..>1556
                     /region_name="U2AF_lg"
                     /note="U2 snRNP auxilliary factor, large subunit, splicing
                     factor; TIGR01642"
                     /db_xref="CDD:273727"
     Site            1450
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1486
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     Site            1516
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q8NI27.2)"
     CDS             1..1593
                     /gene="THOC2"
                     /gene_synonym="AMC7; CXorf3; dJ506G2.1; hTREX120; MRX12;
                     MRX35; THO2; XLID12"
                     /coded_by="NM_001081550.2:31..4812"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS43988.1"
                     /db_xref="GeneID:57187"
                     /db_xref="HGNC:HGNC:19073"
                     /db_xref="MIM:300395"
ORIGIN      
        1 maaaavvvpa ewiknweksg rgeflhlcri lsenkshdss tyrdfqqaly elsyhvikgn
       61 lkheqasnvl sdisefredm psiladvfci ldietnclee kskrdyftql vlaclylvsd
      121 tvlkerldpe tleslglikq sqqfnqksvk iktklfykqq kfnllreene gyakliaelg
      181 qdlsgsitsd lileniksli gcfnldpnrv ldvilevfec rpehddffis llesymsmce
      241 pqtlchilgf kfkfyqepng etpsslyrva avllqfnlid lddlyvhllp adncimdehk
      301 reiaeakqiv rkltmvvlss ekmderekek ekeeekvekp pdnqklglle allkigdwqh
      361 aqnimdqmpp yyaashklia laicklihit ieplyrrvgv pkgakgspvn alqnkrapkq
      421 aesfedlrrd vfnmfcylgp hlshdpilfa kvvrigksfm kefqsdgskq edkektevil
      481 scllsitdqv llpslslmdc nacmseelwg mfktfpyqhr yrlygqwkne tynshpllvk
      541 vkaqtidrak yimkrltken vkpsgrqigk lshsnptilf dyilsqiqky dnlitpvvds
      601 lkyltslnyd vlayciieal anpekermkh ddttisswlq slasfcgavf rkypidlagl
      661 lqyvanqlka gksfdllilk evvqkmagie iteemtmeql eamtggeqlk aeggyfgqir
      721 ntkkssqrlk dalldhdlal plcllmaqqr ngvifqegge khlklvgkly dqchdtlvqf
      781 ggflasnlst edyikrvpsi dvlcnefhtp hdaafflsrp myahhissky delkksekgs
      841 kqqhkvhkyi tscemvmapv heavvslhvs kvwddispqf yatfwsltmy dlavphtsye
      901 revnklkvqm kaiddnqemp pnkkkkeker ctalqdklle eekkqmehvq rvlqrlklek
      961 dnwllakstk netitkflql cifprcifsa idavycarfv elvhqqktpn fstllcydrv
     1021 fsdiiytvas cteneasryg rflccmletv trwhsdraty ekecgnypgf ltilratgfd
     1081 ggnkadqldy enfrhvvhkw hykltkasvh cletgeythi rnilivltki lpwypkvlnl
     1141 gqalerrvhk icqeekekrp dlyalamgys gqlksrksym ipenefhhkd ppprnavasv
     1201 qngpgggpss ssigsasksd essteetdks rersqcgvka vnkassttpk gnssngnsgs
     1261 nsnkavkend kekgkekeke kkektpattp earvlgkdgk ekpkeerpnk dekaretker
     1321 tpksdkekek fkkeekakde kfkttvpnae skstqerere kepsrerdia kemkskenvk
     1381 ggektpvsgs lkspvprsdi pepereqkrr kidthpspsh sstvkdslie lkessaklyi
     1441 nhtppplsks keremdkkdl dksrersrer ekkdekdrke rkrdhsnndr evppdltkrr
     1501 keengtmgvs khksespces pypnekdkek nkskssgkek gsdsfksekm dkissggkke
     1561 srhdkekiek kekrdssggk eekkhhkssd khr
//
LOCUS       NP_001339872             684 aa            linear   PRI 20-NOV-2025
DEFINITION  DNA repair-scaffolding protein isoform 15 [Homo sapiens].
ACCESSION   NP_001339872 XP_016868771
VERSION     NP_001339872.1
DBSOURCE    REFSEQ: accession NM_001352943.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Heddar,A., Guichoux,N., Auger,N. and Misrahi,M.
  TITLE     A SPIDR homozygous nonsense pathogenic variant in isolated primary
            ovarian insufficiency with chromosomal instability
  JOURNAL   Clin Genet 101 (2), 242-246 (2022)
   PUBMED   34697795
  REMARK    GeneRIF: A SPIDR homozygous nonsense pathogenic variant in isolated
            primary ovarian insufficiency with chromosomal instability.
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Rein,H.L., Bernstein,K.A. and Baldock,R.A.
  TITLE     RAD51 paralog function in replicative DNA damage and tolerance
  JOURNAL   Curr Opin Genet Dev 71, 86-91 (2021)
   PUBMED   34311385
  REMARK    Review article
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Martino,J., Brunette,G.J., Barroso-Gonzalez,J., Moiseeva,T.N.,
            Smith,C.M., Bakkenist,C.J., O'Sullivan,R.J. and Bernstein,K.A.
  TITLE     The human Shu complex functions with PDS5B and SPIDR to promote
            homologous recombination
  JOURNAL   Nucleic Acids Res 47 (19), 10151-10165 (2019)
   PUBMED   31665741
  REMARK    GeneRIF: our study uncovers a protein complex, which consists of
            SWS1, SWSAP1, SPIDR and PDS5B, involved in DNA repair and provides
            insight into Shu complex function and composition.
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Wan,L., Han,J., Liu,T., Dong,S., Xie,F., Chen,H. and Huang,J.
  TITLE     Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome
            helicase with homologous recombination repair
  JOURNAL   Proc Natl Acad Sci U S A 110 (26), 10646-10651 (2013)
   PUBMED   23509288
  REMARK    GeneRIF: Consistent with its role as a scaffolding protein for the
            assembly of BLM and RAD51 foci, cells depleted of SPIDR show
            increased rate of sister chromatid exchange and defects in
            homologous recombination repair.
REFERENCE   7  (residues 1 to 684)
  AUTHORS   Fox,C.S., Liu,Y., White,C.C., Feitosa,M., Smith,A.V.,
            Heard-Costa,N., Lohman,K., Johnson,A.D., Foster,M.C.,
            Greenawalt,D.M., Griffin,P., Ding,J., Newman,A.B., Tylavsky,F.,
            Miljkovic,I., Kritchevsky,S.B., Launer,L., Garcia,M.,
            Eiriksdottir,G., Carr,J.J., Gudnason,V., Harris,T.B., Cupples,L.A.
            and Borecki,I.B.
  CONSRTM   GIANT Consortium; MAGIC Consortium; GLGC Consortium
  TITLE     Genome-wide association for abdominal subcutaneous and visceral
            adipose reveals a novel locus for visceral fat in women
  JOURNAL   PLoS Genet 8 (5), e1002695 (2012)
   PUBMED   22589738
REFERENCE   8  (residues 1 to 684)
  AUTHORS   Liu,T., Wan,L., Wu,Y., Chen,J. and Huang,J.
  TITLE     hSWS1.SWSAP1 is an evolutionarily conserved complex required for
            efficient homologous recombination repair
  JOURNAL   J Biol Chem 286 (48), 41758-41766 (2011)
   PUBMED   21965664
REFERENCE   9  (residues 1 to 684)
  AUTHORS   Tang,B.S., Chan,K.H., Cheng,V.C., Woo,P.C., Lau,S.K., Lam,C.C.,
            Chan,T.L., Wu,A.K., Hung,I.F., Leung,S.Y. and Yuen,K.Y.
  TITLE     Comparative host gene transcription by microarray analysis early
            after infection of the Huh7 cell line by severe acute respiratory
            syndrome coronavirus and human coronavirus 229E
  JOURNAL   J Virol 79 (10), 6180-6193 (2005)
   PUBMED   15858003
REFERENCE   10 (residues 1 to 684)
  AUTHORS   Lee,Y.W., Eum,S.Y., Chen,K.C., Hennig,B. and Toborek,M.
  TITLE     Gene expression profile in interleukin-4-stimulated human vascular
            endothelial cells
  JOURNAL   Mol Med 10 (1-6), 19-27 (2004)
   PUBMED   15502879
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC233269.2, AC145060.2, AC024649.10, AC024451.8 and AC023991.9.
            
            On Jun 24, 2017 this sequence version replaced XP_016868771.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR14038192.1020341.1,
                                           SRR14038197.7997.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8q11.21"
     Protein         1..684
                     /product="DNA repair-scaffolding protein isoform 15"
                     /note="DNA repair-scaffolding protein; scaffolding protein
                     involved in DNA repair"
                     /calculated_mol_wt=75813
     Region          <11..205
                     /region_name="DUF4502"
                     /note="Domain of unknown function (DUF4502); pfam14950"
                     /db_xref="CDD:464396"
     Region          357..>616
                     /region_name="DUF4503"
                     /note="Domain of unknown function (DUF4503); pfam14951"
                     /db_xref="CDD:464397"
     CDS             1..684
                     /gene="SPIDR"
                     /gene_synonym="KIAA0146; ODG9"
                     /coded_by="NM_001352943.1:410..2464"
                     /note="isoform 15 is encoded by transcript variant 18"
                     /db_xref="GeneID:23514"
                     /db_xref="HGNC:HGNC:28971"
                     /db_xref="MIM:615384"
ORIGIN      
        1 mkirhflsyr epssieiley ssdsekeddl envllidses phkyhvqfas darqimerli
       61 dprtksteti lhtpqkptak fprtpensak kkllrgglae rlnglqnrer saislwrhqc
      121 isyqktlsgr ksgvltvkil elheecamqv amceqllgsp atsssqsvap rpgaglkvlf
      181 tketagylrg rpqdtvrifp pwqkliipsg scpvilntyf cekvvakeds ektcevycpd
      241 iplprrsisl aqmfvikglt nnspeiqvvc sgvattgtaw thghkeakqr iptstplrds
      301 lldvvesqga aswpgagvrv vvqrvyslps rdstrgqqga ssghtdpagt racllvqdac
      361 gmfgevhlef tmskarqleg kscslvgmkv lqkvtrgrta gifslidtlw ppaiplktpg
      421 rdqpceeikt hlpppalcyi ltahpnlgqi diidedpiyk lyqppvtrcl rdilqmndlg
      481 trcsfyatvi yqkpqlksll lleqreiwll vtdvtlqtke erdprlpktl lvyvaplcvl
      541 gsevlealag aaphslffkd alrdqgrivc aertvlllqk pllsvvsgas scelpgpvml
      601 dsldsatpvn sicsvqelrs eecprkgsgv vklfcpvrnr ppdqlhwigg nrasecrrgl
      661 crtlavaags vnfamwlqgw wwww
//
LOCUS       NP_001350371             684 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 18 isoform 4 [Homo sapiens].
ACCESSION   NP_001350371 XP_011513834
VERSION     NP_001350371.1
DBSOURCE    REFSEQ: accession NM_001363442.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 684)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   2  (residues 1 to 684)
  AUTHORS   Ding,X., Barodia,S.K., Ma,L. and Goldberg,M.S.
  TITLE     Fbxl18 targets LRRK2 for proteasomal degradation and attenuates
            cell toxicity
  JOURNAL   Neurobiol Dis 98, 122-136 (2017)
   PUBMED   27890708
  REMARK    GeneRIF: Study showed that LRRK2 phosphorylation is required for
            LRRK2 to bind to Fbxl18, and that this interaction is important for
            regulating the amount of LRRK2 via ubiquitination of LRRK2 by the
            SCFFbxl18 ubiquitin ligase and subsequent proteasomal degradation
            of LRRK2. We also show that LRRK2 can induce caspase 8 mediated
            cell death and that the degradation of LRRK2 mediated by Fbxl18 can
            prevent LRRK2-mediated toxicity.
REFERENCE   3  (residues 1 to 684)
  AUTHORS   Zhang,J., Yang,Z., Ou,J., Xia,X., Zhi,F. and Cui,J.
  TITLE     The F-box protein FBXL18 promotes glioma progression by promoting
            K63-linked ubiquitination of Akt
  JOURNAL   FEBS Lett 591 (1), 145-154 (2017)
   PUBMED   27926990
  REMARK    GeneRIF: FBXL18 plays an oncogenic role through promoting lysine
            63-linked ubiquitination of Akt in glioma.
REFERENCE   4  (residues 1 to 684)
  AUTHORS   Liu,Y., Lear,T., Zhao,Y., Zhao,J., Zou,C., Chen,B.B. and
            Mallampalli,R.K.
  TITLE     F-box protein Fbxl18 mediates polyubiquitylation and proteasomal
            degradation of the pro-apoptotic SCF subunit Fbxl7
  JOURNAL   Cell Death Dis 6 (2), e1630 (2015)
   PUBMED   25654763
  REMARK    GeneRIF: Fbxl18 regulates apoptosis by mediating
            ubiquitin-dependent proteasomal degradation of the pro-apoptotic
            protein Fbxl7 that may impact cellular processes involved in cell
            cycle progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 684)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   6  (residues 1 to 684)
  AUTHORS   Jin,J., Cardozo,T., Lovering,R.C., Elledge,S.J., Pagano,M. and
            Harper,J.W.
  TITLE     Systematic analysis and nomenclature of mammalian F-box proteins
  JOURNAL   Genes Dev 18 (21), 2573-2580 (2004)
   PUBMED   15520277
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC006483.3 and AC092171.4.
            
            On May 18, 2018 this sequence version replaced XP_011513834.1.
            
            Summary: The protein encoded by this gene is a member of a family
            of proteins that contain an approximately 40-amino acid F-box
            motif. This motif is important for interaction with SKP1 and for
            targeting some proteins for degradation. The encoded protein has
            been shown to control the cellular level of FBXL7, a protein that
            induces mitotic arrest, by targeting it for polyubiquitylation and
            proteasomal degradation. Members of the F-box protein family, such
            as FBXL18, are characterized by an approximately 40-amino acid
            F-box motif. F-box proteins interact with SKP1 through the F box,
            and they interact with ubiquitination targets through other protein
            interaction domains. [provided by RefSeq, Mar 2016].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DRR138522.217727.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA2155628
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..684
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.1"
     Protein         1..684
                     /product="F-box/LRR-repeat protein 18 isoform 4"
                     /note="F-box/LRR-repeat protein 18"
                     /calculated_mol_wt=74670
     Region          28..71
                     /region_name="F-box_FBXL18"
                     /note="F-box domain found in F-box/LRR-repeat protein 18
                     (FBXL18) and similar proteins; cd22128"
                     /db_xref="CDD:438900"
     Site            order(31,35,38..39,42..43,47,49..50,55..57,59)
                     /site_type="other"
                     /note="putative Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438900"
     Region          85..667
                     /region_name="FBXL18_LRR"
                     /note="F-box/LRR-repeat protein 18, LRR; pfam19729"
                     /db_xref="CDD:466163"
     Region          345..384
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          385..414
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          415..484
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          451..477
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          485..532
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          533..559
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          560..589
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          590..615
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          616..640
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..684
                     /gene="FBXL18"
                     /gene_synonym="Fbl18"
                     /coded_by="NM_001363442.2:136..2190"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:80028"
                     /db_xref="HGNC:HGNC:21874"
                     /db_xref="MIM:609084"
ORIGIN      
        1 massgedisn ddddmhpaaa gmadgvhllg fsdeillhil shvpstdlil nvrrtcrkla
       61 alcldkslih tvllqkdyqa sedkvrqlvk eigreiqqls magcywlpgs tvehvarcrs
      121 lvkvnlsgch ltslrlskml salqhlrsla idvspgfdas qlsseckatl srvrelkqtl
      181 ftpsygvvpc ctslekllly feildrtreg ailsgqlmvg qsnvphyqnl rvfyarlapg
      241 yinqevvrly lavlsdrtpq nlhaflisvp gsfaesgatk nlldsmarnv vldalqlpks
      301 wlngssllqh mkfnnpfyfs fsrctlsggh liqqvinggk dlrslaslnl sgcvhclspd
      361 sllrkaeddi dssiletlva sccnlrhlnl saahhhsseg lgrhlcqlla rlrhlrslsl
      421 pvcsvadsap radrapaqpa mhavprgfgk kvrvgvqscp spfsgqacpq pssvfwsllk
      481 nlpflehlel igsnfssamp rnepairnsl ppcsraqsvg dsevaaigql aflrhltlaq
      541 lpsvltgsgl vniglqcqql rslslanlgm mgkvvympal sdmlkhckrl rdlrleqpyf
      601 sanaqffqal sqcpslqrlc lvsrsgtlqp davlafmarc lqvvmchlft geslatcksl
      661 qqsllrrasw slmlcccags qvst
//
LOCUS       NP_001271171             474 aa            linear   PRI 20-NOV-2025
DEFINITION  serine-rich coiled-coil domain-containing protein 2 isoform 4 [Homo
            sapiens].
ACCESSION   NP_001271171 XP_005269966
VERSION     NP_001271171.1
DBSOURCE    REFSEQ: accession NM_001284242.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 474)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 474)
  AUTHORS   Shirai,Y., Okuda,T., Oshima,K. and Nadano,D.
  TITLE     Characterization of human Ccser2 as a protein tracking the
            plus-ends of microtubules
  JOURNAL   BMC Res Notes 16 (1), 198 (2023)
   PUBMED   37684684
  REMARK    GeneRIF: Characterization of human Ccser2 as a protein tracking the
            plus-ends of microtubules.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 474)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 474)
  AUTHORS   Sugis,E., Dauvillier,J., Leontjeva,A., Adler,P., Hindie,V.,
            Moncion,T., Collura,V., Daudin,R., Loe-Mie,Y., Herault,Y.,
            Lambert,J.C., Hermjakob,H., Pupko,T., Rain,J.C., Xenarios,I.,
            Vilo,J., Simonneau,M. and Peterson,H.
  TITLE     HENA, heterogeneous network-based data set for Alzheimer's disease
  JOURNAL   Sci Data 6 (1), 151 (2019)
   PUBMED   31413325
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 474)
  AUTHORS   Camargo,L.M., Collura,V., Rain,J.C., Mizuguchi,K., Hermjakob,H.,
            Kerrien,S., Bonnert,T.P., Whiting,P.J. and Brandon,N.J.
  TITLE     Disrupted in Schizophrenia 1 Interactome: evidence for the close
            connectivity of risk genes and a potential synaptic basis for
            schizophrenia
  JOURNAL   Mol Psychiatry 12 (1), 74-86 (2007)
   PUBMED   17043677
REFERENCE   6  (residues 1 to 474)
  AUTHORS   Grupe,A., Li,Y., Rowland,C., Nowotny,P., Hinrichs,A.L., Smemo,S.,
            Kauwe,J.S., Maxwell,T.J., Cherny,S., Doil,L., Tacey,K., van
            Luchene,R., Myers,A., Wavrant-De Vrieze,F., Kaleem,M.,
            Hollingworth,P., Jehu,L., Foy,C., Archer,N., Hamilton,G.,
            Holmans,P., Morris,C.M., Catanese,J., Sninsky,J., White,T.J.,
            Powell,J., Hardy,J., O'Donovan,M., Lovestone,S., Jones,L.,
            Morris,J.C., Thal,L., Owen,M., Williams,J. and Goate,A.
  TITLE     A scan of chromosome 10 identifies a novel locus showing strong
            association with late-onset Alzheimer disease
  JOURNAL   Am J Hum Genet 78 (1), 78-88 (2006)
   PUBMED   16385451
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC074321.10, BQ440427.1, AK294321.1, AF241785.1, AL356115.9 and
            BQ028021.1.
            
            On Sep 26, 2013 this sequence version replaced XP_005269966.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR, lacks a
            portion of the 5' coding region, and initiates translation at a
            downstream start codon, compared to variant 1. The encoded isoform
            (4) is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ440427.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968189, SAMEA2144120
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..474
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q23.1"
     Protein         1..474
                     /product="serine-rich coiled-coil domain-containing
                     protein 2 isoform 4"
                     /note="protein GCAP14 homolog; protein FAM190B; family
                     with sequence similarity 190, member B; serine-rich
                     coiled-coil domain-containing protein 2"
                     /calculated_mol_wt=53572
     CDS             1..474
                     /gene="CCSER2"
                     /gene_synonym="bA486O22.1; FAM190B; Gcap14; KIAA1128"
                     /coded_by="NM_001284242.2:73..1497"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:54462"
                     /db_xref="HGNC:HGNC:29197"
                     /db_xref="MIM:619944"
ORIGIN      
        1 mnrfdrpdrn vrqpqegfwk rppqrwsgqe hyhlshpdhy hhhgksdlsr gspyresplg
       61 hfesyggmpf fqaqkmfvdv pentvildem tlrhmvqdct avktqllklk rllhqhdgsg
      121 slhdiqlslp sspepedgdk vyknedllne ikqlkdeikk kdekiqllel qlatqhichq
      181 kckeekctya dkytqtpwrr ippqvlqpss slprptdhtq gklikpqrie arsecsiqdm
      241 hqggahpees fthvlhqesn ygleeqpfss gpqltmdvak stpseanlni tvnaqepyhl
      301 annqisdmqf iptslqtppe sstvdqakrv grnqsppvgy msqpkslqll kpsilsslvp
      361 ppvsesspsr tptckkspii ttcnsaklqp tssqtnlann qnlkasklrp psgsfkqkqt
      421 nspqlepqsf qaktsiprpl tqrkeimqnp ngnlhsgdcl asnrysrlpk pkih
//
LOCUS       NP_001032360             814 aa            linear   PRI 20-NOV-2025
DEFINITION  eukaryotic translation initiation factor 3 subunit B isoform 1
            [Homo sapiens].
ACCESSION   NP_001032360
VERSION     NP_001032360.1
DBSOURCE    REFSEQ: accession NM_001037283.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 814)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 814)
  AUTHORS   Khoroshkin,M., Buyan,A., Dodel,M., Navickas,A., Yu,J., Trejo,F.,
            Doty,A., Baratam,R., Zhou,S., Lee,S.B., Joshi,T., Garcia,K.,
            Choi,B., Miglani,S., Subramanyam,V., Modi,H., Carpenter,C.,
            Markett,D., Corces,M.R., Mardakheh,F.K., Kulakovskiy,I.V. and
            Goodarzi,H.
  TITLE     Systematic identification of post-transcriptional regulatory
            modules
  JOURNAL   Nat Commun 15 (1), 7872 (2024)
   PUBMED   39251607
  REMARK    Erratum:[Nat Commun. 2024 Oct 28;15(1):9277. doi:
            10.1038/s41467-024-52903-4. PMID: 39468017]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 814)
  AUTHORS   Huang,R., Nie,W., Mi,L., Yao,C. and Zhu,H.
  TITLE     EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma
  JOURNAL   Aging (Albany NY) 16 (8), 7311-7330 (2024)
   PUBMED   38687509
  REMARK    GeneRIF: EIF3B stabilizes PCNA by counteracting SYVN1-mediated
            ubiquitination to serve as a promotor in cholangiocarcinoma.
REFERENCE   4  (residues 1 to 814)
  AUTHORS   Fang,P., Han,Y., Qu,Y., Wang,X., Zhang,Y., Zhang,W., Zhang,N.,
            Li,G. and Ma,W.
  TITLE     EIF3B stabilizes PTGS2 expression by counteracting MDM2-mediated
            ubiquitination to promote the development and progression of
            malignant melanoma
  JOURNAL   Cancer Sci 113 (12), 4181-4192 (2022)
   PUBMED   36050601
  REMARK    GeneRIF: EIF3B stabilizes PTGS2 expression by counteracting
            MDM2-mediated ubiquitination to promote the development and
            progression of malignant melanoma.
REFERENCE   5  (residues 1 to 814)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   6  (residues 1 to 814)
  AUTHORS   Sizova,D.V., Kolupaeva,V.G., Pestova,T.V., Shatsky,I.N. and
            Hellen,C.U.
  TITLE     Specific interaction of eukaryotic translation initiation factor 3
            with the 5' nontranslated regions of hepatitis C virus and
            classical swine fever virus RNAs
  JOURNAL   J Virol 72 (6), 4775-4782 (1998)
   PUBMED   9573242
REFERENCE   7  (residues 1 to 814)
  AUTHORS   Chaudhuri,J., Chakrabarti,A. and Maitra,U.
  TITLE     Biochemical characterization of mammalian translation initiation
            factor 3 (eIF3). Molecular cloning reveals that p110 subunit is the
            mammalian homologue of Saccharomyces cerevisiae protein Prt1
  JOURNAL   J Biol Chem 272 (49), 30975-30983 (1997)
   PUBMED   9388245
REFERENCE   8  (residues 1 to 814)
  AUTHORS   Methot,N., Rom,E., Olsen,H. and Sonenberg,N.
  TITLE     The human homologue of the yeast Prt1 protein is an integral part
            of the eukaryotic initiation factor 3 complex and interacts with
            p170
  JOURNAL   J Biol Chem 272 (2), 1110-1116 (1997)
   PUBMED   8995410
REFERENCE   9  (residues 1 to 814)
  AUTHORS   Asano,K., Kinzy,T.G., Merrick,W.C. and Hershey,J.W.
  TITLE     Conservation and diversity of eukaryotic translation initiation
            factor eIF3
  JOURNAL   J Biol Chem 272 (2), 1101-1109 (1997)
   PUBMED   8995409
REFERENCE   10 (residues 1 to 814)
  AUTHORS   Kirken,R.A., Rui,H., Evans,G.A. and Farrar,W.L.
  TITLE     Characterization of an interleukin-2 (IL-2)-induced tyrosine
            phosphorylated 116-kDa protein associated with the IL-2 receptor
            beta-subunit
  JOURNAL   J Biol Chem 268 (30), 22765-22770 (1993)
   PUBMED   7693677
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC004971.3, U78525.1 and BQ045103.1.
            
            Transcript Variant: This variant (2) represents the longest
            transcript. Variants 1, 2 and 3 encode the same isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189658.139427.1, U78525.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000360876.9/ ENSP00000354125.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..814
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p22.3"
     Protein         1..814
                     /product="eukaryotic translation initiation factor 3
                     subunit B isoform 1"
                     /note="eukaryotic translation initiation factor 3, subunit
                     9 (eta, 116kD); eukaryotic translation initiation factor
                     3, subunit 9 eta, 116kDa; prt1 homolog; eukaryotic
                     translation initiation factor 3 subunit 9; protein
                     synthesis 1"
                     /calculated_mol_wt=92351
     Region          1..158
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          <4..161
                     /region_name="PRK07764"
                     /note="DNA polymerase III subunits gamma and tau;
                     Validated"
                     /db_xref="CDD:236090"
     Site            78
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            83
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            85
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          124..413
                     /region_name="Sufficient for interaction with EIF3E"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            125
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            152
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            154
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            164
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000255|HAMAP-Rule:MF_03001,
                     ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          170..274
                     /region_name="Sufficient for interaction with EIF3J"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          184..264
                     /region_name="RRM_eIF3B"
                     /note="RNA recognition motif (RRM) found in eukaryotic
                     translation initiation factor 3 subunit B (eIF-3B) and
                     similar proteins; cd12278"
                     /db_xref="CDD:409720"
     Site            order(186,188,190..191,221,230,232,234,262,264)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:409720"
     Site            order(189,192,199,202..203,205..207,209..210,213,249..252,
                     254..255,260..261)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:409720"
     Site            209
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Site            239
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Site            288
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          305..805
                     /region_name="COG5354"
                     /note="Uncharacterized protein, contains Trp-Asp (WD)
                     repeat [General function prediction only]"
                     /db_xref="CDD:227657"
     Region          338..371
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            364
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (P55884.3)"
     Region          366..425
                     /region_name="WD 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          376..423
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          426..489
                     /region_name="WD 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          429..463
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          467..506
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          490..553
                     /region_name="WD 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          514..545
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          554..598
                     /region_name="WD 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          556..604
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          599..642
                     /region_name="WD 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          612..647
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          643..685
                     /region_name="WD 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P55884.3)"
     Region          654..684
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..814
                     /gene="EIF3B"
                     /gene_synonym="EIF3-ETA; EIF3-P110; EIF3-P116; EIF3S9;
                     PRT1"
                     /coded_by="NM_001037283.2:96..2540"
                     /note="isoform 1 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS5332.1"
                     /db_xref="GeneID:8662"
                     /db_xref="HGNC:HGNC:3280"
                     /db_xref="MIM:603917"
ORIGIN      
        1 mqdaenvavp eaaeeraepg qqqpaaeppp aegllrpagp gapeaagtea sseevgiaea
       61 gpesevrtep aaeaeaasgp sespsppaae elpgshaepp vpaqgeapge qardersdsr
      121 aqavsedagg negraaeaep ralengdade psfsdpedfv ddvseeellg dvlkdrpqea
      181 dgidsvivvd nvpqvgpdrl eklknvihki fskfgkitnd fypeedgktk gyifleyasp
      241 ahavdavkna dgykldkqht frvnlftdfd kymtisdewd ipekqpfkdl gnlrywleea
      301 ecrdqysvif esgdrtsifw ndvkdpvsie erarwtetyv rwspkgtyla tfhqrgialw
      361 ggekfkqiqr fshqgvqlid fspcerylvt fsplmdtqdd pqaiiiwdil tghkkrgfhc
      421 essahwpifk wshdgkffar mtldtlsiye tpsmglldkk slkisgikdf swspggniia
      481 fwvpedkdip arvtlmqlpt rqeirvrnlf nvvdcklhwq kngdylcvkv drtpkgtqgv
      541 vtnfeifrmr ekqvpvdvve mketiiafaw epngskfavl hgeaprisvs fyhvknngki
      601 elikmfdkqq antifwspqg qfvvlaglrs mngalafvdt sdctvmniae hymasdvewd
      661 ptgryvvtsv swwshkvdna ywlwtfqgrl lqknnkdrfc qllwrprppt llsqeqikqi
      721 kkdlkkyski feqkdrlsqs kaskelverr rtmmedfrky rkmaqelyme qknerlelrg
      781 gvdtdeldsn vddweeetie ffvteeiipl gnqe
//
LOCUS       NP_001164408             522 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA-binding protein FUS isoform 3 [Homo sapiens].
ACCESSION   NP_001164408
VERSION     NP_001164408.1
DBSOURCE    REFSEQ: accession NM_001170937.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 522)
  AUTHORS   Hou,X., Shi,W., Luo,W., Luo,Y., Huang,X., Li,J., Ji,N. and Chen,Q.
  TITLE     FUS::DDIT3 Fusion Protein in the Development of Myxoid Liposarcoma
            and Possible Implications for Therapy
  JOURNAL   Biomolecules 14 (10), 1297 (2024)
   PUBMED   39456230
  REMARK    GeneRIF: FUS::DDIT3 Fusion Protein in the Development of Myxoid
            Liposarcoma and Possible Implications for Therapy.
            Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 522)
  AUTHORS   Vazquez-Sanchez,S., Tilkin,B., Gasset-Rosa,F., Zhang,S., Piol,D.,
            McAlonis-Downes,M., Artates,J., Govea-Perez,N., Verresen,Y.,
            Guo,L., Cleveland,D.W., Shorter,J. and Da Cruz,S.
  TITLE     Frontotemporal dementia-like disease progression elicited by seeded
            aggregation and spread of FUS
  JOURNAL   Mol Neurodegener 19 (1), 46 (2024)
   PUBMED   38862967
  REMARK    GeneRIF: Frontotemporal dementia-like disease progression elicited
            by seeded aggregation and spread of FUS.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 522)
  AUTHORS   Chen,Y., Pei,X., Chen,L. and Chen,L.
  TITLE     A dynamic regulatory switch for phase separation of FUS protein:
            Zinc ions and zinc finger domain
  JOURNAL   Biochem Biophys Res Commun 710, 149862 (2024)
   PUBMED   38593618
  REMARK    GeneRIF: A dynamic regulatory switch for phase separation of FUS
            protein: Zinc ions and zinc finger domain.
REFERENCE   4  (residues 1 to 522)
  AUTHORS   Ranji,P., Jonasson,E., Andersson,L., Filges,S., Luna Santamaria,M.,
            Vannas,C., Dolatabadi,S., Gustafsson,A., Myklebost,O.,
            Hakansson,J., Fagman,H., Landberg,G., Aman,P. and Stahlberg,A.
  TITLE     Deciphering the role of FUS::DDIT3 expression and tumor
            microenvironment in myxoid liposarcoma development
  JOURNAL   J Transl Med 22 (1), 389 (2024)
   PUBMED   38671504
  REMARK    GeneRIF: Deciphering the role of FUS::DDIT3 expression and tumor
            microenvironment in myxoid liposarcoma development.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 522)
  AUTHORS   Shiramasa,Y., Yamamoto,R., Kashiwagi,N., Sasaki,F., Imai,S.,
            Ike,M., Kitazawa,S., Kameda,T. and Kitahara,R.
  TITLE     An aberrant fused in sarcoma liquid droplet of amyotrophic lateral
            sclerosis pathological variant, R495X, accelerates liquid-solid
            phase transition
  JOURNAL   Sci Rep 14 (1), 8914 (2024)
   PUBMED   38632300
  REMARK    GeneRIF: An aberrant fused in sarcoma liquid droplet of amyotrophic
            lateral sclerosis pathological variant, R495X, accelerates
            liquid-solid phase transition.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 522)
  AUTHORS   Panagopoulos,I., Mandahl,N., Ron,D., Hoglund,M., Nilbert,M.,
            Mertens,F., Mitelman,F. and Aman,P.
  TITLE     Characterization of the CHOP breakpoints and fusion transcripts in
            myxoid liposarcomas with the 12;16 translocation
  JOURNAL   Cancer Res 54 (24), 6500-6503 (1994)
   PUBMED   7987849
REFERENCE   7  (residues 1 to 522)
  AUTHORS   Ichikawa,H., Shimizu,K., Hayashi,Y. and Ohki,M.
  TITLE     An RNA-binding protein gene, TLS/FUS, is fused to ERG in human
            myeloid leukemia with t(16;21) chromosomal translocation
  JOURNAL   Cancer Res 54 (11), 2865-2868 (1994)
   PUBMED   8187069
REFERENCE   8  (residues 1 to 522)
  AUTHORS   Rabbitts,T.H., Forster,A., Larson,R. and Nathan,P.
  TITLE     Fusion of the dominant negative transcription regulator CHOP with a
            novel gene FUS by translocation t(12;16) in malignant liposarcoma
  JOURNAL   Nat Genet 4 (2), 175-180 (1993)
   PUBMED   7503811
REFERENCE   9  (residues 1 to 522)
  AUTHORS   Siddique,N. and Siddique,T.
  TITLE     Amyotrophic Lateral Sclerosis Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301623
REFERENCE   10 (residues 1 to 522)
  AUTHORS   Eneroth,M., Mandahl,N., Heim,S., Willen,H., Rydholm,A.,
            Alberts,K.A. and Mitelman,F.
  TITLE     Localization of the chromosomal breakpoints of the t(12;16) in
            liposarcoma to subbands 12q13.3 and 16p11.2
  JOURNAL   Cancer Genet Cytogenet 48 (1), 101-107 (1990)
   PUBMED   2372777
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC361263.1, DA541747.1,
            U36561.1, AC009088.9 and AI333366.1.
            
            Summary: This gene encodes a multifunctional protein component of
            the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The
            hnRNP complex is involved in pre-mRNA splicing and the export of
            fully processed mRNA to the cytoplasm. This protein belongs to the
            FET family of RNA-binding proteins which have been implicated in
            cellular processes that include regulation of gene expression,
            maintenance of genomic integrity and mRNA/microRNA processing.
            Alternative splicing results in multiple transcript variants.
            Defects in this gene result in amyotrophic lateral sclerosis type
            6. [provided by RefSeq, Sep 2009].
            
            Transcript Variant: This variant (4) uses an alternate in-frame
            splice site in the central coding region, compared to variant 1,
            resulting in an isoform (3) that is shorter than isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMEA1968540,
                              SAMEA1968968 [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..522
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2"
     Protein         1..522
                     /product="RNA-binding protein FUS isoform 3"
                     /note="heterogeneous nuclear ribonucleoprotein P2; fused
                     in sarcoma; fusion gene in myxoid liposarcoma; 75 kDa
                     DNA-pairing protein; RNA-binding protein FUS; oncogene
                     TLS; fus-like protein; oncogene FUS; translocated in
                     liposarcoma protein"
                     /calculated_mol_wt=53067
     Site            26
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29897835; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:29897835; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            42
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by ATM.
                     /evidence=ECO:0000269|PubMed:18620545; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            212
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            214
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            217
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21406692; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            238
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            240
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            244
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            247
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            255
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            262..263
                     /site_type="other"
                     /note="Breakpoint for translocation to form FUS/TLS-CHOP
                     oncogene; propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            273
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          279..364
                     /region_name="RRM_FUS_TAF15"
                     /note="RNA recognition motif (RRM) found in vertebrate
                     fused in Ewing's sarcoma protein (FUS), TATA-binding
                     protein-associated factor 15 (TAF15) and similar proteins;
                     cd12535"
                     /db_xref="CDD:409951"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          371..420
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            373
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            379
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            382
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            384
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            390
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            403
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12964758;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P56959; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Region          418..445
                     /region_name="zf-RanBP"
                     /note="Zn-finger in Ran binding protein and others;
                     pfam00641"
                     /db_xref="CDD:395516"
     Region          440..522
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P35637.1)"
     Site            469
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            472
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            477
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            481
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            483
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            487
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            491
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            494
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000269|PubMed:12964758; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     Site            499
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:12964758;
                     Omega-N-methylarginine, alternate.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (P35637.1)"
     CDS             1..522
                     /gene="FUS"
                     /gene_synonym="ALS6; altFUS; ETM4; FUS1; HNRNPP2; POMP75;
                     TLS"
                     /coded_by="NM_001170937.1:106..1674"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="GeneID:2521"
                     /db_xref="HGNC:HGNC:4010"
                     /db_xref="MIM:137070"
ORIGIN      
        1 masndytqqa tqsygayptq pgqgysqqss qpygqqsysg ysqstdtsgy gqssyssygq
       61 sqntgygtqs tpqgygstgg ygssqssqss ygqqssypgy gqqpapssts gsygsssqss
      121 sygqpqsgsy sqqpsyggqq qsygqqqsyn ppqgygqqnq ynsssggggg gnygqdqssm
      181 ssgggsgggy gnqdqsgggg sggygqqdrg grgrggsggg gggggggynr ssggyeprgr
      241 gggrggrggm ggsdrggfnk fggprdqgsr hdseqdnsdn ntifvqglge nvtiesvady
      301 fkqigiiktn kktgqpminl ytdretgklk geatvsfddp psakaaidwf dgkefsgnpi
      361 kvsfatrrad fnrgggngrg grgrggpmgr ggyggggsgg ggrggfpsgg gggggqqrag
      421 dwkcpnptce nmnfswrnec nqckapkpdg pgggpggshm ggnygddrrg grggydrggy
      481 rgrggdrggf rggrgggdrg gfgpgkmdsr gehrqdrrer py
//
LOCUS       NP_851030                251 aa            linear   PRI 20-NOV-2025
DEFINITION  U11/U12 small nuclear ribonucleoprotein 35 kDa protein isoform b
            [Homo sapiens].
ACCESSION   NP_851030
VERSION     NP_851030.1
DBSOURCE    REFSEQ: accession NM_180699.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 251)
  AUTHORS   Zhao,J., Peter,D., Brandina,I., Liu,X. and Galej,W.P.
  TITLE     Structural basis of 5' splice site recognition by the minor
            spliceosome
  JOURNAL   Mol Cell 85 (3), 652-664 (2025)
   PUBMED   39809272
REFERENCE   2  (residues 1 to 251)
  AUTHORS   Bai,R., Yuan,M., Zhang,P., Luo,T., Shi,Y. and Wan,R.
  TITLE     Structural basis of U12-type intron engagement by the fully
            assembled human minor spliceosome
  JOURNAL   Science 383 (6688), 1245-1252 (2024)
   PUBMED   38484052
REFERENCE   3  (residues 1 to 251)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   4  (residues 1 to 251)
  AUTHORS   Huckins,L.M., Chatzinakos,C., Breen,M.S., Hartmann,J., Klengel,T.,
            da Silva Almeida,A.C., Dobbyn,A., Girdhar,K., Hoffman,G.E.,
            Klengel,C., Logue,M.W., Lori,A., Maihofer,A.X., Morrison,F.G.,
            Nguyen,H.T., Park,Y., Ruderfer,D., Sloofman,L.G., van Rooij,S.J.H.,
            Baker,D.G., Chen,C.Y., Cox,N., Duncan,L.E., Geyer,M.A., Glatt,S.J.,
            Im,H.K., Risbrough,V.B., Smoller,J.W., Stein,D.J., Yehuda,R.,
            Liberzon,I., Koenen,K.C., Jovanovic,T., Kellis,M., Miller,M.W.,
            Bacanu,S.A., Nievergelt,C.M., Buxbaum,J.D., Sklar,P., Ressler,K.J.,
            Stahl,E.A. and Daskalakis,N.P.
  CONSRTM   PTSD Working Group of Psychiatric Genomics Consortium
  TITLE     Analysis of Genetically Regulated Gene Expression Identifies a
            Prefrontal PTSD Gene, SNRNP35, Specific to Military Cohorts
  JOURNAL   Cell Rep 31 (9), 107716 (2020)
   PUBMED   32492425
  REMARK    GeneRIF: Analysis of Genetically Regulated Gene Expression
            Identifies a Prefrontal PTSD Gene, SNRNP35, Specific to Military
            Cohorts.
REFERENCE   5  (residues 1 to 251)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 251)
  AUTHORS   Fertig,N., Domsic,R.T., Rodriguez-Reyna,T., Kuwana,M., Lucas,M.,
            Medsger,T.A. Jr. and Feghali-Bostwick,C.A.
  TITLE     Anti-U11/U12 RNP antibodies in systemic sclerosis: a new serologic
            marker associated with pulmonary fibrosis
  JOURNAL   Arthritis Rheum 61 (7), 958-965 (2009)
   PUBMED   19565553
  REMARK    GeneRIF: Anti-U11/U12 RNP antibodies are present in the sera of
            approximately 3% of patients with systemic sclerosis and are a
            marker for lung fibrosis, which is often severe.
REFERENCE   7  (residues 1 to 251)
  AUTHORS   Pessa,H.K., Will,C.L., Meng,X., Schneider,C., Watkins,N.J.,
            Perala,N., Nymark,M., Turunen,J.J., Luhrmann,R. and Frilander,M.J.
  TITLE     Minor spliceosome components are predominantly localized in the
            nucleus
  JOURNAL   Proc Natl Acad Sci U S A 105 (25), 8655-8660 (2008)
   PUBMED   18559850
REFERENCE   8  (residues 1 to 251)
  AUTHORS   Golas,M.M., Sander,B., Will,C.L., Luhrmann,R. and Stark,H.
  TITLE     Major conformational change in the complex SF3b upon integration
            into the spliceosomal U11/U12 di-snRNP as revealed by electron
            cryomicroscopy
  JOURNAL   Mol Cell 17 (6), 869-883 (2005)
   PUBMED   15780942
REFERENCE   9  (residues 1 to 251)
  AUTHORS   Will,C.L., Schneider,C., Hossbach,M., Urlaub,H., Rauhut,R.,
            Elbashir,S., Tuschl,T. and Luhrmann,R.
  TITLE     The human 18S U11/U12 snRNP contains a set of novel proteins not
            found in the U2-dependent spliceosome
  JOURNAL   RNA 10 (6), 929-941 (2004)
   PUBMED   15146077
REFERENCE   10 (residues 1 to 251)
  AUTHORS   Adams,D.S., Li,Q., Tan,X., Pero,S.C. and Czop,J.K.
  TITLE     Cloning and characterization of a family of cDNAs from human
            histiocyte macrophage cells encoding an arginine-rich basic protein
            related to the 70 kD U1-snRNP splicing factor
  JOURNAL   DNA Seq 9 (4), 205-215 (1998)
   PUBMED   10520751
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC047678.1.
            
            Summary: The protein encoded by this gene is a homolog of the
            U1-snRNP binding protein. The N-terminal half contains a RNA
            recognition motif and the C-terminal half is rich in Arg/Asp and
            Arg/Glu dipeptides, which is a characteristic of a variety of
            splicing factors. This protein is a component of the U11/U12 small
            nuclear ribonucleoproteins (snRNP) that form part of the U12-type
            spliceosome. Alternative splicing results in multiple transcript
            variants encoding two distinct isoforms and representing a
            non-protein coding variant. [provided by RefSeq, Aug 2013].
            
            Transcript Variant: This variant (3) includes an alternate exon and
            initiates translation at an alternate start codon, compared to
            variant 2. The full extent of the 5' UTR of this variant has not
            been determined. The encoded isoform (b) has a longer N-terminus,
            compared to isoform a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.232297.1,
                                           SRR1660807.140783.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..251
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.31"
     Protein         1..251
                     /product="U11/U12 small nuclear ribonucleoprotein 35 kDa
                     protein isoform b"
                     /note="U11/U12 snRNP 35K; U11/U12 small nuclear
                     ribonucleoprotein 35 kDa protein; U11/U12-35K; protein
                     HM-1; U11/U12 snRNP 35 kDa protein; small nuclear
                     ribonucleoprotein 35kDa (U11/U12); small nuclear
                     ribonucleoprotein, U11/U12 35kDa subunit; U1 snRNP-binding
                     protein homolog"
                     /calculated_mol_wt=29861
     Region          52..142
                     /region_name="RRM_snRNP35"
                     /note="RNA recognition motif (RRM) found in U11/U12 small
                     nuclear ribonucleoprotein 35 kDa protein (U11/U12-35K) and
                     similar proteins; cd12237"
                     /db_xref="CDD:409683"
     CDS             1..251
                     /gene="SNRNP35"
                     /gene_synonym="HM-1; HM1; U1SNRNPBP"
                     /coded_by="NM_180699.3:186..941"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS45005.1"
                     /db_xref="GeneID:11066"
                     /db_xref="HGNC:HGNC:30852"
                     /db_xref="MIM:619631"
ORIGIN      
        1 mkpanmndwm piakeydplk agsidgtded phdravwram laryvpnkgv igdplltlfv
       61 arlnlqtked klkevfsryg dirrlrlvrd lvtgfskgya fieykeerav ikayrdadgl
      121 vidqheifvd yelertlkgw iprrlggglg gkkesgqlrf ggrdrpfrkp inlpvvkndl
      181 yregkrerre rsrsrerhwd srtrdrdhdr grekrwqere ptrvwpdndw ererdfrddr
      241 ikgrekkerg k
//
LOCUS       NP_001253976             264 aa            linear   PRI 20-NOV-2025
DEFINITION  FERM domain-containing protein 6 isoform 3 [Homo sapiens].
ACCESSION   NP_001253976
VERSION     NP_001253976.1
DBSOURCE    REFSEQ: accession NM_001267047.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 264)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 264)
  AUTHORS   von Koskull,A., Hagstrom,J., Haglund,C., Kaprio,T. and Bockelman,C.
  TITLE     High-tissue FRMD6 expression predicts better outcomes among
            colorectal cancer patients
  JOURNAL   Biomarkers 29 (3), 127-133 (2024)
   PUBMED   38385211
  REMARK    GeneRIF: High-tissue FRMD6 expression predicts better outcomes
            among colorectal cancer patients.
REFERENCE   3  (residues 1 to 264)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 264)
  AUTHORS   Shen,L., Dang,J., Liu,S., Xian,B., Deng,Y. and Qu,D.
  TITLE     CircRNA VPRBP inhibits tumorigenicity of cervical cancer via
            miR-93-5p/FRMD6 axis
  JOURNAL   Reprod Sci 29 (8), 2251-2264 (2022)
   PUBMED   35501594
  REMARK    GeneRIF: CircRNA VPRBP inhibits tumorigenicity of cervical cancer
            via miR-93-5p/FRMD6 axis.
REFERENCE   5  (residues 1 to 264)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 264)
  AUTHORS   Potkin,S.G., Guffanti,G., Lakatos,A., Turner,J.A., Kruggel,F.,
            Fallon,J.H., Saykin,A.J., Orro,A., Lupoli,S., Salvi,E., Weiner,M.
            and Macciardi,F.
  CONSRTM   Alzheimer's Disease Neuroimaging Initiative
  TITLE     Hippocampal atrophy as a quantitative trait in a genome-wide
            association study identifying novel susceptibility genes for
            Alzheimer's disease
  JOURNAL   PLoS One 4 (8), e6501 (2009)
   PUBMED   19668339
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 264)
  AUTHORS   Hamaratoglu,F., Willecke,M., Kango-Singh,M., Nolo,R., Hyun,E.,
            Tao,C., Jafar-Nejad,H. and Halder,G.
  TITLE     The tumour-suppressor genes NF2/Merlin and Expanded act through
            Hippo signalling to regulate cell proliferation and apoptosis
  JOURNAL   Nat Cell Biol 8 (1), 27-36 (2006)
   PUBMED   16341207
  REMARK    Erratum:[Nat Cell Biol. 2006 Jan;8(1):100]
REFERENCE   8  (residues 1 to 264)
  AUTHORS   Gunn-Moore,F.J., Welsh,G.I., Herron,L.R., Brannigan,F.,
            Venkateswarlu,K., Gillespie,S., Brandwein-Gensler,M., Madan,R.,
            Tavare,J.M., Brophy,P.J., Prystowsky,M.B. and Guild,S.
  TITLE     A novel 4.1 ezrin radixin moesin (FERM)-containing protein,
            'Willin'
  JOURNAL   FEBS Lett 579 (22), 5089-5094 (2005)
   PUBMED   16137681
  REMARK    GeneRIF: Results describe a new FERM domain-containing protein
            called Willin.
REFERENCE   9  (residues 1 to 264)
  AUTHORS   Jin,J., Smith,F.D., Stark,C., Wells,C.D., Fawcett,J.P.,
            Kulkarni,S., Metalnikov,P., O'Donnell,P., Taylor,P., Taylor,L.,
            Zougman,A., Woodgett,J.R., Langeberg,L.K., Scott,J.D. and Pawson,T.
  TITLE     Proteomic, functional, and domain-based analysis of in vivo 14-3-3
            binding proteins involved in cytoskeletal regulation and cellular
            organization
  JOURNAL   Curr Biol 14 (16), 1436-1450 (2004)
   PUBMED   15324660
REFERENCE   10 (residues 1 to 264)
  AUTHORS   Heilig,R., Eckenberg,R., Petit,J.L., Fonknechten,N., Da Silva,C.,
            Cattolico,L., Levy,M., Barbe,V., de Berardinis,V., Ureta-Vidal,A.,
            Pelletier,E., Vico,V., Anthouard,V., Rowen,L., Madan,A., Qin,S.,
            Sun,H., Du,H., Pepin,K., Artiguenave,F., Robert,C., Cruaud,C.,
            Bruls,T., Jaillon,O., Friedlander,L., Samson,G., Brottier,P.,
            Cure,S., Segurens,B., Aniere,F., Samain,S., Crespeau,H., Abbasi,N.,
            Aiach,N., Boscus,D., Dickhoff,R., Dors,M., Dubois,I., Friedman,C.,
            Gouyvenoux,M., James,R., Madan,A., Mairey-Estrada,B., Mangenot,S.,
            Martins,N., Menard,M., Oztas,S., Ratcliffe,A., Shaffer,T.,
            Trask,B., Vacherie,B., Bellemere,C., Belser,C., Besnard-Gonnet,M.,
            Bartol-Mavel,D., Boutard,M., Briez-Silla,S., Combette,S.,
            Dufosse-Laurent,V., Ferron,C., Lechaplais,C., Louesse,C.,
            Muselet,D., Magdelenat,G., Pateau,E., Petit,E.,
            Sirvain-Trukniewicz,P., Trybou,A., Vega-Czarny,N., Bataille,E.,
            Bluet,E., Bordelais,I., Dubois,M., Dumont,C., Guerin,T.,
            Haffray,S., Hammadi,R., Muanga,J., Pellouin,V., Robert,D.,
            Wunderle,E., Gauguet,G., Roy,A., Sainte-Marthe,L., Verdier,J.,
            Verdier-Discala,C., Hillier,L., Fulton,L., McPherson,J.,
            Matsuda,F., Wilson,R., Scarpelli,C., Gyapay,G., Wincker,P.,
            Saurin,W., Quetier,F., Waterston,R., Hood,L. and Weissenbach,J.
  TITLE     The DNA sequence and analysis of human chromosome 14
  JOURNAL   Nature 421 (6923), 601-607 (2003)
   PUBMED   12508121
  REMARK    Erratum:[Nature. 2023 Aug;620(7973):E17. doi:
            10.1038/s41586-023-06403-y. PMID: 37491470]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC029870.1 and AL833661.1.
            
            Transcript Variant: This variant (4) differs in the 5' UTR and
            represents the use of an alternate promoter and an in-frame
            downstream start codon, compared to variant 1. These differences
            result in a protein (isoform 3) with a shorter N-terminus, compared
            to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029870.1, BG717340.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..264
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
     Protein         1..264
                     /product="FERM domain-containing protein 6 isoform 3"
                     /note="4.1 ezrin radixin moesin (FERM)-containing protein;
                     expanded homolog; FERM domain-containing protein 6"
                     /calculated_mol_wt=29104
     CDS             1..264
                     /gene="FRMD6"
                     /gene_synonym="C14orf31; c14_5320; EX1; Willin"
                     /coded_by="NM_001267047.1:117..911"
                     /note="isoform 3 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS58319.1"
                     /db_xref="GeneID:122786"
                     /db_xref="HGNC:HGNC:19839"
                     /db_xref="MIM:614555"
ORIGIN      
        1 mdqlekrsra sgssagsmkh krlsrhstas hssshtsgie adtkprdtgp edsysssaih
       61 rklktcssmt shgsshtsgv esggkdrlee dlqddeieml vddprdleqm neeslevspd
      121 mciyitedml msrklnghsg livkeigsst ssssetvvkl rgqstdslpq ticrkpktst
      181 drhslslddi rlyqkdflri aglcqdtaqs ytfgcgheld eeglycnscl aqqciniqda
      241 fpvkrtskyf sldlthdevp efvv
//
LOCUS       NP_777360                436 aa            linear   PRI 20-NOV-2025
DEFINITION  26S proteasome non-ATPase regulatory subunit 12 isoform 2 [Homo
            sapiens].
ACCESSION   NP_777360
VERSION     NP_777360.1
DBSOURCE    REFSEQ: accession NM_174871.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 436)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 436)
  AUTHORS   Lv,J., Ma,S., Wang,X., Dang,J. and Ma,F.
  TITLE     PSMD12 promotes non-small cell lung cancer progression through
            activating the Nrf2/TrxR1 pathway
  JOURNAL   Genes Genomics 46 (3), 263-277 (2024)
   PUBMED   38243044
  REMARK    GeneRIF: PSMD12 promotes non-small cell lung cancer progression
            through activating the Nrf2/TrxR1 pathway.
REFERENCE   3  (residues 1 to 436)
  AUTHORS   Ma,J., Zhou,W., Yuan,Y., Wang,B. and Meng,X.
  TITLE     PSMD12 interacts with CDKN3 and facilitates pancreatic cancer
            progression
  JOURNAL   Cancer Gene Ther 30 (8), 1072-1083 (2023)
   PUBMED   37037907
  REMARK    GeneRIF: PSMD12 interacts with CDKN3 and facilitates pancreatic
            cancer progression.
REFERENCE   4  (residues 1 to 436)
  AUTHORS   Sun,C., Desch,K., Nassim-Assir,B., Giandomenico,S.L., Nemcova,P.,
            Langer,J.D. and Schuman,E.M.
  TITLE     An abundance of free regulatory (19S) proteasome particles
            regulates neuronal synapses
  JOURNAL   Science 380 (6647), eadf2018 (2023)
   PUBMED   37228199
REFERENCE   5  (residues 1 to 436)
  AUTHORS   Zhang,H., Li,C., Liao,S., Tu,Y., Sun,S., Yao,F., Li,Z. and Wang,Z.
  TITLE     PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer
  JOURNAL   Cancer Biol Ther 23 (1), 1-11 (2022)
   PUBMED   36137220
  REMARK    GeneRIF: PSMD12 promotes the activation of the MEK-ERK pathway by
            upregulating KIF15 to promote the malignant progression of liver
            cancer.
REFERENCE   6  (residues 1 to 436)
  AUTHORS   Madani,N. and Kabat,D.
  TITLE     An endogenous inhibitor of human immunodeficiency virus in human
            lymphocytes is overcome by the viral Vif protein
  JOURNAL   J Virol 72 (12), 10251-10255 (1998)
   PUBMED   9811770
REFERENCE   7  (residues 1 to 436)
  AUTHORS   Saito,A., Watanabe,T.K., Shimada,Y., Fujiwara,T., Slaughter,C.A.,
            DeMartino,G.N., Tanahashi,N. and Tanaka,K.
  TITLE     cDNA cloning and functional analysis of p44.5 and p55, two
            regulatory subunits of the 26S proteasome
  JOURNAL   Gene 203 (2), 241-250 (1997)
   PUBMED   9426256
REFERENCE   8  (residues 1 to 436)
  AUTHORS   Seeger,M., Ferrell,K., Frank,R. and Dubiel,W.
  TITLE     HIV-1 tat inhibits the 20 S proteasome and its 11 S
            regulator-mediated activation
  JOURNAL   J Biol Chem 272 (13), 8145-8148 (1997)
   PUBMED   9079628
REFERENCE   9  (residues 1 to 436)
  AUTHORS   Coux,O., Tanaka,K. and Goldberg,A.L.
  TITLE     Structure and functions of the 20S and 26S proteasomes
  JOURNAL   Annu Rev Biochem 65, 801-847 (1996)
   PUBMED   8811196
  REMARK    Review article
REFERENCE   10 (residues 1 to 436)
  AUTHORS   Kanayama,H.O., Tamura,T., Ugai,S., Kagawa,S., Tanahashi,N.,
            Yoshimura,T., Tanaka,K. and Ichihara,A.
  TITLE     Demonstration that a human 26S proteolytic complex consists of a
            proteasome and multiple associated protein components and
            hydrolyzes ATP and ubiquitin-ligated proteins by closely linked
            mechanisms
  JOURNAL   Eur J Biochem 206 (2), 567-578 (1992)
   PUBMED   1317798
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK091198.1, AC110921.9 and
            BU616916.1.
            
            Summary: The 26S proteasome is a multicatalytic proteinase complex
            with a highly ordered structure composed of 2 complexes, a 20S core
            and a 19S regulator. The 20S core is composed of 4 rings of 28
            non-identical subunits; 2 rings are composed of 7 alpha subunits
            and 2 rings are composed of 7 beta subunits. The 19S regulator is
            composed of a base, which contains 6 ATPase subunits and 2
            non-ATPase subunits, and a lid, which contains up to 10 non-ATPase
            subunits. Proteasomes are distributed throughout eukaryotic cells
            at a high concentration and cleave peptides in an
            ATP/ubiquitin-dependent process in a non-lysosomal pathway. An
            essential function of a modified proteasome, the immunoproteasome,
            is the processing of class I MHC peptides. This gene encodes a
            non-ATPase subunit of the 19S regulator. A pseudogene has been
            identified on chromosome 3. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq, Oct 2015].
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            coding exon compared to variant 1. The resulting isoform (2) has
            the same N- and C-termini but is shorter compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK091198.1, SRR14038192.3094534.1
                                           [ECO:0000332]
            RNAseq introns              :: partial sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0000350]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..436
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q24.2"
     Protein         1..436
                     /product="26S proteasome non-ATPase regulatory subunit 12
                     isoform 2"
                     /note="26S proteasome regulatory subunit p55; 26S
                     proteasome regulatory subunit RPN5; proteasome (prosome,
                     macropain) 26S subunit, non-ATPase, 12"
                     /calculated_mol_wt=50448
     Region          17..436
                     /region_name="RPN5"
                     /note="26S proteasome regulatory complex component
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5071"
                     /db_xref="CDD:227403"
     CDS             1..436
                     /gene="PSMD12"
                     /gene_synonym="p55; Rpn5; STISS"
                     /coded_by="NM_174871.4:59..1369"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS11670.1"
                     /db_xref="GeneID:5718"
                     /db_xref="HGNC:HGNC:9557"
                     /db_xref="MIM:604450"
ORIGIN      
        1 madggserad grivkmevdy satvdqrlpe caklakasdm vstsrilvav vkmcyeakew
       61 dllnenimll skrrsqlkqa vakmvqqcct yveeitdlpi klrlidtlrm vtegkiyvei
      121 erarltktla tikeqngdvk eaasilqelq vetygsmekk ervefileqm rlclavkdyi
      181 rtqiiskkin tkffqeente klklkyynlm iqldqhegsy lsickhyrai ydtpciqaes
      241 ekwqqalksv vlyvilapfd neqsdlvhri sgdkkleeip kykdllklft tmelmrwstl
      301 vedygmelrk gslespatdv fgsteegekr wkdlknrvve hnirimakyy tritmkrmaq
      361 lldlsvdese aflsnlvvnk tifakvdrla giinfqrpkd pnnllndwsq klnslmslvn
      421 ktthliakee mihnlq
//
LOCUS       NP_000055               1663 aa            linear   PRI 20-NOV-2025
DEFINITION  complement C3 preproprotein [Homo sapiens].
ACCESSION   NP_000055
VERSION     NP_000055.2
DBSOURCE    REFSEQ: accession NM_000064.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1663)
  AUTHORS   Li,Y., Perera,L., He,R.S., Baptissart,M., Petrovich,R.M. and
            Morgan,M.
  TITLE     TENT5C functions as a corepressor in the ligand-bound
            glucocorticoid receptor and estrogen receptor alpha complexes
  JOURNAL   FEBS J 292 (19), 5168-5184 (2025)
   PUBMED   40421654
REFERENCE   2  (residues 1 to 1663)
  AUTHORS   Donado,C.A., Theisen,E., Zhang,F., Nathan,A., Fairfield,M.L.,
            Rupani,K.V., Jones,D., Johannes,K.P., Raychaudhuri,S., Dwyer,D.F.,
            Jonsson,A.H. and Brenner,M.B.
  CONSRTM   Accelerating Medicines Partnership RA/SLE Network
  TITLE     Granzyme K activates the entire complement cascade
  JOURNAL   Nature 641 (8061), 211-221 (2025)
   PUBMED   39914456
REFERENCE   3  (residues 1 to 1663)
  AUTHORS   Ge,T.Q., Guan,P.P. and Wang,P.
  TITLE     Complement 3a induces the synapse loss via C3aR in
            mitochondria-dependent NLRP3 activating mechanisms during the
            development and progression of Alzheimer's disease
  JOURNAL   Neurosci Biobehav Rev 165, 105868 (2024)
   PUBMED   39218048
  REMARK    GeneRIF: Complement 3a induces the synapse loss via C3aR in
            mitochondria-dependent NLRP3 activating mechanisms during the
            development and progression of Alzheimer's disease.
            Review article
REFERENCE   4  (residues 1 to 1663)
  AUTHORS   Zimmer,J., Hobkirk,J., Mohamed,F., Browning,M.J. and Stover,C.M.
  TITLE     On the Functional Overlap between Complement and Anti-Microbial
            Peptides
  JOURNAL   Front Immunol 5, 689 (2015)
   PUBMED   25646095
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1663)
  AUTHORS   Nordahl,E.A., Rydengard,V., Nyberg,P., Nitsche,D.P., Morgelin,M.,
            Malmsten,M., Bjorck,L. and Schmidtchen,A.
  TITLE     Activation of the complement system generates antibacterial
            peptides
  JOURNAL   Proc Natl Acad Sci U S A 101 (48), 16879-16884 (2004)
   PUBMED   15550543
  REMARK    GeneRIF: A peptide (C3a) derived from the complement C3 protein has
            antimicrobial activity against E. coli, P. aeruginosa, E. faecalis,
            and C. albicans.
REFERENCE   6  (residues 1 to 1663)
  AUTHORS   Martin,B. and Smith,R.J.H.
  TITLE     C3 Glomerulopathy
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301598
REFERENCE   7  (residues 1 to 1663)
  AUTHORS   Noris,M., Bresin,E., Mele,C. and Remuzzi,G.
  TITLE     Genetic Atypical Hemolytic-Uremic Syndrome
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301541
REFERENCE   8  (residues 1 to 1663)
  AUTHORS   de Bruijn,M.H. and Fey,G.H.
  TITLE     Human complement component C3: cDNA coding sequence and derived
            primary structure
  JOURNAL   Proc Natl Acad Sci U S A 82 (3), 708-712 (1985)
   PUBMED   2579379
REFERENCE   9  (residues 1 to 1663)
  AUTHORS   Fearon,D.T.
  TITLE     Activation of the alternative complement pathway
  JOURNAL   CRC Crit Rev Immunol 1 (1), 1-32 (1979)
   PUBMED   162484
  REMARK    Review article
REFERENCE   10 (residues 1 to 1663)
  AUTHORS   Schreiber,R.D., Pangburn,M.K., Lesavre,P.H. and
            Muller-Eberhard,H.J.
  TITLE     Initiation of the alternative pathway of complement: recognition of
            activators by bound C3b and assembly of the entire pathway from six
            isolated proteins
  JOURNAL   Proc Natl Acad Sci U S A 75 (8), 3948-3952 (1978)
   PUBMED   279011
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK299114.1, K02765.1,
            BC150179.1, BC150299.1, AC008760.7 and AA025232.1.
            
            On Sep 22, 2006 this sequence version replaced NP_000055.1.
            
            Summary: Complement component C3 plays a central role in the
            activation of complement system. Its activation is required for
            both classical and alternative complement activation pathways. The
            encoded preproprotein is proteolytically processed to generate
            alpha and beta subunits that form the mature protein, which is then
            further processed to generate numerous peptide products. The C3a
            peptide, also known as the C3a anaphylatoxin, modulates
            inflammation and possesses antimicrobial activity. Mutations in
            this gene are associated with atypical hemolytic uremic syndrome
            and age-related macular degeneration in human patients. [provided
            by RefSeq, Nov 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC150299.1, SRR1660807.97673.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN04284274 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match                 :: ENST00000245907.11/
                                                  ENSP00000245907.4
            Protein has antimicrobial activity :: PMID: 15550543
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1663
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..1663
                     /product="complement C3 preproprotein"
                     /EC_number="3.4.21.43"
                     /note="acylation-stimulating protein cleavage product;
                     prepro-C3; C3a anaphylatoxin; complement component C3a;
                     complement component C3b; epididymis secretory sperm
                     binding protein Li 62p; C3 and PZP-like
                     alpha-2-macroglobulin domain-containing protein 1;
                     complement component 3"
                     /calculated_mol_wt=184952
     sig_peptide     1..22
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2215
     mat_peptide     23..1663
                     /product="Complement C3. /id=PRO_0000005907"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=184952
     mat_peptide     23..667
                     /product="Complement C3 beta chain.
                     /evidence=ECO:0000305|PubMed:16177781. /id=PRO_0000005908"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=71317
     Region          23..124
                     /region_name="MG1"
                     /note="Macroglobulin domain MG1; pfam17790"
                     /db_xref="CDD:465508"
     Site            38
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            70
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            85
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:12754519,
                     ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952,
                     ECO:0000269|PubMed:17051150, ECO:0000269|PubMed:17684013,
                     ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2579379;
                     propagated from UniProtKB/Swiss-Prot (P01024.2)"
     Region          <128..1338
                     /region_name="YfaS"
                     /note="Uncharacterized conserved protein YfaS,
                     alpha-2-macroglobulin family [General function prediction
                     only]; COG2373"
                     /db_xref="CDD:441940"
     Site            297
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            541..542
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by S.pyogenes SpeB.
                     /evidence=ECO:0000269|PubMed:18160402; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     mat_peptide     569..667
                     /product="C3-beta-c.
                     /evidence=ECO:0000250|UniProtKB:P01026.
                     /id=PRO_0000430430"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=10531
     mat_peptide     672..1663
                     /product="Complement C3 alpha chain. /id=PRO_0000005909"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=113029
     mat_peptide     672..748
                     /product="complement C3"
                     /experiment="DESCRIPTION:antimicrobial
                     peptide[PMID:15550543]"
                     /exception="alternative processing"
                     /calculated_mol_wt=9095
     mat_peptide     672..747
                     /product="Acylation stimulating protein.
                     /id=PRO_0000419935"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=8939
     Site            672
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            744..745
                     /site_type="other"
                     /note="(Microbial infection) Cleavage, by N.meningitidis
                     NalP. /evidence=ECO:0000269|PubMed:24367091; propagated
                     from UniProtKB/Swiss-Prot (P01024.2)"
     Site            747..748
                     /site_type="cleavage"
                     /note="Cleavage, by carboxypeptidases.
                     /evidence=ECO:0000269|PubMed:4098172,
                     ECO:0000269|PubMed:6968751; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            748..749
                     /site_type="cleavage"
                     /note="Cleavage, by C3 convertase.
                     /evidence=ECO:0000305|PubMed:16177781; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     mat_peptide     749..1663
                     /product="Complement C3b.
                     /evidence=ECO:0000305|PubMed:16177781. /id=PRO_0000005911"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=103952
     mat_peptide     749..954
                     /product="Complement C3c alpha' chain fragment 1.
                     /id=PRO_0000005912"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=23590
     Region          770..866
                     /region_name="A2M"
                     /note="Alpha-2-macroglobulin family; pfam00207"
                     /db_xref="CDD:459711"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:14760718,
                     ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150;
                     propagated from UniProtKB/Swiss-Prot (P01024.2)"
     Region          954..973
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
     Site            954..955
                     /site_type="cleavage"
                     /note="Cleavage, by factor I.
                     /evidence=ECO:0000305|PubMed:28671664; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     mat_peptide     955..1303
                     /product="Complement C3dg fragment. /id=PRO_0000005913"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=38906
     mat_peptide     955..1001
                     /product="Complement C3g fragment. /id=PRO_0000005914"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=5137
     Site            968
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Region          996..1282
                     /region_name="complement_C3_C4_C5"
                     /note="Proteins similar to C3, C4 and C5 of vertebrate
                     complement. The vertebrate complement system, comprised of
                     a large number of distinct plasma proteins, is an effector
                     of both the acquired and innate immune systems. The point
                     of convergence of the...; cd02896"
                     /db_xref="CDD:239226"
     mat_peptide     1002..1303
                     /product="Complement C3d fragment.
                     /evidence=ECO:0000305|PubMed:9596584. /id=PRO_0000005915"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=33787
     Site            order(1010,1012..1013,1016,1059,1069,1072,1123,1125..1126,
                     1266)
                     /site_type="other"
                     /note="surface patch"
                     /db_xref="CDD:239226"
     Site            order(1010..1013,1126)
                     /site_type="active"
                     /db_xref="CDD:239226"
     Site            1010..1013
                     /site_type="active"
                     /note="thioester region [active]"
                     /db_xref="CDD:239226"
     Site            order(1112,1116,1118,1126,1131..1132)
                     /site_type="other"
                     /note="specificity defining residues"
                     /db_xref="CDD:239226"
     Site            1303..1304
                     /site_type="cleavage"
                     /note="Cleavage, by factor I.
                     /evidence=ECO:0000305|PubMed:28671664; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     mat_peptide     1304..1320
                     /product="Complement C3f fragment.
                     /evidence=ECO:0000269|PubMed:8376604. /id=PRO_0000005916"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=2021
     Site            1320..1321
                     /site_type="cleavage"
                     /note="Cleavage, by factor I.
                     /evidence=ECO:0000305|PubMed:28671664; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     mat_peptide     1321..1663
                     /product="Complement C3c alpha' chain fragment 2.
                     /id=PRO_0000273948"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
                     /calculated_mol_wt=39489
     Site            1321
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Region          1396..1494
                     /region_name="A2M_recep"
                     /note="A-macroglobulin receptor binding domain; pfam07677"
                     /db_xref="CDD:462226"
     Region          1513..1661
                     /region_name="NTR_complement_C3"
                     /note="NTR/C345C domain, complement C3 subfamily; The NTR
                     domain found in complement C3 is also known as the C345C
                     domain because it occurs at the C-terminus of complement
                     C3, C4 and C5. Complement C3 plays a pivotal role in the
                     activation of the complement...; cd03583"
                     /db_xref="CDD:239638"
     Site            1573
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by FAM20C.
                     /evidence=ECO:0000269|PubMed:26091039; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Site            1617
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     Region          1634..1659
                     /region_name="Interaction with CFP/properdin.
                     /evidence=ECO:0000269|PubMed:28264884,
                     ECO:0000269|PubMed:31507604"
                     /note="propagated from UniProtKB/Swiss-Prot (P01024.2)"
     Site            1663
                     /site_type="other"
                     /note="Coordinates Mg(2+) for interaction with Complement
                     factor B Bb fragment (CFB).
                     /evidence=ECO:0000269|PubMed:28264884,
                     ECO:0000269|PubMed:31507604; propagated from
                     UniProtKB/Swiss-Prot (P01024.2)"
     CDS             1..1663
                     /gene="C3"
                     /gene_synonym="AHUS5; ARMD9; ASP; C3a; C3b; CPAMD1;
                     HEL-S-62p"
                     /coded_by="NM_000064.4:62..5053"
                     /db_xref="CCDS:CCDS32883.1"
                     /db_xref="GeneID:718"
                     /db_xref="HGNC:HGNC:1318"
                     /db_xref="MIM:120700"
ORIGIN      
        1 mgptsgpsll llllthlpla lgspmysiit pnilrlesee tmvleahdaq gdvpvtvtvh
       61 dfpgkklvls sektvltpat nhmgnvtfti panrefksek grnkfvtvqa tfgtqvvekv
      121 vlvslqsgyl fiqtdktiyt pgstvlyrif tvnhkllpvg rtvmvnienp egipvkqdsl
      181 ssqnqlgvlp lswdipelvn mgqwkirayy enspqqvfst efevkeyvlp sfevivepte
      241 kfyyiynekg levtitarfl ygkkvegtaf vifgiqdgeq rislpeslkr ipiedgsgev
      301 vlsrkvlldg vqnpraedlv gkslyvsatv ilhsgsdmvq aersgipivt spyqihftkt
      361 pkyfkpgmpf dlmvfvtnpd gspayrvpva vqgedtvqsl tqgdgvakls inthpsqkpl
      421 sitvrtkkqe lseaeqatrt mqalpystvg nsnnylhlsv lrtelrpget lnvnfllrmd
      481 raheakiryy tylimnkgrl lkagrqvrep gqdlvvlpls ittdfipsfr lvayytliga
      541 sgqrevvads vwvdvkdscv gslvvksgqs edrqpvpgqq mtlkiegdhg arvvlvavdk
      601 gvfvlnkknk ltqskiwdvv ekadigctpg sgkdyagvfs dagltftsss gqqtaqrael
      661 qcpqpaarrr rsvqltekrm dkvgkypkel rkccedgmre npmrfscqrr trfislgeac
      721 kkvfldccny itelrrqhar ashlglarsn ldediiaeen ivsrsefpes wlwnvedlke
      781 ppkngistkl mniflkdsit tweilavsms dkkgicvadp fevtvmqdff idlrlpysvv
      841 rneqveirav lynyrqnqel kvrvellhnp afcslattkr rhqqtvtipp ksslsvpyvi
      901 vplktglqev evkaavyhhf isdgvrkslk vvpegirmnk tvavrtldpe rlgregvqke
      961 dippadlsdq vpdtesetri llqgtpvaqm tedavdaerl khlivtpsgc geqnmigmtp
     1021 tviavhylde teqwekfgle krqgalelik kgytqqlafr qpssafaafv krapstwlta
     1081 yvvkvfslav nliaidsqvl cgavkwlile kqkpdgvfqe dapvihqemi gglrnnnekd
     1141 maltafvlis lqeakdicee qvnslpgsit kagdfleany mnlqrsytva iagyalaqmg
     1201 rlkgpllnkf lttakdknrw edpgkqlynv eatsyallal lqlkdfdfvp pvvrwlneqr
     1261 yygggygstq atfmvfqala qyqkdapdhq elnldvslql psrsskithr ihwesasllr
     1321 seetkenegf tvtaegkgqg tlsvvtmyha kakdqltcnk fdlkvtikpa petekrpqda
     1381 kntmileict ryrgdqdatm sildismmtg fapdtddlkq langvdryis kyeldkafsd
     1441 rntliiyldk vshseddcla fkvhqyfnve liqpgavkvy ayynleesct rfyhpekedg
     1501 klnklcrdel crcaeencfi qksddkvtle erldkacepg vdyvyktrlv kvqlsndfde
     1561 yimaieqtik sgsdevqvgq qrtfispikc realkleekk hylmwglssd fwgekpnlsy
     1621 iigkdtwveh wpeedecqde enqkqcqdlg aftesmvvfg cpn
//
LOCUS       NP_057537                722 aa            linear   PRI 20-NOV-2025
DEFINITION  NCK-interacting protein with SH3 domain isoform 1 [Homo sapiens].
ACCESSION   NP_057537
VERSION     NP_057537.1
DBSOURCE    REFSEQ: accession NM_016453.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 722)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 722)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 722)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 722)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 722)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 722)
  AUTHORS   Lim,C.S., Park,E.S., Kim,D.J., Song,Y.H., Eom,S.H., Chun,J.S.,
            Kim,J.H., Kim,J.K., Park,D. and Song,W.K.
  TITLE     SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor
            protein that is developmentally regulated during cardiac myocyte
            differentiation
  JOURNAL   J Biol Chem 276 (16), 12871-12878 (2001)
   PUBMED   11278500
REFERENCE   7  (residues 1 to 722)
  AUTHORS   Hayakawa,A., Matsuda,Y., Daibata,M., Nakamura,H. and Sano,K.
  TITLE     Genomic organization, tissue expression, and cellular localization
            of AF3p21, a fusion partner of MLL in therapy-related leukemia
  JOURNAL   Genes Chromosomes Cancer 30 (4), 364-374 (2001)
   PUBMED   11241789
REFERENCE   8  (residues 1 to 722)
  AUTHORS   Fukuoka,M., Suetsugu,S., Miki,H., Fukami,K., Endo,T. and
            Takenawa,T.
  TITLE     A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding
            protein, WISH, induces Arp2/3 complex activation independent of
            Cdc42
  JOURNAL   J Cell Biol 152 (3), 471-482 (2001)
   PUBMED   11157975
REFERENCE   9  (residues 1 to 722)
  AUTHORS   Sano,K., Hayakawa,A., Piao,J.H., Kosaka,Y. and Nakamura,H.
  TITLE     Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed
            lineage leukemia protein in a therapy-related leukemia with t(3;11)
            (p21;q23)
  JOURNAL   Blood 95 (3), 1066-1068 (2000)
   PUBMED   10648423
REFERENCE   10 (residues 1 to 722)
  AUTHORS   de Bernard,M., Moschioni,M., Napolitani,G., Rappuoli,R. and
            Montecucco,C.
  TITLE     The VacA toxin of Helicobacter pylori identifies a new intermediate
            filament-interacting protein
  JOURNAL   EMBO J 19 (1), 48-56 (2000)
   PUBMED   10619843
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY010884.1, HY050918.1 and
            AF303581.1.
            
            Summary: The protein encoded by this gene contains a nuclear
            localization signal. It plays a role in signal transduction, and
            may function in the maintenance of sarcomeres and in the assembly
            of myofibrils into sarcomeres. It also plays an important role in
            stress fiber formation This protein is involved in the formation
            and maintenance of dendritic spines, and modulates synaptic
            activity in neurons. The gene is involved in therapy-related
            leukemia by a chromosomal translocation t(3;11)(p21;q23) that
            involves this gene and the myeloid/lymphoid leukemia gene.
            Alternative splicing results in multiple transcript variants of
            this gene. [provided by RefSeq, Aug 2019].
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF178432.1, SRR1803615.191540.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000294129.7/ ENSP00000294129.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..722
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.31"
     Protein         1..722
                     /product="NCK-interacting protein with SH3 domain isoform
                     1"
                     /note="SH3 protein interacting with Nck, 90 kDa; dia
                     interacting protein; diaphanous protein interacting
                     protein; dia-interacting protein 1; SH3 adapter protein
                     SPIN90; 54 kDa VacA-interacting protein; 90 kDa SH3
                     protein interacting with Nck; 54 kDa vimentin-interacting
                     protein; WASP-interacting SH3-domain protein;
                     wiskott-Aldrich syndrome protein-interacting protein"
                     /calculated_mol_wt=78829
     Region          1..54
                     /region_name="SH3_SPIN90"
                     /note="Src homology 3 domain of SH3 protein interacting
                     with Nck, 90 kDa (SPIN90); cd11849"
                     /db_xref="CDD:212783"
     Site            order(6,8,11,15,33..34,49,51..52)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212783"
     Site            57..58
                     /site_type="other"
                     /note="Breakpoint for translocation to form
                     KMT2A/MLL1-AF3P21 oncogene; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          101..122
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ4; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          149..286
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          175..192
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            181
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Site            294
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ESJ4; propagated from
                     UniProtKB/Swiss-Prot (Q9NZQ3.1)"
     Region          <570..683
                     /region_name="SPIN90_LRD"
                     /note="SPIN90/Ldb17, leucine-rich domain; pfam09431"
                     /db_xref="CDD:462796"
     CDS             1..722
                     /gene="NCKIPSD"
                     /gene_synonym="AF3P21; DIP; DIP1; ORF1; SPIN90; VIP54;
                     WASLBP; WISH"
                     /coded_by="NM_016453.4:109..2277"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2776.1"
                     /db_xref="GeneID:51517"
                     /db_xref="HGNC:HGNC:15486"
                     /db_xref="MIM:606671"
ORIGIN      
        1 myralyafrs aepnalafaa getflvlers sahwwlaara rsgetgyvpp aylrrlqgle
       61 qdvlqaidra ieavhntamr dggkysleqr gvlqklihhr ketlsrrgps assvavmtss
      121 tsdhhldaaa arqpngvcra gferqhslps sehlgadggl yqiplpssqi ppqprraapt
      181 tppppvkrrd realmasgsg ghntmpsggn svssgssvss tsldtlytss spsepgsscs
      241 ptpppvprrg thttvsqvqp ppskasapep paeeevatgt tsasddleal gtlslgttee
      301 kaaaeaavpr tigaelmelv rrntglshel crvaigiivg hiqasvpass pvmeqvllsl
      361 vegkdlsmal psgqvchdqq rlevifadla rrkddaqqrs walyedegvi rcyleellhi
      421 ltdadpevck kmckrnefes vlalvayyqm ehraslrlll lkcfgamcsl daaiistlvs
      481 svlpvelard mqtdtqdhqk lcysalilam vfsmgeavpy ahyehlgtpf aqfllnived
      541 glpldtteql pdlcvnllla lnlhlpaadq nvimaalskh anvkifsekl llllnrgddp
      601 vrifkhepqp phsvlkflqd vfgspataai fyhtdmmali ditvrhiadl spgdklrmey
      661 lslmhaivrt tpylqhrhrl pdlqailrri lneeetspqc qmdrmivrem ckeflvlgea
      721 ps
//
LOCUS       NP_001019837             628 aa            linear   PRI 20-NOV-2025
DEFINITION  SH3 domain-containing kinase-binding protein 1 isoform b [Homo
            sapiens].
ACCESSION   NP_001019837
VERSION     NP_001019837.1
DBSOURCE    REFSEQ: accession NM_001024666.3
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 628)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 628)
  AUTHORS   Salokas,K., Liu,X., Ohman,T., Chowdhury,I., Gawriyski,L.,
            Keskitalo,S. and Varjosalo,M.
  TITLE     Physical and functional interactome atlas of human receptor
            tyrosine kinases
  JOURNAL   EMBO Rep 23 (6), e54041 (2022)
   PUBMED   35384245
REFERENCE   3  (residues 1 to 628)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 628)
  AUTHORS   Ahmed,S.F., Buetow,L., Gabrielsen,M., Lilla,S., Sibbet,G.J.,
            Sumpton,D., Zanivan,S., Hedley,A., Clark,W. and Huang,D.T.
  TITLE     E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis
  JOURNAL   Oncogene 40 (12), 2149-2164 (2021)
   PUBMED   33627783
  REMARK    GeneRIF: E3 ligase-inactivation rewires CBL interactome to elicit
            oncogenesis by hijacking RTK-CBL-CIN85 axis.
REFERENCE   5  (residues 1 to 628)
  AUTHORS   Soubeyran,P., Kowanetz,K., Szymkiewicz,I., Langdon,W.Y. and
            Dikic,I.
  TITLE     Cbl-CIN85-endophilin complex mediates ligand-induced downregulation
            of EGF receptors
  JOURNAL   Nature 416 (6877), 183-187 (2002)
   PUBMED   11894095
  REMARK    GeneRIF: Cbl-CIN85-endophilin complex mediates ligand-induced
            downregulation of EGF receptors
            Erratum:[Nature 2002 May 2;417(6884):102]
REFERENCE   6  (residues 1 to 628)
  AUTHORS   Narita,T., Amano,F., Yoshizaki,K., Nishimoto,N., Nishimura,T.,
            Tajima,T., Namiki,H. and Taniyama,T.
  TITLE     Assignment of SH3KBP1 to human chromosome band Xp22.1-->p21.3 by in
            situ hybridization
  JOURNAL   Cytogenet Cell Genet 93 (1-2), 133-134 (2001)
   PUBMED   11474197
REFERENCE   7  (residues 1 to 628)
  AUTHORS   Watanabe,S., Take,H., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Characterization of the CIN85 adaptor protein and identification of
            components involved in CIN85 complexes
  JOURNAL   Biochem Biophys Res Commun 278 (1), 167-174 (2000)
   PUBMED   11071869
REFERENCE   8  (residues 1 to 628)
  AUTHORS   Gout,I., Middleton,G., Adu,J., Ninkina,N.N., Drobot,L.B.,
            Filonenko,V., Matsuka,G., Davies,A.M., Waterfield,M. and
            Buchman,V.L.
  TITLE     Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein
  JOURNAL   EMBO J 19 (15), 4015-4025 (2000)
   PUBMED   10921882
REFERENCE   9  (residues 1 to 628)
  AUTHORS   Take,H., Watanabe,S., Takeda,K., Yu,Z.X., Iwata,N. and Kajigaya,S.
  TITLE     Cloning and characterization of a novel adaptor protein, CIN85,
            that interacts with c-Cbl
  JOURNAL   Biochem Biophys Res Commun 268 (2), 321-328 (2000)
   PUBMED   10679202
REFERENCE   10 (residues 1 to 628)
  AUTHORS   Salvatore,P., Hanash,C.R., Kido,Y., Imai,Y. and Accili,D.
  TITLE     Identification of sirm, a novel insulin-regulated SH3 binding
            protein that associates with Grb-2 and FYN
  JOURNAL   J Biol Chem 273 (12), 6989-6997 (1998)
   PUBMED   9507006
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DC409010.1, AF542051.1 and
            AL732423.12.
            
            Summary: This gene encodes an adapter protein that contains one or
            more N-terminal Src homology domains, a proline rich region and a
            C-terminal coiled-coil domain. The encoded protein facilitates
            protein-protein interactions and has been implicated in numerous
            cellular processes including apoptosis, cytoskeletal rearrangement,
            cell adhesion and in the regulation of clathrin-dependent
            endocytosis. Alternate splicing results in multiple transcript
            variants encoding distinct isoforms. [provided by RefSeq, Jul
            2017].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF542051.1, SRR1803615.88178.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..628
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22.12"
     Protein         1..628
                     /product="SH3 domain-containing kinase-binding protein 1
                     isoform b"
                     /note="Src family kinase-binding protein 1; src-related
                     kinase binding protein-1; CD2-binding protein 3;
                     migration-inducing gene 18; c-Cbl-interacting protein;
                     cbl-interacting protein of 85 kDa; SH3-domain kinase
                     binding protein 1; human Src family kinase-binding protein
                     1"
                     /calculated_mol_wt=68419
     Region          65..117
                     /region_name="SH3_CIN85_2"
                     /note="Second Src Homology 3 domain (SH3B) of
                     Cbl-interacting protein of 85 kDa; cd12055"
                     /db_xref="CDD:212988"
     Site            order(69..75,79,83..84,96..98,108..109,111,113..114)
                     /site_type="other"
                     /note="putative ubiquitin interaction site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Site            order(70,72,75,79,96..98,109,111,113..114)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212988"
     Region          234..289
                     /region_name="SH3_CIN85_3"
                     /note="Third Src Homology 3 domain (SH3C) of
                     Cbl-interacting protein of 85 kDa; cd12057"
                     /db_xref="CDD:212990"
     Site            order(238..245,247..248,252..253,266..269,279..280,282,
                     284..285,287)
                     /site_type="other"
                     /note="ubiquitin interaction site [polypeptide binding]"
                     /db_xref="CDD:212990"
     Site            order(239,241,244,248,267..269,280,282,284..285)
                     /site_type="other"
                     /note="putative peptide ligand binding site [polypeptide
                     binding]"
                     /db_xref="CDD:212990"
     CDS             1..628
                     /gene="SH3KBP1"
                     /gene_synonym="AGMX2; CD2BP3; CIN85; GIG10; HSB-1; HSB1;
                     IMD61; MIG18"
                     /coded_by="NM_001024666.3:90..1976"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS35213.1"
                     /db_xref="GeneID:30011"
                     /db_xref="HGNC:HGNC:13867"
                     /db_xref="MIM:300374"
ORIGIN      
        1 mevsaakaps aadlseieik kemkkdpltn kapekplhev psgnsllsse tilrtnkrge
       61 rrrrrcqvaf sylpqnddel elkvgdiiev vgeveegwwe gvlngktgmf psnfikelsg
      121 esdelgisqd eqlsksslre ttgsesdggd ssstksegan gtvataaiqp kkvkgvgfgd
      181 ifkdkpiklr prsievendf lpvektigkk lpattatpds sktemdsrtk skdyckvifp
      241 yeaqnddelt ikegdivtli nkdcidvgww egelngrrgv fpdnfvkllp pdfekegnrp
      301 kkppppsapv ikqgagtter kheikkippe rpemlpnrte ekerperepk ldlqkpsvpa
      361 ippkkprppk tnslsrpgal pprrperpvg plthtrgdsp kidlagssls gildkdlsdr
      421 sndidlegfd svvsstekls hpttsrpkat grrppsqslt ssslsspdif dspspeedke
      481 ehislahrgv daskktsktv tisqvsdnka slppkpgtma aggggpapls saapsplsss
      541 lgtaghrans pslfgtegkp kmepaassqa aveelrtqvr elrsiietmk dqqkreikql
      601 lseldeekki rlrlqmevnd ikkalqsk
//
LOCUS       NP_002444                727 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor IF-2, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_002444
VERSION     NP_002444.2
DBSOURCE    REFSEQ: accession NM_002453.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Remes,C., Khawaja,A., Pearce,S.F., Dinan,A.M., Gopalakrishna,S.,
            Cipullo,M., Kyriakidis,V., Zhang,J., Dopico,X.C., Yukhnovets,O.,
            Atanassov,I., Firth,A.E., Cooperman,B. and Rorbach,J.
  TITLE     Translation initiation of leaderless and polycistronic transcripts
            in mammalian mitochondria
  JOURNAL   Nucleic Acids Res 51 (2), 891-907 (2023)
   PUBMED   36629253
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Xu,D., Wang,Y., Wu,J., Zhang,Z., Chen,J., Xie,M., Tang,R.,
            Cheng,C., Chen,L., Lin,S., Luo,X. and Zheng,J.
  TITLE     MTIF2 impairs 5 fluorouracil-mediated immunogenic cell death in
            hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance
  JOURNAL   Pharmacol Res 163, 105265 (2021)
   PUBMED   33129983
  REMARK    GeneRIF: MTIF2 impairs 5 fluorouracil-mediated immunogenic cell
            death in hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance.
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Gelernter,J., Kranzler,H.R., Sherva,R., Almasy,L., Koesterer,R.,
            Smith,A.H., Anton,R., Preuss,U.W., Ridinger,M., Rujescu,D.,
            Wodarz,N., Zill,P., Zhao,H. and Farrer,L.A.
  TITLE     Genome-wide association study of alcohol dependence:significant
            findings in African- and European-Americans including novel risk
            loci
  JOURNAL   Mol Psychiatry 19 (1), 41-49 (2014)
   PUBMED   24166409
  REMARK    GeneRIF: This study identified a novel GWS association (1.17 x
            10(-10)) mapped to chromosome 2 at rs1437396, between MTIF2 and
            CCDC88A, across all of the EA and AA cohorts.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Overman,R.G. Jr., Enderle,P.J., Farrow,J.M. 3rd, Wiley,J.E. and
            Farwell,M.A.
  TITLE     The human mitochondrial translation initiation factor 2 gene
            (MTIF2): transcriptional analysis and identification of a
            pseudogene
  JOURNAL   Biochim Biophys Acta 1628 (3), 195-205 (2003)
   PUBMED   12932832
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Koc,E.C. and Spremulli,L.L.
  TITLE     Identification of mammalian mitochondrial translational initiation
            factor 3 and examination of its role in initiation complex
            formation with natural mRNAs
  JOURNAL   J Biol Chem 277 (38), 35541-35549 (2002)
   PUBMED   12095986
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Bonner,D.S., Wiley,J.E. and Farwell,M.A.
  TITLE     Assignment1 of the mitochondrial translational initiation factor 2
            gene (MTIF2) to human chromosome 2 bands p16-->p14 by in situ
            hybridization and with somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 80-81 (1998)
   PUBMED   9925935
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Ma,L. and Spremulli,L.L.
  TITLE     Cloning and sequence analysis of the human mitochondrial
            translational initiation factor 2 cDNA
  JOURNAL   J Biol Chem 270 (4), 1859-1865 (1995)
   PUBMED   7829522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961193.1, BC064977.1,
            AF494407.1, BU684812.1 and AC012358.9.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Oct 1, 2004 this sequence version replaced NP_002444.1.
            
            Summary: During the initiation of protein biosynthesis, initiation
            factor-2 (IF-2) promotes the binding of the initiator tRNA to the
            small subunit of the ribosome in a GTP-dependent manner.
            Prokaryotic IF-2 is a single polypeptide, while eukaryotic
            cytoplasmic IF-2 (eIF-2) is a trimeric protein. Bovine liver
            mitochondria contain IF-2(mt), an 85-kD monomeric protein that is
            equivalent to prokaryotic IF-2. The predicted 727-amino acid human
            protein contains a 29-amino acid presequence. Human IF-2(mt) shares
            32 to 38% amino acid sequence identity with yeast IF-2(mt) and
            several prokaryotic IF-2s, with the greatest degree of conservation
            in the G domains of the proteins. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803615.53320.1,
                                           SRR1660803.9403.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000263629.9/
                                                  ENSP00000263629.4
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..727
                     /product="translation initiation factor IF-2,
                     mitochondrial isoform a precursor"
                     /note="IF-2mt; translation initiation factor IF-2,
                     mitochondrial"
                     /calculated_mol_wt=77711
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=3624
     mat_peptide     30..727
                     /product="Translation initiation factor IF-2,
                     mitochondrial. /id=PRO_0000014480"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=77711
     Region          178..720
                     /region_name="InfB"
                     /note="Translation initiation factor IF-2, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0532"
                     /db_xref="CDD:440298"
     Region          187..194
                     /region_name="G1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          212..216
                     /region_name="G2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          234..237
                     /region_name="G3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          288..291
                     /region_name="G4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          324..326
                     /region_name="G5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91YJ5; propagated from
                     UniProtKB/Swiss-Prot (P46199.2)"
     CDS             1..727
                     /gene="MTIF2"
                     /coded_by="NM_002453.3:300..2483"
                     /note="isoform a precursor is encoded by transcript
                     variant 2"
                     /db_xref="CCDS:CCDS1853.1"
                     /db_xref="GeneID:4528"
                     /db_xref="HGNC:HGNC:7441"
                     /db_xref="MIM:603766"
ORIGIN      
        1 mnqkllklen llrfhtiyrq lhslcqrral rqwrhgfssa ypvwtaqlca wpwptdvltg
       61 aalsqyrllv tkkeegpwks qlsstkskkv vevwigmtie elarameknt dyvyeallnt
      121 dididslead shldevwike vitkagmklk wsklkqdkvr knkdavrrpq adpalltprs
      181 pvvtimghvd hgkttlldkf rktqvaavet ggitqhigaf lvslpsgeki tfldtpghaa
      241 fsamrargaq vtdivvlvva addgvmkqtv esiqhakdaq vpiilavnkc dkaeadpekv
      301 kkellaydvv cedyggdvqa vpvsaltgdn lmalaeatva laemlelkad pngpvegtvi
      361 esftdkgrgl vttaiiqrgt lrkgsvlvag kcwakvrlmf dengktidea ypsmpvgitg
      421 wrdlpsagee ilevesepra revvdwrkye qeqekgqedl kiieekrkeh keahqkarek
      481 yghllwkkrs ilrflerkeq iplkpkekre rdsnvlsvii kgdvdgsvea ilniidtyda
      541 shecelelvh fgvgdvsand vnlaetfdgv iygfnvnagn viqqsaakkg vkiklhkiiy
      601 rlvedlqeel ssrlpcavee hpvgeasila tfsvtegkkk vpvagcrvqk gqlekqkkfk
      661 ltrnghviwk gsltslkhhk ddisivktgm dcglsldedn mefqvgdriv cyeekqiqak
      721 tswdpgf
//
LOCUS       NP_001307930             727 aa            linear   PRI 20-NOV-2025
DEFINITION  translation initiation factor IF-2, mitochondrial isoform a
            precursor [Homo sapiens].
ACCESSION   NP_001307930 XP_011531170
VERSION     NP_001307930.1
DBSOURCE    REFSEQ: accession NM_001321001.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 727)
  AUTHORS   Remes,C., Khawaja,A., Pearce,S.F., Dinan,A.M., Gopalakrishna,S.,
            Cipullo,M., Kyriakidis,V., Zhang,J., Dopico,X.C., Yukhnovets,O.,
            Atanassov,I., Firth,A.E., Cooperman,B. and Rorbach,J.
  TITLE     Translation initiation of leaderless and polycistronic transcripts
            in mammalian mitochondria
  JOURNAL   Nucleic Acids Res 51 (2), 891-907 (2023)
   PUBMED   36629253
REFERENCE   2  (residues 1 to 727)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   3  (residues 1 to 727)
  AUTHORS   Xu,D., Wang,Y., Wu,J., Zhang,Z., Chen,J., Xie,M., Tang,R.,
            Cheng,C., Chen,L., Lin,S., Luo,X. and Zheng,J.
  TITLE     MTIF2 impairs 5 fluorouracil-mediated immunogenic cell death in
            hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance
  JOURNAL   Pharmacol Res 163, 105265 (2021)
   PUBMED   33129983
  REMARK    GeneRIF: MTIF2 impairs 5 fluorouracil-mediated immunogenic cell
            death in hepatocellular carcinoma in vivo: Molecular mechanisms and
            therapeutic significance.
REFERENCE   4  (residues 1 to 727)
  AUTHORS   Gelernter,J., Kranzler,H.R., Sherva,R., Almasy,L., Koesterer,R.,
            Smith,A.H., Anton,R., Preuss,U.W., Ridinger,M., Rujescu,D.,
            Wodarz,N., Zill,P., Zhao,H. and Farrer,L.A.
  TITLE     Genome-wide association study of alcohol dependence:significant
            findings in African- and European-Americans including novel risk
            loci
  JOURNAL   Mol Psychiatry 19 (1), 41-49 (2014)
   PUBMED   24166409
  REMARK    GeneRIF: This study identified a novel GWS association (1.17 x
            10(-10)) mapped to chromosome 2 at rs1437396, between MTIF2 and
            CCDC88A, across all of the EA and AA cohorts.
REFERENCE   5  (residues 1 to 727)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 727)
  AUTHORS   Bouwmeester,T., Bauch,A., Ruffner,H., Angrand,P.O., Bergamini,G.,
            Croughton,K., Cruciat,C., Eberhard,D., Gagneur,J., Ghidelli,S.,
            Hopf,C., Huhse,B., Mangano,R., Michon,A.M., Schirle,M., Schlegl,J.,
            Schwab,M., Stein,M.A., Bauer,A., Casari,G., Drewes,G., Gavin,A.C.,
            Jackson,D.B., Joberty,G., Neubauer,G., Rick,J., Kuster,B. and
            Superti-Furga,G.
  TITLE     A physical and functional map of the human TNF-alpha/NF-kappa B
            signal transduction pathway
  JOURNAL   Nat Cell Biol 6 (2), 97-105 (2004)
   PUBMED   14743216
  REMARK    Erratum:[Nat Cell Biol. 2004 May;6(5):465]
REFERENCE   7  (residues 1 to 727)
  AUTHORS   Overman,R.G. Jr., Enderle,P.J., Farrow,J.M. 3rd, Wiley,J.E. and
            Farwell,M.A.
  TITLE     The human mitochondrial translation initiation factor 2 gene
            (MTIF2): transcriptional analysis and identification of a
            pseudogene
  JOURNAL   Biochim Biophys Acta 1628 (3), 195-205 (2003)
   PUBMED   12932832
REFERENCE   8  (residues 1 to 727)
  AUTHORS   Koc,E.C. and Spremulli,L.L.
  TITLE     Identification of mammalian mitochondrial translational initiation
            factor 3 and examination of its role in initiation complex
            formation with natural mRNAs
  JOURNAL   J Biol Chem 277 (38), 35541-35549 (2002)
   PUBMED   12095986
REFERENCE   9  (residues 1 to 727)
  AUTHORS   Bonner,D.S., Wiley,J.E. and Farwell,M.A.
  TITLE     Assignment1 of the mitochondrial translational initiation factor 2
            gene (MTIF2) to human chromosome 2 bands p16-->p14 by in situ
            hybridization and with somatic cell hybrids
  JOURNAL   Cytogenet Cell Genet 83 (1-2), 80-81 (1998)
   PUBMED   9925935
REFERENCE   10 (residues 1 to 727)
  AUTHORS   Ma,L. and Spremulli,L.L.
  TITLE     Cloning and sequence analysis of the human mitochondrial
            translational initiation factor 2 cDNA
  JOURNAL   J Biol Chem 270 (4), 1859-1865 (1995)
   PUBMED   7829522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB961193.1, AF494407.1,
            AC012358.9 and BU681583.1.
            
            On Mar 12, 2016 this sequence version replaced XP_011531170.1.
            
            Summary: During the initiation of protein biosynthesis, initiation
            factor-2 (IF-2) promotes the binding of the initiator tRNA to the
            small subunit of the ribosome in a GTP-dependent manner.
            Prokaryotic IF-2 is a single polypeptide, while eukaryotic
            cytoplasmic IF-2 (eIF-2) is a trimeric protein. Bovine liver
            mitochondria contain IF-2(mt), an 85-kD monomeric protein that is
            equivalent to prokaryotic IF-2. The predicted 727-amino acid human
            protein contains a 29-amino acid presequence. Human IF-2(mt) shares
            32 to 38% amino acid sequence identity with yeast IF-2(mt) and
            several prokaryotic IF-2s, with the greatest degree of conservation
            in the G domains of the proteins. [provided by RefSeq, Mar 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.19781.1,
                                           SRR1803616.255461.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..727
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p16.1"
     Protein         1..727
                     /product="translation initiation factor IF-2,
                     mitochondrial isoform a precursor"
                     /note="IF-2mt; translation initiation factor IF-2,
                     mitochondrial"
                     /calculated_mol_wt=77711
     transit_peptide 1..29
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=3624
     mat_peptide     30..727
                     /product="Translation initiation factor IF-2,
                     mitochondrial. /id=PRO_0000014480"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
                     /calculated_mol_wt=77711
     Region          178..720
                     /region_name="InfB"
                     /note="Translation initiation factor IF-2, a GTPase
                     [Translation, ribosomal structure and biogenesis];
                     COG0532"
                     /db_xref="CDD:440298"
     Region          187..194
                     /region_name="G1. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          212..216
                     /region_name="G2. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          234..237
                     /region_name="G3. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          288..291
                     /region_name="G4. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Region          324..326
                     /region_name="G5. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P46199.2)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q91YJ5; propagated from
                     UniProtKB/Swiss-Prot (P46199.2)"
     CDS             1..727
                     /gene="MTIF2"
                     /coded_by="NM_001321001.1:273..2456"
                     /note="isoform a precursor is encoded by transcript
                     variant 3"
                     /db_xref="CCDS:CCDS1853.1"
                     /db_xref="GeneID:4528"
                     /db_xref="HGNC:HGNC:7441"
                     /db_xref="MIM:603766"
ORIGIN      
        1 mnqkllklen llrfhtiyrq lhslcqrral rqwrhgfssa ypvwtaqlca wpwptdvltg
       61 aalsqyrllv tkkeegpwks qlsstkskkv vevwigmtie elarameknt dyvyeallnt
      121 dididslead shldevwike vitkagmklk wsklkqdkvr knkdavrrpq adpalltprs
      181 pvvtimghvd hgkttlldkf rktqvaavet ggitqhigaf lvslpsgeki tfldtpghaa
      241 fsamrargaq vtdivvlvva addgvmkqtv esiqhakdaq vpiilavnkc dkaeadpekv
      301 kkellaydvv cedyggdvqa vpvsaltgdn lmalaeatva laemlelkad pngpvegtvi
      361 esftdkgrgl vttaiiqrgt lrkgsvlvag kcwakvrlmf dengktidea ypsmpvgitg
      421 wrdlpsagee ilevesepra revvdwrkye qeqekgqedl kiieekrkeh keahqkarek
      481 yghllwkkrs ilrflerkeq iplkpkekre rdsnvlsvii kgdvdgsvea ilniidtyda
      541 shecelelvh fgvgdvsand vnlaetfdgv iygfnvnagn viqqsaakkg vkiklhkiiy
      601 rlvedlqeel ssrlpcavee hpvgeasila tfsvtegkkk vpvagcrvqk gqlekqkkfk
      661 ltrnghviwk gsltslkhhk ddisivktgm dcglsldedn mefqvgdriv cyeekqiqak
      721 tswdpgf
//
LOCUS       NP_001278531              99 aa            linear   PRI 20-NOV-2025
DEFINITION  dynein light chain Tctex-type 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001278531 XP_005267174
VERSION     NP_001278531.1
DBSOURCE    REFSEQ: accession NM_001291602.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   He,S., Gillies,J.P., Zang,J.L., Cordoba-Beldad,C.M., Yamamoto,I.,
            Fujiwara,Y., Grantham,J., DeSantis,M.E. and Shibuya,H.
  TITLE     Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 regulate
            mitotic and male meiotic spindle bipolarity
  JOURNAL   Nat Commun 14 (1), 1715 (2023)
   PUBMED   36973253
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Canty,J.T., Tan,R., Kusakci,E., Fernandes,J. and Yildiz,A.
  TITLE     Structure and Mechanics of Dynein Motors
  JOURNAL   Annu Rev Biophys 50, 549-574 (2021)
   PUBMED   33957056
  REMARK    Review article
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Schwarzer,C., Barnikol-Watanabe,S., Thinnes,F.P. and Hilschmann,N.
  TITLE     Voltage-dependent anion-selective channel (VDAC) interacts with the
            dynein light chain Tctex1 and the heat-shock protein PBP74
  JOURNAL   Int J Biochem Cell Biol 34 (9), 1059-1070 (2002)
   PUBMED   12009301
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Mueller,S., Cao,X., Welker,R. and Wimmer,E.
  TITLE     Interaction of the poliovirus receptor CD155 with the dynein light
            chain Tctex-1 and its implication for poliovirus pathogenesis
  JOURNAL   J Biol Chem 277 (10), 7897-7904 (2002)
   PUBMED   11751937
  REMARK    GeneRIF: Association with Tctex-1 and, hence, with the dynein motor
            complex may offer an explanation for how poliovirus hijacks the
            cellular transport machinery to retrogradely ascend along the axon
            to the neuronal cell body.
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Strovel,E.T., Wu,D. and Sussman,D.J.
  TITLE     Protein phosphatase 2Calpha dephosphorylates axin and activates
            LEF-1-dependent transcription
  JOURNAL   J Biol Chem 275 (4), 2399-2403 (2000)
   PUBMED   10644691
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Nagano,F., Orita,S., Sasaki,T., Naito,A., Sakaguchi,G., Maeda,M.,
            Watanabe,T., Kominami,E., Uchiyama,Y. and Takai,Y.
  TITLE     Interaction of Doc2 with tctex-1, a light chain of cytoplasmic
            dynein. Implication in dynein-dependent vesicle transport
  JOURNAL   J Biol Chem 273 (46), 30065-30068 (1998)
   PUBMED   9804756
REFERENCE   9  (residues 1 to 99)
  AUTHORS   King,S.M., Dillman,J.F. 3rd, Benashski,S.E., Lye,R.J.,
            Patel-King,R.S. and Pfister,K.K.
  TITLE     The mouse t-complex-encoded protein Tctex-1 is a light chain of
            brain cytoplasmic dynein
  JOURNAL   J Biol Chem 271 (50), 32281-32287 (1996)
   PUBMED   8943288
REFERENCE   10 (residues 1 to 99)
  AUTHORS   Watanabe,T.K., Fujiwara,T., Shimizu,F., Okuno,S., Suzuki,M.,
            Takahashi,E., Nakamura,Y. and Hirai,Y.
  TITLE     Cloning, expression, and mapping of TCTEL1, a putative human
            homologue of murine Tcte1, to 6q
  JOURNAL   Cytogenet Cell Genet 73 (1-2), 153-156 (1996)
   PUBMED   8646886
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY171700.1, HY017024.1 and
            BU675683.1.
            
            On Apr 23, 2014 this sequence version replaced XP_005267174.1.
            
            Summary: This gene encodes a component of the motor complex,
            cytoplasmic dynein, which transports cellular cargo along
            microtubules in the cell. The encoded protein regulates the length
            of primary cilia which are sensory organelles found on the surface
            of cells. The protein encoded by this gene interacts with viral
            proteins, like the minor capsid protein L2 of human papillomavirus,
            and is required for dynein-mediated delivery of the viral nucleic
            acid to the host nucleus. This protein interacts with oncogenic
            nucleoporins to disrupt gene regulation and cause leukemic
            transformation. Pseudogenes of this gene are present on chromosomes
            4 and 17. Alternative splicing results in multiple transcript
            variants encoding different isoforms. [provided by RefSeq, Apr
            2014].
            
            Transcript Variant: This variant (2) lacks an in-frame exon in the
            5' coding region compared to variant 1. The encoded isoform (2) is
            shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: ERR279827.1652.1,
                                           DRR138524.1269894.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q25.3"
     Protein         1..99
                     /product="dynein light chain Tctex-type 1 isoform 2"
                     /note="t-complex-associated-testis-expressed 1-like 1;
                     T-complex testis-specific protein 1 homolog"
                     /calculated_mol_wt=10789
     Region          8..99
                     /region_name="DLC-like_DYNLT1"
                     /note="dynein light chain (DLC)-like domain found in
                     dynein light chain Tctex-type 1 (DYNLT1) and similar
                     proteins; cd21462"
                     /db_xref="CDD:412010"
     Site            order(48,50..56,60..70,72,76,95,97)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:412010"
     CDS             1..99
                     /gene="DYNLT1"
                     /gene_synonym="CW-1; TCTEL1; tctex-1; TCTEX1"
                     /coded_by="NM_001291602.2:36..335"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:6993"
                     /db_xref="HGNC:HGNC:11697"
                     /db_xref="MIM:601554"
ORIGIN      
        1 medyqaaeea iesaiggnay qhskvnqwtt nvveqtlsql tklgkpfkyi vtcvimqkng
       61 aglhtasscf wdsstdgsct vrwenktmyc ivsafglsi
//
LOCUS       NP_001156806             752 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptotagmin-like protein 5 isoform 2 [Homo sapiens].
ACCESSION   NP_001156806
VERSION     NP_001156806.1
DBSOURCE    REFSEQ: accession NM_001163334.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 752)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Huang,D., Zeng,Y., Deng,H.Y., Fu,B.D., Ke,Y., Luo,J.Y., Yu,J.C. and
            Yu,S.T.
  TITLE     SYTL5 Promotes Papillary Thyroid Carcinoma Progression by Enhancing
            Activation of the NF-kappaB Signaling Pathway
  JOURNAL   Endocrinology 164 (1) (2022)
   PUBMED   36378561
  REMARK    GeneRIF: SYTL5 Promotes Papillary Thyroid Carcinoma Progression by
            Enhancing Activation of the NF-kappaB Signaling Pathway.
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Wade,T.D., Gordon,S., Medland,S., Bulik,C.M., Heath,A.C.,
            Montgomery,G.W. and Martin,N.G.
  TITLE     Genetic variants associated with disordered eating
  JOURNAL   Int J Eat Disord 46 (6), 594-608 (2013)
   PUBMED   23568457
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Kerns,S.L., Ostrer,H., Stock,R., Li,W., Moore,J., Pearlman,A.,
            Campbell,C., Shao,Y., Stone,N., Kusnetz,L. and Rosenstein,B.S.
  TITLE     Genome-wide association study to identify single nucleotide
            polymorphisms (SNPs) associated with the development of erectile
            dysfunction in African-American men after radiotherapy for prostate
            cancer
  JOURNAL   Int J Radiat Oncol Biol Phys 78 (5), 1292-1300 (2010)
   PUBMED   20932654
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Colvin,R.A., Means,T.K., Diefenbach,T.J., Moita,L.F., Friday,R.P.,
            Sever,S., Campanella,G.S., Abrazinski,T., Manice,L.A., Moita,C.,
            Andrews,N.W., Wu,D., Hacohen,N. and Luster,A.D.
  TITLE     Synaptotagmin-mediated vesicle fusion regulates cell migration
  JOURNAL   Nat Immunol 11 (6), 495-502 (2010)
   PUBMED   20473299
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Saxena,S.K., Horiuchi,H. and Fukuda,M.
  TITLE     Rab27a regulates epithelial sodium channel (ENaC) activity through
            synaptotagmin-like protein (SLP-5) and Munc13-4 effector mechanism
  JOURNAL   Biochem Biophys Res Commun 344 (2), 651-657 (2006)
   PUBMED   16630545
  REMARK    GeneRIF: These observations decisively prove that Rab27a inhibits
            ENaC function through a complex mechanism that involves GTP/GDP
            status, and protein-protein interactions involving Munc13-4 and
            SLP-5 effector proteins.
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Kuroda,T.S., Fukuda,M., Ariga,H. and Mikoshiba,K.
  TITLE     Synaptotagmin-like protein 5: a novel Rab27A effector with
            C-terminal tandem C2 domains
  JOURNAL   Biochem Biophys Res Commun 293 (3), 899-906 (2002)
   PUBMED   12051743
  REMARK    GeneRIF: molecular cloning of slp5:a novel Rab27A effector with
            C-terminal tandem C2 domains
            GeneRIF: Synaptotagmin-like protein 5 (Slp5) contains an N-terminal
            Slp homology domain (SHD) (PMID: 11327731). The SHD of Slp5
            specifically and directly binds the GTP-bound form of Rab27A.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK125106.1, BC131585.1,
            BX647688.1 and AL135038.1.
            
            Summary: The protein encoded by this gene belongs to the
            synaptotagmin-like (Slp) protein family, which contains a unique
            homology domain at the N-terminus, referred to as the Slp homology
            domain (SHD). The SHD functions as a binding site for Rab27A, which
            plays a role in protein transport. Expression of this gene is
            restricted to placenta and liver, suggesting that it might be
            involved in Rab27A-dependent membrane trafficking in specific
            tissues. Alternatively spliced transcript variants encoding
            different isoforms have been found for this gene. [provided by
            RefSeq, Sep 2009].
            
            Transcript Variant: This variant (3) contains an in-frame coding
            exon missing in variant 1, resulting in a longer isoform (2) with
            an additional 22 aa protein segment compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC131585.1, SRR1803611.154386.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2154361
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.4"
     Protein         1..752
                     /product="synaptotagmin-like protein 5 isoform 2"
                     /note="exophilin 9; synaptotagmin-like protein 5"
                     /calculated_mol_wt=83788
     Region          11..123
                     /region_name="PHD_SF"
                     /note="PHD finger superfamily; cl22851"
                     /db_xref="CDD:473978"
     Region          62..108
                     /region_name="FYVE_Slp5"
                     /note="FYVE-related domain found in synaptotagmin-like
                     protein 5 (Slp5) and similar proteins; cd15766"
                     /db_xref="CDD:277305"
     Region          <218..>376
                     /region_name="AF-4"
                     /note="AF-4 proto-oncoprotein N-terminal region;
                     pfam05110"
                     /db_xref="CDD:461550"
     Region          429..552
                     /region_name="C2A_SLP-4_5"
                     /note="C2 domain first repeat present in
                     Synaptotagmin-like proteins 4 and 5; cd04029"
                     /db_xref="CDD:175995"
     Region          566..744
                     /region_name="C2B_SLP_1-2-3-4"
                     /note="C2 domain second repeat present in
                     Synaptotagmin-like proteins 1-4; cd04020"
                     /db_xref="CDD:175987"
     CDS             1..752
                     /gene="SYTL5"
                     /gene_synonym="slp5"
                     /coded_by="NM_001163334.1:357..2615"
                     /note="isoform 2 is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS55399.1"
                     /db_xref="GeneID:94122"
                     /db_xref="HGNC:HGNC:15589"
                     /db_xref="MIM:301126"
ORIGIN      
        1 msknsefinl sflldhekem ilgvlkrdey lkkvedkrir klknelleak rrsgktqqea
       61 srvcvhchrn lglifdrgdp cqacslrvcr ecrvagpngs wkctvcdkia qlriitgewf
      121 feekakrfkq vnvlgtdvvr qsilrrspga eevqsqeqtr qdaeksdtsp vagkkashdg
      181 pkrkgfllsk frsatrgeii tpktdtgrsy sldldgqhfr slksppgsdr gstgssdlnd
      241 qepgprtpks srsngvtpgt qsspapstrt vtsvisreyg fensmdlaai egtsqeltks
      301 hrrntsgtps iavsgtslss dqsrseldls esftedsedt vsirsksvpg aldkdsleet
      361 eesidalvss qlstnthrla sglstssqag sdrkwtylnv pdadsdttsl nsmmsvyset
      421 gdygnvkvsg eillhisycy ktgglyifvk ncrnlaigde kkqrtdayvk syllpdksrn
      481 nkrktkirtg tnpefnetlk ytishtqlet rtlqlsvwhy drfgrnsflg eveipfdswn
      541 fenptdewfv lqpkvefapd iglqykgelt vvlryippee nlmlppeqlq gnktfkkgkk
      601 kespvisggi levfikeakn ltavksggts dsfvkgyllp ddskatkhkt lvikksvnpq
      661 wnhtfmfsgi hpqdiknvcl eltiwdkeaf ssniflggvr lnsgsgvshg knvdwmdsqg
      721 eeqrlwqkma nnpgtpfegv lmlrssmgkc rl
//
LOCUS       NP_036262                239 aa            linear   PRI 20-NOV-2025
DEFINITION  claudin-14 [Homo sapiens].
ACCESSION   NP_036262
VERSION     NP_036262.1
DBSOURCE    REFSEQ: accession NM_012130.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 239)
  AUTHORS   Mohanty,S., White,J.K., Scheffschick,A., Fischer,B., Pathak,A.,
            Tovi,J., Ostenson,C.G., Aspenstrom,P., Brauner,H. and Brauner,A.
  TITLE     Diabetes compromises tight junction protein claudin 14 in the
            urinary bladder
  JOURNAL   Cell Tissue Res 398 (1), 27-33 (2024)
   PUBMED   39162877
  REMARK    GeneRIF: Diabetes compromises tight junction protein claudin 14 in
            the urinary bladder.
REFERENCE   2  (residues 1 to 239)
  AUTHORS   Mizukami,Y., Ito,A., Hashimoto,S., Ando,T., Ishikawa,Y., Eguchi,H.,
            Yoshino,Y., Matsunaga,T. and Ikari,A.
  TITLE     Downregulation of chemoresistance by claudin-14 silencing in human
            colorectal cancer cells
  JOURNAL   Arch Biochem Biophys 758, 110075 (2024)
   PUBMED   38942107
  REMARK    GeneRIF: Downregulation of chemoresistance by claudin-14 silencing
            in human colorectal cancer cells.
REFERENCE   3  (residues 1 to 239)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 239)
  AUTHORS   Khatami,F., Gorji,A., Khoshchehreh,M., Mashhadi,R., Pishkuhi,M.A.,
            Khajavi,A., Shabestari,A.N. and Aghamir,S.M.K.
  TITLE     The correlation between promoter hypermethylation of VDR, CLDN, and
            CasR genes and recurrent stone formation
  JOURNAL   BMC Med Genomics 15 (1), 109 (2022)
   PUBMED   35546405
  REMARK    GeneRIF: The correlation between promoter hypermethylation of VDR,
            CLDN, and CasR genes and recurrent stone formation.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 239)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 239)
  AUTHORS   Tsukita,S., Furuse,M. and Itoh,M.
  TITLE     Multifunctional strands in tight junctions
  JOURNAL   Nat Rev Mol Cell Biol 2 (4), 285-293 (2001)
   PUBMED   11283726
  REMARK    Review article
REFERENCE   7  (residues 1 to 239)
  AUTHORS   Heiskala,M., Peterson,P.A. and Yang,Y.
  TITLE     The roles of claudin superfamily proteins in paracellular transport
  JOURNAL   Traffic 2 (2), 93-98 (2001)
   PUBMED   11247307
  REMARK    Review article
REFERENCE   8  (residues 1 to 239)
  AUTHORS   Wilcox,E.R., Burton,Q.L., Naz,S., Riazuddin,S., Smith,T.N.,
            Ploplis,B., Belyantseva,I., Ben-Yosef,T., Liburd,N.A., Morell,R.J.,
            Kachar,B., Wu,D.K., Griffith,A.J., Riazuddin,S. and Friedman,T.B.
  TITLE     Mutations in the gene encoding tight junction claudin-14 cause
            autosomal recessive deafness DFNB29
  JOURNAL   Cell 104 (1), 165-172 (2001)
   PUBMED   11163249
REFERENCE   9  (residues 1 to 239)
  AUTHORS   Kniesel,U. and Wolburg,H.
  TITLE     Tight junctions of the blood-brain barrier
  JOURNAL   Cell Mol Neurobiol 20 (1), 57-76 (2000)
   PUBMED   10690502
  REMARK    Review article
REFERENCE   10 (residues 1 to 239)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AP000695.1, AY355349.1 and
            BC012126.1.
            
            Summary: Tight junctions represent one mode of cell-to-cell
            adhesion in epithelial or endothelial cell sheets, forming
            continuous seals around cells and serving as a physical barrier to
            prevent solutes and water from passing freely through the
            paracellular space. These junctions are comprised of sets of
            continuous networking strands in the outwardly facing cytoplasmic
            leaflet, with complementary grooves in the inwardly facing
            extracytoplasmic leaflet. The protein encoded by this gene, a
            member of the claudin family, is an integral membrane protein and a
            component of tight junction strands. The encoded protein also binds
            specifically to the WW domain of Yes-associated protein. Defects in
            this gene are the cause of an autosomal recessive form of
            nonsyndromic sensorineural deafness. It is also reported that four
            synonymous variants in this gene are associated with kidney stones
            and reduced bone mineral density. Several transcript variants
            encoding the same protein have been found for this gene. [provided
            by RefSeq, Jun 2010].
            
            Transcript Variant: This variant (epsilon) differs in the 5' UTR
            compared to variant 1. All five variants encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC012126.1, AY355349.1 [ECO:0000332]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..239
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.13"
     Protein         1..239
                     /product="claudin-14"
                     /calculated_mol_wt=25568
     Site            8..28
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Region          23..181
                     /region_name="PMP22_Claudin"
                     /note="PMP-22/EMP/MP20/Claudin family; cl21598"
                     /db_xref="CDD:473919"
     Site            82..102
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Site            116..136
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Site            163..183
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     Region          196..228
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O95500.1)"
     CDS             1..239
                     /gene="CLDN14"
                     /gene_synonym="DFNB29"
                     /coded_by="NM_012130.4:183..902"
                     /db_xref="CCDS:CCDS13645.1"
                     /db_xref="GeneID:23562"
                     /db_xref="HGNC:HGNC:2035"
                     /db_xref="MIM:605608"
ORIGIN      
        1 mastavqllg fllsflgmvg tlittilphw rrtahvgtni ltavsylkgl wmecvwhstg
       61 iyqcqiyrsl lalpqdlqaa ralmviscll sgiacacavi gmkctrcakg tpakttfail
      121 ggtlfilagl lcmvavswtt ndvvqnfynp llpsgmkfei gqalylgfis sslsliggtl
      181 lclscqdeap yrpyqappra ttttantapa yqppaaykdn rapsvtsath sgyrlndyv
//
LOCUS       NP_002878                660 aa            linear   PRI 20-NOV-2025
DEFINITION  arginine--tRNA ligase, cytoplasmic [Homo sapiens].
ACCESSION   NP_002878 NP_116018
VERSION     NP_002878.2
DBSOURCE    REFSEQ: accession NM_002887.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Li,G., Eriani,G., Wang,E.D. and Zhou,X.L.
  TITLE     Distinct pathogenic mechanisms of various RARS1 mutations in
            Pelizaeus-Merzbacher-like disease
  JOURNAL   Sci China Life Sci 64 (10), 1645-1660 (2021)
   PUBMED   33515434
  REMARK    GeneRIF: Distinct pathogenic mechanisms of various RARS1 mutations
            in Pelizaeus-Merzbacher-like disease.
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Khan,K., Baleanu-Gogonea,C., Willard,B., Gogonea,V. and Fox,P.L.
  TITLE     3-Dimensional architecture of the human multi-tRNA synthetase
            complex
  JOURNAL   Nucleic Acids Res 48 (15), 8740-8754 (2020)
   PUBMED   32644155
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Mendes,M.I., Green,L.M.C., Bertini,E., Tonduti,D., Aiello,C.,
            Smith,D., Salsano,E., Beerepoot,S., Hertecant,J., von Spiczak,S.,
            Livingston,J.H., Emrick,L., Fraser,J., Russell,L., Bernard,G.,
            Magri,S., Di Bella,D., Taroni,F., Koenig,M.K., Moroni,I.,
            Cappuccio,G., Brunetti-Pierri,N., Rhee,J., Mendelsohn,B.A.,
            Helbig,I., Helbig,K., Muhle,H., Ismayl,O., Vanderver,A.L.,
            Salomons,G.S., van der Knaap,M.S. and Wolf,N.I.
  TITLE     RARS1-related hypomyelinating leukodystrophy: Expanding the
            spectrum
  JOURNAL   Ann Clin Transl Neurol 7 (1), 83-93 (2020)
   PUBMED   31814314
  REMARK    GeneRIF: RARS1-related hypomyelinating leukodystrophy: Expanding
            the spectrum.
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Girjes,A.A., Hobson,K., Chen,P. and Lavin,M.F.
  TITLE     Cloning and characterization of cDNA encoding a human arginyl-tRNA
            synthetase
  JOURNAL   Gene 164 (2), 347-350 (1995)
   PUBMED   7590355
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Shiba,K., Suzuki,N., Shigesada,K., Namba,Y., Schimmel,P. and
            Noda,T.
  TITLE     Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence
            of the anticodon-binding domain and acquisition of a new structural
            unit
  JOURNAL   Proc Natl Acad Sci U S A 91 (16), 7435-7439 (1994)
   PUBMED   8052601
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Norcum,M.T.
  TITLE     Structural analysis of the high molecular mass aminoacyl-tRNA
            synthetase complex. Effects of neutral salts and detergents
  JOURNAL   J Biol Chem 266 (23), 15398-15405 (1991)
   PUBMED   1651330
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Wang,H.Y. and Pan,F.
  TITLE     Kinetic mechanism of arginyl-tRNA synthetase from human placenta
  JOURNAL   Int J Biochem 16 (12), 1379-1385 (1984)
   PUBMED   6530022
REFERENCE   10 (residues 1 to 660)
  AUTHORS   McCune,S.A., Yu,P.L. and Nance,W.E.
  TITLE     A genetic study of erythrocyte arginine-tRNA synthetase activity in
            man
  JOURNAL   Acta Genet Med Gemellol (Roma) 26 (1), 21-27 (1977)
   PUBMED   562050
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AU125370.1, BT007394.1,
            BM984528.1 and CA439316.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 13, 2001 this sequence version replaced NP_002878.1.
            
            Summary: Aminoacyl-tRNA synthetases catalyze the aminoacylation of
            tRNA by their cognate amino acid. Because of their central role in
            linking amino acids with nucleotide triplets contained in tRNAs,
            aminoacyl-tRNA synthetases are thought to be among the first
            proteins that appeared in evolution. Arginyl-tRNA synthetase
            belongs to the class-I aminoacyl-tRNA synthetase family. [provided
            by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.1146952.1,
                                           SRR1803616.190698.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000231572.8/ ENSP00000231572.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q34"
     Protein         1..660
                     /product="arginine--tRNA ligase, cytoplasmic"
                     /EC_number="6.1.1.19"
                     /note="arginine tRNA ligase 1, cytoplasmic; arginyl-tRNA
                     synthetase, cytoplasmic"
                     /calculated_mol_wt=75248
     Region          1..72
                     /region_name="Could be involved in the assembly of the
                     multisynthetase complex"
                     /note="propagated from UniProtKB/Swiss-Prot (P54136.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000269|PubMed:37316325,
                     ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (P54136.2)"
     Region          80..660
                     /region_name="PLN02286"
                     /note="arginine-tRNA ligase"
                     /db_xref="CDD:215160"
     Region          201..212
                     /region_name="'HIGH' region"
                     /note="propagated from UniProtKB/Swiss-Prot (P54136.2)"
     Region          529..543
                     /region_name="Interaction with tRNA.
                     /evidence=ECO:0000250|UniProtKB:Q05506"
                     /note="propagated from UniProtKB/Swiss-Prot (P54136.2)"
     CDS             1..660
                     /gene="RARS1"
                     /gene_synonym="ArgRS; DALRD1; HLD9; RARS"
                     /coded_by="NM_002887.4:29..2011"
                     /db_xref="CCDS:CCDS4367.1"
                     /db_xref="GeneID:5917"
                     /db_xref="HGNC:HGNC:9870"
                     /db_xref="MIM:107820"
ORIGIN      
        1 mdvlvsecsa rllqqeeeik sltaeidrlk ncgclgaspn leqlqeenlk lkyrlnilrk
       61 slqaernkpt knminiisrl qevfghaika aypdlenppl lvtpsqqakf gdyqcnsamg
      121 isqmlktkeq kvnpreiaen itkhlpdnec iekveiagpg finvhlrkdf vseqltsllv
      181 ngvqlpalge nkkvivdfss pniakemhvg hlrstiiges isrlfefagy dvlrlnhvgd
      241 wgtqfgmlia hlqdkfpdyl tvsppigdlq vfykeskkrf dteeefkkra yqcvvllqgk
      301 npditkawkl icdvsrqeln kiydaldvsl iergesfyqd rmndivkefe drgfvqvddg
      361 rkivfvpgcs ipltivksdg gytydtsdla aikqrlfeek admiiyvvdn gqsvhfqtif
      421 aaaqmigwyd pkvtrvfhag fgvvlgedkk kfktrsgetv rlmdllgegl krsmdklkek
      481 erdkvltaee lnaaqtsvay gcikyadlsh nrlndyifsf dkmlddrgnt aayllyaftr
      541 irsiarlani deemlqkaar etkilldhek ewklgrcilr fpeilqkild dlflhtlcdy
      601 iyelatafte fydscycvek drqtgkilkv nmwrmllcea vaavmakgfd ilgikpvqrm
//
LOCUS       NP_060848                374 aa            linear   PRI 20-NOV-2025
DEFINITION  F-box/LRR-repeat protein 8 [Homo sapiens].
ACCESSION   NP_060848
VERSION     NP_060848.2
DBSOURCE    REFSEQ: accession NM_018378.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Yao,J., Wang,X.P., Yang,J., Yang,Z. and Zhang,Z.Y.
  TITLE     SCF-FBXL8 contributes to liver metastasis and stem-cell-like
            features in colorectal cancer cells by mediating ubiquitination and
            degradation of TP53
  JOURNAL   Clin Transl Med 13 (3), e1208 (2023)
   PUBMED   36855778
  REMARK    GeneRIF: SCF-FBXL8 contributes to liver metastasis and
            stem-cell-like features in colorectal cancer cells by mediating
            ubiquitination and degradation of TP53.
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Yoshida,A., Choi,J., Jin,H.R., Li,Y., Bajpai,S., Qie,S. and
            Diehl,J.A.
  TITLE     Fbxl8 suppresses lymphoma growth and hematopoietic transformation
            through degradation of cyclin D3
  JOURNAL   Oncogene 40 (2), 292-306 (2021)
   PUBMED   33122824
  REMARK    GeneRIF: Fbxl8 suppresses lymphoma growth and hematopoietic
            transformation through degradation of cyclin D3.
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Mason,B. and Laman,H.
  TITLE     The FBXL family of F-box proteins: variations on a theme
  JOURNAL   Open Biol 10 (11), 200319 (2020)
   PUBMED   33234069
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Bailey,S.D., Xie,C., Do,R., Montpetit,A., Diaz,R., Mohan,V.,
            Keavney,B., Yusuf,S., Gerstein,H.C., Engert,J.C. and Anand,S.
  CONSRTM   DREAM investigators
  TITLE     Variation at the NFATC2 locus increases the risk of
            thiazolidinedione-induced edema in the Diabetes REduction
            Assessment with ramipril and rosiglitazone Medication (DREAM) study
  JOURNAL   Diabetes Care 33 (10), 2250-2253 (2010)
   PUBMED   20628086
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Talmud,P.J., Drenos,F., Shah,S., Shah,T., Palmen,J., Verzilli,C.,
            Gaunt,T.R., Pallas,J., Lovering,R., Li,K., Casas,J.P., Sofat,R.,
            Kumari,M., Rodriguez,S., Johnson,T., Newhouse,S.J., Dominiczak,A.,
            Samani,N.J., Caulfield,M., Sever,P., Stanton,A., Shields,D.C.,
            Padmanabhan,S., Melander,O., Hastie,C., Delles,C., Ebrahim,S.,
            Marmot,M.G., Smith,G.D., Lawlor,D.A., Munroe,P.B., Day,I.N.,
            Kivimaki,M., Whittaker,J., Humphries,S.E. and Hingorani,A.D.
  CONSRTM   ASCOT investigators; NORDIL investigators; BRIGHT Consortium
  TITLE     Gene-centric association signals for lipids and apolipoproteins
            identified via the HumanCVD BeadChip
  JOURNAL   Am J Hum Genet 85 (5), 628-642 (2009)
   PUBMED   19913121
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   8  (residues 1 to 374)
  AUTHORS   Ebstein,F., Lange,N., Urban,S., Seifert,U., Kruger,E. and
            Kloetzel,P.M.
  TITLE     Maturation of human dendritic cells is accompanied by functional
            remodelling of the ubiquitin-proteasome system
  JOURNAL   Int J Biochem Cell Biol 41 (5), 1205-1215 (2009)
   PUBMED   19028597
REFERENCE   9  (residues 1 to 374)
  AUTHORS   Lievens,S., Vanderroost,N., Van der Heyden,J., Gesellchen,V.,
            Vidal,M. and Tavernier,J.
  TITLE     Array MAPPIT: high-throughput interactome analysis in mammalian
            cells
  JOURNAL   J Proteome Res 8 (2), 877-886 (2009)
   PUBMED   19159283
REFERENCE   10 (residues 1 to 374)
  AUTHORS   Winston,J.T., Koepp,D.M., Zhu,C., Elledge,S.J. and Harper,J.W.
  TITLE     A family of mammalian F-box proteins
  JOURNAL   Curr Biol 9 (20), 1180-1182 (1999)
   PUBMED   10531037
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC074143.5.
            
            On Aug 29, 2002 this sequence version replaced NP_060848.1.
            
            Summary: This gene encodes a member of the F-box protein family
            which is characterized by an approximately 40 amino acid motif, the
            F-box. The F-box proteins constitute one of the four subunits of
            the ubiquitin protein ligase complex called SCFs
            (SKP1-cullin-F-box), which function in phosphorylation-dependent
            ubiquitination. The F-box proteins are divided into 3 classes: Fbws
            containing WD-40 domains, Fbls containing leucine-rich repeats, and
            Fbxs containing either different protein-protein interaction
            modules or no recognizable motifs. The protein encoded by this gene
            belongs to the Fbls class. It shares 78% sequence identity with the
            mouse protein. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014414.1, SRR3476690.924531.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968189
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000258200.8/ ENSP00000258200.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q22.1"
     Protein         1..374
                     /product="F-box/LRR-repeat protein 8"
                     /note="F-box protein FBL8"
                     /calculated_mol_wt=40385
     Region          103..136
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          <132..>212
                     /region_name="PPP1R42"
                     /note="protein phosphatase 1 regulatory subunit 42;
                     cl42388"
                     /db_xref="CDD:455733"
     Region          137..163
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     Region          164..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275381"
     CDS             1..374
                     /gene="FBXL8"
                     /gene_synonym="FBL8"
                     /coded_by="NM_018378.3:152..1276"
                     /db_xref="CCDS:CCDS10831.1"
                     /db_xref="GeneID:55336"
                     /db_xref="HGNC:HGNC:17875"
                     /db_xref="MIM:609077"
ORIGIN      
        1 maepgeglpe evlalifrhl slrdraaaar vcrawaaaat csavwhdtki scecelegml
       61 ppylsacldh ihnlrlefep srkpsrraai ellmvlagra pglrglrlec rgekplfdag
      121 rdvleavhav cgaasqlrhl dlrrlsftld dalvlqaars cpelhslfld nstlvgsvgp
      181 gsvlelleac prlralglhl aslshailea laapdrapfa llalrcacpe darasplpne
      241 awvalrrrhp glavelelep alpaesvtrv lqpavpvaal rlnlsgdtvg pvrfaahhya
      301 atlcalevra aasaelnaal eelaarcaal revhcfcvvs hsvldafrah cprlrtytlk
      361 ltrephpwrp tlva
//
LOCUS       NP_001341606             404 aa            linear   PRI 20-NOV-2025
DEFINITION  AP-1 complex subunit gamma-like 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001341606 XP_016877237
VERSION     NP_001341606.1
DBSOURCE    REFSEQ: accession NM_001354677.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 404)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 404)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 404)
  AUTHORS   Tavares,L.A., da Silva,E.M., da Silva-Januario,M.E., Januario,Y.C.,
            de Cavalho,J.V., Czernisz,E.S., Mardones,G.A. and daSilva,L.L.
  TITLE     CD4 downregulation by the HIV-1 protein Nef reveals distinct roles
            for the gamma1 and gamma2 subunits of the AP-1 complex in protein
            trafficking
  JOURNAL   J Cell Sci 130 (2), 429-443 (2017)
   PUBMED   27909244
  REMARK    GeneRIF: Depletion of the gamma2 or mu1A (AP1M1) subunits of AP-1,
            but not of gamma1 (AP1G1), precludes Nef-mediated lysosomal
            degradation of CD4.
REFERENCE   4  (residues 1 to 404)
  AUTHORS   Jurgens,M.C., Voros,J., Rautureau,G.J., Shepherd,D.A., Pye,V.E.,
            Muldoon,J., Johnson,C.M., Ashcroft,A.E., Freund,S.M. and
            Ferguson,N.
  TITLE     The hepatitis B virus preS1 domain hijacks host trafficking
            proteins by motif mimicry
  JOURNAL   Nat Chem Biol 9 (9), 540-547 (2013)
   PUBMED   23851574
REFERENCE   5  (residues 1 to 404)
  AUTHORS   Aouizerat,B.E., Vittinghoff,E., Musone,S.L., Pawlikowska,L.,
            Kwok,P.Y., Olgin,J.E. and Tseng,Z.H.
  TITLE     GWAS for discovery and replication of genetic loci associated with
            sudden cardiac arrest in patients with coronary artery disease
  JOURNAL   BMC Cardiovasc Disord 11, 29 (2011)
   PUBMED   21658281
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 404)
  AUTHORS   Mattera,R., Ritter,B., Sidhu,S.S., McPherson,P.S. and
            Bonifacino,J.S.
  TITLE     Definition of the consensus motif recognized by gamma-adaptin ear
            domains
  JOURNAL   J Biol Chem 279 (9), 8018-8028 (2004)
   PUBMED   14665628
REFERENCE   7  (residues 1 to 404)
  AUTHORS   Mattera,R., Arighi,C.N., Lodge,R., Zerial,M. and Bonifacino,J.S.
  TITLE     Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5
            complex
  JOURNAL   EMBO J 22 (1), 78-88 (2003)
   PUBMED   12505986
REFERENCE   8  (residues 1 to 404)
  AUTHORS   Page,L.J., Sowerby,P.J., Lui,W.W. and Robinson,M.S.
  TITLE     Gamma-synergin: an EH domain-containing protein that interacts with
            gamma-adaptin
  JOURNAL   J Cell Biol 146 (5), 993-1004 (1999)
   PUBMED   10477754
REFERENCE   9  (residues 1 to 404)
  AUTHORS   Lewin,D.A., Sheff,D., Ooi,C.E., Whitney,J.A., Yamamoto,E.,
            Chicione,L.M., Webster,P., Bonifacino,J.S. and Mellman,I.
  TITLE     Cloning, expression, and localization of a novel gamma-adaptin-like
            molecule
  JOURNAL   FEBS Lett 435 (2-3), 263-268 (1998)
   PUBMED   9762922
REFERENCE   10 (residues 1 to 404)
  AUTHORS   Takatsu,H., Sakurai,M., Shin,H.W., Murakami,K. and Nakayama,K.
  TITLE     Identification and characterization of novel clathrin
            adaptor-related proteins
  JOURNAL   J Biol Chem 273 (38), 24693-24700 (1998)
   PUBMED   9733768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL135999.4 and AK304682.1.
            
            On Aug 31, 2017 this sequence version replaced XP_016877237.1.
            
            Summary: Adaptins are important components of clathrin-coated
            vesicles transporting ligand-receptor complexes from the plasma
            membrane or from the trans-Golgi network to lysosomes. The adaptin
            family of proteins is composed of four classes of molecules named
            alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together
            with medium and small subunits, form a heterotetrameric complex
            called an adaptor, whose role is to promote the formation of
            clathrin-coated pits and vesicles. The protein encoded by this gene
            is a gamma-adaptin protein and it belongs to the adaptor complexes
            large subunits family. This protein along with the complex is
            thought to function at some trafficking step in the complex
            pathways between the trans-Golgi network and the cell surface.
            [provided by RefSeq, Aug 2017].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: SRR1163658.560671.1, ERR3218375.295110.1
                                    [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..404
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..404
                     /product="AP-1 complex subunit gamma-like 2 isoform 2"
                     /note="gamma2-adaptin;
                     clathrin-associated/assembly/adaptor protein, large,
                     gamma-2; AP-1 complex subunit gamma-like 2; adaptor
                     related protein complex 1 gamma 2 subunit"
                     /calculated_mol_wt=44407
     Region          <1..194
                     /region_name="Adaptin_N"
                     /note="Adaptin N terminal region; pfam01602"
                     /db_xref="CDD:396262"
     Region          291..399
                     /region_name="Alpha_adaptinC2"
                     /note="Adaptin C-terminal domain; smart00809"
                     /db_xref="CDD:197886"
     CDS             1..404
                     /gene="AP1G2"
                     /gene_synonym="G2AD"
                     /coded_by="NM_001354677.2:1477..2691"
                     /note="isoform 2 is encoded by transcript variant 8"
                     /db_xref="GeneID:8906"
                     /db_xref="HGNC:HGNC:556"
                     /db_xref="MIM:603534"
ORIGIN      
        1 mmqelqafle scppdlradc asgillaaer faptkrwhid tilhvlttag thvrddavan
       61 ltqliggaqe lhaysvrrly nalaedisqq plvqvaawci geygdlllag nceeieplqv
      121 deeevlalle kvlqshmslp atrgyaltal mklstrlcgd nnrirqvvsi ygscldvelq
      181 qraveydtlf rkydhmraai lekmplverd gpqadeeake skeaaqlsea apvptepqas
      241 qlldlldlld gasgdvqhpp hldpspggal vhlldlpcvp pppapipdlk vferegvqln
      301 lsfirppenp alllititat nfsegdvthf icqaavpksl qlqlqapsgn tvpargglpi
      361 tqlfrilnpn kaplrlklrl tydhfhqsvq eifevnnlpv eswq
//
LOCUS       NP_005101                682 aa            linear   PRI 20-NOV-2025
DEFINITION  glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2
            [Homo sapiens].
ACCESSION   NP_005101
VERSION     NP_005101.1
DBSOURCE    REFSEQ: accession NM_005110.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 682)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 682)
  AUTHORS   Wei,J., Zhou,S., Chen,G., Chen,T., Wang,Y., Zou,J., Zhou,F., Liu,J.
            and Gong,Q.
  TITLE     GFPT2: A novel biomarker in mesothelioma for diagnosis and
            prognosis and its molecular mechanism in malignant progression
  JOURNAL   Br J Cancer 131 (9), 1529-1542 (2024)
   PUBMED   39317702
  REMARK    GeneRIF: GFPT2: A novel biomarker in mesothelioma for diagnosis and
            prognosis and its molecular mechanism in malignant progression.
REFERENCE   3  (residues 1 to 682)
  AUTHORS   Hatori,A., Fujii,Y., Kawase-Koga,Y., Ogasawara,T., Chikira,J.,
            Minami,S., Yamakawa,D. and Chikazu,D.
  TITLE     VCAM-1 and GFPT-2: Predictive markers of osteoblast differentiation
            in human dental pulp stem cells
  JOURNAL   Bone 166, 116575 (2023)
   PUBMED   36195245
  REMARK    GeneRIF: VCAM-1 and GFPT-2: Predictive markers of osteoblast
            differentiation in human dental pulp stem cells.
REFERENCE   4  (residues 1 to 682)
  AUTHORS   Kroef,V., Ruegenberg,S., Horn,M., Allmeroth,K., Ebert,L.,
            Bozkus,S., Miethe,S., Elling,U., Schermer,B., Baumann,U. and
            Denzel,M.S.
  TITLE     GFPT2/GFAT2 and AMDHD2 act in tandem to control the hexosamine
            pathway
  JOURNAL   Elife 11, e69223 (2022)
   PUBMED   35229715
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 682)
  AUTHORS   Wang,Q., Karvelsson,S.T., Kotronoulas,A., Gudjonsson,T.,
            Halldorsson,S. and Rolfsson,O.
  TITLE     Glutamine-Fructose-6-Phosphate Transaminase 2 (GFPT2) Is
            Upregulated in Breast Epithelial-Mesenchymal Transition and
            Responds to Oxidative Stress
  JOURNAL   Mol Cell Proteomics 21 (2), 100185 (2022)
   PUBMED   34923141
  REMARK    GeneRIF: Glutamine-Fructose-6-Phosphate Transaminase 2 (GFPT2) Is
            Upregulated in Breast Epithelial-Mesenchymal Transition and
            Responds to Oxidative Stress.
REFERENCE   6  (residues 1 to 682)
  AUTHORS   Prasad,P., Tiwari,A.K., Kumar,K.M., Ammini,A.C., Gupta,A., Gupta,R.
            and Thelma,B.K.
  TITLE     Association analysis of ADPRT1, AKR1B1, RAGE, GFPT2 and PAI-1 gene
            polymorphisms with chronic renal insufficiency among Asian Indians
            with type-2 diabetes
  JOURNAL   BMC Med Genet 11, 52 (2010)
   PUBMED   20353610
  REMARK    GeneRIF: association of nine single nucleotide polymorphisms in
            ADPRT1, AKR1B1), RAGE, GFPT2 and PAI-1 genes with chronic renal
            insufficiency among Asian Indians with type 2 diabetes
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 682)
  AUTHORS   Srinivasan,V., Sandhya,N., Sampathkumar,R., Farooq,S., Mohan,V. and
            Balasubramanyam,M.
  TITLE     Glutamine fructose-6-phosphate amidotransferase (GFAT) gene
            expression and activity in patients with type 2 diabetes:
            inter-relationships with hyperglycaemia and oxidative stress
  JOURNAL   Clin Biochem 40 (13-14), 952-957 (2007)
   PUBMED   17574229
  REMARK    GeneRIF: Increased GFAT activity appears to be associated with
            insulin resistance, postprandial hyperglycaemia and oxidative
            stress in T2DM and may point towards a potential pathway amenable
            for therapeutic intervention.
REFERENCE   8  (residues 1 to 682)
  AUTHORS   Yang,C.T., Hindes,A.E., Hultman,K.A. and Johnson,S.L.
  TITLE     Mutations in gfpt1 and skiv2l2 cause distinct stage-specific
            defects in larval melanocyte regeneration in zebrafish
  JOURNAL   PLoS Genet 3 (6), e88 (2007)
   PUBMED   17542649
REFERENCE   9  (residues 1 to 682)
  AUTHORS   Zhang,H., Jia,Y., Cooper,J.J., Hale,T., Zhang,Z. and Elbein,S.C.
  TITLE     Common variants in glutamine:fructose-6-phosphate amidotransferase
            2 (GFPT2) gene are associated with type 2 diabetes, diabetic
            nephropathy, and increased GFPT2 mRNA levels
  JOURNAL   J Clin Endocrinol Metab 89 (2), 748-755 (2004)
   PUBMED   14764791
  REMARK    GeneRIF: GFPT2 mRNA levels in transformed lymphocytes significantly
            increased among African-Americans. Associated allele of 3' UTR SNP
            approximately 2-fold overexpressed. 3' UTR variant results in
            increased GFPT2 mRNA with resultant increased hexosamine flux.
            GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   10 (residues 1 to 682)
  AUTHORS   Oki,T., Yamazaki,K., Kuromitsu,J., Okada,M. and Tanaka,I.
  TITLE     cDNA cloning and mapping of a novel subtype of
            glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human
            and mouse
  JOURNAL   Genomics 57 (2), 227-234 (1999)
   PUBMED   10198162
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI753491.1, AB016789.1, AK022507.1 and BC000012.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK022507.1, SRR1803616.184569.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed/partial sample support
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000253778.13/ ENSP00000253778.8
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..682
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q35.3"
     Protein         1..682
                     /product="glutamine--fructose-6-phosphate aminotransferase
                     [isomerizing] 2"
                     /EC_number="2.6.1.16"
                     /note="glutamine: fructose-6-phosphate aminotransferase 2;
                     glucosamine--fructose-6-phosphate aminotransferase
                     [isomerizing] 2; hexosephosphate aminotransferase 2;
                     D-fructose-6-phosphate amidotransferase 2;
                     glutamine:fructose-6-phosphate amidotransferase 2"
                     /calculated_mol_wt=76800
     Region          1..682
                     /region_name="PLN02981"
                     /note="glucosamine:fructose-6-phosphate aminotransferase"
                     /db_xref="CDD:215531"
     Site            244
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (O94808.3)"
     CDS             1..682
                     /gene="GFPT2"
                     /gene_synonym="GFAT; GFAT 2; GFAT2"
                     /coded_by="NM_005110.4:120..2168"
                     /db_xref="CCDS:CCDS43411.1"
                     /db_xref="GeneID:9945"
                     /db_xref="HGNC:HGNC:4242"
                     /db_xref="MIM:603865"
ORIGIN      
        1 mcgifaymny rvprtrkeif etlikglqrl eyrgydsagv aidgnnhevk erhiqlvkkr
       61 gkvkaldeel ykqdsmdlkv efethfgiah trwathgvps avnshpqrsd kgnefvvihn
      121 giitnykdlr kfleskgyef esetdtetia klikyvfdnr eteditfstl verviqqleg
      181 afalvfksvh ypgeavatrr gsplligvrs kyklsteqip ilyrtctlen vknicktrmk
      241 rldssaclha vgdkavefff asdasaiieh tnrvifledd diaavadgkl sihrvkrsas
      301 ddpsraiqtl qmelqqimkg nfsafmqkei feqpesvfnt mrgrvnfetn tvllgglkdh
      361 lkeirrcrrl ivigcgtsyh aavatrqvle eltelpvmve lasdfldrnt pvfrddvcff
      421 isqsgetadt llalryckdr galtvgvtnt vgssisretd cgvhinagpe igvastkayt
      481 sqfislvmfg lmmsedrisl qnrrqeiirg lrslpelike vlsleekihd lalelytqrs
      541 llvmgrgyny atclegalki keitymhseg ilagelkhgp lalidkqmpv imvimkdpcf
      601 akcqnalqqv tarqgrpiil cskddtessk fayktielph tvdclqgils viplqllsfh
      661 lavlrgydvd fprnlaksvt ve
//
LOCUS       NP_001137502             953 aa            linear   PRI 20-NOV-2025
DEFINITION  RNA cytidine acetyltransferase isoform b [Homo sapiens].
ACCESSION   NP_001137502
VERSION     NP_001137502.2
DBSOURCE    REFSEQ: accession NM_001144030.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Li,W.P., Mao,X.T., Xie,J.H., Li,J.Y., Liu,B.Q., Wu,L.X., Yang,B.,
            Li,Y.Y. and Jin,J.
  TITLE     N-acetyltransferase 10 is implicated in the pathogenesis of cycling
            T cell-mediated autoimmune and inflammatory disorders in mice
  JOURNAL   Nat Commun 15 (1), 9388 (2024)
   PUBMED   39477944
  REMARK    GeneRIF: N-acetyltransferase 10 is implicated in the pathogenesis
            of cycling T cell-mediated autoimmune and inflammatory disorders in
            mice.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Xing,P., Zhou,M., Sun,J., Wang,D., Huang,W. and An,P.
  TITLE     NAT10-mediated ac4C acetylation of TFRC promotes sepsis-induced
            pulmonary injury through regulating ferroptosis
  JOURNAL   Mol Med 30 (1), 140 (2024)
   PUBMED   39251905
  REMARK    GeneRIF: NAT10-mediated ac[4]C acetylation of TFRC promotes
            sepsis-induced pulmonary injury through regulating ferroptosis.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Song,S., Li,B., Jin,X., Li,H., Wang,H., Wang,F., He,Y. and Zhang,C.
  TITLE     NAT10 Overexpression Promotes Tumorigenesis and
            Epithelial-Mesenchymal Transition Through AKT Pathway in Gastric
            Cancer
  JOURNAL   Dig Dis Sci 69 (9), 3261-3275 (2024)
   PUBMED   38990269
  REMARK    GeneRIF: NAT10 Overexpression Promotes Tumorigenesis and
            Epithelial-Mesenchymal Transition Through AKT Pathway in Gastric
            Cancer.
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Ding,M., Yu,Z., Lu,T., Hu,S., Zhou,X. and Wang,X.
  TITLE     N-acetyltransferase 10 facilitates tumorigenesis of diffuse large
            B-cell lymphoma by regulating AMPK/mTOR signalling through
            N4-acetylcytidine modification of SLC30A9
  JOURNAL   Clin Transl Med 14 (7), e1747 (2024)
   PUBMED   38961519
  REMARK    GeneRIF: N-acetyltransferase 10 facilitates tumorigenesis of
            diffuse large B-cell lymphoma by regulating AMPK/mTOR signalling
            through N4-acetylcytidine modification of SLC30A9.
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Guan,L.Z., Shen,Q., Sun,Y., Wang,J.C., Gong,Y.L., Hou,L. and
            Zhang,B.
  TITLE     [Nucleolar localization of human acetyltransferase-like protein and
            its expression in tumors]
  JOURNAL   Beijing Da Xue Xue Bao Yi Xue Ban 40 (4), 347-351 (2008)
   PUBMED   18677378
  REMARK    GeneRIF: hALP is a nucleolar protein, and the nucleolar
            localization is mediated by its carboxy terminal domain.
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Fu,D. and Collins,K.
  TITLE     Purification of human telomerase complexes identifies factors
            involved in telomerase biogenesis and telomere length regulation
  JOURNAL   Mol Cell 28 (5), 773-785 (2007)
   PUBMED   18082603
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Chi,Y.H., Haller,K., Peloponese,J.M. Jr. and Jeang,K.T.
  TITLE     Histone acetyltransferase hALP and nuclear membrane protein hsSUN1
            function in de-condensation of mitotic chromosomes
  JOURNAL   J Biol Chem 282 (37), 27447-27458 (2007)
   PUBMED   17631499
  REMARK    GeneRIF: chromosome de-condensation needs the function of an inner
            nuclear membrane (INM) protein hsSUN1 and a membrane-associated
            histone acetyltransferase (HAT), hALP.
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Liu,H., Ling,Y., Gong,Y., Sun,Y., Hou,L. and Zhang,B.
  TITLE     DNA damage induces N-acetyltransferase NAT10 gene expression
            through transcriptional activation
  JOURNAL   Mol Cell Biochem 300 (1-2), 249-258 (2007)
   PUBMED   17180247
  REMARK    GeneRIF: The above results suggested that NAT10 could be involved
            in DNA damage response and increased cellular resistance to
            genotoxicity.
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Lv,J., Liu,H., Wang,Q., Tang,Z., Hou,L. and Zhang,B.
  TITLE     Molecular cloning of a novel human gene encoding histone
            acetyltransferase-like protein involved in transcriptional
            activation of hTERT
  JOURNAL   Biochem Biophys Res Commun 311 (2), 506-513 (2003)
   PUBMED   14592445
  REMARK    GeneRIF: The investigation suggested that hALP influences the
            activity of histone acetylation and could up-regulate telomerase
            activity through transactivation of hTERT promoter.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC090469.9.
            
            On May 31, 2019 this sequence version replaced NP_001137502.1.
            
            Summary: The protein encoded by this gene is an RNA cytidine
            acetyltransferase involved in histone acetylation, tRNA
            acetylation, the biosynthesis of 18S rRNA, and the enhancement of
            nuclear architecture and chromatin organization. [provided by
            RefSeq, Oct 2016].
            
            Transcript Variant: This variant (2) lacks two exons in the 5'
            coding region and uses a downstream start codon, compared to
            variant 1. Isoform b has a shorter N-terminus, compared to isoform
            a.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803614.160123.1,
                                           SRR1803617.18977.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145743, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..953
                     /product="RNA cytidine acetyltransferase isoform b"
                     /EC_number="2.3.1.-"
                     /note="N-acetyltransferase-like protein; 18S rRNA cytosine
                     acetyltransferase; RNA cytidine acetyltransferase;
                     N-acetyltransferase 10 (GCN5-related)"
                     /calculated_mol_wt=107166
     Region          35..832
                     /region_name="TmcA"
                     /note="tRNA(Met) C34 N-acetyltransferase TmcA
                     [Translation, ribosomal structure and biogenesis];
                     COG1444"
                     /db_xref="CDD:441053"
     Region          456..680
                     /region_name="GNAT_acetyltr_2"
                     /note="GNAT acetyltransferase 2; pfam13718"
                     /db_xref="CDD:463966"
     Region          691..904
                     /region_name="tRNA_bind_2"
                     /note="Possible tRNA binding domain; pfam13725"
                     /db_xref="CDD:463969"
     CDS             1..953
                     /gene="NAT10"
                     /gene_synonym="ALP; Kre33; NET43"
                     /coded_by="NM_001144030.2:181..3042"
                     /note="isoform b is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS44568.1"
                     /db_xref="GeneID:55226"
                     /db_xref="HGNC:HGNC:29830"
                     /db_xref="MIM:609221"
ORIGIN      
        1 mrqlqkkikn gtlnikqddp felfiaatni rycyynethk ilgntfgmcv lqdfealtpn
       61 llartvetve ggglvvillr tmnslkqlyt vtmdvhsryr teahqdvvgr fnerfilsla
      121 sckkclvidd qlnilpissh vatmealppq tpdeslgpsd lelrelkesl qdtqpvgvlv
      181 dccktldqak avlkfiegis ektlrstval taargrgksa alglaiagav afgysnifvt
      241 spspdnlhtl fefvfkgfda lqyqehldye iiqslnpefn kavirvnvfr ehrqtiqyih
      301 padavklgqa elvvideaaa iplplvksll gpylvfmast ingyegtgrs lslkliqqlr
      361 qqsaqsqvst taenktttta rlasartlye vslqesirya pgdavekwln dllcldclni
      421 trivsgcplp eacelyyvnr dtlfcyhkas evflqrlmal yvashyknsp ndlqmlsdap
      481 ahhlfcllpp vpptqnalpe vlaviqvcle geisrqsiln slsrgkkasg dlipwtvseq
      541 fqdpdfggls ggrvvriavh pdyqgmgygs ralqllqmyy egrfpcleek vletpqeiht
      601 vsseavslle evitprkdlp plllklnerp aerldylgvs ygltprllkf wkragfvpvy
      661 lrqtpndltg ehscimlktl tdedeadqgg wlaafwkdfr rrflallsyq fstfspslal
      721 niiqnrnmgk paqpalsree lealflpydl krlemysrnm vdyhlimdmi paisriyfln
      781 qlgdlalsaa qsalllgigl qhksvdqlek eielpsgqlm glfnriirkv vklfnevqek
      841 aieeqmvaak dvvmeptmkt lsddldeaak efqekhkkev gklksmdlse yiirgddeew
      901 nevlnkagpn asiislksdk krkleakqep kqskklknre tknkkdmklk rkk
//
LOCUS       NP_001308228             907 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/threonine-protein kinase WNK4 isoform 2 [Homo sapiens].
ACCESSION   NP_001308228 XP_006722085
VERSION     NP_001308228.1
DBSOURCE    REFSEQ: accession NM_001321299.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 907)
  AUTHORS   Li,M., Shao,X., Ning,Q., Sun,R., Li,R., Liu,Y., Yuan,Y. and
            Zhang,Y.
  TITLE     Downregulation of WNK4 expression facilitates the proliferation of
            gastric cancer cells via activation of the STAT3 signaling pathway
  JOURNAL   Neoplasma 71 (3), 209-218 (2024)
   PUBMED   38764295
  REMARK    GeneRIF: Downregulation of WNK4 expression facilitates the
            proliferation of gastric cancer cells via activation of the STAT3
            signaling pathway.
REFERENCE   2  (residues 1 to 907)
  AUTHORS   Wang,L., Wu,G. and Peng,J.B.
  TITLE     Identification of a novel KLHL3-interacting motif in the C-terminal
            region of WNK4
  JOURNAL   Biochem Biophys Res Commun 670, 87-93 (2023)
   PUBMED   37285722
  REMARK    GeneRIF: Identification of a novel KLHL3-interacting motif in the
            C-terminal region of WNK4.
REFERENCE   3  (residues 1 to 907)
  AUTHORS   Ying,S., Guo,Q. and Zhang,C.
  TITLE     KLHL3-dependent WNK4 degradation affected by potassium through the
            neddylation and autophagy pathway
  JOURNAL   BMC Nephrol 24 (1), 217 (2023)
   PUBMED   37481568
  REMARK    GeneRIF: KLHL3-dependent WNK4 degradation affected by potassium
            through the neddylation and autophagy pathway.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 907)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   5  (residues 1 to 907)
  AUTHORS   Kahle,K.T., Gimenez,I., Hassan,H., Wilson,F.H., Wong,R.D.,
            Forbush,B., Aronson,P.S. and Lifton,R.P.
  TITLE     WNK4 regulates apical and basolateral Cl- flux in extrarenal
            epithelia
  JOURNAL   Proc Natl Acad Sci U S A 101 (7), 2064-2069 (2004)
   PUBMED   14769928
  REMARK    GeneRIF: general role for WNK4 in the regulation of electrolyte
            flux in diverse epithelia
REFERENCE   6  (residues 1 to 907)
  AUTHORS   Wilson,F.H., Kahle,K.T., Sabath,E., Lalioti,M.D., Rapson,A.K.,
            Hoover,R.S., Hebert,S.C., Gamba,G. and Lifton,R.P.
  TITLE     Molecular pathogenesis of inherited hypertension with hyperkalemia:
            the Na-Cl cotransporter is inhibited by wild-type but not mutant
            WNK4
  JOURNAL   Proc Natl Acad Sci U S A 100 (2), 680-684 (2003)
   PUBMED   12515852
REFERENCE   7  (residues 1 to 907)
  AUTHORS   Wistow,G., Bernstein,S.L., Wyatt,M.K., Fariss,R.N., Behal,A.,
            Touchman,J.W., Bouffard,G., Smith,D. and Peterson,K.
  TITLE     Expressed sequence tag analysis of human RPE/choroid for the
            NEIBank Project: over 6000 non-redundant transcripts, novel genes
            and splice variants
  JOURNAL   Mol Vis 8, 205-220 (2002)
   PUBMED   12107410
  REMARK    Publication Status: Online-Only
REFERENCE   8  (residues 1 to 907)
  AUTHORS   Verissimo,F. and Jordan,P.
  TITLE     WNK kinases, a novel protein kinase subfamily in multi-cellular
            organisms
  JOURNAL   Oncogene 20 (39), 5562-5569 (2001)
   PUBMED   11571656
REFERENCE   9  (residues 1 to 907)
  AUTHORS   Wilson,F.H., Disse-Nicodeme,S., Choate,K.A., Ishikawa,K.,
            Nelson-Williams,C., Desitter,I., Gunel,M., Milford,D.V.,
            Lipkin,G.W., Achard,J.M., Feely,M.P., Dussol,B., Berland,Y.,
            Unwin,R.J., Mayan,H., Simon,D.B., Farfel,Z., Jeunemaitre,X. and
            Lifton,R.P.
  TITLE     Human hypertension caused by mutations in WNK kinases
  JOURNAL   Science 293 (5532), 1107-1112 (2001)
   PUBMED   11498583
REFERENCE   10 (residues 1 to 907)
  AUTHORS   Ellison,D.H.
  TITLE     Pseudohypoaldosteronism Type II
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   22073419
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC100793.8, CA388932.1,
            BC144356.1 and BM683764.1.
            
            On Mar 19, 2016 this sequence version replaced XP_006722085.1.
            
            Summary: This gene encodes a member of the WNK family of
            serine-threonine protein kinases. The kinase is part of the tight
            junction complex in kidney cells, and regulates the balance between
            NaCl reabsorption and K(+) secretion. The kinase regulates the
            activities of several types of ion channels, cotransporters, and
            exchangers involved in electrolyte flux in epithelial cells.
            Mutations in this gene result in pseudohypoaldosteronism type
            IIB.[provided by RefSeq, Sep 2009].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC144356.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142586
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..907
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.2"
     Protein         1..907
                     /product="serine/threonine-protein kinase WNK4 isoform 2"
                     /EC_number="2.7.11.1"
                     /note="serine/threonine-protein kinase WNK4; protein
                     kinase with no lysine 4; protein kinase lysine-deficient
                     4"
                     /calculated_mol_wt=97223
     Region          117..179
                     /region_name="OSR1_C"
                     /note="Oxidative-stress-responsive kinase 1 C-terminal
                     domain; pfam12202"
                     /db_xref="CDD:463491"
     Region          <462..738
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     CDS             1..907
                     /gene="WNK4"
                     /gene_synonym="PHA2B; PRKWNK4"
                     /coded_by="NM_001321299.2:1009..3732"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:65266"
                     /db_xref="HGNC:HGNC:14544"
                     /db_xref="MIM:601844"
ORIGIN      
        1 mslsrdllal sksgtwawpr ssapplprvs sgprnswppr ctrkstmrpw tctrsacacw
       61 rwpplstrtp sarmprksta rslrftiqdl lahaffreer gvhvelaeed dgekpglklw
      121 lrmedarrgg rprdnqaief lfqlgrdaae evaqemvalg lvceadyqpv aravrervaa
      181 iqrkreklrk arelealppe pgpppatvpm apgppsvfpp epeepeadqh qpflfrhasy
      241 ssttsdcetd gylsssgfld asdpalqppg gvpsslaesh lclpsafals iprsgpgsdf
      301 spgdsyasda asglsdvgeg mgqmrrppgr nlrrrprsrl rvtsvsdqnd rvvecqlqth
      361 nskmvtfrfd ldgdspeeia aamvynefil pserdgflrr ireiiqrvet llkrdtgpme
      421 aaedtlspqe epaplpalpv plpdpsneel qsstslehrs wtafstssss pgtplspgnp
      481 fspgtpispg pifpitsppc hpspspfspi ssqvssnpsp hptssplpfs sstpefpvpl
      541 sqcpwsslpt tspptfsptc sqvtlsspff ppcpstssfp sttaapllsl asafslavmt
      601 vaqsllspsp gllsqsppap psplpslplp ppvapggqes psphtaeves easppparpl
      661 pgearlapis eegkpqlvgr fqvtsskepa eplplqptsp tlsgspkpst pqltsessdt
      721 edsagggpet realaesdra aeglgagvee egddgkepqv ggspqplshp spvwmnysys
      781 slclsseese ssgedeefwa elqslrqkhl sevetlqtlq kkeiedlysr lgkqpppgiv
      841 apaamlssrq rrlskgsfpt srrnslqrse ppgpgimrrn slsgsstgsq eqraskgvtf
      901 agdvgrm
//
LOCUS       NP_001333154             715 aa            linear   PRI 20-NOV-2025
DEFINITION  WD repeat-containing protein 48 isoform 4 [Homo sapiens].
ACCESSION   NP_001333154
VERSION     NP_001333154.1
DBSOURCE    REFSEQ: accession NM_001346225.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 715)
  AUTHORS   Yu,Z., Tong,L., Ma,C., Song,H., Wang,J., Chai,L., Wang,C., Wang,M.,
            Wang,C., Yan,R., Fu,Y., Jia,M., Zhao,W. and Zhao,C.
  TITLE     The UAF1-USP1 Deubiquitinase Complex Stabilizes cGAS and
            Facilitates Antiviral Responses
  JOURNAL   J Immunol 212 (2), 295-301 (2024)
   PUBMED   38054892
  REMARK    GeneRIF: The UAF1-USP1 Deubiquitinase Complex Stabilizes cGAS and
            Facilitates Antiviral Responses.
REFERENCE   2  (residues 1 to 715)
  AUTHORS   Ng,V.H., Spencer,Z., Neitzel,L.R., Nayak,A., Loberg,M.A., Shen,C.,
            Kassel,S.N., Kroh,H.K., An,Z., Anthony,C.C., Bryant,J.M.,
            Lawson,A., Goldsmith,L., Benchabane,H., Hansen,A.G., Li,J.,
            D'Souza,S., Lebensohn,A.M., Rohatgi,R., Weiss,W.A., Weiss,V.L.,
            Williams,C., Hong,C.C., Robbins,D.J., Ahmed,Y. and Lee,E.
  TITLE     The USP46 complex deubiquitylates LRP6 to promote Wnt/beta-catenin
            signaling
  JOURNAL   Nat Commun 14 (1), 6173 (2023)
   PUBMED   37798301
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 715)
  AUTHORS   Zarrella,K., Longmire,P., Zeltzer,S., Collins-McMillen,D.,
            Hancock,M., Buehler,J., Reitsma,J.M., Terhune,S.S., Nelson,J.A. and
            Goodrum,F.
  TITLE     Human cytomegalovirus UL138 interaction with USP1 activates STAT1
            in infection
  JOURNAL   PLoS Pathog 19 (6), e1011185 (2023)
   PUBMED   37289831
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 715)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 715)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 715)
  AUTHORS   Cote-Martin,A., Moody,C., Fradet-Turcotte,A., D'Abramo,C.M.,
            Lehoux,M., Joubert,S., Poirier,G.G., Coulombe,B., Laimins,L.A. and
            Archambault,J.
  TITLE     Human papillomavirus E1 helicase interacts with the WD repeat
            protein p80 to promote maintenance of the viral genome in
            keratinocytes
  JOURNAL   J Virol 82 (3), 1271-1283 (2008)
   PUBMED   18032488
  REMARK    GeneRIF: These findings suggest that the interaction of human
            papillomavirus 11 and 31 E1 proteins with p80 is required for
            efficient maintenance of the viral episome in undifferentiated
            keratinocytes.
REFERENCE   7  (residues 1 to 715)
  AUTHORS   Park,J., Cho,N.H., Choi,J.K., Feng,P., Choe,J. and Jung,J.U.
  TITLE     Distinct roles of cellular Lck and p80 proteins in herpesvirus
            saimiri Tip function on lipid rafts
  JOURNAL   J Virol 77 (16), 9041-9051 (2003)
   PUBMED   12885920
REFERENCE   8  (residues 1 to 715)
  AUTHORS   Park,J., Lee,B.S., Choi,J.K., Means,R.E., Choe,J. and Jung,J.U.
  TITLE     Herpesviral protein targets a cellular WD repeat endosomal protein
            to downregulate T lymphocyte receptor expression
  JOURNAL   Immunity 17 (2), 221-233 (2002)
   PUBMED   12196293
REFERENCE   9  (residues 1 to 715)
  AUTHORS   Nair,J.S., DaFonseca,C.J., Tjernberg,A., Sun,W., Darnell,J.E. Jr.,
            Chait,B.T. and Zhang,J.J.
  TITLE     Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in
            response to IFN-gamma
  JOURNAL   Proc Natl Acad Sci U S A 99 (9), 5971-5976 (2002)
   PUBMED   11972023
REFERENCE   10 (residues 1 to 715)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL   (in) Adam MP, Bick S, Mirzaa GM, Pagon RA, Wallace SE and Amemiya A
            (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC123903.2 and AC138124.2.
            
            Summary: The protein encoded by this gene has been shown to
            interact with ubiquitin specific peptidase 1 (USP1), activating the
            deubiquitinating activity of USP1 and allowing it to remove the
            ubiquitin moiety from monoubiquitinated FANCD2. FANCD2 is
            ubiquitinated in response to DNA damage. [provided by RefSeq, Sep
            2016].
            
            Transcript Variant: This variant (4) encodes the longest isoform
            (4).
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.185124.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2154529
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..715
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p22.2"
     Protein         1..715
                     /product="WD repeat-containing protein 48 isoform 4"
                     /note="WD repeat endosomal protein; WD repeat-containing
                     protein 48; USP1 associated factor 1; testicular tissue
                     protein Li 224"
                     /calculated_mol_wt=80266
     Region          30..324
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cd00200"
                     /db_xref="CDD:238121"
     Region          35..73
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Site            order(47,51,57..58,73..74,92,96,102..103,115..116,133,138,
                     144..145,205,222,227,233..234,246..247,265,269,275..276,
                     288..289,306,311,317..318)
                     /site_type="active"
                     /note="structural tetrad [active]"
                     /db_xref="CDD:238121"
     Region          79..115
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          120..156
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          167..203
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          210..245
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          251..287
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          293..328
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          335..362
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          401..427
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          547..711
                     /region_name="DUF3337"
                     /note="Domain of unknown function (DUF3337); pfam11816"
                     /db_xref="CDD:463358"
     CDS             1..715
                     /gene="WDR48"
                     /gene_synonym="Bun62; P80; SPG60; UAF1"
                     /coded_by="NM_001346225.2:11..2158"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="GeneID:57599"
                     /db_xref="HGNC:HGNC:30914"
                     /db_xref="MIM:612167"
ORIGIN      
        1 maahhrqnta grrkvqvsyv irdevekynr ngvnalqldp alnrlftagr dsiiriwsvn
       61 qhkqdpyias mehhtdwvnd ivlccngktl isassdttvk vwnahkgfcm stlrthkdyv
      121 kalayakdke lvasagldrq iflwdvntlt altasnntvt slhresvsyf esastysvla
      181 pksmieqqra ssslqsknas slsgnkdsiy slamnqlgti ivsgstekvl rvwdprtcak
      241 lmklkghtdn vkalllnrdg tqclsgssdg tirlwslgqq rciatyrvhd egvwalqvnd
      301 afthvysggr drkiyctdlr npdirvlice ekapvlkmel drsadpppai wvattkstvn
      361 kwtlkgihnf rasgdydndc tnpitplctq pdqvikggas iiqchilndk rhiltkdtnn
      421 nvaywdvlka ckvedlgkvd fedeikkrfk mvyvpnwfsv dlktgmltit ldesdcfaaw
      481 vsakdagfss pdgsdpklnl gglllqalle ywprthvnpm deeenevnhv ngeqenrvqk
      541 gngyfqvpph tpvifgeagg rtlfrllcrd sggetesmll netvpqwvid itvdknmpkf
      601 nkipfylqph assgaktlkk drlsasdmlq vrkvmehvye kiinldnesq ttsssnnekp
      661 geqekeedia vlaeekiell cqdqvldpnm dlrtvkhfiw ksggdltlhy rqkst
//
LOCUS       NP_001186814              81 aa            linear   PRI 20-NOV-2025
DEFINITION  huntingtin-interacting protein K isoform 2 [Homo sapiens].
ACCESSION   NP_001186814
VERSION     NP_001186814.1
DBSOURCE    REFSEQ: accession NM_001199885.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 81)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 81)
  AUTHORS   Firouzbakht,A., Haider,A., Gaalswyk,K., Alaeen,S., Ghosh,K. and
            Gruebele,M.
  TITLE     HYPK: A marginally disordered protein sensitive to charge
            decoration
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2316408121 (2024)
   PUBMED   38657047
  REMARK    GeneRIF: HYPK: A marginally disordered protein sensitive to charge
            decoration.
REFERENCE   3  (residues 1 to 81)
  AUTHORS   Ghosh,D.K. and Ranjan,A.
  TITLE     HYPK coordinates degradation of polyneddylated proteins by
            autophagy
  JOURNAL   Autophagy 18 (8), 1763-1784 (2022)
   PUBMED   34836490
  REMARK    GeneRIF: HYPK coordinates degradation of polyneddylated proteins by
            autophagy.
REFERENCE   4  (residues 1 to 81)
  AUTHORS   Lin,M.C., Yu,C.J. and Lee,F.S.
  TITLE     Phosphorylation of Arl4A/D promotes their binding by the HYPK
            chaperone for their stable recruitment to the plasma membrane
  JOURNAL   Proc Natl Acad Sci U S A 119 (30), e2207414119 (2022)
   PUBMED   35857868
  REMARK    GeneRIF: Phosphorylation of Arl4A/D promotes their binding by the
            HYPK chaperone for their stable recruitment to the plasma membrane.
REFERENCE   5  (residues 1 to 81)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   6  (residues 1 to 81)
  AUTHORS   Raychaudhuri,S., Majumder,P., Sarkar,S., Giri,K., Mukhopadhyay,D.
            and Bhattacharyya,N.P.
  TITLE     Huntingtin interacting protein HYPK is intrinsically unstructured
  JOURNAL   Proteins 71 (4), 1686-1698 (2008)
   PUBMED   18076027
REFERENCE   7  (residues 1 to 81)
  AUTHORS   Raychaudhuri,S., Sinha,M., Mukhopadhyay,D. and Bhattacharyya,N.P.
  TITLE     HYPK, a Huntingtin interacting protein, reduces aggregates and
            apoptosis induced by N-terminal Huntingtin with 40 glutamines in
            Neuro2a cells and exhibits chaperone-like activity
  JOURNAL   Hum Mol Genet 17 (2), 240-255 (2008)
   PUBMED   17947297
  REMARK    GeneRIF: The present study, has confirmed, by confocal microscopy
            and immunoprecipitation, that HYPK interacts with the N-terminal of
            Htt.
REFERENCE   8  (residues 1 to 81)
  AUTHORS   Kaltenbach,L.S., Romero,E., Becklin,R.R., Chettier,R., Bell,R.,
            Phansalkar,A., Strand,A., Torcassi,C., Savage,J., Hurlburt,A.,
            Cha,G.H., Ukani,L., Chepanoske,C.L., Zhen,Y., Sahasrabudhe,S.,
            Olson,J., Kurschner,C., Ellerby,L.M., Peltier,J.M., Botas,J. and
            Hughes,R.E.
  TITLE     Huntingtin interacting proteins are genetic modifiers of
            neurodegeneration
  JOURNAL   PLoS Genet 3 (5), e82 (2007)
   PUBMED   17500595
REFERENCE   9  (residues 1 to 81)
  AUTHORS   Perez-Gonzalez,A., Rodriguez,A., Huarte,M., Salanueva,I.J. and
            Nieto,A.
  TITLE     hCLE/CGI-99, a human protein that interacts with the influenza
            virus polymerase, is a mRNA transcription modulator
  JOURNAL   J Mol Biol 362 (5), 887-900 (2006)
   PUBMED   16950395
REFERENCE   10 (residues 1 to 81)
  AUTHORS   Faber,P.W., Barnes,G.T., Srinidhi,J., Chen,J., Gusella,J.F. and
            MacDonald,M.E.
  TITLE     Huntingtin interacts with a family of WW domain proteins
  JOURNAL   Hum Mol Genet 7 (9), 1463-1474 (1998)
   PUBMED   9700202
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BQ772100.1, BQ478474.1, BC019262.1 and AC018512.6.
            
            Transcript Variant: This variant (2) lacks an alternate exon
            resulting in a frameshift in the 3' coding region, compared to
            variant 1. The encoded isoform (2) has a distinct and shorter
            C-terminus, compared to isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BQ478474.1, AW168528.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..81
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q15.3"
     Protein         1..81
                     /product="huntingtin-interacting protein K isoform 2"
                     /note="huntingtin yeast partner K"
                     /calculated_mol_wt=8945
     CDS             1..81
                     /gene="HYPK"
                     /gene_synonym="C15orf63; HSPC136"
                     /coded_by="NM_001199885.1:179..424"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:25764"
                     /db_xref="HGNC:HGNC:18418"
                     /db_xref="MIM:612784"
ORIGIN      
        1 mrrrgeidma tegdvelele tetsgperpp ekprkhdsga adlervtdya eekeiqssnl
       61 etgertgksh yqegrsgann d
//
LOCUS       NP_001305136             195 aa            linear   PRI 20-NOV-2025
DEFINITION  transmembrane protein 239 isoform 1 [Homo sapiens].
ACCESSION   NP_001305136 XP_005260690
VERSION     NP_001305136.1
DBSOURCE    REFSEQ: accession NM_001318207.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Zhong,Q., Pevzner,S.J., Hao,T., Wang,Y., Mosca,R., Menche,J.,
            Taipale,M., Tasan,M., Fan,C., Yang,X., Haley,P., Murray,R.R.,
            Mer,F., Gebreab,F., Tam,S., MacWilliams,A., Dricot,A., Reichert,P.,
            Santhanam,B., Ghamsari,L., Calderwood,M.A., Rolland,T.,
            Charloteaux,B., Lindquist,S., Barabasi,A.L., Hill,D.E., Aloy,P.,
            Cusick,M.E., Xia,Y., Roth,F.P. and Vidal,M.
  TITLE     An inter-species protein-protein interaction network across vast
            evolutionary distance
  JOURNAL   Mol Syst Biol 12 (4), 865 (2016)
   PUBMED   27107014
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Sprooten,E., Fleming,K.M., Thomson,P.A., Bastin,M.E., Whalley,H.C.,
            Hall,J., Sussmann,J.E., McKirdy,J., Blackwood,D., Lawrie,S.M. and
            McIntosh,A.M.
  TITLE     White matter integrity as an intermediate phenotype: exploratory
            genome-wide association analysis in individuals at high risk of
            bipolar disorder
  JOURNAL   Psychiatry Res 206 (2-3), 223-231 (2013)
   PUBMED   23218918
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK126033.1, AL035460.15 and AL161656.20.
            
            On Dec 29, 2015 this sequence version replaced XP_005260690.1.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK126033.1, DB083501.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
     Protein         1..195
                     /product="transmembrane protein 239 isoform 1"
                     /calculated_mol_wt=21711
     Region          45..193
                     /region_name="TMEM239"
                     /note="Transmembrane protein 239 family; pfam15841"
                     /db_xref="CDD:374162"
     Site            105..125
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WW34.3)"
     Site            145..171
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8WW34.3)"
     CDS             1..195
                     /gene="TMEM239"
                     /coded_by="NM_001318207.1:34..621"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS82595.1"
                     /db_xref="GeneID:100288797"
                     /db_xref="HGNC:HGNC:40044"
ORIGIN      
        1 mrvgtwiclp grpgrcrkqh dlgncpevpg ifktlalspg apdmmqqprv etdtigageg
       61 pqqavpwsaw vtrhgwvrww vshmppswiq wwstsnwrqp lqrllwgleg ilylllalml
      121 chalfttgsh llsslwpvva avwrhllpal lllvlsalpa llftasflll fstllslvgl
      181 ltsmthpgdt qdldq
//
LOCUS       NP_001308519             492 aa            linear   PRI 20-NOV-2025
DEFINITION  calcium/calmodulin-dependent protein kinase type II subunit delta
            isoform 28 [Homo sapiens].
ACCESSION   NP_001308519
VERSION     NP_001308519.1
DBSOURCE    REFSEQ: accession NM_001321590.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 492)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 492)
  AUTHORS   Rigter,P.M.F., de Konink,C., Dunn,M.J., Proietti Onori,M.,
            Humberson,J.B., Thomas,M., Barnes,C., Prada,C.E., Weaver,K.N.,
            Ryan,T.D., Caluseriu,O., Conway,J., Calamaro,E., Fong,C.T.,
            Wuyts,W., Meuwissen,M., Hordijk,E., Jonkers,C.N., Anderson,L.,
            Yuseinova,B., Polonia,S., Beysen,D., Stark,Z., Savva,E.,
            Poulton,C., McKenzie,F., Bhoj,E., Bupp,C.P., Bezieau,S.,
            Mercier,S., Blevins,A., Wentzensen,I.M., Xia,F., Rosenfeld,J.A.,
            Hsieh,T.C., Krawitz,P.M., Elbracht,M., Veenma,D.C.M., Schulman,H.,
            Stratton,M.M., Kury,S. and van Woerden,G.M.
  TITLE     Role of CAMK2D in neurodevelopment and associated conditions
  JOURNAL   Am J Hum Genet 111 (2), 364-382 (2024)
   PUBMED   38272033
  REMARK    GeneRIF: Role of CAMK2D in neurodevelopment and associated
            conditions.
            Erratum:[Am J Hum Genet. 2025 Sep 4;112(9):2247. doi:
            10.1016/j.ajhg.2025.08.001. PMID: 40795868]
REFERENCE   3  (residues 1 to 492)
  AUTHORS   Chuah,Y.H., Tay,E.X.Y., Grinchuk,O.V., Yoon,J., Feng,J., Kannan,S.,
            Robert,M., Jakhar,R., Liang,Y., Lee,B.W.L., Wang,L.C., Lim,Y.T.,
            Zhao,T., Sobota,R.M., Lu,G., Low,B.C., Crasta,K.C., Verma,C.S.,
            Lin,Z. and Ong,D.S.T.
  TITLE     CAMK2D serves as a molecular scaffold for RNF8-MAD2 complex to
            induce mitotic checkpoint in glioma
  JOURNAL   Cell Death Differ 30 (8), 1973-1987 (2023)
   PUBMED   37468549
  REMARK    GeneRIF: CAMK2D serves as a molecular scaffold for RNF8-MAD2
            complex to induce mitotic checkpoint in glioma.
REFERENCE   4  (residues 1 to 492)
  AUTHORS   Saddouk,F.Z., Ginnan,R. and Singer,H.A.
  TITLE     Ca2+/Calmodulin-Dependent Protein Kinase II in Vascular Smooth
            Muscle
  JOURNAL   Adv Pharmacol 78, 171-202 (2017)
   PUBMED   28212797
  REMARK    Review article
REFERENCE   5  (residues 1 to 492)
  AUTHORS   Bhattacharyya,M., Stratton,M.M., Going,C.C., McSpadden,E.D.,
            Huang,Y., Susa,A.C., Elleman,A., Cao,Y.M., Pappireddi,N.,
            Burkhardt,P., Gee,C.L., Barros,T., Schulman,H., Williams,E.R. and
            Kuriyan,J.
  TITLE     Molecular mechanism of activation-triggered subunit exchange in
            Ca(2+)/calmodulin-dependent protein kinase II
  JOURNAL   Elife 5, e13405 (2016)
   PUBMED   26949248
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 492)
  AUTHORS   Hudmon,A. and Schulman,H.
  TITLE     Neuronal CA2+/calmodulin-dependent protein kinase II: the role of
            structure and autoregulation in cellular function
  JOURNAL   Annu Rev Biochem 71, 473-510 (2002)
   PUBMED   12045104
  REMARK    Review article
REFERENCE   7  (residues 1 to 492)
  AUTHORS   Soderling,T.R. and Stull,J.T.
  TITLE     Structure and regulation of calcium/calmodulin-dependent protein
            kinases
  JOURNAL   Chem Rev 101 (8), 2341-2352 (2001)
   PUBMED   11749376
  REMARK    Review article
REFERENCE   8  (residues 1 to 492)
  AUTHORS   Williams,C.L., Phelps,S.H. and Porter,R.A.
  TITLE     Expression of Ca2+/calmodulin-dependent protein kinase types II and
            IV, and reduced DNA synthesis due to the Ca2+/calmodulin-dependent
            protein kinase inhibitor KN-62
            (1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenyl
            piperazine) in small cell lung carcinoma
  JOURNAL   Biochem Pharmacol 51 (5), 707-715 (1996)
   PUBMED   8615909
REFERENCE   9  (residues 1 to 492)
  AUTHORS   de Groot,R.P., den Hertog,J., Vandenheede,J.R., Goris,J. and
            Sassone-Corsi,P.
  TITLE     Multiple and cooperative phosphorylation events regulate the CREM
            activator function
  JOURNAL   EMBO J 12 (10), 3903-3911 (1993)
   PUBMED   8404858
REFERENCE   10 (residues 1 to 492)
  AUTHORS   Sakagami,H. and Kondo,H.
  TITLE     Differential expression of mRNAs encoding gamma and delta subunits
            of Ca2+/calmodulin-dependent protein kinase type II (CaM kinase II)
            in the mature and postnatally developing rat brain
  JOURNAL   Brain Res Mol Brain Res 20 (1-2), 51-63 (1993)
   PUBMED   8255181
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC004168.2, AC004056.1 and
            AC093900.3.
            
            Summary: The product of this gene belongs to the serine/threonine
            protein kinase family and to the Ca(2+)/calmodulin-dependent
            protein kinase subfamily. Calcium signaling is crucial for several
            aspects of plasticity at glutamatergic synapses. In mammalian
            cells, the enzyme is composed of four different chains: alpha,
            beta, gamma, and delta. The product of this gene is a delta chain.
            Alternative splicing results in multiple transcript variants
            encoding distinct isoforms. Distinct isoforms of this chain have
            different expression patterns.[provided by RefSeq, Nov 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1660803.18385.1,
                                           SRR1660805.56682.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..492
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q26"
     Protein         1..492
                     /product="calcium/calmodulin-dependent protein kinase type
                     II subunit delta isoform 28"
                     /EC_number="2.7.11.17"
                     /note="calcium/calmodulin-dependent protein kinase (CaM
                     kinase) II delta; calcium/calmodulin-dependent protein
                     kinase type II delta chain; CaM-kinase II delta chain; CaM
                     kinase II delta subunit; CaMK-II delta subunit;
                     calcium/calmodulin-dependent protein kinase type II
                     subunit delta"
                     /calculated_mol_wt=55515
     Region          12..303
                     /region_name="STKc_CaMKII"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Calcium/calmodulin-dependent protein kinase Type II;
                     cd14086"
                     /db_xref="CDD:270988"
     Site            order(20..24,28,41,43,74,90..93,97,99,135..136,138,
                     140..141,143,156..157,160,175..179,181)
                     /site_type="active"
                     /db_xref="CDD:270988"
     Site            order(20..23,28,41,43,74,90..93,97,140..141,143,156..157)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270988"
     Site            order(24,97,99,135..136,138,140,160,175..179,181)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270988"
     Site            order(156..166,169..179)
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270988"
     Site            order(294,296..303)
                     /site_type="other"
                     /note="CaM binding site [polypeptide binding]"
                     /db_xref="CDD:270988"
     Region          360..487
                     /region_name="CaMKII_AD"
                     /note="Calcium/calmodulin dependent protein kinase II
                     association domain; pfam08332"
                     /db_xref="CDD:285524"
     CDS             1..492
                     /gene="CAMK2D"
                     /gene_synonym="CAMKD"
                     /coded_by="NM_001321590.2:671..2149"
                     /note="isoform 28 is encoded by transcript variant 31"
                     /db_xref="GeneID:817"
                     /db_xref="HGNC:HGNC:1462"
                     /db_xref="MIM:607708"
ORIGIN      
        1 mastttctrf tdeyqlfeel gkgafsvvrr cmkiptgqey aakiintkkl sardhqkler
       61 earicrllkh pnivrlhdsi seegfhylvf dlvtggelfe divareyyse adashciqqi
      121 lesvnhchln givhrdlkpe nlllaskskg aavkladfgl aievqgdqqa wfgfagtpgy
      181 lspevlrkdp ygkpvdmwac gvilyillvg yppfwdedqh rlyqqikaga ydfpspewdt
      241 vtpeakdlin kmltinpakr itasealkhp wicqrstvas mmhrqetvdc lkkfnarrkl
      301 kgailttmla trnfsaaksl lkkpdgvkep qttvihnpdg nkestessnt tiededvkar
      361 kqeiikvteq lieainngdf eaytkicdpg ltafepealg nlvegmdfhr fyfenalsks
      421 nkpihtiiln phvhlvgdda aciayirltq ymdgsgmpkt mqseetrvwh rrdgkwqnvh
      481 fhrsgsptvp in
//
LOCUS       NP_001353519             833 aa            linear   PRI 20-NOV-2025
DEFINITION  serine/arginine repetitive matrix protein 1 isoform 10 [Homo
            sapiens].
ACCESSION   NP_001353519 XP_011538784
VERSION     NP_001353519.1
DBSOURCE    REFSEQ: accession NM_001366590.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 833)
  AUTHORS   Zhan,X., Lu,Y. and Shi,Y.
  TITLE     Molecular basis for the activation of human spliceosome
  JOURNAL   Nat Commun 15 (1), 6348 (2024)
   PUBMED   39068178
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 833)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   3  (residues 1 to 833)
  AUTHORS   Qin,Y., Huttlin,E.L., Winsnes,C.F., Gosztyla,M.L., Wacheul,L.,
            Kelly,M.R., Blue,S.M., Zheng,F., Chen,M., Schaffer,L.V., Licon,K.,
            Backstrom,A., Vaites,L.P., Lee,J.J., Ouyang,W., Liu,S.N., Zhang,T.,
            Silva,E., Park,J., Pitea,A., Kreisberg,J.F., Gygi,S.P., Ma,J.,
            Harper,J.W., Yeo,G.W., Lafontaine,D.L.J., Lundberg,E. and Ideker,T.
  TITLE     A multi-scale map of cell structure fusing protein images and
            interactions
  JOURNAL   Nature 600 (7889), 536-542 (2021)
   PUBMED   34819669
REFERENCE   4  (residues 1 to 833)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   5  (residues 1 to 833)
  AUTHORS   Bai,R., Wan,R., Wang,L., Xu,K., Zhang,Q., Lei,J. and Shi,Y.
  TITLE     Structure of the activated human minor spliceosome
  JOURNAL   Science 371 (6535) (2021)
   PUBMED   33509932
REFERENCE   6  (residues 1 to 833)
  AUTHORS   Blencowe,B.J., Bauren,G., Eldridge,A.G., Issner,R., Nickerson,J.A.,
            Rosonina,E. and Sharp,P.A.
  TITLE     The SRm160/300 splicing coactivator subunits
  JOURNAL   RNA 6 (1), 111-120 (2000)
   PUBMED   10668804
REFERENCE   7  (residues 1 to 833)
  AUTHORS   Eldridge,A.G., Li,Y., Sharp,P.A. and Blencowe,B.J.
  TITLE     The SRm160/300 splicing coactivator is required for exon-enhancer
            function
  JOURNAL   Proc Natl Acad Sci U S A 96 (11), 6125-6130 (1999)
   PUBMED   10339552
REFERENCE   8  (residues 1 to 833)
  AUTHORS   Wilson,K.F., Fortes,P., Singh,U.S., Ohno,M., Mattaj,I.W. and
            Cerione,R.A.
  TITLE     The nuclear cap-binding complex is a novel target of growth factor
            receptor-coupled signal transduction
  JOURNAL   J Biol Chem 274 (7), 4166-4173 (1999)
   PUBMED   9933612
REFERENCE   9  (residues 1 to 833)
  AUTHORS   Blencowe,B.J., Issner,R., Nickerson,J.A. and Sharp,P.A.
  TITLE     A coactivator of pre-mRNA splicing
  JOURNAL   Genes Dev 12 (7), 996-1009 (1998)
   PUBMED   9531537
REFERENCE   10 (residues 1 to 833)
  AUTHORS   Wang,H.Y., Lin,W., Dyck,J.A., Yeakley,J.M., Songyang,Z.,
            Cantley,L.C. and Fu,X.D.
  TITLE     SRPK2: a differentially expressed SR protein-specific kinase
            involved in mediating the interaction and localization of pre-mRNA
            splicing factors in mammalian cells
  JOURNAL   J Cell Biol 140 (4), 737-750 (1998)
   PUBMED   9472028
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL445686.14 and AL445648.18.
            
            On Oct 11, 2018 this sequence version replaced XP_011538784.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.265650.1,
                                           SRR1803616.73311.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..833
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.11"
     Protein         1..833
                     /product="serine/arginine repetitive matrix protein 1
                     isoform 10"
                     /note="serine/arginine repetitive matrix protein 1;
                     Ser/Arg-related nuclear matrix protein; SR-related nuclear
                     matrix protein of 160 kDa"
                     /calculated_mol_wt=93988
     Region          <1..32
                     /region_name="PWI"
                     /note="PWI domain; pfam01480"
                     /db_xref="CDD:460224"
     Region          <535..>669
                     /region_name="PHA03307"
                     /note="transcriptional regulator ICP4; Provisional"
                     /db_xref="CDD:223039"
     CDS             1..833
                     /gene="SRRM1"
                     /gene_synonym="160-KD; POP101; SRM160"
                     /coded_by="NM_001366590.1:2055..4556"
                     /note="isoform 10 is encoded by transcript variant 30"
                     /db_xref="GeneID:10250"
                     /db_xref="HGNC:HGNC:16638"
                     /db_xref="MIM:605975"
ORIGIN      
        1 mmqinltgfl ngknarefmg elwplllsaq eniagipsaf lelkkeeikq rqieqeklas
       61 mkkqdedkdk rdkeekessr ekrersrspr rrksrspspr rrsspvrrer krshsrsprh
      121 rtksrspspa pekkektpel pepsvkvkep svqeatstsd ilkvpkpepi pepkepspek
      181 nskkekekek trprsrsrsk srsrtrsrsp shtrprrrhr srsrsysprr rpsprrrpsp
      241 rrrtpprrmp ppprhrrsrs pvrrrrrssa slsgssssss ssrsrsppkk ppkrtssppr
      301 ktrrlspsas pprrrhrpsp patpppktrh sptpqqsnrt rksrvsvspg rtsvtkhkgt
      361 ekrespspap kprkvelses eedkggkmaa adsvqqrrqy rrqnqqsssd sgsssssede
      421 rpkrshvkng evgrrrrhsp srsaspsprk rqketsprmq mgkrwqspvt ksgrrrrsps
      481 ppptrrrrsp spappprrrr tptppprrrt psppprrrsp sprrysppiq rryspspppk
      541 rrtasppppp krraspsppp krrvshsppp kqrsspvtkr rspslsskhr kgsspsrstr
      601 earspqpnkr hspsprprap qtssspppvr rgassspqrr qspspstrpi rrvsrtpepk
      661 kikkaaspsp qsvrrvsssr svsgspepaa kkppappspv qsqspstnws pavpvkkaks
      721 ptpspspprn sdqegggkkk kkkkdkkhkk dkkhkkhkkh kkekavaaaa aaavtpaaia
      781 aatttlaqee pvaapepkke teseaednld dlekhlreka lrsmrkaqvs pqs
//
LOCUS       NP_001146918             122 aa            linear   PRI 20-NOV-2025
DEFINITION  short coiled-coil protein isoform 4 [Homo sapiens].
ACCESSION   NP_001146918
VERSION     NP_001146918.1
DBSOURCE    REFSEQ: accession NM_001153446.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 122)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 122)
  AUTHORS   Wirth,M., Mouilleron,S., Zhang,W., Sjottem,E., Princely Abudu,Y.,
            Jain,A., Lauritz Olsvik,H., Bruun,J.A., Razi,M., Jefferies,H.B.J.,
            Lee,R., Joshi,D., O'Reilly,N., Johansen,T. and Tooze,S.A.
  TITLE     Phosphorylation of the LIR Domain of SCOC Modulates ATG8 Binding
            Affinity and Specificity
  JOURNAL   J Mol Biol 433 (13), 166987 (2021)
   PUBMED   33845085
  REMARK    GeneRIF: Phosphorylation of the LIR Domain of SCOC Modulates ATG8
            Binding Affinity and Specificity.
            Erratum:[J Mol Biol. 2021 Jul 23;433(15):167049. doi:
            10.1016/j.jmb.2021.167049. PMID: 34052024]
REFERENCE   3  (residues 1 to 122)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 122)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (residues 1 to 122)
  AUTHORS   Stringer,S., Minica,C.C., Verweij,K.J., Mbarek,H., Bernard,M.,
            Derringer,J., van Eijk,K.R., Isen,J.D., Loukola,A.,
            Maciejewski,D.F., Mihailov,E., van der Most,P.J., Sanchez-Mora,C.,
            Roos,L., Sherva,R., Walters,R., Ware,J.J., Abdellaoui,A.,
            Bigdeli,T.B., Branje,S.J., Brown,S.A., Bruinenberg,M., Casas,M.,
            Esko,T., Garcia-Martinez,I., Gordon,S.D., Harris,J.M.,
            Hartman,C.A., Henders,A.K., Heath,A.C., Hickie,I.B., Hickman,M.,
            Hopfer,C.J., Hottenga,J.J., Huizink,A.C., Irons,D.E., Kahn,R.S.,
            Korhonen,T., Kranzler,H.R., Krauter,K., van Lier,P.A., Lubke,G.H.,
            Madden,P.A., Magi,R., McGue,M.K., Medland,S.E., Meeus,W.H.,
            Miller,M.B., Montgomery,G.W., Nivard,M.G., Nolte,I.M.,
            Oldehinkel,A.J., Pausova,Z., Qaiser,B., Quaye,L.,
            Ramos-Quiroga,J.A., Richarte,V., Rose,R.J., Shin,J.,
            Stallings,M.C., Stiby,A.I., Wall,T.L., Wright,M.J., Koot,H.M.,
            Paus,T., Hewitt,J.K., Ribases,M., Kaprio,J., Boks,M.P., Snieder,H.,
            Spector,T., Munafo,M.R., Metspalu,A., Gelernter,J., Boomsma,D.I.,
            Iacono,W.G., Martin,N.G., Gillespie,N.A., Derks,E.M. and Vink,J.M.
  TITLE     Genome-wide association study of lifetime cannabis use based on a
            large meta-analytic sample of 32 330 subjects from the
            International Cannabis Consortium
  JOURNAL   Transl Psychiatry 6 (3), e769 (2016)
   PUBMED   27023175
  REMARK    GeneRIF: SCOC SNPs were associated with lifetime cannabis use, but
            the association did not reach genome-wide significance.
            [Meta-Analysis]
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 122)
  AUTHORS   Alborghetti,M.R., Furlan Ada,S., da Silva,J.C., Sforca,M.L.,
            Honorato,R.V., Granato,D.C., dos Santos Migueleti,D.L., Neves,J.L.,
            de Oliveira,P.S., Paes-Leme,A.F., Zeri,A.C., de Torriani,I.C. and
            Kobarg,J.
  TITLE     Structural analysis of intermolecular interactions in the kinesin
            adaptor complex fasciculation and elongation protein zeta 1/ short
            coiled-coil protein (FEZ1/SCOCO)
  JOURNAL   PLoS One 8 (10), e76602 (2013)
   PUBMED   24116125
  REMARK    GeneRIF: Studies indicate that FEZ1 (fasciculation and elongation
            protein zeta 1), SCOCO (short coiled-coil protein) and kinesins
            (kinesin heavy chain) are involved in biological transport process.
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 122)
  AUTHORS   Behrens,C., Binotti,B., Schmidt,C., Robinson,C.V., Chua,J.J. and
            Kuhnel,K.
  TITLE     Crystal structure of the human short coiled coil protein and
            insights into SCOC-FEZ1 complex formation
  JOURNAL   PLoS One 8 (10), e76355 (2013)
   PUBMED   24098481
  REMARK    GeneRIF: SCOC forms a stable homogeneous complex with the coiled
            coil domain of FEZ1. SCOC dimerization and the SCOC surface residue
            R117 are important for this interaction.
            Erratum:[PLoS One. 2013;8(10).
            doi:10.1371/annotation/cb60d973-58aa-45e0-bbb3-1c7f5a42a8d2]
            Publication Status: Online-Only
REFERENCE   8  (residues 1 to 122)
  AUTHORS   McKnight,N.C., Jefferies,H.B., Alemu,E.A., Saunders,R.E.,
            Howell,M., Johansen,T. and Tooze,S.A.
  TITLE     Genome-wide siRNA screen reveals amino acid starvation-induced
            autophagy requires SCOC and WAC
  JOURNAL   EMBO J 31 (8), 1931-1946 (2012)
   PUBMED   22354037
  REMARK    GeneRIF: The identification of SCOC and WAC as novel regulatory
            proteins with diverse functions in autophagy contributes towards a
            fuller understanding of autophagosome formation.
REFERENCE   9  (residues 1 to 122)
  AUTHORS   Miyamoto-Sato,E., Fujimori,S., Ishizaka,M., Hirai,N., Masuoka,K.,
            Saito,R., Ozawa,Y., Hino,K., Washio,T., Tomita,M., Yamashita,T.,
            Oshikubo,T., Akasaka,H., Sugiyama,J., Matsumoto,Y. and Yanagawa,H.
  TITLE     A comprehensive resource of interacting protein regions for
            refining human transcription factor networks
  JOURNAL   PLoS One 5 (2), e9289 (2010)
   PUBMED   20195357
  REMARK    Publication Status: Online-Only
REFERENCE   10 (residues 1 to 122)
  AUTHORS   Van Valkenburgh,H., Shern,J.F., Sharer,J.D., Zhu,X. and Kahn,R.A.
  TITLE     ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
            specific and shared effectors: characterizing ARL1-binding proteins
  JOURNAL   J Biol Chem 276 (25), 22826-22837 (2001)
   PUBMED   11303027
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB204055.1, AF448857.1 and
            AA213765.1.
            
            Summary: This gene encodes a short coiled-coiled domain-containing
            protein that localizes to the Golgi apparatus. The encoded protein
            interacts with ADP-ribosylation factor-like proteins. Pseudogenes
            of this gene are found on chromosomes 1 and 14. Alternative
            splicing results in multiple transcript variants. [provided by
            RefSeq, Apr 2009].
            
            Transcript Variant: This variant (6) differs in the 5' UTR and 5'
            coding region, compared to variant 1, resulting in an isoform (4)
            with a distinct and shorter N-terminus, compared to isoform 1.
            Variants 4, 5 and 6 encode the same isoform.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB204055.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1970526, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..122
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q31.1"
     Protein         1..122
                     /product="short coiled-coil protein isoform 4"
                     /calculated_mol_wt=13797
     Region          53..113
                     /region_name="DUF2205"
                     /note="Short coiled-coil protein; pfam10224"
                     /db_xref="CDD:431150"
     CDS             1..122
                     /gene="SCOC"
                     /gene_synonym="HRIHFB2072; SCOCO; UNC-69"
                     /coded_by="NM_001153446.1:46..414"
                     /note="isoform 4 is encoded by transcript variant 6"
                     /db_xref="CCDS:CCDS3750.1"
                     /db_xref="GeneID:60592"
                     /db_xref="HGNC:HGNC:20335"
ORIGIN      
        1 mdgsrkeeee dstftnisla ddidhssril yprpksllpk mmnadmdavd aenqveleek
       61 trlinqvlel qhtledlsar vdavkeenlk lksenqvlgq yienlmsass vfqttdtksk
      121 rk
//
LOCUS       NP_001305964            2519 aa            linear   PRI 20-NOV-2025
DEFINITION  telomerase protein component 1 isoform 2 [Homo sapiens].
ACCESSION   NP_001305964
VERSION     NP_001305964.1
DBSOURCE    REFSEQ: accession NM_001319035.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2519)
  AUTHORS   Taube,M., Lisiak,N., Toton,E. and Rubis,B.
  TITLE     Human Vault RNAs: Exploring Their Potential Role in Cellular
            Metabolism
  JOURNAL   Int J Mol Sci 25 (7), 4072 (2024)
   PUBMED   38612882
  REMARK    Review article
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 2519)
  AUTHORS   Wang,Y., Xu,Y., Li,H., Tang,T., Qiao,Y., Cheng,Y., Zhang,L.,
            Song,J., Su,Y., Zhang,X., Wang,J., Shang,Q., Song,L., Gao,C.,
            Zhu,D., Wang,X., Zhu,C. and Xing,Q.
  TITLE     TEP1 is a risk gene for sporadic cerebral palsy
  JOURNAL   J Genet Genomics 48 (12), 1134-1138 (2021)
   PUBMED   34543729
  REMARK    GeneRIF: TEP1 is a risk gene for sporadic cerebral palsy.
REFERENCE   3  (residues 1 to 2519)
  AUTHORS   Pietras,P., Lesniczak-Staszak,M., Kasprzak,A., Andrzejewska,M.,
            Jopek,K., Sowinski,M., Rucinski,M., Lyons,S.M., Ivanov,P. and
            Szaflarski,W.
  TITLE     MVP Expression Facilitates Tumor Cell Proliferation and Migration
            Supporting the Metastasis of Colorectal Cancer Cells
  JOURNAL   Int J Mol Sci 22 (22), 12121 (2021)
   PUBMED   34829999
  REMARK    GeneRIF: MVP Expression Facilitates Tumor Cell Proliferation and
            Migration Supporting the Metastasis of Colorectal Cancer Cells.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 2519)
  AUTHORS   Li,S., Song,F., Lei,X., Li,J., Li,F. and Tan,H.
  TITLE     hsa_circ_0004018 suppresses the progression of liver fibrosis
            through regulating the hsa-miR-660-3p/TEP1 axis
  JOURNAL   Aging (Albany NY) 12 (12), 11517-11529 (2020)
   PUBMED   32584784
  REMARK    GeneRIF: hsa_circ_0004018 suppresses the progression of liver
            fibrosis through regulating the hsa-miR-660-3p/TEP1 axis.
            Erratum:[Aging (Albany NY). 2021 Jun 15;13(11):15690. doi:
            10.18632/aging.203218. PMID: 34129523]
REFERENCE   5  (residues 1 to 2519)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 2519)
  AUTHORS   Li,H., Zhao,L., Yang,Z., Funder,J.W. and Liu,J.P.
  TITLE     Telomerase is controlled by protein kinase Calpha in human breast
            cancer cells
  JOURNAL   J Biol Chem 273 (50), 33436-33442 (1998)
   PUBMED   9837921
REFERENCE   7  (residues 1 to 2519)
  AUTHORS   Harrington,L., Zhou,W., McPhail,T., Oulton,R., Yeung,D.S., Mar,V.,
            Bass,M.B. and Robinson,M.O.
  TITLE     Human telomerase contains evolutionarily conserved catalytic and
            structural subunits
  JOURNAL   Genes Dev 11 (23), 3109-3115 (1997)
   PUBMED   9389643
REFERENCE   8  (residues 1 to 2519)
  AUTHORS   Saito,T., Matsuda,Y., Suzuki,T., Hayashi,A., Yuan,X., Saito,M.,
            Nakayama,J., Hori,T. and Ishikawa,F.
  TITLE     Comparative gene mapping of the human and mouse TEP1 genes, which
            encode one protein component of telomerases
  JOURNAL   Genomics 46 (1), 46-50 (1997)
   PUBMED   9403057
REFERENCE   9  (residues 1 to 2519)
  AUTHORS   Harrington,L., McPhail,T., Mar,V., Zhou,W., Oulton,R., Bass,M.B.,
            Arruda,I. and Robinson,M.O.
  TITLE     A mammalian telomerase-associated protein
  JOURNAL   Science 275 (5302), 973-977 (1997)
   PUBMED   9020079
REFERENCE   10 (residues 1 to 2519)
  AUTHORS   Joly,E.C., Tremblay,E., Tanguay,R.M., Wu,Y. and Bibor-Hardy,V.
  TITLE     TRiC-P5, a novel TCP1-related protein, is localized in the
            cytoplasm and in the nuclear matrix
  JOURNAL   J Cell Sci 107 (Pt 10), 2851-2859 (1994)
   PUBMED   7876352
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL355075.6.
            
            Summary: This gene product is a component of the ribonucleoprotein
            complex responsible for telomerase activity which catalyzes the
            addition of new telomeres on the chromosome ends. The
            telomerase-associated proteins are conserved from ciliates to
            humans. Alternative splicing results in multiple transcript
            variants. [provided by RefSeq, Jan 2016].
            
            Transcript Variant: This variant (2) lacks alternate in-frame exons
            in the 5' coding region compared to variant 1. The encoded isoform
            (2) is shorter, compared to isoform 1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC143815.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..2519
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.2"
     Protein         1..2519
                     /product="telomerase protein component 1 isoform 2"
                     /note="TROVE domain family, member 1; p80 telomerase
                     homolog; telomerase protein component 1; telomerase
                     protein 1"
                     /calculated_mol_wt=277894
     Region          1..30
                     /region_name="TEP1 N-terminal 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99973.2)"
     Region          1..29
                     /region_name="TEP1_N"
                     /note="TEP1 N-terminal domain; pfam05386"
                     /db_xref="CDD:428450"
     Region          31..60
                     /region_name="TEP1 N-terminal 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99973.2)"
     Region          31..59
                     /region_name="TEP1_N"
                     /note="TEP1 N-terminal domain; pfam05386"
                     /db_xref="CDD:428450"
     Region          61..90
                     /region_name="TEP1 N-terminal 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99973.2)"
     Region          61..89
                     /region_name="TEP1_N"
                     /note="TEP1 N-terminal domain; pfam05386"
                     /db_xref="CDD:428450"
     Region          91..120
                     /region_name="TEP1 N-terminal 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99973.2)"
     Region          91..119
                     /region_name="TEP1_N"
                     /note="TEP1 N-terminal domain; pfam05386"
                     /db_xref="CDD:428450"
     Region          193..214
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99973.2)"
     Region          226..568
                     /region_name="TROVE"
                     /note="TROVE domain; pfam05731"
                     /db_xref="CDD:461724"
     Region          579..781
                     /region_name="DUF5920"
                     /note="Domain of unknown function (DUF5920); pfam19334"
                     /db_xref="CDD:466045"
     Region          792..900
                     /region_name="DUF4062"
                     /note="Domain of unknown function (DUF4062); pfam13271"
                     /db_xref="CDD:463823"
     Region          1054..1229
                     /region_name="NACHT"
                     /note="NACHT domain; pfam05729"
                     /db_xref="CDD:428606"
     Region          <1572..1850
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          1572..1608
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1614..1649
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1654..1693
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1696..1732
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1737..1773
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1741..2160
                     /region_name="WD40"
                     /note="WD40 repeat [General function prediction only];
                     COG2319"
                     /db_xref="CDD:441893"
     Region          1780..1815
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1864..1905
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1908..1951
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          1956..1995
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2003..2037
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2043..2127
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2123..>2283
                     /region_name="WD40"
                     /note="WD40 domain, found in a number of eukaryotic
                     proteins that cover a wide variety of functions including
                     adaptor/regulatory modules in signal transduction,
                     pre-mRNA processing and cytoskeleton assembly; typically
                     contains a GH dipeptide 11-24 residues from...; cl29593"
                     /db_xref="CDD:475233"
     Region          2133..2172
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2175..2199
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2218..2251
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     Region          2264..2310
                     /region_name="WD40 repeat"
                     /note="WD40 repeat [structural motif]"
                     /db_xref="CDD:293791"
     CDS             1..2519
                     /gene="TEP1"
                     /gene_synonym="p240; TLP1; TP1; TROVE1; VAULT2"
                     /coded_by="NM_001319035.2:122..7681"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS81789.1"
                     /db_xref="GeneID:7011"
                     /db_xref="HGNC:HGNC:11726"
                     /db_xref="MIM:601686"
ORIGIN      
        1 meklhghvsa hpdilslenr clamlpdlqp leklhqhvst hsdilslknq clatlpdlkt
       61 mekphgyvsa hpdilslenq clatlsdlkt mekphghvsa hpdilslenr clatlsslks
      121 tvsasplfqs lqishmtqad lyrvnnsncl lseppswraq hfskgldlst cpialksisa
      181 tetaqeatlg rwfdseekkg aetqmpsysl slgeeeeved lavkltsgds eshpeptdhv
      241 lqekkmalls llcstlvsev nmnntsdptl aaifeicrel allepefilk gmeppfshrc
      301 fpryigflre eqrkfekagd tvsekknppr ftlkklvqrl hihkpaqhvq allgyrypsn
      361 lqlfsrsrlp gpwdssragk rmklsrpetw erelslrgnk asvweelien gklpfmamlr
      421 nlcnllrvgi ssrhhelilq rlqhaksvih srqfpfrfln ahdaidalea qlrnqalpfp
      481 snitlmrril trneknrprr rflchlsrqq lrmamripvl yeqlkreklr vhkarqwkyd
      541 gemlnryrqa letavnlsvk hslpllpgrt vlvyltdana drlcpksnpq gpplnyalll
      601 igmmitraeq vdvvlcggdt lktavlkaee gilktaiklq aqvqefdend gwslntfgky
      661 llslagqrvp vdrvillgqs mddgminvak qlywqrvnsk clfvgillrr vqylstdlnp
      721 ndvtlsgctd ailkfiaehg ashllehvgq mdkifkippp pgktgvqslr pleedtpspl
      781 apvsqqgwrs irlfisstfr dmhgerdlll rsvlpalqar aaphrislhg idlrwgvtee
      841 etrrnrqlev clgevenaql fvgilgsryg yippsynlpd hphfhwaqqy psgrsvteme
      901 vmqflnrnqr lqpsaqaliy frdssflssv pdawksdfvs eseeaarris elksylsrqk
      961 gitcrrypce wggvaagrpy vggleefgql vlqdvwnmiq klylqpgall eqpvsipddd
     1021 lvqatfqqlq kppsparprl lqdtvqrlml phgrlslvtg qsgqgktafl aslvsalqap
     1081 dgakvaslvf fhfsgarpdq glaltllrrl ctylrgqlke pgalpstyrs lvwelqqrll
     1141 pksaeslhpg qtqvliidga drlvdqngql isdwipkklp rcvhlvlsvs sdaglgetle
     1201 qsqgahvlal gpleasarar lvreelalyg krleespfnn qmrlllvkre sgrplylrlv
     1261 tdhlrlftly eqvserlrtl patvplllqh ilstlekehg pdvlpqalta levtrsgltv
     1321 dqlhgvlsvw rtlpkgtksw eeavaagnsg dpypmgpfac lvqslrsllg egplerpgar
     1381 lclpdgplrt aakrcygkrp gledtahili aaqlwktcda dasgtfrscp pealgdlpyh
     1441 llqsgnrgll skfltnlhvv aahlelglvs rlleahalya ssvpkeeqkl peadvavfrt
     1501 flrqqasils qyprllpqqa anqpldsplc hqasllsrrw hlqhtlrwln kprtmknqqs
     1561 sslslavsss ptavafstng qraavgtang tvylldlrtw qeeksvvsgc dgisaclfls
     1621 ddtlfltafd gllelwdlqh gcrvlqtkah qyqitgccls pdcrllatvc lggclklwdt
     1681 vrgqlafqht ypkslncvaf hpegqviatg swagsisffq vdglkvtkdl gapgasirtl
     1741 afnvpggvva vgrldsmvel wawregarla afpahhgfva aalflhagcq lltagedgkv
     1801 qvwsgslgrp rghlgslsls palsvalspd gdrvavgyra dgiriykiss gsqgaqgqal
     1861 dvavsalawl spkvlvsgae dgslqgwalk ecslqslwll srfqkpvlgl atsqellasa
     1921 sedftvqlwp rqlltrphka edfpcgtelr ghegpvsccs fstdggslat ggrdrsllcw
     1981 dvrtpktpvl ihsfpachrd wvtgcawtkd nlliscssdg svglwdpesg qrlgqflghq
     2041 savsavaave ehvvsvsrdg tlkvwdhqgv eltsipahsg pishcaaame praagqpgse
     2101 llvvtvgldg atrlwhpllv cqthtllghs gpvraaavse tsglmltase dgsvrlwqvp
     2161 keaddtcipr ssaavtavaw apdgsmavsg nqagelilwq eakavataqa pghigaliws
     2221 sahtffvlsa dekisewqvk lrkgsapgnl slhlnrilqe dlgvltsldw apdghflila
     2281 kadlkllcmk pgdapseiws sytenpmils thkeygifvl qpkdpgvlsf lrqkesgefe
     2341 erlnfdinle npsrtlisit qakpesessf lcassdgilw nlakcspege wttgnmwqkk
     2401 antpetqtpg tdpstcresd asmdsdasmd septphlktr qrrkihsgsv talhvlpell
     2461 vtaskdrdvk lwerpsmqll glfrcegsvs clepwlgans tlqlavgdvq gnvyflnwe
//
LOCUS       NP_001123484             337 aa            linear   PRI 20-NOV-2025
DEFINITION  Na(+)/H(+) exchange regulatory cofactor NHE-RF2 isoform a [Homo
            sapiens].
ACCESSION   NP_001123484
VERSION     NP_001123484.1
DBSOURCE    REFSEQ: accession NM_001130012.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 337)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 337)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 337)
  AUTHORS   Chevalier,B., Baatallah,N., Najm,M., Castanier,S., Jung,V.,
            Pranke,I., Golec,A., Stoven,V., Marullo,S., Antigny,F.,
            Guerrera,I.C., Sermet-Gaudelus,I., Edelman,A. and Hinzpeter,A.
  TITLE     Differential CFTR-Interactome Proximity Labeling Procedures
            Identify Enrichment in Multiple SLC Transporters
  JOURNAL   Int J Mol Sci 23 (16), 8937 (2022)
   PUBMED   36012204
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 337)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   5  (residues 1 to 337)
  AUTHORS   Zizak,M., Lamprecht,G., Steplock,D., Tariq,N., Shenolikar,S.,
            Donowitz,M., Yun,C.H. and Weinman,E.J.
  TITLE     cAMP-induced phosphorylation and inhibition of Na(+)/H(+) exchanger
            3 (NHE3) are dependent on the presence but not the phosphorylation
            of NHE regulatory factor
  JOURNAL   J Biol Chem 274 (35), 24753-24758 (1999)
   PUBMED   10455146
REFERENCE   6  (residues 1 to 337)
  AUTHORS   Imai,K., Sarker,A.H., Akiyama,K., Ikeda,S., Yao,M., Tsutsui,K.,
            Shohmori,T. and Seki,S.
  TITLE     Genomic structure and sequence of a human homologue (NTHL1/NTH1) of
            Escherichia coli endonuclease III with those of the adjacent parts
            of TSC2 and SLC9A3R2 genes
  JOURNAL   Gene 222 (2), 287-295 (1998)
   PUBMED   9831664
REFERENCE   7  (residues 1 to 337)
  AUTHORS   Yun,C.H., Lamprecht,G., Forster,D.V. and Sidor,A.
  TITLE     NHE3 kinase A regulatory protein E3KARP binds the epithelial brush
            border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin
  JOURNAL   J Biol Chem 273 (40), 25856-25863 (1998)
   PUBMED   9748260
REFERENCE   8  (residues 1 to 337)
  AUTHORS   Hall,R.A., Ostedgaard,L.S., Premont,R.T., Blitzer,J.T., Rahman,N.,
            Welsh,M.J. and Lefkowitz,R.J.
  TITLE     A C-terminal motif found in the beta2-adrenergic receptor, P2Y1
            receptor and cystic fibrosis transmembrane conductance regulator
            determines binding to the Na+/H+ exchanger regulatory factor family
            of PDZ proteins
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8496-8501 (1998)
   PUBMED   9671706
REFERENCE   9  (residues 1 to 337)
  AUTHORS   Yun,C.H., Oh,S., Zizak,M., Steplock,D., Tsao,S., Tse,C.M.,
            Weinman,E.J. and Donowitz,M.
  TITLE     cAMP-mediated inhibition of the epithelial brush border Na+/H+
            exchanger, NHE3, requires an associated regulatory protein
  JOURNAL   Proc Natl Acad Sci U S A 94 (7), 3010-3015 (1997)
   PUBMED   9096337
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1997 Sep 2;94(18):10006]
REFERENCE   10 (residues 1 to 337)
  AUTHORS   Poulat,F., de Santa Barbara,P., Desclozeaux,M., Soullier,S.,
            Moniot,B., Bonneaud,N., Boizet,B. and Berta,P.
  TITLE     The human testis determining factor SRY binds a nuclear factor
            containing PDZ protein interaction domains
  JOURNAL   J Biol Chem 272 (11), 7167-7172 (1997)
   PUBMED   9054412
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014513.1 and AC093513.3.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: This gene encodes a member of the NHERF family of PDZ
            scaffolding proteins. These proteins mediate many cellular
            processes by binding to and regulating the membrane expression and
            protein-protein interactions of membrane receptors and transport
            proteins. The encoded protein plays a role in intestinal sodium
            absorption by regulating the activity of the sodium/hydrogen
            exchanger 3, and may also regulate the cystic fibrosis
            transmembrane regulator (CFTR) ion channel. Alternatively spliced
            transcript variants encoding multiple isoforms have been observed
            for this gene. [provided by RefSeq, Nov 2011].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC014513.1, AF004900.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000424542.7/ ENSP00000408005.2
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..337
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
     Protein         1..337
                     /product="Na(+)/H(+) exchange regulatory cofactor NHE-RF2
                     isoform a"
                     /note="solute carrier family 9, subfamily A (NHE3, cation
                     proton antiporter 3), member 3 regulator 2; Na(+)/H(+)
                     exchange regulatory cofactor NHE-RF2; SRY-interacting
                     protein 1; tyrosine kinase activator protein 1; NHE3
                     kinase A regulatory protein E3KARP; NHE3 regulatory factor
                     2; SLC9A3 regulator 2; sodium/hydrogen exchanger 3 kinase
                     A regulatory protein; solute carrier family 9
                     (sodium/hydrogen exchanger), member 3 regulator 2;
                     Na(+)/H(+) exchange regulatory cofactor 2"
                     /calculated_mol_wt=37283
     Region          10..89
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(20..26,37,40,69,73,76..77)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Region          107..144
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15599.2)"
     Site            130
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Region          150..229
                     /region_name="PDZ_NHERF-like"
                     /note="PDZ domains of the Na+/H+ exchange regulatory
                     cofactor (NHERF) family (NHERF1-4), and related domains;
                     cd06768"
                     /db_xref="CDD:467249"
     Site            order(160..166,177,180,209,213,216..217)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467249"
     Site            183
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Region          232..337
                     /region_name="EBP50_C"
                     /note="EBP50, C-terminal; pfam09007"
                     /db_xref="CDD:462654"
     Region          240..337
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15599.2)"
     Site            254
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            269
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JHL1; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            280
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163,
                     ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     Site            303
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q15599.2)"
     CDS             1..337
                     /gene="NHERF2"
                     /gene_synonym="E3KARP; NHE3RF2; NHERF-2; OCTS2; SIP-1;
                     SIP1; SLC9A3R2; TKA-1"
                     /coded_by="NM_001130012.3:105..1118"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS45382.1"
                     /db_xref="GeneID:9351"
                     /db_xref="HGNC:HGNC:11076"
                     /db_xref="MIM:606553"
ORIGIN      
        1 maapeplrpr lcrlvrgeqg ygfhlhgekg rrgqfirrve pgspaeaaal ragdrlvevn
       61 gvnvegethh qvvqrikave gqtrllvvdq etdeelrrrq ltcteemaqr glppahdpwe
      121 pkpdwahtgs hsseagkkdv sgplrelrpr lchlrkgpqg ygfnlhsdks rpgqyirsvd
      181 pgspaarsgl raqdrlievn gqnveglrha evvasikare dearllvvdp etdehfkrlr
      241 vtpteehveg plpspvtngt spaqlnggsa cssrsdlpgs dkdtedgsaw kqdpfqesgl
      301 hlsptaaeak ekaramrvnk rapqmdwnrk reifsnf
//
LOCUS       NP_003322               1187 aa            linear   PRI 20-NOV-2025
DEFINITION  non-receptor tyrosine-protein kinase TYK2 isoform 2 [Homo sapiens].
ACCESSION   NP_003322
VERSION     NP_003322.3
DBSOURCE    REFSEQ: accession NM_003331.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1187)
  AUTHORS   Chen,H., Ge,X., Li,C., Zeng,J. and Wang,X.
  TITLE     Structure and assembly of the human IL-12 signaling complex
  JOURNAL   Structure 32 (10), 1640-1651 (2024)
   PUBMED   39111304
REFERENCE   2  (residues 1 to 1187)
  AUTHORS   Lesgidou,N. and Vlassi,M.
  TITLE     Community analysis of large-scale molecular dynamics simulations
            elucidated dynamics-driven allostery in tyrosine kinase 2
  JOURNAL   Proteins 92 (4), 474-498 (2024)
   PUBMED   37950407
  REMARK    GeneRIF: Community analysis of large-scale molecular dynamics
            simulations elucidated dynamics-driven allostery in tyrosine kinase
            2.
REFERENCE   3  (residues 1 to 1187)
  AUTHORS   Zhang,M., Liu,Z., Zhu,Y., Wu,K., Zhou,L., Peng,Y., Pan,J., Chen,B.,
            Wang,X. and Chen,S.
  TITLE     Associations of genetic variants within TYK2 with pulmonary
            tuberculosis among Chinese population
  JOURNAL   Mol Genet Genomic Med 12 (2), e2386 (2024)
   PUBMED   38337161
  REMARK    GeneRIF: Associations of genetic variants within TYK2 with
            pulmonary tuberculosis among Chinese population.
REFERENCE   4  (residues 1 to 1187)
  AUTHORS   Benmansour,R., Tagajdid,M.R., El Hamzaoui,H., Fjouji,S., Doghmi,N.,
            Houba,A., Belbacha,I., Elkochri,S., Aabi,R., Elannaz,H.,
            Laraqui,A., El Mchichi,B., Chmitah,T., Touil,N., Ennibi,K.,
            Eljaoudi,R., Elmir,E., Amine Lahlou,I. and Oumzil,H.
  TITLE     TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide polymorphisms among
            severe COVID-19 ICU patients in Morocco
  JOURNAL   Int J Immunopathol Pharmacol 38, 3946320241257241 (2024)
   PUBMED   38760017
  REMARK    GeneRIF: TYK2, IFITM3, IFNAR2 and OAS3 single-nucleotide
            polymorphisms among severe COVID-19 ICU patients in Morocco.
REFERENCE   5  (residues 1 to 1187)
  AUTHORS   Yang,Z., Xiang,Q. and Nicholas,J.
  TITLE     Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2
  JOURNAL   PLoS Pathog 19 (11), e1011806 (2023)
   PUBMED   37983265
  REMARK    GeneRIF: Direct and biologically significant interactions of human
            herpesvirus 8 interferon regulatory factor 1 with STAT3 and Janus
            kinase TYK2.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1187)
  AUTHORS   Tavernier,J., Tuypens,T., Plaetinck,G., Verhee,A., Fiers,W. and
            Devos,R.
  TITLE     Molecular basis of the membrane-anchored and two soluble isoforms
            of the human interleukin 5 receptor alpha subunit
  JOURNAL   Proc Natl Acad Sci U S A 89 (15), 7041-7045 (1992)
   PUBMED   1495999
REFERENCE   7  (residues 1 to 1187)
  AUTHORS   Velazquez,L., Fellous,M., Stark,G.R. and Pellegrini,S.
  TITLE     A protein tyrosine kinase in the interferon alpha/beta signaling
            pathway
  JOURNAL   Cell 70 (2), 313-322 (1992)
   PUBMED   1386289
REFERENCE   8  (residues 1 to 1187)
  AUTHORS   Partanen,J., Makela,T.P., Alitalo,R., Lehvaslaiho,H. and Alitalo,K.
  TITLE     Putative tyrosine kinases expressed in K-562 human leukemia cells
  JOURNAL   Proc Natl Acad Sci U S A 87 (22), 8913-8917 (1990)
   PUBMED   2247464
REFERENCE   9  (residues 1 to 1187)
  AUTHORS   Firmbach-Kraft,I., Byers,M., Shows,T., Dalla-Favera,R. and
            Krolewski,J.J.
  TITLE     tyk2, prototype of a novel class of non-receptor tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (9), 1329-1336 (1990)
   PUBMED   2216457
REFERENCE   10 (residues 1 to 1187)
  AUTHORS   Krolewski,J.J., Lee,R., Eddy,R., Shows,T.B. and Dalla-Favera,R.
  TITLE     Identification and chromosomal mapping of new human tyrosine kinase
            genes
  JOURNAL   Oncogene 5 (3), 277-282 (1990)
   PUBMED   2156206
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DA864169.1, BC014243.2 and
            AK308360.1.
            
            On May 7, 2008 this sequence version replaced NP_003322.2.
            
            Summary: This gene encodes a member of the tyrosine kinase and,
            more specifically, the Janus kinases (JAKs) protein families. This
            protein associates with the cytoplasmic domain of type I and type
            II cytokine receptors and promulgate cytokine signals by
            phosphorylating receptor subunits. It is also a component of both
            the type I and type III interferon signaling pathways. As such, it
            may play a role in anti-viral immunity. A mutation in this gene has
            been associated with Immunodeficiency 35. [provided by RefSeq, Sep
            2020].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: MN842724.1, BC014243.2 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            coronavirus related    :: involved in immune response or antiviral
                                      activity
            MANE Ensembl match     :: ENST00000525621.6/ ENSP00000431885.1
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1187
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     Protein         1..1187
                     /product="non-receptor tyrosine-protein kinase TYK2
                     isoform 2"
                     /EC_number="2.7.10.2"
                     /note="non-receptor tyrosine-protein kinase TYK2"
                     /calculated_mol_wt=133519
     Region          28..125
                     /region_name="FERM_F1"
                     /note="FERM F1 ubiquitin-like domain; pfam18379"
                     /db_xref="CDD:465733"
     Region          143..266
                     /region_name="FERM_F2"
                     /note="FERM F2 acyl-CoA binding protein-like domain;
                     pfam18377"
                     /db_xref="CDD:436450"
     Region          285..432
                     /region_name="Jak1_Phl"
                     /note="Jak1 pleckstrin homology-like domain; pfam17887"
                     /db_xref="CDD:465552"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Region          335..366
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Region          437..534
                     /region_name="SH2"
                     /note="Src homology 2 (SH2) domain; cl15255"
                     /db_xref="CDD:472789"
     Site            order(457,474,504,506)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198244"
     Site            499
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Site            order(505,532)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198244"
     Site            525
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9R117; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          589..867
                     /region_name="PTK_Tyk2_rpt1"
                     /note="Pseudokinase (repeat 1) domain of the Protein
                     Tyrosine Kinase, Tyrosine kinase 2; cd05076"
                     /db_xref="CDD:270661"
     Site            604
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9R117; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          610..629
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P29597.3)"
     Site            884
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18691976,
                     ECO:0007744|PubMed:19369195; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Region          892..1174
                     /region_name="PTKc_Tyk2_rpt2"
                     /note="Catalytic (repeat 2) domain of the Protein Tyrosine
                     Kinase, Tyrosine kinase 2; cd05080"
                     /db_xref="CDD:270664"
     Site            order(903..904,906,911,928,930,960,978..982,984,1023,
                     1027..1028,1030,1040..1041,1060..1064,1073,1121)
                     /site_type="active"
                     /db_xref="CDD:270664"
     Site            order(903..904,906,911,928,930,960,978..982,984,
                     1027..1028,1030,1040..1041)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270664"
     Site            order(1023,1027,1060..1064,1073,1121)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270664"
     Site            1040..1066
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270664"
     Site            1054
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000269|PubMed:20478313,
                     ECO:0000269|PubMed:8702790; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     Site            1055
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:8702790; propagated from
                     UniProtKB/Swiss-Prot (P29597.3)"
     CDS             1..1187
                     /gene="TYK2"
                     /gene_synonym="IMD35; JTK1"
                     /coded_by="NM_003331.5:379..3942"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS12236.1"
                     /db_xref="GeneID:7297"
                     /db_xref="HGNC:HGNC:12440"
                     /db_xref="MIM:176941"
ORIGIN      
        1 mplrhwgmar gskpvgdgaq pmaamgglkv llhwagpggg epwvtfsess ltaeevcihi
       61 ahkvgitppc fnlfalfdaq aqvwlppnhi leiprdaslm lyfrirfyfr nwhgmnprep
      121 avyrcgppgt eassdqtaqg mqlldpasfe ylfeqgkhef vndvaslwel steeeihhfk
      181 neslgmaflh lchlalrhgi pleevakkts fkdciprsfr rhirqhsalt rlrlrnvfrr
      241 flrdfqpgrl sqqmvmvkyl atlerlaprf gtervpvchl rllaqaegep cyirdsgvap
      301 tdpgpesaag ppthevlvtg tggiqwwpve eevnkeegss gssgrnpqas lfgkkakahk
      361 avgqpadrpr eplwayfcdf rdithvvlke hcvsihrqdn kclelslpsr aaalsfvslv
      421 dgyfrltads shylchevap prlvmsirdg ihgpllepfv qaklrpedgl ylihwstshp
      481 yrliltvaqr sqapdgmqsl rlrkfpieqq dgafvlegwg rsfpsvrelg aalqgcllra
      541 gddcfslrrc clpqpgetsn liimrgaras prtlnlsqls fhrvdqkeit qlshlgqgtr
      601 tnvyegrlrv egsgdpeegk mddedplvpg rdrgqelrvv lkvldpshhd ialafyetas
      661 lmsqvshthl afvhgvcvrg penimvteyv ehgpldvwlr rerghvpmaw kmvvaqqlas
      721 alsylenknl vhgnvcgrni llarlglaeg tspfiklsdp gvglgalsre erveripwla
      781 peclpggans lstamdkwgf gatlleicfd geaplqsrsp sekehfyqrq hrlpepscpq
      841 latltsqclt yeptqrpsfr tilrdltrlq phnladvltv npdspasdpt vfhkrylkki
      901 rdlgeghfgk vslycydptn dgtgemvavk alkadcgpqh rsgwkqeidi lrtlyhehii
      961 kykgccedqg ekslqlvmey vplgslrdyl prhsiglaql llfaqqiceg maylhaqhyi
     1021 hrdlaarnvl ldndrlvkig dfglakavpe gheyyrvred gdspvfwyap eclkeykfyy
     1081 asdvwsfgvt lyellthcds sqspptkfle ligiaqgqmt vlrlteller gerlprpdkc
     1141 pcevyhlmkn cweteasfrp tfenlipilk tvhekyqgqa psvfsvc
//
LOCUS       NP_003167                976 aa            linear   PRI 20-NOV-2025
DEFINITION  synaptonemal complex protein 1 isoform 1 [Homo sapiens].
ACCESSION   NP_003167
VERSION     NP_003167.2
DBSOURCE    REFSEQ: accession NM_003176.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 976)
  AUTHORS   Nabi,S., Askari,M., Rezaei-Gazik,M., Salehi,N., Almadani,N.,
            Tahamtani,Y. and Totonchi,M.
  TITLE     A rare frameshift mutation in SYCP1 is associated with human male
            infertility
  JOURNAL   Mol Hum Reprod 28 (4) (2022)
   PUBMED   35377450
  REMARK    GeneRIF: A rare frameshift mutation in SYCP1 is associated with
            human male infertility.
REFERENCE   2  (residues 1 to 976)
  AUTHORS   Dunce,J.M., Dunne,O.M., Ratcliff,M., Millan,C., Madgwick,S.,
            Uson,I. and Davies,O.R.
  TITLE     Structural basis of meiotic chromosome synapsis through SYCP1
            self-assembly
  JOURNAL   Nat Struct Mol Biol 25 (7), 557-569 (2018)
   PUBMED   29915389
  REMARK    GeneRIF: SYCP1 has an obligate tetrameric structure in which an
            N-terminal four-helical bundle bifurcates into two elongated
            C-terminal dimeric coiled-coils. This building block assembles into
            a zipper-like lattice through two self-assembly sites. N-terminal
            sites undergo cooperative head-to-head assembly in the midline,
            while C-terminal sites interact back to back on the chromosome
            axis.
REFERENCE   3  (residues 1 to 976)
  AUTHORS   Seo,E.K., Choi,J.Y., Jeong,J.H., Kim,Y.G. and Park,H.H.
  TITLE     Crystal Structure of C-Terminal Coiled-Coil Domain of SYCP1 Reveals
            Non-Canonical Anti-Parallel Dimeric Structure of Transverse
            Filament at the Synaptonemal Complex
  JOURNAL   PLoS One 11 (8), e0161379 (2016)
   PUBMED   27548613
  REMARK    GeneRIF: Crystal structure of C-terminal coiled-coil domain of
            SYCP1 reveals non-canonical anti-parallel dimeric structure of
            transverse filament at the synaptonemal complex.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 976)
  AUTHORS   Cahoon,C.K. and Hawley,R.S.
  TITLE     Regulating the construction and demolition of the synaptonemal
            complex
  JOURNAL   Nat Struct Mol Biol 23 (5), 369-377 (2016)
   PUBMED   27142324
  REMARK    Review article
REFERENCE   5  (residues 1 to 976)
  AUTHORS   Park,H.H.
  TITLE     X-ray crystallographic studies of the middle part of the human
            synaptonemal complex protein 1 coiled-coil domain
  JOURNAL   Acta Crystallogr F Struct Biol Commun 71 (Pt 9), 1131-1134 (2015)
   PUBMED   26323297
  REMARK    GeneRIF: crystal structure of the middle part of the human
            synaptonemal complex protein 1 coiled-coil domain
REFERENCE   6  (residues 1 to 976)
  AUTHORS   Eichmuller,S., Usener,D., Dummer,R., Stein,A., Thiel,D. and
            Schadendorf,D.
  TITLE     Serological detection of cutaneous T-cell lymphoma-associated
            antigens
  JOURNAL   Proc Natl Acad Sci U S A 98 (2), 629-634 (2001)
   PUBMED   11149944
REFERENCE   7  (residues 1 to 976)
  AUTHORS   Tureci,O., Sahin,U., Zwick,C., Koslowski,M., Seitz,G. and
            Pfreundschuh,M.
  TITLE     Identification of a meiosis-specific protein as a member of the
            class of cancer/testis antigens
  JOURNAL   Proc Natl Acad Sci U S A 95 (9), 5211-5216 (1998)
   PUBMED   9560255
REFERENCE   8  (residues 1 to 976)
  AUTHORS   Meuwissen,R.L., Meerts,I., Hoovers,J.M., Leschot,N.J. and
            Heyting,C.
  TITLE     Human synaptonemal complex protein 1 (SCP1): isolation and
            characterization of the cDNA and chromosomal localization of the
            gene
  JOURNAL   Genomics 39 (3), 377-384 (1997)
   PUBMED   9119375
REFERENCE   9  (residues 1 to 976)
  AUTHORS   Kondoh,N., Nishina,Y., Tsuchida,J., Koga,M., Tanaka,H., Uchida,K.,
            Inazawa,J., Taketo,M., Nozaki,M., Nojima,H., Matsumiya,K.,
            Namiki,M., Okuyama,A. and Nishimune,Y.
  TITLE     Assignment of synaptonemal complex protein 1 (SCP1) to human
            chromosome 1p13 by fluorescence in situ hybridization and its
            expression in the testis
  JOURNAL   Cytogenet Cell Genet 78 (2), 103-104 (1997)
   PUBMED   9371398
REFERENCE   10 (residues 1 to 976)
  AUTHORS   Meuwissen,R.L., Offenberg,H.H., Dietrich,A.J., Riesewijk,A., van
            Iersel,M. and Heyting,C.
  TITLE     A coiled-coil related protein specific for synapsed regions of
            meiotic prophase chromosomes
  JOURNAL   EMBO J 11 (13), 5091-5100 (1992)
   PUBMED   1464329
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BI561137.1, BC126266.1 and AA868393.1.
            
            On Sep 22, 2003 this sequence version replaced NP_003167.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Both variants 1 and 2 encode the same isoform.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC026162.2, HM005504.1 [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000369522.8/ ENSP00000358535.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..976
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13.2"
     Protein         1..976
                     /product="synaptonemal complex protein 1 isoform 1"
                     /note="cancer/testis antigen 8; testicular tissue protein
                     Li 191"
                     /calculated_mol_wt=114061
     Region          28..792
                     /region_name="SCP-1"
                     /note="Synaptonemal complex protein 1 (SCP-1); pfam05483"
                     /db_xref="CDD:114219"
     Region          101..111
                     /region_name="Mediates head to head self-assembly of
                     N-terminal ends. /evidence=ECO:0000269|PubMed:29915389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          117..120
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          206..362
                     /region_name="Interaction with SYCE3.
                     /evidence=ECO:0000269|PubMed:36635604"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          676..770
                     /region_name="Required for pH-induced assembly of
                     C-terminal ends into antiparallel tetramers.
                     /evidence=ECO:0000269|PubMed:29915389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          679..682
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          784..976
                     /region_name="DNA-binding.
                     /evidence=ECO:0000269|PubMed:29915389"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     Region          880..883
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q15431.2)"
     CDS             1..976
                     /gene="SYCP1"
                     /gene_synonym="CT8; HOM-TES-14; SCP-1; SCP1"
                     /coded_by="NM_003176.4:181..3111"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS879.1"
                     /db_xref="GeneID:6847"
                     /db_xref="HGNC:HGNC:11487"
                     /db_xref="MIM:602162"
ORIGIN      
        1 mekqkpfalf vpprssssqv savkpqtlgg dstffksfnk cteddfefpf aktnlsknge
       61 nidsdpalqk vnflpvleqv gnsdchyqeg lkdsdlense glsrvyskly keaekikkwk
      121 vsteaelrqk esklqenrki ieaqrkaiqe lqfgnekvsl kleegiqenk dlikennatr
      181 hlcnllketc arsaektkky eyereetrqv ymdlnnniek mitafeelrv qaensrlemh
      241 fklkedyeki qhleqeykke indkekqvsl lliqiteken kmkdltflle esrdkvnqle
      301 ektklqsenl kqsiekqhhl tkeledikvs lqrsvstqka leedlqiatk ticqlteeke
      361 tqmeesnkar aahsfvvtef ettvcsleel lrteqqrlek nedqlkiltm elqkkssele
      421 emtkltnnke veleelkkvl geketllyen kqfekiaeel kgteqeligl lqarekevhd
      481 leiqltaitt seqyyskevk dlktelenek lknteltshc nklslenkel tqetsdmtle
      541 lknqqedinn nkkqeermlk qienlqetet qlrneleyvr eelkqkrdev kckldkseen
      601 cnnlrkqven knkyieelqq enkalkkkgt aeskqlnvye ikvnklelel esakqkfgei
      661 tdtyqkeied kkiseenlle evekakviad eavklqkeid krcqhkiaem valmekhkhq
      721 ydkiieerds elglykskeq eqsslrasle ielsnlkael lsvkkqleie reekeklkre
      781 akentatlke kkdkktqtfl letpeiywkl dskavpsqtv srnftsvdhg iskdkrdylw
      841 tsakntlstp lpkaytvktp tkpklqqren lnipieeskk krkmafefdi nsdssettdl
      901 lsmvseeetl ktlyrnnnpp ashlcvktpk kapsslttpg stlkfgairk mredrwavia
      961 kmdrkkklke aeklfv
//
LOCUS       NP_001273270             421 aa            linear   PRI 20-NOV-2025
DEFINITION  protein chibby homolog 2 isoform 2 [Homo sapiens].
ACCESSION   NP_001273270 XP_005266341
VERSION     NP_001273270.1
DBSOURCE    REFSEQ: accession NM_001286341.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 421)
  AUTHORS   Gogl,G., Zambo,B., Kostmann,C., Cousido-Siah,A., Morlet,B.,
            Durbesson,F., Negroni,L., Eberling,P., Jane,P., Nomine,Y., Zeke,A.,
            Ostergaard,S., Monsellier,E., Vincentelli,R. and Trave,G.
  TITLE     Quantitative fragmentomics allow affinity mapping of interactomes
  JOURNAL   Nat Commun 13 (1), 5472 (2022)
   PUBMED   36115835
  REMARK    Erratum:[Nat Commun. 2022 Dec 7;13(1):7555. doi:
            10.1038/s41467-022-35177-6. PMID: 36477203]
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 421)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   3  (residues 1 to 421)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   4  (residues 1 to 421)
  AUTHORS   Fragoza,R., Das,J., Wierbowski,S.D., Liang,J., Tran,T.N., Liang,S.,
            Beltran,J.F., Rivera-Erick,C.A., Ye,K., Wang,T.Y., Yao,L., Mort,M.,
            Stenson,P.D., Cooper,D.N., Wei,X., Keinan,A., Schimenti,J.C.,
            Clark,A.G. and Yu,H.
  TITLE     Extensive disruption of protein interactions by genetic variants
            across the allele frequency spectrum in human populations
  JOURNAL   Nat Commun 10 (1), 4141 (2019)
   PUBMED   31515488
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 421)
  AUTHORS   Chen,S., Fragoza,R., Klei,L., Liu,Y., Wang,J., Roeder,K., Devlin,B.
            and Yu,H.
  TITLE     An interactome perturbation framework prioritizes damaging missense
            mutations for developmental disorders
  JOURNAL   Nat Genet 50 (7), 1032-1040 (2018)
   PUBMED   29892012
REFERENCE   6  (residues 1 to 421)
  AUTHORS   Yachie,N., Petsalaki,E., Mellor,J.C., Weile,J., Jacob,Y., Verby,M.,
            Ozturk,S.B., Li,S., Cote,A.G., Mosca,R., Knapp,J.J., Ko,M., Yu,A.,
            Gebbia,M., Sahni,N., Yi,S., Tyagi,T., Sheykhkarimli,D., Roth,J.F.,
            Wong,C., Musa,L., Snider,J., Liu,Y.C., Yu,H., Braun,P.,
            Stagljar,I., Hao,T., Calderwood,M.A., Pelletier,L., Aloy,P.,
            Hill,D.E., Vidal,M. and Roth,F.P.
  TITLE     Pooled-matrix protein interaction screens using Barcode Fusion
            Genetics
  JOURNAL   Mol Syst Biol 12 (4), 863 (2016)
   PUBMED   27107012
  REMARK    Publication Status: Online-Only
REFERENCE   7  (residues 1 to 421)
  AUTHORS   Yang,X., Coulombe-Huntington,J., Kang,S., Sheynkman,G.M., Hao,T.,
            Richardson,A., Sun,S., Yang,F., Shen,Y.A., Murray,R.R., Spirohn,K.,
            Begg,B.E., Duran-Frigola,M., MacWilliams,A., Pevzner,S.J.,
            Zhong,Q., Wanamaker,S.A., Tam,S., Ghamsari,L., Sahni,N., Yi,S.,
            Rodriguez,M.D., Balcha,D., Tan,G., Costanzo,M., Andrews,B.,
            Boone,C., Zhou,X.J., Salehi-Ashtiani,K., Charloteaux,B., Chen,A.A.,
            Calderwood,M.A., Aloy,P., Roth,F.P., Hill,D.E., Iakoucheva,L.M.,
            Xia,Y. and Vidal,M.
  TITLE     Widespread Expansion of Protein Interaction Capabilities by
            Alternative Splicing
  JOURNAL   Cell 164 (4), 805-817 (2016)
   PUBMED   26871637
REFERENCE   8  (residues 1 to 421)
  AUTHORS   Sahni,N., Yi,S., Taipale,M., Fuxman Bass,J.I.,
            Coulombe-Huntington,J., Yang,F., Peng,J., Weile,J., Karras,G.I.,
            Wang,Y., Kovacs,I.A., Kamburov,A., Krykbaeva,I., Lam,M.H.,
            Tucker,G., Khurana,V., Sharma,A., Liu,Y.Y., Yachie,N., Zhong,Q.,
            Shen,Y., Palagi,A., San-Miguel,A., Fan,C., Balcha,D., Dricot,A.,
            Jordan,D.M., Walsh,J.M., Shah,A.A., Yang,X., Stoyanova,A.K.,
            Leighton,A., Calderwood,M.A., Jacob,Y., Cusick,M.E.,
            Salehi-Ashtiani,K., Whitesell,L.J., Sunyaev,S., Berger,B.,
            Barabasi,A.L., Charloteaux,B., Hill,D.E., Hao,T., Roth,F.P.,
            Xia,Y., Walhout,A.J.M., Lindquist,S. and Vidal,M.
  TITLE     Widespread macromolecular interaction perturbations in human
            genetic disorders
  JOURNAL   Cell 161 (3), 647-660 (2015)
   PUBMED   25910212
REFERENCE   9  (residues 1 to 421)
  AUTHORS   Yu,H., Tardivo,L., Tam,S., Weiner,E., Gebreab,F., Fan,C.,
            Svrzikapa,N., Hirozane-Kishikawa,T., Rietman,E., Yang,X.,
            Sahalie,J., Salehi-Ashtiani,K., Hao,T., Cusick,M.E., Hill,D.E.,
            Roth,F.P., Braun,P. and Vidal,M.
  TITLE     Next-generation sequencing to generate interactome datasets
  JOURNAL   Nat Methods 8 (6), 478-480 (2011)
   PUBMED   21516116
REFERENCE   10 (residues 1 to 421)
  AUTHORS   Feige,E., Chen,A. and Motro,B.
  TITLE     Nurit, a novel leucine-zipper protein, expressed uniquely in the
            spermatid flower-like structure
  JOURNAL   Mech Dev 117 (1-2), 369-377 (2002)
   PUBMED   12204287
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            HY007057.1, HY026582.1 and BC027609.2.
            
            On Nov 2, 2013 this sequence version replaced XP_005266341.1.
            
            Transcript Variant: This variant (2) lacks an alternate in-frame
            exon, compared to variant 1. The encoded isoform (2) is shorter
            than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: DB028454.1, HY023187.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148093
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..421
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q14.13"
     Protein         1..421
                     /product="protein chibby homolog 2 isoform 2"
                     /note="novel leucine zipper testicular protein; spermatid
                     flower-like structure protein; testis-specific leucine
                     zipper protein nurit; spermatid-associated protein;
                     spermatid associated; protein chibby homolog 2; testicular
                     tissue protein Li 182"
                     /calculated_mol_wt=48278
     Region          50..165
                     /region_name="Cby_like"
                     /note="Chibby, a nuclear inhibitor of Wnt/beta-catenin
                     mediated transcription, and similar proteins; cd07429"
                     /db_xref="CDD:143631"
     Region          <141..>378
                     /region_name="SMC_prok_B"
                     /note="chromosome segregation protein SMC, common
                     bacterial type; TIGR02168"
                     /db_xref="CDD:274008"
     CDS             1..421
                     /gene="CBY2"
                     /gene_synonym="NURIT; SPERT"
                     /coded_by="NM_001286341.2:72..1337"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="GeneID:220082"
                     /db_xref="HGNC:HGNC:30720"
                     /db_xref="MIM:618614"
ORIGIN      
        1 msplecsecf gdqllhrtyt wqltlrgtae pfprlhnlys tprcaqqaal prlsrrmasq
       61 hsyplnrfss vpldpmerpm sqadleldyn pprvqlsdem fvfqdgrwvn encrlqspyf
      121 spsasfhhkl hhkrlakecm lqeenkslre enkalreenr mlskenkilq vfweehkasl
      181 greesrapsp llhkdsasle vvkkdhvalq vprgkedstl qllreenral qqlleqkqay
      241 waqaedtaap aeeskpapsp heepcspgll qdqgsglssr feepkgppar qedskelral
      301 rkmvsnmsgp sgeeeakvgp glpdgcqplq llremrqalq allkenrllq eenrtlqvlr
      361 aehrgfqeen kalwennklk lqqklvidtv tevtarmeml ieelyafmpa rsqdpkkpsr
      421 v
//
LOCUS       NP_006603               1103 aa            linear   PRI 20-NOV-2025
DEFINITION  kinesin-like protein KIF1C [Homo sapiens].
ACCESSION   NP_006603 XP_375394
VERSION     NP_006603.2
DBSOURCE    REFSEQ: accession NM_006612.6
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1103)
  AUTHORS   Schaffer,L.V., Hu,M., Qian,G., Moon,K.M., Pal,A., Soni,N.,
            Latham,A.P., Pontano Vaites,L., Tsai,D., Mattson,N.M., Licon,K.,
            Bachelder,R., Cesnik,A., Gaur,I., Le,T., Leineweber,W., Palar,A.,
            Pulido,E., Qin,Y., Zhao,X., Churas,C., Lenkiewicz,J., Chen,J.,
            Ono,K., Pratt,D., Zage,P., Echeverria,I., Sali,A., Harper,J.W.,
            Gygi,S.P., Foster,L.J., Huttlin,E.L., Lundberg,E. and Ideker,T.
  TITLE     Multimodal cell maps as a foundation for structural and functional
            genomics
  JOURNAL   Nature 642 (8066), 222-231 (2025)
   PUBMED   40205054
  REMARK    Erratum:[Nature. 2025 Oct;646(8086):E16. doi:
            10.1038/s41586-025-09648-x. PMID: 41039152]
REFERENCE   2  (residues 1 to 1103)
  AUTHORS   Laragione,T., Harris,C. and Gulko,P.S.
  TITLE     KIF1C and new Huntingtin-interacting protein 1 binding proteins
            regulate rheumatoid arthritis fibroblast-like synoviocytes'
            phenotypes
  JOURNAL   Front Immunol 15, 1323410 (2024)
   PUBMED   38726004
  REMARK    GeneRIF: KIF1C and new Huntingtin-interacting protein 1 binding
            proteins regulate rheumatoid arthritis fibroblast-like
            synoviocytes' phenotypes.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1103)
  AUTHORS   Segal,D., Maier,S., Mastromarco,G.J., Qian,W.W., Nabeel-Shah,S.,
            Lee,H., Moore,G., Lacoste,J., Larsen,B., Lin,Z.Y.,
            Selvabaskaran,A., Liu,K., Smibert,C., Zhang,Z., Greenblatt,J.,
            Peng,J., Lee,H.O., Gingras,A.C. and Taipale,M.
  TITLE     A central chaperone-like role for 14-3-3 proteins in human cells
  JOURNAL   Mol Cell 83 (6), 974-993 (2023)
   PUBMED   36931259
REFERENCE   4  (residues 1 to 1103)
  AUTHORS   Hancock,W.O.
  TITLE     Intracellular transport: KIF1C produces force along with a few
            slips
  JOURNAL   Curr Biol 32 (17), R914-R916 (2022)
   PUBMED   36099894
  REMARK    GeneRIF: Intracellular transport: KIF1C produces force along with a
            few slips.
REFERENCE   5  (residues 1 to 1103)
  AUTHORS   Siddiqui,N., Roth,D., Toleikis,A., Zwetsloot,A.J., Cross,R.A. and
            Straube,A.
  TITLE     Force generation of KIF1C is impaired by pathogenic mutations
  JOURNAL   Curr Biol 32 (17), 3862-3870 (2022)
   PUBMED   35961316
  REMARK    GeneRIF: Force generation of KIF1C is impaired by pathogenic
            mutations.
REFERENCE   6  (residues 1 to 1103)
  AUTHORS   Beausoleil,S.A., Villen,J., Gerber,S.A., Rush,J. and Gygi,S.P.
  TITLE     A probability-based approach for high-throughput protein
            phosphorylation analysis and site localization
  JOURNAL   Nat Biotechnol 24 (10), 1285-1292 (2006)
   PUBMED   16964243
REFERENCE   7  (residues 1 to 1103)
  AUTHORS   Kopp,P., Lammers,R., Aepfelbacher,M., Woehlke,G., Rudel,T.,
            Machuy,N., Steffen,W. and Linder,S.
  TITLE     The kinesin KIF1C and microtubule plus ends regulate podosome
            dynamics in macrophages
  JOURNAL   Mol Biol Cell 17 (6), 2811-2823 (2006)
   PUBMED   16554367
  REMARK    GeneRIF: Hairpin RNA-based depletion of KIF1C resulted in decreased
            podosome dynamics and ultimately in podosome deficiency.
REFERENCE   8  (residues 1 to 1103)
  AUTHORS   Dorner,C., Ullrich,A., Haring,H.U. and Lammers,R.
  TITLE     The kinesin-like motor protein KIF1C occurs in intact cells as a
            dimer and associates with proteins of the 14-3-3 family
  JOURNAL   J Biol Chem 274 (47), 33654-33660 (1999)
   PUBMED   10559254
REFERENCE   9  (residues 1 to 1103)
  AUTHORS   Dorner,C., Ciossek,T., Muller,S., Moller,P.H., Ullrich,A. and
            Lammers,R.
  TITLE     Characterization of KIF1C, a new kinesin-like protein involved in
            vesicle transport from the Golgi apparatus to the endoplasmic
            reticulum
  JOURNAL   J Biol Chem 273 (32), 20267-20275 (1998)
   PUBMED   9685376
REFERENCE   10 (residues 1 to 1103)
  AUTHORS   Hedera,P.
  TITLE     Uncomplicated (Pure) Hereditary Spastic Paraplegia Overview
  JOURNAL